ENTRY CCHU #type complete TITLE cytochrome c [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 24-Apr-1984 #sequence_revision 30-Sep-1991 #text_change 28-Jul-2000 ACCESSIONS A31764; A05676; I55192; A00001 REFERENCE A31764 !$#authors Evans, M.J.; Scarpulla, R.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:9625-9629 !$#title The human somatic cytochrome c gene: two classes of !1processed pseudogenes demarcate a period of rapid molecular !1evolution. !$#cross-references MUID:89071748; PMID:2849112 !$#accession A31764 !'##molecule_type DNA !'##residues 1-105 ##label EVA !'##cross-references GB:M22877; NID:g181241; PIDN:AAA35732.1; !1PID:g181242 REFERENCE A05676 !$#authors Matsubara, H.; Smith, E.L. !$#journal J. Biol. Chem. (1963) 238:2732-2753 !$#title Human heart cytochrome c. Chymotryptic peptides, tryptic !1peptides, and the complete amino acid sequence. !$#accession A05676 !'##molecule_type protein !'##residues 2-28;29-46;47-100;101-105 ##label MATS REFERENCE A00001 !$#authors Matsubara, H.; Smith, E.L. !$#journal J. Biol. Chem. (1962) 237:3575-3576 !$#title The amino acid sequence of human heart cytochrome c. !$#contents annotation !$#note 66-Leu is found in 10% of the molecules in pooled protein REFERENCE I55192 !$#authors Tanaka, Y.; Ashikari, T.; Shibano, Y.; Amachi, T.; !1Yoshizumi, H.; Matsubara, H. !$#journal J. Biochem. (1988) 103:954-961 !$#title Construction of a human cytochrome c gene and its functional !1expression in Saccharomyces cerevisiae. !$#cross-references MUID:89008207; PMID:2844747 !$#accession I55192 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 78-105 ##label RES !'##cross-references GB:D00265; NID:g2897691; PIDN:BAA00187.1; !1PID:g219557 GENETICS !$#introns 57/1 CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; metalloprotein; mitochondrion; oxidative !1phosphorylation; polymorphism; respiratory chain FEATURE !$2-105 #product cytochrome c #status experimental #label !8MAT\ !$5-99 #domain cytochrome c homology #label CYC\ !$2 #modified_site acetylated amino end (Gly) (in mature !8form) #status experimental\ !$15,18 #binding_site heme (Cys) (covalent) #status !8experimental\ !$19,81 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 105 #molecular-weight 11749 #checksum 3247 SEQUENCE /// ENTRY CCCZ #type complete TITLE cytochrome c - chimpanzee (tentative sequence) ORGANISM #formal_name Pan troglodytes #common_name chimpanzee DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 03-Mar-2000 ACCESSIONS A00002 REFERENCE A94601 !$#authors Needleman, S.B. !$#submission submitted to the Atlas, October 1968 !$#accession A00002 !'##molecule_type protein !'##residues 1-104 ##label NEE REFERENCE A94455 !$#authors Needleman, S.B.; Margoliash, E. !$#citation unpublished results, 1966, cited by Margoliash, E., and !1Fitch, W.M., Ann. N.Y. Acad. Sci. 151, 359-381, 1968 !$#contents annotation; compositions of chymotryptic peptides CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; metalloprotein; mitochondrion; oxidative !1phosphorylation; respiratory chain FEATURE !$4-98 #domain cytochrome c homology #label CYC\ !$1 #modified_site acetylated amino end (Gly) #status !8predicted\ !$14,17 #binding_site heme (Cys) (covalent) #status !8predicted\ !$18,80 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 104 #molecular-weight 11617 #checksum 9501 SEQUENCE /// ENTRY CCMQR #type complete TITLE cytochrome c - rhesus macaque (tentative sequence) ORGANISM #formal_name Macaca mulatta #common_name rhesus macaque DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 03-Mar-2000 ACCESSIONS A00003 REFERENCE A00003 !$#authors Rothfus, J.A.; Smith, E.L. !$#journal J. Biol. Chem. (1965) 240:4277-4283 !$#title Amino acid sequence of rhesus monkey heart cytochrome c. !$#cross-references MUID:66045191; PMID:4954366 !$#contents compositions of chymotryptic peptides; sequences of residues !155-61 and 68-70 !$#accession A00003 !'##molecule_type protein !'##residues 1-104 ##label ROT CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; metalloprotein; mitochondrion; oxidative !1phosphorylation; respiratory chain FEATURE !$4-98 #domain cytochrome c homology #label CYC\ !$1 #modified_site acetylated amino end (Gly) #status !8experimental\ !$14,17 #binding_site heme (Cys) (covalent) #status !8predicted\ !$18,80 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 104 #molecular-weight 11605 #checksum 9512 SEQUENCE /// ENTRY CCMKP #type complete TITLE cytochrome c - spider monkey ORGANISM #formal_name Ateles sp. #common_name spider monkey DATE 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 03-Mar-2000 ACCESSIONS A00004 REFERENCE A00004 !$#authors Margoliash, E. !$#citation unpublished results, cited by Shelnutt, J.A., Rousseau, !1D.L., Dethmers, J.K., and Margoliash, E., Biochemistry 20, !16485-6497, 1981 !$#accession A00004 !'##molecule_type protein !'##residues 1-104 ##label MAR CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; metalloprotein; mitochondrion; oxidative !1phosphorylation; respiratory chain FEATURE !$4-98 #domain cytochrome c homology #label CYC\ !$1 #modified_site acetylated amino end (Gly) #status !8predicted\ !$14,17 #binding_site heme (Cys) (covalent) #status !8predicted\ !$18,80 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 104 #molecular-weight 11710 #checksum 9066 SEQUENCE /// ENTRY CCMS #type complete TITLE cytochrome c [validated] - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1990 #sequence_revision 30-Sep-1991 #text_change 28-Jul-2000 ACCESSIONS A23057; A04604; A00009 REFERENCE A23057 !$#authors Limbach, K.J.; Wu, R. !$#journal Nucleic Acids Res. (1985) 13:617-630 !$#title Characterization of a mouse somatic cytochrome c gene and !1three cytochrome c pseudogenes. !$#cross-references MUID:85215501; PMID:2987801 !$#accession A23057 !'##molecule_type DNA !'##residues 1-105 ##label LIM !'##cross-references EMBL:X01756; NID:g50618; PIDN:CAA25899.1; !1PID:g50619 !'##experimental_source strain BALB/c REFERENCE A04604 !$#authors Carlson, S.S.; Mross, G.A.; Wilson, A.C.; Mead, R.T.; Wolin, !1L.D.; Bowers, S.F.; Foley, N.T.; Muijsers, A.O.; Margoliash, !1E. !$#journal Biochemistry (1977) 16:1437-1442 !$#title Primary structure of mouse, rat, and guinea pig cytochrome !1c. !$#cross-references MUID:77134768; PMID:191069 !$#accession A04604 !'##molecule_type protein !'##residues 2-105 ##label CAR !'##experimental_source strain BALB/c GENETICS !$#introns 57/1 CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; metalloprotein; mitochondrion; oxidative !1phosphorylation; respiratory chain FEATURE !$2-105 #product cytochrome c #status experimental #label !8MAT\ !$5-99 #domain cytochrome c homology #label CYC\ !$2 #modified_site acetylated amino end (Gly) (in mature !8form) #status experimental\ !$15,18 #binding_site heme (Cys) (covalent) #status !8experimental\ !$19,81 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 105 #molecular-weight 11605 #checksum 1273 SEQUENCE /// ENTRY CCRT #type complete TITLE cytochrome c [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1990 #sequence_revision 30-Sep-1991 #text_change 28-Jul-2000 ACCESSIONS A04605; C28160; A00009 REFERENCE A04605 !$#authors Scarpulla, R.C.; Agne, K.M.; Wu, R. !$#journal J. Biol. Chem. (1981) 256:6480-6486 !$#title Isolation and structure of a rat cytochrome c gene. !$#cross-references MUID:81215609; PMID:6263917 !$#accession A04605 !'##molecule_type DNA !'##residues 1-105 ##label SCA !'##cross-references GB:K00750; GB:M28216; NID:g550511; PIDN:AAA21711.1; !1PID:g203699 REFERENCE A28160 !$#authors Virbasius, J.V.; Scarpulla, R.C. !$#journal J. Biol. Chem. (1988) 263:6791-6796 !$#title Structure and expression of rodent genes encoding the !1testis-specific cytochrome c. Differences in gene structure !1and evolution between somatic and testicular variants. !$#cross-references MUID:88198250; PMID:2834389 !$#accession C28160 !'##molecule_type mRNA !'##residues 1-105 ##label VIR !'##cross-references GB:M20622; NID:g203722; PIDN:AAA41014.1; !1PID:g203723 REFERENCE A04604 !$#authors Carlson, S.S.; Mross, G.A.; Wilson, A.C.; Mead, R.T.; Wolin, !1L.D.; Bowers, S.F.; Foley, N.T.; Muijsers, A.O.; Margoliash, !1E. !$#journal Biochemistry (1977) 16:1437-1442 !$#title Primary structure of mouse, rat, and guinea pig cytochrome !1c. !$#cross-references MUID:77134768; PMID:191069 !$#contents annotation !$#note peptide mapping, compositional analysis, and partial !1sequencing indicate that rat cytochrome c is identical with !1that of mouse GENETICS !$#introns 57/1 CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS blocked amino end; chromoprotein; electron transfer; heme; !1iron; metalloprotein; mitochondrion; oxidative !1phosphorylation; respiratory chain FEATURE !$2-105 #product cytochrome c #status experimental #label !8MAT\ !$5-99 #domain cytochrome c homology #label CYC\ !$2 #modified_site blocked amino end (Gly) (in mature !8form) (probably acetylated) #status experimental\ !$15,18 #binding_site heme (Cys) (covalent) #status !8experimental\ !$19,81 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 105 #molecular-weight 11605 #checksum 1273 SEQUENCE /// ENTRY CCRB #type complete TITLE cytochrome c [validated] - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 13-Jul-1981 #sequence_revision 13-Jul-1981 #text_change 28-Jul-2000 ACCESSIONS A00009 REFERENCE A00009 !$#authors Needleman, S.B.; Margoliash, E. !$#journal J. Biol. Chem. (1966) 241:853-863 !$#title Rabbit heart cytochrome c. !$#cross-references MUID:66093127; PMID:5905125 !$#accession A00009 !'##molecule_type protein !'##residues 1-104 ##label NEE CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; metalloprotein; mitochondrion; oxidative !1phosphorylation; respiratory chain FEATURE !$4-98 #domain cytochrome c homology #label CYC\ !$1 #modified_site acetylated amino end (Gly) #status !8experimental\ !$14,17 #binding_site heme (Cys) (covalent) #status !8experimental\ !$18,80 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 104 #molecular-weight 11560 #checksum 8395 SEQUENCE /// ENTRY CCGW #type complete TITLE cytochrome c [validated] - guanaco ORGANISM #formal_name Lama guanicoe #common_name guanaco DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 28-Jul-2000 ACCESSIONS A04608; A00009 REFERENCE A04608 !$#authors Niece, R.L.; Margoliash, E.; Fitch, W.M. !$#journal Biochemistry (1977) 16:68-72 !$#title Complete amino acid sequence of guanaco (Lama guanicoe) !1cytochrome c. !$#cross-references MUID:77087753; PMID:188448 !$#accession A04608 !'##molecule_type protein !'##residues 1-104 ##label NIE CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; metalloprotein; mitochondrion; oxidative !1phosphorylation; respiratory chain FEATURE !$4-98 #domain cytochrome c homology #label CYC\ !$1 #modified_site acetylated amino end (Gly) #status !8experimental\ !$14,17 #binding_site heme (Cys) (covalent) #status !8experimental\ !$18,80 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 104 #molecular-weight 11516 #checksum 8496 SEQUENCE /// ENTRY CCCM #type complete TITLE cytochrome c - Arabian camel ORGANISM #formal_name Camelus dromedarius #common_name Arabian camel DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS A04607; A00009 REFERENCE A04607 !$#authors Sokolovsky, M.; Moldovan, M. !$#journal Biochemistry (1972) 11:145-149 !$#title Primary structure of cytochrome c from the camel, Camelus !1dromedarius. !$#cross-references MUID:72096652; PMID:5061872 !$#accession A04607 !'##molecule_type protein !'##residues 1-104 ##label SOK CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; metalloprotein; mitochondrion; oxidative !1phosphorylation; respiratory chain FEATURE !$4-98 #domain cytochrome c homology #label CYC\ !$1 #modified_site acetylated amino end (Gly) #status !8experimental\ !$14,17 #binding_site heme (Cys) (covalent) #status !8predicted\ !$18,80 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 104 #molecular-weight 11516 #checksum 8496 SEQUENCE /// ENTRY CCWHC #type complete TITLE cytochrome c - California gray whale ORGANISM #formal_name Eschrichtius robustus, Eschrichtius gibbosus #common_name California gray whale DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS A04606; A00009 REFERENCE A04606 !$#authors Goldstone, A.; Smith, E.L. !$#journal J. Biol. Chem. (1966) 241:4480-4486 !$#title Amino acid sequence of whale heart cytochrome c. !$#cross-references MUID:67041932; PMID:5922971 !$#accession A04606 !'##molecule_type protein !'##residues 1-104 ##label GOL CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS blocked amino end; chromoprotein; electron transfer; heme; !1iron; metalloprotein; mitochondrion; oxidative !1phosphorylation; respiratory chain FEATURE !$4-98 #domain cytochrome c homology #label CYC\ !$1 #modified_site blocked amino end (Gly) (probably !8acetylated) #status experimental\ !$14,17 #binding_site heme (Cys) (covalent) #status !8predicted\ !$18,80 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 104 #molecular-weight 11516 #checksum 8496 SEQUENCE /// ENTRY CCPG #type complete TITLE cytochrome c [validated] - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 28-Jul-2000 ACCESSIONS A00007 REFERENCE A90743 !$#authors Stewart, J.W.; Margoliash, E. !$#journal Can. J. Biochem. (1965) 43:1187-1206 !$#title The primary structure of the cytochrome c from various !1organs of the hog. !$#cross-references MUID:66072936; PMID:5855656 !$#accession A00007 !'##molecule_type protein !'##residues 1-104 ##label STE CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; metalloprotein; mitochondrion; oxidative !1phosphorylation; respiratory chain FEATURE !$4-98 #domain cytochrome c homology #label CYC\ !$1 #modified_site acetylated amino end (Gly) #status !8experimental\ !$14,17 #binding_site heme (Cys) (covalent) #status !8experimental\ !$18,80 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 104 #molecular-weight 11572 #checksum 8372 SEQUENCE /// ENTRY CCBO #type complete TITLE cytochrome c - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Mar-2000 ACCESSIONS A92022; A00007 REFERENCE A92022 !$#authors Nakashima, T.; Higa, H.; Matsubara, H.; Benson, A.; !1Yasunobu, K.T. !$#journal J. Biol. Chem. (1966) 241:1166-1177 !$#title The amino acid sequence of bovine heart cytochrome c. !$#cross-references MUID:66132521; PMID:5933874 !$#accession A92022 !'##molecule_type protein !'##residues 1-104 ##label NAK REFERENCE A61297 !$#authors Tsunasawa, S.; Narita, K. !$#journal J. Biochem. (1982) 92:607-613 !$#title Micro-identification of amino-terminal acetylamino acids in !1proteins. !$#cross-references MUID:83056735; PMID:6754709 !$#contents annotation; acetylation CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; metalloprotein; mitochondrion; oxidative !1phosphorylation; respiratory chain FEATURE !$4-98 #domain cytochrome c homology #label CYC\ !$1 #modified_site acetylated amino end (Gly) #status !8experimental\ !$14,17 #binding_site heme (Cys) (covalent) #status !8predicted\ !$18,80 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 104 #molecular-weight 11572 #checksum 8372 SEQUENCE /// ENTRY CCSH #type complete TITLE cytochrome c - sheep (tentative sequence) ORGANISM #formal_name Ovis orientalis aries, Ovis ammon aries #common_name domestic sheep DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Mar-2000 ACCESSIONS A91454; A00007 REFERENCE A91454 !$#authors Smith, E.L.; Margoliash, E. !$#journal Fed. Proc. (1964) 23:1243-1247 !$#title Evolution of cytochrome c. !$#accession A91454 !'##molecule_type protein !'##residues 1-104 ##label SMI !'##note amino acid compositions and mobilities of tryptic and !1chymotryptic peptides were determined CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; metalloprotein; mitochondrion; oxidative !1phosphorylation; respiratory chain FEATURE !$4-98 #domain cytochrome c homology #label CYC\ !$1 #modified_site acetylated amino end (Gly) #status !8predicted\ !$14,17 #binding_site heme (Cys) (covalent) #status !8predicted\ !$18,80 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 104 #molecular-weight 11572 #checksum 8372 SEQUENCE /// ENTRY CCHOD #type complete TITLE cytochrome c - donkey (tentative sequence) ORGANISM #formal_name Equus asinus #common_name donkey DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 03-Mar-2000 ACCESSIONS A00006 REFERENCE A92217 !$#authors Walasek, O.F.; Margoliash, E. !$#journal J. Biol. Chem. (1977) 252:830-834 !$#title Transmission of the cytochrome c structural gene in !1horse-donkey crosses. !$#cross-references MUID:77118552; PMID:190219 !$#accession A00006 !'##molecule_type protein !'##residues 1-104 ##label WAL !'##note compositions of chymotryptic peptides and the sequence of !1residues 47-48 were determined !'##note mules and hinnies are heterozygous, having equal amounts of !1horse and donkey cytochromes c CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; metalloprotein; mitochondrion; oxidative !1phosphorylation; respiratory chain FEATURE !$4-98 #domain cytochrome c homology #label CYC\ !$1 #modified_site acetylated amino end (Gly) #status !8predicted\ !$14,17 #binding_site heme (Cys) (covalent) #status !8predicted\ !$18,80 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 104 #molecular-weight 11687 #checksum 8800 SEQUENCE /// ENTRY CCHOZ #type complete TITLE cytochrome c - common zebra (tentative sequence) ORGANISM #formal_name Equus burchelli, Equus quagga #common_name common zebra, plains zebra DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Mar-2000 ACCESSIONS A91330; A00006 REFERENCE A91330 !$#authors Guertler, L.; Horstmann, H.J. !$#journal FEBS Lett. (1971) 18:106-108 !$#title Zur Primaerstruktur des Cytochromes c des Steppenzebras !1(Equus quagga boehmi). !$#accession A91330 !'##molecule_type protein !'##residues 1-104 ##label GUE !'##note the amino acid composition and the sequence of residues 40-48 !1were determined CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; metalloprotein; mitochondrion; oxidative !1phosphorylation; respiratory chain FEATURE !$4-98 #domain cytochrome c homology #label CYC\ !$1 #modified_site acetylated amino end (Gly) #status !8predicted\ !$14,17 #binding_site heme (Cys) (covalent) #status !8predicted\ !$18,80 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 104 #molecular-weight 11687 #checksum 8800 SEQUENCE /// ENTRY CCHO #type complete TITLE cytochrome c [validated] - horse ORGANISM #formal_name Equus caballus #common_name domestic horse DATE 13-Jul-1981 #sequence_revision 13-Jul-1981 #text_change 28-Jul-2000 ACCESSIONS A00005; S59487 REFERENCE A93145 !$#authors Margoliash, E.; Smith, E.L.; Kreil, G.; Tuppy, H. !$#journal Nature (1961) 192:1125-1127 !$#title The complete amino-acid sequence. !$#accession A00005 !'##molecule_type protein !'##residues 1-104 ##label MAR REFERENCE S59487 !$#authors Theodorakis, J.L.; Armes, L.G.; Margoliash, E. !$#journal Biochim. Biophys. Acta (1995) 1252:114-125 !$#title beta-Thiopropionyl cytochromes c modified at lysyl residues: !1preparation and characterization of the monosubstituted !1horse cytochromes c. !$#cross-references MUID:96001358; PMID:7548153 !$#accession S59487 !'##status preliminary !'##molecule_type protein !'##residues !11-10;11-18;19-26;27-34;38-47;50-54;55-58;60-67;68-74;75-82; !183-97;98-104 ##label THE REFERENCE A52805 !$#authors Luo, Y.; Brayer, G.D. !$#submission submitted to the Brookhaven Protein Data Bank, August 1994 !$#cross-references PDB:1HRC !$#contents annotation; X-ray crystallography, 1.9 angstroms, residues !11-104 REFERENCE A92076 !$#authors Dickerson, R.E.; Takano, T.; Eisenberg, D.; Kallai, O.B.; !1Samson, L.; Cooper, A.; Margoliash, E. !$#journal J. Biol. Chem. (1971) 246:1511-1533 !$#title Ferricytochrome c. I. General features of the horse and !1bonito proteins at 2.8 A resolution. !$#cross-references MUID:71116428; PMID:5545094 !$#contents annotation; X-ray crystallography, 2.8 angstroms CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; metalloprotein; mitochondrion; oxidative !1phosphorylation; respiratory chain FEATURE !$4-98 #domain cytochrome c homology #label CYC\ !$1 #modified_site acetylated amino end (Gly) #status !8experimental\ !$14,17 #binding_site heme (Cys) (covalent) #status !8experimental\ !$18,80 #binding_site heme iron (His, Met) (axial ligands) !8#status experimental SUMMARY #length 104 #molecular-weight 11702 #checksum 8847 SEQUENCE /// ENTRY CCHP #type complete TITLE cytochrome c - hippopotamus ORGANISM #formal_name Hippopotamus amphibius #common_name hippopotamus DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 03-Mar-2000 ACCESSIONS A00008 REFERENCE A00008 !$#authors Thompson, R.B.; Borden, D.; Tarr, G.E.; Margoliash, E. !$#journal J. Biol. Chem. (1978) 253:8957-8961 !$#title Heterogeneity of amino acid sequence in hippopotamus !1cytochrome c. !$#cross-references MUID:79067782; PMID:214435 !$#accession A00008 !'##molecule_type protein !'##residues 1-104 ##label THO !'##note 3-Ile was also found CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; metalloprotein; mitochondrion; oxidative !1phosphorylation; respiratory chain FEATURE !$4-98 #domain cytochrome c homology #label CYC\ !$1 #modified_site acetylated amino end (Gly) #status !8predicted\ !$14,17 #binding_site heme (Cys) (covalent) #status !8predicted\ !$18,80 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 104 #molecular-weight 11530 #checksum 9264 SEQUENCE /// ENTRY CCDG #type complete TITLE cytochrome c - dog (tentative sequence) ORGANISM #formal_name Canis lupus familiaris #common_name dog DATE 13-Jul-1981 #sequence_revision 13-Jul-1981 #text_change 31-Mar-2000 ACCESSIONS A00010 REFERENCE A00010 !$#authors McDowall, M.A.; Smith, E.L. !$#journal J. Biol. Chem. (1965) 240:4635-4647 !$#title Amino acid sequence of dog heart cytochrome c. !$#cross-references MUID:66047448; PMID:5846985 !$#accession A00010 !'##molecule_type protein !'##residues 1-104 ##label MCD CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS blocked amino end; chromoprotein; electron transfer; heme; !1iron; metalloprotein; mitochondrion; oxidative !1phosphorylation; respiratory chain FEATURE !$4-98 #domain cytochrome c homology #label CYC\ !$1 #modified_site blocked amino end (Gly) (probably !8acetylated) #status experimental\ !$14,17 #binding_site heme (Cys) (covalent) #status !8predicted\ !$18,80 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 104 #molecular-weight 11501 #checksum 8373 SEQUENCE /// ENTRY CCSLE #type complete TITLE cytochrome c - southern elephant seal (tentative sequence) ORGANISM #formal_name Mirounga leonina #common_name southern elephant seal DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS A04615; A00010 REFERENCE A04615 !$#authors Augusteyn, R.C.; McDowall, M.A.; Webb, E.C.; Zerner, B. !$#journal Biochim. Biophys. Acta (1972) 257:264-272 !$#title Primary structure of cytochrome c from the elephant seal, !1Mirounga leonina. !$#cross-references MUID:72170090; PMID:4553890 !$#accession A04615 !'##molecule_type protein !'##residues 1-104 ##label AUG !'##note peptides were positioned by homology CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; metalloprotein; mitochondrion; oxidative !1phosphorylation; respiratory chain FEATURE !$4-98 #domain cytochrome c homology #label CYC\ !$1 #modified_site acetylated amino end (Gly) #status !8experimental\ !$14,17 #binding_site heme (Cys) (covalent) #status !8experimental\ !$18,80 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 104 #molecular-weight 11486 #checksum 8287 SEQUENCE /// ENTRY CCBTS #type complete TITLE cytochrome c - Schreibers's long-fingered bat (tentative sequence) ORGANISM #formal_name Miniopterus schreibersi #common_name Schreibers's long-fingered bat DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 11-May-2000 ACCESSIONS A04614; A00010 REFERENCE A04614 !$#authors Strydom, D.J.; van der Walt, S.J.; Botes, D.P. !$#journal Comp. Biochem. Physiol. B (1972) 43:21-24 !$#title The amino acid sequence of bat (Miniopteris schreibersi) !1cytochrome c. !$#cross-references MUID:73123526; PMID:4347193 !$#accession A04614 !'##molecule_type protein !'##residues 1-104 ##label STR CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; metalloprotein; mitochondrion; oxidative !1phosphorylation; respiratory chain FEATURE !$4-98 #domain cytochrome c homology #label CYC\ !$1 #modified_site acetylated amino end (Gly) #status !8predicted\ !$14,17 #binding_site heme (Cys) (covalent) #status !8predicted\ !$18,80 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 104 #molecular-weight 11443 #checksum 8130 SEQUENCE /// ENTRY CCKGG #type complete TITLE cytochrome c [validated] - eastern gray kangaroo ORGANISM #formal_name Macropus giganteus #common_name eastern gray kangaroo DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 28-Jul-2000 ACCESSIONS A00011 REFERENCE A00011 !$#authors Nolan, C.; Margoliash, E. !$#journal J. Biol. Chem. (1966) 241:1049-1059 !$#title Primary structure of the cytochrome c from the great grey !1kangaroo, Macropus canguru. !$#cross-references MUID:66132505; PMID:5933863 !$#accession A00011 !'##molecule_type protein !'##residues 1-104 ##label NOL CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; metalloprotein; mitochondrion; oxidative !1phosphorylation; respiratory chain FEATURE !$4-98 #domain cytochrome c homology #label CYC\ !$1 #modified_site acetylated amino end (Gly) #status !8experimental\ !$14,17 #binding_site heme (Cys) (covalent) #status !8experimental\ !$18,80 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 104 #molecular-weight 11503 #checksum 8356 SEQUENCE /// ENTRY CCMST #type complete TITLE cytochrome c, testis-specific [validated] - mouse ALTERNATE_NAMES cytochrome c T ORGANISM #formal_name Mus musculus #common_name house mouse DATE 24-Apr-1984 #sequence_revision 30-Sep-1991 #text_change 28-Jul-2000 ACCESSIONS B28160; A00012; I48313 REFERENCE A28160 !$#authors Virbasius, J.V.; Scarpulla, R.C. !$#journal J. Biol. Chem. (1988) 263:6791-6796 !$#title Structure and expression of rodent genes encoding the !1testis-specific cytochrome c. Differences in gene structure !1and evolution between somatic and testicular variants. !$#cross-references MUID:88198250; PMID:2834389 !$#accession B28160 !'##molecule_type mRNA !'##residues 1-105 ##label VIR !'##cross-references GB:M20625; NID:g192875; PIDN:AAA37501.1; !1PID:g309203 REFERENCE A00012 !$#authors Hennig, B. !$#journal Eur. J. Biochem. (1975) 55:167-183 !$#title Change of cytochrome c structure during development of the !1mouse. !$#cross-references MUID:76022386; PMID:240690 !$#accession A00012 !'##molecule_type protein !'##residues 2-57,'IV',60-61,'ZZ',64-66,'Z',68-69,'ZB',72-105 ##label !1HEN !'##experimental_source strain BALB/c REFERENCE I48313 !$#authors Hake, L.E.; Alcivar, A.A.; Hecht, N.B. !$#journal Development (1990) 110:249-257 !$#title Changes in mRNA length accompany translational regulation of !1the somatic and testis-specific cytochrome c genes during !1spermatogenesis in the mouse. !$#cross-references MUID:91184013; PMID:1964409 !$#accession I48313 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-105 ##label RES !'##cross-references EMBL:X55771; NID:g288155; PIDN:CAA39293.1; !1PID:g288156 COMMENT Mammalian testis contains two forms of cytochrome c, one !1identical with the form found in somatic tissues and another !1that is expressed in a stage-specific manner during !1spermatogenic differentiation. CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS blocked amino end; chromoprotein; electron transfer; heme; !1iron; metalloprotein; mitochondrion; oxidative !1phosphorylation; respiratory chain; sperm; testis FEATURE !$2-105 #product cytochrome c, testis-specific #status !8experimental #label MAT\ !$5-99 #domain cytochrome c homology #label CYC\ !$2 #modified_site blocked amino end (Gly) (in mature !8form) (probably acetylated) #status experimental\ !$15,18 #binding_site heme (Cys) (covalent) #status !8experimental\ !$19,81 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 105 #molecular-weight 11713 #checksum 4470 SEQUENCE /// ENTRY CCRTT #type complete TITLE cytochrome c, testis-specific - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Mar-2000 ACCESSIONS A28160 REFERENCE A28160 !$#authors Virbasius, J.V.; Scarpulla, R.C. !$#journal J. Biol. Chem. (1988) 263:6791-6796 !$#title Structure and expression of rodent genes encoding the !1testis-specific cytochrome c. Differences in gene structure !1and evolution between somatic and testicular variants. !$#cross-references MUID:88198250; PMID:2834389 !$#accession A28160 !'##molecule_type DNA; mRNA !'##residues 1-105 ##label VIR !'##cross-references GB:M20627; GB:M20628; NID:g203727; PIDN:AAA41015.1; !1PID:g203729; GB:M20623; NID:g203730; PID:g203731 COMMENT Mammalian testis contains two forms of cytochrome c, one !1identical to the form found in somatic tissues and another !1that is expressed in a stage-specific manner during !1spermatogenic differentiation. GENETICS !$#introns 57/1 CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; metalloprotein; mitochondrion; oxidative !1phosphorylation; respiratory chain; sperm; testis FEATURE !$2-105 #product cytochrome c, testis-specific #status !8predicted #label MAT\ !$5-99 #domain cytochrome c homology #label CYC\ !$2 #modified_site acetylated amino end (Gly) (in mature !8form) #status predicted\ !$15,18 #binding_site heme (Cys) (covalent) #status !8predicted\ !$19,81 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 105 #molecular-weight 11742 #checksum 4030 SEQUENCE /// ENTRY CCPY #type complete TITLE cytochrome c - pigeon (tentative sequence) ORGANISM #formal_name Columba livia #common_name domestic pigeon DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 03-Mar-2000 ACCESSIONS A00013 REFERENCE A94490 !$#authors Chan, S.K.; Tulloss, I.; Margoliash, E. !$#citation unpublished results, cited by Wojciech, R., and Margoliash, !1E., in Handbook of Biochemistry, Sober, H.A., ed., !1pp.C158-C161, Chemical Rubber Co., Cleveland, 1968 !$#accession A00013 !'##molecule_type protein !'##residues 1-104 ##label CHA !'##note compositions of tryptic peptides and sequences of residues !189-91, 92-99, and 100-104 were determined CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; metalloprotein; mitochondrion; oxidative !1phosphorylation; respiratory chain FEATURE !$4-98 #domain cytochrome c homology #label CYC\ !$1 #modified_site acetylated amino end (Gly) #status !8predicted\ !$14,17 #binding_site heme (Cys) (covalent) #status !8predicted\ !$18,80 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 104 #molecular-weight 11532 #checksum 7724 SEQUENCE /// ENTRY CCCH #type complete TITLE cytochrome c [validated] - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 24-Apr-1984 #sequence_revision 20-Aug-1994 #text_change 28-Jul-2000 ACCESSIONS A00014; A04611 REFERENCE A00014 !$#authors Limbach, K.J.; Wu, R. !$#journal Nucleic Acids Res. (1983) 11:8931-8950 !$#title Isolation and characterization of two alleles of the chicken !1cytochrome c gene. !$#cross-references MUID:84169527; PMID:6324108 !$#accession A00014 !'##molecule_type DNA !'##residues 1-105 ##label LIM !'##cross-references GB:K02303; NID:g211708; PIDN:AAA48741.1; !1PID:g211709 REFERENCE A04611 !$#authors Chan, S.K.; Margoliash, E. !$#journal J. Biol. Chem. (1966) 241:507-515 !$#title Amino acid sequence of chicken heart cytochrome. !$#cross-references MUID:66080352; PMID:5903744 !$#accession A04611 !'##molecule_type protein !'##residues 2-105 ##label CHA GENETICS !$#introns 57/1 CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; metalloprotein; mitochondrion; oxidative !1phosphorylation; respiratory chain FEATURE !$2-105 #product cytochrome c #status experimental #label !8MAT\ !$5-99 #domain cytochrome c homology #label CYC\ !$2 #modified_site acetylated amino end (Gly) (in mature !8form) #status experimental\ !$15,18 #binding_site heme (Cys) (covalent) #status !8experimental\ !$19,81 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 105 #molecular-weight 11710 #checksum 3056 SEQUENCE /// ENTRY CCTK #type complete TITLE cytochrome c - turkey (tentative sequence) ORGANISM #formal_name Meleagris gallopavo #common_name common turkey DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS A04612; A00014 REFERENCE A04612 !$#authors Chan, S.K.; Tulloss, I.; Margoliash, E. !$#submission submitted to the Atlas, June 1966 !$#accession A04612 !'##molecule_type protein !'##residues 1-104 ##label CHA CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; metalloprotein; mitochondrion; oxidative !1phosphorylation; respiratory chain FEATURE !$4-98 #domain cytochrome c homology #label CYC\ !$1 #modified_site acetylated amino end (Gly) #status !8predicted\ !$14,17 #binding_site heme (Cys) (covalent) #status !8predicted\ !$18,80 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 104 #molecular-weight 11579 #checksum 9304 SEQUENCE /// ENTRY CCDK #type complete TITLE cytochrome c - duck (tentative sequence) ORGANISM #formal_name Anas platyrhynchos #common_name domestic duck DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 03-Mar-2000 ACCESSIONS A00015 REFERENCE A04612 !$#authors Chan, S.K.; Tulloss, I.; Margoliash, E. !$#submission submitted to the Atlas, June 1966 !$#contents compositions of tryptic peptides; sequences of residues 1-5, !192-99, and 100-104 !$#accession A00015 !'##molecule_type protein !'##residues 1-104 ##label CHA !'##experimental_source Pekin breed CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; metalloprotein; mitochondrion; oxidative !1phosphorylation; respiratory chain FEATURE !$4-98 #domain cytochrome c homology #label CYC\ !$1 #modified_site acetylated amino end (Gly) #status !8predicted\ !$14,17 #binding_site heme (Cys) (covalent) #status !8predicted\ !$18,80 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 104 #molecular-weight 11521 #checksum 7780 SEQUENCE /// ENTRY CCOS #type complete TITLE cytochrome c [validated] - ostrich ORGANISM #formal_name Struthio camelus #common_name ostrich DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 28-Jul-2000 ACCESSIONS A00016 REFERENCE A00016 !$#authors Howard, N.L.; Joubert, F.J.; Strydom, D.J. !$#journal Comp. Biochem. Physiol. B (1974) 48:75-85 !$#title The amino acid sequence of ostrich (Struthio camelus) !1cytochrome C. !$#cross-references MUID:74175476; PMID:4364857 !$#accession A00016 !'##molecule_type protein !'##residues 1-104 ##label HOW CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; metalloprotein; mitochondrion; oxidative !1phosphorylation; respiratory chain FEATURE !$4-98 #domain cytochrome c homology #label CYC\ !$1 #modified_site acetylated amino end (Gly) #status !8experimental\ !$14,17 #binding_site heme (Cys) (covalent) #status !8experimental\ !$18,80 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 104 #molecular-weight 11529 #checksum 8437 SEQUENCE /// ENTRY CCEU #type complete TITLE cytochrome c [validated] - emu ORGANISM #formal_name Dromaius novaehollandiae #common_name emu DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 28-Jul-2000 ACCESSIONS A00017 REFERENCE A00017 !$#authors Augusteyn, R.C. !$#journal Biochim. Biophys. Acta (1973) 303:1-7 !$#title Primary structure of cytochrome c from the emu, Dromaeus !1novaehollandiae. !$#cross-references MUID:73171069; PMID:4349739 !$#accession A00017 !'##molecule_type protein !'##residues 1-104 ##label AUG CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS blocked amino end; chromoprotein; electron transfer; heme; !1iron; metalloprotein; mitochondrion; oxidative !1phosphorylation; respiratory chain FEATURE !$4-98 #domain cytochrome c homology #label CYC\ !$1 #modified_site blocked amino end (Gly) (probably !8acetylated) #status experimental\ !$14,17 #binding_site heme (Cys) (covalent) #status !8experimental\ !$18,80 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 104 #molecular-weight 11528 #checksum 8767 SEQUENCE /// ENTRY CCPN #type complete TITLE cytochrome c - king penguin ORGANISM #formal_name Aptenodytes patagonicus #common_name king penguin DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 03-Mar-2000 ACCESSIONS A00018 REFERENCE A38040 !$#authors Chan, S.K.; Tulloss, I.; Margoliash, E. !$#submission submitted to the Atlas, July 1967 !$#accession A00018 !'##molecule_type protein !'##residues 1-104 ##label CHA CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; metalloprotein; mitochondrion; oxidative !1phosphorylation; respiratory chain FEATURE !$4-98 #domain cytochrome c homology #label CYC\ !$1 #modified_site acetylated amino end (Gly) #status !8predicted\ !$14,17 #binding_site heme (Cys) (covalent) #status !8predicted\ !$18,80 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 104 #molecular-weight 11551 #checksum 8464 SEQUENCE /// ENTRY CCST #type complete TITLE cytochrome c - snapping turtle (tentative sequence) ORGANISM #formal_name Chelydra serpentina #common_name snapping turtle DATE 24-Apr-1984 #sequence_revision 30-Sep-1988 #text_change 31-Mar-2000 ACCESSIONS A00019 REFERENCE A00019 !$#authors Chan, S.K.; Tulloss, I.; Margoliash, E. !$#journal Biochemistry (1966) 5:2586-2597 !$#title Primary structure of the cytochrome c from the snapping !1turtle, Chelydra serpentina. !$#cross-references MUID:67172948; PMID:5968568 !$#accession A00019 !'##molecule_type protein !'##residues 1-104 ##label CHA CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; metalloprotein; mitochondrion; oxidative !1phosphorylation; respiratory chain FEATURE !$4-98 #domain cytochrome c homology #label CYC\ !$1 #modified_site acetylated amino end (Gly) #status !8predicted\ !$14,17 #binding_site heme (Cys) (covalent) #status !8predicted\ !$18,80 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 104 #molecular-weight 11476 #checksum 8123 SEQUENCE /// ENTRY CCFG #type complete TITLE cytochrome c - bullfrog (tentative sequence) ORGANISM #formal_name Rana catesbeiana #common_name bullfrog DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 31-Mar-2000 ACCESSIONS A00021 REFERENCE A00021 !$#authors Chan, S.K.; Walasek, O.F.; Barlow, G.H.; Margoliash, E. !$#submission submitted to the Atlas, July 1967 !$#accession A00021 !'##molecule_type protein !'##residues 1-104 ##label CHA COMMENT The presence of Lys-104 is not certain. COMMENT We have arranged the amino acids in positions 88-92 by !1homology with the other cytochrome c sequences. This !1arrangement is contrary to the authors'. CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; metalloprotein; mitochondrion; oxidative !1phosphorylation; respiratory chain FEATURE !$4-98 #domain cytochrome c homology #label CYC\ !$1 #modified_site acetylated amino end (Gly) #status !8predicted\ !$14,17 #binding_site heme (Cys) (covalent) #status !8predicted\ !$18,80 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted\ !$20-102 #disulfide_bonds #status experimental SUMMARY #length 104 #molecular-weight 11458 #checksum 8563 SEQUENCE /// ENTRY CCBN #type complete TITLE cytochrome c [validated] - skipjack tuna ORGANISM #formal_name Euthynnus pelamis, Katsuwonus pelamis #common_name skipjack tuna DATE 13-Jul-1981 #sequence_revision 10-Oct-1997 #text_change 28-Jul-2000 ACCESSIONS A00022 REFERENCE A00022 !$#authors Nakayama, T.; Titani, K.; Narita, K. !$#journal J. Biochem. (1971) 70:311-326 !$#title The amino acid sequence of cytochrome c from bonito !1(Katsuwonus pelamis, Linnaeus). !$#cross-references MUID:72003272; PMID:5106585 !$#accession A00022 !'##molecule_type protein !'##residues 1-103 ##label NAK REFERENCE A50107 !$#authors Tanaka, N.; Yamane, T.; Tsukihara, T.; Ashida, T.; Kakudo, !1M. !$#submission submitted to the Brookhaven Protein Data Bank, August 1976 !$#cross-references PDB:1CYC !$#contents annotation; X-ray crystallography, 2.3 angstroms, residues !11-103 REFERENCE A38036 !$#authors Tanaka, N.; Yamane, T.; Tsukihara, T.; Ashida, T.; Kakudo, !1M. !$#journal J. Biochem. (1975) 77:147-162 !$#title The crystal structure of bonito (katsuo) ferrocytochrome c !1at 2.3 A resolution. II. Structure and function. !$#cross-references MUID:75170243; PMID:166072 !$#contents annotation; X-ray crystallography, reduced form, 2.3 !1angstroms REFERENCE A38037 !$#authors Matsuura, Y.; Hata, Y.; Yamaguchi, T.; Tanaka, N.; Kakudo, !1M. !$#journal J. Biochem. (1979) 85:729-737 !$#title Structure of bonito heart ferricytochrome c and some remarks !1on molecular interaction in its crystalline state. !$#cross-references MUID:79150869; PMID:218921 !$#contents annotation; X-ray crystallography, oxidized form, 2.8 !1angstroms REFERENCE A38038 !$#authors Mandel, N.; Mandel, G.; Trus, B.L.; Rosenburg, J.; Carlson, !1G.; Dickerson, R.E. !$#journal J. Biol. Chem. (1977) 252:4619-4636 !$#title Tuna cytochrome c at 2.0 A resolution. III. Coordinate !1optimization and comparison of structures. !$#cross-references MUID:77207068; PMID:194885 !$#contents annotation; commercial Scombridae, X-ray crystallography, !1oxidized and reduced forms, 2.0 angstroms !$#note this is the final paper in a series CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; metalloprotein; mitochondrion; oxidative !1phosphorylation; respiratory chain FEATURE !$4-98 #domain cytochrome c homology #label CYC\ !$1 #modified_site acetylated amino end (Gly) #status !8experimental\ !$14,17 #binding_site heme (Cys) (covalent) #status !8experimental\ !$18,80 #binding_site heme iron (His, Met) (axial ligands) !8#status experimental SUMMARY #length 103 #molecular-weight 11384 #checksum 8045 SEQUENCE /// ENTRY CCCA #type complete TITLE cytochrome c - common carp (tentative sequence) ORGANISM #formal_name Cyprinus carpio #common_name common carp DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 31-Mar-2000 ACCESSIONS A00023 REFERENCE A00023 !$#authors Guertler, L.; Horstmann, H.J. !$#journal Eur. J. Biochem. (1970) 12:48-57 !$#title Die Aminosaeure-sequenz vom Cytochrom c des Karpfens, !1Cyprinus carpio. !$#cross-references MUID:70137310; PMID:5434283 !$#accession A00023 !'##molecule_type protein !'##residues 1-103 ##label GUE !'##note the sequence of iso-2-cytochrome c differs from that shown in !1having 4-Asp !'##note the protein was obtained from food carp that consisted of two !1cross-bred strains, the European carp and the Amur carp; the !1isocytochromes may be the result of strain differences COMMENT The sequence shown is iso-1-cytochrome c. CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS blocked amino end; chromoprotein; electron transfer; heme; !1iron; metalloprotein; mitochondrion; oxidative !1phosphorylation; respiratory chain FEATURE !$4-98 #domain cytochrome c homology #label CYC\ !$1 #modified_site blocked amino end (Gly) (probably !8acetylated) #status experimental\ !$14,17 #binding_site heme (Cys) (covalent) #status !8experimental\ !$18,80 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 103 #molecular-weight 11364 #checksum 6292 SEQUENCE /// ENTRY CCDF #type complete TITLE cytochrome c [validated] - Puget Sound dogfish ORGANISM #formal_name Squalus sucklii #common_name Puget Sound dogfish DATE 23-Oct-1981 #sequence_revision 23-Oct-1981 #text_change 28-Jul-2000 ACCESSIONS A00024 REFERENCE A00024 !$#authors Goldstone, A.; Smith, E.L. !$#journal J. Biol. Chem. (1967) 242:4702-4710 !$#title Amino acid sequence of the cytochrome c from the dogfish, !1Squalus sucklii. !$#cross-references MUID:68054790; PMID:6061416 !$#accession A00024 !'##molecule_type protein !'##residues 1-104 ##label GOL CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; metalloprotein; mitochondrion; oxidative !1phosphorylation; respiratory chain FEATURE !$4-98 #domain cytochrome c homology #label CYC\ !$1 #modified_site acetylated amino end (Gly) #status !8experimental\ !$14,17 #binding_site heme (Cys) (covalent) #status !8experimental\ !$18,80 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 104 #molecular-weight 11521 #checksum 315 SEQUENCE /// ENTRY CCLM #type complete TITLE cytochrome c [validated] - Pacific lamprey ORGANISM #formal_name Lampetra tridentata, Entosphenus tridentatus #common_name Pacific lamprey DATE 13-Jul-1981 #sequence_revision 13-Jul-1981 #text_change 28-Jul-2000 ACCESSIONS A00025 REFERENCE A00025 !$#authors Nolan, C.; Fitch, W.M.; Uzzell, T.; Weiss, L.J.; Margoliash, !1E. !$#journal Biochemistry (1973) 12:4052-4060 !$#title Amino acid sequence of a cytochrome c from the common !1Pacific lamprey, Entosphenus tridentatus. !$#cross-references MUID:74011773; PMID:4355549 !$#accession A00025 !'##molecule_type protein !'##residues 1-104 ##label NOL CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; metalloprotein; mitochondrion; oxidative !1phosphorylation; respiratory chain FEATURE !$4-98 #domain cytochrome c homology #label CYC\ !$1 #modified_site acetylated amino end (Gly) #status !8experimental\ !$14,17 #binding_site heme (Cys) (covalent) #status !8experimental\ !$18,80 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 104 #molecular-weight 11540 #checksum 468 SEQUENCE /// ENTRY CCRS #type complete TITLE cytochrome c - eastern diamondback rattlesnake ORGANISM #formal_name Crotalus adamanteus #common_name eastern diamondback rattlesnake DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 03-Mar-2000 ACCESSIONS A94624; A92021; A00020 REFERENCE A94624 !$#authors Ambler, R. !$#submission submitted to the Protein Sequence Database, January 1984 !$#accession A94624 !'##molecule_type protein !'##residues 1-104 ##label AMB REFERENCE A92021 !$#authors Bahl, O.P.; Smith, E.L. !$#journal J. Biol. Chem. (1965) 240:3585-3593 !$#title Amino acid sequence of rattlesnake heart cytochrome c. !$#cross-references MUID:66019642; PMID:5835940 !$#accession A92021 !'##molecule_type protein !'##residues 1-85,'SK',88-92,'N',94-100,'K',102-103,'A' ##label BAH CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS blocked amino end; chromoprotein; electron transfer; heme; !1iron; metalloprotein; mitochondrion; oxidative !1phosphorylation; respiratory chain FEATURE !$4-98 #domain cytochrome c homology #label CYC\ !$1 #modified_site blocked amino end (Gly) (probably !8acetylated) #status experimental\ !$14,17 #binding_site heme (Cys) (covalent) #status !8predicted\ !$18,80 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 104 #molecular-weight 11456 #checksum 474 SEQUENCE /// ENTRY CCRSW #type complete TITLE cytochrome c - western rattlesnake ORGANISM #formal_name Crotalus viridis #common_name western rattlesnake DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Mar-2000 ACCESSIONS S14358 REFERENCE S14358 !$#authors Ambler, R.P.; Daniel, M. !$#journal Biochem. J. (1991) 274:825-831 !$#title Rattlesnake cytochrome c. A re-appraisal of the reported !1amino acid sequence. !$#cross-references MUID:91190099; PMID:1849408 !$#accession S14358 !'##molecule_type protein !'##residues 1-104 ##label AMB CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; metalloprotein; mitochondrion; oxidative !1phosphorylation; respiratory chain FEATURE !$4-98 #domain cytochrome c homology #label CYC\ !$1 #modified_site acetylated amino end (Gly) #status !8predicted\ !$14,17 #binding_site heme (Cys) (covalent) #status !8predicted\ !$18,80 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 104 #molecular-weight 11456 #checksum 474 SEQUENCE /// ENTRY CCSF #type complete TITLE cytochrome c - starfish (Asterias rubens) (tentative sequence) ORGANISM #formal_name Asterias rubens #common_name common European starfish DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 31-Mar-2000 ACCESSIONS A00026 REFERENCE A00026 !$#authors Lyddiatt, A.; Boulter, D. !$#journal FEBS Lett. (1976) 67:331-334 !$#title The amino acid sequence of cytochrome c from Asterias rubens !1L. (common starfish). !$#cross-references MUID:77003681; PMID:183984 !$#accession A00026 !'##molecule_type protein !'##residues 1-103 ##label LYD CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1respiratory chain FEATURE !$4-98 #domain cytochrome c homology #label CYC\ !$14,17 #binding_site heme (Cys) (covalent) #status !8predicted\ !$18,80 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 103 #molecular-weight 11529 #checksum 5430 SEQUENCE /// ENTRY T32611 #type complete TITLE cytochrome c [validated] - Caenorhabditis elegans ALTERNATE_NAMES protein E04A4.7 ORGANISM #formal_name Caenorhabditis elegans DATE 03-Mar-2000 #sequence_revision 03-Mar-2000 #text_change 28-Jul-2000 ACCESSIONS T32611; S13048 REFERENCE Z21199 !$#authors Sammons, L.; Wohldmann, P.; Biewald, T. !$#submission submitted to the EMBL Data Library, December 1997 !$#description The sequence of C. elegans cosmid E04A4. !$#accession T32611 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-111 ##label SAM !'##cross-references EMBL:AF038611; PIDN:AAB92035.1; GSPDB:GN00022; !1CESP:E04A4.7 !'##experimental_source strain Bristol N2; clone E04A4 REFERENCE S13048 !$#authors Vanfleteren, J.R.; Evers, E.A.I.M.; van de Werken, G.; van !1Beeumen, J.J. !$#journal Biochem. J. (1990) 271:613-620 !$#title The primary structure of cytochrome c from the nematode !1Caenorhabditis elegans. !$#cross-references MUID:91058490; PMID:2173902 !$#accession S13048 !'##molecule_type protein !'##residues 2-65,'K',67-111 ##label VAN GENETICS !$#gene CESP:E04A4.7 !$#map_position 4 !$#introns 60/3 CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; metalloprotein; mitochondrion FEATURE !$10-103 #domain cytochrome c homology #label CYC\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental\ !$20,23 #binding_site heme (Cys) (covalent) #status !8experimental\ !$24,85 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 111 #molecular-weight 12261 #checksum 9203 SEQUENCE /// ENTRY T27492 #type complete TITLE cytochrome c ZC116.2 - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 03-Nov-2000 #sequence_revision 03-Nov-2000 #text_change 03-Nov-2000 ACCESSIONS T27492 REFERENCE Z20376 !$#authors Smye, R. !$#submission submitted to the EMBL Data Library, June 1996 !$#accession T27492 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-123 ##label WIL !'##cross-references EMBL:Z74046; PIDN:CAA98555.1; GSPDB:GN00023; !1CESP:ZC116.2 !'##experimental_source clone ZC116 GENETICS !$#gene CESP:ZC116.2 !$#map_position 5 !$#introns 24/3; 94/3 CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS chromoprotein; heme; iron; metalloprotein FEATURE !$20-113 #domain cytochrome c homology #label CYC\ !$30,33 #binding_site heme (Cys) (covalent) #status !8predicted\ !$34,95 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 123 #molecular-weight 13362 #checksum 3166 SEQUENCE /// ENTRY CCWB #type complete TITLE cytochrome c - earthworm (Eisenia foetida) ORGANISM #formal_name Eisenia foetida #common_name common brandling worm, common dung-worm DATE 24-Apr-1984 #sequence_revision 01-Feb-1985 #text_change 03-Mar-2000 ACCESSIONS A00027 REFERENCE A00027 !$#authors Lyddiatt, A.; Boulter, D. !$#journal FEBS Lett. (1976) 62:85-88 !$#title The amino acid sequence of cytochrome c from Eisenia foetida !1(Savigny) (common brandling worm). !$#cross-references MUID:76118291; PMID:174956 !$#accession A00027 !'##molecule_type protein !'##residues 1-108 ##label LYD CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1respiratory chain FEATURE !$9-103 #domain cytochrome c homology #label CYC\ !$19,22 #binding_site heme (Cys) (covalent) #status !8predicted\ !$23,85 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 108 #molecular-weight 11815 #checksum 3249 SEQUENCE /// ENTRY CCMM #type complete TITLE cytochrome c - monsoon river-prawn ORGANISM #formal_name Macrobrachium malcolmsonii #common_name monsoon river-prawn DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 11-May-2000 ACCESSIONS A00028 REFERENCE A00028 !$#authors Lyddiatt, A.; Boulter, D. !$#journal Comp. Biochem. Physiol. B (1976) 55:337-342 !$#title A comparison of cytochrome C from Macrobrachium malcomsonii !1with other invertebrate cytochromes C. !$#cross-references MUID:77024998; PMID:185001 !$#accession A00028 !'##molecule_type protein !'##residues 1-104 ##label LYD CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS blocked amino end; chromoprotein; electron transfer; heme; !1iron; metalloprotein; mitochondrion; oxidative !1phosphorylation; respiratory chain FEATURE !$4-98 #domain cytochrome c homology #label CYC\ !$1 #modified_site blocked amino end (Gly) (probably !8acetylated) #status experimental\ !$14,17 #binding_site heme (Cys) (covalent) #status !8predicted\ !$18,80 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 104 #molecular-weight 11430 #checksum 61 SEQUENCE /// ENTRY CCHA #type complete TITLE cytochrome c [validated] - brown garden snail ORGANISM #formal_name Helix aspersa #common_name brown garden snail DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 28-Jul-2000 ACCESSIONS A00029 REFERENCE A00029 !$#authors Brown, R.H.; Richardson, M.; Boulter, D.; Ramshaw, J.A.M.; !1Jefferies, R.P.S. !$#journal Biochem. J. (1972) 128:971-974 !$#title The amino acid sequence of cytochrome c from Helix aspersa !1Mueller (garden snail). !$#cross-references MUID:73054484; PMID:4344699 !$#accession A00029 !'##molecule_type protein !'##residues 1-104 ##label BRO !'##note the amidation states of residues 16, 21, 52, 70, and 90 were !1assigned by homology with other cytochromes c CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1respiratory chain FEATURE !$4-98 #domain cytochrome c homology #label CYC\ !$14,17 #binding_site heme (Cys) (covalent) #status !8experimental\ !$18,80 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 104 #molecular-weight 11542 #checksum 596 SEQUENCE /// ENTRY CCFFCM #type complete TITLE cytochrome c - Mediterranean fruit fly ORGANISM #formal_name Ceratitis capitata #common_name Mediterranean fruit fly DATE 13-Jul-1981 #sequence_revision 30-Jun-1991 #text_change 03-Mar-2000 ACCESSIONS A00030 REFERENCE A00030 !$#authors Fernandez-Sousa, J.M.; Gavilanes, J.G.; Municio, A.M.; !1Paredes, J.A.; Perez-Aranda, A.; Rodriguez, R. !$#journal Biochim. Biophys. Acta (1975) 393:358-367 !$#title Primary structure of cytochrome c from the insect Ceratitis !1capitata. !$#cross-references MUID:75205681; PMID:167835 !$#accession A00030 !'##molecule_type protein !'##residues 1-107 ##label FER !'##note some peptides were positioned by homology CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1respiratory chain FEATURE !$8-102 #domain cytochrome c homology #label CYC\ !$18,21 #binding_site heme (Cys) (covalent) #status !8predicted\ !$22,84 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 107 #molecular-weight 11603 #checksum 9121 SEQUENCE /// ENTRY CCFFDM #type complete TITLE cytochrome c DC4 - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 30-Jun-1991 #sequence_revision 20-Aug-1994 #text_change 03-Mar-2000 ACCESSIONS A22945; A23058; A25506; A38039; A00030 REFERENCE A94704 !$#authors Swanson, M.S.; Zieminn, S.M.; Miller, D.D.; Garber, E.A.E.; !1Margoliash, E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:1964-1968 !$#title Developmental expression of nuclear genes that encode !1mitochondrial proteins: insect cytochromes c. !$#cross-references MUID:85166253; PMID:2984675 !$#accession A22945 !'##molecule_type DNA !'##residues 1-108 ##label SWA !'##cross-references GB:M11381; NID:g157160; PIDN:AAA28437.1; !1PID:g157161 REFERENCE A93584 !$#authors Limbach, K.J.; Wu, R. !$#journal Nucleic Acids Res. (1985) 13:631-644 !$#title Characterization of two Drosophila melanogaster cytochrome c !1genes and their transcripts. !$#cross-references MUID:85215502; PMID:2987802 !$#accession A23058 !'##molecule_type DNA !'##residues 1-108 ##label LIM !'##cross-references GB:X01760; NID:g7782; PIDN:CAA25900.1; PID:g7783 REFERENCE A91907 !$#authors Inoue, S.; Inoue, H.; Hiroyoshi, T.; Matsubara, H.; !1Yamanaka, T. !$#journal J. Biochem. (1986) 100:955-965 !$#title Developmental variation and amino acid sequences of !1cytochromes c of the fruit fly Drosophila melanogaster and !1the flesh fly Boettcherisca peregrina. !$#cross-references MUID:87137362; PMID:3029051 !$#accession A25506 !'##molecule_type protein !'##residues 2-108 ##label INO REFERENCE A38039 !$#authors Nolan, C.; Weiss, L.J.; Adams, J.J.; Margoliash, E. !$#citation unpublished results, cited by Wojciech, R., and Margoliash, !1E., in Handbook of Biochemistry, Sober, H.A., ed., !1pp.C160-C161, Chemical Rubber Co., Cleveland, 1968 !$#accession A38039 !'##molecule_type protein !'##residues 2-54,'N',56-64,'QD',67-108 ##label NOL !'##note some peptides were positioned by homology COMMENT This protein is expressed at varying, but relatively high !1levels throughout development. GENETICS !$#gene DC4 !'##cross-references FlyBase:FBgn0000409 !$#map_position 2 36A 10-11 CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1respiratory chain FEATURE !$2-108 #product cytochrome c DC4 #status experimental #label !8MAT\ !$9-103 #domain cytochrome c homology #label CYC\ !$19,22 #binding_site heme (Cys) (covalent) #status !8predicted\ !$23,85 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 108 #molecular-weight 11735 #checksum 2946 SEQUENCE /// ENTRY CCFHHF #type complete TITLE cytochrome c - horn fly ORGANISM #formal_name Haematobia irritans #common_name horn fly DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 03-Mar-2000 ACCESSIONS A38040; A00030 REFERENCE A38040 !$#authors Chan, S.K.; Tulloss, I.; Margoliash, E. !$#submission submitted to the Atlas, July 1967 !$#accession A38040 !'##molecule_type protein !'##residues 1-107 ##label CHA !'##note some peptides were positioned by homology CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1respiratory chain FEATURE !$8-102 #domain cytochrome c homology #label CYC\ !$18,21 #binding_site heme (Cys) (covalent) #status !8predicted\ !$22,84 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 107 #molecular-weight 11636 #checksum 9515 SEQUENCE /// ENTRY CCHFGB #type complete TITLE cytochrome c - greenbottle fly (Lucilia cuprina) (tentative sequence) ORGANISM #formal_name Lucilia cuprina DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 03-Mar-2000 ACCESSIONS A38041; A00030 REFERENCE A38041 !$#authors Shaw, D.C.; Williams, K.L.; Smith, E.; Birt, L.M. !$#journal Biochim. Biophys. Acta (1978) 532:179-184 !$#title The amino acid sequence of cytochrome c from the blowfly !1Lucilia cuprina. !$#cross-references MUID:78080930; PMID:202328 !$#accession A38041 !'##molecule_type protein !'##residues 1-107 ##label SHA !'##note the compositions of the tryptic peptides and the sequence of !1residues 44-49 were determined CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1respiratory chain FEATURE !$8-102 #domain cytochrome c homology #label CYC\ !$18,21 #binding_site heme (Cys) (covalent) #status !8predicted\ !$22,84 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 107 #molecular-weight 11662 #checksum 235 SEQUENCE /// ENTRY CCLQ #type complete TITLE cytochrome c - desert locust ORGANISM #formal_name Schistocerca gregaria #common_name desert locust DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 03-Mar-2000 ACCESSIONS A00033 REFERENCE A00033 !$#authors Lyddiatt, A.; Boulter, D. !$#journal Biochem. J. (1977) 163:333-338 !$#title The amino acid sequence of cytochrome c from the locust, !1Schistocerca gregaria Forskal. !$#cross-references MUID:77201499; PMID:194585 !$#accession A00033 !'##molecule_type protein !'##residues 1-107 ##label LYD CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1respiratory chain FEATURE !$8-102 #domain cytochrome c homology #label CYC\ !$18,21 #binding_site heme (Cys) (covalent) #status !8predicted\ !$22,84 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 107 #molecular-weight 11812 #checksum 702 SEQUENCE /// ENTRY CCMT #type complete TITLE cytochrome c [validated] - ailanthus silkmoth ORGANISM #formal_name Samia cynthia #common_name ailanthus silkmoth DATE 13-Jul-1981 #sequence_revision 23-Oct-1981 #text_change 28-Jul-2000 ACCESSIONS A00032 REFERENCE A92025 !$#authors Chan, S.K.; Margoliash, E. !$#journal J. Biol. Chem. (1966) 241:335-348 !$#title Properties and primary structure of the cytochrome c from !1the flight muscles of the moth, Samia cynthia. !$#cross-references MUID:66080329; PMID:5903726 !$#accession A00032 !'##molecule_type protein !'##residues 1-107 ##label CHA CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1respiratory chain FEATURE !$8-102 #domain cytochrome c homology #label CYC\ !$18,21 #binding_site heme (Cys) (covalent) #status !8experimental\ !$22,84 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 107 #molecular-weight 11632 #checksum 1307 SEQUENCE /// ENTRY CCWOT #type complete TITLE cytochrome c - tobacco hornworm (tentative sequence) ORGANISM #formal_name Manduca sexta #common_name tobacco hornworm DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Mar-2000 ACCESSIONS A90578; B22945; A00032 REFERENCE A90578 !$#authors Chan, S.K. !$#journal Biochim. Biophys. Acta (1970) 221:497-501 !$#title Biochemical studies in the developing thoracic muscles of !1the tobacco horn worm. !$#cross-references MUID:71108407; PMID:5499433 !$#accession A90578 !'##molecule_type protein !'##residues 1-107 ##label CHA !'##note the compositions of chymotryptic peptides were determined and !1residues were ordered by homology with silkmoth cytochrome c REFERENCE A94704 !$#authors Swanson, M.S.; Zieminn, S.M.; Miller, D.D.; Garber, E.A.E.; !1Margoliash, E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:1964-1968 !$#title Developmental expression of nuclear genes that encode !1mitochondrial proteins: insect cytochromes c. !$#cross-references MUID:85166253; PMID:2984675 !$#accession B22945 !'##molecule_type mRNA !'##residues 26-31,'I',33-53,'D',55-63,'NE',66-107 ##label SWA !'##cross-references GB:M11382; NID:g159496; PIDN:AAA29308.1; !1PID:g159497 !'##note the authors translated the codon GAT for residue 29 as Asn, AAT !1for residue 39 as Gln, and GAG for residue 40 as Asp CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1respiratory chain FEATURE !$8-102 #domain cytochrome c homology #label CYC\ !$18,21 #binding_site heme (Cys) (covalent) #status !8predicted\ !$22,84 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 107 #molecular-weight 11656 #checksum 309 SEQUENCE /// ENTRY B23058 #type complete TITLE cytochrome c DC3 - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 29-Aug-1987 #sequence_revision 20-Aug-1994 #text_change 03-Mar-2000 ACCESSIONS B23058 REFERENCE A93584 !$#authors Limbach, K.J.; Wu, R. !$#journal Nucleic Acids Res. (1985) 13:631-644 !$#title Characterization of two Drosophila melanogaster cytochrome c !1genes and their transcripts. !$#cross-references MUID:85215502; PMID:2987802 !$#accession B23058 !'##molecule_type DNA !'##residues 1-105 ##label LIM !'##cross-references GB:X01761; NID:g7780; PIDN:CAA25901.1; PID:g7781 COMMENT This protein is expressed at constant, but relatively low !1levels during development. GENETICS !$#gene DC3 !'##cross-references FlyBase:FBgn0000408 !$#map_position 2 36A 10-11 CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1respiratory chain FEATURE !$2-105 #product cytochrome c DC3 #status predicted #label !8MAT\ !$7-101 #domain cytochrome c homology #label CYC\ !$17,20 #binding_site heme (Cys) (covalent) #status !8predicted\ !$21,83 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 105 #molecular-weight 11369 #checksum 2256 SEQUENCE /// ENTRY CCHB #type complete TITLE cytochrome c [validated] - honeybee ORGANISM #formal_name Apis mellifera #common_name honeybee DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 28-Jul-2000 ACCESSIONS A00031 REFERENCE A00031 !$#authors Inoue, S.; Matsubara, H.; Yamanaka, T. !$#journal J. Biochem. (1985) 97:947-954 !$#title Complete amino acid sequence of cytochrome c from the !1honeybee, Apis mellifera, and evolutionary relationship of !1the honey bee to other insects on the basis of the amino !1acid sequence. !$#cross-references MUID:85261185; PMID:2991212 !$#accession A00031 !'##molecule_type protein !'##residues 1-107 ##label INO CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1respiratory chain FEATURE !$8-102 #domain cytochrome c homology #label CYC\ !$18,21 #binding_site heme (Cys) (covalent) #status !8experimental\ !$22,84 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 107 #molecular-weight 11778 #checksum 3045 SEQUENCE /// ENTRY CCHQ #type complete TITLE cytochrome c - yeast (Pichia anomala) (tentative sequence) ORGANISM #formal_name Pichia anomala, Candida pelliculosa DATE 23-Oct-1981 #sequence_revision 23-Oct-1981 #text_change 31-Mar-2000 ACCESSIONS A00035 REFERENCE A00035 !$#authors Becam, A.M.; Lederer, F. !$#journal Eur. J. Biochem. (1981) 118:295-302 !$#title Amino-acid sequence of the cytochrome c from the yeast !1Hansenula anomala. Identification of three methylated !1positions. !$#cross-references MUID:82027230; PMID:6269851 !$#accession A00035 !'##molecule_type protein !'##residues 1-109 ##label BEC CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; methylated amino acid; mitochondrion; !1oxidative phosphorylation; respiratory chain FEATURE !$10-104 #domain cytochrome c homology #label CYC\ !$20,23 #binding_site heme (Cys) (covalent) #status !8experimental\ !$24,86 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted\ !$61 #modified_site N6-methyllysine or N6, !8N6-dimethyllysine (Lys) #status experimental\ !$78,79 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental SUMMARY #length 109 #molecular-weight 12064 #checksum 9757 SEQUENCE /// ENTRY CCDBK #type complete TITLE cytochrome c [validated] - yeast (Torulaspora hansenii) ORGANISM #formal_name Torulaspora hansenii, Debaryomyces hansenii, Candida famata DATE 23-Oct-1981 #sequence_revision 23-Oct-1981 #text_change 28-Jul-2000 ACCESSIONS A00036 REFERENCE A00036 !$#authors Sugeno, K.; Narita, K.; Titani, K. !$#journal J. Biochem. (1971) 70:659-682 !$#title The amino acid sequence of cytochrome c from Debaryomyces !1kloeckeri. !$#cross-references MUID:72091989; PMID:5137335 !$#accession A00036 !'##molecule_type protein !'##residues 1-109 ##label SUG !'##note the source was designated as Debaryomyces kloeckeri CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; methylated amino acid; mitochondrion; !1oxidative phosphorylation; respiratory chain FEATURE !$10-104 #domain cytochrome c homology #label CYC\ !$20,23 #binding_site heme (Cys) (covalent) #status !8experimental\ !$24,86 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted\ !$78 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental SUMMARY #length 109 #molecular-weight 11998 #checksum 770 SEQUENCE /// ENTRY CCCK #type complete TITLE cytochrome c [validated] - yeast (Issatchenkia orientalis) ORGANISM #formal_name Issatchenkia orientalis, Candida krusei DATE 23-Oct-1981 #sequence_revision 23-Oct-1981 #text_change 28-Jul-2000 ACCESSIONS A91919; A91202; A91401; A00034 REFERENCE A91919 !$#authors Narita, K.; Titani, K. !$#journal J. Biochem. (1968) 63:226-241 !$#title The amino acid sequence of cytochrome c from Candida krusei. !$#cross-references MUID:68368768; PMID:5669923 !$#accession A91919 !'##molecule_type protein !'##residues 1-21,'E',23-109 ##label NAR REFERENCE A91202 !$#authors Lederer, F. !$#journal Eur. J. Biochem. (1972) 31:144-147 !$#title Candida krusei cytochrome c: a correction to the sequence. !1Glutamine-16, an invariant residue in mitochondrial !1cytochrome c? !$#cross-references MUID:73060342; PMID:4344910 !$#accession A91202 !'##molecule_type protein !'##residues 1-38 ##label LED REFERENCE A91401 !$#authors Machleidt, W.; Wachter, E.; Scheulen, M.; Otto, J. !$#journal FEBS Lett. (1973) 37:217-220 !$#title Solid-phase edman degradation of a protein: N-terminal !1sequence of cytochrome c from Candida krusei. !$#cross-references MUID:74055069; PMID:4357820 !$#accession A91401 !'##molecule_type protein !'##residues 1-35 ##label MAC REFERENCE A92060 !$#authors DeLange, R.J.; Glazer, A.N.; Smith, E.L. !$#journal J. Biol. Chem. (1970) 245:3325-3327 !$#title Identification and location of epsilon-N-trimethyllysine in !1yeast cytochrome c. !$#cross-references MUID:70293148; PMID:5459636 !$#contents annotation; methylation CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; methylated amino acid; mitochondrion; !1oxidative phosphorylation; respiratory chain FEATURE !$10-104 #domain cytochrome c homology #label CYC\ !$20,23 #binding_site heme (Cys) (covalent) #status !8experimental\ !$24,86 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted\ !$78 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8predicted SUMMARY #length 109 #molecular-weight 11888 #checksum 9054 SEQUENCE /// ENTRY CCBY #type complete TITLE cytochrome c 1 [validated] - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES iso-1-cytochrome c; protein GTA109; protein J1653; protein YJR048w ORGANISM #formal_name Saccharomyces cerevisiae DATE 24-Apr-1984 #sequence_revision 30-Jun-1992 #text_change 28-Jul-2000 ACCESSIONS A00037; S46588; A91921; S22785; S57067; S63773 REFERENCE A90782 !$#authors Smith, M.; Leung, D.W.; Gillam, S.; Astell, C.R.; !1Montgomery, D.L.; Hall, B.D. !$#journal Cell (1979) 16:753-761 !$#title Sequence of the gene for iso-1-cytochrome c in Saccharomyces !1cerevisiae. !$#cross-references MUID:79211240; PMID:222467 !$#accession A00037 !'##molecule_type DNA !'##residues 1-109 ##label SMI !'##cross-references EMBL:V01298; NID:g3626; PIDN:CAA24605.1; PID:g3627 REFERENCE S46588 !$#authors Huang, M.E.; Manus, V.; Chuat, J.C.; Galibert, F. !$#journal Yeast (1994) 10:811-818 !$#title Revised nucleotide sequence of the COR region of yeast !1Saccharomyces cerevisiae chromosome X. !$#cross-references MUID:95066383; PMID:7975898 !$#accession S46588 !'##status translation not shown !'##molecule_type DNA !'##residues 1-109 ##label HUA !'##cross-references EMBL:L26347; NID:g508621; PIDN:AAA62856.1; !1PID:g695795 REFERENCE A91921 !$#authors Narita, K.; Titani, K. !$#journal J. Biochem. (1969) 65:259-267 !$#title The complete amino acid sequence in baker's yeast cytochrome !1c. !$#cross-references MUID:69191928; PMID:5771953 !$#accession A91921 !'##molecule_type protein !'##residues 2-20,'EL',23-109 ##label NAR !'##note the final paper in a series !'##note the source is designated as S. oviformis REFERENCE S22785 !$#authors McNeil, J.B.; Smith, M. !$#journal J. Mol. Biol. (1986) 187:363-378 !$#title Transcription initiation of the Saccharomyces cerevisiae !1iso-1-cytochrome c gene. Multiple, independent T-A-T-A !1sequences. !$#cross-references MUID:86200219; PMID:3009831 !$#accession S22785 !'##molecule_type DNA !'##residues 1-22 ##label MCN !'##cross-references EMBL:X03472; NID:g3613; PIDN:CAA27189.1; PID:g3614 REFERENCE A92060 !$#authors DeLange, R.J.; Glazer, A.N.; Smith, E.L. !$#journal J. Biol. Chem. (1970) 245:3325-3327 !$#title Identification and location of epsilon-N-trimethyllysine in !1yeast cytochrome c. !$#cross-references MUID:70293148; PMID:5459636 !$#contents annotation; location of trimethyllysine for isoform 1 REFERENCE S57052 !$#authors Huang, M.E.; Chuat, J.C.; Galibert, F. !$#submission submitted to the Protein Sequence Database, September 1995 !$#accession S57067 !'##molecule_type DNA !'##residues 1-109 ##label MAN !'##cross-references EMBL:Z49548; NID:g1015706; PIDN:CAA89576.1; !1PID:g1015707; GSPDB:GN00010; MIPS:YJR048w REFERENCE S63757 !$#authors Huang, M.E.; Chuat, J.C.; Galibert, F. !$#journal Yeast (1995) 11:775-781 !$#title Analysis of a 42.5 kb DNA sequence of chromosome X reveals !1three tRNA genes and 14 new open reading frames including a !1gene most probably belonging to the family of !1ubiquitin-protein ligases. !$#cross-references MUID:95397595; PMID:7668047 !$#accession S63773 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-109 ##label HUW !'##cross-references EMBL:L36344; NID:g1197060; PIDN:AAA88751.1; !1PID:g1197077 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1February 1996 GENETICS !$#gene SGD:CYC1; MIPS:YJR048w !'##cross-references SGD:S0003809; MIPS:YJR048w !$#map_position 10R !$#genome nuclear CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; methylated amino acid; mitochondrion; !1oxidative phosphorylation; respiratory chain FEATURE !$2-109 #product cytochrome c #status experimental #label !8MAT\ !$10-104 #domain cytochrome c homology #label CYC\ !$20,23 #binding_site heme (Cys) (covalent) #status !8experimental\ !$24,86 #binding_site heme iron (His, Met) (axial ligands) !8#status experimental\ !$78 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental SUMMARY #length 109 #molecular-weight 12182 #checksum 8287 SEQUENCE /// ENTRY CCBYBC #type complete TITLE cytochrome c2 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES iso-2-cytochrome c ORGANISM #formal_name Saccharomyces cerevisiae DATE 28-Feb-1981 #sequence_revision 13-Jul-1981 #text_change 23-Mar-2001 ACCESSIONS A00038; S30842; S50505; S18478; S18480 REFERENCE A00038 !$#authors Montgomery, D.L.; Leung, D.W.; Smith, M.; Shalit, P.; Faye, !1G.; Hall, B.D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1980) 77:541-545 !$#title Isolation and sequence of the gene for iso-2-cytochrome c in !1Saccharomyces cerevisiae. !$#cross-references MUID:80145659; PMID:6244566 !$#accession A00038 !'##molecule_type DNA !'##residues 1-113 ##label MON !'##cross-references EMBL:V01299; NID:g3628; PIDN:CAA24606.1; PID:g3629 REFERENCE S30812 !$#authors Mulligan, J.T.; Dietrich, F.S.; Hennessey, K.M.; Sehl, P.; !1Komp, C.; Wei, Y.; Taylor, P.; Nakahara, K.; Roberts, D.; !1Davis, R.W. !$#submission submitted to the EMBL Data Library, February 1993 !$#accession S30842 !'##molecule_type DNA !'##residues 1-113 ##label MUL !'##cross-references GB:U18779; EMBL:L10830; NID:g603625; !1PIDN:AAB65003.1; PID:g603640 REFERENCE S50429 !$#authors Dietrich, F.S. !$#submission submitted to the EMBL Data Library, December 1994 !$#description The sequence of S. cerevisiae cosmids 8199, 8334, and 9871. !$#accession S50505 !'##molecule_type DNA !'##residues 1-113 ##label DIE !'##cross-references EMBL:U18779; NID:g603625; PIDN:AAB65003.1; !1PID:g603640; GSPDB:GN00005; MIPS:YEL039c REFERENCE S18478 !$#authors Sokolik, C.W.; Cohen, R.E. !$#journal J. Biol. Chem. (1991) 266:9100-9107 !$#title The structures of ubiquitin conjugates of yeast !1iso-2-cytochrome c. !$#cross-references MUID:91225014; PMID:1851166 !$#accession S18478 !'##molecule_type protein !'##residues 2-113 ##label SOK1 !'##note the location of the trimethyllysine was determined for isoform !12 !$#accession S18480 !'##molecule_type protein !'##residues 2-24 ##label SOK2 !'##note the amino-terminal sequence of isoform 2 as synthesized and !1ubiquitinylated by an in vitro rabbit system was determined REFERENCE A92060 !$#authors DeLange, R.J.; Glazer, A.N.; Smith, E.L. !$#journal J. Biol. Chem. (1970) 245:3325-3327 !$#title Identification and location of epsilon-N-trimethyllysine in !1yeast cytochrome c. !$#cross-references MUID:70293148; PMID:5459636 !$#contents annotation; methylation GENETICS !$#gene SGD:CYC7; CYP3; MIPS:YEL039c !'##cross-references MIPS:YEL039c; SGD:S0000765 !$#map_position 5L !$#genome nuclear CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; methylated amino acid; mitochondrion; !1oxidative phosphorylation; respiratory chain FEATURE !$14-108 #domain cytochrome c homology #label CYC\ !$24,27 #binding_site heme (Cys) (covalent) #status !8predicted\ !$28,90 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted\ !$82 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental SUMMARY #length 113 #molecular-weight 12532 #checksum 6332 SEQUENCE /// ENTRY CCZP #type complete TITLE cytochrome c - fission yeast (Schizosaccharomyces pombe) ORGANISM #formal_name Schizosaccharomyces pombe DATE 24-Apr-1984 #sequence_revision 28-Jul-2000 #text_change 28-Jul-2000 ACCESSIONS T41220; T42217; A00039 REFERENCE Z21904 !$#authors Lyne, M.; Rajandream, M.A.; Barrell, B.G.; Volckaert, G. !$#submission submitted to the EMBL Data Library, March 1998 !$#accession T41220 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-109 ##label LYN !'##cross-references EMBL:AL049644; PIDN:CAB41053.1; GSPDB:GN00066; !1SPDB:SPCC191.07 !'##experimental_source strain 972h-; cosmid c191 REFERENCE Z22082 !$#authors Russell, P.R.; Hall, B.D. !$#journal Mol. Cell. Biol. (1982) 2:106-116 !$#title Structure of the Schizosaccharomyces pombe cytochrome c !1gene. !$#cross-references MUID:82271854; PMID:6287225 !$#accession T42217 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-109 ##label RUS !'##cross-references EMBL:J01318; NID:g173376; PIDN:AAA35300.1; !1PID:g173377 REFERENCE A00039 !$#authors Simon-Becam, A.M.; Claisse, M.; Lederer, F. !$#journal Eur. J. Biochem. (1978) 86:407-416 !$#title Cytochrome c from Schizosaccharomyces pombe. 2. Amino-acid !1sequence. !$#cross-references MUID:78190652; PMID:207525 !$#accession A00039 !'##molecule_type protein !'##residues 2-57,'K',59,'R',61-64,'BZZ',68-109 ##label SIM GENETICS !$#gene SPDB:SPCC191.07 !$#map_position 1 CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; methylated amino acid; mitochondrion; !1oxidative phosphorylation; respiratory chain FEATURE !$2-109 #product cytochrome c #status experimental #label !8MAT\ !$9-103 #domain cytochrome c homology #label CYC\ !$19,22 #binding_site heme (Cys) (covalent) #status !8experimental\ !$23,85 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted\ !$77 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental SUMMARY #length 109 #molecular-weight 12022 #checksum 8881 SEQUENCE /// ENTRY CCHL #type complete TITLE cytochrome c - imperfect fungus (Thermomyces lanuginosus) (tentative sequence) ORGANISM #formal_name Thermomyces lanuginosus, Humicola lanuginosa DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 31-Mar-2000 ACCESSIONS A92114; B90188; A00040 REFERENCE A92114 !$#authors Morgan, W.T.; Hensley Jr., C.P.; Riehm, J.P. !$#journal J. Biol. Chem. (1972) 247:6555-6565 !$#title Proteins of the thermophilic fungus Humicola lanuginosa. I. !1Isolation and amino acid sequence of a cytochrome c. !$#cross-references MUID:73015873; PMID:4342602 !$#accession A92114 !'##molecule_type protein !'##residues 1-10,'SA',13-23,'E',25-26,'GEGANVSQ',35-111 ##label MOR !'##experimental_source ATCC 16455 REFERENCE A90188 !$#authors Lederer, F.; Simon, A.M. !$#journal Biochem. Biophys. Res. Commun. (1974) 56:317-323 !$#title Neurospora crassa and Humicola lanuginosa cytochromes C: !1more homology in the heme region. !$#cross-references MUID:74147482; PMID:4363050 !$#accession B90188 !'##molecule_type protein !'##residues 1-37 ##label LED !'##note residues at positions 21, 22, 25, 26, 27, and 34 were not !1positively identified CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; methylated amino acid; mitochondrion; !1oxidative phosphorylation; respiratory chain FEATURE !$12-106 #domain cytochrome c homology #label CYC\ !$22,25 #binding_site heme (Cys) (covalent) #status !8experimental\ !$26,88 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted\ !$80 #modified_site N6,N6-dimethyllysine (Lys) #status !8experimental\ !$94 #modified_site N6,N6,N6-trimethyllysine (Lys) !8(partial) #status experimental SUMMARY #length 111 #molecular-weight 12076 #checksum 8172 SEQUENCE /// ENTRY CCNC #type complete TITLE cytochrome c [validated] - Neurospora crassa ORGANISM #formal_name Neurospora crassa DATE 24-Apr-1984 #sequence_revision 12-Apr-1996 #text_change 28-Jul-2000 ACCESSIONS S48221; A92024; A90188; A00041 REFERENCE S48221 !$#authors Bottorff, D.A.; Parmaksizoglu, S.; Lemire, E.G.; Coffin, !1J.W.; Bertrand, H.; Nargang, F.E. !$#journal Curr. Genet. (1994) 26:329-335 !$#title Mutations in the structural gene for cytochrome c result in !1deficiency of both cytochromes aa(3) and c in Neurospora !1crassa. !$#cross-references MUID:95188270; PMID:7882427 !$#accession S48221 !'##status preliminary !'##molecule_type DNA !'##residues 1-108 ##label BOT !'##cross-references EMBL:L19358; NID:g388929; PIDN:AAA92156.1; !1PID:g388930 REFERENCE A92024 !$#authors Heller, J.; Smith, E.L. !$#journal J. Biol. Chem. (1966) 241:3165-3180 !$#title Neurospora crassa cytochrome c. II. Chymotryptic peptides, !1tryptic peptides, cyanogen bromide peptides, and the !1complete amino acid sequence. !$#cross-references MUID:67002604; PMID:5950080 !$#accession A92024 !'##molecule_type protein !'##residues 2-20,'E',22-23,'GEGGNLTQ',32-108 ##label HEL REFERENCE A90188 !$#authors Lederer, F.; Simon, A.M. !$#journal Biochem. Biophys. Res. Commun. (1974) 56:317-323 !$#title Neurospora crassa and Humicola lanuginosa cytochromes C: !1more homology in the heme region. !$#cross-references MUID:74147482; PMID:4363050 !$#accession A90188 !'##molecule_type protein !'##residues 2-44 ##label LED !'##note residues at positions 19, 22, and 43 were not positively !1identified !'##note at positions 33, 37, and 40, Leu could not be distinguished !1from Ile REFERENCE A92043 !$#authors DeLange, R.J.; Glazer, A.N.; Smith, E.L. !$#journal J. Biol. Chem. (1969) 244:1385-1388 !$#title Presence and location of an unusual amino acid, !1epsilon-N-trimethyllysine, in cytochrome c of wheat germ and !1Neurospora. !$#cross-references MUID:69128197; PMID:4304194 !$#contents annotation; methylation GENETICS !$#introns 6/1; 101/2 CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; methylated amino acid; mitochondrion; !1oxidative phosphorylation; respiratory chain FEATURE !$9-103 #domain cytochrome c homology #label CYC\ !$19,22 #binding_site heme (Cys) (covalent) #status !8experimental\ !$23,85 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted\ !$77 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental SUMMARY #length 108 #molecular-weight 11813 #checksum 2280 SEQUENCE /// ENTRY CCUS #type complete TITLE cytochrome c - smut fungus (Ustilago sphaerogena) (tentative sequence) ORGANISM #formal_name Ustilago sphaerogena DATE 24-Apr-1984 #sequence_revision 30-Sep-1988 #text_change 31-Mar-2000 ACCESSIONS A00042 REFERENCE A00042 !$#authors Bitar, K.G.; Vinogradov, S.N.; Nolan, C.; Weiss, L.J.; !1Margoliash, E. !$#journal Biochem. J. (1972) 129:561-569 !$#title The primary structure of cytochrome c from the rust fungus !1Ustilago sphaerogena. !$#cross-references MUID:73161218; PMID:4349112 !$#accession A00042 !'##molecule_type protein !'##residues 1-107 ##label BIT !'##experimental_source ATCC 12421 CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1respiratory chain FEATURE !$8-102 #domain cytochrome c homology #label CYC\ !$18,21 #binding_site heme (Cys) (covalent) #status !8experimental\ !$22,84 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted\ !$76 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8absent SUMMARY #length 107 #molecular-weight 11945 #checksum 1839 SEQUENCE /// ENTRY CCRPBN #type complete TITLE cytochrome c [validated] - rape ORGANISM #formal_name Brassica napus #common_name rape DATE 13-Jul-1981 #sequence_revision 13-Jul-1981 #text_change 28-Jul-2000 ACCESSIONS A00043 REFERENCE A00043 !$#authors Richardson, M.; Ramshaw, J.A.M.; Boulter, D. !$#journal Biochim. Biophys. Acta (1971) 251:331-333 !$#title The amino acid sequence of rape (Brassica napus L.) !1cytochrome c. !$#accession A00043 !'##molecule_type protein !'##residues 1-111 ##label RIC !'##note 109-Ser was found in 40% of the molecules CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS blocked amino end; chromoprotein; electron transfer; heme; !1iron; metalloprotein; methylated amino acid; mitochondrion; !1oxidative phosphorylation; polymorphism; respiratory chain FEATURE !$12-106 #domain cytochrome c homology #label CYC\ !$1 #modified_site blocked amino end (Ala) (probably !8acetylated) #status experimental\ !$22,25 #binding_site heme (Cys) (covalent) #status !8experimental\ !$26,88 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted\ !$80,94 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental SUMMARY #length 111 #molecular-weight 12083 #checksum 8274 SEQUENCE /// ENTRY CCRPBO #type complete TITLE cytochrome c - cauliflower ORGANISM #formal_name Brassica oleracea var. botrytis #common_name cauliflower DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS A04613; A00043 REFERENCE A04613 !$#authors Thompson, E.W.; Richardson, M.; Boulter, D. !$#journal Biochem. J. (1971) 124:783-785 !$#title The amino acid sequence of cytochrome c of Fagopyrum !1esculentum Moench (buckwheat) and Brassica oleracea L. !1(cauliflower). !$#cross-references MUID:72074418; PMID:5131734 !$#accession A04613 !'##molecule_type protein !'##residues 1-111 ##label THO CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS blocked amino end; chromoprotein; electron transfer; heme; !1iron; metalloprotein; methylated amino acid; mitochondrion; !1oxidative phosphorylation; polymorphism; respiratory chain FEATURE !$12-106 #domain cytochrome c homology #label CYC\ !$1 #modified_site blocked amino end (Ala) (probably !8acetylated) #status experimental\ !$22,25 #binding_site heme (Cys) (covalent) #status !8predicted\ !$26,88 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted\ !$80,94 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental SUMMARY #length 111 #molecular-weight 12083 #checksum 8274 SEQUENCE /// ENTRY CCPU #type complete TITLE cytochrome c - winter squash ORGANISM #formal_name Cucurbita maxima #common_name winter squash DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 23-Sep-2002 ACCESSIONS A00044 REFERENCE A00044 !$#authors Thompson, E.W.; Richardson, M.; Boulter, D. !$#journal Biochem. J. (1971) 124:779-781 !$#title The amino acid sequence of cytochrome c from Cucurbita !1maxima L. (pumpkin). !$#cross-references MUID:72074417; PMID:5131733 !$#accession A00044 !'##molecule_type protein !'##residues 1-111 ##label THO !'##note 47-Lys, 52-Ala, and 109-Ser were also found CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS blocked amino end; chromoprotein; electron transfer; heme; !1iron; metalloprotein; methylated amino acid; mitochondrion; !1oxidative phosphorylation; polymorphism; respiratory chain FEATURE !$12-106 #domain cytochrome c homology #label CYC\ !$1 #modified_site blocked amino end (Ala) (probably !8acetylated) #status experimental\ !$22,25 #binding_site heme (Cys) (covalent) #status !8predicted\ !$26,88 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted\ !$80,94 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental SUMMARY #length 111 #molecular-weight 12121 #checksum 9132 SEQUENCE /// ENTRY CCMB #type complete TITLE cytochrome c - mung bean ORGANISM #formal_name Vigna radiata #common_name mung bean DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 03-Mar-2000 ACCESSIONS A00045; C00047 REFERENCE A94560 !$#authors Thompson, E.W.; Laycock, M.V.; Ramshaw, J.A.M.; Boulter, D. !$#submission submitted to the Atlas, August 1970 !$#accession A00045 !'##molecule_type protein !'##residues 1-111 ##label THO REFERENCE A90248 !$#authors Thompson, E.W.; Laycock, M.V.; Ramshaw, J.A.M.; Boulter, D. !$#journal Biochem. J. (1970) 117:183-192 !$#title The amino acid sequence of Phaseolus aureus L. (mung-bean) !1cytochrome c. !$#cross-references MUID:70207558; PMID:5420954 !$#contents annotation; sequence REFERENCE A00047 !$#authors Thompson, E.W.; Richardson, M.; Boulter, D. !$#journal Biochem. J. (1971) 121:439-446 !$#title The amino acid sequence of sesame (Sesamum indicum L.) and !1castor (Ricinus communis L.) cytochrome c. !$#cross-references MUID:72042446; PMID:5119781 !$#accession C00047 !'##molecule_type protein !'##residues 1-3,'BZ',6-9,'B',11-111 ##label TH2 CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; metalloprotein; methylated amino acid; !1mitochondrion; oxidative phosphorylation; respiratory chain FEATURE !$12-106 #domain cytochrome c homology #label CYC\ !$1 #modified_site acetylated amino end (Ala) #status !8predicted\ !$22,25 #binding_site heme (Cys) (covalent) #status !8predicted\ !$26,88 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted\ !$80,94 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8predicted SUMMARY #length 111 #molecular-weight 12132 #checksum 9511 SEQUENCE /// ENTRY CCHECC #type complete TITLE cytochrome c [validated] - hemp ORGANISM #formal_name Cannabis sativa #common_name hemp, marijuana DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 28-Jul-2000 ACCESSIONS A00046 REFERENCE A00046 !$#authors Wallace, D.G.; Brown, R.H.; Boulter, D. !$#journal Phytochemistry (1973) 12:2617-2622 !$#title The amino acid sequence of Cannabis sativa cytochrome-c. !$#accession A00046 !'##molecule_type protein !'##residues 1-111 ##label WAL CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS blocked amino end; chromoprotein; electron transfer; heme; !1iron; metalloprotein; methylated amino acid; mitochondrion; !1oxidative phosphorylation; respiratory chain FEATURE !$12-106 #domain cytochrome c homology #label CYC\ !$1 #modified_site blocked amino end (Ala) (probably !8acetylated) #status experimental\ !$22,25 #binding_site heme (Cys) (covalent) #status !8experimental\ !$26,88 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted\ !$80,94 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental SUMMARY #length 111 #molecular-weight 12043 #checksum 104 SEQUENCE /// ENTRY CCES #type complete TITLE cytochrome c [validated] - oriental sesame ORGANISM #formal_name Sesamum indicum #common_name oriental sesame DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 28-Jul-2000 ACCESSIONS A00047 REFERENCE A00047 !$#authors Thompson, E.W.; Richardson, M.; Boulter, D. !$#journal Biochem. J. (1971) 121:439-446 !$#title The amino acid sequence of sesame (Sesamum indicum L.) and !1castor (Ricinus communis L.) cytochrome c. !$#cross-references MUID:72042446; PMID:5119781 !$#accession A00047 !'##molecule_type protein !'##residues 1-111 ##label THO !'##note the authors placed the amides at positions 24, 70, and 97 by !1homology with other cytochromes c !'##note 4-Ser was found in 30% of the molecules CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; metalloprotein; methylated amino acid; !1mitochondrion; oxidative phosphorylation; respiratory chain FEATURE !$12-106 #domain cytochrome c homology #label CYC\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$22,25 #binding_site heme (Cys) (covalent) #status !8experimental\ !$26,88 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted\ !$80,94 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental SUMMARY #length 111 #molecular-weight 12051 #checksum 9448 SEQUENCE /// ENTRY CCRZ #type complete TITLE cytochrome c [validated] - rice ORGANISM #formal_name Oryza sativa #common_name rice DATE 31-Jul-1979 #sequence_revision 20-Aug-1994 #text_change 28-Jul-2000 ACCESSIONS JS0709; A00048; T02065 REFERENCE JS0709 !$#authors Nishi, R.; Uchimiya, H.; Kato, A. !$#submission submitted to JIPID, July 1992 !$#accession JS0709 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-112 ##label NIS !'##cross-references DDBJ:D12634; NID:g218248; PIDN:BAA02159.1; !1PID:g218249 !'##experimental_source strain Yamahousi REFERENCE A00048 !$#authors Mori, E.; Morita, Y. !$#journal J. Biochem. (1980) 87:249-266 !$#title Amino acid sequence of cytochrome c from rice. !$#cross-references MUID:80137364; PMID:6244261 !$#accession A00048 !'##molecule_type protein !'##residues 2-112 ##label MOR !'##note the amidation states of residues 25, 37, 40, 42, 48, 69, 70, !171, 98, and 99 were assigned by homology with other plant !1cytochrome c sequences REFERENCE Z14535 !$#authors Lee, M.C.; Kim, C.S.; Lee, J.S.; Eun, M.Y. !$#submission submitted to the EMBL Data Library, August 1997 !$#description Isolation and characterization of cytochrome C from rice. !$#accession T02065 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-85,'E',87-95,'NHRSVLI',103,'FPT' ##label LEE !'##cross-references EMBL:AF017367; NID:g2394299; PIDN:AAB70265.1; !1PID:g2394300 !'##experimental_source strain Milyang 23 CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; metalloprotein; methylated amino acid; !1mitochondrion; oxidative phosphorylation; respiratory chain FEATURE !$2-112 #product cytochrome c #status experimental #label !8MAT\ !$13-107 #domain cytochrome c homology #label CYC\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental\ !$23,26 #binding_site heme (Cys) (covalent) #status !8experimental\ !$27,89 #binding_site heme iron (His, Met) (axial ligands) !8#status experimental\ !$81,95 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental SUMMARY #length 112 #molecular-weight 12271 #checksum 4849 SEQUENCE /// ENTRY CCZM #type complete TITLE cytochrome c - maize ORGANISM #formal_name Zea mays #common_name maize DATE 19-Feb-1984 #sequence_revision 17-Feb-1994 #text_change 03-Mar-2000 ACCESSIONS A00049 REFERENCE A00049 !$#authors Boulter, D. !$#citation unpublished results, cited in Handbook of Biochemistry and !1Molecular Biology, 3rd ed., vol.3, Fasman, G.D., ed., !1pp.284-285, Chemical Rubber Co., Cleveland, 1976 !$#accession A00049 !'##molecule_type protein !'##residues 1-111 ##label BOU CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; methylated amino acid; mitochondrion; !1oxidative phosphorylation; respiratory chain FEATURE !$12-106 #domain cytochrome c homology #label CYC\ !$22,25 #binding_site heme (Cys) (covalent) #status !8predicted\ !$26,88 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted\ !$80,94 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8predicted SUMMARY #length 111 #molecular-weight 12049 #checksum 8563 SEQUENCE /// ENTRY CCCS #type complete TITLE cytochrome c [validated] - castor bean ORGANISM #formal_name Ricinus communis #common_name castor bean DATE 13-Jul-1981 #sequence_revision 13-Jul-1981 #text_change 28-Jul-2000 ACCESSIONS B00047; A00050 REFERENCE A00047 !$#authors Thompson, E.W.; Richardson, M.; Boulter, D. !$#journal Biochem. J. (1971) 121:439-446 !$#title The amino acid sequence of sesame (Sesamum indicum L.) and !1castor (Ricinus communis L.) cytochrome c. !$#cross-references MUID:72042446; PMID:5119781 !$#accession B00047 !'##molecule_type protein !'##residues 1-111 ##label THO REFERENCE A00056 !$#authors Brown, R.H.; Boulter, D. !$#journal Biochem. J. (1973) 131:247-251 !$#title The amino acid sequence of cytochrome c from Allium porrum !1L. (leek). !$#cross-references MUID:73229095; PMID:4352905 !$#contents annotation; variant CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; hydroxyproline; iron; metalloprotein; methylated amino !1acid; mitochondrion; oxidative phosphorylation; respiratory !1chain FEATURE !$12-106 #domain cytochrome c homology #label CYC\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$22,25 #binding_site heme (Cys) (covalent) #status !8experimental\ !$26,88 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted\ !$79 #modified_site 4-hydroxyproline (Pro) (partial) !8#status experimental\ !$80,94 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental SUMMARY #length 111 #molecular-weight 12024 #checksum 9565 SEQUENCE /// ENTRY CCCN #type complete TITLE cytochrome c [validated] - sea-island cotton ORGANISM #formal_name Gossypium barbadense #common_name sea-island cotton DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 28-Jul-2000 ACCESSIONS A00051 REFERENCE A90258 !$#authors Thompson, E.W.; Notton, B.A.; Richardson, M.; Boulter, D. !$#journal Biochem. J. (1971) 124:787-791 !$#title The amino acid sequence of cytochrome c from Abutilon !1theophrasti Medic. and Gossypium barbadense L. (cotton). !$#cross-references MUID:72074419; PMID:5131735 !$#accession A00051 !'##molecule_type protein !'##residues 1-111 ##label THO REFERENCE A00056 !$#authors Brown, R.H.; Boulter, D. !$#journal Biochem. J. (1973) 131:247-251 !$#title The amino acid sequence of cytochrome c from Allium porrum !1L. (leek). !$#cross-references MUID:73229095; PMID:4352905 !$#contents annotation; variant CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; hydroxyproline; iron; metalloprotein; methylated amino !1acid; mitochondrion; oxidative phosphorylation; respiratory !1chain FEATURE !$12-106 #domain cytochrome c homology #label CYC\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$22,25 #binding_site heme (Cys) (covalent) #status !8experimental\ !$26,88 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted\ !$79 #modified_site 4-hydroxyproline (Pro) (partial) !8#status experimental\ !$80,94 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental SUMMARY #length 111 #molecular-weight 12011 #checksum 301 SEQUENCE /// ENTRY CCAB #type complete TITLE cytochrome c [validated] - China jute ORGANISM #formal_name Abutilon theophrasti #common_name China jute DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 28-Jul-2000 ACCESSIONS A00052 REFERENCE A90258 !$#authors Thompson, E.W.; Notton, B.A.; Richardson, M.; Boulter, D. !$#journal Biochem. J. (1971) 124:787-791 !$#title The amino acid sequence of cytochrome c from Abutilon !1theophrasti Medic. and Gossypium barbadense L. (cotton). !$#cross-references MUID:72074419; PMID:5131735 !$#accession A00052 !'##molecule_type protein !'##residues 1-111 ##label THO REFERENCE A00056 !$#authors Brown, R.H.; Boulter, D. !$#journal Biochem. J. (1973) 131:247-251 !$#title The amino acid sequence of cytochrome c from Allium porrum !1L. (leek). !$#cross-references MUID:73229095; PMID:4352905 !$#contents annotation; variant CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; hydroxyproline; iron; metalloprotein; methylated amino !1acid; mitochondrion; oxidative phosphorylation; respiratory !1chain FEATURE !$12-106 #domain cytochrome c homology #label CYC\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$22,25 #binding_site heme (Cys) (covalent) #status !8experimental\ !$26,88 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted\ !$79 #modified_site 4-hydroxyproline (Pro) (partial) !8#status experimental\ !$80,94 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental SUMMARY #length 111 #molecular-weight 12037 #checksum 1083 SEQUENCE /// ENTRY CCTO #type complete TITLE cytochrome c [validated] - tomato ORGANISM #formal_name Lycopersicon esculentum #common_name tomato DATE 13-Jul-1981 #sequence_revision 31-Dec-1991 #text_change 28-Jul-2000 ACCESSIONS A00053; A11461 REFERENCE A00053 !$#authors Scogin, R.; Richardson, M.; Boulter, D. !$#journal Arch. Biochem. Biophys. (1972) 150:489-492 !$#title The amino acid sequence of cytochrome c from tomato !1(Lycopersicon esculentum Mill.). !$#cross-references MUID:72234831; PMID:5044037 !$#accession A00053 !'##molecule_type protein !'##residues 1-97,'Q',99-111 ##label SCO REFERENCE A11461 !$#authors Boulter, D.; Ramshaw, J.A.M.; Thompson, E.W.; Richardson, !1M.; Brown, R.H. !$#journal Proc. R. Soc. Lond. B Biol. Sci. (1972) 181:441-455 !$#title A phylogeny of higher plants based on the amino acid !1sequences of cytochrome c and its biological implications. !$#accession A11461 !'##molecule_type protein !'##residues 98 ##label BOU !'##note residue 98 in reference A00053 should have been shown as Glu CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; metalloprotein; methylated amino acid; !1mitochondrion; oxidative phosphorylation; respiratory chain FEATURE !$12-106 #domain cytochrome c homology #label CYC\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$22,25 #binding_site heme (Cys) (covalent) #status !8experimental\ !$26,88 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted\ !$80,94 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental SUMMARY #length 111 #molecular-weight 12023 #checksum 8073 SEQUENCE /// ENTRY CCPO #type complete TITLE cytochrome c - potato (tentative sequence) ORGANISM #formal_name Solanum tuberosum #common_name potato DATE 31-Dec-1990 #sequence_revision 31-Dec-1991 #text_change 03-Mar-2000 ACCESSIONS A04610; A00053 REFERENCE A04610 !$#authors Martinez, G.; Rochat, H.; Ducet, G. !$#journal FEBS Lett. (1974) 47:212-217 !$#title The amino acid sequence of cytochrome c from Solanum !1tuberosum (potato). !$#cross-references MUID:75039137; PMID:4372092 !$#accession A04610 !'##molecule_type protein !'##residues 1-111 ##label MAR !'##note 98-Asp was also found CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS blocked amino end; chromoprotein; electron transfer; heme; !1iron; metalloprotein; methylated amino acid; mitochondrion; !1oxidative phosphorylation; respiratory chain FEATURE !$12-106 #domain cytochrome c homology #label CYC\ !$1 #modified_site blocked amino end (Ala) (probably !8acetylated) #status experimental\ !$22,25 #binding_site heme (Cys) (covalent) #status !8predicted\ !$26,88 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted\ !$80,94 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8predicted SUMMARY #length 111 #molecular-weight 11982 #checksum 8083 SEQUENCE /// ENTRY CCED #type complete TITLE cytochrome c - European elder ORGANISM #formal_name Sambucus nigra #common_name European elder DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 03-Mar-2000 ACCESSIONS A00054 REFERENCE A00054 !$#authors Brown, R.H.; Boulter, D. !$#journal Biochem. J. (1974) 137:93-100 !$#title The amino acid sequences of cytochrome c from four plant !1sources. !$#cross-references MUID:74140224; PMID:4362498 !$#accession A00054 !'##molecule_type protein !'##residues 1-111 ##label BRO CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; metalloprotein; methylated amino acid; !1mitochondrion; oxidative phosphorylation; respiratory chain FEATURE !$12-106 #domain cytochrome c homology #label CYC\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$22,25 #binding_site heme (Cys) (covalent) #status !8predicted\ !$26,88 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted\ !$80,94 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental SUMMARY #length 111 #molecular-weight 12095 #checksum 169 SEQUENCE /// ENTRY CCBX #type complete TITLE cytochrome c - box elder ORGANISM #formal_name Acer negundo #common_name box elder DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 03-Mar-2000 ACCESSIONS A00055 REFERENCE A00054 !$#authors Brown, R.H.; Boulter, D. !$#journal Biochem. J. (1974) 137:93-100 !$#title The amino acid sequences of cytochrome c from four plant !1sources. !$#cross-references MUID:74140224; PMID:4362498 !$#accession A00055 !'##molecule_type protein !'##residues 1-112 ##label BRO !'##note 112-Ser was found in 50% of the molecules CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; metalloprotein; methylated amino acid; !1mitochondrion; oxidative phosphorylation; respiratory chain FEATURE !$12-106 #domain cytochrome c homology #label CYC\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$22,25 #binding_site heme (Cys) (covalent) #status !8predicted\ !$26,88 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted\ !$80,94 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental SUMMARY #length 112 #molecular-weight 12014 #checksum 3626 SEQUENCE /// ENTRY CCLK #type complete TITLE cytochrome c - leek (tentative sequence) ORGANISM #formal_name Allium porrum #common_name leek DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 31-Mar-2000 ACCESSIONS A00056 REFERENCE A00056 !$#authors Brown, R.H.; Boulter, D. !$#journal Biochem. J. (1973) 131:247-251 !$#title The amino acid sequence of cytochrome c from Allium porrum !1L. (leek). !$#cross-references MUID:73229095; PMID:4352905 !$#accession A00056 !'##molecule_type protein !'##residues 1-111 ##label BRO !'##note one residue of trimethyllysine is placed at position 80, rather !1than 81, by homology with wheat (see A92043) !'##note there are amides at two of the three positions 5, 10, and 11 !1and at one of the three positions 68, 69, and 70 CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; hydroxyproline; iron; metalloprotein; methylated amino !1acid; mitochondrion; oxidative phosphorylation; respiratory !1chain FEATURE !$12-106 #domain cytochrome c homology #label CYC\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$22,25 #binding_site heme (Cys) (covalent) #status !8experimental\ !$26,88 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted\ !$79 #modified_site 4-hydroxyproline (Pro) (partial) !8#status experimental\ !$80,94 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental SUMMARY #length 111 #molecular-weight 12080 #checksum 8945 SEQUENCE /// ENTRY CCRM #type complete TITLE cytochrome c - cuckoopint ORGANISM #formal_name Arum maculatum #common_name cuckoopint DATE 24-Apr-1984 #sequence_revision 17-Feb-1994 #text_change 03-Mar-2000 ACCESSIONS A00057 REFERENCE A00057 !$#authors Boulter, D. !$#citation unpublished results, cited by Dickerson, R.E., and !1Timkovich, R., in The Enzymes, 3rd ed., vol.11, part A, !1Boyer, P.D., ed., pp.397-547, Academic Press, New York, 1975 !$#accession A00057 !'##molecule_type protein !'##residues 1-111 ##label BOU CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; metalloprotein; methylated amino acid; !1mitochondrion; oxidative phosphorylation; respiratory chain FEATURE !$12-106 #domain cytochrome c homology #label CYC\ !$1 #modified_site acetylated amino end (Ala) #status !8predicted\ !$22,25 #binding_site heme (Cys) (covalent) #status !8predicted\ !$26,88 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted\ !$80,94 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8predicted SUMMARY #length 111 #molecular-weight 12039 #checksum 9387 SEQUENCE /// ENTRY CCND #type complete TITLE cytochrome c - love-in-a-mist (tentative sequence) ORGANISM #formal_name Nigella damascena #common_name love-in-a-mist DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 31-Mar-2000 ACCESSIONS A00058 REFERENCE A00058 !$#authors Brown, R.H.; Boulter, D. !$#journal Biochem. J. (1973) 133:251-254 !$#title The amino acid sequence of cytochrome c from Nigella !1damascena L. (love-in-a-mist). !$#cross-references MUID:73233117; PMID:4353234 !$#accession A00058 !'##molecule_type protein !'##residues 1-111 ##label BRO CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; metalloprotein; methylated amino acid; !1mitochondrion; oxidative phosphorylation; respiratory chain FEATURE !$12-106 #domain cytochrome c homology #label CYC\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$22,25 #binding_site heme (Cys) (covalent) #status !8experimental\ !$26,88 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted\ !$80,94 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8predicted SUMMARY #length 111 #molecular-weight 12052 #checksum 1362 SEQUENCE /// ENTRY CCNS #type complete TITLE cytochrome c - common nasturtium (tentative sequence) ORGANISM #formal_name Tropaeolum majus #common_name common nasturtium DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 31-Mar-2000 ACCESSIONS A00059 REFERENCE A00054 !$#authors Brown, R.H.; Boulter, D. !$#journal Biochem. J. (1974) 137:93-100 !$#title The amino acid sequences of cytochrome c from four plant !1sources. !$#cross-references MUID:74140224; PMID:4362498 !$#accession A00059 !'##molecule_type protein !'##residues 1-111 ##label BRO !'##note any one of the Lys residues shown may be an Arg, or an Arg may !1be missing from the sequence CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; metalloprotein; methylated amino acid; !1mitochondrion; oxidative phosphorylation; respiratory chain FEATURE !$12-106 #domain cytochrome c homology #label CYC\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$22,25 #binding_site heme (Cys) (covalent) #status !8predicted\ !$26,88 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted\ !$80,94 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental SUMMARY #length 111 #molecular-weight 11982 #checksum 9204 SEQUENCE /// ENTRY CCWT #type complete TITLE cytochrome c [validated] - wheat ORGANISM #formal_name Triticum aestivum #common_name common wheat DATE 23-Oct-1981 #sequence_revision 23-Oct-1981 #text_change 28-Jul-2000 ACCESSIONS A00060 REFERENCE A92030 !$#authors Stevens, F.C.; Glazer, A.N.; Smith, E.L. !$#journal J. Biol. Chem. (1967) 242:2764-2779 !$#title The amino acid sequence of wheat germ cytochrome c. !$#cross-references MUID:67169616; PMID:5298061 !$#accession A00060 !'##molecule_type protein !'##residues 1-112 ##label STE !'##note the tentative assignment of 24-Gln and 69-Glu is based on !1indirect evidence (electrophoretic mobilities and !1comparisons with other cytochromes c) REFERENCE A92043 !$#authors DeLange, R.J.; Glazer, A.N.; Smith, E.L. !$#journal J. Biol. Chem. (1969) 244:1385-1388 !$#title Presence and location of an unusual amino acid, !1epsilon-N-trimethyllysine, in cytochrome c of wheat germ and !1Neurospora. !$#cross-references MUID:69128197; PMID:4304194 !$#contents annotation; methylation CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; metalloprotein; methylated amino acid; !1mitochondrion; oxidative phosphorylation; respiratory chain FEATURE !$12-106 #domain cytochrome c homology #label CYC\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$22,25 #binding_site heme (Cys) (covalent) #status !8experimental\ !$26,88 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted\ !$80,94 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental SUMMARY #length 112 #molecular-weight 12048 #checksum 3493 SEQUENCE /// ENTRY CCNG #type complete TITLE cytochrome c - niger seed (tentative sequence) ORGANISM #formal_name Guizotia abyssinica #common_name niger seed DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 31-Mar-2000 ACCESSIONS A00061 REFERENCE A00061 !$#authors Ramshaw, J.A.M.; Boulter, D. !$#journal Phytochemistry (1975) 14:1945-1949 !$#title The amino acid sequence of cytochrome c from niger-seed, !1Guizotia abyssinica. !$#accession A00061 !'##molecule_type protein !'##residues 1-111 ##label RAM CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; metalloprotein; methylated amino acid; !1mitochondrion; oxidative phosphorylation; respiratory chain FEATURE !$12-106 #domain cytochrome c homology #label CYC\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$22,25 #binding_site heme (Cys) (covalent) #status !8predicted\ !$26,88 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted\ !$80,94 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental SUMMARY #length 111 #molecular-weight 11897 #checksum 1008 SEQUENCE /// ENTRY CCFS #type complete TITLE cytochrome c - common sunflower (tentative sequence) ORGANISM #formal_name Helianthus annuus #common_name common sunflower DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 31-Mar-2000 ACCESSIONS A00062 REFERENCE A00062 !$#authors Ramshaw, J.A.M.; Thompson, E.W.; Boulter, D. !$#journal Biochem. J. (1970) 119:535-539 !$#title The amino acid sequence of Helianthus annuus L. (sunflower) !1cytochrome c deduced from chymotryptic peptides. !$#cross-references MUID:71112252; PMID:5500313 !$#accession A00062 !'##molecule_type protein !'##residues 1-111 ##label RAM !'##note the authors placed the amides at positions 24, 70, and 97 by !1homology with other cytochromes c CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; metalloprotein; methylated amino acid; !1mitochondrion; oxidative phosphorylation; respiratory chain FEATURE !$12-106 #domain cytochrome c homology #label CYC\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$22,25 #binding_site heme (Cys) (covalent) #status !8experimental\ !$26,88 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted\ !$80,94 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental SUMMARY #length 111 #molecular-weight 11958 #checksum 162 SEQUENCE /// ENTRY CCPZ #type complete TITLE cytochrome c - parsnip ORGANISM #formal_name Pastinaca sativa #common_name parsnip DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 03-Mar-2000 ACCESSIONS A00063 REFERENCE A00054 !$#authors Brown, R.H.; Boulter, D. !$#journal Biochem. J. (1974) 137:93-100 !$#title The amino acid sequences of cytochrome c from four plant !1sources. !$#cross-references MUID:74140224; PMID:4362498 !$#accession A00063 !'##molecule_type protein !'##residues 1-111 ##label BRO CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; metalloprotein; methylated amino acid; !1mitochondrion; oxidative phosphorylation; respiratory chain FEATURE !$12-106 #domain cytochrome c homology #label CYC\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$22,25 #binding_site heme (Cys) (covalent) #status !8predicted\ !$26,88 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted\ !$80,94 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental SUMMARY #length 111 #molecular-weight 11929 #checksum 9196 SEQUENCE /// ENTRY CCFA #type complete TITLE cytochrome c - common buckwheat (tentative sequence) ORGANISM #formal_name Fagopyrum esculentum #common_name common buckwheat DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 31-Mar-2000 ACCESSIONS A00064 REFERENCE A04613 !$#authors Thompson, E.W.; Richardson, M.; Boulter, D. !$#journal Biochem. J. (1971) 124:783-785 !$#title The amino acid sequence of cytochrome c of Fagopyrum !1esculentum Moench (buckwheat) and Brassica oleracea L. !1(cauliflower). !$#cross-references MUID:72074418; PMID:5131734 !$#accession A00064 !'##molecule_type protein !'##residues 1-111 ##label THO !'##note the authors placed the amides at positions 10, 24, and 97 by !1homology with other cytochromes c; there is one amide at !1position 108 or 111 CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS blocked amino end; chromoprotein; electron transfer; heme; !1iron; metalloprotein; methylated amino acid; mitochondrion; !1oxidative phosphorylation; respiratory chain FEATURE !$12-106 #domain cytochrome c homology #label CYC\ !$1 #modified_site blocked amino end (Ala) (probably !8acetylated) #status experimental\ !$22,25 #binding_site heme (Cys) (covalent) #status !8predicted\ !$26,88 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted\ !$80,94 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental SUMMARY #length 111 #molecular-weight 12099 #checksum 746 SEQUENCE /// ENTRY CCSP #type complete TITLE cytochrome c [validated] - spinach ORGANISM #formal_name Spinacia oleracea #common_name spinach DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 28-Jul-2000 ACCESSIONS A00065 REFERENCE A00065 !$#authors Brown, R.H.; Richardson, M.; Scogin, R.; Boulter, D. !$#journal Biochem. J. (1973) 131:253-256 !$#title The amino acid sequence of cytochrome c from Spinacea !1oleracea L. (spinach). !$#cross-references MUID:73229096; PMID:4352906 !$#accession A00065 !'##molecule_type protein !'##residues 1-111 ##label BRO !'##experimental_source cv. Monster Viroflay CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; metalloprotein; methylated amino acid; !1mitochondrion; oxidative phosphorylation; respiratory chain FEATURE !$12-106 #domain cytochrome c homology #label CYC\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$22,25 #binding_site heme (Cys) (covalent) #status !8experimental\ !$26,88 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted\ !$80,94 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental SUMMARY #length 111 #molecular-weight 12054 #checksum 9939 SEQUENCE /// ENTRY CCGK #type complete TITLE cytochrome c - ginkgo (tentative sequence) ORGANISM #formal_name Ginkgo biloba #common_name ginkgo DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 31-Mar-2000 ACCESSIONS A00066 REFERENCE A00066 !$#authors Ramshaw, J.A.M.; Richardson, M.; Boulter, D. !$#journal Eur. J. Biochem. (1971) 23:475-483 !$#title The amino-acid sequence of the cytochrome c of Ginkgo biloba !1L. !$#cross-references MUID:72097686; PMID:5139215 !$#accession A00066 !'##molecule_type protein !'##residues 1-113 ##label RAM !'##note there is one amide at position 24 or 29, probably one at 69 or !170, and one at 97 or 98 CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; metalloprotein; methylated amino acid; !1mitochondrion; oxidative phosphorylation; respiratory chain FEATURE !$12-106 #domain cytochrome c homology #label CYC\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$22,25 #binding_site heme (Cys) (covalent) #status !8experimental\ !$26,88 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted\ !$80,94 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental SUMMARY #length 113 #molecular-weight 12362 #checksum 1420 SEQUENCE /// ENTRY CCEI #type complete TITLE cytochrome c - green alga (Enteromorpha intestinalis) (tentative sequence) ORGANISM #formal_name Enteromorpha intestinalis #common_name hollow green seaweed DATE 24-Apr-1984 #sequence_revision 30-Sep-1988 #text_change 31-Mar-2000 ACCESSIONS A00067 REFERENCE A00067 !$#authors Meatyard, B.T.; Boulter, D. !$#journal Phytochemistry (1974) 13:2777-2782 !$#title The amino acid sequence of cytochrome c from Enteromorpha !1intestinalis. !$#accession A00067 !'##molecule_type protein !'##residues 1-111 ##label MEA !'##note 69-Asx was also found !'##note the source may have been Enteromorpha intestinalis, E. linza, !1E. flexuosa, or a mixed culture of those species CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; metalloprotein; methylated amino acid; !1mitochondrion; oxidative phosphorylation; respiratory chain FEATURE !$12-106 #domain cytochrome c homology #label CYC\ !$1 #modified_site acetylated amino end (Ser) #status !8experimental\ !$22,25 #binding_site heme (Cys) (covalent) #status !8experimental\ !$26,88 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted\ !$80 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental\ !$94 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8absent SUMMARY #length 111 #molecular-weight 11709 #checksum 3982 SEQUENCE /// ENTRY S29514 #type complete TITLE cytochrome c - Chlamydomonas reinhardtii ORGANISM #formal_name Chlamydomonas reinhardtii DATE 13-Jan-1995 #sequence_revision 13-Jan-1995 #text_change 22-Mar-2002 ACCESSIONS S29514 REFERENCE S29514 !$#authors Amati, B.B.; Goldschmidt-Clermont, M.; Wallace, C.J.A.; !1Rochaix, J.D. !$#journal J. Mol. Evol. (1988) 28:151-160 !$#title cDNA and deduced amino acid sequences of cytochrome c from !1Chlamydomonas reinhardtii: unexpected functional and !1phylogenetic implications. !$#cross-references MUID:89178731; PMID:2853233 !$#accession S29514 !'##molecule_type mRNA !'##residues 1-112 ##label AMA !'##cross-references GB:M35173; EMBL:X13852; NID:g167412; !1PIDN:AAA33084.1; PID:g167413 CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS chromoprotein; heme; iron; metalloprotein; mitochondrion FEATURE !$13-107 #domain cytochrome c homology #label CYC\ !$23,26 #binding_site heme (Cys) (covalent) #status !8predicted\ !$27,89 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 112 #molecular-weight 11958 #checksum 8145 SEQUENCE /// ENTRY CCEG #type complete TITLE cytochrome c [validated] - Euglena gracilis ORGANISM #formal_name Euglena gracilis DATE 13-Jul-1981 #sequence_revision 13-Jul-1981 #text_change 28-Jul-2000 ACCESSIONS A00068 REFERENCE A00068 !$#authors Pettigrew, G.W.; Leaver, J.L.; Meyer, T.E.; Ryle, A.P. !$#journal Biochem. J. (1975) 147:291-302 !$#title Purification, properties and amino acid sequence of atypical !1cytochrome c from two protozoa, Euglena gracilis and !1Crithidia oncopelti. !$#cross-references MUID:76039443; PMID:170910 !$#accession A00068 !'##molecule_type protein !'##residues 1-102 ##label PET CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; metalloprotein; methylated amino acid; !1mitochondrion; oxidative phosphorylation; respiratory chain FEATURE !$4-97 #domain cytochrome c homology #label CYC\ !$1 #modified_site acetylated amino end (Gly) #status !8experimental\ !$17 #binding_site heme (Cys) (covalent) #status !8experimental\ !$18,79 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted\ !$85 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental SUMMARY #length 102 #molecular-weight 11210 #checksum 5226 SEQUENCE /// ENTRY CCCRCO #type complete TITLE cytochrome c [validated] - Crithidia oncopelti ORGANISM #formal_name Crithidia oncopelti DATE 13-Jul-1981 #sequence_revision 13-Jul-1981 #text_change 28-Jul-2000 ACCESSIONS A00069; A37571 REFERENCE A00068 !$#authors Pettigrew, G.W.; Leaver, J.L.; Meyer, T.E.; Ryle, A.P. !$#journal Biochem. J. (1975) 147:291-302 !$#title Purification, properties and amino acid sequence of atypical !1cytochrome c from two protozoa, Euglena gracilis and !1Crithidia oncopelti. !$#cross-references MUID:76039443; PMID:170910 !$#accession A00069 !'##molecule_type protein !'##residues 1-112 ##label PET REFERENCE A37571 !$#authors Smith, G.M.; Pettigrew, G.W. !$#journal Eur. J. Biochem. (1980) 110:123-130 !$#title Identification of N,N-dimethylproline as the N-terminal !1blocking group of Crithidia oncopelti cytochrome c557. !$#cross-references MUID:81066625; PMID:6254758 !$#accession A37571 !'##molecule_type protein !'##residues 1-5 ##label SMI CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; methylated amino acid; methylated amino end; !1mitochondrion; oxidative phosphorylation; respiratory chain FEATURE !$14-108 #domain cytochrome c homology #label CYC\ !$1 #modified_site dimethylated amino end (Pro) #status !8experimental\ !$3,82 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental\ !$27 #binding_site heme (Cys) (covalent) #status !8experimental\ !$28,90 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 112 #molecular-weight 11923 #checksum 9014 SEQUENCE /// ENTRY CCCRCF #type complete TITLE cytochrome c - Crithidia fasciculata (tentative sequence) ORGANISM #formal_name Crithidia fasciculata DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 31-Mar-2000 ACCESSIONS A00070 REFERENCE A91231 !$#authors Hill, G.C.; Pettigrew, G.W. !$#journal Eur. J. Biochem. (1975) 57:265-271 !$#title Evidence for the amino-acid sequence of Crithidia !1fasciculata cytochrome c555. !$#cross-references MUID:76022512; PMID:170111 !$#accession A00070 !'##molecule_type protein !'##residues 1-113 ##label HIL !'##note 64-Asp was also found REFERENCE A94573 !$#authors Pettigrew, G.W. !$#submission submitted to the Atlas, July 1977 !$#contents annotation CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS blocked amino end; chromoprotein; electron transfer; heme; !1iron; metalloprotein; methylated amino acid; mitochondrion; !1oxidative phosphorylation; respiratory chain FEATURE !$14-108 #domain cytochrome c homology #label CYC\ !$1 #modified_site blocked amino end (Pro) (probably !8dimethylated) #status experimental\ !$3,82 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental\ !$27 #binding_site heme (Cys) (covalent) #status !8predicted\ !$28,90 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 113 #molecular-weight 11987 #checksum 5473 SEQUENCE /// ENTRY CCTE #type complete TITLE cytochrome c [validated] - Tetrahymena pyriformis ORGANISM #formal_name Tetrahymena pyriformis DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 28-Jul-2000 ACCESSIONS A00071 REFERENCE A00071 !$#authors Tarr, G.E.; Fitch, W.M. !$#journal Biochem. J. (1976) 159:193-199 !$#title Amino acid sequence of cytochrome c from Tetrahymena !1pyriformis phenoset A. !$#cross-references MUID:77065147; PMID:187170 !$#accession A00071 !'##molecule_type protein !'##residues 1-109 ##label TAR !'##experimental_source strain GL-7 of Phenoset A GENETICS !$#genetic_code SGC5 CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1respiratory chain FEATURE !$15-106 #domain cytochrome c homology #label CYC\ !$25,28 #binding_site heme (Cys) (covalent) #status !8experimental\ !$29,88 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 109 #molecular-weight 11475 #checksum 6242 SEQUENCE /// ENTRY CCRF2G #type complete TITLE cytochrome c2 [validated] - Rhodopila globiformis ORGANISM #formal_name Rhodopila globiformis DATE 30-Nov-1979 #sequence_revision 30-Nov-1979 #text_change 28-Jul-2000 ACCESSIONS A32518; A00072 REFERENCE A32518 !$#authors Ambler, R.P.; Meyer, T.E.; Cusanovich, M.A.; Kamen, M.D. !$#journal Biochem. J. (1987) 246:115-120 !$#title The amino acid sequence of the cytochrome c2 from the !1phototrophic bacterium Rhodopseudomonas globiformis. !$#cross-references MUID:88049600; PMID:2823792 !$#accession A32518 !'##molecule_type protein !'##residues 1-106 ##label AMB COMMENT Cytochrome c2 is found mainly in purple, nonsulfur, !1photosynthetic bacteria where it functions as the electron !1donor to the oxidized bacteriochlorophyll in the !1photophosphorylation pathway. However, it may also have a !1role in the respiratory chain and is found in some !1nonphotosynthetic bacteria. CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; photosynthesis FEATURE !$9-102 #domain cytochrome c homology #label CYC\ !$19,22 #binding_site heme (Cys) (covalent) #status !8experimental\ !$23,84 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 106 #molecular-weight 11610 #checksum 162 SEQUENCE /// ENTRY CCAG2 #type complete TITLE cytochrome c2 - Agrobacterium tumefaciens (strain II Chrys) ORGANISM #formal_name Agrobacterium tumefaciens DATE 22-May-1981 #sequence_revision 08-Oct-1981 #text_change 03-Mar-2000 ACCESSIONS A00073 REFERENCE A94434 !$#authors Van Beeumen, J.; Tempst, P.; Stevens, P.; Bral, D.; Van !1Damme, J.; De Ley, J. !$#book Protides of the Biological Fluids, Proc. 28th Colloq., !1Peeters, H., ed., pp.69-74, Pergamon Press, Oxford, 1980 !$#title Cytochromes c of two different sequence classes in !1Agrobacterium tumefaciens. !$#accession A00073 !'##molecule_type protein !'##residues 1-111 ##label VAN CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS chromoprotein; electron transfer; heme; iron; metalloprotein FEATURE !$5-101 #domain cytochrome c homology #label CYC\ !$14,17 #binding_site heme (Cys) (covalent) #status !8predicted\ !$18,83 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 111 #molecular-weight 11648 #checksum 4889 SEQUENCE /// ENTRY JU0381 #type complete TITLE cytochrome c550 - Thiobacillus novellus ORGANISM #formal_name Thiobacillus novellus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS JU0381 REFERENCE JU0381 !$#authors Yamanaka, T.; Nagano, T.; Shouji, K.; Fukumori, Y. !$#journal Viva Origino (1991) 19:72-73 !$#title Cytochrome c of the sulphur oxidizing bacterium, !1Thiobacillus novellus: structure, function and evolution. !$#accession JU0381 !'##molecule_type protein !'##residues 1-109 ##label YAM CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS chromoprotein; electron transfer; heme; iron; metalloprotein FEATURE !$4-100 #domain cytochrome c homology #label CYC\ !$13,16 #binding_site heme (Cys) (covalent) #status !8predicted\ !$17,82 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 109 #molecular-weight 11813 #checksum 6384 SEQUENCE /// ENTRY B40638 #type complete TITLE isocytochrome c2 - Rhodobacter sphaeroides ORGANISM #formal_name Rhodobacter sphaeroides DATE 21-Sep-1993 #sequence_revision 27-Feb-1997 #text_change 03-Mar-2000 ACCESSIONS B40638 REFERENCE A40638 !$#authors Rott, M.A.; Witthuhn, V.C.; Schilke, B.A.; Soranno, M.; Ali, !1A.; Donohue, T.J. !$#journal J. Bacteriol. (1993) 175:358-366 !$#title Genetic evidence for the role of isocytochrome c2 in !1photosynthetic growth of Rhodobacter sphaeroides Spd !1mutants. !$#cross-references MUID:93123153; PMID:8380401 !$#accession B40638 !'##molecule_type DNA !'##residues 1-144 ##label ROT !'##cross-references GB:L02104; NID:g151899; PIDN:AAA61341.1; !1PID:g151901 !'##note sequence extracted from NCBI backbone (NCBIN:122345, !1NCBIP:122347) COMMENT This protein can substitute for cytochrome c2 in !1c2-deficient mutants. GENETICS !$#gene cycI CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; photosynthesis FEATURE !$26-122 #domain cytochrome c homology #label CYC\ !$35,38 #binding_site heme (Cys) (covalent) #status !8predicted\ !$39,104 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 144 #molecular-weight 14874 #checksum 8522 SEQUENCE /// ENTRY CCRD2 #type complete TITLE cytochrome c2 - Rhodomicrobium vannielii ORGANISM #formal_name Rhodomicrobium vannielii DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 03-Mar-2000 ACCESSIONS A00074 REFERENCE A93806 !$#authors Ambler, R.P.; Meyer, T.E.; Kamen, M.D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1976) 73:472-475 !$#title Primary structure determination of two cytochromes c-2: !1close similarity to functionally unrelated mitochondrial !1cytochrome c. !$#cross-references MUID:76102814; PMID:174109 !$#accession A00074 !'##molecule_type protein !'##residues 1-104 ##label AMB CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; photosynthesis FEATURE !$5-98 #domain cytochrome c homology #label CYC\ !$14,17 #binding_site heme (Cys) (covalent) #status !8predicted\ !$18,80 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 104 #molecular-weight 11209 #checksum 1003 SEQUENCE /// ENTRY CCRF2V #type complete TITLE cytochrome c2 precursor - Rhodopseudomonas viridis ORGANISM #formal_name Rhodopseudomonas viridis DATE 24-Apr-1984 #sequence_revision 30-Sep-1991 #text_change 03-Mar-2000 ACCESSIONS A36720; A93806; A00075 REFERENCE A36720 !$#authors Grisshammer, R.; Wiessner, C.; Michel, H. !$#journal J. Bacteriol. (1990) 172:5071-5078 !$#title Sequence analysis and transcriptional organization of the !1Rhodopseudomonas viridis cytochrome c-2 gene. !$#cross-references MUID:90368560; PMID:1697576 !$#accession A36720 !'##molecule_type DNA !'##residues 1-127 ##label GRI !'##cross-references GB:M59302; NID:g151874; PIDN:AAA26092.1; !1PID:g151875 REFERENCE A93806 !$#authors Ambler, R.P.; Meyer, T.E.; Kamen, M.D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1976) 73:472-475 !$#title Primary structure determination of two cytochromes c-2: !1close similarity to functionally unrelated mitochondrial !1cytochrome c. !$#cross-references MUID:76102814; PMID:174109 !$#accession A93806 !'##molecule_type protein !'##residues 21-33,'K',35-65,'S',67-103,'I',105-116,'L',118-127 ##label !1AMB REFERENCE A94582 !$#authors Ambler, R.P. !$#submission submitted to the Atlas, June 1977 !$#contents annotation !$#note residue 34 is Leu GENETICS !$#gene cycA CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS blocked amino end; chromoprotein; electron transfer; heme; !1iron; metalloprotein; photosynthesis FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-127 #product cytochrome c2 #status experimental #label !8MAT\ !$24-117 #domain cytochrome c homology #label CYC\ !$21 #modified_site blocked amino end (Gln) (in mature !8form) (probably pyrrolidone carboxylic acid) #status !8experimental\ !$33,36 #binding_site heme (Cys) (covalent) #status !8predicted\ !$37,99 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 127 #molecular-weight 13665 #checksum 5641 SEQUENCE /// ENTRY CCRF2A #type complete TITLE cytochrome c2 - Rhodopseudomonas acidophila ORGANISM #formal_name Rhodopseudomonas acidophila DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 03-Mar-2000 ACCESSIONS A00076 REFERENCE A94458 !$#authors Ambler, R.P.; Meyer, T.E.; Bartsch, R.G.; Kamen, M.D. !$#citation unpublished results, cited by Ambler, R.P., in Evolution of !1Protein Molecules, Matsubara, H., and Yamanaka, T., eds., !1pp.311-322, Japan Scientific Societies Press/Center for !1Academic Publications Japan, Tokyo, 1978 !$#accession A00076 !'##molecule_type protein !'##residues 1-107 ##label AMB CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; photosynthesis FEATURE !$5-98 #domain cytochrome c homology #label CYC\ !$14,17 #binding_site heme (Cys) (covalent) #status !8predicted\ !$18,80 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 107 #molecular-weight 11305 #checksum 9206 SEQUENCE /// ENTRY CCNA5A #type complete TITLE cytochrome c550 - Nitrobacter winogradskyi ORGANISM #formal_name Nitrobacter winogradskyi DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 03-Mar-2000 ACCESSIONS A00077 REFERENCE A00077 !$#authors Tanaka, Y.; Fukumori, Y.; Yamanaka, T. !$#journal Biochim. Biophys. Acta (1982) 707:14-20 !$#title The complete amino acid sequence of Nitrobacter agilis !1cytochrome c-550. !$#cross-references MUID:83049097; PMID:6291614 !$#accession A00077 !'##molecule_type protein !'##residues 1-109 ##label TAN CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS chromoprotein; electron transfer; heme; iron; metalloprotein FEATURE !$4-97 #domain cytochrome c homology #label CYC\ !$13,16 #binding_site heme (Cys) (covalent) #status !8predicted\ !$17,79 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 109 #molecular-weight 11739 #checksum 7228 SEQUENCE /// ENTRY S00034 #type complete TITLE cytochrome c550 - Aquaspirillum itersonii ORGANISM #formal_name Aquaspirillum itersonii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS S00034 REFERENCE S00034 !$#authors Woolley, K.J. !$#journal Eur. J. Biochem. (1987) 166:131-137 !$#title The soluble c-type cytochromes from the bacterium !1Aquaspirillum itersonii: the complete amino acid sequence of !1the cytochrome c-550. !$#cross-references MUID:87246667; PMID:3036517 !$#accession S00034 !'##molecule_type protein !'##residues 1-111 ##label WOO CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS chromoprotein; electron transfer; heme; iron; metalloprotein FEATURE !$4-107 #domain cytochrome c homology #label CYC\ !$13,16 #binding_site heme (Cys) (covalent) #status !8predicted\ !$17,90 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 111 #molecular-weight 11595 #checksum 3840 SEQUENCE /// ENTRY CCQF2F #type complete TITLE cytochrome c2, iso-1 - Rhodospirillum fulvum ORGANISM #formal_name Rhodospirillum fulvum DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 03-Mar-2000 ACCESSIONS A00078 REFERENCE A94458 !$#authors Ambler, R.P.; Meyer, T.E.; Bartsch, R.G.; Kamen, M.D. !$#citation unpublished results, cited by Ambler, R.P., in Evolution of !1Protein Molecules, Matsubara, H., and Yamanaka, T., eds., !1pp.311-322, Japan Scientific Societies Press/Center for !1Academic Publications Japan, Tokyo, 1978 !$#accession A00078 !'##molecule_type protein !'##residues 1-99 ##label AMB CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; photosynthesis FEATURE !$1-95 #domain cytochrome c homology #label CYC\ !$10,13 #binding_site heme (Cys) (covalent) #status !8predicted\ !$14,75 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 99 #molecular-weight 10288 #checksum 2566 SEQUENCE /// ENTRY CCQF2M #type complete TITLE cytochrome c2, iso-1 - Rhodospirillum molischianum ORGANISM #formal_name Rhodospirillum molischianum DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 03-Mar-2000 ACCESSIONS A00079 REFERENCE A94458 !$#authors Ambler, R.P.; Meyer, T.E.; Bartsch, R.G.; Kamen, M.D. !$#citation unpublished results, cited by Ambler, R.P., in Evolution of !1Protein Molecules, Matsubara, H., and Yamanaka, T., eds., !1pp.311-322, Japan Scientific Societies Press/Center for !1Academic Publications Japan, Tokyo, 1978 !$#accession A00079 !'##molecule_type protein !'##residues 1-100 ##label AMB CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; photosynthesis FEATURE !$1-96 #domain cytochrome c homology #label CYC\ !$11,14 #binding_site heme (Cys) (covalent) #status !8predicted\ !$15,76 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 100 #molecular-weight 10248 #checksum 6135 SEQUENCE /// ENTRY CCQFM2 #type complete TITLE cytochrome c2, iso-2 - Rhodospirillum molischianum ORGANISM #formal_name Rhodospirillum molischianum DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 03-Mar-2000 ACCESSIONS A00080 REFERENCE A94458 !$#authors Ambler, R.P.; Meyer, T.E.; Bartsch, R.G.; Kamen, M.D. !$#citation unpublished results, cited by Ambler, R.P., in Evolution of !1Protein Molecules, Matsubara, H., and Yamanaka, T., eds., !1pp.311-322, Japan Scientific Societies Press/Center for !1Academic Publications Japan, Tokyo, 1978 !$#accession A00080 !'##molecule_type protein !'##residues 1-97 ##label AMB CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; photosynthesis FEATURE !$1-93 #domain cytochrome c homology #label CYC\ !$10,13 #binding_site heme (Cys) (covalent) #status !8predicted\ !$14,75 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 97 #molecular-weight 10222 #checksum 7414 SEQUENCE /// ENTRY CCQFF2 #type complete TITLE cytochrome c2, iso-2 - Rhodospirillum fulvum (tentative sequence) ORGANISM #formal_name Rhodospirillum fulvum DATE 31-May-1979 #sequence_revision 08-Oct-1981 #text_change 31-Mar-2000 ACCESSIONS A00081 REFERENCE A00086 !$#authors Ambler, R.P.; Daniel, M.; Hermoso, J.; Meyer, T.E.; Bartsch, !1R.G.; Kamen, M.D. !$#journal Nature (1979) 278:659-660 !$#title Cytochrome c-2 sequence variation among the recognised !1species of purple nonsulphur photosynthetic bacteria. !$#cross-references MUID:79199667; PMID:221822 !$#accession A00081 !'##molecule_type protein !'##residues 1-96 ##label AMB !'##note 62-Phe is found in about 30% of the molecules CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; photosynthesis FEATURE !$1-93 #domain cytochrome c homology #label CYC\ !$10,13 #binding_site heme (Cys) (covalent) #status !8predicted\ !$14,75 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 96 #molecular-weight 9832 #checksum 2688 SEQUENCE /// ENTRY CCRF2P #type complete TITLE cytochrome c2 - Rhodopseudomonas palustris (strain 2.1.6) ORGANISM #formal_name Rhodopseudomonas palustris DATE 22-May-1981 #sequence_revision 22-May-1981 #text_change 17-Nov-2000 ACCESSIONS B00086; B00089; A00082 REFERENCE A00086 !$#authors Ambler, R.P.; Daniel, M.; Hermoso, J.; Meyer, T.E.; Bartsch, !1R.G.; Kamen, M.D. !$#journal Nature (1979) 278:659-660 !$#title Cytochrome c-2 sequence variation among the recognised !1species of purple nonsulphur photosynthetic bacteria. !$#cross-references MUID:79199667; PMID:221822 !$#accession B00086 !'##molecule_type protein !'##residues 1-114 ##label AMB !'##experimental_source ATCC 17001 REFERENCE A00089 !$#authors Ambler, R.P.; Meyer, T.E.; Murray, S. !$#submission submitted to the Atlas, July 1974 !$#accession B00089 !'##molecule_type protein !'##residues 1-114 ##label AM2 !'##note amino-terminal blocking group CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; photosynthesis; pyroglutamic acid FEATURE !$4-110 #domain cytochrome c homology #label CYC\ !$1 #modified_site pyrrolidone carboxylic acid (Gln) !8#status experimental\ !$13,16 #binding_site heme (Cys) (covalent) #status !8predicted\ !$17,93 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 114 #molecular-weight 12208 #checksum 9230 SEQUENCE /// ENTRY CCRF7P #type complete TITLE cytochrome c2 - Rhodopseudomonas palustris (strain 2.1.37) ORGANISM #formal_name Rhodopseudomonas palustris DATE 22-May-1981 #sequence_revision 22-May-1981 #text_change 03-Mar-2000 ACCESSIONS A00083 REFERENCE A00086 !$#authors Ambler, R.P.; Daniel, M.; Hermoso, J.; Meyer, T.E.; Bartsch, !1R.G.; Kamen, M.D. !$#journal Nature (1979) 278:659-660 !$#title Cytochrome c-2 sequence variation among the recognised !1species of purple nonsulphur photosynthetic bacteria. !$#cross-references MUID:79199667; PMID:221822 !$#accession A00083 !'##molecule_type protein !'##residues 1-114 ##label AMB !'##experimental_source ATCC 17007 CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; photosynthesis; pyroglutamic acid FEATURE !$4-110 #domain cytochrome c homology #label CYC\ !$1 #modified_site pyrrolidone carboxylic acid (Gln) !8#status experimental\ !$13,16 #binding_site heme (Cys) (covalent) #status !8predicted\ !$17,93 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 114 #molecular-weight 12233 #checksum 218 SEQUENCE /// ENTRY CCQF2R #type complete TITLE cytochrome c2 precursor [validated] - Rhodospirillum rubrum ORGANISM #formal_name Rhodospirillum rubrum DATE 24-Apr-1984 #sequence_revision 30-Sep-1991 #text_change 28-Jul-2000 ACCESSIONS S08213; A00084 REFERENCE S08213 !$#authors Self, S.J.; Hunter, C.N.; Leatherbarrow, R.J. !$#journal Biochem. J. (1990) 265:599-604 !$#title Molecular cloning, sequencing and expression of cytochrome c !1(2) from Rhodospirillum rubrum. !$#cross-references MUID:90147629; PMID:2154194 !$#accession S08213 !'##molecule_type DNA !'##residues 1-135 ##label SEL !'##cross-references EMBL:X17605; NID:g46378; PIDN:CAA35607.1; !1PID:g46379 REFERENCE A92038 !$#authors Dus, K.; Sletten, K.; Kamen, M.D. !$#journal J. Biol. Chem. (1968) 243:5507-5518 !$#title Cytochrome c-2 of Rhodospirillum rubrum. II. Complete amino !1acid sequence and phylogenetic relationships. !$#cross-references MUID:69080147; PMID:4883098 !$#accession A00084 !'##molecule_type protein !'##residues 24-67,'N',69-95,'N',97-135 ##label DUS REFERENCE A50409 !$#authors Bhatia, G.; Finzel, B.C.; Kraut, J. !$#submission submitted to the Brookhaven Protein Data Bank, November 1983 !$#cross-references PDB:2C2C !$#contents annotation; X-ray crystallography, 2.0 angstroms, oxidized !1form, residues 24-67,'N',69-95,'N',97-135 REFERENCE A50572 !$#authors Bhatia, G.; Finzel, B.C.; Kraut, J. !$#submission submitted to the Brookhaven Protein Data Bank, November 1983 !$#cross-references PDB:3C2C !$#contents annotation; X-ray crystallography, 1.68 angstroms, reduced !1form, residues 24-67,'N',69-95,'N',97-135 REFERENCE A92135 !$#authors Salemme, F.R.; Freer, S.T.; Xuong, N.H.; Alden, R.A.; Kraut, !1J. !$#journal J. Biol. Chem. (1973) 248:3910-3921 !$#title The structure of oxidized cytochrome c-2 of Rhodospirillum !1rubrum. !$#cross-references MUID:73187380; PMID:4350650 !$#contents annotation; X-ray crystallography, 2.0 angstroms REFERENCE A90186 !$#authors Salemme, F.R.; Freer, S.T.; Alden, R.A.; Kraut, J. !$#journal Biochem. Biophys. Res. Commun. (1973) 54:47-52 !$#title Atomic coordinates for ferricytochrome c-2 of Rhodospirillum !1rubrum. !$#cross-references MUID:74003179; PMID:4200400 !$#contents annotation; X-ray crystallographic coordinates COMMENT A mobile electron carrier in the cyclic photosynthetic !1electron transport system, cytochrome c2 accepts electrons !1from the cytochrome bc1 complex and turns them over to !1photochemically oxidized reaction center. GENETICS !$#gene cycA CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; photosynthesis FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-135 #product cytochrome c2 #status experimental #label !8MAT\ !$28-131 #domain cytochrome c homology #label CYC\ !$37,40 #binding_site heme (Cys) (covalent) #status !8experimental\ !$41,114 #binding_site heme iron (His, Met) (axial ligands) !8#status experimental SUMMARY #length 135 #molecular-weight 14395 #checksum 2556 SEQUENCE /// ENTRY CCQF2P #type complete TITLE cytochrome c2 - Rhodospirillum photometricum (tentative sequence) ORGANISM #formal_name Rhodospirillum photometricum DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 31-Mar-2000 ACCESSIONS A00085 REFERENCE A94459 !$#authors Hermoso, J.; Pettigrew, G.W.; Kamen, M.D. !$#citation unpublished results, cited by Ambler, R.P., in Evolution of !1Protein Molecules, Matsubara, H., and Yamanaka, T., eds., !1pp.311-322, Japan Scientific Societies Press/Center for !1Academic Publications Japan, Tokyo, 1978 !$#accession A00085 !'##molecule_type protein !'##residues 1-113 ##label HER CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; photosynthesis FEATURE !$5-109 #domain cytochrome c homology #label CYC\ !$15,18 #binding_site heme (Cys) (covalent) #status !8predicted\ !$19,92 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 113 #molecular-weight 12069 #checksum 8048 SEQUENCE /// ENTRY CCRF2C #type complete TITLE cytochrome c2 precursor - Rhodobacter capsulatus ORGANISM #formal_name Rhodobacter capsulatus DATE 24-Apr-1984 #sequence_revision 30-Sep-1991 #text_change 03-Mar-2000 ACCESSIONS A25452; A00086 REFERENCE A25452 !$#authors Daldal, F.; Cheng, S.; Applebaum, J.; Davidson, E.; Prince, !1R.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:2012-2016 !$#title Cytochrome c2 is not essential for photosynthetic growth of !1Rhodopseudomonas capsulata. !$#accession A25452 !'##molecule_type DNA !'##residues 1-137 ##label DAL !'##experimental_source strain SB1003 REFERENCE A00086 !$#authors Ambler, R.P.; Daniel, M.; Hermoso, J.; Meyer, T.E.; Bartsch, !1R.G.; Kamen, M.D. !$#journal Nature (1979) 278:659-660 !$#title Cytochrome c-2 sequence variation among the recognised !1species of purple nonsulphur photosynthetic bacteria. !$#cross-references MUID:79199667; PMID:221822 !$#accession A00086 !'##molecule_type protein !'##residues 22-137 ##label AMB !'##experimental_source strain St. Louis, ATCC 23782, and strain 2.3.1, !1ATCC 11166 !'##note the sequence from strain 2.3.1 differs from that shown in !1having 108-Thr and 115-Ser GENETICS !$#gene cycA CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; photosynthesis FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-137 #product cytochrome c2 #status experimental #label !8MAT\ !$25-132 #domain cytochrome c homology #label CYC\ !$34,37 #binding_site heme (Cys) (covalent) #status !8predicted\ !$38,117 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 137 #molecular-weight 14279 #checksum 4855 SEQUENCE /// ENTRY CCBC5E #type complete TITLE cytochrome c551 - Erythrobacter sp. ORGANISM #formal_name Erythrobacter sp. DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 03-Mar-2000 ACCESSIONS JT0008 REFERENCE JT0008 !$#authors Okamura, K.; Miyata, T.; Iwanaga, S.; Takamiya, K.I.; !1Nishimura, M. !$#journal J. Biochem. (1987) 101:957-963 !$#title Complete amino acid sequence of cytochrome c551 from !1Erythrobacter species strain OCh 114. !$#cross-references MUID:87279991; PMID:3038859 !$#accession JT0008 !'##molecule_type protein !'##residues 1-119 ##label OKA !'##experimental_source strain OCh 114 CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; oxidative phosphorylation FEATURE !$5-111 #domain cytochrome c homology #label CYC\ !$14,17 #binding_site heme (Cys) (covalent) #status !8predicted\ !$18,96 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 119 #molecular-weight 12619 #checksum 9710 SEQUENCE /// ENTRY CCRF2S #type complete TITLE cytochrome c2 precursor [validated] - Rhodobacter sphaeroides ORGANISM #formal_name Rhodobacter sphaeroides DATE 24-Apr-1984 #sequence_revision 30-Sep-1991 #text_change 17-Nov-2000 ACCESSIONS A38896; A42458; A25160; A00087; JC4794; T50720 REFERENCE A38896 !$#authors MacGregor, B.J.; Donohue, T.J. !$#submission submitted to GenBank, July 1991 !$#description Evidence for two promoters for the cytochrome c-2 gene !1(cycA) of Rhodobacter sphaeroides. !$#accession A38896 !'##molecule_type DNA !'##residues 1-145 ##label MAC !'##cross-references GB:M64777; NID:g151891; PIDN:AAA26099.1; !1PID:g151892 REFERENCE A42458 !$#authors MacGregor, B.J.; Donohue, T.J. !$#journal J. Bacteriol. (1991) 173:3949-3957 !$#title Evidence for two promoters for the cytochrome c-2 gene !1(cycA) of Rhodobacter sphaeroides. !$#cross-references MUID:91286176; PMID:1648072 !$#accession A42458 !'##molecule_type DNA !'##residues 1-61;82-145 ##label MA2 !'##cross-references GB:M64777 !'##note the sequence of residues 62-81 was omitted in reference A42458 REFERENCE A25160 !$#authors Donohue, T.J.; McEwan, A.G.; Kaplan, S. !$#journal J. Bacteriol. (1986) 168:962-972 !$#title Cloning, DNA sequence, and expression of the Rhodobacter !1sphaeroides cytochrome c2 gene. !$#cross-references MUID:87056995; PMID:3023293 !$#accession A25160 !'##molecule_type DNA !'##residues 1-145 ##label DON !'##cross-references GB:M14501; NID:g151895; PIDN:AAA26101.1; !1PID:g151896 REFERENCE A00087 !$#authors Ambler, R.P.; Meyer, T.E. !$#submission submitted to the Atlas, July 1974 !$#accession A00087 !'##molecule_type protein !'##residues 22-145 ##label AMB !'##note the source is designated as Rhodopseudomonas sphaeroides, !1strain 2.4.1 REFERENCE JC4794 !$#authors Gans, P.; Simorre, J.P.; Caffrey, M.; Marion, D.; Richaud, !1P.; Vermeglio, A. !$#journal J. Biochem. (1996) 119:1131-1142 !$#title Sequential 1H and 15N NMR resonance assignment and secondary !1structure of ferrocytochrome c2 from Rhodobacter !1sphaeroides. !$#cross-references MUID:96424998; PMID:8827449 !$#contents sequence; conformation by (1)H- and (15)N-NMR, residues !122-145 !$#accession JC4794 !'##molecule_type protein !'##residues 22-145 ##label GAN REFERENCE A67911 !$#authors Axelrod, H.L.; Feher, G.; Allen, J.P.; Chirino, A.J.; Day, !1M.W.; Hsu, B.T.; Rees, D.C. !$#submission submitted to the Brookhaven Protein Data Bank, April 1994 !$#cross-references PDB:2CXB !$#contents annotation; X-ray crystallography, 1.95 angstroms, residues !123-145 REFERENCE A65366 !$#authors Axelrod, H.L.; Feher, G.; Allen, J.P.; Chirino, A.J.; Day, !1M.W.; Hsu, B.T.; Rees, D.C. !$#submission submitted to the Brookhaven Protein Data Bank, February 1994 !$#cross-references PDB:1CXC !$#contents annotation; X-ray crystallography, 1.6 angstroms, residues !122-145 REFERENCE Z25222 !$#authors Choudhary, M.; Kaplan, S. !$#journal Nucleic Acids Res. (2000) 28:862-867 !$#title DNA sequence analysis of the photosynthesis region of !1Rhodobacter sphaeroides 2.4.1. !$#cross-references MUID:20115911; PMID:10648776 !$#accession T50720 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-145 ##label CHO !'##cross-references EMBL:AF195122; PIDN:AAF24264.1 !'##experimental_source strain 2.4.1 GENETICS !$#gene cycA CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; photosynthesis; pyroglutamic acid FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-145 #product cytochrome c2 #status experimental #label !8MAT\ !$27-138 #domain cytochrome c homology #label CYC\ !$22 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$36,39 #binding_site heme (Cys) (covalent) #status !8experimental\ !$40,121 #binding_site heme iron (His, Met) (axial ligands) !8#status experimental SUMMARY #length 145 #molecular-weight 15568 #checksum 5080 SEQUENCE /// ENTRY CCPC50 #type complete TITLE cytochrome c2 precursor [validated] - Paracoccus denitrificans ALTERNATE_NAMES cytochrome c550 ORGANISM #formal_name Paracoccus denitrificans DATE 24-Apr-1984 #sequence_revision 20-Aug-1994 #text_change 28-Jul-2000 ACCESSIONS S08269; A35409; B35121; A00088 REFERENCE S08269 !$#authors Raitio, M.; Pispa, J.M.; Metso, T.; Saraste, M. !$#journal FEBS Lett. (1990) 261:431-435 !$#title Are there isoenzymes of cytochrome c oxidase in Paracoccus !1denitrificans? !$#cross-references MUID:90184495; PMID:2155830 !$#accession S08269 !'##molecule_type DNA !'##residues 1-155 ##label RAI !'##cross-references EMBL:Y07533; NID:g45477; PIDN:CAA68820.1; !1PID:g45478 REFERENCE A35409 !$#authors Van Spanning, R.J.M.; Wansell, C.; Harms, N.; Oltmann, L.F.; !1Stouthamer, A.H. !$#journal J. Bacteriol. (1990) 172:3534 !$#cross-references MUID:90264363; PMID:2160949 !$#contents erratum !$#accession A35409 !'##molecule_type DNA !'##residues 1-155 ##label VAN !'##cross-references GB:M27304; NID:g150573; PIDN:AAA88364.1; !1PID:g150574 !'##note this is a revision to the sequence from reference A35121 REFERENCE A35121 !$#authors Van Spanning, R.J.M.; Wansell, C.; Harms, N.; Oltmann, L.F.; !1Stouthamer, A.H. !$#journal J. Bacteriol. (1990) 172:986-996 !$#title Mutagenesis of the gene encoding cytochrome c-550 of !1Paracoccus denitrificans and analysis of the resultant !1physiological effects. !$#cross-references MUID:90130336; PMID:2153663 !$#accession B35121 !'##molecule_type DNA !'##residues 1-51,'SEEGFKYGEGIL',52-68,81-155 ##label VA2 !'##cross-references GB:M27304 !'##note this sequence has been revised in reference A35409 REFERENCE A94565 !$#authors Ambler, R.P. !$#submission submitted to the Atlas, February 1981 !$#accession A00088 !'##molecule_type protein !'##residues 21-149 ##label AMB !'##experimental_source ATCC 13543 REFERENCE A52549 !$#authors Benning, M.M.; Meyer, T.E.; Holden, H.M. !$#submission submitted to the Brookhaven Protein Data Bank, July 1994 !$#cross-references PDB:1COT !$#contents annotation; X-ray crystallography, 1.7 angstroms, residues !122-142 REFERENCE A58602 !$#authors Benning, M.M.; Meyer, T.E.; Holden, H.M. !$#journal Arch. Biochem. Biophys. (1994) 310:460-466 !$#title X-ray structure of the cytochrome C-2 isolated from !1Paracoccus denitrificans refined to 1.7-angstroms !1resolution. !$#cross-references MUID:94234725; PMID:8179333 !$#contents annotation; X-ray crystallography, 1.7 angstroms REFERENCE A92865 !$#authors Ambler, R.P.; Meyer, T.E.; Kamen, M.D.; Schichman, S.A.; !1Sawyer, L. !$#journal J. Mol. Biol. (1981) 147:351-356 !$#title A reassessment of the structure of Paracoccus cytochrome !1c-550. !$#cross-references MUID:82033207; PMID:6270339 !$#contents annotation !$#note 50% of the molecules lack the carboxyl-terminal Ala; !1confirmation of the sequence altered some interpretations of !1the crystallographic structure REFERENCE A92193 !$#authors Timkovich, R.; Dickerson, R.E. !$#journal J. Biol. Chem. (1976) 251:4033-4046 !$#title The structure of Paracoccus denitrificans cytochrome c550. !$#cross-references MUID:76213273; PMID:180013 !$#contents annotation; X-ray crystallography, 2.45 angstroms GENETICS !$#gene cycA CLASSIFICATION #superfamily cytochrome c; cytochrome c homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; oxidative phosphorylation; pyroglutamic acid FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-155 #product cytochrome c550 #status experimental #label !8MAT\ !$26-135 #domain cytochrome c homology #label CYC\ !$21 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$35,38 #binding_site heme (Cys) (covalent) #status !8experimental\ !$39,120 #binding_site heme iron (His, Met) (axial ligands) !8#status experimental SUMMARY #length 155 #molecular-weight 16397 #checksum 9000 SEQUENCE /// ENTRY CCTW5T #type complete TITLE cytochrome c552 [validated] - Thermus aquaticus ORGANISM #formal_name Thermus aquaticus DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 17-Nov-2000 ACCESSIONS A00112 REFERENCE A00112 !$#authors Titani, K.; Ericsson, L.H.; Hon-nami, K.; Miyazawa, T. !$#journal Biochem. Biophys. Res. Commun. (1985) 128:781-787 !$#title Amino acid sequence of cytochrome c-552 from Thermus !1thermophilus HB8. !$#cross-references MUID:85199131; PMID:2986626 !$#accession A00112 !'##molecule_type protein !'##residues 1-131 ##label TIT !'##note the source was designated as Thermus thermophilus REFERENCE A77356 !$#authors Than, M.E.; Hof, P.; Huber, R.; Bourenkov, G.P.; Bartunik, !1H.D.; Buse, G.; Soulimane, T. !$#submission submitted to the Protein Data Bank, June 1997 !$#cross-references PDB:1C52 !$#contents annotation; X-ray crystallography, 1.28 angstroms, residues !11-131 REFERENCE A59160 !$#authors Than, M.E.; Hof, P.; Huber, R.; Bourenkov, G.P.; Bartunik, !1H.D.; Buse, G.; Soulimane, T. !$#journal J. Mol. Biol. (1997) 271:629-644 !$#title Thermus thermophilus cytochrome-c552: a new highly !1thermostable cytochrome-c structure obtained by MAD phasing. !$#cross-references MUID:97428333; PMID:9281430 !$#contents annotation; X-ray crystallography, 1.28 angstroms COMMENT This cytochrome appears to function as an electron donor to !1cytochrome oxidase; it may be a c2-type cytochrome but is !1distantly related to other cytochromes. CLASSIFICATION #superfamily T. aquaticus cytochrome c552; cytochrome c6 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; pyroglutamic acid FEATURE !$2-87 #domain cytochrome c6 homology #label CY6\ !$1 #modified_site pyrrolidone carboxylic acid (Gln) !8#status experimental\ !$11,14 #binding_site heme (Cys) (covalent) #status !8experimental\ !$15,69 #binding_site heme iron (His, Met) (axial ligands) !8#status experimental SUMMARY #length 131 #molecular-weight 14173 #checksum 8621 SEQUENCE /// ENTRY B81167 #type complete TITLE cytochrome c552 NMB0717 precursor [similarity] - Neisseria meningitidis (strain MC58 serogroup B) ORGANISM #formal_name Neisseria meningitidis DATE 01-Sep-2000 #sequence_revision 01-Sep-2000 #text_change 19-Jan-2001 ACCESSIONS B81167 REFERENCE A81000 !$#authors Tettelin, H.; Saunders, N.J.; Heidelberg, J.; Jeffries, !1A.C.; Nelson, K.E.; Eisen, J.A.; Ketchum, K.A.; Hood, D.W.; !1Peden, J.F.; Dodson, R.J.; Nelson, W.C.; Gwinn, M.L.; DeBoy, !1R.; Peterson, J.D.; Hickey, E.K.; Haft, D.H.; Salzberg, !1S.L.; White, O.; Fleischmann, R.D.; Dougherty, B.A.; Mason, !1T.; Ciecko, A.; Parksey, D.S.; Blair, E.; Cittone, H.; !1Clark, E.B.; Cotton, M.D.; Utterback, T.R.; Khouri, H.; Qin, !1H.; Vamathevan, J.; Gill, J.; Scarlato, V.; Masignani, V.; !1Pizza, M.; Grandi, G.; Sun, L.; Smith, H.O.; Fraser, C.M.; !1Moxon, E.R.; Rappuoli, R.; Venter, J.C. !$#journal Science (2000) 287:1809-1815 !$#title Complete genome sequence of Neisseria meningitidis serogroup !1B strain MC58. !$#cross-references MUID:20175755; PMID:10710307 !$#accession B81167 !'##molecule_type DNA !'##residues 1-138 ##label TET !'##cross-references GB:AE002426; GB:AE002098; NID:g7225939; !1PIDN:AAF41130.1; PID:g7225943; GSPDB:GN00119; TIGR:NMB0717 !'##experimental_source serogroup B, strain MC58 GENETICS !$#gene NMB0717 CLASSIFICATION #superfamily T. aquaticus cytochrome c552; cytochrome c6 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; metalloprotein FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-138 #product cytochrome c552 #status predicted #label !8MAT\ !$33-114 #domain cytochrome c6 homology #label CY6\ !$43,46 #binding_site heme (Cys) (covalent) #status !8predicted\ !$47,97 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 138 #molecular-weight 14715 #checksum 1294 SEQUENCE /// ENTRY F81938 #type complete TITLE cytochrome c552 NMA0925 precursor [similarity] - Neisseria meningitidis (strain Z2491 serogroup A) ORGANISM #formal_name Neisseria meningitidis DATE 01-Sep-2000 #sequence_revision 01-Sep-2000 #text_change 02-Feb-2001 ACCESSIONS F81938 REFERENCE A81775 !$#authors Parkhill, J.; Achtman, M.; James, K.D.; Bentley, S.D.; !1Churcher, C.; Klee, S.R.; Morelli, G.; Basham, D.; Brown, !1D.; Chillingworth, T.; Davies, R.M.; Davis, P.; Devlin, K.; !1Feltwell, T.; Hamlin, N.; Holroyd, S.; Jagels, K.; Leather, !1S.; Moule, S.; Mungall, K.; Quail, M.A.; Rajandream, M.A.; !1Rutherford, K.M.; Simmonds, M.; Skelton, J.; Whitehead, S.; !1Spratt, B.G.; Barrell, B.G. !$#journal Nature (2000) 404:502-506 !$#title Complete DNA sequence of a serogroup A strain of Neisseria !1menigitidis Z2491. !$#cross-references MUID:20222556; PMID:10761919 !$#accession F81938 !'##molecule_type DNA !'##residues 1-163 ##label PAR !'##cross-references GB:AL162754; GB:AL157959; NID:g7379424; !1PIDN:CAB84197.1; PID:g7379630; GSPDB:GN00124; NMASP:NMA0925 !'##experimental_source serogroup A, strain Z2491 GENETICS !$#gene NMA0919; NMA0925 CLASSIFICATION #superfamily T. aquaticus cytochrome c552; cytochrome c6 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; metalloprotein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-163 #product cytochrome c552 #status predicted #label !8MAT\ !$28-109 #domain cytochrome c6 homology #label CY6\ !$38,41 #binding_site heme (Cys) (covalent) #status !8predicted\ !$42,92 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 163 #molecular-weight 17403 #checksum 2065 SEQUENCE /// ENTRY CCPC54 #type complete TITLE cytochrome c554 - Paracoccus sp. ORGANISM #formal_name Paracoccus sp. DATE 18-Dec-1981 #sequence_revision 18-Dec-1981 #text_change 03-Mar-2000 ACCESSIONS A00097; S06255 REFERENCE A00097 !$#authors Ambler, R.P. !$#book The Evolution of Metalloenzymes, Metalloproteins and Related !1Materials, Leigh, G.J., ed., pp.100-118, Symposium Press, !1London, 1977 !$#title Cytochrome c and copper protein evolution in prokaryotes. !$#accession A00097 !'##molecule_type protein !'##residues 1-83 ##label AMB !'##experimental_source ATCC 12084 REFERENCE S06255 !$#authors Ambler, R.P.; Daniel, M.; McLellan, L.; Meyer, T.E.; !1Cusanovich, M.A.; Kamen, M.D. !$#journal Biochem. J. (1987) 248:365-371 !$#title Amino acid sequences of cytochrome c-554(548) and cytochrome !1c' from a halophilic denitrifying bacterium of the genus !1Paracoccus. !$#cross-references MUID:88133881; PMID:2829828 !$#accession S06255 !'##molecule_type protein !'##residues 1-83 ##label AM2 !'##experimental_source ATCC 12084 CLASSIFICATION #superfamily cytochrome c6; cytochrome c6 homology KEYWORDS chromoprotein; electron transfer; heme; homodimer; iron; !1metalloprotein; oxidative phosphorylation FEATURE !$5-79 #domain cytochrome c6 homology #label CYC\ !$14,17 #binding_site heme (Cys) (covalent) #status !8predicted\ !$18,63 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 83 #molecular-weight 8500 #checksum 1632 SEQUENCE /// ENTRY CCMP55 #type complete TITLE cytochrome c555 - Methylococcus capsulatus ORGANISM #formal_name Methylococcus capsulatus DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 03-Mar-2000 ACCESSIONS A23321; A05021 REFERENCE A90328 !$#authors Ambler, R.P.; Dalton, H.; Meyer, T.E.; Bartsch, R.G.; Kamen, !1M.D. !$#journal Biochem. J. (1986) 233:333-337 !$#title The amino acid sequence of cytochrome c-555 from the !1methane-oxidizing bacterium Methylococcus capsulatus. !$#cross-references MUID:86158741; PMID:3006666 !$#accession A23321 !'##molecule_type protein !'##residues 1-96 ##label AMB !'##experimental_source strain Bath, NCIB 11132 CLASSIFICATION #superfamily cytochrome c6; cytochrome c6 homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; photosynthesis FEATURE !$8-79 #domain cytochrome c6 homology #label CYC\ !$19,22 #binding_site heme (Cys) (covalent) #status !8experimental\ !$23,59 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 96 #molecular-weight 10506 #checksum 4509 SEQUENCE /// ENTRY CCML6 #type complete TITLE cytochrome c6 - golden alga (Monochrysis lutheri) ALTERNATE_NAMES cytochrome c553; soluble cytochrome f ORGANISM #formal_name Monochrysis lutheri DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 03-Mar-2000 ACCESSIONS A00099 REFERENCE A90746 !$#authors Laycock, M.V. !$#journal Can. J. Biochem. (1972) 50:1311-1325 !$#title The amino acid sequence of cytochrome c-553 from the !1chrysophycean alga Monochrysis lutheri. !$#cross-references MUID:73080382; PMID:4345913 !$#accession A00099 !'##molecule_type protein !'##residues 1-83 ##label LAY REFERENCE A94561 !$#authors Laycock, M.V. !$#submission submitted to the Atlas, December 1974 !$#contents annotation; amidation states, residues 2, 5, 7, 8, 13, and !173 CLASSIFICATION #superfamily cytochrome c6; cytochrome c6 homology KEYWORDS chloroplast; chromoprotein; electron transfer; heme; iron; !1metalloprotein; methylated amino acid; photosynthesis FEATURE !$4-78 #domain cytochrome c6 homology #label CYC\ !$14,17 #binding_site heme (Cys) (covalent) #status !8experimental\ !$18,59 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted\ !$24 #modified_site N6-methyllysine (Lys) (partial) !8#status experimental SUMMARY #length 83 #molecular-weight 8815 #checksum 4090 SEQUENCE /// ENTRY CCPF6 #type complete TITLE cytochrome c6 - brown alga (Petalonia fascia) ALTERNATE_NAMES cytochrome c553; soluble cytochrome f ORGANISM #formal_name Petalonia fascia DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 03-Mar-2000 ACCESSIONS A00100 REFERENCE A00100 !$#authors Sugimura, Y.; Hase, T.; Matsubara, H.; Shimokoriyama, M. !$#journal J. Biochem. (1981) 90:1213-1219 !$#title Studies on algal cytochromes. III. Amino acid sequence of !1cytochrome c-553 from a brown alga, Petalonia fascia. !$#cross-references MUID:82075747; PMID:6273394 !$#accession A00100 !'##molecule_type protein !'##residues 1-85 ##label SUG CLASSIFICATION #superfamily cytochrome c6; cytochrome c6 homology KEYWORDS chloroplast; chromoprotein; electron transfer; heme; iron; !1metalloprotein; photosynthesis FEATURE !$4-77 #domain cytochrome c6 homology #label CYC\ !$14,17 #binding_site heme (Cys) (covalent) #status !8experimental\ !$18,58 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 85 #molecular-weight 9207 #checksum 6681 SEQUENCE /// ENTRY CCAU6 #type complete TITLE cytochrome c6 - brown alga (Alaria esculenta) ALTERNATE_NAMES cytochrome c553; soluble cytochrome f ORGANISM #formal_name Alaria esculenta #common_name Atlantic wakame, badderlocks, murlin, henware DATE 08-Oct-1981 #sequence_revision 08-Oct-1981 #text_change 03-Mar-2000 ACCESSIONS A00101 REFERENCE A00101 !$#authors Laycock, M.V. !$#journal Biochem. J. (1975) 149:271-279 !$#title The amino acid sequence of cytochrome f from the brown alga !1Alaria esculenta (L.) Grev. !$#cross-references MUID:76061523; PMID:1191259 !$#accession A00101 !'##molecule_type protein !'##residues 1-86 ##label LAY COMMENT Cytochrome c6 is a monoheme monomer. It functions as an !1electron carrier between membrane-bound cytochrome f and !1P700 in the photophosphorylation chain in chloroplasts and !1algae. It substitutes for plastocyanin in copper-deficient !1blue-green algae and in the chloroplasts of some eukaryote !1algae. CLASSIFICATION #superfamily cytochrome c6; cytochrome c6 homology KEYWORDS acetylated amino end; chloroplast; chromoprotein; electron !1transfer; heme; iron; metalloprotein; photosynthesis FEATURE !$4-77 #domain cytochrome c6 homology #label CYC\ !$1 #modified_site acetylated amino end (Ile) #status !8absent\ !$14,17 #binding_site heme (Cys) (covalent) #status !8experimental\ !$18,58 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 86 #molecular-weight 9233 #checksum 8637 SEQUENCE /// ENTRY CCBF6 #type complete TITLE cytochrome c6 - yellow-green alga (Bumilleriopsis filiformis) ALTERNATE_NAMES cytochrome c553; soluble cytochrome f ORGANISM #formal_name Bumilleriopsis filiformis DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 03-Mar-2000 ACCESSIONS A00102 REFERENCE A94468 !$#authors Ambler, R. !$#citation unpublished results, cited by Dickerson, R.E., in The !1Evolution of Protein Structure and Function, Sigman, D.S., !1and Brazier, M.A.B., eds., pp.173-202, Academic Press, New !1York and London, 1980 !$#accession A00102 !'##molecule_type protein !'##residues 1-86 ##label AMB CLASSIFICATION #superfamily cytochrome c6; cytochrome c6 homology KEYWORDS chloroplast; chromoprotein; electron transfer; heme; iron; !1metalloprotein; photosynthesis FEATURE !$4-77 #domain cytochrome c6 homology #label CYC\ !$14,17 #binding_site heme (Cys) (covalent) #status !8predicted\ !$18,58 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 86 #molecular-weight 9121 #checksum 7933 SEQUENCE /// ENTRY CCPR6 #type complete TITLE cytochrome c6 - red alga (Porphyra tenera) ALTERNATE_NAMES cytochrome c553; soluble cytochrome f ORGANISM #formal_name Porphyra tenera DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 03-Mar-2000 ACCESSIONS A00103 REFERENCE A00103 !$#authors Ambler, R.P.; Meyer, T.E.; Bartsch, R.G. !$#submission submitted to the Atlas, August 1973 !$#accession A00103 !'##molecule_type protein !'##residues 1-85 ##label AMB CLASSIFICATION #superfamily cytochrome c6; cytochrome c6 homology KEYWORDS chloroplast; chromoprotein; electron transfer; heme; iron; !1metalloprotein; photosynthesis FEATURE !$4-77 #domain cytochrome c6 homology #label CYC\ !$14,17 #binding_site heme (Cys) (covalent) #status !8predicted\ !$18,58 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 85 #molecular-weight 9077 #checksum 5494 SEQUENCE /// ENTRY CCIA6 #type complete TITLE cytochrome c6 - Microcystis aeruginosa ALTERNATE_NAMES cytochrome c553; soluble cytochrome f ORGANISM #formal_name Microcystis aeruginosa DATE 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 03-Mar-2000 ACCESSIONS A00104 REFERENCE A94488 !$#authors Beecher, J.; Margoliash, E. !$#citation unpublished results, cited by Ulrich, E.L., Krogmann, D.W., !1and Markley, J.L., J. Biol. Chem. 257, 9356-9364, 1982 !$#accession A00104 !'##molecule_type protein !'##residues 1-80 ##label BEE CLASSIFICATION #superfamily cytochrome c6; cytochrome c6 homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; photosynthesis FEATURE !$1-72 #domain cytochrome c6 homology #label CYC\ !$10,13 #binding_site heme (Cys) (covalent) #status !8predicted\ !$14,53 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 80 #molecular-weight 8137 #checksum 3971 SEQUENCE /// ENTRY CCAI6 #type complete TITLE cytochrome c6 - Anabaena variabilis (tentative sequence) ALTERNATE_NAMES cytochrome c553; soluble cytochrome f ORGANISM #formal_name Anabaena variabilis DATE 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 31-Mar-2000 ACCESSIONS A94488; A93182; A00105 REFERENCE A94488 !$#authors Beecher, J.; Margoliash, E. !$#citation unpublished results, cited by Ulrich, E.L., Krogmann, D.W., !1and Markley, J.L., J. Biol. Chem. 257, 9356-9364, 1982 !$#accession A94488 !'##molecule_type protein !'##residues 1-86 ##label BEE REFERENCE A93182 !$#authors Aitken, A. !$#journal Nature (1976) 263:793-796 !$#title Protein evolution in cyanobacteria. !$#cross-references MUID:77056395; PMID:825785 !$#accession A93182 !'##molecule_type protein !'##residues 1-22;30-39;56-81,'D',83,'D',85-86 ##label AIT CLASSIFICATION #superfamily cytochrome c6; cytochrome c6 homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; photosynthesis FEATURE !$4-77 #domain cytochrome c6 homology #label CYC\ !$14,17 #binding_site heme (Cys) (covalent) #status !8predicted\ !$18,58 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 86 #molecular-weight 8973 #checksum 5450 SEQUENCE /// ENTRY S03859 #type complete TITLE cytochrome c6 - Microcystis aeruginosa ALTERNATE_NAMES cytochrome c553 ORGANISM #formal_name Microcystis aeruginosa DATE 28-Feb-1990 #sequence_revision 13-Sep-1996 #text_change 03-Mar-2000 ACCESSIONS S03859 REFERENCE S03859 !$#authors Cohn, C.L.; Hermodson, M.A.; Krogmann, D.W. !$#journal Arch. Biochem. Biophys. (1989) 270:219-226 !$#title The amino acid sequence of cytochrome c553 from Microcystis !1aeruginosa. !$#cross-references MUID:89192371; PMID:2539045 !$#accession S03859 !'##molecule_type protein !'##residues 1-81 ##label COH CLASSIFICATION #superfamily cytochrome c6; cytochrome c6 homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; photosynthesis FEATURE !$1-73 #domain cytochrome c6 homology #label CYC\ !$10,13 #binding_site heme (Cys) (covalent) #status !8predicted\ !$14,54 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 81 #molecular-weight 8421 #checksum 7300 SEQUENCE /// ENTRY CCAI53 #type complete TITLE cytochrome c6 precursor - Anabaena sp. (strain PCC 7937) ALTERNATE_NAMES cytochrome c553; soluble cytochrome f ORGANISM #formal_name Anabaena sp. DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 03-Mar-2000 ACCESSIONS S22481; S18858 REFERENCE S22481 !$#authors Bovy, A.; de Vrieze, G.; Borrias, M.; Weisbeek, P. !$#journal Plant Mol. Biol. (1992) 19:491-492 !$#title Isolation and sequence analysis of a gene encoding a basic !1cytochrome c-553 from the cyanobacterium Anabaena SP.PCC !17937. !$#cross-references MUID:92322981; PMID:1320427 !$#accession S22481 !'##molecule_type DNA !'##residues 1-111 ##label BOV !'##cross-references EMBL:X63194; NID:g312896; PIDN:CAA44876.1; !1PID:g39235 CLASSIFICATION #superfamily cytochrome c6; cytochrome c6 homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; photosynthesis FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-111 #product cytochrome c6 #status predicted #label MAT\ !$29-102 #domain cytochrome c6 homology #label CYC\ !$39,42 #binding_site heme (Cys) (covalent) #status !8predicted\ !$43,83 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 111 #molecular-weight 11840 #checksum 4101 SEQUENCE /// ENTRY JQ1083 #type complete TITLE cytochrome c6 precursor - Synechococcus sp. (strain PCC 7942) ALTERNATE_NAMES cytochrome c553; soluble cytochrome f ORGANISM #formal_name Synechococcus sp. DATE 31-Dec-1991 #sequence_revision 13-Sep-1996 #text_change 03-Nov-2000 ACCESSIONS JQ1083; A05180 REFERENCE JQ1083 !$#authors Laudenbach, D.E.; Herbert, S.K.; McDowell, C.; Fork, D.C.; !1Grossman, A.R.; Straus, N.A. !$#journal Plant Cell (1990) 2:913-924 !$#title Cytochrome c-553 is not required for photosynthetic activity !1in the cyanobacterium Synechococcus. !$#cross-references MUID:93005680; PMID:1967057 !$#accession JQ1083 !'##molecule_type DNA !'##residues 1-111 ##label LAU !'##cross-references GB:S44426; NID:g256651; PIDN:AAB23485.1; !1PID:g256652 REFERENCE A94469 !$#authors Margoliash, E. !$#citation unpublished results, cited by Dickerson, R.E., in The !1Evolution of Protein Structure and Function, Sigman, D.S., !1and Brazier, M.A.B., eds., pp.173-202, Academic Press, New !1York and London, 1980 !$#accession A05180 !'##molecule_type protein !'##residues 25-39,'S',41-55,'E',57-61,'E',63-86,'A',88-94,'EG',97-100, !1'A',102-105,'G',107,'E',109 ##label MAR !'##note the source is designated as Anacystis nidulans COMMENT This protein functions as a mobile carrier of electrons !1between the membrane-bound cytochrome b6-f complex and the !1p-700 reaction center of photosystem I in cyanobacteria and !1many eukaryotic algae. GENETICS !$#gene cytA CLASSIFICATION #superfamily cytochrome c6; cytochrome c6 homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; photosynthesis FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-111 #product cytochrome c6 #status predicted #label MAT\ !$28-101 #domain cytochrome c6 homology #label CYC\ !$38,41 #binding_site heme (Cys) (covalent) #status !8predicted\ !$42,82 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 111 #molecular-weight 11388 #checksum 5437 SEQUENCE /// ENTRY A53328 #type complete TITLE cytochrome c6 precursor - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 03-May-1994 #sequence_revision 13-Sep-1996 #text_change 16-Jun-2000 ACCESSIONS A53328; S77507 REFERENCE A53328 !$#authors Zhang, L.; Pakrasi, H.B.; Whitmarsh, J. !$#journal J. Biol. Chem. (1994) 269:5036-5042 !$#title Photoautotrophic growth of the cyanobacterium Synechocystis !1sp. PCC 6803 in the absence of cytochrome c-553 and !1plastocyanin. !$#cross-references MUID:94148959; PMID:8106479 !$#accession A53328 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-120 ##label ZHA !'##cross-references GB:L25252; NID:g468928; PIDN:AAA17489.1; !1PID:g468929 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S77507 !'##status preliminary !'##molecule_type DNA !'##residues 1-120 ##label KAN !'##cross-references EMBL:D90905; GB:AB001339; NID:g1652360; !1PIDN:BAA17354.1; PID:g1652432 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily cytochrome c6; cytochrome c6 homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; photosynthesis FEATURE !$1-35 #domain signal sequence #status predicted #label SIG\ !$36-120 #product cytochrome c6 #status predicted #label MAT\ !$39-112 #domain cytochrome c6 homology #label CYC\ !$49,52 #binding_site heme (Cys) (covalent) #status !8predicted\ !$53,93 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 120 #molecular-weight 12463 #checksum 3504 SEQUENCE /// ENTRY CCYC6L #type complete TITLE cytochrome c6 - Synechococcus lividus ALTERNATE_NAMES cytochrome c553; soluble cytochrome f ORGANISM #formal_name Synechococcus lividus DATE 31-Jan-1980 #sequence_revision 31-Jan-1980 #text_change 03-Mar-2000 ACCESSIONS A00106 REFERENCE A00106 !$#authors Borden, D.; Margoliash, E. !$#submission submitted to the Atlas, December 1979 !$#accession A00106 !'##molecule_type protein !'##residues 1-87 ##label BOR COMMENT Cytochrome c6 substitutes for plastocyanin in !1copper-deficient blue-green algae and the chloroplasts of !1some eukaryotic algae. CLASSIFICATION #superfamily cytochrome c6; cytochrome c6 homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; photosynthesis FEATURE !$4-77 #domain cytochrome c6 homology #label CYC\ !$14,17 #binding_site heme (Cys) (covalent) #status !8predicted\ !$18,58 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 87 #molecular-weight 9129 #checksum 7885 SEQUENCE /// ENTRY CCYC6 #type complete TITLE cytochrome c6 - Synechococcus sp. (ATCC 27167) ALTERNATE_NAMES cytochrome c553; soluble cytochrome f ORGANISM #formal_name Synechococcus sp. DATE 31-Jan-1980 #sequence_revision 23-Oct-1981 #text_change 03-Mar-2000 ACCESSIONS A00107 REFERENCE A00107 !$#authors Aitken, A. !$#journal Eur. J. Biochem. (1979) 101:297-308 !$#title Purification and primary structure of cytochrome c-552 from !1the cyanobacterium, Synechococcus PCC 6312. !$#cross-references MUID:80068924; PMID:228936 !$#accession A00107 !'##molecule_type protein !'##residues 1-87 ##label AIT CLASSIFICATION #superfamily cytochrome c6; cytochrome c6 homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; photosynthesis FEATURE !$4-77 #domain cytochrome c6 homology #label CYC\ !$14,17 #binding_site heme (Cys) (covalent) #status !8experimental\ !$18,58 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 87 #molecular-weight 9098 #checksum 9125 SEQUENCE /// ENTRY CCFZ6 #type complete TITLE cytochrome c6 - Aphanizomenon flos-aquae ALTERNATE_NAMES cytochrome c553; soluble cytochrome f ORGANISM #formal_name Aphanizomenon flos-aquae DATE 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 03-Mar-2000 ACCESSIONS A00108 REFERENCE A94489 !$#authors Sprinkle, J.; Hermodson, M.; Krogmann, D.W. !$#citation unpublished results, cited by Ulrich, E.L., Krogmann, D.W., !1and Markley, J.L., J. Biol. Chem. 257, 9356-9364, 1982 !$#accession A00108 !'##molecule_type protein !'##residues 1-87 ##label SPR CLASSIFICATION #superfamily cytochrome c6; cytochrome c6 homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; photosynthesis FEATURE !$4-77 #domain cytochrome c6 homology #label CYC\ !$14,17 #binding_site heme (Cys) (covalent) #status !8predicted\ !$18,58 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 87 #molecular-weight 9293 #checksum 8476 SEQUENCE /// ENTRY CCPB6 #type complete TITLE cytochrome c6 - Plectonema boryanum ALTERNATE_NAMES cytochrome c553; soluble cytochrome f ORGANISM #formal_name Plectonema boryanum DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 03-Mar-2000 ACCESSIONS A00109 REFERENCE A00109 !$#authors Aitken, A. !$#journal Eur. J. Biochem. (1977) 78:273-279 !$#title Purification and primary structure of cytochrome f from the !1cyanobacterium, Plectonema boryanum. !$#cross-references MUID:78023897; PMID:199428 !$#accession A00109 !'##molecule_type protein !'##residues 1-85 ##label AIT !'##experimental_source CCAP 1462/2 CLASSIFICATION #superfamily cytochrome c6; cytochrome c6 homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; photosynthesis FEATURE !$4-77 #domain cytochrome c6 homology #label CYC\ !$14,17 #binding_site heme (Cys) (covalent) #status !8experimental\ !$18,58 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 85 #molecular-weight 8576 #checksum 3761 SEQUENCE /// ENTRY CCSG6 #type complete TITLE cytochrome c6 - Spirulina maxima ALTERNATE_NAMES cytochrome c553; soluble cytochrome f ORGANISM #formal_name Spirulina maxima DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 03-Mar-2000 ACCESSIONS A00110 REFERENCE A00110 !$#authors Ambler, R.P.; Bartsch, R.G. !$#journal Nature (1975) 253:285-288 !$#title Amino acid sequence similarity between cytochrome f from a !1blue-green bacterium and algal chloroplasts. !$#cross-references MUID:75100362; PMID:803642 !$#accession A00110 !'##molecule_type protein !'##residues 1-89 ##label AMB CLASSIFICATION #superfamily cytochrome c6; cytochrome c6 homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; photosynthesis FEATURE !$4-81 #domain cytochrome c6 homology #label CYC\ !$14,17 #binding_site heme (Cys) (covalent) #status !8predicted\ !$18,62 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 89 #molecular-weight 9236 #checksum 4733 SEQUENCE /// ENTRY CCPSS #type complete TITLE cytochrome c, nitrite reductase associated, precursor - Pseudomonas stutzeri (strain ZoBell) ALTERNATE_NAMES nirC protein ORGANISM #formal_name Pseudomonas stutzeri #variety strain ZoBell DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Mar-2000 ACCESSIONS S13940; S68356 REFERENCE S13613 !$#authors Juengst, A.; Wakabayashi, S.; Matsubara, H.; Zumft, W.G. !$#journal FEBS Lett. (1991) 279:205-209 !$#title The nirSTBM region coding for cytochrome cd(1)-dependent !1nitrite respiration of Pseudomonas stutzeri consists of a !1cluster of mono-, di-, and tetraheme proteins. !$#cross-references MUID:91160715; PMID:2001732 !$#accession S13940 !'##molecule_type DNA !'##residues 1-113 ##label JUE !'##cross-references EMBL:X56813; NID:g45838; PIDN:CAA40154.1; !1PID:g45843 !'##experimental_source strain ZoBell REFERENCE S68351 !$#authors Palmedo, G.; Seither, P.; Koerner, H.; Matthews, J.C.; !1Burkhalter, R.S.; Timkovich, R.; Zumft, W.G. !$#journal Eur. J. Biochem. (1995) 232:737-746 !$#title Resolution of the nirD locus for heme d(1) synthesis of !1cytochrome cd(1) (respiratory nitrite reductase) from !1Pseudomonas stutzeri. !$#cross-references MUID:96028114; PMID:7588711 !$#accession S68356 !'##molecule_type DNA !'##residues 103-113 ##label PAL !'##cross-references EMBL:Z50198 !'##experimental_source strain ZoBell GENETICS !$#gene nirC CLASSIFICATION #superfamily cytochrome c6; cytochrome c6 homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; periplasmic space FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-113 #product cytochrome c, nitrite reductase associated !8#status predicted #label MAT\ !$35-106 #domain cytochrome c6 homology #label CYC\ !$45,48 #binding_site heme (Cys) (covalent) #status !8predicted\ !$49,87 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 113 #molecular-weight 11924 #checksum 3532 SEQUENCE /// ENTRY CCKM6R #type complete TITLE cytochrome c6 precursor - Chlamydomonas reinhardtii ALTERNATE_NAMES cytochrome C552 ORGANISM #formal_name Chlamydomonas reinhardtii DATE 30-Sep-1993 #sequence_revision 03-Oct-1995 #text_change 03-Mar-2000 ACCESSIONS A27113; A39341 REFERENCE A27113 !$#authors Merchant, S.; Bogorad, L. !$#journal J. Biol. Chem. (1987) 262:9062-9067 !$#title The Cu(II)-repressible plastidic cytochrome c. Cloning and !1sequence of a complementary DNA for the pre-apoprotein. !$#cross-references MUID:87250547; PMID:3036842 !$#accession A27113 !'##molecule_type mRNA !'##residues 1-106,'S',108-148 ##label MER !'##cross-references GB:J02774; NID:g167406; PIDN:AAA33081.1; !1PID:g167407 !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing; 107-Ile was !1observed in the protein sequence REFERENCE A39341 !$#authors Hill, K.L.; Li, H.H.; Singer, J.; Merchant, S. !$#journal J. Biol. Chem. (1991) 266:15060-15067 !$#title Isolation and structural characterization of the !1Chlamydomonas reinhardtii gene for cytochrome c-6. Analysis !1of the kinetics and metal specificity of its !1copper-responsive expression. !$#cross-references MUID:91332023; PMID:1714451 !$#accession A39341 !'##molecule_type DNA !'##residues 1-148 ##label HIL !'##cross-references GB:M67448; NID:g167414; PIDN:AAB00729.1; !1PID:g167415 CLASSIFICATION #superfamily cytochrome c6; cytochrome c6 homology KEYWORDS chloroplast; chromoprotein; electron transfer; heme; iron; !1metalloprotein; photosynthesis FEATURE !$1-58 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$59-148 #product cytochrome c6 #status experimental #label !8MAT\ !$62-137 #domain cytochrome c6 homology #label CYC\ !$72,75 #binding_site heme (Cys) (covalent) #status !8predicted\ !$76,118 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 148 #molecular-weight 15426 #checksum 3686 SEQUENCE /// ENTRY S35677 #type complete TITLE cytochrome c6 [validated] - green alga (Monoraphidium braunii) ALTERNATE_NAMES cytochrome c552 ORGANISM #formal_name Monoraphidium braunii DATE 10-Dec-1993 #sequence_revision 13-Sep-1996 #text_change 20-Apr-2000 ACCESSIONS S35677 REFERENCE S35677 !$#authors Campos, A.P.; Aguiar, A.P.; Hervas, M.; Regalla, M.; !1Navarro, J.A.; Ortega, J.M.; Xavier, A.V.; de la Rosa, M.A.; !1Teixeira, M. !$#journal Eur. J. Biochem. (1993) 216:329-341 !$#title Cytochrome c(6) from Monoraphidium braunii. A cytochrome !1with an unusual heme axial coordination. !$#cross-references MUID:93373943; PMID:8396033 !$#accession S35677 !'##molecule_type protein !'##residues 1-89 ##label CAM REFERENCE A65336 !$#authors Sheldrick, G.M. !$#submission submitted to the Brookhaven Protein Data Bank, August 1995 !$#cross-references PDB:1CTJ !$#contents annotation; X-ray crystallography, 1.1 angstroms, residues !11-89 REFERENCE A59224 !$#authors Banci, L.; Bertini, I.; De la Rosa, M.A.; Koulougliotis, D.; !1Navarro, J.A.; Walter, O. !$#journal Biochemistry (1998) 37:4831-4843 !$#title Solution structure of oxidized cytochrome c6 from the green !1alga Monoraphidium braunii. !$#cross-references MUID:98206900; PMID:9538000 !$#contents annotation; conformation by (1)H-NMR REFERENCE A65247 !$#authors Banci, L.; Bertini, I.; Quacquarini, G.; Walter, O.; Diaz, !1A.; Hervas, M.; De La Rosa, M.A. !$#submission submitted to the Brookhaven Protein Data Bank, March 1996 !$#cross-references PDB:1CED !$#contents annotation; conformation by (1)H-NMR, reduced form, residues !11-89 REFERENCE A68953 !$#authors Banci, L.; Bertini, I.; De La Rosa, M.A.; Koulougliotis, D.; !1Navarro, J.A.; Walter, O. !$#submission submitted to the Brookhaven Protein Data Bank, January 1998 !$#cross-references PDB:1A2S !$#contents annotation; conformation by (1)H-NMR, oxidized form, !1residues 1-89 CLASSIFICATION #superfamily cytochrome c6; cytochrome c6 homology KEYWORDS chromoprotein; electron transfer; heme; iron; metalloprotein FEATURE !$5-80 #domain cytochrome c6 homology #label CYC\ !$15,18 #binding_site heme (Cys) (covalent) #status !8experimental\ !$19,61 #binding_site heme iron (His, Met) (axial ligands) !8#status experimental SUMMARY #length 89 #molecular-weight 9352 #checksum 1291 SEQUENCE /// ENTRY CCBM6 #type complete TITLE cytochrome c6 - green alga (Bryopsis maxima) ALTERNATE_NAMES cytochrome c553; soluble cytochrome f ORGANISM #formal_name Bryopsis maxima DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Mar-2000 ACCESSIONS A30021 REFERENCE A30021 !$#authors Okamoto, Y.; Minami, Y.; Matsubara, H.; Sugimura, Y. !$#journal J. Biochem. (1987) 102:1251-1260 !$#title Studies on algal cytochromes VI: some properties and amino !1acid sequence of cytochrome c-6 from a green alga, Bryopsis !1maxima. !$#cross-references MUID:88139277; PMID:3481367 !$#accession A30021 !'##molecule_type protein !'##residues 1-88 ##label OKA CLASSIFICATION #superfamily cytochrome c6; cytochrome c6 homology KEYWORDS chloroplast; chromoprotein; electron transfer; heme; iron; !1metalloprotein; photosynthesis FEATURE !$5-80 #domain cytochrome c6 homology #label CYC\ !$15,18 #binding_site heme (Cys) (covalent) #status !8experimental\ !$19,61 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 88 #molecular-weight 9286 #checksum 2982 SEQUENCE /// ENTRY CCEG6 #type complete TITLE cytochrome c6 - Euglena gracilis ALTERNATE_NAMES cytochrome c553; soluble cytochrome f ORGANISM #formal_name Euglena gracilis DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 03-Mar-2000 ACCESSIONS A00111 REFERENCE A00111 !$#authors Pettigrew, G.W. !$#journal Biochem. J. (1974) 139:449-459 !$#title The purification and amino acid sequence of cytochrome c-552 !1from Euglena gracilis. !$#cross-references MUID:75090229; PMID:4374934 !$#accession A00111 !'##molecule_type protein !'##residues 1-87 ##label PET CLASSIFICATION #superfamily cytochrome c6; cytochrome c6 homology KEYWORDS chloroplast; chromoprotein; electron transfer; heme; iron; !1metalloprotein; photosynthesis FEATURE !$1-75 #domain cytochrome c6 homology #label CYC\ !$10,13 #binding_site heme (Cys) (covalent) #status !8predicted\ !$14,56 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 87 #molecular-weight 9117 #checksum 2043 SEQUENCE /// ENTRY S15453 #type complete TITLE cytochrome c6 - Euglena viridis ORGANISM #formal_name Euglena viridis DATE 13-Jan-1995 #sequence_revision 13-Sep-1996 #text_change 03-Mar-2000 ACCESSIONS S15453 REFERENCE S15425 !$#authors Ambler, R.P.; Kamen, M.D.; Bartsch, R.G.; Meyer, T.E. !$#journal Biochem. J. (1991) 276:47-52 !$#title Amino acid sequences of Euglena viridis ferredoxin and !1cytochromes c. !$#cross-references MUID:91248164; PMID:1645532 !$#accession S15453 !'##status preliminary !'##molecule_type protein !'##residues 1-87 ##label AMB CLASSIFICATION #superfamily cytochrome c6; cytochrome c6 homology KEYWORDS chloroplast; chromoprotein; electron transfer; heme; iron; !1metalloprotein FEATURE !$1-75 #domain cytochrome c6 homology #label CYC\ !$10,13 #binding_site heme (Cys) (covalent) #status !8experimental\ !$14,56 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 87 #molecular-weight 9312 #checksum 2203 SEQUENCE /// ENTRY CCPSVM #type complete TITLE cytochrome c5 - Pseudomonas mendocina ORGANISM #formal_name Pseudomonas mendocina DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 03-Mar-2000 ACCESSIONS A00114 REFERENCE A00114 !$#authors Ambler, R.P.; Taylor, E. !$#journal Biochem. Soc. Trans. (1973) 1:166-168 !$#title Amino acid sequence of cytochrome c-5 from Pseudomonas !1mendocina. !$#accession A00114 !'##molecule_type protein !'##residues 1-87 ##label AMB !'##experimental_source strain CH-110 COMMENT This is a dimeric monoheme c-type cytochrome. It is !1unreactive with cytochrome c reductase or oxidase but seems !1to function as an intermediate in nitrate respiration of !1facultative anaerobic pseudmonads. It appears to be present !1also in the strictly anaerobic nitrogen-fixing Azotobacter. CLASSIFICATION #superfamily cytochrome c6; cytochrome c6 homology KEYWORDS chromoprotein; electron transfer; heme; iron; metalloprotein FEATURE !$8-84 #domain cytochrome c6 homology #label CYC\ !$19,22 #binding_site heme (Cys) (covalent) #status !8predicted\ !$23,63 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 87 #molecular-weight 8657 #checksum 3727 SEQUENCE /// ENTRY CCER51 #type complete TITLE cytochrome c551 - Ectothiorhodospira halophila ORGANISM #formal_name Ectothiorhodospira halophila DATE 30-Nov-1979 #sequence_revision 30-Nov-1979 #text_change 03-Mar-2000 ACCESSIONS S38755; A00115 REFERENCE S38755 !$#authors Ambler, R.P.; Meyer, T.E.; Kamen, M.D. !$#journal Arch. Biochem. Biophys. (1993) 306:83-93 !$#title Amino acid sequences of cytochromes c-551 from the !1halophilic purple phototrophic bacteria, Ectothiorhodospira !1halophila and E. halochloris. !$#cross-references MUID:94028993; PMID:8215425 !$#accession S38755 !'##molecule_type protein !'##residues 1-78 ##label AM1 REFERENCE A00115 !$#authors Ambler, R.P. !$#submission submitted to the Atlas, August 1979 !$#accession A00115 !'##molecule_type protein !'##residues 1-78 ##label AM2 !'##experimental_source strain BN9626 CLASSIFICATION #superfamily cytochrome c6; cytochrome c6 homology KEYWORDS chromoprotein; electron transfer; heme; iron; metalloprotein FEATURE !$3-74 #domain cytochrome c6 homology #label CYC\ !$14,17 #binding_site heme (Cys) (covalent) #status !8predicted\ !$18,55 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 78 #molecular-weight 8258 #checksum 1198 SEQUENCE /// ENTRY CCCF55 #type complete TITLE cytochrome c555 - Chlorobium sp. ORGANISM #formal_name Chlorobium sp. DATE 13-Jul-1981 #sequence_revision 13-Jul-1981 #text_change 03-Mar-2000 ACCESSIONS A00116 REFERENCE A00116 !$#authors Van Beeumen, J.; Ambler, R.P.; Meyer, T.E.; Kamen, M.D.; !1Olson, J.M.; Shaw, E.K. !$#journal Biochem. J. (1976) 159:757-774 !$#title The amino acid sequences of the cytochromes c-555 from two !1green sulphur bacteria of the genus Chlorobium. !$#cross-references MUID:77087088; PMID:188412 !$#accession A00116 !'##molecule_type protein !'##residues 1-86 ##label VAN !'##note the source is designated as Chlorobium thiosulfatophilum REFERENCE A38043 !$#authors Korszun, Z.R.; Salemme, F.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1977) 74:5244-5247 !$#title Structure of cytochrome c555 of Chlorobium !1thiosulfatophilum: primitive low-potential cytochrome c. !$#cross-references MUID:78094383; PMID:202947 !$#contents annotation; X-ray crystallography, 2.7 angstroms COMMENT This basic c-type monoheme cytochrome has been found !1exclusively in the green photosynthetic bacteria, although !1its role in bacterial photosynthesis is not established. It !1has an unusually low redox potential compared with !1mitochondrial cytochrome c. It is reactive with cytochrome c !1oxidases but not with reductases. CLASSIFICATION #superfamily cytochrome c6; cytochrome c6 homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; photosynthesis FEATURE !$4-81 #domain cytochrome c6 homology #label CYC\ !$14,17 #binding_site heme (Cys) (covalent) #status !8experimental\ !$18,60 #binding_site heme iron (His, Met) (axial ligands) !8#status experimental SUMMARY #length 86 #molecular-weight 8780 #checksum 7840 SEQUENCE /// ENTRY CCPH55 #type complete TITLE cytochrome c555 - Prosthecochloris aestuarii ORGANISM #formal_name Prosthecochloris aestuarii DATE 13-Jul-1981 #sequence_revision 13-Jul-1981 #text_change 03-Mar-2000 ACCESSIONS A00117 REFERENCE A00116 !$#authors Van Beeumen, J.; Ambler, R.P.; Meyer, T.E.; Kamen, M.D.; !1Olson, J.M.; Shaw, E.K. !$#journal Biochem. J. (1976) 159:757-774 !$#title The amino acid sequences of the cytochromes c-555 from two !1green sulphur bacteria of the genus Chlorobium. !$#cross-references MUID:77087088; PMID:188412 !$#accession A00117 !'##molecule_type protein !'##residues 1-99 ##label VAN !'##note the source is designated as Chlorobium limicola REFERENCE A38042 !$#authors Olson, J.M. !$#journal Int. J. Syst. Bacteriol. (1978) 28:128-129 !$#contents annotation; taxonomy CLASSIFICATION #superfamily cytochrome c6; cytochrome c6 homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; photosynthesis FEATURE !$13-94 #domain cytochrome c6 homology #label CYC\ !$23,26 #binding_site heme (Cys) (covalent) #status !8predicted\ !$27,73 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 99 #molecular-weight 10473 #checksum 3605 SEQUENCE /// ENTRY CCRFG2 #type complete TITLE cytochrome c2 - Rhodocyclus gelatinosus ORGANISM #formal_name Rhodocyclus gelatinosus DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 03-Mar-2000 ACCESSIONS A00089 REFERENCE A93207 !$#authors Ambler, R.P.; Meyer, T.E.; Kamen, M.D. !$#journal Nature (1979) 278:661-662 !$#title Anomalies in amino acid sequences of small cytochromes c and !1cytochromes c' from two species of purple photosynthetic !1bacteria. !$#cross-references MUID:79199668; PMID:221823 !$#accession A00089 !'##molecule_type protein !'##residues 1-85 ##label AMB COMMENT This sequence is more closely related to the sequences of !1cytochrome c551 from Pseudomonas and Azotobacter than to the !1sequences of cytochrome c2 from other species of !1Rhodopseudomonas. CLASSIFICATION #superfamily cytochrome c6; cytochrome c6 homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; photosynthesis FEATURE !$1-81 #domain cytochrome c6 homology #label CYC\ !$12,15 #binding_site heme (Cys) (covalent) #status !8predicted\ !$16,61 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 85 #molecular-weight 8899 #checksum 4949 SEQUENCE /// ENTRY CCPS5A #type complete TITLE cytochrome c551 precursor [validated] - Pseudomonas aeruginosa ALTERNATE_NAMES cytochrome c8 ORGANISM #formal_name Pseudomonas aeruginosa DATE 24-Apr-1984 #sequence_revision 12-May-1994 #text_change 06-Oct-2000 ACCESSIONS B34141; B34255; PC4130; A90346; B90272; B83582; A00091 REFERENCE A34141 !$#authors Nordling, M.; Young, S.; Karlsson, B.G.; Lundberg, L.G. !$#journal FEBS Lett. (1990) 259:230-232 !$#title The structural gene for cytochrome c-551 from Pseudomonas !1aeruginosa. The nucleotide sequence shows a location !1downstream of the nitrite reductase gene. !$#cross-references MUID:90092552; PMID:2152881 !$#accession B34141 !'##molecule_type DNA !'##residues 1-104 ##label NOR !'##cross-references EMBL:X51319; NID:g45305; PIDN:CAA35703.1; !1PID:g45307 REFERENCE A34255 !$#authors Arai, H.; Sanbongi, Y.; Igarashi, Y.; Kodama, T. !$#journal FEBS Lett. (1990) 261:196-198 !$#title Cloning and sequencing of the gene encoding cytochrome c-551 !1from Pseudomonas aeruginosa. !$#cross-references MUID:90169115; PMID:2155133 !$#accession B34255 !'##molecule_type DNA !'##residues 1-104 ##label ARA !'##cross-references GB:X51631; NID:g45316; PIDN:CAA35958.1; PID:g45318 REFERENCE JC4552 !$#authors Kawasaki, S.; Arai, H.; Igarashi, Y.; Kodama, T. !$#journal Gene (1995) 167:87-91 !$#title Sequencing and characterization of the downstream region of !1the genes encoding nitrite reductase and cytochrome c-551 !1(nirSM) from Pseudomonas aeruginosa: Identification of the !1gene necessary for biosynthesis of heme d1. !$#cross-references MUID:96144254; PMID:8566817 !$#accession PC4130 !'##molecule_type DNA !'##residues 'C',95-104 ##label KAW !'##cross-references DDBJ:D50473; NID:g1217594 REFERENCE A90346 !$#authors Ambler, R.P. !$#journal Biochem. J. (1963) 89:349-378 !$#title The amino acid sequence of Pseudomonas cytochrome c-551. !$#accession A90346 !'##molecule_type protein !'##residues 23-104 ##label AM1 !'##experimental_source strain P6009 REFERENCE A90272 !$#authors Ambler, R.P. !$#journal Biochem. J. (1974) 137:3-14 !$#title The evolutionary stability of cytochrome c-551 in !1Pseudomonas aeruginosa and Pseudomonas fluorescens biotype !1C. !$#cross-references MUID:74140216; PMID:4362497 !$#accession B90272 !'##molecule_type protein !'##residues 23-104 ##label AM2 !'##note nine strains were analyzed; the sequences from eight strains !1appear to be identical with that shown; the sequence of !1strain 129/1224 differs from that shown in having 24-Ala REFERENCE A51484 !$#authors Detlefsen, D.J.; Thanabal, V.; Pecoraro, V.L.; Wagner, G. !$#submission submitted to the Brookhaven Protein Data Bank, May 1993 !$#cross-references PDB:2PAC !$#contents annotation; conformation by (1)H-NMR, residues 23-104 REFERENCE A58605 !$#authors Detlefsen, D.J.; Thanabal, V.; Pecoraro, V.L.; Wagner, G. !$#journal Biochemistry (1991) 30:9040-9046 !$#title Solution structure of Fe(II) cytochrome c551 from !1Pseudomonas aeruginosa as determined by two-dimensional (1)H !1NMR. !$#cross-references MUID:91369910; PMID:1654086 !$#contents annotation; conformation by (1)H-NMR REFERENCE A50561 !$#authors Matsuura, Y.; Takano, T.; Dickerson, R.E. !$#submission submitted to the Brookhaven Protein Data Bank, July 1981 !$#cross-references PDB:351C !$#contents annotation; X-ray crystallography, 1.6 angstroms, oxidized, !1residues 23-104 REFERENCE A50640 !$#authors Matsuura, Y.; Takano, T.; Dickerson, R.E. !$#submission submitted to the Brookhaven Protein Data Bank, July 1981 !$#cross-references PDB:451C !$#contents annotation; X-ray crystallography, 1.6 angstroms, reduced, !1residues 23-104 REFERENCE A92881 !$#authors Matsuura, Y.; Takano, T.; Dickerson, R.E. !$#journal J. Mol. Biol. (1982) 156:389-409 !$#title Structure of cytochrome c-551 from Pseudomonas aeruginosa !1refined at 1.6 angstrom resolution and comparison of the two !1redox forms. !$#cross-references MUID:82216851; PMID:6283101 !$#contents annotation; X-ray crystallography, 1.6 angstroms REFERENCE A82950 !$#authors Stover, C.K.; Pham, X.Q.; Erwin, A.L.; Mizoguchi, S.D.; !1Warrener, P.; Hickey, M.J.; Brinkman, F.S.L.; Hufnagle, !1W.O.; Kowalik, D.J.; Lagrou, M.; Garber, R.L.; Goltry, L.; !1Tolentino, E.; Westbrook-Wadman, S.; Yuan, Y.; Brody, L.L.; !1Coulter, S.N.; Folger, K.R.; Kas, A.; Larbig, K.; Lim, R.M.; !1Smith, K.A.; Spencer, D.H.; Wong, G.K.S.; Wu, Z.; Paulsen, !1I.T.; Reizer, J.; Saier, M.H.; Hancock, R.E.W.; Lory, S.; !1Olson, M.V. !$#journal Nature (2000) 406:959-964 !$#title Complete genome sequence of Pseudomonas aeruginosa PA01, an !1opportunistic pathogen. !$#cross-references MUID:20437337; PMID:10984043 !$#accession B83582 !'##status preliminary !'##molecule_type DNA !'##residues 1-104 ##label STO !'##cross-references GB:AE004488; GB:AE004091; NID:g9946372; !1PIDN:AAG03907.1; GSPDB:GN00131; PASP:PA0518 !'##experimental_source strain PAO1 COMMENT This monoheme cytochrome is unreactive with mitochondrial !1cytochrome c oxidase or reductase. It functions in nitrite !1and nitrate respiration in Pseudomonas. GENETICS !$#gene nirM; PA0518 FUNCTION !$#description electron donor to Pseudomonas cytochrome oxidase (EC !11.9.3.2) !$#pathway nitrate respiration CLASSIFICATION #superfamily cytochrome c6; cytochrome c6 homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; nitrate respiration FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-104 #product cytochrome c551 #status experimental #label !8MAT\ !$23-100 #domain cytochrome c6 homology #label CYC\ !$34,37 #binding_site heme (Cys) (covalent) #status !8experimental\ !$38,83 #binding_site heme iron (His, Met) (axial ligands) !8#status experimental SUMMARY #length 104 #molecular-weight 10967 #checksum 8442 SEQUENCE /// ENTRY CCQF2T #type complete TITLE cytochrome c2 - Rhodocyclus tenuis ORGANISM #formal_name Rhodocyclus tenuis DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 03-Mar-2000 ACCESSIONS A00090 REFERENCE A93207 !$#authors Ambler, R.P.; Meyer, T.E.; Kamen, M.D. !$#journal Nature (1979) 278:661-662 !$#title Anomalies in amino acid sequences of small cytochromes c and !1cytochromes c' from two species of purple photosynthetic !1bacteria. !$#cross-references MUID:79199668; PMID:221823 !$#accession A00090 !'##molecule_type protein !'##residues 1-92 ##label AMB COMMENT This sequence is more closely related to the sequences of !1cytochrome c551 from Pseudomonas and Azotobacter than to the !1sequences of cytochrome c2 from other species of !1Rhodospirillum. CLASSIFICATION #superfamily cytochrome c6; cytochrome c6 homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; photosynthesis FEATURE !$1-83 #domain cytochrome c6 homology #label CYC\ !$12,15 #binding_site heme (Cys) (covalent) #status !8predicted\ !$16,66 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 92 #molecular-weight 9781 #checksum 2620 SEQUENCE /// ENTRY CCPS5F #type complete TITLE cytochrome c551 [validated] - Pseudomonas fluorescens (biotype C) ORGANISM #formal_name Pseudomonas fluorescens DATE 13-Jul-1981 #sequence_revision 13-Jul-1981 #text_change 03-Nov-2000 ACCESSIONS A00092; A90272 REFERENCE A90266 !$#authors Ambler, R.P.; Wynn, M. !$#journal Biochem. J. (1973) 131:485-498 !$#title The amino acid sequences of cytochromes c-551 from three !1species of Pseudomonas. !$#cross-references MUID:73224976; PMID:4352718 !$#accession A00092 !'##molecule_type protein !'##residues 1-82 ##label AMB1 !'##experimental_source strain C18, ATCC 17400 REFERENCE A90272 !$#authors Ambler, R.P. !$#journal Biochem. J. (1974) 137:3-14 !$#title The evolutionary stability of cytochrome c-551 in !1Pseudomonas aeruginosa and Pseudomonas fluorescens biotype !1C. !$#cross-references MUID:74140216; PMID:4362497 !$#accession A90272 !'##molecule_type protein !'##residues 1-82 ##label AMB2 !'##note the sequence from strain 50 differs from that shown at least in !1having 18-Val, 29-Asp, and 47-Arg; the sequences from !1strains 181 and 217 differ in having 1-Asp, 46-Ser, 63-Ala, !1and 65-Pro; the sequence from strain 191 differs in having !11-Asp, 46-Asp, and 70-Gln; the sequence from strain 204 !1differs in having 1-Asp and probably 65-Pro; the sequence !1from strain 8376 is identical with that shown GENETICS !$#gene nirM CLASSIFICATION #superfamily cytochrome c6; cytochrome c6 homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; oxidative phosphorylation FEATURE !$1-78 #domain cytochrome c6 homology #label CYC\ !$12,15 #binding_site heme (Cys) (covalent) #status !8predicted\ !$16,61 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 82 #molecular-weight 8538 #checksum 8028 SEQUENCE /// ENTRY CCPS5S #type complete TITLE cytochrome c551 [validated] - Pseudomonas stutzeri (strain 221) ORGANISM #formal_name Pseudomonas stutzeri DATE 13-Jul-1981 #sequence_revision 13-Jul-1981 #text_change 03-Nov-2000 ACCESSIONS A00093 REFERENCE A90266 !$#authors Ambler, R.P.; Wynn, M. !$#journal Biochem. J. (1973) 131:485-498 !$#title The amino acid sequences of cytochromes c-551 from three !1species of Pseudomonas. !$#cross-references MUID:73224976; PMID:4352718 !$#accession A00093 !'##molecule_type protein !'##residues 1-82 ##label AMB GENETICS !$#gene nirM CLASSIFICATION #superfamily cytochrome c6; cytochrome c6 homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; oxidative phosphorylation FEATURE !$1-78 #domain cytochrome c6 homology #label CYC\ !$12,15 #binding_site heme (Cys) (covalent) #status !8predicted\ !$16,61 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 82 #molecular-weight 8612 #checksum 6641 SEQUENCE /// ENTRY CCPS5B #type complete TITLE cytochrome c551 precursor - Pseudomonas stutzeri (strain ZoBell) ORGANISM #formal_name Pseudomonas stutzeri DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Mar-2000 ACCESSIONS S13939 REFERENCE S13613 !$#authors Juengst, A.; Wakabayashi, S.; Matsubara, H.; Zumft, W.G. !$#journal FEBS Lett. (1991) 279:205-209 !$#title The nirSTBM region coding for cytochrome cd(1)-dependent !1nitrite respiration of Pseudomonas stutzeri consists of a !1cluster of mono-, di-, and tetraheme proteins. !$#cross-references MUID:91160715; PMID:2001732 !$#accession S13939 !'##molecule_type DNA !'##residues 1-104 ##label JUE !'##cross-references EMBL:X56813; NID:g45838; PIDN:CAA40153.1; !1PID:g45842 !'##experimental_source strain ZoBell, ATCC 14405 GENETICS !$#gene nirM CLASSIFICATION #superfamily cytochrome c6; cytochrome c6 homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; oxidative phosphorylation FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-104 #product cytochrome c551 #status predicted #label !8MAT\ !$23-100 #domain cytochrome c6 homology #label CYC\ !$34,37 #binding_site heme (Cys) (covalent) #status !8predicted\ !$38,83 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 104 #molecular-weight 10797 #checksum 7619 SEQUENCE /// ENTRY CCPS5M #type complete TITLE cytochrome c551 [validated] - Pseudomonas mendocina ORGANISM #formal_name Pseudomonas mendocina DATE 13-Jul-1981 #sequence_revision 13-Jul-1981 #text_change 03-Nov-2000 ACCESSIONS A00094 REFERENCE A90266 !$#authors Ambler, R.P.; Wynn, M. !$#journal Biochem. J. (1973) 131:485-498 !$#title The amino acid sequences of cytochromes c-551 from three !1species of Pseudomonas. !$#cross-references MUID:73224976; PMID:4352718 !$#accession A00094 !'##molecule_type protein !'##residues 1-82 ##label AMB !'##experimental_source strain CH110 GENETICS !$#gene nirM CLASSIFICATION #superfamily cytochrome c6; cytochrome c6 homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; oxidative phosphorylation FEATURE !$1-78 #domain cytochrome c6 homology #label CYC\ !$12,15 #binding_site heme (Cys) (covalent) #status !8predicted\ !$16,61 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 82 #molecular-weight 8368 #checksum 8112 SEQUENCE /// ENTRY CCPS5D #type complete TITLE cytochrome c551 - Pseudomonas sp. ORGANISM #formal_name Pseudomonas sp. DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 03-Mar-2000 ACCESSIONS A00095 REFERENCE A94302 !$#authors Ambler, R.P. !$#journal Syst. Zool. (1973) 22:554-565 !$#title Bacterial cytochromes C and molecular evolution. !$#accession A00095 !'##molecule_type protein !'##residues 1-82 ##label AMB !'##experimental_source NCIB 9496, ATCC 13867 CLASSIFICATION #superfamily cytochrome c6; cytochrome c6 homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; oxidative phosphorylation FEATURE !$1-78 #domain cytochrome c6 homology #label CYC\ !$12,15 #binding_site heme (Cys) (covalent) #status !8predicted\ !$16,61 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 82 #molecular-weight 8573 #checksum 9150 SEQUENCE /// ENTRY CCAV5 #type complete TITLE cytochrome c551 - Azotobacter vinelandii ORGANISM #formal_name Azotobacter vinelandii DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 03-Mar-2000 ACCESSIONS A00096 REFERENCE A94302 !$#authors Ambler, R.P. !$#journal Syst. Zool. (1973) 22:554-565 !$#title Bacterial cytochromes C and molecular evolution. !$#accession A00096 !'##molecule_type protein !'##residues 1-82 ##label AMB !'##experimental_source strain O, NCIB 8789, ATCC 12837 CLASSIFICATION #superfamily cytochrome c6; cytochrome c6 homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; oxidative phosphorylation FEATURE !$1-78 #domain cytochrome c6 homology #label CYC\ !$12,15 #binding_site heme (Cys) (covalent) #status !8predicted\ !$16,61 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 82 #molecular-weight 8599 #checksum 7382 SEQUENCE /// ENTRY S32485 #type complete TITLE cytochrome c552 precursor - Hydrogenobacter thermophilus ORGANISM #formal_name Hydrogenobacter thermophilus DATE 06-Jan-1995 #sequence_revision 27-Feb-1997 #text_change 03-Mar-2000 ACCESSIONS S32485; A32226 REFERENCE S32485 !$#authors Sanbongi, Y.; Yang, J.H.; Igarashi, Y.; Kodama, T. !$#journal Eur. J. Biochem. (1991) 198:7-12 !$#title Cloning, nucleotide sequence and expression of the !1cytochrome c-552 gene from Hydrogenobacter thermophilus. !$#cross-references MUID:91249816; PMID:1645652 !$#accession S32485 !'##status preliminary !'##molecule_type DNA !'##residues 1-98 ##label SAN !'##cross-references EMBL:X57735; NID:g43674; PIDN:CAA40902.1; !1PID:g43675 !'##experimental_source strain TK-6 REFERENCE A32226 !$#authors Sanbongi, Y.; Ishii, M.; Igarashi, Y.; Kodama, T. !$#journal J. Bacteriol. (1989) 171:65-69 !$#title Amino acid sequence of cytochrome c-552 from a thermophilic !1hydrogen-oxidizing bacterium, Hydrogenobacter thermophilus. !$#cross-references MUID:89123087; PMID:2536668 !$#accession A32226 !'##molecule_type protein !'##residues 19-98 ##label SA2 !'##experimental_source strain TK-6 FUNCTION !$#description primary electron acceptor for molecular hydrogen activated !1by hydrogenase !$#pathway hydrogen oxidation CLASSIFICATION #superfamily cytochrome c6; cytochrome c6 homology KEYWORDS chromoprotein; electron transfer; heme; iron; metalloprotein FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$17-94 #domain cytochrome c6 homology #label CYC\ !$19-98 #product cytochrome c552 #status experimental #label !8MAT\ !$28,31 #binding_site heme (Cys) (covalent) #status !8predicted\ !$32,77 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 98 #molecular-weight 10431 #checksum 8245 SEQUENCE /// ENTRY S27723 #type complete TITLE cytochrome cytM precursor - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein sll1245 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 17-Apr-1993 #sequence_revision 23-May-1997 #text_change 16-Jun-2000 ACCESSIONS S75611; S27723 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75611 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-128 ##label KAN !'##cross-references EMBL:D90912; GB:AB001339; NID:g1653228; !1PIDN:BAA18172.1; PID:g1653257 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 REFERENCE S27720 !$#authors Malakhov, M.P.; Wada, H.; Los, D.A.; Sakamoto, T.; Murata, !1N. !$#submission submitted to the EMBL Data Library, April 1992 !$#description Structure and expression of the cytM gene, encoding !1cytochrome from synechocystis PCC6803. !$#accession S27723 !'##molecule_type DNA !'##residues 24-128 ##label MAL !'##cross-references EMBL:D10716; NID:g217098; PIDN:BAA01559.1; !1PID:g217102 GENETICS !$#gene cytM CLASSIFICATION #superfamily cytochrome c6; cytochrome c6 homology KEYWORDS chromoprotein; electron transfer; heme; iron; metalloprotein FEATURE !$55-128 #product cytochrome cytM #status predicted #label !8MAT\ !$57-128 #domain cytochrome c6 homology #status atypical !8#label CYC\ !$68,71 #binding_site heme (Cys) (covalent) #status !8predicted\ !$72,108 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 128 #molecular-weight 13823 #checksum 2568 SEQUENCE /// ENTRY CCDV5M #type complete TITLE cytochrome c553 - Desulfovibrio vulgaris (strain Miyazaki) ORGANISM #formal_name Desulfovibrio vulgaris DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 03-Mar-2000 ACCESSIONS A00113 REFERENCE A00113 !$#authors Nakano, K.; Kikumoto, Y.; Yagi, T. !$#journal J. Biol. Chem. (1983) 258:12409-12412 !$#title Amino acid sequence of cytochrome c-553 from Desulfovibrio !1vulgaris Miyazaki. !$#cross-references MUID:84032425; PMID:6313657 !$#accession A00113 !'##molecule_type protein !'##residues 1-79 ##label NAK COMMENT Cytochrome c553 has been reported as the natural electron !1acceptor for a formate dehydrogenase. CLASSIFICATION #superfamily cytochrome c6; cytochrome c6 homology KEYWORDS chromoprotein; electron transfer; heme; iron; metalloprotein FEATURE !$1-76 #domain cytochrome c6 homology #label CYC\ !$10,13 #binding_site heme (Cys) (covalent) #status !8predicted\ !$14,57 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 79 #molecular-weight 8397 #checksum 1930 SEQUENCE /// ENTRY A44752 #type complete TITLE cytochrome c553 precursor - Desulfovibrio vulgaris (strain Hildenborough) ORGANISM #formal_name Desulfovibrio vulgaris DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 03-Mar-2000 ACCESSIONS A44752; A05098 REFERENCE A44752 !$#authors van Rooijen, G.J.H.; Bruschi, M.; Voordouw, G. !$#journal J. Bacteriol. (1989) 171:3575-3578 !$#title Cloning and sequencing of the gene encoding cytochrome C-553 !1from Desulfovibrio vulgaris Hildenborough. !$#cross-references MUID:89255138; PMID:2542232 !$#accession A44752 !'##molecule_type DNA !'##residues 1-103 ##label VAN !'##cross-references EMBL:M27062; NID:g145082; PIDN:AAA23356.1; !1PID:g145083 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE A05098 !$#authors Bruschi, M.; Le Gall, J. !$#journal Biochim. Biophys. Acta (1972) 271:48-60 !$#title c-type cytochromes of Desulfovibrio vulgaris the primary !1structure of cytochrome c-553. !$#cross-references MUID:72218157; PMID:5038698 !$#accession A05098 !'##molecule_type protein !'##residues 25-38,'S',40-42,'G',78-86,'G',87-100,44-63,65-77,'KAM', !1101-103 ##label BRU !'##experimental_source NCIB 8303 !'##note the residues line has been changed based on information from !1reference A44752 COMMENT Cytochrome c553 has been reported as the natural electron !1acceptor for a formate dehydrogenase. CLASSIFICATION #superfamily cytochrome c6; cytochrome c6 homology KEYWORDS chromoprotein; electron transfer; heme; iron; metalloprotein FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-103 #product cytochrome c553 #status experimental #label !8MAT\ !$25-100 #domain cytochrome c6 homology #label CYC\ !$34,37 #binding_site heme (Cys) (covalent) #status !8predicted\ !$38,81 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 103 #molecular-weight 10692 #checksum 3207 SEQUENCE /// ENTRY F71843 #type complete TITLE cytochrome c553 precursor - Helicobacter pylori (strain J99) ORGANISM #formal_name Helicobacter pylori #variety strain J99 DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Mar-2000 ACCESSIONS F71843 REFERENCE A71800 !$#authors Alm, R.A.; Ling, L.S.L.; Moir, D.T.; King, B.L.; Brown, !1E.D.; Doig, P.C.; Smith, D.R.; Noonan, B.; Guild, B.C.; !1deJonge, B.L.; Carmel, G.; Tummino, P.J.; Caruso, A.; !1Uria-Nickelsen, M.; Mills, D.M.; Ives, C.; Gibson, R.; !1Merberg, D.; Mills, S.D.; Jiang, Q.; Taylor, D.E.; Vovis, !1G.F.; Trust, T.J. !$#journal Nature (1999) 397:176-180 !$#title Genomic sequence comparison of two unrelated isolates of the !1human gastric pathogen Helicobacter pylori. !$#cross-references MUID:99120557; PMID:9923682 !$#accession F71843 !'##molecule_type DNA !'##residues 1-96 ##label ARN !'##cross-references GB:AE001542; GB:AE001439; NID:g4155739; !1PIDN:AAD06721.1; PID:g4155742 !'##experimental_source strain J99 GENETICS !$#gene jhp1148 CLASSIFICATION #superfamily cytochrome c6; cytochrome c6 homology KEYWORDS chromoprotein; electron transfer; heme; iron; metalloprotein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-96 #product cytochrome c553 #status predicted #label !8MAT\ !$20-92 #domain cytochrome c6 homology #label CYC\ !$29,32 #binding_site heme (Cys) (covalent) #status !8predicted\ !$33 #binding_site heme iron (His) (axial ligand) #status !8predicted SUMMARY #length 96 #molecular-weight 10354 #checksum 1221 SEQUENCE /// ENTRY C64673 #type complete TITLE cytochrome c553 precursor - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Mar-2000 ACCESSIONS C64673 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession C64673 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-96 ##label TOM !'##cross-references GB:AE000628; GB:AE000511; NID:g2314386; !1PIDN:AAD08272.1; PID:g2314390; TIGR:HP1227 CLASSIFICATION #superfamily cytochrome c6; cytochrome c6 homology KEYWORDS chromoprotein; electron transfer; heme; iron; metalloprotein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-96 #product cytochrome c553 #status predicted #label !8MAT\ !$20-92 #domain cytochrome c6 homology #label CYC\ !$29,32 #binding_site heme (Cys) (covalent) #status !8predicted\ !$33 #binding_site heme iron (His) (axial ligand) #status !8predicted SUMMARY #length 96 #molecular-weight 10346 #checksum 9890 SEQUENCE /// ENTRY A36437 #type complete TITLE flavocytochrome c, heme-containing chain - Chlorobium limicola f.sp. thiosulfatophilum (strain Tassajara) ORGANISM #formal_name Chlorobium limicola f.sp. thiosulfatophilum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS A36437 REFERENCE A36437 !$#authors Van Beeumen, J.; Van Bun, S.; Meyer, T.E.; Bartsch, R.G.; !1Cusanovich, M.A. !$#journal J. Biol. Chem. (1990) 265:9793-9799 !$#title Complete amino acid sequence of the cytochrome subunit and !1amino-terminal sequence of the flavin subunit of !1flavocytochrome c (sulfide dehydrogenase) from Chlorobium !1thiosulfatophilum. !$#cross-references MUID:90277669; PMID:2161842 !$#accession A36437 !'##status preliminary !'##molecule_type protein !'##residues 1-87 ##label VAN CLASSIFICATION #superfamily cytochrome c6; cytochrome c6 homology KEYWORDS chromoprotein; electron transfer; heme; iron; metalloprotein FEATURE !$9-79 #domain cytochrome c6 homology #label CYC\ !$18,21 #binding_site heme (Cys) (covalent) #status !8predicted\ !$22 #binding_site heme iron (His) (axial ligand) #status !8predicted SUMMARY #length 87 #molecular-weight 9351 #checksum 255 SEQUENCE /// ENTRY S31922 #type complete TITLE cytochrome c552, membrane-bound - Paracoccus denitrificans ORGANISM #formal_name Paracoccus denitrificans DATE 06-Jan-1995 #sequence_revision 02-Jul-1996 #text_change 03-Mar-2000 ACCESSIONS S65941; S65915; S31922 REFERENCE S65915 !$#authors Turba, A.; Jetzek, M.; Ludwig, B. !$#journal Eur. J. Biochem. (1995) 231:259-265 !$#title Purification of Paracoccus denitrificans cytochrome c(552) !1and sequence analysis of the gene. !$#cross-references MUID:95354697; PMID:7628479 !$#accession S65941 !'##molecule_type DNA !'##residues 1-176 ##label TUR !'##cross-references EMBL:X70367; NID:g49208; PIDN:CAA49830.1; !1PID:g49209 !'##experimental_source strain PD1235 !$#accession S65915 !'##molecule_type protein !'##residues 66-76;132-139;164-176 ##label TU2 GENETICS !$#gene cycM FUNCTION !$#description electron transfer from the ubiquinol-cytochrome-c reductase !1(bc1) complex to the cytochrome-c oxidase (aa3) complex !1(probable) !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily membrane-bound cytochrome cycM; cytochrome c !1homology KEYWORDS chromoprotein; electron transfer; heme; inner membrane; !1iron; metalloprotein; transmembrane protein FEATURE !$1-9 #domain intracellular #status predicted #label INT\ !$10-26 #domain transmembrane #status predicted #label TMM\ !$27-176 #domain periplasmic #status predicted #label PER\ !$81-172 #domain cytochrome c homology #label CYC\ !$90,93 #binding_site heme (Cys) (covalent) #status !8predicted\ !$94,154 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 176 #molecular-weight 18209 #checksum 2700 SEQUENCE /// ENTRY S31938 #type complete TITLE membrane-bound cytochrome cycY - Rhodobacter capsulatus ORGANISM #formal_name Rhodobacter capsulatus DATE 06-Jan-1995 #sequence_revision 02-Jul-1996 #text_change 03-Mar-2000 ACCESSIONS S31938; S35337 REFERENCE S31938 !$#authors Daldal, F. !$#submission submitted to the EMBL Data Library, February 1993 !$#accession S31938 !'##molecule_type DNA !'##residues 1-199 ##label DAL !'##cross-references EMBL:Z21797; NID:g49366; PIDN:CAA79860.1; !1PID:g49367 REFERENCE S35337 !$#authors Jenney Jr., F.E.; Daldal, F. !$#journal EMBO J. (1993) 12:1283-1292 !$#title A novel membrane-associated c-type cytochrome, cyt c(y), can !1mediate the photosynthetic growth of Rhodobacter capsulatus !1and Rhodobacter sphaeroides. !$#cross-references MUID:93223669; PMID:8385603 !$#accession S35337 !'##molecule_type DNA !'##residues 'MRQPHMPTAGGA',1-199 ##label JEN !'##cross-references EMBL:Z21797 !'##experimental_source strain MT-1131 !'##note it is uncertain which Met is the initiator GENETICS !$#gene cycY FUNCTION !$#description electron transfer from the ubiquinol-cytochrome-c reductase !1(bc1) complex to the photosynthetic reaction center !$#pathway photosynthesis !$#note in this organism, both this protein and cytochrome c2 can !1mediate electron transfer during photosynthesis CLASSIFICATION #superfamily membrane-bound cytochrome cycM; cytochrome c !1homology KEYWORDS chromoprotein; electron transfer; heme; inner membrane; !1iron; metalloprotein; photosynthesis; transmembrane protein FEATURE !$1-9 #domain intracellular #status predicted #label INT\ !$10-26 #domain transmembrane #status predicted #label TMM\ !$27-199 #domain periplasmic #status predicted #label PER\ !$102-194 #domain cytochrome c homology #label CYC\ !$112,115 #binding_site heme (Cys) (covalent) #status !8predicted\ !$116,176 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 199 #molecular-weight 20659 #checksum 2567 SEQUENCE /// ENTRY A41331 #type complete TITLE membrane-bound cytochrome cycM - Bradyrhizobium japonicum ORGANISM #formal_name Bradyrhizobium japonicum DATE 28-May-1992 #sequence_revision 02-Jul-1996 #text_change 03-Mar-2000 ACCESSIONS A41331 REFERENCE A41331 !$#authors Bott, M.; Ritz, D.; Hennecke, H. !$#journal J. Bacteriol. (1991) 173:6766-6772 !$#title The Bradyrhizobium japonicum cycM gene encodes a !1membrane-anchored homolog of mitochondrial cytochrome c. !$#cross-references MUID:92041558; PMID:1657867 !$#accession A41331 !'##molecule_type DNA !'##residues 1-184 ##label BOT !'##cross-references GB:M77189; NID:g152080; PIDN:AAA26198.1; !1PID:g152081 !'##experimental_source strain 110spc4, a spectinomycin-resistant !1derivative of strain 3I1b110 GENETICS !$#gene cycM FUNCTION !$#description electron transfer from the ubiquinol-cytochrome-c reductase !1(bc1) complex to the cytochrome-c oxidase (aa3) complex !1(probable) !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily membrane-bound cytochrome cycM; cytochrome c !1homology KEYWORDS chromoprotein; electron transfer; heme; inner membrane; !1iron; metalloprotein; transmembrane protein FEATURE !$1-8 #domain intracellular #status predicted #label INT\ !$9-25 #domain transmembrane #status predicted #label TMM\ !$26-184 #domain periplasmic #status predicted #label PER\ !$75-169 #domain cytochrome c homology #label CYC\ !$84,87 #binding_site heme (Cys) (covalent) #status !8predicted\ !$88,151 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 184 #molecular-weight 19098 #checksum 4909 SEQUENCE /// ENTRY T46966 #type complete TITLE diheme cytochrome soxD precursor [similarity] - Paracoccus denitrificans ALTERNATE_NAMES cytochrome diheme c-type ORGANISM #formal_name Paracoccus denitrificans DATE 03-Nov-2000 #sequence_revision 03-Nov-2000 #text_change 03-Nov-2000 ACCESSIONS T46966 REFERENCE Z24324 !$#authors Wodara, C.; Bardischewsky, F.; Friedrich, C.G. !$#journal J. Bacteriol. (1997) 179:5014-5023 !$#title Cloning and characterization of sulfite dehydrogenase, two !1c-type cytochromes, and a flavoprotein of Paracoccus !1denitrificans GB17: Essential role of of sulfite !1dehydrogenase in lithotrophic sulfur oxidation. !$#cross-references MUID:97405897; PMID:9260941 !$#accession T46966 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-384 ##label WOD !'##cross-references EMBL:X79242; NID:g2253074; PIDN:CAA55825.1; !1PID:g2222779 !'##experimental_source strain GB17 GENETICS !$#gene soxD FUNCTION !$#description may be a required electron acceptor for soxC sulfite !1dehydrogenase (by analogy with P. versutus) !$#pathway thiosulfate oxidation CLASSIFICATION #superfamily Paracoccus denitrificans diheme cytochrome !1soxD; cytochrome c homology KEYWORDS chromoprotein; electron transfer; heme; iron; metalloprotein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-384 #product c-type cytochrome soxD #status predicted !8#label MAT\ !$283-379 #domain cytochrome c homology #label CYC\ !$70,73 #binding_site heme (Cys) (covalent) #status !8predicted\ !$74,121 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted\ !$292,295 #binding_site heme (Cys) (covalent) #status !8predicted\ !$296,361 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 384 #molecular-weight 39985 #checksum 264 SEQUENCE /// ENTRY CCPS4A #type complete TITLE cytochrome c4 - Pseudomonas aeruginosa ORGANISM #formal_name Pseudomonas aeruginosa DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 03-Mar-2000 ACCESSIONS A00098 REFERENCE A94468 !$#authors Ambler, R. !$#citation unpublished results, cited by Dickerson, R.E., in The !1Evolution of Protein Structure and Function, Sigman, D.S., !1and Brazier, M.A.B., eds., pp.173-202, Academic Press, New !1York and London, 1980 !$#accession A00098 !'##molecule_type protein !'##residues 1-181 ##label AMB COMMENT Cytochrome c4 is a diheme, high potential cytochrome that !1appears to be the result of gene duplication and fusion of a !1smaller monoheme protein similar to Pseudomonas cytochrome !1c551. Although the exact function of c4 is unknown, it is !1produced in significant quantities when P. aeruginosa is !1grown anaerobically. CLASSIFICATION #superfamily cytochrome c4; cytochrome c6 homology KEYWORDS chromoprotein; duplication; electron transfer; heme; iron; !1metalloprotein; oxidative phosphorylation FEATURE !$5-77 #domain cytochrome c6 homology #label CYC1\ !$99-177 #domain cytochrome c6 homology #label CYC2\ !$14,17 #binding_site heme (Cys) (covalent) #status !8predicted\ !$18,58 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted\ !$110,113 #binding_site heme (Cys) (covalent) #status !8predicted\ !$114,157 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 181 #molecular-weight 18598 #checksum 963 SEQUENCE /// ENTRY I39740 #type complete TITLE cytochrome c4 precursor - Azotobacter vinelandii ORGANISM #formal_name Azotobacter vinelandii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS I39740; S56043 REFERENCE I39740 !$#authors Ng, T.C.; Laheri, A.N.; Maier, R.J. !$#journal Biochim. Biophys. Acta (1995) 1230:119-129 !$#title Cloning, sequencing, and mutagenesis of the cytochrome c4 !1gene from Azotobacter vinelandii: characterization of the !1mutant strain and a proposed new branch in the respiratory !1chain. !$#cross-references MUID:95345104; PMID:7619830 !$#accession I39740 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-210 ##label RES !'##cross-references GB:L37290; NID:g600179; PIDN:AAA87314.1; !1PID:g600180 GENETICS !$#gene cycA CLASSIFICATION #superfamily cytochrome c4; cytochrome c6 homology KEYWORDS chromoprotein; duplication; electron transfer; heme; iron; !1metalloprotein; oxidative phosphorylation FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-210 #product cytochrome c4 #status predicted #label MAT\ !$25-105 #domain cytochrome c6 homology #label CYC1\ !$128-206 #domain cytochrome c6 homology #label CYC2\ !$34,37 #binding_site heme (Cys) (covalent) #status !8predicted\ !$38 #binding_site heme iron (His) (axial ligand) #status !8predicted\ !$139,142 #binding_site heme (Cys) (covalent) #status !8predicted\ !$143 #binding_site heme iron (His) (axial ligand) #status !8predicted SUMMARY #length 210 #molecular-weight 21687 #checksum 8899 SEQUENCE /// ENTRY C47169 #type complete TITLE flavocytochrome c, heme-containing chain - Chromatium vinosum ORGANISM #formal_name Chromatium vinosum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS C47169; A39859 REFERENCE A47169 !$#authors Dolata, M.M.; Van Beeumen, J.J.; Ambler, R.P.; Meyer, T.E.; !1Cusanovich, M.A. !$#journal J. Biol. Chem. (1993) 268:14426-14431 !$#title Nucleotide sequence of the heme subunit of flavocytochrome c !1from the purple phototrophic bacterium, Chromatium vinosum. !1A 2.6-kilobase pair DNA fragment contains two multiheme !1cytochromes, a flavoprotein, and a homolog of human ankyrin. !$#cross-references MUID:93300842; PMID:8390993 !$#accession C47169 !'##status preliminary !'##molecule_type DNA !'##residues 1-199 ##label DOL !'##cross-references GB:L13419; NID:g290007; PIDN:AAA23316.1; !1PID:g290010 REFERENCE A39859 !$#authors Van Beeumen, J.J.; Demol, H.; Samyn, B.; Bartsch, R.G.; !1Meyer, T.E.; Dolata, M.M.; Cusanovich, M.A. !$#journal J. Biol. Chem. (1991) 266:12921-12931 !$#title Covalent structure of the diheme cytochrome subunit and !1amino-terminal sequence of the flavoprotein subunit of !1flavocytochrome c from Chromatium vinosum. !$#cross-references MUID:91302306; PMID:1649169 !$#accession A39859 !'##status preliminary !'##molecule_type protein !'##residues 26-199 ##label VAN CLASSIFICATION #superfamily cytochrome c4; cytochrome c6 homology KEYWORDS chromoprotein; duplication; electron transfer; heme; iron; !1metalloprotein; periplasmic space FEATURE !$36,39 #binding_site heme (Cys) (covalent) #status !8predicted\ !$40 #binding_site heme iron (His) (axial ligand) #status !8predicted\ !$126,129 #binding_site heme (Cys) (covalent) #status !8predicted\ !$130 #binding_site heme iron (His) (axial ligand) #status !8predicted SUMMARY #length 199 #molecular-weight 21635 #checksum 4233 SEQUENCE /// ENTRY F75267 #type complete TITLE probable cytochrome c4 - Deinococcus radiodurans (strain R1) ORGANISM #formal_name Deinococcus radiodurans DATE 17-Mar-2000 #sequence_revision 17-Mar-2000 #text_change 17-Mar-2000 ACCESSIONS F75267 REFERENCE A75250 !$#authors White, O.; Eisen, J.A.; Heidelberg, J.F.; Hickey, E.K.; !1Peterson, J.D.; Dodson, R.J.; Haft, D.H.; Gwinn, M.L.; !1Nelson, W.C.; Richardson, D.L.; Moffat, K.S.; Qin, H.; !1Jiang, L.; Pamphile, W.; Crosby, M.; Shen, M.; Vamathevan, !1J.J.; Lam, P.; McDonald, L.; Utterback, T.; Zalewski, C.; !1Makarova, K.S.; Aravind, L.; Daly, M.J.; Minton, K.W.; !1Fleischmann, R.D.; Ketchum, K.A.; Nelson, K.E.; Salzberg, !1S.; Smith, H.O.; Venter, J.C.; Fraser, C.M. !$#journal Science (1999) 286:1571-1577 !$#title Genome sequence of the radioresistant bacterium Deinococcus !1radiodurans R1. !$#cross-references MUID:20036896; PMID:10567266 !$#accession F75267 !'##status preliminary !'##molecule_type DNA !'##residues 1-229 ##label WHI !'##cross-references GB:AE002078; GB:AE000513; NID:g6460306; !1PIDN:AAF12028.1; PID:g6460307; TIGR:DR2487; GSPDB:GN00077 !'##experimental_source strain R1 GENETICS !$#gene DR2487 !$#map_position 1 CLASSIFICATION #superfamily cytochrome c4; cytochrome c6 homology KEYWORDS chromoprotein; duplication; electron transfer; heme; iron; !1metalloprotein FEATURE !$51-122 #domain cytochrome c6 homology #label CYC1\ !$146-225 #domain cytochrome c6 homology #label CYC2\ !$60,63 #binding_site heme (Cys) (covalent) #status !8predicted\ !$64,103 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted\ !$157,160 #binding_site heme (Cys) (covalent) #status !8predicted\ !$161,206 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 229 #molecular-weight 23957 #checksum 9629 SEQUENCE /// ENTRY D55582 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) fixP chain - Azorhizobium caulinodans ALTERNATE_NAMES cb-type cytochrome-c oxidase 32K chain; cytochrome b410; fixP protein ORGANISM #formal_name Azorhizobium caulinodans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS D55582; S42232 REFERENCE A55582 !$#authors Mandon, K.; Kaminski, P.A.; Elmerich, C. !$#journal J. Bacteriol. (1994) 176:2560-2568 !$#title Functional analysis of the fixNOQP region of Azorhizobium !1caulinodans. !$#cross-references MUID:94222833; PMID:8169204 !$#accession D55582 !'##status preliminary; nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-292 ##label MAN !'##cross-references GB:X74410 REFERENCE S42229 !$#authors Mandon, K.; Kaminski, P.A.; Mougel, C.; Desnoues, N.; !1Dreyfus, B.; Elmerich, C. !$#journal FEMS Microbiol. Lett. (1993) 114:185-190 !$#title Role of the fixGHI region of Azorhizobium caulinodans in !1free-living and symbiotic nitrogen fixation. !$#cross-references MUID:94109675; PMID:8282187 !$#accession S42232 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-53,'W',54-292 ##label MA2 !'##cross-references EMBL:X74410; NID:g456310; PIDN:CAA52432.1; !1PID:g580702 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1993 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily Rhizobium cytochrome-c oxidase fixP chain; !1cytochrome c6 homology KEYWORDS chromoprotein; duplication; electron transfer; heme; iron; !1membrane-associated complex; metalloprotein; oxidoreductase; !1respiratory chain FEATURE !$116-196 #domain cytochrome c6 homology #label CYC1\ !$211-285 #domain cytochrome c6 homology #label CYC2\ !$126,129 #binding_site heme (Cys) (covalent) #status !8predicted\ !$130,177 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted\ !$221,224 #binding_site heme (Cys) (covalent) #status !8predicted\ !$225,266 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 292 #molecular-weight 30793 #checksum 8363 SEQUENCE /// ENTRY D47468 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) fixP chain - Bradyrhizobium japonicum ALTERNATE_NAMES cb-type cytochrome-c oxidase 32K chain; cytochrome b410; fixP protein ORGANISM #formal_name Bradyrhizobium japonicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS D47468 REFERENCE A47468 !$#authors Preisig, O.; Anthamatten, D.; Hennecke, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:3309-3313 !$#title Genes for a microaerobically induced oxidase complex in !1Bradyrhizobium japonicum are essential for a nitrogen-fixing !1endosymbiosis. !$#cross-references MUID:93234486; PMID:8386371 !$#accession D47468 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-290 ##label PRE !'##cross-references GB:L07487; NID:g152196; PIDN:AAA26206.1; !1PID:g152202 !'##experimental_source 110spc4 !'##note sequence extracted from NCBI backbone (NCBIP:129656) CLASSIFICATION #superfamily Rhizobium cytochrome-c oxidase fixP chain; !1cytochrome c6 homology KEYWORDS chromoprotein; duplication; electron transfer; heme; iron; !1membrane-associated complex; metalloprotein; oxidoreductase; !1respiratory chain FEATURE !$112-194 #domain cytochrome c6 homology #label CYC1\ !$122,125 #binding_site heme (Cys) (covalent) #status !8predicted\ !$126,173 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted\ !$219,222 #binding_site heme (Cys) (covalent) #status !8predicted\ !$223,264 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 290 #molecular-weight 31024 #checksum 3800 SEQUENCE /// ENTRY S39991 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) fixP chain - Rhizobium meliloti ALTERNATE_NAMES cb-type cytochrome-c oxidase 32K chain; cytochrome b410; fixP protein ORGANISM #formal_name Rhizobium meliloti DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS S39991; S32844 REFERENCE S32837 !$#authors Kahn, D.D. !$#submission submitted to the EMBL Data Library, March 1993 !$#accession S39991 !'##molecule_type DNA !'##residues 1-289 ##label KAH !'##cross-references EMBL:Z21854; NID:g49403; PIDN:CAA79904.1; !1PID:g49411 CLASSIFICATION #superfamily Rhizobium cytochrome-c oxidase fixP chain; !1cytochrome c6 homology KEYWORDS chromoprotein; duplication; electron transfer; heme; iron; !1membrane-associated complex; metalloprotein; oxidoreductase; !1respiratory chain FEATURE !$113-194 #domain cytochrome c6 homology #label CYC1\ !$123,126 #binding_site heme (Cys) (covalent) #status !8predicted\ !$127,175 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted\ !$218,221 #binding_site heme (Cys) (covalent) #status !8predicted\ !$222,263 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 289 #molecular-weight 31097 #checksum 8213 SEQUENCE /// ENTRY S49348 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) fixP chain - Rhodobacter capsulatus ALTERNATE_NAMES cb-type cytochrome-c oxidase 32K chain; ccoP protein; cytochrome b410; fixP protein homolog ORGANISM #formal_name Rhodobacter capsulatus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS S65861; H54235; G54235; I54235; A59014; S49348 REFERENCE S65858 !$#authors Thoeny-Meyer, L.; Beck, C.; Preisig, O.; Hennecke, H. !$#journal Mol. Microbiol. (1994) 14:705-716 !$#title The ccoNOQP gene cluster codes for a cb-type cytochrome !1oxidase that functions in aerobic respiration of Rhodobacter !1capsulatus. !$#cross-references MUID:95198544; PMID:7891558 !$#accession S65861 !'##status preliminary; nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-297 ##label THO !'##cross-references EMBL:X80134; NID:g556812; PIDN:CAA56436.1; !1PID:g556816 REFERENCE A54235 !$#authors Gray, K.A.; Grooms, M.; Myllykallio, H.; Moomaw, C.; !1Slaughter, C.; Daldal, F. !$#journal Biochemistry (1994) 33:3120-3127 !$#title Rhodobacter capsulatus contains a novel cb-type cytochrome c !1oxidase without a CuA center. !$#cross-references MUID:94176508; PMID:8130227 !$#accession H54235 !'##molecule_type protein !'##residues 86-88,'D',90-107 ##label GRA1 !'##experimental_source pMTo-404/MT-RBC1 cells !'##note sequence extracted from NCBI backbone (NCBIP:144522) !$#accession G54235 !'##molecule_type protein !'##residues 'AT',263-266,'X',268,'X',270-274,'X',276 ##label GRA2 !'##experimental_source pMTo-404/MT-RBC1 cells !'##note sequence extracted from NCBI backbone (NCBIP:144520) !$#accession I54235 !'##molecule_type protein !'##residues 285-296,'S' ##label GRA3 !'##experimental_source pMTo-404/MT-RBC1 cells !'##note sequence extracted from NCBI backbone (NCBIP:144524) !$#accession A59014 !'##molecule_type protein !'##residues 91,'M',93-101;251,'I',253,'T',255-256,'SL',259-260 ##label !1GRA4 !'##experimental_source pMTo-404/MT-RBC1 cells GENETICS !$#gene ccoP FUNCTION !$#description this cytochrome-c oxidase complex catalyzes the oxidation of !1four molecules of reduced cytochrome c2 using one oxygen !1molecule and four protons producing two molecules of water !$#pathway respiratory chain CLASSIFICATION #superfamily Rhizobium cytochrome-c oxidase fixP chain; !1cytochrome c6 homology KEYWORDS chromoprotein; duplication; electron transfer; heme; iron; !1membrane-associated complex; metalloprotein; oxidoreductase; !1respiratory chain FEATURE !$209-290 #domain cytochrome c6 homology #label CYC2\ !$121,124 #binding_site heme (Cys) (covalent) #status !8predicted\ !$125,174 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted\ !$219,222 #binding_site heme (Cys) (covalent) #status !8predicted\ !$223,264 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 297 #molecular-weight 31899 #checksum 94 SEQUENCE /// ENTRY C70784 #type complete TITLE probable diheme cytochrome qcrC - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 16-Jun-2000 ACCESSIONS C70784 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession C70784 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-280 ##label COL !'##cross-references GB:Z70283; GB:AL123456; NID:g3261561; !1PIDN:CAA94263.1; PID:g1237047 !'##experimental_source strain H37Rv GENETICS !$#gene qcrC CLASSIFICATION #superfamily Streptomyces coelicolor probable diheme !1cytochrome qcrC; cytochrome c6 homology KEYWORDS chromoprotein; heme; iron; metalloprotein FEATURE !$63-136 #domain cytochrome c6 homology #status atypical !8#label CYC1\ !$164-235 #domain cytochrome c6 homology #label CYC2\ !$73,76 #binding_site heme (Cys) (covalent) #status !8predicted\ !$77 #binding_site heme iron (His) (axial ligand) #status !8predicted\ !$174,177 #binding_site heme (Cys) (covalent) #status !8predicted\ !$178 #binding_site heme iron (His) (axial ligand) #status !8predicted SUMMARY #length 280 #molecular-weight 29138 #checksum 4679 SEQUENCE /// ENTRY T35532 #type complete TITLE probable diheme cytochrome qcrC precursor - Streptomyces coelicolor ORGANISM #formal_name Streptomyces coelicolor DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 19-May-2000 ACCESSIONS T35532 REFERENCE Z21581 !$#authors Seeger, K.; Harris, D.; Bentley, S.D.; Parkhill, J.; !1Barrell, B.G.; Rajandream, M.A. !$#submission submitted to the EMBL Data Library, March 1999 !$#accession T35532 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-269 ##label SEE !'##cross-references EMBL:AL049497; PIDN:CAB39877.1; GSPDB:GN00070; !1SCOEDB:SC6G10.23c !'##experimental_source strain A3(2) GENETICS !$#gene qcrC; SC6G10.23c CLASSIFICATION #superfamily Streptomyces coelicolor probable diheme !1cytochrome qcrC; cytochrome c6 homology KEYWORDS chromoprotein; heme; iron; metalloprotein FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$50-122 #domain cytochrome c6 homology #status atypical !8#label CYC1\ !$145-216 #domain cytochrome c6 homology #label CYC2\ !$60,63 #binding_site heme (Cys) (covalent) #status !8predicted\ !$64 #binding_site heme iron (His) (axial ligand) #status !8predicted\ !$155,158 #binding_site heme (Cys) (covalent) #status !8predicted\ !$159 #binding_site heme iron (His) (axial ligand) #status !8predicted SUMMARY #length 269 #molecular-weight 27526 #checksum 9012 SEQUENCE /// ENTRY T46967 #type complete TITLE diheme cytochrome soxE precursor [similarity] - Paracoccus denitrificans ALTERNATE_NAMES cytochrome monoheme c-type ORGANISM #formal_name Paracoccus denitrificans DATE 03-Nov-2000 #sequence_revision 03-Nov-2000 #text_change 03-Nov-2000 ACCESSIONS T46967 REFERENCE Z24324 !$#authors Wodara, C.; Bardischewsky, F.; Friedrich, C.G. !$#journal J. Bacteriol. (1997) 179:5014-5023 !$#title Cloning and characterization of sulfite dehydrogenase, two !1c-type cytochromes, and a flavoprotein of Paracoccus !1denitrificans GB17: Essential role of of sulfite !1dehydrogenase in lithotrophic sulfur oxidation. !$#cross-references MUID:97405897; PMID:9260941 !$#accession T46967 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-236 ##label WOD !'##cross-references EMBL:X79242; NID:g2253074; PIDN:CAA55828.1; !1PID:g2253075 !'##experimental_source strain GB17 GENETICS !$#gene soxE CLASSIFICATION #superfamily Paracoccus denitrificans diheme cytochrome !1soxE; cytochrome c homology; cytochrome c6 homology KEYWORDS chromoprotein; electron transfer; heme; iron; metalloprotein FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-236 #product c-type cytochrome soxE #status predicted !8#label MAT\ !$30-127 #domain cytochrome c homology #label CYC\ !$163-232 #domain cytochrome c6 homology #label CY6\ !$40,43 #binding_site heme (Cys) (covalent) #status !8predicted\ !$44,109 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted\ !$172,175 #binding_site heme (Cys) (covalent) #status !8predicted\ !$176,213 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 236 #molecular-weight 25844 #checksum 9741 SEQUENCE /// ENTRY B41377 #type complete TITLE cytochrome c-L precursor [validated] - Paracoccus denitrificans ALTERNATE_NAMES cytochrome c551i; cytochrome c552; moxG protein ORGANISM #formal_name Paracoccus denitrificans DATE 28-May-1992 #sequence_revision 02-Jul-1996 #text_change 15-Sep-2000 ACCESSIONS B41377 REFERENCE A41377 !$#authors Van Spanning, R.J.M.; Wansell, C.W.; De Boer, T.; Hazelaar, !1M.J.; Anazawa, H.; Harms, N.; Oltmann, L.F.; Stouthamer, !1A.H. !$#journal J. Bacteriol. (1991) 173:6948-6961 !$#title Isolation and characterization of the moxJ, moxG, moxI, and !1moxR genes of Paracoccus denitrificans: inactivation of !1moxJ, moxG, and moxR and the resultant effect on !1methylotrophic growth. !$#cross-references MUID:92041581; PMID:1657871 !$#accession B41377 !'##molecule_type DNA !'##residues 1-177 ##label VAN !'##cross-references GB:M57684; NID:g150589; PIDN:AAA25583.1; !1PID:g150591 REFERENCE A57985 !$#authors Chen, L.; Durley, R.C.E.; Matthews, F.S.; Davidson, V.L. !$#journal Science (1994) 264:86-90 !$#title Structure of an electron transfer complex: methylamine !1dehydrogenase, amicyanin, and cytochrome c-551i. !$#cross-references MUID:94188715; PMID:8140419 !$#contents annotation; X-ray crystallography, 2.4 angstroms, residues !123-177 REFERENCE A52094 !$#authors Chen, L.; Mathews, F.S. !$#submission submitted to the Brookhaven Protein Data Bank, October 1993 !$#cross-references PDB:2MTA !$#contents annotation; X-ray crystallography, 2.4 angstroms, residues !123-169 GENETICS !$#gene moxG COMPLEX associates in a heterotetramer with methylamine !1dehydrogenase large and small chains and amicyanin to form a !1soluble electron transfer chain; the complex forms a dimer !1in crystals FUNCTION !$#description electron acceptor for methanol dehydrogenase; can also !1accept an electron transferred to amicyanin from methylamine !1dehydrogenase; electron donor to cytochrome-c oxidase !$#pathway methanol oxidation; methylamine oxidation CLASSIFICATION #superfamily cytochrome c-L; cytochrome c6 homology KEYWORDS chromoprotein; electron transfer; heme; heterotetramer; !1iron; metalloprotein; periplasmic space FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-177 #product cytochrome c-L #status experimental #label !8MAT\ !$69-142 #domain cytochrome c6 homology #label CY6\ !$79,82 #binding_site heme (Cys) (covalent) #status !8experimental\ !$83,123 #binding_site heme iron (His, Met) (axial ligands) !8#status experimental SUMMARY #length 177 #molecular-weight 19396 #checksum 5176 SEQUENCE /// ENTRY S01249 #type complete TITLE cytochrome c-L precursor - Methylobacterium sp. ORGANISM #formal_name Methylobacterium sp. DATE 30-Sep-1989 #sequence_revision 02-Jul-1996 #text_change 21-Jul-2000 ACCESSIONS S01249; S02658 REFERENCE S01249 !$#authors Nunn, D.N.; Anthony, C. !$#journal Nucleic Acids Res. (1988) 16:7722 !$#title The nucleotide sequence and deduced amino acid sequence of !1the genes for cytochrome cL and a hypothetical second !1subunit of the methanol dehydrogenase of Methylobacterium !1AM1. !$#cross-references MUID:88319960; PMID:2842733 !$#accession S01249 !'##molecule_type DNA !'##residues 1-197 ##label NUN1 !'##cross-references EMBL:X07856; NID:g44527; PIDN:CAA30704.1; !1PID:g44528 REFERENCE S02658 !$#authors Nunn, D.N.; Anthony, C. !$#journal Biochem. J. (1988) 256:673-676 !$#title The nucleotide sequence and deduced amino acid sequence of !1the cytochrome c(L) gene of Methylobacterium extorquens AM1, !1a novel class of c-type cytochrome. !$#cross-references MUID:89134152; PMID:2851998 !$#accession S02658 !'##molecule_type DNA !'##residues 1-197 ##label NUN2 !'##note source designated as Methylobacterium extorquens AM1 !'##note part of this sequence was confirmed by protein sequencing GENETICS !$#gene moxG FUNCTION !$#description electron acceptor for methanol dehydrogenase; electron donor !1to cytochrome-c oxidase !$#pathway methanol oxidation CLASSIFICATION #superfamily cytochrome c-L; cytochrome c6 homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; periplasmic space FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-197 #product cytochrome c-L #status predicted #label MAT\ !$80-153 #domain cytochrome c6 homology #label CY6\ !$90,93 #binding_site heme (Cys) (covalent) #status !8predicted\ !$94,134 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 197 #molecular-weight 21226 #checksum 3155 SEQUENCE /// ENTRY A45079 #type complete TITLE photosynthetic reaction center cytochrome c551 - Chlorobium vibrioforme ALTERNATE_NAMES photosynthetic reaction center complex 18K protein ORGANISM #formal_name Chlorobium vibrioforme DATE 10-Jun-1993 #sequence_revision 02-Jul-1996 #text_change 03-Mar-2000 ACCESSIONS A45079 REFERENCE A45079 !$#authors Okkels, J.S.; Kjaer, B.; Hansson, O.; Svendsen, I.; Moller, !1B.L.; Scheller, H.V. !$#journal J. Biol. Chem. (1992) 267:21139-21145 !$#title A membrane-bound monoheme cytochrome c551 of a novel type is !1the immediate electron donor to P840 of the Chlorobium !1vibrioforme photosynthetic reaction center complex. !$#cross-references MUID:93016035; PMID:1383218 !$#accession A45079 !'##molecule_type DNA; protein !'##residues 1-206 ##label OKK !'##cross-references GB:M95751; NID:g144472; PIDN:AAA23110.1; !1PID:g144473 !'##experimental_source f. thiosulfatophilum 8327 !'##note sequence extracted from NCBI backbone (NCBIN:116201, !1NCBIP:116202) !'##note part of this sequence, including the amino end of the mature !1protein, confirmed by protein sequencing !'##note authors predicted the Met axial ligand based on its predicted !1location on the periplasmic side of the membrane GENETICS !$#gene cycA COMPLEX tightly bound to the photosynthetic reaction center complex FUNCTION !$#description electron donor to photooxidized P840 of the photosynthetic !1reaction center complex CLASSIFICATION #superfamily Chlorobium photosynthetic reaction center !1cytochrome c551 KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; photosynthesis; transmembrane protein FEATURE !$1-206 #product photosynthetic reaction center cytochrome !8c551 #status experimental #label MAT\ !$1-9 #domain intracellular #status predicted #label INT\ !$10-32 #domain transmembrane #status predicted #label TM1\ !$33-48 #domain periplasmic #status predicted #label PER1\ !$49-67 #domain transmembrane #status predicted #label TM2\ !$78-95 #domain transmembrane #status predicted #label TM3\ !$96-206 #domain periplasmic #status predicted #label PER2\ !$152,155 #binding_site heme (Cys) (covalent) #status !8predicted\ !$156,182 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 206 #molecular-weight 22858 #checksum 5363 SEQUENCE /// ENTRY S00680 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome c1 precursor - human ALTERNATE_NAMES bc1 complex cytochrome c1; complex III cytochrome c1; cytochrome c1 heme protein ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1989 #sequence_revision 15-Oct-1994 #text_change 03-Jun-2002 ACCESSIONS A31481; S00680; A29720 REFERENCE A31481 !$#authors Suzuki, H.; Hosokawa, Y.; Nishikimi, M.; Ozawa, T. !$#journal J. Biol. Chem. (1989) 264:1368-1374 !$#title Structural organization of the human mitochondrial !1cytochrome c-1 gene. !$#cross-references MUID:89109139; PMID:2536365 !$#accession A31481 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-325 ##label SUZ !'##cross-references GB:J04444 REFERENCE S00680 !$#authors Nishikimi, M.; Ohta, S.; Suzuki, H.; Tanaka, T.; Kikkawa, !1F.; Tanaka, M.; Kagawa, Y.; Ozawa, T. !$#journal Nucleic Acids Res. (1988) 16:3577 !$#title Nucleotide sequence of a cDNA encoding the precursor to !1human cytochrome c1. !$#cross-references MUID:88233946; PMID:2836796 !$#accession S00680 !'##molecule_type mRNA !'##residues 1-325 ##label NIS1 !'##cross-references EMBL:X06994; NID:g30302; PIDN:CAA30052.1; !1PID:g30303 REFERENCE A29720 !$#authors Nishikimi, M.; Suzuki, H.; Ohta, S.; Sakurai, T.; Shimomura, !1Y.; Tanaka, M.; Kagawa, Y.; Ozawa, T. !$#journal Biochem. Biophys. Res. Commun. (1987) 145:34-39 !$#title Isolation of a cDNA clone for human cytochrome c1 from a !1lambda-gt11 expression library. !$#cross-references MUID:87241521; PMID:3036122 !$#accession A29720 !'##molecule_type mRNA !'##residues 99-325 ##label NIS2 !'##cross-references GB:M16597; NID:g181237; PIDN:AAA35730.1; !1PID:g181238 GENETICS !$#gene GDB:CYC1 !'##cross-references GDB:119827; OMIM:123980 !$#map_position 8q24.3-8q24.3 !$#introns 43/3; 109/2; 151/3; 202/2; 258/1; 291/3 COMPLEX the transmembrane complex includes cytochrome b (see !1PIR:CBHU), cytochrome c1, Rieske iron-sulfur protein, and !1other accessory proteins CLASSIFICATION #superfamily cytochrome c1 heme protein; cytochrome c1 heme !1protein homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$1-84 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$85-325 #product cytochrome c1 #status predicted #label MAT\ !$90-315 #domain cytochrome c1 heme protein homology #label !8C1H\ !$288-306 #domain transmembrane #status predicted #label TMM\ !$121,124 #binding_site heme (Cys) (covalent) #status !8predicted\ !$125,244 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 325 #molecular-weight 35376 #checksum 3779 SEQUENCE /// ENTRY CCBO1 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome c1 - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Mar-1981 #sequence_revision 31-Mar-1981 #text_change 03-Jun-2002 ACCESSIONS A00118 REFERENCE A00118 !$#authors Wakabayashi, S.; Matsubara, H.; Kim, C.H.; King, T.E. !$#journal J. Biol. Chem. (1982) 257:9335-9344 !$#title Structural studies of bovine heart cytochrome c-1. !$#cross-references MUID:82265565; PMID:6286615 !$#accession A00118 !'##molecule_type protein !'##residues 1-241 ##label WAK COMMENT This is the heme-containing component of the cytochrome c1 !1complex, which is located in the inner membrane of the !1mitochondrion and functions as electron donor to cytochrome !1c in the mitochondrial respiratory chain. COMPLEX the transmembrane complex includes cytochrome b (see !1PIR:CBBO), cytochrome c1, Rieske iron-sulfur protein (see !1PIR:A34660), and other accessory proteins (see PIR:CCBO11, !1PIR:CCBO17, PIR:A24864, PIR:ZPBOC1, and PIR:ZPBOC2) CLASSIFICATION #superfamily cytochrome c1 heme protein; cytochrome c1 heme !1protein homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$6-231 #domain cytochrome c1 heme protein homology #label !8C1H\ !$203-222 #domain transmembrane #status predicted #label TMM\ !$37,40 #binding_site heme (Cys) (covalent) #status !8experimental\ !$41,160 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 241 #molecular-weight 27287 #checksum 4108 SEQUENCE /// ENTRY JQ0347 #type complete TITLE cytochrome c1 - Rhodopseudomonas viridis ORGANISM #formal_name Rhodopseudomonas viridis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS JQ0347 REFERENCE JQ0345 !$#authors Verbist, J.; Lang, F.; Gabellini, N.; Oesterhelt, D. !$#journal Mol. Gen. Genet. (1989) 219:445-452 !$#title Cloning and sequencing of the fbcF, B and C genes encoding !1the cytochrome b/c1 complex from Rhodopseudomonas viridis. !$#cross-references MUID:90158506; PMID:2560136 !$#accession JQ0347 !'##molecule_type DNA !'##residues 1-282 ##label VER !'##experimental_source strain 133 COMMENT This protein is one of the three subunits of the !1ubiquinol-cytochrome C2 oxidoreductase complex which is !1coupled with another membrane-protein complex at the !1reaction center in a cyclic electron-transport system which !1catalyzes the synthesis of ATP. GENETICS !$#gene fbcC CLASSIFICATION #superfamily cytochrome c1 heme protein; cytochrome c1 heme !1protein homology KEYWORDS chromoprotein; electron transfer; heme; iron; metalloprotein FEATURE !$31-278 #domain cytochrome c1 heme protein homology #label !8C1H\ !$62,65 #binding_site heme (Cys) (covalent) #status !8predicted\ !$66,207 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 282 #molecular-weight 31262 #checksum 1181 SEQUENCE /// ENTRY CCBY1H #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome c1 precursor - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein O2816; protein YOR065w ORGANISM #formal_name Saccharomyces cerevisiae DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 03-Jun-2002 ACCESSIONS A22737; S66948; A26500 REFERENCE A90992 !$#authors Sadler, I.; Suda, K.; Schatz, G.; Kaudewitz, F.; Haid, A. !$#journal EMBO J. (1984) 3:2137-2143 !$#title Sequencing of the nuclear gene for the yeast cytochrome c1 !1precursor reveals an unusually complex amino-terminal !1presequence. !$#cross-references MUID:85027167; PMID:6092058 !$#accession A22737 !'##molecule_type DNA !'##residues 1-309 ##label SAD !'##cross-references EMBL:X00791; NID:g1197521; PIDN:CAA25375.1; !1PID:g3610 REFERENCE S66929 !$#authors Bohn, C.; Bolotin-Fukuhara, M.; Daignan-Fornier, B.; Dang, !1D.V.; Valens, M. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S66948 !'##molecule_type DNA !'##residues 1-309 ##label BOH !'##cross-references EMBL:Z74973; NID:g1420210; PIDN:CAA99258.1; !1PID:g1420211; GSPDB:GN00015; MIPS:YOR065w !'##experimental_source strain S288C GENETICS !$#gene SGD:CYT1; CTC1; MIPS:YOR065w !'##cross-references SGD:S0005591; MIPS:YOR065w !$#map_position 15R !$#genome nuclear CLASSIFICATION #superfamily cytochrome c1 heme protein; cytochrome c1 heme !1protein homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$1-61 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$62-309 #product cytochrome c1 #status predicted #label MAT\ !$70-296 #domain cytochrome c1 heme protein homology #label !8C1H\ !$269-286 #domain transmembrane #status predicted #label TMM\ !$101,104 #binding_site heme (Cys) (covalent) #status !8predicted\ !$105,225 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 309 #molecular-weight 34054 #checksum 2924 SEQUENCE /// ENTRY A27187 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome c1 precursor - Neurospora crassa ALTERNATE_NAMES bc1 complex cytochrome c1; complex III cytochrome c1; cytochrome c1 heme protein ORGANISM #formal_name Neurospora crassa DATE 05-Oct-1988 #sequence_revision 15-Oct-1994 #text_change 03-Jun-2002 ACCESSIONS A27187 REFERENCE A27187 !$#authors Roemisch, J.; Tropschug, M.; Sebald, W.; Weiss, H. !$#journal Eur. J. Biochem. (1987) 164:111-115 !$#title The primary structure of cytochrome c-1 from Neurospora !1crassa. !$#cross-references MUID:87161871; PMID:3030747 !$#accession A27187 !'##molecule_type mRNA !'##residues 1-332 ##label ROE !'##cross-references GB:X05235; NID:g3005; PIDN:CAA28860.1; PID:g3006 !'##note the authors translated the codon AGT for residue 316 as Arg CLASSIFICATION #superfamily cytochrome c1 heme protein; cytochrome c1 heme !1protein homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$1-70 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$71-332 #product cytochrome c1 #status predicted #label MAT\ !$79-305 #domain cytochrome c1 heme protein homology #label !8C1H\ !$278-296 #domain transmembrane #status predicted #label TMM\ !$110,113 #binding_site heme (Cys) (covalent) #status !8predicted\ !$114,234 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 332 #molecular-weight 36456 #checksum 1753 SEQUENCE /// ENTRY S20014 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome c1 precursor (clone pC(1)3II) - potato ALTERNATE_NAMES bc1 complex cytochrome c1; complex III cytochrome c1; cytochrome c1 heme protein ORGANISM #formal_name Solanum tuberosum #common_name potato DATE 16-Sep-1992 #sequence_revision 15-Oct-1994 #text_change 03-Jun-2002 ACCESSIONS S20014; S21975; S36371 REFERENCE S20014 !$#authors Braun, H.P.; Emmermann, M.; Kruft, V.; Schmitz, U.K. !$#journal Mol. Gen. Genet. (1992) 231:217-225 !$#title Cytochrome c(1) from potato: a protein with a presequence !1for targeting to the mitochondrial intermembrane space. !$#cross-references MUID:92140360; PMID:1310521 !$#accession S20014 !'##molecule_type mRNA !'##residues 1-320 ##label BRA !'##cross-references EMBL:X62124 REFERENCE S21974 !$#authors Schmitz, U. !$#submission submitted to the EMBL Data Library, September 1991 !$#accession S21975 !'##molecule_type DNA !'##residues 1-211,'A',213-320 ##label SCH !'##cross-references EMBL:X62124; NID:g21438; PIDN:CAA44055.1; !1PID:g21439 REFERENCE S36371 !$#authors Wegener, S.; Schmitz, U.K. !$#journal Curr. Genet. (1993) 24:256-259 !$#title The presequence of cytochrome c(1) from potato mitochondria !1is encoded on four exons. !$#cross-references MUID:94037151; PMID:8221935 !$#accession S36371 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-87,'S',89-201,'N',203-320 ##label WEG !'##cross-references GB:S66866; NID:g440952; PIDN:AAB28813.1; !1PID:g440953 GENETICS !$#gene cyc1 !$#genome nuclear !$#introns 2/1; 13/1; 42/1; 104/2; 197/3; 221/3; 269/3; 282/3 CLASSIFICATION #superfamily cytochrome c1 heme protein; cytochrome c1 heme !1protein homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$1-77 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$78-320 #product cytochrome c1 #status predicted #label MAT\ !$85-310 #domain cytochrome c1 heme protein homology #label !8C1H\ !$282-301 #domain transmembrane #status predicted #label TMM\ !$116,119 #binding_site heme (Cys) (covalent) #status !8predicted\ !$120,239 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 320 #molecular-weight 35145 #checksum 4648 SEQUENCE /// ENTRY JQ0021 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome c1 - Euglena gracilis ALTERNATE_NAMES complex III polypeptide IV; ubiquinol-cytochrome-c reductase polypeptide IV ORGANISM #formal_name Euglena gracilis DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 03-Jun-2002 ACCESSIONS JQ0021; S02075 REFERENCE JQ0021 !$#authors Mukai, K.; Wakabayashi, S.; Matsubara, H. !$#journal J. Biochem. (1989) 106:479-482 !$#title Molecular cloning and nucleotide sequence of a cDNA encoding !1Euglena gracilis cytochrome c1. !$#cross-references MUID:90110031; PMID:2558110 !$#accession JQ0021 !'##molecule_type mRNA !'##residues 1-243 ##label MUK !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE S02075 !$#authors Mukai, K.; Yoshida, M.; Toyosaki, H.; Yao, Y.; Wakabayashi, !1S.; Matsubara, H. !$#journal Eur. J. Biochem. (1989) 178:649-656 !$#title An atypical heme-binding structure of cytochrome c1 of !1Euglena gracilis mitochondrial complex III. !$#cross-references MUID:89107187; PMID:2536325 !$#accession S02075 !'##molecule_type protein !'##residues 1-46 ##label MU2 COMMENT Cytochrome c1 is a subunit of the cytochrome bc1 complex, !1which is one of the oligomeric enzymes in the respiratory !1chain of the mitochondrial inner membrane. CLASSIFICATION #superfamily cytochrome c1 heme protein; cytochrome c1 heme !1protein homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$1-243 #product ubiquinol-cytochrome-c reductase cytochrome !8c1 #status experimental #label MAT\ !$5-233 #domain cytochrome c1 heme protein homology #label !8C1H\ !$57-74,165-172 #region cytochrome c binding #status predicted\ !$207-221 #domain transmembrane #status predicted #label TMM\ !$39 #binding_site heme (Cys) (covalent) #status !8experimental\ !$40,159 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 243 #molecular-weight 27855 #checksum 6699 SEQUENCE /// ENTRY CCQF1R #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome c1 precursor - Rhodospirillum rubrum ORGANISM #formal_name Rhodospirillum rubrum DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 03-Jun-2002 ACCESSIONS S12258; A38815 REFERENCE S12255 !$#authors Majewski, C.; Trebst, A. !$#journal Mol. Gen. Genet. (1990) 224:373-382 !$#title The pet genes of Rhodospirillum rubrum: cloning and !1sequencing of the genes for the cytochrome bc(1)-complex. !$#cross-references MUID:91094774; PMID:2176269 !$#accession S12258 !'##molecule_type DNA !'##residues 1-272 ##label MA1 !'##cross-references EMBL:X55387; NID:g46382; PIDN:CAA39060.1; !1PID:g46386 !'##note the authors translated the codon CCG for residue 111 as Thr, !1GCC for residue 112 as Pro, and GAC for residue 113 as Ala !$#accession A38815 !'##molecule_type protein !'##residues 25-50 ##label MA2 GENETICS !$#gene petC CLASSIFICATION #superfamily cytochrome c1 heme protein; cytochrome c1 heme !1protein homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; oxidoreductase; transmembrane protein FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-272 #product cytochrome c1 #status experimental #label !8MAT\ !$30-271 #domain cytochrome c1 heme protein homology #label !8C1H\ !$244-261 #domain transmembrane #status predicted #label TMM\ !$61,64 #binding_site heme (Cys) (covalent) #status !8predicted\ !$65,200 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 272 #molecular-weight 29494 #checksum 2350 SEQUENCE /// ENTRY C25405 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome c1 precursor - Rhodobacter capsulatus (strain GA) ORGANISM #formal_name Rhodobacter capsulatus DATE 05-Oct-1988 #sequence_revision 22-Jul-1994 #text_change 03-Jun-2002 ACCESSIONS C25405; E25405 REFERENCE A91162 !$#authors Gabellini, N.; Sebald, W. !$#journal Eur. J. Biochem. (1986) 154:569-579 !$#title Nucleotide sequence and transcription of the fbc operon from !1Rhodopseudomonas sphaeroides. Evaluation of the deduced !1amino acid sequences of the FeS protein, cytochrome b and !1cytochrome c-1. !$#cross-references MUID:86136096; PMID:3004982 !$#note source is designated as Rhodopseudomonas sphaeroides !$#accession C25405 !'##molecule_type DNA !'##residues 1-280 ##label GAB1 !'##cross-references GB:X03476; NID:g46007; PIDN:CAA27196.1; PID:g46010 !$#accession E25405 !'##molecule_type protein !'##residues 22-39 ##label GAB2 GENETICS !$#gene fbcC; petC CLASSIFICATION #superfamily cytochrome c1 heme protein; cytochrome c1 heme !1protein homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-280 #product cytochrome c1 #status experimental #label !8MAT\ !$24-276 #domain cytochrome c1 heme protein homology #label !8C1H\ !$249-266 #domain transmembrane #status predicted #label TMM\ !$55,58 #binding_site heme (Cys) (covalent) #status !8predicted\ !$59,205 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 280 #molecular-weight 30382 #checksum 7129 SEQUENCE /// ENTRY C29336 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome c1 precursor - Rhodobacter capsulatus (strain SB 1003) ORGANISM #formal_name Rhodobacter capsulatus #variety strain SB 1003 DATE 31-Dec-1988 #sequence_revision 22-Jul-1994 #text_change 03-Jun-2002 ACCESSIONS C29336 REFERENCE A92938 !$#authors Davidson, E.; Daldal, F. !$#journal J. Mol. Biol. (1987) 195:13-24 !$#title Primary structure of the bc-1 complex of Rhodopseudomonas !1capsulata. Nucleotide sequence of the pet operon encoding !1the Rieske, cytochrome b, and cytochrome c-1 apoproteins. !$#cross-references MUID:88011223; PMID:2821268 !$#accession C29336 !'##molecule_type DNA !'##residues 1-279 ##label DAV !'##cross-references EMBL:X05630; NID:g46093; PIDN:CAA29118.1; !1PID:g46096 GENETICS !$#gene fbcC; petC CLASSIFICATION #superfamily cytochrome c1 heme protein; cytochrome c1 heme !1protein homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-279 #product cytochrome c1 #status predicted #label MAT\ !$24-275 #domain cytochrome c1 heme protein homology #label !8C1H\ !$248-265 #domain transmembrane #status predicted #label TMM\ !$55,58 #binding_site heme (Cys) (covalent) #status !8predicted\ !$59,204 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 279 #molecular-weight 30321 #checksum 1261 SEQUENCE /// ENTRY S13870 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome c1 precursor - Rhodobacter sphaeroides ORGANISM #formal_name Rhodobacter sphaeroides DATE 31-Dec-1988 #sequence_revision 22-Jul-1994 #text_change 03-Jun-2002 ACCESSIONS S13870; B34591; A34935 REFERENCE S13868 !$#authors Yun, C.H.; Beci, R.; Crofts, A.R.; Kaplan, S.; Gennis, R.B. !$#journal Eur. J. Biochem. (1990) 194:399-411 !$#title Cloning and DNA sequencing of the fbc operon encoding the !1cytochrome bc(1) complex from Rhodobacter sphaeroides. !1Characterization of fbc deletion mutants and complementation !1by a site-specific mutational variant. !$#cross-references MUID:91099313; PMID:2176595 !$#accession S13870 !'##molecule_type DNA !'##residues 1-285 ##label YUN !'##cross-references EMBL:X56157; NID:g46425; PIDN:CAA39625.1; !1PID:g46428 !'##note the authors translated the codon CGG for residue 49 as Glu and !1GCA for residue 59 as Ser !'##note the sequence from Fig. 6 is inconsistent with that from Fig. 2 !1in lacking 27-His and having 120-Pro REFERENCE A34591 !$#authors Andrews, K.M.; Crofts, A.R.; Gennis, R.B. !$#journal Biochemistry (1990) 29:2645-2651 !$#title Large-scale purification and characterization of a highly !1active four-subunit cytochrome bc-1 complex from Rhodobacter !1sphaeroides. !$#cross-references MUID:90268011; PMID:2161250 !$#accession B34591 !'##molecule_type protein !'##residues 23-42 ##label AND REFERENCE A34935 !$#authors Purvis, D.J.; Theiler, R.; Niederman, R.A. !$#journal J. Biol. Chem. (1990) 265:1208-1215 !$#title Chromatographic and protein chemical analysis of the !1ubiquinol-cytochrome c-2 oxidoreductase isolated from !1Rhodobacter sphaeroides. !$#cross-references MUID:90110107; PMID:2153104 !$#accession A34935 !'##molecule_type protein !'##residues 66-70,'T',72,'T',74-79,'X',81-82,'XX',85 ##label PUR GENETICS !$#gene fbcC COMPLEX In this organism, ubiquinol-cytochrome-c reductase consists !1of cytochrome b, cytochrome c1, a Rieske iron-sulfur !1protein, and a 14K polypeptide. FUNCTION !$#description electron transfer from dihydroquinol to cytochrome c2 !$#pathway respiratory chain CLASSIFICATION #superfamily cytochrome c1 heme protein; cytochrome c1 heme !1protein homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-285 #product cytochrome c1 #status experimental #label !8MAT\ !$27-278 #domain cytochrome c1 heme protein homology #label !8C1H\ !$251-268 #domain transmembrane #status predicted #label TMM\ !$58,61 #binding_site heme (Cys) (covalent) #status !8predicted\ !$62,207 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 285 #molecular-weight 30603 #checksum 6199 SEQUENCE /// ENTRY C29413 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome c1 precursor - Paracoccus denitrificans ALTERNATE_NAMES bc1 complex cytochrome c1; complex III cytochrome c1; cytochrome c1 heme protein ORGANISM #formal_name Paracoccus denitrificans DATE 31-Mar-1989 #sequence_revision 15-Oct-1994 #text_change 03-Jun-2002 ACCESSIONS C29413 REFERENCE A92613 !$#authors Kurowski, B.; Ludwig, B. !$#journal J. Biol. Chem. (1987) 262:13805-13811 !$#title The genes of the Paracoccus denitrificans bc-1 complex. !1Nucleotide sequence and homologies between bacterial and !1mitochondrial subunits. !$#cross-references MUID:88007612; PMID:2820981 !$#accession C29413 !'##molecule_type DNA !'##residues 1-450 ##label KUR !'##cross-references GB:M17522; NID:g150569; PIDN:AAA25573.1; !1PID:g150572 CLASSIFICATION #superfamily Paracoccus cytochrome c1 heme protein; !1cytochrome c1 heme protein homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1membrane-associated complex; metalloprotein; oxidoreductase; !1transmembrane protein FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-450 #product cytochrome c1 #status predicted #label MAT\ !$214-444 #domain cytochrome c1 heme protein homology #label !8C1H\ !$417-433 #domain transmembrane #status predicted #label TMM\ !$245,248 #binding_site heme (Cys) (covalent) #status !8predicted\ !$249,373 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 450 #molecular-weight 46874 #checksum 7859 SEQUENCE /// ENTRY CCPS2S #type complete TITLE cytochrome c552 precursor - Pseudomonas stutzeri ORGANISM #formal_name Pseudomonas stutzeri DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Mar-2000 ACCESSIONS S13938; S03857 REFERENCE S13613 !$#authors Juengst, A.; Wakabayashi, S.; Matsubara, H.; Zumft, W.G. !$#journal FEBS Lett. (1991) 279:205-209 !$#title The nirSTBM region coding for cytochrome cd(1)-dependent !1nitrite respiration of Pseudomonas stutzeri consists of a !1cluster of mono-, di-, and tetraheme proteins. !$#cross-references MUID:91160715; PMID:2001732 !$#accession S13938 !'##molecule_type DNA !'##residues 1-291 ##label JUE !'##cross-references EMBL:X56813; NID:g45838; PIDN:CAA40152.1; !1PID:g45841 REFERENCE S03857 !$#authors Denariaz, C.M.; Liu, M.Y.; Payne, W.J.; LeGall, J.; Marquez, !1L.; Dunford, H.B.; van Beeumen, J. !$#journal Arch. Biochem. Biophys. (1989) 270:114-125 !$#title Cytochrome c peroxidase activity of a protease-modified form !1of cytochrome c-552 from the denitrifying bacterium !1Pseudomonas perfectomarina. !$#cross-references MUID:89192360; PMID:2539041 !$#accession S03857 !'##molecule_type protein !'##residues 24-58,'D',60-228,'N',230-267,'S',269,'N' ##label DEN !'##note the source is designated as Pseudomonas perfectomarina GENETICS !$#gene nirB CLASSIFICATION #superfamily cytochrome c552 KEYWORDS chromoprotein; electron transfer; heme; iron; metalloprotein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-291 #product cytochrome c552 #status experimental #label !8MAT\ !$68,71 #binding_site heme (Cys) (covalent) #status !8predicted\ !$72 #binding_site heme iron (His) (axial ligand) #status !8predicted\ !$157,161 #binding_site heme (Cys) (covalent) #status !8predicted\ !$162 #binding_site heme iron (His) (axial ligand) #status !8predicted SUMMARY #length 291 #molecular-weight 30426 #checksum 9282 SEQUENCE /// ENTRY O4PSZ #type complete TITLE denitrification system component nirT precursor - Pseudomonas stutzeri ALTERNATE_NAMES membrane-bound tetraheme cytochrome ORGANISM #formal_name Pseudomonas stutzeri DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Mar-2000 ACCESSIONS S13937 REFERENCE S13613 !$#authors Juengst, A.; Wakabayashi, S.; Matsubara, H.; Zumft, W.G. !$#journal FEBS Lett. (1991) 279:205-209 !$#title The nirSTBM region coding for cytochrome cd(1)-dependent !1nitrite respiration of Pseudomonas stutzeri consists of a !1cluster of mono-, di-, and tetraheme proteins. !$#cross-references MUID:91160715; PMID:2001732 !$#accession S13937 !'##molecule_type DNA !'##residues 1-201 ##label JUE !'##cross-references EMBL:X56813; NID:g45838; PIDN:CAA40151.1; !1PID:g45840 GENETICS !$#gene nirT CLASSIFICATION #superfamily denitrification system component nirT; nirT !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; transmembrane protein FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$19-193 #domain nirT homology #label NIRT\ !$29-201 #product denitrification system component nirT !8#status predicted #label MAT\ !$29-45 #domain transmembrane #status predicted #label TMM\ !$58,61 #binding_site heme (Cys) (covalent) #status !8predicted\ !$62 #binding_site heme iron (His) (axial ligand) #status !8predicted\ !$88,91 #binding_site heme (Cys) (covalent) #status !8predicted\ !$92 #binding_site heme iron (His) (axial ligand) #status !8predicted\ !$148,151 #binding_site heme (Cys) (covalent) #status !8predicted\ !$152 #binding_site heme iron (His) (axial ligand) #status !8predicted\ !$180,183 #binding_site heme (Cys) (covalent) #status !8predicted\ !$184 #binding_site heme iron (His) (axial ligand) #status !8predicted SUMMARY #length 201 #molecular-weight 22825 #checksum 1611 SEQUENCE /// ENTRY S56137 #type complete TITLE membrane-bound tetraheme cytochrome napC - Thiosphaera pantotropha ALTERNATE_NAMES cytochrome c, tetraheme ORGANISM #formal_name Thiosphaera pantotropha DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS S56137; S50165 REFERENCE S56128 !$#authors Berks, B.C.; Richardson, D.J.; Reilly, A.; Willis, A.C.; !1Ferguson, S.J. !$#journal Biochem. J. (1995) 309:983-992 !$#title The napEDABC gene cluster encoding the periplasmic nitrate !1reductase system of Thiosphaera pantotropha. !$#cross-references MUID:95366980; PMID:7639719 !$#accession S56137 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-237 ##label BER !'##cross-references EMBL:Z36773; NID:g600089; PIDN:CAA85348.1; !1PID:g600095 GENETICS !$#gene napC CLASSIFICATION #superfamily denitrification system component nirT; nirT !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; transmembrane protein FEATURE !$23-198 #domain nirT homology #label NIRT\ !$29-49 #domain transmembrane #status predicted #label TMM\ !$62,65 #binding_site heme (Cys) (covalent) #status !8predicted\ !$66 #binding_site heme iron (His) (axial ligand) #status !8predicted\ !$92,95 #binding_site heme (Cys) (covalent) #status !8predicted\ !$96 #binding_site heme iron (His) (axial ligand) #status !8predicted\ !$152,155 #binding_site heme (Cys) (covalent) #status !8predicted\ !$156 #binding_site heme iron (His) (axial ligand) #status !8predicted\ !$185,188 #binding_site heme (Cys) (covalent) #status !8predicted\ !$189 #binding_site heme iron (His) (axial ligand) #status !8predicted SUMMARY #length 237 #molecular-weight 27236 #checksum 826 SEQUENCE /// ENTRY H64062 #type complete TITLE membrane-bound tetraheme cytochrome nirT - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES denitrification system component nirT ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS H64062 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession H64062 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-200 ##label TIGR !'##cross-references GB:U32719; GB:L42023; NID:g1573310; !1PIDN:AAC22009.1; PID:g1573318; TIGR:HI0348 !'##note named as homolog to a protein from Pseudomonas stutzeri GENETICS !$#gene nirT CLASSIFICATION #superfamily denitrification system component nirT; nirT !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; transmembrane protein FEATURE !$17-188 #domain nirT homology #label NIRT\ !$22-42 #domain transmembrane #status predicted #label TMM\ !$55,58 #binding_site heme (Cys) (covalent) #status !8predicted\ !$59 #binding_site heme iron (His) (axial ligand) #status !8predicted\ !$83,86 #binding_site heme (Cys) (covalent) #status !8predicted\ !$87 #binding_site heme iron (His) (axial ligand) #status !8predicted\ !$143,146 #binding_site heme (Cys) (covalent) #status !8predicted\ !$147 #binding_site heme iron (His) (axial ligand) #status !8predicted\ !$175,178 #binding_site heme (Cys) (covalent) #status !8predicted\ !$179 #binding_site heme iron (His) (axial ligand) #status !8predicted SUMMARY #length 200 #molecular-weight 22957 #checksum 8324 SEQUENCE /// ENTRY S34221 #type complete TITLE membrane-bound tetraheme cytochrome torC - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 06-Jan-1995 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS B64841; S43697; S34221 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64841 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-390 ##label BLAT !'##cross-references GB:AE000201; GB:U00096; NID:g2367113; !1PIDN:AAC74081.1; PID:g1787230; UWGP:b0996 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S43697 !$#authors Mejean, V.; Iobbi-Nivol, C.; Lepelletier, M.; Giordano, G.; !1Chippaux, M.; Pascal, M.C. !$#journal Mol. Microbiol. (1994) 11:1169-1179 !$#title TMAO anaerobic respiration in Escherichia coli: involvement !1of the tor operon. !$#cross-references MUID:94293785; PMID:8022286 !$#accession S43697 !'##status preliminary !'##molecule_type DNA !'##residues 1-72,'CELN',77-193,'DV',196-390 ##label ME2 !'##cross-references EMBL:X73888; NID:g556701; PIDN:CAA52094.1; !1PID:g556702 !'##experimental_source strain K-12 GENETICS !$#gene torC FUNCTION !$#description electron transfer !$#pathway trimethylamine N-oxide respiratory chain CLASSIFICATION #superfamily membrane-bound tetraheme cytochrome torC; nirT !1homology KEYWORDS chromoprotein; electron transfer; heme; inner membrane; !1iron; metalloprotein; transmembrane protein FEATURE !$1-16 #domain intracellular #status predicted #label INT\ !$9-183 #domain nirT homology #label NIRT\ !$17-33 #domain transmembrane #status predicted #label TMM\ !$34-390 #domain periplasmic #status predicted #label PER\ !$48,51 #binding_site heme (Cys) (covalent) #status !8predicted\ !$52 #binding_site heme iron (His) (axial ligand) #status !8predicted\ !$77,80 #binding_site heme (Cys) (covalent) #status !8predicted\ !$81 #binding_site heme iron (His) (axial ligand) #status !8predicted\ !$138,141 #binding_site heme (Cys) (covalent) #status !8predicted\ !$142 #binding_site heme iron (His) (axial ligand) #status !8predicted\ !$170,173 #binding_site heme (Cys) (covalent) #status !8predicted\ !$174 #binding_site heme iron (His) (axial ligand) #status !8predicted\ !$329,332 #binding_site heme (Cys) (covalent) #status !8predicted\ !$333 #binding_site heme iron (His) (axial ligand) #status !8predicted SUMMARY #length 390 #molecular-weight 43606 #checksum 6641 SEQUENCE /// ENTRY I64083 #type complete TITLE membrane-bound tetraheme cytochrome torC - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 18-Aug-1995 #sequence_revision 26-Jul-1996 #text_change 03-Mar-2000 ACCESSIONS I64083 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession I64083 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-368 ##label TIGR !'##cross-references GB:U32747; GB:L42023; NID:g1573635; !1PIDN:AAC22304.1; PID:g1573642; TIGR:HI0644 !'##note named as homolog to a protein from Escherichia coli GENETICS !$#gene torC !$#start_codon GTG FUNCTION !$#description electron transfer !$#pathway trimethylamine N-oxide respiratory chain CLASSIFICATION #superfamily membrane-bound tetraheme cytochrome torC; nirT !1homology KEYWORDS chromoprotein; electron transfer; heme; inner membrane; !1iron; metalloprotein; transmembrane protein FEATURE !$1-8 #domain intracellular #status predicted #label INT\ !$7-173 #domain nirT homology #label NIRT\ !$9-25 #domain transmembrane #status predicted #label TMM\ !$26-368 #domain periplasmic #status predicted #label PER\ !$39,42 #binding_site heme (Cys) (covalent) #status !8predicted\ !$43 #binding_site heme iron (His) (axial ligand) #status !8predicted\ !$68,71 #binding_site heme (Cys) (covalent) #status !8predicted\ !$72 #binding_site heme iron (His) (axial ligand) #status !8predicted\ !$128,131 #binding_site heme (Cys) (covalent) #status !8predicted\ !$132 #binding_site heme iron (His) (axial ligand) #status !8predicted\ !$160,163 #binding_site heme (Cys) (covalent) #status !8predicted\ !$164 #binding_site heme iron (His) (axial ligand) #status !8predicted\ !$316,319 #binding_site heme (Cys) (covalent) #status !8predicted\ !$320 #binding_site heme iron (His) (axial ligand) #status !8predicted SUMMARY #length 368 #molecular-weight 41145 #checksum 8322 SEQUENCE /// ENTRY A39303 #type complete TITLE cytochrome c554 precursor - Chloroflexus aurantiacus ORGANISM #formal_name Chloroflexus aurantiacus DATE 03-Aug-1992 #sequence_revision 02-Jul-1996 #text_change 03-Mar-2000 ACCESSIONS A39303; I40619; S34211 REFERENCE A39303 !$#authors Dracheva, S.; Williams, J.C.; Van Driessche, G.; Van !1Beeumen, J.J.; Blankenship, R.E. !$#journal Biochemistry (1991) 30:11451-11458 !$#title The primary structure of cytochrome c-554 from the green !1photosynthetic bacterium Chloroflexus aurantiacus. !$#cross-references MUID:92075661; PMID:1660302 !$#accession A39303 !'##molecule_type DNA !'##residues 1-414 ##label DRA !'##cross-references GB:M77813; NID:g144448; PIDN:AAA23100.1; !1PID:g144449 !'##note part of this sequence was confirmed by protein sequencing REFERENCE I40617 !$#authors Watanabe, Y.; Feick, R.G.; Shiozawa, J.A. !$#journal Arch. Microbiol. (1995) 163:124-130 !$#title Cloning and sequencing of the genes encoding the !1light-harvesting B806-866 polypeptides and initial studies !1on the transcriptional organization of puf2B, puf2A and !1puf2C in Chloroflexus aurantiacus. !$#cross-references MUID:95225715; PMID:7535995 !$#accession I40619 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-51 ##label RES !'##cross-references EMBL:X73899; NID:g313697; PIDN:CAA52106.1; !1PID:g313700 FUNCTION !$#description immediate electron donor to the oxidized bacteriochlorophyll !1dimer (BChl2) CLASSIFICATION #superfamily cytochrome c554 KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; periplasmic space; photosynthesis FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-414 #product cytochrome c554 #status predicted #label !8MAT\ !$119,135 #binding_site heme iron (Met, His) (axial ligands) !8#status predicted\ !$131,134 #binding_site heme (Cys) (covalent) #status !8predicted\ !$154,183 #binding_site heme iron (Met, His) (axial ligands) !8#status predicted\ !$179,182 #binding_site heme (Cys) (covalent) #status !8predicted\ !$283,298 #binding_site heme iron (Met, His) (axial ligands) !8#status predicted\ !$294,297 #binding_site heme (Cys) (covalent) #status !8predicted\ !$330,382 #binding_site heme iron (Met, His) (axial ligands) !8#status predicted\ !$378,381 #binding_site heme (Cys) (covalent) #status !8experimental SUMMARY #length 414 #molecular-weight 45593 #checksum 467 SEQUENCE /// ENTRY A59036 #type complete TITLE cytochrome c554, tetraheme, precursor - Nitrosomonas europaea ALTERNATE_NAMES hydroxylamine oxidoreductase-linked cytochrome c554 ORGANISM #formal_name Nitrosomonas europaea DATE 23-Apr-1999 #sequence_revision 23-Apr-1999 #text_change 23-Mar-2001 ACCESSIONS A59036; A59037 REFERENCE A59036 !$#authors Hommes, N.G.; Sayavedra-Soto, L.A.; Arp, D.J. !$#journal Gene (1994) 146:87-89 !$#title Sequence of hcy, a gene encoding cytochrome c-554 from !1Nitrosomonas europaea. !$#cross-references MUID:94341575; PMID:8063110 !$#accession A59036 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-235 ##label HOM !'##cross-references GB:U05951; NID:g454393; PIDN:AAA60464.1; !1PID:g454394 !'##note submitted to GenBank, January 1994 REFERENCE A59037 !$#authors Bergmann, D.J.; Arciero, D.M.; Hooper, A.B. !$#journal J. Bacteriol. (1994) 176:3148-3153 !$#title Organization of the hao gene cluster of Nitrosomonas !1europaea: genes for two tetraheme c-cytochromes. !$#cross-references MUID:94252980; PMID:8195067 !$#accession A59037 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-235 ##label BER !'##cross-references GB:U08288; NID:g476339; PIDN:AAA19967.1; !1PID:g476340 !'##note submitted to GenBank, April 1994 REFERENCE A58952 !$#authors Iverson, T.M.; Arciero, D.M.; Hsu, B.T.; Logan, M.S.P.; !1Hooper, A.B.; Rees, D.C. !$#journal Nat. Struct. Biol. (1998) 5:1005-1012 !$#title Heme packing motifs revealed by the crystal structure of the !1tetra-heme cytochrome c554 from Nitrosomonas europaea. !$#cross-references MUID:99023199; PDB:1BVB; PMID:9808046 !$#contents annotation; X-ray crystallography, 2.6 angstroms !$#note the His-126 is a ligand through the 3'-nitrogen COMMENT For hydroxylamine oxidase, see PIR:A36954. GENETICS !$#gene hcy; cycA !$#note there are at least three copies of this gene, two of which !1may have identical amino acid sequences FUNCTION !$#description transfers two electrons from hydroxylamine oxidase to two !1molecules of cytochrome c552 CLASSIFICATION #superfamily Nitrosomonas cytochrome c554 KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; periplasmic space FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-235 #product cytochrome c554, tetraheme #status !8experimental #label MAT\ !$35,38 #binding_site heme (Cys) (covalent) #status !8experimental\ !$39,126 #binding_site heme iron (His) (axial ligands) #status !8experimental\ !$51,162 #binding_site heme iron (His) (axial ligands) #status !8experimental\ !$84,87 #binding_site heme (Cys) (covalent) #status !8experimental\ !$88 #binding_site heme iron (His) (axial ligand) #status !8experimental\ !$112,115 #binding_site heme (Cys) (covalent) #status !8experimental\ !$116,203 #binding_site heme iron (His) (axial ligands) #status !8experimental\ !$158,161 #binding_site heme (Cys) (covalent) #status !8experimental SUMMARY #length 235 #molecular-weight 25999 #checksum 4845 SEQUENCE /// ENTRY S00139 #type complete TITLE photosynthetic reaction center cytochrome precursor [validated] - Rhodopseudomonas viridis ORGANISM #formal_name Rhodopseudomonas viridis DATE 07-Sep-1990 #sequence_revision 19-Jul-1996 #text_change 15-Sep-2000 ACCESSIONS S00139 REFERENCE S00139 !$#authors Weyer, K.A.; Lottspeich, F.; Gruenberg, H.; Lang, F.; !1Oesterhelt, D.; Michel, H. !$#journal EMBO J. (1987) 6:2197-2202 !$#title Amino acid sequence of the cytochrome subunit of the !1photosynthetic reaction centre from the purple bacterium !1Rhodopseudomonas viridis. !$#accession S00139 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-356 ##label WEY !'##cross-references EMBL:X05768; NID:g46474; PIDN:CAA29223.1; !1PID:g758274 !'##note parts of this sequence, including the amino and carboxyl ends !1of the mature protein, were confirmed by protein sequencing REFERENCE A44772 !$#authors Weyer, K.A.; Schaefer, W.; Lottspeich, F.; Michel, H. !$#journal Biochemistry (1987) 26:2909-2914 !$#title The cytochrome subunit of the photosynthetic reaction center !1from Rhodopseudomonas viridis is a lipoprotein. !$#contents annotation !$#note in the mature form the amino-terminal cysteine has a free !1alpha-amino group REFERENCE A30621 !$#authors Deisenhofer, J.; Michel, H. !$#journal Science (1989) 245:1463-1473 !$#title The photosynthetic reaction center from the purple bacterium !1Rhodopseudomonas viridis. !$#contents annotation; X-ray crytallography of the reaction center, 2.3 !1angstroms REFERENCE A50321 !$#authors Deisenhofer, J.; Epp, O.; Miki, K.; Huber, R.; Michel, H. !$#submission submitted to the Brookhaven Protein Data Bank, February 1988 !$#cross-references PDB:1PRC !$#contents annotation; X-ray crystallography, 2.3 angstroms, residues !121-352 GENETICS !$#gene pufC COMPLEX the photosynthetic reaction center is a heterotetramer of H !1(see PIR:A22841), L (see PIR:A25102), M (see PIR:B25102), !1and cytochrome chains FUNCTION !$#description reduces photo-oxidized bacteriochlorophyll b !$#pathway photosynthesis CLASSIFICATION #superfamily photosynthetic reaction center cytochrome KEYWORDS blocked amino end; chromoprotein; electron transfer; heme; !1heterotetramer; iron; lipoprotein; membrane protein; !1metalloprotein; photosynthesis FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-356 #product photosynthetic reaction center cytochrome !8#status experimental #label MAT\ !$21 #binding_site sn-2,3-diacylglycerol (Cys) (covalent) !8#status experimental\ !$21 #modified_site fatty acylated amino end (Cys) (in !8mature form) #status absent\ !$107,110 #binding_site heme (Cys) (covalent) #status !8experimental\ !$111 #binding_site heme iron (His) (axial ligand) #status !8experimental\ !$152,155 #binding_site heme (Cys) (covalent) #status !8experimental\ !$156 #binding_site heme iron (His) (axial ligand) #status !8experimental\ !$264,267 #binding_site heme (Cys) (covalent) #status !8experimental\ !$268 #binding_site heme iron (His) (axial ligand) #status !8experimental\ !$325,328 #binding_site heme (Cys) (covalent) #status !8experimental\ !$329 #binding_site heme iron (His) (axial ligand) #status !8experimental SUMMARY #length 356 #molecular-weight 39371 #checksum 990 SEQUENCE /// ENTRY G49964 #type complete TITLE photosynthetic reaction center cytochrome precursor - Rhodocyclus gelatinosus ORGANISM #formal_name Rhodocyclus gelatinosus DATE 06-Oct-1994 #sequence_revision 19-Jul-1996 #text_change 16-Jun-2000 ACCESSIONS G49964 REFERENCE A49964 !$#authors Nagashima, K.V.; Matsuura, K.; Ohyama, S.; Shimada, K. !$#journal J. Biol. Chem. (1994) 269:2477-2484 !$#title Primary structure and transcription of genes encoding B870 !1and photosynthetic reaction center apoproteins from !1Rubrivivax gelatinosus. !$#cross-references MUID:94132007; PMID:8300574 !$#accession G49964 !'##molecule_type DNA !'##residues 1-366 ##label NAG !'##cross-references GB:D16822; NID:g464211; PIDN:BAA04102.1; !1PID:g533363 !'##note sequence extracted from NCBI backbone (NCBIN:143423, !1NCBIP:143430) !'##note source designated as Rubrivivax gelatinosus GENETICS !$#gene pufC COMPLEX in this organism the photosynthetic reaction center is a !1heterotetramer of H, L (see PIR:E49964), M (see PIR:F49964), !1and cytochrome chains. FUNCTION !$#description re-reduces photo-oxidized bacteriochlorophyll b !$#pathway photosynthesis CLASSIFICATION #superfamily photosynthetic reaction center cytochrome KEYWORDS blocked amino end; chromoprotein; electron transfer; heme; !1iron; lipoprotein; membrane protein; metalloprotein; !1photosynthesis FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-366 #product photosynthetic reaction center cytochrome !8#status predicted #label MAT\ !$23 #binding_site sn-2,3-diacylglycerol (Cys) (covalent) !8#status predicted\ !$23 #modified_site fatty acylated amino end (Cys) (in !8mature form) #status predicted\ !$107,110 #binding_site heme (Cys) (covalent) #status !8predicted\ !$111 #binding_site heme iron (His) (axial ligand) #status !8predicted\ !$151,154 #binding_site heme (Cys) (covalent) #status !8predicted\ !$155 #binding_site heme iron (His) (axial ligand) #status !8predicted\ !$249,252 #binding_site heme (Cys) (covalent) #status !8predicted\ !$253 #binding_site heme iron (His) (axial ligand) #status !8predicted\ !$309,312 #binding_site heme (Cys) (covalent) #status !8predicted\ !$313 #binding_site heme iron (His) (axial ligand) #status !8predicted SUMMARY #length 366 #molecular-weight 39195 #checksum 9519 SEQUENCE /// ENTRY S14271 #type complete TITLE membrane-bound alcohol dehydrogenase (EC 1.1.-.-) cytochrome c precursor - Acetobacter polyoxogenes ALTERNATE_NAMES membrane-bound alcohol dehydrogenase 44K chain ORGANISM #formal_name Acetobacter polyoxogenes #variety strain NBI1028 DATE 21-Nov-1993 #sequence_revision 09-Aug-1996 #text_change 17-Nov-2000 ACCESSIONS S14271 REFERENCE S14270 !$#authors Tamaki, T.; Fukaya, M.; Takemura, H.; Tayama, K.; Okumura, !1H.; Kawamura, Y.; Nishiyama, M.; Horinouchi, S.; Beppu, T. !$#journal Biochim. Biophys. Acta (1991) 1088:292-300 !$#title Cloning and sequencing of the gene cluster encoding two !1subunits of membrane-bound alcohol dehydrogenase from !1Acetobacter polyoxogenes. !$#cross-references MUID:91159482; PMID:2001402 !$#accession S14271 !'##molecule_type DNA !'##residues 1-468 ##label TAM !'##cross-references GB:D00635; NID:g216185; PIDN:BAA00529.1; !1PID:g216187 !'##experimental_source strain NBI1028 COMPLEX heterodimer of 72K and 44K (cytochrome c) chains CLASSIFICATION #superfamily membrane-bound alcohol dehydrogenase cytochrome !1c; cytochrome c6 homology KEYWORDS alcohol metabolism; blocked amino end; chromoprotein; !1electron transfer; heme; iron; membrane protein; !1metalloprotein; oxidoreductase FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-468 #product membrane-bound alcohol dehydrogenase !8cytochrome c chain #status predicted #label MAT\ !$320-403 #domain cytochrome c6 homology #label CY6\ !$45,48 #binding_site heme (Cys) (covalent) #status !8predicted\ !$49 #binding_site heme iron (His) (axial ligand) #status !8predicted\ !$193,196 #binding_site heme (Cys) (covalent) #status !8predicted\ !$197 #binding_site heme iron (His) (axial ligand) #status !8predicted\ !$330,333 #binding_site heme (Cys) (covalent) #status !8predicted\ !$334 #binding_site heme iron (His) (axial ligand) #status !8predicted SUMMARY #length 468 #molecular-weight 49758 #checksum 6109 SEQUENCE /// ENTRY B49340 #type complete TITLE membrane-bound alcohol dehydrogenase (EC 1.1.-.-) cytochrome c precursor - Acetobacter pasteurianus ALTERNATE_NAMES membrane-bound alcohol dehydrogenase 44K chain ORGANISM #formal_name Acetobacter pasteurianus DATE 07-Apr-1994 #sequence_revision 09-Aug-1996 #text_change 17-Nov-2000 ACCESSIONS B49340 REFERENCE A49340 !$#authors Takemura, H.; Kondo, K.; Horinouchi, S.; Beppu, T. !$#journal J. Bacteriol. (1993) 175:6857-6866 !$#title Induction by ethanol of alcohol dehydrogenase activity in !1Acetobacter pasteurianus. !$#cross-references MUID:94042848; PMID:8226628 !$#accession B49340 !'##status preliminary !'##molecule_type DNA !'##residues 1-472 ##label TAK !'##cross-references GB:D13893; NID:g517067; PIDN:BAA02993.1; !1PID:g452587 !'##experimental_source strain NCI1380 COMPLEX heterodimer of 72K and 44K (cytochrome c) chains CLASSIFICATION #superfamily membrane-bound alcohol dehydrogenase cytochrome !1c; cytochrome c6 homology KEYWORDS alcohol metabolism; blocked amino end; chromoprotein; !1electron transfer; heme; iron; membrane protein; !1metalloprotein; oxidoreductase FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-472 #product membrane-bound alcohol dehydrogenase !8cytochrome c chain #status predicted #label MAT\ !$321-404 #domain cytochrome c6 homology #label CY6\ !$46,49 #binding_site heme (Cys) (covalent) #status !8predicted\ !$50 #binding_site heme iron (His) (axial ligand) #status !8predicted\ !$194,197 #binding_site heme (Cys) (covalent) #status !8predicted\ !$198 #binding_site heme iron (His) (axial ligand) #status !8predicted\ !$331,334 #binding_site heme (Cys) (covalent) #status !8predicted\ !$335 #binding_site heme iron (His) (axial ligand) #status !8predicted SUMMARY #length 472 #molecular-weight 50568 #checksum 9813 SEQUENCE /// ENTRY S00219 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) 11K protein precursor - human ALTERNATE_NAMES complex III 11K protein; cytochrome bc1 complex 11K protein; mitochondrial hinge protein ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1988 #sequence_revision 22-Jul-1994 #text_change 03-Jun-2002 ACCESSIONS S00219; I52694 REFERENCE S00219 !$#authors Ohta, S.; Goto, K.; Arai, H.; Kagawa, Y. !$#journal FEBS Lett. (1987) 226:171-175 !$#title An extremely acidic amino-terminal presequence of the !1precursor for the human mitochondrial hinge protein. !$#cross-references MUID:88083627; PMID:2826252 !$#accession S00219 !'##molecule_type mRNA !'##residues 1-91 ##label OHT !'##cross-references EMBL:M36647; NID:g188564; PIDN:AAA36317.1; !1PID:g188565 REFERENCE I52694 !$#authors Liu, A.Y.; Bradner, R.C. !$#journal Cancer Res. (1993) 53:2460-2465 !$#title Elevated expression of the human mitochondrial hinge protein !1gene in cancer. !$#cross-references MUID:93265436; PMID:7684318 !$#accession I52694 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-56 ##label RES !'##cross-references GB:S61826; NID:g385936; PIDN:AAD13930.1; !1PID:g4261630 GENETICS !$#gene GDB:UQCRH !'##cross-references GDB:141852 !$#map_position 22q13-22q13 CLASSIFICATION #superfamily ubiquinol-cytochrome-c reductase 11K protein; !1ubiquinol-cytochrome-c reductase 11K protein homology KEYWORDS mitochondrion; oxidative phosphorylation; oxidoreductase; !1respiratory chain FEATURE !$1-13 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$14-91 #product ubiquinol-cytochrome-c reductase 11K protein !8#status predicted #label MAT\ !$23-91 #domain ubiquinol-cytochrome-c reductase 11K protein !8homology #label U11\ !$37-81,53-67 #disulfide_bonds #status predicted SUMMARY #length 91 #molecular-weight 10755 #checksum 6291 SEQUENCE /// ENTRY CCBO11 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) 11K protein - bovine ALTERNATE_NAMES cytochrome bc1 complex 11Kprotein; mitochondrial hinge protein ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 18-Apr-1984 #sequence_revision 18-Apr-1984 #text_change 03-Jun-2002 ACCESSIONS A00119 REFERENCE A00119 !$#authors Wakabayashi, S.; Takeda, H.; Matsubara, H.; Kim, C.H.; King, !1T.E. !$#journal J. Biochem. (1982) 91:2077-2085 !$#title Identity of the heme-not-containing protein in bovine heart !1cytochrome c-1 preparation with the protein mediating c-1-c !1complex formation-a protein with high glutamic acid content. !$#cross-references MUID:83007120; PMID:6126477 !$#accession A00119 !'##molecule_type protein !'##residues 1-78 ##label WAK REFERENCE A37438 !$#authors Mukai, K.; Miyazaki, T.; Wakabayashi, S.; Kuramitsu, S.; !1Matsubara, H. !$#journal J. Biochem. (1985) 98:1417-1425 !$#title Dissociation of bovine cytochrome c-1 subcomplex and the !1status of cysteine residues in the subunits. !$#cross-references MUID:86111722; PMID:3003044 !$#contents annotation; disulfide bonds COMMENT This is one of the nonheme components of the cytochrome c1 !1complex, which is located in the inner membrane of the !1mitochondrion and functions as electron donor to cytochrome !1c in the mitochondrial respiratory chain. This protein may !1mediate formation of the complex between cytochromes c and !1c1. CLASSIFICATION #superfamily ubiquinol-cytochrome-c reductase 11K protein; !1ubiquinol-cytochrome-c reductase 11K protein homology KEYWORDS mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain FEATURE !$10-78 #domain ubiquinol-cytochrome-c reductase 11K protein !8homology #label U11\ !$24-68,40-54 #disulfide_bonds #status experimental SUMMARY #length 78 #molecular-weight 9175 #checksum 1704 SEQUENCE /// ENTRY S48690 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) 11K protein - potato ORGANISM #formal_name Solanum tuberosum #common_name potato DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S48690; S55873; S45021 REFERENCE S48690 !$#authors Braun, H.P.; Jaensch, L.; Kruft, V.; Schmitz, U.K. !$#journal FEBS Lett. (1994) 347:90-94 !$#title The 'Hinge' protein of cytochrome c reductase from potato !1lacks the acidic domain and has no cleavable presequence. !$#cross-references MUID:94283637; PMID:8013669 !$#accession S48690 !'##molecule_type mRNA !'##residues 1-69 ##label BRA1 !'##cross-references EMBL:X79273; NID:g488711; PIDN:CAA55860.1; !1PID:g488712 !$#accession S55873 !'##molecule_type protein !'##residues 2-16,'X',18-19 ##label BRA2 GENETICS !$#genome nuclear CLASSIFICATION #superfamily ubiquinol-cytochrome-c reductase 11K protein; !1ubiquinol-cytochrome-c reductase 11K protein homology KEYWORDS mitochondrion; oxidative phosphorylation; oxidoreductase; !1respiratory chain FEATURE !$2-69 #product ubiquinol-cytochrome-c reductase #status !8experimental #label MAT\ !$3-69 #domain ubiquinol-cytochrome-c reductase 11K protein !8homology #label U11\ !$17-59,21-55,31-45 #disulfide_bonds #status predicted SUMMARY #length 69 #molecular-weight 7977 #checksum 580 SEQUENCE /// ENTRY RDBYUC #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) 17K protein - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein R014; protein YFR033c; ubiquinol-cytochrome-c reductase chain VI ORGANISM #formal_name Saccharomyces cerevisiae DATE 25-Feb-1985 #sequence_revision 19-Oct-1995 #text_change 03-Jun-2002 ACCESSIONS S56288; A00120; S62244; S63838 REFERENCE S56186 !$#authors Murakami, Y.; Naitou, M.; Hagiwara, H.; Shibata, T.; Ozawa, !1M.; Sasanuma, S.I.; Sasanuma, M.; Tsuchiya, Y.; Soeda, E.; !1Yokoyama, K.; Yamazaki, M.; Tashiro, H.; Eki, T. !$#submission submitted to the EMBL Data Library, May 1995 !$#description Analysis of the nucleotide sequence of chromosome VI from !1Saccaromyces cerevisiae. !$#accession S56288 !'##molecule_type DNA !'##residues 1-147 ##label MUR !'##cross-references EMBL:D50617; NID:g836685; PIDN:BAA09272.1; !1PID:g836788; GSPDB:GN00006; MIPS:YFR033c REFERENCE A00120 !$#authors Van Loon, A.P.G.M.; De Groot, R.J.; De Haan, M.; Dekker, A.; !1Grivell, L.A. !$#journal EMBO J. (1984) 3:1039-1043 !$#title Amino acid sequence homology among fructose-1, !16-bisphosphates. !$#cross-references MUID:84236098; PMID:6329732 !$#accession A00120 !'##molecule_type DNA !'##residues 1,'D',3-147 ##label VAN !'##cross-references EMBL:X00551; NID:g3597; PIDN:CAA25220.1; PID:g3598 !'##experimental_source strain FL100 REFERENCE S62230 !$#authors Murakami, Y. !$#submission submitted to the EMBL Data Library, December 1994 !$#accession S62244 !'##molecule_type DNA !'##residues 1-147 ##label MUW !'##cross-references EMBL:D44602; NID:g893419; PIDN:BAA08044.1; !1PID:g893428 REFERENCE S63830 !$#authors Eki, T.; Naitou, M.; Hagiwara, H.; Abe, M.; Ozawa, M.; !1Sasanuma, S.I.; Sasanuma, M.; Tsuchiya, Y.; Shibata, T.; !1Watanabe, K.; Ono, A.; Yamazaki, M.A.; Tashiro, H.; Hanaoka, !1F.; Murakami, Y. !$#journal Yeast (1996) 12:177-190 !$#title Fifteen open reading frames in a 30.8 kb region of the right !1arm of chromosome VI from Saccharomyces cerevisiae. !$#cross-references MUID:96287654; PMID:8686381 !$#accession S63838 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-147 ##label EKI !'##cross-references EMBL:D44602; NID:g893419; PIDN:BAA08044.1; !1PID:g893428 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1995 COMMENT This highly acidic protein is one of the components of the !1ubiquinol-cytochrome-c reductase complex (complex III or !1cytochrome b-c1 complex), which is part of the mitochondrial !1respiratory chain and is located in the inner membrane. This !1protein may mediate the formation of the complex between !1cytochromes c and c1. GENETICS !$#gene SGD:QCR6; CR17; MIPS:YFR033c !'##cross-references SGD:S0001929; MIPS:YFR033c !$#map_position 6R !$#genome nuclear CLASSIFICATION #superfamily ubiquinol-cytochrome-c reductase 17K protein; !1ubiquinol-cytochrome-c reductase 11K protein homology KEYWORDS electron transfer; mitochondrial inner membrane; !1mitochondrion; oxidative phosphorylation; oxidoreductase; !1respiratory chain FEATURE !$71-147 #domain ubiquinol-cytochrome-c reductase 11K protein !8homology #label U11\ !$101-123 #disulfide_bonds #status predicted SUMMARY #length 147 #molecular-weight 17257 #checksum 4179 SEQUENCE /// ENTRY A34660 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) Rieske iron-sulfur protein precursor [validated] - bovine ALTERNATE_NAMES cytochrome bc1 complex chain 9; cytochrome bc1 complex iron-sulfur protein; Rieske iron-sulfur protein; ubiquinol-cytochrome-c reductase 8K protein CONTAINS ubiquinol-cytochrome-c reductase chain 5; ubiquinol-cytochrome-c reductase chain 9 ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Mar-1991 #sequence_revision 22-Apr-1995 #text_change 03-Jun-2002 ACCESSIONS A46063; A34660; A24011; S00003; S14162; S65406 REFERENCE A46063 !$#authors Brandt, U.; Yu, L.; Yu, C.A.; Trumpower, B.L. !$#journal J. Biol. Chem. (1993) 268:8387-8390 !$#title The mitochondrial targeting presequence of the Rieske !1iron-sulfur protein is processed in a single step after !1insertion into the cytochrome bc1 complex in mammals and !1retained as a subunit in the complex. !$#cross-references MUID:93231976; PMID:8386158 !$#accession A46063 !'##molecule_type mRNA !'##residues 1-274 ##label BRA !'##cross-references GB:S58789; NID:g299557; PIDN:AAB26197.1; !1PID:g299558 !'##experimental_source heart !'##note sequence extracted from NCBI backbone (NCBIN:129525, !1NCBIP:129529) REFERENCE A34660 !$#authors Usui, S.; Yu, L.; Yu, C.A. !$#journal Biochem. Biophys. Res. Commun. (1990) 167:575-579 !$#title Cloning and sequencing of a cDNA encoding the Rieske !1iron-sulfur protein of bovine heart mitochondrial !1ubiquinol-cytochrome c reductase. !$#cross-references MUID:90211231; PMID:2157409 !$#accession A34660 !'##molecule_type mRNA !'##residues 1-8,'RHSR',13,'SYRPRPA',21,'WR',25-28,'WYSRSSK',39-60,'AA', !164-274 ##label USU !'##cross-references GB:M34336; NID:g163043; PIDN:AAA30515.1; !1PID:g163044 !'##note the authors translated the codon AAG for residue 34 as Arg !'##note this sequence has been revised in reference A46063 REFERENCE A24011 !$#authors Borchart, U.; Machleidt, W.; Schagger, H.; Link, T.A.; von !1Jagow, G. !$#journal FEBS Lett. (1985) 191:125-130 !$#title Isolation and amino acid sequence of the 8 kDa DCCD-binding !1protein of beef heart ubiquinol:cytochrome c reductase. !$#cross-references MUID:86030649; PMID:2996928 !$#accession A24011 !'##molecule_type protein !'##residues 1-78 ##label BOR !'##experimental_source heart !'##note 53-Glu reacts rapidly and specifically with dicyclohexyl !1carbodiimide REFERENCE S00003 !$#authors Schaegger, H.; Borchart, U.; Machleidt, W.; Link, T.A.; von !1Jagow, G. !$#journal FEBS Lett. (1987) 219:161-168 !$#title Isolation and amino acid sequence of the 'Rieske' iron !1sulfur protein of beef heart ubiquinol:cytochrome c !1reductase. !$#cross-references MUID:87247298; PMID:3036596 !$#accession S00003 !'##molecule_type protein !'##residues 79-149,'A',151-268,'G',270-274 ##label SCH REFERENCE S14093 !$#authors Cocco, T.; Lorusso, M.; Sardanelli, A.M.; Minuto, M.; !1Ronchi, S.; Tedeschi, G.; Papa, S. !$#journal Eur. J. Biochem. (1991) 195:731-734 !$#title Structural and functional characteristics of polypeptide !1subunits of the bovine heart ubiquinol - cytochrome-c !1reductase complex. !$#cross-references MUID:91153313; PMID:1847870 !$#accession S14162 !'##molecule_type protein !'##residues 79-90;142-149,'A',151-162 ##label COC REFERENCE S65406 !$#authors Link, T.A.; Saynovits, M.; Assmann, C.; Iwata, S.; Ohnishi, !1T.; von Jagow, G. !$#journal Eur. J. Biochem. (1996) 237:71-75 !$#title Isolation, characterisation and crystallisation of a !1water-soluble fragment of the Rieske iron-sulfur protein of !1bovine heart mitochondrial bc(1) complex. !$#cross-references MUID:96203910; PMID:8620896 !$#accession S65406 !'##molecule_type protein !'##residues 146-150 ##label LIN REFERENCE A66520 !$#authors Iwata, S.; Saynovits, M.; Link, T.A.; Michel, H. !$#submission submitted to the Brookhaven Protein Data Bank, February 1996 !$#cross-references PDB:1RIE !$#contents annotation; X-ray crystallography, 1.5 angstroms REFERENCE A58841 !$#authors Iwata, S.; Lee, J.W.; Okada, K.; Lee, J.K.; Iwata, M.; !1Rasmussen, B.; Link, T.A.; Ramaswamy, S.; Jap, B.K. !$#journal Science (1998) 281:64-71 !$#title Complete structure of the 11-subunit bovine mitochondrial !1cytochrome bc1 complex. !$#cross-references MUID:98316377; PMID:9651245 !$#contents annotation; X-ray crystallography, 4.0 angstroms COMMENT After cleavage the transit peptide remains bound in the !1complex as ubiquinol-cytochrome-c reductase chain 9 (8K !1protein). GENETICS !$#genome nuclear COMPLEX the ubiquinol-cytochrome-c reductase complex consists of two !1subunits with 10 chains each and two chains of chain 9 !1(iron-sulfur protein) shared between the two subunits COMPLEX the transmembrane complex includes cytochrome b (see !1PIR:CBBO), cytochrome c1 (see PIR:CCBO1), Rieske iron-sulfur !1protein, and other accessory proteins (see PIR:CCBO11, !1PIR:CCBO17, PIR:A24864, PIR:ZPBOC1, and PIR:ZPBOC2) CLASSIFICATION #superfamily ubiquinol-cytochrome-c reductase iron-sulfur !1protein; Rieske [2Fe-2S] homology KEYWORDS 2Fe-2S; acetylated amino end; electron transfer; !1membrane-associated complex; metalloprotein; mitochondrion; !1oxidative phosphorylation; oxidoreductase; respiratory !1chain; Rieske iron-sulfur protein FEATURE !$1-78 #domain transit peptide (mitochondrion) #status !8experimental #label TNP\ !$1-78 #product ubiquinol-cytochrome-c reductase chain 9 !8#status experimental #label M8K\ !$79-274 #product ubiquinol-cytochrome-c reductase chain 5 !8#status experimental #label MAT\ !$207-254 #domain Rieske [2Fe-2S] homology #label RSK\ !$1 #modified_site acetylated amino end (Met) #status !8experimental\ !$217,219,236,239 #binding_site 2Fe-2S cluster (Cys, His, Cys, His) !8(covalent) #status experimental\ !$222-238 #disulfide_bonds #status experimental\ !$239 #active_site His #status predicted SUMMARY #length 274 #molecular-weight 29547 #checksum 8317 SEQUENCE /// ENTRY RDNCUF #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) Rieske iron-sulfur protein [similarity] - Neurospora crassa ORGANISM #formal_name Neurospora crassa DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 03-Jun-2002 ACCESSIONS A24612 REFERENCE A24612 !$#authors Harnisch, U.; Weiss, H.; Sebald, W. !$#journal Eur. J. Biochem. (1985) 149:95-99 !$#title The primary structure of the iron-sulfur subunit of !1ubiquinol-cytochrome c reductase from Neurospora, determined !1by cDNA and gene sequencing. !$#cross-references MUID:85203899; PMID:2986972 !$#accession A24612 !'##molecule_type DNA !'##residues 1-231 ##label HAR !'##cross-references GB:X02472; NID:g3001; PIDN:CAA26308.1; PID:g3002 GENETICS !$#introns 92/1; 121/3; 172/1 CLASSIFICATION #superfamily ubiquinol-cytochrome-c reductase iron-sulfur !1protein; Rieske [2Fe-2S] homology KEYWORDS 2Fe-2S; electron transfer; membrane-associated complex; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; Rieske iron-sulfur !1protein FEATURE !$164-211 #domain Rieske [2Fe-2S] homology #label RSK\ !$174,176,193,196 #binding_site 2Fe-2S cluster (Cys, His, Cys, His) !8(covalent) #status predicted\ !$179-195 #disulfide_bonds #status predicted\ !$196 #active_site His #status predicted SUMMARY #length 231 #molecular-weight 24770 #checksum 9118 SEQUENCE /// ENTRY RDQFBR #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) Rieske iron-sulfur protein [validated] - Rhodospirillum rubrum ALTERNATE_NAMES cytochrome bc1 complex iron-sulfur protein ORGANISM #formal_name Rhodospirillum rubrum DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 03-Jun-2002 ACCESSIONS S12256; A38813 REFERENCE S12255 !$#authors Majewski, C.; Trebst, A. !$#journal Mol. Gen. Genet. (1990) 224:373-382 !$#title The pet genes of Rhodospirillum rubrum: cloning and !1sequencing of the genes for the cytochrome bc(1)-complex. !$#cross-references MUID:91094774; PMID:2176269 !$#accession S12256 !'##molecule_type DNA !'##residues 1-183 ##label MA1 !'##cross-references EMBL:X55387; NID:g46382; PIDN:CAA39058.1; !1PID:g46384 !$#accession A38813 !'##molecule_type protein !'##residues 2-35 ##label MA2 GENETICS !$#gene petA CLASSIFICATION #superfamily ubiquinol-cytochrome-c reductase iron-sulfur !1protein; Rieske [2Fe-2S] homology KEYWORDS 2Fe-2S; electron transfer; membrane-associated complex; !1metalloprotein; oxidoreductase; respiratory chain; Rieske !1iron-sulfur protein FEATURE !$2-183 #product ubiquinol-cytochrome-c reductase iron-sulfur !8protein #status experimental #label MAT\ !$111-163 #domain Rieske [2Fe-2S] homology #label RSK\ !$121,123,145,148 #binding_site 2Fe-2S cluster (Cys, His, Cys, His) !8(covalent) #status predicted\ !$126-147 #disulfide_bonds #status predicted\ !$148 #active_site His #status predicted SUMMARY #length 183 #molecular-weight 19513 #checksum 2374 SEQUENCE /// ENTRY A29336 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) Rieske iron-sulfur protein - Rhodobacter capsulatus ALTERNATE_NAMES cytochrome b-c1 complex Rieske iron-sulfur protein ORGANISM #formal_name Rhodobacter capsulatus DATE 31-Dec-1988 #sequence_revision 22-Jul-1994 #text_change 03-Jun-2002 ACCESSIONS A29336; A25405; D25405; S22633; S21003 REFERENCE A92938 !$#authors Davidson, E.; Daldal, F. !$#journal J. Mol. Biol. (1987) 195:13-24 !$#title Primary structure of the bc-1 complex of Rhodopseudomonas !1capsulata. Nucleotide sequence of the pet operon encoding !1the Rieske, cytochrome b, and cytochrome c-1 apoproteins. !$#cross-references MUID:88011223; PMID:2821268 !$#accession A29336 !'##molecule_type DNA !'##residues 1-191 ##label DAV !'##cross-references EMBL:X05630; NID:g46093; PIDN:CAA29116.1; !1PID:g581499 REFERENCE A91162 !$#authors Gabellini, N.; Sebald, W. !$#journal Eur. J. Biochem. (1986) 154:569-579 !$#title Nucleotide sequence and transcription of the fbc operon from !1Rhodopseudomonas sphaeroides. Evaluation of the deduced !1amino acid sequences of the FeS protein, cytochrome b and !1cytochrome c-1. !$#cross-references MUID:86136096; PMID:3004982 !$#note source is designated as Rhodopseudomonas sphaeroides !$#accession A25405 !'##molecule_type DNA !'##residues 1-47,'S',49-113,'S',115,'A',117-191 ##label GAB1 !'##cross-references EMBL:X03476; NID:g46007; PIDN:CAA27194.1; !1PID:g581491 !$#accession D25405 !'##molecule_type protein !'##residues 49-67 ##label GAB2 REFERENCE S22631 !$#authors Tokito, M.K.; Daldal, F. !$#journal Mol. Microbiol. (1992) 6:1645-1654 !$#title petR, located upstream of the fbcFBC operon encoding the !1cytochrome bc(1) complex, is homologous to bacterial !1response regulators and necessary for photosynthetic and !1respiratory growth of Rhodobacter capsulatus. !$#cross-references MUID:92356828; PMID:1323023 !$#accession S22633 !'##molecule_type DNA !'##residues 1-23 ##label TOK !'##cross-references EMBL:Z12113; NID:g49287; PIDN:CAA78099.1; !1PID:g581500 !'##note the authors translated the codon AAC for residue 7 as Gln GENETICS !$#gene fbcF; petA !$#start_codon GTG CLASSIFICATION #superfamily ubiquinol-cytochrome-c reductase iron-sulfur !1protein; Rieske [2Fe-2S] homology KEYWORDS 2Fe-2S; electron transfer; membrane-associated complex; !1metalloprotein; oxidoreductase; respiratory chain; Rieske !1iron-sulfur protein FEATURE !$123-171 #domain Rieske [2Fe-2S] homology #label RSK\ !$133,135,153,156 #binding_site 2Fe-2S cluster (Cys, His, Cys, His) !8(covalent) #status predicted\ !$138-155 #disulfide_bonds #status predicted\ !$156 #active_site His #status predicted SUMMARY #length 191 #molecular-weight 20440 #checksum 8891 SEQUENCE /// ENTRY S13868 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) Rieske iron-sulfur protein [validated] - Rhodobacter sphaeroides ORGANISM #formal_name Rhodobacter sphaeroides DATE 31-Dec-1988 #sequence_revision 22-Jul-1994 #text_change 03-Jun-2002 ACCESSIONS S13868; C34591 REFERENCE S13868 !$#authors Yun, C.H.; Beci, R.; Crofts, A.R.; Kaplan, S.; Gennis, R.B. !$#journal Eur. J. Biochem. (1990) 194:399-411 !$#title Cloning and DNA sequencing of the fbc operon encoding the !1cytochrome bc(1) complex from Rhodobacter sphaeroides. !1Characterization of fbc deletion mutants and complementation !1by a site-specific mutational variant. !$#cross-references MUID:91099313; PMID:2176595 !$#accession S13868 !'##molecule_type DNA !'##residues 1-187 ##label YUN !'##cross-references EMBL:X56157; NID:g46425; PIDN:CAA39623.1; !1PID:g581533 REFERENCE A34591 !$#authors Andrews, K.M.; Crofts, A.R.; Gennis, R.B. !$#journal Biochemistry (1990) 29:2645-2651 !$#title Large-scale purification and characterization of a highly !1active four-subunit cytochrome bc-1 complex from Rhodobacter !1sphaeroides. !$#cross-references MUID:90268011; PMID:2161250 !$#accession C34591 !'##molecule_type protein !'##residues 2-6,'X',8-10,'XX',13-14,'X',16-19 ##label AND GENETICS !$#gene fbcF !$#start_codon GTG CLASSIFICATION #superfamily ubiquinol-cytochrome-c reductase iron-sulfur !1protein; Rieske [2Fe-2S] homology KEYWORDS 2Fe-2S; electron transfer; membrane-associated complex; !1metalloprotein; oxidoreductase; photosynthesis; respiratory !1chain; Rieske iron-sulfur protein FEATURE !$2-187 #product ubiquinol-cytochrome-c reductase iron-sulfur !8protein #status experimental #label MAT\ !$119-167 #domain Rieske [2Fe-2S] homology #label RSK\ !$129,131,149,152 #binding_site 2Fe-2S cluster (Cys, His, Cys, His) !8(covalent) #status predicted\ !$134-151 #disulfide_bonds #status predicted\ !$152 #active_site His #status predicted SUMMARY #length 187 #molecular-weight 19910 #checksum 4427 SEQUENCE /// ENTRY RDBYUN #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) 14K protein - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES complex III 14K protein; cytochrome b-c1 complex 14K protein; protein YDR529c ORGANISM #formal_name Saccharomyces cerevisiae DATE 28-Aug-1985 #sequence_revision 13-Mar-1997 #text_change 03-Jun-2002 ACCESSIONS S69584; A00121 REFERENCE S69553 !$#authors Dietrich, F.S. !$#submission submitted to the EMBL Data Library, August 1995 !$#description The sequence of S. cerevisiae cosmids 8166, 9787, 9717, and !1lambda 3073. !$#accession S69584 !'##molecule_type DNA !'##residues 1-127 ##label DIE !'##cross-references EMBL:U33057; NID:g927764; PIDN:AAB64968.1; !1PID:g927796; GSPDB:GN00004; MIPS:YDR529c REFERENCE A00121 !$#authors De Haan, M.; Van Loon, A.P.G.M.; Kreike, J.; Vaessen, !1R.T.M.J.; Grivell, L.A. !$#journal Eur. J. Biochem. (1984) 138:169-177 !$#title The biosynthesis of the ubiquinol-cytochrome c reductase !1complex in yeast. DNA sequence analysis of the nuclear gene !1coding for the 14-kDa subunit. !$#cross-references MUID:84108379; PMID:6319130 !$#accession A00121 !'##molecule_type DNA !'##residues 1-91,'Q',93-127 ##label DEH !'##cross-references EMBL:X00256; NID:g3600; PIDN:CAA25064.1; PID:g3601 !'##experimental_source strain FL100 GENETICS !$#gene SGD:QCR7; CRO1; UCR7; COR4; MIPS:YDR529c !'##cross-references SGD:S0002937; MIPS:YDR529c !$#map_position 4R !$#genome nuclear CLASSIFICATION #superfamily ubiquinol-cytochrome-c reductase 14K protein KEYWORDS electron transfer; membrane protein; membrane-associated !1complex; mitochondrial inner membrane; mitochondrion; !1oxidative phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 127 #molecular-weight 14565 #checksum 4625 SEQUENCE /// ENTRY UYBO #type complete TITLE ubiquinone-binding protein QP-C - bovine ALTERNATE_NAMES 14K protein; ubiquinol-cytochrome c reductase chain VI ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 26-Feb-1999 ACCESSIONS A00122; A61151; S14163 REFERENCE A00122 !$#authors Wakabayashi, S.; Takao, T.; Shimonishi, Y.; Kuramitsu, S.; !1Matsubara, H.; Wang, T.; Zhang, Z.; King, T.E. !$#journal J. Biol. Chem. (1985) 260:337-343 !$#title Complete amino acid sequence of the ubiquinone binding !1protein (QP-C), a protein similar to the 14,000-dalton !1subunit of the yeast ubiquinol-cytochrome c reductase !1complex. !$#cross-references MUID:85080099; PMID:2981208 !$#accession A00122 !'##molecule_type protein !'##residues 1-110 ##label WAK REFERENCE A61151 !$#authors Usui, S.; Yu, L.; Harmon, J.; Yu, C.A. !$#journal Arch. Biochem. Biophys. (1991) 289:109-117 !$#title Immunochemical study of subunit VI (M-r 13,400) of !1mitochondrial ubiquinol-cytochrome c reductase. !$#cross-references MUID:91378519; PMID:1654841 !$#accession A61151 !'##molecule_type protein !'##residues 22-26;32-46;74-80 ##label USU REFERENCE S14093 !$#authors Cocco, T.; Lorusso, M.; Sardanelli, A.M.; Minuto, M.; !1Ronchi, S.; Tedeschi, G.; Papa, S. !$#journal Eur. J. Biochem. (1991) 195:731-734 !$#title Structural and functional characteristics of polypeptide !1subunits of the bovine heart ubiquinol - cytochrome-c !1reductase complex. !$#cross-references MUID:91153313; PMID:1847870 !$#accession S14163 !'##molecule_type protein !'##residues 1-32 ##label COC COMMENT This is one of the specific mitochondrial proteins that bind !1to ubiquinone and stabilize the ubisemiquinone radicals. CLASSIFICATION #superfamily ubiquinol-cytochrome-c reductase 14K protein KEYWORDS acetylated amino end; electron transfer; mitochondrion; !1oxidative phosphorylation; respiratory chain FEATURE !$1 #modified_site acetylated amino end (Ala) #status !8experimental SUMMARY #length 110 #molecular-weight 13346 #checksum 3634 SEQUENCE /// ENTRY CCBO17 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) 7K protein - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 18-Apr-1984 #sequence_revision 18-Apr-1984 #text_change 03-Jun-2002 ACCESSIONS A00123 REFERENCE A00123 !$#authors Schagger, H.; von Jagow, G.; Borchart, U.; Machleidt, W. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1983) 364:307-311 !$#title Amino-acid sequence of the smallest protein of the !1cytochrome c-1 subcomplex from beef heart mitochondria. !$#cross-references MUID:83236204; PMID:6305819 !$#accession A00123 !'##molecule_type protein !'##residues 1-62 ##label SCH COMMENT This is one of the nonheme components of the cytochrome c1 !1complex, which is located in the inner membrane of the !1mitochondrion and functions as electron donor to cytochrome !1c in the mitochondrial respiratory chain. CLASSIFICATION #superfamily cytochrome c1 nonheme 7K protein KEYWORDS mitochondrion; oxidative phosphorylation; oxidoreductase; !1respiratory chain SUMMARY #length 62 #molecular-weight 7197 #checksum 4032 SEQUENCE /// ENTRY A38325 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) chain 9 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein G7164; protein YGR183c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS A38325; B38325; S64497; S64501 REFERENCE A38325 !$#authors Phillips, J.D.; Schmitt, M.E.; Brown, T.A.; Beckmann, J.D.; !1Trumpower, B.L. !$#journal J. Biol. Chem. (1990) 265:20813-20821 !$#title Isolation and characterization of QCR9, a nuclear gene !1encoding the 7.3-kDa subunit 9 of the Saccharomyces !1cerevisiae ubiquinol-cytochrome c oxidoreductase complex. An !1intron-containing gene with a conserved sequence occurring !1in the intron of COX4. !$#cross-references MUID:91065877; PMID:2174427 !$#accession A38325 !'##molecule_type DNA !'##residues 1-66 ##label PHI !'##cross-references GB:M59797; GB:M37790; NID:g172311; PIDN:AAA63575.1; !1PID:g172312 !$#accession B38325 !'##molecule_type protein !'##residues 2-11 ##label PH2 REFERENCE S64003 !$#authors Hebling, U.; Hofmann, B.; Delius, H. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64497 !'##molecule_type DNA !'##residues 1-66 ##label HEB !'##cross-references EMBL:Z72968; NID:g1323323; PIDN:CAA97209.1; !1PID:g1323324; GSPDB:GN00007; MIPS:YGR183c !'##experimental_source strain S288C REFERENCE S64499 !$#authors Arroyo, J.; Garcia-Gonzalez, M.; Garcia-Saez, M.I.; !1Sanchez-Perez, M.; Nombela, C. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64501 !'##molecule_type DNA !'##residues 1-66 ##label ARR !'##cross-references EMBL:Z72968; NID:g1323323; PIDN:CAA97209.1; !1PID:g1323324; GSPDB:GN00007; MIPS:YGR183c !'##experimental_source strain S288C GENETICS !$#gene SGD:QCR9; UCR9; MIPS:YGR183c !'##cross-references SGD:S0003415; MIPS:YGR183c !$#map_position 7R !$#genome nuclear !$#introns 1/3 CLASSIFICATION #superfamily cytochrome c1 nonheme 7K protein KEYWORDS membrane-associated complex; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain FEATURE !$2-66 #product ubiquinol-cytochrome-c reductase chain 9 !8#status experimental #label MAT SUMMARY #length 66 #molecular-weight 7476 #checksum 8545 SEQUENCE /// ENTRY CCDV3 #type complete TITLE cytochrome c3 precursor - Desulfovibrio vulgaris (strain Hildenborough) ORGANISM #formal_name Desulfovibrio vulgaris DATE 24-Apr-1984 #sequence_revision 17-Feb-1994 #text_change 03-Mar-2000 ACCESSIONS A24799; A00124; D32427 REFERENCE A24799 !$#authors Voordouw, G.; Brenner, S. !$#journal Eur. J. Biochem. (1986) 159:347-351 !$#title Cloning and sequencing of the gene encoding cytochrome c3 !1from Desulfovibrio vulgaris (Hildenborough). !$#cross-references MUID:87004646; PMID:3019687 !$#accession A24799 !'##molecule_type DNA !'##residues 1-129 ##label VOO !'##cross-references GB:X04304; NID:g40820; PIDN:CAA27847.1; PID:g40821 REFERENCE A00124 !$#authors Trousil, E.B.; Campbell, L.L. !$#journal J. Biol. Chem. (1974) 249:386-393 !$#title Amino acid sequence of cytochrome c-3 from Desulfovibrio !1vulgaris. !$#cross-references MUID:74070664; PMID:4358550 !$#accession A00124 !'##molecule_type protein !'##residues 23-129 ##label TRO !'##experimental_source strain Hildenborough, NCIB 8303 REFERENCE A32427 !$#authors Loutfi, M.; Guerlesquin, F.; Bianco, P.; Haladjian, J.; !1Bruschi, M. !$#journal Biochem. Biophys. Res. Commun. (1989) 159:670-676 !$#title Comparative studies of polyhemic cytochromes c isolated from !1Desulfovibrio vulgaris (Hildenborough) and Desulfovibrio !1desulfuricans (Norway). !$#cross-references MUID:89193654; PMID:2539120 !$#accession D32427 !'##molecule_type protein !'##residues 23-44 ##label LOU CLASSIFICATION #superfamily cytochrome c3; cytochrome c3 homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; sulfate respiration FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-129 #product cytochrome c3 #status experimental #label !8MAT\ !$42-128 #domain cytochrome c3 homology #label CC3\ !$44,56 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$47,105 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$52,55 #binding_site heme (Cys) (covalent) #status !8predicted\ !$57,74 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$68,73 #binding_site heme (Cys) (covalent) #status !8predicted\ !$92,128 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$101,104 #binding_site heme (Cys) (covalent) #status !8predicted\ !$122,127 #binding_site heme (Cys) (covalent) #status predicted SUMMARY #length 129 #molecular-weight 13976 #checksum 4690 SEQUENCE /// ENTRY CCDV3M #type complete TITLE cytochrome c3 precursor [validated] - Desulfovibrio vulgaris (strain Miyazaki) ORGANISM #formal_name Desulfovibrio vulgaris DATE 31-Oct-1980 #sequence_revision 10-Oct-1997 #text_change 15-Sep-2000 ACCESSIONS S33874; A00125 REFERENCE S33874 !$#authors Kitamura, M.; Ozawa, K.; Kojima, S.; Kumagai, I.; Akutsu, !1H.; Miura, K. !$#journal Protein Seq. Data Anal. (1993) 5:193-196 !$#title The primary structure of pre-cytochrome c(3) from !1Desulfovibrio vulgaris (Miyazaki F) as determined by !1nucleotide sequencing of its gene and partial amino acid !1sequencing. !$#accession S33874 !'##molecule_type DNA !'##residues 1-130 ##label KIT !'##cross-references DDBJ:D31702; NID:g496361; PIDN:BAA06511.1; !1PID:g496362 REFERENCE A00125 !$#authors Shinkai, W.; Hase, T.; Yagi, T.; Matsubara, H. !$#journal J. Biochem. (1980) 87:1747-1756 !$#title Amino acid sequence of cytochrome c-3 from Desulfovibrio !1vulgaris, Miyazaki. !$#cross-references MUID:80249474; PMID:6249799 !$#accession A00125 !'##molecule_type protein !'##residues 24-64,'N',66-130 ##label SHI REFERENCE A49705 !$#authors Higuchi, Y.; Kusunoki, M.; Matsuura, Y.; Yasuoka, N.; !1Kakudo, M. !$#journal J. Mol. Biol. (1984) 172:109-139 !$#title Refined structure of cytochrome c-3 at 1.8 angstrom !1resolution. !$#cross-references MUID:84114880; PMID:6319712 !$#contents annotation; X-ray crystallography, 1.8 angstroms REFERENCE A50415 !$#authors Higuchi, Y.; Kusunoki, M.; Matsuura, Y.; Yasuoka, N.; !1Kakudo, M. !$#submission submitted to the Brookhaven Protein Data Bank, November 1983 !$#cross-references PDB:2CDV !$#contents annotation; X-ray crystallography, 1.8 angstroms, residues !124-64,'N',66-130 FUNCTION !$#description accepts electrons from cytochrome-c3 hydrogenase (EC !11.12.2.1) and transfers them to ferredoxin !$#pathway sulfate respiration CLASSIFICATION #superfamily cytochrome c3; cytochrome c3 homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; sulfate respiration FEATURE !$24-130 #product cytochrome c3 #status experimental #label !8MAT\ !$43-129 #domain cytochrome c3 homology #label CC3\ !$45,57 #binding_site heme iron (His) (axial ligands) #status !8experimental\ !$48,106 #binding_site heme iron (His) (axial ligands) #status !8experimental\ !$53,56 #binding_site heme (Cys) (covalent) #status !8experimental\ !$58,75 #binding_site heme iron (His) (axial ligands) #status !8experimental\ !$69,74 #binding_site heme (Cys) (covalent) #status !8experimental\ !$93,129 #binding_site heme iron (His) (axial ligands) #status !8experimental\ !$102,105 #binding_site heme (Cys) (covalent) #status !8experimental\ !$123,128 #binding_site heme (Cys) (covalent) #status !8experimental SUMMARY #length 130 #molecular-weight 13843 #checksum 3762 SEQUENCE /// ENTRY CCDV3G #type complete TITLE cytochrome c3 - Desulfovibrio gigas (tentative sequence) ORGANISM #formal_name Desulfovibrio gigas DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 31-Mar-2000 ACCESSIONS A00126 REFERENCE A00126 !$#authors Ambler, R.P.; Bruschi, M.; Le Gall, J. !$#journal FEBS Lett. (1969) 5:115-117 !$#title The structure of cytochrome c'-3 from Desulfovibrio gigas !1(NCIB 9332). !$#accession A00126 !'##molecule_type protein !'##residues 1-111 ##label AMB !'##experimental_source NCIB 9332 !'##note one of the four residues at positions 34, 35, 39, and 42 is !1amidated CLASSIFICATION #superfamily cytochrome c3; cytochrome c3 homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; sulfate respiration FEATURE !$23-109 #domain cytochrome c3 homology #label CC3\ !$25,37 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$28,86 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$33,36 #binding_site heme (Cys) (covalent) #status !8predicted\ !$38,54 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$48,53 #binding_site heme (Cys) (covalent) #status !8predicted\ !$72,109 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$82,85 #binding_site heme (Cys) (covalent) #status !8predicted\ !$103,108 #binding_site heme (Cys) (covalent) #status predicted SUMMARY #length 111 #molecular-weight 11889 #checksum 2511 SEQUENCE /// ENTRY CCDV3D #type complete TITLE cytochrome c3 - Desulfovibrio desulfuricans ORGANISM #formal_name Desulfovibrio desulfuricans DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 03-Mar-2000 ACCESSIONS A00127 REFERENCE A00127 !$#authors Ambler, R.P.; Bruschi, M.; Le Gall, J. !$#journal FEBS Lett. (1971) 18:347-350 !$#title The amino acid sequence of cytochrome c-3 from Desulfovibrio !1desulfuricans (strain El Agheila Z, NCIB 8380). !$#accession A00127 !'##molecule_type protein !'##residues 1-102 ##label AMB !'##experimental_source strain El Agheila Z, NCIB 8380 CLASSIFICATION #superfamily cytochrome c3; cytochrome c3 homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; sulfate respiration FEATURE !$24-99 #domain cytochrome c3 homology #label CC3\ !$26,38 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$29,85 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$34,37 #binding_site heme (Cys) (covalent) #status !8predicted\ !$39,56 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$50,55 #binding_site heme (Cys) (covalent) #status !8predicted\ !$73,99 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$81,84 #binding_site heme (Cys) (covalent) #status !8predicted\ !$95,98 #binding_site heme (Cys) (covalent) #status predicted SUMMARY #length 102 #molecular-weight 10913 #checksum 8502 SEQUENCE /// ENTRY CCDV3S #type complete TITLE cytochrome c3 - Desulfovibrio salexigens (tentative sequence) ORGANISM #formal_name Desulfovibrio salexigens DATE 31-Aug-1980 #sequence_revision 31-Aug-1980 #text_change 31-Mar-2000 ACCESSIONS A00128; A38898 REFERENCE A38897 !$#authors Ambler, R.P.; Bruschi, M.; Le Gall, J. !$#citation unpublished results, cited by Haser, R., Pierrot, M., Frey, !1M., Payan, F., Astier, J.P., Bruschi, M., and Le Gall, J., !1Nature 282, 806-810, 1979 !$#description Structure and sequence of the multihaem cytochrome c-3. !$#accession A00128 !'##molecule_type protein !'##residues 1-106 ##label HAS REFERENCE A38898 !$#authors Ambler, R.P.; Bruschi, M.; Le Gall, J. !$#citation unpublished results, cited by Ambler, R.P., Syst. Zool. 22, !1554-565, 1973 !$#description Bacterial cytochromes C and molecular evolution. !$#accession A38898 !'##molecule_type protein !'##residues 1-4,'G',6-106 ##label HA2 CLASSIFICATION #superfamily cytochrome c3; cytochrome c3 homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; sulfate respiration FEATURE !$24-102 #domain cytochrome c3 homology #label CC3\ !$26,38 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$29,86 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$34,37 #binding_site heme (Cys) (covalent) #status !8predicted\ !$39,56 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$50,55 #binding_site heme (Cys) (covalent) #status !8predicted\ !$75,102 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$82,85 #binding_site heme (Cys) (covalent) #status !8predicted\ !$98,101 #binding_site heme (Cys) (covalent) #status predicted SUMMARY #length 106 #molecular-weight 11306 #checksum 2144 SEQUENCE /// ENTRY CCDV3N #type complete TITLE cytochrome c3, tetraheme [validated] - Desulfovibrio desulfuricans (strain Norway 4) ALTERNATE_NAMES cytochrome c3 M(r) 13,000 ORGANISM #formal_name Desulfovibrio desulfuricans DATE 31-Aug-1980 #sequence_revision 17-Oct-1997 #text_change 15-Sep-2000 ACCESSIONS A00129; A32427 REFERENCE A90639 !$#authors Bruschi, M. !$#journal Biochim. Biophys. Acta (1981) 671:219-226 !$#title The primary structure of the tetrahaem cytochrome C-3 from !1Desulfovibrio desulfuricans (strain Norway 4). !$#accession A00129 !'##molecule_type protein !'##residues 1-85,'S',87-96,'ALK',100-118 ##label BRU !'##note this sequence has been corrected in reference S43400 REFERENCE S43400 !$#authors Bruschi, M.; Leroy, G.; Guerlesquin, F.; Bonicel, J. !$#journal Biochim. Biophys. Acta (1994) 1205:123-131 !$#title Amino-acid sequence of the cytochrome c(3) (M(r) 26000) from !1Desulfovibrio desulfuricans Norway and a comparison with !1those of the other polyhemic cytochromes from Desulfovibrio. !$#cross-references MUID:94191018; PMID:8142476 !$#contents annotation; sequence correction !$#note peptides for sequence A00129 were redetermined and corrected REFERENCE A32427 !$#authors Loutfi, M.; Guerlesquin, F.; Bianco, P.; Haladjian, J.; !1Bruschi, M. !$#journal Biochem. Biophys. Res. Commun. (1989) 159:670-676 !$#title Comparative studies of polyhemic cytochromes c isolated from !1Desulfovibrio vulgaris (Hildenborough) and Desulfovibrio !1desulfuricans (Norway). !$#cross-references MUID:89193654; PMID:2539120 !$#accession A32427 !'##molecule_type protein !'##residues 1-36 ##label LOU REFERENCE A58614 !$#authors Czjzek, M.; Payan, F.; Guerlesquin, F.; Bruschi, M.; Haser, !1R. !$#journal J. Mol. Biol. (1994) 243:653-667 !$#title Crystal structure of cytochrome c3 from Desulfovibrio !1desulfuricans Norway at 1.7 Angstroms resolution. !$#cross-references MUID:95055708; PMID:7966289 !$#contents annotation; X-ray crystallography, 1.7 angstroms !$#note the corrected sequence is shown REFERENCE A52704 !$#authors Czjzek, M.; Payan, F.; Haser, R. !$#submission submitted to the Brookhaven Protein Data Bank, July 1994 !$#cross-references PDB:2CY3 !$#contents annotation; X-ray crystallography, 1.7 angstroms, residues !11-118 REFERENCE A49706 !$#authors Pierrot, M.; Haser, R.; Frey, M.; Payan, F.; Astier, J.P. !$#journal J. Biol. Chem. (1982) 257:14341-14348 !$#title Crystal structure and electron transfer properties of !1cytochrome c-3. !$#cross-references MUID:83056976; PMID:6292223 !$#contents annotation; X-ray crystallography, 2.5 angstroms REFERENCE A93218 !$#authors Haser, R.; Pierrot, M.; Frey, M.; Payan, F.; Astier, J.P.; !1Bruschi, M.; Le Gall, J. !$#journal Nature (1979) 282:806-810 !$#title Structure and sequence of the multihaem cytochrome c-3. !$#cross-references MUID:80078137; PMID:229424 !$#contents annotation; X-ray crystallography, 2.5 angstroms COMPLEX monomer FUNCTION !$#description accepts electrons from cytochrome-c3 hydrogenase (EC !11.12.2.1) and transfers them to ferredoxin II !$#pathway sulfate respiration !$#note this protein is also active in the phosphoroclastic reaction CLASSIFICATION #superfamily cytochrome c3; cytochrome c3 homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; monomer; phosphoroclastic reaction; sulfate !1respiration FEATURE !$34-115 #domain cytochrome c3 homology #label CC3\ !$36,48 #binding_site heme iron (His) (axial ligands) #status !8experimental\ !$39,96 #binding_site heme iron (His) (axial ligands) #status !8experimental\ !$44,47 #binding_site heme (Cys) (covalent) #status !8experimental\ !$49,67 #binding_site heme iron (His) (axial ligands) #status !8experimental\ !$61,66 #binding_site heme (Cys) (covalent) #status !8experimental\ !$89,115 #binding_site heme iron (His) (axial ligands) #status !8experimental\ !$92,95 #binding_site heme (Cys) (covalent) #status !8experimental\ !$111,114 #binding_site heme (Cys) (covalent) #status !8experimental SUMMARY #length 118 #molecular-weight 12622 #checksum 4806 SEQUENCE /// ENTRY S43400 #type complete TITLE cytochrome c3, octaheme [validated] - Desulfovibrio desulfuricans (strain Norway 4) ALTERNATE_NAMES cytochrome c3 M(r) 26,000 ORGANISM #formal_name Desulfovibrio desulfuricans #variety strain Norway DATE 20-Oct-1994 #sequence_revision 03-Aug-1995 #text_change 15-Sep-2000 ACCESSIONS S43400; B32427 REFERENCE S43400 !$#authors Bruschi, M.; Leroy, G.; Guerlesquin, F.; Bonicel, J. !$#journal Biochim. Biophys. Acta (1994) 1205:123-131 !$#title Amino-acid sequence of the cytochrome c(3) (M(r) 26000) from !1Desulfovibrio desulfuricans Norway and a comparison with !1those of the other polyhemic cytochromes from Desulfovibrio. !$#cross-references MUID:94191018; PMID:8142476 !$#accession S43400 !'##molecule_type protein !'##residues 1-111 ##label BRU !'##experimental_source strain Norway, NCIB 8310 REFERENCE A32427 !$#authors Loutfi, M.; Guerlesquin, F.; Bianco, P.; Haladjian, J.; !1Bruschi, M. !$#journal Biochem. Biophys. Res. Commun. (1989) 159:670-676 !$#title Comparative studies of polyhemic cytochromes c isolated from !1Desulfovibrio vulgaris (Hildenborough) and Desulfovibrio !1desulfuricans (Norway). !$#cross-references MUID:89193654; PMID:2539120 !$#accession B32427 !'##molecule_type protein !'##residues 1-30 ##label LOU !'##experimental_source strain Norway 4, NCIB 8310 REFERENCE A65383 !$#authors Czjzek, M.; Haser, R. !$#submission submitted to the Brookhaven Protein Data Bank, January 1996 !$#cross-references PDB:1CZJ !$#contents annotation; X-ray crystallography, 2.16 angstroms, residues !12-111 COMPLEX homodimer CLASSIFICATION #superfamily cytochrome c3; cytochrome c3 homology KEYWORDS chromoprotein; heme; homodimer; iron; metalloprotein; !1sulfate respiration FEATURE !$28-109 #domain cytochrome c3 homology #label CC3\ !$30,42 #binding_site heme iron (His) (axial ligands) #status !8experimental\ !$33,90 #binding_site heme iron (His) (axial ligands) #status !8experimental\ !$38,41 #binding_site heme (Cys) (covalent) #status !8experimental\ !$43,60 #binding_site heme iron (His) (axial ligands) #status !8experimental\ !$54,59 #binding_site heme (Cys) (covalent) #status !8experimental\ !$77,109 #binding_site heme iron (His) (axial ligands) #status !8experimental\ !$86,89 #binding_site heme (Cys) (covalent) #status !8experimental\ !$105,108 #binding_site heme (Cys) (covalent) #status !8experimental SUMMARY #length 111 #molecular-weight 12522 #checksum 8573 SEQUENCE /// ENTRY CCDS7 #type complete TITLE cytochrome c7 (c551.5) - Desulfuromonas acetoxidans ORGANISM #formal_name Desulfuromonas acetoxidans DATE 13-Jul-1981 #sequence_revision 13-Jul-1981 #text_change 03-Mar-2000 ACCESSIONS A00130 REFERENCE A91331 !$#authors Ambler, R.P. !$#journal FEBS Lett. (1971) 18:351-353 !$#title The amino acid sequence of cytochrome c551.5 (cytochrome !1c-7) from the green photosynthetic bacterium !1Chloropseudomonas ethylica. !$#accession A00130 !'##molecule_type protein !'##residues 1-68 ##label AMB REFERENCE A38042 !$#authors Olson, J.M. !$#journal Int. J. Syst. Bacteriol. (1978) 28:128-129 !$#contents annotation; taxonomy COMMENT This c3-type cytochrome, although homologous with cytochrome !1c3 and similar in redox potential, has only three hemes and !1a shorter polypeptide chain. COMMENT This cytochrome was isolated from a culture originally !1called Chloropseudomonas ethylica, which has been found to !1be a mixture of Prosthecochloris aestuarii, a photosynthetic !1green sulfur bacterium, and Desulfuromonas acetoxidans, a !1colorless motile heterotroph. CLASSIFICATION #superfamily cytochrome c3; cytochrome c3 homology KEYWORDS chromoprotein; electron transfer; heme; iron; metalloprotein FEATURE !$15-66 #domain cytochrome c3 homology #label CC3\ !$17,30 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$20,53 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$26,29 #binding_site heme (Cys) (covalent) #status !8predicted\ !$45,66 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$49,52 #binding_site heme (Cys) (covalent) #status !8predicted\ !$62,65 #binding_site heme (Cys) (covalent) #status predicted SUMMARY #length 68 #molecular-weight 7262 #checksum 5497 SEQUENCE /// ENTRY A37129 #type complete TITLE cytochrome c550 cccA - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A37129; B69597 REFERENCE A37129 !$#authors von Wachenfeldt, C.; Hederstedt, L. !$#journal J. Biol. Chem. (1990) 265:13939-13948 !$#title Bacillus subtilis 13-kilodalton cytochrome c-550 encoded by !1cccA consists of a membrane-anchor and a heme domain. !$#cross-references MUID:90338015; PMID:2166045 !$#accession A37129 !'##status preliminary !'##molecule_type DNA !'##residues 1-120 ##label VON !'##cross-references GB:J05569; NID:g142651; PIDN:AAA22294.1; !1PID:g142652 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69597 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-120 ##label KUN !'##cross-references GB:Z99116; GB:AL009126; NID:g2634723; !1PIDN:CAB14449.1; PID:g2634952 !'##experimental_source strain 168 GENETICS !$#gene cccA CLASSIFICATION #superfamily Bacillus cytochrome c550 cccA; cytochrome c6 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; transmembrane protein FEATURE !$50-116 #domain cytochrome c6 homology #label CY6\ !$60,63 #binding_site heme (Cys) (covalent) #status !8predicted\ !$64,99 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 120 #molecular-weight 12766 #checksum 6958 SEQUENCE /// ENTRY S43726 #type complete TITLE cytochrome c551 precursor - thermophilic bacterium PS-3 ORGANISM #formal_name thermophilic bacterium PS-3 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S43726; S77898 REFERENCE S43726 !$#authors Fujiwara, Y.; Oka, M.; Hamamoto, T.; Sone, N. !$#journal Biochim. Biophys. Acta (1993) 1144:213-219 !$#title Cytochrome c-551 of the thermophilic bacterium PS3, DNA !1sequence and analysis of the mature cytochrome. !$#cross-references MUID:93379042; PMID:7916623 !$#accession S43726 !'##molecule_type DNA !'##residues 1-111 ##label FUJ !'##cross-references EMBL:X63125; NID:g402788; PIDN:CAA44835.1; !1PID:g402789 !$#accession S77898 !'##molecule_type protein !'##residues 48-50,'X',52-53,'X',55-67;75-82;91-97,'Q',99-108,110-111 !1##label FUW CLASSIFICATION #superfamily Bacillus cytochrome c550 cccA; cytochrome c6 !1homology KEYWORDS blocked amino end; chromoprotein; electron transfer; heme; !1iron; metalloprotein FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-111 #product cytochrome c551 #status predicted #label !8MAT\ !$41-107 #domain cytochrome c6 homology #label CY6\ !$51,54 #binding_site heme (Cys) (covalent) #status !8predicted\ !$55,90 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 111 #molecular-weight 11136 #checksum 8565 SEQUENCE /// ENTRY A39193 #type complete TITLE cytochrome cc3 precursor - Desulfovibrio vulgaris (strain Hildenborough) ALTERNATE_NAMES high-molecular-weight cytochrome c (HMW) ORGANISM #formal_name Desulfovibrio vulgaris DATE 18-Jun-1999 #sequence_revision 18-Jun-1999 #text_change 01-Dec-2000 ACCESSIONS A39193; B39193; A40605; C32427 REFERENCE A39193 !$#authors Pollock, W.B.R.; Loutfi, M.; Bruschi, M.; Rapp-Giles, B.J.; !1Wall, J.D.; Voordouw, G. !$#journal J. Bacteriol. (1991) 173:220-228 !$#title Cloning, sequencing, and expression of the gene encoding the !1high-molecular-weight cytochrome c from Desulfovibrio !1vulgaris Hildenborough. !$#cross-references MUID:91100286; PMID:1846136 !$#accession A39193 !'##molecule_type DNA !'##residues 1-545 ##label POL1 !'##cross-references GB:M34607; NID:g145080 !'##experimental_source strain Hildenborough !$#accession B39193 !'##molecule_type protein !'##residues !132-150;151-161;162-185;200-211;212-216;231-251;262-274; !1282-301;302-353;375-388;389-500;513-545 ##label POL2 !'##experimental_source strain Hildenborough REFERENCE A40605 !$#authors Rossi, M.; Pollock, W.B.R.; Reij, M.W.; Keon, R.G.; Fu, R.; !1Voordouw, G. !$#journal J. Bacteriol. (1993) 175:4699-4711 !$#title The hmc operon of Desulfovibrio vulgaris subsp. vulgaris !1Hildenborough encodes a potential transmembrane redox !1protein complex. !$#cross-references MUID:93328674; PMID:8335628 !$#accession A40605 !'##status preliminary !'##molecule_type DNA !'##residues 524-545 ##label ROS !'##cross-references GB:L16784; NID:g290377 !'##experimental_source strain Hildenborough !'##note cytochrome cc3 has 16 covalently bound hemes; the second axial !1ligand of heme 12 may be a methionine REFERENCE A32427 !$#authors Loutfi, M.; Guerlesquin, F.; Bianco, P.; Haladjian, J.; !1Bruschi, M. !$#journal Biochem. Biophys. Res. Commun. (1989) 159:670-676 !$#title Comparative studies of polyhemic cytochromes c isolated from !1Desulfovibrio vulgaris (Hildenborough) and Desulfovibrio !1desulfuricans (Norway). !$#cross-references MUID:89193654; PMID:2539120 !$#accession C32427 !'##status preliminary !'##molecule_type protein !'##residues 32-66 ##label LOU !'##experimental_source strain Hildenborough GENETICS !$#gene hmc CLASSIFICATION #superfamily cytochrome cc3; cytochrome c3 homology KEYWORDS chromoprotein; heme; iron; metalloprotein FEATURE !$1-31 #domain signal sequence #status predicted #label SIG\ !$32-545 #product cytochrome cc3 #status experimental #label !8MAT\ !$64-139 #domain cytochrome c3 homology #label CC31\ !$157-248 #domain cytochrome c3 homology #label CC32\ !$296-366 #domain cytochrome c3 homology #label CC33\ !$447-540 #domain cytochrome c3 homology #label CC34\ !$66,84 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$69,118 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$80,83 #binding_site heme (Cys) (covalent) #status !8predicted\ !$111,139 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$114,117 #binding_site heme (Cys) (covalent) #status !8predicted\ !$135,138 #binding_site heme (Cys) (covalent) #status !8predicted\ !$159,182 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$162,229 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$178,181 #binding_site heme (Cys) (covalent) #status !8predicted\ !$183,206 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$202,205 #binding_site heme (Cys) (covalent) #status !8predicted\ !$222,248 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$225,228 #binding_site heme (Cys) (covalent) #status !8predicted\ !$244,247 #binding_site heme (Cys) (covalent) #status !8predicted\ !$298,312 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$301,353 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$308,311 #binding_site heme (Cys) (covalent) #status !8predicted\ !$313,323 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$319,322 #binding_site heme (Cys) (covalent) #status !8predicted\ !$341,366 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$349,352 #binding_site heme (Cys) (covalent) #status !8predicted\ !$362,365 #binding_site heme (Cys) (covalent) #status !8predicted\ !$378,381 #binding_site heme (Cys) (covalent) #status !8predicted\ !$382 #binding_site heme iron (His) (axial ligand) #status !8predicted\ !$449,481 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$470,523 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$477,480 #binding_site heme (Cys) (covalent) #status !8predicted\ !$482,497 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$493,496 #binding_site heme (Cys) (covalent) #status !8predicted\ !$516,540 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$519,522 #binding_site heme (Cys) (covalent) #status !8predicted\ !$536,539 #binding_site heme (Cys) (covalent) #status predicted SUMMARY #length 545 #molecular-weight 58915 #checksum 7631 SEQUENCE /// ENTRY CCALC #type complete TITLE cytochrome c' [validated] - Alcaligenes sp. ORGANISM #formal_name Alcaligenes sp. DATE 13-Jul-1981 #sequence_revision 10-Oct-1997 #text_change 15-Sep-2000 ACCESSIONS A00131 REFERENCE A00131 !$#authors Ambler, R.P. !$#journal Biochem. J. (1973) 135:751-758 !$#title The amino acid sequence of cytochrome c' from Alcaligenes !1sp. N.C.I.B. 11015. !$#cross-references MUID:74100155; PMID:4360249 !$#accession A00131 !'##molecule_type protein !'##residues 'Z',2-127 ##label AMB !'##experimental_source NCIB 11015 !'##note this organism was previously identified as Pseudomonas !1denitrificans REFERENCE A65267 !$#authors Dobbs, A.J.; Faber, H.R.; Anderson, B.F.; Baker, E.N. !$#submission submitted to the Brookhaven Protein Data Bank, May 1995 !$#cross-references PDB:1CGO !$#contents annotation; X-ray crystallography, 1.8 angstroms, residues !11-51,'T',53-125 COMMENT Cytochrome c' is the most widely occurring bacterial c-type !1cytochrome. Cytochromes c' are high-spin heme proteins; the !1heme has no sixth ligand. However, they are confined in !1their reactivity with potential ligands to carbon monoxide !1and nitric oxide. COMPLEX homodimer CLASSIFICATION #superfamily cytochrome c' KEYWORDS chromoprotein; electron transfer; heme; homodimer; iron; !1metalloprotein; pyroglutamic acid FEATURE !$1 #modified_site pyrrolidone carboxylic acid (Gln) !8#status experimental\ !$116,119 #binding_site heme (Cys) (covalent) #status !8experimental\ !$120 #binding_site heme iron (His) (axial ligand) #status !8experimental SUMMARY #length 127 #molecular-weight 13628 #checksum 3037 SEQUENCE /// ENTRY CCAGB6 #type complete TITLE cytochrome c556 - Agrobacterium tumefaciens (strain B2a) ORGANISM #formal_name Agrobacterium tumefaciens DATE 22-May-1981 #sequence_revision 22-May-1981 #text_change 03-Mar-2000 ACCESSIONS A00132 REFERENCE A94434 !$#authors Van Beeumen, J.; Tempst, P.; Stevens, P.; Bral, D.; Van !1Damme, J.; De Ley, J. !$#book Protides of the Biological Fluids, Proc. 28th Colloq., !1Peeters, H., ed., pp.69-74, Pergamon Press, Oxford, 1980 !$#title Cytochromes c of two different sequence classes in !1Agrobacterium tumefaciens. !$#accession A00132 !'##molecule_type protein !'##residues 1-122 ##label VAN CLASSIFICATION #superfamily cytochrome c' KEYWORDS chromoprotein; electron transfer; heme; iron; metalloprotein FEATURE !$11,115 #binding_site heme iron (Met, His) (axial ligands) !8#status predicted\ !$111,114 #binding_site heme (Cys) (covalent) #status predicted SUMMARY #length 122 #molecular-weight 12548 #checksum 5688 SEQUENCE /// ENTRY CCAGC6 #type complete TITLE cytochrome c556 - Agrobacterium tumefaciens (strain II Chrys) ORGANISM #formal_name Agrobacterium tumefaciens DATE 22-May-1981 #sequence_revision 22-May-1981 #text_change 03-Mar-2000 ACCESSIONS A00133 REFERENCE A94434 !$#authors Van Beeumen, J.; Tempst, P.; Stevens, P.; Bral, D.; Van !1Damme, J.; De Ley, J. !$#book Protides of the Biological Fluids, Proc. 28th Colloq., !1Peeters, H., ed., pp.69-74, Pergamon Press, Oxford, 1980 !$#title Cytochromes c of two different sequence classes in !1Agrobacterium tumefaciens. !$#accession A00133 !'##molecule_type protein !'##residues 1-122 ##label VAN CLASSIFICATION #superfamily cytochrome c' KEYWORDS chromoprotein; electron transfer; heme; iron; metalloprotein FEATURE !$11,115 #binding_site heme iron (Met, His) (axial ligands) !8#status predicted\ !$111,114 #binding_site heme (Cys) (covalent) #status predicted SUMMARY #length 122 #molecular-weight 12519 #checksum 6288 SEQUENCE /// ENTRY CCAGA6 #type complete TITLE cytochrome c556 - Agrobacterium tumefaciens (strain Apple 185) ORGANISM #formal_name Agrobacterium tumefaciens DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 03-Mar-2000 ACCESSIONS A00134 REFERENCE A00134 !$#authors Tempst, P.; van Beeumen, J. !$#journal Eur. J. Biochem. (1983) 135:321-330 !$#title The amino acid sequence of cytochrome c-556 from !1Agrobacterium tumefaciens strain Apple 185. !$#cross-references MUID:83287429; PMID:6309523 !$#accession A00134 !'##molecule_type protein !'##residues 1-125 ##label TEM CLASSIFICATION #superfamily cytochrome c' KEYWORDS chromoprotein; electron transfer; heme; iron; metalloprotein FEATURE !$13,117 #binding_site heme iron (Met, His) (axial ligands) !8#status predicted\ !$113,116 #binding_site heme (Cys) (covalent) #status predicted SUMMARY #length 125 #molecular-weight 12985 #checksum 9101 SEQUENCE /// ENTRY CCRFCG #type complete TITLE cytochrome c' - Rhodocyclus gelatinosus ORGANISM #formal_name Rhodocyclus gelatinosus DATE 31-May-1979 #sequence_revision 31-May-1979 #text_change 03-Mar-2000 ACCESSIONS A00135 REFERENCE A93207 !$#authors Ambler, R.P.; Meyer, T.E.; Kamen, M.D. !$#journal Nature (1979) 278:661-662 !$#title Anomalies in amino acid sequences of small cytochromes c and !1cytochromes c' from two species of purple photosynthetic !1bacteria. !$#cross-references MUID:79199668; PMID:221823 !$#accession A00135 !'##molecule_type protein !'##residues 1-129 ##label AMB COMMENT Rhodopseudomonas is a genus of purple, nonsulfur, !1photosynthetic bacteria. CLASSIFICATION #superfamily cytochrome c' KEYWORDS chromoprotein; electron transfer; heme; iron; metalloprotein FEATURE !$119,122 #binding_site heme (Cys) (covalent) #status !8predicted\ !$123 #binding_site heme iron (His) (axial ligand) #status !8predicted SUMMARY #length 129 #molecular-weight 13283 #checksum 1134 SEQUENCE /// ENTRY CCPCC8 #type complete TITLE cytochrome c' - Paracoccus sp. ORGANISM #formal_name Paracoccus sp. DATE 18-Dec-1981 #sequence_revision 18-Dec-1981 #text_change 03-Mar-2000 ACCESSIONS A00136; S06910 REFERENCE A93899 !$#authors Ambler, R.P.; Bartsch, R.G.; Daniel, M.; Kamen, M.D.; !1McLellan, L.; Meyer, T.E.; Van Beeumen, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:6854-6857 !$#title Amino acid sequences of bacterial cytochromes c' and c-556. !$#cross-references MUID:82082545; PMID:6273892 !$#accession A00136 !'##molecule_type protein !'##residues 1-132 ##label AMB !'##experimental_source ATCC 12084 REFERENCE S06255 !$#authors Ambler, R.P.; Daniel, M.; McLellan, L.; Meyer, T.E.; !1Cusanovich, M.A.; Kamen, M.D. !$#journal Biochem. J. (1987) 248:365-371 !$#title Amino acid sequences of cytochrome c-554(548) and cytochrome !1c' from a halophilic denitrifying bacterium of the genus !1Paracoccus. !$#cross-references MUID:88133881; PMID:2829828 !$#accession S06910 !'##molecule_type protein !'##residues 1-132 ##label AMB2 CLASSIFICATION #superfamily cytochrome c' KEYWORDS chromoprotein; electron transfer; heme; iron; metalloprotein FEATURE !$122,125 #binding_site heme (Cys) (covalent) #status !8predicted\ !$126 #binding_site heme iron (His) (axial ligand) #status !8predicted SUMMARY #length 132 #molecular-weight 14442 #checksum 6679 SEQUENCE /// ENTRY CCQFCR #type complete TITLE cytochrome c' - Rhodospirillum rubrum ORGANISM #formal_name Rhodospirillum rubrum DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 03-Mar-2000 ACCESSIONS A00137 REFERENCE A00137 !$#authors Meyer, T.E.; Ambler, R.P.; Bartsch, R.G.; Kamen, M.D. !$#journal J. Biol. Chem. (1975) 250:8416-8421 !$#title Amino acid sequence of cytochrome c' from the purple !1photosynthetic bacterium Rhodospirillum rubrum S1. !$#cross-references MUID:76069185; PMID:172499 !$#accession A00137 !'##molecule_type protein !'##residues 1-126 ##label MEY !'##experimental_source strain S1, ATCC 11170 REFERENCE A38889 !$#authors Yasui, M.; Harada, S.; Kai, Y.; Kasai, N.; Kusunoki, M.; !1Matsuura, Y. !$#journal J. Biochem. (1992) 111:317-324 !$#title Three-dimensional structure of ferricytochrome c' from !1Rhodospirillum rubrum at 2.8 angstrom resolution. !$#cross-references MUID:92268030; PMID:1316891 !$#contents annotation; X-ray crystallography, 2.8 angstroms CLASSIFICATION #superfamily cytochrome c' KEYWORDS chromoprotein; electron transfer; heme; iron; metalloprotein FEATURE !$116,119 #binding_site heme (Cys) (covalent) #status !8experimental\ !$120 #binding_site heme iron (His) (axial ligand) #status !8experimental SUMMARY #length 126 #molecular-weight 13117 #checksum 7587 SEQUENCE /// ENTRY CCQFCP #type complete TITLE cytochrome c' - Rhodospirillum photometricum ORGANISM #formal_name Rhodospirillum photometricum DATE 18-Dec-1981 #sequence_revision 18-Dec-1981 #text_change 03-Mar-2000 ACCESSIONS A00138 REFERENCE A93899 !$#authors Ambler, R.P.; Bartsch, R.G.; Daniel, M.; Kamen, M.D.; !1McLellan, L.; Meyer, T.E.; Van Beeumen, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:6854-6857 !$#title Amino acid sequences of bacterial cytochromes c' and c-556. !$#cross-references MUID:82082545; PMID:6273892 !$#accession A00138 !'##molecule_type protein !'##residues 1-125 ##label AMB !'##experimental_source strain SP113 CLASSIFICATION #superfamily cytochrome c' KEYWORDS chromoprotein; electron transfer; heme; iron; metalloprotein FEATURE !$116,119 #binding_site heme (Cys) (covalent) #status !8predicted\ !$120 #binding_site heme iron (His) (axial ligand) #status !8predicted SUMMARY #length 125 #molecular-weight 12756 #checksum 3737 SEQUENCE /// ENTRY CCRFCX #type complete TITLE cytochrome c' - Rhodopseudomonas sp. ORGANISM #formal_name Rhodopseudomonas sp. DATE 18-Dec-1981 #sequence_revision 18-Dec-1981 #text_change 03-Mar-2000 ACCESSIONS A00139 REFERENCE A93899 !$#authors Ambler, R.P.; Bartsch, R.G.; Daniel, M.; Kamen, M.D.; !1McLellan, L.; Meyer, T.E.; Van Beeumen, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:6854-6857 !$#title Amino acid sequences of bacterial cytochromes c' and c-556. !$#cross-references MUID:82082545; PMID:6273892 !$#accession A00139 !'##molecule_type protein !'##residues 1-128 ##label AMB !'##experimental_source strain TJ12 CLASSIFICATION #superfamily cytochrome c' KEYWORDS chromoprotein; electron transfer; heme; iron; metalloprotein FEATURE !$117,120 #binding_site heme (Cys) (covalent) #status !8predicted\ !$121 #binding_site heme iron (His) (axial ligand) #status !8predicted SUMMARY #length 128 #molecular-weight 13371 #checksum 7026 SEQUENCE /// ENTRY CCRFPP #type complete TITLE cytochrome c' - Rhodobacter capsulatus ORGANISM #formal_name Rhodobacter capsulatus DATE 18-Dec-1981 #sequence_revision 18-Dec-1981 #text_change 03-Mar-2000 ACCESSIONS A00140 REFERENCE A93899 !$#authors Ambler, R.P.; Bartsch, R.G.; Daniel, M.; Kamen, M.D.; !1McLellan, L.; Meyer, T.E.; Van Beeumen, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:6854-6857 !$#title Amino acid sequences of bacterial cytochromes c' and c-556. !$#cross-references MUID:82082545; PMID:6273892 !$#accession A00140 !'##molecule_type protein !'##residues 1-129 ##label AMB !'##experimental_source strain SP7 CLASSIFICATION #superfamily cytochrome c' KEYWORDS chromoprotein; electron transfer; heme; iron; metalloprotein FEATURE !$118,121 #binding_site heme (Cys) (covalent) #status !8predicted\ !$122 #binding_site heme iron (His) (axial ligand) #status !8predicted SUMMARY #length 129 #molecular-weight 13206 #checksum 7163 SEQUENCE /// ENTRY CCRFCS #type complete TITLE cytochrome c' - Rhodobacter sphaeroides ORGANISM #formal_name Rhodobacter sphaeroides DATE 18-Dec-1981 #sequence_revision 18-Dec-1981 #text_change 03-Mar-2000 ACCESSIONS A00141 REFERENCE A93899 !$#authors Ambler, R.P.; Bartsch, R.G.; Daniel, M.; Kamen, M.D.; !1McLellan, L.; Meyer, T.E.; Van Beeumen, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:6854-6857 !$#title Amino acid sequences of bacterial cytochromes c' and c-556. !$#cross-references MUID:82082545; PMID:6273892 !$#accession A00141 !'##molecule_type protein !'##residues 1-130 ##label AMB !'##experimental_source strain 2.4.1, ATCC 17023 COMMENT Rhodopseudomonas is a genus of purple, nonsulfur, !1photosynthetic bacteria. CLASSIFICATION #superfamily cytochrome c' KEYWORDS chromoprotein; electron transfer; heme; iron; metalloprotein FEATURE !$119,122 #binding_site heme (Cys) (covalent) #status !8predicted\ !$123 #binding_site heme iron (His) (axial ligand) #status !8predicted SUMMARY #length 130 #molecular-weight 13409 #checksum 1842 SEQUENCE /// ENTRY CCRFCP #type complete TITLE cytochrome c' - Rhodopseudomonas palustris ORGANISM #formal_name Rhodopseudomonas palustris DATE 18-Dec-1981 #sequence_revision 18-Dec-1981 #text_change 03-Mar-2000 ACCESSIONS A00142 REFERENCE A93899 !$#authors Ambler, R.P.; Bartsch, R.G.; Daniel, M.; Kamen, M.D.; !1McLellan, L.; Meyer, T.E.; Van Beeumen, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:6854-6857 !$#title Amino acid sequences of bacterial cytochromes c' and c-556. !$#cross-references MUID:82082545; PMID:6273892 !$#accession A00142 !'##molecule_type protein !'##residues 1-125 ##label AMB !'##experimental_source strain 2.1.37 COMMENT Rhodopseudomonas is a genus of purple, nonsulfur, !1photosynthetic bacteria. CLASSIFICATION #superfamily cytochrome c' KEYWORDS chromoprotein; electron transfer; heme; iron; metalloprotein FEATURE !$113,116 #binding_site heme (Cys) (covalent) #status !8experimental\ !$117 #binding_site heme iron (His) (axial ligand) #status !8predicted SUMMARY #length 125 #molecular-weight 13131 #checksum 6646 SEQUENCE /// ENTRY CCRF6P #type complete TITLE cytochrome c556 - Rhodopseudomonas palustris ORGANISM #formal_name Rhodopseudomonas palustris DATE 18-Dec-1981 #sequence_revision 18-Dec-1981 #text_change 03-Mar-2000 ACCESSIONS A00143 REFERENCE A93899 !$#authors Ambler, R.P.; Bartsch, R.G.; Daniel, M.; Kamen, M.D.; !1McLellan, L.; Meyer, T.E.; Van Beeumen, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:6854-6857 !$#title Amino acid sequences of bacterial cytochromes c' and c-556. !$#cross-references MUID:82082545; PMID:6273892 !$#accession A00143 !'##molecule_type protein !'##residues 1-129 ##label AMB !'##experimental_source strain 2.1.37, ATCC 17007 CLASSIFICATION #superfamily cytochrome c' KEYWORDS chromoprotein; electron transfer; heme; iron; metalloprotein FEATURE !$12,121 #binding_site heme iron (Met, His) (axial ligands) !8#status predicted\ !$117,120 #binding_site heme (Cys) (covalent) #status predicted SUMMARY #length 129 #molecular-weight 14179 #checksum 2298 SEQUENCE /// ENTRY CCQFCF #type complete TITLE cytochrome c' - Rhodospirillum fulvum ORGANISM #formal_name Rhodospirillum fulvum DATE 30-Nov-1979 #sequence_revision 30-Nov-1979 #text_change 03-Mar-2000 ACCESSIONS A00144 REFERENCE A94447 !$#authors Ambler, R.P. !$#citation Abstr. E17 in Third Int. Symp. Photosynthetic Prokaryotes !1(Oxford), Nichols, J.M., ed., Univ. Liverpool, 1979 !$#accession A00144 !'##molecule_type protein !'##residues 1-128 ##label AMB CLASSIFICATION #superfamily cytochrome c' KEYWORDS chromoprotein; electron transfer; heme; iron; metalloprotein FEATURE !$118,121 #binding_site heme (Cys) (covalent) #status !8predicted\ !$122 #binding_site heme iron (His) (axial ligand) #status !8predicted SUMMARY #length 128 #molecular-weight 13410 #checksum 8203 SEQUENCE /// ENTRY CCQFCM #type complete TITLE cytochrome c' [validated] - Rhodospirillum molischianum ORGANISM #formal_name Rhodospirillum molischianum DATE 30-Nov-1979 #sequence_revision 30-Nov-1979 #text_change 15-Sep-2000 ACCESSIONS A00145 REFERENCE A94447 !$#authors Ambler, R.P. !$#citation Abstr. E17 in Third Int. Symp. Photosynthetic Prokaryotes !1(Oxford), Nichols, J.M., ed., Univ. Liverpool, 1979 !$#accession A00145 !'##molecule_type protein !'##residues 1-128 ##label AMB REFERENCE A50413 !$#authors Finzel, B.C.; Weber, P.C.; Hardman, K.D.; Salemme, F.R. !$#submission submitted to the Brookhaven Protein Data Bank, August 1985 !$#cross-references PDB:2CCY !$#contents annotation; X-ray crystallography, 1.67 angstroms, residues !12-128 REFERENCE A58638 !$#authors Finzel, B.C.; Weber, P.C.; Hardman, K.D.; Salemme, F.R. !$#journal J. Mol. Biol. (1985) 186:627-643 !$#title Structure of ferricytochrome c' from Rhodospirillum !1molischianum at 1.67 Angstroms resolution. !$#cross-references MUID:86143817; PMID:3005592 !$#contents annotation; X-ray crystallography, 1.67 angstroms COMPLEX homodimer CLASSIFICATION #superfamily cytochrome c' KEYWORDS chromoprotein; electron transfer; heme; homodimer; iron; !1metalloprotein FEATURE !$118,121 #binding_site heme (Cys) (covalent) #status !8experimental\ !$122 #binding_site heme iron (His) (axial ligand) #status !8experimental SUMMARY #length 128 #molecular-weight 13421 #checksum 8494 SEQUENCE /// ENTRY CCQFCT #type complete TITLE cytochrome c' - Rhodocyclus tenuis ORGANISM #formal_name Rhodocyclus tenuis DATE 31-May-1979 #sequence_revision 31-May-1979 #text_change 03-Mar-2000 ACCESSIONS A00146 REFERENCE A93207 !$#authors Ambler, R.P.; Meyer, T.E.; Kamen, M.D. !$#journal Nature (1979) 278:661-662 !$#title Anomalies in amino acid sequences of small cytochromes c and !1cytochromes c' from two species of purple photosynthetic !1bacteria. !$#cross-references MUID:79199668; PMID:221823 !$#accession A00146 !'##molecule_type protein !'##residues 1-133 ##label AMB COMMENT Rhodospirillum is a genus of purple, nonsulfur, !1photosynthetic bacteria. CLASSIFICATION #superfamily cytochrome c' KEYWORDS chromoprotein; electron transfer; heme; iron; metalloprotein FEATURE !$122,125 #binding_site heme (Cys) (covalent) #status !8experimental\ !$126 #binding_site heme iron (His) (axial ligand) #status !8predicted SUMMARY #length 133 #molecular-weight 14313 #checksum 8867 SEQUENCE /// ENTRY CCKRCV #type complete TITLE cytochrome c' [validated] - Chromatium vinosum ORGANISM #formal_name Chromatium vinosum DATE 31-May-1979 #sequence_revision 31-May-1979 #text_change 15-Sep-2000 ACCESSIONS A00147 REFERENCE A00147 !$#authors Ambler, R.P.; Daniel, M.; Meyer, T.E.; Bartsch, R.G.; Kamen, !1M.D. !$#journal Biochem. J. (1979) 177:819-823 !$#title The amino acid sequence of cytochrome c' from the purple !1sulphur bacterium Chromatium vinosum. !$#cross-references MUID:79187139; PMID:220951 !$#accession A00147 !'##molecule_type protein !'##residues 1-131 ##label AMB !'##experimental_source strain D, ATCC 17899 REFERENCE A51634 !$#authors Ren, Z.; McRee, D.E. !$#submission submitted to the Brookhaven Protein Data Bank, May 1992 !$#cross-references PDB:1BBH !$#contents annotation; X-ray crystallography, 1.8 angstroms, residues !11-131 REFERENCE A58604 !$#authors Ren, Z.; Meyer, T.; Mcree, D.E. !$#journal J. Mol. Biol. (1993) 234:433-445 !$#title Atomic structure of a cytochrome c' with an unusual !1ligand-controlled dimer dissociation at 1.8 angstroms !1resolution. !$#cross-references MUID:94047091; PMID:8230224 !$#contents annotation; X-ray crystallography, 1.8 angstroms COMPLEX homodimer CLASSIFICATION #superfamily cytochrome c' KEYWORDS chromoprotein; electron transfer; heme; homodimer; iron; !1metalloprotein FEATURE !$121,124 #binding_site heme (Cys) (covalent) #status !8experimental\ !$125 #binding_site heme iron (His) (axial ligand) #status !8experimental SUMMARY #length 131 #molecular-weight 13791 #checksum 4210 SEQUENCE /// ENTRY CFPM #type complete TITLE plastoquinol-plastocyanin reductase (EC 1.10.99.1) cytochrome f precursor - garden pea chloroplast ORGANISM #formal_name chloroplast Pisum sativum #common_name garden pea DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 03-Jun-2002 ACCESSIONS A00148; S19109; E48310 REFERENCE A00148 !$#authors Willey, D.L.; Auffret, A.D.; Gray, J.C. !$#journal Cell (1984) 36:555-562 !$#title Structure and topology of cytochrome f in pea chloroplast !1membranes. !$#cross-references MUID:84106860; PMID:6319031 !$#accession A00148 !'##molecule_type DNA !'##residues 1-342 ##label WIL !'##cross-references GB:K01516; NID:g343020; PIDN:AAA85363.1; !1PID:g552817 !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing REFERENCE S17919 !$#authors Nagano, Y.; Matsuno, R.; Sasaki, Y. !$#journal Curr. Genet. (1991) 20:431-436 !$#title Sequence and transcriptional analysis of the gene cluster !1trnQ-zfpA-psaI-ORF231-petA in pea chloroplasts. !$#cross-references MUID:92224289; PMID:1807835 !$#accession S19109 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-191 ##label NAG !'##cross-references EMBL:X56315 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1990 REFERENCE A48310 !$#authors Willey, D.L.; Gray, J.C. !$#journal Curr. Genet. (1989) 15:213-220 !$#title Two small open reading frames are co-transcribed with the !1pea chloroplast genes for the polypeptides of cytochrome !1b-559. !$#cross-references MUID:89354671; PMID:2766383 !$#accession E48310 !'##molecule_type DNA !'##residues 330-342 ##label WI2 !'##cross-references GB:X15767; NID:g12152; PIDN:CAA33776.1; PID:g12157 COMMENT Cytochrome f is a component of the cytochrome b/f complex, !1which transports protons across the thylakoid membrane and !1transfers electrons from photosystem II to photosystem I. It !1receives electrons from a Rieske iron-sulfur protein and !1passes them to plastocyanin; this function is very similar !1to that of mitochondrial cytochrome c1. GENETICS !$#gene petA !$#genome chloroplast CLASSIFICATION #superfamily cytochrome f KEYWORDS chloroplast; chromoprotein; electron transfer; heme; iron; !1membrane protein; metalloprotein; oxidoreductase; !1photosynthesis; thylakoid FEATURE !$1-57 #domain transit peptide (thylakoid) #status predicted !8#label TRP\ !$58-342 #product plastoquinol-plastocyanin reductase !8cytochrome f #status experimental #label MAT\ !$58-310 #domain thylakoid lumenal #status experimental #label !8THL\ !$311-327 #domain transmembrane #status predicted #label TRM\ !$328-342 #domain chloroplast stroma #status experimental !8#label CHS\ !$78,81 #binding_site heme (Cys) (covalent) #status !8predicted\ !$82 #binding_site heme iron (His) (axial ligand) #status !8predicted SUMMARY #length 342 #molecular-weight 37750 #checksum 2051 SEQUENCE /// ENTRY CFNT #type complete TITLE plastoquinol-plastocyanin reductase (EC 1.10.99.1) cytochrome f precursor - common tobacco chloroplast ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 03-Jun-2002 ACCESSIONS A00149 REFERENCE A00149 !$#authors Sugiura, M. !$#submission submitted to the EMBL Data Library, August 1986 !$#accession A00149 !'##molecule_type DNA !'##residues 1-320 ##label SUG !'##experimental_source cv. Bright Yellow 4 REFERENCE A38013 !$#authors Shinozaki, K.; Ohme, M.; Tanaka, M.; Wakasugi, T.; !1Hayashida, N.; Matsubayashi, T.; Zaita, N.; Chunwongse, J.; !1Obokata, J.; Yamaguchi-Shinozaki, K.; Ohto, C.; Torazawa, !1K.; Meng, B.Y.; Sugita, M.; Deno, H.; Kamogashira, T.; !1Yamada, K.; Kusuda, J.; Takaiwa, F.; Kato, A.; Tohdoh, N.; !1Shimada, H.; Sugiura, M. !$#journal EMBO J. (1986) 5:2043-2049 !$#title The complete nucleotide sequence of the tobacco chloroplast !1genome: its gene organization and expression. !$#contents annotation; gene organization, sites, features COMMENT Cytochrome f is a component of the cytochrome b6-f complex, !1which translocates protons across the thylakoid membrane and !1transfers electrons from photosystem II to photosystem I. It !1receives electrons from the Rieske iron-sulfur protein and !1passes them to plastocyanin; this function is very similar !1to that of mitochondrial cytochrome c1. GENETICS !$#gene petA !$#genome chloroplast CLASSIFICATION #superfamily cytochrome f KEYWORDS chloroplast; chromoprotein; electron transfer; heme; iron; !1membrane protein; metalloprotein; oxidoreductase; !1photosynthesis; thylakoid FEATURE !$1-35 #domain transit peptide (thylakoid) #status predicted !8#label TRP\ !$36-320 #product plastoquinol-plastocyanin reductase !8cytochrome f #status predicted #label MAT\ !$283-307 #domain transmembrane #status predicted #label TRM\ !$56,59 #binding_site heme (Cys) (covalent) #status !8predicted\ !$60 #binding_site heme iron (His) (axial ligand) #status !8predicted SUMMARY #length 320 #molecular-weight 35246 #checksum 9992 SEQUENCE /// ENTRY CFRZ #type complete TITLE plastoquinol-plastocyanin reductase (EC 1.10.99.1) cytochrome f precursor - rice chloroplast ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 03-Jun-2002 ACCESSIONS JQ0239; S05119; A29496 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0239 !'##molecule_type DNA !'##residues 1-320 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05119 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-320 ##label HIR !'##cross-references EMBL:X15901; NID:g11957; PIDN:CAA33961.1; !1PID:g12000 !'##experimental_source cv. Nihonbare REFERENCE A91569 !$#authors Wu, N.H.; Cote, J.C.; Wu, R. !$#journal Gene (1986) 50:271-278 !$#title Nucleotide sequence of the rice cytochrome f gene and the !1presence of sequence variation near this gene. !$#cross-references MUID:87219885; PMID:2884170 !$#accession A29496 !'##molecule_type DNA !'##residues 1-13,'I',15-19,'D',21-320 ##label WUN !'##cross-references GB:M15955; NID:g343206; PIDN:AAA84590.1; !1PID:g552858 !'##experimental_source cv. Labelle COMMENT Cytochrome f is a component of the cytochrome b6-f complex, !1which translocates electrons from photosystem II to !1photosystem I. It receives electrons from the Rieske !1iron-sulfur protein and passes them to plastocyanin; this !1function is very similar to that of mitochondrial cytochrome !1c1. GENETICS !$#gene petA !$#map_position CP59601-60563 !$#genome chloroplast CLASSIFICATION #superfamily cytochrome f KEYWORDS chloroplast; chromoprotein; electron transfer; heme; iron; !1membrane protein; metalloprotein; oxidoreductase; !1photosynthesis; thylakoid FEATURE !$1-35 #domain transit peptide (thylakoid) #status predicted !8#label TRP\ !$36-320 #product cytochrome f #status predicted #label MAT\ !$289-305 #domain transmembrane #status predicted #label TRM\ !$56,59 #binding_site heme (Cys) (covalent) #status !8predicted\ !$60 #binding_site heme iron (His) (axial ligand) #status !8predicted SUMMARY #length 320 #molecular-weight 35467 #checksum 2436 SEQUENCE /// ENTRY CFLV #type complete TITLE plastoquinol-plastocyanin reductase (EC 1.10.99.1) cytochrome f precursor - liverwort (Marchantia polymorpha) chloroplast ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 03-Jun-2002 ACCESSIONS S01534; A00150 REFERENCE S01529 !$#authors Fukuzawa, H.; Kohchi, T.; Sano, T.; Shirai, H.; Umesono, K.; !1Inokuchi, H.; Ozeki, H.; Ohyama, K. !$#journal J. Mol. Biol. (1988) 203:333-351 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. III. Gene organization of the large !1single copy region from rbcL to trnI(CAU). !$#cross-references MUID:89068687; PMID:3199436 !$#accession S01534 !'##molecule_type DNA !'##residues 1-320 ##label FUK !'##cross-references EMBL:X04465; NID:g11640; PIDN:CAA28097.1; !1PID:g11685 REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features GENETICS !$#gene petA !$#genome chloroplast CLASSIFICATION #superfamily cytochrome f KEYWORDS chloroplast; chromoprotein; electron transfer; heme; iron; !1membrane protein; metalloprotein; oxidoreductase; !1photosynthesis; thylakoid FEATURE !$1-35 #domain transit peptide (thylakoid) #status predicted !8#label TRP\ !$36-320 #product plastoquinol-plastocyanin reductase !8cytochrome f #status predicted #label MAT\ !$289-305 #domain transmembrane #status predicted #label TRM\ !$56,59 #binding_site heme (Cys) (covalent) #status !8predicted\ !$60 #binding_site heme iron (His) (axial ligand) #status !8predicted SUMMARY #length 320 #molecular-weight 35431 #checksum 9212 SEQUENCE /// ENTRY CBEC62 #type complete TITLE cytochrome b562 precursor [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 24-Apr-1984 #sequence_revision 02-Jul-1996 #text_change 01-Mar-2002 ACCESSIONS S19544; S25107; S56462; A33153; A00195; G65235 REFERENCE S19544 !$#authors Nikkila, H.; Gennis, R.B.; Sligar, S.G. !$#journal Eur. J. Biochem. (1991) 202:309-313 !$#title Cloning and expression of the gene encoding the soluble !1cytochrome b(562) of Escherichia coli. !$#cross-references MUID:92104149; PMID:1761034 !$#accession S19544 !'##molecule_type DNA !'##residues 1-128 ##label NIK !'##cross-references EMBL:S74736; NID:g241592; PIDN:AAB20782.1; !1PID:g241593 REFERENCE S25107 !$#authors Trower, M.K. !$#submission submitted to the EMBL Data Library, July 1992 !$#accession S25107 !'##molecule_type DNA !'##residues 1-128 ##label TRO !'##cross-references EMBL:X67290; NID:g41194; PIDN:CAA47706.1; !1PID:g41195 !'##experimental_source ssp. B strain OP7 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56462 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 29-38,'V',40-121,'S',123-124,'K',126-128 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97133.1; !1PID:g537078 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A33153 !$#authors Lederer, F.; Glatigny, A.; Bethge, P.H.; Bellamy, H.D.; !1Mathews, F.S. !$#journal J. Mol. Biol. (1981) 148:427-448 !$#title Improvement of the 2.5 angstrom resolution model of !1cytochrome b-562 by redetermining the primary structure and !1using molecular graphics. !$#cross-references MUID:82078041; PMID:7031264 !$#accession A33153 !'##molecule_type protein !'##residues 23-128 ##label LED !'##note sequence revision; X-ray crystallography, 2.5 angstroms REFERENCE A90166 !$#authors Itagaki, E.; Hager, L.P. !$#journal Biochem. Biophys. Res. Commun. (1968) 32:1013-1019 !$#title The amino acid sequence of cytochrome b562 of Escherichia !1coli. !$#cross-references MUID:69077911; PMID:4882876 !$#accession A00195 !'##molecule_type protein !'##residues 23-27,'D',29,'Q',31-42,'BBZKAND',45-49,'L',54-60,'N',62-64, !1'K',65-75,'N',77,'QP',80-92,'E',94-112,'EA',115-123,'K', !1124-128 ##label ITA REFERENCE A50393 !$#authors Hamada, K.; Bethge, P.H.; Mathews, F.S. !$#submission submitted to the Brookhaven Protein Data Bank, January 1990 !$#cross-references PDB:256B !$#contents annotation; X-ray crystallography, 1.4 angstroms, residues !123-128 REFERENCE A92248 !$#authors Mathews, F.S.; Bethge, P.H.; Czerwinski, E.W. !$#journal J. Biol. Chem. (1979) 254:1699-1706 !$#title The structure of cytochrome b562 from Escherichia coli at !12.5A resolution. !$#cross-references MUID:79109778; PMID:368073 !$#contents annotation; X-ray crystallography, 2.5 angstroms REFERENCE A51603 !$#authors Wand, A.J.; Feng, Y.; Sligar, S.G. !$#submission submitted to the Brookhaven Protein Data Bank, October 1993 !$#cross-references PDB:1APC !$#contents annotation; conformation by (1)H-NMR, residues 23-128 REFERENCE A58616 !$#authors Feng, Y.; Sligar, S.G.; Wand, A.J. !$#journal Nat. Struct. Biol. (1994) 1:30-35 !$#title Solution structure of apocytochrome b562. !$#cross-references MUID:95384751; PMID:7656004 !$#contents annotation; conformation by (1)H-NMR, apo form REFERENCE A58617 !$#authors Feng, Y.; Wand, A.J.; Sligar, S.G. !$#journal Biochemistry (1991) 30:7711-7717 !$#title (1)H and (15)N NMR resonance assignments and preliminary !1structural characterization of Escherichia coli !1apocytochrome b562. !$#cross-references MUID:91329334; PMID:1868051 !$#contents annotation; conformation by (1)H-NMR REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65235 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 29-38,'V',40-121,'S',123-124,'K',126-128 ##label BLAT !'##cross-references GB:AE000495; GB:U00096; NID:g2367361; !1PIDN:AAC77193.1; PID:g1790684; UWGP:b4236 !'##experimental_source strain K-12, substrain MG1655 COMMENT This periplasmic electron transfer protein appears to be !1nonessential. GENETICS !$#gene cybC CLASSIFICATION #superfamily cytochrome b562 KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; monomer; periplasmic space FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-128 #product cytochrome b562 #status experimental #label !8MAT\ !$29,124 #binding_site heme iron (Met, His) (axial ligands) !8#status experimental SUMMARY #length 128 #molecular-weight 14061 #checksum 1345 SEQUENCE /// ENTRY CBHU #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - human mitochondrion ORGANISM #formal_name mitochondrion Homo sapiens #common_name man DATE 22-May-1981 #sequence_revision 23-Oct-1981 #text_change 03-Jun-2002 ACCESSIONS A00151; I57452 REFERENCE A00151 !$#authors Anderson, S.; Bankier, A.T.; Barrell, B.G.; de Bruijn, !1M.H.L.; Coulson, A.R.; Drouin, J.; Eperon, I.C.; Nierlich, !1D.P.; Roe, B.A.; Sanger, F.; Schreier, P.H.; Smith, A.J.H.; !1Staden, R.; Young, I.G. !$#journal Nature (1981) 290:457-465 !$#title Sequence and organization of the human mitochondrial genome. !$#cross-references MUID:81173052; PMID:7219534 !$#accession A00151 !'##molecule_type DNA !'##residues 1-380 ##label AND !'##cross-references EMBL:V00662; NID:g13003; PIDN:CAA24038.1; !1PID:g13016; GSPDB:GN00100 REFERENCE I57452 !$#authors Spurr, N.K.; Bodmer, W.F. !$#journal Mol. Biol. Med. (1984) 2:239-249 !$#title Serendipitous cloning of a mitochondrial cDNA and its !1polymorphism. !$#cross-references MUID:86064879; PMID:6100559 !$#accession I57452 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 269-380 ##label SPU !'##cross-references GB:M28016; NID:g337203; PIDN:AAA31851.1; !1PID:g552606 GENETICS !$#gene GDB:MTCYB !'##cross-references GDB:118906 !$#map_position MTH14747-15887 !$#genome mitochondrion !$#genetic_code SGC1 COMPLEX the transmembrane complex includes cytochrome b, cytochrome !1c1 (see PIR:S00680), Rieske iron-sulfur protein, and other !1accessory proteins FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$11-339 #domain cytochrome b homology #label CBH\ !$11-209 #domain cytochrome b6 homology #label CB6\ !$36-52 #domain transmembrane #status predicted #label TM1\ !$81-99 #domain transmembrane #status predicted #label TM2\ !$117-133 #domain transmembrane #status predicted #label TM3\ !$178-200 #domain transmembrane #status predicted #label TM4\ !$221-339 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$229-245 #domain transmembrane #status predicted #label TM5\ !$288-304 #domain transmembrane #status predicted #label TM6\ !$323-343 #domain transmembrane #status predicted #label TM7\ !$353-369 #domain transmembrane #status predicted #label TM8\ !$83,182 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$97,196 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 380 #molecular-weight 42729 #checksum 988 SEQUENCE /// ENTRY CBBO #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - bovine mitochondrion ALTERNATE_NAMES cytochrome bc1 complex cytochrome b component; mitrochondrial complex III cytochrome b subunit; ubiquinol-cytochrome-c oxidoreductase cytochrome b ORGANISM #formal_name mitochondrion Bos primigenius taurus #common_name cattle DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 03-Jun-2002 ACCESSIONS A00152; S27097; A49734 REFERENCE A00152 !$#authors Anderson, S.; de Bruijn, M.H.L.; Coulson, A.R.; Eperon, !1I.C.; Sanger, F.; Young, I.G. !$#journal J. Mol. Biol. (1982) 156:683-717 !$#title Complete sequence of bovine mitochondrial DNA. Conserved !1features of the mammalian mitochondrial genome. !$#cross-references MUID:83010260; PMID:7120390 !$#accession A00152 !'##molecule_type DNA !'##residues 1-379 ##label AND !'##cross-references GB:J01394; NID:g336430; PIDN:AAB59280.1; !1PID:g336443; EMBL:V00654; NID:g12800; PID:g12813 REFERENCE S17405 !$#authors Irwin, D.M.; Kocher, T.D.; Wilson, A.C. !$#journal J. Mol. Evol. (1991) 32:128-144 !$#title Evolution of the cytochrome b gene of mammals. !$#cross-references MUID:91178817; PMID:1901092 !$#accession S27097 !'##molecule_type DNA !'##residues 1-379 ##label IRW !'##note this sequence and translation are not annotated in GenBank !1release 111.0, but do represent a separate determination REFERENCE A49734 !$#authors He, D.Y.; Yu, L.; Yu, C.A. !$#journal J. Biol. Chem. (1994) 269:2292-2298 !$#title Ubiquinone binding domains in bovine heart mitochondrial !1cytochrome b. !$#cross-references MUID:94124591; PMID:8294488 !$#accession A49734 !'##molecule_type protein !'##residues 142-146;327-332 ##label HEA REFERENCE A58900 !$#authors Xia, D.; Yu, C.A.; Kim, H.; Xia, J.Z.; Kachurin, A.M.; !1Zhang, L.; Yu, L.; Deisenhofer, J. !$#journal Science (1997) 277:60-66 !$#title Crystal structure of the cytochrome bc1 complex from bovine !1heart mitochondria. !$#cross-references MUID:97349328; PMID:9204897 !$#contents annotation; X-ray crystallography, 2.9 angstroms GENETICS !$#genome mitochondrion !$#genetic_code SGC1 COMPLEX the transmembrane complex includes cytochrome b, cytochrome !1c1 (see PIR:CCBO1), Rieske iron-sulfur protein (see !1PIR:A34660), and other accessory proteins (see PIR:CCBO11, !1PIR:CCBO17, PIR:A24864, PIR:ZPBOC1, and PIR:ZPBOC2) FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$11-339 #domain cytochrome b homology #label CBH\ !$11-209 #domain cytochrome b6 homology #label CB6\ !$36-52 #domain transmembrane #status predicted #label TM1\ !$81-99 #domain transmembrane #status predicted #label TM2\ !$117-133 #domain transmembrane #status predicted #label TM3\ !$178-200 #domain transmembrane #status predicted #label TM4\ !$221-339 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$229-245 #domain transmembrane #status predicted #label TM5\ !$288-304 #domain transmembrane #status predicted #label TM6\ !$323-343 #domain transmembrane #status predicted #label TM7\ !$353-369 #domain transmembrane #status predicted #label TM8\ !$83,182 #binding_site heme iron (His) (axial ligands) (low !8potential) #status experimental\ !$97,196 #binding_site heme iron (His) (axial ligands) (high !8potential) #status experimental SUMMARY #length 379 #molecular-weight 42590 #checksum 6353 SEQUENCE /// ENTRY CBMS #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - mouse mitochondrion ORGANISM #formal_name mitochondrion Mus musculus #common_name house mouse DATE 02-Apr-1982 #sequence_revision 02-Apr-1982 #text_change 03-Jun-2002 ACCESSIONS A00153 REFERENCE A00153 !$#authors Bibb, M.J.; Van Etten, R.A.; Wright, C.T.; Walberg, M.W.; !1Clayton, D.A. !$#journal Cell (1981) 26:167-180 !$#title Sequence and gene organization of mouse mitochondrial DNA. !$#cross-references MUID:82137051; PMID:7332926 !$#accession A00153 !'##molecule_type DNA !'##residues 1-381 ##label BIB !'##cross-references GB:J01420; NID:g342520; PIDN:AAB48656.1; !1PID:g896302; EMBL:V00711; NID:g13838; PID:g13851 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$11-339 #domain cytochrome b homology #label CBH\ !$11-209 #domain cytochrome b6 homology #label CB6\ !$36-52 #domain transmembrane #status predicted #label TM1\ !$81-99 #domain transmembrane #status predicted #label TM2\ !$117-133 #domain transmembrane #status predicted #label TM3\ !$178-200 #domain transmembrane #status predicted #label TM4\ !$221-339 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$229-245 #domain transmembrane #status predicted #label TM5\ !$288-304 #domain transmembrane #status predicted #label TM6\ !$323-343 #domain transmembrane #status predicted #label TM7\ !$353-369 #domain transmembrane #status predicted #label TM8\ !$83,182 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$97,196 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 381 #molecular-weight 43209 #checksum 2005 SEQUENCE /// ENTRY CBRT #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - rat mitochondrion ORGANISM #formal_name mitochondrion Rattus norvegicus #common_name Norway rat DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 03-Jun-2002 ACCESSIONS A00154; S04759 REFERENCE A00154 !$#authors Koike, K.; Kobayashi, M.; Yaginuma, K.; Taira, M.; Yoshida, !1E.; Imai, M. !$#journal Gene (1982) 20:177-185 !$#title Nucleotide sequence and evolution of the rat mitochondrial !1cytochrome b gene containing the ochre termination codon. !$#cross-references MUID:83158755; PMID:6299885 !$#accession A00154 !'##molecule_type DNA !'##residues 1-380 ##label KOI !'##cross-references GB:J01436; NID:g343168; PIDN:AAA99907.1; !1PID:g829020 !'##note the authors translated the codon ATA for residue 42 as Ile, CAC !1for residue 54 as Asn, ATA for residue 89 as Ile, ATT for !1residue 284 as Leu, ATC for residue 295 as Ala, and TTA for !1residue 296 as Phe. In another figure, the amino acids at !1all these positions except position 89, which was shown as !1Leu, agreed with the nucleic acid translation. In addition, !1the sequence differed from the translation in having 11-Glu REFERENCE S04747 !$#authors Gadaleta, G.; Pepe, G.; De Candia, G.; Quagliariello, C.; !1Sbisa, E.; Saccone, C. !$#journal J. Mol. Evol. (1989) 28:497-516 !$#title The complete nucleotide sequence of the Rattus norvegicus !1mitochondrial genome: cryptic signals revealed by !1comparative analysis between vertebrates. !$#cross-references MUID:89362487; PMID:2504926 !$#accession S04759 !'##molecule_type DNA !'##residues 1-82,'Q',84-152,'I',154-380 ##label GAD !'##cross-references EMBL:X14848; NID:g854269; PIDN:CAA32966.1; !1PID:g639986 GENETICS !$#gene cob !$#map_position 87-94 !$#genome mitochondrion !$#genetic_code SGC1 FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$11-339 #domain cytochrome b homology #label CBH\ !$11-209 #domain cytochrome b6 homology #label CB6\ !$36-52 #domain transmembrane #status predicted #label TM1\ !$81-99 #domain transmembrane #status predicted #label TM2\ !$117-133 #domain transmembrane #status predicted #label TM3\ !$178-200 #domain transmembrane #status predicted #label TM4\ !$221-339 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$229-245 #domain transmembrane #status predicted #label TM5\ !$288-304 #domain transmembrane #status predicted #label TM6\ !$323-343 #domain transmembrane #status predicted #label TM7\ !$353-369 #domain transmembrane #status predicted #label TM8\ !$83,182 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$97,196 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 380 #molecular-weight 42985 #checksum 718 SEQUENCE /// ENTRY S17408 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - black rhinoceros mitochondrion ORGANISM #formal_name mitochondrion Diceros bicornis #common_name black rhinoceros DATE 29-Jan-1993 #sequence_revision 20-Aug-1994 #text_change 03-Jun-2002 ACCESSIONS S17408 REFERENCE S17405 !$#authors Irwin, D.M.; Kocher, T.D.; Wilson, A.C. !$#journal J. Mol. Evol. (1991) 32:128-144 !$#title Evolution of the cytochrome b gene of mammals. !$#cross-references MUID:91178817; PMID:1901092 !$#accession S17408 !'##status translation not shown !'##molecule_type DNA !'##residues 1-379 ##label IRW !'##cross-references EMBL:X56283; NID:g12903; PIDN:CAA39730.1; !1PID:g578698 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$11-339 #domain cytochrome b homology #label CBH\ !$11-209 #domain cytochrome b6 homology #label CB6\ !$36-52 #domain transmembrane #status predicted #label TM1\ !$81-99 #domain transmembrane #status predicted #label TM2\ !$117-133 #domain transmembrane #status predicted #label TM3\ !$178-200 #domain transmembrane #status predicted #label TM4\ !$221-339 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$229-245 #domain transmembrane #status predicted #label TM5\ !$288-304 #domain transmembrane #status predicted #label TM6\ !$323-343 #domain transmembrane #status predicted #label TM7\ !$353-369 #domain transmembrane #status predicted #label TM8\ !$83,182 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$97,196 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 379 #molecular-weight 42663 #checksum 6540 SEQUENCE /// ENTRY S17410 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - Grevy's zebra mitochondrion ORGANISM #formal_name mitochondrion Equus grevyi #common_name Grevy's zebra DATE 29-Jan-1993 #sequence_revision 20-Aug-1994 #text_change 03-Jun-2002 ACCESSIONS S17410 REFERENCE S17405 !$#authors Irwin, D.M.; Kocher, T.D.; Wilson, A.C. !$#journal J. Mol. Evol. (1991) 32:128-144 !$#title Evolution of the cytochrome b gene of mammals. !$#cross-references MUID:91178817; PMID:1901092 !$#accession S17410 !'##status translation not shown !'##molecule_type DNA !'##residues 1-379 ##label IRW !'##cross-references EMBL:X56282; NID:g12948; PIDN:CAA39729.1; !1PID:g578705 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$11-339 #domain cytochrome b homology #label CBH\ !$11-209 #domain cytochrome b6 homology #label CB6\ !$36-52 #domain transmembrane #status predicted #label TM1\ !$81-99 #domain transmembrane #status predicted #label TM2\ !$117-133 #domain transmembrane #status predicted #label TM3\ !$178-200 #domain transmembrane #status predicted #label TM4\ !$221-339 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$229-245 #domain transmembrane #status predicted #label TM5\ !$288-304 #domain transmembrane #status predicted #label TM6\ !$323-343 #domain transmembrane #status predicted #label TM7\ !$353-369 #domain transmembrane #status predicted #label TM8\ !$83,182 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$97,196 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 379 #molecular-weight 42743 #checksum 7279 SEQUENCE /// ENTRY S17419 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - Balabac chevrotain mitochondrion ORGANISM #formal_name mitochondrion Tragulus napu #common_name Balabac chevrotain DATE 29-Jan-1993 #sequence_revision 20-Aug-1994 #text_change 03-Jun-2002 ACCESSIONS S17419 REFERENCE S17405 !$#authors Irwin, D.M.; Kocher, T.D.; Wilson, A.C. !$#journal J. Mol. Evol. (1991) 32:128-144 !$#title Evolution of the cytochrome b gene of mammals. !$#cross-references MUID:91178817; PMID:1901092 !$#accession S17419 !'##status translation not shown !'##molecule_type DNA !'##residues 1-379 ##label IRW !'##cross-references EMBL:X56288; NID:g13836; PIDN:CAA39735.1; !1PID:g578830 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$11-339 #domain cytochrome b homology #label CBH\ !$11-209 #domain cytochrome b6 homology #label CB6\ !$36-52 #domain transmembrane #status predicted #label TM1\ !$81-99 #domain transmembrane #status predicted #label TM2\ !$117-133 #domain transmembrane #status predicted #label TM3\ !$178-200 #domain transmembrane #status predicted #label TM4\ !$221-339 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$229-245 #domain transmembrane #status predicted #label TM5\ !$288-304 #domain transmembrane #status predicted #label TM6\ !$323-343 #domain transmembrane #status predicted #label TM7\ !$353-369 #domain transmembrane #status predicted #label TM8\ !$83,182 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$97,196 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 379 #molecular-weight 42580 #checksum 5826 SEQUENCE /// ENTRY S17405 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - pronghorn mitochondrion ORGANISM #formal_name mitochondrion Antilocapra americana #common_name pronghorn DATE 29-Jan-1993 #sequence_revision 20-Aug-1994 #text_change 03-Jun-2002 ACCESSIONS S17405 REFERENCE S17405 !$#authors Irwin, D.M.; Kocher, T.D.; Wilson, A.C. !$#journal J. Mol. Evol. (1991) 32:128-144 !$#title Evolution of the cytochrome b gene of mammals. !$#cross-references MUID:91178817; PMID:1901092 !$#accession S17405 !'##status translation not shown !'##molecule_type DNA !'##residues 1-379 ##label IRW !'##cross-references EMBL:X56286; NID:g12624; PIDN:CAA39733.1; !1PID:g578675 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$11-339 #domain cytochrome b homology #label CBH\ !$11-209 #domain cytochrome b6 homology #label CB6\ !$36-52 #domain transmembrane #status predicted #label TM1\ !$81-99 #domain transmembrane #status predicted #label TM2\ !$117-133 #domain transmembrane #status predicted #label TM3\ !$178-200 #domain transmembrane #status predicted #label TM4\ !$221-339 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$229-245 #domain transmembrane #status predicted #label TM5\ !$288-304 #domain transmembrane #status predicted #label TM6\ !$323-343 #domain transmembrane #status predicted #label TM7\ !$353-369 #domain transmembrane #status predicted #label TM8\ !$83,182 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$97,196 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 379 #molecular-weight 42845 #checksum 4426 SEQUENCE /// ENTRY S43267 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - Caperea marginata mitochondrion ORGANISM #formal_name mitochondrion Caperea marginata DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S43267 REFERENCE S43261 !$#authors Arnason, U.; Gullberg, A. !$#journal Nature (1994) 367:726-728 !$#title Relationship of baleen whales established by cytochrome b !1gene sequence comparison. !$#cross-references MUID:94150700; PMID:8107866 !$#accession S43267 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-379 ##label ARN !'##cross-references EMBL:X75586; NID:g457773; PIDN:CAA53262.1; !1PID:g578663 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1993 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1membrane-associated complex; metalloprotein; mitochondrion; !1oxidative phosphorylation; oxidoreductase; respiratory !1chain; transmembrane protein FEATURE !$11-339 #domain cytochrome b homology #label CBH\ !$11-209 #domain cytochrome b6 homology #label CB6\ !$36-52 #domain transmembrane #status predicted #label TM1\ !$81-99 #domain transmembrane #status predicted #label TM2\ !$117-133 #domain transmembrane #status predicted #label TM3\ !$178-200 #domain transmembrane #status predicted #label TM4\ !$221-339 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$229-245 #domain transmembrane #status predicted #label TM5\ !$288-304 #domain transmembrane #status predicted #label TM6\ !$323-343 #domain transmembrane #status predicted #label TM7\ !$353-369 #domain transmembrane #status predicted #label TM8\ !$83,182 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$97,196 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 379 #molecular-weight 42913 #checksum 5797 SEQUENCE /// ENTRY S43265 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - Balaena glacialis mitochondrion ORGANISM #formal_name mitochondrion Balaena glacialis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S43265 REFERENCE S43261 !$#authors Arnason, U.; Gullberg, A. !$#journal Nature (1994) 367:726-728 !$#title Relationship of baleen whales established by cytochrome b !1gene sequence comparison. !$#cross-references MUID:94150700; PMID:8107866 !$#accession S43265 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-379 ##label ARN !'##cross-references EMBL:X75587 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1993 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1membrane-associated complex; metalloprotein; mitochondrion; !1oxidative phosphorylation; oxidoreductase; respiratory !1chain; transmembrane protein FEATURE !$11-339 #domain cytochrome b homology #label CBH\ !$11-209 #domain cytochrome b6 homology #label CB6\ !$36-52 #domain transmembrane #status predicted #label TM1\ !$81-99 #domain transmembrane #status predicted #label TM2\ !$117-133 #domain transmembrane #status predicted #label TM3\ !$178-200 #domain transmembrane #status predicted #label TM4\ !$221-339 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$229-245 #domain transmembrane #status predicted #label TM5\ !$288-304 #domain transmembrane #status predicted #label TM6\ !$323-343 #domain transmembrane #status predicted #label TM7\ !$353-369 #domain transmembrane #status predicted #label TM8\ !$83,182 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$97,196 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 379 #molecular-weight 42893 #checksum 5406 SEQUENCE /// ENTRY S17409 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - fallow deer mitochondrion ORGANISM #formal_name mitochondrion Dama dama #common_name fallow deer DATE 29-Jan-1993 #sequence_revision 20-Aug-1994 #text_change 03-Jun-2002 ACCESSIONS S17409 REFERENCE S17405 !$#authors Irwin, D.M.; Kocher, T.D.; Wilson, A.C. !$#journal J. Mol. Evol. (1991) 32:128-144 !$#title Evolution of the cytochrome b gene of mammals. !$#cross-references MUID:91178817; PMID:1901092 !$#accession S17409 !'##status translation not shown !'##molecule_type DNA !'##residues 1-379 ##label IRW !'##cross-references EMBL:X56290; NID:g12907; PIDN:CAA39737.1; !1PID:g578699 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$11-339 #domain cytochrome b homology #label CBH\ !$11-209 #domain cytochrome b6 homology #label CB6\ !$36-52 #domain transmembrane #status predicted #label TM1\ !$81-99 #domain transmembrane #status predicted #label TM2\ !$117-133 #domain transmembrane #status predicted #label TM3\ !$178-200 #domain transmembrane #status predicted #label TM4\ !$221-339 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$229-245 #domain transmembrane #status predicted #label TM5\ !$288-304 #domain transmembrane #status predicted #label TM6\ !$323-343 #domain transmembrane #status predicted #label TM7\ !$353-369 #domain transmembrane #status predicted #label TM8\ !$83,182 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$97,196 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 379 #molecular-weight 42834 #checksum 5818 SEQUENCE /// ENTRY S43266 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - Balaena mysticetus mitochondrion ORGANISM #formal_name mitochondrion Balaena mysticetus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S43266 REFERENCE S43261 !$#authors Arnason, U.; Gullberg, A. !$#journal Nature (1994) 367:726-728 !$#title Relationship of baleen whales established by cytochrome b !1gene sequence comparison. !$#cross-references MUID:94150700; PMID:8107866 !$#accession S43266 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-379 ##label ARN !'##cross-references EMBL:X75588; NID:g457770; PIDN:CAA53264.1; !1PID:g578577 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1993 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1membrane-associated complex; metalloprotein; mitochondrion; !1oxidative phosphorylation; oxidoreductase; respiratory !1chain; transmembrane protein FEATURE !$11-339 #domain cytochrome b homology #label CBH\ !$11-209 #domain cytochrome b6 homology #label CB6\ !$36-52 #domain transmembrane #status predicted #label TM1\ !$81-99 #domain transmembrane #status predicted #label TM2\ !$117-133 #domain transmembrane #status predicted #label TM3\ !$178-200 #domain transmembrane #status predicted #label TM4\ !$221-339 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$229-245 #domain transmembrane #status predicted #label TM5\ !$288-304 #domain transmembrane #status predicted #label TM6\ !$323-343 #domain transmembrane #status predicted #label TM7\ !$353-369 #domain transmembrane #status predicted #label TM8\ !$83,182 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$97,196 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 379 #molecular-weight 42835 #checksum 4110 SEQUENCE /// ENTRY S17411 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - giraffe mitochondrion ORGANISM #formal_name mitochondrion Giraffa camelopardalis #common_name giraffe DATE 29-Jan-1993 #sequence_revision 20-Aug-1994 #text_change 03-Jun-2002 ACCESSIONS S17411 REFERENCE S17405 !$#authors Irwin, D.M.; Kocher, T.D.; Wilson, A.C. !$#journal J. Mol. Evol. (1991) 32:128-144 !$#title Evolution of the cytochrome b gene of mammals. !$#cross-references MUID:91178817; PMID:1901092 !$#accession S17411 !'##status translation not shown !'##molecule_type DNA !'##residues 1-379 ##label IRW !'##cross-references EMBL:X56287; NID:g12951; PIDN:CAA39734.1; !1PID:g578707 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$11-339 #domain cytochrome b homology #label CBH\ !$11-209 #domain cytochrome b6 homology #label CB6\ !$36-52 #domain transmembrane #status predicted #label TM1\ !$81-99 #domain transmembrane #status predicted #label TM2\ !$117-133 #domain transmembrane #status predicted #label TM3\ !$178-200 #domain transmembrane #status predicted #label TM4\ !$221-339 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$229-245 #domain transmembrane #status predicted #label TM5\ !$288-304 #domain transmembrane #status predicted #label TM6\ !$323-343 #domain transmembrane #status predicted #label TM7\ !$353-369 #domain transmembrane #status predicted #label TM8\ !$83,182 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$97,196 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 379 #molecular-weight 43034 #checksum 6651 SEQUENCE /// ENTRY S43268 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - California gray whale mitochondrion ORGANISM #formal_name mitochondrion Eschrichtius robustus, Eschrichtius gibbosus #common_name California gray whale DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S43268 REFERENCE S43261 !$#authors Arnason, U.; Gullberg, A. !$#journal Nature (1994) 367:726-728 !$#title Relationship of baleen whales established by cytochrome b !1gene sequence comparison. !$#cross-references MUID:94150700; PMID:8107866 !$#accession S43268 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-379 ##label ARN !'##cross-references EMBL:X75585; NID:g457777; PIDN:CAA53261.1; !1PID:g578673 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1993 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1membrane-associated complex; metalloprotein; mitochondrion; !1oxidative phosphorylation; oxidoreductase; respiratory !1chain; transmembrane protein FEATURE !$11-339 #domain cytochrome b homology #label CBH\ !$11-209 #domain cytochrome b6 homology #label CB6\ !$36-52 #domain transmembrane #status predicted #label TM1\ !$81-99 #domain transmembrane #status predicted #label TM2\ !$117-133 #domain transmembrane #status predicted #label TM3\ !$178-200 #domain transmembrane #status predicted #label TM4\ !$221-339 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$229-245 #domain transmembrane #status predicted #label TM5\ !$288-304 #domain transmembrane #status predicted #label TM6\ !$323-343 #domain transmembrane #status predicted #label TM7\ !$353-369 #domain transmembrane #status predicted #label TM8\ !$83,182 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$97,196 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 379 #molecular-weight 42900 #checksum 6505 SEQUENCE /// ENTRY S17414 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - mule deer mitochondrion ORGANISM #formal_name mitochondrion Odocoileus hemionus #common_name mule deer DATE 29-Jan-1993 #sequence_revision 20-Aug-1994 #text_change 03-Jun-2002 ACCESSIONS S17414 REFERENCE S17405 !$#authors Irwin, D.M.; Kocher, T.D.; Wilson, A.C. !$#journal J. Mol. Evol. (1991) 32:128-144 !$#title Evolution of the cytochrome b gene of mammals. !$#cross-references MUID:91178817; PMID:1901092 !$#accession S17414 !'##status translation not shown !'##molecule_type DNA !'##residues 1-379 ##label IRW !'##cross-references EMBL:X56291; NID:g13198; PIDN:CAA39738.1; !1PID:g578739 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$11-339 #domain cytochrome b homology #label CBH\ !$11-209 #domain cytochrome b6 homology #label CB6\ !$36-52 #domain transmembrane #status predicted #label TM1\ !$81-99 #domain transmembrane #status predicted #label TM2\ !$117-133 #domain transmembrane #status predicted #label TM3\ !$178-200 #domain transmembrane #status predicted #label TM4\ !$221-339 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$229-245 #domain transmembrane #status predicted #label TM5\ !$288-304 #domain transmembrane #status predicted #label TM6\ !$323-343 #domain transmembrane #status predicted #label TM7\ !$353-369 #domain transmembrane #status predicted #label TM8\ !$83,182 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$97,196 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 379 #molecular-weight 42715 #checksum 5364 SEQUENCE /// ENTRY S17407 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - goat mitochondrion ORGANISM #formal_name mitochondrion Capra aegagrus hircus #common_name domestic goat DATE 29-Jan-1993 #sequence_revision 20-Aug-1994 #text_change 03-Jun-2002 ACCESSIONS S17407 REFERENCE S17405 !$#authors Irwin, D.M.; Kocher, T.D.; Wilson, A.C. !$#journal J. Mol. Evol. (1991) 32:128-144 !$#title Evolution of the cytochrome b gene of mammals. !$#cross-references MUID:91178817; PMID:1901092 !$#accession S17407 !'##status translation not shown !'##molecule_type DNA !'##residues 1-379 ##label IRW !'##cross-references EMBL:X56289; NID:g12871; PIDN:CAA39736.1; !1PID:g578696 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$11-339 #domain cytochrome b homology #label CBH\ !$11-209 #domain cytochrome b6 homology #label CB6\ !$36-52 #domain transmembrane #status predicted #label TM1\ !$81-99 #domain transmembrane #status predicted #label TM2\ !$117-133 #domain transmembrane #status predicted #label TM3\ !$178-200 #domain transmembrane #status predicted #label TM4\ !$221-339 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$229-245 #domain transmembrane #status predicted #label TM5\ !$288-304 #domain transmembrane #status predicted #label TM6\ !$323-343 #domain transmembrane #status predicted #label TM7\ !$353-369 #domain transmembrane #status predicted #label TM8\ !$83,182 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$97,196 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 379 #molecular-weight 42871 #checksum 7126 SEQUENCE /// ENTRY S43269 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - humpback whale mitochondrion ORGANISM #formal_name mitochondrion Megaptera novaeangliae #common_name humpback whale DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S43269 REFERENCE S43261 !$#authors Arnason, U.; Gullberg, A. !$#journal Nature (1994) 367:726-728 !$#title Relationship of baleen whales established by cytochrome b !1gene sequence comparison. !$#cross-references MUID:94150700; PMID:8107866 !$#accession S43269 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-379 ##label ARN !'##cross-references EMBL:X75584; NID:g457794; PIDN:CAA53260.1; !1PID:g578841 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1993 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1membrane-associated complex; metalloprotein; mitochondrion; !1oxidative phosphorylation; oxidoreductase; respiratory !1chain; transmembrane protein FEATURE !$11-339 #domain cytochrome b homology #label CBH\ !$11-209 #domain cytochrome b6 homology #label CB6\ !$36-52 #domain transmembrane #status predicted #label TM1\ !$81-99 #domain transmembrane #status predicted #label TM2\ !$117-133 #domain transmembrane #status predicted #label TM3\ !$178-200 #domain transmembrane #status predicted #label TM4\ !$221-339 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$229-245 #domain transmembrane #status predicted #label TM5\ !$288-304 #domain transmembrane #status predicted #label TM6\ !$323-343 #domain transmembrane #status predicted #label TM7\ !$353-369 #domain transmembrane #status predicted #label TM8\ !$83,182 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$97,196 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 379 #molecular-weight 42942 #checksum 5233 SEQUENCE /// ENTRY S17413 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - sheep mitochondrion ORGANISM #formal_name mitochondrion Ovis orientalis aries, Ovis ammon aries #common_name domestic sheep DATE 29-Jan-1993 #sequence_revision 20-Aug-1994 #text_change 03-Jun-2002 ACCESSIONS S17413; S55933; T11062 REFERENCE S17405 !$#authors Irwin, D.M.; Kocher, T.D.; Wilson, A.C. !$#journal J. Mol. Evol. (1991) 32:128-144 !$#title Evolution of the cytochrome b gene of mammals. !$#cross-references MUID:91178817; PMID:1901092 !$#accession S17413 !'##status translation not shown !'##molecule_type DNA !'##residues 1-379 ##label IRW !'##cross-references EMBL:X56284; NID:g13156; PIDN:CAA39731.1; !1PID:g578735 REFERENCE S55933 !$#authors Zardoya, R.; Villalta, M.; Lopez-Perez, M.J.; !1Garrido-Pertierra, A.; Montoya, J.; Bautista, J.M. !$#journal Curr. Genet. (1995) 28:94-96 !$#title Nucleotide sequence of the sheep mitochondrial DNA D-loop !1and its flanking tRNA genes. !$#cross-references MUID:96022431; PMID:8536319 !$#accession S55933 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 204-237,'T',239-294,'I',296-303,'I',305-379 ##label ZAR !'##cross-references EMBL:L29055; NID:g456705 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1March 1994 !'##note this ORF is not annotated in GenBank entry SHPMTDLOOP, release !1111.0 REFERENCE Z17245 !$#authors Hiendleder, S.; Lewalski, H.; Wassmuth, R.; Janke, A. !$#journal J. Mol. Evol. (1998) 47:441-448 !$#title The complete mitochondrial DNA sequence of the domestic !1sheep (Ovis aries) and comparison with the other major ovine !1haplotype. !$#cross-references MUID:98440761; PMID:9767689 !$#accession T11062 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-294,'I',296-379 ##label HIE !'##cross-references EMBL:AF010406; NID:g3445513; PID:g3445516; !1PIDN:AAD10107.1 !'##experimental_source strain Merinolandschaf; liver GENETICS !$#gene cytb !$#genome mitochondrion !$#genetic_code SGC1 FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$11-339 #domain cytochrome b homology #label CBH\ !$11-209 #domain cytochrome b6 homology #label CB6\ !$36-52 #domain transmembrane #status predicted #label TM1\ !$81-99 #domain transmembrane #status predicted #label TM2\ !$117-133 #domain transmembrane #status predicted #label TM3\ !$178-200 #domain transmembrane #status predicted #label TM4\ !$221-339 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$229-245 #domain transmembrane #status predicted #label TM5\ !$288-304 #domain transmembrane #status predicted #label TM6\ !$323-343 #domain transmembrane #status predicted #label TM7\ !$353-369 #domain transmembrane #status predicted #label TM8\ !$83,182 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$97,196 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 379 #molecular-weight 42849 #checksum 6190 SEQUENCE /// ENTRY S17418 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - pig mitochondrion ORGANISM #formal_name mitochondrion Sus scrofa domestica #common_name domestic pig DATE 29-Jan-1993 #sequence_revision 23-Jul-1999 #text_change 03-Jun-2002 ACCESSIONS T10984; T11882; S17418; S58080; S58021; S58059; S58058; !1S58060; S58079 REFERENCE Z17237 !$#authors Lin, C.S.; Liu, C.Y.; Sun, Y.L.; Chang, L.C.; Cheng, I.C.; !1Yang, P.C.; Mao, S.J.T.; Huang, M.C. !$#submission submitted to the EMBL Data Library, November 1997 !$#description Complete nucleotide sequence of the porcine mitochondrial !1genome. !$#accession T10984 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-379 ##label LIN !'##cross-references EMBL:AF034253; NID:g4958951; PID:g4958964; !1PIDN:AAD34197.1 REFERENCE Z17370 !$#authors Ursing, B.M. !$#submission submitted to the EMBL Data Library, February 1999 !$#description The complete mitochondrial DNA sequence of the pig (Sus !1scrofa). !$#accession T11882 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-313,'G',315-379 ##label URS !'##cross-references EMBL:AJ002189; PIDN:CAA05239.1 REFERENCE S17405 !$#authors Irwin, D.M.; Kocher, T.D.; Wilson, A.C. !$#journal J. Mol. Evol. (1991) 32:128-144 !$#title Evolution of the cytochrome b gene of mammals. !$#cross-references MUID:91178817; PMID:1901092 !$#accession S17418 !'##status translation not shown !'##molecule_type DNA !'##residues 1-197,'M',199-313,'G',315-379 ##label IRW !'##cross-references EMBL:X56295; NID:g13678; PIDN:CAA39742.1; !1PID:g578827 REFERENCE S58021 !$#authors Randi, E.; Lucchini, V.; Diong, C. !$#submission submitted to the EMBL Data Library, July 1995 !$#description Evolutionary genetics of the suiformes. !$#accession S58080 !'##molecule_type DNA !'##residues 1-379 ##label RAN !'##cross-references EMBL:Z50087; NID:g902692; PIDN:CAA90418.1; !1PID:g902693 !'##experimental_source subspecies leucomystax !$#accession S58021 !'##molecule_type DNA !'##residues 1-379 ##label RAW !'##cross-references EMBL:Z50079; NID:g902354; PIDN:CAA90410.1; !1PID:g902355 !'##experimental_source Asian domestic pig !$#accession S58059 !'##molecule_type DNA !'##residues 1-313,'G',315-379 ##label RA2 !'##cross-references EMBL:Z50088; NID:g902696; PIDN:CAA90419.1; !1PID:g902697 !'##experimental_source subspecies majori !$#accession S58058 !'##molecule_type DNA !'##residues 1-313,'G',315-379 ##label RA3 !'##cross-references EMBL:Z50085; NID:g902688; PIDN:CAA90416.1; !1PID:g902689 !'##experimental_source subspecies lybicus, isolate Bulgarian (1) !$#accession S58060 !'##molecule_type DNA !'##residues 1-313,'G',315-367,'V',369-379 ##label RA4 !'##cross-references EMBL:Z50089; NID:g902694; PIDN:CAA90420.1; !1PID:g902695 !'##experimental_source subspecies meridionalis (Sardinian wild boar) !$#accession S58079 !'##molecule_type DNA !'##residues 1-294,'M',296-313,'G',315-379 ##label RA5 !'##cross-references EMBL:Z50086; NID:g902690; PIDN:CAA90417.1; !1PID:g902691 !'##experimental_source subspecies lybicus, isolate Bulgarian (2) GENETICS !$#gene cytb !$#genome mitochondrion !$#genetic_code SGC1 !$#note cytb FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$11-339 #domain cytochrome b homology #label CBH\ !$11-209 #domain cytochrome b6 homology #label CB6\ !$36-52 #domain transmembrane #status predicted #label TM1\ !$81-99 #domain transmembrane #status predicted #label TM2\ !$117-133 #domain transmembrane #status predicted #label TM3\ !$178-200 #domain transmembrane #status predicted #label TM4\ !$221-339 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$229-245 #domain transmembrane #status predicted #label TM5\ !$288-304 #domain transmembrane #status predicted #label TM6\ !$323-343 #domain transmembrane #status predicted #label TM7\ !$353-369 #domain transmembrane #status predicted #label TM8\ !$83,182 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$97,196 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 379 #molecular-weight 42811 #checksum 5304 SEQUENCE /// ENTRY S17415 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - bridled dolphin mitochondrion ORGANISM #formal_name mitochondrion Stenella attenuata #common_name bridled dolphin DATE 29-Jan-1993 #sequence_revision 20-Aug-1994 #text_change 03-Jun-2002 ACCESSIONS S17415 REFERENCE S17405 !$#authors Irwin, D.M.; Kocher, T.D.; Wilson, A.C. !$#journal J. Mol. Evol. (1991) 32:128-144 !$#title Evolution of the cytochrome b gene of mammals. !$#cross-references MUID:91178817; PMID:1901092 !$#accession S17415 !'##status translation not shown !'##molecule_type DNA !'##residues 1-379 ##label IRW !'##cross-references EMBL:X56294; NID:g13495; PIDN:CAA39741.1; !1PID:g578785 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$11-339 #domain cytochrome b homology #label CBH\ !$11-209 #domain cytochrome b6 homology #label CB6\ !$36-52 #domain transmembrane #status predicted #label TM1\ !$81-99 #domain transmembrane #status predicted #label TM2\ !$117-133 #domain transmembrane #status predicted #label TM3\ !$178-200 #domain transmembrane #status predicted #label TM4\ !$221-339 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$229-245 #domain transmembrane #status predicted #label TM5\ !$288-304 #domain transmembrane #status predicted #label TM6\ !$323-343 #domain transmembrane #status predicted #label TM7\ !$353-369 #domain transmembrane #status predicted #label TM8\ !$83,182 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$97,196 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 379 #molecular-weight 42697 #checksum 6002 SEQUENCE /// ENTRY S43263 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - sei whale mitochondrion ORGANISM #formal_name mitochondrion Balaenoptera borealis #common_name sei whale DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S43263 REFERENCE S43261 !$#authors Arnason, U.; Gullberg, A. !$#journal Nature (1994) 367:726-728 !$#title Relationship of baleen whales established by cytochrome b !1gene sequence comparison. !$#cross-references MUID:94150700; PMID:8107866 !$#accession S43263 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-379 ##label ARN !'##cross-references EMBL:X75582; NID:g457763; PIDN:CAA53258.1; !1PID:g578574 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1993 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1membrane-associated complex; metalloprotein; mitochondrion; !1oxidative phosphorylation; oxidoreductase; respiratory !1chain; transmembrane protein FEATURE !$11-339 #domain cytochrome b homology #label CBH\ !$11-209 #domain cytochrome b6 homology #label CB6\ !$36-52 #domain transmembrane #status predicted #label TM1\ !$81-99 #domain transmembrane #status predicted #label TM2\ !$117-133 #domain transmembrane #status predicted #label TM3\ !$178-200 #domain transmembrane #status predicted #label TM4\ !$221-339 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$229-245 #domain transmembrane #status predicted #label TM5\ !$288-304 #domain transmembrane #status predicted #label TM6\ !$323-343 #domain transmembrane #status predicted #label TM7\ !$353-369 #domain transmembrane #status predicted #label TM8\ !$83,182 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$97,196 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 379 #molecular-weight 42818 #checksum 7270 SEQUENCE /// ENTRY S43262 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - Balaenoptera bonaerensis mitochondrion ORGANISM #formal_name mitochondrion Balaenoptera bonaerensis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S43262 REFERENCE S43261 !$#authors Arnason, U.; Gullberg, A. !$#journal Nature (1994) 367:726-728 !$#title Relationship of baleen whales established by cytochrome b !1gene sequence comparison. !$#cross-references MUID:94150700; PMID:8107866 !$#accession S43262 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-379 ##label ARN !'##cross-references EMBL:X75581; NID:g457762; PIDN:CAA53257.1; !1PID:g578573 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1993 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1membrane-associated complex; metalloprotein; mitochondrion; !1oxidative phosphorylation; oxidoreductase; respiratory !1chain; transmembrane protein FEATURE !$11-339 #domain cytochrome b homology #label CBH\ !$11-209 #domain cytochrome b6 homology #label CB6\ !$36-52 #domain transmembrane #status predicted #label TM1\ !$81-99 #domain transmembrane #status predicted #label TM2\ !$117-133 #domain transmembrane #status predicted #label TM3\ !$178-200 #domain transmembrane #status predicted #label TM4\ !$221-339 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$229-245 #domain transmembrane #status predicted #label TM5\ !$288-304 #domain transmembrane #status predicted #label TM6\ !$323-343 #domain transmembrane #status predicted #label TM7\ !$353-369 #domain transmembrane #status predicted #label TM8\ !$83,182 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$97,196 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 379 #molecular-weight 42803 #checksum 5571 SEQUENCE /// ENTRY S17417 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b, isolate 1B - pantropical spinner dolphin mitochondrion ORGANISM #formal_name mitochondrion Stenella longirostris #common_name pantropical spinner dolphin DATE 29-Jan-1993 #sequence_revision 20-Aug-1994 #text_change 03-Jun-2002 ACCESSIONS S17417; S17416 REFERENCE S17405 !$#authors Irwin, D.M.; Kocher, T.D.; Wilson, A.C. !$#journal J. Mol. Evol. (1991) 32:128-144 !$#title Evolution of the cytochrome b gene of mammals. !$#cross-references MUID:91178817; PMID:1901092 !$#accession S17417 !'##status translation not shown !'##molecule_type DNA !'##residues 1-379 ##label IRW !'##cross-references EMBL:X56293; NID:g13628; PIDN:CAA39740.1; !1PID:g578804 !'##experimental_source isolate 1B !$#accession S17416 !'##status translation not shown !'##molecule_type DNA !'##residues 1-59,'T',61-97,'M',99-265,'P',267-299,'I',301-326,'V', !1328-379 ##label IR2 !'##cross-references EMBL:X56292; NID:g13626; PIDN:CAA39739.1; !1PID:g578803 !'##experimental_source isolate 1A GENETICS !$#genome mitochondrion !$#genetic_code SGC1 FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$11-339 #domain cytochrome b homology #label CBH\ !$11-209 #domain cytochrome b6 homology #label CB6\ !$36-52 #domain transmembrane #status predicted #label TM1\ !$81-99 #domain transmembrane #status predicted #label TM2\ !$117-133 #domain transmembrane #status predicted #label TM3\ !$178-200 #domain transmembrane #status predicted #label TM4\ !$221-339 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$229-245 #domain transmembrane #status predicted #label TM5\ !$288-304 #domain transmembrane #status predicted #label TM6\ !$323-343 #domain transmembrane #status predicted #label TM7\ !$353-369 #domain transmembrane #status predicted #label TM8\ !$83,182 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$97,196 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 379 #molecular-weight 42683 #checksum 6026 SEQUENCE /// ENTRY S43261 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - minke whale mitochondrion ORGANISM #formal_name mitochondrion Balaenoptera acutorostrata #common_name minke whale, lesser rorqual DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S43261 REFERENCE S43261 !$#authors Arnason, U.; Gullberg, A. !$#journal Nature (1994) 367:726-728 !$#title Relationship of baleen whales established by cytochrome b !1gene sequence comparison. !$#cross-references MUID:94150700; PMID:8107866 !$#accession S43261 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-379 ##label ARN !'##cross-references EMBL:X75753; NID:g457761; PIDN:CAA53381.1; !1PID:g578572 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1993 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1membrane-associated complex; metalloprotein; mitochondrion; !1oxidative phosphorylation; oxidoreductase; respiratory !1chain; transmembrane protein FEATURE !$11-339 #domain cytochrome b homology #label CBH\ !$11-209 #domain cytochrome b6 homology #label CB6\ !$36-52 #domain transmembrane #status predicted #label TM1\ !$81-99 #domain transmembrane #status predicted #label TM2\ !$117-133 #domain transmembrane #status predicted #label TM3\ !$178-200 #domain transmembrane #status predicted #label TM4\ !$221-339 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$229-245 #domain transmembrane #status predicted #label TM5\ !$288-304 #domain transmembrane #status predicted #label TM6\ !$323-343 #domain transmembrane #status predicted #label TM7\ !$353-369 #domain transmembrane #status predicted #label TM8\ !$83,182 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$97,196 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 379 #molecular-weight 42623 #checksum 4374 SEQUENCE /// ENTRY S41832 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - blue whale mitochondrion ORGANISM #formal_name mitochondrion Balaenoptera musculus #common_name blue whale DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S41832 REFERENCE S41820 !$#authors Arnason, U.; Gullberg, A. !$#journal J. Mol. Evol. (1993) 37:312-322 !$#title Comparison between the complete mtDNA sequences of the blue !1and the fin whale, two species that can hybridize in nature. !$#cross-references MUID:94141932; PMID:8308901 !$#accession S41832 !'##molecule_type DNA !'##residues 1-379 ##label ARN !'##cross-references EMBL:X72204; NID:g414126; PIDN:CAA51007.1; !1PID:g575318 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1membrane-associated complex; metalloprotein; mitochondrion; !1oxidative phosphorylation; oxidoreductase; respiratory !1chain; transmembrane protein FEATURE !$11-339 #domain cytochrome b homology #label CBH\ !$11-209 #domain cytochrome b6 homology #label CB6\ !$36-52 #domain transmembrane #status predicted #label TM1\ !$81-99 #domain transmembrane #status predicted #label TM2\ !$117-133 #domain transmembrane #status predicted #label TM3\ !$178-200 #domain transmembrane #status predicted #label TM4\ !$221-339 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$229-245 #domain transmembrane #status predicted #label TM5\ !$288-304 #domain transmembrane #status predicted #label TM6\ !$323-343 #domain transmembrane #status predicted #label TM7\ !$353-369 #domain transmembrane #status predicted #label TM8\ !$83,182 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$97,196 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 379 #molecular-weight 42798 #checksum 6025 SEQUENCE /// ENTRY S43264 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - Bryde's whale mitochondrion ORGANISM #formal_name mitochondrion Balaenoptera edeni #common_name Bryde's whale DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S43264 REFERENCE S43261 !$#authors Arnason, U.; Gullberg, A. !$#journal Nature (1994) 367:726-728 !$#title Relationship of baleen whales established by cytochrome b !1gene sequence comparison. !$#cross-references MUID:94150700; PMID:8107866 !$#accession S43264 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-379 ##label ARN !'##cross-references EMBL:X75583; NID:g457766; PIDN:CAA53259.1; !1PID:g578575 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1993 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1membrane-associated complex; metalloprotein; mitochondrion; !1oxidative phosphorylation; oxidoreductase; respiratory !1chain; transmembrane protein FEATURE !$11-339 #domain cytochrome b homology #label CBH\ !$11-209 #domain cytochrome b6 homology #label CB6\ !$36-52 #domain transmembrane #status predicted #label TM1\ !$81-99 #domain transmembrane #status predicted #label TM2\ !$117-133 #domain transmembrane #status predicted #label TM3\ !$178-200 #domain transmembrane #status predicted #label TM4\ !$221-339 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$229-245 #domain transmembrane #status predicted #label TM5\ !$288-304 #domain transmembrane #status predicted #label TM6\ !$323-343 #domain transmembrane #status predicted #label TM7\ !$353-369 #domain transmembrane #status predicted #label TM8\ !$83,182 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$97,196 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 379 #molecular-weight 42878 #checksum 8289 SEQUENCE /// ENTRY S43270 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - Physeter macrocephalus mitochondrion ORGANISM #formal_name mitochondrion Physeter macrocephalus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S43270 REFERENCE S43261 !$#authors Arnason, U.; Gullberg, A. !$#journal Nature (1994) 367:726-728 !$#title Relationship of baleen whales established by cytochrome b !1gene sequence comparison. !$#cross-references MUID:94150700; PMID:8107866 !$#accession S43270 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-379 ##label ARN !'##cross-references EMBL:X75589; NID:g457797; PIDN:CAA53265.1; !1PID:g578930 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1993 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1membrane-associated complex; metalloprotein; mitochondrion; !1oxidative phosphorylation; oxidoreductase; respiratory !1chain; transmembrane protein FEATURE !$11-339 #domain cytochrome b homology #label CBH\ !$11-209 #domain cytochrome b6 homology #label CB6\ !$36-52 #domain transmembrane #status predicted #label TM1\ !$81-99 #domain transmembrane #status predicted #label TM2\ !$117-133 #domain transmembrane #status predicted #label TM3\ !$178-200 #domain transmembrane #status predicted #label TM4\ !$221-339 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$229-245 #domain transmembrane #status predicted #label TM5\ !$288-304 #domain transmembrane #status predicted #label TM6\ !$323-343 #domain transmembrane #status predicted #label TM7\ !$353-369 #domain transmembrane #status predicted #label TM8\ !$83,182 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$97,196 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 379 #molecular-weight 43061 #checksum 9557 SEQUENCE /// ENTRY S17420 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - collared peccary mitochondrion ORGANISM #formal_name mitochondrion Tayassu tajacu #common_name collared peccary DATE 29-Jan-1993 #sequence_revision 20-Aug-1994 #text_change 03-Jun-2002 ACCESSIONS S17420 REFERENCE S17405 !$#authors Irwin, D.M.; Kocher, T.D.; Wilson, A.C. !$#journal J. Mol. Evol. (1991) 32:128-144 !$#title Evolution of the cytochrome b gene of mammals. !$#cross-references MUID:91178817; PMID:1901092 !$#accession S17420 !'##status translation not shown !'##molecule_type DNA !'##residues 1-379 ##label IRW !'##cross-references EMBL:X56296; NID:g13874; PIDN:CAA39743.1; !1PID:g578835 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$11-339 #domain cytochrome b homology #label CBH\ !$11-209 #domain cytochrome b6 homology #label CB6\ !$36-52 #domain transmembrane #status predicted #label TM1\ !$81-99 #domain transmembrane #status predicted #label TM2\ !$117-133 #domain transmembrane #status predicted #label TM3\ !$178-200 #domain transmembrane #status predicted #label TM4\ !$221-339 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$229-245 #domain transmembrane #status predicted #label TM5\ !$288-304 #domain transmembrane #status predicted #label TM6\ !$323-343 #domain transmembrane #status predicted #label TM7\ !$353-369 #domain transmembrane #status predicted #label TM8\ !$83,182 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$97,196 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 379 #molecular-weight 42813 #checksum 6910 SEQUENCE /// ENTRY S26163 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - harbor seal mitochondrion ORGANISM #formal_name mitochondrion Phoca vitulina #common_name harbor seal DATE 03-Feb-1994 #sequence_revision 20-Aug-1994 #text_change 03-Jun-2002 ACCESSIONS S26163; S58453 REFERENCE S26151 !$#authors Arnason, U.; Johnsson, E. !$#journal J. Mol. Evol. (1992) 34:493-505 !$#title The complete mitochondrial DNA sequence of the harbor seal, !1Phoca vitulina. !$#cross-references MUID:92277666; PMID:1593642 !$#accession S26163 !'##molecule_type DNA !'##residues 1-379 ##label ARN !'##cross-references EMBL:X63726; NID:g13431; PIDN:CAA45269.1; !1PID:g578776 REFERENCE S58447 !$#authors Arnason, U.; Bodin, K.; Gullberg, A.; Ledje, C.; Mouchaty, !1S. !$#journal J. Mol. Evol. (1995) 40:78-85 !$#title A molecular view of pinniped relationships with particular !1emphasis on the true seals. !$#cross-references MUID:95230701; PMID:7714914 !$#accession S58453 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-14,'D',16-189,'S',191-192,'A',194-213,'N',215-258,'A', !1260-299,'I',301-303,'V',305-349,'I',351-359,'M',361-379 !1##label AR2 !'##cross-references EMBL:X82306; NID:g693981; PIDN:CAA57749.1; !1PID:g693982 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1994 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$11-339 #domain cytochrome b homology #label CBH\ !$11-209 #domain cytochrome b6 homology #label CB6\ !$36-52 #domain transmembrane #status predicted #label TM1\ !$81-99 #domain transmembrane #status predicted #label TM2\ !$117-133 #domain transmembrane #status predicted #label TM3\ !$178-200 #domain transmembrane #status predicted #label TM4\ !$221-339 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$229-245 #domain transmembrane #status predicted #label TM5\ !$288-304 #domain transmembrane #status predicted #label TM6\ !$323-343 #domain transmembrane #status predicted #label TM7\ !$353-369 #domain transmembrane #status predicted #label TM8\ !$83,182 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$97,196 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 379 #molecular-weight 42705 #checksum 8248 SEQUENCE /// ENTRY S41847 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - gray seal mitochondrion ORGANISM #formal_name mitochondrion Halichoerus grypus #common_name gray seal DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S41847 REFERENCE S41833 !$#authors Arnason, U.; Gullberg, A.; Johnsson, E.; Ledje, C. !$#journal J. Mol. Evol. (1993) 37:323-330 !$#title The nucleotide sequence of the mitochondrial DNA molecule of !1the grey seal, Halichoerus grypus, and a comparison with !1mitochondrial sequences of other true seals. !$#cross-references MUID:94141933; PMID:8308902 !$#accession S41847 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-379 ##label ARN !'##cross-references EMBL:X72004; NID:g414757; PIDN:CAA50889.1; !1PID:g578709 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1May 1993 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1membrane-associated complex; metalloprotein; mitochondrion; !1oxidative phosphorylation; oxidoreductase; respiratory !1chain; transmembrane protein FEATURE !$11-339 #domain cytochrome b homology #label CBH\ !$11-209 #domain cytochrome b6 homology #label CB6\ !$36-52 #domain transmembrane #status predicted #label TM1\ !$81-99 #domain transmembrane #status predicted #label TM2\ !$117-133 #domain transmembrane #status predicted #label TM3\ !$178-200 #domain transmembrane #status predicted #label TM4\ !$221-339 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$229-245 #domain transmembrane #status predicted #label TM5\ !$288-304 #domain transmembrane #status predicted #label TM6\ !$323-343 #domain transmembrane #status predicted #label TM7\ !$353-369 #domain transmembrane #status predicted #label TM8\ !$83,182 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$97,196 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 379 #molecular-weight 42566 #checksum 6860 SEQUENCE /// ENTRY S41833 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - Weddell seal mitochondrion ORGANISM #formal_name mitochondrion Leptonychotes weddelli #common_name Weddell seal DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S41833 REFERENCE S41833 !$#authors Arnason, U.; Gullberg, A.; Johnsson, E.; Ledje, C. !$#journal J. Mol. Evol. (1993) 37:323-330 !$#title The nucleotide sequence of the mitochondrial DNA molecule of !1the grey seal, Halichoerus grypus, and a comparison with !1mitochondrial sequences of other true seals. !$#cross-references MUID:94141933; PMID:8308902 !$#accession S41833 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-379 ##label ARN !'##cross-references EMBL:X72005; NID:g414771; PIDN:CAA50890.1; !1PID:g578717 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1May 1993 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1membrane-associated complex; metalloprotein; mitochondrion; !1oxidative phosphorylation; oxidoreductase; respiratory !1chain; transmembrane protein FEATURE !$11-339 #domain cytochrome b homology #label CBH\ !$11-209 #domain cytochrome b6 homology #label CB6\ !$36-52 #domain transmembrane #status predicted #label TM1\ !$81-99 #domain transmembrane #status predicted #label TM2\ !$117-133 #domain transmembrane #status predicted #label TM3\ !$178-200 #domain transmembrane #status predicted #label TM4\ !$221-339 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$229-245 #domain transmembrane #status predicted #label TM5\ !$288-304 #domain transmembrane #status predicted #label TM6\ !$323-343 #domain transmembrane #status predicted #label TM7\ !$353-369 #domain transmembrane #status predicted #label TM8\ !$83,182 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$97,196 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 379 #molecular-weight 42545 #checksum 7715 SEQUENCE /// ENTRY S41834 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - Monachus schauinslandi mitochondrion ORGANISM #formal_name mitochondrion Monachus schauinslandi DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S41834 REFERENCE S41833 !$#authors Arnason, U.; Gullberg, A.; Johnsson, E.; Ledje, C. !$#journal J. Mol. Evol. (1993) 37:323-330 !$#title The nucleotide sequence of the mitochondrial DNA molecule of !1the grey seal, Halichoerus grypus, and a comparison with !1mitochondrial sequences of other true seals. !$#cross-references MUID:94141933; PMID:8308902 !$#accession S41834 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-379 ##label ARN !'##cross-references EMBL:X72209; NID:g414773; PIDN:CAA51008.1; !1PID:g578719 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1May 1993 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1membrane-associated complex; metalloprotein; mitochondrion; !1oxidative phosphorylation; oxidoreductase; respiratory !1chain; transmembrane protein FEATURE !$11-339 #domain cytochrome b homology #label CBH\ !$11-209 #domain cytochrome b6 homology #label CB6\ !$36-52 #domain transmembrane #status predicted #label TM1\ !$81-99 #domain transmembrane #status predicted #label TM2\ !$117-133 #domain transmembrane #status predicted #label TM3\ !$178-200 #domain transmembrane #status predicted #label TM4\ !$221-339 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$229-245 #domain transmembrane #status predicted #label TM5\ !$288-304 #domain transmembrane #status predicted #label TM6\ !$323-343 #domain transmembrane #status predicted #label TM7\ !$353-369 #domain transmembrane #status predicted #label TM8\ !$83,182 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$97,196 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 379 #molecular-weight 42633 #checksum 6909 SEQUENCE /// ENTRY S22931 #type fragment TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - gray-crowned babbler mitochondrion (fragment) ORGANISM #formal_name mitochondrion Pomatostomus temporalis #common_name gray-crowned babbler DATE 29-Jan-1993 #sequence_revision 26-Jul-1996 #text_change 03-Jun-2002 ACCESSIONS S22931; H33285; S21611; S70405; S70404; S21612; S21613; !1S21614; S21615; S21616; S21617; S21618; S21619; S21620; !1S21621; S21622; S21623; S21624; S21625 REFERENCE S22919 !$#authors Edwards, S.V.; Arctander, P.; Wilson, A.C. !$#journal Proc. R. Soc. Lond. B Biol. Sci. (1991) 243:99-107 !$#title Mitochondrial resolution of a deep branch in the !1genealogical tree for perching birds. !$#cross-references MUID:91288587; PMID:1676522 !$#accession S22931 !'##status translation not shown !'##molecule_type DNA !'##residues 1-308 ##label EDW !'##cross-references EMBL:X60936; NID:g13395; PIDN:CAA43271.1; !1PID:g13396 REFERENCE A33285 !$#authors Kocher, T.D.; Thomas, W.K.; Meyer, A.; Edwards, S.V.; !1Paeaebo, S.; Villablanca, F.X.; Wilson, A.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:6196-6200 !$#title Dynamics of mitochondrial DNA evolution in animals: !1amplification and sequencing with conserved primers. !$#cross-references MUID:89345630; PMID:2762322 !$#accession H33285 !'##status translation not shown !'##molecule_type DNA !'##residues 15,'A',17-94 ##label KOC !'##cross-references GB:M25688; NID:g343668; PIDN:AAA32139.1; !1PID:g343669 REFERENCE S21611 !$#authors Edwards, S.V.; Wilson, A.C. !$#submission submitted to the EMBL Data Library, October 1990 !$#description Phylogenetically informative length polymorphism and !1sequence variability in mitochondrial DNA of Australian !1songbirds (Pomatostomus). !$#accession S21611 !'##molecule_type DNA !'##residues 5-98 ##label ED2 !'##cross-references EMBL:X54900; EMBL:X54901; EMBL:X54902; EMBL:X54903; !1EMBL:X54904; EMBL:X54905; EMBL:X54899; EMBL:X54898; !1EMBL:X54897; EMBL:X54896; EMBL:X54895; EMBL:X54894; !1EMBL:X54893; EMBL:X54892; EMBL:X54891 REFERENCE S70404 !$#authors Edwards, S.V.; Wilson, A.C. !$#journal Genetics (1990) 126:695-711 !$#title Phylogenetically informative length polymorphism and !1sequence variability in mitochondrial DNA of Australian !1songbirds (Pomatostomus). !$#cross-references MUID:91065505; PMID:1979038 !$#accession S70405 !'##molecule_type DNA !'##residues 5-98 ##label EDF !'##cross-references EMBL:X54891; EMBL:X54906; EMBL:X54892; EMBL:X54893; !1EMBL:X54894; EMBL:X54895; EMBL:X54896; EMBL:X54897; !1EMBL:X54898; EMBL:X54899; EMBL:X54900; EMBL:X54901; !1EMBL:X54902; EMBL:X54903; EMBL:X54904; EMBL:X54905 !$#accession S70404 !'##status translation not shown !'##molecule_type DNA !'##residues 5-13,'I',15-98 ##label ED3 !'##cross-references EMBL:X54885; NID:g13329; PIDN:CAA38658.1; !1PID:g13330; EMBL:X54914; NID:g13331; PID:g13332 !'##experimental_source individual 23C GENETICS !$#gene cyb !$#genome mitochondrion !$#genetic_code SGC1 FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$1-307 #domain cytochrome b homology (fragment) #label CBH\ !$1-98 #domain cytochrome b6 homology (fragment) #label CB6\ !$4-20 #domain transmembrane #status predicted #label TM1\ !$49-67 #domain transmembrane #status predicted #label TM2\ !$85-101 #domain transmembrane #status predicted #label TM3\ !$146-168 #domain transmembrane #status predicted #label TM4\ !$189-307 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$197-213 #domain transmembrane #status predicted #label TM5\ !$256-272 #domain transmembrane #status predicted #label TM6\ !$51,150 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$65,164 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 308 #checksum 1374 SEQUENCE /// ENTRY S17406 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - Arabian camel mitochondrion ORGANISM #formal_name mitochondrion Camelus dromedarius #common_name Arabian camel DATE 29-Jan-1993 #sequence_revision 20-Aug-1994 #text_change 03-Jun-2002 ACCESSIONS S17406 REFERENCE S17405 !$#authors Irwin, D.M.; Kocher, T.D.; Wilson, A.C. !$#journal J. Mol. Evol. (1991) 32:128-144 !$#title Evolution of the cytochrome b gene of mammals. !$#cross-references MUID:91178817; PMID:1901092 !$#accession S17406 !'##status translation not shown !'##molecule_type DNA !'##residues 1-379 ##label IRW !'##cross-references EMBL:X56281; NID:g12854; PIDN:CAA39728.1; !1PID:g578693 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$11-339 #domain cytochrome b homology #label CBH\ !$11-209 #domain cytochrome b6 homology #label CB6\ !$36-52 #domain transmembrane #status predicted #label TM1\ !$81-99 #domain transmembrane #status predicted #label TM2\ !$117-133 #domain transmembrane #status predicted #label TM3\ !$178-200 #domain transmembrane #status predicted #label TM4\ !$221-339 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$229-245 #domain transmembrane #status predicted #label TM5\ !$288-304 #domain transmembrane #status predicted #label TM6\ !$323-343 #domain transmembrane #status predicted #label TM7\ !$353-369 #domain transmembrane #status predicted #label TM8\ !$83,182 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$97,196 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 379 #molecular-weight 42512 #checksum 7604 SEQUENCE /// ENTRY S33572 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - southern African porcupine mitochondrion ORGANISM #formal_name mitochondrion Hystrix africaeaustralis #common_name southern African porcupine DATE 03-Feb-1994 #sequence_revision 20-Aug-1994 #text_change 03-Jun-2002 ACCESSIONS S33572 REFERENCE S33572 !$#authors Ma, D.P.; Zharkikh, A.; Graur, D.; VandeBerg, J.L.; Li, W.H. !$#journal J. Mol. Evol. (1993) 36:327-334 !$#title Structure and evolution of opossum, guinea pig, and !1porcupine cytochrome b genes. !$#cross-references MUID:93301932; PMID:8315653 !$#accession S33572 !'##molecule_type DNA !'##residues 1-379 ##label MAD !'##cross-references EMBL:X70674; NID:g14012; PIDN:CAA50010.1; !1PID:g602073 !'##note residue 1 and the corresponding nucleotide sequence are not !1shown GENETICS !$#gene cob !$#genome mitochondrion !$#genetic_code SGC1 FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$11-339 #domain cytochrome b homology #label CBH\ !$11-209 #domain cytochrome b6 homology #label CB6\ !$36-52 #domain transmembrane #status predicted #label TM1\ !$81-99 #domain transmembrane #status predicted #label TM2\ !$117-133 #domain transmembrane #status predicted #label TM3\ !$178-200 #domain transmembrane #status predicted #label TM4\ !$221-339 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$229-245 #domain transmembrane #status predicted #label TM5\ !$288-304 #domain transmembrane #status predicted #label TM6\ !$323-343 #domain transmembrane #status predicted #label TM7\ !$353-369 #domain transmembrane #status predicted #label TM8\ !$83,182 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$97,196 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 379 #molecular-weight 42808 #checksum 5554 SEQUENCE /// ENTRY S33573 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - short-tailed opossum (Monodelphis domestica) mitochondrion ORGANISM #formal_name mitochondrion Monodelphis domestica DATE 03-Feb-1994 #sequence_revision 20-Aug-1994 #text_change 03-Jun-2002 ACCESSIONS S33573 REFERENCE S33572 !$#authors Ma, D.P.; Zharkikh, A.; Graur, D.; VandeBerg, J.L.; Li, W.H. !$#journal J. Mol. Evol. (1993) 36:327-334 !$#title Structure and evolution of opossum, guinea pig, and !1porcupine cytochrome b genes. !$#cross-references MUID:93301932; PMID:8315653 !$#accession S33573 !'##molecule_type DNA !'##residues 1-382 ##label MAD !'##cross-references EMBL:X70673; NID:g14019; PIDN:CAA50009.1; !1PID:g14020 !'##note residue 1 and the corresponding nucleotide sequence are not !1shown GENETICS !$#gene cob !$#genome mitochondrion !$#genetic_code SGC1 FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$11-339 #domain cytochrome b homology #label CBH\ !$11-209 #domain cytochrome b6 homology #label CB6\ !$36-52 #domain transmembrane #status predicted #label TM1\ !$81-99 #domain transmembrane #status predicted #label TM2\ !$117-133 #domain transmembrane #status predicted #label TM3\ !$178-200 #domain transmembrane #status predicted #label TM4\ !$221-339 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$229-245 #domain transmembrane #status predicted #label TM5\ !$288-304 #domain transmembrane #status predicted #label TM6\ !$323-343 #domain transmembrane #status predicted #label TM7\ !$353-369 #domain transmembrane #status predicted #label TM8\ !$83,182 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$97,196 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 382 #molecular-weight 43140 #checksum 4537 SEQUENCE /// ENTRY S10198 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - chicken mitochondrion ORGANISM #formal_name mitochondrion Gallus gallus #common_name chicken DATE 31-Dec-1990 #sequence_revision 20-Aug-1994 #text_change 03-Jun-2002 ACCESSIONS S10198 REFERENCE S10187 !$#authors Desjardins, P.; Morais, R. !$#journal J. Mol. Biol. (1990) 212:599-634 !$#title Sequence and gene organization of the chicken mitochondrial !1genome. A novel gene order in higher vertebrates. !$#cross-references MUID:90230301; PMID:2329578 !$#accession S10198 !'##molecule_type DNA !'##residues 1-380 ##label DES !'##cross-references EMBL:X52392; NID:g12960; PIDN:CAA36636.1; !1PID:g12972 GENETICS !$#gene cytB !$#genome mitochondrion !$#genetic_code SGC1 FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$12-340 #domain cytochrome b homology #label CBH\ !$12-210 #domain cytochrome b6 homology #label CB6\ !$37-53 #domain transmembrane #status predicted #label TM1\ !$82-100 #domain transmembrane #status predicted #label TM2\ !$118-134 #domain transmembrane #status predicted #label TM3\ !$179-201 #domain transmembrane #status predicted #label TM4\ !$222-340 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$230-246 #domain transmembrane #status predicted #label TM5\ !$289-305 #domain transmembrane #status predicted #label TM6\ !$324-344 #domain transmembrane #status predicted #label TM7\ !$354-370 #domain transmembrane #status predicted #label TM8\ !$84,183 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$98,197 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 380 #molecular-weight 42592 #checksum 9761 SEQUENCE /// ENTRY S17412 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b [similarity] - African elephant mitochondrion ORGANISM #formal_name mitochondrion Loxodonta africana #common_name African elephant DATE 29-Jan-1993 #sequence_revision 03-Mar-2000 #text_change 03-Jun-2002 ACCESSIONS T45562; S17412 REFERENCE Z23005 !$#authors Hauf, J.; Waddell, P.J.; Chalwatzis, N.; Joger, U.; !1Zimmermann, F.K. !$#submission submitted to the EMBL Data Library, February 1998 !$#description The complete mitochondrial genome sequence of the African !1elephant (Loxodonta africana), phylogenetic relationships of !1Proboscidea to other mammals and D-loop heteroplasmy. !$#accession T45562 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-378 ##label HAU !'##cross-references EMBL:AJ224821; PIDN:CAA12150.1 !'##experimental_source cell type: whole blood cells REFERENCE S17405 !$#authors Irwin, D.M.; Kocher, T.D.; Wilson, A.C. !$#journal J. Mol. Evol. (1991) 32:128-144 !$#title Evolution of the cytochrome b gene of mammals. !$#cross-references MUID:91178817; PMID:1901092 !$#accession S17412 !'##status translation not shown !'##molecule_type DNA !'##residues 1-2,'D',4-26,'M',28-149,'L',151-248,'H',250-256,'TL',259, !1'N',261-263,'N',265,'P',267-321,'LCAYC',326-378 ##label IRW !'##cross-references EMBL:X56285; NID:g13070; PIDN:CAA39732.1; !1PID:g13071 GENETICS !$#gene cytb !$#genome mitochondrion !$#genetic_code SGC1 FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$11-339 #domain cytochrome b homology #label CBH\ !$11-209 #domain cytochrome b6 homology #label CB6\ !$36-52 #domain transmembrane #status predicted #label TM1\ !$81-99 #domain transmembrane #status predicted #label TM2\ !$117-133 #domain transmembrane #status predicted #label TM3\ !$178-200 #domain transmembrane #status predicted #label TM4\ !$221-339 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$229-245 #domain transmembrane #status predicted #label TM5\ !$288-304 #domain transmembrane #status predicted #label TM6\ !$323-343 #domain transmembrane #status predicted #label TM7\ !$353-369 #domain transmembrane #status predicted #label TM8\ !$83,182 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$97,196 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 378 #molecular-weight 42739 #checksum 6869 SEQUENCE /// ENTRY CBXL #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - African clawed frog mitochondrion ORGANISM #formal_name mitochondrion Xenopus laevis #common_name African clawed frog DATE 28-Feb-1986 #sequence_revision 09-Sep-1994 #text_change 03-Jun-2002 ACCESSIONS A23955; A00155 REFERENCE A23955 !$#authors Dunon-Bluteau, D.; Volovitch, M.; Brun, G. !$#journal Gene (1985) 36:65-78 !$#title Nucleotide sequence of a Xenopus laevis mitochondrial DNA !1fragment containing the D-loop, flanking tRNA genes and the !1apocytochrome b gene. !$#cross-references MUID:86056961; PMID:2415430 !$#accession A23955 !'##molecule_type DNA !'##residues 1-380 ##label DUN !'##cross-references GB:M10188 !'##note the authors state that this sequence corrects that which was !1reported in reference A00155 REFERENCE A00155 !$#authors Roe, B.A.; Ma, D.P.; Wilson, R.K.; Wong, J.F.H. !$#journal J. Biol. Chem. (1985) 260:9759-9774 !$#title The complete nucleotide sequence of the Xenopus laevis !1mitochondrial genome. !$#cross-references MUID:85261388; PMID:4019494 !$#accession A00155 !'##molecule_type DNA !'##residues 1-71,'F',73-77,'L',79-87,'L',89-153,'K',155-164,'SL', !1167-284,'M',287-333,'L',335-380 ##label ROE !'##cross-references GB:M10217; GB:X02890; NID:g343717; PIDN:AAA66470.1; !1PID:g807694 GENETICS !$#gene cob !$#genome mitochondrion !$#genetic_code SGC1 FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$12-340 #domain cytochrome b homology #label CBH\ !$12-210 #domain cytochrome b6 homology #label CB6\ !$37-53 #domain transmembrane #status predicted #label TM1\ !$82-100 #domain transmembrane #status predicted #label TM2\ !$118-134 #domain transmembrane #status predicted #label TM3\ !$179-201 #domain transmembrane #status predicted #label TM4\ !$222-340 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$230-246 #domain transmembrane #status predicted #label TM5\ !$289-305 #domain transmembrane #status predicted #label TM6\ !$324-344 #domain transmembrane #status predicted #label TM7\ !$354-370 #domain transmembrane #status predicted #label TM8\ !$84,183 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$98,197 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 380 #molecular-weight 42700 #checksum 9078 SEQUENCE /// ENTRY S36011 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - common carp mitochondrion ORGANISM #formal_name mitochondrion Cyprinus carpio #common_name common carp DATE 31-Dec-1993 #sequence_revision 24-Jul-1998 #text_change 03-Jun-2002 ACCESSIONS S36011; E44651 REFERENCE S21910 !$#authors Chang, Y.S.; Huang, F.L. !$#submission submitted to the EMBL Data Library, July 1991 !$#description The cDNA and primary structure of pregrowth hormones of !1three species of Cyprinadae: silver carp, bighead carp and !1grass carp. !$#accession S36011 !'##molecule_type DNA !'##residues 1-380,'C' ##label CHA1 !'##cross-references EMBL:X61010; NID:g436882 !'##note GenBank entry MICCCG PID:g436884 terminates with a UGC Cys !1codon REFERENCE A44650 !$#authors Chang, Y.S.; Huang, F.L.; Lo, T.B. !$#journal J. Mol. Evol. (1994) 38:138-155 !$#title The complete nucleotide sequence and gene organization of !1carp (Cyprinus carpio) mitochondrial genome. !$#cross-references MUID:94223691; PMID:8169959 !$#accession E44651 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type DNA !'##residues 1-301,'I',303-380 ##label CHA2 !'##cross-references EMBL:X61010; NID:g436882 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$11-339 #domain cytochrome b homology #label CBH\ !$11-209 #domain cytochrome b6 homology #label CB6\ !$36-52 #domain transmembrane #status predicted #label TM1\ !$81-99 #domain transmembrane #status predicted #label TM2\ !$117-133 #domain transmembrane #status predicted #label TM3\ !$178-200 #domain transmembrane #status predicted #label TM4\ !$221-339 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$229-245 #domain transmembrane #status predicted #label TM5\ !$288-304 #domain transmembrane #status predicted #label TM6\ !$323-343 #domain transmembrane #status predicted #label TM7\ !$353-369 #domain transmembrane #status predicted #label TM8\ !$83,182 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$97,196 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 380 #molecular-weight 42708 #checksum 7862 SEQUENCE /// ENTRY S35473 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - hillstream loach (Crossostoma lacustre) mitochondrion ORGANISM #formal_name mitochondrion Crossostoma lacustre DATE 03-Feb-1994 #sequence_revision 02-Aug-1994 #text_change 03-Jun-2002 ACCESSIONS S35473; S60283 REFERENCE S35462 !$#authors Tzeng, C.S.; Hui, C.F.; Shen, S.C.; Huang, P.C. !$#journal Nucleic Acids Res. (1992) 20:4853-4858 !$#title The complete nucleotide sequence of the Crossostoma lacustre !1mitochondrial genome: conservation and variations among !1vertebrates. !$#cross-references MUID:93027205; PMID:1408800 !$#accession S35473 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-398 ##label TZE1 !'##cross-references EMBL:M91245 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1992 REFERENCE S60271 !$#authors Tzeng, C.S.; Shen, S.C.; Huang, P.C. !$#journal Bull. Inst. Zool. Acad. Sin. (1990) 29:11-19 !$#title Mitochondrial DNA identity of Crossostoma (Homalopteridae, !1Pisces) from two river systems of the same geographical !1origin. !$#accession S60283 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-380 ##label TZE2 !'##cross-references GB:M91245; NID:g1381122; PIDN:AAB96823.1; !1PID:g336716 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$11-339 #domain cytochrome b homology #label CBH\ !$11-209 #domain cytochrome b6 homology #label CB6\ !$36-52 #domain transmembrane #status predicted #label TM1\ !$81-99 #domain transmembrane #status predicted #label TM2\ !$117-133 #domain transmembrane #status predicted #label TM3\ !$178-200 #domain transmembrane #status predicted #label TM4\ !$221-339 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$229-245 #domain transmembrane #status predicted #label TM5\ !$288-304 #domain transmembrane #status predicted #label TM6\ !$323-343 #domain transmembrane #status predicted #label TM7\ !$353-369 #domain transmembrane #status predicted #label TM8\ !$83,182 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$97,196 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 398 #molecular-weight 44570 #checksum 3961 SEQUENCE /// ENTRY S04840 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b [similarity] - white sturgeon mitochondrion ORGANISM #formal_name mitochondrion Acipenser transmontanus #common_name white sturgeon DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 03-Jun-2002 ACCESSIONS S04840 REFERENCE S04840 !$#authors Brown, J.R.; Gilbert, T.L.; Kowbel, D.J.; O'Hara, P.J.; !1Buroker, N.E.; Beckenbach, A.T.; Smith, M.J. !$#journal Nucleic Acids Res. (1989) 17:4389 !$#title Nucleotide sequence of the apocytochrome B gene in white !1sturgeon mitochondrial DNA. !$#cross-references MUID:89296501; PMID:2740232 !$#accession S04840 !'##molecule_type DNA !'##residues 1-380 ##label BRO !'##cross-references EMBL:X14944; NID:g12749; PIDN:CAA33076.1; !1PID:g12750 !'##note the termination resulting from transcript polyadenylation is !1shown GENETICS !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$11-339 #domain cytochrome b homology #label CBH\ !$11-209 #domain cytochrome b6 homology #label CB6\ !$36-52 #domain transmembrane #status predicted #label TM1\ !$81-99 #domain transmembrane #status predicted #label TM2\ !$117-133 #domain transmembrane #status predicted #label TM3\ !$178-200 #domain transmembrane #status predicted #label TM4\ !$221-339 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$229-245 #domain transmembrane #status predicted #label TM5\ !$288-304 #domain transmembrane #status predicted #label TM6\ !$323-343 #domain transmembrane #status predicted #label TM7\ !$353-369 #domain transmembrane #status predicted #label TM8\ !$83,182 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$97,196 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 380 #molecular-weight 42490 #checksum 8577 SEQUENCE /// ENTRY S01190 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - fruit fly (Drosophila melanogaster) mitochondrion ORGANISM #formal_name mitochondrion Drosophila melanogaster DATE 28-Feb-1990 #sequence_revision 20-Aug-1994 #text_change 03-Jun-2002 ACCESSIONS S01190; S01742 REFERENCE S01185 !$#authors Garesse, R. !$#journal Genetics (1988) 118:649-663 !$#title Drosophila melanogaster mitochondrial DNA: gene organization !1and evolutionary considerations. !$#cross-references MUID:88212147; PMID:3130291 !$#accession S01190 !'##molecule_type DNA !'##residues 1-378 ##label GAR !'##cross-references GB:M37275; EMBL:Y00610; NID:g336819; !1PIDN:AAA69714.1; PID:g552530 REFERENCE S01630 !$#authors Garesse, R. !$#submission submitted to the EMBL Data Library, February 1988 !$#accession S01742 !'##molecule_type DNA !'##residues 1-257,'YSANSFSNT',267-378 ##label GAR2 !'##cross-references EMBL:Y00610 GENETICS !$#gene FlyBase:mt:Cyt-b !'##cross-references FlyBase:FBgn0013678 !$#genome mitochondrion !$#genetic_code SGC4 FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$12-340 #domain cytochrome b homology #label CBH\ !$12-210 #domain cytochrome b6 homology #label CB6\ !$37-53 #domain transmembrane #status predicted #label TM1\ !$82-100 #domain transmembrane #status predicted #label TM2\ !$118-134 #domain transmembrane #status predicted #label TM3\ !$179-201 #domain transmembrane #status predicted #label TM4\ !$222-340 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$230-246 #domain transmembrane #status predicted #label TM5\ !$289-305 #domain transmembrane #status predicted #label TM6\ !$324-344 #domain transmembrane #status predicted #label TM7\ !$354-370 #domain transmembrane #status predicted #label TM8\ !$84,183 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$98,197 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 378 #molecular-weight 43224 #checksum 5934 SEQUENCE /// ENTRY C30020 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - fruit fly (Drosophila yakuba) mitochondrion ORGANISM #formal_name mitochondrion Drosophila yakuba DATE 05-Jun-1987 #sequence_revision 20-Aug-1994 #text_change 03-Jun-2002 ACCESSIONS C30020; L25797 REFERENCE A92962 !$#authors Clary, D.O.; Wolstenholme, D.R. !$#journal J. Mol. Evol. (1985) 22:252-271 !$#title The mitochondrial DNA molecule of Drosophila yakuba: !1nucleotide sequence, gene organization, and genetic code. !$#cross-references MUID:86089137; PMID:3001325 !$#accession C30020 !'##molecule_type DNA !'##residues 1-378 ##label CLA !'##cross-references GB:X03240; NID:g12923; PIDN:CAA26996.1; PID:g12935 GENETICS !$#gene FlyBase:Dyak/mt:Cyt-b !'##cross-references FlyBase:FBgn0013182 !$#genome mitochondrion !$#genetic_code SGC4 FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$12-340 #domain cytochrome b homology #label CBH\ !$12-210 #domain cytochrome b6 homology #label CB6\ !$37-53 #domain transmembrane #status predicted #label TM1\ !$82-100 #domain transmembrane #status predicted #label TM2\ !$118-134 #domain transmembrane #status predicted #label TM3\ !$179-201 #domain transmembrane #status predicted #label TM4\ !$222-340 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$230-246 #domain transmembrane #status predicted #label TM5\ !$289-305 #domain transmembrane #status predicted #label TM6\ !$324-344 #domain transmembrane #status predicted #label TM7\ !$354-370 #domain transmembrane #status predicted #label TM8\ !$84,183 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$98,197 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 378 #molecular-weight 43137 #checksum 3734 SEQUENCE /// ENTRY D34285 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - sea urchin (Paracentrotus lividus) mitochondrion ORGANISM #formal_name mitochondrion Paracentrotus lividus #common_name common urchin DATE 06-Jul-1990 #sequence_revision 02-Aug-1994 #text_change 03-Jun-2002 ACCESSIONS D34285; H26510 REFERENCE A34284 !$#authors Cantatore, P.; Roberti, M.; Rainaldi, G.; Gadaleta, M.N.; !1Saccone, C. !$#journal J. Biol. Chem. (1989) 264:10965-10975 !$#title The complete nucleotide sequence, gene organization, and !1genetic code of the mitochondrial genome of Paracentrotus !1lividus. !$#cross-references MUID:89291831; PMID:2544576 !$#accession D34285 !'##molecule_type DNA !'##residues 1-380 ##label CAN !'##cross-references GB:J04815; NID:g342913; PIDN:AAA68145.1; !1PID:g854698 REFERENCE A26510 !$#authors Cantatore, P.; Roberti, M.; Morisco, P.; Rainaldi, G.; !1Gadaleta, M.N.; Saccone, C. !$#journal Gene (1987) 53:41-54 !$#title A novel gene order in the Paracentrotus lividus !1mitochondrial genome. !$#cross-references MUID:87248108; PMID:3596250 !$#accession H26510 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 81,'K',83-85,'K',87-98,'M',100-106;'CDEV',112-114,'K', !1116-124,'M',126-129,'M',131-137,'Q',139-147,'T',149-151,'S', !1153,'I',155,'YY',158-182;352-353,'M',355-363,'M',365-374, !1'K',376-377,'M',379-380 ##label CA2 GENETICS !$#genome mitochondrion !$#genetic_code SGC8 FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$12-340 #domain cytochrome b homology #label CBH\ !$12-210 #domain cytochrome b6 homology #label CB6\ !$37-53 #domain transmembrane #status predicted #label TM1\ !$82-100 #domain transmembrane #status predicted #label TM2\ !$118-134 #domain transmembrane #status predicted #label TM3\ !$179-201 #domain transmembrane #status predicted #label TM4\ !$222-340 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$230-246 #domain transmembrane #status predicted #label TM5\ !$289-305 #domain transmembrane #status predicted #label TM6\ !$324-344 #domain transmembrane #status predicted #label TM7\ !$354-370 #domain transmembrane #status predicted #label TM8\ !$84,183 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$98,202 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 380 #molecular-weight 42338 #checksum 8765 SEQUENCE /// ENTRY S01511 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - sea urchin (Strongylocentrotus purpuratus) mitochondrion ORGANISM #formal_name mitochondrion Strongylocentrotus purpuratus #common_name purple urchin DATE 01-Dec-1989 #sequence_revision 20-Aug-1994 #text_change 03-Jun-2002 ACCESSIONS S01511 REFERENCE S01499 !$#authors Jacobs, H.T.; Elliott, D.J.; Math, V.B.; Farquharson, A. !$#journal J. Mol. Biol. (1988) 202:185-217 !$#title Nucleotide sequence and gene organization of sea urchin !1mitochondrial DNA. !$#cross-references MUID:89011951; PMID:3172215 !$#accession S01511 !'##molecule_type DNA !'##residues 1-385 ##label JAC !'##cross-references EMBL:X12631 GENETICS !$#gene cytb !$#genome mitochondrion !$#genetic_code SGC8 !$#start_codon ATA FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$17-345 #domain cytochrome b homology #label CBH\ !$17-215 #domain cytochrome b6 homology #label CB6\ !$42-58 #domain transmembrane #status predicted #label TM1\ !$87-105 #domain transmembrane #status predicted #label TM2\ !$123-139 #domain transmembrane #status predicted #label TM3\ !$184-206 #domain transmembrane #status predicted #label TM4\ !$227-345 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$235-251 #domain transmembrane #status predicted #label TM5\ !$294-310 #domain transmembrane #status predicted #label TM6\ !$329-349 #domain transmembrane #status predicted #label TM7\ !$359-375 #domain transmembrane #status predicted #label TM8\ !$89,188 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$103,202 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 385 #molecular-weight 43292 #checksum 2339 SEQUENCE /// ENTRY S26031 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - Caenorhabditis elegans mitochondrion ORGANISM #formal_name mitochondrion Caenorhabditis elegans DATE 12-Feb-1993 #sequence_revision 02-Aug-1994 #text_change 03-Jun-2002 ACCESSIONS S26031; S25804 REFERENCE S26014 !$#authors Okimoto, R.; Macfarlane, J.L.; Clary, D.O.; Wolstenholme, !1D.R. !$#journal Genetics (1992) 130:471-498 !$#title The mitochondrial genomes of two nematodes, Caenorhabditis !1elegans and Ascaris suum. !$#cross-references MUID:92201635; PMID:1551572 !$#accession S26031 !'##molecule_type DNA !'##residues 1-370 ##label OKI !'##cross-references EMBL:X54252; NID:g13988; PIDN:CAA38156.1; !1PID:g559501 !'##note the authors translated the initiation codon TTG for residue 1 !1as Leu REFERENCE S13139 !$#authors Okimoto, R.; Macfarlane, J.L.; Wolstenholme, D.R. !$#journal Nucleic Acids Res. (1990) 18:6113-6118 !$#title Evidence for the frequent use of TTG as the translation !1initiation codon of mitochondrial protein genes in the !1nematodes, Ascaris suum and Caenorhabditis elegans. !$#cross-references MUID:91045077; PMID:2235493 !$#accession S25804 !'##molecule_type DNA !'##residues 1-25 ##label OK2 !'##cross-references EMBL:X54252 !'##note the authors translated the initiation codon TTG for residue 1 !1as Leu GENETICS !$#gene cytB !$#genome mitochondrion !$#genetic_code SGC4 !$#start_codon TTG FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; membrane !1protein; metalloprotein; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain FEATURE !$8-332 #domain cytochrome b homology #label CBH\ !$8-206 #domain cytochrome b6 homology #label CB6\ !$218-332 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$80,179 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$94,198 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 370 #molecular-weight 42582 #checksum 4518 SEQUENCE /// ENTRY S26019 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - pig roundworm mitochondrion ORGANISM #formal_name mitochondrion Ascaris suum #common_name pig roundworm DATE 12-Feb-1993 #sequence_revision 02-Aug-1994 #text_change 03-Jun-2002 ACCESSIONS S26019; S25792 REFERENCE S26014 !$#authors Okimoto, R.; Macfarlane, J.L.; Clary, D.O.; Wolstenholme, !1D.R. !$#journal Genetics (1992) 130:471-498 !$#title The mitochondrial genomes of two nematodes, Caenorhabditis !1elegans and Ascaris suum. !$#cross-references MUID:92201635; PMID:1551572 !$#accession S26019 !'##molecule_type DNA !'##residues 1-365 ##label OKI !'##cross-references EMBL:X54253; NID:g13971; PIDN:CAA38168.1; !1PID:g559493 !'##note the authors translated the initiation codon ATT for residue 1 !1as Ile REFERENCE S13139 !$#authors Okimoto, R.; Macfarlane, J.L.; Wolstenholme, D.R. !$#journal Nucleic Acids Res. (1990) 18:6113-6118 !$#title Evidence for the frequent use of TTG as the translation !1initiation codon of mitochondrial protein genes in the !1nematodes, Ascaris suum and Caenorhabditis elegans. !$#cross-references MUID:91045077; PMID:2235493 !$#accession S25792 !'##molecule_type DNA !'##residues 1-20 ##label OK2 !'##cross-references EMBL:X54253 !'##note the authors translated the initiation codon ATT for residue 1 !1as Ile GENETICS !$#gene cytB !$#genome mitochondrion !$#genetic_code SGC4 !$#start_codon ATT FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; membrane !1protein; metalloprotein; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain FEATURE !$3-327 #domain cytochrome b homology #label CBH\ !$3-201 #domain cytochrome b6 homology #label CB6\ !$213-327 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$75,174 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$89,188 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 365 #molecular-weight 42361 #checksum 8375 SEQUENCE /// ENTRY CBZM #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - maize mitochondrion ORGANISM #formal_name mitochondrion Zea mays #common_name maize DATE 04-Dec-1986 #sequence_revision 30-Jun-1992 #text_change 03-Jun-2002 ACCESSIONS A00156 REFERENCE A00156 !$#authors Dawson, A.J.; Jones, V.P.; Leaver, C.J. !$#journal EMBO J. (1984) 3:2107-2113 !$#title The apocytochrome b gene in maize mitochondria does not !1contain introns and is preceded by a potential ribosome !1binding site. !$#accession A00156 !'##molecule_type DNA !'##residues 1-388 ##label DAW !'##cross-references EMBL:X00789; NID:g13904; PIDN:CAA25367.1; !1PID:g13905 !'##note the authors translated the codon CGG for residue 239 as Trp, !1assuming a special genetic code for plant mitochondria GENETICS !$#gene cob !$#genome mitochondrion FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$16-346 #domain cytochrome b homology #label CBH\ !$16-216 #domain cytochrome b6 homology #label CB6\ !$41-57 #domain transmembrane #status predicted #label TM1\ !$86-104 #domain transmembrane #status predicted #label TM2\ !$124-140 #domain transmembrane #status predicted #label TM3\ !$185-207 #domain transmembrane #status predicted #label TM4\ !$228-346 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$236-252 #domain transmembrane #status predicted #label TM5\ !$295-311 #domain transmembrane #status predicted #label TM6\ !$330-350 #domain transmembrane #status predicted #label TM7\ !$360-375 #domain transmembrane #status predicted #label TM8\ !$88,189 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$102,203 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 388 #molecular-weight 43567 #checksum 3256 SEQUENCE /// ENTRY CBRZ #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - rice mitochondrion ORGANISM #formal_name mitochondrion Oryza sativa #common_name rice DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 03-Jun-2002 ACCESSIONS JQ0164; S20659; S07874 REFERENCE JQ0164 !$#authors Kaleikau, E.K.; Andre, C.P.; Doshi, B.; Walbot, V. !$#journal Nucleic Acids Res. (1990) 18:372 !$#title Sequence of the rice mitochondrial gene for apocytochrome b. !$#cross-references MUID:90221830; PMID:2326174 !$#accession JQ0164 !'##molecule_type DNA !'##residues 1-397 ##label KAL !'##cross-references EMBL:X17064; NID:g13214; PIDN:CAA34910.1; !1PID:g13215 !'##experimental_source strain IR36 REFERENCE S20659 !$#authors Koh-ichi, K. !$#submission submitted to the EMBL Data Library, June 1990 !$#accession S20659 !'##molecule_type DNA !'##residues 1-27,'T',29-30,'N',32-58,'H',60-395,'V',397 ##label KOH !'##cross-references EMBL:X53710; NID:g13202; PIDN:CAA37747.1; !1PID:g13203 GENETICS !$#gene cob !$#genome mitochondrion FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$16-346 #domain cytochrome b homology #label CBH\ !$16-216 #domain cytochrome b6 homology #label CB6\ !$41-57 #domain transmembrane #status predicted #label TM1\ !$86-104 #domain transmembrane #status predicted #label TM2\ !$124-140 #domain transmembrane #status predicted #label TM3\ !$185-207 #domain transmembrane #status predicted #label TM4\ !$228-346 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$236-252 #domain transmembrane #status predicted #label TM5\ !$295-311 #domain transmembrane #status predicted #label TM6\ !$330-350 #domain transmembrane #status predicted #label TM7\ !$360-375 #domain transmembrane #status predicted #label TM8\ !$88,189 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$102,203 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 397 #molecular-weight 44540 #checksum 9544 SEQUENCE /// ENTRY A22931 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - wheat mitochondrion ORGANISM #formal_name mitochondrion Triticum aestivum #common_name common wheat DATE 20-Aug-1987 #sequence_revision 24-Feb-1995 #text_change 03-Jun-2002 ACCESSIONS A22931; S36920 REFERENCE A22931 !$#authors Boer, P.H.; McIntosh, J.E.; Gray, M.W.; Bonen, L. !$#journal Nucleic Acids Res. (1985) 13:2281-2292 !$#title The wheat mitochondrial gene for apocytochrome b: absence of !1a prokaryotic ribosome binding site. !$#cross-references MUID:85215614; PMID:2987849 !$#accession A22931 !'##molecule_type DNA !'##residues 1-59,'H',61-95,'L',97-99,'H',101-108,'H',110-119,'R', !1121-139,'P',141-189,'H',191-193,'L',195-226,'S',228-238,'R', !1240-241,'S',243-269,'P',271-284,'H',286-302,'P',304-327,'H', !1329-360,'P',362-374,'P',376-398 ##label BOE !'##cross-references EMBL:X02352; NID:g13699; PIDN:CAA26207.1; !1PID:g13700 !'##note the authors translated the codon CGG for residue 239 as Trp, !1assuming a special genetic code for plant mitochondria !'##note the differences between the sequences from reference A22931 and !1S36919 at positions 60, 96, 100, 109, 120, 140, 190, 194, !1227, 239, 242, 270, 285, 303, 328, 361, and 375 are due to !1RNA editing REFERENCE S36919 !$#authors Zanlungo, S.; Begu, D.; Quinones, V.; Araya, A.; Jordana, X. !$#journal Curr. Genet. (1993) 24:344-348 !$#title RNA editing of apocytochrome b (cob) transcripts in !1mitochondria from two genera of plants. !$#cross-references MUID:94073991; PMID:7504589 !$#accession S36920 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues !113-23;55-65;92-112;115-125;135-145;184-199;223-245;266-274; !1280-289;299-306,'C';323-333;357-366;370-380;382-398 ##label !1ZAN GENETICS !$#gene cob !$#genome mitochondrion FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; RNA editing; !1transmembrane protein FEATURE !$16-346 #domain cytochrome b homology #label CBH\ !$16-216 #domain cytochrome b6 homology #label CB6\ !$41-57 #domain transmembrane #status predicted #label TM1\ !$86-104 #domain transmembrane #status predicted #label TM2\ !$124-140 #domain transmembrane #status predicted #label TM3\ !$185-207 #domain transmembrane #status predicted #label TM4\ !$228-346 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$236-252 #domain transmembrane #status predicted #label TM5\ !$295-311 #domain transmembrane #status predicted #label TM6\ !$330-350 #domain transmembrane #status predicted #label TM7\ !$360-375 #domain transmembrane #status predicted #label TM8\ !$88,189 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$102,203 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 398 #molecular-weight 45103 #checksum 7284 SEQUENCE /// ENTRY CBOBE #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - evening primrose mitochondrion ORGANISM #formal_name mitochondrion Oenothera villaricae #common_name evening primrose DATE 30-Jun-1992 #sequence_revision 31-Dec-1992 #text_change 03-Jun-2002 ACCESSIONS S20141; S20142; S03156 REFERENCE S17916 !$#authors Schuster, W.; Ternes, R.; Knoop, V.; Hiesel, R.; Wissinger, !1B.; Brennicke, A. !$#journal Curr. Genet. (1991) 20:397-404 !$#title Distribution of RNA editing sites in Oenothera mitochondrial !1mRNAs and rRNAs. !$#cross-references MUID:92224283; PMID:1725505 !$#accession S20141 !'##molecule_type mRNA !'##residues 1-394 ##label SCH1 !'##note the authors translated the codon TTC for residue 97 as Tyr !$#accession S20142 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-18,'T',20-96,'L',98-100,'H',102-103,'I',105-107,'H', !1109-120,'R',122-136,'T',138-189,'H',191-285,'H',287-303,'P', !1305-328,'H',330-361,'P',363-394 ##label SCH2 REFERENCE S03156 !$#authors Schuster, W.; Brennicke, A. !$#journal Curr. Genet. (1985) 9:157-163 !$#title TGA-Termination codon in the apocytochrome b gene from !1Oenothera mitochondria. !$#accession S03156 !'##molecule_type DNA !'##residues 1-18,'T',20-96,'L',98-100,'H',102-103,'I',105-107,'H', !1109-136,'T',138-189,'H',191-285,'H',287-303,'P',305-328,'H', !1330-361,'P',363-394 ##label SCH3 !'##cross-references EMBL:X07126 !'##note the authors translated the codon ATA for residue 292 as His !'##note the authors translated the codon CGG for residue 121 as Trp, !1assuming a special genetic code for plant mitochondria GENETICS !$#gene cob; cytB !$#genome mitochondrion FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; RNA editing; !1transmembrane protein FEATURE !$17-347 #domain cytochrome b homology #label CBH\ !$17-217 #domain cytochrome b6 homology #label CB6\ !$42-58 #domain transmembrane #status predicted #label TM1\ !$87-105 #domain transmembrane #status predicted #label TM2\ !$125-141 #domain transmembrane #status predicted #label TM3\ !$186-208 #domain transmembrane #status predicted #label TM4\ !$229-347 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$237-253 #domain transmembrane #status predicted #label TM5\ !$296-312 #domain transmembrane #status predicted #label TM6\ !$331-351 #domain transmembrane #status predicted #label TM7\ !$361-376 #domain transmembrane #status predicted #label TM8\ !$89,191 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$103,204 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 394 #molecular-weight 44365 #checksum 9878 SEQUENCE /// ENTRY S38960 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - Arabidopsis thaliana mitochondrion ORGANISM #formal_name mitochondrion Arabidopsis thaliana #common_name mouse-ear cress DATE 10-Mar-1994 #sequence_revision 20-Aug-1994 #text_change 03-Jun-2002 ACCESSIONS S38960; S36912 REFERENCE S36911 !$#authors Brandt, P.; Unseld, M.; Eckert-Ossenkopp, U.; Brennicke, A. !$#journal Curr. Genet. (1993) 24:330-336 !$#title An rps14 pseudogene is transcribed and edited in Arabidopsis !1mitochondria. !$#cross-references MUID:94073989; PMID:7916674 !$#accession S38960 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-393 ##label BRA1 !$#accession S36912 !'##molecule_type DNA !'##residues 1-95,'L',97-108,'H',110-189,'H',191-284,'H',286-302,'P', !1304-327,'H',329-361,'P',363-393 ##label BRA2 !'##cross-references EMBL:X67736; NID:g402960; PIDN:CAA47966.1; !1PID:g402962 !'##note differences from the sequence translated from mRNA are due to !1RNA editing GENETICS !$#gene cob !$#genome mitochondrion FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; RNA editing; !1transmembrane protein FEATURE !$16-346 #domain cytochrome b homology #label CBH\ !$16-216 #domain cytochrome b6 homology #label CB6\ !$41-57 #domain transmembrane #status predicted #label TM1\ !$86-104 #domain transmembrane #status predicted #label TM2\ !$124-140 #domain transmembrane #status predicted #label TM3\ !$185-207 #domain transmembrane #status predicted #label TM4\ !$228-346 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$236-252 #domain transmembrane #status predicted #label TM5\ !$295-311 #domain transmembrane #status predicted #label TM6\ !$330-350 #domain transmembrane #status predicted #label TM7\ !$360-375 #domain transmembrane #status predicted #label TM8\ !$88,189 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$102,203 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 393 #molecular-weight 44281 #checksum 6400 SEQUENCE /// ENTRY CBPOM #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - potato mitochondrion ORGANISM #formal_name mitochondrion Solanum tuberosum #common_name potato DATE 31-Dec-1992 #sequence_revision 24-Feb-1995 #text_change 03-Jun-2002 ACCESSIONS S17427; S36919; S28874 REFERENCE S17427 !$#authors Zanlungo, S.; Litvak, S.; Jordana, X. !$#journal Plant Mol. Biol. (1991) 17:527-530 !$#title Isolation and nucleotide sequence of the potato !1mitochondrial gene for apocytochrome b. !$#cross-references MUID:91355947; PMID:1840690 !$#accession S17427 !'##molecule_type DNA !'##residues 1-17,'T',19-99,'H',101-108,'H',110-119,'R',121-189,'H', !1191-226,'S',228-284,'H',286-302,'P',304-327,'H',329-361,'P', !1363-393 ##label ZAN !'##cross-references EMBL:X58437; NID:g12877; PIDN:CAA41343.1; !1PID:g12878 !'##experimental_source cv. Bintje !'##note differences between the sequences from references S17427 and !1S36919 are due to RNA editing REFERENCE S36919 !$#authors Zanlungo, S.; Begu, D.; Quinones, V.; Araya, A.; Jordana, X. !$#journal Curr. Genet. (1993) 24:344-348 !$#title RNA editing of apocytochrome b (cob) transcripts in !1mitochondria from two genera of plants. !$#cross-references MUID:94073991; PMID:7504589 !$#accession S36919 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues !113-23;55-65;92-112;115-125;135-145;184-199;223-245;266-274; !1280-289;299-307;323-333;357-366;370-380;382-393 ##label ZA2 !'##experimental_source cv. Bintje REFERENCE S28874 !$#authors Braun, H.P.; Schmitz, U.K. !$#journal FEBS Lett. (1993) 316:128-132 !$#title Purification and sequencing of cytochrome b from potato !1reveals methionine cleavage of a mitochondrially encoded !1protein. !$#cross-references MUID:93131029; PMID:8420797 !$#accession S28874 !'##molecule_type protein !'##residues 2-16 ##label BRA GENETICS !$#gene cob !$#genome mitochondrion FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; RNA editing; !1transmembrane protein FEATURE !$2-393 #product ubiquinol-cytochrome-c reductase cytochrome !8b #status experimental #label MAT\ !$16-346 #domain cytochrome b homology #label CBH\ !$16-216 #domain cytochrome b6 homology #label CB6\ !$41-57 #domain transmembrane #status predicted #label TM1\ !$86-104 #domain transmembrane #status predicted #label TM2\ !$124-140 #domain transmembrane #status predicted #label TM3\ !$185-207 #domain transmembrane #status predicted #label TM4\ !$228-346 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$236-252 #domain transmembrane #status predicted #label TM5\ !$295-311 #domain transmembrane #status predicted #label TM6\ !$330-350 #domain transmembrane #status predicted #label TM7\ !$360-375 #domain transmembrane #status predicted #label TM8\ !$88,189 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$102,203 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 393 #molecular-weight 44283 #checksum 5964 SEQUENCE /// ENTRY CBVF #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - fava bean mitochondrion ORGANISM #formal_name mitochondrion Vicia faba #common_name fava bean DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 03-Jun-2002 ACCESSIONS S01221 REFERENCE S01221 !$#authors Wahleithner, J.A.; Wolstenholme, D.R. !$#journal Nucleic Acids Res. (1988) 16:6897-6913 !$#title Ribosomal protein S14 genes in broad bean mitochondrial DNA. !$#cross-references MUID:88303319; PMID:3405753 !$#accession S01221 !'##molecule_type DNA !'##residues 1-392 ##label WAH !'##cross-references EMBL:X07237; NID:g13880; PIDN:CAA30226.1; !1PID:g13882 !'##note the authors translated the codon GGA for residue 137 as Phe !'##note the authors translated the codon CGG for residue 120 as Trp, !1assuming a special genetic code for plant mitochondria GENETICS !$#gene cob !$#genome mitochondrion FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$16-346 #domain cytochrome b homology #label CBH\ !$16-216 #domain cytochrome b6 homology #label CB6\ !$41-57 #domain transmembrane #status predicted #label TM1\ !$86-104 #domain transmembrane #status predicted #label TM2\ !$124-140 #domain transmembrane #status predicted #label TM3\ !$185-207 #domain transmembrane #status predicted #label TM4\ !$228-346 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$236-252 #domain transmembrane #status predicted #label TM5\ !$296-311 #domain transmembrane #status predicted #label TM6\ !$330-350 #domain transmembrane #status predicted #label TM7\ !$360-375 #domain transmembrane #status predicted #label TM8\ !$88,189 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$102,203 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 392 #molecular-weight 44013 #checksum 1384 SEQUENCE /// ENTRY S25953 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - liverwort (Marchantia polymorpha) mitochondrion ORGANISM #formal_name mitochondrion Marchantia polymorpha DATE 07-May-1993 #sequence_revision 02-Aug-1994 #text_change 03-Jun-2002 ACCESSIONS S25953 REFERENCE S25941 !$#authors Oda, K.; Yamato, K.; Ohta, E.; Nakamura, Y.; Takemura, M.; !1Nozato, N.; Akashi, K.; Kanegae, T.; Ogura, Y.; Kohchi, T.; !1Ohyama, K. !$#journal J. Mol. Biol. (1992) 223:1-7 !$#title Gene organization deduced from the complete sequence of !1liverwort Marchantia polymorpha mitochondrial DNA. A !1primitive form of plant mitochondrial genome. !$#cross-references MUID:92114051; PMID:1731062 !$#accession S25953 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-404 ##label ODA !'##cross-references EMBL:M68929; NID:g786182; PIDN:AAC09441.1; !1PID:g786227 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1February 1992 GENETICS !$#gene cob !$#genome mitochondrion !$#introns 124/3; 261/3; 275/2 FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$13-343 #domain cytochrome b homology #label CBH\ !$13-213 #domain cytochrome b6 homology #label CB6\ !$38-54 #domain transmembrane #status predicted #label TM1\ !$83-101 #domain transmembrane #status predicted #label TM2\ !$121-137 #domain transmembrane #status predicted #label TM3\ !$182-204 #domain transmembrane #status predicted #label TM4\ !$225-343 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$233-249 #domain transmembrane #status predicted #label TM5\ !$292-308 #domain transmembrane #status predicted #label TM6\ !$327-347 #domain transmembrane #status predicted #label TM7\ !$357-372 #domain transmembrane #status predicted #label TM8\ !$85,186 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$99,200 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 404 #molecular-weight 45188 #checksum 9703 SEQUENCE /// ENTRY A53224 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - Chlamydomonas reinhardtii mitochondrion ORGANISM #formal_name mitochondrion Chlamydomonas reinhardtii DATE 12-May-1994 #sequence_revision 20-Aug-1994 #text_change 03-Jun-2002 ACCESSIONS A53224; S11966; S12016; PQ0039; S33471 REFERENCE A53224 !$#authors Bennoun, P.; Delosme, M.; Kueck, U. !$#journal Genetics (1991) 127:335-343 !$#title Mitochondrial genetics of Chlamydomonas reinhardtii: !1resistance mutations marking the cytochrome b gene. !$#cross-references MUID:91169284; PMID:2004707 !$#accession A53224 !'##molecule_type DNA !'##residues 1-381 ##label BEN !'##cross-references GB:X59471; NID:g13747; PIDN:CAA42076.1; PID:g13748 REFERENCE S11966 !$#authors Ma, D.P.; Yang, Y.W.; King, T.Y.; Hasnain, S.E. !$#journal Plant Mol. Biol. (1990) 15:357-359 !$#title The mitochondrial apocytochrome b gene from Chlamydomonas !1reinhardtii. !$#cross-references MUID:91355882; PMID:2103454 !$#accession S11966 !'##molecule_type DNA !'##residues 1-187,'F',189-231,'VLCSWL',238,'CSAF',243-381 ##label MAD !'##cross-references EMBL:X52168; NID:g311947; PIDN:CAA36421.1; !1PID:g311948 REFERENCE S12016 !$#authors Michaelis, G.; Vahrenholz, C.; Pratje, E. !$#journal Mol. Gen. Genet. (1990) 223:211-216 !$#title Mitochondrial DNA of Chlamydomonas reinhardtii: the gene for !1apocytochrome b and the complete functional map of the 15.8 !1kb DNA. !$#cross-references MUID:91066832; PMID:2250648 !$#accession S12016 !'##molecule_type DNA !'##residues 1-187,'F',189-381 ##label MIC !'##cross-references GB:X66484; GB:M37212; GB:X01442; GB:X16537; !1GB:X62284; NID:g12510; PIDN:CAA47111.1; PID:g12511 REFERENCE JQ0385 !$#authors Ma, D.P.; Yang, Y.W.; King, Y.T.; Hasnain, S.E. !$#journal Gene (1989) 85:363-370 !$#title Nucleotide sequence of cloned nad4 (urf4) gene from !1Chlamydomonas reinhardtii mitochondrial DNA. !$#cross-references MUID:90185210; PMID:2628173 !$#accession PQ0039 !'##molecule_type DNA !'##residues 1-65 ##label MA2 !'##note the gene encoding this protein is located downstream from gene !1nad4 GENETICS !$#gene cob !$#genome mitochondrion FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$10-337 #domain cytochrome b homology #label CBH\ !$10-210 #domain cytochrome b6 homology #label CB6\ !$36-52 #domain transmembrane #status predicted #label TM1\ !$81-99 #domain transmembrane #status predicted #label TM2\ !$119-135 #domain transmembrane #status predicted #label TM3\ !$180-202 #domain transmembrane #status predicted #label TM4\ !$222-337 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$231-247 #domain transmembrane #status predicted #label TM5\ !$290-306 #domain transmembrane #status predicted #label TM6\ !$325-345 #domain transmembrane #status predicted #label TM7\ !$355-370 #domain transmembrane #status predicted #label TM8\ !$82,183 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$96,197 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 381 #molecular-weight 42296 #checksum 6242 SEQUENCE /// ENTRY CBASN #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - Emericella nidulans mitochondrion ORGANISM #formal_name mitochondrion Emericella nidulans, Aspergillus nidulans DATE 02-Apr-1982 #sequence_revision 02-Apr-1982 #text_change 03-Jun-2002 ACCESSIONS A00157 REFERENCE A00157 !$#authors Waring, R.B.; Davies, R.W.; Lee, S.; Grisi, E.; Berks, M.M.; !1Scazzocchio, C. !$#journal Cell (1981) 27:4-11 !$#title The mosaic organization of the apocytochrome b gene of !1Aspergillus nidulans revealed by DNA sequencing. !$#cross-references MUID:82115341; PMID:7034966 !$#accession A00157 !'##molecule_type DNA !'##residues 1-387 ##label WAR !'##cross-references GB:J01389; GB:V00651; GB:V00652; NID:g336901; !1PIDN:AAA31737.1; PID:g336903 !'##experimental_source imperfect stage GENETICS !$#gene cobA !$#genome mitochondrion !$#genetic_code SGC3 !$#introns 169/2 FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$10-341 #domain cytochrome b homology #label CBH\ !$10-211 #domain cytochrome b6 homology #label CB6\ !$35-51 #domain transmembrane #status predicted #label TM1\ !$80-98 #domain transmembrane #status predicted #label TM2\ !$118-134 #domain transmembrane #status predicted #label TM3\ !$179-201 #domain transmembrane #status predicted #label TM4\ !$223-341 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$231-247 #domain transmembrane #status predicted #label TM5\ !$290-306 #domain transmembrane #status predicted #label TM6\ !$325-345 #domain transmembrane #status predicted #label TM7\ !$355-371 #domain transmembrane #status predicted #label TM8\ !$82,183 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$96,197 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 387 #molecular-weight 43521 #checksum 3697 SEQUENCE /// ENTRY CBNC #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - Neurospora crassa mitochondrion ORGANISM #formal_name mitochondrion Neurospora crassa DATE 15-Nov-1984 #sequence_revision 15-Nov-1984 #text_change 03-Jun-2002 ACCESSIONS A00158; S03128; B28755 REFERENCE A00158 !$#authors Citterich, M.H.; Morelli, G.; Macino, G. !$#journal EMBO J. (1983) 2:1235-1242 !$#title Nucleotide sequence and intron structure of the !1apocytochrome b gene of Neurospora crassa mitochondria. !$#accession A00158 !'##molecule_type DNA !'##residues 1-385 ##label CIT !'##cross-references GB:M37324; NID:g342695 !'##note in GenBank entry NEUMTCYTAB, release 113.0, PID:g497778, !1PIDN:AAA31961.1, although it is stated otherwise, apparently !1GenBank translation table 5 (PIR SGC4) was used rather than !1the correct translation table 4 (PIR SGC3); the translation !1with SGC3 matching the author's translation in Fig. 2 is !1shown here REFERENCE S03127 !$#authors Collins, R.A.; Reynolds, C.A.; Olive, J. !$#journal Nucleic Acids Res. (1988) 16:1125-1134 !$#title The self-splicing intron in the Neurospora apocytochrome b !1gene contains a long reading frame in frame with the !1upstream exon. !$#cross-references MUID:88143984; PMID:2963999 !$#accession S03128 !'##molecule_type DNA !'##residues 1-163 ##label COL !'##cross-references EMBL:X06884; NID:g13115; PIDN:CAA30001.1; !1PID:g13117; PID:g1334408 REFERENCE A28755 !$#authors Burke, J.M.; Breitenberger, C.; Heckman, J.E.; Dujon, B.; !1RajBhandary, U.L. !$#journal J. Biol. Chem. (1984) 259:504-511 !$#title Cytochrome b gene of Neurospora crassa mitochondria. !$#cross-references MUID:84161957; PMID:6231283 !$#accession B28755 !'##molecule_type DNA !'##residues 132-163,'FIW',167-182,'H',184-186,'P',188-190,'AA',193-196, !1'H',198-199,'A',201,'H',203,'TA',206,'S',208-212,'VS', !1215-220,'T',222-279,'Y',281-360,'F',362-385 ##label BUR !'##cross-references GB:K01181; NID:g342694 !'##note this ORF is not translated in GenBank entry NEUMTCYB, release !1106.0 COMMENT See PIR:A28755 for a hypothetical gene cob intron 2 encoded !1protein. GENETICS !$#gene cob !$#genome mitochondrion !$#genetic_code SGC3 !$#introns 131/3; 164/1 FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$10-341 #domain cytochrome b homology #label CBH\ !$10-211 #domain cytochrome b6 homology #label CB6\ !$35-51 #domain transmembrane #status predicted #label TM1\ !$80-98 #domain transmembrane #status predicted #label TM2\ !$118-134 #domain transmembrane #status predicted #label TM3\ !$179-201 #domain transmembrane #status predicted #label TM4\ !$223-341 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$231-247 #domain transmembrane #status predicted #label TM5\ !$290-306 #domain transmembrane #status predicted #label TM6\ !$325-345 #domain transmembrane #status predicted #label TM7\ !$355-371 #domain transmembrane #status predicted #label TM8\ !$82,183 #binding_site heme iron (His, Tyr) (axial ligands) !8(low potential) #status predicted\ !$96,197 #binding_site heme iron (His, Tyr) (axial ligands) !8(high potential) #status predicted SUMMARY #length 385 #molecular-weight 43613 #checksum 6688 SEQUENCE /// ENTRY A48326 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - Podospora anserina mitochondrion ORGANISM #formal_name mitochondrion Podospora anserina DATE 04-Feb-1994 #sequence_revision 20-Aug-1994 #text_change 03-Jun-2002 ACCESSIONS A48326 REFERENCE A48326 !$#authors Cummings, D.J.; Michel, F.; McNally, K.L. !$#journal Curr. Genet. (1989) 16:407-418 !$#title DNA sequence analysis of the apocytochrome b gene of !1Podospora anserina: a new family of intronic open reading !1frame. !$#cross-references MUID:90124723; PMID:2611913 !$#accession A48326 !'##molecule_type DNA !'##residues 1-387 ##label CUM !'##cross-references GB:X55026; NID:g14030; PIDN:CAA38772.1; PID:g14038 GENETICS !$#genome mitochondrion !$#genetic_code SGC3 FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$10-341 #domain cytochrome b homology #label CBH\ !$10-211 #domain cytochrome b6 homology #label CB6\ !$35-51 #domain transmembrane #status predicted #label TM1\ !$80-98 #domain transmembrane #status predicted #label TM2\ !$118-134 #domain transmembrane #status predicted #label TM3\ !$179-201 #domain transmembrane #status predicted #label TM4\ !$223-341 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$231-247 #domain transmembrane #status predicted #label TM5\ !$290-306 #domain transmembrane #status predicted #label TM6\ !$325-345 #domain transmembrane #status predicted #label TM7\ !$355-371 #domain transmembrane #status predicted #label TM8\ !$82,183 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$96,197 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 387 #molecular-weight 43531 #checksum 3660 SEQUENCE /// ENTRY CBBY #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - yeast (Saccharomyces cerevisiae) mitochondrion ORGANISM #formal_name mitochondrion Saccharomyces cerevisiae DATE 31-Dec-1980 #sequence_revision 19-Feb-1984 #text_change 03-Jun-2002 ACCESSIONS A00159; A38011; A38012; S56165; S68973 REFERENCE A00159 !$#authors Nobrega, F.G.; Tzagoloff, A. !$#journal J. Biol. Chem. (1980) 255:9828-9837 !$#title Assembly of the mitochondrial membrane system. DNA sequence !1and organization of the cytochrome b gene in Saccharomyces !1cerevisiae D273-10B. !$#cross-references MUID:81046788; PMID:6253454 !$#accession A00159 !'##molecule_type DNA !'##residues 1-385 ##label NOB !'##cross-references EMBL:V00696 !'##experimental_source strain D273-10B/A21 !'##genetics ST1 !'##note the coding region was identified by homology with mammalian !1cytochromes b; the amino acids at the intron junctions are !1uncertain; residue 253 may be Gln or His and residue 270 may !1be Asp or Val !'##note the authors translated the codon ATA for residue 69 according !1to the standard code REFERENCE A38011 !$#authors Lazowska, J.; Jacq, C.; Slonimski, P.P. !$#journal Cell (1980) 22:333-348 !$#title Sequence of introns and flanking exons in wild-type and box3 !1mutants of cytochrome b reveals an interlaced splicing !1protein coded by an intron. !$#cross-references MUID:81088336; PMID:7004642 !$#accession A38011 !'##molecule_type DNA !'##residues 20-121,'T',123-138 ##label LAZ1 !'##cross-references EMBL:V00686 !'##experimental_source strain 777-3A !'##genetics ST2 !'##note the authors translated the codon ATA for residue 69 according !1to the standard code REFERENCE A38012 !$#authors Lazowska, J.; Jacq, C.; Slonimski, P.P. !$#journal Cell (1981) 27:12-14 !$#title Splice points of the third intron in the yeast mitochondrial !1cytochrome b gene. !$#cross-references MUID:82115326; PMID:7034963 !$#accession A38012 !'##molecule_type DNA !'##residues 144-169 ##label LAZ2 !'##experimental_source strain 777-3A !'##genetics ST2 REFERENCE S56165 !$#authors Jacq, C. !$#submission submitted to the EMBL Data Library, January 1995 !$#accession S56165 !'##molecule_type DNA !'##residues 1-121,'T',123-252,'H',254-269,'V',271-385 ##label JAC !'##cross-references EMBL:X84042; NID:g643020; PIDN:CAA58861.1; !1PID:g643021 !'##experimental_source strain WR200 REFERENCE S68973 !$#authors Claros, M.G.; Perea, J.; Shu, Y.; Samatey, F.A.; Popot, !1J.L.; Jacq, C. !$#journal Eur. J. Biochem. (1995) 228:762-771 !$#title Limitations to in vivo import of hydrophobic proteins into !1yeast mitochondria. The case of a cytoplasmically !1synthesized apocytochrome b. !$#cross-references MUID:95255283; PMID:7737175 !$#accession S68973 !'##molecule_type DNA !'##residues 1-121,'T',123-252,'H',254-269,'V',271-385 ##label CLA !'##cross-references EMBL:X84042; NID:g643020; PIDN:CAA58861.1; !1PID:g643021 GENETICS ST1 !$#gene SGD:COB; cytb; cob !$#map_position 71.6-76.2 !$#genome mitochondrion !$#genetic_code SGC2 !$#introns 253/3; 270/3 !$#note strain D273-10B/A21 GENETICS ST2 !$#gene SGD:COB; cytb; cob !$#genome mitochondrion !$#genetic_code SGC2 !$#introns 139/1; 143/2; 169/2; 253/3; 270/3 !$#note strain 777-3A FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrial inner membrane; mitochondrion; !1oxidative phosphorylation; oxidoreductase; respiratory !1chain; transmembrane protein FEATURE !$10-340 #domain cytochrome b homology #label CBH\ !$10-210 #domain cytochrome b6 homology #label CB6\ !$35-51 #domain transmembrane #status predicted #label TM1\ !$80-98 #domain transmembrane #status predicted #label TM2\ !$118-134 #domain transmembrane #status predicted #label TM3\ !$179-201 #domain transmembrane #status predicted #label TM4\ !$222-340 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$230-246 #domain transmembrane #status predicted #label TM5\ !$289-305 #domain transmembrane #status predicted #label TM6\ !$324-344 #domain transmembrane #status predicted #label TM7\ !$354-370 #domain transmembrane #status predicted #label TM8\ !$82,183 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$96,197 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 385 #molecular-weight 43662 #checksum 7156 SEQUENCE /// ENTRY S15157 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - yeast (Saccharomyces sp.) mitochondrion (strain 4707-22D) ORGANISM #formal_name mitochondrion Saccharomyces sp. DATE 12-Feb-1993 #sequence_revision 20-Aug-1994 #text_change 03-Jun-2002 ACCESSIONS S15157 REFERENCE S15157 !$#authors Tian, G.L.; Michel, F.; Macadre, C.; Slonimski, P.P.; !1Lazowska, J. !$#journal J. Mol. Biol. (1991) 218:747-760 !$#title Incipient mitochondrial evolution in yeasts. II. The !1complete sequence of the gene coding for cytochrome b in !1Saccharomyces douglasii reveals the presence of both new and !1conserved introns and discloses major differences in the !1fixation of mutations in evolution. !$#cross-references MUID:91218158; PMID:1708831 !$#accession S15157 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-385 ##label TIA !'##note the source is designated as Saccharomyces douglasii GENETICS !$#gene cob !$#genome mitochondrion !$#genetic_code SGC2 !$#introns 131/3; 139/1; 143/3; 169/2 FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$10-340 #domain cytochrome b homology #label CBH\ !$10-210 #domain cytochrome b6 homology #label CB6\ !$35-51 #domain transmembrane #status predicted #label TM1\ !$80-98 #domain transmembrane #status predicted #label TM2\ !$118-136 #domain transmembrane #status predicted #label TM3\ !$179-201 #domain transmembrane #status predicted #label TM4\ !$222-340 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$230-246 #domain transmembrane #status predicted #label TM5\ !$289-305 #domain transmembrane #status predicted #label TM6\ !$324-342 #domain transmembrane #status predicted #label TM7\ !$354-370 #domain transmembrane #status predicted #label TM8\ !$82,183 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$96,197 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 385 #molecular-weight 43616 #checksum 7959 SEQUENCE /// ENTRY S12352 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - yeast (Kluyveromyces marxianus var. lactis) mitochondrion ORGANISM #formal_name mitochondrion Kluyveromyces marxianus var. lactis, Candida sphaerica DATE 12-Feb-1993 #sequence_revision 20-Aug-1994 #text_change 03-Jun-2002 ACCESSIONS S12352; S09405 REFERENCE S12352 !$#authors Brunner, A.; Coria, R. !$#journal Yeast (1989) 5:209-218 !$#title Cloning and sequencing of the gene for apocytochrome b of !1the yeast Kluyveromyces lactis strains WM27 (NRRL Y-17066) !1and WM37 (NRRL Y-1140). !$#cross-references MUID:89284741; PMID:2735138 !$#accession S12352 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-386 ##label BRU GENETICS !$#genome mitochondrion !$#genetic_code SGC2 FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$10-340 #domain cytochrome b homology #label CBH\ !$10-210 #domain cytochrome b6 homology #label CB6\ !$35-51 #domain transmembrane #status predicted #label TM1\ !$80-98 #domain transmembrane #status predicted #label TM2\ !$118-134 #domain transmembrane #status predicted #label TM3\ !$179-201 #domain transmembrane #status predicted #label TM4\ !$222-340 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$230-246 #domain transmembrane #status predicted #label TM5\ !$289-305 #domain transmembrane #status predicted #label TM6\ !$324-344 #domain transmembrane #status predicted #label TM7\ !$354-370 #domain transmembrane #status predicted #label TM8\ !$82,183 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$96,197 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 386 #molecular-weight 43652 #checksum 7240 SEQUENCE /// ENTRY CBUTB #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - Trypanosoma brucei mitochondrion ORGANISM #formal_name mitochondrion Trypanosoma brucei DATE 18-Apr-1984 #sequence_revision 18-Apr-1984 #text_change 03-Jun-2002 ACCESSIONS A00160 REFERENCE A00160 !$#authors Benne, R.; De Vries, B.F.; Van den Burg, J.; Klaver, B. !$#journal Nucleic Acids Res. (1983) 11:6925-6941 !$#title The nucleotide sequence of a segment of Trypanosoma brucei !1mitochondrial maxi-circle DNA that contains the gene for !1apocytochrome b and some unusual unassigned reading frames. !$#cross-references MUID:84041494; PMID:6314266 !$#accession A00160 !'##molecule_type DNA !'##residues 1-363 ##label BEN !'##cross-references GB:X00017; NID:g13737; PIDN:CAA24915.1; PID:g578828 !'##note the authors translated the initiation codon ATT for residue 1 !1as Ile COMMENT The cytochrome b gene was isolated from a 20-kb maxicircle. GENETICS !$#genome mitochondrion !$#genetic_code SGC6 !$#start_codon ATT FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; membrane !1protein; metalloprotein; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain FEATURE !$2-334 #domain cytochrome b homology #label CBH\ !$2-202 #domain cytochrome b6 homology #label CB6\ !$216-334 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$74,175 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$88,189 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 363 #molecular-weight 43454 #checksum 2013 SEQUENCE /// ENTRY H22848 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b [validated] - Leishmania tarentolae mitochondrion ORGANISM #formal_name mitochondrion Leishmania tarentolae DATE 30-Jun-1989 #sequence_revision 26-Jul-1996 #text_change 03-Jun-2002 ACCESSIONS H22848; A28118 REFERENCE A22848 !$#authors de la Cruz, V.F.; Neckelmann, N.; Simpson, L. !$#journal J. Biol. Chem. (1984) 259:15136-15147 !$#title Sequences of six genes and several open reading frames in !1the kinetoplast maxicircle DNA of Leishmania tarentolae. !$#cross-references MUID:85079995; PMID:6096360 !$#accession H22848 !'##molecule_type DNA !'##residues 'IIIKAERKEKA',21-371 ##label DEL !'##cross-references GB:M10126; NID:g1256945 !'##note this translation is not annotated in GenBank entry LEIKPMAX, !1release 113.0; it is produced from codons 5393-6481 REFERENCE A28118 !$#authors Feagin, J.E.; Shaw, J.M.; Simpson, L.; Stuart, K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:539-543 !$#title Creation of AUG initiation codons by addition of uridines !1within cytochrome b transcripts of kinetoplastids. !$#cross-references MUID:88124876; PMID:2448777 !$#accession A28118 !'##molecule_type mRNA !'##residues 1-48 ##label FEA !'##cross-references GB:M10126; NID:g1256945 REFERENCE A59216 !$#authors Horvath, A.; Berry, E.A.; Maslov, D.A. !$#journal Science (2000) 287:1639-1640 !$#title Translation of the edited mRNA for cytochrome b in !1trypanosome mitochondria. !$#cross-references MUID:20165033; PMID:10698736 !$#contents annotation; amino acid sequencing !$#note the blocking group was removed; part of this sequence, !1including the unblocked amino end of the mature protein, was !1determined by protein sequencing GENETICS !$#genome mitochondrion !$#genetic_code SGC6 COMPLEX membrane-associated monomer; membrane-associated !1homopolymer; substoichiometric association with !1ubiquinol-cytochrome-c reductase complex FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS blocked amino end; chromoprotein; electron transfer; heme; !1iron; membrane protein; metalloprotein; mitochondrion; !1oxidative phosphorylation; oxidoreductase; respiratory !1chain; RNA editing FEATURE !$10-342 #domain cytochrome b homology #label CBH\ !$10-210 #domain cytochrome b6 homology #label CB6\ !$224-342 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$1 #modified_site blocked amino end (Met) (probably !8formylated) #status experimental\ !$82,183 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$96,202 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 371 #molecular-weight 44555 #checksum 9425 SEQUENCE /// ENTRY A32566 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - Plasmodium gallinaceum mitochondrion ORGANISM #formal_name mitochondrion Plasmodium gallinaceum DATE 07-Sep-1990 #sequence_revision 02-Aug-1994 #text_change 03-Jun-2002 ACCESSIONS A32566 REFERENCE A32566 !$#authors Aldritt, S.M.; Joseph, J.T.; Wirth, D.F. !$#journal Mol. Cell. Biol. (1989) 9:3614-3620 !$#title Sequence identification of cytochrome b in Plasmodium !1gallinaceum. !$#cross-references MUID:89384587; PMID:2779560 !$#accession A32566 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-300 ##label ALD COMMENT The location of the second heme iron ligand for each of the !1two supposed heme groups is uncertain. GENETICS !$#genome mitochondrion !$#genetic_code SGC6 FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$6-280 #domain cytochrome b homology #status atypical #label !8CBH\ !$6-182 #domain cytochrome b6 homology #status atypical !8#label CB6\ !$34-50 #domain transmembrane #status predicted #label TM1\ !$112-128 #domain transmembrane #status predicted #label TM2\ !$168-185 #domain transmembrane #status predicted #label TM3\ !$183-280 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #status atypical #label 17K\ !$228-244 #domain transmembrane #status predicted #label TM4\ !$283-299 #domain transmembrane #status predicted #label TM5\ !$63 #binding_site heme iron (His) (axial ligand) (low !8potential) #status predicted\ !$78 #binding_site heme iron (His) (axial ligand) (high !8potential) #status predicted SUMMARY #length 300 #molecular-weight 35018 #checksum 6259 SEQUENCE /// ENTRY S28664 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - Plasmodium falciparum mitochondrion ORGANISM #formal_name mitochondrion Plasmodium falciparum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S28664 REFERENCE S28662 !$#authors Feagin, J.E.; Werner, E.; Gardner, M.J.; Williamson, D.H.; !1Wilson, R.J.M. !$#journal Nucleic Acids Res. (1992) 20:879-887 !$#title Homologies between the contiguous and fragmented rRNAs of !1the two Plasmodium falciparum extrachromosomal DNAs are !1limited to core sequences. !$#cross-references MUID:92178987; PMID:1542578 !$#accession S28664 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-376 ##label FEA !'##cross-references EMBL:M76611; NID:g1311631; PIDN:AAC63391.1; !1PID:g3721518 GENETICS !$#genome mitochondrion !$#genetic_code SGC6 !$#note this protein originates from a 6K extrachromosomal linear !1element CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$6-329 #domain cytochrome b homology #status atypical #label !8CBH\ !$6-200 #domain cytochrome b6 homology #label CB6\ !$34-50 #domain transmembrane #status predicted #label TM1\ !$112-128 #domain transmembrane #status predicted #label TM2\ !$169-236 #domain transmembrane #status predicted #label TM3\ !$211-329 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #status atypical #label 17K\ !$279-295 #domain transmembrane #status predicted #label TM4\ !$336-352 #domain transmembrane #status predicted #label TM5\ !$78,173 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$92,187 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 376 #molecular-weight 43376 #checksum 2440 SEQUENCE /// ENTRY CBQFR #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - Rhodospirillum rubrum ORGANISM #formal_name Rhodospirillum rubrum DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 03-Jun-2002 ACCESSIONS S12257; A38814 REFERENCE S12255 !$#authors Majewski, C.; Trebst, A. !$#journal Mol. Gen. Genet. (1990) 224:373-382 !$#title The pet genes of Rhodospirillum rubrum: cloning and !1sequencing of the genes for the cytochrome bc(1)-complex. !$#cross-references MUID:91094774; PMID:2176269 !$#accession S12257 !'##molecule_type DNA !'##residues 1-405 ##label MA1 !'##cross-references EMBL:X55387; NID:g46382; PIDN:CAA39059.1; !1PID:g46385 !'##note the authors translated the codon AAT for residue 161 as Leu and !1CTG for residue 162 as Asn !$#accession A38814 !'##molecule_type protein !'##residues 1-26,'E' ##label MA2 GENETICS !$#gene petB CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$1-405 #product cytochrome b #status experimental #label !8MAT\ !$22-354 #domain cytochrome b homology #label CBH\ !$22-222 #domain cytochrome b6 homology #label CB6\ !$47-63 #domain transmembrane #status predicted #label TM1\ !$92-110 #domain transmembrane #status predicted #label TM2\ !$130-146 #domain transmembrane #status predicted #label TM3\ !$191-213 #domain transmembrane #status predicted #label TM4\ !$236-354 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$244-260 #domain transmembrane #status predicted #label TM5\ !$303-319 #domain transmembrane #status predicted #label TM6\ !$338-356 #domain transmembrane #status predicted #label TM7\ !$368-384 #domain transmembrane #status predicted #label TM8\ !$94,195 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$108,209 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 405 #molecular-weight 46369 #checksum 9483 SEQUENCE /// ENTRY B29336 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - Rhodobacter capsulatus ORGANISM #formal_name Rhodobacter capsulatus DATE 31-Dec-1988 #sequence_revision 22-Jul-1994 #text_change 03-Jun-2002 ACCESSIONS B29336; B25405; S09373 REFERENCE A92938 !$#authors Davidson, E.; Daldal, F. !$#journal J. Mol. Biol. (1987) 195:13-24 !$#title Primary structure of the bc-1 complex of Rhodopseudomonas !1capsulata. Nucleotide sequence of the pet operon encoding !1the Rieske, cytochrome b, and cytochrome c-1 apoproteins. !$#cross-references MUID:88011223; PMID:2821268 !$#accession B29336 !'##molecule_type DNA !'##residues 1-437 ##label DAV !'##cross-references EMBL:X05630; NID:g46093; PIDN:CAA29117.1; !1PID:g46095 REFERENCE A91162 !$#authors Gabellini, N.; Sebald, W. !$#journal Eur. J. Biochem. (1986) 154:569-579 !$#title Nucleotide sequence and transcription of the fbc operon from !1Rhodopseudomonas sphaeroides. Evaluation of the deduced !1amino acid sequences of the FeS protein, cytochrome b and !1cytochrome c-1. !$#cross-references MUID:86136096; PMID:3004982 !$#note source is designated as Rhodopseudomonas sphaeroides !$#accession B25405 !'##molecule_type DNA !'##residues 1-66,'ID',69-280,'I',282-437 ##label GAB !'##cross-references EMBL:X03476; NID:g46007; PIDN:CAA27195.1; !1PID:g46009 GENETICS !$#gene fbcB; petB CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$26-381 #domain cytochrome b homology #label CBH\ !$26-225 #domain cytochrome b6 homology #label CB6\ !$51-67 #domain transmembrane #status predicted #label TM1\ !$96-114 #domain transmembrane #status predicted #label TM2\ !$134-150 #domain transmembrane #status predicted #label TM3\ !$146-193 #domain periplasmic #status predicted #label PER1\ !$195-217 #domain transmembrane #status predicted #label TM4\ !$245-381 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$253-269 #domain transmembrane #status predicted #label TM5\ !$270-329 #domain periplasmic #status predicted #label PER2\ !$330-346 #domain transmembrane #status predicted #label TM6\ !$365-383 #domain transmembrane #status predicted #label TM7\ !$395-411 #domain transmembrane #status predicted #label TM8\ !$97,198 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$111,212 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 437 #molecular-weight 49349 #checksum 483 SEQUENCE /// ENTRY B29413 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - Paracoccus denitrificans ALTERNATE_NAMES bc1 complex; complex III ORGANISM #formal_name Paracoccus denitrificans DATE 31-Mar-1989 #sequence_revision 20-Aug-1994 #text_change 03-Jun-2002 ACCESSIONS B29413 REFERENCE A92613 !$#authors Kurowski, B.; Ludwig, B. !$#journal J. Biol. Chem. (1987) 262:13805-13811 !$#title The genes of the Paracoccus denitrificans bc-1 complex. !1Nucleotide sequence and homologies between bacterial and !1mitochondrial subunits. !$#cross-references MUID:88007612; PMID:2820981 !$#accession B29413 !'##molecule_type DNA !'##residues 1-440 ##label KUR !'##cross-references GB:M17522; NID:g150569; PIDN:AAA25572.1; !1PID:g150571 CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; oxidoreductase; transmembrane protein FEATURE !$26-381 #domain cytochrome b homology #label CBH\ !$26-225 #domain cytochrome b6 homology #label CB6\ !$51-67 #domain transmembrane #status predicted #label TM1\ !$96-114 #domain transmembrane #status predicted #label TM2\ !$134-150 #domain transmembrane #status predicted #label TM3\ !$195-217 #domain transmembrane #status predicted #label TM4\ !$245-381 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$253-269 #domain transmembrane #status predicted #label TM5\ !$330-346 #domain transmembrane #status predicted #label TM6\ !$365-383 #domain transmembrane #status predicted #label TM7\ !$395-411 #domain transmembrane #status predicted #label TM8\ !$97,198 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$111,212 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 440 #molecular-weight 50116 #checksum 8256 SEQUENCE /// ENTRY S13869 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - Rhodobacter sphaeroides ORGANISM #formal_name Rhodobacter sphaeroides DATE 31-Dec-1988 #sequence_revision 22-Jul-1994 #text_change 03-Jun-2002 ACCESSIONS S13869; A34591 REFERENCE S13868 !$#authors Yun, C.H.; Beci, R.; Crofts, A.R.; Kaplan, S.; Gennis, R.B. !$#journal Eur. J. Biochem. (1990) 194:399-411 !$#title Cloning and DNA sequencing of the fbc operon encoding the !1cytochrome bc(1) complex from Rhodobacter sphaeroides. !1Characterization of fbc deletion mutants and complementation !1by a site-specific mutational variant. !$#cross-references MUID:91099313; PMID:2176595 !$#accession S13869 !'##molecule_type DNA !'##residues 1-445 ##label YUN !'##cross-references EMBL:X56157; NID:g46425; PIDN:CAA39624.1; !1PID:g46427 !'##note the sequence from Fig. 5 is inconsistent with that from Fig. 2 !1in having 179-Glu, 277-Leu, and 316-Cys REFERENCE A34591 !$#authors Andrews, K.M.; Crofts, A.R.; Gennis, R.B. !$#journal Biochemistry (1990) 29:2645-2651 !$#title Large-scale purification and characterization of a highly !1active four-subunit cytochrome bc-1 complex from Rhodobacter !1sphaeroides. !$#cross-references MUID:90268011; PMID:2161250 !$#accession A34591 !'##molecule_type protein !'##residues 2-6,'X',8-9,'Z',11-15,'XX',18-19 ##label AND GENETICS !$#gene fbcB CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; oxidoreductase; photosynthesis; respiratory !1chain; transmembrane protein FEATURE !$2-445 #product cytochrome b #status experimental #label !8MAT\ !$26-381 #domain cytochrome b homology #label CBH\ !$26-225 #domain cytochrome b6 homology #label CB6\ !$43-67 #domain transmembrane #status predicted #label TM1\ !$95-113 #domain transmembrane #status predicted #label TM2\ !$127-149 #domain transmembrane #status predicted #label TM3\ !$150-193 #domain periplasmic #status predicted #label PER1\ !$194-216 #domain transmembrane #status predicted #label TM4\ !$245-381 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$253-270 #domain transmembrane #status predicted #label TM5\ !$271-329 #domain periplasmic #status predicted #label PER2\ !$330-349 #domain transmembrane #status predicted #label TM6\ !$365-382 #domain transmembrane #status predicted #label TM7\ !$394-413 #domain transmembrane #status predicted #label TM8\ !$97,198 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$111,212 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 445 #molecular-weight 50049 #checksum 2932 SEQUENCE /// ENTRY JQ0346 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - Rhodopseudomonas viridis ORGANISM #formal_name Rhodopseudomonas viridis DATE 07-Sep-1990 #sequence_revision 02-Aug-1994 #text_change 03-Jun-2002 ACCESSIONS JQ0346 REFERENCE JQ0345 !$#authors Verbist, J.; Lang, F.; Gabellini, N.; Oesterhelt, D. !$#journal Mol. Gen. Genet. (1989) 219:445-452 !$#title Cloning and sequencing of the fbcF, B and C genes encoding !1the cytochrome b/c1 complex from Rhodopseudomonas viridis. !$#cross-references MUID:90158506; PMID:2560136 !$#accession JQ0346 !'##molecule_type DNA !'##residues 1-419 ##label VER !'##experimental_source strain 133 COMMENT This protein is one of the three subunits of the !1ubiquinol-cytochrome C2 oxidoreductase complex, which is !1coupled with another membrane-protein complex at the !1reaction center in a cyclic electron-transport system that !1catalyzes the synthesis of ATP. GENETICS !$#gene fbcB CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; oxidoreductase; transmembrane protein FEATURE !$24-356 #domain cytochrome b homology #label CBH\ !$24-224 #domain cytochrome b6 homology #label CB6\ !$49-65 #domain transmembrane #status predicted #label TM1\ !$94-112 #domain transmembrane #status predicted #label TM2\ !$132-148 #domain transmembrane #status predicted #label TM3\ !$193-215 #domain transmembrane #status predicted #label TM4\ !$238-356 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$246-262 #domain transmembrane #status predicted #label TM5\ !$305-321 #domain transmembrane #status predicted #label TM6\ !$340-360 #domain transmembrane #status predicted #label TM7\ !$370-386 #domain transmembrane #status predicted #label TM8\ !$96,197 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$110,211 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 419 #molecular-weight 47237 #checksum 3151 SEQUENCE /// ENTRY S41691 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b - Theileria parva mitochondrion ORGANISM #formal_name mitochondrion Theileria parva DATE 31-Dec-1993 #sequence_revision 20-Aug-1994 #text_change 03-Jun-2002 ACCESSIONS S41691; S40156 REFERENCE S41689 !$#authors Kairo, A.; Fairlamb, A.H.; Gobright, E.; Nene, V. !$#journal EMBO J. (1994) 13:898-905 !$#title A 7.1 kb linear DNA molecule of Theileria parva has !1scrambled rDNA sequences and open reading frames for !1mitochondrially encoded proteins. !$#cross-references MUID:94155854; PMID:8112303 !$#accession S41691 !'##molecule_type DNA !'##residues 1-386 ##label KAI !'##cross-references EMBL:Z23263; NID:g437862; PIDN:CAA80800.1; !1PID:g437865 GENETICS !$#genome mitochondrion !$#genetic_code SGC6 FUNCTION !$#description the net reaction catalyzed by the ubiquinol-cytochrome-c !1reductase complex (complex III) is the oxidation of one !1molecule of ubiquinol to ubiquinone by two molecules of !1cytochrome c, with two hydrogen ions taken up from the !1mitochondrial matrix and four hydrogen ions released into !1the intermembrane space !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome b; cytochrome b homology; cytochrome !1b6 homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$24-347 #domain cytochrome b homology #label CBH\ !$24-218 #domain cytochrome b6 homology #label CB6\ !$49-65 #domain transmembrane #status predicted #label TM1\ !$94-112 #domain transmembrane #status predicted #label TM2\ !$130-146 #domain transmembrane #status predicted #label TM3\ !$187-209 #domain transmembrane #status predicted #label TM4\ !$230-347 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$238-254 #domain transmembrane #status predicted #label TM5\ !$299-316 #domain transmembrane #status predicted #label TM6\ !$339-356 #domain transmembrane #status predicted #label TM7\ !$360-375 #domain transmembrane #status predicted #label TM8\ !$96,191 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$110,205 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 386 #molecular-weight 43756 #checksum 1934 SEQUENCE /// ENTRY B32382 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) - Bradyrhizobium japonicum CONTAINS ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome b; ubiquinol-cytochrome-c reductase (EC 1.10.2.2) cytochrome c1 ORGANISM #formal_name Bradyrhizobium japonicum DATE 12-Oct-1989 #sequence_revision 20-Aug-1994 #text_change 03-Jun-2002 ACCESSIONS B32382; A39715 REFERENCE A32382 !$#authors Thoeny-Meyer, L.; Stax, D.; Hennecke, H. !$#journal Cell (1989) 57:683-697 !$#title An unusual gene cluster for the cytochrome bc-1 complex in !1Bradyrhizobium japonicum and its requirement for effective !1root nodule symbiosis. !$#cross-references MUID:89249332; PMID:2541921 !$#accession B32382 !'##molecule_type DNA !'##residues 1-687 ##label THO !'##cross-references GB:J03176; NID:g152082; PIDN:AAA26200.1; !1PID:g152084 REFERENCE A39715 !$#authors Thoeny-Meyer, L.; James, P.; Hennecke, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:5001-5005 !$#title From one gene to two proteins: the biogenesis of cytochromes !1b and c-1 in Bradyrhizobium japonicum. !$#cross-references MUID:91271320; PMID:1647023 !$#accession A39715 !'##status preliminary !'##molecule_type protein !'##residues 439-444 ##label TH2 GENETICS !$#gene fcbH CLASSIFICATION #superfamily fcbH bifunctional protein; cytochrome b !1homology; cytochrome b6 homology; cytochrome c1 heme protein !1homology; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1membrane-associated complex; metalloprotein; oxidative !1phosphorylation; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$1-412 #product ubiquinol-cytochrome-c reductase, cytochrome !8b #status predicted #label CB1\ !$24-356 #domain cytochrome b homology #label CBH\ !$24-224 #domain cytochrome b6 homology #label CB6\ !$49-65 #domain transmembrane #status predicted #label TM1\ !$94-112 #domain transmembrane #status predicted #label TM2\ !$132-148 #domain transmembrane #status predicted #label TM3\ !$193-215 #domain transmembrane #status predicted #label TM4\ !$238-356 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$244-260 #domain transmembrane #status predicted #label TM5\ !$303-319 #domain transmembrane #status predicted #label TM6\ !$338-358 #domain transmembrane #status predicted #label TM7\ !$368-383 #domain transmembrane #status predicted #label TM8\ !$413-687 #product ubiquinol-cytochrome-c reductase, cytochrome !8c1 #status predicted #label CC1\ !$440-687 #domain cytochrome c1 heme protein homology #label !8C1H\ !$96,197 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$110,211 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted\ !$471,474 #binding_site heme (Cys) (covalent) #status !8predicted\ !$475,616 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 687 #molecular-weight 76469 #checksum 3243 SEQUENCE /// ENTRY CBSP6 #type complete TITLE plastoquinol-plastocyanin reductase (EC 1.10.99.1) cytochrome b6 - spinach chloroplast ORGANISM #formal_name chloroplast Spinacia oleracea #common_name spinach DATE 03-Aug-1984 #sequence_revision 02-Aug-1994 #text_change 03-Jun-2002 ACCESSIONS S03021; A00161; S00429 REFERENCE S03021 !$#authors Westhoff, P.; Herrmann, R.G. !$#journal Eur. J. Biochem. (1988) 171:551-564 !$#title Complex RNA maturation in chloroplasts. !$#cross-references MUID:88151952; PMID:2831053 !$#accession S03021 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-22 ##label WES !'##note this sequence is a revision to the sequence from reference !1S00429 REFERENCE A00161 !$#authors Widger, W.R.; Cramer, W.A.; Herrmann, R.G.; Trebst, A. !$#citation unpublished results, 1984, cited by Widger, W.R., Cramer, !1W.A., Herrmann, R.G., Trebst, A., Proc. Natl. Acad. Sci. !1U.S.A. 81, 674-678, 1984 !$#accession A00161 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 'MIGSKNVSRFRRLRMI',21-215 ##label WID REFERENCE S00429 !$#authors Heinemeyer, W.; Alt, J.; Herrmann, R.G. !$#journal Curr. Genet. (1984) 8:543-549 !$#title Nucleotide sequence of the clustered genes for apocytochrome !1b6 and subunit 4 of the cytochrome b/f complex in the !1spinach plastid chromosome. !$#accession S00429 !'##molecule_type DNA !'##residues 'MIGSKNVSRFRRLRMI',21-215 ##label HEI !'##cross-references EMBL:X07106; NID:g12283 !'##note this sequence has been revised in reference S03021 COMMENT This cytochrome is the chloroplast counterpart of the !1mitochondrial cytochrome b. GENETICS !$#gene petB !$#genome chloroplast !$#introns 2/3 CLASSIFICATION #superfamily cytochrome b6; cytochrome b6 homology KEYWORDS chloroplast; chromoprotein; electron transfer; heme; iron; !1metalloprotein; oxidoreductase; photosynthesis; thylakoid FEATURE !$15-215 #domain cytochrome b6 homology #label CB6\ !$86,187 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$100,202 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 215 #molecular-weight 24166 #checksum 9582 SEQUENCE /// ENTRY CBZM6R #type complete TITLE plastoquinol-plastocyanin reductase (EC 1.10.99.1) cytochrome b6, splice form 2 - maize chloroplast ORGANISM #formal_name chloroplast Zea mays #common_name maize DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 03-Jun-2002 ACCESSIONS S08592 REFERENCE S07171 !$#authors Rock, C.D.; Barkan, A.; Taylor, W.C. !$#journal Curr. Genet. (1987) 12:69-77 !$#title The maize plastid psbB-psbF-petB-petD gene cluster: spliced !1and unspliced petB and petD RNAs encode alternative !1products. !$#cross-references MUID:88210525; PMID:2835175 !$#accession S08592 !'##molecule_type DNA !'##residues 1-215 ##label ROC !'##cross-references EMBL:X05422; NID:g12434; PIDN:CAA28999.1; !1PID:g311718 COMMENT For splice form 1, see PIR:S58581. GENETICS !$#gene petB !$#genome chloroplast !$#introns 2/3 CLASSIFICATION #superfamily cytochrome b6; cytochrome b6 homology KEYWORDS alternative splicing; chloroplast; chromoprotein; electron !1transfer; heme; iron; metalloprotein; oxidoreductase; !1photosynthesis; thylakoid FEATURE !$15-215 #domain cytochrome b6 homology #label CB6\ !$86,187 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$100,202 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 215 #molecular-weight 24180 #checksum 9478 SEQUENCE /// ENTRY S04149 #type complete TITLE plastoquinol-plastocyanin reductase (EC 1.10.99.1) cytochrome b6, splice form 1 - barley chloroplast ORGANISM #formal_name chloroplast Hordeum vulgare #common_name barley DATE 07-Jun-1990 #sequence_revision 02-Aug-1994 #text_change 03-Jun-2002 ACCESSIONS S04149; JN0381 REFERENCE S04100 !$#authors Reverdatto, S.V.; Andreeva, A.V.; Buryakova, A.A.; !1Chakhmakhcheva, O.G.; Efimov, V.A. !$#journal Nucleic Acids Res. (1989) 17:2859-2860 !$#title Nucleotide sequence of the 5.2 kbp barley chloroplast DNA !1fragment, containing psbB-psbH-petB-petD gene cluster. !$#cross-references MUID:89240047; PMID:2654887 !$#accession S04149 !'##molecule_type DNA !'##residues 1-232 ##label REV !'##cross-references EMBL:X14107; NID:g11593; PIDN:CAA32267.1; !1PID:g11596 COMMENT For splice form 2, see PIR:S09186. GENETICS !$#gene petB !$#genome chloroplast CLASSIFICATION #superfamily cytochrome b6; cytochrome b6 homology KEYWORDS alternative splicing; chloroplast; chromoprotein; electron !1transfer; heme; iron; metalloprotein; oxidoreductase; !1photosynthesis; thylakoid FEATURE !$32-232 #domain cytochrome b6 homology #label CB6\ !$103,204 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$117,219 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 232 #molecular-weight 26078 #checksum 4328 SEQUENCE /// ENTRY CBNT6 #type complete TITLE plastoquinol-plastocyanin reductase (EC 1.10.99.1) cytochrome b6 - common tobacco chloroplast ALTERNATE_NAMES cytochrome b563 ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 03-Jun-2002 ACCESSIONS A00162 REFERENCE A00149 !$#authors Sugiura, M. !$#submission submitted to the EMBL Data Library, August 1986 !$#accession A00162 !'##molecule_type DNA !'##residues 1-215 ##label SUG !'##experimental_source cv. Bright Yellow 4 REFERENCE A38013 !$#authors Shinozaki, K.; Ohme, M.; Tanaka, M.; Wakasugi, T.; !1Hayashida, N.; Matsubayashi, T.; Zaita, N.; Chunwongse, J.; !1Obokata, J.; Yamaguchi-Shinozaki, K.; Ohto, C.; Torazawa, !1K.; Meng, B.Y.; Sugita, M.; Deno, H.; Kamogashira, T.; !1Yamada, K.; Kusuda, J.; Takaiwa, F.; Kato, A.; Tohdoh, N.; !1Shimada, H.; Sugiura, M. !$#journal EMBO J. (1986) 5:2043-2049 !$#title The complete nucleotide sequence of the tobacco chloroplast !1genome: its gene organization and expression. !$#contents annotation; gene organization, sites, features COMMENT This cytochrome is one of the components of a specific !1stoichiometric cytochrome b6-f complex that contains two !1molecules of cytochrome b6, one cytochrome f, and one !1nonheme iron-sulfur center. GENETICS !$#gene petB !$#genome chloroplast !$#introns 2/3 CLASSIFICATION #superfamily cytochrome b6; cytochrome b6 homology KEYWORDS chloroplast; chromoprotein; electron transfer; heme; iron; !1metalloprotein; oxidoreductase; photosynthesis; thylakoid FEATURE !$15-215 #domain cytochrome b6 homology #label CB6\ !$86,187 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$100,202 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 215 #molecular-weight 24136 #checksum 9633 SEQUENCE /// ENTRY CBRZ6 #type complete TITLE plastoquinol-plastocyanin reductase (EC 1.10.99.1) cytochrome b6 - rice chloroplast ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 03-Jun-2002 ACCESSIONS JQ0256; S05136 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0256 !'##molecule_type DNA !'##residues 1-215 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05136 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-215 ##label HIR !'##cross-references EMBL:X15901; NID:g11957; PIDN:CAA33977.1; !1PID:g669082 !'##experimental_source cv. Nihonbare COMMENT This cytochrome is one of the components of a specific !1stoichiometric cytochrome b6-f complex that contains two !1molecules of cytochrome b6, one cytochrome f and one nonheme !1iron-sulfur center. GENETICS !$#gene petB !$#map_position CP1232-71237,72049-72690 !$#genome chloroplast !$#introns 2/3 CLASSIFICATION #superfamily cytochrome b6; cytochrome b6 homology KEYWORDS chloroplast; chromoprotein; electron transfer; heme; iron; !1metalloprotein; oxidoreductase; photosynthesis; thylakoid FEATURE !$15-215 #domain cytochrome b6 homology #label CB6\ !$86,187 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$100,202 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 215 #molecular-weight 24182 #checksum 9304 SEQUENCE /// ENTRY S09186 #type complete TITLE plastoquinol-plastocyanin reductase (EC 1.10.99.1) cytochrome b6, splice form 2 - barley chloroplast ORGANISM #formal_name chloroplast Hordeum vulgare #common_name barley DATE 07-Jun-1990 #sequence_revision 02-Aug-1994 #text_change 03-Jun-2002 ACCESSIONS S09186; JN0348 REFERENCE S04100 !$#authors Reverdatto, S.V.; Andreeva, A.V.; Buryakova, A.A.; !1Chakhmakhcheva, O.G.; Efimov, V.A. !$#journal Nucleic Acids Res. (1989) 17:2859-2860 !$#title Nucleotide sequence of the 5.2 kbp barley chloroplast DNA !1fragment, containing psbB-psbH-petB-petD gene cluster. !$#cross-references MUID:89240047; PMID:2654887 !$#accession S09186 !'##molecule_type DNA !'##residues 1-215 ##label REV !'##cross-references EMBL:X14107; NID:g11593; PIDN:CAA32266.1; !1PID:g1617031 COMMENT For splice form 1, see PIR:S04149. GENETICS !$#gene petB !$#genome chloroplast !$#introns 2/3 CLASSIFICATION #superfamily cytochrome b6; cytochrome b6 homology KEYWORDS alternative splicing; chloroplast; chromoprotein; electron !1transfer; heme; iron; metalloprotein; oxidoreductase; !1photosynthesis; thylakoid FEATURE !$15-215 #domain cytochrome b6 homology #label CB6\ !$86,187 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$100,202 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 215 #molecular-weight 24166 #checksum 9436 SEQUENCE /// ENTRY CBLV6 #type complete TITLE plastoquinol-plastocyanin reductase (EC 1.10.99.1) cytochrome b6 - liverwort (Marchantia polymorpha) chloroplast ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 03-Jun-2002 ACCESSIONS S01552; S02432; A00163 REFERENCE S01529 !$#authors Fukuzawa, H.; Kohchi, T.; Sano, T.; Shirai, H.; Umesono, K.; !1Inokuchi, H.; Ozeki, H.; Ohyama, K. !$#journal J. Mol. Biol. (1988) 203:333-351 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. III. Gene organization of the large !1single copy region from rbcL to trnI(CAU). !$#cross-references MUID:89068687; PMID:3199436 !$#accession S01552 !'##molecule_type DNA !'##residues 1-215 ##label FUK !'##cross-references EMBL:X04465; NID:g11640; PIDN:CAA28115.1; !1PID:g4376232 REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features REFERENCE S02432 !$#authors Fukuzawa, H.; Yoshida, T.; Kohchi, T.; Okumura, T.; Sawano, !1Y.; Ohyama, K. !$#journal FEBS Lett. (1987) 220:61-66 !$#title Splicing of group II introns in mRNAs coding for cytochrome !1b6 and subunit IV in the liverwort Marchantia polymorpha !1chloroplast genome. Exon specifying a region coding for two !1genes with the spacer region. !$#accession S02432 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-8 ##label FUW GENETICS !$#gene petB !$#genome chloroplast !$#introns 2/3 CLASSIFICATION #superfamily cytochrome b6; cytochrome b6 homology KEYWORDS chloroplast; chromoprotein; electron transfer; heme; iron; !1metalloprotein; oxidoreductase; photosynthesis; thylakoid FEATURE !$15-215 #domain cytochrome b6 homology #label CB6\ !$86,187 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$100,202 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 215 #molecular-weight 24307 #checksum 8453 SEQUENCE /// ENTRY S34548 #type complete TITLE plastoquinol-plastocyanin reductase (EC 1.10.99.1) cytochrome b6 - Euglena gracilis chloroplast ORGANISM #formal_name chloroplast Euglena gracilis DATE 30-Sep-1993 #sequence_revision 02-Aug-1994 #text_change 03-Jun-2002 ACCESSIONS S34548; S34915; S41617 REFERENCE S34494 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.; Monfort, !1A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#submission submitted to the EMBL Data Library, January 1993 !$#description The complete sequence of the Euglena gracilis chloroplast !1genome (tentative). !$#accession S34548 !'##molecule_type DNA !'##residues 1-215 ##label HAL1 !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50129.1; !1PID:g415785 !'##experimental_source strain Pringsheim Z REFERENCE S34862 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.R.; !1Monfort, A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#journal Nucleic Acids Res. (1993) 21:3537-3544 !$#title Complete sequence of Euglena gracilis chloroplast DNA. !$#cross-references MUID:93347989; PMID:8346031 !$#accession S34915 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-215 ##label HAL2 !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50129.1; !1PID:g415785 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1993 REFERENCE S41615 !$#authors Hong, L.; Hallick, R.B. !$#journal Curr. Genet. (1994) 25:270-281 !$#title Gene structure and expression of a novel Euglena gracilis !1chloroplast operon encoding cytochrome b6 and the beta and !1epsilon subunits of the H(+)-ATP synthase complex. !$#cross-references MUID:95007823; PMID:7923415 !$#accession S41617 !'##status preliminary !'##molecule_type DNA !'##residues 1-215 ##label HON !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50129.1; !1PID:g415785 !'##note the authors translated the codon TTC for residue 8 as Leu GENETICS !$#gene petB !$#genome chloroplast !$#introns 8/2; 22/1 CLASSIFICATION #superfamily cytochrome b6; cytochrome b6 homology KEYWORDS chloroplast; chromoprotein; electron transfer; heme; iron; !1metalloprotein; oxidoreductase; photosynthesis; thylakoid FEATURE !$15-215 #domain cytochrome b6 homology #label CB6\ !$86,187 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$100,202 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 215 #molecular-weight 24385 #checksum 7056 SEQUENCE /// ENTRY CBKL6P #type complete TITLE plastoquinol-plastocyanin reductase (EC 1.10.99.1) cytochrome b6 - Chlorella protothecoides chloroplast ORGANISM #formal_name chloroplast Chlorella protothecoides DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Jun-2002 ACCESSIONS S06159 REFERENCE S06159 !$#authors Reimann, A.; Kueck, U. !$#journal Plant Mol. Biol. (1989) 13:255-256 !$#title Nucleotide sequence of the plastid genes for apocytochrome b !1(6) (petB) and subunit IV of the cytochrome b(6)-f complex !1(petD) from the green alga Chlorella protothecoides: lack of !1introns. !$#cross-references MUID:92003673; PMID:2519117 !$#accession S06159 !'##molecule_type DNA !'##residues 1-215 ##label REI !'##cross-references EMBL:X15244; NID:g18092; PIDN:CAA33322.1; !1PID:g18093 GENETICS !$#gene petB !$#genome chloroplast CLASSIFICATION #superfamily cytochrome b6; cytochrome b6 homology KEYWORDS chloroplast; chromoprotein; electron transfer; heme; iron; !1metalloprotein; oxidoreductase; photosynthesis; thylakoid FEATURE !$15-215 #domain cytochrome b6 homology #label CB6\ !$86,187 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$100,202 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 215 #molecular-weight 24429 #checksum 8314 SEQUENCE /// ENTRY S21253 #type complete TITLE plastoquinol-plastocyanin reductase (EC 1.10.99.1) cytochrome b6 - Chlamydomonas reinhardtii chloroplast ORGANISM #formal_name chloroplast Chlamydomonas reinhardtii DATE 03-Feb-1994 #sequence_revision 02-Aug-1994 #text_change 03-Jun-2002 ACCESSIONS S21253; S16917 REFERENCE S20938 !$#authors Huang, C.; Liu, X.Q. !$#journal Plant Mol. Biol. (1992) 18:985-988 !$#title Nucleotide sequence of the frxC, petB and trnL genes in the !1chloroplast genome of Chlamydomonas reinhardtii. !$#cross-references MUID:92256821; PMID:1581576 !$#accession S21253 !'##status translation not shown !'##molecule_type DNA !'##residues 1-215 ##label HUA !'##cross-references EMBL:X62905; NID:g12497; PIDN:CAA44690.1; !1PID:g12499 REFERENCE S16916 !$#authors Bueschlen, S.; Choquet, Y.; Kuras, R.; Wollman, F.A. !$#journal FEBS Lett. (1991) 284:257-262 !$#title Nucleotide sequences of the continuous and separated petA, !1petB and petD chloroplast genes in Chlamydomonas !1reinhardtii. !$#cross-references MUID:91285146; PMID:2060646 !$#accession S16917 !'##molecule_type DNA !'##residues 1-215 ##label BUE !'##cross-references EMBL:X72918; NID:g603530; PIDN:CAA51423.1; !1PID:g288909 GENETICS !$#gene petB !$#genome chloroplast CLASSIFICATION #superfamily cytochrome b6; cytochrome b6 homology KEYWORDS chloroplast; chromoprotein; electron transfer; heme; iron; !1metalloprotein; oxidoreductase; photosynthesis; thylakoid FEATURE !$15-215 #domain cytochrome b6 homology #label CB6\ !$86,187 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$100,202 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 215 #molecular-weight 24164 #checksum 8607 SEQUENCE /// ENTRY A30807 #type complete TITLE plastoquinol-plastocyanin reductase (EC 1.10.99.1) cytochrome b6 - Nostoc sp. ORGANISM #formal_name Nostoc sp. DATE 01-Dec-1989 #sequence_revision 02-Aug-1994 #text_change 03-Jun-2002 ACCESSIONS A30807 REFERENCE A94683 !$#authors Kallas, T.; Spiller, S.; Malkin, R. !$#journal J. Biol. Chem. (1988) 263:14334-14342 !$#title Characterization of two operons encoding the cytochrome !1b-6-f complex of the cyanobacterium Nostoc PCC 7906. Highly !1conserved sequences but different gene organization than in !1chloroplasts. !$#cross-references MUID:89008280; PMID:2844767 !$#accession A30807 !'##molecule_type DNA !'##residues 1-215 ##label KAL !'##cross-references GB:J03967; NID:g145022; PIDN:AAA23330.1; !1PID:g145023 !'##experimental_source PCC 7906 CLASSIFICATION #superfamily cytochrome b6; cytochrome b6 homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; oxidoreductase; photosynthesis; thylakoid FEATURE !$15-215 #domain cytochrome b6 homology #label CB6\ !$86,187 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$100,202 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted SUMMARY #length 215 #molecular-weight 24259 #checksum 8311 SEQUENCE /// ENTRY WMLV17 #type complete TITLE plastoquinol-plastocyanin reductase (EC 1.10.99.1) 17K protein - liverwort (Marchantia polymorpha) chloroplast ALTERNATE_NAMES cytochrome b6-f complex 17K protein; cytochrome b6-f complex protein 4 ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 03-Jun-2002 ACCESSIONS A00166; S01553; S02433 REFERENCE A00150 !$#authors Ohyama, K. !$#submission submitted to the EMBL Data Library, October 1986 !$#accession A00166 !'##molecule_type DNA !'##residues 1-160 ##label OHY REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features REFERENCE S01529 !$#authors Fukuzawa, H.; Kohchi, T.; Sano, T.; Shirai, H.; Umesono, K.; !1Inokuchi, H.; Ozeki, H.; Ohyama, K. !$#journal J. Mol. Biol. (1988) 203:333-351 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. III. Gene organization of the large !1single copy region from rbcL to trnI(CAU). !$#cross-references MUID:89068687; PMID:3199436 !$#accession S01553 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-160 ##label FUK !'##cross-references GB:X04465; GB:Y00686; NID:g11640; PIDN:CAA28116.1; !1PID:g453594 REFERENCE S02432 !$#authors Fukuzawa, H.; Yoshida, T.; Kohchi, T.; Okumura, T.; Sawano, !1Y.; Ohyama, K. !$#journal FEBS Lett. (1987) 220:61-66 !$#title Splicing of group II introns in mRNAs coding for cytochrome !1b6 and subunit IV in the liverwort Marchantia polymorpha !1chloroplast genome. Exon specifying a region coding for two !1genes with the spacer region. !$#accession S02433 !'##status preliminary !'##molecule_type DNA !'##residues 1-160 ##label FU2 GENETICS !$#gene petD !$#genome chloroplast !$#introns 3/2 CLASSIFICATION #superfamily plastoquinol-plastocyanin reductase 17K !1protein; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chloroplast; oxidoreductase; photosynthesis; thylakoid FEATURE !$24-144 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K SUMMARY #length 160 #molecular-weight 17386 #checksum 4688 SEQUENCE /// ENTRY S58582 #type complete TITLE plastoquinol-plastocyanin reductase (EC 1.10.99.1) 17K protein - maize chloroplast ALTERNATE_NAMES cytochrome b/f complex 17K protein; cytochrome b6-f complex chain IV ORGANISM #formal_name chloroplast Zea mays #common_name maize DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S58582; S08593 REFERENCE S58531 !$#authors Maier, R.M.; Neckermann, K.; Igloi, G.L.; Koessel, H. !$#journal J. Mol. Biol. (1995) 251:614-628 !$#title Complete sequence of the maize chloroplast genome: gene !1content, hotspots of divergence and fine tuning of genetic !1information by transcript editing. !$#cross-references MUID:95395841; PMID:7666415 !$#accession S58582 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-160 ##label MAI !'##cross-references EMBL:X86563; NID:g902200; PIDN:CAA60316.1; !1PID:g902252 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1995 REFERENCE S07171 !$#authors Rock, C.D.; Barkan, A.; Taylor, W.C. !$#journal Curr. Genet. (1987) 12:69-77 !$#title The maize plastid psbB-psbF-petB-petD gene cluster: spliced !1and unspliced petB and petD RNAs encode alternative !1products. !$#cross-references MUID:88210525; PMID:2835175 !$#accession S08593 !'##molecule_type DNA !'##residues 1-68 ##label ROC !'##cross-references EMBL:X05422; NID:g12434; PIDN:CAA29001.1; !1PID:g311719 GENETICS !$#gene petD !$#genome chloroplast !$#introns 3/2 CLASSIFICATION #superfamily plastoquinol-plastocyanin reductase 17K !1protein; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chloroplast; electron transfer; membrane-associated complex; !1oxidoreductase; photosynthesis; thylakoid FEATURE !$24-144 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K SUMMARY #length 160 #molecular-weight 17489 #checksum 7247 SEQUENCE /// ENTRY WMSP17 #type complete TITLE plastoquinol-plastocyanin reductase (EC 1.10.99.1) 17K protein - spinach chloroplast ALTERNATE_NAMES cytochrome b6-f complex 17K protein; cytochrome b6-f complex chain IV ORGANISM #formal_name chloroplast Spinacia oleracea #common_name spinach DATE 03-Aug-1984 #sequence_revision 02-Jul-1996 #text_change 03-Jun-2002 ACCESSIONS S00458; S03022; A00164 REFERENCE S00429 !$#authors Heinemeyer, W.; Alt, J.; Herrmann, R.G. !$#journal Curr. Genet. (1984) 8:543-549 !$#title Nucleotide sequence of the clustered genes for apocytochrome !1b6 and subunit 4 of the cytochrome b/f complex in the !1spinach plastid chromosome. !$#accession S00458 !'##molecule_type DNA !'##residues 'IYKNSPILI',4-160 ##label HEI !'##cross-references EMBL:X07106 !'##note this sequence has been revised in reference S03021 REFERENCE S03021 !$#authors Westhoff, P.; Herrmann, R.G. !$#journal Eur. J. Biochem. (1988) 171:551-564 !$#title Complex RNA maturation in chloroplasts. !$#cross-references MUID:88151952; PMID:2831053 !$#accession S03022 !'##molecule_type DNA !'##residues 1-22 ##label WES2 REFERENCE A00161 !$#authors Widger, W.R.; Cramer, W.A.; Herrmann, R.G.; Trebst, A. !$#citation unpublished results, 1984, cited by Widger, W.R., Cramer, !1W.A., Herrmann, R.G., Trebst, A., Proc. Natl. Acad. Sci. !1U.S.A. 81, 674-678, 1984 !$#accession A00164 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 22-27,32-116,118-160 ##label WID COMMENT This polypeptide is an essential component of the cytochrome !1b6-f complex; its sequence is homologous with that of the !1carboxyl end of mitochondrial cytochrome b. GENETICS !$#gene petD !$#genome chloroplast !$#introns 3/2 CLASSIFICATION #superfamily plastoquinol-plastocyanin reductase 17K !1protein; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chloroplast; oxidoreductase; photosynthesis; thylakoid FEATURE !$24-144 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K SUMMARY #length 160 #molecular-weight 17445 #checksum 6148 SEQUENCE /// ENTRY S14962 #type complete TITLE plastoquinol-plastocyanin reductase (EC 1.10.99.1) 17K protein - wheat chloroplast ALTERNATE_NAMES cytochrome b6-f complex 17K protein; cytochrome b6-f complex chain IV ORGANISM #formal_name chloroplast Triticum aestivum #common_name common wheat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S14962; S05315 REFERENCE S14960 !$#authors Hird, S.M.; Wilson, R.J.; Dyer, T.A.; Gray, J.C. !$#journal Plant Mol. Biol. (1991) 16:745-747 !$#title Nucleotide sequence of the wheat chloroplast petB and petD !1genes encoding apocytochrome b-563 and subunit IV of the !1cytochrome bf complex. !$#cross-references MUID:91329710; PMID:1868207 !$#accession S14962 !'##molecule_type DNA !'##residues 1-160 ##label HIR !'##cross-references EMBL:X54751; NID:g12361; PIDN:CAA38552.1; !1PID:g12364 REFERENCE S05314 !$#authors Hird, S.M.; Dyer, T.A.; Gray, J.C. !$#journal Nucleic Acids Res. (1989) 17:6394 !$#title Nucleotide sequence of the rpoA gene in wheat chloroplast !1DNA. !$#cross-references MUID:89366674; PMID:2671938 !$#accession S05315 !'##molecule_type DNA !'##residues 149-160 ##label HI2 !'##cross-references EMBL:X15595; NID:g12371; PIDN:CAA33619.1; !1PID:g12373 GENETICS !$#gene petD !$#genome chloroplast !$#introns 3/2 CLASSIFICATION #superfamily plastoquinol-plastocyanin reductase 17K !1protein; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chloroplast; electron transfer; membrane-associated complex; !1oxidoreductase; photosynthesis; thylakoid FEATURE !$24-144 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K SUMMARY #length 160 #molecular-weight 17551 #checksum 7439 SEQUENCE /// ENTRY WMRZ17 #type complete TITLE plastoquinol-plastocyanin reductase (EC 1.10.99.1) 17K protein - rice chloroplast ALTERNATE_NAMES cytochrome b6-f complex 17K protein; cytochrome b6-f complex protein 4 ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 03-Jun-2002 ACCESSIONS JQ0257; S05137 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0257 !'##molecule_type DNA !'##residues 1-160 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05137 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-160 ##label HIR !'##cross-references EMBL:X15901; NID:g11957; PIDN:CAA33978.1; !1PID:g669083 !'##experimental_source cv. Nihonbare COMMENT This polypeptide of unknown function is one of the !1components of cytochrome b6-f complex; its sequence is !1homologous with that of carboxyl end of mitochondrial !1cytochrome b. GENETICS !$#gene petD !$#map_position CP72883-72890,73636-74110 !$#genome chloroplast !$#introns 3/2 CLASSIFICATION #superfamily plastoquinol-plastocyanin reductase 17K !1protein; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chloroplast; oxidoreductase; photosynthesis; thylakoid FEATURE !$24-144 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K SUMMARY #length 160 #molecular-weight 17503 #checksum 7285 SEQUENCE /// ENTRY WMNT17 #type complete TITLE plastoquinol-plastocyanin reductase (EC 1.10.99.1) 17K protein - common tobacco chloroplast ALTERNATE_NAMES cytochrome b6-f complex 17K protein; cytochrome b6-f complex protein 4 ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 03-Jun-2002 ACCESSIONS A00165 REFERENCE A00149 !$#authors Sugiura, M. !$#submission submitted to the EMBL Data Library, August 1986 !$#accession A00165 !'##molecule_type DNA !'##residues 1-139 ##label SUG !'##experimental_source cv. Bright Yellow 4 REFERENCE A38013 !$#authors Shinozaki, K.; Ohme, M.; Tanaka, M.; Wakasugi, T.; !1Hayashida, N.; Matsubayashi, T.; Zaita, N.; Chunwongse, J.; !1Obokata, J.; Yamaguchi-Shinozaki, K.; Ohto, C.; Torazawa, !1K.; Meng, B.Y.; Sugita, M.; Deno, H.; Kamogashira, T.; !1Yamada, K.; Kusuda, J.; Takaiwa, F.; Kato, A.; Tohdoh, N.; !1Shimada, H.; Sugiura, M. !$#journal EMBO J. (1986) 5:2043-2049 !$#title The complete nucleotide sequence of the tobacco chloroplast !1genome: its gene organization and expression. !$#contents annotation; gene organization, sites, features COMMENT This polypeptide of unknown function is one of the !1components of the cytochrome b6-f complex; its sequence is !1homologous with that of the carboxyl end of mitochondrial !1cytochrome b. GENETICS !$#gene petD !$#genome chloroplast CLASSIFICATION #superfamily plastoquinol-plastocyanin reductase 17K !1protein; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chloroplast; oxidoreductase; photosynthesis; thylakoid FEATURE !$3-123 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K SUMMARY #length 139 #molecular-weight 15225 #checksum 7198 SEQUENCE /// ENTRY S07297 #type complete TITLE plastoquinol-plastocyanin reductase (EC 1.10.99.1) 17K protein - garden pea chloroplast ALTERNATE_NAMES cytochrome b6-f complex 15.2K protein; cytochrome b6-f complex 17K protein; cytochrome b6-f complex protein 4 ORGANISM #formal_name chloroplast Pisum sativum #common_name garden pea DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S07297; S04385 REFERENCE S07297 !$#authors Phillips, A.L.; Gray, J.C. !$#journal Mol. Gen. Genet. (1984) 194:477-484 !$#title Location and nucleotide sequence of the gene for the 15.2 !1kDa polypeptide of the cytochrome b-f complex from pea !1chloroplasts. !$#accession S07297 !'##molecule_type DNA !'##residues 1-139 ##label PHI !'##cross-references EMBL:X00535; NID:g12150; PIDN:CAA25212.1; !1PID:g12151 REFERENCE S04382 !$#authors Purton, S.; Gray, J.C. !$#journal Mol. Gen. Genet. (1989) 217:77-84 !$#title The plastid rpoA gene encoding a protein homologous to the !1bacterial RNA polymerase alpha subunit is expressed in pea !1chloroplasts. !$#cross-references MUID:89364695; PMID:2671652 !$#accession S04385 !'##molecule_type DNA !'##residues 115-139 ##label PUR !'##cross-references EMBL:X15645; NID:g12178; PIDN:CAA33669.1; !1PID:g12181 GENETICS !$#gene petD !$#genome chloroplast CLASSIFICATION #superfamily plastoquinol-plastocyanin reductase 17K !1protein; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chloroplast; electron transfer; membrane-associated complex; !1oxidoreductase; photosynthesis; thylakoid; transmembrane !1protein FEATURE !$3-123 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K\ !$15-36 #domain transmembrane #status predicted #label TM1\ !$74-93 #domain transmembrane #status predicted #label TM2\ !$106-130 #domain transmembrane #status predicted #label TM3 SUMMARY #length 139 #molecular-weight 15267 #checksum 7278 SEQUENCE /// ENTRY WMKL17 #type complete TITLE plastoquinol-plastocyanin reductase (EC 1.10.99.1) 17K protein - Chlorella protothecoides chloroplast ALTERNATE_NAMES cytochrome b6-f complex 17K protein; cytochrome b6-f complex chain IV ORGANISM #formal_name chloroplast Chlorella protothecoides DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Jun-2002 ACCESSIONS S06160; S12478 REFERENCE S06159 !$#authors Reimann, A.; Kueck, U. !$#journal Plant Mol. Biol. (1989) 13:255-256 !$#title Nucleotide sequence of the plastid genes for apocytochrome b !1(6) (petB) and subunit IV of the cytochrome b(6)-f complex !1(petD) from the green alga Chlorella protothecoides: lack of !1introns. !$#cross-references MUID:92003673; PMID:2519117 !$#accession S06160 !'##molecule_type DNA !'##residues 1-160 ##label REI !'##cross-references EMBL:X15244 REFERENCE S12478 !$#authors Reimann, A. !$#submission submitted to the EMBL Data Library, May 1989 !$#accession S12478 !'##molecule_type DNA !'##residues 1-96,'G',98-160 ##label RE2 !'##cross-references EMBL:X15244; NID:g18092; PIDN:CAA33323.1; !1PID:g18094 GENETICS !$#gene petD !$#genome chloroplast CLASSIFICATION #superfamily plastoquinol-plastocyanin reductase 17K !1protein; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chloroplast; oxidoreductase; photosynthesis; thylakoid FEATURE !$24-144 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K SUMMARY #length 160 #molecular-weight 17474 #checksum 4147 SEQUENCE /// ENTRY S05340 #type complete TITLE plastoquinol-plastocyanin reductase (EC 1.10.99.1) 17K protein - green alga KS3/2 chloroplast ALTERNATE_NAMES cytochrome b6-f complex 17K protein; cytochrome b6-f complex chain IV ORGANISM #formal_name chloroplast Oocystaceae gen. sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S05340 REFERENCE S05340 !$#authors Kueck, U. !$#journal Mol. Gen. Genet. (1989) 218:257-265 !$#title The intron of a plastid gene from a green alga contains an !1open reading frame for a reverse transcriptase-like enzyme. !$#cross-references MUID:89384450; PMID:2476655 !$#accession S05340 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-160 ##label KUE GENETICS !$#gene petD !$#genome chloroplast CLASSIFICATION #superfamily plastoquinol-plastocyanin reductase 17K !1protein; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chloroplast; oxidoreductase; photosynthesis; thylakoid FEATURE !$24-144 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K SUMMARY #length 160 #molecular-weight 17575 #checksum 5589 SEQUENCE /// ENTRY S04089 #type complete TITLE plastoquinol-plastocyanin reductase (EC 1.10.99.1) 17K protein - Chlamydomonas eugametos chloroplast ALTERNATE_NAMES cytochrome b6-f complex 17K protein; cytochrome b6-f complex chain IV ORGANISM #formal_name chloroplast Chlamydomonas eugametos DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S04089 REFERENCE S04089 !$#authors Turmel, M.; Boulanger, J.; Bergeron, A. !$#journal Nucleic Acids Res. (1989) 17:3593 !$#title Nucleotide sequence of the chloroplast petD gene of !1Chlamydomonas eugametos. !$#cross-references MUID:89263804; PMID:2726496 !$#accession S04089 !'##molecule_type DNA !'##residues 1-160 ##label TUR !'##cross-references EMBL:X14503; NID:g11349; PIDN:CAA32656.1; !1PID:g11350 GENETICS !$#gene petD !$#genome chloroplast CLASSIFICATION #superfamily plastoquinol-plastocyanin reductase 17K !1protein; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chloroplast; oxidoreductase; photosynthesis; thylakoid FEATURE !$24-144 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K SUMMARY #length 160 #molecular-weight 17475 #checksum 3640 SEQUENCE /// ENTRY S16918 #type complete TITLE plastoquinol-plastocyanin reductase (EC 1.10.99.1) 17K protein - Chlamydomonas reinhardtii chloroplast ALTERNATE_NAMES cytochrome b6/f complex chain IV ORGANISM #formal_name chloroplast Chlamydomonas reinhardtii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S16918; S26837; S32589 REFERENCE S16916 !$#authors Bueschlen, S.; Choquet, Y.; Kuras, R.; Wollman, F.A. !$#journal FEBS Lett. (1991) 284:257-262 !$#title Nucleotide sequences of the continuous and separated petA, !1petB and petD chloroplast genes in Chlamydomonas !1reinhardtii. !$#cross-references MUID:91285146; PMID:2060646 !$#accession S16918 !'##molecule_type DNA !'##residues 1-160 ##label BUE !'##cross-references EMBL:X72919; NID:g1009385; PIDN:CAA51424.1; !1PID:g603532 REFERENCE S26837 !$#authors Yu, W.; Spreitzer, R.J. !$#journal Nucleic Acids Res. (1991) 19:957 !$#title Sequences of trnR-ACG and petD that contain a tRNA-like !1element within the chloroplast genome of Chlamydomonas !1reinhardtii. !$#cross-references MUID:91204459; PMID:2017378 !$#accession S26837 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-160 ##label YUW !'##cross-references EMBL:X56700; NID:g11461; PIDN:CAA40030.1; !1PID:g11462 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1990 GENETICS !$#gene petD !$#genome chloroplast CLASSIFICATION #superfamily plastoquinol-plastocyanin reductase 17K !1protein; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS chloroplast; membrane-associated complex; oxidoreductase; !1photosynthesis; thylakoid FEATURE !$24-144 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K SUMMARY #length 160 #molecular-weight 17442 #checksum 5862 SEQUENCE /// ENTRY B30807 #type complete TITLE plastoquinol-plastocyanin reductase (EC 1.10.99.1) 17K protein - Nostoc sp. ALTERNATE_NAMES cytochrome b6-f complex 17K protein; cytochrome b6-f complex protein 4 ORGANISM #formal_name Nostoc sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS B30807 REFERENCE A94683 !$#authors Kallas, T.; Spiller, S.; Malkin, R. !$#journal J. Biol. Chem. (1988) 263:14334-14342 !$#title Characterization of two operons encoding the cytochrome !1b-6-f complex of the cyanobacterium Nostoc PCC 7906. Highly !1conserved sequences but different gene organization than in !1chloroplasts. !$#cross-references MUID:89008280; PMID:2844767 !$#accession B30807 !'##molecule_type DNA !'##residues 1-160 ##label KAL !'##cross-references GB:J03967; NID:g145022; PIDN:AAA23331.1; !1PID:g145024 !'##experimental_source PCC 7906 CLASSIFICATION #superfamily plastoquinol-plastocyanin reductase 17K !1protein; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS oxidoreductase; photosynthesis; thylakoid FEATURE !$24-144 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K SUMMARY #length 160 #molecular-weight 17522 #checksum 4289 SEQUENCE /// ENTRY A61088 #type complete TITLE plastoquinol-plastocyanin reductase (EC 1.10.99.1) 17K protein - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES cytochrome b6-f complex chain IV; plastoquinol-plastocyanin reductase (EC 1.10.99.1) chain IV ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS A61088; S76298; S15474 REFERENCE A61088 !$#authors Osiewacz, H.D. !$#journal Arch. Microbiol. (1992) 157:336-342 !$#title Construction of insertion mutants of Synechocystis sp. PCC !16803: evidence for an essential function of subunit IV of !1the cytochrome b-6/f complex. !$#cross-references MUID:92272582; PMID:1590707 !$#accession A61088 !'##molecule_type DNA !'##residues 1-160 ##label OSI !'##cross-references EMBL:X58522; NID:g47376; PIDN:CAA41412.1; !1PID:g47377 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76298 !'##status preliminary !'##molecule_type DNA !'##residues 1-160 ##label KAN !'##cross-references EMBL:D64000; GB:AB001339; NID:g1001484; !1PIDN:BAA10150.1; PID:g1001523 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene petD CLASSIFICATION #superfamily plastoquinol-plastocyanin reductase 17K !1protein; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS oxidoreductase; photosynthesis; thylakoid FEATURE !$24-144 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K SUMMARY #length 160 #molecular-weight 17444 #checksum 7557 SEQUENCE /// ENTRY S26194 #type complete TITLE plastoquinol-plastocyanin reductase (EC 1.10.99.1) 17K protein - Synechococcus sp. (PCC 7002) ORGANISM #formal_name Synechococcus sp. #variety PCC 7002 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S26194; S18124 REFERENCE S26193 !$#authors Brand, S.N.; Tan, X.; Widger, W.R. !$#journal Plant Mol. Biol. (1992) 20:481-491 !$#title Cloning and sequencing of the petBD operon from the !1cyanobacterium Synechococcus sp. PCC 7002. !$#cross-references MUID:93043038; PMID:1421151 !$#accession S26194 !'##molecule_type DNA !'##residues 1-160 ##label BRA !'##cross-references EMBL:X63049; NID:g38962; PIDN:CAA44775.1; !1PID:g38964 GENETICS !$#gene petD CLASSIFICATION #superfamily plastoquinol-plastocyanin reductase 17K !1protein; plastoquinol-plastocyanin reductase 17K protein !1homology KEYWORDS oxidoreductase; thylakoid FEATURE !$24-144 #domain plastoquinol-plastocyanin reductase 17K !8protein homology #label 17K SUMMARY #length 160 #molecular-weight 17537 #checksum 9754 SEQUENCE /// ENTRY WMRZ4 #type complete TITLE plastoquinol-plastocyanin reductase (EC 1.10.99.1) chain V - rice chloroplast ALTERNATE_NAMES cytochrome b6-f complex protein 5 ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 03-Jun-2002 ACCESSIONS JQ0245; S05125 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0245 !'##molecule_type DNA !'##residues 1-37 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05125 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-37 ##label HIR !'##cross-references EMBL:X15901; NID:g11957; PIDN:CAA33967.1; !1PID:g12006 !'##experimental_source cv. Nihonbare GENETICS !$#gene petE !$#map_position CP63799-63912 !$#genome chloroplast CLASSIFICATION #superfamily cytochrome b6-f complex 4.2K protein KEYWORDS chloroplast; electron transfer; oxidoreductase; !1photosynthesis SUMMARY #length 37 #molecular-weight 4170 #checksum 3834 SEQUENCE /// ENTRY A32159 #type complete TITLE plastoquinol-plastocyanin reductase (EC 1.10.99.1) chain V - maize chloroplast ALTERNATE_NAMES cytochrome b6-f complex 4K protein; cytochrome b6-f complex chain 5 ORGANISM #formal_name chloroplast Zea mays #common_name maize DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS A32159; S58570 REFERENCE A32159 !$#authors Haley, J.; Bogorad, L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:1534-1538 !$#title A 4-kDa maize chloroplast polypeptide associated with the !1cytochrome b-6-f complex: subunit 5, encoded by the !1chloroplast petE gene. !$#cross-references MUID:89160811; PMID:2922397 !$#accession A32159 !'##status preliminary !'##molecule_type DNA !'##residues 1-37 ##label HAL !'##cross-references GB:J04502; NID:g342582; PIDN:AAA84480.1; !1PID:g342588 REFERENCE S58531 !$#authors Maier, R.M.; Neckermann, K.; Igloi, G.L.; Koessel, H. !$#journal J. Mol. Biol. (1995) 251:614-628 !$#title Complete sequence of the maize chloroplast genome: gene !1content, hotspots of divergence and fine tuning of genetic !1information by transcript editing. !$#cross-references MUID:95395841; PMID:7666415 !$#accession S58570 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-37 ##label MAI !'##cross-references EMBL:X86563; NID:g902200; PIDN:CAA60304.1; !1PID:g902240 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1995 GENETICS !$#genome chloroplast CLASSIFICATION #superfamily cytochrome b6-f complex 4.2K protein KEYWORDS chloroplast; electron transfer; membrane-associated complex; !1oxidoreductase; photosynthesis SUMMARY #length 37 #molecular-weight 4170 #checksum 3834 SEQUENCE /// ENTRY S20474 #type complete TITLE plastoquinol-plastocyanin reductase (EC 1.10.99.1) chain V - southern Asian dodder chloroplast ALTERNATE_NAMES cytochrome b6-f complex chain V ORGANISM #formal_name chloroplast Cuscuta reflexa #common_name southern Asian dodder DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S20474 REFERENCE S20474 !$#authors Haberhausen, G.; Valentin, K.; Zetsche, K. !$#journal Mol. Gen. Genet. (1992) 232:154-161 !$#title Organization and sequence of photosynthetic genes from the !1plastid genome of the holoparasitic flowering plant Cuscuta !1reflexa. !$#cross-references MUID:92204128; PMID:1552899 !$#accession S20474 !'##molecule_type DNA !'##residues 1-37 ##label HAB !'##cross-references EMBL:X61698; NID:g58330; PIDN:CAA43864.1; !1PID:g58331 GENETICS !$#gene petG !$#genome chloroplast CLASSIFICATION #superfamily cytochrome b6-f complex 4.2K protein KEYWORDS chloroplast; electron transfer; oxidoreductase; !1photosynthesis SUMMARY #length 37 #molecular-weight 4126 #checksum 4337 SEQUENCE /// ENTRY A05054 #type complete TITLE plastoquinol-plastocyanin reductase (EC 1.10.99.1) chain V - liverwort (Marchantia polymorpha) chloroplast ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S01541; A05054 REFERENCE S01529 !$#authors Fukuzawa, H.; Kohchi, T.; Sano, T.; Shirai, H.; Umesono, K.; !1Inokuchi, H.; Ozeki, H.; Ohyama, K. !$#journal J. Mol. Biol. (1988) 203:333-351 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. III. Gene organization of the large !1single copy region from rbcL to trnI(CAU). !$#cross-references MUID:89068687; PMID:3199436 !$#accession S01541 !'##molecule_type DNA !'##residues 1-37 ##label FUK !'##cross-references EMBL:X04465; NID:g11640; PIDN:CAA28104.1; !1PID:g11692 REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features GENETICS !$#genome chloroplast CLASSIFICATION #superfamily cytochrome b6-f complex 4.2K protein KEYWORDS chloroplast; oxidoreductase SUMMARY #length 37 #molecular-weight 4076 #checksum 4106 SEQUENCE /// ENTRY S51367 #type complete TITLE plastoquinol-plastocyanin reductase (EC 1.10.99.1) chain V - Chlamydomonas eugametos chloroplast ALTERNATE_NAMES cytochrome b6/f complex chain V ORGANISM #formal_name chloroplast Chlamydomonas eugametos DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S51367 REFERENCE S51365 !$#authors Turmel, M.; Otis, C. !$#journal Curr. Genet. (1994) 27:54-61 !$#title The chloroplast gene cluster containing psbF, psbL, petG and !1rps3 is conserved in Chlamydomonas. !$#cross-references MUID:95269309; PMID:7750147 !$#accession S51367 !'##molecule_type DNA !'##residues 1-37 ##label TUR !'##cross-references EMBL:L29282; NID:g575472; PIDN:AAA84158.1; !1PID:g575475 GENETICS !$#gene petG !$#genome chloroplast CLASSIFICATION #superfamily cytochrome b6-f complex 4.2K protein KEYWORDS chloroplast; electron transfer; membrane-associated complex; !1oxidoreductase; photosynthesis; thylakoid SUMMARY #length 37 #molecular-weight 3995 #checksum 4092 SEQUENCE /// ENTRY S26880 #type complete TITLE plastoquinol-plastocyanin reductase (EC 1.10.99.1) chain V - Chlamydomonas reinhardtii chloroplast ALTERNATE_NAMES cytochrome b6-f complex 4K protein ORGANISM #formal_name chloroplast Chlamydomonas reinhardtii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S26880; T08172 REFERENCE S26878 !$#authors Fong, S.E.; Surzycki, S.J. !$#journal Curr. Genet. (1992) 21:527-530 !$#title Organization and structure of plastome psbF, psbL, petG and !1ORF712 genes in Chlamydomonas reinhardtii. !$#cross-references MUID:92315354; PMID:1617741 !$#accession S26880 !'##molecule_type DNA !'##residues 1-37 ##label FON !'##cross-references EMBL:X66250; NID:g393459; PIDN:CAA46979.1; !1PID:g393462 GENETICS !$#gene petG !$#genome chloroplast CLASSIFICATION #superfamily cytochrome b6-f complex 4.2K protein KEYWORDS chloroplast; electron transfer; membrane-associated complex; !1oxidoreductase; photosynthesis; thylakoid SUMMARY #length 37 #molecular-weight 3984 #checksum 4503 SEQUENCE /// ENTRY S06916 #type complete TITLE plastoquinol-plastocyanin reductase (EC 1.10.99.1) chain V - Cyanophora paradoxa cyanelle ALTERNATE_NAMES cytochrome b6-f complex 4K protein ORGANISM #formal_name cyanelle Cyanophora paradoxa DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S06916; T06908 REFERENCE S06916 !$#authors Stirewalt, V.L.; Bryant, D.A. !$#journal Nucleic Acids Res. (1989) 17:10095 !$#title Molecular cloning and nucleotide sequence of the petG gene !1of the cyanelle genome of Cyanophora paradoxa. !$#cross-references MUID:90098772; PMID:2513551 !$#accession S06916 !'##molecule_type DNA !'##residues 1-37 ##label STI !'##cross-references EMBL:X16974; NID:g12548; PIDN:CAA34846.1; !1PID:g12549 REFERENCE Z15840 !$#authors Stirewalt, V.L.; Michalowski, C.B.; Luffelhardt, W.; !1Bohnert, H.J.; Bryant, D.A. !$#submission submitted to the EMBL Data Library, July 1995 !$#description Nucleotide sequence of the cyanelle genome from Cyanophora !1paradoxa. !$#accession T06908 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-37 ##label ST2 !'##cross-references EMBL:U30821; NID:g1016083; PIDN:AAA81251.1; !1PID:g1016164 !'##experimental_source strain Pringsheim LB555 GENETICS !$#gene petG !$#map_position 65 !$#genome cyanelle CLASSIFICATION #superfamily cytochrome b6-f complex 4.2K protein KEYWORDS cyanelle; electron transfer; membrane-associated complex; !1oxidoreductase; photosynthesis SUMMARY #length 37 #molecular-weight 4139 #checksum 3795 SEQUENCE /// ENTRY S26087 #type complete TITLE plastoquinol-plastocyanin reductase (EC 1.10.99.1) chain V - Euglena gracilis chloroplast ALTERNATE_NAMES cytochrome b6-f complex chain V ORGANISM #formal_name chloroplast Euglena gracilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S26087; S34880; S34513 REFERENCE S26086 !$#authors Hallick, R.B. !$#submission submitted to the EMBL Data Library, March 1992 !$#accession S26087 !'##molecule_type DNA !'##residues 1-37 ##label HAL !'##cross-references EMBL:Z11874; NID:g14353; PIDN:CAA77909.1; !1PID:g14359 !'##experimental_source strain Z REFERENCE S34862 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.R.; !1Monfort, A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#journal Nucleic Acids Res. (1993) 21:3537-3544 !$#title Complete sequence of Euglena gracilis chloroplast DNA. !$#cross-references MUID:93347989; PMID:8346031 !$#accession S34880 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-37 ##label HAL2 !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50092.1; !1PID:g415748 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1993 GENETICS !$#gene petG !$#genome chloroplast !$#introns 5/3 CLASSIFICATION #superfamily cytochrome b6-f complex 4.2K protein KEYWORDS chloroplast; membrane-associated complex; oxidoreductase; !1photosynthesis; thylakoid SUMMARY #length 37 #molecular-weight 4147 #checksum 4488 SEQUENCE /// ENTRY CBBOC6 #type complete TITLE cytochrome b-c1 complex 6.4K protein - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 13-Jun-1997 ACCESSIONS A24096 REFERENCE A24096 !$#authors Schagger, H.; Borchart, U.; Aquila, H.; Link, T.A.; von !1Jagow, G. !$#journal FEBS Lett. (1985) 190:89-94 !$#title Isolation and amino acid sequence of the smallest subunit of !1beef heart b-c1 complex. !$#cross-references MUID:86005499; PMID:2995132 !$#accession A24096 !'##molecule_type protein !'##residues 1-56 ##label SCH COMMENT This protein is the smallest of the 11 polypeptide chains of !1the cytochrome b-c1 complex; it may be closely linked to the !1iron-sulfur protein in the complex and function as an !1iron-sulfur protein binding factor. CLASSIFICATION #superfamily cytochrome b-c1 6.4K protein KEYWORDS membrane protein FEATURE !$16-36 #domain transmembrane #status predicted #label TRM SUMMARY #length 56 #molecular-weight 6362 #checksum 2164 SEQUENCE /// ENTRY CBNT55 #type complete TITLE cytochrome b559 component psbE - common tobacco chloroplast ALTERNATE_NAMES cytochrome b559 9K component; cytochrome b559 alpha chain ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 03-Mar-2000 ACCESSIONS S55791; B25714 REFERENCE S55789 !$#authors Carrillo, N.; Seyer, P.; Tyagi, A.; Herrmann, R.G. !$#journal Curr. Genet. (1986) 10:619-624 !$#title Cytochrome b-559 genes from Oenothera hookeri and Nicotiana !1tabacum show a remarkably high degree of conservation as !1compared to spinach. !$#cross-references MUID:88165110; PMID:2450682 !$#accession S55791 !'##molecule_type DNA !'##residues 1-83 ##label CAR !'##cross-references EMBL:X03781; NID:g11794; PIDN:CAA27412.1; !1PID:g11795 REFERENCE A00149 !$#authors Sugiura, M. !$#submission submitted to the EMBL Data Library, August 1986 !$#accession B25714 !'##molecule_type DNA !'##residues 1-83 ##label SUG !'##experimental_source cv. Bright Yellow 4 REFERENCE A38013 !$#authors Shinozaki, K.; Ohme, M.; Tanaka, M.; Wakasugi, T.; !1Hayashida, N.; Matsubayashi, T.; Zaita, N.; Chunwongse, J.; !1Obokata, J.; Yamaguchi-Shinozaki, K.; Ohto, C.; Torazawa, !1K.; Meng, B.Y.; Sugita, M.; Deno, H.; Kamogashira, T.; !1Yamada, K.; Kusuda, J.; Takaiwa, F.; Kato, A.; Tohdoh, N.; !1Shimada, H.; Sugiura, M. !$#journal EMBO J. (1986) 5:2043-2049 !$#title The complete nucleotide sequence of the tobacco chloroplast !1genome: its gene organization and expression. !$#contents annotation; gene organization, sites, features GENETICS !$#gene psbE !$#genome chloroplast COMPLEX heterodimer of alpha (psbE) and beta (psbF, see PIR:F2NT4) !1chains FUNCTION !$#description tightly associated with the reaction center of photosystem !1II; may be part of the water-oxidation complex !$#pathway photosystem II CLASSIFICATION #superfamily cytochrome b559 component E KEYWORDS chloroplast; chromoprotein; electron transfer; heme; !1heterodimer; iron; membrane-associated complex; !1metalloprotein; photosynthesis; photosystem II; thylakoid; !1transmembrane protein FEATURE !$2-83 #product cytochrome b559 component psbE #status !8predicted #label MAT\ !$19-43 #domain transmembrane #status predicted #label TMM\ !$44-83 #domain thylakoid lumenal #status predicted #label !8THL\ !$23 #binding_site heme iron (His) (axial ligand) (shared !8with beta chain) #status predicted SUMMARY #length 83 #molecular-weight 9396 #checksum 4628 SEQUENCE /// ENTRY S00418 #type complete TITLE cytochrome b559 component psbE - spinach chloroplast ALTERNATE_NAMES cytochrome b559 9K component; cytochrome b559 alpha chain ORGANISM #formal_name chloroplast Spinacia oleracea #common_name spinach DATE 30-Sep-1989 #sequence_revision 19-Jul-1996 #text_change 03-Mar-2000 ACCESSIONS S00418; A22550 REFERENCE S00418 !$#authors Herrmann, R.G.; Alt, J.; Schiller, B.; Widger, W.R.; Cramer, !1W.A. !$#journal FEBS Lett. (1984) 176:239-244 !$#title Nucleotide sequence of the gene for apocytochrome b-559 on !1the spinach plastid chromosome: implications for the !1structure of the membrane protein. !$#accession S00418 !'##molecule_type DNA !'##residues 1-83 ##label HER !'##cross-references EMBL:M35673; NID:g343357; PIDN:AAA84628.1; !1PID:g343358 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE A22550 !$#authors Widger, W.R.; Cramer, W.A.; Hermodson, M.; Meyer, D.; !1Gullifor, M. !$#journal J. Biol. Chem. (1984) 259:3870-3876 !$#title Purification and partial amino acid sequence of the !1chloroplast cytochrome b-559. !$#cross-references MUID:84162067; PMID:6706983 !$#accession A22550 !'##molecule_type protein !'##residues 2-22,'X',24-28 ##label WID GENETICS !$#gene psbE !$#genome chloroplast COMPLEX heterodimer of alpha (psbE) and beta (psbF, see PIR:S35262) !1chains; tightly associated with the reaction center of !1photosystem II FUNCTION !$#description may be part of the water-oxidation complex of photosystem II !$#pathway photosystem II CLASSIFICATION #superfamily cytochrome b559 component E KEYWORDS chloroplast; chromoprotein; electron transfer; heme; !1heterodimer; iron; membrane-associated complex; !1metalloprotein; photosynthesis; photosystem II; thylakoid; !1transmembrane protein FEATURE !$2-83 #product cytochrome b559 component psbE #status !8predicted #label MAT\ !$19-43 #domain transmembrane #status predicted #label TMM\ !$44-83 #domain thylakoid lumenal #status predicted #label !8THL\ !$23 #binding_site heme iron (His) (axial ligand) (shared !8with beta chain) #status predicted SUMMARY #length 83 #molecular-weight 9386 #checksum 4673 SEQUENCE /// ENTRY CBRZ55 #type complete TITLE cytochrome b559 component psbE - rice chloroplast ALTERNATE_NAMES cytochrome b559 9K component; cytochrome b559 alpha chain ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 03-Mar-2000 ACCESSIONS JQ0243; S05123 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0243 !'##molecule_type DNA !'##residues 1-83 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05123 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-83 ##label HIR !'##cross-references EMBL:X15901; NID:g11957; PIDN:CAA33965.1; !1PID:g12004 !'##experimental_source cv. Nihonbare !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1989 GENETICS !$#gene psbE !$#genome chloroplast COMPLEX heterodimer of alpha (psbE) and beta (psbF, see PIR:F2RZ4) !1chains; tightly associated with the reaction center of !1photosystem II FUNCTION !$#description may be part of the water-oxidation complex of photosystem II !$#pathway photosystem II CLASSIFICATION #superfamily cytochrome b559 component E KEYWORDS chloroplast; chromoprotein; electron transfer; heme; !1heterodimer; iron; membrane-associated complex; !1metalloprotein; photosynthesis; photosystem II; thylakoid; !1transmembrane protein FEATURE !$2-83 #product cytochrome b559 component psbE #status !8predicted #label MAT\ !$19-43 #domain transmembrane #status predicted #label TMM\ !$44-83 #domain thylakoid lumenal #status predicted #label !8THL\ !$23 #binding_site heme iron (His) (axial ligand) (shared !8with beta chain) #status predicted SUMMARY #length 83 #molecular-weight 9444 #checksum 4640 SEQUENCE /// ENTRY CBWT5E #type complete TITLE cytochrome b559 component psbE - wheat chloroplast ALTERNATE_NAMES cytochrome b559 9K component; cytochrome b559 alpha chain ORGANISM #formal_name chloroplast Triticum aestivum #common_name common wheat DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 03-Mar-2000 ACCESSIONS S03621; PW0015; A26015 REFERENCE JG0010 !$#authors Webber, A.N.; Hird, S.M.; Packman, L.C.; Dyer, T.A.; Gray, !1J.C. !$#journal Plant Mol. Biol. (1989) 12:141-151 !$#title A photosystem II polypeptide is encoded by an open reading !1frame cotranscribed with genes for cytochrome b-559 in wheat !1chloroplast DNA. !$#accession S03621 !'##molecule_type DNA !'##residues 1-83 ##label WEB !'##cross-references EMBL:X15225; NID:g14259; PIDN:CAA33294.1; !1PID:g14260 !$#accession PW0015 !'##molecule_type protein !'##residues 2-7,'X',9-16 ##label WEB2 REFERENCE A26015 !$#authors Hird, S.M.; Willey, D.L.; Dyer, T.A.; Gray, J.C. !$#journal Mol. Gen. Genet. (1986) 203:95-100 !$#title Location and nucleotide sequence of the gene for cytochrome !1b-559 in wheat chloroplast DNA. !$#accession A26015 !'##molecule_type DNA !'##residues 1-83 ##label HIR !'##cross-references EMBL:X03776; NID:g12338; PIDN:CAA27405.1; !1PID:g12339 GENETICS !$#gene psbE !$#genome chloroplast COMPLEX heterodimer of alpha (psbE) and beta (psbF, see PIR:F2KT5F) !1chains; tightly associated with the reaction center of !1photosystem II FUNCTION !$#description may be part of the water-oxidation complex of photosystem II !$#pathway photosystem II CLASSIFICATION #superfamily cytochrome b559 component E KEYWORDS chloroplast; chromoprotein; electron transfer; heme; !1heterodimer; iron; membrane-associated complex; !1metalloprotein; photosynthesis; photosystem II; thylakoid; !1transmembrane protein FEATURE !$2-83 #product cytochrome b559 component psbE #status !8experimental #label MAT\ !$19-43 #domain transmembrane #status predicted #label TMM\ !$44-83 #domain thylakoid lumenal #status predicted #label !8THL\ !$23 #binding_site heme iron (His) (axial ligand) (shared !8with beta chain) #status predicted SUMMARY #length 83 #molecular-weight 9444 #checksum 4640 SEQUENCE /// ENTRY A29956 #type complete TITLE cytochrome b559 component psbE - barley chloroplast ALTERNATE_NAMES cytochrome b559 9K component; cytochrome b559 alpha chain ORGANISM #formal_name chloroplast Hordeum vulgare #common_name barley DATE 15-Dec-1988 #sequence_revision 19-Jul-1996 #text_change 03-Mar-2000 ACCESSIONS A29956; A31182; JN0350; S04062 REFERENCE A29956 !$#authors Krupinska, K.; Berry-Lowe, S. !$#journal Carlsberg Res. Commun. (1988) 53:43-55 !$#title Characterization and in vitro expression of the cytochrome !1b-559 genes of barley I. localization and sequence of the !1genes. !$#cross-references MUID:89374539; PMID:3256307 !$#accession A29956 !'##molecule_type DNA !'##residues 1-83 ##label KR2 !'##cross-references GB:M35977; NID:g336408; PIDN:AAA84044.1; !1PID:g336409 REFERENCE A90772 !$#authors Krupinska, K. !$#journal Carlsberg Res. Commun. (1988) 53:233-246 !$#title Characterization and in vitro expression of the cytochrome !1b-559 genes of barley. II. In vitro transcription and !1translation. !$#cross-references MUID:89351277; PMID:3255312 !$#accession A31182 !'##molecule_type DNA !'##residues 1-83 ##label KRU !'##cross-references GB:M35616; NID:g336415; PIDN:AAA84048.1; !1PID:g336416 REFERENCE JN0345 !$#authors Efimov, V.A.; Andreeva, A.V.; Reverdatto, S.V.; !1Chakhmakhcheva, O.G. !$#journal Bioorg. Khim. (1991) 17:1369-1385 !$#title Nucleotide sequence of the barley chloroplast psbB, psbC, !1psbE, psbF, psbH gene coding for the polypeptides of !1photosystem II. !$#cross-references MUID:92207253; PMID:1804121 !$#accession JN0350 !'##molecule_type DNA !'##residues 1-83 ##label EFI !'##note article in Russian with English abstract REFERENCE S04062 !$#authors Chakhmakhcheva, O.G.; Andreeva, A.V.; Buryakova, A.A.; !1Reverdatto, S.V.; Efimov, V.A. !$#journal Nucleic Acids Res. (1989) 17:2858 !$#title Nucleotide sequence of the barley chloroplast psbE, psbF !1genes and flanking regions. !$#cross-references MUID:89240046; PMID:2654886 !$#accession S04062 !'##molecule_type DNA !'##residues 1-15,'C',17-22,'R',24-83 ##label CHA !'##cross-references EMBL:X14108; NID:g12351; PIDN:CAA32270.1; !1PID:g12352 GENETICS !$#gene psbE !$#genome chloroplast COMPLEX heterodimer of alpha (psbE) and beta (psbF, see PIR:S04063) !1chains; tightly associated with the reaction center of !1photosystem II FUNCTION !$#description may be part of the water-oxidation complex of photosystem II !$#pathway photosystem II CLASSIFICATION #superfamily cytochrome b559 component E KEYWORDS chloroplast; chromoprotein; electron transfer; heme; !1heterodimer; iron; membrane-associated complex; !1metalloprotein; photosynthesis; photosystem II; thylakoid; !1transmembrane protein FEATURE !$2-83 #product cytochrome b559 component psbE #status !8predicted #label MAT\ !$19-43 #domain transmembrane #status predicted #label TMM\ !$44-83 #domain thylakoid lumenal #status predicted #label !8THL\ !$23 #binding_site heme iron (His) (axial ligand) (shared !8with beta chain) #status predicted SUMMARY #length 83 #molecular-weight 9444 #checksum 4640 SEQUENCE /// ENTRY S03191 #type complete TITLE cytochrome b559 component psbE - rye chloroplast ALTERNATE_NAMES cytochrome b559 9K component; cytochrome b559 alpha chain ORGANISM #formal_name chloroplast Secale cereale #common_name rye DATE 07-Jun-1990 #sequence_revision 19-Jul-1996 #text_change 03-Mar-2000 ACCESSIONS S03191 REFERENCE S03191 !$#authors Kolosov, V.L.; Klezovich, O.N.; Zolotarev, A.S. !$#journal Nucleic Acids Res. (1989) 17:1760 !$#title Nucleotide sequence of the rye chloroplast DNA fragment, !1comprising psbE and psbF genes. !$#cross-references MUID:89160331; PMID:2646599 !$#accession S03191 !'##molecule_type DNA !'##residues 1-83 ##label KOL !'##cross-references EMBL:X13326; NID:g12230; PIDN:CAA31698.1; !1PID:g12231 !'##note the authors translated the codon CCT for residue 28 as Leu GENETICS !$#gene psbE !$#genome chloroplast COMPLEX heterodimer of alpha (psbE) and beta (psbF, see PIR:S03192) !1chains; tightly associated with the reaction center of !1photosystem II FUNCTION !$#description may be part of the water-oxidation complex of photosystem II !$#pathway photosystem II CLASSIFICATION #superfamily cytochrome b559 component E KEYWORDS chloroplast; chromoprotein; electron transfer; heme; !1heterodimer; iron; membrane-associated complex; !1metalloprotein; photosynthesis; photosystem II; thylakoid; !1transmembrane protein FEATURE !$2-83 #product cytochrome b559 component psbE #status !8predicted #label MAT\ !$19-43 #domain transmembrane #status predicted #label TMM\ !$44-83 #domain thylakoid lumenal #status predicted #label !8THL\ !$23 #binding_site heme iron (His) (axial ligand) (shared !8with beta chain) #status predicted SUMMARY #length 83 #molecular-weight 9444 #checksum 4640 SEQUENCE /// ENTRY S58568 #type complete TITLE cytochrome b559 component psbE - maize chloroplast ALTERNATE_NAMES cytochrome b559 9K component; cytochrome b559 alpha chain ORGANISM #formal_name chloroplast Zea mays #common_name maize DATE 29-Nov-1995 #sequence_revision 19-Jul-1996 #text_change 03-Mar-2000 ACCESSIONS S58568 REFERENCE S58531 !$#authors Maier, R.M.; Neckermann, K.; Igloi, G.L.; Koessel, H. !$#journal J. Mol. Biol. (1995) 251:614-628 !$#title Complete sequence of the maize chloroplast genome: gene !1content, hotspots of divergence and fine tuning of genetic !1information by transcript editing. !$#cross-references MUID:95395841; PMID:7666415 !$#accession S58568 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-83 ##label MAI !'##cross-references EMBL:X86563; NID:g902200; PIDN:CAA60302.1; !1PID:g902238 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1995 GENETICS !$#gene psbE !$#genome chloroplast COMPLEX heterodimer of alpha (psbE) and beta (psbF, see PIR:S58567) !1chains; tightly associated with the reaction center of !1photosystem II FUNCTION !$#description may be part of the water-oxidation complex of photosystem II !$#pathway photosystem II CLASSIFICATION #superfamily cytochrome b559 component E KEYWORDS chloroplast; chromoprotein; electron transfer; heme; !1heterodimer; iron; membrane-associated complex; !1metalloprotein; photosynthesis; photosystem II; thylakoid; !1transmembrane protein FEATURE !$2-83 #product cytochrome b559 component psbE #status !8predicted #label MAT\ !$19-43 #domain transmembrane #status predicted #label TMM\ !$44-83 #domain thylakoid lumenal #status predicted #label !8THL\ !$23 #binding_site heme iron (His) (axial ligand) (shared !8with beta chain) #status predicted SUMMARY #length 83 #molecular-weight 9444 #checksum 4640 SEQUENCE /// ENTRY A48310 #type complete TITLE cytochrome b559 component psbE - garden pea chloroplast ALTERNATE_NAMES cytochrome b559 9K component; cytochrome b559 alpha chain ORGANISM #formal_name chloroplast Pisum sativum #common_name garden pea DATE 31-Dec-1993 #sequence_revision 19-Jul-1996 #text_change 03-Mar-2000 ACCESSIONS A48310 REFERENCE A48310 !$#authors Willey, D.L.; Gray, J.C. !$#journal Curr. Genet. (1989) 15:213-220 !$#title Two small open reading frames are co-transcribed with the !1pea chloroplast genes for the polypeptides of cytochrome !1b-559. !$#cross-references MUID:89354671; PMID:2766383 !$#accession A48310 !'##molecule_type DNA !'##residues 1-83 ##label WIL !'##cross-references GB:X15767; NID:g12152; PIDN:CAA33772.1; PID:g12153 GENETICS !$#genome chloroplast COMPLEX heterodimer of alpha (psbE) and beta (psbF, see PIR:B48310) !1chains; tightly associated with the reaction center of !1photosystem II FUNCTION !$#description may be part of the water-oxidation complex of photosystem II !$#pathway photosystem II CLASSIFICATION #superfamily cytochrome b559 component E KEYWORDS chloroplast; chromoprotein; electron transfer; heme; !1heterodimer; iron; membrane-associated complex; !1metalloprotein; photosynthesis; photosystem II; thylakoid; !1transmembrane protein FEATURE !$2-83 #product cytochrome b559 component psbE #status !8predicted #label MAT\ !$19-43 #domain transmembrane #status predicted #label TMM\ !$44-83 #domain thylakoid lumenal #status predicted #label !8THL\ !$23 #binding_site heme iron (His) (axial ligand) (shared !8with beta chain) #status predicted SUMMARY #length 83 #molecular-weight 9414 #checksum 4402 SEQUENCE /// ENTRY S55789 #type complete TITLE cytochrome b559 component psbE - Hooker's evening primrose chloroplast ALTERNATE_NAMES cytochrome b559 9K component; cytochrome b559 alpha chain ORGANISM #formal_name chloroplast Oenothera hookeri subsp. hookeri #common_name Hooker's evening primrose DATE 27-Oct-1995 #sequence_revision 19-Jul-1996 #text_change 03-Mar-2000 ACCESSIONS S55789 REFERENCE S55789 !$#authors Carrillo, N.; Seyer, P.; Tyagi, A.; Herrmann, R.G. !$#journal Curr. Genet. (1986) 10:619-624 !$#title Cytochrome b-559 genes from Oenothera hookeri and Nicotiana !1tabacum show a remarkably high degree of conservation as !1compared to spinach. !$#cross-references MUID:88165110; PMID:2450682 !$#accession S55789 !'##molecule_type DNA !'##residues 1-83 ##label CAR !'##cross-references EMBL:X03780; NID:g11923; PIDN:CAA27410.1; !1PID:g11924 GENETICS !$#gene psbE !$#genome chloroplast COMPLEX heterodimer of alpha (psbE) and beta (psbF, see PIR:S55790) !1chains; tightly associated with the reaction center of !1photosystem II FUNCTION !$#description may be part of the water-oxidation complex of photosystem II !$#pathway photosystem II CLASSIFICATION #superfamily cytochrome b559 component E KEYWORDS chloroplast; chromoprotein; electron transfer; heme; !1heterodimer; iron; membrane-associated complex; !1metalloprotein; photosynthesis; photosystem II; thylakoid; !1transmembrane protein FEATURE !$2-83 #product cytochrome b559 component psbE #status !8predicted #label MAT\ !$19-43 #domain transmembrane #status predicted #label TMM\ !$44-83 #domain thylakoid lumenal #status predicted #label !8THL\ !$23 #binding_site heme iron (His) (axial ligand) (shared !8with beta chain) #status predicted SUMMARY #length 83 #molecular-weight 9314 #checksum 4687 SEQUENCE /// ENTRY S01243 #type complete TITLE cytochrome b559 component psbE - evening primrose chloroplast ALTERNATE_NAMES cytochrome b559 9K component; cytochrome b559 alpha chain ORGANISM #formal_name chloroplast Oenothera villaricae #common_name evening primrose DATE 30-Jun-1989 #sequence_revision 19-Jul-1996 #text_change 03-Mar-2000 ACCESSIONS S01243 REFERENCE S01243 !$#authors Schuster, W.; Brennicke, A. !$#journal Nucleic Acids Res. (1988) 16:7728 !$#title A plastid fragment from the psbE-psbF coding region in the !1mitochondrial genome of Oenothera berteriana. !$#cross-references MUID:88319966; PMID:3045763 !$#accession S01243 !'##molecule_type DNA !'##residues 1-83 ##label SCH !'##cross-references EMBL:X07951; NID:g11913; PIDN:CAA30776.1; !1PID:g11914 GENETICS !$#gene psbE !$#genome chloroplast COMPLEX heterodimer of alpha (psbE) and beta (psbF, see PIR:S01244) !1chains; tightly associated with the reaction center of !1photosystem II FUNCTION !$#description may be part of the water-oxidation complex of photosystem II !$#pathway photosystem II CLASSIFICATION #superfamily cytochrome b559 component E KEYWORDS chloroplast; chromoprotein; electron transfer; heme; !1heterodimer; iron; membrane-associated complex; !1metalloprotein; photosynthesis; photosystem II; thylakoid; !1transmembrane protein FEATURE !$2-83 #product cytochrome b559 component psbE #status !8predicted #label MAT\ !$19-43 #domain transmembrane #status predicted #label TMM\ !$44-83 #domain thylakoid lumenal #status predicted #label !8THL\ !$23 #binding_site heme iron (His) (axial ligand) (shared !8with beta chain) #status predicted SUMMARY #length 83 #molecular-weight 9314 #checksum 4687 SEQUENCE /// ENTRY CBLV55 #type complete TITLE cytochrome b559 component psbE - liverwort (Marchantia polymorpha) chloroplast ALTERNATE_NAMES cytochrome b559 9K component; cytochrome b559 alpha chain ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 03-Mar-2000 ACCESSIONS S01536; B25809 REFERENCE S01529 !$#authors Fukuzawa, H.; Kohchi, T.; Sano, T.; Shirai, H.; Umesono, K.; !1Inokuchi, H.; Ozeki, H.; Ohyama, K. !$#journal J. Mol. Biol. (1988) 203:333-351 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. III. Gene organization of the large !1single copy region from rbcL to trnI(CAU). !$#cross-references MUID:89068687; PMID:3199436 !$#accession S01536 !'##molecule_type DNA !'##residues 1-83 ##label FUK !'##cross-references EMBL:X04465; NID:g11640; PIDN:CAA28101.1; !1PID:g11689 REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features GENETICS !$#gene psbE !$#genome chloroplast COMPLEX heterodimer of alpha (psbE) and beta (psbF, see PIR:F2LV4) !1chains; tightly associated with the reaction center of !1photosystem II FUNCTION !$#description may be part of the water-oxidation complex of photosystem II !$#pathway photosystem II CLASSIFICATION #superfamily cytochrome b559 component E KEYWORDS chloroplast; chromoprotein; electron transfer; heme; !1heterodimer; iron; membrane-associated complex; !1metalloprotein; photosynthesis; photosystem II; thylakoid; !1transmembrane protein FEATURE !$2-83 #product cytochrome b559 component psbE #status !8predicted #label MAT\ !$19-43 #domain transmembrane #status predicted #label TMM\ !$44-83 #domain thylakoid lumenal #status predicted #label !8THL\ !$23 #binding_site heme iron (His) (axial ligand) (shared !8with beta chain) #status predicted SUMMARY #length 83 #molecular-weight 9494 #checksum 4622 SEQUENCE /// ENTRY S53882 #type complete TITLE cytochrome b559 component psbE - Chlamydomonas reinhardtii chloroplast ALTERNATE_NAMES cytochrome b559 9K component; cytochrome b559 alpha chain ORGANISM #formal_name chloroplast Chlamydomonas reinhardtii DATE 27-Oct-1995 #sequence_revision 19-Jul-1996 #text_change 03-Mar-2000 ACCESSIONS S53882; B41170 REFERENCE S53882 !$#authors Mor, T.S.; Ohad, I.; Hirschberg, J.; Pakrasi, H.B. !$#journal Mol. Gen. Genet. (1995) 246:600-604 !$#title An unusual organization of the genes encoding cytochrome b !1(559) in Chlamydomonas reinhardtii: psbE and psbF genes are !1separately transcribed from different regions of the plastid !1chromosome. !$#cross-references MUID:95214620; PMID:7700232 !$#accession S53882 !'##molecule_type DNA !'##residues 1-82 ##label MOR !'##cross-references EMBL:X79565; NID:g1052575; PIDN:CAA56102.1; !1PID:g1052576 REFERENCE A41170 !$#authors de Vitry, C.; Diner, B.A.; Popot, J.L. !$#journal J. Biol. Chem. (1991) 266:16614-16621 !$#title Photosystem II particles from Chlamydomonas reinhardtii. !1Purification, molecular weight, small subunit composition, !1and protein phosphorylation. !$#cross-references MUID:91358452; PMID:1885590 !$#accession B41170 !'##molecule_type protein !'##residues 2-13 ##label DE3 GENETICS !$#gene psbE !$#genome chloroplast COMPLEX heterodimer of alpha (psbE) and beta (psbF, see PIR:S53883) !1chains; tightly associated with the reaction center of !1photosystem II FUNCTION !$#description may be part of the water-oxidation complex of photosystem II !$#pathway photosystem II CLASSIFICATION #superfamily cytochrome b559 component E KEYWORDS chloroplast; chromoprotein; electron transfer; heme; !1heterodimer; iron; membrane-associated complex; !1metalloprotein; photosynthesis; photosystem II; thylakoid; !1transmembrane protein FEATURE !$2-82 #product cytochrome b559 component psbE #status !8experimental #label MAT\ !$19-43 #domain transmembrane #status predicted #label TMM\ !$44-82 #domain thylakoid lumenal #status predicted #label !8THL\ !$23 #binding_site heme iron (His) (axial ligand) (shared !8with beta chain) #status predicted SUMMARY #length 82 #molecular-weight 9304 #checksum 2894 SEQUENCE /// ENTRY S00689 #type complete TITLE cytochrome b559 component psbE - Euglena gracilis chloroplast ALTERNATE_NAMES cytochrome b559 9K component; cytochrome b559 alpha chain ORGANISM #formal_name chloroplast Euglena gracilis DATE 30-Jun-1989 #sequence_revision 19-Jul-1996 #text_change 03-Mar-2000 ACCESSIONS S00689; S34516; S34883 REFERENCE S00689 !$#authors Cushman, J.C.; Christopher, D.A.; Little, M.C.; Hallick, !1R.B.; Price, C.A. !$#journal Curr. Genet. (1988) 13:173-180 !$#title Organization of the psbE, psbF, orf38, and orf42 gene loci !1on the Euglena gracilis chloroplast genome. !$#cross-references MUID:88223485; PMID:3131027 !$#accession S00689 !'##molecule_type DNA !'##residues 1-81 ##label CUS !'##cross-references EMBL:X07073; NID:g11492; PIDN:CAA30108.1; !1PID:g11493 REFERENCE S34494 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.; Monfort, !1A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#submission submitted to the EMBL Data Library, January 1993 !$#description The complete sequence of the Euglena gracilis chloroplast !1genome (tentative). !$#accession S34516 !'##molecule_type DNA !'##residues 1-81 ##label HAL1 !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50095.1; !1PID:g415751 REFERENCE S34862 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.R.; !1Monfort, A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#journal Nucleic Acids Res. (1993) 21:3537-3544 !$#title Complete sequence of Euglena gracilis chloroplast DNA. !$#cross-references MUID:93347989; PMID:8346031 !$#accession S34883 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-81 ##label HAL2 !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50095.1; !1PID:g415751 !'##experimental_source Pringsheim strain Z !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1993 GENETICS !$#gene psbE !$#genome chloroplast !$#introns 13/3; 23/3 COMPLEX heterodimer of alpha (psbE) and beta (psbF, see PIR:S00690) !1chains; tightly associated with the reaction center of !1photosystem II FUNCTION !$#description may be part of the water-oxidation complex of photosystem II !$#pathway photosystem II CLASSIFICATION #superfamily cytochrome b559 component E KEYWORDS chloroplast; chromoprotein; electron transfer; heme; !1heterodimer; iron; membrane-associated complex; !1metalloprotein; photosynthesis; photosystem II; thylakoid; !1transmembrane protein FEATURE !$2-81 #product cytochrome b559 component psbE #status !8predicted #label MAT\ !$19-43 #domain transmembrane #status predicted #label TMM\ !$44-81 #domain thylakoid lumenal #status predicted #label !8THL\ !$23 #binding_site heme iron (His) (axial ligand) (shared !8with beta chain) #status predicted SUMMARY #length 81 #molecular-weight 9222 #checksum 2194 SEQUENCE /// ENTRY CBKT5E #type complete TITLE cytochrome b559 component psbE - Cyanophora paradoxa cyanelle ALTERNATE_NAMES cytochrome b559 9K component; cytochrome b559 alpha chain ORGANISM #formal_name cyanelle Cyanophora paradoxa DATE 31-Dec-1992 #sequence_revision 21-May-1999 #text_change 03-Mar-2000 ACCESSIONS T06866; S09182 REFERENCE Z15840 !$#authors Stirewalt, V.L.; Michalowski, C.B.; Luffelhardt, W.; !1Bohnert, H.J.; Bryant, D.A. !$#submission submitted to the EMBL Data Library, July 1995 !$#description Nucleotide sequence of the cyanelle genome from Cyanophora !1paradoxa. !$#accession T06866 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-74 ##label STI !'##cross-references EMBL:U30821; NID:g1016083; PIDN:AAA81209.1; !1PID:g1016122 !'##experimental_source strain Pringsheim LB555 REFERENCE S09182 !$#authors Cantrell, A.; Bryant, D.A. !$#journal Prog. Photosyn. Res. (1987) 4:659-662 !$#title Molecular cloning and nucleotide sequences of the genes !1encoding cytochrome B-559 from the cyanelle genome of !1Cyanophora paradoxa. !$#accession S09182 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type DNA !'##residues 1-29,'FFI',33-74 ##label CAN GENETICS !$#gene psbE !$#genome cyanelle COMPLEX heterodimer of alpha (psbE) and beta (psbF, see PIR:CBKT5F) !1chains; tightly associated with the reaction center of !1photosystem II FUNCTION !$#description may be part of the water-oxidation complex of photosystem II !$#pathway photosystem II CLASSIFICATION #superfamily cytochrome b559 component E KEYWORDS chromoprotein; cyanelle; electron transfer; heme; !1heterodimer; iron; metalloprotein; photosynthesis; !1photosystem II; thylakoid; transmembrane protein FEATURE !$2-74 #product cytochrome b559 component psbE #status !8predicted #label MAT\ !$20-44 #domain transmembrane #status predicted #label TMM\ !$45-74 #domain thylakoid lumenal #status predicted #label !8THL\ !$24 #binding_site heme iron (His) (axial ligand) (shared !8with beta chain) #status predicted SUMMARY #length 74 #molecular-weight 8402 #checksum 400 SEQUENCE /// ENTRY CBYB55 #type complete TITLE cytochrome b559 component psbE - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES cytochrome b559 9K component; cytochrome b559 alpha chain; protein ssr3451 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jun-2000 ACCESSIONS S00338; S75178; S67978 REFERENCE S00338 !$#authors Pakrasi, H.B.; Williams, J.G.K.; Arntzen, C.J. !$#journal EMBO J. (1988) 7:325-332 !$#title Targeted mutagenesis of the psbE and psbF genes blocks !1photosynthetic electron transport: evidence for a functional !1role of cytochrome b559 in photosystem II. !$#cross-references MUID:88211541; PMID:3130246 !$#accession S00338 !'##molecule_type DNA !'##residues 1-81 ##label PAK !'##cross-references EMBL:X06988; NID:g47430; PIDN:CAA30048.1; !1PID:g47431 !'##note the sequence from Fig. 3 is inconsistent with that from Fig. 2 !1in having 77-Glu REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75178 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-81 ##label KAN !'##cross-references EMBL:D90903; GB:AB001339; NID:g1652127; !1PIDN:BAA17092.1; PID:g1652168 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 REFERENCE S67978 !$#authors Barbato, R.; Polverino de Laureto, P.; Rigoni, F.; de !1Martini, E.; Giacometti, G.M. !$#journal Eur. J. Biochem. (1995) 234:459-465 !$#title Pigment-protein complexes from the photosynthetic membrane !1of the cyanobacterium Synechocystis sp. PCC 6803. !$#cross-references MUID:96128174; PMID:8536689 !$#accession S67978 !'##molecule_type protein !'##residues 2-6 ##label BAR GENETICS !$#gene psbE COMPLEX heterodimer of alpha (psbE) and beta (psbF, see PIR:F2YB4) !1chains; tightly associated with the reaction center of !1photosystem II FUNCTION !$#description may be part of the water-oxidation complex of photosystem II !$#pathway photosystem II CLASSIFICATION #superfamily cytochrome b559 component E KEYWORDS chromoprotein; electron transfer; heme; heterodimer; iron; !1membrane-associated complex; metalloprotein; photosynthesis; !1photosystem II; thylakoid; transmembrane protein FEATURE !$2-81 #product cytochrome b559 component psbE #status !8predicted #label MAT\ !$19-43 #domain transmembrane #status predicted #label TMM\ !$45-74 #domain thylakoid lumenal #status predicted #label !8THL\ !$23 #binding_site heme iron (His) (axial ligand) (shared !8with beta chain) #status predicted SUMMARY #length 81 #molecular-weight 9449 #checksum 9668 SEQUENCE /// ENTRY F2NT4 #type complete TITLE cytochrome b559 component psbF - common tobacco chloroplast ALTERNATE_NAMES cytochrome b559 beta chain ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 03-Mar-2000 ACCESSIONS A05065; S55792; A25714 REFERENCE A00149 !$#authors Sugiura, M. !$#submission submitted to the EMBL Data Library, August 1986 !$#accession A05065 !'##molecule_type DNA !'##residues 1-39 ##label SUG !'##experimental_source cv. Bright Yellow 4 REFERENCE A38013 !$#authors Shinozaki, K.; Ohme, M.; Tanaka, M.; Wakasugi, T.; !1Hayashida, N.; Matsubayashi, T.; Zaita, N.; Chunwongse, J.; !1Obokata, J.; Yamaguchi-Shinozaki, K.; Ohto, C.; Torazawa, !1K.; Meng, B.Y.; Sugita, M.; Deno, H.; Kamogashira, T.; !1Yamada, K.; Kusuda, J.; Takaiwa, F.; Kato, A.; Tohdoh, N.; !1Shimada, H.; Sugiura, M. !$#journal EMBO J. (1986) 5:2043-2049 !$#title The complete nucleotide sequence of the tobacco chloroplast !1genome: its gene organization and expression. !$#contents annotation; gene organization, sites, features REFERENCE S55789 !$#authors Carrillo, N.; Seyer, P.; Tyagi, A.; Herrmann, R.G. !$#journal Curr. Genet. (1986) 10:619-624 !$#title Cytochrome b-559 genes from Oenothera hookeri and Nicotiana !1tabacum show a remarkably high degree of conservation as !1compared to spinach. !$#cross-references MUID:88165110; PMID:2450682 !$#accession S55792 !'##molecule_type DNA !'##residues 1-16,'I',18-39 ##label CAR !'##cross-references EMBL:X03781; NID:g11794; PIDN:CAA27413.1; !1PID:g11796 GENETICS !$#gene psbF !$#genome chloroplast COMPLEX heterodimer of alpha (psbE, see PIR:CBNT55) and beta (psbF) !1chains; tightly associated with the reaction center of !1photosystem II FUNCTION !$#description may be part of the water-oxidation complex of photosystem II !$#pathway photosystem II CLASSIFICATION #superfamily cytochrome b559 component F KEYWORDS chloroplast; chromoprotein; electron transfer; heme; !1heterodimer; iron; membrane-associated complex; !1metalloprotein; photosynthesis; photosystem II; thylakoid; !1transmembrane protein FEATURE !$15-31 #domain transmembrane #status predicted #label TMM\ !$18 #binding_site heme iron (His) (axial ligand) (shared !8with alpha chain) #status predicted SUMMARY #length 39 #molecular-weight 4484 #checksum 9981 SEQUENCE /// ENTRY F2RZ4 #type complete TITLE cytochrome b559 component psbF - rice chloroplast ALTERNATE_NAMES cytochrome b559 beta chain ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 03-Mar-2000 ACCESSIONS JQ0242; S05122; S08015 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0242 !'##molecule_type DNA !'##residues 1-39 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05122 !'##molecule_type DNA !'##residues 1-39 ##label HIR !'##cross-references EMBL:X15901; NID:g11957; PIDN:CAA33964.1; !1PID:g12003 !'##experimental_source cv. Nihonbare REFERENCE S08015 !$#authors Zhao, X.P.; Zhong-Xun, L.; Jean-Charles, C.; Wu, R. !$#submission submitted to the EMBL Data Library, April 1989 !$#accession S08015 !'##molecule_type DNA !'##residues 1-39 ##label ZHA !'##cross-references EMBL:X15057; NID:g11935; PIDN:CAA33156.1; !1PID:g11936 GENETICS !$#gene psbF !$#map_position CP62072-61953 !$#genome chloroplast COMPLEX heterodimer of alpha (psbE, see PIR:CBRZ55) and beta (psbF) !1chains; tightly associated with the reaction center of !1photosystem II FUNCTION !$#description may be part of the water-oxidation complex of photosystem II !$#pathway photosystem II CLASSIFICATION #superfamily cytochrome b559 component F KEYWORDS chloroplast; chromoprotein; electron transfer; heme; !1heterodimer; iron; membrane-associated complex; !1metalloprotein; photosynthesis; photosystem II; thylakoid; !1transmembrane protein FEATURE !$15-31 #domain transmembrane #status predicted #label TMM\ !$18 #binding_site heme iron (His) (axial ligand) (shared !8with alpha chain) #status predicted SUMMARY #length 39 #molecular-weight 4484 #checksum 9981 SEQUENCE /// ENTRY S58567 #type complete TITLE cytochrome b559 component psbF - maize chloroplast ALTERNATE_NAMES cytochrome b559 beta chain ORGANISM #formal_name chloroplast Zea mays #common_name maize DATE 29-Nov-1995 #sequence_revision 07-Jun-1996 #text_change 03-Mar-2000 ACCESSIONS S58567 REFERENCE S58531 !$#authors Maier, R.M.; Neckermann, K.; Igloi, G.L.; Koessel, H. !$#journal J. Mol. Biol. (1995) 251:614-628 !$#title Complete sequence of the maize chloroplast genome: gene !1content, hotspots of divergence and fine tuning of genetic !1information by transcript editing. !$#cross-references MUID:95395841; PMID:7666415 !$#accession S58567 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-39 ##label MAI !'##cross-references EMBL:X86563; NID:g902200; PIDN:CAA60301.1; !1PID:g902237 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1995 GENETICS !$#gene psbF !$#genome chloroplast COMPLEX heterodimer of alpha (psbE, see PIR:S58568) and beta (psbF) !1chains; tightly associated with the reaction center of !1photosystem II FUNCTION !$#description may be part of the water-oxidation complex of photosystem II !$#pathway photosystem II CLASSIFICATION #superfamily cytochrome b559 component F KEYWORDS chloroplast; chromoprotein; electron transfer; heme; !1heterodimer; iron; membrane-associated complex; !1metalloprotein; photosynthesis; photosystem II; thylakoid; !1transmembrane protein FEATURE !$15-31 #domain transmembrane #status predicted #label TMM\ !$18 #binding_site heme iron (His) (axial ligand) (shared !8with alpha chain) #status predicted SUMMARY #length 39 #molecular-weight 4484 #checksum 9981 SEQUENCE /// ENTRY F2KT5F #type complete TITLE cytochrome b559 component psbF - wheat chloroplast ALTERNATE_NAMES cytochrome b559 4K component; cytochrome b559 beta chain ORGANISM #formal_name chloroplast Triticum aestivum #common_name common wheat DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 03-Mar-2000 ACCESSIONS B26015; JG0012; S03622 REFERENCE A26015 !$#authors Hird, S.M.; Willey, D.L.; Dyer, T.A.; Gray, J.C. !$#journal Mol. Gen. Genet. (1986) 203:95-100 !$#title Location and nucleotide sequence of the gene for cytochrome !1b-559 in wheat chloroplast DNA. !$#accession B26015 !'##molecule_type DNA !'##residues 1-39 ##label HIR REFERENCE JG0010 !$#authors Webber, A.N.; Hird, S.M.; Packman, L.C.; Dyer, T.A.; Gray, !1J.C. !$#journal Plant Mol. Biol. (1989) 12:141-151 !$#title A photosystem II polypeptide is encoded by an open reading !1frame cotranscribed with genes for cytochrome b-559 in wheat !1chloroplast DNA. !$#accession JG0012 !'##molecule_type DNA !'##residues 1-39 ##label WEB !'##cross-references EMBL:X15225; NID:g14259; PIDN:CAA33295.1; !1PID:g14261 GENETICS !$#gene psbF !$#genome chloroplast COMPLEX heterodimer of alpha (psbE, see PIR:CBWT5E) and beta (psbF) !1chains; tightly associated with the reaction center of !1photosystem II FUNCTION !$#description may be part of the water-oxidation complex of photosystem II !$#pathway photosystem II CLASSIFICATION #superfamily cytochrome b559 component F KEYWORDS chloroplast; chromoprotein; electron transfer; heme; !1heterodimer; iron; membrane-associated complex; !1metalloprotein; photosynthesis; photosystem II; thylakoid; !1transmembrane protein FEATURE !$15-31 #domain transmembrane #status predicted #label TMM\ !$18 #binding_site heme iron (His) (axial ligand) (shared !8with alpha chain) #status predicted SUMMARY #length 39 #molecular-weight 4498 #checksum 9760 SEQUENCE /// ENTRY S03192 #type complete TITLE cytochrome b559 component psbF - rye chloroplast ALTERNATE_NAMES cytochrome b559 beta chain ORGANISM #formal_name chloroplast Secale cereale #common_name rye DATE 07-Jun-1990 #sequence_revision 07-Jun-1996 #text_change 03-Mar-2000 ACCESSIONS S03192; JN0357 REFERENCE S03191 !$#authors Kolosov, V.L.; Klezovich, O.N.; Zolotarev, A.S. !$#journal Nucleic Acids Res. (1989) 17:1760 !$#title Nucleotide sequence of the rye chloroplast DNA fragment, !1comprising psbE and psbF genes. !$#cross-references MUID:89160331; PMID:2646599 !$#accession S03192 !'##molecule_type DNA !'##residues 1-39 ##label KOL !'##cross-references EMBL:X13326; NID:g12230; PIDN:CAA31699.1; !1PID:g12232 REFERENCE JN0356 !$#authors Kolosov, V.L.; Klezovich, O.N.; Abdulaev, N.G.; Zolotonev, !1A.S. !$#journal Bioorg. Khim. (1989) 15:1284-1286 !$#title Nucleotide sequences of the rye chloroplast psbE, psbF and !1psbL genes coding for the polypeptides of photosystem II. !$#cross-references MUID:90073796; PMID:2686655 !$#accession JN0357 !'##status preliminary !'##molecule_type DNA !'##residues 1-39 ##label KO2 GENETICS !$#gene psbF !$#genome chloroplast COMPLEX heterodimer of alpha (psbE, see PIR:S03191) and beta (psbF) !1chains; tightly associated with the reaction center of !1photosystem II FUNCTION !$#description may be part of the water-oxidation complex of photosystem II !$#pathway photosystem II CLASSIFICATION #superfamily cytochrome b559 component F KEYWORDS chloroplast; chromoprotein; electron transfer; heme; !1heterodimer; iron; membrane-associated complex; !1metalloprotein; photosynthesis; photosystem II; thylakoid; !1transmembrane protein FEATURE !$15-31 #domain transmembrane #status predicted #label TMM\ !$18 #binding_site heme iron (His) (axial ligand) (shared !8with alpha chain) #status predicted SUMMARY #length 39 #molecular-weight 4498 #checksum 9760 SEQUENCE /// ENTRY S04063 #type complete TITLE cytochrome b559 component psbF - barley chloroplast ALTERNATE_NAMES cytochrome b559 beta chain ORGANISM #formal_name chloroplast Hordeum vulgare #common_name barley DATE 01-Dec-1989 #sequence_revision 07-Jun-1996 #text_change 03-Mar-2000 ACCESSIONS S04063; B29956; B31182; D31182; JN0351 REFERENCE S04062 !$#authors Chakhmakhcheva, O.G.; Andreeva, A.V.; Buryakova, A.A.; !1Reverdatto, S.V.; Efimov, V.A. !$#journal Nucleic Acids Res. (1989) 17:2858 !$#title Nucleotide sequence of the barley chloroplast psbE, psbF !1genes and flanking regions. !$#cross-references MUID:89240046; PMID:2654886 !$#accession S04063 !'##molecule_type DNA !'##residues 1-39 ##label CHA !'##cross-references EMBL:X14108; NID:g12351; PIDN:CAA32271.1; !1PID:g12353 REFERENCE A29956 !$#authors Krupinska, K.; Berry-Lowe, S. !$#journal Carlsberg Res. Commun. (1988) 53:43-55 !$#title Characterization and in vitro expression of the cytochrome !1b-559 genes of barley I. localization and sequence of the !1genes. !$#cross-references MUID:89374539; PMID:3256307 !$#accession B29956 !'##molecule_type DNA !'##residues 1-39 ##label KRU !'##cross-references GB:M35977; NID:g336408; PIDN:AAA84045.1; !1PID:g336410 !'##note the authors translated the codon CAG for residue 35 as Glu REFERENCE A90772 !$#authors Krupinska, K. !$#journal Carlsberg Res. Commun. (1988) 53:233-246 !$#title Characterization and in vitro expression of the cytochrome !1b-559 genes of barley. II. In vitro transcription and !1translation. !$#cross-references MUID:89351277; PMID:3255312 !$#accession B31182 !'##molecule_type DNA !'##residues 1-39 ##label KR2 !'##cross-references GB:M35616; NID:g336415; PIDN:AAA84049.1; !1PID:g336417 !'##note the authors translated the codon CAG for residue 35 as Glu !$#accession D31182 !'##molecule_type DNA !'##residues 'MNLVDPFRRPS',1-39 ##label KR3 !'##cross-references GB:M35616 !'##note the authors translated the codon CAG for residue 35 as Glu GENETICS !$#gene psbF !$#genome chloroplast COMPLEX heterodimer of alpha (psbE, see PIR:A29956) and beta (psbF) !1chains; tightly associated with the reaction center of !1photosystem II FUNCTION !$#description may be part of the water-oxidation complex of photosystem II !$#pathway photosystem II CLASSIFICATION #superfamily cytochrome b559 component F KEYWORDS chloroplast; chromoprotein; electron transfer; heme; !1heterodimer; iron; membrane-associated complex; !1metalloprotein; photosynthesis; photosystem II; thylakoid; !1transmembrane protein FEATURE !$15-31 #domain transmembrane #status predicted #label TMM\ !$18 #binding_site heme iron (His) (axial ligand) (shared !8with alpha chain) #status predicted SUMMARY #length 39 #molecular-weight 4498 #checksum 9760 SEQUENCE /// ENTRY S35262 #type complete TITLE cytochrome b559 component psbF - spinach chloroplast ALTERNATE_NAMES cytochrome b559 beta chain ORGANISM #formal_name chloroplast Spinacia oleracea #common_name spinach DATE 10-Dec-1993 #sequence_revision 07-Jun-1996 #text_change 03-Mar-2000 ACCESSIONS S35262; S60023; S00419; A24223 REFERENCE S35262 !$#authors Bock, R.; Hagemann, R.; Koessel, H.; Kudla, J. !$#journal Mol. Gen. Genet. (1993) 240:238-244 !$#title Tissue- and stage-specific modulation of RNA editing of the !1psbF and psbL transcript from spinach plastids - a new !1regulatory mechanism? !$#cross-references MUID:93360903; PMID:8355656 !$#accession S35262 !'##molecule_type mRNA !'##residues 1-39 ##label BOC !'##experimental_source cv. Matador !$#accession S60023 !'##molecule_type DNA !'##residues 1-25,'S',27-39 ##label BOW !'##experimental_source cv. Matador !'##note 26-Ser is translated as 26-Phe due to RNA editing REFERENCE S00418 !$#authors Herrmann, R.G.; Alt, J.; Schiller, B.; Widger, W.R.; Cramer, !1W.A. !$#journal FEBS Lett. (1984) 176:239-244 !$#title Nucleotide sequence of the gene for apocytochrome b-559 on !1the spinach plastid chromosome: implications for the !1structure of the membrane protein. !$#accession S00419 !'##molecule_type DNA !'##residues 1-25,'S',27-39 ##label HER !'##cross-references EMBL:M35673; NID:g343357; PIDN:AAA84629.1; !1PID:g343359 REFERENCE A24223 !$#authors Widger, W.R.; Cramer, W.A.; Hermodson, M.; Herrmann, R.G. !$#journal FEBS Lett. (1985) 191:186-190 !$#accession A24223 !'##molecule_type protein !'##residues 2-10 ##label WID GENETICS !$#gene psbF !$#genome chloroplast COMPLEX heterodimer of alpha (psbE, see PIR:A22550) and beta (psbF) !1chains; tightly associated with the reaction center of !1photosystem II FUNCTION !$#description may be part of the water-oxidation complex of photosystem II !$#pathway photosystem II CLASSIFICATION #superfamily cytochrome b559 component F KEYWORDS chloroplast; chromoprotein; electron transfer; heme; !1heterodimer; iron; membrane-associated complex; !1metalloprotein; photosynthesis; photosystem II; thylakoid; !1transmembrane protein FEATURE !$15-31 #domain transmembrane #status predicted #label TMM\ !$18 #binding_site heme iron (His) (axial ligand) (shared !8with alpha chain) #status predicted SUMMARY #length 39 #molecular-weight 4498 #checksum 9760 SEQUENCE /// ENTRY F2LV4 #type complete TITLE cytochrome b559 component psbF - liverwort (Marchantia polymorpha) chloroplast ALTERNATE_NAMES cytochrome b559 beta chain ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 03-Mar-2000 ACCESSIONS A25809; S01537 REFERENCE A00150 !$#authors Ohyama, K. !$#submission submitted to the EMBL Data Library, October 1986 !$#accession A25809 !'##molecule_type DNA !'##residues 1-39 ##label OHY REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features REFERENCE S01529 !$#authors Fukuzawa, H.; Kohchi, T.; Sano, T.; Shirai, H.; Umesono, K.; !1Inokuchi, H.; Ozeki, H.; Ohyama, K. !$#journal J. Mol. Biol. (1988) 203:333-351 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. III. Gene organization of the large !1single copy region from rbcL to trnI(CAU). !$#cross-references MUID:89068687; PMID:3199436 !$#accession S01537 !'##molecule_type DNA !'##residues 1-39 ##label FUK !'##cross-references EMBL:X04465; NID:g11640; PIDN:CAA28100.1; !1PID:g11688 GENETICS !$#gene psbF !$#genome chloroplast COMPLEX heterodimer of alpha (psbE, see PIR:CBLV55) and beta (psbF) !1chains; tightly associated with the reaction center of !1photosystem II FUNCTION !$#description may be part of the water-oxidation complex of photosystem II !$#pathway photosystem II CLASSIFICATION #superfamily cytochrome b559 component F KEYWORDS chloroplast; chromoprotein; electron transfer; heme; !1heterodimer; iron; membrane-associated complex; !1metalloprotein; photosynthesis; photosystem II; thylakoid; !1transmembrane protein FEATURE !$15-31 #domain transmembrane #status predicted #label TMM\ !$18 #binding_site heme iron (His) (axial ligand) (shared !8with alpha chain) #status predicted SUMMARY #length 39 #molecular-weight 4468 #checksum 9441 SEQUENCE /// ENTRY B48310 #type complete TITLE cytochrome b559 component psbF - garden pea chloroplast ALTERNATE_NAMES cytochrome b559 beta chain ORGANISM #formal_name chloroplast Pisum sativum #common_name garden pea DATE 31-Dec-1993 #sequence_revision 07-Jun-1996 #text_change 03-Mar-2000 ACCESSIONS B48310 REFERENCE A48310 !$#authors Willey, D.L.; Gray, J.C. !$#journal Curr. Genet. (1989) 15:213-220 !$#title Two small open reading frames are co-transcribed with the !1pea chloroplast genes for the polypeptides of cytochrome !1b-559. !$#cross-references MUID:89354671; PMID:2766383 !$#accession B48310 !'##molecule_type DNA !'##residues 1-39 ##label WIL !'##cross-references GB:X15767; NID:g12152; PIDN:CAA33773.1; PID:g12154 GENETICS !$#genome chloroplast COMPLEX heterodimer of alpha (psbE, see PIR:A48310) and beta (psbF) !1chains; tightly associated with the reaction center of !1photosystem II FUNCTION !$#description may be part of the water-oxidation complex of photosystem II !$#pathway photosystem II CLASSIFICATION #superfamily cytochrome b559 component F KEYWORDS chloroplast; chromoprotein; electron transfer; heme; !1heterodimer; iron; membrane-associated complex; !1metalloprotein; photosynthesis; photosystem II; thylakoid; !1transmembrane protein FEATURE !$15-31 #domain transmembrane #status predicted #label TMM\ !$18 #binding_site heme iron (His) (axial ligand) (shared !8with alpha chain) #status predicted SUMMARY #length 39 #molecular-weight 4424 #checksum 319 SEQUENCE /// ENTRY S01244 #type complete TITLE cytochrome b559 component psbF - evening primrose chloroplast ALTERNATE_NAMES cytochrome b559 beta chain ORGANISM #formal_name chloroplast Oenothera villaricae #common_name evening primrose DATE 30-Jun-1989 #sequence_revision 07-Jun-1996 #text_change 03-Mar-2000 ACCESSIONS S01244 REFERENCE S01243 !$#authors Schuster, W.; Brennicke, A. !$#journal Nucleic Acids Res. (1988) 16:7728 !$#title A plastid fragment from the psbE-psbF coding region in the !1mitochondrial genome of Oenothera berteriana. !$#cross-references MUID:88319966; PMID:3045763 !$#accession S01244 !'##molecule_type DNA !'##residues 1-39 ##label SCH !'##cross-references EMBL:X07951; NID:g11913; PIDN:CAA30777.1; !1PID:g11915 GENETICS !$#gene psbF !$#genome chloroplast COMPLEX heterodimer of alpha (psbE, see PIR:S01243) and beta (psbF) !1chains; tightly associated with the reaction center of !1photosystem II FUNCTION !$#description may be part of the water-oxidation complex of photosystem II !$#pathway photosystem II CLASSIFICATION #superfamily cytochrome b559 component F KEYWORDS chloroplast; chromoprotein; electron transfer; heme; !1heterodimer; iron; membrane-associated complex; !1metalloprotein; photosynthesis; photosystem II; thylakoid; !1transmembrane protein FEATURE !$15-31 #domain transmembrane #status predicted #label TMM\ !$18 #binding_site heme iron (His) (axial ligand) (shared !8with alpha chain) #status predicted SUMMARY #length 39 #molecular-weight 4424 #checksum 319 SEQUENCE /// ENTRY S55790 #type complete TITLE cytochrome b559 component psbF - Hooker's evening primrose chloroplast ALTERNATE_NAMES cytochrome b559 beta chain ORGANISM #formal_name chloroplast Oenothera hookeri subsp. hookeri #common_name Hooker's evening primrose DATE 27-Oct-1995 #sequence_revision 07-Jun-1996 #text_change 03-Mar-2000 ACCESSIONS S55790 REFERENCE S55789 !$#authors Carrillo, N.; Seyer, P.; Tyagi, A.; Herrmann, R.G. !$#journal Curr. Genet. (1986) 10:619-624 !$#title Cytochrome b-559 genes from Oenothera hookeri and Nicotiana !1tabacum show a remarkably high degree of conservation as !1compared to spinach. !$#cross-references MUID:88165110; PMID:2450682 !$#accession S55790 !'##molecule_type DNA !'##residues 1-39 ##label CAR !'##cross-references EMBL:X03780; NID:g11923; PIDN:CAA27411.1; !1PID:g11925 GENETICS !$#gene psbF !$#genome chloroplast COMPLEX heterodimer of alpha (psbE, see PIR:S55789) and beta (psbF) !1chains; tightly associated with the reaction center of !1photosystem II FUNCTION !$#description may be part of the water-oxidation complex of photosystem II !$#pathway photosystem II CLASSIFICATION #superfamily cytochrome b559 component F KEYWORDS chloroplast; chromoprotein; electron transfer; heme; !1heterodimer; iron; membrane-associated complex; !1metalloprotein; photosynthesis; photosystem II; thylakoid; !1transmembrane protein FEATURE !$15-31 #domain transmembrane #status predicted #label TMM\ !$18 #binding_site heme iron (His) (axial ligand) (shared !8with alpha chain) #status predicted SUMMARY #length 39 #molecular-weight 4424 #checksum 319 SEQUENCE /// ENTRY S00690 #type complete TITLE cytochrome b559 component psbF - Euglena gracilis chloroplast ALTERNATE_NAMES cytochrome b559 beta chain ORGANISM #formal_name chloroplast Euglena gracilis DATE 30-Jun-1989 #sequence_revision 07-Jun-1996 #text_change 03-Mar-2000 ACCESSIONS S00690; S34884; S34517 REFERENCE S00689 !$#authors Cushman, J.C.; Christopher, D.A.; Little, M.C.; Hallick, !1R.B.; Price, C.A. !$#journal Curr. Genet. (1988) 13:173-180 !$#title Organization of the psbE, psbF, orf38, and orf42 gene loci !1on the Euglena gracilis chloroplast genome. !$#cross-references MUID:88223485; PMID:3131027 !$#accession S00690 !'##molecule_type DNA !'##residues 1-41 ##label CUS !'##cross-references EMBL:X07073; NID:g11492; PIDN:CAA30109.1; !1PID:g11494 REFERENCE S34862 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.R.; !1Monfort, A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#journal Nucleic Acids Res. (1993) 21:3537-3544 !$#title Complete sequence of Euglena gracilis chloroplast DNA. !$#cross-references MUID:93347989; PMID:8346031 !$#accession S34884 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-41 ##label HAL2 !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50096.1; !1PID:g415752 !'##experimental_source Pringsheim strain Z !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1993 GENETICS !$#gene psbF !$#genome chloroplast !$#introns 5/3 COMPLEX heterodimer of alpha (psbE, see PIR:S00689) and beta (psbF) !1chains; tightly associated with the reaction center of !1photosystem II FUNCTION !$#description may be part of the water-oxidation complex of photosystem II !$#pathway photosystem II CLASSIFICATION #superfamily cytochrome b559 component F KEYWORDS chloroplast; chromoprotein; electron transfer; heme; !1heterodimer; iron; membrane-associated complex; !1metalloprotein; photosynthesis; photosystem II; thylakoid; !1transmembrane protein FEATURE !$17-33 #domain transmembrane #status predicted #label TMM\ !$20 #binding_site heme iron (His) (axial ligand) (shared !8with alpha chain) #status predicted SUMMARY #length 41 #molecular-weight 4791 #checksum 5611 SEQUENCE /// ENTRY F2YB4 #type complete TITLE cytochrome b559 component psbF - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES cytochrome b559 beta chain; protein smr0006 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jun-2000 ACCESSIONS S00339; S75179 REFERENCE S00338 !$#authors Pakrasi, H.B.; Williams, J.G.K.; Arntzen, C.J. !$#journal EMBO J. (1988) 7:325-332 !$#title Targeted mutagenesis of the psbE and psbF genes blocks !1photosynthetic electron transport: evidence for a functional !1role of cytochrome b559 in photosystem II. !$#cross-references MUID:88211541; PMID:3130246 !$#accession S00339 !'##molecule_type DNA !'##residues 1-44 ##label PAK !'##cross-references EMBL:X06988; NID:g47430; PIDN:CAA30049.1; !1PID:g47432 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75179 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-44 ##label KAN !'##cross-references EMBL:D90903; GB:AB001339; NID:g1652127; !1PIDN:BAA17093.1; PID:g1652169 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene psbF COMPLEX heterodimer of alpha (psbE, see PIR:CBYB55) and beta (psbF) !1chains; tightly associated with the reaction center of !1photosystem II FUNCTION !$#description may be part of the water-oxidation complex of photosystem II !$#pathway photosystem II CLASSIFICATION #superfamily cytochrome b559 component F KEYWORDS chromoprotein; electron transfer; heme; heterodimer; iron; !1membrane-associated complex; metalloprotein; photosynthesis; !1photosystem II; thylakoid; transmembrane protein FEATURE !$2-44 #product cytochrome b559 component psbF #status !8experimental #label MAT\ !$20-36 #domain transmembrane #status predicted #label TMM\ !$23 #binding_site heme iron (His) (axial ligand) (shared !8with alpha chain) #status predicted SUMMARY #length 44 #molecular-weight 4933 #checksum 5764 SEQUENCE /// ENTRY S51365 #type complete TITLE cytochrome b559 component psbF - Chlamydomonas eugametos chloroplast ALTERNATE_NAMES cytochrome b559 beta chain ORGANISM #formal_name chloroplast Chlamydomonas eugametos DATE 01-Aug-1995 #sequence_revision 07-Jun-1996 #text_change 03-Mar-2000 ACCESSIONS S51365 REFERENCE S51365 !$#authors Turmel, M.; Otis, C. !$#journal Curr. Genet. (1994) 27:54-61 !$#title The chloroplast gene cluster containing psbF, psbL, petG and !1rps3 is conserved in Chlamydomonas. !$#cross-references MUID:95269309; PMID:7750147 !$#accession S51365 !'##molecule_type DNA !'##residues 1-44 ##label TUR !'##cross-references EMBL:L29282; NID:g575472; PIDN:AAA84156.1; !1PID:g575473 GENETICS !$#gene psbF !$#genome chloroplast COMPLEX heterodimer of alpha (psbE, see PIR:S53882) and beta (psbF) !1chains; tightly associated with the reaction center of !1photosystem II FUNCTION !$#description may be part of the water-oxidation complex of photosystem II !$#pathway photosystem II CLASSIFICATION #superfamily cytochrome b559 component F KEYWORDS chloroplast; chromoprotein; electron transfer; heme; !1heterodimer; iron; membrane-associated complex; !1metalloprotein; photosynthesis; photosystem II; thylakoid; !1transmembrane protein FEATURE !$20-36 #domain transmembrane #status predicted #label TMM\ !$23 #binding_site heme iron (His) (axial ligand) (shared !8with alpha chain) #status predicted SUMMARY #length 44 #molecular-weight 5043 #checksum 6024 SEQUENCE /// ENTRY S53883 #type complete TITLE cytochrome b559 component psbF - Chlamydomonas reinhardtii chloroplast ALTERNATE_NAMES cytochrome b559 beta chain ORGANISM #formal_name chloroplast Chlamydomonas reinhardtii DATE 27-Oct-1995 #sequence_revision 07-Jun-1996 #text_change 03-Mar-2000 ACCESSIONS S53883; S26878; T08170 REFERENCE S53882 !$#authors Mor, T.S.; Ohad, I.; Hirschberg, J.; Pakrasi, H.B. !$#journal Mol. Gen. Genet. (1995) 246:600-604 !$#title An unusual organization of the genes encoding cytochrome b !1(559) in Chlamydomonas reinhardtii: psbE and psbF genes are !1separately transcribed from different regions of the plastid !1chromosome. !$#cross-references MUID:95214620; PMID:7700232 !$#accession S53883 !'##molecule_type DNA !'##residues 1-44 ##label MOR !'##cross-references EMBL:X79564; NID:g853811; PIDN:CAA56101.1; !1PID:g853812 REFERENCE S26878 !$#authors Fong, S.E.; Surzycki, S.J. !$#journal Curr. Genet. (1992) 21:527-530 !$#title Organization and structure of plastome psbF, psbL, petG and !1ORF712 genes in Chlamydomonas reinhardtii. !$#cross-references MUID:92315354; PMID:1617741 !$#accession S26878 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-21,'TTVLQYQQF',31-44 ##label FON !'##cross-references GB:X66250; NID:g393459; PIDN:CAA46977.1; !1PID:g393460 GENETICS !$#gene psbF !$#genome chloroplast COMPLEX heterodimer of alpha (psbE, see PIR:S53882) and beta (psbF) !1chains; tightly associated with the reaction center of !1photosystem II FUNCTION !$#description may be part of the water-oxidation complex of photosystem II !$#pathway photosystem II CLASSIFICATION #superfamily cytochrome b559 component F KEYWORDS chloroplast; chromoprotein; electron transfer; heme; !1heterodimer; iron; membrane-associated complex; !1metalloprotein; photosynthesis; photosystem II; thylakoid; !1transmembrane protein FEATURE !$20-36 #domain transmembrane #status predicted #label TMM\ !$23 #binding_site heme iron (His) (axial ligand) (shared !8with alpha chain) #status predicted SUMMARY #length 44 #molecular-weight 4981 #checksum 4909 SEQUENCE /// ENTRY CBKT5F #type complete TITLE cytochrome b559 component psbF - Cyanophora paradoxa cyanelle ALTERNATE_NAMES cytochrome b559 beta chain ORGANISM #formal_name cyanelle Cyanophora paradoxa DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 03-Mar-2000 ACCESSIONS S09482; T06867 REFERENCE S09182 !$#authors Cantrell, A.; Bryant, D.A. !$#journal Prog. Photosyn. Res. (1987) 4:659-662 !$#title Molecular cloning and nucleotide sequences of the genes !1encoding cytochrome B-559 from the cyanelle genome of !1Cyanophora paradoxa. !$#accession S09482 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type DNA !'##residues 1-42 ##label CAN REFERENCE Z15840 !$#authors Stirewalt, V.L.; Michalowski, C.B.; Luffelhardt, W.; !1Bohnert, H.J.; Bryant, D.A. !$#submission submitted to the EMBL Data Library, July 1995 !$#description Nucleotide sequence of the cyanelle genome from Cyanophora !1paradoxa. !$#accession T06867 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-42 ##label STI !'##cross-references EMBL:U30821; NID:g1016083; PIDN:AAA81210.1; !1PID:g1016123 !'##experimental_source strain Pringsheim LB555 GENETICS !$#gene psbF !$#genome cyanelle COMPLEX heterodimer of alpha (psbE, see PIR:CBKT5E) and beta (psbF) !1chains; tightly associated with the reaction center of !1photosystem II FUNCTION !$#description may be part of the water-oxidation complex of photosystem II !$#pathway photosystem II CLASSIFICATION #superfamily cytochrome b559 component F KEYWORDS chromoprotein; cyanelle; electron transfer; heme; !1heterodimer; iron; membrane-associated complex; !1metalloprotein; photosynthesis; photosystem II; thylakoid; !1transmembrane protein FEATURE !$18-34 #domain transmembrane #status predicted #label TMM\ !$21 #binding_site heme iron (His) (axial ligand) (shared !8with alpha chain) #status predicted SUMMARY #length 42 #molecular-weight 4761 #checksum 8435 SEQUENCE /// ENTRY CBHU5 #type complete TITLE cytochrome b5, microsomal splice form [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 29-Jul-1981 #sequence_revision 05-Apr-1995 #text_change 20-Apr-2000 ACCESSIONS A28936; S04976; A91933; A00167; A24211; A32912 REFERENCE A28936 !$#authors Yoo, M.; Steggles, A.W. !$#journal Biochem. Biophys. Res. Commun. (1988) 156:576-580 !$#title The complete nucleotide sequence of human liver cytochrome !1b5 mRNA. !$#cross-references MUID:89025904; PMID:3178851 !$#accession A28936 !'##molecule_type mRNA !'##residues 1-134 ##label YOO !'##cross-references GB:M22865; NID:g181226; PIDN:AAA35729.1; !1PID:g181227 !'##experimental_source liver REFERENCE S04976 !$#authors Ozols, J. !$#journal Biochim. Biophys. Acta (1989) 997:121-130 !$#title Structure of cytochrome b(5) and its topology in the !1microsomal membrane. !$#cross-references MUID:89323209; PMID:2752049 !$#accession S04976 !'##molecule_type protein !'##residues 2-3,'E',5-36;84-121,'V',123-134 ##label OZO !'##experimental_source liver REFERENCE A91933 !$#authors Rashid, M.A.; Hagihara, B.; Kobayashi, M.; Tani, S.; !1Tsugita, A. !$#journal J. Biochem. (1973) 74:985-1002 !$#title Structural studies of cytochrome b-5. III. Sequential !1studies on human liver cytochrome b-5. !$#cross-references MUID:74074962; PMID:4770377 !$#accession A91933 !'##molecule_type protein !'##residues 'QZA',5-14,'Q',16-17,'E',19-21,23-61,'D',63-88,'K',90,'R' !1##label RAS !'##experimental_source liver !'##note blocked amino-terminal peptide attributed to pyrrolidone !1carboxylic acid REFERENCE A92077 !$#authors Nobrega, F.G.; Ozols, J. !$#journal J. Biol. Chem. (1971) 246:1706-1717 !$#title Amino acid sequences of tryptic peptides of cytochromes b-5 !1from microsomes of human, monkey, porcine, and chicken !1liver. !$#cross-references MUID:71134790; PMID:4993957 !$#accession A00167 !'##molecule_type protein !'##residues 5-14,'Q',16-17,'E',19-61,'D',63-88,'K',90,'R' ##label NOB !'##experimental_source liver REFERENCE A32912 !$#authors Yoo, M.; Steggles, A.W. !$#journal Biochem. Biophys. Res. Commun. (1989) 163:18-24 !$#title The characterization of three types of partially processed !1mRNA and two pseudogenes for human liver cytochrome b-5. !$#cross-references MUID:89374222; PMID:2775258 !$#contents annotation; introns REFERENCE A91992 !$#authors Abe, K.; Kimura, S.; Kizawa, R.; Anan, F.K.; Sugita, Y. !$#journal J. Biochem. (1985) 97:1659-1668 !$#title Amino acid sequences of cytochrome b5 from human, porcine, !1and bovine erythrocytes and comparison with liver microsomal !1cytochrome b5. !$#cross-references MUID:85289161; PMID:4030743 !$#contents annotation; amino-terminal acetylation REFERENCE A92103 !$#authors Ozols, J. !$#journal J. Biol. Chem. (1972) 247:2242-2245 !$#title Cytochrome b-5 from a normal human liver. Isolation and the !1partial amino acid sequence. !$#cross-references MUID:72154531; PMID:5062820 !$#contents annotation COMMENT Cytochrome b5 exists in at least two alternative splice !1forms. This longer form is found bound in microsome !1membranes, on the cytoplasmic side of the endoplasmic !1reticulum. The shorter form (see PIR:CBHU5E) is found in !1erythrocytes. GENETICS !$#gene GDB:CYB5 !'##cross-references GDB:125236; OMIM:250790 !$#map_position 18q22.3-18q23 !$#introns 86/3 !$#note the list of introns may be incomplete FUNCTION !$#description acts an electron carrier for membrane bound oxygenases; with !1cytochrome-b5 reductase enables exchange between NADPH and !1membrane bound oxidases CLASSIFICATION #superfamily cytochrome b5; cytochrome b5 core homology KEYWORDS acetylated amino end; alternative splicing; chromoprotein; !1electron transfer; heme; iron; membrane protein; !1metalloprotein; microsome FEATURE !$2-134 #product cytochrome b5, microsomal splice form !8#status experimental #label MAT\ !$9-84 #domain cytochrome b5 core homology #label CB5\ !$119-131 #domain transmembrane #status predicted #label TRM\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental\ !$44,68 #binding_site heme iron (His) (axial ligands) #status !8predicted SUMMARY #length 134 #molecular-weight 15330 #checksum 9842 SEQUENCE /// ENTRY CBHU5E #type complete TITLE cytochrome b5, erythrocyte splice form [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 08-Aug-1987 #sequence_revision 05-Apr-1995 #text_change 20-Apr-2000 ACCESSIONS JN0075; B24211 REFERENCE JN0075 !$#authors Giordano, S.J.; Steggles, A.W. !$#journal Biochem. Biophys. Res. Commun. (1991) 178:38-44 !$#title The human liver and reticulocyte cytochrome b5 mRNAs are !1products from a single gene. !$#cross-references MUID:91298976; PMID:1712589 !$#accession JN0075 !'##molecule_type mRNA !'##residues 1-98 ##label GIO !'##cross-references GB:M60174; NID:g181391; PIDN:AAA52165.1; !1PID:g181392 !'##experimental_source erythrocyte REFERENCE A91992 !$#authors Abe, K.; Kimura, S.; Kizawa, R.; Anan, F.K.; Sugita, Y. !$#journal J. Biochem. (1985) 97:1659-1668 !$#title Amino acid sequences of cytochrome b5 from human, porcine, !1and bovine erythrocytes and comparison with liver microsomal !1cytochrome b5. !$#cross-references MUID:85289161; PMID:4030743 !$#accession B24211 !'##molecule_type protein !'##residues 2-88,'K',90,'R',92-98 ##label ABE !'##experimental_source erythrocyte COMMENT Cytochrome b5 exists in at least two alternative splice !1forms. This shorter form is found in erythrocyte cytoplasm. !1The longer form (see PIR:CBHU5) is found bound in microsome !1membranes. GENETICS !$#gene GDB:CYB5 !'##cross-references GDB:125236; OMIM:250790 !$#map_position 18q23-18q23 !$#introns 86/3 !$#note the list of introns may be incomplete FUNCTION !$#description acts to reduce methemoglobin to functional hemoglobin; the !1oxidized form is reduced by cytochrome b5 reductase with !1NADPH !$#note a deficiency of this protein causes type IV hereditary !1methemoglobinemia CLASSIFICATION #superfamily cytochrome b5; cytochrome b5 core homology KEYWORDS acetylated amino end; alternative splicing; chromoprotein; !1electron transfer; erythrocyte; heme; iron; metalloprotein FEATURE !$2-98 #product cytochrome b5, erythrocyte splice form !8#status experimental #label MAT\ !$9-84 #domain cytochrome b5 core homology #label CB5\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental\ !$44,68 #binding_site heme iron (His) (axial ligands) #status !8predicted SUMMARY #length 98 #molecular-weight 11268 #checksum 9298 SEQUENCE /// ENTRY CBRB5 #type complete TITLE cytochrome b5, microsomal splice form [validated] - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 29-Jul-1981 #sequence_revision 31-Dec-1993 #text_change 20-Apr-2000 ACCESSIONS S03373; S07961; A91920; A93774; A92068; A91953; A92269; !1A61482; A00168; A31221 REFERENCE S03373 !$#authors Dariush, N.; Fisher, C.W.; Steggles, A.W. !$#journal Protein Seq. Data Anal. (1988) 1:351-353 !$#title The nucleotide sequence of rabbit liver cytochrome b(5) !1mRNA. !$#cross-references MUID:89128816; PMID:3222252 !$#accession S03373 !'##molecule_type mRNA !'##residues 1-134 ##label DAR !'##cross-references GB:M24844; NID:g1431635; PIDN:AAB03878.1; !1PID:g164785 !'##note the authors translated the codon GAC for residues 6 and 8 as !1Asn, AAC for residue 21 as Asp, GAT for residues 58 and 104 !1as Asn, and ATG for residue 126 as Phe REFERENCE S04976 !$#authors Ozols, J. !$#journal Biochim. Biophys. Acta (1989) 997:121-130 !$#title Structure of cytochrome b(5) and its topology in the !1microsomal membrane. !$#cross-references MUID:89323209; PMID:2752049 !$#accession S07961 !'##molecule_type protein !'##residues 2-4 ##label OZO REFERENCE A91920 !$#authors Tsugita, A.; Kobayashi, M.; Kajihara, T.; Hagihara, B. !$#journal J. Biochem. (1968) 64:727-730 !$#title Primary structure of rabbit liver cytochrome b5. !$#cross-references MUID:69108767; PMID:5709273 !$#accession A91920 !'##molecule_type protein !'##residues 9-46;40-61,'D',63-91 ##label TS1 REFERENCE A93774 !$#authors Tsugita, A.; Kobayashi, M.; Tani, S.; Kyo, S.; Rashid, M.A.; !1Yoshida, Y.; Kajihara, T.; Hagihara, B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1970) 67:442-447 !$#title Comparative study of the primary structures of cytochrome !1b-5 from four species. !$#cross-references MUID:70289989; PMID:5272324 !$#accession A93774 !'##molecule_type protein !'##residues 7-8;47-49 ##label TS2 REFERENCE A92068 !$#authors Ozols, J. !$#journal J. Biol. Chem. (1970) 245:4863-4874 !$#title Amino acid sequence of rabbit liver microsomal cytochrome !1b-5. !$#cross-references MUID:71001482; PMID:5506260 !$#accession A92068 !'##molecule_type protein !'##residues 5-15,'Q',17-98 ##label OZ2 !'##note the two minor components have either 11-Phe and 14-Glu or !196-Thr and an additional carboxyl-terminal Glx REFERENCE A91953 !$#authors Kondo, K.; Tajima, S.; Sato, R.; Narita, K. !$#journal J. Biochem. (1979) 86:1119-1128 !$#title Primary structure of the membrane-binding segment of rabbit !1cytochrome b-5. !$#cross-references MUID:80049603; PMID:500581 !$#accession A91953 !'##molecule_type protein !'##residues 92-103,'N',105-134 ##label KON !'##note this segment corresponds to the membrane-binding carboxyl end !1of the molecule REFERENCE A92269 !$#authors Takagaki, Y.; Gerber, G.E.; Nihei, K.; Khorana, H.G. !$#journal J. Biol. Chem. (1980) 255:1536-1541 !$#title Amino acid sequence of the membranous segment of rabbit !1liver cytochrome b-5. Methodology for separation of !1hydrophobic peptides. !$#cross-references MUID:80115672; PMID:7354043 !$#accession A92269 !'##molecule_type protein !'##residues 99-134 ##label TAK REFERENCE A61482 !$#authors Gibson, B.W.; Falick, A.M.; Lipka, J.J.; Waskell, L.A. !$#journal J. Protein Chem. (1990) 9:695-703 !$#title Mass spectrometric analysis of rabbit and bovine !1trypsin-solubilized cytochrome b-5. !$#cross-references MUID:91158806; PMID:2073321 !$#accession A61482 !'##molecule_type protein !'##residues 2-3,'E',5-16 ##label GIB CLASSIFICATION #superfamily cytochrome b5; cytochrome b5 core homology KEYWORDS acetylated amino end; alternative splicing; chromoprotein; !1heme; iron; metalloprotein FEATURE !$2-134 #product cytochrome b5 #status experimental #label !8MAT\ !$9-84 #domain cytochrome b5 core homology #label CB5\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental\ !$44,68 #binding_site heme iron (His) (axial ligands) #status !8predicted SUMMARY #length 134 #molecular-weight 15349 #checksum 260 SEQUENCE /// ENTRY JN0316 #type complete TITLE cytochrome b5, erythrocyte splice form [validated] - rabbit ALTERNATE_NAMES soluble cytochrome b5 ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 16-Jun-2000 ACCESSIONS JN0316; S29841 REFERENCE JN0316 !$#authors Takematsu, H.; Kozutsumi, Y.; Suzuki, A.; Kawasaki, T. !$#journal Biochem. Biophys. Res. Commun. (1992) 185:845-851 !$#title Molecular cloning of rabbit cytochrome B5 genes; evidence !1for the occurrence of two separate genes encoding the !1soluble and microsomal forms. !$#cross-references MUID:92328788; PMID:1627141 !$#accession JN0316 !'##molecule_type mRNA !'##residues 1-98 ##label TAK !'##cross-references GB:D10901; NID:g471149; PIDN:BAA01712.1; !1PID:g471150 !'##note Thr-96 was also found REFERENCE S29841 !$#authors Giordano, S.J.; Steggles, A.W. !$#journal Biochim. Biophys. Acta (1993) 1172:95-100 !$#title Differential expression of the mRNAs for the soluble and !1membrane-bound forms of rabbit cytochrome b(5). !$#cross-references MUID:93176833; PMID:8439576 !$#accession S29841 !'##status preliminary !'##molecule_type mRNA !'##residues 1-98 ##label GIO !'##cross-references EMBL:Z14091; NID:g1542 !'##note this translation is not annotated in GenBank entry OCCYTB5, !1release 113.0 CLASSIFICATION #superfamily cytochrome b5; cytochrome b5 core homology KEYWORDS acetylated amino end; alternative splicing; chromoprotein; !1electron transfer; heme; iron; liver; metalloprotein FEATURE !$9-84 #domain cytochrome b5 core homology #label CB5\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status predicted\ !$44,68 #binding_site heme iron (His) (axial ligands) #status !8predicted SUMMARY #length 98 #molecular-weight 11232 #checksum 9388 SEQUENCE /// ENTRY CBHO5 #type complete TITLE cytochrome b5, microsomal form [validated] - horse ALTERNATE_NAMES hepatic cytochrome b5; membrane-bound cytochrome b5 ORGANISM #formal_name Equus caballus #common_name domestic horse DATE 29-Jul-1981 #sequence_revision 20-Apr-2000 #text_change 05-May-2000 ACCESSIONS S07964; A92196; A92218; A00169 REFERENCE S04976 !$#authors Ozols, J. !$#journal Biochim. Biophys. Acta (1989) 997:121-130 !$#title Structure of cytochrome b(5) and its topology in the !1microsomal membrane. !$#cross-references MUID:89323209; PMID:2752049 !$#accession S07964 !'##molecule_type protein !'##residues 1-133 ##label OZO1 REFERENCE A92196 !$#authors Ozols, J.; Gerard, C.; Nobrega, F.G. !$#journal J. Biol. Chem. (1976) 251:6767-6774 !$#title Proteolytic cleavage of horse liver cytochrome b5. !$#cross-references MUID:77028943; PMID:977596 !$#accession A92196 !'##molecule_type protein !'##residues 'Z',2,'DAS',6-41,'D',43-98 ##label OZO2 !'##note the amino terminal is shown to be blocked by acetylation and !1not pyroglutamic acid in reference S07964, MUID:89323209 REFERENCE A92218 !$#authors Ozols, J.; Gerard, C. !$#journal J. Biol. Chem. (1977) 252:8549-8553 !$#title Covalent structure of the membranous segment of horse !1cytochrome b-5. Chemical cleavage of the native hemoprotein. !$#cross-references MUID:78045981; PMID:562879 !$#accession A92218 !'##molecule_type protein !'##residues 89-133 ##label OZO3 CLASSIFICATION #superfamily cytochrome b5; cytochrome b5 core homology KEYWORDS acetylated amino end; alternative splicing; chromoprotein; !1electron transfer; heme; iron; liver; metalloprotein FEATURE !$8-83 #domain cytochrome b5 core homology #label CB5\ !$108-129 #domain transmembrane #status predicted #label TRM\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$43,67 #binding_site heme iron (His) (axial ligands) #status !8predicted SUMMARY #length 133 #molecular-weight 15154 #checksum 7828 SEQUENCE /// ENTRY CBBO5 #type complete TITLE cytochrome b5, microsomal form [validated] - bovine CONTAINS cytochrome b5, erythrocyte form ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 12-Aug-1981 #sequence_revision 05-May-1995 #text_change 15-Sep-2000 ACCESSIONS A47215; S03428; F24211; S07963; A90383; A92053; B93774; !1A92231; A00170 REFERENCE A47215 !$#authors Cristiano, R.J.; Giordano, S.J.; Steggles, A.W. !$#journal Genomics (1993) 17:348-354 !$#title The isolation and characterization of the bovine cytochrome !1b5 gene, and a transcribed pseudogene. !$#cross-references MUID:94010928; PMID:8406485 !$#accession A47215 !'##molecule_type DNA !'##residues 1-134 ##label CRI !'##cross-references GB:M63226; GB:M63227; GB:M63228; GB:M63329; !1GB:L22966; NID:g387580 !'##note sequence extracted from NCBI backbone and corrected to !1correspond with the published sequence !'##note the authors conclude that the erythrocyte form is generated by !1posttranslational processing of the microsomal form and not !1from the possible alternative splicing REFERENCE S03428 !$#authors Cristiano, R.J.; Steggles, A.W. !$#journal Nucleic Acids Res. (1989) 17:799 !$#title The complete nucleotide sequence of bovine liver cytochrome !1b(5) mRNA. !$#cross-references MUID:89128451; PMID:2915932 !$#accession S03428 !'##molecule_type mRNA !'##residues 1-134 ##label CR2 !'##cross-references EMBL:X13617; NID:g297; PIDN:CAA31949.1; PID:g298 REFERENCE A91992 !$#authors Abe, K.; Kimura, S.; Kizawa, R.; Anan, F.K.; Sugita, Y. !$#journal J. Biochem. (1985) 97:1659-1668 !$#title Amino acid sequences of cytochrome b5 from human, porcine, !1and bovine erythrocytes and comparison with liver microsomal !1cytochrome b5. !$#cross-references MUID:85289161; PMID:4030743 !$#accession F24211 !'##molecule_type protein !'##residues 2,'Z',4-98 ##label ABE !'##experimental_source erythrocyte !'##note residues 2-3 were positioned by homology with the bovine liver !1sequence REFERENCE S04976 !$#authors Ozols, J. !$#journal Biochim. Biophys. Acta (1989) 997:121-130 !$#title Structure of cytochrome b(5) and its topology in the !1microsomal membrane. !$#cross-references MUID:89323209; PMID:2752049 !$#accession S07963 !'##molecule_type protein !'##residues 2-6;15-18 ##label OZO1 REFERENCE A90383 !$#authors Ozols, J. !$#journal Biochemistry (1974) 13:426-434 !$#title Cytochrome beta-5 from microsomal membranes of equine, !1bovine, and porcine livers. Isolation and properties of !1preparations containing the membranous segment. !$#cross-references MUID:74080219; PMID:4810060 !$#accession A90383 !'##molecule_type protein !'##residues 'ZB',2,'ZZ',5-11;131-133,'D' ##label OZO2 REFERENCE A92053 !$#authors Ozols, J.; Strittmatter, P. !$#journal J. Biol. Chem. (1969) 244:6617-6618 !$#title Correction of the amino acid sequence of calf liver !1microsomal cytochrome b5. !$#cross-references MUID:70067001; PMID:5391285 !$#accession A92053 !'##molecule_type protein !'##residues 6-15,'QEI',19-61,'D',63-97 ##label OZO3 !'##experimental_source liver REFERENCE A93774 !$#authors Tsugita, A.; Kobayashi, M.; Tani, S.; Kyo, S.; Rashid, M.A.; !1Yoshida, Y.; Kajihara, T.; Hagihara, B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1970) 67:442-447 !$#title Comparative study of the primary structures of cytochrome !1b-5 from four species. !$#cross-references MUID:70289989; PMID:5272324 !$#accession B93774 !'##molecule_type protein !'##residues 6-17,'E',19-61,'D',63-96 ##label TSU REFERENCE A92231 !$#authors Fleming, P.J.; Dailey, H.A.; Corcoran, D.; Strittmatter, P. !$#journal J. Biol. Chem. (1978) 253:5369-5372 !$#title The primary structure of the nonpolar segment of bovine !1cytochrome b5. !$#cross-references MUID:78218214; PMID:670203 !$#accession A92231 !'##molecule_type protein !'##residues 92-134 ##label FLE REFERENCE A66921 !$#authors Muskett, F.W.; Kelly, G.P.; Whitford, D. !$#submission submitted to the Brookhaven Protein Data Bank, February 1996 !$#cross-references PDB:1WDB !$#contents annotation; conformation by (1)H-, (15)N-NMR, residues 6-89 REFERENCE A58628 !$#authors Muskett, F.W.; Kelly, G.P.; Whitford, D. !$#journal J. Mol. Biol. (1996) 258:172-189 !$#title The solution structure of bovine ferricytochrome b5 !1determined using heteronuclear NMR methods. !$#cross-references MUID:96200988; PMID:8613986 !$#contents annotation; conformation by (1)H-, (15)N-NMR REFERENCE A52769 !$#authors Durley, R.C.E.; Mathews, F.S. !$#submission submitted to the Brookhaven Protein Data Bank, August 1994 !$#cross-references PDB:1CYO !$#contents annotation; X-ray crystallography, 1.5 angstroms, residues !16-93 REFERENCE A50568 !$#authors Mathews, F.S.; Durley, R.C.E. !$#submission submitted to the Brookhaven Protein Data Bank, January 1990 !$#cross-references PDB:3B5C !$#contents annotation; X-ray crystallography, 1.5 angstroms, 8-92 REFERENCE A90922 !$#authors Mathews, F.S.; Argos, P.; Levine, M. !$#journal Cold Spring Harb. Symp. Quant. Biol. (1971) 37:387-395 !$#title The structure of cytochrome b-5 at 2.0 angstrom resolution. !$#contents annotation; oxidized form, X-ray crystallography, 2.0 !1angstroms; revision to residues 18 and 19 REFERENCE A92186 !$#authors Argos, P.; Mathews, F.S. !$#journal J. Biol. Chem. (1975) 250:747-751 !$#title The structure of ferrocytochrome b5 at 2.8 A resolution. !$#cross-references MUID:75095526; PMID:1167544 !$#contents annotation; reduced form, X-ray crystallography, 2.8 !1angstroms !$#note the structure of the reduced form was found to be the same !1as that of the oxidized form, except for a slight !1displacement of one lysine side chain caused by the binding !1of a cation at the entrance of the heme crevice COMMENT This protein contains two domains: a hydrophilic, catalytic, !1amino-terminal segment consisting of about 85 residues and a !1hydrophobic carboxyl-terminal segment that is required for !1binding the cytochrome to biological membranes. GENETICS !$#gene CYB5 !$#introns 43/3; 86/3; 96/3; 108/2 FUNCTION MIC !$#description acts as an electron carrier for membrane bound oxygenases; !1with cytochrome-b5 reductase enables exchange between NADPH !1and membrane bound oxidases !$#note microsomal form FUNCTION ERY !$#description acts to reduce methemoglobin to functional hemoglobin; the !1oxidized form is reduced by cytochrome b5 reductase with !1NADPH !$#note erythrocyte form CLASSIFICATION #superfamily cytochrome b5; cytochrome b5 core homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; membrane protein; metalloprotein; microsome FEATURE !$2-134 #product cytochrome b5, microsomal form #status !8experimental #label MAT\ !$2-98 #product cytochrome b5, erythrocyte form #status !8experimental #label MA2\ !$9-84 #domain cytochrome b5 core homology #label CB5\ !$105-127 #domain membrane-bound #status predicted #label MEM\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental\ !$44,68 #binding_site heme iron (His) (axial ligands) #status !8experimental SUMMARY #length 134 #molecular-weight 15329 #checksum 204 SEQUENCE /// ENTRY CBPG5 #type complete TITLE cytochrome b5, microsomal splice form [validated] - pig ALTERNATE_NAMES hepatic cytochrome b5; membrane-bound cytochrome b5 ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 29-Jul-1981 #sequence_revision 20-Apr-2000 #text_change 05-May-2000 ACCESSIONS JC5782; C24211; S07962; B90383; B92077; A93813; A00171 REFERENCE JC5782 !$#authors VanDerMark, P.K.; Steggles, A.W. !$#journal Biochem. Biophys. Res. Commun. (1997) 240:80-83 !$#title The isolation and characterization of the soluble and !1membrane-bound porcine cytochrome b5 cDNAs. !$#cross-references MUID:98042520; PMID:9367886 !$#accession JC5782 !'##molecule_type mRNA !'##residues 1-134 ##label VAN !'##cross-references GB:AF016388; NID:g2642485; PIDN:AAC48779.1; !1PID:g2642486 !'##experimental_source testis REFERENCE A91992 !$#authors Abe, K.; Kimura, S.; Kizawa, R.; Anan, F.K.; Sugita, Y. !$#journal J. Biochem. (1985) 97:1659-1668 !$#title Amino acid sequences of cytochrome b5 from human, porcine, !1and bovine erythrocytes and comparison with liver microsomal !1cytochrome b5. !$#cross-references MUID:85289161; PMID:4030743 !$#contents sequence revisions !$#accession C24211 !'##molecule_type protein !'##residues 2-134 ##label ABE REFERENCE S04976 !$#authors Ozols, J. !$#journal Biochim. Biophys. Acta (1989) 997:121-130 !$#title Structure of cytochrome b(5) and its topology in the !1microsomal membrane. !$#cross-references MUID:89323209; PMID:2752049 !$#accession S07962 !'##molecule_type protein !'##residues 2-134 ##label OZO1 REFERENCE A90383 !$#authors Ozols, J. !$#journal Biochemistry (1974) 13:426-434 !$#title Cytochrome beta-5 from microsomal membranes of equine, !1bovine, and porcine livers. Isolation and properties of !1preparations containing the membranous segment. !$#cross-references MUID:74080219; PMID:4810060 !$#accession B90383 !'##molecule_type protein !'##residues 'ZZDAS',7 ##label OZO2 REFERENCE A92077 !$#authors Nobrega, F.G.; Ozols, J. !$#journal J. Biol. Chem. (1971) 246:1706-1717 !$#title Amino acid sequences of tryptic peptides of cytochromes b-5 !1from microsomes of human, monkey, porcine, and chicken !1liver. !$#cross-references MUID:71134790; PMID:4993957 !$#accession B92077 !'##molecule_type protein !'##residues 8-14,'ZZ',17,'Z',19-89 ##label NOB REFERENCE A93813 !$#authors Ozols, J.; Gerard, C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1977) 74:3725-3729 !$#title Primary structure of the membranous segment of cytochrome !1b-5. !$#cross-references MUID:78012290; PMID:269425 !$#accession A93813 !'##molecule_type protein !'##residues 15-16;'D';90-134 ##label OZO3 !'##note the residue 62 was identified as Asp CLASSIFICATION #superfamily cytochrome b5; cytochrome b5 core homology KEYWORDS acetylated amino end; alternative splicing; chromoprotein; !1electron transfer; heme; iron; liver; metalloprotein FEATURE !$9-84 #domain cytochrome b5 core homology #label CB5\ !$109-130 #domain transmembrane #status predicted #label TRM\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental\ !$44,68 #binding_site heme iron (His) (axial ligands) #status !8predicted SUMMARY #length 134 #molecular-weight 15310 #checksum 732 SEQUENCE /// ENTRY JC5783 #type complete TITLE cytochrome b5, erythrocyte splice form [validated] - pig ALTERNATE_NAMES soluble cytochrome b5 ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 19-May-2000 ACCESSIONS JC5783; D24211 REFERENCE JC5782 !$#authors VanDerMark, P.K.; Steggles, A.W. !$#journal Biochem. Biophys. Res. Commun. (1997) 240:80-83 !$#title The isolation and characterization of the soluble and !1membrane-bound porcine cytochrome b5 cDNAs. !$#cross-references MUID:98042520; PMID:9367886 !$#accession JC5783 !'##molecule_type mRNA !'##residues 1-98 ##label VAN !'##cross-references GB:AF016389; NID:g2642487; PIDN:AAC48780.1; !1PID:g2642488 !'##experimental_source testis !'##note this splice form is not completely annotated in GenBank entry !1AF016389, release 113.0 REFERENCE A91992 !$#authors Abe, K.; Kimura, S.; Kizawa, R.; Anan, F.K.; Sugita, Y. !$#journal J. Biochem. (1985) 97:1659-1668 !$#title Amino acid sequences of cytochrome b5 from human, porcine, !1and bovine erythrocytes and comparison with liver microsomal !1cytochrome b5. !$#cross-references MUID:85289161; PMID:4030743 !$#accession D24211 !'##molecule_type protein !'##residues 2-98 ##label ABE CLASSIFICATION #superfamily cytochrome b5; cytochrome b5 core homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; liver; metalloprotein FEATURE !$9-84 #domain cytochrome b5 core homology #label CB5\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental\ !$44,68 #binding_site heme iron (His) (axial ligands) #status !8predicted SUMMARY #length 98 #molecular-weight 11153 #checksum 9220 SEQUENCE /// ENTRY CBRT5 #type complete TITLE cytochrome b5, microsomal splice form [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 15-Oct-1982 #sequence_revision 31-Dec-1992 #text_change 16-Jun-2000 ACCESSIONS S28404; A00172; A23338; JC5597; JS0745; S07960 REFERENCE S28404 !$#authors Mitoma, J.; Ito, A. !$#journal EMBO J. (1992) 11:4197-4203 !$#title The carboxy-terminal 10 amino acid residues of cytochrome b !1(5) are necessary for its targeting to the endoplasmic !1reticulum. !$#cross-references MUID:93011015; PMID:1396600 !$#accession S28404 !'##molecule_type mRNA !'##residues 1-134 ##label MIT !'##cross-references EMBL:D13205; NID:g220729; PIDN:BAA02492.1; !1PID:g220730 REFERENCE A00172 !$#authors Ozols, J.; Heinemann, F.S. !$#journal Biochim. Biophys. Acta (1982) 704:163-173 !$#title Chemical structure of rat liver cytochrome b-5. Isolation of !1peptides by high-pressure liquid chromatography. !$#cross-references MUID:82232110; PMID:7093287 !$#accession A00172 !'##molecule_type protein !'##residues 2-134 ##label OZO REFERENCE A91128 !$#authors Lederer, F.; Ghrir, R.; Guiard, B.; Cortial, S.; Ito, A. !$#journal Eur. J. Biochem. (1983) 132:95-102 !$#title Two homologous cytochromes b-5 in a single cell. !$#cross-references MUID:83182449; PMID:6840088 !$#accession A23338 !'##molecule_type protein !'##residues 7,'B',9-17,'E',19-89 ##label LED REFERENCE JC5596 !$#authors Yoo, M. !$#journal Biochem. Biophys. Res. Commun. (1997) 236:641-642 !$#title Identification of two homologous cytochrome b5s in rat !1brain. !$#cross-references MUID:97396150; PMID:9245704 !$#accession JC5597 !'##molecule_type mRNA !'##residues 1-134 ##label YOO !'##cross-references DDBJ:AF007108; NID:g2257956; PIDN:AAB67610.1; !1PID:g2257957 !'##experimental_source brain COMMENT This protein is a small heme-containing protein which !1supplies electrons for many cytochrome P450 catalyzed !1reactions in the liver and for the reduction of !1methemoglobin in erythrocyte cell. CLASSIFICATION #superfamily cytochrome b5; cytochrome b5 core homology KEYWORDS acetylated amino end; alternative splicing; chromoprotein; !1electron transfer; heme; iron; membrane protein; !1metalloprotein FEATURE !$2-134 #product cytochrome b5 #status experimental #label !8MAT\ !$9-84 #domain cytochrome b5 core homology #label CB5\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental\ !$44,68 #binding_site heme iron (His) (axial ligands) #status !8predicted SUMMARY #length 134 #molecular-weight 15355 #checksum 578 SEQUENCE /// ENTRY CBRT5M #type complete TITLE cytochrome b5, outer mitochondrial membrane - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 04-Dec-1986 #sequence_revision 29-Aug-1997 #text_change 16-Jun-2000 ACCESSIONS A00173; S66501 REFERENCE A91128 !$#authors Lederer, F.; Ghrir, R.; Guiard, B.; Cortial, S.; Ito, A. !$#journal Eur. J. Biochem. (1983) 132:95-102 !$#title Two homologous cytochromes b-5 in a single cell. !$#cross-references MUID:83182449; PMID:6840088 !$#accession A00173 !'##molecule_type protein !'##residues 1-92 ##label LED REFERENCE S66501 !$#authors de Silvestris, M.; D'Arrigo, A.; Borgese, N. !$#journal FEBS Lett. (1995) 370:69-74 !$#title The targeting information of the mitochondrial outer !1membrane isoform of cytochrome b(5) is contained within the !1carboxyl-terminal region. !$#cross-references MUID:95377460; PMID:7649306 !$#accession S66501 !'##molecule_type mRNA !'##residues 32-135 ##label DES !'##cross-references GB:X96392; EMBL:S79339; NID:g1217654; !1PIDN:CAA65256.1; PID:g1217655 COMMENT Cytochrome b5, found attached to various hepatic cell !1membranes, is a major component of the electron transport !1system, catalyzing the NADH-linked desaturation of fatty !1acids in the endoplasmic reticulum. It may also be involved !1in the NADH-linked pathway of drug hydroxylation reactions !1catalyzed by cytochrome p450. GENETICS !$#genome nuclear CLASSIFICATION #superfamily cytochrome b5; cytochrome b5 core homology KEYWORDS chromoprotein; electron transfer; heme; iron; membrane !1protein; metalloprotein; mitochondrion FEATURE !$1-92 #domain heme binding #status predicted #label HMB\ !$9-84 #domain cytochrome b5 core homology #label CB5\ !$44,68 #binding_site heme iron (His) (axial ligands) #status !8predicted SUMMARY #length 135 #molecular-weight 15221 #checksum 281 SEQUENCE /// ENTRY CBCH5 #type complete TITLE cytochrome b5 precursor - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 24-Apr-1984 #sequence_revision 10-Nov-1995 #text_change 03-Mar-2000 ACCESSIONS A28811; S10746; S04977; A00174 REFERENCE A28811 !$#authors Zhang, H.; Somerville, C. !$#journal Arch. Biochem. Biophys. (1988) 264:343-347 !$#title The primary structure of chicken liver cytochrome b-5 !1deduced from the DNA sequence of a cDNA clone. !$#cross-references MUID:88280278; PMID:3395128 !$#accession A28811 !'##molecule_type mRNA !'##residues 1-138 ##label ZHA !'##cross-references GB:M18539; NID:g211692; PIDN:AAA48733.1; !1PID:g211693 REFERENCE S10746 !$#authors Zhang, H.; Somerville, C. !$#journal Arch. Biochem. Biophys. (1990) 280:412-415 !$#title Soluble and membrane-bound forms of cytochrome b5 are the !1products of a single gene in chicken. !$#cross-references MUID:90314412; PMID:2369133 !$#accession S10746 !'##molecule_type mRNA !'##residues 1-138 ##label ZH2 !'##cross-references EMBL:M32293; NID:g211706; PIDN:AAA48740.1; !1PID:g211707 REFERENCE S04976 !$#authors Ozols, J. !$#journal Biochim. Biophys. Acta (1989) 997:121-130 !$#title Structure of cytochrome b(5) and its topology in the !1microsomal membrane. !$#cross-references MUID:89323209; PMID:2752049 !$#accession S04977 !'##molecule_type protein !'##residues 4-11,'E',13-113,'W',115-123,'T',125-138,'E' ##label OZO REFERENCE A92077 !$#authors Nobrega, F.G.; Ozols, J. !$#journal J. Biol. Chem. (1971) 246:1706-1717 !$#title Amino acid sequences of tryptic peptides of cytochromes b-5 !1from microsomes of human, monkey, porcine, and chicken !1liver. !$#cross-references MUID:71134790; PMID:4993957 !$#accession A00174 !'##molecule_type protein !'##residues 14-26,'Z',28,'B',30-66,'D',68-97 ##label NOB CLASSIFICATION #superfamily cytochrome b5; cytochrome b5 core homology KEYWORDS acetylated amino end; chromoprotein; electron transfer; !1heme; iron; membrane protein; metalloprotein FEATURE !$7-138 #product cytochrome b5 #status experimental #label !8MAT\ !$14-89 #domain cytochrome b5 core homology #label CB5\ !$7 #modified_site acetylated amino end (Ala) (in mature !8form) #status predicted\ !$49,73 #binding_site heme iron (His) (axial ligands) #status !8predicted SUMMARY #length 138 #molecular-weight 15545 #checksum 6736 SEQUENCE /// ENTRY S44303 #type complete TITLE phenol 2-monooxygenase (EC 1.14.13.7) component K - Pseudomonas putida ALTERNATE_NAMES phenolhydroxylase chain A ORGANISM #formal_name Pseudomonas putida DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A58972; S54768; S44303; S47414 REFERENCE A58972 !$#authors Ng, L.C.; Shingler, V.; Sze, C.C.; Poh, C.L. !$#journal Gene (1994) 151:29-36 !$#title Cloning and sequences of the first eight genes of the !1chromosomally encoded (methyl) phenol degradation pathway !1from Pseudomonas putida P35X. !$#cross-references MUID:95129877; PMID:7828892 !$#accession A58972 !'##status preliminary !'##molecule_type DNA !'##residues 1-92 ##label NGL !'##cross-references EMBL:X79063; NID:g483477; PIDN:CAA55660.1; !1PID:g483478 !'##experimental_source strain P35X (NCBI 9869) !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1994 REFERENCE S54761 !$#authors Herrmann, H.; Mueller, C.; Schmidt, I.; Mahnke, J.; !1Petruschka, L.; Hahnke, K. !$#journal Mol. Gen. Genet. (1995) 247:240-246 !$#title Localization and organization of phenol degradation genes of !1Pseudomonas putida strain H. !$#cross-references MUID:95272534; PMID:7753034 !$#accession S54768 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-87,'L',89-92 ##label HE2 !'##cross-references EMBL:X80765; NID:g527546; PIDN:CAA56740.1; !1PID:g527547 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1994 GENETICS !$#gene phlA; phhK CLASSIFICATION #superfamily phenol 2-monooxygenase component K KEYWORDS oxidoreductase SUMMARY #length 92 #molecular-weight 10590 #checksum 1373 SEQUENCE /// ENTRY A37831 #type complete TITLE phenol 2-monooxygenase (EC 1.14.13.7) chain P0 - Pseudomonas sp. (strain CF600) ORGANISM #formal_name Pseudomonas sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A37831 REFERENCE A37831 !$#authors Nordlund, I.; Powlowski, J.; Shingler, V. !$#journal J. Bacteriol. (1990) 172:6826-6833 !$#title Complete nucleotide sequence and polypeptide analysis of !1multicomponent phenol hydroxylase from Pseudomonas sp. !1strain CF600. !$#cross-references MUID:91072230; PMID:2254258 !$#accession A37831 !'##status preliminary !'##molecule_type DNA !'##residues 1-92 ##label NOR !'##cross-references GB:M60276; GB:M37764; NID:g151449; PIDN:AAA25939.1; !1PID:g151450 CLASSIFICATION #superfamily phenol 2-monooxygenase component K KEYWORDS oxidoreductase SUMMARY #length 92 #molecular-weight 10586 #checksum 1390 SEQUENCE /// ENTRY S47287 #type complete TITLE phenol 2-monooxygenase (EC 1.14.13.7) chain mopK - Acinetobacter calcoaceticus ALTERNATE_NAMES phenol hydroxylase ORGANISM #formal_name Acinetobacter calcoaceticus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S70080; S47287 REFERENCE S70080 !$#authors Ehrt, S.; Schirmer, F.; Hillen, W. !$#journal Mol. Microbiol. (1995) 18:13-20 !$#title Genetic organization, nucleotide sequence and regulation of !1expression of genes encoding phenol hydroxylase and catechol !11,2-dioxygenase in Acinetobacter calcoaceticus NCIB8250. !$#cross-references MUID:96154937; PMID:8596453 !$#accession S70080 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-96 ##label EH2 !'##cross-references EMBL:Z36909; NID:g535279; PIDN:CAA85380.1; !1PID:g535280 !'##experimental_source strain NCIB8250 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1September 1994 GENETICS !$#gene mopK CLASSIFICATION #superfamily phenol 2-monooxygenase component K KEYWORDS aromatic hydrocarbon catabolism; oxidoreductase SUMMARY #length 96 #molecular-weight 11274 #checksum 3101 SEQUENCE /// ENTRY S44304 #type complete TITLE phenol 2-monooxygenase (EC 1.14.13.7) component L - Pseudomonas putida ALTERNATE_NAMES phenolhydroxylase chain B ORGANISM #formal_name Pseudomonas putida DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C58972; S54767; S44304; S47415 REFERENCE A58972 !$#authors Ng, L.C.; Shingler, V.; Sze, C.C.; Poh, C.L. !$#journal Gene (1994) 151:29-36 !$#title Cloning and sequences of the first eight genes of the !1chromosomally encoded (methyl) phenol degradation pathway !1from Pseudomonas putida P35X. !$#cross-references MUID:95129877; PMID:7828892 !$#accession C58972 !'##status preliminary !'##molecule_type DNA !'##residues 1-331 ##label NGL !'##cross-references EMBL:X79063; NID:g483477; PIDN:CAA55661.1; !1PID:g483479 !'##experimental_source strain P35X (NCBI 9869) !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1994 REFERENCE S54761 !$#authors Herrmann, H.; Mueller, C.; Schmidt, I.; Mahnke, J.; !1Petruschka, L.; Hahnke, K. !$#journal Mol. Gen. Genet. (1995) 247:240-246 !$#title Localization and organization of phenol degradation genes of !1Pseudomonas putida strain H. !$#cross-references MUID:95272534; PMID:7753034 !$#accession S54767 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 'MGIQQQEGTVD',1-8,'T',10-57,'R',59-86,'G',88-331 ##label !1HE2 !'##cross-references EMBL:X80765; NID:g527546; PIDN:CAA56741.1; !1PID:g527548 !'##experimental_source strain H !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1994 GENETICS !$#gene phlB; phhL CLASSIFICATION #superfamily phenol 2-monooxygenase component L KEYWORDS oxidoreductase SUMMARY #length 331 #molecular-weight 38178 #checksum 1758 SEQUENCE /// ENTRY B37831 #type complete TITLE phenol 2-monooxygenase (EC 1.14.13.7) chain P1 - Pseudomonas sp. (strain CF600) ORGANISM #formal_name Pseudomonas sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B37831 REFERENCE A37831 !$#authors Nordlund, I.; Powlowski, J.; Shingler, V. !$#journal J. Bacteriol. (1990) 172:6826-6833 !$#title Complete nucleotide sequence and polypeptide analysis of !1multicomponent phenol hydroxylase from Pseudomonas sp. !1strain CF600. !$#cross-references MUID:91072230; PMID:2254258 !$#accession B37831 !'##status preliminary !'##molecule_type DNA !'##residues 1-331 ##label NOR !'##cross-references GB:M60276; GB:M37764; NID:g151449; PIDN:AAA25940.1; !1PID:g151451 CLASSIFICATION #superfamily phenol 2-monooxygenase component L KEYWORDS oxidoreductase SUMMARY #length 331 #molecular-weight 38208 #checksum 1929 SEQUENCE /// ENTRY S47288 #type complete TITLE phenol 2-monooxygenase (EC 1.14.13.7) chain mopL - Acinetobacter calcoaceticus ALTERNATE_NAMES phenol hydroxylase ORGANISM #formal_name Acinetobacter calcoaceticus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S70081; S47288 REFERENCE S70080 !$#authors Ehrt, S.; Schirmer, F.; Hillen, W. !$#journal Mol. Microbiol. (1995) 18:13-20 !$#title Genetic organization, nucleotide sequence and regulation of !1expression of genes encoding phenol hydroxylase and catechol !11,2-dioxygenase in Acinetobacter calcoaceticus NCIB8250. !$#cross-references MUID:96154937; PMID:8596453 !$#accession S70081 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-333 ##label EH2 !'##cross-references EMBL:Z36909; NID:g535279; PIDN:CAA85381.1; !1PID:g535281 !'##experimental_source strain NCIB8250 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1September 1994 GENETICS !$#gene mopL CLASSIFICATION #superfamily phenol 2-monooxygenase component L KEYWORDS aromatic hydrocarbon catabolism; oxidoreductase SUMMARY #length 333 #molecular-weight 38382 #checksum 312 SEQUENCE /// ENTRY S44305 #type complete TITLE phenol 2-monooxygenase (EC 1.14.13.7) component M - Pseudomonas putida ALTERNATE_NAMES phenolhydroxylase chain C ORGANISM #formal_name Pseudomonas putida DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS D58972; S54766; S44305; S47416 REFERENCE A58972 !$#authors Ng, L.C.; Shingler, V.; Sze, C.C.; Poh, C.L. !$#journal Gene (1994) 151:29-36 !$#title Cloning and sequences of the first eight genes of the !1chromosomally encoded (methyl) phenol degradation pathway !1from Pseudomonas putida P35X. !$#cross-references MUID:95129877; PMID:7828892 !$#accession D58972 !'##status preliminary !'##molecule_type DNA !'##residues 1-90 ##label NGL !'##cross-references EMBL:X79063; NID:g483477; PIDN:CAA55662.1; !1PID:g483480 !'##experimental_source strain P35X (NCBI 9869) !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1994 REFERENCE S54761 !$#authors Herrmann, H.; Mueller, C.; Schmidt, I.; Mahnke, J.; !1Petruschka, L.; Hahnke, K. !$#journal Mol. Gen. Genet. (1995) 247:240-246 !$#title Localization and organization of phenol degradation genes of !1Pseudomonas putida strain H. !$#cross-references MUID:95272534; PMID:7753034 !$#accession S54766 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-41,'V',43-55,'K',57-76,'V',78-90,'N' ##label HE2 !'##cross-references EMBL:X80765; NID:g527546; PIDN:CAA56742.1; !1PID:g527549 !'##experimental_source strain H !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1994 GENETICS !$#gene phlC; phhM CLASSIFICATION #superfamily phenol 2-monooxygenase component M KEYWORDS oxidoreductase SUMMARY #length 90 #molecular-weight 10519 #checksum 6722 SEQUENCE /// ENTRY C37831 #type complete TITLE phenol 2-monooxygenase (EC 1.14.13.7) chain P2 - Pseudomonas sp. (strain CF600) ORGANISM #formal_name Pseudomonas sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C37831 REFERENCE A37831 !$#authors Nordlund, I.; Powlowski, J.; Shingler, V. !$#journal J. Bacteriol. (1990) 172:6826-6833 !$#title Complete nucleotide sequence and polypeptide analysis of !1multicomponent phenol hydroxylase from Pseudomonas sp. !1strain CF600. !$#cross-references MUID:91072230; PMID:2254258 !$#accession C37831 !'##status preliminary !'##molecule_type DNA !'##residues 1-90 ##label NOR !'##cross-references GB:M60276; GB:M37764; NID:g151449; PIDN:AAA25941.1; !1PID:g151452 CLASSIFICATION #superfamily phenol 2-monooxygenase component M KEYWORDS oxidoreductase SUMMARY #length 90 #molecular-weight 10491 #checksum 7162 SEQUENCE /// ENTRY S47289 #type complete TITLE phenol 2-monooxygenase (EC 1.14.13.7) chain mopM - Acinetobacter calcoaceticus ALTERNATE_NAMES phenol hydroxylase ORGANISM #formal_name Acinetobacter calcoaceticus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S70082; S47289 REFERENCE S70080 !$#authors Ehrt, S.; Schirmer, F.; Hillen, W. !$#journal Mol. Microbiol. (1995) 18:13-20 !$#title Genetic organization, nucleotide sequence and regulation of !1expression of genes encoding phenol hydroxylase and catechol !11,2-dioxygenase in Acinetobacter calcoaceticus NCIB8250. !$#cross-references MUID:96154937; PMID:8596453 !$#accession S70082 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-89 ##label EH2 !'##cross-references EMBL:Z36909; NID:g535279; PIDN:CAA85382.1; !1PID:g535282 !'##experimental_source strain NCIB8250 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1September 1994 GENETICS !$#gene mopM CLASSIFICATION #superfamily phenol 2-monooxygenase component M KEYWORDS aromatic hydrocarbon catabolism; oxidoreductase SUMMARY #length 89 #molecular-weight 10136 #checksum 7100 SEQUENCE /// ENTRY S44306 #type complete TITLE phenol 2-monooxygenase (EC 1.14.13.7) component N - Pseudomonas putida ALTERNATE_NAMES phenolhydroxylase chain D ORGANISM #formal_name Pseudomonas putida DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS E58972; S54765; S44306; S47417 REFERENCE A58972 !$#authors Ng, L.C.; Shingler, V.; Sze, C.C.; Poh, C.L. !$#journal Gene (1994) 151:29-36 !$#title Cloning and sequences of the first eight genes of the !1chromosomally encoded (methyl) phenol degradation pathway !1from Pseudomonas putida P35X. !$#cross-references MUID:95129877; PMID:7828892 !$#accession E58972 !'##status preliminary !'##molecule_type DNA !'##residues 1-516 ##label NGL !'##cross-references EMBL:X79063; NID:g483477; PIDN:CAA55663.1; !1PID:g483481 !'##experimental_source strain P35X (NCBI 9869) !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1994 REFERENCE S54761 !$#authors Herrmann, H.; Mueller, C.; Schmidt, I.; Mahnke, J.; !1Petruschka, L.; Hahnke, K. !$#journal Mol. Gen. Genet. (1995) 247:240-246 !$#title Localization and organization of phenol degradation genes of !1Pseudomonas putida strain H. !$#cross-references MUID:95272534; PMID:7753034 !$#accession S54765 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-63,'H',65-100,'F',102-106,'M',108-137,'EL',140-512,'Q', !1514-516 ##label HE2 !'##cross-references EMBL:X80765; NID:g527546; PIDN:CAA56743.1; !1PID:g527550 !'##experimental_source strain H !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1994 GENETICS !$#gene phlD; phhN CLASSIFICATION #superfamily phenol 2-monooxygenase component N KEYWORDS oxidoreductase SUMMARY #length 516 #molecular-weight 60381 #checksum 6497 SEQUENCE /// ENTRY D37831 #type complete TITLE phenol 2-monooxygenase (EC 1.14.13.7) chain P3 - Pseudomonas sp. (strain CF600) ORGANISM #formal_name Pseudomonas sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS D37831 REFERENCE A37831 !$#authors Nordlund, I.; Powlowski, J.; Shingler, V. !$#journal J. Bacteriol. (1990) 172:6826-6833 !$#title Complete nucleotide sequence and polypeptide analysis of !1multicomponent phenol hydroxylase from Pseudomonas sp. !1strain CF600. !$#cross-references MUID:91072230; PMID:2254258 !$#accession D37831 !'##status preliminary !'##molecule_type DNA !'##residues 1-517 ##label NOR !'##cross-references GB:M60276; GB:M37764; NID:g151449; PIDN:AAA25942.1; !1PID:g151453 CLASSIFICATION #superfamily phenol 2-monooxygenase component N KEYWORDS oxidoreductase SUMMARY #length 517 #molecular-weight 60522 #checksum 6342 SEQUENCE /// ENTRY S47290 #type complete TITLE phenol 2-monooxygenase (EC 1.14.13.7) chain mopN - Acinetobacter calcoaceticus ALTERNATE_NAMES phenol hydroxylase ORGANISM #formal_name Acinetobacter calcoaceticus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S70083; S47290 REFERENCE S70080 !$#authors Ehrt, S.; Schirmer, F.; Hillen, W. !$#journal Mol. Microbiol. (1995) 18:13-20 !$#title Genetic organization, nucleotide sequence and regulation of !1expression of genes encoding phenol hydroxylase and catechol !11,2-dioxygenase in Acinetobacter calcoaceticus NCIB8250. !$#cross-references MUID:96154937; PMID:8596453 !$#accession S70083 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-511 ##label EH2 !'##cross-references EMBL:Z36909; NID:g535279; PIDN:CAA85383.1; !1PID:g535283 !'##experimental_source strain NCIB8250 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1September 1994 GENETICS !$#gene mopN CLASSIFICATION #superfamily phenol 2-monooxygenase component N KEYWORDS aromatic hydrocarbon catabolism; oxidoreductase SUMMARY #length 511 #molecular-weight 60316 #checksum 537 SEQUENCE /// ENTRY S44307 #type complete TITLE phenol 2-monooxygenase (EC 1.14.13.7) component O - Pseudomonas putida ALTERNATE_NAMES phenolhydroxylase chain E ORGANISM #formal_name Pseudomonas putida DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS F58972; S54764; S44307; S47418 REFERENCE A58972 !$#authors Ng, L.C.; Shingler, V.; Sze, C.C.; Poh, C.L. !$#journal Gene (1994) 151:29-36 !$#title Cloning and sequences of the first eight genes of the !1chromosomally encoded (methyl) phenol degradation pathway !1from Pseudomonas putida P35X. !$#cross-references MUID:95129877; PMID:7828892 !$#accession F58972 !'##status preliminary !'##molecule_type DNA !'##residues 1-119 ##label NGL !'##cross-references EMBL:X79063; NID:g483477; PIDN:CAA55664.1; !1PID:g483482 !'##experimental_source strain P35X (NCBI 9869) !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1994 REFERENCE S54761 !$#authors Herrmann, H.; Mueller, C.; Schmidt, I.; Mahnke, J.; !1Petruschka, L.; Hahnke, K. !$#journal Mol. Gen. Genet. (1995) 247:240-246 !$#title Localization and organization of phenol degradation genes of !1Pseudomonas putida strain H. !$#cross-references MUID:95272534; PMID:7753034 !$#accession S54764 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-9,'T',11-40,'G',42-119 ##label HE2 !'##cross-references EMBL:X80765; NID:g527546; PIDN:CAA56744.1; !1PID:g527551 !'##experimental_source strain H !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1994 GENETICS !$#gene phlE; phhO CLASSIFICATION #superfamily phenol 2-monooxygenase component O KEYWORDS oxidoreductase SUMMARY #length 119 #molecular-weight 13231 #checksum 540 SEQUENCE /// ENTRY E37831 #type complete TITLE phenol 2-monooxygenase (EC 1.14.13.7) chain P4 - Pseudomonas sp. (strain CF600) ORGANISM #formal_name Pseudomonas sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS E37831 REFERENCE A37831 !$#authors Nordlund, I.; Powlowski, J.; Shingler, V. !$#journal J. Bacteriol. (1990) 172:6826-6833 !$#title Complete nucleotide sequence and polypeptide analysis of !1multicomponent phenol hydroxylase from Pseudomonas sp. !1strain CF600. !$#cross-references MUID:91072230; PMID:2254258 !$#accession E37831 !'##status preliminary !'##molecule_type DNA !'##residues 1-119 ##label NOR !'##cross-references GB:M60276; GB:M37764; NID:g151449; PIDN:AAA25943.1; !1PID:g151454 CLASSIFICATION #superfamily phenol 2-monooxygenase component O KEYWORDS oxidoreductase SUMMARY #length 119 #molecular-weight 13207 #checksum 489 SEQUENCE /// ENTRY S47291 #type complete TITLE phenol 2-monooxygenase (EC 1.14.13.7) chain mopO - Acinetobacter calcoaceticus ALTERNATE_NAMES phenol hydroxylase ORGANISM #formal_name Acinetobacter calcoaceticus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S70084; S47291 REFERENCE S70080 !$#authors Ehrt, S.; Schirmer, F.; Hillen, W. !$#journal Mol. Microbiol. (1995) 18:13-20 !$#title Genetic organization, nucleotide sequence and regulation of !1expression of genes encoding phenol hydroxylase and catechol !11,2-dioxygenase in Acinetobacter calcoaceticus NCIB8250. !$#cross-references MUID:96154937; PMID:8596453 !$#accession S70084 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-120 ##label EH2 !'##cross-references EMBL:Z36909; NID:g535279; PIDN:CAA85384.1; !1PID:g535284 !'##experimental_source strain NCIB8250 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1September 1994 GENETICS !$#gene mopO CLASSIFICATION #superfamily phenol 2-monooxygenase component O KEYWORDS aromatic hydrocarbon catabolism; oxidoreductase SUMMARY #length 120 #molecular-weight 13848 #checksum 430 SEQUENCE /// ENTRY S44308 #type complete TITLE phenol 2-monooxygenase (EC 1.14.13.7) reductase component - Pseudomonas putida ALTERNATE_NAMES phenol hydroxylase P1 component; phenolhydroxylase chain F ORGANISM #formal_name Pseudomonas putida DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS G58972; S54763; S44308; S47419 REFERENCE A58972 !$#authors Ng, L.C.; Shingler, V.; Sze, C.C.; Poh, C.L. !$#journal Gene (1994) 151:29-36 !$#title Cloning and sequences of the first eight genes of the !1chromosomally encoded (methyl) phenol degradation pathway !1from Pseudomonas putida P35X. !$#cross-references MUID:95129877; PMID:7828892 !$#accession G58972 !'##status preliminary !'##molecule_type DNA !'##residues 1-353 ##label NGL !'##cross-references EMBL:X79063; NID:g483477; PIDN:CAA55665.1; !1PID:g483483 !'##experimental_source strain P35X (NCBI 9869) !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1994 REFERENCE S54761 !$#authors Herrmann, H.; Mueller, C.; Schmidt, I.; Mahnke, J.; !1Petruschka, L.; Hahnke, K. !$#journal Mol. Gen. Genet. (1995) 247:240-246 !$#title Localization and organization of phenol degradation genes of !1Pseudomonas putida strain H. !$#cross-references MUID:95272534; PMID:7753034 !$#accession S54763 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-8,'P',10-35,'A',37-79,'M',81-144,'I',146-176,'G',178-201, !1'G',203-223,'V',225-227,'LAQ',231-353 ##label HE2 !'##cross-references EMBL:X80765; NID:g527546; PIDN:CAA56745.1; !1PID:g527552 !'##experimental_source strain H !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1994 GENETICS !$#gene phlF; phhP CLASSIFICATION #superfamily methane monooxygenase reductase component; !1cytochrome-b5 reductase homology; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; flavoprotein; iron-sulfur protein; metalloprotein; !1oxidoreductase FEATURE !$22-78 #domain ferredoxin [2Fe-2S] homology #label FER\ !$109-334 #domain cytochrome-b5 reductase homology #label CBR\ !$37,42,45,77 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 353 #molecular-weight 38674 #checksum 6615 SEQUENCE /// ENTRY S65531 #type complete TITLE sodium-translocating NADH dehydrogenase (ubiquinone) (EC 1.6.5.-) nqrF chain - Vibrio alginolyticus ORGANISM #formal_name Vibrio alginolyticus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Sep-2000 ACCESSIONS S65531 REFERENCE S65528 !$#authors Hayashi, M.; Hirai, K.; Unemoto, T. !$#journal FEBS Lett. (1995) 363:75-77 !$#title Sequencing and the alignment of structural genes in the nqr !1operon encoding the Na(+)-translocating NADH-quinone !1reductase from Vibrio alginolyticus. !$#cross-references MUID:95246889; PMID:7729558 !$#accession S65531 !'##status preliminary !'##molecule_type DNA !'##residues 1-407 ##label HAY !'##cross-references EMBL:D49364; NID:g2558472; PIDN:BAA22915.1; !1PID:g2558478 GENETICS !$#gene nqr6 CLASSIFICATION #superfamily methane monooxygenase reductase component; !1cytochrome-b5 reductase homology; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; flavoprotein; iron-sulfur protein; metalloprotein; !1oxidoreductase FEATURE !$54-111 #domain ferredoxin [2Fe-2S] homology #label FER\ !$136-405 #domain cytochrome-b5 reductase homology #label CBR\ !$69,75,78,110 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 407 #molecular-weight 45274 #checksum 2064 SEQUENCE /// ENTRY A36952 #type complete TITLE CDP-6-deoxy-Delta(3,4)-glucoseen reductase (EC 1.3.1.-) - Yersinia pseudotuberculosis ORGANISM #formal_name Yersinia pseudotuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A36952; B47070 REFERENCE A36952 !$#authors Lo, S.F.; Miller, V.P.; Lei, Y.; Thorson, J.S.; Liu, H.W.; !1Schottel, J.L. !$#journal J. Bacteriol. (1994) 176:460-468 !$#title CDP-6-deoxy-delta(3,4)-glucoseen reductase from Yersinia !1pseudotuberculosis: enzyme purification and characterization !1of the cloned gene. !$#cross-references MUID:94117382; PMID:8288541 !$#accession A36952 !'##molecule_type DNA !'##residues 1-329 ##label LOA !'##cross-references GB:L25594; NID:g456127; PIDN:AAA16760.1; !1PID:g456128 REFERENCE A47070 !$#authors Kessler, A.C.; Haase, A.; Reeves, P.R. !$#journal J. Bacteriol. (1993) 175:1412-1422 !$#title Molecular analysis of the 3,6-dideoxyhexose pathway genes of !1Yersinia pseudotuberculosis serogroup IIA. !$#cross-references MUID:93186709; PMID:8444803 !$#accession B47070 !'##status preliminary !'##molecule_type DNA !'##residues 1-329 ##label KES !'##cross-references GB:L01777; NID:g896325; PIDN:AAB49398.1; !1PID:g155495 !'##experimental_source serogroup IIA, M85 !'##note sequence extracted from NCBI backbone (NCBIN:126815, !1NCBIP:126827) GENETICS !$#gene ascD CLASSIFICATION #superfamily methane monooxygenase reductase component; !1cytochrome-b5 reductase homology; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; flavoprotein; iron-sulfur protein; metalloprotein; !1oxidoreductase FEATURE !$22-76 #domain ferredoxin [2Fe-2S] homology #label FER\ !$105-325 #domain cytochrome-b5 reductase homology #label CBR\ !$37,42,45,75 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 329 #molecular-weight 36047 #checksum 8273 SEQUENCE /// ENTRY D64052 #type complete TITLE Na+-translocating NADH-ubiquinone oxidoreductase (EC 1.-.-.-) beta chain - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS D64052 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession D64052 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-411 ##label TIGR !'##cross-references GB:U32702; GB:L42023; NID:g1573118; !1PIDN:AAC21841.1; PID:g1573127; TIGR:HI0171 CLASSIFICATION #superfamily methane monooxygenase reductase component; !1cytochrome-b5 reductase homology; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; flavoprotein; iron-sulfur protein; metalloprotein; !1oxidoreductase FEATURE !$58-115 #domain ferredoxin [2Fe-2S] homology #label FER\ !$140-409 #domain cytochrome-b5 reductase homology #label CBR\ !$73,79,82,114 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 411 #molecular-weight 45705 #checksum 5333 SEQUENCE /// ENTRY S15303 #type complete TITLE probable CDP-6-deoxy-Delta(3,4)-glucoseen reductase (EC 1.3.1.-) - Salmonella typhimurium ALTERNATE_NAMES hypothetical protein 7.6 ORGANISM #formal_name Salmonella typhimurium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S15303 REFERENCE S15296 !$#authors Jiang, X.M.; Neal, B.; Santiago, F.; Lee, S.J.; Romana, !1L.K.; Reeves, P.R. !$#journal Mol. Microbiol. (1991) 5:695-713 !$#title Structure and sequence of the rfb (O antigen) gene cluster !1of Salmonella serovar typhimurium (strain LT2). !$#cross-references MUID:91260454; PMID:1710759 !$#accession S15303 !'##status preliminary !'##molecule_type DNA !'##residues 1-330 ##label MOL CLASSIFICATION #superfamily methane monooxygenase reductase component; !1cytochrome-b5 reductase homology; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; iron-sulfur protein; metalloprotein; oxidoreductase FEATURE !$22-72 #domain ferredoxin [2Fe-2S] homology #label FER\ !$101-320 #domain cytochrome-b5 reductase homology #label CBR\ !$37,42,45,71 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 330 #molecular-weight 36582 #checksum 1548 SEQUENCE /// ENTRY S23479 #type complete TITLE probable benzoate 1,2-dioxygenase (EC 1.14.12.10) reductase component benC - Acinetobacter calcoaceticus ORGANISM #formal_name Acinetobacter calcoaceticus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S23479 REFERENCE S23477 !$#authors Neidle, E.L.; Hartnett, C.; Ornston, L.N.; Bairoch, A.; !1Rekik, M.; Harayama, S. !$#journal Eur. J. Biochem. (1992) 204:113-120 !$#title Cis-diol dehydrogenases encoded by the TOL pWW0 plasmid xylL !1gene and the Acinetobacter calcoaceticus chromosomal benD !1gene are members of the short-chain alcohol dehydrogenase !1superfamily. !$#cross-references MUID:92155191; PMID:1740120 !$#accession S23479 !'##status preliminary; translation not shown !'##molecule_type DNA !'##residues 1-338 ##label NEI !'##cross-references EMBL:M76990; NID:g141746; PID:g141749 CLASSIFICATION #superfamily methane monooxygenase reductase component; !1cytochrome-b5 reductase homology; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; flavoprotein; iron-sulfur protein; metalloprotein; !1oxidoreductase FEATURE !$26-84 #domain ferredoxin [2Fe-2S] homology #label FER\ !$113-335 #domain cytochrome-b5 reductase homology #label CBR\ !$41,46,49,83 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 338 #molecular-weight 37628 #checksum 5864 SEQUENCE /// ENTRY C48360 #type complete TITLE methane monooxygenase (EC 1.14.13.25) reductase chain - Methylosinus trichosporium ORGANISM #formal_name Methylosinus trichosporium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C48360; E39049 REFERENCE A48360 !$#authors Cardy, D.L.; Laidler, V.; Salmond, G.P.; Murrell, J.C. !$#journal Arch. Microbiol. (1991) 156:477-483 !$#title The methane monooxygenase gene cluster of Methylosinus !1trichosporium: cloning and sequencing of the mmoC gene. !$#cross-references MUID:92153031; PMID:1785954 !$#accession C48360 !'##status preliminary !'##molecule_type DNA !'##residues 1-340 ##label CAR !'##cross-references GB:S81887; NID:g245213; PIDN:AAB21393.1; !1PID:g245216 !'##experimental_source OB3b !'##note sequence extracted from NCBI backbone (NCBIN:81887, !1NCBIP:81915) REFERENCE A39049 !$#authors Fox, B.G.; Liu, Y.; Dege, J.E.; Lipscomb, J.D. !$#journal J. Biol. Chem. (1991) 266:540-550 !$#title Complex formation between the protein components of methane !1monooxygenase from Methylosinus trichosporium OB3b. !1Identification of sites of component interaction. !$#cross-references MUID:91093180; PMID:1845980 !$#accession E39049 !'##status preliminary !'##molecule_type protein !'##residues 1-13 ##label FOX CLASSIFICATION #superfamily methane monooxygenase reductase component; !1cytochrome-b5 reductase homology; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; flavoprotein; iron-sulfur protein; metalloprotein; !1oxidoreductase FEATURE !$21-77 #domain ferredoxin [2Fe-2S] homology #label FER\ !$108-336 #domain cytochrome-b5 reductase homology #label CBR\ !$37,41,44,76 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 340 #molecular-weight 37991 #checksum 9843 SEQUENCE /// ENTRY JQ0701 #type complete TITLE methane monooxygenase (EC 1.14.13.25) reductase component - Methylococcus capsulatus ORGANISM #formal_name Methylococcus capsulatus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JQ0701; PS0319 REFERENCE JQ0700 !$#authors Stainthorpe, A.C.; Lees, V.; Salmond, G.P.C.; Dalton, H.; !1Murrell, J.C. !$#journal Gene (1990) 91:27-34 !$#title The methane monooxygenase gene cluster of Methylococcus !1capsulatus (Bath). !$#cross-references MUID:90382694; PMID:2205538 !$#accession JQ0701 !'##molecule_type DNA !'##residues 1-348 ##label STA1 !'##cross-references GB:M90050; GB:M32314; NID:g149833; PIDN:AAB62391.1; !1PID:g2243160; GB:M58498; NID:g150022; PIDN:AAA25384.1; !1PID:g150025 !$#accession PS0319 !'##molecule_type protein !'##residues 1,'T',3-16 ##label STA2 COMMENT This multicomponent enzyme catalyzes the conversion of !1methane to methanol using molecular oxygen. GENETICS !$#gene mmoC CLASSIFICATION #superfamily methane monooxygenase reductase component; !1cytochrome-b5 reductase homology; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; flavoprotein; iron-sulfur protein; metalloprotein; !1oxidoreductase FEATURE !$27-83 #domain ferredoxin [2Fe-2S] homology #label FER\ !$113-342 #domain cytochrome-b5 reductase homology #label CBR\ !$42,47,50,82 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 348 #molecular-weight 38577 #checksum 2052 SEQUENCE /// ENTRY C41659 #type complete TITLE benzoate 1,2-dioxygenase (EC 1.14.12.10) reductase component - Pseudomonas putida plasmid TOL pWW0 ORGANISM #formal_name Pseudomonas putida DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C41659; S23484 REFERENCE A41659 !$#authors Harayama, S.; Rekik, M.; Bairoch, A.; Neidle, E.L.; Ornston, !1L.N. !$#journal J. Bacteriol. (1991) 173:7540-7548 !$#title Potential DNA slippage structures acquired during !1evolutionary divergence of Acinetobacter calcoaceticus !1chromosomal benABC and Pseudomonas putida TOL pWWO plasmid !1xylXYZ, genes encoding benzoate dioxygenases. !$#cross-references MUID:92041666; PMID:1938949 !$#accession C41659 !'##status preliminary !'##molecule_type DNA !'##residues 1-336 ##label HAR !'##cross-references GB:M64747; NID:g151718; PIDN:AAA26049.1; !1PID:g151721 REFERENCE S23477 !$#authors Neidle, E.L.; Hartnett, C.; Ornston, L.N.; Bairoch, A.; !1Rekik, M.; Harayama, S. !$#journal Eur. J. Biochem. (1992) 204:113-120 !$#title Cis-diol dehydrogenases encoded by the TOL pWW0 plasmid xylL !1gene and the Acinetobacter calcoaceticus chromosomal benD !1gene are members of the short-chain alcohol dehydrogenase !1superfamily. !$#cross-references MUID:92155191; PMID:1740120 !$#accession S23484 !'##status preliminary !'##molecule_type DNA !'##residues 1-336 ##label NEI !'##cross-references EMBL:M64747; NID:g151718; PIDN:AAA26049.1; !1PID:g151721 GENETICS !$#gene xylZ !$#genome plasmid CLASSIFICATION #superfamily methane monooxygenase reductase component; !1cytochrome-b5 reductase homology; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; flavoprotein; iron-sulfur protein; metalloprotein; !1oxidoreductase FEATURE !$25-82 #domain ferredoxin [2Fe-2S] homology #label FER\ !$111-332 #domain cytochrome-b5 reductase homology #label CBR\ !$40,45,48,81 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 336 #molecular-weight 36220 #checksum 5068 SEQUENCE /// ENTRY JN0640 #type complete TITLE naphthalene 1,2-dioxygenase (EC 1.14.12.12) reductase component - Pseudomonas putida (strain G7) ALTERNATE_NAMES nahAa protein ORGANISM #formal_name Pseudomonas putida DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Dec-1999 ACCESSIONS JN0640 REFERENCE JN0640 !$#authors Simon, M.J.; Osslund, T.D.; Saunders, R.; Ensley, B.D.; !1Suggs, S.; Harcourt, A.; Suen, W.; Cruden, D.L.; Gibson, !1D.T.; Zylstra, G.J. !$#journal Gene (1993) 127:31-37 !$#title Sequences of genes encoding naphthalene dioxygenase in !1Pseudomonas putida strains G7 and NCIB9816-4. !$#cross-references MUID:93252277; PMID:8486285 !$#accession JN0640 !'##molecule_type DNA !'##residues 1-328 ##label SIM !'##cross-references GB:M83949; NID:g151384; PIDN:AAA25900.1; !1PID:g151385 COMMENT This protein is a member of naphthalene dioxygenase !1multicomponent enzyme system, and is involved in the !1catabolism of naphthalene. GENETICS !$#gene nahAa CLASSIFICATION #superfamily methane monooxygenase reductase component; !1cytochrome-b5 reductase homology; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; flavoprotein; iron-sulfur protein; metalloprotein; !1oxidoreductase FEATURE !$20-74 #domain ferredoxin [2Fe-2S] homology #label FER\ !$103-323 #domain cytochrome-b5 reductase homology #label CBR\ !$35,40,43,73 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 328 #molecular-weight 35593 #checksum 1095 SEQUENCE /// ENTRY JN0642 #type complete TITLE naphthalene 1,2-dioxygenase (EC 1.14.12.12) reductase component - Pseudomonas putida (strain NCIB9816-4) ALTERNATE_NAMES nahAa protein ORGANISM #formal_name Pseudomonas putida DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Dec-1999 ACCESSIONS JN0642 REFERENCE JN0640 !$#authors Simon, M.J.; Osslund, T.D.; Saunders, R.; Ensley, B.D.; !1Suggs, S.; Harcourt, A.; Suen, W.; Cruden, D.L.; Gibson, !1D.T.; Zylstra, G.J. !$#journal Gene (1993) 127:31-37 !$#title Sequences of genes encoding naphthalene dioxygenase in !1Pseudomonas putida strains G7 and NCIB9816-4. !$#cross-references MUID:93252277; PMID:8486285 !$#accession JN0642 !'##molecule_type DNA !'##residues 1-328 ##label SIM !'##cross-references GB:M83950; NID:g151389; PIDN:AAA25904.1; !1PID:g151390 COMMENT This protein is a member of naphthalene dioxygenase !1multicomponent enzyme system, and is involved in the !1catabolism of naphthalene. GENETICS !$#gene nahAa CLASSIFICATION #superfamily methane monooxygenase reductase component; !1cytochrome-b5 reductase homology; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; flavoprotein; iron-sulfur protein; metalloprotein; !1oxidoreductase FEATURE !$20-74 #domain ferredoxin [2Fe-2S] homology #label FER\ !$103-323 #domain cytochrome-b5 reductase homology #label CBR\ !$35,40,43,73 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 328 #molecular-weight 35500 #checksum 9844 SEQUENCE /// ENTRY A47016 #type complete TITLE toluene-4-monooxygenase (EC 1.-.-.-) reductase component - Pseudomonas mendocina ORGANISM #formal_name Pseudomonas mendocina DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A47016 REFERENCE A47016 !$#authors Yen, K.M.; Karl, M.R. !$#journal J. Bacteriol. (1992) 174:7253-7261 !$#title Identification of a new gene, tmoF, in the Pseudomonas !1mendocina KR1 gene cluster encoding toluene-4-monooxygenase. !$#cross-references MUID:93054339; PMID:1429451 !$#accession A47016 !'##status preliminary !'##molecule_type DNA !'##residues 1-326 ##label YEN !'##cross-references GB:M95045; NID:g151596; PIDN:AAA26004.1; !1PID:g151597 !'##experimental_source KR1 !'##note sequence extracted from NCBI backbone (NCBIN:118027, !1NCBIP:118029) GENETICS !$#gene tmoF CLASSIFICATION #superfamily methane monooxygenase reductase component; !1cytochrome-b5 reductase homology; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; flavoprotein; iron-sulfur protein; metalloprotein; !1oxidoreductase FEATURE !$21-77 #domain ferredoxin [2Fe-2S] homology #label FER\ !$107-320 #domain cytochrome-b5 reductase homology #label CBR\ !$36,41,44,76 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 326 #molecular-weight 35983 #checksum 7094 SEQUENCE /// ENTRY JC5499 #type complete TITLE para-isopropyl toluene methyl hydroxylase (EC 1.-.-.-) - Pseudomonas aureofaciens ALTERNATE_NAMES p-cymene methyl hydroxylase ORGANISM #formal_name Pseudomonas aureofaciens DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JC5499; PC4335 REFERENCE JC5499 !$#authors Dutta, T.K.; Gunsalus, I.C. !$#journal Biochem. Biophys. Res. Commun. (1997) 233:502-506 !$#title Reductase gene sequences and protein structures: p-Cymene !1methyl hydroxylase. !$#cross-references MUID:97289661; PMID:9144566 !$#accession JC5499 !'##molecule_type DNA !'##residues 1-349 ##label DUT1 !'##cross-references GB:U86603; NID:g1840136; PIDN:AAC45296.1; !1PID:g1840137 !'##experimental_source strain PJC !'##note the authors translated the codon ACC for residue 53 as Leu !$#accession PC4335 !'##molecule_type protein !'##residues 11-320 ##label DUT2 GENETICS !$#gene cymA CLASSIFICATION #superfamily methane monooxygenase reductase component; !1cytochrome-b5 reductase homology; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; flavoprotein; iron-sulfur protein; metalloprotein; !1oxidoreductase FEATURE !$34-90 #domain ferredoxin [2Fe-2S] homology #label FER\ !$119-343 #domain cytochrome-b5 reductase homology #label CBR\ !$49,54,57,89 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 349 #molecular-weight 38433 #checksum 6423 SEQUENCE /// ENTRY O4HUD1 #type complete TITLE debrisoquine 4-hydroxylase (EC 1.14.14.-) cytochrome P450 2D6 - human ALTERNATE_NAMES CYP2D6; cytochrome P450 isozyme 2D; cytochrome P450db1 ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Mar-2000 ACCESSIONS S01199; A28883; JC4156; A33629; A30335 REFERENCE S01199 !$#authors Gonzalez, F.J.; Skoda, R.C.; Kimura, S.; Umeno, M.; Zanger, !1U.M.; Nebert, D.W.; Gelboin, H.V.; Hardwick, J.P.; Meyer, !1U.A. !$#journal Nature (1988) 331:442-446 !$#title Characterization of the common genetic defect in humans !1deficient in debrisoquine metabolism. !$#cross-references MUID:88122614; PMID:3123997 !$#accession S01199 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-497 ##label GON !'##cross-references EMBL:X08006; NID:g30450; PIDN:CAA30807.1; !1PID:g30451 REFERENCE A28883 !$#authors Gonzalez, F.J.; Vilbois, F.; Hardwick, J.P.; McBride, O.W.; !1Nebert, D.W.; Gelboin, H.V.; Meyer, U.A. !$#journal Genomics (1988) 2:174-179 !$#title Human debrisoquine 4-hydroxylase (P450IID1): cDNA and !1deduced amino acid sequence and assignment of the CYP2D !1locus to chromosome 22. !$#cross-references MUID:88314109; PMID:3410476 !$#accession A28883 !'##molecule_type mRNA !'##residues 1-497 ##label GON2 !'##cross-references EMBL:M20403; NID:g181349; PIDN:AAA52153.1; !1PID:g181350 REFERENCE JC4153 !$#authors Jiang, Q.; Voigt, J.M.; Colby, H.D. !$#journal Biochem. Biophys. Res. Commun. (1995) 209:1149-1156 !$#title Molecular cloning and sequencing of a guinea pig cytochrome !1P4502D (CYP2D16): high level expression in adrenal !1microsomes. !$#cross-references MUID:95251703; PMID:7733969 !$#accession JC4156 !'##status preliminary !'##molecule_type mRNA !'##residues 1-497 ##label JIA REFERENCE A33629 !$#authors Kimura, S.; Umeno, M.; Skoda, R.C.; Meyer, U.A.; Gonzalez, !1F.J. !$#journal Am. J. Hum. Genet. (1989) 45:889-904 !$#title The human debrisoquine 4-hydroxylase (CYP2D) locus: sequence !1and identification of the polymorphic CYP2D6 gene, a related !1gene, and a pseudogene. !$#cross-references MUID:90072069; PMID:2574001 !$#accession A33629 !'##molecule_type DNA !'##residues 1-373,'V',375-497 ##label KIM !'##cross-references EMBL:M33388; NID:g181303; PIDN:AAA53500.1; !1PID:g181304 REFERENCE A30335 !$#authors Manns, M.P.; Johnson, E.F.; Griffin, K.J.; Tan, E.M.; !1Sullivan, K.F. !$#journal J. Clin. Invest. (1989) 83:1066-1072 !$#title Major antigen of liver kidney microsomal autoantibodies in !1idiopathic autoimmune hepatitis is cytochrome P450db1. !$#cross-references MUID:89155788; PMID:2466049 !$#accession A30335 !'##molecule_type mRNA !'##residues 125-373,'V',375-485,'T',487-497 ##label MAN !'##cross-references EMBL:M24499; NID:g522194; PIDN:AAA36403.1; !1PID:g522195 GENETICS !$#gene GDB:CYP2D6 !'##cross-references GDB:132127; OMIM:124030 !$#map_position 22q13.1-22q13.1 !$#introns 60/3; 118/1; 169/1; 222/3; 281/3; 329/1; 391/3; 439/1 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; endoplasmic reticulum; !1heme; iron; metalloprotein; monooxygenase; oxidoreductase; !1transmembrane protein FEATURE !$302-465 #domain cytochrome P450 homology #label CYP\ !$443 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 497 #molecular-weight 55801 #checksum 8605 SEQUENCE /// ENTRY G02938 #type complete TITLE probable debrisoquine 4-hydroxylase (EC 1.14.14.-) cytochrome P450 - crab-eating macaque ORGANISM #formal_name Macaca fascicularis #common_name crab-eating macaque DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS G02938 REFERENCE G12616 !$#authors Lawton, M.P.; Laddison, K.J.; Speirs, A.A.; Mankowski, D.C.; !1Tweedie, D.J. !$#submission submitted to the EMBL Data Library, October 1995 !$#accession G02938 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-497 ##label LAW !'##cross-references EMBL:U38218; NID:g1022899; PIDN:AAA79722.1; !1PID:g1022900 GENETICS !$#gene CYP2D17 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; heme; iron; metalloprotein; monooxygenase; !1oxidoreductase; transmembrane protein FEATURE !$302-465 #domain cytochrome P450 homology #label P45\ !$443 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 497 #molecular-weight 56010 #checksum 7987 SEQUENCE /// ENTRY JC5819 #type complete TITLE cytochrome P450 2D [validated] - pig ALTERNATE_NAMES 25-hydroxyvitamin D(3) 25-monooxygenase; cytochrome P450 (14DM); cytochrome P450(25) CONTAINS lanosterol 14 alpha-demethylase; vitamin D3 25-hydroxylase (EC 1.14.14.-) ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 18-Aug-2000 ACCESSIONS JC5819; PC4502; S27177; S17048 REFERENCE JC5819 !$#authors Postlind, H.; Axen, E.; Bergman, T.; Wikvall, K. !$#journal Biochem. Biophys. Res. Commun. (1997) 241:491-497 !$#title Cloning, structure, and expression of a cDNA encoding !1vitamin D3 25-hydroxylase. !$#cross-references MUID:98086378; PMID:9425298 !$#accession JC5819 !'##molecule_type DNA !'##residues 1-500 ##label POS !'##cross-references GB:Y16417; NID:g2956687; PIDN:CAA76205.1; !1PID:g2956688 !$#accession PC4502 !'##molecule_type protein !'##residues 2-57;249-273;408-430 ##label AXE !'##experimental_source liver REFERENCE S27177 !$#authors Axen, E.; Bergman, T.; Wikvall, K. !$#journal Biochem. J. (1992) 287:725-731 !$#title Purification and characterization of a vitamin D(3) !125-hydroxylase from pig liver microsomes. !$#cross-references MUID:93075023; PMID:1445236 !$#accession S27177 !'##molecule_type protein !'##residues 2-17 ##label AXW !'##experimental_source liver REFERENCE S17048 !$#authors Sono, H.; Sonoda, Y.; Sato, Y. !$#journal Biochim. Biophys. Acta (1991) 1078:388-394 !$#title Purification and characterization of cytochrome P-450(14DM) !1(lanosterol 14-alpha-demethylase) from pig liver microsomes. !$#cross-references MUID:91316123; PMID:1859829 !$#accession S17048 !'##status preliminary !'##molecule_type protein !'##residues 2-11 ##label SON !'##note 6-Leu was also found COMMENT This enzyme catalyzes the first step in the metabolic !1activation of vitamin D3 into its hormonal form 1-alpha, !125-dihydroxyvitamin D3. CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; endoplasmic reticulum; !1heme; iron; metalloprotein; monooxygenase; oxidoreductase; !1transmembrane protein FEATURE !$305-468 #domain cytochrome P450 homology #label P45\ !$446 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 500 #molecular-weight 56511 #checksum 8000 SEQUENCE /// ENTRY B26822 #type complete TITLE cytochrome P450 2D2 - rat ALTERNATE_NAMES cytochrome P450CMF2; cytochrome P450db2 CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Mar-2000 ACCESSIONS B26822; D32970; C31579; S16871 REFERENCE A90957 !$#authors Gonzalez, F.J.; Matsunaga, T.; Nagata, K.; Meyer, U.A.; !1Nebert, D.W.; Pastewka, J.; Kozak, C.A.; Gillette, J.; !1Gelboin, H.V.; Hardwick, J.P. !$#journal DNA (1987) 6:149-161 !$#title Debrisoquine 4-hydroxylase: characterization of a new P450 !1gene subfamily, regulation, chromosomal mapping, and !1molecular analysis of the DA rat polymorphism. !$#cross-references MUID:87217961; PMID:3582092 !$#accession B26822 !'##molecule_type mRNA !'##residues 1-500 ##label GON !'##cross-references EMBL:M16655; NID:g203835; PIDN:AAA41055.1; !1PID:g203836 !'##note the authors translated the codon CCT for residue 240 as Ala REFERENCE A32970 !$#authors Matsunaga, E.; Zanger, U.M.; Hardwick, J.P.; Gelboin, H.V.; !1Meyer, U.A.; Gonzalez, F.J. !$#journal Biochemistry (1989) 28:7349-7355 !$#title The CYP2D gene subfamily: analysis of the molecular basis of !1the debrisoquine 4-hydroxylase deficiency in DA rats. !$#cross-references MUID:90057430; PMID:2819073 !$#accession D32970 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-500 ##label MAT REFERENCE A90151 !$#authors Ishida, N.; Tawaragi, Y.; Inuzuka, C.; Sugita, O.; Kubota, !1I.; Nakazato, H.; Noguchi, T.; Sassa, S. !$#journal Biochem. Biophys. Res. Commun. (1988) 156:681-688 !$#title Four species of cDNAs for cytochrome P450 isozymes !1immunorelated to P450c-M/F encode for members of P450IID !1subfamily, increasing the number of members within the !1subfamily. !$#cross-references MUID:89050091; PMID:3190674 !$#accession C31579 !'##molecule_type mRNA !'##residues 1-116,'D',118-345,'R',347-357,'F',359-406,'K',408-500 !1##label ISH !'##cross-references EMBL:M22330; NID:g203823; PIDN:AAA41049.1; !1PID:g203824 REFERENCE S16871 !$#authors Matsunaga, E.; Umeno, M.; Gonzalez, F.J. !$#journal J. Mol. Evol. (1990) 30:155-169 !$#title The rat P450 IID subfamily: complete sequences of four !1closely linked genes and evidence that gene conversions !1maintained sequence homogeneity at the heme-binding region !1of the cytochrome P450 active site. !$#cross-references MUID:90189185; PMID:2107330 !$#accession S16871 !'##molecule_type DNA !'##residues 1-345,'R',347-357,'F',359-406,'K',408-500 ##label MA2 !'##cross-references EMBL:X52027; NID:g57811; PIDN:CAA36269.1; !1PID:g57812 GENETICS !$#gene CYP2D2 !$#introns 63/3; 121/1; 172/1; 225/3; 284/3; 332/1; 394/3; 442/1 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; endoplasmic reticulum; !1heme; iron; metalloprotein; monooxygenase; oxidoreductase; !1transmembrane protein FEATURE !$9-25 #domain transmembrane #status predicted #label TM1\ !$305-468 #domain cytochrome P450 homology #label CYP\ !$310-326 #domain transmembrane #status predicted #label TM2\ !$446 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 500 #molecular-weight 56607 #checksum 8170 SEQUENCE /// ENTRY JE0258 #type complete TITLE cytochrome P450 2D23 - rabbit CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Mar-2000 ACCESSIONS JE0258 REFERENCE JE0258 !$#authors Yamamoto, Y.; Ishizuka, M.; Takada, A.; Fujita, S. !$#journal J. Biochem. (1998) 124:503-508 !$#title Cloning, tissue distribution, and functional expression of !1two novel rabbit cytochrome P450 isozymes,CYP2D23 and !1CYP2D24. !$#cross-references MUID:98391821; PMID:9722658 !$#accession JE0258 !'##molecule_type mRNA !'##residues 1-500 ##label YAM !'##cross-references DDBJ:AB008784 !'##experimental_source liver COMMENT This protein shows high drug metabolizing activity. CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; endoplasmic reticulum; !1heme; iron; metalloprotein; oxidoreductase; transmembrane !1protein FEATURE !$9-25 #domain transmembrane #status predicted #label TM1\ !$305-468 #domain cytochrome P450 homology #label CYP\ !$310-326 #domain transmembrane #status predicted #label TM2\ !$446 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 500 #molecular-weight 55604 #checksum 9403 SEQUENCE /// ENTRY JE0259 #type complete TITLE cytochrome P450 2D24 - rabbit CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Mar-2000 ACCESSIONS JE0259 REFERENCE JE0258 !$#authors Yamamoto, Y.; Ishizuka, M.; Takada, A.; Fujita, S. !$#journal J. Biochem. (1998) 124:503-508 !$#title Cloning, tissue distribution, and functional expression of !1two novel rabbit cytochrome P450 isozymes,CYP2D23 and !1CYP2D24. !$#cross-references MUID:98391821; PMID:9722658 !$#accession JE0259 !'##molecule_type mRNA !'##residues 1-500 ##label YAM !'##cross-references DDBJ:AB008785 COMMENT This protein shows high drug metabolizing activity. CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; endoplasmic reticulum; !1heme; iron; metalloprotein; oxidoreductase; transmembrane !1protein FEATURE !$9-25 #domain transmembrane #status predicted #label TM1\ !$305-468 #domain cytochrome P450 homology #label CYP\ !$310-326 #domain transmembrane #status predicted #label TM2\ !$446 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 500 #molecular-weight 55721 #checksum 6224 SEQUENCE /// ENTRY JC4157 #type complete TITLE cytochrome P450 2D, endoplasmic reticulum - dog ALTERNATE_NAMES cytochrome P450 2D, microsomal CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Canis lupus familiaris #common_name dog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS JC4157; S65962; S65898 REFERENCE JC4153 !$#authors Jiang, Q.; Voigt, J.M.; Colby, H.D. !$#journal Biochem. Biophys. Res. Commun. (1995) 209:1149-1156 !$#title Molecular cloning and sequencing of a guinea pig cytochrome !1P4502D (CYP2D16): high level expression in adrenal !1microsomes. !$#cross-references MUID:95251703; PMID:7733969 !$#accession JC4157 !'##molecule_type mRNA !'##residues 1-500 ##label JIA !'##cross-references GB:U21486; NID:g862481 REFERENCE S65898 !$#authors Sakamoto, K.; Kirita, S.; Baba, T.; Nakamura, Y.; Yamazoe, !1Y.; Kato, R.; Takanaka, A.; Matsubara, T. !$#journal Arch. Biochem. Biophys. (1995) 319:372-382 !$#title A new cytochrome P450 form belonging to the CYP2D in dog !1liver microsomes: purification, cDNA cloning, and enzyme !1characterization. !$#cross-references MUID:95305574; PMID:7786018 !$#accession S65962 !'##status preliminary !'##molecule_type mRNA !'##residues 1-500 ##label SAK !'##cross-references EMBL:D17397; NID:g397824; PIDN:BAA04220.1; !1PID:g397825 !$#accession S65898 !'##molecule_type protein !'##residues 2-37,'X',39 ##label SAW COMMENT This protein is a member of the CYP2D subfamily, it !1represents the isozyme associated with adrenal xenobiotic !1metabolism. GENETICS !$#gene CYP2D15 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS adrenal gland; chromoprotein; endoplasmic reticulum; heme; !1iron; metalloprotein; oxidoreductase; transmembrane protein FEATURE !$305-468 #domain cytochrome P450 homology #label P45\ !$446 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 500 #molecular-weight 56432 #checksum 1262 SEQUENCE /// ENTRY O4RTD5 #type complete TITLE cytochrome P450 2D5 - rat ALTERNATE_NAMES cytochrome P450CMF1b; cytochrome P450db5 CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Mar-2000 ACCESSIONS S09611; A32970; S16874; B31579 REFERENCE S09611 !$#authors Ishida, N.; Inuzuka, C.; Tawaragi, Y.; Sugita, O.; Nakazato, !1H.; Noguchi, T.; Sassa, S.; Kappas, A. !$#journal Nucleic Acids Res. (1989) 17:6407 !$#title Cytochrome P450CMF cDNA: nucleotide sequence of P450CMF1b. !$#cross-references MUID:89366685; PMID:2771656 !$#accession S09611 !'##molecule_type mRNA !'##residues 1-504 ##label ISH !'##cross-references EMBL:M25143; NID:g203775; PIDN:AAA41034.1; !1PID:g203776 REFERENCE A32970 !$#authors Matsunaga, E.; Zanger, U.M.; Hardwick, J.P.; Gelboin, H.V.; !1Meyer, U.A.; Gonzalez, F.J. !$#journal Biochemistry (1989) 28:7349-7355 !$#title The CYP2D gene subfamily: analysis of the molecular basis of !1the debrisoquine 4-hydroxylase deficiency in DA rats. !$#cross-references MUID:90057430; PMID:2819073 !$#accession A32970 !'##molecule_type mRNA !'##residues 1-504 ##label MAT1 !'##cross-references EMBL:J02869; NID:g203673; PIDN:AAA41003.1; !1PID:g203674 REFERENCE S16871 !$#authors Matsunaga, E.; Umeno, M.; Gonzalez, F.J. !$#journal J. Mol. Evol. (1990) 30:155-169 !$#title The rat P450 IID subfamily: complete sequences of four !1closely linked genes and evidence that gene conversions !1maintained sequence homogeneity at the heme-binding region !1of the cytochrome P450 active site. !$#cross-references MUID:90189185; PMID:2107330 !$#accession S16874 !'##molecule_type DNA !'##residues 1-504 ##label MAT2 !'##cross-references EMBL:X52030; NID:g57817; PIDN:CAA36272.1; !1PID:g57818 REFERENCE A90151 !$#authors Ishida, N.; Tawaragi, Y.; Inuzuka, C.; Sugita, O.; Kubota, !1I.; Nakazato, H.; Noguchi, T.; Sassa, S. !$#journal Biochem. Biophys. Res. Commun. (1988) 156:681-688 !$#title Four species of cDNAs for cytochrome P450 isozymes !1immunorelated to P450c-M/F encode for members of P450IID !1subfamily, increasing the number of members within the !1subfamily. !$#cross-references MUID:89050091; PMID:3190674 !$#accession B31579 !'##molecule_type mRNA !'##residues 18-504 ##label IS2 !'##cross-references EMBL:M22329; NID:g203806; PIDN:AAA41045.1; !1PID:g203807 GENETICS !$#gene CYP2D5 !$#introns 63/3; 121/1; 172/1; 225/3; 284/3; 332/1; 394/3; 442/1 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; endoplasmic reticulum; !1heme; iron; metalloprotein; monooxygenase; oxidoreductase; !1transmembrane protein FEATURE !$305-468 #domain cytochrome P450 homology #label P45\ !$446 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 504 #molecular-weight 57076 #checksum 7669 SEQUENCE /// ENTRY A26822 #type complete TITLE debrisoquine 4-hydroxylase (EC 1.14.14.-) cytochrome P450 2D1 - rat ALTERNATE_NAMES cytochrome P450 UT-7; cytochrome P450db1 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Mar-2000 ACCESSIONS A26822; A30495; B32970; C32970; A31579; JC4158; S39761 REFERENCE A90957 !$#authors Gonzalez, F.J.; Matsunaga, T.; Nagata, K.; Meyer, U.A.; !1Nebert, D.W.; Pastewka, J.; Kozak, C.A.; Gillette, J.; !1Gelboin, H.V.; Hardwick, J.P. !$#journal DNA (1987) 6:149-161 !$#title Debrisoquine 4-hydroxylase: characterization of a new P450 !1gene subfamily, regulation, chromosomal mapping, and !1molecular analysis of the DA rat polymorphism. !$#cross-references MUID:87217961; PMID:3582092 !$#accession A26822 !'##molecule_type mRNA !'##residues 1-504 ##label GON !'##cross-references EMBL:M16654; NID:g203833; PIDN:AAA41054.1; !1PID:g203834 !$#accession A30495 !'##molecule_type protein !'##residues 'X',5-7,'X',9,'XX',12-23 ##label GO2 REFERENCE A32970 !$#authors Matsunaga, E.; Zanger, U.M.; Hardwick, J.P.; Gelboin, H.V.; !1Meyer, U.A.; Gonzalez, F.J. !$#journal Biochemistry (1989) 28:7349-7355 !$#title The CYP2D gene subfamily: analysis of the molecular basis of !1the debrisoquine 4-hydroxylase deficiency in DA rats. !$#cross-references MUID:90057430; PMID:2819073 !$#accession B32970 !'##molecule_type mRNA !'##residues 1-504 ##label MA1 !'##cross-references EMBL:J02867; NID:g203669; PIDN:AAA41001.1; !1PID:g203670 !$#accession C32970 !'##molecule_type mRNA !'##residues 1-122,'VF',125-172,'R',174-379,'I',381-504 ##label MAT1 REFERENCE A90151 !$#authors Ishida, N.; Tawaragi, Y.; Inuzuka, C.; Sugita, O.; Kubota, !1I.; Nakazato, H.; Noguchi, T.; Sassa, S. !$#journal Biochem. Biophys. Res. Commun. (1988) 156:681-688 !$#title Four species of cDNAs for cytochrome P450 isozymes !1immunorelated to P450c-M/F encode for members of P450IID !1subfamily, increasing the number of members within the !1subfamily. !$#cross-references MUID:89050091; PMID:3190674 !$#accession A31579 !'##molecule_type mRNA !'##residues 1-122,'VF',125-172,'R',174-379,'I',381-504 ##label ISH !'##cross-references EMBL:M22328; NID:g203802; PIDN:AAA41043.1; !1PID:g203803 REFERENCE JC4153 !$#authors Jiang, Q.; Voigt, J.M.; Colby, H.D. !$#journal Biochem. Biophys. Res. Commun. (1995) 209:1149-1156 !$#title Molecular cloning and sequencing of a guinea pig cytochrome !1P4502D (CYP2D16): high level expression in adrenal !1microsomes. !$#cross-references MUID:95251703; PMID:7733969 !$#accession JC4158 !'##status preliminary !'##molecule_type mRNA !'##residues 1-504 ##label JIA REFERENCE S39761 !$#authors Ohishi, N.; Imaoka, S.; Suzuki, T.; Funae, Y. !$#journal Biochim. Biophys. Acta (1993) 1158:227-236 !$#title Characterization of two P-450 isozymes placed in the rat !1CYP2D subfamily. !$#cross-references MUID:94072607; PMID:8251521 !$#accession S39761 !'##molecule_type protein !'##residues 1-9,'X',11-13 ##label OHI GENETICS !$#gene CYP2D1 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; endoplasmic reticulum; !1heme; iron; metalloprotein; monooxygenase; oxidoreductase; !1transmembrane protein FEATURE !$1-504 #product cytochrome P450 2D1 #status experimental !8#label MAT\ !$4-504 #product cytochrome P450 2D1v #status experimental !8#label MAT2\ !$9-25 #domain transmembrane #status predicted #label TM1\ !$305-468 #domain cytochrome P450 homology #label CYP\ !$310-326 #domain transmembrane #status predicted #label TM2\ !$446 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 504 #molecular-weight 57175 #checksum 8199 SEQUENCE /// ENTRY I49428 #type complete TITLE cytochrome P450 16a-ms2 - western wild mouse CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Mus spretus #common_name western wild mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS I49428 REFERENCE A57454 !$#authors Sueyoshi, T.; Kobayashi, R.; Nishio, K.; Aida, K.; Moore, !1R.; Wada, T.; Handa, H.; Negishi, M. !$#journal Mol. Cell. Biol. (1995) 15:4158-4166 !$#title A nuclear factor (NF2d9) that binds to the male-specific !1P450 (Cyp 2d-9) gene in mouse liver. !$#cross-references MUID:95349581; PMID:7623810 !$#accession I49428 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-504 ##label RES !'##cross-references EMBL:U20088; NID:g951101; PIDN:AAC52246.1; !1PID:g951102 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxidoreductase; !1transmembrane protein FEATURE !$305-468 #domain cytochrome P450 homology #label P45\ !$446 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 504 #molecular-weight 57191 #checksum 5154 SEQUENCE /// ENTRY A27384 #type complete TITLE steroid 16alpha-hydroxylase (EC 1.14.14.-) cytochrome P450 2D9 - mouse ALTERNATE_NAMES cytochrome P450 16alpha; cytochrome P450ca; testosterone 16alpha-hydroxylase ORGANISM #formal_name Mus musculus #common_name house mouse DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Mar-2000 ACCESSIONS S15806; A27384; B30247 REFERENCE S15806 !$#authors Wong, G.; Itakura, T.; Kawajiri, K.; Skow, L.; Negishi, M. !$#journal J. Biol. Chem. (1989) 264:2920-2927 !$#title Gene family of male-specific testosterone !116-alpha-hydroxylase (C-P-450(16-alpha)) in mice. !1Organization, differential regulation, and chromosome !1localization. !$#cross-references MUID:89123394; PMID:2914938 !$#accession S15806 !'##status translation not shown !'##molecule_type DNA !'##residues 1-504 ##label WON !'##cross-references EMBL:M24262 REFERENCE A90528 !$#authors Wong, G.; Kawajiri, K.; Negishi, M. !$#journal Biochemistry (1987) 26:8683-8690 !$#title Gene family of male-specific testosterone !116-alpha-hydroxylase (C-P-450-16-alpha) in mouse liver: cDNA !1sequences, neonatal imprinting, and reversible regulation by !1androgen. !$#cross-references MUID:88163547; PMID:2831949 !$#accession A27384 !'##molecule_type mRNA !'##residues 1-504 ##label WON2 !'##cross-references EMBL:M23998; NID:g201972; PIDN:AAA40427.1; !1PID:g201973 REFERENCE A30247 !$#authors Ichikawa, T.; Itakura, T.; Negishi, M. !$#journal Biochemistry (1989) 28:4779-4784 !$#title Functional characterization of two cytochrome P-450s within !1the mouse, male-specific steroid 16alpha-hydroxylase gene !1family: expression in mammalian cells and chimeric proteins. !$#cross-references MUID:89352551; PMID:2788458 !$#accession B30247 !'##molecule_type mRNA !'##residues 1-504 ##label ICH !'##cross-references EMBL:M27168 !'##note the authors translated the codon CAG for residue 54 as Leu and !1GAT for residue 55 as Gly; the sequence shown follows the !1authors' translation GENETICS !$#gene Cyp2d-9 !$#map_position 15 !$#introns 63/3; 121/1; 172/1; 225/3; 284/3; 332/1; 394/3; 442/1 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; endoplasmic reticulum; !1heme; iron; metalloprotein; monooxygenase; oxidoreductase; !1transmembrane protein FEATURE !$9-25 #domain transmembrane #status predicted #label TM1\ !$305-468 #domain cytochrome P450 homology #label CYP\ !$310-326 #domain transmembrane #status predicted #label TM2\ !$446 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 504 #molecular-weight 56949 #checksum 8434 SEQUENCE /// ENTRY B27384 #type complete TITLE probable truncated cytochrome P450 2D9 (clone p16alpha-16) - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B27384 REFERENCE A90528 !$#authors Wong, G.; Kawajiri, K.; Negishi, M. !$#journal Biochemistry (1987) 26:8683-8690 !$#title Gene family of male-specific testosterone !116-alpha-hydroxylase (C-P-450-16-alpha) in mouse liver: cDNA !1sequences, neonatal imprinting, and reversible regulation by !1androgen. !$#cross-references MUID:88163547; PMID:2831949 !$#accession B27384 !'##molecule_type mRNA !'##residues 1-294 ##label WON !'##cross-references EMBL:M23997; NID:g201974; PIDN:AAA40428.1; !1PID:g201975 COMMENT This truncated protein is derived from a cDNA lacking exon 6 !1and, consequently, part of the heme-binding domain. It may !1be a structural component of testosterone 16alpha !1hydroxylase. GENETICS !$#gene Cyp2d-9 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS alternative splicing; microsome; transmembrane protein SUMMARY #length 294 #molecular-weight 33300 #checksum 4570 SEQUENCE /// ENTRY A30247 #type complete TITLE cytochrome P450 2D10 - mouse ALTERNATE_NAMES cytochrome P450cb CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Mus musculus #common_name house mouse DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Mar-2000 ACCESSIONS A30247; S15807; S19168 REFERENCE A30247 !$#authors Ichikawa, T.; Itakura, T.; Negishi, M. !$#journal Biochemistry (1989) 28:4779-4784 !$#title Functional characterization of two cytochrome P-450s within !1the mouse, male-specific steroid 16alpha-hydroxylase gene !1family: expression in mammalian cells and chimeric proteins. !$#cross-references MUID:89352551; PMID:2788458 !$#accession A30247 !'##molecule_type mRNA !'##residues 1-504 ##label ICH !'##cross-references EMBL:M27167; NID:g529437; PIDN:AAA39878.1; !1PID:g529438 REFERENCE S15806 !$#authors Wong, G.; Itakura, T.; Kawajiri, K.; Skow, L.; Negishi, M. !$#journal J. Biol. Chem. (1989) 264:2920-2927 !$#title Gene family of male-specific testosterone !116-alpha-hydroxylase (C-P-450(16-alpha)) in mice. !1Organization, differential regulation, and chromosome !1localization. !$#cross-references MUID:89123394; PMID:2914938 !$#accession S15807 !'##status translation not shown !'##molecule_type DNA !'##residues 1-504 ##label WON2 !'##cross-references EMBL:M24263 !'##note this sequence has been revised in reference S19168 REFERENCE S19168 !$#authors Wong, G.; Itakura, T.; Kawajiri, K.; Skow, L.; Negishi, M. !$#submission submitted to the EMBL Data Library, July 1989 !$#accession S19168 !'##molecule_type DNA !'##residues 1-45,'L',47-220,'LAYS',225-504 ##label WON !'##cross-references EMBL:M24263; NID:g192919; PIDN:AAA79023.1; !1PID:g387141 GENETICS !$#gene Cyp2d10 !$#map_position 15 !$#introns 63/3; 121/1; 172/1; 225/3; 284/3; 332/1; 394/3; 442/1 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; endoplasmic reticulum; !1heme; iron; metalloprotein; monooxygenase; oxidoreductase; !1transmembrane protein FEATURE !$9-25 #domain transmembrane #status predicted #label TM1\ !$305-468 #domain cytochrome P450 homology #label CYP\ !$310-326 #domain transmembrane #status predicted #label TM2\ !$446 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 504 #molecular-weight 57248 #checksum 9138 SEQUENCE /// ENTRY S19169 #type complete TITLE cytochrome P450 2D11 - mouse ALTERNATE_NAMES cytochrome P450cc CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Mus musculus #common_name house mouse DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 21-Jul-2000 ACCESSIONS S19169; S15808 REFERENCE S19168 !$#authors Wong, G.; Itakura, T.; Kawajiri, K.; Skow, L.; Negishi, M. !$#submission submitted to the EMBL Data Library, July 1989 !$#accession S19169 !'##molecule_type DNA !'##residues 1-505 ##label WON !'##cross-references EMBL:M24264; NID:g192921; PIDN:AAA37514.1; !1PID:g387142 !'##experimental_source strain BALB/cJ REFERENCE S15806 !$#authors Wong, G.; Itakura, T.; Kawajiri, K.; Skow, L.; Negishi, M. !$#journal J. Biol. Chem. (1989) 264:2920-2927 !$#title Gene family of male-specific testosterone !116-alpha-hydroxylase (C-P-450(16-alpha)) in mice. !1Organization, differential regulation, and chromosome !1localization. !$#cross-references MUID:89123394; PMID:2914938 !$#contents annotation !$#note the published nucleotide sequence has been revised in !1reference S19169 GENETICS !$#gene Cyp2d-11 !$#map_position 15 !$#introns 63/3; 120/3; 172/1; 225/3; 284/3; 332/1; 395/3; 443/1 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; endoplasmic reticulum; !1heme; iron; metalloprotein; monooxygenase; oxidoreductase; !1transmembrane protein FEATURE !$9-25 #domain transmembrane #status predicted #label TM1\ !$305-469 #domain cytochrome P450 homology #label P45\ !$310-326 #domain transmembrane #status predicted #label TM2\ !$447 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 505 #molecular-weight 57155 #checksum 8200 SEQUENCE /// ENTRY JC4153 #type complete TITLE cytochrome P450 2D16, CYP2D16 - guinea pig CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Cavia porcellus #common_name guinea pig DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS JC4153; PC4052 REFERENCE JC4153 !$#authors Jiang, Q.; Voigt, J.M.; Colby, H.D. !$#journal Biochem. Biophys. Res. Commun. (1995) 209:1149-1156 !$#title Molecular cloning and sequencing of a guinea pig cytochrome !1P4502D (CYP2D16): high level expression in adrenal !1microsomes. !$#cross-references MUID:95251703; PMID:7733969 !$#accession JC4153 !'##molecule_type mRNA !'##residues 1-500 ##label JIA !'##cross-references GB:U21486; NID:g862481; PIDN:AAA68479.1; !1PID:g862482 !$#accession PC4052 !'##molecule_type protein !'##residues 1-37 ##label JI2 COMMENT This protein is a member of the CYP2D subfamily, it !1represents the isozyme associated with adrenal xenobiotic !1metabolism. CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS adrenal gland; chromoprotein; heme; iron; metalloprotein; !1microsome; oxidoreductase; transmembrane protein FEATURE !$305-468 #domain cytochrome P450 homology #label P45\ !$496 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 500 #molecular-weight 55800 #checksum 2529 SEQUENCE /// ENTRY S37284 #type complete TITLE cytochrome P450 2D - bovine CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS S37284; S29295; S29862 REFERENCE S29295 !$#authors Tsuneoka, Y.; Matsuo, Y.; Higuchi, R.; Ichikawa, Y. !$#journal Eur. J. Biochem. (1992) 208:739-746 !$#title Characterization of the cytochrome P-450IID subfamily in !1bovine liver. Nucleotide sequences and microheterogeneity. !$#cross-references MUID:93011103; PMID:1396678 !$#accession S37284 !'##molecule_type mRNA !'##residues 1-500 ##label TSU !'##cross-references EMBL:X68481; NID:g295; PIDN:CAA48501.1; PID:g296 !'##experimental_source clone pBVL 180 !$#accession S29295 !'##molecule_type mRNA !'##residues 14-111,'R',113-131,'R',133-162,'L',164-178,'G',180-219,'F', !1221-247,'R',249-255,'G',257-367,'A',369-412,'Q',414-500 !1##label TS2 !'##cross-references EMBL:X68013; NID:g293; PIDN:CAA48149.1; PID:g294 !'##experimental_source clone pBVL 76 GENETICS !$#gene CYP2D CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; endoplasmic reticulum; !1heme; iron; metalloprotein; monooxygenase; oxidoreductase; !1transmembrane protein FEATURE !$305-468 #domain cytochrome P450 homology #label P45\ !$446 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 500 #molecular-weight 55921 #checksum 9181 SEQUENCE /// ENTRY D31579 #type complete TITLE cytochrome P450 2D4 - rat ALTERNATE_NAMES cytochrome P450CMF3 CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 21-Jul-2000 ACCESSIONS S16873; D31579; I52313 REFERENCE S16871 !$#authors Matsunaga, E.; Umeno, M.; Gonzalez, F.J. !$#journal J. Mol. Evol. (1990) 30:155-169 !$#title The rat P450 IID subfamily: complete sequences of four !1closely linked genes and evidence that gene conversions !1maintained sequence homogeneity at the heme-binding region !1of the cytochrome P450 active site. !$#cross-references MUID:90189185; PMID:2107330 !$#accession S16873 !'##molecule_type DNA !'##residues 1-500 ##label MAT !'##cross-references EMBL:X52029; NID:g57815; PIDN:CAA36271.1; !1PID:g57816 REFERENCE A90151 !$#authors Ishida, N.; Tawaragi, Y.; Inuzuka, C.; Sugita, O.; Kubota, !1I.; Nakazato, H.; Noguchi, T.; Sassa, S. !$#journal Biochem. Biophys. Res. Commun. (1988) 156:681-688 !$#title Four species of cDNAs for cytochrome P450 isozymes !1immunorelated to P450c-M/F encode for members of P450IID !1subfamily, increasing the number of members within the !1subfamily. !$#cross-references MUID:89050091; PMID:3190674 !$#accession D31579 !'##molecule_type mRNA !'##residues 177-500 ##label ISH !'##cross-references EMBL:M22331; NID:g203829; PIDN:AAA41052.1; !1PID:g203830 REFERENCE I52313 !$#authors Kawashima, H.; Strobel, H.W. !$#journal Biochem. Biophys. Res. Commun. (1995) 209:535-540 !$#title cDNA cloning of a novel rat brain cytochrome P450 belonging !1to the CYP2D subfamily. !$#cross-references MUID:95251650; PMID:7733922 !$#accession I52313 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-326,'R',328-399,'I',401-472,'A',474-479,'N',481-482,'V', !1484-500 ##label RES !'##cross-references GB:S77859; NID:g1200515; PIDN:AAC52882.1; !1PID:g1200516 !'##experimental_source brain, strain Sprague-Dawley GENETICS !$#gene CYP2D4 !$#introns 63/3; 121/1; 172/1; 225/3; 284/3; 332/1; 394/3; 442/1 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; endoplasmic reticulum; !1heme; iron; metalloprotein; monooxygenase; oxidoreductase; !1transmembrane protein FEATURE !$9-25 #domain transmembrane #status predicted #label TM1\ !$305-468 #domain cytochrome P450 homology #label CYP\ !$310-326 #domain transmembrane #status predicted #label TM2\ !$446 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 500 #molecular-weight 56697 #checksum 7863 SEQUENCE /// ENTRY S16872 #type complete TITLE cytochrome P450 2D3 - rat ALTERNATE_NAMES cytochrome P450db3 CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Mar-2000 ACCESSIONS S16872; E32970 REFERENCE S16871 !$#authors Matsunaga, E.; Umeno, M.; Gonzalez, F.J. !$#journal J. Mol. Evol. (1990) 30:155-169 !$#title The rat P450 IID subfamily: complete sequences of four !1closely linked genes and evidence that gene conversions !1maintained sequence homogeneity at the heme-binding region !1of the cytochrome P450 active site. !$#cross-references MUID:90189185; PMID:2107330 !$#accession S16872 !'##molecule_type DNA !'##residues 1-500 ##label MAT !'##cross-references EMBL:X52028; NID:g57813; PIDN:CAA36270.1; !1PID:g57814 REFERENCE A32970 !$#authors Matsunaga, E.; Zanger, U.M.; Hardwick, J.P.; Gelboin, H.V.; !1Meyer, U.A.; Gonzalez, F.J. !$#journal Biochemistry (1989) 28:7349-7355 !$#title The CYP2D gene subfamily: analysis of the molecular basis of !1the debrisoquine 4-hydroxylase deficiency in DA rats. !$#cross-references MUID:90057430; PMID:2819073 !$#accession E32970 !'##molecule_type mRNA !'##residues 1-500 ##label MATS !'##cross-references EMBL:J02868; NID:g203671; PIDN:AAA41002.1; !1PID:g203672 GENETICS !$#gene CYP2D3 !$#introns 63/3; 121/1; 172/1; 225/3; 284/3; 332/1; 394/3; 442/1 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; endoplasmic reticulum; !1heme; iron; metalloprotein; monooxygenase; oxidoreductase; !1transmembrane protein FEATURE !$9-25 #domain transmembrane #status predicted #label TM1\ !$305-468 #domain cytochrome P450 homology #label CYP\ !$310-326 #domain transmembrane #status predicted #label TM2\ !$446 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 500 #molecular-weight 56677 #checksum 9825 SEQUENCE /// ENTRY A40938 #type complete TITLE cytochrome P450 ib - rabbit CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A40938 REFERENCE A40938 !$#authors Kikuta, Y.; Sogawa, K.; Haniu, M.; Kinosaki, M.; Kusunose, !1E.; Nojima, Y.; Yamamoto, S.; Ichihara, K.; Kusunose, M.; !1Fujii-Kuriyama, Y. !$#journal J. Biol. Chem. (1991) 266:17821-17825 !$#title A novel species of cytochrome P-450 (P-450-ib) specific for !1the small intestine of rabbits. cDNA cloning and its !1expression in COS cells. !$#cross-references MUID:92011499; PMID:1717443 !$#accession A40938 !'##status preliminary !'##molecule_type mRNA !'##residues 1-501 ##label KIK !'##cross-references GB:D90405; NID:g217717; PIDN:BAA14401.1; !1PID:g217718 GENETICS !$#gene CYP2J1 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxidoreductase FEATURE !$308-469 #domain cytochrome P450 homology #label CYP\ !$447 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 501 #molecular-weight 57325 #checksum 9593 SEQUENCE /// ENTRY O4RTPB #type complete TITLE cytochrome P450 2B1 - rat ALTERNATE_NAMES cytochrome P450 b; cytochrome P450, phenobarbital-inducible CONTAINS unspecific monooxygenase (EC 1.14.14.1) ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 18-Aug-1982 #sequence_revision 17-May-1996 #text_change 03-Mar-2000 ACCESSIONS A00176; A54251; A22363; A29298; S03854; A92255; I54796 REFERENCE A93912 !$#authors Fujii-Kuriyama, Y.; Mizukami, Y.; Kawajiri, K.; Sogawa, K.; !1Muramatsu, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:2793-2797 !$#title Primary structure of a cytochrome p-450: coding nucleotide !1sequence of phenobarbital-inducible cytochrome p450 cDNA !1from rat liver. !$#cross-references MUID:82222224; PMID:6953431 !$#accession A00176 !'##molecule_type mRNA !'##residues 6-491 ##label FUJ !'##cross-references EMBL:J00719; NID:g203752; PIDN:AAA41024.1; !1PID:g203753 !'##note the authors translated the codon GAT for residue 166 as Glu, !1CTG for residue 292 as Pro, and CGA for residue 378 as Gln REFERENCE A93925 !$#authors Fujii-Kuriyama, Y.; Mizukami, Y.; Kawajiri, K.; Sogawa, K.; !1Muramatsu, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:5443 !$#title Primary structure of a cytochrome P450: coding nucleotide !1sequence of phenobarbital-inducible cytochrome P-450 cDNA !1from rat liver. !$#contents annotation !$#note the mistranslations shown in reference A93912 are !1acknowledged REFERENCE A54251 !$#authors Roberts, E.S.; Hopkins, N.E.; Zaluzec, E.J.; Gage, D.A.; !1Alworth, W.L.; Hollenberg, P.F. !$#journal Biochemistry (1994) 33:3766-3771 !$#title Identification of active-site peptides from (3)H-labeled !12-ethynylnaphthalene-inactivated P450 2B1 and 2B4 using !1amino acid sequencing and mass spectrometry. !$#cross-references MUID:94190899; PMID:8142377 !$#accession A54251 !'##molecule_type protein !'##residues 290-301,'X' ##label ROB REFERENCE A22363 !$#authors Suwa, Y.; Mizukami, Y.; Sogawa, K.; Fujii-Kuriyama, Y. !$#journal J. Biol. Chem. (1985) 260:7980-7984 !$#title Gene structure of a major form of phenobarbital-inducible !1cytochrome P-450 in rat liver. !$#cross-references MUID:85234490; PMID:2989270 !$#accession A22363 !'##molecule_type DNA !'##residues 1-91,'P',93-204,'R',206-327,'V',329-356,'H',358-391,'R', !1393-415,'V',417-433,'H',435-491 ##label SUW !'##cross-references GB:L00320; NID:g203816; PIDN:AAA41046.1; !1PID:g203818 !'##note the authors translated the codon CAG for residue 57 as Gly, CCT !1for residue 92 as Ala, ATT for residue 146 as Val, TCC for !1residue 181 as Thr, AGG for residue 205 as Thr, AGC for !1residue 214 as Glu, AAA for residue 236 as Leu, AGC for !1residue 259 as Asn, GTT for residue 328 as Ile, CAT for !1residue 357 as Gln, GAC for residue 398 as Tyr, GTT for !1residue 416 as Ala, and CAC for residue 434 as Arg REFERENCE A29298 !$#authors Rangarajan, P.N.; Ravishankar, H.; Padmanaban, G. !$#journal Biochem. Biophys. Res. Commun. (1987) 144:258-263 !$#title Isolation of a cytochrome P-450e gene variant and !1characterization of its 5' flanking sequences. !$#cross-references MUID:87213174; PMID:3579906 !$#accession A29298 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-57 ##label RAN REFERENCE S03854 !$#authors Oesch, F.; Waxman, D.J.; Morrissey, J.J.; Honscha, W.; !1Kissel, W.; Friedberg, T. !$#journal Arch. Biochem. Biophys. (1989) 270:23-32 !$#title Antibodies targeted against hypervariable and constant !1regions of cytochromes P450IIB1 and P450IIB2. !$#cross-references MUID:89192373; PMID:2539047 !$#accession S03854 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-18;146-160,'E',162-165;166,330-361;362-380;402-423 !1##label OES REFERENCE A92255 !$#authors Botelho, L.H.; Ryan, D.E.; Levin, W. !$#journal J. Biol. Chem. (1979) 254:5635-5640 !$#title Amino acid compositions and partial amino acid sequences of !1three highly purified forms of liver microsomal cytochrome !1P-450 from rats treated with polychlorinated biphenyls, !1phenobarbital, or 3-methylcholanthrene. !$#cross-references MUID:79194111; PMID:109438 !$#accession A92255 !'##molecule_type protein !'##residues 1-3,'T',5-22 ##label BOT REFERENCE I54796 !$#authors Fujii-Kuriyama, Y.; Mizukami, Y.; Taniguchi, T.; Muramatsu, !1M. !$#journal Int. Symp. Princess Takamatsu Cancer Res. Fund (1982) !112:31-40 !$#title Molecular cloning and coding nucleotide sequence of !1complementary DNA of cytochrome P-450 involved in metabolic !1activation of carcinogenic substances. !$#cross-references MUID:83160754; PMID:6300027 !$#accession I54796 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 6-491 ##label RES !'##cross-references GB:M37134; NID:g203784; PIDN:AAC42028.1; !1PID:g203785 GENETICS !$#gene CYP2B1 !$#introns 57/3; 112/1; 162/1; 215/3; 274/3; 322/1; 384/3; 432/1 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; endoplasmic reticulum; !1heme; iron; metalloprotein; monooxygenase; oxidoreductase; !1phosphoprotein; transmembrane protein FEATURE !$295-458 #domain cytochrome P450 homology #label P45\ !$302 #active_site Thr #status predicted\ !$436 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 491 #molecular-weight 55919 #checksum 2524 SEQUENCE /// ENTRY O4RTP2 #type complete TITLE cytochrome P450 2B2 - rat ALTERNATE_NAMES cytochrome P450 PB-4; cytochrome P450, phenobarbital-inducible; cytochrome P450e-L CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 04-Dec-1986 #sequence_revision 17-May-1996 #text_change 01-Dec-2000 ACCESSIONS A21162; A00177; B00176; B92255; S15589; A21872; A32736; !1S03855; I59060 REFERENCE A21162 !$#authors Mizukami, Y.; Sogawa, K.; Suwa, Y.; Muramatsu, M.; !1Fujii-Kuriyama, Y. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:3958-3962 !$#title Gene structure of a phenobarbital-inducible cytochrome P-450 !1in rat liver. !$#cross-references MUID:83247397; PMID:6306654 !$#accession A21162 !'##molecule_type DNA !'##residues 1-472,'M',474-491 ##label MIZ !'##cross-references EMBL:J00728; NID:g203845; PIDN:AAA41056.1; !1PID:g203847 !'##note the authors translated the codon AGT for residue 4 as Thr, and !1ATG for residue 376 as Ala REFERENCE A00177 !$#authors Frey, A.B.; Waxman, D.J.; Kreibich, G. !$#journal J. Biol. Chem. (1985) 260:15253-15265 !$#title The structure of phenobarbital-inducible rat liver !1cytochrome P-450 isoenzyme PB-4. Production and !1characterization of site-specific antibodies. !$#cross-references MUID:86059379; PMID:3877725 !$#accession A00177 !'##molecule_type protein !'##residues 1-291,'P',293-320,'AE',323-475,'D',477-491 ##label FRE REFERENCE A93912 !$#authors Fujii-Kuriyama, Y.; Mizukami, Y.; Kawajiri, K.; Sogawa, K.; !1Muramatsu, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:2793-2797 !$#title Primary structure of a cytochrome p-450: coding nucleotide !1sequence of phenobarbital-inducible cytochrome p450 cDNA !1from rat liver. !$#cross-references MUID:82222224; PMID:6953431 !$#accession B00176 !'##molecule_type mRNA !'##residues 6-359,'S',361-362,'V',364-366,'V',368-406,'S',408-416,'N', !1418,'A',420-477,'G',479-491 ##label FUJ !'##note nucleotide sequence for residues 1-5 is not given !'##note the authors translated the codon GAT for residue 166 as Glu, !1CTG for residue 292 as Pro, and CGA for residue 378 as Gln REFERENCE A93925 !$#authors Fujii-Kuriyama, Y.; Mizukami, Y.; Kawajiri, K.; Sogawa, K.; !1Muramatsu, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:5443 !$#title Primary structure of a cytochrome P450: coding nucleotide !1sequence of phenobarbital-inducible cytochrome P-450 cDNA !1from rat liver. !$#contents annotation; revisions !$#note the mistranslations in reference A93912 are acknowledged REFERENCE A92255 !$#authors Botelho, L.H.; Ryan, D.E.; Levin, W. !$#journal J. Biol. Chem. (1979) 254:5635-5640 !$#title Amino acid compositions and partial amino acid sequences of !1three highly purified forms of liver microsomal cytochrome !1P-450 from rats treated with polychlorinated biphenyls, !1phenobarbital, or 3-methylcholanthrene. !$#cross-references MUID:79194111; PMID:109438 !$#accession B92255 !'##molecule_type protein !'##residues 1-3,'T',5-22 ##label BOT REFERENCE S15589 !$#authors Lacroix, D.; Desrochers, M.; Lambert, M.; Anderson, A. !$#journal Gene (1990) 86:201-207 !$#title Alternative splicing of mRNA encoding rat liver cytochrome !1P450e (P450IIB2). !$#cross-references MUID:90215299; PMID:2323573 !$#accession S15589 !'##molecule_type mRNA !'##residues 105-113,'F',115-274,'VSPAWMRE',275-321,'E',323-491 ##label !1LAC !'##cross-references EMBL:M34452; NID:g203679; PIDN:AAA41004.1; !1PID:g203680 !'##note translation of the nucleotide sequence is not complete REFERENCE A21872 !$#authors Philips, I.R.; Shephard, E.A.; Ashworth, A.; Rabin, B.R. !$#journal Gene (1983) 24:41-52 !$#accession A21872 !'##molecule_type mRNA !'##residues 168-321,'E',323-443,'K',445-491 ##label PHI REFERENCE A32736 !$#authors Affolter, M.; Anderson, A. !$#journal Biochem. Biophys. Res. Commun. (1984) 118:655-662 !$#title Segmental homologies in the coding and 3' non-coding !1sequences of rat liver cytochrome P-450e and P-450b cDNAs !1and cytochrome P-450e-like genes. !$#cross-references MUID:84153837; PMID:6322758 !$#accession A32736 !'##molecule_type mRNA !'##residues 385-491 ##label AFF !'##cross-references GB:K01626; NID:g203782; PIDN:AAA41037.1; !1PID:g203783 REFERENCE S03854 !$#authors Oesch, F.; Waxman, D.J.; Morrissey, J.J.; Honscha, W.; !1Kissel, W.; Friedberg, T. !$#journal Arch. Biochem. Biophys. (1989) 270:23-32 !$#title Antibodies targeted against hypervariable and constant !1regions of cytochromes P450IIB1 and P450IIB2. !$#cross-references MUID:89192373; PMID:2539047 !$#accession S03855 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 329-358,'AS',361;362,363-380;402-423 ##label OES REFERENCE I59060 !$#authors Atchison, M.L.; Adesnik, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:2300-2304 !$#title Gene conversion in a cytochrome P-450 gene family. !$#cross-references MUID:86205943; PMID:3458196 !$#accession I59060 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 323-431 ##label RES !'##cross-references GB:M13234; NID:g203848; PIDN:AAA41057.1; !1PID:g554434 GENETICS !$#gene CYP2B2 !$#introns 384/3 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS alternative splicing; chromoprotein; electron transfer; !1endoplasmic reticulum; heme; iron; metalloprotein; !1monooxygenase; oxidoreductase; phosphoprotein; transmembrane !1protein FEATURE !$295-458 #domain cytochrome P450 homology #label P45\ !$436 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 491 #molecular-weight 55902 #checksum 2838 SEQUENCE /// ENTRY O4RBPC #type complete TITLE cytochrome P450 2B4 - rabbit ALTERNATE_NAMES cytochrome P450-LM2 CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 20-Sep-1984 #sequence_revision 20-Sep-1984 #text_change 03-Mar-2000 ACCESSIONS A00179; A61538; S31279; A00178; B27717; C27717; E27717 REFERENCE A00179 !$#authors Tarr, G.E.; Black, S.D.; Fujita, V.S.; Coon, M.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:6552-6556 !$#title Complete amino acid sequence and predicted membrane topology !1of phenobarbital-induced cytochrome P-450 (isozyme 2) from !1rabbit liver microsomes. !$#cross-references MUID:84042509; PMID:6579541 !$#accession A00179 !'##molecule_type protein !'##residues 1-491 ##label TAR REFERENCE A61538 !$#authors Parandoosh, Z.; Fujita, V.S.; Coon, M.J.; Philpot, R.M. !$#journal Drug Metab. Dispos. (1987) 15:59-67 !$#title Cytochrome P-450 isozymes 2 and 5 in rabbit lung and liver. !1Comparisons of structure and inducibility. !$#cross-references MUID:87161284; PMID:2881760 !$#accession A61538 !'##molecule_type protein !'##residues 1-24 ##label PAR REFERENCE S31277 !$#authors Gasser, R.; Negishi, M.; Philpot, R.M. !$#journal Mol. Pharmacol. (1988) 33[32]:22-30 !$#title Primary structures of multiple forms of cytochrome P-450 !1isozyme 2 derived from rabbit pulmonary and hepatic cDNAs. !$#note header on page 22 gives volume number as 32 !$#accession S31279 !'##molecule_type mRNA !'##residues 1-491 ##label GAS !'##cross-references EMBL:M20856; NID:g164958; PIDN:AAA65840.1; !1PID:g164959 REFERENCE A00178 !$#authors Heinemann, F.S.; Ozols, J. !$#journal J. Biol. Chem. (1983) 258:4195-4201 !$#title The complete amino acid sequence of rabbit !1phenobarbital-induced liver microsomal cytochrome P-450. !$#cross-references MUID:83160983; PMID:6833251 !$#accession A00178 !'##molecule_type protein !'##residues 1-90,'E',92-94,96,95,97-98,101-134,'GY',137-140,'G', !1142-192,'K',194-220,'S',222-302,'A',304-460,'GNLSL',466-491 !1##label HEI REFERENCE A90538 !$#authors Komori, M.; Imai, Y.; Tsunasawa, S.; Sato, R. !$#journal Biochemistry (1988) 27:73-80 !$#title Microheterogeneity in the major phenobarbital-inducible !1forms of rabbit liver microsomal cytochrome P-450 as !1revealed by nucleotide sequencing of cloned cDNAs. !$#cross-references MUID:88163620; PMID:2831964 !$#accession B27717 !'##molecule_type mRNA !'##residues 301-313,'L',315-419,'M',421-491 ##label KOM !'##experimental_source clone b14 !$#accession C27717 !'##molecule_type mRNA !'##residues 52-103,'M',105-173,'V',175-220,'S',222-313,'L',315-424,'C', !1426-491 ##label KO2 !'##experimental_source clone b46 !'##note the authors translated the codon AAG for residue 191 as Arg !$#accession E27717 !'##molecule_type mRNA !'##residues 297-479,'L',481-491 ##label KO3 !'##experimental_source clone b54 COMMENT Cytochromes P450 are a group of membrane-bound hemoprotein !1monooxygenases. In liver microsomes, this enzyme is involved !1in an NADPH-dependent electron transport pathway and !1oxidizes a wide variety of structurally unrelated compounds, !1including steroids, fatty acids, and xenobiotics. GENETICS !$#gene CYP2B4 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; endoplasmic reticulum; !1heme; iron; metalloprotein; monooxygenase; oxidoreductase; !1phosphoprotein; transmembrane protein FEATURE !$295-458 #domain cytochrome P450 homology #label P45\ !$436 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 491 #molecular-weight 55713 #checksum 3972 SEQUENCE /// ENTRY O4RBC6 #type complete TITLE cytochrome P450 2C16 - rabbit ALTERNATE_NAMES cytochrome P450 1a, phenobarbital-inducible, hepatic CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Mar-2000 ACCESSIONS S12765; A27479 REFERENCE S12765 !$#authors Hassett, C.; Omiecinski, C.J. !$#journal Nucleic Acids Res. (1990) 18:1429-1434 !$#title Sequence and gene expression of rabbit cytochrome P450 !1IIC16: comparison to highly related family members. !$#cross-references MUID:90221865; PMID:2326187 !$#accession S12765 !'##molecule_type mRNA !'##residues 1-487 ##label HAS !'##cross-references EMBL:M29968; NID:g164966; PIDN:AAA31226.1; !1PID:g164967 !'##experimental_source strain New Zealand White !'##note the authors translated the codon AGG for residue 330 as His REFERENCE A27479 !$#authors Hassett, C.; Omiecinski, C.J. !$#journal Biochem. Biophys. Res. Commun. (1987) 149:326-333 !$#title Use of a conserved consensus oligomer in the identification !1of cytochrome P-450 mRNAs. !$#cross-references MUID:88106440; PMID:3426576 !$#accession A27479 !'##molecule_type mRNA !'##residues 414-487 ##label HA2 !'##cross-references GB:M18376; NID:g164922; PIDN:AAA31215.1; !1PID:g164923 GENETICS !$#gene CYP2C16 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; monooxygenase; oxidoreductase; transmembrane !1protein FEATURE !$1-20 #domain transmembrane #status predicted #label TMM\ !$291-454 #domain cytochrome P450 homology #label P45\ !$432 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 487 #molecular-weight 55541 #checksum 946 SEQUENCE /// ENTRY O4RBP4 #type complete TITLE progesterone monooxygenase (EC 1.14.99.4) cytochrome P450 2C5 - rabbit ALTERNATE_NAMES cytochrome P450 form 1; progesterone 21-hydroxylase ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 03-Mar-2000 ACCESSIONS A00180; A37828 REFERENCE A00180 !$#authors Tukey, R.H.; Okino, S.; Barnes, H.; Griffin, K.J.; Johnson, !1E.F. !$#journal J. Biol. Chem. (1985) 260:13347-13354 !$#title Multiple gene-like sequences related to the rabbit hepatic !1progesterone 21-hydroxylase cytochrome P-450 1. !$#cross-references MUID:86033780; PMID:3902818 !$#accession A00180 !'##molecule_type mRNA !'##residues 1-487 ##label TUK !'##cross-references EMBL:M11299 REFERENCE A37828 !$#authors Pendurthi, U.R.; Lamb, J.G.; Nguyen, N.; Johnson, E.F.; !1Tukey, R.H. !$#journal J. Biol. Chem. (1990) 265:14662-14668 !$#title Characterization of the CYP2C5 gene in 21L III/J rabbits. !1Allelic variation affects the expression of P450IIC5. !$#cross-references MUID:90354466; PMID:2387874 !$#accession A37828 !'##molecule_type DNA !'##residues 1-96,'R',98-487 ##label PEN !'##cross-references GB:M55664; GB:J05575; NID:g164968; PIDN:AAA63461.1; !1PID:g164969 GENETICS !$#gene CYP2C5 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; endoplasmic reticulum; !1heme; iron; metalloprotein; monooxygenase; oxidoreductase; !1transmembrane protein FEATURE !$291-454 #domain cytochrome P450 homology #label P45\ !$432 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 487 #molecular-weight 55220 #checksum 2127 SEQUENCE /// ENTRY O4RBP1 #type complete TITLE cytochrome P450 2C1 - rabbit CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 20-Sep-1984 #sequence_revision 16-Feb-1996 #text_change 03-Mar-2000 ACCESSIONS A00181; A34257 REFERENCE A90484 !$#authors Leighton, J.K.; DeBrunner-Vossbrinck, B.A.; Kemper, B. !$#journal Biochemistry (1984) 23:204-210 !$#title Isolation and sequence analysis of three cloned cDNAs for !1rabbit liver proteins that are related to rabbit cytochrome !1P-450 (form 2), the major phenobarbital-inducible form. !$#cross-references MUID:84128536; PMID:6546520 !$#accession A00181 !'##molecule_type mRNA !'##residues 11-490 ##label LE2 !'##cross-references EMBL:K01522; NID:g164914; PIDN:AAA31211.1; !1PID:g164915 !'##note the authors translated the codon CAA for residue 48 as Lys, GAT !1for residue 133 as Asn, CTG for residue 291 as Val, AGT for !1residue 292 as Thr, GTG for residue 439 as Ala, and GCC for !1residue 441 as Val REFERENCE A94658 !$#authors Zhao, J.; Chan, G.; Govind, S.; Bell, P.; Kemper, B. !$#journal DNA Cell Biol. (1990) 9:37-48 !$#title Structure of 5' regions and expression of !1phenobarbital-inducible rabbit cytochrome P450IIC genes. !$#cross-references MUID:90197893; PMID:2317269 !$#accession A34257 !'##molecule_type DNA !'##residues 1-24 ##label ZHA !'##cross-references GB:M74199 GENETICS !$#gene CYP2C1 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; endoplasmic reticulum; !1heme; iron; metalloprotein; monooxygenase; oxidoreductase; !1transmembrane protein FEATURE !$294-457 #domain cytochrome P450 homology #label P45\ !$435 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 490 #molecular-weight 55614 #checksum 4387 SEQUENCE /// ENTRY O4RBP2 #type complete TITLE laurate omega-minus-1 hydroxylase (EC 1.14.14.-) cytochrome P450 2C2 - rabbit ALTERNATE_NAMES cytochrome P450 PBc2 ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 20-Sep-1984 #sequence_revision 16-Feb-1996 #text_change 03-Mar-2000 ACCESSIONS A27718; A00182; S15587 REFERENCE A90540 !$#authors Imai, Y.; Komori, M.; Sato, R. !$#journal Biochemistry (1988) 27:80-88 !$#title Comparison of primary structures deduced from cDNA !1nucleotide sequences for various forms of liver microsomal !1cytochrome P-450 from phenobarbital-treated rabbits. !$#cross-references MUID:88163622; PMID:2831965 !$#accession A27718 !'##molecule_type mRNA !'##residues 1-490 ##label IMA !'##experimental_source clone HP2 REFERENCE A90484 !$#authors Leighton, J.K.; DeBrunner-Vossbrinck, B.A.; Kemper, B. !$#journal Biochemistry (1984) 23:204-210 !$#title Isolation and sequence analysis of three cloned cDNAs for !1rabbit liver proteins that are related to rabbit cytochrome !1P-450 (form 2), the major phenobarbital-inducible form. !$#cross-references MUID:84128536; PMID:6546520 !$#accession A00182 !'##molecule_type mRNA !'##residues 12-470,'L',472-490 ##label LEI !'##cross-references EMBL:K01521; NID:g164912; PIDN:AAA31210.1; !1PID:g164913 REFERENCE S15587 !$#authors Govind, S.; Bell, P.A.; Kemper, B. !$#journal DNA (1986) 5:371-382 !$#title Structure of genes in the cytochrome P-450PBc subfamily: !1conservation of intron locations in the !1phenobarbital-inducible family. !$#cross-references MUID:87053173; PMID:3780371 !$#accession S15587 !'##status preliminary !'##molecule_type DNA !'##residues 1-22 ##label GOV !'##cross-references EMBL:M14955; NID:g164908; PIDN:AAA31208.1; !1PID:g164909 GENETICS !$#gene CYP2C2 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; endoplasmic reticulum; !1heme; iron; metalloprotein; monooxygenase; oxidoreductase; !1transmembrane protein FEATURE !$294-457 #domain cytochrome P450 homology #label P45\ !$435 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 490 #molecular-weight 55791 #checksum 1914 SEQUENCE /// ENTRY O4RBP3 #type complete TITLE progesterone 16alpha-hydroxylase (EC 1.14.-.-) cytochrome P450 2C3 - rabbit ALTERNATE_NAMES cytochrome P450 form 3b; progesterone 6beta-hydroxylase ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 20-Sep-1984 #sequence_revision 16-Feb-1996 #text_change 03-Mar-2000 ACCESSIONS A00183; A34534; A22606 REFERENCE A90484 !$#authors Leighton, J.K.; DeBrunner-Vossbrinck, B.A.; Kemper, B. !$#journal Biochemistry (1984) 23:204-210 !$#title Isolation and sequence analysis of three cloned cDNAs for !1rabbit liver proteins that are related to rabbit cytochrome !1P-450 (form 2), the major phenobarbital-inducible form. !$#cross-references MUID:84128536; PMID:6546520 !$#accession A00183 !'##molecule_type mRNA !'##residues 87-489 ##label LE2 !'##cross-references EMBL:K01523 !'##note the authors translated the codon AGC for residue 216 as Tyr, !1TGG for residue 360 as Leu, TTC for residue 361 as Val, and !1CTG for residue 471 as Val. An extra Phe between residues !1222 and 223 and the codon given for residue 299 (TAG) are !1inconsistent with the codon usage table and the authors' !1translation REFERENCE A34534 !$#authors Chan, G.; Kemper, B. !$#journal Biochemistry (1990) 29:3743-3750 !$#title Structure of the rabbit cytochrome P450IIC3 gene, a !1constitutive member of the P450IIC subfamily. !$#cross-references MUID:90254101; PMID:2340269 !$#accession A34534 !'##molecule_type DNA !'##residues 1-110 ##label CHA !'##cross-references GB:M31245; GB:J02901; GB:M31246; GB:M31247 REFERENCE A22606 !$#authors Ozols, J.; Heinemann, F.S.; Johnson, E.F. !$#journal J. Biol. Chem. (1985) 260:5427-5434 !$#title The complete amino acid sequence of a constitutive form of !1liver microsomal cytochrome P-450. !$#cross-references MUID:85182688; PMID:3988762 !$#accession A22606 !'##molecule_type protein !'##residues 1-48,'D',50-81,'G',83,'I',85-88,'Y',90-215,'Y',217-222,'G', !1223-337,'S',339-341,'S',343-359,'LV',362-428,'T',430-470, !1'V',472-489 ##label OZO GENETICS !$#gene CYP2C3 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; endoplasmic reticulum; !1heme; iron; metalloprotein; monooxygenase; oxidoreductase; !1transmembrane protein FEATURE !$293-456 #domain cytochrome P450 homology #label P45\ !$434 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 489 #molecular-weight 55910 #checksum 9125 SEQUENCE /// ENTRY O4HUPB #type fragment TITLE cytochrome P450 2A3, hepatic - human (fragment) ALTERNATE_NAMES cytochrome P450-LM2 CONTAINS unspecific monooxygenase (EC 1.14.14.1) ORGANISM #formal_name Homo sapiens #common_name man DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 03-Mar-2000 ACCESSIONS A00190 REFERENCE A00190 !$#authors Phillips, I.R.; Shephard, E.A.; Ashworth, A.; Rabin, B.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:983-987 !$#title Isolation and sequence of a human cytochrome P-450 cDNA !1clone. !$#cross-references MUID:85140280; PMID:3856261 !$#accession A00190 !'##molecule_type mRNA !'##residues 1-331 ##label PHI !'##cross-references GB:K03192; NID:g181321; PIDN:AAA52147.1; !1PID:g181322 COMMENT Cytochromes P450 are a group of membrane-bound hemoprotein !1monooxygenases. In liver microsomes, this enzyme is involved !1in an NADPH-dependent electron transport pathway and !1oxidizes a wide variety of structurally unrelated compounds, !1including steroids, fatty acids, and xenobiotics. GENETICS !$#gene GDB:CYP2A3 !'##cross-references GDB:377635 !$#map_position 19q13.2-19q13.2 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; endoplasmic reticulum; !1heme; iron; metalloprotein; monooxygenase; oxidoreductase; !1transmembrane protein FEATURE !$135-298 #domain cytochrome P450 homology #label P45\ !$276 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 331 #checksum 2690 SEQUENCE /// ENTRY O4HUA6 #type complete TITLE coumarin 7-hydroxylase (EC 1.14.14.-) cytochrome P450 2A6 - human ALTERNATE_NAMES CYP450 2A3; CYP450 2A3v; CYP450 2A4; cytochrome P450MP81 ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Mar-2000 ACCESSIONS S04698; S04581; A61272; S05946; A34271; B34271; S17220; !1S09329 REFERENCE S04698 !$#authors Yamano, S.; Nagata, K.; Yamazoe, Y.; Kato, R.; Gelboin, !1H.V.; Gonzalez, F.J. !$#journal Nucleic Acids Res. (1989) 17:4888 !$#title cDNA and deduced amino acid sequences of human P450 IIA3 !1(CYP2A3). !$#cross-references MUID:89315238; PMID:2748347 !$#accession S04698 !'##molecule_type mRNA !'##residues 1-494 ##label YAM !'##cross-references EMBL:X13929 !'##note the authors identified this protein as cytochrome P450IIA3 REFERENCE S04581 !$#authors Miles, J.S.; Bickmore, W.; Brook, J.D.; McLaren, A.W.; !1Meehan, R.; Wolf, C.R. !$#journal Nucleic Acids Res. (1989) 17:2907-2917 !$#title Close linkage of the human cytochrome P450IIA and P450IIB !1gene subfamilies: implications for the assignment of !1substrate specificity. !$#cross-references MUID:89263705; PMID:2726448 !$#accession S04581 !'##molecule_type mRNA !'##residues 6-28,'N',30-254,'K',256-325,'Q',327-494 ##label MIL !'##cross-references EMBL:X13897; NID:g29546; PIDN:CAA32097.1; !1PID:g29547 !'##note 326-Lys and 386-Leu were also found REFERENCE A61272 !$#authors Yun, C.H.; Shimada, T.; Guengerich, F.P. !$#journal Mol. Pharmacol. (1991) 40:679-685 !$#title Purification and characterization of human liver microsomal !1cytochrome P-450 2A6. !$#cross-references MUID:92049260; PMID:1944238 !$#accession A61272 !'##molecule_type protein !'##residues 1-13 ##label YUN !'##experimental_source liver REFERENCE S05946 !$#authors Landsman, D. !$#submission submitted to the EMBL Data Library, January 1989 !$#accession S05946 !'##molecule_type mRNA !'##residues 1-159,'H',161-494 ##label LAN !'##cross-references EMBL:X13930; NID:g30331; PIDN:CAA32118.1; !1PID:g30332 REFERENCE A34271 !$#authors Yamano, S.; Tatsuno, J.; Gonzalez, F.J. !$#journal Biochemistry (1990) 29:1322-1329 !$#title The CYP2A3 gene product catalyzes coumarin 7-hydroxylation !1in human liver microsomes. !$#cross-references MUID:90212623; PMID:2322567 !$#accession A34271 !'##molecule_type mRNA !'##residues 1-494 ##label YA2 !'##cross-references GB:M33318; NID:g180986; PIDN:AAA52067.1; !1PID:g180987; GB:M33316 !'##note this allele was designated cytochrome P450 2A3 !$#accession B34271 !'##molecule_type mRNA !'##residues 1-159,'H',161-494 ##label YA3 !'##cross-references GB:M33318; GB:M33316 !'##note this allele was designated cytochrome P450 2A3v REFERENCE S17220 !$#authors Maurice, M.; Emiliani, S.; Dalet-Beluche, I.; Derancourt, !1J.; Lange, R. !$#journal Eur. J. Biochem. (1991) 200:511-517 !$#title Isolation and characterization of a cytochrome P450 of the !1IIA subfamily from human liver microsomes. !$#cross-references MUID:91364703; PMID:1889415 !$#accession S17220 !'##molecule_type protein !'##residues 1-13,'X',15,'X',17-20 ##label MAU GENETICS !$#gene GDB:CYP2A6 !'##cross-references GDB:377803 !$#map_position 19q13.2-19q13.2 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; endoplasmic reticulum; !1heme; iron; metalloprotein; monooxygenase; oxidoreductase; !1transmembrane protein FEATURE !$298-461 #domain cytochrome P450 homology #label CYP\ !$439 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 494 #molecular-weight 56517 #checksum 5751 SEQUENCE /// ENTRY S45644 #type complete TITLE cytochrome P450 2K1 - rainbow trout CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Oncorhynchus mykiss #common_name rainbow trout DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS S45644; S62858 REFERENCE S45644 !$#authors Buhler, D.R.; Yang, Y.H.; Dreher, T.W.; Miranda, C.L.; Wang, !1J.L. !$#journal Arch. Biochem. Biophys. (1994) 312:45-51 !$#title Cloning and sequencing of the major rainbow trout !1constitutive cytochrome P450 (CYP2K1): identification of a !1new cytochrome P450 gene subfamily and its expression in !1mature rainbow trout liver and trunk kidney. !$#cross-references MUID:94304231; PMID:8031145 !$#accession S45644 !'##molecule_type mRNA !'##residues 1-504 ##label BUH !'##cross-references EMBL:L11528; NID:g309631; PIDN:AAA52078.1; !1PID:g309632 !$#accession S62858 !'##molecule_type protein !'##residues 1-15 ##label BUW GENETICS !$#gene CYP2K1 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxidoreductase FEATURE !$307-469 #domain cytochrome P450 homology #label CYP\ !$447 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 504 #molecular-weight 56792 #checksum 2802 SEQUENCE /// ENTRY S68856 #type complete TITLE cytochrome P450 2L - spiny lobster CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Panulirus argus #common_name spiny lobster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-May-2000 ACCESSIONS S68856; S74194 REFERENCE S68856 !$#authors James, M.O.; Boyle, S.M.; Trapido-Rosenthal, H.G.; Smith, !1W.C.; Greenberg, R.M.; Shiverick, K.T. !$#journal Arch. Biochem. Biophys. (1996) 329:31-38 !$#title cDNA and protein sequence of a major form of P450, CYP2L, in !1the hepatopancreas of the spiny lobster, Panulirus argus. !$#cross-references MUID:96201120; PMID:8619632 !$#accession S68856 !'##molecule_type mRNA !'##residues 1-492 ##label JAM !'##cross-references EMBL:U44826; NID:g1304739; PIDN:AAB03106.1; !1PID:g1304740 !'##experimental_source hepatopancreas !$#accession S74194 !'##molecule_type protein !'##residues 1-10,'X',12-39 ##label JAN GENETICS !$#gene CYP2L1 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; endoplasmic reticulum; !1heme; iron; metalloprotein; monooxygenase; oxidoreductase; !1phosphoprotein; transmembrane protein FEATURE !$295-458 #domain cytochrome P450 homology #label CYP\ !$436 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 492 #molecular-weight 56767 #checksum 4099 SEQUENCE /// ENTRY O4HU6 #type complete TITLE aryl hydrocarbon (benzo[a]pyrene) hydroxylase (EC 1.14.14.-) cytochrome P450 1A1 - human ALTERNATE_NAMES cytochrome P450c ORGANISM #formal_name Homo sapiens #common_name man DATE 28-Dec-1987 #sequence_revision 01-Mar-1996 #text_change 03-Mar-2000 ACCESSIONS A24797; S15803; S16714; B23585; S19336 REFERENCE A24797 !$#authors Kawajiri, K.; Watanabe, J.; Gotoh, O.; Tagashira, Y.; !1Sogawa, K.; Fujii-Kuriyama, Y. !$#journal Eur. J. Biochem. (1986) 159:219-225 !$#title Structure and drug inducibility of the human cytochrome !1P-450c gene. !$#cross-references MUID:87004629; PMID:3019683 !$#accession A24797 !'##molecule_type DNA !'##residues 1-512 ##label KAW !'##cross-references EMBL:X04300; NID:g30346; PIDN:CAA27843.1; !1PID:g30347 REFERENCE S15803 !$#authors Jaiswal, A.K.; Gonzalez, F.J.; Nebert, D.W. !$#journal Nucleic Acids Res. (1985) 13:4503-4520 !$#title Human P(1)-450 gene sequence and correlation of mRNA with !1genetic differences in benzo[a]pyrene metabolism. !$#cross-references MUID:85242117; PMID:2989797 !$#accession S15803 !'##molecule_type DNA !'##residues 1-380,'L',382-461,'V',463-512 ##label JAI !'##cross-references EMBL:X02612; NID:g30340; PIDN:CAA26458.1; !1PID:g30341 REFERENCE S16714 !$#authors Jaiswal, A.K.; Gonzalez, F.J.; Nebert, D.W. !$#journal Science (1985) 228:80-83 !$#title Human dioxin-inducible cytochrome P(1)-450: complementary !1DNA and amino acid sequence. !$#cross-references MUID:85142181; PMID:3838385 !$#accession S16714 !'##molecule_type mRNA !'##residues 1-461,'V',463-512 ##label JAI1 !'##cross-references EMBL:K03191 REFERENCE A90953 !$#authors Quattrochi, L.C.; Okino, S.T.; Pendurthi, U.R.; Tukey, R.H. !$#journal DNA (1985) 4:395-400 !$#title Cloning and isolation of human cytochrome P-450 cDNAs !1homologous to dioxin-inducible rabbit mRNAs encoding P-450 4 !1and P-450 6. !$#cross-references MUID:86081170; PMID:3000715 !$#accession B23585 !'##molecule_type mRNA !'##residues 295-461,'V',463-484 ##label QUA GENETICS !$#gene GDB:CYP1A1 !'##cross-references GDB:120604; OMIM:108330 !$#map_position 15q22-15q24 !$#introns 275/3; 318/1; 348/1; 389/2; 418/2 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; endoplasmic reticulum; !1heme; iron; metalloprotein; monooxygenase; oxidoreductase; !1transmembrane protein FEATURE !$314-479 #domain cytochrome P450 homology #label CYP\ !$457 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 512 #molecular-weight 58165 #checksum 7447 SEQUENCE /// ENTRY O4MSM1 #type complete TITLE aryl hydrocarbon (benzo[a]pyrene) hydroxylase (EC 1.14.14.-) cytochrome P450 1A1 - mouse ALTERNATE_NAMES cytochrome P1 450; cytochrome P450-P1 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 17-May-1985 #sequence_revision 01-Mar-1996 #text_change 03-Mar-2000 ACCESSIONS A23923; S15588; A00184; A45955; A24953; C24406 REFERENCE A92519 !$#authors Gonzalez, F.J.; Kimura, S.; Nebert, D.W. !$#journal J. Biol. Chem. (1985) 260:5040-5049 !$#title Comparison of the flanking regions and introns of the mouse !12,3,7,8-tetrachlorodibenzo-p-dioxin-inducible cytochrome !1P1-450 and P3-450 genes. !$#cross-references MUID:85182627; PMID:3988744 !$#accession A23923 !'##molecule_type DNA !'##residues 1-524 ##label GON !'##cross-references EMBL:M10021; NID:g192887; PIDN:AAA37507.1; !1PID:g387138 REFERENCE S15588 !$#authors Kimura, S.; Smith, H.H.; Hankinson, O.; Nebert, D.W. !$#journal EMBO J. (1987) 6:1929-1933 !$#title Analysis of two benzo[a]pyrene-resistant mutants of the !1mouse hepatoma Hepa-1 P(1)450 gene via cDNA expression in !1yeast. !$#cross-references MUID:88004400; PMID:3308449 !$#accession S15588 !'##molecule_type mRNA !'##residues 1-524 ##label KIM !'##cross-references EMBL:Y00071; NID:g50625; PIDN:CAA68277.1; !1PID:g50626 REFERENCE A92443 !$#authors Kimura, S.; Gonzalez, F.J.; Nebert, D.W. !$#journal J. Biol. Chem. (1984) 259:10705-10713 !$#title The murine Ah locus. Comparison of the complete cytochrome !1P-1-450 and P-3-450 cDNA nucleotide and amino acid !1sequences. !$#cross-references MUID:84289486; PMID:6547952 !$#accession A00184 !'##molecule_type mRNA !'##residues 4-524 ##label KI2 !'##cross-references EMBL:K02588; NID:g192885; PIDN:AAA37506.1; !1PID:g309204 REFERENCE A45955 !$#authors Peterson, T.C.; Gonzalez, F.J.; Nebert, D.W. !$#journal Biochem. Pharmacol. (1986) 35:2107-2114 !$#title Methylation differences in the murine P-1-450 and P-3-450 !1genes in wild-type and mutant hepatoma cell culture. !$#cross-references MUID:86269072; PMID:2425809 !$#accession A45955 !'##molecule_type DNA !'##residues 280-321 ##label PET !'##cross-references GB:M25623; NID:g200175; PIDN:AAA39868.1; !1PID:g554249 REFERENCE A91515 !$#authors Gonzalez, F.J.; Mackenzie, P.I.; Kimura, S.; Nebert, D.W. !$#journal Gene (1984) 29:281-292 !$#title Isolation and characterization of full-length mouse cDNA and !1genomic clones of 3-methylcholanthrene-inducible cytochrome !1P1-450 and P3-450. !$#cross-references MUID:85028449; PMID:6548461 !$#accession A24953 !'##molecule_type mRNA !'##residues 4-33 ##label GO2 !'##cross-references EMBL:M10021 REFERENCE A24406 !$#authors Cheng, K.C.; Park, S.S.; Krutzsch, H.C.; Grantham, P.H.; !1Gelboin, H.V.; Friedman, F.K. !$#journal Biochemistry (1986) 25:2397-2402 !$#title Amino-terminal sequence and structure of monoclonal antibody !1immunopurified cytochromes P-450. !$#cross-references MUID:86243357; PMID:3718958 !$#accession C24406 !'##molecule_type protein !'##residues 2-23,'X',25 ##label CHE !'##experimental_source strain C57BL/6 REFERENCE A92495 !$#authors Gonzalez, F.J.; Kimura, S.; Nebert, D.W. !$#journal J. Biol. Chem. (1985) 260:11884-11889 !$#contents annotation GENETICS !$#gene Cyp1a1 !$#map_position 9 !$#introns 279/3; 322/1; 352/1; 393/2; 422/2 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; endoplasmic reticulum; !1heme; iron; metalloprotein; monooxygenase; oxidoreductase; !1transmembrane protein FEATURE !$318-483 #domain cytochrome P450 homology #label P45\ !$461 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 524 #molecular-weight 59229 #checksum 6165 SEQUENCE /// ENTRY O4RTMC #type complete TITLE unspecific monooxygenase (EC 1.14.14.1) cytochrome P450 1A1, hepatic - rat ALTERNATE_NAMES cytochrome P450 MC2; cytochrome P450, 57K, 3-methylcholanthrene-inducible; cytochrome P450c ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 17-May-1985 #sequence_revision 27-Nov-1985 #text_change 03-Mar-2000 ACCESSIONS A00185; A93513; A24406; D60822; S15584; S69265; S09617 REFERENCE A94002 !$#authors Sogawa, K.; Gotoh, O.; Kawajiri, K.; Fujii-Kuriyama, Y. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:5066-5070 !$#title Distinct organization of methylcholanthrene- and !1phenobarbital- inducible cytochrome P-450 genes in the rat. !$#cross-references MUID:84298082; PMID:6089174 !$#accession A00185 !'##molecule_type DNA !'##residues 1-524 ##label SOG !'##cross-references GB:K02246; NID:g203760; PIDN:AAA41027.1; !1PID:g203761 REFERENCE A93513 !$#authors Yabusaki, Y.; Shimizu, M.; Murakami, H.; Nakamura, K.; Oeda, !1K.; Ohkawa, H. !$#journal Nucleic Acids Res. (1984) 12:2929-2938 !$#title Nucleotide sequence of a full-length cDNA coding for !13-methylcholanthrene-induced rat liver cytochrome P-450MC. !$#cross-references MUID:84169583; PMID:6324135 !$#accession A93513 !'##molecule_type mRNA !'##residues 1-52,'M',54-524 ##label YAB !'##cross-references GB:X00469; NID:g56043; PIDN:CAA25153.1; PID:g56044 REFERENCE A24406 !$#authors Cheng, K.C.; Park, S.S.; Krutzsch, H.C.; Grantham, P.H.; !1Gelboin, H.V.; Friedman, F.K. !$#journal Biochemistry (1986) 25:2397-2402 !$#title Amino-terminal sequence and structure of monoclonal antibody !1immunopurified cytochromes P-450. !$#cross-references MUID:86243357; PMID:3718958 !$#accession A24406 !'##molecule_type protein !'##residues 2-23,'X',25-26 ##label CHE REFERENCE A60822 !$#authors Amelizad, Z.; Narbonne, J.F.; Wolf, C.R.; Robertson, L.W.; !1Oesch, F. !$#journal Biochem. Pharmacol. (1988) 37:3245-3249 !$#title Effect of nutritional imbalances on cytochrome P-450 !1isozymes in rat liver. !$#cross-references MUID:88293549; PMID:3041969 !$#accession D60822 !'##molecule_type protein !'##residues 2-20,'VV' ##label AME REFERENCE S15584 !$#authors Hines, R.N.; Levy, J.B.; Conrad, R.D.; Iversen, P.L.; Shen, !1M.L.; Renli, A.M.; Bresnick, E. !$#journal Arch. Biochem. Biophys. (1985) 237:465-476 !$#title Gene structure and nucleotide sequence for rat cytochrome !1P-450c. !$#cross-references MUID:85147736; PMID:3838427 !$#accession S15584 !'##molecule_type DNA !'##residues 1-493,'S',495-524 ##label HIN !'##cross-references EMBL:M26129; NID:g203754; PIDN:AAA41025.1; !1PID:g203755 !'##note the authors translated the codon GAG for residue 278 as Gly, !1GAG for residue 291 as Gly, and AGT for residue 494 as Ser REFERENCE S69265 !$#authors Cvrk, T.; Hodek, P.; Strobel, H.W. !$#journal Arch. Biochem. Biophys. (1996) 330:142-152 !$#title Identification and characterization of cytochrome P4501A1 !1amino acid residues interacting with a radiolabeled !1photoaffinity diazido-benzphetamine analogue. !$#cross-references MUID:96230251; PMID:8651689 !$#accession S69265 !'##molecule_type protein !'##residues 118-119;122-123,'X';'I',258-260;276-278;436-444;'X', !1462;469-470,'X',472-473;492-500 ##label CVR GENETICS !$#gene CYP1A1 !$#introns 279/3; 322/1; 352/1; 393/1; 422/2 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; endoplasmic reticulum; !1heme; iron; metalloprotein; monooxygenase; oxidoreductase; !1transmembrane protein FEATURE !$11-30 #domain transmembrane #status predicted #label TMM\ !$318-483 #domain cytochrome P450 homology #label P45\ !$461 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 524 #molecular-weight 59393 #checksum 2914 SEQUENCE /// ENTRY O4MSM3 #type complete TITLE acetanilide 4-hydroxylase (EC 1.14.14.-) cytochrome P450 1A2 - mouse ALTERNATE_NAMES cytochrome P450-P3 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 03-Mar-2000 ACCESSIONS B92495; B23923; A00186; A26373; B45955; A93512; B24953; !1E24406; D24406 REFERENCE A92495 !$#authors Gonzalez, F.J.; Kimura, S.; Nebert, D.W. !$#journal J. Biol. Chem. (1985) 260:11884-11889 !$#contents erratum !$#accession B92495 !'##molecule_type DNA !'##residues 1-513 ##label GON2 REFERENCE A92519 !$#authors Gonzalez, F.J.; Kimura, S.; Nebert, D.W. !$#journal J. Biol. Chem. (1985) 260:5040-5049 !$#title Comparison of the flanking regions and introns of the mouse !12,3,7,8-tetrachlorodibenzo-p-dioxin-inducible cytochrome !1P1-450 and P3-450 genes. !$#cross-references MUID:85182627; PMID:3988744 !$#accession B23923 !'##molecule_type DNA !'##residues 1-513 ##label GON !'##cross-references EMBL:M10022; NID:g192892; PIDN:AAA37508.1; !1PID:g387139 REFERENCE A92443 !$#authors Kimura, S.; Gonzalez, F.J.; Nebert, D.W. !$#journal J. Biol. Chem. (1984) 259:10705-10713 !$#title The murine Ah locus. Comparison of the complete cytochrome !1P-1-450 and P-3-450 cDNA nucleotide and amino acid !1sequences. !$#cross-references MUID:84289486; PMID:6547952 !$#accession A00186 !'##molecule_type mRNA !'##residues 1-513 ##label KIM1 !'##cross-references EMBL:K02589 REFERENCE A26373 !$#authors Kimura, S.; Nebert, D.W. !$#journal Nucleic Acids Res. (1986) 14:6765-6766 !$#title cDNA and complete amino acid sequence of mouse P2-450: !1allelic variant of mouse P3-450 gene. !$#cross-references MUID:86312932; PMID:3755821 !$#accession A26373 !'##molecule_type mRNA !'##residues 1-383,'M',385-513 ##label KIM !'##cross-references EMBL:X04283; NID:g50627; PIDN:CAA27832.1; !1PID:g50628 REFERENCE A45955 !$#authors Peterson, T.C.; Gonzalez, F.J.; Nebert, D.W. !$#journal Biochem. Pharmacol. (1986) 35:2107-2114 !$#title Methylation differences in the murine P-1-450 and P-3-450 !1genes in wild-type and mutant hepatoma cell culture. !$#cross-references MUID:86269072; PMID:2425809 !$#accession B45955 !'##status preliminary !'##molecule_type DNA !'##residues 277-315 ##label PET !'##cross-references GB:M25624; NID:g200188; PIDN:AAA39873.1; !1PID:g554250 REFERENCE A93512 !$#authors Kimura, S.; Gonzalez, F.J.; Nebert, D.W. !$#journal Nucleic Acids Res. (1984) 12:2917-2928 !$#title Mouse cytochrome P-3-450: complete cDNA and amino acid !1sequence. !$#cross-references MUID:84169582; PMID:6324134 !$#accession A93512 !'##molecule_type mRNA !'##residues 1-27,'QSLKDPGSQRPEESTRTL',46-513 ##label KIM2 !'##cross-references EMBL:X00479 !'##note the sequences from references A92443 and A93512 differ due to !1frameshifts in the reported nucleotide sequences REFERENCE A91515 !$#authors Gonzalez, F.J.; Mackenzie, P.I.; Kimura, S.; Nebert, D.W. !$#journal Gene (1984) 29:281-292 !$#title Isolation and characterization of full-length mouse cDNA and !1genomic clones of 3-methylcholanthrene-inducible cytochrome !1P1-450 and P3-450. !$#cross-references MUID:85028449; PMID:6548461 !$#accession B24953 !'##molecule_type mRNA !'##residues 1-27,'QSL' ##label GO2 !'##cross-references EMBL:M10022 REFERENCE A24406 !$#authors Cheng, K.C.; Park, S.S.; Krutzsch, H.C.; Grantham, P.H.; !1Gelboin, H.V.; Friedman, F.K. !$#journal Biochemistry (1986) 25:2397-2402 !$#title Amino-terminal sequence and structure of monoclonal antibody !1immunopurified cytochromes P-450. !$#cross-references MUID:86243357; PMID:3718958 !$#accession E24406 !'##molecule_type mRNA !'##residues 2-20,'X',22-26 ##label CHE !'##experimental_source strain DBA/2 !$#accession D24406 !'##molecule_type protein !'##residues 2-20,'X',22-24,'X',26 ##label CH2 !'##experimental_source strain C57BL/6 GENETICS !$#gene Cyp1a2 !$#map_position position 9 !$#introns 276/3; 316/1; 346/1; 387/2; 416/2 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; endoplasmic reticulum; !1heme; iron; metalloprotein; monooxygenase; oxidoreductase; !1transmembrane protein FEATURE !$312-478 #domain cytochrome P450 homology #label P45\ !$456 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 513 #molecular-weight 58183 #checksum 2625 SEQUENCE /// ENTRY O4RBBN #type complete TITLE cytochrome P450 1A2 - rabbit ALTERNATE_NAMES acetanilide 4-hydroxylase (EC 1.14.14.-); cytochrome P450 LM4; cytochrome P450-4 ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 28-May-1986 #sequence_revision 24-Feb-1994 #text_change 03-Mar-2000 ACCESSIONS B27821; S02038; B25143; A00187; A00188; A44250 REFERENCE A91910 !$#authors Kagawa, N.; Mihara, K.; Sato, R. !$#journal J. Biochem. (1987) 101:1471-1479 !$#title Structural analysis of cloned cDNAs for polycyclic !1hydrocarbon-inducible forms of rabbit liver microsomal !1cytochrome P-450. !$#cross-references MUID:88032911; PMID:3667560 !$#accession B27821 !'##molecule_type mRNA !'##residues 1-120,'H',122-516 ##label KA2 !'##cross-references EMBL:X05686; NID:g1540; PIDN:CAA29171.1; PID:g1541 REFERENCE S02038 !$#authors Pompon, D. !$#journal Eur. J. Biochem. (1988) 177:285-293 !$#title cDNA cloning and functional expression in yeast !1Saccharomyces cerevisiae of beta-naphthoflavone-induced !1rabbit liver P-450 LM4 and LM6. !$#cross-references MUID:89052697; PMID:2847925 !$#accession S02038 !'##molecule_type mRNA !'##residues 1-173,'S',175-207,'H',209-232,'S',234-298,'G',300-353,'PG', !1356-516 ##label POM !'##cross-references EMBL:X13853; NID:g1532; PIDN:CAA32066.1; PID:g1533 !'##note the authors translated the codon GAC for residue 276 as Gln and !1CCC for residue 354 as Ala REFERENCE A94056 !$#authors Okino, S.T.; Quattrochi, L.C.; Barnes, H.J.; Osanto, S.; !1Griffin, K.J.; Johnson, E.F.; Tukey, R.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:5310-5314 !$#title Cloning and characterization of cDNAs encoding 2,3,7, !18-tetrachlorodibenzo-p-dioxin-inducible rabbit mRNAs for !1cytochrome P-450 isozymes 4 and 6. !$#cross-references MUID:85270514; PMID:2991917 !$#accession B25143 !'##molecule_type mRNA !'##residues 'H',94-207,'H',209-287,'I',289-290,'N',292,'MD',295, !1'MDDGAHV',303-308,'T',310-357,'L',359-461,'I',463-516 !1##label OKI !'##cross-references EMBL:M11728; NID:g165578; PIDN:AAA31433.1; !1PID:g165579 REFERENCE A00187 !$#authors Ozols, J. !$#journal J. Biol. Chem. (1986) 261:3965-3979 !$#title Complete amino acid sequence of a cytochrome P-450 isolated !1from beta-naphthoflavone-induced rabbit liver microsomes. !1Comparison with phenobarbital-induced and constitutive !1isozymes and identification of invariant residues. !$#cross-references MUID:86140205; PMID:3949797 !$#accession A00187 !'##molecule_type protein !'##residues 2-21,'S',23-69,'Q',71-91,'N',93-171,'F',173-193,'S', !1195-207,'FPQGM',213-246,'QPN',250,'R',252-289,'SH', !1292-294;296-298,'G',300-493,'T',495-516 ##label OZO !'##note 233-Ser and 247-Asn were also found REFERENCE A00188 !$#authors Fujita, V.S.; Black, S.D.; Tarr, G.E.; Koop, D.R.; Coon, !1M.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:4260-4264 !$#title On the amino acid sequence of cytochrome P-450 isozyme 4 !1from rabbit liver microsomes. !$#cross-references MUID:84272618; PMID:6589592 !$#accession A00188 !'##molecule_type protein !'##residues 2-45,'S',47,'V',49;107-118;133-173,'S',175-197,'X', !1199-206;217-232,'S',234-241,'V', !1243-246;255-264;267-274;297-298,'G',300-341;362-376,'XX', !1379-381;394-444,'A',446-477,'X',479-486;500-511,'S',513;'K' !1##label FUJ REFERENCE A44250 !$#authors Yun, C.H.; Hammons, G.J.; Jones, G.; Martin, M.V.; Hopkins, !1N.E.; Alworth, W.L.; Guengerich, F.P. !$#journal Biochemistry (1992) 31:10556-10563 !$#title Modification of cytochrome P450 1A2 enzymes by the !1mechanism-based inactivator 2-ethynylnaphthalene and the !1photoaffinity label 4-azidobiphenyl. !$#cross-references MUID:93041749; PMID:1420171 !$#accession A44250 !'##molecule_type protein !'##residues 176-185 ##label YUN !'##note only this tryptic peptide was photoaffinify labeled by !14-azidobenphenyl, a substrate analog COMMENT There are three forms of this protein that differ only in !1the absence or presence of the first one or two residues. GENETICS !$#gene CYP1A2 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; endoplasmic reticulum; !1heme; iron; metalloprotein; monooxygenase; oxidoreductase; !1transmembrane protein FEATURE !$314-480 #domain cytochrome P450 homology #label P45\ !$458 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 516 #molecular-weight 58334 #checksum 3338 SEQUENCE /// ENTRY O4HU4 #type complete TITLE cytochrome P450 1A2 - human ALTERNATE_NAMES cytochrome P450 HLd; cytochrome P450-4; cytochrome P450-P3 CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Homo sapiens #common_name man DATE 28-Dec-1987 #sequence_revision 31-Mar-1992 #text_change 03-Mar-2000 ACCESSIONS S16718; A25892; A23585; S07373; S22433; A60881 REFERENCE S16718 !$#authors Ikeya, K.; Jaiswal, A.K.; Owens, R.A.; Jones, J.E.; Nebert, !1D.W.; Kimura, S. !$#journal Mol. Endocrinol. (1989) 3:1399-1408 !$#title Human CYP1A2: sequence, gene structure, comparison with the !1mouse and rat orthologous gene, and differences in liver 1A2 !1mRNA expression. !$#cross-references MUID:90114205; PMID:2575218 !$#accession S16718 !'##molecule_type DNA !'##residues 1-515 ##label IKE !'##cross-references EMBL:M31664; NID:g181377; EMBL:M31665; NID:g181378; !1EMBL:M31666; NID:g181379; EMBL:M31667; NID:g181380; !1PIDN:AAA52163.1; PID:g181382 REFERENCE A25892 !$#authors Quattrochi, L.C.; Pendurthi, U.R.; Okino, S.T.; Potenza, C.; !1Tukey, R.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:6731-6735 !$#title Human cytochrome P-450 4 mRNA and gene: part of a multigene !1family that contains Alu sequences in its mRNA. !$#cross-references MUID:86313652; PMID:3462722 !$#accession A25892 !'##molecule_type DNA !'##residues 1-78,'S',80-510,'LP',512-515 ##label QUA !'##cross-references EMBL:L00388; GB:L00389; EMBL:M14337; NID:g181315; !1PIDN:AAA35738.1; PID:g181317 REFERENCE A90953 !$#authors Quattrochi, L.C.; Okino, S.T.; Pendurthi, U.R.; Tukey, R.H. !$#journal DNA (1985) 4:395-400 !$#title Cloning and isolation of human cytochrome P-450 cDNAs !1homologous to dioxin-inducible rabbit mRNAs encoding P-450 4 !1and P-450 6. !$#cross-references MUID:86081170; PMID:3000715 !$#accession A23585 !'##molecule_type mRNA !'##residues 295-310,'L',312-449,'M',450,'V',452-485 ##label QU2 !'##cross-references GB:M12078; NID:g181351; PIDN:AAA52154.1; !1PID:g553246 REFERENCE S07373 !$#authors Jaiswal, A.K.; Nebert, D.W.; Gonzalez, F.J. !$#journal Nucleic Acids Res. (1986) 14:6773-6774 !$#title Human P(3)450: cDNA and complete amino acid sequence. !$#cross-references MUID:86312938; PMID:3755823 !$#accession S07373 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-515 ##label JA1 !'##cross-references EMBL:Z00036; NID:g30338; PIDN:CAA77335.1; !1PID:g30339 REFERENCE S22433 !$#authors Jaiswal, A.K.; Nebert, D.W.; McBride, O.W.; Gonzalez, F.J. !$#journal J. Exp. Pathol. (1987) 3:1-17 !$#title Human P(3)450: cDNA and complete protein sequence, !1repetitive Alu sequences in the 3' nontranslated region, and !1localization of gene to chromosome 15. !$#cross-references MUID:88061719; PMID:3681487 !$#accession S22433 !'##status preliminary !'##molecule_type mRNA !'##residues 1-515 ##label JA2 !'##cross-references EMBL:M55053; NID:g181307; PIDN:AAA52146.1; !1PID:g181308 REFERENCE A60881 !$#authors Wrighton, S.A.; Campanile, C.; Thomas, P.E.; Maines, S.L.; !1Watkins, P.B.; Parker, G.; Mendez-Picon, G.; Haniu, M.; !1Shively, J.E.; Levin, W.; Guzelian, P.S. !$#journal Mol. Pharmacol. (1986) 29:405-410 !$#title Identification of a human liver cytochrome P-450 homologous !1to the major isosafrole-inducible cytochrome P-450 in the !1rat. !$#cross-references MUID:86203234; PMID:3517618 !$#accession A60881 !'##molecule_type protein !'##residues 2-19 ##label WRI GENETICS !$#gene GDB:CYP1A2 !'##cross-references GDB:118780; OMIM:124060 !$#map_position 15q22-15qter !$#introns 277/3; 318/1; 348/1; 389/2; 418/2 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; endoplasmic reticulum; !1heme; iron; metalloprotein; microsome; monooxygenase; !1oxidoreductase; transmembrane protein FEATURE !$314-480 #domain cytochrome P450 homology #label P45\ !$458 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 515 #molecular-weight 58294 #checksum 960 SEQUENCE /// ENTRY A54116 #type complete TITLE cytochrome P450 1B1 - human CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS A54116 REFERENCE A54116 !$#authors Sutter, T.R.; Tang, Y.M.; Hayes, C.L.; Wo, Y.Y.P.; Jabs, !1E.W.; Li, X.; Yin, H.; Cody, C.W.; Greenlee, W.F. !$#journal J. Biol. Chem. (1994) 269:13092-13099 !$#title Complete cDNA sequence of a human dioxin-inducible mRNA !1identifies a new gene subfamily of cytochrome P450 that maps !1to chromosome 2. !$#cross-references MUID:94230403; PMID:8175734 !$#accession A54116 !'##status preliminary !'##molecule_type mRNA !'##residues 1-543 ##label SUT !'##cross-references GB:U03688; NID:g501030; PIDN:AAA19567.1; !1PID:g501031 GENETICS !$#gene GDB:CYP1B1 !'##cross-references GDB:353515; OMIM:601771 !$#map_position 2pter-2qter CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxidoreductase FEATURE !$327-492 #domain cytochrome P450 homology #label CYP\ !$470 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 543 #molecular-weight 60831 #checksum 2492 SEQUENCE /// ENTRY O4CHC7 #type complete TITLE steroid 17alpha-monooxygenase (EC 1.14.99.9) cytochrome P450 17 - chicken ALTERNATE_NAMES cytochrome P450(c17); steroid 17alpha-hydroxylase ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 03-Mar-2000 ACCESSIONS JT0318 REFERENCE JT0318 !$#authors Ono, H.; Iwasaki, M.; Sakamoto, N.; Mizuno, S. !$#journal Gene (1988) 66:77-85 !$#title cDNA cloning and sequence analysis of a chicken gene !1expressed during the gonadal development and homologous to !1mammalian cytochrome P-450c17. !$#cross-references MUID:88329730; PMID:3047010 !$#accession JT0318 !'##molecule_type mRNA !'##residues 1-508 ##label ONO !'##cross-references GB:M21406; NID:g212492; PIDN:AAA48997.1; !1PID:g212493 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; heme; iron; metalloprotein; monooxygenase; !1ovary; oxidoreductase; steroid biosynthesis; testis FEATURE !$302-467 #domain cytochrome P450 homology #label CYP\ !$445 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 508 #molecular-weight 56984 #checksum 1464 SEQUENCE /// ENTRY S21125 #type complete TITLE steroid 17alpha-monooxygenase (EC 1.14.99.9) cytochrome P450 17 - rainbow trout ALTERNATE_NAMES cytochrome P450 c17; steroid 17,20-lyase ORGANISM #formal_name Oncorhynchus mykiss #common_name rainbow trout DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS S21125 REFERENCE S21125 !$#authors Sakai, N.; Tanaka, M.; Adachi, S.; Miller, W.L.; Nagahama, !1Y. !$#journal FEBS Lett. (1992) 301:60-64 !$#title Rainbow trout cytochrome P-450(c17) (17alpha-hydroxylase/17, !120-lyase). cDNA cloning, enzymatic properties and temporal !1pattern of ovarian P-450(c17) mRNA expression during !1oogenesis. !$#cross-references MUID:93083625; PMID:1451787 !$#accession S21125 !'##status preliminary !'##molecule_type mRNA !'##residues 1-514 ##label SAK !'##cross-references EMBL:Z14246; EMBL:X65800; NID:g64316; !1PIDN:CAA46675.1; PID:g64317 GENETICS !$#gene CYP17 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; heme; iron; membrane protein; metalloprotein; !1microsome; monooxygenase; oxidoreductase FEATURE !$306-471 #domain cytochrome P450 homology #label P45\ !$449 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 514 #molecular-weight 57408 #checksum 6846 SEQUENCE /// ENTRY I51281 #type complete TITLE steroid 17alpha-monooxygenase (EC 1.14.99.9) cytochrome P450 c17 - spiny dogfish ORGANISM #formal_name Squalus acanthias #common_name spiny dogfish DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS I51281 REFERENCE I51281 !$#authors Trant, J.M. !$#journal J. Exp. Zool. (1995) 272:25-33 !$#title Isolation and characterization of the cDNA encoding the !1spiny dogfish shark (Squalus acanthias) form of cytochrome !1P450c17. !$#cross-references MUID:95256824; PMID:7738515 !$#accession I51281 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-509 ##label TRA !'##cross-references GB:S77384; NID:g999087; PIDN:AAB34256.1; !1PID:g999088 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; heme; iron; membrane protein; metalloprotein; !1microsome; monooxygenase; oxidoreductase FEATURE !$302-467 #domain cytochrome P450 homology #label P45\ !$445 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 509 #molecular-weight 57208 #checksum 1124 SEQUENCE /// ENTRY A26366 #type complete TITLE steroid 17alpha-monooxygenase (EC 1.14.99.9) cytochrome P450 17 - human ALTERNATE_NAMES cytochrome P450(17alpha); steroid 17alpha-hydroxylase ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS A40921; A40908; A26366; A29587; S16717; S16903 REFERENCE A40921 !$#authors Kagimoto, M.; Winter, J.S.D.; Kagimoto, K.; Simpson, E.R.; !1Waterman, M.R. !$#journal Mol. Endocrinol. (1988) 2:564-570 !$#title Structural characterization of normal and mutant human !1steroid 17alpha-hydroxylase genes: molecular basis of one !1example of combined 17alpha-hydroxylase/17,20 lyase !1deficiency. !$#cross-references MUID:88334559; PMID:2843762 !$#accession A40921 !'##molecule_type DNA !'##residues 1-508 ##label KAG !'##cross-references GB:M31146; GB:M31153; NID:g181284 !'##note the authors translated the codon TCT for residue 154 as Cys REFERENCE A40908 !$#authors Bradshaw, K.D.; Waterman, M.R.; Couch, R.T.; Simpson, E.R.; !1Zuber, M.X. !$#journal Mol. Endocrinol. (1987) 1:348-354 !$#title Characterization of complementary deoxyribonucleic acid for !1human adrenocortical 17alpha-hydroxylase: a probe for !1analysis of 17alpha-hydroxylase deficiency. !$#cross-references MUID:90331926; PMID:3274893 !$#accession A40908 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-508 ##label BRA REFERENCE A94159 !$#authors Chung, B.C.; Picado-Leonard, J.; Haniu, M.; Bienkowski, M.; !1Hall, P.F.; Shively, J.E.; Miller, W.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:407-411 !$#title Cytochrome P450c17 (steroid 17 alpha-hydroxylase/17,20 !1lyase): cloning of human adrenal and testis cDNAs indicates !1the same gene is expressed in both tissues. !$#cross-references MUID:87092418; PMID:3025870 !$#accession A26366 !'##molecule_type mRNA !'##residues 1-508 ##label CHU !'##cross-references GB:M14564; NID:g181341; PIDN:AAA52151.1; !1PID:g181342 !'##experimental_source adrenal gland REFERENCE A29587 !$#authors Picado-Leonard, J.; Miller, W.L. !$#journal DNA (1987) 6:439-448 !$#title Cloning and sequence of the human gene for P450c17 (steroid !117-alpha-hydroxylase/17,20 lyase): similarity with the gene !1for P450c21. !$#cross-references MUID:88054468; PMID:3500022 !$#accession A29587 !'##molecule_type DNA !'##residues 1-21,'W',23-508 ##label PIC !'##cross-references GB:M19489; NID:g189442; PIDN:AAA36405.1; !1PID:g386992; GB:M63871; NID:g189444; PIDN:AAA59984.1; !1PID:g189445 !'##note the authors translated the codon TGG for residue 22 as Cys GENETICS !$#gene GDB:CYP17 !'##cross-references GDB:119829; OMIM:202110 !$#map_position 10q24.3-10q24.3 !$#introns 99/3; 146/1; 222/3; 251/3; 323/3; 380/2; 415/1 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; endoplasmic reticulum; !1heme; iron; metalloprotein; monooxygenase; oxidoreductase; !1transmembrane protein FEATURE !$299-464 #domain cytochrome P450 homology #label CYP\ !$442 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 508 #molecular-weight 57370 #checksum 9548 SEQUENCE /// ENTRY S22339 #type complete TITLE steroid 17alpha-monooxygenase (EC 1.14.99.9) cytochrome P450 17 - pig ALTERNATE_NAMES cytochrome P450(C17); steroid 17alpha-hydroxylase ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS S22339; S24233; B26366; S30074 REFERENCE S22339 !$#authors Conley, A.J.; Graham-Lorence, S.E.; Kagimoto, M.; Lorence, !1M.C.; Murry, B.A.; Oka, K.; Sanders, D.; Mason, J.I. !$#journal Biochim. Biophys. Acta (1992) 1130:75-77 !$#title Nucleotide sequence of a cDNA encoding porcine testis !117alpha-hydroxylase cytochrome P-450. !$#cross-references MUID:92182016; PMID:1543750 !$#accession S22339 !'##status preliminary !'##molecule_type mRNA !'##residues 1-509 ##label CON !'##cross-references EMBL:M63507; NID:g164396; PIDN:AAA31008.1; !1PID:g164397 REFERENCE S24233 !$#authors Zhang, P.; Nason, T.F.; Han, X.G.; Hall, P.F. !$#journal Biochim. Biophys. Acta (1992) 1131:345-348 !$#title Gene for 17-alpha-hydroxylase/C(17-20) lyase P-450: complete !1nucleotide sequence of the porcine gene and 5' upstream !1sequence of the rat gene. !$#cross-references MUID:92329554; PMID:1627653 !$#accession S24233 !'##molecule_type DNA !'##residues 1-50,'I',52-107,117-291,'S',293-318,'ATLC',322-329,'E', !1331-332,'E',334-406,'H',408-509 ##label ZHA !'##cross-references EMBL:Z11854; GB:S40340; NID:g1855; PIDN:CAA77878.1; !1PID:g833797 !'##note the authors translated the codon TCC for residue 94 as Glu REFERENCE A94159 !$#authors Chung, B.C.; Picado-Leonard, J.; Haniu, M.; Bienkowski, M.; !1Hall, P.F.; Shively, J.E.; Miller, W.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:407-411 !$#title Cytochrome P450c17 (steroid 17 alpha-hydroxylase/17,20 !1lyase): cloning of human adrenal and testis cDNAs indicates !1the same gene is expressed in both tissues. !$#cross-references MUID:87092418; PMID:3025870 !$#accession B26366 !'##molecule_type protein !'##residues 1-45,'F','L',54-69,'D',71-97,'K',99-116,'E',118-125,'S', !1127,'F',141-160,'VIQNA',183,'EMDRL',189,'EI',192-195,'D', !1197-200,'IEE',204,'E',206,'T',211-237,'E',239-256,265,'L', !1267-270,286-290,302,'C',304-307,'V',309-310,'FI',313-314, !1329,'E',331-332,'E',334-388,'A',390-394,'S',396,'F',398-406, !1'H',408-509 ##label CHU !'##experimental_source adrenal gland, testis GENETICS !$#gene CYP17 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; endoplasmic reticulum; !1heme; iron; metalloprotein; monooxygenase; oxidoreductase; !1transmembrane protein FEATURE !$299-464 #domain cytochrome P450 homology #label P45\ !$442 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 509 #molecular-weight 57422 #checksum 3351 SEQUENCE /// ENTRY S04346 #type complete TITLE steroid 17alpha-monooxygenase (EC 1.14.99.9) cytochrome P450 17 precursor - bovine ALTERNATE_NAMES cytochrome P450(C17) ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS S04346; A26289 REFERENCE S04346 !$#authors Bhasker, C.R.; Adler, B.S.; Dee, A.; John, M.E.; Kagimoto, !1M.; Zuber, M.X.; Ahlgren, R.; Wang, X.; Simpson, E.R.; !1Waterman, M.R. !$#journal Arch. Biochem. Biophys. (1989) 271:479-487 !$#title Structural characterization of the bovine CYP17 !1(17-alpha--hydroxylase) gene. !$#cross-references MUID:89271931; PMID:2543297 !$#accession S04346 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-509 ##label BHA REFERENCE A26289 !$#authors Zuber, M.X.; John, M.E.; Okamura, T.; Simpson, E.R.; !1Waterman, M.R. !$#journal J. Biol. Chem. (1986) 261:2475-2482 !$#title Bovine adrenocortical cytochrome P-450-17-alpha. Regulation !1of gene expression by ACTH and elucidation of primary !1sequence. !$#cross-references MUID:86111956; PMID:3003117 !$#accession A26289 !'##molecule_type mRNA !'##residues 1-422,'T',424-457,'R',459-508,'P' ##label ZUB !'##cross-references GB:M12547; NID:g162942; PIDN:AAA30485.1; !1PID:g162943 GENETICS !$#gene CYP17 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; endoplasmic reticulum; !1heme; iron; metalloprotein; monooxygenase; oxidoreductase; !1transmembrane protein FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-509 #product steroid 17alpha-monooxygenase cytochrome !8P450 17 #status predicted #label MAT\ !$299-464 #domain cytochrome P450 homology #label P45\ !$442 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 509 #molecular-weight 57233 #checksum 8646 SEQUENCE /// ENTRY A30828 #type complete TITLE steroid 17alpha-monooxygenase (EC 1.14.99.9) cytochrome P450 17 - rat ALTERNATE_NAMES cytochrome P450 17-alpha; cytochrome P450 IF-5, hepatic; steroid 17,20-lyase; steroid 17alpha-hydroxylase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS A31359; S16719; S24316; A33980; A27659; D41425; I60207; !1A30828; S20655 REFERENCE A90154 !$#authors Namiki, M.; Kitamura, M.; Buczko, E.; Dufau, M.L. !$#journal Biochem. Biophys. Res. Commun. (1988) 157:705-712 !$#title Rat testis P-450-17-alpha cDNA: the deduced amino acid !1sequence, expression and secondary structural configuration. !$#cross-references MUID:89076306; PMID:3264499 !$#accession A31359 !'##molecule_type mRNA !'##residues 1-507 ##label NAM !'##cross-references GB:M22204; NID:g205921; PIDN:AAA41783.1; !1PID:g205922; GB:X14086; NID:g56051; PIDN:CAA32248.1; !1PID:g56052 REFERENCE S16719 !$#authors Fevold, H.R.; Lorence, M.C.; McCarthy, J.L.; Trant, J.M.; !1Kagimoto, M.; Waterman, M.R.; Mason, J.I. !$#journal Mol. Endocrinol. (1989) 3:968-975 !$#title Rat P450(17-alpha) from testis: characterization of a !1full-length cDNA encoding a unique steroid hydroxylase !1capable of catalyzing both Delta(4)- and Delta !1(5)-steroid-17,20-lyase reactions. !$#cross-references MUID:89295447; PMID:2786990 !$#accession S16719 !'##status preliminary !'##molecule_type mRNA !'##residues 1-507 ##label FEV !'##cross-references EMBL:M31681; NID:g205909; PIDN:AAA41777.1; !1PID:g205910 REFERENCE S24233 !$#authors Zhang, P.; Nason, T.F.; Han, X.G.; Hall, P.F. !$#journal Biochim. Biophys. Acta (1992) 1131:345-348 !$#title Gene for 17-alpha-hydroxylase/C(17-20) lyase P-450: complete !1nucleotide sequence of the porcine gene and 5' upstream !1sequence of the rat gene. !$#cross-references MUID:92329554; PMID:1627653 !$#accession S24316 !'##molecule_type DNA !'##residues 1-97 ##label NAS !'##cross-references EMBL:Z11902; NID:g56031; PIDN:CAA77954.1; !1PID:g56032 REFERENCE A33980 !$#authors Mellon, S.H.; Vaisse, C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:7775-7779 !$#title cAMP regulates P450scc gene expression by a !1cycloheximide-insensitive mechanism in cultured mouse Leydig !1MA-10 cells. !$#cross-references MUID:90046678; PMID:2554289 !$#accession A33980 !'##molecule_type mRNA !'##residues 273-507 ##label MEL !'##cross-references GB:M27282; NID:g205913; PIDN:AAA41779.1; !1PID:g205914 REFERENCE A27659 !$#authors Nishihara, M.; Winters, C.A.; Buzko, E.; Waterman, M.R.; !1Dufau, M.L. !$#journal Biochem. Biophys. Res. Commun. (1988) 154:151-158 !$#title Hormonal regulation of rat Leydig cell cytochrome !1P-450-17-alpha mRNA levels and characterization of a partial !1length rat P-450-17-alpha cDNA. !$#cross-references MUID:88280759; PMID:3260774 !$#accession A27659 !'##molecule_type mRNA !'##residues 271-507 ##label NIS !'##cross-references GB:M21208; NID:g203825 !'##note the authors translated the codon GAT for residues 288, 401, and !1478 as Glu, Asn, and Asn respectively REFERENCE A41425 !$#authors Imaoka, S.; Kamataki, T.; Funae, Y. !$#journal J. Biochem. (1987) 102:843-851 !$#title Purification and characterization of six cytochromes P-450 !1from hepatic microsomes of immature female rats. !$#cross-references MUID:88139237; PMID:3436956 !$#accession D41425 !'##molecule_type protein !'##residues 'XXXE',5-16 ##label IMA REFERENCE I60207 !$#authors Givens, C.R.; Zhang, P.; Bair, S.R.; Mellon, S.H. !$#journal DNA Cell Biol. (1994) 13:1087-1098 !$#title Transcriptional regulation of rat cytochrome P450c17 !1expression in mouse Leydig MA-10 and adrenal Y-1 cells: !1identification of a single protein that mediates both basal !1and cAMP-induced activities. !$#cross-references MUID:95217329; PMID:7702752 !$#accession I60207 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-507 ##label RES !'##cross-references EMBL:X69816; NID:g619900; PIDN:CAA49470.1; !1PID:g940818 GENETICS !$#gene CYP17 !$#introns 99/3; 145/1; 221/3; 250/3; 322/3; 379/2; 414/1 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; endoplasmic reticulum; !1heme; iron; liver; metalloprotein; microsome; monooxygenase; !1oxidoreductase; transmembrane protein FEATURE !$2-21 #domain transmembrane #status predicted #label TM1\ !$169-186 #domain transmembrane #status predicted #label TM2\ !$298-463 #domain cytochrome P450 homology #label P45\ !$441 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 507 #molecular-weight 57250 #checksum 9025 SEQUENCE /// ENTRY A39072 #type complete TITLE steroid 17alpha-monooxygenase (EC 1.14.99.9) cytochrome P450 17 - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS A39072 REFERENCE A39072 !$#authors Youngblood, G.L.; Sartorius, C.; Taylor, B.A.; Payne, A.H. !$#journal Genomics (1991) 10:270-275 !$#title Isolation, characterization, and chromosomal mapping of !1mouse P450 17alpha-hydroxylase/C-17-20 lyase. !$#cross-references MUID:91257840; PMID:1840559 !$#accession A39072 !'##status preliminary !'##molecule_type mRNA !'##residues 1-507 ##label YOU !'##cross-references GB:M64863; NID:g200192; PIDN:AAA39877.1; !1PID:g200193 !'##note the authors translated the codon AAG for residue 126 as Arg GENETICS !$#gene Cyp17 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; monooxygenase; oxidoreductase; transmembrane !1protein FEATURE !$298-463 #domain cytochrome P450 homology #label P45\ !$441 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 507 #molecular-weight 57637 #checksum 6545 SEQUENCE /// ENTRY O4HUC2 #type complete TITLE steroid 21-monooxygenase (EC 1.14.99.10) cytochrome P450 21 - human ALTERNATE_NAMES cytochrome P450(C21B); steroid 21-hydroxylase cytochrome P450 21A2 ORGANISM #formal_name Homo sapiens #common_name man DATE 04-Dec-1986 #sequence_revision 08-Feb-1996 #text_change 03-Mar-2000 ACCESSIONS A25446; A00191; A27865; A32715; A21889; S26484; S29670; !1S29671; S26584; S29673; I55547; I59109; I58113; A29406 REFERENCE A94108 !$#authors White, P.C.; New, M.I.; Dupont, B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:5111-5115 !$#title Structure of human steroid 21-hydroxylase genes. !$#cross-references MUID:86259742; PMID:3487786 !$#accession A25446 !'##molecule_type DNA !'##residues 1-494 ##label WHI !'##cross-references GB:M13936; NID:g187899; PIDN:AAA59695.1; !1PID:g386910 REFERENCE A00191 !$#authors Higashi, Y.; Yoshioka, H.; Yamane, M.; Gotoh, O.; !1Fujii-Kuriyama, Y. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:2841-2845 !$#title Complete nucleotide sequence of two steroid 21-hydroxylase !1genes tandemly arranged in human chromosome: a pseudogene !1and a genuine gene. !$#cross-references MUID:86206051; PMID:3486422 !$#accession A00191 !'##molecule_type mRNA !'##residues 1-425,'P',427-494 ##label HIG REFERENCE A27865 !$#authors Rodrigues, N.R.; Dunham, I.; Yu, C.Y.; Carroll, M.C.; !1Porter, R.R.; Campbell, R.D. !$#journal EMBO J. (1987) 6:1653-1661 !$#title Molecular characterization of the HLA-linked steroid !121-hydroxylase B gene from an individual with congenital !1adrenal hyperplasia. !$#cross-references MUID:87275858; PMID:3038528 !$#accession A27865 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-9,'L',10-101,'R',103-372,'S',373-494 ##label ROD REFERENCE A32715 !$#authors Matteson, K.J.; Phillips III, J.A.; Miller, W.L.; Chung, B.; !1Orlando, P.J.; Frisch, H.; Ferrandez, A.; Burr, I.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:5858-5862 !$#title P450XXI (steroid 21-hydroxylase) gene deletions are not !1found in family studies of congenital adrenal hyperplasia. !$#cross-references MUID:87289701; PMID:3497399 !$#accession A32715 !'##molecule_type mRNA !'##residues 265-310,'L',312-345,'I',347-494 ##label MAT !'##cross-references GB:M17252; NID:g189446; PIDN:AAA59985.1; !1PID:g386993 !'##note the authors translated the codon ATT for residue 346 as Asn REFERENCE A21889 !$#authors Carroll, M.C.; Campbell, R.D.; Porter, R.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:521-525 !$#title Mapping of steroid 21-hydroxylase genes adjacent to !1complement component C4 genes in HLA, the major !1histocompatibility complex in man. !$#cross-references MUID:85113228; PMID:3871526 !$#accession A21889 !'##molecule_type DNA !'##residues 149-171,'N',173-182 ##label CAR !'##cross-references GB:K02771; NID:g187928; PIDN:AAA59706.1; !1PID:g443672 REFERENCE S26484 !$#authors Helmberg, A.; Kofler, R. !$#submission submitted to the EMBL Data Library, March 1991 !$#accession S26484 !'##molecule_type DNA !'##residues 1-101,'R',103-371 ##label HEL !'##cross-references EMBL:X58904; NID:g30319; PIDN:CAA41707.1; !1PID:g30320 !$#accession S29670 !'##molecule_type DNA !'##residues 1-9,'L',10-101,'R',103-338,'H',340-452,'S',454-492,'S',494 !1##label HE3 !'##cross-references EMBL:X58906; NID:g30321; PIDN:CAA41709.1; !1PID:g30322 !$#accession S29671 !'##molecule_type DNA !'##residues 1-9,'L',10-101,'R',103-371 ##label HE4 !'##cross-references EMBL:X58902; NID:g30325; PIDN:CAA41706.1; !1PID:g30326 REFERENCE S26584 !$#authors Helmberg, A.; Tabarelli, M.; Dobler, G.; Kofler, R. !$#submission submitted to the EMBL Data Library, March 1991 !$#description Identification of molecular defects causing congenital !1adrenal Hyperplasia by cloning of PCR-amplified !121-hydroxylase genes. !$#accession S26584 !'##molecule_type DNA !'##residues 1-171,'N',173-371 ##label HE2 !'##cross-references EMBL:X58898; NID:g30316; PIDN:CAA41702.1; !1PID:g30317 !$#accession S29673 !'##molecule_type DNA !'##residues 1-9,'L',10-101,'R',103-371 ##label HE5 !'##cross-references EMBL:X58900; NID:g30328; PIDN:CAA41704.1; !1PID:g30329 REFERENCE I55547 !$#authors Globerman, H.; Amor, M.; Parker, K.L.; New, M.I.; White, !1P.C. !$#journal J. Clin. Invest. (1988) 82:139-144 !$#title Nonsense mutation causing steroid 21-hydroxylase deficiency. !$#cross-references MUID:88273565; PMID:3267225 !$#accession I55547 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-9,'L',10-280,'L',282-494 ##label RES !'##cross-references GB:M21550; NID:g180960; PIDN:AAA52063.1; !1PID:g180962 REFERENCE I59109 !$#authors Amor, M.; Parker, K.L.; Globerman, H.; New, M.I.; White, !1P.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:1600-1604 !$#title Mutation in the CYP21B gene (Ile-172----Asn) causes steroid !121-hydroxylase deficiency. !$#cross-references MUID:88144483; PMID:3257825 !$#accession I59109 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 149-182 ##label RE2 !'##cross-references GB:M19711; NID:g181289; PIDN:AAA83248.1; !1PID:g181290 REFERENCE I58113 !$#authors Collier, S.; Tassabehji, M.; Strachan, T. !$#journal Nature Genet. (1993) 3:260-265 !$#title A de novo pathological point mutation at the 21-hydroxylase !1locus: implications for gene conversion in the human genome. !$#cross-references MUID:93251047; PMID:8485582 !$#accession I58113 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 109-171,'N',173-185 ##label RE3 !'##cross-references GB:S60612; NID:g300314 COMMENT Deficiency of this enzyme (21-hydroxylase deficiency) causes !1about 90 % of cases of congenital adrenal hyperplasia, an !1inborn error of cortisol biosynthesis. GENETICS !$#gene GDB:CYP21; CYP21B !'##cross-references GDB:120605; OMIM:201910 !$#map_position 6p21.3-6p21.3 !$#introns 67/1; 97/1; 148/3; 182/3; 216/3; 245/3; 312/3; 372/2; 407/1 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; monooxygenase; oxidoreductase; transmembrane !1protein FEATURE !$288-450 #domain cytochrome P450 homology #label CYP\ !$428 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 494 #molecular-weight 55887 #checksum 8049 SEQUENCE /// ENTRY O4BOC2 #type complete TITLE steroid 21-monooxygenase (EC 1.14.99.10) cytochrome P450 21A1 - bovine ALTERNATE_NAMES cytochrome P450 (C21); steroid 21-hydroxylase ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 28-May-1986 #sequence_revision 05-Apr-1995 #text_change 03-Mar-2000 ACCESSIONS A27555; A00192; A24101; C28860; A21181 REFERENCE A27555 !$#authors Chung, B.; Matteson, K.J.; Miller, W.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:4243-4247 !$#title Structure of a bovine gene for P-450c21 (steroid !121-hydroxylase) defines a novel cytochrome P-450 gene !1family. !$#cross-references MUID:86233409; PMID:3487086 !$#accession A27555 !'##molecule_type DNA !'##residues 1-496 ##label CHU !'##cross-references GB:M11267; NID:g163468; PIDN:AAA83247.1; !1PID:g163469 REFERENCE A00192 !$#authors Yoshioka, H.; Morohashi, K.; Sogawa, K.; Yamane, M.; !1Kominami, S.; Takemori, S.; Okada, Y.; Omura, T.; !1Fujii-Kuriyama, Y. !$#journal J. Biol. Chem. (1986) 261:4106-4109 !$#title Structural analysis of cloned cDNA for mRNA of microsomal !1cytochrome P-450(C21) which catalyzes steroid !121-hydroxylation in bovine adrenal cortex. !$#cross-references MUID:86140226; PMID:3005319 !$#accession A00192 !'##molecule_type mRNA !'##residues 1-13,'S',15-400,'Y',402-496 ##label YOS !'##cross-references GB:M12918; NID:g162947; PIDN:AAA30487.1; !1PID:g162948 !'##experimental_source adrenal cortex microsomes REFERENCE A24101 !$#authors John, M.E.; Okamura, T.; Dee, A.; Adler, B.; John, M.C.; !1White, P.C.; Simpson, E.R.; Waterman, M.R. !$#journal Biochemistry (1986) 25:2846-2853 !$#title Bovine steroid 21-hydroxylase: regulation of biosynthesis. !$#cross-references MUID:86243279; PMID:2424492 !$#accession A24101 !'##molecule_type mRNA !'##residues 121-430,'C',432-496 ##label JOH !'##cross-references GB:K01333; NID:g162944; PIDN:AAA30486.1; !1PID:g162945 REFERENCE A91972 !$#authors Ogishima, T.; Okada, Y.; Kominami, S.; Takemori, S.; Omura, !1T. !$#journal J. Biochem. (1983) 94:1711-1714 !$#title Partial amino acid sequences of two mitochondrial and two !1microsomal cytochrome P-450's from adrenal cortex. !$#cross-references MUID:84087829; PMID:6654880 !$#accession C28860 !'##molecule_type protein !'##residues 1-12,'K',14-15,248-250,'S' ##label OGS !'##experimental_source adrenal cortex microsomes REFERENCE A21181 !$#authors White, P.C.; New, M.I.; Dupont, B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:1986-1990 !$#title Cloning and expression of cDNA encoding a bovine adrenal !1cytochrome P-450 specific for steroid 21-hydroxylation. !$#cross-references MUID:84193940; PMID:6609358 !$#contents annotation; sequence report !$#note this sequence differs substantially from that in reference !1A24101 GENETICS !$#introns 68/1; 98/1; 149/3; 181/3; 215/3; 244/3; 311/3; 371/2; 406/1 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; endoplasmic reticulum; !1heme; iron; metalloprotein; monooxygenase; oxidoreductase; !1transmembrane protein FEATURE !$287-449 #domain cytochrome P450 homology #label P45\ !$427 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 496 #molecular-weight 56077 #checksum 8337 SEQUENCE /// ENTRY A43349 #type complete TITLE steroid 21-monooxygenase (EC 1.14.99.10) cytochrome P450 21A1 - sheep ALTERNATE_NAMES cytochrome P450(C21) ORGANISM #formal_name Ovis orientalis aries, Ovis ammon aries #common_name domestic sheep DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS A43349; B43349 REFERENCE A43349 !$#authors Crawford, R.J.; Hammond, V.E.; Connell, J.M.; Coghlan, J.P. !$#journal J. Biol. Chem. (1992) 267:16212-16218 !$#title The structure and activity of two cytochrome P450c21 !1proteins encoded in the ovine adrenal cortex. !$#cross-references MUID:92355577; PMID:1644806 !$#accession A43349 !'##molecule_type mRNA !'##residues 1-497 ##label CRA1 !'##cross-references GB:M92836; NID:g165851 !'##experimental_source adrenal cortex !'##note sequence extracted from NCBI backbone (NCBIN:110514, !1NCBIP:110515) !$#accession B43349 !'##molecule_type mRNA !'##residues 1-478,'D' ##label CRA2 !'##cross-references GB:M92837; NID:g165852 !'##note sequence extracted from NCBI backbone (NCBIN:111338, !1NCBIP:111339) CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS alternative splicing; chromoprotein; electron transfer; !1heme; iron; metalloprotein; monooxygenase; oxidoreductase; !1transmembrane protein FEATURE !$288-450 #domain cytochrome P450 homology #label P45\ !$428 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 497 #molecular-weight 56176 #checksum 10 SEQUENCE /// ENTRY A32525 #type complete TITLE steroid 21-monooxygenase (EC 1.14.99.10) cytochrome P450 21A1 - pig ALTERNATE_NAMES cytochrome P450(C21); steroid 21-hydroxylase ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS S28169; A32525; A60677 REFERENCE S28169 !$#authors Burghelle-Mayeur, C.; Geffrotin, C.; Vaiman, M. !$#journal Biochim. Biophys. Acta (1992) 1171:153-161 !$#title Sequences of the swine 21-hydroxylase gene (CYP21) and a !1portion of the opposite-strand overlapping gene of unknown !1function previously described in human. !$#cross-references MUID:93129614; PMID:1482677 !$#accession S28169 !'##molecule_type DNA !'##residues 1-492 ##label BUR !'##cross-references EMBL:M83939; NID:g164559; PIDN:AAA31080.1; !1PID:g164560 REFERENCE A32525 !$#authors Haniu, M.; Yanagibashi, K.; Hall, P.F.; Shively, J.E. !$#journal Arch. Biochem. Biophys. (1987) 254:380-384 !$#title Complete amino acid sequence of 21-hydroxylase cytochrome !1P-450 from porcine adrenal microsomes. !$#cross-references MUID:87212013; PMID:3495238 !$#accession A32525 !'##molecule_type protein !'##residues 1-9,'T',11-12,'K',14-54,'K',56-140,'C',142-200,'D',202-390, !1'I',392-462,'V',464,'Y',466-492 ##label HAN !'##experimental_source adrenal glands REFERENCE A60677 !$#authors Geffrotin, C.; Chardon, P.; De Andres-Cara, D.F.; Feil, R.; !1Renard, C.; Vaiman, M. !$#journal Anim. Genet. (1990) 21:1-13 !$#title The swine steroid 21-hydroxylase gene (CYP21): cloning and !1mapping within the swine leucocyte antigen complex. !$#cross-references MUID:90233515; PMID:2109953 !$#accession A60677 !'##molecule_type DNA !'##residues 1-99 ##label GEF GENETICS !$#gene CYP21A1 !$#introns 68/1; 98/1; 149/3; 181/3; 215/3; 244/3; 311/3; 371/2; 406/1 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; microsome; monooxygenase; oxidoreductase; !1transmembrane protein FEATURE !$287-449 #domain cytochrome P450 homology #label P45\ !$427 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 492 #molecular-weight 55619 #checksum 4495 SEQUENCE /// ENTRY A26660 #type complete TITLE steroid 21-monooxygenase (EC 1.14.99.10) cytochrome P450 21A1 - mouse ALTERNATE_NAMES cytochrome P450(C21); steroid 21-hydroxylase ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS A26660; A00193 REFERENCE A26660 !$#authors Chaplin, D.D.; Galbraith, L.J.; Seidman, J.G.; White, P.C.; !1Parker, K.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:9601-9605 !$#title Nucleotide sequence analysis of murine 21-hydroxylase genes: !1mutations affecting gene expression. !$#cross-references MUID:87092295; PMID:3491986 !$#accession A26660 !'##molecule_type DNA !'##residues 1-487 ##label CHA !'##cross-references GB:M15009 !'##note the authors translated the codon CGC for residue 63 as His, TTC !1for residue 163 as Pro, AAG for residue 177 as Leu, GAC for !1residue 178 as Asn, CGG for residue 270 as Gln, and GCC for !1residue 314 as Glu REFERENCE A00193 !$#authors Amor, M.; Tosi, M.; Duponchel, C.; Steinmetz, M.; Meo, T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:4453-4457 !$#title Liver mRNA probes disclose two cytochrome P-450 genes !1duplicated in tandem with the complement C4 loci of the !1mouse H-2S region. !$#cross-references MUID:85242702; PMID:3874401 !$#accession A00193 !'##molecule_type DNA !'##residues 'RPLLGQTSLALHLLPT',399-487 ##label AMO !'##cross-references GB:K03234; NID:g199331 !'##note this translation includes a region likely to represent an !1intron GENETICS !$#gene Cyp21 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; monooxygenase; oxidoreductase; transmembrane !1protein FEATURE !$283-442 #domain cytochrome P450 homology #label P45\ !$420 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 487 #molecular-weight 55328 #checksum 6706 SEQUENCE /// ENTRY S36878 #type complete TITLE cytochrome P450 - alfalfa CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Medicago sativa #common_name alfalfa DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS S36878 REFERENCE S36878 !$#authors Fahrendorf, T.; Dixon, R.A. !$#journal Arch. Biochem. Biophys. (1993) 305:509-515 !$#title Stress responses in alfalfa (Medicago sativa L.). XVIII: !1Molecular cloning and expression of the elicitor-inducible !1cinnamic acid 4-hydroxylase cytochrome P450. !$#cross-references MUID:93384309; PMID:8373188 !$#accession S36878 !'##status preliminary !'##molecule_type mRNA !'##residues 1-506 ##label FAH !'##cross-references EMBL:L11046 GENETICS !$#gene CYP73A3 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxidoreductase FEATURE !$304-470 #domain cytochrome P450 homology #label CYP\ !$448 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 506 #molecular-weight 58279 #checksum 4212 SEQUENCE /// ENTRY A35867 #type complete TITLE cytochrome P450 71A1 - avocado CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Persea americana #common_name avocado DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS A35867; A44973 REFERENCE A35867 !$#authors Bozak, K.R.; Yu, H.; Sirevag, R.; Christoffersen, R.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:3904-3908 !$#title Sequence analysis of ripening-related cytochrome P-450 cDNAs !1from avocado fruit. !$#cross-references MUID:90251665; PMID:1692626 !$#accession A35867 !'##molecule_type mRNA !'##residues 1-471 ##label BOZ !'##cross-references GB:M32885 REFERENCE A44973 !$#authors O'Keefe, D.P.; Leto, K.J. !$#journal Plant Physiol. (1989) 89:1141-1149 !$#title Cytochrome P-450 from the mesocarp of avocado (Persea !1americana). !$#accession A44973 !'##molecule_type protein !'##residues 1-40 ##label OAK !'##note a second sequence was identical except for the lack of the lack !1of Met-1 GENETICS !$#gene CYP71A1 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; monooxygenase; oxidoreductase; transmembrane !1protein FEATURE !$301-465 #domain cytochrome P450 homology #label CYP\ !$443 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 471 #molecular-weight 53074 #checksum 5957 SEQUENCE /// ENTRY S36805 #type complete TITLE cytochrome P450 71A4 - eggplant CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Solanum melongena #common_name eggplant, aubergine DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS S36805 REFERENCE S36805 !$#authors Umemoto, N.; Kobayashi, O.; Ishizaki-Nishizawa, O.; Toguri, !1T. !$#journal FEBS Lett. (1993) 330:169-173 !$#title cDNAs sequences encoding cytochrome P450 (CYP71 family) from !1eggplant seedlings. !$#cross-references MUID:93374057; PMID:8365486 !$#accession S36805 !'##status preliminary !'##molecule_type mRNA !'##residues 1-507 ##label UME !'##cross-references EMBL:X70981; NID:g402223; PIDN:CAA50312.1; !1PID:g402224 GENETICS !$#gene CYP71A4 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxidoreductase FEATURE !$305-470 #domain cytochrome P450 homology #label CYP\ !$448 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 507 #molecular-weight 57637 #checksum 7654 SEQUENCE /// ENTRY S45039 #type complete TITLE cytochrome P450 - Mentha piperita (peppermint) CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Mentha piperita #common_name peppermint DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS S45039 REFERENCE S45039 !$#authors Kang, M.H.; Choi, Y.D. !$#submission submitted to the EMBL Data Library, May 1994 !$#description Molecular cloning of a genomic DNA for cytochrome P-450 !1oxidase from Mentha piperita. !$#accession S45039 !'##molecule_type DNA !'##residues 1-502 ##label KAN !'##cross-references EMBL:Z33875; NID:g493474; PIDN:CAA83941.1; !1PID:g493475 GENETICS !$#introns 303/3 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; monooxygenase; oxidoreductase FEATURE !$305-469 #domain cytochrome P450 homology #label CYP\ !$447 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 502 #molecular-weight 57213 #checksum 4697 SEQUENCE /// ENTRY S62899 #type complete TITLE cytochrome P450 (CYP93 A1) - soybean CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Glycine max #common_name soybean DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S62899 REFERENCE S62899 !$#authors Suzuki, G.; Ohta, H.; Kato, T.; Igarashi, T.; Sakai, F.; !1Shibata, D.; Takano, A.; Masuda, T.; Shioi, Y.; Takamiya, K. !$#journal FEBS Lett. (1996) 383:83-86 !$#title Induction of a novel cytochrome P450 (CYP93 family) by !1methyl jasmonate in soybean suspension-cultured cells. !$#cross-references MUID:96184393; PMID:8612798 !$#accession S62899 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-509 ##label SUZ !'##cross-references GB:D83968; NID:g1435059; PIDN:BAA12159.1; !1PID:g1232111 GENETICS !$#gene cyp93A1 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; monooxygenase; oxidoreductase FEATURE !$303-469 #domain cytochrome P450 homology #label CYP\ !$447 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 509 #molecular-weight 57870 #checksum 6134 SEQUENCE /// ENTRY A71418 #type complete TITLE cytochrome P450 d13725w - Arabidopsis thaliana CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress #variety columbia DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A71418 REFERENCE A71400 !$#authors Bevan, M.; Bancroft, I.; Bent, E.; Love, K.; Goodman, H.; !1Dean, C.; Bergkamp, R.; Dirkse, W.; Van Staveren, M.; !1Stiekema, W.; Drost, L.; Ridley, P.; Hudson, S.A.; Patel, !1K.; Murphy, G.; Piffanelli, P.; Wedler, H.; Wedler, E.; !1Wambutt, R.; Weitzenegger, T.; Pohl, T.M.; Terryn, N.; !1Gielen, J.; Villarroel, R.; De Clerck, R.; Van Montagu, M.; !1Lecharny, A.; Auborg, S.; Gy, I.; Kreis, M.; Lao, N.; !1Kavanagh, T.; Hempel, S.; Kotter, P.; Entian, K.D.; Rieger, !1M.; Schaeffer, M.; Funk, B.; Mueller-Auer, S.; Silvey, M.; !1James, R.; Montfort, A.; Pons, A.; Puigdomenech, P.; Douka, !1A.; Voukelatou, E.; Milioni, D.; Hatzopoulos, P.; Piravandi, !1E.; Obermaier, B.; Hilbert, H.; Duesterhoft, A.; Moores, T.; !1Jones, J.D.G.; Eneva, T.; Palme, K.; Benes, V.; Rechman, S.; !1Ansorge, W.; Cooke, R.; Berger, C.; Delseny, M.; Voet, M.; !1Volckaert, G.; Mewes, H.W.; Klosterman, S.; Schueller, C.; !1Chalwatzis, N. !$#journal Nature (1998) 391:485-488 !$#title Analysis of 1.9 Mb of contiguous sequence from chromosome 4 !1of Arabidopsis thaliana. !$#cross-references MUID:98121113; PMID:9461215 !$#accession A71418 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-527 ##label BEV !'##cross-references GB:Z97338; NID:g2244870; PIDN:CAB10315.1; !1PID:g2244893 GENETICS !$#gene d13725w !$#map_position 4COP9-4G3845 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxidoreductase FEATURE !$308-473 #domain cytochrome P450 homology #label CYP\ !$451 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 527 #molecular-weight 60298 #checksum 8927 SEQUENCE /// ENTRY S38534 #type complete TITLE cytochrome P450 76A2 - eggplant CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Solanum melongena #common_name eggplant, aubergine DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS S38534 REFERENCE S38534 !$#authors Toguri, T.; Kobayashi, O.; Umemoto, N. !$#journal Biochim. Biophys. Acta (1993) 1216:165-169 !$#title The cloning of eggplant seedling cDNAs encoding proteins !1from a novel cytochrome P-450 family (CYP76). !$#cross-references MUID:94032483; PMID:8218411 !$#accession S38534 !'##status preliminary !'##molecule_type mRNA !'##residues 1-505 ##label TOG !'##cross-references EMBL:X71657; NID:g415910; PIDN:CAA50648.1; !1PID:g415911 GENETICS !$#gene CYP76A2 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxidoreductase FEATURE !$306-470 #domain cytochrome P450 homology #label CYP\ !$448 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 505 #molecular-weight 57807 #checksum 6089 SEQUENCE /// ENTRY S43342 #type complete TITLE flavonoid 3',5'-hydroxylase (EC 1.14.-.-) cytochrome P450 - eggplant ORGANISM #formal_name Solanum melongena #common_name eggplant, aubergine DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS S43342 REFERENCE S43342 !$#authors Toguri, T.; Umemoto, N.; Kobayashi, O.; Ohtani, T. !$#journal Plant Mol. Biol. (1993) 23:933-946 !$#title Activation of anthocyanin synthesis genes by white light in !1eggplant hypocotyl tissues, and identification of an !1inducible P-450 cDNA. !$#cross-references MUID:94083564; PMID:8260632 !$#accession S43342 !'##status preliminary !'##molecule_type mRNA !'##residues 1-513 ##label TOG !'##cross-references EMBL:X70824; NID:g395260; PIDN:CAA50155.1; !1PID:g395261 GENETICS !$#gene CYP75A2 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxidoreductase FEATURE !$301-468 #domain cytochrome P450 homology #label CYP\ !$446 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 513 #molecular-weight 57783 #checksum 7964 SEQUENCE /// ENTRY S41598 #type complete TITLE cytochrome P450 77A2 - eggplant CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Solanum melongena #common_name eggplant, aubergine DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS S41598; S40266 REFERENCE S41598 !$#authors Toguri, T.; Tokugawa, K. !$#journal FEBS Lett. (1994) 338:290-294 !$#title Cloning of eggplant hypocotyl cDNAs encoding cytochromes !1P450 belonging to a novel family (CYP77). !$#cross-references MUID:94139942; PMID:8307197 !$#accession S41598 !'##molecule_type mRNA !'##residues 1-511 ##label TOG !'##cross-references EMBL:X71655; NID:g438240; PIDN:CAA50646.1; !1PID:g438241 !'##experimental_source clone cyp77A2 GENETICS !$#gene CYP77A2 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxidoreductase FEATURE !$312-478 #domain cytochrome P450 homology #label CYP\ !$456 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 511 #molecular-weight 58114 #checksum 6104 SEQUENCE /// ENTRY S68203 #type complete TITLE tyrosine N-monooxygenase (EC 1.14.13.41) cytochrome P450tyr - sorghum ALTERNATE_NAMES tyrosine N-hydroxylase ORGANISM #formal_name Sorghum bicolor #common_name sorghum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS S68203 REFERENCE S68203 !$#authors Koch, B.M.; Sibbesen, O.; Halkier, B.A.; Svendsen, I.; !1Moller, B.L. !$#journal Arch. Biochem. Biophys. (1995) 323:177-186 !$#title The primary sequence of cytochrome P450tyr, the !1multifunctional N-hydroxylase catalyzing the conversion of !1L-tyrosine to p-hydroxyphenylacetaldehyde oxime in the !1biosynthesis of the cyanogenic glucoside dhurrin in Sorghum !1bicolor (L.) Moench. !$#cross-references MUID:96019962; PMID:7487064 !$#accession S68203 !'##status preliminary !'##molecule_type mRNA !'##residues 1-558 ##label KOC !'##cross-references EMBL:U32624; NID:g984542; PIDN:AAA85440.1; !1PID:g984543 GENETICS !$#gene CYP79 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxidoreductase FEATURE !$348-515 #domain cytochrome P450 homology #label CYP\ !$493 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 558 #molecular-weight 61887 #checksum 7646 SEQUENCE /// ENTRY S51475 #type complete TITLE cytochrome P450 cyp78 - maize ORGANISM #formal_name Zea mays #common_name maize DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS S51475; S46317 REFERENCE S51475 !$#authors Larkin, J.C. !$#submission submitted to the EMBL Data Library, August 1993 !$#description Isolation of a cytochrome P450 homologue preferentially !1expressed in developing inflorescences of Zea mays L. !$#accession S51475 !'##status preliminary !'##molecule_type mRNA !'##residues 1-547 ##label LAR1 !'##cross-references EMBL:L23209; NID:g349717; PIDN:AAA61607.1; !1PID:g349718 REFERENCE S46317 !$#authors Larkin, J.C. !$#journal Plant Mol. Biol. (1994) 25:343-353 !$#title Isolation of a cytochrome P450 homologue preferentially !1expressed in developing inflorescences of Zea mays. !$#cross-references MUID:94325460; PMID:8049361 !$#accession S46317 !'##status preliminary !'##molecule_type mRNA !'##residues 1-174,'N',176-547 ##label LAR2 !'##cross-references EMBL:L23209; NID:g349717 GENETICS !$#gene cyp78 CLASSIFICATION #superfamily human cytochrome P450 CYP2D6; cytochrome P450 !1homology KEYWORDS chromoprotein; heme; iron; metalloprotein FEATURE !$342-512 #domain cytochrome P450 homology #label CYP\ !$490 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 547 #molecular-weight 58399 #checksum 8129 SEQUENCE /// ENTRY S11338 #type complete TITLE steroid 11beta-monooxygenase (EC 1.14.15.4) cytochrome P450 11B1 precursor - human ALTERNATE_NAMES cytochrome P450(11beta); steroid 11beta-hydroxylase ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S11338; S29068; A34181; B40223 REFERENCE S11338 !$#authors Kawamoto, T.; Mitsuuchi, Y.; Toda, K.; Miyahara, K.; !1Yokoyama, Y.; Nakao, K.; Hosoda, K.; Yamamoto, Y.; Imura, !1H.; Shizuta, Y. !$#journal FEBS Lett. (1990) 269:345-349 !$#title Cloning of cDNA and genomic DNA for human cytochrome P-450 !1(11-beta). !$#cross-references MUID:90382577; PMID:2401360 !$#accession S11338 !'##molecule_type mRNA !'##residues 1-503 ##label KAW !'##cross-references EMBL:X55764; NID:g30183; PIDN:CAA39290.1; !1PID:g30184 !$#accession S29068 !'##molecule_type DNA !'##residues 1-30 ##label KA3 !'##cross-references EMBL:X55765; NID:g30362; PIDN:CAA39291.1; !1PID:g30363 REFERENCE A92738 !$#authors Mornet, E.; Dupont, J.; Vitek, A.; White, P.C. !$#journal J. Biol. Chem. (1989) 264:20961-20967 !$#title Characterization of two genes encoding human steroid !111beta-hydroxylase (P-450-11beta). !$#cross-references MUID:90078185; PMID:2592361 !$#accession A34181 !'##molecule_type DNA !'##residues 1-42,'R',44-373,375-385,'A',387-431,'K',433-457,'V', !1459-493,'C',495-503 ##label MOR !'##cross-references GB:M32863; GB:M32878; GB:M32879; GB:J05140 REFERENCE A40223 !$#authors Kawamoto, T.; Mitsuuchi, Y.; Toda, K.; Yokoyama, Y.; !1Miyahara, K.; Miura, S.; Ohnishi, T.; Ichikawa, Y.; Nakao, !1K.; Imura, H.; Ulick, S.; Shizuta, Y. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:1458-1462 !$#title Role of steroid 11 beta-hydroxylase and steroid !118-hydroxylase in the biosynthesis of glucocorticoids and !1mineralocorticoids in humans. !$#cross-references MUID:92159068; PMID:1741400 !$#accession B40223 !'##molecule_type DNA !'##residues 1-30 ##label KA2 !'##cross-references GB:D10169; GB:D90428; NID:g219561; PIDN:BAA01039.1; !1PID:g219562 !'##note sequence extracted from NCBI backbone (NCBIN:82634, !1NCBIP:82638) GENETICS !$#gene GDB:CYP11B1; CYP11B !'##cross-references GDB:120603; OMIM:202010 !$#map_position 8q21-8q22 !$#introns 80/2; 132/2; 198/3; 266/3; 318/3; 373/3; 400/3; 466/3 CLASSIFICATION #superfamily human cytochrome P450 CYP11B1; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; monooxygenase; !1oxidoreductase; transmembrane protein FEATURE !$1-24 #domain transit peptide (mitochondrion) #status !8predicted #label TRN\ !$25-503 #product steroid 11beta-monooxygenase #status !8predicted #label MAT\ !$311-472 #domain cytochrome P450 homology #label P45\ !$450 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 503 #molecular-weight 57572 #checksum 438 SEQUENCE /// ENTRY O4BOM #type complete TITLE cholesterol monooxygenase (side-chain-cleaving) (EC 1.14.15.6) cytochrome P450 11A1 precursor, mitochondrial - bovine ALTERNATE_NAMES cytochrome P450(SCC) ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 03-Mar-2000 ACCESSIONS A00189; S15865; A24067; A42033; A28860; S29644; S04947 REFERENCE A00189 !$#authors Morohashi, K.; Fujii-Kuriyama, Y.; Okada, Y.; Sogawa, K.; !1Hirose, T.; Inayama, S.; Omura, T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:4647-4651 !$#title Molecular cloning and nucleotide sequence of cDNA for mRNA !1of mitochondrial cytochrome P-450(SCC) of bovine adrenal !1cortex. !$#cross-references MUID:84272690; PMID:6589615 !$#accession A00189 !'##molecule_type DNA !'##residues 1-520 ##label MOR !'##cross-references GB:K02130; NID:g162950; PIDN:AAA30488.1; !1PID:g162951 REFERENCE S15865 !$#authors Ahlgren, R.; Simpson, E.R.; Waterman, M.R.; Lund, J. !$#journal J. Biol. Chem. (1990) 265:3313-3319 !$#title Characterization of the promoter/regulatory region of the !1bovine CYP11A (P-450(scc)) gene. Basal and cAMP-dependent !1expression. !$#cross-references MUID:90153984; PMID:2154474 !$#accession S15865 !'##molecule_type DNA !'##residues 1-21,'S',23-90 ##label AHL !'##cross-references EMBL:J05245 REFERENCE A24067 !$#authors Chashchin, V.L.; Lapko, V.N.; Adamovich, T.B.; Lapko, A.G.; !1Kuprina, N.S.; Akhrem, A.A. !$#journal Biochim. Biophys. Acta (1986) 871:217-223 !$#title Primary structure of the cholesterol side-chain cleavage !1cytochrome P-450 from bovine adrenocortical mitochondria and !1some aspects of its functioning on a structural level. !$#cross-references MUID:86216225; PMID:3518802 !$#accession A24067 !'##molecule_type protein !'##residues 40-56,'D',58-105,'N',107-196,'N',198-520 ##label CHA REFERENCE A42033 !$#authors Pikuleva, I.A.; Lapko, A.G.; Chashchin, V.L. !$#journal J. Biol. Chem. (1992) 267:1438-1442 !$#title Functional reconstitution of cytochrome P-450-scc with hemin !1activated with Woodward's reagent K. Formation of a !1hemeprotein cross-link. !$#cross-references MUID:92112852; PMID:1730693 !$#accession A42033 !'##molecule_type protein !'##residues 216-233 ##label PIK REFERENCE A91972 !$#authors Ogishima, T.; Okada, Y.; Kominami, S.; Takemori, S.; Omura, !1T. !$#journal J. Biochem. (1983) 94:1711-1714 !$#title Partial amino acid sequences of two mitochondrial and two !1microsomal cytochrome P-450's from adrenal cortex. !$#cross-references MUID:84087829; PMID:6654880 !$#accession A28860 !'##molecule_type protein !'##residues 40-54 ##label OGS REFERENCE S29644 !$#authors Tsujita, M.; Ichikawa, Y. !$#journal Biochim. Biophys. Acta (1993) 1161:124-130 !$#title Substrate-binding region of cytochrome P-450(scc) (P-450 !1XIA1). Identification and primary structure of the !1cholesterol binding region in cytochrome P-450(scc). !$#cross-references MUID:93160229; PMID:8431464 !$#accession S29644 !'##molecule_type protein !'##residues 47-67 ##label TSU REFERENCE S04947 !$#authors Adamovich, T.B.; Pikuleva, I.A.; Chashchin, V.L.; Usanov, !1S.A. !$#journal Biochim. Biophys. Acta (1989) 996:247-253 !$#title Selective chemical modification of cytochrome P-450(SCC) !1lysine residues. Identification of lysines involved in the !1interaction with adrenodoxin. !$#cross-references MUID:89323202; PMID:2502182 !$#accession S04947 !'##molecule_type protein !'##residues 112-117;142-161;183-194;306-309;377-384 ##label ADA COMMENT This cytochrome P450 catalyzes the side-chain cleavage !1reaction of cholesterol in bovine adrenal cortex !1mitochondria. CLASSIFICATION #superfamily human cytochrome P450 CYP11B1; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; monooxygenase; !1oxidoreductase; transmembrane protein FEATURE !$1-39 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$40-520 #product cholesterol monooxygenase !8(side-chain-cleaving) cytochrome P450 11A1, !8mitochondrial #status experimental #label MAT\ !$47-67 #region substrate binding\ !$322-483 #domain cytochrome P450 homology #label CYP\ !$461 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 520 #molecular-weight 60332 #checksum 7382 SEQUENCE /// ENTRY S03188 #type complete TITLE cholesterol monooxygenase (side-chain-cleaving) (EC 1.14.15.6) cytochrome P450 11A1 precursor, mitochondrial - pig ALTERNATE_NAMES cytochrome P450(SCC) ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS S03188; PN0018; A54723; A30825 REFERENCE S03188 !$#authors Mulheron, G.W.; Stone, R.T.; Miller, W.L.; Wise, T. !$#journal Nucleic Acids Res. (1989) 17:1773 !$#title Nucleotide sequence of cytochrome P-450 cholesterol !1side-chain cleavage cDNA isolated from porcine testis. !$#cross-references MUID:89160344; PMID:2922297 !$#accession S03188 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-520 ##label MUL !'##cross-references EMBL:X13768; NID:g2024; PIDN:CAA32018.1; PID:g2025 REFERENCE PN0018 !$#authors Kuwada, M.; Kitajima, R.; Suzuki, H.; Horie, S. !$#journal Biochem. Biophys. Res. Commun. (1991) 176:1501-1508 !$#title Purification and properties of cytochrome P-450(SCC) from !1pig testis mitochondria. !$#cross-references MUID:91248248; PMID:2039527 !$#accession PN0018 !'##molecule_type protein !'##residues 41-58,'X',60-61 ##label KUW !'##experimental_source testis mitochondria REFERENCE A54723 !$#authors Iwahashi, K.; Tsubaki, M.; Miyatake, A.; Ichikawa, Y. !$#journal Int. J. Biochem. (1991) 23:901-909 !$#title Purification and comparative characterization of cytochrome !1P-450scc from porcine adrenocortical mitochondria. !$#cross-references MUID:92128625; PMID:1773895 !$#accession A54723 !'##molecule_type protein !'##residues 40-45,'F',47-64 ##label IWA !'##note sequence extracted from NCBI backbone (NCBIP:79244) COMMENT This protein catalyzes the conversion of cholesterol to !1pregnenolone. GENETICS !$#gene CYP11A1 CLASSIFICATION #superfamily human cytochrome P450 CYP11B1; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; monooxygenase; !1oxidoreductase; transmembrane protein FEATURE !$1-40 #domain transit peptide (mitochondrion) #status !8predicted #label TPP\ !$41-520 #product cholesterol monooxygenase !8(side-chain-cleaving) #status experimental #label !8MAT\ !$322-483 #domain cytochrome P450 homology #label P45\ !$369-392 #region steroid binding #status predicted\ !$461 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 520 #molecular-weight 60257 #checksum 6886 SEQUENCE /// ENTRY A34164 #type complete TITLE cholesterol monooxygenase (side-chain-cleaving) (EC 1.14.15.6) cytochrome P450 11A1 precursor, mitochondrial - rat ALTERNATE_NAMES cytochrome P450 SCC ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS A34164; A27321; A23688 REFERENCE A34164 !$#authors Oonk, R.B.; Krasnow, J.S.; Beattie, W.G.; Richards, J.S. !$#journal J. Biol. Chem. (1989) 264:21934-21942 !$#title Cyclic AMP-dependent and -independent regulation of !1cholesterol side chain cleavage cytochrome P-450 (P-450-scc) !1in rat ovarian granulosa cells and corpora lutea. cDNA and !1deduced amino acid sequence of rat P-450-scc. !$#cross-references MUID:90094378; PMID:2480959 !$#accession A34164 !'##molecule_type mRNA !'##residues 1-526 ##label OON !'##cross-references GB:J05156; NID:g203638; PIDN:AAA40989.1; !1PID:g203639 REFERENCE A27321 !$#authors McMasters, K.M.; Dickson, L.A.; Shamy, R.V.; Robischon, K.; !1Macdonald, G.J.; Moyle, W.R. !$#journal Gene (1987) 57:1-9 !$#title Rat cholesterol side-chain cleavage enzyme (P-450scc): use !1of a cDNA probe to study the hormonal regulation of P-450scc !1mRNA levels in ovarian granulosa cells. !$#cross-references MUID:88112851; PMID:3123325 !$#accession A27321 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 344-526 ##label MCM !'##cross-references GB:M22615; NID:g666941; PIDN:AAA62267.1; !1PID:g666942 REFERENCE A23688 !$#authors Oonk, R.B.; Parker, K.L.; Gibson, J.L.; Richards, J.S. !$#journal J. Biol. Chem. (1990) 265:22392-22401 !$#title Rat cholesterol side-chain cleavage cytochrome P-450 !1(P-450-SCC) gene. Structure and regulation by cAMP in vitro. !$#cross-references MUID:91093084; PMID:2176216 !$#accession A23688 !'##status preliminary !'##molecule_type DNA !'##residues 1-526 ##label OON2 !'##cross-references GB:M63133; NID:g203559; PIDN:AAA40958.1; !1PID:g203561 CLASSIFICATION #superfamily human cytochrome P450 CYP11B1; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; monooxygenase; !1oxidoreductase; transmembrane protein FEATURE !$320-481 #domain cytochrome P450 homology #label P45\ !$459 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 526 #molecular-weight 60585 #checksum 6451 SEQUENCE /// ENTRY A39740 #type complete TITLE sterol 27-monooxygenase (EC 1.14.14.-) cytochrome P450 27, precursor - human ALTERNATE_NAMES sterol 27-hydroxylase; vitamin D3 25-hydroxylase ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS A39740; I39233; I55588 REFERENCE A39740 !$#authors Cali, J.J.; Russell, D.W. !$#journal J. Biol. Chem. (1991) 266:7774-7778 !$#title Characterization of human sterol 27-hydroxylase. A !1mitochondrial cytochrome P-450 that catalyzes multiple !1oxidation reactions in bile acid biosynthesis. !$#cross-references MUID:91210301; PMID:1708392 !$#accession A39740 !'##molecule_type mRNA !'##residues 1-531 ##label CAL !'##cross-references GB:M62401; NID:g181291; PIDN:AAA52142.1; !1PID:g181292 REFERENCE I39233 !$#authors Guo, Y.D.; Strugnell, S.; Back, D.W.; Jones, G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:8668-8672 !$#title Transfected human liver cytochrome P-450 hydroxylates !1vitamin D analogs at different side-chain positions. !$#cross-references MUID:93391416; PMID:7690968 !$#accession I39233 !'##molecule_type mRNA !'##residues 1-19,'SA',22,'T',24,26-170,'R',172-531 ##label RES !'##cross-references EMBL:X59812; NID:g414120; PIDN:CAA42481.1; !1PID:g414121 !'##experimental_source HepG2 cells !'##note this enzyme, after transfection into transformed monkey kidney !1cells, was capable of 24-, 25-, and 26(27)-hydroxylation of !1vitamin D analogs REFERENCE I55588 !$#authors Leitersdorf, E.; Reshef, A.; Meiner, V.; Levitzki, R.; !1Schwartz, S.P.; Dann, E.J.; Berkman, N.; Cali, J.J.; !1Klapholz, L.; Berginer, V.M. !$#journal J. Clin. Invest. (1993) 91:2488-2496 !$#title Frameshift and splice-junction mutations in the sterol !127-hydroxylase gene cause cerebrotendinous xanthomatosis in !1Jews or Moroccan origin. !$#cross-references MUID:93293982; PMID:8514861 !$#accession I55588 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-15 ##label RE2 !'##cross-references GB:S62709; NID:g386290; PIDN:AAB27199.1; !1PID:g386291 GENETICS !$#gene GDB:CYP27 !'##cross-references GDB:128129; OMIM:213700 !$#map_position 2q33-2qter CLASSIFICATION #superfamily human cytochrome P450 CYP11B1; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; mitochondrion; monooxygenase; !1oxidoreductase; transmembrane protein FEATURE !$332-498 #domain cytochrome P450 homology #label P45\ !$476 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 531 #molecular-weight 60234 #checksum 8693 SEQUENCE /// ENTRY A33813 #type complete TITLE sterol 26-monooxygenase (EC 1.14.14.-) cytochrome P450 26A1 precursor, mitochondrial - rabbit ALTERNATE_NAMES cytochrome P450XXVIA1; sterol 26-hydroxylase ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS A33813; A90152; A90155; A30293; A32279 REFERENCE A33813 !$#authors Andersson, S.; Davis, D.L.; Dahlbaeck, H.; Joernvall, H.; !1Russell, D.W. !$#journal J. Biol. Chem. (1989) 264:8222-8229 !$#title Cloning, structure, and expression of the mitochondrial !1cytochrome P-450 sterol 26-hydroxylase, a bile acid !1biosynthetic enzyme. !$#cross-references MUID:89255259; PMID:2722778 !$#accession A33813 !'##molecule_type mRNA !'##residues 1-535 ##label AND !'##cross-references GB:J04717; NID:g164964; PIDN:AAA31225.1; !1PID:g164965 !'##note parts of this sequence, including the amino and carboxyl ends !1of the mature protein, were confirmed by peptide sequencing REFERENCE A90152 !$#authors Dahlbaeck, H. !$#journal Biochem. Biophys. Res. Commun. (1988) 157:30-36 !$#title Characterization of the liver mitochondrial cytochrome P-450 !1catalyzing the 26-hydroxylation of 5beta-cholestane-3alpha, !17alpha,12alpha-triol. !$#cross-references MUID:89061727; PMID:3196340 !$#accession A90152 !'##molecule_type protein !'##residues 37-44,'E',46-49,51-54,'GGV' ##label DAH REFERENCE A90155 !$#authors Dahlbaeck, H. !$#journal Biochem. Biophys. Res. Commun. (1989) 159:370 !$#accession A90155 !'##molecule_type protein !'##residues 37-54,'GGV' ##label DA2 GENETICS !$#gene CYP27 FUNCTION !$#description catalyzes the first step in the oxidation of the side chain !1of sterol intermediates for bile acid biosynthesis CLASSIFICATION #superfamily human cytochrome P450 CYP11B1; cytochrome P450 !1homology KEYWORDS cholesterol metabolism; chromoprotein; electron transfer; !1heme; iron; metalloprotein; mitochondrion; monooxygenase; !1oxidoreductase; transmembrane protein FEATURE !$1-36 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$37-535 #product cytochrome P450 27 #status experimental !8#label MAT\ !$335-502 #domain cytochrome P450 homology #label P45\ !$480 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 535 #molecular-weight 60254 #checksum 6107 SEQUENCE /// ENTRY O4RTV3 #type complete TITLE vitamin D3 25-monooxygenase (EC 1.14.14.-) cytochrome P450 27 precursor, mitochondrial - rat ALTERNATE_NAMES cholesterol 26-hydroxylase; cytochrome P450 CYP27; cytochrome P450c26/25; cytochrome P450mt3, phenobarbital-inducible; vitamin D3 25-hydroxylase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 03-Mar-2000 ACCESSIONS S09198; A34558; A36239; A33406; A40291 REFERENCE A34558 !$#authors Usui, E.; Noshiro, M.; Okuda, K. !$#journal FEBS Lett. (1990) 262:135-138 !$#title Molecular cloning of cDNA for vitamin D3 25-hydroxylase from !1rat liver mitochondria. !$#cross-references MUID:90201359; PMID:2318307 !$#accession S09198 !'##molecule_type mRNA !'##residues 1-533 ##label USU !'##cross-references EMBL:Y07534; NID:g56033; PIDN:CAA68822.1; !1PID:g56034 !$#accession A34558 !'##molecule_type protein !'##residues 33-37 ##label USU1 REFERENCE A36239 !$#authors Su, P.; Rennert, H.; Shayiq, R.M.; Yamamoto, R.; Zheng, !1Y.M.; Addya, S.; Strauss III, J.F.; Avadhani, N.G. !$#journal DNA Cell Biol. (1990) 9:657-665 !$#title A cDNA encoding a rat mitochondrial cytochrome P450 !1catalyzing both the 26-hydroxylation of cholesterol and !125-hydroxylation of vitamin D-3: gonadotropic regulation of !1the cognate mRNA in ovaries. !$#cross-references MUID:91083838; PMID:2175615 !$#accession A36239 !'##molecule_type mRNA !'##residues 1-430,'T',432-533 ##label SUA !'##cross-references GB:M38566; NID:g858743; PIDN:AAB02287.1; !1PID:g1374714 REFERENCE A33406 !$#authors Shayiq, R.M.; Avadhani, N.G. !$#journal Biochemistry (1989) 28:7546-7554 !$#title Purification and characterization of a hepatic mitochondrial !1cytochrome P-450 active in aflatoxin B-1 metabolism. !$#cross-references MUID:90122729; PMID:2514788 !$#accession A33406 !'##molecule_type protein !'##residues 33-39,'TD' ##label SHA REFERENCE A40291 !$#authors Addya, S.; Zheng, Y.M.; Shayiq, R.M.; Fan, J.; Avadhani, !1N.G. !$#journal Biochemistry (1991) 30:8323-8330 !$#title Characterization of a female-specific hepatic mitochondrial !1cytochrome P-450 whose steady-state level is modulated by !1testosterone. !$#cross-references MUID:91355184; PMID:1883820 !$#accession A40291 !'##molecule_type protein !'##residues 33-42 ##label ADD GENETICS !$#gene CYP27 CLASSIFICATION #superfamily human cytochrome P450 CYP11B1; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; liver; !1metalloprotein; mitochondrion; monooxygenase; !1oxidoreductase; transmembrane protein FEATURE !$1-32 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$33-533 #product vitamin D3 25-hydroxylase #status !8experimental #label MAT\ !$334-501 #domain cytochrome P450 homology #label CYP\ !$479 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 533 #molecular-weight 60733 #checksum 9229 SEQUENCE /// ENTRY JC5713 #type complete TITLE 25-hydroxyvitamin D3 1-alpha-hydroxylase (EC 1.14.-.-) precursor - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS JC5713 REFERENCE JC5713 !$#authors Monkawa, T.; Yoshida, T.; Wakino, S.; Shinki, T.; Anazawa, !1H.; DeLuca, H.F.; Suda, T.; Hayashi, M.; Saruta, T. !$#journal Biochem. Biophys. Res. Commun. (1997) 239:527-533 !$#title Molecular cloning of cDNA and genomic DNA for human !125-hydroxyvitamin D3 1-alpha-hydroxylase. !$#cross-references MUID:98008873; PMID:9344864 !$#accession JC5713 !'##molecule_type mRNA !'##residues 1-508 ##label MON !'##cross-references DDBJ:AB005038; NID:g2626736; PIDN:BAA23416.1; !1PID:g2626737 COMMENT This enzyme catalyzes the conversion of 25-hydroxyvitamin D3 !1to 1-alpha,25-dihydroxyvitamin D3. It plays also a role in !1calcium homeostasis. GENETICS !$#gene GDB:PDDR; VDR; VDD1; CYP27B; CYP1ALPHA !'##cross-references GDB:120486; OMIM:264700 !$#map_position 12q12-12q13 CLASSIFICATION #superfamily human cytochrome P450 CYP11B1; cytochrome P450 !1homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxidoreductase FEATURE !$314-477 #domain cytochrome P450 homology #label P45\ !$450-470 #domain heme-binding #status predicted #label HMB\ !$455 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 508 #molecular-weight 56503 #checksum 6863 SEQUENCE /// ENTRY A47436 #type complete TITLE 1,25-dihydroxyvitamin D3 24-hydroxylase (EC 1.14.-.-) precursor - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A47436 REFERENCE A47436 !$#authors Chen, K.S.; Prahl, J.M.; DeLuca, H.F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:4543-4547 !$#title Isolation and expression of human 1,25-dihydroxyvitamin D-3 !124-hydroxylase cDNA. !$#cross-references MUID:93281615; PMID:8506296 !$#accession A47436 !'##status preliminary !'##molecule_type mRNA !'##residues 1-513 ##label CHE !'##cross-references GB:L13286; NID:g306703; PIDN:AAA62379.1; !1PID:g306704 GENETICS !$#gene GDB:CYP24 !'##cross-references GDB:134534; OMIM:600125 !$#map_position 20q13.3-20q13.3 CLASSIFICATION #superfamily human cytochrome P450 CYP11B1; cytochrome P450 !1homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxidoreductase FEATURE !$1-35 #domain transit peptide (mitochondrion) #status !8predicted #label TRP\ !$36-513 #product 1,25-dihydroxyvitamin D3 24-hydroxylase !8#status predicted #label MAT\ !$322-483 #domain cytochrome P450 homology #label P45\ !$461 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 513 #molecular-weight 58781 #checksum 9111 SEQUENCE /// ENTRY JX0225 #type complete TITLE cytochrome P450 CYP10 - great pond snail CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Lymnaea stagnalis #common_name great pond snail DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS JX0225 REFERENCE JX0225 !$#authors Teunissen, Y.; Geraerts, W.P.M.; van Heerikhuizen, H.; !1Planta, R.J.; Joosse, J. !$#journal J. Biochem. (1992) 112:249-252 !$#title Molecular cloning of a cDNA encoding a member of a novel !1cytochrome P-450 family in the mollusc Lymnaea stagnalis. !$#cross-references MUID:93015787; PMID:1400265 !$#accession JX0225 !'##molecule_type mRNA !'##residues 1-545 ##label TEU !'##cross-references GB:S46130; NID:g257242; PIDN:AAB23599.1; !1PID:g257243 GENETICS !$#gene CYP10 CLASSIFICATION #superfamily human cytochrome P450 CYP11B1; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; monooxygenase; oxidoreductase FEATURE !$348-515 #domain cytochrome P450 homology #label P45\ !$493 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 545 #molecular-weight 62360 #checksum 1398 SEQUENCE /// ENTRY JH0659 #type complete TITLE cholesterol 7alpha-monooxygenase (EC 1.14.13.17) chain 1 - human ALTERNATE_NAMES cholesterol 7alpha-hydroxylase; cytochrome P450, subfamily VIIA ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 03-Mar-2000 ACCESSIONS S29818; JH0659; S11051; A42201; A54310 REFERENCE S29818 !$#authors Nishimoto, M.; Noshiro, M.; Okuda, K. !$#journal Biochim. Biophys. Acta (1993) 1172:147-150 !$#title Structure of the gene encoding human liver cholesterol !17alpha-hydroxylase. !$#cross-references MUID:93176797; PMID:8439551 !$#accession S29818 !'##status preliminary !'##molecule_type DNA !'##residues 1-504 ##label NIS !'##cross-references EMBL:L04633 REFERENCE JH0659 !$#authors Karam, W.G.; Chiang, J.Y.L. !$#journal Biochem. Biophys. Res. Commun. (1992) 185:588-595 !$#title Polymorphisms of human cholesterol 7 alpha-hydroxylase. !$#cross-references MUID:92304280; PMID:1610352 !$#accession JH0659 !'##molecule_type mRNA !'##residues 1-504 ##label KAR !'##cross-references GB:M93133; NID:g181318; PIDN:AAA58435.1; !1PID:g181319 !'##experimental_source liver !'##note 100-Ser was also found REFERENCE S11051 !$#authors Noshiro, M.; Okuda, K. !$#journal FEBS Lett. (1990) 268:137-140 !$#title Molecular cloning and sequence analysis of cDNA encoding !1human cholesterol 7-alpha-hydroxylase. !$#cross-references MUID:90346120; PMID:2384150 !$#accession S11051 !'##molecule_type mRNA !'##residues 1-346,'N',348-384,'S',386-504 ##label NOS !'##cross-references GB:M93133 REFERENCE A42201 !$#authors Molowa, D.T.; Chen, W.S.; Cimis, G.M.; Tan, C.P. !$#journal Biochemistry (1992) 31:2539-2544 !$#title Transcriptional regulation of the human cholesterol 7 !1alpha-hydroxylase gene. !$#cross-references MUID:92190183; PMID:1312351 !$#accession A42201 !'##molecule_type DNA !'##residues 1-25 ##label MOL !'##cross-references GB:M89647; GB:J05363; NID:g180469; PIDN:AAA58423.1; !1PID:g553228 !'##note sequence extracted from NCBI backbone (NCBIN:89078, !1NCBIP:89079) REFERENCE A54310 !$#authors Wang, D.P.; Chiang, J.Y. !$#journal Genomics (1994) 20:320-323 !$#title Structure and nucleotide sequences of the human cholesterol !17 alpha-hydroxylase gene (CYP7). !$#cross-references MUID:94292222; PMID:8020987 !$#accession A54310 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-140 ##label RES !'##cross-references GB:L13460; NID:g499855; PIDN:AAA61350.1; !1PID:g624966 COMMENT This liver microsomal enzyme catalyzes the conversion of !1cholesterol to bile acid; this reaction is the first and !1rate-limiting step in bile acid synthesis in the liver. GENETICS !$#gene GDB:CYP7A1; CYP7 !'##cross-references GDB:132221; OMIM:118455 !$#map_position 8q11-8q12 !$#introns 27/2; 107/3; 303/2; 347/1; 405/3 CLASSIFICATION #superfamily human cytochrome P450 CYP7A1; cytochrome P450 !1homology KEYWORDS cholesterol metabolism; chromoprotein; electron transfer; !1heme; iron; metalloprotein; monooxygenase; oxidoreductase; !1transmembrane protein FEATURE !$282-466 #domain cytochrome P450 homology #label CYP\ !$444 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 504 #molecular-weight 57660 #checksum 7470 SEQUENCE /// ENTRY A35376 #type complete TITLE cholesterol 7alpha-monooxygenase (EC 1.14.13.17) - rat ALTERNATE_NAMES cholesterol 7alpha-hydroxylase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 21-Jul-2000 ACCESSIONS A35376; A35609; A36450; S06632; A37071; A38736; S27206 REFERENCE A35376 !$#authors Jelinek, D.F.; Andersson, S.; Slaughter, C.A.; Russell, D.W. !$#journal J. Biol. Chem. (1990) 265:8190-8197 !$#title Cloning and regulation of cholesterol 7alpha-hydroxylase, !1the rate-limiting enzyme in bile acid biosynthesis. !$#cross-references MUID:90243699; PMID:2335522 !$#accession A35376 !'##molecule_type mRNA !'##residues 1-503 ##label JEL1 !'##cross-references GB:J05430; NID:g203792; PIDN:AAA41041.1; !1PID:g203793 REFERENCE A35609 !$#authors Jelinek, D.F.; Russell, D.W. !$#journal Biochemistry (1990) 29:7781-7785 !$#title Structure of the rat gene encoding cholesterol !17alpha-hydroxylase. !$#cross-references MUID:91084435; PMID:2261433 !$#accession A35609 !'##molecule_type DNA !'##residues 1-26 ##label JEL2 !'##cross-references GB:J02926 REFERENCE A36450 !$#authors Noshiro, M.; Nishimoto, M.; Okuda, K. !$#journal J. Biol. Chem. (1990) 265:10036-10041 !$#title Rat liver cholesterol 7alpha-hydroxylase. Pretranslational !1regulation for circadian rhythm. !$#cross-references MUID:90277612; PMID:1693613 !$#accession A36450 !'##molecule_type mRNA !'##residues 1-503 ##label NOS1 !'##cross-references GB:J05460; NID:g203455; PIDN:AAA03649.1; !1PID:g203456 REFERENCE S06632 !$#authors Noshiro, M.; Nishimoto, M.; Morohashi, K.I.; Okuda, K. !$#journal FEBS Lett. (1989) 257:97-100 !$#title Molecular cloning of cDNA for cholesterol 7alpha-hydroxylase !1from rat liver microsomes. Nucleotide sequence and !1expression. !$#cross-references MUID:90033362; PMID:2806567 !$#accession S06632 !'##molecule_type mRNA !'##residues 1-503 ##label NOS2 !'##cross-references GB:X17595; NID:g57535; PIDN:CAB57878.1; !1PID:g6018697 REFERENCE A37071 !$#authors Li, Y.C.; Wang, D.P.; Chiang, J.Y.L. !$#journal J. Biol. Chem. (1990) 265:12012-12019 !$#title Regulation of cholesterol 7alpha-hydroxylase in the liver. !1Cloning, sequencing, and regulation of cholesterol !17alpha-hydroxylase mRNA. !$#cross-references MUID:90307735; PMID:1694852 !$#accession A37071 !'##molecule_type mRNA !'##residues 1-503 ##label LIA !'##cross-references GB:J05509; NID:g203204; PIDN:AAA40839.1; !1PID:g203205 REFERENCE A38736 !$#authors Nishimoto, M.; Gotoh, O.; Okuda, K.; Noshiro, M. !$#journal J. Biol. Chem. (1991) 266:6467-6471 !$#title Structural analysis of the gene encoding rat cholesterol !1alpha-hydroxylase, the key enzyme for bile acid !1biosynthesis. !$#cross-references MUID:91177904; PMID:2007596 !$#accession A38736 !'##molecule_type DNA !'##residues 1-370,'S',372-503 ##label NIS !'##cross-references GB:M59184 REFERENCE S27206 !$#authors Chiang, J.Y.L.; Yang, T.P.; Wang, D.P. !$#journal Biochim. Biophys. Acta (1992) 1132:337-339 !$#title Cloning and 5'-flanking sequence of a rat cholesterol !17alpha-hydroxylase gene. !$#cross-references MUID:93041942; PMID:1420318 !$#accession S27206 !'##molecule_type DNA !'##residues 1-26 ##label CHI !'##cross-references GB:Z14108; GB:S48135; NID:g55835; PIDN:CAA78481.1; !1PID:g55836 COMMENT This liver microsomal enzyme catalyzes the conversion of !1cholesterol to bile acid; this reaction is the first and !1rate-limiting step in bile acid synthesis in the liver. GENETICS !$#introns 27/2; 107/3; 303/2; 347/1; 405/3 CLASSIFICATION #superfamily human cytochrome P450 CYP7A1; cytochrome P450 !1homology KEYWORDS cholesterol metabolism; chromoprotein; electron transfer; !1heme; iron; metalloprotein; monooxygenase; oxidoreductase; !1transmembrane protein FEATURE !$282-466 #domain cytochrome P450 homology #label P45\ !$444 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 503 #molecular-weight 56882 #checksum 6159 SEQUENCE /// ENTRY JC2231 #type complete TITLE prostaglandin-I synthase (EC 5.3.99.4) - human ALTERNATE_NAMES prostacyclin synthase ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS JC2231 REFERENCE JC2231 !$#authors Miyata, A.; Hara, S.; Yokoyama, C.; Inoue, H.; Ullrich, V.; !1Tanabe, T. !$#journal Biochem. Biophys. Res. Commun. (1994) 200:1728-1734 !$#title Molecular cloning and expression of human prostacyclin !1synthase. !$#cross-references MUID:94242046; PMID:8185632 !$#accession JC2231 !'##molecule_type mRNA !'##residues 1-500 ##label MIY !'##cross-references GB:D38145; NID:g537948; PIDN:BAA07343.1; !1PID:g537949 !'##experimental_source aortic endothelial cell COMMENT This enzyme catalyzes the conversion of prostaglandin H2 to !1prostaglandin I2. GENETICS !$#gene GDB:PTGIS; PGIS; CYP8 !'##cross-references GDB:362921; OMIM:601699 !$#map_position 20q13.11-20q13.13 CLASSIFICATION #superfamily human cytochrome P450 CYP7A1; cytochrome P450 !1homology KEYWORDS intramolecular oxidoreductase; isomerase SUMMARY #length 500 #molecular-weight 57103 #checksum 5644 SEQUENCE /// ENTRY S68855 #type complete TITLE lanosterol 14alpha-demethylase (EC 1.14.14.-) cytochrome P450 51 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S68855 REFERENCE S68855 !$#authors Stroemstedt, M.; Rozman, D.; Waterman, M.R. !$#journal Arch. Biochem. Biophys. (1996) 329:73-81 !$#title The ubiquitously expressed human CYP51 encodes lanosterol !114alpha-demethylase, a cytochrome P450 whose expression is !1regulated by oxysterols. !$#cross-references MUID:96201125; PMID:8619637 !$#accession S68855 !'##status preliminary; nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-509 ##label STR !'##cross-references EMBL:U23942 GENETICS !$#gene GDB:CYP51 !'##cross-references GDB:4073039; OMIM:601637 !$#map_position 7q21.2-7q21.3 CLASSIFICATION #superfamily human cytochrome P450 CYP51; cytochrome P450 !1homology KEYWORDS chromoprotein; heme; iron; metalloprotein; monooxygenase; !1oxidoreductase FEATURE !$314-477 #domain cytochrome P450 homology #label P45\ !$455 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 509 #molecular-weight 57306 #checksum 8776 SEQUENCE /// ENTRY O4CK51 #type complete TITLE lanosterol 14alpha-demethylase (EC 1.14.14.-) cytochrome P450 51 - yeast (Candida albicans) ALTERNATE_NAMES cytochrome P450 LIA1 ORGANISM #formal_name Candida albicans DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Mar-2000 ACCESSIONS S02713 REFERENCE S02713 !$#authors Lai, M.H.; Kirsch, D.R. !$#journal Nucleic Acids Res. (1989) 17:804 !$#title Nucleotide sequence of cytochrome P450 L1A1 (lanosterol !114alpha-demethylase) from Candida albicans. !$#cross-references MUID:89128456; PMID:2644625 !$#accession S02713 !'##molecule_type DNA !'##residues 1-528 ##label LAI !'##cross-references EMBL:X13296 GENETICS !$#gene CYP51 CLASSIFICATION #superfamily human cytochrome P450 CYP51; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; monooxygenase; oxidoreductase FEATURE !$304-492 #domain cytochrome P450 homology #label CYP\ !$470 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 528 #molecular-weight 60701 #checksum 5623 SEQUENCE /// ENTRY A31854 #type complete TITLE lanosterol 14alpha-demethylase (EC 1.14.14.-) cytochrome P450 51 - yeast (Candida tropicalis) ALTERNATE_NAMES cytochrome P450 14DM ORGANISM #formal_name Candida tropicalis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS A31854; A26828 REFERENCE A31854 !$#authors Chen, C.; Kalb, V.F.; Turi, T.G.; Loper, J.C. !$#journal DNA (1988) 7:617-626 !$#title Primary structure of the cytochrome P450 lanosterol !114alpha-demethylase gene from Candida tropicalis. !$#cross-references MUID:89152749; PMID:3068024 !$#accession A31854 !'##molecule_type DNA !'##residues 1-528 ##label CHE !'##cross-references GB:M23673; NID:g341007; PIDN:AAA53284.1; !1PID:g576547 !'##experimental_source ATCC 750 REFERENCE A26828 !$#authors Chen, C.; Turi, T.G.; Sanglard, D.; Loper, J.C. !$#journal Biochem. Biophys. Res. Commun. (1987) 146:1311-1317 !$#title Isolation of the Candida tropicalis gene for P450 lanosterol !1demethylase and its expression in Saccharomyces cerevisiae. !$#cross-references MUID:87298576; PMID:3304292 !$#accession A26828 !'##molecule_type DNA !'##residues 434-447,'V',449-499,'G',501-528 ##label CH2 !'##cross-references GB:M17595; NID:g170811; PIDN:AAA34316.1; !1PID:g170812 !'##experimental_source ATCC 750 !'##note the authors translated the codon GTT for residue 448 as Gly and !1GGT for residue 500 as Val GENETICS !$#gene CYP51 CLASSIFICATION #superfamily human cytochrome P450 CYP51; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; monooxygenase; oxidoreductase FEATURE !$304-492 #domain cytochrome P450 homology #label P45\ !$470 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 528 #molecular-weight 60927 #checksum 4431 SEQUENCE /// ENTRY A27491 #type complete TITLE lanosterol 14alpha-demethylase (EC 1.14.14.-) cytochrome P450 51 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YHR007c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 23-Mar-2001 ACCESSIONS A27491; S46804; B31569; A25563 REFERENCE A27491 !$#authors Kalb, V.F.; Woods, C.W.; Turi, T.G.; Dey, C.R.; Sutter, !1T.R.; Loper, J.C. !$#journal DNA (1987) 6:529-537 !$#title Primary structure of the P450 lanosterol demethylase gene !1from Saccharomyces cerevisiae. !$#cross-references MUID:88111027; PMID:3322742 !$#accession A27491 !'##molecule_type DNA !'##residues 1-530 ##label KAL1 !'##cross-references EMBL:M18109; NID:g170945; PIDN:AAA34379.1; !1PID:g170946 REFERENCE S46797 !$#authors Favello, T. !$#submission submitted to the EMBL Data Library, June 1994 !$#description The sequence of S. cerevisiae cosmid 9780. !$#accession S46804 !'##molecule_type DNA !'##residues 1-530 ##label FAV !'##cross-references EMBL:U10555; NID:g500813; PIDN:AAB68433.1; !1PID:g500824; GSPDB:GN00008; MIPS:YHR007c REFERENCE A31569 !$#authors Ishida, N.; Aoyama, Y.; Hatanaka, R.; Oyama, Y.; Imajo, S.; !1Ishiguro, M.; Oshima, T.; Nakazato, H.; Noguchi, T.; Maitra, !1U.S.; Mohan, V.P.; Sprinson, D.B.; Yoshida, Y. !$#journal Biochem. Biophys. Res. Commun. (1988) 155:317-323 !$#title A single amino acid substitution converts cytochrome !1P450-14DM to an inactive form, cytochrome P450-SG1: complete !1primary structures deduced from cloned DNAs. !$#cross-references MUID:88326319; PMID:3046615 !$#accession B31569 !'##molecule_type DNA !'##residues 1-432,'N',434-530 ##label ISH !'##cross-references EMBL:M21483; NID:g171353; PIDN:AAA34546.1; !1PID:g171354 REFERENCE A25563 !$#authors Kalb, V.F.; Loper, J.C.; Dey, C.R.; Woods, C.W.; Sutter, !1T.R. !$#journal Gene (1986) 45:237-245 !$#title Isolation of a cytochrome P-450 structural gene from !1Saccharomyces cerevisiae. !$#cross-references MUID:87106820; PMID:3542713 !$#accession A25563 !'##molecule_type DNA !'##residues 444-530 ##label KAL2 !'##cross-references EMBL:M15663 GENETICS !$#gene SGD:ERG11; MIPS:YHR007c !'##cross-references SGD:S0001049; MIPS:YHR007c !$#map_position 8R CLASSIFICATION #superfamily human cytochrome P450 CYP51; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; monooxygenase; oxidoreductase FEATURE !$311-492 #domain cytochrome P450 homology #label P45\ !$470 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 530 #molecular-weight 60720 #checksum 2571 SEQUENCE /// ENTRY S52319 #type complete TITLE unspecific monooxygenase (EC 1.14.14.1) - smut fungus (Ustilago maydis) ORGANISM #formal_name Ustilago maydis #common_name corn smut DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S52319 REFERENCE S52319 !$#authors Hargreaves, J.A.; Keon, J.P.R. !$#submission submitted to the EMBL Data Library, February 1995 !$#description The sterol 14 alpha-demethylase (ERG11) gene from Ustilago !1maydis. !$#accession S52319 !'##status preliminary !'##molecule_type DNA !'##residues 1-561 ##label HAR !'##cross-references EMBL:Z48164; NID:g663266; PIDN:CAA88176.1; !1PID:g663267 CLASSIFICATION #superfamily human cytochrome P450 CYP51; cytochrome P450 !1homology KEYWORDS chromoprotein; heme; iron; metalloprotein; monooxygenase; !1oxidoreductase FEATURE !$322-523 #domain cytochrome P450 homology #label P45\ !$501 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 561 #molecular-weight 62197 #checksum 8272 SEQUENCE /// ENTRY S65578 #type complete TITLE lanosterol 14alpha-demethylase (EC 1.14.14.-) cytochrome P450 51 - Penicillium italicum ORGANISM #formal_name Penicillium italicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S65578; S54836 REFERENCE S65578 !$#authors van Nistelrooy, J.G.M.; van den Brink, J.M.; van Kan, !1J.A.L.; van Gorcom, R.F.M.; de Waard, M.A. !$#journal Mol. Gen. Genet. (1996) 250:725-733 !$#title Isolation and molecular characterisation of the gene !1encoding eburicol 14-alpha-demethylase (CYP51) from !1Penicillium italicum. !$#cross-references MUID:96204513; PMID:8628233 !$#accession S65578 !'##molecule_type DNA !'##residues 1-515 ##label VAN !'##cross-references EMBL:Z49750; NID:g836641; PIDN:CAA89824.1; !1PID:g836642 GENETICS !$#gene CYP51 !$#introns 72/3; 138/3; 497/3 CLASSIFICATION #superfamily human cytochrome P450 CYP51; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; monooxygenase; oxidoreductase FEATURE !$301-481 #domain cytochrome P450 homology #label P45\ !$459 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 515 #molecular-weight 58136 #checksum 2742 SEQUENCE /// ENTRY G70706 #type complete TITLE probable sterol demethylase (EC 1.14.-.-) Rv0764c - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G70706 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession G70706 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-451 ##label COL !'##cross-references GB:Z80226; GB:AL123456; NID:g3261638; !1PIDN:CAB02394.1; PID:g1550642 !'##experimental_source strain H37Rv GENETICS !$#gene Rv0764c CLASSIFICATION #superfamily human cytochrome P450 CYP51; cytochrome P450 !1homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxidoreductase FEATURE !$253-416 #domain cytochrome P450 homology #label P45\ !$394 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 451 #molecular-weight 50877 #checksum 6784 SEQUENCE /// ENTRY O4HU19 #type complete TITLE aromatase (EC 1.14.14.-) cytochrome P450 19 - human ALTERNATE_NAMES cytochrome P450 aromatase; estrogen synthetase ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Mar-2000 ACCESSIONS A34451; A40542; S03962; A31580; A31255; A40142; S22908; !1A48762; A29480; B29840; A42405; A24344; A23546; A38241; !1B24344; C24344; D24344; E24344; PC2041 REFERENCE A34451 !$#authors Means, G.D.; Mahendroo, M.S.; Corbin, C.J.; Mathis, J.M.; !1Powell, F.E.; Mendelson, C.R.; Simpson, E.R. !$#journal J. Biol. Chem. (1989) 264:19385-19391 !$#title Structural analysis of the gene encoding human aromatase !1cytochrome P-450, the enzyme responsible for estrogen !1biosynthesis. !$#cross-references MUID:90037080; PMID:2808431 !$#accession A34451 !'##molecule_type DNA !'##residues 1-503 ##label MEA !'##cross-references EMBL:M30803 !'##note the authors translated the codon ATC for residue 70 as Thr REFERENCE A40542 !$#authors Mahendroo, M.S.; Means, G.D.; Mendelson, C.R.; Simpson, E.R. !$#journal J. Biol. Chem. (1991) 266:11276-11281 !$#title Tissue-specific expression of human P-450-AROM. The promoter !1responsible for expression in adipose tissue is different !1from that utilized in placenta. !$#cross-references MUID:91250444; PMID:2040633 !$#accession A40542 !'##status preliminary !'##molecule_type DNA !'##residues 1-48 ##label MAH !'##cross-references GB:M74174 REFERENCE S03962 !$#authors Toda, K.; Terashima, M.; Mitsuuchi, Y.; Yamasaki, Y.; !1Yokoyama, Y.; Nojima, S.; Ushiro, H.; Maeda, T.; Yamamoto, !1Y.; Sagara, Y.; Shizuta, Y. !$#journal FEBS Lett. (1989) 247:371-376 !$#title Alternative usage of different poly(A) addition signals for !1two major species of mRNA encoding human aromatase P-450. !$#cross-references MUID:89232157; PMID:2541021 !$#accession S03962 !'##molecule_type mRNA !'##residues 1-503 ##label TOD !'##cross-references EMBL:Y07508; NID:g28848; PIDN:CAA68807.1; !1PID:g28849 !'##note 14-Ser was also found REFERENCE A31580 !$#authors Harada, N. !$#journal Biochem. Biophys. Res. Commun. (1988) 156:725-732 !$#title Cloning of a complete cDNA encoding human aromatase: !1immunochemical identification and sequence analysis. !$#cross-references MUID:89050098; PMID:2973313 !$#accession A31580 !'##molecule_type mRNA !'##residues 1-495,'S',497-503 ##label HAR !'##cross-references EMBL:M22246; NID:g179001; PIDN:AAA35557.1; !1PID:g179002 REFERENCE A31255 !$#authors Corbin, C.J.; Graham-Lorence, S.; McPhaul, M.; Mason, J.I.; !1Mendelson, C.R.; Simpson, E.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:8948-8952 !$#title Isolation of a full-length cDNA insert encoding human !1aromatase system cytochrome P-450 and its expression in !1nonsteroidogenic cells. !$#cross-references MUID:89057856; PMID:2848247 !$#accession A31255 !'##molecule_type mRNA !'##residues 1-263,'C',265-503 ##label CO1 !'##cross-references EMBL:J04127; NID:g181212; PIDN:AAA52132.1; !1PID:g181213 REFERENCE A40142 !$#authors Pompon, D.; Liu, R.Y.K.; Besman, M.J.; Wang, P.L.; Shively, !1J.E.; Chen, S. !$#journal Mol. Endocrinol. (1989) 3:1477-1487 !$#title Expression of human placental aromatase in Saccharomyces !1cerevisiae. !$#cross-references MUID:90114215; PMID:2691883 !$#accession A40142 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-7,'Q',9-440,'V',442-503 ##label POM !'##experimental_source placenta REFERENCE S22908 !$#authors Simpson, E.R.; Evans, C.T.; Corbin, C.J.; Powell, F.E.; !1Ledesma, D.B.; Mendelson, C.R. !$#journal Mol. Cell. Endocrinol. (1987) 52:267-272 !$#title Sequencing of cDNA inserts encoding aromatase cytochrome !1P-450 (P-450(AROM)). !$#cross-references MUID:88005438; PMID:3653507 !$#accession S22908 !'##molecule_type mRNA !'##residues 85-263,'C',265-503 ##label CO2 !'##cross-references EMBL:M28420; NID:g181287; PIDN:AAA52141.1; !1PID:g181288 !'##note the authors translated the codon ATG for residue 219 as His REFERENCE A48762 !$#authors Mahendroo, M.S.; Mendelson, C.R.; Simpson, E.R. !$#journal J. Biol. Chem. (1993) 268:19463-19470 !$#title Tissue-specific and hormonally controlled alternative !1promoters regulate aromatase cytochrome P450 gene expression !1in human adipose tissue. !$#cross-references MUID:93374934; PMID:7690033 !$#accession A48762 !'##molecule_type mRNA !'##residues 1-48 ##label MA2 !'##note different 5'-untranslated sequences were demonstrated in a !1variety of clones REFERENCE A29480 !$#authors Chen, S.; Besman, M.J.; Sparkes, R.S.; Zollman, S.; Klisak, !1I.; Mohandas, T.; Hall, P.F.; Shively, J.E. !$#journal DNA (1988) 7:27-38 !$#title Human aromatase: cDNA cloning, southern blot analysis, and !1assignment of the gene to chromosome 15. !$#cross-references MUID:88166351; PMID:3390233 !$#accession A29480 !'##molecule_type mRNA !'##residues 85-503 ##label CHE !'##cross-references EMBL:M18856; NID:g178999; PIDN:AAA35556.1; !1PID:g179000 !$#accession B29840 !'##molecule_type protein !'##residues !1120-142;151-169;253-262;294-311;335-343;347-443;462-483; !1486-503 ##label CH2 REFERENCE A42405 !$#authors Harada, N.; Ogawa, H.; Shozu, M.; Yamada, K.; Suhara, K.; !1Nishida, E.; Takagi, Y. !$#journal J. Biol. Chem. (1992) 267:4781-4785 !$#title Biochemical and molecular genetic analyses on placental !1aromatase (P-450AROM) deficiency. !$#cross-references MUID:92165841; PMID:1371509 !$#accession A42405 !'##molecule_type mRNA !'##residues 246-248,'QVIQLWKIYEYNWIGFFPLCLCCFSWPLS',249-258 ##label HA2 !'##cross-references GB:S85075; NID:g246080; PIDN:AAB21500.1; !1PID:g246081 !'##experimental_source placenta; placental aromatase deficiency patient !'##note sequence extracted from NCBI backbone (NCBIN:85075, !1NCBIP:85080) !'##note mutation of the splice donor for intron 6 and splicing instead !1at a cryptic splice donor causes an in-frame insertion in !1this patient with placental aromatase deficiency REFERENCE A24344 !$#authors Chen, S.; Shively, J.E.; Nakajin, S.; Shinoda, M.; Hall, !1P.F. !$#journal Biochem. Biophys. Res. Commun. (1986) 135:713-719 !$#title Amino terminal sequence analysis of human placenta !1aromatase. !$#cross-references MUID:86186829; PMID:3964273 !$#accession A24344 !'##molecule_type protein !'##residues 2-11,'L',13,'LVL',17,'LP',20-21,'V';120-126,'HE', !1129-130;160-170;463-473;496-503 ##label CH3 !'##experimental_source placenta REFERENCE A23546 !$#authors Evans, C.T.; Ledesma, D.B.; Schulz, T.Z.; Simpson, E.R.; !1Mendelson, C.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:6387-6391 !$#title Isolation and characterization of a complementary DNA !1specific for human aromatase-system cytochrome P-450 mRNA. !$#cross-references MUID:86313586; PMID:3018730 !$#accession A23546 !'##molecule_type mRNA !'##residues 458-476 ##label EVA REFERENCE A38241 !$#authors Hagerman, D.D. !$#submission submitted to the Protein Sequence Database, July 1992 !$#accession A38241 !'##molecule_type protein !'##residues 'XXX',8-11,'L',13-18,'Z',20-23,'L',25-27,'T',29 ##label HAG !'##experimental_source placenta REFERENCE PC2041 !$#authors Honda, S.; Harada, N.; Takagi, Y. !$#journal Biochem. Biophys. Res. Commun. (1994) 198:1153-1160 !$#title Novel exon 1 of the aromatase gene specific for aromatase !1transcripts in human brain. !$#cross-references MUID:94161727; PMID:8117272 !$#contents annotation; alternative exons 1 (coding region begins in !1exon 2) GENETICS !$#gene GDB:CYP19 !'##cross-references GDB:119830; OMIM:107910 !$#map_position 15q21.1-15q21.1 !$#introns 49/1; 99/2; 151/1; 210/1; 248/2; 286/3; 341/1; 421/3 CLASSIFICATION #superfamily human cytochrome P450 CYP19; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; endoplasmic reticulum; !1heme; iron; metalloprotein; monooxygenase; oxidoreductase; !1polymorphism; steroid biosynthesis; transmembrane protein FEATURE !$303-459 #domain cytochrome P450 homology #label CYP\ !$437 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 503 #molecular-weight 57882 #checksum 1937 SEQUENCE /// ENTRY A36121 #type complete TITLE aromatase (EC 1.14.14.-) cytochrome P450 19 - rat ALTERNATE_NAMES cytochrome P450 arom ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS A36121; S16901; S26817 REFERENCE A36121 !$#authors Hickey, G.J.; Krasnow, J.S.; Beattie, W.G.; Richards, J.S. !$#journal Mol. Endocrinol. (1990) 4:3-12 !$#title Aromatase cytochrome P450 in rat ovarian granulosa cells !1before and after luteinization: adenosine 3', !15'-monophosphate-dependent and independent regulation. !1Cloning and sequencing of rat aromatase cDNA and 5' genomic !1DNA. !$#cross-references MUID:90220647; PMID:2157976 !$#accession A36121 !'##molecule_type mRNA !'##residues 1-508 ##label HIC !'##cross-references EMBL:M33986; NID:g203804; PIDN:AAA41044.1; !1PID:g203805 REFERENCE S16901 !$#authors Lephart, E.D.; Peterson, K.G.; Noble, J.F.; George, F.W.; !1McPhaul, M.J. !$#journal Mol. Cell. Endocrinol. (1990) 70:31-40 !$#title The structure of cDNA clones encoding the aromatase P-450 !1isolated from a rat Leydig cell tumor line demonstrates !1differential processing of aromatase mRNA in rat ovary and a !1neoplastic cell line. !$#cross-references MUID:90255798; PMID:2340950 !$#accession S16901 !'##status preliminary !'##molecule_type mRNA !'##residues 1-2,'FQ',5-9,'Q',11-87,'C',89-100,'L',102-122,'VVH',126, !1'HAR',130-187,'L',189-209,'G',211-327,'WKQ',332-341,'A', !1343-363,'CGIS',368,'F',370-421,'L',423-424,'T',426-448,'I', !1450-465,'K',467-492,'SPRNS' ##label LEP GENETICS !$#gene CYP19 CLASSIFICATION #superfamily human cytochrome P450 CYP19; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; endoplasmic reticulum; !1heme; iron; metalloprotein; microsome; monooxygenase; !1oxidoreductase; transmembrane protein FEATURE !$303-459 #domain cytochrome P450 homology #label P45\ !$437 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 508 #molecular-weight 58411 #checksum 7209 SEQUENCE /// ENTRY A31916 #type complete TITLE aromatase (EC 1.14.14.-) cytochrome P450 19 (version 1) - chicken ALTERNATE_NAMES cytochrome P450 arom ORGANISM #formal_name Gallus gallus #common_name chicken DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 21-Jul-2000 ACCESSIONS A31916 REFERENCE A31916 !$#authors McPhaul, M.J.; Noble, J.F.; Simpson, E.R.; Mendelson, C.R.; !1Wilson, J.D. !$#journal J. Biol. Chem. (1988) 263:16358-16363 !$#title The expression of a functional cDNA encoding the chicken !1cytochrome P-450-arom (aromatase) that catalyzes the !1formation of estrogen from androgen. !$#cross-references MUID:89034107; PMID:3182796 !$#accession A31916 !'##molecule_type mRNA !'##residues 1-507 ##label MCP !'##cross-references EMBL:J04047; NID:g211703; PIDN:AAA48738.1; !1PID:g211704 !'##note it is uncertain whether Met-1 or Met-20 is the initiator GENETICS !$#gene CYP19 CLASSIFICATION #superfamily human cytochrome P450 CYP19; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; endoplasmic reticulum; !1heme; iron; metalloprotein; monooxygenase; oxidoreductase; !1transmembrane protein FEATURE !$302-458 #domain cytochrome P450 homology #label P45\ !$436 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 507 #molecular-weight 58146 #checksum 1052 SEQUENCE /// ENTRY O4HUB1 #type complete TITLE cytochrome P450 4B1 - human ALTERNATE_NAMES cytochrome P450-HP CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Mar-2000 ACCESSIONS S07765; S17971; A33414 REFERENCE S07765 !$#authors Yokotani, N.; Sogawa, K.; Matsubara, S.; Gotoh, O.; !1Kusunose, E.; Kusunose, M.; Fujii-Kuriyama, Y. !$#journal Eur. J. Biochem. (1990) 187:23-29 !$#title cDNA cloning of cytochrome P-450 related to P-450(p-2) from !1the cDNA library of human placenta. Gene structure and !1expression. !$#cross-references MUID:90126824; PMID:2298205 !$#accession S07765 !'##molecule_type DNA !'##residues 1-511 ##label YOK !'##cross-references GB:X16699; NID:g35204; PIDN:CAA34672.1; PID:g35205 !$#accession S17971 !'##molecule_type mRNA !'##residues 9-511 ##label YOK2 !'##cross-references EMBL:X16699 REFERENCE A33414 !$#authors Nhamburo, P.T.; Gonzalez, F.J.; McBride, O.W.; Gelboin, !1H.V.; Kimura, S. !$#journal Biochemistry (1989) 28:8060-8066 !$#title Identification of a new P450 expressed in human lung: !1complete cDNA sequence, cDNA-directed expression, and !1chromosome mapping. !$#cross-references MUID:90105307; PMID:2574990 !$#accession A33414 !'##molecule_type DNA !'##residues 1-36,'R',38-511 ##label NHA !'##cross-references EMBL:J02871; NID:g180968; PIDN:AAA35712.1; !1PID:g180969 GENETICS !$#gene GDB:CYP4B1 !'##cross-references GDB:125372; OMIM:124075 !$#map_position 1p34-1p12 !$#introns 60/3; 108/1; 123/1; 165/3; 258/1; 293/3; 357/2; 402/1; 423/ !13; 451/2 CLASSIFICATION #superfamily human cytochrome P450 CYP4B1; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; monooxygenase; oxidoreductase; transmembrane !1protein FEATURE !$312-475 #domain cytochrome P450 homology #label CYP\ !$453 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 511 #molecular-weight 58991 #checksum 8787 SEQUENCE /// ENTRY A40164 #type complete TITLE cytochrome P450 4B1 - rabbit ALTERNATE_NAMES cytochrome P450 isoform 5 CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Mar-2000 ACCESSIONS A40164; B61538 REFERENCE A40164 !$#authors Gasser, R.; Philpot, R.M. !$#journal Mol. Pharmacol. (1989) 35:617-625 !$#title Primary structures of cytochrome P-450 isozyme 5 from rabbit !1and rat and regulation of species-dependent expression and !1induction in lung and liver: identification of cytochrome !1P-450 gene subfamily IVB. !$#cross-references MUID:89261667; PMID:2725471 !$#accession A40164 !'##molecule_type mRNA !'##residues 1-506 ##label GAS !'##cross-references GB:M29852; NID:g164920; PIDN:AAA31214.1; !1PID:g164921 !'##note the authors translated the codon CAG for residue 57 as Gly REFERENCE A61538 !$#authors Parandoosh, Z.; Fujita, V.S.; Coon, M.J.; Philpot, R.M. !$#journal Drug Metab. Dispos. (1987) 15:59-67 !$#title Cytochrome P-450 isozymes 2 and 5 in rabbit lung and liver. !1Comparisons of structure and inducibility. !$#cross-references MUID:87161284; PMID:2881760 !$#accession B61538 !'##molecule_type protein !'##residues 1-21 ##label PAR CLASSIFICATION #superfamily human cytochrome P450 CYP4B1; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; monooxygenase; oxidoreductase; transmembrane !1protein FEATURE !$307-470 #domain cytochrome P450 homology #label CYP\ !$448 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 506 #molecular-weight 58603 #checksum 4074 SEQUENCE /// ENTRY B40164 #type complete TITLE cytochrome P450 4B1 - rat ALTERNATE_NAMES cytochrome P450 L-2; P450 isozyme 5 CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Mar-2000 ACCESSIONS B40164; PQ0092 REFERENCE A40164 !$#authors Gasser, R.; Philpot, R.M. !$#journal Mol. Pharmacol. (1989) 35:617-625 !$#title Primary structures of cytochrome P-450 isozyme 5 from rabbit !1and rat and regulation of species-dependent expression and !1induction in lung and liver: identification of cytochrome !1P-450 gene subfamily IVB. !$#cross-references MUID:89261667; PMID:2725471 !$#accession B40164 !'##molecule_type mRNA !'##residues 1-511 ##label GAS !'##cross-references GB:M29853; NID:g205911; PIDN:AAA41778.1; !1PID:g205912 !'##note the authors translated the codon CAG for residue 62 as Gly REFERENCE PQ0092 !$#authors Imaoka, S.; Funae, Y. !$#journal J. Biochem. (1990) 108:33-36 !$#title Purification and characterization of rat pulmonary !1cytochrome P-450. !$#cross-references MUID:91035323; PMID:2229008 !$#accession PQ0092 !'##molecule_type protein !'##residues 2-6,'X',8,'X',10,'X' ##label IMA !'##experimental_source lung microsomes GENETICS !$#gene CYP4B1 CLASSIFICATION #superfamily human cytochrome P450 CYP4B1; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; lung; !1metalloprotein; monooxygenase; oxidoreductase; transmembrane !1protein FEATURE !$312-475 #domain cytochrome P450 homology #label CYP\ !$453 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 511 #molecular-weight 58936 #checksum 6116 SEQUENCE /// ENTRY A29368 #type complete TITLE prostaglandin omega-hydroxylase (EC 1.14.15.-) cytochrome P450 4A4 - rabbit ALTERNATE_NAMES cytochrome P450-P2; cytochrome P450kd ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Mar-2000 ACCESSIONS S32315; S32423; A29368; JN0089 REFERENCE S32315 !$#authors Palmer, C.N.A.; Griffin, K.J.; Johnson, E.F. !$#journal Arch. Biochem. Biophys. (1993) 300:670-676 !$#title Rabbit prostaglandin omega-hydroxylase (CYP4A4): gene !1structure and expression. !$#cross-references MUID:93167855; PMID:8434947 !$#accession S32315 !'##molecule_type DNA !'##residues 1-510 ##label PAL1 REFERENCE S32423 !$#authors Palmer, C.N.A.; Griffin, K.J.; Johnson, E.F. !$#submission submitted to the EMBL Data Library, May 1993 !$#description Rabbit prostaglandin omega-hydroxylase (CYP4A4): gene !1structure and expression. !$#accession S32423 !'##molecule_type DNA !'##residues 1-26,'CSCCCSRQLSSTCTASGCSERSSSSRARPSTGSWGTAE' ##label PAL2 !'##cross-references EMBL:L04758; NID:g164972; PIDN:AAA31228.1; !1PID:g552372 !'##note the difference at the amino end is due to a frameshift error REFERENCE A29368 !$#authors Matsubara, S.; Yamamoto, S.; Sogawa, K.; Yokotani, N.; !1Fujii-Kuriyama, Y.; Haniu, M.; Shively, J.E.; Gotoh, O.; !1Kusunose, E.; Kusunose, M. !$#journal J. Biol. Chem. (1987) 262:13366-13371 !$#title cDNA cloning and inducible expression during pregnancy of !1the mRNA for rabbit pulmonary prostaglandin !1omega-hydroxylase (cytochrome P-450-p-2). !$#cross-references MUID:88007548; PMID:3654614 !$#accession A29368 !'##molecule_type mRNA !'##residues 5-475,'V',477-486,'I',488-510 ##label MAT !'##note portions of this protein, including residues 5-29, were !1determined by protein sequencing REFERENCE JN0089 !$#authors Yoshimura, R.; Kusunose, E.; Yokotani, N.; Yamamoto, S.; !1Kubota, I.; Kusunose, M. !$#journal J. Biochem. (1990) 108:544-548 !$#title Purification and characterization of two forms of fatty acid !1omega-hydroxylase cytochrome P-450 from rabbit kidney cortex !1microsomes. !$#cross-references MUID:91154157; PMID:2127276 !$#accession JN0089 !'##molecule_type protein !'##residues 5-24 ##label YOS !'##experimental_source kidney COMMENT This protein catalyzes the omega- and !1(omega-1)-hydroxylation of fatty acids. GENETICS !$#gene CYP4A4 !$#introns 65/3; 113/1; 128/1; 170/3; 212/2; 264/1; 299/3; 363/2; 408/ !11; 429/3; 455/2 CLASSIFICATION #superfamily human cytochrome P450 CYP4B1; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; monooxygenase; oxidoreductase; transmembrane !1protein FEATURE !$318-479 #domain cytochrome P450 homology #label CYP\ !$457 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 510 #molecular-weight 58930 #checksum 8195 SEQUENCE /// ENTRY B34160 #type complete TITLE cytochrome P450 4A7 - rabbit ALTERNATE_NAMES cytochrome P450ka-2; cytochrome P450kc CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Mar-2000 ACCESSIONS B34160; C34260; JN0090 REFERENCE A34160 !$#authors Yokotani, N.; Bernhardt, R.; Sogawa, K.; Kusunose, E.; !1Gotoh, O.; Kusunose, M.; Fujii-Kuriyama, Y. !$#journal J. Biol. Chem. (1989) 264:21665-21669 !$#title Two forms of omega-hydroxylase toward prostaglandin A and !1laurate. cDNA cloning and their expression. !$#cross-references MUID:90094341; PMID:2600085 !$#accession B34160 !'##molecule_type mRNA !'##residues 1-511 ##label YOK !'##cross-references GB:M29530; NID:g164984; PIDN:AAA31233.1; !1PID:g164985; GB:J05150 REFERENCE A34260 !$#authors Johnson, E.F.; Walker, D.L.; Griffin, K.J.; Clark, J.E.; !1Okita, R.T.; Muerhoff, A.S.; Masters, B.S. !$#journal Biochemistry (1990) 29:873-879 !$#title Cloning and expression of three rabbit kidney cDNAs encoding !1lauric acid omega-hydroxylases. !$#cross-references MUID:90254128; PMID:2340280 !$#accession C34260 !'##molecule_type mRNA !'##residues 1-98,'C',100-149,'F',151-391,'SK',394-476,'V',478-511 !1##label JOH !'##cross-references GB:M28657; NID:g164978; PIDN:AAA31231.1; !1PID:g164979 REFERENCE JN0089 !$#authors Yoshimura, R.; Kusunose, E.; Yokotani, N.; Yamamoto, S.; !1Kubota, I.; Kusunose, M. !$#journal J. Biochem. (1990) 108:544-548 !$#title Purification and characterization of two forms of fatty acid !1omega-hydroxylase cytochrome P-450 from rabbit kidney cortex !1microsomes. !$#cross-references MUID:91154157; PMID:2127276 !$#accession JN0090 !'##molecule_type protein !'##residues 5-7,'X',9-15,'X',17-22,'X',24 ##label YOS !'##experimental_source kidney COMMENT This protein catalyzes the omega- and !1(omega-1)-hydroxylation of fatty acids. CLASSIFICATION #superfamily human cytochrome P450 CYP4B1; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; monooxygenase; oxidoreductase; transmembrane !1protein FEATURE !$319-480 #domain cytochrome P450 homology #label CYP\ !$458 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 511 #molecular-weight 58337 #checksum 4545 SEQUENCE /// ENTRY A34160 #type complete TITLE laurate omega-hydroxylase (EC 1.14.15.3) cytochrome P450 4A6 - rabbit ALTERNATE_NAMES cytochrome P450ka-1; cytochrome P450LPGA omega 1 ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Mar-2000 ACCESSIONS A34160; B34260; PQ0047; S23949 REFERENCE A34160 !$#authors Yokotani, N.; Bernhardt, R.; Sogawa, K.; Kusunose, E.; !1Gotoh, O.; Kusunose, M.; Fujii-Kuriyama, Y. !$#journal J. Biol. Chem. (1989) 264:21665-21669 !$#title Two forms of omega-hydroxylase toward prostaglandin A and !1laurate. cDNA cloning and their expression. !$#cross-references MUID:90094341; PMID:2600085 !$#accession A34160 !'##molecule_type mRNA !'##residues 1-510 ##label YOK !'##cross-references GB:M29531; NID:g164986; PIDN:AAA31234.1; !1PID:g164987; GB:J05150 REFERENCE A34260 !$#authors Johnson, E.F.; Walker, D.L.; Griffin, K.J.; Clark, J.E.; !1Okita, R.T.; Muerhoff, A.S.; Masters, B.S. !$#journal Biochemistry (1990) 29:873-879 !$#title Cloning and expression of three rabbit kidney cDNAs encoding !1lauric acid omega-hydroxylases. !$#cross-references MUID:90254128; PMID:2340280 !$#accession B34260 !'##molecule_type mRNA !'##residues 1-423,'VW',426-434,'R',436-475,'V',477-510 ##label JOH !'##cross-references GB:M28656 REFERENCE PQ0047 !$#authors Kikuta, Y.; Kusunose, E.; Okumoto, T.; Kubota, I.; Kusunose, !1M. !$#journal J. Biochem. (1990) 107:280-286 !$#title Purification and characterization of two forms of cytochrome !1P-450 with omega-hydroxylase activities toward prostaglandin !1A and fatty acids from rabbit liver microsomes. !$#cross-references MUID:90299866; PMID:2361958 !$#accession PQ0047 !'##molecule_type protein !'##residues 5-24 ##label KIK !'##experimental_source liver !'##note amino-terminal sequence REFERENCE S23949 !$#authors Muerhoff, A.S.; Griffin, K.J.; Johnson, E.F. !$#journal Arch. Biochem. Biophys. (1992) 296:66-72 !$#title Characterization of a rabbit gene encoding a !1clofibrate-inducible fatty acid omega-hydroxylase: CYP4A6. !$#cross-references MUID:92296782; PMID:1605646 !$#accession S23949 !'##molecule_type DNA !'##residues 1-26,'C',28-379,'M',381-423,'VW',426-434,'R',436-475,'V', !1477-510 ##label MUE COMMENT This enzyme catalyzes the omega-hydroxylation of !1prostaglandin A1 and A2, as well as the omega- and !1(omega-1)-hydroxylation of fatty acid. GENETICS !$#gene CYP4A6 CLASSIFICATION #superfamily human cytochrome P450 CYP4B1; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; monooxygenase; oxidoreductase; transmembrane !1protein FEATURE !$318-479 #domain cytochrome P450 homology #label CYP\ !$457 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 510 #molecular-weight 58129 #checksum 6263 SEQUENCE /// ENTRY A34260 #type complete TITLE laurate omega-hydroxylase (EC 1.14.15.3) cytochrome P450 4A5 - rabbit ALTERNATE_NAMES cytochrome P450kd ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Mar-2000 ACCESSIONS A34260; S14761 REFERENCE A34260 !$#authors Johnson, E.F.; Walker, D.L.; Griffin, K.J.; Clark, J.E.; !1Okita, R.T.; Muerhoff, A.S.; Masters, B.S. !$#journal Biochemistry (1990) 29:873-879 !$#title Cloning and expression of three rabbit kidney cDNAs encoding !1lauric acid omega-hydroxylases. !$#cross-references MUID:90254128; PMID:2340280 !$#accession A34260 !'##molecule_type mRNA !'##residues 1-511 ##label JOH !'##cross-references GB:M28655 REFERENCE S14761 !$#authors Yokotani, N.; Kusunose, E.; Sogawa, K.; Kawashima, H.; !1Kinosaki, M.; Kusunose, M.; Fujii-Kuriyama, Y. !$#journal Eur. J. Biochem. (1991) 196:531-536 !$#title cDNA cloning and expression of the mRNA for cytochrome P-450 !1(kd) which shows a fatty acid omega-hydroxylating activity. !$#cross-references MUID:91192021; PMID:2013275 !$#accession S14761 !'##molecule_type mRNA !'##residues 1-476,'L',478-511 ##label YOK !'##cross-references EMBL:X57209; NID:g1655; PIDN:CAA40493.1; PID:g1656 GENETICS !$#gene CYP4A5 CLASSIFICATION #superfamily human cytochrome P450 CYP4B1; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; microsome; monooxygenase; oxidoreductase; !1transmembrane protein FEATURE !$319-480 #domain cytochrome P450 homology #label CYP\ !$458 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 511 #molecular-weight 58387 #checksum 4245 SEQUENCE /// ENTRY A36304 #type complete TITLE cytochrome P450 4A8 - rat ALTERNATE_NAMES cytochrome P450 KP1; cytochrome P450K-4 CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Mar-2000 ACCESSIONS A36304; S08300 REFERENCE A36304 !$#authors Stroemstedt, M.; Hayashi, S.I.; Zaphiropoulos, P.G.; !1Gustafsson, J.A. !$#journal DNA Cell Biol. (1990) 9:569-577 !$#title Cloning and characterization of a novel member of the !1cytochrome P450 subfamily IVA in rat prostate. !$#cross-references MUID:91103877; PMID:1980193 !$#accession A36304 !'##molecule_type mRNA !'##residues 1-508 ##label STR !'##cross-references GB:M37828; NID:g203756; PIDN:AAA63485.1; !1PID:g203757 !'##experimental_source kidney, prostate REFERENCE S08282 !$#authors Imaoka, S.; Nagashima, K.; Funae, Y. !$#journal Arch. Biochem. Biophys. (1990) 276:473-480 !$#title Characterization of three cytochrome P450s purified from !1renal microsomes of untreated male rats and comparison with !1human renal cytochrome P450. !$#cross-references MUID:90165442; PMID:2306108 !$#accession S08300 !'##molecule_type protein !'##residues 8-12,'X',14-22 ##label IMA GENETICS !$#gene CYP4A8 CLASSIFICATION #superfamily human cytochrome P450 CYP4B1; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; monooxygenase; oxidoreductase; transmembrane !1protein FEATURE !$316-477 #domain cytochrome P450 homology #label CYP\ !$455 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 508 #molecular-weight 58518 #checksum 1521 SEQUENCE /// ENTRY JE0361 #type complete TITLE cytochromes P450, CYP4T2 - European sea bass CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Dicentrarchus labrax #common_name European sea bass DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 19-May-2000 ACCESSIONS JE0361 REFERENCE JE0361 !$#authors Sabourault, C.; Berge, J.B.; Lafaurie, M.; Girard, J.P.; !1Amichot, M. !$#journal Biochem. Biophys. Res. Commun. (1998) 251:213-219 !$#title Molecular cloning of a phthalate-inducible CYP4 gene !1(CYP4T2) in kidney from the sea bass, Dicentrarchus labrax. !$#cross-references MUID:99009248; PMID:9790933 !$#accession JE0361 !'##molecule_type mRNA !'##residues 1-515 ##label SAB !'##cross-references GB:AF045468; NID:g4091077; PIDN:AAC98961.1; !1PID:g4091078 CLASSIFICATION #superfamily human cytochrome P450 CYP4B1; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; oxidoreductase FEATURE !$318-481 #domain cytochrome P450 homology #label CYP\ !$459 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 515 #molecular-weight 59750 #checksum 8977 SEQUENCE /// ENTRY O4RTLO #type complete TITLE laurate omega-hydroxylase (EC 1.14.15.3) cytochrome P450 4A1 - rat ALTERNATE_NAMES cytochrome P450 LA-omega; cytochrome P452 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Mar-2000 ACCESSIONS S01336; A26137; B32965; S21711 REFERENCE S01336 !$#authors Earnshaw, D.; Dale, J.W.; Goldfarb, P.S.; Gibson, G.G. !$#journal FEBS Lett. (1988) 236:357-361 !$#title Differential splicing in the 3'non-coding region of rat !1cytochrome P-452 (P450 IV A1) mRNA. !$#cross-references MUID:88312998; PMID:3410047 !$#accession S01336 !'##molecule_type mRNA !'##residues 1-509 ##label EAR !'##cross-references EMBL:X07259; NID:g56046; PIDN:CAA30245.1; !1PID:g56047 REFERENCE A26137 !$#authors Hardwick, J.P.; Song, B.J.; Huberman, E.; Gonzalez, F.J. !$#journal J. Biol. Chem. (1987) 262:801-810 !$#title Isolation, complementary DNA sequence, and regulation of rat !1hepatic lauric acid omega-hydroxylase (cytochrome !1P-450-LA-omega). Identification of a new cytochrome P-450 !1gene family. !$#cross-references MUID:87109183; PMID:3027069 !$#accession A26137 !'##molecule_type mRNA !'##residues 1-509 ##label HAR !'##cross-references GB:M14972; NID:g203865; PIDN:AAA41061.1; !1PID:g203866 REFERENCE A32965 !$#authors Kimura, S.; Hanioka, N.; Matsunaga, E.; Gonzalez, F.J. !$#journal DNA (1989) 8:503-516 !$#title The rat clofibrate-inducible CYP4A gene subfamily I. !1Complete intron and exon sequence of the CYP4A1 and CYP4A2 !1genes, unique exon organization, and identification of a !1conserved 19-bp upstream element. !$#cross-references MUID:89356271; PMID:2766932 !$#accession B32965 !'##molecule_type DNA !'##residues 1-340,'E',342-509 ##label KIM !'##cross-references EMBL:M57718; NID:g203786; PIDN:AAA41038.1; !1PID:g203787 REFERENCE S21711 !$#authors Okita, R.T.; Okita, J.R. !$#journal Arch. Biochem. Biophys. (1992) 294:475-481 !$#title Characterization of a cytochrome P450 from Di(2-ethylhexyl) !1phthalate-treated rats which hydroxylates fatty acids. !$#cross-references MUID:92231570; PMID:1567203 !$#accession S21711 !'##status preliminary !'##molecule_type protein !'##residues 1-22 ##label OKI !'##experimental_source strain Sprague-Dawley !'##note this sequence was confirmed by protein sequencing GENETICS !$#gene CYP4A1 !$#introns 63/3; 112/1; 127/1; 169/3; 211/2; 263/1; 298/3; 362/2; 407/ !11; 428/3; 454/2 CLASSIFICATION #superfamily human cytochrome P450 CYP4B1; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; endoplasmic reticulum; !1fatty acid oxidation; heme; iron; metalloprotein; microsome; !1monooxygenase; oxidoreductase; transmembrane protein FEATURE !$317-478 #domain cytochrome P450 homology #label P45\ !$456 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 509 #molecular-weight 58214 #checksum 2428 SEQUENCE /// ENTRY A32966 #type complete TITLE cytochrome P450 4A3 - rat ALTERNATE_NAMES cytochrome P450DM-2, streptozotocin-inducible, hepatic CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Mar-2000 ACCESSIONS A32966; A27700 REFERENCE A32966 !$#authors Kimura, S.; Hardwick, J.P.; Kozak, C.A.; Gonzalez, F.J. !$#journal DNA (1989) 8:517-525 !$#title The rat clofibrate-inducible CYP4A subfamily II. cDNA !1sequence of IVA3, mapping of the Cyp4a locus to mouse !1chromosome 4, and coordinate and tissue-specific regulation !1of the CYP4A genes. !$#cross-references MUID:89356272; PMID:2766933 !$#accession A32966 !'##molecule_type mRNA !'##residues 1-507 ##label KIM !'##cross-references GB:M33936; NID:g204989; PIDN:AAA41458.1; !1PID:g204990 !'##experimental_source clofibrate-treated rat liver !'##note the authors translated the codon ACC for residue 215 as Tyr REFERENCE A27700 !$#authors Imaoka, S.; Shimojo, N.; Funae, Y. !$#journal Biochem. Biophys. Res. Commun. (1988) 152:680-687 !$#title Induction of renal cytochrome P-450 in hepatic microsomes of !1diabetic rats. !$#cross-references MUID:88209045; PMID:3365247 !$#accession A27700 !'##molecule_type protein !'##residues 5-15,'X',17-19 ##label IMA !'##note amino-terminal sequence GENETICS !$#gene CYP4A3 CLASSIFICATION #superfamily human cytochrome P450 CYP4B1; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; liver; !1metalloprotein; monooxygenase; oxidoreductase; transmembrane !1protein FEATURE !$315-476 #domain cytochrome P450 homology #label CYP\ !$454 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 507 #molecular-weight 58232 #checksum 6319 SEQUENCE /// ENTRY A32965 #type complete TITLE cytochrome P450 4A2 - rat CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Mar-2000 ACCESSIONS A32965 REFERENCE A32965 !$#authors Kimura, S.; Hanioka, N.; Matsunaga, E.; Gonzalez, F.J. !$#journal DNA (1989) 8:503-516 !$#title The rat clofibrate-inducible CYP4A gene subfamily I. !1Complete intron and exon sequence of the CYP4A1 and CYP4A2 !1genes, unique exon organization, and identification of a !1conserved 19-bp upstream element. !$#cross-references MUID:89356271; PMID:2766932 !$#accession A32965 !'##molecule_type DNA !'##residues 1-504 ##label KIM !'##cross-references EMBL:M57719; NID:g203788; PIDN:AAA41039.1; !1PID:g203789 GENETICS !$#gene CYP4A2 !$#introns 65/3; 110/1; 122/1; 164/3; 206/2; 258/1; 293/3; 357/2; 402/ !11; 423/3; 449/2 CLASSIFICATION #superfamily human cytochrome P450 CYP4B1; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; endoplasmic reticulum; !1fatty acid oxidation; heme; iron; metalloprotein; !1monooxygenase; oxidoreductase; transmembrane protein FEATURE !$312-473 #domain cytochrome P450 homology #label CYP\ !$451 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 504 #molecular-weight 57968 #checksum 6368 SEQUENCE /// ENTRY A46661 #type complete TITLE leukotriene B4 omega-hydroxylase (EC 1.14.15.-) cytochrome P450 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A46661 REFERENCE A46661 !$#authors Kikuta, Y.; Kusunose, E.; Endo, K.; Yamamoto, S.; Sogawa, !1K.; Fujii-Kuriyama, Y.; Kusunose, M. !$#journal J. Biol. Chem. (1993) 268:9376-9380 !$#title A novel form of cytochrome P-450 family 4 in human !1polymorphonuclear leukocytes. cDNA cloning and expression of !1leukotriene B4 omega-hydroxylase. !$#cross-references MUID:93252801; PMID:8486631 !$#accession A46661 !'##status preliminary !'##molecule_type DNA; mRNA !'##residues 1-520 ##label KIK !'##cross-references GB:AB002454; NID:g3123722; PIDN:BAA25990.1; !1PID:g3123723; GB:AB002461; NID:g3126633; PIDN:BAA25991.1; !1PID:g3126635; GB:D12620; NID:g391715; PIDN:BAA02144.1; !1PID:g391716 !'##experimental_source polymorphonuclear leukocytes !'##note sequence extracted from NCBI backbone (NCBIN:131350, !1NCBIP:131351) GENETICS !$#gene GDB:LTB4H; CYP4F3 !'##cross-references GDB:139142; OMIM:601270 CLASSIFICATION #superfamily human cytochrome P450 CYP4B1; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; fatty acid oxidation; !1heme; iron; metalloprotein; monooxygenase; oxidoreductase FEATURE !$325-490 #domain cytochrome P450 homology #label P45\ !$468 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 520 #molecular-weight 59805 #checksum 5839 SEQUENCE /// ENTRY A39381 #type complete TITLE cytochrome P450 4 - cockroach (Blaberus discoidalis) CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Blaberus discoidalis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A39381 REFERENCE A39381 !$#authors Bradfield, J.Y.; Lee, Y.H.; Keeley, L.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:4558-4562 !$#title Cytochrome P450 family 4 in a cockroach: molecular cloning !1and regulation by hypertrehalosemic hormone. !$#cross-references MUID:91239607; PMID:2034694 !$#accession A39381 !'##status preliminary !'##molecule_type DNA !'##residues 1-511 ##label BRA !'##cross-references GB:M63798; NID:g155946; PIDN:AAA27819.1; !1PID:g155947 !'##note the authors translated the codon CAG for residue 23 as Ser, and !1TTT for residue 170 as Glu GENETICS !$#gene CYP4C1 CLASSIFICATION #superfamily human cytochrome P450 CYP4B1; cytochrome P450 !1homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxidoreductase FEATURE !$311-474 #domain cytochrome P450 homology #label P45\ !$452 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 511 #molecular-weight 58754 #checksum 6677 SEQUENCE /// ENTRY S66374 #type complete TITLE cytochrome P450 4M2 - tobacco hornworm CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Manduca sexta #common_name tobacco hornworm DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S66374; S66477 REFERENCE S66374 !$#authors Snyder, M.J.; Stevens, J.L.; Andersen, J.F.; Feyereisen, R. !$#journal Arch. Biochem. Biophys. (1995) 321:13-20 !$#title Expression of cytochrome P450 genes of the CYP4 family in !1midgut and fat body of the tobacco hornworm, Manduca sexta. !$#cross-references MUID:95366751; PMID:7639512 !$#accession S66374 !'##molecule_type mRNA !'##residues 1-503 ##label SNY !'##cross-references GB:L38671; NID:g3207185; PIDN:AAC21661.1; !1PID:g3207186 !$#accession S66477 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 313-444 ##label SNW !'##cross-references EMBL:L38671; NID:g606409; PID:g606410 !'##experimental_source fat body and midgut GENETICS !$#gene CYP4M2 CLASSIFICATION #superfamily human cytochrome P450 CYP4B1; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; monooxygenase; oxidoreductase; transmembrane !1protein FEATURE !$305-468 #domain cytochrome P450 homology #label P45\ !$446 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 503 #molecular-weight 58501 #checksum 4371 SEQUENCE /// ENTRY S25707 #type complete TITLE cytochrome P450 4D1 - fruit fly (Drosophila melanogaster) CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S25707 REFERENCE S25707 !$#authors Gandhi, R.; Varak, E.; Goldberg, M.L. !$#journal DNA Cell Biol. (1992) 11:397-404 !$#title Molecular analysis of a cytochrome P450 gene of family 4 on !1the Drosophila X chromosome. !$#cross-references MUID:92297166; PMID:1605861 !$#accession S25707 !'##status preliminary !'##molecule_type mRNA !'##residues 1-511 ##label GAN !'##cross-references EMBL:X67645; NID:g7790; PIDN:CAA47887.1; PID:g7791 GENETICS !$#gene Cyp4d1 !'##cross-references FlyBase:FBgn0005670 CLASSIFICATION #superfamily human cytochrome P450 CYP4B1; cytochrome P450 !1homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxidoreductase FEATURE !$313-478 #domain cytochrome P450 homology #label P45\ !$456 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 511 #molecular-weight 58384 #checksum 6514 SEQUENCE /// ENTRY S41192 #type complete TITLE cytochrome P450 4D2 - fruit fly (Drosophila melanogaster) CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S41192; S34291 REFERENCE S41192 !$#authors Frolov, M.V.; Alatortsev, V.E. !$#submission submitted to the EMBL Data Library, December 1993 !$#description A cluster of cytochrome P450 genes in the X-chromosome of !1Drosophila melanogaster. !$#accession S41192 !'##molecule_type DNA !'##residues 1-496 ##label FRO !'##cross-references EMBL:X75955; NID:g439650; PIDN:CAA53568.1; !1PID:g439651 !'##experimental_source strain Oregon R REFERENCE S34291 !$#authors Frolov, M.V.; Alatortsev, V.E. !$#submission submitted to the EMBL Data Library, June 1993 !$#description Cluster of cytochrome P-450 genes on the X-chromosome in !1Drosophila melanogaster. !$#accession S34291 !'##molecule_type DNA !'##residues 'A',31-496 ##label FRW !'##cross-references EMBL:Z23005; NID:g312903; PIDN:CAA80549.1; !1PID:g312904 !'##experimental_source strain Oregon R GENETICS !$#gene Cyp4d2 !'##cross-references FlyBase:FBgn0011576 !$#map_position X !$#introns 53/1; 182/1; 205/2; 392/1 CLASSIFICATION #superfamily human cytochrome P450 CYP4B1; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; oxidoreductase FEATURE !$308-471 #domain cytochrome P450 homology #label P45\ !$449 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 496 #molecular-weight 57461 #checksum 539 SEQUENCE /// ENTRY JC5236 #type complete TITLE cytochrome P450, Cyp4e2 - fruit fly (Drosophila melanogaster) CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS JC5236 REFERENCE JC5236 !$#authors Pittendrigh, B.R.; Mocelin, G.; Andreev, O.; !1ffrench-Constant, R.H. !$#journal Gene (1996) 179:295-296 !$#title The sequence of a Drosophila Cyp4e2 cytochrome P450-encoding !1cDNA. !$#cross-references MUID:97128322; PMID:8972915 !$#accession JC5236 !'##status preliminary !'##molecule_type mRNA !'##residues 1-485 ##label PIT !'##cross-references GB:U56957; NID:g1480636; PIDN:AAC47424.1; !1PID:g1480637 !'##experimental_source embryo COMMENT This protein lacks the hydrophobic amino-terminus, typical !1of microsomal cytochrome P450, and contains a small !1insertion at the carboxyl-terminus. CLASSIFICATION #superfamily human cytochrome P450 CYP4B1; cytochrome P450 !1homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxidoreductase FEATURE !$263-425 #domain cytochrome P450 homology #label P45\ !$403 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 485 #molecular-weight 55802 #checksum 4211 SEQUENCE /// ENTRY A34101 #type complete TITLE cytochrome P450 3A5 - human ALTERNATE_NAMES cytochrome P450 HLp2 CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A34101; S06491; I52302 REFERENCE A34101 !$#authors Aoyama, T.; Yamano, S.; Waxman, D.J.; Lapenson, D.P.; Meyer, !1U.A.; Fischer, V.; Tyndale, R.; Inaba, T.; Kalow, W.; !1Gelboin, H.V.; Gonzalez, F.J. !$#journal J. Biol. Chem. (1989) 264:10388-10395 !$#title Cytochrome P-450 hPCN3, a novel cytochrome P-450 IIIA gene !1product that is differentially expressed in adult human !1liver. cDNA and deduced amino acid sequence and distinct !1specificities of cDNA-expressed hPCN1 and hPCN3 for the !1metabolism of steroid hormones and cyclosporine. !$#cross-references MUID:89278095; PMID:2732228 !$#accession A34101 !'##molecule_type mRNA !'##residues 1-502 ##label AOY !'##cross-references GB:J04813; NID:g181345; PIDN:AAA02993.1; !1PID:g181346 REFERENCE S06491 !$#authors Schuetz, J.D.; Molowa, D.T.; Guzelian, P.S. !$#journal Arch. Biochem. Biophys. (1989) 274:355-365 !$#title Characterization of a cDNA encoding a new member of the !1glucocorticoid-responsive cytochromes P450 in human liver. !$#cross-references MUID:90025114; PMID:2802615 !$#accession S06491 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-304,'P',306-317,'F',319-323,'D',325-376,'G',378-502 !1##label SCH REFERENCE I52302 !$#authors Jounaidi, Y.; Guzelian, P.S.; Maurel, P.; Vilarem, M.J. !$#journal Biochem. Biophys. Res. Commun. (1994) 205:1741-1747 !$#title Sequence of the 5'-flanking region of CYP3A5: comparative !1analysis with CYP3A4 and CYP3A7. !$#cross-references MUID:95110318; PMID:7811260 !$#accession I52302 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-24 ##label RES !'##cross-references GB:S74699; NID:g786472; PIDN:AAD14157.1; !1PID:g4261857 GENETICS !$#gene GDB:CYP3A5 !'##cross-references GDB:118783 !$#map_position 7q22.1-7q22.1 CLASSIFICATION #superfamily human cytochrome P450 CYP3A5; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; monooxygenase; oxidoreductase; transmembrane !1protein FEATURE !$302-463 #domain cytochrome P450 homology #label P45\ !$441 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 502 #molecular-weight 57108 #checksum 8293 SEQUENCE /// ENTRY S48161 #type complete TITLE thromboxane-A synthase (EC 5.3.99.5) - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S48161 REFERENCE S48161 !$#authors Miyata, A.; Yokoyama, C.; Ihara, H.; Bandoh, S.; Takeda, O.; !1Takahashi, E.; Tanabe, T. !$#journal Eur. J. Biochem. (1994) 224:273-279 !$#title Characterization of the human gene (TBXAS1) encoding !1thromboxane synthase. !$#cross-references MUID:95010003; PMID:7925341 !$#accession S48161 !'##status preliminary !'##molecule_type mRNA !'##residues 1-533 ##label MIY !'##cross-references GB:D34625; NID:g559364 GENETICS !$#gene GDB:TBXAS1; CYP5 !'##cross-references GDB:128744; OMIM:274180 !$#map_position 7q34-7q35 CLASSIFICATION #superfamily human cytochrome P450 CYP3A5; cytochrome P450 !1homology KEYWORDS chromoprotein; heme; intramolecular oxidoreductase; iron; !1isomerase; metalloprotein FEATURE !$338-501 #domain cytochrome P450 homology #label P45\ !$479 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 533 #molecular-weight 60470 #checksum 3059 SEQUENCE /// ENTRY A32157 #type complete TITLE cytochrome P450 6 - house fly CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Musca domestica #common_name house fly DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A32157 REFERENCE A32157 !$#authors Feyereisen, R.; Koener, J.F.; Farnsworth, D.E.; Nebert, D.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:1465-1469 !$#title Isolation and sequence of cDNA encoding a cytochrome P-450 !1from an insecticide-resistant strain of the house fly, Musca !1domestica. !$#cross-references MUID:89160799; PMID:2922393 !$#accession A32157 !'##molecule_type mRNA !'##residues 1-509 ##label FEY !'##cross-references GB:M25367 GENETICS !$#gene CYP6A1 CLASSIFICATION #superfamily human cytochrome P450 CYP3A5; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; monooxygenase; oxidoreductase FEATURE !$302-471 #domain cytochrome P450 homology #label P45\ !$449 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 509 #molecular-weight 58730 #checksum 2355 SEQUENCE /// ENTRY A47198 #type complete TITLE cytochrome P450 6A2 - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES cytochrome P450-B1 CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A45378; A47198 REFERENCE A45378 !$#authors Waters, L.C.; Zelhof, A.C.; Shaw, B.J.; Ch'ang, L.Y. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:4855-4859 !$#title Possible involvement of the long terminal repeat of !1transposable element 17.6 in regulating expression of an !1insecticide resistance-associated P450 gene in Drosophila. !$#cross-references MUID:92279225; PMID:1317576 !$#accession A45378 !'##molecule_type DNA; mRNA !'##residues 1-82,'FFMRLVNDTIALRERENFKRNDFMNI',83-90,'HQ',93-246,273-507 !1##label WA2 !'##cross-references GB:M88009; NID:g157165 !'##experimental_source strain 91-C, insecticide susceptible strain !'##note sequence inconsistent with the nucleotide translation !'##note sequence extracted from NCBI backbone (NCBIN:104184, !1NCBIP:104179) !'##note this sequence has been corrected in A47198 REFERENCE A47198 !$#authors Waters, L.C.; Zelhof, A.C.; Shaw, B.J.; Ch'ang, L.Y. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:12209 !$#title "Possible involvement of the long terminal repeat of !1transposable element 17.6 in regulating expression of an !1insecticide resistance-associated P450 gene in Drosophila." !$#cross-references MUID:93101696; PMID:1465460 !$#accession A47198 !'##molecule_type DNA; mRNA !'##residues 1-507 ##label WAT !'##cross-references GB:S51248; NID:g261816; PIDN:AAB24525.1; !1PID:g261817 !'##note sequence extracted from NCBI backbone (NCBIN:120806, !1NCBIP:120807) GENETICS !$#gene Cyp6a2 !'##cross-references FlyBase:FBgn0000473 !$#introns #status absent CLASSIFICATION #superfamily human cytochrome P450 CYP3A5; cytochrome P450 !1homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxidoreductase; !1transmembrane protein FEATURE !$308-474 #domain cytochrome P450 homology #label P45\ !$452 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 507 #molecular-weight 58850 #checksum 1184 SEQUENCE /// ENTRY S48058 #type complete TITLE cytochrome P450 CYP6B1 - black swallowtail CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Papilio polyxenes #common_name black swallowtail DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S48058; A46367 REFERENCE S48058 !$#authors Prapaipong, H.; Berenbaum, M.R.; Schuler, M.A. !$#journal Nucleic Acids Res. (1994) 22:3210-3217 !$#title Transcriptional regulation of the Papilio polyxenes CYP6B1 !1gene. !$#cross-references MUID:94344788; PMID:8065937 !$#accession S48058 !'##status preliminary !'##molecule_type DNA !'##residues 1-498 ##label PRA !'##cross-references EMBL:Z29624; NID:g520879; PIDN:CAA82732.1; !1PID:g520880 REFERENCE A46367 !$#authors Cohen, M.B.; Schuler, M.A.; Berenbaum, M.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:10920-10924 !$#title A host-inducible cytochrome P-450 from a host-specific !1caterpillar: molecular cloning and evolution. !$#cross-references MUID:93066355; PMID:1279697 !$#accession A46367 !'##status preliminary !'##molecule_type mRNA; protein !'##residues 1-23,'N',25-154,'NS',157-498 ##label COH !'##cross-references GB:M80828; NID:g160763; PIDN:AAA29789.1; !1PID:g160764 !'##note sequence extracted from NCBI backbone (NCBIN:118719, !1NCBIP:118720) GENETICS !$#introns 445/1 CLASSIFICATION #superfamily human cytochrome P450 CYP3A5; cytochrome P450 !1homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxidoreductase FEATURE !$300-465 #domain cytochrome P450 homology #label P45\ !$443 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 498 #molecular-weight 57514 #checksum 8769 SEQUENCE /// ENTRY S57337 #type complete TITLE trichodiene oxygenase (EC 1.14.-.-) cytochrome P450 CYP58 - fungus (Fusarium sporotrichioides) ALTERNATE_NAMES TRI4 protein ORGANISM #formal_name Fusarium sporotrichioides DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S57337 REFERENCE S57337 !$#authors Hohn, T.M.; Desjardins, A.E.; McCormick, S.P. !$#journal Mol. Gen. Genet. (1995) 248:95-102 !$#title The Tri4 gene of Fusarium sporotrichioides encodes a !1cytochrome P450 monooxygenase involved in trichothecene !1biosynthesis. !$#cross-references MUID:95379755; PMID:7651333 !$#accession S57337 !'##status preliminary !'##molecule_type DNA !'##residues 1-520 ##label HOH !'##cross-references EMBL:U22462; NID:g837031; PIDN:AAB72032.1; !1PID:g837032 !'##note the authors did not translate the codon for residue 101 GENETICS !$#gene tri4 !$#introns 82/1; 403/3; 459/2 CLASSIFICATION #superfamily Fusarium trichodiene oxygenase 4; cytochrome !1P450 homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxidoreductase FEATURE !$311-477 #domain cytochrome P450 homology #label P45\ !$455 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 520 #molecular-weight 59073 #checksum 295 SEQUENCE /// ENTRY B36395 #type complete TITLE cytochrome P450 56 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YDR402c; spore wall maturation protein DIT2 CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS B36395; S14228; S69684; S13502 REFERENCE A36395 !$#authors Briza, P.; Breitenbach, M.; Ellinger, A.; Segall, J. !$#journal Genes Dev. (1990) 4:1775-1789 !$#title Isolation of two developmentally regulated genes involved in !1spore wall maturation in Saccharomyces cerevisiae. !$#cross-references MUID:91065523; PMID:2249774 !$#accession B36395 !'##molecule_type DNA !'##residues 1-489 ##label BRI !'##cross-references EMBL:X55713 REFERENCE S14228 !$#authors Segall, J. !$#submission submitted to the EMBL Data Library, October 1990 !$#accession S14228 !'##molecule_type DNA !'##residues 1-444,'I',446-489 ##label SEG !'##cross-references EMBL:X55713; NID:g3655; PIDN:CAA39246.1; PID:g3656 REFERENCE S69665 !$#authors Dietrich, F.S. !$#submission submitted to the EMBL Data Library, July 1995 !$#description The sequence of S. cerevisiae cosmids 9481, 9509, 9926, !19461, and lambda 3641. !$#accession S69684 !'##molecule_type DNA !'##residues 1-489 ##label DIE !'##cross-references EMBL:U32274; NID:g927313; PIDN:AAB64842.1; !1PID:g927333; GSPDB:GN00004; MIPS:YDR402c GENETICS !$#gene SGD:DIT2; DIT2; CYP56; MIPS:YDR402c !'##cross-references SGD:S0002810 !$#map_position 4R FUNCTION !$#description probably involved in dityrosine biosynthesis CLASSIFICATION #superfamily yeast cytochrome P450 CYP56; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; monooxygenase; oxidoreductase; transmembrane !1protein FEATURE !$8-24 #domain transmembrane #status predicted #label TM1\ !$33-49 #domain transmembrane #status predicted #label TM2\ !$290-457 #domain cytochrome P450 homology #label P45\ !$435 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 489 #molecular-weight 56071 #checksum 3707 SEQUENCE /// ENTRY S45583 #type complete TITLE pisatin demethylase (EC 1.14.-.-) cytochrome P450 CYP57 - fungus (Nectria haematococca) ALTERNATE_NAMES PDAT9 protein ORGANISM #formal_name Nectria haematococca DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS S45583 REFERENCE S45583 !$#authors Maloney, A.P.; VanEtten, H.D. !$#journal Mol. Gen. Genet. (1994) 243:506-514 !$#title A gene from the fungal plant pathogen Nectria haematococca !1that encodes the phytoalexin-detoxifying enzyme pisatin !1demethylase defines a new cytochrome P450 family. !$#cross-references MUID:94268495; PMID:8208242 !$#accession S45583 !'##molecule_type DNA !'##residues 1-515 ##label MAL !'##cross-references EMBL:L20976; NID:g309579; PIDN:AAC01762.1; !1PID:g487426 GENETICS !$#gene PDAT9 !$#introns 84/1; 200/3; 402/3; 445/3 CLASSIFICATION #superfamily pisatin demethylase; cytochrome P450 homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxidoreductase FEATURE !$312-475 #domain cytochrome P450 homology #label P45\ !$453 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 515 #molecular-weight 58186 #checksum 1032 SEQUENCE /// ENTRY S34286 #type complete TITLE pisatin demethylase PDA6-1 - fungus (Nectria haematococca) CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Nectria haematococca DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Mar-2000 ACCESSIONS S34286 REFERENCE S34286 !$#authors Reimmann, C.; van Etten, H.D. !$#submission submitted to the EMBL Data Library, June 1993 !$#description Cloning and characterization of PDA6-1 a fungal gene !1encoding a cytochrome P-450 which can detoxify the !1phytoalexin pisatin from garden pea. !$#accession S34286 !'##molecule_type DNA !'##residues 1-506 ##label REI !'##cross-references EMBL:X73145; NID:g312163; PIDN:CAA51665.1; !1PID:g312164 GENETICS !$#introns 84/1; 200/3; 402/3; 445/3 CLASSIFICATION #superfamily pisatin demethylase; cytochrome P450 homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; oxidoreductase FEATURE !$312-475 #domain cytochrome P450 homology #label CYP\ !$453 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 506 #molecular-weight 56876 #checksum 3863 SEQUENCE /// ENTRY S12015 #type complete TITLE benzoate 4-monooxygenase (EC 1.14.13.12) cytochrome P450 53 - Aspergillus niger ALTERNATE_NAMES benzoate-para-hydroxylase ORGANISM #formal_name Aspergillus niger DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Mar-2000 ACCESSIONS S12015; S10453 REFERENCE S12015 !$#authors van Gorcom, R.F.M.; Boschloo, J.G.; Kuijvenhoven, A.; Lange, !1J.; van Vark, A.J.; Bos, C.J.; van Balken, J.A.M.; Pouwels, !1P.H.; van den Hondel, C.A.M.J.J. !$#journal Mol. Gen. Genet. (1990) 223:192-197 !$#title Isolation and molecular characterisation of the !1benzoate-para-hydroxylase gene (bphA) of Aspergillus niger: !1a member of a new gene family of the cytochrome P450 !1superfamily. !$#cross-references MUID:91066829; PMID:2250647 !$#accession S12015 !'##molecule_type DNA !'##residues 1-517 ##label VAN !'##cross-references EMBL:X52521; NID:g2336; PIDN:CAA36753.1; !1PID:g295920 GENETICS !$#gene bphA !$#map_position 1 !$#introns 100/2 CLASSIFICATION #superfamily pisatin demethylase; cytochrome P450 homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; monooxygenase; oxidoreductase; transmembrane !1protein FEATURE !$1-21 #domain transmembrane #status predicted #label TMM\ !$315-483 #domain cytochrome P450 homology #label CYP\ !$461 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 517 #molecular-weight 58015 #checksum 5754 SEQUENCE /// ENTRY O4CKA3 #type complete TITLE cytochrome P450 52A3-a - yeast (Candida maltosa) ALTERNATE_NAMES cytochrome P450, alkane-inducible; cytochrome P450-cm1 CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Candida maltosa DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Nov-2000 ACCESSIONS B56578; JU0095; JQ1040; A33254; S65522; S50815; S08667 REFERENCE A56578 !$#authors Schunck, W.H.; Vogel, F.; Gross, B.; Kargel, E.; !1Mauersberger, S.; Kopke, K.; Gengnagel, C.; Muller, H.G. !$#journal Eur. J. Cell Biol. (1991) 55:336-345 !$#title Comparison of two cytochromes P-450 from Candida maltosa: !1primary structures, substrate specificities and effects of !1their expression in Saccharomyces cerevisiae on the !1proliferation of the endoplasmic reticulum. !$#cross-references MUID:92037671; PMID:1935996 !$#accession B56578 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-523 ##label SCH !'##cross-references EMBL:X51931; NID:g2607; PIDN:CAA36197.1; PID:g2608 !'##experimental_source strain EH15D !'##note submitted to the EMBL Data Library, February 1990 REFERENCE JU0095 !$#authors Takagi, M.; Ohkuma, M.; Kobayashi, N.; Watanabe, M.; Yano, !1K. !$#journal Agric. Biol. Chem. (1989) 53:2217-2226 !$#title Purification of cytochrome P-450alk from n-alkane-grown !1cells of Candida maltosa, and cloning and nucleotide !1sequencing of the encoding gene. !$#accession JU0095 !'##molecule_type mRNA !'##residues 1-20,'L',22-51,'E',53-146,'L',148-523 ##label TAK !'##cross-references DDBJ:D00481; NID:g218379; PIDN:BAA00371.1; !1PID:g218380 !'##experimental_source strain IAM12247 !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing REFERENCE JQ1039 !$#authors Ohkuma, M.; Hikiji, T.; Tanimoto, T.; Schunck, W.H.; !1Mueller, H.G.; Yano, K.; Takagi, M. !$#journal Agric. Biol. Chem. (1991) 55:1757-1764 !$#title Evidence that more than one gene encodes n-alkane-inducible !1cytochrome P-450s in Candida maltosa, found by two-step gene !1disruption. !$#cross-references MUID:92109967; PMID:1368716 !$#accession JQ1040 !'##molecule_type DNA !'##residues 1-20,'L',22-51,'E',53-146,'L',148-523 ##label OHK !'##cross-references DDBJ:D12475; NID:g218377 !'##experimental_source strain CHA1, gene a REFERENCE A33254 !$#authors Schunck, W.H.; Kaergel, E.; Gross, B.; Wiedmann, B.; !1Mauersberger, S.; Koepke, K.; Kiessling, U.; Strauss, M.; !1Gaestel, M.; Mueller, H.G. !$#journal Biochem. Biophys. Res. Commun. (1989) 161:843-850 !$#title Molecular cloning and characterization of the primary !1structure of the alkane hydroxylating cytochrome P-450 from !1the yeast Candida maltosa. !$#cross-references MUID:89286595; PMID:2735924 !$#accession A33254 !'##molecule_type mRNA !'##residues 1-216,'S',218-220,223-230,'VR',233-523 ##label SC2 !'##cross-references GB:M27081; NID:g553117; PIDN:AAA34320.1; !1PID:g553118 !'##experimental_source strain EH-15 REFERENCE S65522 !$#authors Scheller, U.; Zimmer, T.; Kaergel, E.; Schunck, W.H. !$#journal Arch. Biochem. Biophys. (1996) 328:245-254 !$#title Characterization of the n-alkane and fatty acid !1hydroxylating cytochrome P450 forms 52A3 and 52A4. !$#cross-references MUID:96213873; PMID:8645001 !$#accession S65522 !'##molecule_type protein !'##residues 2-21 ##label SC3 REFERENCE S50815 !$#authors Sugiyama, H.; Ohkuma, M.; Masuda, Y.; Park, S.M.; Ohta, A.; !1Takagi, M. !$#journal Yeast (1995) 11:43-52 !$#title In vivo evidence for non-universal usage of the codon CUG in !1Candida maltosa. !$#cross-references MUID:95282512; PMID:7762300 !$#accession S50815 !'##status preliminary !'##molecule_type protein !'##residues 2-8 ##label SUG COMMENT Cytochromes P450 are heme-containing monooxygenases that !1catalyze diverse oxidative reactions in the metabolism of a !1number of endogenous and xenobiotic compounds. GENETICS !$#gene CYP52A3-a CLASSIFICATION #superfamily Candida cytochrome P450 52A3; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; endoplasmic reticulum; !1heme; iron; metalloprotein; monooxygenase; oxidoreductase; !1transmembrane protein FEATURE !$2-523 #product cytochrome P450 52A3 #status predicted !8#label MAT\ !$18-35 #domain transmembrane #status predicted #label TMM\ !$317-493 #domain cytochrome P450 homology #label CYP\ !$471 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 523 #molecular-weight 59862 #checksum 6509 SEQUENCE /// ENTRY JQ1039 #type complete TITLE cytochrome P450 52A3-b - yeast (Candida maltosa) CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Candida maltosa DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Nov-2000 ACCESSIONS JQ1039 REFERENCE JQ1039 !$#authors Ohkuma, M.; Hikiji, T.; Tanimoto, T.; Schunck, W.H.; !1Mueller, H.G.; Yano, K.; Takagi, M. !$#journal Agric. Biol. Chem. (1991) 55:1757-1764 !$#title Evidence that more than one gene encodes n-alkane-inducible !1cytochrome P-450s in Candida maltosa, found by two-step gene !1disruption. !$#cross-references MUID:92109967; PMID:1368716 !$#accession JQ1039 !'##molecule_type DNA !'##residues 1-523 ##label OHK !'##cross-references GB:D12475; GB:D01168; NID:g218377; PIDN:BAA02041.1; !1PID:g218378; GB:S77461; NID:g242017; PIDN:AAC60531.1; !1PID:g242018 !'##experimental_source strain CHA1 GENETICS !$#gene CYP52A3-b CLASSIFICATION #superfamily Candida cytochrome P450 52A3; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; endoplasmic reticulum; !1heme; iron; metalloprotein; monooxygenase; oxidoreductase; !1transmembrane protein FEATURE !$317-493 #domain cytochrome P450 homology #label CYP\ !$471 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 523 #molecular-weight 59868 #checksum 7727 SEQUENCE /// ENTRY O4CKA4 #type complete TITLE cytochrome P450 52A4 - yeast (Candida maltosa) ALTERNATE_NAMES cytochrome P450-cm2 CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Candida maltosa DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Mar-2000 ACCESSIONS S08668; A56578; S65523 REFERENCE S08667 !$#authors Schunck, W.H.; Gross, B.; Mueller, H.G. !$#submission submitted to the EMBL Data Library, February 1990 !$#accession S08668 !'##molecule_type mRNA !'##residues 1-538 ##label SCH !'##cross-references EMBL:X51932; NID:g2609; PIDN:CAA36198.1; PID:g2610 !'##experimental_source strain EH15D REFERENCE A56578 !$#authors Schunck, W.H.; Vogel, F.; Gross, B.; Kargel, E.; !1Mauersberger, S.; Kopke, K.; Gengnagel, C.; Muller, H.G. !$#journal Eur. J. Cell Biol. (1991) 55:336-345 !$#title Comparison of two cytochromes P-450 from Candida maltosa: !1primary structures, substrate specificities and effects of !1their expression in Saccharomyces cerevisiae on the !1proliferation of the endoplasmic reticulum. !$#cross-references MUID:92037671; PMID:1935996 !$#accession A56578 !'##molecule_type mRNA !'##residues 1-255,'D',257-538 ##label SC2 !'##note sequence inconsistent with nucleotide translation !'##note sequence extracted from NCBI backbone (NCBIN:64322, !1NCBIP:64324) REFERENCE S65522 !$#authors Scheller, U.; Zimmer, T.; Kaergel, E.; Schunck, W.H. !$#journal Arch. Biochem. Biophys. (1996) 328:245-254 !$#title Characterization of the n-alkane and fatty acid !1hydroxylating cytochrome P450 forms 52A3 and 52A4. !$#cross-references MUID:96213873; PMID:8645001 !$#accession S65523 !'##molecule_type protein !'##residues 2-15 ##label SCW GENETICS !$#gene CYP52A4 CLASSIFICATION #superfamily Candida cytochrome P450 52A3; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; monooxygenase; oxidoreductase FEATURE !$2-538 #product cytochrome P450 52A4 #status experimental !8#label MAT\ !$331-507 #domain cytochrome P450 homology #label P45\ !$485 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 538 #molecular-weight 61843 #checksum 2348 SEQUENCE /// ENTRY B40576 #type complete TITLE cytochrome P450 ALK3-A - yeast (Candida maltosa) CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Candida maltosa DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Mar-2000 ACCESSIONS B40576 REFERENCE A40576 !$#authors Ohkuma, M.; Tanimoto, T.; Yano, K.; Takagi, M. !$#journal DNA Cell Biol. (1991) 10:271-282 !$#title CYP52 (cytochrome P450alk) multigene family in Candida !1maltosa: molecular cloning and nucleotide sequence of the !1two tandemly arranged genes. !$#cross-references MUID:91229697; PMID:2039569 !$#accession B40576 !'##molecule_type DNA !'##residues 1-538 ##label OHK CLASSIFICATION #superfamily Candida cytochrome P450 52A3; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; monooxygenase; oxidoreductase FEATURE !$331-507 #domain cytochrome P450 homology #label CYP\ !$485 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 538 #molecular-weight 61911 #checksum 1518 SEQUENCE /// ENTRY S22972 #type complete TITLE cytochrome P450 52A6 - yeast (Candida tropicalis) ALTERNATE_NAMES cytochrome P450alk3 CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Candida tropicalis DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Mar-2000 ACCESSIONS S22972 REFERENCE S22972 !$#authors Seghezzi, W.; Meili, C.; Ruffiner, R.; Kuenzi, R.; Sanglard, !1D.; Fiechter, A. !$#submission submitted to the EMBL Data Library, June 1992 !$#description Isolation and characterization of additional members of the !1cytochrome P450 gene family CYP52 of Candida tropicalis. !$#accession S22972 !'##molecule_type DNA !'##residues 1-524 ##label SEG !'##cross-references EMBL:Z13010; NID:g2659; PIDN:CAA78354.1; PID:g2660 GENETICS !$#gene CYP52A6 CLASSIFICATION #superfamily Candida cytochrome P450 52A3; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; oxidoreductase FEATURE !$318-494 #domain cytochrome P450 homology #label CYP\ !$472 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 524 #molecular-weight 59927 #checksum 1922 SEQUENCE /// ENTRY JS0203 #type complete TITLE cytochrome P450 52A1, alkane-inducible - yeast (Candida tropicalis) ALTERNATE_NAMES cytochrome P450alk 1 CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Candida tropicalis DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Mar-2000 ACCESSIONS JS0203; A29297 REFERENCE JS0203 !$#authors Sanglard, D.; Loper, J.C. !$#journal Gene (1989) 76:121-136 !$#title Characterization of the alkane-inducible cytochrome P450 !1(P450alk) gene from the yeast Candida tropicalis: !1identification of a new P450 gene family. !$#cross-references MUID:89306647; PMID:2663647 !$#accession JS0203 !'##molecule_type DNA !'##residues 1-543 ##label SAN !'##experimental_source ATCC 750 REFERENCE A29297 !$#authors Sanglard, D.; Chen, C.; Loper, J.C. !$#journal Biochem. Biophys. Res. Commun. (1987) 144:251-257 !$#title Isolation of the alkane inducible cytochrome. P450 (P450alk) !1gene from the yeast candida tropicalis. !$#cross-references MUID:87213173; PMID:3579905 !$#accession A29297 !'##molecule_type DNA !'##residues 438-543 ##label SA2 !'##cross-references GB:M15945; NID:g170846; PIDN:AAA34334.1; !1PID:g170847 !'##experimental_source ATCC 750 COMMENT Candida tropicalis contains an alkane-inducible !1monooxygenase consisting of this protein and NADPH !1cytochrome P450 oxidoreductase. This system catalyzes the !1terminal hydroxylation as the first step in the assimilation !1of alkanes and fatty acids. GENETICS !$#gene CYP52A1; P450alk CLASSIFICATION #superfamily Candida cytochrome P450 52A3; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; monooxygenase; oxidoreductase; transmembrane !1protein FEATURE !$29-48 #domain transmembrane #status predicted #label TM1\ !$59-80 #domain transmembrane #status predicted #label TM2\ !$333-509 #domain cytochrome P450 homology #label CYP\ !$487 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 543 #molecular-weight 62512 #checksum 7773 SEQUENCE /// ENTRY JT0980 #type complete TITLE cytochrome P450 52A2, alkane-inducible - yeast (Candida tropicalis) ALTERNATE_NAMES cytochrome P450-alk2 CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Candida tropicalis DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Mar-2000 ACCESSIONS JT0980; S06148 REFERENCE JT0980 !$#authors Seghezzi, W.; Sanglard, D.; Fiechter, A. !$#journal Gene (1991) 106:51-60 !$#title Characterization of a second alkane-inducible cytochrome !1P450-encoding gene, CYP52A2, from Candida tropicalis. !$#cross-references MUID:92039063; PMID:1937041 !$#accession JT0980 !'##molecule_type DNA !'##residues 1-522 ##label SEG !'##cross-references GB:M63258; NID:g170890; PIDN:AAA34353.1; !1PID:g170891 !'##note the gene encoding this protein is located 1Kb upstream from the !1gene encoding another alkane-inducible protein, alk1 !'##note the authors translated the codon AGA for residue 152 as Thr REFERENCE S06148 !$#authors Sanglard, D.; Fiechter, A. !$#journal FEBS Lett. (1989) 256:128-134 !$#title Heterogeneity within the alkane-inducible cytochrome P450 !1gene family of the yeast Candida tropicalis. !$#cross-references MUID:90033287; PMID:2806542 !$#accession S06148 !'##molecule_type DNA !'##residues 'IS',312-522 ##label SAN !'##cross-references EMBL:X17560; NID:g2671; PIDN:CAA35593.1; !1PID:g685237 GENETICS !$#gene CYP52A2 CLASSIFICATION #superfamily Candida cytochrome P450 52A3; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; monooxygenase; oxidoreductase; transmembrane !1protein FEATURE !$14-33 #domain transmembrane #status predicted #label MEM\ !$315-491 #domain cytochrome P450 homology #label CYP\ !$469 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 522 #molecular-weight 60150 #checksum 9739 SEQUENCE /// ENTRY A40576 #type complete TITLE cytochrome P450 ALK2-A - yeast (Candida maltosa) CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Candida maltosa DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Mar-2000 ACCESSIONS A40576 REFERENCE A40576 !$#authors Ohkuma, M.; Tanimoto, T.; Yano, K.; Takagi, M. !$#journal DNA Cell Biol. (1991) 10:271-282 !$#title CYP52 (cytochrome P450alk) multigene family in Candida !1maltosa: molecular cloning and nucleotide sequence of the !1two tandemly arranged genes. !$#cross-references MUID:91229697; PMID:2039569 !$#accession A40576 !'##status preliminary !'##molecule_type DNA !'##residues 1-526 ##label OHK GENETICS !$#gene CYP52A5 CLASSIFICATION #superfamily Candida cytochrome P450 52A3; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; monooxygenase; oxidoreductase FEATURE !$319-495 #domain cytochrome P450 homology #label CYP\ !$473 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 526 #molecular-weight 60261 #checksum 3089 SEQUENCE /// ENTRY JS0723 #type complete TITLE cytochrome P450 ALK5-A, alkane-inducible - yeast (Candida maltosa) CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Candida maltosa DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 21-Jul-2000 ACCESSIONS JS0723 REFERENCE JS0721 !$#authors Ohkuma, M. !$#submission submitted to JIPID, July 1992 !$#accession JS0723 !'##status translation not shown !'##molecule_type DNA !'##residues 1-521 ##label OHK !'##cross-references DDBJ:D12717; NID:g218352; PIDN:BAA02211.1; !1PID:g218353 GENETICS !$#gene ALK5-A CLASSIFICATION #superfamily Candida cytochrome P450 52A3; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; monooxygenase; oxidoreductase FEATURE !$314-490 #domain cytochrome P450 homology #label P45\ !$468 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 521 #molecular-weight 59871 #checksum 1124 SEQUENCE /// ENTRY S22974 #type complete TITLE cytochrome P450 52A8 - yeast (Candida tropicalis) ALTERNATE_NAMES cytochrome P450alk5 CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Candida tropicalis DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Mar-2000 ACCESSIONS S22974 REFERENCE S22972 !$#authors Seghezzi, W.; Meili, C.; Ruffiner, R.; Kuenzi, R.; Sanglard, !1D.; Fiechter, A. !$#submission submitted to the EMBL Data Library, June 1992 !$#description Isolation and characterization of additional members of the !1cytochrome P450 gene family CYP52 of Candida tropicalis. !$#accession S22974 !'##molecule_type DNA !'##residues 1-517 ##label SEG !'##cross-references EMBL:Z13012; NID:g2663; PIDN:CAA78356.1; PID:g2664 GENETICS !$#gene CYP52A8 CLASSIFICATION #superfamily Candida cytochrome P450 52A3; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; oxidoreductase FEATURE !$310-486 #domain cytochrome P450 homology #label CYP\ !$464 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 517 #molecular-weight 59525 #checksum 8502 SEQUENCE /// ENTRY S22973 #type complete TITLE cytochrome P450 52A7 - yeast (Candida tropicalis) ALTERNATE_NAMES cytochrome P450alk4 CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Candida tropicalis DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Mar-2000 ACCESSIONS S22973 REFERENCE S22972 !$#authors Seghezzi, W.; Meili, C.; Ruffiner, R.; Kuenzi, R.; Sanglard, !1D.; Fiechter, A. !$#submission submitted to the EMBL Data Library, June 1992 !$#description Isolation and characterization of additional members of the !1cytochrome P450 gene family CYP52 of Candida tropicalis. !$#accession S22973 !'##molecule_type DNA !'##residues 1-507 ##label SEG !'##cross-references EMBL:Z13011; NID:g2661; PIDN:CAA78355.1; PID:g2662 GENETICS !$#gene CYP52A7 CLASSIFICATION #superfamily Candida cytochrome P450 52A3; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; oxidoreductase; transmembrane protein FEATURE !$303-478 #domain cytochrome P450 homology #label CYP\ !$456 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 507 #molecular-weight 58670 #checksum 9944 SEQUENCE /// ENTRY JS0726 #type complete TITLE cytochrome P450 ALK8, alkane-inducible - yeast (Candida maltosa) CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Candida maltosa DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 16-Jun-2000 ACCESSIONS JS0726 REFERENCE JS0721 !$#authors Ohkuma, M. !$#submission submitted to JIPID, July 1992 !$#accession JS0726 !'##status translation not shown !'##molecule_type DNA !'##residues 1-519 ##label OHK !'##cross-references DDBJ:D12719; NID:g218356; PIDN:BAA02214.1; !1PID:g218358 GENETICS !$#gene ALK8 CLASSIFICATION #superfamily Candida cytochrome P450 52A3; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; monooxygenase; oxidoreductase FEATURE !$312-488 #domain cytochrome P450 homology #label CYP\ !$466 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 519 #molecular-weight 59476 #checksum 7791 SEQUENCE /// ENTRY JS0725 #type complete TITLE cytochrome P450 ALK7, alkane-inducible - yeast (Candida maltosa) CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Candida maltosa DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 16-Jun-2000 ACCESSIONS JS0725 REFERENCE JS0721 !$#authors Ohkuma, M. !$#submission submitted to JIPID, July 1992 !$#accession JS0725 !'##status translation not shown !'##molecule_type DNA !'##residues 1-519 ##label OHK !'##cross-references DDBJ:D12719; NID:g218356; PIDN:BAA02213.1; !1PID:g218357 GENETICS !$#gene ALK7 CLASSIFICATION #superfamily Candida cytochrome P450 52A3; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; monooxygenase; oxidoreductase FEATURE !$312-488 #domain cytochrome P450 homology #label CYP\ !$466 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 519 #molecular-weight 59749 #checksum 6796 SEQUENCE /// ENTRY S69988 #type complete TITLE unspecific monooxygenase (EC 1.14.14.1) cytochrome P450 52E1 - Candida apicola (ATCC 96134) ORGANISM #formal_name Candida apicola #variety ATCC 96134 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS S69988; S38894 REFERENCE S69988 !$#authors Lottermoser, K.; Schunck, W.H.; Asperger, O. !$#journal Yeast (1996) 12:565-575 !$#title Cytochromes P450 of the sophorose lipid-producing yeast !1Candida apicola: heterogeneity and polymerase chain !1reaction-mediated cloning of two genes. !$#cross-references MUID:96367597; PMID:8771711 !$#accession S69988 !'##molecule_type DNA !'##residues 1-519 ##label LOT !'##cross-references EMBL:X76225; NID:g840727; PIDN:CAA53811.1; !1PID:g431234 !'##experimental_source ATCC 96134 CLASSIFICATION #superfamily Candida cytochrome P450 52A3; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; monooxygenase; oxidoreductase FEATURE !$309-483 #domain cytochrome P450 homology #label P45\ !$461 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 519 #molecular-weight 58656 #checksum 180 SEQUENCE /// ENTRY S22976 #type complete TITLE cytochrome P450 52C1 - yeast (Candida tropicalis) ALTERNATE_NAMES cytochrome P450alk7 CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Candida tropicalis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS S22976 REFERENCE S22972 !$#authors Seghezzi, W.; Meili, C.; Ruffiner, R.; Kuenzi, R.; Sanglard, !1D.; Fiechter, A. !$#submission submitted to the EMBL Data Library, June 1992 !$#description Isolation and characterization of additional members of the !1cytochrome P450 gene family CYP52 of Candida tropicalis. !$#accession S22976 !'##molecule_type DNA !'##residues 1-505 ##label SEG !'##cross-references EMBL:Z13014; NID:g2667; PIDN:CAA78358.1; PID:g2668 GENETICS !$#gene CYP52C1 CLASSIFICATION #superfamily Candida cytochrome P450 52A3; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; monooxygenase; oxidoreductase; transmembrane !1protein FEATURE !$307-475 #domain cytochrome P450 homology #label P45\ !$453 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 505 #molecular-weight 58093 #checksum 2617 SEQUENCE /// ENTRY S22975 #type complete TITLE cytochrome P450 52B1 - yeast (Candida tropicalis) ALTERNATE_NAMES cytochrome P450alk6 CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Candida tropicalis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS S22975 REFERENCE S22972 !$#authors Seghezzi, W.; Meili, C.; Ruffiner, R.; Kuenzi, R.; Sanglard, !1D.; Fiechter, A. !$#submission submitted to the EMBL Data Library, June 1992 !$#description Isolation and characterization of additional members of the !1cytochrome P450 gene family CYP52 of Candida tropicalis. !$#accession S22975 !'##status preliminary !'##molecule_type DNA !'##residues 1-506 ##label SEG !'##cross-references EMBL:Z13013; NID:g2665; PIDN:CAA78357.1; PID:g2666 GENETICS !$#gene CYP52B1 CLASSIFICATION #superfamily Candida cytochrome P450 52A3; cytochrome P450 !1homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxidoreductase; !1transmembrane protein FEATURE !$299-473 #domain cytochrome P450 homology #label P45\ !$451 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 506 #molecular-weight 58541 #checksum 3203 SEQUENCE /// ENTRY C37842 #type complete TITLE cytochrome P450 - Anabaena sp. (strain PCC 7120) CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Anabaena sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C37842 REFERENCE A37842 !$#authors Lammers, P.J.; McLaughlin, S.; Papin, S.; !1Trujillo-Provencio, C.; Ryncarz II, A.J. !$#journal J. Bacteriol. (1990) 172:6981-6990 !$#title Developmental rearrangement of cyanobacterial nif genes: !1nucleotide sequence, open reading frames, and cytochrome !1P-450 homology of the Anabaena sp. strain PCC 7120 nifD !1element. !$#cross-references MUID:91072249; PMID:2123860 !$#accession C37842 !'##molecule_type DNA !'##residues 1-354 ##label LAM !'##cross-references GB:M38044 GENETICS !$#gene CYP110 CLASSIFICATION #superfamily Anabaena cytochrome P450 CYP110; cytochrome !1P450 homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; monooxygenase; oxidoreductase FEATURE !$153-310 #domain cytochrome P450 homology #label P45\ !$288 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 354 #molecular-weight 40488 #checksum 6179 SEQUENCE /// ENTRY S75761 #type complete TITLE cytochrome P450 - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein slr0574 CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S75761 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75761 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-444 ##label KAN !'##cross-references EMBL:D64003; GB:AB001339; NID:g1001200; !1PIDN:BAA10496.1; PID:g1001252 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene cyp CLASSIFICATION #superfamily Synechocystis cytochrome P450 slr0574; !1cytochrome P450 homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxidoreductase FEATURE !$251-413 #domain cytochrome P450 homology #label P45\ !$391 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 444 #molecular-weight 50578 #checksum 7738 SEQUENCE /// ENTRY S55379 #type complete TITLE cytochrome P450 CYP90 - Arabidopsis thaliana CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S55379 REFERENCE S55379 !$#authors Szekeres, M.; Nemeth, K.; Koncz, Z.; Nagy, F.; Koncz, C. !$#submission submitted to the EMBL Data Library, May 1995 !$#accession S55379 !'##molecule_type mRNA !'##residues 1-472 ##label SZE !'##cross-references EMBL:X87367; NID:g853718; PIDN:CAA60793.1; !1PID:g853719 GENETICS !$#gene CYP90 CLASSIFICATION #superfamily Synechocystis cytochrome P450 slr0574; !1cytochrome P450 homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; monooxygenase; oxidoreductase FEATURE !$275-440 #domain cytochrome P450 homology #label P45\ !$418 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 472 #molecular-weight 53785 #checksum 2519 SEQUENCE /// ENTRY D71417 #type complete TITLE cytochrome P450 d13700w - Arabidopsis thaliana CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress #variety columbia DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS D71417 REFERENCE A71400 !$#authors Bevan, M.; Bancroft, I.; Bent, E.; Love, K.; Goodman, H.; !1Dean, C.; Bergkamp, R.; Dirkse, W.; Van Staveren, M.; !1Stiekema, W.; Drost, L.; Ridley, P.; Hudson, S.A.; Patel, !1K.; Murphy, G.; Piffanelli, P.; Wedler, H.; Wedler, E.; !1Wambutt, R.; Weitzenegger, T.; Pohl, T.M.; Terryn, N.; !1Gielen, J.; Villarroel, R.; De Clerck, R.; Van Montagu, M.; !1Lecharny, A.; Auborg, S.; Gy, I.; Kreis, M.; Lao, N.; !1Kavanagh, T.; Hempel, S.; Kotter, P.; Entian, K.D.; Rieger, !1M.; Schaeffer, M.; Funk, B.; Mueller-Auer, S.; Silvey, M.; !1James, R.; Montfort, A.; Pons, A.; Puigdomenech, P.; Douka, !1A.; Voukelatou, E.; Milioni, D.; Hatzopoulos, P.; Piravandi, !1E.; Obermaier, B.; Hilbert, H.; Duesterhoft, A.; Moores, T.; !1Jones, J.D.G.; Eneva, T.; Palme, K.; Benes, V.; Rechman, S.; !1Ansorge, W.; Cooke, R.; Berger, C.; Delseny, M.; Voet, M.; !1Volckaert, G.; Mewes, H.W.; Klosterman, S.; Schueller, C.; !1Chalwatzis, N. !$#journal Nature (1998) 391:485-488 !$#title Analysis of 1.9 Mb of contiguous sequence from chromosome 4 !1of Arabidopsis thaliana. !$#cross-references MUID:98121113; PMID:9461215 !$#accession D71417 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-324 ##label BEV !'##cross-references GB:Z97338; NID:g2244870; PIDN:CAB10310.1; !1PID:g2244889 GENETICS !$#gene d13700w !$#map_position 4COP9-4G3845 CLASSIFICATION #superfamily Synechocystis cytochrome P450 slr0574; !1cytochrome P450 homology KEYWORDS oxidoreductase SUMMARY #length 324 #molecular-weight 36941 #checksum 4654 SEQUENCE /// ENTRY C71417 #type complete TITLE cytochrome P450 d13695c - Arabidopsis thaliana CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress #variety columbia DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS C71417 REFERENCE A71400 !$#authors Bevan, M.; Bancroft, I.; Bent, E.; Love, K.; Goodman, H.; !1Dean, C.; Bergkamp, R.; Dirkse, W.; Van Staveren, M.; !1Stiekema, W.; Drost, L.; Ridley, P.; Hudson, S.A.; Patel, !1K.; Murphy, G.; Piffanelli, P.; Wedler, H.; Wedler, E.; !1Wambutt, R.; Weitzenegger, T.; Pohl, T.M.; Terryn, N.; !1Gielen, J.; Villarroel, R.; De Clerck, R.; Van Montagu, M.; !1Lecharny, A.; Auborg, S.; Gy, I.; Kreis, M.; Lao, N.; !1Kavanagh, T.; Hempel, S.; Kotter, P.; Entian, K.D.; Rieger, !1M.; Schaeffer, M.; Funk, B.; Mueller-Auer, S.; Silvey, M.; !1James, R.; Montfort, A.; Pons, A.; Puigdomenech, P.; Douka, !1A.; Voukelatou, E.; Milioni, D.; Hatzopoulos, P.; Piravandi, !1E.; Obermaier, B.; Hilbert, H.; Duesterhoft, A.; Moores, T.; !1Jones, J.D.G.; Eneva, T.; Palme, K.; Benes, V.; Rechman, S.; !1Ansorge, W.; Cooke, R.; Berger, C.; Delseny, M.; Voet, M.; !1Volckaert, G.; Mewes, H.W.; Klosterman, S.; Schueller, C.; !1Chalwatzis, N. !$#journal Nature (1998) 391:485-488 !$#title Analysis of 1.9 Mb of contiguous sequence from chromosome 4 !1of Arabidopsis thaliana. !$#cross-references MUID:98121113; PMID:9461215 !$#accession C71417 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-487 ##label BEV !'##cross-references GB:Z97338; NID:g2244870; PIDN:CAB10309.1; !1PID:g2244888 GENETICS !$#gene d13695c !$#map_position 4COP9-4G3845 CLASSIFICATION #superfamily Synechocystis cytochrome P450 slr0574; !1cytochrome P450 homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxidoreductase FEATURE !$433 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 487 #molecular-weight 56273 #checksum 1181 SEQUENCE /// ENTRY T02263 #type complete TITLE cytochrome P450 DWARF3 - maize CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Zea mays #common_name maize DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS T02263 REFERENCE Z14648 !$#authors Winkler, R.G.; Helentjaris, T. !$#journal Plant Cell (1995) 7:1307-1317 !$#title The maize dwarf3 gene encodes a cytochrome P450-mediated !1early step in gibberellin biosynthesis. !$#cross-references MUID:96004534; PMID:7549486 !$#accession T02263 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-519 ##label WIN !'##cross-references EMBL:U32579; NID:g987266; PIDN:AAC49067.1; !1PID:g987267 !'##experimental_source strain B73 GENETICS !$#gene dwarf3 FUNCTION !$#description involved in an early step in gibberellin biosynthesis !$#pathway gibberellin biosynthesis CLASSIFICATION #superfamily Synechocystis cytochrome P450 slr0574; !1cytochrome P450 homology KEYWORDS oxidoreductase FEATURE !$325-488 #domain cytochrome P450 homology #label P45 SUMMARY #length 519 #molecular-weight 57905 #checksum 7372 SEQUENCE /// ENTRY S71163 #type complete TITLE cytochrome P450 - garden pea CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Pisum sativum #common_name garden pea DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S71163 REFERENCE S71163 !$#authors Baltrusch, M. !$#submission submitted to the EMBL Data Library, May 1995 !$#description Isolation of cytochrome P450 cDNA from Pisum sativum !1seedlings. !$#accession S71163 !'##status preliminary !'##molecule_type mRNA !'##residues 1-552 ##label BAL !'##cross-references EMBL:Z49263; NID:g1360117; PIDN:CAA89260.1; !1PID:g1360118 CLASSIFICATION #superfamily pea cytochrome P450 CYP97; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; monooxygenase; oxidoreductase FEATURE !$359-549 #domain cytochrome P450 homology #label P45\ !$528 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 552 #molecular-weight 62281 #checksum 2090 SEQUENCE /// ENTRY H71414 #type complete TITLE probable cytochrome P450 - Arabidopsis thaliana CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress #variety columbia DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H71414 REFERENCE A71400 !$#authors Bevan, M.; Bancroft, I.; Bent, E.; Love, K.; Goodman, H.; !1Dean, C.; Bergkamp, R.; Dirkse, W.; Van Staveren, M.; !1Stiekema, W.; Drost, L.; Ridley, P.; Hudson, S.A.; Patel, !1K.; Murphy, G.; Piffanelli, P.; Wedler, H.; Wedler, E.; !1Wambutt, R.; Weitzenegger, T.; Pohl, T.M.; Terryn, N.; !1Gielen, J.; Villarroel, R.; De Clerck, R.; Van Montagu, M.; !1Lecharny, A.; Auborg, S.; Gy, I.; Kreis, M.; Lao, N.; !1Kavanagh, T.; Hempel, S.; Kotter, P.; Entian, K.D.; Rieger, !1M.; Schaeffer, M.; Funk, B.; Mueller-Auer, S.; Silvey, M.; !1James, R.; Montfort, A.; Pons, A.; Puigdomenech, P.; Douka, !1A.; Voukelatou, E.; Milioni, D.; Hatzopoulos, P.; Piravandi, !1E.; Obermaier, B.; Hilbert, H.; Duesterhoft, A.; Moores, T.; !1Jones, J.D.G.; Eneva, T.; Palme, K.; Benes, V.; Rechman, S.; !1Ansorge, W.; Cooke, R.; Berger, C.; Delseny, M.; Voet, M.; !1Volckaert, G.; Mewes, H.W.; Klosterman, S.; Schueller, C.; !1Chalwatzis, N. !$#journal Nature (1998) 391:485-488 !$#title Analysis of 1.9 Mb of contiguous sequence from chromosome 4 !1of Arabidopsis thaliana. !$#cross-references MUID:98121113; PMID:9461215 !$#accession H71414 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-576 ##label BEV !'##cross-references GB:Z97337; NID:g2244829; PIDN:CAB10290.1; !1PID:g2244868 GENETICS !$#map_position 4COP9-4G3845 CLASSIFICATION #superfamily pea cytochrome P450 CYP97; cytochrome P450 !1homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; monooxygenase; oxidoreductase FEATURE !$352-543 #domain cytochrome P450 homology #label P45\ !$521 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 576 #molecular-weight 64802 #checksum 5363 SEQUENCE /// ENTRY O4BS6M #type complete TITLE cytochrome P450 106 - Bacillus megaterium ALTERNATE_NAMES cytochrome P450BM-1 CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Bacillus megaterium DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Mar-2000 ACCESSIONS S07764; S17973 REFERENCE S07764 !$#authors He, J.S.; Ruettinger, R.T.; Liu, H.M.; Fulco, A.J. !$#journal Biochim. Biophys. Acta (1989) 1009:301-303 !$#title Molecular cloning, coding nucleotides and the deduced amino !1acid sequence of P-450(BM-1) from Bacillus megaterium. !$#cross-references MUID:90089408; PMID:2597681 !$#accession S07764 !'##molecule_type DNA !'##residues 1-410 ##label HEJ1 !'##cross-references EMBL:X16610; NID:g39626; PIDN:CAA34612.1; !1PID:g39627 !$#accession S17973 !'##molecule_type protein !'##residues 1-25 ##label HEJ2 GENETICS !$#gene CYP106 CLASSIFICATION #superfamily Bacillus cytochrome P450 CYP106; cytochrome !1P450 homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; monooxygenase; oxidoreductase FEATURE !$1-410 #product cytochrome P450 106 #status experimental !8#label MAT\ !$241-378 #domain cytochrome P450 homology #label CYP\ !$356 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 410 #molecular-weight 47460 #checksum 5558 SEQUENCE /// ENTRY B69851 #type complete TITLE cytochrome P450 yjiB - Bacillus subtilis CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS B69851 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69851 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-396 ##label KUN !'##cross-references GB:Z99110; GB:AL009126; NID:g2633472; !1PIDN:CAB13078.1; PID:g2633575 !'##experimental_source strain 168 GENETICS !$#gene yjiB CLASSIFICATION #superfamily Bacillus cytochrome P450 CYP106; cytochrome !1P450 homology KEYWORDS oxidoreductase FEATURE !$236-371 #domain cytochrome P450 homology #label CYP SUMMARY #length 396 #molecular-weight 44990 #checksum 5785 SEQUENCE /// ENTRY S49051 #type complete TITLE cytochrome P450 tylI (EC 1.1.-.-) [validated] - Streptomyces fradiae (strain T59235) ORGANISM #formal_name Streptomyces fradiae #variety strain T59235 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S49051 REFERENCE S49051 !$#authors Merson-Davies, L.A.; Cundliffe, E. !$#journal Mol. Microbiol. (1994) 13:349-355 !$#title Analysis of five tylosin biosynthetic genes from the tyIIBA !1region of the Streptomyces fradiae genome. !$#cross-references MUID:95075319; PMID:7984112 !$#accession S49051 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-417 ##label MER !'##cross-references EMBL:U08223; NID:g6849140; PIDN:AAA21341.1; !1PID:g473597 !'##experimental_source strain T59235 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1March 1994 GENETICS !$#gene tylI FUNCTION !$#description involved in C20ring oxidation of O-mycaminosyl tylactone !1[validated, MUID:95075319] CLASSIFICATION #superfamily Bacillus cytochrome P450 CYP106; cytochrome !1P450 homology KEYWORDS heme; oxidoreductase FEATURE !$253-388 #domain cytochrome P450 homology #label CYP SUMMARY #length 417 #molecular-weight 47224 #checksum 3403 SEQUENCE /// ENTRY B40634 #type complete TITLE erythromycin monooxygenase (EC 1.14.-.-) - Saccharopolyspora erythraea ALTERNATE_NAMES erythromycin C-12 hydroxylase EryK ORGANISM #formal_name Saccharopolyspora erythraea DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS B40634 REFERENCE A40634 !$#authors Stassi, D.; Donadio, S.; Staver, M.J.; Katz, L. !$#journal J. Bacteriol. (1993) 175:182-189 !$#title Identification of a Saccharopolyspora erythraea gene !1required for the final hydroxylation step in erythromycin !1biosynthesis. !$#cross-references MUID:93106953; PMID:8416893 !$#accession B40634 !'##status preliminary !'##molecule_type DNA !'##residues 1-412 ##label STA !'##cross-references GB:U82823; GB:L05776; NID:g2327012 !'##note sequence extracted from NCBI backbone (NCBIN:121243, !1NCBIP:121245) GENETICS !$#gene CYP113A1 CLASSIFICATION #superfamily Bacillus cytochrome P450 CYP106; cytochrome !1P450 homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxidoreductase FEATURE !$238-376 #domain cytochrome P450 homology #label CYP\ !$354 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 412 #molecular-weight 45440 #checksum 3109 SEQUENCE /// ENTRY S71328 #type complete TITLE cytochrome P450 CYP119 - Sulfolobus solfataricus CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Sulfolobus solfataricus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS S71328 REFERENCE S71328 !$#authors Wright, R.L.; Harris, K.; Solow, B.; White, R.H.; Kennelly, !1P.J. !$#journal FEBS Lett. (1996) 384:235-239 !$#title Cloning of a potential cytochrome P450 from the Archaeon !1Sulfolobus solfataricus. !$#cross-references MUID:96197795; PMID:8617361 !$#accession S71328 !'##molecule_type DNA !'##residues 1-368 ##label WRI !'##cross-references EMBL:U51337; NID:g1256447; PIDN:AAB03278.1; !1PID:g1256448 !'##experimental_source ATCC 35091 GENETICS !$#gene CYP119 CLASSIFICATION #superfamily Bacillus cytochrome P450 CYP106; cytochrome !1P450 homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxidoreductase FEATURE !$206-339 #domain cytochrome P450 homology #label CYP\ !$317 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 368 #molecular-weight 42863 #checksum 2593 SEQUENCE /// ENTRY B42606 #type complete TITLE cytochrome P450 CVIIB1 - Saccharopolyspora erythraea CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Saccharopolyspora erythraea DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS B42606 REFERENCE A42606 !$#authors Andersen, J.F.; Hutchinson, C.R. !$#journal J. Bacteriol. (1992) 174:725-735 !$#title Characterization of Saccharopolyspora erythraea cytochrome !1P-450 genes and enzymes, including 6-deoxyerythronolide B !1hydroxylase. !$#cross-references MUID:92121109; PMID:1732208 !$#accession B42606 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA; protein !'##residues 1-405 ##label AND !'##cross-references GB:M83110; NID:g152682; PIDN:AAA26483.1; !1PID:g152684 !'##experimental_source NRRL2338 !'##note sequence extracted from NCBI backbone (NCBIP:77484) GENETICS !$#gene CYP107B1 CLASSIFICATION #superfamily Bacillus cytochrome P450 CYP106; cytochrome !1P450 homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxidoreductase FEATURE !$238-374 #domain cytochrome P450 homology #label CYP\ !$352 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 405 #molecular-weight 45238 #checksum 5014 SEQUENCE /// ENTRY JC4003 #type complete TITLE cytochrome P450 - Streptomyces sp. CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Streptomyces sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS JC4003 REFERENCE JC4001 !$#authors Arisawa, A.; Tsunekawa, H.; Okamura, K.; Okamoto, R. !$#journal Biosci. Biotechnol. Biochem. (1995) 59:582-588 !$#title Nucleotide sequence analysis of the carbomycin biosynthetic !1genes including the 3-O-acyltransferase gene from !1Streptomyces thermotolerans. !$#cross-references MUID:95290751; PMID:7772821 !$#accession JC4003 !'##molecule_type DNA !'##residues 1-411 ##label ARI !'##cross-references DDBJ:D30759; NID:g551628; PIDN:BAA06420.1; !1PID:g551630 !'##note the source was designated as Streptomyces thermotolerans CLASSIFICATION #superfamily Bacillus cytochrome P450 CYP106; cytochrome !1P450 homology KEYWORDS oxidoreductase FEATURE !$242-382 #domain cytochrome P450 homology #label CYP SUMMARY #length 411 #molecular-weight 45273 #checksum 3256 SEQUENCE /// ENTRY S18531 #type complete TITLE cytochrome P450 eryF - Saccharopolyspora erythraea CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Saccharopolyspora erythraea DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S18531; S16745 REFERENCE S18530 !$#authors Haydock, S.F.; Dowson, J.A.; Dhillon, N.; Roberts, G.A.; !1Cortes, J.; Leadlay, P.F. !$#journal Mol. Gen. Genet. (1991) 230:120-128 !$#title Cloning and sequence analysis of genes involved in !1erythromycin biosynthesis in Saccharopolyspora erythraea: !1sequence similarities between EryG and a family of !1S-adenosylmethionine-dependent methyltransferases. !$#cross-references MUID:92079886; PMID:1840640 !$#accession S18531 !'##molecule_type DNA !'##residues 1-406 ##label HAY !'##cross-references EMBL:X60379; NID:g48941; PIDN:CAA42927.1; !1PID:g48943 !'##note the authors translated the codon AGG for residue 190 as Lys GENETICS !$#gene eryF CLASSIFICATION #superfamily Bacillus cytochrome P450 CYP106; cytochrome !1P450 homology KEYWORDS oxidoreductase FEATURE !$238-375 #domain cytochrome P450 homology #label CYP SUMMARY #length 406 #molecular-weight 45441 #checksum 3305 SEQUENCE /// ENTRY S51594 #type complete TITLE cytochrome P450 mycG - Micromonospora griseorubida CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Micromonospora griseorubida DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S51594 REFERENCE S51593 !$#authors Inouye, M.; Takada, Y.; Muto, N.; Beppu, T.; Horinouchi, S. !$#journal Mol. Gen. Genet. (1994) 245:456-464 !$#title Characterization and expression of a P-450-like mycinamicin !1biosynthesis gene using a novel Micromonospora-Escherichia !1coli shuttle cosmid vector. !$#cross-references MUID:95107242; PMID:7808395 !$#accession S51594 !'##molecule_type DNA !'##residues 1-397 ##label INO !'##cross-references EMBL:D16098; NID:g286050; PIDN:BAA03672.1; !1PID:g303644 GENETICS !$#gene mycG !$#start_codon GTG CLASSIFICATION #superfamily Bacillus cytochrome P450 CYP106; cytochrome !1P450 homology KEYWORDS heme; oxidoreductase FEATURE !$231-368 #domain cytochrome P450 homology #label CYP SUMMARY #length 397 #molecular-weight 44331 #checksum 7013 SEQUENCE /// ENTRY JC5859 #type complete TITLE polyketide synthase cytochrome P450 chain 10 - Actinomadura hibisca CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Actinomadura hibisca DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS JC5859 REFERENCE JC5850 !$#authors Dairi, T.; Hamano, Y.; Igarashi, Y.; Furumai, T.; Oki, T. !$#journal Biosci. Biotechnol. Biochem. (1997) 61:1445-1453 !$#title Cloning and nucleotide sequence of the putative polyketide !1synthase genes for pradimicin biosynthesis from Actinomadura !1hibisca. !$#cross-references MUID:97480928; PMID:9339544 !$#accession JC5859 !'##molecule_type DNA !'##residues 1-411 ##label DAI !'##cross-references DDBJ:D87924; NID:g2580441; PIDN:BAA23153.1; !1PID:g2580451 COMMENT This enzyme is involved in pradimicin A biosynthesis. GENETICS !$#gene pms10 CLASSIFICATION #superfamily Bacillus cytochrome P450 CYP106; cytochrome !1P450 homology KEYWORDS antibiotic biosynthesis; oxidoreductase FEATURE !$245-382 #domain cytochrome P450 homology #label CYP SUMMARY #length 411 #molecular-weight 44860 #checksum 212 SEQUENCE /// ENTRY S15809 #type complete TITLE cytochrome P450 CYP105C1 - Streptomyces sp. CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Streptomyces sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS S15809; S19629 REFERENCE S15809 !$#authors Horii, M.; Ishizaki, T.; Paik, S.Y.; Manome, T.; Murooka, Y. !$#journal J. Bacteriol. (1990) 172:3644-3653 !$#title An operon containing the genes for cholesterol oxidase and a !1cytochrome P-450-like protein from a Streptomyces sp. !$#cross-references MUID:90299781; PMID:2361941 !$#accession S15809 !'##molecule_type DNA !'##residues 1-381 ##label ISH1 !'##cross-references EMBL:M31939 REFERENCE S19629 !$#authors Ishizaki, T. !$#submission submitted to the EMBL Data Library, February 1990 !$#accession S19629 !'##molecule_type DNA !'##residues 1-144,'P',146-148,'H',150-381 ##label ISH2 !'##cross-references EMBL:M31939; NID:g153210; PIDN:AAA26718.1; !1PID:g153211 GENETICS !$#gene CYP105C1 CLASSIFICATION #superfamily Bacillus cytochrome P450 CYP106; cytochrome !1P450 homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; monooxygenase; oxidoreductase FEATURE !$216-352 #domain cytochrome P450 homology #label CYP\ !$358 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 381 #molecular-weight 41668 #checksum 6548 SEQUENCE /// ENTRY A55578 #type complete TITLE cytochrome P450 - Rhodococcus fascians plasmid CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Rhodococcus fascians DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A55578; S42052 REFERENCE A55578 !$#authors Crespi, M.; Vereecke, D.; Temmerman, W.; Van Montagu, M.; !1Desomer, J. !$#journal J. Bacteriol. (1994) 176:2492-2501 !$#title The fas operon of Rhodococcus fascians encodes new genes !1required for efficient fasciation of host plants. !$#cross-references MUID:94222824; PMID:8169198 !$#accession A55578 !'##status preliminary !'##molecule_type DNA !'##residues 1-399 ##label CRE !'##cross-references GB:Z29635; NID:g455000; PIDN:CAA82741.1; !1PID:g455001 !'##experimental_source plasmid pFiD188 GENETICS !$#genome plasmid CLASSIFICATION #superfamily Bacillus cytochrome P450 CYP106; cytochrome !1P450 homology KEYWORDS oxidoreductase FEATURE !$235-371 #domain cytochrome P450 homology #label CYP SUMMARY #length 399 #molecular-weight 43595 #checksum 3413 SEQUENCE /// ENTRY E69611 #type complete TITLE cytochrome P450 cypA - Bacillus subtilis CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69611; T44774 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69611 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-410 ##label KUN !'##cross-references GB:Z99117; GB:AL009126; NID:g2634966; !1PIDN:CAB14615.1; PID:g2635119 !'##experimental_source strain 168 REFERENCE Z22837 !$#authors Belitsky, B.R.; Gustafsson, M.C.U.; Sonenshein, A.L.; von !1Wachenfeldt, C. !$#journal J. Bacteriol. (1997) 179:5448-5457 !$#title An lrp-like gene of Bacillus subtilis involved in !1branched-chain amino acid transport. !$#cross-references MUID:97431495; PMID:9287000 !$#accession T44774 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-410 ##label BEL !'##cross-references EMBL:Y11043; NID:g1926275; PIDN:CAA71937.1; !1PID:g1926278 !'##experimental_source strain 1A1 GENETICS !$#gene cypA CLASSIFICATION #superfamily Bacillus cytochrome P450 CYP106; cytochrome !1P450 homology KEYWORDS oxidoreductase FEATURE !$245-381 #domain cytochrome P450 homology #label CYP SUMMARY #length 410 #molecular-weight 47384 #checksum 9608 SEQUENCE /// ENTRY G69679 #type complete TITLE polyketide hydroxylase (EC 1.-.-.-) pksS - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS G69679 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69679 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-376 ##label KUN !'##cross-references GB:Z99113; GB:AL009126; NID:g2634090; !1PIDN:CAB13607.1; PID:g2634107 !'##experimental_source strain 168 GENETICS !$#gene pksS CLASSIFICATION #superfamily Bacillus cytochrome P450 CYP106; cytochrome !1P450 homology KEYWORDS oxidoreductase FEATURE !$240-376 #domain cytochrome P450 homology #label CYP SUMMARY #length 376 #molecular-weight 43418 #checksum 767 SEQUENCE /// ENTRY G69594 #type complete TITLE cytochrome P450 bioI - Bacillus subtilis CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS G69594 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69594 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-395 ##label KUN !'##cross-references GB:Z99119; GB:AL009126; NID:g2635411; !1PIDN:CAB14997.1; PID:g2635503 !'##experimental_source strain 168 GENETICS !$#gene bioI CLASSIFICATION #superfamily Bacillus cytochrome P450 CYP106; cytochrome !1P450 homology KEYWORDS oxidoreductase FEATURE !$232-367 #domain cytochrome P450 homology #label CYP SUMMARY #length 395 #molecular-weight 44865 #checksum 3781 SEQUENCE /// ENTRY I40208 #type complete TITLE cytochrome P450 BJ-1 CYP112 - Bradyrhizobium japonicum CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Bradyrhizobium japonicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS I40208 REFERENCE I40207 !$#authors Tully, R.E.; Keister, D.L. !$#journal Appl. Environ. Microbiol. (1993) 59:4136-4142 !$#title Cloning and mutagenesis of a cytochrome P-450 locus from !1Bradyrhizobium japonicum that is expressed anaerobically and !1symbiotically. !$#accession I40208 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-401 ##label RES !'##cross-references EMBL:U12678; NID:g529961; PIDN:AAC28889.1; !1PID:g529962 GENETICS !$#gene CYP112 CLASSIFICATION #superfamily Bacillus cytochrome P450 CYP106; cytochrome !1P450 homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxidoreductase FEATURE !$234-372 #domain cytochrome P450 homology #label CYP\ !$350 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 401 #molecular-weight 44496 #checksum 2431 SEQUENCE /// ENTRY I40209 #type complete TITLE cytochrome P450 BJ-3 CYP114 - Bradyrhizobium japonicum CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Bradyrhizobium japonicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS I40209 REFERENCE I40207 !$#authors Tully, R.E.; Keister, D.L. !$#journal Appl. Environ. Microbiol. (1993) 59:4136-4142 !$#title Cloning and mutagenesis of a cytochrome P-450 locus from !1Bradyrhizobium japonicum that is expressed anaerobically and !1symbiotically. !$#accession I40209 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-382 ##label TUL !'##cross-references EMBL:U12678; NID:g529961; PIDN:AAC28890.1; !1PID:g529963 GENETICS !$#gene CYP114 !$#start_codon TTG CLASSIFICATION #superfamily Bacillus cytochrome P450 CYP106; cytochrome !1P450 homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxidoreductase FEATURE !$204-351 #domain cytochrome P450 homology #label CYP\ !$329 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 382 #molecular-weight 41625 #checksum 6542 SEQUENCE /// ENTRY JC5150 #type complete TITLE nitric-oxide reductase (EC 1.7.99.7) cytochrome P450 55A1 - fungus (Fusarium oxysporum) ALTERNATE_NAMES cytochrome P450 norA; nitric-oxide reductase A ORGANISM #formal_name Fusarium oxysporum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS JC5150; PC4246; A40401; JX0335 REFERENCE JC5150 !$#authors Nakahara, K.; Shoun, H. !$#journal J. Biochem. (1996) 120:1082-1087 !$#title N-terminal processing and amino acid sequence of two !1isoforms of nitric oxide reductase cytochrome P450nor from !1Fusarium oxysporum. !$#cross-references MUID:97164007; PMID:9010754 !$#accession JC5150 !'##status preliminary !'##molecule_type mRNA !'##residues 1-404 ##label NAK !$#accession PC4246 !'##status preliminary !'##molecule_type protein !'##residues !11-31;32-39;51-57;68-78;90-121;129-138;144-169;215-227; !1246-268;278-293;300-381;386-393 ##label NA2 REFERENCE A40401 !$#authors Kizawa, H.; Tomura, D.; Oda, M.; Fukamizu, A.; Hoshino, T.; !1Gotoh, O.; Yasui, T.; Shoun, H. !$#journal J. Biol. Chem. (1991) 266:10632-10637 !$#title Nucleotide sequence of the unique nitrate/nitrite-inducible !1cytochrome P-450 cDNA from Fusarium oxysporum. !$#cross-references MUID:91244845; PMID:2037602 !$#accession A40401 !'##molecule_type mRNA !'##residues 2-404 ##label KIZ !'##cross-references GB:M63340; NID:g168152; PIDN:AAA33337.1; !1PID:g168153 REFERENCE JX0335 !$#authors Tomura, D.; Obika, K.; Fukamizu, A.; Shoun, H. !$#journal J. Biochem. (1994) 116:88-94 !$#title Nitric oxide reductase cytochrome P-450 gene, CYP 55, of the !1fungus Fusarium oxysporum containing a potential !1binding-site for FNR, the transcription factor involved in !1the regulation of anaerobic growth of Escherichia coli. !$#cross-references MUID:95096031; PMID:7798191 !$#accession JX0335 !'##molecule_type DNA !'##residues 2-404 ##label TOM !'##cross-references DDBJ:D14517; NID:g285800; PIDN:BAA03390.1; !1PID:g285801 !'##experimental_source strain MT-811 COMMENT The expression of this protein is regulated in response to !1oxygen tension by an fumarate and nitrate reduction-like !1system. COMMENT This enzyme is involved in fungal denitrification, acting as !1a nitric oxide reductase. GENETICS !$#gene CYP55A1 !$#introns 63/3; 99/2; 152/3; 190/2; 251/3; 304/3; 368/1 CLASSIFICATION #superfamily Bacillus cytochrome P450 CYP106; cytochrome !1P450 homology KEYWORDS chromoprotein; cytosol; heme; iron; metalloprotein; !1oxidoreductase FEATURE !$3-404 #product nitric-oxide reductase cytochrome P450 55A1 !8#status experimental #label MAT\ !$237-375 #domain cytochrome P450 homology #label CYP\ !$353 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 404 #molecular-weight 44473 #checksum 3453 SEQUENCE /// ENTRY S47520 #type complete TITLE vitamin D-3 25-hydroxylase (EC 1.-.-.-) cytochrome P450 VD25 - Amycolata autotrophica ORGANISM #formal_name Amycolata autotrophica DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S47520 REFERENCE S47520 !$#authors Kawauchi, H.; Sasaki, J.; Adachi, T.; Hanada, K.; Beppu, T.; !1Horinouchi, S. !$#journal Biochim. Biophys. Acta (1994) 1219:179-183 !$#title Cloning and nucleotide sequence of a bacterial cytochrome !1P-450(VD25) gene encoding vitamin D-3 25-hydroxylase. !$#cross-references MUID:94368852; PMID:8086461 !$#accession S47520 !'##molecule_type DNA !'##residues 1-398 ##label KAW !'##cross-references GB:D26543; NID:g559303; PIDN:BAA05541.1; !1PID:g1225904 !'##note the sequence from Fig. 4 is inconsistent with that from Fig. 3 !1in having 296-Asp GENETICS !$#gene P450-VD25 CLASSIFICATION #superfamily Bacillus cytochrome P450 CYP106; cytochrome !1P450 homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxidoreductase FEATURE !$238-369 #domain cytochrome P450 homology #label CYP\ !$347 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 398 #molecular-weight 44308 #checksum 8665 SEQUENCE /// ENTRY A48495 #type complete TITLE linalool 8-monooxygenase (EC 1.14.99.28) - Pseudomonas incognita ORGANISM #formal_name Pseudomonas incognita DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A48495 REFERENCE A48495 !$#authors Ropp, J.D.; Gunsalus, I.C.; Sligar, S.G. !$#journal J. Bacteriol. (1993) 175:6028-6037 !$#title Cloning and expression of a member of a new cytochrome P-450 !1family: cytochrome P-450lin (CYP111) from Pseudomonas !1incognita. !$#cross-references MUID:93388536; PMID:8376348 !$#accession A48495 !'##status preliminary !'##molecule_type DNA !'##residues 1-406 ##label ROP !'##cross-references GB:L23310; NID:g405542; PIDN:AAA25810.1; !1PID:g405543 CLASSIFICATION #superfamily Bacillus cytochrome P450 CYP106; cytochrome !1P450 homology KEYWORDS oxidoreductase FEATURE !$242-377 #domain cytochrome P450 homology #label CYP SUMMARY #length 406 #molecular-weight 45637 #checksum 5536 SEQUENCE /// ENTRY A42971 #type complete TITLE cytochrome P450terp - Pseudomonas sp. ALTERNATE_NAMES cytochrome P450-terpredoxin CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Pseudomonas sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A42971; S27653 REFERENCE A42971 !$#authors Peterson, J.A.; Lu, J.Y.; Geisselsoder, J.; Graham-Lorence, !1S.; Carmona, C.; Witney, F.; Lorence, M.C. !$#journal J. Biol. Chem. (1992) 267:14193-14203 !$#title Cytochrome P-450terp. Isolation and purification of the !1protein and cloning and sequencing of its operon. !$#cross-references MUID:92332528; PMID:1629218 !$#accession A42971 !'##status preliminary !'##molecule_type DNA; protein !'##residues 1-428 ##label PET !'##cross-references EMBL:M91440; NID:g151584; PIDN:AAA25996.1; !1PID:g151587 !'##note sequence extracted from NCBI backbone (NCBIP:108469) CLASSIFICATION #superfamily Bacillus cytochrome P450 CYP106; cytochrome !1P450 homology KEYWORDS oxidoreductase FEATURE !$264-399 #domain cytochrome P450 homology #label CYP SUMMARY #length 428 #molecular-weight 47922 #checksum 8787 SEQUENCE /// ENTRY F69611 #type complete TITLE cytochrome P450 cypX - Bacillus subtilis CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS F69611 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69611 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-405 ##label KUN !'##cross-references GB:Z99121; GB:Z99122; GB:AL009126; NID:g2636029; !1PIDN:CAB15523.1; PID:g2636032; NID:g2635827; PID:g2636019 !'##experimental_source strain 168 GENETICS !$#gene cypX CLASSIFICATION #superfamily Bacillus cytochrome P450 CYP106; cytochrome !1P450 homology KEYWORDS oxidoreductase FEATURE !$230-375 #domain cytochrome P450 homology #label CYP SUMMARY #length 405 #molecular-weight 45472 #checksum 9467 SEQUENCE /// ENTRY A70707 #type complete TITLE cytochrome P450 Rv0766c - Mycobacterium tuberculosis (strain H37RV) CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A70707 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession A70707 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-402 ##label COL !'##cross-references GB:Z80226; GB:AL123456; NID:g3261638; !1PIDN:CAB02396.1; PID:g1550644 !'##experimental_source strain H37Rv GENETICS !$#gene Rv0766c CLASSIFICATION #superfamily Bacillus cytochrome P450 CYP106; cytochrome !1P450 homology KEYWORDS oxidoreductase FEATURE !$236-372 #domain cytochrome P450 homology #label CYP SUMMARY #length 402 #molecular-weight 45421 #checksum 405 SEQUENCE /// ENTRY E70708 #type complete TITLE cytochrome P450 Rv0778 - Mycobacterium tuberculosis (strain H37RV) CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS E70708 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession E70708 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-414 ##label COL !'##cross-references GB:Z80226; GB:AL123456; NID:g3261638; !1PIDN:CAB02390.1; PID:g1550656 !'##experimental_source strain H37Rv GENETICS !$#gene Rv0778 CLASSIFICATION #superfamily Bacillus cytochrome P450 CYP106; cytochrome !1P450 homology KEYWORDS oxidoreductase FEATURE !$250-385 #domain cytochrome P450 homology #label CYP SUMMARY #length 414 #molecular-weight 45954 #checksum 599 SEQUENCE /// ENTRY H70752 #type complete TITLE cytochrome P450 Rv1256c - Mycobacterium tuberculosis (strain H37RV) CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS H70752 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession H70752 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-405 ##label COL !'##cross-references GB:Z77137; GB:AL123456; NID:g3261593; !1PIDN:CAB00896.1; PID:g1480330 !'##experimental_source strain H37Rv GENETICS !$#gene Rv1256c CLASSIFICATION #superfamily Bacillus cytochrome P450 CYP106; cytochrome !1P450 homology KEYWORDS oxidoreductase FEATURE !$240-376 #domain cytochrome P450 homology #label CYP SUMMARY #length 405 #molecular-weight 44580 #checksum 8960 SEQUENCE /// ENTRY F70729 #type complete TITLE cytochrome P450 Rv2266 - Mycobacterium tuberculosis (strain H37RV) CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS F70729 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession F70729 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-428 ##label COL !'##cross-references GB:Z77163; GB:AL123456; NID:g3261610; !1PIDN:CAB00969.1; PID:g1449354 !'##experimental_source strain H37Rv GENETICS !$#gene Rv2266 CLASSIFICATION #superfamily Bacillus cytochrome P450 CYP106; cytochrome !1P450 homology KEYWORDS oxidoreductase FEATURE !$264-401 #domain cytochrome P450 homology #label CYP SUMMARY #length 428 #molecular-weight 47824 #checksum 7839 SEQUENCE /// ENTRY H70729 #type complete TITLE cytochrome P450 Rv2268c - Mycobacterium tuberculosis (strain H37RV) CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H70729 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession H70729 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-489 ##label COL !'##cross-references GB:Z77163; GB:AL123456; NID:g3261610; !1PIDN:CAB00967.1; PID:g1449352 !'##experimental_source strain H37Rv GENETICS !$#gene Rv2268c CLASSIFICATION #superfamily Bacillus cytochrome P450 CYP106; cytochrome !1P450 homology KEYWORDS oxidoreductase FEATURE !$322-457 #domain cytochrome P450 homology #label P45 SUMMARY #length 489 #molecular-weight 53313 #checksum 9771 SEQUENCE /// ENTRY H70730 #type complete TITLE cytochrome P450 Rv2276 - Mycobacterium tuberculosis (strain H37RV) CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H70730 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession H70730 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-396 ##label COL !'##cross-references GB:Z77163; GB:AL123456; NID:g3261610; !1PIDN:CAB00959.1; PID:g1449344 !'##experimental_source strain H37Rv GENETICS !$#gene Rv2276 CLASSIFICATION #superfamily Bacillus cytochrome P450 CYP106; cytochrome !1P450 homology KEYWORDS oxidoreductase FEATURE !$230-367 #domain cytochrome P450 homology #label P45 SUMMARY #length 396 #molecular-weight 43255 #checksum 4994 SEQUENCE /// ENTRY B70677 #type complete TITLE cytochrome P450 Rv3545c - Mycobacterium tuberculosis (strain H37RV) CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS B70677 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession B70677 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-433 ##label COL !'##cross-references GB:Z82098; GB:AL123456; NID:g3261664; !1PIDN:CAB05061.1; PID:g1666115 !'##experimental_source strain H37Rv GENETICS !$#gene Rv3545c CLASSIFICATION #superfamily Bacillus cytochrome P450 CYP106; cytochrome !1P450 homology KEYWORDS oxidoreductase FEATURE !$265-399 #domain cytochrome P450 homology #label P45 SUMMARY #length 433 #molecular-weight 48432 #checksum 7986 SEQUENCE /// ENTRY D70985 #type complete TITLE cytochrome P450 Rv1666c - Mycobacterium tuberculosis (strain H37RV) CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D70985 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession D70985 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-430 ##label COL !'##cross-references GB:Z95617; GB:AL123456; NID:g3242249; !1PIDN:CAB09102.1; PID:g3242251 !'##experimental_source strain H37Rv GENETICS !$#gene Rv1666c CLASSIFICATION #superfamily Bacillus cytochrome P450 CYP106; cytochrome !1P450 homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxidoreductase FEATURE !$231-394 #domain cytochrome P450 homology #label P45\ !$372 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 430 #molecular-weight 47864 #checksum 2888 SEQUENCE /// ENTRY B70511 #type complete TITLE cytochrome P450 Rv1777 - Mycobacterium tuberculosis (strain H37RV) CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B70511 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession B70511 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-434 ##label COL !'##cross-references GB:Z97345; GB:AL123456; NID:g3261824; !1PIDN:CAB10567.1; PID:g2245328 !'##experimental_source strain H37Rv GENETICS !$#gene Rv1777 CLASSIFICATION #superfamily Bacillus cytochrome P450 CYP106; cytochrome !1P450 homology KEYWORDS oxidoreductase FEATURE !$271-407 #domain cytochrome P450 homology #label P45 SUMMARY #length 434 #molecular-weight 47218 #checksum 6822 SEQUENCE /// ENTRY E70515 #type complete TITLE cytochrome P450 Rv1880c - Mycobacterium tuberculosis (strain H37RV) CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS E70515 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession E70515 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-438 ##label COL !'##cross-references GB:Z97193; GB:AL123456; NID:g3261816; !1PIDN:CAB10066.1; PID:g2225980 !'##experimental_source strain H37Rv GENETICS !$#gene Rv1880c CLASSIFICATION #superfamily Bacillus cytochrome P450 CYP106; cytochrome !1P450 homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxidoreductase FEATURE !$267-403 #domain cytochrome P450 homology #label P45\ !$381 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 438 #molecular-weight 48871 #checksum 1896 SEQUENCE /// ENTRY H70807 #type complete TITLE cytochrome P450 Rv3518c - Mycobacterium tuberculosis (strain H37RV) CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H70807 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession H70807 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-398 ##label COL !'##cross-references GB:AL022022; GB:AL123456; NID:g3261554; !1PIDN:CAA17755.1; PID:g2924455 !'##experimental_source strain H37Rv GENETICS !$#gene Rv3518c CLASSIFICATION #superfamily Bacillus cytochrome P450 CYP106; cytochrome !1P450 homology KEYWORDS oxidoreductase FEATURE !$227-362 #domain cytochrome P450 homology #label P45 SUMMARY #length 398 #molecular-weight 44398 #checksum 3559 SEQUENCE /// ENTRY H70921 #type complete TITLE cytochrome P450 Rv3121 - Mycobacterium tuberculosis (strain H37RV) CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS H70921 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession H70921 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-400 ##label COL !'##cross-references GB:Z95150; GB:AL123456; NID:g3250708; !1PIDN:CAB08378.1; PID:g2076696 !'##experimental_source strain H37Rv GENETICS !$#gene Rv3121 CLASSIFICATION #superfamily Bacillus cytochrome P450 CYP106; cytochrome !1P450 homology KEYWORDS oxidoreductase FEATURE !$232-368 #domain cytochrome P450 homology #label CYP SUMMARY #length 400 #molecular-weight 43730 #checksum 9647 SEQUENCE /// ENTRY C70929 #type complete TITLE cytochrome P450 Rv1785c - Mycobacterium tuberculosis (strain H37RV) CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C70929 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession C70929 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-393 ##label COL !'##cross-references GB:AL022021; GB:AL123456; NID:g3250699; !1PIDN:CAA17707.1; PID:g2924467 !'##experimental_source strain H37Rv GENETICS !$#gene Rv1785c CLASSIFICATION #superfamily Bacillus cytochrome P450 CYP106; cytochrome !1P450 homology KEYWORDS oxidoreductase FEATURE !$229-364 #domain cytochrome P450 homology #label P45 SUMMARY #length 393 #molecular-weight 43541 #checksum 8877 SEQUENCE /// ENTRY A32306 #type complete TITLE cytochrome P450 CYP103 - Agrobacterium tumefaciens plasmid pTiA6 ALTERNATE_NAMES cytochrome P450 pinF1 CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Agrobacterium tumefaciens DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A32306 REFERENCE A32306 !$#authors Kanemoto, R.H.; Powell, A.T.; Akiyoshi, D.E.; Regier, D.A.; !1Kerstetter, R.A.; Nester, E.W.; Hawes, M.C.; Gordon, M.P. !$#journal J. Bacteriol. (1989) 171:2506-2512 !$#title Nucleotide sequence and analysis of the plant-inducible !1locus pinF from Agrobacterium tumefaciens. !$#cross-references MUID:89213933; PMID:2708311 !$#accession A32306 !'##molecule_type DNA !'##residues 1-422 ##label KAN !'##cross-references GB:M19352; NID:g142260; PIDN:AAA82502.1; !1PID:g142261 GENETICS !$#gene pinF1 !$#genome plasmid CLASSIFICATION #superfamily Agrobacterium plasmid cytochrome P450 pinF1; !1cytochrome P450 homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; monooxygenase; oxidoreductase FEATURE !$255-391 #domain cytochrome P450 homology #label P45\ !$369 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 422 #molecular-weight 47519 #checksum 9364 SEQUENCE /// ENTRY O4PSCP #type complete TITLE camphor 5-monooxygenase (EC 1.14.15.1) cytochrome P450 101 - Pseudomonas putida plasmid CAM ALTERNATE_NAMES cytochrome P450-CAM ORGANISM #formal_name Pseudomonas putida DATE 30-Apr-1982 #sequence_revision 31-Dec-1993 #text_change 03-Mar-2000 ACCESSIONS A25660; S34614; C60886; A00194 REFERENCE A94678 !$#authors Unger, B.P.; Gunsalus, I.C.; Sligar, S.G. !$#journal J. Biol. Chem. (1986) 261:1158-1163 !$#title Nucleotide sequence of the Pseudomonas putida cytochrome !1P-450-cam gene and its expression in Escherichia coli. !$#cross-references MUID:86111751; PMID:3003058 !$#accession A25660 !'##molecule_type DNA !'##residues 1-415 ##label UNG !'##cross-references GB:M12546; NID:g151114; PIDN:AAA25760.1; !1PID:g151115 REFERENCE S34613 !$#authors Aramaki, H.; Koga, H.; Sagara, Y.; Hosoi, M.; Horiuchi, T. !$#journal Biochim. Biophys. Acta (1993) 1174:91-94 !$#title Complete nucleotide sequence of the 5-exo-hydroxycamphor !1dehydrogenase gene on the CAM plasmid of Pseudomonas putida !1(ATCC 17453). !$#cross-references MUID:93326643; PMID:8334169 !$#accession S34614 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-42 ##label ARA !'##experimental_source PpG1; ATCC 17453; CAM plasmid REFERENCE A60886 !$#authors Romeo, C.; Moriwaki, N.; Yasunobu, K.T.; Gunsalus, I.C.; !1Koga, H. !$#journal J. Protein Chem. (1987) 6:253-261 !$#title Identification of the coding region for the putidaredoxin !1reductase gene from the plasmid of Pseudomonas putida. !$#accession C60886 !'##molecule_type DNA !'##residues 408-415 ##label ROM REFERENCE A00194 !$#authors Haniu, M.; Armes, L.G.; Yasunobu, K.T.; Shastry, B.A.; !1Gunsalus, I.C. !$#journal J. Biol. Chem. (1982) 257:12664-12671 !$#title Amino acid sequence of the Pseudomonas putida cytochrome !1P-450. II. Cyanogen bromide peptides, acid cleavage !1peptides, and the complete sequence. !$#cross-references MUID:83030788; PMID:7130171 !$#accession A00194 !'##molecule_type protein !'##residues 2-55,58-276,'Q',278-361,'S',363-407,'N',409-415 ##label HAN GENETICS !$#gene camC; CYP101 !$#genome plasmid FUNCTION !$#description catalyzes hydroxylation of camphor to yield !15-exo-hydroxycamphor; electron transfer; monooxygenase; !1oxidoreductase CLASSIFICATION #superfamily Pseudomonas plasmid camphor 5-monooxygenase; !1cytochrome P450 homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; monooxygenase; oxidoreductase FEATURE !$246-380 #domain cytochrome P450 homology #label CYP\ !$358 #binding_site heme iron (Cys) (axial ligand) #status !8experimental SUMMARY #length 415 #molecular-weight 46669 #checksum 6876 SEQUENCE /// ENTRY FECL2P #type complete TITLE ferredoxin [2Fe-2S] - Clostridium pasteurianum ORGANISM #formal_name Clostridium pasteurianum DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 11-Jun-1999 ACCESSIONS JH0804; S34628; A24460; S31452 REFERENCE JH0804 !$#authors Fujinaga, J.; Meyer, J. !$#journal Biochem. Biophys. Res. Commun. (1993) 192:1115-1122 !$#title Cloning and expression in Escherichia coli of the gene !1encoding the [2Fe-2S] ferredoxin from Clostridium !1pasteurianum. !$#cross-references MUID:93282812; PMID:7916603 !$#accession JH0804 !'##molecule_type DNA !'##residues 1-102 ##label FUJ !'##cross-references EMBL:Z19005; NID:g40561; PIDN:CAA79492.1; !1PID:g40563 REFERENCE S34627 !$#authors Meyer, J. !$#journal Biochim. Biophys. Acta (1993) 1174:108-110 !$#title Cloning and sequencing of the gene encoding the [2Fe-2S] !1ferredoxin from Clostridium pasteurianum. !$#cross-references MUID:93326627; PMID:8334159 !$#accession S34628 !'##molecule_type DNA !'##residues 1-102 ##label ME2 !'##cross-references EMBL:Z19005; NID:g40561; PIDN:CAA79492.1; !1PID:g40563 REFERENCE A24460 !$#authors Meyer, J.; Bruschi, M.H.; Bonicel, J.J.; Bovier-Lapierre, !1G.E. !$#journal Biochemistry (1986) 25:6054-6061 !$#title Amino acid sequence of [2Fe-2S] ferredoxin from Clostridium !1pasteurianum. !$#cross-references MUID:87076518; PMID:3790505 !$#accession A24460 !'##molecule_type protein !'##residues 1-102 ##label MEY REFERENCE A55988 !$#authors Meyer, J.; Fujinaga, J.; Gaillard, J.; Lutz, M. !$#journal Biochemistry (1994) 33:13642-13650 !$#title Mutated forms of the [2Fe-2S] ferredoxin from Clostridium !1pasteurianum with noncysteinyl ligands to the iron-sulfur !1cluster. !$#cross-references MUID:95034798; PMID:7947772 !$#contents annotation; iron-sulfur cluster ligands !$#note Cys-14 is not a ligand for the iron-sulfur cluster; the !1fourth ligand was not determined REFERENCE A58991 !$#authors Golinelli, M.P.; Akin, L.A.; Crouse, B.R.; Johnson, M.K.; !1Meyer, J. !$#journal Biochemistry (1996) 35:8995-9002 !$#title Cysteine ligand swapping on a deletable loop of the [2Fe-2S] !1ferredoxin from Clostridium pasteurianum. !$#cross-references MUID:96280659; PMID:8688437 !$#contents annotation; iron-sulfur cluster ligands COMMENT Cys-24 is normally a ligand for the 2Fe-2S cluster. The !1binding loop is sufficiently flexible for Cys-14 also to !1serve as a ligand when Cys-24 is converted to Ala by !1mutagenesis. CLASSIFICATION #superfamily Clostridium ferredoxin [2Fe-2S] KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$11,24,56,60 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8experimental SUMMARY #length 102 #molecular-weight 11428 #checksum 6066 SEQUENCE /// ENTRY JC7085 #type complete TITLE ferredoxin [2Fe-2S] fdx4 [validated] - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS JC7085; D70310 REFERENCE JC7085 !$#authors Chatelet, C.; Gaillard, J.; Petillot, Y.; Louwagie, M.; !1Meyer, J. !$#journal Biochem. Biophys. Res. Commun. (1999) 261:885-889 !$#title A [2Fe-2S] protein from the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:99373173; PMID:10441520 !$#accession JC7085 !'##molecule_type DNA !'##residues 1-111 ##label CHA !'##note this corrects the sequence in reference A70300; a C is inserted !1in nucleotide sequence GB:AE000674 after position 151 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession D70310 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 47-111 ##label AQF !'##cross-references GB:AE000674; NID:g2982850; PIDN:AAC06474.1; !1PID:g2982853; GB:AE000657 !'##experimental_source strain VF5 !'##note this predicted open reading frame is incomplete at the amino !1end compared with other members of the superfamily !'##note this sequence is corrected in reference JC7085 GENETICS !$#gene fdx4 CLASSIFICATION #superfamily Clostridium ferredoxin [2Fe-2S] KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$2-111 #product ferredoxin [2Fe-2S] fdx4 #status predicted !8#label MAT\ !$10,23,56,60 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 111 #molecular-weight 12323 #checksum 287 SEQUENCE /// ENTRY FEHS #type complete TITLE ferredoxin [2Fe-2S] [validated] - Halobacterium salinarum ORGANISM #formal_name Halobacterium salinarum DATE 24-Apr-1984 #sequence_revision 10-Oct-1997 #text_change 28-Jan-2000 ACCESSIONS S35235; A00220 REFERENCE S35235 !$#authors Pfeifer, F.; Griffig, J.; Oesterhelt, D. !$#journal Mol. Gen. Genet. (1993) 239:66-71 !$#title The fdx gene encoding the [2Fe-2S] ferredoxin of !1Halobacterium salinarium (H. halobium). !$#cross-references MUID:93288008; PMID:8510664 !$#accession S35235 !'##molecule_type DNA !'##residues 1-129 ##label PFE !'##cross-references EMBL:X68103; NID:g311840; PIDN:CAA48224.1; !1PID:g311841 !'##experimental_source strain R1 !'##note the source is designated as Halobacterium salinarium (H. !1halobium) REFERENCE A00220 !$#authors Hase, T.; Wakabayashi, S.; Matsubara, H.; Kerscher, L.; !1Oesterhelt, D.; Rao, K.K.; Hall, D.O. !$#journal J. Biochem. (1978) 83:1657-1670 !$#title Complete amino acid sequence of Halobacterium halobium !1ferredoxin containing an N(epsilon)-acetyllysine residue. !$#cross-references MUID:78218096; PMID:670159 !$#accession A00220 !'##molecule_type protein !'##residues 2-129 ##label HAS !'##experimental_source NRL R1 strain M1 !'##note the source is designated as Halobacterium halobium GENETICS !$#gene fdx FUNCTION !$#description redox cofactor for various oxidoreductases [validated, !1MUID:78218096] CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; acetyllysine; electron transfer; iron-sulfur !1protein; metalloprotein FEATURE !$2-129 #product ferredoxin [2Fe-2S] #status experimental !8#label MAT\ !$49-104 #domain ferredoxin [2Fe-2S] homology #label FER\ !$64,69,72,103 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted\ !$119 #binding_site acetyl (Lys) (covalent) #status !8experimental SUMMARY #length 129 #molecular-weight 14418 #checksum 1686 SEQUENCE /// ENTRY FEHSX #type complete TITLE ferredoxin [2Fe-2S] [validated] - Haloarcula marismortui ORGANISM #formal_name Haloarcula marismortui DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 23-Mar-2001 ACCESSIONS A00221 REFERENCE A00221 !$#authors Hase, T.; Wakabayashi, S.; Matsubara, H.; Mevarech, M.; !1Werber, M.M. !$#journal Biochim. Biophys. Acta (1980) 623:139-145 !$#title Amino acid sequence of 2Fe-2S ferredoxin from an extreme !1halophile, Halobacterium of the Dead Sea. !$#cross-references MUID:80198519; PMID:7378468 !$#accession A00221 !'##molecule_type protein !'##residues 1-128 ##label HAS !'##note the source is designated as Halobacterium sp. from the Dead Sea REFERENCE A65442 !$#authors Frolow, F.; Harel, M.; Sussman, J.L.; Shoham, M. !$#submission submitted to the Brookhaven Protein Data Bank, April 1996 !$#cross-references PDB:1DOI !$#contents annotation; X-ray crystallography, 1.9 angstroms, residues !11-128 REFERENCE A58606 !$#authors Frolow, F.; Harel, M.; Sussman, J.L.; Mevarech, M.; Shoham, !1M. !$#journal Nat. Struct. Biol. (1996) 3:452-458 !$#title Insights into protein adaptation to a saturated salt !1environment from the crystal structure of a halophilic !12Fe-2S ferredoxin. !$#cross-references MUID:96196882; PMID:8612076 !$#contents annotation; X-ray crystallography, 1.9 angstroms REFERENCE A26031 !$#authors Sussman, J.L.; Brown, J.H.; Shoham, M. !$#book Iron-Sulfur Protein Research, Matsubara, H., et al., eds., !1pp.69-82, Japan Sci. Soc. Press, Tokyo, 1986 !$#title X-ray structural studies on a salt-loving ferredoxin from !1Halobacterium of the Dead Sea. !$#contents annotation; X-ray crystallography, 2.2 angstroms FUNCTION !$#description redox cofactor for various oxidoreductases [validated, !1MUID:80198519] CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; acetyllysine; electron transfer; iron-sulfur !1protein; metalloprotein FEATURE !$1-128 #product ferredoxin [2Fe-2S] #status experimental !8#label MAT\ !$48-103 #domain ferredoxin [2Fe-2S] homology #label FER\ !$63,68,71,102 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8experimental\ !$118 #binding_site acetyl (Lys) (covalent) #status !8experimental SUMMARY #length 128 #molecular-weight 14406 #checksum 4042 SEQUENCE /// ENTRY B39181 #type complete TITLE ferredoxin [2Fe-2S]-like protein nahG-nahH intergenic region - Pseudomonas putida (strain PpG7) ORGANISM #formal_name Pseudomonas putida DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Dec-1999 ACCESSIONS B39181; S16368 REFERENCE A39181 !$#authors You, I.S.; Ghosal, D.; Gunsalus, I.C. !$#journal Biochemistry (1991) 30:1635-1641 !$#title Nucleotide sequence analysis of the Pseudomonas putida PpG7 !1salicylate hydroxylase gene (nahG) and its 3'-flanking !1region. !$#cross-references MUID:91129237; PMID:1993181 !$#accession B39181 !'##molecule_type DNA !'##residues 1-108 ##label YOU !'##cross-references GB:M60055; GB:J05317; NID:g151380; PIDN:AAA25898.1; !1PID:g151382 REFERENCE S16193 !$#authors Harayama, S.; Polissi, A.; Rekik, M. !$#journal FEBS Lett. (1991) 285:85-88 !$#title Divergent evolution of chloroplast-type ferredoxins. !$#cross-references MUID:91293320; PMID:2065785 !$#accession S16368 !'##molecule_type DNA !'##residues 1-108 ##label HAR !'##cross-references GB:X61466; GB:S40145; NID:g311896; PIDN:CAA43701.1; !1PID:g311897 CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$24-81 #domain ferredoxin [2Fe-2S] homology #label FER\ !$40,45,48,80 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 108 #molecular-weight 11913 #checksum 6136 SEQUENCE /// ENTRY S54762 #type complete TITLE ferredoxin [2Fe-2S]-like protein phlG - Pseudomonas putida ORGANISM #formal_name Pseudomonas putida DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Dec-1999 ACCESSIONS S54762; B58972; S44309; S47420 REFERENCE S54761 !$#authors Herrmann, H.; Mueller, C.; Schmidt, I.; Mahnke, J.; !1Petruschka, L.; Hahnke, K. !$#journal Mol. Gen. Genet. (1995) 247:240-246 !$#title Localization and organization of phenol degradation genes of !1Pseudomonas putida strain H. !$#cross-references MUID:95272534; PMID:7753034 !$#accession S54762 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-101 ##label HER !'##cross-references EMBL:X80765; NID:g527546; PIDN:CAA56746.1; !1PID:g527553 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1994 REFERENCE A58972 !$#authors Ng, L.C.; Shingler, V.; Sze, C.C.; Poh, C.L. !$#journal Gene (1994) 151:29-36 !$#title Cloning and sequences of the first eight genes of the !1chromosomally encoded (methyl) phenol degradation pathway !1from Pseudomonas putida P35X. !$#cross-references MUID:95129877; PMID:7828892 !$#accession B58972 !'##molecule_type DNA !'##residues 1-72,'GE',75-101 ##label NGL !'##cross-references EMBL:X79063; NID:g483477; PIDN:CAA55666.1; !1PID:g483484 !'##experimental_source strain P35X (NCBI 9869) !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1994 GENETICS !$#gene phlG CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$25-82 #domain ferredoxin [2Fe-2S] homology #label FER\ !$41,46,49,81 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 101 #molecular-weight 10978 #checksum 2160 SEQUENCE /// ENTRY S24417 #type complete TITLE ferredoxin [2Fe-2S]-like protein dmpQ - Pseudomonas putida ORGANISM #formal_name Pseudomonas putida DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Dec-1999 ACCESSIONS S24417 REFERENCE S24417 !$#authors Shingler, V.; Powlowski, J.; Marklund, U. !$#journal J. Bacteriol. (1992) 174:711-724 !$#title Nucleotide sequence and functional analysis of the complete !1phenol/3,4-dimethylphenol catabolic pathway of Pseudomonas !1sp. strain CF600. !$#cross-references MUID:92121108; PMID:1732207 !$#accession S24417 !'##molecule_type DNA !'##residues 1-112 ##label SHI !'##cross-references EMBL:X60657; NID:g45687; PIDN:CAA43064.1; !1PID:g45688 GENETICS !$#gene dmpQ CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$25-82 #domain ferredoxin [2Fe-2S] homology #label FER\ !$41,46,49,81 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 112 #molecular-weight 12222 #checksum 3869 SEQUENCE /// ENTRY S16193 #type complete TITLE ferredoxin [2Fe-2S]-like protein xylT - Pseudomonas putida plasmid pWW0 ORGANISM #formal_name Pseudomonas putida DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Dec-1999 ACCESSIONS S16193; S23486 REFERENCE S16193 !$#authors Harayama, S.; Polissi, A.; Rekik, M. !$#journal FEBS Lett. (1991) 285:85-88 !$#title Divergent evolution of chloroplast-type ferredoxins. !$#cross-references MUID:91293320; PMID:2065785 !$#accession S16193 !'##molecule_type DNA !'##residues 1-112 ##label HAR !'##cross-references EMBL:X61467; NID:g311898; PIDN:CAA43702.1; !1PID:g311899 REFERENCE S23477 !$#authors Neidle, E.L.; Hartnett, C.; Ornston, L.N.; Bairoch, A.; !1Rekik, M.; Harayama, S. !$#journal Eur. J. Biochem. (1992) 204:113-120 !$#title Cis-diol dehydrogenases encoded by the TOL pWW0 plasmid xylL !1gene and the Acinetobacter calcoaceticus chromosomal benD !1gene are members of the short-chain alcohol dehydrogenase !1superfamily. !$#cross-references MUID:92155191; PMID:1740120 !$#accession S23486 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-112 ##label NEI !'##cross-references EMBL:M64747; NID:g151718; PIDN:AAA26051.1; !1PID:g151723 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1March 1992 GENETICS !$#gene xylT !$#genome plasmid pWW0 CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$25-82 #domain ferredoxin [2Fe-2S] homology #label FER\ !$41,46,49,81 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 112 #molecular-weight 12034 #checksum 2066 SEQUENCE /// ENTRY FEPM1 #type complete TITLE ferredoxin [2Fe-2S] I precursor - garden pea ORGANISM #formal_name Pisum sativum #common_name garden pea DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 11-Jun-1999 ACCESSIONS S11495; S06468; S07445 REFERENCE S11495 !$#authors Elliott, R.C.; Pedersen, T.J.; Fristensky, B.; White, M.J.; !1Dickey, L.F.; Thompson, W.F. !$#journal Plant Cell (1989) 1:681-690 !$#title Characterization of a single copy gene encoding ferredoxin I !1from pea. !$#cross-references MUID:92393406; PMID:2535518 !$#accession S11495 !'##molecule_type DNA !'##residues 1-149 ##label ELI !'##cross-references GB:M31713; EMBL:X14207; NID:g169086; !1PIDN:AAA33665.1; PID:g169087 REFERENCE S06468 !$#authors Dobres, M.S.; Elliott, R.C.; Watson, J.C.; Thompson, W.F. !$#journal Plant Mol. Biol. (1987) 8:53-59 !$#title A phytochrome regulated pea transcript encodes ferredoxin I. !$#accession S06468 !'##molecule_type mRNA !'##residues 31-130 ##label DOB !'##cross-references EMBL:M17107 REFERENCE S07445 !$#authors Dutton, J.E.; Rogers, L.J.; Haslett, B.G.; Takruri, I.A.H.; !1Gleaves, J.T.; Boulter, D. !$#journal J. Exp. Bot. (1980) 31:379-391 !$#title Comparative studies on the properties of two ferredoxins !1from Pisum sativum L. !$#accession S07445 !'##molecule_type protein !'##residues 53-58,'I',60-84,'L',86-92 ##label DUT GENETICS !$#gene FedI CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; chloroplast; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-52 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$53-149 #product ferredoxin [2Fe-2S] #status experimental !8#label MAT\ !$76-130 #domain ferredoxin [2Fe-2S] homology #label FER\ !$91,96,99,129 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 149 #molecular-weight 15804 #checksum 9719 SEQUENCE /// ENTRY FESP1 #type complete TITLE ferredoxin [2Fe-2S] I precursor - spinach ORGANISM #formal_name Spinacia oleracea #common_name spinach DATE 13-Jun-1983 #sequence_revision 31-Mar-1992 #text_change 11-Jun-1999 ACCESSIONS S00437; A00228; S13386 REFERENCE S00437 !$#authors Wedel, N.; Bartling, D.; Herrmann, R.G. !$#journal Bot. Acta (1988) 101:295-300 !$#title Analysis of cDNA clones encoding the entire ferredoxin I !1precursor polypeptide from spinach. !$#accession S00437 !'##molecule_type mRNA !'##residues 1-147 ##label WED !'##cross-references GB:M35660; NID:g170108; PIDN:AAA34028.1; !1PID:g170109 REFERENCE A00228 !$#authors Matsubara, H.; Sasaki, R.M. !$#journal J. Biol. Chem. (1968) 243:1732-1757 !$#title Spinach ferredoxin. II. Tryptic, chymotryptic, and !1thermolytic peptides, and complete amino acid sequence. !$#cross-references MUID:68243193; PMID:5651327 !$#accession A00228 !'##molecule_type protein !'##residues 51-147 ##label MATS !'##note there may be variants with 81-Lys and 83-Met and a possible !1deletion of 141-Lys REFERENCE S13274 !$#authors Morigasaki, S.; Takata, K.; Sanada, Y.; Wada, K.; Yee, B.C.; !1Shin, S.; Buchanan, B.B. !$#journal Arch. Biochem. Biophys. (1990) 283:75-80 !$#title Novel forms of ferredoxin and ferredoxin-NADP reductase from !1spinach roots. !$#cross-references MUID:91053194; PMID:2241175 !$#accession S13386 !'##molecule_type protein !'##residues 51-69 ##label MOR !'##experimental_source leaf CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; chloroplast; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-50 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$51-147 #product ferredoxin [2Fe-2S] I #status experimental !8#label MAT\ !$74-128 #domain ferredoxin [2Fe-2S] homology #label FER\ !$89,94,97,127 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 147 #molecular-weight 15658 #checksum 3711 SEQUENCE /// ENTRY FESP2 #type complete TITLE ferredoxin [2Fe-2S] II - spinach ORGANISM #formal_name Spinacia oleracea #common_name spinach DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 13-Nov-1998 ACCESSIONS A00231 REFERENCE A00231 !$#authors Takahashi, Y.; Hase, T.; Wada, K.; Matsubara, H. !$#journal Plant Cell Physiol. (1983) 24:189-198 !$#title Ferredoxins in developing spinach cotyledons: the presence !1of two molecular species. !$#accession A00231 !'##molecule_type protein !'##residues 1-97 ##label TAK !'##experimental_source cv. Munstarlander CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-97 #product ferredoxin [2Fe-2S] II #status experimental !8#label MAT\ !$24-78 #domain ferredoxin [2Fe-2S] homology #label FER\ !$39,44,47,77 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 97 #molecular-weight 10334 #checksum 5740 SEQUENCE /// ENTRY FELG #type complete TITLE ferredoxin [2Fe-2S] - white popinac (tentative sequence) ORGANISM #formal_name Leucaena leucocephala #common_name white popinac DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 31-Mar-2000 ACCESSIONS A92055; A93771; A00232 REFERENCE A92055 !$#authors Benson, A.M.; Yasunobu, K.T. !$#journal J. Biol. Chem. (1969) 244:955-963 !$#title Non-heme iron proteins. X. The amino acid sequences of !1ferredoxins from Leucaena glauca. !$#cross-references MUID:69184140; PMID:5769192 !$#accession A92055 !'##molecule_type protein !'##residues 1-96 ##label BEN !'##note sequence heterogeneity in several positions: Glu and Asp at !1position 33, Gly and Ala at position 96, and either 6-Leu !1and 12-Pro or 6-Val and 12-Ala REFERENCE A93771 !$#authors Benson, A.M.; Yasunobu, K.T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1969) 63:1269-1273 !$#title Nonheme iron proteins, XI. Some genetic aspects. !$#cross-references MUID:70050801; PMID:5260930 !$#accession A93771 !'##molecule_type protein !'##residues 1-96 ##label BE2 !'##note ferredoxin from individual trees was analyzed; half of the !1molecules contained 6-Leu and 12-Pro, and the other half !1contained 6-Val and 12-Ala; 66% 96-Gly and 34% 96-Ala were !1also found CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-96 #product ferredoxin [2Fe-2S] #status experimental !8#label MAT\ !$23-77 #domain ferredoxin [2Fe-2S] homology #label FER\ !$38,43,46,76 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 96 #molecular-weight 10588 #checksum 1756 SEQUENCE /// ENTRY FEED #type complete TITLE ferredoxin [2Fe-2S] - European elder (tentative sequence) ORGANISM #formal_name Sambucus nigra #common_name European elder DATE 30-Apr-1980 #sequence_revision 30-Apr-1980 #text_change 31-Mar-2000 ACCESSIONS A00233 REFERENCE A00233 !$#authors Takruri, I.A.H.; Boulter, D. !$#journal Phytochemistry (1979) 18:1481-1484 !$#title The amino acid sequence of ferredoxin from Sambucus nigra. !$#accession A00233 !'##molecule_type protein !'##residues 1-97 ##label TAK !'##note the amidation states of residues 57, 58, 60, 61, 68, and 88 !1were identified by homology with other ferredoxin sequences CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-97 #product ferredoxin [2Fe-2S] #status experimental !8#label MAT\ !$24-78 #domain ferredoxin [2Fe-2S] homology #label FER\ !$39,44,47,77 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 97 #molecular-weight 10616 #checksum 5325 SEQUENCE /// ENTRY FETA #type complete TITLE ferredoxin [2Fe-2S] - taro (tentative sequence) ORGANISM #formal_name Colocasia esculenta #common_name taro DATE 24-Apr-1984 #sequence_revision 30-Sep-1988 #text_change 31-Mar-2000 ACCESSIONS A00229 REFERENCE A00229 !$#authors Rao, K.K.; Matsubara, H. !$#journal Biochem. Biophys. Res. Commun. (1970) 38:500-506 !$#title The amino acid sequence of taro ferredoxin. !$#cross-references MUID:70181822; PMID:5443697 !$#accession A00229 !'##molecule_type protein !'##residues 1-97 ##label RAO CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-97 #product ferredoxin [2Fe-2S] #status experimental !8#label MAT\ !$24-78 #domain ferredoxin [2Fe-2S] homology #label FER\ !$39,44,47,77 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 97 #molecular-weight 10437 #checksum 6512 SEQUENCE /// ENTRY FERP #type complete TITLE ferredoxin [2Fe-2S] - rape ORGANISM #formal_name Brassica napus #common_name rape DATE 28-Feb-1980 #sequence_revision 28-Feb-1980 #text_change 13-Nov-1998 ACCESSIONS A00234 REFERENCE A00234 !$#authors Takruri, I.; Boulter, D. !$#journal Biochem. J. (1980) 185:239-243 !$#title The amino acid sequence of ferredoxin from Brassica napus !1(rape). !$#cross-references MUID:80197725; PMID:7378049 !$#accession A00234 !'##molecule_type protein !'##residues 1-96 ##label TAK CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-96 #product ferredoxin [2Fe-2S] #status experimental !8#label MAT\ !$24-78 #domain ferredoxin [2Fe-2S] homology #label FER\ !$39,44,47,77 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 96 #molecular-weight 10367 #checksum 2671 SEQUENCE /// ENTRY FEAA #type complete TITLE ferredoxin [2Fe-2S] - alfalfa ORGANISM #formal_name Medicago sativa #common_name alfalfa DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 13-Nov-1998 ACCESSIONS A00227 REFERENCE A00227 !$#authors Keresztes-Nagy, S.; Perini, F.; Margoliash, E. !$#journal J. Biol. Chem. (1969) 244:981-995 !$#title Primary structure of alfalfa ferredoxin. !$#cross-references MUID:69184143; PMID:5769194 !$#accession A00227 !'##molecule_type protein !'##residues 1-97 ##label KER CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-97 #product ferredoxin [2Fe-2S] #status experimental !8#label MAT\ !$24-78 #domain ferredoxin [2Fe-2S] homology #label FER\ !$39,44,47,77 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 97 #molecular-weight 10493 #checksum 4774 SEQUENCE /// ENTRY FEBQ #type complete TITLE ferredoxin [2Fe-2S] - great burdock ORGANISM #formal_name Arctium lappa #common_name great burdock DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 13-Nov-1998 ACCESSIONS A00230 REFERENCE A00230 !$#authors Takruri, I.A.H.; Gilroy, J.; Boulter, D. !$#journal Phytochemistry (1982) 21:325-327 !$#title Amino acid sequence of ferredoxin from Arctium lappa. !$#accession A00230 !'##molecule_type protein !'##residues 1-97 ##label TAK !'##note 63-Phe was also found CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-97 #product ferredoxin [2Fe-2S] #status experimental !8#label MAT\ !$24-78 #domain ferredoxin [2Fe-2S] homology #label FER\ !$39,44,47,77 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 97 #molecular-weight 10425 #checksum 6516 SEQUENCE /// ENTRY FEQH #type complete TITLE ferredoxin [2Fe-2S] precursor - white campion ORGANISM #formal_name Silene pratensis, Lychnis alba #common_name white campion, evening lychnis DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 11-Jun-1999 ACCESSIONS A23011 REFERENCE A23011 !$#authors Smeekens, S.; van Binsbergen, J.; Weisbeek, P. !$#journal Nucleic Acids Res. (1985) 13:3179-3194 !$#title The plant ferredoxin precursor: nucleotide sequence of a !1full length cDNA clone. !$#cross-references MUID:85215678; PMID:2987875 !$#accession A23011 !'##molecule_type mRNA !'##residues 1-146 ##label SME !'##cross-references GB:X02432; NID:g21361; PIDN:CAA26281.1; PID:g21362 CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; chloroplast; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-48 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$49-146 #product ferredoxin [2Fe-2S] #status predicted #label !8MAT\ !$73-127 #domain ferredoxin [2Fe-2S] homology #label FER\ !$88,93,96,126 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 146 #molecular-weight 15351 #checksum 2501 SEQUENCE /// ENTRY FEWT #type complete TITLE ferredoxin [2Fe-2S] precursor - wheat ORGANISM #formal_name Triticum aestivum #common_name common wheat DATE 30-Jun-1979 #sequence_revision 19-May-1995 #text_change 07-Dec-1999 ACCESSIONS S52993; A00235; S37226 REFERENCE S52993 !$#authors Bringloe, D.H.; Dyer, T.A.; Gray, J.C. !$#journal Plant Mol. Biol. (1995) 27:293-306 !$#title Developmental, circadian and light regulation of wheat !1ferredoxin gene expression. !$#cross-references MUID:95195157; PMID:7888619 !$#accession S52993 !'##molecule_type DNA !'##residues 1-143 ##label BR2 !'##cross-references EMBL:X75089; NID:g403032; PIDN:CAA52980.1; !1PID:g403033 !'##experimental_source leaf !'##note submitted to the EMBL Data Library, August 1993 REFERENCE A00235 !$#authors Takruri, I.; Boulter, D. !$#journal Biochem. J. (1979) 179:373-378 !$#title The amino acid sequence of ferredoxin from Triticum aestivum !1(wheat). !$#cross-references MUID:80020138; PMID:486088 !$#accession A00235 !'##molecule_type protein !'##residues 47-143 ##label TAK GENETICS !$#gene petF FUNCTION !$#description multifunctional electron carrier CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-46 #domain transit peptide (chloroplast) #status !8predicted #label SIG\ !$47-143 #product ferredoxin [2Fe-2S] #status experimental !8#label MAT\ !$70-124 #domain ferredoxin [2Fe-2S] homology #label FER\ !$85,90,93,123 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 143 #molecular-weight 15286 #checksum 1818 SEQUENCE /// ENTRY FERZ #type complete TITLE ferredoxin [2Fe-2S] I precursor - rice ORGANISM #formal_name Oryza sativa #common_name rice DATE 31-Mar-1989 #sequence_revision 28-May-1999 #text_change 16-Jun-2000 ACCESSIONS T03738; S03730; JT0223 REFERENCE Z15043 !$#authors Ohmori, K.; Doyama, N.; Ida, S. !$#journal Plant Physiol. (1996) 111:348 !$#title Molecular cloning of a rice leaf ferredoxin cDNA. !$#accession T03738 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-139 ##label OHM !'##cross-references EMBL:D30763; PIDN:BAA06436.1 !'##experimental_source subsp. Japonica, cv. Kinmaze REFERENCE S03730 !$#authors Kamo, M.; Kotani, N.; Tsugita, A.; He, Y.K.; Nozu, Y. !$#journal Protein Seq. Data Anal. (1989) 2:289-293 !$#title Amino acid sequences of ferredoxins from rice cultivars, !1japonica and indica. !$#cross-references MUID:89367259; PMID:2771933 !$#accession S03730 !'##molecule_type protein !'##residues 44-139 ##label KAM !'##note sequences from cultivars japonica and indica are identical CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$44-139 #product ferredoxin [2Fe-2S] I #status experimental !8#label MAT\ !$67-121 #domain ferredoxin [2Fe-2S] homology #label FER\ !$82,87,90,120 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 139 #molecular-weight 14951 #checksum 5480 SEQUENCE /// ENTRY FEFW1 #type complete TITLE ferredoxin [2Fe-2S] I - Virginian pokeweed ORGANISM #formal_name Phytolacca americana #common_name Virginian pokeweed DATE 30-Jun-1979 #sequence_revision 23-Oct-1981 #text_change 13-Nov-1998 ACCESSIONS A00236 REFERENCE A00236 !$#authors Wakabayashi, S.; Hase, T.; Wada, K.; Matsubara, H.; Suzuki, !1K.; Takaichi, S. !$#journal J. Biochem. (1978) 83:1305-1319 !$#title Amino acid sequences of two ferredoxins from pokeweed, !1Phytolacca americana. !$#cross-references MUID:78194079; PMID:659398 !$#accession A00236 !'##molecule_type protein !'##residues 1-96 ##label WAK CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-96 #product ferredoxin [2Fe-2S] I #status experimental !8#label MAT\ !$24-78 #domain ferredoxin [2Fe-2S] homology #label FER\ !$39,44,47,77 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 96 #molecular-weight 10184 #checksum 3459 SEQUENCE /// ENTRY FEFWF #type complete TITLE ferredoxin [2Fe-2S] I - food pokeweed ORGANISM #formal_name Phytolacca esculenta #common_name food pokeweed DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 13-Nov-1998 ACCESSIONS B00238; A00236 REFERENCE A00238 !$#authors Wakabayashi, S.; Hase, T.; Wada, K.; Matsubara, H.; Suzuki, !1K. !$#journal J. Biochem. (1980) 87:227-236 !$#title Amino acid sequences of two ferredoxins from Phytolacca !1esculenta. Gene duplication and speciation. !$#cross-references MUID:80137361; PMID:7358632 !$#accession B00238 !'##molecule_type protein !'##residues 1-96 ##label WAK !'##note 48-Ala and 96-Ala were also found CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-96 #product ferredoxin [2Fe-2S] I #status experimental !8#label MAT\ !$24-78 #domain ferredoxin [2Fe-2S] homology #label FER\ !$39,44,47,77 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 96 #molecular-weight 10200 #checksum 3896 SEQUENCE /// ENTRY FEFW2 #type complete TITLE ferredoxin [2Fe-2S] II - Virginian pokeweed ORGANISM #formal_name Phytolacca americana #common_name Virginian pokeweed DATE 30-Jun-1979 #sequence_revision 30-Jun-1979 #text_change 13-Nov-1998 ACCESSIONS A00237 REFERENCE A00236 !$#authors Wakabayashi, S.; Hase, T.; Wada, K.; Matsubara, H.; Suzuki, !1K.; Takaichi, S. !$#journal J. Biochem. (1978) 83:1305-1319 !$#title Amino acid sequences of two ferredoxins from pokeweed, !1Phytolacca americana. !$#cross-references MUID:78194079; PMID:659398 !$#accession A00237 !'##molecule_type protein !'##residues 1-98 ##label WAK CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-98 #product ferredoxin [2Fe-2S] II #status experimental !8#label MAT\ !$25-79 #domain ferredoxin [2Fe-2S] homology #label FER\ !$40,45,48,78 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 98 #molecular-weight 10262 #checksum 8867 SEQUENCE /// ENTRY FEFW2E #type complete TITLE ferredoxin [2Fe-2S] II - food pokeweed ORGANISM #formal_name Phytolacca esculenta #common_name food pokeweed DATE 31-Aug-1980 #sequence_revision 31-Aug-1980 #text_change 13-Nov-1998 ACCESSIONS A00238 REFERENCE A00238 !$#authors Wakabayashi, S.; Hase, T.; Wada, K.; Matsubara, H.; Suzuki, !1K. !$#journal J. Biochem. (1980) 87:227-236 !$#title Amino acid sequences of two ferredoxins from Phytolacca !1esculenta. Gene duplication and speciation. !$#cross-references MUID:80137361; PMID:7358632 !$#accession A00238 !'##molecule_type protein !'##residues 1-98 ##label WAK CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-98 #product ferredoxin [2Fe-2S] II #status experimental !8#label MAT\ !$25-79 #domain ferredoxin [2Fe-2S] homology #label FER\ !$40,45,48,78 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 98 #molecular-weight 10264 #checksum 9782 SEQUENCE /// ENTRY FEFNG #type complete TITLE ferredoxin [2Fe-2S] - fern (Gleichenia japonica) (tentative sequence) ORGANISM #formal_name Gleichenia japonica #common_name urajiro DATE 06-Jul-1982 #sequence_revision 30-Sep-1988 #text_change 31-Mar-2000 ACCESSIONS A00239 REFERENCE A00239 !$#authors Hase, T.; Yamanashi, H.; Matsubara, H. !$#journal J. Biochem. (1982) 91:341-346 !$#title Purification and amino acid sequence of a fern (Gleichenia !1japonica) ferredoxin. !$#cross-references MUID:82167301; PMID:7068564 !$#accession A00239 !'##molecule_type protein !'##residues 1-95 ##label HAS CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-95 #product ferredoxin [2Fe-2S] #status experimental !8#label MAT\ !$24-78 #domain ferredoxin [2Fe-2S] homology #label FER\ !$39,44,47,77 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 95 #molecular-weight 10289 #checksum 7372 SEQUENCE /// ENTRY FEEQ1 #type complete TITLE ferredoxin [2Fe-2S] I - horsetail (Equisetum telmateia) ORGANISM #formal_name Equisetum telmateia DATE 30-Jun-1979 #sequence_revision 08-Oct-1981 #text_change 13-Nov-1998 ACCESSIONS A00240 REFERENCE A00240 !$#authors Hase, T.; Wada, K.; Matsubara, H. !$#journal J. Biochem. (1977) 82:267-276 !$#title Horsetail (Equisetum telmateia) ferredoxins I and II. !$#cross-references MUID:77249491; PMID:893383 !$#accession A00240 !'##molecule_type protein !'##residues 1-95 ##label HAS CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-95 #product ferredoxin [2Fe-2S] I #status experimental !8#label MAT\ !$23-77 #domain ferredoxin [2Fe-2S] homology #label FER\ !$38,43,46,76 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 95 #molecular-weight 10097 #checksum 9423 SEQUENCE /// ENTRY FEEQ1F #type complete TITLE ferredoxin [2Fe-2S] I [validated] - field horsetail ORGANISM #formal_name Equisetum arvense #common_name field horsetail DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 15-Sep-2000 ACCESSIONS A04609; A00240 REFERENCE A04609 !$#authors Hase, T.; Wada, K.; Matsubara, H. !$#journal J. Biochem. (1977) 82:277-286 !$#title Horsetail (Equisetum arvense) ferredoxins I and II. !$#cross-references MUID:77249492; PMID:893384 !$#accession A04609 !'##molecule_type protein !'##residues 1-95 ##label HAS REFERENCE A51728 !$#authors Tsukihara, T. !$#submission submitted to the Brookhaven Protein Data Bank, September !11993 !$#cross-references PDB:1FRR !$#contents annotation; X-ray crystallography, 1.8 angstroms, residues !11-95 CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-95 #product ferredoxin [2Fe-2S] I #status experimental !8#label MAT\ !$23-77 #domain ferredoxin [2Fe-2S] homology #label FER\ !$38,43,46,76 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8experimental SUMMARY #length 95 #molecular-weight 10098 #checksum 8739 SEQUENCE /// ENTRY FEEQ2 #type complete TITLE ferredoxin [2Fe-2S] II - horsetail (Equisetum telmateia) ORGANISM #formal_name Equisetum telmateia DATE 30-Jun-1979 #sequence_revision 08-Oct-1981 #text_change 13-Nov-1998 ACCESSIONS A00241 REFERENCE A00240 !$#authors Hase, T.; Wada, K.; Matsubara, H. !$#journal J. Biochem. (1977) 82:267-276 !$#title Horsetail (Equisetum telmateia) ferredoxins I and II. !$#cross-references MUID:77249491; PMID:893383 !$#accession A00241 !'##molecule_type protein !'##residues 1-93 ##label HAS CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-93 #product ferredoxin [2Fe-2S] II #status experimental !8#label MAT\ !$23-76 #domain ferredoxin [2Fe-2S] homology #label FER\ !$37,42,45,75 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 93 #molecular-weight 9976 #checksum 4375 SEQUENCE /// ENTRY FEEQ2F #type complete TITLE ferredoxin [2Fe-2S] II - field horsetail ORGANISM #formal_name Equisetum arvense #common_name field horsetail DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 13-Nov-1998 ACCESSIONS B04609; A00241 REFERENCE A04609 !$#authors Hase, T.; Wada, K.; Matsubara, H. !$#journal J. Biochem. (1977) 82:277-286 !$#title Horsetail (Equisetum arvense) ferredoxins I and II. !$#cross-references MUID:77249492; PMID:893384 !$#accession B04609 !'##molecule_type protein !'##residues 1-93 ##label HAS CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-93 #product ferredoxin [2Fe-2S] II #status experimental !8#label MAT\ !$23-76 #domain ferredoxin [2Fe-2S] homology #label FER\ !$37,42,45,75 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 93 #molecular-weight 9962 #checksum 4537 SEQUENCE /// ENTRY FEPRR #type complete TITLE ferredoxin [2Fe-2S] - red alga (Palmaria palmata) ORGANISM #formal_name Palmaria palmata #common_name dulse DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 13-Nov-1998 ACCESSIONS A93760; A93759; JT0018 REFERENCE A93760 !$#authors Inoue, K.; Hase, T.; Matsubara, H.; Fitzgerald, M.P.; !1Rogers, L.J. !$#journal Phytochemistry (1984) 23:773-776 !$#title Amino acid sequence of a ferredoxin from Rhodymenia palmata, !1a red alga in the Florideophyceae. !$#accession A93760 !'##molecule_type protein !'##residues 1-97 ##label INO REFERENCE A93759 !$#authors Andrew, P.W.; Rogers, L.J.; Haslett, B.G.; Boulter, D. !$#journal Phytochemistry (1981) 20:579-583 !$#title Partial structure and properties of the ferredoxin from !1Rhodymenia palmata. !$#accession A93759 !'##molecule_type protein !'##residues 1-48 ##label AND CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-97 #product ferredoxin [2Fe-2S] #status experimental !8#label MAT\ !$25-79 #domain ferredoxin [2Fe-2S] homology #label FER\ !$40,45,48,78 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 97 #molecular-weight 10479 #checksum 7252 SEQUENCE /// ENTRY FEKM #type complete TITLE ferredoxin [2Fe-2S] precursor, chloroplast - Chlamydomonas reinhardtii ORGANISM #formal_name Chlamydomonas reinhardtii DATE 30-Sep-1990 #sequence_revision 28-May-1999 #text_change 11-Jun-1999 ACCESSIONS T08054; S00361; S29222 REFERENCE Z16320 !$#authors Stein, M. !$#submission submitted to the EMBL Data Library, June 1995 !$#accession T08054 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-126 ##label STE !'##cross-references EMBL:U29516; NID:g1009713; PIDN:AAC49171.1; !1PID:g1009714 !'##experimental_source strain CW15 REFERENCE S00361 !$#authors Schmitter, J.M.; Jacquot, J.P.; de Lamotte-Guery, F.; !1Beauvallet, C.; Dutka, S.; Gadal, P.; Decottignies, P. !$#journal Eur. J. Biochem. (1988) 172:405-412 !$#title Purification, properties and complete amino acid sequence of !1the ferredoxin from a green alga, Chlamydomonas reinhardtii. !$#cross-references MUID:88166713; PMID:3350005 !$#accession S00361 !'##molecule_type protein !'##residues 33-126 ##label SCH REFERENCE S29222 !$#authors Rogers, W.J.; Hodges, M.; Decottignies, P.; Schmitter, J.M.; !1Gadal, P.; Jacquot, J.P. !$#journal FEBS Lett. (1992) 310:240-245 !$#title Isolation of a cDNA fragment coding for Chlamydomonas !1reinhardtii ferredoxin and expression of the recombinant !1protein in Escherichia coli. !$#cross-references MUID:93011926; PMID:1327872 !$#accession S29222 !'##molecule_type mRNA !'##residues 37-38,'S',40-100,'K',102-121 ##label ROG !'##note the sequence presented Fig. 1 is not found in GenBank entry !1CRTRX, release 111.0 although the reference is cited there GENETICS !$#introns 59/3 CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; chloroplast; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-32 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$33-126 #product ferredoxin [2Fe-2S] #status experimental !8#label MAT\ !$54-108 #domain ferredoxin [2Fe-2S] homology #label FER\ !$69,74,77,107 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8experimental SUMMARY #length 126 #molecular-weight 13232 #checksum 5962 SEQUENCE /// ENTRY FESC #type complete TITLE ferredoxin [2Fe-2S] - green alga (Scenedesmus quadricauda) ORGANISM #formal_name Scenedesmus quadricauda DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 13-Nov-1998 ACCESSIONS A00242 REFERENCE A00242 !$#authors Sugeno, K.; Matsubara, H. !$#journal J. Biol. Chem. (1969) 244:2979-2989 !$#title The amino acid sequence of Scenedesmus ferredoxin. !$#cross-references MUID:69193756; PMID:5772470 !$#accession A00242 !'##molecule_type protein !'##residues 1-96 ##label SUG CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-96 #product ferredoxin [2Fe-2S] #status experimental !8#label MAT\ !$24-78 #domain ferredoxin [2Fe-2S] homology #label FER\ !$39,44,47,77 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 96 #molecular-weight 10170 #checksum 507 SEQUENCE /// ENTRY FEDH1 #type complete TITLE ferredoxin [2Fe-2S] I - green alga (Dunaliella salina) (tentative sequence) ORGANISM #formal_name Dunaliella salina DATE 30-Apr-1980 #sequence_revision 30-Apr-1980 #text_change 31-Mar-2000 ACCESSIONS A00243 REFERENCE A93757 !$#authors Hase, T.; Matsubara, H.; Ben-Amotz, A.; Rao, K.K.; Hall, !1D.O. !$#journal Phytochemistry (1980) 19:2065-2070 !$#title Purification and sequence determination of two ferredoxins !1from Dunaliella salina. !$#accession A00243 !'##molecule_type protein !'##residues 1-95 ##label HAS !'##note 3-Gln, 32-Leu, and 50-Leu were also found CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-95 #product ferredoxin [2Fe-2S] I #status experimental !8#label MAT\ !$23-77 #domain ferredoxin [2Fe-2S] homology #label FER\ !$38,43,46,76 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 95 #molecular-weight 10162 #checksum 2187 SEQUENCE /// ENTRY FEDH2 #type complete TITLE ferredoxin [2Fe-2S] II - green alga (Dunaliella salina) (tentative sequence) ORGANISM #formal_name Dunaliella salina DATE 30-Apr-1980 #sequence_revision 30-Apr-1980 #text_change 31-Mar-2000 ACCESSIONS A00244 REFERENCE A93757 !$#authors Hase, T.; Matsubara, H.; Ben-Amotz, A.; Rao, K.K.; Hall, !1D.O. !$#journal Phytochemistry (1980) 19:2065-2070 !$#title Purification and sequence determination of two ferredoxins !1from Dunaliella salina. !$#accession A00244 !'##molecule_type protein !'##residues 1-95 ##label HAS CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-95 #product ferredoxin [2Fe-2S] II #status experimental !8#label MAT\ !$23-77 #domain ferredoxin [2Fe-2S] homology #label FER\ !$38,43,46,76 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 95 #molecular-weight 10065 #checksum 9134 SEQUENCE /// ENTRY FEKK #type complete TITLE ferredoxin [2Fe-2S] - red alga (Cyanidium caldarium) ORGANISM #formal_name Cyanidium caldarium DATE 31-May-1979 #sequence_revision 23-Oct-1981 #text_change 13-Nov-1998 ACCESSIONS A00245 REFERENCE A00245 !$#authors Hase, T.; Wakabayashi, S.; Wada, K.; Matsubara, H.; Juttner, !1F.; Rao, K.K.; Fry, I.; Hall, D.O. !$#journal FEBS Lett. (1978) 96:41-44 !$#title Cyanidium caldarium ferredoxin: a red algal type? !$#accession A00245 !'##molecule_type protein !'##residues 1-98 ##label HAS CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-98 #product ferredoxin [2Fe-2S] #status experimental !8#label MAT\ !$26-80 #domain ferredoxin [2Fe-2S] homology #label FER\ !$41,46,49,79 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 98 #molecular-weight 10694 #checksum 7633 SEQUENCE /// ENTRY FEKT1 #type complete TITLE ferredoxin [2Fe-2S] I - Cyanophora paradoxa cyanelle ORGANISM #formal_name cyanelle Cyanophora paradoxa DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 21-Jan-2000 ACCESSIONS S11048; JU0459; T06893; S10427 REFERENCE S11048 !$#authors Neumann-Spallart, C.; Brandtner, M.; Kraus, M.; Jakowitsch, !1J.; Bayer, M.G.; Maier, T.L.; Schenk, H.E.A.; Loeffelhardt, !1W. !$#journal FEBS Lett. (1990) 268:55-58 !$#title The petFI gene encoding ferredoxin I is located close to the !1str operon on the cyanelle genome of Cyanophora paradoxa. !$#cross-references MUID:90346172; PMID:2116981 !$#accession S11048 !'##molecule_type DNA !'##residues 1-99 ##label LOE !'##cross-references EMBL:X52143; NID:g11389; PIDN:CAA36387.1; !1PID:g11390 !'##experimental_source strain LB 555UTEX REFERENCE JU0459 !$#authors Bryant, D.A.; Schluchter, W.M.; Stirewalt, V.L. !$#journal Gene (1991) 98:169-175 !$#title Ferredoxin and ribosomal protein S10 are encoded on the !1cyanelle genome of Cyanophora paradoxa. !$#cross-references MUID:91200662; PMID:1901820 !$#accession JU0459 !'##molecule_type DNA !'##residues 1-99 ##label BRY !'##cross-references GB:M35206; NID:g336630; PIDN:AAA31699.1; !1PID:g336631 REFERENCE Z15840 !$#authors Stirewalt, V.L.; Michalowski, C.B.; Luffelhardt, W.; !1Bohnert, H.J.; Bryant, D.A. !$#submission submitted to the EMBL Data Library, July 1995 !$#description Nucleotide sequence of the cyanelle genome from Cyanophora !1paradoxa. !$#accession T06893 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-99 ##label STI !'##cross-references EMBL:U30821; NID:g1016083; PIDN:AAA81236.1; !1PID:g1016149 !'##experimental_source strain Pringsheim LB555 GENETICS !$#gene petFI; petF !$#genome cyanelle CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; cyanelle; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$2-99 #product ferredoxin [2Fe-2S] I #status predicted !8#label MAT\ !$27-81 #domain ferredoxin [2Fe-2S] homology #label FER\ !$42,47,50,80 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 99 #molecular-weight 10726 #checksum 2151 SEQUENCE /// ENTRY FEPRU #type complete TITLE ferredoxin [2Fe-2S] - red alga (Porphyra umbilicalis) ORGANISM #formal_name Porphyra umbilicalis #common_name laver DATE 31-May-1979 #sequence_revision 23-Oct-1981 #text_change 13-Nov-1998 ACCESSIONS A00246 REFERENCE A00246 !$#authors Takruri, I.; Haslett, B.G.; Boulter, D.; Andrew, P.W.; !1Rogers, L.J. !$#journal Biochem. J. (1978) 173:459-466 !$#title The amino acid sequence of ferredoxin from the red alga !1Porphyra umbilicalis. !$#cross-references MUID:79020768; PMID:697730 !$#accession A00246 !'##molecule_type protein !'##residues 1-98 ##label TAK CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-98 #product ferredoxin [2Fe-2S] #status experimental !8#label MAT\ !$26-80 #domain ferredoxin [2Fe-2S] homology #label FER\ !$41,46,49,79 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 98 #molecular-weight 10829 #checksum 8782 SEQUENCE /// ENTRY FEYB6 #type complete TITLE ferredoxin [2Fe-2S] [validated] - Synechocystis sp. ORGANISM #formal_name Synechocystis sp. DATE 13-Jun-1983 #sequence_revision 13-Nov-1998 #text_change 15-Sep-2000 ACCESSIONS S76345; A56811; A00247 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76345 !'##molecule_type DNA !'##residues 1-97 ##label KAN !'##cross-references EMBL:D64000; GB:AB001339; NID:g1001484; !1PIDN:BAA10197.1; PID:g1001570 !'##experimental_source strain PCC 6803 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 REFERENCE A56811 !$#authors Bottin, H.; Lagoutte, B. !$#journal Biochim. Biophys. Acta (1992) 1101:48-56 !$#title Ferredoxin and flavodoxin from the cyanobacterium !1Synechocystis sp PCC 6803. !$#cross-references MUID:92338182; PMID:1633177 !$#accession A56811 !'##molecule_type protein !'##residues 2-97 ##label BOT !'##experimental_source strain PCC 6714 !'##note sequence extracted from NCBI backbone (NCBIP:109680) REFERENCE A00247 !$#authors Hase, T.; Inoue, K.; Matsubara, H.; Williams, M.M.; Rogers, !1L.J. !$#journal J. Biochem. (1982) 92:1357-1362 !$#title Amino acid sequence of Synechocystis 6714 ferredoxin: a !1unique structural feature of unicellular blue-green algal !1ferredoxin. !$#cross-references MUID:83108768; PMID:6818221 !$#accession A00247 !'##molecule_type protein !'##residues 2-14,'N',16-97 ##label HAS !'##experimental_source strain PCC 6714 REFERENCE A65450 !$#authors Lelong, C.; Setif, P.; Bottin, H.; Andre, F.; Neumann, J.M. !$#submission submitted to the Brookhaven Protein Data Bank, September !11995 !$#cross-references PDB:1DOX !$#contents annotation; conformation and disulfide bond assignments by !1(1)H- and (15)N-NMR, without disulfide bond, residues 2-97 REFERENCE A65451 !$#authors Lelong, C.; Setif, P.; Bottin, H.; Andre, F.; Neumann, J.M. !$#submission submitted to the Brookhaven Protein Data Bank, September !11995 !$#cross-references PDB:1DOY !$#contents annotation; conformation and disulfide bond assignments by !1(1)H- and (15)N-NMR, with disulfide bond, residues 2-97 REFERENCE A58608 !$#authors Lelong, C.; Setif, P.; Bottin, H.; Andre, F.; Neumann, J.M. !$#journal Biochemistry (1995) 34:14462-14473 !$#title (1)H and (15)N NMR sequential assignment, secondary !1structure, and tertiary fold of [2Fe-2S] ferredoxin from !1Synechocystis sp. PCC 6803. !$#cross-references MUID:96062510; PMID:7578051 !$#contents annotation; conformation and disulfide bond assignments by !1(1)H-NMR CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$2-97 #product ferredoxin [2Fe-2s] #status experimental !8#label MAT\ !$25-79 #domain ferredoxin [2Fe-2S] homology #label FER\ !$19-86 #disulfide_bonds #status predicted\ !$40,45,48,78 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8experimental SUMMARY #length 97 #molecular-weight 10363 #checksum 4810 SEQUENCE /// ENTRY FEFZ1 #type complete TITLE ferredoxin [2Fe-2S] I - Aphanizomenon flos-aquae ORGANISM #formal_name Aphanizomenon flos-aquae DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 13-Nov-1998 ACCESSIONS A00248 REFERENCE A00248 !$#authors Lee, I.S.; Hase, T.; Matsubara, H.; Ho, K.K.; Krogmann, D.W. !$#journal Biochim. Biophys. Acta (1983) 744:53-56 !$#title Amino acid sequence of ferredoxin from Aphanizomenon !1flos-aquae. !$#accession A00248 !'##molecule_type protein !'##residues 1-97 ##label LEE CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-97 #product ferredoxin [2Fe-2S] I #status experimental !8#label MAT\ !$25-79 #domain ferredoxin [2Fe-2S] homology #label FER\ !$40,45,48,78 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 97 #molecular-weight 10383 #checksum 6114 SEQUENCE /// ENTRY FESG #type complete TITLE ferredoxin [2Fe-2S] - Spirulina maxima ORGANISM #formal_name Spirulina maxima DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 13-Nov-1998 ACCESSIONS A00249 REFERENCE A00249 !$#authors Tanaka, M.; Haniu, M.; Yasunobu, K.T.; Rao, K.K.; Hall, D.O. !$#journal Biochemistry (1975) 14:5535-5540 !$#title Modification of the automated sequence determination as !1applied to the sequence determination of the Spirulina !1maxima ferredoxin. !$#cross-references MUID:76062440; PMID:811255 !$#accession A00249 !'##molecule_type protein !'##residues 1-98 ##label TAN CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-98 #product ferredoxin [2Fe-2S] #status experimental !8#label MAT\ !$26-80 #domain ferredoxin [2Fe-2S] homology #label FER\ !$41,46,49,79 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 98 #molecular-weight 10488 #checksum 8264 SEQUENCE /// ENTRY FESGAL #type complete TITLE ferredoxin [2Fe-2S] [validated] - Spirulina platensis ORGANISM #formal_name Spirulina platensis DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 15-Sep-2000 ACCESSIONS A00250 REFERENCE A00250 !$#authors Tanaka, M.; Haniu, M.; Yasunobu, K.T.; Rao, K.K.; Hall, D.O. !$#journal Biochem. Biophys. Res. Commun. (1976) 69:759-765 !$#title The complete amino acid sequence of the Spirulina platensis !1ferredoxin. !$#cross-references MUID:76184180; PMID:817723 !$#accession A00250 !'##molecule_type protein !'##residues 1-98 ##label TAN REFERENCE A67348 !$#authors Fukuyama, K.; Tsukihara, T. !$#submission submitted to the Brookhaven Protein Data Bank, April 1995 !$#cross-references PDB:4FXC !$#contents annotation; X-ray crystallography, 2.5 angstroms, residues !11-98 REFERENCE A50594 !$#authors Kakudo, M.; Tsukihara, T.; Katsube, Y. !$#submission submitted to the Brookhaven Protein Data Bank, December 1981 !$#cross-references PDB:3FXC !$#contents annotation; X-ray crystallography, 2.5 angstroms, residues !11-98 REFERENCE A44591 !$#authors Tsukihara, T.; Fukuyama, K.; Nakamura, M.; Katsube, Y.; !1Tanaka, N.; Kakudo, M.; Wada, K.; Hase, T.; Matsubara, H. !$#journal J. Biochem. (1981) 90:1763-1773 !$#title X-Ray analysis of a [2Fe-2S] ferredoxin from Spirulina !1platensis. Main chain fold and location of side chains at !12.5 angstroms resolution. !$#cross-references MUID:82142259; PMID:6801028 !$#contents annotation; X-ray crystallography, 2.5 angstroms CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-98 #product ferredoxin [2Fe-2S] #status experimental !8#label MAT\ !$26-80 #domain ferredoxin [2Fe-2S] homology #label FER\ !$41,46,49,79 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8experimental SUMMARY #length 98 #molecular-weight 10502 #checksum 8546 SEQUENCE /// ENTRY FEEF #type complete TITLE ferredoxin [2Fe-2S] - Chlorogloeopsis fritschii ORGANISM #formal_name Chlorogloeopsis fritschii DATE 18-Dec-1981 #sequence_revision 18-Dec-1981 #text_change 13-Nov-1998 ACCESSIONS A00251 REFERENCE A00251 !$#authors Takahashi, Y.; Hase, T.; Matsubara, H.; Hutber, G.N.; !1Rogers, L.J. !$#journal J. Biochem. (1982) 92:1363-1368 !$#title Amino acid sequence of Chlorogloeopsis fritschii ferredoxin: !1taxonomic and evolutionary aspects. !$#cross-references MUID:83108769; PMID:6818222 !$#accession A00251 !'##molecule_type protein !'##residues 1-98 ##label TAK CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-98 #product ferredoxin [2Fe-2S] #status experimental !8#label MAT\ !$26-80 #domain ferredoxin [2Fe-2S] homology #label FER\ !$41,46,49,79 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 98 #molecular-weight 10610 #checksum 7736 SEQUENCE /// ENTRY FEMW #type complete TITLE ferredoxin [2Fe-2S] - Fischerella sp. ORGANISM #formal_name Fischerella sp. DATE 31-May-1979 #sequence_revision 31-May-1979 #text_change 13-Nov-1998 ACCESSIONS A00252 REFERENCE A00252 !$#authors Hase, T.; Wakabayashi, S.; Matsubara, H.; Rao, K.K.; Hall, !1D.O.; Widmer, H.; Gysi, J.; Zuber, H. !$#submission submitted to the Atlas, September 1978 !$#accession A00252 !'##molecule_type protein !'##residues 1-98 ##label HAS !'##note the source was designated as Mastigocladus laminosus CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-98 #product ferredoxin [2Fe-2S] #status experimental !8#label MAT\ !$26-80 #domain ferredoxin [2Fe-2S] homology #label FER\ !$41,46,49,79 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 98 #molecular-weight 10617 #checksum 7838 SEQUENCE /// ENTRY FENM2M #type complete TITLE ferredoxin [2Fe-2S] II - Nostoc muscorum ORGANISM #formal_name Nostoc muscorum DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 13-Nov-1998 ACCESSIONS A00253 REFERENCE A91968 !$#authors Hase, T.; Matsubara, H.; Hutber, G.N.; Rogers, L.J. !$#journal J. Biochem. (1982) 92:1347-1355 !$#title Amino acid sequences of Nostoc strain MAC ferredoxins I and !1II. !$#cross-references MUID:83108767; PMID:6818220 !$#accession A00253 !'##molecule_type protein !'##residues 1-98 ##label HAS !'##experimental_source strain mac CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-98 #product ferredoxin [2Fe-2S] II #status experimental !8#label MAT\ !$26-80 #domain ferredoxin [2Fe-2S] homology #label FER\ !$41,46,49,79 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 98 #molecular-weight 10549 #checksum 6766 SEQUENCE /// ENTRY FEAH #type complete TITLE ferredoxin [2Fe-2S] I [validated] - Aphanothece sacrum ORGANISM #formal_name Aphanothece sacrum DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 15-Sep-2000 ACCESSIONS A00254 REFERENCE A00254 !$#authors Hase, T.; Wada, K.; Matsubara, H. !$#journal J. Biochem. (1976) 79:329-343 !$#title Amino acid sequence of the major component of Aphanothece !1sacrum ferredoxin. !$#cross-references MUID:76190060; PMID:818078 !$#accession A00254 !'##molecule_type protein !'##residues 1-96 ##label HAS REFERENCE A50133 !$#authors Tsukihara, T. !$#submission submitted to the Brookhaven Protein Data Bank, August 1990 !$#cross-references PDB:1FXI !$#contents annotation; X-ray crystallography, 2.2 angstroms, residues !11-96 REFERENCE A44586 !$#authors Tsukihara, T.; Fukuyama, K.; Mizushima, M.; Harioka, T.; !1Kusunoki, M.; Katsube, Y.; Hase, T.; Matsubara, H. !$#journal J. Mol. Biol. (1990) 216:399-410 !$#title Structure of the [2Fe-2S] ferredoxin I from the blue-green !1alga Aphanothece sacrum at 2.2 angstroms resolution. !$#cross-references MUID:91073403; PMID:2123937 !$#contents annotation; X-ray crystallography, 2.2 angstroms CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-96 #product ferredoxin [2Fe-2S] I #status experimental !8#label MAT\ !$24-78 #domain ferredoxin [2Fe-2S] homology #label FER\ !$39,44,47,77 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8experimental SUMMARY #length 96 #molecular-weight 10308 #checksum 2377 SEQUENCE /// ENTRY FEAH2 #type complete TITLE ferredoxin [2Fe-2S] II - Aphanothece sacrum ORGANISM #formal_name Aphanothece sacrum DATE 31-May-1979 #sequence_revision 08-Oct-1981 #text_change 13-Nov-1998 ACCESSIONS A00255 REFERENCE A00255 !$#authors Hase, T.; Wakabayashi, S.; Wada, K.; Matsubara, H. !$#journal J. Biochem. (1978) 83:761-770 !$#title Amino acid sequence of Aphanothece sacrum ferredoxin II !1(minor component). !$#cross-references MUID:78150873; PMID:417074 !$#accession A00255 !'##molecule_type protein !'##residues 1-99 ##label HAS !'##note there is no clear evidence of functional difference between !1this ferredoxin and ferredoxin I (major component) from this !1organism; the different amino acid compositions suggest they !1are genetically independent isoenzymes CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-99 #product ferredoxin [2Fe-2S] II #status experimental !8#label MAT\ !$26-81 #domain ferredoxin [2Fe-2S] homology #label FER\ !$41,46,49,80 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 99 #molecular-weight 10354 #checksum 1021 SEQUENCE /// ENTRY FENM1M #type complete TITLE ferredoxin [2Fe-2S] I - Nostoc muscorum ORGANISM #formal_name Nostoc muscorum DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 13-Nov-1998 ACCESSIONS A00256 REFERENCE A91968 !$#authors Hase, T.; Matsubara, H.; Hutber, G.N.; Rogers, L.J. !$#journal J. Biochem. (1982) 92:1347-1355 !$#title Amino acid sequences of Nostoc strain MAC ferredoxins I and !1II. !$#cross-references MUID:83108767; PMID:6818220 !$#accession A00256 !'##molecule_type protein !'##residues 1-98 ##label HAS !'##experimental_source strain MAC CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-98 #product ferredoxin [2Fe-2S] I #status experimental !8#label MAT\ !$26-80 #domain ferredoxin [2Fe-2S] homology #label FER\ !$41,46,49,79 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 98 #molecular-weight 10747 #checksum 9400 SEQUENCE /// ENTRY FENM #type complete TITLE ferredoxin [2Fe-2S] - Nostoc muscorum ORGANISM #formal_name Nostoc muscorum DATE 24-Apr-1984 #sequence_revision 03-Aug-1984 #text_change 13-Nov-1998 ACCESSIONS A00257 REFERENCE A00257 !$#authors Hase, T.; Wada, K.; Ohmiya, M.; Matsubara, H. !$#journal J. Biochem. (1976) 80:993-999 !$#title Amino acid sequence of the major component of Nostoc !1muscorum ferredoxin. !$#cross-references MUID:77071433; PMID:826526 !$#accession A00257 !'##molecule_type protein !'##residues 1-98 ##label HAS CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-98 #product ferredoxin [2Fe-2S] #status experimental !8#label MAT\ !$26-80 #domain ferredoxin [2Fe-2S] homology #label FER\ !$41,46,49,79 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 98 #molecular-weight 10700 #checksum 8837 SEQUENCE /// ENTRY S25233 #type complete TITLE ferredoxin [2Fe-2S] I [validated] - Anabaena sp. (strain PCC 7120) ORGANISM #formal_name Anabaena sp. DATE 28-May-1993 #sequence_revision 28-May-1993 #text_change 15-Sep-2000 ACCESSIONS S25233 REFERENCE S25233 !$#authors Alam, J.; Whitaker, R.A.; Krogmann, D.W.; Curtis, S.E. !$#journal J. Bacteriol. (1986) 168:1265-1271 !$#title Isolation and sequence of the gene for ferredoxin I from the !1cyanobacterium Anabaena sp. strain PCC 7120. !$#cross-references MUID:87057031; PMID:2430949 !$#accession S25233 !'##molecule_type DNA !'##residues 1-99 ##label ALA !'##cross-references EMBL:M14737; NID:g142075; PIDN:AAA22021.1; !1PID:g142076 REFERENCE A50838 !$#authors Rypniewski, W.R.; Breiter, D.R.; Benning, M.M.; Wesenberg, !1G.; Oh, B.H.; Markley, J.L.; Rayment, I.; Holden, H.M. !$#submission submitted to the Brookhaven Protein Data Bank, January 1991 !$#cross-references PDB:1FXA !$#contents annotation; X-ray crystallography, 2.5 angstroms, residues !12-97 REFERENCE A58609 !$#authors Rypniewski, W.R.; Breiter, D.R.; Benning, M.M.; Wesenberg, !1G.; Oh, B.H.; Markley, J.L.; Rayment, I.; Holden, H.M. !$#journal Biochemistry (1991) 30:4126-4131 !$#title Crystallization and structure determination to 2.5-Angstroms !1resolution of the oxidized [2Fe-2S] ferredoxin isolated from !1Anabaena 7120. !$#cross-references MUID:91214942; PMID:1902376 !$#contents annotation; X-ray crystallography, 2.5 angstroms GENETICS !$#gene petF CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$2-99 #product ferredoxin [2Fe-2S] I #status experimental !8#label MAT\ !$27-81 #domain ferredoxin [2Fe-2S] homology #label FER\ !$42,47,50,80 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8experimental SUMMARY #length 99 #molecular-weight 10830 #checksum 1898 SEQUENCE /// ENTRY FEAI #type complete TITLE ferredoxin [2Fe-2S] - Anabaena variabilis ALTERNATE_NAMES ferredoxin II ORGANISM #formal_name Anabaena variabilis DATE 31-Dec-1990 #sequence_revision 06-Feb-1995 #text_change 11-Jun-1999 ACCESSIONS A25761; S08121; A04618; A00257 REFERENCE A25761 !$#authors van der Plas, J.; de Groot, R.P.; Weisbeek, P.J.; van Arkel, !1G.A. !$#journal Nucleic Acids Res. (1986) 14:7803 !$#title Coding sequence of a ferredoxin gene from Anabaena !1variabilis ATCC 29413. !$#cross-references MUID:87040742; PMID:3095790 !$#accession A25761 !'##molecule_type DNA !'##residues 1-99 ##label VAN !'##cross-references GB:X06210; NID:g39246; PIDN:CAA29563.1; PID:g39247 REFERENCE S08121 !$#authors van der Plas, J.; de Groot, R.; Woortman, M.; Cremers, F.; !1Borrias, M.; van Arkel, G.; Weisbeek, P. !$#journal Photosyn. Res. (1988) 18:179-204 !$#title Genes encoding ferredoxins from Anabaena sp. PCC 7937 and !1Synechococcus sp. PCC 7942: structure and regulation. !$#accession S08121 !'##molecule_type DNA !'##residues 1-99 ##label VA2 !'##cross-references EMBL:X14343; NID:g38884; PIDN:CAA32528.1; !1PID:g38885 REFERENCE A04618 !$#authors Chan, T.M.; Hermodson, M.A.; Ulrich, E.L.; Markley, J.L. !$#journal Biochemistry (1983) 22:5988-5995 !$#title Nuclear magnetic resonance studies of two-iron-two-sulfur !1ferredoxins. 2. Determination of the sequence of Anabaena !1variabilis ferredoxin II, assignment of aromatic resonances !1in proton spectra, and effects of chemical modification. !$#accession A04618 !'##molecule_type protein !'##residues 2-15,'KHE',19,'E',21-33,'E',35-87,'CV',90-99 ##label CHA !'##note the supposed modification of 16-Lys and its effect on the NMR !1shifts for 17-His are reported GENETICS !$#gene petF1 CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$2-99 #product ferredoxin [2Fe-2S] #status experimental !8#label MAT\ !$27-81 #domain ferredoxin [2Fe-2S] homology #label FER\ !$42,47,50,80 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 99 #molecular-weight 10726 #checksum 2314 SEQUENCE /// ENTRY FEYCAL #type complete TITLE ferredoxin [2Fe-2S] - Synechococcus lividus ORGANISM #formal_name Synechococcus lividus DATE 31-Jan-1980 #sequence_revision 24-Sep-1981 #text_change 13-Nov-1998 ACCESSIONS A00258 REFERENCE A00106 !$#authors Borden, D.; Margoliash, E. !$#submission submitted to the Atlas, December 1979 !$#accession A00258 !'##molecule_type protein !'##residues 1-96 ##label BOR CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-96 #product ferredoxin [2Fe-2S] #status experimental !8#label MAT\ !$24-78 #domain ferredoxin [2Fe-2S] homology #label FER\ !$39,44,47,77 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 96 #molecular-weight 10652 #checksum 1012 SEQUENCE /// ENTRY FEYCT #type complete TITLE ferredoxin [2Fe-2S] [validated] - Synechococcus sp. ORGANISM #formal_name Synechococcus sp. DATE 25-Feb-1985 #sequence_revision 03-Nov-2000 #text_change 03-Nov-2000 ACCESSIONS A00259 REFERENCE A00259 !$#authors Hase, T.; Matsubara, H.; Koike, H.; Katoh, S. !$#journal Biochim. Biophys. Acta (1983) 744:46-52 !$#title Amino acid sequence of ferredoxin from a thermophilic !1blue-green alga, Synechococcus sp. !$#accession A00259 !'##molecule_type protein !'##residues 1-97 ##label HAS REFERENCE A67906 !$#authors Hatanaka, H.; Tanimura, R.; Katoh, S.; Inagaki, F. !$#submission submitted to the Brookhaven Protein Data Bank, February 1997 !$#cross-references PDB:2CJN !$#contents annotation; conformation (1)H-NMR, residues 1-97 !$#note the source is designated as Synechococcus elongatus REFERENCE A66539 !$#authors Roesch, P.; Baumann, B.; Sticht, H.; Sutter, M.; Haehnel, W. !$#submission submitted to the Brookhaven Protein Data Bank, November 1995 !$#cross-references PDB:1ROE !$#contents annotation; conformation (1)H-NMR, residues 1-97 !$#note the source is designated as Synechococcus elongatus CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-97 #product ferredoxin [2Fe-2S] #status experimental !8#label MAT\ !$25-79 #domain ferredoxin [2Fe-2S] homology #label FER\ !$40,45,48,78 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8experimental SUMMARY #length 97 #molecular-weight 10716 #checksum 4697 SEQUENCE /// ENTRY FEYO #type complete TITLE ferredoxin [2Fe-2S] - green alga (Bryopsis maxima) ORGANISM #formal_name Bryopsis maxima DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 13-Nov-1998 ACCESSIONS S07452 REFERENCE S07452 !$#authors Minami, Y.; Sugimura, Y.; Wakabayashi, S.; Wada, K.; !1Takahashi, Y.; Matsubara, H. !$#journal Physiol. Veg. (1985) 23:669-678 !$#title Isolation, properties, and amino acid sequence of a !1ferredoxin from a multinuclear, unicellular green alga, !1Bryopsis marina. !$#accession S07452 !'##molecule_type protein !'##residues 1-98 ##label MIN CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-98 #product ferredoxin [2Fe-2S] #status experimental !8#label MAT\ !$25-79 #domain ferredoxin [2Fe-2S] homology #label FER\ !$40,45,48,78 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 98 #molecular-weight 10615 #checksum 7543 SEQUENCE /// ENTRY FEBF2 #type complete TITLE ferredoxin [2Fe-2S] - yellow-green alga (Bumilleriopsis filiformis) ORGANISM #formal_name Bumilleriopsis filiformis DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 13-Nov-1998 ACCESSIONS A28857 REFERENCE A28857 !$#authors Inoue, K.; Hase, T.; Boeger, P.; Matsubara, H. !$#journal J. Biochem. (1983) 94:1451-1455 !$#title Amino acid sequence of a ferredoxin from Bumilleriopsis !1filiformis, a yellow-green alga: relationship with red !1algae, protoflorideophyceae, and filamentous blue-green !1algae. !$#cross-references MUID:84087800; PMID:6418731 !$#accession A28857 !'##molecule_type protein !'##residues 1-98 ##label INO !'##note 1-Ala was also found CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-98 #product ferredoxin [2Fe-2S] #status experimental !8#label MAT\ !$26-80 #domain ferredoxin [2Fe-2S] homology #label FER\ !$41,46,49,79 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 98 #molecular-weight 10620 #checksum 8112 SEQUENCE /// ENTRY FEDQ #type complete TITLE ferredoxin [2Fe-2S] - dinoflagellate (Peridinium bipes) ORGANISM #formal_name Peridinium bipes DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 13-Nov-1998 ACCESSIONS A30036 REFERENCE A30036 !$#authors Uchida, A.; Ebata, S.; Wada, K.; Matsubara, H.; Ishida, Y. !$#journal J. Biochem. (1988) 104:700-705 !$#title Complete amino acid sequence of ferredoxin from Peridinium !1bipes (Dinophyceae). !$#cross-references MUID:89174497; PMID:3235446 !$#accession A30036 !'##molecule_type protein !'##residues 1-93 ##label UCH COMMENT Peridinium is a dinoflagellate, a unicellular alga. CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-93 #product ferredoxin [2Fe-2S] #status experimental !8#label MAT\ !$22-76 #domain ferredoxin [2Fe-2S] homology #label FER\ !$37,42,45,75 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 93 #molecular-weight 9958 #checksum 5571 SEQUENCE /// ENTRY FELV #type complete TITLE ferredoxin [2Fe-2S] - liverwort (Marchantia polymorpha) ORGANISM #formal_name Marchantia polymorpha DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 13-Nov-1998 ACCESSIONS A24126 REFERENCE A24126 !$#authors Minami, Y.; Wakabayashi, S.; Imoto, S.; Ohta, Y.; Matsubara, !1H. !$#journal J. Biochem. (1985) 98:649-655 !$#title Ferredoxin from a liverwort, Marchantia polymorpha. !1Purification and amino acid sequence. !$#cross-references MUID:86111669; PMID:4086466 !$#accession A24126 !'##molecule_type protein !'##residues 1-95 ##label MIN CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-95 #product ferredoxin [2Fe-2S] #status experimental !8#label MAT\ !$23-77 #domain ferredoxin [2Fe-2S] homology #label FER\ !$38,43,46,76 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 95 #molecular-weight 10174 #checksum 8731 SEQUENCE /// ENTRY FEYC2 #type complete TITLE ferredoxin [2Fe-2S] II - Synechococcus sp. (strain PCC 6301) ORGANISM #formal_name Synechococcus sp. DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 11-Jun-1999 ACCESSIONS S10833; S00605 REFERENCE S07286 !$#authors Cozens, A.L.; Walker, J.E. !$#journal J. Mol. Biol. (1987) 194:359-383 !$#title The organization and sequence of the genes for ATP synthase !1subunits in the cyanobacterium Synechococcus 6301. Support !1for an endosymbiotic origin of chloroplasts. !$#cross-references MUID:87311713; PMID:3041005 !$#accession S10833 !'##molecule_type DNA !'##residues 1-105 ##label COZ !'##cross-references EMBL:X05302; NID:g48009; PIDN:CAA28930.1; !1PID:g48019 REFERENCE S00604 !$#authors Cozens, A.L.; Walker, J.E. !$#journal Biochem. J. (1988) 252:563-569 !$#title Expression of a gene encoding a novel ferredoxin in the !1cyanobacterium Synechococcus 6301. !$#cross-references MUID:88326273; PMID:2843173 !$#accession S00605 !'##molecule_type DNA !'##residues 1-105 ##label COZ1 CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein; respiratory chain FEATURE !$2-105 #product ferredoxin [2Fe-2S] II #status predicted !8#label MAT\ !$25-79 #domain ferredoxin [2Fe-2S] homology #label FER\ !$40,45,48,78 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 105 #molecular-weight 11132 #checksum 3645 SEQUENCE /// ENTRY FERFND #type complete TITLE ferredoxin [2Fe-2S]-like protein, fdxD - Rhodobacter capsulatus ORGANISM #formal_name Rhodobacter capsulatus DATE 28-Aug-1985 #sequence_revision 27-Jan-1995 #text_change 11-Jun-1999 ACCESSIONS JN0887; S18916; S44466 REFERENCE JN0887 !$#authors Willison, J.C.; Pierrard, J.; Huebner, P. !$#journal Gene (1993) 133:39-46 !$#title Sequence and transcript analysis of the nitrogenase !1structural gene operon (nifHDK) of Rhodobacter capsulatus: !1evidence for intramolecular processing of nifHDK mRNA. !$#cross-references MUID:94040794; PMID:7693551 !$#accession JN0887 !'##molecule_type DNA !'##residues 1-123 ##label WIL !'##cross-references EMBL:X63352; NID:g550144; PIDN:CAA44953.1; !1PID:g550145 REFERENCE S18916 !$#authors Willison, J.C.; Pierrard, J.; Huebner, P.; Chabert, J.; !1Vignais, P.M. !$#submission submitted to the EMBL Data Library, November 1991 !$#description Northern blot analysis of the nitrogenase structural gene !1operon (nifHDK) of Rhodobacter capsulatus and identification !1of a ferredoxin-like gene (fdxD) upstream of nifHDK. !$#accession S18916 !'##molecule_type DNA !'##residues 1-52,'DL',55-123 ##label WI2 REFERENCE S44466 !$#authors Armengaud, J.; Meyer, C.; Jouanneau, Y. !$#journal Biochem. J. (1994) 300:413-418 !$#title Recombinant expression of the fdxD gene of Rhodobacter !1capsulatus and characterization of its product, a [2Fe-2S] !1ferredoxin. !$#cross-references MUID:94271155; PMID:8002946 !$#accession S44466 !'##status preliminary !'##molecule_type DNA !'##residues 1-123 ##label ARM GENETICS !$#gene fdxD CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$2-123 #product ferredoxin [2Fe-2S]-like protein, fdxD !8#status predicted #label MAT\ !$27-103 #domain ferredoxin [2Fe-2S] homology #status atypical !8#label FER\ !$42,47,50,102 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 123 #molecular-weight 13450 #checksum 8490 SEQUENCE /// ENTRY FERFNC #type complete TITLE ferredoxin [2Fe-2S] - Rhodobacter capsulatus ALTERNATE_NAMES ferredoxin IV; plant-type ferredoxin ORGANISM #formal_name Rhodobacter capsulatus DATE 31-Dec-1990 #sequence_revision 27-Jan-1995 #text_change 11-Jun-1999 ACCESSIONS S08393; B39857; A39519; S39897 REFERENCE S08393 !$#authors Saeki, K.; Miyatake, Y.; Young, D.A.; Marrs, B.L.; !1Matsubara, H. !$#journal Nucleic Acids Res. (1990) 18:1060 !$#title A plant-ferredoxin-like gene is located upstream of !1ferredoxin I gene (fdxN) of Rhodobacter capsulatus. !$#cross-references MUID:90192101; PMID:2315024 !$#accession S08393 !'##molecule_type DNA !'##residues 1-95 ##label SAE !'##cross-references EMBL:X51316; NID:g46141; PIDN:CAA35698.1; !1PID:g46142 REFERENCE A39857 !$#authors Saeki, K.; Suetsugu, Y.; Tokuda, K.; Miyatake, Y.; Young, !1D.A.; Marrs, B.L.; Matsubara, H. !$#journal J. Biol. Chem. (1991) 266:12889-12895 !$#title Genetic analysis of functional differences among distinct !1ferredoxins in Rhodobacter capsulatus. !$#cross-references MUID:91302301; PMID:2071578 !$#accession B39857 !'##molecule_type DNA !'##residues 1-95 ##label SA2 !'##cross-references GB:X51316; GB:S42008; NID:g46141; PIDN:CAA35698.1; !1PID:g46142 REFERENCE A39519 !$#authors Grabau, C.; Schatt, E.; Jouanneau, Y.; Vignais, P.M. !$#journal J. Biol. Chem. (1991) 266:3294-3299 !$#title A new [2Fe-2S] ferredoxin from Rhodobacter capsulatus. !1Coexpression with a 2[4Fe-4S] ferredoxin in Escherichia !1coli. !$#cross-references MUID:91131639; PMID:1847145 !$#accession A39519 !'##molecule_type DNA !'##residues 1-95 ##label GRA !'##cross-references GB:M59855; GB:J05743; NID:g151915; PIDN:AAA26109.1; !1PID:g151916 REFERENCE S39892 !$#authors Schmehl, M.; Jahn, A.; Meyer zu Vilsendorf, A.; Hennecke, !1S.; Masepohl, B.; Schuppler, M.; Marxer, M.; Oelze, J.; !1Klipp, W. !$#journal Mol. Gen. Genet. (1993) 241:602-615 !$#title Identification of a new class of nitrogen fixation genes in !1Rhodobacter capsulatus: a putative membrane complex involved !1in electron transport to nitrogenase. !$#cross-references MUID:94088454; PMID:8264535 !$#accession S39897 !'##status preliminary !'##molecule_type DNA !'##residues 1-95 ##label SCH !'##cross-references EMBL:X72888; NID:g435523; PIDN:CAA51403.1; !1PID:g435529 GENETICS !$#gene fdxC CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$2-95 #product ferredoxin [2Fe-2S] #status predicted #label !8MAT\ !$23-82 #domain ferredoxin [2Fe-2S] homology #label FER\ !$38,43,46,81 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 95 #molecular-weight 10163 #checksum 695 SEQUENCE /// ENTRY A36003 #type complete TITLE ferredoxin [2Fe-2S] precursor, hydrogenosomal - Trichomonas vaginalis ORGANISM #formal_name Trichomonas vaginalis #note host Homo sapiens (man) DATE 21-Dec-1990 #sequence_revision 27-Jan-1995 #text_change 13-Nov-1998 ACCESSIONS A36003; B36003 REFERENCE A36003 !$#authors Johnson, P.J.; d'Oliveira, C.E.; Gorrell, T.E.; Mueller, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:6097-6101 !$#title Molecular analysis of the hydrogenosomal ferredoxin of the !1anaerobic protist Trichomonas vaginalis. !$#cross-references MUID:90349562; PMID:1696716 !$#accession A36003 !'##molecule_type DNA !'##residues 1-101 ##label JOH !'##cross-references GB:M33717 !'##experimental_source strain C1 (ATCC 30001) !$#accession B36003 !'##molecule_type protein !'##residues 9-70,'X',72-79,'X',81,'X',83-101 ##label JOH2 CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-8 #domain transit peptide (hydrogenosome) #status !8predicted #label TRN\ !$9-101 #product ferredoxin [2Fe-2S] #status experimental !8#label MAT\ !$34-87 #domain ferredoxin [2Fe-2S] homology #label FER\ !$46,52,55,86 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 101 #molecular-weight 10746 #checksum 3962 SEQUENCE /// ENTRY AXHU #type complete TITLE adrenodoxin precursor [validated] - human ALTERNATE_NAMES adrenal ferredoxin; ferredoxin [2Fe-2S] 1; placental ferredoxin ORGANISM #formal_name Homo sapiens #common_name man DATE 03-Feb-1994 #sequence_revision 03-Feb-1994 #text_change 19-Jan-2001 ACCESSIONS A31853; A28999; A29920; A34586; S06400; S09484 REFERENCE A31853 !$#authors Chang, C.Y.; Wu, D.A.; Lai, C.C.; Miller, W.L.; Chung, B.C. !$#journal DNA (1988) 7:609-615 !$#title Cloning and structure of the human adrenodoxin gene. !$#cross-references MUID:89152748; PMID:3229285 !$#accession A31853 !'##molecule_type DNA !'##residues 1-184 ##label CH2 !'##cross-references GB:M23665; NID:g340999 REFERENCE A28999 !$#authors Picado-Leonard, J.; Voutilainen, R.; Kao, L.; Chung, B.; !1Strauss III, J.F.; Miller, W.L. !$#journal J. Biol. Chem. (1988) 263:3240-3244 !$#title Human adrenodoxin: cloning of three cDNAs and cycloheximide !1enhancement in JEG-3 cells. !$#cross-references MUID:88139395; PMID:3343244 !$#accession A28999 !'##molecule_type mRNA !'##residues 1-184 ##label PIC !'##cross-references GB:J03548; NID:g178085; PIDN:AAA96806.1; !1PID:g178086 !'##note this sequence has been revised in reference A29920; the revised !1sequence is shown REFERENCE A29920 !$#authors Picado-Leonard, J.; Voutilainen, R.; Kao, L.; Chung, B.; !1Strauss III, J.F.; Miller, W.L. !$#journal J. Biol. Chem. (1988) 263:11016 !$#contents erratum: addition of residues 4-7 and revision of residues !128 and 55 !$#accession A29920 !'##molecule_type mRNA !'##residues 1-184 ##label PI2 !'##cross-references GB:J03548; NID:g178085; PIDN:AAA96806.1; !1PID:g178086 REFERENCE A34586 !$#authors Chang, C.Y.; Wu, D.A.; Mohandas, T.K.; Chung, B.C. !$#journal DNA Cell Biol. (1990) 9:205-212 !$#title Structure, sequence, chromosomal location, and evolution of !1the human ferredoxin gene family. !$#cross-references MUID:90253614; PMID:2340092 !$#accession A34586 !'##molecule_type mRNA !'##residues 1-184 ##label CHA !'##cross-references GB:M34788; NID:g182495; PIDN:AAA35829.1; !1PID:g182496 !'##genetics FDX1 !'##note partial genomic sequences from two expressed genes and two !1pseudogenes were also determined REFERENCE S06400 !$#authors Mittal, S.; Zhu, Y.Z.; Vickery, L.E. !$#journal Arch. Biochem. Biophys. (1988) 264:383-391 !$#title Molecular cloning and sequence analysis of human placental !1ferredoxin. !$#cross-references MUID:88292950; PMID:2969697 !$#accession S06400 !'##molecule_type mRNA !'##residues 1-184 ##label MIT !'##cross-references GB:M18003; NID:g182493; PIDN:AAA76853.1; !1PID:g182494 !'##genetics FDX2 REFERENCE S09484 !$#authors Coghlan, V.M.; Cupp, J.R.; Vickery, L.E. !$#journal Arch. Biochem. Biophys. (1988) 264:376-382 !$#title Purification and characterization of human placental !1ferredoxin. !$#cross-references MUID:88292949; PMID:3401007 !$#accession S09484 !'##molecule_type protein !'##residues 61-68;182-184 ##label COG !'##experimental_source placenta GENETICS FDX1 !$#gene GDB:FDX1; FDX; ADX !'##cross-references GDB:119657; OMIM:103260 !$#map_position 11q22-11q23 !$#introns 62/2; 104/1; 147/2 GENETICS FDX2 !$#gene GDB:FDX2 !'##cross-references GDB:128254 !$#map_position 11q22-11q23 !$#introns 62/2; 104/1; 147/2 !$#note there are two functional genes on chromosome 11; there is !1disagreement about the position of FDX2 FUNCTION !$#description an electron transfer intermediate between ferredoxin-NADP+ !1reductase (adrenodoxin reductase) and mitochondrial forms of !1cytochrome P450 CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein; mitochondrion FEATURE !$1-60 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$61-184 #product adrenodoxin #status experimental #label MAT\ !$89-153 #domain ferredoxin [2Fe-2S] homology #label FER\ !$106,112,115,152 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 184 #molecular-weight 19392 #checksum 3494 SEQUENCE /// ENTRY AXBO #type complete TITLE adrenodoxin precursor - bovine ALTERNATE_NAMES adrenal ferredoxin; ferredoxin [2Fe-2S]; hepatoredoxin ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 24-Apr-1984 #sequence_revision 31-Mar-1993 #text_change 13-Nov-1998 ACCESSIONS JX0094; A28069; B28441; A00260; JN0409; A28776; S06486; !1S21113 REFERENCE JX0094 !$#authors Sagara, Y.; Sawae, H.; Kimura, A.; Sagara-Nakano, Y.; !1Morohashi, K.; Miyoshi, K.; Horiuchi, T. !$#journal J. Biochem. (1990) 107:77-83 !$#title Structural organization of the bovine adrenodoxin gene. !$#cross-references MUID:90236984; PMID:2332422 !$#accession JX0094 !'##molecule_type DNA !'##residues 1-186 ##label SAG !'##cross-references GB:D00468 REFERENCE A28069 !$#authors Kagimoto, M.; Kagimoto, K.; Simpson, E.R.; Waterman, M.R. !$#journal J. Biol. Chem. (1988) 263:8925-8928 !$#title Transcription of the bovine adrenodoxin gene produces two !1species of mRNA of which only one is translated into !1adrenodoxin. !$#cross-references MUID:88243758; PMID:2454231 !$#accession A28069 !'##molecule_type DNA !'##residues 1-101 ##label KAG !'##cross-references EMBL:D00467 REFERENCE A92599 !$#authors Okamura, T.; Kagimoto, M.; Simpson, E.R.; Waterman, M.R. !$#journal J. Biol. Chem. (1987) 262:10335-10338 !$#title Multiple species of bovine adrenodoxin mRNA. Occurrence of !1two different mitochondrial precursor sequences associated !1with the same mature sequence. !$#cross-references MUID:87280062; PMID:2440863 !$#accession B28441 !'##molecule_type mRNA !'##residues 23,'V',25-70 ##label OKA REFERENCE A00260 !$#authors Tanaka, M.; Haniu, M.; Yasunobu, K.T.; Kimura, T. !$#journal J. Biol. Chem. (1973) 248:1141-1157 !$#title The amino acid sequence of bovine adrenodoxin. !$#cross-references MUID:73097075; PMID:4686920 !$#accession A00260 !'##molecule_type protein !'##residues 59-61,'Q',63-129,'N',131-133,'N',135-172 ##label TAN REFERENCE JN0409 !$#authors Chashchin, V.L.; Lapko, V.N.; Adamovich, T.B.; Kirillova, !1N.M.; Lapko, A.G.; Akhrem, A.A. !$#journal Bioorg. Khim. (1986) 12:1286-1289 !$#title The primary structure of hepatoredoxin from bovine liver !1mitochondria. !$#cross-references MUID:87048987; PMID:3778538 !$#accession JN0409 !'##molecule_type protein !'##residues 84-175 ##label CHA REFERENCE A28776 !$#authors Sakihama, N.; Hiwatashi, A.; Miyatake, A.; Shin, M.; !1Ichikawa, Y. !$#journal Arch. Biochem. Biophys. (1988) 264:23-29 !$#title Isolation and purification of mature bovine adrenocortical !1ferredoxin with an elongated carboxyl end. !$#cross-references MUID:88280262; PMID:3395121 !$#accession A28776 !'##molecule_type protein !'##residues 171-185 ##label SAK !'##note this protein purification yielded a form complete at the !1carboxyl end except for a single amino acid; it is unclear !1whether the absence represents processing in vivo or an !1artifact of purification; these results contradict the !1evidence for a carboxyl-terminal propeptide in reference !1JN0409 REFERENCE S06485 !$#authors Driscoll, W.J.; Omdahl, J.L. !$#journal Eur. J. Biochem. (1989) 185:181-187 !$#title Characterization and N-terminal amino acid sequence of !1multiple ferredoxins in kidney and adrenal mitochondria. !$#cross-references MUID:90032674; PMID:2553401 !$#accession S06486 !'##molecule_type protein !'##residues 59-76 ##label DRI COMMENT Adrenodoxin is a component of the steroid hydroxylating !1system in adrenal cortex mitochondria. COMMENT A minor (10%) component of adrenodoxin mRNA includes a !1defective alternate first exon that contains a stop codon !1and cannot lead to expression of the mature protein. GENETICS !$#introns 60/2; 100/1; 145/2 CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; alternative splicing; electron transfer; iron-sulfur !1protein; metalloprotein; mitochondrion FEATURE !$1-58 #domain transit peptide (mitochondrion) #status !8predicted #label TRN\ !$59-186 #product (or 59-185) adrenodoxin #status experimental !8#label MAT\ !$87-151 #domain ferredoxin [2Fe-2S] homology #label FER\ !$104,110,113,150 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 186 #molecular-weight 19756 #checksum 2914 SEQUENCE /// ENTRY AXPG #type complete TITLE adrenodoxin precursor - pig ALTERNATE_NAMES adrenal ferredoxin; ferredoxin [2Fe-2S]; renodoxin ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 31-Jul-1979 #sequence_revision 07-Jun-1996 #text_change 13-Nov-1998 ACCESSIONS S20332; A00261; S06485 REFERENCE S20332 !$#authors Omdahl, J.L.; Wilson, K.; Swerdlow, H.; Driscoll, W.J. !$#journal Arch. Biochem. Biophys. (1992) 293:213-218 !$#title Molecular cloning and immunological characterization of !1porcine kidney ferredoxin. !$#cross-references MUID:92161799; PMID:1536558 !$#accession S20332 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-186 ##label OMD REFERENCE A00261 !$#authors Akhrem, A.A.; Lapko, A.G.; Lapko, V.N.; Morozova, L.A.; !1Repin, V.A.; Tishchenko, I.V.; Chashchin, V.L. !$#journal Bioorg. Khim. (1978) 4:462-475 !$#title Adrenodoxin. !$#accession A00261 !'##molecule_type protein !'##residues 59-175 ##label AKH REFERENCE S06485 !$#authors Driscoll, W.J.; Omdahl, J.L. !$#journal Eur. J. Biochem. (1989) 185:181-187 !$#title Characterization and N-terminal amino acid sequence of !1multiple ferredoxins in kidney and adrenal mitochondria. !$#cross-references MUID:90032674; PMID:2553401 !$#accession S06485 !'##molecule_type protein !'##residues 59-76 ##label DRI CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein; mitochondrion FEATURE !$1-58 #domain transit peptide (mitochondrion) #status !8predicted #label TPP\ !$59-186 #product adrenodoxin #status predicted #label MAT\ !$87-151 #domain ferredoxin [2Fe-2S] homology #label FER\ !$104,110,113,150 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 186 #molecular-weight 19931 #checksum 597 SEQUENCE /// ENTRY A39553 #type complete TITLE adrenodoxin precursor - rat ALTERNATE_NAMES adrenal ferredoxin; ferredoxin [2Fe-2S] ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A39553; JC4538; PC4124 REFERENCE A39553 !$#authors Mellon, S.H.; Kushner, J.A.; Vaisse, C. !$#journal DNA Cell Biol. (1991) 10:339-347 !$#title Expression and regulation of adrenodoxin and P450-scc mRNA !1in rodent tissues. !$#cross-references MUID:91321737; PMID:1863358 !$#accession A39553 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-188 ##label MEL REFERENCE JC4538 !$#authors Sagara, Y.; Watanabe, Y.; Kawamura, K.; Yubisui, T. !$#journal Biol. Pharm. Bull. (1996) 19:39-41 !$#title Cloning and sequence analysis of a full-length cDNA of rat !1adrenodoxin. !$#cross-references MUID:96418123; PMID:8820908 !$#accession JC4538 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-126,'M',128-188 ##label SAG !'##cross-references GB:D50436; NID:g801871 !$#accession PC4124 !'##molecule_type protein !'##residues 65-79 ##label SA2 !'##experimental_source adrenal gland COMMENT Adrenodoxin is located in the mitochondrial matrix of !1steroidogenic tissues and functions as the common electron !1transporter from NADPH-adrenodoxin reductase to !1mitochondrial cytochromes P-450 which catalyze steroid !1hormone biosynthesis. CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; adrenal gland; electron transfer; iron-sulfur !1protein; metalloprotein; mitochondrion FEATURE !$1-64 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$65-188 #product adrenodoxin #status predicted #label MAT\ !$93-157 #domain ferredoxin [2Fe-2S] homology #label FER\ !$110,116,119,156 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 188 #molecular-weight 20135 #checksum 6720 SEQUENCE /// ENTRY S53524 #type complete TITLE adrenodoxin precursor - mouse ALTERNATE_NAMES adrenal ferredoxin; cytochrome P450-linked ferredoxin ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S53524; S60451; S60452 REFERENCE S53524 !$#authors Stromstedt, M.; Watermann, M.R. !$#journal Biochim. Biophys. Acta (1995) 1261:126-128 !$#title A full-length cDNA encoding mouse adrenodoxin. !$#cross-references MUID:95200960; PMID:7893748 !$#accession S53524 !'##molecule_type mRNA !'##residues 1-188 ##label STR !'##cross-references EMBL:L29123; NID:g457297; PIDN:AAA74303.1; !1PID:g457298 REFERENCE S60451 !$#authors Itoh, S.; Iemura, O.; Yamada, E.; Yoshimura, T.; Tsujikawa, !1K.; Kohama, Y.; Mimura, T. !$#journal Biochim. Biophys. Acta (1995) 1263:173-178 !$#title Mouse cytochrome P-450 linked ferredoxin: its cDNA cloning !1and inducibility by dibutyryladenosine 3',5'-cyclic !1monophosphate and forskolin. !$#cross-references MUID:95367595; PMID:7640310 !$#accession S60451 !'##molecule_type mRNA !'##residues 1-188 ##label ITO !'##cross-references EMBL:D43689; NID:g1065599; PIDN:BAA07786.1; !1PID:g1769821 !'##experimental_source clone F1-1 !$#accession S60452 !'##molecule_type mRNA !'##residues 1-188 ##label ITW !'##cross-references EMBL:D43690; NID:g1065600; PIDN:BAA07787.1; !1PID:g1769822 !'##experimental_source clone F41-1 GENETICS !$#genome nuclear CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein; mitochondrion FEATURE !$1-64 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$65-188 #product adrenodoxin #status predicted #label MAT\ !$93-157 #domain ferredoxin [2Fe-2S] homology #label FER\ !$110,116,119,156 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 188 #molecular-weight 20123 #checksum 5273 SEQUENCE /// ENTRY PXPSEP #type complete TITLE putidaredoxin [validated] - Pseudomonas putida ORGANISM #formal_name Pseudomonas putida DATE 24-Apr-1984 #sequence_revision 06-Feb-1995 #text_change 15-Sep-2000 ACCESSIONS JX0079; B35226; A00262 REFERENCE JX0078 !$#authors Koga, H.; Yamaguchi, E.; Matsunaga, K.; Aramaki, H.; !1Horiuchi, T. !$#journal J. Biochem. (1989) 106:831-836 !$#title Cloning and nucleotide sequences of NADH-putidaredoxin !1reductase gene (camA) and putidaredoxin gene (camB) involved !1in cytochrome P-450cam hydroxylase of Pseudomonas putida. !$#cross-references MUID:90130389; PMID:2613690 !$#accession JX0079 !'##molecule_type DNA !'##residues 1-107 ##label KOG !'##cross-references GB:D00528; NID:g216870; PIDN:BAA00414.1; !1PID:g216873 !'##experimental_source strain PpGl ATCC17453 REFERENCE A35226 !$#authors Peterson, J.A.; Lorence, M.C.; Amarneh, B. !$#journal J. Biol. Chem. (1990) 265:6066-6073 !$#title Putidaredoxin reductase and putidaredoxin. Cloning, sequence !1determination, and heterologous expression of the proteins. !$#cross-references MUID:90202873; PMID:2180940 !$#accession B35226 !'##molecule_type DNA !'##residues 1-107 ##label PET !'##cross-references GB:J05406; NID:g151111; PIDN:AAA25759.1; !1PID:g151113 REFERENCE A00262 !$#authors Tanaka, M.; Haniu, M.; Yasunobu, K.T.; Dus, K.; Gunsalus, !1I.C. !$#journal J. Biol. Chem. (1974) 249:3689-3701 !$#title The amino acid sequence of putidaredoxin, an iron-sulfur !1protein from Pseudomonas putida. !$#cross-references MUID:74268163; PMID:4833743 !$#accession A00262 !'##molecule_type protein !'##residues 2-14,'Q',16-107 ##label TAN REFERENCE A52668 !$#authors Pochapsky, T.C.; Ye, X.M.; Ratnaswamy, G.; Lyons, T.A. !$#submission submitted to the Brookhaven Protein Data Bank, July 1994 !$#cross-references PDB:1PUT !$#contents annotation; conformation by (1)H-NMR, residues 2-14,'Q', !116-107 REFERENCE A53724 !$#authors Pochapsky, T.C.; Ye, X.M.; Ratnaswamy, G.; Lyons, T.A. !$#journal Biochemistry (1994) 33:6424-6432 !$#title An NMR-derived model for the solution structure of oxidized !1putidaredoxin, a 2-Fe, 2-S ferredoxin from Pseudomonas. !$#cross-references MUID:95274325; PMID:7754712 !$#contents annotation; conformation by (1)H-NMR COMMENT Putidaredoxin, which is involved in camphor hydroxylation, !1is distantly related to adrenodoxin from adrenal !1mitochondria and to the 2Fe-2S ferredoxin from Halobacterium !1halobium. The gene is located in a bacterial plasmid. GENETICS !$#gene camB CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$2-107 #product putidaredoxin #status experimental #label !8MAT\ !$24-88 #domain ferredoxin [2Fe-2S] homology #label FER\ !$40,46,49,87 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8experimental SUMMARY #length 107 #molecular-weight 11550 #checksum 1946 SEQUENCE /// ENTRY E42971 #type complete TITLE terpredoxin - Pseudomonas sp. ORGANISM #formal_name Pseudomonas sp. DATE 04-Mar-1993 #sequence_revision 17-May-1996 #text_change 11-Jun-1999 ACCESSIONS E42971; S27655 REFERENCE A42971 !$#authors Peterson, J.A.; Lu, J.Y.; Geisselsoder, J.; Graham-Lorence, !1S.; Carmona, C.; Witney, F.; Lorence, M.C. !$#journal J. Biol. Chem. (1992) 267:14193-14203 !$#title Cytochrome P-450terp. Isolation and purification of the !1protein and cloning and sequencing of its operon. !$#cross-references MUID:92332528; PMID:1629218 !$#accession E42971 !'##molecule_type DNA; protein !'##residues 1-106 ##label PET !'##cross-references EMBL:M91440; NID:g151584; PIDN:AAA25998.1; !1PID:g151589 !'##note submitted to the EMBL Data Library, April 1992 !'##note sequence extracted from NCBI backbone (NCBIP:108477) and !1corrected to correspond with the published sequence CLASSIFICATION #superfamily ferredoxin [2Fe-2S]; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$2-106 #product terpredoxin #status experimental #label MAT\ !$24-88 #domain ferredoxin [2Fe-2S] homology #label FER\ !$40,46,49,87 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 106 #molecular-weight 11229 #checksum 6630 SEQUENCE /// ENTRY FEPE #type complete TITLE ferredoxin 2[4Fe-4S] [validated] - Peptostreptococcus asaccharolyticus ORGANISM #formal_name Peptostreptococcus asaccharolyticus DATE 24-Apr-1984 #sequence_revision 23-Mar-1995 #text_change 20-Apr-2000 ACCESSIONS A00196 REFERENCE A92040 !$#authors Tsunoda, J.N.; Yasunobu, K.T.; Whiteley, H.R. !$#journal J. Biol. Chem. (1968) 243:6262-6272 !$#title Non-heme iron proteins. IX. The amino acid sequence of !1ferredoxin from Micrococcus aerogenes. !$#cross-references MUID:69054261; PMID:5723466 !$#note the source is designated as Micrococcus aerogenes !$#accession A00196 !'##molecule_type protein !'##residues 1-21,23-24,'Q',26-55 ##label TSU REFERENCE A44688 !$#authors Backes, G.; Mino, Y.; Loehr, T.M.; Meyer, T.E.; Cusanovich, !1M.A.; Sweeney, W.V.; Adman, E.T.; Sanders-Loehr, J. !$#journal J. Am. Chem. Soc. (1991) 113:2055-2064 !$#title The environment of Fe4S4 clusters in ferredoxins and !1high-potential iron proteins. New information from x-ray !1crystallography and resonance Raman spectroscopy. !$#contents annotation; X-ray crystallography, 2.0 angstroms; sequence !1revision !$#note sequence correction confirmed by peptide sequencing REFERENCE A50836 !$#authors Adman, E.T.; Sieker, L.C.; Jensen, L.H. !$#submission submitted to the Brookhaven Protein Data Bank, August 1976 !$#cross-references PDB:1FDX !$#contents annotation; X-ray crystallography, 2.0 angstroms, residues !11-21,'I',23-24,26-55 REFERENCE A92192 !$#authors Adman, E.T.; Sieker, L.C.; Jensen, L.H. !$#journal J. Biol. Chem. (1976) 251:3801-3806 !$#title Structure of Peptococcus aerogenes ferredoxin. Refinement at !12 angstroms resolution. !$#cross-references MUID:76213238; PMID:932007 !$#contents annotation; X-ray crystallography, 2.0 angstroms REFERENCE A92136 !$#authors Adman, E.T.; Sieker, L.C.; Jensen, L.H. !$#journal J. Biol. Chem. (1973) 248:3987-3996 !$#title The structure of a bacterial ferredoxin. !$#cross-references MUID:73187389; PMID:4708097 !$#contents annotation; X-ray crystallography, 2.8 angstroms CLASSIFICATION #superfamily ferredoxin 2[4Fe-4S]; ferredoxin 2[4Fe-4S] !1homology KEYWORDS 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-54 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$8,11,14,46 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8experimental\ !$18,36,39,42 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8experimental SUMMARY #length 55 #molecular-weight 5556 #checksum 3559 SEQUENCE /// ENTRY FEQFR #type complete TITLE ferredoxin 2[4Fe-4S] - Rhodospirillum rubrum ORGANISM #formal_name Rhodospirillum rubrum DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 18-Sep-1998 ACCESSIONS A00197 REFERENCE A00197 !$#authors Matsubara, H.; Inoue, K.; Hase, T.; Hiura, H.; Kakuno, T.; !1Yamashita, J.; Horio, T. !$#journal J. Biochem. (1983) 93:1385-1390 !$#title Structure of the extracellular ferredoxin from !1Rhodospirillum rubrum: close similarity to clostridial !1ferredoxins. !$#cross-references MUID:83290779; PMID:6411697 !$#accession A00197 !'##molecule_type protein !'##residues 1-55 ##label MAT !'##note this is one of the four ferredoxins, most likely ferredoxin I, !1of R. rubrum CLASSIFICATION #superfamily ferredoxin 2[4Fe-4S]; ferredoxin 2[4Fe-4S] !1homology KEYWORDS 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-55 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$8,11,14,47 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$18,37,40,43 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 55 #molecular-weight 5567 #checksum 3491 SEQUENCE /// ENTRY FECLCP #type complete TITLE ferredoxin 2[4Fe-4S] [validated] - Clostridium pasteurianum ORGANISM #formal_name Clostridium pasteurianum DATE 07-May-1981 #sequence_revision 14-Nov-1997 #text_change 20-Apr-2000 ACCESSIONS A94028; A90550; A00198 REFERENCE A94028 !$#authors Graves, M.C.; Mullenbach, G.T.; Rabinowitz, J.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:1653-1657 !$#title Cloning and nucleotide sequence determination of the !1Clostridium pasteurianum ferredoxin gene. !$#cross-references MUID:85166189; PMID:3856844 !$#accession A94028 !'##molecule_type DNA !'##residues 1-56 ##label GRA !'##cross-references GB:M11214; GB:M13633; GB:M13682; NID:g144805; !1PIDN:AAA83524.1; PID:g144806 !'##experimental_source ATCC:6013; soil spore !'##note initiator Met not shown REFERENCE A90550 !$#authors Tanaka, M.; Nakashima, T.; Benson, A.M.; Mower, H.F.; !1Yasunobu, K.T. !$#journal Biochemistry (1966) 5:1666-1680 !$#title The amino acid sequence of Clostridium pasteurianum !1ferredoxin. !$#cross-references MUID:67120720; PMID:5335811 !$#accession A90550 !'##molecule_type protein !'##residues 2-56 ##label TAN REFERENCE A65284 !$#authors Bertini, I.; Donaire, A.; Feinberg, B.A.; Luchinat, C.; !1Piccioli, M.; Yuan, H. !$#submission submitted to the Brookhaven Protein Data Bank, June 1995 !$#cross-references PDB:1CLF !$#contents annotation; conformation by (1)H-NMR, residues 2-56 REFERENCE A58660 !$#authors Bertini, I.; Donaire, A.; Feinberg, B.A.; Luchinat, C.; !1Piccioli, M.; Yuan, H. !$#journal Eur. J. Biochem. (1995) 232:192-205 !$#title Solution structure of the oxidized 2[4Fe-4S] ferredoxin from !1Clostridium pasteurianum. !$#cross-references MUID:96048047; PMID:7556151 !$#contents annotation; conformation by (1)H-NMR REFERENCE A58659 !$#authors Scrofani, S.D.B.; Brereton, P.S.; Hamer, A.M.; Lavery, M.J.; !1McDowall, S.G.; Vincent, G.A.; Brownlee, R.T.C.; Hoogenraad, !1N.J.; Sadek, M.; Wedd, A.G. !$#journal Biochemistry (1994) 33:14486-14495 !$#title Comparison of native and mutant proteins provides a !1sequence-specific assignment of the cysteinyl ligand proton !1NMR resonances in the 2[Fe-4-S-4] ferredoxin from !1Clostridium pasteurianum. !$#cross-references MUID:95072020; PMID:7981209 !$#contents annotation; conformation by (1)H-NMR CLASSIFICATION #superfamily ferredoxin 2[4Fe-4S]; ferredoxin 2[4Fe-4S] !1homology KEYWORDS 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$2-56 #product ferredoxin 2[4Fe-4S] #status experimental !8#label MAT\ !$2-56 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$9,12,15,48 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8experimental\ !$19,38,41,44 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8experimental SUMMARY #length 56 #molecular-weight 5630 #checksum 8434 SEQUENCE /// ENTRY FECLCB #type complete TITLE ferredoxin 2[4Fe-4S] - Clostridium butyricum ORGANISM #formal_name Clostridium butyricum DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 18-Sep-1998 ACCESSIONS A00199 REFERENCE A00199 !$#authors Benson, A.M.; Mower, H.F.; Yasunobu, K.T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1966) 55:1532-1535 !$#title The amino acid sequence of Clostridium butyricum ferredoxin. !$#cross-references MUID:67125829; PMID:5227671 !$#accession A00199 !'##molecule_type protein !'##residues 1-55 ##label BEN CLASSIFICATION #superfamily ferredoxin 2[4Fe-4S]; ferredoxin 2[4Fe-4S] !1homology KEYWORDS 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-55 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$8,11,14,47 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$18,37,40,43 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 55 #molecular-weight 5498 #checksum 4122 SEQUENCE /// ENTRY FECLCE #type complete TITLE ferredoxin 2[4Fe-4S] - Clostridium sp. ORGANISM #formal_name Clostridium sp. DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 18-Sep-1998 ACCESSIONS A00200 REFERENCE A00200 !$#authors Tanaka, M.; Haniu, M.; Yasunobu, K.T.; Jones, J.B.; !1Stadtman, T.C. !$#journal Biochemistry (1974) 13:5284-5289 !$#title Amino acid sequence determination of the Clostridium M-E !1ferredoxin and a comment on the role of the aromatic !1residues in the clostridial ferredoxins. !$#cross-references MUID:75054829; PMID:4433520 !$#accession A00200 !'##molecule_type protein !'##residues 1-55 ##label TAN !'##experimental_source strain M-E CLASSIFICATION #superfamily ferredoxin 2[4Fe-4S]; ferredoxin 2[4Fe-4S] !1homology KEYWORDS 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-55 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$8,11,14,47 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$18,37,40,43 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 55 #molecular-weight 5622 #checksum 2187 SEQUENCE /// ENTRY FECLCU #type complete TITLE ferredoxin 2[4Fe-4S] [validated] - Clostridium acidiurici ORGANISM #formal_name Clostridium acidiurici DATE 24-Apr-1984 #sequence_revision 22-Apr-1995 #text_change 20-Apr-2000 ACCESSIONS S36790; A00201 REFERENCE S36790 !$#authors Meyer, J.; Moulis, J.M.; Scherrer, N.; Gagnon, J.; Ulrich, !1J. !$#journal Biochem. J. (1993) 294:622-623 !$#title Sequences of clostridial ferredoxins: determination of the !1Clostridium sticklandii sequence and correction of the !1Clostridium acidurici sequence. !$#cross-references MUID:93384542; PMID:8373379 !$#accession S36790 !'##molecule_type protein !'##residues 1-55 ##label MEY REFERENCE A00201 !$#authors Rall, S.C.; Bolinger, R.E.; Cole, R.D. !$#journal Biochemistry (1969) 8:2486-2496 !$#title The amino acid sequence of ferredoxin from Clostridium !1acidi-urici. !$#cross-references MUID:69253175; PMID:5799135 !$#accession A00201 !'##molecule_type protein !'##residues 1-14,'D',16-20,'D',22-24,'Q',26-27,'S',29-55 ##label RAL REFERENCE A52567 !$#authors Duee, E.; Fanchon, E.; Vicat, J.; Sieker, L.C.; Meyer, J.; !1Moulis, J.M. !$#submission submitted to the Brookhaven Protein Data Bank, March 1994 !$#cross-references PDB:1FDN !$#contents annotation; X-ray crystallography, 1.84 angstroms, residues !11-55 !$#note ATCC:7906 REFERENCE A65570 !$#authors Tranqui, D.; Jesior, J.C. !$#submission submitted to the Brookhaven Protein Data Bank, September !11994 !$#cross-references PDB:1FCA !$#contents annotation; X-ray crystallography, 1.8 angstroms, residues !11-20,'D',22-24,'Q',26,'GS',29-55 CLASSIFICATION #superfamily ferredoxin 2[4Fe-4S]; ferredoxin 2[4Fe-4S] !1homology KEYWORDS 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-55 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$8,11,14,47 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8experimental\ !$18,37,40,43 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8experimental SUMMARY #length 55 #molecular-weight 5539 #checksum 3392 SEQUENCE /// ENTRY FECLCT #type complete TITLE ferredoxin 2[4Fe-4S] - Clostridium thermosaccharolyticum ORGANISM #formal_name Clostridium thermosaccharolyticum, Clostridium tartarivorum DATE 24-Apr-1984 #sequence_revision 04-Dec-1986 #text_change 18-Sep-1998 ACCESSIONS A92138; A92086; A00202 REFERENCE A92138 !$#authors Tanaka, M.; Haniu, M.; Yasunobu, K.T.; Himes, R.H.; Akagi, !1J.M. !$#journal J. Biol. Chem. (1973) 248:5215-5217 !$#title The primary structure of the Clostridium !1thermosaccharolyticum ferredoxin, a heat-stable ferredoxin. !$#cross-references MUID:74071583; PMID:4768897 !$#accession A92138 !'##molecule_type protein !'##residues 1-55 ##label TAN REFERENCE A92086 !$#authors Tanaka, M.; Haniu, M.; Matsueda, G.; Yasunobu, K.T.; Himes, !1R.H.; Akagi, J.M.; Barnes, E.M.; Devanathan, T. !$#journal J. Biol. Chem. (1971) 246:3953-3960 !$#title The primary structure of the Clostridium tartarivorum !1ferredoxin, a heat-stable ferredoxin. !$#cross-references MUID:71259897; PMID:4934841 !$#accession A92086 !'##molecule_type protein !'##residues 1-30,'Q',32-43,'Q',45-55 ##label TA2 !'##note the authors considered C. tartarivorum to be a separate species CLASSIFICATION #superfamily ferredoxin 2[4Fe-4S]; ferredoxin 2[4Fe-4S] !1homology KEYWORDS 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-55 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$8,11,14,47 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$18,37,40,43 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 55 #molecular-weight 5545 #checksum 1513 SEQUENCE /// ENTRY FEME #type complete TITLE ferredoxin 2[4Fe-4S] - Megasphaera elsdenii ORGANISM #formal_name Megasphaera elsdenii DATE 13-Jul-1981 #sequence_revision 13-Jul-1981 #text_change 18-Sep-1998 ACCESSIONS A00203 REFERENCE A00203 !$#authors Azari, P.; Glantz, M.; Tsunoda, J.; Yasunobu, K.T. !$#citation unpublished results, cited by Yasunobu, K.T., and Tanaka, !1M., Syst. Zool. 22, 570-589, 1973 !$#accession A00203 !'##molecule_type protein !'##residues 1-54 ##label AZA CLASSIFICATION #superfamily ferredoxin 2[4Fe-4S]; ferredoxin 2[4Fe-4S] !1homology KEYWORDS 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-54 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$8,11,14,46 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$18,36,39,42 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 54 #molecular-weight 5430 #checksum 9079 SEQUENCE /// ENTRY FEMZB #type complete TITLE ferredoxin 2[4Fe-4S] - Methanosarcina barkeri ORGANISM #formal_name Methanosarcina barkeri DATE 05-Apr-1983 #sequence_revision 05-Apr-1983 #text_change 18-Sep-1998 ACCESSIONS A00204 REFERENCE A00204 !$#authors Hausinger, R.P.; Moura, I.; Moura, J.J.G.; Xavier, A.V.; !1Santos, M.H.; LeGall, J.; Howard, J.B. !$#journal J. Biol. Chem. (1982) 257:14192-14197 !$#title Amino acid sequence of a 3Fe:3S ferredoxin from the !1"archaebacterium" Methanosarcina barkeri (DSM 800). !$#cross-references MUID:83056954; PMID:6754724 !$#accession A00204 !'##molecule_type protein !'##residues 1-59 ##label HAU !'##experimental_source strain DSM 800 CLASSIFICATION #superfamily ferredoxin 2[4Fe-4S]; ferredoxin 2[4Fe-4S] !1homology KEYWORDS 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$2-58 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$9,12,15,50 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$19,40,43,46 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 59 #molecular-weight 6121 #checksum 553 SEQUENCE /// ENTRY FECI #type complete TITLE ferredoxin 2[4Fe-4S] I - Chlorobium limicola ORGANISM #formal_name Chlorobium limicola DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 18-Sep-1998 ACCESSIONS A00206 REFERENCE A00206 !$#authors Tanaka, M.; Haniu, M.; Yasunobu, K.T.; Evans, M.C.W.; Rao, !1K.K. !$#journal Biochemistry (1974) 13:2953-2959 !$#title Amino acid sequence of ferredoxin from a photosynthetic !1green bacterium, Chlorobium limicola. !$#cross-references MUID:74271985; PMID:4407619 !$#accession A00206 !'##molecule_type protein !'##residues 1-60 ##label TAN CLASSIFICATION #superfamily ferredoxin 2[4Fe-4S]; ferredoxin 2[4Fe-4S] !1homology KEYWORDS 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-60 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$8,11,14,52 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$18,37,40,48 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 60 #molecular-weight 6223 #checksum 730 SEQUENCE /// ENTRY FECF #type complete TITLE ferredoxin 2[4Fe-4S] - Chlorobium sp. ORGANISM #formal_name Chlorobium sp. DATE 30-Jun-1979 #sequence_revision 23-Oct-1981 #text_change 18-Sep-1998 ACCESSIONS A00207 REFERENCE A00207 !$#authors Hase, T.; Wakabayashi, S.; Matsubara, H.; Evans, M.C.W.; !1Jennings, J.V. !$#journal J. Biochem. (1978) 83:1321-1325 !$#title Amino acid sequence of a ferredoxin from Chlorobium !1thiosulfatophilum strain Tassajara, a photosynthetic green !1sulfur bacterium. !$#cross-references MUID:78194080; PMID:659399 !$#accession A00207 !'##molecule_type protein !'##residues 1-61 ##label HAS !'##experimental_source strain Tassajara !'##note the source was designated as Chlorobium thiosulfatophilum CLASSIFICATION #superfamily ferredoxin 2[4Fe-4S]; ferredoxin 2[4Fe-4S] !1homology KEYWORDS 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-61 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$8,11,14,53 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$18,37,40,49 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 61 #molecular-weight 6140 #checksum 9569 SEQUENCE /// ENTRY FECI2 #type complete TITLE ferredoxin 2[4Fe-4S] II - Chlorobium limicola ORGANISM #formal_name Chlorobium limicola DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 18-Sep-1998 ACCESSIONS A00208 REFERENCE A00208 !$#authors Tanaka, M.; Haniu, M.; Yasunobu, K.T.; Evans, M.C.W.; Rao, !1K.K. !$#journal Biochemistry (1975) 14:1938-1943 !$#title The amino acid sequence of ferredoxin II from Chlorobium !1limicola, a photosynthetic green bacterium. !$#cross-references MUID:75146531; PMID:1125205 !$#accession A00208 !'##molecule_type protein !'##residues 1-61 ##label TAN CLASSIFICATION #superfamily ferredoxin 2[4Fe-4S]; ferredoxin 2[4Fe-4S] !1homology KEYWORDS 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-61 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$8,11,14,53 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$18,37,40,49 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 61 #molecular-weight 6593 #checksum 3908 SEQUENCE /// ENTRY FERF1P #type complete TITLE ferredoxin 2[4Fe-4S] I - Rhodopseudomonas palustris ORGANISM #formal_name Rhodopseudomonas palustris DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 18-Sep-1998 ACCESSIONS A00209 REFERENCE A00209 !$#authors Minami, Y.; Wakabayashi, S.; Yamada, F.; Wada, K.; Zumft, !1W.G.; Matsubara, H. !$#journal J. Biochem. (1984) 96:585-592 !$#title Ferredoxins from the photosynthetic purple non-sulfur !1bacterium Rhodopseudomonas palustris. Isolation and amino !1acid sequence of ferredoxin I. !$#cross-references MUID:85054727; PMID:6389527 !$#accession A00209 !'##molecule_type protein !'##residues 1-63 ##label MIN CLASSIFICATION #superfamily ferredoxin 2[4Fe-4S]; ferredoxin 2[4Fe-4S] !1homology KEYWORDS 4Fe-4S; duplication; electron transfer; iron-sulfur protein; !1metalloprotein; photosynthesis FEATURE !$2-62 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$9,12,15,54 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$19,38,41,50 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 63 #molecular-weight 6718 #checksum 4543 SEQUENCE /// ENTRY FERF1C #type complete TITLE ferredoxin 2[4Fe-4S] I - Rhodobacter capsulatus ORGANISM #formal_name Rhodobacter capsulatus DATE 27-Feb-1990 #sequence_revision 27-Jan-1995 #text_change 24-Sep-1999 ACCESSIONS A33498; S08394; C39857; B39519; S39898; JX0133 REFERENCE A33498 !$#authors Schatt, E.; Jouanneau, Y.; Vignais, P.M. !$#journal J. Bacteriol. (1989) 171:6218-6226 !$#title Molecular cloning and sequence analysis of the structural !1gene of ferredoxin I from the photosynthetic bacterium !1Rhodobacter capsulatus. !$#cross-references MUID:90036712; PMID:2681157 !$#accession A33498 !'##molecule_type DNA !'##residues 1-65 ##label SCH !'##cross-references GB:M31073; NID:g151918; PIDN:AAA26111.1; !1PID:g151919 REFERENCE S08393 !$#authors Saeki, K.; Miyatake, Y.; Young, D.A.; Marrs, B.L.; !1Matsubara, H. !$#journal Nucleic Acids Res. (1990) 18:1060 !$#title A plant-ferredoxin-like gene is located upstream of !1ferredoxin I gene (fdxN) of Rhodobacter capsulatus. !$#cross-references MUID:90192101; PMID:2315024 !$#accession S08394 !'##molecule_type DNA !'##residues 1-65 ##label SA3 !'##cross-references EMBL:X51316; NID:g46141; PIDN:CAA35699.1; !1PID:g46143 REFERENCE A39857 !$#authors Saeki, K.; Suetsugu, Y.; Tokuda, K.; Miyatake, Y.; Young, !1D.A.; Marrs, B.L.; Matsubara, H. !$#journal J. Biol. Chem. (1991) 266:12889-12895 !$#title Genetic analysis of functional differences among distinct !1ferredoxins in Rhodobacter capsulatus. !$#cross-references MUID:91302301; PMID:2071578 !$#accession C39857 !'##molecule_type DNA !'##residues 1-65 ##label SAE !'##cross-references GB:X51316; GB:S42008; NID:g46141; PIDN:CAA35699.1; !1PID:g46143 REFERENCE A39519 !$#authors Grabau, C.; Schatt, E.; Jouanneau, Y.; Vignais, P.M. !$#journal J. Biol. Chem. (1991) 266:3294-3299 !$#title A new [2Fe-2S] ferredoxin from Rhodobacter capsulatus. !1Coexpression with a 2[4Fe-4S] ferredoxin in Escherichia !1coli. !$#cross-references MUID:91131639; PMID:1847145 !$#accession B39519 !'##molecule_type DNA !'##residues 1-8 ##label GRA !'##cross-references GB:M59855; GB:J05743; NID:g151915; PIDN:AAA26110.1; !1PID:g151917 REFERENCE S39892 !$#authors Schmehl, M.; Jahn, A.; Meyer zu Vilsendorf, A.; Hennecke, !1S.; Masepohl, B.; Schuppler, M.; Marxer, M.; Oelze, J.; !1Klipp, W. !$#journal Mol. Gen. Genet. (1993) 241:602-615 !$#title Identification of a new class of nitrogen fixation genes in !1Rhodobacter capsulatus: a putative membrane complex involved !1in electron transport to nitrogenase. !$#cross-references MUID:94088454; PMID:8264535 !$#accession S39898 !'##status preliminary !'##molecule_type DNA !'##residues 1-65 ##label SC2 !'##cross-references EMBL:X72888; NID:g435523; PIDN:CAA51404.1; !1PID:g435530 REFERENCE JX0133 !$#authors Saeki, K.; Suetsugu, Y.; Yao, Y.; Horio, T.; Marrs, B.L.; !1Matsubara, H. !$#journal J. Biochem. (1990) 108:475-482 !$#title Two distinct ferredoxins from Rhodobacter capsulatus: !1complete amino acid sequences and molecular evolution. !$#cross-references MUID:91115797; PMID:2277040 !$#accession JX0133 !'##molecule_type protein !'##residues 2-65 ##label SA2 GENETICS !$#gene fdxN CLASSIFICATION #superfamily ferredoxin 2[4Fe-4S]; ferredoxin 2[4Fe-4S] !1homology KEYWORDS 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$2-65 #product ferredoxin 2[4Fe-4S] I #status experimental !8#label MAT\ !$3-63 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$10,13,16,55 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$20,39,42,51 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 65 #molecular-weight 6864 #checksum 5833 SEQUENCE /// ENTRY FERMN #type complete TITLE ferredoxin 2[4Fe-4S] - Rhizobium meliloti ORGANISM #formal_name Rhizobium meliloti DATE 21-May-1990 #sequence_revision 27-Jan-1995 #text_change 11-Jun-1999 ACCESSIONS C32361; JE0034; S04411 REFERENCE A91884 !$#authors Mulligan, M.E.; Buikema, W.J.; Haselkorn, R. !$#journal J. Bacteriol. (1988) 170:4406-4410 !$#title Bacterial-type ferredoxin genes in the nitrogen fixation !1regions of the cyanobacterium Anabaena sp. strain PCC 7120 !1and Rhizobium meliloti. !$#cross-references MUID:88314954; PMID:2842320 !$#accession C32361 !'##molecule_type DNA !'##residues 1-64 ##label MUL !'##cross-references GB:M21841; NID:g152194; PIDN:AAA26268.1; !1PID:g152195 REFERENCE JE0034 !$#authors Klipp, W.; Reilaender, H.; Schlueter, A.; Krey, R.; Puehler, !1A. !$#journal Mol. Gen. Genet. (1989) 216:293-302 !$#title The Rhizobium meliloti fdxN gene encoding a ferredoxin-like !1protein is necessary for nitrogen fixation and is !1cotranscribed with nifA and nifB. !$#cross-references MUID:89313667; PMID:2747618 !$#accession JE0034 !'##molecule_type DNA !'##residues 1-64 ##label KLI !'##cross-references GB:X52662; NID:g288340; PIDN:CAA36890.1; !1PID:g288342 !'##experimental_source strain 2011 GENETICS !$#gene fdxN CLASSIFICATION #superfamily ferredoxin 2[4Fe-4S]; ferredoxin 2[4Fe-4S] !1homology KEYWORDS 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$2-64 #product ferredoxin 2[4Fe-4S] I #status predicted !8#label MAT\ !$3-63 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$10,13,16,55 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$20,39,42,51 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 64 #molecular-weight 6829 #checksum 6033 SEQUENCE /// ENTRY FEKRV #type complete TITLE ferredoxin 2[4Fe-4S] [validated] - Chromatium vinosum ORGANISM #formal_name Chromatium vinosum DATE 13-Jul-1981 #sequence_revision 30-Jan-1998 #text_change 20-Apr-2000 ACCESSIONS S72167; S78121; A00210 REFERENCE S72166 !$#authors Moulis, J.M. !$#journal Biochim. Biophys. Acta (1996) 1308:12-14 !$#title Molecular cloning and expression of the gene encoding !1Chromatium vinosum 2[4Fe-4S] ferredoxin. !$#cross-references MUID:96328257; PMID:8765743 !$#accession S72167 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-83 ##label MOU !'##cross-references EMBL:U45327; NID:g1518925; PIDN:AAC44333.1; !1PID:g1518927 !$#accession S78121 !'##molecule_type protein !'##residues 2-18 ##label MOL REFERENCE A00210 !$#authors Hase, T.; Matsubara, H.; Evans, M.C.W. !$#journal J. Biochem. (1977) 81:1745-1749 !$#title Amino acid sequence of Chromatium vinosum ferredoxin: !1revisions. !$#cross-references MUID:77249448; PMID:893371 !$#accession A00210 !'##molecule_type protein !'##residues 2-7,'Q',9-12,'N',14-15,'Q',17-83 ##label HAS REFERENCE A65183 !$#authors Dauter, Z.; Wilson, K.S.; Sieker, L.C.; Moulis, J.M. !$#submission submitted to the Brookhaven Protein Data Bank, April 1996 !$#cross-references PDB:1BLU !$#contents annotation; X-ray crystallography, 2.1 angstroms, residues !12-81 REFERENCE A56076 !$#authors Huber, J.G.; Gaillard, J.; Moulis, J.M. !$#journal Biochemistry (1995) 34:194-205 !$#title NMR of Chromatium vinosum ferredoxin: evidence for !1structural inequivalence and impeded electron transfer !1between the two [4Fe-4S] clusters. !$#cross-references MUID:95118987; PMID:7819196 !$#contents annotation; conformation by (1)H-NMR and (13)C-NMR CLASSIFICATION #superfamily ferredoxin 2[4Fe-4S]; ferredoxin 2[4Fe-4S] !1homology KEYWORDS 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$2-83 #product ferredoxin 2[4Fe-4S] #status experimental !8#label MAT\ !$2-62 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$9,12,15,54 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8experimental\ !$19,38,41,50 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8experimental SUMMARY #length 83 #molecular-weight 9189 #checksum 2112 SEQUENCE /// ENTRY E64554 #type complete TITLE ferredoxin 2[4Fe-4S] HP0277 [similarity] - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 21-Jul-2000 ACCESSIONS E64554 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession E64554 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-84 ##label TOM !'##cross-references GB:AE000546; GB:AE000511; NID:g2313363; !1PIDN:AAD07340.1; PID:g2313367; TIGR:HP0277 CLASSIFICATION #superfamily ferredoxin 2[4Fe-4S]; ferredoxin 2[4Fe-4S] !1homology KEYWORDS 4Fe-4S; iron-sulfur protein; metalloprotein FEATURE !$2-63 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$9,12,15,55 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$19,38,41,51 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 84 #molecular-weight 9514 #checksum 2903 SEQUENCE /// ENTRY E71954 #type complete TITLE ferredoxin 2[4Fe-4S] jhp0262 [similarity] - Helicobacter pylori (strain J99) ORGANISM #formal_name Helicobacter pylori #variety strain J99 DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 21-Jul-2000 ACCESSIONS E71954 REFERENCE A71800 !$#authors Alm, R.A.; Ling, L.S.L.; Moir, D.T.; King, B.L.; Brown, !1E.D.; Doig, P.C.; Smith, D.R.; Noonan, B.; Guild, B.C.; !1deJonge, B.L.; Carmel, G.; Tummino, P.J.; Caruso, A.; !1Uria-Nickelsen, M.; Mills, D.M.; Ives, C.; Gibson, R.; !1Merberg, D.; Mills, S.D.; Jiang, Q.; Taylor, D.E.; Vovis, !1G.F.; Trust, T.J. !$#journal Nature (1999) 397:176-180 !$#title Genomic sequence comparison of two unrelated isolates of the !1human gastric pathogen Helicobacter pylori. !$#cross-references MUID:99120557; PMID:9923682 !$#accession E71954 !'##molecule_type DNA !'##residues 1-84 ##label ARN !'##cross-references GB:AE001463; GB:AE001439; NID:g4154775; !1PIDN:AAD05841.1; PID:g4154783 !'##experimental_source strain J99 GENETICS !$#gene jhp0262 CLASSIFICATION #superfamily ferredoxin 2[4Fe-4S]; ferredoxin 2[4Fe-4S] !1homology KEYWORDS 4Fe-4S; iron-sulfur protein; metalloprotein FEATURE !$2-63 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$9,12,15,55 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$19,38,41,51 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 84 #molecular-weight 9513 #checksum 2843 SEQUENCE /// ENTRY FEAIN #type complete TITLE ferredoxin 2[4Fe-4S] fdxN - Anabaena sp. (strain PCC 7120) ORGANISM #formal_name Anabaena sp. DATE 21-May-1990 #sequence_revision 27-Jan-1995 #text_change 11-Jun-1999 ACCESSIONS A32361; B34443 REFERENCE A91884 !$#authors Mulligan, M.E.; Buikema, W.J.; Haselkorn, R. !$#journal J. Bacteriol. (1988) 170:4406-4410 !$#title Bacterial-type ferredoxin genes in the nitrogen fixation !1regions of the cyanobacterium Anabaena sp. strain PCC 7120 !1and Rhizobium meliloti. !$#cross-references MUID:88314954; PMID:2842320 !$#accession A32361 !'##molecule_type DNA !'##residues 1-116 ##label MUL !'##cross-references GB:J05111; NID:g142034; PIDN:AAA22005.1; !1PID:g142036 REFERENCE A34443 !$#authors Mulligan, M.E.; Haselkorn, R. !$#journal J. Biol. Chem. (1989) 264:19200-19207 !$#title Nitrogen fixation (nif) genes of the cyanobacterium Anabaena !1species strain PCC 7120. The nifB-fdxN-nifS-nifU operon. !$#cross-references MUID:90037054; PMID:2553733 !$#accession B34443 !'##molecule_type DNA !'##residues 98-116 ##label MU2 !'##cross-references GB:J05111; GB:J01538; GB:M21840; GB:X05593; !1GB:X05595 GENETICS !$#gene fdxN CLASSIFICATION #superfamily ferredoxin 2[4Fe-4S]; ferredoxin 2[4Fe-4S] !1homology KEYWORDS 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$2-116 #product ferredoxin 2[4Fe-4S] fdxN #status predicted !8#label MAT\ !$2-64 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$9,12,15,56 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$19,39,42,52 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 116 #molecular-weight 13192 #checksum 3104 SEQUENCE /// ENTRY FERF3C #type complete TITLE ferredoxin 2[4Fe-4S] III - Rhodobacter capsulatus ALTERNATE_NAMES dimeric ferredoxin ORGANISM #formal_name Rhodobacter capsulatus DATE 08-Dec-1989 #sequence_revision 27-Jan-1995 #text_change 11-Jun-1999 ACCESSIONS B32308; A46701 REFERENCE A32308 !$#authors Moreno-Vivian, C.; Hennecke, S.; Puehler, A.; Klipp, W. !$#journal J. Bacteriol. (1989) 171:2591-2598 !$#title Open reading frame 5 (ORF5), encoding a ferredoxinlike !1protein, and nifQ are cotranscribed with nifE, nifN, nifX, !1and ORF4 in Rhodobacter capsulatus. !$#cross-references MUID:89213944; PMID:2708314 !$#accession B32308 !'##molecule_type DNA !'##residues 1-102 ##label MOR !'##cross-references GB:M26323; NID:g341472; PIDN:AAA26146.1; !1PID:g516637 REFERENCE A46701 !$#authors Jouanneau, Y.; Meyer, C.; Gaillard, J.; Forest, E.; Gagnon, !1J. !$#journal J. Biol. Chem. (1993) 268:10636-10644 !$#title Purification and characterization of a novel dimeric !1ferredoxin (FdIII) from Rhodobacter capsulatus. !$#cross-references MUID:93252956; PMID:8387524 !$#accession A46701 !'##molecule_type protein !'##residues 3-102 ##label JOU !'##experimental_source strain B10 !'##note sequence extracted from NCBI backbone (NCBIP:131349) COMPLEX homodimer CLASSIFICATION #superfamily ferredoxin 2[4Fe-4S]; ferredoxin 2[4Fe-4S] !1homology KEYWORDS 4Fe-4S; homodimer; iron-sulfur protein; metalloprotein FEATURE !$3-102 #product ferredoxin 2[4Fe-4S] III #status !8experimental #label MAT\ !$20-99 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$27,30,33,91 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$37,81,84,87 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 102 #molecular-weight 10951 #checksum 1114 SEQUENCE /// ENTRY FERMX #type complete TITLE ferredoxin [4Fe-4S] - Rhizobium meliloti ORGANISM #formal_name Rhizobium meliloti DATE 05-Oct-1988 #sequence_revision 27-Jan-1995 #text_change 11-Jun-1999 ACCESSIONS D26952; A26933 REFERENCE A26952 !$#authors Earl, C.D.; Ronson, C.W.; Ausubel, F.M. !$#journal J. Bacteriol. (1987) 169:1127-1136 !$#title Genetic and structural analysis of the Rhizobium meliloti !1fixA, fixB, fixC, and fixX genes. !$#cross-references MUID:87137267; PMID:3029021 !$#accession D26952 !'##molecule_type DNA !'##residues 1-98 ##label EAR !'##cross-references GB:M15546; NID:g340664; PIDN:AAA21771.1; !1PID:g551201 !'##experimental_source strain 1021 REFERENCE A26933 !$#authors Dusha, I.; Kovalenko, S.; Banfalvi, Z.; Kondorosi, A. !$#journal J. Bacteriol. (1987) 169:1403-1409 !$#title Rhizobium meliloti insertion element ISRm2 and its use for !1identification of the fixX gene. !$#cross-references MUID:87165742; PMID:3031010 !$#accession A26933 !'##molecule_type DNA !'##residues 1-61,'I',63-96,'S',98 ##label DUS !'##cross-references GB:M15787; NID:g152228; PIDN:AAA26282.1; !1PID:g152229 !'##experimental_source strain 41 !'##note the authors translated the codon TCC for residue 97 as Phe GENETICS !$#gene fixX CLASSIFICATION #superfamily ferredoxin 2[4Fe-4S]; ferredoxin 2[4Fe-4S] !1homology KEYWORDS 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$2-98 #product ferredoxin [4Fe-4S] #status predicted #label !8MAT\ !$29-84 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$46,66,69,72 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 98 #molecular-weight 10937 #checksum 1483 SEQUENCE /// ENTRY JC1001 #type complete TITLE ferredoxin [4Fe-4S] fixX - Rhizobium leguminosarum plasmid pRL6JI ORGANISM #formal_name Rhizobium leguminosarum DATE 03-Dec-1999 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS B25878; JC1001 REFERENCE A93661 !$#authors Gronger, P.; Manian, S.S.; Reilander, H.; O'Connell, M.; !1Priefer, U.B.; Puhler, A. !$#journal Nucleic Acids Res. (1987) 15:31-49 !$#title Organization and partial sequence of a DNA region of the !1Rhizobium leguminosarum symbiotic plasmid pRL6JI containing !1the genes fixABC, nifA, nifB and a novel open reading frame. !$#cross-references MUID:87146339; PMID:3029674 !$#accession B25878 !'##molecule_type DNA !'##residues 1-98 ##label GRO !'##cross-references GB:X05049; NID:g46199; PIDN:CAA28722.1; PID:g46201 REFERENCE JC1001 !$#authors Ni, F.D.; Hong, G.F. !$#journal Acta Biochim. Biophys. Sin. (1991) 23:458-462 !$#title DNA sequence study of the Fix X gene of Rhizobium !1leguminosarum 248. !$#accession JC1001 !'##molecule_type DNA !'##residues 1,'R',3-4,'I',6-22,'G',24-37,'N',39-52,'L',54-62,'P',64-75, !1'C',77-98 ##label NIF !'##note article in Chinese with English abstract !'##note the authors translated the codon AGG for residue 2 as Lys GENETICS !$#gene fixX !$#genome plasmid CLASSIFICATION #superfamily ferredoxin 2[4Fe-4S]; ferredoxin 2[4Fe-4S] !1homology KEYWORDS 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$29-84 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$46,66,69,72 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 98 #molecular-weight 10971 #checksum 1706 SEQUENCE /// ENTRY A27510 #type complete TITLE ferredoxin 2[4Fe-4S]-like protein - Rhizobium leguminosarum bv. trifolii ORGANISM #formal_name Rhizobium leguminosarum bv. trifolii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A27510 REFERENCE A27510 !$#authors Iismaa, S.E.; Watson, J.M. !$#journal Nucleic Acids Res. (1987) 15:3180 !$#title A gene upstream of the Rhizobium trifolii nifA gene encodes !1a ferredoxin-like protein. !$#cross-references MUID:87174837; PMID:3562251 !$#accession A27510 !'##molecule_type DNA !'##residues 1-98 ##label IIS !'##cross-references GB:X05257; NID:g46456; PIDN:CAA28879.1; PID:g46457 !'##experimental_source strain ANU843 GENETICS !$#gene FixX CLASSIFICATION #superfamily ferredoxin 2[4Fe-4S]; ferredoxin 2[4Fe-4S] !1homology KEYWORDS electron transfer FEATURE !$29-84 #domain ferredoxin 2[4Fe-4S] homology #label FER SUMMARY #length 98 #molecular-weight 11110 #checksum 2244 SEQUENCE /// ENTRY S04185 #type complete TITLE ferredoxin [4Fe-4S] fixX - Bradyrhizobium japonicum ALTERNATE_NAMES ferredoxin homolog ORGANISM #formal_name Bradyrhizobium japonicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S04185 REFERENCE S04182 !$#authors Gubler, M.; Zuercher, T.; Hennecke, H. !$#journal Mol. Microbiol. (1989) 3:141-148 !$#title The Bradyrhizobium japonicum fixBCX operon: identification !1of fixX and of a 5' mRNA region affecting the level of the !1fixBCX transcript. !$#cross-references MUID:89343618; PMID:2503674 !$#accession S04185 !'##molecule_type DNA !'##residues 1-98 ##label GUB !'##cross-references EMBL:X13144; NID:g39519; PIDN:CAA31540.1; !1PID:g39521 GENETICS !$#gene fixX CLASSIFICATION #superfamily ferredoxin 2[4Fe-4S]; ferredoxin 2[4Fe-4S] !1homology KEYWORDS 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$29-84 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$46,66,69,72 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 98 #molecular-weight 10958 #checksum 1068 SEQUENCE /// ENTRY FEPSTV #type complete TITLE ferredoxin [3Fe-4S][4Fe-4S] - Pseudomonas stutzeri ORGANISM #formal_name Pseudomonas stutzeri DATE 08-Mar-1989 #sequence_revision 27-Jan-1995 #text_change 18-Sep-1998 ACCESSIONS A30025 REFERENCE A30025 !$#authors Saeki, K.; Wakabayashi, S.; Zumft, W.G.; Matsubara, H. !$#journal J. Biochem. (1988) 104:242-246 !$#title Pseudomonas stutzeri ferredoxin: close similarity to !1Azotobacter vinelandii and Pseudomonas ovalis ferredoxins. !$#cross-references MUID:89034013; PMID:3053681 !$#accession A30025 !'##molecule_type protein !'##residues 1-106 ##label SAE COMMENT The identity of the iron-sulfur clusters is uncertain; !1[3Fe-4S][4Fe-4S] clusters have been assigned on the basis of !1similarity with Azotobacter vinelandii ferredoxin [3Fe-4S] !1[4Fe-4S] (see PIR:JS0191). CLASSIFICATION #superfamily ferredoxin 2[4Fe-4S]; ferredoxin 2[4Fe-4S] !1homology KEYWORDS 3Fe-4S; 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-57 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$8,16,49 #binding_site 3Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$20,39,42,45 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 106 #molecular-weight 12110 #checksum 2181 SEQUENCE /// ENTRY FEAV #type complete TITLE ferredoxin [3Fe-4S][4Fe-4S] [validated] - Azotobacter vinelandii ALTERNATE_NAMES ferredoxin I ORGANISM #formal_name Azotobacter vinelandii DATE 17-Dec-1982 #sequence_revision 31-Mar-1992 #text_change 20-Apr-2000 ACCESSIONS A29936; A00218 REFERENCE A29936 !$#authors Morgan, T.V.; Lundell, D.J.; Burgess, B.K. !$#journal J. Biol. Chem. (1988) 263:1370-1375 !$#title Azotobacter vinelandii ferredoxin I: cloning, sequencing, !1and mutant analysis. !$#cross-references MUID:88087274; PMID:2826477 !$#accession A29936 !'##molecule_type DNA !'##residues 1-107 ##label MOR !'##cross-references GB:J03521; NID:g142303; PIDN:AAA22125.1; !1PID:g142304 REFERENCE A00218 !$#authors Howard, J.B.; Lorsbach, T.W.; Ghosh, D.; Melis, K.; Stout, !1C.D. !$#journal J. Biol. Chem. (1983) 258:508-522 !$#title Structure of Azotobacter vinelandii 7Fe ferredoxin. Amino !1acid sequence and electron density maps of residues. !$#cross-references MUID:83082915; PMID:6848518 !$#contents sequence; X-ray crystallography, 2 angstroms !$#accession A00218 !'##molecule_type protein !'##residues 2-107 ##label HOW REFERENCE A51174 !$#authors Stout, C.D. !$#submission submitted to the Brookhaven Protein Data Bank, June 1993 !$#cross-references PDB:1FDA !$#contents annotation; X-ray crystallography, 2.1 angstroms, oxidized, !1pH 6, residues 2-107 REFERENCE A51175 !$#authors Stout, C.D. !$#submission submitted to the Brookhaven Protein Data Bank, June 1993 !$#cross-references PDB:1FDB !$#contents annotation; X-ray crystallography, 2.2 angstroms, reduced, !1pH 6, residues 2-107 REFERENCE A51536 !$#authors Stout, C.D. !$#submission submitted to the Brookhaven Protein Data Bank, June 1993 !$#cross-references PDB:5FD1 !$#contents annotation; X-ray crystallography, 1.9 angstroms, oxidized, !1pH 8, residues 2-107 REFERENCE A51176 !$#authors Stout, C.D. !$#submission submitted to the Brookhaven Protein Data Bank, June 1993 !$#cross-references PDB:1FDC !$#contents annotation; X-ray crystallography, 2.1 angstroms, reduced, !1pH 8, residues 2-107 REFERENCE A50837 !$#authors Merritt, E.A.; Stout, G.H.; Turley, S.; Sieker, L.C.; !1Jensen, L.H.; Orme-johnson, W.H. !$#submission submitted to the Brookhaven Protein Data Bank, September !11992 !$#cross-references PDB:1FER !$#contents annotation; X-ray crystallography, 2.3 angstroms, residues !12-107 REFERENCE JS0191 !$#authors Stout, G.H.; Turley, S.; Sieker, L.C.; Jensen, L.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:1020-1022 !$#title Structure of ferredoxin I from Azotobacter vinelandii. !$#cross-references MUID:88124966; PMID:3422475 !$#contents annotation; X-ray crystallography REFERENCE A58666 !$#authors Stout, C.D. !$#journal J. Mol. Biol. (1989) 205:545-555 !$#title Refinement of the 7 Fe ferredoxin from Azotobacter !1vinelandii at 1.9 Angstroms resolution. !$#cross-references MUID:89178673; PMID:2926817 !$#contents annotation; X-ray crystallography, 1.9 angstroms REFERENCE A58673 !$#authors Stout, C.D. !$#journal J. Biol. Chem. (1988) 263:9256-9260 !$#title 7-Iron ferredoxin revisited. !$#cross-references MUID:88243805; PMID:3379067 !$#contents annotation; X-ray crystallography, 2.7 angstroms GENETICS !$#gene fdxA CLASSIFICATION #superfamily ferredoxin 2[4Fe-4S]; ferredoxin 2[4Fe-4S] !1homology KEYWORDS 3Fe-4S; 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$2-107 #product ferredoxin [3Fe-4S][4Fe-4S] #status !8experimental #label MAT\ !$2-58 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$9,17,50 #binding_site 3Fe-4S cluster (Cys) (covalent) #status !8experimental\ !$21,40,43,46 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8experimental SUMMARY #length 107 #molecular-weight 12182 #checksum 6551 SEQUENCE /// ENTRY FEPSFV #type complete TITLE ferredoxin [3Fe-4S][4Fe-4S] - Pseudomonas putida ORGANISM #formal_name Pseudomonas putida DATE 31-May-1979 #sequence_revision 08-Oct-1981 #text_change 18-Sep-1998 ACCESSIONS A00217 REFERENCE A00217 !$#authors Hase, T.; Wakabayashi, S.; Matsubara, H.; Ohmori, D.; !1Suzuki, K. !$#journal FEBS Lett. (1978) 91:315-319 !$#title Pseudomonas ovalis ferredoxin: similarity to Azotobacter and !1Chromatium ferredoxins. !$#cross-references MUID:78239082; PMID:680138 !$#accession A00217 !'##molecule_type protein !'##residues 1-106 ##label HAS !'##note the source was designated as Pseudomonas ovalis COMMENT The identity of the iron-sulfur clusters is uncertain; !1[3Fe-4S][4Fe-4S] cluster have been assigned on the basis of !1similarity with Azotobacter vinelandii ferredoxin [3Fe-4S] !1[4Fe-4S] (see PIR:JS0191). CLASSIFICATION #superfamily ferredoxin 2[4Fe-4S]; ferredoxin 2[4Fe-4S] !1homology KEYWORDS 3Fe-4S; 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-57 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$8,16,49 #binding_site 3Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$20,39,42,45 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 106 #molecular-weight 11916 #checksum 724 SEQUENCE /// ENTRY FETWT #type complete TITLE ferredoxin [3Fe-4S][4Fe-4S] - Thermus aquaticus (tentative sequence) ORGANISM #formal_name Thermus aquaticus DATE 13-Aug-1986 #sequence_revision 13-Aug-1986 #text_change 03-Nov-2000 ACCESSIONS A00216 REFERENCE A90636 !$#authors Sato, S.; Nakazawa, K.; Hon-Nami, K.; Oshima, T. !$#journal Biochim. Biophys. Acta (1981) 668:277-289 !$#title Purification, some properties and amino acid sequence of !1Thermus thermophilus HB8 ferredoxin. !$#cross-references MUID:81184605; PMID:7225412 !$#accession A00216 !'##molecule_type protein !'##residues 1-69;97-105 ##label SAT !'##experimental_source strain HB8; ATCC 27634 REFERENCE A92402 !$#authors Hille, R.; Yoshida, T.; Tarr, G.E.; Williams Jr., C.H.; !1Ludwig, M.I.; Fee, J.A.; Kent, T.A.; Huynh, B.H.; Munck, E. !$#journal J. Biol. Chem. (1983) 258:13008-13013 !$#title Studies of the ferredoxin from Thermus thermophilus. !$#cross-references MUID:84032522; PMID:6313685 !$#contents annotation; composition !$#note we have positioned residues 70-96 by homology with other !1Azotobacter-type ferredoxins; strain ATCC 696 CLASSIFICATION #superfamily ferredoxin 2[4Fe-4S]; ferredoxin 2[4Fe-4S] !1homology KEYWORDS 3Fe-4S; 4Fe-4S; duplication; electron transfer; iron-sulfur !1protein; metalloprotein FEATURE !$1-57 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$8,16,49 #binding_site 3Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$20,39,42,45 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 105 #molecular-weight 11800 #checksum 421 SEQUENCE /// ENTRY FERF2C #type complete TITLE ferredoxin [3Fe-4S][4Fe-4S] - Rhodobacter capsulatus ALTERNATE_NAMES ferredoxin II ORGANISM #formal_name Rhodobacter capsulatus DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 11-Jun-1999 ACCESSIONS S10976; A34968; A39857; JX0134 REFERENCE S10976 !$#authors Duport, C.; Jouanneau, Y.; Vignais, P.M. !$#journal Nucleic Acids Res. (1990) 18:4618 !$#title Nucleotide sequence of fdxA encoding a 7Fe ferredoxin of !1Rhodobacter capsulatus. !$#cross-references MUID:90356425; PMID:2388848 !$#accession S10976 !'##molecule_type DNA !'##residues 1-112 ##label DUP !'##cross-references EMBL:X53300; NID:g46011; PIDN:CAA37388.1; !1PID:g46012 !$#accession A34968 !'##molecule_type protein !'##residues 2-31 ##label DUP2 REFERENCE A39857 !$#authors Saeki, K.; Suetsugu, Y.; Tokuda, K.; Miyatake, Y.; Young, !1D.A.; Marrs, B.L.; Matsubara, H. !$#journal J. Biol. Chem. (1991) 266:12889-12895 !$#title Genetic analysis of functional differences among distinct !1ferredoxins in Rhodobacter capsulatus. !$#cross-references MUID:91302301; PMID:2071578 !$#accession A39857 !'##molecule_type DNA !'##residues 1-112 ##label SAE !'##cross-references GB:M64555; NID:g151913; PIDN:AAA26108.1; !1PID:g151914 REFERENCE JX0133 !$#authors Saeki, K.; Suetsugu, Y.; Yao, Y.; Horio, T.; Marrs, B.L.; !1Matsubara, H. !$#journal J. Biochem. (1990) 108:475-482 !$#title Two distinct ferredoxins from Rhodobacter capsulatus: !1complete amino acid sequences and molecular evolution. !$#cross-references MUID:91115797; PMID:2277040 !$#accession JX0134 !'##molecule_type protein !'##residues 2-112 ##label SA2 GENETICS !$#gene fdxA CLASSIFICATION #superfamily ferredoxin 2[4Fe-4S]; ferredoxin 2[4Fe-4S] !1homology KEYWORDS 3Fe-4S; 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$2-112 #product ferredoxin [3Fe-4S][4Fe-4S] #status !8experimental #label MAT\ !$2-58 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$9,17,50 #binding_site 3Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$21,40,43,46 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 112 #molecular-weight 12679 #checksum 9560 SEQUENCE /// ENTRY FEBSA #type complete TITLE ferredoxin [3Fe-4S][4Fe-4S] - Alicyclobacillus acidocaldarius ORGANISM #formal_name Alicyclobacillus acidocaldarius DATE 13-Aug-1986 #sequence_revision 13-Aug-1986 #text_change 18-Sep-1998 ACCESSIONS A00215 REFERENCE A00215 !$#authors Schlatter, D.; Waldvogel, S.; Zulli, F.; Suter, F.; !1Portmann, W.; Zuber, H. !$#journal Biol. Chem. Hoppe-Seyler (1985) 366:223-231 !$#title Purification, amino-acid sequence and some properties of the !1ferredoxin isolated from Bacillus acidocaldarius. !$#cross-references MUID:85225952; PMID:2988582 !$#accession A00215 !'##molecule_type protein !'##residues 1-78 ##label SCH CLASSIFICATION #superfamily ferredoxin 2[4Fe-4S]; ferredoxin 2[4Fe-4S] !1homology KEYWORDS 3Fe-4S; 4Fe-4S; duplication; electron transfer; iron-sulfur !1protein; metalloprotein FEATURE !$1-57 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$8,16,49 #binding_site 3Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$20,39,42,45 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 78 #molecular-weight 8872 #checksum 96 SEQUENCE /// ENTRY FEDV2N #type complete TITLE ferredoxin 2[4Fe-4S] II - Desulfovibrio desulfuricans ORGANISM #formal_name Desulfovibrio desulfuricans DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 18-Sep-1998 ACCESSIONS A00213 REFERENCE A00213 !$#authors Guerlesquin, F.; Bruschi, M.; Bovier-Lapierre, G.; Bonicel, !1J.; Couchoud, P. !$#journal Biochimie (1983) 65:43-47 !$#title Primary structure of the two (4 Fe-4 S) clusters ferredoxin !1from Desulfovibrio desulfuricans (strain Norway 4). !$#cross-references MUID:83153918; PMID:6403056 !$#accession A00213 !'##molecule_type protein !'##residues 1-59 ##label GUE !'##experimental_source strain Norway 4 !'##note the active protein is a dimer of identical chains, each !1containing two 4Fe-4S clusters CLASSIFICATION #superfamily ferredoxin 2[4Fe-4S]; ferredoxin 2[4Fe-4S] !1homology KEYWORDS 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$2-59 #product ferredoxin 2[4Fe-4S] II #status experimental !8#label MAT\ !$5-59 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$12,15,18,52 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$22,42,45,48 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 59 #molecular-weight 6313 #checksum 3488 SEQUENCE /// ENTRY FEDV3A #type complete TITLE ferredoxin [3Fe-4S][4Fe-4S] III - Desulfovibrio africanus ORGANISM #formal_name Desulfovibrio africanus DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 18-Sep-1998 ACCESSIONS S07149 REFERENCE S07149 !$#authors Bovier-Lapierre, G.; Bruschi, M.; Bonicel, J.; Hatchikian, !1E.C. !$#journal Biochim. Biophys. Acta (1987) 913:20-26 !$#title Amino-acid sequence of Desulfovibrio africanus ferredoxin !1III: a unique structural feature for accommodating !1iron-sulfur clusters. !$#accession S07149 !'##molecule_type protein !'##residues 1-61 ##label BOV CLASSIFICATION #superfamily ferredoxin 2[4Fe-4S]; ferredoxin 2[4Fe-4S] !1homology KEYWORDS 3Fe-4S; 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$4-59 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$11,17,51 #binding_site 3Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$21,41,44,47 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 61 #molecular-weight 6577 #checksum 3381 SEQUENCE /// ENTRY A30024 #type complete TITLE ferredoxin [3Fe-4S][4Fe-4S] I - Desulfovibrio vulgaris ORGANISM #formal_name Desulfovibrio vulgaris DATE 08-Mar-1989 #sequence_revision 02-May-1994 #text_change 18-Sep-1998 ACCESSIONS A30024; A41412 REFERENCE A30024 !$#authors Okawara, N.; Ogata, M.; Yagi, T.; Wakabayashi, S.; !1Matsubara, H. !$#journal J. Biochem. (1988) 104:196-199 !$#title Amino acid sequence of ferredoxin I from Desulfovibrio !1vulgaris Miyazaki. !$#cross-references MUID:89034004; PMID:3182762 !$#accession A30024 !'##molecule_type protein !'##residues 1-61 ##label OKA !'##experimental_source strain Miyazaki REFERENCE A41412 !$#authors Ogata, M.; Kondo, S.; Okawara, N.; Yagi, T. !$#journal J. Biochem. (1988) 103:121-125 !$#title Purification and characterization of ferredoxin from !1Desulfovibrio vulgaris Miyazaki. !$#cross-references MUID:88198088; PMID:3360752 !$#accession A41412 !'##molecule_type protein !'##residues 1-15 ##label OGA COMMENT Ferredoxin I mediates electron transfer between pyruvate !1dehydrogenase and the hydrogenase-cytochrome c3 system. COMMENT Ferredoxin I has two distinguishable iron-sulfur clusters. CLASSIFICATION #superfamily ferredoxin 2[4Fe-4S]; ferredoxin 2[4Fe-4S] !1homology KEYWORDS 3Fe-4S; 4Fe-4S; electron transfer; homodimer; iron-sulfur !1protein; metalloprotein FEATURE !$4-59 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$11,17,51 #binding_site 3Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$21,41,44,47 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 61 #molecular-weight 6471 #checksum 2874 SEQUENCE /// ENTRY FEMYFS #type complete TITLE ferredoxin [3Fe-4S][4Fe-4S] - Mycobacterium smegmatis ORGANISM #formal_name Mycobacterium smegmatis DATE 30-Nov-1979 #sequence_revision 30-Nov-1979 #text_change 18-Sep-1998 ACCESSIONS A00219 REFERENCE A00219 !$#authors Hase, T.; Wakabayashi, S.; Matsubara, H.; Imai, T.; !1Matsumoto, T.; Tobari, J. !$#journal FEBS Lett. (1979) 103:224-228 !$#title Mycobacterium smegmatis ferredoxin: a unique distribution of !1cysteine residues constructing iron--sulfur clusters. !$#cross-references MUID:79236790; PMID:467663 !$#accession A00219 !'##molecule_type protein !'##residues 1-106 ##label HAS CLASSIFICATION #superfamily ferredoxin 2[4Fe-4S]; ferredoxin 2[4Fe-4S] !1homology KEYWORDS 3Fe-4S; 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-57 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$8,16,49 #binding_site 3Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$20,39,42,45 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 106 #molecular-weight 11510 #checksum 4304 SEQUENCE /// ENTRY FEDVFG #type complete TITLE ferredoxin [4Fe-4S] I [validated] - Desulfovibrio gigas ALTERNATE_NAMES ferredoxin [3Fe-4S] II ORGANISM #formal_name Desulfovibrio gigas DATE 28-Feb-1980 #sequence_revision 19-Oct-1995 #text_change 15-Sep-2000 ACCESSIONS S48666; A90216; A00211; S17118 REFERENCE S48666 !$#authors Chen, B.; Menon, N.K.; Dervertarnian, L.; Moura, J.J.G.; !1Przybyla, A.E. !$#journal FEBS Lett. (1994) 351:401-404 !$#title Cloning, sequencing and overexpression of the Desulfovibrio !1gigas ferredoxin gene in E. coli. !$#cross-references MUID:94364513; PMID:8082803 !$#accession S48666 !'##molecule_type DNA !'##residues 1-59 ##label CHE !'##note tetrameric ferredoxin [3Fe-4S] II interconverts with dimeric !1ferredoxin [4Fe-4S] I REFERENCE A90216 !$#authors Bruschi, M. !$#journal Biochem. Biophys. Res. Commun. (1979) 91:623-628 !$#title Amino acid sequence of Desulfovibrio gigas ferredoxin: !1revisions. !$#cross-references MUID:80087755; PMID:518659 !$#accession A90216 !'##molecule_type protein !'##residues 2-56,58-59 ##label BRU REFERENCE A50839 !$#authors Kissinger, C.R.; Sieker, L.C.; Adman, E.T.; Jensen, L.H. !$#submission submitted to the Brookhaven Protein Data Bank, April 1991 !$#cross-references PDB:1FXD !$#contents annotation; X-ray crystallography, 1.7 angstroms, residues !12-56,'V',58-59 REFERENCE S17118 !$#authors Kissinger, C.R.; Sieker, L.C.; Adman, E.T.; Jensen, L.H. !$#journal J. Mol. Biol. (1991) 219:693-715 !$#title Refined crystal structure of ferredoxin II from !1Desulfovibrio gigas at 1.7 A. !$#cross-references MUID:91278096; PMID:2056535 !$#contents annotation; X-ray crystallography, 1.7 angstroms !$#note evidence for residue 57, modeled as Val REFERENCE A90174 !$#authors Travis, J.; Newman, D.J.; Legall, J.; Peck Jr., H.D. !$#journal Biochem. Biophys. Res. Commun. (1971) 45:452-458 !$#title The amino acid sequence of ferredoxin from the sulfate !1reducing bacterium, Desulfovibrio gigas. !$#cross-references MUID:72117540; PMID:4946273 !$#contents annotation !$#note this sequence differs from that shown at a number of !1positions COMPLEX homotetramer ferredoxin [3Fe-4S] II; homodimer ferredoxin !1[4Fe-4S] I CLASSIFICATION #superfamily ferredoxin 2[4Fe-4S]; ferredoxin 2[4Fe-4S] !1homology KEYWORDS 3Fe-4S; 4Fe-4S; electron transfer; homodimer; homotetramer; !1iron-sulfur protein; metalloprotein FEATURE !$2-59 #product ferredoxin [4Fe-4S] I #status experimental !8#label MAT\ !$2-59 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$9,15,51 #binding_site 3Fe-4S cluster (Cys) (covalent) #status !8experimental\ !$9,12,15,51 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$12 #modified_site cysteine derivative (Cys) (probably !8cysteine methyl disulfide) #status experimental\ !$19-43 #disulfide_bonds #status experimental SUMMARY #length 59 #molecular-weight 6407 #checksum 331 SEQUENCE /// ENTRY FEDV2V #type complete TITLE ferredoxin [4Fe-4S] II - Desulfovibrio vulgaris ORGANISM #formal_name Desulfovibrio vulgaris DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 18-Sep-1998 ACCESSIONS S07154 REFERENCE S07154 !$#authors Okawara, N.; Ogata, M.; Yagi, T.; Wakabayashi, S.; !1Matsubara, H. !$#journal Biochimie (1988) 70:1815-1820 !$#title Characterization and complete amino acid sequence of !1ferredoxin II from Desulfovibrio vulgaris Miyazaki. !$#cross-references MUID:89274328; PMID:2855025 !$#accession S07154 !'##molecule_type protein !'##residues 1-63 ##label OKA CLASSIFICATION #superfamily ferredoxin 2[4Fe-4S]; ferredoxin 2[4Fe-4S] !1homology KEYWORDS 4Fe-4S; electron transfer; homodimer; iron-sulfur protein; !1metalloprotein FEATURE !$4-61 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$11,14,17,53 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 63 #molecular-weight 7091 #checksum 4546 SEQUENCE /// ENTRY FEDV1A #type complete TITLE ferredoxin [4Fe-4S] I [validated] - Desulfovibrio africanus ORGANISM #formal_name Desulfovibrio africanus DATE 15-Oct-1982 #sequence_revision 12-May-1995 #text_change 15-Sep-2000 ACCESSIONS A56050; A00212; S50183 REFERENCE A56050 !$#authors Sery, A.; Housset, D.; Serre, L.; Bonicel, J.; Hatchikian, !1C.; Frey, M.; Roth, M. !$#journal Biochemistry (1994) 33:15408-15417 !$#title Crystal structure of the ferredoxin I from Desulfovibrio !1africanus at 2.3 angstrom resolution. !$#cross-references MUID:95101634; PMID:7803404 !$#accession A56050 !'##molecule_type protein !'##residues 1-64 ##label SER !'##note X-ray crystallography, 2.3 angstroms; correction confirmed by !1protein sequencing REFERENCE A00212 !$#authors Bruschi, M.; Hatchikian, E.C. !$#journal Biochimie (1982) 64:503-507 !$#title Non-heme iron proteins of Desulfovibrio: the primary !1structure of ferredoxin I from Desulfovibrio africanus. !$#cross-references MUID:83023363; PMID:7126685 !$#accession A00212 !'##molecule_type protein !'##residues 1-57,'S',59,'EE' ##label BRU !'##experimental_source strain Benghazi, NCIB 8401 REFERENCE S50183 !$#authors Davy, S.L.; Breton, J.; Osborne, M.J.; Thomson, A.J.; !1Thurgood, A.P.; Lian, L.Y.; Petillot, Y.; Hatchikian, C.; !1Moore, G.R. !$#journal Biochim. Biophys. Acta (1994) 1209:33-39 !$#title MCD and (1)H-NMR spectroscopic studies of Desulfovibrio !1africanus ferredoxin I: revised amino-acid sequence and !1identification of secondary structure. !$#cross-references MUID:95035051; PMID:7947979 !$#accession S50183 !'##molecule_type protein !'##residues 1-64 ##label DAV !'##note conformation by (1)H-NMR REFERENCE A52981 !$#authors Frey, M.; Roth, M. !$#submission submitted to the Brookhaven Protein Data Bank, November 1994 !$#cross-references PDB:1FXR !$#contents annotation; X-ray crystallography, 2.3 angstroms, residues !11-64 CLASSIFICATION #superfamily ferredoxin 2[4Fe-4S]; ferredoxin 2[4Fe-4S] !1homology KEYWORDS 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-64 #product ferredoxin [4Fe-4S] I #status experimental !8#label MAT\ !$4-62 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$11,14,17,54 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8experimental SUMMARY #length 64 #molecular-weight 7202 #checksum 4726 SEQUENCE /// ENTRY FEDV1V #type complete TITLE ferredoxin [4Fe-4S] I - Desulfovibrio desulfuricans ORGANISM #formal_name Desulfovibrio desulfuricans DATE 25-Oct-1987 #sequence_revision 27-Jan-1995 #text_change 18-Sep-1998 ACCESSIONS A25273 REFERENCE A25273 !$#authors Bruschi, M.H.; Guerlesquin, F.A.; Bovier-Lapierre, G.E.; !1Bonicel, J.J.; Couchoud, P.M. !$#journal J. Biol. Chem. (1985) 260:8292-8296 !$#title Amino acid sequence of the [4Fe-4S] ferredoxin isolated from !1Desulfovibrio desulfuricans Norway. !$#cross-references MUID:85234535; PMID:4008492 !$#accession A25273 !'##molecule_type protein !'##residues 1-59 ##label BRU !'##experimental_source strain Norway CLASSIFICATION #superfamily ferredoxin 2[4Fe-4S]; ferredoxin 2[4Fe-4S] !1homology KEYWORDS 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$2-59 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$9,12,15,51 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 59 #molecular-weight 6261 #checksum 565 SEQUENCE /// ENTRY B44203 #type complete TITLE ferredoxin [3Fe-4S] - Thermococcus litoralis ORGANISM #formal_name Thermococcus litoralis DATE 19-Feb-1999 #sequence_revision 19-Feb-1999 #text_change 19-Feb-1999 ACCESSIONS B44203 REFERENCE A44203 !$#authors Howard, J.B.; Park, J.B.; Zhai, Z.H.; Adams, M.W.W. !$#citation unpublished results, cited by Busse, S.C., La Mar, G.N., Yu, !1L.P., Howard, J.B., Smith, E.T., Zhou, Z.H., Adams, M.W.W., !1Biochemistry 31, 11952-11962, 1992 !$#accession B44203 !'##molecule_type protein !'##residues 1-59 ##label HOW REFERENCE A58591 !$#authors Wang, P.L.; Donaire, A.; Zhou, Z.H.; Adams, M.W.W.; La Mar, !1G.N. !$#journal Biochemistry (1996) 35:11319-11328 !$#title Molecular model of the solution structure for the !1paramagnetic four-iron ferredoxin from the hyperthermophilic !1archaeon Thermococcus litoralis. !$#cross-references MUID:96378623; PMID:8784186 !$#contents annotation; conformation by (1)H-NMR COMMENT This ferredoxin can form a 4Fe-4S cluster but it readily !1converts to a stable 3Fe-4S cluster. CLASSIFICATION #superfamily ferredoxin 2[4Fe-4S]; ferredoxin 2[4Fe-4S] !1homology KEYWORDS 3Fe-4S; 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-59 #product ferredoxin [3Fe-4S] #status experimental !8#label FE3\ !$1-59 #product ferredoxin [4Fe-4S] #status experimental !8#label FE4\ !$3-59 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$10,16,51 #binding_site 3Fe-4S cluster (Cys) (covalent) #link !8FE3 #status experimental\ !$10,13,16,51 #binding_site 4Fe-4S cluster (Cys) (covalent) #link !8FE4 #status experimental\ !$20-43 #disulfide_bonds #status experimental SUMMARY #length 59 #molecular-weight 6055 #checksum 7 SEQUENCE /// ENTRY FECLC #type complete TITLE ferredoxin [4Fe-4S] - Clostridium thermaceticum ORGANISM #formal_name Clostridium thermaceticum DATE 15-Oct-1982 #sequence_revision 15-Oct-1982 #text_change 18-Sep-1998 ACCESSIONS A00205 REFERENCE A00205 !$#authors Elliott, J.I.; Yang, S.S.; Ljungdahl, L.G.; Travis, J.; !1Reilly, C.F. !$#journal Biochemistry (1982) 21:3294-3298 !$#title Complete amino acid sequence of the 4Fe-4S, thermostable !1ferredoxin from Clostridium thermoaceticum. !$#cross-references MUID:83000247; PMID:7115670 !$#accession A00205 !'##molecule_type protein !'##residues 1-63 ##label ELL CLASSIFICATION #superfamily ferredoxin 2[4Fe-4S]; ferredoxin 2[4Fe-4S] !1homology KEYWORDS 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$3-63 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$10,13,16,55 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 63 #molecular-weight 6831 #checksum 5159 SEQUENCE /// ENTRY FEBSFF #type complete TITLE ferredoxin [4Fe-4S] - Bacillus stearothermophilus ORGANISM #formal_name Bacillus stearothermophilus DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 18-Sep-1998 ACCESSIONS A00214 REFERENCE A00214 !$#authors Hase, T.; Ohmiya, N.; Matsubara, H.; Mullinger, R.N.; Rao, !1K.K.; Hall, D.O. !$#journal Biochem. J. (1976) 159:55-63 !$#title Amino acid sequence of four-iron-four-sulphur ferredoxin !1isolated from Bacillus stearothermophilus. !$#cross-references MUID:77065140; PMID:999643 !$#accession A00214 !'##molecule_type protein !'##residues 1-81 ##label HAS CLASSIFICATION #superfamily ferredoxin 2[4Fe-4S]; ferredoxin 2[4Fe-4S] !1homology KEYWORDS 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$1-81 #product ferredoxin [4Fe-4S] #status experimental !8#label MAT\ !$4-69 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$11,14,17,61 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 81 #molecular-weight 8770 #checksum 3752 SEQUENCE /// ENTRY A55790 #type complete TITLE ferredoxin [4Fe-4S] [validated] - Bacillus "thermoproteolyticus" ORGANISM #formal_name Bacillus "thermoproteolyticus" DATE 23-Mar-1995 #sequence_revision 23-Mar-1995 #text_change 15-Sep-2000 ACCESSIONS A55790 REFERENCE A55790 !$#authors Fukuyama, K.; Nagahara, Y.; Tsukihara, T.; Katsube, Y.; !1Hase, T.; Matsubara, H. !$#journal J. Mol. Biol. (1988) 199:183-193 !$#title Tertiary structure of Bacillus thermoproteolyticus [4Fe-4S] !1ferredoxin. Evolutionary implications for bacterial !1ferredoxins. !$#cross-references MUID:88172459; PMID:3351918 !$#contents sequence; X-ray crystallography, 2.3 angstroms !$#accession A55790 !'##molecule_type protein !'##residues 1-81 ##label FUK REFERENCE A50884 !$#authors Fukuyama, K.; Tsukihara, T.; Katsube, Y. !$#submission submitted to the Brookhaven Protein Data Bank, February 1990 !$#cross-references PDB:2FXB !$#contents annotation; X-ray crystallography, 2.3 angstroms, residues !11-81 REFERENCE A44690 !$#authors Fukuyama, K.; Matsubara, H.; Tsukihara, T.; Katsube, Y. !$#journal J. Mol. Biol. (1989) 210:383-398 !$#title Structure of [4Fe-4S] ferredoxin from Bacillus !1thermoproteolyticus refined at 2.3 angstrom resolution. !1Structural comparisons of bacterial ferredoxins. !$#cross-references MUID:90096160; PMID:2600971 !$#contents annotation; X-ray crystallography, 2.3 angstroms CLASSIFICATION #superfamily ferredoxin 2[4Fe-4S]; ferredoxin 2[4Fe-4S] !1homology KEYWORDS 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$4-69 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$11,14,17,61 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8experimental SUMMARY #length 81 #molecular-weight 8770 #checksum 3769 SEQUENCE /// ENTRY FELVA #type complete TITLE photosystem I iron-sulfur protein psaC - liverwort (Marchantia polymorpha) chloroplast ALTERNATE_NAMES photosystem I iron-sulfur protein frxA ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 11-Jun-1999 ACCESSIONS S01527; A00224 REFERENCE S01512 !$#authors Kohchi, T.; Shirai, H.; Fukuzawa, H.; Sano, T.; Komano, T.; !1Umesono, K.; Inokuchi, H.; Ozeki, H.; Ohyama, K. !$#journal J. Mol. Biol. (1988) 203:353-372 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. IV. Inverted repeat and small single !1copy regions. !$#cross-references MUID:89068688; PMID:3199437 !$#accession S01527 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-81 ##label KOH !'##cross-references GB:X04465; GB:Y00686; NID:g11640; PIDN:CAA28135.1; !1PID:g11724 REFERENCE A00150 !$#authors Ohyama, K. !$#submission submitted to the EMBL Data Library, October 1986 !$#accession A00224 !'##molecule_type DNA !'##residues 1-81 ##label OHY REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features GENETICS !$#gene frxA !$#genome chloroplast CLASSIFICATION #superfamily ferredoxin 2[4Fe-4S]; ferredoxin 2[4Fe-4S] !1homology KEYWORDS 4Fe-4S; chloroplast; electron transfer; iron-sulfur protein; !1membrane-associated complex; metalloprotein; photosynthesis; !1photosystem I; thylakoid FEATURE !$2-81 #product photosystem I iron-sulfur protein psaC !8#status predicted #label MAT\ !$4-66 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$11,14,17,58 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$21,48,51,54 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 81 #molecular-weight 8941 #checksum 7723 SEQUENCE /// ENTRY FERZA #type complete TITLE photosystem I iron-sulfur protein psaC - rice chloroplast ALTERNATE_NAMES photosystem I protein C ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 11-Jun-1999 ACCESSIONS JQ0290; S05169 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0290 !'##molecule_type DNA !'##residues 1-81 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05169 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-81 ##label HIR !'##cross-references EMBL:X15901; NID:g11957; PIDN:CAA33954.1; !1PID:g12051 !'##experimental_source cv. Nihonbare GENETICS !$#gene psaC !$#map_position CP108265-108020 !$#genome chloroplast CLASSIFICATION #superfamily ferredoxin 2[4Fe-4S]; ferredoxin 2[4Fe-4S] !1homology KEYWORDS 4Fe-4S; chloroplast; electron transfer; iron-sulfur protein; !1membrane-associated complex; metalloprotein; photosynthesis; !1photosystem I; thylakoid FEATURE !$2-81 #product photosystem I iron-sulfur protein psaC !8#status predicted #label MAT\ !$4-66 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$11,14,17,58 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$21,48,51,54 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 81 #molecular-weight 8899 #checksum 6653 SEQUENCE /// ENTRY FEWT1 #type complete TITLE photosystem I iron-sulfur protein psaC - wheat chloroplast ALTERNATE_NAMES photosystem I 8K protein ORGANISM #formal_name chloroplast Triticum aestivum #common_name common wheat DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 11-Jun-1999 ACCESSIONS S04034; JU0006 REFERENCE S04033 !$#authors Dunn, P.P.J.; Gray, J.C. !$#journal Plant Mol. Biol. (1988) 11:311-319 !$#title Localization and nucleotide sequence of the gene for the 8 !1kDa subunit of photosystem I in pea and wheat chloroplast !1DNA. !$#accession S04034 !'##molecule_type DNA !'##residues 1-81 ##label DUN !'##cross-references EMBL:X13158; NID:g12349; PIDN:CAA31555.1; !1PID:g12350 GENETICS !$#gene psaC !$#genome chloroplast CLASSIFICATION #superfamily ferredoxin 2[4Fe-4S]; ferredoxin 2[4Fe-4S] !1homology KEYWORDS 4Fe-4S; chloroplast; electron transfer; iron-sulfur protein; !1membrane-associated complex; metalloprotein; photosynthesis; !1photosystem I; thylakoid FEATURE !$2-81 #product photosystem I iron-sulfur protein psaC !8#status predicted #label MAT\ !$4-66 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$11,14,17,58 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$21,48,51,54 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 81 #molecular-weight 8899 #checksum 6653 SEQUENCE /// ENTRY FEZM1C #type complete TITLE photosystem I iron-sulfur protein psaC - maize chloroplast ORGANISM #formal_name chloroplast Zea mays #common_name maize DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 11-Jun-1999 ACCESSIONS JU0008 REFERENCE JU0008 !$#authors Schantz, R.; Bogorad, L. !$#journal Plant Mol. Biol. (1988) 11:239-247 !$#title Maize chloroplast genes ndhD, ndhE, and psaC. Sequences, !1transcripts and transcript pools. !$#accession JU0008 !'##molecule_type DNA !'##residues 1-81 ##label SCH !'##cross-references GB:X13159; NID:g12421; PIDN:CAA31557.1; PID:g12423 GENETICS !$#gene psaC !$#genome chloroplast CLASSIFICATION #superfamily ferredoxin 2[4Fe-4S]; ferredoxin 2[4Fe-4S] !1homology KEYWORDS 4Fe-4S; chloroplast; electron transfer; iron-sulfur protein; !1membrane-associated complex; metalloprotein; photosynthesis; !1photosystem I; thylakoid FEATURE !$2-81 #product photosystem I iron-sulfur protein psaC !8#status predicted #label MAT\ !$4-66 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$11,14,17,58 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$21,48,51,54 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 81 #molecular-weight 8908 #checksum 6509 SEQUENCE /// ENTRY FEPM1S #type complete TITLE photosystem I iron-sulfur protein psaC - garden pea chloroplast ALTERNATE_NAMES photosystem I 8K protein ORGANISM #formal_name chloroplast Pisum sativum #common_name garden pea DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 11-Jun-1999 ACCESSIONS S04033; S00319; JU0007 REFERENCE S04033 !$#authors Dunn, P.P.J.; Gray, J.C. !$#journal Plant Mol. Biol. (1988) 11:311-319 !$#title Localization and nucleotide sequence of the gene for the 8 !1kDa subunit of photosystem I in pea and wheat chloroplast !1DNA. !$#accession S04033 !'##molecule_type DNA !'##residues 1-81 ##label DUN1 !'##cross-references EMBL:X13157; NID:g12169; PIDN:CAA31554.1; !1PID:g12170 REFERENCE S00314 !$#authors Dunn, P.P.J.; Packman, L.C.; Pappin, D.; Gray, J.C. !$#journal FEBS Lett. (1988) 228:157-161 !$#title N-terminal amino acid sequence analysis of the subunits of !1pea photosystem I. !$#cross-references MUID:88137587; PMID:3277857 !$#accession S00319 !'##molecule_type protein !'##residues 2-44,'X',46-47,'X',49,'XX',52 ##label DUN2 GENETICS !$#gene psaC !$#genome chloroplast CLASSIFICATION #superfamily ferredoxin 2[4Fe-4S]; ferredoxin 2[4Fe-4S] !1homology KEYWORDS 4Fe-4S; chloroplast; electron transfer; iron-sulfur protein; !1membrane-associated complex; metalloprotein; photosynthesis; !1photosystem I; thylakoid FEATURE !$2-81 #product photosystem I iron-sulfur protein psaC !8#status experimental #label MAT\ !$4-66 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$11,14,17,58 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$21,48,51,54 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 81 #molecular-weight 8980 #checksum 6557 SEQUENCE /// ENTRY FEAI1C #type complete TITLE photosystem I iron-sulfur protein psaC - Anabaena sp. (strain PCC 7120) ALTERNATE_NAMES photosystem I 9K protein; photosystem I apoprotein FA/FB ORGANISM #formal_name Anabaena sp. DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 11-Jun-1999 ACCESSIONS S20851; S18052 REFERENCE S20851 !$#authors Mulligan, M.E.; Jackman, D.M. !$#journal Plant Mol. Biol. (1992) 18:803-808 !$#title Nucleotide sequence and expression of the gene for the 9 kDa !1F(A)/F(B) component of photosystem I from the cyanobacterium !1Anabaena sp. PCC7120. !$#cross-references MUID:92216058; PMID:1558954 !$#accession S20851 !'##molecule_type DNA !'##residues 1-81 ##label MUL !'##cross-references EMBL:X61369; NID:g39046; PIDN:CAA43645.1; !1PID:g39047 GENETICS !$#gene psaC CLASSIFICATION #superfamily ferredoxin 2[4Fe-4S]; ferredoxin 2[4Fe-4S] !1homology KEYWORDS 4Fe-4S; duplication; electron transfer; iron-sulfur protein; !1membrane-associated complex; metalloprotein; photosynthesis; !1photosystem I; thylakoid FEATURE !$4-66 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$11,14,17,58 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$21,48,51,54 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 81 #molecular-weight 8816 #checksum 7381 SEQUENCE /// ENTRY FEAICV #type complete TITLE photosystem I iron-sulfur protein psaC - Anabaena variabilis ALTERNATE_NAMES photosystem I apoprotein FA/FB ORGANISM #formal_name Anabaena variabilis DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 11-Jun-1999 ACCESSIONS S14475 REFERENCE S14475 !$#authors Mannan, M.R.; Pakrasi, H.B. !$#submission submitted to the EMBL Data Library, January 1991 !$#accession S14475 !'##molecule_type DNA !'##residues 1-81 ##label MAN !'##cross-references EMBL:X57153; NID:g39044; PIDN:CAA40443.1; !1PID:g39045 GENETICS !$#gene psaC CLASSIFICATION #superfamily ferredoxin 2[4Fe-4S]; ferredoxin 2[4Fe-4S] !1homology KEYWORDS 4Fe-4S; duplication; electron transfer; iron-sulfur protein; !1membrane-associated complex; metalloprotein; photosynthesis; !1photosystem I; thylakoid FEATURE !$4-66 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$11,14,17,58 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$21,48,51,54 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 81 #molecular-weight 8816 #checksum 7381 SEQUENCE /// ENTRY B64019 #type complete TITLE hypothetical protein HI1043 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 18-Aug-1995 #sequence_revision 18-Aug-1995 #text_change 30-Sep-2002 ACCESSIONS B64019 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession B64019 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-166 ##label TIGR !'##cross-references GB:U32785; GB:L42023; NID:g3212212; !1PIDN:AAC22702.1; PID:g1574077; TIGR:HI1043 CLASSIFICATION #superfamily ferredoxin protein NapF; ferredoxin 2[4Fe-4S] !1homology FEATURE !$46-102 #domain ferredoxin 2[4Fe-4S] homology #label FER3\ !$116-166 #domain ferredoxin 2[4Fe-4S] homology #label FER SUMMARY #length 166 #molecular-weight 18144 #checksum 1428 SEQUENCE /// ENTRY A91016 #type complete TITLE ferredoxin-type protein [imported] - Escherichia coli (strain O157:H7, substrain RIMD 0509952) ORGANISM #formal_name Escherichia coli DATE 18-Jul-2001 #sequence_revision 18-Jul-2001 #text_change 30-Sep-2002 ACCESSIONS A91016 REFERENCE A99629 !$#authors Hayashi, T.; Makino, K.; Ohnishi, M.; Kurokawa, K.; Ishii, !1K.; Yokoyama, K.; Han, C.G.; Ohtsubo, E.; Nakayama, K.; !1Murata, T.; Tanaka, M.; Tobe, T.; Iida, T.; Takami, H.; !1Honda, T.; Sasakawa, C.; Ogasawara, N.; Yasunaga, T.; !1Kuhara, S.; Shiba, T.; Hattori, M.; Shinagawa, H. !$#journal DNA Res. (2001) 8:11-22 !$#title Complete genome sequence of enterohemorrhagic Escherichia !1coli O157:H7 and genomic comparison with a laboratory strain !1K-12. !$#cross-references MUID:21156231; PMID:11258796 !$#accession A91016 !'##status preliminary !'##molecule_type DNA !'##residues 1-164 ##label HAY !'##cross-references GB:BA000007; PIDN:BAB36520.1; PID:g13362566; !1GSPDB:GN00154 !'##experimental_source strain O157:H7, substrain RIMD 0509952 GENETICS !$#gene ECs3097 CLASSIFICATION #superfamily ferredoxin protein NapF; ferredoxin 2[4Fe-4S] !1homology SUMMARY #length 164 #molecular-weight 18047 #checksum 2514 SEQUENCE /// ENTRY C85860 #type complete TITLE ferredoxin-type protein, electron transfer [imported] - Escherichia coli (strain O157:H7, substrain EDL933) ORGANISM #formal_name Escherichia coli DATE 16-Feb-2001 #sequence_revision 16-Feb-2001 #text_change 30-Sep-2002 ACCESSIONS C85860 REFERENCE A85480 !$#authors Perna, N.T.; Plunkett III, G.; Burland, V.; Mau, B.; !1Glasner, J.D.; Rose, D.J.; Mayhew, G.F.; Evans, P.S.; !1Gregor, J.; Kirkpatrick, H.A.; Posfai, G.; Hackett, J.; !1Klink, S.; Boutin, A.; Shao, Y.; Miller, L.; Grotbeck, E.J.; !1Davis, N.W.; Lim, A.; Dimalanta, E.; Potamousis, K.; !1Apodaca, J.; Anantharaman, T.S.; Lin, J.; Yen, G.; Schwartz, !1D.C.; Welch, R.A.; Blattner, F.R. !$#journal Nature (2001) 409:529-533 !$#title Genome sequence of enterohemorrhagic Escherichia coli !1O157:H7. !$#cross-references MUID:21074935; PMID:11206551 !$#accession C85860 !'##status preliminary !'##molecule_type DNA !'##residues 1-164 ##label STO !'##cross-references GB:AE005174; NID:g12516540; PIDN:AAG57343.1; !1GSPDB:GN00145; UWGP:Z3465 !'##experimental_source strain O157:H7, substrain EDL933 GENETICS !$#gene napF CLASSIFICATION #superfamily ferredoxin protein NapF; ferredoxin 2[4Fe-4S] !1homology SUMMARY #length 164 #molecular-weight 18047 #checksum 2514 SEQUENCE /// ENTRY F64990 #type complete TITLE ferredoxin-type protein NapF - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 12-Sep-1997 #sequence_revision 17-Sep-1997 #text_change 30-Sep-2002 ACCESSIONS F64990 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64990 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-164 ##label BLAT !'##cross-references GB:AE000309; GB:U00096; NID:g1788520; !1PIDN:AAC75268.1; PID:g1788536; UWGP:b2208 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene napF CLASSIFICATION #superfamily ferredoxin protein NapF; ferredoxin 2[4Fe-4S] !1homology SUMMARY #length 164 #molecular-weight 18047 #checksum 2514 SEQUENCE /// ENTRY AG0369 #type complete TITLE ferredoxin-type protein NapF [imported] - Yersinia pestis (strain CO92) ORGANISM #formal_name Yersinia pestis DATE 02-Nov-2001 #sequence_revision 02-Nov-2001 #text_change 30-Sep-2002 ACCESSIONS AG0369 REFERENCE AB0001 !$#authors Parkhill, J.; Wren, B.W.; Thomson, N.R.; Titball, R.W.; !1Holden, M.T.G.; Prentice, M.B.; Sebaihia, M.; James, K.D.; !1Churcher, C.; Mungall, K.L.; Baker, S.; Basham, D.; Bentley, !1S.D.; Brooks, K.; Cerdeno-Tarraga, A.M.; Chillingworth, T.; !1Cronin, A.; Davies, R.M.; Davis, P.; Dougan, G.; Feltwell, !1T.; Hamlin, N.; Holroyd, S.; Jagels, K.; Leather, S.; !1Karlyshev, A.V.; Moule, S.; Oyston, P.C.F.; Quail, M.; !1Rutherford, K.; Simmonds, M.; Skelton, J.; Stevens, K.; !1Whitehead, S.; Barrell, B.G. !$#journal Nature (2001) 413:523-527 !$#title Genome sequence of Yersinia pestis, the causative agent of !1plague. !$#cross-references MUID:21470413; PMID:11586360 !$#accession AG0369 !'##status preliminary !'##molecule_type DNA !'##residues 1-167 ##label KUR !'##cross-references GB:AL590842; PIDN:CAC92282.1; PID:g15980993; !1GSPDB:GN00175 GENETICS !$#gene napF CLASSIFICATION #superfamily ferredoxin protein NapF; ferredoxin 2[4Fe-4S] !1homology SUMMARY #length 167 #molecular-weight 18075 #checksum 7783 SEQUENCE /// ENTRY H83499 #type complete TITLE ferredoxin protein NapF PA1176 [imported] - Pseudomonas aeruginosa (strain PAO1) ORGANISM #formal_name Pseudomonas aeruginosa DATE 15-Sep-2000 #sequence_revision 15-Sep-2000 #text_change 30-Sep-2002 ACCESSIONS H83499 REFERENCE A82950 !$#authors Stover, C.K.; Pham, X.Q.; Erwin, A.L.; Mizoguchi, S.D.; !1Warrener, P.; Hickey, M.J.; Brinkman, F.S.L.; Hufnagle, !1W.O.; Kowalik, D.J.; Lagrou, M.; Garber, R.L.; Goltry, L.; !1Tolentino, E.; Westbrook-Wadman, S.; Yuan, Y.; Brody, L.L.; !1Coulter, S.N.; Folger, K.R.; Kas, A.; Larbig, K.; Lim, R.M.; !1Smith, K.A.; Spencer, D.H.; Wong, G.K.S.; Wu, Z.; Paulsen, !1I.T.; Reizer, J.; Saier, M.H.; Hancock, R.E.W.; Lory, S.; !1Olson, M.V. !$#journal Nature (2000) 406:959-964 !$#title Complete genome sequence of Pseudomonas aeruginosa PA01, an !1opportunistic pathogen. !$#cross-references MUID:20437337; PMID:10984043 !$#accession H83499 !'##status preliminary !'##molecule_type DNA !'##residues 1-163 ##label STO !'##cross-references GB:AE004547; GB:AE004091; NID:g9947089; !1PIDN:AAG04565.1; GSPDB:GN00131; PASP:PA1176 !'##experimental_source strain PAO1 GENETICS !$#gene napF; PA1176 CLASSIFICATION #superfamily ferredoxin protein NapF; ferredoxin 2[4Fe-4S] !1homology SUMMARY #length 163 #molecular-weight 16812 #checksum 2050 SEQUENCE /// ENTRY B82430 #type complete TITLE iron-sulfur cluster-binding protein NapF VCA0676 [imported] - Vibrio cholerae (strain N16961 serogroup O1) ORGANISM #formal_name Vibrio cholerae DATE 18-Aug-2000 #sequence_revision 20-Aug-2000 #text_change 30-Sep-2002 ACCESSIONS B82430 REFERENCE A82035 !$#authors Heidelberg, J.F.; Eisen, J.A.; Nelson, W.C.; Clayton, R.A.; !1Gwinn, M.L.; Dodson, R.J.; Haft, D.H.; Hickey, E.K.; !1Peterson, J.D.; Umayam, L.A.; Gill, S.R.; Nelson, K.E.; !1Read, T.D.; Tettelin, H.; Richardson, D.; Ermolaeva, M.D.; !1Vamathevan, J.; Bass, S.; Qin, H.; Dragoi, I.; Sellers, P.; !1McDonald, L.; Utterback, T.; Fleishmann, R.D.; Nierman, !1W.C.; White, O.; Salzberg, S.L.; Smith, H.O.; Colwell, R.R.; !1Mekalanos, J.J.; Venter, J.C.; Fraser, C.M. !$#journal Nature (2000) 406:477-483 !$#title DNA Sequence of both chromosomes of the cholera pathogen !1Vibrio cholerae. !$#cross-references MUID:20406833; PMID:10952301 !$#accession B82430 !'##status preliminary !'##molecule_type DNA !'##residues 1-168 ##label HEI !'##cross-references GB:AE004397; GB:AE003853; NID:g9658089; !1PIDN:AAF96576.1; GSPDB:GN00127; TIGR:VCA0676 !'##experimental_source serogroup O1; strain N16961; biotype El Tor GENETICS !$#gene VCA0676 !$#map_position 2 CLASSIFICATION #superfamily ferredoxin protein NapF; ferredoxin 2[4Fe-4S] !1homology SUMMARY #length 168 #molecular-weight 18710 #checksum 2869 SEQUENCE /// ENTRY D95346 #type complete TITLE NapF Ferredoxin component of periplasmic nitrate reductase [imported] - Sinorhizobium meliloti (strain 1021) magaplasmid pSymA ORGANISM #formal_name Sinorhizobium meliloti DATE 24-Aug-2001 #sequence_revision 24-Aug-2001 #text_change 30-Sep-2002 ACCESSIONS D95346 REFERENCE A95262 !$#authors Barnett, M.J.; Fisher, R.F.; Jones, T.; Komp, C.; Abola, !1A.P.; Barloy-Hubler, F.; Bowser, L.; Capela, D.; Galibert, !1F.; Gouzy, J.; Gurjal, M.; Hong, A.; Huizar, L.; Hyman, !1R.W.; Kahn, D.; Kahn, M.L.; Kalman, S.; Keating, D.H.; Palm, !1C.; Peck, M.C.; Surzycki, R.; Wells, D.H.; Yeh, K.C.; Davis, !1R.W.; Federspiel, N.A.; Long, S.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (2001) 98:9883-9888 !$#title Nucleotide sequence and predicted functions of the entire !1Sinorhizobium meliloti pSymA megaplasmid. !$#cross-references MUID:21396509; PMID:11481432 !$#accession D95346 !'##status preliminary !'##molecule_type DNA !'##residues 1-166 ##label KUR !'##cross-references GB:AE006469; PIDN:AAK65334.1; PID:g14523791; !1GSPDB:GN00165 !'##experimental_source strain 1021, megaplasmid pSymA REFERENCE A96039 !$#authors Galibert, F.; Finan, T.M.; Long, S.R.; Puhler, A.; Abola, !1P.; Ampe, F.; Barloy-Hubler, F.; Barnett, M.J.; Becker, A.; !1Boistard, P.; Bothe, G.; Boutry, M.; Bowser, L.; Buhrmester, !1J.; Cadieu, E.; Capela, D.; Chain, P.; Cowie, A.; Davis, !1R.W.; Dreano, S.; Federspiel, N.A.; Fisher, R.F.; Gloux, S.; !1Godrie, T.; Goffeau, A.; Golding, B.; Gouzy, J.; Gurjal, M.; !1Hernandez-Lucas, I.; Hong, A.; Huizar, L.; Hyman, R.W.; !1Jones, T.; Kahn, D.; Kahn, M.L.; Kalman, S.; Keating, D.H.; !1Kiss, E.; Komp, C.; Lelaure, V.; Masuy, D.; Palm, C.; Peck, !1M.C.; Pohl, T.M.; Portetelle, D.; Purnelle, B.; Ramsperger, !1U.; Surzycki, R.; Thebault, P.; Vandenbol, M.; Vorholter, !1F.J.; Weidner, S.; Wells, D.H.; Wong, K.; Yeh, K.C.; Batut, !1J. !$#journal Science (2001) 293:668-672 !$#title The composite genome of the legume symbiont Sinorhizobium !1meliloti. !$#cross-references MUID:21368234; PMID:11474104 !$#contents annotation GENETICS !$#gene napF !$#genome plasmid CLASSIFICATION #superfamily ferredoxin protein NapF; ferredoxin 2[4Fe-4S] !1homology SUMMARY #length 166 #molecular-weight 17926 #checksum 7436 SEQUENCE /// ENTRY G98188 #type complete TITLE ferrodoxin-like protein (AF083948) [imported] - Agrobacterium tumefaciens (strain C58, Cereon) ORGANISM #formal_name Agrobacterium tumefaciens DATE 22-Oct-2001 #sequence_revision 22-Oct-2001 #text_change 18-Nov-2002 ACCESSIONS G98188 REFERENCE A97359 !$#authors Goodner, B.; Hinkle, G.; Gattung, S.; Miller, N.; Blanchard, !1M.; Qurollo, B.; Goldman, B.S.; Cao, Y.; Askenazi, M.; !1Halling, C.; Mullin, L.; Houmiel, K.; Gordon, J.; Vaudin, !1M.; Iartchouk, O.; Epp, A.; Liu, F.; Wollam, C.; Allinger, !1M.; Doughty, D.; Scott, C.; Lappas, C.; Markelz, B.; !1Flanagan, C.; Crowell, C.; Gurson, J.; Lomo, C.; Sear, C.; !1Strub, G.; Cielo, C.; Slater, S. !$#journal Science (2001) 294:2323-2328 !$#title Genome Sequence of the Plant Pathogen and Biotechnology !1Agent Agrobacterium tumefaciens C58. !$#cross-references MUID:21608551; PMID:11743194 !$#accession G98188 !'##status preliminary !'##molecule_type DNA !'##residues 1-166 ##label KUR !'##cross-references GB:AE007870; PIDN:AAK89033.1; PID:g15158827; !1GSPDB:GN00170 GENETICS !$#gene AGR_L_920 !$#map_position linear chromosome CLASSIFICATION #superfamily ferredoxin protein NapF; ferredoxin 2[4Fe-4S] !1homology SUMMARY #length 166 #molecular-weight 17360 #checksum 7024 SEQUENCE /// ENTRY AC0789 #type complete TITLE ferredoxin-type protein NapF [imported] - Salmonella enterica subsp. enterica serovar Typhi (strain CT18) ORGANISM #formal_name Salmonella enterica subsp. enterica serovar Typhi #note this species has also been called Salmonella typhi DATE 09-Nov-2001 #sequence_revision 09-Nov-2001 #text_change 18-Nov-2002 ACCESSIONS AC0789 REFERENCE AB0502 !$#authors Parkhill, J.; Dougan, G.; James, K.D.; Thomson, N.R.; !1Pickard, D.; Wain, J.; Churcher, C.; Mungall, K.L.; Bentley, !1S.D.; Holden, M.T.G.; Sebaihia, M.; Baker, S.; Basham, D.; !1Brooks, K.; Chillingworth, T.; Connerton, P.; Cronin, A.; !1Davis, P.; Davies, R.M.; Dowd, L.; White, N.; Farrar, J.; !1Feltwell, T.; Hamlin, N.; Haque, A.; Hien, T.T.; Holroyd, !1S.; Jagels, K.; Krogh, A.; Larsen, T.S.; Leather, S.; Moule, !1S.; O'Gaora, P.; Parry, C.; Quail, M.; Rutherford, K.; !1Simmonds, M.; Skelton, J.; Stevens, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (2001) 413:848-852 !$#title Complete genome sequence of a multiple drug resistant !1Salmonella enterica serovar Typhi CT18. !$#cross-references MUID:21534947; PMID:11677608 !$#accession AC0789 !'##status preliminary !'##molecule_type DNA !'##residues 1-163 ##label PAR !'##cross-references GB:AL513382; PIDN:CAD07493.1; PID:g16503488; !1GSPDB:GN00176 GENETICS !$#gene STY2487 CLASSIFICATION #superfamily ferredoxin protein NapF; ferredoxin 2[4Fe-4S] !1homology SUMMARY #length 163 #molecular-weight 18071 #checksum 6602 SEQUENCE /// ENTRY FEUC #type complete TITLE ferredoxin [3Fe-4S][4Fe-4S], zinc-containing [validated] - Sulfolobus acidocaldarius (strain DSM 639) ORGANISM #formal_name Sulfolobus acidocaldarius #variety DSM 639 DATE 28-Aug-1985 #sequence_revision 11-Jun-1999 #text_change 20-Apr-2000 ACCESSIONS A00223; S63479 REFERENCE A00223 !$#authors Minami, Y.; Wakabayashi, S.; Wada, K.; Matsubara, H.; !1Kerscher, L.; Oesterhelt, D. !$#journal J. Biochem. (1985) 97:745-753 !$#title Amino acid sequence of a ferredoxin from thermoacidophilic !1archaebacterium, Sulfolobus acidocaldarius. Presence of an N !1(6)-monomethyllysine and phyletic consideration of !1archaebacteria. !$#cross-references MUID:85261163; PMID:3926756 !$#accession A00223 !'##molecule_type protein !'##residues 1-8,'H',10-15,'S',17-103 ##label MIN REFERENCE S63479 !$#authors Breton, J.L.; Duff, J.L.C.; Butt, J.N.; Armstrong, F.A.; !1George, S.J.; Petillot, Y.; Forest, E.; Schaefer, G.; !1Thomson, A.J. !$#journal Eur. J. Biochem. (1995) 233:937-946 !$#title Identification of the iron-sulfur clusters in a ferredoxin !1from the archaeon Sulfolobus acidocaldarius: evidence for a !1reduced [3Fe-4S] cluster with pH-dependent electronic !1properties. !$#cross-references MUID:96085161; PMID:8521862 !$#accession S63479 !'##molecule_type protein !'##residues 1-30 ##label BRE !'##experimental_source DSM 639 COMMENT Originally thought to have 2 4Fe-4S clusters, this !1ferredoxin has been shown to be of the [3Fe-4S][4Fe-4S] !1type. CLASSIFICATION #superfamily Sulfolobus zinc-containing ferredoxin; !1ferredoxin 2[4Fe-4S] homology KEYWORDS 3Fe-4S; 4Fe-4S; duplication; electron transfer; iron-sulfur !1protein; metalloprotein; methylated amino acid; zinc FEATURE !$38-101 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$16,19,34,76 #binding_site zinc (His, His, His, Asp) #status !8predicted\ !$29 #modified_site N6-methyllysine (Lys) #status !8experimental\ !$45,51,93 #binding_site 3Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$55,83,86,89 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 103 #molecular-weight 10892 #checksum 5655 SEQUENCE /// ENTRY JC4907 #type complete TITLE ferredoxin [3Fe-4S][4Fe-4S], zinc-containing, precursor [validated] - Sulfolobus sp. (strain 7) ORGANISM #formal_name Sulfolobus sp. #variety strain 7 DATE 04-Feb-2000 #sequence_revision 04-Feb-2000 #text_change 23-Mar-2001 ACCESSIONS JC4907; S78038; PC2290 REFERENCE JC4907 !$#authors Wakagi, T.; Fujii, T.; Oshima, T. !$#journal Biochem. Biophys. Res. Commun. (1996) 225:489-493 !$#title Molecular cloning, sequencing, and heterologous expression !1of a novel zinc-containing ferredoxin gene from a !1thermoacidophilic Archaeon Sulfolobus sp. strain 7. !$#cross-references MUID:96354813; PMID:8753789 !$#accession JC4907 !'##molecule_type DNA !'##residues 1-104 ##label WAK1 !'##cross-references GB:D78179; NID:g2467370 !'##experimental_source strain 7 !$#accession S78038 !'##molecule_type protein !'##residues 2-5,'Q',7-39;64-65,'N',67-70,'A',72-75,'A',77-82,'P',84-87 !1##label WAK2 !'##experimental_source strain 7 REFERENCE PC2290 !$#authors Iwasaki, T.; Fujii, T.; Wakagi, T.; Oshima, T. !$#journal Biochem. Biophys. Res. Commun. (1995) 206:563-569 !$#title Alternative form of the dicluster ferredoxin from the !1thermoacidophilic archaeon, Sulfolobus sp. strain 7. !$#cross-references MUID:95126955; PMID:7826373 !$#accession PC2290 !'##molecule_type protein !'##residues 2-25,'L',27-31 ##label IWA REFERENCE A44672 !$#authors Iwasaki, T.; Wakagi, T.; Isogai, Y.; Tanaka, K.; Iizuka, T.; !1Oshima, T. !$#journal J. Biol. Chem. (1994) 269:29444-29450 !$#title Functional and evolutionary implications of a [3Fe-4S] !1cluster of the dicluster-type ferredoxin from the !1thermoacidophilic archaeon, Sulfolobus sp. strain 7. !$#cross-references MUID:95050783; PMID:7961925 !$#contents annotation; reclassification of source species; !1characterization of iron-sulfur clusters REFERENCE A73354 !$#authors Fujii, T.; Hata, Y.; Moriyama, H.; Wakagi, T.; Tanaka, N.; !1Oshima, T. !$#submission submitted to the Brookhaven Protein Data Bank, August 1996 !$#cross-references PDB:1XER !$#contents annotation; X-ray crystallography, 2.0 angstroms, residues !12-104 REFERENCE A58990 !$#authors Fujii, T.; Hata, Y.; Wakagi, T.; Tanaka, N.; Oshima, T. !$#journal Nat. Struct. Biol. (1996) 3:834-837 !$#title Novel zinc-binding centre in thermoacidophilic archaeal !1ferredoxins. !$#cross-references MUID:96433069; PMID:8836097 !$#contents annotation; X-ray crystallography, 2.0 angstroms CLASSIFICATION #superfamily Sulfolobus zinc-containing ferredoxin; !1ferredoxin 2[4Fe-4S] homology KEYWORDS 3Fe-4S; 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein; methylated amino acid; zinc FEATURE !$2-103 #product ferredoxin #status experimental #label MAT\ !$39-102 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$17,20,35,77 #binding_site zinc (His, His, His, Asp) #status !8experimental\ !$30 #modified_site N6-methyllysine (Lys) #status !8experimental\ !$46,52,94 #binding_site 3Fe-4S cluster (Cys) (covalent) #status !8experimental\ !$56,84,90 #binding_site 3Fe-4S cluster (Cys) (covalent) #link !8FE3 #status experimental\ !$56,84,87,90 #binding_site 4Fe-4S cluster (Cys) (covalent) #link !8FE4 #status predicted SUMMARY #length 104 #molecular-weight 11134 #checksum 7850 SEQUENCE /// ENTRY FEYTA #type complete TITLE ferredoxin [3Fe-4S][4Fe-4S], zinc-containing [validated] - Thermoplasma acidophilum ORGANISM #formal_name Thermoplasma acidophilum DATE 19-Feb-1984 #sequence_revision 04-Feb-2000 #text_change 16-Jun-2000 ACCESSIONS T37333; A00222 REFERENCE Z21695 !$#authors Cosper, N.J.; Stalhandske, C.M.V.; Iwasaki, H.; Oshima, T.; !1Scott, R.A.; Iwasaki, T. !$#journal J. Biol. Chem. (1999) 274:23160-23168 !$#title Structural conservation of the isolated zinc site in !1archaeal zinc-containing ferredoxins as revealed by X-ray !1absorption spectroscopic analysis and its evolutionary !1implications. !$#cross-references MUID:99367440; PMID:10438486 !$#accession T37333 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-143 ##label COS !'##cross-references EMBL:AB023294; NID:g5689050; PIDN:BAA82797.1; !1PID:g5689051 !'##experimental_source strain HO-62 REFERENCE A00222 !$#authors Wakabayashi, S.; Fujimoto, N.; Wada, K.; Matsubara, H.; !1Kerscher, L.; Oesterhelt, D. !$#journal FEBS Lett. (1983) 162:21-24 !$#title Amino acid sequence of a ferredoxin from thermoacidophilic !1archaebacteria, Thermoplasma acidophilum. !$#accession A00222 !'##molecule_type protein !'##residues 2-101,'Q',103-105,'E',107-143 ##label WAK !'##experimental_source strain DSM 1728 !'##note the authors believe this ferredoxin has two 4Fe-4S clusters REFERENCE A59164 !$#authors Iwasaki, T.; Suzuki, T.; Kon, T.; Imai, T.; Urushiyama, A.; !1Ohmori, D.; Oshima, T. !$#journal J. Biol. Chem. (1997) 272:3453-3458 !$#title Novel zinc-containing ferredoxin family in thermoacidophilic !1archaea. !$#cross-references MUID:97166191; PMID:9013590 !$#contents annotation; metal binding sites !$#note the protein is shown to have one zinc, one 3Fe-4S cluster !1and one 4Fe-4S cluster COMMENT For the structure of a closely related sequence with !1[3Fe-4S][4Fe-4S] clusters, see PIR:JC4907. GENETICS !$#gene zfx CLASSIFICATION #superfamily Sulfolobus zinc-containing ferredoxin; !1ferredoxin 2[4Fe-4S] homology KEYWORDS 3Fe-4S; 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein; zinc FEATURE !$2-143 #product ferredoxin [3Fe-4S][4Fe-4S] #status !8experimental #label MAT\ !$62-142 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$31,34,58,117 #binding_site zinc (His, His, His, Asp) #status !8experimental\ !$69,75,134 #binding_site 3Fe-4S cluster (Cys) (covalent) #status !8experimental\ !$79,124,127,130 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8experimental SUMMARY #length 143 #molecular-weight 16036 #checksum 2864 SEQUENCE /// ENTRY C37777 #type complete TITLE polyferredoxin 6x2[4Fe-4S] - Methanothermus fervidus ORGANISM #formal_name Methanothermus fervidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C37777 REFERENCE A37777 !$#authors Steigerwald, V.J.; Beckler, G.S.; Reeve, J.N. !$#journal J. Bacteriol. (1990) 172:4715-4718 !$#title Conservation of hydrogenase and polyferredoxin structures in !1the hyperthermophilic archaebacterium Methanothermus !1fervidus. !$#cross-references MUID:90330590; PMID:2115877 !$#accession C37777 !'##status preliminary !'##molecule_type DNA !'##residues 1-412 ##label STE !'##cross-references GB:M34016; NID:g149803; PIDN:AAA72833.1; !1PID:g149806 CLASSIFICATION #superfamily polyferredoxin 6x2[4Fe-4S]; ferredoxin !12[4Fe-4S] homology KEYWORDS electron transfer FEATURE !$2-55 #domain ferredoxin 2[4Fe-4S] homology #label FER1\ !$68-125 #domain ferredoxin 2[4Fe-4S] homology #label FER2\ !$139-195 #domain ferredoxin 2[4Fe-4S] homology #label FER3\ !$209-263 #domain ferredoxin 2[4Fe-4S] homology #label FER4\ !$277-342 #domain ferredoxin 2[4Fe-4S] homology #label FER5\ !$358-412 #domain ferredoxin 2[4Fe-4S] homology #label FER6 SUMMARY #length 412 #molecular-weight 44642 #checksum 5230 SEQUENCE /// ENTRY G30315 #type complete TITLE polyferredoxin 6x2[4Fe-4S] mvhB - Methanobacterium thermoautotrophicum (strains Delta H and Marburg) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS G30315; H69017; S20413 REFERENCE A30315 !$#authors Reeve, J.N.; Beckler, G.S.; Cram, D.S.; Hamilton, P.T.; !1Brown, J.W.; Krzycki, J.A.; Kolodziej, A.F.; Alex, L.; !1Orme-Johnson, W.H.; Walsh, C.T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:3031-3035 !$#title A hydrogenase-linked gene in Methanobacterium !1thermoautotrophicum strain delta-H encodes a polyferredoxin. !$#cross-references MUID:89240669; PMID:2654933 !$#accession G30315 !'##molecule_type DNA !'##residues 1-388,'A',390-412 ##label REE !'##cross-references GB:J04540; NID:g149730 !'##experimental_source strain Delta H !'##note the sequence is revised in GenBank entry MBFMVRH, release !1109.0, (PID:g149734) REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession H69017 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-95,'G',97-412 ##label MTH !'##cross-references GB:AE000883; GB:AE000666; NID:g2622231; !1PIDN:AAB85622.1; PID:g2622237 !'##experimental_source strain Delta H REFERENCE S20413 !$#authors Hedderich, R.; Albracht, S.P.J.; Linder, D.; Koch, J.; !1Thauer, R.K. !$#journal FEBS Lett. (1992) 298:65-68 !$#title Isolation and characterization of polyferredoxin from !1Methanobacterium thermoautotrophicum. The mvhB gene product !1of the methylviologen-reducing hydrogenase operon. !$#cross-references MUID:92183831; PMID:1312016 !$#accession S20413 !'##molecule_type protein !'##residues 1-2,'V',4-28 ##label HED !'##cross-references PIDN:AAB21772.1; PID:g247131 !'##experimental_source strain Marburg, DSM 2133 GENETICS !$#gene mvhB; MTH1133 CLASSIFICATION #superfamily polyferredoxin 6x2[4Fe-4S]; ferredoxin !12[4Fe-4S] homology KEYWORDS 4Fe-4S; iron-sulfur protein; metalloprotein FEATURE !$2-55 #domain ferredoxin 2[4Fe-4S] homology #label FER1\ !$69-125 #domain ferredoxin 2[4Fe-4S] homology #label FER2\ !$139-195 #domain ferredoxin 2[4Fe-4S] homology #label FER3\ !$209-264 #domain ferredoxin 2[4Fe-4S] homology #label FER4\ !$278-343 #domain ferredoxin 2[4Fe-4S] homology #label FER5\ !$359-412 #domain ferredoxin 2[4Fe-4S] homology #label FER6\ !$9,12,15,47 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8experimental\ !$19,34,37,43 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$76,79,82,117 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$86,107,110,113 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$146,149,152,187 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$156,177,180,183 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$216,219,222,256 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$226,246,249,252 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$285,291,335 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$295,325,328,331 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$366,369,372,404 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$376,394,397,400 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 412 #molecular-weight 44117 #checksum 4332 SEQUENCE /// ENTRY S24802 #type complete TITLE polyferredoxin 6x2[4Fe-4S] vhuB [similarity] - Methanococcus voltae ORGANISM #formal_name Methanococcus voltae DATE 10-Sep-1999 #sequence_revision 18-Aug-2000 #text_change 19-Jan-2001 ACCESSIONS S24802 REFERENCE S16721 !$#authors Halboth, S.; Klein, A. !$#submission submitted to the EMBL Data Library, August 1991 !$#description Methanococcus voltae harbors two gene groups each of !1homologous (NiFe)- and (NiFeSe)- hydrogenases which reduce !1cofactor F420 or only electron accepting dyes. !$#accession S24802 !'##molecule_type DNA !'##residues 1-398 ##label HAL !'##cross-references EMBL:X61204; NID:g1747406; PIDN:CAA43512.1; !1PID:g1747410 !'##experimental_source strain PS(DSM1537) REFERENCE A59304 !$#authors Halboth, S.; Klein, A. !$#journal Mol. Gen. Genet. (1992) 233:217-224 !$#title Methanococcus voltae harbors four gene clusters potentially !1encoding two [NiFe] and two [NiFeSe] hydrogenases, each of !1the cofactor F420-reducing or F420-non-reducing types. !$#cross-references MUID:92293118; PMID:1603063 !$#contents annotation GENETICS !$#gene vhuB CLASSIFICATION #superfamily polyferredoxin 6x2[4Fe-4S]; ferredoxin !12[4Fe-4S] homology FEATURE !$4-52 #domain ferredoxin 2[4Fe-4S] homology #label FER1\ !$56-109 #domain ferredoxin 2[4Fe-4S] homology #label FER2\ !$125-179 #domain ferredoxin 2[4Fe-4S] homology #label FER3\ !$192-247 #domain ferredoxin 2[4Fe-4S] homology #label FER4\ !$261-329 #domain ferredoxin 2[4Fe-4S] homology #label FER5\ !$341-395 #domain ferredoxin 2[4Fe-4S] homology #label FER6 SUMMARY #length 398 #molecular-weight 43187 #checksum 7902 SEQUENCE /// ENTRY IHKREV #type complete TITLE high potential iron-sulfur protein [validated] - Chromatium vinosum ALTERNATE_NAMES HiPIP ORGANISM #formal_name Chromatium vinosum DATE 24-Apr-1984 #sequence_revision 24-Oct-1997 #text_change 15-Sep-2000 ACCESSIONS A92330; A92143; A00263 REFERENCE A92330 !$#authors Tedro, S.M.; Meyer, T.E.; Bartsch, R.G.; Kamen, M.D. !$#journal J. Biol. Chem. (1981) 256:731-735 !$#title Primary structures of high potential, four-iron-sulfur !1ferredoxins from the purple sulfur photosynthetic bacteria, !1Thiocapsa roseopersicina and Chromatium gracile. !$#cross-references MUID:81094036; PMID:7451471 !$#accession A92330 !'##molecule_type protein !'##residues 1-73,'D',75-85 ##label TED REFERENCE A92143 !$#authors Dus, K.; Tedro, S.; Bartsch, R.G. !$#journal J. Biol. Chem. (1973) 248:7318-7331 !$#title The complete amino acid sequence of Chromatium high !1potential iron sulfur protein. !$#cross-references MUID:74012043; PMID:4745771 !$#accession A92143 !'##molecule_type protein !'##residues 1-10,'N',12-44,'D',46-85 ##label DUS !'##experimental_source strain D REFERENCE A65814 !$#authors Banci, L.; Bertini, I.; Dikiy, A.; Kastrau, D.H.W.; !1Luchinat, C.; Sompornpisut, P. !$#submission submitted to the Brookhaven Protein Data Bank, January 1995 !$#cross-references PDB:1HRQ !$#contents annotation; conformation by (1)H-NMR, reduced form, residues !11-85 REFERENCE A66207 !$#authors Bertini, I.; Dikiy, A.; Kastrau, D.H.W.; Luchinat, C.; !1Sompornpisut, P. !$#submission submitted to the Brookhaven Protein Data Bank, December 1995 !$#cross-references PDB:1NEH !$#contents annotation; conformation by (1)H-NMR, oxidized form, !1residues 1-85 REFERENCE A44688 !$#authors Backes, G.; Mino, Y.; Loehr, T.M.; Meyer, T.E.; Cusanovich, !1M.A.; Sweeney, W.V.; Adman, E.T.; Sanders-Loehr, J. !$#journal J. Am. Chem. Soc. (1991) 113:2055-2064 !$#title The environment of Fe4S4 clusters in ferredoxins and !1high-potential iron proteins. New information from x-ray !1crystallography and resonance Raman spectroscopy. !$#contents annotation; X-ray crystallography, 2.0 angstroms !$#note assignment of Raman spectra frequencies and hydrogen bonds !1around the iron-sulfur cluster REFERENCE A92153 !$#authors Carter Jr., C.W.; Kraut, J.; Freer, S.T.; Xuong, N.H.; !1Alden, R.A.; Bartsch, R.G. !$#journal J. Biol. Chem. (1974) 249:4212-4225 !$#title Two-angstrom crystal structure of oxidized Chromatium high !1potential iron protein. !$#cross-references MUID:74309824; PMID:4855287 !$#contents annotation; X-ray crystallography, 2.0 angstroms REFERENCE A92161 !$#authors Carter Jr., C.W.; Kraut, J.; Freer, S.T.; Alden, R.A. !$#journal J. Biol. Chem. (1974) 249:6339-6346 !$#title Comparison of oxidation-reduction site geometries in !1oxidized and reduced Chromatium high potential iron protein !1and oxidized Peptococcus aerogenes ferredoxin. !$#cross-references MUID:75019502; PMID:4417854 !$#contents annotation; X-ray crystallography !$#note structures of the oxidized and reduced forms are compared !1with each other and with oxidized bacterial ferredoxin CLASSIFICATION #superfamily high potential iron-sulfur protein KEYWORDS 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$43,46,63,77 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8experimental SUMMARY #length 85 #molecular-weight 8905 #checksum 1546 SEQUENCE /// ENTRY IHTFER #type complete TITLE high potential iron-sulfur protein - Thiocapsa roseopersicina (tentative sequence) ORGANISM #formal_name Thiocapsa roseopersicina DATE 31-Mar-1981 #sequence_revision 31-Mar-1981 #text_change 31-Mar-2000 ACCESSIONS A00264 REFERENCE A92330 !$#authors Tedro, S.M.; Meyer, T.E.; Bartsch, R.G.; Kamen, M.D. !$#journal J. Biol. Chem. (1981) 256:731-735 !$#title Primary structures of high potential, four-iron-sulfur !1ferredoxins from the purple sulfur photosynthetic bacteria, !1Thiocapsa roseopersicina and Chromatium gracile. !$#cross-references MUID:81094036; PMID:7451471 !$#accession A00264 !'##molecule_type protein !'##residues 1-85 ##label TED CLASSIFICATION #superfamily high potential iron-sulfur protein KEYWORDS 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$43,46,63,77 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 85 #molecular-weight 8889 #checksum 1802 SEQUENCE /// ENTRY IHKREG #type complete TITLE high potential iron-sulfur protein - Chromatium gracile (tentative sequence) ORGANISM #formal_name Chromatium gracile DATE 31-Mar-1981 #sequence_revision 31-Mar-1981 #text_change 31-Mar-2000 ACCESSIONS A00265 REFERENCE A92330 !$#authors Tedro, S.M.; Meyer, T.E.; Bartsch, R.G.; Kamen, M.D. !$#journal J. Biol. Chem. (1981) 256:731-735 !$#title Primary structures of high potential, four-iron-sulfur !1ferredoxins from the purple sulfur photosynthetic bacteria, !1Thiocapsa roseopersicina and Chromatium gracile. !$#cross-references MUID:81094036; PMID:7451471 !$#accession A00265 !'##molecule_type protein !'##residues 1-83 ##label TED CLASSIFICATION #superfamily high potential iron-sulfur protein KEYWORDS 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$43,46,61,75 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 83 #molecular-weight 9052 #checksum 8390 SEQUENCE /// ENTRY IHTF #type complete TITLE high potential iron-sulfur protein - Thiocapsa pfennigii ORGANISM #formal_name Thiocapsa pfennigii DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 18-Sep-1998 ACCESSIONS A00266 REFERENCE A00266 !$#authors Tedro, S.M.; Meyer, T.E.; Kamen, M.D. !$#journal J. Biol. Chem. (1974) 249:1182-1188 !$#title Primary structure of a high potential iron-sulfur protein !1from the photosynthetic bacterium Thiocapsa pfennigii. !$#cross-references MUID:74107423; PMID:4814341 !$#accession A00266 !'##molecule_type protein !'##residues 1-81 ##label TED !'##experimental_source strain KIMG 8816 CLASSIFICATION #superfamily high potential iron-sulfur protein KEYWORDS 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$43,46,59,73 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 81 #molecular-weight 8951 #checksum 7320 SEQUENCE /// ENTRY IHPC #type complete TITLE high potential iron-sulfur protein - Paracoccus sp. ORGANISM #formal_name Paracoccus sp. DATE 31-May-1979 #sequence_revision 23-Oct-1981 #text_change 18-Sep-1998 ACCESSIONS A00267 REFERENCE A00267 !$#authors Tedro, S.M.; Meyer, T.E.; Kamen, M.D. !$#journal J. Biol. Chem. (1977) 252:7826-7833 !$#title Primary structure of a high potential iron-sulfur protein !1from a moderately halophilic denitrifying coccus. !$#cross-references MUID:78026535; PMID:914842 !$#accession A00267 !'##molecule_type protein !'##residues 1-71 ##label TED !'##experimental_source ATCC 12084 COMMENT Paracoccus sp. is a halotolerant species isolated from !1decaying whale meat. CLASSIFICATION #superfamily high potential iron-sulfur protein KEYWORDS 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein; pyroglutamic acid FEATURE !$1 #modified_site pyrrolidone carboxylic acid (Gln) !8#status experimental\ !$37,40,50,64 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 71 #molecular-weight 7809 #checksum 785 SEQUENCE /// ENTRY IHRFG #type complete TITLE high potential iron-sulfur protein - Rhodocyclus gelatinosus ORGANISM #formal_name Rhodocyclus gelatinosus DATE 13-Jul-1981 #sequence_revision 13-Jul-1981 #text_change 18-Sep-1998 ACCESSIONS A00268 REFERENCE A00268 !$#authors Tedro, S.M.; Meyer, T.E.; Kamen, M.D. !$#journal J. Biol. Chem. (1976) 251:129-136 !$#title Primary structure of a high potential iron-sulfur protein !1from the purple non-sulfur photosynthetic bacterium !1Rhodopseudomonas gelatinosa. !$#cross-references MUID:76069285; PMID:1244346 !$#accession A00268 !'##molecule_type protein !'##residues 1-74 ##label TED !'##experimental_source strain C.B. van Niel ATH 2.2.1, ATCC 17011 CLASSIFICATION #superfamily high potential iron-sulfur protein KEYWORDS 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$36,39,53,67 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 74 #molecular-weight 7616 #checksum 2272 SEQUENCE /// ENTRY IHQFT #type complete TITLE high potential iron-sulfur protein - Rhodocyclus tenuis ORGANISM #formal_name Rhodocyclus tenuis DATE 30-Jun-1979 #sequence_revision 30-Jun-1979 #text_change 18-Sep-1998 ACCESSIONS A00269 REFERENCE A00269 !$#authors Tedro, S.M.; Meyer, T.E.; Kamen, M.D. !$#journal J. Biol. Chem. (1979) 254:1495-1500 !$#title Primary structure of a high potential, four-iron-sulfur !1ferredoxin from the photosynthetic bacterium Rhodospirillum !1tenue. !$#cross-references MUID:79109745; PMID:762147 !$#accession A00269 !'##molecule_type protein !'##residues 1-63 ##label TED !'##experimental_source strain 3761 !'##note the identities of Asp-47 and Gln-49 are tentative CLASSIFICATION #superfamily high potential iron-sulfur protein KEYWORDS 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$23,26,41,56 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 63 #molecular-weight 6503 #checksum 4830 SEQUENCE /// ENTRY IHER1 #type complete TITLE high potential iron-sulfur protein 1 [validated] - Ectothiorhodospira halophila ALTERNATE_NAMES high-redox-potential ferredoxin I; HiPIP ORGANISM #formal_name Ectothiorhodospira halophila DATE 04-Dec-1986 #sequence_revision 10-Oct-1997 #text_change 15-Sep-2000 ACCESSIONS S48703; A00270 REFERENCE S48703 !$#authors Bertini, I.; Felli, I.C.; Kastrau, D.H.W.; Luchinat, C.; !1Piccioli, M.; Viezzoli, M.S. !$#journal Eur. J. Biochem. (1994) 225:703-714 !$#title Sequence-specific assignment of the (1)H and (15)N nuclear !1magnetic resonance spectra of the reduced recombinant !1high-potential iron-sulfur protein I from Ectothiorhodospira !1halophila. !$#cross-references MUID:95045521; PMID:7957186 !$#accession S48703 !'##molecule_type protein !'##residues 'AS',1-33;35-71 ##label BER !'##note sequenced by (1)H and (15)N NMR; modified sequence expressed in !1E. coli REFERENCE A90077 !$#authors Tedro, S.M.; Meyer, T.E.; Kamen, M.D. !$#journal Arch. Biochem. Biophys. (1985) 241:656-664 !$#title Amino acid sequence of high-redox-potential ferrodoxin !1(HiPIP) isozymes from the extremely halophilic purple !1phototrophic bacterium, Ectothiorhodospira halophila. !$#cross-references MUID:85305760; PMID:4037807 !$#accession A00270 !'##molecule_type protein !'##residues 1-18,'PSHG',24-71 ##label TED REFERENCE A50456 !$#authors Breiter, D.R.; Meyer, T.E.; Rayment, I.; Holden, H.M. !$#submission submitted to the Brookhaven Protein Data Bank, June 1991 !$#cross-references PDB:2HIP !$#contents annotation; X-ray crystallography, 2.5 angstroms, residues !11-71 REFERENCE A41003 !$#authors Breiter, D.R.; Meyer, T.E.; Rayment, I.; Holden, H.M. !$#journal J. Biol. Chem. (1991) 266:18660-18667 !$#title The molecular structure of the high potential iron-sulfur !1protein isolated from Ectothiorhodospira halophila !1determined at 2.5-Angstrom resolution. !$#cross-references MUID:92011624; PMID:1917989 !$#contents annotation; X-ray crystallography, 2.5 angstroms; sequence !1revision !$#note sequence correction; peptide sequencing not performed FUNCTION !$#description high reduction potential electron transfer CLASSIFICATION #superfamily high potential iron-sulfur protein KEYWORDS 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$31,34,48,64 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 71 #molecular-weight 7837 #checksum 972 SEQUENCE /// ENTRY IHER2 #type complete TITLE high potential iron-sulfur protein II - Ectothiorhodospira halophila ALTERNATE_NAMES high-redox-potential ferredoxin 2; HiPIP ORGANISM #formal_name Ectothiorhodospira halophila DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 18-Sep-1998 ACCESSIONS A00271 REFERENCE A90077 !$#authors Tedro, S.M.; Meyer, T.E.; Kamen, M.D. !$#journal Arch. Biochem. Biophys. (1985) 241:656-664 !$#title Amino acid sequence of high-redox-potential ferrodoxin !1(HiPIP) isozymes from the extremely halophilic purple !1phototrophic bacterium, Ectothiorhodospira halophila. !$#cross-references MUID:85305760; PMID:4037807 !$#accession A00271 !'##molecule_type protein !'##residues 1-76 ##label TED COMMENT The high potential iron-sulfur protein (HiPIP) are a class !1of high-redox-potential 4Fe-4S proteins distinct from !1ferrdoxins. They function in anaerobic electron transport in !1most purple and in some other photosynthetic bacteria and in !1at least one genus (Paracoccus) of halophilic, denitrifying !1bacteria. In E. halophila, an extremely halophilic, purple, !1sulfur, photosynthetic bacterium, two HiPIP forms are found. CLASSIFICATION #superfamily high potential iron-sulfur protein KEYWORDS 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$38,41,54,70 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 76 #molecular-weight 8560 #checksum 9572 SEQUENCE /// ENTRY RUPE #type complete TITLE rubredoxin - Peptostreptococcus asaccharolyticus ORGANISM #formal_name Peptostreptococcus asaccharolyticus DATE 13-Jul-1981 #sequence_revision 13-Jul-1981 #text_change 24-Oct-1997 ACCESSIONS A00272 REFERENCE A00272 !$#authors Bachmayer, H.; Benson, A.M.; Yasunobu, K.T.; Garrard, W.T.; !1Whiteley, H.R. !$#journal Biochemistry (1968) 7:986-996 !$#title Nonheme iron proteins. IV. Structural studies of Micrococcus !1aerogenes rubredoxin. !$#cross-references MUID:68311179; PMID:5657864 !$#accession A00272 !'##molecule_type protein !'##residues 1-53 ##label BAC !'##note the source was designated as Peptococcus aerogenes CLASSIFICATION #superfamily rubredoxin; rubredoxin homology KEYWORDS electron transfer; iron; metalloprotein FEATURE !$3-48 #domain rubredoxin homology #label RUB\ !$6,9,38,41 #binding_site iron (Cys) #status predicted SUMMARY #length 53 #molecular-weight 5911 #checksum 6231 SEQUENCE /// ENTRY RUCLEP #type complete TITLE rubredoxin [validated] - Clostridium pasteurianum ORGANISM #formal_name Clostridium pasteurianum DATE 24-Apr-1984 #sequence_revision 19-May-1995 #text_change 15-Sep-2000 ACCESSIONS S29120; A00273 REFERENCE S29117 !$#authors Mathieu, I.; Meyer, J.; Moulis, J.M. !$#journal Biochem. J. (1992) 285:255-262 !$#title Cloning, sequencing and expression in Escherichia coli of !1the rubredoxin gene from Clostridium pasteurianum. !$#cross-references MUID:92344580; PMID:1637309 !$#accession S29120 !'##molecule_type DNA !'##residues 1-54 ##label MAT !'##cross-references EMBL:M60116; NID:g144905; PIDN:AAA23279.1; !1PID:g144909 !'##note the amidation states of residues 14, 22, and 48 were confirmed !1by protein sequencing of the protein from Clostridium !1pasteurianum !'##note the amino end of the mature protein from Clostridium !1pasteurianum is blocked, but that expressed by Escherichia !1coli is not REFERENCE A94450 !$#authors McCarthy, K.F. !$#citation Ph.D. thesis, George Washington University, 1972 !$#description The primary structure of Clostridium pasteurianum !1rubredoxin. !$#accession A00273 !'##molecule_type protein !'##residues 1-13,'D',15-21,'D',23-47,'E',49-54 ##label MCC !'##note peptides for which chemical overlaps were not determined were !1positioned on the basis of X-ray crystallographic data REFERENCE A65887 !$#authors Dauter, Z.; Wilson, K.S.; Sieker, L.C.; Moulis, J.M.; Meyer, !1J. !$#submission submitted to the Brookhaven Protein Data Bank, December 1995 !$#cross-references PDB:1IRO !$#contents annotation; X-ray crystallography, 1.1 angstroms, residues !11-53 REFERENCE A65886 !$#authors Dauter, Z.; Wilson, K.S.; Sieker, L.C.; Moulis, J.M.; Meyer, !1J. !$#submission submitted to the Brookhaven Protein Data Bank, December 1995 !$#cross-references PDB:1IRN !$#contents annotation; X-ray crystallography, 1.2 angstroms, residues !11-53 REFERENCE A58640 !$#authors Watenpaugh, K.D.; Sieker, L.C.; Jensen, L.H. !$#journal J. Mol. Biol. (1980) 138:615-633 !$#title Crystallographic refinement of rubredoxin at 1.2 Angstroms !1resolution. !$#cross-references MUID:81009589; PMID:7411618 !$#contents annotation; X-ray crystallography, 1.2 angstroms REFERENCE A90009 !$#authors Watenpaugh, K.D.; Siecker, L.C.; Herriott, J.R.; Jensen, !1L.H. !$#journal Acta Crystallogr. (1973) B29:943-956 !$#title Refinement of the model of a protein: rubredoxin at 1.5 !1angstrom resolution. !$#contents annotation; X-ray crystallography, 1.5 angstroms CLASSIFICATION #superfamily rubredoxin; rubredoxin homology KEYWORDS electron transfer; iron; metalloprotein FEATURE !$3-49 #domain rubredoxin homology #label RUB\ !$1 #modified_site N-formylmethionine #status !8experimental\ !$6,9,39,42 #binding_site iron (Cys) #status experimental SUMMARY #length 54 #molecular-weight 6048 #checksum 673 SEQUENCE /// ENTRY JU0074 #type complete TITLE rubredoxin - Clostridium perfringens ORGANISM #formal_name Clostridium perfringens DATE 28-Feb-1990 #sequence_revision 22-Jul-1994 #text_change 24-Oct-1997 ACCESSIONS JU0074 REFERENCE JU0074 !$#authors Seki, Y.; Seki, S.; Satoh, M.; Ikeda, A.; Ishimoto, M. !$#journal J. Biochem. (1989) 106:336-341 !$#title Rubredoxin from Clostridium perfringens: complete amino acid !1sequence and participation in nitrate reduction. !$#cross-references MUID:90036784; PMID:2553684 !$#accession JU0074 !'##molecule_type protein !'##residues 1-54 ##label SEK COMMENT The protein is reduced with NADH in the presence of a !1specific NAD(P)H oxidoreductase. CLASSIFICATION #superfamily rubredoxin; rubredoxin homology KEYWORDS electron transfer; iron; metalloprotein FEATURE !$3-49 #domain rubredoxin homology #label RUB\ !$6,9,39,42 #binding_site iron (Cys) #status predicted SUMMARY #length 54 #molecular-weight 6004 #checksum 1502 SEQUENCE /// ENTRY JU0127 #type complete TITLE rubredoxin - "Butyribacterium methylotrophicum" ORGANISM #formal_name "Butyribacterium methylotrophicum" DATE 31-Mar-1990 #sequence_revision 22-Jul-1994 #text_change 24-Oct-1997 ACCESSIONS JU0127 REFERENCE A91913 !$#authors Saeki, K.; Yao, Y.; Wakabayashi, S.; Shen, G.J.; Zeikus, !1J.G.; Matsubara, H. !$#journal J. Biochem. (1989) 106:656-662 !$#title Ferredoxin and rubredoxin from Butyribacterium !1methylotrophicum: complete primary structures and !1construction of phylogenetic trees. !$#cross-references MUID:90110065; PMID:2606914 !$#accession JU0127 !'##molecule_type protein !'##residues 1-53 ##label SAE COMMENT Rubredoxin is a nonheme iron protein and substitutes for !1ferredoxin in some enzymatic reactions. CLASSIFICATION #superfamily rubredoxin; rubredoxin homology KEYWORDS electron transfer; iron; metalloprotein FEATURE !$3-49 #domain rubredoxin homology #label RUB\ !$6,9,39,42 #binding_site iron (Cys) #status predicted SUMMARY #length 53 #molecular-weight 5672 #checksum 6265 SEQUENCE /// ENTRY A33173 #type complete TITLE rubredoxin [validated] - Clostridium thermosaccharolyticum ORGANISM #formal_name Clostridium thermosaccharolyticum, Clostridium tartarivorum DATE 30-Apr-1991 #sequence_revision 24-Oct-1997 #text_change 16-Jun-2000 ACCESSIONS A33173 REFERENCE A33173 !$#authors Meyer, J.; Gagnon, J.; Sieker, L.C.; Van Dorsselaer, A.; !1Moulis, J.M. !$#journal Biochem. J. (1990) 271:839-841 !$#title Rubredoxin from Clostridium thermosaccharolyticum. Amino !1acid sequence, mass-spectrometric and preliminary !1crystallographic data. !$#cross-references MUID:91058526; PMID:2244884 !$#accession A33173 !'##molecule_type protein !'##residues 1-52 ##label MEY CLASSIFICATION #superfamily rubredoxin; rubredoxin homology KEYWORDS electron transfer; iron; metalloprotein FEATURE !$3-49 #domain rubredoxin homology #label RUB\ !$1 #modified_site N-formylmethionine #status !8experimental\ !$6,9,39,42 #binding_site iron (Cys) #status predicted SUMMARY #length 52 #molecular-weight 5909 #checksum 3140 SEQUENCE /// ENTRY A27537 #type complete TITLE rubredoxin - Chlorobium limicola f.sp. thiosulfatophilum ORGANISM #formal_name Chlorobium limicola f.sp. thiosulfatophilum DATE 05-Jun-1988 #sequence_revision 22-Jul-1994 #text_change 24-Oct-1997 ACCESSIONS A27537 REFERENCE A27537 !$#authors Woolley, K.J.; Meyer, T.E. !$#journal Eur. J. Biochem. (1987) 163:161-166 !$#title The complete amino acid sequence of rubredoxin from the !1green phototrophic bacterium Chlorobium thiosulphatophilum !1strain PM. !$#cross-references MUID:87133563; PMID:3816795 !$#note Chlorobium thiosulphatophilum !$#accession A27537 !'##molecule_type protein !'##residues 1-53 ##label WOO CLASSIFICATION #superfamily rubredoxin; rubredoxin homology KEYWORDS electron transfer; iron; metalloprotein FEATURE !$3-49 #domain rubredoxin homology #label RUB\ !$6,9,39,42 #binding_site iron (Cys) #status predicted SUMMARY #length 53 #molecular-weight 5843 #checksum 6847 SEQUENCE /// ENTRY A33182 #type complete TITLE rubredoxin - Clostridium sticklandii ORGANISM #formal_name Clostridium sticklandii DATE 03-Feb-1994 #sequence_revision 03-Feb-1994 #text_change 24-Oct-1997 ACCESSIONS A33182 REFERENCE A33182 !$#authors Meyer, J.; Gagnon, J.; Moulis, J.M. !$#submission submitted to the Protein Sequence Database, April 1991 !$#accession A33182 !'##molecule_type protein !'##residues 1-53 ##label MEY !'##experimental_source ATCC 12662 CLASSIFICATION #superfamily rubredoxin; rubredoxin homology KEYWORDS electron transfer; iron; metalloprotein FEATURE !$3-49 #domain rubredoxin homology #label RUB\ !$1 #modified_site N-formylmethionine #status !8experimental\ !$6,9,39,42 #binding_site iron (Cys) #status predicted SUMMARY #length 53 #molecular-weight 5889 #checksum 6706 SEQUENCE /// ENTRY RUDV #type complete TITLE rubredoxin [validated] - Desulfovibrio vulgaris (strain Hildenborough) ORGANISM #formal_name Desulfovibrio vulgaris #variety strain Hildenborough DATE 24-Apr-1984 #sequence_revision 30-Jun-1991 #text_change 15-Sep-2000 ACCESSIONS B33962; A00274 REFERENCE A33962 !$#authors Brumlik, M.J.; Voordouw, G. !$#journal J. Bacteriol. (1989) 171:4996-5004 !$#title Analysis of the transcriptional unit encoding the genes for !1rubredoxin (rub) and a putative rubredoxin oxidoreductase !1(rbo) in Desulfovibrio vulgaris Hildenborough. !$#cross-references MUID:89359139; PMID:2549009 !$#accession B33962 !'##molecule_type DNA !'##residues 1-52 ##label BRUM !'##cross-references GB:M28848; NID:g342028; PIDN:AAA64798.1; !1PID:g758677 REFERENCE A00274 !$#authors Bruschi, M. !$#journal Biochim. Biophys. Acta (1976) 434:4-17 !$#title Non-heme iron proteins. The amino acid sequence of !1rubredoxin from Desulfovibrio vulgaris. !$#cross-references MUID:76232334; PMID:7308 !$#accession A00274 !'##molecule_type protein !'##residues 1-20,'T',22-52 ##label BRUS !'##experimental_source strain Hildenborough REFERENCE A50939 !$#authors Adman, E.T.; Sieker, L.C.; Jensen, L.H. !$#submission submitted to the Brookhaven Protein Data Bank, May 1990 !$#cross-references PDB:7RXN !$#contents annotation; X-ray crystallography, 1.5 angstroms, residues !11-52 REFERENCE A22814 !$#authors Adman, E.T.; Seiker, L.C.; Jensen, L.H. !$#journal J. Mol. Biol. (1991) 217:337-352 !$#title Structure of rubredoxin from Desulfovibrio vulgaris at 1.5 A !1resolution. !$#cross-references MUID:91124457; PMID:1992166 !$#contents annotation; X-ray crystallography, 1.5 angstroms REFERENCE A51562 !$#authors Dauter, Z.; Sieker, L.; Wilson, K. !$#submission submitted to the Brookhaven Protein Data Bank, August 1991 !$#cross-references PDB:8RXN !$#contents annotation; X-ray crystallography, 1.0 angstroms, residues !11-52 GENETICS !$#gene rub CLASSIFICATION #superfamily rubredoxin; rubredoxin homology KEYWORDS electron transfer; iron; metalloprotein FEATURE !$3-49 #domain rubredoxin homology #label RUB\ !$6,9,39,42 #binding_site iron (Cys) #status experimental SUMMARY #length 52 #molecular-weight 5574 #checksum 1926 SEQUENCE /// ENTRY JX0241 #type complete TITLE rubredoxin - Desulfovibrio vulgaris (strain Miyazaki) ORGANISM #formal_name Desulfovibrio vulgaris DATE 10-Jun-1993 #sequence_revision 22-Jul-1994 #text_change 24-Oct-1997 ACCESSIONS JX0241 REFERENCE JX0241 !$#authors Shimizu, F.; Ogata, M.; Yagi, T.; Wakabayashi, S.; !1Matsubara, H. !$#journal Biochimie (1989) 71:1171-1177 !$#title Amino acid sequence and function of rubredoxin from !1Desulfovibrio vulgaris Miyazaki. !$#cross-references MUID:90234754; PMID:2561345 !$#accession JX0241 !'##molecule_type protein !'##residues 1-52 ##label SHI CLASSIFICATION #superfamily rubredoxin; rubredoxin homology KEYWORDS electron transfer; iron; metalloprotein FEATURE !$3-49 #domain rubredoxin homology #label RUB\ !$1 #modified_site N-formylmethionine (partial) #status !8experimental\ !$6,9,39,42 #binding_site iron (Cys) #status predicted SUMMARY #length 52 #molecular-weight 5598 #checksum 1997 SEQUENCE /// ENTRY RUDVEG #type complete TITLE rubredoxin [validated] - Desulfovibrio gigas ORGANISM #formal_name Desulfovibrio gigas DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 15-Sep-2000 ACCESSIONS A00275 REFERENCE A00275 !$#authors Bruschi, M. !$#journal Biochem. Biophys. Res. Commun. (1976) 70:615-621 !$#title The amino acid sequence of rubredoxin from the sulfate !1reducing bacterium, Desulfovibrio gigas. !$#cross-references MUID:76231572; PMID:938515 !$#accession A00275 !'##molecule_type protein !'##residues 1-52 ##label BRU REFERENCE A50332 !$#authors Frey, M.; Sieker, L.C.; Payan, F. !$#submission submitted to the Brookhaven Protein Data Bank, March 1988 !$#cross-references PDB:1RDG !$#contents annotation; X-ray crystallography, 1.4 angstroms, residues !11-52 REFERENCE A44624 !$#authors Frey, M.; Sieker, L.; Payan, F.; Haser, R.; Bruschi, M.; !1Pepe, G.; LeGall, J. !$#journal J. Mol. Biol. (1987) 197:525-541 !$#title Rubredoxin from Desulfovibrio gigas. A molecular model of !1the oxidized form at 1.4 angstroms resolution. !$#cross-references MUID:88155649; PMID:3441010 !$#contents annotation; X-ray crystallography, 1.4 angstroms CLASSIFICATION #superfamily rubredoxin; rubredoxin homology KEYWORDS blocked amino end; electron transfer; iron; metalloprotein FEATURE !$3-49 #domain rubredoxin homology #label RUB\ !$1 #modified_site N-formylmethionine #status !8experimental\ !$6,9,39,42 #binding_site iron (Cys) #status experimental SUMMARY #length 52 #molecular-weight 5677 #checksum 1492 SEQUENCE /// ENTRY RUDVD #type complete TITLE rubredoxin [validated] - Desulfovibrio desulfuricans ORGANISM #formal_name Desulfovibrio desulfuricans DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 15-Sep-2000 ACCESSIONS A00276 REFERENCE A00276 !$#authors Hormel, S.; Walsh, K.A.; Prickril, B.C.; Titani, K.; LeGall, !1J.; Sieker, L.C. !$#journal FEBS Lett. (1986) 201:147-150 !$#title Amino acid sequence of rubredoxin from Desulfovibrio !1desulfuricans strain 27774. !$#cross-references MUID:86220785; PMID:3709804 !$#accession A00276 !'##molecule_type protein !'##residues 1-45 ##label HOR REFERENCE A50770 !$#authors Stenkamp, R.E.; Sieker, L.C.; Jensen, L.H. !$#submission submitted to the Brookhaven Protein Data Bank, January 1990 !$#cross-references PDB:6RXN !$#contents annotation; X-ray crystallography, 1.5 angstroms REFERENCE A44623 !$#authors Sieker, L.C.; Stenkamp, R.E.; Jensen, L.H.; Prickril, B.; !1LeGall, J. !$#journal FEBS Lett. (1986) 208:73-76 !$#title Structure of rubredoxin from the bacterium Desulfovibrio !1desulfuricans. !$#cross-references MUID:87030959; PMID:3770211 !$#contents annotation; X-ray crystallography, 1.5 angstroms COMMENT Rubredoxin, found mostly in anaerobic bacteria, is a small, !1nonheme, iron protein lacking acid-labile sulfide. CLASSIFICATION #superfamily rubredoxin; rubredoxin homology KEYWORDS blocked amino end; electron transfer; iron; metalloprotein FEATURE !$3-42 #domain rubredoxin homology #label RUB\ !$1 #modified_site N-formylmethionine #status !8experimental\ !$6,9,32,35 #binding_site iron (Cys) #status experimental SUMMARY #length 45 #molecular-weight 5115 #checksum 8073 SEQUENCE /// ENTRY RUME #type complete TITLE rubredoxin - Megasphaera elsdenii ORGANISM #formal_name Megasphaera elsdenii DATE 13-Jul-1981 #sequence_revision 13-Jul-1981 #text_change 24-Oct-1997 ACCESSIONS A00277 REFERENCE A00277 !$#authors Bachmayer, H.; Yasunobu, K.T.; Peel, J.L.; Mayhew, S. !$#journal J. Biol. Chem. (1968) 243:1022-1030 !$#title Non-heme iron proteins. V. The amino acid sequence of !1rubredoxin from Peptostreptococcus elsdenii. !$#cross-references MUID:68161650; PMID:5640967 !$#accession A00277 !'##molecule_type protein !'##residues 1-52 ##label BAC CLASSIFICATION #superfamily rubredoxin; rubredoxin homology KEYWORDS electron transfer; iron; metalloprotein FEATURE !$3-48 #domain rubredoxin homology #label RUB\ !$6,9,38,41 #binding_site iron (Cys) #status predicted SUMMARY #length 52 #molecular-weight 5616 #checksum 696 SEQUENCE /// ENTRY RUPF #type complete TITLE rubredoxin [validated] - Pyrococcus furiosus ORGANISM #formal_name Pyrococcus furiosus DATE 30-Jun-1992 #sequence_revision 20-Apr-2000 #text_change 21-Jul-2000 ACCESSIONS T44570; A41189 REFERENCE Z22794 !$#authors Jenney Jr., F.E.; Verhagen, M.F.; Cui, X.; Adams, M.W. !$#journal Science (1999) 286:306-309 !$#title Anaerobic microbes: oxygen detoxification without superoxide !1dismutase. !$#cross-references MUID:99445924; PMID:10514376 !$#accession T44570 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-54 ##label JEN !'##cross-references EMBL:AF156097; NID:g6066235; PIDN:AAF03228.1; !1PID:g6066243 REFERENCE A41189 !$#authors Blake, P.R.; Park, J.B.; Bryant, F.O.; Aono, S.; Magnuson, !1J.K.; Eccleston, E.; Howard, J.B.; Summers, M.F.; Adams, !1M.W.W. !$#journal Biochemistry (1991) 30:10885-10895 !$#title Determinants of protein hyperthermostability: purification !1and amino acid sequence of rubredoxin from the !1hyperthermophilic archaebacterium Pyrococcus furiosus and !1secondary structure of the zinc adduct by NMR. !$#cross-references MUID:92031546; PMID:1932012 !$#accession A41189 !'##molecule_type protein !'##residues 2-54 ##label BLA REFERENCE A51069 !$#authors Day, M.W.; Hsu, B.T.; Joshua-tor, L.; Park, J.B.; Zhou, !1Z.H.; Adams, M.W.W.; Rees, D.C. !$#submission submitted to the Brookhaven Protein Data Bank, May 1992 !$#cross-references PDB:1CAA !$#contents annotation; X-ray crystallography, 1.8 angstroms, oxidized !1form, residues 1-53 REFERENCE A51070 !$#authors Day, M.W.; Hsu, B.T.; Joshua-tor, L.; Park, J.B.; Zhou, !1Z.H.; Adams, M.W.W.; Rees, D.C. !$#submission submitted to the Brookhaven Protein Data Bank, May 1992 !$#cross-references PDB:1CAD !$#contents annotation; X-ray crystallography, 1.8 angstroms, reduced !1form, residues 1-53 REFERENCE A44625 !$#authors Day, M.W.; Hsu, B.T.; Joshua-tor, L.; Park, J.B.; Zhou, !1Z.H.; Adams, M.W.W.; Rees, D.C. !$#journal Protein Sci. (1992) 1:1494-1507 !$#title X-ray crystal structures of the oxidized and reduced forms !1of the rubredoxin from the marine hyperthermophilic !1archaebacterium Pyrococcus furiosus. !$#cross-references MUID:93271899; PMID:1303768 !$#contents annotation; X-ray crystallography, 1.8 angstroms REFERENCE A51443 !$#authors Blake, P.R.; Park, J.B.; Zhou, Z.H.; Hare, D.R.; Adams, !1M.W.W.; Summers, M.F. !$#submission submitted to the Brookhaven Protein Data Bank, July 1992 !$#cross-references PDB:1ZRP !$#contents annotation; conformation by (1)H-NMR, residues 1-53 REFERENCE A58634 !$#authors Blake, P.R.; Park, J.B.; Zhou, Z.H.; Hare, D.R.; Adams, !1M.W.W.; Summers, M.F. !$#journal Protein Sci. (1992) 1:1508-1521 !$#title Solution-state structure by NMR of zinc-substituted !1rubredoxin from the marine hyperthermophilic archaebacterium !1Pyrococcus furiosus. !$#cross-references MUID:93271900; PMID:1303769 !$#contents annotation; conformation by (1)H-NMR CLASSIFICATION #superfamily rubredoxin; rubredoxin homology KEYWORDS electron transfer; iron; metalloprotein FEATURE !$2-54 #product rubredoxin #status experimental #label MAT\ !$3-49 #domain rubredoxin homology #label RUB\ !$6,9,39,42 #binding_site iron (Cys) #status experimental SUMMARY #length 54 #molecular-weight 6027 #checksum 9296 SEQUENCE /// ENTRY RUPSO1 #type complete TITLE rubredoxin I - Pseudomonas oleovorans plasmid OCT ORGANISM #formal_name Pseudomonas oleovorans DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 11-Jun-1999 ACCESSIONS A32850; S27991; B31266 REFERENCE A32850 !$#authors Kok, M.; Oldenhuis, R.; van der Linden, M.P.G.; Meulenberg, !1C.H.C.; Kingma, J.; Witholt, B. !$#journal J. Biol. Chem. (1989) 264:5442-5451 !$#title The Pseudomonas oleovorans alkBAC operon encodes two !1structurally related rubredoxins and an aldehyde !1dehydrogenase. !$#cross-references MUID:89174582; PMID:2647719 !$#accession A32850 !'##molecule_type DNA !'##residues 1-132 ##label KOK !'##cross-references GB:X65936; GB:J04618; NID:g49078; PIDN:CAA46734.1; !1PID:g49080; GB:J04619 REFERENCE S27990 !$#authors van Beilen, J.B.; Eggink, G.; Enequist, H.; Bos, R.; !1Witholt, B. !$#journal Mol. Microbiol. (1992) 6:3121-3136 !$#title DNA sequence determination and functional characterization !1of the OCT-plasmid-encoded alkJKL genes of Pseudomonas !1oleovorans. !$#cross-references MUID:93086421; PMID:1453953 !$#accession S27991 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-132 ##label BEI !'##cross-references EMBL:X65936; NID:g49078; PIDN:CAA46734.1; !1PID:g49080 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1992 GENETICS !$#gene alkF !$#genome plasmid OCT CLASSIFICATION #superfamily Pseudomonas rubredoxin I; rubredoxin homology KEYWORDS electron transfer; hydrocarbon hydroxylation; iron; !1metalloprotein FEATURE !$3-48 #domain rubredoxin homology #label RUB\ !$6,9,39,42 #binding_site iron (Cys) #status predicted SUMMARY #length 132 #molecular-weight 14619 #checksum 9881 SEQUENCE /// ENTRY RUPSEO #type complete TITLE rubredoxin II - Pseudomonas oleovorans plasmid OCT ORGANISM #formal_name Pseudomonas oleovorans DATE 24-Apr-1984 #sequence_revision 30-Sep-1993 #text_change 21-Jul-2000 ACCESSIONS B32850; A00278; S27992; C31266 REFERENCE A32850 !$#authors Kok, M.; Oldenhuis, R.; van der Linden, M.P.G.; Meulenberg, !1C.H.C.; Kingma, J.; Witholt, B. !$#journal J. Biol. Chem. (1989) 264:5442-5451 !$#title The Pseudomonas oleovorans alkBAC operon encodes two !1structurally related rubredoxins and an aldehyde !1dehydrogenase. !$#cross-references MUID:89174582; PMID:2647719 !$#accession B32850 !'##molecule_type DNA !'##residues 1-173 ##label KOK !'##cross-references GB:J04618; GB:J04619 REFERENCE A00278 !$#authors Benson, A.; Tomoda, K.; Chang, J.; Matsueda, G.; Lode, E.T.; !1Coon, M.J.; Yasunobu, K.T. !$#journal Biochem. Biophys. Res. Commun. (1971) 42:640-646 !$#title Evolutionary and phylogenetic relationships of !1rubredoxin-containing microbes. !$#cross-references MUID:71113196; PMID:5543946 !$#accession A00278 !'##molecule_type protein !'##residues 2-37,'D',39-40,'C',42-106,'E',108-113,'E',115-132,'W', !1133-153,155,'D',156-157,'WCBP',161-165,'N',167-173 ##label !1BEN REFERENCE S27990 !$#authors van Beilen, J.B.; Eggink, G.; Enequist, H.; Bos, R.; !1Witholt, B. !$#journal Mol. Microbiol. (1992) 6:3121-3136 !$#title DNA sequence determination and functional characterization !1of the OCT-plasmid-encoded alkJKL genes of Pseudomonas !1oleovorans. !$#cross-references MUID:93086421; PMID:1453953 !$#accession S27992 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 'MVMS',1-173 ##label BEI !'##cross-references EMBL:X65936; NID:g49078; PIDN:CAA46735.1; !1PID:g49081 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1992 GENETICS !$#gene alkG !$#genome plasmid OCT CLASSIFICATION #superfamily Pseudomonas rubredoxin II; rubredoxin homology KEYWORDS duplication; electron transfer; hydrocarbon hydroxylation; !1iron; metalloprotein FEATURE !$2-173 #product rubredoxin II #status experimental #label !8MAT\ !$3-48 #domain rubredoxin homology #label RUB1\ !$56-119 #domain middle #label MID\ !$121-167 #domain rubredoxin homology #label RUB2\ !$6,9,39,42 #binding_site iron (Cys) #status predicted\ !$124,127,157,160 #binding_site iron (Cys) #status predicted SUMMARY #length 173 #molecular-weight 18899 #checksum 4577 SEQUENCE /// ENTRY S25690 #type complete TITLE hupJ protein - Rhodobacter capsulatus ORGANISM #formal_name Rhodobacter capsulatus DATE 04-Dec-1992 #sequence_revision 13-Mar-1997 #text_change 03-Mar-2000 ACCESSIONS S32946; S25690; A38532 REFERENCE S32941 !$#authors Colbeau, A.; Richaud, P.; Toussaint, B.; Caballero, F.J.; !1Elster, C.; Delphin, C.; Smith, R.L.; Chabert, J.; Vignais, !1P.M. !$#journal Mol. Microbiol. (1993) 8:15-29 !$#title Organization of the genes necessary for hydrogenase !1expression in Rhodobacter capsulatus. Sequence analysis and !1identification of two hyp regulatory mutants. !$#cross-references MUID:93268090; PMID:8497190 !$#accession S32946 !'##status preliminary !'##molecule_type DNA !'##residues 1-278 ##label COL !'##cross-references EMBL:Z15089; NID:g313868; PIDN:CAA78802.1; !1PID:g581495 !'##note the authors translated the initiation codon TTG for residue 1 !1as Leu !'##note the authors translated the codon ATA for residue 34 as B REFERENCE S25686 !$#authors Toussaint, B. !$#submission submitted to the EMBL Data Library, September 1992 !$#accession S25690 !'##molecule_type DNA !'##residues 26-278 ##label TOU !'##cross-references EMBL:Z15089 REFERENCE A38532 !$#authors Xu, H.W.; Wall, J.D. !$#journal J. Bacteriol. (1991) 173:2401-2405 !$#title Clustering of genes necessary for hydrogen oxidation in !1Rhodobacter capsulatus. !$#cross-references MUID:91177833; PMID:2007559 !$#accession A38532 !'##molecule_type DNA !'##residues 172-250,'PGPRRWRNRRGGG' ##label XUA !'##cross-references GB:M55089; NID:g151949; PIDN:AAA72923.1; !1PID:g151950 GENETICS !$#gene hupJ !$#start_codon TTG !$#note part of an operon containing 18 genes involved in !1hydrogenase activity and expression CLASSIFICATION #superfamily Rhodobacter hupJ protein; rubredoxin homology KEYWORDS electron transfer; iron; metalloprotein FEATURE !$25-71 #domain rubredoxin homology #label RUB\ !$28,31,61,64 #binding_site iron (Cys) #status predicted SUMMARY #length 278 #molecular-weight 30329 #checksum 560 SEQUENCE /// ENTRY SDDVEG #type complete TITLE desulforedoxin - Desulfovibrio gigas ORGANISM #formal_name Desulfovibrio gigas DATE 31-Oct-1979 #sequence_revision 31-Mar-1993 #text_change 03-Mar-2000 ACCESSIONS A37857; A00279 REFERENCE A37857 !$#authors Brumlik, M.J.; Leroy, G.; Bruschi, M.; Voordouw, G. !$#journal J. Bacteriol. (1990) 172:7289-7292 !$#title The nucleotide sequence of the Desulfovibrio gigas !1desulforedoxin gene indicates that the Desulfovibrio !1vulgaris rbo gene originated from a gene fusion event. !$#cross-references MUID:91072291; PMID:2254288 !$#accession A37857 !'##molecule_type DNA !'##residues 1-37 ##label BRU !'##cross-references GB:M62784; NID:g145084; PIDN:AAA23365.1; !1PID:g145085 REFERENCE A00279 !$#authors Bruschi, M.; Moura, I.; Le Gall, J.; Xavier, A.V.; Sieker, !1L.C. !$#journal Biochem. Biophys. Res. Commun. (1979) 90:596-605 !$#title The amino acid sequence of desulforedoxin, a new type of non !1heme iron protein from Desulfovibrio gigas. !$#cross-references MUID:80064861; PMID:508323 !$#accession A00279 !'##molecule_type protein !'##residues 2-37 ##label BR2 COMMENT Desulforedoxin, a nonheme iron protein, is a dimer with two !1iron atoms linked to eight cysteine residues. GENETICS !$#gene dsr CLASSIFICATION #superfamily desulforedoxin; desulforedoxin homology KEYWORDS electron transfer; homodimer; iron; metalloprotein FEATURE !$1-36 #domain desulforedoxin homology #label DSX\ !$2-37 #product desulforedoxin #status experimental #label !8MAT\ !$10,13,29,30 #binding_site iron (Cys) #status predicted SUMMARY #length 37 #molecular-weight 3936 #checksum 2886 SEQUENCE /// ENTRY S29861 #type complete TITLE hybrid cluster [4Fe-2S-3O] protein [validated] - Desulfovibrio vulgaris ALTERNATE_NAMES prismane [6Fe-6S] protein [misnomer] ORGANISM #formal_name Desulfovibrio vulgaris DATE 10-Sep-1999 #sequence_revision 28-Jul-2000 #text_change 28-Jul-2000 ACCESSIONS S29861 REFERENCE S29861 !$#authors Stokkermans, J.P.W.G.; Pierik, A.J.; Wolbert, R.B.G.; Hagen, !1W.R.; van Dongen, W.M.A.M.; Veeger, C. !$#journal Eur. J. Biochem. (1992) 208:435-442 !$#title The primary structure of a protein containing a putative !1[6Fe-6S] prismane cluster from Desulfovibrio vulgaris !1(Hildenborough). !$#cross-references MUID:92394141; PMID:1339351 !$#accession S29861 !'##molecule_type DNA !'##residues 1-201,'GRR',205-553 ##label STO !'##cross-references EMBL:Z11707; NID:g40832; PID:g40833 !'##note this sequence has been corrected in reference A58942 REFERENCE A57798 !$#authors Pierik, A.J.; Hagen, W.R.; Dunham, W.R.; Sands, R.H. !$#journal Eur. J. Biochem. (1992) 206:705-719 !$#title Multi-frequency EPR and high-resolution Moessbauer !1spectroscopy of a putative [6Fe-6S] !1prismane-cluster-containing protein from Desulfovibrio !1vulgaris (Hildenborough). !$#cross-references MUID:92298998; PMID:1318833 !$#contents annotation; evidence for a 6Fe-6S cluster REFERENCE A58942 !$#authors Arendsen, A.F.; Hadden, J.; Card, G.; McAlpine, A.S.; !1Bailey, S.; Zaitsev, V.; Duke, E.H.M.; Lindley, P.F.; !1Kroeckel, M.; Trautwein, A.X.; Feiters, M.C.; Charnock, !1J.M.; Garner, C.D.; Marritt, S.J.; Thomson, A.J.; Kooter, !1I.M.; Johnson, M.K.; van den Berg, W.A.M.; van Dongen, !1W.M.A.M.; Hagen, W.R. !$#journal J. Biol. Inorg. Chem. (1998) 3:81-95 !$#title The "prismane" protein resolved: X-ray structure at 1.7 !1angstroms and multiple spectroscopy of two novel 4Fe !1clusters. !$#contents annotation; sequence correction; X-ray crystallography, 1.7 !1angstroms; EPR, Moessbauer, and MCD spectrographic analysis !$#note because of model inconsistencies with sequence, the authors !1redetermined the nucleotide sequence and found residues !1202-204 should be Ala-Gly-Gly COMMENT The name "prismane" for this protein is a now known to be a !1misnomer. The structure for the metal clusters determined by !1X-ray consists of one four iron/four sulfur cluster and one !1four iron cluster with mixed ligands. For a description of !1the 4Fe-2S-3O cluster, see RESID:AA0268. CLASSIFICATION #superfamily Desulfovibrio hybrid cluster [4Fe-2S-3O] !1protein; hybrid cluster [4Fe-2S-3O] homology KEYWORDS 4Fe-2S-3O; 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$221-516 #domain hybrid cluster [4Fe-2S-3O] homology #label !8HCL\ !$3,6,15,21 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8experimental\ !$244,268,312,406, !$434,459,494 #binding_site 4Fe-2S-3O cluster (His, Glu, Cys, Cys, !8Cys, Cys, Glu) (covalent) #status experimental\ !$406 #modified_site cysteine persulfide (Cys) #status !8experimental SUMMARY #length 553 #molecular-weight 59978 #checksum 4293 SEQUENCE /// ENTRY JH0568 #type complete TITLE thioredoxin [validated] - human ALTERNATE_NAMES ATL-derived factor (ADF); eosinophil cytotoxicity-enhancing factor; thioredoxin-related surface protein SASP ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1992 #sequence_revision 26-May-1994 #text_change 15-Sep-2000 ACCESSIONS JH0568; S04106; S44375; A31993; PT0079; A60749; A38922; !1S53453; A60870 REFERENCE JH0568 !$#authors Tonissen, K.F.; Wells, J.R.E. !$#journal Gene (1991) 102:221-228 !$#title Isolation and characterization of human thioredoxin-encoding !1genes. !$#cross-references MUID:91340156; PMID:1874447 !$#accession JH0568 !'##molecule_type DNA !'##residues 1-105 ##label TON !'##cross-references EMBL:X54539; NID:g37455; PIDN:CAA38410.1; !1PID:g825724; EMBL:X54540; EMBL:X54541 REFERENCE S04106 !$#authors Tagaya, Y.; Maeda, Y.; Mitsui, A.; Kondo, N.; Matsui, H.; !1Hamuro, J.; Brown, N.; Arai, K.I.; Yokota, T.; Wakasugi, H.; !1Yodoi, J. !$#journal EMBO J. (1989) 8:757-764 !$#title ATL-derived factor (ADF), an IL-2 receptor/Tac inducer !1homologous to thioredoxin; possible involvement of !1dithiol-reduction in the IL-2 receptor induction. !$#cross-references MUID:89251607; PMID:2785919 !$#accession S04106 !'##molecule_type mRNA !'##residues 1-105 ##label TAG1 !'##cross-references GB:X77584; NID:g453963; PIDN:CAA54687.1; !1PID:g453964 !'##note this sequence has been revised in reference S44375 REFERENCE S44375 !$#authors Tagaya, Y.; Maeda, Y.; Mitsui, A.; Kando, N.; Matsui, H.; !1Hamuro, J.; Brown, N.; Arai, K.; Tokota, T.; Wakasugi, H.; !1Yodoi, J. !$#journal EMBO J. (1994) 13:2244 !$#cross-references MUID:94244626; PMID:8187776 !$#contents erratum !$#accession S44375 !'##molecule_type mRNA !'##residues 1-105 ##label TAG2 !'##cross-references EMBL:X77584; NID:g453963; PIDN:CAA54687.1; !1PID:g453964 REFERENCE A31993 !$#authors Wollman, E.E.; d'Auriol, L.; Rimsky, L.; Shaw, A.; Jacquot, !1J.P.; Wingfield, P.; Graber, P.; Dessarps, F.; Robin, P.; !1Galibert, F.; Bertoglio, J.; Fradelizi, D. !$#journal J. Biol. Chem. (1988) 263:15506-15512 !$#title Cloning and expression of a cDNA for human thioredoxin. !$#cross-references MUID:89008454; PMID:3170595 !$#accession A31993 !'##molecule_type mRNA !'##residues 1-38,'N',40-73,'T',75-105 ##label WOL !'##cross-references GB:J04026; NID:g339648; PIDN:AAA74596.1; !1PID:g339649 REFERENCE PT0079 !$#authors Martin, H.; Dean, M. !$#journal Biochem. Biophys. Res. Commun. (1991) 175:123-128 !$#title Identification of a thioredoxin-related protein associated !1with plasma membranes. !$#cross-references MUID:91151337; PMID:1998498 !$#accession PT0079 !'##molecule_type protein !'##residues 2-13,'X',15 ##label MAR REFERENCE A60749 !$#authors Silberstein, D.S.; Ali, M.H.; Baker, S.L.; David, J.R. !$#journal J. Immunol. (1989) 143:979-983 !$#title Human eosinophil cytotoxicity-enhancing factor. !1Purification, physical characteristics, and partial amino !1acid sequence of an active polypeptide. !$#cross-references MUID:89309777; PMID:2745979 !$#accession A60749 !'##molecule_type protein !'##residues 2-12,'K',14-15,'XX',18-19,'X',21-22 ##label SIL !'##note the abstract is inconsistent with figure 4 in having one !1undetermined residue after 15-Leu rather than two REFERENCE A38922 !$#authors Rimsky, L.; Wakasugi, H.; Ferrara, P.; Robin, P.; !1Capdevielle, J.; Tursz, T.; Fradelizi, D.; Bertoglio, J. !$#journal J. Immunol. (1986) 136:3304-3310 !$#title Purification to homogeneity and NH-2-terminal amino acid !1sequence of a novel interleukin 1 species derived from a !1human B cell line. !$#cross-references MUID:86169684; PMID:3485686 !$#accession A38922 !'##molecule_type protein !'##residues 2-16 ##label WAK REFERENCE S53453 !$#authors Dean, M.F.; Martin, H.; Sansom, P.A. !$#journal Biochem. J. (1994) 304:861-867 !$#title Characterization of a thioredoxin-related surface protein. !$#cross-references MUID:95118305; PMID:7818492 !$#accession S53453 !'##molecule_type protein !'##residues 1-21;38-57 ##label DEA !'##note described to be a surface-associated thioredoxin REFERENCE A60870 !$#authors Wakasugi, H.; Rimsky, L.; Mahe, Y.; Kamel, A.M.; Fradelizi, !1D.; Tursz, T.; Bertoglio, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:804-808 !$#title Epstein-Barr virus-containing B-cell line produces an !1interleukin 1 that it uses as a growth factor. !$#cross-references MUID:87118252; PMID:3027706 !$#contents annotation REFERENCE A65533 !$#authors Weichsel, A.; Gasdaska, J.R.; Powis, G.; Montfort, W.R. !$#submission submitted to the Brookhaven Protein Data Bank, February 1996 !$#cross-references PDB:1ERT !$#contents annotation; X-ray crystallography, 1.7 angstroms, reduced !1form, residues 1-105 REFERENCE A65534 !$#authors Weichsel, A.; Gasdaska, J.R.; Powis, G.; Montfort, W.R. !$#submission submitted to the Brookhaven Protein Data Bank, February 1996 !$#cross-references PDB:1ERU !$#contents annotation; X-ray crystallography, 2.1 angstroms, oxidized !1form, residues 1-105 REFERENCE A50924 !$#authors Forman-Kay, J.D.; Clore, G.M.; Gronenborn, A.M. !$#submission submitted to the Brookhaven Protein Data Bank, December 1990 !$#cross-references PDB:4TRX !$#contents annotation; conformation by (1)H-NMR, residues 1-73,'T', !175-105 REFERENCE A38953 !$#authors Forman-Kay, J.D.; Clore, G.M.; Wingfield, P.T.; Gronenborn, !1A.M. !$#journal Biochemistry (1991) 30:2685-2698 !$#title High-resolution three-dimensional structure of reduced !1recombinant human thioredoxin in solution. !$#cross-references MUID:91159399; PMID:2001356 !$#contents annotation; conformation by (1)H- and (15)N-NMR COMMENT This small ubiquitous protein functions in many !1intracellular biological pathways. GENETICS !$#gene GDB:TXN !'##cross-references GDB:120475; OMIM:187700 !$#map_position 9q31-9q31 !$#introns 8/3; 43/3; 63/3; 85/3 CLASSIFICATION #superfamily thioredoxin; thioredoxin homology KEYWORDS redox-active disulfide FEATURE !$2-105 #product thioredoxin #status experimental #label MAT\ !$9-92 #domain thioredoxin homology #label THR\ !$32-35 #disulfide_bonds redox-active #status experimental SUMMARY #length 105 #molecular-weight 11737 #checksum 3392 SEQUENCE /// ENTRY JS0667 #type complete TITLE thioredoxin - rhesus macaque ORGANISM #formal_name Macaca mulatta #common_name rhesus macaque DATE 30-Jun-1992 #sequence_revision 26-May-1994 #text_change 11-Jun-1999 ACCESSIONS JS0667 REFERENCE JS0667 !$#authors An, G.; Wu, R. !$#journal Biochem. Biophys. Res. Commun. (1992) 183:170-175 !$#title Thioredoxin gene expression is transcriptionally !1up-regulated by retinol in monkey conducting airway !1epithelial cells. !$#cross-references MUID:92181438; PMID:1543487 !$#accession JS0667 !'##molecule_type mRNA !'##residues 1-105 ##label ANG !'##cross-references GB:M84643; NID:g342338; PIDN:AAA36921.1; !1PID:g342339 CLASSIFICATION #superfamily thioredoxin; thioredoxin homology KEYWORDS redox-active disulfide FEATURE !$9-92 #domain thioredoxin homology #label THR\ !$32-35 #disulfide_bonds redox-active #status predicted SUMMARY #length 105 #molecular-weight 11737 #checksum 3961 SEQUENCE /// ENTRY A28086 #type complete TITLE thioredoxin - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 30-Jun-1989 #sequence_revision 26-May-1994 #text_change 19-Oct-1995 ACCESSIONS A28086 REFERENCE A28086 !$#authors Johnson, R.S.; Mathews, W.R.; Biemann, K.; Hopper, S. !$#journal J. Biol. Chem. (1988) 263:9589-9597 !$#title Amino acid sequence of thioredoxin isolated from rabbit bone !1marrow determined by tandem mass spectrometry. !$#cross-references MUID:88257078; PMID:3164311 !$#accession A28086 !'##molecule_type protein !'##residues 1-104 ##label JOH CLASSIFICATION #superfamily thioredoxin; thioredoxin homology KEYWORDS redox-active disulfide FEATURE !$8-91 #domain thioredoxin homology #label THR\ !$31-34 #disulfide_bonds redox-active #status predicted SUMMARY #length 104 #molecular-weight 11629 #checksum 7776 SEQUENCE /// ENTRY S04352 #type complete TITLE thioredoxin - rat ALTERNATE_NAMES thioredoxin-related surface protein SASP ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1990 #sequence_revision 26-May-1994 #text_change 11-Jun-1999 ACCESSIONS S04352; S66372 REFERENCE S04352 !$#authors Tonissen, K.F.; Robins, A.J.; Wells, J.R.E. !$#journal Nucleic Acids Res. (1989) 17:3973 !$#title Nucleotide sequence of a cDNA encoding rat thioredoxin. !$#cross-references MUID:89282399; PMID:2734107 !$#accession S04352 !'##molecule_type mRNA !'##residues 1-105 ##label TON !'##cross-references EMBL:X14878; NID:g57385; PIDN:CAA33019.1; !1PID:g57386 REFERENCE S53453 !$#authors Dean, M.F.; Martin, H.; Sansom, P.A. !$#journal Biochem. J. (1994) 304:861-867 !$#title Characterization of a thioredoxin-related surface protein. !$#cross-references MUID:95118305; PMID:7818492 !$#accession S66372 !'##molecule_type protein !'##residues 2-21 ##label DEA !'##note 12-Lys, 15-Gly, 16-Leu, 17-Gln, and 18-Leu were also found !'##note described to be a surface-associated thioredoxin CLASSIFICATION #superfamily thioredoxin; thioredoxin homology KEYWORDS redox-active disulfide FEATURE !$2-105 #product thioredoxin #status experimental #label MAT\ !$9-92 #domain thioredoxin homology #label THR\ !$32-35 #disulfide_bonds redox-active #status predicted SUMMARY #length 105 #molecular-weight 11673 #checksum 2321 SEQUENCE /// ENTRY S04107 #type complete TITLE thioredoxin - mouse ALTERNATE_NAMES ATL-derived factor (ADF) ORGANISM #formal_name Mus musculus #common_name house mouse DATE 21-Nov-1993 #sequence_revision 17-Oct-1997 #text_change 11-Jun-1999 ACCESSIONS JC4068; S44376; S04107 REFERENCE JC4068 !$#authors Matsui, M.; Taniguchi, Y.; Hirota, K.; Taketo, M.; Yodoi, J. !$#journal Gene (1995) 152:165-171 !$#title Structure of the mouse thioredoxin-encoding gene and its !1processed pseudogene. !$#cross-references MUID:95137382; PMID:7835695 !$#accession JC4068 !'##molecule_type DNA !'##residues 1-105 ##label MAT !'##cross-references DDBJ:D21855; NID:g517128 REFERENCE S44375 !$#authors Tagaya, Y.; Maeda, Y.; Mitsui, A.; Kando, N.; Matsui, H.; !1Hamuro, J.; Brown, N.; Arai, K.; Tokota, T.; Wakasugi, H.; !1Yodoi, J. !$#journal EMBO J. (1994) 13:2244 !$#cross-references MUID:94244626; PMID:8187776 !$#contents erratum !$#accession S44376 !'##molecule_type mRNA !'##residues 1-105 ##label TAG1 !'##cross-references EMBL:X77585; NID:g453971; PIDN:CAA54688.1; !1PID:g453972 REFERENCE S04106 !$#authors Tagaya, Y.; Maeda, Y.; Mitsui, A.; Kondo, N.; Matsui, H.; !1Hamuro, J.; Brown, N.; Arai, K.I.; Yokota, T.; Wakasugi, H.; !1Yodoi, J. !$#journal EMBO J. (1989) 8:757-764 !$#title ATL-derived factor (ADF), an IL-2 receptor/Tac inducer !1homologous to thioredoxin; possible involvement of !1dithiol-reduction in the IL-2 receptor induction. !$#cross-references MUID:89251607; PMID:2785919 !$#accession S04107 !'##molecule_type mRNA !'##residues 1-93,'N',94-96,'ALT',100-104,'S' ##label TAG2 !'##cross-references GB:X77585 COMMENT This small ubiquitous protein functions in many !1intracellular biological pathways. GENETICS !$#gene MGI:Txn !'##cross-references MGI:36258 !$#map_position 4:24.6 !$#introns 29/2; 44/1; 84/2 CLASSIFICATION #superfamily thioredoxin; thioredoxin homology KEYWORDS redox-active disulfide FEATURE !$9-92 #domain thioredoxin homology #label THR\ !$32-35 #disulfide_bonds redox-active #status predicted SUMMARY #length 105 #molecular-weight 11675 #checksum 3171 SEQUENCE /// ENTRY A30006 #type complete TITLE thioredoxin - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 31-Mar-1989 #sequence_revision 26-May-1994 #text_change 11-Jun-1999 ACCESSIONS A30006 REFERENCE A30006 !$#authors Jones, S.W.; Luk, K.C. !$#journal J. Biol. Chem. (1988) 263:9607-9611 !$#title Isolation of a chicken thioredoxin cDNA clone: thioredoxin !1mRNA is differentially expressed in normal and Rous sarcoma !1virus-transformed chicken embryo fibroblasts. !$#cross-references MUID:88257080; PMID:2838473 !$#accession A30006 !'##molecule_type mRNA !'##residues 1-105 ##label JON !'##cross-references GB:J03882; NID:g212765; PIDN:AAA49092.1; !1PID:g212766 CLASSIFICATION #superfamily thioredoxin; thioredoxin homology KEYWORDS redox-active disulfide FEATURE !$9-92 #domain thioredoxin homology #label THR\ !$32-35 #disulfide_bonds redox-active #status predicted SUMMARY #length 105 #molecular-weight 11700 #checksum 1607 SEQUENCE /// ENTRY S34812 #type complete TITLE thioredoxin h2 - common tobacco ORGANISM #formal_name Nicotiana tabacum #common_name common tobacco DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS S34812 REFERENCE S34812 !$#authors Brugidou, C.; Marty, I.; Chartier, Y.; Meyer, Y. !$#journal Mol. Gen. Genet. (1993) 238:285-293 !$#title The Nicotiana tabacum genome encodes two cytoplasmic !1thioredoxin genes which are differently expressed. !$#cross-references MUID:93241165; PMID:8479434 !$#accession S34812 !'##molecule_type DNA !'##residues 1-118 ##label BRU !'##cross-references EMBL:Z11803; NID:g297518; PIDN:CAA77847.1; !1PID:g297519 GENETICS !$#introns 29/3; 70/3 CLASSIFICATION #superfamily thioredoxin; thioredoxin homology FEATURE !$17-99 #domain thioredoxin homology #label THR SUMMARY #length 118 #molecular-weight 13047 #checksum 8849 SEQUENCE /// ENTRY S16590 #type complete TITLE thioredoxin h1 - common tobacco ORGANISM #formal_name Nicotiana tabacum #common_name common tobacco DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS S16590 REFERENCE S16590 !$#authors Marty, I.; Meyer, Y. !$#journal Plant Mol. Biol. (1991) 17:143-147 !$#title Nucleotide sequence of a cDNA encoding a tobacco !1thioredoxin. !$#cross-references MUID:91329721; PMID:1868216 !$#accession S16590 !'##molecule_type mRNA !'##residues 1-126 ##label MAR !'##cross-references EMBL:X58527; NID:g20046; PIDN:CAA41415.1; !1PID:g20047 !'##note the authors translated the codon CCA for residue 54 as Arg CLASSIFICATION #superfamily thioredoxin; thioredoxin homology FEATURE !$24-106 #domain thioredoxin homology #label THR SUMMARY #length 126 #molecular-weight 13956 #checksum 6220 SEQUENCE /// ENTRY JQ2242 #type complete TITLE thioredoxin h - Arabidopsis thaliana ALTERNATE_NAMES protein F24M12.70 ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 19-May-1994 #sequence_revision 26-May-1994 #text_change 18-Feb-2000 ACCESSIONS JQ2242; T45734; S29905 REFERENCE JQ2242 !$#authors Rivera-Madrid, R.; Marinho, P.; Brugidou, C.; Chartier, Y.; !1Meyer, Y. !$#journal Plant Physiol. (1993) 102:327-328 !$#title Nucleotide sequence of a cDNA clone encoding an Arabidopsis !1thaliana thioredoxin h. !$#cross-references MUID:94151431; PMID:8108503 !$#accession JQ2242 !'##molecule_type mRNA !'##residues 1-114 ##label RIV !'##cross-references EMBL:Z14084; NID:g16551; PIDN:CAA78462.1; !1PID:g16552 REFERENCE Z23012 !$#authors Vitale, D.; Liguori, R.; Flores, M.; Argiriou, A.; De !1Simone, V.; Mewes, H.W.; Lemcke, K.; Mayer, K.F.X.; Quetier, !1F.; Salanoubat, M. !$#submission submitted to the Protein Sequence Database, December 1999 !$#accession T45734 !'##status preliminary !'##molecule_type DNA !'##residues 1-114 ##label VIT !'##cross-references EMBL:AL132980 !'##experimental_source cultivar Columbia; BAC clone F24M12 GENETICS !$#gene F24M12.70 !$#map_position 3 !$#introns 30/3; 71/3 CLASSIFICATION #superfamily thioredoxin; thioredoxin homology KEYWORDS redox-active disulfide FEATURE !$18-100 #domain thioredoxin homology #label THR\ !$40-43 #disulfide_bonds redox-active #status predicted SUMMARY #length 114 #molecular-weight 12673 #checksum 6600 SEQUENCE /// ENTRY TXBY1 #type complete TITLE thioredoxin I - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein G7746; protein YGR209c; thioredoxin 2 ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jun-2000 ACCESSIONS S15049; B39847; S05793; S53932; S61947; S64531; S63858; !1A38669 REFERENCE A38669 !$#authors Gan, Z.R. !$#journal J. Biol. Chem. (1991) 266:1692-1696 !$#title Yeast thioredoxin genes. !$#cross-references MUID:91107668; PMID:1988444 !$#accession S15049 !'##molecule_type DNA !'##residues 1-104 ##label GAN !'##cross-references GB:M59168; NID:g173025; PIDN:AAA35170.1; !1PID:g173026 REFERENCE A39847 !$#authors Muller, E.G.D. !$#journal J. Biol. Chem. (1991) 266:9194-9202 !$#title Thioredoxin deficiency in yeast prolongs S phase and !1shortens the G1 interval of the cell cycle. !$#cross-references MUID:91225027; PMID:2026619 !$#accession B39847 !'##molecule_type DNA !'##residues 1-104 ##label MUL !'##cross-references GB:M62648; NID:g173049; PIDN:AAA35178.1; !1PID:g173050 REFERENCE S05793 !$#authors Hall, D.E.; Baldesten, A.; Holmgren, A.; Reichard, P. !$#journal Eur. J. Biochem. (1971) 23:328-335 !$#title Yeast thioredoxin. Amino-acid sequence around the !1active-center disulfide of thioredoxin I and II. !$#cross-references MUID:72100583; PMID:4945270 !$#accession S05793 !'##molecule_type protein !'##residues 2;27-43;98-104 ##label HAL !'##note the sequence from the summary and from Fig. 5 is inconsistent !1with that from page 332 in having 98-Glu REFERENCE S53922 !$#authors Guerreiro, P.; Barreiros, T.; Soares, H.; Cyrne, L.; Maia e !1Silva, A.; Rodrigues-Pousada, C. !$#submission submitted to the EMBL Data Library, April 1995 !$#description Sequencing of a 17.6 kb segment on the right arm of yeast !1chromosome VII reveals 12 open reading frames, including !1CCT, ADE3 and TR-I genes, homologous to the yeast YAL023 and !1EF1G genes, of the human. !$#accession S53932 !'##molecule_type DNA !'##residues 1-104 ##label GUE !'##cross-references EMBL:Z49133; NID:g790489; PIDN:CAA89002.1; !1PID:g790500 !'##experimental_source strain S288C REFERENCE S61947 !$#authors Song, J.M.; Cheung, E.; Rabinowitz, J.C. !$#submission submitted to the EMBL Data Library, November 1995 !$#description Analysis of the 15.6-kb fragment encompassing the ADE3 gene. !$#accession S61947 !'##molecule_type DNA !'##residues 1-104 ##label SON !'##cross-references EMBL:U40843; NID:g1165213; PIDN:AAA85584.1; !1PID:g1165214 !'##experimental_source strain GRF88 REFERENCE S64517 !$#authors Guerreiro, P.; Barreiros, T.; Cyrne, L.; Soares, H.; Maia e !1Silva, A.; Rodrigues-Pousada, C. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64531 !'##molecule_type DNA !'##residues 1-104 ##label GUW !'##cross-references EMBL:Z72994; NID:g1323374; PIDN:CAA97236.1; !1PID:g1323375; GSPDB:GN00007; MIPS:YGR209c !'##experimental_source strain S288C REFERENCE S63848 !$#authors Guerreiro, P.; Barreiros, T.; Soares, H.; Cyrne, L.; Maia e !1Silva, A.; Rodrigues-Pousada, C. !$#journal Yeast (1996) 12:273-280 !$#title Sequencing of a 17.6 kb segment on the right arm of yeast !1chromosome VII reveals 12 ORFs, including CCT, ADE3 and TR-I !1genes, homologues of the yeast PMT and EF1G genes, of the !1human and bacterial electron-transferring flavoproteins !1(beta-chain) and of the Escherichia coli phosphoserine !1phosphohydrolase, and five new ORFs. !$#cross-references MUID:97060019; PMID:8904340 !$#accession S63858 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-104 ##label GUF !'##cross-references EMBL:Z49133; NID:g790489; PIDN:CAA89002.1; !1PID:g790500 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1995 GENETICS !$#gene SGD:TRX2; TR-I; MIPS:YGR209c !'##cross-references SGD:S0003441; MIPS:YGR209c !$#map_position 7R CLASSIFICATION #superfamily thioredoxin; thioredoxin homology KEYWORDS redox-active disulfide FEATURE !$2-104 #product thioredoxin I #status experimental #label !8MAT\ !$9-91 #domain thioredoxin homology #label THR\ !$31-34 #disulfide_bonds redox-active #status experimental SUMMARY #length 104 #molecular-weight 11204 #checksum 8528 SEQUENCE /// ENTRY TXBY2 #type complete TITLE thioredoxin II - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein L1933; protein YLR043c ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jun-2000 ACCESSIONS S15048; A39847; S15360; S64870; B38669 REFERENCE A38669 !$#authors Gan, Z.R. !$#journal J. Biol. Chem. (1991) 266:1692-1696 !$#title Yeast thioredoxin genes. !$#cross-references MUID:91107668; PMID:1988444 !$#accession S15048 !'##molecule_type DNA !'##residues 1-103 ##label GAN !'##cross-references EMBL:M59169; NID:g173027; PIDN:AAA35171.1; !1PID:g173028 REFERENCE A39847 !$#authors Muller, E.G.D. !$#journal J. Biol. Chem. (1991) 266:9194-9202 !$#title Thioredoxin deficiency in yeast prolongs S phase and !1shortens the G1 interval of the cell cycle. !$#cross-references MUID:91225027; PMID:2026619 !$#accession A39847 !'##molecule_type DNA !'##residues 1-103 ##label MUL !'##cross-references GB:M62647; NID:g173047; PIDN:AAA35177.1; !1PID:g173048 REFERENCE S05793 !$#authors Hall, D.E.; Baldesten, A.; Holmgren, A.; Reichard, P. !$#journal Eur. J. Biochem. (1971) 23:328-335 !$#title Yeast thioredoxin. Amino-acid sequence around the !1active-center disulfide of thioredoxin I and II. !$#cross-references MUID:72100583; PMID:4945270 !$#accession S15360 !'##molecule_type protein !'##residues 26-34 ##label HAL REFERENCE S64863 !$#authors Koetter, P.; Rose, M.; Entian, K.D. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64870 !'##molecule_type DNA !'##residues 1-103 ##label KOE !'##cross-references EMBL:Z73215; NID:g1360372; PIDN:CAA97572.1; !1PID:g1360373; GSPDB:GN00012; MIPS:YLR043c !'##note experimental_source strain S288C GENETICS !$#gene SGD:TRX1; TR-II; MIPS:YLR043c !'##cross-references SGD:S0004033; MIPS:YLR043c !$#map_position 12R CLASSIFICATION #superfamily thioredoxin; thioredoxin homology KEYWORDS redox-active disulfide FEATURE !$2-103 #product thioredoxin II #status predicted #label MAT\ !$9-90 #domain thioredoxin homology #label THR\ !$30-33 #disulfide_bonds redox-active #status experimental SUMMARY #length 103 #molecular-weight 11235 #checksum 4526 SEQUENCE /// ENTRY G64213 #type complete TITLE thioredoxin - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 17-Nov-1995 #sequence_revision 16-Aug-1996 #text_change 07-Dec-1999 ACCESSIONS G64213 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession G64213 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-102 ##label TIGR !'##cross-references GB:U39691; GB:L43967; NID:g1045794; PID:g1045804; !1TIGR:MG124 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily thioredoxin; thioredoxin homology KEYWORDS redox-active disulfide FEATURE !$9-90 #domain thioredoxin homology #label THR\ !$30-33 #disulfide_bonds redox-active #status predicted SUMMARY #length 102 #molecular-weight 11498 #checksum 2245 SEQUENCE /// ENTRY TXEC #type complete TITLE thioredoxin [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 24-Apr-1984 #sequence_revision 01-Sep-1995 #text_change 01-Mar-2002 ACCESSIONS A91519; H65181; S30676; I54863; A91802; I52550; A91236; !1A00280; A22425; A24435; S45671 REFERENCE A91519 !$#authors Wallace, B.J.; Kushner, S.R. !$#journal Gene (1984) 32:399-408 !$#title Genetic and physical analysis of the thioredoxin (trxA) gene !1of Escherichia coli K-12. !$#cross-references MUID:85155506; PMID:6099324 !$#accession A91519 !'##molecule_type DNA !'##residues 'MLHQQRNQHARLIPVELY',1-109 ##label WAL !'##cross-references GB:K02845; NID:g147610; PIDN:AAA24534.1; !1PID:g147611 !'##note the sequence represents translation from an upstream ATG !1triplet that seems not to lie in an appropriate context for !1translation initiation REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65181 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 'MLHQQRNQHARLIPVELY',1-109 ##label BLAT !'##cross-references GB:AE000454; GB:U00096; NID:g2367278; !1PIDN:AAC76786.1; PID:g1790215; UWGP:b3781 !'##experimental_source strain K-12, substrain MG1655 !'##note the sequence represents translation from an upstream ATG !1triplet that seems not to lie in an appropriate context for !1translation initiation REFERENCE S30660 !$#authors Daniels, D.L.; Plunkett III, G.; Burland, V.; Blattner, F.R. !$#journal Science (1992) 257:771-778 !$#title Analysis of the Escherichia coli genome: DNA sequence of the !1region from 84.5 to 86.5 minutes. !$#cross-references MUID:92358234; PMID:1379743 !$#accession S30676 !'##molecule_type DNA !'##residues 'MLHQQRNQHARLIPVELY',1-109 ##label DAN !'##cross-references EMBL:M87049; NID:g836656; PIDN:AAA67582.1; !1PID:g148185 !'##note the sequence represents translation from an upstream ATG !1triplet that seems not to lie in an appropriate context for !1translation initiation REFERENCE I54863 !$#authors Matsumoto, Y.; Shigesada, K.; Hirano, M.; Imai, M. !$#journal J. Bacteriol. (1986) 166:945-958 !$#title Autogenous regulation of the gene for transcription !1termination factor rho in Escherichia coli: Localization and !1function of its attenuators. !$#cross-references MUID:86223816; PMID:2423505 !$#accession I54863 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-109 ##label MAS !'##cross-references GB:M12779; NID:g148067; PIDN:AAA24694.1; !1PID:g148068 REFERENCE A91802 !$#authors Lim, C.J.; Geraghty, D.; Fuchs, J.A. !$#journal J. Bacteriol. (1985) 163:311-316 !$#title Cloning and nucleotide sequence of the trxA gene of !1Escherichia coli K-12. !$#cross-references MUID:85234377; PMID:3891733 !$#accession A91802 !'##molecule_type DNA !'##residues 1-109 ##label LIM !'##cross-references GB:M10424; NID:g147608; PIDN:AAA24533.1; !1PID:g147609 !'##experimental_source strain K12 REFERENCE I52550 !$#authors Hoeoeg, J. !$#journal Biosci. Rep. (1984) 4:917-923 !$#title Nucleotide sequence of the thioredoxin gene from Escherichia !1coli. !$#cross-references MUID:85123150; PMID:6098320 !$#accession I52550 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-109 ##label HOE !'##cross-references GB:M26133; NID:g148065; PIDN:AAA24693.1; !1PID:g148066 REFERENCE A91236 !$#authors Holmgren, A. !$#journal Eur. J. Biochem. (1968) 6:475-484 !$#title Thioredoxin. 6. The amino acid sequence of the protein from !1Escherichia coli B. !$#cross-references MUID:69079993; PMID:4883076 !$#accession A91236 !'##molecule_type protein !'##residues 2-16,'LV',19-71,'IG',74-109 ##label HOL !'##experimental_source strain B REFERENCE S45671 !$#authors Haeberlein, I. !$#journal Eur. J. Biochem. (1994) 223:473-479 !$#title Structure requirements for disulfide bridge sulfitolysis of !1oxidized Escherichia coli thioredoxin studied by !1fluorescence spectroscopy. !$#cross-references MUID:94333336; PMID:8055916 !$#contents annotation; chemical activity of wild type and engineered !1sequence REFERENCE A50900 !$#authors Katti, S.K.; LeMaster, D.M.; Eklund, H. !$#submission submitted to the Brookhaven Protein Data Bank, March 1990 !$#cross-references PDB:2TRX !$#contents annotation; X-ray crystallography, 1.68 angstroms, residues !12-109 REFERENCE A58630 !$#authors Katti, S.K.; LeMaster, D.M.; Eklund, H. !$#journal J. Mol. Biol. (1990) 212:167-184 !$#title Crystal structure of thioredoxin from Escherichia coli at !11.68 Angstroms resolution. !$#cross-references MUID:90204538; PMID:2181145 !$#contents annotation; X-ray crystallography, 1.68 angstroms REFERENCE A93800 !$#authors Holmgren, A.; Soderberg, B.O.; Eklund, H.; Branden, C.I. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1975) 72:2305-2309 !$#title Three-dimensional structure of Escherichia coli !1thioredoxin-S-2 to 2.8 angstrom resolution. !$#cross-references MUID:75176930; PMID:1094461 !$#contents annotation; X-ray crystallography, 2.8 angstroms REFERENCE A50871 !$#authors Dyson, H.J.; Gippert, G.P.; Case, D.A.; Holmgren, A.; !1Wright, P.E. !$#submission submitted to the Brookhaven Protein Data Bank, January 1990 !$#cross-references PDB:1TRX !$#contents annotation; conformation by (1)H-NMR, reduced form, residues !12-109 REFERENCE A58631 !$#authors Dyson, H.J.; Gippert, G.P.; Case, D.A.; Holmgren, A.; !1Wright, P.E. !$#journal Biochemistry (1990) 29:4129-4136 !$#title Three-dimensional solution structure of the reduced form of !1Escherichia coli thioredoxin determined by nuclear magnetic !1resonance spectroscopy. !$#cross-references MUID:90298180; PMID:2193685 !$#contents annotation; conformation by (1)H-NMR REFERENCE A66947 !$#authors Jeng, M.F.; Campbell, A.P.; Begley, T.; Holmgren, A.; Case, !1D.A.; Wright, P.E.; Dyson, H.J. !$#submission submitted to the Brookhaven Protein Data Bank, November 1995 !$#cross-references PDB:1XOA !$#contents annotation; conformation by (1)H-, (15)N-NMR, oxidized form, !1residues 2-109 REFERENCE A66948 !$#authors Jeng, M.F.; Campbell, A.P.; Begley, T.; Holmgren, A.; Case, !1D.A.; Wright, P.E.; Dyson, H.J. !$#submission submitted to the Brookhaven Protein Data Bank, November 1995 !$#cross-references PDB:1XOB !$#contents annotation; conformation by (1)H-, (15)N-NMR, reduced form, !1residues 2-109 GENETICS !$#gene trxA !$#map_position 85 min FUNCTION !$#description is reduced with NADPH by thioredoxin reductase (EC 1.6.4.5); !1the reduced form acts as a two hydrogen atom donor in a !1variety of intracellular reduction reactions; participates !1in dithiol-disulfide exchange reactions CLASSIFICATION #superfamily thioredoxin; thioredoxin homology KEYWORDS redox-active disulfide FEATURE !$2-109 #product thioredoxin #status experimental #label MAT\ !$11-94 #domain thioredoxin homology #label THR\ !$33-36 #disulfide_bonds redox-active #status experimental SUMMARY #length 109 #molecular-weight 11806 #checksum 4730 SEQUENCE /// ENTRY S35497 #type complete TITLE thioredoxin - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 09-Dec-1993 #sequence_revision 26-May-1994 #text_change 08-Dec-2000 ACCESSIONS S35497; A49917; S31928 REFERENCE S35497 !$#authors Kotani, H.; Nakajima, K. !$#journal Nucleic Acids Res. (1992) 20:1424 !$#title Cloning and sequence of thioredoxin gene of Salmonella !1typhimurium LT2. !$#cross-references MUID:92220625; PMID:1561103 !$#accession S35497 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-109 ##label KOT !'##cross-references EMBL:D10015; NID:g217084; PIDN:BAA00903.1; !1PID:g217085 !'##experimental_source strain LT2 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1March 1992 REFERENCE A49917 !$#authors Miloso, M.; Limauro, D.; Alifano, P.; Rivellini, F.; !1Lavitola, A.; Gulletta, E.; Bruni, C.B. !$#journal J. Bacteriol. (1993) 175:8030-8037 !$#title Characterization of the rho genes of Neisseria gonorrhoeae !1and Salmonella typhimurium. !$#cross-references MUID:94075245; PMID:8253691 !$#accession A49917 !'##molecule_type DNA !'##residues 1-109 ##label MIL !'##cross-references GB:Z21789; NID:g49361; PIDN:CAA79851.1; PID:g49362 !'##note submitted to the EMBL Data Library, February 1993 GENETICS !$#gene trxA CLASSIFICATION #superfamily thioredoxin; thioredoxin homology KEYWORDS redox-active disulfide FEATURE !$11-94 #domain thioredoxin homology #label THR\ !$33-36 #disulfide_bonds redox-active #status predicted SUMMARY #length 109 #molecular-weight 11806 #checksum 4730 SEQUENCE /// ENTRY TXAI #type complete TITLE thioredoxin 1 - Anabaena sp. ORGANISM #formal_name Anabaena sp. DATE 31-Dec-1988 #sequence_revision 11-Apr-1997 #text_change 11-Jun-1999 ACCESSIONS I39624; A23910 REFERENCE I39624 !$#authors Lim, C. !$#journal J. Bacteriol. (1986) 168:1258-1264 !$#title Cloning, expression, and characterization of the Anabaena !1thioredoxin gene in Escherichia coli. !$#cross-references MUID:87057030; PMID:3096973 !$#accession I39624 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-107 ##label RES !'##cross-references GB:M14736; NID:g142117; PIDN:AAA22049.1; !1PID:g142118 REFERENCE A23910 !$#authors Gleason, F.K.; Whittaker, M.M.; Holmgren, A.; Joernvall, H. !$#journal J. Biol. Chem. (1985) 260:9567-9573 !$#title The primary structure of thioredoxin from the filamentous !1cyanobacterium Anabaena sp. 7119. !$#cross-references MUID:85261357; PMID:3926769 !$#accession A23910 !'##molecule_type protein !'##residues 2-107 ##label GLE !'##experimental_source PCC 7119, ATCC 29151 CLASSIFICATION #superfamily thioredoxin; thioredoxin homology KEYWORDS heat-stable protein; redox-active disulfide FEATURE !$2-107 #product thioredoxin #status experimental #label MAT\ !$10-93 #domain thioredoxin homology #label THR\ !$32-35 #disulfide_bonds redox-active #status predicted SUMMARY #length 107 #molecular-weight 11721 #checksum 5823 SEQUENCE /// ENTRY A26622 #type complete TITLE thioredoxin - Chromatium vinosum ORGANISM #formal_name Chromatium vinosum DATE 31-Mar-1988 #sequence_revision 26-May-1994 #text_change 11-Apr-1995 ACCESSIONS A26622 REFERENCE A26622 !$#authors Johnson, R.S.; Biemann, K. !$#journal Biochemistry (1987) 26:1209-1214 !$#title The primary structure of thioredoxin from Chromatium vinosum !1determined by high-performance tandem mass spectrometry. !$#cross-references MUID:87185419; PMID:3567166 !$#accession A26622 !'##molecule_type protein !'##residues 1-107 ##label JOH !'##note unidentified residues are Ile or Leu CLASSIFICATION #superfamily thioredoxin; thioredoxin homology KEYWORDS heat-stable protein; redox-active disulfide FEATURE !$10-93 #domain thioredoxin homology #label THR\ !$32-35 #disulfide_bonds redox-active #status predicted SUMMARY #length 107 #molecular-weight 11727 #checksum 3880 SEQUENCE /// ENTRY A35135 #type complete TITLE thioredoxin - Rhodobacter sphaeroides ORGANISM #formal_name Rhodobacter sphaeroides DATE 27-Jul-1990 #sequence_revision 26-May-1994 #text_change 11-Jun-1999 ACCESSIONS A35135; A30508 REFERENCE A35135 !$#authors Pille, S.; Chuat, J.C.; Breton, A.M.; Clement-Metral, J.D.; !1Galibert, F. !$#journal J. Bacteriol. (1990) 172:1556-1561 !$#title Cloning, nucleotide sequence, and expression of the !1Rhodobacter sphaeroides Y thioredoxin gene. !$#cross-references MUID:90170874; PMID:2137818 !$#accession A35135 !'##molecule_type DNA !'##residues 1-106 ##label PIL !'##cross-references GB:M33806; NID:g152044; PIDN:AAA26182.1; !1PID:g152045 !'##experimental_source strain Y REFERENCE A30508 !$#authors Clement-Metral, J.D.; Holmgren, A.; Cambillau, C.; !1Joernvall, H.; Eklund, H.; Thomas, D.; Lederer, F. !$#journal Eur. J. Biochem. (1988) 172:413-419 !$#title Amino acid sequence determination and three-dimensional !1modelling of thioredoxin from the photosynthetic bacterium !1Rhodobacter sphaeroides Y. !$#cross-references MUID:88166714; PMID:3280308 !$#accession A30508 !'##molecule_type protein !'##residues 2-63,'Z',65-106 ##label CLE !'##experimental_source strain Y CLASSIFICATION #superfamily thioredoxin; thioredoxin homology KEYWORDS redox-active disulfide FEATURE !$9-92 #domain thioredoxin homology #label THR\ !$31-34 #disulfide_bonds redox-active #status predicted SUMMARY #length 106 #molecular-weight 11343 #checksum 7899 SEQUENCE /// ENTRY A28215 #type complete TITLE thioredoxin - Rhodospirillum rubrum ORGANISM #formal_name Rhodospirillum rubrum DATE 28-Aug-1989 #sequence_revision 26-May-1994 #text_change 11-Apr-1995 ACCESSIONS A28215 REFERENCE A28215 !$#authors Johnson, T.C.; Yee, B.C.; Carlson, D.E.; Buchanan, B.B.; !1Johnson, R.S.; Mathews, W.R.; Biemann, K. !$#journal J. Bacteriol. (1988) 170:2406-2408 !$#title Thioredoxin from Rhodospirillum rubrum: primary structure !1and relation to thioredoxins from other photosynthetic !1bacteria. !$#cross-references MUID:88198045; PMID:3129411 !$#accession A28215 !'##molecule_type protein !'##residues 1-104 ##label JOH CLASSIFICATION #superfamily thioredoxin; thioredoxin homology KEYWORDS redox-active disulfide FEATURE !$7-90 #domain thioredoxin homology #label THR\ !$29-32 #disulfide_bonds redox-active #status predicted SUMMARY #length 104 #molecular-weight 11299 #checksum 9678 SEQUENCE /// ENTRY A32956 #type complete TITLE thioredoxin m - Synechococcus sp. ORGANISM #formal_name Synechococcus sp. DATE 17-Jul-1992 #sequence_revision 26-May-1994 #text_change 11-Jun-1999 ACCESSIONS A32956; A30842 REFERENCE A32956 !$#authors Muller, E.G.D.; Buchanan, B.B. !$#journal J. Biol. Chem. (1989) 264:4008-4014 !$#title Thioredoxin is essential for photosynthetic growth. The !1thioredoxin m gene of Anacystis nidulans. !$#cross-references MUID:89139466; PMID:2492995 !$#accession A32956 !'##molecule_type DNA !'##residues 1-107 ##label MUL !'##cross-references GB:J04475; NID:g142153; PIDN:AAA22057.1; !1PID:g142154 !'##note the source is designated as Anacystis nidulans R2, which is !1also called Synechococcus R2 GENETICS !$#gene trxM CLASSIFICATION #superfamily thioredoxin; thioredoxin homology KEYWORDS redox-active disulfide FEATURE !$10-93 #domain thioredoxin homology #label THR\ !$32-35 #disulfide_bonds redox-active #status predicted SUMMARY #length 107 #molecular-weight 11648 #checksum 6615 SEQUENCE /// ENTRY S31915 #type complete TITLE thioredoxin - red alga (Cyanidium caldarium) ORGANISM #formal_name Cyanidium caldarium DATE 03-Mar-1994 #sequence_revision 26-May-1994 #text_change 11-Jun-1999 ACCESSIONS S31915; S45488 REFERENCE S31915 !$#authors Langsdorf, A.; Emich, A.; Zetsche, K. !$#submission submitted to the EMBL Data Library, February 1993 !$#description A thioredoxin gene is located upstream of rbcLS in the !1unicellular red alga Cyanidium caldarium, strain RK-1. !$#accession S31915 !'##molecule_type DNA !'##residues 1-107 ##label LAN !'##cross-references EMBL:Z21723; NID:g14402; PIDN:CAA79820.1; !1PID:g14403 REFERENCE S45488 !$#authors Ohta, N.; Kawano, S.; Kuroiwa, T. !$#journal Curr. Genet. (1994) 26:136-138 !$#title Physical map of the plastid genome of the unicellular red !1alga Cyanidium caldarium strain RK-1. !$#cross-references MUID:95094309; PMID:8001167 !$#accession S45488 !'##status preliminary !'##molecule_type DNA !'##residues 'M',6,'IDEL',11-12,'DT',15-16,'LQ',19,'HQ',22-38,'A',40, !1'IL',43-44,'I',46-48,'LDI',54,'V',56-57,'L',59-64,'NLAT', !169-82,'K',84,'Q',86,'L',88-99,'M',101,'TIE',105-107 ##label !1OHT GENETICS !$#gene trx CLASSIFICATION #superfamily thioredoxin; thioredoxin homology KEYWORDS redox-active disulfide FEATURE !$10-93 #domain thioredoxin homology #label THR\ !$32-35 #disulfide_bonds redox-active #status predicted SUMMARY #length 107 #molecular-weight 12032 #checksum 5637 SEQUENCE /// ENTRY TXFK #type complete TITLE thioredoxin - coryneform bacterium ATCC11425 ORGANISM #formal_name coryneform bacterium ATCC11425 DATE 02-Apr-1982 #sequence_revision 02-Apr-1982 #text_change 11-Apr-1995 ACCESSIONS A00281 REFERENCE A00281 !$#authors Meng, M.; Hogenkamp, H.P.C. !$#journal J. Biol. Chem. (1981) 256:9174-9182 !$#title Purification, characterization, and amino acid sequence of !1thioredoxin from Corynebacterium nephridii. !$#cross-references MUID:81264365; PMID:7021558 !$#accession A00281 !'##molecule_type protein !'##residues 1-105 ##label MEN !'##note the source was designated as Corynebacterium nephridii COMMENT Thioredoxins are ubiquitous small hydrogen carrier proteins !1that participate in a wide variety of biochemical reactions. CLASSIFICATION #superfamily thioredoxin; thioredoxin homology KEYWORDS redox-active disulfide FEATURE !$8-91 #domain thioredoxin homology #label THR\ !$30-33 #disulfide_bonds redox-active #status experimental SUMMARY #length 105 #molecular-weight 11279 #checksum 1012 SEQUENCE /// ENTRY TXSPM #type complete TITLE thioredoxin m precursor - spinach ORGANISM #formal_name Spinacia oleracea #common_name spinach DATE 30-Sep-1988 #sequence_revision 13-Mar-1998 #text_change 11-Jun-1999 ACCESSIONS S20496; JT0023; B20273 REFERENCE S20496 !$#authors Wedel, N.; Clausmeyer, S.; Herrmann, R.G.; Gardet-Salvi, L.; !1Schuermann, P. !$#journal Plant Mol. Biol. (1992) 18:527-533 !$#title Nucleotide sequence of cDNAs encoding the entire precursor !1polypeptide for thioredoxin m from spinach chloroplasts. !$#cross-references MUID:92163017; PMID:1536927 !$#accession S20496 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-181 ##label WED !'##cross-references GB:X51462; GB:S84848; NID:g21347; PIDN:CAA35826.1; !1PID:g21348 REFERENCE A91158 !$#authors Maeda, K.; Tsugita, A.; Dalzoppo, D.; Vilbois, F.; !1Schurmann, P. !$#journal Eur. J. Biochem. (1986) 154:197-203 !$#title Further characterization and amino acid sequence of m-type !1thioredoxins from spinach chloroplasts. !$#cross-references MUID:86108311; PMID:3510868 !$#accession JT0023 !'##molecule_type protein !'##residues 68-82,'G',84-89,'Q',91,'SE',94,'S',96-127,'T',129-164,'D', !1166,'S',168,'YQ',171 ##label MAE COMMENT This enzyme has amino-terminal heterogeneity. Thioredoxin m !1activates malate dehydrogenase. COMMENT Arg-145 and Gly-164 are both essential for thioredoxin to !1interact with thioredoxin reductase and ribonucleotide !1reductase. CLASSIFICATION #superfamily thioredoxin; thioredoxin homology KEYWORDS chloroplast; redox-active disulfide FEATURE !$1-67 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$68-171 #product thioredoxin mb #status experimental #label !8PRB\ !$69-171 #product thioredoxin mc #status experimental #label !8PRC\ !$70-171 #product thioredoxin md #status experimental #label !8PRD\ !$82-165 #domain thioredoxin homology #label THR\ !$104-107 #disulfide_bonds redox-active #status experimental SUMMARY #length 181 #molecular-weight 19840 #checksum 8336 SEQUENCE /// ENTRY B37192 #type complete TITLE thioredoxin - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 31-Jan-1992 #sequence_revision 26-May-1994 #text_change 16-Jun-2000 ACCESSIONS B37192; H69726 REFERENCE A37192 !$#authors Chen, N.Y.; Zhang, J.J.; Paulus, H. !$#journal J. Gen. Microbiol. (1989) 135:2931-2940 !$#title Chromosomal location of the Bacillus subtilis aspartokinase !1II gene and nucleotide sequence of the adjacent genes !1homologous to uvrC and trx of Escherichia coli. !$#cross-references MUID:90132525; PMID:2559145 !$#accession B37192 !'##molecule_type DNA !'##residues 1-104 ##label CHE !'##cross-references GB:J03294; GB:M26384; NID:g142519; PIDN:AAA87315.1; !1PID:g142520 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69726 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-104 ##label KUN !'##cross-references GB:Z99118; GB:AL009126; NID:g2635200; !1PIDN:CAB14810.1; PID:g2635315 !'##experimental_source strain 168 GENETICS !$#gene trxA !$#map_position 70 min CLASSIFICATION #superfamily thioredoxin; thioredoxin homology KEYWORDS redox-active disulfide FEATURE !$9-90 #domain thioredoxin homology #label THR\ !$29-32 #disulfide_bonds redox-active #status experimental SUMMARY #length 104 #molecular-weight 11393 #checksum 9852 SEQUENCE /// ENTRY S02802 #type complete TITLE thioredoxin C-2 - coryneform bacterium ORGANISM #formal_name coryneform bacterium DATE 28-Feb-1990 #sequence_revision 26-May-1994 #text_change 28-May-1999 ACCESSIONS S02802; A29797 REFERENCE S02802 !$#authors McFarlan, S.C.; Hogenkamp, H.P.C.; Eccleston, E.D.; Howard, !1J.B.; Fuchs, J.A. !$#journal Eur. J. Biochem. (1989) 179:389-398 !$#title Purification, characterization and revised amino acid !1sequence of a second thioredoxin from Corynebacterium !1nephridii. !$#cross-references MUID:89137116; PMID:2917572 !$#accession S02802 !'##molecule_type protein !'##residues 1-108 ##label MCF !'##note the source is designated as Corynebacterium nephridii REFERENCE A29797 !$#authors Lim, C.J.; Fuchs, J.A.; McFarlan, S.C.; Hogenkamp, H.P.C. !$#journal J. Biol. Chem. (1987) 262:12114-12119 !$#title Cloning, expression, and nucleotide sequence of a gene !1encoding a second thioredoxin from Corynebacterium !1nephridii. !$#cross-references MUID:87308211; PMID:3040729 !$#accession A29797 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 'MMFKFALYFLNLEQPY',2-108 ##label MCF2 !'##cross-references GB:J02801; NID:g144988; PIDN:AAA23305.1; !1PID:g144989 !'##note the source is designated as Corynebacterium nephridii !'##note this sequence has been revised in reference S02802 CLASSIFICATION #superfamily thioredoxin; thioredoxin homology KEYWORDS redox-active disulfide FEATURE !$2-108 #product thioredoxin C-2 #status experimental #label !8MAT\ !$11-94 #domain thioredoxin homology #label THR\ !$33-36 #disulfide_bonds redox-active #status predicted SUMMARY #length 108 #molecular-weight 11716 #checksum 3605 SEQUENCE /// ENTRY S38909 #type complete TITLE thioredoxin m precursor - garden pea ORGANISM #formal_name Pisum sativum #common_name garden pea DATE 22-Jan-1994 #sequence_revision 26-May-1994 #text_change 11-Jun-1999 ACCESSIONS S38909 REFERENCE S38909 !$#authors Lopez Jaramillo, J.; Chueca, A.; Sahrawy, M.; Prado, F.; !1Lazaro, J.J.; Hermoso, R.; Lopez Gorge, J. !$#submission submitted to the EMBL Data Library, November 1993 !$#accession S38909 !'##molecule_type mRNA !'##residues 1-172 ##label LOP !'##cross-references EMBL:X76269; NID:g431956; PIDN:CAA53900.1; !1PID:g431957 CLASSIFICATION #superfamily thioredoxin; thioredoxin homology KEYWORDS chloroplast; redox-active disulfide FEATURE !$1-57 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$58-172 #product thioredoxin m #status predicted #label TMB\ !$75-158 #domain thioredoxin homology #label THR\ !$97-100 #disulfide_bonds redox-active #status predicted SUMMARY #length 172 #molecular-weight 19156 #checksum 7833 SEQUENCE /// ENTRY A32233 #type complete TITLE thioredoxin 2 [validated] - Anabaena sp. (strain PCC 7120) ORGANISM #formal_name Anabaena sp. #variety strain PCC 7120 DATE 08-Sep-1989 #sequence_revision 26-May-1994 #text_change 15-Sep-2000 ACCESSIONS A32233 REFERENCE A32233 !$#authors Alam, J.; Curtis, S.; Gleason, F.K.; Gerami-Nejad, M.; !1Fuchs, J.A. !$#journal J. Bacteriol. (1989) 171:162-171 !$#title Isolation, sequence, and expression in Escherichia coli of !1an unusual thioredoxin gene from the cyanobacterium Anabaena !1sp. strain PCC 7120. !$#cross-references MUID:89123014; PMID:2492494 !$#accession A32233 !'##molecule_type DNA !'##residues 1-111 ##label ALA !'##cross-references GB:M22997; NID:g340784; PIDN:AAA22048.1; !1PID:g517044 !'##experimental_source PCC 7120 REFERENCE A58615 !$#authors Gleason, F.K. !$#journal J. Bacteriol. (1992) 174:2592-2598 !$#title Activities of two dissimilar thioredoxins from the !1cyanobacterium Anabaena sp. strain PCC 7120. !$#cross-references MUID:92210503; PMID:1556078 !$#contents annotation; expression and possible metabolic role REFERENCE A66730 !$#authors Saarinen, M.; Gleason, F.K.; Eklund, H. !$#submission submitted to the Brookhaven Protein Data Bank, July 1995 !$#cross-references PDB:1THX !$#contents annotation; X-ray crystallography, 1.7 angstroms, residues !12-109 !$#note strain PCC 7120, ATCC:27893, expressed in Escherichia coli FUNCTION !$#description is reduced with NADPH by thioredoxin reductase (EC 1.6.4.5); !1the reduced form acts as a two hydrogen atom donor in a !1variety of intracellular reduction reactions; participates !1in dithiol-disulfide exchange reactions !$#note thioredoxin 2 is expressed at very low levels and may !1function in glucose metabolism CLASSIFICATION #superfamily thioredoxin; thioredoxin homology KEYWORDS redox-active disulfide FEATURE !$11-94 #domain thioredoxin homology #label THR\ !$33-36 #disulfide_bonds redox-active #status predicted SUMMARY #length 111 #molecular-weight 12366 #checksum 1382 SEQUENCE /// ENTRY S57775 #type complete TITLE thioredoxin h, cytosolic [validated] - Chlamydomonas reinhardtii ORGANISM #formal_name Chlamydomonas reinhardtii DATE 27-Oct-1995 #sequence_revision 21-Jan-1997 #text_change 15-Sep-2000 ACCESSIONS S57775; S57799; S54868; S16090; S54870 REFERENCE S57774 !$#authors Stein, M.; Jacquot, J.P.; Jeannette, E.; Decottignies, P.; !1Hodges, M.; Lancelin, J.M.; Mittard, V.; Schmitter, J.M.; !1Miginiac-Maslow, M. !$#journal Plant Mol. Biol. (1995) 28:487-503 !$#title Chlamydomonas reinhardtii thioredoxins: structure of the !1genes coding for the chloroplastic m and cytosolic h !1isoforms; expression in Escherichia coli of the recombinant !1proteins, purification and biochemical properties. !$#cross-references MUID:95359406; PMID:7632918 !$#accession S57775 !'##molecule_type DNA !'##residues 1-113 ##label STE !'##cross-references EMBL:X80887; NID:g840742; PIDN:CAA56850.1; !1PID:g840743 !$#accession S57799 !'##molecule_type protein !'##residues 2-15 ##label STW REFERENCE S54844 !$#authors Stein, M.; Hodges, M.; Jeanette, E.; Lancelin, J.M.; !1Jacquot, J.P. !$#submission submitted to the EMBL Data Library, April 1994 !$#description Chlamydomonas reinhardtii thioredoxins I : cDNA and amino !1acid deduced sequences of chloroplastic m and cytosolic h !1isoforms. !$#accession S54868 !'##molecule_type mRNA !'##residues 1-113 ##label STF !'##cross-references EMBL:X78822; NID:g840740; PIDN:CAA55399.1; !1PID:g840741 REFERENCE S16090 !$#authors Decottignies, P.; Schmitter, J.M.; Dutka, S.; Jacquot, J.P.; !1Miginiac-Maslow, M. !$#journal Eur. J. Biochem. (1991) 198:505-512 !$#title Characterization and primary structure of a second !1thioredoxin from the green alga, Chlamydomonas reinhardtii. !$#cross-references MUID:91249849; PMID:2040309 !$#accession S16090 !'##molecule_type protein !'##residues 2-112 ##label MIG REFERENCE A66748 !$#authors Mittard, V.; Blackledge, M.J.; Stein, M.; Jacquot, J.P.; !1Marion, D.; Lancelin, J.M. !$#submission submitted to the Brookhaven Protein Data Bank, May 1996 !$#cross-references PDB:1TOF !$#contents annotation; conformation by (1)H, (13)C, (15)N-NMR, residues !12-113 REFERENCE A58618 !$#authors Mittard, V.; Morelle, N.; Brutscher, B.; Simorre, J.P.; !1Marion, D.; Stein, M.; Jacquot, J.P.; Lirsac, P.N.; !1Lancelin, J.M. !$#journal Eur. J. Biochem. (1995) 229:473-485 !$#title (1)H, (13)C, (15)N-NMR resonance assignments of oxidized !1thioredoxin h from the eukaryotic green alga Chlamydomonas !1reinhardtii using new methods based on two-dimensional !1triple-resonance NMR spectroscopy and computer-assisted !1backbone assignment. !$#cross-references MUID:95262711; PMID:7744070 !$#contents annotation; conformation by (1)H, (13)C, (15)N-NMR GENETICS !$#introns 27/3; 35/3; 69/3 CLASSIFICATION #superfamily thioredoxin; thioredoxin homology KEYWORDS redox-active disulfide FEATURE !$2-113 #product thioredoxin h #status experimental #label !8MAT\ !$15-98 #domain thioredoxin homology #label THR\ !$37-40 #disulfide_bonds redox-active #status experimental SUMMARY #length 113 #molecular-weight 11844 #checksum 706 SEQUENCE /// ENTRY A55124 #type complete TITLE thioredoxin - Chloroflexus aurantiacus ORGANISM #formal_name Chloroflexus aurantiacus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A55124 REFERENCE A55124 !$#authors Biemann, K.; Papayannopoulos, I.A. !$#journal Acc. Chem. Res. (1994) 27:370-378 !$#title Amino acid sequencing of proteins. !$#accession A55124 !'##status preliminary !'##molecule_type protein !'##residues 1-109 ##label BIE !'##note 41-Asn, 58-Asp, 59-Val were also found !'##note the species is identified as Chlorofleuxus aurianticus COMMENT Unidentified residue is Ile or Leu. CLASSIFICATION #superfamily thioredoxin; thioredoxin homology KEYWORDS methylated amino acid; redox-active disulfide FEATURE !$9-92 #domain thioredoxin homology #label THR\ !$31-34 #disulfide_bonds redox-active #status predicted\ !$104 #modified_site N6-methyllysine or N6, !8N6-dimethyllysine (Lys) (partial) #status !8experimental SUMMARY #length 109 #molecular-weight 11997 #checksum 8659 SEQUENCE /// ENTRY S38989 #type complete TITLE thioredoxin - Eubacterium acidaminophilum ALTERNATE_NAMES glycine reductase complex thioredoxin chain A ORGANISM #formal_name Eubacterium acidaminophilum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S38989 REFERENCE S38988 !$#authors Luebbers, M.; Andreesen, J.R. !$#journal Eur. J. Biochem. (1993) 217:791-798 !$#title Components of glycine reductase from Eubacterium !1acidaminophilum. Cloning, sequencing and identification of !1the genes for thioredoxin reductase, thioredoxin and !1selenoprotein P(A). !$#cross-references MUID:94039119; PMID:8223622 !$#accession S38989 !'##status preliminary !'##molecule_type DNA !'##residues 1-110 ##label LUE !'##cross-references GB:L04500; NID:g2708733; PIDN:AAB93304.1; !1PID:g388295 CLASSIFICATION #superfamily thioredoxin; thioredoxin homology KEYWORDS redox-active disulfide FEATURE !$11-94 #domain thioredoxin homology #label THR\ !$33-36 #disulfide_bonds redox-active #status predicted SUMMARY #length 110 #molecular-weight 12142 #checksum 617 SEQUENCE /// ENTRY A46264 #type complete TITLE thioredoxin 1 - slime mold (Dictyostelium discoideum) ORGANISM #formal_name Dictyostelium discoideum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A46264 REFERENCE A46264 !$#authors Wetterauer, B.; Jacquot, J.P.; Veron, M. !$#journal J. Biol. Chem. (1992) 267:9895-9904 !$#title Thioredoxins from Dictyostelium discoideum are a !1developmentally regulated multigene family. !$#cross-references MUID:92250653; PMID:1577820 !$#accession A46264 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-105 ##label WET !'##cross-references GB:M91384; NID:g167928; PIDN:AAA33258.1; !1PID:g167929 CLASSIFICATION #superfamily thioredoxin; thioredoxin homology KEYWORDS redox-active disulfide FEATURE !$9-92 #domain thioredoxin homology #label THR\ !$32-35 #disulfide_bonds redox-active #status predicted SUMMARY #length 105 #molecular-weight 11926 #checksum 5932 SEQUENCE /// ENTRY S47867 #type complete TITLE thioredoxin-like protein - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S47867 REFERENCE S47867 !$#authors Salz, H.K.; Flickinger, T.W.; Mittendorf, E.; !1Pellicena-Palle, A.; Petschek, J.P.; Brown Albrecht, E. !$#journal Genetics (1994) 136:1075-1086 !$#title The Drosophila maternal effect locus deadhead encodes a !1thioredoxin homolog required for female meiosis and early !1embryonic development. !$#cross-references MUID:94274010; PMID:7516301 !$#accession S47867 !'##status preliminary !'##molecule_type mRNA !'##residues 1-107 ##label SAL !'##cross-references EMBL:L27072; NID:g435591; PIDN:AAA28937.1; !1PID:g435963 GENETICS !$#gene FlyBase:dhd !'##cross-references FlyBase:FBgn0011761 CLASSIFICATION #superfamily thioredoxin; thioredoxin homology KEYWORDS redox-active disulfide FEATURE !$8-92 #domain thioredoxin homology #label THR\ !$31-34 #disulfide_bonds redox-active #status predicted SUMMARY #length 107 #molecular-weight 12384 #checksum 2884 SEQUENCE /// ENTRY S19498 #type complete TITLE thioredoxin homolog YCR083w - yeast (Saccharomyces cerevisiae) ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S19498 REFERENCE S19429 !$#authors Feldmann, H.; Mannhaupt, G.; Vetter, I. !$#submission submitted to the Protein Sequence Database, March 1992 !$#accession S19498 !'##molecule_type DNA !'##residues 1-127 ##label FEL !'##cross-references EMBL:X59720; NID:g1907116; PIDN:CAA42258.1; !1PID:g1907220; GSPDB:GN00003; MIPS:YCR083w GENETICS !$#gene SGD:TRX3; MIPS:YCR083w !'##cross-references SGD:S0000679 !$#map_position 3R CLASSIFICATION #superfamily thioredoxin; thioredoxin homology KEYWORDS redox-active disulfide FEATURE !$34-115 #domain thioredoxin homology #label THR\ !$55-58 #disulfide_bonds redox-active #status predicted SUMMARY #length 127 #molecular-weight 14432 #checksum 7770 SEQUENCE /// ENTRY S57774 #type complete TITLE thioredoxin m precursor, chloroplast - Chlamydomonas reinhardtii ORGANISM #formal_name Chlamydomonas reinhardtii DATE 27-Oct-1995 #sequence_revision 21-Jan-1997 #text_change 05-May-2000 ACCESSIONS S57774; S57800; S54844; S22810; S10743; S18859; S54869 REFERENCE S57774 !$#authors Stein, M.; Jacquot, J.P.; Jeannette, E.; Decottignies, P.; !1Hodges, M.; Lancelin, J.M.; Mittard, V.; Schmitter, J.M.; !1Miginiac-Maslow, M. !$#journal Plant Mol. Biol. (1995) 28:487-503 !$#title Chlamydomonas reinhardtii thioredoxins: structure of the !1genes coding for the chloroplastic m and cytosolic h !1isoforms; expression in Escherichia coli of the recombinant !1proteins, purification and biochemical properties. !$#cross-references MUID:95359406; PMID:7632918 !$#accession S57774 !'##molecule_type DNA !'##residues 1-140 ##label STE !'##cross-references EMBL:X80888; NID:g840746; PIDN:CAA56851.1; !1PID:g840747 !$#accession S57800 !'##molecule_type protein !'##residues 35-42 ##label STW REFERENCE S54844 !$#authors Stein, M.; Hodges, M.; Jeanette, E.; Lancelin, J.M.; !1Jacquot, J.P. !$#submission submitted to the EMBL Data Library, April 1994 !$#description Chlamydomonas reinhardtii thioredoxins I : cDNA and amino !1acid deduced sequences of chloroplastic m and cytosolic h !1isoforms. !$#accession S54844 !'##molecule_type mRNA !'##residues 13-140 ##label STF !'##cross-references EMBL:X78821; NID:g840744; PIDN:CAA55398.1; !1PID:g840745 REFERENCE S22810 !$#authors Jacquot, J.P.; Stein, M.; Hodges, M.; Miginiac-Maslow, M. !$#journal Nucleic Acids Res. (1992) 20:617 !$#title PCR cloning of a nucleotidic sequence coding for the mature !1part of Chlamydomonas reinhardtii thioredoxin Ch2. !$#cross-references MUID:92158682; PMID:1741302 !$#accession S22810 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type mRNA !'##residues 35-140 ##label JA2 !'##cross-references EMBL:X62335; NID:g18240; PIDN:CAA44209.1; !1PID:g18241 !'##note this sequence was submitted to the EMBL Data Library, November !11991 REFERENCE S10743 !$#authors Decottignies, P.; Schmitter, J.M.; Jacquot, J.P.; Dutka, S.; !1Picaud, A.; Gadal, P. !$#journal Arch. Biochem. Biophys. (1990) 280:112-121 !$#title Purification, characterization, and complete amino acid !1sequence of a thioredoxin from a green alga, Chlamydomonas !1reinhardtii. !$#cross-references MUID:90282480; PMID:2191628 !$#accession S10743 !'##molecule_type protein !'##residues 35-40,'EE',43-86,'E',88-118,'D',120-140 ##label DEC GENETICS !$#genome nuclear !$#introns 111/3 CLASSIFICATION #superfamily thioredoxin; thioredoxin homology KEYWORDS chloroplast; redox-active disulfide FEATURE !$1-34 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$35-140 #product thioredoxin #status experimental #label MAT\ !$42-125 #domain thioredoxin homology #label THR\ !$64-67 #disulfide_bonds redox-active #status predicted SUMMARY #length 140 #molecular-weight 15101 #checksum 2003 SEQUENCE /// ENTRY S47472 #type complete TITLE glutaredoxin - human ALTERNATE_NAMES thioltransferase ORGANISM #formal_name Homo sapiens #common_name man DATE 13-Jan-1995 #sequence_revision 02-Jul-1998 #text_change 11-Jun-1999 ACCESSIONS S68701; S45357; S70628; S77693; A44568; B44568; I37436; !1S67515; S47472; S67480 REFERENCE S68701 !$#authors Padilla, C.A.; Spyrou, G.; Holmgren, A. !$#journal FEBS Lett. (1996) 378:69-73 !$#title High-level expression of fully active human glutaredoxin !1(thioltransferase) in E. coli and characterization of Cys(7) !1to Ser mutant protein. !$#cross-references MUID:96140711; PMID:8549805 !$#accession S68701 !'##molecule_type mRNA !'##residues 1-106 ##label PAD !'##cross-references EMBL:X76648; NID:g531404; PIDN:CAA54094.1; !1PID:g531405 REFERENCE S45357 !$#authors Fernando, M.R.; Sumimoto, H.; Nanri, H.; Kawabata, S.; !1Iwanaga, S.; Minakami, S.; Fukumaki, Y.; Takeshige, K. !$#journal Biochim. Biophys. Acta (1994) 1218:229-231 !$#title Cloning and sequencing of the cDNA encoding human !1glutaredoxin. !$#cross-references MUID:94289487; PMID:8018729 !$#accession S45357 !'##molecule_type mRNA !'##residues 1-95,'V',97-106 ##label FER !'##cross-references EMBL:D21238; NID:g643694; PIDN:BAA04769.1; !1PID:g643695 REFERENCE S70628 !$#authors Park, J.B.; Levine, M. !$#journal Biochem. J. (1996) 315:931-938 !$#title Purification, cloning and expression of dehydroascorbic !1acid-reducing activity from human neutrophils: !1identification as glutaredoxin. !$#cross-references MUID:96220709; PMID:8645179 !$#accession S70628 !'##molecule_type mRNA !'##residues 1-106 ##label PAR1 !'##cross-references EMBL:U40574; NID:g1172130; PID:g1172131 !'##experimental_source cell-type neutrophil !$#accession S77693 !'##molecule_type protein !'##residues 15-27;78-87,'X',89-94 ##label PAR2 !'##experimental_source cell-type neutrophil REFERENCE A44568 !$#authors Papov, V.V.; Gravina, S.A.; Mieyal, J.J.; Biemann, K. !$#journal Protein Sci. (1994) 3:428-434 !$#title The primary structure and properties of thioltransferase !1(glutaredoxin) from human red blood cells. !$#cross-references MUID:94290317; PMID:8019414 !$#accession A44568 !'##molecule_type protein !'##residues 2-51,'D',53-106 ##label PAP !$#accession B44568 !'##molecule_type protein !'##residues 2-106 ##label PA2 REFERENCE I37436 !$#authors Padilla, C.A.; Martinez-Galisteo, E.; Barcena, J.A.; Spyrou, !1G.; Holmgren, A. !$#journal Eur. J. Biochem. (1995) 227:27-34 !$#title Purification from placenta, amino acid sequence, structure !1comparisons and cDNA cloning of human glutaredoxin. !$#cross-references MUID:95154298; PMID:7851394 !$#accession I37436 !'##molecule_type mRNA !'##residues 1-106 ##label PAF !'##cross-references EMBL:X76648; NID:g531404; PIDN:CAA54094.1; !1PID:g531405 !'##experimental_source placenta !$#accession S67515 !'##molecule_type protein !'##residues 4-105 ##label PAW !'##experimental_source placenta GENETICS !$#gene GDB:GLRX; GDB:GXN !'##cross-references GDB:574099; GDB:377324; OMIM:600443 !$#map_position 5q14-5q14 FUNCTION !$#description catalyzes reduction of a variety of disulfides, including !1protein disulfides, in the presence of reduced glutathione CLASSIFICATION #superfamily glutaredoxin; glutaredoxin homology KEYWORDS acetylated amino end; deoxyribonucleotide biosynthesis; !1disulfide bond; electron transfer; redox-active disulfide FEATURE !$5-99 #domain glutaredoxin homology #label GLUT\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental\ !$23-26 #disulfide_bonds redox-active #status predicted\ !$79-83 #disulfide_bonds #status predicted SUMMARY #length 106 #molecular-weight 11776 #checksum 9054 SEQUENCE /// ENTRY GDPG #type complete TITLE glutaredoxin - pig ALTERNATE_NAMES thioltransferase ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 11-Jun-1999 ACCESSIONS JQ0117; A29322 REFERENCE JQ0117 !$#authors Yang, Y.; Gan, Z.R.; Wells, W.W. !$#journal Gene (1989) 83:339-346 !$#title Cloning and sequencing the cDNA encoding pig liver !1thioltransferase. !$#cross-references MUID:90060846; PMID:2583530 !$#accession JQ0117 !'##molecule_type mRNA !'##residues 1-106 ##label YAN !'##cross-references GB:M31453; NID:g164705; PIDN:AAA31132.1; !1PID:g164706 !'##experimental_source liver REFERENCE A29322 !$#authors Gan, Z.R.; Wells, W.W. !$#journal J. Biol. Chem. (1987) 262:6699-6703 !$#title The primary structure of pig liver thioltransferase. !$#cross-references MUID:87194912; PMID:3571278 !$#accession A29322 !'##molecule_type protein !'##residues 3-4,'A',5-106 ##label GAN !'##experimental_source liver COMMENT This enzyme catalyzes the reduction of a variety of !1disulfides, including protein disulfides, in the presence of !1reduced glutathione. CLASSIFICATION #superfamily glutaredoxin; glutaredoxin homology KEYWORDS acetylated amino end; deoxyribonucleotide biosynthesis; !1electron transfer; redox-active disulfide FEATURE !$2-106 #product glutaredoxin #status experimental #label !8MAT\ !$5-99 #domain glutaredoxin homology #label GLUT\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental\ !$23-26 #disulfide_bonds redox-active #status predicted\ !$79-83 #disulfide_bonds #status experimental SUMMARY #length 106 #molecular-weight 11828 #checksum 7594 SEQUENCE /// ENTRY GDBO #type complete TITLE glutaredoxin - bovine ALTERNATE_NAMES thioltransferase ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 05-Dec-1997 ACCESSIONS A30164; S07229 REFERENCE A30164 !$#authors Papayannopoulos, I.A.; Gan, Z.R.; Wells, W.W.; Biemann, K. !$#journal Biochem. Biophys. Res. Commun. (1989) 159:1448-1454 !$#title A revised sequence of calf thymus glutaredoxin. !$#cross-references MUID:89193746; PMID:2930571 !$#accession A30164 !'##molecule_type protein !'##residues 1-105 ##label PAP !'##experimental_source calf thymus REFERENCE S07229 !$#authors Klintrot, I.M.; Hoeoeg, J.O.; Joernvall, H.; Holmgren, A.; !1Luthman, M. !$#journal Eur. J. Biochem. (1984) 144:417-423 !$#title The primary structure of calf thymus glutaredoxin. Homology !1with the corresponding Escherichia coli protein but !1elongation at both ends and with an additional half-cystine/ !1cysteine pair. !$#cross-references MUID:85027238; PMID:6386471 !$#accession S07229 !'##molecule_type protein !'##residues 'QA',3-67,72-105 ##label KLI COMMENT This enzyme catalyzes the reduction of a variety of !1disulfides, including protein disulfides, in the presence of !1reduced glutathione. CLASSIFICATION #superfamily glutaredoxin; glutaredoxin homology KEYWORDS acetylated amino end; deoxyribonucleotide biosynthesis; !1electron transfer; redox-active disulfide FEATURE !$4-98 #domain glutaredoxin homology #label GLUT\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$22-25 #disulfide_bonds redox-active #status predicted\ !$78-82 #disulfide_bonds #status predicted SUMMARY #length 105 #molecular-weight 11652 #checksum 4192 SEQUENCE /// ENTRY GDRB #type complete TITLE glutaredoxin - rabbit ALTERNATE_NAMES thioltransferase ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 05-Dec-1997 ACCESSIONS A32682 REFERENCE A32682 !$#authors Hopper, S.; Johnson, R.S.; Vath, J.E.; Biemann, K. !$#journal J. Biol. Chem. (1989) 264:20438-20447 !$#title Glutaredoxin from rabbit bone marrow. Purification, !1characterization, and amino acid sequence determined by !1tandem mass spectrometry. !$#cross-references MUID:90062176; PMID:2684977 !$#accession A32682 !'##molecule_type protein !'##residues 1-106 ##label HOP !'##experimental_source bone marrow COMMENT This enzyme catalyzes the reduction of a variety of !1disulfides, including protein disulfides, in the presence of !1reduced glutathione. CLASSIFICATION #superfamily glutaredoxin; glutaredoxin homology KEYWORDS acetylated amino end; deoxyribonucleotide biosynthesis; !1electron transfer; redox-active disulfide FEATURE !$4-98 #domain glutaredoxin homology #label GLUT\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$22-25 #disulfide_bonds redox-active #status predicted\ !$78-82 #disulfide_bonds #status predicted SUMMARY #length 106 #molecular-weight 11823 #checksum 6891 SEQUENCE /// ENTRY GDBY #type complete TITLE glutaredoxin - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YDR513w; thioltransferase ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Dec-1990 #sequence_revision 13-Mar-1997 #text_change 05-Nov-1999 ACCESSIONS S69570; JQ1612; A35492 REFERENCE S69553 !$#authors Dietrich, F.S. !$#submission submitted to the EMBL Data Library, August 1995 !$#description The sequence of S. cerevisiae cosmids 8166, 9787, 9717, and !1lambda 3073. !$#accession S69570 !'##molecule_type DNA !'##residues 1-143 ##label DIE !'##cross-references EMBL:U33057; NID:g927764; PIDN:AAB64953.1; !1PID:g927781; GSPDB:GN00004; MIPS:YDR513w REFERENCE JQ1612 !$#authors Gan, Z.R. !$#journal Biochem. Biophys. Res. Commun. (1992) 187:949-955 !$#title Cloning and sequencing of a gene encoding yeast !1thioltransferase. !$#cross-references MUID:92412147; PMID:1530649 !$#accession JQ1612 !'##molecule_type DNA !'##residues 35-143 ##label GAN !'##cross-references GB:S45268; NID:g256162; PIDN:AAB23389.1; !1PID:g256163 !'##experimental_source strain DMY6 REFERENCE A35492 !$#authors Gan, Z.R.; Polokoff, M.A.; Jacobs, J.W.; Sardana, M.K. !$#journal Biochem. Biophys. Res. Commun. (1990) 168:944-951 !$#title Complete amino acid sequence of yeast thioltransferase !1(glutaredoxin). !$#cross-references MUID:90267489; PMID:2189409 !$#accession A35492 !'##molecule_type protein !'##residues 36-141 ##label GA2 GENETICS !$#gene SGD:TTR1; GRX2; MIPS:YDR513w !'##cross-references SGD:S0002921; MIPS:YDR513w !$#map_position 4R FUNCTION !$#description thioltransferase catalyzes cellular thiol-disulfide !1transhydrogenation reactions CLASSIFICATION #superfamily glutaredoxin; glutaredoxin homology KEYWORDS acetylated amino end; cytosol; electron transfer; !1redox-active disulfide FEATURE !$36-141 #product glutaredoxin #status experimental #label !8MAT\ !$43-138 #domain glutaredoxin homology #label GLUT\ !$36 #modified_site acetylated amino end (Val) (in mature !8form) #status experimental\ !$61-64 #disulfide_bonds redox-active #status predicted SUMMARY #length 143 #molecular-weight 15861 #checksum 4942 SEQUENCE /// ENTRY S19363 #type complete TITLE glutaredoxin GRX1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YCL035c; thioltransferase ORGANISM #formal_name Saccharomyces cerevisiae DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 16-Jun-2000 ACCESSIONS S19363 REFERENCE S19350 !$#authors Hollenberg, C.P.; Kleinhans, U.; Lutzenkirchen, K.; Ramezani !1Rad, M.; Xu, G. !$#submission submitted to the Protein Sequence Database, March 1992 !$#accession S19363 !'##molecule_type DNA !'##residues 1-110 ##label HOL !'##cross-references EMBL:X59720; NID:g1907116; PIDN:CAA42381.1; !1PID:g5328; GSPDB:GN00003; MIPS:YCL035c GENETICS !$#gene GRX1 !'##cross-references SGD:S0000540; MIPS:YCL035c !$#map_position 3L FUNCTION !$#description thioltransferase catalyzes cellular thiol-disulfide !1transhydrogenation reactions; required for protection during !1oxidative stress CLASSIFICATION #superfamily glutaredoxin; glutaredoxin homology KEYWORDS electron transfer; redox-active disulfide FEATURE !$9-104 #domain glutaredoxin homology #label GLUT\ !$27-30 #disulfide_bonds redox-active #status predicted SUMMARY #length 110 #molecular-weight 12380 #checksum 3182 SEQUENCE /// ENTRY GDEC #type complete TITLE glutaredoxin 1 - Escherichia coli (strain K-12) ALTERNATE_NAMES thioltransferase ORGANISM #formal_name Escherichia coli DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 01-Mar-2002 ACCESSIONS A00283; A24397; I59418; A64823; A39568 REFERENCE A00283 !$#authors Hoeoeg, J.O.; Joernvall, H.; Holmgren, A.; Carlquist, M.; !1Persson, M. !$#journal Eur. J. Biochem. (1983) 136:223-232 !$#title The primary structure of Escherichia coli glutaredoxin. !1Distant homology with thioredoxins in a superfamily of small !1proteins with a redox-active cystine disulfide/cysteine !1dithiol. !$#cross-references MUID:84004402; PMID:6352262 !$#accession A00283 !'##molecule_type protein !'##residues 1-85 ##label HO1 !'##experimental_source K-12, strain C10-17 REFERENCE A24397 !$#authors Hoeoeg, J.O.; von Bahr-Lindstroem, H.; Joernvall, H.; !1Holmgren, A. !$#journal Gene (1986) 43:13-21 !$#title Cloning and expression of the glutaredoxin (grx) gene of !1Escherichia coli. !$#cross-references MUID:87005940; PMID:3530878 !$#accession A24397 !'##molecule_type DNA !'##residues 1-85 ##label HO2 !'##cross-references GB:M13449; NID:g146272; PIDN:AAA23936.1; !1PID:g146273 REFERENCE I59418 !$#authors Chatterjee, P.K.; Sternberg, N.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1995) 92:8950-8954 !$#title A general genetic approach in Escherichia coli for !1determining the mechanism(s) of action of tumoricidal !1agents: application to DMP 840, a tumoricidal agent. !$#cross-references MUID:96004656; PMID:7568050 !$#accession I59418 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-85 ##label RES !'##cross-references EMBL:U18655; NID:g609323; PIDN:AAC43449.1; !1PID:g609325 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64823 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-85 ##label BLAT !'##cross-references GB:AE000187; GB:U00096; NID:g1787070; !1PIDN:AAC73936.1; PID:g1787073; UWGP:b0849 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A39568 !$#authors Sandberg, V.A.; Kren, B.; Fuchs, J.A.; Woodward, C. !$#journal Biochemistry (1991) 30:5475-5484 !$#title Escherichia coli glutaredoxin: cloning and overexpression, !1thermodynamic stability of the oxidized and reduced forms, !1and report of an N-terminal extended species. !$#cross-references MUID:91242463; PMID:2036416 !$#accession A39568 !'##status preliminary !'##molecule_type DNA !'##residues 'MRREI',1-15 ##label SAN GENETICS !$#gene grxA; grx !$#map_position 19 min FUNCTION !$#description the disulfide bond functions as an electron carrier in the !1glutathione-dependent synthesis of deoxyribonucleotides from !1ribonucleotides by the enzyme ribonucleotide reductase; in !1addition, it is also involved in reducing some disulfides in !1a coupled system with glutathione reductase !$#pathway deoxyribonucleotide biosynthesis CLASSIFICATION #superfamily glutaredoxin; glutaredoxin homology KEYWORDS deoxyribonucleotide biosynthesis; electron transfer; !1monomer; redox-active disulfide FEATURE !$1-85 #domain glutaredoxin homology #label GLUT\ !$11-14 #disulfide_bonds redox-active #status experimental SUMMARY #length 85 #molecular-weight 9685 #checksum 4761 SEQUENCE /// ENTRY I64127 #type complete TITLE glutaredoxin - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS I64127 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession I64127 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-87 ##label TIGR !'##cross-references GB:U32829; GB:L42023; NID:g1574375; !1PIDN:AAC23182.1; PID:g1574376; TIGR:HI1532 !'##note named as homolog to a protein from Escherichia coli CLASSIFICATION #superfamily glutaredoxin; glutaredoxin homology KEYWORDS deoxyribonucleotide biosynthesis; electron transfer; !1redox-active disulfide FEATURE !$11-14 #disulfide_bonds redox-active #status predicted SUMMARY #length 87 #molecular-weight 9670 #checksum 8891 SEQUENCE /// ENTRY TXBPT4 #type complete TITLE thioredoxin [validated] - phage T4 ALTERNATE_NAMES glutaredoxin ORGANISM #formal_name phage T4 DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 15-Sep-2000 ACCESSIONS A00282; G30292 REFERENCE A92121 !$#authors Sjoberg, B.M.; Holmgren, A. !$#journal J. Biol. Chem. (1972) 247:8063-8068 !$#title Studies on the structure of T4 thioredoxin. II. Amino acid !1sequence of the protein and comparison with thioredoxin from !1Escherichia coli. !$#cross-references MUID:73061516; PMID:4565673 !$#accession A00282 !'##molecule_type protein !'##residues 1-87 ##label SJO REFERENCE A30291 !$#authors Tomaschewski, J.; Rueger, W. !$#journal Nucleic Acids Res. (1987) 15:3632-3633 !$#title Nucleotide sequence and primary structures of gene products !1coded for by the T4 genome between map positions 48.266 kb !1and 39.166 kb. !$#cross-references MUID:87203398; PMID:3575111 !$#accession G30292 !'##molecule_type DNA !'##residues 1-87 ##label TOM !'##cross-references GB:AF158101; NID:g5508842; PIDN:AAD42626.1; !1PID:g5354419 REFERENCE A51009 !$#authors Eklund, H.; Ingelman, M.; Soderberg, B.O.; Uhlin, T.; !1Nordlund, P.; Nikkola, M.; Sonnerstam, U.; Joelson, T.; !1Petratos, K. !$#submission submitted to the Brookhaven Protein Data Bank, April 1992 !$#cross-references PDB:1AAZ !$#contents annotation; X-ray crystallography, 2.0 angstroms, residues !11-87 REFERENCE A93825 !$#authors Soderberg, B.O.; Sjoberg, B.M.; Sonnerstam, U.; Branden, !1C.I. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1978) 75:5827-5830 !$#title Three-dimensional structure of thioredoxin induced by !1bacteriophage T4. !$#cross-references MUID:79096070; PMID:366603 !$#contents annotation; X-ray crystallography, 2.8 angstroms COMMENT The name thioredoxin, assigned to this protein before !1glutaredoxin was discovered, should probably be regarded as !1a misnomer. GENETICS !$#gene nrdC FUNCTION !$#description reduced by NADPH and thioredoxin reductase, and oxidized by !1ribonucleotide reductase !$#pathway deoxyribonucleotide biosynthesis !$#note oxidized T4 thioredoxin can be reduced by host thioredoxin !1reductase, but reduced T4 thioredoxin functions efficiently !1only with phage ribonucleotide reductase CLASSIFICATION #superfamily glutaredoxin; glutaredoxin homology KEYWORDS deoxyribonucleotide biosynthesis; electron transfer; !1redox-active disulfide FEATURE !$1-87 #domain glutaredoxin homology #status atypical #label !8GLUT\ !$14-17 #disulfide_bonds redox-active #status experimental SUMMARY #length 87 #molecular-weight 10050 #checksum 8585 SEQUENCE /// ENTRY E42510 #type complete TITLE glutaredoxin 1 - vaccinia virus (strains Copenhagen, Ankara and L-IVP) ALTERNATE_NAMES 12K protein; O2L protein ORGANISM #formal_name vaccinia virus #note host Homo sapiens (man) DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 18-Feb-2000 ACCESSIONS E42510; PN0120; T37337 REFERENCE A33172 !$#authors Johnson, G.P. !$#submission submitted to GenBank, June 1990 !$#accession E42510 !'##status preliminary !'##molecule_type DNA !'##residues 1-108 ##label JOH !'##cross-references GB:M35027; NID:g335317; PIDN:AAA48055.1; !1PID:g335403 !'##experimental_source strain Copenhagen, strain L-IVP REFERENCE PN0119 !$#authors Rjazankina, O.I.; Shchelkunov, S.N.; Muravlev, A.I.; !1Netesova, N.A.; Mikrjukov, N.N.; Gutorov, V.V.; Nikulin, !1A.E.; Kulichkov, V.A.; Malygin, E.G. !$#journal Mol. Biol. (Mosk.) (1990) 24:968-976 !$#title The molecular biological study of vaccinia virus genome II; !1localization and fine structure of the vaccinia virus genes !1encoding 36K and 12K polypeptides. !$#cross-references MUID:91066899; PMID:2250685 !$#accession PN0120 !'##molecule_type DNA !'##residues 1-108 ##label RJA !'##note strain L-IVP REFERENCE Z20877 !$#authors Antoine, G.; Scheiflinger, F.; Falkner, F.G.; Dorner, F. !$#submission submitted to the EMBL Data Library, March 1997 !$#description The complete genomic sequence of the Modified Vaccinia !1Ankara (MVA) strain. !$#accession T37337 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-108 ##label ANT !'##cross-references EMBL:U94848; PIDN:AAB96432.1 !'##experimental_source strain Ankara GENETICS !$#note MVA061L CLASSIFICATION #superfamily glutaredoxin; glutaredoxin homology KEYWORDS deoxyribonucleotide biosynthesis; electron transfer; !1redox-active disulfide FEATURE !$5-99 #domain glutaredoxin homology #label GLUT\ !$23-26 #disulfide_bonds redox-active #status predicted SUMMARY #length 108 #molecular-weight 12355 #checksum 3905 SEQUENCE /// ENTRY G36842 #type complete TITLE glutaredoxin - variola virus (strain India-1967) ALTERNATE_NAMES Q2L protein ORGANISM #formal_name variola virus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S33069; G36842 REFERENCE S33069 !$#authors Shchelkunov, S.N.; Blinov, V.M.; Totmenin, A.V.; !1Marennikova, S.S.; Kolykhalov, A.A.; Frolov, I.V.; !1Chizhikov, V.E.; Gytorov, V.V.; Gashikov, P.V.; Belanov, !1E.F.; Belavin, P.A.; Resenchuk, S.M.; Andzhaparidze, O.G.; !1Sandakhchiev, L.S. !$#journal Virus Res. (1993) 27:25-35 !$#title Nucleotide sequence analysis of variola virus HindIII M, L, !1I genome fragments. !$#cross-references MUID:93190624; PMID:8383392 !$#accession S33069 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-108 ##label SHC !'##cross-references EMBL:X67119; NID:g62330; PIDN:CAA47554.1; !1PID:g62331 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1992 REFERENCE A36859 !$#authors Blinov, V.M. !$#submission submitted to GenBank, November 1992 !$#accession G36842 !'##status preliminary !'##molecule_type DNA !'##residues 1-108 ##label BLI !'##cross-references GB:X69198; NID:g456758; PIDN:CAA48995.1; !1PID:g297235 CLASSIFICATION #superfamily glutaredoxin; glutaredoxin homology KEYWORDS deoxyribonucleotide biosynthesis; electron transfer; !1redox-active disulfide FEATURE !$5-99 #domain glutaredoxin homology #label GLUT\ !$23-26 #disulfide_bonds redox-active #status predicted SUMMARY #length 108 #molecular-weight 12349 #checksum 4041 SEQUENCE /// ENTRY S45869 #type complete TITLE glutaredoxin homolog YBR014c - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein YBR0219 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S45869 REFERENCE S45862 !$#authors Entian, K.D.; Koetter, P.; Rose, M.; Li, Z.; Thermann, R.; !1Brendel, M.; Baur, A.; Boles, E.; Miosga, T.; !1Schaaff-Gerstenschlaeger, I.; Zimmermann, F.K. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S45869 !'##molecule_type DNA !'##residues 1-203 ##label ENT !'##cross-references EMBL:Z35883; NID:g536211; PIDN:CAA84956.1; !1PID:g536212; GSPDB:GN00002; MIPS:YBR014c !'##experimental_source strain S288C GENETICS !$#gene MIPS:YBR014c !'##cross-references SGD:S0000218 !$#map_position 2R CLASSIFICATION #superfamily probable membrane protein YDL010W; glutaredoxin !1homology KEYWORDS transmembrane protein FEATURE !$8-30 #domain transmembrane #status predicted #label TMM\ !$91-184 #domain glutaredoxin homology #label GLUT SUMMARY #length 203 #molecular-weight 22565 #checksum 1134 SEQUENCE /// ENTRY S52509 #type complete TITLE probable membrane protein YDL010w - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein D2890 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S52509; S67542 REFERENCE S52492 !$#authors Andre, B.; Vissers, S.; Urrestarazu, L. !$#submission submitted to the EMBL Data Library, February 1995 !$#description The sequence of a 42 kb segment located on the left arm of !1chromosome IV from Saccharomyces cerevisiae. !$#accession S52509 !'##molecule_type DNA !'##residues 1-231 ##label AND !'##cross-references EMBL:Z48432; NID:g683669; PIDN:CAA88349.1; !1PID:g683687 !'##experimental_source strain S288C REFERENCE S67535 !$#authors Urrestarazu, L.A.; Andre, B.; Vissers, S. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67542 !'##molecule_type DNA !'##residues 1-231 ##label URR !'##cross-references EMBL:Z74059; NID:g1430970; PIDN:CAA98567.1; !1PID:g1430972; GSPDB:GN00004; MIPS:YDL010w !'##experimental_source strain S288C GENETICS !$#gene MIPS:YDL010w !'##cross-references SGD:S0002168 !$#map_position 4L CLASSIFICATION #superfamily probable membrane protein YDL010W; glutaredoxin !1homology KEYWORDS transmembrane protein FEATURE !$11-27 #domain transmembrane #status predicted #label TMM\ !$119-212 #domain glutaredoxin homology #label GLUT SUMMARY #length 231 #molecular-weight 25783 #checksum 3331 SEQUENCE /// ENTRY SSUL #type complete TITLE stellacyanin - Japanese lacquer-tree ORGANISM #formal_name Rhus vernicifera #common_name Japanese lacquer-tree DATE 31-May-1979 #sequence_revision 31-May-1979 #text_change 04-Nov-2002 ACCESSIONS A00311 REFERENCE A90206 !$#authors Bergman, C.; Gandvik, E.K.; Nyman, P.O.; Strid, L. !$#journal Biochem. Biophys. Res. Commun. (1977) 77:1052-1059 !$#title The amino acid sequence of stellacyanin from the lacquer !1tree. !$#cross-references MUID:77266668; PMID:901509 !$#accession A00311 !'##molecule_type protein !'##residues 1-107 ##label BER REFERENCE A90207 !$#authors Bergman, C.; Gandvik, E.K.; Nyman, P.O.; Strid, L. !$#journal Biochem. Biophys. Res. Commun. (1977) 79:1013 !$#contents annotation; erratum REFERENCE A91324 !$#authors Engeseth, H.R.; Hermodson, M.A.; McMillin, D.R. !$#journal FEBS Lett. (1984) 171:257-261 !$#title A new assignment of the disulfide linkage in stellacyanin. !$#cross-references MUID:84208877; PMID:6723985 !$#contents annotation; disulfide bond COMMENT This is a blue, type 1 copper glycoprotein. CLASSIFICATION #superfamily stellacyanin KEYWORDS copper; electron transfer; glycoprotein FEATURE !$28,60,102 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$46,87,92,97 #binding_site copper (His, Cys, His, Gln) #status !8predicted\ !$59-93 #disulfide_bonds #status experimental SUMMARY #length 107 #molecular-weight 12296 #checksum 7797 SEQUENCE /// ENTRY AZBR #type complete TITLE azurin - Bordetella bronchiseptica ORGANISM #formal_name Bordetella bronchiseptica DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 20-Apr-2000 ACCESSIONS A00284 REFERENCE A00284 !$#authors Ambler, R.P. !$#book Chemotaxonomy and Serotaxonomy, Hawkes, J.G., ed., pp.57-64, !1Academic Press, London, 1968 !$#title Species differences in the amino acid sequences of bacterial !1proteins. !$#accession A00284 !'##molecule_type protein !'##residues 1-129 ##label AMB !'##experimental_source strain NCTC 8344 CLASSIFICATION #superfamily plastocyanin KEYWORDS copper; electron transfer; metalloprotein FEATURE !$3-26 #disulfide_bonds #status predicted\ !$46,112,117,121 #binding_site copper (His, Cys, His, Met) (type 1) !8#status predicted SUMMARY #length 129 #molecular-weight 13838 #checksum 9583 SEQUENCE /// ENTRY AZALCX #type complete TITLE azurin - Alcaligenes sp. (tentative sequence) ORGANISM #formal_name Alcaligenes sp. DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 20-Apr-2000 ACCESSIONS A00285 REFERENCE A94436 !$#authors Ambler, R.P. !$#book Recent Developments in the Chemical Study of Protein !1Structures, pp.289-305, INSERM, Paris, 1971 !$#accession A00285 !'##molecule_type protein !'##residues 1-129 ##label AMB !'##note the author assigned the amides at positions 10, 14, and 47 by !1homology REFERENCE A94460 !$#authors Stanier, R.Y. !$#citation unpublished results, cited by Ambler, R.P., submitted to the !1Atlas, December 1972 !$#contents annotation !$#note this organism, previously called Pseudomonas denitrificans !1by some workers, was characterized as a species of !1Alcaligenes CLASSIFICATION #superfamily plastocyanin KEYWORDS copper; electron transfer; metalloprotein FEATURE !$3-26 #disulfide_bonds #status predicted\ !$46,112,117,121 #binding_site copper (His, Cys, His, Met) (type 1) !8#status predicted SUMMARY #length 129 #molecular-weight 13957 #checksum 9352 SEQUENCE /// ENTRY AZALCD #type complete TITLE azurin precursor [validated] - Alcaligenes denitrificans ORGANISM #formal_name Alcaligenes denitrificans DATE 24-Apr-1984 #sequence_revision 27-Jan-1995 #text_change 15-Sep-2000 ACCESSIONS JQ0643; A00286 REFERENCE JQ0643 !$#authors Hoitink, C.W.G.; Woudt, L.P.; Turenhout, J.C.M.; van de !1Kamp, M.; Canters, G.W. !$#journal Gene (1990) 90:15-20 !$#title Isolation and sequencing of the Alcaligenes denitrificans !1azurin-encoding gene: comparison with the genes encoding !1blue copper proteins from Pseudomonas aeruginosa and !1Alcaligenes faecalis. !$#cross-references MUID:90337337; PMID:2116366 !$#accession JQ0643 !'##molecule_type DNA !'##residues 1-149 ##label HOI !'##cross-references GB:M30388; NID:g141901; PIDN:AAA21954.1; !1PID:g141902 !'##experimental_source strain NCTC8582 REFERENCE A00088 !$#authors Ambler, R.P. !$#submission submitted to the Atlas, July 1974 !$#accession A00286 !'##molecule_type protein !'##residues 21-61,'AV',64-76,'E',78-149 ##label AMB !'##experimental_source NCIB 8582 REFERENCE A51034 !$#authors Baker, E.N.; Shepard, W.E.B.; Kingston, R.L. !$#submission submitted to the Brookhaven Protein Data Bank, December 1992 !$#cross-references PDB:1AZC !$#contents annotation; X-ray crystallography, 1.8 angstroms, reduced !1form, residues 21-149 REFERENCE A50403 !$#authors Baker, E.N.; Norris, G.E. !$#submission submitted to the Brookhaven Protein Data Bank, October 1986 !$#cross-references PDB:2AZA !$#contents annotation; X-ray crystallography, 1.8 angstroms, oxdized !1form, residues 21-15,'D',17-41,'S',43-76,'E',78-149 REFERENCE A58635 !$#authors Baker, E.N. !$#journal J. Mol. Biol. (1988) 203:1071-1095 !$#title Structure of azurin from Alcaligenes denitrificans !1refinement at 1.8 Angstroms resolution and comparison of the !1two crystallographically independent molecules. !$#cross-references MUID:89094855; PMID:3210236 !$#contents annotation; X-ray crystallography, 1.8 angstroms REFERENCE A92898 !$#authors Norris, G.E.; Anderson, B.F.; Baker, E.N. !$#journal J. Mol. Biol. (1983) 165:501-521 !$#title Structure of azurin from Alcaligenes denitrificans at 2.5 !1Angstrom resolution. !$#cross-references MUID:83189162; PMID:6842609 !$#contents annotation; X-ray crystallography, 2.5 angstroms COMMENT Azurin is thought to transfer electrons from cytochrome c551 !1to cytochrome oxidase. GENETICS !$#gene azu CLASSIFICATION #superfamily plastocyanin KEYWORDS copper; electron transfer; metalloprotein FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-149 #product azurin #status experimental #label MAT\ !$23-46 #disulfide_bonds #status experimental\ !$66,132,137,141 #binding_site copper (His, Cys, His, Met) (type 1) !8#status experimental SUMMARY #length 149 #molecular-weight 15924 #checksum 8001 SEQUENCE /// ENTRY A58648 #type complete TITLE azurin II [validated] - Alcaligenes denitrificans subsp. xylosoxydans ORGANISM #formal_name Alcaligenes denitrificans subsp. xylosoxydans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 15-Sep-2000 ACCESSIONS A58648 REFERENCE A65121 !$#authors Dodd, F.E.; Hasnain, S.S.; Abraham, Z.H.L.; Eady, R.R.; !1Smith, B.E. !$#submission submitted to the Brookhaven Protein Data Bank, March 1995 !$#cross-references PDB:1ARN !$#contents sequence; X-ray crystallography, 2.1 angstroms !$#accession A58648 !'##molecule_type protein !'##residues 1-129 ##label DOD !'##experimental_source NCIMB 11015 CLASSIFICATION #superfamily plastocyanin KEYWORDS copper; electron transfer; metalloprotein FEATURE !$3-26 #disulfide_bonds #status experimental\ !$46,112,117,121 #binding_site copper (His, Cys, His, Met) (type 1) !8#status experimental SUMMARY #length 129 #molecular-weight 13775 #checksum 8150 SEQUENCE /// ENTRY AZALCF #type complete TITLE azurin - Alcaligenes faecalis (tentative sequence) ORGANISM #formal_name Alcaligenes faecalis DATE 13-Jul-1981 #sequence_revision 13-Jul-1981 #text_change 20-Apr-2000 ACCESSIONS A00287 REFERENCE A94436 !$#authors Ambler, R.P. !$#book Recent Developments in the Chemical Study of Protein !1Structures, pp.289-305, INSERM, Paris, 1971 !$#accession A00287 !'##molecule_type protein !'##residues 1-128 ##label AMB !'##experimental_source NCIB 8156 !'##note the author assigned the amide at position 13 by homology CLASSIFICATION #superfamily plastocyanin KEYWORDS copper; electron transfer; metalloprotein FEATURE !$2-25 #disulfide_bonds #status predicted\ !$45,111,116,120 #binding_site copper (His, Cys, His, Met) (type 1) !8#status predicted SUMMARY #length 128 #molecular-weight 13693 #checksum 7458 SEQUENCE /// ENTRY AZPSCA #type complete TITLE azurin precursor [validated] - Pseudomonas aeruginosa ORGANISM #formal_name Pseudomonas aeruginosa DATE 24-Apr-1984 #sequence_revision 31-Mar-1993 #text_change 31-Dec-2000 ACCESSIONS JQ0644; S02268; A29339; A94436; H83030; A00288 REFERENCE JQ0643 !$#authors Hoitink, C.W.G.; Woudt, L.P.; Turenhout, J.C.M.; van de !1Kamp, M.; Canters, G.W. !$#journal Gene (1990) 90:15-20 !$#title Isolation and sequencing of the Alcaligenes denitrificans !1azurin-encoding gene: comparison with the genes encoding !1blue copper proteins from Pseudomonas aeruginosa and !1Alcaligenes faecalis. !$#cross-references MUID:90337337; PMID:2116366 !$#accession JQ0644 !'##molecule_type DNA !'##residues 1-148 ##label HOI !'##cross-references GB:M30389; NID:g151060; PIDN:AAA25730.1; !1PID:g151062 REFERENCE S02268 !$#authors Arvidsson, R.H.A.; Nordling, M.; Lundberg, L.G. !$#journal Eur. J. Biochem. (1989) 179:195-200 !$#title The azurin gene from Pseudomonas aeruginosa. Cloning and !1characterization. !$#cross-references MUID:89137081; PMID:2537198 !$#accession S02268 !'##molecule_type DNA !'##residues 1-148 ##label ARV !'##cross-references EMBL:X07317; NID:g45291; PIDN:CAA30279.1; !1PID:g45292 REFERENCE A29339 !$#authors Canters, G.W. !$#journal FEBS Lett. (1987) 212:168-172 !$#title The azurin gene from Pseudomonas aeruginosa codes for a !1pre-protein with a signal peptide. Cloning and sequencing of !1the azurin gene. !$#cross-references MUID:87105995; PMID:3100334 !$#accession A29339 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-148 ##label CAN REFERENCE A94436 !$#authors Ambler, R.P. !$#book Recent Developments in the Chemical Study of Protein !1Structures, pp.289-305, INSERM, Paris, 1971 !$#accession A94436 !'##molecule_type protein !'##residues 21-148 ##label AMB !'##experimental_source strain P6009 REFERENCE A52133 !$#authors Nar, H.; Messerschmidt, A.; Huber, R. !$#submission submitted to the Brookhaven Protein Data Bank, June 1993 !$#cross-references PDB:4AZU !$#contents annotation; X-ray crystallography, 1.9 angstroms, pH 5.5, !1residues 21-148 REFERENCE A52138 !$#authors Nar, H.; Messerschmidt, A.; Huber, R. !$#submission submitted to the Brookhaven Protein Data Bank, June 1993 !$#cross-references PDB:5AZU !$#contents annotation; X-ray crystallography, 1.9 angstroms, pH 9.0, !1residues 21-148 REFERENCE A58636 !$#authors Nar, H.; Messerschmidt, A.; Huber, R.; van de Kamp, M.; !1Canters, G.W. !$#journal J. Mol. Biol. (1991) 221:765-772 !$#title Crystal structure analysis of oxidized Pseudomonas !1aeruginosa azurin at pH 5.5 and pH 9.0. A pH-induced !1conformational transition involves a peptide bond flip. !$#cross-references MUID:92046032; PMID:1942029 !$#contents annotation; X-ray crystallography, 1.93 angstroms REFERENCE A50075 !$#authors Adman, E.T.; Sieker, L.C.; Jensen, L.H. !$#submission submitted to the Brookhaven Protein Data Bank, August 1980 !$#cross-references PDB:1AZU !$#contents annotation; X-ray crystallography, 2.7 angstroms, residues !123-148 REFERENCE A38858 !$#authors Adman, E.T.; Stenkamp, R.E.; Sieker, L.C.; Jensen, L.H. !$#journal J. Mol. Biol. (1978) 123:35-47 !$#title A crystallographic model for azurin at 3 angstrom !1resolution. !$#cross-references MUID:78244655; PMID:98639 !$#contents annotation; X-ray crystallography, 3.0 angstroms REFERENCE A82950 !$#authors Stover, C.K.; Pham, X.Q.; Erwin, A.L.; Mizoguchi, S.D.; !1Warrener, P.; Hickey, M.J.; Brinkman, F.S.L.; Hufnagle, !1W.O.; Kowalik, D.J.; Lagrou, M.; Garber, R.L.; Goltry, L.; !1Tolentino, E.; Westbrook-Wadman, S.; Yuan, Y.; Brody, L.L.; !1Coulter, S.N.; Folger, K.R.; Kas, A.; Larbig, K.; Lim, R.M.; !1Smith, K.A.; Spencer, D.H.; Wong, G.K.S.; Wu, Z.; Paulsen, !1I.T.; Reizer, J.; Saier, M.H.; Hancock, R.E.W.; Lory, S.; !1Olson, M.V. !$#journal Nature (2000) 406:959-964 !$#title Complete genome sequence of Pseudomonas aeruginosa PA01, an !1opportunistic pathogen. !$#cross-references MUID:20437337; PMID:10984043 !$#accession H83030 !'##status preliminary !'##molecule_type DNA !'##residues 1-148 ##label STO !'##cross-references GB:AE004905; GB:AE004091; NID:g9951195; !1PIDN:AAG08307.1; GSPDB:GN00131; PASP:PA4922 !'##experimental_source strain PAO1 GENETICS !$#gene azu; PA4922 CLASSIFICATION #superfamily plastocyanin KEYWORDS copper; electron transfer; metalloprotein FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-148 #product azurin #status experimental #label MAT\ !$23-46 #disulfide_bonds #status experimental\ !$66,132,137,141 #binding_site copper (His, Cys, His, Met) (type 1) !8#status experimental SUMMARY #length 148 #molecular-weight 16008 #checksum 6039 SEQUENCE /// ENTRY AZPSCD #type complete TITLE azurin - Pseudomonas sp. (tentative sequence) ORGANISM #formal_name Pseudomonas sp. DATE 13-Jul-1981 #sequence_revision 13-Jul-1981 #text_change 20-Apr-2000 ACCESSIONS A00289 REFERENCE A94436 !$#authors Ambler, R.P. !$#book Recent Developments in the Chemical Study of Protein !1Structures, pp.289-305, INSERM, Paris, 1971 !$#accession A00289 !'##molecule_type protein !'##residues 1-128 ##label AMB !'##experimental_source ATCC 13867, NCIB 9496 !'##note the author assigned the amide and acid at positions 57 and 62 !1by homology CLASSIFICATION #superfamily plastocyanin KEYWORDS copper; electron transfer; metalloprotein FEATURE !$3-26 #disulfide_bonds #status predicted\ !$46,112,117,121 #binding_site copper (His, Cys, His, Met) (type 1) !8#status predicted SUMMARY #length 128 #molecular-weight 13620 #checksum 8211 SEQUENCE /// ENTRY AZPSBF #type complete TITLE azurin - Pseudomonas fluorescens (biotype B) (tentative sequence) ORGANISM #formal_name Pseudomonas fluorescens DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 20-Apr-2000 ACCESSIONS A00290 REFERENCE A94436 !$#authors Ambler, R.P. !$#book Recent Developments in the Chemical Study of Protein !1Structures, pp.289-305, INSERM, Paris, 1971 !$#accession A00290 !'##molecule_type protein !'##residues 1-128 ##label AMB !'##experimental_source Stanier B-93; ATCC 17467 !'##note the author assigned the amides and acid at positions 11, 12, !1and 57 by homology CLASSIFICATION #superfamily plastocyanin KEYWORDS copper; electron transfer; metalloprotein FEATURE !$3-26 #disulfide_bonds #status predicted\ !$46,112,117,121 #binding_site copper (His, Cys, His, Met) (type 1) !8#status predicted SUMMARY #length 128 #molecular-weight 13799 #checksum 7421 SEQUENCE /// ENTRY AZPSCF #type complete TITLE azurin - Pseudomonas fluorescens (biotype C) (tentative sequence) ORGANISM #formal_name Pseudomonas fluorescens DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 20-Apr-2000 ACCESSIONS A00291 REFERENCE A94436 !$#authors Ambler, R.P. !$#book Recent Developments in the Chemical Study of Protein !1Structures, pp.289-305, INSERM, Paris, 1971 !$#accession A00291 !'##molecule_type protein !'##residues 1-128 ##label AMB !'##experimental_source Stanier C-18; ATCC 17400 !'##note the author assigned the amide and acids at positions 8, 11, 12, !1and 55 by homology CLASSIFICATION #superfamily plastocyanin KEYWORDS copper; electron transfer; metalloprotein FEATURE !$3-26 #disulfide_bonds #status predicted\ !$46,112,117,121 #binding_site copper (His, Cys, His, Met) (type 1) !8#status predicted SUMMARY #length 128 #molecular-weight 13953 #checksum 8595 SEQUENCE /// ENTRY AZPSDF #type complete TITLE azurin - Pseudomonas fluorescens (biotype D) (tentative sequence) ORGANISM #formal_name Pseudomonas fluorescens DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 20-Apr-2000 ACCESSIONS A00292 REFERENCE A94436 !$#authors Ambler, R.P. !$#book Recent Developments in the Chemical Study of Protein !1Structures, pp.289-305, INSERM, Paris, 1971 !$#accession A00292 !'##molecule_type protein !'##residues 1-128 ##label AMB !'##experimental_source Stanier D-35; ATCC 17414 CLASSIFICATION #superfamily plastocyanin KEYWORDS copper; electron transfer; metalloprotein FEATURE !$3-26 #disulfide_bonds #status predicted\ !$46,112,117,121 #binding_site copper (His, Cys, His, Met) (type 1) !8#status predicted SUMMARY #length 128 #molecular-weight 13743 #checksum 9491 SEQUENCE /// ENTRY AZNHM #type complete TITLE azurin precursor - Neisseria meningitidis ALTERNATE_NAMES H.8 antigen; outer membrane protein H.8 ORGANISM #formal_name Neisseria meningitidis DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 20-Apr-2000 ACCESSIONS S03752 REFERENCE S03752 !$#authors Kawula, T.H.; Spinola, S.M.; Klapper, D.G.; Cannon, J.G. !$#journal Mol. Microbiol. (1987) 1:179-185 !$#title Localization of a conserved epitope and an azurin-like !1domain in the H.8 protein of pathogenic Neisseria. !$#cross-references MUID:88216161; PMID:2452958 !$#accession S03752 !'##molecule_type DNA !'##residues 1-183 ##label KAW !'##cross-references EMBL:Y00530; NID:g45041; PIDN:CAA68589.1; !1PID:g45042 CLASSIFICATION #superfamily plastocyanin KEYWORDS blocked amino end; copper; electron transfer; lipoprotein; !1metalloprotein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-183 #product azurin #status predicted #label MAT\ !$22-56 #region alanine/proline-rich\ !$18 #modified_site fatty acylated amino end (Cys) (in !8mature form) #status predicted\ !$18 #binding_site sn-2,3-diacylglycerol (Cys) (covalent) !8#status predicted\ !$59-82 #disulfide_bonds #status predicted\ !$102,166,171,175 #binding_site copper (His, Cys, His, Met) (type 1) !8#status predicted SUMMARY #length 183 #molecular-weight 18546 #checksum 7330 SEQUENCE /// ENTRY AZNHG #type complete TITLE azurin precursor - Neisseria gonorrhoeae ALTERNATE_NAMES H.8 antigen; outer membrane protein H.8 ORGANISM #formal_name Neisseria gonorrhoeae DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 20-Apr-2000 ACCESSIONS S06374 REFERENCE S06374 !$#authors Gotschlich, E.C.; Seiff, M.E. !$#journal FEMS Microbiol. Lett. (1987) 43:253-255 !$#title Identification and gene structure of an azurin-like protein !1with a lipoprotein signal peptide in Neisseria gonorrhoeae. !$#accession S06374 !'##molecule_type DNA !'##residues 1-183 ##label GOT !'##cross-references EMBL:X06208; NID:g44841; PIDN:CAA29561.1; !1PID:g44842 CLASSIFICATION #superfamily plastocyanin KEYWORDS blocked amino end; copper; electron transfer; lipoprotein; !1metalloprotein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-183 #product azurin #status predicted #label MAT\ !$22-56 #region alanine/proline-rich\ !$18 #modified_site fatty acylated amino end (Cys) (in !8mature form) #status predicted\ !$18 #binding_site sn-2,3-diacylglycerol (Cys) (covalent) !8#status predicted\ !$59-82 #disulfide_bonds #status predicted\ !$102,166,171,175 #binding_site copper (His, Cys, His, Met) (type 1) !8#status predicted SUMMARY #length 183 #molecular-weight 18532 #checksum 7528 SEQUENCE /// ENTRY A23706 #type complete TITLE amicyanin - Thiobacillus versutus ALTERNATE_NAMES amine dehydrogenase amicyanin component ORGANISM #formal_name Thiobacillus versutus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S19732; A23706 REFERENCE S19730 !$#authors Ubbink, M.; van Kleef, M.A.G.; Kleinjan, D.J.; Hoitink, !1C.W.G.; Huitema, F.; Beintema, J.J.; Duine, J.A.; Canters, !1G.W. !$#journal Eur. J. Biochem. (1991) 202:1003-1012 !$#title Cloning, sequencing and expression studies of the genes !1encoding amicyanin and the beta-subunit of methylamine !1dehydrogenase from Thiobacillus versutus. !$#cross-references MUID:92111471; PMID:1765062 !$#accession S19732 !'##status preliminary !'##molecule_type DNA !'##residues 1-132 ##label UBB !'##cross-references GB:M58001; NID:g154632; PIDN:AAA50571.1; !1PID:g154635 REFERENCE A23706 !$#authors Van Beeumen, J.; Van Bun, S.; Canters, G.W.; Lommen, A.; !1Chothia, C. !$#journal J. Biol. Chem. (1991) 266:4869-4877 !$#title The structural homology of amicyanin from Thiobacillus !1versutus to plant plastocyanins. !$#cross-references MUID:91161570; PMID:2002033 !$#accession A23706 !'##status preliminary !'##molecule_type protein !'##residues 28-132 ##label VAN CLASSIFICATION #superfamily plastocyanin KEYWORDS copper; electron transfer; metalloprotein FEATURE !$80,119,122,125 #binding_site copper (His, Cys, His, Met) (type 1) !8#status predicted SUMMARY #length 132 #molecular-weight 14258 #checksum 949 SEQUENCE /// ENTRY S12972 #type complete TITLE amicyanin - Paracoccus denitrificans ORGANISM #formal_name Paracoccus denitrificans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 20-Apr-2000 ACCESSIONS S12972 REFERENCE S12971 !$#authors van Spanning, R.J.M.; Wansell, C.W.; Reijnders, W.N.M.; !1Oltmann, L.F.; Stouthamer, A.H. !$#journal FEBS Lett. (1990) 275:217-220 !$#title Mutagenesis of the gene encoding amicyanin of Paracoccus !1denitrificans and the resultant effect on methylamine !1oxidation. !$#cross-references MUID:91085564; PMID:2261991 !$#accession S12972 !'##status preliminary !'##molecule_type DNA !'##residues 1-131 ##label SPA !'##cross-references EMBL:X55665; NID:g45458; PIDN:CAA39199.1; !1PID:g45460 CLASSIFICATION #superfamily plastocyanin KEYWORDS copper; electron transfer; metalloprotein FEATURE !$79,118,121,124 #binding_site copper (His, Cys, His, Met) (type 1) !8#status experimental SUMMARY #length 131 #molecular-weight 13983 #checksum 8737 SEQUENCE /// ENTRY CUPSZM #type complete TITLE pseudoazurin [validated] - Methylobacterium extorquens ORGANISM #formal_name Methylobacterium extorquens DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 15-Sep-2000 ACCESSIONS A00293 REFERENCE A90327 !$#authors Ambler, R.P.; Tobari, J. !$#journal Biochem. J. (1985) 232:451-457 !$#title The primary structures of Pseudomonas AM1 amicyanin and !1pseudoazurin. Two new sequence classes of blue copper !1proteins. !$#cross-references MUID:86130354; PMID:4091802 !$#accession A00293 !'##molecule_type protein !'##residues 1-123 ##label AMB !'##experimental_source AM1, NCIB 9133 REFERENCE A52410 !$#authors Inoue, T.; Kai, Y.; Harada, S.; Kasai, N.; Ohshiro, Y.; !1Suzuki, S.; Kohzuma, T.; Tobari, J. !$#submission submitted to the Brookhaven Protein Data Bank, January 1994 !$#cross-references PDB:1PMY !$#contents annotation; X-ray crystallography, 1.5 angstroms, residues !11-123 COMMENT This species of Pseudomonas, isolated as an airborne !1contaminant, uses compounds such as methanol, methylamine, !1and formate as the sole carbon and energy source; it is !1quite distinct from the true pseudomonads as well as !1methylotrophs. CLASSIFICATION #superfamily plastocyanin KEYWORDS copper; electron transfer; metalloprotein FEATURE !$40,78,81,86 #binding_site copper (His, Cys, His, Met) (type 1) !8#status experimental SUMMARY #length 123 #molecular-weight 13392 #checksum 4247 SEQUENCE /// ENTRY CUALBF #type complete TITLE blue copper protein precursor - Alcaligenes faecalis ALTERNATE_NAMES cupredoxin; pseudoazurin ORGANISM #formal_name Alcaligenes faecalis DATE 17-Mar-1987 #sequence_revision 27-Jan-1995 #text_change 20-Apr-2000 ACCESSIONS A28385; A00294 REFERENCE A28385 !$#authors Yamamoto, K.; Uozumi, T.; Beppu, T. !$#journal J. Bacteriol. (1987) 169:5648-5652 !$#title The blue copper protein gene of Alcaligenes faecalis S-6 !1directs secretion of blue copper protein from Escherichia !1coli cells. !$#cross-references MUID:88058779; PMID:2824441 !$#accession A28385 !'##molecule_type DNA !'##residues 1-146 ##label YAM !'##cross-references GB:M18267; NID:g141903; PIDN:AAA21955.1; !1PID:g141904 !'##note strain S-6 REFERENCE A00294 !$#authors Hormel, S.; Adman, E.; Walsh, K.A.; Beppu, T.; Titani, K. !$#journal FEBS Lett. (1986) 197:301-304 !$#title The amino acid sequence of the blue copper protein of !1Alcaligenes faecalis. !$#cross-references MUID:86136586; PMID:3512305 !$#accession A00294 !'##molecule_type protein !'##residues 24-146 ##label HOR REFERENCE A27039 !$#authors Petratos, K.; Banner, D.W.; Beppu, T.; Wilson, K.S.; !1Tsernoglou, D. !$#journal FEBS Lett. (1987) 218:209-214 !$#title The crystal structure of pseudoazurin from Alcaligenes !1faecalis S-6 determined at 2.9 angstroms resolution. !$#cross-references MUID:87247273; PMID:3595868 !$#contents annotation !$#note strain S-6 REFERENCE A44676 !$#authors Adman, E.T.; Turley, S.; Bramson, R.; Petratos, K.; Banner, !1D.; Tsernoglou, D.; Beppu, T.; Watanabe, H. !$#journal J. Biol. Chem. (1989) 264:87-99 !$#title A 2.0-angstrom structure of the blue copper protein !1(cupredoxin) from Alcaligenes faecalis S-6. !$#cross-references MUID:89079731; PMID:2909547 !$#contents annotation !$#note strain S-6 COMMENT This soluble electron transfer copper protein, required for !1the inactivation of copper-containing nitrite reductase in !1the presence of oxygen, belongs to a class of blue proteins !1that includes pseudoazurin and amicyanin. CLASSIFICATION #superfamily plastocyanin KEYWORDS copper; electron transfer; metalloprotein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-146 #product blue copper protein #status experimental !8#label MAT\ !$63,101,104,109 #binding_site copper (His, Cys, His, Met) (type 1) !8#status experimental SUMMARY #length 146 #molecular-weight 15647 #checksum 7728 SEQUENCE /// ENTRY JC4649 #type complete TITLE pseudoazurin precursor [validated] - Achromobacter cycloclastes ALTERNATE_NAMES blue copper protein ORGANISM #formal_name Achromobacter cycloclastes DATE 10-May-1996 #sequence_revision 10-Oct-1997 #text_change 15-Sep-2000 ACCESSIONS JC4649; A27039 REFERENCE JC4648 !$#authors Chen, J.Y.; Chang, W.C.; Chang, T.; Chang, W.C.; Liu, M.Y.; !1Payne, W.J.; LeGall, J. !$#journal Biochem. Biophys. Res. Commun. (1996) 219:423-428 !$#title Cloning, characterization, and expression of the nitric !1oxide-generating nitrite reductase and of the blue copper !1protein genes of Achromobacter cycloclastes. !$#cross-references MUID:96193667; PMID:8605003 !$#accession JC4649 !'##molecule_type DNA !'##residues 1-148 ##label CHE !'##cross-references EMBL:Z48669; NID:g1125636; PID:g1125637 !'##experimental_source IAM1013 REFERENCE A27039 !$#authors Petratos, K.; Banner, D.W.; Beppu, T.; Wilson, K.S.; !1Tsernoglou, D. !$#journal FEBS Lett. (1987) 218:209-214 !$#title The crystal structure of pseudoazurin from Alcaligenes !1faecalis S-6 determined at 2.9 angstroms resolution. !$#cross-references MUID:87247273; PMID:3595868 !$#accession A27039 !'##molecule_type protein !'##residues 25-114,'E',116-148 ##label PET !'##note the source may be Vibrio alginolyticus REFERENCE A67029 !$#authors Inoue, T.; Nishio, N.; Hamanaka, S.; Shimomura, T.; Harada, !1S.; Suzuki, S.; Kohzuma, T.; Shidara, S.; Iwasaki, H.; Kai, !1Y. !$#submission submitted to the Brookhaven Protein Data Bank, April 1996 !$#cross-references PDB:1ZIA !$#contents annotation; X-ray crystallography, 1.54 angstroms, oxidized !1form, residues 25-148 REFERENCE A67030 !$#authors Inoue, T.; Nishio, N.; Hamanaka, S.; Shimomura, T.; Harada, !1S.; Suzuki, S.; Kohzuma, T.; Shidara, S.; Iwasaki, H.; Kai, !1Y. !$#submission submitted to the Brookhaven Protein Data Bank, April 1996 !$#cross-references PDB:1ZIB !$#contents annotation; X-ray crystallography, 2.0 angstroms, reduced !1form, residues 25-148 GENETICS !$#gene bcp FUNCTION !$#description transfers electrons to nitrite reductase CLASSIFICATION #superfamily plastocyanin KEYWORDS copper; electron transfer; metalloprotein FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-148 #product blue copper protein #status experimental !8#label MAT\ !$64,102,105,110 #binding_site copper (His, Cys, His, Met) (type 1) !8#status experimental SUMMARY #length 148 #molecular-weight 15271 #checksum 3697 SEQUENCE /// ENTRY CUPSAM #type complete TITLE amicyanin precursor - Methylobacterium extorquens (strain AM1) ORGANISM #formal_name Methylobacterium extorquens DATE 04-Dec-1986 #sequence_revision 21-Jul-1995 #text_change 20-Apr-2000 ACCESSIONS A56621; A00295 REFERENCE A56621 !$#authors Chistoserdov, A.Y.; Tsygankov, Y.D.; Lidstrom, M.E. !$#journal DNA Seq. (1991) 2:53-55 !$#title Nucleotide sequence of the amicyanin gene from !1Methylobacterium extorquens AM1. !$#cross-references MUID:92199244; PMID:1802036 !$#accession A56621 !'##molecule_type DNA !'##residues 1-119 ##label CHI !'##cross-references GB:M57963; NID:g150014; PIDN:AAA68895.1; !1PID:g150016 !'##note sequence modified after extraction from NCBI backbone !'##note the authors translated the codon CAC for residue 70 as Asn !'##note sequence extracted from NCBI backbone (NCBIN:89409, !1NCBIP:89412) REFERENCE A90327 !$#authors Ambler, R.P.; Tobari, J. !$#journal Biochem. J. (1985) 232:451-457 !$#title The primary structures of Pseudomonas AM1 amicyanin and !1pseudoazurin. Two new sequence classes of blue copper !1proteins. !$#cross-references MUID:86130354; PMID:4091802 !$#accession A00295 !'##molecule_type protein !'##residues 21-119 ##label AMB COMMENT This species of Pseudomonas, isolated as an airborne !1contaminant, uses compounds such as methanol, methylamine, !1and formate as the sole carbon and energy source; it is !1quite distinct from the true pseudomonads as well as !1methylotrophs. CLASSIFICATION #superfamily plastocyanin KEYWORDS copper; electron transfer; metalloprotein; periplasmic space FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-119 #product amicyanin #status experimental #label MAT\ !$67,106,109,112 #binding_site copper (His, Cys, His, Met) (type 1) !8#status predicted SUMMARY #length 119 #molecular-weight 12609 #checksum 1650 SEQUENCE /// ENTRY CUAI #type complete TITLE plastocyanin - Anabaena variabilis ORGANISM #formal_name Anabaena variabilis DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 20-Feb-1998 ACCESSIONS A00296 REFERENCE A00296 !$#authors Aitken, A. !$#journal Biochem. J. (1975) 149:675-683 !$#title Prokaryote-eukaryote relationships and the amino acid !1sequence of plastocyanin from Anabaena variabilis. !$#cross-references MUID:76087796; PMID:812489 !$#accession A00296 !'##molecule_type protein !'##residues 1-105 ##label AIT CLASSIFICATION #superfamily plastocyanin KEYWORDS copper; electron transfer; metalloprotein FEATURE !$39,89,92,97 #binding_site copper (His, Cys, His, Met) (type 1) !8#status predicted SUMMARY #length 105 #molecular-weight 11104 #checksum 2427 SEQUENCE /// ENTRY CUFB #type complete TITLE plastocyanin [validated] - kidney bean ORGANISM #formal_name Phaseolus vulgaris #common_name kidney bean DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 26-May-2000 ACCESSIONS A00297; S01778 REFERENCE A00297 !$#authors Milne, P.R.; Wells, J.R.E.; Ambler, R.P. !$#journal Biochem. J. (1974) 143:691-701 !$#title The amino acid sequence of plastocyanin from French bean !1(Phaseolus vulgaris). !$#cross-references MUID:75183337; PMID:4462751 !$#accession A00297 !'##molecule_type protein !'##residues 1-99 ##label MIL !'##note the source is designated as Phaseolus vulgaris (French bean) REFERENCE S01778 !$#authors Chazin, W.J.; Wright, P.E. !$#journal J. Mol. Biol. (1988) 202:623-636 !$#title Complete assignment of the H(1) nuclear magnetic resonance !1spectrum of french bean plastocyanin. Sequential resonance !1assignments, secondary structure and global fold. !$#cross-references MUID:89011985; PMID:3172230 !$#accession S01778 !'##molecule_type protein !'##residues 1-99 ##label CHA REFERENCE A51567 !$#authors Moore, J.M.; Lepre, C.A.; Gippert, G.P.; Chazin, W.J.; Case, !1D.A.; Wright, P.E. !$#submission submitted to the Brookhaven Protein Data Bank, March 1991 !$#cross-references PDB:9PCY !$#contents annotation; conformation by (1)H-NMR, residues 1-99 REFERENCE A58729 !$#authors Moore, J.M.; Lepre, C.A.; Gippert, G.P.; Chazin, W.J.; Case, !1D.A.; Wright, P.E. !$#journal J. Mol. Biol. (1991) 221:533-555 !$#title High-resolution solution structure of reduced French bean !1plastocyanin and comparison with the crystal structure of !1poplar plastocyanin. !$#cross-references MUID:92015245; PMID:1920431 !$#contents annotation; conformation by (1)H-NMR FUNCTION !$#description functions as electron carrier [validated, MUID:92015245] CLASSIFICATION #superfamily plastocyanin KEYWORDS chloroplast; copper; electron transfer; metalloprotein FEATURE !$37,84,87,92 #binding_site copper (His, Cys, His, Met) (type 1) !8#status experimental SUMMARY #length 99 #molecular-weight 10492 #checksum 4830 SEQUENCE /// ENTRY CUSP #type complete TITLE plastocyanin precursor - spinach ORGANISM #formal_name Spinacia oleracea #common_name spinach DATE 24-Apr-1984 #sequence_revision 12-Apr-1996 #text_change 11-Jun-1999 ACCESSIONS S00446; A00299 REFERENCE S00446 !$#authors Rother, C.; Jansen, T.; Tyagi, A.; Tittgen, J.; Herrmann, !1R.G. !$#journal Curr. Genet. (1986) 11:171-176 !$#title Plastocyanin is encoded by an uninterrupted nuclear gene in !1spinach. !$#cross-references MUID:88194671; PMID:2834087 !$#accession S00446 !'##molecule_type DNA !'##residues 1-168 ##label ROT !'##cross-references EMBL:X04693; NID:g21266; PIDN:CAA28398.1; !1PID:g21267 REFERENCE A00299 !$#authors Scawen, M.D.; Ramshaw, J.A.M.; Boulter, D. !$#journal Biochem. J. (1975) 147:343-349 !$#title The amino acid sequence of plastocyanin from spinach !1(Spinacia oleracea L.). !$#cross-references MUID:76039448; PMID:1180895 !$#accession A00299 !'##molecule_type protein !'##residues 70-168 ##label SCA CLASSIFICATION #superfamily plastocyanin KEYWORDS chloroplast; copper; electron transfer; metalloprotein FEATURE !$1-69 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$70-168 #product plastocyanin #status predicted #label MAT\ !$106,153,156,161 #binding_site copper (His, Cys, His, Met) (type 1) !8#status predicted SUMMARY #length 168 #molecular-weight 16917 #checksum 4545 SEQUENCE /// ENTRY CULC #type complete TITLE plastocyanin - garden lettuce ORGANISM #formal_name Lactuca sativa #common_name garden lettuce DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 20-Feb-1998 ACCESSIONS A00300 REFERENCE A00300 !$#authors Ramshaw, J.A.M.; Scawen, M.D.; Jones, E.A.; Brown, R.H.; !1Boulter, D. !$#journal Phytochemistry (1976) 15:1199-1202 !$#title The amino acid sequence of plastocyanin from Lactuca sativa !1(lettuce). !$#accession A00300 !'##molecule_type protein !'##residues 1-99 ##label RAM CLASSIFICATION #superfamily plastocyanin KEYWORDS chloroplast; copper; electron transfer; metalloprotein FEATURE !$37,84,87,92 #binding_site copper (His, Cys, His, Met) (type 1) !8#status predicted SUMMARY #length 99 #molecular-weight 10359 #checksum 3513 SEQUENCE /// ENTRY CUED #type complete TITLE plastocyanin - European elder ORGANISM #formal_name Sambucus nigra #common_name European elder DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 20-Feb-1998 ACCESSIONS A00301 REFERENCE A00301 !$#authors Scawen, M.D.; Ramshaw, J.A.M.; Brown, R.H.; Boulter, D. !$#journal Eur. J. Biochem. (1974) 44:299-303 !$#title The amino-acid sequence of plastocyanin from Sambucus nigra !1L. (elder). !$#cross-references MUID:74308155; PMID:4854645 !$#accession A00301 !'##molecule_type protein !'##residues 1-99 ##label SCA !'##note position 15 is Ile in 60% and Val in 40% of the chains !'##note 17-Ser and 17-Gly are found in approximately equal amounts CLASSIFICATION #superfamily plastocyanin KEYWORDS chloroplast; copper; electron transfer; metalloprotein FEATURE !$37,84,87,92 #binding_site copper (His, Cys, His, Met) (type 1) !8#status predicted SUMMARY #length 99 #molecular-weight 10461 #checksum 5549 SEQUENCE /// ENTRY CUVM #type complete TITLE plastocyanin - field pumpkin ORGANISM #formal_name Cucurbita pepo var. pepo #common_name field pumpkin, vegetable marrow DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 20-Feb-1998 ACCESSIONS A00302 REFERENCE A00302 !$#authors Scawen, M.D.; Boulter, D. !$#journal Biochem. J. (1974) 143:257-264 !$#title The amino acid sequence of plastocyanin from Cucurbita pepo !1L. (vegetable marrow). !$#cross-references MUID:75183285; PMID:4462555 !$#accession A00302 !'##molecule_type protein !'##residues 1-99 ##label SCA CLASSIFICATION #superfamily plastocyanin KEYWORDS chloroplast; copper; electron transfer; metalloprotein FEATURE !$37,84,87,92 #binding_site copper (His, Cys, His, Met) (type 1) !8#status predicted SUMMARY #length 99 #molecular-weight 10494 #checksum 3222 SEQUENCE /// ENTRY CUKV #type complete TITLE plastocyanin - cucumber (tentative sequence) ORGANISM #formal_name Cucumis sativus #common_name cucumber DATE 18-Apr-1984 #sequence_revision 18-Apr-1984 #text_change 31-Mar-2000 ACCESSIONS A00303 REFERENCE A00303 !$#authors Ramshaw, J.A.M.; Felton, A.A. !$#journal Phytochemistry (1982) 21:1317-1320 !$#title The amino acid sequence of plastocyanin from Cucumis !1sativus. !$#accession A00303 !'##molecule_type protein !'##residues 1-99 ##label RAM COMMENT Plastocyanin, coded by a nuclear gene, is found loosely !1bound to the inner thylakoid membrane surface in !1chloroplasts, where it participates in electron transfer !1between photosystem I and the cytochrome b/f complex. CLASSIFICATION #superfamily plastocyanin KEYWORDS chloroplast; copper; electron transfer; metalloprotein FEATURE !$37,84,87,92 #binding_site copper (His, Cys, His, Met) (type 1) !8#status predicted SUMMARY #length 99 #molecular-weight 10555 #checksum 5820 SEQUENCE /// ENTRY CUSU #type complete TITLE plastocyanin - shepherd's purse ORGANISM #formal_name Capsella bursa-pastoris #common_name shepherd's purse DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 20-Feb-1998 ACCESSIONS A00304 REFERENCE A94461 !$#authors Scawen, M.D.; Ramshaw, J.A.M.; Brown, R.H.; Boulter, D. !$#citation unpublished results, cited by Boulter, D., Haslett, B.G., !1Peacock, D., Ramshaw, J.A.M., and Scawen, M.D., in Plant !1Biochemistry II, vol.13, Northcote, D.H., ed., pp.1-40, !1University Park Press, Baltimore, 1977 !$#accession A00304 !'##molecule_type protein !'##residues 1-99 ##label SCA CLASSIFICATION #superfamily plastocyanin KEYWORDS chloroplast; copper; electron transfer; metalloprotein FEATURE !$37,84,87,92 #binding_site copper (His, Cys, His, Met) (type 1) !8#status predicted SUMMARY #length 99 #molecular-weight 10383 #checksum 2918 SEQUENCE /// ENTRY CUDM #type complete TITLE plastocyanin - dog's mercury ORGANISM #formal_name Mercurialis perennis #common_name dog's mercury DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 20-Feb-1998 ACCESSIONS A00305 REFERENCE A94461 !$#authors Scawen, M.D.; Ramshaw, J.A.M.; Brown, R.H.; Boulter, D. !$#citation unpublished results, cited by Boulter, D., Haslett, B.G., !1Peacock, D., Ramshaw, J.A.M., and Scawen, M.D., in Plant !1Biochemistry II, vol.13, Northcote, D.H., ed., pp.1-40, !1University Park Press, Baltimore, 1977 !$#accession A00305 !'##molecule_type protein !'##residues 1-99 ##label SCA CLASSIFICATION #superfamily plastocyanin KEYWORDS chloroplast; copper; electron transfer; metalloprotein FEATURE !$37,84,87,92 #binding_site copper (His, Cys, His, Met) (type 1) !8#status predicted SUMMARY #length 99 #molecular-weight 10486 #checksum 4762 SEQUENCE /// ENTRY CUPO #type complete TITLE plastocyanin - potato ORGANISM #formal_name Solanum tuberosum #common_name potato DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 20-Feb-1998 ACCESSIONS A00306 REFERENCE A00306 !$#authors Ramshaw, J.A.M.; Scawen, M.D.; Bailey, C.J.; Boulter, D. !$#journal Biochem. J. (1974) 139:583-592 !$#title The amino acid sequence of plastocyanin from Solanum !1tuberosum L. (potato). !$#cross-references MUID:74308153; PMID:4854644 !$#accession A00306 !'##molecule_type protein !'##residues 1-99 ##label RAM CLASSIFICATION #superfamily plastocyanin KEYWORDS chloroplast; copper; electron transfer; metalloprotein FEATURE !$37,84,87,92 #binding_site copper (His, Cys, His, Met) (type 1) !8#status predicted SUMMARY #length 99 #molecular-weight 10330 #checksum 2956 SEQUENCE /// ENTRY CUUA #type complete TITLE plastocyanin - Chilean potato-tree ORGANISM #formal_name Solanum crispum #common_name Chilean potato-tree DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 20-Feb-1998 ACCESSIONS A00307 REFERENCE A00307 !$#authors Haslett, B.G.; Evans, I.M.; Boulter, D. !$#journal Phytochemistry (1978) 17:735-739 !$#title Amino acid sequence of plastocyanin from Solanum crispum !1using automatic methods. !$#accession A00307 !'##molecule_type protein !'##residues 1-99 ##label HAS COMMENT Plastocyanin, coded by a nuclear gene, is found loosely !1bound to the inner thylakoid membrane surface in !1chloroplasts, where it participates in electron transfer !1between photosystem I and the cytochrome b/f complex. CLASSIFICATION #superfamily plastocyanin KEYWORDS chloroplast; copper; electron transfer; metalloprotein FEATURE !$37,84,87,92 #binding_site copper (His, Cys, His, Met) (type 1) !8#status predicted SUMMARY #length 99 #molecular-weight 10398 #checksum 3459 SEQUENCE /// ENTRY CURXCO #type complete TITLE plastocyanin - bitter dock ORGANISM #formal_name Rumex obtusifolius #common_name bitter dock DATE 13-Jul-1981 #sequence_revision 13-Jul-1981 #text_change 20-Feb-1998 ACCESSIONS A90349; A94472; A00308 REFERENCE A90349 !$#authors Haslett, B.; Bailey, C.J.; Ramshaw, J.A.M.; Scawen, M.D.; !1Boulter, D. !$#journal Biochem. Soc. Trans. (1974) 2:1329-1331 !$#title Studies of the amino acid sequence of plastocyanin from !1Rumex obtusifolius (broad-leaved dock). !$#accession A90349 !'##molecule_type protein !'##residues 1-91,'L',93-99 ##label HAS REFERENCE A94472 !$#authors Ramshaw, J.A.M.; Boulter, D. !$#citation unpublished results, cited by Freeman, H.C., J. Proc. Royal !1Soc. N.S. Wales 112, 45-62, 1979 !$#contents revision !$#accession A94472 !'##molecule_type protein !'##residues 92 ##label RAM !'##note the residue at position 92 is Met, not Leu CLASSIFICATION #superfamily plastocyanin KEYWORDS chloroplast; copper; electron transfer; metalloprotein FEATURE !$37,84,87,92 #binding_site copper (His, Cys, His, Met) (type 1) !8#status predicted SUMMARY #length 99 #molecular-weight 10355 #checksum 3277 SEQUENCE /// ENTRY CUMUM #type complete TITLE plastocyanin precursor - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 11-Jun-1999 ACCESSIONS JA0065 REFERENCE JA0065 !$#authors Vorst, O.; Oosterhoff-Teertstra, R.; Vankan, P.; Smeekens, !1S.; Weisbeek, P. !$#journal Gene (1988) 65:59-69 !$#title Plastocyanin of Arabidopsis thaliana; isolation and !1characterization of the gene and chloroplast import of the !1precursor protein. !$#cross-references MUID:88284381; PMID:3396882 !$#accession JA0065 !'##molecule_type DNA !'##residues 1-171 ##label VOR !'##cross-references GB:M20937; NID:g166789; PIDN:AAA32834.1; !1PID:g166790 CLASSIFICATION #superfamily plastocyanin KEYWORDS chloroplast; copper; electron transfer; metalloprotein FEATURE !$1-72 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$73-171 #product plastocyanin #status predicted #label MAT\ !$109,156,159,164 #binding_site copper (His, Cys, His, Met) (type 1) !8#status predicted SUMMARY #length 171 #molecular-weight 17575 #checksum 6673 SEQUENCE /// ENTRY CUQH #type complete TITLE plastocyanin precursor - white campion ORGANISM #formal_name Silene pratensis, Lychnis alba #common_name white campion, evening lychnis DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 20-Feb-1998 ACCESSIONS A24404 REFERENCE A24404 !$#authors Smeekens, S.; de Groot, M.; van Binsbergen, J.; Weisbeek, P. !$#journal Nature (1985) 317:456-458 !$#title Sequence of the precursor of the chloroplast thylakoid lumen !1protein plastocyanin. !$#accession A24404 !'##molecule_type DNA !'##residues 1-165 ##label SME !'##cross-references GB:X02965 CLASSIFICATION #superfamily plastocyanin KEYWORDS chloroplast; copper; electron transfer; metalloprotein FEATURE !$1-66 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$67-165 #product plastocyanin #status predicted #label MAT\ !$103,150,153,158 #binding_site copper (His, Cys, His, Met) (type 1) !8#status predicted SUMMARY #length 165 #molecular-weight 16650 #checksum 8327 SEQUENCE /// ENTRY CUVF #type complete TITLE plastocyanin - fava bean ORGANISM #formal_name Vicia faba #common_name fava bean DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 20-Feb-1998 ACCESSIONS A00298 REFERENCE A00298 !$#authors Ramshaw, J.A.M.; Scawen, M.D.; Boulter, D. !$#journal Biochem. J. (1974) 141:835-843 !$#title The amino acid sequence of plastocyanin from Vicia faba L. !1(broad bean). !$#cross-references MUID:75204778; PMID:4463964 !$#accession A00298 !'##molecule_type protein !'##residues 1-99 ##label RAM CLASSIFICATION #superfamily plastocyanin KEYWORDS chloroplast; copper; electron transfer; metalloprotein FEATURE !$37,84,87,92 #binding_site copper (His, Cys, His, Met) (type 1) !8#status predicted SUMMARY #length 99 #molecular-weight 10394 #checksum 3389 SEQUENCE /// ENTRY CUPX #type complete TITLE plastocyanin a precursor [validated] - Lombardy poplar ORGANISM #formal_name Populus nigra var. italica #common_name Lombardy poplar DATE 31-May-1980 #sequence_revision 31-Oct-1997 #text_change 15-Sep-2000 ACCESSIONS S58209; A00309 REFERENCE S58208 !$#authors Reichert, J.; Jenzelewski, V.; Haehnel, W. !$#submission submitted to the EMBL Data Library, July 1995 !$#description Kinetic studies of recombinant poplar plastocyanins. !$#accession S58209 !'##molecule_type mRNA !'##residues 1-168 ##label REI !'##cross-references EMBL:Z50185; NID:g929812; PIDN:CAA90564.1; !1PID:g929813 !'##experimental_source var. italica REFERENCE A94471 !$#authors Ambler, R. !$#citation unpublished results, cited by Freeman, H.C., J. Proc. Royal !1Soc. N.S. Wales 112, 45-62, 1979 !$#accession A00309 !'##molecule_type protein !'##residues 70-127,'ZZB',131-168 ##label AMB REFERENCE A51342 !$#authors Guss, J.M.; Freeman, H.C. !$#submission submitted to the Brookhaven Protein Data Bank, March 1992 !$#cross-references PDB:1PLC !$#contents annotation; X-ray crystallography, 1.33 angstroms, residues !170-168 REFERENCE A50737 !$#authors Guss, J.M.; Freeman, H.C. !$#submission submitted to the Brookhaven Protein Data Bank, September !11986 !$#cross-references PDB:5PCY !$#contents annotation; X-ray crystallography, 1.80 angstroms, residues !170-168 REFERENCE A58637 !$#authors Guss, J.M.; Harrowell, P.R.; Murata, M.; Norris, V.A.; !1Freeman, H.C. !$#journal J. Mol. Biol. (1986) 192:361-387 !$#title Crystal structure analyses of reduced (Cu(I)) poplar !1plastocyanin at six pH values. !$#cross-references MUID:87169729; PMID:3560221 !$#contents annotation; X-ray crystallography, 1.80 angstroms REFERENCE A58639 !$#authors Guss, J.M.; Freeman, H.C. !$#journal J. Mol. Biol. (1983) 169:521-563 !$#title Structure of oxidized poplar plastocyanin at 1.6 Angstroms !1resolution. !$#cross-references MUID:84010876; PMID:6620385 !$#contents annotation; X-ray crystallography, 1.60 angstroms REFERENCE A93194 !$#authors Colman, P.M.; Freeman, H.C.; Guss, J.M.; Murata, M.; Norris, !1V.A.; Ramshaw, J.A.M.; Venkatappa, M.P. !$#journal Nature (1978) 272:319-324 !$#title X-ray crystal structure analysis of plastocyanin at 2.7 !1angstrom resolution. !$#contents annotation; X-ray crystallography, 2.7 angstroms COMMENT Plastocyanin is found loosely bound to the inner thylakoid !1membrane surface in chloroplasts. GENETICS !$#gene petE !$#genome nuclear FUNCTION !$#description accepts electrons from cytochrome f and donates electrons to !1photosystem I CLASSIFICATION #superfamily plastocyanin KEYWORDS chloroplast; copper; electron transfer; membrane-associated !1protein; metalloprotein FEATURE !$1-69 #domain transit peptide (chloroplast) #status !8predicted #label TRP\ !$70-168 #product plastocyanin a #status experimental #label !8MAT\ !$106,153,156,161 #binding_site copper (His, Cys, His, Met) (type 1) !8#status experimental SUMMARY #length 168 #molecular-weight 17020 #checksum 2619 SEQUENCE /// ENTRY CUKLCF #type complete TITLE plastocyanin - Chlorella fusca ORGANISM #formal_name Chlorella fusca DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 20-Feb-1998 ACCESSIONS A00310 REFERENCE A00310 !$#authors Kelly, J.; Ambler, R.P. !$#journal Biochem. J. (1974) 143:681-690 !$#title The amino acid sequence of plastocyanin from Chlorella !1fusca. !$#cross-references MUID:75183336; PMID:4462750 !$#accession A00310 !'##molecule_type protein !'##residues 1-98 ##label KEL CLASSIFICATION #superfamily plastocyanin KEYWORDS chloroplast; copper; electron transfer; metalloprotein FEATURE !$38,83,86,91 #binding_site copper (His, Cys, His, Met) (type 1) !8#status predicted SUMMARY #length 98 #molecular-weight 10299 #checksum 9528 SEQUENCE /// ENTRY CUEI #type complete TITLE plastocyanin [validated] - green alga (Enteromorpha prolifera) ORGANISM #formal_name Enteromorpha prolifera DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 15-Sep-2000 ACCESSIONS A25055 REFERENCE A25055 !$#authors Simpson, R.J.; Moritz, R.L.; Nice, E.C.; Grego, B.; !1Yoshizaki, F.; Sugimura, Y.; Freeman, H.C.; Murata, M. !$#journal Eur. J. Biochem. (1986) 157:497-506 !$#title Complete amino acid sequence of plastocyanin from a green !1alga, Enteromorpha prolifera. !$#cross-references MUID:86247647; PMID:3522227 !$#accession A25055 !'##molecule_type protein !'##residues 1-98 ##label SIM REFERENCE A50786 !$#authors Collyer, C.A.; Guss, J.M.; Freeman, H.C. !$#submission submitted to the Brookhaven Protein Data Bank, September !11989 !$#cross-references PDB:7PCY !$#contents annotation; X-ray crystallography, 1.8 angstroms, residues !11-98 REFERENCE A58731 !$#authors Collyer, C.A.; Guss, J.M.; Sugimura, Y.; Yoshizaki, F.; !1Freeman, H.C. !$#journal J. Mol. Biol. (1990) 211:617-632 !$#title Crystal structure of plastocyanin from a green alga, !1Enteromorpha prolifera. !$#cross-references MUID:90172425; PMID:2308169 !$#contents annotation; X-ray crystallography, 1.8 angstroms COMMENT Plastocyanin, a copper-containing protein coded by a nuclear !1gene, is found loosely bound to the inner thylakoid membrane !1surface in chloroplasts, where it functions as an electron !1carrier between the P700 of photosystem I and the cytochrome !1b/f complex. CLASSIFICATION #superfamily plastocyanin KEYWORDS chloroplast; copper; electron transfer; metalloprotein FEATURE !$38,83,86,91 #binding_site copper (His, Cys, His, Met) (type 1) !8#status experimental SUMMARY #length 98 #molecular-weight 10114 #checksum 8571 SEQUENCE /// ENTRY CUUV #type complete TITLE plastocyanin - Arasaki's sea lettuce ORGANISM #formal_name Ulva arasakii #common_name Arasaki's sea lettuce DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 28-Jul-2000 ACCESSIONS JU0073; JW0010 REFERENCE JU0073 !$#authors Yoshizaki, F.; Fukazawa, T.; Mishina, Y.; Sugimura, Y. !$#journal J. Biochem. (1989) 106:282-288 !$#title Some properties and amino acid sequence of plastocyanin from !1a green alga, Ulva arasakii. !$#cross-references MUID:90036775; PMID:2509442 !$#accession JU0073 !'##molecule_type protein !'##residues 1-98 ##label YOS COMMENT Plastocyanin, coded by a nuclear gene, is found loosely !1bound to the inner thylakoid membrane surface in !1chloroplasts, where it functions as an electron carrier !1between the P700 of photosystem I and the cytochrome b/f !1complex. CLASSIFICATION #superfamily plastocyanin KEYWORDS chloroplast; copper; electron transfer; metalloprotein FEATURE !$38,83,86,91 #binding_site copper (His, Cys, His, Met) (type 1) !8#status predicted SUMMARY #length 98 #molecular-weight 10173 #checksum 7592 SEQUENCE /// ENTRY CUBCRT #type complete TITLE rusticyanin - Thiobacillus ferrooxidans ORGANISM #formal_name Thiobacillus ferrooxidans DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 20-Apr-2000 ACCESSIONS A40302 REFERENCE A40302 !$#authors Ronk, M.; Shively, J.E.; Shute, E.A.; Blake II, R.C. !$#journal Biochemistry (1991) 30:9435-9442 !$#title Amino acid sequence of the blue copper protein rusticyanin !1from Thiobacillus ferrooxidans. !$#cross-references MUID:91369963; PMID:1892844 !$#accession A40302 !'##molecule_type protein !'##residues 1-155 ##label RON CLASSIFICATION #superfamily plastocyanin KEYWORDS copper; electron transfer; metalloprotein FEATURE !$85,138,143,148 #binding_site copper (His, Cys, His, Met) (type 1) !8#status predicted SUMMARY #length 155 #molecular-weight 16551 #checksum 9573 SEQUENCE /// ENTRY BUKV #type complete TITLE basic blue protein [validated] - cucumber ALTERNATE_NAMES cusacyanin; phytocyanin; plantacyanin ORGANISM #formal_name Cucumis sativus #common_name cucumber DATE 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 15-Sep-2000 ACCESSIONS A00312 REFERENCE A00312 !$#authors Murata, M.; Begg, G.S.; Lambrou, F.; Leslie, B.; Simpson, !1R.J.; Freeman, H.C.; Morgan, F.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:6434-6437 !$#title Amino acid sequence of a basic glue protein from cucumber !1seedlings. !$#accession A00312 !'##molecule_type protein !'##residues 1-96 ##label MUR !'##experimental_source seedling REFERENCE A67903 !$#authors Guss, J.M.; Freeman, H.C. !$#submission submitted to the Brookhaven Protein Data Bank, March 1996 !$#cross-references PDB:2CBP !$#contents annotation; X-ray crystallography, 1.8 angstroms, residues !11-36,'S',38-96 !$#note residue 37 was not determined but modeled as Ser REFERENCE A58824 !$#authors Guss, J.M.; Merritt, E.A.; Phizackerley, R.P.; Freeman, H.C. !$#journal J. Mol. Biol. (1996) 262:686-705 !$#title The structure of phytocyanin, the basic blue protein from !1cucumber, refined at 1.8 Angstroms resolution. !$#cross-references MUID:97030706; PMID:8876647 !$#contents annotation; X-ray crystallography, 1.8 angstroms CLASSIFICATION #superfamily plastocyanin KEYWORDS copper; electron transfer; extracellular protein FEATURE !$39,79,84,89 #binding_site copper (His, Cys, His, Met) (type 1) !8#status experimental\ !$52-85 #disulfide_bonds #status experimental SUMMARY #length 96 #molecular-weight 10384 #checksum 6484 SEQUENCE /// ENTRY ARRA3 #type complete TITLE allergen Ra3 - common ragweed ORGANISM #formal_name Ambrosia artemisiifolia var. elatior #common_name common ragweed DATE 28-Feb-1981 #sequence_revision 30-Jun-1993 #text_change 25-Oct-1996 ACCESSIONS A00313 REFERENCE A00313 !$#authors Klapper, D.G.; Goodfriend, L.; Capra, J.D. !$#journal Biochemistry (1980) 19:5729-5734 !$#title Amino acid sequence of ragweed allergen Ra3. !$#cross-references MUID:81110503; PMID:7459340 !$#accession A00313 !'##molecule_type protein !'##residues 1-40,'D',42-101 ##label KLA !'##note the residue identified as 41-Asp is bound to carbohydrate; !1therefore we have shown it as Asn CLASSIFICATION #superfamily plastocyanin KEYWORDS blocked carboxyl end; copper; electron transfer; !1glycoprotein; pollen FEATURE !$41 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$61-88 #disulfide_bonds #status predicted\ !$84 #binding_site carbohydrate (Ser) (covalent) #status !8experimental\ !$101 #modified_site blocked carboxyl end (Arg) #status !8experimental SUMMARY #length 101 #molecular-weight 11375 #checksum 1312 SEQUENCE /// ENTRY SSKV #type complete TITLE cupredoxin [validated] - cucumber ALTERNATE_NAMES stellacyanin ORGANISM #formal_name Cucumis sativus #common_name cucumber DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 15-Sep-2000 ACCESSIONS S27034; S26511 REFERENCE S27034 !$#authors Mann, K.; Schaefer, W.; Thoenes, U.; Messerschmidt, A.; !1Mehrabian, Z.; Nalbandyan, R. !$#journal FEBS Lett. (1992) 314:220-223 !$#title The amino acid sequence of a type I copper protein with an !1unusual serine- and hydroxyproline-rich C-terminal domain !1isolated from cucumber peelings. !$#cross-references MUID:93106154; PMID:1468551 !$#accession S27034 !'##molecule_type protein !'##residues 1-137 ##label MA2 !'##note submitted to the Protein Sequence Database, September 1992 REFERENCE A65911 !$#authors Hart, P.J.; Nersissian, A.M.; Herrmann, R.G.; Nalbandyan, !1R.M.; Valentine, J.S.; Eisenberg, D. !$#submission submitted to the Brookhaven Protein Data Bank, August 1996 !$#cross-references PDB:1JER !$#contents annotation; X-ray crystallography, 1.6 angstroms, residues !1'M',2-109 !$#note Cucumis sativus (cucumber) sequence expressed in Escherichia !1coli REFERENCE A58823 !$#authors Hart, P.J.; Nersissian, A.M.; Herrmann, R.G.; Nalbandyan, !1R.M.; Valentine, J.S.; Eisenberg, D. !$#journal Protein Sci. (1996) 5:2175-2183 !$#title A missing link in cupredoxins: crystal structure of cucumber !1stellacyanin at 1.6 Angstroms resolution. !$#cross-references MUID:97084802; PMID:8931136 !$#contents annotation; X-ray crystallography, 1.6 angstroms CLASSIFICATION #superfamily plastocyanin KEYWORDS copper; electron transfer; extracellular protein; !1glycoprotein; hydroxyproline; pyroglutamic acid FEATURE !$1-110 #domain copper binding #label COP\ !$111-137 #domain carboxyl-terminal #label TAI\ !$1 #modified_site pyrrolidone carboxylic acid (Gln) !8#status experimental\ !$46,89,94,99 #binding_site copper (His, Cys, His, Gln) #status !8experimental\ !$60-95 #disulfide_bonds #status experimental\ !$109 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$115,127 #modified_site 4-hydroxyproline (Pro) (partial) !8#status experimental\ !$116,117,121,122, !$128,129,133,134,136 #modified_site 4-hydroxyproline (Pro) #status !8experimental SUMMARY #length 137 #molecular-weight 14747 #checksum 5867 SEQUENCE /// ENTRY CFKKA #type complete TITLE C-phycocyanin alpha chain [validated] - red alga (Cyanidium caldarium) ORGANISM #formal_name Cyanidium caldarium DATE 31-May-1979 #sequence_revision 02-Apr-1982 #text_change 15-Sep-2000 ACCESSIONS A92297; A91464; A60844; A00314 REFERENCE A92297 !$#authors Offner, G.D.; Brown-Mason, A.S.; Ehrhardt, M.M.; Troxler, !1R.F. !$#journal J. Biol. Chem. (1981) 256:12167-12175 !$#title Primary structure of phycocyanin from the unicellular !1rhodophyte Cyanidium caldarium. I. Complete amino acid !1sequence of the alpha subunit. !$#cross-references MUID:82053081; PMID:7298651 !$#accession A92297 !'##molecule_type protein !'##residues 1-162 ##label OFF REFERENCE A91464 !$#authors Troxler, R.F.; Brown, A.S. !$#journal Fed. Proc. (1979) 38:325B !$#title Amino acid sequence of the phycocyanin alpha subunit from !1the alga, Cyanidium caldarium. !$#accession A91464 !'##molecule_type protein !'##residues 1-48,'Q',50-52,'D',54-60,'Q',62-94,'I',96-100,'A',102-162 !1##label TRO REFERENCE A60844 !$#authors Brown, A.S.; Offner, G.D.; Ehrhardt, M.M.; Troxler, R.F. !$#journal J. Biol. Chem. (1979) 254:7803-7811 !$#title Phycobilin-apoprotein linkages in the alpha and beta !1subunits of phycocyanin from the unicellular rhodophyte, !1Cyanidium caldarium. Amino acid sequences of (35)S-labeled !1chromopeptides. !$#cross-references MUID:79239364; PMID:468790 !$#accession A60844 !'##molecule_type protein !'##residues 70-94 ##label BRO REFERENCE A68150 !$#authors Stec, B.; Troxler, R.F.; Teeter, M.M. !$#submission submitted to the Brookhaven Protein Data Bank, June 1995 !$#cross-references PDB:1PHN !$#contents annotation; X-ray crystallography, 1.65 angstroms, residues !11-162 COMMENT This protein was isolated from the phycobilisomes on the !1chloroplasts of this unicellular, acido-thermal, eukaryote !1red alga. COMPLEX heterodimers of alpha and beta (see PIR:CFKKB) chains form !1larger multimers CLASSIFICATION #superfamily phycocyanin KEYWORDS chloroplast; chromoprotein; heterodimer; photosynthesis; !1phycocyanobilin FEATURE !$84 #binding_site phycocyanobilin (Cys) (covalent) !8#status experimental SUMMARY #length 162 #molecular-weight 17505 #checksum 9110 SEQUENCE /// ENTRY CFMWA #type complete TITLE C-phycocyanin alpha chain - Fischerella sp. ORGANISM #formal_name Fischerella sp. DATE 30-Jun-1979 #sequence_revision 30-Jun-1979 #text_change 30-Apr-1999 ACCESSIONS A00315 REFERENCE A00315 !$#authors Frank, G.; Sidler, W.; Widmer, H.; Zuber, H. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1978) 359:1491-1507 !$#title The complete amino acid sequence of both subunits of !1C-phycocyanin from the cyanobacterium Mastigocladus !1laminosus. !$#cross-references MUID:79087164; PMID:103794 !$#accession A00315 !'##molecule_type protein !'##residues 1-162 ##label FRA !'##note the source was designated as Mastigocladus laminosus CLASSIFICATION #superfamily phycocyanin KEYWORDS chromoprotein; photosynthesis; phycocyanobilin FEATURE !$84 #binding_site phycocyanobilin (Cys) (covalent) !8#status experimental SUMMARY #length 162 #molecular-weight 17416 #checksum 6191 SEQUENCE /// ENTRY CFYCAA #type complete TITLE C-phycocyanin alpha chain - Synechococcus sp. (strain PCC 7002) ORGANISM #formal_name Synechococcus sp. DATE 13-Aug-1986 #sequence_revision 13-Aug-1986 #text_change 11-Jun-1999 ACCESSIONS A94024; A94017; A60662; A00316; B22972 REFERENCE A94024 !$#authors de Lorimier, R.; Bryant, D.A.; Porter, R.D.; Liu, W.Y.; Jay, !1E.; Stevens Jr., S.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:7946-7950 !$#title Genes of the alpha and beta subunits of phycocyanin. !$#cross-references MUID:85088525; PMID:6096868 !$#accession A94024 !'##molecule_type DNA !'##residues 1-162 ##label DEL !'##cross-references GB:K02660; NID:g142182; PIDN:AAB05344.1; !1PID:g142184 REFERENCE A94017 !$#authors Pilot, T.J.; Fox, J.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:6983-6987 !$#title Cloning and sequencing of the genes encoding the alpha and !1beta subunits of C-phycocyanin from the cyanobacterium !1Agmenellum quadruplicatum. !$#cross-references MUID:85063716; PMID:6438628 !$#accession A94017 !'##molecule_type DNA !'##residues 1-162 ##label PIL !'##cross-references GB:K02659; NID:g142176; PIDN:AAB05342.1; !1PID:g142178 REFERENCE A60662 !$#authors de Lorimier, R.; Guglielmi, G.; Bryant, D.A.; Stevens Jr., !1S.E. !$#journal Arch. Microbiol. (1990) 153:541-549 !$#title Structure and mutation of a gene encoding a M-r 33000 !1phycocyanin-associated linker polypeptide. !$#cross-references MUID:90314661; PMID:2114862 !$#accession A60662 !'##molecule_type DNA !'##residues 149-162 ##label DEA !'##cross-references GB:X81868; NID:g732557; PIDN:CAA57456.1; !1PID:g732558 GENETICS !$#gene cpcA CLASSIFICATION #superfamily phycocyanin KEYWORDS chromoprotein; photosynthesis; phycocyanobilin FEATURE !$84 #binding_site phycocyanobilin (Cys) (covalent) !8#status predicted SUMMARY #length 162 #molecular-weight 17622 #checksum 7517 SEQUENCE /// ENTRY CFYCA #type complete TITLE C-phycocyanin alpha chain - Synechococcus sp. (PCC 6301) ORGANISM #formal_name Synechococcus sp. #variety PCC 6301 #note Synechococcus sp. PCC 6301 (ATCC 27144) was named Anacystis nidulans in other culture collections, e.g., CCAP, SAUG, and UTEX DATE 18-Dec-1981 #sequence_revision 02-Jul-1996 #text_change 11-Jun-1999 ACCESSIONS A29015; S60070; S60075; A00317 REFERENCE A29015 !$#authors Lau, R.H.; Alvarado-Urbina, G.; Lau, P.C.K. !$#journal Gene (1987) 52:21-29 !$#title Phycocyanin alpha-subunit gene of Anacystis nidulans R2: !1cloning, nucleotide sequencing and expression in Escherichia !1coli. !$#cross-references MUID:87248092; PMID:3036657 !$#note Anacystis nidulans !$#accession A29015 !'##molecule_type DNA !'##residues 1-163 ##label LAU !'##cross-references GB:M16325; NID:g142137; PIDN:AAA22051.1; !1PID:g142139 !'##experimental_source strain R2 REFERENCE S60069 !$#authors Kalla, S.R.; Lind, L.K.; Lidholm, J.; Gustafsson, P. !$#journal J. Bacteriol. (1988) 170:2961-2970 !$#title Transcriptional organization of the phycocyanin subunit gene !1clusters of the cyanobacterium Anacystis nidulans UTEX 625. !$#cross-references MUID:88257006; PMID:2454910 !$#accession S60070 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-163 ##label KAL !'##cross-references EMBL:M94218; NID:g142121; PIDN:AAA64527.1; !1PID:g142123 !'##experimental_source PCC 6301 !'##note source designated as Anacystis nidulans !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1992 !$#accession S60075 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-163 ##label KA2 !'##cross-references EMBL:M94218; NID:g142121; PIDN:AAA64527.1; !1PID:g142123 !'##note the source is designated as Anacystis nidulans !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1992 REFERENCE A00317 !$#authors Walsh, R.G.; Wingfield, P.; Glazer, A.N.; DeLange, R.J. !$#journal Fed. Proc. (1980) 39:1998 !$#accession A00317 !'##molecule_type protein !'##residues 2-53,'D',55-120,'TK',123-157,'IL',160-163 ##label WAL COMPLEX associates with beta chain (see PIR:CFCYB) FUNCTION !$#description photon energy transfer from phycoerythrin to allophycocyanin !$#pathway photosynthesis CLASSIFICATION #superfamily phycocyanin KEYWORDS chromoprotein; photosynthesis; phycocyanobilin FEATURE !$2-163 #product C-phycocyanin alpha chain #status !8experimental #label MAT\ !$85 #binding_site phycocyanobilin (Cys) (covalent) !8#status experimental SUMMARY #length 163 #molecular-weight 17288 #checksum 9822 SEQUENCE /// ENTRY CFYCA3 #type complete TITLE R-phycocyanin II alpha chain - Synechococcus sp. ORGANISM #formal_name Synechococcus sp. DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 20-Apr-2000 ACCESSIONS S17735; S31068; S31073; A26703; S27718; S31061 REFERENCE S17734 !$#authors Wilson, W.H.; Newman, J.; Mann, N.H.; Carr, N.G. !$#journal Plant Mol. Biol. (1991) 17:931-933 !$#title Cloning and sequence analysis of the phycocyanin genes of !1the marine cyanobacterium Synechococcus sp. WH7803. !$#cross-references MUID:92003705; PMID:1912508 !$#accession S17735 !'##molecule_type DNA !'##residues 1-162 ##label WIL !'##cross-references EMBL:X59809; NID:g48036; PIDN:CAA42480.1; !1PID:g48038 !'##experimental_source strain WH7803 REFERENCE S31066 !$#authors de Lorimier, R.; Wilbanks, S.M.; Glazer, A.N. !$#journal Plant Mol. Biol. (1993) 21:225-237 !$#title Genes of the R-phycocyanin II locus of marine Synechococcus !1spp., and comparison of protein-chromophore interactions in !1phycocyanins differing in bilin composition. !$#cross-references MUID:93144698; PMID:8425055 !$#accession S31068 !'##molecule_type DNA !'##residues 1-9,'A',11-20,'N',22-34,'K',36-42,'G',44,'T',46-49,'S', !151-52,'SS',55,'T',57-60,'T',62-71,'P',73-75,'A',77,'S', !179-87,'I',89-134,'H',136,'Q',138-154,'N',156-161,'T' ##label !1DEL !'##cross-references EMBL:M95288; NID:g154551; PIDN:AAA27346.1; !1PID:g154566 !'##experimental_source strain WH8020 !$#accession S31073 !'##molecule_type DNA !'##residues 1-9,'A',11-20,'N',22-34,'K',36-44,'TS',47-49,'S',51-60,'S', !162-75,'A',77-134,'H',136-137,'A',139-162 ##label LOR !'##cross-references EMBL:M95289; NID:g154605; PIDN:AAA27366.1; !1PID:g154607 !'##experimental_source strain WH8103 REFERENCE A92644 !$#authors Ong, L.J.; Glazer, A.N. !$#journal J. Biol. Chem. (1987) 262:6323-6327 !$#title R-phycocyanin II, a new phycocyanin occurring in marine !1Synechococcus species. Identification of the terminal energy !1acceptor bilin in phycocyanins. !$#cross-references MUID:87194855; PMID:3571260 !$#accession A26703 !'##molecule_type protein !'##residues 2-9,'A',11-20,'N';84-86 ##label ONG GENETICS !$#gene cpcA; rpcA CLASSIFICATION #superfamily phycocyanin KEYWORDS chromoprotein; photosynthesis; phycocyanobilin FEATURE !$2-162 #product R-phycocyanin II alpha chain #status !8predicted #label MAT\ !$84 #binding_site phycocyanobilin (Cys) (covalent) !8#status predicted SUMMARY #length 162 #molecular-weight 17320 #checksum 5667 SEQUENCE /// ENTRY RFMWA #type complete TITLE phycoerythrocyanin alpha chain - Fischerella sp. ORGANISM #formal_name Fischerella sp. DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 29-Sep-1999 ACCESSIONS JQ0764; A00318 REFERENCE JQ0763 !$#authors Eberlein, M.; Kufer, W. !$#journal Gene (1990) 94:133-136 !$#title Genes encoding both subunits of phycoerythrocyanin, a !1light-harvesting biliprotein from the cyanobacterium !1Mastigocladus laminosus. !$#cross-references MUID:91033055; PMID:2121619 !$#accession JQ0764 !'##molecule_type DNA !'##residues 1-162 ##label EBE !'##cross-references GB:M34254; NID:g149774; PIDN:AAC64654.1; !1PID:g149776 REFERENCE A91722 !$#authors Fuglistaller, P.; Suter, F.; Zuber, H. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1983) 364:691-712 !$#title The complete amino-acid sequence of both subunits of !1phycoerythrocyanin from the thermophilic cyanobacterium !1Mastigocladus laminosus. !$#cross-references MUID:83289130; PMID:6411579 !$#accession A00318 !'##molecule_type protein !'##residues 1-162 ##label FUG !'##note the source is designated as Mastigocladus laminosus REFERENCE A30650 !$#authors Duerring, M.; Huber, R.; Bode, W.; Ruembeli, R.; Zuber, H. !$#journal J. Mol. Biol. (1990) 211:633-644 !$#title Refined three-dimensional structure of phycoerythrocyanin !1from the cyanobacterium Mastigocladus laminosus at 2.7 A. !$#cross-references MUID:90172426; PMID:2106585 !$#contents annotation; X-ray crystallography, 2.7 angstroms GENETICS !$#gene pecA COMPLEX heterodimer of alpha and beta (see PIR:RFMWB) chains; !1heterodimers associate to form trimeric and larger complexes FUNCTION !$#description phycobilisome light harvesting !$#pathway photosynthesis !$#note maximum absorption at approximately 550-570 nanometers CLASSIFICATION #superfamily phycocyanin KEYWORDS chromoprotein; light-harvesting complex; photosynthesis; !1phycobiliviolin; thylakoid FEATURE !$84 #binding_site phycobiliviolin (Cys) (covalent) !8#status experimental SUMMARY #length 162 #molecular-weight 17564 #checksum 6492 SEQUENCE /// ENTRY B41841 #type complete TITLE phycoerythrocyanin alpha chain - Anabaena sp. (strain PCC 7120) ORGANISM #formal_name Anabaena sp. DATE 24-Sep-1999 #sequence_revision 24-Sep-1999 #text_change 20-Apr-2001 ACCESSIONS B41841 REFERENCE A41841 !$#authors Swanson, R.V.; de Lorimier, R.; Glazer, A.N. !$#journal J. Bacteriol. (1992) 174:2640-2647 !$#title Genes encoding the phycobilisome rod substructure are !1clustered on the Anabaena chromosome: characterization of !1the phycoerythrocyanin operon. !$#cross-references MUID:92210509; PMID:1556083 !$#accession B41841 !'##status preliminary !'##molecule_type DNA !'##residues 1-162 ##label SWA !'##cross-references GB:M80357; NID:g142069; PIDN:AAA22017.1; !1PID:g142071 REFERENCE A30654 !$#authors Bishop, J.E.; Rapoport, H.; Klotz, A.V.; Chan, C.F.; Glazer, !1A.N.; Fueglistaller, P.; Zuber, H. !$#journal J. Am. Chem. Soc. (1987) 109:875-881 !$#title Chromopeptides from phycoerythrocyanin. Structure and !1linkage of the three bilin groups. !$#contents annotation !$#note spectrographic characterization; peptide linkage COMPLEX heterodimer of alpha and beta (see PIR:A41841) chains; !1heterodimers associate to form trimeric and larger complexes FUNCTION !$#description phycobilisome light harvesting !$#pathway photosynthesis !$#note maximum absorption at approximately 550-570 nanometers CLASSIFICATION #superfamily phycocyanin KEYWORDS chromoprotein; light-harvesting complex; photosynthesis; !1phycobiliviolin; thylakoid FEATURE !$84 #binding_site phycobiliviolin (Cys) (covalent) !8#status experimental SUMMARY #length 162 #molecular-weight 17454 #checksum 8760 SEQUENCE /// ENTRY A44462 #type complete TITLE allophycocyanin alpha chain - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A44462; S75012 REFERENCE A44462 !$#authors Su, X.; Fraenkel, P.G.; Bogorad, L. !$#journal J. Biol. Chem. (1992) 267:22944-22950 !$#title Excitation energy transfer from phycocyanin to chlorophyll !1in an apcA-defective mutant of Synechocystis sp. PCC 6803. !$#cross-references MUID:93054612; PMID:1429645 !$#accession A44462 !'##molecule_type mRNA !'##residues 1-161 ##label SU1 !'##cross-references GB:M77135; NID:g154453; PIDN:AAA27276.1; !1PID:g154454 !'##experimental_source PCC 6803 !'##note sequence extracted from NCBI backbone (NCBIP:118109) REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75012 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-161 ##label KAN !'##cross-references EMBL:D90910; GB:AB001339; NID:g1652956; !1PIDN:BAA17874.1; PID:g1652957 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene apcA CLASSIFICATION #superfamily phycocyanin KEYWORDS chromoprotein; photosynthesis; phycocyanobilin FEATURE !$81 #binding_site phycocyanobilin (Cys) (covalent) !8#status predicted SUMMARY #length 161 #molecular-weight 17412 #checksum 6984 SEQUENCE /// ENTRY B28539 #type complete TITLE C-phycocyanin 2 alpha chain - Calothrix sp. ALTERNATE_NAMES inducible phycocyanin alpha chain ORGANISM #formal_name Calothrix sp. DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS B28539; S00712 REFERENCE A93683 !$#authors Capuano, V.; Mazel, D.; Tandeau de Marsac, N.; Houmard, J. !$#journal Nucleic Acids Res. (1988) 16:1626 !$#title Complete nucleotide sequence of the red-light specific set !1of phycocyanin genes from the cyanobacterium Calothrix PCC !17601. !$#cross-references MUID:88157728; PMID:3126486 !$#accession B28539 !'##molecule_type DNA !'##residues 1-162 ##label CAP !'##cross-references GB:M36276; NID:g144937; PIDN:AAA23290.1; !1PID:g144939 !'##experimental_source PCC 7601 REFERENCE S00711 !$#authors Conley, P.B.; Lemaux, P.G.; Grossman, A. !$#journal J. Mol. Biol. (1988) 199:447-465 !$#title Molecular characterization and evolution of sequences !1encoding light-harvesting components in the chromatically !1adapting cyanobacterium Fremyella diplosiphon. !$#cross-references MUID:88172492; PMID:3127591 !$#accession S00712 !'##molecule_type DNA !'##residues 1-7,'G',9-54,'TA',57-149,'V',151-162 ##label CON !'##cross-references EMBL:X07012; NID:g43381; PIDN:CAA30062.1; !1PID:g43383 !'##note source designated as Fremyella diplosiphon GENETICS !$#gene cpcA2 CLASSIFICATION #superfamily phycocyanin KEYWORDS chromoprotein; photosynthesis; phycocyanobilin FEATURE !$1-162 #product C-phycocyanin 2 alpha chain #status !8experimental #label MAT\ !$84 #binding_site phycocyanobilin (Cys) (covalent) !8#status predicted SUMMARY #length 162 #molecular-weight 17465 #checksum 8259 SEQUENCE /// ENTRY A28539 #type complete TITLE C-phycocyanin 2 beta chain - Calothrix sp. ALTERNATE_NAMES inducible phycocyanin beta chain ORGANISM #formal_name Calothrix sp. DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS A28539; S00711 REFERENCE A93683 !$#authors Capuano, V.; Mazel, D.; Tandeau de Marsac, N.; Houmard, J. !$#journal Nucleic Acids Res. (1988) 16:1626 !$#title Complete nucleotide sequence of the red-light specific set !1of phycocyanin genes from the cyanobacterium Calothrix PCC !17601. !$#cross-references MUID:88157728; PMID:3126486 !$#accession A28539 !'##molecule_type DNA !'##residues 1-172 ##label CAP !'##cross-references GB:M36276; NID:g144937; PIDN:AAA23289.1; !1PID:g144938 !'##experimental_source PCC 7601 REFERENCE S00711 !$#authors Conley, P.B.; Lemaux, P.G.; Grossman, A. !$#journal J. Mol. Biol. (1988) 199:447-465 !$#title Molecular characterization and evolution of sequences !1encoding light-harvesting components in the chromatically !1adapting cyanobacterium Fremyella diplosiphon. !$#cross-references MUID:88172492; PMID:3127591 !$#accession S00711 !'##molecule_type DNA !'##residues 1-28,'D',30-172 ##label CON !'##cross-references EMBL:X07012 !'##note source designated as Fremyella diplosiphon GENETICS !$#gene cpcB2 CLASSIFICATION #superfamily phycocyanin KEYWORDS chromoprotein; methylated amino acid; photosynthesis; !1phycocyanobilin FEATURE !$1-172 #product C-phycocyanin 2 beta chain #status !8experimental #label MAT\ !$72 #modified_site N4-methylasparagine (Asn) #status !8predicted\ !$82 #binding_site phycocyanobilin (Cys) (covalent) !8#status predicted\ !$153 #binding_site phycocyanobilin (Cys) (covalent) !8#status predicted SUMMARY #length 172 #molecular-weight 18121 #checksum 3719 SEQUENCE /// ENTRY CFXCA #type complete TITLE C-phycoerythrin alpha chain - Calothrix sp. (strain PCC 7601) ORGANISM #formal_name Calothrix sp. DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jun-2000 ACCESSIONS A25527; A24307; S00287 REFERENCE A93645 !$#authors Mazel, D.; Guglielmi, G.; Houmard, J.; Sidler, W.; Bryant, !1D.A.; Tandeau de Marsac, N. !$#journal Nucleic Acids Res. (1986) 14:8279-8290 !$#title Green light induces transcription of the phycoerythrin !1operon in the cyanobacterium Calothrix 7601. !$#cross-references MUID:87066711; PMID:2431391 !$#accession A25527 !'##molecule_type DNA !'##residues 1-164 ##label MAZ !'##cross-references EMBL:X04592; NID:g1546895; PIDN:CAA28261.1; !1PID:g43390 REFERENCE A90711 !$#authors Sidler, W.; Kumpf, B.; Rudiger, W.; Zuber, H. !$#journal Biol. Chem. Hoppe-Seyler (1986) 367:627-642 !$#title The complete amino-acid sequence of C-phycoerythrin from the !1cyanobacterium Fremyella diplosiphon. !$#cross-references MUID:87000169; PMID:3092842 !$#note Fremyella diplosiphon !$#accession A24307 !'##molecule_type protein !'##residues 1-164 ##label SID GENETICS !$#gene cpeA CLASSIFICATION #superfamily phycocyanin KEYWORDS chromoprotein; heterodimer; phytochromobilin; thylakoid FEATURE !$1-164 #product C-phycoerythrin alpha chain #status !8experimental #label MAT\ !$82 #binding_site phycoerythrobilin (Cys) (covalent) !8#status experimental\ !$139 #binding_site phycoerythrobilin (Cys) (covalent) !8#status experimental SUMMARY #length 164 #molecular-weight 17626 #checksum 5191 SEQUENCE /// ENTRY CFMWB #type complete TITLE C-phycocyanin beta chain - Fischerella sp. ORGANISM #formal_name Fischerella sp. DATE 31-Jan-1980 #sequence_revision 31-Dec-1990 #text_change 30-Apr-1999 ACCESSIONS S02500; A00319; S02611 REFERENCE S02496 !$#authors Ruembeli, R.; Suter, F.; Wirth, M.; Sidler, W.; Zuber, H. !$#journal Biol. Chem. Hoppe-Seyler (1987) 368:1401-1406 !$#title Isolation and localization of N(4)-methylasparagine in !1phycobiliproteins from the cyanobacterium Mastigocladus !1laminosus. !$#cross-references MUID:88107006; PMID:3122783 !$#accession S02500 !'##molecule_type protein !'##residues 37-92 ##label RUE !'##note source designated as Mastigocladus laminosus REFERENCE A00315 !$#authors Frank, G.; Sidler, W.; Widmer, H.; Zuber, H. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1978) 359:1491-1507 !$#title The complete amino acid sequence of both subunits of !1C-phycocyanin from the cyanobacterium Mastigocladus !1laminosus. !$#cross-references MUID:79087164; PMID:103794 !$#accession A00319 !'##molecule_type protein !'##residues 1-71,'S',73,'TR',76,'GT',79-172 ##label FRA !'##note source designated as Mastigocladus laminosus !'##note sequence revised in reference S02496 REFERENCE S02611 !$#authors Ruembeli, R.; Suter, F.; Wirth, M.; Sidler, W.; Zuber, H. !$#journal FEBS Lett. (1987) 221:1-2 !$#title Gamma-N-methylasparagine in phycobiliproteins from the !1cyanobacteria Mastigocladus laminosus and Calothrix. !$#accession S02611 !'##molecule_type protein !'##residues 55-83 ##label RU2 !'##note source designated as Mastigocladus laminosus COMPLEX associates with alpha chain (see PIR:CFMWA) FUNCTION !$#description photon energy transfer from phycoerythrin to allophycocyanin !$#pathway photosynthesis CLASSIFICATION #superfamily phycocyanin KEYWORDS chromoprotein; methylated amino acid; photosynthesis; !1phycocyanobilin FEATURE !$72 #modified_site N4-methylasparagine (Asn) #status !8experimental\ !$82 #binding_site phycocyanobilin (Cys) (covalent) !8#status experimental\ !$153 #binding_site phycocyanobilin (Cys) (covalent) !8#status experimental SUMMARY #length 172 #molecular-weight 18390 #checksum 2978 SEQUENCE /// ENTRY CFKKB #type complete TITLE C-phycocyanin beta chain [validated] - red alga (Cyanidium caldarium) ORGANISM #formal_name Cyanidium caldarium DATE 02-Apr-1982 #sequence_revision 30-Apr-1999 #text_change 15-Sep-2000 ACCESSIONS A00320; B60844 REFERENCE A00320 !$#authors Troxler, R.F.; Ehrhardt, M.M.; Brown-Mason, A.S.; Offner, !1G.D. !$#journal J. Biol. Chem. (1981) 256:12176-12184 !$#title Primary structure of phycocyanin from the unicellular !1rhodophyte Cyanidium caldarium. II. Complete amino acid !1sequence of the beta subunit. !$#cross-references MUID:82053082; PMID:7028751 !$#accession A00320 !'##molecule_type protein !'##residues 1-71,'T',73-172 ##label TRO REFERENCE A60844 !$#authors Brown, A.S.; Offner, G.D.; Ehrhardt, M.M.; Troxler, R.F. !$#journal J. Biol. Chem. (1979) 254:7803-7811 !$#title Phycobilin-apoprotein linkages in the alpha and beta !1subunits of phycocyanin from the unicellular rhodophyte, !1Cyanidium caldarium. Amino acid sequences of (35)S-labeled !1chromopeptides. !$#cross-references MUID:79239364; PMID:468790 !$#accession B60844 !'##molecule_type protein !'##residues 80-86;136-166 ##label BRO REFERENCE A68150 !$#authors Stec, B.; Troxler, R.F.; Teeter, M.M. !$#submission submitted to the Brookhaven Protein Data Bank, June 1995 !$#cross-references PDB:1PHN !$#contents annotation; X-ray crystallography, 1.65 angstroms, residues !11-172 !$#note residue 72 is identified as N4-methylasparagine COMMENT This protein was isolated from the phycobilisomes on the !1chloroplasts of this unicellular, acido-thermal, eukaryote !1red alga. COMPLEX heterodimers of alpha (see PIR:CFKKA) and beta chains form !1larger multimers CLASSIFICATION #superfamily phycocyanin KEYWORDS chloroplast; chromoprotein; heterodimer; methylated amino !1acid; photosynthesis; phycocyanobilin FEATURE !$72 #modified_site N4-methylasparagine (Asn) #status !8experimental\ !$82 #binding_site phycocyanobilin (Cys) (covalent) !8#status experimental\ !$153 #binding_site phycocyanobilin (Cys) (covalent) !8#status experimental SUMMARY #length 172 #molecular-weight 18253 #checksum 4378 SEQUENCE /// ENTRY CFYCBB #type complete TITLE C-phycocyanin beta chain - Synechococcus sp. ORGANISM #formal_name Synechococcus sp. DATE 13-Aug-1986 #sequence_revision 13-Aug-1986 #text_change 11-Jun-1999 ACCESSIONS B94024; B94017; A00321; A22972 REFERENCE A94024 !$#authors de Lorimier, R.; Bryant, D.A.; Porter, R.D.; Liu, W.Y.; Jay, !1E.; Stevens Jr., S.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:7946-7950 !$#title Genes of the alpha and beta subunits of phycocyanin. !$#cross-references MUID:85088525; PMID:6096868 !$#note Agmenellum quadruplicatum !$#accession B94024 !'##molecule_type DNA !'##residues 1-172 ##label DEL !'##cross-references GB:K02660; NID:g142182; PIDN:AAB05343.1; !1PID:g142183 !'##experimental_source strain PR-6 REFERENCE A94017 !$#authors Pilot, T.J.; Fox, J.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:6983-6987 !$#title Cloning and sequencing of the genes encoding the alpha and !1beta subunits of C-phycocyanin from the cyanobacterium !1Agmenellum quadruplicatum. !$#cross-references MUID:85063716; PMID:6438628 !$#note Agmenellum quadruplicatum !$#accession B94017 !'##molecule_type DNA !'##residues 1-172 ##label PIL !'##cross-references GB:K02659; NID:g142176; PIDN:AAB05341.1; !1PID:g142177 !'##experimental_source strain PR-6 CLASSIFICATION #superfamily phycocyanin KEYWORDS chromoprotein; methylated amino acid; photosynthesis; !1phycocyanobilin FEATURE !$72 #modified_site N4-methylasparagine (Asn) #status !8predicted\ !$82 #binding_site phycocyanobilin (Cys) (covalent) !8#status predicted\ !$153 #binding_site phycocyanobilin (Cys) (covalent) !8#status predicted SUMMARY #length 172 #molecular-weight 18336 #checksum 6218 SEQUENCE /// ENTRY CFYCB #type complete TITLE C-phycocyanin beta chain - Synechococcus sp. (PCC 6301) ORGANISM #formal_name Synechococcus sp. #variety PCC 6301 #note Synechococcus sp. PCC 6301 (ATCC 27144) was named Anacystis nidulans in other culture collections, e.g., CCAP, SAUG, and UTEX DATE 30-Apr-1979 #sequence_revision 02-Jul-1996 #text_change 11-Jun-1999 ACCESSIONS A26577; S60069; S60074; A23999; A92224; A00322 REFERENCE A26577 !$#authors Lau, P.C.K.; Condie, J.A.; Alvarado-Urbina, G.; Lau, R.H. !$#journal Nucleic Acids Res. (1987) 15:2394 !$#title Nucleotide sequence of phycocyanin beta-subunit gene of !1cyanobacterium Anacystis nidulans strain R2. !$#cross-references MUID:87174767; PMID:3104880 !$#accession A26577 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-173 ##label LAU !'##cross-references GB:X04916; NID:g38899; PIDN:CAA28585.1; PID:g38900 !'##experimental_source strain R2 REFERENCE S60069 !$#authors Kalla, S.R.; Lind, L.K.; Lidholm, J.; Gustafsson, P. !$#journal J. Bacteriol. (1988) 170:2961-2970 !$#title Transcriptional organization of the phycocyanin subunit gene !1clusters of the cyanobacterium Anacystis nidulans UTEX 625. !$#cross-references MUID:88257006; PMID:2454910 !$#accession S60069 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-173 ##label KAL !'##cross-references EMBL:M94218; NID:g142121; PIDN:AAA64526.1; !1PID:g142122 !'##experimental_source strain PCC 6301 !'##note source designated as Anacystis nidulans !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June j1992 !$#accession S60074 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-173 ##label KA2 !'##cross-references EMBL:M94218; NID:g142121; PIDN:AAA64531.1; !1PID:g142127 !'##note the source is designated as Anacystis nidulans !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1992 REFERENCE A23999 !$#authors Lind, L.K.; Kalla, S.R.; Lonneborg, A.; Oquist, G.; !1Gustafsson, P. !$#journal FEBS Lett. (1985) 188:27-32 !$#title Cloning of the beta-phycocyanin gene from Anacystis !1nidulans. !$#accession A23999 !'##molecule_type DNA !'##residues 52-78 ##label LIN !'##note source designated as Anacystis nidulans REFERENCE A92224 !$#authors Freidenreich, P.; Apell, G.S.; Glazer, A.N. !$#journal J. Biol. Chem. (1978) 253:212-219 !$#title Structural studies on phycobiliproteins. II. C-phycocyanin: !1amino acid sequence of the beta subunit. Specific cleavage !1of the alpha subunit. !$#cross-references MUID:78066839; PMID:412848 !$#accession A92224 !'##molecule_type protein !'##residues 2-27,'SL',30-78,80-111,'D',113-120,'S',122-126,'L',128-157, !1159-173 ##label FRE REFERENCE A92223 !$#authors Williams, V.P.; Glazer, A.N. !$#journal J. Biol. Chem. (1978) 253:202-211 !$#title Structural studies on phycobiliproteins. I. Bilin-containing !1peptides of C-phycocyanin. !$#cross-references MUID:78066837; PMID:412846 !$#contents annotation; attachment sites of chromophores COMPLEX associates with alpha chain (see PIR:CFYCA) FUNCTION !$#description photon energy transfer from phycoerythrin to allophycocyanin !$#pathway photosynthesis CLASSIFICATION #superfamily phycocyanin KEYWORDS chromoprotein; methylated amino acid; photosynthesis; !1phycocyanobilin FEATURE !$2-173 #product C-phycocyanin beta chain #status !8experimental #label MAT\ !$73 #modified_site N4-methylasparagine (Asn) #status !8predicted\ !$83 #binding_site phycocyanobilin (Cys) (covalent) !8#status experimental\ !$154 #binding_site phycocyanobilin (Cys) (covalent) !8#status experimental SUMMARY #length 173 #molecular-weight 18269 #checksum 684 SEQUENCE /// ENTRY CFYCB3 #type complete TITLE R-phycocyanin II beta chain - Synechococcus sp. ORGANISM #formal_name Synechococcus sp. DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 20-Apr-2000 ACCESSIONS S17734; S31067; S31072; B26703; S27717; S31060 REFERENCE S17734 !$#authors Wilson, W.H.; Newman, J.; Mann, N.H.; Carr, N.G. !$#journal Plant Mol. Biol. (1991) 17:931-933 !$#title Cloning and sequence analysis of the phycocyanin genes of !1the marine cyanobacterium Synechococcus sp. WH7803. !$#cross-references MUID:92003705; PMID:1912508 !$#accession S17734 !'##molecule_type DNA !'##residues 1-172 ##label WIL !'##cross-references EMBL:X59809; NID:g48036; PIDN:CAA42479.1; !1PID:g48037 !'##experimental_source strain WH7803 REFERENCE S31066 !$#authors de Lorimier, R.; Wilbanks, S.M.; Glazer, A.N. !$#journal Plant Mol. Biol. (1993) 21:225-237 !$#title Genes of the R-phycocyanin II locus of marine Synechococcus !1spp., and comparison of protein-chromophore interactions in !1phycocyanins differing in bilin composition. !$#cross-references MUID:93144698; PMID:8425055 !$#accession S31067 !'##molecule_type DNA !'##residues 1-20,'T',22-32,'GR',35-41,'S',43-45,'N',47-57,'E',59-64, !1'A',66-67,'S',69-95,'SA',98,'T',100-124,'T',126-135,'DA', !1138-139,'S',141-149,'N',151-169,'S',171-172 ##label DEL !'##cross-references EMBL:M95288; NID:g154551; PIDN:AAA27345.1; !1PID:g154565 !'##experimental_source strain WH8020 !'##note the authors translated the codon AGG for residue 34 as Ser and !1TCC for residue 149 as Thr !$#accession S31072 !'##molecule_type DNA !'##residues 1-20,'T',22-64,'A',66-95,'SA',98,'T',100-104,'M',106-135, !1'DA',138-141,'I',143-144,'K',146-169,'S',171-172 ##label LOR !'##cross-references EMBL:M95289; NID:g154605; PIDN:AAA27365.1; !1PID:g154606 !'##experimental_source strain WH8103 REFERENCE A92644 !$#authors Ong, L.J.; Glazer, A.N. !$#journal J. Biol. Chem. (1987) 262:6323-6327 !$#title R-phycocyanin II, a new phycocyanin occurring in marine !1Synechococcus species. Identification of the terminal energy !1acceptor bilin in phycocyanins. !$#cross-references MUID:87194855; PMID:3571260 !$#accession B26703 !'##molecule_type protein !'##residues 2-20,'T';79-84;147-149,'X',151-158,'D',160-166 ##label ONG GENETICS !$#gene cpcB; rpcB CLASSIFICATION #superfamily phycocyanin KEYWORDS chromoprotein; methylated amino acid; photosynthesis; !1phycocyanobilin FEATURE !$2-172 #product R-phycocyanin II beta chain #status !8predicted #label MAT\ !$72 #modified_site N4-methylasparagine (Asn) #status !8predicted\ !$82 #binding_site phycocyanobilin (Cys) (covalent) !8#status predicted\ !$153 #binding_site phycocyanobilin (Cys) (covalent) !8#status predicted SUMMARY #length 172 #molecular-weight 17909 #checksum 1908 SEQUENCE /// ENTRY RFMWB #type complete TITLE phycoerythrocyanin beta chain - Fischerella sp. ORGANISM #formal_name Fischerella sp. #note Fischerella is a genus of nitrogen-fixing, thermophilic, branching, filamentous blue-green algae DATE 03-Aug-1984 #sequence_revision 12-Apr-1996 #text_change 29-Sep-1999 ACCESSIONS JQ0763; A00323 REFERENCE JQ0763 !$#authors Eberlein, M.; Kufer, W. !$#journal Gene (1990) 94:133-136 !$#title Genes encoding both subunits of phycoerythrocyanin, a !1light-harvesting biliprotein from the cyanobacterium !1Mastigocladus laminosus. !$#cross-references MUID:91033055; PMID:2121619 !$#accession JQ0763 !'##status preliminary !'##molecule_type DNA !'##residues 1-172 ##label EBE !'##cross-references GB:M34254; NID:g149774; PIDN:AAC64653.1; !1PID:g149775 REFERENCE A91722 !$#authors Fuglistaller, P.; Suter, F.; Zuber, H. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1983) 364:691-712 !$#title The complete amino-acid sequence of both subunits of !1phycoerythrocyanin from the thermophilic cyanobacterium !1Mastigocladus laminosus. !$#cross-references MUID:83289130; PMID:6411579 !$#accession A00323 !'##molecule_type protein !'##residues 1-171 ##label FUG !'##note the source is designated as Mastigocladus laminosus REFERENCE A30650 !$#authors Duerring, M.; Huber, R.; Bode, W.; Ruembeli, R.; Zuber, H. !$#journal J. Mol. Biol. (1990) 211:633-644 !$#title Refined three-dimensional structure of phycoerythrocyanin !1from the cyanobacterium Mastigocladus laminosus at 2.7 A. !$#cross-references MUID:90172426; PMID:2106585 !$#contents annotation; X-ray crystallography, 2.7 angstroms GENETICS !$#gene pecB COMPLEX heterodimer of alpha (see PIR:RFMWA) and beta chains; !1heterodimers associate to form trimeric and larger complexes FUNCTION !$#description phycobilisome light harvesting !$#pathway photosynthesis !$#note maximum absorption at approximately 550-570 nanometers CLASSIFICATION #superfamily phycocyanin KEYWORDS chromoprotein; light-harvesting complex; photosynthesis; !1phycocyanobilin; thylakoid FEATURE !$82 #binding_site phycocyanobilin (Cys) (covalent) !8#status predicted\ !$153 #binding_site phycocyanobilin (Cys) (covalent) !8#status predicted SUMMARY #length 172 #molecular-weight 18487 #checksum 5424 SEQUENCE /// ENTRY A41841 #type complete TITLE phycoerythrocyanin beta chain - Anabaena sp. (strain PCC 7120) ORGANISM #formal_name Anabaena sp. DATE 24-Sep-1999 #sequence_revision 24-Sep-1999 #text_change 20-Apr-2001 ACCESSIONS A41841 REFERENCE A41841 !$#authors Swanson, R.V.; de Lorimier, R.; Glazer, A.N. !$#journal J. Bacteriol. (1992) 174:2640-2647 !$#title Genes encoding the phycobilisome rod substructure are !1clustered on the Anabaena chromosome: characterization of !1the phycoerythrocyanin operon. !$#cross-references MUID:92210509; PMID:1556083 !$#accession A41841 !'##status preliminary !'##molecule_type DNA !'##residues 1-172 ##label SWA !'##cross-references GB:M80357; NID:g142069; PIDN:AAA22016.1; !1PID:g142070 REFERENCE A30654 !$#authors Bishop, J.E.; Rapoport, H.; Klotz, A.V.; Chan, C.F.; Glazer, !1A.N.; Fueglistaller, P.; Zuber, H. !$#journal J. Am. Chem. Soc. (1987) 109:875-881 !$#title Chromopeptides from phycoerythrocyanin. Structure and !1linkage of the three bilin groups. !$#contents annotation !$#note spectrographic characterization; peptide linkage COMPLEX heterodimer of alpha (see PIR:B41841) and beta chains; !1heterodimers associate to form trimeric and larger complexes FUNCTION !$#description phycobilisome light harvesting !$#pathway photosynthesis !$#note maximum absorption at approximately 550-570 nanometers CLASSIFICATION #superfamily phycocyanin KEYWORDS chromoprotein; light-harvesting complex; photosynthesis; !1phycocyanobilin; thylakoid FEATURE !$82 #binding_site phycocyanobilin (Cys) (covalent) !8#status experimental\ !$153 #binding_site phycocyanobilin (Cys) (covalent) !8#status experimental SUMMARY #length 172 #molecular-weight 18283 #checksum 3975 SEQUENCE /// ENTRY AFMDB #type complete TITLE phycoerythrin beta chain - Cryptomonas sp. chloroplast ORGANISM #formal_name chloroplast Cryptomonas sp. DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 30-Apr-1999 ACCESSIONS S14676; S10457 REFERENCE S14676 !$#authors Reith, M.; Douglas, S. !$#journal Plant Mol. Biol. (1990) 15:585-592 !$#title Localization of beta-phycoerythrin to the thylakoid lumen of !1Cryptomonas Phi does not involve a signal peptide. !$#cross-references MUID:91338697; PMID:2102376 !$#accession S14676 !'##molecule_type DNA !'##residues 1-177 ##label REI !'##cross-references EMBL:X52158; NID:g11383; PID:g11384 GENETICS !$#gene cpeB !$#genome chloroplast CLASSIFICATION #superfamily phycocyanin KEYWORDS chloroplast; chromoprotein; heterotetramer; methylated amino !1acid; phycocyanobilin; thylakoid FEATURE !$50,61 #binding_site phycocyanobilin (Cys) (covalent) !8#status predicted\ !$72 #modified_site N4-methylasparagine (Asn) #status !8predicted\ !$82 #binding_site phycocyanobilin (Cys) (covalent) !8#status predicted\ !$137-165 #disulfide_bonds #status predicted\ !$158 #binding_site phycocyanobilin (Cys) (covalent) !8#status predicted SUMMARY #length 177 #molecular-weight 18568 #checksum 7644 SEQUENCE /// ENTRY E22102 #type complete TITLE phycocyanin-645 beta chain - cryptomonad (Chroomonas sp.) ORGANISM #formal_name Chroomonas sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S10604; E22102 REFERENCE S10602 !$#authors Sidler, W.; Nutt, H.; Kumpf, B.; Frank, G.; Suter, F.; !1Brenzel, A.; Wehrmeyer, W.; Zuber, H. !$#journal Biol. Chem. Hoppe-Seyler (1990) 371:537-547 !$#title The complete amino-acid sequence and the phylogenetic origin !1of phycocyanin-645 from the cryptophytan alga Chroomonas !1sp.. !$#cross-references MUID:91025621; PMID:2222853 !$#accession S10604 !'##status preliminary !'##molecule_type protein !'##residues 1-177 ##label SID REFERENCE A94645 !$#authors Sidler, W.; Kumpf, B.; Suter, F.; Morisset, W.; Wehrmeyer, !1W.; Zuber, H. !$#journal Biol. Chem. Hoppe-Seyler (1985) 366:233-244 !$#title Structural studies on cryptomonad biliprotein subunits. Two !1different alpha-subunits in Chroomonas phycocyanin-645 and !1Cryptomonas phycoerythrin-545. !$#cross-references MUID:85225953; PMID:4005040 !$#accession E22102 !'##molecule_type protein !'##residues 1-31,'R',33-43 ##label SI2 COMPLEX heterotetramer of two alpha chains (see PIR:S10602 and !1PIR:S10603) and two beta chains CLASSIFICATION #superfamily phycocyanin KEYWORDS chromoprotein; heterotetramer; photosynthesis; !1phycocyanobilin FEATURE !$50,61 #binding_site cryptoviolin (Cys) (covalent) #status !8experimental\ !$82 #binding_site phycocyanobilin (Cys) (covalent) !8#status experimental\ !$158 #binding_site phycocyanobilin (Cys) (covalent) !8#status experimental SUMMARY #length 177 #molecular-weight 18388 #checksum 6788 SEQUENCE /// ENTRY CFXCB #type complete TITLE C-phycoerythrin beta chain - Calothrix sp. (strain PCC 7601) ORGANISM #formal_name Calothrix sp. DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jun-2000 ACCESSIONS B25527; B24307; S02614; S00286 REFERENCE A93645 !$#authors Mazel, D.; Guglielmi, G.; Houmard, J.; Sidler, W.; Bryant, !1D.A.; Tandeau de Marsac, N. !$#journal Nucleic Acids Res. (1986) 14:8279-8290 !$#title Green light induces transcription of the phycoerythrin !1operon in the cyanobacterium Calothrix 7601. !$#cross-references MUID:87066711; PMID:2431391 !$#accession B25527 !'##molecule_type DNA !'##residues 1-184 ##label MAZ !'##cross-references EMBL:X04592; NID:g1546895; PIDN:CAA28260.1; !1PID:g43389 REFERENCE A90711 !$#authors Sidler, W.; Kumpf, B.; Rudiger, W.; Zuber, H. !$#journal Biol. Chem. Hoppe-Seyler (1986) 367:627-642 !$#title The complete amino-acid sequence of C-phycoerythrin from the !1cyanobacterium Fremyella diplosiphon. !$#cross-references MUID:87000169; PMID:3092842 !$#note Fremyella diplosiphon !$#accession B24307 !'##molecule_type protein !'##residues 1-69,'S',71-184 ##label SID !'##note this sequence has been revised in reference S02611 REFERENCE S02611 !$#authors Ruembeli, R.; Suter, F.; Wirth, M.; Sidler, W.; Zuber, H. !$#journal FEBS Lett. (1987) 221:1-2 !$#title Gamma-N-methylasparagine in phycobiliproteins from the !1cyanobacteria Mastigocladus laminosus and Calothrix. !$#accession S02614 !'##molecule_type protein !'##residues 53-81 ##label RUE GENETICS !$#gene cpeB CLASSIFICATION #superfamily phycocyanin KEYWORDS chromoprotein; heterodimer; methylated amino acid; !1phytochromobilin; thylakoid FEATURE !$1-184 #product C-phycoerythrin beta chain #status !8experimental #label MAT\ !$48,59 #binding_site phycoerythrobilin (Cys) (covalent) !8#status experimental\ !$70 #modified_site N4-methylasparagine (Asn) #status !8experimental\ !$80 #binding_site phycoerythrobilin (Cys) (covalent) !8#status experimental\ !$165 #binding_site phycoerythrobilin (Cys) (covalent) !8#status experimental SUMMARY #length 184 #molecular-weight 19238 #checksum 9305 SEQUENCE /// ENTRY AFKKA #type complete TITLE allophycocyanin alpha chain - red alga (Cyanidium caldarium) ORGANISM #formal_name Cyanidium caldarium DATE 25-Feb-1985 #sequence_revision 12-Jul-1996 #text_change 15-Oct-1999 ACCESSIONS S37089; A00324 REFERENCE S37088 !$#authors Kostrzewa, M.; Zetsche, K. !$#submission submitted to the EMBL Data Library, August 1993 !$#accession S37089 !'##molecule_type DNA !'##residues 1-161 ##label KOS !'##cross-references EMBL:X74548; NID:g398386; PIDN:CAA52641.1; !1PID:g398388 !'##note the source is designated as Galdieria sulphuraria REFERENCE A92440 !$#authors Offner, G.D.; Troxler, R.F. !$#journal J. Biol. Chem. (1983) 258:9931-9940 !$#title Primary structure of allophycocyanin from the unicellular !1rhodophyte, Cyanidium caldarium. The complete amino acid !1sequences of the alpha and beta subunits. !$#cross-references MUID:83290919; PMID:6885776 !$#accession A00324 !'##molecule_type protein !'##residues 1,3-130,'D',132-145,'R',147-155,'KLP',159,'SS' ##label OFF GENETICS !$#gene apcA COMPLEX associates with beta chain (see PIR:AFKKB) FUNCTION !$#description photon energy transfer from phycocyanin to allophycocyanin-B !$#pathway photosynthesis CLASSIFICATION #superfamily phycocyanin KEYWORDS chloroplast; chromoprotein; photosynthesis; phycocyanobilin FEATURE !$81 #binding_site phycocyanobilin (Cys) (covalent) !8#status predicted SUMMARY #length 161 #molecular-weight 17532 #checksum 6031 SEQUENCE /// ENTRY AFMWA #type complete TITLE allophycocyanin alpha chain - Fischerella sp. ORGANISM #formal_name Fischerella sp. DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 30-Apr-1999 ACCESSIONS A00325 REFERENCE A00325 !$#authors Sidler, W.; Gysi, J.; Isker, E.; Zuber, H. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1981) 362:611-628 !$#title The complete amino acid sequence of both subunits of !1allophycocyanin, a light harvesting protein-pigment complex !1from the cyanobacterium Mastigocladus laminosus. !$#cross-references MUID:82005802; PMID:6792029 !$#accession A00325 !'##molecule_type protein !'##residues 1-160 ##label SID !'##note the source was designated as Mastigocladus laminosus COMMENT Allophycocyanin is a photosynthetic pigment-protein complex !1(with maximum absorption at approximately 650 nanometers) !1composed of two dissimilar chains. Both the alpha chain and !1the beta chain contain a covalently linked phycocyanobilin !1chromophore. CLASSIFICATION #superfamily phycocyanin KEYWORDS chromoprotein; photosynthesis; phycocyanobilin FEATURE !$80 #binding_site phycocyanobilin (Cys) (covalent) !8#status experimental SUMMARY #length 160 #molecular-weight 17121 #checksum 852 SEQUENCE /// ENTRY AFKTA #type complete TITLE allophycocyanin alpha chain - Cyanophora paradoxa cyanelle ORGANISM #formal_name cyanelle Cyanophora paradoxa DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 11-Jun-1999 ACCESSIONS A00326; C24650; T06847 REFERENCE A94045 !$#authors Bryant, D.A.; De Lorimier, R.; Lambert, D.H.; Dubbs, J.M.; !1Stirewalt, V.L.; Stevens Jr., S.E.; Porter, R.D.; Tam, J.; !1Jay, E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:3242-3246 !$#title Molecular cloning and nucleotide sequence of the alpha and !1beta subunits of allophycocyanin from the cyanelle genome of !1Cyanophora paradoxa. !$#cross-references MUID:85216477; PMID:2987916 !$#accession A00326 !'##molecule_type DNA !'##residues 1-161 ##label BRY !'##cross-references GB:M11159; NID:g336622; PIDN:AAA31693.1; !1PID:g336623 REFERENCE A91009 !$#authors Lemaux, P.G.; Grossman, A.R. !$#journal EMBO J. (1985) 4:1911-1919 !$#title Major light-harvesting polypeptides encoded in polycistronic !1transcripts in a eukaryotic alga. !$#cross-references MUID:86055745; PMID:2998775 !$#accession C24650 !'##molecule_type DNA !'##residues 1-15 ##label LEM !'##cross-references GB:X02791; NID:g11377; PIDN:CAA26558.1; PID:g951229 REFERENCE Z15840 !$#authors Stirewalt, V.L.; Michalowski, C.B.; Luffelhardt, W.; !1Bohnert, H.J.; Bryant, D.A. !$#submission submitted to the EMBL Data Library, July 1995 !$#description Nucleotide sequence of the cyanelle genome from Cyanophora !1paradoxa. !$#accession T06847 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-161 ##label STI !'##cross-references EMBL:U30821; NID:g1016083; PIDN:AAA81190.1; !1PID:g1016103 !'##experimental_source strain Pringsheim LB555 GENETICS !$#gene apcA !$#genome cyanelle COMPLEX heterotetramer of two alpha and two beta chains (see !1PIR:AFKTB) CLASSIFICATION #superfamily phycocyanin KEYWORDS chromoprotein; cyanelle; heterotetramer; photosynthesis; !1phycocyanobilin FEATURE !$81 #binding_site phycocyanobilin (Cys) (covalent) !8#status predicted SUMMARY #length 161 #molecular-weight 17278 #checksum 5111 SEQUENCE /// ENTRY AFAIAC #type complete TITLE allophycocyanin alpha chain - Anabaena cylindrica ORGANISM #formal_name Anabaena cylindrica DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 30-Apr-1999 ACCESSIONS A24224 REFERENCE A91349 !$#authors Minami, Y.; Yamada, F.; Hase, T.; Matsubara, H.; Murakami, !1A.; Fujita, Y.; Takao, T.; Shimonishi, Y. !$#journal FEBS Lett. (1985) 191:216-220 !$#title Amino acid sequences of allophycocyanin alpha- and !1beta-subunits isolated from Anabaena cylindrica. !$#accession A24224 !'##molecule_type protein !'##residues 1-160 ##label MIN COMMENT This protein is a common component of light-gathering !1protein complexes called phycobilisomes, which are involved !1in the energy transfer process to chlorophyll a. CLASSIFICATION #superfamily phycocyanin KEYWORDS chromoprotein; photosynthesis; phycocyanobilin FEATURE !$80 #binding_site phycocyanobilin (Cys) (covalent) !8#status experimental SUMMARY #length 160 #molecular-weight 17081 #checksum 4631 SEQUENCE /// ENTRY AFKTB #type complete TITLE allophycocyanin beta chain - Cyanophora paradoxa cyanelle ORGANISM #formal_name cyanelle Cyanophora paradoxa DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 11-Jun-1999 ACCESSIONS A00327; D24650; T06846 REFERENCE A94045 !$#authors Bryant, D.A.; De Lorimier, R.; Lambert, D.H.; Dubbs, J.M.; !1Stirewalt, V.L.; Stevens Jr., S.E.; Porter, R.D.; Tam, J.; !1Jay, E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:3242-3246 !$#title Molecular cloning and nucleotide sequence of the alpha and !1beta subunits of allophycocyanin from the cyanelle genome of !1Cyanophora paradoxa. !$#cross-references MUID:85216477; PMID:2987916 !$#accession A00327 !'##molecule_type DNA !'##residues 1-161 ##label BRY !'##cross-references GB:M11159; NID:g336622; PIDN:AAA31694.1; !1PID:g336624 REFERENCE A91009 !$#authors Lemaux, P.G.; Grossman, A.R. !$#journal EMBO J. (1985) 4:1911-1919 !$#title Major light-harvesting polypeptides encoded in polycistronic !1transcripts in a eukaryotic alga. !$#cross-references MUID:86055745; PMID:2998775 !$#accession D24650 !'##molecule_type DNA !'##residues 1-15 ##label LEM !'##cross-references GB:X02792; NID:g11379; PIDN:CAA26559.1; PID:g11380 REFERENCE Z15840 !$#authors Stirewalt, V.L.; Michalowski, C.B.; Luffelhardt, W.; !1Bohnert, H.J.; Bryant, D.A. !$#submission submitted to the EMBL Data Library, July 1995 !$#description Nucleotide sequence of the cyanelle genome from Cyanophora !1paradoxa. !$#accession T06846 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-161 ##label STI !'##cross-references EMBL:U30821; NID:g1016083; PIDN:AAA81189.1; !1PID:g1016102 !'##experimental_source strain Pringsheim LB555 GENETICS !$#gene apcB !$#genome cyanelle CLASSIFICATION #superfamily phycocyanin KEYWORDS chromoprotein; cyanelle; methylated amino acid; !1photosynthesis; phycocyanobilin FEATURE !$71 #modified_site N4-methylasparagine (Asn) #status !8predicted\ !$81 #binding_site phycocyanobilin (Cys) (covalent) !8#status predicted SUMMARY #length 161 #molecular-weight 17282 #checksum 5552 SEQUENCE /// ENTRY AFAIB #type complete TITLE allophycocyanin beta chain - Anabaena variabilis ORGANISM #formal_name Anabaena variabilis DATE 18-Dec-1981 #sequence_revision 18-Dec-1981 #text_change 30-Apr-1999 ACCESSIONS A00328; A61422 REFERENCE A00328 !$#authors DeLange, R.J.; Williams, L.C.; Glazer, A.N. !$#journal J. Biol. Chem. (1981) 256:9558-9566 !$#title The amino acid sequence of the beta subunit of !1allophycocyanin. !$#cross-references MUID:82030740; PMID:6793571 !$#accession A00328 !'##molecule_type protein !'##residues 1-161 ##label DEL REFERENCE A61422 !$#authors Klotz, A.V.; Leary, J.A.; Glazer, A.N. !$#journal J. Biol. Chem. (1986) 261:15891-15894 !$#title Post-translational methylation of asparaginyl residues. !1Identification of beta-71 gamma-N-methylasparagine in !1allophycocyanin. !$#cross-references MUID:87057240; PMID:3782095 !$#accession A61422 !'##molecule_type protein !'##residues 63-71 ##label KLO CLASSIFICATION #superfamily phycocyanin KEYWORDS chromoprotein; methylated amino acid; photosynthesis; !1phycocyanobilin FEATURE !$71 #modified_site N4-methylasparagine (Asn) #status !8experimental\ !$81 #binding_site phycocyanobilin (Cys) (covalent) !8#status experimental SUMMARY #length 161 #molecular-weight 17186 #checksum 4890 SEQUENCE /// ENTRY AFAIBC #type complete TITLE allophycocyanin beta chain - Anabaena cylindrica ORGANISM #formal_name Anabaena cylindrica DATE 28-Dec-1987 #sequence_revision 08-Nov-1996 #text_change 30-Apr-1999 ACCESSIONS B24224 REFERENCE A91349 !$#authors Minami, Y.; Yamada, F.; Hase, T.; Matsubara, H.; Murakami, !1A.; Fujita, Y.; Takao, T.; Shimonishi, Y. !$#journal FEBS Lett. (1985) 191:216-220 !$#title Amino acid sequences of allophycocyanin alpha- and !1beta-subunits isolated from Anabaena cylindrica. !$#accession B24224 !'##molecule_type protein !'##residues 1-70,'D',72-161 ##label MIN !'##note residue 71 presented as Asp was identified as !1N4-hydroxymethylasparagine; therefore, we have shown it as !1Asn COMMENT This protein is a common component of light-gathering !1protein complexes called phycobilisomes, which are involved !1in the energy transfer process to chlorophyll a. CLASSIFICATION #superfamily phycocyanin KEYWORDS chromoprotein; methylated amino acid; photosynthesis; !1phycocyanobilin FEATURE !$71 #modified_site asparagine derivative (Asn) (probably !8N4-hydroxymethylasparagine) #status experimental\ !$81 #binding_site phycocyanobilin (Cys) (covalent) !8#status predicted SUMMARY #length 161 #molecular-weight 17315 #checksum 6020 SEQUENCE /// ENTRY AFMWB #type complete TITLE allophycocyanin beta chain - Fischerella sp. ORGANISM #formal_name Fischerella sp. DATE 14-Nov-1983 #sequence_revision 31-Dec-1990 #text_change 30-Apr-1999 ACCESSIONS S02501; A00329; S02612 REFERENCE S02496 !$#authors Ruembeli, R.; Suter, F.; Wirth, M.; Sidler, W.; Zuber, H. !$#journal Biol. Chem. Hoppe-Seyler (1987) 368:1401-1406 !$#title Isolation and localization of N(4)-methylasparagine in !1phycobiliproteins from the cyanobacterium Mastigocladus !1laminosus. !$#cross-references MUID:88107006; PMID:3122783 !$#accession S02501 !'##molecule_type protein !'##residues 59-82 ##label RUE !'##note source designated as Mastigocladus laminosus REFERENCE A00325 !$#authors Sidler, W.; Gysi, J.; Isker, E.; Zuber, H. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1981) 362:611-628 !$#title The complete amino acid sequence of both subunits of !1allophycocyanin, a light harvesting protein-pigment complex !1from the cyanobacterium Mastigocladus laminosus. !$#cross-references MUID:82005802; PMID:6792029 !$#accession A00329 !'##molecule_type protein !'##residues 1-58,'LT',61-66,'L',68-70,'D',72-161 ##label SID !'##note source designated as Mastigocladus laminosus !'##note sequence revised in reference S02496 REFERENCE S02611 !$#authors Ruembeli, R.; Suter, F.; Wirth, M.; Sidler, W.; Zuber, H. !$#journal FEBS Lett. (1987) 221:1-2 !$#title Gamma-N-methylasparagine in phycobiliproteins from the !1cyanobacteria Mastigocladus laminosus and Calothrix. !$#accession S02612 !'##molecule_type protein !'##residues 55-82 ##label RU2 !'##note source designated as Mastigocladus laminosus COMMENT This phycocyanin beta chain contains only one covalently !1attached chromophore. COMPLEX associates with alpha chain (see PIR:AFMWA) FUNCTION !$#description photon energy transfer from phycocyanin to allophycocyanin-B !$#pathway photosynthesis CLASSIFICATION #superfamily phycocyanin KEYWORDS chromoprotein; methylated amino acid; photosynthesis; !1phycocyanobilin FEATURE !$71 #modified_site N4-methylasparagine (Asn) #status !8experimental\ !$81 #binding_site phycocyanobilin (Cys) (covalent) !8#status experimental SUMMARY #length 161 #molecular-weight 17374 #checksum 4693 SEQUENCE /// ENTRY AFKKB #type complete TITLE allophycocyanin beta chain - red alga (Cyanidium caldarium) chloroplast ORGANISM #formal_name chloroplast Cyanidium caldarium DATE 25-Feb-1985 #sequence_revision 12-Jul-1996 #text_change 01-Dec-2000 ACCESSIONS S37090; S70823; A00330; S36414 REFERENCE S37088 !$#authors Kostrzewa, M.; Zetsche, K. !$#submission submitted to the EMBL Data Library, August 1993 !$#accession S37090 !'##molecule_type DNA !'##residues 1-161 ##label KOS1 !'##cross-references EMBL:X74548; NID:g398386; PIDN:CAA52642.1; !1PID:g398389 !'##note the source is designated as Galdieria sulphuraria REFERENCE S39512 !$#authors Kostrzewa, M.; Zetsche, K. !$#journal Plant Mol. Biol. (1993) 23:67-76 !$#title Organization of plastid-encoded ATPase genes and flanking !1regions including homologues of infB and tsf in the !1thermophilic red alga Galdieria sulphuraria. !$#cross-references MUID:94033298; PMID:8219057 !$#accession S70823 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 51-161 ##label KOS2 !'##cross-references EMBL:X66698; NID:g396522; PIDN:CAA47243.1; !1PID:g396527 !'##note the source is designated as Galdieria sulphuraria !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1992 REFERENCE A92440 !$#authors Offner, G.D.; Troxler, R.F. !$#journal J. Biol. Chem. (1983) 258:9931-9940 !$#title Primary structure of allophycocyanin from the unicellular !1rhodophyte, Cyanidium caldarium. The complete amino acid !1sequences of the alpha and beta subunits. !$#cross-references MUID:83290919; PMID:6885776 !$#accession A00330 !'##molecule_type protein !'##residues 1-22,'I',24-69,'LD',72-93,'L',95-142,'P',144-161 ##label !1OFF GENETICS !$#gene apcB !$#genome chloroplast COMPLEX associates with alpha chain (see PIR:AFKKA) FUNCTION !$#description photon energy transfer from phycocyanin to allophycocyanin-B !$#pathway photosynthesis CLASSIFICATION #superfamily phycocyanin KEYWORDS chloroplast; chromoprotein; methylated amino acid; !1photosynthesis; phycocyanobilin FEATURE !$71 #modified_site N4-methylasparagine (Asn) #status !8predicted\ !$81 #binding_site phycocyanobilin (Cys) (covalent) !8#status predicted SUMMARY #length 161 #molecular-weight 17407 #checksum 4298 SEQUENCE /// ENTRY AFMWB6 #type complete TITLE phycobiliprotein 16.2 beta chain - Fischerella sp. ORGANISM #formal_name Fischerella sp. DATE 28-Dec-1987 #sequence_revision 31-Dec-1990 #text_change 30-Apr-1999 ACCESSIONS A26428; S02502; S02613 REFERENCE A26428 !$#authors Ruembeli, R.; Wirth, M.; Suter, F.; Zuber, H. !$#journal Biol. Chem. Hoppe-Seyler (1987) 368:1-9 !$#title The phycobiliprotein beta-16.2 of the allophycocyanin core !1from the cyanobacterium Mastigocladus laminosus. !$#cross-references MUID:87157096; PMID:3103645 !$#accession A26428 !'##molecule_type protein !'##residues 1-71,'S',73-169 ##label RUE2 !'##note the source is designated as Mastigocladus laminosus !'##note this sequence has been revised in reference S02496 REFERENCE S02496 !$#authors Ruembeli, R.; Suter, F.; Wirth, M.; Sidler, W.; Zuber, H. !$#journal Biol. Chem. Hoppe-Seyler (1987) 368:1401-1406 !$#title Isolation and localization of N(4)-methylasparagine in !1phycobiliproteins from the cyanobacterium Mastigocladus !1laminosus. !$#cross-references MUID:88107006; PMID:3122783 !$#accession S02502 !'##molecule_type protein !'##residues 58-100 ##label RUE1 !'##note the source is designated as Mastigocladus laminosus REFERENCE S02611 !$#authors Ruembeli, R.; Suter, F.; Wirth, M.; Sidler, W.; Zuber, H. !$#journal FEBS Lett. (1987) 221:1-2 !$#title Gamma-N-methylasparagine in phycobiliproteins from the !1cyanobacteria Mastigocladus laminosus and Calothrix. !$#accession S02613 !'##molecule_type protein !'##residues 55-83 ##label RUE !'##note the source is designated as Mastigocladus laminosus FUNCTION !$#description this is one of the components of phycobilisomes, which are !1high-molecular mass complexes of phycobiliproteins attached !1to the photosynthetic membranes of cyanobacteria and red !1algae; it is a protein functionally equivalent to, but with !1weaker absorbance than, allophycocyanin beta chain CLASSIFICATION #superfamily phycocyanin KEYWORDS chromoprotein; methylated amino acid; photosynthesis; !1phycocyanobilin FEATURE !$72 #modified_site N4-methylasparagine (Asn) #status !8experimental\ !$82 #binding_site phycocyanobilin (Cys) (covalent) !8#status experimental SUMMARY #length 169 #molecular-weight 18845 #checksum 7818 SEQUENCE /// ENTRY S74962 #type complete TITLE probable allophycocyanin linker protein - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein sll1509 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S74962 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74962 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-109 ##label KAN !'##cross-references EMBL:D90902; GB:AB001339; NID:g1652027; !1PIDN:BAA17002.1; PID:g1652077 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily probable allophycocyanin linker protein SUMMARY #length 109 #molecular-weight 12555 #checksum 2697 SEQUENCE /// ENTRY S25307 #type complete TITLE probable allophycocyanin linker protein - red alga (Cyanidium caldarium) chloroplast ORGANISM #formal_name chloroplast Cyanidium caldarium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S25307 REFERENCE S25306 !$#authors Valentin, K.; Maid, U.; Emich, A.; Zetsche, K. !$#journal Plant Mol. Biol. (1992) 20:267-276 !$#title Organization and expression of a phycobiliprotein gene !1cluster from the unicellular red alga Cyanidium caldarium. !$#cross-references MUID:93004479; PMID:1391770 !$#accession S25307 !'##molecule_type DNA !'##residues 1-83 ##label VAL !'##cross-references EMBL:X57251; NID:g17969; PIDN:CAA40532.1; !1PID:g17971 GENETICS !$#gene apcL !$#genome chloroplast CLASSIFICATION #superfamily probable allophycocyanin linker protein KEYWORDS chloroplast SUMMARY #length 83 #molecular-weight 9485 #checksum 4421 SEQUENCE /// ENTRY S73135 #type complete TITLE probable allophycocyanin linker protein - red alga (Porphyra purpurea) chloroplast ORGANISM #formal_name chloroplast Porphyra purpurea DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S73135 REFERENCE S73108 !$#authors Reith, M.; Munholland, J. !$#journal Plant Mol. Biol. Rep. (1995) 13:333-335 !$#title Complete nucleotide sequence of the Porphyra purpurea !1chloroplast genome. !$#accession S73135 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-108 ##label REI !'##cross-references EMBL:U38804; NID:g1276652; PIDN:AAC08100.1; !1PID:g1276680 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1995 GENETICS !$#gene ycf20 !$#genome chloroplast CLASSIFICATION #superfamily probable allophycocyanin linker protein KEYWORDS chloroplast SUMMARY #length 108 #molecular-weight 11875 #checksum 8292 SEQUENCE /// ENTRY S59989 #type complete TITLE allophycocyanin core-associated linker subunit L8c - Synechocystis sp. ALTERNATE_NAMES hypothetical protein ssr3383; phycobilisome LC linker protein; small core linker protein ORGANISM #formal_name Synechocystis sp. #variety PCC 6714 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S59989; S75014; C44462 REFERENCE S33623 !$#authors DiMagno, L.; Haselkorn, R. !$#journal Plant Mol. Biol. (1993) 21:835-845 !$#title Isolation and characterization of the genes encoding !1allophycocyanin subunits and two linker proteins from !1Synechocystis 6714. !$#cross-references MUID:93222481; PMID:8467079 !$#accession S59989 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-67 ##label DIM !'##cross-references EMBL:L02308; NID:g154449; PIDN:AAA69684.1; !1PID:g154452 !'##experimental_source PCC 6714 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1September 1992 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75014 !'##molecule_type DNA !'##residues 1-67 ##label KAN !'##cross-references EMBL:D90910; GB:AB001339; NID:g1652956; !1PIDN:BAA17876.1; PID:g1652959 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 REFERENCE A44462 !$#authors Su, X.; Fraenkel, P.G.; Bogorad, L. !$#journal J. Biol. Chem. (1992) 267:22944-22950 !$#title Excitation energy transfer from phycocyanin to chlorophyll !1in an apcA-defective mutant of Synechocystis sp. PCC 6803. !$#cross-references MUID:93054612; PMID:1429645 !$#accession C44462 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-35,'S',37-67 ##label SU1 !'##cross-references GB:M77135; NID:g154453; PIDN:AAA27278.1; !1PID:g154456 !'##experimental_source PCC 6803 !'##note sequence extracted from NCBI backbone (NCBIP:118111) GENETICS !$#gene apcC CLASSIFICATION #superfamily allophycocyanin linker protein SUMMARY #length 67 #molecular-weight 7805 #checksum 2161 SEQUENCE /// ENTRY C27873 #type complete TITLE allophycocyanin linker protein - Synechococcus sp. (PCC 6301) ORGANISM #formal_name Synechococcus sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C27873 REFERENCE A93127 !$#authors Houmard, J.; Mazel, D.; Moguet, C.; Bryant, D.A.; Tandeau de !1Marsac, N. !$#journal Mol. Gen. Genet. (1986) 205:404-410 !$#title Organization and nucleotide sequence of genes encoding core !1components of the phycobilisomes from Synechococcus 6301. !$#cross-references MUID:87172294; PMID:3031427 !$#accession C27873 !'##molecule_type DNA !'##residues 1-67 ##label HOU !'##cross-references GB:X04716; NID:g46819; PIDN:CAA28423.1; PID:g46822 !'##experimental_source PCC 6301 CLASSIFICATION #superfamily allophycocyanin linker protein SUMMARY #length 67 #molecular-weight 7809 #checksum 718 SEQUENCE /// ENTRY D31385 #type complete TITLE allophycocyanin linker protein L (C-7.8) - Calothrix sp. ORGANISM #formal_name Calothrix sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS D31385; C30764 REFERENCE A91890 !$#authors Houmard, J.; Capuano, V.; Coursin, T.; Tandeau de Marsac, N. !$#journal J. Bacteriol. (1988) 170:5512-5521 !$#title Genes encoding core components of the phycobilisome in the !1cyanobacterium Calothrix sp. strain PCC 7601: occurrence of !1a multigene family. !$#cross-references MUID:89053869; PMID:2461358 !$#accession D31385 !'##molecule_type DNA !'##residues 1-68 ##label HOU !'##cross-references GB:M20806; GB:M31224; NID:g148538; PIDN:AAA24876.1; !1PID:g148542 !'##experimental_source PCC 7601 CLASSIFICATION #superfamily allophycocyanin linker protein SUMMARY #length 68 #molecular-weight 7889 #checksum 2302 SEQUENCE /// ENTRY S00284 #type complete TITLE allophycocyanin linker protein, 8.9K - Fischerella sp. ORGANISM #formal_name Fischerella sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S00284 REFERENCE S00284 !$#authors Fueglistaller, P.; Ruembeli, R.; Suter, F.; Zuber, H. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1984) 365:1085-1096 !$#title Minor polypeptides from the phycobilisome of the !1cyanobacterium Mastigocladus laminosus. Isolation, !1characterization and amino-acid sequences of a colourless !18.9-kDa polypeptide and of a 16.2-kDa phycobiliprotein. !$#accession S00284 !'##molecule_type protein !'##residues 1-67 ##label FUE !'##note 9-Ser was also found !'##note the source is designated as Mastigocladus laminosus CLASSIFICATION #superfamily allophycocyanin linker protein SUMMARY #length 67 #molecular-weight 7741 #checksum 2394 SEQUENCE /// ENTRY FKPUZ #type complete TITLE phytochrome - zucchini ORGANISM #formal_name Cucurbita pepo var. melopepo #common_name zucchini DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 11-Jun-1999 ACCESSIONS S00099 REFERENCE S00099 !$#authors Sharrock, R.A.; Lissemore, J.L.; Quail, P.H. !$#journal Gene (1986) 47:287-295 !$#title Nucleotide and amino acid sequence of a Cucurbita !1phytochrome cDNA clone: identification of conserved features !1by comparison with Avena phytochrome. !$#cross-references MUID:87163500; PMID:3557123 !$#accession S00099 !'##molecule_type mRNA !'##residues 1-1124 ##label SHA !'##cross-references EMBL:M15265; NID:g167500; PIDN:AAA33115.1; !1PID:g167501 CLASSIFICATION #superfamily phytochrome; phytochrome homology KEYWORDS chromoprotein; homodimer; photoreceptor; phytochromobilin; !1transcription regulation FEATURE !$67-581 #domain phytochrome homology #label PHYT\ !$867-1124 #domain signal transduction #label STD\ !$323 #binding_site phytochromobilin (Cys) (covalent) !8#status predicted SUMMARY #length 1124 #molecular-weight 125081 #checksum 3834 SEQUENCE /// ENTRY FKMUA #type complete TITLE phytochrome A - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 11-Jun-1999 ACCESSIONS A33473; S07719 REFERENCE A33473 !$#authors Sharrock, R.A.; Quail, P.H. !$#journal Genes Dev. (1989) 3:1745-1757 !$#title Novel phytochrome sequences in Arabidopsis thaliana: !1structure, evolution, and differential expression of a plant !1regulatory photoreceptor family. !$#cross-references MUID:90108670; PMID:2606345 !$#accession A33473 !'##molecule_type mRNA !'##residues 1-1122 ##label SHA !'##cross-references EMBL:X17341; NID:g16420; PIDN:CAA35221.1; !1PID:g16421 GENETICS !$#gene phyA CLASSIFICATION #superfamily phytochrome; phytochrome homology KEYWORDS chromoprotein; dimer; photoreceptor; phytochromobilin; !1transcription regulation FEATURE !$67-583 #domain phytochrome homology #label PHYT\ !$869-1122 #domain signal transduction #label STD\ !$323 #binding_site phytochromobilin (Cys) (covalent) !8#status predicted SUMMARY #length 1122 #molecular-weight 124485 #checksum 3656 SEQUENCE /// ENTRY FKMUB #type complete TITLE phytochrome B - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 24-May-2001 ACCESSIONS B33473; JQ2141; F84568; S07718 REFERENCE A33473 !$#authors Sharrock, R.A.; Quail, P.H. !$#journal Genes Dev. (1989) 3:1745-1757 !$#title Novel phytochrome sequences in Arabidopsis thaliana: !1structure, evolution, and differential expression of a plant !1regulatory photoreceptor family. !$#cross-references MUID:90108670; PMID:2606345 !$#accession B33473 !'##molecule_type mRNA !'##residues 1-1172 ##label SHA !'##cross-references EMBL:X17342; NID:g16422; PIDN:CAA35222.1; !1PID:g16423 REFERENCE JQ2141 !$#authors Reed, J.W.; Nagpal, P.; Poole, D.S.; Furuya, M.; Chory, J. !$#journal Plant Cell (1993) 5:147-157 !$#title Mutations in the gene for the red/far-red light receptor !1phytochrome B alter cell elongation and physiological !1responses throughout Arabidopsis development. !$#cross-references MUID:93200802; PMID:8453299 !$#accession JQ2141 !'##molecule_type DNA !'##residues 1-1172 ##label REE !'##cross-references GB:L09262 !'##experimental_source ecotype Landsberg, mutant hy3 REFERENCE A84420 !$#authors Lin, X.; Kaul, S.; Rounsley, S.D.; Shea, T.P.; Benito, M.I.; !1Town, C.D.; Fujii, C.Y.; Mason, T.M.; Bowman, C.L.; !1Barnstead, M.E.; Feldblyum, T.V.; Buell, C.R.; Ketchum, !1K.A.; Lee, J.J.; Ronning, C.M.; Koo, H.; Moffat, K.S.; !1Cronin, L.A.; Shen, M.; VanAken, S.E.; Umayam, L.; Tallon, !1L.J.; Gill, J.E.; Adams, M.D.; Carrera, A.J.; Creasy, T.H.; !1Goodman, H.M.; Somerville, C.R.; Copenhaver, G.P.; Preuss, !1D.; Nierman, W.C.; White, O.; Eisen, J.A.; Salzberg, S.L.; !1Fraser, C.M.; Venter, J.C. !$#journal Nature (1999) 402:761-768 !$#title Sequence and analysis of chromosome 2 of the plant !1Arabidopsis thaliana. !$#cross-references MUID:20083487; PMID:10617197 !$#accession F84568 !'##status preliminary !'##molecule_type DNA !'##residues 1-1172 ##label STO !'##cross-references GB:AE002093; NID:g4185145; PIDN:AAD08948.1; !1GSPDB:GN00139 GENETICS !$#gene phyB; At2g18790 !$#map_position 2 !$#introns 722/1; 991/2; 1088/2 CLASSIFICATION #superfamily phytochrome; phytochrome homology KEYWORDS chromoprotein; dimer; photoreceptor; phytochromobilin; !1transcription regulation FEATURE !$101-614 #domain phytochrome homology #label PHYT\ !$901-1172 #domain signal transduction #label STD\ !$357 #binding_site phytochromobilin (Cys) (covalent) !8#status predicted SUMMARY #length 1172 #molecular-weight 129330 #checksum 6013 SEQUENCE /// ENTRY FKMUC #type complete TITLE phytochrome C - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 11-Jun-1999 ACCESSIONS C33473; S07717 REFERENCE A33473 !$#authors Sharrock, R.A.; Quail, P.H. !$#journal Genes Dev. (1989) 3:1745-1757 !$#title Novel phytochrome sequences in Arabidopsis thaliana: !1structure, evolution, and differential expression of a plant !1regulatory photoreceptor family. !$#cross-references MUID:90108670; PMID:2606345 !$#accession C33473 !'##molecule_type mRNA !'##residues 1-1111 ##label SHA !'##cross-references EMBL:X17343; NID:g16424; PIDN:CAA35223.1; !1PID:g16425 GENETICS !$#gene phyC CLASSIFICATION #superfamily phytochrome; phytochrome homology KEYWORDS chromoprotein; dimer; photoreceptor; phytochromobilin; !1transcription regulation FEATURE !$62-573 #domain phytochrome homology #label PHYT\ !$856-1111 #domain signal transduction #label STD\ !$318 #binding_site phytochromobilin (Cys) (covalent) !8#status predicted SUMMARY #length 1111 #molecular-weight 123721 #checksum 3846 SEQUENCE /// ENTRY S27396 #type complete TITLE phytochrome / protein kinase (EC 2.7.1.-) - moss (Ceratodon purpureus) ORGANISM #formal_name Ceratodon purpureus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S27396; S20160; S12966 REFERENCE S27396 !$#authors Thuemmler, F.; Dufner, M.; Kreisl, P.; Dittrich, P. !$#journal Plant Mol. Biol. (1992) 20:1003-1017 !$#title Molecular cloning of a novel phytochrome gene of the moss !1Ceratodon purpureus which encodes a putative light-regulated !1protein kinase. !$#cross-references MUID:93099252; PMID:1463836 !$#accession S27396 !'##molecule_type DNA !'##residues 1-1303 ##label THU !'##cross-references GB:U87632; GB:S51224; NID:g1839247 REFERENCE S20160 !$#authors Thuemmler, F.; Dufner, M.; Kreisl, P.; Dittrich, P. !$#submission submitted to the Protein Sequence Database, April 1992 !$#description Molecular cloning of a novel phytochrome gene of the moss !1Ceratodon purpureus which encodes a putative light regulated !1protein kinase. !$#accession S20160 !'##molecule_type DNA !'##residues 1-1303 ##label TH2 !'##cross-references GB:U87632; GB:S51224; NID:g1839247 REFERENCE S12966 !$#authors Thuemmler, F.; Beetz, A.; Ruediger, W. !$#journal FEBS Lett. (1990) 275:125-129 !$#title Phytochrome in lower plants. Detection and partial sequence !1of a phytochrome gene in the moss Ceratodon purpureus using !1the polymerase chain reaction. !$#cross-references MUID:91085543; PMID:2261981 !$#accession S12966 !'##molecule_type DNA !'##residues 49-539 ##label FEB !'##cross-references GB:X17084; NID:g296090 GENETICS !$#gene phy !$#introns 679/1; 779/1 CLASSIFICATION #superfamily phytochrome / protein kinase; phytochrome !1homology; protein kinase homology KEYWORDS ATP; chromoprotein; phosphotransferase; photoreceptor; !1phytochromobilin; serine/threonine-specific protein kinase; !1transcription regulation FEATURE !$63-575 #domain phytochrome homology #label PHYT\ !$1002-1289 #domain protein kinase homology #label KIN\ !$320 #binding_site phytochromobilin (Cys) (covalent) !8#status predicted SUMMARY #length 1303 #molecular-weight 145369 #checksum 4924 SEQUENCE /// ENTRY S74389 #type complete TITLE phytochrome phy - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES hypothetical protein slr0473 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 25-Apr-1997 #sequence_revision 25-Apr-1997 #text_change 03-Feb-2003 ACCESSIONS S74389 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74389 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-748 ##label KAN !'##cross-references EMBL:D64001; GB:AB001339; NID:g1001102; !1PIDN:BAA10307.1; PID:g1001165 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene phy CLASSIFICATION #superfamily bacteriophytochrome; phytochrome homology KEYWORDS chromoprotein; photoreceptor; phytochromobilin FEATURE !$2-504 #domain phytochrome homology #label PHYT\ !$507-745 #domain sensor histidine kinase homology #label SHK\ !$259 #binding_site phytochromobilin (Cys) (covalent) !8#status predicted SUMMARY #length 748 #molecular-weight 84232 #checksum 4183 SEQUENCE /// ENTRY JC5446 #type complete TITLE photoactive yellow protein - Ectothiorhodospira halophila ORGANISM #formal_name Ectothiorhodospira halophila DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Dec-1999 ACCESSIONS B55993; A37428; JC5446 REFERENCE A55993 !$#authors Baca, M.; Borgstahl, G.E.O.; Boissinot, M.; Burke, P.M.; !1Williams, D.R.; Slater, K.A.; Getzoff, E.D. !$#journal Biochemistry (1994) 33:14369-14377 !$#title Complete chemical structure of photoactive yellow protein: !1novel thioester-linked 4-hydroxycinnamyl chromophore and !1photocycle chemistry. !$#cross-references MUID:95072006; PMID:7981196 !$#accession B55993 !'##molecule_type DNA !'##residues 1-125 ##label BAC !'##cross-references GB:U17017; NID:g602427; PIDN:AAA61735.1; !1PID:g602429 REFERENCE A37428 !$#authors Van Beeumen, J.J.; Devreese, B.V.; Van Bun, S.M.; Hoff, !1W.D.; Hellingwerf, K.J.; Meyer, T.E.; McRee, D.E.; !1Cusanovich, M.A. !$#journal Protein Sci. (1993) 2:1114-1125 !$#title Primary structure of a photoactive yellow protein from the !1phototrophic bacterium Ectothiorhodospira halophila, with !1evidence for the mass and the binding site of the !1chromophore. !$#cross-references MUID:93364264; PMID:8358295 !$#accession A37428 !'##molecule_type protein !'##residues 1-55,'E',57-125 ##label VAN REFERENCE JC5446 !$#authors Mihara, K.; Hisatomi, O.; Imamoto, Y.; Kataoka, M.; !1Tokunaga, F. !$#journal J. Biochem. (1997) 121:876-880 !$#title Functional expression and site-directed mutagenesis of !1photoactive yellow protein. !$#cross-references MUID:97335933; PMID:9192728 !$#contents annotation COMMENT This small, soluble protein functions as a photoreceptor for !1the negative phototaxis of this organism. GENETICS !$#gene pyp CLASSIFICATION #superfamily Ectothiorhodospira halophila photoactive yellow !1protein KEYWORDS chromoprotein; photoreceptor; thiolester bond FEATURE !$69 #binding_site 4-hydroxycinnamyl (Cys) (covalent) !8#status experimental SUMMARY #length 125 #molecular-weight 13874 #checksum 5335 SEQUENCE /// ENTRY FXME #type complete TITLE flavodoxin - Megasphaera elsdenii ORGANISM #formal_name Megasphaera elsdenii DATE 13-Jul-1981 #sequence_revision 13-Jul-1981 #text_change 07-May-1999 ACCESSIONS A92137; A92156; A00331 REFERENCE A92137 !$#authors Tanaka, M.; Haniu, M.; Yasunobu, K.T.; Mayhew, S.; Massey, !1V. !$#journal J. Biol. Chem. (1973) 248:4354-4366 !$#cross-references MUID:73197809; PMID:4711610 !$#accession A92137 !'##molecule_type protein !'##residues 1-77,'GKKLK',83-137 ##label TAN !'##experimental_source strain LC1 REFERENCE A92156 !$#authors Tanaka, M.; Haniu, M.; Yasunobu, K.T.; Mayhew, S.G.; Massey, !1V. !$#journal J. Biol. Chem. (1974) 249:4397 !$#title Correction of the amino acid sequence of Peptostreptococcus !1elsdenii flavodoxin. !$#cross-references MUID:74277393; PMID:4843143 !$#accession A92156 !'##molecule_type protein !'##residues 78-82 ##label TA2 REFERENCE A61338 !$#authors Tanaka, M.; Haniu, M.; Matsueda, G.; Yasunobu, K.T.; Mayhew, !1S.; Massey, V. !$#journal Biochemistry (1971) 10:3041-3046 !$#title Amino- and carboxyl-terminal amino acid sequences of the !1Peptostreptococcus elsdenii and Clostridium pasteurianum !1flavodoxins. !$#cross-references MUID:72062407; PMID:5126921 !$#contents annotation COMMENT Some anaerobic bacteria, when grown on iron-deficient media, !1produce flavodoxin instead of ferredoxin, which flavodoxin !1can replace in certain reactions. CLASSIFICATION #superfamily flavodoxin; flavodoxin homology KEYWORDS electron transfer; flavoprotein; FMN FEATURE !$4-135 #domain flavodoxin homology #label FLX SUMMARY #length 137 #molecular-weight 14550 #checksum 8682 SEQUENCE /// ENTRY A39414 #type complete TITLE flavodoxin - Enterobacter agglomerans plasmid pEA3 ALTERNATE_NAMES electron transport protein nifF ORGANISM #formal_name Enterobacter agglomerans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A39414 REFERENCE A39414 !$#authors Kreutzer, R.; Dayananda, S.; Klingmueller, W. !$#journal J. Bacteriol. (1991) 173:3252-3256 !$#title Cotranscription of the electron transport protein genes nifJ !1and nifF in Enterobacter agglomerans 333. !$#cross-references MUID:91217003; PMID:1708766 !$#accession A39414 !'##molecule_type DNA !'##residues 1-177 ##label KRE !'##cross-references GB:M38221; NID:g145132; PIDN:AAA23385.1; !1PID:g145134 GENETICS !$#gene nifF !$#genome plasmid CLASSIFICATION #superfamily flavodoxin; flavodoxin homology KEYWORDS electron transfer; flavoprotein; FMN FEATURE !$6-173 #domain flavodoxin homology #label FLX SUMMARY #length 177 #molecular-weight 19581 #checksum 1188 SEQUENCE /// ENTRY S02511 #type complete TITLE flavodoxin - Klebsiella pneumoniae ORGANISM #formal_name Klebsiella pneumoniae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S02511 REFERENCE S01836 !$#authors Arnold, W.; Rump, A.; Klipp, W.; Priefer, U.B.; Puehler, A. !$#journal J. Mol. Biol. (1988) 203:715-738 !$#title Nucleotide sequence of a 24,206-base-pair DNA fragment !1carrying the entire nitrogen fixation gene cluster of !1Klebsiella pneumoniae. !$#cross-references MUID:89094839; PMID:3062178 !$#accession S02511 !'##molecule_type DNA !'##residues 1-176 ##label ARN !'##cross-references EMBL:X13303; NID:g43820; PIDN:CAA31680.1; !1PID:g43836 GENETICS !$#gene nifF CLASSIFICATION #superfamily flavodoxin; flavodoxin homology KEYWORDS electron transfer; flavoprotein; FMN FEATURE !$6-172 #domain flavodoxin homology #label FLX SUMMARY #length 176 #molecular-weight 19112 #checksum 6687 SEQUENCE /// ENTRY FXDV #type complete TITLE flavodoxin - Desulfovibrio vulgaris ORGANISM #formal_name Desulfovibrio vulgaris DATE 24-Apr-1984 #sequence_revision 31-Dec-1993 #text_change 11-Jun-1999 ACCESSIONS A31991; S06447; A00333; S45692 REFERENCE A31991 !$#authors Krey, G.D.; Vanin, E.F.; Swenson, R.P. !$#journal J. Biol. Chem. (1988) 263:15436-15443 !$#title Cloning, nucleotide sequence, and expression of the !1flavodoxin gene from Desulfovibrio vulgaris (Hildenborough). !$#cross-references MUID:89008444; PMID:3170590 !$#accession A31991 !'##molecule_type DNA !'##residues 1-148 ##label KRE !'##cross-references GB:J04033; NID:g145088; PIDN:AAA23367.1; !1PID:g145089 REFERENCE S06447 !$#authors Curley, G.P.; Voordouw, G. !$#journal FEMS Microbiol. Lett. (1988) 49:295-299 !$#title Cloning and sequencing of the gene encoding flavodoxin from !1Desulfovibrio vulgaris Hildenborough. !$#accession S06447 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-148 ##label CUR REFERENCE A92199 !$#authors Dubourdieu, M.; Fox, J.L. !$#journal J. Biol. Chem. (1977) 252:1453-1463 !$#title Amino acid sequence of Desulfovibrio vulgaris flavodoxin. !$#cross-references MUID:77118626; PMID:402366 !$#accession A00333 !'##molecule_type protein !'##residues 1-27,'N',29-148 ##label DUB !'##experimental_source strain Hildenborough REFERENCE A93786 !$#authors Watenpaugh, K.D.; Sieker, L.C.; Jensen, L.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1973) 70:3857-3860 !$#title The binding of riboflavin-5'-phosphate in a flavoprotein: !1flavodoxin at 2.0 angstrom resolution. !$#cross-references MUID:74087652; PMID:4521211 !$#contents annotation; X-ray crystallography, 2.0 angstroms !$#note the flavin mononucleotide binding site is described REFERENCE A93781 !$#authors Watenpaugh, K.D.; Sieker, L.C.; Jensen, L.H.; LeGall, J.; !1Dubourdieu, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1972) 69:3185-3188 !$#title Structure of the oxidized form of a flavodoxin at !12.5-angstrom resolution: resolution of the phase ambiguity !1by anomalous scattering. !$#cross-references MUID:73044810; PMID:4508313 !$#contents annotation; X-ray crystallography, 2.5 angstroms REFERENCE S45692 !$#authors Pirola, M.C.; Monti, F.; Aliverti, A.; Zanetti, G. !$#journal Arch. Biochem. Biophys. (1994) 311:480-486 !$#title A functional heterologous electron-transfer protein complex: !1Desulfovibrio vulgaris flavodoxin covalently linked to !1spinach ferredoxin-NADP(+) reductase. !$#cross-references MUID:94263229; PMID:8203913 !$#accession S45692 !'##molecule_type protein !'##residues 2-15 ##label PIR COMMENT No disulfide bonds are present. CLASSIFICATION #superfamily flavodoxin; flavodoxin homology KEYWORDS electron transfer; flavoprotein; FMN FEATURE !$1-148 #product flavodoxin #status experimental #label MAT\ !$6-145 #domain flavodoxin homology #label FLX\ !$10-15,58-62,95-102 #region FMN-phosphate binding #status experimental SUMMARY #length 148 #molecular-weight 15823 #checksum 7783 SEQUENCE /// ENTRY A34640 #type complete TITLE flavodoxin - Desulfovibrio salexigens ORGANISM #formal_name Desulfovibrio salexigens DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A34640 REFERENCE A34640 !$#authors Helms, L.R.; Krey, G.D.; Swenson, R.P. !$#journal Biochem. Biophys. Res. Commun. (1990) 168:809-817 !$#title Identification, sequence determination, and expression of !1the flavodoxin gene from Desulfovibrio salexigens. !$#cross-references MUID:90241257; PMID:2334437 !$#accession A34640 !'##status preliminary !'##molecule_type DNA !'##residues 1-146 ##label HEL !'##cross-references GB:M35475; NID:g145090; PIDN:AAA23368.1; !1PID:g145091 CLASSIFICATION #superfamily flavodoxin; flavodoxin homology KEYWORDS electron transfer; flavoprotein; FMN FEATURE !$6-143 #domain flavodoxin homology #label FLX SUMMARY #length 146 #molecular-weight 15812 #checksum 6139 SEQUENCE /// ENTRY S24310 #type complete TITLE flavodoxin - Desulfovibrio gigas (ATCC 29494) ORGANISM #formal_name Desulfovibrio gigas DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 05-May-2000 ACCESSIONS S24310 REFERENCE S24310 !$#authors Helms, L.R.; Swenson, R.P. !$#journal Biochim. Biophys. Acta (1992) 1131:325-328 !$#title The primary structures of the flavodoxins from two strains !1of Desulfovibrio gigas. Cloning and nucleotide sequence of !1the structural genes. !$#cross-references MUID:92329549; PMID:1627649 !$#accession S24310 !'##molecule_type DNA !'##residues 1-147 ##label HEL !'##cross-references EMBL:X64765; NID:g40798; PIDN:CAA46012.1; !1PID:g40799 !'##experimental_source strain ATCC 29494 CLASSIFICATION #superfamily flavodoxin; flavodoxin homology KEYWORDS electron transfer; flavoprotein; FMN FEATURE !$6-143 #domain flavodoxin homology #label FLX SUMMARY #length 147 #molecular-weight 15186 #checksum 5946 SEQUENCE /// ENTRY S24311 #type complete TITLE flavodoxin - Desulfovibrio gigas (ATCC 19364) ORGANISM #formal_name Desulfovibrio gigas DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 05-May-2000 ACCESSIONS S24311 REFERENCE S24310 !$#authors Helms, L.R.; Swenson, R.P. !$#journal Biochim. Biophys. Acta (1992) 1131:325-328 !$#title The primary structures of the flavodoxins from two strains !1of Desulfovibrio gigas. Cloning and nucleotide sequence of !1the structural genes. !$#cross-references MUID:92329549; PMID:1627649 !$#accession S24311 !'##molecule_type DNA !'##residues 1-146 ##label HEL !'##cross-references EMBL:X64766; NID:g40800; PIDN:CAA46013.1; !1PID:g40801 !'##experimental_source strain ATCC 19364 CLASSIFICATION #superfamily flavodoxin; flavodoxin homology KEYWORDS electron transfer; flavoprotein; FMN FEATURE !$6-143 #domain flavodoxin homology #label FLX SUMMARY #length 146 #molecular-weight 15470 #checksum 8676 SEQUENCE /// ENTRY FXDVD #type complete TITLE flavodoxin - Desulfovibrio desulfuricans (ATCC 29577) ORGANISM #formal_name Desulfovibrio desulfuricans DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 11-Jun-1999 ACCESSIONS S17000 REFERENCE S17000 !$#authors Helms, L.R.; Swenson, R.P. !$#journal Biochim. Biophys. Acta (1991) 1089:417-419 !$#title Cloning and characterization of the flavodoxin gene from !1Desulfovibrio desulfuricans. !$#cross-references MUID:91316149; PMID:1859847 !$#accession S17000 !'##molecule_type DNA !'##residues 1-148 ##label HEL !'##cross-references EMBL:X59438; NID:g40796; PIDN:CAA42064.1; !1PID:g40797 !'##experimental_source strain ATCC 29577 CLASSIFICATION #superfamily flavodoxin; flavodoxin homology KEYWORDS electron transfer; flavoprotein; FMN FEATURE !$6-145 #domain flavodoxin homology #label FLX SUMMARY #length 148 #molecular-weight 15694 #checksum 5039 SEQUENCE /// ENTRY FXCLEX #type complete TITLE flavodoxin - Clostridium sp. ORGANISM #formal_name Clostridium sp. DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 05-Apr-1995 ACCESSIONS A00332 REFERENCE A92155 !$#authors Tanaka, M.; Haniu, M.; Yasunobu, K.T.; Mayhew, S.G. !$#journal J. Biol. Chem. (1974) 249:4393-4396 !$#title The amino acid sequence of the Clostridium MP flavodoxin. !$#cross-references MUID:74277392; PMID:4843142 !$#accession A00332 !'##molecule_type protein !'##residues 1-138 ##label TAN !'##experimental_source strain MP REFERENCE A92154 !$#authors Burnett, R.M.; Darling, G.D.; Kendall, D.S.; LeQuesne, M.E.; !1Mayhew, S.G.; Smith, W.W.; Ludwig, M.L. !$#journal J. Biol. Chem. (1974) 249:4383-4392 !$#title The structure of the oxidized form of clostridial flavodoxin !1at 1.9-A resolution. Description of the flavin !1mononucleotide binding site. !$#cross-references MUID:74277391; PMID:4843141 !$#contents annotation; X-ray crystallography, 1.9 angstroms, oxidized !1form !$#note no disulfide bonds are present CLASSIFICATION #superfamily flavodoxin; flavodoxin homology KEYWORDS electron transfer; flavoprotein; FMN FEATURE !$3-136 #domain flavodoxin homology #label FLX SUMMARY #length 138 #molecular-weight 15332 #checksum 1338 SEQUENCE /// ENTRY FXAVEP #type complete TITLE flavodoxin - Azotobacter vinelandii ORGANISM #formal_name Azotobacter vinelandii DATE 24-Apr-1984 #sequence_revision 20-Aug-1994 #text_change 11-Jun-1999 ACCESSIONS A29935; A00334 REFERENCE A29935 !$#authors Bennett, L.T.; Jacobson, M.R.; Dean, D.R. !$#journal J. Biol. Chem. (1988) 263:1364-1369 !$#title Isolation, sequencing, and mutagenesis of the nifF gene !1encoding flavodoxin from Azotobacter vinelandii. !$#cross-references MUID:88087273; PMID:3121629 !$#accession A29935 !'##molecule_type DNA !'##residues 1-180 ##label BEN !'##cross-references GB:J03519; NID:g142373; PIDN:AAA22154.1; !1PID:g142374 REFERENCE A00334 !$#authors Tanaka, M.; Haniu, M.; Yasunobu, K.T.; Yoch, D.C. !$#journal Biochemistry (1977) 16:3525-3537 !$#title Complete amino acid sequence of azotoflavin, a flavodoxin !1from Azotobacter vinelandii. !$#cross-references MUID:77242321; PMID:889809 !$#accession A00334 !'##molecule_type protein !'##residues 2-180 ##label TAN !'##experimental_source strain OP GENETICS !$#gene nifF CLASSIFICATION #superfamily flavodoxin; flavodoxin homology KEYWORDS electron transfer; flavoprotein; FMN FEATURE !$2-180 #product flavodoxin #status experimental #label MAT\ !$6-173 #domain flavodoxin homology #label FLX SUMMARY #length 180 #molecular-weight 19663 #checksum 7465 SEQUENCE /// ENTRY A28670 #type complete TITLE flavodoxin [validated] - Synechococcus sp. ORGANISM #formal_name Synechococcus sp. DATE 19-Feb-1999 #sequence_revision 19-Feb-1999 #text_change 17-Nov-2000 ACCESSIONS A28670; A05103 REFERENCE A28670 !$#authors Laudenbach, D.E.; Reith, M.E.; Straus, N.A. !$#journal J. Bacteriol. (1988) 170:258-265 !$#title Isolation, sequence analysis, and transcriptional studies of !1the flavodoxin gene from Anacystis nidulans R2. !$#cross-references MUID:88086879; PMID:3121586 !$#accession A28670 !'##molecule_type DNA !'##residues 1-170 ##label LAU !'##cross-references GB:M19116; NID:g142132; PIDN:AAA22050.1; !1PID:g142133 !'##note the source is designated as Anacystis nidulans REFERENCE A05103 !$#authors Smith, W.W.; Pattridge, K.A.; Ludwig, M.L.; Petsko, G.A.; !1Tsernoglou, D.; Tanaka, M.; Yasunobu, K.T. !$#journal J. Mol. Biol. (1983) 165:737-755 !$#cross-references MUID:83216115; PMID:6406674 !$#contents sequence; X-ray crystallography, oxidized form, 2.5 !1angstroms !$#accession A05103 !'##molecule_type protein !'##residues 2-54,'S',56;167,'GF',170 ##label SMI REFERENCE A51893 !$#authors Smith, W.W.; Pattridge, K.A.; Luschinsky, C.L.; Ludwig, M.L. !$#submission submitted to the Brookhaven Protein Data Bank, June 1992 !$#cross-references PDB:1OFV !$#contents annotation; X-ray crystallography, 1.7 angstroms, residues !12-170 !$#note oxidized form; the source is designated as Anacystis !1nidulans CLASSIFICATION #superfamily flavodoxin; flavodoxin homology KEYWORDS electron transfer; flavoprotein; FMN FEATURE !$2-170 #product flavodoxin #status experimental #label MAT\ !$6-165 #domain flavodoxin homology #label FLX\ !$10-15,58-62,90-100 #region FMN-phosphate binding #status experimental SUMMARY #length 170 #molecular-weight 18777 #checksum 9910 SEQUENCE /// ENTRY S38632 #type complete TITLE flavodoxin - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein sll0248 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S38632; S75085; B56811 REFERENCE S38632 !$#authors Poncelet, M.G.; Cassier-Chauvat, C.J.; Chauvat, F.R. !$#submission submitted to the EMBL Data Library, November 1993 !$#description Sequence of the flavodoxin gene from Synechocystis PCC6803. !$#accession S38632 !'##status preliminary !'##molecule_type DNA !'##residues 1-170 ##label PON !'##cross-references EMBL:Z27091; NID:g415403; PIDN:CAA81614.1; !1PID:g415404 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75085 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-170 ##label KAN !'##cross-references EMBL:D90910; GB:AB001339; NID:g1652956; !1PIDN:BAA17947.1; PID:g1653030 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 REFERENCE A56811 !$#authors Bottin, H.; Lagoutte, B. !$#journal Biochim. Biophys. Acta (1992) 1101:48-56 !$#title Ferredoxin and flavodoxin from the cyanobacterium !1Synechocystis sp PCC 6803. !$#cross-references MUID:92338182; PMID:1633177 !$#accession B56811 !'##molecule_type protein !'##residues 1,3-24,'X',26-34,'X',36-40,'A',41-42 ##label BOT !'##note sequence extracted from NCBI backbone (NCBIP:109694) GENETICS !$#gene isiB CLASSIFICATION #superfamily flavodoxin; flavodoxin homology KEYWORDS electron transfer; flavoprotein; FMN FEATURE !$6-165 #domain flavodoxin homology #label FLX SUMMARY #length 170 #molecular-weight 18822 #checksum 9516 SEQUENCE /// ENTRY B47673 #type complete TITLE flavodoxin isiB - Synechococcus sp. (PCC 7002) ORGANISM #formal_name Synechococcus sp. DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS B47673 REFERENCE A47673 !$#authors Leonhardt, K.; Straus, N.A. !$#journal J. Gen. Microbiol. (1992) 138:1613-1621 !$#title An iron stress operon involved in photosynthetic electron !1transport in the marine cyanobacterium Synechococcus sp. PCC !17002. !$#cross-references MUID:92407507; PMID:1527503 !$#accession B47673 !'##molecule_type DNA !'##residues 1-170 ##label LEO !'##cross-references GB:M88253; NID:g154526; PIDN:AAA27318.1; !1PID:g154528 !'##experimental_source PCC 7002 !'##note sequence extracted from NCBI backbone (NCBIN:113303, !1NCBIP:113305) GENETICS !$#gene isiB CLASSIFICATION #superfamily flavodoxin; flavodoxin homology KEYWORDS electron transfer; flavoprotein; FMN FEATURE !$6-165 #domain flavodoxin homology #label FLX SUMMARY #length 170 #molecular-weight 18479 #checksum 4008 SEQUENCE /// ENTRY S04600 #type complete TITLE flavodoxin - Anabaena variabilis ORGANISM #formal_name Anabaena variabilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S04600; S05277 REFERENCE S04600 !$#authors Leonhardt, K.G.; Straus, N.A. !$#journal Nucleic Acids Res. (1989) 17:4384 !$#title Sequence of the flavodoxin gene from Anabaena variabilis !17120. !$#cross-references MUID:89296496; PMID:2500643 !$#accession S04600 !'##molecule_type DNA !'##residues 1-170 ##label LEO1 !'##cross-references EMBL:X14577; NID:g312908; PIDN:CAA32720.1; !1PID:g312909 REFERENCE S05277 !$#authors Leonhardt, K.G. !$#submission submitted to the EMBL Data Library, March 1989 !$#accession S05277 !'##molecule_type DNA !'##residues 1,'X',3-21,'X',23-170 ##label LEO2 !'##cross-references EMBL:X14577 CLASSIFICATION #superfamily flavodoxin; flavodoxin homology KEYWORDS electron transfer; flavoprotein; FMN FEATURE !$7-165 #domain flavodoxin homology #label FLX SUMMARY #length 170 #molecular-weight 18964 #checksum 345 SEQUENCE /// ENTRY S06648 #type complete TITLE flavodoxin - red alga (Chondrus crispus) ORGANISM #formal_name Chondrus crispus #common_name carragheen DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S06648 REFERENCE S06648 !$#authors Wakabayashi, S.; Kimura, T.; Fukuyama, K.; Matsubara, H.; !1Rogers, L.J. !$#journal Biochem. J. (1989) 263:981-984 !$#title The amino acid sequence of a flavodoxin from the eukaryotic !1red alga Chondrus crispus. !$#cross-references MUID:90088453; PMID:2597140 !$#accession S06648 !'##molecule_type protein !'##residues 1-173 ##label WAK CLASSIFICATION #superfamily flavodoxin; flavodoxin homology KEYWORDS electron transfer; flavoprotein; FMN FEATURE !$4-168 #domain flavodoxin homology #label FLX SUMMARY #length 173 #molecular-weight 18871 #checksum 837 SEQUENCE /// ENTRY A38177 #type complete TITLE flavodoxin - Clostridium acetobutylicum ORGANISM #formal_name Clostridium acetobutylicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A38177 REFERENCE A38177 !$#authors Santangelo, J.D.; Jones, D.T.; Woods, D.R. !$#journal J. Bacteriol. (1991) 173:1088-1095 !$#title Metronidazole activation and isolation of Clostridium !1acetobutylicum electron transport genes. !$#cross-references MUID:91123180; PMID:1991710 !$#accession A38177 !'##molecule_type DNA !'##residues 1-160 ##label SAN !'##cross-references GB:M36770; NID:g144813; PIDN:AAA23238.1; !1PID:g144814 CLASSIFICATION #superfamily flavodoxin; flavodoxin homology KEYWORDS electron transfer; flavoprotein; FMN FEATURE !$5-160 #domain flavodoxin homology #label FLX SUMMARY #length 160 #molecular-weight 17763 #checksum 8907 SEQUENCE /// ENTRY C64053 #type complete TITLE flavodoxin A - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C64053 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession C64053 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-174 ##label TIGR !'##cross-references GB:U32704; GB:L42023; NID:g1573143; !1PIDN:AAC21860.1; PID:g1573149; TIGR:HI0191 !'##note named as homolog to a protein from Escherichia coli CLASSIFICATION #superfamily flavodoxin; flavodoxin homology KEYWORDS electron transfer; flavoprotein; FMN FEATURE !$6-165 #domain flavodoxin homology #label FLX SUMMARY #length 174 #molecular-weight 19627 #checksum 8175 SEQUENCE /// ENTRY A37319 #type complete TITLE flavodoxin A - Escherichia coli (strain K-12) ALTERNATE_NAMES flavodoxin 1 ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS A37319; C64803 REFERENCE A37319 !$#authors Osborne, C.; Chen, L.M.; Matthews, R.G. !$#journal J. Bacteriol. (1991) 173:1729-1737 !$#title Isolation, cloning, mapping, and nucleotide sequencing of !1the gene encoding flavodoxin in Escherichia coli. !$#cross-references MUID:91154129; PMID:1999390 !$#accession A37319 !'##status preliminary !'##molecule_type DNA !'##residues 1-176 ##label OSB !'##cross-references GB:M59426; NID:g145985; PIDN:AAA23789.1; !1PID:g145986 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64803 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-176 ##label BLAT !'##cross-references GB:AE000172; GB:U00096; NID:g1786896; !1PIDN:AAC73778.1; PID:g1786900; UWGP:b0684 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene fldA !$#map_position 15.9 min CLASSIFICATION #superfamily flavodoxin; flavodoxin homology KEYWORDS electron transfer; flavoprotein; FMN FEATURE !$6-165 #domain flavodoxin homology #label FLX SUMMARY #length 176 #molecular-weight 19737 #checksum 9726 SEQUENCE /// ENTRY A31998 #type complete TITLE electron transfer flavoprotein alpha chain precursor - human ORGANISM #formal_name Homo sapiens #common_name man DATE 21-May-1990 #sequence_revision 12-Jul-1996 #text_change 11-Jun-1999 ACCESSIONS A31998 REFERENCE A31998 !$#authors Finocchiaro, G.; Ito, M.; Ikeda, Y.; Tanaka, K. !$#journal J. Biol. Chem. (1988) 263:15773-15780 !$#title Molecular cloning and nucleotide sequence of cDNAs encoding !1the alpha-subunit of human electron transfer flavoprotein. !$#cross-references MUID:89008492; PMID:3170610 !$#accession A31998 !'##molecule_type mRNA !'##residues 1-333 ##label FIN !'##cross-references GB:J04058; PIDN:AAA52406.1; PID:g182251; !1NID:g182250 !'##note an upstream inphase ATG was considered unlikely to be the !1initiator because the predicted transit peptide would not be !1positively charged, both the precursor and the mature !1peptide would be larger than is found, and a product !1synthesized in vitro using this Met as initiator was not !1imported into mitochondria whereas the precursor shown was !1processed and imported !'##note amino end of the mature protein is blocked GENETICS !$#gene GDB:ETFA !'##cross-references GDB:119121; OMIM:231680 !$#map_position 15q23-15q25 !$#note defects cause glutaric aciduria type II or !1ethylmalonic-adipic aciduria COMPLEX heterodimer of alpha and beta chains (see PIR:S32482) that !1binds one molecule of FAD FUNCTION !$#description electron transfer from any of several dehydrogenases in the !1mitochondrial matrix to the mitochondrial respiratory chain !1via electron-transferring-flavoprotein dehydrogenase CLASSIFICATION #superfamily electron transfer flavoprotein alpha chain KEYWORDS blocked amino end; electron transfer; FAD; flavoprotein; !1heterodimer; mitochondrial matrix FEATURE !$1-25 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$26-333 #product electron transfer flavoprotein alpha chain !8#status predicted #label MAT SUMMARY #length 333 #molecular-weight 35079 #checksum 5479 SEQUENCE /// ENTRY A31568 #type complete TITLE electron transfer flavoprotein alpha chain precursor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1990 #sequence_revision 12-Jul-1996 #text_change 11-Jun-1999 ACCESSIONS A31568; B31568; B31998 REFERENCE A31568 !$#authors Shinzawa, K.; Inagaki, T.; Ohishi, N.; Ichihara, C.; !1Tsukagoshi, N.; Udaka, S.; Yagi, K. !$#journal Biochem. Biophys. Res. Commun. (1988) 155:300-304 !$#title Molecular cloning of a cDNA for alpha-subunit of rat liver !1electron transfer flavoprotein. !$#cross-references MUID:88326316; PMID:3415685 !$#accession A31568 !'##molecule_type mRNA !'##residues 'EGTAGLTRTET',1-289 ##label SH2 !'##cross-references GB:M22030; NID:g204069; PIDN:AAA41130.1; !1PID:g204070 !$#accession B31568 !'##status translation not shown !'##molecule_type mRNA !'##residues 290-333 ##label SHI !'##cross-references GB:M22030 !'##note sequence obtained by translating residues 900-1034 of the !1GenBank entry !'##note authors' translation ended prematurely because of a missing !1residue in the nucleotide sequence REFERENCE A31998 !$#authors Finocchiaro, G.; Ito, M.; Ikeda, Y.; Tanaka, K. !$#journal J. Biol. Chem. (1988) 263:15773-15780 !$#title Molecular cloning and nucleotide sequence of cDNAs encoding !1the alpha-subunit of human electron transfer flavoprotein. !$#cross-references MUID:89008492; PMID:3170610 !$#accession B31998 !'##molecule_type protein !'##residues 86-101;140-146;189-203;207-216;250-268;'D',296-331 ##label !1FIN COMPLEX heterodimer of alpha and beta chains that binds one molecule !1of FAD FUNCTION !$#description electron transfer from any of several dehydrogenases in the !1mitochondrial matrix to the mitochondrial respiratory chain !1via electron-transferring-flavoprotein dehydrogenase CLASSIFICATION #superfamily electron transfer flavoprotein alpha chain KEYWORDS blocked amino end; electron transfer; FAD; flavoprotein; !1heterodimer; mitochondrial matrix FEATURE !$1-25 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$26-333 #product electron transfer flavoprotein alpha chain !8#status predicted #label MAT SUMMARY #length 333 #molecular-weight 34976 #checksum 5777 SEQUENCE /// ENTRY S49188 #type complete TITLE electron transfer flavoprotein alpha chain fixB homolog - Azotobacter vinelandii ORGANISM #formal_name Azotobacter vinelandii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S49188 REFERENCE S49186 !$#authors Wientjens, R.; van Dongen, W.; Haaker, H. !$#submission submitted to the EMBL Data Library, April 1992 !$#description Molecular cloning of fixA, fixB, fixC and fixX genes of !1Azotobacter vinelandii. !$#accession S49188 !'##molecule_type DNA !'##residues 1-360 ##label WIE !'##cross-references EMBL:X65515; NID:g510483; PIDN:CAA46489.1; !1PID:g510486 CLASSIFICATION #superfamily electron transfer flavoprotein alpha chain KEYWORDS electron transfer; flavoprotein SUMMARY #length 360 #molecular-weight 39030 #checksum 5511 SEQUENCE /// ENTRY S14071 #type complete TITLE electron transfer flavoprotein alpha chain fixB homolog - Azorhizobium caulinodans ORGANISM #formal_name Azorhizobium caulinodans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S14071 REFERENCE S14070 !$#authors Arigoni, F.; Kaminski, P.A.; Hennecke, H.; Elmerich, C. !$#journal Mol. Gen. Genet. (1991) 225:514-520 !$#title Nucleotide sequence of the fixABC region of Azorhizobium !1caulinodans ORS571: similarity of the fixB product with !1eukaryotic flavoproteins, characterization of fixX, and !1identification of nifW. !$#cross-references MUID:91203829; PMID:1850088 !$#accession S14071 !'##status preliminary !'##molecule_type DNA !'##residues 1-369 ##label ARI !'##cross-references EMBL:X55450; NID:g38695; PIDN:CAA39092.1; !1PID:g38697 CLASSIFICATION #superfamily electron transfer flavoprotein alpha chain KEYWORDS electron transfer; flavoprotein SUMMARY #length 369 #molecular-weight 39712 #checksum 897 SEQUENCE /// ENTRY S52817 #type complete TITLE electron transfer flavoprotein alpha chain precursor - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein LPZ4c; protein YP9723.04c; protein YPR004c ORGANISM #formal_name Saccharomyces cerevisiae DATE 19-May-1995 #sequence_revision 12-Jul-1996 #text_change 19-Apr-2002 ACCESSIONS S52817; S59749 REFERENCE S52814 !$#authors Pearson, D.; Bowman, S. !$#submission submitted to the EMBL Data Library, April 1995 !$#accession S52817 !'##molecule_type DNA !'##residues 1-344 ##label PEA !'##cross-references EMBL:Z48951; NID:g762999; PIDN:CAA88782.1; !1PID:g763003; GSPDB:GN00016; MIPS:YPR004c !'##experimental_source strain AB972 REFERENCE S59746 !$#authors Wang, Y.; Ahmed, A.; Bussey, H.; Fortin, N.; Friesen, J.D.; !1Hall, J.; Storms, R.K.; Vo, D.H.; Winnett, E. !$#submission submitted to the EMBL Data Library, July 1995 !$#description The sequence of Saccharomyces cerevisiae chromosome XVI !1right arm. !$#accession S59749 !'##molecule_type DNA !'##residues 1-344 ##label WAN !'##cross-references EMBL:U31900; NID:g1276597; PIDN:AAA97583.1; !1PID:g939738; GSPDB:GN00016; MIPS:YPR004c GENETICS !$#gene MIPS:YPR004c !'##cross-references SGD:S0006208 !$#map_position 16R COMPLEX heterodimer of alpha and beta chains that binds one molecule !1of FAD FUNCTION !$#description electron transfer from any of several dehydrogenases in the !1mitochondrial matrix to the mitochondrial respiratory chain !1via electron-transferring-flavoprotein dehydrogenase CLASSIFICATION #superfamily electron transfer flavoprotein alpha chain KEYWORDS electron transfer; FAD; flavoprotein; heterodimer; !1mitochondrial matrix; mitochondrion FEATURE !$1-26 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$27-344 #product electron transfer flavoprotein alpha chain !8#status predicted #label MAT SUMMARY #length 344 #molecular-weight 36802 #checksum 7265 SEQUENCE /// ENTRY B48008 #type complete TITLE electron transfer flavoprotein alpha chain - Paracoccus denitrificans ORGANISM #formal_name Paracoccus denitrificans DATE 02-Jun-1995 #sequence_revision 12-Jul-1996 #text_change 11-Jun-1999 ACCESSIONS B48008; S23165 REFERENCE A48008 !$#authors Bedzyk, L.A.; Escudero, K.W.; Gill, R.E.; Griffin, K.J.; !1Frerman, F.E. !$#journal J. Biol. Chem. (1993) 268:20211-20217 !$#title Cloning, sequencing, and expression of the genes encoding !1subunits of Paracoccus denitrificans electron transfer !1flavoprotein. !$#cross-references MUID:93388590; PMID:8376381 !$#accession B48008 !'##molecule_type DNA !'##residues 1-308 ##label BED !'##cross-references GB:L14864; NID:g309664; PIDN:AAA03072.1; !1PID:g309666 REFERENCE S23165 !$#authors Watmough, N.J.; Kiss, J.; Frerman, F.E. !$#journal Eur. J. Biochem. (1992) 205:1089-1097 !$#title Structural and redox relationships between Paracoccus !1denitrificans, porcine and human electron-transferring !1flavoproteins. !$#cross-references MUID:92249313; PMID:1576992 !$#accession S23165 !'##molecule_type protein !'##residues 2-22;215-219,'H',221-238,'X',240-250;252-268,'XD';274-281, !1283-287 ##label WAT COMPLEX heterodimer of alpha and beta chains (see PIR:A48008) that !1binds one molecule of FAD FUNCTION !$#description electron transfer from any of several dehydrogenases to the !1respiratory chain via electron-transferring-flavoprotein !1dehydrogenase CLASSIFICATION #superfamily electron transfer flavoprotein alpha chain KEYWORDS electron transfer; FAD; flavoprotein; heterodimer FEATURE !$2-308 #product electron transfer flavoprotein alpha chain !8#status predicted #label MAT SUMMARY #length 308 #molecular-weight 31293 #checksum 4052 SEQUENCE /// ENTRY B26952 #type complete TITLE electron transfer flavoprotein alpha chain homolog - Rhizobium meliloti ALTERNATE_NAMES fixB protein ORGANISM #formal_name Rhizobium meliloti DATE 05-Oct-1988 #sequence_revision 12-Jul-1996 #text_change 11-Jun-1999 ACCESSIONS B26952 REFERENCE A26952 !$#authors Earl, C.D.; Ronson, C.W.; Ausubel, F.M. !$#journal J. Bacteriol. (1987) 169:1127-1136 !$#title Genetic and structural analysis of the Rhizobium meliloti !1fixA, fixB, fixC, and fixX genes. !$#cross-references MUID:87137267; PMID:3029021 !$#accession B26952 !'##molecule_type DNA !'##residues 1-353 ##label EAR !'##cross-references GB:M15546; NID:g340664; PIDN:AAA21769.1; !1PID:g551199 COMMENT This protein is essential for symbiotic nitrogen fixation. GENETICS !$#gene fixB !$#note operon contains fixA, fixB, fixC, and fixX genes CLASSIFICATION #superfamily electron transfer flavoprotein alpha chain KEYWORDS electron transfer; flavoprotein; nitrogen fixation SUMMARY #length 353 #molecular-weight 37786 #checksum 7176 SEQUENCE /// ENTRY S32482 #type complete TITLE electron transfer flavoprotein beta chain - human ORGANISM #formal_name Homo sapiens #common_name man DATE 06-Jan-1995 #sequence_revision 12-Jul-1996 #text_change 11-Jun-1999 ACCESSIONS S32482 REFERENCE S32482 !$#authors Finocchiaro, G.; Colombo, I.; Garavaglia, B.; Gellera, C.; !1Valdameri, G.; Garbuglio, N.; DiDonato, S. !$#journal Eur. J. Biochem. (1993) 213:1003-1008 !$#title cDNA cloning and mitochondrial import of the beta-subunit of !1the human electron-transfer flavoprotein. !$#cross-references MUID:93279298; PMID:8504797 !$#accession S32482 !'##molecule_type mRNA !'##residues 1-255 ##label FIN !'##cross-references EMBL:X71129; NID:g297901; PIDN:CAA50441.1; !1PID:g297902 COMMENT This protein does not have a cleavable transit peptide. GENETICS !$#gene GDB:ETFB !'##cross-references GDB:119887; OMIM:130410 !$#map_position 19q13.4-19q13.4 COMPLEX heterodimer of alpha (see PIR:A31998) and beta chains that !1binds one molecule of FAD FUNCTION !$#description electron transfer from any of several dehydrogenases in the !1mitochondrial matrix to the mitochondrial respiratory chain !1via electron-transferring-flavoprotein dehydrogenase CLASSIFICATION #superfamily electron transfer flavoprotein beta chain KEYWORDS electron transfer; FAD; flavoprotein; heterodimer; !1mitochondrial matrix SUMMARY #length 255 #molecular-weight 27843 #checksum 7710 SEQUENCE /// ENTRY A48008 #type complete TITLE electron transfer flavoprotein beta chain - Paracoccus denitrificans ORGANISM #formal_name Paracoccus denitrificans DATE 02-Jun-1995 #sequence_revision 12-Jul-1996 #text_change 08-May-1998 ACCESSIONS A48008; S23293 REFERENCE A48008 !$#authors Bedzyk, L.A.; Escudero, K.W.; Gill, R.E.; Griffin, K.J.; !1Frerman, F.E. !$#journal J. Biol. Chem. (1993) 268:20211-20217 !$#title Cloning, sequencing, and expression of the genes encoding !1subunits of Paracoccus denitrificans electron transfer !1flavoprotein. !$#cross-references MUID:93388590; PMID:8376381 !$#accession A48008 !'##molecule_type DNA !'##residues 1-252 ##label BED !'##cross-references GB:L14864 REFERENCE S23165 !$#authors Watmough, N.J.; Kiss, J.; Frerman, F.E. !$#journal Eur. J. Biochem. (1992) 205:1089-1097 !$#title Structural and redox relationships between Paracoccus !1denitrificans, porcine and human electron-transferring !1flavoproteins. !$#cross-references MUID:92249313; PMID:1576992 !$#accession S23293 !'##molecule_type protein !'##residues 1-22,'R';33-49,'AVA',50-51;74-82;'Y',164-167,'E', !1169-183;189-197 ##label WAT COMPLEX heterodimer of alpha (see PIR:B48008) and beta chains that !1binds one molecule of FAD FUNCTION !$#description electron transfer from any of several dehydrogenases to the !1respiratory chain via electron-transferring-flavoprotein !1dehydrogenase CLASSIFICATION #superfamily electron transfer flavoprotein beta chain KEYWORDS electron transfer; FAD; flavoprotein; heterodimer FEATURE !$1-252 #product electron transfer flavoprotein beta chain !8#status predicted #label MAT SUMMARY #length 252 #molecular-weight 26659 #checksum 6655 SEQUENCE /// ENTRY A64725 #type complete TITLE electron transfer flavoprotein beta chain fixA - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS A64725; S40562 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64725 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-268 ##label BLAT !'##cross-references GB:AE000114; GB:U00096; NID:g1786217; !1PIDN:AAC73152.1; PID:g1786225; UWGP:b0041 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40562 !'##status preliminary !'##molecule_type DNA !'##residues 1-91,'D',93-268 ##label YUR !'##cross-references EMBL:D10483; NID:g216434; PIDN:BAA01317.1; !1PID:g216466 GENETICS !$#gene fixA COMPLEX heterodimer; alpha and beta chain CLASSIFICATION #superfamily electron transfer flavoprotein beta chain KEYWORDS electron transfer; flavoprotein; heterodimer SUMMARY #length 268 #molecular-weight 28412 #checksum 8245 SEQUENCE /// ENTRY S53930 #type complete TITLE electron transfer flavoprotein beta chain - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein G7742; protein YGR207c ORGANISM #formal_name Saccharomyces cerevisiae DATE 08-Jul-1995 #sequence_revision 12-Jul-1996 #text_change 19-Apr-2002 ACCESSIONS S53930; S64529; S63856 REFERENCE S53922 !$#authors Guerreiro, P.; Barreiros, T.; Soares, H.; Cyrne, L.; Maia e !1Silva, A.; Rodrigues-Pousada, C. !$#submission submitted to the EMBL Data Library, April 1995 !$#description Sequencing of a 17.6 kb segment on the right arm of yeast !1chromosome VII reveals 12 open reading frames, including !1CCT, ADE3 and TR-I genes, homologous to the yeast YAL023 and !1EF1G genes, of the human. !$#accession S53930 !'##molecule_type DNA !'##residues 1-261 ##label GUE !'##cross-references EMBL:Z49133; NID:g790489; PIDN:CAA89000.1; !1PID:g790498 !'##experimental_source strain S288C REFERENCE S64517 !$#authors Guerreiro, P.; Barreiros, T.; Cyrne, L.; Soares, H.; Maia e !1Silva, A.; Rodrigues-Pousada, C. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64529 !'##molecule_type DNA !'##residues 1-261 ##label GUW !'##cross-references EMBL:Z72992; NID:g1323370; PIDN:CAA97234.1; !1PID:g1323371; GSPDB:GN00007; MIPS:YGR207c !'##experimental_source strain S288C REFERENCE S63848 !$#authors Guerreiro, P.; Barreiros, T.; Soares, H.; Cyrne, L.; Maia e !1Silva, A.; Rodrigues-Pousada, C. !$#journal Yeast (1996) 12:273-280 !$#title Sequencing of a 17.6 kb segment on the right arm of yeast !1chromosome VII reveals 12 ORFs, including CCT, ADE3 and TR-I !1genes, homologues of the yeast PMT and EF1G genes, of the !1human and bacterial electron-transferring flavoproteins !1(beta-chain) and of the Escherichia coli phosphoserine !1phosphohydrolase, and five new ORFs. !$#cross-references MUID:97060019; PMID:8904340 !$#accession S63856 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-261 ##label GUF !'##cross-references EMBL:Z49133; NID:g790489; PIDN:CAA89000.1; !1PID:g790498 GENETICS !$#gene ETF-beta; MIPS:YGR207c !'##cross-references SGD:S0003439 !$#map_position 7R !$#genome nuclear COMPLEX heterodimer of alpha and beta chains FUNCTION !$#description electron transfer from any of several dehydrogenases in the !1mitochondrial matrix to the mitochondrial respiratory chain !1via electron-transferring-flavoprotein dehydrogenase CLASSIFICATION #superfamily electron transfer flavoprotein beta chain KEYWORDS electron transfer; FAD; flavoprotein; mitochondrial matrix; !1mitochondrion SUMMARY #length 261 #molecular-weight 28758 #checksum 8339 SEQUENCE /// ENTRY A26952 #type complete TITLE electron transfer flavoprotein beta chain homolog - Rhizobium meliloti ALTERNATE_NAMES fixA protein ORGANISM #formal_name Rhizobium meliloti DATE 05-Oct-1988 #sequence_revision 12-Jul-1996 #text_change 11-Jun-1999 ACCESSIONS A26952 REFERENCE A26952 !$#authors Earl, C.D.; Ronson, C.W.; Ausubel, F.M. !$#journal J. Bacteriol. (1987) 169:1127-1136 !$#title Genetic and structural analysis of the Rhizobium meliloti !1fixA, fixB, fixC, and fixX genes. !$#cross-references MUID:87137267; PMID:3029021 !$#accession A26952 !'##molecule_type DNA !'##residues 1-292 ##label EAR !'##cross-references GB:M15546; NID:g340664; PIDN:AAA21768.1; !1PID:g551198 COMMENT This protein is essential for symbiotic nitrogen fixation. GENETICS !$#gene fixA !$#note operon contains fixA, fixB, fixC, and fixX genes CLASSIFICATION #superfamily electron transfer flavoprotein beta chain KEYWORDS electron transfer; flavoprotein; nitrogen fixation SUMMARY #length 292 #molecular-weight 31146 #checksum 8924 SEQUENCE /// ENTRY S14070 #type complete TITLE electron transfer flavoprotein beta chain fixA - Azorhizobium caulinodans ORGANISM #formal_name Azorhizobium caulinodans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S14070; S29388 REFERENCE S14070 !$#authors Arigoni, F.; Kaminski, P.A.; Hennecke, H.; Elmerich, C. !$#journal Mol. Gen. Genet. (1991) 225:514-520 !$#title Nucleotide sequence of the fixABC region of Azorhizobium !1caulinodans ORS571: similarity of the fixB product with !1eukaryotic flavoproteins, characterization of fixX, and !1identification of nifW. !$#cross-references MUID:91203829; PMID:1850088 !$#accession S14070 !'##status preliminary !'##molecule_type DNA !'##residues 1-281 ##label ARI !'##cross-references EMBL:X55450; NID:g38695; PIDN:CAA39091.1; !1PID:g38696 REFERENCE S29387 !$#authors Kaminski, P.A.; Norel, F.; Desnoues, N.; Kush, A.; Salzano, !1G.; Elmerich, C. !$#journal Mol. Gen. Genet. (1988) 214:496-502 !$#title Characterization of the fixABC region of Azorhizobium !1caulinodans ORS571 and identification of a new nitrogen !1fixation gene. !$#cross-references MUID:89112157; PMID:3216855 !$#accession S29388 !'##status preliminary !'##molecule_type DNA !'##residues 1-34 ##label KAM !'##cross-references GB:M35122; NID:g152066; PIDN:AAA26189.1; !1PID:g152068 CLASSIFICATION #superfamily electron transfer flavoprotein beta chain KEYWORDS electron transfer; flavoprotein; nitrogen fixation SUMMARY #length 281 #molecular-weight 30110 #checksum 3079 SEQUENCE /// ENTRY S49187 #type complete TITLE electron transfer flavoprotein beta chain fixA - Azotobacter vinelandii ORGANISM #formal_name Azotobacter vinelandii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S49187 REFERENCE S49186 !$#authors Wientjens, R.; van Dongen, W.; Haaker, H. !$#submission submitted to the EMBL Data Library, April 1992 !$#description Molecular cloning of fixA, fixB, fixC and fixX genes of !1Azotobacter vinelandii. !$#accession S49187 !'##status preliminary !'##molecule_type DNA !'##residues 1-281 ##label WIE !'##cross-references EMBL:X65515; NID:g510483; PIDN:CAA46488.1; !1PID:g510485 CLASSIFICATION #superfamily electron transfer flavoprotein beta chain KEYWORDS electron transfer; flavoprotein SUMMARY #length 281 #molecular-weight 30740 #checksum 6869 SEQUENCE /// ENTRY DEHUAA #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) 1 - human ALTERNATE_NAMES alcohol dehydrogenase alpha chain; class I alcohol dehydrogenase ORGANISM #formal_name Homo sapiens #common_name man DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 18-Feb-2000 ACCESSIONS S02265; A25428; A24408; I39398; I39397 REFERENCE S02265 !$#authors Matsuo, Y.; Yokoyama, S. !$#journal FEBS Lett. (1989) 243:57-60 !$#title Molecular structure of the human alcohol dehydrogenase 1 !1gene. !$#cross-references MUID:89153548; PMID:2920825 !$#accession S02265 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-375 ##label MATS REFERENCE A94120 !$#authors Ikuta, T.; Szeto, S.; Yoshida, A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:634-638 !$#title Three human alcohol dehydrogenase subunits: cDNA structure !1and molecular and evolutionary divergence. !$#cross-references MUID:86120995; PMID:2935875 !$#accession A25428 !'##molecule_type mRNA !'##residues 1-375 ##label IKU !'##cross-references GB:M12271; NID:g178091; PIDN:AAA68131.1; !1PID:g178092 REFERENCE A24408 !$#authors von Bahr-Lindstrom, H.; Hoog, J.O.; Heden, L.O.; Kaiser, R.; !1Fleetwood, L.; Larsson, K.; Lake, M.; Holmquist, B.; !1Holmgren, A.; Hempel, J.; Vallee, B.L.; Jornvall, H. !$#journal Biochemistry (1986) 25:2465-2470 !$#title cDNA and protein structure for the alpha subunit of human !1liver alcohol dehydrogenase. !$#cross-references MUID:86243367; PMID:3013304 !$#accession A24408 !'##molecule_type mRNA !'##residues 1-375 ##label VON !'##cross-references GB:M12963; NID:g178089; PIDN:AAA51590.1; !1PID:g178090 REFERENCE I39398 !$#authors Yasunami, M.; Kikuchi, I.; Sarapata, D.; Yoshida, A. !$#journal Genomics (1990) 7:152-158 !$#title The human class I alcohol dehydrogenase gene cluster: three !1genes are tandemly organized in an 80-kb-long segment of the !1genome. !$#cross-references MUID:90269803; PMID:2347582 !$#accession I39398 !'##status translation not shown !'##molecule_type DNA !'##residues 1-6 ##label YAS !'##cross-references GB:M37066; NID:g178095; PIDN:AAA51591.1; !1PID:g178096 REFERENCE I39397 !$#authors Stewart, M.J.; McBride, M.S.; Winter, L.A.; Duester, G. !$#journal Gene (1990) 90:271-279 !$#title Promoters for the human alcohol dehydrogenase genes ADH1, !1ADH2, and ADH3: interaction of CCAAT/enhancer-binding !1protein with elements flanking the ADH2 TATA box. !$#cross-references MUID:90382676; PMID:2169444 !$#accession I39397 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-6 ##label STE !'##cross-references GB:M32656; NID:g178093; PIDN:AAA52276.1; !1PID:g178094 COMMENT Class I alcohol dehydrogenases are pyrazole-sensitive and !1have a high activity for ethanol. GENETICS !$#gene GDB:ADH1 !'##cross-references GDB:119650; OMIM:103700 !$#map_position 4q21-4q23 !$#introns 6/3; 40/3; 87/1; 116/2; 189/3; 276/3; 322/1; 368/2 COMPLEX homo- or heterodimer of three types of chains (alpha, beta, !1or gamma) coded by three nonallelic genes (see also !1PIR:DEHUAB, PIR:DEHUAG) FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway ethanol degradation !$#note human alcohol dehydrogenase 1 is expressed predominately in !1fetal and neonatal liver CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS acetylated amino end; alcohol metabolism; dimer; !1metalloprotein; NAD; oxidoreductase; zinc FEATURE !$2-375 #product alcohol dehydrogenase 1 #status predicted !8#label MAT\ !$32-366 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$195-224 #region beta-alpha-beta NAD nucleotide-binding fold\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status predicted\ !$47,68,175 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$98,101,104,112 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 375 #molecular-weight 39858 #checksum 7545 SEQUENCE /// ENTRY I55359 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) 1 - rhesus macaque ALTERNATE_NAMES alcohol dehydrogenase alpha chain; class I alcohol dehydrogenase ORGANISM #formal_name Macaca mulatta #common_name rhesus macaque DATE 24-May-1996 #sequence_revision 24-May-1996 #text_change 11-Jun-1999 ACCESSIONS I55359 REFERENCE I55359 !$#authors Light, D.R.; Dennis, M.S.; Forsythe, I.J.; Liu, C. !$#journal J. Biol. Chem. (1992) 267:12592-12599 !$#title Alpha-isoenzyme of alcohol dehydrogenase form monkey liver: !1cloning, expression, mechanism, coenzyme, and substrate !1specificity. !$#cross-references MUID:92316940; PMID:1618764 !$#accession I55359 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-375 ##label RES !'##cross-references GB:M81807; NID:g342064; PIDN:AAA36830.1; !1PID:g342065 COMMENT Class I alcohol dehydrogenases are pyrazole-sensitive and !1have a high activity for ethanol. COMPLEX homo- or heterodimer of three types of chains (alpha, beta, !1or gamma) coded by three nonallelic genes FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation !$#note human alcohol dehydrogenase 1 is expressed predominately in !1fetal and neonatal liver CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS acetylated amino end; alcohol metabolism; dimer; !1metalloprotein; NAD; oxidoreductase; zinc FEATURE !$2-375 #product alcohol dehydrogenase 1 #status predicted !8#label MAT\ !$32-366 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$195-224 #region beta-alpha-beta NAD nucleotide-binding fold\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status predicted\ !$47,68,175 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$98,101,104,112 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 375 #molecular-weight 39912 #checksum 741 SEQUENCE /// ENTRY DEHUAB #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) 2 [validated] - human ALTERNATE_NAMES alcohol dehydrogenase beta chain; class I alcohol dehydrogenase ORGANISM #formal_name Homo sapiens #common_name man DATE 25-Feb-1985 #sequence_revision 02-Aug-1994 #text_change 15-Sep-2000 ACCESSIONS A23607; A38916; I39399; A26281; I39402; I39401; S05202; !1S10621; I39400; A00335; A05182; A26826; B25428 REFERENCE A23607 !$#authors Heden, L.O.; Hoog, J.O.; Larsson, K.; Lake, M.; Lagerholm, !1E.; Holmgren, A.; Vallee, B.L.; Jornvall, H.; von !1Bahr-Lindstrom, H. !$#journal FEBS Lett. (1986) 194:327-332 !$#title cDNA clones coding for the beta-subunit of human liver !1alcohol dehydrogenase have differently sized 3'-non-coding !1regions. !$#cross-references MUID:86082371; PMID:3000832 !$#accession A23607 !'##molecule_type mRNA !'##residues 1-375 ##label HED !'##cross-references EMBL:X03350; NID:g28415; PIDN:CAA27056.1; !1PID:g28416 REFERENCE A38916 !$#authors Ikuta, T.; Fujiyoshi, T.; Kurachi, K.; Yoshida, A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:2703-2707 !$#title Molecular cloning of a full-length cDNA for human alcohol !1dehydrogenase. !$#cross-references MUID:85190565; PMID:2986130 !$#accession A38916 !'##molecule_type mRNA !'##residues 1-375 ##label IKU !'##cross-references GB:M24317; NID:g178097 !'##note this sequence has been revised in reference A38917 REFERENCE A38917 !$#authors Ikuta, T.; Fujiyoshi, T.; Kurachi, K.; Yoshida, A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:5578 !$#contents annotation; erratum REFERENCE I39399 !$#authors Yokoyama, S.; Yokoyama, R.; Rotwein, P. !$#journal Jpn. J. Genet. (1987) 62:241-256 !$#title Molecular characterization of cDNA clones encoding the human !1alcohol dehydrogenase beta 1 and the evolutionary !1relationship to the other class I subunits alpha and gamma. !$#accession I39399 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-375 ##label YOK !'##cross-references GB:D00137; NID:g219427; PIDN:BAA00084.1; !1PID:g219428 REFERENCE A26281 !$#authors Duester, G.; Smith, M.; Bilanchone, V.; Hatfield, G.W. !$#journal J. Biol. Chem. (1986) 261:2027-2033 !$#title Molecular analysis of the human class I alcohol !1dehydrogenase gene family and nucleotide sequence of the !1gene encoding the beta subunit. !$#cross-references MUID:86111889; PMID:2935533 !$#accession A26281 !'##molecule_type DNA !'##residues 1-229,'K',231-375 ##label DUE !'##cross-references GB:M24317; GB:K01883; NID:g178097; PIDN:AAA51884.1; !1PID:g178098 !'##note the authors translated the codon AAA for residue 230 as Phe REFERENCE I39398 !$#authors Yasunami, M.; Kikuchi, I.; Sarapata, D.; Yoshida, A. !$#journal Genomics (1990) 7:152-158 !$#title The human class I alcohol dehydrogenase gene cluster: three !1genes are tandemly organized in an 80-kb-long segment of the !1genome. !$#cross-references MUID:90269803; PMID:2347582 !$#accession I39402 !'##status translation not shown !'##molecule_type DNA !'##residues 1-6 ##label YAS !'##cross-references GB:M37067; NID:g178114; PIDN:AAA51593.1; !1PID:g178115 REFERENCE I39397 !$#authors Stewart, M.J.; McBride, M.S.; Winter, L.A.; Duester, G. !$#journal Gene (1990) 90:271-279 !$#title Promoters for the human alcohol dehydrogenase genes ADH1, !1ADH2, and ADH3: interaction of CCAAT/enhancer-binding !1protein with elements flanking the ADH2 TATA box. !$#cross-references MUID:90382676; PMID:2169444 !$#accession I39401 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-6 ##label STE !'##cross-references GB:M32657; NID:g178112; PIDN:AAA52277.1; !1PID:g178113 REFERENCE S05202 !$#authors Matsuo, Y.; Yokoyama, R.; Yokoyama, S. !$#journal Eur. J. Biochem. (1989) 183:317-320 !$#title The genes for human alcohol dehydrogenases beta(1) and beta !1(2) differ by only one nucleotide. !$#cross-references MUID:89338401; PMID:2547609 !$#accession S05202 !'##molecule_type DNA !'##residues 1-47,'H',49-375 ##label MATS !'##cross-references EMBL:X15447; NID:g28385 !'##note allelic beta-2 variant found predominately in oriental !1populations !'##note the sequence in GenBank entry HSADH221, release 103 !1(PID:e228260), has an incorrect splice boundary and an !1inserted Val before Val-190 REFERENCE S10621 !$#authors Ehrig, T.; von Wartburg, J.P.; Wermuth, B. !$#journal FEBS Lett. (1988) 234:53-55 !$#title cDNA sequence of the beta(2)-subunit of human liver alcohol !1dehydrogenase. !$#cross-references MUID:88271624; PMID:2968918 !$#accession S10621 !'##molecule_type mRNA !'##residues 1-47,'H',49-343 ##label EHR !'##note only a list of differences from various previously published !1sequences is shown REFERENCE I39400 !$#authors Xu, Y.L.; Carr, L.G.; Bosron, W.F.; Li, T.K.; Edenberg, H.J. !$#journal Genomics (1988) 2:209-214 !$#title Genotyping of human alcohol dehydrogenases at the ADH2 and !1ADH3 loci following DNA sequence amplification. !$#cross-references MUID:88284699; PMID:3397059 !$#accession I39400 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-7,'M',9-56,'K',58-165,'K',167-234,'V',236-375 ##label RE3 !'##cross-references GB:M21692; NID:g178099; PIDN:AAA51592.1; !1PID:g178100 REFERENCE A00335 !$#authors Hempel, J.; Buhler, R.; Kaiser, R.; Holmquist, B.; de !1Zalenski, C.; von Wartburg, J.P.; Vallee, B.; Jornvall, H. !$#journal Eur. J. Biochem. (1984) 145:437-445 !$#title Human liver alcohol dehydrogenase. 1. The primary structure !1of the beta-1beta-1 isoenzyme. !$#cross-references MUID:85076637; PMID:6391920 !$#accession A00335 !'##molecule_type protein !'##residues 2-129,131-375 ##label HEM !'##note allelic beta-1 variant found predominately in caucasian and !1negroid populations REFERENCE A05182 !$#authors Buhler, R.; Hempel, J.; Kaiser, R.; von Wartburg, J.P.; !1Vallee, B.L.; Jornvall, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:6320-6324 !$#title Human alcohol dehydrogenase: structural differences between !1the beta and gamma subunits suggest parallel duplications in !1isoenzyme evolution and predominant expression of separate !1gene descendants in livers of different mammals. !$#cross-references MUID:85038508; PMID:6387702 !$#accession A05182 !'##molecule_type protein !'##residues 12-34,'V',36-38, !141-85;101-114;131-160;170-213;273-313;317-331;341-367 !1##label BUH REFERENCE A26826 !$#authors Burnell, J.C.; Carr, L.G.; Dwulet, F.E.; Edenberg, H.J.; Li, !1T.K.; Bosron, W.F. !$#journal Biochem. Biophys. Res. Commun. (1987) 146:1227-1233 !$#title The human beta-3 alcohol dehydrogenase subunit differs from !1beta-1 by a Cys for Arg-369 substitution which decreases NAD !1(H) binding. !$#accession A26826 !'##molecule_type protein !'##residues 368-369,'C',371-375 ##label BUR !'##note allelic beta-3 variant found as a minor form occurring to a !1greater extent in negroid populations; formerly called !1beta-Indianapolis REFERENCE A40987 !$#authors Hurley, T.D.; Bosron, W.F.; Hamilton, J.A.; Amzel, L.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:8149-8153 !$#title Structure of human beta-1beta-1 alcohol dehydrogenase: !1catalytic effects of nonactive-site substitutions. !$#cross-references MUID:91376103; PMID:1896463 !$#contents annotation; X-ray crystallography, 3.0 angstroms !$#note structure of beta-1 variant dimer REFERENCE A52127 !$#authors Hurley, T.D.; Bosron, W.F.; Hamilton, J.A.; Amzel, L.M. !$#submission submitted to the Brookhaven Protein Data Bank, January 1993 !$#cross-references PDB:3HUD !$#contents annotation; X-ray crystallography, 3.2 angstroms, residues !12-375 COMMENT Class I alcohol dehydrogenases are pyrazole-sensitive and !1have a high activity for ethanol. GENETICS !$#gene GDB:ADH2 !'##cross-references GDB:119651; OMIM:103720 !$#map_position 4q22-4q22 !$#introns 6/3; 40/3; 87/1; 116/2; 189/3; 276/3; 322/1; 368/2 COMPLEX homo- or heterodimer of three types of chains (alpha, beta, !1or gamma) coded by three nonallelic genes (see also !1PIR:DEHUAA, PIR:DEHUAG) FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation !$#note human alcohol dehydrogenase beta is expressed predominately !1in fetal lung and neonatal and adult liver CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS acetylated amino end; alcohol metabolism; dimer; !1metalloprotein; NAD; oxidoreductase; zinc FEATURE !$2-375 #product alcohol dehydrogenase 2 #status experimental !8#label MAT\ !$32-366 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$195-224 #region beta-alpha-beta NAD nucleotide-binding fold\ !$2 #modified_site blocked amino end (Ser) (in mature !8form) (probably acetylated) #status experimental\ !$47,68,175 #binding_site zinc, catalytic (Cys, His, Cys) #status !8experimental\ !$98,101,104,112 #binding_site zinc, noncatalytic (Cys) #status !8experimental SUMMARY #length 375 #molecular-weight 39854 #checksum 1183 SEQUENCE /// ENTRY A33909 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) 2 - baboon ALTERNATE_NAMES alcohol dehydrogenase beta chain; class I alcohol dehydrogenase ORGANISM #formal_name Papio sp. #common_name baboon DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 11-Jun-1999 ACCESSIONS A33909 REFERENCE A33909 !$#authors Trezise, A.E.O.; Godfrey, E.A.; Holmes, R.S.; Beacham, I.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:5454-5458 !$#title Cloning and sequencing of cDNA encoding baboon liver alcohol !1dehydrogenase: evidence for a common ancestral lineage with !1the human alcohol dehydrogenase beta-subunit and for class I !1ADH gene duplications predating primate radiation. !$#cross-references MUID:89315815; PMID:2748595 !$#accession A33909 !'##molecule_type mRNA !'##residues 1-375 ##label TRE !'##cross-references GB:M25035; NID:g176563; PIDN:AAA35378.1; !1PID:g176564 COMMENT Class I alcohol dehydrogenases are pyrazole-sensitive and !1have a high activity for ethanol. COMPLEX homo- or heterodimer of three types of chains (alpha, beta, !1or gamma) coded by three nonallelic genes FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation !$#note human alcohol dehydrogenase 2 is expressed predominately in !1fetal lung and neonatal and adult liver CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS acetylated amino end; alcohol metabolism; dimer; !1metalloprotein; NAD; oxidoreductase; zinc FEATURE !$2-375 #product alcohol dehydrogenase 2 #status predicted !8#label MAT\ !$32-366 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$195-224 #region beta-alpha-beta NAD nucleotide-binding fold\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status predicted\ !$47,68,175 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$98,101,104,112 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 375 #molecular-weight 39846 #checksum 2136 SEQUENCE /// ENTRY DEHUAG #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) 3 [validated] - human ALTERNATE_NAMES alcohol dehydrogenase gamma chain; class I alcohol dehydrogenase ORGANISM #formal_name Homo sapiens #common_name man DATE 28-May-1986 #sequence_revision 28-Oct-1994 #text_change 08-Dec-2000 ACCESSIONS C25428; A24798; A00336; I39404; I39403 REFERENCE A94120 !$#authors Ikuta, T.; Szeto, S.; Yoshida, A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:634-638 !$#title Three human alcohol dehydrogenase subunits: cDNA structure !1and molecular and evolutionary divergence. !$#cross-references MUID:86120995; PMID:2935875 !$#accession C25428 !'##molecule_type mRNA !'##residues 1-375 ##label IKU !'##cross-references GB:M12272; NID:g178147; PIDN:AAC41757.1; !1PID:g178148 !'##note allelic gamma-1 variant REFERENCE A24798 !$#authors Hoog, J.O.; Heden, L.O.; Larsson, K.; Jornvall, H.; von !1Bahr-Lindstrom, H. !$#journal Eur. J. Biochem. (1986) 159:215-218 !$#title The gamma-1 and gamma-2 subunits of human liver alcohol !1dehydrogenase. !$#cross-references MUID:87004628; PMID:3758060 !$#accession A24798 !'##molecule_type mRNA !'##residues 2-271,'Q',273-349,'V',351-375 ##label HOO !'##cross-references EMBL:X04299; NID:g28403; PIDN:CAA27842.1; !1PID:g28404 !'##note allelic gamma-2 variant found as a minor form occurring to a !1greater extent in caucasian populations REFERENCE A00336 !$#authors Buhler, R.; Hempel, J.; Kaiser, R.; de Zalenski, C.; von !1Wartburg, J.P.; Jornvall, H. !$#journal Eur. J. Biochem. (1984) 145:447-453 !$#title Human liver alcohol dehydrogenase. 2. The primary structure !1of the gamma-1 protein chain. !$#cross-references MUID:85076638; PMID:6391921 !$#accession A00336 !'##molecule_type protein !'##residues 2-129,131-276,'V',278-375 ##label BUH !'##note allelic gamma-1 variant REFERENCE I39398 !$#authors Yasunami, M.; Kikuchi, I.; Sarapata, D.; Yoshida, A. !$#journal Genomics (1990) 7:152-158 !$#title The human class I alcohol dehydrogenase gene cluster: three !1genes are tandemly organized in an 80-kb-long segment of the !1genome. !$#cross-references MUID:90269803; PMID:2347582 !$#accession I39404 !'##status translation not shown !'##molecule_type DNA !'##residues 1-6 ##label YAS !'##cross-references GB:M37068; NID:g178118; PIDN:AAA51594.1; !1PID:g178119 REFERENCE I39397 !$#authors Stewart, M.J.; McBride, M.S.; Winter, L.A.; Duester, G. !$#journal Gene (1990) 90:271-279 !$#title Promoters for the human alcohol dehydrogenase genes ADH1, !1ADH2, and ADH3: interaction of CCAAT/enhancer-binding !1protein with elements flanking the ADH2 TATA box. !$#cross-references MUID:90382676; PMID:2169444 !$#accession I39403 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-6 ##label STE !'##cross-references GB:M32658; NID:g178116; PIDN:AAA52278.1; !1PID:g178117 COMMENT Class I alcohol dehydrogenases are pyrazole-sensitive and !1have a high activity for ethanol. GENETICS !$#gene GDB:ADH3 !'##cross-references GDB:119652; OMIM:103730 !$#map_position 4q22-4q22 COMPLEX homo- or heterodimer of three types of chains (alpha, beta, !1or gamma) coded by three nonallelic genes (see also !1PIR:DEHUAA, PIR:DEHUAB) FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#note human alcohol dehydrogenase gamma is expressed predominately !1in neonatal and adult liver and stomach CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS acetylated amino end; alcohol metabolism; dimer; !1metalloprotein; NAD; oxidoreductase; zinc FEATURE !$2-375 #product alcohol dehydrogenase 3 #status experimental !8#label MAT\ !$32-366 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$195-224 #region beta-alpha-beta NAD nucleotide-binding fold\ !$2 #modified_site blocked amino end (Ser) (in mature !8form) (probably acetylated) #status experimental\ !$47,68,175 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$98,101,104,112 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 375 #molecular-weight 39867 #checksum 184 SEQUENCE /// ENTRY DEHOAL #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) E - horse ORGANISM #formal_name Equus caballus #common_name domestic horse DATE 24-Apr-1984 #sequence_revision 28-Oct-1994 #text_change 11-Jun-1999 ACCESSIONS A39872; A00337 REFERENCE A39872 !$#authors Park, D.H.; Plapp, B.V. !$#journal J. Biol. Chem. (1991) 266:13296-13302 !$#title Isoenzymes of horse liver alcohol dehydrogenase active on !1ethanol and steroids. cDNA cloning, expression, and !1comparison of active sites. !$#cross-references MUID:91302361; PMID:1712777 !$#accession A39872 !'##molecule_type mRNA !'##residues 1-375 ##label PAR !'##cross-references GB:M64864; NID:g164175; PIDN:AAA30931.1; !1PID:g164176 REFERENCE A91175 !$#authors Jornvall, H. !$#journal Eur. J. Biochem. (1970) 16:41-49 !$#title Horse liver alcohol dehydrogenase. On the primary structures !1of the isoenzymes. !$#cross-references MUID:70283434; PMID:5466062 !$#accession A00337 !'##molecule_type protein !'##residues 2-375 ##label JOR !'##experimental_source liver REFERENCE A92838 !$#authors Eklund, H.; Nordstrom, B.; Zeppezauer, E.; Soderlund, G.; !1Ohlsson, I.; Boiwe, T.; Soderberg, B.O.; Tapia, O.; Branden, !1C.I.; Akeson, A. !$#journal J. Mol. Biol. (1976) 102:27-59 !$#title Three-dimensional structure of horse liver alcohol !1dehydrogenase at 2.4 angstrom resolution. !$#cross-references MUID:76193761; PMID:178875 !$#contents annotation; X-ray crystallography, 2.4 angstroms COMMENT The active, zinc-containing enzyme converts primary and !1secondary alcohols to aldehydes using NAD as acceptor. COMMENT This enzyme is a homo- or heterodimer of two types of chains !1(E or S) coded by two nonallelic genes. COMMENT This enzyme is active for ethanol and not steroids. CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS acetylated amino end; alcohol metabolism; dimer; !1metalloprotein; NAD; oxidoreductase; zinc FEATURE !$32-366 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$195-224 #region beta-alpha-beta NAD nucleotide-binding fold\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental\ !$47,68,175 #binding_site zinc, catalytic (Cys, His, Cys) #status !8experimental\ !$98,101,104,112 #binding_site zinc, noncatalytic (Cys) #status !8experimental SUMMARY #length 375 #molecular-weight 39935 #checksum 533 SEQUENCE /// ENTRY DEHOAS #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) S - horse ORGANISM #formal_name Equus caballus #common_name domestic horse DATE 31-Mar-1992 #sequence_revision 28-Oct-1994 #text_change 11-Jun-1999 ACCESSIONS B39872; A91175; A00337 REFERENCE A39872 !$#authors Park, D.H.; Plapp, B.V. !$#journal J. Biol. Chem. (1991) 266:13296-13302 !$#title Isoenzymes of horse liver alcohol dehydrogenase active on !1ethanol and steroids. cDNA cloning, expression, and !1comparison of active sites. !$#cross-references MUID:91302361; PMID:1712777 !$#accession B39872 !'##molecule_type mRNA !'##residues 1-374 ##label PAR !'##cross-references GB:M64865; NID:g164177; PIDN:AAA30932.1; !1PID:g164178 REFERENCE A91175 !$#authors Jornvall, H. !$#journal Eur. J. Biochem. (1970) 16:41-49 !$#title Horse liver alcohol dehydrogenase. On the primary structures !1of the isoenzymes. !$#cross-references MUID:70283434; PMID:5466062 !$#accession A91175 !'##molecule_type protein !'##residues 2-43,'T',45-59,'T',61-115,'S',116-171,'I',173-276,'T', !1278-374 ##label JOR COMMENT The active, zinc-containing enzyme converts primary and !1secondary alcohols to aldehydes using NAD as acceptor. COMMENT This enzyme is a homo- or heterodimer of two types of chains !1(E or S) coded by two nonallelic genes. COMMENT This enzyme is active for both ethanol and steroids. CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS acetylated amino end; alcohol metabolism; dimer; !1metalloprotein; NAD; oxidoreductase; zinc FEATURE !$32-365 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$194-223 #region beta-alpha-beta NAD nucleotide-binding fold\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental\ !$47,68,174 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$98,101,104,112 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 374 #molecular-weight 39623 #checksum 5895 SEQUENCE /// ENTRY DEMSAA #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) A - mouse ALTERNATE_NAMES alcohol dehydrogenase beta ORGANISM #formal_name Mus musculus #common_name house mouse DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 11-Jun-1999 ACCESSIONS A27322; A29628; A00338; S50103; A25849 REFERENCE A27322 !$#authors Zhang, K.; Bosron, W.F.; Edenberg, H.J. !$#journal Gene (1987) 57:27-36 !$#title Structure of the mouse Adh-1 gene and identification of a !1deletion in a long alternating purine-pyrimidine sequence in !1the first intron of strains expressing low alcohol !1dehydrogenase activity. !$#cross-references MUID:88112859; PMID:3428612 !$#accession A27322 !'##molecule_type DNA !'##residues 1-375 ##label ZHA !'##cross-references GB:M11307; NID:g191717; PIDN:AAA37180.1; !1PID:g309094 REFERENCE A29628 !$#authors Ceci, J.D.; Zheng, Y.W.; Felder, M.R. !$#journal Gene (1987) 59:171-182 !$#title Molecular analysis of mouse alcohol dehydrogenase: !1nucleotide sequence of the Adh-1 gene and genetic mapping of !1a related nucleotide sequence to chromosome 3. !$#cross-references MUID:88137953; PMID:2893758 !$#accession A29628 !'##molecule_type DNA !'##residues 1-375 ##label CEC !'##cross-references GB:M22611 REFERENCE A00338 !$#authors Edenberg, H.J.; Zhang, K.; Fong, K.; Bosron, W.F.; Li, T.K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:2262-2266 !$#title Cloning and sequencing of cDNA encoding the complete mouse !1liver alcohol dehydrogenase. !$#cross-references MUID:85190477; PMID:3157987 !$#accession A00338 !'##molecule_type mRNA !'##residues 1-375 ##label EDE !'##cross-references GB:M11307; NID:g191717; PIDN:AAA37180.1; !1PID:g309094 !'##note in Genbank entry MUSADHIA, release 109.0, the source is !1designated as Mus caroli REFERENCE S50102 !$#authors Caubin, J.; Iglesias, T.; Bernal, J.; Munoz, A.; Marquez, !1G.; Barbero, J.L.; Zaballos, A. !$#journal Nucleic Acids Res. (1994) 22:4132-4138 !$#title Isolation of genomic DNA fragments corresponding to genes !1modulated in vivo by a transcription factor. !$#cross-references MUID:95023181; PMID:7937138 !$#accession S50103 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 8-51 ##label CAU !'##cross-references EMBL:Z32540 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1March 1994 REFERENCE A25849 !$#authors Ceci, J.D.; Lawther, R.; Duester, G.; Hatfield, G.W.; Smith, !1M.; O'Malley, M.P.; Felder, M.R. !$#journal Gene (1986) 41:217-224 !$#title Androgen induction of alcohol dehydrogenase in mouse kidney. !1Studies with a cDNA probe confirmed by nucleotide sequence !1analysis. !$#cross-references MUID:86221702; PMID:3011597 !$#accession A25849 !'##molecule_type mRNA !'##residues 224-375 ##label CE2 !'##cross-references GB:M22611; NID:g191719; PIDN:AAA37181.1; !1PID:g191720 COMMENT This enzyme converts primary and secondary alcohols to !1aldehydes using NAD as acceptor. COMMENT The active enzyme is a dimer of identical or nonidentical !1zinc-containing polypeptide chains of three types (A, B, or !1C), which are coded by three separate genes at different !1loci. GENETICS !$#gene Adh-1 !$#introns 6/3; 40/3; 87/1; 116/2; 189/3; 276/3; 322/1; 368/2 CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS acetylated amino end; alcohol metabolism; dimer; !1metalloprotein; NAD; oxidoreductase; zinc FEATURE !$2-375 #product alcohol dehydrogenase chain A #status !8predicted #label MAT\ !$32-366 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$195-224 #region beta-alpha-beta NAD nucleotide-binding fold\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status predicted\ !$47,68,175 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$98,101,104,112 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 375 #molecular-weight 39771 #checksum 514 SEQUENCE /// ENTRY A49107 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) I - deer mouse ALTERNATE_NAMES alcohol dehydrogenase 1 ORGANISM #formal_name Peromyscus maniculatus #common_name deer mouse DATE 19-Mar-1997 #sequence_revision 19-Mar-1997 #text_change 11-Jun-1999 ACCESSIONS A49107 REFERENCE A49107 !$#authors Zheng, Y.W.; Bey, M.; Liu, H.; Felder, M.R. !$#journal J. Biol. Chem. (1993) 268:24933-24939 !$#title Molecular basis of the alcohol dehydrogenase-negative deer !1mouse. Evidence for deletion of the gene for class I enzyme !1and identification of a possible new enzyme class. !$#cross-references MUID:94043358; PMID:8227055 !$#accession A49107 !'##molecule_type mRNA !'##residues 1-375 ##label ZHE !'##cross-references GB:L15703; NID:g416387; PIDN:AAA40591.1; !1PID:g416388 COMMENT The class I alcohol dehydrogenases are pyrazole-sensitive !1and have a high activity for ethanol. GENETICS !$#gene Adh-1 COMPLEX homodimer (A2 isozyme) FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS acetylated amino end; alcohol metabolism; dimer; !1metalloprotein; NAD; oxidoreductase; zinc FEATURE !$2-375 #product alcohol dehydrogenase alpha #status !8predicted #label MAT\ !$32-366 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$195-224 #region beta-alpha-beta NAD nucleotide-binding fold\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status predicted\ !$47,68,175 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$98,101,104,112 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 375 #molecular-weight 39833 #checksum 3372 SEQUENCE /// ENTRY A26468 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) I - rat ALTERNATE_NAMES alcohol dehydrogenase 1; class I alcohol dehydrogenase alpha chain ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 19-Nov-1988 #sequence_revision 19-Nov-1988 #text_change 11-Jun-1999 ACCESSIONS A26468; A26211; A33372; S34774 REFERENCE A26468 !$#authors Crabb, D.W.; Edenberg, H.J. !$#journal Gene (1986) 48:287-291 !$#title Complete amino acid sequence of rat liver alcohol !1dehydrogenase deduced from the cDNA sequence. !$#cross-references MUID:87163532; PMID:2881847 !$#accession A26468 !'##molecule_type mRNA !'##residues 1-376 ##label CRA !'##cross-references GB:M15327; NID:g202726; PIDN:AAA40681.1; !1PID:g202727 REFERENCE A26211 !$#authors Jornvall, H.; Markovic, O. !$#journal Eur. J. Biochem. (1972) 29:167-174 !$#title Structural studies of alcohol dehydrogenase from rat liver. !$#cross-references MUID:73031732; PMID:4673366 !$#accession A26211 !'##molecule_type protein !'##residues 2-6;10-11;41-45,'S',47-48;77-102;215-220;236-251;372-376 !1##label JOR !'##experimental_source liver REFERENCE A33372 !$#authors Crabb, D.W.; Stein, P.M.; Dipple, K.M.; Hittle, J.B.; Sidhu, !1R.; Qulali, M.; Zhang, K.; Edenberg, H.J. !$#journal Genomics (1989) 5:906-914 !$#title Structure and expression of the rat class I alcohol !1dehydrogenase gene. !$#cross-references MUID:90077433; PMID:2591969 !$#accession A33372 !'##molecule_type DNA !'##residues 1-142,'I',144-376 ##label CR2 !'##cross-references GB:M29523; GB:J04747; NID:g202735; PIDN:AAA85462.1; !1PID:g202737 REFERENCE S34774 !$#authors Estonius, M.; Danielsson, O.; Karlsson, C.; Persson, H.; !1Joernvall, H.; Hoeoeg, J.O. !$#journal Eur. J. Biochem. (1993) 215:497-503 !$#title Distribution of alcohol and sorbitol dehydrogenases. !1Assessment of mRNA species in mammalian tissues. !$#cross-references MUID:93345539; PMID:8344317 !$#accession S34774 !'##status preliminary !'##molecule_type mRNA !'##residues 47-142,'I',144-163,'T',165-179 ##label EST !'##cross-references EMBL:X72792; NID:g297818; PIDN:CAA51307.1; !1PID:g871524 COMMENT The class I alcohol dehydrogenases are pyrazole-sensitive !1and have a high activity for ethanol. GENETICS !$#introns 6/3; 40/3; 87/2; 116/2; 190/3; 323/1; 369/2 COMPLEX homodimer FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS acetylated amino end; alcohol metabolism; homodimer; !1metalloprotein; NAD; oxidoreductase; zinc FEATURE !$2-376 #product alcohol dehydrogenase I #status predicted !8#label MAT\ !$32-367 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$196-225 #region beta-alpha-beta NAD nucleotide-binding fold\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental\ !$47,68,176 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$98,101,104,112 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 376 #molecular-weight 39645 #checksum 1480 SEQUENCE /// ENTRY S29343 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) I - rabbit ALTERNATE_NAMES alcohol dehydrogenase 1 ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 25-Feb-1994 #sequence_revision 10-Nov-1995 #text_change 11-Jun-1999 ACCESSIONS S30353; S29343 REFERENCE S30353 !$#authors Hoeoeg, J.O.; Vagelopoulos, N.; Yip, P.K.; Keung, W.M.; !1Joernvall, H. !$#journal Eur. J. Biochem. (1993) 213:31-38 !$#title Isozyme developments in mammalian class-I alcohol !1dehydrogenase. cDNA cloning, functional correlations, and !1lack of evidence for genetic isozymes in rabbit. !$#cross-references MUID:93238701; PMID:8477702 !$#accession S30353 !'##molecule_type mRNA !'##residues 1-375 ##label HO2 !'##cross-references EMBL:X69799; NID:g1441; PIDN:CAA49458.1; PID:g1442 !'##note the authors did not translate the codon for residue 1 !'##note submitted to the EMBL Data Library, December 1992 COMMENT The class I alcohol dehydrogenases are pyrazole-sensitive !1and have a high activity for ethanol. COMPLEX homodimer FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS acetylated amino end; alcohol metabolism; dimer; !1metalloprotein; NAD; oxidoreductase; zinc FEATURE !$2-375 #product alcohol dehydrogenase I #status predicted !8#label MAT\ !$32-366 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$195-224 #region beta-alpha-beta NAD nucleotide-binding fold\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status predicted\ !$47,68,175 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$98,101,104,112 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 375 #molecular-weight 39588 #checksum 8227 SEQUENCE /// ENTRY A48257 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) I - pocket gopher (Geomys bursarius) ORGANISM #formal_name Geomys bursarius #common_name pocket gopher DATE 04-Sep-1997 #sequence_revision 04-Sep-1997 #text_change 11-Jun-1999 ACCESSIONS A48257; I60972 REFERENCE A48257 !$#authors Bradley, R.D.; Bull, J.J.; Johnson, A.D.; Hillis, D.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:8939-8941 !$#title Origin of a novel allele in a mammalian hybrid zone. !$#cross-references MUID:94022290; PMID:8415634 !$#accession A48257 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-375 ##label RES !'##cross-references GB:L15463; NID:g294289; PIDN:AAA03595.1; !1PID:g294290 !'##experimental_source wild gophers (G. bursarius major), M allele !$#accession I60972 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-128,'S',130-375 ##label RE2 !'##cross-references GB:L15466; NID:g294295; PIDN:AAA03598.1; !1PID:g294296 !'##experimental_source wild gophers (G. bursarius major), M'' allele !'##note only the differences from PIR:I60973 and GenBank entry PPGADHAA !1are shown COMMENT The class I alcohol dehydrogenases are pyrazole-sensitive !1and have a high activity for ethanol. GENETICS !$#gene ADH1 COMPLEX dimer FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS acetylated amino end; alcohol metabolism; dimer; !1metalloprotein; NAD; oxidoreductase; zinc FEATURE !$2-375 #product alcohol dehydrogenase I #status predicted !8#label MAT\ !$32-366 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$195-224 #region beta-alpha-beta NAD nucleotide-binding fold\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status predicted\ !$47,68,175 #binding_site zinc, catalytic (Cys, His, Cys) #status !8experimental\ !$98,101,104,112 #binding_site zinc, noncatalytic (Cys) #status !8experimental SUMMARY #length 375 #molecular-weight 39985 #checksum 2409 SEQUENCE /// ENTRY I60970 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) I - pocket gopher hybrid (Geomys knoxjonesi x Geomys bursarius major) ORGANISM #formal_name Geomys knoxjonesi x Geomys bursarius major #common_name pocket gopher DATE 04-Sep-1997 #sequence_revision 04-Sep-1997 #text_change 11-Jun-1999 ACCESSIONS I60970; I60971 REFERENCE A48257 !$#authors Bradley, R.D.; Bull, J.J.; Johnson, A.D.; Hillis, D.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:8939-8941 !$#title Origin of a novel allele in a mammalian hybrid zone. !$#cross-references MUID:94022290; PMID:8415634 !$#accession I60970 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-375 ##label RES !'##cross-references GB:L15464; NID:g294291; PIDN:AAA03596.1; !1PID:g294292 !'##experimental_source wild gophers from a hybrid zone (G. knoxjonesi x !1G. bursarius major), N allele !'##note only the differences from PIR:I60973 and GenBank entry PPGADHAA !1are shown; the N allele has been found only in hybrid !1animals !$#accession I60971 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-115,'D',117-375 ##label RE2 !'##cross-references GB:L15465; NID:g294293; PIDN:AAA03597.1; !1PID:g294294 !'##experimental_source wild gophers from a hybrid zone (G. knoxjonesi x !1G. bursarius major), M' allele !'##note only the differences from PIR:I60973 and GenBank entry PPGADHAA !1are shown; two silent mutations distinguish the M' allele !1from the parental M allele COMMENT The class I alcohol dehydrogenases are pyrazole-sensitive !1and have a high activity for ethanol. GENETICS !$#gene ADH1 COMPLEX dimer FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS acetylated amino end; alcohol metabolism; dimer; !1metalloprotein; NAD; oxidoreductase; zinc FEATURE !$2-375 #product alcohol dehydrogenase I #status predicted !8#label MAT\ !$32-366 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$195-224 #region beta-alpha-beta NAD nucleotide-binding fold\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status predicted\ !$47,68,175 #binding_site zinc, catalytic (Cys, His, Cys) #status !8experimental\ !$98,101,104,112 #binding_site zinc, noncatalytic (Cys) #status !8experimental SUMMARY #length 375 #molecular-weight 39984 #checksum 2429 SEQUENCE /// ENTRY I60973 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) I - pocket gopher (Geomys knoxjonesi) ORGANISM #formal_name Geomys knoxjonesi #common_name pocket gopher DATE 04-Sep-1997 #sequence_revision 04-Sep-1997 #text_change 11-Jun-1999 ACCESSIONS I60973; I60974 REFERENCE A48257 !$#authors Bradley, R.D.; Bull, J.J.; Johnson, A.D.; Hillis, D.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:8939-8941 !$#title Origin of a novel allele in a mammalian hybrid zone. !$#cross-references MUID:94022290; PMID:8415634 !$#accession I60973 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-375 ##label RES !'##cross-references GB:L15462; NID:g294297; PIDN:AAA03599.1; !1PID:g294298 !'##experimental_source wild gophers (G. knoxjonesi), K allele !'##note only the differences from PIR:I60973 and GenBank entry PPGADHAA !1are shown !$#accession I60974 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-29,'A',31-375 ##label RE2 !'##cross-references GB:L15461; NID:g294299; PIDN:AAA03600.1; !1PID:g294300 !'##experimental_source wild gophers (G. knoxjonesi), K' allele !'##note only the differences from PIR:I60973 and GenBank entry PPGADHAA !1are shown COMMENT The class I alcohol dehydrogenases are pyrazole-sensitive !1and have a high activity for ethanol. GENETICS !$#gene ADH1 COMPLEX dimer FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS acetylated amino end; alcohol metabolism; dimer; !1metalloprotein; NAD; oxidoreductase; zinc FEATURE !$2-375 #product alcohol dehydrogenase I #status predicted !8#label MAT\ !$32-366 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$195-224 #region beta-alpha-beta NAD nucleotide-binding fold\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status predicted\ !$47,68,175 #binding_site zinc, catalytic (Cys, His, Cys) #status !8experimental\ !$98,101,104,112 #binding_site zinc, noncatalytic (Cys) #status !8experimental SUMMARY #length 375 #molecular-weight 39942 #checksum 2578 SEQUENCE /// ENTRY DECHA1 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) I - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 11-Jun-1999 ACCESSIONS S13851; A38775; S11076 REFERENCE S13851 !$#authors Estonius, M.; Karlsson, C.; Fox, E.A.; Hoeoeg, J.O.; !1Holmquist, B.; Vallee, B.L.; Davidson, W.S.; Joernvall, H. !$#journal Eur. J. Biochem. (1990) 194:593-602 !$#title Avian alcohol dehydrogenase: the chicken liver enzyme. !1Primary structure, cDNA-cloning, and relationships to other !1alcohol dehydrogenases. !$#cross-references MUID:91099336; PMID:2269284 !$#accession S13851 !'##molecule_type protein !'##residues 1-375 ##label EST1 !$#accession A38775 !'##molecule_type mRNA !'##residues 47-375 ##label EST2 !'##cross-references EMBL:X54612; NID:g62840; PIDN:CAA38433.1; !1PID:g62841 REFERENCE S11074 !$#authors Egestad, B.; Estonius, M.; Danielsson, O.; Persson, B.; !1Cederlund, E.; Kaiser, R.; Holmquist, B.; Vallee, B.; Pares, !1X.; Jefferey, J.; Joernvall, H. !$#journal FEBS Lett. (1990) 269:194-196 !$#title Fast atom bombardment mass spectrometry and chemical !1analysis in determinations of acyl-blocked protein !1structures. !$#cross-references MUID:90353571; PMID:2387402 !$#accession S11076 !'##molecule_type protein !'##residues 1-16;359-375 ##label EGE FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway ethanol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS acetylated amino end; alcohol metabolism; metalloprotein; !1NAD; oxidoreductase; zinc FEATURE !$31-366 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$195-224 #region beta-alpha-beta NAD nucleotide-binding fold\ !$1 #modified_site acetylated amino end (Ser) #status !8experimental\ !$46,67,175 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$97,100,103,111 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 375 #molecular-weight 39676 #checksum 861 SEQUENCE /// ENTRY A35837 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) I - Japanese quail ALTERNATE_NAMES alcohol dehydrogenase ADH3 ORGANISM #formal_name Coturnix coturnix japonica #common_name Japanese quail DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 17-Apr-1998 ACCESSIONS A35837 REFERENCE A35837 !$#authors Kaiser, R.; Nussrallah, B.; Dam, R.; Wagner, F.W.; !1Joernvall, H. !$#journal Biochemistry (1990) 29:8365-8371 !$#title Avian alcohol dehydrogenase. Characterization of the quail !1enzyme, functional interpretations, and relationships to the !1different classes of mammalian alcohol dehydrogenase. !$#cross-references MUID:91070061; PMID:2252897 !$#accession A35837 !'##molecule_type protein !'##residues 1-375 ##label KAI !'##experimental_source liver FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS acetylated amino end; alcohol metabolism; metalloprotein; !1NAD; oxidoreductase; zinc FEATURE !$31-366 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$195-224 #region beta-alpha-beta NAD nucleotide-binding fold\ !$1 #modified_site acetylated amino end (Ser) #status !8experimental\ !$46,67,175 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$97,100,103,111 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 375 #molecular-weight 39807 #checksum 1024 SEQUENCE /// ENTRY S48157 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) I - ostrich ORGANISM #formal_name Struthio camelus #common_name ostrich DATE 07-May-1995 #sequence_revision 21-Jul-1995 #text_change 26-Feb-1999 ACCESSIONS S48157; S66191 REFERENCE S48157 !$#authors Estonius, M.; Hjelmqvist, L.; Joernvall, H. !$#journal Eur. J. Biochem. (1994) 224:373-378 !$#title Diversity of vertebrate class I alcohol dehydrogenase. !1Mammalian and non-mammalian enzyme functions correlated !1through the structure of a ratite enzyme. !$#cross-references MUID:95010012; PMID:7925350 !$#accession S48157 !'##molecule_type protein !'##residues 1-374 ##label EST !'##note 112-Cys was also found REFERENCE S66191 !$#authors Hjelmqvist, L.; Hackett, M.; Shafqat, J.; Danielsson, O.; !1Iida, J.; Hendrickson, R.C.; Michel, H.; Shabanowitz, J.; !1Hunt, D.F.; Joernvall, H. !$#journal FEBS Lett. (1995) 367:237-240 !$#title Multiplicity of N-terminal structures of medium-chain !1alcohol dehydrogenases. Mass-spectrometric analysis of !1plant, lower vertebrate and higher vertebrate class I, II, !1and III forms of the enzyme. !$#cross-references MUID:95331382; PMID:7607314 !$#accession S66191 !'##molecule_type protein !'##residues 6-8;11-25 ##label HJE COMMENT The class I alcohol dehydrogenases are pyrazole-sensitive !1and have a high activity for ethanol. COMPLEX homodimer FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS acetylated amino end; alcohol metabolism; dimer; !1metalloprotein; NAD; oxidoreductase; zinc FEATURE !$31-365 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$194-223 #region beta-alpha-beta NAD nucleotide-binding fold\ !$1 #modified_site acetylated amino end (Ser) #status !8experimental\ !$46,67,174 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$97,100,103,111 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 374 #molecular-weight 39583 #checksum 8157 SEQUENCE /// ENTRY S66272 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) I - brown kiwi ORGANISM #formal_name Apteryx australis #common_name brown kiwi DATE 19-Mar-1997 #sequence_revision 29-Aug-1997 #text_change 11-Jun-1999 ACCESSIONS S66272; S66200; S66193; I51312 REFERENCE I51312 !$#authors Hjelmqvist, L.; Metsis, M.; Persson, H.; Hoeoeg, J.O.; !1McLennan, J.; Joernvall, H. !$#journal FEBS Lett. (1995) 367:306-310 !$#title Alcohol dehydrogenase of class I: kiwi liver enzyme, !1parallel evolution in separate vertebrate lines, and !1correlation with 12S rRNA patterns. !$#cross-references MUID:95331397; PMID:7541757 !$#accession S66272 !'##molecule_type mRNA !'##residues 1-375 ##label HJE !'##cross-references EMBL:S78778; NID:g1042207; PIDN:AAC60755.1; !1PID:g1042208 !'##experimental_source subsp. australis; liver !'##note the authors did not translate the codon for residue 1 !$#accession S66200 !'##molecule_type protein !'##residues 2-108;115-134;161-169;235-245;302-324;332-365 ##label HJW REFERENCE S66191 !$#authors Hjelmqvist, L.; Hackett, M.; Shafqat, J.; Danielsson, O.; !1Iida, J.; Hendrickson, R.C.; Michel, H.; Shabanowitz, J.; !1Hunt, D.F.; Joernvall, H. !$#journal FEBS Lett. (1995) 367:237-240 !$#title Multiplicity of N-terminal structures of medium-chain !1alcohol dehydrogenases. Mass-spectrometric analysis of !1plant, lower vertebrate and higher vertebrate class I, II, !1and III forms of the enzyme. !$#cross-references MUID:95331382; PMID:7607314 !$#accession S66193 !'##molecule_type protein !'##residues 2-26 ##label HJF COMMENT The class I alcohol dehydrogenases are pyrazole-sensitive !1and have a high activity for ethanol. COMPLEX homodimer FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS acetylated amino end; alcohol metabolism; metalloprotein; !1NAD; oxidoreductase; zinc FEATURE !$2-375 #product alcohol dehydrogenase I #status experimental !8#label MAT\ !$32-366 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$195-224 #region beta-alpha-beta NAD nucleotide-binding fold\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental\ !$47,68,175 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$98,101,104,112 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 375 #molecular-weight 39631 #checksum 6802 SEQUENCE /// ENTRY S35669 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) I - American alligator ORGANISM #formal_name Alligator mississippiensis #common_name American alligator DATE 19-Mar-1997 #sequence_revision 25-Apr-1997 #text_change 26-Feb-1999 ACCESSIONS S35669 REFERENCE S35669 !$#authors Persson, B.; Bergman, T.; Keung, W.M.; Waldenstroem, U.; !1Holmquist, B.; Vallee, B.L.; Joernvall, H. !$#journal Eur. J. Biochem. (1993) 216:49-56 !$#title Basic features of class-I alcohol dehydrogenase: variable !1and constant segments coordinated by inter-class and !1intra-class variability. Conclusions from characterization !1of the alligator enzyme. !$#cross-references MUID:93373946; PMID:8365416 !$#accession S35669 !'##status preliminary !'##molecule_type protein !'##residues 1-374 ##label PER !'##note 317-Ser was also found COMMENT The class I alcohol dehydrogenases are pyrazole-sensitive !1and have a high activity for ethanol. FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS acetylated amino end; alcohol metabolism; metalloprotein; !1NAD; oxidoreductase; zinc FEATURE !$31-365 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$194-223 #region beta-alpha-beta NAD nucleotide-binding fold\ !$1 #modified_site acetylated amino end (Ser) #status !8experimental\ !$46,67,174 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$97,100,103,111 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 374 #molecular-weight 39684 #checksum 5321 SEQUENCE /// ENTRY S62640 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) I - Indian cobra ORGANISM #formal_name Naja naja naja #common_name Indian cobra DATE 06-Dec-1996 #sequence_revision 13-Mar-1997 #text_change 17-Mar-2000 ACCESSIONS S62640 REFERENCE S62640 !$#authors Shafqat, J.; Hjelmqvist, L.; Joernvall, H. !$#journal Eur. J. Biochem. (1996) 236:571-578 !$#title Liver class-I alcohol dehydrogenase isozyme relationships !1and constant patterns in a variable basic structure. !1Distinctions from characterization of an ethanol !1dehydrogenase in cobra, Naja naja. !$#cross-references MUID:96195667; PMID:8612631 !$#accession S62640 !'##status preliminary !'##molecule_type protein !'##residues 1-375 ##label SHA !'##note the source is designated as Naja naja and was obtained from !1Pakistan, so we have assigned it to the most probable !1subspecies COMMENT The class I alcohol dehydrogenases are pyrazole-sensitive !1and have a high activity for ethanol. FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS acetylated amino end; alcohol metabolism; metalloprotein; !1NAD; oxidoreductase; zinc FEATURE !$31-366 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$194-223 #region beta-alpha-beta NAD nucleotide-binding fold\ !$1 #modified_site acetylated amino end (Ser) #status !8predicted\ !$46,67,174 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$97,100,103,111 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 375 #molecular-weight 39954 #checksum 5293 SEQUENCE /// ENTRY S62638 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) I chain A - Indian spiny-tailed lizard ORGANISM #formal_name Uromastyx hardwickii #common_name Indian spiny-tailed lizard DATE 24-Aug-1996 #sequence_revision 13-Mar-1997 #text_change 26-Feb-1999 ACCESSIONS S62638; S20429 REFERENCE S62638 !$#authors Hjelmqvist, L.; Shafqat, J.; Siddiqi, A.R.; Joernvall, H. !$#journal Eur. J. Biochem. (1996) 236:563-570 !$#title Linking of isozyme and class variability patterns in the !1emergence of novel alcohol dehydrogenase functions: !1characterization of isozymes in Uromastix hardwickii. !$#cross-references MUID:96195666; PMID:8612630 !$#accession S62638 !'##status preliminary !'##molecule_type protein !'##residues 1-375 ##label HJE REFERENCE S20429 !$#authors Hjelmqvist, L.; Ericsson, M.; Shafqat, J.; Carlquist, M.; !1Siddiqi, A.R.; Hoeoeg, J.O.; Joernvall, H. !$#journal FEBS Lett. (1992) 298:297-300 !$#title Reptilian alcohol dehydrogenase. Heterogeneity relevant to !1class multiplicity of the mammalian enzyme. !$#cross-references MUID:92183888; PMID:1544464 !$#accession S20429 !'##molecule_type protein !'##residues 1-18 ##label HJ2 COMMENT The class I alcohol dehydrogenases are pyrazole-sensitive !1and have a high activity for ethanol. FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS acetylated amino end; alcohol metabolism; dimer; !1metalloprotein; NAD; oxidoreductase; zinc FEATURE !$31-366 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$194-223 #region beta-alpha-beta NAD nucleotide-binding fold\ !$1 #modified_site acetylated amino end (Gly) #status !8experimental\ !$46,67,174 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$97,100,103,111 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 375 #molecular-weight 39663 #checksum 3336 SEQUENCE /// ENTRY S62639 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) I chain B - Indian spiny-tailed lizard ORGANISM #formal_name Uromastyx hardwickii #common_name Indian spiny-tailed lizard DATE 24-Aug-1996 #sequence_revision 13-Mar-1997 #text_change 26-Feb-1999 ACCESSIONS S62639; S20430 REFERENCE S62638 !$#authors Hjelmqvist, L.; Shafqat, J.; Siddiqi, A.R.; Joernvall, H. !$#journal Eur. J. Biochem. (1996) 236:563-570 !$#title Linking of isozyme and class variability patterns in the !1emergence of novel alcohol dehydrogenase functions: !1characterization of isozymes in Uromastix hardwickii. !$#cross-references MUID:96195666; PMID:8612630 !$#accession S62639 !'##status preliminary !'##molecule_type protein !'##residues 1-375 ##label HJE REFERENCE S20429 !$#authors Hjelmqvist, L.; Ericsson, M.; Shafqat, J.; Carlquist, M.; !1Siddiqi, A.R.; Hoeoeg, J.O.; Joernvall, H. !$#journal FEBS Lett. (1992) 298:297-300 !$#title Reptilian alcohol dehydrogenase. Heterogeneity relevant to !1class multiplicity of the mammalian enzyme. !$#cross-references MUID:92183888; PMID:1544464 !$#accession S20430 !'##molecule_type protein !'##residues 1-18 ##label HJ2 COMMENT The class I alcohol dehydrogenases are pyrazole-sensitive !1and have a high activity for ethanol. FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS acetylated amino end; alcohol metabolism; dimer; !1metalloprotein; NAD; oxidoreductase; zinc FEATURE !$31-366 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$194-223 #region beta-alpha-beta NAD nucleotide-binding fold\ !$1 #modified_site acetylated amino end (Ser) #status !8experimental\ !$46,67,174 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$97,100,103,111 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 375 #molecular-weight 40060 #checksum 2145 SEQUENCE /// ENTRY A38405 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) I - Perez's frog ORGANISM #formal_name Rana perezi #common_name Perez's frog DATE 12-Jul-1991 #sequence_revision 12-Jul-1991 #text_change 24-Apr-1998 ACCESSIONS A38405 REFERENCE A38405 !$#authors Cederlund, E.; Peralba, J.M.; Pares, X.; Joernvall, H. !$#journal Biochemistry (1991) 30:2811-2816 !$#title Amphibian alcohol dehydrogenase, the major frog liver !1enzyme. Relationships to other forms and assessment of an !1early gene duplication separating vertebrate class I and !1class III alcohol dehydrogenases. !$#cross-references MUID:91175722; PMID:2007119 !$#accession A38405 !'##molecule_type protein !'##residues 1-375 ##label CED COMMENT The class I alcohol dehydrogenases are pyrazole-sensitive !1and have a high activity for ethanol. COMPLEX homodimer FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS acetylated amino end; alcohol metabolism; dimer; !1metalloprotein; NAD; oxidoreductase; zinc FEATURE !$31-366 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$195-224 #region beta-alpha-beta NAD nucleotide-binding fold\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$46,68,175 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$98,101,104,112 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 375 #molecular-weight 40184 #checksum 3638 SEQUENCE /// ENTRY DEHUAS #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) 7 [validated] - human ALTERNATE_NAMES alcohol dehydrogenase mu chain [misnomer]; alcohol dehydrogenase sigma chain; class IV alcohol dehydrogenase; gastric alcohol dehydrogenase; stomach alcohol dehydrogenase CONTAINS retinol dehydrogenase (EC 1.1.1.105) ORGANISM #formal_name Homo sapiens #common_name man DATE 23-Mar-1995 #sequence_revision 08-Mar-1996 #text_change 15-Sep-2000 ACCESSIONS A55878; A54018; A56083; S48667; JC2546; S48147; S21170 REFERENCE A55878 !$#authors Kedishvili, N.Y.; Bosron, W.F.; Stone, C.L.; Hurley, T.D.; !1Peggs, C.F.; Thomasson, H.R.; Popov, K.M.; Carr, L.G.; !1Edenberg, H.J.; Li, T.K. !$#journal J. Biol. Chem. (1995) 270:3625-3630 !$#title Expression and kinetic characterization of recombinant human !1stomach alcohol dehydrogenase. Active-site amino acid !1sequence explains substrate specificity compared with liver !1isozymes. !$#cross-references MUID:95181314; PMID:7876099 !$#accession A55878 !'##molecule_type mRNA !'##residues 1-374 ##label KED !'##cross-references GB:U09623; NID:g790523; PIDN:AAA82165.1; !1PID:g790524 !'##note parts of this sequence were determined by protein sequencing; !1the amino end of the mature protein is blocked !'##note the authors found this sequence possesses retinol dehydrogenase !1activity in the stomach REFERENCE A54018 !$#authors Satre, M.A.; Zgombic-Knight, M.; Duester, G. !$#journal J. Biol. Chem. (1994) 269:15606-15612 !$#title The complete structure of human class IV alcohol !1dehydrogenase (retinol dehydrogenase) determined from the !1ADH7 gene. !$#cross-references MUID:94253145; PMID:8195208 !$#accession A54018 !'##molecule_type mRNA !'##residues 1-374 ##label SAT !'##cross-references GB:U07821; NID:g499097; PIDN:AAA19002.1; !1PID:g499098 !'##experimental_source stomach REFERENCE A56083 !$#authors Zgombic-Knight, M.; Foglio, M.H.; Duester, G. !$#journal J. Biol. Chem. (1995) 270:4305-4311 !$#title Genomic structure and expression of the ADH7 gene encoding !1human class IV alcohol dehydrogenase, the form most !1efficient for retinol metabolism in vitro. !$#cross-references MUID:95181413; PMID:7876191 !$#accession A56083 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-374 ##label ZGO !'##cross-references GB:U16286; GB:U16287; GB:U16288; GB:U16289; !1GB:U16290; GB:U16291; GB:U16292; GB:U16293; NID:g642480; !1PIDN:AAC51351.1; PID:g642482 REFERENCE S48667 !$#authors Yokoyama, S.; Matsuo, Y.; Ramsbotham, R.; Yokoyama, R. !$#journal FEBS Lett. (1994) 351:411-415 !$#title Molecular characterization of a class IV human alcohol !1dehydrogenase gene (ADH7). !$#cross-references MUID:94364515; PMID:8082805 !$#accession S48667 !'##molecule_type DNA !'##residues 1-107,'E',109-272,'D',274-286,'V',288-374 ##label YOK1 !'##cross-references GB:L33179; NID:g516617 !'##note the authors translated the codon GAT (Asp) for residue 108 as !1Glu and GAA (Glu) for residue 273 as Asp !'##note the sequence in GenBank entry HUMALDE, release 103 !1(PID:g516618) corresponds to a processed mRNA sequence REFERENCE JC2546 !$#authors Yokoyama, H.; Baraona, E.; Lieber, C.S. !$#journal Biochem. Biophys. Res. Commun. (1994) 203:219-224 !$#title Molecular cloning of human class IV alcohol dehydrogenase !1cDNA. !$#cross-references MUID:94354804; PMID:8074657 !$#accession JC2546 !'##molecule_type mRNA !'##residues 2-374 ##label YOK2 !'##cross-references GB:L33179; NID:g516617; PIDN:AAA59211.1; !1PID:g516618 !'##experimental_source stomach REFERENCE S48147 !$#authors Farres, J.; Moreno, A.; Crosas, B.; Peralba, J.M.; !1Allali-Hassani, A.; Hjelmqvist, L.; Joernvall, H.; Pares, X. !$#journal Eur. J. Biochem. (1994) 224:549-557 !$#title Alcohol dehydrogenase of class IV (sigma-sigma-ADH) from !1human stomach. cDNA sequence and structure/function !1relationships. !$#cross-references MUID:95010033; PMID:7925371 !$#accession S48147 !'##molecule_type mRNA !'##residues 1-374 ##label FAR !'##cross-references EMBL:X76342; NID:g541674; PIDN:CAA53961.1; !1PID:g541676 REFERENCE S21170 !$#authors Pares, X.; Cederlund, E.; Moreno, A.; Saubi, N.; Hoeoeg, !1J.O.; Joernvall, H. !$#journal FEBS Lett. (1992) 303:69-72 !$#title Class IV alcohol dehydrogenase (the gastric enzyme). !1Structural analysis of human sigmasigma-ADH reveals class IV !1to be variable and confirms the presence of a fifth !1mammalian alcohol dehydrogenase class. !$#cross-references MUID:92275085; PMID:1592118 !$#accession S21170 !'##molecule_type protein !'##residues 12-18,'XR',21;41-46;62-70,'R',72-77,'X',79,'XXXXX',85-86, !1'X',88-111;135-137,'GR',140-142,169;170,171-174 ##label PAR REFERENCE A65066 !$#authors Hurley, T.D.; Xie, P. !$#submission submitted to the Brookhaven Protein Data Bank, June 1996 !$#cross-references PDB:1AGN !$#contents annotation; X-ray crystallography, 3.0 angstroms, residues !12-374 GENETICS !$#gene GDB:ADH7 !'##cross-references GDB:362911; OMIM:600086 !$#map_position 4q23-4q24 !$#introns 6/3; 40/3; 87/1; 116/2; 188/3; 275/3; 321/1; 367/2 COMPLEX homodimer FUNCTION ADH !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation FUNCTION RDH !$#description catalyzes the oxidation of retinol to retinal by NAD+ !$#pathway retinoic acid biosynthesis !$#note retinoic acid regulates epithelial cell differentiation !$#note abundant in stomach, eye, skin, thymus, and ovary CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS acetylated amino end; alcohol metabolism; dimer; !1metalloprotein; NAD; oxidoreductase; zinc FEATURE !$2-374 #product alcohol dehydrogenase 7 #status experimental !8#label MAT\ !$32-365 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$194-223 #region beta-alpha-beta NAD nucleotide-binding fold\ !$2 #modified_site acetylated amino end (Gly) (in mature !8form) #status predicted\ !$47,68,174 #binding_site zinc, catalytic (Cys, His, Cys) #status !8experimental\ !$98,101,104,112 #binding_site zinc, noncatalytic (Cys) #status !8experimental SUMMARY #length 374 #molecular-weight 40005 #checksum 9297 SEQUENCE /// ENTRY A56436 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) IV - mouse ALTERNATE_NAMES class IV alcohol dehydrogenase mu chain; class IV alcohol dehydrogenase sigma chain; gastric alcohol dehydrogenase; stomach alcohol dehydrogenase CONTAINS retinol dehydrogenase (EC 1.1.1.105) ORGANISM #formal_name Mus musculus #common_name house mouse DATE 21-Jul-1995 #sequence_revision 21-Jul-1995 #text_change 11-Jun-1999 ACCESSIONS A56436 REFERENCE A56436 !$#authors Zgombic-Knight, M.; Ang, H.L.; Foglio, M.H.; Duester, G. !$#journal J. Biol. Chem. (1995) 270:10868-10877 !$#title Cloning of the mouse class IV alcohol dehydrogenase (retinol !1dehydrogenase) cDNA and tissue-specific expression patterns !1of the murine ADH gene family. !$#cross-references MUID:95256259; PMID:7738026 !$#accession A56436 !'##molecule_type mRNA !'##residues 1-374 ##label ZGO !'##cross-references GB:U20257; NID:g897584; PIDN:AAA76735.1; !1PID:g897585 GENETICS !$#gene Adh-3 COMPLEX homodimer FUNCTION ADH !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation FUNCTION RDH !$#description catalyzes the oxidation of retinol to retinal by NAD+ !$#pathway retinoic acid biosynthesis !$#note retinoic acid regulates epithelial cell differentiation !$#note abundant in stomach, eye, skin, thymus, and ovary CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS acetylated amino end; alcohol metabolism; dimer; !1metalloprotein; NAD; oxidoreductase; zinc FEATURE !$2-374 #product alcohol dehydrogenase IV #status predicted !8#label MAT\ !$32-365 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$194-223 #region beta-alpha-beta NAD nucleotide-binding fold\ !$2 #modified_site acetylated amino end (Gly) (in mature !8form) #status predicted\ !$47,68,174 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$98,101,104,112 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 374 #molecular-weight 39837 #checksum 577 SEQUENCE /// ENTRY A53142 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) IV - rat ALTERNATE_NAMES class IV alcohol dehydrogenase mu chain; class IV alcohol dehydrogenase sigma chain; gastric alcohol dehydrogenase; stomach alcohol dehydrogenase CONTAINS retinol dehydrogenase (EC 1.1.1.105) ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 06-Oct-1994 #sequence_revision 18-Nov-1994 #text_change 17-Apr-1998 ACCESSIONS A53142 REFERENCE A53142 !$#authors Pares, X.; Cederlund, E.; Moreno, A.; Hjelmqvist, L.; !1Farres, J.; Jornvall, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1994) 91:1893-1897 !$#title Mammalian class IV alcohol dehydrogenase (stomach alcohol !1dehydrogenase): structure, origin, and correlation with !1enzymology. !$#cross-references MUID:94173934; PMID:8127901 !$#accession A53142 !'##molecule_type protein !'##residues 1-374 ##label PAR !'##experimental_source Sprague-Dawley, stomach !'##note sequence extracted from NCBI backbone (NCBIP:145889) COMPLEX homodimer FUNCTION ADH !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation FUNCTION RDH !$#description catalyzes the oxidation of retinol to retinal by NAD+ !$#pathway retinoic acid biosynthesis !$#note retinoic acid regulates epithelial cell differentiation !$#note abundant in stomach, eye, skin, thymus, and ovary CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS acetylated amino end; alcohol metabolism; dimer; !1metalloprotein; NAD; oxidoreductase; zinc FEATURE !$1-374 #product alcohol dehydrogenase IV #status predicted !8#label MAT\ !$32-365 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$194-223 #region beta-alpha-beta NAD nucleotide-binding fold\ !$1 #modified_site acetylated amino end (Ser) #status !8experimental\ !$47,68,174 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$98,101,104,112 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 374 #molecular-weight 40157 #checksum 371 SEQUENCE /// ENTRY DEHUC2 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) 5 [validated] - human ALTERNATE_NAMES alcohol dehydrogenase chi chain; class III alcohol dehydrogenase CONTAINS formaldehyde dehydrogenase (glutathione) (EC 1.2.1.1) ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1991 #sequence_revision 05-Aug-1994 #text_change 15-Sep-2000 ACCESSIONS JH0789; A36739; A33428; A56397; A29983; A61428; S02618; !1S11077 REFERENCE JH0789 !$#authors Hur, M.W.; Edenberg, H.J. !$#journal Gene (1992) 121:305-311 !$#title Cloning and characterization of the ADH5 gene encoding human !1alcohol dehydrogenase 5, formaldehyde dehydrogenase. !$#cross-references MUID:93077045; PMID:1446828 !$#accession JH0789 !'##molecule_type DNA !'##residues 1-374 ##label HUR !'##cross-references GB:M81112; GB:M81118; NID:g178128; PIDN:AAA51596.1; !1PID:g178130 !'##note the authors present evidence that translation is initiated at !1Met-1 REFERENCE A36739 !$#authors Sharma, C.P.; Fox, E.A.; Holmquist, B.; Joernvall, H.; !1Vallee, B.L. !$#journal Biochem. Biophys. Res. Commun. (1989) 164:631-637 !$#title cDNA sequence of human class III alcohol dehydrogenase. !$#cross-references MUID:90056459; PMID:2818582 !$#accession A36739 !'##molecule_type mRNA !'##residues 1-374 ##label SHA !'##cross-references GB:M30471; NID:g178133; PIDN:AAA79018.1; !1PID:g178134 REFERENCE A33428 !$#authors Giri, P.R.; Krug, J.F.; Kozak, C.; Moretti, T.; O'Brien, !1S.J.; Seuanez, H.N.; Goldman, D. !$#journal Biochem. Biophys. Res. Commun. (1989) 164:453-460 !$#title Cloning and comparative mapping of a human class III (chi) !1alcohol dehydrogenase cDNA. !$#cross-references MUID:90026418; PMID:2679557 !$#accession A33428 !'##molecule_type mRNA !'##residues 'MGAATPVDSPPRRPESVN',1-166,'Y',168-374 ##label GIR !'##cross-references GB:M29872; NID:g178131 !'##note the authors translated sequence upstream of Met-1 REFERENCE A56397 !$#authors Hur, M.W.; Edenberg, H.J. !$#journal J. Biol. Chem. (1995) 270:9002-9009 !$#title Cell-specific function of cis-acting elements in the !1regulation of human alcohol dehydrogenase 5 gene expression !1and effect of the 5'-nontranslated region. !$#cross-references MUID:95238401; PMID:7721811 !$#accession A56397 !'##molecule_type DNA !'##residues 1-4 ##label HU2 !'##cross-references GB:U10902; NID:g854723; PIDN:AAA83432.1; !1PID:g1122906 REFERENCE A29983 !$#authors Kaiser, R.; Holmquist, B.; Hempel, J.; Vallee, B.L.; !1Joernvall, H. !$#journal Biochemistry (1988) 27:1132-1140 !$#title Class III human liver alcohol dehydrogenase: a novel !1structural type equidistantly related to the class I and !1class II enzymes. !$#cross-references MUID:88209465; PMID:3365377 !$#accession A29983 !'##molecule_type protein !'##residues 2-374 ##label KAI REFERENCE A61428 !$#authors Kaiser, R.; Holmquist, B.; Vallee, B.L.; Joernvall, H. !$#journal J. Protein Chem. (1991) 10:69-73 !$#title Human class III alcohol dehydrogenase/glutathione-dependent !1formaldehyde dehydrogenase. !$#cross-references MUID:91273763; PMID:2054065 !$#accession A61428 !'##molecule_type protein !'##residues 2-374 ##label KA2 REFERENCE A66716 !$#authors Yang, Z.N.; Hurley, T.D. !$#submission submitted to the Brookhaven Protein Data Bank, February 1996 !$#cross-references PDB:1TEH !$#contents annotation; X-ray crystallography, 2.70 angstroms, residues !12-374 COMMENT Class III alcohol dehydrogenases are pyrazole-insensitive, !1are not very active toward ethanol and possess !1glutathione-dependent formaldehyde dehydrogenase activity. GENETICS !$#gene GDB:ADH5 !'##cross-references GDB:118978; OMIM:103710 !$#map_position 4q21-4q25 !$#introns 4/3; 38/3; 86/1; 115/2; 188/3; 275/3; 321/1; 367/2 COMPLEX homodimer; does not form heterodimers with the class I !1alcohol dehydrogenases FUNCTION ADH !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#note human alcohol dehydrogenase chi is expressed predominately !1in liver, kidney, and brain, but is expressed in all tissues !1tested and in all stages of development FUNCTION FDH !$#description catalyzes the oxidation by NAD+ of formaldehyde and !1glutathione to S-formylglutathione CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS acetylated amino end; alcohol metabolism; homodimer; !1metalloprotein; NAD; oxidoreductase; zinc FEATURE !$2-374 #product alcohol dehydrogenase 5 #status experimental !8#label MAT\ !$30-365 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$194-223 #region beta-alpha-beta NAD nucleotide-binding fold\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental\ !$45,67,174 #binding_site zinc, catalytic (Cys, His, Cys) #status !8experimental\ !$97,100,103,111 #binding_site zinc, noncatalytic (Cys) #status !8experimental SUMMARY #length 374 #molecular-weight 39724 #checksum 9148 SEQUENCE /// ENTRY A33419 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) class III - horse CONTAINS formaldehyde dehydrogenase (glutathione) (EC 1.2.1.1) ORGANISM #formal_name Equus caballus #common_name domestic horse DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 01-May-1998 ACCESSIONS A33419 REFERENCE A33419 !$#authors Kaiser, R.; Holmquist, B.; Vallee, B.L.; Joernvall, H. !$#journal Biochemistry (1989) 28:8432-8438 !$#title Characteristics of mammalian class III alcohol !1dehydrogenases, an enzyme less variable than the traditional !1liver enzyme of class I. !$#cross-references MUID:90105360; PMID:2690942 !$#accession A33419 !'##molecule_type protein !'##residues 1-373 ##label KAI COMMENT Class III alcohol dehydrogenases are pyrazole-insensitive, !1are not very active toward ethanol and possess !1glutathione-dependent formaldehyde dehydrogenase activity. COMPLEX homodimer; does not form heterodimers with the class I !1alcohol dehydrogenases FUNCTION ADH !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ FUNCTION FDH !$#description catalyzes the oxidation by NAD+ of formaldehyde and !1glutathione to S-formylglutathione CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS acetylated amino end; alcohol metabolism; homodimer; !1metalloprotein; NAD; oxidoreductase; zinc FEATURE !$1-373 #product alcohol dehydrogenase chi chain #status !8experimental #label MAT\ !$29-364 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$193-222 #region beta-alpha-beta NAD nucleotide-binding fold\ !$1 #modified_site acetylated amino end (Ser) #status !8experimental\ !$44,66,173 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$96,99,102,110 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 373 #molecular-weight 39440 #checksum 6584 SEQUENCE /// ENTRY DERTA #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) 2 - rat ALTERNATE_NAMES alcohol dehydrogenase chi chain; class III alcohol dehydrogenase CONTAINS formaldehyde dehydrogenase (glutathione) (EC 1.2.1.1) ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 01-May-1998 ACCESSIONS S00331; S02619; S06633 REFERENCE S00331 !$#authors Julia, P.; Pares, X.; Joernvall, H. !$#journal Eur. J. Biochem. (1988) 172:73-83 !$#title Rat liver alcohol dehydrogenase of class III. Primary !1structure, functional consequences and relationships to !1other alcohol dehydrogenases. !$#cross-references MUID:88152004; PMID:3278908 !$#accession S00331 !'##molecule_type protein !'##residues 1-373 ##label JUL REFERENCE S02617 !$#authors Fairwell, T.; Julia, P.; Kaiser, R.; Holmquist, B.; Pares, !1X.; Vallee, B.L.; Joernvall, H. !$#journal FEBS Lett. (1987) 222:99-103 !$#title Acetylated N-terminal structures of class III alcohol !1dehydrogenases. Differences among the three enzyme classes. !$#cross-references MUID:88005160; PMID:3653405 !$#accession S02619 !'##molecule_type protein !'##residues 1-6 ##label FAI REFERENCE S06633 !$#authors Koivusalo, M.; Baumann, M.; Uotila, L. !$#journal FEBS Lett. (1989) 257:105-109 !$#title Evidence for the identity of glutathione-dependent !1formaldehyde dehydrogenase and class III alcohol !1dehydrogenase. !$#cross-references MUID:90033321; PMID:2806555 !$#accession S06633 !'##status preliminary !'##molecule_type protein !'##residues 9-25;84-95,'X',97-98,'X',187;188,189-193,'X', !1195-198;357-365 ##label KOI !'##experimental_source strain Wistar COMMENT Class III alcohol dehydrogenases are pyrazole-insensitive, !1are not very active toward ethanol and possess !1glutathione-dependent formaldehyde dehydrogenase activity. GENETICS !$#gene ADH-2 COMPLEX homodimer; does not form heterodimers with the class I !1alcohol dehydrogenases FUNCTION ADH !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ FUNCTION FDH !$#description catalyzes the oxidation by NAD+ of formaldehyde and !1glutathione to S-formylglutathione CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS acetylated amino end; alcohol metabolism; homodimer; !1metalloprotein; NAD; oxidoreductase; zinc FEATURE !$1-373 #product alcohol dehydrogenase 2 #status experimental !8#label MAT\ !$29-364 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$193-222 #region beta-alpha-beta NAD nucleotide-binding fold\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$44,66,173 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$96,99,102,110 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 373 #molecular-weight 39426 #checksum 6609 SEQUENCE /// ENTRY A56643 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) 2 - mouse ALTERNATE_NAMES alcohol dehydrogenase chi chain; class III alcohol dehydrogenase CONTAINS formaldehyde dehydrogenase (glutathione) (EC 1.2.1.1) ORGANISM #formal_name Mus musculus #common_name house mouse DATE 11-Aug-1995 #sequence_revision 11-Aug-1995 #text_change 11-Jun-1999 ACCESSIONS A56643; A60269; S71333 REFERENCE A56643 !$#authors Hur, M.W.; Ho, W.H.; Brown, C.J.; Goldman, D.; Edenberg, !1H.J. !$#journal DNA Seq. (1992) 3:167-175 !$#title Molecular cloning of mouse alcohol dehydrogenase-B2 cDNA: !1nucleotide sequences of the class III ADH genes evolve !1slowly even for silent substitutions. !$#cross-references MUID:93112997; PMID:1472709 !$#accession A56643 !'##status preliminary !'##molecule_type mRNA !'##residues 1-374 ##label HUR !'##cross-references GB:M84147; GB:M61707; GB:M81315; NID:g191721; !1PIDN:AAA68896.1; PID:g191722 !'##note sequence extracted from NCBI backbone (NCBIN:121466, !1NCBIP:121468) REFERENCE A60269 !$#authors Edenberg, H.J.; Brown, C.J.; Carr, L.G.; Ho, W.H.; Hur, M.W. !$#journal Adv. Exp. Med. Biol. (1991) 284:253-262 !$#title Alcohol dehydrogenase gene expression and cloning of the !1mouse-chi-like ADH. !$#cross-references MUID:91272926; PMID:2053480 !$#accession A60269 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type mRNA !'##residues 2-374 ##label EDE REFERENCE S71333 !$#authors Foglio, M.H.; Duester, G. !$#journal Eur. J. Biochem. (1996) 237:496-504 !$#title Characterization of the functional gene encoding mouse class !1III alcohol dehydrogenase (glutathione-dependent !1formaldehyde dehydrogenase) and an unexpressed processed !1pseudogene with an intact open reading frame. !$#cross-references MUID:96215448; PMID:8647091 !$#accession S71333 !'##status preliminary !'##molecule_type DNA !'##residues 1-374 ##label FOG !'##cross-references EMBL:U48969; NID:g1399475 COMMENT Class III alcohol dehydrogenases are pyrazole-insensitive, !1are not very active toward ethanol and possess !1glutathione-dependent formaldehyde dehydrogenase activity. GENETICS !$#gene adh-2 !$#introns 4/3; 38/3; 86/1; 115/2; 188/3; 275/3; 321/1; 367/2 COMPLEX homodimer; does not form heterodimers with the class I !1alcohol dehydrogenases FUNCTION ADH !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ FUNCTION FDH !$#description catalyzes the oxidation by NAD+ of formaldehyde and !1glutathione to S-formylglutathione CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS acetylated amino end; alcohol metabolism; homodimer; !1metalloprotein; NAD; oxidoreductase; zinc FEATURE !$2-374 #product alcohol dehydrogenase 2 #status predicted !8#label MAT\ !$30-365 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$194-223 #region beta-alpha-beta NAD nucleotide-binding fold\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status predicted\ !$45,67,174 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$97,100,103,111 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 374 #molecular-weight 39633 #checksum 1156 SEQUENCE /// ENTRY S68061 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) class III - Indian spiny-tailed lizard CONTAINS formaldehyde dehydrogenase (glutathione) (EC 1.2.1.1) ORGANISM #formal_name Uromastyx hardwickii #common_name Indian spiny-tailed lizard DATE 19-Mar-1997 #sequence_revision 29-Aug-1997 #text_change 01-May-1998 ACCESSIONS S68061; S66194 REFERENCE S68061 !$#authors Hjelmqvist, L.; Shafqat, J.; Siddiqi, A.R.; Joernvall, H. !$#journal FEBS Lett. (1995) 373:212-216 !$#title Alcohol dehydrogenase of class III: consistent patterns of !1structural and functional conservation in relation to class !1I and other proteins. !$#cross-references MUID:96033975; PMID:7589468 !$#accession S68061 !'##molecule_type protein !'##residues 1-373 ##label HJE REFERENCE S66191 !$#authors Hjelmqvist, L.; Hackett, M.; Shafqat, J.; Danielsson, O.; !1Iida, J.; Hendrickson, R.C.; Michel, H.; Shabanowitz, J.; !1Hunt, D.F.; Joernvall, H. !$#journal FEBS Lett. (1995) 367:237-240 !$#title Multiplicity of N-terminal structures of medium-chain !1alcohol dehydrogenases. Mass-spectrometric analysis of !1plant, lower vertebrate and higher vertebrate class I, II, !1and III forms of the enzyme. !$#cross-references MUID:95331382; PMID:7607314 !$#accession S66194 !'##molecule_type protein !'##residues 9-14 ##label HJW COMMENT Class III alcohol dehydrogenases are pyrazole-insensitive, !1are not very active toward ethanol and possess !1glutathione-dependent formaldehyde dehydrogenase activity. COMPLEX homodimer FUNCTION ADH !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ FUNCTION FDH !$#description catalyzes the oxidation by NAD+ of formaldehyde and !1glutathione to S-formylglutathione CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS acetylated amino end; alcohol metabolism; dimer; !1metalloprotein; NAD; oxidoreductase; zinc FEATURE !$1-373 #product alcohol dehydrogenase class III #status !8experimental #label MAT\ !$29-364 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$193-222 #region beta-alpha-beta NAD nucleotide-binding fold\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$44,66,173 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$96,99,102,110 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 373 #molecular-weight 39430 #checksum 5507 SEQUENCE /// ENTRY JC4967 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) class III - gilthead sea bream CONTAINS formaldehyde dehydrogenase (glutathione) (EC 1.2.1.1) ORGANISM #formal_name Sparus aurata #common_name gilthead sea bream DATE 31-Dec-1996 #sequence_revision 31-Dec-1996 #text_change 11-Jun-1999 ACCESSIONS JC4967 REFERENCE JC4967 !$#authors Funkenstein, B.; Jakowlew, S.B. !$#journal Gene (1996) 174:159-164 !$#title Molecular cloning of fish alcohol dehydrogenase cDNA. !$#cross-references MUID:97017142; PMID:8863743 !$#accession JC4967 !'##molecule_type mRNA !'##residues 1-376 ##label FUN !'##cross-references GB:U84791; NID:g1814385; PIDN:AAB41888.1; !1PID:g1814386 COMMENT Class III alcohol dehydrogenases are pyrazole-insensitive, !1are not very active toward ethanol and possess !1glutathione-dependent formaldehyde dehydrogenase activity. COMPLEX homodimer FUNCTION ADH !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ FUNCTION FDH !$#description catalyzes the oxidation by NAD+ of formaldehyde and !1glutathione to S-formylglutathione CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; dimer; metalloprotein; NAD; !1oxidoreductase; zinc FEATURE !$2-376 #product alcohol dehydrogenase class III #status !8predicted #label MAT\ !$32-367 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$196-225 #region beta-alpha-beta NAD nucleotide-binding fold\ !$47,69,176 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$99,102,105,113 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 376 #molecular-weight 40214 #checksum 6805 SEQUENCE /// ENTRY S51187 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) class III - Atlantic hagfish CONTAINS formaldehyde dehydrogenase (glutathione) (EC 1.2.1.1) ORGANISM #formal_name Myxine glutinosa #common_name Atlantic hagfish DATE 19-Mar-1997 #sequence_revision 25-Apr-1997 #text_change 26-Feb-1999 ACCESSIONS S51187; S66197 REFERENCE S51187 !$#authors Danielsson, O.; Shafqat, J.; Estonius, M.; Joernvall, H. !$#journal Eur. J. Biochem. (1994) 225:1081-1088 !$#title Alcohol dehydrogenase class III contrasted to class I. !1Characterization of the cyclostome enzyme, the existence of !1multiple forms as for the human enzyme, and distant !1cross-species hybridization. !$#cross-references MUID:95045537; PMID:7957198 !$#accession S51187 !'##molecule_type protein !'##residues 1-376 ##label DAN REFERENCE S66191 !$#authors Hjelmqvist, L.; Hackett, M.; Shafqat, J.; Danielsson, O.; !1Iida, J.; Hendrickson, R.C.; Michel, H.; Shabanowitz, J.; !1Hunt, D.F.; Joernvall, H. !$#journal FEBS Lett. (1995) 367:237-240 !$#title Multiplicity of N-terminal structures of medium-chain !1alcohol dehydrogenases. Mass-spectrometric analysis of !1plant, lower vertebrate and higher vertebrate class I, II, !1and III forms of the enzyme. !$#cross-references MUID:95331382; PMID:7607314 !$#accession S66197 !'##molecule_type protein !'##residues 1-17 ##label HJE COMMENT Class III alcohol dehydrogenases are pyrazole-insensitive, !1are not very active toward ethanol and possess !1glutathione-dependent formaldehyde dehydrogenase activity. COMPLEX homodimer FUNCTION ADH !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ FUNCTION FDH !$#description catalyzes the oxidation by NAD+ of formaldehyde and !1glutathione to S-formylglutathione CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS acetylated amino end; alcohol metabolism; dimer; !1metalloprotein; NAD; oxidoreductase; zinc FEATURE !$32-367 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$196-225 #region beta-alpha-beta NAD nucleotide-binding fold\ !$1 #modified_site acetylated amino end (Ser) #status !8experimental\ !$47,69,176 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$99,102,105,113 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 376 #molecular-weight 39747 #checksum 4299 SEQUENCE /// ENTRY A49662 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) class III - common octopus CONTAINS formaldehyde dehydrogenase (glutathione) (EC 1.2.1.1) ORGANISM #formal_name Octopus vulgaris #common_name common octopus DATE 07-Apr-1994 #sequence_revision 31-Dec-1995 #text_change 01-May-1998 ACCESSIONS A49662 REFERENCE A49662 !$#authors Kaiser, R.; Fernandez, M.R.; Pares, X.; Jornvall, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:11222-11226 !$#title Origin of the human alcohol dehydrogenase system: !1implications from the structure and properties of the !1octopus protein. !$#cross-references MUID:94068576; PMID:8248232 !$#accession A49662 !'##molecule_type protein !'##residues 1-378 ##label KAI !'##experimental_source gills, salivary glands, heart !'##note sequence extracted from NCBI backbone (NCBIP:140464) COMMENT Class III alcohol dehydrogenases are pyrazole-insensitive, !1are not very active toward ethanol and possess !1glutathione-dependent formaldehyde dehydrogenase activity. COMPLEX homodimer FUNCTION ADH !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ FUNCTION FDH !$#description catalyzes the oxidation by NAD+ of formaldehyde and !1glutathione to S-formylglutathione CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS acetylated amino end; alcohol metabolism; dimer; !1metalloprotein; NAD; oxidoreductase; zinc FEATURE !$1-378 #product alcohol dehydrogenase class III #status !8experimental #label MAT\ !$32-367 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$196-225 #region beta-alpha-beta NAD nucleotide-binding fold\ !$1 #modified_site acetylated amino end (Thr) #status !8experimental\ !$47,69,176 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$99,102,105,113 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 378 #molecular-weight 40400 #checksum 6276 SEQUENCE /// ENTRY S51357 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) Fdh - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES class III alcohol dehydrogenase CONTAINS formaldehyde dehydrogenase (glutathione) (EC 1.2.1.1); octanol dehydrogenase (EC 1.1.1.73) ORGANISM #formal_name Drosophila melanogaster DATE 01-Aug-1995 #sequence_revision 01-Sep-1995 #text_change 03-Dec-1999 ACCESSIONS S51357 REFERENCE S51357 !$#authors Luque, T.; Atrian, S.; Danielsson, O.; Joernvall, H.; !1Gonzalez-Duarte, R. !$#journal Eur. J. Biochem. (1994) 225:985-993 !$#title Structure of the Drosophila melanogaster !1glutathione-dependent formaldehyde dehydrogenase/octanol !1dehydrogenase gene (class III alcohol dehydrogenase). !1Evolutionary pathway of the alcohol dehydrogenase genes. !$#cross-references MUID:95045575; PMID:7957234 !$#accession S51357 !'##status preliminary !'##molecule_type DNA !'##residues 1-379 ##label LUQ !'##cross-references EMBL:U07799; NID:g538264; PIDN:AAA57187.1; !1PID:g538265 COMMENT Class III alcohol dehydrogenases are pyrazole-insensitive, !1are not very active toward ethanol and possess !1glutathione-dependent formaldehyde dehydrogenase activity. GENETICS !$#gene FlyBase:Fdh !'##cross-references FlyBase:FBgn0011768 !$#introns 7/3; 37/3 COMPLEX homodimer FUNCTION ADH !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ FUNCTION FDH !$#description catalyzes the oxidation by NAD+ of formaldehyde and !1glutathione to S-formylglutathione CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS acetylated amino end; alcohol metabolism; dimer; !1metalloprotein; NAD; oxidoreductase; zinc FEATURE !$2-379 #product alcohol dehydrogenase Fdh #status predicted !8#label MAT\ !$33-370 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$197-226 #region beta-alpha-beta NAD nucleotide-binding fold\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status predicted\ !$48,70,177 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$100,103,106,114 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 379 #molecular-weight 40389 #checksum 1032 SEQUENCE /// ENTRY S71244 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) class III - Arabidopsis thaliana CONTAINS formaldehyde dehydrogenase (glutathione) (EC 1.2.1.1) ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 28-Oct-1996 #sequence_revision 27-Feb-1997 #text_change 16-Jun-2000 ACCESSIONS S71244 REFERENCE S71244 !$#authors Martinez, M.C. !$#submission submitted to the EMBL Data Library, November 1994 !$#accession S71244 !'##molecule_type mRNA !'##residues 1-379 ##label MAR !'##cross-references EMBL:X82647; NID:g1143387; PIDN:CAA57973.1; !1PID:g1143388 COMMENT Class III alcohol dehydrogenases are pyrazole-insensitive, !1are not very active toward ethanol and possess !1glutathione-dependent formaldehyde dehydrogenase activity. FUNCTION ADH !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ FUNCTION FDH !$#description catalyzes the oxidation by NAD+ of formaldehyde and !1glutathione to S-formylglutathione CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; metalloprotein; NAD; oxidoreductase; !1zinc FEATURE !$32-368 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$197-226 #region beta-alpha-beta NAD nucleotide-binding fold\ !$47,69,177 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$99,102,105,113 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 379 #molecular-weight 40685 #checksum 5257 SEQUENCE /// ENTRY A42343 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) I - Baltic cod ORGANISM #formal_name Gadus morhua callarias #common_name Baltic cod DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 26-Feb-1999 ACCESSIONS A42343 REFERENCE A42343 !$#authors Danielsson, O.; Eklund, H.; Joernvall, H. !$#journal Biochemistry (1992) 31:3751-3759 !$#title The major piscine liver alcohol dehydrogenase has !1class-mixed properties in relation to mammalian alcohol !1dehydrogenases of classes I and III. !$#cross-references MUID:92232665; PMID:1567829 !$#accession A42343 !'##molecule_type protein !'##residues 1-375 ##label DAN COMMENT This enzyme is functionally a class I alcohol dehydrogenase !1although it is structurally more similar to class III !1enzymes. COMMENT The class I alcohol dehydrogenases are pyrazole-sensitive !1and have a high activity for ethanol. COMPLEX homodimer FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway ethanol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS acetylated amino end; alcohol metabolism; dimer; !1metalloprotein; NAD; oxidoreductase; zinc FEATURE !$1-375 #product alcohol dehydrogenase III #status !8experimental #label MAT\ !$31-365 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$195-224 #region beta-alpha-beta NAD nucleotide-binding fold\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$46,68,175 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$98,101,104,112 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 375 #molecular-weight 40127 #checksum 3027 SEQUENCE /// ENTRY D64763 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) C - Escherichia coli (strain K-12) ALTERNATE_NAMES class III alcohol dehydrogenase CONTAINS formaldehyde dehydrogenase (glutathione) (EC 1.2.1.1) ORGANISM #formal_name Escherichia coli DATE 12-Sep-1997 #sequence_revision 17-Sep-1997 #text_change 01-Mar-2002 ACCESSIONS D64763; A42015; S78608 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64763 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-369 ##label BLAT !'##cross-references GB:AE000142; GB:U00096; NID:g1786542; !1PIDN:AAC73459.1; PID:g1786552; UWGP:b0356 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A42015 !$#authors Gutheil, W.G.; Holmquist, B.; Vallee, B.L. !$#journal Biochemistry (1992) 31:475-481 !$#title Purification, characterization, and partial sequence of the !1glutathione-dependent formaldehyde dehydrogenase from !1Escherichia coli: a class III alcohol dehydrogenase. !$#cross-references MUID:92118844; PMID:1731906 !$#accession A42015 !'##molecule_type protein !'##residues 1-24,'X',26-40,'E',42-45,'G',47 ##label GUT !'##note this enzyme also has hemithiolacetal dehydrogenase activity REFERENCE S78608 !$#authors Nashimoto, H.; Saito, N. !$#submission submitted to the EMBL Data Library, May 1996 !$#description Kohara library:8F10. !$#accession S78608 !'##molecule_type DNA !'##residues 'MLPLHLL',11,'VNRWKSLKLTLHHR',26-369 ##label NAS !'##cross-references EMBL:D85613 !'##experimental_source strain K12 COMMENT Class III alcohol dehydrogenases are pyrazole-insensitive, !1are not very active toward ethanol and possess !1glutathione-dependent formaldehyde dehydrogenase activity. GENETICS !$#gene adhC COMPLEX homodimer FUNCTION ADH !$#description catalyzes oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ FUNCTION FDH !$#description catalyzes oxidation by NAD+ of formaldehyde and glutathione !1to S-formylglutathione CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; homodimer; metalloprotein; NAD; !1oxidoreductase; zinc FEATURE !$25-360 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$189-218 #region beta-alpha-beta NAD nucleotide-binding fold\ !$40,62,169 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$92,95,98,106 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 369 #molecular-weight 39359 #checksum 7661 SEQUENCE /// ENTRY S57525 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) C - Escherichia coli (isolate VU 3685) ALTERNATE_NAMES class III alcohol dehydrogenase CONTAINS formaldehyde dehydrogenase (glutathione) (EC 1.2.1.1) ORGANISM #formal_name Escherichia coli DATE 10-Jul-1992 #sequence_revision 01-May-1998 #text_change 11-Jun-1999 ACCESSIONS S57525 REFERENCE S57525 !$#authors Kuemmerle, N.; Feucht, H.; Kaulfers, P.M. !$#submission submitted to the EMBL Data Library, June 1993 !$#description Plasmid-mediated formaldehyde-resistance in E. coli: !1nucleotide sequence of the resistance genes. !$#accession S57525 !'##molecule_type DNA !'##residues 1-369 ##label KUE !'##cross-references EMBL:X73835; NID:g887430; PIDN:CAA52057.1; !1PID:g887431 !'##experimental_source clinical isolate COMMENT Class III alcohol dehydrogenases are pyrazole-insensitive, !1are not very active toward ethanol and possess !1glutathione-dependent formaldehyde dehydrogenase activity. COMPLEX homodimer FUNCTION ADH !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ FUNCTION FDH !$#description catalyzes the oxidation by NAD+ of formaldehyde and !1glutathione to S-formylglutathione CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; homodimer; metalloprotein; NAD; !1oxidoreductase; zinc FEATURE !$25-360 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$189-218 #region beta-alpha-beta NAD nucleotide-binding fold\ !$40,62,169 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$92,95,98,106 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 369 #molecular-weight 39089 #checksum 7402 SEQUENCE /// ENTRY H64052 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) HI0185 - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES class III alcohol dehydrogenase CONTAINS formaldehyde dehydrogenase (glutathione) (EC 1.2.1.1) ORGANISM #formal_name Haemophilus influenzae DATE 18-Aug-1995 #sequence_revision 18-Aug-1995 #text_change 11-Jun-1999 ACCESSIONS H64052 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession H64052 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-378 ##label TIGR !'##cross-references GB:U32703; GB:L42023; NID:g1573133; !1PIDN:AAC21854.1; PID:g1573141; TIGR:HI0185 COMMENT Class III alcohol dehydrogenases are pyrazole-insensitive, !1are not very active toward ethanol and possess !1glutathione-dependent formaldehyde dehydrogenase activity. COMPLEX homodimer FUNCTION ADH !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ FUNCTION FDH !$#description catalyzes the oxidation by NAD+ of formaldehyde and !1glutathione to S-formylglutathione CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; homodimer; metalloprotein; NAD; !1oxidoreductase; zinc FEATURE !$34-369 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$198-227 #region beta-alpha-beta NAD nucleotide-binding fold\ !$49,71,178 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$101,104,107,115 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 378 #molecular-weight 40651 #checksum 2043 SEQUENCE /// ENTRY S75250 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) sll0990 - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES class III alcohol dehydrogenase; protein sll0990 CONTAINS formaldehyde dehydrogenase (glutathione) (EC 1.2.1.1) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 25-Apr-1997 #sequence_revision 25-Apr-1997 #text_change 16-Jun-2000 ACCESSIONS S75250 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75250 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-369 ##label KAN !'##cross-references EMBL:D90904; GB:AB001339; NID:g1652225; !1PIDN:BAA17164.1; PID:g1652241 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 COMMENT Class III alcohol dehydrogenases are pyrazole-insensitive, !1are not very active toward ethanol and possess !1glutathione-dependent formaldehyde dehydrogenase activity. COMPLEX homodimer FUNCTION ADH !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ FUNCTION FDH !$#description catalyzes the oxidation by NAD+ of formaldehyde and !1glutathione to S-formylglutathione CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; homodimer; metalloprotein; NAD; !1oxidoreductase; zinc FEATURE !$25-360 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$189-218 #region beta-alpha-beta NAD nucleotide-binding fold\ !$40,62,169 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$92,95,98,106 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 369 #molecular-weight 39211 #checksum 9552 SEQUENCE /// ENTRY S31140 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) SFA1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES class III alcohol dehydrogenase; protein D1473; protein YDL168w CONTAINS formaldehyde dehydrogenase (glutathione) (EC 1.2.1.1) ORGANISM #formal_name Saccharomyces cerevisiae DATE 28-May-1993 #sequence_revision 28-May-1993 #text_change 21-Jul-2000 ACCESSIONS S31140; S61045; S67720 REFERENCE S31138 !$#authors Wehner, E.P.; Rao, E.; Brendel, M. !$#journal Mol. Gen. Genet. (1993) 237:351-358 !$#title Molecular structure and genetic regulation of SFA, a gene !1responsible for resistance to formaldehyde in Saccharomyces !1cerevisiae, and characterization of its protein product. !$#cross-references MUID:93247548; PMID:8483449 !$#accession S31140 !'##molecule_type DNA !'##residues 1-386 ##label WEH !'##cross-references EMBL:X68020; NID:g577609; PIDN:CAA48161.1; !1PID:g288591 REFERENCE S61010 !$#authors Pohl, T.M. !$#submission submitted to the EMBL Data Library, November 1995 !$#accession S61045 !'##molecule_type DNA !'##residues 1-386 ##label POH !'##cross-references EMBL:Z67750; NID:g1061256; PIDN:CAA91578.1; !1PID:g1061271 REFERENCE S67708 !$#authors Pohl, T.M. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67720 !'##molecule_type DNA !'##residues 1-386 ##label POW !'##cross-references EMBL:Z74216; NID:g1431267; PIDN:CAA98742.1; !1PID:g1431268; GSPDB:GN00004; MIPS:YDL168w !'##experimental_source strain S288C COMMENT Class III alcohol dehydrogenases are pyrazole-insensitive, !1are not very active toward ethanol and possess !1glutathione-dependent formaldehyde dehydrogenase activity. GENETICS !$#gene SGD:SFA1; MIPS:YDL168w !'##cross-references SGD:S0002327; MIPS:YDL168w !$#map_position 4L FUNCTION ADH !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ FUNCTION FDH !$#description catalyzes the oxidation by NAD+ of formaldehyde and !1glutathione to S-formylglutathione CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; metalloprotein; NAD; oxidoreductase; !1zinc FEATURE !$34-373 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$199-228 #region beta-alpha-beta NAD nucleotide-binding fold\ !$49,71,179 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$101,104,107,115 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 386 #molecular-weight 41042 #checksum 583 SEQUENCE /// ENTRY JN0447 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) FDH1 - yeast (Candida maltosa) ALTERNATE_NAMES class III alcohol dehydrogenase CONTAINS formaldehyde dehydrogenase (glutathione) (EC 1.2.1.1) ORGANISM #formal_name Candida maltosa DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 11-Jun-1999 ACCESSIONS JN0447 REFERENCE JN0447 !$#authors Sasnauskas, K.; Jomantiene, R.; Januska, A.; Lebediene, E.; !1Lebedys, J.; Janulaitis, A. !$#journal Gene (1992) 122:207-211 !$#title Cloning and analysis of a Candida maltosa gene which confers !1resistance to formaldehyde in Saccharomyces cerevisiae. !$#cross-references MUID:93083986; PMID:1339376 !$#accession JN0447 !'##molecule_type DNA !'##residues 1-381 ##label SAS !'##cross-references GB:M58332; NID:g170870; PIDN:AAA34344.1; !1PID:g170871 COMMENT This protein confers resistance to formaldehyde in yeast. COMMENT Class III alcohol dehydrogenases are pyrazole-insensitive, !1are not very active toward ethanol and possess !1glutathione-dependent formaldehyde dehydrogenase activity. GENETICS !$#gene FDH1 !$#introns 8/3 FUNCTION ADH !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ FUNCTION FDH !$#description catalyzes the oxidation by NAD+ of formaldehyde and !1glutathione to S-formylglutathione CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; metalloprotein; NAD; oxidoreductase; !1zinc FEATURE !$34-371 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$198-227 #region beta-alpha-beta NAD nucleotide-binding fold\ !$49,71,178 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$101,104,107,115 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 381 #molecular-weight 40075 #checksum 8341 SEQUENCE /// ENTRY DEHUA6 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) 6 - human ALTERNATE_NAMES alcohol dehydrogenase mu chain; alcohol dehydrogenase sigma chain [misnomer]; aldehyde reductase; class II alcohol dehydrogenase ORGANISM #formal_name Homo sapiens #common_name man DATE 16-Sep-1992 #sequence_revision 08-Mar-1996 #text_change 04-Feb-2000 ACCESSIONS A41274; B41274 REFERENCE A41274 !$#authors Yasunami, M.; Chen, C.S.; Yoshida, A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:7610-7614 !$#title A human alcohol dehydrogenase gene (ADH6) encoding an !1additional class of isozyme. !$#cross-references MUID:91352038; PMID:1881901 !$#accession A41274 !'##molecule_type DNA !'##residues 1-368 ##label YAS !'##cross-references GB:M68895; NID:g178135; PIDN:AAA35508.1; !1PID:g178136 !$#accession B41274 !'##molecule_type mRNA !'##residues 1-368 ##label YAS2 !'##cross-references GB:M68895; NID:g178135; PIDN:AAA35508.1; !1PID:g178136 !'##note the authors translated the codon GAC for residue 60 as Glu GENETICS !$#gene GDB:ADH6 !'##cross-references GDB:129087; OMIM:103735 !$#map_position 4q21-4q23 !$#introns 6/3; 40/3; 88/1; 117/2; 189/3; 276/3; 322/1 FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; metalloprotein; NAD; oxidoreductase; !1zinc FEATURE !$2-368 #product alcohol dehydrogenase 6 #status predicted !8#label MAT\ !$32-366 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$195-224 #region beta-alpha-beta NAD nucleotide-binding fold\ !$47,69,175 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$99,102,105,113 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 368 #molecular-weight 39072 #checksum 1106 SEQUENCE /// ENTRY B49107 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) 2 - deer mouse ALTERNATE_NAMES alcohol dehydrogenase 2; aldehyde reductase ORGANISM #formal_name Peromyscus maniculatus #common_name deer mouse DATE 19-Mar-1997 #sequence_revision 19-Mar-1997 #text_change 11-Jun-1999 ACCESSIONS B49107 REFERENCE A49107 !$#authors Zheng, Y.W.; Bey, M.; Liu, H.; Felder, M.R. !$#journal J. Biol. Chem. (1993) 268:24933-24939 !$#title Molecular basis of the alcohol dehydrogenase-negative deer !1mouse. Evidence for deletion of the gene for class I enzyme !1and identification of a possible new enzyme class. !$#cross-references MUID:94043358; PMID:8227055 !$#accession B49107 !'##molecule_type mRNA !'##residues 1-375 ##label ZHE !'##cross-references GB:L15704; NID:g416389; PIDN:AAA40592.1; !1PID:g416390 COMMENT Although most similar to the class VI human enzyme, this !1protein may represent a new class. FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; metalloprotein; NAD; oxidoreductase; !1zinc FEATURE !$2-368 #product alcohol dehydrogenase VI #status predicted !8#label MAT\ !$32-366 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$195-224 #region beta-alpha-beta NAD nucleotide-binding fold\ !$47,69,175 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$99,102,105,113 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 375 #molecular-weight 39828 #checksum 8529 SEQUENCE /// ENTRY DEHUAP #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) 4 [validated] - human ALTERNATE_NAMES alcohol dehydrogenase pi chain; class II alcohol dehydrogenase ORGANISM #formal_name Homo sapiens #common_name man DATE 21-May-1988 #sequence_revision 28-Oct-1994 #text_change 08-Dec-2000 ACCESSIONS A27109; S18820 REFERENCE A27109 !$#authors Hoog, J.O.; von Bahr-Lindstrom, H.; Heden, L.O.; Holmquist, !1B.; Larsson, K.; Hempel, J.; Vallee, B.L.; Jornvall, H. !$#journal Biochemistry (1987) 26:1926-1932 !$#title Structure of the class II enzyme of human liver alcohol !1dehydrogenase: combined cDNA and protein sequence !1determination of the pi subunit. !$#cross-references MUID:87242382; PMID:3036213 !$#accession A27109 !'##molecule_type mRNA !'##residues 1-392 ##label HOO !'##cross-references GB:M15943; NID:g178120; PIDN:AAA51595.1; !1PID:g178121 !'##note part of the sequence was confirmed by protein sequencing !'##note the mature protein has at least the following differences from !1the sequence shown: 309-Val, 318-Lys, and 374-Ile; these !1differences may be due to a genetic polymorphism REFERENCE S18820 !$#authors von Bahr-Lindstroem, H.; Joernvall, H.; Hoeoeg, J.O. !$#journal Gene (1991) 103:269-274 !$#title Cloning and characterization of the human ADH4 gene. !$#cross-references MUID:91365257; PMID:1889753 !$#accession S18820 !'##molecule_type DNA !'##residues 1-380 ##label BAH !'##cross-references EMBL:X56418 COMMENT Class II alcohol dehydrogenases are moderately !1pyrazole-sensitive and have a moderate activity for ethanol. GENETICS !$#gene GDB:ADH4 !'##cross-references GDB:119653; OMIM:103740 !$#map_position 4q22-4q22 !$#introns 6/3; 40/3; 88/1; 117/2; 194/3; 281/3; 327/1; 373/2 COMPLEX homodimer; does not form heterodimers with other forms FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation !$#note expressed predominately in liver and stomach CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS acetylated amino end; alcohol metabolism; homodimer; !1metalloprotein; NAD; oxidoreductase; zinc FEATURE !$2-380 #product alcohol dehydrogenase 4 #status experimental !8#label MAT\ !$32-371 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$200-229 #region beta-alpha-beta NAD nucleotide-binding fold\ !$2 #modified_site blocked amino end (Gly) (in mature !8form) (probably acetylated) #status experimental\ !$47,69,180 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$99,102,105,113 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 392 #molecular-weight 41641 #checksum 1623 SEQUENCE /// ENTRY S66286 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) 2 - rat ALTERNATE_NAMES class II alcohol dehydrogenase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 15-Feb-1997 #sequence_revision 13-Mar-1997 #text_change 11-Jun-1999 ACCESSIONS S66286 REFERENCE S66286 !$#authors Hoeoeg, J.O. !$#journal FEBS Lett. (1995) 368:445-448 !$#title Cloning and characterization of a novel rat alcohol !1dehydrogenase of class II type. !$#cross-references MUID:95361920; PMID:7635195 !$#accession S66286 !'##status preliminary !'##molecule_type mRNA !'##residues 1-377 ##label HOE !'##cross-references EMBL:X90710; NID:g951039; PIDN:CAA62241.1; !1PID:g951040 !'##experimental_source strain Sprague-Dawley !'##note the authors did not translate the codon for residue 1 COMMENT Class II alcohol dehydrogenases are moderately !1pyrazole-sensitive and have a moderate activity for ethanol. GENETICS !$#gene adh2 COMPLEX homodimer FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS acetylated amino end; alcohol metabolism; homodimer; !1metalloprotein; NAD; oxidoreductase; zinc FEATURE !$2-377 #product alcohol dehydrogenase pi #status predicted !8#label MAT\ !$32-368 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$199-228 #region beta-alpha-beta NAD nucleotide-binding fold\ !$2 #modified_site acetylated amino end (Gly) (in mature !8form) #status predicted\ !$47,68,179 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$98,101,104,112 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 377 #molecular-weight 40276 #checksum 7294 SEQUENCE /// ENTRY S04571 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) 1 - maize ORGANISM #formal_name Zea mays #common_name maize DATE 07-Sep-1990 #sequence_revision 07-Sep-1990 #text_change 11-Jun-1999 ACCESSIONS S04571; S04572; A05102; A00342 REFERENCE S04571 !$#authors Dennis, E.S.; Gerlach, W.L.; Pryor, A.J.; Bennetzen, J.L.; !1Inglis, A.; Llewellyn, D.; Sachs, M.M.; Ferl, R.J.; Peacock, !1W.J. !$#journal Nucleic Acids Res. (1984) 12:3983-4000 !$#title Molecular analysis of the alcohol dehydrogenase (Adh1) gene !1of maize. !$#cross-references MUID:84221411; PMID:6328449 !$#accession S04571 !'##molecule_type DNA !'##residues 1-379 ##label DEN !'##cross-references EMBL:X04049; NID:g22123; PIDN:CAA27681.1; !1PID:g22124 !'##note part of this sequence was confirmed by protein sequencing !'##note the sequence of the S (slow) allele is shown. 127-Ala and !1363-Asp were found in F (fast) allele !'##note the sequence from Fig. 2 is inconsistent with that from Fig. 5 !1in having 212-Gly; the sequence from Fig. 2 has been revised !1in reference S02097 REFERENCE S02097 !$#authors Dennis, E.S.; Sachs, M.M.; Gerlach, W.L.; Finnegan, E.J.; !1Peacock, W.J. !$#journal Nucleic Acids Res. (1985) 13:727-743 !$#title Molecular analysis of the alcohol dehydrogenase 2 (Adh2) !1gene of maize. !$#cross-references MUID:85215511; PMID:2987807 !$#contents annotation REFERENCE S04572 !$#authors Sachs, M.M.; Dennis, E.S.; Gerlach, W.L.; Peacock, W.J. !$#journal Genetics (1986) 113:449-467 !$#title Two alleles of maize alcohol dehydrogenase 1 have 3' !1structural and poly(A) addition polymorphisms. !$#accession S04572 !'##status translation not shown !'##molecule_type DNA !'##residues 1-126,'A',128-362,'D',364-379 ##label SAC !'##cross-references EMBL:X04049 !'##note the F allele was sequenced REFERENCE A05102 !$#authors Branden, C.I.; Eklund, H.; Cambillau, C.; Pryor, A.J. !$#journal EMBO J. (1984) 3:1307-1310 !$#title Correlation of exons with structural domains in alcohol !1dehydrogenase. !$#cross-references MUID:84261418; PMID:6378620 !$#accession A05102 !'##molecule_type protein !'##residues 1-126,'A',128-178,'Y',180-211,'G',213-362,'D',364-379 !1##label BRA REFERENCE A00342 !$#authors Gerlach, W.L.; Pryor, A.J.; Dennis, E.S.; Ferl, R.J.; Sachs, !1M.M.; Peacock, W.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:2981-2985 !$#title cDNA cloning and induction of the alcohol dehydrogenase gene !1(Adh1) of maize. !$#accession A00342 !'##molecule_type mRNA !'##residues 'G',213-362,'D',364-379 ##label GER !'##cross-references GB:J01239; NID:g168405 !'##note the maize alcohol dehydrogenase is a dimer; the two polypeptide !1chains are encoded by two unlinked genes, Adh1 on chromosome !11 and Adh2 on chromosome 4 GENETICS !$#gene Adh1 !$#map_position 1 !$#introns 12/1; 57/3; 73/2; 182/1; 209/3; 235/1; 255/3; 287/3; 341/3 COMPLEX dimer FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; dimer; metalloprotein; NAD; !1oxidoreductase; zinc FEATURE !$32-368 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$47,69,177 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$99,102,105,113 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 379 #molecular-weight 40916 #checksum 9656 SEQUENCE /// ENTRY DEILSP #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) 1 - pearl millet ORGANISM #formal_name Pennisetum americanum #common_name pearl millet DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 11-Jun-1999 ACCESSIONS S14905; S06693 REFERENCE S14905 !$#authors Ha, D.B.D.; Buffard, D.; Berger, F.; Breda, C.; Esnault, R. !$#journal Plant Mol. Biol. (1990) 14:453-455 !$#title Nucleotide sequence encoding a slow allele of Adh1 in pearl !1millet. !$#cross-references MUID:91346634; PMID:2102826 !$#accession S14905 !'##molecule_type mRNA !'##residues 1-379 ##label HAD !'##cross-references EMBL:X16547; NID:g20408; PIDN:CAA34547.1; !1PID:g20409 !'##experimental_source var. Massue !'##note sequence is of slow allele GENETICS !$#gene Adh1 COMPLEX dimer FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; dimer; metalloprotein; NAD; !1oxidoreductase; zinc FEATURE !$32-368 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$197-226 #region beta-alpha-beta NAD nucleotide-binding fold\ !$47,69,177 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$99,102,105,113 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 379 #molecular-weight 40916 #checksum 9483 SEQUENCE /// ENTRY S01893 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) 1 - barley ORGANISM #formal_name Hordeum vulgare #common_name barley DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 11-Jun-1999 ACCESSIONS S01893 REFERENCE S01893 !$#authors Good, A.G.; Pelcher, L.E.; Crosby, W.L. !$#journal Nucleic Acids Res. (1988) 16:7182 !$#title Nucleotide sequence of a complete barley alcohol !1dehydrogenase 1 cDNA. !$#cross-references MUID:88303342; PMID:3405765 !$#accession S01893 !'##molecule_type mRNA !'##residues 1-379 ##label GOO !'##cross-references EMBL:X07774; NID:g18874; PIDN:CAA30600.1; !1PID:g18875 COMPLEX dimer FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; dimer; metalloprotein; NAD; !1oxidoreductase; zinc FEATURE !$32-368 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$47,69,177 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$99,102,105,113 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 379 #molecular-weight 40884 #checksum 9953 SEQUENCE /// ENTRY JQ0474 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) 1 - rice ORGANISM #formal_name Oryza sativa #common_name rice DATE 03-Feb-1994 #sequence_revision 03-Feb-1994 #text_change 11-Jun-1999 ACCESSIONS JQ0474 REFERENCE JQ0474 !$#authors Xie, Y.; Wu, R. !$#journal Plant Mol. Biol. (1989) 13:53-68 !$#title Rice alcohol dehydrogenase genes: anaerobic induction, organ !1specific expression and characterization of cDNA clones. !$#cross-references MUID:93357433; PMID:2562760 !$#accession JQ0474 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-376 ##label XIE !'##cross-references GB:X16296; NID:g20164; PIDN:CAA34363.1; PID:g20165 !'##experimental_source seedling, strain IR26 GENETICS !$#gene Adh1 COMPLEX dimer FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; dimer; metalloprotein; NAD; !1oxidoreductase; zinc FEATURE !$30-365 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$45,67,175 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$97,100,103,111 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 376 #molecular-weight 40852 #checksum 9462 SEQUENCE /// ENTRY S04040 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) 3 - barley ORGANISM #formal_name Hordeum vulgare #common_name barley DATE 28-Feb-1990 #sequence_revision 28-Feb-1990 #text_change 11-Jun-1999 ACCESSIONS S04040 REFERENCE S04038 !$#authors Trick, M.; Dennis, E.S.; Edwards, K.J.R.; Peacock, W.J. !$#journal Plant Mol. Biol. (1988) 11:147-160 !$#title Molecular analysis of the alcohol dehydrogenase gene family !1of barley. !$#accession S04040 !'##molecule_type DNA !'##residues 1-379 ##label TRI !'##cross-references EMBL:X12734; NID:g18885; PIDN:CAA31231.1; !1PID:g18886 GENETICS !$#gene Adh3 !$#introns 12/1; 57/3; 73/2; 182/1; 209/3; 235/1; 255/3; 287/3 COMPLEX dimer FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; dimer; metalloprotein; NAD; !1oxidoreductase; zinc FEATURE !$32-368 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$47,69,177 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$99,102,105,113 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 379 #molecular-weight 41011 #checksum 30 SEQUENCE /// ENTRY A61024 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) - wheat (cv. Millewa) ORGANISM #formal_name Triticum aestivum #common_name common wheat DATE 12-May-1994 #sequence_revision 12-May-1994 #text_change 07-May-1999 ACCESSIONS A61024 REFERENCE A61024 !$#authors Mitchell, L.E.; Dennis, E.S.; Peacock, W.J. !$#journal Genome (1989) 32:349-358 !$#title Molecular analysis of an alcohol dehydrogenase (Adh) gene !1from chromosome 1 of wheat. !$#cross-references MUID:89306583; PMID:2545522 !$#accession A61024 !'##status translation not shown !'##molecule_type DNA !'##residues 1-379 ##label MIT COMMENT Southern analysis shows several copies of this gene on !1chromosome 1. COMMENT This gene is transcribed under anaerobic conditions such as !1prolonged flooding of seedlings. GENETICS !$#gene Adh !$#map_position 1A COMPLEX dimer FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; dimer; metalloprotein; NAD; !1oxidoreductase; zinc FEATURE !$32-368 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$47,69,177 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$99,102,105,113 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 379 #molecular-weight 41119 #checksum 8758 SEQUENCE /// ENTRY A23084 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) 2 - maize ORGANISM #formal_name Zea mays #common_name maize DATE 15-Dec-1988 #sequence_revision 15-Dec-1988 #text_change 11-Jun-1999 ACCESSIONS A23084 REFERENCE S02097 !$#authors Dennis, E.S.; Sachs, M.M.; Gerlach, W.L.; Finnegan, E.J.; !1Peacock, W.J. !$#journal Nucleic Acids Res. (1985) 13:727-743 !$#title Molecular analysis of the alcohol dehydrogenase 2 (Adh2) !1gene of maize. !$#cross-references MUID:85215511; PMID:2987807 !$#accession A23084 !'##molecule_type mRNA !'##residues 1-379 ##label DEN !'##cross-references GB:X01965; NID:g22136; PIDN:CAA26001.1; PID:g22137 !'##note the authors translated the codon AGC for residue 370 as Gly GENETICS !$#gene Adh2 COMPLEX dimer FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; dimer; metalloprotein; NAD; !1oxidoreductase; zinc FEATURE !$32-368 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$47,69,177 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$99,102,105,113 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 379 #molecular-weight 41054 #checksum 9915 SEQUENCE /// ENTRY S04039 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) 2 - barley ORGANISM #formal_name Hordeum vulgare #common_name barley DATE 28-Feb-1990 #sequence_revision 28-Feb-1990 #text_change 11-Jun-1999 ACCESSIONS S04039 REFERENCE S04038 !$#authors Trick, M.; Dennis, E.S.; Edwards, K.J.R.; Peacock, W.J. !$#journal Plant Mol. Biol. (1988) 11:147-160 !$#title Molecular analysis of the alcohol dehydrogenase gene family !1of barley. !$#accession S04039 !'##molecule_type DNA !'##residues 1-373 ##label TRI !'##cross-references EMBL:X12733; NID:g18883; PIDN:CAA31230.1; !1PID:g18884 GENETICS !$#gene Adh2 !$#introns 12/1; 57/3; 73/2; 182/1; 209/3; 235/1; 255/3; 287/3 COMPLEX dimer FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; dimer; metalloprotein; NAD; !1oxidoreductase; zinc FEATURE !$32-362 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$47,69,177 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$99,102,105,113 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 373 #molecular-weight 40511 #checksum 2278 SEQUENCE /// ENTRY DERZA2 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) 2 - rice ORGANISM #formal_name Oryza sativa #common_name rice DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 11-Jun-1999 ACCESSIONS JH0111; JQ0475 REFERENCE JH0111 !$#authors Xie, Y.; Wu, R. !$#journal Gene (1990) 87:185-191 !$#title Molecular analysis of an alcohol dehydrogenase-encoding !1genomic clone (adh2) from rice. !$#cross-references MUID:90236308; PMID:2332167 !$#accession JH0111 !'##molecule_type DNA !'##residues 1-375 ##label XIE !'##cross-references GB:M36469; NID:g169756 !'##note conceptual translation of the sequence in GenBank release 103 !1replaces residues 365-375 with 'RVSAAS' REFERENCE JQ0474 !$#authors Xie, Y.; Wu, R. !$#journal Plant Mol. Biol. (1989) 13:53-68 !$#title Rice alcohol dehydrogenase genes: anaerobic induction, organ !1specific expression and characterization of cDNA clones. !$#cross-references MUID:93357433; PMID:2562760 !$#accession JQ0475 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-375 ##label XI2 !'##cross-references GB:X16297; NID:g20168; PIDN:CAA34364.1; PID:g20169 !'##experimental_source seed GENETICS !$#gene Adh2 !$#introns 11/1; 56/3; 72/2; 181/2; 208/3; 234/1; 253/3; 285/3; 338/3 COMPLEX dimer FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; dimer; metalloprotein; NAD; !1oxidoreductase; zinc FEATURE !$31-364 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$196-225 #region beta-alpha-beta NAD nucleotide-binding fold\ !$46,68,176 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$98,101,104,112 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 375 #molecular-weight 40839 #checksum 9632 SEQUENCE /// ENTRY DEPOA1 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) - potato ORGANISM #formal_name Solanum tuberosum #common_name potato DATE 31-Mar-1992 #sequence_revision 01-May-1998 #text_change 21-Jan-2000 ACCESSIONS S11853; S12767; S12766 REFERENCE S11853 !$#authors Matton, D.P.; Constabel, P.; Brisson, N. !$#journal Plant Mol. Biol. (1990) 14:775-783 !$#title Alcohol dehydrogenase gene expression in potato following !1elicitor and stress treatment. !$#cross-references MUID:91346668; PMID:2102855 !$#accession S11853 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-380 ##label MAT !'##cross-references GB:X53242; GB:S50972; NID:g297177; PIDN:CAA37333.1; !1PID:g297178 !'##experimental_source cv. Kennebec REFERENCE S12766 !$#authors Matton, D.P.; Brisson, N. !$#journal Nucleic Acids Res. (1990) 18:3070 !$#title Nucleotide sequence of two potato alcohol dehydrogenase !1cDNAs. !$#cross-references MUID:90272434; PMID:2349116 !$#accession S12767 !'##molecule_type mRNA !'##residues 1-4,'T',6-311,'F',313-380 ##label MA2 !'##cross-references EMBL:M25153; NID:g169468; PIDN:AAA33807.1; !1PID:g169469 !'##experimental_source cv. Kennebec; clone ADH-2 !$#accession S12766 !'##molecule_type mRNA !'##residues 1-311,'F',313-380 ##label MA3 !'##cross-references EMBL:M25152; NID:g169470; PIDN:AAA33808.1; !1PID:g169471 !'##experimental_source cv. Kennebec; clone ADH-3 FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; metalloprotein; NAD; oxidoreductase; !1zinc FEATURE !$33-369 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$198-227 #region beta-alpha-beta NAD nucleotide-binding fold\ !$48,70,178 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$100,103,106,114 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 380 #molecular-weight 41108 #checksum 3946 SEQUENCE /// ENTRY S51826 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) 2 - tomato ALTERNATE_NAMES aldehyde reductase ORGANISM #formal_name Lycopersicon esculentum #common_name tomato DATE 14-Jul-1995 #sequence_revision 21-Jul-1995 #text_change 11-Jun-1999 ACCESSIONS S51826; JT0618; S20613; S16038 REFERENCE S51826 !$#authors Longhurst, T.; Lee, E.; Hinde, R.; Brady, C.; Speirs, J. !$#journal Plant Mol. Biol. (1994) 26:1073-1084 !$#title Structure of the tomato Adh2 gene and Adh2 pseudogenes, and !1a study of Adh2 gene expression in fruit. !$#cross-references MUID:95111092; PMID:7811967 !$#accession S51826 !'##status preliminary !'##molecule_type DNA !'##residues 1-380 ##label LON !'##cross-references EMBL:X77233; NID:g623248; PIDN:CAA54450.1; !1PID:g623249 REFERENCE JT0618 !$#authors Genez, A.L.; Staraci, L.C.; Alexander, D.C.; Rejda, J.M.; !1Williamson, V.M.; Chase Jr., T.; Williams, B.G. !$#journal Gene (1993) 123:157-164 !$#title Isolation of a tomato alcohol dehydrogenase 2-encoding cDNA !1using phage-promoted antibody screening of a plasmid cDNA !1library. !$#cross-references MUID:93154579; PMID:8428654 !$#accession JT0618 !'##molecule_type mRNA !'##residues 229-380 ##label GEN !'##cross-references GB:M86724 !'##note the authors translated the codon CGT for residue 373 as Lys REFERENCE S20613 !$#authors van der Straeten, D.; Pousada, R.A.R.; Gielen, J.; van !1Montagu, M. !$#journal FEBS Lett. (1991) 295:39-42 !$#title Tomato alcohol dehydrogenase. Expression during fruit !1ripening and under hypoxic conditions. !$#cross-references MUID:92111754; PMID:1765164 !$#accession S20613 !'##molecule_type mRNA !'##residues 'R',252-380 ##label EMB !'##cross-references EMBL:X60600; NID:g19171; PIDN:CAA43055.1; !1PID:g19172 !'##experimental_source cv. Supersonic GENETICS !$#gene Adh2 !$#map_position 6 !$#introns 13/1; 58/3; 74/2; 183/1; 210/3; 236/1; 256/3; 289/1 FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; metalloprotein; NAD; oxidoreductase; !1zinc FEATURE !$33-369 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$198-227 #region beta-alpha-beta NAD nucleotide-binding fold\ !$48,70,178 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$100,103,106,114 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 380 #molecular-weight 41040 #checksum 2795 SEQUENCE /// ENTRY S52973 #type fragment TITLE alcohol dehydrogenase (EC 1.1.1.1) 2 - garden petunia (fragment) ORGANISM #formal_name Petunia x hybrida #common_name garden petunia DATE 15-Jul-1995 #sequence_revision 18-Jul-1997 #text_change 11-Jun-1999 ACCESSIONS S52973 REFERENCE S52973 !$#authors Gregerson, R.G.; Cameron, L.; McLean, M.; Dennis, P.; !1Strommer, J. !$#journal Genetics (1993) 133:999-1007 !$#title Structure, expression, chromosomal location and product of !1the gene encoding ADH2 in Petunia. !$#cross-references MUID:93216096; PMID:8096485 !$#accession S52973 !'##status preliminary !'##molecule_type DNA !'##residues 1-281 ##label GRE !'##cross-references GB:U25536; EMBL:S58282; NID:g829591; !1PIDN:AAB02990.1; PID:g829592 !'##experimental_source cultivar V30 GENETICS !$#gene Adh2 !$#introns 13/1; 58/3; 74/2; 182/3; 209/3; 234/3; 255/3 FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; metalloprotein; NAD; oxidoreductase; !1zinc FEATURE !$33-281 #domain long-chain alcohol dehydrogenase homology !8(fragment) #label LADH\ !$197-226 #region beta-alpha-beta NAD nucleotide-binding fold\ !$48,70,178 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$100,103,106,114 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 281 #checksum 5870 SEQUENCE /// ENTRY JC4320 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) - garden lettuce ALTERNATE_NAMES gibberellin responsive protein LRG5 ORGANISM #formal_name Lactuca sativa #common_name garden lettuce DATE 29-Nov-1995 #sequence_revision 08-Feb-1996 #text_change 16-Jun-2000 ACCESSIONS JC4320 REFERENCE JC4320 !$#authors Toyomasu, T.; Yamauchi, T.; Yamane, H.; Murofushi, N.; !1Inoue, Y. !$#journal Biosci. Biotechnol. Biochem. (1995) 59:1846-1849 !$#title cDNA cloning and characterization of gibberellin-responsive !1genes in photoblastic lettuce seeds. !$#cross-references MUID:96068927; PMID:8534973 !$#accession JC4320 !'##molecule_type mRNA !'##residues 1-380 ##label TOY !'##cross-references DDBJ:D44449; NID:g1066003; PIDN:BAA07911.1; !1PID:g1401037 !'##experimental_source seeds of cv. Grand Rapids FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; metalloprotein; NAD; oxidoreductase; !1seed; zinc FEATURE !$33-369 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$198-227 #region beta-alpha-beta NAD nucleotide-binding fold\ !$48,70,178 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$100,103,106,114 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 380 #molecular-weight 41335 #checksum 3027 SEQUENCE /// ENTRY A58722 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) - garden strawberry ORGANISM #formal_name Fragaria x ananassa #common_name garden strawberry DATE 01-May-1998 #sequence_revision 01-May-1998 #text_change 11-Jun-1999 ACCESSIONS A58722; S10019 REFERENCE A58722 !$#authors Wolyn, D. !$#submission submitted to GenBank, August 1990 !$#accession A58722 !'##molecule_type DNA !'##residues 1-380 ##label WOL !'##cross-references EMBL:X15588; NID:g18452; PIDN:CAA33613.1; !1PID:g18453 REFERENCE S10019 !$#authors Wolyn, D.J.; Jelenkovic, G. !$#journal Plant Mol. Biol. (1990) 14:855-857 !$#title Nucleotide sequence of an alcohol dehydrogenase gene in !1octoploid strawberry (Fragaria x Ananassa Duch.). !$#cross-references MUID:91346676; PMID:2102862 !$#accession S10019 !'##molecule_type DNA !'##residues 1-33,'HP',36-380 ##label WO2 !'##cross-references EMBL:X15588; NID:g18452 !'##note the authors translated the codon CAC for residue 34 as Gln, CCT !1for residue 35 as Ala, AAG for residue 58 as Leu, GAT for !1residue 85 as O, GGC for residue 196 as Ser, TCA for residue !1197 as Gly, ATG for residue 279 as Asn, and AAC for residue !1325 as Val GENETICS !$#gene Adh !$#introns 13/1; 58/3; 74/2; 183/1; 210/3; 236/1; 256/3; 288/3; 342/3 FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; metalloprotein; NAD; oxidoreductase; !1zinc FEATURE !$33-369 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$198-227 #region beta-alpha-beta NAD nucleotide-binding fold\ !$48,70,178 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$100,103,106,114 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 380 #molecular-weight 41459 #checksum 6937 SEQUENCE /// ENTRY S57650 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) - apple tree ORGANISM #formal_name Malus domestica #common_name apple tree DATE 19-Oct-1995 #sequence_revision 03-Nov-1995 #text_change 11-Jun-1999 ACCESSIONS S57650 REFERENCE S57650 !$#authors Reid, S.J.; Janssen, B.; Watkins, C.B.; Ross, G.S. !$#submission submitted to the EMBL Data Library, May 1995 !$#description Apple fruit alcohol dehydrogenase gene expression during !1postharvest ripening and storage. !$#accession S57650 !'##status preliminary !'##molecule_type mRNA !'##residues 1-380 ##label REI !'##cross-references EMBL:Z48234; NID:g886884; PIDN:CAA88271.1; !1PID:g886885 FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; metalloprotein; NAD; oxidoreductase; !1zinc FEATURE !$33-369 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$198-227 #region beta-alpha-beta NAD nucleotide-binding fold\ !$48,70,178 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$100,103,106,114 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 380 #molecular-weight 41408 #checksum 4776 SEQUENCE /// ENTRY DEJYAW #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) 1 - white clover ORGANISM #formal_name Trifolium repens #common_name white clover DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 11-Jun-1999 ACCESSIONS S14680; S06200 REFERENCE S14680 !$#authors Ellison, N.W.; Yu, P.L.; White, D.W.R. !$#journal Nucleic Acids Res. (1990) 18:4913 !$#title Nucleotide sequence of a white clover alcohol dehydrogenase !1cDNA. !$#cross-references MUID:90370476; PMID:2395651 !$#accession S14680 !'##molecule_type mRNA !'##residues 1-380 ##label ELL !'##cross-references EMBL:X14826; NID:g21950; PIDN:CAA32934.1; !1PID:g21951 !'##experimental_source cv. Huia GENETICS !$#gene Adh1 FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; metalloprotein; NAD; oxidoreductase; !1zinc FEATURE !$33-369 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$198-227 #region beta-alpha-beta NAD nucleotide-binding fold\ !$48,70,178 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$100,103,106,114 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 380 #molecular-weight 41172 #checksum 2907 SEQUENCE /// ENTRY S00912 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) 1 - garden pea ORGANISM #formal_name Pisum sativum #common_name garden pea DATE 07-Jun-1990 #sequence_revision 07-Jun-1990 #text_change 11-Jun-1999 ACCESSIONS S00912 REFERENCE S00912 !$#authors Llewellyn, D.J.; Finnegan, E.J.; Ellis, J.G.; Dennis, E.S.; !1Peacock, W.J. !$#journal J. Mol. Biol. (1987) 195:115-123 !$#title Structure and expression of an alcohol dehydrogenase 1 gene !1from Pisum sativum (cv. "Greenfeast"). !$#cross-references MUID:88011221; PMID:3309331 !$#accession S00912 !'##status translation not shown !'##molecule_type DNA !'##residues 1-380 ##label LLE !'##cross-references EMBL:X06281; NID:g20638; PIDN:CAA29609.1; !1PID:g20639 GENETICS !$#gene Adh1 !$#introns 13/1; 58/3; 74/2; 183/1; 210/3; 236/1; 256/3; 288/3; 342/3 FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; metalloprotein; NAD; oxidoreductase; !1zinc FEATURE !$33-369 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$198-227 #region beta-alpha-beta NAD nucleotide-binding fold\ !$48,70,178 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$100,103,106,114 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 380 #molecular-weight 41155 #checksum 2627 SEQUENCE /// ENTRY S53307 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) 1 - Phaseolus acutifolius ORGANISM #formal_name Phaseolus acutifolius DATE 19-Mar-1997 #sequence_revision 06-Jun-1997 #text_change 11-Jun-1999 ACCESSIONS S53307; S53308 REFERENCE S53307 !$#authors Garvin, D.F.; Weeden, N.F.; Doyle, J.J. !$#journal Plant Mol. Biol. (1994) 26:643-655 !$#title The reduced stability of a plant alcohol dehydrogenase is !1due to the substitution of serine for a highly conserved !1phenylalanine residue. !$#cross-references MUID:95036045; PMID:7948919 !$#accession S53307 !'##molecule_type mRNA !'##residues 1-380 ##label GAR !'##cross-references EMBL:Z23170; NID:g452768; PIDN:CAA80691.1; !1PID:g452769 !'##note sequence of F isotype !$#accession S53308 !'##molecule_type mRNA !'##residues 1-143,'S',145-380 ##label GA2 !'##cross-references EMBL:Z23171; NID:g452766; PIDN:CAA80692.1; !1PID:g452767 !'##note sequence of CN isotype FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; metalloprotein; NAD; oxidoreductase; !1zinc FEATURE !$33-369 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$198-227 #region beta-alpha-beta NAD nucleotide-binding fold\ !$48,70,178 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$100,103,106,114 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 380 #molecular-weight 40969 #checksum 3970 SEQUENCE /// ENTRY DEPJA1 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) 1 - garden petunia ORGANISM #formal_name Petunia x hybrida #common_name garden petunia DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 11-Jun-1999 ACCESSIONS S16596 REFERENCE S16596 !$#authors Gregerson, R.; McLean, M.; Beld, M.; Gerats, A.G.M.; !1Strommer, J. !$#journal Plant Mol. Biol. (1991) 17:37-48 !$#title Structure, expression, chromosomal location and product of !1the gene encoding ADH1 in Petunia. !$#cross-references MUID:91329736; PMID:1678286 !$#accession S16596 !'##molecule_type DNA !'##residues 1-382 ##label GRE !'##cross-references EMBL:X54106; NID:g20505; PIDN:CAA38039.1; !1PID:g20506 !'##experimental_source cv. V30 GENETICS !$#gene Adh1 !$#map_position 4 !$#introns 13/3; 59/3; 75/3; 183/3; 211/3; 236/3; 258/3; 290/3; 344/3 COMPLEX dimer FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; dimer; metalloprotein; NAD; !1oxidoreductase; zinc FEATURE !$34-371 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$199-228 #region beta-alpha-beta NAD nucleotide-binding fold\ !$49,71,179 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$101,104,107,115 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 382 #molecular-weight 41573 #checksum 4117 SEQUENCE /// ENTRY S57819 #type fragment TITLE alcohol dehydrogenase (EC 1.1.1.1) - common tobacco (fragment) ORGANISM #formal_name Nicotiana tabacum #common_name common tobacco DATE 28-Oct-1995 #sequence_revision 03-Nov-1995 #text_change 11-Jun-1999 ACCESSIONS S57819 REFERENCE S57819 !$#authors Bucher, M.; Brander, K.A.; Sbicego, S.; Mandel, T.; !1Kuhlemeier, C. !$#journal Plant Mol. Biol. (1995) 28:739-750 !$#title Aerobic fermentation in tobacco pollen. !$#cross-references MUID:95375236; PMID:7647304 !$#accession S57819 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type mRNA !'##residues 1-379 ##label BUC !'##cross-references EMBL:X81853; NID:g551256; PIDN:CAA57446.1; !1PID:g551257 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1September 1994 FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; metalloprotein; NAD; oxidoreductase; !1zinc FEATURE !$32-368 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$197-226 #region beta-alpha-beta NAD nucleotide-binding fold\ !$47,69,177 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$99,102,105,113 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 379 #checksum 4147 SEQUENCE /// ENTRY S71570 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) 2a - upland cotton ORGANISM #formal_name Gossypium hirsutum #common_name upland cotton DATE 04-Feb-1998 #sequence_revision 20-Feb-1998 #text_change 11-Jun-1999 ACCESSIONS S71570 REFERENCE S71569 !$#authors Millar, A.A.; Dennis, E.S. !$#journal Plant Mol. Biol. (1996) 31:897-904 !$#title The alcohol dehydrogenase genes of cotton. !$#cross-references MUID:96400043; PMID:8806419 !$#accession S71570 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type mRNA !'##residues 1-379 ##label MIL !'##cross-references EMBL:U49061; NID:g1220195; PIDN:AAA91811.1; !1PID:g1220196 !'##experimental_source strain Blue Tag Siokra !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1February 1996 FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; metalloprotein; NAD; oxidoreductase; !1zinc FEATURE !$32-368 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$197-226 #region beta-alpha-beta NAD nucleotide-binding fold\ !$47,69,177 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$99,102,105,113 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 379 #molecular-weight 41074 #checksum 2746 SEQUENCE /// ENTRY S71571 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) 2b - upland cotton ORGANISM #formal_name Gossypium hirsutum #common_name upland cotton DATE 04-Feb-1998 #sequence_revision 20-Feb-1998 #text_change 11-Jun-1999 ACCESSIONS S71571; S71572 REFERENCE S71569 !$#authors Millar, A.A.; Dennis, E.S. !$#journal Plant Mol. Biol. (1996) 31:897-904 !$#title The alcohol dehydrogenase genes of cotton. !$#cross-references MUID:96400043; PMID:8806419 !$#accession S71571 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-379 ##label MIL !'##cross-references EMBL:U49452; NID:g1263290; PIDN:AAA97409.1; !1PID:g1263291 !'##experimental_source strain Blue Tag Siokra !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1February 1996 !$#accession S71572 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type mRNA !'##residues 222-379 ##label MIF !'##cross-references EMBL:U53704; NID:g1297364; PIDN:AAA98987.1; !1PID:g1297365 !'##experimental_source strain Blue Tag Siokra !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1996 GENETICS !$#introns 12/1; 57/3; 73/2; 182/1; 209/3; 235/1; 255/3; 287/3; 341/3 FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; metalloprotein; NAD; oxidoreductase; !1zinc FEATURE !$32-368 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$197-226 #region beta-alpha-beta NAD nucleotide-binding fold\ !$47,69,177 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$99,102,105,113 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 379 #molecular-weight 41090 #checksum 2015 SEQUENCE /// ENTRY DEMUAM #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 11-Jun-1999 ACCESSIONS A23815; S42883 REFERENCE A23815 !$#authors Chang, C.; Meyerowitz, E.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:1408-1412 !$#title Molecular cloning and DNA sequence of the Arabidopsis !1thaliana alcohol dehydrogenase gene. !$#cross-references MUID:86149313; PMID:2937058 !$#accession A23815 !'##molecule_type DNA !'##residues 1-379 ##label CHA !'##cross-references GB:M12196; NID:g166583; PIDN:AAA32728.1; !1PID:g166584 REFERENCE S42883 !$#authors Hanfstingl, U.; Berry, A.; Kellogg, E.A.; Costa III, J.T.; !1Rudiger, W. !$#submission submitted to the EMBL Data Library, February 1994 !$#description Haplotypic divergence coupled with lack of diversity at the !1A. Thaliana Adh Locus: roles for both balancing and !1directional selection. !$#accession S42883 !'##molecule_type DNA !'##residues 1-100,'E',102-105,'H',107-341,'NIN' ##label HAN !'##cross-references EMBL:X77943 !'##experimental_source cv. Columbia COMMENT The enzyme can be induced by 2,4-dichlorophenoxyacetic acid !1in Arabidopsis as well as in maize. Unlike most plants, !1Arabidopsis contains only one gene locus for Adh. GENETICS !$#gene Adh !$#introns 12/1; 57/3; 73/2; 235/1; 287/3; 341/3 COMPLEX homodimer FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; metalloprotein; NAD; oxidoreductase; !1zinc FEATURE !$32-368 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$197-226 #region beta-alpha-beta NAD nucleotide-binding fold\ !$47,69,177 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$99,102,105,113 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 379 #molecular-weight 41155 #checksum 41 SEQUENCE /// ENTRY A46704 #type complete TITLE aryl-alcohol dehydrogenase (EC 1.1.1.90) - Pseudomonas putida plasmid pWW0 ORGANISM #formal_name Pseudomonas putida DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A46704 REFERENCE A46704 !$#authors Shaw, J.P.; Rekik, M.; Schwager, F.; Harayama, S. !$#journal J. Biol. Chem. (1993) 268:10842-10850 !$#title Kinetic studies on benzyl alcohol dehydrogenase encoded by !1TOL plasmid pWW0. A member of the zinc-containing long chain !1alcohol dehydrogenase family. !$#cross-references MUID:93266524; PMID:8496150 !$#accession A46704 !'##status preliminary !'##molecule_type DNA !'##residues 1-366 ##label SHA !'##cross-references GB:M94184 GENETICS !$#genome plasmid CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; oxidoreductase FEATURE !$25-356 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$189-218 #region beta-alpha-beta NAD nucleotide-binding fold SUMMARY #length 366 #molecular-weight 38510 #checksum 3766 SEQUENCE /// ENTRY B42971 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) - Pseudomonas sp. ORGANISM #formal_name Pseudomonas sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B42971; S27651 REFERENCE A42971 !$#authors Peterson, J.A.; Lu, J.Y.; Geisselsoder, J.; Graham-Lorence, !1S.; Carmona, C.; Witney, F.; Lorence, M.C. !$#journal J. Biol. Chem. (1992) 267:14193-14203 !$#title Cytochrome P-450terp. Isolation and purification of the !1protein and cloning and sequencing of its operon. !$#cross-references MUID:92332528; PMID:1629218 !$#accession B42971 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA; protein !'##residues 1-319 ##label PET !'##cross-references EMBL:M91440; NID:g151584; PIDN:AAA25994.1; !1PID:g151585 !'##note sequence extracted from NCBI backbone (NCBIP:108470) GENETICS !$#gene terpD CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; metalloprotein; NAD; oxidoreductase; !1zinc FEATURE !$3-319 #domain long-chain alcohol dehydrogenase homology !8#label LADH SUMMARY #length 319 #molecular-weight 33400 #checksum 9960 SEQUENCE /// ENTRY A54674 #type complete TITLE L-iditol 2-dehydrogenase (EC 1.1.1.14) - human ALTERNATE_NAMES sorbitol dehydrogenase ORGANISM #formal_name Homo sapiens #common_name man DATE 18-Aug-1995 #sequence_revision 18-Aug-1995 #text_change 11-Jun-1999 ACCESSIONS A54674; A56746 REFERENCE A54674 !$#authors Lee, F.K.; Cheung, M.C.; Chung, S. !$#journal Genomics (1994) 21:354-358 !$#title The human sorbitol dehydrogenase gene: cDNA cloning, !1sequence determination, and mapping by fluorescence in situ !1hybridization. !$#cross-references MUID:94375058; PMID:8088829 !$#accession A54674 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-357 ##label LEE !'##cross-references GB:U07361; NID:g805074; PIDN:AAA66064.1; !1PID:g520450 REFERENCE A56746 !$#authors Iwata, T.; Popescu, N.C.; Zimonjic, D.B.; Karlsson, C.; !1Hoeoeg, J.O.; Vaca, G.; Rodriguez, I.R.; Carper, D. !$#journal Genomics (1995) 26:55-62 !$#title Structural organization of the human sorbitol dehydrogenase !1gene (SORD). !$#cross-references MUID:95301293; PMID:7782086 !$#accession A56746 !'##molecule_type mRNA !'##residues 1-357 ##label IWA !'##cross-references GB:L29008; NID:g496077 !'##note the sequence in GenBank entry HUMLI2D, release 103, !1(PID:g496078) has the codon CTG for 239-Gln rather than the !1published CAG GENETICS !$#gene GDB:SORD !'##cross-references GDB:119598; OMIM:182500 !$#map_position 15q15.1-15q21.1 COMPLEX homotetramer FUNCTION !$#description catalyzes the oxidation by NAD+ of sorbitol to fructose CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS acetylated amino end; homotetramer; NAD; oxidoreductase; !1zinc FEATURE !$30-341 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$175-204 #region beta-alpha-beta NAD nucleotide-binding fold\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental\ !$45,70,156 #binding_site zinc, catalytic (Cys, His, Glu) #status !8predicted SUMMARY #length 357 #molecular-weight 38311 #checksum 3347 SEQUENCE /// ENTRY S10065 #type complete TITLE L-iditol 2-dehydrogenase (EC 1.1.1.14) - sheep (tentative sequence) ALTERNATE_NAMES sorbitol dehydrogenase ORGANISM #formal_name Ovis orientalis aries, Ovis ammon aries #common_name domestic sheep DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 11-May-2000 ACCESSIONS S10065; S07225 REFERENCE S10065 !$#authors Joernvall, H.; Carlquist, M.; Jeffery, J. !$#journal Pharmacol. Biochem. Behav. (1983) 18:67-71 !$#title Alcohol and polyol dehydrogenases. !$#cross-references MUID:84042881; PMID:6356166 !$#accession S10065 !'##molecule_type protein !'##residues 1-93 ##label JOE REFERENCE S07225 !$#authors Jeffery, J.; Cederlund, E.; Joernvall, H. !$#journal Eur. J. Biochem. (1984) 140:7-16 !$#title Sorbitol dehydrogenase. The primary structure of the !1sheep-liver enzyme. !$#cross-references MUID:84158607; PMID:6705798 !$#accession S07225 !'##molecule_type protein !'##residues 61-354 ##label JEF COMPLEX homotetramer FUNCTION !$#description catalyzes the oxidation by NAD+ of sorbitol to fructose CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS acetylated amino end; homotetramer; NAD; oxidoreductase; !1zinc FEATURE !$28-338 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$172-201 #region beta-alpha-beta NAD nucleotide-binding fold\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$43,67,153 #binding_site zinc, catalytic (Cys, His, Glu) #status !8predicted SUMMARY #length 354 #molecular-weight 37830 #checksum 8652 SEQUENCE /// ENTRY S16132 #type complete TITLE L-iditol 2-dehydrogenase (EC 1.1.1.14), long form - rat ALTERNATE_NAMES sorbitol dehydrogenase CONTAINS L-iditol 2-dehydrogenase, short form ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1993 #sequence_revision 24-Apr-1998 #text_change 11-Jun-1999 ACCESSIONS S38363; S16132 REFERENCE S38363 !$#authors Wen, Y.; Bekhor, I. !$#journal Eur. J. Biochem. (1993) 217:83-87 !$#title Sorbitol dehydrogenase. Full-length cDNA sequencing reveals !1a mRNA coding for a protein containing an additional 42 !1amino acids at the N-terminal end. !$#cross-references MUID:94039079; PMID:8223590 !$#accession S38363 !'##molecule_type mRNA !'##residues 1-399 ##label WEN !'##cross-references EMBL:X74593; NID:g397356; PIDN:CAA52670.1; !1PID:g397357 REFERENCE S16132 !$#authors Karlsson, C.; Joernvall, H.; Hoeoeg, J.O. !$#journal Eur. J. Biochem. (1991) 198:761-765 !$#title Sorbitol dehydrogenase: cDNA coding for the rat enzyme. !1Variations within the alcohol dehydrogenase family !1independent of quaternary structure and metal content. !$#cross-references MUID:91266961; PMID:2050152 !$#accession S16132 !'##molecule_type mRNA !'##residues 43-300,'D',302-399 ##label KAR !'##cross-references EMBL:X59037; NID:g57222; PIDN:CAA41761.1; !1PID:g57223 COMPLEX homotetramer FUNCTION !$#description catalyzes the oxidation by NAD+ of sorbitol to fructose CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS homotetramer; NAD; oxidoreductase; zinc FEATURE !$44-399 #product L-iditol dehydrogenase, short form #status !8predicted #label MAT\ !$72-383 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$217-246 #region beta-alpha-beta NAD nucleotide-binding fold\ !$87,112,198 #binding_site zinc, catalytic (Cys, His, Glu) #status !8predicted SUMMARY #length 399 #molecular-weight 42820 #checksum 7365 SEQUENCE /// ENTRY S65956 #type fragment TITLE L-iditol 2-dehydrogenase (EC 1.1.1.14), long form - mouse (fragment) ALTERNATE_NAMES sorbitol dehydrogenase CONTAINS L-iditol 2-dehydrogenase, short form ORGANISM #formal_name Mus musculus #common_name house mouse DATE 28-Oct-1996 #sequence_revision 24-Apr-1998 #text_change 11-Jun-1999 ACCESSIONS S65956 REFERENCE S65956 !$#authors Lee, F.K.; Lee, A.Y.W.; Lin, C.X.F.; Chung, S.S.M.; Chung, !1S.K. !$#journal Eur. J. Biochem. (1995) 230:1059-1065 !$#title Cloning, sequencing, and determination of the sites of !1expression of mouse sorbitol dehydrogenase cDNA. !$#cross-references MUID:95324564; PMID:7601136 !$#accession S65956 !'##status preliminary !'##molecule_type mRNA !'##residues 1-375 ##label LEE !'##cross-references EMBL:U27014; NID:g1009705; PIDN:AAA79043.1; !1PID:g1009706 COMPLEX homotetramer FUNCTION !$#description catalyzes the oxidation by NAD+ of sorbitol to fructose CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS homotetramer; NAD; oxidoreductase; zinc FEATURE !$20-375 #product L-iditol dehydrogenase, short form #status !8predicted #label MAT\ !$48-359 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$193-222 #region beta-alpha-beta NAD nucleotide-binding fold\ !$63,88,174 #binding_site zinc, catalytic (Cys, His, Glu) #status !8predicted SUMMARY #length 375 #checksum 7921 SEQUENCE /// ENTRY S32484 #type complete TITLE L-iditol 2-dehydrogenase (EC 1.1.1.14) - silkworm ALTERNATE_NAMES sorbitol dehydrogenase ORGANISM #formal_name Bombyx mori #common_name silkworm DATE 06-Jan-1995 #sequence_revision 06-Jan-1995 #text_change 16-Jun-2000 ACCESSIONS S32484 REFERENCE S32484 !$#authors Niimi, T.; Yamashita, O.; Yaginuma, T. !$#journal Eur. J. Biochem. (1993) 213:1125-1131 !$#title A cold-inducible Bombyx gene encoding a protein similar to !1mammalian sorbitol dehydrogenase. Yolk nuclei-dependent gene !1expression in diapause eggs. !$#cross-references MUID:97087160; PMID:8504807 !$#accession S32484 !'##status preliminary !'##molecule_type mRNA !'##residues 1-348 ##label NII !'##cross-references EMBL:D13371; NID:g217259; PIDN:BAA02634.1; !1PID:g217260 COMPLEX homotetramer FUNCTION !$#description catalyzes the oxidation by NAD+ of sorbitol to fructose CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS homotetramer; metalloprotein; NAD; oxidoreductase; zinc FEATURE !$25-337 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$170-199 #region beta-alpha-beta NAD nucleotide-binding fold\ !$40,65,151 #binding_site zinc, catalytic (Cys, His, Gln) #status !8predicted\ !$95,98,101,109 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 348 #molecular-weight 37158 #checksum 1043 SEQUENCE /// ENTRY S35981 #type complete TITLE L-iditol 2-dehydrogenase (EC 1.1.1.14) - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES sorbitol dehydrogenase ORGANISM #formal_name Schizosaccharomyces pombe DATE 13-Jan-1995 #sequence_revision 01-Dec-2000 #text_change 01-Dec-2000 ACCESSIONS T39670; S38345; S35981 REFERENCE Z21847 !$#authors Lyne, M.; Rajandream, M.A.; Barrell, B.G.; Beck, A.; Borzym, !1K.; Klages, S.; Langer, I.; Reinhardt, R. !$#submission submitted to the EMBL Data Library, November 1998 !$#accession T39670 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-360 ##label LYN !'##cross-references EMBL:AL033389; PIDN:CAA21910.1; GSPDB:GN00067; !1SPDB:SPBC1773.05c !'##experimental_source strain 972h-; cosmid c1773 REFERENCE S38345 !$#authors Wagner, P.; Grimaldi, M.; Jenkins, J.R. !$#journal Eur. J. Biochem. (1993) 217:731-736 !$#title Putative dehydrogenase tms1 suppresses growth arrest induced !1by a p53 tumour mutant in fission yeast. !$#cross-references MUID:94039112; PMID:8223615 !$#accession S38345 !'##status preliminary !'##molecule_type DNA !'##residues 14-360 ##label WA2 !'##cross-references EMBL:X74422; NID:g396478; PIDN:CAA52443.1; !1PID:g396479 !'##note submitted to the EMBL Data Library, July 1993 GENETICS !$#gene SPDB:SPBC1773.05c; tms1 !$#map_position 2 COMPLEX homotetramer FUNCTION !$#description catalyzes the oxidation by NAD+ of sorbitol to fructose CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS homotetramer; metalloprotein; NAD; oxidoreductase; zinc FEATURE !$27-346 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$172-201 #region beta-alpha-beta NAD nucleotide-binding fold\ !$42,67,153 #binding_site zinc, catalytic (Cys, His, Glu) #status !8predicted\ !$97,100,103,111 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 360 #molecular-weight 38851 #checksum 586 SEQUENCE /// ENTRY S55941 #type complete TITLE L-iditol 2-dehydrogenase (EC 1.1.1.14) SOR1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein J2395; protein YJR159w; sorbitol dehydrogenase ORGANISM #formal_name Saccharomyces cerevisiae DATE 23-Aug-1995 #sequence_revision 08-Sep-1995 #text_change 21-Jul-2000 ACCESSIONS S55941; S57188; S57189 REFERENCE S55941 !$#authors Sarthy, A.V.; Schopp, C.; Idler, K.B. !$#journal Gene (1994) 140:121-126 !$#title Cloning and sequence determination of the gene encoding !1sorbitol dehydrogenase from Saccharomyces cerevisiae. !$#cross-references MUID:94171068; PMID:8125328 !$#accession S55941 !'##molecule_type DNA !'##residues 1-357 ##label SAR !'##cross-references EMBL:L11039; NID:g295660; PIDN:AAA35027.1; !1PID:g295661 REFERENCE S57052 !$#authors Huang, M.E.; Chuat, J.C.; Galibert, F. !$#submission submitted to the Protein Sequence Database, September 1995 !$#accession S57188 !'##molecule_type DNA !'##residues 1-20 ##label HUA !'##cross-references EMBL:Z49659; GSPDB:GN00010; MIPS:YJR159w REFERENCE S57189 !$#authors Wedler, H.; Underwood, A.P.; Louis, E.J.; Wambutt, R. !$#submission submitted to the Protein Sequence Database, September 1995 !$#accession S57189 !'##molecule_type DNA !'##residues 11-357 ##label WED !'##cross-references EMBL:Z49659; GSPDB:GN00010; MIPS:YJR159w GENETICS !$#gene SGD:SOR1; MIPS:YJR159w !'##cross-references SGD:S0003920; MIPS:YJR159w !$#map_position 10R FUNCTION !$#description catalyzes the oxidation by NAD+ of sorbitol to fructose CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS NAD; oxidoreductase; zinc FEATURE !$28-344 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$173-202 #region beta-alpha-beta NAD nucleotide-binding fold\ !$43,68,154 #binding_site zinc, catalytic (Cys, His, Glu) #status !8predicted SUMMARY #length 357 #molecular-weight 38165 #checksum 3981 SEQUENCE /// ENTRY S67811 #type complete TITLE L-iditol 2-dehydrogenase (EC 1.1.1.14) YDL246c - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein D0225; sorbitol dehydrogenase ORGANISM #formal_name Saccharomyces cerevisiae DATE 12-Jul-1996 #sequence_revision 12-Jul-1996 #text_change 19-Apr-2002 ACCESSIONS S67811 REFERENCE S67655 !$#authors Rieger, M.; Mueller-Auer, S.; Brueckner, M.; Schaefer, M.; !1Wagner, G. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67811 !'##molecule_type DNA !'##residues 1-357 ##label RIE !'##cross-references EMBL:Z74294; NID:g1431419; PIDN:CAA98826.1; !1PID:g1431420; GSPDB:GN00004; MIPS:YDL246c !'##experimental_source strain S288C GENETICS !$#gene MIPS:YDL246c !'##cross-references SGD:S0002405 !$#map_position 4L FUNCTION !$#description catalyzes the oxidation by NAD+ of sorbitol to fructose CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS NAD; oxidoreductase; zinc FEATURE !$28-344 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$173-202 #region beta-alpha-beta NAD nucleotide-binding fold\ !$43,68,154 #binding_site zinc, catalytic (Cys, His, Glu) #status !8predicted SUMMARY #length 357 #molecular-weight 38096 #checksum 4032 SEQUENCE /// ENTRY S64902 #type complete TITLE probable sugar reductase (EC 1.1.1.-) YLR070c - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein L2301 ORGANISM #formal_name Saccharomyces cerevisiae DATE 01-Aug-1995 #sequence_revision 24-May-1996 #text_change 21-Jul-2000 ACCESSIONS S64902; S64898 REFERENCE S64899 !$#authors Pohl, T.M. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64902 !'##molecule_type DNA !'##residues 1-356 ##label POH !'##cross-references EMBL:Z73242; NID:g1360423; PIDN:CAA97627.1; !1PID:g1360424; GSPDB:GN00012; MIPS:YLR070c !'##experimental_source strain S288C REFERENCE S64872 !$#authors Andre, B.; Urrestarazu, L.A. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64898 !'##molecule_type DNA !'##residues 287-356 ##label AND !'##cross-references EMBL:Z73242; GSPDB:GN00012; MIPS:YLR070c !'##experimental_source strain S288C COMMENT This protein is related to L-iditol 2-dehydrogenase and !1D-xylulose reductase. GENETICS !$#gene MIPS:YLR070c !'##cross-references SGD:S0004060 !$#map_position 12R CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS NAD; oxidoreductase; zinc FEATURE !$29-343 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$174-203 #region beta-alpha-beta NAD nucleotide-binding fold\ !$186-202 #domain transmembrane #status predicted #label TMM\ !$44,69,155 #binding_site zinc, catalytic (Cys, His, Glu) #status !8predicted SUMMARY #length 356 #molecular-weight 38600 #checksum 5532 SEQUENCE /// ENTRY S13529 #type complete TITLE D-xylulose reductase (EC 1.1.1.9) - yeast (Pichia stipitis) ALTERNATE_NAMES xylitol dehydrogenase ORGANISM #formal_name Pichia stipitis DATE 04-Dec-1992 #sequence_revision 04-Dec-1992 #text_change 11-Jun-1999 ACCESSIONS S13529 REFERENCE S13529 !$#authors Koetter, P.; Amore, R.; Hollenberg, C.P.; Ciriacy, M. !$#journal Curr. Genet. (1990) 18:493-500 !$#title Isolation and characterization of the Pichia stipitis !1xylitol dehydrogenase gene, XYL2, and construction of a !1xylose-utilizing Saccharomyces cerevisiae transformant. !$#cross-references MUID:91168296; PMID:2127555 !$#accession S13529 !'##molecule_type DNA !'##residues 1-363 ##label KOE !'##cross-references EMBL:X55392; NID:g3262; PIDN:CAA39066.1; PID:g3263 GENETICS !$#gene XYL2 FUNCTION !$#description catalyzes the reversible reduction by NADH of D-xylulose to !1xylitol !$#pathway carbohydrate metabolism CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS NAD; oxidoreductase; zinc FEATURE !$26-351 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$178-207 #region beta-alpha-beta NAD nucleotide-binding fold\ !$41,66,159 #binding_site zinc, catalytic (Cys, His, Glu) #status !8predicted SUMMARY #length 363 #molecular-weight 38521 #checksum 4667 SEQUENCE /// ENTRY A45052 #type complete TITLE L-iditol 2-dehydrogenase (EC 1.1.1.14) - Bacillus subtilis ALTERNATE_NAMES glucitol dehydrogenase; polyol dehydrogenase; sorbitol dehydrogenase ORGANISM #formal_name Bacillus subtilis DATE 10-Mar-1994 #sequence_revision 10-Mar-1994 #text_change 03-Nov-2000 ACCESSIONS A45052; E69638; I39862 REFERENCE A45052 !$#authors Ng, K.; Ye, R.; Wu, X.C.; Wong, S.L. !$#journal J. Biol. Chem. (1992) 267:24989-24994 !$#title Sorbitol dehydrogenase from Bacillus subtilis. Purification, !1characterization, and gene cloning. !$#cross-references MUID:93094198; PMID:1460002 !$#accession A45052 !'##molecule_type DNA !'##residues 1-353 ##label NG1 !'##cross-references GB:M96947; NID:g304152; PIDN:AAA22508.1; !1PID:g304153 !'##experimental_source strain W168 !'##note sequence extracted from NCBI backbone (NCBIN:120108, !1NCBIP:120111) !'##note sequencing of the amino end of the mature protein indicated !1that Met-1 is removed in about half of the molecules !'##note presents arguments that the third ligand of the catalytic zinc !1is 156-Glu REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69638 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-353 ##label KUN !'##cross-references GB:Z99107; GB:AL009126; NID:g2632866; !1PIDN:CAB12434.1; PID:g2632928 !'##experimental_source strain W168 REFERENCE I39862 !$#authors Ye, R.; Wong, S.L. !$#journal J. Bacteriol. (1994) 176:3314-3320 !$#title Transcriptional regulation of the Bacillus subtilis glucitol !1dehydrogenase gene. !$#cross-references MUID:94253000; PMID:8195086 !$#accession I39862 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-8 ##label YER !'##cross-references GB:L16626; NID:g436962; PIDN:AAA20875.1; !1PID:g530793 GENETICS !$#gene gutB COMPLEX homotetramer FUNCTION !$#description catalyzes the oxidation by NAD+ of sorbitol to fructose CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS homotetramer; NAD; oxidoreductase; zinc FEATURE !$30-340 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$175-204 #region beta-alpha-beta NAD nucleotide-binding fold\ !$45,70,156 #binding_site zinc, catalytic (Cys, His, Glu) #status !8predicted\ !$100,103,106,114 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 353 #molecular-weight 38390 #checksum 3251 SEQUENCE /// ENTRY H69789 #type complete TITLE probable alcohol dehydrogenase (EC 1.1.1.-) ydjL [similarity] - Bacillus subtilis ALTERNATE_NAMES L-iditol 2-dehydrogenase homolog ydjL; sorbitol dehydrogenase homolog ORGANISM #formal_name Bacillus subtilis DATE 05-Dec-1997 #sequence_revision 05-Dec-1997 #text_change 15-Sep-2000 ACCESSIONS H69789 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69789 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-346 ##label KUN !'##cross-references GB:Z99107; GB:AL009126; NID:g2632866; !1PIDN:CAB12443.1; PID:g2632937 !'##experimental_source strain 168 GENETICS !$#gene ydjL CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS metalloprotein; NAD; oxidoreductase; zinc FEATURE !$22-334 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$171-200 #region beta-alpha-beta NAD nucleotide-binding fold\ !$37,70,152 #binding_site zinc, catalytic (Cys, His, Glu) #status !8predicted SUMMARY #length 346 #molecular-weight 37341 #checksum 8595 SEQUENCE /// ENTRY F64937 #type complete TITLE probable L-iditol 2-dehydrogenase (EC 1.1.1.14) b1774 - Escherichia coli (strain K-12) ALTERNATE_NAMES sorbitol dehydrogenase ORGANISM #formal_name Escherichia coli DATE 12-Sep-1997 #sequence_revision 17-Sep-1997 #text_change 01-Mar-2002 ACCESSIONS F64937 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64937 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-347 ##label BLAT !'##cross-references GB:AE000272; GB:U00096; NID:g1788067; !1PIDN:AAC74844.1; PID:g1788073; UWGP:b1774 !'##experimental_source strain K-12, substrain MG1655 FUNCTION !$#description catalyzes the oxidation by NAD+ of sorbitol to fructose CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS metalloprotein; NAD; oxidoreductase; zinc FEATURE !$24-334 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$171-200 #region beta-alpha-beta NAD nucleotide-binding fold\ !$39,65,152 #binding_site zinc, catalytic (Cys, His, Glu) #status !8predicted\ !$95,98,101,109 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 347 #molecular-weight 37701 #checksum 266 SEQUENCE /// ENTRY F64141 #type complete TITLE probable L-iditol 2-dehydrogenase (EC 1.1.1.14) HI0053 - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES sorbitol dehydrogenase ORGANISM #formal_name Haemophilus influenzae DATE 18-Aug-1995 #sequence_revision 18-Aug-1995 #text_change 11-Jun-1999 ACCESSIONS F64141 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession F64141 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-342 ##label TIGR !'##cross-references GB:U32690; GB:L42023; NID:g1572991; !1PIDN:AAC21731.1; PID:g1573000; TIGR:HI0053 FUNCTION !$#description catalyzes the oxidation by NAD+ of sorbitol to fructose CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS metalloprotein; NAD; oxidoreductase; zinc FEATURE !$26-331 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$168-197 #region beta-alpha-beta NAD nucleotide-binding fold\ !$41,63,149 #binding_site zinc, catalytic (Cys, His, Glu) #status !8predicted\ !$94,97,100,108 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 342 #molecular-weight 37429 #checksum 3199 SEQUENCE /// ENTRY S56585 #type complete TITLE L-iditol 2-dehydrogenase (EC 1.1.1.14) homolog yjjN - Escherichia coli (strain K-12) ALTERNATE_NAMES hypothetical protein o345; sorbitol dehydrogenase ORGANISM #formal_name Escherichia coli DATE 28-Oct-1995 #sequence_revision 03-Nov-1995 #text_change 01-Mar-2002 ACCESSIONS S56585; H65250 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56585 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-345 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97256.1; !1PID:g537201 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65250 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-345 ##label BLAT !'##cross-references GB:AE000506; GB:U00096; NID:g2367377; !1PIDN:AAC77314.1; PID:g1790819; UWGP:b4358 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yjjN !$#start_codon GTG CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS metalloprotein; NAD; oxidoreductase; zinc FEATURE !$30-334 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$170-198 #region beta-alpha-beta NAD nucleotide-binding fold\ !$45,67,151 #binding_site zinc, catalytic (Cys, His, Glu) #status !8predicted\ !$97,100,103,111 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 345 #molecular-weight 37064 #checksum 5028 SEQUENCE /// ENTRY F69852 #type complete TITLE L-iditol 2-dehydrogenase (EC 1.1.1.14) homolog yjmD - Bacillus subtilis ALTERNATE_NAMES sorbitol dehydrogenase homolog ORGANISM #formal_name Bacillus subtilis DATE 05-Dec-1997 #sequence_revision 05-Dec-1997 #text_change 16-Jun-2000 ACCESSIONS F69852 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69852 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-339 ##label KUN !'##cross-references GB:Z99110; GB:AL009126; NID:g2633472; !1PIDN:CAB13090.1; PID:g2633587 !'##experimental_source strain 168 GENETICS !$#gene yjmD CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS metalloprotein; NAD; oxidoreductase; zinc FEATURE !$23-327 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$164-192 #region beta-alpha-beta NAD nucleotide-binding fold\ !$38,60,145 #binding_site zinc, catalytic (Cys, His, Glu) #status !8predicted\ !$90,93,96,104 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 339 #molecular-weight 36762 #checksum 1733 SEQUENCE /// ENTRY I81185 #type complete TITLE starvation-sensing protein rspB (EC 1.1.1.-) - Escherichia coli (strain K-12) ALTERNATE_NAMES L-iditol 2-dehydrogenase homolog; sorbitol dehydrogenase homolog ORGANISM #formal_name Escherichia coli DATE 07-Jun-1996 #sequence_revision 07-Jun-1996 #text_change 01-Mar-2002 ACCESSIONS I81185; F64913 REFERENCE I59589 !$#authors Huisman, G.W.; Kolter, R. !$#journal Science (1994) 265:537-539 !$#title Sensing starvation: a homoserine lactone--dependent !1signaling pathway in Escherichia coli. !$#cross-references MUID:94310441; PMID:7545940 !$#accession I81185 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-339 ##label RES !'##cross-references GB:L31628; NID:g495781; PIDN:AAA21686.1; !1PID:g495783 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64913 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-339 ##label BLAT !'##cross-references GB:AE000254; GB:U00096; NID:g1787862; !1PIDN:AAC74652.1; PID:g1787863; UWGP:b1580 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene rspB !$#map_position 36.5 min CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS metalloprotein; NAD; oxidoreductase; zinc FEATURE !$22-326 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$163-193 #region beta-alpha-beta NAD nucleotide-binding fold\ !$37,59,144 #binding_site zinc, catalytic (Cys, His, Glu) #status !8predicted\ !$89,92,95,103 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 339 #molecular-weight 36564 #checksum 9784 SEQUENCE /// ENTRY S56493 #type complete TITLE probable alcohol dehydrogenase (EC 1.1.1.-) yjgV - Escherichia coli (strain K-12) ALTERNATE_NAMES hypothetical protein f343a ORGANISM #formal_name Escherichia coli DATE 28-Oct-1995 #sequence_revision 03-Nov-1995 #text_change 01-Mar-2002 ACCESSIONS S56493; F65239 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56493 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-343 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97164.1; !1PID:g537109 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65239 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-343 ##label BLAT !'##cross-references GB:AE000497; GB:U00096; NID:g1790711; !1PIDN:AAC77224.1; PID:g1790718; UWGP:b4267 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yjgV CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS metalloprotein; NAD; oxidoreductase; zinc FEATURE !$25-333 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$172-201 #region beta-alpha-beta NAD nucleotide-binding fold\ !$40,65,153 #binding_site zinc, catalytic (Cys, His, Glu) #status !8predicted\ !$93,96,99,107 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 343 #molecular-weight 37146 #checksum 7236 SEQUENCE /// ENTRY A42654 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1), thermostable - Bacillus stearothermophilus (strain NCA1503) ORGANISM #formal_name Bacillus stearothermophilus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jun-2000 ACCESSIONS A42654; S07218; A10207 REFERENCE A42654 !$#authors Sakoda, H.; Imanaka, T. !$#journal J. Bacteriol. (1992) 174:1397-1402 !$#title Cloning and sequencing of the gene coding for alcohol !1dehydrogenase of Bacillus stearothermophilus and rational !1shift of the optimum pH. !$#cross-references MUID:92138636; PMID:1735726 !$#accession A42654 !'##molecule_type DNA !'##residues 1-337 ##label SAK !'##cross-references GB:D90421; NID:g216229; PIDN:BAA14411.1; !1PID:g216230 !'##note sequence extracted from NCBI backbone (NCBIN:79664, !1NCBIP:79665) REFERENCE S07218 !$#authors Jeck, R.; Woenckhaus, C.; Harris, J.I.; Runswick, M.J. !$#journal Eur. J. Biochem. (1979) 93:57-64 !$#title Identification of the amino acid residue modified in !1Bacillus stearothermophilus alcohol dehydrogenase by the !1NAD+ analogue 4- !1(3-Bromoacetylpyridinio)butyldiphosphoadenosine. !$#cross-references MUID:79169263; PMID:436831 !$#accession S07218 !'##molecule_type protein !'##residues 34-40,'B',42-47,'B',49-51,'PK',54 ##label JEC !'##note this is a revision to the sequence from reference A10207 REFERENCE A10207 !$#authors Bridgen, J.; Kolb, E.; Harris, J.I. !$#journal FEBS Lett. (1973) 33:1-3 !$#title Amino acid sequence homology in alcohol dehydrogenase. !$#cross-references MUID:73229257; PMID:4578954 !$#accession A10207 !'##molecule_type protein !'##residues 1-21,23-32,34-40,'V',42,'G',44-45 ##label BRI GENETICS !$#gene adhT FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; metalloprotein; NAD; oxidoreductase; !1zinc FEATURE !$23-326 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$167-195 #region beta-alpha-beta NAD nucleotide-binding fold\ !$38,61,148 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$92,95,98,106 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 337 #molecular-weight 36100 #checksum 407 SEQUENCE /// ENTRY S45605 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1), thermostable - Bacillus stearothermophilus (strain NCIMB 12403) ORGANISM #formal_name Bacillus stearothermophilus DATE 07-Oct-1994 #sequence_revision 10-Nov-1995 #text_change 11-Jun-1999 ACCESSIONS S45605 REFERENCE S45605 !$#authors Cannio, R.; Rossi, M.; Bartolucci, S. !$#journal Eur. J. Biochem. (1994) 222:345-352 !$#title A few amino acid substitutions are responsible for the !1higher thermostability of a novel NAD(+)-dependent bacillar !1alcohol dehydrogenase. !$#cross-references MUID:94291628; PMID:8020473 !$#accession S45605 !'##molecule_type DNA !'##residues 1-339 ##label CAN !'##cross-references EMBL:Z27089; NID:g440137; PIDN:CAA81612.1; !1PID:g440138 GENETICS !$#gene adhT FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; metalloprotein; NAD; oxidoreductase; !1zinc FEATURE !$23-326 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$167-195 #region beta-alpha-beta NAD nucleotide-binding fold\ !$38,61,148 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$92,95,98,106 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 339 #molecular-weight 36338 #checksum 5348 SEQUENCE /// ENTRY S47643 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) - Bacillus stearothermophilus (strain DSM 2334) ORGANISM #formal_name Bacillus stearothermophilus DATE 01-Feb-1995 #sequence_revision 08-Sep-1995 #text_change 11-Jun-1999 ACCESSIONS S47643; S56072; S44262 REFERENCE S47643 !$#authors Robinson, G.A.; Bailey, C.J.; Dowds, B.C.A. !$#journal Biochim. Biophys. Acta (1994) 1218:432-434 !$#title Gene structure and amino acid sequences of alcohol !1dehydrogenases of Bacillus stearothermophilus. !$#cross-references MUID:94325354; PMID:8049268 !$#accession S47643 !'##molecule_type DNA !'##residues 1-339 ##label ROB1 !'##cross-references EMBL:Z25544; NID:g479043; PIDN:CAA80989.1; !1PID:g580823 !'##experimental_source strain DSM 2334 !$#accession S56072 !'##molecule_type protein !'##residues 1-34;36-37;39-40 ##label ROB2 GENETICS !$#start_codon GTG FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; metalloprotein; NAD; oxidoreductase; !1zinc FEATURE !$23-326 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$167-195 #region beta-alpha-beta NAD nucleotide-binding fold\ !$38,61,148 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$92,95,98,106 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 339 #molecular-weight 36205 #checksum 5616 SEQUENCE /// ENTRY A64901 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) b1478 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 12-Sep-1997 #sequence_revision 17-Sep-1997 #text_change 01-Mar-2002 ACCESSIONS A64901 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64901 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-346 ##label BLAT !'##cross-references GB:AE000245; GB:U00096; NID:g1787752; !1PIDN:AAC74551.1; PID:g1787753; UWGP:b1478 !'##experimental_source strain K-12, substrain MG1655 FUNCTION !$#description catalyzes the reversible oxidation of primary and secondary !1alcohols to aldehydes and ketones, respectively, by NAD+ CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; metalloprotein; NAD; oxidoreductase; !1zinc FEATURE !$32-334 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$47,68,155 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$99,102,105,113 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 346 #molecular-weight 36479 #checksum 7856 SEQUENCE /// ENTRY A35260 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) 1 - Zymomonas mobilis ORGANISM #formal_name Zymomonas mobilis DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 11-Jun-1999 ACCESSIONS A35260; E40649; A24801 REFERENCE A35260 !$#authors Keshav, K.F.; Yomano, L.P.; An, H.; Ingram, L.O. !$#journal J. Bacteriol. (1990) 172:2491-2497 !$#title Cloning of the Zymomonas mobilis structural gene encoding !1alcohol dehydrogenase I (adhA): sequence comparison and !1expression in Escherichia coli. !$#cross-references MUID:90236908; PMID:2185223 !$#accession A35260 !'##molecule_type DNA !'##residues 1-337 ##label KES !'##cross-references GB:M32100; NID:g155570; PIDN:AAA27682.1; !1PID:g155571 REFERENCE A40649 !$#authors Yomano, L.P.; Scopes, R.K.; Ingram, L.O. !$#journal J. Bacteriol. (1993) 175:3926-3933 !$#title Cloning, sequencing, and expression of the Zymomonas mobilis !1phosphoglycerate mutase gene (pgm) in Escherichia coli. !$#cross-references MUID:93308069; PMID:8320209 !$#accession E40649 !'##molecule_type DNA !'##residues 1-40 ##label YOM !'##cross-references GB:L09650; NID:g155572; PIDN:AAA71935.1; !1PID:g155575 REFERENCE A91156 !$#authors Neale, A.D.; Scopes, R.K.; Kelly, J.M.; Wettenhall, R.E.H. !$#journal Eur. J. Biochem. (1986) 154:119-124 !$#title The two alcohol dehydrogenases of Zymomonas mobilis. !1Purification by differential dye ligand chromatography, !1molecular characterisation and physiological roles. !$#cross-references MUID:86108298; PMID:2935393 !$#accession A24801 !'##molecule_type protein !'##residues 1-16,'I',18-25,'F',27,'H',29,'P',31 ##label NEA GENETICS !$#gene adhA FUNCTION !$#description catalyzes the reversible oxidation of primary and secondary !1alcohols to aldehydes and ketones, respectively, by NAD+ CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; metalloprotein; NAD; oxidoreductase; !1zinc FEATURE !$22-324 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$37,58,145 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$89,92,95,103 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 337 #molecular-weight 36094 #checksum 7978 SEQUENCE /// ENTRY B64976 #type complete TITLE galactitol-1-phosphate dehydrogenase (EC 1.1.1.-) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 12-Sep-1997 #sequence_revision 17-Sep-1997 #text_change 01-Mar-2002 ACCESSIONS B64976; S49084; S55906 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64976 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-346 ##label BLAT !'##cross-references GB:AE000298; GB:U00096; NID:g1788395; !1PIDN:AAC75152.1; PID:g1788407; UWGP:b2091 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S49079 !$#authors Nobelmann, B.; Lengeler, J.W. !$#submission submitted to the EMBL Data Library, June 1994 !$#description Molecular analysis of the gat-genes for Galactitol transport !1and metabolism. !$#accession S49084 !'##status preliminary !'##molecule_type DNA !'##residues 1-212,'L',214-221,'G',223-225,'DV',228-270,'T',272-326,'T', !1328,'V',330-346 ##label NOB !'##cross-references EMBL:X79837; NID:g599737; PIDN:CAA56231.1; !1PID:g508176 REFERENCE S55901 !$#authors Nobelmann, B.; Lengeler, J.W. !$#journal Biochim. Biophys. Acta (1995) 1262:69-72 !$#title Sequence of the gat operon for galactitol utilization from a !1wild-type strain EC3132 of Escherichia coli. !$#cross-references MUID:95290497; PMID:7772602 !$#accession S55906 !'##status preliminary !'##molecule_type DNA !'##residues 1-212,'L',214-221,'G',223-225,'DV',228-270,'T',272-326,'T', !1328,'V',330-346 ##label NO2 !'##cross-references EMBL:X79837; NID:g599737; PIDN:CAA56231.1; !1PID:g508176 !'##experimental_source strain EC3132 GENETICS !$#gene gatD FUNCTION !$#description catalyzes the reversible oxidation by NAD+ of !1galactitol-1-phosphate to tagatose-6-phosphate CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS metalloprotein; NAD; oxidoreductase; zinc FEATURE !$23-336 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$163-192 #region beta-alpha-beta NAD nucleotide-binding fold\ !$38,59,144 #binding_site zinc, catalytic (Cys, His, Glu) #status !8predicted\ !$89,92,95,103 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 346 #molecular-weight 37390 #checksum 9555 SEQUENCE /// ENTRY DEBYA #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) 1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein O0947; protein YOL086c ORGANISM #formal_name Saccharomyces cerevisiae DATE 24-Apr-1984 #sequence_revision 16-Feb-1996 #text_change 21-Jul-2000 ACCESSIONS S57383; S50419; A92365; S38795; A00339; S66780; S05821 REFERENCE S57374 !$#authors Zumstein, E.; Pearson, B.M.; Kalogeropoulos, A.; Schweizer, !1M. !$#journal Yeast (1995) 11:975-986 !$#title A 29.425 kb segment on the left arm of yeast chromosome XV !1contains more than twice as many unknown as known open !1reading frames. !$#cross-references MUID:96021609; PMID:8533473 !$#accession S57383 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-348 ##label ZUM !'##cross-references EMBL:X83121; NID:g600461; PIDN:CAA58193.1; !1PID:g600472 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1994 REFERENCE S50410 !$#authors Zumstein, E.; Pearson, B.M.; Kalogeropoulos, A.; Schweizer, !1M. !$#submission submitted to the EMBL Data Library, December 1994 !$#accession S50419 !'##molecule_type DNA !'##residues 1-348 ##label ZUW !'##cross-references EMBL:X83121; NID:g600461; PIDN:CAA58193.1; !1PID:g600472 REFERENCE A92365 !$#authors Bennetzen, J.L.; Hall, B.D. !$#journal J. Biol. Chem. (1982) 257:3018-3025 !$#title The primary structure of the Saccharomyces cerevisiae gene !1for alcohol dehydrogenase I. !$#cross-references MUID:82142434; PMID:6277922 !$#accession A92365 !'##molecule_type DNA !'##residues 1-20,'H',22-348 ##label BEN !'##cross-references EMBL:V01292; NID:g3338; PIDN:CAA24601.1; PID:g3339 REFERENCE S38795 !$#authors Young, T.; Williamson, V.; Taguchi, A.; Smith, M.; !1Sledziewski, A.; Russell, D.; Osterman, J.; Denis, C.; Cox, !1D.; Beier, D. !$#journal Basic Life Sci. (1982) 19:335-361 !$#title The alcohol dehydrogenase genes of the yeast, Saccharomyces !1cerevisiae: isolation, structure, and regulation. !$#cross-references MUID:82160017; PMID:6279086 !$#accession S38795 !'##molecule_type DNA !'##residues 1-20,'H',22-348 ##label YOU !'##cross-references EMBL:M38456; NID:g171024; PIDN:AAA34410.1; !1PID:g171025 REFERENCE A91243 !$#authors Joernvall, H. !$#journal Eur. J. Biochem. (1977) 72:425-442 !$#title The primary structure of yeast alcohol dehydrogenase. !$#cross-references MUID:77115785; PMID:320000 !$#accession A00339 !'##molecule_type protein !'##residues 2-58,'T',60-147,'E',149-151,'V',153-236,'N',238-313,'I', !1315-337,'V',339-348 ##label JOR !'##note 236-Ile was also found !'##note microheterogeneities may also occur at positions 138, 139, !1243-245, and 256 and near position 288 REFERENCE S66775 !$#authors Zumstein, E.; Pearson, B.M.; Kalogeropoulos, A.; Schweizer, !1M. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S66780 !'##molecule_type DNA !'##residues 1-348 ##label ZUF !'##cross-references EMBL:Z74828; NID:g1419925; PIDN:CAA99098.1; !1PID:g1419926; GSPDB:GN00015; MIPS:YOL086c !'##experimental_source strain S288C GENETICS !$#gene SGD:ADH1; ADE1; ADC1; MIPS:YOL086c !'##cross-references SGD:S0005446; MIPS:YOL086c !$#map_position 15L FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS acetylated amino end; alcohol metabolism; metalloprotein; !1NAD; oxidoreductase; zinc FEATURE !$2-348 #product alcohol dehydrogenase I #status experimental !8#label MAT\ !$29-336 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$173-202 #region beta-alpha-beta NAD nucleotide-binding fold\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental\ !$44,67,154 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$98,101,104,112 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 348 #molecular-weight 36849 #checksum 191 SEQUENCE /// ENTRY DEBYA2 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) 2 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YM9952.05c; protein YMR303c ORGANISM #formal_name Saccharomyces cerevisiae DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 21-Jul-2000 ACCESSIONS A00340; S38796; S53973 REFERENCE A00340 !$#authors Russell, D.W.; Smith, M.; Williamson, V.M.; Young, E.T. !$#journal J. Biol. Chem. (1983) 258:2674-2682 !$#title Nucleotide sequence of the yeast alcohol dehydrogenase II !1gene. !$#cross-references MUID:83109119; PMID:6337160 !$#accession A00340 !'##molecule_type DNA !'##residues 1-348 ##label RUS !'##cross-references EMBL:V01293; NID:g3344; PIDN:CAA24602.1; !1PID:g600021 REFERENCE S38795 !$#authors Young, T.; Williamson, V.; Taguchi, A.; Smith, M.; !1Sledziewski, A.; Russell, D.; Osterman, J.; Denis, C.; Cox, !1D.; Beier, D. !$#journal Basic Life Sci. (1982) 19:335-361 !$#title The alcohol dehydrogenase genes of the yeast, Saccharomyces !1cerevisiae: isolation, structure, and regulation. !$#cross-references MUID:82160017; PMID:6279086 !$#accession S38796 !'##molecule_type DNA !'##residues 1-15,'H',17-30,'A',32-348 ##label YOU !'##cross-references EMBL:M38457; NID:g171028; PIDN:AAA34411.1; !1PID:g171029 REFERENCE S53969 !$#authors Connor, R.; Churcher, C.M. !$#submission submitted to the EMBL Data Library, April 1995 !$#accession S53973 !'##molecule_type DNA !'##residues 1-348 ##label CON !'##cross-references EMBL:Z49212; NID:g798940; PIDN:CAA89136.1; !1PID:g798945; GSPDB:GN00013; MIPS:YMR303c GENETICS !$#gene SGD:ADH2; ADR2; MIPS:YMR303c !'##cross-references SGD:S0004918; MIPS:YMR303c !$#map_position 13R COMPLEX homotetramer FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; homotetramer; metalloprotein; NAD; !1oxidoreductase; zinc FEATURE !$29-336 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$173-202 #region beta-alpha-beta NAD nucleotide-binding fold\ !$44,67,154 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$98,101,104,112 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 348 #molecular-weight 36732 #checksum 8944 SEQUENCE /// ENTRY S20911 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) II - yeast (Kluyveromyces marxianus var. lactis) ORGANISM #formal_name Kluyveromyces marxianus var. lactis, Candida sphaerica DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS S20911; S19804 REFERENCE S20911 !$#authors Shain, D.H.; Salvadore, C.; Denis, C.L. !$#journal Mol. Gen. Genet. (1992) 232:479-488 !$#title Evolution of the alcohol dehydrogenase (ADH) genes in yeast: !1characterization of a fourth ADH in Kluyveromyces lactis. !$#cross-references MUID:92269769; PMID:1588917 !$#accession S20911 !'##molecule_type DNA !'##residues 1-348 ##label SHA !'##cross-references EMBL:X64397; NID:g2832; PIDN:CAA45739.1; PID:g2833 GENETICS !$#gene ADH2 CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; metalloprotein; NAD; oxidoreductase; !1zinc FEATURE !$29-336 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$173-202 #region beta-alpha-beta NAD nucleotide-binding fold\ !$44,67,154 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$98,101,104,112 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 348 #molecular-weight 37097 #checksum 2871 SEQUENCE /// ENTRY S32521 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) 1 - yeast (Kluyveromyces marxianus var. marxianus) ORGANISM #formal_name Kluyveromyces marxianus var. marxianus, Candida kefyr DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS S32521 REFERENCE S32521 !$#authors Ladriere, J.M.; Delcour, J.; Vandenhaute, J. !$#journal Biochim. Biophys. Acta (1993) 1173:99-101 !$#title Sequence of a gene coding for a cytoplasmic alcohol !1dehydrogenase from Kluyveromyces marxianus ATCC 12424. !$#cross-references MUID:93250057; PMID:8485163 !$#accession S32521 !'##molecule_type DNA !'##residues 1-348 ##label LAD !'##cross-references EMBL:X60224; NID:g6822201; PIDN:CAA42785.1; !1PID:g297908 GENETICS !$#gene ADH1 CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; metalloprotein; NAD; oxidoreductase; !1zinc FEATURE !$29-336 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$44,67,154 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$98,101,104,112 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 348 #molecular-weight 37158 #checksum 2823 SEQUENCE /// ENTRY S17252 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) 3 precursor - yeast (Kluyveromyces marxianus var. lactis) ORGANISM #formal_name Kluyveromyces marxianus var. lactis, Candida sphaerica DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS S17252; S09293 REFERENCE S17252 !$#authors Saliola, M.; Gonnella, R.; Mazzoni, C.; Falcone, C. !$#journal Yeast (1991) 7:391-400 !$#title Two genes encoding putative mitochondrial alcohol !1dehydrogenases are present in the yeast Kluyveromyces !1lactis. !$#cross-references MUID:91335895; PMID:1872030 !$#accession S17252 !'##molecule_type DNA !'##residues 1-374 ##label SAL !'##cross-references EMBL:X62766; NID:g2807; PIDN:CAA44613.1; PID:g2808 !'##note the authors translated the codon CGT for residue 156 as Ala REFERENCE S09293 !$#authors Saliola, M.; Shuster, J.R.; Falcone, C. !$#journal Yeast (1990) 6:193-204 !$#title The alcohol dehydrogenase system in the yeast, Kluyveromyces !1lactis. !$#cross-references MUID:90273773; PMID:2190430 !$#accession S09293 !'##molecule_type DNA !'##residues 1-154 ##label SA2 !'##experimental_source strain 2359/152 !'##note not compared to nucleotide translation GENETICS !$#gene ADH3 !$#genome nuclear FUNCTION !$#description oxidoreductase CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; metalloprotein; mitochondrion; NAD; !1oxidoreductase; zinc FEATURE !$1-24 #domain (or 1-27) transit peptide (mitochondrion) !8#status predicted #label TRN\ !$25-374 #product (or 28-374) alcohol dehydrogenase 3 #status !8predicted #label MAT\ !$55-362 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$70,93,180 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$124,127,130,138 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 374 #molecular-weight 39682 #checksum 4128 SEQUENCE /// ENTRY S54458 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) 3 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YM9582.08; protein YMR083w ORGANISM #formal_name Saccharomyces cerevisiae DATE 08-Jul-1995 #sequence_revision 01-Sep-1995 #text_change 21-Jul-2000 ACCESSIONS S54458; S22244 REFERENCE S54451 !$#authors Gentles, S.; Bowman, S. !$#submission submitted to the EMBL Data Library, May 1995 !$#accession S54458 !'##molecule_type DNA !'##residues 1-375 ##label GEN !'##cross-references EMBL:Z49259; NID:g807956; PIDN:CAA89229.1; !1PID:g807965; GSPDB:GN00013; MIPS:YMR083w !'##experimental_source strain AB972 REFERENCE S22244 !$#authors Pilgrim, D.; Ciriacy, M. !$#submission submitted to the EMBL Data Library, October 1985 !$#accession S22244 !'##molecule_type DNA !'##residues 1-9,'K',11-44,'N',46-375 ##label PIL !'##cross-references EMBL:K03292; NID:g171022; PIDN:AAA34409.1; !1PID:g171023 GENETICS !$#gene SGD:ADH3; MIPS:YMR083w !'##cross-references SGD:S0004688; MIPS:YMR083w !$#map_position 13R FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; metalloprotein; NAD; oxidoreductase; !1zinc FEATURE !$56-363 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$200-229 #region beta-alpha-beta NAD nucleotide-binding fold\ !$71,94,181 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$125,128,131,139 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 375 #molecular-weight 40369 #checksum 6669 SEQUENCE /// ENTRY S46016 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) 5 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YBR1122; protein YBR145w ORGANISM #formal_name Saccharomyces cerevisiae DATE 26-Aug-1994 #sequence_revision 09-Sep-1994 #text_change 21-Jul-2000 ACCESSIONS S46016 REFERENCE S46013 !$#authors Entian, K.D.; Koetter, P.; Rose, M.; Becker, J.; Grey, M.; !1Li, Z.; Niegemann, E.; Schenk-Groeninger, R.; Servos, J.; !1Wehner, E.; Wolter, R.; Brendel, M.; Bauer, J.; Braun, H.; !1Dern, K.; Duesterhus, S.; Gruenbein, R.; Hedges, D.; Kiesau, !1P.; Korol, S.; Krems, B.; Proft, M.; Siegers, K.; Baur, A.; !1Boles, E.; Miosga, T.; Schaaff-Gerstenschlaeger, I.; !1Zimmermann, F.K. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S46016 !'##molecule_type DNA !'##residues 1-351 ##label ENT !'##cross-references EMBL:Z36014; NID:g536447; PIDN:CAA85103.1; !1PID:g536448; GSPDB:GN00002; MIPS:YBR145w !'##experimental_source strain S288C GENETICS !$#gene SGD:ADH5; MIPS:YBR145w !'##cross-references SGD:S0000349; MIPS:YBR145w !$#map_position 2R FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; metalloprotein; NAD; oxidoreductase; !1zinc FEATURE !$32-339 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$176-205 #region beta-alpha-beta NAD nucleotide-binding fold\ !$47,70,157 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$101,104,107,115 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 351 #molecular-weight 37648 #checksum 617 SEQUENCE /// ENTRY S52153 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) - yeast (Candida albicans) ALTERNATE_NAMES 40K allergen ORGANISM #formal_name Candida albicans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 08-Dec-2000 ACCESSIONS S63781; A61504; S52153 REFERENCE S63781 !$#authors Bertram, G.; Swoboda, R.K.; Gooday, G.W.; Gow, N.A.R.; !1Brown, A.J.P. !$#journal Yeast (1996) 12:115-127 !$#title Structure and regulation of the Candida albicans ADH1 gene !1encoding an immunogenic alcohol dehydrogenase. !$#cross-references MUID:96287648; PMID:8686375 !$#accession S63781 !'##status preliminary !'##molecule_type DNA !'##residues 1-350 ##label BE2 !'##cross-references EMBL:X81694; NID:g608689; PIDN:CAA57342.1; !1PID:g608690 !'##note only a part of the coding sequence is given REFERENCE A61504 !$#authors Shen, H.D.; Choo, K.B.; Lee, H.H.; Hsieh, J.C.; Lin, W.L.; !1Lee, W.R.; Han, S.H. !$#journal Clin. Exp. Allergy (1991) 21:675-681 !$#title The 40-kilodalton allergen of Candida albicans is an alcohol !1dehydrogenase: molecular cloning and immunological analysis !1using monoclonal antibodies. !$#cross-references MUID:92136159; PMID:1777830 !$#accession A61504 !'##molecule_type mRNA !'##residues 104-139,'T',141-226,'A',228-312,'S' ##label SHE !'##cross-references GB:X81694; NID:g608689 !'##note sequence extracted from NCBI backbone (NCBIN:80403, !1NCBIP:80409) GENETICS !$#gene ADH1 CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; NAD; oxidoreductase; zinc FEATURE !$31-338 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$46,69,156 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted SUMMARY #length 350 #molecular-weight 36879 #checksum 8325 SEQUENCE /// ENTRY DEZPA #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) - fission yeast (Schizosaccharomyces pombe) ORGANISM #formal_name Schizosaccharomyces pombe DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 05-May-2000 ACCESSIONS A00341; T40962 REFERENCE A00341 !$#authors Russell, P.R.; Hall, B.D. !$#journal J. Biol. Chem. (1983) 258:143-149 !$#title The primary structure of the alcohol dehydrogenase gene from !1the fission yeast Schizosaccharomyces pombe. !$#cross-references MUID:83082852; PMID:6294096 !$#accession A00341 !'##molecule_type DNA !'##residues 1-350 ##label RUS !'##cross-references GB:J01341; NID:g173343 !'##note this translation is not annotated in GenBank entry YSPADH, !1release 113.0 REFERENCE Z21960 !$#authors Purnelle, B.; Goffeau, A.; Lyne, M.; Rajandream, M.A.; !1Barrell, B.G. !$#submission submitted to the EMBL Data Library, October 1998 !$#accession T40962 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-236,'A',238-350 ##label PUR !'##cross-references EMBL:AL032681; PIDN:CAA21782.1; GSPDB:GN00068; !1SPDB:SPCC13B11.01 !'##experimental_source strain 972h-; cosmid c13B11 GENETICS !$#gene SPDB:SPCC13B11.01 !$#map_position 3 CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; metalloprotein; NAD; oxidoreductase; !1zinc FEATURE !$31-338 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$175-204 #region beta-alpha-beta NAD nucleotide-binding fold\ !$46,69,156 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$100,103,106,114 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 350 #molecular-weight 37428 #checksum 1180 SEQUENCE /// ENTRY S62746 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) B - Emericella nidulans ALTERNATE_NAMES alcohol dehydrogenase (EC 1.1.1.1) II ORGANISM #formal_name Emericella nidulans, Aspergillus nidulans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S62746 REFERENCE S62746 !$#authors Hunter, G.D.; Jones, I.G.; Sealy-Lewis, H.M. !$#journal Curr. Genet. (1996) 29:122-129 !$#title The cloning and sequencing of the alcB gene, coding for !1alcohol dehydrogenase II, in Aspergillus nidulans. !$#cross-references MUID:96418873; PMID:8821658 !$#accession S62746 !'##status preliminary !'##molecule_type DNA !'##residues 1-367 ##label HUN !'##cross-references EMBL:Z48000; NID:g1149565; PIDN:CAA88034.1; !1PID:g1149566 GENETICS !$#introns 42/2; 58/3; 111/1 CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; metalloprotein; NAD; oxidoreductase; !1zinc FEATURE !$33-356 #domain long-chain alcohol dehydrogenase homology !8#label LADH SUMMARY #length 367 #molecular-weight 38775 #checksum 4346 SEQUENCE /// ENTRY A44245 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) - Sulfolobus solfataricus ORGANISM #formal_name Sulfolobus solfataricus DATE 10-Mar-1994 #sequence_revision 10-Mar-1994 #text_change 11-Jun-1999 ACCESSIONS A44245 REFERENCE A44245 !$#authors Ammendola, S.; Raia, C.A.; Caruso, C.; Camardella, L.; !1D'Auria, S.; De Rosa, M.; Rossi, M. !$#journal Biochemistry (1992) 31:12514-12523 !$#title Thermostable NAD(+)-dependent alcohol dehydrogenase from !1Sulfolobus solfataricus: gene and protein sequence !1determination and relationship to other alcohol !1dehydrogenases. !$#cross-references MUID:93099126; PMID:1463738 !$#accession A44245 !'##molecule_type DNA !'##residues 1-347 ##label AMM !'##cross-references GB:S51211; NID:g261968; PIDN:AAB24546.1; !1PID:g261969 !'##experimental_source strain DSM1617 !'##note sequence extracted from NCBI backbone (NCBIN:120928, !1NCBIP:120938) !'##note part of this sequence was confirmed by protein sequencing COMPLEX homodimer FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; heat-stable protein; homodimer; !1metalloprotein; methylated amino acid; NAD; oxidoreductase; !1zinc FEATURE !$23-337 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$174-203 #region beta-alpha-beta NAD nucleotide-binding fold\ !$11,213 #modified_site N6-methyllysine (Lys) (partial) !8#status experimental\ !$38,68,154 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$98,101,104,112 #binding_site zinc, noncatalytic (Glu, Cys, Cys, Cys) !8#status predicted SUMMARY #length 347 #molecular-weight 37568 #checksum 427 SEQUENCE /// ENTRY S51120 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) - Sulfolobus sp. ORGANISM #formal_name Sulfolobus sp. DATE 19-Mar-1997 #sequence_revision 09-May-1997 #text_change 11-Jun-1999 ACCESSIONS S51120 REFERENCE S51120 !$#authors Cannio, R.; Fiorentino, G.; Carpinelli, P.; Rossi, M.; !1Bartolucci, S. !$#submission submitted to the EMBL Data Library, January 1995 !$#description Cloning and overexpression in Escherichia coli of the genes !1encoding NAD-dependent alcohol dehydrogenase from two !1Sulfolobus species. !$#accession S51120 !'##molecule_type DNA !'##residues 1-347 ##label CAN !'##cross-references EMBL:Z47543; NID:g623347; PIDN:CAA87591.1; !1PID:g623348 !'##experimental_source strain RC3 COMPLEX homodimer FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; heat-stable protein; homodimer; !1metalloprotein; methylated amino acid; NAD; oxidoreductase; !1zinc FEATURE !$23-337 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$174-203 #region beta-alpha-beta NAD nucleotide-binding fold\ !$11,213 #modified_site N6-methyllysine (Lys) #status !8predicted\ !$38,68,154 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$98,101,104,112 #binding_site zinc, noncatalytic (Glu, Cys, Cys, Cys) !8#status predicted SUMMARY #length 347 #molecular-weight 37583 #checksum 128 SEQUENCE /// ENTRY D69583 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) adhB - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS D69583 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D69583 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-378 ##label KUN !'##cross-references GB:Z99117; GB:AL009126; NID:g2634966; !1PIDN:CAB14638.1; PID:g2635142 !'##experimental_source strain 168 GENETICS !$#gene adhB FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; metalloprotein; NAD; oxidoreductase; !1zinc FEATURE !$23-367 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$181-210 #region beta-alpha-beta NAD nucleotide-binding fold\ !$38,60,162 #binding_site zinc, catalytic (Cys, His, Asp) #status !8predicted\ !$90,93,96,104 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 378 #molecular-weight 41196 #checksum 2919 SEQUENCE /// ENTRY S19417 #type complete TITLE alcohol dehydrogenase (NADP) (EC 1.1.1.2) homolog YCR105w - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YCR105w ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Jun-2002 ACCESSIONS S19417 REFERENCE S19415 !$#authors van der Linden, C.G.; Maurer, C.T.C.; Planta, R.J.; van !1Vliet-Reedijk, J.C.; Vreken, P. !$#submission submitted to the Protein Sequence Database, March 1992 !$#accession S19417 !'##molecule_type DNA !'##residues 1-361 ##label LIN !'##cross-references EMBL:X59720; NID:g1907116; PIDN:CAA42237.1; !1PID:g1907243; GSPDB:GN00003; MIPS:YCR105w COMMENT Although there is no direct evidence, this protein is most !1similar to members of this superfamily that use NADP rather !1than NAD as cofactor. GENETICS !$#gene MIPS:YCR105w !'##cross-references SGD:0000702 !$#map_position 3R CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; metalloprotein; NADP; oxidoreductase; !1zinc FEATURE !$31-344 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$183-212 #region beta-alpha-beta NADP nucleotide-binding fold\ !$46,68,164 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$100,103,106,114 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 361 #molecular-weight 39348 #checksum 109 SEQUENCE /// ENTRY S59311 #type complete TITLE alcohol dehydrogenase (NADP) (EC 1.1.1.2) homolog YMR318c - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein YM9924.10c ORGANISM #formal_name Saccharomyces cerevisiae DATE 29-Nov-1995 #sequence_revision 23-Feb-1996 #text_change 03-Jun-2002 ACCESSIONS S59311 REFERENCE S59302 !$#authors Churcher, C.M. !$#submission submitted to the EMBL Data Library, September 1995 !$#accession S59311 !'##molecule_type DNA !'##residues 1-360 ##label CHU !'##cross-references EMBL:Z54141; NID:g1072408; PIDN:CAA90836.1; !1PID:g984691; GSPDB:GN00013; MIPS:YMR318c !'##experimental_source strain AB972 COMMENT Although there is no direct evidence, this protein is most !1similar to members of this superfamily that use NADP rather !1than NAD as cofactor. GENETICS !$#gene MIPS:YMR318c !'##cross-references SGD:S0004937 !$#map_position 13R CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; metalloprotein; NADP; oxidoreductase; !1zinc FEATURE !$31-343 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$182-211 #region beta-alpha-beta NADP nucleotide-binding fold\ !$46,68,163 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$100,103,106,114 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 360 #molecular-weight 39617 #checksum 2758 SEQUENCE /// ENTRY S28043 #type complete TITLE cinnamyl-alcohol dehydrogenase (EC 1.1.1.195) ELI3-2 - Arabidopsis thaliana ALTERNATE_NAMES protein F20D10.110 ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 15-Oct-1999 ACCESSIONS S28043; T05626 REFERENCE S28043 !$#authors Kiedrowski, S.; Kawalleck, P.; Hahlbrock, K.; Somssich, !1I.E.; Dangl, J.L. !$#journal EMBO J. (1992) 11:4677-4684 !$#title Rapid activation of a novel plant defense gene is strictly !1dependent on the Arabidopsis RPM1 disease resistance locus. !$#cross-references MUID:93099840; PMID:1464303 !$#accession S28043 !'##molecule_type mRNA !'##residues 1-359 ##label KIE !'##cross-references EMBL:X67815; NID:g16268; PIDN:CAA48026.1; !1PID:g16269 REFERENCE Z15420 !$#authors Bevan, M.; Wedler, H.; Kutzner, M.; Wambutt, R.; Bancroft, !1I.; Mewes, H.W.; Mayer, K.F.X.; Schueller, C. !$#submission submitted to the Protein Sequence Database, February 1999 !$#accession T05626 !'##molecule_type DNA !'##residues 1-359 ##label BEV !'##cross-references EMBL:AL035538 !'##experimental_source cultivar Columbia; BAC clone F20D10 GENETICS !$#gene ELI3-2 !$#map_position 4 !$#introns 29/2; 67/2; 290/1 !$#note F20D10.110 CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; metalloprotein; oxidoreductase; zinc FEATURE !$31-339 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$46,68,162 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted SUMMARY #length 359 #molecular-weight 38942 #checksum 658 SEQUENCE /// ENTRY H64657 #type complete TITLE probable cinnamyl-alcohol dehydrogenase (EC 1.1.1.195) - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS H64657 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession H64657 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-348 ##label TOM !'##cross-references GB:AE000617; GB:AE000511; NID:g2314256; !1PIDN:AAD08150.1; PID:g2314257; TIGR:HP1104 CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; metalloprotein; oxidoreductase; zinc FEATURE !$27-333 #domain long-chain alcohol dehydrogenase homology !8#label LADH SUMMARY #length 348 #molecular-weight 38645 #checksum 8977 SEQUENCE /// ENTRY S76928 #type complete TITLE probable aryl alcohol dehydrogenase (EC 1.1.1.-) - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S76928 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76928 !'##molecule_type DNA !'##residues 1-336 ##label KAN !'##cross-references EMBL:D90917; GB:AB001339; NID:g1653836; !1PIDN:BAA18840.1; PID:g1653930 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS metalloprotein; NAD; oxidoreductase; zinc FEATURE !$24-323 #domain long-chain alcohol dehydrogenase homology !8#label LADH SUMMARY #length 336 #molecular-weight 35868 #checksum 9626 SEQUENCE /// ENTRY S56495 #type complete TITLE probable aryl alcohol dehydrogenase (EC 1.1.1.-) yjgB - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS S56495; H65239 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56495 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-353 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97166.1; !1PID:g537111 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65239 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-353 ##label BLAT !'##cross-references GB:AE000497; GB:U00096; NID:g1790711; !1PIDN:AAC77226.1; PID:g1790720; UWGP:b4269 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yjgB CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS metalloprotein; NAD; oxidoreductase; zinc FEATURE !$40-341 #domain long-chain alcohol dehydrogenase homology !8#label LADH SUMMARY #length 353 #molecular-weight 38153 #checksum 5894 SEQUENCE /// ENTRY DEECTH #type complete TITLE L-threonine 3-dehydrogenase (EC 1.1.1.103) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 01-Mar-2002 ACCESSIONS A33276; S47837; B65162; S69161; A30269 REFERENCE A33276 !$#authors Aronson, B.D.; Somerville, R.L.; Epperly, B.R.; Dekker, E.E. !$#journal J. Biol. Chem. (1989) 264:5226-5232 !$#title The primary structure of Escherichia coli L-threonine !1dehydrogenase. !$#cross-references MUID:89174812; PMID:2647748 !$#accession A33276 !'##molecule_type DNA !'##residues 1-341 ##label ARO !'##cross-references EMBL:X06690; NID:g41862; PIDN:CAA29884.1; !1PID:g41864 REFERENCE S47666 !$#authors Plunkett, G. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S47837 !'##molecule_type DNA !'##residues 1-341 ##label PLU !'##cross-references EMBL:U00039; NID:g466582; PIDN:AAB18593.1; !1PID:g466754 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65162 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-341 ##label BLAT !'##cross-references GB:AE000439; GB:U00096; NID:g1790036; !1PIDN:AAC76640.1; PID:g1790045; UWGP:b3616 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S69161 !$#authors Marcus, J.P.; Dekker, E.E. !$#journal Arch. Biochem. Biophys. (1995) 316:413-420 !$#title Identification of a second active site residue in !1Escherichia coli L-threonine dehydrogenase: methylation of !1histidine-90 with methyl p-nitrobenzenesulfonate. !$#cross-references MUID:95142657; PMID:7840645 !$#accession S69161 !'##molecule_type protein !'##residues 85-97 ##label MAR GENETICS !$#gene tdh !$#map_position 1 min COMPLEX homotetramer FUNCTION !$#description catalyzes oxidation of threonine by NAD+ to !12-amino-3-oxobutanoate, which spontaneously decarboxylates !1to aminoacetone CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS homotetramer; metalloprotein; NAD; oxidoreductase; zinc FEATURE !$23-331 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$166-195 #region beta-alpha-beta NAD nucleotide-binding fold\ !$38,90 #active_site Cys, His #status experimental\ !$38,63,148 #binding_site zinc, catalytic (Cys, His, Asp) #status !8predicted\ !$93,96,99,107 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 341 #molecular-weight 37239 #checksum 5810 SEQUENCE /// ENTRY JC5524 #type complete TITLE L-threonine 3-dehydrogenase (EC 1.1.1.103) - Xanthomonas campestris pv. campestris ORGANISM #formal_name Xanthomonas campestris pv. campestris DATE 02-Sep-1997 #sequence_revision 05-Sep-1997 #text_change 11-Jun-1999 ACCESSIONS JC5524; PC4438 REFERENCE JC5524 !$#authors Liu, Y.S.; Tseng, Y.H.; Lin, J.W.; Weng, S.F. !$#journal Biochem. Biophys. Res. Commun. (1997) 235:300-305 !$#title Molecular characterization of the gene coding for threonine !1dehydrogenase in Xanthomonas campestris. !$#cross-references MUID:97342489; PMID:9199186 !$#accession JC5524 !'##molecule_type DNA !'##residues 1-340 ##label LIU !'##cross-references GB:U96384; NID:g2228762; PIDN:AAC45449.1; !1PID:g2228763 REFERENCE PC4438 !$#authors Weng, S.F.; Liu, Y.S.; Lin, J.W.; Tseng, Y.H. !$#journal Biochem. Biophys. Res. Commun. (1997) 240:523-529 !$#title Transcriptional analysis of the threonine dehydrogenase gene !1of Xanthomonas campestris. !$#cross-references MUID:98063269; PMID:9398597 !$#accession PC4438 !'##molecule_type DNA !'##residues 'MAQT',1-30 ##label WEN GENETICS !$#gene tdh COMPLEX homotetramer FUNCTION !$#description catalyzes the oxidation of threonine by NAD+ to !12-amino-3-oxobutanoate, which spontaneously decarboxylates !1to aminoacetone CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS homotetramer; metalloprotein; NAD; oxidoreductase; zinc FEATURE !$23-330 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$166-195 #region beta-alpha-beta NAD nucleotide-binding fold\ !$38,63,148 #binding_site zinc, catalytic (Cys, His, Asp) #status !8predicted\ !$93,96,99,107 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 340 #molecular-weight 37044 #checksum 1714 SEQUENCE /// ENTRY C69721 #type complete TITLE L-threonine 3-dehydrogenase (EC 1.1.1.103) - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 05-Dec-1997 #sequence_revision 05-Dec-1997 #text_change 16-Jun-2000 ACCESSIONS C69721 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69721 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-347 ##label KUN !'##cross-references GB:Z99112; GB:AL009126; NID:g2633902; !1PIDN:CAB13572.1; PID:g2634071 !'##experimental_source strain 168 GENETICS !$#gene tdh COMPLEX homotetramer FUNCTION !$#description catalyzes the oxidation of threonine by NAD+ to !12-amino-3-oxobutanoate, which spontaneously decarboxylates !1to aminoacetone CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS homotetramer; metalloprotein; NAD; oxidoreductase; zinc FEATURE !$28-338 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$171-200 #region beta-alpha-beta NAD nucleotide-binding fold\ !$43,68,153 #binding_site zinc, catalytic (Cys, His, Glu) #status !8predicted\ !$98,101,104,112 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 347 #molecular-weight 36997 #checksum 2378 SEQUENCE /// ENTRY H64937 #type complete TITLE probable alcohol dehydrogenase (EC 1.1.1.-) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS H64937 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64937 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-358 ##label BLAT !'##cross-references GB:AE000272; GB:U00096; NID:g1788067; !1PIDN:AAC74846.1; PID:g1788075; UWGP:b1776 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS metalloprotein; NAD; oxidoreductase; zinc FEATURE !$24-345 #domain long-chain alcohol dehydrogenase homology !8#label LADH SUMMARY #length 358 #molecular-weight 38731 #checksum 7310 SEQUENCE /// ENTRY F64794 #type complete TITLE probable alcohol dehydrogenase (EC 1.1.1.1) ybdR - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 12-Sep-1997 #sequence_revision 17-Sep-1997 #text_change 01-Mar-2002 ACCESSIONS F64794 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64794 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-412 ##label BLAT !'##cross-references GB:AE000166; GB:U00096; NID:g1786819; !1PIDN:AAC73709.1; PID:g1786825; UWGP:b0608 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ybdR CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; metalloprotein; NAD; oxidoreductase; !1zinc FEATURE !$23-377 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$189-218 #region beta-alpha-beta NAD nucleotide-binding fold\ !$38,60,170 #binding_site zinc, catalytic (Cys, His, Asp) #status !8predicted\ !$90,93,96,104 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 412 #molecular-weight 44175 #checksum 2095 SEQUENCE /// ENTRY F70090 #type complete TITLE probable formaldehyde dehydrogenase (EC 1.2.1.46) yycR - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS F70090 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F70090 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-408 ##label KUN !'##cross-references GB:Z99124; GB:AL009126; NID:g2636442; !1PIDN:CAB16062.1; PID:g2636572 !'##experimental_source strain 168 GENETICS !$#gene yycR CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS oxidoreductase FEATURE !$46-394 #domain long-chain alcohol dehydrogenase homology !8#label LADH SUMMARY #length 408 #molecular-weight 42947 #checksum 4709 SEQUENCE /// ENTRY A30196 #type complete TITLE probable alcohol dehydrogenase (EC 1.1.1.1) - Alcaligenes eutrophus ORGANISM #formal_name Alcaligenes eutrophus DATE 18-Oct-1989 #sequence_revision 30-Sep-1991 #text_change 08-Dec-2000 ACCESSIONS A30196 REFERENCE A30196 !$#authors Jendrossek, D.; Steinbuechel, A.; Schlegel, H.G. !$#journal J. Bacteriol. (1988) 170:5248-5256 !$#title Alcohol dehydrogenase gene from Alcaligenes eutrophus: !1subcloning, heterologous expression in Escherichia coli, !1sequencing, and location of Tn5 insertions. !$#cross-references MUID:89033912; PMID:2846513 !$#accession A30196 !'##molecule_type DNA !'##residues 1-366 ##label JEN !'##cross-references GB:M22342 !'##note the authors translated the codon CAC for residue 185 as Asp FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NAD+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; NAD; oxidoreductase; zinc FEATURE !$26-354 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$186-215 #region beta-alpha-beta NAD nucleotide-binding fold\ !$41,62,167 #binding_site zinc, catalytic (Cys, His, Asp) #status !8predicted SUMMARY #length 366 #molecular-weight 38566 #checksum 3158 SEQUENCE /// ENTRY S34613 #type complete TITLE 5-exo-hydroxycamphor dehydrogenase (EC 1.1.1.-) - Pseudomonas putida plasmid CAM ORGANISM #formal_name Pseudomonas putida DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S34613; A29844 REFERENCE S34613 !$#authors Aramaki, H.; Koga, H.; Sagara, Y.; Hosoi, M.; Horiuchi, T. !$#journal Biochim. Biophys. Acta (1993) 1174:91-94 !$#title Complete nucleotide sequence of the 5-exo-hydroxycamphor !1dehydrogenase gene on the CAM plasmid of Pseudomonas putida !1(ATCC 17453). !$#cross-references MUID:93326643; PMID:8334169 !$#accession S34613 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-361 ##label ARA !'##cross-references GB:D14680; GB:D14452; GB:D14453; NID:g473744 !'##experimental_source PpG1; ATCC 17453; CAM plasmid REFERENCE A29844 !$#authors Koga, H.; Aramaki, H.; Yamaguchi, E.; Takeuchi, K.; !1Horiuchi, T.; Gunsalus, I.C. !$#journal J. Bacteriol. (1986) 166:1089-1095 !$#title camR, a negative regulator locus of the cytochrome P-450-cam !1hydroxylase operon. !$#cross-references MUID:86223770; PMID:3011733 !$#accession A29844 !'##molecule_type DNA !'##residues 1-96,'RAIAV' ##label KOG !'##cross-references GB:M13471; NID:g151117 !'##note this sequence has been revised in reference S34613 GENETICS !$#gene camD !$#genome plasmid COMPLEX homodimer FUNCTION !$#description catalyzes formation of 2,5-diketo-camphane from !15-exo-hydroxycamphor CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS NAD; oxidoreductase; zinc FEATURE !$25-350 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$178-207 #region beta-alpha-beta NAD nucleotide-binding fold\ !$40,62,158 #binding_site zinc, catalytic (Cys, His, Cys) #status !8predicted\ !$98,101,104,112 #binding_site zinc, noncatalytic (Cys) #status !8predicted SUMMARY #length 361 #molecular-weight 38377 #checksum 992 SEQUENCE /// ENTRY S73604 #type complete TITLE alcohol dehydrogenase (NADP) (EC 1.1.1.2) - Mycoplasma pneumoniae (strain ATCC 29342) ALTERNATE_NAMES hypothetical protein H03_orf351 ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 27-Feb-1997 #sequence_revision 25-Apr-1997 #text_change 03-Jun-2002 ACCESSIONS S73604 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73604 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-351 ##label HIM !'##cross-references EMBL:AE000027; GB:U00089; NID:g1673941; !1PIDN:AAB95926.1; PID:g1673949 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#gene adh !$#genetic_code SGC3 COMPLEX homotetramer FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NADP+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; homotetramer; NADP; oxidoreductase; zinc FEATURE !$22-340 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$169-198 #region beta-alpha-beta NADP nucleotide-binding fold\ !$37,59,150 #binding_site zinc, catalytic (Cys, His, Asp) #status !8predicted SUMMARY #length 351 #molecular-weight 37812 #checksum 1486 SEQUENCE /// ENTRY S71131 #type complete TITLE alcohol dehydrogenase (NADP) (EC 1.1.1.2) - Thermoanaerobacter ethanolicus ALTERNATE_NAMES secondary-alcohol dehydrogenase ORGANISM #formal_name Thermoanaerobacter ethanolicus DATE 19-Mar-1997 #sequence_revision 19-Mar-1997 #text_change 03-Jun-2002 ACCESSIONS S71131 REFERENCE S71131 !$#authors Burdette, D.S.; Vieille, C.; Zeikus, J.G. !$#journal Biochem. J. (1996) 316:115-122 !$#title Cloning and expression of the gene encoding the !1Thermoanaerobacter ethanolicus 39E secondary-alcohol !1dehydrogenase and biochemical characterization of the !1enzyme. !$#cross-references MUID:96235180; PMID:8645192 !$#accession S71131 !'##molecule_type DNA !'##residues 1-352 ##label BUR !'##cross-references EMBL:U49975; NID:g1513070; PIDN:AAB06720.1; !1PID:g1513071 !'##experimental_source strain 39E; ATCC 33223 COMMENT This protein is more active toward secondary than primary !1alcohols and is inhibited by pyrazole. GENETICS !$#gene adhB COMPLEX homotetramer FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NADP+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; heat-stable protein; homotetramer; NADP; !1oxidoreductase; zinc FEATURE !$22-339 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$169-198 #region beta-alpha-beta NADP nucleotide-binding fold\ !$37,59,150 #binding_site zinc, catalytic (Cys, His, Asp) #status !8predicted SUMMARY #length 352 #molecular-weight 37590 #checksum 1477 SEQUENCE /// ENTRY A32973 #type complete TITLE alcohol dehydrogenase (NADP) (EC 1.1.1.2) - Thermoanaerobacter brockii ALTERNATE_NAMES secondary-alcohol dehydrogenase ORGANISM #formal_name Thermoanaerobacter brockii DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 03-Jun-2002 ACCESSIONS A32973 REFERENCE A32973 !$#authors Peretz, M.; Burstein, Y. !$#journal Biochemistry (1989) 28:6549-6555 !$#title Amino acid sequence of alcohol dehydrogenase from the !1thermophilic bacterium Thermoanaerobium brockii. !$#cross-references MUID:90001210; PMID:2790012 !$#accession A32973 !'##molecule_type protein !'##residues 1-352 ##label PER COMMENT The functional enzyme is stable at high temperature (up to !185 degrees Centigrade). COMMENT This protein is more active toward secondary than primary !1alcohols and is inhibited by pyrazole. COMPLEX homotetramer FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NADP+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; heat-stable protein; homotetramer; NADP; !1oxidoreductase; zinc FEATURE !$22-339 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$169-198 #region beta-alpha-beta NADP nucleotide-binding fold\ !$37,59,150 #binding_site zinc, catalytic (Cys, His, Asp) #status !8predicted SUMMARY #length 352 #molecular-weight 37647 #checksum 1403 SEQUENCE /// ENTRY A46409 #type complete TITLE alcohol dehydrogenase (NADP) (EC 1.1.1.2) - Entamoeba histolytica ORGANISM #formal_name Entamoeba histolytica DATE 19-Nov-1993 #sequence_revision 18-Nov-1994 #text_change 03-Jun-2002 ACCESSIONS A46409 REFERENCE A46409 !$#authors Kumar, A.; Shen, P.S.; Descoteaux, S.; Pohl, J.; Bailey, G.; !1Samuelson, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:10188-10192 !$#title Cloning and expression of an NADP(+)-dependent alcohol !1dehydrogenase gene of Entamoeba histolytica. !$#cross-references MUID:93066205; PMID:1438208 !$#accession A46409 !'##molecule_type mRNA !'##residues 1-360 ##label KUM !'##cross-references GB:M88600; NID:g158917; PIDN:AAA51479.1; !1PID:g158918 !'##experimental_source HM-1:IHSS !'##note sequence extracted from NCBI backbone (NCBIP:117664) COMMENT This protein is more active toward secondary than primary !1alcohols and is inhibited by pyrazole. COMPLEX homotetramer FUNCTION !$#description catalyzes the oxidation of primary and secondary alcohols to !1aldehydes and ketones, respectively, by NADP+ !$#pathway alcohol degradation CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; homotetramer; NADP; oxidoreductase; zinc FEATURE !$22-339 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$169-198 #region beta-alpha-beta NADP nucleotide-binding fold\ !$37,59,150 #binding_site zinc, catalytic (Cys, His, Asp) #status !8predicted SUMMARY #length 360 #molecular-weight 38567 #checksum 8624 SEQUENCE /// ENTRY PN0448 #type complete TITLE zeta-crystallin / quinone reductase (NADPH) (EC 1.6.-.-) - human ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1993 #sequence_revision 07-Jul-1995 #text_change 11-Jun-1999 ACCESSIONS PN0448; A54672 REFERENCE PN0448 !$#authors Gonzalez, P.; Rao, P.V.; Zigler Jr., J.S. !$#journal Biochem. Biophys. Res. Commun. (1993) 191:902-907 !$#title Molecular cloning and sequencing of zeta-crystallin/quinone !1reductase cDNA from human liver. !$#cross-references MUID:93221534; PMID:8466529 !$#accession PN0448 !'##molecule_type mRNA !'##residues 1-329 ##label GON !'##cross-references GB:S58039; NID:g299369; PIDN:AAB26039.1; !1PID:g299370 !'##experimental_source liver !'##note translation of initiator Met is not shown; the authors !1translated the codon ATC for residue 141 as Thr REFERENCE A54672 !$#authors Gonzalez, P.; Rao, P.V.; Zigler Jr., J.S. !$#journal Genomics (1994) 21:317-324 !$#title Organization of the human zeta-crystallin/quinone reductase !1gene (CRYZ). !$#cross-references MUID:94375054; PMID:8088825 !$#accession A54672 !'##status preliminary !'##molecule_type DNA !'##residues 1-37 ##label GO2 !'##cross-references GB:L31521 COMMENT This protein is present at low (enzymatic) levels in this !1species, in contrast to species such as rodents and camels !1where the enzyme serves also as a major structural protein !1of the lens. GENETICS !$#gene GDB:CRYZ !'##cross-references GDB:139194; OMIM:123691 !$#map_position 1p31-1p22 CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS eye lens; NADP; oxidoreductase FEATURE !$33-318 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$152-181 #region beta-alpha-beta NADP nucleotide-binding fold SUMMARY #length 329 #molecular-weight 35206 #checksum 7775 SEQUENCE /// ENTRY CYGPZ #type complete TITLE zeta-crystallin / quinone reductase (NADPH) (EC 1.6.-.-) - guinea pig ALTERNATE_NAMES quinone reductase (NADP) ORGANISM #formal_name Cavia porcellus #common_name guinea pig DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 11-Jun-1999 ACCESSIONS JS0230 REFERENCE JS0230 !$#authors Rodokanaki, A.; Holmes, R.K.; Borras, T. !$#journal Gene (1989) 78:215-224 !$#title Zeta-crystallin, a novel protein from the guinea pig lens is !1related to alcohol dehydrogenases. !$#cross-references MUID:89378748; PMID:2777081 !$#accession JS0230 !'##molecule_type mRNA !'##residues 1-329 ##label ROD !'##cross-references GB:M26936; NID:g191252; PIDN:AAA37035.1; !1PID:g305333 !'##experimental_source strain 13/N !'##note the sequences of seven fragments (79-98, 95-106, 106-114, !1209-215, 264-275, 291-324, and 292-305) coincide with the !1sequence presented here !'##note this protein is distantly related to mammalian and yeast !1alcohol dehydrogenases COMMENT This protein constitutes about 10% of the water-soluble !1proteins of the lens. It is expressed at enzymatic levels in !1other tissues from a different promoter. CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS eye lens; NADP; oxidoreductase FEATURE !$33-318 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$152-181 #region beta-alpha-beta NADP nucleotide-binding fold SUMMARY #length 329 #molecular-weight 35202 #checksum 1588 SEQUENCE /// ENTRY A54932 #type complete TITLE zeta-crystallin / quinone reductase (NADPH) (EC 1.6.-.-) - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 25-Apr-1995 #sequence_revision 07-Jul-1995 #text_change 11-Jun-1999 ACCESSIONS A54932; S42273 REFERENCE A54932 !$#authors Gonzalez, P.; Hernandez-Calzadilla, C.; Rao, P.V.; !1Rodriguez, I.R.; Zigler Jr., J.S.; Borras, T. !$#journal Mol. Biol. Evol. (1994) 11:305-315 !$#title Comparative analysis of the zeta-crystallin/quinone !1reductase gene in guinea pig and mouse. !$#cross-references MUID:94224126; PMID:8170370 !$#accession A54932 !'##molecule_type mRNA !'##residues 1-331 ##label GON !'##cross-references GB:S70056; NID:g546493; PIDN:AAB30620.1; !1PID:g546494 !'##experimental_source liver !'##note sequence extracted from NCBI backbone (NCBIN:147625, !1NCBIP:147626) !'##note translation of initiator Met is not shown REFERENCE S42272 !$#authors Joernvall, H.; Persson, B.; du Bois, G.C.; Lavers, G.C.; !1Chen, J.H.; Gonzalez, P.; Rao, P.V.; Zigler Jr., J.S. !$#journal FEBS Lett. (1993) 322:240-244 !$#title zeta-Crystallin versus other members of the alcohol !1dehydrogenase super-family. Variability as a functional !1characteristic. !$#cross-references MUID:93252077; PMID:8486156 !$#contents annotation COMMENT This protein is a major soluble protein of the lens in this !1species and is expressed at low (enzymatic) levels in !1certain tissues. CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS eye lens; NADP; oxidoreductase FEATURE !$33-320 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$152-181 #region beta-alpha-beta NADP nucleotide-binding fold SUMMARY #length 331 #molecular-weight 35268 #checksum 5374 SEQUENCE /// ENTRY S45529 #type complete TITLE NADPH2:quinone reductase (EC 1.6.5.5) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S45529; B65213 REFERENCE S45528 !$#authors Dixon, N.E.; Lilley, P.E. !$#submission submitted to the EMBL Data Library, September 1992 !$#description E. coli homolog of zeta crystallin. !$#accession S45529 !'##molecule_type DNA !'##residues 1-327 ##label DIX !'##cross-references EMBL:L02312; NID:g145764; PIDN:AAA23691.1; !1PID:g145766 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65213 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-327 ##label BLAT !'##cross-references GB:AE000478; GB:U00096; NID:g2367339; !1PIDN:AAC77021.1; PID:g1790485; UWGP:b4051 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene qor CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS NADP; oxidoreductase FEATURE !$26-317 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$144-173 #region beta-alpha-beta NADP nucleotide-binding fold SUMMARY #length 327 #molecular-weight 35172 #checksum 6217 SEQUENCE /// ENTRY S52923 #type complete TITLE NADPH2:quinone reductase (EC 1.6.5.5) - Pseudomonas aeruginosa ORGANISM #formal_name Pseudomonas aeruginosa DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S52923 REFERENCE S52923 !$#authors Hungerer, C.; Troup, B.; Jahn, D. !$#submission submitted to the EMBL Data Library, February 1995 !$#description Cloning and regulation of the Pseudomonas aeruginosa hemF !1gene encoding oxygen-dependent coproporphyrinogen III !1oxidase. !$#accession S52923 !'##status preliminary !'##molecule_type DNA !'##residues 1-325 ##label HUN !'##cross-references EMBL:X85015; NID:g747872; PIDN:CAA59375.1; !1PID:g695692 CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS oxidoreductase FEATURE !$26-314 #domain long-chain alcohol dehydrogenase homology !8#label LADH SUMMARY #length 325 #molecular-weight 35034 #checksum 251 SEQUENCE /// ENTRY S45904 #type complete TITLE probable NADPH2:quinone reductase (EC 1.6.5.5) YBR046c - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein YBR0421 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S45904 REFERENCE S45893 !$#authors Andre, B.; Cziepluch, C.; Hein, C.; Jauniaux, J.C.; !1Urrestarazu, A.; Vissers, S. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S45904 !'##molecule_type DNA !'##residues 1-334 ##label AND !'##cross-references EMBL:Z35915; NID:g536273; PIDN:CAA84988.1; !1PID:g536274; GSPDB:GN00002; MIPS:YBR046c !'##experimental_source strain S288C GENETICS !$#gene SGD:ZTA1; MIPS:YBR046c !'##cross-references SGD:S0000250; MIPS:YBR046c !$#map_position 2R CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS oxidoreductase FEATURE !$33-322 #domain long-chain alcohol dehydrogenase homology !8#label LADH SUMMARY #length 334 #molecular-weight 37018 #checksum 7620 SEQUENCE /// ENTRY JQ0121 #type complete TITLE 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide a dehydrogenase (EC 1.1.1.-) - Rhodobacter capsulatus ORGANISM #formal_name Rhodobacter capsulatus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JQ0121; S04902; A49850 REFERENCE JQ0121 !$#authors Wellington, C.L.; Beatty, J.T. !$#journal Gene (1989) 83:251-261 !$#title Promoter mapping and nucleotide sequence of the bchC !1bacteriochlorophyll biosynthesis gene from Rhodobacter !1capsulatus. !$#cross-references MUID:90060837; PMID:2555268 !$#accession JQ0121 !'##molecule_type DNA !'##residues 1-314 ##label WEL !'##cross-references GB:M29966; NID:g151885; PIDN:AAA26096.1; !1PID:g151887; GB:Z11165; NID:g46097; PIDN:CAA77547.1; !1PID:g46130 REFERENCE S04901 !$#authors Young, D.A.; Bauer, C.E.; Williams, J.A.C.; Marrs, B.L. !$#journal Mol. Gen. Genet. (1989) 218:1-12 !$#title Genetic evidence for superoperonal organization of genes for !1photosynthetic pigments and pigment-binding proteins in !1Rhodobacter capsulatus. !$#cross-references MUID:89384422; PMID:2550757 !$#accession S04902 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-120 ##label YOU !'##cross-references GB:X16164; NID:g45991 REFERENCE A49850 !$#authors Burke, D.H.; Alberti, M.; Hearst, J.E. !$#journal J. Bacteriol. (1993) 175:2407-2413 !$#title The Rhodobacter capsulatus chlorin reductase-encoding locus, !1bchA, consists of three genes, bchX, bchY, and bchZ. !$#cross-references MUID:93224464; PMID:8468299 !$#accession A49850 !'##status preliminary !'##molecule_type DNA !'##residues 283-314 ##label BUR !'##experimental_source SB1003 !'##note sequence extracted from NCBI backbone (NCBIN:129230, !1NCBIP:129231) GENETICS !$#gene bchC FUNCTION !$#description catalyzes the penultimate step in bacteriochlorophyll a !1biosynthesis. CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS bacteriochlorophyll a biosynthesis; NAD; oxidoreductase FEATURE !$24-300 #domain long-chain alcohol dehydrogenase homology !8#label LADH SUMMARY #length 314 #molecular-weight 33010 #checksum 1497 SEQUENCE /// ENTRY S30914 #type complete TITLE 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide a dehydrogenase (EC 1.1.1.-) - Rhodobacter sphaeroides ORGANISM #formal_name Rhodobacter sphaeroides DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S30914; S28269; S32850 REFERENCE S30914 !$#authors McGlynn, P.; Hunter, C.N. !$#journal Mol. Gen. Genet. (1993) 236:227-234 !$#title Genetic analysis of the bchC and bchA genes of Rhodobacter !1sphaeroides. !$#cross-references MUID:93173096; PMID:8437569 !$#accession S30914 !'##molecule_type DNA !'##residues 1-318 ##label MCG !'##cross-references EMBL:X68795; NID:g49170; PID:g581530 GENETICS !$#gene bchC !$#start_codon GTG CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS bacteriochlorophyll a biosynthesis; NAD; oxidoreductase FEATURE !$27-304 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$152-181 #region beta-alpha-beta NAD nucleotide-binding fold SUMMARY #length 318 #molecular-weight 34046 #checksum 5323 SEQUENCE /// ENTRY F69905 #type complete TITLE probable alcohol dehydrogenase (EC 1.1.1.-) yogA - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS F69905 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69905 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-329 ##label KUN !'##cross-references GB:Z99113; GB:Z99114; GB:AL009126; NID:g2634230; !1PIDN:CAB13736.1; PID:g2634237; NID:g2634090; PID:g2634226 !'##experimental_source strain 168 GENETICS !$#gene yogA CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS NAD; oxidoreductase FEATURE !$25-318 #domain long-chain alcohol dehydrogenase homology !8#label LADH SUMMARY #length 329 #molecular-weight 35811 #checksum 3508 SEQUENCE /// ENTRY C70418 #type complete TITLE probable alcohol dehydrogenase (EC 1.1.1.-) - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C70418 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession C70418 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-343 ##label AQF !'##cross-references GB:AE000736; NID:g2983763; PIDN:AAC07327.1; !1PID:g2983768; GB:AE000657 !'##experimental_source strain VF5 GENETICS !$#gene adh1 CLASSIFICATION #superfamily alcohol dehydrogenase; long-chain alcohol !1dehydrogenase homology KEYWORDS NAD; oxidoreductase FEATURE !$26-332 #domain long-chain alcohol dehydrogenase homology !8#label LADH SUMMARY #length 343 #molecular-weight 38043 #checksum 5763 SEQUENCE /// ENTRY S16453 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) - fruit fly (Drosophila ambigua) ORGANISM #formal_name Drosophila ambigua DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS S16453 REFERENCE S16453 !$#authors Marfany, G.; Gonzalez-Duarte, R. !$#journal J. Mol. Evol. (1991) 32:454-462 !$#title The Adh genomic region of Drosophila ambigua: evolutionary !1trends in different species. !$#cross-references MUID:91332913; PMID:1908016 !$#accession S16453 !'##molecule_type DNA !'##residues 1-254 ##label MAR !'##cross-references EMBL:X54813; NID:g7143; PIDN:CAA38581.1; PID:g7144 GENETICS !$#gene Adh !'##cross-references FlyBase:FBgn0012099 !$#introns 31/3; 166/3 CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; NAD; oxidoreductase FEATURE !$6-182 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 254 #molecular-weight 27618 #checksum 2018 SEQUENCE /// ENTRY DEFFA #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) [validated] - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 31-Mar-1981 #sequence_revision 19-Feb-1984 #text_change 03-Nov-2000 ACCESSIONS A93309; B93309; A93873; A93713; A90308; A93875; S17083; !1S17085; S17084; A37092; A00343 REFERENCE A93309 !$#authors Kreitman, M. !$#journal Nature (1983) 304:412-417 !$#title Nucleotide polymorphism at the alcohol dehydrogenase locus !1of Drosophila melanogaster. !$#cross-references MUID:83271489; PMID:6410283 !$#accession A93309 !'##molecule_type DNA !'##residues 1-256 ##label KRE1 !'##cross-references GB:Z00030; GB:J01066; GB:M14802; GB:V00197; !1GB:V00198; GB:V00199; NID:g7558; PIDN:CAA77330.1; !1PID:g599727 !'##experimental_source Adh-s allele !$#accession B93309 !'##molecule_type DNA !'##residues 1-192,'T',194-256 ##label KRE2 !'##cross-references GB:M17833; GB:K00651; NID:g156871; PIDN:AAA28346.1; !1PID:g156872 !'##experimental_source Adh-f allele !'##note virtually all natural populations of this species are !1polymorphic for two electrophoretically distinguishable !1alleles, Adh-s and Adh-f; these alleles differ in that the !1sequences from Adh-s strains have the codon AAG for 193-Lys !1whereas those from Adh-f strains have the codon ACG for !1193-Thr REFERENCE A93873 !$#authors Benyajati, C.; Place, A.R.; Powers, D.A.; Sofer, W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:2717-2721 !$#title Alcohol dehydrogenase gene of Drosophila melanogaster: !1relationship of intervening sequences to functional domains !1in the protein. !$#cross-references MUID:81247357; PMID:6789320 !$#accession A93873 !'##molecule_type mRNA !'##residues 1-256 ##label BEN1 !'##cross-references GB:Z00030; GB:J01066; GB:M14802; GB:V00197; !1GB:V00198; GB:V00199; NID:g7558; PIDN:CAA77330.1; !1PID:g599727 !'##experimental_source Adh-s allele REFERENCE A93713 !$#authors Benyajati, C.; Wang, N.; Reddy, A.; Weinberg, E.; Sofer, W. !$#journal Nucleic Acids Res. (1980) 8:5649-5667 !$#title Alcohol dehydrogenase in Drosophila: isolation and !1characterization of messenger RNA and cDNA clone. !$#cross-references MUID:81124290; PMID:6780981 !$#accession A93713 !'##molecule_type mRNA !'##residues 141-192,'T',194-256 ##label BEN2 !'##experimental_source Adh-f allele REFERENCE A90308 !$#authors Thatcher, D.R. !$#journal Biochem. J. (1980) 187:875-886 !$#title The complete amino acid sequence of three alcohol !1dehydrogenase alleloenzymes (Adh[N-11], Adh[S] and Adh[UF]) !1from the fruitfly Drosophila melanogaster. !$#cross-references MUID:84256516; PMID:6821373 !$#accession A90308 !'##molecule_type protein !'##residues 1-25,'Q',27-192,'T',194-256 ##label THA !'##experimental_source Adh-f allele REFERENCE A90310 !$#authors Thatcher, D.R. !$#journal Biochem. J. (1980) 191:895 !$#contents annotation; erratum REFERENCE A93875 !$#authors Chambers, G.K.; Laver, W.G.; Campbell, S.; Gibson, J.B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:3103-3107 !$#title Structural analysis of an electrophoretically cryptic !1alcohol dehydrogenase variant from an Australian population !1of Drosophila melanogaster. !$#cross-references MUID:81247428; PMID:6789328 !$#accession A93875 !'##molecule_type protein !'##residues 208-214,'S',216-225 ##label CHA !'##experimental_source Adh-fCh.D. allele REFERENCE S17083 !$#authors Laurie, C.C.; Bridgham, J.T.; Choudhary, M. !$#submission submitted to the EMBL Data Library, July 1991 !$#description Associations between DNA sequence variation and variation in !1expression of the Adh gene in natural populations of !1Drosophila melanogaster. !$#accession S17083 !'##molecule_type DNA !'##residues 1-192,'T',194-256 ##label LAU1 !'##cross-references EMBL:X60791; NID:g8151; PIDN:CAA43204.1; PID:g8152 !'##experimental_source strain KA12 !$#accession S17085 !'##molecule_type DNA !'##residues 1-192,'T',194-256 ##label LAU2 !'##cross-references EMBL:X60792; NID:g8440; PIDN:CAA43205.1; PID:g8441 !'##experimental_source strain RI32 !$#accession S17084 !'##molecule_type DNA !'##residues 1-45,'V',47-70,'S',72-256 ##label LAU3 !'##cross-references EMBL:X60793; NID:g8281; PIDN:CAA43206.1; PID:g8282 REFERENCE A37092 !$#authors Eisses, K.T.; Andriesse, A.J.; Douwe de Boer, A.; Thoerig, !1G.E.W.; Weisbeek, P.J. !$#journal Mol. Biol. Evol. (1990) 7:459-469 !$#title Analysis of the gene encoding the multifunctional alcohol !1dehydrogenase allozyme ADH-71k of Drosophila melanogaster. !$#cross-references MUID:91087763; PMID:2124644 !$#accession A37092 !'##molecule_type DNA !'##residues 1-192,'T',194-214,'S',216-256 ##label EIS !'##cross-references GB:M57239; GB:M34654; NID:g156797; PIDN:AAA28330.1; !1PID:g156800 COMMENT The sequence of the Adh-s allele is shown. GENETICS !$#gene Adh; ADH-71K; FlyBase:Adh !'##cross-references FlyBase:FBgn0000055 !$#map_position 2L,50.1 (35B2-35B3) !$#introns 33/3; 168/3 CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS acetylated amino end; alcohol metabolism; NAD; !1oxidoreductase FEATURE !$2-256 #product alcohol dehydrogenase #status experimental !8#label MAT\ !$8-184 #domain short-chain alcohol dehydrogenase homology !8#label SADH\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental SUMMARY #length 256 #molecular-weight 27761 #checksum 1862 SEQUENCE /// ENTRY S07439 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) - fruit fly (Drosophila sechellia) ORGANISM #formal_name Drosophila sechellia DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S07439 REFERENCE S07439 !$#authors Coyne, J.A.; Kreitman, M. !$#journal Evolution (1986) 40:673-691 !$#title Evolutionary genetics of two sibling species, Drosophila !1simulans and D. sechellia. !$#accession S07439 !'##molecule_type DNA !'##residues 1-256 ##label COY !'##cross-references EMBL:X04672; NID:g9105; PIDN:CAA28377.1; !1PID:g295759 GENETICS !$#gene Adh !'##cross-references FlyBase:FBgn0012780 !$#introns 33/3; 168/3 CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; NAD; oxidoreductase FEATURE !$8-184 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 256 #molecular-weight 27745 #checksum 1670 SEQUENCE /// ENTRY S18273 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) - fruit fly (Drosophila simulans) (isolate Australia, individual c and others) ORGANISM #formal_name Drosophila simulans #variety isolate Australia, individual c; isolate Ottawa, Canada, individual d; isolate France, individual e, isolate Brazzaville, Congo, individual f DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S18273; S18274; S18275; S18276; S07333; S07287 REFERENCE S18273 !$#authors McDonald, J.H.; Kreitman, M. !$#journal Nature (1991) 351:652-654 !$#title Adaptive protein evolution at the Adh locus in Drosophila. !$#cross-references MUID:91270370; PMID:1904993 !$#accession S18273 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-256 ##label MCD !'##cross-references EMBL:X57361; NID:g9097; PIDN:CAA40635.1; PID:g9098 !'##experimental_source isolate Australia, individual c !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1991 !$#accession S18274 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-256 ##label MCW !'##cross-references EMBL:X57362; NID:g9099; PIDN:CAA40636.1; PID:g9100 !'##experimental_source isolate Ottawa, Canada, individual d !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1991 !$#accession S18275 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-256 ##label MCF !'##cross-references EMBL:X57363; NID:g9101; PIDN:CAA40637.1; PID:g9102 !'##experimental_source isolate France, individual e !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1991 !$#accession S18276 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-256 ##label MCA !'##cross-references EMBL:X57364; NID:g9103; PIDN:CAA40638.1; PID:g9104 !'##experimental_source isolate Brazzaville, Congo, individual f !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1991 REFERENCE S07333 !$#authors Bodmer, M.; Ashburner, M. !$#journal Nature (1984) 309:425-430 !$#title Conservation and change in the DNA sequences coding for !1alcohol dehydrogenase in sibling species of Drosophila. !$#cross-references MUID:84219730; PMID:6427630 !$#accession S07333 !'##status translation not shown !'##molecule_type DNA !'##residues 1-88,'X',90-256 ##label BOD !'##cross-references EMBL:X00607 REFERENCE S07287 !$#authors Cohn, V.H.; Thompson, M.A.; Moore, G.P. !$#journal J. Mol. Evol. (1984) 20:31-37 !$#title Nucleotide sequence comparison of the Adh gene in three !1drosophilids. !$#cross-references MUID:84242854; PMID:6429340 !$#accession S07287 !'##status translation not shown !'##molecule_type DNA !'##residues 1-178,'X',180-189 ##label COH !'##cross-references EMBL:X00607 GENETICS !$#gene FlyBase:Adh !'##cross-references FlyBase:FBgn0013162; FlyBase:FBgn0012824 !$#introns 33/3; 168/3 CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; NAD; oxidoreductase FEATURE !$8-184 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 256 #molecular-weight 27745 #checksum 1670 SEQUENCE /// ENTRY S09633 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) - fruit fly (Drosophila mauritiana) ORGANISM #formal_name Drosophila mauritiana DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S09633; S09577 REFERENCE S07333 !$#authors Bodmer, M.; Ashburner, M. !$#journal Nature (1984) 309:425-430 !$#title Conservation and change in the DNA sequences coding for !1alcohol dehydrogenase in sibling species of Drosophila. !$#cross-references MUID:84219730; PMID:6427630 !$#accession S09633 !'##status translation not shown !'##molecule_type DNA !'##residues 1-256 ##label BOD !'##cross-references EMBL:Z00033; NID:g7556; PIDN:CAA77334.1; PID:g7557 REFERENCE S07287 !$#authors Cohn, V.H.; Thompson, M.A.; Moore, G.P. !$#journal J. Mol. Evol. (1984) 20:31-37 !$#title Nucleotide sequence comparison of the Adh gene in three !1drosophilids. !$#cross-references MUID:84242854; PMID:6429340 !$#accession S09577 !'##status translation not shown !'##molecule_type DNA !'##residues 1-178,'X',180-189 ##label COH !'##cross-references GB:M19275; EMBL:Z00033; NID:g156899; !1PIDN:AAA28361.1; PID:g156900 GENETICS !$#gene Adh !'##cross-references FlyBase:FBgn0012496 !$#introns 33/3; 168/3 CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; NAD; oxidoreductase FEATURE !$8-184 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 256 #molecular-weight 27761 #checksum 2412 SEQUENCE /// ENTRY S09634 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) - fruit fly (Drosophila orena) ORGANISM #formal_name Drosophila orena DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S09634 REFERENCE S07333 !$#authors Bodmer, M.; Ashburner, M. !$#journal Nature (1984) 309:425-430 !$#title Conservation and change in the DNA sequences coding for !1alcohol dehydrogenase in sibling species of Drosophila. !$#cross-references MUID:84219730; PMID:6427630 !$#accession S09634 !'##status translation not shown !'##molecule_type DNA !'##residues 1-256 ##label BOD !'##cross-references GB:M37837; EMBL:Z00032; NID:g8864; PIDN:CAA77332.1; !1PID:g8865 GENETICS !$#gene Adh !'##cross-references FlyBase:FBgn0012616 !$#introns 33/3; 168/3 CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; NAD; oxidoreductase FEATURE !$8-184 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 256 #molecular-weight 27719 #checksum 2432 SEQUENCE /// ENTRY DEFFRL #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) - fruit fly (Drosophila lebanonensis) ORGANISM #formal_name Drosophila lebanonensis DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 11-Jun-1999 ACCESSIONS S12695; S12613; JN0564; S03569 REFERENCE S12695 !$#authors Alabat, R.; Gonzalez-Duarte, R. !$#journal Nucleic Acids Res. (1990) 18:6706 !$#title Nucleotide sequence of the Adh gene of Drosophila !1lebanonensis. !$#cross-references MUID:91067480; PMID:2251140 !$#accession S12695 !'##molecule_type DNA !'##residues 1-254 ##label ALB !'##cross-references EMBL:X54814; NID:g7478; PIDN:CAA38583.1; PID:g7479 !'##note the first author's name has been corrected from Alabat to !1Albalat in reference S18005 REFERENCE S18805 !$#authors Albalat, R.; Gonzalez-Duarte, R. !$#journal Nucleic Acids Res. (1991) 19:424 !$#cross-references MUID:91195079; PMID:1849634 !$#contents annotation !$#note this corrects an author's name in reference S12695 REFERENCE S12613 !$#authors Juan, E.; Papaceit, M.; Quintana, A. !$#journal Nucleic Acids Res. (1990) 18:6420 !$#title Nucleotide sequence of the Adh gene of Drosophila !1lebanonensis. !$#cross-references MUID:91057126; PMID:2243785 !$#accession S12613 !'##molecule_type DNA !'##residues 1-254 ##label JUA !'##cross-references EMBL:X53429 !'##note the authors did not translate the codons for residues 32-49 and !1130 !'##note the authors translated the codon TAT for residue 177 as Thr REFERENCE JN0564 !$#authors Albalat, R.; Gonzalez-Duarte, R. !$#journal Gene (1993) 126:171-178 !$#title Adh and Adh-dup sequences of Drosophila lebanonensis and D. !1immigrans: interspecies comparisons. !$#cross-references MUID:93246241; PMID:8482531 !$#accession JN0564 !'##molecule_type DNA !'##residues 1-254 ##label AL2 !'##cross-references GB:M97637; NID:g304657; PIDN:AAA28355.1; !1PID:g304658 REFERENCE S03569 !$#authors Villarroya, A.; Juan, E.; Egestad, B.; Joernvall, H. !$#journal Eur. J. Biochem. (1989) 180:191-197 !$#title The primary structure of alcohol dehydrogenase from !1Drosophila lebanonensis. Extensive variation within insect !1'short-chain' alcohol dehydrogenase lacking zinc. !$#cross-references MUID:89210852; PMID:2707261 !$#accession S03569 !'##molecule_type protein !'##residues 1-254 ##label VIL COMMENT This enzyme shows a high level of activity in alcohol-rich !1environments. GENETICS !$#gene Adh !'##cross-references FlyBase:FBgn0012438 !$#introns 31/3; 166/3 CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS acetylated amino end; alcohol metabolism; NAD; !1oxidoreductase FEATURE !$1-254 #product alcohol dehydrogenase #status experimental !8#label MAT\ !$6-182 #domain short-chain alcohol dehydrogenase homology !8#label SADH\ !$1 #modified_site acetylated amino end (Met) #status !8experimental SUMMARY #length 254 #molecular-weight 27792 #checksum 8331 SEQUENCE /// ENTRY A40553 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) - fruit fly (Drosophila mettleri) ORGANISM #formal_name Drosophila mettleri DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A40553 REFERENCE A40553 !$#authors Yum, J.; Starmer, W.T.; Sullivan, D.T. !$#journal Mol. Biol. Evol. (1991) 8:857-867 !$#title The structure of the Adh locus of Drosophila mettleri: an !1intermediate in the evolution of the Adh locus in the !1repleta group of Drosophila. !$#cross-references MUID:92130806; PMID:1775067 !$#accession A40553 !'##status preliminary !'##molecule_type DNA !'##residues 1-254 ##label YUM !'##cross-references GB:M57300; NID:g156907; PIDN:AAA28364.1; !1PID:g156908 GENETICS !$#gene FlyBase:Dmet/Adh-1 !'##cross-references FlyBase:FBgn0012533 CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; NAD; oxidoreductase FEATURE !$6-182 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 254 #molecular-weight 27539 #checksum 8738 SEQUENCE /// ENTRY S15711 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) 2 - fruit fly (Drosophila hydei) ORGANISM #formal_name Drosophila hydei DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS S15711 REFERENCE S15711 !$#authors Menotti-Raymond, M.; Starmer, W.T.; Sullivan, D.T. !$#journal Genetics (1991) 127:355-366 !$#title Characterization of the structure and evolution of the Adh !1region of Drosophila hydei. !$#cross-references MUID:91169286; PMID:2004708 !$#accession S15711 !'##molecule_type DNA !'##residues 1-254 ##label MEN !'##cross-references EMBL:X58694; NID:g7424; PIDN:CAA41539.1; PID:g7425 GENETICS !$#gene Adh-2 !'##cross-references FlyBase:FBgn0012359 !$#introns 31/3; 166/3 CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; NAD; oxidoreductase FEATURE !$6-182 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 254 #molecular-weight 27414 #checksum 6928 SEQUENCE /// ENTRY S15712 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) 1 - fruit fly (Drosophila hydei) ORGANISM #formal_name Drosophila hydei DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS S15712 REFERENCE S15711 !$#authors Menotti-Raymond, M.; Starmer, W.T.; Sullivan, D.T. !$#journal Genetics (1991) 127:355-366 !$#title Characterization of the structure and evolution of the Adh !1region of Drosophila hydei. !$#cross-references MUID:91169286; PMID:2004708 !$#accession S15712 !'##molecule_type DNA !'##residues 1-254 ##label MEN !'##cross-references EMBL:X58694; NID:g7424; PIDN:CAA41540.1; PID:g7426 GENETICS !$#gene Adh-1 !'##cross-references FlyBase:FBgn0012358 !$#introns 31/3; 166/3 CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; NAD; oxidoreductase FEATURE !$6-182 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 254 #molecular-weight 27400 #checksum 7646 SEQUENCE /// ENTRY S06001 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) 1 - fruit fly (Drosophila navojoa) ORGANISM #formal_name Drosophila navojoa DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S06001 REFERENCE S06001 !$#authors Weaver, J.R.; Andrews, J.M.; Sullivan, D.T. !$#journal Nucleic Acids Res. (1989) 17:7524 !$#title Nucleotide sequence of the Adh-1 gene of Drosophila navojoa. !$#cross-references MUID:90016820; PMID:2798109 !$#accession S06001 !'##molecule_type DNA !'##residues 1-254 ##label WEA !'##cross-references EMBL:X15585; NID:g8861; PIDN:CAA33610.1; PID:g8862 GENETICS !$#gene FlyBase:Dnav/Adh-1 !'##cross-references FlyBase:FBgn0012589 !$#introns 31/3; 166/3 CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; NAD; oxidoreductase FEATURE !$6-182 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 254 #molecular-weight 27547 #checksum 8274 SEQUENCE /// ENTRY S01902 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) 1 - fruit fly (Drosophila mojavensis) ORGANISM #formal_name Drosophila mojavensis DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS S01902 REFERENCE S01901 !$#authors Atkinson, P.W.; Mills, L.E.; Starmer, W.T.; Sullivan, D.T. !$#journal Genetics (1988) 120:713-723 !$#title Structure and evolution of the Adh genes of Drosophila !1mojavensis. !$#cross-references MUID:89137903; PMID:3224808 !$#accession S01902 !'##molecule_type DNA !'##residues 1-254 ##label ATK !'##cross-references EMBL:X12536; NID:g7553; PIDN:CAA31055.1; PID:g7555 GENETICS !$#gene Adh-1 !'##cross-references FlyBase:FBgn0012566 !$#introns 31/3; 166/3 CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; NAD; oxidoreductase FEATURE !$6-182 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 254 #molecular-weight 27565 #checksum 7898 SEQUENCE /// ENTRY B24268 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) 2 - fruit fly (Drosophila mulleri) ORGANISM #formal_name Drosophila mulleri DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS B24268 REFERENCE A93592 !$#authors Fischer, J.A.; Maniatis, T. !$#journal Nucleic Acids Res. (1985) 13:6899-6917 !$#cross-references MUID:86041886; PMID:2997730 !$#accession B24268 !'##molecule_type DNA !'##residues 1-254 ##label FIS !'##cross-references GB:X03048; NID:g8769; PIDN:CAA26857.1; PID:g295758 !'##note the authors translated the codon ACC for residue 65 as Tyr and !1CTG for residue 188 as Lys GENETICS !$#gene Adh-1 !'##cross-references FlyBase:FBgn0012582 !$#introns 31/3; 166/3 CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; NAD; oxidoreductase FEATURE !$6-182 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 254 #molecular-weight 27494 #checksum 9601 SEQUENCE /// ENTRY A24268 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) 1 - fruit fly (Drosophila mulleri) ORGANISM #formal_name Drosophila mulleri DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS A24268 REFERENCE A93592 !$#authors Fischer, J.A.; Maniatis, T. !$#journal Nucleic Acids Res. (1985) 13:6899-6917 !$#cross-references MUID:86041886; PMID:2997730 !$#accession A24268 !'##molecule_type DNA !'##residues 1-254 ##label FIS !'##cross-references GB:X03048; NID:g8769; PIDN:CAA26856.1; PID:g295757 GENETICS !$#gene Adh-1 !'##cross-references FlyBase:FBgn0012581 !$#introns 31/3; 166/3 CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; NAD; oxidoreductase FEATURE !$6-182 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 254 #molecular-weight 27592 #checksum 8695 SEQUENCE /// ENTRY S01901 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) 2 - fruit fly (Drosophila mojavensis) ORGANISM #formal_name Drosophila mojavensis DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 03-Nov-2000 ACCESSIONS S01901; A45962 REFERENCE S01901 !$#authors Atkinson, P.W.; Mills, L.E.; Starmer, W.T.; Sullivan, D.T. !$#journal Genetics (1988) 120:713-723 !$#title Structure and evolution of the Adh genes of Drosophila !1mojavensis. !$#cross-references MUID:89137903; PMID:3224808 !$#accession S01901 !'##molecule_type DNA !'##residues 1-254 ##label ATK !'##cross-references EMBL:X12536; NID:g7553; PIDN:CAA31054.1; PID:g7554 REFERENCE A45962 !$#authors Mills, L.E.; Batterham, P.; Alegre, J.; Starmer, W.T.; !1Sullivan, D.T. !$#journal Genetics (1986) 112:295-310 !$#title Molecular genetic characterization of a locus that contains !1duplicate Adh genes in Drosophila mojavensis and related !1species. !$#cross-references MUID:86083142; PMID:3000866 !$#accession A45962 !'##status preliminary !'##molecule_type DNA !'##residues 167-201,'L',203-249,'S',251-254 ##label MIL !'##cross-references GB:X03630; NID:g8302; PIDN:CAA27280.1; PID:g666992 GENETICS !$#gene Adh-2 !'##cross-references FlyBase:FBgn0012567 !$#introns 31/3; 166/3 CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; NAD; oxidoreductase FEATURE !$6-182 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 254 #molecular-weight 27514 #checksum 8887 SEQUENCE /// ENTRY B23724 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) - fruit fly (Drosophila picticornis) ORGANISM #formal_name Drosophila picticornis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 02-Nov-2001 ACCESSIONS B23724 REFERENCE A23724 !$#authors Rowan, R.G.; Hunt, J.A. !$#journal Mol. Biol. Evol. (1991) 8:49-70 !$#title Rates of DNA change and phylogeny from the DNA sequences of !1the alcohol dehydrogenase gene for five closely related !1species of Hawaiian Drosophila. !$#cross-references MUID:91163323; PMID:2002765 !$#accession B23724 !'##status preliminary !'##molecule_type DNA !'##residues 1-223 ##label RO2 !'##note the protein translation is not shown in this reference GENETICS !$#gene FlyBase:Dpic/Adh !'##cross-references FlyBase:FBgn0012651 CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; NAD; oxidoreductase FEATURE !$1-151 #domain short-chain alcohol dehydrogenase homology !8#status atypical #label SADH SUMMARY #length 223 #molecular-weight 24446 #checksum 4664 SEQUENCE /// ENTRY C23724 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) - fruit fly (Drosophila planitibia) ORGANISM #formal_name Drosophila planitibia DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 02-Nov-2001 ACCESSIONS C23724 REFERENCE A23724 !$#authors Rowan, R.G.; Hunt, J.A. !$#journal Mol. Biol. Evol. (1991) 8:49-70 !$#title Rates of DNA change and phylogeny from the DNA sequences of !1the alcohol dehydrogenase gene for five closely related !1species of Hawaiian Drosophila. !$#cross-references MUID:91163323; PMID:2002765 !$#accession C23724 !'##status preliminary !'##molecule_type DNA !'##residues 1-223 ##label RO3 GENETICS !$#gene FlyBase:Dpla/Adh !'##cross-references FlyBase:FBgn0012666 !$#start_codon AAC !$#introns 135/3 CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; NAD; oxidoreductase FEATURE !$1-151 #domain short-chain alcohol dehydrogenase homology !8#status atypical #label SADH SUMMARY #length 223 #molecular-weight 24328 #checksum 5929 SEQUENCE /// ENTRY E23724 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) - fruit fly (Drosophila differens) ORGANISM #formal_name Drosophila differens DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS E23724 REFERENCE A23724 !$#authors Rowan, R.G.; Hunt, J.A. !$#journal Mol. Biol. Evol. (1991) 8:49-70 !$#title Rates of DNA change and phylogeny from the DNA sequences of !1the alcohol dehydrogenase gene for five closely related !1species of Hawaiian Drosophila. !$#cross-references MUID:91163323; PMID:2002765 !$#accession E23724 !'##status preliminary !'##molecule_type DNA !'##residues 1-254 ##label RO5 !'##cross-references GB:M63303; GB:M36785; NID:g156881; PIDN:AAA28350.1; !1PID:g156882 !'##note the protein translation is not shown in this reference GENETICS !$#gene FlyBase:Ddif/Adh !'##cross-references FlyBase:FBgn0012249 !$#start_codon AAC !$#introns 31/3; 166/3 CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; NAD; oxidoreductase FEATURE !$6-182 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 254 #molecular-weight 27451 #checksum 9908 SEQUENCE /// ENTRY D23724 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) - fruit fly (Drosophila silvestris) ORGANISM #formal_name Drosophila silvestris DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 02-Nov-2001 ACCESSIONS D23724 REFERENCE A23724 !$#authors Rowan, R.G.; Hunt, J.A. !$#journal Mol. Biol. Evol. (1991) 8:49-70 !$#title Rates of DNA change and phylogeny from the DNA sequences of !1the alcohol dehydrogenase gene for five closely related !1species of Hawaiian Drosophila. !$#cross-references MUID:91163323; PMID:2002765 !$#accession D23724 !'##status preliminary !'##molecule_type DNA !'##residues 1-223 ##label RO4 !'##note the protein translation is not shown in this reference GENETICS !$#gene FlyBase:Dsil/Adh !'##cross-references FlyBase:FBgn0012805 !$#start_codon AAC !$#introns 135/3 CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; NAD; oxidoreductase FEATURE !$1-151 #domain short-chain alcohol dehydrogenase homology !8#status atypical #label SADH SUMMARY #length 223 #molecular-weight 24398 #checksum 5682 SEQUENCE /// ENTRY S07246 #type complete TITLE alcohol dehydrogenase-related enzyme (EC 1.1.1.-) - fruit fly (Drosophila pseudoobscura) ALTERNATE_NAMES Adh-dup protein; Adh-related protein; Adhr protein; alcohol dehydrogenase dup ORGANISM #formal_name Drosophila pseudoobscura DATE 29-Jan-1993 #sequence_revision 07-Feb-1997 #text_change 11-Jun-1999 ACCESSIONS S07246 REFERENCE S06292 !$#authors Schaeffer, S.W.; Aquadro, C.F. !$#journal Genetics (1987) 117:61-73 !$#title Nucleotide sequence of the Adh gene region of Drosophila !1pseudoobscura: evolutionary change and evidence for an !1ancient gene duplication. !$#cross-references MUID:88030644; PMID:3666441 !$#accession S07246 !'##molecule_type DNA !'##residues 1-278 ##label SCH !'##cross-references EMBL:Y00602; NID:g8869; PIDN:CAA68646.1; PID:g8871 GENETICS !$#gene FlyBase:Adhr; Adh-dup !'##cross-references FlyBase:FBgn0012689 !$#introns 32/3; 167/3 CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS oxidoreductase FEATURE !$7-185 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 278 #molecular-weight 30895 #checksum 412 SEQUENCE /// ENTRY S16454 #type complete TITLE alcohol dehydrogenase-related protein (EC 1.1.1.-) - fruit fly (Drosophila ambigua) ALTERNATE_NAMES Adh-dup protein; Adh-related protein; Adhr protein; alcohol dehydrogenase dup ORGANISM #formal_name Drosophila ambigua DATE 12-Feb-1993 #sequence_revision 07-Feb-1997 #text_change 11-Jun-1999 ACCESSIONS S16454 REFERENCE S16453 !$#authors Marfany, G.; Gonzalez-Duarte, R. !$#journal J. Mol. Evol. (1991) 32:454-462 !$#title The Adh genomic region of Drosophila ambigua: evolutionary !1trends in different species. !$#cross-references MUID:91332913; PMID:1908016 !$#accession S16454 !'##molecule_type DNA !'##residues 1-281 ##label MAR !'##cross-references EMBL:X54813; NID:g7143; PIDN:CAA38582.1; PID:g7145 GENETICS !$#gene FlyBase:Adhr; Adh-dup !'##cross-references FlyBase:FBgn0012100 !$#introns 32/3; 167/3 CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS oxidoreductase FEATURE !$7-185 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 281 #molecular-weight 31227 #checksum 1627 SEQUENCE /// ENTRY B42180 #type complete TITLE alcohol dehydrogenase related protein (EC 1.1.1.-) - fruit fly (Drosophila subobscura) ALTERNATE_NAMES Adh-dup protein; Adh-related protein; Adhr protein; alcohol dehydrogenase dup ORGANISM #formal_name Drosophila subobscura DATE 18-May-1994 #sequence_revision 07-Feb-1997 #text_change 21-Feb-1997 ACCESSIONS B42180 REFERENCE A42180 !$#authors Marfany, G.; Gonzalez-Duarte, R. !$#journal Mol. Biol. Evol. (1992) 9:261-277 !$#title The Drosophila subobscura Adh genomic region contains !1valuable evolutionary markers. !$#cross-references MUID:92219958; PMID:1560762 !$#accession B42180 !'##molecule_type DNA !'##residues 1-279 ##label MAR !'##note sequence extracted from NCBI backbone (NCBIN:95355) GENETICS !$#gene FlyBase:Adhr; Adh-dup !'##cross-references FlyBase:FBgn0012931 !$#introns 32/3; 167/3 CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS oxidoreductase FEATURE !$7-185 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 279 #molecular-weight 31063 #checksum 6574 SEQUENCE /// ENTRY D40731 #type complete TITLE alcohol dehydrogenase related protein (EC 1.1.1.-) - fruit fly (Drosophila madeirensis) ALTERNATE_NAMES Adh-dup protein; Adh-related protein; Adhr protein; alcohol dehydrogenase dup ORGANISM #formal_name Drosophila madeirensis DATE 14-Sep-1994 #sequence_revision 07-Feb-1997 #text_change 11-Jun-1999 ACCESSIONS D40731 REFERENCE A40731 !$#authors Marfany, G.; Gonzalez-Duarte, R. !$#journal Mol. Phylogenet. Evol. (1993) 2:13-22 !$#title Characterization and evolution of the Adh genomic region in !1Drosophila guanche and Drosophila madeirensis. !$#cross-references MUID:94362951; PMID:8081544 !$#accession D40731 !'##status translation not shown !'##molecule_type DNA !'##residues 1-279 ##label MAR !'##cross-references GB:X60112; NID:g397370; PIDN:CAA42710.1; !1PID:g397372 GENETICS !$#gene FlyBase:Adhr; Adh-dup !'##cross-references FlyBase:FBgn0012467 !$#introns 32/3; 167/3 CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS oxidoreductase FEATURE !$7-185 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 279 #molecular-weight 31018 #checksum 6291 SEQUENCE /// ENTRY B40731 #type complete TITLE alcohol dehydrogenase-related enzyme (EC 1.1.1.-) - fruit fly (Drosophila guanche) ALTERNATE_NAMES Adh-dup protein; Adh-related protein; Adhr protein; alcohol dehydrogenase dup ORGANISM #formal_name Drosophila guanche DATE 14-Sep-1994 #sequence_revision 07-Feb-1997 #text_change 11-Jun-1999 ACCESSIONS B40731 REFERENCE A40731 !$#authors Marfany, G.; Gonzalez-Duarte, R. !$#journal Mol. Phylogenet. Evol. (1993) 2:13-22 !$#title Characterization and evolution of the Adh genomic region in !1Drosophila guanche and Drosophila madeirensis. !$#cross-references MUID:94362951; PMID:8081544 !$#accession B40731 !'##molecule_type DNA !'##residues 1-279 ##label MAR !'##cross-references GB:X60113; NID:g397367; PIDN:CAA42712.1; !1PID:g397369 GENETICS !$#gene FlyBase:Adhr; Adh-dup !'##cross-references FlyBase:FBgn0012325 !$#introns 32/3; 167/3 CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS oxidoreductase FEATURE !$7-185 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 279 #molecular-weight 30988 #checksum 6277 SEQUENCE /// ENTRY S20716 #type complete TITLE alcohol dehydrogenase-related enzyme (EC 1.1.1.-) - fruit fly (Drosophila teissieri) ALTERNATE_NAMES Adh-dup protein; Adh-related protein; Adhr protein; alcohol dehydrogenase dup ORGANISM #formal_name Drosophila teissieri DATE 20-Feb-1995 #sequence_revision 07-Feb-1997 #text_change 11-Jun-1999 ACCESSIONS S20716; S20715 REFERENCE S20713 !$#authors Ashburner, M. !$#submission submitted to the EMBL Data Library, July 1990 !$#accession S20716 !'##molecule_type DNA !'##residues 1-272 ##label ASH !'##cross-references EMBL:X54118; NID:g9151; PIDN:CAA38061.1; PID:g9153 GENETICS !$#gene FlyBase:Adhr; Adh-dup !'##cross-references FlyBase:FBgn0013014 !$#introns 32/3; 167/3 CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS oxidoreductase FEATURE !$7-185 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 272 #molecular-weight 30301 #checksum 9475 SEQUENCE /// ENTRY JN0565 #type complete TITLE alcohol dehydrogenase-related enzyme (EC 1.1.1.-) - fruit fly (Drosophila lebanonensis) ALTERNATE_NAMES Adh-dup protein; Adh-related protein; Adhr protein; alcohol dehydrogenase dup ORGANISM #formal_name Drosophila lebanonensis DATE 10-Mar-1994 #sequence_revision 07-Feb-1997 #text_change 11-Jun-1999 ACCESSIONS JN0565; S32722 REFERENCE JN0564 !$#authors Albalat, R.; Gonzalez-Duarte, R. !$#journal Gene (1993) 126:171-178 !$#title Adh and Adh-dup sequences of Drosophila lebanonensis and D. !1immigrans: interspecies comparisons. !$#cross-references MUID:93246241; PMID:8482531 !$#accession JN0565 !'##molecule_type DNA !'##residues 1-269 ##label ALB !'##cross-references GB:M97637; NID:g304657; PIDN:AAA28356.1; !1PID:g304659 REFERENCE S32722 !$#authors Juan, E.; Papaceit, M. !$#submission submitted to the EMBL Data Library, February 1992 !$#accession S32722 !'##molecule_type DNA !'##residues 1-264,'T',266,'RMIRQIRSFQKTIYI' ##label JUA !'##cross-references EMBL:X63716; NID:g297082; PIDN:CAA45249.1; !1PID:g297083 GENETICS !$#gene FlyBase:Adhr; Adh-dup !'##cross-references FlyBase:FBgn0012439 !$#introns 32/3; 167/3 CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; NAD; oxidoreductase FEATURE !$7-185 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 269 #molecular-weight 29658 #checksum 8965 SEQUENCE /// ENTRY JN0567 #type complete TITLE alcohol dehydrogenase-related enzyme (EC 1.1.1.-) - fruit fly (Drosophila immigrans) ALTERNATE_NAMES Adh-dup protein; Adh-related protein; Adhr protein; alcohol dehydrogenase dup ORGANISM #formal_name Drosophila immigrans DATE 10-Mar-1994 #sequence_revision 07-Feb-1997 #text_change 11-Jun-1999 ACCESSIONS JN0567 REFERENCE JN0564 !$#authors Albalat, R.; Gonzalez-Duarte, R. !$#journal Gene (1993) 126:171-178 !$#title Adh and Adh-dup sequences of Drosophila lebanonensis and D. !1immigrans: interspecies comparisons. !$#cross-references MUID:93246241; PMID:8482531 !$#accession JN0567 !'##molecule_type DNA !'##residues 1-273 ##label ALB !'##cross-references GB:M97638; NID:g304660; PIDN:AAA28358.1; !1PID:g304662 GENETICS !$#gene FlyBase:Adhr; Adh-dup !'##cross-references FlyBase:FBgn0012412 !$#introns 32/3; 167/3 CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS oxidoreductase FEATURE !$7-185 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 273 #molecular-weight 30430 #checksum 3292 SEQUENCE /// ENTRY S20713 #type complete TITLE alcohol dehydrogenase related protein (EC 1.1.1.-) - fruit fly (Drosophila erecta) ALTERNATE_NAMES Adh-dup protein; Adh-related protein; Adhr protein; alcohol dehydrogenase dup ORGANISM #formal_name Drosophila erecta DATE 22-Nov-1993 #sequence_revision 07-Feb-1997 #text_change 21-Feb-1997 ACCESSIONS S20713; S20714 REFERENCE S20713 !$#authors Ashburner, M. !$#submission submitted to the EMBL Data Library, July 1990 !$#accession S20713 !'##status preliminary !'##molecule_type DNA !'##residues 1-256 ##label ASH !'##cross-references EMBL:X54116 GENETICS !$#gene FlyBase:Adhr; Adh-dup !'##cross-references FlyBase:FBgn0012262 !$#introns 32/3; 167/3 CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; NAD; oxidoreductase FEATURE !$7-185 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 256 #molecular-weight 28098 #checksum 3223 SEQUENCE /// ENTRY A24181 #type complete TITLE probable alcohol dehydrogenase (EC 1.1.1.-) - flesh fly (Sarcophaga peregrina) ALTERNATE_NAMES development-specific 25K protein ORGANISM #formal_name Sarcophaga peregrina DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A24181 REFERENCE A24181 !$#authors Matsumoto, N.; Sekimizu, K.; Soma, G.I.; Ohmura, Y.; Andoh, !1T.; Nakanishi, Y.; Obinata, M.; Natori, S. !$#journal J. Biochem. (1985) 97:1501-1508 !$#title Structural analysis of a developmentally regulated 25-kDa !1protein gene of Sarcophaga peregrina. !$#cross-references MUID:85289142; PMID:2993269 !$#accession A24181 !'##molecule_type mRNA !'##residues 1-184 ##label MAT !'##note the authors translated the codons TTC and TTG for residues 18 !1and 108 as Ile and Phe, respectively, and GGT for residues !194 and 158 as Val COMMENT This protein is expressed in the fat body of middle !1third-instar larvae. GENETICS !$#introns 33/1; 109/1; 167/1 CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS NAD; oxidoreductase FEATURE !$7-184 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 184 #molecular-weight 19993 #checksum 6468 SEQUENCE /// ENTRY RDHUCB #type complete TITLE carbonyl reductase (NADPH2) (EC 1.1.1.184) - human ALTERNATE_NAMES aldehyde reductase I; NADPH-dependent carbonyl reductase; prostaglandin 9-ketoreductase; xenobiotic ketone reductase ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 03-Jun-2002 ACCESSIONS A61271; A31912; S09013; A47326 REFERENCE A61271 !$#authors Forrest, G.L.; Akman, S.; Doroshow, J.; Rivera, H.; Kaplan, !1W.D. !$#journal Mol. Pharmacol. (1991) 40:502-507 !$#title Genomic sequence and expression of a cloned human carbonyl !1reductase gene with daunorubicin reductase activity. !$#cross-references MUID:92017676; PMID:1921984 !$#accession A61271 !'##status translation not shown !'##molecule_type DNA !'##residues 1-277 ##label FOR !'##cross-references GB:M62420; NID:g179977; PIDN:AAA17881.1; !1PID:g179978 REFERENCE A31912 !$#authors Wermuth, B.; Bohren, K.M.; Heinemann, G.; von Wartburg, !1J.P.; Gabbay, K.H. !$#journal J. Biol. Chem. (1988) 263:16185-16188 !$#title Human carbonyl reductase. Nucleotide sequence analysis of a !1cDNA and amino acid sequence of the encoded protein. !$#cross-references MUID:89034082; PMID:3141401 !$#accession A31912 !'##molecule_type mRNA !'##residues 1-277 ##label WER !'##cross-references GB:J04056; NID:g181036; PIDN:AAA52070.1; !1PID:g181037 !'##note part of this sequence was confirmed by protein sequencing REFERENCE S09013 !$#authors Forrest, G.L.; Akman, S.; Krutzik, S.; Paxton, R.J.; !1Sparkes, R.S.; Doroshow, J.; Felsted, R.L.; Glover, C.J.; !1Mohandas, T.; Bachur, N.R. !$#journal Biochim. Biophys. Acta (1990) 1048:149-155 !$#title Induction of a human carbonyl reductase gene located on !1chromosome 21. !$#cross-references MUID:90212644; PMID:2182121 !$#accession S09013 !'##molecule_type mRNA !'##residues 1-277 ##label FO2 !'##cross-references GB:J04056; EMBL:X51818; NID:g181036; !1PIDN:AAA52070.1; PID:g181037 REFERENCE A47326 !$#authors Krook, M.; Ghosh, D.; Stroemberg, R.; Carlquist, M.; !1Joernvall, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:502-506 !$#title Carboxyethyllysine in a protein: native carbonyl reductase/ !1NADP+-dependent prostaglandin dehydrogenase. !$#cross-references MUID:93133816; PMID:8421682 !$#accession A47326 !'##molecule_type protein !'##residues 221-242 ##label KRO !'##note identification of carboxyethyllysine modification COMMENT This cytosolic aldoketoreductase and quinone reductase !1reduces a variety of carbonyl compounds to the corresponding !1alcohols. GENETICS !$#gene GDB:CBR !'##cross-references GDB:126610; OMIM:114830 !$#map_position 21q22.12-21q22.12 !$#introns 97/1; 133/1 CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS blocked amino end; monomer; NADP; oxidoreductase FEATURE !$6-185 #domain short-chain alcohol dehydrogenase homology !8#label SADH\ !$239 #modified_site N6-1-carboxyethyllysine (Lys) !8(partial) #status experimental SUMMARY #length 277 #molecular-weight 30375 #checksum 7216 SEQUENCE /// ENTRY A42912 #type complete TITLE 3alpha(or 20beta)-hydroxysteroid dehydrogenase (EC 1.1.1.53) - pig ALTERNATE_NAMES (R)-20-hydroxysteroid dehydrogenase; cortisone reductase ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A42912 REFERENCE A42912 !$#authors Tanaka, M.; Ohno, S.; Adachi, S.; Nakajin, S.; Shinoda, M.; !1Nagahama, Y. !$#journal J. Biol. Chem. (1992) 267:13451-13455 !$#title Pig testicular 20 beta-hydroxysteroid dehydrogenase exhibits !1carbonyl reductase-like structure and activity. cDNA cloning !1of pig testicular 20 beta-hydroxysteroid dehydrogenase. !$#cross-references MUID:92317067; PMID:1377683 !$#accession A42912 !'##status preliminary !'##molecule_type mRNA !'##residues 1-289 ##label TAN !'##cross-references GB:M80709; NID:g164293; PIDN:AAA30980.1; !1PID:g164294 !'##experimental_source testis !'##note sequence extracted from NCBI backbone (NCBIN:107764, !1NCBIP:107765) CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS NADP; oxidoreductase FEATURE !$6-185 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 289 #molecular-weight 31693 #checksum 9769 SEQUENCE /// ENTRY A35802 #type complete TITLE 15-hydroxyprostaglandin dehydrogenase (NAD) (EC 1.1.1.141), placental [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 23-Oct-1990 #sequence_revision 18-Oct-1996 #text_change 03-Jun-2002 ACCESSIONS A35802; A33947; B33947 REFERENCE A35802 !$#authors Ensor, C.M.; Yang, J.Y.; Okita, R.T.; Tai, H.H. !$#journal J. Biol. Chem. (1990) 265:14888-14891 !$#title Cloning and sequence analysis of the cDNA for human !1placental NAD+-dependent 15-hydroxyprostaglandin !1dehydrogenase. !$#cross-references MUID:90368660; PMID:1697582 !$#accession A35802 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-266 ##label ENS !'##cross-references GB:J05594; NID:g1203981; PIDN:AAA89174.1; !1PID:g1203982 !'##note part of this sequence was confirmed by protein sequencing REFERENCE A33947 !$#authors Krook, M.; Marekov, L.; Joernvall, H. !$#journal Biochemistry (1990) 29:738-743 !$#title Purification and structural characterization of placental !1NAD+-linked 15-hydroxyprostaglandin dehydrogenase. The !1primary structure reveals the enzyme to belong to the !1short-chain alcohol dehydrogenase family. !$#cross-references MUID:90248418; PMID:2337593 !$#accession A33947 !'##molecule_type protein !'##residues 1-216,'C',218-266 ##label KRO1 !'##cross-references CAS:124041-95-8 !$#accession B33947 !'##molecule_type protein !'##residues 1-266 ##label KRO2 !'##cross-references CAS:124041-96-9 GENETICS !$#gene GDB:HPGD !'##cross-references GDB:126731; OMIM:601688 !$#map_position 7q33-7qter FUNCTION !$#description oxidizes prostaglandins to much less active 15-keto !1metabolites CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS cytosol; homodimer; NAD; oxidoreductase FEATURE !$1-266 #product 15-hydroxyprostaglandin dehydrogenase (NAD+) !8#status experimental #label MAT\ !$6-184 #domain short-chain alcohol dehydrogenase homology !8#label SADH\ !$6-36 #region beta-alpha-beta NAD nucleotide-binding fold SUMMARY #length 266 #molecular-weight 28977 #checksum 4512 SEQUENCE /// ENTRY JN0703 #type complete TITLE carbonyl reductase (NADPH2) (EC 1.1.1.184) - pig ALTERNATE_NAMES tetrameric carbonyl reductase ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS JN0703; PN0569 REFERENCE JN0703 !$#authors Nakanishi, M.; Deyashiki, Y.; Nakayama, T.; Sato, K.; Hara, !1A. !$#journal Biochem. Biophys. Res. Commun. (1993) 194:1311-1316 !$#title Cloning and sequence analysis of a cDNA encoding tetrameric !1carbonyl reductase of pig lung. !$#cross-references MUID:93356806; PMID:8352790 !$#accession JN0703 !'##molecule_type mRNA !'##residues 1-244 ##label NAK !'##cross-references GB:D16511; NID:g416424; PIDN:BAA03963.1; !1PID:g416425 !$#accession PN0569 !'##molecule_type protein !'##residues 1-22;123-136;138-151;166-175;187-201;240-244 ##label NA2 COMMENT This enzyme is an NADPH-linked oxidoreductase that catalyzes !1the reduction of various carbonyl compounds to the !1corresponding alcohols. CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS NADP; oxidoreductase FEATURE !$8-180 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 244 #molecular-weight 25986 #checksum 8918 SEQUENCE /// ENTRY A28053 #type complete TITLE carbonyl reductase (NADPH2) (EC 1.1.1.184) - mouse ALTERNATE_NAMES adipocyte p27 protein ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S03382; S69141; S69142; A28053 REFERENCE S03382 !$#authors Navre, M.; Ringold, G.M. !$#journal J. Cell Biol. (1988) 107:279-286 !$#title A growth factor-repressible gene associated with protein !1kinase C-mediated inhibition of adipocyte differentiation. !$#cross-references MUID:88273310; PMID:2455724 !$#accession S03382 !'##molecule_type mRNA !'##residues 1-244 ##label NAV !'##cross-references EMBL:X07411; NID:g50003; PIDN:CAA30309.1; !1PID:g50004 !'##experimental_source strain C3H REFERENCE S69141 !$#authors Nakanishi, M.; Deyashiki, Y.; Ohshima, K.; Hara, A. !$#journal Eur. J. Biochem. (1995) 228:381-387 !$#title Cloning, expression and tissue distribution of mouse !1tetrameric carbonyl reductase. Identity with an adipocyte !127-kDa protein. !$#cross-references MUID:95220366; PMID:7705352 !$#accession S69141 !'##molecule_type mRNA !'##residues 1-244 ##label NAK !'##cross-references EMBL:D26123; NID:g440371; PIDN:BAA05120.1; !1PID:g699608 !'##experimental_source lung; strain CD-1 !$#accession S69142 !'##molecule_type protein !'##residues 1-29;40-80;84-96;110-198;209-223;227-244 ##label NAW !'##experimental_source lung; strain CD-1 GENETICS !$#genome nuclear COMPLEX homotetramer FUNCTION !$#description catalyzes the reduction of various carbonyl compounds to !1corresponding alcohols !$#pathway involved in pulmonary metabolism of endogenous carbonyl !1compounds and xenobiotic metabolism !$#note member of short-chain alcohol dehydrogenase family CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS mitochondrion; NADP; oxidoreductase FEATURE !$1-244 #product carbonyl reductase (NADPH) #status !8experimental #label MAT\ !$8-180 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 244 #molecular-weight 25958 #checksum 5185 SEQUENCE /// ENTRY RDALAE #type complete TITLE acetoacetyl-CoA reductase (EC 1.1.1.36) [validated] - Alcaligenes eutrophus ORGANISM #formal_name Alcaligenes eutrophus DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 18-Aug-2000 ACCESSIONS B34340 REFERENCE A34340 !$#authors Peoples, O.P.; Sinskey, A.J. !$#journal J. Biol. Chem. (1989) 264:15293-15297 !$#title Poly-beta-hydroxybutyrate biosynthesis in Alcaligenes !1eutrophus H16. Characterization of the genes encoding !1beta-ketothiolase and acetoacetyl-CoA reductase. !$#cross-references MUID:89359356; PMID:2670935 !$#accession B34340 !'##molecule_type DNA !'##residues 1-246 ##label PEO !'##cross-references EMBL:J04987; NID:g141953; PIDN:AAA21973.1; !1PID:g141955 !'##experimental_source strain H16 GENETICS !$#gene phbB FUNCTION !$#description EC 1.1.1.36 [validated, MUID:89359356]; catalyzes the !1reduction of acetoacetyl-CoA to hydroxylacyl-CoA in the !1presence of NADPH !$#note essential step in the biosynthesis of !1poly-beta-hydroxybutyrate CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS NAD; oxidoreductase; poly-beta-hydroxybutyrate biosynthesis FEATURE !$4-184 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 246 #molecular-weight 26370 #checksum 2829 SEQUENCE /// ENTRY A43744 #type complete TITLE N-acylmannosamine 1-dehydrogenase (EC 1.1.1.233) - Flavobacterium sp. (strain 141-8) ORGANISM #formal_name Flavobacterium sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A43744 REFERENCE A43744 !$#authors Yamamoto-Otake, H.; Koyama, Y.; Horiuchi, T.; Nakano, E. !$#journal Appl. Environ. Microbiol. (1991) 57:1418-1422 !$#title Cloning, sequencing, and expression of the !1N-acyl-D-mannosamine dehydrogenase gene from Flavobacterium !1sp. strain 141-8 in Escherichia coli. !$#cross-references MUID:91307310; PMID:1854199 !$#accession A43744 !'##status preliminary !'##molecule_type DNA !'##residues 1-271 ##label YAM !'##cross-references EMBL:D90316; NID:g216704; PIDN:BAA14346.1; !1PID:g216705 CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS NAD; oxidoreductase FEATURE !$16-197 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 271 #molecular-weight 27469 #checksum 3705 SEQUENCE /// ENTRY B39930 #type complete TITLE internalin B - Listeria monocytogenes ORGANISM #formal_name Listeria monocytogenes DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B39930 REFERENCE A39930 !$#authors Gaillard, J.L.; Berche, P.; Frehel, C.; Gouin, E.; Cossart, !1P. !$#journal Cell (1991) 65:1127-1141 !$#title Entry of Listeria monocytogenes into cells is mediated by !1internalin, a repeat protein reminiscent of surface antigens !1from gram-positive cocci. !$#cross-references MUID:91292517; PMID:1905979 !$#accession B39930 !'##status preliminary !'##molecule_type DNA !'##residues 1-248 ##label GAI !'##cross-references GB:M67471 CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology FEATURE !$6-187 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 248 #molecular-weight 26782 #checksum 5347 SEQUENCE /// ENTRY A28788 #type complete TITLE actinorhodin polyketide ketoreductase (EC 1.1.1.-) actIII - Streptomyces coelicolor ORGANISM #formal_name Streptomyces coelicolor DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Dec-1999 ACCESSIONS JS0108; A28788; T42026 REFERENCE JS0108 !$#authors Hallam, S.E.; Malpartida, F.; Hopwood, D.A. !$#journal Gene (1988) 74:305-320 !$#title Nucleotide sequence, transcription and deduced function of a !1gene involved in polyketide antibiotic synthesis in !1Streptomyces coelicolor. !$#cross-references MUID:89232723; PMID:2469622 !$#accession JS0108 !'##molecule_type DNA !'##residues 1-261 ##label HAL !'##cross-references GB:M19536; NID:g153141; PIDN:AAA26688.1; !1PID:g153142 !'##experimental_source strain A3[2] COMMENT This protein is responsible for catalyzing a beta-keto !1reductive step during assembly of the actinorhodin !1polyketide chain. GENETICS !$#gene actIII CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS NAD; oxidoreductase FEATURE !$7-188 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 261 #molecular-weight 27265 #checksum 4328 SEQUENCE /// ENTRY DEKCNG #type complete TITLE acetoacetyl-CoA reductase (EC 1.1.1.36) - Azospirillum brasilense ALTERNATE_NAMES nodulation protein nodG ORGANISM #formal_name Azospirillum brasilense DATE 31-Dec-1991 #sequence_revision 13-Jan-1995 #text_change 11-Jun-1999 ACCESSIONS S20485; S14679; S10469 REFERENCE S20483 !$#authors Vieille, C.; Elmerich, C. !$#journal Mol. Gen. Genet. (1992) 231:375-384 !$#title Characterization of an Azospirillum brasilense Sp7 gene !1homologous to Alcaligenes eutrophus phbB and to Rhizobium !1meliloti nodG. !$#cross-references MUID:92167956; PMID:1538694 !$#accession S20485 !'##molecule_type DNA !'##residues 1-246 ##label VIE !'##cross-references EMBL:X64772; NID:g38684; PIDN:CAA46021.1; !1PID:g38686 !'##experimental_source strain Sp7 !'##note named according to sequennce homology REFERENCE S14679 !$#authors Delledonne, M.; Porcari, R.; Fogher, C. !$#journal Nucleic Acids Res. (1990) 18:6435 !$#title Nucleotide sequence of the nodG gene of Azospirillum !1brasilense. !$#cross-references MUID:91057141; PMID:2243795 !$#accession S14679 !'##status translation not shown; significant sequence differences !'##molecule_type DNA !'##cross-references EMBL:X52913; NID:g38682; PID:g38683 !'##experimental_source strain Sp7 !'##note the sequence reported in this reference is incorrect due to !1multiple frameshift errors CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS NAD; nodulation; oxidoreductase; poly-beta-hydroxybutyrate !1biosynthesis FEATURE !$4-184 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 246 #molecular-weight 25717 #checksum 7590 SEQUENCE /// ENTRY S05397 #type complete TITLE granaticin polyketide ketoreductase (EC 1.1.1.-) graIII [similarity] - Streptomyces violaceoruber ALTERNATE_NAMES 3-hydroxyacyl-CoA dehydrogenase homolog 1; polyketide ketoreductase ORGANISM #formal_name Streptomyces violaceoruber DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 11-May-2000 ACCESSIONS S05397; T46536 REFERENCE S05393 !$#authors Sherman, D.H.; Malpartida, F.; Bibb, M.J.; Kieser, H.M.; !1Bibb, M.J.; Hopwood, D.A. !$#journal EMBO J. (1989) 8:2717-2725 !$#title Structure and deduced function of the granaticin-producing !1polyketide synthase gene cluster of Streptomyces !1violaceoruber Tue22. !$#cross-references MUID:90060034; PMID:2583128 !$#accession S05397 !'##molecule_type DNA !'##residues 1-272 ##label SHE !'##cross-references EMBL:X16144; NID:g47976; PIDN:CAA34263.1; !1PID:g47978 REFERENCE Z23045 !$#authors Ichinose, K.; Bedford, D.J.; Tornus, D.; Bechthold, A.; !1Bibb, M.J.; Revill, W.P.; Floss, H.G.; Hopwood, D.A. !$#journal Chem. Biol. (1998) 5:647-659 !$#title The granaticin biosynthetic gene cluster of Streptomyces !1violaceoruber Tu22: sequence analysis and expression in a !1heterologous host. !$#cross-references MUID:99051446; PMID:9831526 !$#accession T46536 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-272 ##label ICH !'##cross-references EMBL:AJ011500; PIDN:CAA09652.1 !'##experimental_source strain Tu22 GENETICS !$#gene graIII !$#note gra-orf5 CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS NAD; oxidoreductase FEATURE !$18-199 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 272 #molecular-weight 28393 #checksum 3104 SEQUENCE /// ENTRY S29279 #type complete TITLE acetoacetyl-CoA reductase (EC 1.1.1.36) - Chromatium vinosum ORGANISM #formal_name Chromatium vinosum DATE 22-Nov-1993 #sequence_revision 13-Jan-1995 #text_change 11-Jun-1999 ACCESSIONS S29279 REFERENCE S29274 !$#authors Liebergesell, M.; Steinbuechel, A. !$#journal Eur. J. Biochem. (1992) 209:135-150 !$#title Cloning and nucleotide sequences of genes relevant for !1biosynthesis of poly(3-hydroxybutyric acid) in Chromatium !1vinosum strain D. !$#cross-references MUID:93011119; PMID:1396692 !$#accession S29279 !'##molecule_type DNA !'##residues 1-246 ##label LIE !'##cross-references GB:L01112; NID:g145010; PIDN:AAA23325.1; !1PID:g145016 COMMENT In the presence of NADPH, this enzyme catalyzes the !1reduction of acetoacetyl-CoA to hydroxylacyl-CoA, an !1essential step in the biosynthesis of !1poly-beta-hydroxybutyrate. CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS NADP; oxidoreductase; poly-beta-hydroxybutyrate biosynthesis FEATURE !$3-184 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 246 #molecular-weight 26123 #checksum 3923 SEQUENCE /// ENTRY S25079 #type complete TITLE monensin polyketide ketoreductase (EC 1.1.1.-) - Streptomyces cinnamonensis ORGANISM #formal_name Streptomyces cinnamonensis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S25079; S18170 REFERENCE S25076 !$#authors Arrowsmith, T.J.; Malpartida, F.; Sherman, D.H.; Birch, A.; !1Hopwood, D.A.; Robinson, J.A. !$#journal Mol. Gen. Genet. (1992) 234:254-264 !$#title Characterisation of actI-homologous DNA encoding polyketide !1synthase genes from the monensin producer Streptomyces !1cinnamonensis. !$#cross-references MUID:92374994; PMID:1508151 !$#accession S25079 !'##molecule_type DNA !'##residues 1-261 ##label ARR !'##cross-references EMBL:Z11511; NID:g46799; PIDN:CAA77599.1; !1PID:g46803 CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS NAD; oxidoreductase FEATURE !$7-188 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 261 #molecular-weight 27080 #checksum 4473 SEQUENCE /// ENTRY S06998 #type complete TITLE acetoacetyl-CoA reductase (EC 1.1.1.36) - Zoogloea ramigera ORGANISM #formal_name Zoogloea ramigera DATE 22-Jan-1993 #sequence_revision 13-Jan-1995 #text_change 06-Jun-1997 ACCESSIONS S06998; S26992; S02631 REFERENCE S06998 !$#authors Peoples, O.P.; Sinskey, A.J. !$#journal Mol. Microbiol. (1989) 3:349-357 !$#title Fine structural analysis of the Zoogloea ramigera phbA-phbB !1locus encoding beta-ketothiolase and acetoacetyl-CoA !1reductase: nucleotide sequence of phbB. !$#cross-references MUID:89313287; PMID:2546004 !$#accession S06998 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-241 ##label PEO !$#accession S26992 !'##molecule_type protein !'##residues 2-7 ##label PE2 REFERENCE S02631 !$#authors Ploux, O.; Masamune, S.; Walsh, C.T. !$#journal Eur. J. Biochem. (1988) 174:177-182 !$#title The NADPH-linked acetoacetyl-CoA reductase from Zoogloea !1ramigera. Characterization and mechanistic studies of the !1cloned enzyme over-produced in Escherichia coli. !$#cross-references MUID:88225101; PMID:3286259 !$#accession S02631 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 3-31 ##label PLO COMMENT In the presence of NADPH, this enzyme catalyzes the !1reduction of acetoacetyl-CoA to hydroxylacyl-CoA, an !1essential step in the biosynthesis of !1poly-beta-hydroxybutyrate. GENETICS !$#gene phbB CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS NADP; oxidoreductase; poly-beta-hydroxybutyrate biosynthesis FEATURE !$2-241 #product acetoacetyl-CoA reductase #status !8experimental #label MAT\ !$3-178 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 241 #molecular-weight 25285 #checksum 2274 SEQUENCE /// ENTRY B42147 #type complete TITLE 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100) - Escherichia coli (strain K-12) ALTERNATE_NAMES 3-ketoacyl-ACP reductase ORGANISM #formal_name Escherichia coli DATE 30-Sep-1993 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS B64853; B42147; C41856 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64853 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-244 ##label BLAT !'##cross-references GB:AE000210; GB:U00096; NID:g1787332; !1PIDN:AAC74177.1; PID:g1787335; UWGP:b1093 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A42147 !$#authors Rawlings, M.; Cronan Jr., J.E. !$#journal J. Biol. Chem. (1992) 267:5751-5754 !$#title The gene encoding Escherichia coli acyl carrier protein lies !1within a cluster of fatty acid biosynthetic genes. !$#cross-references MUID:92210530; PMID:1556094 !$#accession B42147 !'##molecule_type DNA !'##residues 1-29,'G',31-244 ##label RAW !'##cross-references GB:M84991; NID:g145879; PIDN:AAA23739.1; !1PID:g145881 REFERENCE A41856 !$#authors Verwoert, I.I.; Verbree, E.C.; van der Linden, K.H.; !1Nijkamp, H.J.; Stuitje, A.R. !$#journal J. Bacteriol. (1992) 174:2851-2857 !$#title Cloning, nucleotide sequence, and expression of the !1Escherichia coli fabD gene, encoding malonyl coenzyme A-acyl !1carrier protein transacylase. !$#cross-references MUID:92234941; PMID:1314802 !$#accession C41856 !'##molecule_type DNA !'##residues 1-42,'R',44-45 ##label VER !'##cross-references GB:M87040; NID:g145885; PIDN:AAA23743.1; !1PID:g145888 !'##note sequence inconsistent with the nucleotide translation !'##note sequence extracted from NCBI backbone (NCBIN:97135, !1NCBIP:97150) GENETICS !$#gene fabG !$#map_position 24 min FUNCTION !$#pathway fatty acid biosynthesis CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS fatty acid biosynthesis; NADP; oxidoreductase FEATURE !$6-182 #domain short-chain alcohol dehydrogenase homology !8#label SADH\ !$6-36 #region beta-alpha-beta NADP nucleotide-binding fold\ !$151 #active_site Tyr #status predicted SUMMARY #length 244 #molecular-weight 25560 #checksum 3492 SEQUENCE /// ENTRY A64590 #type complete TITLE probable 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100) - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A64590 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession A64590 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-247 ##label TOM !'##cross-references GB:AE000570; GB:AE000511; NID:g2313672; !1PIDN:AAD07627.1; PID:g2313678; TIGR:HP0561 CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS fatty acid biosynthesis; NAD; oxidoreductase FEATURE !$6-186 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 247 #molecular-weight 26668 #checksum 3169 SEQUENCE /// ENTRY A48154 #type complete TITLE short-chain alcohol dehydrogenase (EC 1.1.1.-) Ke 6 - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A48154 REFERENCE A48154 !$#authors Aziz, N.; Maxwell, M.M.; St. Jacques, B.; Brenner, B.M. !$#journal Mol. Cell. Biol. (1993) 13:1847-1853 !$#title Downregulation of Ke 6, a novel gene encoded within the !1major histocompatibility complex, in murine polycystic !1kidney disease. !$#cross-references MUID:93180832; PMID:8441417 !$#accession A48154 !'##status preliminary !'##molecule_type DNA !'##residues 1-260 ##label AZI !'##cross-references GB:U34072; NID:g1103843 !'##note sequence extracted from NCBI backbone (NCBIN:126003, !1NCBIP:126004) CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; NAD; oxidoreductase FEATURE !$10-199 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 260 #molecular-weight 26645 #checksum 9155 SEQUENCE /// ENTRY S39737 #type complete TITLE glucose 1-dehydrogenase homolog ywfD - Bacillus subtilis ALTERNATE_NAMES protein ipa-82d CONTAINS probable dehydrogenase (EC 1.1.1.-) ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S39737; E70055 REFERENCE S39655 !$#authors Glaser, P.; Kunst, F.; Arnaud, M.; Coudart, M.P.; Gonzales, !1W.; Hullo, M.F.; Ionescu, M.; Lubochinsky, B.; Marcelino, !1L.; Moszer, I.; Presecan, E.; Santana, M.; Schneider, E.; !1Schweizer, J.; Vertes, A.; Rapoport, G.; Danchin, A. !$#journal Mol. Microbiol. (1993) 10:371-384 !$#title Bacillus subtilis genome project: cloning and sequencing of !1the 97 kb region from 325 degrees to 333 degrees. !$#cross-references MUID:95020537; PMID:7934828 !$#accession S39737 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-255 ##label GLA !'##cross-references EMBL:X73124; NID:g413923; PIDN:CAA51638.1; !1PID:g414006 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1993 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E70055 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-255 ##label KUN !'##cross-references GB:Z99123; GB:AL009126; NID:g2636240; !1PIDN:CAB15799.1; PID:g2636308 !'##experimental_source strain 168 GENETICS !$#gene ywfD CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS NAD; oxidoreductase FEATURE !$8-185 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 255 #molecular-weight 27324 #checksum 6669 SEQUENCE /// ENTRY JC4041 #type complete TITLE D-arabinitol 2-dehydrogenase (EC 1.1.1.-) - yeast (Candida tropicalis) ALTERNATE_NAMES D-arabinitol dehydrogenase (ribulose-forming) ORGANISM #formal_name Candida tropicalis DATE 13-Jun-1995 #sequence_revision 25-Apr-1997 #text_change 11-Jun-1999 ACCESSIONS JC4041; PC4017 REFERENCE JC4041 !$#authors Murray, J.S.; Wong, M.L.; Miyada, C.G.; Switchenko, A.C.; !1Goodman, T.C.; Wong, B. !$#journal Gene (1995) 155:123-128 !$#title Isolation, characterization and expression of the gene that !1encodes D-arabinitol dehydrogenase in Candida tropicalis. !$#cross-references MUID:95212917; PMID:7698655 !$#accession JC4041 !'##molecule_type DNA !'##residues 1-282 ##label MUR !'##cross-references GB:U00675; NID:g392785; PIDN:AAA66355.1; !1PID:g392786 !$#accession PC4017 !'##molecule_type protein !'##residues 110-129;198-205;206-209;225-234 ##label MU2 COMMENT This enzyme is a NAD-dependent short-chain-alcohol !1dehydrogenase. GENETICS !$#gene ard FUNCTION !$#description interconverts D-arabinitol plus NAD with D-ribulose plus !1NADH CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS NAD; oxidoreductase FEATURE !$21-216 #domain short-chain alcohol dehydrogenase homology !8#label SADH\ !$21-51 #region beta-alpha-beta NAD nucleotide-binding fold SUMMARY #length 282 #molecular-weight 30748 #checksum 7773 SEQUENCE /// ENTRY C24706 #type complete TITLE nodulation protein nodG - Rhizobium meliloti plasmid ALTERNATE_NAMES hsnC protein ORGANISM #formal_name Rhizobium meliloti DATE 30-Jun-1988 #sequence_revision 13-Jan-1995 #text_change 11-Jun-1999 ACCESSIONS C24706; S07675; C24193 REFERENCE A93638 !$#authors Debelle, F.; Sharma, S.B. !$#journal Nucleic Acids Res. (1986) 14:7453-7472 !$#title Nucleotide sequence of Rhizobium meliloti RCR2011 genes !1involved in host specificity of nodulation. !$#cross-references MUID:87016382; PMID:3020515 !$#accession C24706 !'##molecule_type DNA !'##residues 1-245 ##label DEB !'##cross-references GB:X04379; NID:g46305; PIDN:CAA27962.1; PID:g46308 !'##experimental_source strain RCR2011 symbiotic plasmid REFERENCE S06395 !$#authors Fisher, R.F.; Swanson, J.A.; Mulligan, J.T.; Long, S.R. !$#journal Genetics (1987) 117:191-201 !$#title Extended region of nodulation genes in Rhizobium meliloti !11021. II. Nucleotide sequence, transcription start sites and !1protein products. !$#accession S07675 !'##molecule_type DNA !'##residues 1-245 ##label FIS !'##experimental_source strain 1021 symbiotic plasmid REFERENCE A94655 !$#authors Horvath, B.; Kondorosi, E.; John, M.; Schmidt, J.; Toeroek, !1I.; Gyoergypal, Z.; Barabas, I.; Wieneke, U.; Schell, J.; !1Kondorosi, A. !$#journal Cell (1986) 46:335-343 !$#title Organization, structure and symbiotic function of Rhizobium !1meliloti nodulation genes determining host specificity for !1alfalfa. !$#cross-references MUID:86272081; PMID:3731273 !$#accession C24193 !'##status significant sequence differences !'##molecule_type DNA !'##cross-references GB:M14052; NID:g152239; PID:g455349 !'##experimental_source strain AK631 (a variant of strain 41) !'##note the sequence reported in this reference is incorrect due to !1multiple frameshift errors COMMENT This is one of several proteins that control host !1specificity of root hair infection and nodulation. GENETICS !$#gene nodG; hsnC !$#genome plasmid CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS host range; nodulation FEATURE !$7-183 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 245 #molecular-weight 26088 #checksum 6343 SEQUENCE /// ENTRY E70027 #type complete TITLE probable 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100) yvaG - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS E70027 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E70027 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-264 ##label KUN !'##cross-references GB:Z99121; GB:AL009126; NID:g2635827; !1PIDN:CAB15364.1; PID:g2635872 !'##experimental_source strain 168 GENETICS !$#gene yvaG CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS NAD; oxidoreductase FEATURE !$8-185 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 264 #molecular-weight 29009 #checksum 187 SEQUENCE /// ENTRY H70046 #type complete TITLE probable 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100) yvrD - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS H70046 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H70046 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-263 ##label KUN !'##cross-references GB:Z99120; GB:Z99121; GB:AL009126; NID:g2635827; !1PIDN:CAB15324.1; PID:g2635832; NID:g2635613; PID:g2635816 !'##experimental_source strain 168 GENETICS !$#gene yvrD CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS NAD; oxidoreductase FEATURE !$8-185 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 263 #molecular-weight 28222 #checksum 1280 SEQUENCE /// ENTRY DEKBR #type complete TITLE ribitol 2-dehydrogenase (EC 1.1.1.56) - Enterobacter aerogenes ORGANISM #formal_name Enterobacter aerogenes DATE 13-Jul-1981 #sequence_revision 13-Jul-1981 #text_change 23-Mar-1995 ACCESSIONS A94585; A00344 REFERENCE A94585 !$#authors Hartley, B.S. !$#submission submitted to the Atlas, June 1977 !$#accession A94585 !'##molecule_type protein !'##residues 1-247 ##label HAR !'##note this enzyme binds the coenzyme nicotine adenine dinucleotide REFERENCE A94480 !$#authors Moore, C.H.; Taylor, S.S.; Smith, M.J.; Hartley, B.S. !$#citation unpublished results, cited by Morris, H.R., Williams, D.H., !1Midwinter, G.G., and Hartley, B.S., Biochem. J. 141, !1701-713, 1974 !$#contents annotation !$#note Cys-30 and Cys-126 are carboxymethylcysteine CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS oxidoreductase FEATURE !$15-189 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 247 #molecular-weight 26317 #checksum 3406 SEQUENCE /// ENTRY DEECSP #type complete TITLE sorbitol-6-phosphate 2-dehydrogenase (EC 1.1.1.140) - Escherichia coli (strain K-12) ALTERNATE_NAMES glucitol-6-phosphate dehydrogenase ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 21-Nov-1997 #text_change 01-Mar-2002 ACCESSIONS E65050; C26725; S11015 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65050 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-259 ##label BLAT !'##cross-references GB:AE000354; GB:U00096; NID:g2367149; !1PIDN:AAC75747.1; PID:g1789057; UWGP:b2705 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A92638 !$#authors Yamada, M.; Saier Jr., M.H. !$#journal J. Biol. Chem. (1987) 262:5455-5463 !$#title Glucitol-specific enzymes of the phosphotransferase system !1in Escherichia coli: nucleotide sequence of the gut operon. !$#cross-references MUID:87194727; PMID:3553176 !$#accession C26725 !'##molecule_type DNA !'##residues 1-67,'C',69-259 ##label YAM !'##cross-references GB:J02708; GB:M36721; NID:g3002464; !1PIDN:AAC13413.1; PID:g146280 REFERENCE S10685 !$#authors Novotny, M.J.; Reizer, J.; Esch, F.; Saier Jr., M.H. !$#journal J. Bacteriol. (1984) 159:986-990 !$#title Purification and properties of D-mannitol-1-phosphate !1dehydrogenase and D-glucitol-6-phosphate dehydrogenase from !1Escherichia coli. !$#cross-references MUID:85006766; PMID:6384188 !$#accession S11015 !'##molecule_type protein !'##residues 1-18,'X',20-31,'X',33-34 ##label JBA GENETICS !$#gene srlD; gutD !$#map_position 58 min CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS NAD; oxidoreductase; phosphotransferase system FEATURE !$3-185 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 259 #molecular-weight 27858 #checksum 285 SEQUENCE /// ENTRY E36516 #type complete TITLE cis-1,2-dihydrobenzene-1,2-diol dehydrogenase (EC 1.3.1.19) - Pseudomonas putida ALTERNATE_NAMES 17K benzene oxidation protein; cis-1,2-dihydrotoluene-1, 2-diol (EC 1.3.1.-) ORGANISM #formal_name Pseudomonas putida DATE 15-Feb-1991 #sequence_revision 06-Jan-1995 #text_change 11-Jun-1999 ACCESSIONS E36516; E29830 REFERENCE A36516 !$#authors Zylstra, G.J.; Gibson, D.T. !$#journal J. Biol. Chem. (1989) 264:14940-14946 !$#title Toluene degradation by Pseudomonas putida F1. Nucleotide !1sequence of the todC1C2BADE genes and their expression in !1Escherichia coli. !$#cross-references MUID:89359301; PMID:2670929 !$#accession E36516 !'##molecule_type DNA !'##residues 1-275 ##label ZYL !'##cross-references GB:J04996; NID:g151600; PIDN:AAA26009.1; !1PID:g151605 !'##experimental_source strain F1 REFERENCE A91848 !$#authors Irie, S.; Doi, S.; Yorifuji, T.; Takagi, M.; Yano, K. !$#journal J. Bacteriol. (1987) 169:5174-5179 !$#title Nucleotide sequencing and characterization of the genes !1encoding benzene oxidation enzymes of Pseudomonas putida. !$#cross-references MUID:88032840; PMID:3667527 !$#accession E29830 !'##molecule_type DNA !'##residues 1-275 ##label IRI !'##experimental_source strain 136R-3 !'##note the authors assume Met-111 as the translation initiator GENETICS !$#gene todD CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS aromatic hydrocarbon catabolism; NAD; oxidoreductase FEATURE !$6-185 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 275 #molecular-weight 28782 #checksum 8035 SEQUENCE /// ENTRY F42409 #type complete TITLE cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase (EC 1.3.1.-) - Pseudomonas pseudoalcaligenes ORGANISM #formal_name Pseudomonas pseudoalcaligenes DATE 04-Mar-1993 #sequence_revision 06-Jan-1995 #text_change 11-Jun-1999 ACCESSIONS F42409 REFERENCE A42409 !$#authors Taira, K.; Hirose, J.; Hayashida, S.; Furukawa, K. !$#journal J. Biol. Chem. (1992) 267:4844-4853 !$#title Analysis of bph operon from the polychlorinated !1biphenyl-degrading strain of Pseudomonas pseudoalcaligenes !1KF707. !$#cross-references MUID:92165849; PMID:1537863 !$#accession F42409 !'##molecule_type DNA !'##residues 1-277 ##label TAI !'##cross-references GB:M83673; NID:g151090; PIDN:AAA25748.1; !1PID:g151096 !'##experimental_source strain KF707 !'##note sequence extracted from NCBI backbone (NCBIN:84014, !1NCBIP:84022) GENETICS !$#gene bphB CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS aromatic hydrocarbon catabolism; oxidoreductase; PCB !1biodegradation FEATURE !$6-185 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 277 #molecular-weight 28929 #checksum 8019 SEQUENCE /// ENTRY JN0814 #type complete TITLE cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase (EC 1.3.1.-) - Pseudomonas sp. ORGANISM #formal_name Pseudomonas sp. DATE 10-Mar-1994 #sequence_revision 06-Jan-1995 #text_change 05-May-2000 ACCESSIONS JN0814; G41858 REFERENCE PN0632 !$#authors Hofer, B.; Eltis, L.D.; Dowling, D.N.; Timmis, K.N. !$#journal Gene (1993) 130:47-55 !$#title Genetic analysis of a Pseudomonas locus encoding a pathway !1for biphenyl/polychlorinated biphenyl degradation. !$#cross-references MUID:93345822; PMID:8344527 !$#accession JN0814 !'##molecule_type DNA !'##residues 1-277 ##label HOF !'##cross-references GB:X66122; NID:g397882; PIDN:CAA46909.1; !1PID:g397883 !'##experimental_source strain LB400 REFERENCE A41858 !$#authors Erickson, B.D.; Mondello, F.J. !$#journal J. Bacteriol. (1992) 174:2903-2912 !$#title Nucleotide sequencing and transcriptional mapping of the !1genes encoding biphenyl dioxygenase, a multicomponent !1polychlorinated-biphenyl-degrading enzyme in Pseudomonas !1strain LB400. !$#cross-references MUID:92234948; PMID:1569021 !$#accession G41858 !'##molecule_type DNA !'##residues 1-22 ##label ERI !'##cross-references GB:M86348; NID:g349602; PIDN:AAB63430.1; !1PID:g151089 !'##experimental_source strain LB400 !'##note sequence extracted from NCBI backbone (NCBIN:97256, !1NCBIP:97265) GENETICS !$#gene bphB CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS aromatic hydrocarbon catabolism; NAD; oxidoreductase; PCB !1biodegradation FEATURE !$6-185 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 277 #molecular-weight 28901 #checksum 8038 SEQUENCE /// ENTRY A35124 #type fragment TITLE cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase (EC 1.3.1.-) - Pseudomonas putida (fragment) ORGANISM #formal_name Pseudomonas putida DATE 03-Aug-1990 #sequence_revision 06-Jan-1995 #text_change 11-Jun-1999 ACCESSIONS A35124 REFERENCE A35124 !$#authors Hayase, N.; Taira, K.; Furukawa, K. !$#journal J. Bacteriol. (1990) 172:1160-1164 !$#title Pseudomonas putida KF715 bphABCD operon encoding biphenyl !1and polychlorinated biphenyl degradation: cloning, analysis, !1and expression in soil bacteria. !$#cross-references MUID:90130279; PMID:2105297 !$#accession A35124 !'##molecule_type DNA !'##residues 1-175 ##label HAY !'##cross-references GB:M33813; NID:g151105; PIDN:AAA25755.1; !1PID:g151106 !'##experimental_source strain KF715 GENETICS !$#gene bphB CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS aromatic hydrocarbon catabolism; oxidoreductase; PCB !1biodegradation FEATURE !$1-88 #domain short-chain alcohol dehydrogenase homology !8(fragment) #label SADH SUMMARY #length 175 #checksum 5187 SEQUENCE /// ENTRY A53419 #type complete TITLE 2,3-dihydroxy-4-phenylhexa-4,6-diene dehydrogenase (EC 1.3.1.-) - Rhodococcus globerulus ORGANISM #formal_name Rhodococcus globerulus DATE 25-May-1994 #sequence_revision 06-Jan-1995 #text_change 11-Jun-1999 ACCESSIONS A53419 REFERENCE A53419 !$#authors Asturias, J.A.; Eltis, L.D.; Prucha, M.; Timmis, K.N. !$#journal J. Biol. Chem. (1994) 269:7807-7815 !$#title Analysis of three 2,3-dihydroxybiphenyl 1,2-dioxygenases !1found in Rhodococcus globerulus P6. Identification of a new !1family of extradiol dioxygenases. !$#cross-references MUID:94171820; PMID:8126007 !$#accession A53419 !'##molecule_type DNA !'##residues 1-280 ##label AST !'##cross-references GB:X75633; NID:g473115; PIDN:CAA53296.1; !1PID:g581506 !'##experimental_source strain P6 CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS aromatic hydrocarbon catabolism; oxidoreductase; PCB !1biodegradation FEATURE !$6-185 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 280 #molecular-weight 29389 #checksum 722 SEQUENCE /// ENTRY A31841 #type complete TITLE bile acid dehydroxylase - Eubacterium sp. (strain VPI 12708) ALTERNATE_NAMES 27K-2 protein (cholic acid-induced); baiA2 27K protein ORGANISM #formal_name Eubacterium sp. DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 18-Aug-2000 ACCESSIONS A31841; E37844 REFERENCE A91886 !$#authors White, W.B.; Franklund, C.V.; Coleman, J.P.; Hylemon, P.B. !$#journal J. Bacteriol. (1988) 170:4555-4561 !$#title Evidence for a multigene family involved in bile acid !17-dehydroxylation in Eubacterium sp. strain VPI 12708. !$#cross-references MUID:89008068; PMID:3170477 !$#accession A31841 !'##molecule_type DNA !'##residues 1-249 ##label WHI !'##cross-references GB:M22623; NID:g290675; PIDN:AAB61150.1; !1PID:g290676 REFERENCE A37844 !$#authors Mallonee, D.H.; White, W.B.; Hylemon, P.B. !$#journal J. Bacteriol. (1990) 172:7011-7019 !$#title Cloning and sequencing of a bile acid-inducible operon from !1Eubacterium sp. strain VPI 12708. !$#cross-references MUID:91072253; PMID:2254270 !$#accession E37844 !'##molecule_type DNA !'##residues 1-249 ##label MAL !'##cross-references GB:U57489; GB:M36292; NID:g1381562; !1PIDN:AAC45414.1; PID:g1381567 CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology FEATURE !$7-188 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 249 #molecular-weight 26538 #checksum 8274 SEQUENCE /// ENTRY B37762 #type complete TITLE bile acid 7-dehydroxylase - Eubacterium sp. (strain VPI 12708) ORGANISM #formal_name Eubacterium sp. DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 18-Aug-2000 ACCESSIONS B37762; A26938; A28212 REFERENCE A37762 !$#authors Gopal-Srivastava, R.; Mallonee, D.H.; White, W.B.; Hylemon, !1P.B. !$#journal J. Bacteriol. (1990) 172:4420-4426 !$#title Multiple copies of a bile acid-inducible gene in Eubacterium !1sp. strain VPI 12708. !$#cross-references MUID:90330548; PMID:2376563 !$#accession B37762 !'##molecule_type DNA !'##residues 1-249 ##label GOP !'##cross-references GB:M34658; NID:g148521; PIDN:AAB61155.1; !1PID:g148522 REFERENCE A26938 !$#authors Coleman, J.P.; White, W.B.; Hylemon, P.B. !$#journal J. Bacteriol. (1987) 169:1516-1521 !$#title Molecular cloning of bile acid 7-dehydroxylase from !1Eubacterium sp. strain VPI 12708. !$#cross-references MUID:87165759; PMID:3549693 !$#accession A26938 !'##molecule_type DNA !'##residues 1-55 ##label COL !'##cross-references GB:M15813; NID:g148513; PIDN:AAB61153.1; !1PID:g148514 !'##experimental_source strain VPI 12708 REFERENCE A28212 !$#authors Coleman, J.P.; White, W.B.; Lijewski, M.; Hylemon, P.B. !$#journal J. Bacteriol. (1988) 170:2070-2077 !$#title Nucleotide sequence and regulation of a gene involved in !1bile acid 7-dehydroxylation by Eubacterium sp. strain VPI !112708. !$#cross-references MUID:88197993; PMID:2834320 !$#accession A28212 !'##molecule_type DNA !'##residues 1-158,'YQQG',163-249 ##label CO2 !'##cross-references GB:M19654; NID:g148515; PIDN:AAB61154.1; !1PID:g148516 !'##experimental_source strain VPI 12708 CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology FEATURE !$7-188 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 249 #molecular-weight 26658 #checksum 9638 SEQUENCE /// ENTRY D69930 #type complete TITLE probable 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100) yoxD - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS D69930; S01270 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D69930 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-238 ##label KUN !'##cross-references GB:Z99114; GB:AL009126; NID:g2634230; !1PIDN:CAB13743.1; PID:g2634244 !'##experimental_source strain 168 REFERENCE S01270 !$#authors Carrigan, C.M.; Haarsma, J.A.; Smith, M.T.; Wake, R.G. !$#journal Nucleic Acids Res. (1987) 15:8501-8509 !$#title Sequence features of the replication terminus of the !1Bacillus subtilis chromosome. !$#cross-references MUID:88040469; PMID:3118336 !$#accession S01270 !'##molecule_type DNA !'##residues 62-238 ##label CAR !'##cross-references EMBL:X06168; NID:g40205; PIDN:CAA29533.1; !1PID:g809662 GENETICS !$#gene yoxD CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS NAD; oxidoreductase FEATURE !$7-186 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 238 #molecular-weight 25299 #checksum 2171 SEQUENCE /// ENTRY S00812 #type complete TITLE glucose 1-dehydrogenase (EC 1.1.1.47) A - Bacillus megaterium ORGANISM #formal_name Bacillus megaterium DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS S00812 REFERENCE S00812 !$#authors Heilmann, H.J.; Maegert, H.J.; Gassen, H.G. !$#journal Eur. J. Biochem. (1988) 174:485-490 !$#title Identification and isolation of glucose dehydrogenase genes !1of Bacillus megaterium M1286 and their expression in !1Escherichia coli. !$#cross-references MUID:88271315; PMID:3134196 !$#accession S00812 !'##molecule_type DNA !'##residues 1-261 ##label HEI !'##cross-references EMBL:X12370; NID:g39634; PIDN:CAA30931.1; !1PID:g39635 !'##note the sequence from Fig. 6 is inconsistent with that from Fig. 3 !1in having 208-Asn and 257-Glu GENETICS !$#gene gdhA CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS oxidoreductase FEATURE !$8-189 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 261 #molecular-weight 28187 #checksum 1498 SEQUENCE /// ENTRY A57149 #type complete TITLE gluconate 5-dehydrogenase (EC 1.1.1.69) - Gluconobacter oxydans ORGANISM #formal_name Gluconobacter oxydans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A57149; S48845 REFERENCE A57149 !$#authors Klasen, R.; Bringer-Meyer, S.; Sahm, H. !$#journal J. Bacteriol. (1995) 177:2637-2643 !$#title Biochemical characterization and sequence analysis of the !1gluconate:NADP 5-oxidoreductase gene from Gluconobacter !1oxydans. !$#cross-references MUID:95270578; PMID:7751271 !$#accession A57149 !'##status preliminary !'##molecule_type DNA !'##residues 1-256 ##label KLA !'##cross-references GB:X80019; NID:g563365; PIDN:CAA56322.1; !1PID:g563366 CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS NAD; oxidoreductase FEATURE !$12-191 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 256 #molecular-weight 27256 #checksum 9931 SEQUENCE /// ENTRY S17711 #type complete TITLE probable dehydrogenase (EC 1.1.1.-) kduD - Erwinia chrysanthemi ORGANISM #formal_name Erwinia chrysanthemi DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S17711 REFERENCE S17709 !$#authors Condemine, G.; Robert-Baudouy, J. !$#journal Mol. Microbiol. (1991) 5:2191-2202 !$#title Analysis of an Erwinia chrysanthemi gene cluster involved in !1pectin degradation. !$#cross-references MUID:92114798; PMID:1766386 !$#accession S17711 !'##molecule_type DNA !'##residues 1-253 ##label CON !'##cross-references EMBL:X62073; NID:g4157974; PIDN:CAA43989.1; !1PID:g48986 GENETICS !$#gene kduD CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS NAD; oxidoreductase FEATURE !$11-189 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 253 #molecular-weight 27275 #checksum 5234 SEQUENCE /// ENTRY S05398 #type complete TITLE granaticin polyketide ketoreductase (EC 1.1.1.-) - Streptomyces violaceoruber ALTERNATE_NAMES 3-hydroxyacyl-CoA dehydrogenase homolog 2; granaticin polyketide synthase chain 6 ORGANISM #formal_name Streptomyces violaceoruber DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 11-May-2000 ACCESSIONS S05398; T46535 REFERENCE S05393 !$#authors Sherman, D.H.; Malpartida, F.; Bibb, M.J.; Kieser, H.M.; !1Bibb, M.J.; Hopwood, D.A. !$#journal EMBO J. (1989) 8:2717-2725 !$#title Structure and deduced function of the granaticin-producing !1polyketide synthase gene cluster of Streptomyces !1violaceoruber Tue22. !$#cross-references MUID:90060034; PMID:2583128 !$#accession S05398 !'##molecule_type DNA !'##residues 1-249 ##label SHE !'##cross-references EMBL:X16144; NID:g47976; PIDN:CAA34262.1; !1PID:g47977 REFERENCE Z23045 !$#authors Ichinose, K.; Bedford, D.J.; Tornus, D.; Bechthold, A.; !1Bibb, M.J.; Revill, W.P.; Floss, H.G.; Hopwood, D.A. !$#journal Chem. Biol. (1998) 5:647-659 !$#title The granaticin biosynthetic gene cluster of Streptomyces !1violaceoruber Tu22: sequence analysis and expression in a !1heterologous host. !$#cross-references MUID:99051446; PMID:9831526 !$#accession T46535 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-249 ##label ICH !'##cross-references EMBL:AJ011500; PIDN:CAA09651.1 !'##experimental_source strain Tu22 GENETICS !$#gene graIII !$#note gra-orf6 CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS NAD; oxidoreductase FEATURE !$9-187 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 249 #molecular-weight 25977 #checksum 393 SEQUENCE /// ENTRY A42468 #type complete TITLE 7alpha-hydroxysteroid dehydrogenase (EC 1.1.1.159) - Eubacterium sp. (strain VPI 12708) ORGANISM #formal_name Eubacterium sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A42468; A36439 REFERENCE A42468 !$#authors Baron, S.F.; Franklund, C.V.; Hylemon, P.B. !$#journal J. Bacteriol. (1991) 173:4558-4569 !$#title Cloning, sequencing, and expression of the gene coding for !1bile acid 7alpha-hydroxysteroid dehydrogenase from !1Eubacterium sp. strain VPI 12708. !$#cross-references MUID:91310560; PMID:1856160 !$#accession A42468 !'##status preliminary !'##molecule_type DNA !'##residues 1-266 ##label BAR !'##cross-references GB:M58743 !'##note the authors translated the codon CCC for residue 95 as Phe, and !1CCG for residue 106 as Phe REFERENCE A36439 !$#authors Franklund, C.V.; de Prada, P.; Hylemon, P.B. !$#journal J. Biol. Chem. (1990) 265:9842-9849 !$#title Purification and characterization of a microbial, !1NADP-dependent bile acid 7alpha-hydroxysteroid !1dehydrogenase. !$#cross-references MUID:90277676; PMID:2351678 !$#accession A36439 !'##status preliminary !'##molecule_type protein !'##residues 1-22 ##label FRA CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS NAD; oxidoreductase FEATURE !$6-188 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 266 #molecular-weight 28543 #checksum 3689 SEQUENCE /// ENTRY A38527 #type complete TITLE 7alpha-hydroxysteroid dehydrogenase (EC 1.1.1.159) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS A38527; E64918; JT0951 REFERENCE A38527 !$#authors Yoshimoto, T.; Higashi, H.; Kanatani, A.; Lin, X.S.; Nagai, !1H.; Oyama, H.; Kurazono, K.; Tsuru, D. !$#journal J. Bacteriol. (1991) 173:2173-2179 !$#title Cloning and sequencing of the 7alpha-hydroxysteroid !1dehydrogenase gene from Escherichia coli HB101 and !1characterization of the expressed enzyme. !$#cross-references MUID:91177803; PMID:2007545 !$#accession A38527 !'##status preliminary !'##molecule_type DNA !'##residues 1-255 ##label YOS !'##cross-references GB:D10497; NID:g216570; PIDN:BAA01384.1; !1PID:g912437; GB:D90475 !'##experimental_source strain HB101 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64918 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-255 ##label BLAT !'##cross-references GB:AE000257; GB:U00096; NID:g1787898; !1PIDN:AAC74691.1; PID:g1787905; UWGP:b1619 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene hdhA; hsdh !$#start_codon GTG FUNCTION !$#description catalyzes oxidation 7-alpha-hydroxyl group of bile acids and !1alcohols both in their free and conjugated forms CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS NAD; oxidoreductase FEATURE !$12-190 #domain short-chain alcohol dehydrogenase homology !8#label SADH\ !$159 #active_site Tyr #status predicted SUMMARY #length 255 #molecular-weight 26778 #checksum 4084 SEQUENCE /// ENTRY S01065 #type complete TITLE probable dehydrogenase (EC 1.1.1.-) fixR - Bradyrhizobium japonicum ORGANISM #formal_name Bradyrhizobium japonicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S01065 REFERENCE S01065 !$#authors Thoeny, B.; Fischer, H.M.; Anthamatten, D.; Bruderer, T.; !1Hennecke, H. !$#journal Nucleic Acids Res. (1987) 15:8479-8499 !$#title The symbiotic nitrogen fixation regulatory operon (fixRnifA) !1of Bradyrhizobium japonicum is expressed aerobically and is !1subject to a novel, nifA-independent type of activation. !$#cross-references MUID:88040468; PMID:3313281 !$#accession S01065 !'##molecule_type DNA !'##residues 1-278 ##label THO !'##cross-references EMBL:X06167; NID:g39526; PIDN:CAA29530.1; !1PID:g580771 GENETICS !$#gene fixR !$#start_codon GTG CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS NAD; oxidoreductase FEATURE !$37-220 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 278 #molecular-weight 29715 #checksum 3435 SEQUENCE /// ENTRY S25286 #type complete TITLE probable dehydrogenase (EC 1.1.1.-) ltdh - Leishmania tarentolae ALTERNATE_NAMES antifolate resistance protein; methotrexate resistance protein ORGANISM #formal_name Leishmania tarentolae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S25286; S21355 REFERENCE S25286 !$#authors Papadopoulou, B.; Roy, G.; Ouellette, M. !$#journal EMBO J. (1992) 11:3601-3608 !$#title A novel antifolate resistance gene on the amplified H circle !1of Leishmania. !$#cross-references MUID:93010951; PMID:1396560 !$#accession S25286 !'##molecule_type DNA !'##residues 1-289 ##label PAP !'##cross-references EMBL:Z11978; NID:g9661; PIDN:CAA78031.1; PID:g9662 GENETICS !$#gene ltdh CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS NAD; oxidoreductase FEATURE !$8-226 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 289 #molecular-weight 30743 #checksum 9317 SEQUENCE /// ENTRY A45168 #type complete TITLE probable 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100) - Leishmania major ALTERNATE_NAMES H region methotrexate resistance protein ORGANISM #formal_name Leishmania major DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A45168 REFERENCE A45168 !$#authors Callahan, H.L.; Beverley, S.M. !$#journal J. Biol. Chem. (1992) 267:24165-24168 !$#title A member of the aldoketo reductase family confers !1methotrexate resistance in Leishmania. !$#cross-references MUID:93077490; PMID:1339441 !$#accession A45168 !'##status preliminary !'##molecule_type DNA !'##residues 1-287 ##label CAL !'##cross-references GB:L01699; NID:g159347; PIDN:AAA29249.1; !1PID:g159348 CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS NAD; oxidoreductase FEATURE !$7-224 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 287 #molecular-weight 30440 #checksum 9743 SEQUENCE /// ENTRY DEECDB #type complete TITLE 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase (EC 1.3.1.28) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 01-Mar-2002 ACCESSIONS A91904; A91903; B64793; B32046; C32047 REFERENCE A91904 !$#authors Liu, J.; Duncan, K.; Walsh, C.T. !$#journal J. Bacteriol. (1989) 171:791-798 !$#title Nucleotide sequence of a cluster of Escherichia coli !1enterobactin biosynthesis genes: identification of entA and !1purification of its product 2,3-dihydro-2, !13-dihydroxybenzoate dehydrogenase. !$#cross-references MUID:89123155; PMID:2521622 !$#accession A91904 !'##molecule_type DNA !'##residues 1-248 ##label LIU !'##cross-references GB:M24148; NID:g304949; PIDN:AAA16103.1; !1PID:g450382 !'##note residues 1-14 were confirmed by protein sequencing REFERENCE A91903 !$#authors Nahlik, M.S.; Brickman, T.J.; Ozenberger, B.A.; McIntosh, !1M.A. !$#journal J. Bacteriol. (1989) 171:784-790 !$#title Nucleotide sequence and transcriptional organization of the !1Escherichia coli enterobactin biosynthesis cistrons entB and !1entA. !$#cross-references MUID:89123154; PMID:2521621 !$#accession A91903 !'##molecule_type DNA !'##residues 1-248 ##label NAH !'##cross-references GB:M24143; NID:g341118; PIDN:AAA76836.1; !1PID:g522183 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64793 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-248 ##label BLAT !'##cross-references GB:AE000165; GB:U00096; NID:g1786808; !1PIDN:AAC73697.1; PID:g1786812; UWGP:b0596 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene entA !$#map_position 13 min COMPLEX homooctamer FUNCTION !$#description catalyzes the NAD-dependent oxidation of 2,3-dihydro-2, !13-dihydroxybenzoate to 2,3-dihydroxybenzoate CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS enterobactin biosynthesis; homooctamer; NAD; oxidoreductase FEATURE !$6-175 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 248 #molecular-weight 26249 #checksum 1750 SEQUENCE /// ENTRY A69615 #type complete TITLE 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase (EC 1.3.1.28) - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 05-Dec-1997 #sequence_revision 02-Jul-1998 #text_change 16-Jun-2000 ACCESSIONS A69615; PN0683 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69615 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-261 ##label KUN !'##cross-references GB:Z99120; GB:AL009126; NID:g2635613; !1PIDN:CAB15190.1; PID:g2635697 !'##experimental_source strain 168 REFERENCE PN0683 !$#authors Adams, R.; Schumann, W. !$#journal Gene (1993) 133:119-121 !$#title Cloning and mapping of the Bacillus subtilis locus !1homologous to Escherichia coli ent genes. !$#cross-references MUID:94040785; PMID:8224884 !$#accession PN0683 !'##molecule_type DNA !'##residues 61-145,'D',147-230,'MRC',235-246,'RCIFMRRCAT' ##label ADA !'##cross-references GB:L08644; NID:g348057; PIDN:AAA16899.1; !1PID:g348058 GENETICS !$#gene dhbA FUNCTION !$#description catalyzes the oxidation of 2,3-dihydro-2,3-dihydroxybenzoate !1to 2,3-dihydroxybenzoate by NAD+ CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS enterobactin biosynthesis; NAD; oxidoreductase FEATURE !$9-188 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 261 #molecular-weight 27494 #checksum 1802 SEQUENCE /// ENTRY A65017 #type complete TITLE probable 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100) yfeF - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS A65017 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65017 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-285 ##label BLAT !'##cross-references GB:AE000330; GB:U00096; NID:g1788763; !1PIDN:AAC75479.1; PID:g1788766; UWGP:b2426 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yfeF CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS NAD; oxidoreductase FEATURE !$29-208 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 285 #molecular-weight 30581 #checksum 4680 SEQUENCE /// ENTRY S10707 #type complete TITLE 20beta-hydroxysteroid dehydrogenase (EC 1.1.1.-) - Streptomyces exfoliatus ORGANISM #formal_name Streptomyces exfoliatus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S10707 REFERENCE S10707 !$#authors Marekov, L.; Krook, M.; Joernvall, H. !$#journal FEBS Lett. (1990) 266:51-54 !$#title Prokaryotic 20-beta-hydroxysteroid dehydrogenase is an !1enzyme of the 'short-chain, non-metalloenzyme' alcohol !1dehydrogenase type. !$#cross-references MUID:90306362; PMID:2194840 !$#accession S10707 !'##status preliminary !'##molecule_type protein !'##residues 1-255 ##label MAR CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS NAD; oxidoreductase FEATURE !$7-183 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 255 #molecular-weight 26484 #checksum 9557 SEQUENCE /// ENTRY S47054 #type complete TITLE probable dehydrogenase (EC 1.1.1.-) - Xanthobacter sp. ALTERNATE_NAMES hypothetical protein 4 ORGANISM #formal_name Xanthobacter sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S47054 REFERENCE S47051 !$#authors Swaving, J.; Weijers, C.A.G.M.; van Ooyen, A.J.J.; de Bont, !1J.A.M. !$#submission submitted to the EMBL Data Library, June 1994 !$#description Plementation of Xanthobacter Py2 mutants in epoxyalkane !1degradation; expression and nucleotide sequence of the !1complementing DNA fragment. !$#accession S47054 !'##molecule_type DNA !'##residues 1-250 ##label SWA !'##cross-references EMBL:X79863; NID:g520947; PIDN:CAA56244.1; !1PID:g581833 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS NAD; oxidoreductase FEATURE !$3-186 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 250 #molecular-weight 26143 #checksum 1745 SEQUENCE /// ENTRY B65059 #type complete TITLE probable dehydrogenase (EC 1.1.1.-) b2774 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS B65059 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65059 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-286 ##label BLAT !'##cross-references GB:AE000361; GB:U00096; NID:g2367160; !1PIDN:AAC75816.1; PID:g1789135; UWGP:b2774 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS NAD; oxidoreductase FEATURE !$44-222 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 286 #molecular-weight 31010 #checksum 2667 SEQUENCE /// ENTRY H64981 #type complete TITLE probable dehydrogenase (EC 1.1.1.-) yohF - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS H64981 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64981 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-253 ##label BLAT !'##cross-references GB:AE000303; GB:U00096; NID:g1788456; !1PIDN:AAC75198.1; PID:g1788459; UWGP:b2137 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yohF CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS NAD; oxidoreductase FEATURE !$3-184 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 253 #molecular-weight 26951 #checksum 9738 SEQUENCE /// ENTRY S34678 #type complete TITLE short-chain alcohol dehydrogenase (EC 1.1.1.-) - Norway spruce ORGANISM #formal_name Picea abies #common_name Norway spruce DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S34678 REFERENCE S34678 !$#authors Ernst, D. !$#submission submitted to the EMBL Data Library, July 1993 !$#accession S34678 !'##status preliminary !'##molecule_type mRNA !'##residues 1-271 ##label ERN !'##cross-references EMBL:X74115; NID:g395222; PIDN:CAA52213.1; !1PID:g395223 CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS alcohol metabolism; oxidoreductase FEATURE !$22-210 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 271 #molecular-weight 28724 #checksum 150 SEQUENCE /// ENTRY A48674 #type complete TITLE tropinone reductase (EC 1.1.1.236) I - jimsonweed ORGANISM #formal_name Datura stramonium #common_name jimsonweed, common thornapple DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A48674 REFERENCE A48674 !$#authors Nakajima, K.; Hashimoto, T.; Yamada, Y. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:9591-9595 !$#title Two tropinone reductases with different stereospecificities !1are short-chain dehydrogenases evolved from a common !1ancestor. !$#cross-references MUID:94022421; PMID:8415746 !$#accession A48674 !'##status preliminary !'##molecule_type mRNA !'##residues 1-273 ##label NAK !'##cross-references GB:L20473; NID:g424159; PIDN:AAA33281.1; !1PID:g424160 CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS oxidoreductase FEATURE !$22-202 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 273 #molecular-weight 29617 #checksum 9747 SEQUENCE /// ENTRY E47069 #type complete TITLE (R,R)-butanediol dehydrogenase (EC 1.1.1.4) - Klebsiella terrigena ALTERNATE_NAMES acetoin (diacetyl) reductase ORGANISM #formal_name Klebsiella terrigena DATE 21-Sep-1993 #sequence_revision 11-Apr-1997 #text_change 18-Jul-2001 ACCESSIONS E47069 REFERENCE A47069 !$#authors Blomqvist, K.; Nikkola, M.; Lehtovaara, P.; Suihko, M.L.; !1Airaksinen, U.; Straby, K.B.; Knowles, J.K.; Penttila, M.E. !$#journal J. Bacteriol. (1993) 175:1392-1404 !$#title Characterization of the genes of the 2,3-butanediol operons !1from Klebsiella terrigena and Enterobacter aerogenes. !$#cross-references MUID:93186707; PMID:8444801 !$#accession E47069 !'##molecule_type DNA !'##residues 1-241 ##label BLO !'##cross-references GB:L04507; NID:g149170; PIDN:AAA25056.1; !1PID:g149173 !'##experimental_source VTT-E-74023 !'##note sequence extracted from NCBI backbone (NCBIN:126766, !1NCBIP:126769) !'##note this enzyme was shown in a cell-free extract after transfection !1into E. coli to reduce acetoin with NADH COMMENT This enzyme converts acetoin to 2,3-butanediol with NADH as !1a reductant. It also can convert diacetyl into acetoin with !1NADH as a reductant, as does acetoin dehydrogenase (EC !11.1.1.5). GENETICS !$#gene budC CLASSIFICATION #superfamily ribitol dehydrogenase; short-chain alcohol !1dehydrogenase homology KEYWORDS NAD; oxidoreductase FEATURE !$3-183 #domain short-chain alcohol dehydrogenase homology !8#label SADH\ !$3-33 #region beta-alpha-beta NAD nucleotide-binding fold SUMMARY #length 241 #molecular-weight 25313 #checksum 6326 SEQUENCE /// ENTRY S48029 #type complete TITLE enoyl-[acyl-carrier-protein] reductase (NADH2) (EC 1.3.1.9) - Escherichia coli (strain K-12) ALTERNATE_NAMES enoyl-ACP reductase; short-chain alcohol dehydrogenase homolog envM ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S48029; A47681; C64877 REFERENCE S48029 !$#authors Kater, M.M.; Koningstein, G.M.; Nijkamp, H.J.J.; Stuitje, !1A.R. !$#journal Plant Mol. Biol. (1994) 25:771-790 !$#title The use of a hybrid genetic system to study the functional !1relationship between prokaryotic and plant multi-enzyme !1fatty acid synthetase complexes. !$#cross-references MUID:94355651; PMID:8075395 !$#accession S48029 !'##status preliminary !'##molecule_type DNA !'##residues 1-262 ##label KAT !'##cross-references EMBL:X78733; NID:g587105; PIDN:CAA55381.1; !1PID:g587106 !'##experimental_source strain K-12, substrain W3110 REFERENCE A47681 !$#authors Bergler, H.; Hogenauer, G.; Turnowsky, F. !$#journal J. Gen. Microbiol. (1992) 138:2093-2100 !$#title Sequences of the envM gene and of two mutated alleles in !1Escherichia coli. !$#cross-references MUID:93123967; PMID:1364817 !$#accession A47681 !'##status preliminary !'##molecule_type DNA !'##residues 1-262 ##label BER !'##cross-references GB:M97219; NID:g145850; PIDN:AAA17755.1; !1PID:g145851 !'##note sequence extracted from NCBI backbone (NCBIN:121825, !1NCBIP:121826) REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64877 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-262 ##label BLAT !'##cross-references GB:AE000227; GB:U00096; NID:g1787543; !1PIDN:AAC74370.1; PID:g1787545; UWGP:b1288 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene fabI; envM FUNCTION !$#description catalyzes reduction by NADH of enoyl-acyl-carrier-protein to !1the corresponding fatty acid acylated-carrier protein !$#pathway fatty acid biosynthesis !$#note inhibited by palmitoyl-CoA and diazaborine CLASSIFICATION #superfamily enoyl-[acyl-carrier-protein] reductase (NADH); !1short-chain alcohol dehydrogenase homology KEYWORDS fatty acid biosynthesis; homotetramer; inner membrane; NAD; !1oxidoreductase FEATURE !$7-190 #domain short-chain alcohol dehydrogenase homology !8#label SADH\ !$9-35 #region NAD binding SUMMARY #length 262 #molecular-weight 27864 #checksum 2286 SEQUENCE /// ENTRY B43729 #type complete TITLE enoyl-[acyl-carrier-protein] reductase (NADH2) (EC 1.3.1.9) - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS B43729; S70724 REFERENCE A43729 !$#authors Turnowsky, F.; Fuchs, K.; Jeschek, C.; Hoegenauer, G. !$#journal J. Bacteriol. (1989) 171:6555-6565 !$#title envM genes of Salmonella typhimurium and Escherichia coli. !$#cross-references MUID:90078098; PMID:2687243 !$#accession B43729 !'##status preliminary !'##molecule_type DNA !'##residues 1-262 ##label TUR !'##cross-references GB:M31806; NID:g153953; PIDN:AAA27059.1; !1PID:g153955 REFERENCE S70719 !$#authors Qi, S.Y.; Li, Y.; Szyroki, A.; Giles, I.G.; Moir, A.; !1O'Connor, C.D. !$#journal Mol. Microbiol. (1995) 17:523-531 !$#title Salmonella typhimurium responses to a bactericidal protein !1from human neutrophils. !$#cross-references MUID:96100451; PMID:8559071 !$#accession S70724 !'##molecule_type protein !'##residues 'X',3-4,'X',6-11 ##label QIS !'##experimental_source strain SL1344 GENETICS !$#gene envM FUNCTION !$#description catalyzes reduction by NADH of enoyl-acyl-carrier-protein to !1the corresponding fatty acid acylated-carrier protein !$#pathway fatty acid biosynthesis !$#note inhibited by diazaborine CLASSIFICATION #superfamily enoyl-[acyl-carrier-protein] reductase (NADH); !1short-chain alcohol dehydrogenase homology KEYWORDS fatty acid biosynthesis; inner membrane; NAD; oxidoreductase FEATURE !$7-190 #domain short-chain alcohol dehydrogenase homology !8#label SADH\ !$9-35 #region NAD binding SUMMARY #length 262 #molecular-weight 27761 #checksum 2093 SEQUENCE /// ENTRY B64139 #type complete TITLE enoyl-[acyl-carrier-protein] reductase (NADH2) (EC 1.3.1.9) - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS B64139 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession B64139 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-295 ##label TIGR !'##cross-references GB:U32846; GB:L42023; NID:g3212237; !1PIDN:AAC23379.1; PID:g1574591; TIGR:HI1734 GENETICS !$#gene fabI; envM !$#start_codon GTG FUNCTION !$#description catalyzes reduction by NADH of enoyl-acyl-carrier-protein to !1the corresponding fatty acid acylated-carrier protein !$#pathway fatty acid biosynthesis CLASSIFICATION #superfamily enoyl-[acyl-carrier-protein] reductase (NADH); !1short-chain alcohol dehydrogenase homology KEYWORDS fatty acid biosynthesis; inner membrane; NAD; oxidoreductase FEATURE !$9-35 #region NAD binding\ !$40-223 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 295 #molecular-weight 31994 #checksum 6301 SEQUENCE /// ENTRY S74996 #type complete TITLE enoyl-[acyl-carrier-protein] reductase (NADH2) (EC 1.3.1.9) - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein slr1051 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S74996 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74996 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-278 ##label KAN !'##cross-references EMBL:D90902; GB:AB001339; NID:g1652027; !1PIDN:BAA17036.1; PID:g1652111 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene envM FUNCTION !$#description catalyzes reduction by NADH of enoyl-acyl-carrier-protein to !1the corresponding fatty acid acylated-carrier protein !$#pathway fatty acid biosynthesis CLASSIFICATION #superfamily enoyl-[acyl-carrier-protein] reductase (NADH); !1short-chain alcohol dehydrogenase homology KEYWORDS fatty acid biosynthesis; NAD; oxidoreductase FEATURE !$27-212 #domain short-chain alcohol dehydrogenase homology !8#label SADH SUMMARY #length 278 #molecular-weight 29774 #checksum 6593 SEQUENCE /// ENTRY DEHUE7 #type complete TITLE estradiol 17beta-dehydrogenase (EC 1.1.1.62) type 1 [validated] - human ALTERNATE_NAMES 17beta-estradiol dehydrogenase; 17beta-hydroxysteroid dehydrogenase ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 08-Dec-2000 ACCESSIONS A36081; S29288; S01654; S43212; A40146; A60440; A21031; !1A60628; G02067; A37190; A37239 REFERENCE A36081 !$#authors Luu-The, V.; Labrie, C.; Simard, J.; Lachance, Y.; Zhao, !1H.F.; Couet, J.; Leblanc, G.; Labrie, F. !$#journal Mol. Endocrinol. (1990) 4:268-275 !$#title Structure of two in tandem human 17beta-hydroxysteroid !1dehydrogenase genes. !$#cross-references MUID:90231340; PMID:2330005 !$#accession A36081 !'##molecule_type DNA !'##residues 1-328 ##label LUU !'##cross-references GB:M27138; NID:g181950; PIDN:AAB16941.1; !1PID:g181951 REFERENCE S29288 !$#authors Peltoketo, H.; Isomaa, V.; Vihko, R. !$#journal Eur. J. Biochem. (1992) 209:459-466 !$#title Genomic organization and DNA sequences of human !117beta-hydroxysteroid dehydrogenase genes and flanking !1regions. Localization of multiple Alu sequences and putative !1cis-acting elements. !$#cross-references MUID:93011163; PMID:1327779 !$#accession S29288 !'##molecule_type DNA !'##residues 1-328 ##label PEL !'##cross-references EMBL:M84472; NID:g806392; PIDN:AAB16942.1; !1PID:g177127 !'##note the authors did not translate the codon for residue 1 !'##note the authors translated the codon AAC for residue 233 as Asp REFERENCE S01654 !$#authors Peltoketo, H.; Isomaa, V.; Maeentausta, O.; Vihko, R. !$#journal FEBS Lett. (1988) 239:73-77 !$#title Complete amino acid sequence of human placental !117-beta-hydroxysteroid dehydrogenase deduced from cDNA. !$#cross-references MUID:89031223; PMID:2846351 !$#accession S01654 !'##molecule_type mRNA !'##residues 2-328 ##label PEL2 !'##cross-references GB:X13440; NID:g23364; PIDN:CAA31792.1; PID:g23365 !$#accession S43212 !'##molecule_type protein !'##residues 2-24;53-68;205-223 ##label PE2 REFERENCE A40146 !$#authors Luu The, V.; Labrie, C.; Zhao, H.F.; Couet, J.; Lachance, !1Y.; Simard, J.; Leblanc, G.; Cote, J.; Berube, D.; Gagne, !1R.; Labrie, F. !$#journal Mol. Endocrinol. (1989) 3:1301-1309 !$#title Characterization of cDNAs for human estradiol !117beta-dehydrogenase and assignment of the gene to !1chromosome 17: evidence of two mRNA species with distinct !15'-termini in human placenta. !$#cross-references MUID:89384667; PMID:2779584 !$#accession A40146 !'##molecule_type mRNA !'##residues 1-328 ##label THE !'##cross-references GB:M27138; NID:g181950; PIDN:AAB16941.1; !1PID:g181951 REFERENCE A60440 !$#authors Gast, M.J.; Sims, H.F.; Murdock, G.L.; Gast, P.M.; Strauss, !1A.W. !$#journal Am. J. Obstet. Gynecol. (1989) 161:1726-1731 !$#title Isolation and sequencing of a complementary deoxyribonucleic !1acid clone encoding human placental 17beta-estradiol !1dehydrogenase: identification of the putative cofactor !1binding site. !$#cross-references MUID:90102621; PMID:2603933 !$#accession A60440 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 6-68,'G',70-91,'EAWAGAAG',102-158,160-178,'P',181-311,'A', !1313-328 ##label GAS REFERENCE A21031 !$#authors Murdock, G.L.; Chin, C.C.; Offord, R.E.; Bradshaw, R.A.; !1Warren, J.C. !$#journal J. Biol. Chem. (1983) 258:11460-11464 !$#title Human placental estradiol 17-beta-dehydrogenase. !1Identification of a single histidine residue !1affinity-labeled by both 3-bromoacetoxyestrone and !112-beta-bromoacetoxy-4-estrene-3,17-dione. !$#cross-references MUID:84008135; PMID:6578212 !$#accession A21031 !'##molecule_type protein !'##residues 220-224 ##label MUR REFERENCE A60628 !$#authors Murdock, G.L.; Chin, C.C.; Warren, J.C. !$#journal Biochemistry (1986) 25:641-646 !$#title Human placental estradiol 17beta-dehydrogenase: sequence of !1a histidine-bearing peptide in the catalytic region. !$#cross-references MUID:86159758; PMID:3456799 !$#accession A60628 !'##molecule_type protein !'##residues 208-215 ##label MU2 REFERENCE A37190 !$#authors Labrie, F.; Luu-The, V.; Labrie, C.; Berube, D.; Couet, J.; !1Zhao, H.F.; Gagne, R.; Simard, J. !$#journal J. Steroid Biochem. (1989) 34:189-197 !$#title Characterization of two mRNA species encoding human !1estradiol 17beta-dehydrogenase and assignment of the gene to !1chromosome 17. !$#cross-references MUID:90173172; PMID:2483219 !$#contents annotation REFERENCE G09150 !$#authors Shen, Y. !$#submission submitted to the EMBL Data Library, August 1995 !$#accession G02067 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-328 ##label SHE !'##cross-references EMBL:U34879; NID:g975894; PIDN:AAD05019.1; !1PID:g975895 GENETICS !$#gene GDB:HSD17B1; EDH17B2; EDHB !'##cross-references GDB:127970 !$#map_position 17q11-17q21 !$#introns 33/1; 89/1; 149/1; 180/2; 239/3 FUNCTION !$#description catalyzes the reversible oxidation of estradiol-17beta to !1estrone using NAD(P) as coenzyme !$#note also catalyzes the reversible oxidation of 5-androstenediol !1to dehydroepiandrosterone (DHEA), and of testosterone to !14-androstenedione CLASSIFICATION #superfamily estradiol 17beta-dehydrogenase; short-chain !1alcohol dehydrogenase homology KEYWORDS oxidoreductase FEATURE !$2-328 #product estradiol 17beta-dehydrogenase #status !8experimental #label MAT\ !$4-189 #domain short-chain alcohol dehydrogenase homology !8#label SADH\ !$211,214,222 #active_site His #status experimental SUMMARY #length 328 #molecular-weight 34980 #checksum 6709 SEQUENCE /// ENTRY S32607 #type complete TITLE trifunctional enzyme HDE, peroxisomal - yeast (Candida tropicalis) ALTERNATE_NAMES trifunctional beta-oxidation enzyme HDE CONTAINS 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35); 3-hydroxyacyl-CoA epimerase (EC 5.1.2.-); enoyl-CoA hydratase (EC 4.2.1.17) ORGANISM #formal_name Candida tropicalis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 31-Mar-2000 ACCESSIONS S32607; JH0474; JT0350; S18126 REFERENCE S32607 !$#authors Sloots, J.A.; Aitchison, J.D.; Rachubinski, R.A. !$#journal Gene (1991) 105:129-134 !$#title Glucose-responsive and oleic acid-responsive elements in the !1gene encoding the peroxisomal trifunctional enzyme of !1Candida tropicalis. !$#cross-references MUID:92039009; PMID:1937002 !$#accession S32607 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-906 ##label AIT !'##cross-references EMBL:X57854; NID:g2669; PIDN:CAA40989.1; PID:g2670 !'##note nucleotide sequence submitted to the EMBL Data Library, !1February 1991 REFERENCE JH0474 !$#authors Aitchison, J.D.; Sloots, J.A.; Nuttley, W.M.; Rachubinski, !1R.A. !$#journal Gene (1991) 105:135-136 !$#title Sequence of the gene encoding Candida tropicalis peroxisomal !1trifunctional enzyme. !$#cross-references MUID:92039010; PMID:1937003 !$#accession JH0474 !'##status translation not shown !'##molecule_type DNA !'##residues 1-906 ##label AI3 !'##cross-references EMBL:X57854; NID:g2669; PIDN:CAA40989.1; PID:g2670 REFERENCE JT0350 !$#authors Nuttley, W.M.; Aitchison, J.D.; Rachubinski, R.A. !$#journal Gene (1988) 69:171-180 !$#title cDNA cloning and primary structure determination of the !1peroxisomal trifunctional enzyme !1hydratase-dehydrogenase-epimerase from the yeast Candida !1tropicalis pK233. !$#cross-references MUID:89172062; PMID:3267241 !$#accession JT0350 !'##molecule_type mRNA !'##residues 1-539,'S',541-906 ##label NUT !'##cross-references GB:M22765; NID:g695397; PIDN:AAA62847.1; !1PID:g695398 !'##note the authors translated the codon TCC for residue 540 as Phe GENETICS !$#gene HDE CLASSIFICATION #superfamily peroxisomal trifunctional enzyme HDE; !1short-chain alcohol dehydrogenase homology KEYWORDS carbon-oxygen lyase; fatty acid beta-oxidation; hydro-lyase; !1isomerase; multifunctional enzyme; oxidoreductase; !1peroxisome FEATURE !$9-194 #domain short-chain alcohol dehydrogenase homology !8#label SAD1\ !$323-498 #domain short-chain alcohol dehydrogenase homology !8#label SAD2 SUMMARY #length 906 #molecular-weight 99468 #checksum 3700 SEQUENCE /// ENTRY S25322 #type complete TITLE bifunctional beta-oxidation protein FOX2, peroxisomal - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YK108; protein YKR009c CONTAINS 2-enoyl-CoA hydratase 2 (EC 4.2.1.-); D-3-hydroxyacyl CoA dehydrogenase (EC 1.1.1.-) ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 31-Mar-2000 ACCESSIONS S25322; A42426; S38078 REFERENCE S25322 !$#authors Duesterhoeft, A.; Philippsen, P. !$#journal Yeast (1992) 8:749-759 !$#title DNA sequencing and analysis of a 24.7 kb segment !1encompassing centromere CEN11 of Saccharomyces cerevisiae !1reveals nine previously unknown open reading frames. !$#cross-references MUID:93070612; PMID:1441752 !$#accession S25322 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-900 ##label DUE !'##cross-references EMBL:X65124; NID:g3517; PIDN:CAA46243.1; PID:g3520 !'##experimental_source strain S288C REFERENCE A42426 !$#authors Hiltunen, J.K.; Wenzel, B.; Beyer, A.; Erdmann, R.; Fossa, !1A.; Kunau, W.H. !$#journal J. Biol. Chem. (1992) 267:6646-6653 !$#title Peroxisomal multifunctional beta-oxidation protein of !1Saccharomyces cerevisiae. Molecular analysis of the fox2 !1gene and gene product. !$#cross-references MUID:92202210; PMID:1551874 !$#accession A42426 !'##molecule_type DNA !'##residues 1-900 ##label HIL !'##cross-references GB:M86456; NID:g171946; PIDN:AAA34779.1; !1PID:g171947 !'##note sequence extracted from NCBI backbone (NCBIN:89904, !1NCBIP:89905) REFERENCE S37811 !$#authors Duesterhoeft, A.; Moestl, D.; Poehlmann, R.; Philippsen, P. !$#submission submitted to the Protein Sequence Database, March 1994 !$#accession S38078 !'##molecule_type DNA !'##residues 1-900 ##label DU2 !'##cross-references EMBL:Z28234; NID:g486418; PIDN:CAA82079.1; !1PID:g486419; GSPDB:GN00011; MIPS:YKR009c GENETICS !$#gene SGD:FOX2; MIPS:YKR009c !'##cross-references SGD:S0001717; MIPS:YKR009c !$#map_position 11R CLASSIFICATION #superfamily peroxisomal trifunctional enzyme HDE; !1short-chain alcohol dehydrogenase homology KEYWORDS ATP; carbon-oxygen lyase; duplication; fatty acid !1beta-oxidation; hydro-lyase; multifunctional enzyme; !1oxidoreductase; P-loop; peroxisome; purine nucleotide !1binding FEATURE !$10-196 #domain short-chain alcohol dehydrogenase homology !8#label SAD1\ !$323-500 #domain short-chain alcohol dehydrogenase homology !8#label SAD2\ !$330-337 #region nucleotide-binding motif A (P-loop)\ !$898-900 #region peroxisome/glyoxysome location signal !8(S-[RKH]-L) motif\ !$336 #binding_site ATP/GTP (Lys) #status predicted SUMMARY #length 900 #molecular-weight 98702 #checksum 6974 SEQUENCE /// ENTRY A39763 #type complete TITLE aldehyde reductase (EC 1.1.1.21) [validated] - human ALTERNATE_NAMES aldose reductase ORGANISM #formal_name Homo sapiens #common_name man DATE 08-Dec-2000 #sequence_revision 08-Dec-2000 #text_change 08-Dec-2000 ACCESSIONS A39763; S06591; B33851; A34583; A36510; A36436; S29630; !1A31432; S39368 REFERENCE A39763 !$#authors Graham, A.; Brown, L.; Hedge, P.J.; Gammack, A.J.; Markham, !1A.F. !$#journal J. Biol. Chem. (1991) 266:6872-6877 !$#title Structure of the human aldose reductase gene. !$#cross-references MUID:91201333; PMID:1901857 !$#accession A39763 !'##status preliminary !'##molecule_type DNA !'##residues 1-316 ##label GRA1 !'##cross-references GB:M59856; GB:M59783; NID:g178483; PIDN:AAA51712.1; !1PID:g178485 REFERENCE S06591 !$#authors Graham, A.; Hedge, P.J.; Powell, S.J.; Riley, J.; Brown, L.; !1Gammack, A.; Carey, F.; Markham, A.F. !$#journal Nucleic Acids Res. (1989) 17:8368 !$#title Nucleotide sequence of cDNA for human aldose reductase. !$#cross-references MUID:90045960; PMID:2510130 !$#accession S06591 !'##molecule_type mRNA !'##residues 1-316 ##label GRA2 !'##cross-references EMBL:X15414; NID:g28646; PIDN:CAA33460.1; !1PID:g28647 REFERENCE A33851 !$#authors Bohren, K.M.; Bullock, B.; Wermuth, B.; Gabbay, K.H. !$#journal J. Biol. Chem. (1989) 264:9547-9551 !$#title The aldo-keto reductase superfamily. cDNAs and deduced amino !1acid sequences of human aldehyde and aldose reductases. !$#cross-references MUID:89255461; PMID:2498333 !$#accession B33851 !'##status preliminary !'##molecule_type mRNA !'##residues 1-316 ##label BOH !'##cross-references GB:J04795; NID:g178486; PIDN:AAA51713.1; !1PID:g178487 REFERENCE A34583 !$#authors Grundmann, U.; Bohn, H.; Obermeier, R.; Amann, E. !$#journal DNA Cell Biol. (1990) 9:149-157 !$#title Cloning and prokaryotic expression of a biologically active !1human placental aldose reductase. !$#cross-references MUID:90253609; PMID:2111143 !$#accession A34583 !'##status preliminary !'##molecule_type mRNA !'##residues 1-316 ##label GRU !'##cross-references GB:M34720; NID:g179035; PIDN:AAA35560.1; !1PID:g179036 REFERENCE A36510 !$#authors Chung, S.; LaMendola, J. !$#journal J. Biol. Chem. (1989) 264:14775-14777 !$#title Cloning and sequence determination of human placental aldose !1reductase gene. !$#cross-references MUID:89359274; PMID:2504709 !$#accession A36510 !'##status preliminary !'##molecule_type mRNA !'##residues 1-4,'I',6-316 ##label CHU !'##cross-references GB:J05017; NID:g178488; PIDN:AAA51714.1; !1PID:g178489 REFERENCE A36436 !$#authors Nishimura, C.; Matsuura, Y.; Kokai, Y.; Akera, T.; Carper, !1D.; Morjana, N.; Lyons, C.; Flynn, T.G. !$#journal J. Biol. Chem. (1990) 265:9788-9792 !$#title Cloning and expression of human aldose reductase. !$#cross-references MUID:90277668; PMID:2112546 !$#accession A36436 !'##status preliminary !'##molecule_type mRNA !'##residues 1-316 ##label NIS !'##cross-references GB:J05474; NID:g178490; PIDN:AAA51715.1; !1PID:g178491 REFERENCE S29630 !$#authors Ferraretto, A.; Negri, A.; Giuliani, A.; de Grada, L.; !1Fuhrman Conti, A.M.; Ronchi, S. !$#journal Biochim. Biophys. Acta (1993) 1175:283-288 !$#title Aldose reductase is involved in long-term adaptation of EUE !1cells to hyperosmotic stress. !$#cross-references MUID:93168787; PMID:8435445 !$#accession S29630 !'##molecule_type protein !'##residues 131-157,'XX',160-162 ##label FER REFERENCE A31432 !$#authors Morjana, N.A.; Lyons, C.; Flynn, T.G. !$#journal J. Biol. Chem. (1989) 264:2912-2919 !$#title Aldose reductase from human psoas muscle. Affinity labeling !1of an active site lysine by pyridoxal 5'-phosphate and !1pyridoxal 5'-diphospho-5'-adenosine. !$#cross-references MUID:89123393; PMID:2492527 !$#accession A31432 !'##status preliminary !'##molecule_type protein !'##residues 244-275 ##label MOR REFERENCE S39368 !$#authors Liu, S.Q.; Bhatnagar, A.; Ansari, N.H.; Srivastava, S.K. !$#journal Biochim. Biophys. Acta (1993) 1164:268-272 !$#title Identification of the reactive cysteine residue in human !1placenta aldose reductase. !$#cross-references MUID:93344424; PMID:8343525 !$#accession S39368 !'##molecule_type protein !'##residues 298-306,'M',308-316 ##label LIU GENETICS !$#gene GDB:ALDR1 !'##cross-references GDB:128041; OMIM:103880 !$#map_position 7q35-7q35 CLASSIFICATION #superfamily aldehyde reductase KEYWORDS NADP; oxidoreductase FEATURE !$263 #active_site Lys #status predicted SUMMARY #length 316 #molecular-weight 35853 #checksum 101 SEQUENCE /// ENTRY A35452 #type complete TITLE aldehyde reductase (EC 1.1.1.21) - bovine ALTERNATE_NAMES 20alpha-hydroxysteroid dehydrogenase (EC 1.1.1.149); aldose reductase ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS A35452; A48316; A46379 REFERENCE A35452 !$#authors Schade, S.Z.; Early, S.L.; Williams, T.R.; Kezdy, F.J.; !1Heinrikson, R.L.; Grimshaw, C.E.; Doughty, C.C. !$#journal J. Biol. Chem. (1990) 265:3628-3635 !$#title Sequence analysis of bovine lens aldose reductase. !$#cross-references MUID:90154035; PMID:2105951 !$#accession A35452 !'##molecule_type protein !'##residues 1-315 ##label SCH !'##experimental_source lens REFERENCE A48316 !$#authors Petrash, J.M.; Favello, A.D. !$#journal Curr. Eye Res. (1989) 8:1021-1027 !$#title Isolation and characterization of cDNA clones encoding !1aldose reductase. !$#cross-references MUID:90125780; PMID:2515032 !$#accession A48316 !'##molecule_type mRNA !'##residues 20-315 ##label PET !'##cross-references GB:M31463; NID:g162651; PIDN:AAA30370.1; !1PID:g162652 REFERENCE A46379 !$#authors Warren, J.C.; Murdock, G.L.; Ma, Y.; Goodman, S.R.; Zimmer, !1W.E. !$#journal Biochemistry (1993) 32:1401-1406 !$#title Molecular cloning of testicular 20 alpha-hydroxysteroid !1dehydrogenase: identity with aldose reductase. !$#cross-references MUID:93160176; PMID:8431420 !$#accession A46379 !'##molecule_type mRNA !'##residues 9-315 ##label WAR !'##cross-references GB:S54973; NID:g265403; PIDN:AAB25333.1; !1PID:g265404 !'##experimental_source testes !'##note sequence extracted from NCBI backbone (NCBIN:124742, !1NCBIP:124745) !'##note part of this sequence was confirmed by protein sequencing COMMENT This enzyme, after purification to homogeneity, was shown to !1reduce glucose, glyceradehyde, and benzaldehyde, as well as !117-hydroxyprogesterone. CLASSIFICATION #superfamily aldehyde reductase KEYWORDS acetylated amino end; monomer; oxidoreductase FEATURE !$1 #modified_site acetylated amino end (Ala) #status !8experimental SUMMARY #length 315 #molecular-weight 35919 #checksum 3564 SEQUENCE /// ENTRY A60603 #type complete TITLE aldehyde reductase (EC 1.1.1.21) - rat ALTERNATE_NAMES aldose reductase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS A60603; S00079; B60603; I53649 REFERENCE A60603 !$#authors Carper, D.A.; Wistow, G.; Nishimura, C.; Graham, C.; !1Watanabe, K.; Fujii, Y.; Hayashi, H.; Hayaishi, O. !$#journal Exp. Eye Res. (1989) 49:377-388 !$#title A superfamily of NADPH-dependent reductases in eukaryotes !1and prokaryotes. !$#cross-references MUID:90005742; PMID:2507340 !$#accession A60603 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-316 ##label CAR REFERENCE S00079 !$#authors Carper, D.; Nishimura, C.; Shinohara, T.; Dietzchold, B.; !1Wistow, G.; Craft, C.; Kador, P.; Kinoshita, J.H. !$#journal FEBS Lett. (1987) 220:209-213 !$#title Aldose reductase and rho-crystallin belong to the same !1protein superfamily as aldehyde reductase. !$#cross-references MUID:87276556; PMID:3111886 !$#accession S00079 !'##molecule_type mRNA !'##residues 33-316 ##label CA2 !'##cross-references EMBL:X05884 !'##note 45-Ser and 54-Trp were also found !$#accession B60603 !'##molecule_type protein !'##residues 34-60,'XXX',92-108,146-173,204-231,244-252,276-294 ##label !1CA3 !'##note part of this sequence was confirmed by protein sequencing REFERENCE I53649 !$#authors Graham, C.E.; Szpirer, C.; Levan, G.; Carper, D. !$#journal Gene (1991) 107:259-267 !$#title Characterization of the aldose reductase-encoding gene !1family in rat. !$#cross-references MUID:92084118; PMID:1748296 !$#accession I53649 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-316 ##label RES !'##cross-references GB:M60322; NID:g202851; PIDN:AAA40721.1; !1PID:g202852 COMMENT Aldose reductase catalyzes reduction of a variety of sugars !1to sugar alcohols using NADPH as a coenzyme. COMMENT This enzyme is active in the eye lens, where an accumulation !1of sugar alcohols may cause osmotic cataracts. GENETICS !$#introns 22/3; 78/3; 117/3; 143/3; 184/3; 220/2; 247/3; 275/3; 303/2 CLASSIFICATION #superfamily aldehyde reductase KEYWORDS eye lens; NADP; oxidoreductase FEATURE !$263 #active_site Lys #status predicted SUMMARY #length 316 #molecular-weight 35797 #checksum 9850 SEQUENCE /// ENTRY S15835 #type complete TITLE 3-oxo-5beta-steroid 4-dehydrogenase (EC 1.3.99.6) - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 16-Jun-2000 ACCESSIONS S15835; S23616; S20272; S23617 REFERENCE S15835 !$#authors Onishi, Y.; Noshiro, M.; Shimosato, T.; Okuda, K. !$#journal FEBS Lett. (1991) 283:215-218 !$#title Molecular cloning and sequence analysis of cDNA encoding !1Delta(4)-3-ketosteroid 5-beta-reductase of rat liver. !$#cross-references MUID:91257305; PMID:1710579 !$#accession S15835 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-326 ##label ONI1 !'##cross-references GB:D17309; NID:g450474; PIDN:BAA04131.1; !1PID:g456303 !$#accession S23616 !'##molecule_type protein !'##residues 36-58;86-104;143-157;163-185;240-250;282-291 ##label ONI2 REFERENCE S20272 !$#authors Onishi, Y.; Noshiro, M.; Shimosato, T.; Okuda, K. !$#journal Biol. Chem. Hoppe-Seyler (1991) 372:1039-1049 !$#title Delta(4)-3-oxosteroid 5beta-reductase. Structure and !1function. !$#cross-references MUID:92162187; PMID:1789929 !$#accession S20272 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-326 ##label ONI3 !'##cross-references GB:D17309; NID:g450474; PIDN:BAA04131.1; !1PID:g456303 !$#accession S23617 !'##molecule_type protein !'##residues 36-58;87-109;144-157;164-185;241-249;250,254-268;282-291 !1##label ONI4 CLASSIFICATION #superfamily aldehyde reductase KEYWORDS blocked amino end; oxidoreductase FEATURE !$273 #active_site Lys #status predicted SUMMARY #length 326 #molecular-weight 37378 #checksum 9105 SEQUENCE /// ENTRY S41120 #type complete TITLE cholestenone 5beta-reductase (EC 1.3.1.23) [validated] - human ALTERNATE_NAMES delta 4-3-oxosteroid 5 beta-reductase ORGANISM #formal_name Homo sapiens #common_name man DATE 08-Dec-2000 #sequence_revision 08-Dec-2000 #text_change 08-Dec-2000 ACCESSIONS S41120 REFERENCE S41120 !$#authors Kondo, K.H.; Kai, M.H.; Setoguchi, Y.; Eggertsen, G.; !1Sjoeblom, P.; Setoguchi, T.; Okuda, K.I.; Bjoerkhem, I. !$#journal Eur. J. Biochem. (1994) 219:357-363 !$#title Cloning and expression of cDNA of human Delta !1(4)-3-oxosteroid 5-beta-reductase and substrate specificity !1of the expressed enzyme. !$#cross-references MUID:94139710; PMID:7508385 !$#accession S41120 !'##molecule_type mRNA !'##residues 1-326 ##label KON !'##cross-references EMBL:Z28339; NID:g431856; PIDN:CAA82193.1; !1PID:g431857 GENETICS !$#gene GDB:SRD5B1 !'##cross-references GDB:313097 !$#map_position Xq24-Xqter CLASSIFICATION #superfamily aldehyde reductase KEYWORDS oxidoreductase FEATURE !$273 #active_site Lys #status predicted SUMMARY #length 326 #molecular-weight 37377 #checksum 9241 SEQUENCE /// ENTRY A39350 #type complete TITLE 3alpha-hydroxysteroid dehydrogenase (B-specific) (EC 1.1.1.50) - rat ALTERNATE_NAMES dehydroascorbate reductase; dihydrodiol dehydrogenase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 19-Jan-2001 ACCESSIONS A39350; A39839; A61163; A23730; S53338 REFERENCE A39350 !$#authors Stolz, A.; Rahimi-Kiani, M.; Ameis, D.; Chan, E.; Ronk, M.; !1Shively, J.E. !$#journal J. Biol. Chem. (1991) 266:15253-15257 !$#title Molecular structure of rat hepatic 3alpha-hydroxysteroid !1dehydrogenase. A member of the oxidoreductase gene family. !$#cross-references MUID:91332047; PMID:1714456 !$#accession A39350 !'##molecule_type mRNA !'##residues 1-322 ##label STO !'##cross-references GB:M64393; NID:g202528; PIDN:AAA40605.1; !1PID:g202529 !'##note parts of this sequence were confirmed by peptide sequencing REFERENCE A39839 !$#authors Pawlowski, J.E.; Huizinga, M.; Penning, T.M. !$#journal J. Biol. Chem. (1991) 266:8820-8825 !$#title Cloning and sequencing of the cDNA for rat liver !13alpha-hydroxysteroid/dihydrodiol dehydrogenase. !$#cross-references MUID:91224978; PMID:1840601 !$#accession A39839 !'##molecule_type mRNA !'##residues 1-322 ##label PAW !'##cross-references GB:M61937; NID:g203917; PIDN:AAA41077.1; !1PID:g203918 !'##note parts of this sequence were confirmed by peptide sequencing REFERENCE A61163 !$#authors Pawlowski, J.; Huizinga, M.; Penning, T.M. !$#journal Agents Actions (1991) 34:289-293 !$#title Isolation and partial characterization of a full-length cDNA !1clone for 3alpha-hydroxysteroid dehydrogenase: a potential !1target enzyme for nonsteroidal anti-inflammatory drugs. !$#cross-references MUID:92170599; PMID:1793046 !$#accession A61163 !'##molecule_type mRNA !'##residues 112-169;238-322 ##label PA2 !'##cross-references GB:S35751; GB:S35752 REFERENCE A23730 !$#authors Cheng, K.C.; White, P.C.; Qin, K.N. !$#journal Mol. Endocrinol. (1991) 5:823-828 !$#title Molecular cloning and expression of rat liver !13alpha-hydroxysteroid dehydrogenase. !$#cross-references MUID:92017888; PMID:1922097 !$#accession A23730 !'##molecule_type mRNA !'##residues 1-107,'Q',109-272,'KP',275-279,'P',281-322 ##label CHE !'##cross-references GB:S57790; NID:g236057; PIDN:AAB19918.1; !1PID:g236058 !'##note it is unclear whether the differences in this report indicate !1the presence of multiple isozymes REFERENCE S53338 !$#authors del Bello, B.; Maellaro, E.; Sugherini, L.; Santucci, A.; !1Comporti, M.; Casini, A.F. !$#journal Biochem. J. (1994) 304:385-390 !$#title Purification of NADPH-dependent dehydroascorbate reductase !1from rat liver and its identification with !13-alpha-hydroxysteroid dehydrogenase. !$#cross-references MUID:95091669; PMID:7998972 !$#accession S53338 !'##molecule_type protein !'##residues 2-16;121-135;152-166;203-217 ##label DEL !'##experimental_source liver COMMENT This enzyme also has 9-, 11-, and 15-hydroxyprostaglandin !1dehydrogenase activities. COMMENT This enzyme is inhibited by nonsteroidal anti-inflammatory !1drugs. CLASSIFICATION #superfamily aldehyde reductase KEYWORDS monomer; NADP; oxidoreductase SUMMARY #length 322 #molecular-weight 37027 #checksum 5294 SEQUENCE /// ENTRY JC2330 #type complete TITLE luteal 20-alpha-hydroxysteroid dehydrogenase (EC 1.1.1.-) - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 16-Jun-2000 ACCESSIONS JC2330; S43842 REFERENCE JC2330 !$#authors Mao, J.; Duan, W.R.; Albarracin, C.T.; Parmer, T.G.; Gibori, !1G. !$#journal Biochem. Biophys. Res. Commun. (1994) 201:1289-1295 !$#title Isolation and characterization of a rat luteal cDNA encoding !120alpha-hydroxysteroid dehydrogenase. !$#cross-references MUID:94296401; PMID:8024573 !$#accession JC2330 !'##molecule_type mRNA !'##residues 1-323 ##label MAO !'##experimental_source corpus luteum !'##note the authors translated the codon AAG for residue 312 as Leu REFERENCE S43842 !$#authors Miura, R.; Shiota, K.; Noda, K.; Yagi, S.; Ogawa, T.; !1Takahashi, M. !$#journal Biochem. J. (1994) 299:561-567 !$#title Molecular cloning of cDNA for rat ovarian !120-alpha-hydroxysteroid dehydrogenase (HSD1). !$#cross-references MUID:94226624; PMID:8172618 !$#accession S43842 !'##molecule_type mRNA !'##residues 1-194,'L',196-323 ##label MIU !'##cross-references GB:D14424; NID:g471151; PIDN:BAA03317.1; !1PID:g471152 COMMENT This enzyme is a NADP-dependent enzyme which catalyzes the !1reduction of progesterone to 20alpha hydroxyprogesterone. CLASSIFICATION #superfamily aldehyde reductase KEYWORDS glycoprotein; oxidoreductase; phosphoprotein FEATURE !$20-23 #region NADP binding #status predicted\ !$34 #binding_site phosphate (Ser) (covalent) (by !8cAMP-dependent kinase) #status predicted\ !$37,89,102,121 #binding_site phosphate (Ser) (covalent) (by protein !8kinase C) #status predicted\ !$67 #binding_site phosphate (Ser) (covalent) (by casein !8kinase II) #status predicted\ !$73,82,221 #binding_site phosphate (Thr) (covalent) (by protein !8kinase C) #status predicted\ !$81 #binding_site phosphate (Tyr) (covalent) #status !8predicted\ !$198 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 323 #molecular-weight 37323 #checksum 8027 SEQUENCE /// ENTRY A28396 #type complete TITLE prostaglandin-F synthase (EC 1.1.1.188) - bovine ALTERNATE_NAMES prostaglandin F synthase ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS A28396 REFERENCE A28396 !$#authors Watanabe, K.; Fujii, Y.; Nakayama, K.; Ohkubo, H.; !1Kuramitsu, S.; Kagamiyama, H.; Nakanishi, S.; Hayaishi, O. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:11-15 !$#title Structural similarity of bovine lung prostaglandin F !1synthase to lens epsilon-crystallin of the European common !1frog. !$#cross-references MUID:88124772; PMID:2829166 !$#accession A28396 !'##molecule_type mRNA !'##residues 1-323 ##label WAT !'##cross-references GB:J03570; NID:g163511; PIDN:AAA30694.1; !1PID:g163512 !'##experimental_source lung tissue CLASSIFICATION #superfamily aldehyde reductase KEYWORDS monomer; oxidoreductase SUMMARY #length 323 #molecular-weight 36720 #checksum 6310 SEQUENCE /// ENTRY CYFGE #type fragment TITLE epsilon-crystallin - common frog (fragment) ORGANISM #formal_name Rana temporaria #common_name common frog DATE 28-Aug-1985 #sequence_revision 30-Sep-1988 #text_change 16-Jun-2000 ACCESSIONS A02938 REFERENCE A02938 !$#authors Tomarev, S.I.; Zinovieva, R.D.; Dolgilevich, S.M.; Luchin, !1S.V.; Krayev, A.S.; Skryabin, K.G.; Gause Jr., G.G. !$#journal FEBS Lett. (1984) 171:297-302 !$#title A novel type of crystallin in the frog eye lens. 35-kDa !1polypeptide is not homologous to any of the major classes of !1lens crystallins. !$#cross-references MUID:84208883; PMID:6609843 !$#accession A02938 !'##molecule_type mRNA !'##residues 1-225 ##label TOM !'##cross-references GB:X00659; GB:M32516; NID:g64298; PID:g1334775 !'##note the authors translated the codon GAG for residue 156 as Asp COMMENT This crystallin belongs to a new class of crystallin that !1shows no detectable homology with other major classes of !1crystallins. The name epsilon crystallin was proposed by the !1authors. CLASSIFICATION #superfamily aldehyde reductase KEYWORDS eye lens SUMMARY #length 225 #checksum 1211 SEQUENCE /// ENTRY JC4280 #type complete TITLE carbonyl reductase (NADPH2) (EC 1.1.1.184) - bullfrog CONTAINS carbonyl reductase (NADPH) (EC 1.1.1.184) [validated] ORGANISM #formal_name Rana catesbeiana #common_name bullfrog DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 03-Jun-2002 ACCESSIONS JC4280; A36444; S57463 REFERENCE JC4280 !$#authors Lu, S.F.; Pan, F.M.; Chiou, S.H. !$#journal Biochem. Biophys. Res. Commun. (1995) 214:1079-1088 !$#title Sequence analysis of frog rho-crystallin by cDNA cloning and !1sequencing. !$#cross-references MUID:96024608; PMID:7575513 !$#accession JC4280 !'##molecule_type mRNA !'##residues 1-324 ##label LUA !'##cross-references EMBL:X87724; NID:g871518; PIDN:CAA61023.1; !1PID:g871519 REFERENCE A36444 !$#authors Fujii, Y.; Watanabe, K.; Hayashi, H.; Urade, Y.; Kuramitsu, !1S.; Kagamiyama, H.; Hayaishi, O. !$#journal J. Biol. Chem. (1990) 265:9914-9923 !$#title Purification and characterization of rho-crystallin from !1Japanese common bullfrog lens. !$#cross-references MUID:90277687; PMID:2190986 !$#accession A36444 !'##molecule_type protein !'##residues 2-75,'K',77-154,'R',156-204,'S',206-215,'T',217-233,'P', !1235-251,'T',253-324 ##label FUJ !'##note some prostaglandin 9-ketoreductase activity was observed CLASSIFICATION #superfamily aldehyde reductase KEYWORDS blocked amino end; NADP; oxidoreductase FEATURE !$2-324 #product rho-crystallin #status experimental #label !8MAT\ !$2 #modified_site blocked amino end (Thr) (in mature !8form) (partial) (probably acetylated) #status !8experimental SUMMARY #length 324 #molecular-weight 36826 #checksum 9153 SEQUENCE /// ENTRY JH0575 #type complete TITLE prostaglandin-F synthase (EC 1.1.1.188) II, hepatic [validated] - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS E75572; JH0575 REFERENCE JH0575 !$#authors Kuchinke, W.; Barski, O.; Watanabe, K.; Hayaishi, O. !$#journal Biochem. Biophys. Res. Commun. (1992) 183:1238-1246 !$#title A lung type prostaglandin F synthase is expressed in bovine !1liver: cDNA sequence and expression in E.coli. !$#cross-references MUID:92231889; PMID:1339268 !$#accession E75572 !'##molecule_type mRNA !'##residues 1-323 ##label KUC !'##cross-references GB:M86544; NID:g163605; PIDN:AAA30730.1; !1PID:g163606 !'##experimental_source lung tissue !$#accession JH0575 !'##molecule_type mRNA !'##residues 1-250,'A',252-323 ##label KU2 !'##cross-references GB:M86544 !'##note the translated sequence in GenBank entry BOVPRGFSII, release !1114, (PIDN:AAA30730.1) differs from the published sequence !1in having 251-Thr COMMENT Prostaglandin-F synthase catalyzes the reduction of !1prostaglandin D2 to 9-alpha and 11-beta prostaglandin F2, !1and the reduction of prostaglandin H2 to prostaglandin F2 !12-alpha. COMMENT Two types of prostaglandin-F synthases are found in liver. !1Prostaglandin F synthase II has a low affinity for !1prostaglandin D2 and catalyzes prostaglandin H2 with a !1relative activity of 10% (relative to 4-nitrobenzaldehyde !1reductase activity); prostaglandin F synthetase I has a high !1affinity for prostaglandin D2 and catalyzes prostaglandin H2 !1with a relative activity of 1%. GENETICS !$#gene PGFSII CLASSIFICATION #superfamily aldehyde reductase KEYWORDS liver; monomer; oxidoreductase SUMMARY #length 323 #molecular-weight 36742 #checksum 6598 SEQUENCE /// ENTRY A57407 #type complete TITLE chlordecone reductase (EC 1.1.1.225) / 3alpha-hydroxysteroid dehydrogenase (EC 1.1.1.-) I [validated] - human ALTERNATE_NAMES 3-alpha-hydroxysteroid/dihydrodiol dehydrogenase ORGANISM #formal_name Homo sapiens #common_name man DATE 08-Dec-2000 #sequence_revision 08-Dec-2000 #text_change 08-Dec-2000 ACCESSIONS A57407; PC1129; A34263; S43844; I56599 REFERENCE A57407 !$#authors Khanna, M.; Qin, K.N.; Wang, R.W.; Cheng, K.C. !$#journal J. Biol. Chem. (1995) 270:20162-20168 !$#title Substrate specificity, gene structure, and tissue-specific !1distribution of multiple human 3alpha-hydroxysteroid !1dehydrogenases. !$#cross-references MUID:95378275; PMID:7650035 !$#accession A57407 !'##status preliminary !'##molecule_type DNA !'##residues 1-323 ##label KHA !'##cross-references GB:L43822; NID:g972744; GB:L43823; NID:g972745; !1GB:L43824; NID:g972746; GB:L43825; NID:g972747; GB:L43826; !1NID:g972748; GB:L43827; NID:g972749; GB:L43828; NID:g972750; !1GB:L43829; NID:g972751; GB:L43830; NID:g972752 !'##note authors translated the codon AAC for residue 32 as Gln, AAT for !1residue 56 as Gln, AAT for residue 57 as Gln, and ACC for !1residue 251 as Tyr !'##note this translation is not annotated in GenBank entry HUMHSDI09, !1release 117.0 REFERENCE PC1129 !$#authors Binstock, J.M.; Iyer, R.B.; Hamby, C.V.; Fried, V.A.; !1Schwartz, I.S.; Weinstein, B.I.; Southren, A.L. !$#journal Biochem. Biophys. Res. Commun. (1992) 187:760-766 !$#title Human hepatic 3-alpha-hydroxysteroid dehydrogenase: Possible !1identity with human hepatic chlordecone reductase. !$#cross-references MUID:92412118; PMID:1530633 !$#accession PC1129 !'##molecule_type protein !'##residues 40-54;105-121;162-175;184-196;277-291;307-321 ##label BIN !'##experimental_source liver REFERENCE A34263 !$#authors Winters, C.J.; Molowa, D.T.; Guzelian, P.S. !$#journal Biochemistry (1990) 29:1080-1087 !$#title Isolation and characterization of cloned cDNAs encoding !1human liver chlordecone reductase. !$#cross-references MUID:90254121; PMID:2187532 !$#accession A34263 !'##molecule_type mRNA !'##residues 16-323 ##label WIN !'##cross-references GB:M33375; NID:g179986; PIDN:AAA35658.1; !1PID:g179987 REFERENCE S43843 !$#authors Deyashiki, Y.; Ogasawara, A.; Nakayama, T.; Nakanishi, M.; !1Miyabe, Y.; Sato, K.; Hara, A. !$#journal Biochem. J. (1994) 299:545-552 !$#title Molecular cloning of two human liver 3-alpha-hydroxysteroid/ !1dihydrodiol dehydrogenase isoenzymes that are identical with !1chlordecone reductase and bile-acid binder. !$#cross-references MUID:94226622; PMID:8172617 !$#accession S43844 !'##status preliminary !'##molecule_type mRNA !'##residues 3-323 ##label DEY !'##cross-references GB:D26125; NID:g556517; PIDN:BAA05122.1; !1PID:g556518 REFERENCE I56599 !$#authors Qin, K.N.; New, M.I.; Cheng, K.C. !$#journal J. Steroid Biochem. Mol. Biol. (1993) 46:673-679 !$#title Molecular cloning of multiple cDNAs encoding human enzymes !1structurally related to 3 alpha-hydroxysteroid !1dehydrogenase. !$#cross-references MUID:94100121; PMID:8274401 !$#accession I56599 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-323 ##label QI2 !'##cross-references GB:S68287; NID:g544761; PIDN:AAD14010.1; !1PID:g4261710 GENETICS !$#gene GDB:AKR1C4; CHDR !'##cross-references GDB:127896; OMIM:600451 !$#map_position 10p15-10p14 FUNCTION !$#description catalyzes the reduction by NADPH of 3-keto-5-dihydrosteroids !1to the tetrahydro forms CLASSIFICATION #superfamily aldehyde reductase KEYWORDS monomer; NADP; oxidoreductase FEATURE !$270 #active_site Lys #status predicted SUMMARY #length 323 #molecular-weight 37095 #checksum 96 SEQUENCE /// ENTRY A56424 #type complete TITLE estradiol 17beta-dehydrogenase (EC 1.1.1.62), A-specific - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 16-Jun-2000 ACCESSIONS A56424 REFERENCE A56424 !$#authors Deyashiki, Y.; Ohshima, K.; Nakanishi, M.; Sato, K.; !1Matsuura, K.; Hara, A. !$#journal J. Biol. Chem. (1995) 270:10461-10467 !$#title Molecular cloning and characterization of mouse estradiol !117beta-dehydrogenase (A-specific), a member of the !1aldoketoreductase family. !$#cross-references MUID:95256203; PMID:7737980 !$#accession A56424 !'##molecule_type mRNA !'##residues 1-323 ##label DEY !'##cross-references GB:D45850; NID:g1321648; PIDN:BAA08285.1; !1PID:g1321649 CLASSIFICATION #superfamily aldehyde reductase KEYWORDS liver; monomer; oxidoreductase SUMMARY #length 323 #molecular-weight 37047 #checksum 7586 SEQUENCE /// ENTRY A45366 #type complete TITLE 20alpha-hydroxysteroid dehydrogenase (EC 1.1.1.149) - rabbit ALTERNATE_NAMES NADP-dependent aldo-keto reductase CONTAINS 20alpha-hydroxysteroid dehydrogenase (EC 1.1.1.149); prostaglandin-E2 9-reductase (EC 1.1.1.189) ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A45366; S63512 REFERENCE A45366 !$#authors Lacy, W.R.; Washenick, K.J.; Cook, R.G.; Dunbar, B.S. !$#journal Mol. Endocrinol. (1993) 7:58-66 !$#title Molecular cloning and expression of an abundant rabbit !1ovarian protein with 20 alpha-hydroxysteroid dehydrogenase !1activity. !$#cross-references MUID:93188865; PMID:8446108 !$#accession A45366 !'##status preliminary !'##molecule_type mRNA; protein !'##residues 1-323 ##label LAC !'##cross-references GB:L17006; NID:g294470; PIDN:AAA31155.1; !1PID:g294471 !'##experimental_source ovary !'##note sequence inconsistent with the nucleotide translation !'##note sequence extracted from NCBI backbone (NCBIN:127810, !1NCBIP:127802) REFERENCE S63512 !$#authors Wintergalen, N.; Thole, H.H.; Galla, H.J.; Schlegel, W. !$#journal Eur. J. Biochem. (1995) 234:264-270 !$#title Prostaglandin-E(2) 9-reductase from corpus luteum of !1pseudopregnant rabbit is a member of the aldo-keto reductase !1superfamily featuring 20-alpha-hydroxysteroid dehydrogenase !1activity. !$#cross-references MUID:96096748; PMID:8529651 !$#accession S63512 !'##molecule_type protein !'##residues 5-15;85-93;134-170;193-207;210-223;279-314 ##label WIN CLASSIFICATION #superfamily aldehyde reductase KEYWORDS NADP; oxidoreductase SUMMARY #length 323 #molecular-weight 36670 #checksum 3951 SEQUENCE /// ENTRY JN0629 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) - rat ALTERNATE_NAMES aldehyde reductase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 16-Jun-2000 ACCESSIONS JN0629; PN0532 REFERENCE JN0629 !$#authors Takahashi, M.; Fujii, J.; Teshima, T.; Suzuki, K.; Shiba, !1T.; Taniguchi, N. !$#journal Gene (1993) 127:249-253 !$#title Identity of a major 3-deoxyglucosone-reducing enzyme with !1aldehyde reductase in rat liver established by amino acid !1sequencing and cDNA expression. !$#cross-references MUID:93273240; PMID:8500767 !$#accession JN0629 !'##molecule_type mRNA !'##residues 1-325 ##label TAK !'##cross-references GB:D10854; NID:g399659; PIDN:BAA01627.1; !1PID:g399660 !$#accession PN0532 !'##molecule_type protein !'##residues 14-23;35-45;69-77;81-91;135-145;241-249;295-305;309-318 !1##label TAA COMMENT This enzyme catalyzes the NADPH-dependent reduction of !13-deoxyglucosone,a major intermediate in the Maillard !1reaction and a potent cross-linker responsible for the !1polymerization of proteins. CLASSIFICATION #superfamily aldehyde reductase KEYWORDS alcohol metabolism; NADP; oxidoreductase FEATURE !$263 #binding_site NADP (Lys) #status predicted SUMMARY #length 325 #molecular-weight 36506 #checksum 5138 SEQUENCE /// ENTRY A32950 #type complete TITLE probable aldehyde reductase (EC 1.1.1.-) - Leishmania major ALTERNATE_NAMES plant-metabolite dehydrogenase homolog ORGANISM #formal_name Leishmania major DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A32950 REFERENCE A32950 !$#authors Samaras, N.; Spithill, T.W. !$#journal J. Biol. Chem. (1989) 264:4251-4254 !$#title The developmentally regulated P100/11E gene of Leishmania !1major shows homology to a superfamily of reductase genes. !$#cross-references MUID:89139503; PMID:2918000 !$#accession A32950 !'##status preliminary !'##molecule_type mRNA !'##residues 1-284 ##label SAM !'##cross-references GB:J04483 CLASSIFICATION #superfamily aldehyde reductase KEYWORDS oxidoreductase SUMMARY #length 284 #molecular-weight 31850 #checksum 2790 SEQUENCE /// ENTRY S22846 #type complete TITLE probable aldehyde reductase (EC 1.1.1.-) GCY1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein O3269; protein YOR120w; protein YOR3269w ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S22846; S60986; S61678; S67005; S63863 REFERENCE S22846 !$#authors Oechsner, U.; Magdolen, V.; Bandlow, W. !$#journal FEBS Lett. (1988) 238:123-128 !$#title A nuclear yeast gene (GCY) encodes a polypeptide with high !1homology to a vertebrate eye lens protein. !$#cross-references MUID:89005653; PMID:2901985 !$#accession S22846 !'##molecule_type DNA !'##residues 1-312 ##label OEC !'##cross-references EMBL:X13228; NID:g3737; PIDN:CAA31615.1; PID:g3738 REFERENCE S60983 !$#authors Wiemann, S.; Rechmann, S.; Benes, V.; Voss, H.; Schwager, !1C.; Vlcek, C.; Stegemann, J.; Zimmermann, J.; Erfle, H.; !1Paces, V.; Ansorge, W. !$#submission submitted to the EMBL Data Library, August 1995 !$#description Sequencing of 51 kilobases on the right arm of chromosome XV !1from S. cerevisiae reveals 30 open reading frames. !$#accession S60986 !'##molecule_type DNA !'##residues 1-312 ##label WIE !'##cross-references EMBL:X90518; NID:g1050808; PIDN:CAA62107.1; !1PID:g1050812 REFERENCE S61643 !$#authors Benes, V.; Andrade, M.A.; Rechmann, S.; Teodoru, C.; !1Banrevi, A.; Sander, C.; Valencia, A.; Ansorge, W.; Voss, H. !$#submission submitted to the EMBL Data Library, December 1995 !$#description Nucleotide sequence and analysis of a 130 kb fragment of !1yeast chromosome XV. !$#accession S61678 !'##molecule_type DNA !'##residues 1-312 ##label BEN !'##cross-references EMBL:X94335; NID:g1262139; PIDN:CAA64040.1; !1PID:g1164965 REFERENCE S66965 !$#authors Voss, H.; Benes, V.; Rechmann, S.; Teodoru, C.; Schwager, !1C.; Paces, V.; Ansorge, W. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67005 !'##molecule_type DNA !'##residues 1-312 ##label VOS !'##cross-references EMBL:Z75028; NID:g1420316; PIDN:CAA99318.1; !1PID:g1420317; GSPDB:GN00015; MIPS:YOR120w !'##experimental_source strain S288C REFERENCE S63860 !$#authors Wiemann, S.; Rechmann, S.; Benes, V.; Voss, H.; Schwager, !1C.; Vlcek, C.; Stegemann, J.; Zimmermann, J.; Erfle, H.; !1Paces, V.; Ansorge, W. !$#journal Yeast (1996) 12:281-288 !$#title Sequencing and analysis of 51 kb on the right arm of !1chromosome XV from Saccharomyces cerevisiae reveals 30 open !1reading frames. !$#cross-references MUID:97060020; PMID:8904341 !$#accession S63863 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-312 ##label WIW !'##cross-references EMBL:X90518; NID:g1050808; PIDN:CAA62107.1; !1PID:g1050812 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1995 GENETICS !$#gene SGD:GCY1; MIPS:YOR120w !'##cross-references SGD:S0005646; MIPS:YOR120w !$#map_position 15R CLASSIFICATION #superfamily aldehyde reductase KEYWORDS oxidoreductase SUMMARY #length 312 #molecular-weight 35079 #checksum 3701 SEQUENCE /// ENTRY S46020 #type complete TITLE probable aldehyde reductase (EC 1.1.1.21) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein YBR1127; hypothetical protein YBR149w ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S46020; S28668 REFERENCE S46013 !$#authors Entian, K.D.; Koetter, P.; Rose, M.; Becker, J.; Grey, M.; !1Li, Z.; Niegemann, E.; Schenk-Groeninger, R.; Servos, J.; !1Wehner, E.; Wolter, R.; Brendel, M.; Bauer, J.; Braun, H.; !1Dern, K.; Duesterhus, S.; Gruenbein, R.; Hedges, D.; Kiesau, !1P.; Korol, S.; Krems, B.; Proft, M.; Siegers, K.; Baur, A.; !1Boles, E.; Miosga, T.; Schaaff-Gerstenschlaeger, I.; !1Zimmermann, F.K. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S46020 !'##molecule_type DNA !'##residues 1-344 ##label ENT !'##cross-references EMBL:Z36018; NID:g536473; PIDN:CAA85107.1; !1PID:g536474; GSPDB:GN00002; MIPS:YBR149w !'##experimental_source strain S288C REFERENCE S28668 !$#authors Martinez-Soriano, J.P.; Wong, W.M.; van Ryk, D.I.; Nazar, !1R.N. !$#journal J. Mol. Biol. (1991) 217:629-635 !$#title A widely distributed "cat" family of repetitive DNA !1sequences. !$#cross-references MUID:91171289; PMID:2005616 !$#accession S28668 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-55,'LQSKLDN',63-70,'SR',74-344 ##label MAR !'##cross-references EMBL:M95580; NID:g172583; PIDN:AAA35037.1; !1PID:g172584 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1992 GENETICS !$#gene SGD:ARA1; MIPS:YBR149w !'##cross-references SGD:S0000353 !$#map_position 2R CLASSIFICATION #superfamily aldehyde reductase KEYWORDS oxidoreductase SUMMARY #length 344 #molecular-weight 38883 #checksum 5725 SEQUENCE /// ENTRY I40838 #type complete TITLE 2,5-diketo-D-gluconic acid reductase (EC 1.1.1.-) - Corynebacterium sp. ORGANISM #formal_name Corynebacterium sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS I40838 REFERENCE I40838 !$#authors Anderson, S.; Marks, C.B.; Lazarus, R.; Miller, J.; !1Stafford, K.; Seymour, J.; Light, D.; Rastetter, W.; Estell, !1D.A. !$#journal Science (1985) 230:144-149 !$#title Production of 2-keto-L-gulonate, an intermediate in !1L-ascorbate synthesis, by a genetically modified Erwinia !1herbicola. !$#accession I40838 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-278 ##label RES !'##cross-references GB:M12799; NID:g144968; PIDN:AAA83534.1; !1PID:g144969 CLASSIFICATION #superfamily aldehyde reductase KEYWORDS oxidoreductase SUMMARY #length 278 #molecular-weight 30118 #checksum 3764 SEQUENCE /// ENTRY S30383 #type complete TITLE morphine 6-dehydrogenase (EC 1.1.1.218) - Pseudomonas putida plasmid pMdh7.2 ORGANISM #formal_name Pseudomonas putida DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S30383; S14366 REFERENCE S30383 !$#authors Willey, D.L.; Caswell, D.A.; Lowe, C.R.; Bruce, N.C. !$#journal Biochem. J. (1993) 290:539-544 !$#title Nucleotide sequence and over-expression of morphine !1dehydrogenase, a plasmid-encoded gene from Pseudomonas !1putida M10. !$#cross-references MUID:93199531; PMID:8452544 !$#accession S30383 !'##molecule_type DNA !'##residues 1-295 ##label WIL !'##cross-references EMBL:M94775 !'##experimental_source strain M10 REFERENCE S14366 !$#authors Bruce, N.C.; Wilmot, C.J.; Jordan, K.N.; Stephens, L.D.G.; !1Lowe, C.R. !$#journal Biochem. J. (1991) 274:875-880 !$#title Microbial degradation of the morphine alkaloids. !1Purification and characterization of morphine dehydrogenase !1from Pseudomonas putida M10. !$#cross-references MUID:91190106; PMID:2012614 !$#accession S14366 !'##molecule_type protein !'##residues 2-26 ##label BRU !'##experimental_source M10 GENETICS !$#gene morA !$#genome plasmid pMdh7.2 FUNCTION !$#description catalyses the oxidation of morphine to morphinone CLASSIFICATION #superfamily aldehyde reductase KEYWORDS alkaloid degradation; monomer; NADP; oxidoreductase SUMMARY #length 295 #molecular-weight 32378 #checksum 6164 SEQUENCE /// ENTRY A45961 #type complete TITLE 2,5-diketo-D-gluconate reductase (EC 1.1.1.-) - Corynebacterium sp. (strain SHS752001) ORGANISM #formal_name Corynebacterium sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A45961 REFERENCE A45961 !$#authors Grindley, J.F.; Payton, M.A.; van de Pol, H.; Hardy, K.G. !$#journal Appl. Environ. Microbiol. (1988) 54:1770-1775 !$#title Conversion of glucose to 2-keto-L-gulonate, an intermediate !1in L-ascorbate synthesis, by a recombinant strain of Erwinia !1citreus. !$#accession A45961 !'##status preliminary !'##molecule_type DNA !'##residues 1-277 ##label GRI !'##cross-references GB:M21193; NID:g144962; PIDN:AAA23291.1; !1PID:g144963 CLASSIFICATION #superfamily aldehyde reductase KEYWORDS oxidoreductase SUMMARY #length 277 #molecular-weight 30548 #checksum 1477 SEQUENCE /// ENTRY A64745 #type complete TITLE probable aldehyde reductase (EC 1.1.1.-) yafB - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS A64745; I58331; JS0715 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64745 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-267 ##label BLAT !'##cross-references GB:AE000129; GB:U00096; NID:g1786395; !1PIDN:AAC73312.1; PID:g1786400; UWGP:b0207 !'##experimental_source strain K-12, substrain MG1655 REFERENCE I58331 !$#authors Sekiya, T.; Mori, M.; Takahashi, N.; Nishimura, S. !$#journal Nucleic Acids Res. (1980) 8:3809-3827 !$#title Sequence of the distal tRNA1Asp gene and the transcription !1termination signal in the Escherichia coli ribosomal RNA !1operon rrnF(or G). !$#cross-references MUID:81076581; PMID:6255418 !$#accession I58331 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-20 ##label RES !'##cross-references EMBL:V00336; NID:g42763; PIDN:CAA23619.1; !1PID:g42764 REFERENCE JS0715 !$#authors Nishimura, K.; Komine, Y.; Miyamoto, K.; Kitabatake, M.; !1Mathunaga, F.; Hisano, T.; Miki, T.; Inokuchi, H. !$#submission submitted to JIPID, July 1992 !$#accession JS0715 !'##status translation not shown !'##molecule_type DNA !'##residues 1-193,'AY',196-267 ##label NIS !'##cross-references DDBJ:D12650; NID:g216644; PIDN:BAA02170.1; !1PID:g216645 !'##experimental_source strain K12 GENETICS !$#gene yafB !$#map_position 5.2 min CLASSIFICATION #superfamily aldehyde reductase KEYWORDS oxidoreductase SUMMARY #length 267 #molecular-weight 29436 #checksum 1317 SEQUENCE /// ENTRY S76143 #type complete TITLE probable aldehyde reductase (EC 1.1.1.-) - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S76143 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76143 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-327 ##label KAN !'##cross-references EMBL:D90914; GB:AB001339; NID:g1653477; !1PIDN:BAA18402.1; PID:g1653489 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily aldehyde reductase KEYWORDS oxidoreductase SUMMARY #length 327 #molecular-weight 36014 #checksum 6899 SEQUENCE /// ENTRY JC4251 #type complete TITLE D-xylose 1-dehydrogenase (NADP) (EC 1.1.1.179) - yeast (Kluyveromyces marxianus var. lactis) ORGANISM #formal_name Kluyveromyces marxianus var. lactis, Candida sphaerica DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS JC4251 REFERENCE JC4251 !$#authors Billard, P.; Menart, S.; Fleer, R.; Bolotin-Fukuhara, M. !$#journal Gene (1995) 162:93-97 !$#title Isolation and characterization of the gene encoding xylose !1reductase from Kluyveromyces lactis. !$#cross-references MUID:96009884; PMID:7557424 !$#accession JC4251 !'##molecule_type DNA !'##residues 1-329 ##label BIL !'##cross-references GB:L36993; NID:g559294; PIDN:AAA99507.1; !1PID:g559295 COMMENT This enzyme is NADPH-dependent and essential for growth on !1xylose. GENETICS !$#gene xyl1 !$#map_position V CLASSIFICATION #superfamily aldehyde reductase KEYWORDS NADP; oxidoreductase SUMMARY #length 329 #molecular-weight 37516 #checksum 5185 SEQUENCE /// ENTRY S14222 #type complete TITLE chalcone reductase (EC 1.-.-.-) - soybean ORGANISM #formal_name Glycine max #common_name soybean DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S14222 REFERENCE S14222 !$#authors Welle, R.; Schroeder, G.; Schiltz, E.; Grisebach, H.; !1Schroeder, J. !$#journal Eur. J. Biochem. (1991) 196:423-430 !$#title Induced plant responses to pathogen attack. Analysis and !1heterologous expression of the key enzyme in the !1biosynthesis of phytoalexins in soybean (Glycine max L. !1Merr. cv. Harosoy 63). !$#cross-references MUID:91177016; PMID:1840523 !$#accession S14222 !'##status preliminary !'##molecule_type mRNA !'##residues 1-315 ##label WEL !'##cross-references EMBL:X55730; NID:g18727; PIDN:CAA39261.1; !1PID:g18728 CLASSIFICATION #superfamily aldehyde reductase KEYWORDS oxidoreductase SUMMARY #length 315 #molecular-weight 35490 #checksum 5688 SEQUENCE /// ENTRY S15024 #type complete TITLE aldose reductase-related protein - barley ORGANISM #formal_name Hordeum vulgare #common_name barley DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S15024 REFERENCE S15024 !$#authors Bartels, D.; Engelhardt, K.; Roncarati, R.; Schneider, K.; !1Rotter, M.; Salamini, F. !$#journal EMBO J. (1991) 10:1037-1043 !$#title An ABA and GA modulated gene expressed in the barley embryo !1encodes an aldose reductase related protein. !$#cross-references MUID:91216096; PMID:1827067 !$#accession S15024 !'##status preliminary !'##molecule_type DNA !'##residues 1-320 ##label BAR !'##cross-references EMBL:X57526; NID:g18890; PIDN:CAA40747.1; !1PID:g18891 CLASSIFICATION #superfamily aldehyde reductase SUMMARY #length 320 #molecular-weight 35807 #checksum 4795 SEQUENCE /// ENTRY S57117 #type complete TITLE probable aldehyde reductase (EC 1.1.1.-) YJR096w - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein J1926; protein YJR096w ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S57117 REFERENCE S57111 !$#authors Ramezani Rad, M.; Kirchrath, L.; Hollenberg, C.P. !$#submission submitted to the Protein Sequence Database, September 1995 !$#accession S57117 !'##molecule_type DNA !'##residues 1-282 ##label RAM !'##cross-references EMBL:Z49596; NID:g1015795; PIDN:CAA89626.1; !1PID:g1015796; GSPDB:GN00010; MIPS:YJR096w GENETICS !$#gene MIPS:YJR096w !'##cross-references SGD:S0003857 !$#map_position 10R CLASSIFICATION #superfamily aldehyde reductase KEYWORDS oxidoreductase SUMMARY #length 282 #molecular-weight 32344 #checksum 7349 SEQUENCE /// ENTRY S72569 #type complete TITLE probable aldehyde reductase (EC 1.1.1.-) C35D10.6 - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S72569 REFERENCE S72566 !$#authors Wilson, R.; Ainscough, R.; Anderson, K.; Baynes, C.; Berks, !1M.; Bonfield, J.; Burton, J.; Connell, M.; Copsey, T.; !1Cooper, J.; Coulson, A.; Craxton, M.; Dear, S.; Du, Z.; !1Durbin, R.; Favello, A.; Fulton, L.; Gardner, A.; Green, P.; !1Hawkins, T.; Hillier, L.; Jier, M.; Johnston, L.; Jones, M.; !1Kershaw, J.; Kirsten, J.; Laister, N.; Latreille, P.; !1Lightning, J.; Lloyd, C.; McMurray, A.; Mortimore, B.; !1O'Callaghan, M.; Parsons, J.; Percy, C.; Rifken, L.; Roopra, !1A.; Saunders, D.; Shownkeen, R.; Smaldon, N.; Smith, A.; !1Sonnhammer, E.; Staden, R.; Sulston, J.; Thierry-Mieg, J.; !1Thomas, K.; Vaudin, M.; Vaughan, K.; Waterston, R.; Watson, !1A.; Weinstock, L.; Wilkinson-Sproat, J.; Wohldman, P. !$#submission submitted to the EMBL Data Library, February 1995 !$#description The C. elegans genome project: Contiguous nucleotide !1sequence of over two megabases from chromosome III. !$#accession S72569 !'##molecule_type DNA !'##residues 1-287 ##label WIL !'##cross-references EMBL:U21324; NID:g687879; PIDN:AAA62562.1; !1PID:g687885 !'##experimental_source strain Bristol N2 GENETICS !$#map_position 3 !$#introns 20/3; 69/2; 195/3; 261/3 !$#note C35D10.6 CLASSIFICATION #superfamily aldehyde reductase KEYWORDS oxidoreductase SUMMARY #length 287 #molecular-weight 32840 #checksum 2540 SEQUENCE /// ENTRY E64938 #type complete TITLE probable aldehyde reductase (EC 1.1.1.-) b1781 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS E64938 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64938 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-284 ##label BLAT !'##cross-references GB:AE000273; GB:U00096; NID:g1788078; !1PIDN:AAC74851.1; PID:g1788081; UWGP:b1781 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily aldehyde reductase KEYWORDS oxidoreductase SUMMARY #length 284 #molecular-weight 30986 #checksum 1335 SEQUENCE /// ENTRY DEECHS #type complete TITLE homoserine dehydrogenase (EC 1.1.1.3) - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 30-Jun-1991 #sequence_revision 02-Jul-1998 #text_change 16-Jun-2000 ACCESSIONS A31973; C25364; D69642 REFERENCE A31973 !$#authors Parsot, C.; Cohen, G.N. !$#journal J. Biol. Chem. (1988) 263:14654-14660 !$#title Cloning and nucleotide sequence of the Bacillus subtilis hom !1gene coding for homoserine dehydrogenase. Structural and !1evolutionary relationships with Escherichia coli !1aspartokinases-homoserine dehydrogenases I and II. !$#cross-references MUID:89008330; PMID:3139660 !$#accession A31973 !'##molecule_type DNA !'##residues 1-401,'Q',403-433 ##label PAR1 !'##cross-references EMBL:M23217; NID:g340846; PIDN:AAA50609.1; !1PID:g558494 !'##note these authors used TTG as a start codon; the codon given for !1402-Glu (CAA) is inconsistent with the authors' translation REFERENCE A91055 !$#authors Parsot, C. !$#journal EMBO J. (1986) 5:3013-3019 !$#title Evolution of biosynthetic pathways: a common ancestor for !1threonine synthase, threonine dehydratase and D-serine !1dehydratase. !$#cross-references MUID:87080286; PMID:3098560 !$#accession C25364 !'##molecule_type DNA !'##residues 353-374,'T',376-433 ##label PAR2 !'##cross-references GB:X04603; NID:g40210; PIDN:CAA28269.1; PID:g809663 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D69642 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-433 ##label KUN !'##cross-references GB:Z99120; GB:AL009126; NID:g2635613; !1PIDN:CAB15216.1; PID:g2635723 !'##experimental_source strain 168 GENETICS !$#gene hom !$#map_position 78 min FUNCTION !$#description catalyzes the reduction of L-aspartate 4-semialdehyde to !1L-homoserine by NADH or NADPH !$#pathway threonine biosynthesis CLASSIFICATION #superfamily homoserine dehydrogenase; homoserine !1dehydrogenase homology KEYWORDS NADP; oxidoreductase; threonine biosynthesis FEATURE !$1-243 #domain homoserine dehydrogenase homology #label HSD\ !$5-33 #region beta-alpha-beta NADP nucleotide-binding fold SUMMARY #length 433 #molecular-weight 47494 #checksum 236 SEQUENCE /// ENTRY DEFKHG #type complete TITLE homoserine dehydrogenase (EC 1.1.1.3) - Corynebacterium glutamicum ORGANISM #formal_name Corynebacterium glutamicum DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 11-Jun-1999 ACCESSIONS S00865; S06325; JC5868 REFERENCE S00865 !$#authors Peoples, O.P.; Liebl, W.; Bodis, M.; Maeng, P.J.; Follettie, !1M.T.; Archer, J.A.; Sinskey, A.J. !$#journal Mol. Microbiol. (1988) 2:63-72 !$#title Nucleotide sequence and fine structural analysis of the !1Corynebacterium glutamicum hom-thrB operon. !$#cross-references MUID:88216182; PMID:2835591 !$#accession S00865 !'##molecule_type DNA !'##residues 1-445 ##label PEO !'##cross-references EMBL:Y00546; NID:g40502; PIDN:CAA68614.1; !1PID:g40503 REFERENCE S06325 !$#authors Mateos, L.M.; del Real, G.; Aguilar, A.; Martin, J.F. !$#journal Nucleic Acids Res. (1987) 15:10598 !$#title Nucleotide sequence of the homoserine dehydrogenase (thr A) !1gene of Brevibacterium lactofermentum. !$#cross-references MUID:88096601; PMID:3320973 !$#accession S06325 !'##molecule_type DNA !'##residues 1-445 ##label MAT !'##cross-references GB:Y00476; NID:g297382; PIDN:CAA68536.1; !1PID:g297383 !'##note the source is designated as Brevibacterium lactofermentum REFERENCE JC5868 !$#authors Sugimoto, M.; Tanaka, A.; Suzuki, T.; Matsui, H.; Nakamori, !1S.; Takagi, H. !$#journal Biosci. Biotechnol. Biochem. (1997) 61:1760-1762 !$#title Sequence analysis of functional regions of homoserine !1dehydrogenase genes from L-lysine and L-threonine-producing !1mutants of Brevibacterium lactofermentum. !$#cross-references MUID:98028217; PMID:9362124 !$#accession JC5868 !'##molecule_type DNA !'##residues 1-445 ##label SUG GENETICS !$#gene hom; thrA CLASSIFICATION #superfamily homoserine dehydrogenase; homoserine !1dehydrogenase homology KEYWORDS NADP; oxidoreductase; threonine biosynthesis FEATURE !$16-259 #domain homoserine dehydrogenase homology #label HSD\ !$20-48 #region beta-alpha-beta NAD(P) nucleotide-binding !8fold SUMMARY #length 445 #molecular-weight 46438 #checksum 8951 SEQUENCE /// ENTRY DEPSHA #type complete TITLE homoserine dehydrogenase (EC 1.1.1.3) - Pseudomonas aeruginosa ORGANISM #formal_name Pseudomonas aeruginosa DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 11-Jun-1999 ACCESSIONS S27979; S19918 REFERENCE S27979 !$#authors Clepet, C.; Borne, F.; Krishnapillai, V.; Baird, C.; Patte, !1J.C.; Cami, B. !$#journal Mol. Microbiol. (1992) 6:3109-3119 !$#title Isolation, organization and expression of the Pseudomonas !1aeruginosa threonine genes. !$#cross-references MUID:93086420; PMID:1333566 !$#accession S27979 !'##molecule_type DNA !'##residues 1-439 ##label CLE !'##cross-references EMBL:X65033; NID:g45328; PIDN:CAA46167.1; !1PID:g45329 GENETICS !$#gene hom !$#map_position 31 min CLASSIFICATION #superfamily homoserine dehydrogenase; homoserine !1dehydrogenase homology KEYWORDS NADP; oxidoreductase; threonine biosynthesis FEATURE !$6-246 #domain homoserine dehydrogenase homology #label HSD SUMMARY #length 439 #molecular-weight 46829 #checksum 8114 SEQUENCE /// ENTRY JC6049 #type complete TITLE homoserine dehydrogenase (EC 1.1.1.3) - Lactococcus lactis ORGANISM #formal_name Lactococcus lactis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS JC6049 REFERENCE JC6049 !$#authors Madsen, S.M.; Albrechtsen, B.; Hansen, E.B.; Israelsen, H. !$#journal J. Bacteriol. (1996) 178:3689-3694 !$#title Cloning and transcriptional analysis of two threonine !1biosynthetic genes from Lactococcus lactis MG1614. !$#cross-references MUID:96272237; PMID:8682767 !$#accession JC6049 !'##molecule_type mRNA !'##residues 1-428 ##label MAD !'##cross-references EMBL:X96988; NID:g1255938; PIDN:CAA65713.1; !1PID:g1255939 !'##experimental_source strain MG1614 COMMENT This enzyme is involved in threonine biosynthesis and the !1part of methionine biosynthetic pathway. It leads to !1reduction of aspartate semialdehyde to homoserine. GENETICS !$#gene hom CLASSIFICATION #superfamily homoserine dehydrogenase; homoserine !1dehydrogenase homology KEYWORDS methionine biosynthesis; oxidoreductase; threonine !1biosynthesis SUMMARY #length 428 #molecular-weight 46629 #checksum 1392 SEQUENCE /// ENTRY A64500 #type complete TITLE homoserine dehydrogenase (EC 1.1.1.3) - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A64500 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession A64500 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-336 ##label BUL !'##cross-references GB:U67600; GB:L77117; NID:g2826437; !1PIDN:AAB99622.1; PID:g1500499; TIGR:MJ1602 GENETICS !$#map_position FOR1574042-1575052 CLASSIFICATION #superfamily homoserine dehydrogenase; homoserine !1dehydrogenase homology KEYWORDS oxidoreductase FEATURE !$1-261 #domain homoserine dehydrogenase homology #label HSD\ !$2-30 #region beta-alpha-beta NAD(P) nucleotide-binding !8fold SUMMARY #length 336 #molecular-weight 36462 #checksum 8490 SEQUENCE /// ENTRY DEECHT #type complete TITLE histidinol dehydrogenase (EC 1.1.1.23) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS C64967; A26022; JQ0522; I41286 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64967 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-434 ##label BLAT !'##cross-references GB:AE000293; GB:U00096; NID:g2367127; !1PIDN:AAC75081.1; PID:g1788331; UWGP:b2020 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A26022 !$#authors Chiariotti, L.; Alifano, P.; Carlomagno, M.S.; Bruni, C.B. !$#journal Mol. Gen. Genet. (1986) 203:382-388 !$#title Nucleotide sequence of the Escherichia coli hisD gene and of !1the Escherichia coli and Salmonella typhimurium hisIE !1region. !$#cross-references MUID:86310273; PMID:3018428 !$#accession A26022 !'##molecule_type DNA !'##residues 1-14,'V',16-21,'T',23-149,'R',151-312,'S',314-402,'V', !1404-434 ##label CHI !'##cross-references GB:X03972; NID:g41697; PIDN:CAA27610.1; PID:g41698 !'##note the authors translated the codon GAA for residue 337 as Asp and !1GTG for residue 403 as Leu REFERENCE JQ0522 !$#authors Jovanovic, G.; Kostic, T.; Savic, D.J. !$#journal Nucleic Acids Res. (1990) 18:3634 !$#title Nucleotide and amino acid polymorphism in the gene for !1L-histidinol dehydrogenase of Escherichia coli K12. !$#cross-references MUID:90301483; PMID:2194167 !$#accession JQ0522 !'##molecule_type DNA !'##residues 1-156,'A',158-434 ##label JOV !'##cross-references EMBL:X52656; NID:g41919; PIDN:CAA36882.1; !1PID:g41920 !'##experimental_source strain K12 W3110 DY100 REFERENCE I41286 !$#authors Bruni, C.B.; Musti, A.M.; Frunzio, R.; Blasi, F. !$#journal J. Bacteriol. (1980) 142:32-42 !$#title Structural and physiological studies of the Escherichia coli !1histidine operon inserted into plasmid vectors. !$#cross-references MUID:80182046; PMID:6246067 !$#accession I41286 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 296-319 ##label RES !'##cross-references GB:M10483; NID:g146357; PIDN:AAA23962.1; !1PID:g146358 GENETICS !$#gene hisD !$#map_position 44 min CLASSIFICATION #superfamily histidinol dehydrogenase; histidinol !1dehydrogenase homology KEYWORDS histidine biosynthesis; oxidoreductase FEATURE !$38-428 #domain histidinol dehydrogenase homology #label HID SUMMARY #length 434 #molecular-weight 46110 #checksum 4875 SEQUENCE /// ENTRY DEEBHT #type complete TITLE histidinol dehydrogenase (EC 1.1.1.23) - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 28-May-1999 ACCESSIONS JS0157 REFERENCE JS0131 !$#authors Carlomagno, M.S.; Chiariotti, L.; Alifano, P.; Nappo, A.G.; !1Bruni, C.B. !$#journal J. Mol. Biol. (1988) 203:585-606 !$#title Structure and function of the Salmonella typhimurium and !1Escherichia coli K-12 histidine operons. !$#cross-references MUID:89094829; PMID:3062174 !$#accession JS0157 !'##molecule_type DNA !'##residues 1-434 ##label CAR !'##cross-references GB:X13464; NID:g47719; PIDN:CAA31823.1; PID:g47722 !'##note the authors translated the codons GTA and GTC for residues 214 !1and 252 as Asp, AAG for residue 280 as Arg, and AAC for !1residue 366 as Leu COMMENT This enzyme is involved in the histidine biosynthetic !1pathway. GENETICS !$#gene hisD !$#map_position 42 min CLASSIFICATION #superfamily histidinol dehydrogenase; histidinol !1dehydrogenase homology KEYWORDS histidine biosynthesis; oxidoreductase FEATURE !$38-428 #domain histidinol dehydrogenase homology #label HID SUMMARY #length 434 #molecular-weight 45888 #checksum 4567 SEQUENCE /// ENTRY A64008 #type complete TITLE histidinol dehydrogenase (EC 1.1.1.23) - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES protein HI0469 ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A64008 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession A64008 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-427 ##label TIGR !'##cross-references GB:U32729; GB:L42023; NID:g1573439; !1PIDN:AAC22128.1; PID:g1573447; TIGR:HI0469 CLASSIFICATION #superfamily histidinol dehydrogenase; histidinol !1dehydrogenase homology KEYWORDS histidine biosynthesis; oxidoreductase FEATURE !$35-423 #domain histidinol dehydrogenase homology #label HID SUMMARY #length 427 #molecular-weight 46339 #checksum 2105 SEQUENCE /// ENTRY A39358 #type complete TITLE histidinol dehydrogenase (EC 1.1.1.23) precursor, chloroplast [validated] - cabbage ORGANISM #formal_name Brassica oleracea var. capitata #common_name cabbage DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 17-Mar-2000 ACCESSIONS A39358; S23939 REFERENCE A39358 !$#authors Nagai, A.; Ward, E.; Beck, J.; Tada, S.; Chang, J.Y.; !1Scheidegger, A.; Ryals, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:4133-4137 !$#title Structural and functional conservation of histidinol !1dehydrogenase between plants and microbes. !$#cross-references MUID:91239521; PMID:2034659 !$#accession A39358 !'##status preliminary !'##molecule_type mRNA !'##residues 1-469 ##label NAG !'##cross-references GB:M60466; NID:g167141; PIDN:AAA32991.1; !1PID:g167142 REFERENCE S23939 !$#authors Nagai, A.; Suzuki, K.; Ward, E.; Moyer, M.; Hashimoto, M.; !1Mano, J.; Ohta, D.; Scheidegger, A. !$#journal Arch. Biochem. Biophys. (1992) 295:235-239 !$#title Overexpression of plant histidinol dehydrogenase using a !1baculovirus expression vector system. !$#cross-references MUID:92264718; PMID:1586152 !$#accession S23939 !'##molecule_type protein !'##residues 19-35 ##label NAW GENETICS !$#gene HDH FUNCTION !$#description EC 1.1.1.23 [validated, MUID:92264718] CLASSIFICATION #superfamily histidinol dehydrogenase; histidinol !1dehydrogenase homology KEYWORDS chloroplast; histidine biosynthesis; oxidoreductase FEATURE !$1-31 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$32-469 #product histidinol dehydrogenase #status !8experimental #label MAT\ !$66-459 #domain histidinol dehydrogenase homology #label HID SUMMARY #length 469 #molecular-weight 50958 #checksum 5 SEQUENCE /// ENTRY S26209 #type complete TITLE histidinol dehydrogenase (EC 1.1.1.23) - Mycobacterium smegmatis ORGANISM #formal_name Mycobacterium smegmatis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S26209; S25668 REFERENCE S26209 !$#authors Hinshelwood, S.; Stoker, N.G. !$#journal Mol. Microbiol. (1992) 6:2887-2895 !$#title Cloning of mycobacterial histidine synthesis genes by !1complementation of a Mycobacterium smegmatis auxotroph. !$#cross-references MUID:93062022; PMID:1435262 !$#accession S26209 !'##molecule_type DNA !'##residues 1-445 ##label HIN !'##cross-references EMBL:X65542; NID:g44515; PIDN:CAA46509.1; !1PID:g44516 GENETICS !$#gene hisD CLASSIFICATION #superfamily histidinol dehydrogenase; histidinol !1dehydrogenase homology KEYWORDS histidine biosynthesis; oxidoreductase FEATURE !$44-444 #domain histidinol dehydrogenase homology #label HID SUMMARY #length 445 #molecular-weight 46702 #checksum 7962 SEQUENCE /// ENTRY DEECDL #type complete TITLE D-lactate dehydrogenase (EC 1.1.1.28) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 01-Mar-2002 ACCESSIONS A21893; I41048; D64981 REFERENCE A21893 !$#authors Rule, G.S.; Pratt, E.A.; Chin, C.C.Q.; Wold, F.; Ho, C. !$#journal J. Bacteriol. (1985) 161:1059-1068 !$#title Overproduction and nucleotide sequence of the respiratory !1D-lactate dehydrogenase of Escherichia coli. !$#cross-references MUID:85130784; PMID:3882663 !$#accession A21893 !'##molecule_type DNA !'##residues 1-571 ##label RUL !'##cross-references GB:M10038; NID:g145752; PIDN:AAA23688.1; !1PID:g145753 !'##note this enzyme has been found on the inner surface of the !1cytoplasmic membrane REFERENCE I41048 !$#authors Campbell, H.D.; Rogers, B.L.; Young, I.G. !$#journal Eur. J. Biochem. (1984) 144:367-373 !$#title Nucleotide sequence of the respiratory D-lactate !1dehydrogenase gene of Escherichia coli. !$#cross-references MUID:85027231; PMID:6386470 !$#accession I41048 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-571 ##label RES !'##cross-references EMBL:X01067; NID:g41286; PIDN:CAA25531.1; !1PID:g41287 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64981 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-571 ##label BLAT !'##cross-references GB:AE000302; GB:U00096; NID:g1788447; !1PIDN:AAC75194.1; PID:g1788454; UWGP:b2133 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene dld !$#map_position 47 min CLASSIFICATION #superfamily D-lactate dehydrogenase KEYWORDS membrane protein; oxidoreductase; respiratory chain SUMMARY #length 571 #molecular-weight 64612 #checksum 610 SEQUENCE /// ENTRY DEHULH #type complete TITLE L-lactate dehydrogenase (EC 1.1.1.27) chain H - human ALTERNATE_NAMES L-lactate dehydrogenase B; lactic acid dehydrogenase ORGANISM #formal_name Homo sapiens #common_name man DATE 01-Dec-1989 #sequence_revision 18-Aug-1995 #text_change 16-Jun-2000 ACCESSIONS S02795; S06281 REFERENCE S02795 !$#authors Takeno, T.; Li, S.S.L. !$#journal Biochem. J. (1989) 257:921-924 !$#title Structure of the human lactate dehydrogenase B gene. !$#cross-references MUID:89193506; PMID:2930497 !$#accession S02795 !'##molecule_type DNA !'##residues 1-334 ##label TAK !'##cross-references EMBL:X13794; NID:g34314; PIDN:CAA32033.1; !1PID:g1200083 REFERENCE S06281 !$#authors Sakai, I.; Sharief, F.S.; Pan, Y.C.E.; Li, S.S.L. !$#journal Biochem. J. (1987) 248:933-936 !$#title The cDNA and protein sequences of human lactate !1dehydrogenase B. !$#cross-references MUID:88133965; PMID:3435492 !$#accession S06281 !'##molecule_type mRNA !'##residues 1-334 ##label SAK !'##cross-references GB:Y00711; NID:g34328; PIDN:CAA68701.1; PID:g34329 !'##note part of this sequence was confirmed by protein sequencing COMMENT This H chain form is predominantly expressed in heart !1muscle. GENETICS !$#gene GDB:LDHB !'##cross-references GDB:120147; OMIM:150100 !$#map_position 12p12.2-12p12.1 !$#introns 43/3; 83/1; 141/1; 199/1; 238/2; 279/3 COMPLEX homotetramer; heterotetramer with chain M FUNCTION !$#description catalyzes the reversible oxidation of lactate to pyruvate !1using NAD as coenzyme !$#pathway anaerobic glycolysis CLASSIFICATION #superfamily L-lactate dehydrogenase KEYWORDS acetylated amino end; NAD; oxidoreductase; tetramer FEATURE !$2-334 #product L-lactate dehydrogenase chain H #status !8predicted #label MAT\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status predicted\ !$167,194 #active_site Asp, His #status predicted SUMMARY #length 334 #molecular-weight 36638 #checksum 6440 SEQUENCE /// ENTRY A38231 #type complete TITLE L-lactate dehydrogenase (EC 1.1.1.27) - sea lamprey ORGANISM #formal_name Petromyzon marinus #common_name sea lamprey DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A38231 REFERENCE A38231 !$#authors Stock, D.W.; Whitt, G.S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:1799-1803 !$#title Evolutionary implications of the cDNA sequence of the single !1lactate dehydrogenase of a lamprey. !$#cross-references MUID:92179269; PMID:1542673 !$#accession A38231 !'##molecule_type mRNA !'##residues 1-334 ##label STO !'##cross-references GB:M74064; NID:g213205; PIDN:AAA49267.1; !1PID:g213206 !'##note sequence extracted from NCBI backbone (NCBIN:87197, !1NCBIP:87198) CLASSIFICATION #superfamily L-lactate dehydrogenase KEYWORDS NAD; oxidoreductase; tetramer FEATURE !$168,195 #active_site Asp, His #status predicted SUMMARY #length 334 #molecular-weight 36432 #checksum 6973 SEQUENCE /// ENTRY DEPGLH #type complete TITLE L-lactate dehydrogenase (EC 1.1.1.27) chain H - pig (tentative sequence) ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 31-Mar-2000 ACCESSIONS A91671; A94603; A00345 REFERENCE A91671 !$#authors Kiltz, H.H.; Keil, W.; Griesbach, M.; Petry, K.; Meyer, H. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1977) 358:123-127 !$#title The primary structure of porcine lactate dehydrogenase: !1isoenzymes M-4 and H-4. !$#cross-references MUID:77117453; PMID:838465 !$#accession A91671 !'##molecule_type protein !'##residues 1-20,'B',22-146,'A',148-214,'B',216,'Z',218-333 ##label KIL REFERENCE A94603 !$#authors Kiltz, H.H. !$#submission submitted to the Atlas, October 1977 !$#accession A94603 !'##molecule_type protein !'##residues 1-333 ##label KI2 REFERENCE A92870 !$#authors Grau, U.M.; Trommer, W.E.; Rossmann, M.G. !$#journal J. Mol. Biol. (1981) 151:289-307 !$#title Structure of the active ternary complex of pig heart lactate !1dehydrogenase with S-lac-NAD at 2.7 angstrom resolution. !$#cross-references MUID:82170431; PMID:7338899 !$#contents annotation; X-ray crystallography, 2.7 angstroms !$#note the structure of a complex with a coenzyme-substrate analog !1was solved COMMENT A tetramer of H chains is the predominant form of the enzyme !1in heart muscle. FUNCTION !$#description catalyzes the reversible oxidation of (S)-lactate to !1pyruvate by NAD+ CLASSIFICATION #superfamily L-lactate dehydrogenase KEYWORDS acetylated amino end; NAD; oxidoreductase; tetramer FEATURE !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$166,193 #active_site Asp, His #status predicted SUMMARY #length 333 #molecular-weight 36476 #checksum 6356 SEQUENCE /// ENTRY DECHLH #type complete TITLE L-lactate dehydrogenase (EC 1.1.1.27) chain H - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 03-Dec-1999 ACCESSIONS A00346 REFERENCE A94435 !$#authors Torff, H.J.; Becker, D.; Schwarzwalder, J. !$#book Pyridine Nucleotide Dependent Dehydrogenases, Sund, H., ed., !1pp.31-42, Walter de Gruyter, Berlin, 1977 !$#accession A00346 !'##molecule_type protein !'##residues 1-332 ##label TOR FUNCTION !$#description catalyzes the reversible oxidation of (S)-lactate to !1pyruvate by NAD+ CLASSIFICATION #superfamily L-lactate dehydrogenase KEYWORDS acetylated amino end; NAD; oxidoreductase FEATURE !$1 #modified_site acetylated amino end (Ala) #status !8predicted\ !$165,192 #active_site Asp, His #status predicted SUMMARY #length 332 #molecular-weight 36185 #checksum 1403 SEQUENCE /// ENTRY DEHULM #type complete TITLE L-lactate dehydrogenase (EC 1.1.1.27) chain M - human ALTERNATE_NAMES L-lactate dehydrogenase A; lactic acid dehydrogenase ORGANISM #formal_name Homo sapiens #common_name man DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 28-Jan-2000 ACCESSIONS A00347; I37993; I54259 REFERENCE A00347 !$#authors Tsujibo, H.; Tiano, H.F.; Li, S.S.L. !$#journal Eur. J. Biochem. (1985) 147:9-15 !$#title Nucleotide sequences of the cDNA and an intronless !1pseudogene for human lactate dehydrogenase-A isozyme. !$#cross-references MUID:85127030; PMID:3838278 !$#accession A00347 !'##molecule_type mRNA !'##residues 1-332 ##label TSU !'##cross-references GB:X02152; NID:g34312; PIDN:CAA26088.1; PID:g34313 REFERENCE I37993 !$#authors Chung, F.Z.; Tsujibo, H.; Bhattacharyya, U.; Sharief, F.S.; !1LI, S.S. !$#journal Biochem. J. (1985) 231:537-541 !$#title Genomic organization of human lactate dehydrogenase-A gene. !$#cross-references MUID:86076881; PMID:3000353 !$#accession I37993 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-332 ##label CHU !'##cross-references EMBL:X03077; NID:g34301; PIDN:CAA26879.1; !1PID:g780261 REFERENCE I54259 !$#authors Maekawa, M.; Sudo, K.; Li, S.S.; Kanno, T. !$#journal Hum. Genet. (1991) 88:34-38 !$#title Genotypic analysis of families with lactate dehydrogenase A !1(M) deficiency by selective DNA amplification. !$#cross-references MUID:92070941; PMID:1959923 !$#accession I54259 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 249-253,'REYNEES' ##label MAE !'##cross-references GB:S66853; NID:g239612; PIDN:AAB20418.1; !1PID:g239613 COMMENT This M chain form is predominantly expressed in skeletal !1muscle. GENETICS !$#gene GDB:LDHA !'##cross-references GDB:120141; OMIM:150000 !$#map_position 11p15.4-11p15.4 !$#introns 42/3; 82/1; 140/1; 198/1; 237/2; 278/3 COMPLEX homotetramer; heterotetramer with chain H FUNCTION !$#description catalyzes the reversible oxidation of lactate to pyruvate !1using NAD as coenzyme !$#pathway anaerobic glycolysis CLASSIFICATION #superfamily L-lactate dehydrogenase KEYWORDS acetylated amino end; NAD; oxidoreductase; tetramer FEATURE !$2-332 #product L-lactate dehydrogenase chain M #status !8predicted #label MAT\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status predicted\ !$166,193 #active_site Asp, His #status predicted SUMMARY #length 332 #molecular-weight 36688 #checksum 7516 SEQUENCE /// ENTRY DEMSLM #type complete TITLE L-lactate dehydrogenase (EC 1.1.1.27) chain M - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 24-Nov-1999 ACCESSIONS A25205; S06290; I54769 REFERENCE A25205 !$#authors Li, S.S.L.; Tiano, H.F.; Fukasawa, K.M.; Yagi, K.; Shimizu, !1M.; Sharief, F.S.; Nakashima, Y.; Pan, Y.E. !$#journal Eur. J. Biochem. (1985) 149:215-225 !$#title Protein structure and gene organization of mouse lactate !1dehydrogenase-A isozyme. !$#cross-references MUID:85203900; PMID:3996406 !$#accession A25205 !'##molecule_type DNA !'##residues 1-332 ##label LIS !'##note the authors translated the codon ATT for residue 11 as Asn !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing REFERENCE S06290 !$#authors Fukasawa, K.M.; Li, S.S.L. !$#journal Genetics (1987) 116:99-105 !$#title Complete nucleotide sequence of the mouse lactate !1dehydrogenase-A functional gene: comparison of the !1exon-intron organization of dehydrogenase genes. !$#cross-references MUID:87248042; PMID:3036647 !$#accession S06290 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-10,'N',12-332 ##label FUK !'##cross-references GB:Y00309; GB:M27554; NID:g52881; PIDN:CAA68410.1; !1PID:g535924 REFERENCE I54769 !$#authors Akai, K.; Yagi, K.; Tiano, H.F.; Pan, Y. !$#journal Int. J. Biochem. (1985) 17:645-648 !$#title Isolation and characterization of a cDNA and a pseudogene !1for mouse lactate dehydrogenase-A isozyme. !$#cross-references MUID:85285968; PMID:2993055 !$#accession I54769 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 202-332 ##label RES !'##cross-references GB:M17516; NID:g198776; PIDN:AAA39424.1; !1PID:g387404 GENETICS !$#gene LDH-A !$#map_position 7 !$#introns 42/3; 82/1; 140/1; 198/1; 237/2; 278/3 FUNCTION !$#description catalyzes the reversible oxidation of (S)-lactate to !1pyruvate by NAD+ CLASSIFICATION #superfamily L-lactate dehydrogenase KEYWORDS blocked amino end; NAD; oxidoreductase; tetramer FEATURE !$2-332 #product L-lactate dehydrogenase chain M #status !8predicted #label MAT\ !$2 #modified_site blocked amino end (Ala) (in mature !8form) (probably acetylated) #status experimental\ !$166,193 #active_site Asp, His #status predicted SUMMARY #length 332 #molecular-weight 36497 #checksum 6573 SEQUENCE /// ENTRY DEPGLM #type complete TITLE L-lactate dehydrogenase (EC 1.1.1.27) chain M - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 06-Dec-1996 ACCESSIONS A00348 REFERENCE A91671 !$#authors Kiltz, H.H.; Keil, W.; Griesbach, M.; Petry, K.; Meyer, H. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1977) 358:123-127 !$#title The primary structure of porcine lactate dehydrogenase: !1isoenzymes M-4 and H-4. !$#cross-references MUID:77117453; PMID:838465 !$#accession A00348 !'##molecule_type protein !'##residues 1-331 ##label KIL FUNCTION !$#description catalyzes the reversible oxidation of (S)-lactate to !1pyruvate by NAD+ CLASSIFICATION #superfamily L-lactate dehydrogenase KEYWORDS acetylated amino end; NAD; oxidoreductase; tetramer FEATURE !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$165,192 #active_site Asp, His #status predicted SUMMARY #length 331 #molecular-weight 36487 #checksum 2715 SEQUENCE /// ENTRY DECHLM #type complete TITLE L-lactate dehydrogenase (EC 1.1.1.27) chain M - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 03-Dec-1999 ACCESSIONS A00349 REFERENCE A94435 !$#authors Torff, H.J.; Becker, D.; Schwarzwalder, J. !$#book Pyridine Nucleotide Dependent Dehydrogenases, Sund, H., ed., !1pp.31-42, Walter de Gruyter, Berlin, 1977 !$#accession A00349 !'##molecule_type protein !'##residues 1-331 ##label TOR FUNCTION !$#description catalyzes the reversible oxidation of (S)-lactate to !1pyruvate by NAD+ CLASSIFICATION #superfamily L-lactate dehydrogenase KEYWORDS acetylated amino end; NAD; oxidoreductase FEATURE !$1 #modified_site acetylated amino end (Ser) #status !8predicted\ !$165,192 #active_site Asp, His #status predicted SUMMARY #length 331 #molecular-weight 36388 #checksum 9984 SEQUENCE /// ENTRY DEDFLM #type complete TITLE L-lactate dehydrogenase (EC 1.1.1.27) chain M - spiny dogfish ORGANISM #formal_name Squalus acanthias #common_name spiny dogfish DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 06-Dec-1996 ACCESSIONS A00350 REFERENCE A92200 !$#authors Taylor, S.S. !$#journal J. Biol. Chem. (1977) 252:1799-1806 !$#title Amino acid sequence of dogfish muscle lactate dehydrogenase. !$#cross-references MUID:77118674; PMID:838743 !$#accession A00350 !'##molecule_type protein !'##residues 1-329 ##label TAY REFERENCE A93811 !$#authors Eventoff, W.; Rossmann, M.G.; Taylor, S.S.; Torff, H.J.; !1Meyer, H.; Keil, W.; Kiltz, H.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1977) 74:2677-2681 !$#title Structural adaptations of lactate dehydrogenase isozymes. !$#cross-references MUID:77257015; PMID:197516 !$#contents annotation; X-ray crystallography, 2.0 angstroms !$#note Arg-99 and Arg-169 are involved in substrate binding. !1Arg-106 is involved in binding the coenzyme nicotine adenine !1dinucleotide. His-193 accepts a proton during catalysis !$#note Cys-163, previously thought to be essential, does not appear !1to participate in catalysis or in substrate or coenzyme !1binding COMMENT A tetramer of M chains is the predominant form of the enzyme !1in skeletal muscle. FUNCTION !$#description catalyzes the reversible oxidation of (S)-lactate to !1pyruvate by NAD+ CLASSIFICATION #superfamily L-lactate dehydrogenase KEYWORDS acetylated amino end; NAD; oxidoreductase; tetramer FEATURE !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$166 #active_site Asp #status predicted\ !$193 #active_site His #status experimental SUMMARY #length 329 #molecular-weight 36421 #checksum 6296 SEQUENCE /// ENTRY DEHULC #type complete TITLE L-lactate dehydrogenase (EC 1.1.1.27) chain X - human ALTERNATE_NAMES L-lactate dehydrogenase C; lactic acid dehydrogenase ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1989 #sequence_revision 31-Dec-1992 #text_change 11-Jun-1999 ACCESSIONS A30933; A28330 REFERENCE A30933 !$#authors Takano, T.; Li, S.S.L. !$#journal Biochem. Biophys. Res. Commun. (1989) 159:579-583 !$#title Human testicular lactate dehydrogenase-C gene is interrupted !1by six introns at positions homologous to those of LDH-A !1(muscle) and LDH-B (heart) genes. !$#cross-references MUID:89193640; PMID:2930531 !$#accession A30933 !'##molecule_type DNA !'##residues 42-308 ##label LIS REFERENCE A28330 !$#authors Millan, J.L.; Driscoll, C.E.; LeVan, K.M.; Goldberg, E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:5311-5315 !$#title Epitopes of human testis-specific lactate dehydrogenase !1deduced from a cDNA sequence. !$#cross-references MUID:87260977; PMID:2440048 !$#accession A28330 !'##molecule_type mRNA !'##residues 1-118,'I',120-332 ##label MIL !'##cross-references GB:J02938; NID:g187065; PIDN:AAA59507.1; !1PID:g307120 COMMENT This testis-specific protein is synthesized only in the !1spermatogenic tissue of mammals and birds. The active enzyme !1is a homotetramer. GENETICS !$#gene GDB:LDHC !'##cross-references GDB:120150; OMIM:150150 !$#map_position 11p15.5-11p15.3 !$#introns 42/3; 82/1; 140/1; 198/1; 237/2; 278/3 FUNCTION !$#description catalyzes the reversible oxidation of lactate to pyruvate !1using NAD as coenzyme !$#pathway anaerobic glycolysis CLASSIFICATION #superfamily L-lactate dehydrogenase KEYWORDS acetylated amino end; homotetramer; NAD; oxidoreductase FEATURE !$2-309 #product L-lactate dehydrogenase chain X #status !8predicted #label MAT\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status predicted\ !$166,193 #active_site Asp, His #status predicted SUMMARY #length 332 #molecular-weight 36297 #checksum 7689 SEQUENCE /// ENTRY DEMSLC #type complete TITLE L-lactate dehydrogenase (EC 1.1.1.27) chain X [validated] - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1979 #sequence_revision 20-Aug-1994 #text_change 03-Nov-2000 ACCESSIONS A26824; A24347; A27246; A00351; A27879 REFERENCE A26824 !$#authors Wu, K.C.; Chan, K.; Lee, C.Y.G.; Lau, Y.F. !$#journal Biochem. Biophys. Res. Commun. (1987) 146:964-970 !$#title Molecular isolation and sequence determination of the cDNA !1for the mouse sperm-specific lactate dehydrogenase-X gene. !$#cross-references MUID:87298613; PMID:3619944 !$#accession A26824 !'##molecule_type mRNA !'##residues 1-332 ##label WUK !'##cross-references GB:M17587; NID:g198781; PIDN:AAA39425.1; !1PID:g293698 REFERENCE A24347 !$#authors Tanaka, S.; Fujimoto, H. !$#journal Biochem. Biophys. Res. Commun. (1986) 136:760-766 !$#title A postmeiotically expressed clone encodes lactate !1dehydrogenase isozyme X. !$#cross-references MUID:86215264; PMID:3754749 !$#accession A24347 !'##molecule_type mRNA !'##residues 194-332 ##label TAN !'##cross-references GB:M12781; NID:g198783; PIDN:AAA88315.1; !1PID:g198784 REFERENCE A92426 !$#authors Pan, Y.C.E.; Sharief, F.S.; Okabe, M.; Huang, S.; Li, S.S.L. !$#journal J. Biol. Chem. (1983) 258:7005-7016 !$#title Amino acid sequence studies on lactate dehydrogenase C-4 !1isozymes from mouse and rat testes. !$#cross-references MUID:83213445; PMID:6343385 !$#accession A27246 !'##molecule_type protein !'##residues 2-6,'E',8-14,16-29,'D',31-55,'D',57-103,'Q',105-123,'VI', !1126-134,'V',136-222,'N',224,'Q',226-242,'D',244-296,'E', !1298-328,'N',330,'E',332 ##label PA2 REFERENCE A91692 !$#authors Pan, Y.C.E.; Huang, S.; Marciniszyn Jr., J.P.; Lee, C.Y.; !1Li, S.S.L. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1980) 361:795-799 !$#title The preliminary amino acid sequence of mouse testicular !1lactate dehydrogenase. !$#cross-references MUID:81045459; PMID:7429427 !$#accession A00351 !'##molecule_type protein !'##residues 2-6,'E',8-9,'ZB',12-14,16-29,'B',31-53,'B',55,'B',57-103, !1'Q',105-134,'V',136-137,'B',139-154,'GV',157-188,'I', !1190-214,'B',216-220,'BKBSZ',226-232,'G',234-235,'BSAAZIIG', !1244-257,'B',259-296,'ZA',299-301,'B',303-304,'S',306,'BL', !1309,'PBZVAH',316-324,'B',326-330,'E',332 ##label PAN REFERENCE A27879 !$#authors Sakai, I.; Sharief, F.S.; Li, S.S.L. !$#journal Biochem. J. (1987) 242:619-622 !$#title Molecular cloning and nucleotide sequence of the cDNA for !1sperm-specific lactate dehydrogenase-C from mouse. !$#cross-references MUID:87241369; PMID:2439071 !$#accession A27879 !'##molecule_type mRNA !'##residues 1-332 ##label SAK !'##cross-references GB:X04752; NID:g52885; PIDN:CAA28449.1; PID:g52886 REFERENCE A92258 !$#authors Musick, W.D.L.; Rossmann, M.G. !$#journal J. Biol. Chem. (1979) 254:7611-7620 !$#title The structure of mouse testicular lactate dehydrogenase !1isoenzyme C-4 at 2.9 angstrom resolution. !$#cross-references MUID:79239334; PMID:468772 !$#contents annotation; X-ray crystallography, 2.9 angstroms COMMENT Lactate dehydrogenase X chains are synthesized only in !1spermatogenic tissue. GENETICS !$#gene Ldh-x; Ldh-c COMPLEX homotetramer FUNCTION !$#description catalyzes the reversible oxidation of (S)-lactate to !1pyruvate by NAD+ CLASSIFICATION #superfamily L-lactate dehydrogenase KEYWORDS blocked amino end; homotetramer; NAD; oxidoreductase FEATURE !$2-332 #product L-lactate dehydrogenase chain X #status !8experimental #label MAT\ !$2 #modified_site blocked amino end (Ser) (in mature !8form) (probably acetylated) #status experimental\ !$166,193 #active_site Asp, His #status predicted SUMMARY #length 332 #molecular-weight 35912 #checksum 7732 SEQUENCE /// ENTRY DELBLA #type complete TITLE L-lactate dehydrogenase (EC 1.1.1.27) - Lactobacillus casei ORGANISM #formal_name Lactobacillus casei DATE 18-Apr-1984 #sequence_revision 31-Dec-1993 #text_change 07-Feb-1997 ACCESSIONS A43944; JU0280; A00352 REFERENCE A43944 !$#authors Kim, S.F.; Baek, S.J.; Pack, M.Y. !$#journal Appl. Environ. Microbiol. (1991) 57:2413-2417 !$#title Cloning and nucleotide sequence of the Lactobacillus casei !1lactate dehydrogenase gene. !$#cross-references MUID:92117575; PMID:1768113 !$#accession A43944 !'##molecule_type DNA !'##residues 1-326 ##label KIM !'##experimental_source strain ATCC 393 !'##note sequence extracted from NCBI backbone (NCBIN:77578, !1NCBIP:77579) REFERENCE JU0280 !$#authors Taguchi, H.; Ohta, T. !$#submission submitted to JIPID, November 1991 !$#accession JU0280 !'##molecule_type DNA !'##residues 2-326 ##label TAG !'##experimental_source strain ATCC393 REFERENCE A00352 !$#authors Hensel, R.; Mayr, U.; Yang, C. !$#journal Eur. J. Biochem. (1983) 134:503-511 !$#title The complete primary structure of the allosteric L-lactate !1dehydrogenase from Lactobacillus casei. !$#cross-references MUID:83287369; PMID:6411465 !$#accession A00352 !'##molecule_type protein !'##residues 2-25,'F',27-51,'T',53-87,'KQ',90-118,'L',120-269,'I', !1271-272,'L',274-326 ##label HEN GENETICS !$#gene l-lct FUNCTION !$#description catalyzes the reversible oxidation of (S)-lactate to !1pyruvate by NAD+ CLASSIFICATION #superfamily L-lactate dehydrogenase KEYWORDS homotetramer; NAD; oxidoreductase FEATURE !$2-326 #product L-lactate dehydrogenase #status experimental !8#label MAT\ !$11-41 #region beta-alpha-beta NAD nucleotide-binding fold\ !$154,181 #active_site Asp, His #status predicted SUMMARY #length 326 #molecular-weight 35530 #checksum 165 SEQUENCE /// ENTRY DEBSLF #type complete TITLE L-lactate dehydrogenase (EC 1.1.1.27) [validated] - Bacillus stearothermophilus ORGANISM #formal_name Bacillus stearothermophilus DATE 03-Aug-1984 #sequence_revision 07-Feb-1997 #text_change 03-Nov-2000 ACCESSIONS A26053; A29704; A91726; A00353 REFERENCE A26053 !$#authors Barstow, D.A.; Clarke, A.R.; Chia, W.N.; Wigley, D.; !1Sharman, A.F.; Holbrook, J.J.; Atkinson, T.; Minton, N.P. !$#journal Gene (1986) 46:47-55 !$#title Cloning, expression and complete nucleotide sequence of the !1Bacillus stearothermophilus L-lactate dehydrogenase gene. !$#cross-references MUID:87106842; PMID:3026926 !$#accession A26053 !'##molecule_type DNA !'##residues 1-317 ##label BAR !'##cross-references GB:M14788; NID:g143139; PIDN:AAA22568.1; !1PID:g143140 REFERENCE A29704 !$#authors Zuelli, F.; Weber, H.; Zuber, H. !$#journal Biol. Chem. Hoppe-Seyler (1987) 368:1167-1177 !$#title Structure and function of L-lactate dehydrogenases from !1thermophilic and mesophilic bacteria, VI. Nucleotide !1sequences of lactate dehydrogenase genes from the !1thermophilic bacteria Bacillus stearothermophilus, Bacillus !1caldolyticus and Bacillus caldotenax. !$#cross-references MUID:88050101; PMID:3675869 !$#accession A29704 !'##status preliminary !'##molecule_type DNA !'##residues 1-317 ##label ZUE !'##cross-references GB:M19396; GB:M19386; NID:g143137; PIDN:AAA22567.1; !1PID:g143138 REFERENCE A91726 !$#authors Wirz, B.; Suter, F.; Zuber, H. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1983) 364:893-909 !$#title Structure and function of L-lactate dehydrogenases from !1thermophilic and mesophilic bacteria. !$#cross-references MUID:84006440; PMID:6352452 !$#accession A91726 !'##molecule_type protein !'##residues 1-107,'SE',110-112,'H',114-317 ##label WIR !'##experimental_source NCIB 8924 REFERENCE A91725 !$#authors Tratschin, J.D.; Wirz, B.; Frank, G.; Zuber, H. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1983) 364:879-892 !$#title Structure and function of L-lactate dehydrogenases from !1thermophilic and mesophilic bacteria. II. The primary !1structure of thermophilic lactate dehydrogenase from !1Bacillus stearothermophilus. Cyanogen bromide fragments and !1partial sequence. !$#cross-references MUID:84006439; PMID:6618448 !$#contents annotation; CNBr fragments; partial sequence !$#note strain NCIB 8924 FUNCTION !$#description catalyzes the reversible oxidation of (S)-lactate to !1pyruvate by NAD+ CLASSIFICATION #superfamily L-lactate dehydrogenase KEYWORDS NAD; oxidoreductase; tetramer FEATURE !$8-38 #region beta-alpha-beta NAD nucleotide-binding fold\ !$152,179 #active_site Asp, His #status predicted SUMMARY #length 317 #molecular-weight 34862 #checksum 4862 SEQUENCE /// ENTRY DEBSLM #type complete TITLE L-lactate dehydrogenase (EC 1.1.1.27) - Bacillus megaterium ORGANISM #formal_name Bacillus megaterium DATE 03-Aug-1984 #sequence_revision 30-Sep-1991 #text_change 11-Jun-1999 ACCESSIONS S00133; S01472; A00354 REFERENCE S00133 !$#authors Waldvogel, S.; Weber, H.; Zuber, H. !$#journal Biol. Chem. Hoppe-Seyler (1987) 368:1391-1399 !$#title Structure and function of L-lactate dehydrogenases from !1thermophilic and mesophilic bacteria VII. Nucleotide !1sequence of the lactate dehydrogenase gene from the !1mesophilic bacterium Bacillus megaterium. Preparation and !1properties of a hybrid lactate dehydrogenase comprising !1moieties of the B. megaterium and B. stearothermophilus !1enzymes. !$#cross-references MUID:88107005; PMID:3122782 !$#accession S00133 !'##molecule_type DNA !'##residues 1-318 ##label WAL !'##cross-references EMBL:M22305; NID:g143135; PIDN:AAA22566.1; !1PID:g143136 REFERENCE S01472 !$#authors Stangl, D.; Wiederkehr, F.; Suter, F.; Zuber, H. !$#journal Biol. Chem. Hoppe-Seyler (1987) 368:1157-1166 !$#title Structure and function of L-lactate dehydrogenases from !1thermophilic and mesophilic bacteria, V. The complete !1amino-acid sequence of the mesophilic L-lactate !1dehydrogenase from Bacillus megaterium. !$#cross-references MUID:88050100; PMID:3118900 !$#accession S01472 !'##molecule_type protein !'##residues 1-318 ##label STA COMMENT This enzyme is activated by fructose-1,6-diphosphate. FUNCTION !$#description catalyzes the reversible oxidation of (S)-lactate to !1pyruvate by NAD+ CLASSIFICATION #superfamily L-lactate dehydrogenase KEYWORDS homotetramer; NAD; oxidoreductase FEATURE !$1-318 #product L-lactate dehydrogenase #status experimental !8#label MAT\ !$11-41 #region beta-alpha-beta NAD nucleotide-binding fold\ !$154,181 #active_site Asp, His #status predicted SUMMARY #length 318 #molecular-weight 35035 #checksum 5138 SEQUENCE /// ENTRY JX0090 #type complete TITLE L-lactate dehydrogenase (EC 1.1.1.27) - Thermus aquaticus (strain YT-1) ORGANISM #formal_name Thermus aquaticus DATE 07-Sep-1990 #sequence_revision 07-Oct-1994 #text_change 16-Jun-2000 ACCESSIONS JX0090; A22394 REFERENCE JX0090 !$#authors Ono, M.; Matsuzawa, H.; Ohta, T. !$#journal J. Biochem. (1990) 107:21-26 !$#title Nucleotide sequence and characteristics of the gene for !1L-lactate dehydrogenase of Thermus aquaticus YT-1 and the !1deduced amino acid sequence of the enzyme. !$#cross-references MUID:90236973; PMID:2185236 !$#accession JX0090 !'##molecule_type DNA !'##residues 1-310 ##label ONO !'##cross-references GB:D00585; NID:g217175; PIDN:BAA00463.1; !1PID:g912427 !'##experimental_source strain YT-1 !'##note the authors translated the codon CGG for residue 136 as Gly REFERENCE A22394 !$#authors Machida, M.; Matsuzawa, H.; Ohta, T. !$#journal J. Biochem. (1985) 97:899-909 !$#title Fructose 1,6-bisphosphate-dependent L-lactate dehydrogenase !1from Thermus aquaticus YT-1, and extreme thermophile: !1activation by citrate and modification reagents and !1comparison with Thermus caldophilus GK24 L-lactate !1dehydrogenase. !$#cross-references MUID:85261181; PMID:4019440 !$#accession A22394 !'##molecule_type protein !'##residues 1-33,'R' ##label MAC !'##experimental_source strain YT-1 GENETICS !$#start_codon GTG FUNCTION !$#description catalyzes the reversible oxidation of (S)-lactate to !1pyruvate by NAD+ CLASSIFICATION #superfamily L-lactate dehydrogenase KEYWORDS homotetramer; NAD; oxidoreductase FEATURE !$1-310 #product L-lactate dehydrogenase #status predicted !8#label MAT\ !$145,172 #active_site Asp, His #status predicted SUMMARY #length 310 #molecular-weight 33210 #checksum 1429 SEQUENCE /// ENTRY DEPGMM #type complete TITLE malate dehydrogenase (EC 1.1.1.37), mitochondrial - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 15-Jun-1996 ACCESSIONS A00355; S00204; S01480 REFERENCE A00355 !$#authors Birktoft, J.J.; Fernley, R.T.; Bradshaw, R.A.; Banaszak, !1L.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:6166-6170 !$#title Amino acid sequence homology among the 2-hydroxy acid !1dehydrogenases: mitochondrial and cytoplasmic malate !1dehydrogenases form a homologous system with lactate !1dehydrogenase. !$#cross-references MUID:83065139; PMID:6959107 !$#accession A00355 !'##molecule_type protein !'##residues 1-314 ##label BIR REFERENCE S00194 !$#authors Joh, T.; Takeshima, H.; Tsuzuki, T.; Shimada, K.; Tanase, !1S.; Morino, Y. !$#journal Biochemistry (1987) 26:2515-2520 !$#title Cloning and sequence analysis of cDNAs encoding mammalian !1mitochondrial malate dehydrogenase. !$#cross-references MUID:87271646; PMID:3038184 !$#accession S00204 !'##molecule_type mRNA !'##residues 17-95,'M',97-101,'V',103-125,'M',127-312,'T',314 ##label !1JOH !'##cross-references EMBL:M16427 !'##note the authors translated the codon ATG for residues 80 and 110 as !1Ile and GTC for residue 86 as Ala CLASSIFICATION #superfamily L-lactate dehydrogenase KEYWORDS homodimer; mitochondrion; NAD; oxidoreductase; tricarboxylic !1acid cycle FEATURE !$1-146 #domain NAD binding #status predicted #label NAD\ !$147-314 #domain catalytic #status predicted #label CAT\ !$149,176 #active_site Asp, His #status predicted\ !$152 #binding_site substrate (Arg) #status predicted SUMMARY #length 314 #molecular-weight 33082 #checksum 7445 SEQUENCE /// ENTRY DERTMM #type complete TITLE malate dehydrogenase (EC 1.1.1.37) precursor, mitochondrial - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 11-Jun-1999 ACCESSIONS A25509; A26474; S00193 REFERENCE A25509 !$#authors Grant, P.M.; Tellam, J.; May, V.L.; Strauss, A.W. !$#journal Nucleic Acids Res. (1986) 14:6053-6066 !$#title Isolation and nucleotide sequence of a cDNA clone encoding !1rat mitochondrial malate dehydrogenase. !$#cross-references MUID:86312879; PMID:3755817 !$#accession A25509 !'##molecule_type mRNA !'##residues 1-338 ##label GRA1 !'##cross-references EMBL:X04240; NID:g56642; PIDN:CAA27812.1; !1PID:g56643 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing !'##note 229-Arg and 299-Ile were also found REFERENCE A26474 !$#authors Grant, P.M.; Roderick, S.L.; Grant, G.A.; Banaszak, L.J.; !1Strauss, A.W. !$#journal Biochemistry (1987) 26:128-134 !$#title Comparison of the precursor and mature forms of rat heart !1mitochondrial malate dehydrogenase. !$#cross-references MUID:87157605; PMID:3828294 !$#accession A26474 !'##molecule_type protein !'##residues 25-228,'R',230-298,'I',300-338 ##label GRA2 CLASSIFICATION #superfamily L-lactate dehydrogenase KEYWORDS homodimer; mitochondrion; NAD; oxidoreductase; tricarboxylic !1acid cycle FEATURE !$1-24 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$25-338 #product malate dehydrogenase, mitochondrial #status !8experimental #label MAT\ !$173,200 #active_site Asp, His #status predicted\ !$176 #binding_site substrate (Arg) #status predicted SUMMARY #length 338 #molecular-weight 35655 #checksum 5723 SEQUENCE /// ENTRY DEMSMM #type complete TITLE malate dehydrogenase (EC 1.1.1.37) precursor, mitochondrial - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 31-Dec-1993 ACCESSIONS S01350; S00194; S17074 REFERENCE S01350 !$#authors Takeshima, H.; Joh, T.; Tsuzuki, T.; Shimada, K.; Matsukado, !1Y. !$#journal J. Mol. Biol. (1988) 200:1-11 !$#title Structural organization of the mouse mitochondrial malate !1dehydrogenase gene. !$#cross-references MUID:88245174; PMID:3379635 !$#accession S01350 !'##molecule_type DNA !'##residues 1-338 ##label TAK !'##cross-references EMBL:X07295 REFERENCE S00194 !$#authors Joh, T.; Takeshima, H.; Tsuzuki, T.; Shimada, K.; Tanase, !1S.; Morino, Y. !$#journal Biochemistry (1987) 26:2515-2520 !$#title Cloning and sequence analysis of cDNAs encoding mammalian !1mitochondrial malate dehydrogenase. !$#cross-references MUID:87271646; PMID:3038184 !$#accession S00194 !'##molecule_type mRNA !'##residues 1-75,'K',77-338 ##label JOH1 !'##cross-references EMBL:M16229 REFERENCE S17074 !$#authors Joh, T.; Takeshima, H.; Tsuzuki, T.; Shimada, K.; Tanase, !1S.; Morino, Y. !$#submission submitted to the EMBL Data Library, July 1987 !$#accession S17074 !'##molecule_type mRNA !'##residues 1-75,'K',76-268,'L',270-338 ##label JOH2 !'##cross-references EMBL:M16229 GENETICS !$#map_position 5 !$#introns 22/3; 79/1; 107/1; 143/3; 185/3; 211/3; 245/1; 295/3 CLASSIFICATION #superfamily L-lactate dehydrogenase KEYWORDS homodimer; mitochondrion; NAD; oxidoreductase; tricarboxylic !1acid cycle FEATURE !$1-24 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$25-338 #product malate dehydrogenase, mitochondrial #status !8predicted #label MAT\ !$173,200 #active_site Asp, His #status predicted\ !$176 #binding_site substrate (Arg) #status predicted SUMMARY #length 338 #molecular-weight 35611 #checksum 5939 SEQUENCE /// ENTRY DEPUMW #type complete TITLE malate dehydrogenase (EC 1.1.1.37) precursor, mitochondrial - watermelon ORGANISM #formal_name Citrullus lanatus #common_name watermelon DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 11-Jun-1999 ACCESSIONS S10162; S31273; S11014 REFERENCE S10162 !$#authors Gietl, C.; Lehnerer, M.; Olsen, O. !$#journal Plant Mol. Biol. (1990) 14:1019-1030 !$#title Mitochondrial malate dehydrogenase from watermelon: sequence !1of cDNA clones and primary structure of the higher-plant !1precursor protein. !$#cross-references MUID:91346686; PMID:2102869 !$#accession S10162 !'##molecule_type mRNA !'##residues 1-347 ##label GIE1 !'##cross-references EMBL:X17362; NID:g18296; PIDN:CAA35239.1; !1PID:g18297 !'##note the authors translated the codon GAT for residue 121 as Asn !$#accession S31273 !'##molecule_type protein !'##residues 28-77;118-134;149-166;261-288 ##label GIE2 !'##note the source is designated as Citrullus vulgaris REFERENCE S10687 !$#authors Gietl, C.; Lottspeich, F.; Hock, B. !$#journal Planta (1986) 169:555-558 !$#title Sequence homologies between glyoxysomal and mitochondrial !1malate dehydrogenase. !$#accession S11014 !'##molecule_type protein !'##residues 28-55 ##label PLA !'##note the source is designated as Citrullus vulgaris CLASSIFICATION #superfamily L-lactate dehydrogenase KEYWORDS homodimer; mitochondrion; NAD; oxidoreductase; tricarboxylic !1acid cycle FEATURE !$1-27 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$28-347 #product malate dehydrogenase, mitochondrial #status !8experimental #label MAT\ !$183,210 #active_site Asp, His #status predicted\ !$186 #binding_site substrate (Arg) #status predicted SUMMARY #length 347 #molecular-weight 36200 #checksum 1052 SEQUENCE /// ENTRY DEPUGW #type complete TITLE malate dehydrogenase (EC 1.1.1.37) precursor, glyoxysomal - watermelon ORGANISM #formal_name Citrullus lanatus #common_name watermelon DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 11-Jun-1999 ACCESSIONS A35957; S10687 REFERENCE A35957 !$#authors Gietl, C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:5773-5777 !$#title Glyoxysomal malate dehydrogenase from watermelon is !1synthesized with an amino-terminal transit peptide. !$#cross-references MUID:90332664; PMID:2377615 !$#accession A35957 !'##molecule_type mRNA !'##residues 1-356 ##label GIE !'##cross-references GB:M33148; NID:g167283; PIDN:AAA33041.1; !1PID:g167284 REFERENCE S10687 !$#authors Gietl, C.; Lottspeich, F.; Hock, B. !$#journal Planta (1986) 169:555-558 !$#title Sequence homologies between glyoxysomal and mitochondrial !1malate dehydrogenase. !$#accession S10687 !'##molecule_type protein !'##residues 'S',38-65 ##label GI2 !'##note the source is designated as Citrullus vulgaris CLASSIFICATION #superfamily L-lactate dehydrogenase KEYWORDS glyoxysome; NAD; oxidoreductase FEATURE !$1-36 #domain transit peptide (glyoxysome) #status !8predicted #label TNP\ !$37-356 #product malate dehydrogenase, glyoxysomal #status !8experimental #label MAT\ !$193,220 #active_site Asp, His #status predicted\ !$196 #binding_site substrate (Arg) #status predicted SUMMARY #length 356 #molecular-weight 37636 #checksum 4567 SEQUENCE /// ENTRY DEECM #type complete TITLE malate dehydrogenase (EC 1.1.1.37) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1993 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS F65115; PC6019; A26525; S06393; S01479; A24927; S00190 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65115 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-312 ##label BLAT !'##cross-references GB:AE000403; GB:U00096; NID:g2367205; !1PIDN:AAC76268.1; PID:g1789632; UWGP:b3236 !'##experimental_source strain K-12, substrain MG1655 REFERENCE JC6051 !$#authors Bass, S.; Gu, Q.; Christen, A. !$#journal J. Bacteriol. (1996) 178:1154-1161 !$#title Multicopy suppressors of Prc mutant Escherichia coli include !1two HtrA (DegP) protease homologs (HhoAB), DksA, and a !1truncated RlpA. !$#cross-references MUID:96165273; PMID:8576052 !$#accession PC6019 !'##molecule_type DNA !'##residues 302-312 ##label BAS !'##cross-references GB:U15661 REFERENCE A26525 !$#authors McAlister-Henn, L.; Blaber, M.; Bradshaw, R.A.; Nisco, S.J. !$#journal Nucleic Acids Res. (1987) 15:4993 !$#title Complete nucleotide sequence of the Escherichia coli gene !1encoding malate dehydrogenase. !$#cross-references MUID:87259981; PMID:3299262 !$#accession A26525 !'##molecule_type DNA !'##residues 1-79,'R',81-143,'L',145-306,'Q',308-312 ##label MCA !'##cross-references EMBL:Y00129; NID:g41988; PIDN:CAA68326.1; !1PID:g41989 !'##note the authors translated the codon TTG for residue 144 as Phe REFERENCE S06393 !$#authors Vogel, R.F.; Entian, K.D.; Mecke, D. !$#journal Arch. Microbiol. (1987) 149:36-42 !$#title Cloning and sequence of the mdh structural gene of !1Escherichia coli coding for malate dehydrogenase. !$#cross-references MUID:88105815; PMID:3322223 !$#accession S06393 !'##molecule_type DNA !'##residues 1-69,'R',71-79,'R',81-115,'N',117-304,'WAKSSLISN' ##label !1VOG !'##cross-references EMBL:M24777; NID:g341248; PIDN:AAA16107.1; !1PID:g450385 REFERENCE S01479 !$#authors Fernley, R.T.; Lentz, S.R.; Bradshaw, R.A. !$#journal Biosci. Rep. (1981) 1:497-507 !$#title Malate dehydrogenase: isolation from E. coli and comparison !1with the eukaryotic mitochondrial and cytoplasmic forms. !$#cross-references MUID:82047078; PMID:7028159 !$#accession S01479 !'##molecule_type protein !'##residues 1-36 ##label FER REFERENCE A24927 !$#authors Sutherland, P.; McAlister-Henn, L. !$#journal J. Bacteriol. (1985) 163:1074-1079 !$#title Isolation and expression of the Escherichia coli gene !1encoding malate dehydrogenase. !$#cross-references MUID:85288979; PMID:2993232 !$#accession A24927 !'##molecule_type DNA !'##residues 1-36,'S',38-40 ##label SUT !'##cross-references EMBL:M10417; NID:g146798; PIDN:AAA24147.1; !1PID:g146799 GENETICS !$#gene mdh !$#map_position 70 min CLASSIFICATION #superfamily L-lactate dehydrogenase KEYWORDS homodimer; NAD; oxidoreductase; tricarboxylic acid cycle FEATURE !$1-312 #product malate dehydrogenase #status experimental !8#label MAT\ !$83-90 #region NAD binding #status predicted\ !$150,177 #active_site Asp, His #status predicted\ !$153 #binding_site substrate (Arg) #status predicted SUMMARY #length 312 #molecular-weight 32337 #checksum 6018 SEQUENCE /// ENTRY DEEBM #type complete TITLE malate dehydrogenase (EC 1.1.1.37) - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 11-Jun-1999 ACCESSIONS S16143; JN0504 REFERENCE S16143 !$#authors Lu, C.D.; Abdelal, A.T. !$#submission submitted to the EMBL Data Library, July 1991 !$#description Complete nucleotide sequence of Salmonella typhimurium gene !1encoding malate dehydrogenase. !$#accession S16143 !'##molecule_type DNA !'##residues 1-312 ##label LUC !'##cross-references EMBL:X61029; NID:g47776; PIDN:CAA43363.1; !1PID:g47777 REFERENCE JN0504 !$#authors Lu, C.D.; Abdelal, A.T. !$#journal Gene (1993) 123:143-144 !$#title Complete sequence of the Salmonella typhimurium gene !1encoding malate dehydrogenase. !$#cross-references MUID:93138424; PMID:8422999 !$#accession JN0504 !'##molecule_type DNA !'##residues 1-312 ##label LU2 !'##cross-references GB:M95049; NID:g154165; PIDN:AAA27158.1; !1PID:g154166 GENETICS !$#gene mdh CLASSIFICATION #superfamily L-lactate dehydrogenase KEYWORDS homodimer; NAD; oxidoreductase; tricarboxylic acid cycle FEATURE !$83-90 #region NAD binding #status predicted\ !$150,177 #active_site Asp, His #status predicted\ !$153 #binding_site substrate (Arg) #status predicted SUMMARY #length 312 #molecular-weight 32451 #checksum 5474 SEQUENCE /// ENTRY DEBYMM #type complete TITLE malate dehydrogenase (EC 1.1.1.37) precursor, mitochondrial - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YKL085w ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 21-Jul-2000 ACCESSIONS A31945; B31945; S37910; S05771; S05769 REFERENCE A31945 !$#authors Thompson, L.M.; Sutherland, P.; Steffan, J.S.; !1McAlister-Henn, L. !$#journal Biochemistry (1988) 27:8393-8400 !$#title Gene sequence and primary structure of mitochondrial malate !1dehydrogenase from Saccharomyces cerevisiae. !$#cross-references MUID:89207449; PMID:3072021 !$#accession A31945 !'##molecule_type DNA !'##residues 1-334 ##label THO !'##cross-references GB:J02841; NID:g171891; PIDN:AAA34759.1; !1PID:g171892 !$#accession B31945 !'##molecule_type protein !'##residues 18-33 ##label THO2 REFERENCE S37897 !$#authors Pohl, T.M.; Pohl, F.M. !$#submission submitted to the Protein Sequence Database, March 1994 !$#accession S37910 !'##molecule_type DNA !'##residues 1-334 ##label POH !'##cross-references EMBL:Z28085; NID:g486124; PIDN:CAA81923.1; !1PID:g486125; GSPDB:GN00011; MIPS:YKL085w !'##experimental_source strain S288C REFERENCE S05770 !$#authors Kopetzki, E.; Entian, K.D.; Lottspeich, F.; Mecke, D. !$#journal Biochim. Biophys. Acta (1987) 912:398-403 !$#title Purification procedure and N-terminal amino acid sequence of !1yeast malate dehydrogenase isoenzymes. !$#cross-references MUID:87185517; PMID:3552052 !$#accession S05771 !'##molecule_type protein !'##residues 18-67,'G',69-73 ##label KOP GENETICS !$#gene SGD:MDH1; MIPS:YKL085w !'##cross-references SGD:S0001568; MIPS:YKL085w !$#map_position 11L !$#genome nuclear CLASSIFICATION #superfamily L-lactate dehydrogenase KEYWORDS homodimer; mitochondrion; NAD; oxidoreductase; tricarboxylic !1acid cycle FEATURE !$1-17 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$18-334 #product malate dehydrogenase, mitochondrial #status !8experimental #label MAT\ !$168,195 #active_site Asp, His #status predicted\ !$171 #binding_site substrate (Arg) #status predicted SUMMARY #length 334 #molecular-weight 35650 #checksum 8901 SEQUENCE /// ENTRY DEBYMC #type complete TITLE malate dehydrogenase (EC 1.1.1.37), cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein AOE423; protein O0537; protein YOL126c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1993 #sequence_revision 19-Jul-1996 #text_change 16-Jun-2000 ACCESSIONS S63444; S12937; A34986; S05770; S66823; S71982 REFERENCE S63440 !$#authors Casamayor, A.; Khalid, H.; Balcells, L.; Aldea, M.; Casas, !1C.; Herrero, E.; Arino, J. !$#submission submitted to the EMBL Data Library, November 1995 !$#description Sequencing of a 13.4 kbp fragment of the left arm of !1chromosome XV reveals a putative ser/thr protein kinase !1gene, the malate dehydrogenase MDH2 gene, a ribosomal L25 !1gene. !$#accession S63444 !'##molecule_type DNA !'##residues 1-423 ##label CAS !'##cross-references EMBL:U41293; NID:g1209710; PIDN:AAC49466.1; !1PID:g1209715 !'##experimental_source strain FY1679 REFERENCE S12937 !$#authors Minard, K.I.; McAlister-Henn, L. !$#journal Mol. Cell. Biol. (1991) 11:370-380 !$#title Isolation, nucleotide sequence analysis, and disruption of !1the MDH2 gene from Saccharomyces cerevisiae: evidence for !1three isozymes of yeast malate dehydrogenase. !$#cross-references MUID:91094852; PMID:1986231 !$#accession S12937 !'##molecule_type DNA !'##residues 47-423 ##label MIN1 !'##cross-references EMBL:M62808; NID:g171915; PIDN:AAA34766.1; !1PID:g171916 !$#accession A34986 !'##molecule_type protein !'##residues 48-73 ##label MIN2 REFERENCE S05770 !$#authors Kopetzki, E.; Entian, K.D.; Lottspeich, F.; Mecke, D. !$#journal Biochim. Biophys. Acta (1987) 912:398-403 !$#title Purification procedure and N-terminal amino acid sequence of !1yeast malate dehydrogenase isoenzymes. !$#cross-references MUID:87185517; PMID:3552052 !$#accession S05770 !'##molecule_type protein !'##residues 48-73,'P',75-81 ##label KOP REFERENCE S66814 !$#authors Arino, J.; Casamayor, A.; Gamo, F.J.; Gancedo, C.; Lafuente, !1M.J.; Aldea, M.; Casas, C.; Herrero, E. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S66823 !'##molecule_type DNA !'##residues 1-423 ##label ARI !'##cross-references EMBL:Z74868; NID:g1420008; PIDN:CAA99145.1; !1PID:g1420009; GSPDB:GN00015; MIPS:YOL126c !'##experimental_source strain S288C REFERENCE S71978 !$#authors Casamayor, A.; Khalid, H.; Balcells, L.; Aldea, M.; Casas, !1C.; Herrero, E.; Arino, J. !$#journal Yeast (1996) 12:1013-1020 !$#title Sequence analysis of a 13.4 kbp fragment from the left arm !1of chromosome XV reveals a malate dehydrogenase gene, a !1putative Ser/Thr protein kinase, the ribosomal L25 gene and !1four new open reading frames. !$#cross-references MUID:97051588; PMID:8896265 !$#accession S71982 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-423 ##label CAW !'##cross-references EMBL:U41293; NID:g1209710; PIDN:AAC49466.1; !1PID:g1209715 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1995 GENETICS !$#gene SGD:MDH2; MIPS:YOL126c !'##cross-references SGD:S0005486; MIPS:YOL126c !$#map_position 15L CLASSIFICATION #superfamily L-lactate dehydrogenase KEYWORDS cytosol; homodimer; NAD; oxidoreductase FEATURE !$48-423 #product malate dehydrogenase #status experimental !8#label MAT\ !$228,261 #active_site Asp, His #status predicted\ !$231 #binding_site substrate (Arg) #status predicted SUMMARY #length 423 #molecular-weight 46170 #checksum 6679 SEQUENCE /// ENTRY DEBYMP #type complete TITLE malate dehydrogenase (EC 1.1.1.37), peroxisomal - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein D2468; protein YDL078c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1993 #sequence_revision 23-Aug-1996 #text_change 21-Jul-2000 ACCESSIONS S67614; S31255; S31465 REFERENCE S67608 !$#authors Wambutt, R.; Wedler, H.; Wedler, E.; Scharfe, M. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67614 !'##molecule_type DNA !'##residues 1-343 ##label WAM !'##cross-references EMBL:Z74126; NID:g1431095; PIDN:CAA98644.1; !1PID:g1431096; GSPDB:GN00004; MIPS:YDL078c !'##experimental_source strain S288C REFERENCE S31255 !$#authors Steffan, J.S.; McAlister-Henn, L. !$#journal J. Biol. Chem. (1992) 267:24708-24715 !$#title Isolation and characterization of the yeast gene encoding !1the MDH3 isozyme of malate dehydrogenase. !$#cross-references MUID:93077569; PMID:1447211 !$#accession S31255 !'##molecule_type DNA !'##residues 1-239,'R',241-343 ##label STE !'##cross-references EMBL:M98763; NID:g171917; PIDN:AAA34767.1; !1PID:g171918 !$#accession S31465 !'##molecule_type protein !'##residues 2-16;23-36;153-167 ##label ST2 GENETICS !$#gene SGD:MDH3; MIPS:YDL078c !'##cross-references SGD:S0002236; MIPS:YDL078c !$#map_position 4L CLASSIFICATION #superfamily L-lactate dehydrogenase KEYWORDS homodimer; NAD; oxidoreductase; peroxisome FEATURE !$2-343 #product malate dehydrogenase, peroxisomal #status !8experimental #label MAT\ !$341-343 #region peroxisome/glyoxysome location signal !8(S-[RKH]-L) motif\ !$149,187 #active_site Asp, His #status predicted\ !$152 #binding_site substrate (Arg) #status predicted SUMMARY #length 343 #molecular-weight 37186 #checksum 5039 SEQUENCE /// ENTRY DEMSMC #type complete TITLE malate dehydrogenase (EC 1.1.1.37), cytosolic - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 11-Jun-1999 ACCESSIONS S02654; S00195 REFERENCE S02654 !$#authors Setoyama, C.; Joh, T.; Tsuzuki, T.; Shimada, K. !$#journal J. Mol. Biol. (1988) 202:355-364 !$#title Structural organization of the mouse cytosolic malate !1dehydrogenase gene: comparison with that of the mouse !1mitochondrial malate dehydrogenase gene. !$#cross-references MUID:89011964; PMID:3172222 !$#accession S02654 !'##molecule_type DNA !'##residues 1-334 ##label SET !'##cross-references EMBL:M36083 REFERENCE S00192 !$#authors Joh, T.; Takeshima, H.; Tsuzuki, T.; Setoyama, C.; Shimada, !1K.; Tanase, S.; Kuramitsu, S.; Kagamiyama, H.; Morino, Y. !$#journal J. Biol. Chem. (1987) 262:15127-15131 !$#title Cloning and sequence analysis of cDNAs encoding mammalian !1cytosolic malate dehydrogenase. !$#cross-references MUID:88033094; PMID:3312200 !$#accession S00195 !'##molecule_type mRNA !'##residues 1-334 ##label JOH !'##cross-references EMBL:M29462; NID:g199094; PIDN:AAA39510.1; !1PID:g387423 GENETICS !$#introns 1/3; 34/3; 67/1; 125/3; 166/3; 225/3; 263/3; 293/3 CLASSIFICATION #superfamily L-lactate dehydrogenase KEYWORDS homodimer; NAD; oxidoreductase FEATURE !$159,187 #active_site Asp, His #status predicted\ !$162 #binding_site substrate (Arg) #status predicted SUMMARY #length 334 #molecular-weight 36477 #checksum 9845 SEQUENCE /// ENTRY A32472 #type complete TITLE malate dehydrogenase (EC 1.1.1.37), cytosolic - pig ALTERNATE_NAMES malic dehydrogenase ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 30-Jun-1992 #sequence_revision 01-Dec-2000 #text_change 08-Dec-2000 ACCESSIONS JC4876; A32472; S00192; S31276; S28987 REFERENCE JC4876 !$#authors Trejo, F.; Costa, M.; Gelpi, J.L.; Busquets, M.; Clarke, !1A.R.; Holbrook, J.J.; Cortes, A. !$#journal Gene (1996) 172:303-308 !$#title Cloning, sequencing and functional expression of a DNA !1encoding pig cytosolic malate dehydrogenase: Purification !1and characterization of the recombinant enzyme. !$#cross-references MUID:96269423; PMID:8682322 !$#accession JC4876 !'##molecule_type DNA !'##residues 1-334 ##label TRE !'##cross-references GB:U44846; NID:g1469401; PIDN:AAC48610.1; !1PID:g1469402 !'##experimental_source heart REFERENCE A32472 !$#authors Birktoft, J.J.; Rhodes, G.; Banaszak, L.J. !$#journal Biochemistry (1989) 28:6065-6081 !$#title Refined crystal structure of cytoplasmic malate !1dehydrogenase at 2.5-angstroms resolution. !$#cross-references MUID:89375338; PMID:2775751 !$#accession A32472 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 2-334 ##label BIR REFERENCE S00192 !$#authors Joh, T.; Takeshima, H.; Tsuzuki, T.; Setoyama, C.; Shimada, !1K.; Tanase, S.; Kuramitsu, S.; Kagamiyama, H.; Morino, Y. !$#journal J. Biol. Chem. (1987) 262:15127-15131 !$#title Cloning and sequence analysis of cDNAs encoding mammalian !1cytosolic malate dehydrogenase. !$#cross-references MUID:88033094; PMID:3312200 !$#accession S00192 !'##molecule_type mRNA !'##residues 46-237,'Q',239-334 ##label JOH1 !'##cross-references EMBL:M29463; NID:g164542; PIDN:AAA31072.1; !1PID:g164543 !'##note the authors translated the codon CAG for residue 194 as Arg !$#accession S31276 !'##molecule_type protein !'##residues 97-136;270-312 ##label JOH2 CLASSIFICATION #superfamily L-lactate dehydrogenase KEYWORDS acetylated amino end; blocked amino end; cytosol; homodimer; !1NAD; oxidoreductase FEATURE !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental\ !$159,187 #active_site Asp, His #status predicted\ !$162 #binding_site substrate (Arg) #status predicted SUMMARY #length 334 #molecular-weight 36454 #checksum 5879 SEQUENCE /// ENTRY DETWMA #type complete TITLE malate dehydrogenase (EC 1.1.1.37) - Thermus aquaticus ORGANISM #formal_name Thermus aquaticus DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 11-Jun-1999 ACCESSIONS A26065; S31275; S15952; S12139; S00191 REFERENCE A26065 !$#authors Nishiyama, M.; Matsubara, N.; Yamamoto, K.; Iijima, S.; !1Uozumi, T.; Beppu, T. !$#journal J. Biol. Chem. (1986) 261:14178-14183 !$#title Nucleotide sequence of the malate dehydrogenase gene of !1Thermus flavus and its mutation directing an increase in !1enzyme activity. !$#cross-references MUID:87033605; PMID:3771528 !$#accession A26065 !'##molecule_type DNA !'##residues 1-327 ##label NIS1 !'##cross-references EMBL:J02598; NID:g155112; PIDN:AAA27499.1; !1PID:g295401 !$#accession S31275 !'##molecule_type protein !'##residues 1-37;265-284 ##label NIS2 !'##experimental_source strain AT-62 !'##note the sequence from Fig. 7 is inconsistent with that from Fig. 3 !1in having 75-Asp !'##note the source is designated as Thermus flavus REFERENCE S15948 !$#authors Nishiyama, M.; Horinouchi, S.; Beppu, T. !$#journal Mol. Gen. Genet. (1991) 226:1-9 !$#title Characterization of an operon encoding succinyl-CoA !1synthetase and malate dehydrogenase from Thermus flavus !1AT-62 and its expression in Escherichia coli. !$#cross-references MUID:91238680; PMID:2034208 !$#accession S15952 !'##molecule_type DNA !'##residues 1-327 ##label NIS !'##cross-references EMBL:X54073; NID:g48174; PIDN:CAA38008.1; !1PID:g48179 !'##experimental_source strain B !'##note the source is designated as Thermus flavus REFERENCE S12137 !$#authors Nicholls, D.J.; Sundaram, T.K.; Atkinson, T.; Minton, N.P. !$#journal FEMS Microbiol. Lett. (1990) 70:7-14 !$#title Cloning and nucleotide sequences of the mdh and sucD genes !1from Thermus aquaticus B. !$#accession S12139 !'##molecule_type DNA !'##residues 1-327 ##label NIC !'##cross-references EMBL:X56033; NID:g48077; PIDN:CAA39508.1; !1PID:g581795 GENETICS !$#gene mdh !$#start_codon GTG CLASSIFICATION #superfamily L-lactate dehydrogenase KEYWORDS homodimer; NAD; oxidoreductase; tricarboxylic acid cycle FEATURE !$1-327 #product malate dehydrogenase #status experimental !8#label MAT\ !$159,187 #active_site Asp, His #status predicted\ !$162 #binding_site substrate (Arg) #status predicted SUMMARY #length 327 #molecular-weight 35426 #checksum 2373 SEQUENCE /// ENTRY DEMZMC #type complete TITLE malate dehydrogenase (NADP) (EC 1.1.1.82) precursor, chloroplast - maize ALTERNATE_NAMES NADP-malate dehydrogenase ORGANISM #formal_name Zea mays #common_name maize DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 03-Jun-2002 ACCESSIONS S04859; A31071; S32512 REFERENCE S04859 !$#authors Metzler, M.C.; Rothermel, B.A.; Nelson, T. !$#journal Plant Mol. Biol. (1989) 12:713-722 !$#title Maize NADP-malate dehydrogenase: cDNA cloning, sequence, and !1mRNA characterization. !$#accession S04859 !'##molecule_type mRNA !'##residues 1-432 ##label MET !'##cross-references EMBL:X16084; NID:g22367; PIDN:CAA34213.1; !1PID:g22368 REFERENCE A31071 !$#authors Decottignies, P.; Schmitter, J.M.; Miginiac-Maslow, M.; Le !1Marechal, P.; Jacquot, J.P.; Gadal, P. !$#journal J. Biol. Chem. (1988) 263:11780-11785 !$#title Primary structure of the light-dependent regulatory site of !1corn NADP-malate dehydrogenase. !$#cross-references MUID:88298851; PMID:3403553 !$#accession A31071 !'##molecule_type protein !'##residues 58-84 ##label DEC REFERENCE S32512 !$#authors Ocheretina, O.; Harnecker, J.; Rother, T.; Schmid, R.; !1Scheibe, R. !$#journal Biochim. Biophys. Acta (1993) 1163:10-16 !$#title Effects of N-terminal truncations upon chloroplast !1NADP-malate dehydrogenases from pea and spinach. !$#cross-references MUID:93237315; PMID:8476924 !$#accession S32512 !'##molecule_type protein !'##residues 41-49 ##label OCH GENETICS !$#genome nuclear CLASSIFICATION #superfamily L-lactate dehydrogenase KEYWORDS chloroplast; NADP; oxidoreductase; redox-active disulfide FEATURE !$1-57 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$58-432 #product malate dehydrogenase, chloroplast #status !8experimental #label MAT\ !$67-72 #disulfide_bonds redox-active #status experimental\ !$244,272 #active_site Asp, His #status predicted\ !$247 #binding_site substrate (Arg) #status predicted\ !$408-420 #disulfide_bonds #status predicted SUMMARY #length 432 #molecular-weight 46859 #checksum 3076 SEQUENCE /// ENTRY C42902 #type complete TITLE 3-hydroxyisobutyrate dehydrogenase (EC 1.1.1.31) - Pseudomonas aeruginosa ORGANISM #formal_name Pseudomonas aeruginosa DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 31-Dec-2000 ACCESSIONS C42902; D83198; S27603 REFERENCE A42902 !$#authors Steele, M.I.; Lorenz, D.; Hatter, K.; Park, A.; Sokatch, !1J.R. !$#journal J. Biol. Chem. (1992) 267:13585-13592 !$#title Characterization of the mmsAB operon of Pseudomonas !1aeruginosa PAO encoding methylmalonate-semialdehyde !1dehydrogenase and 3-hydroxyisobutyrate dehydrogenase. !$#cross-references MUID:92317087; PMID:1339433 !$#accession C42902 !'##status preliminary !'##molecule_type DNA !'##residues 1-298 ##label STE !'##cross-references EMBL:M84911; NID:g151360; PIDN:AAA25892.1; !1PID:g151363 !'##experimental_source PAO, ATCC 15692 !'##note sequence extracted from NCBI backbone (NCBIN:107704, !1NCBIP:107708) REFERENCE A82950 !$#authors Stover, C.K.; Pham, X.Q.; Erwin, A.L.; Mizoguchi, S.D.; !1Warrener, P.; Hickey, M.J.; Brinkman, F.S.L.; Hufnagle, !1W.O.; Kowalik, D.J.; Lagrou, M.; Garber, R.L.; Goltry, L.; !1Tolentino, E.; Westbrook-Wadman, S.; Yuan, Y.; Brody, L.L.; !1Coulter, S.N.; Folger, K.R.; Kas, A.; Larbig, K.; Lim, R.M.; !1Smith, K.A.; Spencer, D.H.; Wong, G.K.S.; Wu, Z.; Paulsen, !1I.T.; Reizer, J.; Saier, M.H.; Hancock, R.E.W.; Lory, S.; !1Olson, M.V. !$#journal Nature (2000) 406:959-964 !$#title Complete genome sequence of Pseudomonas aeruginosa PA01, an !1opportunistic pathogen. !$#cross-references MUID:20437337; PMID:10984043 !$#accession D83198 !'##status preliminary !'##molecule_type DNA !'##residues 1-298 ##label STO !'##cross-references GB:AE004778; GB:AE004091; NID:g9949722; !1PIDN:AAG06957.1; GSPDB:GN00131; PASP:PA3569 !'##experimental_source strain PAO1 GENETICS !$#gene mmsB; PA3569 CLASSIFICATION #superfamily 3-hydroxyisobutyrate dehydrogenase; !13-hydroxyisobutyrate dehydrogenase homology KEYWORDS oxidoreductase FEATURE !$4-272 #domain 3-hydroxyisobutyrate dehydrogenase homology !8#label HIB SUMMARY #length 298 #molecular-weight 30486 #checksum 1712 SEQUENCE /// ENTRY JQ0613 #type complete TITLE 3-hydroxyisobutyrate dehydrogenase (EC 1.1.1.31) homolog - Escherichia coli (strain K-12) ALTERNATE_NAMES hypothetical 31K protein (rnpB-sohA intergenic region) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS JQ0613; A65102 REFERENCE JQ0612 !$#authors Komine, Y.; Inokuchi, H. !$#submission submitted to JIPID, September 1990 !$#accession JQ0613 !'##molecule_type DNA !'##residues 1-299 ##label KOM !'##experimental_source strain K12, W3110 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65102 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-299 ##label BLAT !'##cross-references GB:AE000394; GB:U00096; NID:g2367197; !1PIDN:AAC76159.1; PID:g1789513; UWGP:b3125 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yhaE !$#map_position 68 min CLASSIFICATION #superfamily 3-hydroxyisobutyrate dehydrogenase; !13-hydroxyisobutyrate dehydrogenase homology KEYWORDS oxidoreductase FEATURE !$8-269 #domain 3-hydroxyisobutyrate dehydrogenase homology !8#label HIB SUMMARY #length 299 #molecular-weight 31019 #checksum 4591 SEQUENCE /// ENTRY RDHUE #type complete TITLE hydroxymethylglutaryl-CoA reductase (NADPH2) (EC 1.1.1.34) - human ORGANISM #formal_name Homo sapiens #common_name man DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 04-Nov-2002 ACCESSIONS A00356 REFERENCE A00356 !$#authors Luskey, K.L.; Stevens, B. !$#journal J. Biol. Chem. (1985) 260:10271-10277 !$#title Human 3-hydroxy-3-methylglutaryl coenzyme A reductase. !1Conserved domains responsible for catalytic activity and !1sterol-regulated degradation. !$#cross-references MUID:85261451; PMID:2991281 !$#accession A00356 !'##molecule_type mRNA !'##residues 1-888 ##label LUS !'##cross-references GB:M11058; NID:g184243; PIDN:AAA52679.1; !1PID:g306865 COMMENT This transmembrane glycoprotein of the endoplasmic reticulum !1is involved in the control of cholesterol biosynthesis. GENETICS !$#gene GDB:HMGCR !'##cross-references GDB:119312; OMIM:142910 !$#map_position 5q13.3-5q14 CLASSIFICATION #superfamily human hydroxymethylglutaryl-CoA reductase !1(NADPH2) KEYWORDS cholesterol biosynthesis; coenzyme A; endoplasmic reticulum; !1glycoprotein; membrane protein; oxidoreductase FEATURE !$1-339 #domain membrane-bound #label MBD\ !$340-449 #domain linker #label LKR\ !$450-888 #domain catalytic #label CAT\ !$281,518,870 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 888 #molecular-weight 97475 #checksum 2950 SEQUENCE /// ENTRY RDHYE #type complete TITLE hydroxymethylglutaryl-CoA reductase (NADPH2) (EC 1.1.1.34) - Chinese hamster ORGANISM #formal_name Cricetulus griseus #common_name Chinese hamster DATE 15-Nov-1984 #sequence_revision 15-Nov-1984 #text_change 04-Nov-2002 ACCESSIONS A93328; A00357 REFERENCE A93328 !$#authors Chin, D.J.; Gil, G.; Russell, D.W.; Liscum, L.; Luskey, !1K.L.; Basu, S.K.; Okayama, H.; Berg, P.; Goldstein, J.L.; !1Brown, M.S. !$#journal Nature (1984) 308:613-617 !$#title Nucleotide sequence of 3-hydroxy-3-methyl-glutaryl coenzyme !1a reductase, a glycoprotein of endoplasmic reticulum. !$#cross-references MUID:84168178; PMID:6546784 !$#accession A93328 !'##molecule_type mRNA !'##residues 1-887 ##label CHI !'##cross-references GB:L00183; GB:X00494; NID:g191109; PIDN:AAA36989.1; !1PID:g387052 !'##note 673-Cys was also found REFERENCE A90852 !$#authors Reynolds, G.A.; Basu, S.K.; Osborne, T.F.; Chin, D.J.; Gil, !1G.; Brown, M.S.; Goldstein, J.L.; Luskey, K.L. !$#journal Cell (1984) 38:275-285 !$#title HMG CoA reductase: a negatively regulated gene with unusual !1promoter and 5' untranslated regions. !$#cross-references MUID:84282711; PMID:6088070 !$#contents annotation; introns REFERENCE A92521 !$#authors Liscum, L.; Finer-Moore, J.; Stroud, R.M.; Luskey, K.L.; !1Brown, M.S.; Goldstein, J.L. !$#journal J. Biol. Chem. (1985) 260:522-530 !$#title Domain structure of 3-hydroxy-3-methylglutaryl coenzyme a !1reductase, a glycoprotein of the endoplasmic reticulum. !$#cross-references MUID:85080129; PMID:3965461 !$#contents annotation; domains COMMENT This transmembrane glycoprotein of the endoplasmic reticulum !1is an enzyme of cholesterol biosynthesis. An enzymatically !1active 62K fragment can be released from the membrane by !1cleavage (between residues 368-380) by an endogenous !1protease; this fragment can be further cleaved (between !1residues 450-470) by exogenous protease, producing a 53K !1fragment, which retains full enzymatic activity. GENETICS !$#introns 55/3; 93/1; 122/2; 150/3; 186/1; 221/3; 260/1; 314/2; 397/1; !1455/3; 520/3; 573/3; 626/2; 661/3; 718/3; 765/3; 818/3; 870/ !12 CLASSIFICATION #superfamily human hydroxymethylglutaryl-CoA reductase !1(NADPH2) KEYWORDS cholesterol biosynthesis; coenzyme A; endoplasmic reticulum; !1glycoprotein; oxidoreductase; transmembrane protein FEATURE !$1-339 #domain membrane-bound #label MBD\ !$10-39 #domain transmembrane #status predicted #label TM1\ !$57-78 #domain transmembrane #status predicted #label TM2\ !$90-114 #domain transmembrane #status predicted #label TM3\ !$124-149 #domain transmembrane #status predicted #label TM4\ !$160-187 #domain transmembrane #status predicted #label TM5\ !$192-220 #domain transmembrane #status predicted #label TM6\ !$315-339 #domain transmembrane #status predicted #label TM7\ !$340-887 #domain catalytic hydrophilic #label HYL\ !$281 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 887 #molecular-weight 97080 #checksum 872 SEQUENCE /// ENTRY A23586 #type complete TITLE hydroxymethylglutaryl-CoA reductase (EC 1.1.1.88) - golden hamster ORGANISM #formal_name Mesocricetus auratus #common_name golden hamster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 04-Nov-2002 ACCESSIONS A23586 REFERENCE A23586 !$#authors Skalnik, D.G.; Simoni, R.D. !$#journal DNA (1985) 4:439-444 !$#title The nucleotide sequence of Syrian hamster HMG-CoA reductase !1cDNA. !$#cross-references MUID:86135263; PMID:3841506 !$#accession A23586 !'##molecule_type mRNA !'##residues 1-887 ##label SKA CLASSIFICATION #superfamily human hydroxymethylglutaryl-CoA reductase !1(NADPH2) KEYWORDS coenzyme A; oxidoreductase; transmembrane protein SUMMARY #length 887 #molecular-weight 96970 #checksum 74 SEQUENCE /// ENTRY A35728 #type complete TITLE hydroxymethylglutaryl-CoA reductase (NADPH2) (EC 1.1.1.34) - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 04-Nov-2002 ACCESSIONS A35728 REFERENCE A35728 !$#authors Chen, H.; Shapiro, D.J. !$#journal J. Biol. Chem. (1990) 265:4622-4629 !$#title Nucleotide sequence and estrogen induction of Xenopus laevis !13-hydroxy-3-methylglutaryl-coenzyme A reductase. !$#cross-references MUID:90170974; PMID:2307680 !$#accession A35728 !'##status preliminary !'##molecule_type mRNA !'##residues 1-883 ##label CHE !'##cross-references GB:M29258; NID:g214236; PIDN:AAA49740.1; !1PID:g214237 CLASSIFICATION #superfamily human hydroxymethylglutaryl-CoA reductase !1(NADPH2) KEYWORDS coenzyme A; NADP; oxidoreductase; transmembrane protein SUMMARY #length 883 #molecular-weight 96719 #checksum 6785 SEQUENCE /// ENTRY A31898 #type complete TITLE hydroxymethylglutaryl-CoA reductase (NADPH2) (EC 1.1.1.34) - sea urchin (Strongylocentrotus purpuratus) ORGANISM #formal_name Strongylocentrotus purpuratus #common_name purple urchin DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 04-Nov-2002 ACCESSIONS A31898; A28367 REFERENCE A31898 !$#authors Woodward, H.D.; Allen, J.M.C.; Lennarz, W.J. !$#journal J. Biol. Chem. (1988) 263:18411-18418 !$#title 3-hydroxy-3-methylglutaryl-coenzyme A reductase of the sea !1urchin embryo. Deduced structure and regulatory properties. !$#cross-references MUID:89054023; PMID:3192541 !$#accession A31898 !'##molecule_type mRNA !'##residues 1-932 ##label WOO !'##cross-references GB:J04200; NID:g161522; PIDN:AAA30060.1; !1PID:g161523 !'##note the authors rearranged portions of the coding region in Figure !12, and the above sequence is taken directly from Figure 3; !1it matches the translation of the nucleotide sequence that !1the author submitted to GenBank !'##note the authors translated the codon GGA for residue 805 as Glu REFERENCE A28367 !$#authors Woodward, H.D.; Allen, J.M.C.; Lennarz, W.J. !$#journal J. Biol. Chem. (1988) 263:2513-2517 !$#title 3-hydroxy-3-methylglutaryl coenzyme A reductase in the sea !1urchin embryo is developmentally regulated. !$#cross-references MUID:88115403; PMID:3276692 !$#accession A28367 !'##molecule_type mRNA !'##residues 689-735 ##label WO2 COMMENT This transmembrane glycoprotein of the endoplasmic reticulum !1is involved in the control of cholesterol biosynthesis. CLASSIFICATION #superfamily human hydroxymethylglutaryl-CoA reductase !1(NADPH2) KEYWORDS cholesterol biosynthesis; coenzyme A; endoplasmic reticulum; !1glycoprotein; NADP; oxidoreductase FEATURE !$279,850,886,930 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 932 #molecular-weight 100965 #checksum 3584 SEQUENCE /// ENTRY S32572 #type complete TITLE hydroxymethylglutaryl-CoA reductase (NADPH2) (EC 1.1.1.34) - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 04-Nov-2002 ACCESSIONS S32572 REFERENCE S32572 !$#authors Gertler, F.B.; Chiu, C.Y.; Richter-Mann, L.; Chin, D.J. !$#journal Mol. Cell. Biol. (1988) 8:2713-2721 !$#title Developmental and metabolic regulation of the Drosophila !1melanogaster 3-hydroxy-3-methylglutaryl coenzyme A !1reductase. !$#cross-references MUID:88302188; PMID:3136321 !$#accession S32572 !'##molecule_type DNA !'##residues 1-916 ##label GER !'##cross-references EMBL:M21329; NID:g157623; PIDN:AAA28608.1; !1PID:g157624 GENETICS !$#gene FlyBase:HmG-CoAR !'##cross-references FlyBase:FBgn0001205 CLASSIFICATION #superfamily human hydroxymethylglutaryl-CoA reductase !1(NADPH2) KEYWORDS coenzyme A; NADP; oxidoreductase; transmembrane protein SUMMARY #length 916 #molecular-weight 98295 #checksum 6674 SEQUENCE /// ENTRY S25316 #type complete TITLE hydroxymethylglutaryl-CoA reductase (NADPH2) (EC 1.1.1.34) - tomato ORGANISM #formal_name Lycopersicon esculentum #common_name tomato DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S25316 REFERENCE S25316 !$#authors Park, H.; Denbow, C.J.; Cramer, C.L. !$#journal Plant Mol. Biol. (1992) 20:327-331 !$#title Structure and nucleotide sequence of tomato HMG2 encoding !13-hydroxy-3-methyl-glutaryl coenzyme A reductase. !$#cross-references MUID:93004487; PMID:1391777 !$#accession S25316 !'##molecule_type DNA !'##residues 1-602 ##label PAR !'##cross-references EMBL:M63642; NID:g170451; PIDN:AAA34169.1; !1PID:g170452 GENETICS !$#gene HMG2 !$#introns 346/2; 407/1; 522/3 CLASSIFICATION #superfamily hydroxymethylglutaryl-CoA reductase (NADPH) KEYWORDS coenzyme A; isoprenoid biosynthesis; NADP; oxidoreductase SUMMARY #length 602 #molecular-weight 64714 #checksum 4306 SEQUENCE /// ENTRY A34416 #type complete TITLE hydroxymethylglutaryl-CoA reductase (NADPH2) (EC 1.1.1.34) - fluke (Schistosoma mansoni) ORGANISM #formal_name Schistosoma mansoni DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 03-Jun-2002 ACCESSIONS A34416 REFERENCE A34416 !$#authors Rajkovic, A.; Simonsen, J.N.; Davis, R.E.; Rottman, F.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:8217-8221 !$#title Molecular cloning and sequence analysis of !13-hydroxy-3-methylglutaryl-coenzyme A reductase from the !1human parasite Schistosoma mansoni. !$#cross-references MUID:90046767; PMID:2813388 !$#accession A34416 !'##molecule_type mRNA !'##residues 1-948 ##label RAJ !'##cross-references GB:M27294; NID:g161020; PIDN:AAA29896.1; !1PID:g161021 CLASSIFICATION #superfamily hydroxymethylglutaryl-CoA reductase (NADPH) KEYWORDS coenzyme A; NADP; oxidoreductase; transmembrane protein SUMMARY #length 948 #molecular-weight 107044 #checksum 2405 SEQUENCE /// ENTRY JC4879 #type complete TITLE 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35), short chain-specific, precursor - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Aug-1996 #sequence_revision 01-Nov-1996 #text_change 16-Jun-2000 ACCESSIONS JC4879 REFERENCE JC4879 !$#authors Vredendaal, P.J.C.M.; van den Berg, I.E.T.; Malingre, !1H.E.M.; Stroobants, A.K.; OldeWeghuis, D.E.M.; Berger, R. !$#journal Biochem. Biophys. Res. Commun. (1996) 223:718-723 !$#title Human short-chain L-3-hydroxyacyl-CoA dehydrogenase: Cloning !1and characterization of the coding sequence. !$#cross-references MUID:96268746; PMID:8687463 !$#accession JC4879 !'##molecule_type mRNA !'##residues 1-314 ##label VRE !'##cross-references EMBL:X96752; NID:g1483510; PIDN:CAA65528.1; !1PID:g1483511 !'##experimental_source liver COMMENT This enzyme plays a role in the mitochondrial beta-oxidation !1of short chain fatty acids. It catalyzes the reversible !1dehydrogenation of 3-hydroxyacyl-CoA's to their !1corresponding 3-ketoacyl-CoA's with concomitant reduction of !1NAD to NADH and exerts its highest activity towards !13-hydroxybutyryl-CoA. GENETICS !$#gene GDB:HADHSC; SCHAD !'##cross-references GDB:3846732; OMIM:601609 !$#map_position 4q22-4q26 CLASSIFICATION #superfamily 3-hydroxyacyl-CoA dehydrogenase; !13-hydroxyacyl-CoA dehydrogenase homology KEYWORDS fatty acid beta-oxidation; homodimer; mitochondrion; NAD; !1oxidoreductase FEATURE !$1-12 #domain transit peptide (mitochondrion) #status !8predicted #label TPP\ !$13-314 #product 3-hydroxyacyl-CoA dehydrogenase, short !8chain-specific #status predicted #label MAT\ !$27-314 #domain 3-hydroxyacyl-CoA dehydrogenase homology !8#label HCD\ !$29-57 #region beta-alpha-beta NAD nucleotide-binding fold SUMMARY #length 314 #molecular-weight 34286 #checksum 9578 SEQUENCE /// ENTRY DEPGC #type complete TITLE 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35), short chain-specific - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 02-Apr-1982 #sequence_revision 03-Aug-1984 #text_change 01-Nov-1996 ACCESSIONS A91280; A94605; A00358 REFERENCE A91280 !$#authors Bitar, K.G.; Perez-Aranda, A.; Bradshaw, R.A. !$#journal FEBS Lett. (1980) 116:196-198 !$#title Amino acid sequence of L-3-hydroxyacyl-CoA dehydrogenase !1from pig heart muscle. !$#cross-references MUID:81004379; PMID:7409145 !$#accession A91280 !'##molecule_type protein !'##residues 1-3,'A',5-8,'K',10-307 ##label BIT REFERENCE A94605 !$#authors Fang, J.K.; Bradshaw, R.A. !$#submission submitted to the Atlas, October 1982 !$#accession A94605 !'##molecule_type protein !'##residues 1-307 ##label FAN COMMENT This mitochondrial enzyme catalyzes the NAD-dependent !1oxidation of L(+)-3-hydroxyacyl CoA intermediates formed !1during the beta-oxidation of fatty acids. CLASSIFICATION #superfamily 3-hydroxyacyl-CoA dehydrogenase; !13-hydroxyacyl-CoA dehydrogenase homology KEYWORDS fatty acid beta-oxidation; homodimer; mitochondrion; NAD; !1oxidoreductase FEATURE !$15-307 #domain 3-hydroxyacyl-CoA dehydrogenase homology !8#label HCD\ !$17-45 #region beta-alpha-beta NAD nucleotide-binding fold SUMMARY #length 307 #molecular-weight 33280 #checksum 8806 SEQUENCE /// ENTRY JC4210 #type complete TITLE 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35), short chain-specific, precursor - mouse ALTERNATE_NAMES RAE-38 protein ORGANISM #formal_name Mus musculus #common_name house mouse DATE 04-Oct-1995 #sequence_revision 01-Nov-1996 #text_change 01-Nov-1996 ACCESSIONS JC4210 REFERENCE JC4210 !$#authors Nomura, M.; Takihara, Y.; Shimada, K. !$#journal Gene (1995) 160:309-310 !$#title Isolation of a cDNA clone encoding mouse 3-hydroxyacyl CoA !1dehydrogenase. !$#cross-references MUID:95369712; PMID:7642117 !$#accession JC4210 !'##molecule_type mRNA !'##residues 1-314 ##label NOM !'##cross-references DDBJ:D29639 !'##experimental_source embryonal carcinoma F9 cells COMMENT This enzyme plays a role in the mitochondrial beta-oxidation !1of short chain fatty acids. It catalyzes the reversible !1dehydrogenation of 3-hydroxyacyl-CoA's to their !1corresponding 3-ketoacyl-CoA's with concomitant reduction of !1NAD to NADH and exerts its highest activity towards !13-hydroxybutyryl-CoA. CLASSIFICATION #superfamily 3-hydroxyacyl-CoA dehydrogenase; !13-hydroxyacyl-CoA dehydrogenase homology KEYWORDS fatty acid beta-oxidation; homodimer; mitochondrion; NAD; !1oxidoreductase FEATURE !$1-12 #domain transit peptide (mitochondrion) #status !8predicted #label TPP\ !$13-314 #product 3-hydroxyacyl-CoA dehydrogenase, short !8chain-specific #status predicted #label MAT\ !$27-314 #domain 3-hydroxyacyl-CoA dehydrogenase homology !8#label HCD\ !$29-57 #region beta-alpha-beta NAD nucleotide-binding fold SUMMARY #length 314 #molecular-weight 34425 #checksum 315 SEQUENCE /// ENTRY S40743 #type complete TITLE 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35) short chain-specific form homolog - Caenorhabditis elegans ALTERNATE_NAMES hypothetical protein F54C8.1 ORGANISM #formal_name Caenorhabditis elegans DATE 06-Feb-1995 #sequence_revision 01-Nov-1996 #text_change 05-Sep-1997 ACCESSIONS S40743 REFERENCE S40473 !$#authors Berks, M.; Smith, A. !$#submission submitted to the EMBL Data Library, February 1992 !$#accession S40743 !'##molecule_type DNA !'##residues 1-298 ##label BER !'##cross-references EMBL:Z22178; NID:g297949; PID:g297950 GENETICS !$#introns 70/3; 225/3 CLASSIFICATION #superfamily 3-hydroxyacyl-CoA dehydrogenase; !13-hydroxyacyl-CoA dehydrogenase homology KEYWORDS fatty acid beta-oxidation; homodimer; NAD; oxidoreductase FEATURE !$11-297 #domain 3-hydroxyacyl-CoA dehydrogenase homology !8#label HCD\ !$13-41 #region beta-alpha-beta NAD nucleotide-binding fold SUMMARY #length 298 #molecular-weight 32492 #checksum 8831 SEQUENCE /// ENTRY A43723 #type complete TITLE beta-hydroxybutyryl-CoA dehydrogenase, NAD-dependent (EC 1.1.1.-) - Clostridium acetobutylicum ORGANISM #formal_name Clostridium acetobutylicum DATE 03-Mar-1993 #sequence_revision 01-Nov-1996 #text_change 11-Jun-1999 ACCESSIONS A43723; JU0054 REFERENCE A43723 !$#authors Youngleson, J.S.; Jones, D.T.; Woods, D.R. !$#journal J. Bacteriol. (1989) 171:6800-6807 !$#title Homology between hydroxybutyryl and hydroxyacyl coenzyme A !1dehydrogenase enzymes from Clostridium acetobutylicum !1fermentation and vertebrate fatty acid beta-oxidation !1pathways. !$#cross-references MUID:90078130; PMID:2687255 !$#accession A43723 !'##molecule_type DNA !'##residues 1-282 ##label YOU !'##cross-references GB:M31799; NID:g144732; PIDN:AAA23208.1; !1PID:g144733 REFERENCE A91610 !$#authors Youngleson, J.S.; Jones, W.A.; Jones, D.T.; Woods, D.R. !$#journal Gene (1989) 78:355-364 !$#title Molecular analysis and nucleotide sequence of the adh1 gene !1encoding an NADPH-dependent butanol dehydrogenase in the !1gram-positive anaerobe Clostridium acetobutylicum. !$#cross-references MUID:89378762; PMID:2673928 !$#accession JU0054 !'##status translation not shown !'##molecule_type DNA !'##residues 231-282 ##label YO2 GENETICS !$#gene hbd CLASSIFICATION #superfamily 3-hydroxyacyl-CoA dehydrogenase; !13-hydroxyacyl-CoA dehydrogenase homology KEYWORDS NAD; oxidoreductase FEATURE !$1-281 #domain 3-hydroxyacyl-CoA dehydrogenase homology !8#label HCD\ !$3-31 #region beta-alpha-beta NAD nucleotide-binding fold SUMMARY #length 282 #molecular-weight 30536 #checksum 8183 SEQUENCE /// ENTRY I40679 #type complete TITLE beta-hydroxybutyryl-CoA dehydrogenase, NAD-dependent (EC 1.1.1.-) - Clostridium difficile ORGANISM #formal_name Clostridium difficile DATE 12-Aug-1996 #sequence_revision 01-Nov-1996 #text_change 11-Jun-1999 ACCESSIONS I40679; S49138 REFERENCE I40678 !$#authors Mullany, P.; Clayton, C.L.; Pallen, M.J.; Slone, R.; !1al-Saleh, A.; Tabaqchali, S. !$#journal FEMS Microbiol. Lett. (1994) 124:61-67 !$#title Genes encoding homologues of three consecutive enzymes in !1the butyrate/butanol-producing pathway of Clostridium !1acetobutylicum are clustered on the Clostridium difficile !1chromosome. !$#cross-references MUID:95095030; PMID:8001771 !$#accession I40679 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-281 ##label RES !'##cross-references EMBL:X79899; NID:g509743; PIDN:CAA56272.1; !1PID:g509744 GENETICS !$#gene hbd CLASSIFICATION #superfamily 3-hydroxyacyl-CoA dehydrogenase; !13-hydroxyacyl-CoA dehydrogenase homology KEYWORDS NAD; oxidoreductase FEATURE !$1-280 #domain 3-hydroxyacyl-CoA dehydrogenase homology !8#label HCD\ !$2-30 #region beta-alpha-beta NAD nucleotide-binding fold SUMMARY #length 281 #molecular-weight 30668 #checksum 8868 SEQUENCE /// ENTRY A39503 #type complete TITLE malate dehydrogenase (NAD+) (EC 1.1.1.-) precursor, mitochondrial - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A39503 REFERENCE A39503 !$#authors Loeber, G.; Infante, A.A.; Maurer-Fogy, I.; Krystek, E.; !1Dworkin, M.B. !$#journal J. Biol. Chem. (1991) 266:3016-3021 !$#title Human NAD(+)-dependent mitochondrial malic enzyme. cDNA !1cloning, primary structure, and expression in Escherichia !1coli. !$#cross-references MUID:91131600; PMID:1993674 !$#accession A39503 !'##molecule_type mRNA !'##residues 1-584 ##label LOE !'##cross-references GB:M55905; NID:g187299; PIDN:AAA36197.1; !1PID:g187300 !'##note the authors use enzyme nomenclature (EC 1.1.1.40) which is !1inconsistent with their finding that this enzyme is !1virtually inactive with NADP+ GENETICS !$#gene GDB:ME2 !'##cross-references GDB:119382; OMIM:154270 !$#map_position 6p25-6p24 CLASSIFICATION #superfamily malate dehydrogenase !1(oxaloacetate-decarboxylating) KEYWORDS homotetramer; mitochondrion; NAD; oxidoreductase FEATURE !$1-20 #domain transit peptide (mitochondrion) #status !8predicted #label TPP\ !$21-584 #product malate dehydrogenase (NAD+), mitochondrial !8#status predicted #label MAT SUMMARY #length 584 #molecular-weight 65443 #checksum 4158 SEQUENCE /// ENTRY DEMSMX #type complete TITLE malate dehydrogenase (oxaloacetate-decarboxylating) (NADP) (EC 1.1.1.40) - mouse ALTERNATE_NAMES 'malic' enzyme; pyruvic-malic carboxylase ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Jun-2002 ACCESSIONS A26683; I51951 REFERENCE A26683 !$#authors Bagchi, S.; Wise, L.S.; Brown, M.L.; Bregman, D.; Sul, H.S.; !1Rubin, C.S. !$#journal J. Biol. Chem. (1987) 262:1558-1565 !$#title Structure and expression of murine malic enzyme mRNA. !1Differentiation-dependent accumulation of two forms of malic !1enzyme mRNA in 3T3-L1 cells. !$#cross-references MUID:87109297; PMID:3805042 !$#accession A26683 !'##molecule_type mRNA !'##residues 1-572 ##label BAG !'##cross-references GB:J02652; NID:g199762; PIDN:AAA39727.1; !1PID:g199763 REFERENCE I51951 !$#authors Bagchi, S.; Wise, L.S.; Brown, M.L.; Sul, H.S.; Bregman, !1D.B.; Rubin, C.S. !$#journal Ann. N. Y. Acad. Sci. (1986) 478:77-92 !$#title Regulation and structure of murine malic enzyme mRNA. !$#cross-references MUID:87098422; PMID:3541755 !$#accession I51951 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-572 ##label BA2 !'##cross-references GB:M26756; NID:g199020; PIDN:AAA39489.1; !1PID:g199021 CLASSIFICATION #superfamily malate dehydrogenase !1(oxaloacetate-decarboxylating) KEYWORDS homotetramer; NADP; oxidoreductase FEATURE !$296-325 #region beta-alpha-beta NADP nucleotide-binding fold SUMMARY #length 572 #molecular-weight 63998 #checksum 7727 SEQUENCE /// ENTRY DERTMX #type complete TITLE malate dehydrogenase (oxaloacetate-decarboxylating) (NADP) (EC 1.1.1.40) - rat ALTERNATE_NAMES 'malic' enzyme; pyruvic-malic carboxylase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1991 #sequence_revision 31-Dec-1992 #text_change 03-Jun-2002 ACCESSIONS A37228; A25662; A32942 REFERENCE A37228 !$#authors Nikodem, V.M.; Magnuson, M.A.; Dozin, B.; Morioka, H. !$#journal Endocr. Res. (1989) 15:547-564 !$#title Coding nucleotide sequence of rat malic enzyme mRNA and !1tissue specific regulation by thyroid hormone. !$#cross-references MUID:90235791; PMID:2699453 !$#accession A37228 !'##molecule_type mRNA !'##residues 1-572 ##label NIK !'##cross-references GB:M12545 !'##note part of this sequence was confirmed by protein sequencing REFERENCE A25662 !$#authors Magnuson, M.A.; Morioka, H.; Tecce, M.F.; Nikodem, V.M. !$#journal J. Biol. Chem. (1986) 261:1183-1186 !$#title Coding nucleotide sequence of rat liver malic enzyme mRNA. !$#cross-references MUID:86111756; PMID:3753699 !$#accession A25662 !'##molecule_type mRNA !'##residues 1-563,'PENTDQSQSVTQQLEFLTLLIRS' ##label MAG !'##cross-references GB:M26594; GB:M12545; NID:g205292; PIDN:AAA41563.1; !1PID:g205294 !'##note this sequence contains an error, noted in reference A32942, !1that leads to a frameshift REFERENCE A32942 !$#authors Morioka, H.; Magnuson, M.A.; Mitsuhashi, T.; Song, M.K.H.; !1Rall, J.E.; Nikodem, V.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:4912-4916 !$#title Structural characterization of the rat malic enzyme gene. !$#cross-references MUID:89296914; PMID:2740332 !$#accession A32942 !'##molecule_type DNA !'##residues !125-28;70-72;120-122;145-148;199-202;234-236;271-273;303-306; !1341-344;377-379;424-427;482-485;515-518 ##label MOR !'##cross-references GB:M12545 COMMENT This protein is cytoplasmic. GENETICS !$#introns 26/3; 71/2; 121/2; 146/3; 200/3; 235/2; 272/1; 304/3; 342/3; !1378/; 425/3; 483/3; 516/3 CLASSIFICATION #superfamily malate dehydrogenase !1(oxaloacetate-decarboxylating) KEYWORDS homotetramer; NADP; oxidoreductase FEATURE !$296-325 #region beta-alpha-beta NADP nucleotide-binding fold SUMMARY #length 572 #molecular-weight 64002 #checksum 7429 SEQUENCE /// ENTRY S23435 #type complete TITLE malate dehydrogenase (oxaloacetate-decarboxylating) (NADP) (EC 1.1.1.40) - duck ALTERNATE_NAMES malic enzyme ORGANISM #formal_name Anas platyrhynchos #common_name domestic duck DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S23435; S17867 REFERENCE S23435 !$#authors Hsu, R.Y.; Glynias, M.J.; Satterlee, J.; Feeney, R.; Clarke, !1A.R.; Emery, D.C.; Roe, B.A.; Wilson, R.K.; Goodridge, A.G.; !1Holbrook, J.J. !$#journal Biochem. J. (1992) 284:869-876 !$#title Duck liver 'malic' enzyme. Expression in Escherichia coli !1and characterization of the wild-type enzyme and !1site-directed mutants. !$#cross-references MUID:92322014; PMID:1622402 !$#accession S23435 !'##molecule_type mRNA !'##residues 1-557 ##label HSU !'##cross-references EMBL:X66418; NID:g62459; PIDN:CAA47049.1; !1PID:g62460 REFERENCE S17867 !$#authors Satterlee, J.; Hsu, R.Y. !$#journal Biochim. Biophys. Acta (1991) 1079:247-252 !$#title Duck liver malic enzyme: sequence of a tryptic peptide !1containing the cysteine residue labeled by the substrate !1analog bromopyruvate. !$#cross-references MUID:92002141; PMID:1911848 !$#accession S17867 !'##molecule_type protein !'##residues 86-98,'X',100-107 ##label SAT CLASSIFICATION #superfamily malate dehydrogenase !1(oxaloacetate-decarboxylating) KEYWORDS NADP; oxidoreductase FEATURE !$285-314 #region beta-alpha-beta NADP nucleotide-binding fold\ !$99 #active_site Cys #status predicted SUMMARY #length 557 #molecular-weight 61898 #checksum 6180 SEQUENCE /// ENTRY S29742 #type complete TITLE malate dehydrogenase (oxaloacetate-decarboxylating) (NADP) (EC 1.1.1.40) - pig roundworm ALTERNATE_NAMES malic enzyme ORGANISM #formal_name Ascaris suum #common_name pig roundworm DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S29742 REFERENCE S29742 !$#authors Kulkarni, G.; Cook, P.F.; Harris, B.G. !$#journal Arch. Biochem. Biophys. (1993) 300:231-237 !$#title Cloning and nucleotide sequence of a full-length cDNA !1encoding Ascaris suum malic enzyme. !$#cross-references MUID:93143319; PMID:8424657 !$#accession S29742 !'##molecule_type mRNA !'##residues 1-617 ##label KUL !'##cross-references EMBL:M81055 CLASSIFICATION #superfamily malate dehydrogenase !1(oxaloacetate-decarboxylating) KEYWORDS mitochondrion; NADP; oxidoreductase FEATURE !$334-363 #region beta-alpha-beta NADP nucleotide-binding fold SUMMARY #length 617 #molecular-weight 69818 #checksum 5743 SEQUENCE /// ENTRY DEZMMX #type complete TITLE malate dehydrogenase (oxaloacetate-decarboxylating) (NADP) (EC 1.1.1.40) precursor, chloroplast - maize ALTERNATE_NAMES 'malic' enzyme; pyruvic-malic carboxylase ORGANISM #formal_name Zea mays #common_name maize DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Jun-2002 ACCESSIONS A34482 REFERENCE A34482 !$#authors Rothermel, B.A.; Nelson, T. !$#journal J. Biol. Chem. (1989) 264:19587-19592 !$#title Primary structure of the maize NADP-dependent malic enzyme. !$#cross-references MUID:90062054; PMID:2584183 !$#accession A34482 !'##molecule_type mRNA !'##residues 1-636 ##label ROT !'##cross-references GB:J05130; NID:g168527; PIDN:AAA33487.1; !1PID:g168528 COMMENT This is one of the enzymes in the C-4 photosynthetic !1pathway; it can use either NADP or NAD as a cofactor. CLASSIFICATION #superfamily malate dehydrogenase !1(oxaloacetate-decarboxylating) KEYWORDS chloroplast; homotetramer; NAD; NADP; oxidoreductase FEATURE !$1-62 #domain (or 1-80) transit peptide (chloroplast) !8#status predicted #label TNP\ !$63-636 #product (or 81-636) malate dehydrogenase !8(oxaloacetate-decarboxylating) (NADP+) #status !8predicted #label MAT\ !$378-408 #region beta-alpha-beta NADP nucleotide-binding fold SUMMARY #length 636 #molecular-weight 69823 #checksum 3350 SEQUENCE /// ENTRY S12893 #type complete TITLE malate dehydrogenase (oxaloacetate-decarboxylating) (NADP) (EC 1.1.1.40) precursor - Flaveria trinervia ALTERNATE_NAMES malic enzyme; NADP-malic enzyme ORGANISM #formal_name Flaveria trinervia DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S12893; S78588 REFERENCE S12893 !$#authors Boersch, D.; Westhoff, P. !$#journal FEBS Lett. (1990) 273:111-115 !$#title Primary structure of NADP-dependent malic enzyme in the !1dicotyledonous C(4) plant Flaveria trinervia. !$#cross-references MUID:91032157; PMID:2226841 !$#accession S12893 !'##molecule_type mRNA !'##residues 1-648 ##label BOE !'##cross-references EMBL:X57142; NID:g18459; PIDN:CAA40421.1; !1PID:g18460 REFERENCE S17455 !$#authors Rajeevan, M.S.; Bassett, C.L.; Hughes, D.W. !$#journal Plant Mol. Biol. (1991) 17:371-383 !$#title Isolation and characterization of cDNA clones for NADP-malic !1enzyme from leaves of Flaveria: transcript abundance !1distinguishes C(3), C(3)-C(4) and C(4) photosynthetic types. !$#cross-references MUID:91355929; PMID:1883995 !$#accession S78588 !'##molecule_type mRNA !'##residues 461-579,'L',581-648 ##label RAJ !'##cross-references EMBL:M59416; NID:g168171; PIDN:AAB19243.1; !1PID:g1679885 GENETICS !$#genome nuclear CLASSIFICATION #superfamily malate dehydrogenase !1(oxaloacetate-decarboxylating) KEYWORDS chloroplast; NADP; oxidoreductase FEATURE !$1-61 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$62-648 #product malate dehydrogenase !8(oxaloacetate-decarboxylating) (NADP+) #status !8predicted #label MAT\ !$390-420 #region beta-alpha-beta NADP nucleotide-binding fold SUMMARY #length 648 #molecular-weight 71469 #checksum 4142 SEQUENCE /// ENTRY S42939 #type complete TITLE malate dehydrogenase (oxaloacetate-decarboxylating) (NADP) (EC 1.1.1.40) precursor - Flaveria pringlei ORGANISM #formal_name Flaveria pringlei DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S52016; S42939 REFERENCE S52016 !$#authors Lipka, B.; Steinmueller, K.; Rosche, E.; Boersch, D.; !1Westhoff, P. !$#journal Plant Mol. Biol. (1994) 26:1775-1783 !$#title The C(3) plant Flaveria pringlei contains a plastidic !1NADP-malic enzyme which is orthologous to the C(4) isoform !1of the C(4) plant F. trinervia. !$#cross-references MUID:95161702; PMID:7858216 !$#accession S52016 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-647 ##label LIP !'##cross-references EMBL:X78069; NID:g459440; PIDN:CAA54986.1; !1PID:g459441 CLASSIFICATION #superfamily malate dehydrogenase !1(oxaloacetate-decarboxylating) KEYWORDS chloroplast; NADP; oxidoreductase FEATURE !$389-419 #region beta-alpha-beta NADP nucleotide-binding fold SUMMARY #length 647 #molecular-weight 71203 #checksum 2685 SEQUENCE /// ENTRY DEFBC #type complete TITLE malate dehydrogenase (oxaloacetate-decarboxylating) (NADP) (EC 1.1.1.40) - kidney bean ALTERNATE_NAMES cinnamyl-alcohol dehydrogenase [misidentification]; malic enzyme, NADP-dependent ORGANISM #formal_name Phaseolus vulgaris #common_name kidney bean DATE 30-Sep-1991 #sequence_revision 11-Apr-1997 #text_change 03-Jun-2002 ACCESSIONS S48198; S51804; A31323 REFERENCE S48198 !$#authors Walter, M.H.; Grima-Pettenati, J.; Feuillet, C. !$#journal Eur. J. Biochem. (1994) 224:999-1009 !$#title Characterization of a bean (Phaseolus vulgaris L.) !1malic-enzyme gene. !$#cross-references MUID:95010093; PMID:7925425 !$#accession S48198 !'##molecule_type DNA !'##residues 1-589 ##label WAL !'##cross-references EMBL:X80051 !'##experimental_source Phaseolus vulgaris L., cv. Processor !'##note the identification as cinnamyl-alcohol dehydrogenase (EC !11.1.1.195) has been corrected in reference A31323 REFERENCE S51804 !$#authors Walter, M.H.; Grima-Pettenati, J.; Feuillet, C. !$#submission submitted to the EMBL Data Library, July 1994 !$#description Characterization of a bean (Phaeolus vulgaris L.) malic !1enzyme. !$#accession S51804 !'##molecule_type DNA !'##residues 1-15,'N',17-589 ##label WAW !'##cross-references EMBL:X80051; NID:g510875; PIDN:CAA56354.1; !1PID:g510876 !'##experimental_source Phaseolus vulgaris L., cv. Processor REFERENCE A31323 !$#authors Walter, M.H.; Grima-Pettenati, J.; Grand, C.; Boudet, A.M.; !1Lamb, C.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:5546-5550 !$#title Cinnamyl-alcohol dehydrogenase, a molecular marker specific !1for lignin synthesis: cDNA cloning and mRNA induction by !1fungal elicitor. !$#cross-references MUID:88289756; PMID:3041415 !$#accession A31323 !'##molecule_type mRNA !'##residues 1-129,'A',131-257,'TF',260-349,'V',351-566,'K',568-589 !1##label WA2 !'##cross-references GB:J03825; NID:g169326; PIDN:AAA19575.1; !1PID:g169327 !'##experimental_source Phaseolus vulgaris L., cv. Canadian Wonder GENETICS !$#introns 49/2; 89/3; 114/3; 165/2; 200/3; 222/3; 254/3; 278/3; 306/3; !1339/3; 355/3; 373/3; 406/3; 436/3; 462/3; 487/3; 518/1; 561/ !11 CLASSIFICATION #superfamily malate dehydrogenase !1(oxaloacetate-decarboxylating) KEYWORDS NADP; oxidoreductase FEATURE !$331-361 #region beta-alpha-beta NADP nucleotide-binding fold SUMMARY #length 589 #molecular-weight 64967 #checksum 1344 SEQUENCE /// ENTRY S18826 #type complete TITLE malate dehydrogenase (oxaloacetate-decarboxylating) (NADP) (EC 1.1.1.40) (clone 064) - western balsam poplar x cottonwood ALTERNATE_NAMES malic enzyme ORGANISM #formal_name Populus trichocarpa x Populus deltoides #common_name western balsam poplar x cottonwood DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S18826; S26809 REFERENCE S18826 !$#authors van Doorsselaere, J.; Villarroel, R.; van Montagu, M.; Inze, !1D. !$#journal Plant Physiol. (1991) 96:1385-1386 !$#title Nucleotide sequence of a cDNA encoding malic enzyme from !1poplar. !$#accession S18826 !'##molecule_type mRNA !'##residues 1-589 ##label VAN1 !'##cross-references EMBL:X56233 !'##note the authors translated the codon CTA for residue 325 as Ile, !1ATA for residue 413 as Leu, CAA for residue 457 as Glu, and !1ACT for residue 463 as Gly REFERENCE S26809 !$#authors van Doorsselaere, J. !$#submission submitted to the EMBL Data Library, December 1990 !$#accession S26809 !'##molecule_type mRNA !'##residues 1-501,'GL',502-589 ##label VAN2 !'##cross-references EMBL:X56233; NID:g20468; PIDN:CAA39690.1; !1PID:g20469 CLASSIFICATION #superfamily malate dehydrogenase !1(oxaloacetate-decarboxylating) KEYWORDS NADP; oxidoreductase FEATURE !$333-363 #region beta-alpha-beta NADP nucleotide-binding fold SUMMARY #length 589 #molecular-weight 65052 #checksum 3757 SEQUENCE /// ENTRY DEBSXS #type complete TITLE malate dehydrogenase (oxaloacetate-decarboxylating) (EC 1.1.1.38) - Bacillus stearothermophilus ALTERNATE_NAMES 'malic' enzyme; pyruvic-malic carboxylase ORGANISM #formal_name Bacillus stearothermophilus DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 11-Jun-1999 ACCESSIONS A33307 REFERENCE A33307 !$#authors Kobayashi, K.; Doi, S.; Negoro, S.; Urabe, I.; Okada, H. !$#journal J. Biol. Chem. (1989) 264:3200-3205 !$#title Structure and properties of malic enzyme from Bacillus !1stearothermophilus. !$#cross-references MUID:89123439; PMID:2644282 !$#accession A33307 !'##molecule_type DNA !'##residues 1-478 ##label KOB !'##cross-references GB:M19485; NID:g143164; PIDN:AAA22585.1; !1PID:g143165 COMMENT This enzyme strictly requires divalent metal ions for its !1activity. In addition to the NAD-dependent oxidative !1decarboxylation of L-malate, the enzyme catalyzes the !1decarboxylation of oxalacetate. CLASSIFICATION #superfamily malate dehydrogenase !1(oxaloacetate-decarboxylating) KEYWORDS homotetramer; NAD; oxidoreductase FEATURE !$264-293 #region beta-alpha-beta NAD nucleotide-binding fold SUMMARY #length 478 #molecular-weight 51536 #checksum 30 SEQUENCE /// ENTRY DCECIS #type complete TITLE isocitrate dehydrogenase (NADP) (EC 1.1.1.42) [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES oxalosuccinate decarboxylase ORGANISM #formal_name Escherichia coli DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 03-Jun-2002 ACCESSIONS A28482; E64858 REFERENCE A28482 !$#authors Thorsness, P.E.; Koshland Jr., D.E. !$#journal J. Biol. Chem. (1987) 262:10422-10425 !$#title Inactivation of isocitrate dehydrogenase by phosphorylation !1is mediated by the negative charge of the phosphate. !$#cross-references MUID:87280090; PMID:3112144 !$#accession A28482 !'##molecule_type DNA !'##residues 1-416 ##label THO !'##cross-references GB:J02799; NID:g146431; PIDN:AAA24006.1; !1PID:g146432 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64858 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-416 ##label BLAT !'##cross-references GB:AE000213; GB:U00096; NID:g1787371; !1PIDN:AAC74220.1; PID:g1787381; UWGP:b1136 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene icdA; icd; icdE !$#map_position 25 min FUNCTION !$#description EC 1.1.1.42 [validated, MUID:87280090]; catalyzes the !1NADP-specific oxidative decarboxylation of isocitrate to !12-oxoglutarate !$#note inhibition by phosphorylation regulates the branch point !1between the Krebs cycle and the glyoxylate bypass, which is !1an alternate route that accumulates carbon for biosynthesis !1when acetate is the sole carbon source for growth of E. coli CLASSIFICATION #superfamily isocitrate dehydrogenase (NADP) KEYWORDS glyoxylate bypass; homodimer; NADP; oxidoreductase; !1phosphoprotein; tricarboxylic acid cycle FEATURE !$113 #binding_site phosphate (Ser) (covalent) #status !8experimental SUMMARY #length 416 #molecular-weight 45756 #checksum 705 SEQUENCE /// ENTRY B49341 #type complete TITLE isocitrate dehydrogenase (NADP) (EC 1.1.1.42) I - Vibrio sp. (strain ABE-1) ALTERNATE_NAMES oxalosuccinate decarboxylase 1 ORGANISM #formal_name Vibrio sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS B49341 REFERENCE A49341 !$#authors Ishii, A.; Suzuki, M.; Sahara, T.; Takada, Y.; Sasaki, S.; !1Fukunaga, N. !$#journal J. Bacteriol. (1993) 175:6873-6880 !$#title Genes encoding two isocitrate dehydrogenase isozymes of a !1psychrophilic bacterium, Vibrio sp. strain ABE-1. !$#cross-references MUID:94042850; PMID:8226630 !$#accession B49341 !'##status preliminary !'##molecule_type DNA !'##residues 1-415 ##label ISH !'##cross-references GB:D14047; NID:g217187; PIDN:BAA03135.1; !1PID:g217189 !'##experimental_source strain ABE-1 GENETICS !$#gene icdI FUNCTION !$#description catalyzes the NADP-specific oxidative decarboxylation of !1isocitrate to 2-oxoglutarate !$#note induction by acetate CLASSIFICATION #superfamily isocitrate dehydrogenase (NADP) KEYWORDS glyoxylate bypass; homodimer; NADP; oxidoreductase; !1phosphoprotein; tricarboxylic acid cycle FEATURE !$113 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 415 #molecular-weight 45145 #checksum 5764 SEQUENCE /// ENTRY I40382 #type complete TITLE isocitrate dehydrogenase (NADP) (EC 1.1.1.42) - Bacillus subtilis ALTERNATE_NAMES oxalosuccinate decarboxylase ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS I40382; H69599 REFERENCE I40379 !$#authors Jin, S.; Sonenshein, A.L. !$#journal J. Bacteriol. (1994) 176:4669-4679 !$#title Identification of two distinct Bacillus subtilis citrate !1synthase genes. !$#cross-references MUID:94321340; PMID:8045898 !$#accession I40382 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-423 ##label RES !'##cross-references EMBL:U05257; NID:g1045295; PIDN:AAA96342.1; !1PID:g487434 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69599 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-423 ##label KUN !'##cross-references GB:Z99118; GB:AL009126; NID:g2635200; !1PIDN:CAB14873.1; PID:g2635378 !'##experimental_source strain 168 GENETICS !$#gene citC !$#start_codon GTG FUNCTION !$#description catalyzes the NADP-specific oxidative decarboxylation of !1isocitrate to 2-oxoglutarate CLASSIFICATION #superfamily isocitrate dehydrogenase (NADP) KEYWORDS glyoxylate bypass; NADP; oxidoreductase; phosphoprotein; !1tricarboxylic acid cycle FEATURE !$104 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 423 #molecular-weight 46417 #checksum 3362 SEQUENCE /// ENTRY DCBYIS #type complete TITLE isocitrate dehydrogenase (NADP) (EC 1.1.1.42) precursor, mitochondrial - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein D2522; protein YDL066w ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 03-Jun-2002 ACCESSIONS A38610; B38610; S67601; S69170 REFERENCE A38610 !$#authors Haselbeck, R.J.; McAlister-Henn, L. !$#journal J. Biol. Chem. (1991) 266:2339-2345 !$#title Isolation, nucleotide sequence, and disruption of the !1Saccharomyces cerevisiae gene encoding mitochondrial NADP !1(H)-specific isocitrate dehydrogenase. !$#cross-references MUID:91115852; PMID:1989987 !$#accession A38610 !'##molecule_type DNA !'##residues 1-428 ##label HAS !'##cross-references GB:M57229; NID:g171748; PIDN:AAA34703.1; !1PID:g171749 !$#accession B38610 !'##molecule_type protein !'##residues 17-36 ##label HA2 REFERENCE S67587 !$#authors Bloecker, H.; Brandt, P. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67601 !'##molecule_type DNA !'##residues 1-428 ##label BLO !'##cross-references EMBL:Z74114; NID:g1431073; PIDN:CAA98631.1; !1PID:g1431074; GSPDB:GN00004; MIPS:YDL066w !'##experimental_source strain S288C REFERENCE S69170 !$#authors Huang, Y.C.; Haselbeck, R.J.; McAlister-Henn, L.; Colman, !1R.F. !$#journal Arch. Biochem. Biophys. (1995) 316:485-492 !$#title N-ethylmaleimide profiling of yeast NADP-dependent !1isocitrate dehydrogenase. !$#cross-references MUID:95142667; PMID:7840654 !$#accession S69170 !'##molecule_type protein !'##residues 'X',90-98;356-358,'X',360;361-369,'X',371;393-397,'X', !1399-403 ##label HUA GENETICS !$#gene SGD:IDP1; MIPS:YDL066w !'##cross-references SGD:S0002224; MIPS:YDL066w !$#map_position 4L CLASSIFICATION #superfamily yeast isocitrate dehydrogenase (NADP+) KEYWORDS homodimer; mitochondrion; NADP; oxidoreductase; !1tricarboxylic acid cycle FEATURE !$1-16 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$17-428 #product isocitrate dehydrogenase (NADP+), !8mitochondrial #status experimental #label MAT\ !$63 #active_site Glu #status predicted SUMMARY #length 428 #molecular-weight 48190 #checksum 9126 SEQUENCE /// ENTRY A43294 #type complete TITLE isocitrate dehydrogenase (NADP) (EC 1.1.1.42), mitochondrial - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS A43294; A27371; A27372; A39333 REFERENCE A43294 !$#authors Haselbeck, R.J.; Colman, R.F.; McAlister-Henn, L. !$#journal Biochemistry (1992) 31:6219-6223 !$#title Isolation and sequence of a cDNA encoding porcine !1mitochondrial NADP-specific isocitrate dehydrogenase. !$#cross-references MUID:92329444; PMID:1627563 !$#accession A43294 !'##molecule_type mRNA !'##residues 1-421 ##label HAS !'##cross-references GB:M86719; NID:g294222; PIDN:AAA31089.1; !1PID:g294223 !'##note sequence extracted from NCBI backbone (NCBIN:108410, !1NCBIP:108411) REFERENCE A27371 !$#authors Ehrlich, R.S.; Colman, R.F. !$#journal J. Biol. Chem. (1987) 262:12614-12619 !$#title Characterization of an active site peptide modified by the !1substrate analogue 3-bromo-2-ketoglutarate on a single chain !1of dimeric NADP(+)-dependent isocitrate dehydrogenase. !$#cross-references MUID:87308292; PMID:3624273 !$#accession A27371 !'##molecule_type protein !'##residues 383-386,'X',388-395 ##label EHR REFERENCE A27372 !$#authors Bailey, J.M.; Colman, R.F. !$#journal J. Biol. Chem. (1987) 262:12620-12626 !$#title Isolation of the glutamyl peptide labeled by the nucleotide !1analogue 2-(4-bromo-2,3-dioxobutylthio)-1,N !1(6)-ethenoadenosine 2',5'-bisphosphate in the active site of !1NADP(+)-specific isocitrate dehydrogenase. !$#cross-references MUID:87308293; PMID:2887570 !$#accession A27372 !'##molecule_type protein !'##residues 383-386,'E',388-395 ##label BAI !'##note later work from this lab showed this fragment is not a glutamyl !1peptide, but a cysteinyl peptide modified by a substrate !1analog at position 387-Cys; this modification seems to be !1near the coenzyme site REFERENCE A39333 !$#authors Smyth, G.E.; Colman, R.F. !$#journal J. Biol. Chem. (1991) 266:14918-14925 !$#title Cysteinyl peptides of pig heart NADP-dependent isocitrate !1dehydrogenase that are modified upon inactivation by !1N-ethylmaleimide. !$#cross-references MUID:91332002; PMID:1869531 !$#accession A39333 !'##status preliminary !'##molecule_type protein !'##residues 82-91;119-124;372-382;201-211;269-278;383-395 ##label SMY CLASSIFICATION #superfamily yeast isocitrate dehydrogenase (NADP+) KEYWORDS homodimer; mitochondrion; NADP; oxidoreductase; !1tricarboxylic acid cycle SUMMARY #length 421 #molecular-weight 47526 #checksum 9935 SEQUENCE /// ENTRY S33859 #type complete TITLE isocitrate dehydrogenase (NADP) (EC 1.1.1.42) precursor, mitochondrial - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S33859; S31390 REFERENCE S33859 !$#authors Huh, T.L.; Ryu, J.H.; Huh, J.W.; Sung, H.C.; Oh, I.U.; Song, !1B.J.; Veech, R.L. !$#journal Biochem. J. (1993) 292:705-710 !$#title Cloning of a cDNA encoding bovine mitochondrial NADP !1(+)-specific isocitrate dehydrogenase and structural !1comparison with its isoenzymes from different species. !$#cross-references MUID:93305052; PMID:8318002 !$#accession S33859 !'##molecule_type mRNA !'##residues 1-452 ##label HUH !'##cross-references EMBL:X69432; NID:g429; PIDN:CAA49207.1; PID:g430 CLASSIFICATION #superfamily yeast isocitrate dehydrogenase (NADP+) KEYWORDS homodimer; mitochondrion; NADP; oxidoreductase SUMMARY #length 452 #molecular-weight 50824 #checksum 9418 SEQUENCE /// ENTRY T46280 #type complete TITLE isocitrate dehydrogenase (NADP) (EC 1.1.1.42), cytosolic [similarity] - human ALTERNATE_NAMES protein DKFZp566J151.1 ORGANISM #formal_name Homo sapiens #common_name man DATE 03-Mar-2000 #sequence_revision 03-Mar-2000 #text_change 03-Jun-2002 ACCESSIONS T46280 REFERENCE Z23034 !$#authors Blum, H.; Bauersachs, S.; Mewes, H.W.; Gassenhuber, J.; !1Wiemann, S. !$#submission submitted to the Protein Sequence Database, January 2000 !$#accession T46280 !'##molecule_type mRNA !'##residues 1-414 ##label BLU !'##cross-references EMBL:AL136702; NID:g6807654; PIDN:CAB66637.1; !1PID:g6807655 !'##experimental_source fetal kidney; clone DKFZp566J151 GENETICS !$#gene GDB:IDH1 !'##cross-references GDB:119325; OMIM:147700 !$#map_position 2q32-2qter !$#note DKFZp566J151.1 FUNCTION !$#description catalyzes the oxidative decarboxylation of isocitrate to !1form alpha-ketoglutarate CLASSIFICATION #superfamily yeast isocitrate dehydrogenase (NADP+) KEYWORDS cytosol; NADP; oxidoreductase FEATURE !$47,139,212 #active_site Glu, Tyr, Lys #status predicted SUMMARY #length 414 #molecular-weight 46626 #checksum 1182 SEQUENCE /// ENTRY A54756 #type complete TITLE isocitrate dehydrogenase (NADP) (EC 1.1.1.42), cytosolic - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS A54756 REFERENCE A54756 !$#authors Jennings, G.T.; Sechi, S.; Stevenson, P.M.; Tuckey, R.C.; !1Parmelee, D.; McAlister-Henn, L. !$#journal J. Biol. Chem. (1994) 269:23128-23134 !$#title Cytosolic NADP(+)-dependent isocitrate dehydrogenase. !1Isolation of rat cDNA and study of tissue-specific and !1developmental expression of mRNA. !$#cross-references MUID:94365011; PMID:8083215 !$#accession A54756 !'##status preliminary !'##molecule_type mRNA !'##residues 1-414 ##label JEN !'##cross-references GB:L35317; NID:g537940; PIDN:AAA59356.1; !1PID:g537941 CLASSIFICATION #superfamily yeast isocitrate dehydrogenase (NADP+) KEYWORDS cytosol; NADP; oxidoreductase SUMMARY #length 414 #molecular-weight 46734 #checksum 120 SEQUENCE /// ENTRY JH0531 #type complete TITLE phosphogluconate dehydrogenase (decarboxylating) (EC 1.1.1.44) - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES 6-phosphogluconate dehydrogenase ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS JH0531; T13608 REFERENCE JH0531 !$#authors Scott, M.J.; Lucchesi, J.C. !$#journal Gene (1991) 109:177-183 !$#title Structure and expression of the Drosophila melanogaster gene !1encoding 6-phosphogluconate dehydrogenase. !$#cross-references MUID:92112041; PMID:1765265 !$#accession JH0531 !'##molecule_type DNA !'##residues 1-481 ##label SCO !'##cross-references GB:M80598; NID:g401733; PIDN:AAA28786.1; !1PID:g158123 REFERENCE Z17668 !$#authors Murphy, L.; Harris, D.; Barrell, B. !$#submission submitted to the EMBL Data Library, April 1999 !$#description Sequencing the distal X chromosome of Drosophila !1melanogaster. !$#accession T13608 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-481 ##label MUR !'##cross-references EMBL:Z98269; PIDN:CAB10974.1 COMMENT This protein is one of the key enzymes of the pentose !1phosphate pathway. GENETICS !$#gene Pgd+ !'##cross-references FlyBase:FBgn0004654 !$#introns 3/2; 78/1 CLASSIFICATION #superfamily phosphogluconate dehydrogenase !1(decarboxylating); 3-hydroxyisobutyrate dehydrogenase !1homology KEYWORDS oxidoreductase; pentose phosphate pathway FEATURE !$7-284 #domain 3-hydroxyisobutyrate dehydrogenase homology !8#label HIB SUMMARY #length 481 #molecular-weight 52491 #checksum 8418 SEQUENCE /// ENTRY DEECGC #type complete TITLE phosphogluconate dehydrogenase (decarboxylating) (EC 1.1.1.44) - Escherichia coli (strain K-12) ALTERNATE_NAMES gluconate-6-phosphate dehydrogenase ORGANISM #formal_name Escherichia coli DATE 28-Feb-1986 #sequence_revision 23-Jan-1998 #text_change 01-Mar-2002 ACCESSIONS D64968; I62464; I62462; A00360; I41248; I41246; I41243; !1I41244; I41245; I41247; E40630; I54956 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64968 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-468 ##label BLAT !'##cross-references GB:AE000294; GB:U00096; NID:g1788338; !1PIDN:AAC75090.1; PID:g1788341; UWGP:b2029 !'##experimental_source strain K-12, substrain MG1655 REFERENCE I41249 !$#authors Dykhuizen, D.E.; Green, L. !$#journal J. Bacteriol. (1991) 173:7257-7268 !$#title Recombination in Escherichia coli and definition of !1biological species. !$#cross-references MUID:92041624; PMID:1938920 !$#accession I62464 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-208,'S',210-307,'G',309-421,'A',423-468 ##label RES !'##cross-references GB:M64330; NID:g146939; PIDN:AAA24208.1; !1PID:g146940 !'##experimental_source strain ECOR68 !$#accession I62462 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-210,'S',212-324,'Q',326-349,'A',351-421,'A',423-468 !1##label RE9 !'##cross-references GB:M64328; NID:g146935; PIDN:AAA24206.1; !1PID:g146936 !'##experimental_source strain ECOR69 REFERENCE A00360 !$#authors Nasoff, M.S.; Baker II, H.V.; Wolf Jr., R.E. !$#journal Gene (1984) 27:253-264 !$#title DNA sequence of the Escherichia coli gene, gnd, for !16-phosphogluconate dehydrogenase. !$#cross-references MUID:84237540; PMID:6329905 !$#accession A00360 !'##molecule_type DNA !'##residues 1-305,'R',307-468 ##label NAS !'##cross-references GB:K02072; NID:g146231; PIDN:AAA23918.1; !1PID:g146232 REFERENCE I41248 !$#authors Miller, R.D.; Dykhuizen, D.E.; Hartl, D.L. !$#journal Mol. Biol. Evol. (1988) 5:691-703 !$#title Fitness effects of a deletion mutation increasing !1transcription of the 6-phosphogluconate dehydrogenase gene !1in Escherichia coli. !$#cross-references MUID:89126937; PMID:2464736 !$#accession I41248 !'##molecule_type DNA !'##residues 1-125 ##label RE8 !'##cross-references GB:M23181; NID:g146243; PIDN:AAA23924.1; !1PID:g146244 REFERENCE I41243 !$#authors Barcak, G.J.; Wolf, R.E. !$#journal J. Bacteriol. (1988) 170:372-379 !$#title Comparative nucleotide sequence analysis of !1growth-rate-regulated gnd alleles from natural isolates of !1Escherichia coli and from Salmonella typhimurium LT-2. !$#cross-references MUID:88086897; PMID:3275621 !$#accession I41246 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-125 ##label RE4 !'##cross-references GB:M18960; NID:g146239; PIDN:AAA23922.1; !1PID:g146240 !'##experimental_source strain 558 !$#accession I41243 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-125 ##label RE2 !'##cross-references GB:M18956; NID:g146233; PIDN:AAA23919.1; !1PID:g146234 !'##experimental_source strain B/r !$#accession I41244 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-125 ##label RE3 !'##cross-references GB:M18957; NID:g146235; PIDN:AAA23920.1; !1PID:g146236 !'##experimental_source strain 740 !$#accession I41245 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-30,'V',32-36,'D',38-53,'F',55-125 ##label RE6 !'##cross-references GB:M18958; NID:g146237; PIDN:AAA23921.1; !1PID:g146238 !'##experimental_source strain 567 !$#accession I41247 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-48,'Q',50-125 ##label RE7 !'##cross-references GB:M18961; NID:g146241; PIDN:AAA23923.1; !1PID:g146242 !'##experimental_source strain 745 REFERENCE A40630 !$#authors Marolda, C.L.; Valvano, M.A. !$#journal J. Bacteriol. (1993) 175:148-158 !$#title Identification, expression, and DNA sequence of the !1GDP-mannose biosynthesis genes encoded by the O7 rfb gene !1cluster of strain VW187 (Escherichia coli O7:K1). !$#cross-references MUID:93106949; PMID:7677991 !$#accession E40630 !'##molecule_type DNA !'##residues 1-38,'Q',40-122,'YRY' ##label MAR !'##cross-references GB:L04596; NID:g5524160; PIDN:AAC27540.1; !1PID:g415625 !'##experimental_source strain VW187 (Escherichia coli O7:K1) !'##note sequence extracted from NCBI backbone (NCBIN:121128, !1NCBIP:121133) !'##note the final three residues of this fragment differ by an apparant !1frameshift error REFERENCE I54956 !$#authors Bisercic, M.; Feutrier, J.Y.; Reeves, P.R. !$#journal J. Bacteriol. (1991) 173:3894-3900 !$#title Nucleotide sequences of the gnd genes from nine natural !1isolates of escherichia coli: evidence of intragenic !1recombination as a contributing factor in the evolution of !1the polymorphic gnd locus. !$#cross-references MUID:91267957; PMID:2050640 !$#accession I54956 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-51,'D',53-54,'F',56-169,'F',171-210,'S',212-329,'S', !1331-349,'A',351-368,'R',370-421,'A',423-468 ##label RE5 !'##cross-references GB:M63821; NID:g147486; PIDN:AAA24488.1; !1PID:g147487 !'##experimental_source strain ECOR10 COMMENT This phosphogluconate dehydrogenase catalyzes the oxidative !1decarboxylation of 6-phosphogluconate in the presence of !1NADP to form D-ribulose 5-phosphate and NADPH in the hexose !1monophosphate shunt. GENETICS !$#gene gnd !$#map_position 44 min CLASSIFICATION #superfamily phosphogluconate dehydrogenase !1(decarboxylating); 3-hydroxyisobutyrate dehydrogenase !1homology KEYWORDS NADP; oxidative decarboxylation; oxidoreductase; pentose !1phosphate pathway FEATURE !$6-285 #domain 3-hydroxyisobutyrate dehydrogenase homology !8#label HIB SUMMARY #length 468 #molecular-weight 51481 #checksum 7624 SEQUENCE /// ENTRY DESHGC #type complete TITLE phosphogluconate dehydrogenase (decarboxylating) (EC 1.1.1.44) - sheep ALTERNATE_NAMES 6-phosphogluconate carboxylase; 6-phosphogluconate dehydrogenase; phosphogluconic acid dehydrogenase ORGANISM #formal_name Ovis orientalis aries, Ovis ammon aries #common_name domestic sheep DATE 28-Feb-1986 #sequence_revision 02-May-1994 #text_change 11-Jun-1999 ACCESSIONS S27359; A00359; S21875 REFERENCE S27359 !$#authors Somers, D.O.; Medd, S.M.; Walker, J.E.; Adams, M.J. !$#journal Biochem. J. (1992) 288:1061-1067 !$#title Sheep 6-phosphogluconate dehydrogenase. Revised protein !1sequence based upon the sequences of cDNA clones obtained !1with the polymerase chain reaction. !$#cross-references MUID:93111932; PMID:1471978 !$#accession S27359 !'##molecule_type mRNA !'##residues 1-483 ##label SOM !'##cross-references EMBL:X60195; NID:g1192; PIDN:CAA42751.1; PID:g1193 REFERENCE A00359 !$#authors Carne, A.; Walker, J.E. !$#journal J. Biol. Chem. (1983) 258:12895-12906 !$#title Amino acid sequence of ovine 6-phosphogluconate !1dehydrogenase. !$#cross-references MUID:84032505; PMID:6685125 !$#contents annotation; preliminary sequence; modified site !$#note the sequence differs extensively from that shown COMMENT This phosphogluconate dehydrogenase catalyzes the oxidative !1decarboxylation of 6-phosphogluconate in the presence of !1NADP to form D-ribulose 5-phosphate and NADPH in the hexose !1monophosphate shunt. CLASSIFICATION #superfamily phosphogluconate dehydrogenase !1(decarboxylating); 3-hydroxyisobutyrate dehydrogenase !1homology KEYWORDS acetylated amino end; homodimer; NADP; oxidative !1decarboxylation; oxidoreductase; pentose phosphate pathway FEATURE !$2-483 #product phosphogluconate dehydrogenase !8(decarboxylating) #status predicted #label MAT\ !$6-286 #domain 3-hydroxyisobutyrate dehydrogenase homology !8#label HIB\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental SUMMARY #length 483 #molecular-weight 52969 #checksum 1871 SEQUENCE /// ENTRY S15280 #type complete TITLE phosphogluconate dehydrogenase (decarboxylating) (EC 1.1.1.44) - sheep ORGANISM #formal_name Ovis orientalis aries, Ovis ammon aries #common_name domestic sheep DATE 24-Oct-2000 #sequence_revision 24-Oct-2000 #text_change 24-Oct-2000 ACCESSIONS S15280 REFERENCE S15279 !$#authors Reizer, A.; Deutscher, J.; Saier Jr., M.H.; Reizer, J. !$#journal Mol. Microbiol. (1991) 5:1081-1089 !$#title Analysis of the gluconate (gnt) operon of Bacillus subtilis. !$#cross-references MUID:92065803; PMID:1659648 !$#accession S15280 !'##status preliminary !'##molecule_type DNA !'##residues 1-466 ##label REI CLASSIFICATION #superfamily phosphogluconate dehydrogenase !1(decarboxylating); 3-hydroxyisobutyrate dehydrogenase !1homology KEYWORDS oxidoreductase; pentose phosphate pathway FEATURE !$3-283 #domain 3-hydroxyisobutyrate dehydrogenase homology !8#label HIB SUMMARY #length 466 #molecular-weight 51270 #checksum 5700 SEQUENCE /// ENTRY S46671 #type complete TITLE phosphogluconate dehydrogenase (decarboxylating) (EC 1.1.1.44) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES 6-phosphogluconate dehydrogenase; protein H9186.2; protein YHR183w ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 23-Mar-2001 ACCESSIONS S46671; S50242; S49601 REFERENCE S46672 !$#authors Macri, C. !$#submission submitted to the EMBL Data Library, February 1994 !$#description The sequence of S. cerevisiae cosmid 9186. !$#accession S46671 !'##molecule_type DNA !'##residues 1-489 ##label MAC !'##cross-references EMBL:U00028; NID:g458909; PIDN:AAB68452.1; !1PID:g458910; GSPDB:GN00008; MIPS:YHR183w REFERENCE S50242 !$#authors DeSouza, M.; Lobo, Z.; Maitra, P.K. !$#submission submitted to the EMBL Data Library, November 1994 !$#description 6-phosphogluconate dehydrogenase in Saccharomyces !1cerevisiae. !$#accession S50242 !'##molecule_type DNA !'##residues 1-489 ##label DES !'##cross-references EMBL:U17155; NID:g577838; PIDN:AAA53637.1; !1PID:g577839; EMBL:Z46631; NID:g575390; PID:g575391 GENETICS !$#gene SGD:GND1; MIPS:YHR183w !'##cross-references SGD:S0001226; MIPS:YHR183w !$#map_position 8R FUNCTION !$#description oxidoreductase !$#pathway pentose phosphate pathway CLASSIFICATION #superfamily phosphogluconate dehydrogenase !1(decarboxylating); 3-hydroxyisobutyrate dehydrogenase !1homology KEYWORDS oxidoreductase; pentose phosphate pathway FEATURE !$5-284 #domain 3-hydroxyisobutyrate dehydrogenase homology !8#label HIB SUMMARY #length 489 #molecular-weight 53543 #checksum 8965 SEQUENCE /// ENTRY S04397 #type complete TITLE phosphogluconate dehydrogenase (decarboxylating) (EC 1.1.1.44) - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S04397; S15315 REFERENCE S04397 !$#authors Reeves, P.; Stevenson, G. !$#journal Mol. Gen. Genet. (1989) 217:182-184 !$#title Cloning and nucleotide sequence of the Salmonella !1typhimurium LT2 gnd gene and its homology with the !1corresponding sequence of Escherichia coli K12. !$#cross-references MUID:89364685; PMID:2671649 !$#accession S04397 !'##molecule_type DNA !'##residues 1-468 ##label REE REFERENCE S15296 !$#authors Jiang, X.M.; Neal, B.; Santiago, F.; Lee, S.J.; Romana, !1L.K.; Reeves, P.R. !$#journal Mol. Microbiol. (1991) 5:695-713 !$#title Structure and sequence of the rfb (O antigen) gene cluster !1of Salmonella serovar typhimurium (strain LT2). !$#cross-references MUID:91260454; PMID:1710759 !$#accession S15315 !'##status preliminary !'##molecule_type DNA !'##residues 1-57 ##label JIA GENETICS !$#gene gnd CLASSIFICATION #superfamily phosphogluconate dehydrogenase !1(decarboxylating); 3-hydroxyisobutyrate dehydrogenase !1homology KEYWORDS oxidoreductase; pentose phosphate pathway FEATURE !$6-285 #domain 3-hydroxyisobutyrate dehydrogenase homology !8#label HIB SUMMARY #length 468 #molecular-weight 51395 #checksum 6833 SEQUENCE /// ENTRY S14628 #type complete TITLE phosphogluconate dehydrogenase (decarboxylating) (EC 1.1.1.44) - Synechococcus sp. ORGANISM #formal_name Synechococcus sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S14628 REFERENCE S14628 !$#authors Culler, D.C.; Krogmann, D.W. !$#submission submitted to the EMBL Data Library, April 1991 !$#description Amino acid sequence comparisons of 6-Phosphogluconate !1Dehydrogenase. !$#accession S14628 !'##status preliminary !'##molecule_type DNA !'##residues 1-470 ##label CUL !'##cross-references EMBL:X58719; NID:g47524; PIDN:CAA41555.1; !1PID:g47525 CLASSIFICATION #superfamily phosphogluconate dehydrogenase !1(decarboxylating); 3-hydroxyisobutyrate dehydrogenase !1homology KEYWORDS oxidoreductase; pentose phosphate pathway FEATURE !$6-288 #domain 3-hydroxyisobutyrate dehydrogenase homology !8#label HIB SUMMARY #length 470 #molecular-weight 51308 #checksum 6537 SEQUENCE /// ENTRY D26190 #type complete TITLE phosphogluconate dehydrogenase (decarboxylating) (EC 1.1.1.44) gntZ - Bacillus subtilis ALTERNATE_NAMES 6-phosphogluconate dehydrogenase gntZ ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS D26190; F69636 REFERENCE A92561 !$#authors Fujita, Y.; Fujita, T.; Miwa, Y.; Nihashi, J.; Aratani, Y. !$#journal J. Biol. Chem. (1986) 261:13744-13753 !$#title Organization and transcription of the gluconate operon, gnt, !1of Bacillus subtilis. !$#cross-references MUID:87008613; PMID:3020045 !$#accession D26190 !'##molecule_type DNA !'##residues 1-468 ##label FUJ !'##cross-references GB:AB005554; GB:D45242; GB:D31629; NID:g2280496; !1PIDN:BAA21576.1; PID:g563930 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69636 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-468 ##label KUN !'##cross-references GB:Z99124; GB:AL009126; NID:g2636442; !1PIDN:CAB16045.1; PID:g2636555 !'##experimental_source strain 168 GENETICS !$#gene gntZ CLASSIFICATION #superfamily phosphogluconate dehydrogenase !1(decarboxylating); 3-hydroxyisobutyrate dehydrogenase !1homology KEYWORDS oxidoreductase; pentose phosphate pathway FEATURE !$5-284 #domain 3-hydroxyisobutyrate dehydrogenase homology !8#label HIB SUMMARY #length 468 #molecular-weight 51983 #checksum 468 SEQUENCE /// ENTRY DEHUG6 #type complete TITLE glucose-6-phosphate 1-dehydrogenase (EC 1.1.1.49) - human ALTERNATE_NAMES G6PD ORGANISM #formal_name Homo sapiens #common_name man DATE 17-Jul-1992 #sequence_revision 23-Mar-1995 #text_change 11-Jun-1999 ACCESSIONS A40309; S17292; S70771; I58283; A24935; A25756; B23949; !1I59122; I53003; A22002; A23949; JC2533; S21809 REFERENCE A40309 !$#authors Chen, E.Y.; Cheng, A.; Lee, A.; Kuang, W.J.; Hillier, L.; !1Green, P.; Schlessinger, D.; Ciccodicola, A.; D'Urso, M. !$#journal Genomics (1991) 10:792-800 !$#title Sequence of human glucose-6-phosphate dehydrogenase cloned !1in plasmids and a yeast artificial chromosome. !$#cross-references MUID:91365390; PMID:1889820 !$#accession A40309 !'##molecule_type DNA !'##residues 1-515 ##label CHE !'##cross-references EMBL:X55448; NID:g450527; PIDN:CAA39089.1; !1PID:g452269 REFERENCE S17292 !$#authors Toniolo, D.; Filippi, M.; Dono, R.; Lettieri, T.; Martini, !1G. !$#journal Gene (1991) 102:197-203 !$#title The CpG island in the 5' region of the G6PD gene of man and !1mouse. !$#cross-references MUID:91340153; PMID:1874446 !$#accession S17292 !'##molecule_type DNA !'##residues 1-40 ##label TON1 !'##cross-references EMBL:X53815; NID:g31538 !$#accession S70771 !'##molecule_type DNA !'##residues 1-15 ##label TON2 !'##cross-references EMBL:X53815; NID:g31538; PIDN:CAA37811.1; !1PID:g31539 REFERENCE I58283 !$#authors Chao, L.T.; Du, C.S.; Louie, E.; Zuo, L.; Chen, E.; Lubin, !1B.; Chiu, D.T. !$#journal Nucleic Acids Res. (1991) 19:6056 !$#title A to G substitution identified in exon 2 of the G6PD gene !1among G6PD deficient Chinese. !$#cross-references MUID:92051408; PMID:1945893 !$#accession I58283 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 30-31,'R',33-34 ##label CHA !'##cross-references GB:S64462; NID:g238727; PIDN:AAB20299.1; !1PID:g238728 !'##note variant sequence with 32-Arg REFERENCE A93611 !$#authors Persico, M.G.; Viglietto, G.; Martini, G.; Toniolo, D.; !1Paonessa, G.; Moscatelli, C.; Dono, R.; Vulliamy, T.; !1Luzzatto, L.; D'Urso, M. !$#journal Nucleic Acids Res. (1986) 14:2511-2522 !$#title Isolation of human glucose-6-phosphate dehydrogenase (G6PD) !1cDNA clones: primary structure of the protein and unusual 5' !1non-coding region. !$#cross-references MUID:86176746; PMID:3515319 !$#accession A24935 !'##molecule_type mRNA !'##residues 37-67,'V',69-125,'N',127-515 ##label PER1 !'##cross-references EMBL:X03674; NID:g31542 !'##experimental_source HeLa cells !'##note this sequence revised by A25756 REFERENCE A25756 !$#authors Persico, M.G.; Viglietto, G.; Martini, G.; Toniolo, D.; !1Paonessa, G.; Moscatelli, C.; Dono, R.; Vulliamy, T.; !1Luzzatto, L.; D'Urso, M. !$#journal Nucleic Acids Res. (1986) 14:7822 !$#title Isolation of human glucose-6-phosphate dehydrogenase (G6PD) !1cDNA clones: primary structure of the protein and unusual 5' !1non-coding region. !$#accession A25756 !'##molecule_type mRNA !'##residues 1-10,'H',12-67,'V',69-125,'N',127-515 ##label PER2 !'##cross-references EMBL:X03674; NID:g31542; PIDN:CAA27309.1; !1PID:g31543 !'##experimental_source HeLa cells REFERENCE A94101 !$#authors Takizawa, T.; Huang, I.Y.; Ikuta, T.; Yoshida, A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:4157-4161 !$#title Human glucose-6-phosphate dehydrogenase: primary structure !1and cDNA cloning. !$#cross-references MUID:86233391; PMID:3012556 !$#accession B23949 !'##molecule_type mRNA !'##residues 154-434,'EP',437-515 ##label TAK !'##cross-references GB:M12996; NID:g457135; PIDN:AAA52499.1; !1PID:g182869 REFERENCE I59122 !$#authors Hirono, A.; Beutler, E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:3951-3954 !$#title Molecular cloning and nucleotide sequence of cDNA for human !1glucose-6-phosphate dehydrogenase variant A(-). !$#cross-references MUID:88234536; PMID:2836867 !$#accession I59122 !'##status nucleic acid sequence not shown; translation not shown; !1translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-10,'H',12-515 ##label HIR !'##cross-references GB:M21248; NID:g182870; PIDN:AAA52500.1; !1PID:g182871 !'##experimental_source A(-) allelic variant REFERENCE I53003 !$#authors Kanno, H.; Kondoh, T.; Yoshida, A. !$#journal DNA Cell Biol. (1993) 12:209-215 !$#title 5' structure and expression of human glucose-6-phosphate !1dehydrogenase mRNA. !$#cross-references MUID:93221678; PMID:8466644 !$#accession I53003 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 'MGRRGSAPGNGRTLRGCERGGRRRRSADSV',1-67,'V',69-71 ##label KAN !'##cross-references GB:S58359; NID:g299498; PIDN:AAB26169.1; !1PID:g299499 REFERENCE A22002 !$#authors Descalzi-Cancedda, F.; Caruso, C.; Romano, M.; di Prisco, !1G.; Camardella, L. !$#journal Biochem. Biophys. Res. Commun. (1984) 118:332-338 !$#title Amino acid sequence of the carboxy-terminal end of human !1erythrocyte glucose-6-phosphate dehydrogenase. !$#cross-references MUID:84128051; PMID:6696761 !$#accession A22002 !'##molecule_type protein !'##residues 509-510,'D',512-515 ##label DES REFERENCE JC2533 !$#authors Camardella, L.; Damonte, G.; Carratore, V.; Benatti, U.; !1Tonetti, M.; Moneti, G. !$#journal Biochem. Biophys. Res. Commun. (1995) 207:331-338 !$#title Glucose 6-phosphate dehydrogenase from human erythrocytes: !1Identification of N-acetyl-alanine at the N-terminus of the !1mature protein. !$#cross-references MUID:95160695; PMID:7857286 !$#contents annotation; proof of N-acetyl-alanine at amino end GENETICS !$#gene GDB:G6PD !'##cross-references GDB:120621; OMIM:305900 !$#map_position Xq28-Xq28 !$#introns 40/3; 53/2; 89/3; 162/2/ 215/2; 257/2; 288/3; 351/1; 429/3; !1455/2; 486/2 !$#note this gene has a high degree of allelic variation COMPLEX homodimer; homotetramer FUNCTION !$#description catalyzes oxidation of glucose-6-phosphate to !1gluconolactone-6-phosphate using NADP+; oxidoreductase !$#pathway pentose phosphate pathway !$#note catalyzes the first reaction of the pentose phosphate !1pathway and is a major intracellular source of NADPH for !1biosynthetic and detoxification reactions !$#note a deficiency of this enzyme in erythrocytes is a cause of !1hemolytic anemia CLASSIFICATION #superfamily glucose-6-phosphate dehydrogenase KEYWORDS acetylated amino end; hereditary hemolytic anemia; !1homodimer; homotetramer; NADP; oxidoreductase; pentose !1phosphate pathway FEATURE !$2-515 #product glucose-6-phosphate 1-dehydrogenase #status !8predicted #label MAT\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental\ !$205 #active_site Lys #status predicted SUMMARY #length 515 #molecular-weight 59289 #checksum 5054 SEQUENCE /// ENTRY A56686 #type complete TITLE glucose-6-phosphate 1-dehydrogenase (EC 1.1.1.49) - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A56686; S17293; S31406 REFERENCE A56686 !$#authors Zollo, M.; D'Urso, M.; Schlessinger, D.; Chen, E.Y. !$#journal DNA Seq. (1993) 3:319-322 !$#title Sequence of mouse glucose-6-phosphate dehydrogenase cDNA. !$#cross-references MUID:94003403; PMID:8400362 !$#accession A56686 !'##status preliminary !'##molecule_type mRNA !'##residues 1-515 ##label ZOL !'##cross-references EMBL:Z11911; NID:g51113; PIDN:CAA77967.1; !1PID:g51114 REFERENCE S17292 !$#authors Toniolo, D.; Filippi, M.; Dono, R.; Lettieri, T.; Martini, !1G. !$#journal Gene (1991) 102:197-203 !$#title The CpG island in the 5' region of the G6PD gene of man and !1mouse. !$#cross-references MUID:91340153; PMID:1874446 !$#accession S17293 !'##molecule_type DNA !'##residues 1-23,'Y',25-40 ##label TON !'##cross-references EMBL:X53617; NID:g51022; PIDN:CAA37679.1; !1PID:g51023 !'##experimental_source strain BALB/C GENETICS !$#gene G6PD !$#map_position X CLASSIFICATION #superfamily glucose-6-phosphate dehydrogenase KEYWORDS oxidoreductase; pentose phosphate pathway SUMMARY #length 515 #molecular-weight 59262 #checksum 5100 SEQUENCE /// ENTRY S01233 #type complete TITLE glucose-6-phosphate 1-dehydrogenase (EC 1.1.1.49) precursor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S01233; JS0284; S07083 REFERENCE S01233 !$#authors Ho, Y.S.; Howard, A.J.; Crapo, J.D. !$#journal Nucleic Acids Res. (1988) 16:7746 !$#title Cloning and sequence of a cDNA encoding rat !1glucose-6-phosphate dehydrogenase. !$#cross-references MUID:88319984; PMID:3412913 !$#accession S01233 !'##molecule_type mRNA !'##residues 1-515 ##label HOY !'##cross-references GB:X07467; NID:g56195; PIDN:CAA30355.1; PID:g56196 !'##experimental_source liver REFERENCE JS0284 !$#authors Jeffery, J.; Soederling-Barros, J.; Murray, L.A.; Hansen, !1R.J.; Szepesi, B.; Joernvall, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:7840-7843 !$#title Molecular diversity of glucose-6-phosphate dehydrogenase: !1rat enzyme structure identifies NH2-terminal segment, shows !1initiation from sites nonequivalent in different organisms, !1and establishes otherwise extensive sequence conservation. !$#cross-references MUID:89042082; PMID:3141918 !$#accession JS0284 !'##molecule_type protein !'##residues 2-72 ##label JEF REFERENCE S07083 !$#authors Jeffery, J.; Barros-Soederling, J.; Murray, L.; Wood, I.; !1Hansen, R.; Szepesi, B.; Joernvall, H. !$#journal Eur. J. Biochem. (1989) 186:551-556 !$#title Glucose-6-phosphate dehydrogenase. Characteristics revealed !1by the rat liver enzyme structure. !$#cross-references MUID:90107986; PMID:2606104 !$#accession S07083 !'##molecule_type protein !'##residues 2-319,'D',321-514 ##label JE2 CLASSIFICATION #superfamily glucose-6-phosphate dehydrogenase KEYWORDS acetylated amino end; oxidoreductase; pentose phosphate !1pathway FEATURE !$2-515 #product glucose-6-phosphate dehydrogenase #status !8experimental #label MAT\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental SUMMARY #length 515 #molecular-weight 59375 #checksum 5915 SEQUENCE /// ENTRY DEFFG6 #type complete TITLE glucose-6-phosphate 1-dehydrogenase (EC 1.1.1.49) - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES D-glucose-6-phosphate:NADP+ oxidoreductase ORGANISM #formal_name Drosophila melanogaster DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 11-Jun-1999 ACCESSIONS JT0272; A38006 REFERENCE JT0272 !$#authors Fouts, D.; Ganguly, R.; Gutierrez, A.G.; Lucchesi, J.C.; !1Manning, J.E. !$#journal Gene (1988) 63:261-275 !$#title Nucleotide sequence of the Drosophila glucose-6-phosphate !1dehydrogenase gene and comparison with the homologous human !1gene. !$#cross-references MUID:88255872; PMID:2838391 !$#accession JT0272 !'##molecule_type genomic RNA !'##residues 1-523 ##label FOU !'##cross-references GB:M26674; NID:g157468; PIDN:AAA51463.1; !1PID:g157470 !$#accession A38006 !'##molecule_type mRNA !'##residues 1-523 ##label FOU2 !'##cross-references GB:M26674; NID:g157468; PIDN:AAA51463.1; !1PID:g157470 !'##note the authors translated the codon AAG for residue 214 as Asn COMMENT This is the first and dominant regulatory enzyme in the !1hexose monophosphate shunt. GENETICS !$#gene FlyBase:Zw !'##cross-references FlyBase:FBgn0004057 !$#introns 6/2; 94/2; 166/2 CLASSIFICATION #superfamily glucose-6-phosphate dehydrogenase KEYWORDS oxidoreductase; pentose phosphate pathway FEATURE !$209 #active_site Lys #status predicted SUMMARY #length 523 #molecular-weight 60117 #checksum 5016 SEQUENCE /// ENTRY A56841 #type complete TITLE glucose-6-phosphate 1-dehydrogenase (EC 1.1.1.49) - Japanese pufferfish ORGANISM #formal_name Fugu rubripes #common_name Japanese pufferfish DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A56841 REFERENCE A56841 !$#authors Mason, P.J.; Stevens, D.J.; Luzzatto, L.; Brenner, S.; !1Aparicio, S. !$#journal Genomics (1995) 26:587-591 !$#title Genomic structure and sequence of the Fugu rubripes !1glucose-6-phosphate dehydrogenase gene (G6PD). !$#cross-references MUID:95331796; PMID:7607684 !$#accession A56841 !'##status preliminary !'##molecule_type DNA !'##residues 1-530 ##label MAS !'##cross-references GB:X83611; NID:g619454; PIDN:CAA58590.2; !1PID:g5459313 !'##note authors translated the codon GCG for residue 469 as Arg, AGT !1for residue 470 as Gly, and AGT for residue 501 as Arg GENETICS !$#introns 55/3; 68/2; 104/3; 177/2; 230/2; 272/2; 303/3; 366/1; 444/3; !1470/2; 501/2 CLASSIFICATION #superfamily glucose-6-phosphate dehydrogenase KEYWORDS oxidoreductase SUMMARY #length 530 #molecular-weight 60469 #checksum 4788 SEQUENCE /// ENTRY DEYCG6 #type complete TITLE glucose-6-phosphate 1-dehydrogenase (EC 1.1.1.49) - Synechococcus sp. (strain PCC 7942) ORGANISM #formal_name Synechococcus sp. DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 11-Jun-1999 ACCESSIONS S23520; S19897 REFERENCE S23520 !$#authors Scanlan, D.J.; Newman, J.; Sebaihia, M.; Mann, N.H.; Carr, !1N.G. !$#journal Plant Mol. Biol. (1992) 19:877-880 !$#title Cloning and sequence analysis of the glucose-6-phosphate !1dehydrogenase gene from the cyanobacterium Synechococcus PCC !17942. !$#cross-references MUID:92353398; PMID:1643289 !$#accession S23520 !'##molecule_type DNA !'##residues 1-524 ##label SCA !'##cross-references GB:U33285; EMBL:X64768; NID:g988284; !1PIDN:AAA98847.1; PID:g988286 GENETICS !$#gene zwf CLASSIFICATION #superfamily glucose-6-phosphate dehydrogenase KEYWORDS NAD; oxidoreductase; pentose phosphate pathway FEATURE !$202 #active_site Lys #status predicted SUMMARY #length 524 #molecular-weight 59023 #checksum 1200 SEQUENCE /// ENTRY S13744 #type complete TITLE glucose-6-phosphate 1-dehydrogenase (EC 1.1.1.49) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein N1110; protein YNL241c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S13744; JQ0890; A33126; S16814; A61430; A21823; S12509; !1S63207; S67357; S72075; S12948 REFERENCE S13744 !$#authors Thomas, D.; Cherest, H.; Surdin-Kerjan, Y. !$#journal EMBO J. (1991) 10:547-553 !$#title Identification of the structural gene for !1glucose-6-phosphate dehydrogenase in yeast. Inactivation !1leads to a nutritional requirement for organic sulfur. !$#cross-references MUID:91160508; PMID:2001672 !$#accession S13744 !'##molecule_type DNA !'##residues 1-505 ##label THO !'##cross-references EMBL:X57336; NID:g3925; PIDN:CAA40611.1; PID:g3926 REFERENCE JQ0890 !$#authors Nogae, I.; Johnston, M. !$#journal Gene (1990) 96:161-169 !$#title Isolation and characterization of the ZWF1 gene of !1Saccharomyces cerevisiae, encoding glucose-6-phosphate !1dehydrogenase. !$#cross-references MUID:91099671; PMID:2269430 !$#accession JQ0890 !'##molecule_type DNA !'##residues 1-174,'A',176-505 ##label NOG1 !'##cross-references GB:M34709; NID:g171543; PIDN:AAA34619.1; !1PID:g171545 REFERENCE A33126 !$#authors Nogae, I.; Johnston, M. !$#submission submitted to the Protein Sequence Database, September 1990 !$#accession A33126 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-174,'A',176-505 ##label NOG2 REFERENCE S16814 !$#authors Persson, B.; Joernvall, H.; Wood, I.; Jeffery, J. !$#journal Eur. J. Biochem. (1991) 198:485-491 !$#title Functionally important regions of glucose-6-phosphate !1dehydrogenase defined by the Saccharomyces cerevisiae enzyme !1and its differences from the mammalian and insect forms. !$#cross-references MUID:91249846; PMID:2040308 !$#accession S16814 !'##molecule_type protein !'##residues 2-57,59-505 ##label PER REFERENCE A61430 !$#authors Bergman, T.; Joernvall, H.; Wood, I.; Jeffery, J. !$#journal J. Protein Chem. (1991) 10:25-29 !$#title Eukaryotic glucose-6-phosphate dehydrogenases: structural !1screening of related proteins. !$#cross-references MUID:91273757; PMID:2054059 !$#accession A61430 !'##molecule_type protein !'##residues 59-72,'X',74,'X',76;88-108,'X',110-113,'X', !1115-118;260-279;'X',340-365,'X',367-373 ##label BER REFERENCE A21823 !$#authors Jeffery, J.; Hobbs, L.; Jornvall, H. !$#journal Biochemistry (1985) 24:666-671 !$#title Glucose-6-phosphate dehydrogenase from Saccharomyces !1cerevisiae: characterization of a reactive lysine residue !1labeled with acetylsalicylic acid. !$#cross-references MUID:85199795; PMID:3922403 !$#accession A21823 !'##molecule_type protein !'##residues 185-195 ##label JEF REFERENCE S11074 !$#authors Egestad, B.; Estonius, M.; Danielsson, O.; Persson, B.; !1Cederlund, E.; Kaiser, R.; Holmquist, B.; Vallee, B.; Pares, !1X.; Jefferey, J.; Joernvall, H. !$#journal FEBS Lett. (1990) 269:194-196 !$#title Fast atom bombardment mass spectrometry and chemical !1analysis in determinations of acyl-blocked protein !1structures. !$#cross-references MUID:90353571; PMID:2387402 !$#accession S12509 !'##molecule_type protein !'##residues 1-3,'VP',6 ##label EGE REFERENCE S63188 !$#authors Pandolfo, D.; De Antoni, A.; Lanfranchi, G.; Valle, G. !$#submission submitted to the Protein Sequence Database, April 1996 !$#accession S63207 !'##molecule_type DNA !'##residues 1-505 ##label PAN !'##cross-references EMBL:Z71517; NID:g1302275; PIDN:CAA96146.1; !1PID:g1302276; GSPDB:GN00014; MIPS:YNL241c !'##experimental_source strain S288C REFERENCE S67355 !$#authors Pandolfo, D.; de Antoni, A.; Lanfranchi, G.; Valle, G. !$#submission submitted to the EMBL Data Library, February 1996 !$#description DNA sequence of cosmid 14-5 from chromosome XIV. !$#accession S67357 !'##molecule_type DNA !'##residues 1-505 ##label PAW !'##cross-references EMBL:Z69381; NID:g1183970; PIDN:CAA93357.1; !1PID:g1183973 REFERENCE S72073 !$#authors Pandolfo, D.; de Antoni, A.; Lanfranchi, G.; Valle, G. !$#journal Yeast (1996) 12:1071-1076 !$#title The DNA sequence of cosmid 14-5 from chromosome XIV reveals !121 open reading frames including a novel gene encoding a !1globin-like domain. !$#cross-references MUID:97051596; PMID:8896273 !$#accession S72075 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-505 ##label PAF !'##cross-references EMBL:Z69381; NID:g1183970; PIDN:CAA93357.1; !1PID:g1183973 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1February 1996 GENETICS !$#gene SGD:ZWF1; MET19; MIPS:YNL241c !'##cross-references MIPS:YNL241c; SGD:S0005185 !$#map_position 14L !$#note YNL241c FUNCTION !$#pathway pentose phosphate pathway !$#note first step CLASSIFICATION #superfamily glucose-6-phosphate dehydrogenase KEYWORDS acetylated amino end; blocked amino end; NADP; !1oxidoreductase; pentose phosphate pathway FEATURE !$2-505 #product glucose-6-phosphate 1-dehydrogenase #status !8experimental #label MAT\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental\ !$191 #active_site Lys #status predicted SUMMARY #length 505 #molecular-weight 57521 #checksum 9643 SEQUENCE /// ENTRY S31337 #type complete TITLE glucose-6-phosphate 1-dehydrogenase (EC 1.1.1.49) - yeast (Kluyveromyces marxianus var. lactis) ORGANISM #formal_name Kluyveromyces marxianus var. lactis, Candida sphaerica DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S31337 REFERENCE S31336 !$#authors Wesolowski-Louvel, M.; Tanguy-Rougeau, C.; Fukuhau, H. !$#submission submitted to the EMBL Data Library, February 1993 !$#accession S31337 !'##molecule_type DNA !'##residues 1-497 ##label WES !'##cross-references EMBL:X70373; NID:g5537; PIDN:CAA49834.1; PID:g5539 CLASSIFICATION #superfamily glucose-6-phosphate dehydrogenase KEYWORDS oxidoreductase SUMMARY #length 497 #molecular-weight 56574 #checksum 8329 SEQUENCE /// ENTRY S54720 #type complete TITLE glucose-6-phosphate 1-dehydrogenase (EC 1.1.1.49) - Aspergillus niger ORGANISM #formal_name Aspergillus niger DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS S54720; S57485 REFERENCE S54720 !$#authors van den Broek, P.; Goosen, T.; Wennekes, B.; van den Broek, !1H. !$#journal Mol. Gen. Genet. (1995) 247:229-239 !$#title Isolation and characterization of the glucose-6-phosphate !1dehydrogenase encoding gene (gsdA) from Aspergillus niger. !$#cross-references MUID:95272533; PMID:7753033 !$#accession S54720 !'##molecule_type DNA !'##residues 1-511 ##label VAN !'##cross-references GB:X77829; NID:g1523781 !'##experimental_source strain N400 !'##note mRNA sequencing confirmed exon/intron boundaries !'##note the sequence in GenBank entry ANNGSDA, release 114, !1(PIDN:CAA54840.1) has 15-Gly rather than the published !115-Val REFERENCE S57485 !$#authors Thamm, A. !$#submission submitted to the EMBL Data Library, June 1995 !$#description G6PD-promoter activity in A. niger. !$#accession S57485 !'##molecule_type mRNA !'##residues 1-14,'G',16-134,'L',136-507,'NRL' ##label THA !'##cross-references EMBL:X87942; NID:g870830; PIDN:CAA61194.1; !1PID:g870831 GENETICS !$#gene gsdA !$#introns 15/2; 39/3; 46/3; 161/3; 227/3; 256/1; 281/3; 351/1; 475/1 CLASSIFICATION #superfamily glucose-6-phosphate dehydrogenase KEYWORDS NADP; oxidoreductase; pentose phosphate pathway SUMMARY #length 511 #molecular-weight 59074 #checksum 5314 SEQUENCE /// ENTRY S57785 #type complete TITLE glucose-6-phosphate 1-dehydrogenase (EC 1.1.1.49) - alfalfa ORGANISM #formal_name Medicago sativa #common_name alfalfa DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S57785 REFERENCE S57785 !$#authors Fahrendorf, T.; Ni, W.; Shorrosh, B.S.; Dixon, R.A. !$#journal Plant Mol. Biol. (1995) 28:885-900 !$#title Stress responses in alfalfa (Medicago sativa L.) XIX. !1Transcriptional activation of oxidative pentose phosphate !1pathway genes at the onset of the isoflavonoid phytoalexin !1response. !$#cross-references MUID:95367649; PMID:7640360 !$#accession S57785 !'##status preliminary !'##molecule_type mRNA !'##residues 1-515 ##label FAH !'##cross-references EMBL:U18238; NID:g603218; PIDN:AAB41552.1; !1PID:g603219 CLASSIFICATION #superfamily glucose-6-phosphate dehydrogenase KEYWORDS oxidoreductase; pentose phosphate pathway SUMMARY #length 515 #molecular-weight 58923 #checksum 9237 SEQUENCE /// ENTRY S60287 #type complete TITLE glucose-6-phosphate 1-dehydrogenase (EC 1.1.1.49) - potato ORGANISM #formal_name Solanum tuberosum #common_name potato DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S60287 REFERENCE S60287 !$#authors Graeve, K.; von Schaewen, A.; Scheibe, R. !$#journal Plant J. (1994) 5:353-361 !$#title Purification, characterization, and cDNA sequence of !1glucose-6-phosphate dehydrogenase from potato (Solanum !1tuberosum L.). !$#cross-references MUID:94236152; PMID:8180621 !$#accession S60287 !'##status preliminary !'##molecule_type mRNA !'##residues 1-511 ##label GRA !'##cross-references EMBL:X74421; NID:g471344; PIDN:CAA52442.1; !1PID:g471345 CLASSIFICATION #superfamily glucose-6-phosphate dehydrogenase KEYWORDS oxidoreductase SUMMARY #length 511 #molecular-weight 58470 #checksum 1052 SEQUENCE /// ENTRY B37855 #type complete TITLE glucose-6-phosphate 1-dehydrogenase (EC 1.1.1.49) - Zymomonas mobilis ORGANISM #formal_name Zymomonas mobilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B37855 REFERENCE A37855 !$#authors Barnell, W.O.; Yi, K.C.; Conway, T. !$#journal J. Bacteriol. (1990) 172:7227-7240 !$#title Sequence and genetic organization of a Zymomonas mobilis !1gene cluster that encodes several enzymes of glucose !1metabolism. !$#cross-references MUID:91072278; PMID:2254282 !$#accession B37855 !'##status preliminary !'##molecule_type DNA !'##residues 1-485 ##label BAR !'##cross-references GB:M60615; GB:M37982; NID:g155589; PIDN:AAA27692.1; !1PID:g155591 CLASSIFICATION #superfamily glucose-6-phosphate dehydrogenase KEYWORDS oxidoreductase SUMMARY #length 485 #molecular-weight 53859 #checksum 1071 SEQUENCE /// ENTRY D64947 #type complete TITLE glucose-6-phosphate 1-dehydrogenase (EC 1.1.1.49) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS D64947; A38174; S35910; I81198; I81204; I81206; I81205; !1I81197; I81195; I81196; I81199; I81203; I81200; I81202; !1I81201 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64947 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-491 ##label BLAT !'##cross-references GB:AE000279; GB:U00096; NID:g1788154; !1PIDN:AAC74922.1; PID:g1788158; UWGP:b1852 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A38174 !$#authors Rowley, D.L.; Wolf Jr., R.E. !$#journal J. Bacteriol. (1991) 173:968-977 !$#title Molecular characterization of the Escherichia coli K-12 zwf !1gene encoding glucose 6-phosphate dehydrogenase. !$#cross-references MUID:91123224; PMID:1704005 !$#accession A38174 !'##status preliminary !'##molecule_type DNA !'##residues 1-267,'PEVSSPH',276,'PLQ',280,'TRKN',285,'TRAIYCVP',294-491 !1##label ROW !'##cross-references GB:M55005; NID:g148285; PIDN:AAA24775.1; !1PID:g148286 !'##note the authors translated the codon GCG for residue 2 as Val REFERENCE S35910 !$#authors Carter, A.T. !$#submission submitted to the EMBL Data Library, January 1992 !$#accession S35910 !'##molecule_type DNA !'##residues 321-491 ##label CAR !'##cross-references EMBL:X63694; NID:g395401; PIDN:CAA45220.1; !1PID:g395402 !'##experimental_source strain K-12 REFERENCE I59590 !$#authors Guttman, D.S.; Dykhuizen, D.E. !$#journal Science (1994) 266:1380-1383 !$#title Clonal divergence in Escherichia coli is driven by !1recombination, not mutation. !$#cross-references MUID:95064015; PMID:7973728 !$#accession I81198 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 72-368 ##label RES !'##cross-references EMBL:U13786; NID:g535549; PIDN:AAA57021.1; !1PID:g600738 !'##experimental_source strain 65 !$#accession I81204 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 72-368 ##label RE2 !'##cross-references EMBL:U13792; NID:g535561; PIDN:AAA57027.1; !1PID:g600744 !'##experimental_source strain ECOR16 !$#accession I81206 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 72-368 ##label RE3 !'##cross-references EMBL:U13794; NID:g535565; PIDN:AAA57029.1; !1PID:g600746 !'##experimental_source strain ECOR38 !$#accession I81205 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 72-368 ##label RE4 !'##cross-references EMBL:U13793; NID:g535563; PIDN:AAA57028.1; !1PID:g600745 !'##experimental_source strain ECOR39 !$#accession I81197 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 72-368 ##label RE5 !'##cross-references EMBL:U13785; NID:g535547; PIDN:AAA57020.1; !1PID:g600737 !'##experimental_source strain ECOR40 !$#accession I81195 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 72-368 ##label RE6 !'##cross-references EMBL:U13783; NID:g535543; PIDN:AAA57018.1; !1PID:g600735 !'##experimental_source strain ECOR49 !$#accession I81196 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 72-368 ##label RE7 !'##cross-references EMBL:U13784; NID:g535545; PIDN:AAA57019.1; !1PID:g600736 !'##experimental_source strain ECOR50 !$#accession I81199 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 72-368 ##label RE8 !'##cross-references EMBL:U13787; NID:g535551; PIDN:AAA57022.1; !1PID:g600739 !'##experimental_source strain ECOR68 !$#accession I81203 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 72-368 ##label RE9 !'##cross-references EMBL:U13791; NID:g535559; PIDN:AAA57026.1; !1PID:g600743 !'##experimental_source strain ECOR8 !$#accession I81200 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 72-368 ##label R10 !'##cross-references EMBL:U13788; NID:g535553; PIDN:AAA57023.1; !1PID:g600740 !'##experimental_source strain K-12 !$#accession I81202 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 72-368 ##label R11 !'##cross-references EMBL:U13790; NID:g535557; PIDN:AAA57025.1; !1PID:g600742 !'##experimental_source strain ECOR10 !$#accession I81201 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 72-368 ##label R12 !'##cross-references EMBL:U13789; NID:g535555; PIDN:AAA57024.1; !1PID:g600741 !'##experimental_source strain ECOR4 GENETICS !$#gene zwf !$#map_position 41 min FUNCTION !$#description catalyzes reduction of glucose-6-phosphate to gluconolactone !16-phosphate !$#pathway pentose phosphate pathway CLASSIFICATION #superfamily glucose-6-phosphate dehydrogenase KEYWORDS NADP; oxidoreductase; pentose phosphate pathway FEATURE !$181 #active_site Lys #status predicted SUMMARY #length 491 #molecular-weight 55704 #checksum 4572 SEQUENCE /// ENTRY A39864 #type complete TITLE glucose-6-phosphate 1-dehydrogenase (EC 1.1.1.49) - Leuconostoc mesenteroides ORGANISM #formal_name Leuconostoc mesenteroides DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A39864; A29027 REFERENCE A39864 !$#authors Lee, W.T.; Flynn, T.G.; Lyons, C.; Levy, H.R. !$#journal J. Biol. Chem. (1991) 266:13028-13034 !$#title Cloning of the gene and amino acid sequence for glucose !16-phosphate dehydrogenase from Leuconostoc mesenteroides. !$#cross-references MUID:91302321; PMID:2071589 !$#accession A39864 !'##molecule_type DNA !'##residues 1-486 ##label LEE !'##cross-references GB:M64446; NID:g149630; PIDN:AAA25265.1; !1PID:g149631 REFERENCE A29027 !$#authors Bhadbhade, M.M.; Adams, M.J.; Flynn, T.G.; Levy, H.R. !$#journal FEBS Lett. (1987) 211:243-246 !$#title Sequence identity between a lysine-containing peptide from !1Leuconostoc mesenteroides glucose-6-phosphate dehydrogenase !1and an active site peptide from human erythrocyte !1glucose-6-phosphate dehydrogenase. !$#cross-references MUID:87105980; PMID:3100332 !$#accession A29027 !'##molecule_type protein !'##residues 147-153,'H',155,'I',157-164,'F',166-188 ##label BHA CLASSIFICATION #superfamily glucose-6-phosphate dehydrogenase KEYWORDS oxidoreductase; pentose phosphate pathway SUMMARY #length 486 #molecular-weight 54441 #checksum 5490 SEQUENCE /// ENTRY DEEC #type complete TITLE acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) / alcohol dehydrogenase (EC 1.1.1.1) [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES acetaldehyde/alcohol dehydrogenase; AdhE; aldehyde reductase CONTAINS pyruvate-formate-lyase deactivase ORGANISM #formal_name Escherichia coli DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 01-Mar-2002 ACCESSIONS JS0406; S14809; I76913; D64871; S23871 REFERENCE JS0406 !$#authors Goodlove, P.E.; Cunningham, P.R.; Parker, J.; Clark, D.P. !$#journal Gene (1989) 85:209-214 !$#title Cloning and sequence analysis of the fermentative !1alcohol-dehydrogenase-encoding gene of Escherichia coli. !$#cross-references MUID:90152365; PMID:2695398 !$#accession JS0406 !'##molecule_type DNA !'##residues 1-891 ##label GOO !'##cross-references GB:M33504; NID:g145205; PIDN:AAA23420.1; !1PID:g145206 !'##experimental_source plasmid pHIL8 !'##note residues 2-11 were confirmed by protein sequencing REFERENCE S14809 !$#authors Kessler, D.; Leibrecht, I.; Knappe, J. !$#journal FEBS Lett. (1991) 281:59-63 !$#title Pyruvate-formate-lyase-deactivase and acetyl-CoA reductase !1activities of Escherichia coli reside on a polymeric protein !1particle encoded by adhE. !$#cross-references MUID:91200315; PMID:2015910 !$#accession S14809 !'##molecule_type DNA !'##residues 1-891 ##label KES !'##cross-references EMBL:X59263; NID:g40899; PIDN:CAA41955.1; !1PID:g40900 !'##note only nucleotide sequences flanking the coding region are shown !'##note enzyme assays demonstrated stimulation by ferrous ion when !1either acetyl-CoA or acetaldehyde were substrates REFERENCE I57117 !$#authors Danchin, A.; Krin, E. !$#journal Microbiology (1995) 141:959-960 !$#title Filling the gap between hns and adhE in Escherichia coli !1K12. !$#cross-references MUID:95291445; PMID:7773397 !$#accession I76913 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 849-891 ##label DAN !'##cross-references EMBL:X67326; NID:g43077; PIDN:CAA47743.1; !1PID:g43081 !'##note submitted to the EMBL Data Library, July 1992 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64871 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-891 ##label BLAT !'##cross-references GB:AE000222; GB:U00096; NID:g1787486; !1PIDN:AAC74323.1; PID:g1787493; UWGP:b1241 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene adhE COMPLEX homomultimer containing more than 40 chains FUNCTION AADH !$#description catalyzes the reduction of acetyl-CoA to enzyme-bound !1thiohemiacetal using NADH !$#pathway anaerobic glucose fermentation !$#note operates only in the absence of nitrate FUNCTION ARD !$#description catalyzes the reduction of the thiohemiacetal to ethanol !1using NADH !$#pathway anaerobic glucose fermentation !$#note operates only in the absence of nitrate; generates ethanol !1and NAD+ CLASSIFICATION #superfamily acetaldehyde/alcohol dehydrogenase; aldehyde !1dehydrogenase homology; lactaldehyde reductase homology KEYWORDS alcohol metabolism; coenzyme A; homomultimer; iron; !1multifunctional enzyme; NAD; oxidoreductase FEATURE !$2-891 #product acetaldehyde/alcohol dehydrogenase #status !8predicted #label MAT\ !$8-266 #domain aldehyde dehydrogenase homology #link AADH !8#label ALDD\ !$454-858 #domain lactaldehyde reductase homology #link ARD !8#label LAR\ !$246 #active_site Cys #link AADH #status predicted SUMMARY #length 891 #molecular-weight 96126 #checksum 989 SEQUENCE /// ENTRY A49346 #type complete TITLE aldehyde dehydrogenase (NAD) (EC 1.2.1.3) / alcohol dehydrogenase (EC 1.1.1.1) E - Clostridium acetobutylicum ALTERNATE_NAMES AdhE; aldehyde reductase; aldehyde/alcohol dehydrogenase ORGANISM #formal_name Clostridium acetobutylicum DATE 03-May-1994 #sequence_revision 21-Jan-1997 #text_change 03-Jun-2002 ACCESSIONS A49346; A36972; S33434 REFERENCE A49346 !$#authors Fischer, R.J.; Helms, J.; Duerre, P. !$#journal J. Bacteriol. (1993) 175:6959-6969 !$#title Cloning, sequencing, and molecular analysis of the sol !1operon of Clostridium acetobutylicum, a chromosomal locus !1involved in solventogenesis. !$#cross-references MUID:94042861; PMID:8226639 !$#accession A49346 !'##molecule_type DNA !'##residues 1-862 ##label FIS !'##cross-references EMBL:X72831; NID:g298080; PIDN:CAA51344.1; !1PID:g298083 !'##experimental_source strain DSM 792 REFERENCE A36972 !$#authors Nair, R.V.; Bennett, G.N.; Papoutsakis, E.T. !$#journal J. Bacteriol. (1994) 176:871-885 !$#title Molecular characterization of an aldehyde/alcohol !1dehydrogenase gene from Clostridium acetobutylicum ATCC 824. !$#cross-references MUID:94131967; PMID:8300540 !$#accession A36972 !'##molecule_type DNA !'##residues 1-856,'FVLKNNLKPSYFNYFL' ##label NAI !'##cross-references GB:L14817; NID:g456558; PID:g456560 !'##experimental_source ATCC 824 GENETICS !$#gene adhE; aad FUNCTION ADH !$#description catalyzes the reversible reduction of an acid to an aldehyde !1using NADH !$#note may be specific for butyric acid FUNCTION ARD !$#description catalyzes the reversible reduction of an aldehyde to an !1alcohol using NADH !$#note may be specific for butanal; formation of butanol with !1generation of NAD+ is induced at the end of exponential !1growth CLASSIFICATION #superfamily acetaldehyde/alcohol dehydrogenase; aldehyde !1dehydrogenase homology; lactaldehyde reductase homology KEYWORDS alcohol metabolism; multifunctional enzyme; NAD; !1oxidoreductase FEATURE !$8-264 #domain aldehyde dehydrogenase homology #link ADH !8#label ALDD\ !$452-854 #domain lactaldehyde reductase homology #link ARD !8#label LAR\ !$244 #active_site Cys #link ARD #status predicted SUMMARY #length 862 #molecular-weight 95320 #checksum 6691 SEQUENCE /// ENTRY S53319 #type complete TITLE acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) / alcohol dehydrogenase (EC 1.1.1.1) - Entamoeba histolytica ALTERNATE_NAMES acetaldehyde/alcohol dehydrogenase; ADH2; aldehyde reductase ORGANISM #formal_name Entamoeba histolytica DATE 15-Jul-1995 #sequence_revision 21-Jan-1997 #text_change 05-May-2000 ACCESSIONS S53319; S62071; S41377 REFERENCE S53319 !$#authors Bruchhaus, I.; Tannich, E. !$#journal Biochem. J. (1994) 303:743-748 !$#title Purification and molecular characterization of the NAD !1(+)-dependent acetaldehyde/alcohol dehydrogenase from !1Entamoeba histolytica. !$#cross-references MUID:95071285; PMID:7980441 !$#accession S53319 !'##status nucleic acid sequence not shown !'##molecule_type mRNA; DNA !'##residues 1-872 ##label BRU !'##cross-references EMBL:X77132; NID:g443984; PIDN:CAA54388.1; !1PID:g443985 !$#accession S62071 !'##molecule_type protein !'##residues 2-5 ##label BRW GENETICS !$#gene ADH2 COMPLEX homomultimer containing more than 20 chains FUNCTION AADH !$#description catalyzes the reduction of acetyl-CoA to enzyme-bound !1thiohemiacetal using NADH !$#pathway anaerobic glucose fermentation FUNCTION ARD !$#description catalyzes the reduction of the thiohemiacetal to ethanol !1using NADH !$#pathway anaerobic glucose fermentation !$#note generates ethanol and NAD+ CLASSIFICATION #superfamily acetaldehyde/alcohol dehydrogenase; aldehyde !1dehydrogenase homology; lactaldehyde reductase homology KEYWORDS alcohol metabolism; blocked amino end; coenzyme A; !1homomultimer; multifunctional enzyme; NAD; oxidoreductase FEATURE !$2-872 #product acetaldehyde/alcohol dehyrogenase #status !8predicted #label MAT\ !$14-274 #domain aldehyde dehydrogenase homology #link AADH !8#label ALDD\ !$467-864 #domain lactaldehyde reductase homology #link ARD !8#label LAR\ !$2 #modified_site blocked amino end (Asn) (in mature !8form) #status experimental\ !$254 #active_site Cys #link AADH #status predicted SUMMARY #length 872 #molecular-weight 95871 #checksum 2250 SEQUENCE /// ENTRY S75881 #type complete TITLE glycerol dehydrogenase (EC 1.1.1.6) - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein slr1167 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S75881 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75881 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-385 ##label KAN !'##cross-references EMBL:D90913; GB:AB001339; NID:g1653348; !1PIDN:BAA18340.1; PID:g1653426 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily glycerol dehydrogenase; lactaldehyde reductase !1homology KEYWORDS oxidoreductase FEATURE !$14-362 #domain lactaldehyde reductase homology #label LAR SUMMARY #length 385 #molecular-weight 41188 #checksum 8975 SEQUENCE /// ENTRY E64793 #type complete TITLE glycerol dehydrogenase (EC 1.1.1.6) ybdH - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS E64793 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64793 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-362 ##label BLAT !'##cross-references GB:AE000165; GB:U00096; NID:g1786808; !1PIDN:AAC73700.1; PID:g1786815; UWGP:b0599 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ybdH CLASSIFICATION #superfamily glycerol dehydrogenase; lactaldehyde reductase !1homology KEYWORDS oxidoreductase; transmembrane protein FEATURE !$9-354 #domain lactaldehyde reductase homology #label LAR\ !$109-125 #domain transmembrane #status predicted #label TMM SUMMARY #length 362 #molecular-weight 39091 #checksum 8562 SEQUENCE /// ENTRY D65201 #type complete TITLE glycerol dehydrogenase (EC 1.1.1.6) gldA - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS D65201 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65201 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-380 ##label BLAT !'##cross-references GB:AE000468; GB:U00096; NID:g1790374; !1PIDN:AAC76927.1; PID:g1790381; UWGP:b3945 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene gldA CLASSIFICATION #superfamily glycerol dehydrogenase; lactaldehyde reductase !1homology KEYWORDS oxidoreductase FEATURE !$18-365 #domain lactaldehyde reductase homology #label LAR SUMMARY #length 380 #molecular-weight 40057 #checksum 6928 SEQUENCE /// ENTRY JQ1474 #type complete TITLE glycerol dehydrogenase (EC 1.1.1.6) [validated] - Bacillus stearothermophilus ORGANISM #formal_name Bacillus stearothermophilus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 26-May-2000 ACCESSIONS JQ1474; S38514 REFERENCE JQ1474 !$#authors Mallinder, P.R.; Pritchard, A.; Moir, A. !$#journal Gene (1992) 110:9-16 !$#title Cloning and characterization of a gene from Bacillus !1stearothermophilus var. non-diastaticus encoding a glycerol !1dehydrogenase. !$#cross-references MUID:92184120; PMID:1339360 !$#accession JQ1474 !'##molecule_type DNA !'##residues 1-370 ##label MAL !'##cross-references GB:M65289; NID:g142976; PIDN:AAA22477.1; !1PID:g142978 !'##experimental_source strain var. non-diastaticus REFERENCE S38514 !$#authors Paine, L.J.; Perry, N.; Popplewell, A.G.; Gore, M.G.; !1Atkinson, T. !$#journal Biochim. Biophys. Acta (1993) 1202:235-243 !$#title The identification of a lysine residue reactive to !1pyridoxal-5-phosphate in the glycerol dehydrogenase from the !1thermophile Bacillus stearothermophilus. !$#cross-references MUID:94002255; PMID:8399385 !$#accession S38514 !'##status preliminary !'##molecule_type protein !'##residues 84-87,'T',89-99,'N',101-103 ##label PAI GENETICS !$#gene gldA FUNCTION !$#description EC 1.1.1.6 [validated, MUID:92184120]; catalyzes the !1conversion of glycerol to dihydroxyacetone CLASSIFICATION #superfamily glycerol dehydrogenase; lactaldehyde reductase !1homology KEYWORDS oxidoreductase FEATURE !$7-354 #domain lactaldehyde reductase homology #label LAR SUMMARY #length 370 #molecular-weight 39501 #checksum 2375 SEQUENCE /// ENTRY RDECLA #type complete TITLE lactaldehyde reductase (EC 1.1.1.77) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 01-Mar-2002 ACCESSIONS A32883; A33495; S30352; C65062; JV0034; S04702 REFERENCE A32883 !$#authors Conway, T.; Ingram, L.O. !$#journal J. Bacteriol. (1989) 171:3754-3759 !$#title Similarity of Escherichia coli propanediol oxidoreductase !1(fucO product) and an unusual alcohol dehydrogenase from !1Zymomonas mobilis and Saccharomyces cerevisiae. !$#cross-references MUID:89291720; PMID:2661535 !$#accession A32883 !'##molecule_type DNA !'##residues 1-383 ##label CON !'##cross-references GB:M27177; NID:g146044; PIDN:AAA23825.1; !1PID:g146045 REFERENCE A33495 !$#authors Chen, Y.M.; Lu, Z.; Lin, E.C.C. !$#journal J. Bacteriol. (1989) 171:6097-6105 !$#title Constitutive activation of the fucAO operon and silencing of !1the divergently transcribed fucPIK operon by an IS5 element !1in Escherichia coli mutants selected for growth on L-1, !12-propanediol. !$#cross-references MUID:90036697; PMID:2553671 !$#accession A33495 !'##molecule_type DNA !'##residues 1-383 ##label CHE !'##cross-references GB:M31059; NID:g146040; PIDN:AAA23824.1; !1PID:g146043 REFERENCE S30351 !$#authors Shao, Z.Q.; Newman, E.B. !$#journal Eur. J. Biochem. (1993) 212:777-784 !$#title Sequencing and characterization of the sdaB gene from !1Escherichia coli K-12. !$#cross-references MUID:93215657; PMID:8385012 !$#accession S30352 !'##status preliminary !'##molecule_type DNA !'##residues 353-383 ##label SHA !'##cross-references EMBL:L07763 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65062 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-383 ##label BLAT !'##cross-references GB:AE000363; GB:U00096; NID:g1789153; !1PIDN:AAC75841.1; PID:g1789163; UWGP:b2799 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene fucO !$#map_position 60 min FUNCTION !$#description catalyzes the reduction of lactaldehyde to propane-1,2-diol !1using NADH !$#pathway anaerobic L-fucose catabolism CLASSIFICATION #superfamily lactaldehyde reductase; lactaldehyde reductase !1homology KEYWORDS iron; metalloprotein; NAD; oxidoreductase FEATURE !$6-379 #domain lactaldehyde reductase homology #label LAR\ !$15-20 #region NAD-binding motif\ !$260-278 #region iron binding #status predicted SUMMARY #length 383 #molecular-weight 40644 #checksum 9399 SEQUENCE /// ENTRY S47810 #type complete TITLE probable alcohol dehydrogenase (EC 1.1.1.1) - Escherichia coli (strain K-12) ALTERNATE_NAMES orf f382 ORGANISM #formal_name Escherichia coli DATE 27-Jan-1995 #sequence_revision 21-Jan-1997 #text_change 01-Mar-2002 ACCESSIONS S47810; A57259; G65158 REFERENCE S47666 !$#authors Plunkett, G. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S47810 !'##molecule_type DNA !'##residues 1-382 ##label PLU !'##cross-references EMBL:U00039; NID:g466582; PIDN:AAB18566.1; !1PID:g466727 REFERENCE A57259 !$#authors Xu, J.; Johnson, R.C. !$#journal J. Bacteriol. (1995) 177:3166-3175 !$#title aldB, an RpoS-dependent gene in Escherichia coli encoding an !1aldehyde dehydrogenase that is repressed by Fis and !1activated by Crp. !$#cross-references MUID:95286498; PMID:7768815 !$#accession A57259 !'##molecule_type DNA !'##residues 336-379,'R',380-381,'M' ##label XUA !'##cross-references GB:L40742; NID:g712824; PIDN:AAC36938.1; !1PID:g862623 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65158 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-382 ##label BLAT !'##cross-references GB:AE000436; GB:U00096; NID:g2367246; !1PIDN:AAC76613.1; PID:g1790015; UWGP:b3589 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yiaY !$#map_position 76-81.5 minutes !$#note between aldB and selB CLASSIFICATION #superfamily lactaldehyde reductase; lactaldehyde reductase !1homology KEYWORDS alcohol metabolism; metalloprotein; NAD; oxidoreductase FEATURE !$6-379 #domain lactaldehyde reductase homology #label LAR SUMMARY #length 382 #molecular-weight 40220 #checksum 9523 SEQUENCE /// ENTRY A25978 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) 2 - Zymomonas mobilis ORGANISM #formal_name Zymomonas mobilis DATE 05-Oct-1988 #sequence_revision 21-Jan-1997 #text_change 01-Dec-2000 ACCESSIONS A25978; S07584; B24801; T33729 REFERENCE A25978 !$#authors Conway, T.; Sewell, G.W.; Osman, Y.A.; Ingram, L.O. !$#journal J. Bacteriol. (1987) 169:2591-2597 !$#title Cloning and sequencing of the alcohol dehydrogenase II gene !1from Zymomonas mobilis. !$#cross-references MUID:87222181; PMID:3584063 !$#accession A25978 !'##molecule_type DNA !'##residues 1-383 ##label CON !'##cross-references GB:M15394; NID:g155576; PIDN:AAA27683.1; !1PID:g155577 REFERENCE S07584 !$#authors Yoon, K.H.; Pack, M.Y. !$#journal Nucleic Acids Res. (1990) 18:187 !$#title Nucleotide sequence of the Zymomonas mobilis alcohol !1dehydrogenase II gene. !$#cross-references MUID:90174920; PMID:2308827 !$#accession S07584 !'##molecule_type DNA !'##residues 1-56,'T',58-383 ##label YOO !'##cross-references EMBL:X17065; NID:g48650; PIDN:CAA34911.1; !1PID:g48651 REFERENCE A91156 !$#authors Neale, A.D.; Scopes, R.K.; Kelly, J.M.; Wettenhall, R.E.H. !$#journal Eur. J. Biochem. (1986) 154:119-124 !$#title The two alcohol dehydrogenases of Zymomonas mobilis. !1Purification by differential dye ligand chromatography, !1molecular characterisation and physiological roles. !$#cross-references MUID:86108298; PMID:2935393 !$#accession B24801 !'##molecule_type protein !'##residues 2-37,'G',39-44,46-47,'S',49-50 ##label NEA REFERENCE Z21392 !$#authors Lee, J.S.; Jin, S.J.; Kang, H.L.; Kang, H.S. !$#submission submitted to the EMBL Data Library, August 1998 !$#description Sequence analysis of 67E10 cosmid clone of Zymomonas mobilis !1ZM4. !$#accession T33729 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-332,'P',334-383 ##label LEE !'##cross-references EMBL:AF086791; NID:g3820591; PID:g3820588; !1PIDN:AAC70367.1 COMMENT This organism contains both a zinc-containing and an !1iron-containing alcohol dehydrogenase; the iron-containing !1enzyme is inactivated by zinc, activated by ethanol in both !1reaction directions, accounts for 90% of the !1ethanol-oxidizing activity in extracts, and has lower !1acetaldehyde reductase activity than the zinc-containing !1enzyme. GENETICS !$#gene adhB FUNCTION !$#description catalyzes the reversible oxidation of ethanol to !1acetaldehyde using NAD+ !$#pathway ethanol biosynthesis CLASSIFICATION #superfamily lactaldehyde reductase; lactaldehyde reductase !1homology KEYWORDS alcohol metabolism; iron; metalloprotein; NAD; !1oxidoreductase FEATURE !$6-379 #domain lactaldehyde reductase homology #label LAR\ !$260-278 #region iron binding #status predicted SUMMARY #length 383 #molecular-weight 40145 #checksum 6316 SEQUENCE /// ENTRY DEBY4 #type complete TITLE alcohol dehydrogenase (EC 1.1.1.1) 4 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein G0352; protein NRC465; protein YGL256w ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1991 #sequence_revision 12-Apr-1996 #text_change 16-Jun-2000 ACCESSIONS S61605; S07614; S64282 REFERENCE S61598 !$#authors Coissac, E.; Maillier, E.; Robineau, S.; Netter, P. !$#submission submitted to the EMBL Data Library, December 1995 !$#accession S61605 !'##molecule_type DNA !'##residues 1-465 ##label COI !'##cross-references EMBL:X94357; NID:g1150575; PIDN:CAA64131.1; !1PID:g1150583 REFERENCE S07614 !$#authors Williamson, V.M.; Paquin, C.E. !$#journal Mol. Gen. Genet. (1987) 209:374-381 !$#title Homology of Saccharomyces cerevisiae ADH4 to an !1iron-activated alcohol dehydrogenase from Zymomonas mobilis. !$#cross-references MUID:88038383; PMID:2823079 !$#accession S07614 !'##molecule_type DNA !'##residues 1-142,'G',144-170,'E',172-392,'C',394-421,'D',423-430,'D', !1432-465 ##label WIL !'##cross-references EMBL:X05992 !'##note it is uncertain whether Met-1 or Met-84 is the initiator REFERENCE S64271 !$#authors Coissac, E.; Maillier, E.; Netter, P. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64282 !'##molecule_type DNA !'##residues 1-465 ##label COW !'##cross-references EMBL:Z72778; NID:g1322936; PIDN:CAA96976.1; !1PID:g1322937; GSPDB:GN00007; MIPS:YGL256w !'##experimental_source strain S288C GENETICS !$#gene SGD:ADH4; MIPS:YGL256w !'##cross-references SGD:S0003225; MIPS:YGL256w !$#map_position 7L CLASSIFICATION #superfamily lactaldehyde reductase; lactaldehyde reductase !1homology KEYWORDS alcohol metabolism; NAD; oxidoreductase FEATURE !$90-459 #domain lactaldehyde reductase homology #label LAR SUMMARY #length 465 #molecular-weight 50618 #checksum 9515 SEQUENCE /// ENTRY A42952 #type complete TITLE methanol dehydrogenase (EC 1.1.1.244) - Bacillus sp. ORGANISM #formal_name Bacillus sp. DATE 04-Mar-1993 #sequence_revision 21-Jan-1997 #text_change 01-Sep-2000 ACCESSIONS A42952; A38658 REFERENCE A42952 !$#authors de Vries, G.E.; Arfman, N.; Terpstra, P.; Dijkhuizen, L. !$#journal J. Bacteriol. (1992) 174:5346-5353 !$#title Cloning, expression, and sequence analysis of the Bacillus !1methanolicus C1 methanol dehydrogenase gene. !$#cross-references MUID:92355510; PMID:1644761 !$#accession A42952 !'##molecule_type DNA !'##residues 1-381 ##label DE1 !'##cross-references GB:M65004; NID:g143174; PIDN:AAA22593.1; !1PID:g143175 !'##experimental_source strain C1 !'##note sequence extracted from NCBI backbone (NCBIN:110510, !1NCBIP:110511) !'##note authors state that the inconsistencies between this sequence !1and A38658 was due to misinterpretation of the earlier !1results !'##note the source is designated as Bacillus methanolicus REFERENCE A38658 !$#authors Vonck, J.; Arfman, N.; De Vries, G.E.; Van Beeumen, J.; Van !1Bruggen, E.F.J.; Dijkhuizen, L. !$#journal J. Biol. Chem. (1991) 266:3949-3954 !$#title Electron microscopic analysis and biochemical !1characterization of a novel methanol dehydrogenase from the !1thermotolerant Bacillus sp. C1. !$#cross-references MUID:91139696; PMID:1995642 !$#accession A38658 !'##molecule_type protein !'##residues 2-17,'L',19-41,'A',43-44,'X',46-47,'X',49,'DX',52-53,'X', !155-58,'N',60-61 ##label VON GENETICS !$#gene mdh COMPLEX homodecamer FUNCTION !$#description catalyzes the reversible oxidation of methanol to !1formaldehyde using NAD+ CLASSIFICATION #superfamily lactaldehyde reductase; lactaldehyde reductase !1homology KEYWORDS homodecamer; magnesium; metalloprotein; NAD; oxidoreductase; !1zinc FEATURE !$2-381 #product methanol dehydrogenase #status experimental !8#label MAT\ !$4-377 #domain lactaldehyde reductase homology #label LAR SUMMARY #length 381 #molecular-weight 40045 #checksum 5635 SEQUENCE /// ENTRY S06759 #type complete TITLE glycerol-3-phosphate dehydrogenase (NAD) (EC 1.1.1.8) 2 - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S06759; B28995 REFERENCE S06758 !$#authors Bewley, G.C.; Cook, J.L.; Kusakabe, S.; Mukai, T.; Rigby, !1D.L.; Chambers, G.K. !$#journal Nucleic Acids Res. (1989) 17:8553-8567 !$#title Sequence, structure and evolution of the gene coding for !1sn-glycerol-3-phosphate dehydrogenase in Drosophila !1melanogaster. !$#cross-references MUID:90067829; PMID:2511555 !$#accession S06759 !'##molecule_type DNA !'##residues 1-360 ##label BEW !'##cross-references EMBL:X14179 !'##note the authors translated the codon ACG for residue 38 as Ala !'##note part of this sequence was confirmed by protein sequencing !'##note the slow form of glycerol-3-phosphate dehydrogenase (NAD+) !1differs from the fast form in having 337-Lys REFERENCE A92660 !$#authors Cook, J.L.; Bewley, G.C.; Shaffer, J.B. !$#journal J. Biol. Chem. (1988) 263:10858-10864 !$#title Drosophila sn-glycerol-3-phosphate dehydrogenase isozymes !1are generated by alternate pathways of RNA processing !1resulting in different carboxyl-terminal amino acid !1sequences. !$#cross-references MUID:88273210; PMID:2839508 !$#accession B28995 !'##molecule_type DNA !'##residues 298-360 ##label COO !'##cross-references GB:J03927; NID:g157463; PIDN:AAA28554.1; !1PID:g157465 GENETICS !$#gene gpdh !'##cross-references FlyBase:FBgn0001128 !$#map_position 2L 26A !$#introns 15/2; 74/3; 143/3; 268/1; 319/2; 350/2 CLASSIFICATION #superfamily glycerol-3-phosphate dehydrogenase KEYWORDS alternative splicing; NAD; oxidoreductase FEATURE !$2-360 #product glycerol-3-phosphate dehydrogenase (NAD+) 2 !8#status experimental #label MAT SUMMARY #length 360 #molecular-weight 39328 #checksum 4671 SEQUENCE /// ENTRY DEBYI #type complete TITLE 3-isopropylmalate dehydrogenase (EC 1.1.1.85) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YCL018w ORGANISM #formal_name Saccharomyces cerevisiae DATE 04-Dec-1986 #sequence_revision 30-Sep-1993 #text_change 16-Jun-2000 ACCESSIONS S19344; A00361; A24966 REFERENCE S19337 !$#authors Oliver, S.G.; Anwar, R.; Brown, A.; Gent, M.E.; Indge, K.J.; !1James, C.M.; Stateva, L.I.; Warmington, J.R. !$#submission submitted to the Protein Sequence Database, March 1992 !$#accession S19344 !'##molecule_type DNA !'##residues 1-364 ##label OLI !'##cross-references EMBL:X59720; NID:g1907116; PIDN:CAA42366.1; !1PID:g1907128; GSPDB:GN00003; MIPS:YCL018w REFERENCE A00361 !$#authors Andreadis, A.; Hsu, Y.P.; Hermodson, M.; Kohlhaw, G.; !1Schimmel, P. !$#journal J. Biol. Chem. (1984) 259:8059-8062 !$#title Yeast LEU2. Repression of mRNA levels by leucine and primary !1structure of the gene product. !$#cross-references MUID:84239765; PMID:6330094 !$#accession A00361 !'##molecule_type mRNA !'##residues 1-299,'D',301-364 ##label AND !'##cross-references GB:J01333; NID:g171836; PIDN:AAA93044.1; !1PID:g171837 REFERENCE A24966 !$#authors Froman, B.E.; Tait, R.C.; Rodriguez, R.L. !$#journal Gene (1984) 31:257-261 !$#title Nucleotide sequence of the 3' terminal region of the LEU2 !1gene from Saccharomyces cerevisiae. !$#cross-references MUID:85128444; PMID:6396161 !$#accession A24966 !'##molecule_type DNA !'##residues 213-364 ##label FRO !'##cross-references EMBL:M12909; NID:g171838; PIDN:AAA66917.1; !1PID:g171839 GENETICS !$#gene SGD:LEU2; MIPS:YCL018w !'##cross-references SGD:S0000523; MIPS:YCL018w !$#map_position 3L FUNCTION !$#description catalyzes the oxidation of !13-carboxy-2-hydroxy-4-methylpentanoate to !13-carboxy-4-methyl-2-oxopentanoate by NAD+ !$#pathway leucine biosynthesis CLASSIFICATION #superfamily 3-isopropylmalate dehydrogenase KEYWORDS leucine biosynthesis; NAD; oxidoreductase SUMMARY #length 364 #molecular-weight 38981 #checksum 8043 SEQUENCE /// ENTRY A43324 #type complete TITLE 3-isopropylmalate dehydrogenase (EC 1.1.1.85) - yeast (Candida boidinii) ORGANISM #formal_name Candida boidinii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A43324 REFERENCE A43324 !$#authors Sakai, Y.; Tani, Y. !$#journal J. Bacteriol. (1992) 174:5988-5993 !$#title Directed mutagenesis in an asporogenous methylotrophic !1yeast: cloning, sequencing, and one-step gene disruption of !1the 3-isopropylmalate dehydrogenase gene (LEU2) of Candida !1boidinii to derive doubly auxotrophic marker strains. !$#cross-references MUID:92394905; PMID:1522074 !$#accession A43324 !'##molecule_type DNA !'##residues 1-365 ##label SAK !'##cross-references GB:M98832; NID:g170879; PIDN:AAA34349.1; !1PID:g170880 !'##note sequence extracted from NCBI backbone (NCBIN:113056, !1NCBIP:113057) CLASSIFICATION #superfamily 3-isopropylmalate dehydrogenase KEYWORDS leucine biosynthesis; NAD; oxidoreductase SUMMARY #length 365 #molecular-weight 39124 #checksum 2146 SEQUENCE /// ENTRY S25369 #type complete TITLE 3-isopropylmalate dehydrogenase (EC 1.1.1.85) - yeast (Kluyveromyces marxianus var. lactis) ORGANISM #formal_name Kluyveromyces marxianus var. lactis, Candida sphaerica DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S25369 REFERENCE S25368 !$#authors Zhang, Y.P.; Chen, X.J.; Li, Y.Y.; Fukuhara, H. !$#journal Yeast (1992) 8:801-804 !$#title LEU2 gene homolog in Kluyveromyces lactis. !$#cross-references MUID:93070618; PMID:1441757 !$#accession S25369 !'##molecule_type DNA !'##residues 1-362 ##label ZHA !'##cross-references EMBL:X65545; NID:g2854; PIDN:CAA46514.1; PID:g2855 !'##note the authors translated the codon GAT for residue 58 as Asn GENETICS !$#gene LEU2 CLASSIFICATION #superfamily 3-isopropylmalate dehydrogenase KEYWORDS leucine biosynthesis; NAD; oxidoreductase SUMMARY #length 362 #molecular-weight 38629 #checksum 5107 SEQUENCE /// ENTRY A47620 #type complete TITLE 3-isopropylmalate dehydrogenase (EC 1.1.1.85) - yeast (Pichia jadinii) ORGANISM #formal_name Pichia jadinii, Candida utilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A47620 REFERENCE A47620 !$#authors Hamasawa, K.; Kobayashi, Y.; Harada, S.; Yoda, K.; Yamasaki, !1M.; Tamura, G. !$#journal J. Gen. Microbiol. (1987) 133:1089-1097 !$#title Molecular cloning and nucleotide sequence of the !13-isopropylmalate dehydrogenase gene of Candida utilis. !$#cross-references MUID:88009903; PMID:3309174 !$#accession A47620 !'##status preliminary !'##molecule_type DNA !'##residues 1-363 ##label HAM !'##cross-references GB:M16014; NID:g170873; PIDN:AAA34347.1; !1PID:g170874 GENETICS !$#gene 3-IMDH FUNCTION !$#pathway leucine biosynthesis CLASSIFICATION #superfamily 3-isopropylmalate dehydrogenase KEYWORDS leucine biosynthesis; NAD; oxidoreductase SUMMARY #length 363 #molecular-weight 38705 #checksum 8894 SEQUENCE /// ENTRY S43454 #type complete TITLE 3-isopropylmalate dehydrogenase (EC 1.1.1.85) - yeast (Pichia angusta) ORGANISM #formal_name Pichia angusta DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 20-Apr-2000 ACCESSIONS S43454 REFERENCE S43454 !$#authors Agaphonov, M.O.; Poznyakovski, A.I.; Bogdanova, A.I.; !1Ter-Avanesyan, M.D. !$#journal Yeast (1994) 10:509-513 !$#title Isolation and characterization of the LEU2 gene of Hansenula !1polymorpha. !$#cross-references MUID:95028149; PMID:7941737 !$#accession S43454 !'##molecule_type DNA !'##residues 1-362 ##label AGA !'##cross-references EMBL:U00889; NID:g392892; PIDN:AAA19109.1; !1PID:g392893 GENETICS !$#gene LEU2 !$#map_position 1 CLASSIFICATION #superfamily 3-isopropylmalate dehydrogenase KEYWORDS leucine biosynthesis; NAD; oxidoreductase SUMMARY #length 362 #molecular-weight 38046 #checksum 5742 SEQUENCE /// ENTRY T43407 #type complete TITLE 3-isopropylmalate dehydrogenase (EC 1.1.1.85) [validated] - fission yeast (Schizosaccharomyces pombe) ORGANISM #formal_name Schizosaccharomyces pombe DATE 18-Feb-2000 #sequence_revision 18-Feb-2000 #text_change 21-Jul-2000 ACCESSIONS T43407; T39850; T39871 REFERENCE Z22491 !$#authors Kikuchi, Y.; Kitazawa, Y.; Shimatake, G.; Yamamoto, M. !$#journal Curr. Genet. (1988) 14:375-379 !$#title The primary structure of the leu1+ gene of !1Schizosaccharomyces pombe. !$#cross-references MUID:89106270; PMID:3063400 !$#accession T43407 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-371 ##label KIK !'##cross-references EMBL:M36910; NID:g173411; PIDN:AAA35316.1; !1PID:g173412 REFERENCE Z21885 !$#authors Wood, V.; Rajandream, M.A.; Barrell, B.G.; Volckaert, G. !$#submission submitted to the EMBL Data Library, July 1998 !$#accession T39850 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-371 ##label WOO !'##cross-references EMBL:AL031174; PIDN:CAA20106.1; GSPDB:GN00067 !'##experimental_source strain 972h-; cosmid c1A4 REFERENCE Z21887 !$#authors Volckaert, G.; Lyne, M.; Rajandream, M.A.; Barrell, B.G. !$#submission submitted to the EMBL Data Library, February 1998 !$#accession T39871 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 152-371 ##label VOL !'##cross-references EMBL:AL021746; PIDN:CAA16840.1; GSPDB:GN00067; !1SPDB:SPBC1E8.07c !'##experimental_source strain 972h-; cosmid c1E8 GENETICS !$#gene leu1; SPDB:SPBC1E8.07c; SPBC1A4.02c !$#map_position 2 FUNCTION IPD1 !$#description catalyzes the oxidation of !13-carboxy-2-hydroxy-4-methylpentanoate to !13-carboxy-4-methyl-2-oxopentanoate by NAD+ !$#pathway leucine biosynthesis FUNCTION IPD2 !$#description EC 1.1.1.85 [validated, MUID:89106270] CLASSIFICATION #superfamily 3-isopropylmalate dehydrogenase KEYWORDS oxidoreductase SUMMARY #length 371 #molecular-weight 39732 #checksum 4589 SEQUENCE /// ENTRY S48225 #type complete TITLE 3-isopropylmalate dehydrogenase (EC 1.1.1.85) (allele LEa) - yeast (Candida maltosa) ORGANISM #formal_name Candida maltosa DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S48225; S32711 REFERENCE S48225 !$#authors Becher, D.; Schulze, S.; Kasueske, A.; Schulze, H.; !1Samsonova, I.A.; Oliver, S.G. !$#journal Curr. Genet. (1994) 26:208-216 !$#title Molecular analysis of a leu2(-) mutant of Candida maltosa !1demonstrates the presence of multiple alleles. !$#cross-references MUID:95163116; PMID:7859302 !$#accession S48225 !'##molecule_type DNA !'##residues 1-373 ##label BEC !'##cross-references EMBL:X72937; NID:g296349; PIDN:CAA51442.1; !1PID:g296350 !'##experimental_source strain G587:leu2 GENETICS !$#gene leu2 !$#map_position III FUNCTION !$#pathway leucine biosynthesis CLASSIFICATION #superfamily 3-isopropylmalate dehydrogenase KEYWORDS leucine biosynthesis; NAD; oxidoreductase SUMMARY #length 373 #molecular-weight 40270 #checksum 7837 SEQUENCE /// ENTRY DETWIT #type complete TITLE 3-isopropylmalate dehydrogenase (EC 1.1.1.85) - Thermus aquaticus ORGANISM #formal_name Thermus aquaticus DATE 28-May-1986 #sequence_revision 06-Jun-1997 #text_change 16-Jun-2000 ACCESSIONS S41223; A00362; S35096; JX0173 REFERENCE S41197 !$#authors Kirino, H.; Aoki, M.; Aoshima, M.; Hayashi, Y.; Ohba, M.; !1Yamagishi, A.; Wakagi, T.; Oshima, T. !$#journal Eur. J. Biochem. (1994) 220:275-281 !$#title Hydrophobic interaction at the subunit interface contributes !1to the thermostability of 3-isopropylmalate dehydrogenase !1from an extreme thermophile, Thermus thermophilus. !$#cross-references MUID:94164169; PMID:8119295 !$#accession S41223 !'##status preliminary !'##molecule_type DNA !'##residues 1-345 ##label KIR !'##note the source is given as Thermus thermophilus REFERENCE A00362 !$#authors Kagawa, Y.; Nojima, H.; Nukiwa, N.; Ishizuka, M.; Nakajima, !1T.; Yasuhara, T.; Tanaka, T.; Oshima, T. !$#journal J. Biol. Chem. (1984) 259:2956-2960 !$#title High guanine plus cytosine content in the third letter of !1codons of an extreme thermophile. DNA sequence of the !1isopropylmalate dehydrogenase of Thermus thermophilus. !$#cross-references MUID:84135791; PMID:6321488 !$#accession A00362 !'##molecule_type DNA !'##residues 1-31,33,'PT',36-48,'SA',52-75,'RLGRPSPQDP',86,'GD',89, !1'ASF',93,'KEKP',98-194,'R',196-243,'GN',246,'RAD',250-278, !1'Y',280-283,'R',286-299,'QLRPGG',307-314,316-330,'EAR', !1335-345 ##label KAG1 !'##cross-references EMBL:K01444 !'##experimental_source strain thermophilus HB8, ATCC 27634 !'##note the authors translated the codon GAG for residue 332 as Ala !'##note this sequence has been revised in reference S41197 !$#accession S35096 !'##molecule_type protein !'##residues 1-8;108-114;133-139;265-271;343-345 ##label KAG2 !'##experimental_source strain thermophilus HB8, ATCC 27634 REFERENCE JX0173 !$#authors Kirino, H.; Oshima, T. !$#journal J. Biochem. (1991) 109:852-857 !$#title Molecular cloning and nucleotide sequence of !13-isopropylmalate dehydrogenase gene (leuB) from an extreme !1thermophile, Thermus aquaticus YT-1. !$#cross-references MUID:92041736; PMID:1939005 !$#accession JX0173 !'##molecule_type DNA !'##residues 1,'R',3-20,'R',22-23,'K',25-28,'R',30-34,'T',36-37,'T', !139-47,'GY',50-55,'V',57-62,'A',64-78,'A',80-87,'S',89-91, !1'A',93-166,'K',168-177,'R',179,'LT',182-202,'HK',205-211, !1'D',213-224,'KN',227-309,'R',311-312,'A',314-319,'R', !1321-333,'Q',335-337,'EE',340-344 ##label KIW !'##cross-references GB:D10700; GB:D01110; NID:g217177; PIDN:BAA01542.1; !1PID:g217178 !'##experimental_source YT-1 GENETICS !$#gene leuB COMPLEX homodimer FUNCTION !$#description catalyzes the oxidation of !13-carboxy-2-hydroxy-4-methylpentanoate to !13-carboxy-4-methyl-2-oxopentanoate by NAD+ !$#pathway leucine biosynthesis CLASSIFICATION #superfamily 3-isopropylmalate dehydrogenase KEYWORDS homodimer; leucine biosynthesis; NAD; oxidoreductase SUMMARY #length 345 #molecular-weight 36780 #checksum 6694 SEQUENCE /// ENTRY JX0286 #type complete TITLE 3-isopropylmalate dehydrogenase (EC 1.1.1.85) - Thiobacillus ferrooxidans ORGANISM #formal_name Thiobacillus ferrooxidans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS JX0286 REFERENCE JX0286 !$#authors Kawaguchi, H.; Inagaki, K.; Kuwata, Y.; Tanaka, H.; Tano, T. !$#journal J. Biochem. (1993) 114:370-377 !$#title 3-Isopropylmalate dehydrogenase from chemolithoautotroph !1Thiobacillus ferrooxidans: DNA sequence, enzyme !1purification, and characterization. !$#cross-references MUID:94110259; PMID:8282728 !$#accession JX0286 !'##molecule_type DNA !'##residues 1-358 ##label KAW !'##cross-references GB:D14585; NID:g414354; PIDN:BAA03437.1; !1PID:g414355 GENETICS !$#gene leuB FUNCTION !$#pathway leucine biosynthesis CLASSIFICATION #superfamily 3-isopropylmalate dehydrogenase KEYWORDS leucine biosynthesis; NAD; oxidoreductase SUMMARY #length 358 #molecular-weight 38462 #checksum 7841 SEQUENCE /// ENTRY A44851 #type complete TITLE 3-isopropylmalate dehydrogenase (EC 1.1.1.85) - Spirulina platensis ORGANISM #formal_name Spirulina platensis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A44851 REFERENCE A44851 !$#authors Bini, F.; De Rossi, E.; Barbierato, L.; Riccardi, G. !$#journal J. Gen. Microbiol. (1992) 138:493-498 !$#title Molecular cloning and sequencing of the beta-isopropylmalate !1dehydrogenase gene from the cyanobacterium Spirulina !1platensis. !$#cross-references MUID:92277052; PMID:1593261 !$#accession A44851 !'##status preliminary !'##molecule_type DNA !'##residues 1-355 ##label BIN !'##note this sequence is inconsistent with the nucleotide translation !'##note sequence extracted from NCBI backbone (NCBIN:103823, !1NCBIP:103824) GENETICS !$#gene leuB FUNCTION !$#pathway leucine biosynthesis CLASSIFICATION #superfamily 3-isopropylmalate dehydrogenase KEYWORDS leucine biosynthesis; NAD; oxidoreductase SUMMARY #length 355 #molecular-weight 38137 #checksum 3228 SEQUENCE /// ENTRY S20510 #type complete TITLE 3-isopropylmalate dehydrogenase (EC 1.1.1.85) precursor - rape ORGANISM #formal_name Brassica napus #common_name rape DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S20510 REFERENCE S20510 !$#authors Ellerstroem, M.; Josefsson, L.G.; Rask, L.; Ronne, H. !$#journal Plant Mol. Biol. (1992) 18:557-566 !$#title Cloning of a cDNA for rape chloroplast 3-isopropylmalate !1dehydrogenase by genetic complementation in yeast. !$#cross-references MUID:92163020; PMID:1371407 !$#accession S20510 !'##molecule_type mRNA !'##residues 1-406 ##label ELL !'##cross-references EMBL:X59970; NID:g17826; PIDN:CAA42596.1; !1PID:g17827 !'##experimental_source strain Svalfs Karat 20516-K GENETICS !$#genome nuclear FUNCTION !$#pathway leucine biosynthesis CLASSIFICATION #superfamily 3-isopropylmalate dehydrogenase KEYWORDS chloroplast; leucine biosynthesis; NAD; oxidoreductase FEATURE !$1-34 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$35-406 #product 3-isopropylmalate dehydrogenase #status !8predicted #label MAT SUMMARY #length 406 #molecular-weight 43350 #checksum 5687 SEQUENCE /// ENTRY DEBSIC #type complete TITLE 3-isopropylmalate dehydrogenase (EC 1.1.1.85) - Bacillus coagulans ORGANISM #formal_name Bacillus coagulans DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 02-Jul-1998 ACCESSIONS A24537 REFERENCE A24537 !$#authors Sekiguchi, T.; Ortega-Cesena, J.; Nosoh, Y.; Ohashi, S.; !1Tsuda, K.; Kanaya, S. !$#journal Biochim. Biophys. Acta (1986) 867:36-44 !$#title DNA and amino-acid sequences of 3-isopropylmalate !1dehydrogenase of Bacillus coagulans. Comparison with the !1enzymes of Saccharomyces cerevisiae and Thermus !1thermophilus. !$#accession A24537 !'##molecule_type DNA !'##residues 1-366 ##label SEK COMMENT This enzyme is involved in leucine biosynthesis and !1catalyzes the conversion of 3-isopropylmalate to !1alpha-ketoisocaproate. FUNCTION !$#description catalyzes the oxidation of !13-carboxy-2-hydroxy-4-methylpentanoate to !13-carboxy-4-methyl-2-oxopentanoate by NAD+ !$#pathway leucine biosynthesis CLASSIFICATION #superfamily 3-isopropylmalate dehydrogenase KEYWORDS leucine biosynthesis; NAD; oxidoreductase SUMMARY #length 366 #molecular-weight 39808 #checksum 2444 SEQUENCE /// ENTRY I40226 #type complete TITLE 3-isopropylmalate dehydrogenase (EC 1.1.1.85) - Bacillus megaterium ORGANISM #formal_name Bacillus megaterium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS I40226; S38506 REFERENCE I40226 !$#authors Meinhardt, F.; Wittchen, K.D.; Buakamp, M. !$#journal Appl. Microbiol. Biotechnol. (1994) 41:344-351 !$#title Cloning and sequencing of the lenC and npM genes and a !1putative spoIV gene from bacillus megattinm DSM319. !$#cross-references MUID:94288995; PMID:7764969 !$#accession I40226 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-367 ##label RES !'##cross-references EMBL:X65184; NID:g414096; PIDN:CAA46295.1; !1PID:g414097 !'##experimental_source DSM 319 GENETICS !$#gene leuC FUNCTION !$#pathway leucine biosynthesis CLASSIFICATION #superfamily 3-isopropylmalate dehydrogenase KEYWORDS leucine biosynthesis; NAD; oxidoreductase SUMMARY #length 367 #molecular-weight 39942 #checksum 4571 SEQUENCE /// ENTRY A26522 #type complete TITLE 3-isopropylmalate dehydrogenase (EC 1.1.1.85) - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A26522; A69650 REFERENCE A26522 !$#authors Imai, R.; Sekiguchi, T.; Nosoh, Y.; Tsuda, K. !$#journal Nucleic Acids Res. (1987) 15:4988 !$#title The nucleotide sequence of 3-isopropylmalate dehydrogenase !1gene from Bacillus subtilis. !$#cross-references MUID:87259976; PMID:3110742 !$#accession A26522 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-365 ##label IMA !'##cross-references GB:Y00353; NID:g39975; PIDN:CAA68432.1; PID:g580891 !'##experimental_source strain 168 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69650 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-181,'A',183-365 ##label KUN !'##cross-references GB:Z99118; GB:AL009126; NID:g2635200; !1PIDN:CAB14787.1; PID:g2635292 !'##experimental_source strain 168 GENETICS !$#gene leuB !$#start_codon TTG FUNCTION !$#description catalyzes the oxidation of !13-carboxy-2-hydroxy-4-methylpentanoate to !13-carboxy-4-methyl-2-oxopentanoate by NAD+ !$#pathway leucine biosynthesis CLASSIFICATION #superfamily 3-isopropylmalate dehydrogenase KEYWORDS leucine biosynthesis; NAD; oxidoreductase SUMMARY #length 365 #molecular-weight 39975 #checksum 9104 SEQUENCE /// ENTRY A26447 #type complete TITLE 3-isopropylmalate dehydrogenase (EC 1.1.1.85) - Bacillus caldotenax ORGANISM #formal_name Bacillus caldotenax DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A26447 REFERENCE A26447 !$#authors Sekiguchi, T.; Suda, M.; Ishii, T.; Nosoh, Y.; Tsuda, K. !$#journal Nucleic Acids Res. (1987) 15:853 !$#title The nucleotide sequence of 3-isopropylmalate dehydrogenase !1gene from Bacillus caldotenax. !$#cross-references MUID:87146398; PMID:3547331 !$#accession A26447 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-366 ##label SEK !'##cross-references GB:X04762; NID:g39405; PIDN:CAA28455.1; PID:g39406 FUNCTION !$#pathway leucine biosynthesis CLASSIFICATION #superfamily 3-isopropylmalate dehydrogenase KEYWORDS leucine biosynthesis; NAD; oxidoreductase SUMMARY #length 366 #molecular-weight 39635 #checksum 6094 SEQUENCE /// ENTRY A64729 #type complete TITLE 3-isopropylmalate dehydrogenase (EC 1.1.1.85) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS A64729; S41197; S40587 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64729 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-364 ##label BLAT !'##cross-references GB:AE000117; GB:U00096; NID:g1786250; !1PIDN:AAC73184.1; PID:g1786260; UWGP:b0073 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S41197 !$#authors Kirino, H.; Aoki, M.; Aoshima, M.; Hayashi, Y.; Ohba, M.; !1Yamagishi, A.; Wakagi, T.; Oshima, T. !$#journal Eur. J. Biochem. (1994) 220:275-281 !$#title Hydrophobic interaction at the subunit interface contributes !1to the thermostability of 3-isopropylmalate dehydrogenase !1from an extreme thermophile, Thermus thermophilus. !$#cross-references MUID:94164169; PMID:8119295 !$#accession S41197 !'##status preliminary !'##molecule_type DNA !'##residues 2-364 ##label KIR !'##cross-references EMBL:D17631; NID:g409068; PIDN:BAA04537.1; !1PID:g457440 REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40587 !'##status preliminary !'##molecule_type DNA !'##residues 2-364 ##label YUR !'##cross-references EMBL:D10483; NID:g216434; PIDN:BAA01342.1; !1PID:g216491 GENETICS !$#gene leuB FUNCTION !$#pathway leucine biosynthesis CLASSIFICATION #superfamily 3-isopropylmalate dehydrogenase KEYWORDS leucine biosynthesis; NAD; oxidoreductase SUMMARY #length 364 #molecular-weight 39648 #checksum 4163 SEQUENCE /// ENTRY F64106 #type complete TITLE 3-isopropylmalate dehydrogenase (EC 1.1.1.85) - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS F64106 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession F64106 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-358 ##label TIGR !'##cross-references GB:U32779; GB:L42023; NID:g1574009; !1PIDN:AAC22648.1; PID:g1574016; TIGR:HI0987 !'##note named as homolog to a protein from Salmonella typhimurium CLASSIFICATION #superfamily 3-isopropylmalate dehydrogenase KEYWORDS leucine biosynthesis; NAD; oxidoreductase SUMMARY #length 358 #molecular-weight 38808 #checksum 7094 SEQUENCE /// ENTRY S35133 #type complete TITLE 3-isopropylmalate dehydrogenase (EC 1.1.1.85) - Lactococcus lactis subsp. lactis ORGANISM #formal_name Lactococcus lactis subsp. lactis #variety strain NCDO2118 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS S35133; C36889 REFERENCE S35132 !$#authors Godon, J.J.; Chopin, M.C.; Ehrlich, S.D. !$#journal J. Bacteriol. (1992) 174:6580-6589 !$#title Branched-chain amino acid biosynthesis genes in Lactococcus !1lactis subsp. lactis. !$#cross-references MUID:93015710; PMID:1400210 !$#accession S35133 !'##molecule_type DNA !'##residues 1-345 ##label GOD !'##cross-references EMBL:M90761; NID:g2565137; PIDN:AAB81914.1; !1PID:g2565152 !'##note the authors translated the initiation codon TTG for residue 1 !1as Leu REFERENCE A36889 !$#authors Godon, J.J.; Delorme, C.; Bardowski, J.; Chopin, M.C.; !1Ehrlich, S.D.; Renault, P. !$#journal J. Bacteriol. (1993) 175:4383-4390 !$#title Gene inactivation in Lactococcus lactis: branched-chain !1amino acid biosynthesis. !$#cross-references MUID:93322316; PMID:8331070 !$#accession C36889 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-15,'G',17-65,'R',67-127,'M',129-307,'T',309-320 ##label !1GO2 !'##experimental_source auxotrophic mutant strain strain IL1403 GENETICS !$#gene leuB !$#start_codon TTG FUNCTION !$#pathway leucine biosynthesis CLASSIFICATION #superfamily 3-isopropylmalate dehydrogenase KEYWORDS leucine biosynthesis; NAD; oxidoreductase SUMMARY #length 345 #molecular-weight 37587 #checksum 2304 SEQUENCE /// ENTRY S49786 #type complete TITLE 3-isopropylmalate dehydrogenase homolog YIL094c - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein YI9910.01 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S49786 REFERENCE S49786 !$#authors Connor, R.; Churcher, C. !$#submission submitted to the EMBL Data Library, November 1994 !$#accession S49786 !'##molecule_type DNA !'##residues 1-371 ##label CON !'##cross-references GB:Z47047; EMBL:Z46728; NID:g603997; PID:g763252; !1GSPDB:GN00009; MIPS:YIL094c GENETICS !$#gene SGD:LYS12; MIPS:YIL094c !'##cross-references SGD:S0001356 !$#map_position 9L CLASSIFICATION #superfamily 3-isopropylmalate dehydrogenase SUMMARY #length 371 #molecular-weight 40069 #checksum 6267 SEQUENCE /// ENTRY S30897 #type complete TITLE 3-isopropylmalate dehydrogenase (EC 1.1.1.85) precursor - potato ALTERNATE_NAMES beta-isopropylmalate dehydrogenase ORGANISM #formal_name Solanum tuberosum #common_name potato DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S30897; S25670 REFERENCE S30897 !$#authors Jackson, S.D.; Sonnewald, U.; Willmitzer, L. !$#journal Mol. Gen. Genet. (1993) 236:309-314 !$#title Cloning and expression analysis of beta-isopropylmalate !1dehydrogenase from potato. !$#cross-references MUID:93173106; PMID:8437576 !$#accession S30897 !'##molecule_type mRNA !'##residues 1-357 ##label JAC !'##cross-references EMBL:X67310; NID:g22642; PIDN:CAA47720.1; !1PID:g22643 !'##experimental_source cv. Desiree REFERENCE S25670 !$#authors Jackson, S.D. !$#submission submitted to the EMBL Data Library, July 1992 !$#accession S25670 !'##molecule_type mRNA !'##residues 1-240,'C',242-357 ##label JAW !'##cross-references EMBL:X67310; NID:g22642; PIDN:CAA47720.1; !1PID:g22643 GENETICS !$#genome nuclear CLASSIFICATION #superfamily 3-isopropylmalate dehydrogenase KEYWORDS chloroplast; oxidoreductase FEATURE !$1-29 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$30-357 #product 3-isopropylmalate dehydrogenase #status !8predicted #label MAT SUMMARY #length 357 #molecular-weight 39793 #checksum 2419 SEQUENCE /// ENTRY S48640 #type complete TITLE tartrate dehydrogenase (EC 1.1.1.93) - Pseudomonas putida CONTAINS D-malate dehydrogenase (decarboxylating) (EC 1.1.1.83); tartrate decarboxylase (EC 4.1.1.73) ORGANISM #formal_name Pseudomonas putida DATE 15-Jul-1995 #sequence_revision 09-May-1997 #text_change 11-Jun-1999 ACCESSIONS S48640 REFERENCE S48640 !$#authors Tipton, P.A.; Beecher, B.S. !$#journal Arch. Biochem. Biophys. (1994) 313:15-21 !$#title Tartrate dehydrogenase, a new member of the family of !1metal-dependent decarboxylating R-hydroxyacid !1dehydrogenases. !$#cross-references MUID:94330710; PMID:8053675 !$#accession S48640 !'##molecule_type DNA !'##residues 1-365 ##label TIP !'##cross-references GB:U05986; NID:g458334; PIDN:AAA60327.1; !1PID:g458335 REFERENCE A58577 !$#authors Tipton, P.A.; Peisach, J. !$#journal Biochemistry (1990) 29:1749-1756 !$#title Characterization of the multiple catalytic activities of !1tartrate dehydrogenase. !$#cross-references MUID:90234688; PMID:2184888 !$#contents annotation; enzymatic activities COMMENT This enzyme, closely related to and weakly possessing the !1activity of 3-isopropylmalate dehydrogenase (EC 1.1.1.85), !1performs a number of reactions on four-carbon dicarboxylic !1acid substrates utilizing the same active site. The !12-oxoacid products tend to undergo spontaneous !1decarboxylation. FUNCTION TDH !$#description as tartrate dehydrogenase catalyzes the oxidation of (R, !1R)-tartrate to oxaloglycolate by NAD+ !$#note enables the organism to grow with tartrate as the sole !1carbon source; from a racemic mixture, only (R,R)-tartrate !1is consumed FUNCTION DMD !$#description as D-malate dehydrogenase (decarboxylating) catalyzes the !1oxidative decarboxylation of D-malate to pyruvate and carbon !1dioxide by NAD+ FUNCTION MTD !$#description as tartrate decarboxylase catalyzes the decarboxylation of !1meso-tartrate to D-glycerate and carbon dioxide !$#note this activity requires only catalytic quantities of NAD+ CLASSIFICATION #superfamily 3-isopropylmalate dehydrogenase KEYWORDS carbon-carbon lyase; carboxy-lyase; manganese; NAD; !1oxidoreductase FEATURE !$2-365 #product tartrate dehydrogenase #status experimental !8#label MAT SUMMARY #length 365 #molecular-weight 40630 #checksum 1404 SEQUENCE /// ENTRY ISECKR #type complete TITLE ketol-acid reductoisomerase (EC 1.1.1.86) - Escherichia coli (strain K-12) ALTERNATE_NAMES acetohydroxy acid isomeroreductase; dihydroxyisovalerate dehydrogenase ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 10-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS A65181; A26287; S30672 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65181 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-491 ##label BLAT !'##cross-references GB:AE000454; GB:U00096; NID:g2367278; !1PIDN:AAC76779.1; PID:g1790210; UWGP:b3774 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A92575 !$#authors Wek, R.C.; Hatfield, G.W. !$#journal J. Biol. Chem. (1986) 261:2441-2450 !$#title Nucleotide sequence and in vivo expression of the ilvY and !1ilvC genes in Escherichia coli K12: transcription from !1divergent overlapping promoters. !$#cross-references MUID:86111952; PMID:3003115 !$#accession A26287 !'##molecule_type DNA !'##residues 1-250,'K',252-491 ##label WEK !'##cross-references GB:M11689; GB:M14492; NID:g146474; PIDN:AAA24029.1; !1PID:g146477 !'##experimental_source strain K12 REFERENCE S30660 !$#authors Daniels, D.L.; Plunkett III, G.; Burland, V.; Blattner, F.R. !$#journal Science (1992) 257:771-778 !$#title Analysis of the Escherichia coli genome: DNA sequence of the !1region from 84.5 to 86.5 minutes. !$#cross-references MUID:92358234; PMID:1379743 !$#accession S30672 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-491 ##label DAN !'##cross-references EMBL:M87049; NID:g836656; PIDN:AAA67577.1; !1PID:g148181 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1992 COMMENT This is the second enzyme in the parallel isoleucine-valine !1pathway of E. coli. ilvC gene expression is induced in the !1presence of acetohydroxybutyrate and acetolactate, the !1substrates of ketol-acid reductoisomerase. GENETICS !$#gene ilvC !$#map_position 85 min CLASSIFICATION #superfamily Escherichia coli ketol-acid reductoisomerase; !1ketol-acid reductoisomerase homology KEYWORDS intramolecular transferase; isoleucine-valine biosynthesis; !1isomerase; oxidoreductase FEATURE !$41-229 #domain ketol-acid reductoisomerase homology #label !8KAR SUMMARY #length 491 #molecular-weight 54069 #checksum 2794 SEQUENCE /// ENTRY B64086 #type complete TITLE ketol-acid reductoisomerase (EC 1.1.1.86) - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS B64086 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession B64086 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-492 ##label TIGR !'##cross-references GB:U32751; GB:L42023; NID:g3212200; !1PIDN:AAC22342.1; PID:g1573684; TIGR:HI0682 !'##note named as homolog to a protein from Escherichia coli CLASSIFICATION #superfamily Escherichia coli ketol-acid reductoisomerase; !1ketol-acid reductoisomerase homology KEYWORDS intramolecular transferase; isoleucine-valine biosynthesis; !1isomerase; oxidoreductase FEATURE !$41-229 #domain ketol-acid reductoisomerase homology #label !8KAR SUMMARY #length 492 #molecular-weight 54239 #checksum 5683 SEQUENCE /// ENTRY F64492 #type complete TITLE ketol-acid reductoisomerase (EC 1.1.1.86) - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F64492 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession F64492 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-348 ##label BUL !'##cross-references GB:U67595; GB:L77117; NID:g1592170; !1PIDN:AAB99561.1; PID:g1592174; TIGR:MJ1543 GENETICS !$#map_position FOR1521365-1522411 CLASSIFICATION #superfamily Methanococcus ketol-acid reductoisomerase; !1ketol-acid reductoisomerase homology KEYWORDS intramolecular transferase; isoleucine-valine biosynthesis; !1isomerase; oxidoreductase FEATURE !$39-221 #domain ketol-acid reductoisomerase homology #label !8KAR SUMMARY #length 348 #molecular-weight 38938 #checksum 2355 SEQUENCE /// ENTRY A47037 #type complete TITLE ketol-acid reductoisomerase (EC 1.1.1.86) - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S76754; A47037 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76754 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-367 ##label KAN !'##cross-references EMBL:D90916; GB:AB001339; NID:g1653715; !1PIDN:BAA18666.1; PID:g1653755 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 REFERENCE A47037 !$#authors Rieble, S.; Beale, S.I. !$#journal J. Bacteriol. (1992) 174:7910-7918 !$#title Structure and expression of a cyanobacterial ilvC gene !1encoding acetohydroxyacid isomeroreductase. !$#cross-references MUID:93094118; PMID:1459938 !$#accession A47037 !'##molecule_type DNA; protein !'##residues 37-327,'A',329-367 ##label RIE !'##experimental_source PCC 6803 !'##note sequence extracted from NCBI backbone (NCBIN:119932, !1NCBIP:119933) GENETICS !$#gene ilvC CLASSIFICATION #superfamily Methanococcus ketol-acid reductoisomerase; !1ketol-acid reductoisomerase homology KEYWORDS intramolecular transferase; isoleucine-valine biosynthesis; !1isomerase; oxidoreductase FEATURE !$57-239 #domain ketol-acid reductoisomerase homology #label !8KAR SUMMARY #length 367 #molecular-weight 39951 #checksum 8264 SEQUENCE /// ENTRY S35140 #type complete TITLE probable ketol-acid reductoisomerase (EC 1.1.1.86) - Lactococcus lactis subsp. lactis ORGANISM #formal_name Lactococcus lactis subsp. lactis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS S35140 REFERENCE S35132 !$#authors Godon, J.J.; Chopin, M.C.; Ehrlich, S.D. !$#journal J. Bacteriol. (1992) 174:6580-6589 !$#title Branched-chain amino acid biosynthesis genes in Lactococcus !1lactis subsp. lactis. !$#cross-references MUID:93015710; PMID:1400210 !$#accession S35140 !'##molecule_type DNA !'##residues 1-344 ##label GOD !'##cross-references EMBL:M90761; NID:g2565137; PIDN:AAB81921.1; !1PID:g2565159 GENETICS !$#gene ilvC CLASSIFICATION #superfamily Methanococcus ketol-acid reductoisomerase; !1ketol-acid reductoisomerase homology KEYWORDS intramolecular transferase; isoleucine-valine biosynthesis; !1isomerase; oxidoreductase FEATURE !$22-203 #domain ketol-acid reductoisomerase homology #label !8KAR SUMMARY #length 344 #molecular-weight 37752 #checksum 2730 SEQUENCE /// ENTRY C48648 #type complete TITLE ketol-acid reductoisomerase (EC 1.1.1.86) - Corynebacterium glutamicum ORGANISM #formal_name Corynebacterium glutamicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C48648 REFERENCE A48648 !$#authors Keilhauer, C.; Eggeling, L.; Sahm, H. !$#journal J. Bacteriol. (1993) 175:5595-5603 !$#title Isoleucine synthesis in Corynebacterium glutamicum: !1molecular analysis of the ilvB-ilvN-ilvC operon. !$#cross-references MUID:93374855; PMID:8366043 !$#accession C48648 !'##status preliminary !'##molecule_type DNA !'##residues 1-338 ##label KEI !'##cross-references GB:L09232; NID:g551777; PIDN:AAA62431.1; !1PID:g400336 CLASSIFICATION #superfamily Methanococcus ketol-acid reductoisomerase; !1ketol-acid reductoisomerase homology KEYWORDS intramolecular transferase; isoleucine-valine biosynthesis; !1isomerase; oxidoreductase FEATURE !$22-204 #domain ketol-acid reductoisomerase homology #label !8KAR SUMMARY #length 338 #molecular-weight 36158 #checksum 9092 SEQUENCE /// ENTRY JC5166 #type complete TITLE ketol-acid reductoisomerase (EC 1.1.1.86) - Mycobacterium avium ALTERNATE_NAMES acetohydroxy acid isomeroreductase ORGANISM #formal_name Mycobacterium avium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JC5166 REFERENCE JC5164 !$#authors Gusberti, L.; Cantoni, R.; De Rossi, E.; Branzoni, M.; !1Riccardi, G. !$#journal Gene (1996) 177:83-85 !$#title Cloning and sequencing of the ilvBNC gene cluster from !1Mycobacterium avium. !$#cross-references MUID:97080504; PMID:8921849 !$#accession JC5166 !'##status preliminary !'##molecule_type DNA !'##residues 1-333 ##label GUS !'##cross-references GB:L49392; NID:g1196506; PIDN:AAB38428.1; !1PID:g1196509 GENETICS !$#gene ilvC CLASSIFICATION #superfamily Methanococcus ketol-acid reductoisomerase; !1ketol-acid reductoisomerase homology KEYWORDS intramolecular transferase; isoleucine-valine biosynthesis; !1isomerase; oxidoreductase FEATURE !$18-200 #domain ketol-acid reductoisomerase homology #label !8KAR SUMMARY #length 333 #molecular-weight 36058 #checksum 1327 SEQUENCE /// ENTRY B64561 #type complete TITLE ketol-acid reductoisomerase (EC 1.1.1.86) - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B64561 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession B64561 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-330 ##label TOM !'##cross-references GB:AE000551; GB:AE000511; NID:g2313430; !1PIDN:AAD07399.1; PID:g2313431; TIGR:HP0330 GENETICS !$#start_codon TTG CLASSIFICATION #superfamily Methanococcus ketol-acid reductoisomerase; !1ketol-acid reductoisomerase homology KEYWORDS intramolecular transferase; isoleucine-valine biosynthesis; !1isomerase; oxidoreductase FEATURE !$22-205 #domain ketol-acid reductoisomerase homology #label !8KAR SUMMARY #length 330 #molecular-weight 36533 #checksum 9933 SEQUENCE /// ENTRY S17180 #type complete TITLE ketol-acid reductoisomerase (EC 1.1.1.86) precursor - spinach ALTERNATE_NAMES acetohydroxy acid reductoisomerase ORGANISM #formal_name Spinacia oleracea #common_name spinach DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 07-Dec-1999 ACCESSIONS S17180; S23644 REFERENCE S17180 !$#authors Dumas, R.; Lebrun, M.; Douce, R. !$#journal Biochem. J. (1991) 277:469-475 !$#title Isolation, characterization and sequence analysis of a !1full-length cDNA clone encoding acetohydroxy acid !1reductoisomerase from spinach chloroplasts. !$#cross-references MUID:91315421; PMID:1713446 !$#accession S17180 !'##molecule_type mRNA !'##residues 1-595 ##label DUM !'##cross-references EMBL:X57073; NID:g21233; PIDN:CAA40356.1; !1PID:g21234 !$#accession S23644 !'##molecule_type protein !'##residues 73-88 ##label DUM1 CLASSIFICATION #superfamily plant ketol-acid reductoisomerase; ketol-acid !1reductoisomerase homology KEYWORDS chloroplast; intramolecular transferase; isoleucine-valine !1biosynthesis; isomerase; oxidoreductase; tetramer FEATURE !$1-72 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$73-595 #product ketol-acid reductoisomerase #status !8experimental #label MAT\ !$129-327 #domain ketol-acid reductoisomerase homology #label !8KAR SUMMARY #length 595 #molecular-weight 63754 #checksum 2107 SEQUENCE /// ENTRY S30145 #type complete TITLE ketol-acid reductoisomerase (EC 1.1.1.86) precursor - Arabidopsis thaliana ALTERNATE_NAMES acetohydroxy acid isomeroreductase ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S30145; S34040; S36884 REFERENCE S30145 !$#authors Curien, G.; Dumas, R.; Douce, R. !$#journal Plant Mol. Biol. (1993) 21:717-722 !$#title Nucleotide sequence and characterization of a cDNA encoding !1the acetohydroxy acid isomeroreductase from Arabidopsis !1thaliana. !$#cross-references MUID:93192533; PMID:8448371 !$#accession S30145 !'##molecule_type mRNA !'##residues 1-591 ##label CUR !'##cross-references EMBL:X68150 REFERENCE S34040 !$#authors Dumas, R. !$#submission submitted to the EMBL Data Library, July 1992 !$#accession S34040 !'##molecule_type mRNA !'##residues 1-284,'R',286-591 ##label DUM !'##cross-references EMBL:X68150; NID:g288062; PIDN:CAA48253.1; !1PID:g288063 REFERENCE S36884 !$#authors Dumas, R.; Curien, G.; DeRose, R.T.; Douce, R. !$#journal Biochem. J. (1993) 294:821-828 !$#title Branched-chain-amino-acid biosynthesis in plants: molecular !1cloning and characterization of the gene encoding !1acetohydroxy acid isomeroreductase (ketol-acid !1reductoisomerase) from Arabidopsis thaliana (thale cress). !$#cross-references MUID:93393563; PMID:8379936 !$#accession S36884 !'##molecule_type DNA !'##residues 1-578,'A',580-591 ##label DU2 !'##cross-references EMBL:X69880; NID:g402551; PIDN:CAA49506.1; !1PID:g402552 GENETICS !$#genome nuclear !$#introns 99/3; 130/3; 152/3; 199/3; 275/3; 315/1; 361/3; 417/3; 469/3 CLASSIFICATION #superfamily plant ketol-acid reductoisomerase; ketol-acid !1reductoisomerase homology KEYWORDS chloroplast; intramolecular transferase; isoleucine-valine !1biosynthesis; isomerase; oxidoreductase FEATURE !$1-67 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$68-591 #product ketol-acid reductoisomerase #status !8predicted #label MAT\ !$123-321 #domain ketol-acid reductoisomerase homology #label !8KAR SUMMARY #length 591 #molecular-weight 63840 #checksum 3243 SEQUENCE /// ENTRY A24709 #type complete TITLE ketol-acid reductoisomerase (EC 1.1.1.86) ILV5 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES acetohydroxyacid reductoisomerase ILV5; protein L9638.7; protein YLR355c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A24709; S51463 REFERENCE A24709 !$#authors Petersen, J.G.L.; Holmberg, S. !$#journal Nucleic Acids Res. (1986) 14:9631-9651 !$#title The ILV5 gene of Saccharomyces cerevisiae is highly !1expressed. !$#cross-references MUID:87117524; PMID:3027658 !$#accession A24709 !'##molecule_type DNA !'##residues 1-395 ##label PET !'##cross-references EMBL:X04969; NID:g3826; PIDN:CAA28643.1; PID:g3827 REFERENCE S51459 !$#authors Du, Z. !$#submission submitted to the EMBL Data Library, December 1994 !$#description The sequence of S. cerevisiae cosmid 9638. !$#accession S51463 !'##molecule_type DNA !'##residues 1-395 ##label DUZ !'##cross-references EMBL:U19102; NID:g609396; PIDN:AAB67753.1; !1PID:g609403; GSPDB:GN00012; MIPS:YLR355c GENETICS !$#gene SGD:ILV5; MIPS:YLR355c !'##cross-references SGD:S0004347; MIPS:YLR355c !$#map_position 12R CLASSIFICATION #superfamily yeast ketol-acid reductoisomerase; ketol-acid !1reductoisomerase homology KEYWORDS intramolecular transferase; isoleucine-valine biosynthesis; !1isomerase; mitochondrion; oxidoreductase FEATURE !$81-267 #domain ketol-acid reductoisomerase homology #label !8KAR SUMMARY #length 395 #molecular-weight 44368 #checksum 8344 SEQUENCE /// ENTRY JC1428 #type complete TITLE ketol-acid reductoisomerase (EC 1.1.1.86) - Neurospora crassa ALTERNATE_NAMES alpha-keto-beta-hydroxylacyl reductoisomerase ORGANISM #formal_name Neurospora crassa DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JC1428 REFERENCE JC1428 !$#authors Sista, H.; Bowman, B. !$#journal Gene (1992) 120:115-118 !$#title Characterization of the ilv-2 gene from Neurospora crassa !1encoding alpha-keto-beta-hydroxylacyl reductoisomerase. !$#cross-references MUID:93013010; PMID:1398116 !$#accession JC1428 !'##molecule_type DNA !'##residues 1-400 ##label SIS !'##cross-references GB:M84189; NID:g168821; PIDN:AAB00797.1; !1PID:g168822 GENETICS !$#gene ilv-2 !$#map_position V !$#introns 68/1; 78/3; 170/3; 392/3 CLASSIFICATION #superfamily yeast ketol-acid reductoisomerase; ketol-acid !1reductoisomerase homology KEYWORDS intramolecular transferase; isoleucine-valine biosynthesis; !1isomerase; mitochondrion; oxidoreductase FEATURE !$87-273 #domain ketol-acid reductoisomerase homology #label !8KAR SUMMARY #length 400 #molecular-weight 44508 #checksum 3064 SEQUENCE /// ENTRY DEKVG #type complete TITLE glycerate dehydrogenase (EC 1.1.1.29) - cucumber ALTERNATE_NAMES NADH-dependent hydroxypyruvate reductase ORGANISM #formal_name Cucumis sativus #common_name cucumber DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 11-Jun-1999 ACCESSIONS S17733; S06617 REFERENCE S17733 !$#authors Schwartz, B.W.; Sloan, J.S.; Becker, W.M. !$#journal Plant Mol. Biol. (1991) 17:941-947 !$#title Characterization of genes encoding hydroxypyruvate reductase !1in cucumber. !$#cross-references MUID:92003707; PMID:1912510 !$#accession S17733 !'##molecule_type DNA !'##residues 1-382 ##label SCH !'##cross-references EMBL:X58542; NID:g18263; PIDN:CAA41434.1; !1PID:g18264 REFERENCE S06617 !$#authors Greenler, J.M.; Sloan, J.S.; Schwartz, B.W.; Becker, W.M. !$#journal Plant Mol. Biol. (1989) 13:139-150 !$#title Isolation, characterization and sequence analysis of a !1full-length cDNA clone encoding NADH-dependent !1hydroxypyruvate reductase from cucumber. !$#cross-references MUID:92003662; PMID:2519111 !$#accession S06617 !'##molecule_type mRNA !'##residues 1-382 ##label GRE !'##cross-references EMBL:X14609; NID:g18274; PIDN:CAA32764.1; !1PID:g18275 !'##note the authors translated the codon CAG for residue 166 as Glu GENETICS !$#gene hpr-A !$#introns 41/3; 69/3; 116/3; 157/2; 184/3; 209/1; 239/3; 264/3; 300/3; !1326/3; 341/3 CLASSIFICATION #superfamily phosphoglycerate dehydrogenase KEYWORDS NAD; oxidoreductase; photorespiration FEATURE !$166-196 #region beta-alpha-beta NAD nucleotide-binding fold SUMMARY #length 382 #molecular-weight 41706 #checksum 3417 SEQUENCE /// ENTRY DEECPG #type complete TITLE phosphoglycerate dehydrogenase (EC 1.1.1.95) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 01-Mar-2002 ACCESSIONS A25200; B38156; S22096; H65075 REFERENCE A25200 !$#authors Tobey, K.L.; Grant, G.A. !$#journal J. Biol. Chem. (1986) 261:12179-12183 !$#title The nucleotide sequence of the serA gene of Escherichia coli !1and the amino acid sequence of the encoded protein, !1D-3-phosphoglycerate dehydrogenase. !$#cross-references MUID:86304370; PMID:3017965 !$#accession A25200 !'##molecule_type DNA !'##residues 1-410 ##label TOB !'##cross-references GB:L29397; GB:N00029; NID:g459754; PIDN:AAA24625.1; !1PID:g459755 REFERENCE A38156 !$#authors Rex, J.H.; Aronson, B.D.; Somerville, R.L. !$#journal J. Bacteriol. (1991) 173:5944-5953 !$#title The tdh and serA operons of Escherichia coli: mutational !1analysis of the regulatory elements of leucine-responsive !1genes. !$#cross-references MUID:92011350; PMID:1917830 !$#accession B38156 !'##status preliminary !'##molecule_type DNA !'##residues 1-29 ##label REX !'##cross-references GB:M64630; NID:g147807; PIDN:AAA73016.1; !1PID:g551837 REFERENCE S22096 !$#authors Roy, I.; Leadlay, P.F. !$#submission submitted to the EMBL Data Library, June 1992 !$#accession S22096 !'##molecule_type DNA !'##residues 1-99 ##label ROY !'##cross-references EMBL:X66836; NID:g42941; PIDN:CAA47308.1; !1PID:g42942 !'##experimental_source strain K12-38 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65075 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-410 ##label BLAT !'##cross-references GB:AE000374; GB:U00096; NID:g1789270; !1PIDN:AAC75950.1; PID:g1789279; UWGP:b2913 !'##experimental_source strain K-12, substrain MG1655 COMMENT The active enzyme is a tetramer of identical chains; it !1catalyzes the first committed step in the "phosphorylated" !1pathway of L-serine biosynthesis by using NAD in the !1conversion of phosphoglyceric acid to !13-phosphohydroxypyruvic acid. In bacteria, this enzyme !1displays feedback inhibition by L-serine. GENETICS !$#gene serA !$#map_position 63 min CLASSIFICATION #superfamily phosphoglycerate dehydrogenase KEYWORDS NAD; oxidoreductase; serine biosynthesis FEATURE !$153-181 #region beta-alpha-beta NAD nucleotide-binding fold SUMMARY #length 410 #molecular-weight 44175 #checksum 2093 SEQUENCE /// ENTRY C64070 #type complete TITLE phosphoglycerate dehydrogenase (EC 1.1.1.95) - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C64070 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession C64070 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-410 ##label TIGR !'##cross-references GB:U32729; GB:L42023; NID:g1573439; !1PIDN:AAC22124.1; PID:g1573443; TIGR:HI0465 !'##note named as homolog to a protein from Escherichia coli CLASSIFICATION #superfamily phosphoglycerate dehydrogenase KEYWORDS NAD; oxidoreductase; serine biosynthesis FEATURE !$154-182 #region beta-alpha-beta NAD nucleotide-binding fold SUMMARY #length 410 #molecular-weight 44665 #checksum 1044 SEQUENCE /// ENTRY DELBC #type complete TITLE D-2-hydroxyisocaproate dehydrogenase (EC 1.1.1.-) - Lactobacillus casei ORGANISM #formal_name Lactobacillus casei DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 11-Jun-1999 ACCESSIONS JU0050 REFERENCE JU0050 !$#authors Lerch, H.P.; Bloecker, H.; Kallwass, H.; Hoppe, J.; Tsai, !1H.; Collins, J. !$#journal Gene (1989) 78:47-57 !$#title Cloning, sequencing and expression in Escherichia coli of !1the D-2-hydroxyisocaproate dehydrogenase gene of !1Lactobacillus casei. !$#cross-references MUID:89357502; PMID:2504649 !$#accession JU0050 !'##molecule_type DNA !'##residues 1-335 ##label LER !'##cross-references GB:M26929; NID:g149537; PIDN:AAA25236.1; !1PID:g149538 !'##note 67% of the sequence was confirmed by partial peptide sequencing COMMENT This NAD(H)-dependent enzyme catalyzes the stereospecific !1and reversible reduction of various aliphatic and aromatic !12-ketocarboxylic acids to form the corresponding !1D-2-hydroxycarboxylic acids. CLASSIFICATION #superfamily phosphoglycerate dehydrogenase KEYWORDS NAD; oxidoreductase FEATURE !$146-175 #region beta-alpha-beta NAD nucleotide-binding fold SUMMARY #length 335 #molecular-weight 37357 #checksum 1971 SEQUENCE /// ENTRY DEECPP #type complete TITLE probable erythronate-4-phosphate dehydrogenase (EC 1.1.1.-) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 01-Mar-2002 ACCESSIONS JV0051; I54872; F65004 REFERENCE JV0051 !$#authors Schoenlein, P.V.; Roa, B.B.; Winkler, M.E. !$#journal J. Bacteriol. (1989) 171:6084-6092 !$#title Divergent transcription of pdxB and homology between the !1pdxB and serA gene products in Escherichia coli K-12. !$#cross-references MUID:90036695; PMID:2681152 !$#accession JV0051 !'##molecule_type DNA !'##residues 1-378 ##label SCH !'##cross-references GB:M29962; NID:g147122; PIDN:AAA24308.1; !1PID:g147124 REFERENCE I54872 !$#authors Arps, P.J.; Winkler, M.E. !$#journal J. Bacteriol. (1987) 169:1061-1070 !$#title Structural analysis of the Escherichia coli K-12 hisT operon !1by using a kanamycin resistance cassette. !$#cross-references MUID:87137258; PMID:3029016 !$#accession I54872 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 273-378 ##label RES !'##cross-references GB:M15541; NID:g147126; PIDN:AAA24310.1; !1PID:g147130 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65004 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-378 ##label BLAT !'##cross-references GB:AE000321; GB:U00096; NID:g1788659; !1PIDN:AAC75380.1; PID:g1788660; UWGP:b2320 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene pdxB !$#map_position 50 min !$#start_codon GTG CLASSIFICATION #superfamily phosphoglycerate dehydrogenase KEYWORDS NAD; oxidoreductase; pyridoxine biosynthesis FEATURE !$117-146 #region beta-alpha-beta NAD nucleotide-binding fold SUMMARY #length 378 #molecular-weight 41367 #checksum 6820 SEQUENCE /// ENTRY S29296 #type complete TITLE D-lactate dehydrogenase (EC 1.1.1.28) - Lactobacillus helveticus ORGANISM #formal_name Lactobacillus helveticus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S29296; S24969 REFERENCE S29296 !$#authors Kochhar, S.; Hottinger, H.; Chuard, N.; Taylor, P.G.; !1Atkinson, T.; Scawen, M.D.; Nicholls, D.J. !$#journal Eur. J. Biochem. (1992) 208:799-805 !$#title Cloning and overexpression of Lactobacillus helveticus !1D-lactate dehydrogenase gene in Escherichia coli. !$#cross-references MUID:93011111; PMID:1396685 !$#accession S29296 !'##molecule_type DNA !'##residues 1-337 ##label KOC !'##cross-references EMBL:X66723; NID:g43996; PIDN:CAA47255.1; !1PID:g43997 COMMENT This enzyme catalyzes the conversion of pyruvate to !1D-lactate. CLASSIFICATION #superfamily phosphoglycerate dehydrogenase KEYWORDS homodimer; NAD; oxidoreductase FEATURE !$147-176 #region beta-alpha-beta NAD nucleotide-binding fold SUMMARY #length 337 #molecular-weight 37779 #checksum 7445 SEQUENCE /// ENTRY A38094 #type complete TITLE D-lactate dehydrogenase (EC 1.1.1.28) - Lactobacillus delbrueckii subsp. bulgaricus ORGANISM #formal_name Lactobacillus delbrueckii subsp. bulgaricus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A38094; JN0245; S17556; A61517 REFERENCE A38094 !$#authors Kochhar, S.; Hunziker, P.E.; Leong-Morgenthaler, P.; !1Hottinger, H. !$#journal J. Biol. Chem. (1992) 267:8499-8513 !$#title Primary structure, physicochemical properties, and chemical !1modification of NAD(+)-dependent D-lactate dehydrogenase. !1Evidence for the presence of Arg-235, His-303, Tyr-101, and !1Trp-19 at or near the active site. !$#cross-references MUID:92235079; PMID:1569100 !$#accession A38094 !'##molecule_type DNA !'##residues 1-333 ##label KOC !'##cross-references GB:M85224; NID:g149576; PIDN:AAA25246.1; !1PID:g149577 REFERENCE JN0245 !$#authors Kochhar, S.; Chuard, N.; Hottinger, H. !$#journal Biochem. Biophys. Res. Commun. (1992) 185:705-712 !$#title Cloning and overexpression of the Lactobacillus bulgaricus !1NAD+-dependent D-lactate dehydrogenase gene in Escherichia !1coli: purification and characterization of the recombinant !1enzyme. !$#cross-references MUID:92304298; PMID:1610363 !$#accession JN0245 !'##molecule_type DNA !'##residues 1-272,'W',274-310,'I',312-320,'I',322-333 ##label KO2 !'##cross-references EMBL:M85224 REFERENCE S17556 !$#authors Bernard, N.; Ferain, T.; Garmyn, D.; Hols, P.; Delcour, J. !$#journal FEBS Lett. (1991) 290:61-64 !$#title Cloning of the D-lactate dehydrogenase gene from !1Lactobacillus delbrueckii subsp. bulgaricus by !1complementation in Escherichia coli. !$#cross-references MUID:92008688; PMID:1915894 !$#accession S17556 !'##molecule_type DNA !'##residues 1-40,'V',42-116,'A',118-121,'D',123-151,'I',153-173,'T', !1175-219,'E',221-253,'I',255-267,'I',269-272,'W',274-333 !1##label BER !'##cross-references EMBL:X60220; NID:g43982; PIDN:CAA42781.1; !1PID:g43983 REFERENCE A61517 !$#authors Garel, J.R. !$#journal FEMS Microbiol. Lett. (1991) 79:89-94 !$#title Properties of D-lactate dehydrogenase from Lactobacillus !1bulgaricus: a possible different evolutionary origin for the !1D- and L-lactate dehydrogenases. !$#accession A61517 !'##molecule_type protein !'##residues 2-29,'G',31-39,'NX',42-48,'R',50-51 ##label GAR COMMENT This enzyme catalyzes the conversion of pyruvate to !1D-lactate. CLASSIFICATION #superfamily phosphoglycerate dehydrogenase KEYWORDS homodimer; NAD; oxidoreductase FEATURE !$147-176 #region beta-alpha-beta NAD nucleotide-binding fold SUMMARY #length 333 #molecular-weight 36904 #checksum 1950 SEQUENCE /// ENTRY A40885 #type complete TITLE D-lactate dehydrogenase (EC 1.1.1.28) - Lactobacillus pentosus (ATCC 8041) ORGANISM #formal_name Lactobacillus pentosus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A40885 REFERENCE A40885 !$#authors Taguchi, H.; Ohta, T. !$#journal J. Biol. Chem. (1991) 266:12588-12594 !$#title D-lactate dehydrogenase is a member of the D-isomer-specific !12-hydroxyacid dehydrogenase family. Cloning, sequencing, and !1expression in Escherichia coli of the D-lactate !1dehydrogenase gene of Lactobacillus plantarum. !$#cross-references MUID:91286290; PMID:1840590 !$#accession A40885 !'##molecule_type DNA !'##residues 1-332 ##label TAG !'##cross-references GB:D90339; NID:g216745; PIDN:BAA14352.1; !1PID:g216746 !'##note the source designation Lactobacillus plantarum is inconsistent !1with ATCC number 8041; see reference A36957 for discussion CLASSIFICATION #superfamily phosphoglycerate dehydrogenase KEYWORDS NAD; oxidoreductase FEATURE !$147-175 #region beta-alpha-beta NAD nucleotide-binding fold SUMMARY #length 332 #molecular-weight 37183 #checksum 9220 SEQUENCE /// ENTRY C69705 #type complete TITLE phosphoglycerate dehydrogenase (EC 1.1.1.95) serA - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS C69705; S45534 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69705 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-525 ##label KUN !'##cross-references GB:Z99116; GB:AL009126; NID:g2634723; !1PIDN:CAB14239.1; PID:g2634742 !'##experimental_source strain 168 REFERENCE S45533 !$#authors Sorokin, A.; Zumstein, E.; Azevedo, V.; Ehrlich, S.D.; !1Serror, P. !$#submission submitted to the EMBL Data Library, November 1993 !$#accession S45534 !'##molecule_type DNA !'##residues 107-525 ##label SOR !'##cross-references EMBL:L09228; NID:g410114; PIDN:AAA67502.1; !1PID:g410116 GENETICS !$#gene serA CLASSIFICATION #superfamily Bacillus phosphoglycerate dehydrogenase KEYWORDS oxidoreductase SUMMARY #length 525 #molecular-weight 57115 #checksum 1057 SEQUENCE /// ENTRY S75325 #type complete TITLE dihydrokaempferol 4-reductase (EC 1.1.1.219) - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES dihydroflavonol 4-reductase; protein slr1706 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 16-Jun-2000 ACCESSIONS S75325 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75325 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-343 ##label KAN !'##cross-references EMBL:D90904; GB:AB001339; NID:g1652225; !1PIDN:BAA17239.1; PID:g1652316 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene dfrA !$#start_codon GTG CLASSIFICATION #superfamily Synechocystis dihydrokaempferol 4-reductase; !1UDPglucose 4-epimerase homology KEYWORDS oxidoreductase FEATURE !$13-343 #domain UDPglucose 4-epimerase homology #label UDP SUMMARY #length 343 #molecular-weight 37864 #checksum 7516 SEQUENCE /// ENTRY DEHUHS #type complete TITLE 3beta-hydroxy-Delta5-steroid dehydrogenase multifunctional protein I [validated] - human ALTERNATE_NAMES 3 beta-hydroxysteroid dehydrogenase/delta 5-delta 4 isomerase; progesterone reductase CONTAINS 3beta-hydroxy-Delta5-steroid dehydrogenase (EC 1.1.1.145); steroid Delta-isomerase (EC 5.3.3.1) ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 08-Dec-2000 ACCESSIONS A36551; A37400; A32746; A23657; A61454; S30509; I56327 REFERENCE A36551 !$#authors Lorence, M.C.; Corbin, C.J.; Kamimura, N.; Mahendroo, M.S.; !1Mason, J.I. !$#journal Mol. Endocrinol. (1990) 4:1850-1855 !$#title Structural analysis of the gene encoding human !13beta-hydroxysteroid dehydrogenase/Delta(5->4)-isomerase. !$#cross-references MUID:91186993; PMID:2082186 !$#accession A36551 !'##molecule_type DNA !'##residues 1-373 ##label LOR !'##cross-references GB:M63395 !'##experimental_source liver REFERENCE A37400 !$#authors Lorence, M.C.; Murry, B.A.; Trant, J.M.; Mason, J.I. !$#journal Endocrinology (1990) 126:2493-2498 !$#title Human 3beta-hydroxysteroid dehydrogenase/delta(5)-> !1(4)isomerase from placenta: expression in nonsteroidogenic !1cells of a protein that catalyzes the dehydrogenation/ !1isomerization of C21 and C19 steroids. !$#cross-references MUID:90228249; PMID:2139411 !$#accession A37400 !'##molecule_type mRNA !'##residues 1-373 ##label LOR2 !'##cross-references GB:M35493; NID:g177190; PIDN:AAA51538.1; !1PID:g177191 REFERENCE A32746 !$#authors Luu The, V.; Lachance, Y.; Labrie, C.; Leblanc, G.; Thomas, !1J.L.; Strickler, R.C.; Labrie, F. !$#journal Mol. Endocrinol. (1989) 3:1310-1312 !$#title Full length cDNA structure and deduced amino acid sequence !1of human 3beta-hydroxy-5-ene steroid dehydrogenase. !$#cross-references MUID:89384668; PMID:2779585 !$#accession A32746 !'##molecule_type mRNA !'##residues 1-373 ##label LUU !'##cross-references GB:M27137; NID:g184398; PIDN:AAA36015.1; !1PID:g306889 REFERENCE A23657 !$#authors Lachance, Y.; Luu-The, V.; Labrie, C.; Simard, J.; Dumont, !1M.; de Launoit, Y.; Guerin, S.; Leblanc, G.; Labrie, F. !$#journal J. Biol. Chem. (1990) 265:20469-20475 !$#title Characterization of human 3beta-hydroxysteroid !1dehydrogenase/Delta(5)-Delta(4)-isomerase gene and its !1expression in mammalian cells. !$#cross-references MUID:91056097; PMID:2243100 !$#accession A23657 !'##molecule_type DNA !'##residues 1-366,'N',368-373 ##label LAC !'##cross-references GB:M38178; GB:M38179; GB:M38180; NID:g179467; !1PIDN:AAA51831.1; PID:g179468 REFERENCE A61454 !$#authors Thomas, J.L.; Myers, R.P.; Strickler, R.C. !$#journal J. Steroid Biochem. (1989) 33:209-217 !$#title Human placental 3beta-hydroxy-5-ene-steroid dehydrogenase !1and steroid 5->4-ene-isomerase: purification from !1mitochondria and kinetic profiles, biophysical !1characterization of the purified mitochondrial and !1microsomal enzymes. !$#cross-references MUID:89363421; PMID:2770297 !$#accession A61454 !'##molecule_type protein !'##residues 2-30 ##label THO !'##note microsomal and mitochondrial enzymes are identical REFERENCE S30509 !$#authors Nickson, D.A.; McBride, M.; Zeinali, S.; Hawes, C.; !1Petropoulos, A.; Mueller, U.W.; Sutcliffe, R.G. !$#submission submitted to the EMBL Data Library, October 1990 !$#accession S30509 !'##status preliminary !'##molecule_type DNA !'##residues 1-373 ##label NIC !'##cross-references EMBL:X55997; NID:g23861; PIDN:CAA39469.1; !1PID:g23862 REFERENCE I56327 !$#authors Dumont, M.; Van, L.T.; Dupont, E.; Pelletier, G.; Labrie, F. !$#journal J. Invest. Dermatol. (1992) 99:415-421 !$#title Characterization, expression, and immunohistochemical !1localization of 3 beta-hydroxysteroid dehydrogenase/delta !15-delta 4 isomerase in human skin. !$#cross-references MUID:93018017; PMID:1401999 !$#accession I56327 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-373 ##label RES !'##cross-references GB:S45679; NID:g257052; PIDN:AAB23543.1; !1PID:g257053 !'##experimental_source skin COMMENT Two isozymes, I and II, are found in human. Isozyme I is !1almost exclusively in the placenta and skin and also !1predominately in mammary gland tissue. GENETICS !$#gene GDB:HSD3B1 !'##cross-references GDB:120056; OMIM:109715 !$#map_position 1p13.1-1p13.1 !$#introns 49/1; 104/1 COMPLEX homodimer FUNCTION !$#description catalyzes the conversion of Delta5-ene-3beta-hydroxy steroid !1precursors into Delta4-3-ketosteroids !$#pathway steroidogenesis !$#note crucial for the biosynthesis of all classes of hormonal !1steroids !$#note deficiency causes severe reduction of steroid formation by !1the adrenals and gonads and is usually lethal in early life CLASSIFICATION #superfamily 3beta-hydroxy-Delta5-steroid dehydrogenase KEYWORDS homodimer; intramolecular oxidoreductase; isomerase; NAD; !1oxidoreductase; steroid biosynthesis; transmembrane protein FEATURE !$2-373 #product 3beta-hydroxy-Delta5-steroid dehydrogenase !8multifunctional protein #status experimental #label !8MAT SUMMARY #length 373 #molecular-weight 42251 #checksum 714 SEQUENCE /// ENTRY DEHUH2 #type complete TITLE 3beta-hydroxy-Delta5-steroid dehydrogenase multifunctional protein II - human ALTERNATE_NAMES progesterone reductase CONTAINS 3beta-hydroxy-Delta5-steroid dehydrogenase (EC 1.1.1.145); steroid Delta-isomerase (EC 5.3.3.1) ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 11-Jun-1999 ACCESSIONS A39488; A40379; I58105; I78391 REFERENCE A39488 !$#authors Lachance, Y.; Luu-The, V.; Verreault, H.; Dumont, M.; !1Rheaume, E.; Leblanc, G.; Labrie, F. !$#journal DNA Cell Biol. (1991) 10:701-711 !$#title Structure of the human type II 3beta-hydroxysteroid !1dehydrogenase/Delta(5)-Delta(4) isomerase (3beta-HSD) gene: !1adrenal and gonadal specificity. !$#cross-references MUID:92075161; PMID:1741954 !$#accession A39488 !'##molecule_type DNA !'##residues 1-372 ##label LAC !'##cross-references GB:M77144; NID:g184396; PIDN:AAA36014.1; !1PID:g184397 !'##note the authors translated the codon GAC for residue 74 as Asn REFERENCE A40379 !$#authors Rheaume, E.; Lachance, Y.; Zhao, H.F.; Breton, N.; Dumont, !1M.; de Launoit, Y.; Trudel, C.; Luu-The, V.; Simard, J.; !1Labrie, F. !$#journal Mol. Endocrinol. (1991) 5:1147-1157 !$#title Structure and expression of a new complementary DNA encoding !1the almost exclusive 3beta-hydroxysteroid dehydrogenase/ !1Delta(5)-Delta(4)-isomerase in human adrenals and gonads. !$#cross-references MUID:92049394; PMID:1944309 !$#accession A40379 !'##molecule_type mRNA !'##residues 1-372 ##label RHE !'##cross-references GB:M67466; NID:g184400; PIDN:AAA36016.1; !1PID:g184401 REFERENCE I58105 !$#authors Rheaume, E.; Simard, J.; Morel, Y.; Mebarki, F.; Zachmann, !1M.; Forest, M.G.; New, M.I.; Labrie, F. !$#journal Nature Genet. (1992) 1:239-245 !$#title Congenital adrenal hyperplasia due to point mutations in the !1type II 3 beta-hydroxysteroid dehydrogenase gene. !$#cross-references MUID:93250999; PMID:1363812 !$#accession I58105 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 167-205 ##label RES !'##cross-references GB:S60309; NID:g300243; PIDN:AAC60599.1; !1PID:g300244 !'##note normal form !$#accession I78391 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 167-186,'HIYLWGRRPIPFCQYK' ##label RE2 !'##cross-references GB:S60310; NID:g300245; PIDN:AAC60600.1; !1PID:g300246 !'##note mutant form COMMENT Two isozymes, I and II, are found in human. Isozyme II is !1found almost exclusively in the adrenal gland, ovary, and !1testis. GENETICS !$#gene GDB:HSD3B2 !'##cross-references GDB:134044; OMIM:201810 !$#map_position 1p13.1-1p13.1 !$#introns 48/1; 103/1 FUNCTION !$#description catalyzes the conversion of Delta5-ene-3beta-hydroxy steroid !1precursors into Delta4-3-ketosteroids !$#pathway steroidogenesis !$#note crucial for the biosynthesis of all classes of hormonal !1steroids !$#note deficiency causes severe reduction of steroid formation by !1the adrenals and gonads and is usually lethal in early life CLASSIFICATION #superfamily 3beta-hydroxy-Delta5-steroid dehydrogenase KEYWORDS intramolecular oxidoreductase; isomerase; NAD; !1oxidoreductase; steroid biosynthesis; transmembrane protein FEATURE !$2-372 #product 3beta-hydroxy-Delta5-steroid dehydrogenase !8multifunctional protein II #status predicted #label !8MAT SUMMARY #length 372 #molecular-weight 42052 #checksum 1278 SEQUENCE /// ENTRY DEBOHS #type complete TITLE 3beta-hydroxy-Delta5-steroid dehydrogenase multifunctional protein - bovine ALTERNATE_NAMES progesterone reductase CONTAINS 3beta-hydroxy-Delta5-steroid dehydrogenase (EC 1.1.1.145); steroid Delta-isomerase (EC 5.3.3.1) ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 11-Jun-1999 ACCESSIONS S07102; A40285 REFERENCE S07102 !$#authors Zhao, H.F.; Simard, J.; Labrie, C.; Breton, N.; Rheaume, E.; !1Luu-The, V.; Labrie, F. !$#journal FEBS Lett. (1989) 259:153-157 !$#title Molecular cloning, cDNA structure and predicted amino acid !1sequence of bovine 3beta-hydroxy-5-ene steroid !1dehydrogenase/Delta(5)-Delta(4) isomerase. !$#cross-references MUID:90092517; PMID:2599102 !$#accession S07102 !'##molecule_type mRNA !'##residues 1-373 ##label ZHA !'##cross-references EMBL:X17614; NID:g34; PIDN:CAA35615.1; PID:g35 REFERENCE A40285 !$#authors Rutherfurd, K.J.; Chen, S.; Shively, J.E. !$#journal Biochemistry (1991) 30:8108-8116 !$#title Isolation and amino acid sequence analysis of bovine adrenal !13beta-hydroxysteroid dehydrogenase/steroid isomerase. !$#cross-references MUID:91329389; PMID:1868086 !$#accession A40285 !'##molecule_type protein !'##residues 2-121;136-159;165-283;311-332;334-350;353-369 ##label RUT COMMENT This complex enzyme catalyzes the conversion of !1Delta5-ene-3beta-hydroxy steroid precursors into !1Delta4-3-ketosteroids; its function is crucial for the !1biosynthesis of hormones and steroids. Deficiency in this !1enzyme system causes severe reduction of steroid formation !1by the adrenals and gonads and is usually lethal in early !1life. CLASSIFICATION #superfamily 3beta-hydroxy-Delta5-steroid dehydrogenase KEYWORDS intramolecular oxidoreductase; isomerase; NAD; !1oxidoreductase; steroid biosynthesis; transmembrane protein FEATURE !$2-373 #product 3beta-hydroxy-Delta5-steroid dehydrogenase !8multifunctional protein #status experimental #label !8MAT SUMMARY #length 373 #molecular-weight 42219 #checksum 696 SEQUENCE /// ENTRY DERTH1 #type complete TITLE 3beta-hydroxy-Delta5-steroid dehydrogenase multifunctional protein I - rat ALTERNATE_NAMES progesterone reductase CONTAINS 3beta-hydroxy-Delta5-steroid dehydrogenase (EC 1.1.1.145); steroid Delta-isomerase (EC 5.3.3.1) ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 11-Jun-1999 ACCESSIONS A39051; A61401 REFERENCE A39051 !$#authors Zhao, H.F.; Labrie, C.; Simard, J.; de Launoit, Y.; Trudel, !1C.; Martel, C.; Rheaume, E.; Dupont, E.; Luu-The, V.; !1Pelletier, G.; Labrie, F. !$#journal J. Biol. Chem. (1991) 266:583-593 !$#title Characterization of rat 3beta-hydroxysteroid dehydrogenase/ !1Delta(5)-Delta(4) isomerase cDNAs and differential !1tissue-specific expression of the corresponding mRNAs in !1steroidogenic and peripheral tissues. !$#cross-references MUID:91093186; PMID:1985917 !$#accession A39051 !'##molecule_type mRNA !'##residues 1-373 ##label ZHA !'##cross-references GB:M38178; NID:g531215; PIDN:AAA63474.1; !1PID:g202531 REFERENCE A61401 !$#authors Lorence, M.C.; Naville, D.; Graham-Lorence, S.E.; Mack, !1S.O.; Murry, B.A.; Trant, J.M.; Mason, J.I. !$#journal Mol. Cell. Endocrinol. (1991) 80:21-31 !$#title 3beta-hydroxysteroid dehydrogenase/delta(5->4)-isomerase !1expression in rat and characterization of the testis !1isoform. !$#cross-references MUID:92064139; PMID:1955079 !$#accession A61401 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-373 ##label LOR !'##experimental_source testis COMMENT This complex enzyme catalyzes the conversion of !1Delta5-ene-3beta-hydroxy steroid precursors into !1Delta4-3-ketosteroids; its function is crucial for the !1biosynthesis of hormones and steroids. Deficiency in this !1enzyme system causes severe reduction of steroid formation !1by the adrenals and gonads and is usually lethal in early !1life. CLASSIFICATION #superfamily 3beta-hydroxy-Delta5-steroid dehydrogenase KEYWORDS intramolecular oxidoreductase; isomerase; NAD; !1oxidoreductase; steroid biosynthesis; transmembrane protein FEATURE !$2-373 #product 3beta-hydroxy-Delta5-steroid dehydrogenase !8multifunctional protein I #status predicted #label !8MAT SUMMARY #length 373 #molecular-weight 42037 #checksum 487 SEQUENCE /// ENTRY DERTH2 #type complete TITLE 3beta-hydroxy-Delta5-steroid dehydrogenase multifunctional protein II - rat ALTERNATE_NAMES progesterone reductase CONTAINS 3beta-hydroxy-Delta5-steroid dehydrogenase (EC 1.1.1.145); steroid Delta-isomerase (EC 5.3.3.1) ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 11-Jun-1999 ACCESSIONS B39051 REFERENCE A39051 !$#authors Zhao, H.F.; Labrie, C.; Simard, J.; de Launoit, Y.; Trudel, !1C.; Martel, C.; Rheaume, E.; Dupont, E.; Luu-The, V.; !1Pelletier, G.; Labrie, F. !$#journal J. Biol. Chem. (1991) 266:583-593 !$#title Characterization of rat 3beta-hydroxysteroid dehydrogenase/ !1Delta(5)-Delta(4) isomerase cDNAs and differential !1tissue-specific expression of the corresponding mRNAs in !1steroidogenic and peripheral tissues. !$#cross-references MUID:91093186; PMID:1985917 !$#accession B39051 !'##molecule_type mRNA !'##residues 1-373 ##label ZHA !'##cross-references GB:M38179; NID:g531216; PIDN:AAA63475.1; !1PID:g202533 COMMENT This complex enzyme catalyzes the conversion of !1Delta5-ene-3beta-hydroxy steroid precursors into !1Delta4-3-ketosteroids; its function is crucial for the !1biosynthesis of hormones and steroids. Deficiency in this !1enzyme system causes severe reduction of steroid formation !1by the adrenals and gonads and is usually lethal in early !1life. CLASSIFICATION #superfamily 3beta-hydroxy-Delta5-steroid dehydrogenase KEYWORDS intramolecular oxidoreductase; isomerase; NAD; !1oxidoreductase; steroid biosynthesis; transmembrane protein FEATURE !$2-373 #product 3beta-hydroxy-Delta5-steroid dehydrogenase !8multifunctional protein II #status predicted #label !8MAT SUMMARY #length 373 #molecular-weight 42276 #checksum 2086 SEQUENCE /// ENTRY DERTHM #type complete TITLE 3beta-hydroxy-Delta5-steroid dehydrogenase multifunctional protein, male-specific microsomal - rat ALTERNATE_NAMES progesterone reductase CONTAINS 3beta-hydroxy-Delta5-steroid dehydrogenase (EC 1.1.1.145); steroid Delta-isomerase (EC 5.3.3.1) ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 11-Jun-1999 ACCESSIONS A40378 REFERENCE A40378 !$#authors Naville, D.; Keeney, D.S.; Jenkin, G.; Murry, B.A.; Head, !1J.R.; Mason, J.I. !$#journal Mol. Endocrinol. (1991) 5:1090-1100 !$#title Regulation of expression of male-specific rat liver !1microsomal 3beta-hydroxysteroid dehydrogenase. !$#cross-references MUID:92049388; PMID:1944305 !$#accession A40378 !'##molecule_type mRNA !'##residues 1-373 ##label NAV !'##cross-references GB:S63167; NID:g238335; PIDN:AAB20228.1; !1PID:g238336 !'##experimental_source liver COMMENT This is a male-specific liver microsomal protein. !1Immunoreactive protein was not detected in liver of immature !1rats of either sex or in adult female liver. CLASSIFICATION #superfamily 3beta-hydroxy-Delta5-steroid dehydrogenase KEYWORDS intramolecular oxidoreductase; isomerase; microsome; NAD; !1oxidoreductase; steroid biosynthesis; transmembrane protein FEATURE !$2-373 #product 3beta-hydroxy-Delta5-steroid dehydrogenase !8multifunctional protein II #status predicted #label !8MAT SUMMARY #length 373 #molecular-weight 42292 #checksum 3975 SEQUENCE /// ENTRY WMVZ1W #type complete TITLE 3beta-hydroxy-Delta5-steroid dehydrogenase multifunctional protein - vaccinia virus (strain Copenhagen) CONTAINS 3beta-hydroxy-Delta5-steroid dehydrogenase (EC 1.1.1.145); steroid Delta-isomerase (EC 5.3.3.1) ORGANISM #formal_name vaccinia virus #note host Homo sapiens (man) DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 11-Jun-1999 ACCESSIONS A42522 REFERENCE A42501 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:517-563 !$#title Appendix to "The complete DNA sequence of vaccinia virus". !$#accession A42522 !'##molecule_type DNA !'##residues 1-346 ##label GOE !'##cross-references GB:M35027; NID:g335317; PIDN:AAA48175.1; !1PID:g335523 !'##experimental_source strain Copenhagen REFERENCE A42531 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:247-266 !$#title The complete DNA sequence of vaccinia virus. !$#cross-references MUID:91021027; PMID:2219722 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given CLASSIFICATION #superfamily 3beta-hydroxy-Delta5-steroid dehydrogenase KEYWORDS intramolecular oxidoreductase; isomerase; NAD; !1oxidoreductase; steroid biosynthesis SUMMARY #length 346 #molecular-weight 39366 #checksum 1297 SEQUENCE /// ENTRY WMVZ2W #type complete TITLE 3beta-hydroxy-Delta5-steroid dehydrogenase multifunctional protein - vaccinia virus (strain WR) ALTERNATE_NAMES SalF7L protein CONTAINS 3beta-hydroxy-Delta5-steroid dehydrogenase (EC 1.1.1.145); steroid Delta-isomerase (EC 5.3.3.1) ORGANISM #formal_name vaccinia virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jun-2000 ACCESSIONS E40897; JQ1782 REFERENCE A40897 !$#authors Blasco, R.; Cole, N.B.; Moss, B. !$#journal J. Virol. (1991) 65:4598-4608 !$#title Sequence analysis, expression, and deletion of a vaccinia !1virus gene encoding a homolog of profilin, a eukaryotic !1actin-binding protein. !$#cross-references MUID:91332999; PMID:1870190 !$#accession E40897 !'##molecule_type DNA !'##residues 1-346 ##label BLA !'##cross-references GB:M72474; NID:g335761; PIDN:AAA48311.1; !1PID:g335766 REFERENCE JQ1767 !$#authors Smith, G.L.; Chan, Y.S.; Howard, S.T. !$#journal J. Gen. Virol. (1991) 72:1349-1376 !$#title Nucleotide sequence of 42kbp of vaccinia virus strain WR !1from near the right inverted terminal repeat. !$#cross-references MUID:91259063; PMID:2045793 !$#accession JQ1782 !'##molecule_type DNA !'##residues 1-346 ##label SMI !'##cross-references DDBJ:D11079; NID:g222717; PIDN:BAA01818.1; !1PID:g222733 CLASSIFICATION #superfamily 3beta-hydroxy-Delta5-steroid dehydrogenase KEYWORDS intramolecular oxidoreductase; isomerase; NAD; !1oxidoreductase; steroid biosynthesis SUMMARY #length 346 #molecular-weight 39396 #checksum 2046 SEQUENCE /// ENTRY DEPSGD #type complete TITLE GDPmannose 6-dehydrogenase (EC 1.1.1.132) - Pseudomonas aeruginosa ORGANISM #formal_name Pseudomonas aeruginosa DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 11-Jun-1999 ACCESSIONS S07391; A41774 REFERENCE S07391 !$#authors Deretic, V.; Gill, J.F.; Chakrabarty, A.M. !$#journal Nucleic Acids Res. (1987) 15:4567-4581 !$#title Pseudomonas aeruginosa infection in cystic fibrosis: !1nucleotide sequence and transcriptional regulation of the !1algD gene. !$#cross-references MUID:87231034; PMID:3108855 !$#accession S07391 !'##molecule_type DNA !'##residues 1-436 ##label DER !'##cross-references EMBL:Y00337; NID:g45267; PIDN:CAA68425.1; !1PID:g45268 REFERENCE A41774 !$#authors Roychoudhury, S.; Chakrabarty, K.; Ho, Y.K.; Chakrabarty, !1A.M. !$#journal J. Biol. Chem. (1992) 267:990-996 !$#title Characterization of guanosine diphospho-D-mannose !1dehydrogenase from Pseudomonas aeruginosa. Structural !1analysis by limited proteolyses. !$#cross-references MUID:92112841; PMID:1370473 !$#accession A41774 !'##molecule_type protein !'##residues 1,'X',3-11;'X',280,'F',282-286,'X',288-289;'X',297-299, !1'XX',302-303,'XX',306 ##label ROY GENETICS !$#gene algD !$#map_position 45 min CLASSIFICATION #superfamily GDPmannose dehydrogenase KEYWORDS oxidoreductase FEATURE !$268 #active_site Cys #status predicted SUMMARY #length 436 #molecular-weight 47633 #checksum 1695 SEQUENCE /// ENTRY QQECB8 #type complete TITLE UDP-N-acetylmuramate dehydrogenase (EC 1.1.1.158) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 01-Mar-2002 ACCESSIONS A24029; C65204; S28100 REFERENCE A91525 !$#authors Howard, P.K.; Shaw, J.; Otsuka, A.J. !$#journal Gene (1985) 35:321-331 !$#title Nucleotide sequence of the birA gene encoding the biotin !1operon repressor and biotin holoenzyme synthetase functions !1of Escherichia coli. !$#cross-references MUID:86006282; PMID:3899863 !$#accession A24029 !'##molecule_type DNA !'##residues 1-342 ##label HOW !'##cross-references GB:M10123; NID:g145430; PIDN:AAA23519.1; !1PID:g145431 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65204 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-342 ##label BLAT !'##cross-references GB:AE000471; GB:U00096; NID:g1790404; !1PIDN:AAC76950.1; PID:g1790407; UWGP:b3972 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S28099 !$#authors Brosius, J.; Dull, T.J.; Sleeter, D.D.; Noller, H.F. !$#journal J. Mol. Biol. (1981) 148:107-127 !$#title Gene organization and primary structure of a ribosomal RNA !1operon from Escherichia coli. !$#cross-references MUID:82055570; PMID:7028991 !$#accession S28100 !'##molecule_type DNA !'##residues 1-198 ##label BRO !'##cross-references EMBL:V00348 !'##note the authors translated the codon GAC for residue 169 as Val and !1CTG for residue 180 as Thr GENETICS !$#gene murB !$#map_position 89 min CLASSIFICATION #superfamily UDP-N-acetylmuramate dehydrogenase KEYWORDS oxidoreductase SUMMARY #length 342 #molecular-weight 37851 #checksum 2953 SEQUENCE /// ENTRY G64058 #type complete TITLE UDP-N-acetylmuramate dehydrogenase (EC 1.1.1.158) - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS G64058 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession G64058 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-341 ##label TIGR !'##cross-references GB:U32713; GB:L42023; NID:g1573231; !1PIDN:AAC21934.1; PID:g1573234; TIGR:HI0268 CLASSIFICATION #superfamily UDP-N-acetylmuramate dehydrogenase KEYWORDS oxidoreductase SUMMARY #length 341 #molecular-weight 38344 #checksum 7409 SEQUENCE /// ENTRY DXHUBH #type complete TITLE 11beta-hydroxysteroid dehydrogenase (EC 1.1.1.146) - human ALTERNATE_NAMES corticosteroid 11beta dehydrogenase ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 11-Jun-1999 ACCESSIONS A41173 REFERENCE A41173 !$#authors Tannin, G.M.; Agarwal, A.K.; Monder, C.; New, M.I.; White, !1P.C. !$#journal J. Biol. Chem. (1991) 266:16653-16658 !$#title The human gene for 11beta-hydroxysteroid dehydrogenase. !1Structure, tissue distribution, and chromosomal !1localization. !$#cross-references MUID:91358458; PMID:1885595 !$#accession A41173 !'##molecule_type DNA !'##residues 1-292 ##label TAN !'##cross-references GB:M76665; GB:M68487; NID:g179473; PIDN:AAC31757.1; !1PID:g179475 GENETICS !$#gene GDB:HSD11B1; HSD11B; HSD11 !'##cross-references GDB:128737; OMIM:600713 !$#map_position 1pter-1qter !$#introns 30/1; 73/3; 111/1; 173/1; 221/1 FUNCTION !$#description catalyzes the reversible oxidation of 11beta-hydroxysteroid, !1cortisol, to 11-oxosteroid, cortisone, using NADP as !1coenzyme CLASSIFICATION #superfamily 11beta-hydroxysteroid dehydrogenase; !1short-chain alcohol dehydrogenase homology KEYWORDS endoplasmic reticulum; glycoprotein; oxidoreductase; !1transmembrane protein FEATURE !$2-292 #product 11beta-hydroxysteroid dehydrogenase #status !8predicted #label MAT\ !$2-6 #domain cytoplasmic #status predicted #label CYT\ !$7-24 #domain transmembrane #status predicted #label TMM\ !$25-292 #domain endoplasmic reticulum lumenal #status !8predicted #label LUM\ !$35-214 #domain short-chain alcohol dehydrogenase homology !8#label SADH\ !$78-213 #disulfide_bonds #status predicted\ !$123,162,207 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 292 #molecular-weight 32401 #checksum 5314 SEQUENCE /// ENTRY A55573 #type complete TITLE 11beta-hydroxysteroid dehydrogenase (EC 1.1.1.146) - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 03-Mar-1995 #sequence_revision 03-Mar-1995 #text_change 26-Feb-1999 ACCESSIONS A55573; A44619 REFERENCE A55573 !$#authors Ozols, J. !$#journal J. Biol. Chem. (1995) 270:2305-2312 !$#title Lumenal orientation and post-translational modifications of !1the liver microsomal 11beta-hydroxysteroid dehydrogenase. !$#cross-references MUID:95138203; PMID:7836463 !$#accession A55573 !'##molecule_type protein !'##residues 1-291 ##label OZO FUNCTION !$#description catalyzes the reversible oxidation of 11beta-hydroxysteroid, !1cortisol, to 11-oxosteroid, cortisone, using NADP as !1coenzyme CLASSIFICATION #superfamily 11beta-hydroxysteroid dehydrogenase; !1short-chain alcohol dehydrogenase homology KEYWORDS endoplasmic reticulum; glycoprotein; oxidoreductase; !1transmembrane protein FEATURE !$1-5 #domain cytoplasmic #status predicted #label CYT\ !$6-23 #domain transmembrane #status predicted #label TMM\ !$24-291 #domain endoplasmic reticulum lumenal #status !8predicted #label LUM\ !$34-213 #domain short-chain alcohol dehydrogenase homology !8#label SADH\ !$77-212 #disulfide_bonds #status experimental\ !$122,161,206 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 291 #molecular-weight 31993 #checksum 5412 SEQUENCE /// ENTRY DXRTBH #type complete TITLE 11beta-hydroxysteroid dehydrogenase (EC 1.1.1.146) - rat ALTERNATE_NAMES 11 beta-OHSD; corticosteroid 11beta dehydrogenase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 11-Jun-1999 ACCESSIONS A34430; A45398; A61100; A42331; B42331 REFERENCE A34430 !$#authors Agarwal, A.K.; Monder, C.; Eckstein, B.; White, P.C. !$#journal J. Biol. Chem. (1989) 264:18939-18943 !$#title Cloning and expression of rat cDNA encoding corticosteroid !111beta-dehydrogenase. !$#cross-references MUID:90037015; PMID:2808402 !$#accession A34430 !'##molecule_type mRNA !'##residues 1-287 ##label AGA !'##cross-references GB:J05107; NID:g203349; PIDN:AAA40886.1; !1PID:g203350 REFERENCE A45398 !$#authors Moisan, M.P.; Edwards, C.R.; Seckl, J.R. !$#journal Mol. Endocrinol. (1992) 6:1082-1087 !$#title Differential promoter usage by the rat 11 !1beta-hydroxysteroid dehydrogenase gene. !$#cross-references MUID:92375101; PMID:1508221 !$#accession A45398 !'##molecule_type DNA !'##residues 1-69 ##label MOI !'##cross-references GB:S43333; NID:g254212; PIDN:AAB22993.1; !1PID:g254213 !'##note sequence extracted from NCBI backbone (NCBIN:111828, !1NCBIP:111829) REFERENCE A61100 !$#authors Lakshmi, V.; Monder, C. !$#journal Endocrinology (1988) 123:2390-2398 !$#title Purification and characterization of the corticosteroid !111beta-dehydrogenase component of the rat liver !111beta-hydroxysteroid dehydrogenase complex. !$#cross-references MUID:89004913; PMID:3139396 !$#accession A61100 !'##molecule_type protein !'##residues 1-11,'X',13-38,'R',40,'X',42 ##label LAK !'##note the authors found that the purified protein lacked !1corticosteroid 11beta dehydrogenase activity REFERENCE A42331 !$#authors Krozowski, Z.; Obeyesekere, V.; Smith, R.; Mercer, W. !$#journal J. Biol. Chem. (1992) 267:2569-2574 !$#title Tissue-specific expression of an 11 beta-hydroxysteroid !1dehydrogenase with a truncated N-terminal domain. A !1potential mechanism for differential intracellular !1localization within mineralocorticoid target cells. !$#cross-references MUID:92129344; PMID:1733955 !$#accession A42331 !'##status preliminary !'##molecule_type mRNA !'##residues 1-35 ##label KRO !'##note sequence extracted from NCBI backbone (NCBIN:78538, !1NCBIP:78541) !$#accession B42331 !'##status preliminary !'##molecule_type mRNA !'##residues 27-35 ##label KR2 !'##cross-references GB:M77835; NID:g202520; PIDN:AAA40600.1; !1PID:g202521 !'##note sequence extracted from NCBI backbone (NCBIN:78542, !1NCBIP:78547) FUNCTION !$#description catalyzes the reversible oxidation of 11beta-hydroxysteroid, !1cortisol, to 11-oxosteroid, cortisone, using NADP as !1coenzyme CLASSIFICATION #superfamily 11beta-hydroxysteroid dehydrogenase; !1short-chain alcohol dehydrogenase homology KEYWORDS endoplasmic reticulum; glycoprotein; oxidoreductase; !1transmembrane protein FEATURE !$1-3 #domain cytoplasmic #status predicted #label CYT\ !$4-20 #domain transmembrane #status predicted #label TMM\ !$21-287 #domain endoplasmic reticulum lumenal #status !8predicted #label LUM\ !$31-210 #domain short-chain alcohol dehydrogenase homology !8#label SADH\ !$74-209 #disulfide_bonds #status predicted\ !$158,203 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 287 #molecular-weight 31769 #checksum 8692 SEQUENCE /// ENTRY I56604 #type complete TITLE 11beta-hydroxysteroid dehydrogenase (EC 1.1.1.146) 1 - mouse ALTERNATE_NAMES corticosteroid 11beta dehydrogenase; microsomal carbonyl reductase ORGANISM #formal_name Mus musculus #common_name house mouse DATE 26-Jul-1996 #sequence_revision 26-Jul-1996 #text_change 11-Jun-1999 ACCESSIONS I56604; S67488 REFERENCE I56604 !$#authors Rajan, V.; Chapman, K.E.; Lyons, V.; Jamieson, P.; Mullins, !1J.J.; Edwards, C.R.; Seckl, J.R. !$#journal J. Steroid Biochem. Mol. Biol. (1995) 52:141-147 !$#title Cloning, sequencing and tissue-distribution of mouse 11 !1beta-hydroxysteroid dehydrogenase-1 cDNA. !$#cross-references MUID:95178382; PMID:7873449 !$#accession I56604 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-292 ##label RES !'##cross-references GB:S75207; NID:g806927; PIDN:AAB33601.1; !1PID:g806928 REFERENCE S67488 !$#authors Oppermann, U.C.T.; Netter, K.J.; Maser, E. !$#journal Eur. J. Biochem. (1995) 227:202-208 !$#title Cloning and primary structure of murine !111-beta-hydroxysteroid dehydrogenase/microsomal carbonyl !1reductase. !$#cross-references MUID:95154291; PMID:7851387 !$#accession S67488 !'##molecule_type mRNA !'##residues 1-14,'S',16-231,'D',233,'L',235-260,'L',262-292 ##label OPP !'##cross-references EMBL:X83202; NID:g633241; PIDN:CAA58209.1; !1PID:g633242 FUNCTION !$#description catalyzes the reversible oxidation of 11beta-hydroxysteroid, !1cortisol, to 11-oxosteroid, cortisone, using NADP as !1coenzyme CLASSIFICATION #superfamily 11beta-hydroxysteroid dehydrogenase; !1short-chain alcohol dehydrogenase homology KEYWORDS endoplasmic reticulum; glycoprotein; oxidoreductase; !1transmembrane protein FEATURE !$2-292 #product 11beta-hydroxysteroid dehydrogenase #status !8predicted #label MAT\ !$2-6 #domain cytoplasmic #status predicted #label CYT\ !$7-24 #domain transmembrane #status predicted #label TMM\ !$25-292 #domain endoplasmic reticulum lumenal #status !8predicted #label LUM\ !$35-214 #domain short-chain alcohol dehydrogenase homology !8#label SADH\ !$78-213 #disulfide_bonds #status predicted\ !$162,207 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 292 #molecular-weight 32364 #checksum 3704 SEQUENCE /// ENTRY S33117 #type complete TITLE 11beta-hydroxysteroid dehydrogenase (EC 1.1.1.146) - sheep ALTERNATE_NAMES corticosteroid 11beta dehydrogenase ORGANISM #formal_name Ovis orientalis aries, Ovis ammon aries #common_name domestic sheep DATE 02-Dec-1993 #sequence_revision 10-Nov-1995 #text_change 11-Jun-1999 ACCESSIONS S33117 REFERENCE S33117 !$#authors Yang, K.; Smith, C.L.; Dales, D.; Hammond, G.L.; Challis, !1J.R.G. !$#journal Endocrinology (1992) 131:2120-2126 !$#title Cloning of an ovine 11-beta-hydroxysteroid dehydrogenase !1complementary deoxyribonucleic acid: tissue and temporal !1distribution of its messenger ribonucleic acid during fetal !1and neonatal development. !$#cross-references MUID:93048946; PMID:1425412 !$#accession S33117 !'##molecule_type mRNA !'##residues 1-292 ##label YAN !'##cross-references EMBL:X69561; NID:g1190; PIDN:CAA49290.1; PID:g1191 FUNCTION !$#description catalyzes the reversible oxidation of 11beta-hydroxysteroid, !1cortisol, to 11-oxosteroid, cortisone, using NADP as !1coenzyme CLASSIFICATION #superfamily 11beta-hydroxysteroid dehydrogenase; !1short-chain alcohol dehydrogenase homology KEYWORDS endoplasmic reticulum; glycoprotein; oxidoreductase; !1transmembrane protein FEATURE !$2-292 #product 11beta-hydroxysteroid dehydrogenase #status !8predicted #label MAT\ !$2-6 #domain cytoplasmic #status predicted #label CYT\ !$7-24 #domain transmembrane #status predicted #label TMM\ !$25-292 #domain endoplasmic reticulum lumenal #status !8predicted #label LUM\ !$35-214 #domain short-chain alcohol dehydrogenase homology !8#label SADH\ !$78-213 #disulfide_bonds #status predicted\ !$95,122,207 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 292 #molecular-weight 32153 #checksum 2938 SEQUENCE /// ENTRY XOHUDH #type complete TITLE xanthine dehydrogenase (EC 1.1.1.204) / xanthine oxidase (EC 1.1.3.22) - human ALTERNATE_NAMES hypoxanthine oxidase ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1993 #sequence_revision 07-Feb-1997 #text_change 19-Jan-2001 ACCESSIONS S66573; JC2010; A58497; JC2138; PC2068 REFERENCE S66573 !$#authors Saksela, M.; Raivio, K.O. !$#journal Biochem. J. (1996) 315:235-239 !$#title Cloning and expression in vitro of human xanthine !1dehydrogenase/oxidase. !$#cross-references MUID:96207586; PMID:8670112 !$#accession S66573 !'##molecule_type mRNA !'##residues 1-1333 ##label SAK !'##cross-references EMBL:U39487; NID:g1314286; PIDN:AAB08399.1; !1PID:g1314287 REFERENCE JC2010 !$#authors Ichida, K.; Amaya, Y.; Noda, K.; Minoshima, S.; Hosoya, T.; !1Sakai, O.; Shimizu, N.; Nishino, T. !$#journal Gene (1993) 133:279-284 !$#title Cloning of the cDNA encoding human xanthine dehydrogenase !1(oxidase): structural analysis of the protein and !1chromosomal location of the gene. !$#cross-references MUID:94040824; PMID:8224915 !$#accession JC2010 !'##molecule_type mRNA !'##residues 1-190,'H',192-230,'R',232-1149,'R',1151-1333 ##label ICH !'##cross-references DDBJ:D11456; NID:g452195; PIDN:BAA02013.1; !1PID:g452196 REFERENCE A58497 !$#authors Xu, P.; Huecksteadt, T.P.; Harrison, R.; Hoidal, J.R. !$#journal Biochem. Biophys. Res. Commun. (1995) 215:429 !$#cross-references MUID:96003791; PMID:7575623 !$#contents erratum !$#accession A58497 !'##molecule_type mRNA !'##residues 1-171,'R',173-258,'E',260-332,'HV',335-494,'Q',496-514, !1'LLL',518-1333 ##label XUP !'##cross-references GB:U06117; NID:g984266; PIDN:AAA75287.1; !1PID:g984267 !'##note authors' sequence revision to JC2138 submitted to GenBank REFERENCE JC2138 !$#authors Xu, P.; Huecksteadt, T.P.; Harrison, R.; Hoidal, J.R. !$#journal Biochem. Biophys. Res. Commun. (1994) 199:998-1004 !$#title Molecular cloning, tissue expression of human xanthine !1dehydrogenase. !$#cross-references MUID:94183289; PMID:8135849 !$#accession JC2138 !'##status significant sequence differences !'##molecule_type mRNA !'##cross-references GB:U06117; NID:g984266; PID:g984267 !'##note this sequence revised by A58497 !$#accession PC2068 !'##molecule_type protein !'##residues 1-27 ##label XU2 COMMENT Xanthine dehydrogenase is reversibly converted to xanthine !1oxidase by oxidized glutathione catalyzed by enzyme-thiol !1transhydrogenase (oxidized-glutathione) (EC 1.8.4.7). The !1reversible conversion to xanthine oxidase can also be !1performed artificially by a variety of sulfhydryl reagents. !1An irreversible conversion can be performed by limited !1proteolysis. COMMENT This enzyme contains four cofactors per subunit, one FAD, !1two iron-sulfur clusters, and one molybdopterin. GENETICS !$#gene GDB:XDH !'##cross-references GDB:266386; OMIM:278300 !$#map_position 2p23-2p22 !$#note defects in this gene may cause xanthinuria COMPLEX homodimer FUNCTION XDH !$#description catalyzes oxidation of xanthine to uric acid by NAD+ and !1water !$#pathway purine catabolism FUNCTION XO !$#description catalyzes oxidation of xanthine to uric acid and hydrogen !1peroxide by dioxygen and water !$#pathway purine catabolism CLASSIFICATION #superfamily xanthine dehydrogenase; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; FAD; flavoprotein; homodimer; iron-sulfur protein; !1metalloprotein; molybdenum; molybdopterin; nucleotide !1binding; oxidoreductase; P-loop; peroxisome; phosphoprotein; !1purine catabolism FEATURE !$2-1333 #product xanthine dehydrogenase / xanthine oxidase !8#status predicted #label MAT\ !$26-74 #domain ferredoxin [2Fe-2S] homology #label FER1\ !$389-401 #region NAD binding\ !$796-803 #region nucleotide-binding motif A (P-loop)\ !$43,48,51,73 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted\ !$113,116,148,150 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted\ !$826 #binding_site molybdopterin (Cys) (covalent) #status !8predicted\ !$913 #binding_site molybdopterin (Arg) #status predicted\ !$1262 #active_site Glu #status predicted SUMMARY #length 1333 #molecular-weight 146423 #checksum 3103 SEQUENCE /// ENTRY XORTDH #type complete TITLE xanthine dehydrogenase (EC 1.1.1.204) / xanthine oxidase (EC 1.1.3.22) - rat ALTERNATE_NAMES hypoxanthine oxidase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Apr-1991 #sequence_revision 07-Feb-1997 #text_change 19-Jan-2001 ACCESSIONS A37810; S45259; S45260; S71397; I58308 REFERENCE A37810 !$#authors Amaya, Y.; Yamazaki, K.; Sato, M.; Noda, K.; Nishino, T.; !1Nishino, T. !$#journal J. Biol. Chem. (1990) 265:14170-14175 !$#title Proteolytic conversion of xanthine dehydrogenase from the !1NAD-dependent type to the O-2-dependent type. Amino acid !1sequence of rat liver xanthine dehydrogenase and !1identification of the cleavage sites of the enzyme protein !1during irreversible conversion by trypsin. !$#cross-references MUID:90354396; PMID:2387845 !$#accession A37810 !'##molecule_type mRNA !'##residues 1-478,491-493,'Q',495-1331 ##label AMA !'##cross-references GB:J05579; NID:g207686 !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing REFERENCE I58308 !$#authors Chow, C.W.; Clark, M.; Rinaldo, J.; Chalkley, R. !$#journal Nucleic Acids Res. (1994) 22:1846-1854 !$#title Identification of the rat xanthine dehydrogenase/oxidase !1promoter. !$#cross-references MUID:94268906; PMID:8208609 !$#accession S45259 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 476-494 ##label RES !'##cross-references EMBL:U08123; NID:g473260; PIDN:AAB60444.1; !1PID:g473261 !'##note correction to A37810; sequence thought by authors to be !1macrophage splice form !$#accession S45260 !'##status translation not shown !'##molecule_type DNA !'##residues 1-55 ##label CHO !'##cross-references GB:U08122; NID:g472856; PIDN:AAA18869.1; !1PID:g472858; EMBL:U08121 REFERENCE A55711 !$#authors Sato, A.; Nishino, T.; Noda, K.; Amaya, Y.; Nishino, T. !$#journal J. Biol. Chem. (1995) 270:2818-2826 !$#title The structure of chicken liver xanthine dehydrogenase. cDNA !1cloning and the domain structure. !$#cross-references MUID:95155354; PMID:7852355 !$#contents annotation; confirmation of sequence !$#note the authors confirmed that both liver and macrophage mRNA's !1of the rat have a sequence in accordance with the correction !1in I58308 REFERENCE S71397 !$#authors McManaman, J.L.; Shellman, V.; Wright, R.M.; Repine, J.E. !$#journal Arch. Biochem. Biophys. (1996) 332:135-141 !$#title Purification of rat liver xanthine oxidase and xanthine !1dehydrogenase by affinity chromatography on !1benzamidine-sepharose. !$#cross-references MUID:96400342; PMID:8806718 !$#accession S71397 !'##molecule_type protein !'##residues 2-11 ##label MCM COMMENT Xanthine dehydrogenase is reversibly converted to xanthine !1oxidase by oxidized glutathione catalyzed by enzyme-thiol !1transhydrogenase (oxidized-glutathione) (EC 1.8.4.7). The !1reversible conversion to xanthine oxidase can also be !1performed artificially by a variety of sulfhydryl reagents. !1An irreversible conversion can be performed by limited !1proteolysis. COMMENT This enzyme contains four cofactors per subunit, one FAD, !1two iron-sulfur clusters, and one molybdopterin. GENETICS !$#introns 14/3; 34/1 !$#note the list of introns may be incomplete COMPLEX homodimer FUNCTION XDH !$#description catalyzes oxidation of xanthine to uric acid by NAD+ and !1water !$#pathway purine catabolism FUNCTION XO !$#description catalyzes oxidation of xanthine to uric acid and hydrogen !1peroxide by dioxygen and water !$#pathway purine catabolism CLASSIFICATION #superfamily xanthine dehydrogenase; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; FAD; flavoprotein; homodimer; iron-sulfur protein; !1metalloprotein; molybdenum; molybdopterin; nucleotide !1binding; oxidoreductase; P-loop; peroxisome; phosphoprotein; !1purine catabolism FEATURE !$2-1331 #product xanthine dehydrogenase / xanthine oxidase !8#status experimental #label MAT\ !$26-74 #domain ferredoxin [2Fe-2S] homology #label FER1\ !$795-802 #region nucleotide-binding motif A (P-loop)\ !$43,48,51,73 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted\ !$112,115,147,149 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted\ !$825 #binding_site molybdopterin (Cys) (covalent) #status !8predicted\ !$912 #binding_site molybdopterin (Arg) #status predicted\ !$1261 #active_site Glu #status predicted SUMMARY #length 1331 #molecular-weight 146251 #checksum 2718 SEQUENCE /// ENTRY XOMSDH #type complete TITLE xanthine dehydrogenase (EC 1.1.1.204) / xanthine oxidase (EC 1.1.3.22) - mouse ALTERNATE_NAMES hypoxanthine oxidase ORGANISM #formal_name Mus musculus #common_name house mouse DATE 15-Mar-1996 #sequence_revision 07-Feb-1997 #text_change 19-Jan-2001 ACCESSIONS I48374; S22419; S65134 REFERENCE A55561 !$#authors Cazzaniga, G.; Terao, M.; Lo Schiavo, P.; Galbiati, F.; !1Segalla, F.; Seldin, M.F.; Garattini, E. !$#journal Genomics (1994) 23:390-402 !$#title Chromosomal mapping, isolation, and characterization of the !1mouse xanthine dehydrogenase gene. !$#cross-references MUID:95137585; PMID:7835888 !$#accession I48374 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1335 ##label RES !'##cross-references EMBL:X75129; NID:g473040; PIDN:CAA52997.1; !1PID:g817959 !'##note the sequence and translation are shown only for the splice !1boundaries REFERENCE S22419 !$#authors Terao, M.; Cazzaniga, G.; Ghezzi, P.; Bianchi, M.; Falciani, !1F.; Perani, P.; Garattini, E. !$#journal Biochem. J. (1992) 283:863-870 !$#title Molecular cloning of a cDNA coding for mouse liver xanthine !1dehydrogenase: regulation of its transcript by interferons !1in vivo. !$#cross-references MUID:92272690; PMID:1590774 !$#accession S22419 !'##molecule_type mRNA !'##residues 1-240,'I',242-620,'M',622-1335 ##label TER !'##cross-references EMBL:X62932; NID:g55443; PIDN:CAA44705.1; !1PID:g55444 REFERENCE S65133 !$#authors Ishii, T.; Aoki, N.; Noda, A.; Adachi, T.; Nakamura, R.; !1Matsuda, T. !$#journal Biochim. Biophys. Acta (1995) 1245:285-292 !$#title Carboxy-terminal cytoplasmic domain of mouse butyrophilin !1specifically associates with a 150-kDa protein of mammary !1epithelial cells and milk fat globule membrane. !$#cross-references MUID:96125722; PMID:8541302 !$#accession S65134 !'##molecule_type protein !'##residues 2-9 ##label ISH COMMENT Xanthine dehydrogenase is reversibly converted to xanthine !1oxidase by oxidized glutathione catalyzed by enzyme-thiol !1transhydrogenase (oxidized-glutathione) (EC 1.8.4.7). The !1reversible conversion to xanthine oxidase can also be !1performed artificially by a variety of sulfhydryl reagents. !1An irreversible conversion can be performed by limited !1proteolysis. COMMENT This enzyme contains four cofactors per subunit, one FAD, !1two iron-sulfur clusters, and one molybdopterin. GENETICS !$#gene XDH; XD; XO !$#introns 17/3; 37/1; 69/2; 104/3; 147/1; 167/3; 190/3; 219/3; 267/1; !1298/1; 348/3; 380/1; 416/3; 478/2; 536/3; 564/3; 621/2; 662/ !13; 702/3; 735/1; 776/3; 821/2; 850/3; 879/3; 943/3; 992/2; !11019/3; 1051/3; 1094/3; 1119/3; 1137/2; 1175/3; 1197/3; !11260/3; 1319/3 COMPLEX homodimer FUNCTION XDH !$#description catalyzes oxidation of xanthine to uric acid by NAD+ and !1water !$#pathway purine catabolism FUNCTION XO !$#description catalyzes oxidation of xanthine to uric acid and hydrogen !1peroxide by dioxygen and water !$#pathway purine catabolism CLASSIFICATION #superfamily xanthine dehydrogenase; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; FAD; flavoprotein; homodimer; iron-sulfur protein; !1metalloprotein; molybdenum; molybdopterin; nucleotide !1binding; oxidoreductase; P-loop; peroxisome; phosphoprotein; !1purine catabolism FEATURE !$2-1335 #product xanthine dehydrogenase / xanthine oxidase !8#status predicted #label MAT\ !$29-77 #domain ferredoxin [2Fe-2S] homology #label FER1\ !$798-805 #region nucleotide-binding motif A (P-loop)\ !$46,51,54,76 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted\ !$115,118,150,152 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted\ !$828 #binding_site molybdopterin (Cys) (covalent) #status !8predicted\ !$915 #binding_site molybdopterin (Arg) #status predicted\ !$1264 #active_site Glu #status predicted SUMMARY #length 1335 #molecular-weight 146517 #checksum 5776 SEQUENCE /// ENTRY XOCHDH #type complete TITLE xanthine dehydrogenase (EC 1.1.1.204) - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 03-Mar-1995 #sequence_revision 07-Feb-1997 #text_change 19-Jan-2001 ACCESSIONS A55711; S34758 REFERENCE A55711 !$#authors Sato, A.; Nishino, T.; Noda, K.; Amaya, Y.; Nishino, T. !$#journal J. Biol. Chem. (1995) 270:2818-2826 !$#title The structure of chicken liver xanthine dehydrogenase. cDNA !1cloning and the domain structure. !$#cross-references MUID:95155354; PMID:7852355 !$#accession A55711 !'##molecule_type mRNA !'##residues 1-1358 ##label SAT !'##cross-references DDBJ:D13221; NID:g507879; PIDN:BAA02502.1; !1PID:g507880 !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing REFERENCE S34758 !$#authors Schieber, A.; Edmondson, D.E. !$#journal Eur. J. Biochem. (1993) 215:307-314 !$#title Studies on the induction and phosphorylation of xanthine !1dehydrogenase in cultured chick embryo hepatocytes. !$#cross-references MUID:93345517; PMID:8344298 !$#accession S34758 !'##molecule_type protein !'##residues 2-20 ##label SCH COMMENT This enzyme contains four cofactors per subunit, one FAD, !1two iron-sulfur clusters, and one molybdopterin. COMPLEX homodimer FUNCTION !$#description catalyzes oxidation of xanthine to uric acid by NAD+ and !1water !$#pathway purine catabolism CLASSIFICATION #superfamily xanthine dehydrogenase; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; FAD; flavoprotein; homodimer; iron-sulfur protein; !1metalloprotein; molybdenum; molybdopterin; nucleotide !1binding; oxidoreductase; P-loop; peroxisome; phosphoprotein; !1purine catabolism FEATURE !$2-1358 #product xanthine dehydrogenase #status experimental !8#label MAT\ !$30-78 #domain ferredoxin [2Fe-2S] homology #label FER1\ !$824-831 #region nucleotide-binding motif A (P-loop)\ !$47,52,55,77 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted\ !$117,120,152,154 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted\ !$854 #binding_site molybdopterin (Cys) (covalent) #status !8predicted\ !$941 #binding_site molybdopterin (Arg) #status predicted\ !$1290 #active_site Glu #status predicted SUMMARY #length 1358 #molecular-weight 149613 #checksum 6207 SEQUENCE /// ENTRY A55875 #type complete TITLE xanthine dehydrogenase (EC 1.1.1.204) - Emericella nidulans ALTERNATE_NAMES purine hydroxylase I ORGANISM #formal_name Emericella nidulans, Aspergillus nidulans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A55875; S49819 REFERENCE A55875 !$#authors Glatigny, A.; Scazzocchio, C. !$#journal J. Biol. Chem. (1995) 270:3534-3550 !$#title Cloning and molecular characterization of hxA, the gene !1coding for the xanthine dehydrogenase (purine hydroxylase I) !1of Aspergillus nidulans. !$#cross-references MUID:95181302; PMID:7876088 !$#accession A55875 !'##molecule_type DNA !'##residues 1-1363 ##label GLA !'##cross-references EMBL:X82827; NID:g577730; PIDN:CAA58034.1; !1PID:g577731 GENETICS !$#gene hxA !$#introns 83/3; 151/3; 803/2 CLASSIFICATION #superfamily xanthine dehydrogenase; ferredoxin [2Fe-2S] !1homology KEYWORDS 2Fe-2S; FAD; flavoprotein; iron-sulfur protein; !1metalloprotein; molybdenum; oxidoreductase FEATURE !$57-104 #domain ferredoxin [2Fe-2S] homology #label FER1\ !$73,78,81,103 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 1363 #molecular-weight 149503 #checksum 4806 SEQUENCE /// ENTRY A57429 #type complete TITLE aldehyde oxidase (EC 1.2.3.1) [validated] - Desulfovibrio gigas ORGANISM #formal_name Desulfovibrio gigas DATE 30-Nov-1995 #sequence_revision 07-Feb-1997 #text_change 15-Sep-2000 ACCESSIONS A57429; S42565; S35043; S41442 REFERENCE A57429 !$#authors Ramao, M.J.; Archer, M.; Moura, I.; Moura, J.J.G.; LeGall, !1J.; Engh, R.; Schneider, M.; Hof, P.; Huber, R. !$#journal Science (1995) 270:1170-1176 !$#title Crystal structure of the xanthine oxidase-related aldehyde !1oxido-reductase from Desulfovibrio gigas. !$#cross-references MUID:96072968; PMID:7502041 !$#contents corrections; annotation; X-ray crystallography, 2.25 !1angstroms !$#accession A57429 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-907 ##label RAM !'##cross-references EMBL:X77222; NID:g853816; PIDN:CAA54439.1; !1PID:g853817 !'##note X-ray structure structure indicated two frame shift errors that !1were confirmed by resequencing REFERENCE S42565 !$#authors Thoenes, U.; Flores, O.L.; Neves, A.; Devreese, B.; van !1Beeumen, J.J.; Huber, R.; Romao, M.J.; LeGall, J.; Moura, !1J.J.G.; Rodrigues-Pousada, C. !$#journal Eur. J. Biochem. (1994) 220:901-910 !$#title Molecular cloning and sequence analysis of the gene of the !1molybdenum-containing aldehyde oxido-reductase of !1Desulfovibrio gigas. The deduced amino acid sequence shows !1similarity to xanthine dehydrogenase. !$#cross-references MUID:94192682; PMID:8143744 !$#accession S42565 !'##molecule_type DNA; protein !'##residues 1-624,'AWTALTPPKPGPSSMPTAPSPCIRPGKTMARARTSAAWA', !1'RRTKPCVPWAWLRKRSSSPGPTPPPPPTPAPPAWAE',701-782,'RPPWTAL', !1790-907 ##label THO !'##cross-references EMBL:X77222; NID:g853816 !'##experimental_source strain ATCC 27774 REFERENCE S35043 !$#authors Romao, M.J.; Barata, B.A.S.; Archer, M.; Lobeck, K.; Moura, !1I.; Carrondo, M.A.; LeGall, J.; Lottspeich, F.; Huber, R.; !1Moura, J.J.G. !$#journal Eur. J. Biochem. (1993) 215:729-732 !$#title Subunit composition, crystallization and preliminary !1crystallographic studies of the Desulfovibrio gigas aldehyde !1oxidoreductase containing molybdenum and [2Fe-2S] centers. !$#cross-references MUID:93358896; PMID:8354279 !$#accession S35043 !'##molecule_type protein !'##residues 1-29,'DXX',33-34 ##label ROM REFERENCE A65095 !$#authors Romao, M.J.; Archer, M.; Moura, I.; Moura, J.J.G.; LeGall, !1J.; Engh, R.; Schneider, M.; Hof, P.; Huber, R. !$#submission submitted to the Brookhaven Protein Data Bank, September !11995 !$#cross-references PDB:1ALO !$#contents annotation; X-ray crystallography, 2.0 angstroms, residues !11-699,'E',701-907 COMMENT This enzyme contains two 2Fe-2S clusters and a !1non-covalently bound molybdopterin cytosine dinucleotide. GENETICS !$#gene MOP COMPLEX homodimer FUNCTION !$#description catalyzes the oxidation of a broad range of aldehydes to !1carboxylic acids CLASSIFICATION #superfamily Desulfovibrio gigas aldehyde oxidase; !1ferredoxin [2Fe-2S] homology KEYWORDS 2Fe-2S; FAD; flavoprotein; homodimer; iron-sulfur protein; !1metalloprotein; molybdenum; molybdopterin; oxidoreductase FEATURE !$1-907 #product aldehyde oxidase #status predicted #label !8MAT\ !$23-61 #domain ferredoxin [2Fe-2S] homology #label FER1\ !$40,45,48,60 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8experimental\ !$100,103,137,139 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8experimental\ !$533 #binding_site molybdopterin cytosine dinucleotide !8(Arg) #status experimental\ !$653,869 #active_site His, Glu #status predicted SUMMARY #length 907 #molecular-weight 97034 #checksum 7709 SEQUENCE /// ENTRY D72660 #type complete TITLE probable aldehyde oxidoreductase APE0708 - Aeropyrum pernix (strain K1) ORGANISM #formal_name Aeropyrum pernix DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 09-Dec-2002 ACCESSIONS D72660 REFERENCE A72450 !$#authors Kawarabayasi, Y.; Hino, Y.; Horikawa, H.; Yamazaki, S.; !1Haikawa, Y.; Jin-no, K.; Takahashi, M.; Sekine, M.; Baba, !1S.; Ankai, A.; Kosugi, H.; Hosoyama, A.; Fukui, S.; Nagai, !1Y.; Nishijima, K.; Nakazawa, H.; Takamiya, M.; Masuda, S.; !1Funahashi, T.; Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, !1N.; Oguchi, A.; Aoki, K.; Kubota, K.; Nakamura, Y.; Nomura, !1N.; Sako, Y.; Kikuchi, H. !$#journal DNA Res. (1999) 6:83-101 !$#title Complete genome sequence of an aerobic hyper-thermophilic !1Crenarchaeon, Aeropyrum pernix K1. !$#cross-references MUID:99310339; PMID:10382966 !$#accession D72660 !'##molecule_type DNA !'##residues 1-753 ##label KAW !'##cross-references DDBJ:AP000060; NID:g5104188; PIDN:BAA79684.1; !1PID:g5104369 !'##experimental_source strain K1 GENETICS !$#gene APE0708 CLASSIFICATION #superfamily carbon-monoxide dehydrogenase molybdoprotein SUMMARY #length 753 #molecular-weight 82419 #checksum 1539 SEQUENCE /// ENTRY D72530 #type complete TITLE probable nicotine dehydrogenase chain C APE2216 - Aeropyrum pernix (strain K1) ORGANISM #formal_name Aeropyrum pernix DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 09-Dec-2002 ACCESSIONS D72530 REFERENCE A72450 !$#authors Kawarabayasi, Y.; Hino, Y.; Horikawa, H.; Yamazaki, S.; !1Haikawa, Y.; Jin-no, K.; Takahashi, M.; Sekine, M.; Baba, !1S.; Ankai, A.; Kosugi, H.; Hosoyama, A.; Fukui, S.; Nagai, !1Y.; Nishijima, K.; Nakazawa, H.; Takamiya, M.; Masuda, S.; !1Funahashi, T.; Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, !1N.; Oguchi, A.; Aoki, K.; Kubota, K.; Nakamura, Y.; Nomura, !1N.; Sako, Y.; Kikuchi, H. !$#journal DNA Res. (1999) 6:83-101 !$#title Complete genome sequence of an aerobic hyper-thermophilic !1Crenarchaeon, Aeropyrum pernix K1. !$#cross-references MUID:99310339; PMID:10382966 !$#accession D72530 !'##molecule_type DNA !'##residues 1-750 ##label KAW !'##cross-references DDBJ:AP000063; NID:g5105654; PIDN:BAA81228.1; !1PID:g5105916 !'##experimental_source strain K1 GENETICS !$#gene APE2216 CLASSIFICATION #superfamily carbon-monoxide dehydrogenase molybdoprotein SUMMARY #length 750 #molecular-weight 81668 #checksum 9410 SEQUENCE /// ENTRY C56279 #type complete TITLE carbon-monoxide dehydrogenase (EC 1.2.99.2) large chain - Pseudomonas carboxydovorans ORGANISM #formal_name Pseudomonas carboxydovorans DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 09-Dec-2002 ACCESSIONS C56279; PL0138 REFERENCE A56279 !$#authors Schuebel, U.; Kraut, M.; Moersdorf, G.; Meyer, O. !$#journal J. Bacteriol. (1995) 177:2197-2203 !$#title Molecular characterization of the gene cluster coxMSL !1encoding the molybdenum-containing carbon monoxide !1dehydrogenase of Oligotropha carboxidovorans. !$#cross-references MUID:95238294; PMID:7721710 !$#accession C56279 !'##molecule_type DNA !'##residues 1-809 ##label SCH !'##cross-references GB:X82447; NID:g809563; PIDN:CAA57829.1; !1PID:g809566 !'##note the source is designated as Oligotropha carboxidovorans REFERENCE PL0138 !$#authors Kraut, M.; Hugendieck, I.; Herwig, S.; Meyer, O. !$#journal Arch. Microbiol. (1989) 152:335-341 !$#title Homology and distribution of CO dehydrogenase structural !1genes in carboxydotrophic bacteria. !$#cross-references MUID:90055678; PMID:2818128 !$#accession PL0138 !'##molecule_type protein !'##residues 1-5,7-10,'AG',13 ##label KRA !'##experimental_source strain OM5 !'##note 12-Glu and 13-Lys were also found GENETICS !$#gene coxL COMPLEX heterotrimer of large, medium (see PIR:A56279), and small !1(see PIR:B56279) chains CLASSIFICATION #superfamily carbon-monoxide dehydrogenase molybdoprotein KEYWORDS heterotrimer; metalloprotein; molybdenum; molybdopterin; !1oxidoreductase; selenium FEATURE !$240,763 #binding_site molybdopterin cytosine dinucleotide !8(Gln, Glu) #status experimental\ !$388 #modified_site S-selenylcysteine (Cys) #status !8experimental SUMMARY #length 809 #molecular-weight 88739 #checksum 1429 SEQUENCE /// ENTRY I39627 #type complete TITLE nicotine dehydrogenase (EC 1.5.99.4) chain C - Arthrobacter nicotinovorans ORGANISM #formal_name Arthrobacter nicotinovorans DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 09-Dec-2002 ACCESSIONS I39627; S37570 REFERENCE I39625 !$#authors Grether-Beck, S.; Igloi, G.L.; Pust, S.; Schilz, E.; Decker, !1K.; Brandsch, R. !$#journal Mol. Microbiol. (1994) 13:929-936 !$#title Structural analysis and molybdenum-dependent expression of !1the pAO1-encoded nicotine dehydrogenase genes of !1Arthrobacter nicotinovorans. !$#cross-references MUID:95115562; PMID:7815950 !$#accession I39627 !'##molecule_type DNA !'##residues 1-814 ##label GRE !'##cross-references EMBL:X75338; NID:g665598; PIDN:CAA53088.1; !1PID:g406609 GENETICS !$#gene ndhC CLASSIFICATION #superfamily carbon-monoxide dehydrogenase molybdoprotein KEYWORDS molybdenum; molybdopterin; oxidoreductase FEATURE !$226,743 #binding_site molybdopterin cytosine dinucleotide !8(Gln, Glu) #status predicted SUMMARY #length 814 #molecular-weight 87665 #checksum 4951 SEQUENCE /// ENTRY D75614 #type complete TITLE xanthine dehydrogenase, C-terminal chain [similarity] - Deinococcus radiodurans (strain R1) ORGANISM #formal_name Deinococcus radiodurans DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 09-Dec-2002 ACCESSIONS D75614 REFERENCE A75250 !$#authors White, O.; Eisen, J.A.; Heidelberg, J.F.; Hickey, E.K.; !1Peterson, J.D.; Dodson, R.J.; Haft, D.H.; Gwinn, M.L.; !1Nelson, W.C.; Richardson, D.L.; Moffat, K.S.; Qin, H.; !1Jiang, L.; Pamphile, W.; Crosby, M.; Shen, M.; Vamathevan, !1J.J.; Lam, P.; McDonald, L.; Utterback, T.; Zalewski, C.; !1Makarova, K.S.; Aravind, L.; Daly, M.J.; Minton, K.W.; !1Fleischmann, R.D.; Ketchum, K.A.; Nelson, K.E.; Salzberg, !1S.; Smith, H.O.; Venter, J.C.; Fraser, C.M. !$#journal Science (1999) 286:1571-1577 !$#title Genome sequence of the radioresistant bacterium Deinococcus !1radiodurans R1. !$#cross-references MUID:20036896; PMID:10567266 !$#accession D75614 !'##molecule_type DNA !'##residues 1-807 ##label WHI !'##cross-references GB:AE001862; GB:AE001825; NID:g6460468; !1PIDN:AAF12194.1; PID:g6460488; TIGR:DRA0178; GSPDB:GN00078 !'##experimental_source strain R1 GENETICS !$#gene DRA0178 !$#map_position 2 CLASSIFICATION #superfamily carbon-monoxide dehydrogenase molybdoprotein SUMMARY #length 807 #molecular-weight 86382 #checksum 775 SEQUENCE /// ENTRY H75575 #type complete TITLE probable oxidoreductase (EC 1.-.-.-) DRA0231 [similarity] - Deinococcus radiodurans (strain R1) ORGANISM #formal_name Deinococcus radiodurans DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 09-Dec-2002 ACCESSIONS H75575 REFERENCE A75250 !$#authors White, O.; Eisen, J.A.; Heidelberg, J.F.; Hickey, E.K.; !1Peterson, J.D.; Dodson, R.J.; Haft, D.H.; Gwinn, M.L.; !1Nelson, W.C.; Richardson, D.L.; Moffat, K.S.; Qin, H.; !1Jiang, L.; Pamphile, W.; Crosby, M.; Shen, M.; Vamathevan, !1J.J.; Lam, P.; McDonald, L.; Utterback, T.; Zalewski, C.; !1Makarova, K.S.; Aravind, L.; Daly, M.J.; Minton, K.W.; !1Fleischmann, R.D.; Ketchum, K.A.; Nelson, K.E.; Salzberg, !1S.; Smith, H.O.; Venter, J.C.; Fraser, C.M. !$#journal Science (1999) 286:1571-1577 !$#title Genome sequence of the radioresistant bacterium Deinococcus !1radiodurans R1. !$#cross-references MUID:20036896; PMID:10567266 !$#accession H75575 !'##molecule_type DNA !'##residues 1-742 ##label WHI !'##cross-references GB:AE001863; GB:AE001825; NID:g6460670; !1PIDN:AAF12405.1; PID:g6460700; TIGR:DRA0231; GSPDB:GN00078 !'##experimental_source strain R1 GENETICS !$#gene DRA0231 !$#map_position 2 CLASSIFICATION #superfamily carbon-monoxide dehydrogenase molybdoprotein KEYWORDS oxidoreductase SUMMARY #length 742 #molecular-weight 79507 #checksum 5884 SEQUENCE /// ENTRY T35479 #type complete TITLE probable oxidoreductase [similarity] - Streptomyces coelicolor ORGANISM #formal_name Streptomyces coelicolor DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 09-Dec-2002 ACCESSIONS T35479 REFERENCE Z21579 !$#authors Oliver, K.; Harris, D.; Bentley, S.D.; Parkhill, J.; !1Barrell, B.G.; Rajandream, M.A. !$#submission submitted to the EMBL Data Library, December 1998 !$#accession T35479 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-828 ##label OLI !'##cross-references EMBL:AL034492; PIDN:CAA22506.1; GSPDB:GN00070; !1SCOEDB:SC6C5.08 !'##experimental_source strain A3(2) GENETICS !$#gene SCOEDB:SC6C5.08 CLASSIFICATION #superfamily carbon-monoxide dehydrogenase molybdoprotein SUMMARY #length 828 #molecular-weight 87500 #checksum 644 SEQUENCE /// ENTRY DEECIP #type complete TITLE IMP dehydrogenase (EC 1.1.1.205) [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 28-Dec-1987 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS C65027; A93555; A91529; S20017; A23023; A23953 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65027 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-488 ##label BLAT !'##cross-references GB:AE000337; GB:U00096; NID:g1788850; !1PIDN:AAC75561.1; PID:g1788855; UWGP:b2508 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A93555 !$#authors Tiedeman, A.A.; Smith, J.M. !$#journal Nucleic Acids Res. (1985) 13:1303-1316 !$#title Nucleotide sequence of the guaB locus encoding IMP !1dehydrogenase of Escherichia coli K12. !$#cross-references MUID:85215547; PMID:2860637 !$#accession A93555 !'##molecule_type DNA !'##residues 'MQSVTLCIMPRQYLLTTLVEILP',1-205,'A',207-488 ##label TIE !'##cross-references GB:X02209; NID:g41626; PIDN:CAA26133.1; PID:g41627 !'##experimental_source strain K12 REFERENCE A91529 !$#authors Thomas, M.S.; Drabble, W.T. !$#journal Gene (1985) 36:45-53 !$#title Nucleotide sequence and organisation of the gua promoter !1region of Escherichia coli. !$#cross-references MUID:86056959; PMID:2998937 !$#accession A91529 !'##molecule_type DNA !'##residues 1-96 ##label THO REFERENCE S20017 !$#authors Tesfa-Selase, F.; Drabble, W.T. !$#journal Mol. Gen. Genet. (1992) 231:256-264 !$#title Regulation of the gua operon of Escherichia coli by the DnaA !1protein. !$#cross-references MUID:92140365; PMID:1736096 !$#accession S20017 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-90 ##label TES GENETICS !$#gene guaB !$#map_position 54 min COMPLEX homotetramer [validated, MUID:80153366] FUNCTION !$#description EC 1.1.1.205 [validated, MUID:80153366]; IMP dehydrogenase; !1catalyzes the oxidation of inosine 5'-phosphate by NAD and !1one molecule of water to xanthosine 5'-phosphate !$#pathway purine nucleotide biosynthesis CLASSIFICATION #superfamily IMP dehydrogenase; CBS homology; IMP !1dehydrogenase amino-terminal homology; IMP dehydrogenase !1catalytic homology KEYWORDS GMP biosynthesis; NAD; oxidoreductase; purine nucleotide !1biosynthesis FEATURE !$9-75 #domain IMP dehydrogenase amino-terminal homology !8#label IDHN\ !$96-144 #domain CBS homology #label CBS1\ !$158-206 #domain CBS homology #label CBS2\ !$207-450 #domain IMP dehydrogenase catalytic homology #label !8IDHC\ !$305 #active_site Cys #status predicted SUMMARY #length 488 #molecular-weight 52022 #checksum 7566 SEQUENCE /// ENTRY H64055 #type complete TITLE IMP dehydrogenase (EC 1.1.1.205) - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES inosine-5'-monophosphate dehydrogenase ORGANISM #formal_name Haemophilus influenzae DATE 18-Aug-1995 #sequence_revision 04-Oct-1996 #text_change 28-Jul-2000 ACCESSIONS H64055 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession H64055 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-488 ##label TIGR !'##cross-references GB:U32708; GB:L42023; NID:g3212186; !1PIDN:AAC21890.1; PID:g1573185; TIGR:HI0221 COMMENT The active enzyme, a tetramer of identical chains, catalyzes !1the conversion of IMP to XMP in the presence of NAD; this !1reaction is the first unique step to GMP biosynthesis. GENETICS !$#gene guaB FUNCTION !$#description catalyzes the oxidation of inosine 5'-phosphate by NAD and !1one molecule of water to xanthosine 5'-phosphate !$#pathway purine nucleotide biosynthesis CLASSIFICATION #superfamily IMP dehydrogenase; CBS homology; IMP !1dehydrogenase amino-terminal homology; IMP dehydrogenase !1catalytic homology KEYWORDS GMP biosynthesis; homotetramer; NAD; oxidoreductase; purine !1nucleotide biosynthesis FEATURE !$10-76 #domain IMP dehydrogenase amino-terminal homology !8#label IDHN\ !$97-145 #domain CBS homology #label CBS1\ !$159-207 #domain CBS homology #label CBS2\ !$208-451 #domain IMP dehydrogenase catalytic homology #label !8IDHC\ !$306 #active_site Cys #status predicted SUMMARY #length 488 #molecular-weight 51980 #checksum 8585 SEQUENCE /// ENTRY S23226 #type complete TITLE IMP dehydrogenase (EC 1.1.1.205) - Acinetobacter calcoaceticus ORGANISM #formal_name Acinetobacter calcoaceticus DATE 04-Jun-1999 #sequence_revision 04-Jun-1999 #text_change 16-Jul-1999 ACCESSIONS S23226 REFERENCE S23225 !$#authors Anderegg, U.; Schnuck, W.H.; Asperger, O.; Kleber, H.P. !$#submission submitted to the EMBL Data Library, June 1992 !$#accession S23226 !'##molecule_type DNA !'##residues 1-488 ##label AND !'##cross-references EMBL:X66859; NID:g38718; PIDN:CAA47328.1; !1PID:g38720 FUNCTION !$#description catalyzes the oxidation of inosine 5'-phosphate by NAD and !1one molecule of water to xanthosine 5'-phosphate !$#pathway purine nucleotide biosynthesis CLASSIFICATION #superfamily IMP dehydrogenase; CBS homology; IMP !1dehydrogenase amino-terminal homology; IMP dehydrogenase !1catalytic homology KEYWORDS duplication; GMP biosynthesis; NAD; oxidoreductase; purine !1nucleotide biosynthesis FEATURE !$9-75 #domain IMP dehydrogenase amino-terminal homology !8#label IDHN\ !$96-143 #domain CBS homology #label CBS1\ !$157-205 #domain CBS homology #label CBS2\ !$206-451 #domain IMP dehydrogenase catalytic homology #label !8IDHC\ !$304 #active_site Cys #status predicted SUMMARY #length 488 #molecular-weight 51530 #checksum 7816 SEQUENCE /// ENTRY H81109 #type complete TITLE IMP dehydrogenase (EC 1.1.1.205) NMB1201 [similarity] - Neisseria meningitidis (strain MC58 serogroup B) ALTERNATE_NAMES IMP:NAD+ oxidoreductase; IMPDH; inosine-5'-monophosphate dehydrogenase ORGANISM #formal_name Neisseria meningitidis DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 19-Jan-2001 ACCESSIONS H81109 REFERENCE A81000 !$#authors Tettelin, H.; Saunders, N.J.; Heidelberg, J.; Jeffries, !1A.C.; Nelson, K.E.; Eisen, J.A.; Ketchum, K.A.; Hood, D.W.; !1Peden, J.F.; Dodson, R.J.; Nelson, W.C.; Gwinn, M.L.; DeBoy, !1R.; Peterson, J.D.; Hickey, E.K.; Haft, D.H.; Salzberg, !1S.L.; White, O.; Fleischmann, R.D.; Dougherty, B.A.; Mason, !1T.; Ciecko, A.; Parksey, D.S.; Blair, E.; Cittone, H.; !1Clark, E.B.; Cotton, M.D.; Utterback, T.R.; Khouri, H.; Qin, !1H.; Vamathevan, J.; Gill, J.; Scarlato, V.; Masignani, V.; !1Pizza, M.; Grandi, G.; Sun, L.; Smith, H.O.; Fraser, C.M.; !1Moxon, E.R.; Rappuoli, R.; Venter, J.C. !$#journal Science (2000) 287:1809-1815 !$#title Complete genome sequence of Neisseria meningitidis serogroup !1B strain MC58. !$#cross-references MUID:20175755; PMID:10710307 !$#accession H81109 !'##molecule_type DNA !'##residues 1-487 ##label TET !'##cross-references GB:AE002468; GB:AE002098; NID:g7226436; !1PIDN:AAF41583.1; PID:g7226438; GSPDB:GN00119; TIGR:NMB1201 !'##experimental_source serogroup B, strain MC58 GENETICS !$#gene NMB1201 FUNCTION !$#description catalyzes the oxidation of inosine 5'-phosphate by NAD and !1one molecule of water to xanthosine 5'-phosphate !$#pathway purine nucleotide biosynthesis CLASSIFICATION #superfamily IMP dehydrogenase; CBS homology; IMP !1dehydrogenase amino-terminal homology; IMP dehydrogenase !1catalytic homology KEYWORDS duplication; GMP biosynthesis; NAD; oxidoreductase; purine !1nucleotide biosynthesis FEATURE !$8-74 #domain IMP dehydrogenase amino-terminal homology !8#label IDHN\ !$95-144 #domain CBS homology #label CBS1\ !$158-206 #domain CBS homology #label CBS2\ !$207-451 #domain IMP dehydrogenase catalytic homology #label !8IDHC\ !$305 #active_site Cys #status predicted SUMMARY #length 487 #molecular-weight 52383 #checksum 4026 SEQUENCE /// ENTRY H70473 #type complete TITLE IMP dehydrogenase (EC 1.1.1.205) - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 04-Jun-1999 #sequence_revision 04-Jun-1999 #text_change 16-Jul-1999 ACCESSIONS H70473 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession H70473 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-490 ##label AQF !'##cross-references GB:AE000768; NID:g2984249; PIDN:AAC07779.1; !1PID:g2984252; GB:AE000657 !'##experimental_source strain VF5 GENETICS !$#gene guaB FUNCTION !$#description catalyzes the oxidation of inosine 5'-phosphate by NAD and !1one molecule of water to xanthosine 5'-phosphate !$#pathway purine nucleotide biosynthesis CLASSIFICATION #superfamily IMP dehydrogenase; CBS homology; IMP !1dehydrogenase amino-terminal homology; IMP dehydrogenase !1catalytic homology KEYWORDS duplication; GMP biosynthesis; NAD; oxidoreductase; purine !1nucleotide biosynthesis FEATURE !$12-78 #domain IMP dehydrogenase amino-terminal homology !8#label IDHN\ !$99-147 #domain CBS homology #label CBS1\ !$162-210 #domain CBS homology #label CBS2\ !$211-453 #domain IMP dehydrogenase catalytic homology #label !8IDHC\ !$309 #active_site Cys #status predicted SUMMARY #length 490 #molecular-weight 53400 #checksum 847 SEQUENCE /// ENTRY DEBSMP #type complete TITLE IMP dehydrogenase (EC 1.1.1.205) - Bacillus subtilis ALTERNATE_NAMES inositol-monophosphate dehydrogenase guaB ORGANISM #formal_name Bacillus subtilis DATE 31-Dec-1991 #sequence_revision 09-Aug-1997 #text_change 16-Jun-2000 ACCESSIONS S66039; S12623; D69638 REFERENCE S65967 !$#authors Ogasawara, N.; Nakai, S.; Yoshikawa, H. !$#journal DNA Res. (1994) 1:1-14 !$#title Systematic sequencing of the 180 kilobase region of the !1Bacillus subtilis chromosome containing the replication !1origin. !$#cross-references MUID:96051385; PMID:7584024 !$#accession S66039 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-488 ##label OGA !'##cross-references EMBL:D26185; NID:g467326; PIDN:BAA05245.1; !1PID:g467399 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1993 REFERENCE S12623 !$#authors Kanzaki, N.; Miyagawa, K. !$#journal Nucleic Acids Res. (1990) 18:6710 !$#title Nucleotide sequence of the Bacillus subtilis IMP !1dehydrogenase gene. !$#cross-references MUID:91067483; PMID:1979163 !$#accession S12623 !'##molecule_type DNA !'##residues 1-27,'H',29-479,'VHRNKALPGLFGSHQKKTGFVYDECCQSGFFSSD' !1##label KAN !'##cross-references EMBL:X55669; NID:g39958; PIDN:CAA39204.1; !1PID:g39959 !'##note the authors translated the codon CAG for residue 66 as Glu REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D69638 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-488 ##label KUN !'##cross-references GB:Z99104; GB:AL009126; NID:g2632267; !1PIDN:CAB11785.1; PID:g2632276 !'##experimental_source strain 168 GENETICS !$#gene guaB FUNCTION !$#description catalyzes the oxidation of inosine 5'-phosphate by NAD and !1one molecule of water to xanthosine 5'-phosphate !$#pathway purine nucleotide biosynthesis CLASSIFICATION #superfamily IMP dehydrogenase; CBS homology; IMP !1dehydrogenase amino-terminal homology; IMP dehydrogenase !1catalytic homology KEYWORDS GMP biosynthesis; NAD; oxidoreductase; purine nucleotide !1biosynthesis FEATURE !$11-77 #domain IMP dehydrogenase amino-terminal homology !8#label IDHN\ !$98-148 #domain CBS homology #label CBS1\ !$161-209 #domain CBS homology #label CBS2\ !$210-451 #domain IMP dehydrogenase catalytic homology #label !8IDHC\ !$308 #active_site Cys #status predicted SUMMARY #length 488 #molecular-weight 52990 #checksum 7257 SEQUENCE /// ENTRY JC4372 #type complete TITLE IMP dehydrogenase (EC 1.1.1.205) - Streptococcus pyogenes ALTERNATE_NAMES IMP:NAD+ oxidoreductase ORGANISM #formal_name Streptococcus pyogenes DATE 04-Jun-1999 #sequence_revision 04-Jun-1999 #text_change 16-Jul-1999 ACCESSIONS JC4372 REFERENCE JC4372 !$#authors Ashbaugh, C.D.; Wessels, M.R. !$#journal Gene (1995) 165:57-60 !$#title Cloning, sequence analysis and expression of the group A !1Streptococcal guaB gene encoding inosine monophosphate !1dehydrogenase. !$#cross-references MUID:96084952; PMID:7489916 !$#accession JC4372 !'##molecule_type DNA !'##residues 1-493 ##label ASH !'##cross-references GB:U26056; NID:g924847; PIDN:AAB03846.1; !1PID:g924848 !'##experimental_source TX4 !'##note the source is designated only as group A Streptococcus COMMENT This enzyme is required for purine biosynthesis. GENETICS !$#gene guaB FUNCTION !$#description catalyzes the oxidation of inosine 5'-phosphate by NAD and !1one molecule of water to xanthosine 5'-phosphate !$#pathway purine nucleotide biosynthesis CLASSIFICATION #superfamily IMP dehydrogenase; CBS homology; IMP !1dehydrogenase amino-terminal homology; IMP dehydrogenase !1catalytic homology KEYWORDS duplication; GMP biosynthesis; NAD; oxidoreductase; purine !1nucleotide biosynthesis FEATURE !$13-79 #domain IMP dehydrogenase amino-terminal homology !8#label IDHN\ !$100-150 #domain CBS homology #label CBS1\ !$163-211 #domain CBS homology #label CBS2\ !$212-456 #domain IMP dehydrogenase catalytic homology #label !8IDHC\ !$310 #active_site Cys #status predicted SUMMARY #length 493 #molecular-weight 52807 #checksum 7848 SEQUENCE /// ENTRY E64623 #type complete TITLE IMP dehydrogenase (EC 1.1.1.205) - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 04-Jun-1999 #sequence_revision 04-Jun-1999 #text_change 16-Jul-1999 ACCESSIONS E64623 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession E64623 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-481 ##label TOM !'##cross-references GB:AE000594; GB:AE000511; NID:g2313957; !1PIDN:AAD07879.1; PID:g2313963; TIGR:HP0829 FUNCTION !$#description catalyzes the oxidation of inosine 5'-phosphate by NAD and !1one molecule of water to xanthosine 5'-phosphate !$#pathway purine nucleotide biosynthesis CLASSIFICATION #superfamily IMP dehydrogenase; CBS homology; IMP !1dehydrogenase amino-terminal homology; IMP dehydrogenase !1catalytic homology KEYWORDS duplication; GMP biosynthesis; NAD; oxidoreductase; purine !1nucleotide biosynthesis FEATURE !$8-74 #domain IMP dehydrogenase amino-terminal homology !8#label IDHN\ !$95-143 #domain CBS homology #label CBS1\ !$156-204 #domain CBS homology #label CBS2\ !$205-445 #domain IMP dehydrogenase catalytic homology #label !8IDHC\ !$300 #active_site Cys #status predicted SUMMARY #length 481 #molecular-weight 51802 #checksum 462 SEQUENCE /// ENTRY H71890 #type complete TITLE IMP dehydrogenase (EC 1.1.1.205) - Helicobacter pylori (strain J99) ORGANISM #formal_name Helicobacter pylori #variety strain J99 DATE 04-Jun-1999 #sequence_revision 04-Jun-1999 #text_change 16-Jul-1999 ACCESSIONS H71890 REFERENCE A71800 !$#authors Alm, R.A.; Ling, L.S.L.; Moir, D.T.; King, B.L.; Brown, !1E.D.; Doig, P.C.; Smith, D.R.; Noonan, B.; Guild, B.C.; !1deJonge, B.L.; Carmel, G.; Tummino, P.J.; Caruso, A.; !1Uria-Nickelsen, M.; Mills, D.M.; Ives, C.; Gibson, R.; !1Merberg, D.; Mills, S.D.; Jiang, Q.; Taylor, D.E.; Vovis, !1G.F.; Trust, T.J. !$#journal Nature (1999) 397:176-180 !$#title Genomic sequence comparison of two unrelated isolates of the !1human gastric pathogen Helicobacter pylori. !$#cross-references MUID:99120557; PMID:9923682 !$#accession H71890 !'##molecule_type DNA !'##residues 1-481 ##label ARN !'##cross-references GB:AE001507; GB:AE001439; NID:g4155326; !1PIDN:AAD06347.1; PID:g4155333 !'##experimental_source strain J99 GENETICS !$#gene guaB FUNCTION !$#description catalyzes the oxidation of inosine 5'-phosphate by NAD and !1one molecule of water to xanthosine 5'-phosphate !$#pathway purine nucleotide biosynthesis CLASSIFICATION #superfamily IMP dehydrogenase; CBS homology; IMP !1dehydrogenase amino-terminal homology; IMP dehydrogenase !1catalytic homology KEYWORDS duplication; GMP biosynthesis; NAD; oxidoreductase; purine !1nucleotide biosynthesis FEATURE !$8-74 #domain IMP dehydrogenase amino-terminal homology !8#label IDHN\ !$95-143 #domain CBS homology #label CBS1\ !$156-204 #domain CBS homology #label CBS2\ !$205-445 #domain IMP dehydrogenase catalytic homology #label !8IDHC\ !$300 #active_site Cys #status predicted SUMMARY #length 481 #molecular-weight 51688 #checksum 109 SEQUENCE /// ENTRY S72823 #type complete TITLE IMP dehydrogenase (EC 1.1.1.205) guaB2 - Mycobacterium leprae ALTERNATE_NAMES B1620_C3_238 protein ORGANISM #formal_name Mycobacterium leprae DATE 04-Jun-1999 #sequence_revision 04-Jun-1999 #text_change 23-Mar-2001 ACCESSIONS S72823 REFERENCE S72584 !$#authors Smith, D.R.; Robison, K. !$#submission submitted to the EMBL Data Library, November 1993 !$#description Mycobacterium leprae cosmid B1620. !$#accession S72823 !'##molecule_type DNA !'##residues 1-529 ##label SMI !'##cross-references EMBL:U00015; NID:g466931; PIDN:AAC43232.1; !1PID:g466944 GENETICS !$#gene guaB2 FUNCTION !$#description catalyzes the oxidation of inosine 5'-phosphate by NAD and !1one molecule of water to xanthosine 5'-phosphate !$#pathway purine nucleotide biosynthesis CLASSIFICATION #superfamily IMP dehydrogenase; CBS homology; IMP !1dehydrogenase amino-terminal homology; IMP dehydrogenase !1catalytic homology KEYWORDS duplication; GMP biosynthesis; NAD; oxidoreductase; purine !1nucleotide biosynthesis FEATURE !$45-111 #domain IMP dehydrogenase amino-terminal homology !8#label IDHN\ !$132-180 #domain CBS homology #label CBS1\ !$193-241 #domain CBS homology #label CBS2\ !$242-493 #domain IMP dehydrogenase catalytic homology #label !8IDHC\ !$341 #active_site Cys #status predicted SUMMARY #length 529 #molecular-weight 54814 #checksum 2745 SEQUENCE /// ENTRY H70736 #type complete TITLE IMP dehydrogenase (EC 1.1.1.205) guaB2 - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 04-Jun-1999 #sequence_revision 04-Jun-1999 #text_change 16-Jun-2000 ACCESSIONS H70736 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession H70736 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-529 ##label COL !'##cross-references GB:Z77165; GB:AL123456; NID:g3261609; !1PIDN:CAB01012.1; PID:g1449376 !'##experimental_source strain H37Rv GENETICS !$#gene guaB2 FUNCTION !$#description catalyzes the oxidation of inosine 5'-phosphate by NAD and !1one molecule of water to xanthosine 5'-phosphate !$#pathway purine nucleotide biosynthesis CLASSIFICATION #superfamily IMP dehydrogenase; CBS homology; IMP !1dehydrogenase amino-terminal homology; IMP dehydrogenase !1catalytic homology KEYWORDS duplication; GMP biosynthesis; NAD; oxidoreductase; purine !1nucleotide biosynthesis FEATURE !$45-111 #domain IMP dehydrogenase amino-terminal homology !8#label IDHN\ !$132-180 #domain CBS homology #label CBS1\ !$193-241 #domain CBS homology #label CBS2\ !$242-493 #domain IMP dehydrogenase catalytic homology #label !8IDHC\ !$341 #active_site Cys #status predicted SUMMARY #length 529 #molecular-weight 54867 #checksum 6059 SEQUENCE /// ENTRY G64501 #type complete TITLE IMP dehydrogenase (EC 1.1.1.205) - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 04-Jun-1999 #sequence_revision 04-Jun-1999 #text_change 21-Jul-2000 ACCESSIONS G64501 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession G64501 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-496 ##label BUL !'##cross-references GB:U67602; GB:L77117; NID:g1592214; !1PIDN:AAB99638.1; PID:g1592337; TIGR:MJ1616 GENETICS !$#map_position FOR1591580-1593070 !$#start_codon TTG FUNCTION !$#description catalyzes the oxidation of inosine 5'-phosphate by NAD and !1one molecule of water to xanthosine 5'-phosphate !$#pathway purine nucleotide biosynthesis CLASSIFICATION #superfamily IMP dehydrogenase; CBS homology; IMP !1dehydrogenase amino-terminal homology; IMP dehydrogenase !1catalytic homology KEYWORDS duplication; GMP biosynthesis; NAD; oxidoreductase; purine !1nucleotide biosynthesis FEATURE !$13-78 #domain IMP dehydrogenase amino-terminal homology !8#label IDHN\ !$99-147 #domain CBS homology #label CBS1\ !$159-207 #domain CBS homology #label CBS2\ !$208-458 #domain IMP dehydrogenase catalytic homology #label !8IDHC\ !$306 #active_site Cys #status predicted SUMMARY #length 496 #molecular-weight 53316 #checksum 8421 SEQUENCE /// ENTRY E71456 #type complete TITLE IMP dehydrogenase (EC 1.1.1.205) - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 04-Jun-1999 #sequence_revision 04-Jun-1999 #text_change 21-Jul-2000 ACCESSIONS E71456 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession E71456 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-486 ##label KAW !'##cross-references GB:AP000001; NID:g3236128; PIDN:BAA29380.1; !1PID:g3256697 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0307 FUNCTION !$#description catalyzes the oxidation of inosine 5'-phosphate by NAD and !1one molecule of water to xanthosine 5'-phosphate !$#pathway purine nucleotide biosynthesis CLASSIFICATION #superfamily IMP dehydrogenase; CBS homology; IMP !1dehydrogenase amino-terminal homology; IMP dehydrogenase !1catalytic homology KEYWORDS duplication; GMP biosynthesis; NAD; oxidoreductase; purine !1nucleotide biosynthesis FEATURE !$15-81 #domain IMP dehydrogenase amino-terminal homology !8#label IDHN\ !$102-149 #domain CBS homology #label CBS1\ !$159-207 #domain CBS homology #label CBS2\ !$208-447 #domain IMP dehydrogenase catalytic homology #label !8IDHC\ !$301 #active_site Cys #status predicted SUMMARY #length 486 #molecular-weight 52932 #checksum 6451 SEQUENCE /// ENTRY JC4998 #type complete TITLE IMP dehydrogenase (EC 1.1.1.205) - Pyrococcus furiosus ORGANISM #formal_name Pyrococcus furiosus DATE 04-Jun-1999 #sequence_revision 04-Jun-1999 #text_change 16-Jul-1999 ACCESSIONS JC4998 REFERENCE JC4998 !$#authors Collart, F.R.; Osipiuk, J.; Trent, J.; Olsen, G.J.; !1Huberman, E. !$#journal Gene (1996) 174:209-216 !$#title Cloning, characterization and sequence comparison of the !1gene coding for IMP dehydrogenase from Pyrococcus furiosus. !$#cross-references MUID:97045814; PMID:8890736 !$#accession JC4998 !'##molecule_type DNA !'##residues 1-485 ##label COL !'##cross-references GB:U08814; NID:g595286; PIDN:AAC44532.1; !1PID:g595287 GENETICS !$#gene guaB COMPLEX homotetramer FUNCTION !$#description catalyzes the oxidation of inosine 5'-phosphate by NAD and !1one molecule of water to xanthosine 5'-phosphate !$#pathway purine nucleotide biosynthesis CLASSIFICATION #superfamily IMP dehydrogenase; CBS homology; IMP !1dehydrogenase amino-terminal homology; IMP dehydrogenase !1catalytic homology KEYWORDS duplication; GMP biosynthesis; NAD; oxidoreductase; purine !1nucleotide biosynthesis FEATURE !$15-81 #domain IMP dehydrogenase amino-terminal homology !8#label IDHN\ !$102-149 #domain CBS homology #label CBS1\ !$159-207 #domain CBS homology #label CBS2\ !$208-447 #domain IMP dehydrogenase catalytic homology #label !8IDHC\ !$301 #active_site Cys #status predicted SUMMARY #length 485 #molecular-weight 52900 #checksum 6440 SEQUENCE /// ENTRY B69056 #type complete TITLE IMP dehydrogenase (EC 1.1.1.205) - Methanobacterium thermoautotrophicum (strain Delta H) ALTERNATE_NAMES inosine-5'-monophosphate dehydrogenase ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 04-Jun-1999 #sequence_revision 04-Jun-1999 #text_change 16-Jul-1999 ACCESSIONS B69056 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession B69056 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-484 ##label MTH !'##cross-references GB:AE000803; GB:AE000666; NID:g2621179; !1PIDN:AAB84648.1; PID:g2621183 !'##experimental_source strain Delta H GENETICS !$#gene MTH142 FUNCTION !$#description catalyzes the oxidation of inosine 5'-phosphate by NAD and !1one molecule of water to xanthosine 5'-phosphate !$#pathway purine nucleotide biosynthesis CLASSIFICATION #superfamily IMP dehydrogenase; CBS homology; IMP !1dehydrogenase amino-terminal homology; IMP dehydrogenase !1catalytic homology KEYWORDS duplication; GMP biosynthesis; NAD; oxidoreductase; purine !1nucleotide biosynthesis FEATURE !$13-79 #domain IMP dehydrogenase amino-terminal homology !8#label IDHN\ !$100-149 #domain CBS homology #label CBS1\ !$161-208 #domain CBS homology #label CBS2\ !$209-455 #domain IMP dehydrogenase catalytic homology #label !8IDHC\ !$304 #active_site Cys #status predicted SUMMARY #length 484 #molecular-weight 52206 #checksum 6744 SEQUENCE /// ENTRY F75342 #type complete TITLE IMP dehydrogenase (EC 1.1.1.205) DR1878 [similarity] - Deinococcus radiodurans (strain R1) ALTERNATE_NAMES IMP:NAD+ oxidoreductase; IMPDH; inosine-5'-monophosphate dehydrogenase ORGANISM #formal_name Deinococcus radiodurans DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 05-May-2000 ACCESSIONS F75342 REFERENCE A75250 !$#authors White, O.; Eisen, J.A.; Heidelberg, J.F.; Hickey, E.K.; !1Peterson, J.D.; Dodson, R.J.; Haft, D.H.; Gwinn, M.L.; !1Nelson, W.C.; Richardson, D.L.; Moffat, K.S.; Qin, H.; !1Jiang, L.; Pamphile, W.; Crosby, M.; Shen, M.; Vamathevan, !1J.J.; Lam, P.; McDonald, L.; Utterback, T.; Zalewski, C.; !1Makarova, K.S.; Aravind, L.; Daly, M.J.; Minton, K.W.; !1Fleischmann, R.D.; Ketchum, K.A.; Nelson, K.E.; Salzberg, !1S.; Smith, H.O.; Venter, J.C.; Fraser, C.M. !$#journal Science (1999) 286:1571-1577 !$#title Genome sequence of the radioresistant bacterium Deinococcus !1radiodurans R1. !$#cross-references MUID:20036896; PMID:10567266 !$#accession F75342 !'##molecule_type DNA !'##residues 1-500 ##label WHI !'##cross-references GB:AE002027; GB:AE000513; NID:g6459655; !1PIDN:AAF11432.1; PID:g6459660; TIGR:DR1878; GSPDB:GN00077 !'##experimental_source strain R1 GENETICS !$#gene DR1878 !$#map_position 1 FUNCTION !$#description catalyzes the oxidation of inosine 5'-phosphate by NAD and !1one molecule of water to xanthosine 5'-phosphate !$#pathway purine nucleotide biosynthesis CLASSIFICATION #superfamily IMP dehydrogenase; CBS homology; IMP !1dehydrogenase amino-terminal homology; IMP dehydrogenase !1catalytic homology KEYWORDS duplication; GMP biosynthesis; NAD; oxidoreductase; purine !1nucleotide biosynthesis FEATURE !$27-93 #domain IMP dehydrogenase amino-terminal homology !8#label IDHN\ !$114-162 #domain CBS homology #label CBS1\ !$175-222 #domain CBS homology #label CBS2\ !$223-463 #domain IMP dehydrogenase catalytic homology #label !8IDHC\ !$320 #active_site Cys #status predicted SUMMARY #length 500 #molecular-weight 53141 #checksum 317 SEQUENCE /// ENTRY T17196 #type complete TITLE IMP dehydrogenase (EC 1.1.1.205) [similarity] - Chlorobium vibrioforme ALTERNATE_NAMES guaB1 protein; IMP:NAD+ oxidoreductase; IMPDH; inosine-5'-monophosphate dehydrogenase ORGANISM #formal_name Chlorobium vibrioforme DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 16-Jun-2000 ACCESSIONS T17196 REFERENCE Z18717 !$#authors Petersen, B.L.; Moeller, M.G.; Stummann, B.M.; Henningsen, !1K.W. !$#submission submitted to the EMBL Data Library, January 1997 !$#description Structure and organization of a 25 kbp region of the genome !1of the green sulfur bacterium Chlorobium vibrioforme !1containing Mg-chelatase encoding genes. !$#accession T17196 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-521 ##label PET !'##cross-references EMBL:Z83933; PIDN:CAB06303.1 GENETICS !$#gene guaB FUNCTION !$#description catalyzes the oxidation of inosine 5'-phosphate by NAD and !1one molecule of water to xanthosine 5'-phosphate !$#pathway purine nucleotide biosynthesis CLASSIFICATION #superfamily IMP dehydrogenase; CBS homology; IMP !1dehydrogenase amino-terminal homology; IMP dehydrogenase !1catalytic homology KEYWORDS duplication; GMP biosynthesis; NAD; oxidoreductase; purine !1nucleotide biosynthesis FEATURE !$37-103 #domain IMP dehydrogenase amino-terminal homology !8#label IDHN\ !$124-177 #domain CBS homology #label CBS1\ !$189-237 #domain CBS homology #label CBS2\ !$238-483 #domain IMP dehydrogenase catalytic homology #label !8IDHC\ !$336 #active_site Cys #status predicted SUMMARY #length 521 #molecular-weight 56627 #checksum 8235 SEQUENCE /// ENTRY C70664 #type complete TITLE IMP dehydrogenase (EC 1.1.1.205) guaB1 [similarity] - Mycobacterium tuberculosis (strain H37RV) ALTERNATE_NAMES guaB1 protein; IMP:NAD+ oxidoreductase; IMPDH; inosine-5'-monophosphate dehydrogenase ORGANISM #formal_name Mycobacterium tuberculosis DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 16-Jun-2000 ACCESSIONS C70664 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession C70664 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-479 ##label COL !'##cross-references GB:Z83859; GB:AL123456; NID:g3261678; !1PIDN:CAB06111.1; PID:g1781204 !'##experimental_source strain H37Rv GENETICS !$#gene guaB1 FUNCTION !$#description catalyzes the oxidation of inosine 5'-phosphate by NAD and !1one molecule of water to xanthosine 5'-phosphate !$#pathway purine nucleotide biosynthesis CLASSIFICATION #superfamily IMP dehydrogenase; CBS homology; IMP !1dehydrogenase amino-terminal homology; IMP dehydrogenase !1catalytic homology KEYWORDS duplication; GMP biosynthesis; NAD; oxidoreductase; purine !1nucleotide biosynthesis FEATURE !$14-79 #domain IMP dehydrogenase amino-terminal homology !8#label IDHN\ !$99-146 #domain CBS homology #label CBS1\ !$157-205 #domain CBS homology #label CBS2\ !$206-452 #domain IMP dehydrogenase catalytic homology #label !8IDHC\ !$303 #active_site Cys #status predicted SUMMARY #length 479 #molecular-weight 49964 #checksum 3958 SEQUENCE /// ENTRY T44751 #type complete TITLE IMP dehydrogenase (EC 1.1.1.205) guaB1 [similarity] - Mycobacterium leprae ALTERNATE_NAMES guaB1 protein; IMP:NAD+ oxidoreductase; IMPDH; inosine-5'-monophosphate dehydrogenase ORGANISM #formal_name Mycobacterium leprae DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 05-May-2000 ACCESSIONS T44751 REFERENCE Z22833 !$#authors Parkhill, J.; Barrell, B.G.; Rajandream, M.A. !$#submission submitted to the EMBL Data Library, October 1997 !$#accession T44751 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-478 ##label PAR !'##cross-references EMBL:AL008609; PIDN:CAA15452.1 !'##experimental_source cosmid B1788 GENETICS !$#gene guaB1 FUNCTION !$#description catalyzes the oxidation of inosine 5'-phosphate by NAD and !1one molecule of water to xanthosine 5'-phosphate !$#pathway purine nucleotide biosynthesis CLASSIFICATION #superfamily IMP dehydrogenase; CBS homology; IMP !1dehydrogenase amino-terminal homology; IMP dehydrogenase !1catalytic homology KEYWORDS duplication; GMP biosynthesis; NAD; oxidoreductase; purine !1nucleotide biosynthesis FEATURE !$13-78 #domain IMP dehydrogenase amino-terminal homology !8#label IDHN\ !$98-145 #domain CBS homology #label CBS1\ !$156-204 #domain CBS homology #label CBS2\ !$205-451 #domain IMP dehydrogenase catalytic homology #label !8IDHC\ !$302 #active_site Cys #status predicted SUMMARY #length 478 #molecular-weight 50383 #checksum 405 SEQUENCE /// ENTRY JC4999 #type complete TITLE IMP dehydrogenase (EC 1.1.1.205) - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JC4999 REFERENCE JC4999 !$#authors Collart, F.R.; Osipiuk, J.; Trent, J.; Olsen, G.J.; !1Huberman, E. !$#journal Gene (1996) 174:217-220 !$#title Cloning and characterization of the gene encoding IMP !1dehydrogenase from Arabidopsis thaliana. !$#cross-references MUID:97045815; PMID:8890737 !$#accession JC4999 !'##molecule_type DNA !'##residues 1-503 ##label COL !'##cross-references GB:L34684; NID:g1100062; PIDN:AAB41940.1; !1PID:g1100063 GENETICS !$#gene impdh !$#introns 135/1; 334/3; 404/3; 490/3 COMPLEX homotetramer FUNCTION !$#description provides precursors for DNA and RNA biosynthesis; it !1catalyzes the conversion of IMP to XMP in the presence of !1NAD; this reaction is the first unique step to GMP !1biosynthesis CLASSIFICATION #superfamily IMP dehydrogenase; CBS homology; IMP !1dehydrogenase amino-terminal homology; IMP dehydrogenase !1catalytic homology KEYWORDS GMP biosynthesis; NAD; oxidoreductase; purine nucleotide !1biosynthesis FEATURE !$20-86 #domain IMP dehydrogenase amino-terminal homology !8#label IDHN\ !$172-220 #domain CBS homology #label CBS2\ !$221-465 #domain IMP dehydrogenase catalytic homology #label !8IMP\ !$322 #active_site Cys #status predicted SUMMARY #length 503 #molecular-weight 54194 #checksum 2741 SEQUENCE /// ENTRY A31997 #type complete TITLE IMP dehydrogenase (EC 1.1.1.205) II - human ALTERNATE_NAMES inosine 5'-monophosphate dehydrogenase (IMPDH) type II ORGANISM #formal_name Homo sapiens #common_name man DATE 21-May-1990 #sequence_revision 22-May-1998 #text_change 16-Jul-1999 ACCESSIONS I52303; I54184; A92676; B35566; A31997; A94550 REFERENCE I52303 !$#authors Glesne, D.A.; Huberman, E. !$#journal Biochem. Biophys. Res. Commun. (1994) 205:537-544 !$#title Cloning and sequence of the human type II IMP dehydrogenase !1gene. !$#cross-references MUID:95091778; PMID:7999076 !$#accession I52303 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-514 ##label GLE1 !'##cross-references GB:L33842; NID:g602457; PIDN:AAA67054.1; !1PID:g602458 REFERENCE I54184 !$#authors Glesne, D.A.; Collart, F.R.; Varkony, T.; Drabkin, H.; !1Huberman, E. !$#journal Genomics (1993) 16:274-277 !$#title Chromosomal localization and structure of the human type II !1IMP dehydrogenase gene. !$#cross-references MUID:93252398; PMID:8098009 !$#accession I54184 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 461-514 ##label GLE2 !'##cross-references GB:L08114; NID:g292239; PIDN:AAA36113.1; !1PID:g292240 REFERENCE A92676 !$#authors Collart, F.R.; Huberman, E. !$#journal J. Biol. Chem. (1988) 263:15769-15772 !$#title Cloning and sequence analysis of the human and Chinese !1hamster inosine-5'-monophosphate dehydrogenase cDNAs. !$#cross-references MUID:89008491; PMID:2902093 !$#accession A92676 !'##molecule_type mRNA !'##residues 1-189,'RS',192-514 ##label COL !'##cross-references GB:J04208; NID:g186391; PIDN:AAA36112.1; !1PID:g307066 !'##note submitted to the Protein Sequence Database, November 1989 REFERENCE A35566 !$#authors Natsumeda, Y.; Ohno, S.; Kawasaki, H.; Konno, Y.; Weber, G.; !1Suzuki, K. !$#journal J. Biol. Chem. (1990) 265:5292-5295 !$#title Two distinct cDNAs for human IMP dehydrogenase. !$#cross-references MUID:90203022; PMID:1969416 !$#accession B35566 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type mRNA !'##residues 1-514 ##label NAT COMMENT mRNA for IMP dehydrogenase I (see PIR:A35566) predominated !1in normal leukocytes, whereas that for IMP dehydrogenase II !1predominated in ovarian tumor cells. GENETICS !$#gene GDB:IMPDH2 !'##cross-references GDB:128086; OMIM:146691 !$#map_position 3p24.2-3p21.2 !$#introns 33/2; 49/3; 83/3; 108/3; 177/3; 207/1; 274/1; 304/1; 336/1; !1432/2; 480/2; 508/2 FUNCTION !$#description catalyzes the oxidation of inosine 5'-phosphate by NAD and !1one molecule of water to xanthosine 5'-phosphate !$#pathway purine nucleotide biosynthesis CLASSIFICATION #superfamily IMP dehydrogenase; CBS homology; IMP !1dehydrogenase amino-terminal homology; IMP dehydrogenase !1catalytic homology KEYWORDS GMP biosynthesis; NAD; oxidoreductase; purine nucleotide !1biosynthesis FEATURE !$30-96 #domain IMP dehydrogenase amino-terminal homology !8#label IDHN\ !$117-168 #domain CBS homology #label CBS1\ !$184-232 #domain CBS homology #label CBS2\ !$233-476 #domain IMP dehydrogenase catalytic homology #label !8IDHC\ !$331 #active_site Cys #status predicted SUMMARY #length 514 #molecular-weight 55804 #checksum 2165 SEQUENCE /// ENTRY B31997 #type complete TITLE IMP dehydrogenase (EC 1.1.1.205) - Chinese hamster ALTERNATE_NAMES IMP:NAD+ oxidoreductase; IMPDH; inosine-5'-monophosphate dehydrogenase ORGANISM #formal_name Cricetulus griseus #common_name Chinese hamster DATE 13-Nov-1998 #sequence_revision 13-Nov-1998 #text_change 05-May-2000 ACCESSIONS B31997 REFERENCE A92676 !$#authors Collart, F.R.; Huberman, E. !$#journal J. Biol. Chem. (1988) 263:15769-15772 !$#title Cloning and sequence analysis of the human and Chinese !1hamster inosine-5'-monophosphate dehydrogenase cDNAs. !$#cross-references MUID:89008491; PMID:2902093 !$#accession B31997 !'##molecule_type mRNA !'##residues 1-514 ##label COL !'##cross-references GB:J04209; NID:g191119; PIDN:AAA36993.1; !1PID:g304517 FUNCTION !$#description catalyzes the oxidation of inosine 5'-phosphate by NAD and !1one molecule of water to xanthosine 5'-phosphate !$#pathway purine nucleotide biosynthesis CLASSIFICATION #superfamily IMP dehydrogenase; CBS homology; IMP !1dehydrogenase amino-terminal homology; IMP dehydrogenase !1catalytic homology KEYWORDS duplication; GMP biosynthesis; NAD; oxidoreductase; purine !1nucleotide biosynthesis FEATURE !$30-96 #domain IMP dehydrogenase amino-terminal homology !8#label IDHN\ !$117-168 #domain CBS homology #label CBS1\ !$184-232 #domain CBS homology #label CBS2\ !$233-476 #domain IMP dehydrogenase catalytic homology #label !8IDHC\ !$331 #active_site Cys #status predicted SUMMARY #length 514 #molecular-weight 55890 #checksum 1805 SEQUENCE /// ENTRY JT0565 #type complete TITLE IMP dehydrogenase (EC 1.1.1.205) - mouse ALTERNATE_NAMES IMP:NAD+ oxidoreductase; IMPDH; inosine-5'-monophosphate dehydrogenase ORGANISM #formal_name Mus musculus #common_name house mouse DATE 13-Nov-1998 #sequence_revision 13-Nov-1998 #text_change 05-May-2000 ACCESSIONS JT0565; A34375; S42724 REFERENCE JT0565 !$#authors Tiedeman, A.A.; Smith, J.M. !$#journal Gene (1991) 97:289-293 !$#title Isolation and sequence of a cDNA encoding mouse IMP !1dehydrogenase. !$#cross-references MUID:91153661; PMID:1671845 !$#accession JT0565 !'##molecule_type mRNA !'##residues 1-514 ##label TIE !'##cross-references GB:M33934; NID:g198393; PIDN:AAA39311.1; !1PID:g309413 REFERENCE A34375 !$#authors Hodges, S.D.; Fung, E.; McKay, D.J.; Renaux, B.S.; Snyder, !1F.F. !$#journal J. Biol. Chem. (1989) 264:18137-18141 !$#title Increased activity, amount, and altered kinetic properties !1of IMP dehydrogenase from mycophenolic acid-resistant !1neuroblastoma cells. !$#cross-references MUID:90036890; PMID:2572589 !$#accession A34375 !'##molecule_type protein !'##residues 125-134;182-194;289-290;439-449;456-457,'L',459-464,'S', !1466;475-478 ##label HOD REFERENCE S42724 !$#authors Lightfoot, T.; Snyder, F.F. !$#journal Biochim. Biophys. Acta (1994) 1217:156-162 !$#title Gene amplification and dual point mutations of mouse IMP !1dehydrogenase associated with cellular resistance to !1mycophenolic acid. !$#cross-references MUID:94153991; PMID:7906545 !$#accession S42724 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type mRNA !'##residues 1-332,'I',334-350,'Y',352-482,'M',484-514 ##label LIG !'##cross-references EMBL:M98333; NID:g425157; PIDN:AAA20181.1; !1PID:g425158 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1993 FUNCTION !$#description catalyzes the oxidation of inosine 5'-phosphate by NAD and !1one molecule of water to xanthosine 5'-phosphate !$#pathway purine nucleotide biosynthesis CLASSIFICATION #superfamily IMP dehydrogenase; CBS homology; IMP !1dehydrogenase amino-terminal homology; IMP dehydrogenase !1catalytic homology KEYWORDS duplication; GMP biosynthesis; NAD; oxidoreductase; purine !1nucleotide biosynthesis FEATURE !$30-96 #domain IMP dehydrogenase amino-terminal homology !8#label IDHN\ !$117-168 #domain CBS homology #label CBS1\ !$184-232 #domain CBS homology #label CBS2\ !$233-476 #domain IMP dehydrogenase catalytic homology #label !8IDHC\ !$331 #active_site Cys #status predicted SUMMARY #length 514 #molecular-weight 55784 #checksum 2974 SEQUENCE /// ENTRY A35566 #type complete TITLE IMP dehydrogenase (EC 1.1.1.205) I - human ALTERNATE_NAMES IMP:NAD+ oxidoreductase; IMPDH; inosine-5'-monophosphate dehydrogenase ORGANISM #formal_name Homo sapiens #common_name man DATE 21-Sep-1990 #sequence_revision 21-Sep-1990 #text_change 05-May-2000 ACCESSIONS A35566 REFERENCE A35566 !$#authors Natsumeda, Y.; Ohno, S.; Kawasaki, H.; Konno, Y.; Weber, G.; !1Suzuki, K. !$#journal J. Biol. Chem. (1990) 265:5292-5295 !$#title Two distinct cDNAs for human IMP dehydrogenase. !$#cross-references MUID:90203022; PMID:1969416 !$#accession A35566 !'##molecule_type mRNA !'##residues 1-514 ##label NAT !'##cross-references GB:J05272; NID:g186393 !'##note the sequence in GenBank entry HUMIMPH, release 103, !1(PID:g307067) has 273-Phe, 274-His, 419-Pro and 497-Pro !1rather than the published sequence COMMENT mRNA for IMP dehydrogenase I predominated in normal !1leukocytes, whereas that for IMP dehydrogenase II (see !1PIR:A31997) predominated in ovarian tumor cells. GENETICS !$#gene GDB:IMPDH1; sWSS2608 !'##cross-references GDB:128085; OMIM:146690 !$#map_position 7q31.3-7q32 FUNCTION !$#description catalyzes the oxidation of inosine 5'-phosphate by NAD and !1one molecule of water to xanthosine 5'-phosphate !$#pathway purine nucleotide biosynthesis CLASSIFICATION #superfamily IMP dehydrogenase; CBS homology; IMP !1dehydrogenase amino-terminal homology; IMP dehydrogenase !1catalytic homology KEYWORDS duplication; GMP biosynthesis; NAD; oxidoreductase; purine !1nucleotide biosynthesis FEATURE !$30-96 #domain IMP dehydrogenase amino-terminal homology !8#label IDHN\ !$117-168 #domain CBS homology #label CBS1\ !$184-232 #domain CBS homology #label CBS2\ !$233-476 #domain IMP dehydrogenase catalytic homology #label !8IDHC\ !$331 #active_site Cys #status predicted SUMMARY #length 514 #molecular-weight 55449 #checksum 3403 SEQUENCE /// ENTRY T32709 #type complete TITLE IMP dehydrogenase (EC 1.1.1.205) T22D1.3 - Caenorhabditis elegans ALTERNATE_NAMES IMP:NAD+ oxidoreductase; IMPDH; inosine-5'-monophosphate dehydrogenase ORGANISM #formal_name Caenorhabditis elegans DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 05-May-2000 ACCESSIONS T32709 REFERENCE Z21211 !$#authors Geisel, C.; Bradshaw, H.; Hawkins, M. !$#submission submitted to the EMBL Data Library, December 1997 !$#description The sequence of C. elegans cosmid T22D1. !$#accession T32709 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-499 ##label GEI !'##cross-references EMBL:AF039052; PIDN:AAB94282.1; GSPDB:GN00022; !1CESP:T22D1.3 !'##experimental_source strain Bristol N2; clone T22D1 GENETICS !$#gene CESP:T22D1.3 !$#map_position 4 !$#introns 35/2; 85/3; 159/1; 183/3; 342/1; 412/3; 493/2 FUNCTION !$#description catalyzes the oxidation of inosine 5'-phosphate by NAD and !1one molecule of water to xanthosine 5'-phosphate !$#pathway purine nucleotide biosynthesis CLASSIFICATION #superfamily IMP dehydrogenase; CBS homology; IMP !1dehydrogenase amino-terminal homology; IMP dehydrogenase !1catalytic homology KEYWORDS duplication; GMP biosynthesis; NAD; oxidoreductase; purine !1nucleotide biosynthesis FEATURE !$32-98 #domain IMP dehydrogenase amino-terminal homology !8#label IDHN\ !$120-170 #domain CBS homology #label CBS1\ !$188-238 #domain CBS homology #label CBS2\ !$239-461 #domain IMP dehydrogenase catalytic homology #label !8IDHC\ !$337 #active_site Cys #status predicted SUMMARY #length 499 #molecular-weight 54298 #checksum 3484 SEQUENCE /// ENTRY S41064 #type complete TITLE IMP dehydrogenase (EC 1.1.1.205) impdh - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES IMP:NAD+ oxidoreductase; IMPDH; inosine-5'-monophosphate dehydrogenase ORGANISM #formal_name Drosophila melanogaster DATE 13-Nov-1998 #sequence_revision 13-Nov-1998 #text_change 05-May-2000 ACCESSIONS S41064; S61482 REFERENCE S41064 !$#authors Sifri, C.D.; Wilson, K.; Smolik, S.; Forte, M.; Ullman, B. !$#journal Biochim. Biophys. Acta (1994) 1217:103-106 !$#title Cloning and sequence analysis of a Drosophila melanogaster !1cDNA encoding IMP dehydrogenase. !$#cross-references MUID:94114565; PMID:7904480 !$#accession S41064 !'##molecule_type mRNA !'##residues 1-537 ##label SIF !'##cross-references EMBL:L22608; NID:g348101; PIDN:AAA16839.1; !1PID:g348102 REFERENCE S61482 !$#authors Nash, D.; Hu, S.; Leonard, N.J.; Tiong, S.Y.K.; Fillips, D. !$#journal Genome (1994) 37:333-344 !$#title The raspberry locus of Drosophila melanogaster includes an !1inosine monophosphate dehydrogenase like coding sequence. !$#cross-references MUID:94259281; PMID:7911114 !$#accession S61482 !'##status preliminary !'##molecule_type DNA !'##residues 1-537 ##label NAS !'##cross-references EMBL:L14847; NID:g290245; PIDN:AAA21831.1; !1PID:g387594 GENETICS !$#gene impdh !'##cross-references FlyBase:FBgn0003204 !$#map_position 10 !$#introns 55/2; 105/3; 323/1; 503/2 FUNCTION !$#description catalyzes the oxidation of inosine 5'-phosphate by NAD and !1one molecule of water to xanthosine 5'-phosphate !$#pathway purine nucleotide biosynthesis CLASSIFICATION #superfamily IMP dehydrogenase; CBS homology; IMP !1dehydrogenase amino-terminal homology; IMP dehydrogenase !1catalytic homology KEYWORDS duplication; GMP biosynthesis; NAD; oxidoreductase; purine !1nucleotide biosynthesis FEATURE !$52-118 #domain IMP dehydrogenase amino-terminal homology !8#label IDHN\ !$139-189 #domain CBS homology #label CBS1\ !$203-251 #domain CBS homology #label CBS2\ !$252-499 #domain IMP dehydrogenase catalytic homology #label !8IDHC\ !$350 #active_site Cys #status predicted SUMMARY #length 537 #molecular-weight 57829 #checksum 392 SEQUENCE /// ENTRY S59508 #type complete TITLE IMP dehydrogenase (EC 1.1.1.205) ras - fruit fly (Drosophila sp.) ALTERNATE_NAMES IMP:NAD+ oxidoreductase; IMPDH; inosine-5'-monophosphate dehydrogenase ORGANISM #formal_name Drosophila sp. DATE 13-Nov-1998 #sequence_revision 13-Nov-1998 #text_change 05-May-2000 ACCESSIONS S59508 REFERENCE S59508 !$#authors Slee, R.; Bownes, M. !$#journal Mol. Gen. Genet. (1995) 248:755-766 !$#title The raspberry locus encodes Drosophila inosine monophosphate !1dehydrogenase. !$#cross-references MUID:96069715; PMID:7476879 !$#accession S59508 !'##molecule_type mRNA !'##residues 1-537 ##label SLE !'##cross-references GB:S80430; NID:g1245860; PIDN:AAB35628.1; !1PID:g1245861 GENETICS !$#gene FlyBase:ras !'##cross-references FlyBase:FBgn0003204 FUNCTION !$#description catalyzes the oxidation of inosine 5'-phosphate by NAD and !1one molecule of water to xanthosine 5'-phosphate !$#pathway purine nucleotide biosynthesis CLASSIFICATION #superfamily IMP dehydrogenase; CBS homology; IMP !1dehydrogenase amino-terminal homology; IMP dehydrogenase !1catalytic homology KEYWORDS duplication; GMP biosynthesis; NAD; oxidoreductase; purine !1nucleotide biosynthesis FEATURE !$52-117 #domain IMP dehydrogenase amino-terminal homology !8#label IDHN\ !$138-189 #domain CBS homology #label CBS1\ !$202-249 #domain CBS homology #label CBS2\ !$250-499 #domain IMP dehydrogenase catalytic homology #label !8IDHC\ !$350 #active_site Cys #status predicted SUMMARY #length 537 #molecular-weight 57837 #checksum 8905 SEQUENCE /// ENTRY S50890 #type complete TITLE IMP dehydrogenase (EC 1.1.1.205) YML056c - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES inosine 5'-monophosphate dehydrogenase (IMPDH); protein YM9958.06c ORGANISM #formal_name Saccharomyces cerevisiae DATE 13-Nov-1998 #sequence_revision 13-Nov-1998 #text_change 19-Apr-2002 ACCESSIONS S50890 REFERENCE S49800 !$#authors Devlin, K.; Churcher, C. !$#submission submitted to the EMBL Data Library, November 1994 !$#accession S50890 !'##molecule_type DNA !'##residues 1-524 ##label DEV !'##cross-references EMBL:Z46729; NID:g577134; PIDN:CAA86719.1; !1PID:g577140; GSPDB:GN00013; MIPS:YML056c GENETICS !$#gene SGD:IMD4; MIPS:YML056c !'##cross-references SGD:S0004520 !$#map_position 13L !$#introns 154/1 FUNCTION !$#description catalyzes the oxidation of inosine 5'-phosphate by NAD and !1one molecule of water to xanthosine 5'-phosphate !$#pathway purine nucleotide biosynthesis CLASSIFICATION #superfamily IMP dehydrogenase; CBS homology; IMP !1dehydrogenase amino-terminal homology; IMP dehydrogenase !1catalytic homology KEYWORDS GMP biosynthesis; NAD; oxidoreductase; purine nucleotide !1biosynthesis FEATURE !$38-104 #domain IMP dehydrogenase amino-terminal homology !8#label IDHN\ !$188-236 #domain CBS homology #label CBS\ !$237-485 #domain IMP dehydrogenase catalytic homology #label !8IDHC\ !$336 #active_site Cys #status predicted SUMMARY #length 524 #molecular-weight 56394 #checksum 8318 SEQUENCE /// ENTRY S59402 #type complete TITLE IMP dehydrogenase (EC 1.1.1.205) YLR432w - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES inosine 5'-monophosphate dehydrogenase (IMPDH); protein L9553.4 ORGANISM #formal_name Saccharomyces cerevisiae DATE 13-Nov-1998 #sequence_revision 13-Nov-1998 #text_change 19-Apr-2002 ACCESSIONS S59402 REFERENCE S53391 !$#authors Du, Z. !$#submission submitted to the EMBL Data Library, February 1995 !$#description The sequence of S. cerevisiae cosmid 9753. !$#accession S59402 !'##molecule_type DNA !'##residues 1-523 ##label DUZ !'##cross-references EMBL:U21094; NID:g665967; PIDN:AAB67516.1; !1PID:g665971; GSPDB:GN00012; MIPS:YLR432w !'##experimental_source strain S288C (AB972) GENETICS !$#gene SGD:IMD3; MIPS:YLR432w !'##cross-references SGD:S0004424 !$#map_position 12R FUNCTION !$#description catalyzes the oxidation of inosine 5'-phosphate by NAD and !1one molecule of water to xanthosine 5'-phosphate !$#pathway purine nucleotide biosynthesis CLASSIFICATION #superfamily IMP dehydrogenase; CBS homology; IMP !1dehydrogenase amino-terminal homology; IMP dehydrogenase !1catalytic homology KEYWORDS GMP biosynthesis; NAD; oxidoreductase; purine nucleotide !1biosynthesis FEATURE !$37-103 #domain IMP dehydrogenase amino-terminal homology !8#label IDHN\ !$187-235 #domain CBS homology #label CBS\ !$236-484 #domain IMP dehydrogenase catalytic homology #label !8IDHC\ !$335 #active_site Cys #status predicted SUMMARY #length 523 #molecular-weight 56584 #checksum 6616 SEQUENCE /// ENTRY S48997 #type complete TITLE IMP dehydrogenase (EC 1.1.1.205) PUR5 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES inosine 5'-monophosphate dehydrogenase (IMPDH); protein YHR216w ORGANISM #formal_name Saccharomyces cerevisiae DATE 13-Nov-1998 #sequence_revision 13-Nov-1998 #text_change 19-Apr-2002 ACCESSIONS S48997 REFERENCE S48997 !$#authors Macri, C. !$#submission submitted to the EMBL Data Library, February 1994 !$#description The sequence of S. cerevisiae cosmid 9177. !$#accession S48997 !'##molecule_type DNA !'##residues 1-523 ##label MAC !'##cross-references EMBL:U00029; NID:g551322; PIDN:AAB69728.1; !1PID:g458916; GSPDB:GN00008; MIPS:YHR216w GENETICS !$#gene SGD:IMD2; PUR5; MIPS:YHR216w !'##cross-references SGD:S0001259 !$#map_position 8R FUNCTION !$#description catalyzes the oxidation of inosine 5'-phosphate by NAD and !1one molecule of water to xanthosine 5'-phosphate !$#pathway purine nucleotide biosynthesis CLASSIFICATION #superfamily IMP dehydrogenase; CBS homology; IMP !1dehydrogenase amino-terminal homology; IMP dehydrogenase !1catalytic homology KEYWORDS GMP biosynthesis; NAD; oxidoreductase; purine nucleotide !1biosynthesis FEATURE !$37-103 #domain IMP dehydrogenase amino-terminal homology !8#label IDHN\ !$187-235 #domain CBS homology #label CBS\ !$236-484 #domain IMP dehydrogenase catalytic homology #label !8IDHC\ !$335 #active_site Cys #status predicted SUMMARY #length 523 #molecular-weight 56530 #checksum 8520 SEQUENCE /// ENTRY T40127 #type complete TITLE IMP dehydrogenase (EC 1.1.1.205) SPBC2F12.14c - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES IMP:NAD+ oxidoreductase; IMPDH; inosine-5'-monophosphate dehydrogenase ORGANISM #formal_name Schizosaccharomyces pombe DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 21-Jul-2000 ACCESSIONS T40127; T42083 REFERENCE Z21907 !$#authors Wood, V.; Rajandream, M.A.; Barrell, B.G.; Skelton, J.; !1Churcher, C.M. !$#submission submitted to the EMBL Data Library, June 1997 !$#accession T40127 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-524 ##label WOO !'##cross-references EMBL:Z97211; PIDN:CAB10161.1; GSPDB:GN00067; !1SPDB:SPBC2F12.14c !'##experimental_source strain 972h-; cosmid c2F12 REFERENCE Z17323 !$#authors Yoshioka, S.; Kato, K.; Nakai, K.; Okayama, H.; Nojima, H. !$#journal DNA Res. (1997) 4:363-369 !$#title Identification of open reading frames in Schizosaccharomyces !1pombe cDNAs. !$#cross-references MUID:98162722; PMID:9501991 !$#accession T42083 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 62-252,'G',254-262,'P',264-293 ##label YOS !'##cross-references EMBL:D89106; NID:g1749419; PIDN:BAA13769.1; !1PID:g1749420 !'##experimental_source strain PR745 GENETICS !$#gene SPDB:SPBC2F12.14c !$#map_position 2 !$#introns 153/1 FUNCTION !$#description catalyzes the oxidation of inosine 5'-phosphate by NAD and !1one molecule of water to xanthosine 5'-phosphate !$#pathway purine nucleotide biosynthesis CLASSIFICATION #superfamily IMP dehydrogenase; CBS homology; IMP !1dehydrogenase amino-terminal homology; IMP dehydrogenase !1catalytic homology KEYWORDS duplication; GMP biosynthesis; NAD; oxidoreductase; purine !1nucleotide biosynthesis FEATURE !$37-103 #domain IMP dehydrogenase amino-terminal homology !8#label IDHN\ !$124-174 #domain CBS homology #label CBS1\ !$187-237 #domain CBS homology #label CBS2\ !$238-486 #domain IMP dehydrogenase catalytic homology #label !8IDHC\ !$337 #active_site Cys #status predicted SUMMARY #length 524 #molecular-weight 57026 #checksum 2977 SEQUENCE /// ENTRY A38668 #type complete TITLE IMP dehydrogenase (EC 1.1.1.205) - Leishmania donovani ALTERNATE_NAMES IMPDH; inosine 5'-monophosphate dehydrogenase ORGANISM #formal_name Leishmania donovani DATE 13-Nov-1998 #sequence_revision 13-Nov-1998 #text_change 16-Jul-1999 ACCESSIONS A38668 REFERENCE A38668 !$#authors Wilson, K.; Collart, F.R.; Huberman, E.; Stringer, J.R.; !1Ullman, B. !$#journal J. Biol. Chem. (1991) 266:1665-1671 !$#title Amplification and molecular cloning of the IMP dehydrogenase !1gene of Leishmania donovani. !$#cross-references MUID:91107664; PMID:1671039 !$#accession A38668 !'##molecule_type DNA !'##residues 1-514 ##label WIL !'##cross-references GB:M55667; NID:g159360 FUNCTION !$#description catalyzes the oxidation of inosine 5'-phosphate by NAD and !1one molecule of water to xanthosine 5'-phosphate !$#pathway purine nucleotide biosynthesis CLASSIFICATION #superfamily IMP dehydrogenase; CBS homology; IMP !1dehydrogenase amino-terminal homology; IMP dehydrogenase !1catalytic homology KEYWORDS GMP biosynthesis; NAD; oxidoreductase; purine nucleotide !1biosynthesis FEATURE !$28-94 #domain IMP dehydrogenase amino-terminal homology !8#label IDHN\ !$179-228 #domain CBS homology #label CBS\ !$229-472 #domain IMP dehydrogenase catalytic homology #label !8IDHC\ !$327 #active_site Cys #status predicted SUMMARY #length 514 #molecular-weight 55623 #checksum 8498 SEQUENCE /// ENTRY A55407 #type complete TITLE IMP dehydrogenase (EC 1.1.1.205) - Trypanosoma brucei brucei ALTERNATE_NAMES inosine 5'-monophosphate dehydrogenase (IMPDH) ORGANISM #formal_name Trypanosoma brucei brucei DATE 13-Nov-1998 #sequence_revision 13-Nov-1998 #text_change 16-Jul-1999 ACCESSIONS A55407 REFERENCE A55407 !$#authors Wilson, K.; Berens, R.L.; Sifri, C.D.; Ullman, B. !$#journal J. Biol. Chem. (1994) 269:28979-28987 !$#title Amplification of the inosinate dehydrogenase gene in !1Trypanosoma brucei gambiense due to an increase in !1chromosome copy number. !$#cross-references MUID:95050714; PMID:7961861 !$#accession A55407 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-512 ##label WIL !'##cross-references GB:M97794; NID:g162135; PIDN:AAB46420.1; !1PID:g162136 !'##note authors translated the codon CGT for residue 76 as Leu GENETICS !$#gene impdh FUNCTION !$#description catalyzes the oxidation of inosine 5'-phosphate by NAD and !1one molecule of water to xanthosine 5'-phosphate !$#pathway purine nucleotide biosynthesis CLASSIFICATION #superfamily IMP dehydrogenase; CBS homology; IMP !1dehydrogenase amino-terminal homology; IMP dehydrogenase !1catalytic homology KEYWORDS GMP biosynthesis; NAD; oxidoreductase; purine nucleotide !1biosynthesis FEATURE !$26-92 #domain IMP dehydrogenase amino-terminal homology !8#label IDHN\ !$177-226 #domain CBS homology #label CBS\ !$227-470 #domain IMP dehydrogenase catalytic homology #label !8IDHC\ !$325 #active_site Cys #status predicted SUMMARY #length 512 #molecular-weight 55708 #checksum 8314 SEQUENCE /// ENTRY A58910 #type complete TITLE IMP dehydrogenase (EC 1.1.1.205) [validated] - Tritrichomonas foetus ALTERNATE_NAMES IMPDH; inosine 5'-monophosphate dehydrogenase ORGANISM #formal_name Tritrichomonas foetus DATE 05-Dec-1998 #sequence_revision 05-Dec-1998 #text_change 15-Sep-2000 ACCESSIONS A58910 REFERENCE A58910 !$#authors Beck, J.T.; Zhao, S.; Wang, C.C. !$#journal Exp. Parasitol. (1994) 78:101-112 !$#title Cloning, sequencing, and structural analysis of the DNA !1encoding inosine monophosphate dehydrogenase (EC 1.1.1.205) !1from Tritrichomonas foetus. !$#cross-references MUID:94131049; PMID:7905423 !$#accession A58910 !'##molecule_type DNA !'##residues 1-503 ##label BEC !'##cross-references GB:L18917; NID:g1352864; PIDN:AAB01581.1; !1PID:g1352865 REFERENCE A67991 !$#authors Whitby, F.G. !$#submission submitted to the Brookhaven Protein Data Bank, May 1997 !$#cross-references PDB:1AK5 !$#contents annotation; X-ray crystallography, 2.3 angstroms, residues !12-101;222-313;328-412;432-483 REFERENCE A58906 !$#authors Whitby, F.G.; Luecke, H.; Kuhn, P.; Somoza, J.R.; !1Huete-Perez, J.A.; Phillips, J.D.; Hill, C.P.; Fletterick, !1R.J.; Wang, C.C. !$#journal Biochemistry (1997) 36:10666-10674 !$#title Crystal structure of Tritrichomonas foetus !1inosine-5'-monophosphate dehydrogenase and the !1enzyme-product complex. !$#cross-references MUID:97419130; PMID:9271497 !$#contents annotation !$#note enzyme activity increases when the disulfide bond observed !1in the crystallographic structure is reduced REFERENCE A58909 !$#authors Huete-Perez, J.A.; Wu, J.C.; Whitby, F.G.; Wang, C.C. !$#journal Biochemistry (1995) 34:13889-13894 !$#title Identification of the IMP binding site in the IMP !1dehydrogenase from Tritrichomonas foetus. !$#cross-references MUID:96046660; PMID:7577983 !$#contents annotation GENETICS !$#gene IMPDH COMPLEX homotetramer FUNCTION !$#description catalyzes the oxidation of inosine 5'-phosphate to !1xanthosine 5'-phosphate by NAD and one molecule of water !$#pathway purine nucleotide biosynthesis CLASSIFICATION #superfamily IMP dehydrogenase; CBS homology; IMP !1dehydrogenase amino-terminal homology; IMP dehydrogenase !1catalytic homology KEYWORDS GMP biosynthesis; homotetramer; NAD; oxidoreductase; purine !1nucleotide biosynthesis FEATURE !$10-85 #domain IMP dehydrogenase amino-terminal homology !8#label IDHN\ !$172-220 #domain CBS homology #label CBS1\ !$221-466 #domain IMP dehydrogenase catalytic homology #label !8IDHC\ !$26-459 #disulfide_bonds #status experimental\ !$319 #active_site Cys #status experimental\ !$319 #active_site Cys #status predicted SUMMARY #length 503 #molecular-weight 55473 #checksum 6137 SEQUENCE /// ENTRY E70218 #type complete TITLE IMP dehydrogenase (EC 1.1.1.205) guaB [validated] - Lyme disease spirochete plasmid B/cp26 ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 04-Jun-1999 #sequence_revision 04-Jun-1999 #text_change 03-May-2002 ACCESSIONS E70218; I40154 REFERENCE A70100 !$#authors Fraser, C.M.; Casjens, S.; Huang, W.M.; Sutton, G.G.; !1Clayton, R.; Lathigra, R.; White, O.; Ketchum, K.A.; Dodson, !1R.; Hickey, E.K.; Gwinn, M.; Dougherty, B.; Tomb, J.F.; !1Fleischmann, R.D.; Richardson, D.; Peterson, J.; Kerlavage, !1A.R.; Quackenbush, J.; Salzberg, S.; Hanson, M.; Vugt, R.V.; !1Palmer, N.; Adams, M.D.; Gocayne, J.; Weidman, J.; !1Utterback, T.; Watthey, L.; McDonald, L.; Artiach, P.; !1Bowman, C.; Garland, S.; Fujii, C.; Cotton, M.D.; Horst, K.; !1Roberts, K.; Hatch, B.; Smith, H.O.; Venter, J.C. !$#journal Nature (1997) 390:580-586 !$#title Genomic sequence of a Lyme disease spirochaete, Borrelia !1burgdorferi. !$#cross-references MUID:98065943; PMID:9403685 !$#accession E70218 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-404 ##label KLE !'##cross-references GB:AE000792; NID:g3253098; PIDN:AAC66314.1; !1PID:g2689886; TIGR:BBB17 !'##experimental_source strain B31 REFERENCE I40154 !$#authors Margolis, N.; Hogan, D.; Tilly, K.; Rosa, P. !$#journal J. Bacteriol. (1994) 176:6427-6432 !$#title Plasmid location of Borrelia purine biosynthesis gene !1homologs. !$#cross-references MUID:95050198; PMID:7961392 !$#accession I40154 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-404 ##label RES !'##cross-references EMBL:U13372; NID:g532791; PIDN:AAA53247.1; !1PID:g532792 COMMENT This sequence is missing the two CBS domains characteristic !1of most IMP dehydrogenases. GENETICS !$#gene guaB !$#genome plasmid COMPLEX homotetramer [validated; PMID:10758003] FUNCTION !$#description catalyzes the reductive deamination of GMP into IMP using !1NADPH [validated; PMID:9268334] !$#pathway purine metabolism CLASSIFICATION #superfamily Lyme disease spirochete IMP dehydrogenase !1homolog; IMP dehydrogenase amino-terminal homology; IMP !1dehydrogenase catalytic homology KEYWORDS GMP biosynthesis; NAD; oxidoreductase FEATURE !$10-76 #domain IMP dehydrogenase amino-terminal homology !8#label IDHN\ !$131-375 #domain IMP dehydrogenase catalytic homology #label !8IDHC\ !$229 #active_site Cys #status predicted SUMMARY #length 404 #molecular-weight 43767 #checksum 7038 SEQUENCE /// ENTRY E81701 #type complete TITLE probable IMP dehydrogenase (EC 1.1.1.205) TC0443 [similarity] - Chlamydia muridarum (strain Nigg) ALTERNATE_NAMES IMP:NAD+ oxidoreductase; IMPDH; inosine-5'-monophosphate dehydrogenase ORGANISM #formal_name Chlamydia muridarum, Chlamydia trachomatis MoPn DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 05-May-2000 ACCESSIONS E81701 REFERENCE A81500 !$#authors Read, T.D.; Brunham, R.C.; Shen, C.; Gill, S.R.; Heidelberg, !1J.F.; White, O.; Hickey, E.K.; Peterson, J.; Utterback, T.; !1Berry, K.; Bass, S.; Linher, K.; Weidman, J.; Khouri, H.; !1Craven, B.; Bowman, C.; Dodson, R.; Gwinn, M.; Nelson, W.; !1DeBoy, R.; Kolonay, J.; McClarty, G.; Salzberg, S.L.; Eisen, !1J.; Fraser, C.M. !$#journal Nucleic Acids Res. (2000) 28:1397-1406 !$#title Genome sequences of Chlamydia trachomatis MoPn and Chlamydia !1pneumoniae AR39. !$#cross-references MUID:20150255; PMID:10684935 !$#accession E81701 !'##molecule_type DNA !'##residues 1-357 ##label TET !'##cross-references GB:AE002313; GB:AE002160; NID:g7190484; !1PIDN:AAF39297.1; PID:g7190488; GSPDB:GN00121; TIGR:TC0443 !'##experimental_source strain Nigg (MoPn) COMMENT This sequence is very similar to IMP dehydrogenase at the !1amino end and at the carboxyl end. It contains the active !1site motif characteristic of IMP dehydrogenase and GMP !1reductase but, like the latter, is missing the two CBS !1domains. GENETICS !$#gene TC0443 CLASSIFICATION #superfamily Lyme disease spirochete IMP dehydrogenase !1homolog; IMP dehydrogenase amino-terminal homology; IMP !1dehydrogenase catalytic homology KEYWORDS GMP biosynthesis; NAD; oxidoreductase; purine nucleotide !1biosynthesis FEATURE !$5-71 #domain IMP dehydrogenase amino-terminal homology !8#label IDHN\ !$91-319 #domain IMP dehydrogenase catalytic homology #status !8atypical #label IDHC\ !$175 #active_site Cys #status predicted SUMMARY #length 357 #molecular-weight 37642 #checksum 7854 SEQUENCE /// ENTRY D72631 #type complete TITLE probable IMP dehydrogenase (EC 1.1.1.205) APE1507 [similarity] - Aeropyrum pernix (strain K1) ALTERNATE_NAMES IMP:NAD+ oxidoreductase; IMPDH; inosine-5'-monophosphate dehydrogenase ORGANISM #formal_name Aeropyrum pernix DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 16-Jun-2000 ACCESSIONS D72631 REFERENCE A72450 !$#authors Kawarabayasi, Y.; Hino, Y.; Horikawa, H.; Yamazaki, S.; !1Haikawa, Y.; Jin-no, K.; Takahashi, M.; Sekine, M.; Baba, !1S.; Ankai, A.; Kosugi, H.; Hosoyama, A.; Fukui, S.; Nagai, !1Y.; Nishijima, K.; Nakazawa, H.; Takamiya, M.; Masuda, S.; !1Funahashi, T.; Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, !1N.; Oguchi, A.; Aoki, K.; Kubota, K.; Nakamura, Y.; Nomura, !1N.; Sako, Y.; Kikuchi, H. !$#journal DNA Res. (1999) 6:83-101 !$#title Complete genome sequence of an aerobic hyper-thermophilic !1Crenarchaeon, Aeropyrum pernix K1. !$#cross-references MUID:99310339; PMID:10382966 !$#accession D72631 !'##molecule_type DNA !'##residues 1-444 ##label KAW !'##cross-references DDBJ:AP000061; NID:g5104821; PIDN:BAA80506.1; !1PID:g5105192 !'##experimental_source strain K1 COMMENT This sequence is very similar to IMP dehydrogenase at the !1amino end and at the carboxyl end. It contains the active !1site motif characteristic of IMP dehydrogenase and GMP !1reductase but, like the latter, the two CBS domains are !1missing or degenerate. GENETICS !$#gene APE1507 CLASSIFICATION #superfamily Lyme disease spirochete IMP dehydrogenase !1homolog; IMP dehydrogenase amino-terminal homology; IMP !1dehydrogenase catalytic homology KEYWORDS GMP biosynthesis; NAD; oxidoreductase; purine nucleotide !1biosynthesis FEATURE !$25-91 #domain IMP dehydrogenase amino-terminal homology !8#label IDHN\ !$174-417 #domain IMP dehydrogenase catalytic homology #label !8IDHC\ !$271 #active_site Cys #status predicted SUMMARY #length 444 #molecular-weight 47215 #checksum 2211 SEQUENCE /// ENTRY S75050 #type complete TITLE IMP dehydrogenase homolog (EC 1.-.-.-) guaB - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES inosine-5'-monophosphate dehydrogenase; protein slr1722 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 04-Jun-1999 #sequence_revision 04-Jun-1999 #text_change 16-Jun-2000 ACCESSIONS S75050 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75050 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-387 ##label KAN !'##cross-references EMBL:D90910; GB:AB001339; NID:g1652956; !1PIDN:BAA17912.1; PID:g1652995 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 COMMENT This sequence is similar to IMP dehydrogenase at the amino !1end and at the carboxyl end. It contains the active site !1motif characteristic of IMP dehydrogenase and GMP reductase !1but, like the latter, is missing the two CBS domains. GENETICS !$#gene guaB !$#start_codon GTG CLASSIFICATION #superfamily Synechocystis IMP dehydrogenase homolog; IMP !1dehydrogenase amino-terminal homology; IMP dehydrogenase !1catalytic homology KEYWORDS oxidoreductase FEATURE !$15-80 #domain IMP dehydrogenase amino-terminal homology !8#label IDHN\ !$123-356 #domain IMP dehydrogenase catalytic homology #label !8IDHC\ !$222 #active_site Cys #status predicted SUMMARY #length 387 #molecular-weight 40234 #checksum 6113 SEQUENCE /// ENTRY G70736 #type complete TITLE IMP dehydrogenase-related protein guaB3 - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 04-Jun-1999 #sequence_revision 04-Jun-1999 #text_change 16-Jun-2000 ACCESSIONS G70736 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession G70736 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-375 ##label COL !'##cross-references GB:Z77165; GB:AL123456; NID:g3261609; !1PIDN:CAB01013.1; PID:g1449377 !'##experimental_source strain H37Rv COMMENT This sequence is similar to IMP dehydrogenase at the amino !1end and at the carboxyl end. However, it is missing the two !1CBS domains and the active site motif characteristic of IMP !1dehydrogenase and GMP reductase. GENETICS !$#gene guaB3 CLASSIFICATION #superfamily Synechocystis IMP dehydrogenase homolog; IMP !1dehydrogenase amino-terminal homology; IMP dehydrogenase !1catalytic homology FEATURE !$14-79 #domain IMP dehydrogenase amino-terminal homology !8#label IDHN\ !$127-363 #domain IMP dehydrogenase catalytic homology #label !8IDHC SUMMARY #length 375 #molecular-weight 38990 #checksum 800 SEQUENCE /// ENTRY S72812 #type complete TITLE IMP dehydrogenase-related protein guaB1 - Mycobacterium leprae ALTERNATE_NAMES B1620_C2_193 protein ORGANISM #formal_name Mycobacterium leprae DATE 04-Jun-1999 #sequence_revision 04-Jun-1999 #text_change 23-Mar-2001 ACCESSIONS S72812 REFERENCE S72584 !$#authors Smith, D.R.; Robison, K. !$#submission submitted to the EMBL Data Library, November 1993 !$#description Mycobacterium leprae cosmid B1620. !$#accession S72812 !'##molecule_type DNA !'##residues 1-375 ##label SMI !'##cross-references EMBL:U00015; NID:g466931; PIDN:AAC43221.1; !1PID:g466933 COMMENT This sequence is similar to IMP dehydrogenase at the amino !1end and at the carboxyl end. However, it is missing the two !1CBS domains and the active site motif characteristic of IMP !1dehydrogenase and GMP reductase. GENETICS !$#gene guaB1 CLASSIFICATION #superfamily Synechocystis IMP dehydrogenase homolog; IMP !1dehydrogenase amino-terminal homology; IMP dehydrogenase !1catalytic homology FEATURE !$14-79 #domain IMP dehydrogenase amino-terminal homology !8#label IDHN\ !$127-363 #domain IMP dehydrogenase catalytic homology #label !8IDHC SUMMARY #length 375 #molecular-weight 38923 #checksum 3169 SEQUENCE /// ENTRY C72109 #type complete TITLE IMP dehydrogenase homolog (EC 1.-.-.-) - Chlamydophila pneumoniae (strain CWL029) ORGANISM #formal_name Chlamydophila pneumoniae, Chlamydia pneumoniae DATE 04-Jun-1999 #sequence_revision 04-Jun-1999 #text_change 20-Apr-2000 ACCESSIONS C72109 REFERENCE A72000 !$#authors Kalman, S.; Mitchell, W.; Marathe, R.; Lammel, C.; Fan, J.; !1Olinger, L.; Grimwood, J.; Davis, R.W.; Stephens, R.S. !$#journal Nature Genet. (1999) 21:385-389 !$#title Comparative genomes of Clamydia pneumoniae and C. !1trachomatis. !$#cross-references MUID:99206606; PMID:10192388 !$#accession C72109 !'##molecule_type DNA !'##residues 1-246 ##label ARN !'##cross-references GB:AE001604; GB:AE001363; NID:g4376438; !1PIDN:AAD18325.1; PID:g4376441 !'##experimental_source strain CWL029 COMMENT The sequence is very similar to the carboxyl half of IMP !1dehydrogenases (see, for example, PIR:H70473). It contains !1the active site motif characteristic of IMP dehydrogenase !1and GMP reductase but, like the latter, is missing the two !1CBS domains. GENETICS !$#gene guaB CLASSIFICATION #superfamily Chlamydia pneumoniae IMP dehydrogenase homolog; !1IMP dehydrogenase catalytic homology KEYWORDS oxidoreductase FEATURE !$1-212 #domain IMP dehydrogenase catalytic homology #status !8atypical #label IDHC\ !$68 #active_site Cys #status predicted SUMMARY #length 246 #molecular-weight 25751 #checksum 7442 SEQUENCE /// ENTRY T03447 #type complete TITLE dihydrokaempferol 4-reductase (EC 1.1.1.219) A - sorghum ALTERNATE_NAMES dihydroflavonol 4-reductase; NADPH-dependent reductase A1-a ORGANISM #formal_name Sorghum bicolor #common_name sorghum DATE 12-Nov-1999 #sequence_revision 12-Nov-1999 #text_change 12-Nov-1999 ACCESSIONS T03447 REFERENCE Z14952 !$#authors Chen, M.; SanMiguel, P.; Bennetzen, J.L. !$#journal Genetics (1998) 148:435-443 !$#title Sequence organization and conservation of Sh2/A1-homologous !1regions of sorghum and rice. !$#cross-references MUID:98133900; PMID:9475753 !$#accession T03447 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-350 ##label CHE !'##cross-references EMBL:AF010283; NID:g2735839; PID:g2735842 GENETICS !$#introns 52/1; 108/3; 173/3 CLASSIFICATION #superfamily dihydrokaempferol 4-reductase KEYWORDS oxidoreductase SUMMARY #length 350 #molecular-weight 38236 #checksum 4308 SEQUENCE /// ENTRY T02760 #type complete TITLE dihydrokaempferol 4-reductase (EC 1.1.1.219) A - maize ALTERNATE_NAMES dihydroflavonol 4-reductase; protein A1, isoform B ORGANISM #formal_name Zea mays #common_name maize DATE 12-Nov-1999 #sequence_revision 12-Nov-1999 #text_change 16-Jun-2000 ACCESSIONS T02760; T02757 REFERENCE Z14723 !$#authors Bernhardt, J.; Stich, K.; Schwarz-Sommer, Z.S.; Saedler, H.; !1Wienand, U. !$#submission submitted to the EMBL Data Library, December 1997 !$#description Molecular analysis of a second functional A1 gene !1(dihydroflavonol4-reductase) in Zea mays. !$#accession T02760 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-353 ##label BER !'##cross-references EMBL:Y16042; PIDN:CAA75998.1 !'##experimental_source strain Teosinte guerrero, sub species !1parviglumis !$#accession T02757 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-67,'M',69-140,'R',142-288,'D',290-353 ##label BE2 !'##cross-references EMBL:Y16040; PIDN:CAA75996.1 !'##experimental_source strain Line C GENETICS !$#gene A1* !$#introns 42/1; 98/3; 163/3 CLASSIFICATION #superfamily dihydrokaempferol 4-reductase KEYWORDS oxidoreductase SUMMARY #length 353 #molecular-weight 38368 #checksum 1589 SEQUENCE /// ENTRY T03448 #type complete TITLE dihydrokaempferol 4-reductase (EC 1.1.1.219) B - sorghum ALTERNATE_NAMES dihydroflavonol 4-reductase; NADPH-dependent reductase A1-b ORGANISM #formal_name Sorghum bicolor #common_name sorghum DATE 12-Nov-1999 #sequence_revision 12-Nov-1999 #text_change 12-Nov-1999 ACCESSIONS T03448 REFERENCE Z14952 !$#authors Chen, M.; SanMiguel, P.; Bennetzen, J.L. !$#journal Genetics (1998) 148:435-443 !$#title Sequence organization and conservation of Sh2/A1-homologous !1regions of sorghum and rice. !$#cross-references MUID:98133900; PMID:9475753 !$#accession T03448 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-379 ##label CHE !'##cross-references EMBL:AF010283; NID:g2735839; PIDN:AAB94015.1; !1PID:g2735843 GENETICS !$#introns 42/1; 98/3; 163/3 CLASSIFICATION #superfamily dihydrokaempferol 4-reductase KEYWORDS oxidoreductase SUMMARY #length 379 #molecular-weight 41229 #checksum 7768 SEQUENCE /// ENTRY T02758 #type complete TITLE dihydrokaempferol 4-reductase (EC 1.1.1.219) B - maize ALTERNATE_NAMES A1 protein; dihydroflavonol 4-reductase ORGANISM #formal_name Zea mays #common_name maize DATE 12-Nov-1999 #sequence_revision 12-Nov-1999 #text_change 16-Jun-2000 ACCESSIONS T02758; T02756 REFERENCE Z14723 !$#authors Bernhardt, J.; Stich, K.; Schwarz-Sommer, Z.S.; Saedler, H.; !1Wienand, U. !$#submission submitted to the EMBL Data Library, December 1997 !$#description Molecular analysis of a second functional A1 gene !1(dihydroflavonol4-reductase) in Zea mays. !$#accession T02758 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-357 ##label BER !'##cross-references EMBL:Y16041; PIDN:CAA75997.1 !'##experimental_source strain Teosinte guerrero REFERENCE Z14722 !$#authors Schwarz-Sommer, Z.; Shepherd, N.; Tacke, E.; Gierl, A.; !1Rohde, W.; Leclercq, L.; Mattes, M.; Berndtgen, R.; !1Peterson, P.A.; Saedler, H. !$#journal EMBO J. (1987) 6:287-294 !$#title Influence of transposable elements on the structure and !1funktion of the A1 gene of Zea mays. !$#accession T02756 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-2,'R',4-31,'Q',33-59,'T',61-357 ##label SCH !'##cross-references EMBL:X05068; NID:g22102; PIDN:CAA28734.1; !1PID:g313678 !'##experimental_source strain W22 GENETICS !$#gene A1 !$#introns 44/1; 100/3; 165/3 CLASSIFICATION #superfamily dihydrokaempferol 4-reductase KEYWORDS oxidoreductase SUMMARY #length 357 #molecular-weight 38792 #checksum 3875 SEQUENCE /// ENTRY S18595 #type complete TITLE dihydrokaempferol 4-reductase (EC 1.1.1.219) - barley ALTERNATE_NAMES dihydroflavonol 4-reductase ORGANISM #formal_name Hordeum vulgare #common_name barley DATE 12-Nov-1999 #sequence_revision 12-Nov-1999 #text_change 21-Jul-2000 ACCESSIONS S18595 REFERENCE S18595 !$#authors Kristiansen, K.N.; Rohde, W. !$#journal Mol. Gen. Genet. (1991) 230:49-59 !$#title Structure of the Hordeum vulgare gene encoding !1dihydroflavonol-4-reductase and molecular analysis of ant18 !1mutants blocked in flavonoid synthesis. !$#cross-references MUID:92079919; PMID:1720864 !$#accession S18595 !'##status preliminary !'##molecule_type DNA !'##residues 1-354 ##label KRI !'##cross-references GB:S69616; NID:g240051; PIDN:AAB20555.1; !1PID:g240052 CLASSIFICATION #superfamily dihydrokaempferol 4-reductase KEYWORDS oxidoreductase SUMMARY #length 354 #molecular-weight 38434 #checksum 4867 SEQUENCE /// ENTRY T04157 #type complete TITLE dihydrokaempferol 4-reductase (EC 1.1.1.219) - rice ALTERNATE_NAMES DFR; dihydroflavonol-4-reductase; NADPH-dependent reductase A1 ORGANISM #formal_name Oryza sativa #common_name rice DATE 12-Nov-1999 #sequence_revision 12-Nov-1999 #text_change 16-Jun-2000 ACCESSIONS T04157; T03728 REFERENCE Z15243 !$#authors Chen, M.; Bennetzen, J.L. !$#journal Plant Mol. Biol. (1996) 32:999-1001 !$#title Sequence composition and organization in the Sh2/ !1A1-homologous region of rice. !$#cross-references MUID:97156138; PMID:9002598 !$#accession T04157 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-372 ##label CHE !'##cross-references EMBL:U70541; NID:g2149018; PIDN:AAB58474.1; !1PID:g1778297 !'##experimental_source subsp. Indica, cv. Teqing REFERENCE Z15033 !$#authors Reddy, V.S. !$#submission submitted to the EMBL Data Library, September 1996 !$#accession T03728 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-372 ##label RED !'##cross-references EMBL:Y07956; PIDN:CAA69253.1 !'##experimental_source subsp. Indica, cv. Purpleputtu, shoot GENETICS !$#gene Dfr !$#introns 41/1; 162/3 FUNCTION !$#description catalyzes the conversion of dihydroflavonols into flavan-3, !14-diols !$#pathway flavonoid biosynthesis, the first enzyme of the anthocyanin !1pathway CLASSIFICATION #superfamily dihydrokaempferol 4-reductase KEYWORDS flavonoid biosynthesis; NADP; oxidoreductase SUMMARY #length 372 #molecular-weight 40417 #checksum 762 SEQUENCE /// ENTRY JQ1688 #type complete TITLE dihydrokaempferol 4-reductase (EC 1.1.1.219) - Arabidopsis thaliana ALTERNATE_NAMES dihydroflavonol 4-reductase ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 12-Nov-1999 #sequence_revision 12-Nov-1999 #text_change 12-Nov-1999 ACCESSIONS JQ1688 REFERENCE JQ1687 !$#authors Shirley, B.W.; Hanley, S.; Goodman, H.M. !$#journal Plant Cell (1992) 4:333-347 !$#title Effects of ionizing radiation on a plant genome: analysis of !1two Arabidopsis transparent testa mutations. !$#cross-references MUID:92361255; PMID:1354004 !$#accession JQ1688 !'##molecule_type DNA !'##residues 1-384 ##label SHI !'##cross-references GB:M86359; NID:g166685; PID:g166686 !'##experimental_source strain columbia COMMENT This enzyme catalyzes the conversion of dihydroflavonols !1into flavan-3,4-diols. GENETICS !$#introns 40/1; 96/3; 161/3; 215/1; 279/2 CLASSIFICATION #superfamily dihydrokaempferol 4-reductase KEYWORDS oxidoreductase SUMMARY #length 384 #molecular-weight 42985 #checksum 8876 SEQUENCE /// ENTRY T10716 #type complete TITLE dihydrokaempferol 4-reductase (EC 1.1.1.219) A - clove pink ALTERNATE_NAMES dihydroflavonol 4-reductase ORGANISM #formal_name Dianthus caryophyllus #common_name clove pink DATE 12-Nov-1999 #sequence_revision 12-Nov-1999 #text_change 12-Nov-1999 ACCESSIONS T10716 REFERENCE Z17093 !$#authors Henkel, J. !$#submission submitted to the EMBL Data Library, November 1995 !$#accession T10716 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-360 ##label HEN !'##cross-references EMBL:Z67983; NID:g1067126; PID:g1067127 !'##experimental_source cv. Tanga; petals from buds and flowers GENETICS !$#gene A FUNCTION !$#description catalyzes the conversion of dihydroflavonols into flavan-3, !14-diols !$#pathway flavonoid biosynthesis, the first enzyme of the anthocyanin !1pathway CLASSIFICATION #superfamily dihydrokaempferol 4-reductase KEYWORDS flavonoid biosynthesis; oxidoreductase SUMMARY #length 360 #molecular-weight 40429 #checksum 5583 SEQUENCE /// ENTRY S35189 #type complete TITLE dihydrokaempferol 4-reductase (EC 1.1.1.219) - gerbera hybrid ALTERNATE_NAMES dihydroflavonol 4-reductase ORGANISM #formal_name Gerbera x sp. #common_name gerbera hybrid DATE 12-Nov-1999 #sequence_revision 12-Nov-1999 #text_change 12-Nov-1999 ACCESSIONS S35189; S34374 REFERENCE S35189 !$#authors Helariutta, Y.; Elomaa, P.; Kotilainen, M.; Seppaenen, P.; !1Teeri, T.H. !$#journal Plant Mol. Biol. (1993) 22:183-193 !$#title Cloning of cDNA coding for dihydroflavonol-4-reductase (DFR) !1and characterization of dfr expression in the corollas of !1Gerbera hybrida var. Regina (Compositae). !$#cross-references MUID:93283624; PMID:8507822 !$#accession S35189 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-366 ##label HEL !'##cross-references EMBL:Z17221; NID:g312776; PID:g312777 !'##experimental_source var. Regina GENETICS !$#gene dfr CLASSIFICATION #superfamily dihydrokaempferol 4-reductase KEYWORDS flavonoid biosynthesis; oxidoreductase SUMMARY #length 366 #molecular-weight 41102 #checksum 8518 SEQUENCE /// ENTRY S07464 #type complete TITLE dihydrokaempferol 4-reductase (EC 1.1.1.219) - garden snapdragon ALTERNATE_NAMES dihydroflavonol 4-reductase ORGANISM #formal_name Antirrhinum majus #common_name garden snapdragon DATE 12-Nov-1999 #sequence_revision 12-Nov-1999 #text_change 21-Jul-2000 ACCESSIONS S07464 REFERENCE S07463 !$#authors Beld, M.; Martin, C.; Huits, H.; Stuitje, A.R.; Gerats, !1A.G.M. !$#journal Plant Mol. Biol. (1989) 13:491-502 !$#title Flavonoid synthesis in Petunia hybrida: partial !1characterization of dihydroflavonol-4-reductase genes. !$#cross-references MUID:91370831; PMID:2491667 !$#accession S07464 !'##molecule_type mRNA !'##residues 1-446 ##label BEL !'##cross-references EMBL:X15536; NID:g16026; PIDN:CAA33543.1; !1PID:g16027 !'##note the authors translated the codon GTC for residue 324 as Phe and !1AAG for residue 427 as Asn CLASSIFICATION #superfamily dihydrokaempferol 4-reductase KEYWORDS flavonoid biosynthesis; oxidoreductase SUMMARY #length 446 #molecular-weight 49633 #checksum 4934 SEQUENCE /// ENTRY S07463 #type complete TITLE dihydrokaempferol 4-reductase (EC 1.1.1.219) - garden petunia ALTERNATE_NAMES dihydroflavonol 4-reductase ORGANISM #formal_name Petunia x hybrida #common_name garden petunia DATE 12-Nov-1999 #sequence_revision 12-Nov-1999 #text_change 21-Jul-2000 ACCESSIONS S07463 REFERENCE S07463 !$#authors Beld, M.; Martin, C.; Huits, H.; Stuitje, A.R.; Gerats, !1A.G.M. !$#journal Plant Mol. Biol. (1989) 13:491-502 !$#title Flavonoid synthesis in Petunia hybrida: partial !1characterization of dihydroflavonol-4-reductase genes. !$#cross-references MUID:91370831; PMID:2491667 !$#accession S07463 !'##molecule_type mRNA !'##residues 1-373 ##label BEL !'##cross-references EMBL:X15537; NID:g20543; PIDN:CAA33544.1; !1PID:g20544 !'##note the authors translated the codon AAT for residue 219 as Asp CLASSIFICATION #superfamily dihydrokaempferol 4-reductase KEYWORDS flavonoid biosynthesis; oxidoreductase SUMMARY #length 373 #molecular-weight 41829 #checksum 3785 SEQUENCE /// ENTRY S38474 #type complete TITLE dihydrokaempferol 4-reductase (EC 1.1.1.219) - tomato ALTERNATE_NAMES dihydroflavonol 4-reductase ORGANISM #formal_name Lycopersicon esculentum #common_name tomato DATE 12-Nov-1999 #sequence_revision 12-Nov-1999 #text_change 12-Nov-1999 ACCESSIONS S38474 REFERENCE S38474 !$#authors Bongue-Bartelsman, M.; O'Neill, S.D.; Tong, Y.; Yoder, J.I. !$#submission submitted to the EMBL Data Library, November 1992 !$#description Characterization of the dihydroflavonol 4-reductase gene in !1tomato. !$#accession S38474 !'##status preliminary !'##molecule_type DNA !'##residues 1-379 ##label BON !'##cross-references EMBL:Z18277; NID:g410489; PID:g410490 CLASSIFICATION #superfamily dihydrokaempferol 4-reductase KEYWORDS oxidoreductase SUMMARY #length 379 #molecular-weight 42428 #checksum 194 SEQUENCE /// ENTRY T08007 #type complete TITLE dihydrokaempferol 4-reductase (EC 1.1.1.219) 2 - common morning-glory ORGANISM #formal_name Ipomoea purpurea #common_name common morning-glory DATE 12-Nov-1999 #sequence_revision 12-Nov-1999 #text_change 12-Nov-1999 ACCESSIONS T08007 REFERENCE Z16284 !$#authors Tiffin, P.; Miller, R.E.; Rausher, M.D. !$#submission submitted to the EMBL Data Library, October 1997 !$#description Regulation of anthocyanin gene expression in Ipomoea !1purpurea. !$#accession T08007 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-386 ##label TIF !'##cross-references EMBL:AF028601; NID:g2599071; PIDN:AAB84048.1; !1PID:g2599072 GENETICS !$#gene DFR-FL2 CLASSIFICATION #superfamily dihydrokaempferol 4-reductase KEYWORDS flavonoid biosynthesis; oxidoreductase SUMMARY #length 386 #molecular-weight 43309 #checksum 1068 SEQUENCE /// ENTRY CBBY2 #type complete TITLE L-lactate dehydrogenase (cytochrome) (EC 1.1.2.3) precursor - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES cytochrome b2; flavocytochrome B2; protein YM9958.08c; protein YML054c ORGANISM #formal_name Saccharomyces cerevisiae DATE 24-Apr-1984 #sequence_revision 31-Mar-1993 #text_change 21-Jul-2000 ACCESSIONS A24583; S49806; A91136; A93173; A23095; A90671; A00175 REFERENCE A24583 !$#authors Guiard, B. !$#journal EMBO J. (1985) 4:3265-3272 !$#title Structure, expression and regulation of a nuclear gene !1encoding a mitochondrial protein: the yeast L-(+)-lactate !1cytochrome c oxidoreductase (cytochrome b(2)). !$#cross-references MUID:86135959; PMID:3004948 !$#accession A24583 !'##molecule_type DNA !'##residues 1-591 ##label GUI1 !'##cross-references EMBL:X03215; NID:g3632; PIDN:CAA26959.1; PID:g3633 REFERENCE S49800 !$#authors Devlin, K.; Churcher, C. !$#submission submitted to the EMBL Data Library, November 1994 !$#accession S49806 !'##molecule_type DNA !'##residues 1-591 ##label DEV !'##cross-references EMBL:Z46729; NID:g577134; PIDN:CAA86721.1; !1PID:g577142; GSPDB:GN00013; MIPS:YML054c REFERENCE A91136 !$#authors Ghrir, R.; Becam, A.M.; Lederer, F. !$#journal Eur. J. Biochem. (1984) 139:59-74 !$#title Primary structure of flavocytochrome b2 from baker's yeast. !$#cross-references MUID:84132029; PMID:6365548 !$#accession A91136 !'##molecule_type protein !'##residues 80,82-164,'E',166-394 ##label GHR REFERENCE A93173 !$#authors Guiard, B.; Lederer, F.; Jacq, C. !$#journal Nature (1975) 255:422-423 !$#title More similarity between bakers' yeast L-(+)-lactate !1dehydrogenase and liver microsomal cytochrome b(5). !$#cross-references MUID:75156546; PMID:165435 !$#accession A93173 !'##molecule_type protein !'##residues 'N',82-94 ##label GUI2 REFERENCE A91154 !$#authors Lederer, F.; Cortial, S.; Becam, A.M.; Haumont, P.Y.; Perez, !1L. !$#journal Eur. J. Biochem. (1985) 152:419-428 !$#title Complete amino acid sequence of flavocytochrome b2 from !1baker's yeast. !$#cross-references MUID:86030284; PMID:3902473 !$#accession A23095 !'##molecule_type protein !'##residues 395-465,'Q',467-513,'E',515-591 ##label LED REFERENCE A90671 !$#authors Guiard, B.; Lederer, F. !$#journal Biochimie (1976) 58:305-316 !$#title Complete amino acid sequence of the heme-binding core in !1bakers' yeast cytochrome b(2) (L-(+)-lactate dehydrogenase). !$#cross-references MUID:76206228; PMID:776230 !$#accession A90671 !'##molecule_type protein !'##residues 88-121,'D',123-164,'E',166-183 ##label GUI3 REFERENCE A44532 !$#authors Xia, Z.; Mathews, F.S. !$#journal J. Mol. Biol. (1990) 212:837-863 !$#title Molecular structure of flavocytochrome b-2 at 2.4 angstrom !1resolution. !$#cross-references MUID:90230315; PMID:2329585 !$#contents annotation; X-ray crystallography, 2.4 angstroms GENETICS !$#gene SGD:CYB2; MIPS:YML054c !'##cross-references SGD:S0004518; MIPS:YML054c !$#map_position 13L !$#genome nuclear CLASSIFICATION #superfamily lactate dehydrogenase (cytochrome); !1(S)-2-hydroxy-acid oxidase homology; cytochrome b5 core !1homology KEYWORDS chromoprotein; electron transfer; flavoprotein; FMN; heme; !1homotetramer; iron; metalloprotein; mitochondrion; !1oxidoreductase; respiratory chain FEATURE !$1-80 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$81-591 #product L-lactate dehydrogenase (cytochrome) #status !8predicted #label MAT\ !$88-159 #domain cytochrome b5 core homology #label CB5\ !$200-504 #domain (S)-2-hydroxy-acid oxidase homology #label !82HY\ !$123,146 #binding_site heme iron (His) (axial ligands) #status !8experimental\ !$429,459,493,513 #binding_site FMN (Lys, Asp, Arg, Arg) #status !8experimental\ !$453 #active_site His #status experimental SUMMARY #length 591 #molecular-weight 65539 #checksum 2055 SEQUENCE /// ENTRY S06600 #type complete TITLE L-lactate dehydrogenase (cytochrome) (EC 1.1.2.3) precursor - yeast (Pichia anomala) ALTERNATE_NAMES flavocytochrome B2 ORGANISM #formal_name Pichia anomala, Candida pelliculosa DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS S06600; S00223; S12297 REFERENCE S06600 !$#authors Risler, Y.; Tegoni, M.; Gervais, M. !$#journal Nucleic Acids Res. (1989) 17:8381 !$#title Nucleotide sequence of the Hansenula anomala gene encoding !1flavocytochrome b(2) (L-lactate:cytochrome c !1oxidoreductase). !$#cross-references MUID:90045973; PMID:2813072 !$#accession S06600 !'##status translation not shown !'##molecule_type DNA !'##residues 1-573 ##label RIS !'##cross-references EMBL:X16051; NID:g2747; PIDN:CAA34183.1; PID:g2748 REFERENCE S00223 !$#authors Haumont, P.Y.; Thomas, M.A.; Labeyrie, F.; Lederer, F. !$#journal Eur. J. Biochem. (1987) 169:539-546 !$#title Amino-acid sequence of the cytochrome-b5-like heme-binding !1domain from Hansenula anomala flavocytochrome b2. !$#cross-references MUID:88082787; PMID:3319613 !$#accession S00223 !'##molecule_type protein !'##residues 80-163 ##label HAU REFERENCE S12297 !$#authors Gervais, M.; Corazzin, S.; Risler, Y. !$#journal Biochimie (1982) 64:509-522 !$#title How the loss of several residues, at the level of one !1interglobule junction, modulates the lactate dehydrogenase !1activity of yeast flavocytochrome b(2): a study of the !1nicked enzymes resulting from clostripain and trypsin !1action. !$#cross-references MUID:83023364; PMID:6751411 !$#accession S12297 !'##molecule_type protein !'##residues 374-410,'E',412-423,'I' ##label GER CLASSIFICATION #superfamily lactate dehydrogenase (cytochrome); !1(S)-2-hydroxy-acid oxidase homology; cytochrome b5 core !1homology KEYWORDS chromoprotein; electron transfer; flavoprotein; FMN; heme; !1iron; metalloprotein; mitochondrion; oxidoreductase; !1respiratory chain FEATURE !$1-73 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$74-573 #product L-lactate dehydrogenase (cytochrome) #status !8predicted #label MAT\ !$80-151 #domain cytochrome b5 core homology #label CB5\ !$185-483 #domain (S)-2-hydroxy-acid oxidase homology #label !82HY\ !$115,138 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$408,438,472,492 #binding_site FMN (Lys, Asp, Arg, Arg) #status !8predicted\ !$432 #active_site His #status predicted SUMMARY #length 573 #molecular-weight 64201 #checksum 2105 SEQUENCE /// ENTRY OXRTGU #type complete TITLE L-gulonolactone oxidase (EC 1.1.3.8) - rat ALTERNATE_NAMES L-gulono-gamma-lactone oxidase; methylguanidine-synthesizing enzyme ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1989 #sequence_revision 14-Jul-1994 #text_change 16-Jun-2000 ACCESSIONS A45123; A61199; B61199; A28266; S06473; A56673 REFERENCE A45123 !$#authors Nishikimi, M.; Kawai, T.; Yagi, K. !$#journal J. Biol. Chem. (1992) 267:21967-21972 !$#title Guinea pigs possess a highly mutated gene for !1L-gulono-gamma-lactone oxidase, the key enzyme for !1L-ascorbic acid biosynthesis missing in this species. !$#cross-references MUID:93016162; PMID:1400507 !$#accession A45123 !'##molecule_type DNA !'##residues 1-440 ##label NIS !'##cross-references GB:D12744 !'##note sequence extracted from NCBI backbone (NCBIP:116851) REFERENCE A61199 !$#authors Nishikimi, M.; Yagi, K. !$#journal Am. J. Clin. Nutr. (1991) 54:1203S-1208S !$#title Molecular basis for the deficiency in humans of !1gulonolactone oxidase, a key enzyme for ascorbic acid !1biosynthesis. !$#cross-references MUID:92074404; PMID:1962571 !$#accession A61199 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-403,'Q',405-440 ##label NI2 !'##note this is a revision to the sequence from reference A28266 !$#accession B61199 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 202-237;264-367;399-403,'Q',405-440 ##label NI3 REFERENCE A28266 !$#authors Koshizaka, T.; Nishikimi, M.; Ozawa, T.; Yagi, K. !$#journal J. Biol. Chem. (1988) 263:1619-1621 !$#title Isolation and sequence analysis of a complementary DNA !1encoding rat liver L-gulono-gamma-lactone oxidase, a key !1enzyme for L-ascorbic acid biosynthesis. !$#cross-references MUID:88115275; PMID:3338984 !$#accession A28266 !'##molecule_type mRNA !'##residues 1-188,'Q',190-403,'Q',405-440 ##label KOS !'##cross-references GB:J03536; NID:g204149; PIDN:AAA41164.1; !1PID:g204150 REFERENCE S06473 !$#authors Nishikimi, M.; Koshizaka, T.; Ozawa, T.; Yagi, K. !$#journal Arch. Biochem. Biophys. (1988) 267:842-846 !$#title Occurrence in humans and guinea pigs of the gene related to !1their missing enzyme L-gulono-gamma-lactone oxidase. !$#cross-references MUID:89104405; PMID:3214183 !$#accession S06473 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 202-237 ##label NI4 !'##cross-references GB:D00526; GB:M27451; NID:g220747; PIDN:BAA33497.1; !1PID:g3702677 REFERENCE A56673 !$#authors Fujitsuka, N.; Yokozawa, T.; Oura, H.; Akao, T.; Kobashi, !1K.; Ienaga, K.; Nakamura, K. !$#journal Nephron (1993) 63:445-451 !$#title L-gulono-gamma-lactone oxidase is the enzyme responsible for !1the production of methylguanidine in the rat liver. !$#cross-references MUID:93211519; PMID:8459881 !$#accession A56673 !'##molecule_type protein !'##residues 2-18,'X',20-31,'X',33-34,'X',36-37,'X',39-41 ##label FUJ !'##experimental_source liver microsomes !'##note sequence extracted from NCBI backbone (NCBIP:128443) COMMENT This microsomal membrane flavoprotein catalyzes the !1oxidation of L-gulono-1,4-lactone to L-xylo-hexulonolactone, !1which spontaneously isomerizes to L-ascorbic acid. GENETICS !$#gene GULO !$#introns 1/3; 35/3; 77/3; 109/2; 139/3; 201/3; 237/3; 263/2; 313/2; !1368/2; 398/3 CLASSIFICATION #superfamily L-gulonolactone oxidase KEYWORDS ascorbic acid biosynthesis; FAD; flavoprotein; microsome; !1oxidoreductase; transmembrane protein FEATURE !$2-440 #product L-gulonolactone oxidase #status experimental !8#label MAT SUMMARY #length 440 #molecular-weight 50643 #checksum 9782 SEQUENCE /// ENTRY A38084 #type complete TITLE galactose oxidase (EC 1.1.3.9) precursor [validated] - fungus (Cladobotryum dendroides) ORGANISM #formal_name Cladobotryum dendroides DATE 20-Oct-2000 #sequence_revision 20-Oct-2000 #text_change 20-Oct-2000 ACCESSIONS A38084 REFERENCE A38084 !$#authors McPherson, M.J.; Ogel, Z.B.; Stevens, C.; Yadav, K.D.S.; !1Keen, J.N.; Knowles, P.F. !$#journal J. Biol. Chem. (1992) 267:8146-8152 !$#title Galactose oxidase of Dactylium dendroides. Gene cloning and !1sequence analysis. !$#cross-references MUID:92235025; PMID:1569070 !$#accession A38084 !'##molecule_type DNA !'##residues 1-728 ##label MCP !'##cross-references GB:M86819 !'##note it is uncertain whether Met-1 or Met-49 is the initiator !'##note parts of this sequence, including the amino end of the mature !1protein, were confirmed by protein sequencing REFERENCE A48244 !$#authors Ito, N.; Phililips, S.E.V.; Stevens, C.; Ogel, Z.B.; !1McPherson, M.J.; Keen, J.N.; Yadav, K.D.S.; Knowles, P.F. !$#journal Nature (1991) 350:87-90 !$#title Novel thioether bond revealed by a 1.7 angstrom crystal !1structure of galactose oxidase. !$#cross-references MUID:91163641; PMID:2002850 !$#contents annotation REFERENCE A51740 !$#authors Ito, N.; Phillips, S.E.V.; Knowles, P.F. !$#submission submitted to the Brookhaven Protein Data Bank, September !11993 !$#cross-references PDB:1GOF !$#contents annotation; X-ray crystallography, 1.7 angstroms, residues !190-728 REFERENCE A51741 !$#authors Ito, N.; Phillips, S.E.V.; Knowles, P.F. !$#submission submitted to the Brookhaven Protein Data Bank, September !11993 !$#cross-references PDB:1GOG !$#contents annotation; X-ray crystallography, 1.9 angstroms, residues !190-728 REFERENCE A51742 !$#authors Ito, N.; Phillips, S.E.V.; Knowles, P.F. !$#submission submitted to the Brookhaven Protein Data Bank, September !11993 !$#cross-references PDB:1GOH !$#contents annotation; X-ray crystallography, 2.2 angstroms, residues !190-728 GENETICS !$#gene gaoA CLASSIFICATION #superfamily Cladobotryum dendroides galactose oxidase KEYWORDS disulfide bond; metal binding; oxidoreductase FEATURE !$1-64 #domain signal sequence #status predicted #label SIG\ !$65-89 #domain propeptide #status predicted #label PRO\ !$90-728 #product galactose oxidase #status experimental !8#label MAT\ !$107-116,604-607 #disulfide_bonds #status experimental\ !$317-361 #cross-link cysteinyltyrosine (Cys-Tyr) #status !8experimental\ !$361,584,585,670 #binding_site copper (Tyr, Tyr, His, His) #status !8experimental\ !$419 #binding_site substrate (Arg) #status predicted SUMMARY #length 728 #molecular-weight 78066 #checksum 1641 SEQUENCE /// ENTRY OXHQAP #type complete TITLE alcohol oxidase (EC 1.1.3.13) - yeast (Pichia angusta) ALTERNATE_NAMES methanol oxidase ORGANISM #formal_name Pichia angusta DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 20-Apr-2000 ACCESSIONS A23010; A05223 REFERENCE A93565 !$#authors Ledeboer, A.M.; Edens, L.; Maat, J.; Visser, C.; Bos, J.W.; !1Verrips, C.T. !$#journal Nucleic Acids Res. (1985) 13:3063-3082 !$#title Molecular cloning and characterization of a gene coding for !1methanol oxidase in Hansenula polymorpha. !$#cross-references MUID:85215671; PMID:2582370 !$#accession A23010 !'##molecule_type DNA !'##residues 1-664 ##label LED !'##cross-references GB:X02425; NID:g2778; PIDN:CAA26278.1; PID:g2780 COMMENT This enzyme catalyzes the oxidation of methanol and other !1lower primary alcohols to the corresponding aldehyde and !1hydrogen peroxide. It is the first reaction in C1-metabolism !1in yeast wherein methanol is oxidized to formaldehyde, which !1is then broken down to carbon dioxide. CLASSIFICATION #superfamily alcohol oxidase KEYWORDS alcohol metabolism; flavoprotein; one-carbon metabolism; !1oxidoreductase FEATURE !$8-39 #region beta-alpha-beta FAD nucleotide-binding fold SUMMARY #length 664 #molecular-weight 74089 #checksum 9367 SEQUENCE /// ENTRY JC1117 #type complete TITLE alcohol oxidase (EC 1.1.3.13) precursor - yeast (Candida boidinii) ORGANISM #formal_name Candida boidinii DATE 09-Oct-1992 #sequence_revision 09-May-1997 #text_change 11-Jun-1999 ACCESSIONS JC1117; PS0393 REFERENCE JC1117 !$#authors Sakai, Y.; Tani, Y. !$#journal Gene (1992) 114:67-73 !$#title Cloning and sequencing of the alcohol oxidase-encoding gene !1(AOD1) from the formaldehyde-producing asporogeneous !1methylotrophic yeast, Candida boidinii S2. !$#cross-references MUID:92267386; PMID:1587486 !$#accession JC1117 !'##molecule_type DNA !'##residues 1-663 ##label SAK !'##cross-references GB:M81702; NID:g170819; PIDN:AAA34321.1; !1PID:g170820 !'##experimental_source strain S2 !$#accession PS0393 !'##molecule_type protein !'##residues 2-11,'X',13-18,'X',20-35 ##label SAK1 COMMENT In methylotrophic yeast, this enzyme participates in the !1oxidation of methanol to formaldehyde. GENETICS !$#gene AOD1 CLASSIFICATION #superfamily alcohol oxidase KEYWORDS alcohol metabolism; FAD; oxidoreductase FEATURE !$2-663 #product alcohol oxidase #status experimental #label !8MAT\ !$8-38 #region beta-alpha-beta FAD nucleotide-binding fold SUMMARY #length 663 #molecular-weight 74082 #checksum 6922 SEQUENCE /// ENTRY A23483 #type fragment TITLE alcohol oxidase (EC 1.1.3.13) - yeast (Pichia pastoris) (fragment) ORGANISM #formal_name Pichia pastoris DATE 05-Jun-1987 #sequence_revision 09-May-1997 #text_change 09-May-1997 ACCESSIONS A23483 REFERENCE A23483 !$#authors Ellis, S.B.; Brust, P.F.; Koutz, P.J.; Waters, A.F.; !1Harpold, M.M.; Gingeras, T.R. !$#journal Mol. Cell. Biol. (1985) 5:1111-1121 !$#cross-references MUID:85213482; PMID:3889590 !$#accession A23483 !'##molecule_type protein !'##residues 1-33 ##label ELL CLASSIFICATION #superfamily alcohol oxidase KEYWORDS alcohol metabolism; FAD; flavoprotein; oxidoreductase FEATURE !$8-33 #region beta-alpha-beta FAD nucleotide-binding fold !8(fragment) SUMMARY #length 33 #checksum 1730 SEQUENCE /// ENTRY A39019 #type complete TITLE glucose dehydrogenase (acceptor) (EC 1.1.99.10) - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 27-Nov-1991 #sequence_revision 09-May-1997 #text_change 16-Jun-2000 ACCESSIONS A39019; S06628 REFERENCE A39019 !$#authors Krasney, P.A.; Carr, C.; Cavener, D.R. !$#journal Mol. Biol. Evol. (1990) 7:155-177 !$#title Evolution of the glucose dehydrogenase gene in Drosophila. !$#cross-references MUID:90205602; PMID:2108306 !$#accession A39019 !'##molecule_type DNA !'##residues 1-612 ##label KRA !'##cross-references GB:M29298; NID:g157499; PIDN:AAA28571.1; !1PID:g157500 REFERENCE S06628 !$#authors Whetten, R.; Organ, E.; Krasney, P.; Cox-Foster, D.; !1Cavener, D. !$#journal Genetics (1988) 120:475-484 !$#title Molecular structure and transformation of the glucose !1dehydrogenase gene in Drosophila melanogaster. !$#cross-references MUID:89065357; PMID:3143620 !$#accession S06628 !'##molecule_type DNA !'##residues 1-96 ##label WHE !'##cross-references EMBL:X13582; NID:g8008; PIDN:CAA31918.1; !1PID:g1841419 GENETICS !$#gene FlyBase:Gld !'##cross-references FlyBase:FBgn0001112 !$#map_position 3 84C8 !$#introns 56/3 CLASSIFICATION #superfamily alcohol oxidase KEYWORDS FAD; flavoprotein; oxidoreductase FEATURE !$66-95 #region beta-alpha-beta FAD nucleotide-binding fold SUMMARY #length 612 #molecular-weight 66863 #checksum 8589 SEQUENCE /// ENTRY B39019 #type complete TITLE glucose dehydrogenase (acceptor) (EC 1.1.99.10) - fruit fly (Drosophila pseudoobscura) ORGANISM #formal_name Drosophila pseudoobscura DATE 27-Nov-1991 #sequence_revision 09-May-1997 #text_change 09-May-1997 ACCESSIONS B39019 REFERENCE A39019 !$#authors Krasney, P.A.; Carr, C.; Cavener, D.R. !$#journal Mol. Biol. Evol. (1990) 7:155-177 !$#title Evolution of the glucose dehydrogenase gene in Drosophila. !$#cross-references MUID:90205602; PMID:2108306 !$#accession B39019 !'##molecule_type DNA !'##residues 1-612 ##label KRA !'##cross-references GB:M29299 GENETICS !$#gene FlyBase:Dpse/Gld !'##cross-references FlyBase:FBgn0012699 CLASSIFICATION #superfamily alcohol oxidase KEYWORDS FAD; flavoprotein; oxidoreductase FEATURE !$66-95 #region beta-alpha-beta FAD nucleotide-binding fold SUMMARY #length 612 #molecular-weight 66971 #checksum 8303 SEQUENCE /// ENTRY S27994 #type complete TITLE alcohol dehydrogenase (EC 1.1.99.-) - Pseudomonas oleovorans plasmid OCT ORGANISM #formal_name Pseudomonas oleovorans DATE 13-Jan-1995 #sequence_revision 09-May-1997 #text_change 11-Jun-1999 ACCESSIONS S27994 REFERENCE S27990 !$#authors van Beilen, J.B.; Eggink, G.; Enequist, H.; Bos, R.; !1Witholt, B. !$#journal Mol. Microbiol. (1992) 6:3121-3136 !$#title DNA sequence determination and functional characterization !1of the OCT-plasmid-encoded alkJKL genes of Pseudomonas !1oleovorans. !$#cross-references MUID:93086421; PMID:1453953 !$#accession S27994 !'##molecule_type DNA !'##residues 1-558 ##label VAN !'##cross-references EMBL:X65936; NID:g49078; PIDN:CAA46737.1; !1PID:g49083 GENETICS !$#gene alkJ !$#genome plasmid OCT CLASSIFICATION #superfamily alcohol oxidase KEYWORDS alcohol metabolism; FAD; flavoprotein; oxidoreductase FEATURE !$3-32 #region beta-alpha-beta FAD nucleotide-binding fold SUMMARY #length 558 #molecular-weight 61195 #checksum 9908 SEQUENCE /// ENTRY S10901 #type complete TITLE choline dehydrogenase (EC 1.1.99.1) betA - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 23-Sep-1997 #text_change 01-Mar-2002 ACCESSIONS S15182; G64757; S10901 REFERENCE S15178 !$#authors Lamark, T.; Kaasen, I.; Eshoo, M.W.; Falkenberg, P.; !1McDougall, J.; Strom, A.R. !$#journal Mol. Microbiol. (1991) 5:1049-1064 !$#title DNA sequence and analysis of the bet genes encoding the !1osmoregulatory choline-glycine betaine pathway of !1Escherichia coli. !$#cross-references MUID:92065800; PMID:1956285 !$#accession S15182 !'##molecule_type DNA !'##residues 1-556 ##label LAM !'##cross-references EMBL:X52905; NID:g48714; PIDN:CAA37093.1; !1PID:g581047 !'##experimental_source strain K12 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64757 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-556 ##label BLAT !'##cross-references GB:AE000138; GB:U00096; NID:g1786501; !1PIDN:AAC73414.1; PID:g1786503; UWGP:b0311 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene betA !$#map_position 7.5 min !$#start_codon TTG CLASSIFICATION #superfamily alcohol oxidase KEYWORDS FAD; flavoprotein; oxidoreductase FEATURE !$4-33 #region beta-alpha-beta FAD nucleotide-binding fold SUMMARY #length 556 #molecular-weight 61877 #checksum 9615 SEQUENCE /// ENTRY A35459 #type complete TITLE glucose oxidase (EC 1.1.3.4) precursor [validated] - Aspergillus niger ORGANISM #formal_name Aspergillus niger DATE 31-Aug-1990 #sequence_revision 09-May-1997 #text_change 20-Oct-2000 ACCESSIONS A35459; S05668; S14129 REFERENCE A35459 !$#authors Frederick, K.R.; Tung, J.; Emerick, R.S.; Masiarz, F.R.; !1Chamberlain, S.H.; Vasavada, A.; Rosenberg, S.; Chakraborty, !1S.; Schopter, L.M.; Massey, V. !$#journal J. Biol. Chem. (1990) 265:3793-3802 !$#title Glucose oxidase from Aspergillus niger. Cloning, gene !1sequence, secretion from Saccharomyces cerevisiae and !1kinetic analysis of a yeast-derived enzyme. !$#cross-references MUID:90154060; PMID:2406261 !$#accession A35459 !'##molecule_type DNA !'##residues 1-605 ##label FRE !'##cross-references GB:J05242; NID:g166510; PIDN:AAA32695.1; !1PID:g166511 REFERENCE S05668 !$#authors Kriechbaum, M.; Heilmann, H.J.; Wientjes, F.J.; Hahn, M.; !1Jany, K.D.; Gassen, H.G.; Sharif, F.; Alaeddinoglu, G. !$#journal FEBS Lett. (1989) 255:63-66 !$#title Cloning and DNA sequence analysis of the glucose oxidase !1gene from Aspergillus niger NRRL-3. !$#cross-references MUID:90005974; PMID:2792372 !$#accession S05668 !'##molecule_type DNA !'##residues 1-605 ##label KRI !'##cross-references EMBL:X16061; NID:g2356; PIDN:CAA34197.1; PID:g2357 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE S14129 !$#authors Whittington, H.; Kerry-Williams, S.; Bidgood, K.; Dodsworth, !1N.; Peberdy, J.; Dobson, M.; Hinchliffe, E.; Ballance, D.J. !$#journal Curr. Genet. (1990) 18:531-536 !$#title Expression of the Aspergillus niger glucose oxidase gene in !1A. niger, A. nidulans and Saccharomyces cerevisiae. !$#cross-references MUID:91168301; PMID:2076553 !$#accession S14129 !'##status preliminary !'##molecule_type DNA !'##residues 1-32 ##label WHI !'##cross-references GB:X56443; NID:g2354; PIDN:CAA39826.1; PID:g2355 GENETICS !$#gene gox CLASSIFICATION #superfamily alcohol oxidase KEYWORDS FAD; flavoprotein; oxidoreductase FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-605 #product glucose oxidase #status experimental #label !8MAT\ !$43-72 #region beta-alpha-beta FAD nucleotide-binding fold SUMMARY #length 605 #molecular-weight 65638 #checksum 9946 SEQUENCE /// ENTRY S52489 #type complete TITLE choline oxidase (EC 1.1.3.17) - Arthrobacter globiformis ORGANISM #formal_name Arthrobacter globiformis DATE 08-May-1995 #sequence_revision 09-May-1997 #text_change 11-Jun-1999 ACCESSIONS S62689; S62684; S52489 REFERENCE S62684 !$#authors Deshnium, P.; Los, D.A.; Hayashi, H.; Mustardy, L.; Murata, !1N. !$#journal Plant Mol. Biol. (1995) 29:897-907 !$#title Transformation of Synechococcus with a gene for choline !1oxidase enhances tolerance to salt stress. !$#cross-references MUID:96145502; PMID:8555454 !$#accession S62689 !'##status preliminary !'##molecule_type DNA !'##residues 1-547 ##label DES !'##cross-references EMBL:X84895; NID:g685231; PIDN:CAA59321.1; !1PID:g685232 !$#accession S62684 !'##status preliminary !'##molecule_type protein !'##residues 1-21 ##label DE2 CLASSIFICATION #superfamily alcohol oxidase KEYWORDS FAD; flavoprotein; oxidoreductase FEATURE !$15-44 #region beta-alpha-beta FAD nucleotide-binding fold SUMMARY #length 547 #molecular-weight 58865 #checksum 1883 SEQUENCE /// ENTRY OXSPH #type complete TITLE (S)-2-hydroxy-acid oxidase (EC 1.1.3.15), peroxisomal - spinach ALTERNATE_NAMES glycolate oxidase ORGANISM #formal_name Spinacia oleracea #common_name spinach DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 24-Nov-1999 ACCESSIONS A28496; S00621 REFERENCE A28496 !$#authors Volokita, M.; Somerville, C.R. !$#journal J. Biol. Chem. (1987) 262:15825-15828 !$#title The primary structure of spinach glycolate oxidase deduced !1from the DNA sequence of a cDNA clone. !$#cross-references MUID:88058933; PMID:2824469 !$#accession A28496 !'##molecule_type mRNA !'##residues 1-369 ##label VOL !'##cross-references GB:J03492; NID:g170112; PIDN:AAA34030.1; !1PID:g170113 REFERENCE S00621 !$#authors Cederlund, E.; Lindqvist, Y.; Soederlund, G.; Braenden, !1C.I.; Joernvall, H. !$#journal Eur. J. Biochem. (1988) 173:523-530 !$#title Primary structure of glycolate oxidase from spinach. !$#cross-references MUID:88225066; PMID:3286256 !$#accession S00621 !'##molecule_type protein !'##residues 1-369 ##label CED COMMENT This FMN-dependent enzyme catalyzes the second reaction of !1the photorespiratory pathway, the oxidation of glycolate to !1glyoxylate and hydrogen peroxide. It is generally isolated !1as a tetramer or octamer of identical chains. CLASSIFICATION #superfamily (S)-2-hydroxy-acid oxidase; (S)-2-hydroxy-acid !1oxidase homology KEYWORDS blocked amino end; flavoprotein; FMN; oxidoreductase; !1peroxisome; photorespiration FEATURE !$1-369 #product (S)-2-hydroxy-acid oxidase #status !8experimental #label MAT\ !$1-300 #domain (S)-2-hydroxy-acid oxidase homology #label !82HY\ !$1 #modified_site blocked amino end (Met) (probably !8acetylated) #status experimental\ !$254 #active_site His #status predicted SUMMARY #length 369 #molecular-weight 40285 #checksum 2094 SEQUENCE /// ENTRY S75231 #type complete TITLE (S)-2-hydroxy-acid oxidase (EC 1.1.3.15) - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES glycolate oxidase; protein sll1831 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S75231 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75231 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-460 ##label KAN !'##cross-references EMBL:D90903; GB:AB001339; NID:g1652127; !1PIDN:BAA17145.1; PID:g1652221 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene glcF !$#start_codon GTG CLASSIFICATION #superfamily Synechocystis (S)-2-hydroxy-acid oxidase KEYWORDS oxidoreductase SUMMARY #length 460 #molecular-weight 50548 #checksum 6792 SEQUENCE /// ENTRY E69984 #type complete TITLE glycolate oxidase subunit homolog ysfD - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS E69984 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69984 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-444 ##label KUN !'##cross-references GB:Z99118; GB:AL009126; NID:g2635200; !1PIDN:CAB14829.1; PID:g2635334 !'##experimental_source strain 168 GENETICS !$#gene ysfD CLASSIFICATION #superfamily Synechocystis (S)-2-hydroxy-acid oxidase SUMMARY #length 444 #molecular-weight 49205 #checksum 8697 SEQUENCE /// ENTRY DEECGD #type complete TITLE glycerol-3-phosphate dehydrogenase (EC 1.1.99.5), aerobic - Escherichia coli (strain K-12) ALTERNATE_NAMES sn-glycerol-3-phosphate dehydrogenase ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 18-Oct-1996 #text_change 01-Mar-2002 ACCESSIONS A39186; JT0465; A32355; E65138 REFERENCE A39186 !$#authors Austin, D.; Larson, T.J. !$#journal J. Bacteriol. (1991) 173:101-107 !$#title Nucleotide sequence of the glpD gene encoding aerobic !1sn-glycerol 3-phosphate dehydrogenase of Escherichia coli !1K-12. !$#cross-references MUID:91100269; PMID:1987111 !$#accession A39186 !'##molecule_type DNA !'##residues 1-501 ##label AUS !'##cross-references GB:M55989; NID:g147837; PIDN:AAA24636.1; !1PID:g147838 REFERENCE JT0476 !$#authors Choi, Y.L.; Kawase, S.; Kawamukai, M.; Utsumi, R.; Sakai, !1H.; Komano, T. !$#journal Agric. Biol. Chem. (1989) 53:1135-1143 !$#title Nucleotide sequence of the glycerol-3-phosphate !1dehydrogenase gene of Escherichia coli and regulation by the !1cAMP-CRP complex. !$#accession JT0465 !'##molecule_type DNA !'##residues 1-22,'G',24-327,'HVLPVITPLIFMMKMAKHRCCRYSAA',354-463, !1'ARRPVASHKTRHVAKCGSTISCESVAGGVYAAEVIAGVVN' ##label CHO !'##note probable errors in the sequence from reference JT0476 are !1discussed in reference A39186 REFERENCE A32355 !$#authors Ye, S.; Larson, T.J. !$#journal J. Bacteriol. (1988) 170:4209-4215 !$#title Structures of the promoter and operator of the glpD gene !1encoding aerobic sn-glycerol-3-phosphate dehydrogenase of !1Escherichia coli K-12. !$#cross-references MUID:88314921; PMID:3045087 !$#accession A32355 !'##molecule_type DNA !'##residues 1-61 ##label YES !'##cross-references GB:M21277; NID:g146180; PIDN:AAA23885.1; !1PID:g146181 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65138 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-501 ##label BLAT !'##cross-references GB:AE000418; GB:U00096; NID:g2367222; !1PIDN:AAC76451.1; PID:g2367226; UWGP:b3426 !'##experimental_source strain K-12, substrain MG1655 COMMENT Residues 5-34 form a structure known as the Rossmann fold, !1comprising an alpha helix flanked by beta-structure. It is !1this structure that binds the AMP moiety of the flavin !1cofactor. GENETICS !$#gene glpD !$#map_position 75 min CLASSIFICATION #superfamily glycerol-3-phosphate dehydrogenase (aerobic) KEYWORDS FAD; flavoprotein; glycerol metabolism; oxidoreductase FEATURE !$5-33 #region beta-alpha-beta FAD nucleotide-binding fold SUMMARY #length 501 #molecular-weight 56750 #checksum 5612 SEQUENCE /// ENTRY DEECNA #type complete TITLE glycerol-3-phosphate dehydrogenase (EC 1.1.99.5) chain A, anaerobic [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 01-Mar-2002 ACCESSIONS A32006; G64994 REFERENCE A32006 !$#authors Cole, S.T.; Eiglmeier, K.; Ahmed, S.; Honore, N.; Elmes, L.; !1Anderson, W.F.; Weiner, J.H. !$#journal J. Bacteriol. (1988) 170:2448-2456 !$#title Nucleotide sequence and gene-polypeptide relationships of !1the glpABC operon encoding the anaerobic !1sn-glycerol-3-phosphate dehydrogenase of Escherichia coli !1K-12. !$#cross-references MUID:88227815; PMID:3286606 !$#accession A32006 !'##molecule_type DNA !'##residues 1-542 ##label COL !'##cross-references GB:M20938 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64994 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-542 ##label BLAT !'##cross-references GB:AE000314; GB:U00096; NID:g1788570; !1PIDN:AAC75301.1; PID:g1788574; UWGP:b2241 !'##experimental_source strain K-12, substrain MG1655 COMMENT This is one of the glycerol-3-phosphate dehydrogenases in E. !1coli; it functions under anaerobic growth conditions. The !1solubilized purified enzyme is composed of a catalytic dimer !1of an FAD-binding A chain and an FMN-binding B chain; the !1third component, the C chain, an iron-sulfur protein, is !1involved in binding the enzyme to the cytoplasmic membrane. GENETICS !$#gene glpA !$#map_position 49 min COMPLEX heterodimer; chain A (PIR:DEECNA) and chain B (PIR:DEECNB) !1[validated, MUID:88227815] FUNCTION !$#description EC 1.1.99.5 [validated, MUID:88227815] CLASSIFICATION #superfamily glycerol-3-phosphate dehydrogenase (aerobic) KEYWORDS FAD; flavoprotein; glycerol metabolism; heterodimer; !1oxidoreductase FEATURE !$10-39 #region beta-alpha-beta FAD nucleotide-binding fold SUMMARY #length 542 #molecular-weight 58958 #checksum 6926 SEQUENCE /// ENTRY DEECNB #type complete TITLE glycerol-3-phosphate dehydrogenase (EC 1.1.99.5) chain B, anaerobic [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 01-Mar-2002 ACCESSIONS B32006; H64994 REFERENCE A32006 !$#authors Cole, S.T.; Eiglmeier, K.; Ahmed, S.; Honore, N.; Elmes, L.; !1Anderson, W.F.; Weiner, J.H. !$#journal J. Bacteriol. (1988) 170:2448-2456 !$#title Nucleotide sequence and gene-polypeptide relationships of !1the glpABC operon encoding the anaerobic !1sn-glycerol-3-phosphate dehydrogenase of Escherichia coli !1K-12. !$#cross-references MUID:88227815; PMID:3286606 !$#accession B32006 !'##molecule_type DNA !'##residues 1-419 ##label COL !'##cross-references GB:M20938; NID:g146176; PIDN:AAA83865.1; !1PID:g146178 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64994 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-419 ##label BLAT !'##cross-references GB:AE000314; GB:U00096; NID:g1788570; !1PIDN:AAC75302.1; PID:g1788575; UWGP:b2242 !'##experimental_source strain K-12, substrain MG1655 COMMENT This is one of the glycerol-3-phosphate dehydrogenases in E. !1coli; it functions under anaerobic growth conditions. The !1solubilized purified enzyme is composed of a catalytic dimer !1of an FAD-binding A chain and an FMN-binding B chain; the !1third component, the C chain, an iron-sulfur protein, is !1involved in binding the enzyme to the cytoplasmic membrane. !1The active center is believed to be located on the B chain. GENETICS !$#gene glpB !$#map_position 49 min COMPLEX heterodimer; chain A (PIR:DEECNA) and chain B (PIR:DEECNB) !1[validated, MUID:88227815] FUNCTION !$#description EC 1.1.99.5 [validated, MUID:88227815] CLASSIFICATION #superfamily glycerol-3-phosphate dehydrogenase (anaerobic) !1chain B KEYWORDS flavoprotein; FMN; glycerol metabolism; heterodimer; !1oxidoreductase FEATURE !$4-33 #region beta-alpha-beta FMN nucleotide-binding fold SUMMARY #length 419 #molecular-weight 45357 #checksum 9588 SEQUENCE /// ENTRY D64086 #type complete TITLE glycerol-3-phosphate dehydrogenase (EC 1.1.99.5) chain B, anaerobic - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 18-Aug-1995 #sequence_revision 18-Oct-1996 #text_change 06-Jun-1997 ACCESSIONS D64086 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession D64086 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-442 ##label TIGR !'##cross-references GB:L42023; TIGR:HI0684 CLASSIFICATION #superfamily glycerol-3-phosphate dehydrogenase (anaerobic) !1chain B KEYWORDS flavoprotein; FMN; glycerol metabolism; oxidoreductase FEATURE !$14-43 #region beta-alpha-beta FMN nucleotide-binding fold SUMMARY #length 442 #molecular-weight 48401 #checksum 9976 SEQUENCE /// ENTRY DEECNC #type complete TITLE glycerol-3-phosphate dehydrogenase (EC 1.1.99.5) (anaerobic) chain C [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1991 #sequence_revision 21-Nov-1997 #text_change 01-Mar-2002 ACCESSIONS A64995; C32006 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64995 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-396 ##label BLAT !'##cross-references GB:AE000314; GB:U00096; NID:g1788570; !1PIDN:AAC75303.1; PID:g1788576; UWGP:b2243 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A32006 !$#authors Cole, S.T.; Eiglmeier, K.; Ahmed, S.; Honore, N.; Elmes, L.; !1Anderson, W.F.; Weiner, J.H. !$#journal J. Bacteriol. (1988) 170:2448-2456 !$#title Nucleotide sequence and gene-polypeptide relationships of !1the glpABC operon encoding the anaerobic !1sn-glycerol-3-phosphate dehydrogenase of Escherichia coli !1K-12. !$#cross-references MUID:88227815; PMID:3286606 !$#accession C32006 !'##molecule_type DNA !'##residues 1-168,'V',170-205,'V',207-396 ##label COL !'##cross-references GB:M20938; NID:g146176; PIDN:AAA83866.1; !1PID:g146179 COMMENT This is one of the glycerol-3-phosphate dehydrogenases in E. !1coli; it functions under anaerobic growth conditions. The !1solubilized purified enzyme is composed of a catalytic dimer !1of an FAD-binding A chain and an FMN-binding B chain; the !1third component, the C chain, containing two iron-sulfur !1centers, is tightly associated with the membrane fraction. !1It may serve as the electron acceptor from the catalytic !1dimer; it is also involved in binding the enzyme to the !1cytoplasmic membrane. GENETICS !$#gene glpC !$#map_position 49 min !$#note transcription unit glpABC FUNCTION !$#description EC 1.1.99.5 [validated, MUID:88227815] CLASSIFICATION #superfamily glycerol-3-phosphate dehydrogenase (anaerobic) !1chain C; ferredoxin 2[4Fe-4S] homology KEYWORDS 4Fe-4S; glycerol metabolism; iron-sulfur protein; !1metalloprotein; oxidoreductase FEATURE !$2-74 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$9,12,15,66 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$19,56,59,62 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 396 #molecular-weight 44108 #checksum 6840 SEQUENCE /// ENTRY QPKEX #type complete TITLE glucose dehydrogenase (pyrroloquinoline-quinone) (EC 1.1.99.17) - Gluconobacter oxydans ORGANISM #formal_name Gluconobacter oxydans DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 22-May-1998 ACCESSIONS S17716; S19265 REFERENCE S17716 !$#authors Cleton-Jansen, A.M.; Dekker, S.; van de Putte, P.; Goosen, !1N. !$#journal Mol. Gen. Genet. (1991) 229:206-212 !$#title A single amino acid substitution changes the substrate !1specificity of quinoprotein glucose dehydrogenase in !1Gluconobacter oxydans. !$#cross-references MUID:92017653; PMID:1833618 !$#accession S17716 !'##molecule_type DNA !'##residues 1-808 ##label CLE !'##cross-references EMBL:X62710 REFERENCE S19265 !$#authors Goosen, N. !$#submission submitted to the EMBL Data Library, February 1992 !$#accession S19265 !'##molecule_type DNA !'##residues 1-212,'A',214-808 ##label GOO !'##cross-references EMBL:X62710; NID:g58416; PID:g58417 GENETICS !$#gene gdh FUNCTION !$#description catalyzes the oxidation of D-glucose to D-gluconic acid by !1ubiquinone !$#pathway respiratory chain CLASSIFICATION #superfamily glucose dehydrogenase !1(pyrroloquinoline-quinone) KEYWORDS oxidoreductase; pyrroloquinoline quinone; respiratory chain; !1transmembrane protein FEATURE !$9-28 #domain transmembrane #status predicted #label TM1\ !$35-54 #domain transmembrane #status predicted #label TM2\ !$60-76 #domain transmembrane #status predicted #label TM3\ !$94-110 #domain transmembrane #status predicted #label TM4\ !$122-138 #domain transmembrane #status predicted #label TM5\ !$91,93 #binding_site ubiquinone (Arg, Asp) #status !8predicted\ !$470 #active_site Asp #status predicted SUMMARY #length 808 #molecular-weight 87567 #checksum 4910 SEQUENCE /// ENTRY JV0107 #type complete TITLE glucose dehydrogenase (pyrroloquinoline-quinone) (EC 1.1.99.17) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1992 #sequence_revision 12-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS D64735; JV0107; A45997; S45201; I41228 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64735 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-796 ##label BLAT !'##cross-references GB:AE000122; GB:U00096; NID:g1786315; !1PIDN:AAC73235.1; PID:g1786316; UWGP:b0124 !'##experimental_source strain K-12, substrain MG1655 REFERENCE JV0107 !$#authors Cleton-Jansen, A.M.; Goosen, N.; Fayet, O.; van de Putte, P. !$#journal J. Bacteriol. (1990) 172:6308-6315 !$#title Cloning, mapping, and sequencing of the gene encoding !1Escherichia coli quinoprotein glucose dehydrogenase. !$#cross-references MUID:91035240; PMID:2228962 !$#accession JV0107 !'##molecule_type DNA !'##residues 1-58,'L',60-148,'H',150,'KRRCHT',157-192,'K',194-796 !1##label CLE !'##cross-references GB:X51323; NID:g41553; PIDN:CAA35706.1; PID:g41554 !'##experimental_source strain K12 REFERENCE A45997 !$#authors Yamada, M.; Sumi, K.; Matsushita, K.; Adachi, O.; Yamada, Y. !$#journal J. Biol. Chem. (1993) 268:12812-12817 !$#title Topological analysis of quinoprotein glucose dehydrogenase !1in Escherichia coli and its ubiquinone-binding site. !$#cross-references MUID:93286127; PMID:8509415 !$#accession A45997 !'##status preliminary !'##molecule_type protein !'##residues 1-20 ##label YAM REFERENCE S45181 !$#authors Fujita, N. !$#submission submitted to the EMBL Data Library, January 1994 !$#accession S45201 !'##molecule_type DNA !'##residues 1-796 ##label FUJ !'##cross-references EMBL:D26562; NID:g473770; PIDN:BAA05580.1; !1PID:g473791 !'##experimental_source strain K-12 substrain W3110 REFERENCE I41228 !$#authors Yamada, M.; Asaoka, S.; Saier, M.H.; Yamada, Y. !$#journal J. Bacteriol. (1993) 175:568-571 !$#title Characterization of the gcd gene from Escherichia coli K-12 !1W3110 and regulation of its expression. !$#cross-references MUID:93123180; PMID:8419307 !$#accession I41228 !'##status preliminary !'##molecule_type DNA !'##residues 1-148,'H',150,'KRRCHT',157-192,'K',194-665,'H',667-796 !1##label RES !'##cross-references GB:D12651; NID:g216555; PIDN:BAA02174.1; !1PID:g216556 GENETICS !$#gene gcd !$#map_position 3 min FUNCTION !$#description catalyzes the oxidation of D-glucose to D-gluconic acid by !1ubiquinone !$#pathway respiratory chain CLASSIFICATION #superfamily glucose dehydrogenase !1(pyrroloquinoline-quinone) KEYWORDS oxidoreductase; pyrroloquinoline quinone; respiratory chain; !1transmembrane protein FEATURE !$11-37 #domain transmembrane #status predicted #label TM1\ !$41-59 #domain transmembrane #status predicted #label TM2\ !$63-81 #domain transmembrane #status predicted #label TM3\ !$96-110 #domain transmembrane #status predicted #label TM4\ !$120-140 #domain transmembrane #status predicted #label TM5\ !$93,95 #binding_site ubiquinone (Arg, Asp) #status !8predicted\ !$466 #active_site Asp #status predicted SUMMARY #length 796 #molecular-weight 86747 #checksum 9982 SEQUENCE /// ENTRY S00943 #type complete TITLE glucose dehydrogenase (pyrroloquinoline-quinone) (EC 1.1.99.17) - Acinetobacter calcoaceticus ORGANISM #formal_name Acinetobacter calcoaceticus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S00943 REFERENCE S00943 !$#authors Cleton-Jansen, A.M.; Goosen, N.; Odle, G.; van de Putte, P. !$#journal Nucleic Acids Res. (1988) 16:6228 !$#title Nucleotide sequence of the gene coding for quinoprotein !1glucose dehydrogenase from Acinetobacter calcoaceticus. !$#cross-references MUID:88289368; PMID:3399393 !$#accession S00943 !'##molecule_type DNA !'##residues 1-801 ##label CLE !'##cross-references EMBL:X07235; NID:g38711; PIDN:CAA30222.1; !1PID:g38712 !'##experimental_source strain LMD 79.41 FUNCTION !$#description catalyzes the oxidation of D-glucose to D-gluconic acid by !1ubiquinone !$#pathway respiratory chain CLASSIFICATION #superfamily glucose dehydrogenase !1(pyrroloquinoline-quinone) KEYWORDS oxidoreductase; pyrroloquinoline quinone; respiratory chain; !1transmembrane protein FEATURE !$9-35 #domain transmembrane #status predicted #label TM1\ !$39-57 #domain transmembrane #status predicted #label TM2\ !$61-79 #domain transmembrane #status predicted #label TM3\ !$94-108 #domain transmembrane #status predicted #label TM4\ !$118-137 #domain transmembrane #status predicted #label TM5\ !$91,93 #binding_site ubiquinone (Arg, Asp) #status !8predicted\ !$471 #active_site Asp #status predicted SUMMARY #length 801 #molecular-weight 86956 #checksum 4327 SEQUENCE /// ENTRY DEECFS #type complete TITLE formate dehydrogenase (EC 1.2.1.2) H (hydrogenase-linked) [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES formate dehydrogenase H (benzylviologen-linked) (FDH-H); formate hydrogenlyase complex selenocysteine-containing protein ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Dec-1992 #text_change 01-Mar-2002 ACCESSIONS A24145; F65216; A36088 REFERENCE A24145 !$#authors Zinoni, F.; Birkmann, A.; Stadtman, T.C.; Boeck, A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:4650-4654 !$#title Nucleotide sequence and expression of the !1selenocysteine-containing polypeptide of formate !1dehydrogenase (formate-hydrogen-lyase-linked) from !1Escherichia coli. !$#cross-references MUID:86259655; PMID:2941757 !$#accession A24145 !'##molecule_type DNA !'##residues 1-139,'X',141-715 ##label ZIN !'##cross-references GB:M13563; GB:M18632; NID:g145911; PIDN:AAA23754.1; !1PID:g145912 !'##experimental_source strain MC4100 !'##note the authors translated the selenocysteine UGA codon for residue !1140 as 'X'; we have shown the residue as Cys REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65216 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-139,'X',141-715 ##label BLAT !'##cross-references GB:AE000481; GB:U00096; NID:g2367346; !1PIDN:AAD13462.1; PID:g3868721; UWGP:b4079 !'##experimental_source strain K-12, substrain MG1655 !'##note the authors translated the selenocysteine UGA codon for residue !1140 as 'X'; we have shown the residue as Cys REFERENCE A36088 !$#authors Axley, M.J.; Grahame, D.A.; Stadtman, T.C. !$#journal J. Biol. Chem. (1990) 265:18213-18218 !$#title Escherichia coli formate-hydrogen lyase. Purification and !1properties of the selenium-dependent formate dehydrogenase !1component. !$#cross-references MUID:91009309; PMID:2211698 !$#accession A36088 !'##molecule_type protein !'##residues 1-7,'X',9-10,'X',12 ##label AXL REFERENCE A58332 !$#authors Gladyshev, V.N.; Khangulov, S.V.; Axley, M.J.; Stadtman, !1T.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1994) 91:7708-7711 !$#title Coordination of selenium to molybdenum in formate !1dehydrogenase H from Escherichia coli. !$#cross-references MUID:94329585; PMID:8052647 !$#contents annotation; selenium coordination of cofactor by EPR REFERENCE A67458 !$#authors Sun, P.D.; Boyington, J.C. !$#submission submitted to the Brookhaven Protein Data Bank, January 1997 !$#cross-references PDB:1AA6 !$#contents annotation; X-ray crystallography, 2.3 angstroms, reduced !1form, residues 1-657;676-715 REFERENCE A67589 !$#authors Sun, P.D.; Boyington, J.C. !$#submission submitted to the Brookhaven Protein Data Bank, January 1997 !$#cross-references PDB:1FDI !$#contents annotation; X-ray crystallography, 2.9 angstroms, oxidized !1form, residues 1-715 REFERENCE A67590 !$#authors Sun, P.D.; Boyington, J.C. !$#submission submitted to the Brookhaven Protein Data Bank, January 1997 !$#cross-references PDB:1FDO !$#contents annotation; X-ray crystallography, 2.8 angstroms, oxidized !1form, residues 1-715 REFERENCE A58962 !$#authors Boyington, J.C.; Gladyshev, V.N.; Khangulov, S.V.; Stadtman, !1T.C.; Sun, P.D. !$#journal Science (1997) 275:1305-1308 !$#title Crystal structure of formate dehydrogenase H: catalysis !1involving Mo, molybdopterin, selenocysteine, and an Fe4S4 !1cluster. !$#cross-references MUID:97190104; PMID:9036855 !$#contents annotation; X-ray crystallography GENETICS !$#gene fdhF !$#map_position 92 min COMPLEX associates with chains of hydrogenase 3 (see PIR:H65052, !1PIR:G65052, PIR:S08622, PIR:S08623, PIR:S08624, and !1PIR:S08625) to form formate hydrogenlyase complex FUNCTION !$#description catalyzes the reversible oxidation of formate to carbon !1dioxide with NAD+ CLASSIFICATION #superfamily formate dehydrogenase KEYWORDS 4Fe-4S; iron-sulfur protein; metalloprotein; molybdenum; !1molybdopterin; NAD; oxidoreductase; phosphoprotein; !1selenocysteine FEATURE !$8,11,15,42 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8experimental\ !$44,141 #active_site Lys, His #status predicted\ !$140 #binding_site molybdopterin guanine dinucleotide !8(Cys) (covalent) #status experimental\ !$140 #modified_site selenocysteine #status experimental SUMMARY #length 715 #molecular-weight 79326 #checksum 2913 SEQUENCE /// ENTRY A24698 #type complete TITLE formate dehydrogenase (EC 1.2.1.2) chain A [similarity] - Methanobacterium formicicum ALTERNATE_NAMES formate dehydrogenase alpha subunit ORGANISM #formal_name Methanobacterium formicicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Nov-2000 ACCESSIONS A24698; B42712 REFERENCE A92557 !$#authors Shuber, A.P.; Orr, E.C.; Recny, M.A.; Schendel, P.F.; May, !1H.D.; Schauer, N.L.; Ferry, J.G. !$#journal J. Biol. Chem. (1986) 261:12942-12947 !$#title Cloning, expression, and nucleotide sequence of the formate !1dehydrogenase genes from Methanobacterium formicicum. !$#cross-references MUID:87008493; PMID:3531194 !$#accession A24698 !'##molecule_type DNA !'##residues 1-684 ##label SHU !'##cross-references GB:J02581; NID:g149707; PIDN:AAA72182.1; !1PID:g149708 REFERENCE A42712 !$#authors White, W.B.; Ferry, J.G. !$#journal J. Bacteriol. (1992) 174:4997-5004 !$#title Identification of formate dehydrogenase-specific mRNA !1species and nucleotide sequence of the fdhC gene of !1Methanobacterium formicicum. !$#cross-references MUID:92332434; PMID:1378430 !$#accession B42712 !'##status preliminary !'##molecule_type DNA !'##residues 1-20 ##label WHI !'##cross-references GB:M64798; NID:g149712 !'##experimental_source strain JF-1 !'##note sequence extracted from NCBI backbone (NCBIN:108950, !1NCBIP:108952); this translation is not annotated in GenBank !1entry MBFFDHC, release 117.0 CLASSIFICATION #superfamily formate dehydrogenase KEYWORDS oxidoreductase SUMMARY #length 684 #molecular-weight 75717 #checksum 704 SEQUENCE /// ENTRY JS0628 #type complete TITLE formate dehydrogenase (EC 1.2.1.2) N (nitrate-inducible) alpha chain - Escherichia coli (strain K-12) ALTERNATE_NAMES formate dehydrogenase N selenocysteine-containing protein ORGANISM #formal_name Escherichia coli DATE 31-Mar-1992 #sequence_revision 17-Sep-1997 #text_change 01-Mar-2002 ACCESSIONS E64900; JS0628 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64900 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-195,'X',197-1015 ##label BLAT !'##cross-references GB:AE000244; GB:U00096; NID:g1787742; !1PIDN:AAD13438.1; PID:g3868719; UWGP:b1474 !'##experimental_source strain K-12, substrain MG1655 !'##note the authors translated the selenocysteine UGA codon for residue !1196 as 'X'; we have shown the residue as Cys REFERENCE JS0628 !$#authors Berg, B.L.; Li, J.; Heider, J.; Stewart, V. !$#journal J. Biol. Chem. (1991) 266:22380-22385 !$#title Nitrate-inducible formate dehydrogenase in Escherichia coli !1K-12. I. Nucleotide sequence of the fdnGHI operon and !1evidence that opal (UGA) encodes selenocysteine. !$#cross-references MUID:92042178; PMID:1834669 !$#accession JS0628 !'##molecule_type DNA !'##residues 1-95,'P',97-195,'X',197-483,'GEHAERRRW',492-940,'A', !1942-1015 ##label BER !'##cross-references GB:M75029; NID:g145913 !'##experimental_source strain K12 !'##note the authors translated the selenocysteine UGA codon for residue !1196 as 'X'; we have shown the residue as Cys !'##note this ORF is not annotated in GenBank entry ECOFDNGHI GENETICS !$#gene fdnG !$#map_position 32 min COMPLEX heterotrimer of alpha, beta (see PIR:JS0629) and gamma (see !1PIR:JS0630) chains FUNCTION !$#description catalyzes the reversible oxidation of formate to carbon !1dioxide with NAD+ !$#pathway anaerobic nitrate respiration !$#note this form of the enzyme is induced by anaerobiosis and !1nitrate !$#note formate serves as major electron donor for nitrate !1respiration CLASSIFICATION #superfamily formate dehydrogenase KEYWORDS 4Fe-4S; heterotrimer; iron-sulfur protein; metalloprotein; !1molybdenum; molybdopterin; NAD; oxidoreductase; !1phosphoprotein; selenocysteine FEATURE !$50,53,57,92 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$196 #modified_site selenocysteine #status predicted\ !$196 #binding_site molybdopterin guanine dinucleotide !8(Cys) (covalent) #status experimental SUMMARY #length 1015 #molecular-weight 112916 #checksum 1510 SEQUENCE /// ENTRY S40838 #type complete TITLE formate dehydrogenase (EC 1.2.1.2) O (aerobic) alpha chain - Escherichia coli (strain K-12) ALTERNATE_NAMES formate dehydrogenase O selenocysteine-containing protein ORGANISM #formal_name Escherichia coli DATE 06-Oct-1994 #sequence_revision 17-Sep-1997 #text_change 01-Mar-2002 ACCESSIONS A65195; S40838; S55376 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65195 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-195,'X',197-1016 ##label BLAT !'##cross-references GB:AE000464; GB:U00096; NID:g2367324; !1PIDN:AAD13456.1; PID:g3868720; UWGP:b3894 !'##experimental_source strain K-12, substrain MG1655 !'##note the authors translated the selenocysteine UGA codon for residue !1196 as 'X"; we have shown the residue as Cys REFERENCE S40802 !$#authors Plunkett III, G.; Burland, V.; Daniels, D.L.; Blattner, F.R. !$#journal Nucleic Acids Res. (1993) 21:3391-3398 !$#title Analysis of the Escherichia coli genome. III. DNA sequence !1of the region from 87.2 to 89.2 minutes. !$#cross-references MUID:93347969; PMID:8346018 !$#accession S40838 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-195,'X',197-251,'RREADCDRSC',262-343,'GKRLR',349-1016 !1##label PLU !'##cross-references EMBL:L19201; NID:g304961; PIDN:AAB03027.1; !1PID:g304998 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1993 !'##note the authors translated the selenocysteine UGA codon for residue !1196 as 'X"; we have shown the residue as Cys REFERENCE S55376 !$#authors Abaibou, H.; Pommier, J.; Giordano, G.; Mandrand-Berthelot, !1M. !$#submission submitted to the EMBL Data Library, May 1995 !$#description Expression, characterization and physiological role of the !1Escherichia coli fdo locus specifying aerobic formate !1dehydrogenase. !$#accession S55376 !'##molecule_type DNA !'##residues 1-190 ##label ABA !'##cross-references EMBL:X87583; NID:g853824; PIDN:CAA60887.1; !1PID:g853825 GENETICS !$#gene fdoG !$#map_position 87.2-89.2 min COMPLEX heterotrimer of alpha, beta (see PIR:S40837) and gamma !1chains (see PIR:S40836) FUNCTION !$#description catalyzes the reversible oxidation of formate to carbon !1dioxide with NAD+ !$#note formate may be used as major electron donor during aerobic !1respiration CLASSIFICATION #superfamily formate dehydrogenase KEYWORDS 4Fe-4S; heterotrimer; iron-sulfur protein; metalloprotein; !1molybdenum; molybdopterin; NAD; oxidoreductase; !1phosphoprotein; selenocysteine FEATURE !$50,53,57,92 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$196 #modified_site selenocysteine #status predicted\ !$196 #binding_site molybdopterin guanine dinucleotide !8(Cys) (covalent) #status predicted SUMMARY #length 1016 #molecular-weight 112502 #checksum 4753 SEQUENCE /// ENTRY G70389 #type complete TITLE formate dehydrogenase (EC 1.2.1.2) alpha chain - Aquifex aeolicus ALTERNATE_NAMES formate dehydrogenase selenocysteine-containing protein ORGANISM #formal_name Aquifex aeolicus DATE 08-May-1998 #sequence_revision 15-May-1998 #text_change 11-Jun-1999 ACCESSIONS G70389 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession G70389 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-198,'X',200-1015 ##label AQF !'##cross-references GB:AE000720; NID:g2983529; PIDN:AAC07107.1; !1PID:g2983532; GB:AE000657 !'##experimental_source strain VF5 !'##note the authors translated the selenocysteine UGA codon for residue !1199 as 'X'; we have shown the residue as Cys COMMENT The nature of the molybdopterin cofactor has not been !1determined but is predicted by homology. GENETICS !$#gene fdoG FUNCTION !$#description catalyzes the reversible oxidation of formate to carbon !1dioxide with NAD+ CLASSIFICATION #superfamily formate dehydrogenase KEYWORDS 4Fe-4S; iron-sulfur protein; metalloprotein; molybdenum; !1molybdopterin; NAD; oxidoreductase; phosphoprotein; !1selenocysteine FEATURE !$53,56,60,95 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$199 #modified_site selenocysteine #status predicted\ !$199 #binding_site molybdopterin guanine dinucleotide !8(Cys) (covalent) #status predicted SUMMARY #length 1015 #molecular-weight 114419 #checksum 5918 SEQUENCE /// ENTRY B64042 #type complete TITLE formate dehydrogenase (EC 1.2.1.2) O gamma chain - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B64042 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession B64042 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-257 ##label TIGR !'##cross-references GB:L42023; TIGR:HI0008 CLASSIFICATION #superfamily formate dehydrogenase gamma chain KEYWORDS NAD; oxidoreductase SUMMARY #length 257 #molecular-weight 30060 #checksum 1303 SEQUENCE /// ENTRY JS0630 #type complete TITLE formate dehydrogenase (EC 1.2.1.2) N (nitrate-inducible) gamma chain - Escherichia coli (strain K-12) ALTERNATE_NAMES cytochrome b556 ORGANISM #formal_name Escherichia coli DATE 14-May-1999 #sequence_revision 14-May-1999 #text_change 01-Mar-2002 ACCESSIONS G64900; JS0630 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64900 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-217 ##label BLAT !'##cross-references GB:AE000244; GB:U00096; NID:g1787742; !1PIDN:AAD13440.1; PID:g1787750; UWGP:b1476 !'##experimental_source strain K-12, substrain MG1655 REFERENCE JS0628 !$#authors Berg, B.L.; Li, J.; Heider, J.; Stewart, V. !$#journal J. Biol. Chem. (1991) 266:22380-22385 !$#title Nitrate-inducible formate dehydrogenase in Escherichia coli !1K-12. I. Nucleotide sequence of the fdnGHI operon and !1evidence that opal (UGA) encodes selenocysteine. !$#cross-references MUID:92042178; PMID:1834669 !$#accession JS0630 !'##molecule_type DNA !'##residues 1-159,'YHPDPRHPDPYVYGILGERID' ##label BER !'##cross-references GB:M75029 !'##experimental_source strain K12 !'##note two possible initiation codons are found; the first initiation !1codon would result in six additional residues, !1Met-Thr-Arg-Arg-Ile-Ile, preceding the amino-terminus of the !1sequence shown here; the authors claim that the initiation !1context shown here is more favorable GENETICS !$#gene fdnI COMPLEX heterotrimer of alpha (see PIR:JS0628), beta (see !1PIR:JS0629) and gamma chains FUNCTION !$#description catalyzes the reversible oxidation of formate to carbon !1dioxide with NAD+ !$#pathway anaerobic nitrate respiration !$#note this form of the enzyme is induced by anaerobiosis and !1nitrate !$#note formate serves as major electron donor for nitrate !1respiration !$#note gamma chain is probably the cytochrome b556 component of !1formate dehydrogenase CLASSIFICATION #superfamily formate dehydrogenase gamma chain KEYWORDS heterotrimer; NAD; oxidoreductase; transmembrane protein FEATURE !$21-37 #domain transmembrane #status predicted #label TM1\ !$60-76 #domain transmembrane #status predicted #label TM2\ !$118-134 #domain transmembrane #status predicted #label TM3\ !$152-168 #domain transmembrane #status predicted #label TM4 SUMMARY #length 217 #molecular-weight 25368 #checksum 8604 SEQUENCE /// ENTRY S40836 #type complete TITLE formate dehydrogenase (EC 1.2.1.2) (aerobic) gamma chain [similarity] - Escherichia coli (strain K-12) ALTERNATE_NAMES cytochrome b556 ORGANISM #formal_name Escherichia coli DATE 14-May-1999 #sequence_revision 14-May-1999 #text_change 01-Mar-2002 ACCESSIONS S40836; G65194 REFERENCE S40802 !$#authors Plunkett III, G.; Burland, V.; Daniels, D.L.; Blattner, F.R. !$#journal Nucleic Acids Res. (1993) 21:3391-3398 !$#title Analysis of the Escherichia coli genome. III. DNA sequence !1of the region from 87.2 to 89.2 minutes. !$#cross-references MUID:93347969; PMID:8346018 !$#accession S40836 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-211 ##label PLU !'##cross-references EMBL:L19201; NID:g304961; PIDN:AAB03025.1; !1PID:g304996 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1993 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65194 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-211 ##label BLAT !'##cross-references GB:AE000464; GB:U00096; NID:g2367324; !1PIDN:AAD13454.1; PID:g1790325; UWGP:b3892 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene fdoI COMPLEX heterotrimer of alpha (see PIR:S40838), beta (see !1PIR:S40837) and gamma chains FUNCTION !$#description catalyzes the reversible oxidation of formate to carbon !1dioxide with NAD+ !$#note formate may be used as major electron donor during aerobic !1respiration !$#note gamma chain is probably the cytochrome b556 component of !1formate dehydrogenase CLASSIFICATION #superfamily formate dehydrogenase gamma chain KEYWORDS heterotrimer; NAD; oxidoreductase; transmembrane protein FEATURE !$20-36 #domain transmembrane #status predicted #label TM1\ !$55-71 #domain transmembrane #status predicted #label TM2\ !$116-132 #domain transmembrane #status predicted #label TM3\ !$150-166 #domain transmembrane #status predicted #label TM4 SUMMARY #length 211 #molecular-weight 24606 #checksum 9867 SEQUENCE /// ENTRY A70390 #type complete TITLE formate dehydrogenase (EC 1.2.1.2) gamma chain - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A70390 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession A70390 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-211 ##label AQF !'##cross-references GB:AE000720; NID:g2983529; PIDN:AAC07109.1; !1PID:g2983534; GB:AE000657 !'##experimental_source strain VF5 GENETICS !$#gene fdoI CLASSIFICATION #superfamily formate dehydrogenase gamma chain KEYWORDS heterotrimer; NAD; oxidoreductase; transmembrane protein SUMMARY #length 211 #molecular-weight 24297 #checksum 8366 SEQUENCE /// ENTRY S18215 #type complete TITLE formate dehydrogenase (EC 1.2.1.2) chain C - Wolinella succinogenes ORGANISM #formal_name Wolinella succinogenes DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S18215 REFERENCE S18213 !$#authors Bokranz, M.; Gutmann, M.; Koertner, C.; Kojro, E.; !1Fahrenholz, F.; Lauterbach, F.; Kroeger, A. !$#journal Arch. Microbiol. (1991) 156:119-128 !$#title Cloning and nucleotide sequence of the structural genes !1encoding the formate dehydrogenase of Wolinella !1succinogenes. !$#cross-references MUID:92143671; PMID:1781728 !$#accession S18215 !'##status preliminary !'##molecule_type DNA !'##residues 1-306 ##label BOK !'##cross-references EMBL:X54057; NID:g48506; PIDN:CAA37991.1; !1PID:g48509 GENETICS !$#gene fdhC CLASSIFICATION #superfamily formate dehydrogenase chain C KEYWORDS NAD; oxidoreductase SUMMARY #length 306 #molecular-weight 33848 #checksum 6894 SEQUENCE /// ENTRY DEHUE1 #type complete TITLE aldehyde dehydrogenase (NAD) (EC 1.2.1.3) 1, cytosolic [validated] - human ALTERNATE_NAMES aldehyde dehydrogenase E1 ORGANISM #formal_name Homo sapiens #common_name man DATE 28-May-1986 #sequence_revision 31-Dec-1993 #text_change 03-Jun-2002 ACCESSIONS A33371; I51846; I39431; JC5554; A00363; A61010; A26817 REFERENCE A33371 !$#authors Hsu, L.C.; Chang, W.C.; Yoshida, A. !$#journal Genomics (1989) 5:857-865 !$#title Genomic structure of the human cytosolic aldehyde !1dehydrogenase gene. !$#cross-references MUID:90077427; PMID:2591967 !$#accession A33371 !'##molecule_type DNA !'##residues 1-501 ##label HSU !'##cross-references GB:M31994; NID:g178370; PIDN:AAA51692.1; !1PID:g178372 REFERENCE I51846 !$#authors Yoshida, A.; Hsu, L.C.; Yanagawa, Y. !$#journal Adv. Exp. Med. Biol. (1993) 328:37-44 !$#title Biological role of human cytosolic aldehyde dehydrogenase 1: !1hormonal response, retinal oxidation and implication in !1testicular feminization. !$#cross-references MUID:93263033; PMID:8493914 !$#accession I51846 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-6 ##label YOS1 !'##cross-references GB:S61235; NID:g300399; PIDN:AAD13925.1; !1PID:g4261625 REFERENCE I39431 !$#authors Yoshida, A.; Ikawa, M.; Hsu, L.C.; Tani, K. !$#journal Alcohol (1985) 2:103-106 !$#title Molecular abnormality and cDNA cloning of human aldehyde !1dehydrogenases. !$#cross-references MUID:85252089; PMID:4015823 !$#accession I39431 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 'I',163-501 ##label YOS2 !'##cross-references GB:M26761; NID:g178393; PIDN:AAA35518.1; !1PID:g178394 REFERENCE JC5553 !$#authors Kathmann, E.C.; Lipsky, J.J. !$#journal Biochem. Biophys. Res. Commun. (1997) 236:527-531 !$#title Cloning of a cDNA encoding a constitutively expressed rat !1liver cytosolic aldehyde dehydrogenase. !$#cross-references MUID:97382470; PMID:9240474 !$#accession JC5554 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type mRNA !'##residues 1-120,'S',122-501 ##label KAT !'##cross-references DDBJ:AF003341; NID:g2183298; PIDN:AAC51652.1; !1PID:g2183299 !'##experimental_source liver REFERENCE A00363 !$#authors Hempel, J.; von Bahr-Lindstrom, H.; Jornvall, H. !$#journal Eur. J. Biochem. (1984) 141:21-35 !$#title Aldehyde dehydrogenase from human liver. Primary structure !1of the cytoplasmic isoenzyme. !$#cross-references MUID:84208019; PMID:6723659 !$#accession A00363 !'##molecule_type protein !'##residues 2-501 ##label HEM REFERENCE A61010 !$#authors Agarwal, D.P.; Cohn, P.; Goedde, H.W.; Hempel, J. !$#journal Enzyme (1989) 42:47-52 !$#title Aldehyde dehydrogenase from human erythrocytes: structural !1relationship to the liver cytosolic isozyme. !$#cross-references MUID:89377753; PMID:2776714 !$#accession A61010 !'##molecule_type protein !'##residues !123-27;79-85;101-107;114-128;132-142;144-154;309-319;421-434; !1477-483 ##label AGA !'##experimental_source erythrocytes REFERENCE A26817 !$#authors Abriola, D.P.; Fields, R.; Stein, S.; MacKerell Jr., A.D.; !1Pietruszko, R. !$#journal Biochemistry (1987) 26:5679-5684 !$#title Active site of human liver aldehyde dehydrogenase. !$#cross-references MUID:88050861; PMID:3676276 !$#accession A26817 !'##molecule_type protein !'##residues 266-273 ##label ABR !'##note the active site Glu was identified by suicide inhibition with !1bromoacetophenone GENETICS !$#gene GDB:ALDH1 !'##cross-references GDB:119667; OMIM:100640 !$#map_position 9q21-9q21 COMPLEX homotetramer FUNCTION !$#description catalyzes oxidation of an aldehyde to an acid using NAD+ and !1water !$#note enzymes with this activity are involved in diverse metabolic !1pathways in various organisms and tissues CLASSIFICATION #superfamily aldehyde dehydrogenase (NAD+); aldehyde !1dehydrogenase homology KEYWORDS acetylated amino end; alcohol metabolism; cytosol; !1homotetramer; liver; NAD; oxidoreductase FEATURE !$2-501 #product aldehyde dehydrogenase (NAD+) 1 #status !8experimental #label MAT\ !$59-323 #domain aldehyde dehydrogenase homology #label ALDD\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental\ !$269,303 #active_site Glu, Cys #status experimental\ !$456 #binding_site NAD (Cys) #status experimental SUMMARY #length 501 #molecular-weight 54861 #checksum 4167 SEQUENCE /// ENTRY S02302 #type complete TITLE aldehyde dehydrogenase (NAD) (EC 1.2.1.3) 1, cytosolic - horse ORGANISM #formal_name Equus caballus #common_name domestic horse DATE 01-Dec-1989 #sequence_revision 31-Jan-1997 #text_change 03-Jun-2002 ACCESSIONS S02302 REFERENCE S02302 !$#authors von Bahr-Lindstroem, H.; Hempel, J.; Joernvall, H. !$#journal Eur. J. Biochem. (1984) 141:37-42 !$#title The cytoplasmic isoenzyme of horse liver aldehyde !1dehydrogenase. Relationship to the corresponding human !1isoenzyme. !$#cross-references MUID:84208025; PMID:6723662 !$#accession S02302 !'##molecule_type protein !'##residues 1-500 ##label VON !'##note residues in the regions 1-16 and 443-475 were positioned by !1homology with the human sequence COMPLEX homotetramer FUNCTION !$#description catalyzes the oxidation of an aldehyde to an acid using NAD+ !1and water !$#note enzymes with this activity are involved in diverse metabolic !1pathways in various organisms and tissues CLASSIFICATION #superfamily aldehyde dehydrogenase (NAD+); aldehyde !1dehydrogenase homology KEYWORDS acetylated amino end; alcohol metabolism; cytosol; !1homotetramer; liver; NAD; oxidoreductase FEATURE !$58-322 #domain aldehyde dehydrogenase homology #label ALDD\ !$1 #modified_site blocked amino end (Ser) (probably !8acetylated) #status experimental\ !$268,302 #active_site Glu, Cys #status predicted\ !$455 #binding_site NAD (Cys) #status predicted SUMMARY #length 500 #molecular-weight 54743 #checksum 1205 SEQUENCE /// ENTRY JQ1004 #type complete TITLE aldehyde dehydrogenase (NAD) (EC 1.2.1.3) 1 precursor, cytosolic - mouse ALTERNATE_NAMES aldehyde dehydrogenase II ORGANISM #formal_name Mus musculus #common_name house mouse DATE 23-Nov-1991 #sequence_revision 31-Jan-1997 #text_change 03-Jun-2002 ACCESSIONS JQ1004; A33248; A60126 REFERENCE JQ1004 !$#authors Rongnoparut, P.; Weaver, S. !$#journal Gene (1991) 101:261-265 !$#title Isolation and characterization of a cytosolic aldehyde !1dehydrogenase-encoding cDNA from mouse liver. !$#cross-references MUID:91276281; PMID:2055490 !$#accession JQ1004 !'##molecule_type mRNA !'##residues 1-501 ##label RON !'##cross-references GB:M74570; NID:g191803; PIDN:AAA37202.1; !1PID:g191804 !'##experimental_source liver !$#accession A33248 !'##molecule_type DNA !'##residues 1-22 ##label RO2 !'##cross-references GB:M74571; NID:g191805; PIDN:AAA37203.1; !1PID:g191806 REFERENCE A60126 !$#authors McCaffery, P.; Tempst, P.; Lara, G.; Draeger, U.C. !$#journal Development (1991) 112:693-702 !$#title Aldehyde dehydrogenase is a positional marker in the retina. !$#cross-references MUID:92037178; PMID:1935685 !$#accession A60126 !'##molecule_type protein !'##residues 23-49,'XX',52;'Y',141-150,'X',152-156;211,'XX',214-218,'X', !1220-230;309-320;330-339,'XX',342-349;400-410;421-435;477-490 !1##label MCC !'##experimental_source embryonic mouse retina GENETICS !$#gene Aldh1; Ahd-2 !$#map_position 19 COMPLEX homotetramer FUNCTION !$#description catalyzes the oxidation of an aldehyde to an acid using NAD+ !1and water !$#pathway oxidation of retinaldehyde to retinoic acid !$#note enzymes with this activity are involved in diverse metabolic !1pathways in various organisms and tissues CLASSIFICATION #superfamily aldehyde dehydrogenase (NAD+); aldehyde !1dehydrogenase homology KEYWORDS acetylated amino end; alcohol metabolism; cytosol; !1homotetramer; liver; NAD; oxidoreductase FEATURE !$2-501 #product aldehyde dehydrogenase (NAD+) 1 #status !8predicted #label MAT\ !$59-323 #domain aldehyde dehydrogenase homology #label ALDD\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status predicted\ !$269,303 #active_site Glu, Cys #status predicted\ !$456 #binding_site NAD (Cys) #status predicted SUMMARY #length 501 #molecular-weight 54481 #checksum 1116 SEQUENCE /// ENTRY A32616 #type complete TITLE aldehyde dehydrogenase (NAD) (EC 1.2.1.3) PB, cytosolic - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 21-May-1990 #sequence_revision 31-Jan-1997 #text_change 03-Jun-2002 ACCESSIONS A32616 REFERENCE A32616 !$#authors Dunn, T.J.; Koleske, A.J.; Lindahl, R.; Pitot, H.C. !$#journal J. Biol. Chem. (1989) 264:13057-13065 !$#title Phenobarbital-inducible aldehyde dehydrogenase in the rat. !1cDNA sequence and regulation of the mRNA by phenobarbital in !1responsive rats. !$#cross-references MUID:89327272; PMID:2753900 !$#accession A32616 !'##molecule_type mRNA !'##residues 1-501 ##label DUN !'##cross-references GB:M23995; NID:g202845; PIDN:AAA40718.1; !1PID:g202846 !'##experimental_source strain Long-Evans, liver of males COMMENT This isozyme is expressed at a low level in many tissues. In !1responsive rats, it is inducible by phenobarbitol in liver !1but not in other tissues tested. COMPLEX homotetramer (or larger oligomer) FUNCTION !$#description catalyzes the oxidation of an aldehyde to an acid using NAD+ !1and water !$#pathway catabolism of aliphatic aldehydes !$#note enzymes with this activity are involved in diverse metabolic !1pathways in various organisms and tissues CLASSIFICATION #superfamily aldehyde dehydrogenase (NAD+); aldehyde !1dehydrogenase homology KEYWORDS acetylated amino end; cytosol; homotetramer; liver; NAD; !1oxidoreductase FEATURE !$2-501 #product aldehyde dehydrogenase (NAD+) PB #status !8predicted #label MAT\ !$59-323 #domain aldehyde dehydrogenase homology #label ALDD\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status predicted\ !$269,303 #active_site Glu, Cys #status predicted\ !$456 #binding_site NAD (Cys) #status predicted SUMMARY #length 501 #molecular-weight 54559 #checksum 3036 SEQUENCE /// ENTRY S14629 #type complete TITLE aldehyde dehydrogenase (NAD) (EC 1.2.1.3) 1, cytosolic - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 21-Nov-1993 #sequence_revision 31-Jan-1997 #text_change 03-Jun-2002 ACCESSIONS S14629 REFERENCE S14629 !$#authors Godbout, R. !$#submission submitted to the EMBL Data Library, April 1991 !$#description High levels of aldehyde dehydrogenase transcripts in the !1undifferentiated chick retina. !$#accession S14629 !'##molecule_type mRNA !'##residues 1-509 ##label GOD !'##cross-references EMBL:X58869; NID:g63032; PIDN:CAA41679.1; !1PID:g63033 !'##experimental_source retina COMPLEX homotetramer FUNCTION !$#description catalyzes the oxidation of an aldehyde to an acid using NAD+ !1and water !$#pathway ethanol catabolism !$#note enzymes with this activity are involved in diverse metabolic !1pathways in various organisms and tissues CLASSIFICATION #superfamily aldehyde dehydrogenase (NAD+); aldehyde !1dehydrogenase homology KEYWORDS alcohol metabolism; cytosol; homotetramer; liver; NAD; !1oxidoreductase FEATURE !$67-331 #domain aldehyde dehydrogenase homology #label ALDD\ !$277,311 #active_site Glu, Cys #status predicted\ !$464 #binding_site NAD (Cys) #status predicted SUMMARY #length 509 #molecular-weight 55809 #checksum 190 SEQUENCE /// ENTRY A55684 #type complete TITLE aldehyde dehydrogenase (NAD) (EC 1.2.1.3) 6 precursor, salivary - human ORGANISM #formal_name Homo sapiens #common_name man DATE 03-Mar-1995 #sequence_revision 31-Jan-1997 #text_change 03-Jun-2002 ACCESSIONS A55684 REFERENCE A55684 !$#authors Hsu, L.C.; Chang, W.C.; Hiraoka, L.; Hsieh, C.L. !$#journal Genomics (1994) 24:333-341 !$#title Molecular cloning, genomic organization, and chromosomal !1localization of an additional human aldehyde dehydrogenase !1gene, ALDH6. !$#cross-references MUID:95213025; PMID:7698756 !$#accession A55684 !'##molecule_type mRNA; DNA !'##residues 1-512 ##label HSU !'##cross-references GB:U07919; NID:g995897; PIDN:AAA79036.1; !1PID:g544482 COMMENT This isozyme is found at highest levels in saliva, stomach, !1and kidney and at low levels in many tissues. GENETICS !$#gene GDB:ALDH6 !'##cross-references GDB:364103; OMIM:600463 !$#map_position 15q26-15q26 !$#introns 33/3; 68/3; 115/3; 159/1; 179/3; 222/3; 260/3; 295/1; 356/3; !1411/3; 464/2; 489/2 FUNCTION !$#description catalyzes oxidation of an aldehyde to an acid using NAD+ and !1water !$#note enzymes with this activity are involved in diverse metabolic !1pathways in various organisms and tissues CLASSIFICATION #superfamily aldehyde dehydrogenase (NAD+); aldehyde !1dehydrogenase homology KEYWORDS NAD; oxidoreductase; saliva FEATURE !$70-334 #domain aldehyde dehydrogenase homology #label ALDD\ !$280,314 #active_site Glu, Cys #status predicted\ !$467 #binding_site NAD (Cys) #status predicted SUMMARY #length 512 #molecular-weight 56009 #checksum 2217 SEQUENCE /// ENTRY DEHUE2 #type complete TITLE aldehyde dehydrogenase (NAD) (EC 1.2.1.3) 2 precursor, mitochondrial [validated] - human ALTERNATE_NAMES aldehyde dehydrogenase E2; aldehyde dehydrogenase I ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1988 #sequence_revision 17-Nov-1995 #text_change 03-Jun-2002 ACCESSIONS A29975; S00804; A23503; A27509; A26743; I39432; I39433; !1I39430 REFERENCE A29975 !$#authors Hsu, L.C.; Bendel, R.E.; Yoshida, A. !$#journal Genomics (1988) 2:57-65 !$#title Genomic structure of the human mitochondrial aldehyde !1dehydrogenase gene. !$#cross-references MUID:88256152; PMID:2838413 !$#accession A29975 !'##molecule_type DNA !'##residues 1-517 ##label HSU1 !'##cross-references GB:M26760; NID:g178397; PIDN:AAA51694.1; !1PID:g178398 REFERENCE S00804 !$#authors Braun, T.; Bober, E.; Singh, S.; Agarwal, D.P.; Goedde, H.W. !$#journal FEBS Lett. (1988) 233:440 !$#accession S00804 !'##molecule_type mRNA !'##residues 1-6,'ARA',10,'P',13-49 ##label BRA !'##cross-references EMBL:X05409; NID:g28605 !'##note correction to A26743 REFERENCE A23503 !$#authors Hempel, J.; Kaiser, R.; Joernvall, H. !$#journal Eur. J. Biochem. (1985) 153:13-28 !$#title Mitochondrial aldehyde dehydrogenase from human liver. !1Primary structure, differences in relation to the cytosolic !1enzyme, and functional correlations. !$#cross-references MUID:86055846; PMID:4065146 !$#accession A23503 !'##molecule_type protein !'##residues 'A',19-517 ##label HEM !'##note the sequence shown is presumably that of the mature protein; !1however, the number of alanines at the amino end is !1questionable REFERENCE A27509 !$#authors Braun, T.; Bober, E.; Singh, S.; Agarwal, D.P.; Goedde, H.W. !$#journal Nucleic Acids Res. (1987) 15:3179 !$#title Isolation and sequence analysis of a full length cDNA clone !1coding for human mitochondrial aldehyde dehydrogenase. !$#cross-references MUID:87174836; PMID:3562250 !$#accession A27509 !'##molecule_type mRNA !'##residues 1-6,'AWPAWA',10,'P',12,'VS',15,'RHPGR',21,27-79,'REGRPG', !186-336,'V',338-517 ##label BR2 !'##cross-references EMBL:Y00109; NID:g28607; PIDN:CAA68290.1; !1PID:g28608 REFERENCE A26743 !$#authors Braun, T.; Bober, E.; Singh, S.; Agarwal, D.P.; Goedde, H.W. !$#journal FEBS Lett. (1987) 215:233-236 !$#title Evidence for a signal peptide at the amino-terminal end of !1human mitochondrial aldehyde dehydrogenase. !$#cross-references MUID:87219091; PMID:3582651 !$#accession A26743 !'##molecule_type mRNA !'##residues 1-6,'AWPAWA',10,'P',12,'VS',15,'RHPGR',21,27-79,'REGRPG', !186-336,'V',338-517 ##label BR3 !'##cross-references EMBL:X05409; NID:g28605 !'##note this sequence is revised in reference S00804 REFERENCE I39432 !$#authors Hsu, L.C.; Tani, K.; Fujiyoshi, T.; Kurachi, K.; Yoshida, A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:3771-3775 !$#title Cloning of cDNAs for human aldehyde dehydrogenases 1 and 2. !$#cross-references MUID:85216574; PMID:2987944 !$#accession I39432 !'##status preliminary !'##molecule_type mRNA !'##residues 119-336,'V',338-517 ##label HSU2 !'##cross-references GB:K03001; NID:g178395; PIDN:AAB59500.1; !1PID:g178396 !'##note thirty-three tryptic peptides were also sequenced REFERENCE I39431 !$#authors Yoshida, A.; Ikawa, M.; Hsu, L.C.; Tani, K. !$#journal Alcohol (1985) 2:103-106 !$#title Molecular abnormality and cDNA cloning of human aldehyde !1dehydrogenases. !$#cross-references MUID:85252089; PMID:4015823 !$#accession I39433 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 119-336,'V',338-517 ##label YOS !'##cross-references GB:M26760; NID:g178397; PIDN:AAA51694.1; !1PID:g178398 REFERENCE I39430 !$#authors Agarwal, D.P.; Goedde, H.W. !$#journal Isozymes Curr. Top. Biol. Med. Res. (1987) 16:21-48 !$#title Human aldehyde dehydrogenase isozymes and alcohol !1sensitivity. !$#cross-references MUID:87279033; PMID:3610592 !$#accession I39430 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 214-215,'S',217,'R',219-246,'P',248-336,'V',338-425, !1'EVQDHRGGCWESQQFHVRAG',446-449,'AQRIWTRPITCPSP',464-500 !1##label AGA !'##cross-references GB:M54931; NID:g178391; PIDN:AAA62825.1; !1PID:g178392 !'##note the sequence is misidentified as aldehyde dehydrogenase I GENETICS !$#gene GDB:ALDH2 !'##cross-references GDB:119668; OMIM:100650 !$#map_position 12q24.2-12q24.2 !$#introns 38/3; 73/3; 120/3; 147/2; 184/3; 227/3; 265/3; 300/1; 361/2; !1416/3; 469/2; 507/3 COMPLEX homotetramer FUNCTION !$#description catalyzes the oxidation of an aldehyde to an acid using NAD+ !1and water !$#pathway ethanol catabolism !$#note enzymes with this activity are involved in diverse metabolic !1pathways in various organisms and tissues CLASSIFICATION #superfamily aldehyde dehydrogenase (NAD+); aldehyde !1dehydrogenase homology KEYWORDS alcohol metabolism; homotetramer; liver; mitochondrion; NAD; !1oxidoreductase FEATURE !$1-17 #domain transit peptide (mitochondrion) #status !8predicted #label SIG\ !$18-517 #product aldehyde dehydrogenase (NAD+) 2 #status !8experimental #label MAT\ !$75-339 #domain aldehyde dehydrogenase homology #label ALDD\ !$211-291 #domain NAD binding #status predicted #label NAD\ !$285 #active_site Glu #status predicted\ !$319 #active_site Cys #status experimental\ !$472 #binding_site NAD (Cys) #status predicted SUMMARY #length 517 #molecular-weight 56381 #checksum 428 SEQUENCE /// ENTRY S00364 #type complete TITLE aldehyde dehydrogenase (NAD) (EC 1.2.1.3) 2, mitochondrial - horse (tentative sequence) ORGANISM #formal_name Equus caballus #common_name domestic horse DATE 30-Jun-1989 #sequence_revision 31-Jan-1997 #text_change 03-Jun-2002 ACCESSIONS S00364 REFERENCE S00364 !$#authors Johansson, J.; von Bahr-Lindstroem, H.; Jeck, R.; !1Woenckhaus, C.; Joernvall, H. !$#journal Eur. J. Biochem. (1988) 172:527-533 !$#title Mitochondrial aldehyde dehydrogenase from horse liver. !1Correlations of the same species variants for both the !1cytosolic and the mitochondrial forms of an enzyme. !$#cross-references MUID:88166730; PMID:3350012 !$#accession S00364 !'##molecule_type protein !'##residues 1-500 ##label JOH !'##note amino-terminal residue is uncertain; 1-Ser and 1-Leu were also !1found; forms beginning at residues 2, 4, 5, 7, and 8 were !1also found COMPLEX homotetramer FUNCTION !$#description catalyzes the oxidation of an aldehyde to an acid using NAD+ !1and water !$#pathway ethanol catabolism !$#note enzymes with this activity are involved in diverse metabolic !1pathways in various organisms and tissues CLASSIFICATION #superfamily aldehyde dehydrogenase (NAD+); aldehyde !1dehydrogenase homology KEYWORDS alcohol metabolism; homotetramer; liver; mitochondrion; NAD; !1oxidoreductase FEATURE !$58-322 #domain aldehyde dehydrogenase homology #label ALDD\ !$268,302 #active_site Glu, Cys #status predicted\ !$455 #binding_site NAD (Cys) #status predicted SUMMARY #length 500 #molecular-weight 54166 #checksum 2370 SEQUENCE /// ENTRY S03564 #type complete TITLE aldehyde dehydrogenase (NAD) (EC 1.2.1.3) 2 precursor, mitochondrial - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 28-Feb-1990 #sequence_revision 31-Jan-1997 #text_change 03-Jun-2002 ACCESSIONS S03564; A27713; S12903; S17492 REFERENCE S03564 !$#authors Farres, J.; Guan, K.L.; Weiner, H. !$#journal Eur. J. Biochem. (1989) 180:67-74 !$#title Primary structures of rat and bovine liver mitochondrial !1aldehyde dehydrogenases deduced from cDNA sequences. !$#cross-references MUID:89210865; PMID:2540003 !$#accession S03564 !'##molecule_type mRNA !'##residues 1-519 ##label FAR !'##cross-references EMBL:X14977; NID:g55604; PIDN:CAA33101.1; !1PID:g55605 !'##experimental_source strain Sprague Dawley; liver REFERENCE A27713 !$#authors Farres, J.; Guan, K.L.; Weiner, H. !$#journal Biochem. Biophys. Res. Commun. (1988) 150:1083-1087 !$#title Sequence of the signal peptide for rat liver mitochondrial !1aldehyde dehydrogenase. !$#cross-references MUID:88134217; PMID:3342060 !$#accession A27713 !'##molecule_type mRNA !'##residues 1-29 ##label FA2 !'##cross-references GB:M19030; NID:g202847; PIDN:AAA40719.1; !1PID:g202848 REFERENCE S12903 !$#authors Diwan, J.J.; Paliwal, R.; Kaftan, E.; Bawa, R. !$#journal FEBS Lett. (1990) 273:215-218 !$#title A mitochondrial protein fraction catalyzing transport of the !1K(+) analog T1(+). !$#cross-references MUID:91032184; PMID:1699808 !$#accession S12903 !'##molecule_type protein !'##residues 327-340 ##label DIW REFERENCE S17492 !$#authors Jeng, J.; Weiner, H. !$#journal Arch. Biochem. Biophys. (1991) 289:214-222 !$#title Purification and characterization of catalytically active !1precursor of rat liver mitochondrial aldehyde dehydrogenase !1expressed in Escherichia coli. !$#cross-references MUID:91378548; PMID:1898068 !$#accession S17492 !'##molecule_type protein !'##residues 1-19 ##label JEN GENETICS !$#genome nuclear COMPLEX homotetramer FUNCTION !$#description catalyzes the oxidation of an aldehyde to an acid using NAD+ !1and water !$#pathway ethanol catabolism !$#note enzymes with this activity are involved in diverse metabolic !1pathways in various organisms and tissues CLASSIFICATION #superfamily aldehyde dehydrogenase (NAD+); aldehyde !1dehydrogenase homology KEYWORDS alcohol metabolism; homotetramer; liver; mitochondrion; NAD; !1oxidoreductase FEATURE !$1-19 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$20-519 #product aldehyde dehydrogenase (NAD+) 2 #status !8predicted #label MAT\ !$77-341 #domain aldehyde dehydrogenase homology #label ALDD\ !$287,321 #active_site Glu, Cys #status predicted\ !$474 #binding_site NAD (Cys) #status predicted SUMMARY #length 519 #molecular-weight 56488 #checksum 479 SEQUENCE /// ENTRY I48966 #type complete TITLE aldehyde dehydrogenase (NAD) (EC 1.2.1.3) 2 precursor, mitochondrial - mouse ALTERNATE_NAMES aldehyde dehydrogenase AHD-M1 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 02-Jul-1996 #sequence_revision 31-Jan-1997 #text_change 03-Jun-2002 ACCESSIONS I48966; S50106; I57960 REFERENCE I48966 !$#authors Chang, C.; Yoshida, A. !$#journal Gene (1994) 148:331-336 !$#title Cloning and characterization of the gene encoding mouse !1mitochondrial aldehyde dehydrogenase. !$#cross-references MUID:95047445; PMID:7958964 !$#accession I48966 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA; DNA !'##residues 1-519 ##label RES !'##cross-references EMBL:U07235; NID:g466253; PIDN:AAA64636.1; !1PID:g466254 REFERENCE S50102 !$#authors Caubin, J.; Iglesias, T.; Bernal, J.; Munoz, A.; Marquez, !1G.; Barbero, J.L.; Zaballos, A. !$#journal Nucleic Acids Res. (1994) 22:4132-4138 !$#title Isolation of genomic DNA fragments corresponding to genes !1modulated in vivo by a transcription factor. !$#cross-references MUID:95023181; PMID:7937138 !$#accession S50106 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 472-509 ##label CAU !'##cross-references EMBL:Z32545; NID:g563496 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1March 1994 REFERENCE I57960 !$#authors Chen, M.; Achkar, C.; Gudas, L.J. !$#journal Mol. Pharmacol. (1994) 46:88-96 !$#title Enzymatic conversion of retinaldehyde to retinoic acid by !1cloned murine cytosolic and mitochondrial aldehyde !1dehydrogenases. !$#cross-references MUID:94335908; PMID:8058062 !$#accession I57960 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-87,'C',90-180,182-226,'S',228-343,'G',345-369,'N', !1371-377,'M',379-475,'V',477-519 ##label RE2 !'##cross-references GB:S71509; NID:g560644; PIDN:AAC60691.1; !1PID:g560645 GENETICS !$#gene Aldh2; Ahd5; Ahd-5 !$#introns 40/3; 75/3; 122/3; 149/2; 186/3; 229/3; 267/3; 302/1; 363/3; !1418/3; 471/2; 509/3 COMPLEX homotetramer FUNCTION !$#description catalyzes the oxidation of an aldehyde to an acid using NAD+ !1and water !$#pathway ethanol catabolism !$#note enzymes with this activity are involved in diverse metabolic !1pathways in various organisms and tissues CLASSIFICATION #superfamily aldehyde dehydrogenase (NAD+); aldehyde !1dehydrogenase homology KEYWORDS alcohol metabolism; homotetramer; liver; mitochondrion; NAD; !1oxidoreductase FEATURE !$1-19 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$20-519 #product aldehyde dehydrogenase (NAD+) 2 #status !8predicted #label MAT\ !$77-341 #domain aldehyde dehydrogenase homology #label ALDD\ !$287,321 #active_site Glu, Cys #status predicted\ !$474 #binding_site NAD (Cys) #status predicted SUMMARY #length 519 #molecular-weight 56537 #checksum 921 SEQUENCE /// ENTRY S09030 #type complete TITLE aldehyde dehydrogenase (NAD) (EC 1.2.1.3) 2 precursor, mitochondrial - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Jun-1992 #sequence_revision 31-Jan-1997 #text_change 03-Jun-2002 ACCESSIONS S09030; S03565; PQ0543 REFERENCE S09030 !$#authors Guan, K.; Weiner, H. !$#journal Arch. Biochem. Biophys. (1990) 277:351-360 !$#title Sequence of the precursor of bovine liver mitochondrial !1aldehyde dehydrogenase as determined from its cDNA, its !1gene, and its functionality. !$#cross-references MUID:90179198; PMID:1689984 !$#accession S09030 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-520 ##label GUA REFERENCE S03564 !$#authors Farres, J.; Guan, K.L.; Weiner, H. !$#journal Eur. J. Biochem. (1989) 180:67-74 !$#title Primary structures of rat and bovine liver mitochondrial !1aldehyde dehydrogenases deduced from cDNA sequences. !$#cross-references MUID:89210865; PMID:2540003 !$#accession S03565 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 92-520 ##label FAR !'##experimental_source liver REFERENCE PQ0543 !$#authors Lee, J.E.; Cho, Y.D. !$#journal Biochem. Biophys. Res. Commun. (1992) 189:450-454 !$#title Purification and characterization of bovine brain !1gamma-aminobutyraldehyde dehydrogenase. !$#cross-references MUID:93080596; PMID:1449496 !$#accession PQ0543 !'##molecule_type protein !'##residues 22-34 ##label LEE !'##experimental_source brain COMMENT This enzyme may be responsible for gamma-aminobutyraldehyde !1dehydrogenase activity in the brain. COMPLEX homotetramer FUNCTION !$#description catalyzes the oxidation of an aldehyde to an acid using NAD+ !1and water !$#pathway ethanol catabolism !$#note enzymes with this activity are involved in diverse metabolic !1pathways in various organisms and tissues CLASSIFICATION #superfamily aldehyde dehydrogenase (NAD+); aldehyde !1dehydrogenase homology KEYWORDS alcohol metabolism; homotetramer; liver; mitochondrion; NAD; !1oxidoreductase FEATURE !$1-21 #domain transit peptide (mitochondrion) #status !8predicted #label SIG\ !$22-520 #product aldehyde dehydrogenase (NAD+) 2 #status !8predicted #label MAT\ !$78-342 #domain aldehyde dehydrogenase homology #label ALDD\ !$288,322 #active_site Glu, Cys #status predicted\ !$475 #binding_site NAD (Cys) #status predicted SUMMARY #length 520 #molecular-weight 56708 #checksum 1211 SEQUENCE /// ENTRY A40872 #type complete TITLE aldehyde dehydrogenase (NAD) (EC 1.2.1.3) 5 precursor, mitochondrial - human ORGANISM #formal_name Homo sapiens #common_name man DATE 27-Mar-1992 #sequence_revision 31-Jan-1997 #text_change 03-Jun-2002 ACCESSIONS A40872 REFERENCE A40872 !$#authors Hsu, L.C.; Chang, W.C. !$#journal J. Biol. Chem. (1991) 266:12257-12265 !$#title Cloning and characterization of a new functional human !1aldehyde dehydrogenase gene. !$#cross-references MUID:91286241; PMID:2061311 !$#accession A40872 !'##molecule_type DNA; mRNA !'##residues 1-517 ##label HSU !'##cross-references GB:M63967; NID:g337184; PIDN:AAA96830.1; !1PID:g1263008 !'##note 86-Ala and 107-Leu were also found COMMENT Based on similarity, this form is assumed to be !1mitochondrial and to have properties similar to the major !1mitochondrial form. It is expressed at low levels in liver, !1testis, and brain. GENETICS !$#gene GDB:ALDH5; ALDHX !'##cross-references GDB:128788 !$#map_position 9p13-9p13 !$#note the only intron occurs before the initiator codon COMPLEX homotetramer (probably) FUNCTION !$#description catalyzes oxidation of an aldehyde to an acid using NAD+ and !1water !$#pathway ethanol catabolism !$#note enzymes with this activity are involved in diverse metabolic !1pathways in various organisms and tissues CLASSIFICATION #superfamily aldehyde dehydrogenase (NAD+); aldehyde !1dehydrogenase homology KEYWORDS alcohol metabolism; homotetramer; liver; mitochondrion; NAD; !1oxidoreductase FEATURE !$1-20 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$21-517 #product aldehyde dehydrogenase (NAD+) 5 #status !8predicted #label MAT\ !$75-339 #domain aldehyde dehydrogenase homology #label ALDD\ !$285,319 #active_site Glu, Cys #status predicted SUMMARY #length 517 #molecular-weight 57309 #checksum 6757 SEQUENCE /// ENTRY S31308 #type complete TITLE aldehyde dehydrogenase (NAD) (EC 1.2.1.3) 2 precursor, mitochondrial - yeast (Saccharomyces cerevisiae) ORGANISM #formal_name Saccharomyces cerevisiae DATE 28-May-1993 #sequence_revision 31-Jan-1997 #text_change 03-Jun-2002 ACCESSIONS S31308 REFERENCE S31308 !$#authors Thielen, J. !$#submission submitted to the EMBL Data Library, October 1992 !$#accession S31308 !'##molecule_type DNA !'##residues 1-511 ##label THI !'##cross-references EMBL:Z17314; NID:g3361; PIDN:CAA78962.1; PID:g3362 COMMENT This form is probably mitochondrial. GENETICS !$#gene ALD2 FUNCTION !$#description catalyzes the oxidation of an aldehyde to an acid using NAD+ !1and water !$#note enzymes with this activity are involved in diverse metabolic !1pathways in various organisms and tissues CLASSIFICATION #superfamily aldehyde dehydrogenase (NAD+); aldehyde !1dehydrogenase homology KEYWORDS alcohol metabolism; mitochondrion; NAD; oxidoreductase FEATURE !$1-21 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$22-511 #product aldehyde dehydrogenase (NAD+) 2 #status !8predicted #label MAT\ !$80-351 #domain aldehyde dehydrogenase homology #label ALDD\ !$297,331 #active_site Glu, Cys #status predicted\ !$483 #binding_site NAD (Cys) #status predicted SUMMARY #length 511 #molecular-weight 56466 #checksum 6761 SEQUENCE /// ENTRY A29055 #type complete TITLE aldehyde dehydrogenase (NAD) (EC 1.2.1.3) - Emericella nidulans ORGANISM #formal_name Emericella nidulans, Aspergillus nidulans DATE 30-Jun-1988 #sequence_revision 31-Jan-1997 #text_change 03-Jun-2002 ACCESSIONS A29055 REFERENCE A29055 !$#authors Pickett, M.; Gwynne, D.I.; Buxton, F.P.; Elliott, R.; !1Davies, R.W.; Lockington, R.A.; Scazzocchio, C.; !1Sealy-Lewis, H.M. !$#journal Gene (1987) 51:217-226 !$#title Cloning and characterization of the aldA gene of Aspergillus !1nidulans. !$#cross-references MUID:87248080; PMID:3036652 !$#accession A29055 !'##molecule_type DNA !'##residues 1-497 ##label PIC !'##cross-references GB:M16197; NID:g168010; PIDN:AAA33293.1; !1PID:g168011 !'##experimental_source strain Glasgow FGSC4 GENETICS !$#gene aldA !$#map_position VIII !$#introns 21/2; 422/1 FUNCTION !$#description catalyzes the oxidation of an aldehyde to an acid using NAD+ !1and water !$#pathway ethanol catabolism !$#note enzymes with this activity are involved in diverse metabolic !1pathways in various organisms and tissues CLASSIFICATION #superfamily aldehyde dehydrogenase (NAD+); aldehyde !1dehydrogenase homology KEYWORDS alcohol metabolism; NAD; oxidoreductase FEATURE !$57-318 #domain aldehyde dehydrogenase homology #label ALDD\ !$264,298 #active_site Glu, Cys #status predicted SUMMARY #length 497 #molecular-weight 54088 #checksum 6330 SEQUENCE /// ENTRY A46725 #type complete TITLE omega-crystallin - giant octopus ORGANISM #formal_name Octopus dofleini #common_name giant octopus DATE 21-Sep-1993 #sequence_revision 31-Jan-1997 #text_change 11-Jun-1999 ACCESSIONS A46725; E41681 REFERENCE A46725 !$#authors Zinovieva, R.D.; Tomarev, S.I.; Piatigorsky, J. !$#journal J. Biol. Chem. (1993) 268:11449-11455 !$#title Aldehyde dehydrogenase-derived omega-crystallins of squid !1and octopus. Specialization for lens expression. !$#cross-references MUID:93266606; PMID:7684383 !$#accession A46725 !'##molecule_type mRNA !'##residues 1-496 ##label ZIN !'##cross-references GB:L06902; NID:g159742; PIDN:AAA29392.1; !1PID:g159743 !'##experimental_source adult eye lens !'##note sequence extracted from NCBI backbone (NCBIN:132862, !1NCBIP:132863) and corrected to add Met-1 REFERENCE A41681 !$#authors Tomarev, S.I.; Zinovieva, R.D.; Piatigorsky, J. !$#journal J. Biol. Chem. (1991) 266:24226-24231 !$#title Crystallins of the octopus lens. Recruitment from !1detoxification enzymes. !$#cross-references MUID:92084735; PMID:1721068 !$#accession E41681 !'##molecule_type protein !'##residues 94-111;'I',304-315;326-345;373-381,'I',383-390;391-399,'X', !1401 ##label TOM COMPLEX homotetramer FUNCTION !$#description crystallins are soluble proteins of the lens responsible for !1its refractive properties !$#note enzymatically inactive CLASSIFICATION #superfamily aldehyde dehydrogenase (NAD+); aldehyde !1dehydrogenase homology KEYWORDS eye lens; homotetramer FEATURE !$54-317 #domain aldehyde dehydrogenase homology #label ALDD SUMMARY #length 496 #molecular-weight 55493 #checksum 1657 SEQUENCE /// ENTRY S43184 #type complete TITLE aldehyde dehydrogenase (NAD) (EC 1.2.1.3) precursor, mitochondrial - Leishmania tarentolae ORGANISM #formal_name Leishmania tarentolae DATE 06-Feb-1995 #sequence_revision 31-Jan-1997 #text_change 03-Jun-2002 ACCESSIONS S43184 REFERENCE S43177 !$#authors Bringaud, F.; Freedland, S.; Liu, X.; Peris, M.; Turck, C.; !1Simpson, L. !$#submission submitted to the EMBL Data Library, March 1994 !$#description Identification of several proteins in mitochondrial !1nucleoprotein T-complexes in Leshmania tarentolae. !$#accession S43184 !'##molecule_type DNA !'##residues 1-498 ##label BRI !'##cross-references EMBL:Z31698; NID:g469149; PIDN:CAA83503.1; !1PID:g469150 !'##experimental_source strain UC FUNCTION !$#description catalyzes the oxidation of an aldehyde to an acid using NAD+ !1and water !$#note enzymes with this activity are involved in diverse metabolic !1pathways in various organisms and tissues CLASSIFICATION #superfamily aldehyde dehydrogenase (NAD+); aldehyde !1dehydrogenase homology KEYWORDS alcohol metabolism; mitochondrion; NAD; oxidoreductase FEATURE !$1-17 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$18-498 #product aldehyde dehydrogenase (NAD+), mitochondrial !8#status predicted #label MAT\ !$58-319 #domain aldehyde dehydrogenase homology #label ALDD\ !$265,299 #active_site Glu, Cys #status predicted SUMMARY #length 498 #molecular-weight 54251 #checksum 8272 SEQUENCE /// ENTRY S54527 #type complete TITLE aldehyde dehydrogenase (NAD) (EC 1.2.1.3) 3 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES ALD3 protein; protein YM8520.18c; protein YMR169c ORGANISM #formal_name Saccharomyces cerevisiae DATE 08-Jul-1995 #sequence_revision 31-Jan-1997 #text_change 03-Jun-2002 ACCESSIONS S54527; S54614 REFERENCE S54510 !$#authors Hunt, S.; Bowman, S. !$#submission submitted to the EMBL Data Library, May 1995 !$#accession S54527 !'##molecule_type DNA !'##residues 1-506 ##label HUN !'##cross-references EMBL:Z49705; NID:g825556; PIDN:CAA89805.1; !1PID:g825574; GSPDB:GN00013; MIPS:YMR169c !'##experimental_source strain AB972 GENETICS !$#gene SGD:ALD3; MIPS:YMR169c !'##cross-references SGD:S0004779; MIPS:YMR169c !$#map_position 13R FUNCTION !$#description catalyzes oxidation of an aldehyde to an acid using NAD+ and !1water !$#note enzymes with this activity are involved in diverse metabolic !1pathways in various organisms and tissues CLASSIFICATION #superfamily aldehyde dehydrogenase (NAD+); aldehyde !1dehydrogenase homology KEYWORDS NAD; oxidoreductase FEATURE !$59-322 #domain aldehyde dehydrogenase homology #label ALDD\ !$268,302 #active_site Glu, Cys #status predicted SUMMARY #length 506 #molecular-weight 55385 #checksum 6877 SEQUENCE /// ENTRY S54615 #type complete TITLE aldehyde dehydrogenase [NAD(P)] (EC 1.2.1.5) 2 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YM8520.19c; protein YMR170c ORGANISM #formal_name Saccharomyces cerevisiae DATE 08-Jul-1995 #sequence_revision 17-Apr-1998 #text_change 03-Jun-2002 ACCESSIONS S70189; S54615; S52786; S54528 REFERENCE S70188 !$#authors Miralles, V.J.; Serrano, R. !$#journal Mol. Microbiol. (1995) 17:653-662 !$#title A genomic locus in Saccharomyces cerevisiae with four genes !1up-regulated by osmotic stress. !$#cross-references MUID:96111486; PMID:8801420 !$#accession S70189 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-506 ##label MIR !'##cross-references EMBL:X85987; NID:g758647; PIDN:CAA59975.1; !1PID:g758648 !'##experimental_source strain DBY939 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1March 1995 REFERENCE S54510 !$#authors Hunt, S.; Bowman, S. !$#submission submitted to the EMBL Data Library, May 1995 !$#accession S54615 !'##molecule_type DNA !'##residues 1-22,'L',24-461,'S',463-485,'QSG',489-496,'A',498-499,'IN', !1502-506 ##label HUN !'##cross-references EMBL:Z49705; NID:g825556; PIDN:CAA89806.1; !1PID:g825575; GSPDB:GN00013; MIPS:YMR170c !'##experimental_source strain AB972 REFERENCE S52786 !$#authors Mirales, V.J.; Serrano, R. !$#submission submitted to the EMBL Data Library, March 1995 !$#description A genomic locus in Saccharomyces cerevisiae with four genes !1up regulated by osmotic stress. !$#accession S52786 !'##molecule_type DNA !'##residues 1-506 ##label MIW !'##cross-references EMBL:X85987; NID:g758647; PIDN:CAA59975.1; !1PID:g758648 !'##experimental_source strain DBY939 GENETICS !$#gene SGD:ALD2; MIPS:YMR170c !'##cross-references SGD:L0002991 !$#map_position 13R FUNCTION !$#description catalyzes oxidation of an aldehyde to an acid using NAD(P)+ !1and water CLASSIFICATION #superfamily aldehyde dehydrogenase (NAD+); aldehyde !1dehydrogenase homology KEYWORDS NAD; NADP; oxidoreductase FEATURE !$59-322 #domain aldehyde dehydrogenase homology #label ALDD\ !$268,302 #active_site Glu, Cys #status predicted SUMMARY #length 506 #molecular-weight 55310 #checksum 8353 SEQUENCE /// ENTRY S60929 #type complete TITLE probable aldehyde dehydrogenase (NAD) (EC 1.2.1.3) YPL061w - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein LPE9w ORGANISM #formal_name Saccharomyces cerevisiae DATE 15-Feb-1996 #sequence_revision 31-Jan-1997 #text_change 03-Jun-2002 ACCESSIONS S60929 REFERENCE S60921 !$#authors Winnett, E.; Ahmed, A.; Bussey, H.; Fortin, N.; Friesen, !1J.D.; Hall, J.; Storms, R.K.; Vo, D.H.; Wang, Y. !$#submission submitted to the EMBL Data Library, October 1995 !$#accession S60929 !'##molecule_type DNA !'##residues 1-500 ##label WIN !'##cross-references EMBL:U39205; NID:g1079672; PIDN:AAB68304.1; !1PID:g1079681; GSPDB:GN00016; MIPS:YPL061w GENETICS !$#gene SGD:ALD6; MIPS:YPL061w !'##cross-references SGD:S0005982; MIPS:YPL061w !$#map_position 16L FUNCTION !$#description catalyzes oxidation of an aldehyde to an acid using NAD+ and !1water !$#note enzymes with this activity are involved in diverse metabolic !1pathways in various organisms and tissues CLASSIFICATION #superfamily aldehyde dehydrogenase (NAD+); aldehyde !1dehydrogenase homology KEYWORDS NAD; oxidoreductase FEATURE !$64-326 #domain aldehyde dehydrogenase homology #label ALDD\ !$272,306 #active_site Glu, Cys #status predicted SUMMARY #length 500 #molecular-weight 54414 #checksum 6847 SEQUENCE /// ENTRY S67286 #type complete TITLE probable aldehyde dehydrogenase (NAD) (EC 1.2.1.3) YOR374w - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein O6730 ORGANISM #formal_name Saccharomyces cerevisiae DATE 12-Jul-1996 #sequence_revision 31-Jan-1997 #text_change 03-Jun-2002 ACCESSIONS S67286 REFERENCE S67261 !$#authors Delius, H.; Hebling, U.; Hofmann, B. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67286 !'##molecule_type DNA !'##residues 1-519 ##label DEL !'##cross-references EMBL:Z75282; PIDN:CAA99705.1; GSPDB:GN00015; !1MIPS:YOR374w !'##experimental_source strain S288C GENETICS !$#gene SGD:ALD7; MIPS:YOR374w !'##cross-references SGD:S0005901; MIPS:YOR374w !$#map_position 15R FUNCTION !$#description catalyzes oxidation of an aldehyde to an acid using NAD+ and !1water !$#note enzymes with this activity are involved in diverse metabolic !1pathways in various organisms and tissues CLASSIFICATION #superfamily aldehyde dehydrogenase (NAD+); aldehyde !1dehydrogenase homology KEYWORDS NAD; oxidoreductase FEATURE !$83-344 #domain aldehyde dehydrogenase homology #label ALDD\ !$290,324 #active_site Glu, Cys #status predicted SUMMARY #length 519 #molecular-weight 56723 #checksum 2650 SEQUENCE /// ENTRY S50576 #type complete TITLE probable aldehyde dehydrogenase (NAD) (EC 1.2.1.3) YER073w - yeast (Saccharomyces cerevisiae) ORGANISM #formal_name Saccharomyces cerevisiae DATE 28-May-1993 #sequence_revision 31-Jan-1997 #text_change 03-Jun-2002 ACCESSIONS S50576 REFERENCE S50438 !$#authors Dietrich, F.S. !$#submission submitted to the EMBL Data Library, December 1994 !$#description The sequence of S. cerevisiae lambda clone 3612 and cosmid !19747. !$#accession S50576 !'##molecule_type DNA !'##residues 1-520 ##label DIE !'##cross-references EMBL:U18814; NID:g603309; PIDN:AAB64612.1; !1PID:g603310; GSPDB:GN00005; MIPS:YER073w !'##experimental_source strain S288C (AB972) GENETICS !$#gene SGD:ALD5; MIPS:YER073w !'##cross-references SGD:S0000875 !$#map_position 5R FUNCTION !$#description catalyzes oxidation of an aldehyde to an acid using NAD+ and !1water !$#note enzymes with this activity are involved in diverse metabolic !1pathways in various organisms and tissues CLASSIFICATION #superfamily aldehyde dehydrogenase (NAD+); aldehyde !1dehydrogenase homology KEYWORDS alcohol metabolism; NAD; oxidoreductase FEATURE !$82-342 #domain aldehyde dehydrogenase homology #label ALDD\ !$288,322 #active_site Glu, Cys #status predicted SUMMARY #length 520 #molecular-weight 56620 #checksum 3417 SEQUENCE /// ENTRY S19135 #type complete TITLE betaine-aldehyde dehydrogenase (EC 1.2.1.8) precursor - beet ALTERNATE_NAMES betB protein ORGANISM #formal_name Beta vulgaris #common_name beet DATE 22-Nov-1993 #sequence_revision 31-Jan-1997 #text_change 11-Jun-1999 ACCESSIONS S19135; S19136 REFERENCE S19135 !$#authors McCue, K.F.; Hanson, A.D. !$#journal Plant Mol. Biol. (1992) 18:1-11 !$#title Salt-inducible betaine aldehyde dehydrogenase from sugar !1beet: cDNA cloning and expression. !$#cross-references MUID:92119215; PMID:1731961 !$#accession S19135 !'##molecule_type mRNA !'##residues 1-500 ##label MCC !'##cross-references EMBL:X58463; NID:g17933; PIDN:CAA41377.1; !1PID:g17934 !$#accession S19136 !'##molecule_type mRNA !'##residues 1-411,'D',413-500 ##label MC2 !'##cross-references EMBL:X58462; NID:g17935; PIDN:CAA41376.1; !1PID:g17936 GENETICS !$#genome nuclear COMPLEX homodimer FUNCTION !$#description catalyzes the oxidation of betaine aldehyde to betaine using !1NAD+ and water !$#pathway betaine biosynthesis !$#note betaine is a protective osmolyte induced to accumulate under !1saline or dry conditions CLASSIFICATION #superfamily aldehyde dehydrogenase (NAD+); aldehyde !1dehydrogenase homology KEYWORDS blocked amino end; chloroplast; NAD; oxidoreductase; !1stress-induced protein FEATURE !$1-7 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$8-500 #product betaine-aldehyde dehydrogenase #status !8predicted #label MAT\ !$46-314 #domain aldehyde dehydrogenase homology #label ALDD\ !$8 #modified_site blocked amino end (Arg) (in mature !8form) #status predicted\ !$260,294 #active_site Glu, Cys #status predicted\ !$449 #binding_site NAD (Cys) #status predicted SUMMARY #length 500 #molecular-weight 54720 #checksum 8795 SEQUENCE /// ENTRY A35994 #type complete TITLE betaine-aldehyde dehydrogenase (EC 1.2.1.8) precursor - spinach ALTERNATE_NAMES betB protein ORGANISM #formal_name Spinacia oleracea #common_name spinach DATE 16-Nov-1990 #sequence_revision 31-Jan-1997 #text_change 11-Jun-1999 ACCESSIONS A35994; A58459 REFERENCE A35994 !$#authors Weretilnyk, E.A.; Hanson, A.D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:2745-2749 !$#title Molecular cloning of a plant betaine-aldehyde dehydrogenase, !1an enzyme implicated in adaptation to salinity and drought. !$#cross-references MUID:90207274; PMID:2320587 !$#accession A35994 !'##molecule_type mRNA !'##residues 1-497 ##label WER !'##cross-references GB:M31480; NID:g170099; PIDN:AAA34025.1; !1PID:g170100 !'##experimental_source cv. Savoy hybrid 612, leaves of salt-stressed !1mature plants !'##note parts of this sequence, including residues 9-15, were !1determined by protein sequencing; the amino end is blocked REFERENCE A58459 !$#authors Ma, D.; Lue, W.; Tang, L.; Luo, A.; Liang, Z. !$#journal Chinese J. Biotechnol. (1996) 12:65-70 !$#title A cDNA cloning and sequence encoding betaine aldehyde !1dehydrogenase (BADH) from spinach. !$#accession A58459 !'##molecule_type mRNA !'##residues 1-180,'R',182-276,'G',278-497 ##label MAA GENETICS !$#genome nuclear COMPLEX homodimer FUNCTION !$#description catalyzes the oxidation of betaine aldehyde to betaine using !1NAD+ and water !$#pathway betaine biosynthesis !$#note betaine is a protective osmolyte induced to accumulate under !1saline or dry conditions CLASSIFICATION #superfamily aldehyde dehydrogenase (NAD+); aldehyde !1dehydrogenase homology KEYWORDS blocked amino end; chloroplast; NAD; oxidoreductase; !1stress-induced protein FEATURE !$1-7 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$8-497 #product betaine-aldehyde dehydrogenase #status !8predicted #label MAT\ !$46-311 #domain aldehyde dehydrogenase homology #label ALDD\ !$8 #modified_site blocked amino end (Arg) (in mature !8form) #status predicted\ !$257,291 #active_site Glu, Cys #status predicted\ !$446 #binding_site NAD (Cys) #status predicted SUMMARY #length 497 #molecular-weight 54270 #checksum 939 SEQUENCE /// ENTRY S49205 #type complete TITLE betaine-aldehyde dehydrogenase (EC 1.2.1.8) precursor - Atriplex hortensis ALTERNATE_NAMES BADH; betB protein ORGANISM #formal_name Atriplex hortensis DATE 16-Feb-1995 #sequence_revision 31-Jan-1997 #text_change 11-Jun-1999 ACCESSIONS S49205 REFERENCE S49205 !$#authors Xiao, G.; Zhang, G.; Liu, F.; Chen, S. !$#submission submitted to the EMBL Data Library, December 1992 !$#description cDNA and partial genomic DNA sequence of mountain spinach !1(Atriplex hortenis) betaine aldehyde dehydrogenase (BADH). !$#accession S49205 !'##molecule_type mRNA !'##residues 1-502 ##label XIA !'##cross-references EMBL:X69770; NID:g510573; PIDN:CAA49425.1; !1PID:g510574 GENETICS !$#genome nuclear COMPLEX homodimer FUNCTION !$#description catalyzes the oxidation of betaine aldehyde to betaine using !1NAD+ and water !$#pathway betaine biosynthesis !$#note betaine is a protective osmolyte induced to accumulate under !1saline or dry conditions CLASSIFICATION #superfamily aldehyde dehydrogenase (NAD+); aldehyde !1dehydrogenase homology KEYWORDS blocked amino end; chloroplast; NAD; oxidoreductase; !1stress-induced protein FEATURE !$1-7 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$8-502 #product betaine-aldehyde dehydrogenase #status !8predicted #label MAT\ !$46-316 #domain aldehyde dehydrogenase homology #label ALDD\ !$8 #modified_site blocked amino end (Arg) (in mature !8form) #status predicted\ !$262,296 #active_site Glu, Cys #status predicted\ !$451 #binding_site NAD (Cys) #status predicted SUMMARY #length 502 #molecular-weight 55270 #checksum 4071 SEQUENCE /// ENTRY S71413 #type complete TITLE betaine-aldehyde dehydrogenase (EC 1.2.1.8) precursor - barley ALTERNATE_NAMES BADH; betB protein ORGANISM #formal_name Hordeum vulgare #common_name barley DATE 20-Jul-1996 #sequence_revision 31-Jan-1997 #text_change 11-Jun-1999 ACCESSIONS S71413; S53009 REFERENCE S71413 !$#authors Ishitani, M.; Nakamura, T.; Han, S.Y.; Takabe, T. !$#submission submitted to the EMBL Data Library, January 1994 !$#description Expression of the betaine aldehyde dehydrogenase gene in !1barley in response to osmotic stress and abscisic acid. !$#accession S71413 !'##molecule_type mRNA !'##residues 1-505 ##label ISH !'##cross-references EMBL:D26448; NID:g927642; PIDN:BAA05466.1; !1PID:g927643 REFERENCE S53009 !$#authors Ishitani, M.; Nakamura, T.; Han, S.Y.; Takabe, T. !$#journal Plant Mol. Biol. (1995) 27:307-315 !$#title Expression of the betaine aldehyde dehydrogenase gene in !1barley in response to osmotic stress and abscisic acid. !$#cross-references MUID:95195158; PMID:7888620 !$#accession S53009 !'##molecule_type mRNA !'##residues 216-307 ##label ISW !'##cross-references EMBL:D26448; NID:g927642 GENETICS !$#genome nuclear COMPLEX homodimer FUNCTION !$#description catalyzes the oxidation of betaine aldehyde to betaine using !1NAD+ and water !$#pathway betaine biosynthesis !$#note betaine is a protective osmolyte induced to accumulate under !1saline or dry conditions CLASSIFICATION #superfamily aldehyde dehydrogenase (NAD+); aldehyde !1dehydrogenase homology KEYWORDS chloroplast; NAD; oxidoreductase; stress-induced protein FEATURE !$1-9 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$10-502 #product betaine-aldehyde dehydrogenase #status !8predicted #label MAT\ !$48-316 #domain aldehyde dehydrogenase homology #label ALDD\ !$261,296 #active_site Glu, Cys #status predicted\ !$451 #binding_site NAD (Cys) #status predicted SUMMARY #length 505 #molecular-weight 54289 #checksum 1677 SEQUENCE /// ENTRY S15181 #type complete TITLE betaine-aldehyde dehydrogenase (EC 1.2.1.8) - Escherichia coli (strain K-12) ALTERNATE_NAMES betB protein ORGANISM #formal_name Escherichia coli DATE 09-Oct-1992 #sequence_revision 31-Jan-1997 #text_change 01-Mar-2002 ACCESSIONS S15181; JQ1230; H64757; S10900 REFERENCE S15178 !$#authors Lamark, T.; Kaasen, I.; Eshoo, M.W.; Falkenberg, P.; !1McDougall, J.; Strom, A.R. !$#journal Mol. Microbiol. (1991) 5:1049-1064 !$#title DNA sequence and analysis of the bet genes encoding the !1osmoregulatory choline-glycine betaine pathway of !1Escherichia coli. !$#cross-references MUID:92065800; PMID:1956285 !$#accession S15181 !'##molecule_type DNA !'##residues 1-490 ##label LAM !'##cross-references EMBL:X52905; NID:g48714; PIDN:CAA37092.1; !1PID:g48718 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE JQ1230 !$#authors Boyd, L.A.; Adam, L.; Pelcher, L.E.; McHughen, A.; Hirji, !1R.; Selvaraj, G. !$#journal Gene (1991) 103:45-52 !$#title Characterization of an Escherichia coli gene encoding !1betaine aldehyde dehydrogenase (BADH): structural similarity !1to mammalian ALDHs and a plant BADH. !$#cross-references MUID:91348527; PMID:1879697 !$#accession JQ1230 !'##molecule_type DNA !'##residues 'M',1-231,'R',233-311,'P',313-490 ##label BOY !'##cross-references GB:M77739; NID:g145403; PIDN:AAA23505.1; !1PID:g145404 !'##experimental_source strain K-12 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64757 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-490 ##label BLAT !'##cross-references GB:AE000138; GB:U00096; NID:g1786501; !1PIDN:AAC73415.1; PID:g1786504; UWGP:b0312 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene betB !$#map_position 7.5 min COMPLEX homotetramer FUNCTION !$#description catalyzes the oxidation of betaine aldehyde to betaine using !1NAD+ and water !$#pathway betaine biosynthesis !$#note betaine is a protective osmolyte induced to accumulate by !1osmotic stress CLASSIFICATION #superfamily aldehyde dehydrogenase (NAD+); aldehyde !1dehydrogenase homology KEYWORDS alternative initiators; homotetramer; NAD; oxidoreductase; !1stress-induced protein FEATURE !$2-490 #product betaine-aldehyde dehydrogenase #status !8experimental #label MAT\ !$45-306 #domain aldehyde dehydrogenase homology #label ALDD\ !$252,286 #active_site Glu, Cys #status predicted SUMMARY #length 490 #molecular-weight 52911 #checksum 8214 SEQUENCE /// ENTRY S39532 #type complete TITLE aldehyde dehydrogenase (NAD) (EC 1.2.1.3) 7, cytosolic - human ALTERNATE_NAMES aldehyde dehydrogenase E3; aldehyde dehydrogenase E3'; r-aminobutyraldehyde dehydrogenase CONTAINS aminobutyraldehyde dehydrogenase (EC 1.2.1.19) ORGANISM #formal_name Homo sapiens #common_name man DATE 26-Jul-1996 #sequence_revision 10-Jul-1998 #text_change 03-Jun-2002 ACCESSIONS G02054; S71133; S77918; S39532; S39538 REFERENCE G09132 !$#authors Chen, J.C. !$#submission submitted to the EMBL Data Library, August 1995 !$#accession G02054 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-493 ##label CHE !'##cross-references EMBL:U34252; NID:g1049218; PIDN:AAB18827.1; !1PID:g1049219 REFERENCE S71133 !$#authors Kikonyogo, A.; Pietruszko, R. !$#journal Biochem. J. (1996) 316:317-324 !$#title Aldehyde dehydrogenase from adult human brain that !1dehydrogenates gamma-aminobutyraldehyde: purification, !1characterization, cloning and distribution. !$#cross-references MUID:96235208; PMID:8645224 !$#accession S71133 !'##molecule_type mRNA !'##residues 28-493 ##label KIK1 !'##cross-references EMBL:U50203; NID:g1354221; PIDN:AAB06721.1; !1PID:g1354222 !'##experimental_source brain !'##note the authors translated the codon TTC for residue 42 as Gly, TCA !1for residue 462 as Phe, and GAG for residue 467 as Ala !'##note in the authors' translation residues 232-237 do not match the !1nucleotide sequence !$#accession S77918 !'##molecule_type protein !'##residues 258-273;352-365;411-425;433-449,'X',451-452 ##label KIK2 !'##experimental_source brain REFERENCE S39532 !$#authors Kurys, G.; Shah, P.C.; Kikonyogo, A.; Reed, D.; Ambroziak, !1W.; Pietruszko, R. !$#journal Eur. J. Biochem. (1993) 218:311-320 !$#title Human aldehyde dehydrogenase. cDNA cloning and primary !1structure of the enzyme that catalyzes dehydrogenation of !14-aminobutyraldehyde. !$#cross-references MUID:94094820; PMID:8269919 !$#accession S39532 !'##molecule_type mRNA !'##residues 32-114,'S',116-170,'R',172-493 ##label KUR !'##cross-references EMBL:X75425; NID:g435486; PIDN:CAA53176.1; !1PID:g435487 !'##experimental_source liver !'##note the authors translated the codon CGG for residue 171 as Ala !$#accession S39538 !'##molecule_type protein !'##residues 107-114,'S',116-125,'X',127;144-148,'Q',150-157;'W', !1159-160,207-218;246-266;298-308;367-380;433-448;471-492 !1##label KUW !'##experimental_source liver !'##note 93-Thr and 156-Leu were also found GENETICS !$#gene GDB:ALDH7; ALDH4; E3 !'##cross-references GDB:309335; OMIM:600466 !$#map_position 1pter-1qter COMPLEX homotetramer FUNCTION !$#description catalyzes the oxidation of an aldehyde to an acid using NAD+ !1and water; this form is much more active on !1gamma-aminobutanal than are the major liver isozymes (ALDH1 !1and ALDH2) !$#note enzymes with this activity are involved in diverse metabolic !1pathways in various organisms and tissues CLASSIFICATION #superfamily aldehyde dehydrogenase (NAD+); aldehyde !1dehydrogenase homology KEYWORDS alcohol metabolism; blocked amino end; brain; cytosol; !1homotetramer; liver; NAD; oxidoreductase FEATURE !$49-307 #domain aldehyde dehydrogenase homology #label ALDD\ !$253,287 #active_site Glu, Cys #status predicted SUMMARY #length 493 #molecular-weight 53532 #checksum 4138 SEQUENCE /// ENTRY A42597 #type complete TITLE aldehyde dehydrogenase (NAD) (EC 1.2.1.3) [validated] - Alcaligenes eutrophus ALTERNATE_NAMES acetaldehyde dehydrogenase II ORGANISM #formal_name Alcaligenes eutrophus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS A42597 REFERENCE A42597 !$#authors Priefert, H.; Kruger, N.; Jendrossek, D.; Schmidt, B.; !1Steinbuchel, A. !$#journal J. Bacteriol. (1992) 174:899-907 !$#title Identification and molecular characterization of the gene !1coding for acetaldehyde dehydrogenase II (acoD) of !1Alcaligenes eutrophus. !$#cross-references MUID:92121129; PMID:1732222 !$#accession A42597 !'##status preliminary !'##molecule_type DNA !'##residues 1-506 ##label PRI !'##cross-references GB:M74003; NID:g141885; PIDN:AAA21943.1; !1PID:g141886 !'##experimental_source strain TF93 !'##note sequence extracted from NCBI backbone (NCBIP:77618) GENETICS !$#gene acoD CLASSIFICATION #superfamily aldehyde dehydrogenase (NAD+); aldehyde !1dehydrogenase homology KEYWORDS NAD; oxidoreductase FEATURE !$57-321 #domain aldehyde dehydrogenase homology #label ALDD\ !$262,301 #active_site Glu, Cys #status predicted\ !$458 #binding_site NAD (Cys) #status predicted SUMMARY #length 506 #molecular-weight 54881 #checksum 5848 SEQUENCE /// ENTRY S47809 #type complete TITLE aldehyde dehydrogenase (NAD) (EC 1.2.1.3) aldB [similarity] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S47809; B57259; F65158 REFERENCE S47666 !$#authors Plunkett, G. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S47809 !'##status preliminary !'##molecule_type DNA !'##residues 1-542 ##label PLU !'##cross-references EMBL:U00039; NID:g466582; PIDN:AAB18565.1; !1PID:g912476 REFERENCE A57259 !$#authors Xu, J.; Johnson, R.C. !$#journal J. Bacteriol. (1995) 177:3166-3175 !$#title aldB, an RpoS-dependent gene in Escherichia coli encoding an !1aldehyde dehydrogenase that is repressed by Fis and !1activated by Crp. !$#cross-references MUID:95286498; PMID:7768815 !$#accession B57259 !'##status preliminary !'##molecule_type DNA !'##residues 31-542 ##label XUA !'##cross-references GB:L40742; NID:g712824; PIDN:AAC36939.1; !1PID:g712825 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65158 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-542 ##label BLAT !'##cross-references GB:AE000436; GB:U00096; NID:g2367246; !1PIDN:AAC76612.1; PID:g1790014; UWGP:b3588 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene aldB !$#start_codon GTG CLASSIFICATION #superfamily aldehyde dehydrogenase (NAD+); aldehyde !1dehydrogenase homology KEYWORDS NAD; oxidoreductase FEATURE !$93-357 #domain aldehyde dehydrogenase homology #label ALDD\ !$298,337 #active_site Glu, Cys #status predicted\ !$494 #binding_site NAD (Cys) #status predicted SUMMARY #length 542 #molecular-weight 59695 #checksum 8127 SEQUENCE /// ENTRY I39769 #type complete TITLE aldehyde dehydrogenase (EC 1.2.-.-) - Bacillus stearothermophilus ORGANISM #formal_name Bacillus stearothermophilus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS I39769 REFERENCE I39769 !$#authors Imanaka, T.; Ohta, T.; Sakoda, H.; Widhyastuti, N.; !1Matsuoka, M. !$#journal J. Ferment. Bioeng. (1993) 76:161-167 !$#title Cloning, nucleotide sequence, and efficient expression of !1the gene coding for thermostable aldehyde dehydrogenase from !1Bacillus stearothermophilus, and Characterization of the !1enzyme. !$#accession I39769 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-488 ##label RES !'##cross-references GB:D13846; NID:g456298; PIDN:BAA02975.1; !1PID:g456299 CLASSIFICATION #superfamily aldehyde dehydrogenase (NAD+); aldehyde !1dehydrogenase homology KEYWORDS oxidoreductase FEATURE !$49-309 #domain aldehyde dehydrogenase homology #label ALDD\ !$255,289 #active_site Glu, Cys #status predicted SUMMARY #length 488 #molecular-weight 52915 #checksum 8422 SEQUENCE /// ENTRY G64878 #type complete TITLE aldehyde dehydrogenase (NAD) (EC 1.2.1.3) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS G64878; JU0397 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64878 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-495 ##label BLAT !'##cross-references GB:AE000228; GB:U00096; NID:g2367117; !1PIDN:AAC74382.1; PID:g1787558; UWGP:b1300 !'##experimental_source strain K-12, substrain MG1655 REFERENCE JU0397 !$#authors Heim, R.; Strehler, E.E. !$#journal Gene (1991) 99:15-23 !$#title Cloning an Escherichia coli gene encoding a protein !1remarkably similar to mammalian aldehyde dehydrogenases. !$#cross-references MUID:91216440; PMID:1840553 !$#accession JU0397 !'##molecule_type DNA !'##residues 1-312,'R',314-495 ##label HEI !'##cross-references GB:M38433; NID:g145223; PIDN:AAA23428.1; !1PID:g145224 !'##note the authors translated the codon AGG for residue 313 as Ser GENETICS !$#gene aldH CLASSIFICATION #superfamily aldehyde dehydrogenase (NAD+); aldehyde !1dehydrogenase homology KEYWORDS NAD; nucleotide binding; oxidoreductase; P-loop FEATURE !$49-56 #region nucleotide-binding motif A (P-loop)\ !$58-322 #domain aldehyde dehydrogenase homology #label ALDD\ !$267,302 #active_site Glu, Cys #status predicted SUMMARY #length 495 #molecular-weight 53418 #checksum 4889 SEQUENCE /// ENTRY I41082 #type complete TITLE 5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase (EC 1.2.1.-) - Escherichia coli ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS I41082; A61080 REFERENCE I41082 !$#authors Roper, D.I.; Stringfellow, J.M.; Cooper, R.A. !$#journal Gene (1995) 156:47-51 !$#title Sequence of the hpcC and hpcG genes of the meta-fission !1homoprotocatechuic acid pathway of Escherichia coli C: !1nearly 40% amino-acid identity with the analogous enzymes of !1the catechol pathway. !$#cross-references MUID:95255666; PMID:7737515 !$#accession I41082 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-468 ##label RES !'##cross-references EMBL:X81322; NID:g587109; PIDN:CAA57102.1; !1PID:g587110 REFERENCE A61080 !$#authors Fawcett, T.; Garrido-Pertierra, A.; Cooper, R.A. !$#journal FEMS Microbiol. Lett. (1989) 57:307-312 !$#title 5-carboxymethyl-2-hydroxymuconic semialdehyde dehydrogenases !1of Escherichia coli C and Klebsiella pneumoniae M5a1 show !1very high N-terminal sequence homology. !$#accession A61080 !'##molecule_type protein !'##residues 1-19,'Q',21-34 ##label FAW !'##experimental_source strain C CLASSIFICATION #superfamily aldehyde dehydrogenase (NAD+); aldehyde !1dehydrogenase homology KEYWORDS oxidoreductase FEATURE !$40-298 #domain aldehyde dehydrogenase homology #label ALDD\ !$244,278 #active_site Glu, Cys #status predicted SUMMARY #length 468 #molecular-weight 50827 #checksum 2561 SEQUENCE /// ENTRY A46600 #type complete TITLE methylmalonate-semialdehyde dehydrogenase (acylating) (EC 1.2.1.27) precursor - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-May-2000 ACCESSIONS A46600 REFERENCE A46600 !$#authors Deichaite, I.; Berthiaume, L.; Peseckis, S.M.; Patton, W.F.; !1Resh, M.D. !$#journal J. Biol. Chem. (1993) 268:13738-13747 !$#title Novel use of an iodo-myristyl-CoA analog identifies a !1semialdehyde dehydrogenase in bovine liver. !$#cross-references MUID:93293905; PMID:8514806 !$#accession A46600 !'##status preliminary !'##molecule_type mRNA !'##residues 1-537 ##label DEI !'##cross-references GB:L08643; NID:g289441; PIDN:AAA30650.1; !1PID:g289442 CLASSIFICATION #superfamily aldehyde dehydrogenase (NAD+); aldehyde !1dehydrogenase homology KEYWORDS coenzyme A; mitochondrion; oxidoreductase FEATURE !$80-338 #domain aldehyde dehydrogenase homology #label ALDD\ !$319 #active_site Cys #status predicted SUMMARY #length 537 #molecular-weight 58062 #checksum 6723 SEQUENCE /// ENTRY A44097 #type complete TITLE methylmalonate-semialdehyde dehydrogenase (acylating) (EC 1.2.1.27) - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-May-2000 ACCESSIONS A44097; A36518; S18379 REFERENCE A44097 !$#authors Kedishvili, N.Y.; Popov, K.M.; Rougraff, P.M.; Zhao, Y.; !1Crabb, D.W.; Harris, R.A. !$#journal J. Biol. Chem. (1992) 267:19724-19729 !$#title CoA-dependent methylmalonate-semialdehyde dehydrogenase, a !1unique member of the aldehyde dehydrogenase superfamily. !1cDNA cloning, evolutionary relationships, and tissue !1distribution. !$#cross-references MUID:92406934; PMID:1527093 !$#accession A44097 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-535 ##label KED !'##cross-references GB:M93401; NID:g205525; PIDN:AAA41638.1; !1PID:g205526 !'##experimental_source liver !'##note sequence extracted from NCBI backbone (NCBIP:114132) REFERENCE A36518 !$#authors Goodwin, G.W.; Rougraff, P.M.; Davis, E.J.; Harris, R.A. !$#journal J. Biol. Chem. (1989) 264:14965-14971 !$#title Purification and characterization of !1methylmalonate-semialdehyde dehydrogenase from rat liver. !1Identity to malonate-semialdehyde dehydrogenase. !$#cross-references MUID:89359305; PMID:2768248 !$#accession A36518 !'##status preliminary !'##molecule_type protein !'##residues 33-49 ##label GOO REFERENCE S18379 !$#authors Kedishvili, N.Y.; Popov, K.M.; Harris, R.A. !$#journal Arch. Biochem. Biophys. (1991) 290:21-26 !$#title The effect of ligand binding on the proteolytic pattern of !1methylmalonate semialdehyde dehydrogenase. !$#cross-references MUID:91378593; PMID:1898092 !$#accession S18379 !'##molecule_type protein !'##residues 33-44,'N',46-49,'QN',167,'N',169-189,'G' ##label KE2 CLASSIFICATION #superfamily aldehyde dehydrogenase (NAD+); aldehyde !1dehydrogenase homology KEYWORDS coenzyme A; mitochondrion; oxidoreductase FEATURE !$78-336 #domain aldehyde dehydrogenase homology #label ALDD\ !$317 #active_site Cys #status predicted SUMMARY #length 535 #molecular-weight 57807 #checksum 4583 SEQUENCE /// ENTRY B42902 #type complete TITLE methylmalonate-semialdehyde dehydrogenase (acylating) (EC 1.2.1.27) - Pseudomonas aeruginosa (ATCC 15692) ORGANISM #formal_name Pseudomonas aeruginosa DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 31-Dec-2000 ACCESSIONS B42902; E83198; S27602 REFERENCE A42902 !$#authors Steele, M.I.; Lorenz, D.; Hatter, K.; Park, A.; Sokatch, !1J.R. !$#journal J. Biol. Chem. (1992) 267:13585-13592 !$#title Characterization of the mmsAB operon of Pseudomonas !1aeruginosa PAO encoding methylmalonate-semialdehyde !1dehydrogenase and 3-hydroxyisobutyrate dehydrogenase. !$#cross-references MUID:92317087; PMID:1339433 !$#accession B42902 !'##status preliminary !'##molecule_type DNA !'##residues 1-497 ##label STE !'##cross-references EMBL:M84911; NID:g151360; PIDN:AAA25891.1; !1PID:g151362 !'##note sequence extracted from NCBI backbone (NCBIP:107707) REFERENCE A82950 !$#authors Stover, C.K.; Pham, X.Q.; Erwin, A.L.; Mizoguchi, S.D.; !1Warrener, P.; Hickey, M.J.; Brinkman, F.S.L.; Hufnagle, !1W.O.; Kowalik, D.J.; Lagrou, M.; Garber, R.L.; Goltry, L.; !1Tolentino, E.; Westbrook-Wadman, S.; Yuan, Y.; Brody, L.L.; !1Coulter, S.N.; Folger, K.R.; Kas, A.; Larbig, K.; Lim, R.M.; !1Smith, K.A.; Spencer, D.H.; Wong, G.K.S.; Wu, Z.; Paulsen, !1I.T.; Reizer, J.; Saier, M.H.; Hancock, R.E.W.; Lory, S.; !1Olson, M.V. !$#journal Nature (2000) 406:959-964 !$#title Complete genome sequence of Pseudomonas aeruginosa PA01, an !1opportunistic pathogen. !$#cross-references MUID:20437337; PMID:10984043 !$#accession E83198 !'##status preliminary !'##molecule_type DNA !'##residues 1-497 ##label STO !'##cross-references GB:AE004778; GB:AE004091; NID:g9949722; !1PIDN:AAG06958.1; GSPDB:GN00131; PASP:PA3570 !'##experimental_source strain PAO1 GENETICS !$#gene mmsA; PA3570 CLASSIFICATION #superfamily aldehyde dehydrogenase (NAD+); aldehyde !1dehydrogenase homology KEYWORDS coenzyme A; oxidoreductase FEATURE !$43-301 #domain aldehyde dehydrogenase homology #label ALDD\ !$282 #active_site Cys #status predicted SUMMARY #length 497 #molecular-weight 53663 #checksum 4590 SEQUENCE /// ENTRY A30149 #type complete TITLE aldehyde dehydrogenase (NADP) (EC 1.2.1.4) 3, tumor-associated [similarity] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 03-Jun-2002 ACCESSIONS A30149; A45986 REFERENCE A30149 !$#authors Jones Jr., D.E.; Brennan, M.D.; Hempel, J.; Lindahl, R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:1782-1786 !$#title Cloning and complete nucleotide sequence of a full-length !1cDNA encoding a catalytically functional tumor-associated !1aldehyde dehydrogenase. !$#cross-references MUID:88158077; PMID:2831537 !$#accession A30149 !'##molecule_type mRNA !'##residues 1-453 ##label JON !'##cross-references GB:J03637; NID:g202832; PIDN:AAA40713.1; !1PID:g202833 REFERENCE A45986 !$#authors Asman, D.C.; Takimoto, K.; Pitot, H.C.; Dunn, T.J.; Lindahl, !1R. !$#journal J. Biol. Chem. (1993) 268:12530-12536 !$#title Organization and characterization of the rat class 3 !1aldehyde dehydrogenase gene. !$#cross-references MUID:93286088; PMID:8509394 !$#accession A45986 !'##molecule_type DNA !'##residues 1-49,'L',51-54 ##label ASM !'##cross-references GB:J03637; NID:g202832 !'##note sequence inconsistent with the nucleotide translation !'##note sequence extracted from NCBI backbone (NCBIN:133585, !1NCBIP:133586) CLASSIFICATION #superfamily aldehyde dehydrogenase (NAD+); aldehyde !1dehydrogenase homology KEYWORDS NADP; oxidoreductase FEATURE !$3-264 #domain aldehyde dehydrogenase homology #label ALDD\ !$210,244 #active_site Glu, Cys #status predicted SUMMARY #length 453 #molecular-weight 50338 #checksum 7552 SEQUENCE /// ENTRY A42584 #type complete TITLE aldehyde dehydrogenase [NAD(P)] (EC 1.2.1.5) 3 - human ALTERNATE_NAMES aldehyde dehydrogenase, high Km ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS A42584; I51845; A60267; S15777 REFERENCE A42584 !$#authors Hsu, L.C.; Chang, W.C.; Shibuya, A.; Yoshida, A. !$#journal J. Biol. Chem. (1992) 267:3030-3037 !$#title Human stomach aldehyde dehydrogenase cDNA and genomic !1cloning, primary structure, and expression in Escherichia !1coli. !$#cross-references MUID:92147646; PMID:1737758 !$#accession A42584 !'##status preliminary !'##molecule_type mRNA !'##residues 1-453 ##label HSU !'##cross-references GB:M77477; NID:g178374; PIDN:AAB46377.1; !1PID:g178375 !'##experimental_source stomach !'##note sequence extracted from NCBI backbone (NCBIN:80919, !1NCBIP:80920) REFERENCE I51845 !$#authors Hsu, L.C.; Yoshida, A. !$#journal Adv. Exp. Med. Biol. (1993) 328:141-152 !$#title Human stomach aldehyde dehydrogenase, ALDH3. !$#cross-references MUID:93263008; PMID:8493892 !$#accession I51845 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-453 ##label RES !'##cross-references GB:S61044; NID:g300401; PIDN:AAB26658.1; !1PID:g300402 REFERENCE A60267 !$#authors Eckey, R.; Timmann, R.; Hempel, J.; Agarwal, D.P.; Goedde, !1H.W. !$#journal Adv. Exp. Med. Biol. (1991) 284:43-52 !$#title Biochemical, immunological, and molecular characterization !1of a "high Km" aldehyde dehydrogenase. !$#cross-references MUID:91272937; PMID:1905102 !$#accession A60267 !'##molecule_type protein !'##residues 27-35;203-214;294-298,'N',300-302;315-321,'E', !1323-327;377-398,'T',400-404 ##label ECK !'##experimental_source stomach REFERENCE S15777 !$#authors Yin, S.J.; Vagelopoulos, N.; Wang, S.L.; Joernvall, H. !$#journal FEBS Lett. (1991) 283:85-88 !$#title Structural features of stomach aldehyde dehydrogenase !1distinguish dimeric aldehyde dehydrogenase as a "variable" !1enzyme. "Variable" and "constant" enzymes within the alcohol !1and aldehyde dehydrogenase families. !$#cross-references MUID:91243885; PMID:2037078 !$#accession S15777 !'##molecule_type protein !'##residues 51-61;84-96;162-166,'X',168-169,'L',171-216,'X', !1218-220;254-275;282-322;350-371;391-420;437-453 ##label YIN COMMENT This isozyme of aldehyde dehydrogenase accepts both NAD+ and !1NADP+ as coenzymes. GENETICS !$#gene GDB:ALDH3 !'##cross-references GDB:118992; OMIM:100660 !$#map_position 17pter-17qter CLASSIFICATION #superfamily aldehyde dehydrogenase (NAD+); aldehyde !1dehydrogenase homology KEYWORDS NAD; NADP; oxidoreductase FEATURE !$3-264 #domain aldehyde dehydrogenase homology #label ALDD\ !$210,244 #active_site Glu, Cys #status predicted SUMMARY #length 453 #molecular-weight 50335 #checksum 6759 SEQUENCE /// ENTRY A41028 #type complete TITLE aldehyde dehydrogenase (NAD) (EC 1.2.1.3) 4, microsomal [similarity] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 03-Jun-2002 ACCESSIONS A41028 REFERENCE A41028 !$#authors Miyauchi, K.; Masaki, R.; Taketani, S.; Yamamoto, A.; !1Akayama, M.; Tashiro, Y. !$#journal J. Biol. Chem. (1991) 266:19536-19542 !$#title Molecular cloning, sequencing, and expression of cDNA for !1rat liver microsomal aldehyde dehydrogenase. !$#cross-references MUID:92011753; PMID:1717467 !$#accession A41028 !'##molecule_type mRNA !'##residues 1-484 ##label MIY !'##cross-references GB:M73714; NID:g205265; PIDN:AAA41555.1; !1PID:g205266 CLASSIFICATION #superfamily aldehyde dehydrogenase (NAD+); aldehyde !1dehydrogenase homology KEYWORDS NAD; oxidoreductase; transmembrane protein FEATURE !$1-261 #domain aldehyde dehydrogenase homology #label ALDD\ !$207,241 #active_site Glu, Cys #status predicted SUMMARY #length 484 #molecular-weight 54081 #checksum 9633 SEQUENCE /// ENTRY S53503 #type complete TITLE probable aldehyde dehydrogenase (EC 1.1.1.-) btg-26 - rape ORGANISM #formal_name Brassica napus #common_name rape DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S53503 REFERENCE S53503 !$#authors Stroeher, V.L.; Boothe, J.G.; Good, A.G. !$#journal Plant Mol. Biol. (1995) 27:541-551 !$#title Molecular cloning and expression of a turgor-responsive gene !1in Brassica napus. !$#cross-references MUID:95201247; PMID:7894018 !$#accession S53503 !'##molecule_type DNA !'##residues 1-494 ##label STR !'##cross-references EMBL:S77096; NID:g913940; PIDN:AAB33843.1; !1PID:g913941 GENETICS !$#gene btg-26 !$#introns 48/3; 77/3; 121/3; 146/1; 153/3; 175/1; 190/2; 250/3; 309/3; !1364/3; 411/3; 444/2 CLASSIFICATION #superfamily aldehyde dehydrogenase (NAD+); aldehyde !1dehydrogenase homology KEYWORDS NAD; oxidoreductase; stress-induced protein FEATURE !$60-323 #domain aldehyde dehydrogenase homology #label ALDD\ !$269,303 #active_site Glu, Cys #status predicted SUMMARY #length 494 #molecular-weight 52687 #checksum 2118 SEQUENCE /// ENTRY S43832 #type complete TITLE glyceraldehyde-3-phosphate dehydrogenase (NADP) (EC 1.2.1.9) - garden pea ORGANISM #formal_name Pisum sativum #common_name garden pea DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S43832 REFERENCE S43832 !$#authors Habenicht, A.; Hellman, U.; Cerff, R. !$#journal J. Mol. Biol. (1994) 237:165-171 !$#title Non-phosphorylating GAPDH of higher plants is a member of !1the aldehyde dehydrogenase superfamily with no sequence !1homology to phosphorylating GAPDH. !$#cross-references MUID:94180387; PMID:7545914 !$#accession S43832 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-496 ##label HAB !'##cross-references EMBL:X75327 CLASSIFICATION #superfamily aldehyde dehydrogenase (NAD+); aldehyde !1dehydrogenase homology KEYWORDS NADP; oxidoreductase FEATURE !$54-318 #domain aldehyde dehydrogenase homology #label ALDD\ !$264,298 #active_site Glu, Cys #status predicted SUMMARY #length 496 #molecular-weight 53006 #checksum 3619 SEQUENCE /// ENTRY S43833 #type complete TITLE glyceraldehyde-3-phosphate dehydrogenase (NADP) (EC 1.2.1.9) - maize ORGANISM #formal_name Zea mays #common_name maize DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S43833 REFERENCE S43832 !$#authors Habenicht, A.; Hellman, U.; Cerff, R. !$#journal J. Mol. Biol. (1994) 237:165-171 !$#title Non-phosphorylating GAPDH of higher plants is a member of !1the aldehyde dehydrogenase superfamily with no sequence !1homology to phosphorylating GAPDH. !$#cross-references MUID:94180387; PMID:7545914 !$#accession S43833 !'##molecule_type mRNA !'##residues 1-498 ##label HAB !'##cross-references EMBL:X75326; NID:g474407; PIDN:CAA53075.1; !1PID:g474408 CLASSIFICATION #superfamily aldehyde dehydrogenase (NAD+); aldehyde !1dehydrogenase homology KEYWORDS NADP; oxidoreductase FEATURE !$56-320 #domain aldehyde dehydrogenase homology #label ALDD\ !$266,300 #active_site Glu, Cys #status predicted SUMMARY #length 498 #molecular-weight 53146 #checksum 685 SEQUENCE /// ENTRY RDBYC #type complete TITLE 1-pyrroline-5-carboxylate dehydrogenase (EC 1.5.1.12) precursor - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein H8179.11; protein YHR037w ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1991 #sequence_revision 10-Feb-1995 #text_change 23-Mar-2001 ACCESSIONS S46738; S05876 REFERENCE S46732 !$#authors Du, Z. !$#submission submitted to the EMBL Data Library, May 1994 !$#description The sequence of S. cerevisiae cosmid 8179. !$#accession S46738 !'##molecule_type DNA !'##residues 1-575 ##label DUZ !'##cross-references EMBL:U00062; NID:g488162; PIDN:AAB68907.1; !1PID:g488172; GSPDB:GN00008; MIPS:YHR037w REFERENCE S05876 !$#authors Krzywicki, K.A.; Brandriss, M.C. !$#journal Mol. Cell. Biol. (1984) 4:2837-2842 !$#title Primary structure of the nuclear PUT2 gene involved in the !1mitochondrial pathway for proline utilization in !1Saccharomyces cerevisiae. !$#cross-references MUID:85137477; PMID:6098824 !$#accession S05876 !'##molecule_type DNA !'##residues 1-186,'SR',189-263,'L',265-540,'G',542-560,'S',562-575 !1##label KRZ !'##cross-references EMBL:M10029; NID:g172302; PIDN:AAA34924.1; !1PID:g172303 GENETICS !$#gene SGD:PUT2; MIPS:YHR037w !'##cross-references SGD:S0001079; MIPS:YHR037w !$#map_position 8R !$#genome nuclear CLASSIFICATION #superfamily aldehyde dehydrogenase (NAD+); aldehyde !1dehydrogenase homology KEYWORDS mitochondrial matrix; mitochondrion; NAD; oxidoreductase FEATURE !$101-371 #domain aldehyde dehydrogenase homology #label ALDD\ !$317,351 #active_site Glu, Cys #status predicted SUMMARY #length 575 #molecular-weight 64435 #checksum 2797 SEQUENCE /// ENTRY DEECDA #type complete TITLE aspartate-semialdehyde dehydrogenase (EC 1.2.1.11) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 01-Mar-2002 ACCESSIONS A00364; D65139 REFERENCE A00364 !$#authors Haziza, C.; Stragier, P.; Patte, J.C. !$#journal EMBO J. (1982) 1:379-384 !$#title Nucleotide sequence of the asd gene of Escherichia coli: !1absence of a typical attenuation signal. !$#cross-references MUID:84182485; PMID:6143662 !$#accession A00364 !'##molecule_type DNA !'##residues 1-367 ##label HAZ !'##cross-references GB:V00262; NID:g40991; PIDN:CAA23511.1; PID:g40992 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65139 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-367 ##label BLAT !'##cross-references GB:AE000420; GB:U00096; NID:g1789840; !1PIDN:AAC76458.1; PID:g1789841; UWGP:b3433 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene asd COMPLEX homodimer FUNCTION !$#description catalyzes the reversible conversion of L-4-aspartyl !1phosphate and NADPH to L-aspartate 4-semialdehyde, phosphate !1and NADP+ !$#pathway threonine biosynthesis CLASSIFICATION #superfamily aspartate-semialdehyde dehydrogenase KEYWORDS homodimer; NADP; oxidoreductase; threonine biosynthesis FEATURE !$135 #active_site Cys #status predicted SUMMARY #length 367 #molecular-weight 40018 #checksum 9758 SEQUENCE /// ENTRY QQECH3 #type complete TITLE probable dehydrogenase (EC 1.2.1.-) usg1 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS A23792; B33494; I69363; I69364; E65004 REFERENCE A93577 !$#authors Arps, P.J.; Marvel, C.C.; Rubin, B.C.; Tolan, D.A.; Penhoet, !1E.E.; Winkler, M.E. !$#journal Nucleic Acids Res. (1985) 13:5297-5315 !$#title Structural features of the hisT operon of Escherichia coli !1K-12. !$#cross-references MUID:85269644; PMID:2991861 !$#accession A23792 !'##molecule_type DNA !'##residues 1-337 ##label ARP !'##cross-references GB:X02743; NID:g41716; PIDN:CAA26521.1; PID:g41717 !'##experimental_source strain K12 REFERENCE JV0051 !$#authors Schoenlein, P.V.; Roa, B.B.; Winkler, M.E. !$#journal J. Bacteriol. (1989) 171:6084-6092 !$#title Divergent transcription of pdxB and homology between the !1pdxB and serA gene products in Escherichia coli K-12. !$#cross-references MUID:90036695; PMID:2681152 !$#accession B33494 !'##molecule_type DNA !'##residues 1-27 ##label SCH !'##cross-references GB:M29962; NID:g147122; PIDN:AAA24309.1; !1PID:g147125 REFERENCE I54872 !$#authors Arps, P.J.; Winkler, M.E. !$#journal J. Bacteriol. (1987) 169:1061-1070 !$#title Structural analysis of the Escherichia coli K-12 hisT operon !1by using a kanamycin resistance cassette. !$#cross-references MUID:87137258; PMID:3029016 !$#accession I69363 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-13 ##label ARP2 !'##cross-references GB:M15541; NID:g147126; PIDN:AAA24311.1; !1PID:g147131 !$#accession I69364 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 329-337 ##label AR2 !'##cross-references GB:M15542; NID:g147127; PIDN:AAA24312.1; !1PID:g147132 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65004 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-337 ##label BLAT !'##cross-references GB:AE000320; GB:U00096; NID:g1788647; !1PIDN:AAC75379.1; PID:g1788658; UWGP:b2319 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene usg; usg1 !$#map_position 50 min CLASSIFICATION #superfamily aspartate-semialdehyde dehydrogenase KEYWORDS NAD; oxidoreductase SUMMARY #length 337 #molecular-weight 36364 #checksum 9570 SEQUENCE /// ENTRY F69590 #type complete TITLE aspartate-semialdehyde dehydrogenase (EC 1.2.1.11) - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 05-Dec-1997 #sequence_revision 02-Jul-1998 #text_change 16-Jun-2000 ACCESSIONS F69590; D46665; S34599; S35653 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69590 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-346 ##label KUN !'##cross-references GB:Z99112; GB:AL009126; NID:g2633902; !1PIDN:CAB13548.1; PID:g2634047 !'##experimental_source strain 168 REFERENCE A46665 !$#authors Chen, N.Y.; Jiang, S.Q.; Klein, D.A.; Paulus, H. !$#journal J. Biol. Chem. (1993) 268:9448-9465 !$#title Organization and nucleotide sequence of the Bacillus !1subtilis diaminopimelate operon, a cluster of genes encoding !1the first three enzymes of diaminopimelate synthesis and !1dipicolinate synthase. !$#cross-references MUID:93252813; PMID:8098035 !$#accession D46665 !'##molecule_type DNA !'##residues 1-41,'A',43-346 ##label CHE1 !'##cross-references EMBL:L08471 !'##note authors translated the codon GCT for residue 42 as Val REFERENCE S34595 !$#authors Chen, N.Y.; Jiang, S.Q.; Klein, D.A.; Paulus, H. !$#submission submitted to the EMBL Data Library, January 1993 !$#description Organization and nucleotide sequence of the Bacillus !1subtilis diaminopimelate operon, a cluster of genes encoding !1the first three enzymes of diaminopimelate synthesis and !1dipicolinate synthase. !$#accession S34599 !'##molecule_type DNA !'##residues 1-346 ##label CHE2 !'##cross-references EMBL:L08471; NID:g142823; PIDN:AAA22383.1; !1PID:g142828 REFERENCE S35651 !$#authors Daniel, R.A.; Errington, J. !$#journal J. Mol. Biol. (1993) 232:468-483 !$#title Cloning, DNA sequence, functional analysis and !1transcriptional regulation of the genes encoding dipicolinic !1acid synthetase required for sporulation in Bacillus !1subtilis. !$#cross-references MUID:93347235; PMID:8345520 !$#accession S35653 !'##molecule_type DNA !'##residues 1-41,'A',43-76,'T',78-208 ##label DAN !'##cross-references EMBL:Z22554; NID:g296144; PIDN:CAA80276.1; !1PID:g296147 GENETICS !$#gene asd FUNCTION !$#description catalyzes the reversible conversion of L-4-aspartyl !1phosphate and NADPH to L-aspartate 4-semialdehyde, phosphate !1and NADP+ !$#pathway threonine biosynthesis CLASSIFICATION #superfamily aspartate-semialdehyde dehydrogenase KEYWORDS NADP; oxidoreductase; threonine biosynthesis FEATURE !$130 #active_site Cys #status predicted SUMMARY #length 346 #molecular-weight 37847 #checksum 5973 SEQUENCE /// ENTRY A29137 #type complete TITLE aspartate-semialdehyde dehydrogenase (EC 1.2.1.11) - Streptococcus mutans ORGANISM #formal_name Streptococcus mutans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A29137 REFERENCE A29137 !$#authors Cardineau, G.A.; Curtiss III, R. !$#journal J. Biol. Chem. (1987) 262:3344-3353 !$#title Nucleotide sequence of the asd gene of Streptococcus mutans. !1Identification of the promoter region and evidence for !1attenuator-like sequences preceding the structural gene. !$#cross-references MUID:87137615; PMID:2434499 !$#accession A29137 !'##molecule_type DNA !'##residues 1-357 ##label CAR !'##cross-references GB:J02667; NID:g153560; PIDN:AAA26850.1; !1PID:g153562 GENETICS !$#gene asd CLASSIFICATION #superfamily aspartate-semialdehyde dehydrogenase KEYWORDS NAD; oxidoreductase SUMMARY #length 357 #molecular-weight 38899 #checksum 6779 SEQUENCE /// ENTRY S14523 #type complete TITLE aspartate-semialdehyde dehydrogenase (EC 1.2.1.11) - Vibrio cholerae ORGANISM #formal_name Vibrio cholerae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S14523 REFERENCE S14523 !$#authors Avest Ter, A.R.; Frits, R.M. !$#submission submitted to the EMBL Data Library, November 1990 !$#accession S14523 !'##molecule_type DNA !'##residues 1-337 ##label AVE !'##cross-references EMBL:X55363; NID:g48345; PIDN:CAA39048.1; !1PID:g48346 CLASSIFICATION #superfamily aspartate-semialdehyde dehydrogenase KEYWORDS NAD; oxidoreductase SUMMARY #length 337 #molecular-weight 37359 #checksum 4921 SEQUENCE /// ENTRY B64123 #type complete TITLE probable dehydrogenase (EC 1.2.1.-) usg1 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B64123 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession B64123 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-317 ##label TIGR !'##cross-references GB:U32822; GB:L42023; NID:g1574265; !1PIDN:AAC23080.1; PID:g1574271; TIGR:HI1433 CLASSIFICATION #superfamily aspartate-semialdehyde dehydrogenase KEYWORDS NAD; oxidoreductase SUMMARY #length 317 #molecular-weight 35414 #checksum 5083 SEQUENCE /// ENTRY S49978 #type complete TITLE aspartate-semialdehyde dehydrogenase (EC 1.2.1.11) - Corynebacterium glutamicum ORGANISM #formal_name Corynebacterium glutamicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S49978; S12251 REFERENCE S49977 !$#authors Serebrijski, I.; Wojcik, F.; Reyes, O.; Leblon, G. !$#submission submitted to the EMBL Data Library, November 1994 !$#description Two loci of Corynebacterium glutamicum ATCC17965 that !1complement Escherichia coli mutants affected in the !1expression of the proA gene product. !$#accession S49978 !'##status preliminary !'##molecule_type DNA !'##residues 1-344 ##label SER !'##cross-references EMBL:X82928; NID:g599716; PIDN:CAA58101.1; !1PID:g599718 REFERENCE S12250 !$#authors Kalinowski, J.; Bachmann, B.; Thierbach, G.; Puehler, A. !$#journal Mol. Gen. Genet. (1990) 224:317-324 !$#title Aspartokinase genes lysC-alpha and lysC-beta overlap and are !1adjacent to the aspartate beta-semialdehyde dehydrogenase !1gene asd in Corynebacterium glutamicum. !$#cross-references MUID:91094767; PMID:1980002 !$#accession S12251 !'##status preliminary !'##molecule_type DNA !'##residues 1-271,'D',273-344 ##label MOL !'##cross-references GB:X57226; NID:g40509; PIDN:CAA40504.1; PID:g40512 GENETICS !$#gene asd CLASSIFICATION #superfamily aspartate-semialdehyde dehydrogenase KEYWORDS NAD; oxidoreductase SUMMARY #length 344 #molecular-weight 36226 #checksum 136 SEQUENCE /// ENTRY S76022 #type complete TITLE aspartate-semialdehyde dehydrogenase (EC 1.2.1.11) - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S76022 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76022 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-280 ##label KAN !'##cross-references EMBL:D64006; GB:AB001339; NID:g1001291; !1PIDN:BAA10869.1; PID:g1001379 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily aspartate-semialdehyde dehydrogenase KEYWORDS NAD; oxidoreductase SUMMARY #length 280 #molecular-weight 30605 #checksum 4824 SEQUENCE /// ENTRY E64668 #type complete TITLE aspartate-semialdehyde dehydrogenase (EC 1.2.1.11) - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS E64668 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession E64668 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-346 ##label TOM !'##cross-references GB:AE000625; GB:AE000511; NID:g2314349; !1PIDN:AAD08235.1; PID:g2314350; TIGR:HP1189 CLASSIFICATION #superfamily aspartate-semialdehyde dehydrogenase KEYWORDS oxidoreductase SUMMARY #length 346 #molecular-weight 38116 #checksum 8847 SEQUENCE /// ENTRY DEHUG3 #type complete TITLE glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) (EC 1.2.1.12) [validated] - human ALTERNATE_NAMES triose phosphate dehydrogenase CONTAINS uracil DNA glycosylase (EC 3.2.2.-), nuclear ORGANISM #formal_name Homo sapiens #common_name man DATE 02-Apr-1982 #sequence_revision 08-Dec-1994 #text_change 03-Jun-2002 ACCESSIONS A31988; A00365; A21939; I53309; B22939; A45924; I55258; !1A41297; S26758; A12103; A00366; S66563; S18779 REFERENCE A31988 !$#authors Ercolani, L.; Florence, B.; Denaro, M.; Alexander, M. !$#journal J. Biol. Chem. (1988) 263:15335-15341 !$#title Isolation and complete sequence of a functional human !1glyceraldehyde-3-phosphate dehydrogenase gene. !$#cross-references MUID:89008430; PMID:3170585 !$#accession A31988 !'##molecule_type DNA !'##residues 1-335 ##label ERC !'##cross-references GB:J04038; NID:g182980; PIDN:AAA53191.1; !1PID:g182981 REFERENCE A00365 !$#authors Arcari, P.; Martinelli, R.; Salvatore, F. !$#journal Nucleic Acids Res. (1984) 12:9179-9189 !$#title The complete sequence of a full length cDNA for human liver !1glyceraldehyde-3-phosphate dehydrogenase: evidence for !1multiple mRNA species. !$#cross-references MUID:85087928; PMID:6096821 !$#accession A00365 !'##molecule_type mRNA !'##residues 1-224,'D',226-335 ##label ARC !'##cross-references GB:X01677; GB:K03121; GB:M17851; GB:X01110; !1NID:g31644; PIDN:CAA25833.1; PID:g31645 REFERENCE A21939 !$#authors Hanauer, A.; Mandel, J.L. !$#journal EMBO J. (1984) 3:2627-2633 !$#title The glyceraldehyde 3 phosphate dehydrogenase gene family: !1structure of a human cDNA and of an X chromosome linked !1pseudogene: amazing complexity of the gene family in mouse. !$#cross-references MUID:85076585; PMID:6096136 !$#accession A21939 !'##molecule_type mRNA !'##residues 1-335 ##label HAN !'##cross-references GB:X01677; GB:K03121; GB:M17851; GB:X01110; !1NID:g31644 REFERENCE I53309 !$#authors Dani, C.; Piechaczyk, M.; Audigier, Y.; El Sabouty, S.; !1Cathala, G.; Marty, L.; Fort, P.; Blanchard, J.M.; Jeanteur, !1P. !$#journal Eur. J. Biochem. (1984) 145:299-304 !$#title Characterization of the transcription products of !1glyceraldehyde 3-phosphate-dehydrogenase gene in HeLa cells. !$#cross-references MUID:85051356; PMID:6499844 !$#accession I53309 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 292-310,'V',312-335 ##label DAN !'##cross-references GB:M28283; NID:g182978; PIDN:AAA52519.1; !1PID:g182979 REFERENCE A93562 !$#authors Tso, J.Y.; Sun, X.H.; Kao, T.; Reece, K.S.; Wu, R. !$#journal Nucleic Acids Res. (1985) 13:2485-2502 !$#title Isolation and characterization of rat and human !1glyceraldehyde-3-phosphate dehydrogenase cDNAs: genomic !1complexity and molecular evolution of the gene. !$#cross-references MUID:85215629; PMID:2987855 !$#accession B22939 !'##molecule_type mRNA !'##residues 2-335 ##label TSO !'##cross-references GB:M17851; NID:g182860; PIDN:AAA86283.1; !1PID:g182861 REFERENCE A45924 !$#authors Tokunaga, K.; Nakamura, Y.; Sakata, K.; Fujimori, K.; !1Ohkubo, M.; Sawada, K.; Sakiyama, S. !$#journal Cancer Res. (1987) 47:5616-5619 !$#title Enhanced expression of a glyceraldehyde-3-phosphate !1dehydrogenase gene in human lung cancers. !$#cross-references MUID:88026722; PMID:3664468 !$#accession A45924 !'##molecule_type mRNA !'##residues 1-335 ##label TOK !'##cross-references GB:M33197; NID:g182976; PIDN:AAA52518.1; !1PID:g182977 REFERENCE I55258 !$#authors Allen, R.W.; Trach, K.A.; Hoch, J.A. !$#journal J. Biol. Chem. (1987) 262:649-653 !$#title Identification of the 37-kDa protein displaying a variable !1interaction with the erythroid cell membrane as !1glyceraldehyde-3-phosphate dehydrogenase. !$#cross-references MUID:87109159; PMID:3027061 !$#accession I55258 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-335 ##label ALL !'##cross-references GB:J02642; NID:g182862; PIDN:AAA52496.1; !1PID:g182863 REFERENCE A41297 !$#authors Meyer-Siegler, K.; Mauro, D.J.; Seal, G.; Wurzer, J.; !1deRiel, J.K.; Sirover, M.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:8460-8464 !$#title A human nuclear uracil DNA glycosylase is the 37-kDa subunit !1of glyceraldehyde-3-phosphate dehydrogenase. !$#cross-references MUID:92020872; PMID:1924305 !$#accession A41297 !'##molecule_type mRNA !'##residues 1-335 ##label MEY !'##cross-references GB:X53778 REFERENCE S26758 !$#authors Sirover, M.A. !$#submission submitted to the EMBL Data Library, July 1990 !$#accession S26758 !'##molecule_type mRNA !'##residues 1-193,'NCGVMAA',201,203,'SRTSSLPLL',213,'L',215-329,333-335 !1##label SIR !'##cross-references EMBL:X53778; NID:g35052; PIDN:CAA37794.1; !1PID:g35053 REFERENCE A12103 !$#authors Nowak, K.; Kuczek, M.; Ostropolska, L.; Malarska, A.; Wolny, !1M.; Branowski, T. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1975) 356:1181-1183 !$#title The covalent structure of glyceraldehyde-phosphate !1dehydrogenase from human muscles. Isolation and amino acid !1sequences of peptides from tryptic digest. !$#cross-references MUID:76067491; PMID:1193541 !$#accession A12103 !'##molecule_type protein !'##residues 2-8,'B',10-23,'B',25-27;46-47,'Z',49,'B',51-61,67-69,'B', !171,'K';'B',82,'AZ',85-86;108-112,'K';114-117;'I',119-120, !1122-126,'B',128-132,'VMGB',137,'Z',139-140,'BB',143-165, !1'BH',168-169,'GIIV',171,'ZZ',174-176,'SS',179-180,'AB', !1186-188,'B',190-194;'B',199-202;'A',204-205,'L',207-224,'D', !1226-242,'L',244-249,'Z',251-255,'BB',258-259,261-263,'Z', !1265-266,'Z',268-271;'L',273,'BW',276,'B','BBZ',318-321, !1323-334,'SKGVK' ##label NOW !'##note some of this partial sequence was assigned tentatively based on !1composition REFERENCE A00366 !$#authors Nowak, K.; Wolny, M.; Banas, T. !$#journal FEBS Lett. (1981) 134:143-146 !$#title The complete amino acid sequence of human muscle !1glyceraldehyde 3-phosphate dehydrogenase. !$#cross-references MUID:82073291; PMID:7030790 !$#accession A00366 !'##molecule_type protein !'##residues 2-8,'D',10-40,'H',42-63,'D',65-69,'D',71,'KA',74-82,'EN', !185-91,'TA',94-112,'K',114-118,'IV',121-137,'F',139-140,'A', !1142-166,'H',168-189,'S',191-197,'G',199-202,'A',204-205,'L', !1207-224,'D',226-242,'L',244-263,'E',265-278,'DE',281-283, !1'D',285-287,'GSN',291-293,'I',295-301,'E',303-305,'T', !1307-310,'V',312-321,'E',323-335 ##label NO2 REFERENCE S66563 !$#authors Sioud, M.; Jespersen, L. !$#journal J. Mol. Biol. (1996) 257:775-789 !$#title Enhancement of hammerhead ribozyme catalysis by !1glyceraldehyde-3-phosphate dehydrogenase. !$#cross-references MUID:96194445; PMID:8636981 !$#accession S66563 !'##molecule_type protein !'##residues 4-15 ##label SIO REFERENCE A38927 !$#authors Mercer, W.D.; Winn, S.I.; Watson, H.C. !$#journal J. Mol. Biol. (1976) 104:277-283 !$#title Twinning in crystals of human skeletal muscle !1D-glyceraldehyde-3-phosphate dehydrogenase. !$#cross-references MUID:76265083; PMID:957435 !$#contents annotation; X-ray crystallography, 3.5 angstroms REFERENCE A50598 !$#authors Watson, H.C.; Campbell, J.C. !$#submission submitted to the Brookhaven Protein Data Bank, June 1983 !$#cross-references PDB:3GPD !$#contents annotation; X-ray crystallography, 3.5 angstroms, residues !12-8,'D',10-40,'H',42-63,'D',65-69,'D',71,'KA',74-82,'EN', !185-91,'TA',94-112,'K',114-118,'IV',121-137,'F',139-140,'A', !1142-166,'H',168-189,'S',191-197,'G',199-202,'A',204-205,'L', !1207-224,'D',226-242,'L',244-263,'E',265-278,'DE',281-283, !1'D',285-287,'GSN',291-293,'I',295-301,'E',303-305,'T', !1307-310,'V',312-321,'E',323-335 COMMENT Although the gene for this protein is a member of a !1multigene family and there are many differences between the !1reported sequence from muscle protein and from liver !1nucleotide translations, only one gene appears to be !1expressed. GENETICS !$#gene GDB:GAPD !'##cross-references GDB:119249; OMIM:138400 !$#map_position 12p13.31-12p13.1 !$#introns 10/2; 43/3; 79/2; 109/3; 148/2; 175/3; 313/2 COMPLEX homotetramer; crystallizes as two symmetric dimers in which !1the partners have different conformations COMPLEX monomer FUNCTION CYT !$#description oxidoreductase; reversibly catalyzes the oxidative !1phosphorylation of glyceraldehyde-3-phosphate to 1, !13-diphosphoglycerate in the presence of inorganic phosphate !1and NAD+ !$#pathway gluconeogenesis; glycolysis !$#note tetrameric form; cytosol FUNCTION NUC !$#description DNA repair; uracil DNA glycosylase for base-excision in DNA !1repair !$#note monomeric form; nuclear CLASSIFICATION #superfamily glyceraldehyde-3-phosphate dehydrogenase KEYWORDS cytosol; DNA repair; gluconeogenesis; glycolysis; !1glycosidase; homotetramer; hydrolase; monomer; !1multifunctional enzyme; NAD; nucleus; oxidoreductase FEATURE !$2-335 #product glyceraldehyde-3-phosphate dehydrogenase !8#status experimental #label MAT\ !$5-35 #region beta-alpha-beta NAD nucleotide-binding fold\ !$152 #active_site Cys #status experimental\ !$179 #active_site His #status predicted SUMMARY #length 335 #molecular-weight 36053 #checksum 3660 SEQUENCE /// ENTRY DEPGG3 #type complete TITLE glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) (EC 1.2.1.12) - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 08-Oct-1981 #sequence_revision 08-Oct-1981 #text_change 03-Jun-2002 ACCESSIONS A93156; A94413; A00367 REFERENCE A93156 !$#authors Harris, J.I.; Perham, R.N. !$#journal Nature (1968) 219:1025-1028 !$#title Glyceraldehyde 3-phosphate dehydrogenase from pig muscle. !$#cross-references MUID:68399311; PMID:4299800 !$#accession A93156 !'##molecule_type protein !'##residues 1-44,'E',46-332 ##label HAR REFERENCE A94413 !$#authors Harris, J.I.; Davidson, B.E.; Sajgo, M.; Noller, H.F.; !1Perham, R.N. !$#book Enzymes and Isoenzymes: Structure, Properties and Function, !1Shugar, D., ed., pp.1-15, Academic Press, London and New !1York, 1970 !$#accession A94413 !'##molecule_type protein !'##residues 45 ##label HA2 COMMENT Cys-149 covalently binds glyceraldehyde-3-phosphate. CLASSIFICATION #superfamily glyceraldehyde-3-phosphate dehydrogenase KEYWORDS gluconeogenesis; glycolysis; homotetramer; NAD; !1oxidoreductase FEATURE !$2-32 #region beta-alpha-beta NAD nucleotide-binding fold\ !$149,176 #active_site Cys, His #status predicted SUMMARY #length 332 #molecular-weight 35709 #checksum 9548 SEQUENCE /// ENTRY DEHYG #type complete TITLE glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) (EC 1.2.1.12) - Chinese hamster ORGANISM #formal_name Cricetulus griseus #common_name Chinese hamster DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 03-Jun-2002 ACCESSIONS S10221 REFERENCE S10221 !$#authors Vincent, S.; Fort, P. !$#journal Nucleic Acids Res. (1990) 18:3054 !$#title Nucleotide sequence of hamster glyceraldehyde-3-phosphate !1dehydrogenase mRNA. !$#cross-references MUID:90272420; PMID:2349105 !$#accession S10221 !'##molecule_type mRNA !'##residues 1-333 ##label VIN !'##cross-references EMBL:X52123; NID:g49434; PIDN:CAA36368.1; !1PID:g49435 CLASSIFICATION #superfamily glyceraldehyde-3-phosphate dehydrogenase KEYWORDS gluconeogenesis; glycolysis; homotetramer; NAD; !1oxidoreductase FEATURE !$3-33 #region beta-alpha-beta NAD nucleotide-binding fold\ !$150,177 #active_site Cys, His #status predicted SUMMARY #length 333 #molecular-weight 35748 #checksum 4631 SEQUENCE /// ENTRY DEMSG #type complete TITLE glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) (EC 1.2.1.12) - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 03-Jun-2002 ACCESSIONS JT0553; S14160 REFERENCE JT0553 !$#authors Sabath, D.E.; Broome, H.E.; Prystowsky, M.B. !$#journal Gene (1990) 91:185-191 !$#title Glyceraldehyde-3-phosphate dehydrogenase mRNA is a major !1interleukin 2-induced transcript in a cloned T-helper !1lymphocyte. !$#cross-references MUID:91007274; PMID:2145197 !$#accession JT0553 !'##molecule_type mRNA !'##residues 1-333 ##label SAB !'##cross-references GB:M32599; NID:g193423; PIDN:AAA37659.1; !1PID:g309243 REFERENCE S14090 !$#authors Filipek, A.; Gerke, V.; Weber, K.; Kuznicki, J. !$#journal Eur. J. Biochem. (1991) 195:795-800 !$#title Characterization of the cell-cycle-regulated protein !1calcyclin from Ehrlich ascites tumor cells. Identification !1of two binding proteins obtained by Ca(2+)-dependent !1affinity chromatography. !$#cross-references MUID:91153321; PMID:1999197 !$#accession S14160 !'##molecule_type protein !'##residues 2-20,'FSCD',25-26,'D',28-64,'I',66-70,'F',72-77,'F',79-80, !1'VK',83-86,'D',88-154,'I',156-263,'A',265-304,'I',306-333 !1##label FIL CLASSIFICATION #superfamily glyceraldehyde-3-phosphate dehydrogenase KEYWORDS gluconeogenesis; glycolysis; homotetramer; NAD; !1oxidoreductase FEATURE !$2-333 #product glyceraldehyde-3-phosphate dehydrogenase !8#status experimental #label MAT\ !$3-33 #region beta-alpha-beta NAD nucleotide-binding fold\ !$150,177 #active_site Cys, His #status predicted SUMMARY #length 333 #molecular-weight 35810 #checksum 5233 SEQUENCE /// ENTRY DERTG #type complete TITLE glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) (EC 1.2.1.12) - rat ALTERNATE_NAMES triosephosphate dehydrogenase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Jun-2002 ACCESSIONS A23013; A22939; A22887; A23280; A17155; JN0401; A60208; !1B17155 REFERENCE A23013 !$#authors Fort, P.; Marty, L.; Piechaczyk, M.; El Sabrouty, S.; Dani, !1C.; Jeanteur, P.; Blanchard, J.M. !$#journal Nucleic Acids Res. (1985) 13:1431-1442 !$#title Various rat adult tissues express only one major mRNA !1species from the glyceraldehyde-3-phosphate-dehydrogenase !1multigenic family. !$#cross-references MUID:85215556; PMID:2987824 !$#accession A23013 !'##molecule_type mRNA !'##residues 1-333 ##label FOR !'##cross-references GB:X02231; NID:g56187; PIDN:CAA26150.1; PID:g56188 REFERENCE A93562 !$#authors Tso, J.Y.; Sun, X.H.; Kao, T.; Reece, K.S.; Wu, R. !$#journal Nucleic Acids Res. (1985) 13:2485-2502 !$#title Isolation and characterization of rat and human !1glyceraldehyde-3-phosphate dehydrogenase cDNAs: genomic !1complexity and molecular evolution of the gene. !$#cross-references MUID:85215629; PMID:2987855 !$#accession A22939 !'##molecule_type mRNA !'##residues 1-80,'AN',83-304,'F',306-333 ##label TSO !'##cross-references GB:M17701; NID:g204248; PIDN:AAA41193.1; !1PID:g204249 REFERENCE A22887 !$#authors Piechaczyk, M.; Blanchard, J.M.; Marty, L.; Dani, C.; !1Panabieres, F.; El Sabouty, S.; Fort, P.; Jeanteur, P. !$#journal Nucleic Acids Res. (1984) 12:6951-6963 !$#title Post-transcriptional regulation of !1glyceraldehyde-3-phosphate-dehydrogenase gene expression in !1rat tissues. !$#cross-references MUID:85014145; PMID:6548307 !$#accession A22887 !'##molecule_type mRNA !'##residues 261-323 ##label PIE !'##cross-references GB:X00972 REFERENCE A23280 !$#authors Maehara, Y.; Fujiyoshi, T.; Takahashi, K.; Yamamoto, M.; !1Endo, H. !$#journal Biochem. Biophys. Res. Commun. (1985) 131:800-805 !$#title 1.5 KB mRNA abundantly expressed in rat tumors encodes a 37 !1kilodalton protein in vitro. !$#cross-references MUID:86025533; PMID:2413848 !$#accession A23280 !'##molecule_type mRNA !'##residues 267-304,'F',306-333 ##label MAE !'##cross-references GB:M11561; NID:g205963; PIDN:AAA41795.1; !1PID:g205964 REFERENCE A90313 !$#authors Vospelnikova, N.D.; Safronova, M.I.; Shuvalova, E.R.; !1Baratova, L.A.; Kniazev, S.P.; Nagradova, N.K. !$#journal Biochem. J. (1981) 199:757-765 !$#title Identification of an arginine residue important for !1catalytic activity in the primary structure of !1D-glyceraldehyde 3-phosphate dehydrogenase. !$#cross-references MUID:82182080; PMID:7340828 !$#accession A17155 !'##molecule_type protein !'##residues 117-119,'N',121-122,'T',124-126,'Z',128,'LF',131-133, !1'BRZH',138,'SK';294-297,'T',299-301,'BZRF',306-307 ##label !1VOS REFERENCE JN0401 !$#authors Baibakov, B.A.; Zheltova, A.O.; Belyanova, L.P.; Baratova, !1L.A.; Vospelnikova, N.D.; Safronova, M.I. !$#journal Bioorg. Khim. (1977) 3:826-830 !$#title Peptide sequence containing the active site cysteine of !1D-glyceraldehyde-3-phosphate dehydrohenase from rat skeletal !1muscles. !$#accession JN0401 !'##molecule_type protein !'##residues 144-160 ##label BAI !'##experimental_source skeletal muscle REFERENCE A60208 !$#authors Leung, T.K.C.; Hall, C.; Monfries, C.; Lim, L. !$#journal J. Neurochem. (1987) 49:232-238 !$#title Trifluoperazine activates and releases latent ATP-generating !1enzymes associated with the synaptic plasma membrane. !$#cross-references MUID:87224934; PMID:3585333 !$#accession A60208 !'##status preliminary; translation not shown !'##molecule_type mRNA !'##residues 235-304,'F',306-333 ##label LEU !'##cross-references GB:M29341; NID:g203141; PIDN:AAA40814.1; !1PID:g203142 !'##experimental_source brain CLASSIFICATION #superfamily glyceraldehyde-3-phosphate dehydrogenase KEYWORDS gluconeogenesis; glycolysis; homotetramer; NAD; !1oxidoreductase FEATURE !$3-33 #region beta-alpha-beta NAD nucleotide-binding fold\ !$150 #active_site Cys #status experimental\ !$177 #active_site His #status predicted SUMMARY #length 333 #molecular-weight 35836 #checksum 4410 SEQUENCE /// ENTRY DECHG3 #type complete TITLE glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) (EC 1.2.1.12) - chicken ALTERNATE_NAMES GAP dehydrogenase ORGANISM #formal_name Gallus gallus #common_name chicken DATE 03-Aug-1984 #sequence_revision 30-Sep-1989 #text_change 03-Jun-2002 ACCESSIONS A00368; A32737; A22035; I50231; I50640 REFERENCE A00368 !$#authors Dugaiczyk, A.; Haron, J.A.; Stone, E.M.; Dennison, O.E.; !1Rothblum, K.N.; Schwartz, R.J. !$#journal Biochemistry (1983) 22:1605-1613 !$#title Cloning and sequencing of a deoxyribonucleic acid copy of !1glyceraldehyde-3-phosphate dehydrogenase messenger !1ribonucleic acid isolated from chicken muscle. !$#cross-references MUID:83204759; PMID:6303388 !$#accession A00368 !'##molecule_type mRNA !'##residues 1-333 ##label DUG !'##cross-references GB:V00407; GB:J00849; NID:g63402; PIDN:CAA23698.1; !1PID:g1628381 REFERENCE A32737 !$#authors Panabieres, F.; Piechaczyk, M.; Rainer, B.; Dani, C.; Fort, !1P.; Riaad, S.; Marty, L.; Imbach, J.L.; Jeanteur, P.; !1Blanchard, J.M. !$#journal Biochem. Biophys. Res. Commun. (1984) 118:767-773 !$#title Complete nucleotide sequence of the messenger RNA coding for !1chicken muscle glyceraldehyde-3-phosphate dehydrogenase. !$#cross-references MUID:84153854; PMID:6322764 !$#accession A32737 !'##status preliminary !'##molecule_type mRNA !'##residues 1-333 ##label PAN !'##cross-references GB:K01458; NID:g211800; PIDN:AAA48778.1; !1PID:g211801 REFERENCE A22035 !$#authors Stone, E.M.; Rothblum, K.N.; Alevy, M.C.; Kuo, T.M.; !1Schwartz, R.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:1628-1632 !$#title Complete sequence of the chicken glyceraldehyde-3-phosphate !1dehydrogenase gene. !$#cross-references MUID:85166184; PMID:3856841 !$#accession A22035 !'##molecule_type DNA !'##residues 1-293,'H',295-333 ##label STO !'##cross-references GB:M11213; NID:g211796; PIDN:AAA48774.1; !1PID:g211797 !'##note the authors translated the codon CAT for residue 294 as Asp REFERENCE I50231 !$#authors Arnold, H.H.; Domdey, H.; Wiebauer, K.; Datta, K.; Siddiqui, !1M.A.Q. !$#journal J. Biol. Chem. (1982) 257:9872-9877 !$#title Cloning, partial sequencing, and expression of !1glyceraldehyde-3-phosphate dehydrogenase gene in chick !1embryonic heart muscle cells. !$#cross-references MUID:82265644; PMID:6179937 !$#accession I50231 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 'G',198-276,'E',278-333 ##label ARN !'##cross-references GB:J00848; NID:g211798; PIDN:AAA48777.1; !1PID:g211799 !$#accession I50640 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 'G',198-276,'E',278-328,'T',330-333 ##label AR2 !'##cross-references EMBL:V00406; NID:g63400; PIDN:CAA23697.1; !1PID:g63401 GENETICS !$#introns 8/2; 41/3; 77/3; 107/3; 146/2; 173/3; 224/2; 250/3; 278/3; !1311/2 CLASSIFICATION #superfamily glyceraldehyde-3-phosphate dehydrogenase KEYWORDS gluconeogenesis; glycolysis; homotetramer; NAD; !1oxidoreductase FEATURE !$2-333 #product glyceraldehyde-3-phosphate dehydrogenase !8#status predicted #label MAT\ !$3-33 #region beta-alpha-beta NAD nucleotide-binding fold\ !$150,177 #active_site Cys, His #status predicted SUMMARY #length 333 #molecular-weight 35762 #checksum 3868 SEQUENCE /// ENTRY DEKWG1 #type complete TITLE glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) (EC 1.2.1.12) 1 - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 03-Jun-2002 ACCESSIONS S03911; T24754 REFERENCE S03911 !$#authors Huang, X.Y.; Barrios, L.A.M.; Vonkhorporn, P.; Honda, S.; !1Albertson, D.G.; Hecht, R.M. !$#journal J. Mol. Biol. (1989) 206:411-424 !$#title Genomic organization of the glyceraldehyde-3-phosphate !1dehydrogenase gene family of Caenorhabditis elegans. !$#cross-references MUID:89236409; PMID:2716055 !$#accession S03911 !'##molecule_type DNA !'##residues 1-341 ##label HUA !'##cross-references EMBL:X52674; NID:g6741; PIDN:CAA36900.1; PID:g6742 REFERENCE Z19932 !$#authors Lloyd, C. !$#submission submitted to the EMBL Data Library, April 1995 !$#accession T24754 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-341 ##label WIL !'##cross-references EMBL:Z49070; PIDN:CAA88870.1; GSPDB:GN00020; !1CESP:T09F3.3 !'##experimental_source clone T09F3 GENETICS !$#gene gpd-1 !$#map_position 2 !$#introns 175/1; 319/2 CLASSIFICATION #superfamily glyceraldehyde-3-phosphate dehydrogenase KEYWORDS gluconeogenesis; glycolysis; homotetramer; NAD; !1oxidoreductase FEATURE !$5-35 #region beta-alpha-beta NAD nucleotide-binding fold\ !$158,185 #active_site Cys, His #status predicted SUMMARY #length 341 #molecular-weight 36382 #checksum 2218 SEQUENCE /// ENTRY DEKWG4 #type complete TITLE glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) (EC 1.2.1.12) 4 - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 03-Jun-2002 ACCESSIONS S03912; T21704 REFERENCE S03911 !$#authors Huang, X.Y.; Barrios, L.A.M.; Vonkhorporn, P.; Honda, S.; !1Albertson, D.G.; Hecht, R.M. !$#journal J. Mol. Biol. (1989) 206:411-424 !$#title Genomic organization of the glyceraldehyde-3-phosphate !1dehydrogenase gene family of Caenorhabditis elegans. !$#cross-references MUID:89236409; PMID:2716055 !$#accession S03912 !'##molecule_type DNA !'##residues 1-341 ##label HUA !'##cross-references EMBL:X52673; NID:g6746; PIDN:CAA36899.1; PID:g6747 REFERENCE Z19462 !$#authors Wilkinson, J. !$#submission submitted to the EMBL Data Library, March 1995 !$#accession T21704 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-341 ##label WIL !'##cross-references EMBL:Z48783; PIDN:CAA88697.1; GSPDB:GN00020; !1CESP:F33H1.2 !'##experimental_source clone F33H1 GENETICS !$#gene gpd-4 !$#map_position 2 !$#introns 175/1; 319/2 CLASSIFICATION #superfamily glyceraldehyde-3-phosphate dehydrogenase KEYWORDS gluconeogenesis; glycolysis; homotetramer; NAD; !1oxidoreductase FEATURE !$5-35 #region beta-alpha-beta NAD nucleotide-binding fold\ !$158,185 #active_site Cys, His #status predicted SUMMARY #length 341 #molecular-weight 36426 #checksum 2053 SEQUENCE /// ENTRY DEKWG2 #type complete TITLE glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) (EC 1.2.1.12) 2 - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 03-Jun-2002 ACCESSIONS S03913 REFERENCE S03911 !$#authors Huang, X.Y.; Barrios, L.A.M.; Vonkhorporn, P.; Honda, S.; !1Albertson, D.G.; Hecht, R.M. !$#journal J. Mol. Biol. (1989) 206:411-424 !$#title Genomic organization of the glyceraldehyde-3-phosphate !1dehydrogenase gene family of Caenorhabditis elegans. !$#cross-references MUID:89236409; PMID:2716055 !$#accession S03913 !'##molecule_type DNA !'##residues 1-341 ##label HUA !'##cross-references EMBL:X15254; NID:g6743; PIDN:CAA33326.1; PID:g6744 GENETICS !$#gene gpd-2 !$#map_position X !$#introns 80/3; 123/3 CLASSIFICATION #superfamily glyceraldehyde-3-phosphate dehydrogenase KEYWORDS gluconeogenesis; glycolysis; homotetramer; NAD; !1oxidoreductase FEATURE !$5-35 #region beta-alpha-beta NAD nucleotide-binding fold\ !$158,185 #active_site Cys, His #status predicted SUMMARY #length 341 #molecular-weight 36498 #checksum 9062 SEQUENCE /// ENTRY DEKWG3 #type complete TITLE glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) (EC 1.2.1.12) 3 - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 03-Jun-2002 ACCESSIONS S03914; T16610; T16611 REFERENCE S03911 !$#authors Huang, X.Y.; Barrios, L.A.M.; Vonkhorporn, P.; Honda, S.; !1Albertson, D.G.; Hecht, R.M. !$#journal J. Mol. Biol. (1989) 206:411-424 !$#title Genomic organization of the glyceraldehyde-3-phosphate !1dehydrogenase gene family of Caenorhabditis elegans. !$#cross-references MUID:89236409; PMID:2716055 !$#accession S03914 !'##molecule_type DNA !'##residues 1-341 ##label HUA !'##cross-references EMBL:X15254; NID:g6743; PIDN:CAA33327.1; PID:g6745 REFERENCE Z18546 !$#authors Gattung, S. !$#submission submitted to the EMBL Data Library, February 1996 !$#description The sequence of C. elegans cosmid K10B3. !$#accession T16610 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-341 ##label GA1 !'##cross-references EMBL:U49941; NID:g1206038; PID:g1206039; !1PIDN:AAB53869.1; GSPDB:GN00028 !'##experimental_source strain Bristol N2; clone K10B3 !$#accession T16611 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1,'P',3-341 ##label GA2 !'##cross-references EMBL:U49941; NID:g1206038; PID:g1206046; !1PIDN:AAB53874.1; GSPDB:GN00028; CESP:gpd-2 !'##experimental_source strain Bristol N2; clone K10B3 GENETICS GAT !$#gene gpd-3 GENETICS GN2 !$#gene CESP:gpd-2 !$#map_position X !$#introns 80/3; 123/3 CLASSIFICATION #superfamily glyceraldehyde-3-phosphate dehydrogenase KEYWORDS gluconeogenesis; glycolysis; homotetramer; NAD; !1oxidoreductase FEATURE !$5-35 #region beta-alpha-beta NAD nucleotide-binding fold\ !$158,185 #active_site Cys, His #status predicted SUMMARY #length 341 #molecular-weight 36459 #checksum 9653 SEQUENCE /// ENTRY DELOG3 #type complete TITLE glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) (EC 1.2.1.12) - American lobster ORGANISM #formal_name Homarus americanus #common_name American lobster DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 03-Jun-2002 ACCESSIONS A00369 REFERENCE A93153 !$#authors Davidson, B.E.; Sajgo, M.; Noller, H.F.; Harris, J.I. !$#journal Nature (1967) 216:1181-1185 !$#title Amino-acid sequence of glyceraldehyde 3-phosphate !1dehydrogenase from lobster muscle. !$#cross-references MUID:68098010; PMID:4294736 !$#accession A00369 !'##molecule_type protein !'##residues 1-333 ##label DAV !'##note the source species is not provided by the authors REFERENCE A92188 !$#authors Moras, D.; Olsen, K.W.; Sabesan, M.N.; Buehner, M.; Ford, !1G.C.; Rossmann, M.G. !$#journal J. Biol. Chem. (1975) 250:9137-9162 !$#title Studies of asymmetry in the three-dimensional structure of !1lobster D-glyceraldehyde-3-phosphate dehydrogenase. !$#cross-references MUID:76069246; PMID:127793 !$#contents annotation; X-ray crystallography, 2.9 angstroms !$#note the source species is not provided by the authors REFERENCE A44655 !$#authors Allison, W.S.; Kaplan, N.O. !$#journal J. Biol. Chem. (1964) 239:2140-2152 !$#title The comparative enzymology of triosephosphate dehydrogenase. !$#contents annotation; source CLASSIFICATION #superfamily glyceraldehyde-3-phosphate dehydrogenase KEYWORDS acetylated amino end; gluconeogenesis; glycolysis; !1homotetramer; NAD; oxidoreductase FEATURE !$2-31 #region beta-alpha-beta NAD nucleotide-binding fold\ !$1 #modified_site acetylated amino end (Ser) #status !8experimental\ !$148,175 #active_site Cys, His #status experimental SUMMARY #length 333 #molecular-weight 35717 #checksum 4046 SEQUENCE /// ENTRY DEUSGM #type complete TITLE glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) (EC 1.2.1.12) - smut fungus (Ustilago maydis) ORGANISM #formal_name Ustilago maydis #common_name corn smut DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 03-Jun-2002 ACCESSIONS JN0096; S03111 REFERENCE JN0096 !$#authors Smith, T.L.; Leong, S.A. !$#journal Gene (1990) 93:111-117 !$#title Isolation and characterization of a Ustilago maydis !1glyceraldehyde-3-phosphate dehydrogenase-encoding gene. !$#cross-references MUID:91033000; PMID:2227419 !$#accession JN0096 !'##molecule_type DNA !'##residues 1-337 ##label SMI !'##cross-references GB:X07879; NID:g5218; PIDN:CAA30726.1; PID:g5219 GENETICS !$#gene gapd !$#introns 10/2 CLASSIFICATION #superfamily glyceraldehyde-3-phosphate dehydrogenase KEYWORDS gluconeogenesis; glycolysis; homotetramer; NAD; !1oxidoreductase FEATURE !$5-35 #region beta-alpha-beta NAD nucleotide-binding fold\ !$152,179 #active_site Cys, His #status predicted SUMMARY #length 337 #molecular-weight 35913 #checksum 3159 SEQUENCE /// ENTRY DEJNGI #type complete TITLE glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) (EC 1.2.1.12) - Phytophthora infestans ORGANISM #formal_name Phytophthora infestans #common_name potato late blight agent DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 03-Jun-2002 ACCESSIONS S22487; S19220 REFERENCE S22487 !$#authors Moon, R.P.; Unkles, S.E.; Duncan, J.M.; Hawkins, A.R.; !1Kinghorn, J.R. !$#journal Plant Mol. Biol. (1992) 18:1209-1211 !$#title Sequence of the Phytophthora infestans !1glyceraldehyde-3-phosphate dehydrogenase-encoding gene !1(gpdA). !$#cross-references MUID:92288319; PMID:1600159 !$#accession S22487 !'##molecule_type DNA !'##residues 1-332 ##label MOO !'##cross-references EMBL:X64537 !'##note the authors did not translate the codon for residue 1 GENETICS !$#gene gpdA !$#start_codon GTG CLASSIFICATION #superfamily glyceraldehyde-3-phosphate dehydrogenase KEYWORDS gluconeogenesis; glycolysis; homotetramer; NAD; !1oxidoreductase FEATURE !$2-32 #region beta-alpha-beta NAD nucleotide-binding fold\ !$149,176 #active_site Cys, His #status predicted SUMMARY #length 332 #molecular-weight 36117 #checksum 5373 SEQUENCE /// ENTRY DEJJGC #type complete TITLE glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) (EC 1.2.1.12) - chestnut blight fungus ORGANISM #formal_name Cryphonectria parasitica, Endothia parasitica #common_name chestnut blight fungus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Jun-2002 ACCESSIONS S11447 REFERENCE S11447 !$#authors Choi, G.H.; Nuss, D.L. !$#journal Nucleic Acids Res. (1990) 18:5566 !$#title Nucleotide sequence of the glyceraldehyde-3-phosphate !1dehydrogenase gene from Cryphonectria parasitica. !$#cross-references MUID:91016863; PMID:2216743 !$#accession S11447 !'##molecule_type DNA !'##residues 1-337 ##label CHO !'##cross-references EMBL:X53996; NID:g2638; PIDN:CAA37943.1; !1PID:g295939 GENETICS !$#gene gpd-1 !$#introns 42/3; 271/1 CLASSIFICATION #superfamily glyceraldehyde-3-phosphate dehydrogenase KEYWORDS gluconeogenesis; glycolysis; homotetramer; NAD; !1oxidoreductase FEATURE !$4-34 #region beta-alpha-beta NAD nucleotide-binding fold\ !$151,178 #active_site Cys, His #status predicted SUMMARY #length 337 #molecular-weight 36194 #checksum 1665 SEQUENCE /// ENTRY DEYDGC #type complete TITLE glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) (EC 1.2.1.12) - fungus (Curvularia lunata) ORGANISM #formal_name Curvularia lunata DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 03-Jun-2002 ACCESSIONS S17981 REFERENCE S17981 !$#authors Osiewacz, H.D.; Ridder, R. !$#journal Curr. Genet. (1991) 20:151-155 !$#title Genome analysis of imperfect fungi: electrophoretic !1karyotyping and characterization of the nuclear gene coding !1for glyceraldehyde-3-phosphate dehydrogenase (gpd) of !1Curvularia lunata. !$#cross-references MUID:92035062; PMID:1934112 !$#accession S17981 !'##molecule_type DNA !'##residues 1-337 ##label OSI !'##cross-references EMBL:X58718; NID:g2600; PIDN:CAA41554.1; PID:g2601 GENETICS !$#gene gpd !$#introns 4/3; 21/2; 42/3; 271/1 CLASSIFICATION #superfamily glyceraldehyde-3-phosphate dehydrogenase KEYWORDS gluconeogenesis; glycolysis; homotetramer; NAD; !1oxidoreductase FEATURE !$4-34 #region beta-alpha-beta NAD nucleotide-binding fold\ !$151,178 #active_site Cys, His #status predicted SUMMARY #length 337 #molecular-weight 36549 #checksum 3963 SEQUENCE /// ENTRY DEASG3 #type complete TITLE glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) (EC 1.2.1.12) - Emericella nidulans ALTERNATE_NAMES triosephosphate dehydrogenase ORGANISM #formal_name Emericella nidulans, Aspergillus nidulans DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Jun-2002 ACCESSIONS JT0344 REFERENCE JT0344 !$#authors Punt, P.J.; Dingemanse, M.A.; Jacobs-Meijsing, B.J.M.; !1Pouwels, P.H.; van den Hondel, C.A.M.J.J. !$#journal Gene (1988) 69:49-57 !$#title Isolation and characterization of the !1glyceraldehyde-3-phosphate dehydrogenase gene of Aspergillus !1nidulans. !$#cross-references MUID:89137994; PMID:3066699 !$#accession JT0344 !'##molecule_type DNA !'##residues 1-336 ##label PUN !'##cross-references GB:M19694; GB:M22758; NID:g168048; PIDN:AAA33307.1; !1PID:g168049 !'##note the authors translated the codon ACC for residue 328 as Ser GENETICS !$#gene gpdA !$#introns 4/3; 16/3; 21/2; 42/3; 271/1; 328/1 CLASSIFICATION #superfamily glyceraldehyde-3-phosphate dehydrogenase KEYWORDS glycolysis; homotetramer; NAD; oxidoreductase FEATURE !$4-34 #region beta-alpha-beta NAD nucleotide-binding fold\ !$151,178 #active_site Cys, His #status predicted SUMMARY #length 336 #molecular-weight 36311 #checksum 58 SEQUENCE /// ENTRY DEBYG1 #type complete TITLE glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) (EC 1.2.1.12) 2 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein J1433; protein YJR009c ORGANISM #formal_name Saccharomyces cerevisiae DATE 14-Nov-1983 #sequence_revision 08-Sep-1995 #text_change 03-Jun-2002 ACCESSIONS S57024; S40915; S55197; A00370; S17014 REFERENCE S56771 !$#authors de Haan, M.; Grivell, L.A.; Smits, P.H.M. !$#submission submitted to the Protein Sequence Database, September 1995 !$#accession S57024 !'##molecule_type DNA !'##residues 1-332 ##label ZAG !'##cross-references EMBL:Z49509; NID:g1015635; PIDN:CAA89531.1; !1PID:g1015636; GSPDB:GN00010; MIPS:YJR009c REFERENCE S40915 !$#authors Mountain, H.A.; Korch, C. !$#journal Yeast (1991) 7:873-880 !$#title TDH2 is linked to MET3 on chromosome X of Saccharomyces !1cerevisiae. !$#cross-references MUID:92160396; PMID:1789010 !$#accession S40915 !'##molecule_type DNA !'##residues 1-332 ##label MOU !'##cross-references EMBL:X60157; NID:g3935; PIDN:CAA42725.1; PID:g3936 !'##experimental_source strain S288C REFERENCE S55183 !$#authors de Haan, M.; Smits, P.H.M.; Grivell, L.A. !$#submission submitted to the EMBL Data Library, May 1995 !$#accession S55197 !'##molecule_type DNA !'##residues 1-332 ##label DEH !'##cross-references EMBL:X87611; NID:g854567; PIDN:CAA60931.1; !1PID:g854582 REFERENCE A00370 !$#authors Holland, J.P.; Holland, M.J. !$#journal J. Biol. Chem. (1980) 255:2596-2605 !$#title Structural comparison of two nontandemly repeated yeast !1glyceraldehyde-3-phosphate dehydrogenase genes. !$#cross-references MUID:80137492; PMID:6244283 !$#accession A00370 !'##molecule_type mRNA !'##residues 1-241,'B',243-332 ##label HOL !'##cross-references EMBL:V01301; NID:g3723; PIDN:CAA24608.1; PID:g3724 GENETICS !$#gene SGD:TDH2; GPD2; MIPS:YJR009c !'##cross-references SGD:S0003769; MIPS:YJR009c !$#map_position 10R CLASSIFICATION #superfamily glyceraldehyde-3-phosphate dehydrogenase KEYWORDS gluconeogenesis; glycolysis; homotetramer; NAD; !1oxidoreductase FEATURE !$2-332 #product glyceraldehyde-3-phosphate dehydrogenase !8#status predicted #label MAT\ !$3-33 #region beta-alpha-beta NAD nucleotide-binding fold\ !$150,177 #active_site Cys, His #status predicted SUMMARY #length 332 #molecular-weight 35847 #checksum 903 SEQUENCE /// ENTRY DEBYG2 #type complete TITLE glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) (EC 1.2.1.12) 3 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein G7576; protein YGR192c ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Jul-1980 #sequence_revision 08-Sep-1995 #text_change 03-Jun-2002 ACCESSIONS S55870; A00371; S64510 REFERENCE S55869 !$#authors Arroyo, J.; Garcia-Gonzalez, M.; Garcia-Saez, M.I.; Sanchez, !1M.; Nombela, C. !$#journal Yeast (1995) 11:587-591 !$#title The complete sequence of a 9037 bp DNA fragment of the right !1arm of Saccharomyces cerevisiae chromosome VII. !$#cross-references MUID:95373283; PMID:7645350 !$#accession S55870 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-332 ##label ARR !'##cross-references EMBL:X82408; NID:g755795; PIDN:CAA57803.1; !1PID:g755797 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1994 REFERENCE A00371 !$#authors Holland, J.P.; Holland, M.J. !$#journal J. Biol. Chem. (1979) 254:9839-9845 !$#title The primary structure of a glyceraldehyde-3-phosphate !1dehydrogenase gene from Saccharomyces cerevisiae. !$#cross-references MUID:80027306; PMID:385592 !$#accession A00371 !'##molecule_type mRNA !'##residues 1-135,'V',137-247,'D',249-328,'I',330-332 ##label HOL !'##cross-references EMBL:V01300; NID:g3719; PIDN:CAA24607.1; PID:g3720 REFERENCE S64499 !$#authors Arroyo, J.; Garcia-Gonzalez, M.; Garcia-Saez, M.I.; !1Sanchez-Perez, M.; Nombela, C. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64510 !'##molecule_type DNA !'##residues 1-332 ##label ARW !'##cross-references EMBL:Z72977; NID:g1323340; PIDN:CAA97218.1; !1PID:g1323341; GSPDB:GN00007; MIPS:YGR192c !'##experimental_source strain S288C GENETICS !$#gene SGD:TDH3; GPD3; MIPS:YGR192c !'##cross-references SGD:S0003424; MIPS:YGR192c !$#map_position 7R CLASSIFICATION #superfamily glyceraldehyde-3-phosphate dehydrogenase KEYWORDS gluconeogenesis; glycolysis; homotetramer; NAD; !1oxidoreductase FEATURE !$2-332 #product glyceraldehyde-3-phosphate dehydrogenase !8#status predicted #label MAT\ !$3-33 #region beta-alpha-beta NAD nucleotide-binding fold\ !$150,177 #active_site Cys, His #status predicted SUMMARY #length 332 #molecular-weight 35746 #checksum 1733 SEQUENCE /// ENTRY DEBYG3 #type complete TITLE glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) (EC 1.2.1.12) 1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein J1154; protein YJL052w ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Jul-1980 #sequence_revision 08-Sep-1995 #text_change 03-Jun-2002 ACCESSIONS S56824; A00372 REFERENCE S56793 !$#authors Pohl, T.M.; Aljinovic, G. !$#submission submitted to the Protein Sequence Database, September 1995 !$#accession S56824 !'##molecule_type DNA !'##residues 1-332 ##label TOV !'##cross-references EMBL:Z49327; NID:g1008188; PIDN:CAA89343.1; !1PID:g1008189; GSPDB:GN00010; MIPS:YJL052w REFERENCE A00372 !$#authors Holland, J.P.; Labieniec, L.; Swimmer, C.; Holland, M.J. !$#journal J. Biol. Chem. (1983) 258:5291-5299 !$#title Homologous nucleotide sequences at the 5' termini of !1messenger RNAs synthesized from the yeast enolase and !1glyceraldehyde-3-phosphate dehydrogenase gene families. !$#cross-references MUID:83161156; PMID:6833300 !$#accession A00372 !'##molecule_type mRNA !'##residues 1-31,'DN',34-247,'A',249-323,'N',325-332 ##label HOL !'##cross-references EMBL:V01302 GENETICS !$#gene SGD:TDH1; GPD1; MIPS:YJL052w !'##cross-references SGD:S0003588; MIPS:YJL052w !$#map_position 10L CLASSIFICATION #superfamily glyceraldehyde-3-phosphate dehydrogenase KEYWORDS gluconeogenesis; glycolysis; homotetramer; NAD; !1oxidoreductase FEATURE !$2-332 #product glyceraldehyde-3-phosphate dehydrogenase !8#status predicted #label MAT\ !$3-33 #region beta-alpha-beta NAD nucleotide-binding fold\ !$150,177 #active_site Cys, His #status predicted SUMMARY #length 332 #molecular-weight 35750 #checksum 2410 SEQUENCE /// ENTRY DEVKGL #type complete TITLE glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) (EC 1.2.1.12) - yeast (Kluyveromyces marxianus var. lactis) ORGANISM #formal_name Kluyveromyces marxianus var. lactis, Candida sphaerica DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 03-Jun-2002 ACCESSIONS S12721 REFERENCE S12721 !$#authors Shuster, J.R. !$#journal Nucleic Acids Res. (1990) 18:4271 !$#title Kluyveromyces lactis glyceraldehyde-3-phosphate !1dehydrogenase and alcohol dehydrogenase-1 genes are linked !1and divergently transcribed. !$#cross-references MUID:90332443; PMID:2377477 !$#accession S12721 !'##molecule_type DNA !'##residues 1-329 ##label SHU !'##cross-references EMBL:X52871; NID:g2823; PIDN:CAA37051.1; PID:g2824 GENETICS !$#gene GAP1 CLASSIFICATION #superfamily glyceraldehyde-3-phosphate dehydrogenase KEYWORDS gluconeogenesis; glycolysis; homotetramer; NAD; !1oxidoreductase FEATURE !$3-33 #region beta-alpha-beta NAD nucleotide-binding fold\ !$149,176 #active_site Cys, His #status predicted SUMMARY #length 329 #molecular-weight 35324 #checksum 1236 SEQUENCE /// ENTRY DEKZGR #type complete TITLE glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) (EC 1.2.1.12) - yeast (Zygosaccharomyces rouxii) ORGANISM #formal_name Zygosaccharomyces rouxii, Candida mogii DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 03-Jun-2002 ACCESSIONS S00152 REFERENCE S00152 !$#authors Imura, T.; Utatsu, I.; Toh-e, A. !$#journal Agric. Biol. Chem. (1987) 51:1641-1647 !$#title Glyceraldehyde-3-phosphate dehydrogenase genes of !1Zygosaccharomyces rouxii: the source of a promoter for a !1host-vector system for Z. rouxii. !$#accession S00152 !'##molecule_type DNA !'##residues 1-333 ##label IMU !'##cross-references EMBL:D00134; NID:g218528; PIDN:BAA00081.1; !1PID:g218529 CLASSIFICATION #superfamily glyceraldehyde-3-phosphate dehydrogenase KEYWORDS gluconeogenesis; glycolysis; homotetramer; NAD; !1oxidoreductase FEATURE !$3-33 #region beta-alpha-beta NAD nucleotide-binding fold\ !$150,177 #active_site Cys, His #status predicted SUMMARY #length 333 #molecular-weight 35601 #checksum 3670 SEQUENCE /// ENTRY DEUT1C #type complete TITLE glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) (EC 1.2.1.12), glycosomal - Trypanosoma cruzi ORGANISM #formal_name Trypanosoma cruzi DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Jun-2002 ACCESSIONS S12565; S16508 REFERENCE S12565 !$#authors Kendall, G.; Wilderspin, A.F.; Ashall, F.; Miles, M.A.; !1Kelly, J.M. !$#journal EMBO J. (1990) 9:2751-2758 !$#title Trypanosoma cruzi glycosomal glyceraldehyde-3-phosphate !1dehydrogenase does not conform to the 'hotspot' topogenic !1signal model. !$#cross-references MUID:90360985; PMID:2167831 !$#accession S12565 !'##molecule_type DNA !'##residues 1-359 ##label KEN1 !'##cross-references EMBL:X52898; NID:g10607; PIDN:CAA37079.1; !1PID:g10608 !$#accession S16508 !'##molecule_type DNA !'##residues 1-359 ##label KEN2 !'##cross-references EMBL:X52898; NID:g10607; PIDN:CAA37079.1; !1PID:g10608 GENETICS !$#introns #status absent !$#note tandem genes GAPDH I and II are identical within the !1protein-coding region at the nucleotide level CLASSIFICATION #superfamily glyceraldehyde-3-phosphate dehydrogenase KEYWORDS gluconeogenesis; glycolysis; glycosome; homotetramer; NAD; !1oxidoreductase FEATURE !$4-38 #region beta-alpha-beta NAD nucleotide-binding fold\ !$166,194 #active_site Cys, His #status predicted SUMMARY #length 359 #molecular-weight 39060 #checksum 3897 SEQUENCE /// ENTRY DEUT1B #type complete TITLE glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) (EC 1.2.1.12), glycosomal - Trypanosoma brucei ORGANISM #formal_name Trypanosoma brucei DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Jun-2002 ACCESSIONS S18806; S18807; S19071 REFERENCE S18806 !$#authors Michels, P.A.M.; Poliszczak, A.; Osinga, K.A.; Misset, O.; !1van Beeumen, J.; Wierenga, R.K.; Borst, P.; Opperdoes, F.R. !$#journal EMBO J. (1986) 5:1049-1056 !$#title Two tandemly linked identical genes code for the glycosomal !1glyceraldehyde-phosphate dehydrogenase in Trypanosoma !1brucei. !$#cross-references MUID:86247562; PMID:3013612 !$#accession S18806 !'##molecule_type DNA !'##residues 1-359 ##label MIC !'##cross-references EMBL:X59955; NID:g11009; PIDN:CAA42576.1; !1PID:g11010 !'##experimental_source strain 427 !'##genetics GA1 !$#accession S18807 !'##molecule_type DNA !'##residues 1-359 ##label MIA !'##cross-references EMBL:X59955; NID:g11009; PIDN:CAA42576.1; !1PID:g11010 !'##experimental_source strain 427 !'##genetics GA2 !$#accession S19071 !'##molecule_type protein !'##residues 2-21,'X',23-48,'X',50-53 ##label MIC2 GENETICS GA1 !$#gene GAPDH1 GENETICS GA2 !$#gene GAPDH2 CLASSIFICATION #superfamily glyceraldehyde-3-phosphate dehydrogenase KEYWORDS glycolysis; glycosome; homotetramer; NAD; oxidoreductase FEATURE !$2-359 #product glyceraldehyde-3-phosphate dehydrogenase !8#status experimental #label MAT\ !$4-38 #region beta-alpha-beta NAD nucleotide-binding fold\ !$166,194 #active_site Cys, His #status predicted SUMMARY #length 359 #molecular-weight 39037 #checksum 3474 SEQUENCE /// ENTRY DEZMGC #type complete TITLE glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) (EC 1.2.1.12) C, cytosolic - maize ORGANISM #formal_name Zea mays #common_name maize DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 03-Jun-2002 ACCESSIONS S00354; S06879 REFERENCE S00353 !$#authors Brinkmann, H.; Martinez, P.; Quigley, F.; Martin, W.; Cerff, !1R. !$#journal J. Mol. Evol. (1987) 26:320-328 !$#title Endosymbiotic origin and codon bias of the nuclear gene for !1chloroplast glyceraldehyde-3-phosphate dehydrogenase from !1maize. !$#cross-references MUID:88230473; PMID:3131533 !$#accession S00354 !'##molecule_type mRNA !'##residues 1-337 ##label BRI !'##cross-references EMBL:X07156; NID:g22237; PIDN:CAA30151.1; !1PID:g22238 REFERENCE S06879 !$#authors Martinez, P.; Martin, W.; Cerff, R. !$#journal J. Mol. Biol. (1989) 208:551-565 !$#title Structure, evolution and anaerobic regulation of a nuclear !1gene encoding cytosolic glyceraldehyde-3-phosphate !1dehydrogenase from maize. !$#cross-references MUID:90040690; PMID:2810356 !$#accession S06879 !'##molecule_type DNA !'##residues 1-335,'T',337 ##label MAR !'##cross-references EMBL:X15596; NID:g22302; PIDN:CAA33620.1; !1PID:g295853 GENETICS !$#gene Gpc1 !$#introns 2/1; 10/1; 43/3; 82/2; 115/3; 164/3; 185/1; 217/3; 265/2; !1293/2 CLASSIFICATION #superfamily glyceraldehyde-3-phosphate dehydrogenase KEYWORDS gluconeogenesis; glycolysis; homotetramer; NAD; !1oxidoreductase FEATURE !$5-35 #region beta-alpha-beta NAD nucleotide-binding fold\ !$154,181 #active_site Cys, His #status predicted SUMMARY #length 337 #molecular-weight 36508 #checksum 2992 SEQUENCE /// ENTRY DEBHG #type complete TITLE glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) (EC 1.2.1.12) - barley ORGANISM #formal_name Hordeum vulgare #common_name barley DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Jun-2002 ACCESSIONS S18482 REFERENCE S17991 !$#authors Martin, W.; Gierl, A.; Saedler, H. !$#journal Nature (1989) 339:46-48 !$#title Molecular evidence for pre-Cretaceous angiosperm origins. !$#accession S18482 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type mRNA !'##residues 1-337 ##label MAR !'##cross-references EMBL:X60343; NID:g18977; PIDN:CAA42901.1; !1PID:g18978 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1May 1991 CLASSIFICATION #superfamily glyceraldehyde-3-phosphate dehydrogenase KEYWORDS gluconeogenesis; glycolysis; homotetramer; NAD; !1oxidoreductase FEATURE !$5-35 #region beta-alpha-beta NAD nucleotide-binding fold\ !$154,181 #active_site Cys, His #status predicted SUMMARY #length 337 #molecular-weight 36513 #checksum 3593 SEQUENCE /// ENTRY DEIS3C #type complete TITLE glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) (EC 1.2.1.12), cytosolic - white mustard ALTERNATE_NAMES triosephosphate dehydrogenase ORGANISM #formal_name Sinapis alba #common_name white mustard DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Jun-2002 ACCESSIONS A24796 REFERENCE A24796 !$#authors Martin, W.; Cerff, R. !$#journal Eur. J. Biochem. (1986) 159:323-331 !$#title Prokaryotic features of a nucleus-encoded enzyme. cDNA !1sequences for chloroplast and cytosolic !1glyceraldehyde-3-phosphate dehydrogenases from mustard !1(Sinapis alba). !$#cross-references MUID:87004643; PMID:3530755 !$#accession A24796 !'##molecule_type mRNA !'##residues 1-338 ##label MAR !'##cross-references GB:X04301; NID:g21142; PIDN:CAA27844.1; PID:g21143 CLASSIFICATION #superfamily glyceraldehyde-3-phosphate dehydrogenase KEYWORDS gluconeogenesis; glycolysis; homotetramer; NAD; !1oxidoreductase FEATURE !$2-338 #product glyceraldehyde-3-phosphate dehydrogenase !8#status experimental #label MAT\ !$7-37 #region beta-alpha-beta NAD nucleotide-binding fold\ !$156,183 #active_site Cys, His #status predicted SUMMARY #length 338 #molecular-weight 36924 #checksum 8083 SEQUENCE /// ENTRY DESKG #type complete TITLE glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) (EC 1.2.1.12) - garden snapdragon ORGANISM #formal_name Antirrhinum majus #common_name garden snapdragon DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Jun-2002 ACCESSIONS S17991 REFERENCE S17991 !$#authors Martin, W.; Gierl, A.; Saedler, H. !$#journal Nature (1989) 339:46-48 !$#title Molecular evidence for pre-Cretaceous angiosperm origins. !$#accession S17991 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type mRNA !'##residues 1-337 ##label MAR !'##cross-references EMBL:X59517; NID:g16021; PIDN:CAA42103.1; !1PID:g1345501 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1May 1991 CLASSIFICATION #superfamily glyceraldehyde-3-phosphate dehydrogenase KEYWORDS gluconeogenesis; glycolysis; homotetramer; NAD; !1oxidoreductase FEATURE !$5-35 #region beta-alpha-beta NAD nucleotide-binding fold\ !$154,181 #active_site Cys, His #status predicted SUMMARY #length 337 #molecular-weight 36685 #checksum 5069 SEQUENCE /// ENTRY DEPJG #type complete TITLE glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) (EC 1.2.1.12) - garden petunia ORGANISM #formal_name Petunia x hybrida #common_name garden petunia DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Jun-2002 ACCESSIONS S18485 REFERENCE S17991 !$#authors Martin, W.; Gierl, A.; Saedler, H. !$#journal Nature (1989) 339:46-48 !$#title Molecular evidence for pre-Cretaceous angiosperm origins. !$#accession S18485 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type mRNA !'##residues 1-337 ##label MAR !'##cross-references EMBL:X60346; NID:g20550; PIDN:CAA42904.1; !1PID:g20551 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1May 1991 CLASSIFICATION #superfamily glyceraldehyde-3-phosphate dehydrogenase KEYWORDS gluconeogenesis; glycolysis; homotetramer; NAD; !1oxidoreductase FEATURE !$5-35 #region beta-alpha-beta NAD nucleotide-binding fold\ !$154,181 #active_site Cys, His #status predicted SUMMARY #length 337 #molecular-weight 36527 #checksum 2561 SEQUENCE /// ENTRY DEJMG #type complete TITLE glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) (EC 1.2.1.12) - Magnolia liliiflora ORGANISM #formal_name Magnolia liliiflora DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Jun-2002 ACCESSIONS S18483 REFERENCE S17991 !$#authors Martin, W.; Gierl, A.; Saedler, H. !$#journal Nature (1989) 339:46-48 !$#title Molecular evidence for pre-Cretaceous angiosperm origins. !$#accession S18483 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type mRNA !'##residues 1-341 ##label MAR !'##cross-references EMBL:X60347; NID:g19565; PIDN:CAA42905.1; !1PID:g19566 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1May 1991 CLASSIFICATION #superfamily glyceraldehyde-3-phosphate dehydrogenase KEYWORDS gluconeogenesis; glycolysis; homotetramer; NAD; !1oxidoreductase FEATURE !$7-37 #region beta-alpha-beta NAD nucleotide-binding fold\ !$156,183 #active_site Cys, His #status predicted SUMMARY #length 341 #molecular-weight 36982 #checksum 8619 SEQUENCE /// ENTRY DENDG #type complete TITLE glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) (EC 1.2.1.12) - common buttercup ORGANISM #formal_name Ranunculus acer #common_name common buttercup DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Jun-2002 ACCESSIONS S18486 REFERENCE S17991 !$#authors Martin, W.; Gierl, A.; Saedler, H. !$#journal Nature (1989) 339:46-48 !$#title Molecular evidence for pre-Cretaceous angiosperm origins. !$#accession S18486 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type mRNA !'##residues 1-338 ##label MAR !'##cross-references EMBL:X60345; NID:g21065; PIDN:CAA42903.1; !1PID:g21066 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1May 1991 CLASSIFICATION #superfamily glyceraldehyde-3-phosphate dehydrogenase KEYWORDS gluconeogenesis; glycolysis; homotetramer; NAD; !1oxidoreductase FEATURE !$6-36 #region beta-alpha-beta NAD nucleotide-binding fold\ !$155,182 #active_site Cys, His #status predicted SUMMARY #length 338 #molecular-weight 36570 #checksum 95 SEQUENCE /// ENTRY DEPZG #type complete TITLE glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) (EC 1.2.1.12) - parsley ORGANISM #formal_name Petroselinum crispum #common_name parsley DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Jun-2002 ACCESSIONS S18484 REFERENCE S17991 !$#authors Martin, W.; Gierl, A.; Saedler, H. !$#journal Nature (1989) 339:46-48 !$#title Molecular evidence for pre-Cretaceous angiosperm origins. !$#accession S18484 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type mRNA !'##residues 1-336 ##label MAR !'##cross-references EMBL:X60344; NID:g20548; PIDN:CAA42902.1; !1PID:g20549 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1May 1991 CLASSIFICATION #superfamily glyceraldehyde-3-phosphate dehydrogenase KEYWORDS gluconeogenesis; glycolysis; homotetramer; NAD; !1oxidoreductase FEATURE !$4-34 #region beta-alpha-beta NAD nucleotide-binding fold\ !$153,180 #active_site Cys, His #status predicted SUMMARY #length 336 #molecular-weight 36371 #checksum 8603 SEQUENCE /// ENTRY DEECG3 #type complete TITLE glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) (EC 1.2.1.12) A - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 03-Jun-2002 ACCESSIONS A25209; C64938 REFERENCE A25209 !$#authors Branlant, G.; Branlant, C. !$#journal Eur. J. Biochem. (1985) 150:61-66 !$#title Nucleotide sequence of the Escherichia coli gap gene. !1Different evolutionary behavior of the NAD+-binding domain !1and of the catalytic domain of D-glyceraldehyde-3-phosphate !1dehydrogenase. !$#cross-references MUID:85257641; PMID:2990926 !$#accession A25209 !'##molecule_type DNA !'##residues 1-331 ##label BRA !'##cross-references GB:X02662; NID:g41538; PIDN:CAA26498.1; PID:g41539 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64938 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-331 ##label BLAT !'##cross-references GB:AE000273; GB:U00096; NID:g1788078; !1PIDN:AAC74849.1; PID:g1788079; UWGP:b1779 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene gapA (gap) !$#map_position 39 min CLASSIFICATION #superfamily glyceraldehyde-3-phosphate dehydrogenase KEYWORDS gluconeogenesis; glycolysis; homotetramer; NAD; !1oxidoreductase FEATURE !$4-34 #region beta-alpha-beta NAD nucleotide-binding fold\ !$150,177 #active_site Cys, His #status predicted SUMMARY #length 331 #molecular-weight 35532 #checksum 4188 SEQUENCE /// ENTRY DEUTGC #type complete TITLE glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) (EC 1.2.1.12), cytosolic - Trypanosoma brucei ORGANISM #formal_name Trypanosoma brucei DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Jun-2002 ACCESSIONS S16091; A29069 REFERENCE S16091 !$#authors Michels, P.A.M.; Marchand, M.; Kohl, L.; Allert, S.; !1Wierenga, R.K.; Opperdoes, F.R. !$#journal Eur. J. Biochem. (1991) 198:421-428 !$#title The cytosolic and glycosomal isoenzymes of !1glyceraldehyde-3-phosphate dehydrogenase in Trypanosoma !1brucei have a distant evolutionary relationship. !$#cross-references MUID:91249838; PMID:2040303 !$#accession S16091 !'##molecule_type DNA !'##residues 1-331 ##label MIC !'##cross-references EMBL:X53472; NID:g10406; PIDN:CAA37568.1; !1PID:g10407 REFERENCE A29069 !$#authors Misset, O.; van Beeumen, J.; Lambeir, A.M.; van der Meer, !1R.; Opperdoes, F.R. !$#journal Eur. J. Biochem. (1987) 162:501-507 !$#title Glyceraldehyde-phosphate dehydrogenase from Trypanosoma !1brucei. Comparison of the glycosomal and cytosolic !1isoenzymes. !$#cross-references MUID:87161817; PMID:3830153 !$#accession A29069 !'##molecule_type protein !'##residues 2-56,'T',58-60,'K',62-72,'I',74-75,'AQXK',80-81,'X',83-84, !1'XA' ##label MIS !'##note 73-Arg was also found GENETICS !$#gene gap CLASSIFICATION #superfamily glyceraldehyde-3-phosphate dehydrogenase KEYWORDS homotetramer; NAD; oxidoreductase FEATURE !$4-34 #region beta-alpha-beta NAD nucleotide-binding fold\ !$150,177 #active_site Cys, His #status predicted SUMMARY #length 331 #molecular-weight 35634 #checksum 6465 SEQUENCE /// ENTRY DEHGGT #type complete TITLE glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) (EC 1.2.1.12) [validated] - Thermotoga maritima (strain MSB8) ORGANISM #formal_name Thermotoga maritima DATE 30-Sep-1992 #sequence_revision 12-Apr-1996 #text_change 03-Jun-2002 ACCESSIONS S33325; S11345; F72344; S32193 REFERENCE S33325 !$#authors Tomschy, A.; Glockshuber, R.; Jaenicke, R. !$#journal Eur. J. Biochem. (1993) 214:43-50 !$#title Functional expression of D-glyceraldehyde-3-phosphate !1dehydrogenase from the hyperthermophilic eubacterium !1Thermotoga maritima in Escherichia coli. Authenticity and !1kinetic properties of the recombinant enzyme. !$#cross-references MUID:93285164; PMID:8508805 !$#accession S33325 !'##molecule_type DNA !'##residues 1-333 ##label TOM !'##cross-references EMBL:X72629; NID:g288270; PIDN:CAA51205.1; !1PID:g939978 REFERENCE S11345 !$#authors Schultes, V.; Deutzmann, R.; Jaenicke, R. !$#journal Eur. J. Biochem. (1990) 192:25-31 !$#title Complete amino-acid sequence of glyceraldehyde-3-phosphate !1dehydrogenase from the hyperthermophilic eubacterium !1Thermotoga maritima. !$#cross-references MUID:90382451; PMID:2401296 !$#accession S11345 !'##molecule_type protein !'##residues 2-333 ##label SCH REFERENCE A52997 !$#authors Korndoerfer, I.; Steipe, B.; Huber, R.; Tomschy, A.; !1Jaenicke, R. !$#submission submitted to the Brookhaven Protein Data Bank, January 1995 !$#cross-references PDB:1HDG !$#contents annotation; X-ray crystallography, 2.5 angstroms, residues !12-333 REFERENCE A72200 !$#authors Nelson, K.E.; Clayton, R.A.; Gill, S.R.; Gwinn, M.L.; !1Dodson, R.J.; Haft, D.H.; Hickey, E.K.; Peterson, J.D.; !1Nelson, W.C.; Ketchum, K.A.; McDonald, L.; Utterback, T.R.; !1Malek, J.A.; Linher, K.D.; Garrett, M.M.; Stewart, A.M.; !1Cotton, M.D.; Pratt, M.S.; Phillips, C.A.; Richardson, D.; !1Heidelberg, J.; Sutton, G.G.; Fleischmann, R.D.; White, O.; !1Salzberg, S.L.; Smith, H.O.; Venter, J.C.; Fraser, C.M. !$#journal Nature (1999) 399:323-329 !$#title Evidence for lateral gene transfer between Archaea and !1Bacteria from genome sequence of Thermotoga maritima. !$#cross-references MUID:99287316; PMID:10360571 !$#accession F72344 !'##molecule_type DNA !'##residues 1-333 ##label ARN !'##cross-references GB:AE001741; GB:AE000512; NID:g4981208; !1PIDN:AAD35770.1; PID:g4981211; TIGR:TM0688 !'##experimental_source strain MSB8 GENETICS !$#gene TM0688 COMPLEX homotetramer FUNCTION !$#description catalyzes the oxidation and phosphorylation of !1D-glyceraldehyde-3-phosphate to 3-phospho-D-glyceroyl !1phosphate by NAD+ and phosphate !$#pathway glycolysis CLASSIFICATION #superfamily glyceraldehyde-3-phosphate dehydrogenase KEYWORDS glycolysis; homotetramer; NAD; oxidoreductase FEATURE !$2-333 #product glyceraldehyde-3-phosphate dehydrogenase !8#status experimental #label MAT\ !$3-35 #region beta-alpha-beta NAD nucleotide-binding fold\ !$152,179 #active_site Cys, His #status predicted SUMMARY #length 333 #molecular-weight 36425 #checksum 7690 SEQUENCE /// ENTRY DETWG3 #type complete TITLE glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) (EC 1.2.1.12) - Thermus aquaticus ORGANISM #formal_name Thermus aquaticus DATE 24-Apr-1984 #sequence_revision 31-Dec-1990 #text_change 03-Jun-2002 ACCESSIONS S06930; A00373 REFERENCE S06930 !$#authors Hecht, R.M.; Garza, A.; Lee, Y.H.; Miller, M.D.; Pisegna, !1M.A. !$#journal Nucleic Acids Res. (1989) 17:10123 !$#title Nucleotide sequence of the glyceraldehyde-3-phosphate !1dehydrogenase gene from Thermus aquaticus YT1. !$#cross-references MUID:90098797; PMID:2602126 !$#accession S06930 !'##molecule_type DNA !'##residues 1-331 ##label HEC !'##cross-references EMBL:X16595; NID:g48120; PIDN:CAA34605.1; !1PID:g48121 REFERENCE A00373 !$#authors Hocking, J.D.; Harris, J.I. !$#journal Eur. J. Biochem. (1980) 108:567-579 !$#title D-Glyceraldehyde-3-phosphate dehydrogenase. Amino-acid !1sequence of the enzyme from the extreme thermophile Thermus !1aquaticus. !$#cross-references MUID:81003879; PMID:6773768 !$#accession A00373 !'##molecule_type protein !'##residues 1-33,'ND',36-126,'L',128-179,'BBZ',183-279,'ZB',282-302, !1'XX',304-331 ##label HOC GENETICS !$#gene gap CLASSIFICATION #superfamily glyceraldehyde-3-phosphate dehydrogenase KEYWORDS gluconeogenesis; glycolysis; homotetramer; NAD; !1oxidoreductase FEATURE !$2-31 #region beta-alpha-beta NAD nucleotide-binding fold\ !$149,176 #active_site Cys, His #status predicted SUMMARY #length 331 #molecular-weight 35892 #checksum 2794 SEQUENCE /// ENTRY DEBSGF #type complete TITLE glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) (EC 1.2.1.12) [validated] - Bacillus stearothermophilus ALTERNATE_NAMES triosephosphate dehydrogenase ORGANISM #formal_name Bacillus stearothermophilus DATE 24-Apr-1984 #sequence_revision 17-Nov-2000 #text_change 03-Jun-2002 ACCESSIONS JS0164; PS0343; A93186; A91096; A00374 REFERENCE JS0164 !$#authors Branlant, C.; Oster, T.; Branlant, G. !$#journal Gene (1989) 75:145-155 !$#title Nucleotide sequence determination of the DNA region coding !1for Bacillus stearothermophilus glyceraldehyde-3-phosphate !1dehydrogenase and of the flanking DNA regions required for !1its expression in Escherichia coli. !$#cross-references MUID:89252911; PMID:2656407 !$#accession JS0164 !'##molecule_type DNA !'##residues 1-335 ##label BRA !'##cross-references GB:M24493; NID:g142951; PIDN:AAA22461.1; !1PID:g142952 REFERENCE JQ1399 !$#authors Davies, G.J.; Littlechild, J.A.; Watson, H.C.; Hall, L. !$#journal Gene (1991) 109:39-45 !$#title Sequence and expression of the gene encoding !13-phosphoglycerate kinase from Bacillus stearothermophilus. !$#cross-references MUID:92097950; PMID:1756980 !$#accession PS0343 !'##molecule_type DNA !'##residues 315-335 ##label DAV !'##cross-references EMBL:X58059; NID:g48853; PIDN:CAA41092.1; !1PID:g48854 !'##experimental_source strain NCA1503 REFERENCE A93186 !$#authors Biesecker, G.; Harris, J.I.; Thierry, J.C.; Walker, J.E.; !1Wonacott, A.J. !$#journal Nature (1977) 266:328-333 !$#title Sequence and structure of D-glyceraldehyde 3-phosphate !1dehydrogenase from Bacillus stearothermophilus. !$#cross-references MUID:77171226; PMID:193030 !$#contents sequence; X-ray crystallography, 2.7 angstroms !$#accession A93186 !'##molecule_type protein !'##residues 2-36,'N',38,'DG',41-58,'V',60-61,'DGDVS',67-78,'N',80-124, !1'V',126,'N',128-129,'V',131-165,'QE',168-183,'N',185-196, !1'G',198-283,'N',285-330,'NA',333-335 ##label ACC REFERENCE A91096 !$#authors Walker, J.E.; Carne, A.F.; Runswick, M.J.; Bridgen, J.; !1Harris, J.I. !$#journal Eur. J. Biochem. (1980) 108:549-565 !$#title D-Glyceraldehyde-3-phosphate dehydrogenase. Complete !1amino-acid sequence of the enzyme from Bacillus !1stearothermophilus. !$#cross-references MUID:81003878; PMID:7408868 !$#accession A91096 !'##molecule_type protein !'##residues 2-36,'N',38,'DG',41-58,'V',60-61,'DGDVS',67-78,'N',80-124, !1'V',126,'N',128-129,'V',131-165,'QE',168-183,'N',185-196, !1'G',198-283,'N',285-330,'NA',333-335 ##label WAL GENETICS !$#gene gap CLASSIFICATION #superfamily glyceraldehyde-3-phosphate dehydrogenase KEYWORDS gluconeogenesis; glycolysis; homotetramer; NAD; !1oxidoreductase FEATURE !$4-34 #region beta-alpha-beta NAD nucleotide-binding fold\ !$152 #active_site Cys #status experimental\ !$179 #active_site His #status predicted SUMMARY #length 335 #molecular-weight 36075 #checksum 8146 SEQUENCE /// ENTRY DEBSG #type complete TITLE glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) (EC 1.2.1.12) gap [similarity] - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 03-Jun-2002 ACCESSIONS S02754; A35806; H69628 REFERENCE S02754 !$#authors Viaene, A.; Dhaese, P. !$#journal Nucleic Acids Res. (1989) 17:1251 !$#title Sequence of the glyceraldehyde-3-phosphate dehydrogenase !1gene from Bacillus subtilis. !$#cross-references MUID:89160255; PMID:2493629 !$#accession S02754 !'##molecule_type DNA !'##residues 1-335 ##label VIA !'##cross-references EMBL:X13011; NID:g39920; PIDN:CAA31434.1; !1PID:g39921 REFERENCE A35806 !$#authors Graves, L.M.; Switzer, R.L. !$#journal J. Biol. Chem. (1990) 265:14947-14955 !$#title Aspartokinase II from Bacillus subtilis is degraded in !1response to nutrient limitation. !$#cross-references MUID:90368669; PMID:2168395 !$#accession A35806 !'##molecule_type protein !'##residues 1,'K',3-5,'A',7-15,'M',17-19,'K' ##label GRA !'##note this material was a 38K protein protein cross-reacting with !1antibody specific to aspartokinase II; although sequence !1differs from that of glyceraldehyde-3-phosphate !1dehydrogenase at only three positions, authors suggest their !138K protein is not the same protein REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69628 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-335 ##label KUN !'##cross-references GB:Z99121; GB:AL009126; NID:g2635827; !1PIDN:CAB15399.1; PID:g2635907 !'##experimental_source strain 168 GENETICS !$#gene gap CLASSIFICATION #superfamily glyceraldehyde-3-phosphate dehydrogenase KEYWORDS gluconeogenesis; glycolysis; homotetramer; NAD; !1oxidoreductase FEATURE !$4-34 #region beta-alpha-beta NAD nucleotide-binding fold\ !$152,179 #active_site Cys, His #status predicted SUMMARY #length 335 #molecular-weight 35832 #checksum 7060 SEQUENCE /// ENTRY DEZMG3 #type complete TITLE glyceraldehyde-3-phosphate dehydrogenase (NADP) (phosphorylating) (EC 1.2.1.13) A precursor, chloroplast - maize ORGANISM #formal_name Zea mays #common_name maize DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Jun-2002 ACCESSIONS A30890; S00353; S19255 REFERENCE A30890 !$#authors Quigley, F.; Martin, W.F.; Cerff, R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:2672-2676 !$#title Intron conservation across the prokaryote-eukaryote !1boundary: structure of the nuclear gene for chloroplast !1glyceraldehyde-3-phosphate dehydrogenase from maize. !$#cross-references MUID:88190130; PMID:3357887 !$#accession A30890 !'##molecule_type DNA !'##residues 1-403 ##label QUI !'##cross-references EMBL:M18976; NID:g168478; PIDN:AAA33464.1; !1PID:g168479 REFERENCE S00353 !$#authors Brinkmann, H.; Martinez, P.; Quigley, F.; Martin, W.; Cerff, !1R. !$#journal J. Mol. Evol. (1987) 26:320-328 !$#title Endosymbiotic origin and codon bias of the nuclear gene for !1chloroplast glyceraldehyde-3-phosphate dehydrogenase from !1maize. !$#cross-references MUID:88230473; PMID:3131533 !$#accession S00353 !'##molecule_type mRNA !'##residues 21-403 ##label BRI !'##cross-references EMBL:X07157; NID:g22239; PIDN:CAA30152.1; !1PID:g22240 REFERENCE S19254 !$#authors Gowri, G.; Campbell, W.H. !$#journal Plant Physiol. (1989) 90:792-798 !$#title cDNA clones for corn leaf NADH: nitrate reductase and !1chloroplast NAD(P)(+): glyceraldehyde-3-phosphate !1dehydrogenase. !$#accession S19255 !'##status preliminary !'##molecule_type mRNA !'##residues 1-125;301-403 ##label GOW !'##cross-references EMBL:M31481 GENETICS !$#gene Gpa1 !$#introns 15/3; 52/3; 237/1 CLASSIFICATION #superfamily glyceraldehyde-3-phosphate dehydrogenase KEYWORDS Calvin cycle; chloroplast; NADP; oxidoreductase; tetramer FEATURE !$1-66 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$67-403 #product glyceraldehyde-3-phosphate dehydrogenase A !8#status predicted #label MAT\ !$69-102 #region beta-alpha-beta NADP nucleotide-binding fold\ !$220,247 #active_site Cys, His #status predicted SUMMARY #length 403 #molecular-weight 42866 #checksum 805 SEQUENCE /// ENTRY DEPMNA #type complete TITLE glyceraldehyde-3-phosphate dehydrogenase (NADP) (phosphorylating) (EC 1.2.1.13) A precursor, chloroplast - garden pea ORGANISM #formal_name Pisum sativum #common_name garden pea DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Jun-2002 ACCESSIONS S14243; S05554; A38270 REFERENCE A38270 !$#authors Liaud, M.F.; Zhang, D.X.; Cerff, R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:8918-8922 !$#title Differential intron loss and endosymbiotic transfer of !1chloroplast glyceraldehyde-3-phosphate dehydrogenase genes !1to the nucleus. !$#cross-references MUID:91062390; PMID:2247465 !$#accession S14243 !'##molecule_type DNA !'##residues 1-405 ##label LIA !'##cross-references EMBL:X52148; NID:g12158; PIDN:CAA36396.1; !1PID:g12159 REFERENCE S05552 !$#authors Brinkmann, H.; Cerff, R.; Salomon, M.; Soll, J. !$#journal Plant Mol. Biol. (1989) 13:81-94 !$#title Cloning and sequence analysis of cDNAs encoding the !1cytosolic precursors of subunits GapA and GapB of !1chloroplast glyceraldehyde-3-phosphate dehydrogenase from !1pea and spinach. !$#cross-references MUID:93357435; PMID:2562762 !$#accession S05554 !'##molecule_type mRNA !'##residues 1-405 ##label BRI !'##cross-references EMBL:X15190 !'##note the authors translated the codon AGA for residue 194 as Gly; !1the sequence shown follows the authors' translation GENETICS !$#gene Gpa1 !$#introns 14/3; 53/3; 157/2; 239/1 CLASSIFICATION #superfamily glyceraldehyde-3-phosphate dehydrogenase KEYWORDS Calvin cycle; chloroplast; NADP; oxidoreductase; tetramer FEATURE !$1-68 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$69-405 #product glyceraldehyde-3-phosphate dehydrogenase !8(NADP+) (phosphorylating) A #status predicted #label !8MAT\ !$222,249 #active_site Cys, His #status predicted SUMMARY #length 405 #molecular-weight 43338 #checksum 1819 SEQUENCE /// ENTRY DESPGA #type complete TITLE glyceraldehyde-3-phosphate dehydrogenase (NADP) (phosphorylating) (EC 1.2.1.13) A, chloroplast - spinach ORGANISM #formal_name Spinacia oleracea #common_name spinach DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 03-Jun-2002 ACCESSIONS S13155 REFERENCE S13155 !$#authors Ferri, G.; Stoppini, M.; Meloni, M.L.; Zapponi, M.C.; !1Iadarola, P. !$#journal Biochim. Biophys. Acta (1990) 1041:36-42 !$#title Chloroplast glyceraldehyde-3-phosphate dehydrogenase (NADP): !1amino acid sequence of the subunits from isoenzyme I and !1structural relationship with isoenzyme II. !$#cross-references MUID:91027867; PMID:2223845 !$#accession S13155 !'##molecule_type protein !'##residues 1-337 ##label FER CLASSIFICATION #superfamily glyceraldehyde-3-phosphate dehydrogenase KEYWORDS Calvin cycle; chloroplast; NADP; oxidoreductase; tetramer FEATURE !$3-35 #region beta-alpha-beta NADP nucleotide-binding fold\ !$153,180 #active_site Cys, His #status predicted SUMMARY #length 337 #molecular-weight 36226 #checksum 1213 SEQUENCE /// ENTRY DEPMNB #type complete TITLE glyceraldehyde-3-phosphate dehydrogenase (NADP) (phosphorylating) (EC 1.2.1.13) B precursor, chloroplast - garden pea ORGANISM #formal_name Pisum sativum #common_name garden pea DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Jun-2002 ACCESSIONS S16507; S05552; S05609; B38270 REFERENCE A38270 !$#authors Liaud, M.F.; Zhang, D.X.; Cerff, R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:8918-8922 !$#title Differential intron loss and endosymbiotic transfer of !1chloroplast glyceraldehyde-3-phosphate dehydrogenase genes !1to the nucleus. !$#cross-references MUID:91062390; PMID:2247465 !$#accession S16507 !'##molecule_type DNA !'##residues 1-451 ##label LIA !'##cross-references EMBL:M55147; NID:g309670; PIDN:AAA84543.1; !1PID:g309671 REFERENCE S05552 !$#authors Brinkmann, H.; Cerff, R.; Salomon, M.; Soll, J. !$#journal Plant Mol. Biol. (1989) 13:81-94 !$#title Cloning and sequence analysis of cDNAs encoding the !1cytosolic precursors of subunits GapA and GapB of !1chloroplast glyceraldehyde-3-phosphate dehydrogenase from !1pea and spinach. !$#cross-references MUID:93357435; PMID:2562762 !$#accession S05552 !'##molecule_type mRNA !'##residues 5-451 ##label BRI !'##cross-references EMBL:X15188 REFERENCE S05609 !$#authors Cerff, R. !$#submission submitted to the EMBL Data Library, May 1989 !$#accession S05609 !'##molecule_type mRNA !'##residues 5-254,'S',256-451 ##label CER !'##cross-references EMBL:X15188; NID:g20732; PIDN:CAA33262.1; !1PID:g20733 GENETICS !$#gene Gpb1 !$#introns 33/3; 71/3; 125/3; 181/3; 235/2; 256/1; 272/3; 408/2 CLASSIFICATION #superfamily glyceraldehyde-3-phosphate dehydrogenase KEYWORDS Calvin cycle; chloroplast; NADP; oxidoreductase; tetramer FEATURE !$1-84 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$85-451 #product glyceraldehyde-3-phosphate dehydrogenase !8(NADP+) (phosphorylating) B #status predicted #label !8MAT\ !$239,266 #active_site Cys, His #status predicted SUMMARY #length 451 #molecular-weight 48097 #checksum 433 SEQUENCE /// ENTRY DESPGB #type complete TITLE glyceraldehyde-3-phosphate dehydrogenase (NADP) (phosphorylating) (EC 1.2.1.13) B precursor, chloroplast - spinach ORGANISM #formal_name Spinacia oleracea #common_name spinach DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 03-Jun-2002 ACCESSIONS S05553; S05610; S13156 REFERENCE S05552 !$#authors Brinkmann, H.; Cerff, R.; Salomon, M.; Soll, J. !$#journal Plant Mol. Biol. (1989) 13:81-94 !$#title Cloning and sequence analysis of cDNAs encoding the !1cytosolic precursors of subunits GapA and GapB of !1chloroplast glyceraldehyde-3-phosphate dehydrogenase from !1pea and spinach. !$#cross-references MUID:93357435; PMID:2562762 !$#accession S05553 !'##molecule_type mRNA !'##residues 1-451 ##label BRI !'##cross-references EMBL:X15189 REFERENCE S05609 !$#authors Cerff, R. !$#submission submitted to the EMBL Data Library, May 1989 !$#accession S05610 !'##molecule_type mRNA !'##residues 1-28,'L',30-451 ##label CER !'##cross-references EMBL:X15189; NID:g21251; PIDN:CAA33263.1; !1PID:g21252 REFERENCE S13155 !$#authors Ferri, G.; Stoppini, M.; Meloni, M.L.; Zapponi, M.C.; !1Iadarola, P. !$#journal Biochim. Biophys. Acta (1990) 1041:36-42 !$#title Chloroplast glyceraldehyde-3-phosphate dehydrogenase (NADP): !1amino acid sequence of the subunits from isoenzyme I and !1structural relationship with isoenzyme II. !$#cross-references MUID:91027867; PMID:2223845 !$#accession S13156 !'##molecule_type protein !'##residues 84-451 ##label FER GENETICS !$#gene Gpb1 CLASSIFICATION #superfamily glyceraldehyde-3-phosphate dehydrogenase KEYWORDS Calvin cycle; chloroplast; NADP; oxidoreductase; tetramer FEATURE !$1-83 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$84-451 #product glyceraldehyde-3-phosphate dehydrogenase !8(NADP+) (phosphorylating) B #status experimental !8#label MAT\ !$238,265 #active_site Cys, His #status predicted SUMMARY #length 451 #molecular-weight 48109 #checksum 9082 SEQUENCE /// ENTRY DEZYG3 #type complete TITLE glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) (EC 1.2.1.12) - Zymomonas mobilis ORGANISM #formal_name Zymomonas mobilis DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 03-Jun-2002 ACCESSIONS A28386 REFERENCE A28386 !$#authors Conway, T.; Sewell, G.W.; Ingram, L.O. !$#journal J. Bacteriol. (1987) 169:5653-5662 !$#title Glyceraldehyde-3-phosphate dehydrogenase gene from Zymomonas !1mobilis: cloning, sequencing, and identification of promoter !1region. !$#cross-references MUID:88058780; PMID:3680173 !$#accession A28386 !'##molecule_type DNA !'##residues 1-337 ##label CON !'##cross-references GB:M18802; NID:g155584; PIDN:AAA27688.1; !1PID:g155585 COMMENT The enzyme is a tetramer of identical chains. GENETICS !$#gene gap CLASSIFICATION #superfamily glyceraldehyde-3-phosphate dehydrogenase KEYWORDS gluconeogenesis; glycolysis; homotetramer; NAD; !1oxidoreductase FEATURE !$154,181 #active_site Cys, His #status predicted SUMMARY #length 337 #molecular-weight 36102 #checksum 2323 SEQUENCE /// ENTRY DEECGB #type complete TITLE glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) (EC 1.2.1.12) B - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 03-Jun-2002 ACCESSIONS S04732; F65077 REFERENCE S04730 !$#authors Alefounder, P.R.; Perham, R.N. !$#journal Mol. Microbiol. (1989) 3:723-732 !$#title Identification, molecular cloning and sequence analysis of a !1gene cluster encoding the class II fructose 1,6-bisphosphate !1aldolase, 3-phosphoglycerate kinase and a putative second !1glyceraldehyde 3-phosphate dehydrogenase of Escherichia !1coli. !$#cross-references MUID:89313302; PMID:2546007 !$#accession S04732 !'##molecule_type DNA !'##residues 1-339 ##label ALE !'##cross-references EMBL:X14436; NID:g41417; PIDN:CAA32603.1; !1PID:g41421 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65077 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-339 ##label BLAT !'##cross-references GB:AE000376; GB:U00096; NID:g2367176; !1PIDN:AAC75964.1; PID:g1789295; UWGP:b2927 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene epd; gapB !$#map_position 63 min CLASSIFICATION #superfamily glyceraldehyde-3-phosphate dehydrogenase KEYWORDS gluconeogenesis; glycolysis; homotetramer; NAD; !1oxidoreductase FEATURE !$155,182 #active_site Cys, His #status predicted SUMMARY #length 339 #molecular-weight 37299 #checksum 9172 SEQUENCE /// ENTRY DEQYG #type complete TITLE glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (EC 1.2.1.-) - Pyrococcus woesei ORGANISM #formal_name Pyrococcus woesei DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 11-Jun-1999 ACCESSIONS S10653; A38806 REFERENCE S10650 !$#authors Zwickl, P.; Fabry, S.; Bogedain, C.; Haas, A.; Hensel, R. !$#journal J. Bacteriol. (1990) 172:4329-4338 !$#title Glyceraldehyde-3-phosphate dehydrogenase from the !1hyperthermophilic archaebacterium Pyrococcus woesei: !1characterization of the enzyme, cloning and sequencing of !1the gene, and expression in Escherichia coli. !$#cross-references MUID:90330536; PMID:2165475 !$#accession S10653 !'##molecule_type DNA !'##residues 1-334 ##label ZWI !'##cross-references GB:M83988; NID:g151734; PIDN:AAA73180.1; !1PID:g151735 !$#accession A38806 !'##molecule_type protein !'##residues 1-14 ##label ZWI2 COMMENT This enzyme is active in the presence of NAD and NADP. GENETICS !$#start_codon GTG CLASSIFICATION #superfamily glyceraldehyde-3-phosphate dehydrogenase KEYWORDS NAD; NADP; oxidoreductase; tetramer FEATURE !$1-334 #product glyceraldehyde-3-phosphate dehydrogenase !8#status experimental #label MAT\ !$141 #active_site Cys #status predicted SUMMARY #length 334 #molecular-weight 37436 #checksum 300 SEQUENCE /// ENTRY JT0286 #type complete TITLE glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) (EC 1.2.1.12) - Methanothermus fervidus ORGANISM #formal_name Methanothermus fervidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS JT0286 REFERENCE JT0286 !$#authors Fabry, S.; Hensel, R. !$#journal Gene (1988) 64:189-197 !$#title Primary structure of glyceraldehyde-3-phosphate !1dehydrogenase deduced from the nucleotide sequence of the !1thermophilic archaebacterium Methanothermus fervidus. !$#cross-references MUID:88297150; PMID:2841192 !$#accession JT0286 !'##molecule_type DNA !'##residues 1-337 ##label FAB !'##cross-references GB:M19980; NID:g149791; PIDN:AAA88227.1; !1PID:g149792 !'##note part of this sequence was confirmed by protein sequencing GENETICS !$#gene gap CLASSIFICATION #superfamily glyceraldehyde-3-phosphate dehydrogenase KEYWORDS oxidoreductase FEATURE !$146 #active_site Cys #status predicted SUMMARY #length 337 #molecular-weight 37408 #checksum 1314 SEQUENCE /// ENTRY S02804 #type complete TITLE glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (EC 1.2.1.-) - Methanobacterium bryantii ORGANISM #formal_name Methanobacterium bryantii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S02804 REFERENCE S02803 !$#authors Fabry, S.; Lang, J.; Niermann, T.; Vingron, M.; Hensel, R. !$#journal Eur. J. Biochem. (1989) 179:405-413 !$#title Nucleotide sequence of the glyceraldehyde-3-phosphate !1dehydrogenase gene from the mesophilic methanogenic !1archaebacteria Methanobacterium bryantii and !1Methanobacterium formicicum. Comparison with the respective !1gene structure of the closely related extreme thermophile !1Methanothermus fervidus. !$#cross-references MUID:89137118; PMID:2492940 !$#accession S02804 !'##molecule_type DNA !'##residues 1-338 ##label FAB !'##cross-references EMBL:X14631; NID:g44174; PIDN:CAA32780.1; !1PID:g44175 !'##experimental_source strain DSM 862 !'##note the authors translated the codon AAT for residue 46 as Lys COMMENT This enzyme is active in the presence of NAD and NADP. GENETICS !$#gene gap CLASSIFICATION #superfamily glyceraldehyde-3-phosphate dehydrogenase KEYWORDS NAD; NADP; oxidoreductase; tetramer FEATURE !$141 #active_site Cys #status predicted SUMMARY #length 338 #molecular-weight 37013 #checksum 7129 SEQUENCE /// ENTRY S02803 #type complete TITLE glyceraldehyde-3-phosphate dehydrogenase NAD(P) (EC 1.2.1.-) - Methanobacterium formicicum ORGANISM #formal_name Methanobacterium formicicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S02803; S13773 REFERENCE S02803 !$#authors Fabry, S.; Lang, J.; Niermann, T.; Vingron, M.; Hensel, R. !$#journal Eur. J. Biochem. (1989) 179:405-413 !$#title Nucleotide sequence of the glyceraldehyde-3-phosphate !1dehydrogenase gene from the mesophilic methanogenic !1archaebacteria Methanobacterium bryantii and !1Methanobacterium formicicum. Comparison with the respective !1gene structure of the closely related extreme thermophile !1Methanothermus fervidus. !$#cross-references MUID:89137118; PMID:2492940 !$#accession S02803 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-338 ##label FAB !'##cross-references GB:X14632; NID:g44273; PIDN:CAB37402.1; !1PID:g4456664 !'##experimental_source DSM 1312 REFERENCE S13773 !$#authors Hensel, R. !$#submission submitted to the Protein Sequence Database, October 1990 !$#accession S13773 !'##molecule_type DNA !'##residues 1-44,'X',46-338 ##label HEN COMMENT This enzyme is active in the presence of NAD and NADP. GENETICS !$#gene gap CLASSIFICATION #superfamily glyceraldehyde-3-phosphate dehydrogenase KEYWORDS NAD; NADP; oxidoreductase; tetramer FEATURE !$141 #active_site Cys #status predicted SUMMARY #length 338 #molecular-weight 37220 #checksum 5359 SEQUENCE /// ENTRY RDECEP #type complete TITLE N-acetyl-gamma-glutamyl-phosphate reductase (EC 1.2.1.38) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 01-Mar-2002 ACCESSIONS JT0332; A42377; A65203; A30776 REFERENCE JT0331 !$#authors Parsot, C.; Boyen, A.; Cohen, G.N.; Glansdorff, N. !$#journal Gene (1988) 68:275-283 !$#title Nucleotide sequence of Escherichia coli argB and argC genes: !1comparison of N-acetylglutamate kinase and !1N-acetylglutamate-gamma-semialdehyde dehydrogenase with !1homologous and analogous enzymes. !$#cross-references MUID:89121510; PMID:2851495 !$#accession JT0332 !'##molecule_type DNA !'##residues 1-334 ##label PAR !'##cross-references GB:M21446; NID:g145332; PIDN:AAA23477.1; !1PID:g145333 REFERENCE A42377 !$#authors Meinnel, T.; Schmitt, E.; Mechulam, Y.; Blanquet, S. !$#journal J. Bacteriol. (1992) 174:2323-2331 !$#title Structural and biochemical characterization of the !1Escherichia coli argE gene product. !$#cross-references MUID:92202162; PMID:1551850 !$#accession A42377 !'##status preliminary !'##molecule_type DNA !'##residues 1-19 ##label MEI !'##cross-references GB:X55417 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65203 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-334 ##label BLAT !'##cross-references GB:AE000470; GB:U00096; NID:g2367332; !1PIDN:AAC76940.1; PID:g1790396; UWGP:b3958 !'##experimental_source strain K-12, substrain MG1655 COMMENT In arginine biosynthesis glutamate is first converted to !1N-acetylglutamate, which leads to N-acetylglutamylphosphate !1and then to N-acetylglutamate semialdehyde. The latter two !1reactions are catalyzed by acetylglutamate kinase and !1N-acetyl-gamma-glutamyl-phosphate reductase. GENETICS !$#gene argC !$#map_position 90 min CLASSIFICATION #superfamily N-acetyl-gamma-glutamyl-phosphate reductase KEYWORDS arginine biosynthesis; oxidoreductase FEATURE !$154 #active_site Cys #status predicted SUMMARY #length 334 #molecular-weight 35952 #checksum 6342 SEQUENCE /// ENTRY I40372 #type complete TITLE N-acetyl-gamma-glutamyl-phosphate reductase (EC 1.2.1.38) - Bacillus subtilis ALTERNATE_NAMES acetylglutamate semialdehyde dehydrogenase; N-acetylglutamate-gamma-semialdehyde dehydrogenase argC ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS I40372; S12592; A26526; S38428; F69588; S20023 REFERENCE I40372 !$#authors O'Reilly, M.; Devine, K.M. !$#journal Microbiology (1994) 140:1023-1025 !$#title Sequence and analysis of the citrulline biosynthetic operon !1argC-F from Bacillus subtilis. !$#cross-references MUID:94297722; PMID:8025667 !$#accession I40372 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-346 ##label RES !'##cross-references EMBL:Z26919; NID:g408113; PID:g575620 REFERENCE S12592 !$#authors Smith, M.C.M.; Mountain, A.; Baumberg, S. !$#journal Nucleic Acids Res. (1990) 18:4595 !$#title Nucleotide sequence of the Bacillus subtilis argC gene !1encoding N-acetylglutamate-gamma-semialdehyde dehydrogenase. !$#cross-references MUID:90356403; PMID:2117746 !$#accession S12592 !'##molecule_type DNA !'##residues 1-340,342-346 ##label SM1 !'##cross-references EMBL:X52834; NID:g39806; PIDN:CAA37016.1; !1PID:g580828 REFERENCE A26526 !$#authors Smith, M.C.M.; Mountain, A.; Baumberg, S. !$#journal Gene (1986) 49:53-60 !$#title Sequence analysis of the Bacillus subtilis argC promoter !1region. !$#cross-references MUID:87192000; PMID:3106155 !$#accession A26526 !'##molecule_type DNA !'##residues 1-56 ##label SM2 !'##cross-references GB:M15420; NID:g142533; PIDN:AAA22248.1; !1PID:g142534 REFERENCE S38428 !$#authors O'Reilly, M.; Devine, K.M. !$#submission submitted to the EMBL Data Library, October 1993 !$#accession S38428 !'##status preliminary !'##molecule_type DNA !'##residues 1-346 ##label OAR !'##cross-references EMBL:Z26919 REFERENCE S20023 !$#authors Czaplewski, L.G.; North, A.K.; Smith, M.C.M.; Baumberg, S.; !1Stockley, P.G. !$#journal Mol. Microbiol. (1992) 6:267-275 !$#title Purification and initial characterization of AhrC: the !1regulator of arginine metabolism genes in Bacillus subtilis. !$#cross-references MUID:92186717; PMID:1312212 !$#contents annotation REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69588 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-234,'V',236-346 ##label KUN !'##cross-references GB:Z99109; GB:Z99110; GB:AL009126; NID:g2633472; !1PIDN:CAB12976.1; PID:g2633473; NID:g2633260; PID:g2633456 !'##experimental_source strain 168 GENETICS !$#gene argC !$#start_codon TTG CLASSIFICATION #superfamily N-acetyl-gamma-glutamyl-phosphate reductase KEYWORDS oxidoreductase SUMMARY #length 346 #molecular-weight 38121 #checksum 5424 SEQUENCE /// ENTRY S76613 #type complete TITLE N-acetyl-gamma-glutamyl-phosphate reductase (EC 1.2.1.38) - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S76613 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76613 !'##status preliminary !'##molecule_type DNA !'##residues 1-351 ##label KAN !'##cross-references EMBL:D64004; GB:AB001339; NID:g1001701; !1PIDN:BAA10557.1; PID:g1001720 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily N-acetyl-gamma-glutamyl-phosphate reductase KEYWORDS oxidoreductase SUMMARY #length 351 #molecular-weight 38209 #checksum 6477 SEQUENCE /// ENTRY A42987 #type complete TITLE N-acetyl-gamma-glutamyl-phosphate reductase (EC 1.2.1.38) - Streptomyces clavuligerus ORGANISM #formal_name Streptomyces clavuligerus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A42987 REFERENCE A42987 !$#authors Ludovice, M.; Martin, J.F.; Carrachas, P.; Liras, P. !$#journal J. Bacteriol. (1992) 174:4606-4613 !$#title Characterization of the Streptomyces clavuligerus argC gene !1encoding N-acetylglutamyl-phosphate reductase: expression in !1Streptomyces lividans and effect on clavulanic acid !1production. !$#cross-references MUID:92325051; PMID:1339424 !$#accession A42987 !'##status preliminary !'##molecule_type DNA !'##residues 1-340 ##label LUD !'##cross-references GB:M83659; NID:g153165; PIDN:AAA26704.1; !1PID:g153166 !'##note sequence extracted from NCBI backbone (NCBIN:108141, !1NCBIP:108142) CLASSIFICATION #superfamily N-acetyl-gamma-glutamyl-phosphate reductase KEYWORDS oxidoreductase SUMMARY #length 340 #molecular-weight 35299 #checksum 4287 SEQUENCE /// ENTRY B70462 #type complete TITLE N-acetyl-gamma-glutamyl-phosphate reductase (EC 1.2.1.38) - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B70462 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession B70462 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-340 ##label AQF !'##cross-references GB:AE000761; NID:g2984149; PIDN:AAC07684.1; !1PID:g2984150; GB:AE000657 !'##experimental_source strain VF5 GENETICS !$#gene argC CLASSIFICATION #superfamily N-acetyl-gamma-glutamyl-phosphate reductase KEYWORDS oxidoreductase SUMMARY #length 340 #molecular-weight 38957 #checksum 1960 SEQUENCE /// ENTRY G64436 #type complete TITLE N-acetyl-gamma-glutamyl-phosphate reductase (EC 1.2.1.38) - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G64436 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession G64436 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-375 ##label BUL !'##cross-references GB:U67552; GB:L77117; NID:g1591737; !1PIDN:AAB99099.1; PID:g1591740; TIGR:MJ1096 GENETICS !$#map_position REV1036979-1035852 !$#start_codon TTG CLASSIFICATION #superfamily N-acetyl-gamma-glutamyl-phosphate reductase KEYWORDS oxidoreductase SUMMARY #length 375 #molecular-weight 42212 #checksum 7836 SEQUENCE /// ENTRY H69212 #type complete TITLE N-acetyl-gamma-glutamyl-phosphate reductase (EC 1.2.1.38) - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS H69212 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession H69212 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-382 ##label MTH !'##cross-references GB:AE000861; GB:AE000666; NID:g2621930; !1PIDN:AAB85344.1; PID:g2621937 !'##experimental_source strain Delta H GENETICS !$#gene MTH846 !$#start_codon GTG CLASSIFICATION #superfamily N-acetyl-gamma-glutamyl-phosphate reductase KEYWORDS oxidoreductase SUMMARY #length 382 #molecular-weight 41885 #checksum 8103 SEQUENCE /// ENTRY F69508 #type complete TITLE N-acetyl-gamma-glutamyl-phosphate reductase (EC 1.2.1.38) - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS F69508 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession F69508 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-332 ##label KLE !'##cross-references GB:AE000961; GB:AE000782; NID:g2689284; !1PIDN:AAB89185.1; PID:g2648465; TIGR:AF2071 CLASSIFICATION #superfamily N-acetyl-gamma-glutamyl-phosphate reductase KEYWORDS oxidoreductase SUMMARY #length 332 #molecular-weight 37304 #checksum 8527 SEQUENCE /// ENTRY RDECER #type complete TITLE glutamate-5-semialdehyde dehydrogenase (EC 1.2.1.41) - Escherichia coli (strain K-12) ALTERNATE_NAMES gamma-glutamylphosphate reductase ORGANISM #formal_name Escherichia coli DATE 31-Dec-1988 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS D64749; B31001; S28005; S22962 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64749 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-417 ##label BLAT !'##cross-references GB:AE000132; GB:U00096; NID:g2367098; !1PIDN:AAC73347.1; PID:g1786438; UWGP:b0243 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A93531 !$#authors Deutch, A.H.; Rushlow, K.E.; Smith, C.J. !$#journal Nucleic Acids Res. (1984) 12:6337-6355 !$#title Analysis of the Escherichia coli proBA locus by DNA and !1protein sequencing. !$#cross-references MUID:84297232; PMID:6089111 !$#accession B31001 !'##molecule_type DNA !'##residues 1-357,368-417 ##label DEU !'##cross-references GB:D83536; NID:g4902908; PIDN:BAA77912.1; !1PID:g4902978 REFERENCE S28005 !$#authors Lim, D. !$#journal Mol. Microbiol. (1992) 6:3531-3542 !$#title Structure and biosynthesis of unbranched multicopy !1single-stranded DNA by reverse transcriptase in a clinical !1Escherichia coli isolate. !$#cross-references MUID:93116591; PMID:1282191 !$#accession S28005 !'##molecule_type DNA !'##residues 377-417 ##label LIM !'##cross-references EMBL:Z12832 GENETICS !$#gene proA !$#map_position 6 min FUNCTION !$#description catalyzes the NADPH-dependent reduction of !1glutamate-5-phosphate to NADP and glutamate-5-semialdehyde, !1which then cyclizes spontaneously to pyrroline-5-carboxylate !$#pathway amino acid metabolism; proline biosynthesis CLASSIFICATION #superfamily glutamate-5-semialdehyde dehydrogenase KEYWORDS NADP; oxidoreductase; proline biosynthesis SUMMARY #length 417 #molecular-weight 44630 #checksum 6069 SEQUENCE /// ENTRY RDSEEM #type complete TITLE glutamate-5-semialdehyde dehydrogenase (EC 1.2.1.41) - Serratia marcescens ORGANISM #formal_name Serratia marcescens DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 11-Jun-1999 ACCESSIONS B49753; S11645 REFERENCE A49753 !$#authors Omori, K.; Suzuki, S.I.; Imai, Y.; Komatsubara, S. !$#journal J. Gen. Microbiol. (1991) 137:509-517 !$#title Analysis of the Serratia marcescens proBA operon and !1feedback control of proline biosynthesis. !$#cross-references MUID:91237315; PMID:1851803 !$#accession B49753 !'##molecule_type DNA !'##residues 1-417 ##label OMO !'##cross-references GB:X53086; NID:g47251; PIDN:CAA37255.1; PID:g47254 GENETICS !$#gene proA CLASSIFICATION #superfamily glutamate-5-semialdehyde dehydrogenase KEYWORDS oxidoreductase; proline biosynthesis SUMMARY #length 417 #molecular-weight 44639 #checksum 7882 SEQUENCE /// ENTRY D64112 #type complete TITLE glutamate-5-semialdehyde dehydrogenase (EC 1.2.1.41) - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS D64112 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession D64112 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-417 ##label TIGR !'##cross-references GB:U32804; GB:L42023; NID:g1574170; !1PIDN:AAC22892.1; PID:g1574171; TIGR:HI1239 !'##note named as homolog to a protein from Escherichia coli CLASSIFICATION #superfamily glutamate-5-semialdehyde dehydrogenase KEYWORDS oxidoreductase; proline biosynthesis SUMMARY #length 417 #molecular-weight 45396 #checksum 9700 SEQUENCE /// ENTRY DEHUPA #type complete TITLE pyruvate dehydrogenase (lipoamide) (EC 1.2.4.1) alpha chain precursor - human ALTERNATE_NAMES pyruvate dehydrogenase (PDH) complex, E1 component alpha chain ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1989 #sequence_revision 31-Dec-1992 #text_change 23-Mar-2001 ACCESSIONS JQ0770; A33905; A28275; S11715; S11716; A28398; A29577; !1I56309; I54262; I54356 REFERENCE JQ0770 !$#authors Koike, K.; Urata, Y.; Matsuo, S.; Koike, M. !$#journal Gene (1990) 93:307-311 !$#title Characterization and nucleotide sequence of the gene !1encoding the human pyruvate dehydrogenase alpha-subunit. !$#cross-references MUID:91033044; PMID:2227443 !$#accession JQ0770 !'##molecule_type DNA !'##residues 1-390 ##label KOI !'##cross-references GB:D90084; NID:g219981; PIDN:BAA14121.1; !1PID:g219982 !'##experimental_source leukocyte REFERENCE A33905 !$#authors Ho, L.; Wexler, I.D.; Liu, T.C.; Thekkumkara, T.J.; Patel, !1M.S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:5330-5334 !$#title Characterization of cDNAs encoding human pyruvate !1dehydrogenase alpha-subunit. !$#cross-references MUID:89315791; PMID:2748588 !$#accession A33905 !'##molecule_type mRNA !'##residues 1-390 ##label HOL !'##cross-references GB:M24848; NID:g190761; PIDN:AAA36533.1; !1PID:g190762 REFERENCE A28275 !$#authors De Meirleir, L.; MacKay, N.; Wah, A.M.L.H.; Robinson, B.H. !$#journal J. Biol. Chem. (1988) 263:1991-1995 !$#title Isolation of a full-length complementary DNA coding for !1human E-1-alpha subunit of the pyruvate dehydrogenase !1complex. !$#cross-references MUID:88115327; PMID:2828359 !$#accession A28275 !'##molecule_type mRNA !'##residues 1-348,'P',350-353,'A',355-390 ##label DEM1 !'##cross-references EMBL:J03503; NID:g189765 !'##note the translated sequence in GenBank entry HUMPDHE1B, release !1114.0, (PIDN:AAA60055.1) differs from the published sequence !1by including the translation of 24 codons before the Met !1initiator codon REFERENCE S11715 !$#authors Huh, T.L.; Chi, Y.T.; Casazza, J.P.; Veech, R.L.; Song, B.J. !$#submission submitted to the EMBL Data Library, April 1990 !$#description Identical sequences for human brain and liver pyruvate !1dehydrogenase E1' subunits. !$#accession S11715 !'##molecule_type mRNA !'##residues 1-390 ##label HU1 !'##cross-references EMBL:X52709; NID:g35378; PIDN:CAA36933.1; !1PID:g35379 !'##experimental_source brain !$#accession S11716 !'##molecule_type mRNA !'##residues 1-390 ##label HU2 !'##cross-references EMBL:X52710; NID:g35380; PIDN:CAA36934.1; !1PID:g35381 !'##experimental_source liver REFERENCE A94198 !$#authors Koike, K.; Ohta, S.; Urata, Y.; Kagawa, Y.; Koike, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:41-45 !$#title Cloning and sequencing of cDNAs encoding alpha and beta !1subunits of human pyruvate dehydrogenase. !$#cross-references MUID:88124815; PMID:3422424 !$#accession A28398 !'##status significant sequence differences !'##molecule_type mRNA !'##cross-references GB:J03575; NID:g189737; PIDN:AAA60050.1; !1PID:g189738 !'##note the sequence is extensively revised in reference JQ0770; the !1revised sequence is shown in GenBank entry HUMPDHA, release !1114.0 REFERENCE A29577 !$#authors Dahl, H.H.M.; Hunt, S.M.; Hutchison, W.M.; Brown, G.K. !$#journal J. Biol. Chem. (1987) 262:7398-7403 !$#title The human pyruvate dehydrogenase complex. Isolation of cDNA !1clones for the E1-alpha subunit, sequence analysis, and !1characterization of the mRNA. !$#cross-references MUID:87222349; PMID:3034892 !$#accession A29577 !'##status significant sequence differences !'##molecule_type mRNA !'##cross-references GB:M27166; NID:g488487; PIDN:AAA60051.1; !1PID:g387009 !'##note the sequence reported in this reference is incorrect due to !1multiple frameshift errors; the revised sequence is shown in !1GenBank entry HUMPDHA12, release 114.0 REFERENCE I56309 !$#authors Ito, M.; Huq, A.H.; Naito, E.; Saijo, T.; Takeda, E.; !1Kuroda, Y. !$#journal J. Inherit. Metab. Dis. (1992) 15:848-856 !$#title Mutation of E1 alpha gene in a female patient with pyruvate !1dehydrogenase deficiency due to rapid degradation of E1 !1protein. !$#cross-references MUID:93188403; PMID:1338114 !$#accession I56309 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 374-382,'SVDQV' ##label ITO !'##cross-references GB:S56181; NID:g299257; PIDN:AAB25674.1; !1PID:g299258 REFERENCE I54262 !$#authors De Meirleir, L.; Lissens, W.; Vamos, E.; Liebaers, I. !$#journal Hum. Genet. (1992) 88:649-652 !$#title Pyruvate dehydrogenase (PDH) deficiency caused by a 21-base !1pair insertion mutation in the E1 alpha subunit. !$#cross-references MUID:92201830; PMID:1551669 !$#accession I54262 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 300-305,'DSYRTRE',306-309 ##label DEM2 !'##cross-references GB:S89908; NID:g247722; PIDN:AAB21863.1; !1PID:g247723 REFERENCE I54356 !$#authors Hansen, L.L.; Horn, N.; Dahl, H.H.; Kruse, T.A. !$#journal Hum. Mol. Genet. (1994) 3:1021-1022 !$#title Pyruvate dehydrogenase deficiency caused by a 33 base pair !1duplication in the PDH E1 alpha subunit. !$#cross-references MUID:95038723; PMID:7545958 !$#accession I54356 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 300-307,'PPHSYRTREEI',308-311 ##label HAN !'##cross-references GB:S75842; NID:g861533; PIDN:AAB32351.1; !1PID:g861534 COMMENT The phosphorylation of several serine sites by [pyruvate !1dehydrogenase (lipoamide)] kinase (EC 2.7.1.99) (see !1PIR:I55465, PIR:I70159, and PIR:I70160) inhibits the !1activity of the enzyme complex. The enzyme is !1dephosphorylated by [pyruvate dehydrogenase (lipoamide)] !1-phosphatase (EC 3.1.3.43). GENETICS !$#gene GDB:PDHA1 !'##cross-references GDB:118895; OMIM:312170 !$#map_position Xp22.1-Xp22.1 !$#introns 19/3; 23/3; 97/3; 140/1; 170/3; 201/3; 253/3; 272/3; 300/2; !1336/3 COMPLEX the E1 component (pyruvate dehydrogenase) is a !1heterotetramer of two alpha and two beta (see PIR:DEHUPB) !1chains; 30 E1 components form a complex with 60 E2 component !1(dihydrolipoamide acetyltransferase) monomers and 6 E3 !1component (lipoamide dehydrogenase) dimers FUNCTION !$#description catalyzes the reaction of pyruvate and lipoamide (on the E2 !1component) to form s-acetyldihydrolipoamide and carbon !1dioxide; the complex overall catalyzes the oxidative !1decarboxylation of pyruvate by NAD to form acetyl-CoA, !1carbon dioxide and NADH !$#pathway pyruvate metabolism !$#note thiamin pyrophosphate is a cofactor CLASSIFICATION #superfamily pyruvate dehydrogenase (lipoamide) alpha chain; !1thiamin pyrophosphate-binding domain homology KEYWORDS flavoprotein; heterotetramer; mitochondrion; oxidoreductase; !1phosphoprotein; thiamin pyrophosphate FEATURE !$1-29 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$30-390 #product pyruvate dehydrogenase (lipoamide) alpha !8chain #status predicted #label MAT\ !$185-234 #domain thiamin pyrophosphate-binding domain homology !8#label TPB\ !$232,293,300 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 390 #molecular-weight 43295 #checksum 7563 SEQUENCE /// ENTRY DERTP1 #type complete TITLE pyruvate dehydrogenase (lipoamide) (EC 1.2.4.1) alpha chain 1 precursor - rat ALTERNATE_NAMES pyruvate dehydrogenase complex, E1 component alpha chain ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 02-Jun-2000 ACCESSIONS S21553; I56503 REFERENCE S21553 !$#authors Cullingford, T.E.; Phillips, I.I.; Clark, J.J. !$#submission submitted to the EMBL Data Library, June 1992 !$#accession S21553 !'##molecule_type mRNA !'##residues 1-390 ##label CULS !'##cross-references EMBL:Z12158; NID:g57656; PIDN:CAA78146.1; !1PID:g57657 !'##experimental_source liver REFERENCE I56503 !$#authors Cullingford, T.E.; Clark, J.B.; Phillips, I.R. !$#journal J. Neurochem. (1994) 62:1682-1690 !$#title The pyruvate dehydrogenase complex: cloning of the rat !1somatic E1 alpha subunit and its coordinate expression with !1the mRNAs for the E1 beta, E2, and E3 catalytic subunits in !1developing rat brain. !$#cross-references MUID:94209873; PMID:8158120 !$#accession I56503 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-390 ##label CULP !'##cross-references EMBL:Z12158; NID:g57656; PIDN:CAA78146.1; !1PID:g57657 !'##note in Genbank entry RRPDHYE1A, release 113.0, the source is !1designated as Rattus rattus, strain Sprague-Dawley CLASSIFICATION #superfamily pyruvate dehydrogenase (lipoamide) alpha chain; !1thiamin pyrophosphate-binding domain homology KEYWORDS flavoprotein; heterotetramer; mitochondrion; oxidoreductase; !1phosphoprotein; thiamin pyrophosphate FEATURE !$1-29 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$30-390 #product pyruvate dehydrogenase (lipoamide) alpha !8chain #status predicted #label MAT\ !$185-234 #domain thiamin pyrophosphate-binding domain homology !8#label TPB\ !$232 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$293 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$300 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 390 #molecular-weight 43196 #checksum 6740 SEQUENCE /// ENTRY DERTPA #type complete TITLE pyruvate dehydrogenase (lipoamide) (EC 1.2.4.1) alpha chain precursor - rat ALTERNATE_NAMES pyruvate dehydrogenase complex, E1 component alpha chain ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 15-Oct-1999 ACCESSIONS S15891 REFERENCE S15891 !$#authors Matuda, S.; Nakano, K.; Ohta, S.; Saheki, T.; Kawanishi, Y.; !1Miyata, T. !$#journal Biochim. Biophys. Acta (1991) 1089:1-7 !$#title The alpha-ketoacid dehydrogenase complexes. Sequence !1similarity of rat pyruvate dehydrogenase with Escherichia !1coli and Azotobacter vinelandii alpha-ketoglutarate !1dehydrogenase. !$#cross-references MUID:91223087; PMID:2025639 !$#accession S15891 !'##molecule_type mRNA !'##residues 1-390 ##label MAT1 CLASSIFICATION #superfamily pyruvate dehydrogenase (lipoamide) alpha chain; !1thiamin pyrophosphate-binding domain homology KEYWORDS flavoprotein; heterotetramer; mitochondrion; oxidoreductase; !1phosphoprotein; thiamin pyrophosphate FEATURE !$1-29 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$30-390 #product pyruvate dehydrogenase (lipoamide) alpha !8chain #status predicted #label MAT\ !$185-234 #domain thiamin pyrophosphate-binding domain homology !8#label TPB\ !$232 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$293 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$300 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 390 #molecular-weight 43212 #checksum 6728 SEQUENCE /// ENTRY DEPGPA #type fragment TITLE pyruvate dehydrogenase (lipoamide) (EC 1.2.4.1) alpha chain precursor - pig (fragment) ALTERNATE_NAMES pyruvate dehydrogenase complex, E1 component alpha chain ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 15-Oct-1999 ACCESSIONS S20813 REFERENCE S20813 !$#authors Sermon, K.; DeMeirleir, L.; Elpers, I.; Lissens, W.; !1Liebaers, I. !$#submission submitted to the EMBL Data Library, May 1990 !$#accession S20813 !'##molecule_type mRNA !'##residues 1-389 ##label SER !'##cross-references EMBL:X52990; NID:g1850; PIDN:CAA37180.1; PID:g1851 !'##experimental_source muscle CLASSIFICATION #superfamily pyruvate dehydrogenase (lipoamide) alpha chain; !1thiamin pyrophosphate-binding domain homology KEYWORDS flavoprotein; heterotetramer; mitochondrion; oxidoreductase; !1phosphoprotein; thiamin pyrophosphate FEATURE !$1-28 #domain transit peptide (mitochondrion) (fragment) !8#status predicted #label TNP\ !$29-389 #product pyruvate dehydrogenase (lipoamide) alpha !8chain #status predicted #label MAT\ !$184-233 #domain thiamin pyrophosphate-binding domain homology !8#label TPB\ !$231 #binding_site phosphate (Ser) (covalent) #status !8experimental\ !$292 #binding_site phosphate (Ser) (covalent) #status !8experimental\ !$299 #binding_site phosphate (Ser) (covalent) #status !8experimental SUMMARY #length 389 #checksum 5305 SEQUENCE /// ENTRY DEHUPT #type complete TITLE pyruvate dehydrogenase (lipoamide) (EC 1.2.4.1) alpha chain precursor, testis-specific - human ALTERNATE_NAMES pyruvate dehydrogenase complex, E1 component alpha chain ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 15-Oct-1999 ACCESSIONS A37104 REFERENCE A37104 !$#authors Dahl, H.H.M.; Brown, R.M.; Hutchison, W.M.; Maragos, C.; !1Brown, G.K. !$#journal Genomics (1990) 8:225-232 !$#title A testis-specific form of the human pyruvate dehydrogenase !1E1alpha subunit is coded for by an intronless gene on !1chromosome 4. !$#cross-references MUID:91065637; PMID:2249846 !$#accession A37104 !'##molecule_type mRNA !'##residues 1-388 ##label DAH !'##cross-references GB:M86808; GB:J04769; NID:g190789; PIDN:AAA60232.1; !1PID:g190790 GENETICS !$#gene GDB:PDHA2 !'##cross-references GDB:120711; OMIM:179061 !$#map_position 4q22-4q23 CLASSIFICATION #superfamily pyruvate dehydrogenase (lipoamide) alpha chain; !1thiamin pyrophosphate-binding domain homology KEYWORDS flavoprotein; heterotetramer; mitochondrion; oxidoreductase; !1phosphoprotein; testis; thiamin pyrophosphate FEATURE !$1-27 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$28-388 #product pyruvate dehydrogenase (lipoamide) alpha !8chain #status predicted #label MAT\ !$183-232 #domain thiamin pyrophosphate-binding domain homology !8#label TPB\ !$230 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$291 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$298 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 388 #molecular-weight 42933 #checksum 3072 SEQUENCE /// ENTRY DEBYPA #type complete TITLE pyruvate dehydrogenase (lipoamide) (EC 1.2.4.1) alpha chain precursor - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YER178w; pyruvate decarboxylase complex component E1 alpha chain ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Dec-1992 #sequence_revision 12-May-1995 #text_change 23-Mar-2001 ACCESSIONS A36743; B36743; S30864; S42685; B38214; S30275; S50681 REFERENCE A36743 !$#authors Behal, R.H.; Browning, K.S.; Reed, L.J. !$#journal Biochem. Biophys. Res. Commun. (1989) 164:941-946 !$#title Nucleotide and deduced amino acid sequence of the alpha !1subunit of yeast pyruvate dehydrogenase. !$#cross-references MUID:90056501; PMID:2684159 !$#accession A36743 !'##molecule_type mRNA !'##residues 24-98,'S',100-443 ##label BEH1 !'##cross-references GB:M29582; NID:g172107; PIDN:AAA34847.1; !1PID:g172108 !$#accession B36743 !'##molecule_type protein !'##residues 56-76;332-345 ##label BEH2 REFERENCE S30812 !$#authors Mulligan, J.T.; Dietrich, F.S.; Hennessey, K.M.; Sehl, P.; !1Komp, C.; Wei, Y.; Taylor, P.; Nakahara, K.; Roberts, D.; !1Davis, R.W. !$#submission submitted to the EMBL Data Library, February 1993 !$#accession S30864 !'##molecule_type DNA !'##residues 24-443 ##label MUL !'##cross-references EMBL:L11229 REFERENCE S42684 !$#authors Wenzel, T.J.; Zuurmond, A.M.; Bergmans, A.; van den Berg, !1J.A.; Steensma, H.Y. !$#journal Yeast (1994) 10:297-308 !$#title Promoter analysis of the PDA1 gene encoding the E1-alpha !1subunit of the pyruvate dehydrogenase complex from !1Saccharomyces cerevisiae. !$#cross-references MUID:94287707; PMID:8017100 !$#accession S42685 !'##molecule_type DNA !'##residues 24-443 ##label WEN !'##cross-references EMBL:X71664; NID:g298058; PIDN:CAA50657.1; !1PID:g298059 REFERENCE A38214 !$#authors Bishop, D.K.; Park, D.; Xu, L.; Kleckner, N. !$#journal Cell (1992) 69:439-456 !$#title DMC1: a meiosis-specific yeast homolog of Escherichia coli !1recA required for recombination, synaptonemal complex !1formation, and cell cycle progression. !$#cross-references MUID:92257586; PMID:1581960 !$#accession B38214 !'##molecule_type DNA !'##residues 358-443 ##label BIS !'##cross-references GB:M87549; NID:g171400; PIDN:AAA34572.1; !1PID:g553126 REFERENCE S30275 !$#authors Kobayashi, T.; Hotta, Y.; Tabata, S. !$#journal Mol. Gen. Genet. (1993) 237:225-232 !$#title Isolation and characterization of a yeast gene that is !1homologous with a meiosis-specific cDNA from a plant. !$#cross-references MUID:93204898; PMID:8455558 !$#accession S30275 !'##molecule_type DNA !'##residues 380-443 ##label KOB !'##cross-references EMBL:D10865; NID:g287607; PIDN:BAA01636.1; !1PID:g287609 REFERENCE S50431 !$#authors Dietrich, F.S. !$#submission submitted to the EMBL Data Library, December 1994 !$#description The sequence of S. cerevisiae cosmids 9163 and 9132. !$#accession S50681 !'##molecule_type DNA !'##residues 1-443 ##label DIE !'##cross-references EMBL:U18922; NID:g603405; PIDN:AAB64705.1; !1PID:g603419; GSPDB:GN00005; MIPS:YER178w GENETICS !$#gene SGD:PDA1; PDH-alpha-1; MIPS:YER178w !'##cross-references SGD:S0000980; MIPS:YER178w !$#map_position 5R !$#genome nuclear CLASSIFICATION #superfamily pyruvate dehydrogenase (lipoamide) alpha chain; !1thiamin pyrophosphate-binding domain homology KEYWORDS flavoprotein; heterotetramer; mitochondrion; oxidoreductase; !1phosphoprotein; thiamin pyrophosphate FEATURE !$1-56 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$57-443 #product pyruvate dehydrogenase (lipoamide) alpha !8chain #status predicted #label MAT\ !$228-277 #domain thiamin pyrophosphate-binding domain homology !8#label TPB\ !$277 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$336 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$343 #binding_site phosphate (Thr) (covalent) #status !8predicted SUMMARY #length 443 #molecular-weight 48891 #checksum 5671 SEQUENCE /// ENTRY DEBSPF #type complete TITLE pyruvate dehydrogenase (lipoamide) (EC 1.2.4.1) E1-alpha chain [validated] - Bacillus stearothermophilus ALTERNATE_NAMES pyruvate dehydrogenase complex, E1 component alpha chain ORGANISM #formal_name Bacillus stearothermophilus DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 21-Jul-2000 ACCESSIONS S10798; A43006; T46889 REFERENCE S10796 !$#authors Hawkins, C.F.; Borges, A.; Perham, R.N. !$#journal Eur. J. Biochem. (1990) 191:337-346 !$#title Cloning and sequence analysis of the genes encoding the !1alpha and beta subunits of the E1 component of the pyruvate !1dehydrogenase multienzyme complex of Bacillus !1stearothermophilus. !$#cross-references MUID:90345939; PMID:2200674 !$#accession S10798 !'##molecule_type DNA !'##residues 1-369 ##label HAW1 !'##cross-references EMBL:X53560; NID:g40038; PIDN:CAA37628.1; !1PID:g40041 !$#accession A43006 !'##molecule_type protein !'##residues 2-35;54-111;269-331 ##label HAW2 REFERENCE S13838 !$#authors Borges, A.; Hawkins, C.F.; Packman, L.C.; Perham, R.N. !$#journal Eur. J. Biochem. (1990) 194:95-102 !$#title Cloning and sequence analysis of the genes encoding the !1dihydrolipoamide acetyltransferase and dihydrolipoamide !1dehydrogenase components of the pyruvate dehydrogenase !1multienzyme complex of Bacillus stearothermophilus. !$#cross-references MUID:91071217; PMID:2253629 !$#accession T46889 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-369 ##label BOR !'##cross-references EMBL:X53560; NID:g40038; PIDN:CAA37628.1; !1PID:g40041 !'##experimental_source strain NCA1503 GENETICS !$#gene pdhA FUNCTION !$#description EC 1.2.4.1 [validated, MUID: 90345939] CLASSIFICATION #superfamily pyruvate dehydrogenase (lipoamide) alpha chain; !1thiamin pyrophosphate-binding domain homology KEYWORDS flavoprotein; oxidoreductase; phosphoprotein; thiamin !1pyrophosphate FEATURE !$2-369 #product pyruvate dehydrogenase (lipoamide) alpha !8chain #status experimental #label MAT\ !$163-212 #domain thiamin pyrophosphate-binding domain homology !8#label TPB SUMMARY #length 369 #molecular-weight 41469 #checksum 8802 SEQUENCE /// ENTRY DEBSPA #type complete TITLE pyruvate dehydrogenase (lipoamide) (EC 1.2.4.1) alpha chain - Bacillus subtilis ALTERNATE_NAMES pyruvate dehydrogenase complex, E1 component alpha chain ORGANISM #formal_name Bacillus subtilis DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jun-2000 ACCESSIONS B36718; H69673 REFERENCE A36718 !$#authors Hemilae, H.; Palva, A.; Paulin, L.; Arvidson, S.; Palva, I. !$#journal J. Bacteriol. (1990) 172:5052-5063 !$#title Secretory S complex of Bacillus subtilis: sequence analysis !1and identity to pyruvate dehydrogenase. !$#cross-references MUID:90368558; PMID:1697575 !$#accession B36718 !'##molecule_type DNA !'##residues 1-371 ##label HEM !'##cross-references GB:M57435; GB:M31542; NID:g143375; PIDN:AAA62681.1; !1PID:g143377 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69673 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-178,'A',180-371 ##label KUN !'##cross-references GB:Z99111; GB:AL009126; NID:g2633699; !1PIDN:CAB13331.1; PID:g2633829 !'##experimental_source strain 168 GENETICS !$#gene pdhA FUNCTION !$#description catalyzes the decarboxylation of pyruvate coupled with !1formation of S-acetyldihydrolipoamide from lipoamide !$#pathway glycolysis !$#note uses thiamine diphosphate as a cofactor CLASSIFICATION #superfamily pyruvate dehydrogenase (lipoamide) alpha chain; !1thiamin pyrophosphate-binding domain homology KEYWORDS flavoprotein; glycolysis; oxidoreductase; phosphoprotein; !1thiamin pyrophosphate FEATURE !$2-371 #product pyruvate dehydrogenase (lipoamide) alpha !8chain #status predicted #label MAT\ !$165-212 #domain thiamin pyrophosphate-binding domain homology !8#label TPB SUMMARY #length 371 #molecular-weight 41633 #checksum 8923 SEQUENCE /// ENTRY DEHUXA #type complete TITLE 3-methyl-2-oxobutanoate dehydrogenase (lipoamide) (EC 1.2.4.4) alpha chain precursor - human ALTERNATE_NAMES 2-oxoisovalerate dehydrogenase (lipoamide) E1-alpha chain; branched-chain alpha-keto acid decarboxylase complex E1-alpha chain ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1992 #sequence_revision 22-Nov-1996 #text_change 05-Nov-1999 ACCESSIONS S27156; S25017; A30783; A33311; JT0335; S15868; S50201; !1A30841 REFERENCE S27156 !$#authors McKean, M.C.; Winkeler, K.A.; Danner, D.J. !$#journal Biochim. Biophys. Acta (1992) 1171:109-112 !$#title Nucleotide sequence of the 5' end including the initiation !1codon of cDNA for the E1alpha subunit of the human branched !1chain alpha-ketoacid dehydrogenase complex. !$#cross-references MUID:93041997; PMID:1420356 !$#accession S27156 !'##molecule_type mRNA !'##residues 1-445 ##label MCK1 !'##cross-references EMBL:Z14093; NID:g29390; PIDN:CAA78475.1; !1PID:g29391 REFERENCE S25017 !$#authors McKean, M.; Winkeler, K.A.; Danner, D.J. !$#submission submitted to the EMBL Data Library, July 1992 !$#accession S25017 !'##molecule_type mRNA !'##residues 1-35,'A',37-445 ##label MCK2 !'##cross-references EMBL:Z14093 REFERENCE A30783 !$#authors Fisher, C.W.; Chuang, J.L.; Griffin, T.A.; Lau, K.S.; Cox, !1R.P.; Chuang, D.T. !$#submission submitted to GenBank, November 1988 !$#accession A30783 !'##molecule_type mRNA !'##residues 'GG',4-35,'A',37-445 ##label FIS1 !'##cross-references GB:J03759 REFERENCE A33311 !$#authors Fisher, C.W.; Chuang, J.L.; Griffin, T.A.; Lau, K.S.; Cox, !1R.P.; Chuang, D.T. !$#journal J. Biol. Chem. (1989) 264:3448-3453 !$#title Molecular phenotypes in cultured maple syrup urine disease !1cells. Complete E-1alpha-cDNA sequence and mRNA and subunit !1contents of the human branched chain alpha-keto acid !1dehydrogenase complex. !$#cross-references MUID:89123475; PMID:2914958 !$#accession A33311 !'##molecule_type mRNA !'##residues 'G',4-35,'A',37-445 ##label FIS2 !'##cross-references GB:J04474 REFERENCE JT0335 !$#authors Zhang, B.; Crabb, D.W.; Harris, R.A. !$#journal Gene (1988) 69:159-164 !$#title Nucleotide and deduced amino acid sequence of the E1 alpha !1subunit of human liver branched-chain alpha-ketoacid !1dehydrogenase. !$#cross-references MUID:89137989; PMID:3224821 !$#accession JT0335 !'##molecule_type mRNA !'##residues 68-247,'D',249-445 ##label ZHA !'##cross-references GB:M22221; NID:g179359; PIDN:AAA35590.1; !1PID:g179360 REFERENCE S15868 !$#authors Dariush, N.; Fisher, C.W.; Cox, R.P.; Chuang, D.T. !$#journal FEBS Lett. (1991) 284:34-38 !$#title Structure of the gene encoding the entire mature E1-alpha !1subunit of human branched-chain alpha-keto acid !1dehydrogenase complex. !$#cross-references MUID:91285101; PMID:2060625 !$#accession S15868 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 'G',4-128,'F',130-445 ##label DAR !'##note sequence display was clarified in reference S18468 REFERENCE S18468 !$#authors Dariush, N.; Fisher, C.W.; Cox, R.P.; Chuang, D.T. !$#journal FEBS Lett. (1991) 291:376-376 !$#title Corrigendum. Structure of the gene encoding the entire !1mature E1-alpha subunit of human branched-chain alpha-keto !1acid dehydrogenase complex. !$#cross-references MUID:92038074; PMID:1682165 !$#contents annotation; this reference clarifies the sequence display in !1reference S15868 REFERENCE S50200 !$#authors Wynn, R.M.; Kochi, H.; Cox, R.P.; Chuang, D.T. !$#journal Biochim. Biophys. Acta (1994) 1201:125-128 !$#title Differential processing of human and rat E1-alpha precursors !1of the branched-chain alpha-keto acid dehydrogenase complex !1caused by an N-terminal proline in the rat sequence. !$#cross-references MUID:95002090; PMID:7918575 !$#accession S50201 !'##molecule_type protein !'##residues 31-57 ##label WYN COMMENT This enzyme is a component of a multi-subunit complex that !1catalyzes the conversion of alpha-keto acids to acyl-CoA and !1carbon dioxide. The E1 component, composed of alpha and beta !1chains, catalyzes the formation of S- !1(2-methylpropanoyl)dihydrolipoamide from !13-methyl-2-oxobutanoate and lipoamide. GENETICS !$#gene GDB:OVD1A !'##cross-references GDB:118849 !$#map_position 14q21-14q22 !$#introns 36/3; 96/3; 125/3; 162/1; 216/1; 285/1; 332/2; 389/3 CLASSIFICATION #superfamily pyruvate dehydrogenase (lipoamide) alpha chain; !1thiamin pyrophosphate-binding domain homology KEYWORDS heterodimer; mitochondrion; oxidoreductase; phosphoprotein; !1thiamin pyrophosphate FEATURE !$1-45 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$46-445 #product 3-methyl-2-oxobutanoate dehydrogenase !8(lipoamide) alpha chain #status predicted #label MAT\ !$227-276 #domain thiamin pyrophosphate-binding domain homology !8#label TPB\ !$337 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$347 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 445 #molecular-weight 50471 #checksum 3018 SEQUENCE /// ENTRY DEBOXA #type complete TITLE 3-methyl-2-oxobutanoate dehydrogenase (lipoamide) (EC 1.2.4.4) alpha chain precursor - bovine ALTERNATE_NAMES 2-oxoisovalerate dehydrogenase (lipoamide) E1-alpha chain; branched-chain alpha-keto acid decarboxylase complex E1-alpha chain ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 15-Oct-1999 ACCESSIONS A28073 REFERENCE A28073 !$#authors Hu, C.W.C.; Lau, K.S.; Griffin, T.A.; Chuang, J.L.; Fisher, !1C.W.; Cox, R.P.; Chuang, D.T. !$#journal J. Biol. Chem. (1988) 263:9007-9014 !$#title Isolation and sequencing of a cDNA encoding the !1decarboxylase (E1)-alpha precursor of bovine branched-chain !1alpha-keto acid dehydrogenase complex. Expression of !1E1-alpha mRNA and subunit in maple-syrup-urine-disease and !13T3-L1 cells. !$#cross-references MUID:88243770; PMID:3379058 !$#accession A28073 !'##molecule_type mRNA !'##residues 1-455 ##label HUC !'##cross-references GB:J03759; NID:g163238; PIDN:AAA30595.1; !1PID:g163239 CLASSIFICATION #superfamily pyruvate dehydrogenase (lipoamide) alpha chain; !1thiamin pyrophosphate-binding domain homology KEYWORDS heterodimer; mitochondrion; oxidoreductase; phosphoprotein; !1thiamin pyrophosphate FEATURE !$1-55 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$56-455 #product 3-methyl-2-oxobutanoate dehydrogenase !8(lipoamide) alpha chain #status predicted #label MAT\ !$237-284 #domain thiamin pyrophosphate-binding domain homology !8#label TPB\ !$347 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$357 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 455 #molecular-weight 51678 #checksum 4630 SEQUENCE /// ENTRY DERTXA #type fragment TITLE 3-methyl-2-oxobutanoate dehydrogenase (lipoamide) (EC 1.2.4.4) alpha chain precursor - rat (fragment) ALTERNATE_NAMES 2-oxoisovalerate dehydrogenase (lipoamide) E1-alpha chain; branched-chain alpha-keto acid decarboxylase complex E1-alpha chain ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 15-Oct-1999 ACCESSIONS A29468 REFERENCE A29468 !$#authors Zhang, B.; Kuntz, M.J.; Goodwin, G.W.; Harris, R.A.; Crabb, !1D.W. !$#journal J. Biol. Chem. (1987) 262:15220-15224 !$#title Molecular cloning of a cDNA for the E1-alpha subunit of rat !1liver branched chain alpha-ketoacid dehydrogenase. !$#cross-references MUID:88033108; PMID:2822716 !$#accession A29468 !'##molecule_type mRNA !'##residues 1-441 ##label ZHA !'##cross-references GB:J02827; NID:g203120; PIDN:AAA40811.1; !1PID:g203121 CLASSIFICATION #superfamily pyruvate dehydrogenase (lipoamide) alpha chain; !1thiamin pyrophosphate-binding domain homology KEYWORDS heterodimer; mitochondrion; oxidoreductase; phosphoprotein; !1thiamin pyrophosphate FEATURE !$1-40 #domain transit peptide (mitochondrion) (fragment) !8#status predicted #label TNP\ !$41-441 #product 3-methyl-2-oxobutanoate dehydrogenase !8(lipoamide) alpha chain #status predicted #label MAT\ !$223-270 #domain thiamin pyrophosphate-binding domain homology !8#label TPB\ !$333 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$343 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 441 #checksum 8882 SEQUENCE /// ENTRY DEPSXA #type complete TITLE 3-methyl-2-oxobutanoate dehydrogenase (lipoamide) (EC 1.2.4.4) alpha chain - Pseudomonas putida ALTERNATE_NAMES 2-oxoisovalerate dehydrogenase (lipoamide) E1-alpha chain; branched-chain alpha-keto acid decarboxylase complex E1-alpha chain ORGANISM #formal_name Pseudomonas putida DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 05-Nov-1999 ACCESSIONS S01317; B36133; S63475 REFERENCE S01317 !$#authors Burns, G.; Brown, T.; Hatter, K.; Idriss, J.M.; Sokatch, !1J.R. !$#journal Eur. J. Biochem. (1988) 176:311-317 !$#title Similarity of the E1 subunits of branched-chain-oxoacid !1dehydrogenase from Pseudomonas putida to the corresponding !1subunits of mammalian branched-chain-oxoacid and pyruvate !1dehydrogenases. !$#cross-references MUID:88329084; PMID:3416875 !$#accession S01317 !'##molecule_type DNA !'##residues 1-410 ##label BUR !'##cross-references EMBL:X13004 REFERENCE A36133 !$#authors Madhusudhan, K.T.; Huang, G.; Burns, G.; Sokatch, J.R. !$#journal J. Bacteriol. (1990) 172:5655-5663 !$#title Transcriptional analysis of the promoter region of the !1Pseudomonas putida branched-chain keto acid dehydrogenase !1operon. !$#cross-references MUID:91008935; PMID:2211503 !$#accession B36133 !'##status preliminary !'##molecule_type DNA !'##residues 1-17 ##label MAD !'##cross-references GB:M33715 REFERENCE S63475 !$#authors Hester, K.; Luo, J.; Burns, G.; Braswell, E.H.; Sokatch, !1J.R. !$#journal Eur. J. Biochem. (1995) 233:828-836 !$#title Purification of active E1-alpha(2)-beta(2) of Pseudomonas !1putida branched-chain-oxoacid dehydrogenase. !$#cross-references MUID:96085147; PMID:8521848 !$#accession S63475 !'##status preliminary !'##molecule_type protein !'##residues 1-13 ##label HES GENETICS !$#gene bkdA1 CLASSIFICATION #superfamily pyruvate dehydrogenase (lipoamide) alpha chain; !1thiamin pyrophosphate-binding domain homology KEYWORDS lipoamide; oxidoreductase; phosphoprotein; thiamin !1pyrophosphate FEATURE !$2-410 #product 3-methyl-2-oxobutanoate dehydrogenase !8(lipoamide) alpha chain #status predicted #label MAT\ !$202-251 #domain thiamin pyrophosphate-binding domain homology !8#label TPB\ !$313 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 410 #molecular-weight 45284 #checksum 669 SEQUENCE /// ENTRY DEALXE #type complete TITLE acetoin[2,6-dichlorophenolindophenol] oxidoreductase (EC 1.-.-.-) alpha chain - Alcaligenes eutrophus (strain H16) ORGANISM #formal_name Alcaligenes eutrophus DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 15-Oct-1999 ACCESSIONS B42462 REFERENCE A42462 !$#authors Priefert, H.; Hein, S.; Krueger, N.; Zeh, K.; Schmidt, B.; !1Steinbuechel, A. !$#journal J. Bacteriol. (1991) 173:4056-4071 !$#title Identification and molecular characterization of the !1Alcaligenes eutrophus H16 aco operon genes involved in !1acetoin catabolism. !$#cross-references MUID:91286190; PMID:2061286 !$#accession B42462 !'##molecule_type DNA !'##residues 1-333 ##label PRI !'##cross-references GB:M66060; NID:g141892; PIDN:AAA21948.1; !1PID:g141894 COMMENT This is a component of the enzyme complex that catalyzes 2, !16-dichlorophenolindophenol-dependent cleavage of acetoin !1into acetate and acetaldehyde. The functional enzyme is a !1tetramer of two alpha and two beta chains. CLASSIFICATION #superfamily pyruvate dehydrogenase (lipoamide) alpha chain; !1thiamin pyrophosphate-binding domain homology KEYWORDS heterotetramer; oxidoreductase FEATURE !$145-194 #domain thiamin pyrophosphate-binding domain homology !8#label TPB SUMMARY #length 333 #molecular-weight 35375 #checksum 2647 SEQUENCE /// ENTRY C25937 #type complete TITLE arsenate reductase (EC 1.-.-.-) - Escherichia coli plasmid R773 ALTERNATE_NAMES arsenical pump modifier protein ORGANISM #formal_name Escherichia coli DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 11-Jun-1999 ACCESSIONS C25937; S13901 REFERENCE A92563 !$#authors Chen, C.M.; Misra, T.K.; Silver, S.; Rosen, B.P. !$#journal J. Biol. Chem. (1986) 261:15030-15038 !$#title Nucleotide sequence of the structural genes for an anion !1pump. !$#cross-references MUID:87033737; PMID:3021763 !$#accession C25937 !'##molecule_type DNA !'##residues 1-141 ##label CHE !'##cross-references GB:J02591; NID:g151856; PIDN:AAA21096.1; !1PID:g151859 REFERENCE S13901 !$#authors Rosen, B.P.; Weigel, U.; Monticello, R.A.; Edwards, B.P.F. !$#journal Arch. Biochem. Biophys. (1991) 284:381-385 !$#title Molecular analysis of an anion pump: purification of the !1ArsC protein. !$#cross-references MUID:91112837; PMID:1703401 !$#accession S13901 !'##status preliminary !'##molecule_type protein !'##residues 5-11,'X',13 ##label ROS GENETICS !$#gene arsC !$#genome plasmid FUNCTION !$#description catalyzes the reduction of arsenate [As(V)] to arsenite [As !1(III)] !$#pathway expands the substrate specificity of the arsAB pump CLASSIFICATION #superfamily Escherichia coli arsenate reductase KEYWORDS oxidoreductase; toxic oxyanion resistance SUMMARY #length 141 #molecular-weight 15830 #checksum 1621 SEQUENCE /// ENTRY C56269 #type complete TITLE arsenate reductase (EC 1.-.-.-) - Escherichia coli (strain K-12) ALTERNATE_NAMES arsenical pump modifier ORGANISM #formal_name Escherichia coli DATE 03-Oct-1995 #sequence_revision 03-Nov-1995 #text_change 01-Mar-2002 ACCESSIONS C56269; S47722; B65148 REFERENCE A56269 !$#authors Diorio, C.; Cai, J.; Marmor, J.; Shinder, R.; DuBow, M.S. !$#journal J. Bacteriol. (1995) 177:2050-2056 !$#title An Escherichia coli chromosomal ars operon homolog is !1functional in arsenic detoxification and is conserved in !1gram-negative bacteria. !$#cross-references MUID:95238276; PMID:7721697 !$#accession C56269 !'##molecule_type DNA !'##residues 1-141 ##label DIO !'##cross-references GB:X80057; NID:g510824; PIDN:CAA56363.1; !1PID:g516212 REFERENCE S47666 !$#authors Plunkett, G. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S47722 !'##molecule_type DNA !'##residues 1-141 ##label PLU !'##cross-references EMBL:U00039; NID:g466582; PIDN:AAB18479.1; !1PID:g466640 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65148 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-141 ##label BLAT !'##cross-references GB:AE000426; GB:U00096; NID:g1789910; !1PIDN:AAC76528.1; PID:g1789918; UWGP:b3503 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene arsC !$#map_position 80 min FUNCTION !$#description catalyzes the reduction of arsenate [As(V)] to arsenite [As !1(III)] CLASSIFICATION #superfamily Escherichia coli arsenate reductase KEYWORDS oxidoreductase; toxic oxyanion resistance SUMMARY #length 141 #molecular-weight 15853 #checksum 1685 SEQUENCE /// ENTRY DEHUPB #type complete TITLE pyruvate dehydrogenase (lipoamide) (EC 1.2.4.1) beta chain precursor, long splice form [validated] - human ALTERNATE_NAMES protein DKFZp564K0164.1; pyruvate dehydrogenase (PDH) complex, E1 component beta chain CONTAINS pyruvate dehydrogenase (lipoamide) beta chain precursor, short splice form ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1989 #sequence_revision 19-Oct-1995 #text_change 08-Dec-2000 ACCESSIONS JU0145; S13825; A36631; B28398; A35952; A27712; A60729; !1T17327 REFERENCE JU0145 !$#authors Ho, L.; Patel, M.S. !$#journal Gene (1990) 86:297-302 !$#title Cloning and cDNA sequence of the beta-subunit component of !1human pyruvate dehydrogenase complex. !$#cross-references MUID:90215313; PMID:2323578 !$#accession JU0145 !'##molecule_type mRNA !'##residues 5-359 ##label HO1 !'##cross-references GB:M34479; NID:g189759; PIDN:AAA36428.1; !1PID:g189760 !'##note the sequence in GenBank entry HUMPDHBA, release 114.0, !1(PIDN:AAA36428.1) includes residues 1-4 that were reported !1elsewhere and not determined in this work REFERENCE S13825 !$#authors Chun, K.; Mackay, N.; Willard, H.F.; Robinson, B.H. !$#journal Eur. J. Biochem. (1990) 194:587-592 !$#title Isolation, characterization and chromosomal localization of !1cDNA clones for the E(1)beta subunit of the pyruvate !1dehydrogenase complex. !$#cross-references MUID:91099335; PMID:1702713 !$#accession S13825 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-359 ##label CHU !'##cross-references GB:X57778; NID:g31070; PIDN:CAA40924.1; PID:g31071 REFERENCE A36631 !$#authors Huh, T.L.; Casazza, J.P.; Huh, J.W.; Chi, Y.T.; Song, B.J. !$#journal J. Biol. Chem. (1990) 265:13320-13326 !$#title Characterization of two cDNA clones for pyruvate !1dehydrogenase E-1beta subunit and its regulation in !1tricarboxylic acid cycle-deficient fibroblast. !$#cross-references MUID:90330681; PMID:2376596 !$#accession A36631 !'##status preliminary !'##molecule_type mRNA !'##residues 1-30,'V',32-359 ##label HUH !'##cross-references GB:M54788; NID:g189761; PIDN:AAA60053.1; !1PID:g189762 REFERENCE A94198 !$#authors Koike, K.; Ohta, S.; Urata, Y.; Kagawa, Y.; Koike, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:41-45 !$#title Cloning and sequencing of cDNAs encoding alpha and beta !1subunits of human pyruvate dehydrogenase. !$#cross-references MUID:88124815; PMID:3422424 !$#accession B28398 !'##molecule_type mRNA !'##residues 1-8,'AETPS',14-30,'V',32-212,'LRKLSQ',219,'IL',222-309, !1'NGS',313-359 ##label KOI1 !'##cross-references GB:J03576; PID:g189753 !'##note the authors translated the codon CAG for residue 160 as Gly REFERENCE A35952 !$#authors Koike, K.; Urata, Y.; Koike, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:5594-5597 !$#title Molecular cloning and characterization of human pyruvate !1dehydrogenase beta subunit gene. !$#cross-references MUID:90332628; PMID:2377599 !$#accession A35952 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-212,'L',214-359 ##label KOI2 !'##cross-references GB:J03576; PID:g189753; PIDN:AAA88097.1; !1PID:g189754; GB:D90086; NID:g219983; PIDN:BAA14123.1; !1PID:g219984 !'##experimental_source note Alu repeat 1; note beta subunit mRNA and !1introns; note beta subunit exon 1 !'##note neither the complete nucleic acid sequence nor the complete !1translation are shown REFERENCE A90140 !$#authors Ho, L.; Javed, A.A.; Pepin, R.A.; Thekkumkara, T.J.; !1Raefsky, C.; Mole, J.E.; Caliendo, A.M.; Kwon, M.S.; Kerr, !1D.S.; Patel, M.S. !$#journal Biochem. Biophys. Res. Commun. (1988) 150:904-908 !$#title Identification of a cDNA clone for the beta-subunit of the !1pyruvate dehydrogenase component of human pyruvate !1dehydrogenase complex. !$#cross-references MUID:88134251; PMID:2829898 !$#accession A27712 !'##molecule_type mRNA !'##residues 23-69,'RSRAVEEIW' ##label HOL !'##cross-references GB:M19123; NID:g189755; PIDN:AAA60052.1; !1PID:g189758 !'##note the last eight residues of this fragment differ from the !1canonical sequence by an apparent frame shift REFERENCE A60729 !$#authors Muno, D.; Kominami, E.; Ishii, H.; Usui, K.; Saifuku, K.; !1Sakakibara, Y.; Namihisa, T. !$#journal Hepatology (1990) 11:16-23 !$#title Isolation of tryptic fragment of antigen from mitochondrial !1inner membrane proteins reacting with antimitochondrial !1antibody in sera of patients with primary biliary cirrhosis. !$#cross-references MUID:90109038; PMID:2295468 !$#accession A60729 !'##molecule_type protein !'##residues 31-35,'QE',38-45,'X',47,'XV',50-55 ##label MUN REFERENCE Z18727 !$#authors Duesterhoeft, A.; Lauber, J.; Mewes, H.W.; Gassenhuber, J.; !1Wiemann, S. !$#submission submitted to the Protein Sequence Database, September 1999 !$#accession T17327 !'##molecule_type mRNA !'##residues 1-15,34-359 ##label DUE !'##cross-references EMBL:AL117618; NID:g5912196; PIDN:CAB56017.1; !1PID:g5912197 !'##experimental_source fetal brain; clone DKFZp564K0164 GENETICS !$#gene GDB:PDHB; DKFZp564K0164.1 !'##cross-references GDB:120268; OMIM:179060 !$#map_position 3p21.1-3p14.2 !$#introns 14/3; 32/3; 68/3; 89/3; 101/3; 197/1; 234/1; 264/3; 312/1 COMPLEX the E1 component (pyruvate dehydrogenase) is a !1heterotetramer of two alpha (see PIR:DEHUPA) and two beta !1chains; 30 E1 components form a complex with 60 E2 component !1(dihydrolipoamide acetyltransferase) monomers and 6 E3 !1component (lipoamide dehydrogenase) dimers FUNCTION !$#description catalyzes the reaction of pyruvate and lipoamide (on the E2 !1component) to form s-acetyldihydrolipoamide and carbon !1dioxide; the complex overall catalyzes the oxidative !1decarboxylation of pyruvate by NAD to form acetyl-CoA, !1carbon dioxide and NADH !$#pathway pyruvate metabolism !$#note thiamin pyrophosphate bound by the alpha chain is a cofactor CLASSIFICATION #superfamily pyruvate dehydrogenase (lipoamide) beta chain KEYWORDS alternative splicing; flavoprotein; heterotetramer; !1mitochondrion; oxidoreductase; thiamin pyrophosphate FEATURE !$1-359 #product pyruvate dehydrogenase (lipoamide) beta !8chain precursor, long splice form #status predicted !8#label SPL\ !$1-30 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$1-15,34-359 #product pyruvate dehydrogenase (lipoamide) beta !8chain precursor, short splice form #status predicted !8#label SPS\ !$31-359 #product pyruvate dehydrogenase (lipoamide) beta !8chain #status experimental #label MAT SUMMARY #length 359 #molecular-weight 39233 #checksum 6560 SEQUENCE /// ENTRY S46097 #type complete TITLE pyruvate dehydrogenase (lipoamide) (EC 1.2.4.1) beta chain precursor - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YBR1511; protein YBR221c; pyruvate dehydrogenase complex, E1 component beta chain ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-Nov-1999 ACCESSIONS S46097; A47273; B47273 REFERENCE S45782 !$#authors Dubois, E.; El Bakkoury, M.; Glansdorff, N.; Messenguy, F.; !1Pierard, A.; Scherens, B.; Vierendeels, F. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S46097 !'##molecule_type DNA !'##residues 1-366 ##label DUB !'##cross-references EMBL:Z36090; NID:g536612; PIDN:CAA85184.1; !1PID:g536613; GSPDB:GN00002; MIPS:YBR221c !'##experimental_source strain S288C REFERENCE A47273 !$#authors Miran, S.G.; Lawson, J.E.; Reed, L.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:1252-1256 !$#title Characterization of PDH beta 1, the structural gene for the !1pyruvate dehydrogenase beta subunit from Saccharomyces !1cerevisiae. !$#cross-references MUID:93165675; PMID:8433986 !$#accession A47273 !'##molecule_type DNA !'##residues 1-159,'L',161-366 ##label MIR !'##cross-references EMBL:M98476; NID:g171428; PIDN:AAA34583.1; !1PID:g171429 !'##note sequence extracted from NCBI backbone (NCBIN:124865, !1NCBIP:124866) !$#accession B47273 !'##molecule_type protein !'##residues 34-54;206-219 ##label MI2 GENETICS !$#gene SGD:PDB1; MIPS:YBR221c !'##cross-references SGD:S0000425; MIPS:YBR221c !$#map_position 2R CLASSIFICATION #superfamily pyruvate dehydrogenase (lipoamide) beta chain KEYWORDS flavoprotein; mitochondrion; oxidoreductase; thiamin !1pyrophosphate FEATURE !$1-33 #domain transit peptide (mitochondrion) #status !8experimental #label TNP\ !$34-366 #product pyruvate dehydrogenase (lipoamide) beta !8chain #status experimental #label MAT SUMMARY #length 366 #molecular-weight 40053 #checksum 4977 SEQUENCE /// ENTRY JC4080 #type complete TITLE pyruvate dehydrogenase (lipoamide) (EC 1.2.4.1) E1 beta chain - fission yeast (Schizosaccharomyces pombe) ORGANISM #formal_name Schizosaccharomyces pombe DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Dec-1999 ACCESSIONS JC4080; T40183 REFERENCE JC4080 !$#authors Cavan, G.; MacDonald, D. !$#journal Gene (1995) 152:117-120 !$#title Cloning and sequence of a gene encoding the pyruvate !1dehydrogenase E1 beta subunit of Schizosaccharomyces pombe. !$#cross-references MUID:95129904; PMID:7828917 !$#accession JC4080 !'##molecule_type DNA !'##residues 1-366 ##label CAV !'##cross-references EMBL:X75648; NID:g515933; PIDN:CAA53303.1; !1PID:g515934 !'##note The authors translated the codon ACC for residue 39 as Trp, CAA !1for residue 165 as Gly, GGT for residue 266 as Gln and TTA !1for residue 280 as Phe REFERENCE Z21910 !$#authors Wood, V.; Rajandream, M.A.; Barrell, B.G.; Lauber, J.; !1Hilbert, H.; Duesterhoeft, A. !$#submission submitted to the EMBL Data Library, February 1998 !$#accession T40183 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-366 ##label WOO !'##cross-references EMBL:Z97992; PIDN:CAB10808.1; GSPDB:GN00067; !1SPDB:SPBC30D10.13c !'##experimental_source strain 972h-; cosmid c30D10 GENETICS !$#gene SPBC30D10.13c !$#map_position 2 !$#genome nuclear CLASSIFICATION #superfamily pyruvate dehydrogenase (lipoamide) beta chain KEYWORDS oxidoreductase SUMMARY #length 366 #molecular-weight 39623 #checksum 2589 SEQUENCE /// ENTRY S28950 #type fragment TITLE 3-methyl-2-oxobutanoate dehydrogenase (lipoamide) (EC 1.2.4.4) chain E1-beta precursor - rat (fragment) ALTERNATE_NAMES branched-chain alpha-keto acid dehydrogenase E1-beta chain ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 11-Jun-1999 ACCESSIONS S28950; S38859; S30870; S52471 REFERENCE S28950 !$#authors Zhao, Y.; Kuntz, M.J.; Harris, R.A.; Crabb, D.W. !$#journal Biochim. Biophys. Acta (1992) 1132:207-210 !$#title Molecular cloning of the E1beta subunit of the rat branched !1chain alpha-ketoacid dehydrogenase. !$#cross-references MUID:93003326; PMID:1390893 !$#accession S28950 !'##molecule_type mRNA !'##residues 1-369 ##label ZHA1 !'##cross-references EMBL:M94040; NID:g202807; PIDN:AAA73899.1; !1PID:g202808 !'##note the amino acid sequence from Fig. 1 is inconsistent with the !1nucleotide sequence from Fig. 1 in having a double !1frameshift; the second base in the codon for 80-Val is !1missing and the codon for 100-Pro is given as CCCG; the !1sequence shown follows the authors' translation; the !1nucleotide sequence has been revised in S52471 !$#accession S38859 !'##molecule_type protein !'##residues 28-54 ##label ZHA2 REFERENCE S52471 !$#authors Zhao, Y.; Kuntz, M.J.; Harris, R.A.; Crabb, D.W. !$#journal Biochim. Biophys. Acta (1995) 1260:243 !$#cross-references MUID:95143286; PMID:7841205 !$#contents annotation; nucleotide sequence revision !$#note this is a revision to the nucleotide sequence from reference !1S28950 GENETICS !$#genome nuclear CLASSIFICATION #superfamily pyruvate dehydrogenase (lipoamide) beta chain KEYWORDS mitochondrion; oxidoreductase FEATURE !$1-27 #domain transit peptide (mitochondrion) (fragment) !8#status predicted #label TRN\ !$28-369 #product 3-methyl-2-oxobutanoate dehydrogenase !8(lipoamide) chain E1-beta #status experimental #label !8MAT SUMMARY #length 369 #checksum 1115 SEQUENCE /// ENTRY A34267 #type complete TITLE 3-methyl-2-oxobutanoate dehydrogenase (lipoamide) (EC 1.2.4.4) E1 beta chain precursor - bovine ALTERNATE_NAMES branched-chain alpha-keto acid dehydrogenase E1-beta chain ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A34267; A42048 REFERENCE A34267 !$#authors Nobukuni, Y.; Mitsubuchi, H.; Endo, F.; Asaka, J.; Oyama, !1R.; Titani, K.; Matsuda, I. !$#journal Biochemistry (1990) 29:1154-1160 !$#title Isolation and characterization of a complementary DNA clone !1coding for the E-1-beta subunit of the bovine branched-chain !1alpha-ketoacid dehydrogenase complex: complete amino acid !1sequence of the precursor protein and its proteolytic !1processing. !$#cross-references MUID:90212602; PMID:2322554 !$#accession A34267 !'##molecule_type mRNA !'##residues 1-392 ##label NOB !'##cross-references GB:M33323; NID:g506802; PIDN:AAA30407.1; !1PID:g506803 !'##experimental_source liver REFERENCE A42048 !$#authors Wynn, R.M.; Chuang, J.L.; Davie, J.R.; Fisher, C.W.; Hale, !1M.A.; Cox, R.P.; Chuang, D.T. !$#journal J. Biol. Chem. (1992) 267:1881-1887 !$#title Cloning and expression in Escherichia coli of mature E1 beta !1subunit of bovine mitochondrial branched-chain alpha-keto !1acid dehydrogenase complex. Mapping of the E1 beta-binding !1region on E2. !$#cross-references MUID:92112917; PMID:1730724 !$#accession A42048 !'##molecule_type mRNA !'##residues 21-22,25-282,'E',284-287,'A',289-392 ##label WYN !'##cross-references GB:M81742 !'##experimental_source liver !'##note sequence extracted from NCBI backbone (NCBIN:76036, !1NCBIP:76039) CLASSIFICATION #superfamily pyruvate dehydrogenase (lipoamide) beta chain KEYWORDS mitochondrion; oxidoreductase FEATURE !$1-50 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$51-392 #product 3-methyl-2-oxobutanoate dehydrogenase !8(lipoamide) E1 beta chain #status predicted #label !8MAT SUMMARY #length 392 #molecular-weight 42979 #checksum 703 SEQUENCE /// ENTRY A37157 #type complete TITLE 3-methyl-2-oxobutanoate dehydrogenase (lipoamide) (EC 1.2.4.4) E1-beta chain precursor - human ALTERNATE_NAMES alpha-keto dehydrogenase E1 beta chain ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A37157; S09081; S38937; S50202 REFERENCE A37157 !$#authors Nobukuni, Y.; Mitsubuchi, H.; Endo, F.; Akaboshi, I.; Asaka, !1J.; Matsuda, I. !$#journal J. Clin. Invest. (1990) 86:242-247 !$#title Maple syrup urine disease. Complete primary structure of the !1E-1beta subunit of human branched chain alpha-ketoacid !1dehydrogenase complex deduced from the nucleotide sequence !1and a gene analysis of patients with this disease. !$#cross-references MUID:90307967; PMID:2365818 !$#accession A37157 !'##molecule_type mRNA !'##residues 1-392 ##label NOB !'##cross-references GB:M55575; NID:g179361; PIDN:AAA51812.1; !1PID:g179362 !'##experimental_source placenta REFERENCE S09081 !$#authors Chuang, J.L.; Cox, R.P.; Chuang, D.T. !$#journal FEBS Lett. (1990) 262:305-309 !$#title Molecular cloning of the mature E1b-beta subunit of human !1branched-chain alpha-keto acid dehydrogenase complex. !$#cross-references MUID:90242952; PMID:2335211 !$#accession S09081 !'##molecule_type mRNA !'##residues 'RLPP',24-321,'S',323-392 ##label CHU !'##cross-references EMBL:X52446; NID:g30945; PIDN:CAA36685.1; !1PID:g747713 !$#accession S38937 !'##molecule_type protein !'##residues 51-78,290-298 ##label CH2 REFERENCE S50200 !$#authors Wynn, R.M.; Kochi, H.; Cox, R.P.; Chuang, D.T. !$#journal Biochim. Biophys. Acta (1994) 1201:125-128 !$#title Differential processing of human and rat E1-alpha precursors !1of the branched-chain alpha-keto acid dehydrogenase complex !1caused by an N-terminal proline in the rat sequence. !$#cross-references MUID:95002090; PMID:7918575 !$#accession S50202 !'##status preliminary !'##molecule_type protein !'##residues 36-62 ##label WYN GENETICS !$#gene GDB:BCKDHB !'##cross-references GDB:118759; OMIM:248611 !$#map_position 6p22-6p21 !$#note a defect in this gene can result in maple syrup urine !1disease CLASSIFICATION #superfamily pyruvate dehydrogenase (lipoamide) beta chain KEYWORDS mitochondrion; oxidoreductase FEATURE !$1-50 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$51-392 #product 3-methyl-2-oxobutanoate dehydrogenase !8(lipoamide) E1 beta chain #status predicted #label !8MAT SUMMARY #length 392 #molecular-weight 43122 #checksum 7648 SEQUENCE /// ENTRY DEPSEB #type complete TITLE 3-methyl-2-oxobutanoate dehydrogenase (lipoamide) (EC 1.2.4.4) chain E1-beta - Pseudomonas putida ALTERNATE_NAMES branched-chain oxoacid dehydrogenase chain E1-beta ORGANISM #formal_name Pseudomonas putida DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 11-Jun-1999 ACCESSIONS S01318; S05058 REFERENCE S01317 !$#authors Burns, G.; Brown, T.; Hatter, K.; Idriss, J.M.; Sokatch, !1J.R. !$#journal Eur. J. Biochem. (1988) 176:311-317 !$#title Similarity of the E1 subunits of branched-chain-oxoacid !1dehydrogenase from Pseudomonas putida to the corresponding !1subunits of mammalian branched-chain-oxoacid and pyruvate !1dehydrogenases. !$#cross-references MUID:88329084; PMID:3416875 !$#accession S01318 !'##molecule_type DNA !'##residues 1-339 ##label BUR !'##cross-references GB:M57613; EMBL:X13004; NID:g790512; !1PIDN:AAA65616.1; PID:g790516 !$#accession S05058 !'##molecule_type protein !'##residues 2-23 ##label BUR2 !'##note it is uncertain whether Met-1 is the initiator, as shown in !1Fig. 3, or whether translation is initiated 13 codons !1upstream, as shown in Fig. 5 GENETICS !$#gene bkdA2 CLASSIFICATION #superfamily pyruvate dehydrogenase (lipoamide) beta chain KEYWORDS oxidoreductase; thiamin pyrophosphate FEATURE !$2-339 #product 3-methyl-2-oxobutanoate dehydrogenase !8(lipoamide) chain E1-beta #status experimental #label !8MAT SUMMARY #length 339 #molecular-weight 37134 #checksum 7418 SEQUENCE /// ENTRY DEECPV #type complete TITLE pyruvate dehydrogenase (lipoamide) (EC 1.2.4.1) - Escherichia coli (strain K-12) ALTERNATE_NAMES pyruvate dehydrogenase complex component E1 ORGANISM #formal_name Escherichia coli DATE 31-Mar-1989 #sequence_revision 21-Nov-1997 #text_change 01-Mar-2002 ACCESSIONS B64734; A30272; S45193; I67628 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64734 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-887 ##label BLAT !'##cross-references GB:AE000120; GB:U00096; NID:g1786298; !1PIDN:AAC73225.1; PID:g1786304; UWGP:b0114 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A91130 !$#authors Stephens, P.E.; Darlison, M.G.; Lewis, H.M.; Guest, J.R. !$#journal Eur. J. Biochem. (1983) 133:155-162 !$#title The pyruvate dehydrogenase complex of Escherichia coli K12. !1Nucleotide sequence encoding the pyruvate dehydrogenase !1component. !$#cross-references MUID:83209630; PMID:6343085 !$#accession A30272 !'##molecule_type DNA !'##residues 1-145,'R',147-275,277-887 ##label STE !'##cross-references EMBL:V01498; NID:g431915; PIDN:CAA24740.1; !1PID:g434010 !'##experimental_source strain K-12 REFERENCE S45181 !$#authors Fujita, N. !$#submission submitted to the EMBL Data Library, January 1994 !$#accession S45193 !'##molecule_type DNA !'##residues 1-145,'R',147-275,277-887 ##label FUJ !'##cross-references EMBL:D26562; NID:g473770; PIDN:BAA05572.1; !1PID:g473783 !'##experimental_source strain K-12 substrain W3110 REFERENCE I53482 !$#authors Haydon, D.J.; Quail, M.A.; Guest, J.R. !$#journal FEBS Lett. (1993) 336:43-47 !$#title A mutation causing constitutive synthesis of the pyruvate !1dehydrogenase complex in Escherichia coli is located within !1the pdhR gene. !$#cross-references MUID:94085588; PMID:8262214 !$#accession I67628 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-23 ##label RES !'##cross-references GB:S67363; NID:g455921; PIDN:AAB29357.1; !1PID:g455923 COMMENT This enzyme, the E1 component of the pyruvate dehydrogenase !1complex, is a dimer of identical chains; it catalyzes the !1initial decarboxylation and oxidation of pyruvate and !1generates a reduced and acetylated form of the !1dihydrolipoamide acetyltransferase component (E2). GENETICS !$#gene aceE !$#map_position 3 min CLASSIFICATION #superfamily pyruvate dehydrogenase (lipoamide); thiamin !1pyrophosphate-binding domain homology KEYWORDS oxidoreductase; thiamin pyrophosphate FEATURE !$220-268 #domain thiamin pyrophosphate-binding domain homology !8#label TPB SUMMARY #length 887 #molecular-weight 99668 #checksum 9107 SEQUENCE /// ENTRY DEBY #type complete TITLE oxoglutarate dehydrogenase (lipoamide) (EC 1.2.4.2) precursor - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES alpha-ketoglutarate dehydrogenase; protein YI8277.04; protein YIL125w ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1991 #sequence_revision 24-Feb-1995 #text_change 12-Nov-1999 ACCESSIONS S49884; A32321; S05741 REFERENCE S49881 !$#authors Hamlyn, N.; Churcher, C. !$#submission submitted to the EMBL Data Library, November 1994 !$#accession S49884 !'##molecule_type DNA !'##residues 1-1014 ##label HAM !'##cross-references GB:Z47047; EMBL:Z46833; NID:g603997; PID:g763221; !1GSPDB:GN00009; MIPS:YIL125w REFERENCE A32321 !$#authors Repetto, B.; Tzagoloff, A. !$#journal Mol. Cell. Biol. (1989) 9:2695-2705 !$#title Structure and regulation of KGD1, the structural gene for !1yeast alpha-ketoglutarate dehydrogenase. !$#cross-references MUID:89343987; PMID:2503710 !$#accession A32321 !'##molecule_type DNA !'##residues 1-324,'LNL',328-512,'R',514-567,'T',569-1014 ##label REP !'##cross-references EMBL:M26390; NID:g171784; PIDN:AAA34721.1; !1PID:g171785 GENETICS !$#gene SGD:KGD1; OGD1; MIPS:YIL125w !'##cross-references SGD:S0001387; MIPS:YIL125w !$#map_position 9L !$#genome nuclear CLASSIFICATION #superfamily oxoglutarate dehydrogenase (lipoamide); thiamin !1pyrophosphate-binding domain homology KEYWORDS mitochondrion; oxidoreductase; thiamin pyrophosphate; !1tricarboxylic acid cycle FEATURE !$1-30 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$31-1014 #product oxoglutarate dehydrogenase (lipoamide) !8#status predicted #label MAT\ !$402-447 #domain thiamin pyrophosphate-binding domain homology !8#label TPB SUMMARY #length 1014 #molecular-weight 114415 #checksum 6585 SEQUENCE /// ENTRY DEECOG #type complete TITLE oxoglutarate dehydrogenase (lipoamide) (EC 1.2.4.2) - Escherichia coli (strain K-12) ALTERNATE_NAMES 2-oxoglutarate dehydrogenase complex E1 component; alpha-ketoglutaric dehydrogenase; oxoglutarate decarboxylase ORGANISM #formal_name Escherichia coli DATE 31-Mar-1989 #sequence_revision 24-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS E64808; A30256 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64808 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-933 ##label BLAT !'##cross-references GB:AE000175; GB:U00096; NID:g1786934; !1PIDN:AAC73820.1; PID:g1786945; UWGP:b0726 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A30256 !$#authors Darlison, M.G.; Spencer, M.E.; Guest, J.R. !$#journal Eur. J. Biochem. (1984) 141:351-359 !$#title Nucleotide sequence of the sucA gene encoding the !12-oxoglutarate dehydrogenase of Escherichia coli K12. !$#cross-references MUID:84236168; PMID:6376123 !$#accession A30256 !'##molecule_type DNA !'##residues 1-453,'S',455-933 ##label DAR !'##cross-references GB:X00661; NID:g43018; PIDN:CAA25280.1; PID:g43019 GENETICS !$#gene sucA !$#map_position 17 min COMPLEX homodimer; approximately 12 monomeric chains associate with !1the E2 component core which is an octamer of homotrimers FUNCTION !$#description catalyzes reaction of 2-oxoglutarate and lipoamide to form !1S-succinyl-dihydrolipoamide (bound to the E2 component) and !1carbon dioxide !$#note the 2-oxoglutarate dehydrogenase complex, including !12-oxoglutarate dehydrogenase (E1), dihydrolipoamide !1succinyltransferase (E2) and lipoamide dehydrogenase (E3), !1catalyzes the oxidative decarboxylation of 2-oxoglutarate to !1succinyl-CoA and carbon dioxide CLASSIFICATION #superfamily oxoglutarate dehydrogenase (lipoamide); thiamin !1pyrophosphate-binding domain homology KEYWORDS homodimer; oxidoreductase; thiamin pyrophosphate; !1tricarboxylic acid cycle FEATURE !$353-399 #domain thiamin pyrophosphate-binding domain homology !8#label TPB SUMMARY #length 933 #molecular-weight 105061 #checksum 2731 SEQUENCE /// ENTRY S07776 #type complete TITLE oxoglutarate dehydrogenase (lipoamide) (EC 1.2.4.2) - Azotobacter vinelandii ALTERNATE_NAMES 2-oxogluturate dehydrogenase complex chain E1 ORGANISM #formal_name Azotobacter vinelandii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 15-Oct-1999 ACCESSIONS S07776 REFERENCE S07776 !$#authors Schulze, E.; Westphal, A.H.; Hanemaaijer, R.; de Kok, A. !$#journal Eur. J. Biochem. (1990) 187:229-234 !$#title The 2-oxoglutarate dehydrogenase complex from Azotobacter !1vinelandii. 1. Molecular cloning and sequence analysis of !1the gene encoding the 2-oxoglutarate dehydrogenase !1component. !$#cross-references MUID:90126823; PMID:2404759 !$#accession S07776 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-943 ##label SCH !'##cross-references GB:X52433; NID:g39231; PIDN:CAA36680.1; PID:g39232 GENETICS !$#gene sucA CLASSIFICATION #superfamily oxoglutarate dehydrogenase (lipoamide); thiamin !1pyrophosphate-binding domain homology KEYWORDS oxidoreductase; thiamin pyrophosphate; tricarboxylic acid !1cycle FEATURE !$359-405 #domain thiamin pyrophosphate-binding domain homology !8#label TPB SUMMARY #length 943 #molecular-weight 105687 #checksum 1645 SEQUENCE /// ENTRY S42874 #type complete TITLE oxoglutarate dehydrogenase (lipoamide) (EC 1.2.4.2) - Coxiella burnetii ALTERNATE_NAMES 2-oxoglutarate dehydrogenase ORGANISM #formal_name Coxiella burnetii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 15-Oct-1999 ACCESSIONS S42874; I40851 REFERENCE S42872 !$#authors Thiele, D.; Willems, H.; Oswald, W.; Krauss, H. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S42874 !'##status preliminary !'##molecule_type DNA !'##residues 1-934 ##label THI !'##cross-references EMBL:X77919; NID:g510881; PIDN:CAA54874.1; !1PID:g457725 REFERENCE I40844 !$#authors Heinzen, R.A.; Mo, Y.Y.; Robertson, S.J.; Mallavia, L.P. !$#journal Gene (1995) 155:27-34 !$#title Characterization of the succinate dehydrogenase-encoding !1gene cluster (sdh) from the rickettsia Coxiella burnetii. !$#cross-references MUID:95212926; PMID:7698664 !$#accession I40851 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-280 ##label RES !'##cross-references GB:L33409; NID:g495749; PIDN:AAA74135.1; !1PID:g495757 GENETICS !$#gene sucA CLASSIFICATION #superfamily oxoglutarate dehydrogenase (lipoamide); thiamin !1pyrophosphate-binding domain homology KEYWORDS oxidoreductase; thiamin pyrophosphate; tricarboxylic acid !1cycle FEATURE !$351-397 #domain thiamin pyrophosphate-binding domain homology !8#label TPB SUMMARY #length 934 #molecular-weight 106722 #checksum 7821 SEQUENCE /// ENTRY S22397 #type complete TITLE pyruvate synthase (EC 1.2.7.1) beta chain [validated] - Halobacterium salinarum ORGANISM #formal_name Halobacterium salinarum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-May-2000 ACCESSIONS S22397 REFERENCE S22396 !$#authors Plaga, W.; Lottspeich, F.; Oesterhelt, D. !$#journal Eur. J. Biochem. (1992) 205:391-397 !$#title Improved purification, crystallization and primary structure !1of pyruvate: ferredoxin oxidoreductase from Halobacterium !1halobium. !$#cross-references MUID:92209529; PMID:1555599 !$#accession S22397 !'##status preliminary !'##molecule_type DNA !'##residues 1-312 ##label PLA !'##cross-references EMBL:X64521; NID:g43497; PIDN:CAA45826.1; !1PID:g43499 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing !'##note the source was designated as Halobacterium halobium COMPLEX heterotetramer; 2 alpha chains (PIR:S22396), 2 beta chains !1(PIR:S22397) [validated, MUID:92209529] FUNCTION !$#description EC 1.2.7.1 [validated, MUID:92209529] CLASSIFICATION #superfamily pyruvate synthase beta chain KEYWORDS coenzyme A; oxidoreductase FEATURE !$2-312 #product pyruvate synthase beta chain #status !8experimental #label MAT SUMMARY #length 312 #molecular-weight 34627 #checksum 4552 SEQUENCE /// ENTRY A64367 #type complete TITLE pyruvate synthase (EC 1.2.7.1) beta chain - Methanococcus jannaschii ALTERNATE_NAMES ferredoxin oxidoreductase, beta subunit ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A64367 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession A64367 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-270 ##label BUL !'##cross-references GB:U67503; GB:L77117; NID:g1591239; !1PIDN:AAB98531.1; PID:g1591241; TIGR:MJ0537 GENETICS !$#map_position REV473748-472936 !$#start_codon TTG CLASSIFICATION #superfamily pyruvate synthase beta chain KEYWORDS coenzyme A; oxidoreductase SUMMARY #length 270 #molecular-weight 29894 #checksum 5318 SEQUENCE /// ENTRY F64593 #type complete TITLE pyruvate synthase (EC 1.2.7.1) beta chain - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-May-2000 ACCESSIONS F64593 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession F64593 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-273 ##label TOM !'##cross-references GB:AE000572; GB:AE000511; NID:g2313703; !1PIDN:AAD07655.1; PID:g2313708; TIGR:HP0590 CLASSIFICATION #superfamily pyruvate synthase beta chain KEYWORDS coenzyme A; oxidoreductase SUMMARY #length 273 #molecular-weight 30414 #checksum 8631 SEQUENCE /// ENTRY G64658 #type complete TITLE probable pyruvate synthase (EC 1.2.7.1) beta chain - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-May-2000 ACCESSIONS G64658 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession G64658 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-314 ##label TOM !'##cross-references GB:AE000617; GB:AE000511; NID:g2314256; !1PIDN:AAD08155.1; PID:g2314262; TIGR:HP1111 CLASSIFICATION #superfamily pyruvate synthase beta chain KEYWORDS coenzyme A; oxidoreductase SUMMARY #length 314 #molecular-weight 34956 #checksum 961 SEQUENCE /// ENTRY C64333 #type complete TITLE probable pyruvate synthase (EC 1.2.7.1) beta chain - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C64333 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession C64333 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-298 ##label BUL !'##cross-references GB:U67482; GB:L77117; NID:g2826267; !1PIDN:AAB98253.1; PID:g1590994; TIGR:MJ0266 GENETICS !$#map_position REV253867-252971 !$#start_codon GTG CLASSIFICATION #superfamily pyruvate synthase beta chain KEYWORDS coenzyme A; oxidoreductase SUMMARY #length 298 #molecular-weight 33098 #checksum 1877 SEQUENCE /// ENTRY QQKBFP #type complete TITLE pyruvate (flavodoxin) dehydrogenase nifJ (EC 1.2.99.-) - Klebsiella pneumoniae ORGANISM #formal_name Klebsiella pneumoniae DATE 25-Feb-1985 #sequence_revision 12-Apr-1996 #text_change 11-Jun-1999 ACCESSIONS S01997; S01836; S35903; S21414; A04461; S36947 REFERENCE S01997 !$#authors Cannon, M.; Cannon, F.; Buchanan-Wollaston, V.; Ally, D.; !1Ally, A.; Beynon, J. !$#journal Nucleic Acids Res. (1988) 16:11379 !$#title The nucleotide sequence of the nifJ gene of Klebsiella !1pneumoniae. !$#cross-references MUID:89083580; PMID:3060860 !$#accession S01997 !'##status translation not shown !'##molecule_type DNA !'##residues 1-1171 ##label CAN !'##cross-references EMBL:X13109; NID:g43862; PIDN:CAA31501.1; !1PID:g43863 REFERENCE S01836 !$#authors Arnold, W.; Rump, A.; Klipp, W.; Priefer, U.B.; Puehler, A. !$#journal J. Mol. Biol. (1988) 203:715-738 !$#title Nucleotide sequence of a 24,206-base-pair DNA fragment !1carrying the entire nitrogen fixation gene cluster of !1Klebsiella pneumoniae. !$#cross-references MUID:89094839; PMID:3062178 !$#accession S01836 !'##molecule_type DNA !'##residues 1-405,'A',407-1171 ##label ARN !'##cross-references EMBL:X13303; NID:g43820; PIDN:CAA31665.1; !1PID:g43821 REFERENCE S35903 !$#authors Charlton, W.; Cannon, W.; Buck, M. !$#journal Mol. Microbiol. (1993) 7:1007-1021 !$#title The Klebsiella pneumoniae nifJ promoter: analysis of !1promoter elements regulating activation by the NifA !1promoter. !$#cross-references MUID:93247479; PMID:8483412 !$#accession S35903 !'##molecule_type DNA !'##residues 1-131 ##label CHA !'##cross-references EMBL:X13109 !'##note the authors translated the codon ATT for residue 27 as Tyr, TAC !1for residue 28 as Ile, and GAA for residue 103 as Gly REFERENCE S21414 !$#authors Wu, Y.; Yu, G.; Zhu, J.; Shen, S.C. !$#submission submitted to the EMBL Data Library, August 1989 !$#description Evidence that the open reading frame (ORF) upstream of nifH !1directs the transcription of nifJ in Klebsiella pneumoniae. !$#accession S21414 !'##molecule_type DNA !'##residues 1-127,129-135,'S',137-153,'TI',160,'IST',161-169 ##label !1WUY !'##cross-references EMBL:X16345; NID:g43864; PIDN:CAA34396.1; !1PID:g43865 REFERENCE A04461 !$#authors Shen, S.; Xue, Z.; Kong, Q.; Wu, Q. !$#journal Nucleic Acids Res. (1983) 11:4241-4250 !$#title An open reading frame upstream from the nifH gene of !1Klebsiella pneumoniae. !$#cross-references MUID:83246546; PMID:6306580 !$#accession A04461 !'##molecule_type DNA !'##residues 1-127 ##label SHE !'##cross-references GB:X01007; NID:g43860; PIDN:CAA25502.1; PID:g43861 GENETICS !$#gene nifJ FUNCTION !$#description transfers one electron from pyruvate to flavodoxin !$#pathway nitrogen fixation CLASSIFICATION #superfamily pyruvate (flavodoxin) dehydrogenase; ferredoxin !12[4Fe-4S] homology KEYWORDS 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein; oxidoreductase FEATURE !$684-763 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$691,694,697,755 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$701,745,748,751 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 1171 #molecular-weight 128125 #checksum 4222 SEQUENCE /// ENTRY DEBYPX #type complete TITLE pyruvate dehydrogenase complex protein X precursor - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein G7579; protein YGR193c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 21-Jul-2000 ACCESSIONS A36183; A34974; S55871; S64511; S07856 REFERENCE A36183 !$#authors Behal, R.H.; Browning, K.S.; Hall, T.B.; Reed, L.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:8732-8736 !$#title Cloning and nucleotide sequence of the gene for protein X !1from Saccharomyces cerevisiae. !$#cross-references MUID:90046867; PMID:2682658 !$#accession A36183 !'##molecule_type DNA !'##residues 1-410 ##label BEH !'##cross-references GB:M28222; NID:g172267; PIDN:AAA34910.1; !1PID:g172268 !$#accession A34974 !'##molecule_type protein !'##residues 31-51,'X',53-54,'X',56-60;192,'X',194-206 ##label BEH2 REFERENCE S55869 !$#authors Arroyo, J.; Garcia-Gonzalez, M.; Garcia-Saez, M.I.; Sanchez, !1M.; Nombela, C. !$#journal Yeast (1995) 11:587-591 !$#title The complete sequence of a 9037 bp DNA fragment of the right !1arm of Saccharomyces cerevisiae chromosome VII. !$#cross-references MUID:95373283; PMID:7645350 !$#accession S55871 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-410 ##label ARR !'##cross-references EMBL:X82408; NID:g755795; PIDN:CAA57804.1; !1PID:g755798 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1994 REFERENCE S64499 !$#authors Arroyo, J.; Garcia-Gonzalez, M.; Garcia-Saez, M.I.; !1Sanchez-Perez, M.; Nombela, C. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64511 !'##molecule_type DNA !'##residues 1-410 ##label ARW !'##cross-references EMBL:Z72978; NID:g1323342; PIDN:CAA97219.1; !1PID:g1323343; GSPDB:GN00007; MIPS:YGR193c !'##experimental_source strain S288C GENETICS !$#gene SGD:PDX1; ODPX; MIPS:YGR193c !'##cross-references SGD:S0003425; MIPS:YGR193c !$#map_position 7R !$#genome nuclear CLASSIFICATION #superfamily pyruvate dehydrogenase complex protein X; !1lipoyl/biotin-binding homology KEYWORDS lipoamide; mitochondrion FEATURE !$1-30 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$31-410 #product pyruvate dehydrogenase complex protein X !8#status experimental #label MAT\ !$34-108 #domain lipoyl/biotin-binding homology #label LPB\ !$73 #binding_site lipoamide (Lys) (covalent) #status !8predicted SUMMARY #length 410 #molecular-weight 45361 #checksum 2451 SEQUENCE /// ENTRY RDECPD #type complete TITLE dihydrodipicolinate reductase (EC 1.3.1.26) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 01-Mar-2002 ACCESSIONS A00375; S40554; G64723 REFERENCE A00375 !$#authors Bouvier, J.; Richaud, C.; Richaud, F.; Patte, J.C.; !1Stragier, P. !$#journal J. Biol. Chem. (1984) 259:14829-14834 !$#title Nucleotide sequence and expression of the Escherichia coli !1dapB gene. !$#cross-references MUID:85054974; PMID:6094578 !$#accession A00375 !'##molecule_type DNA !'##residues 1-273 ##label BOU !'##cross-references GB:D10483; GB:J01597; GB:J01683; GB:J01706; !1GB:K01298; GB:K01990; GB:M10420; GB:M10611; GB:M12544; !1GB:V00259; GB:X04711; GB:X54847; GB:X54945; GB:X55034; !1GB:X56742; NID:g216434; PIDN:BAA01309.1; PID:g216458 !'##note the authors translated the codon GGT for residue 218 as Val REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40554 !'##molecule_type DNA !'##residues 1-273 ##label YUR !'##cross-references EMBL:D10483; NID:g216434; PIDN:BAA01309.1; !1PID:g216458 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64723 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-273 ##label BLAT !'##cross-references GB:AE000113; GB:U00096; NID:g2367095; !1PIDN:AAC73142.1; PID:g1786214; UWGP:b0031 !'##experimental_source strain K-12, substrain MG1655 COMMENT The enzyme activity is repressed by lysine. GENETICS !$#gene dapB !$#map_position 1 min FUNCTION !$#description catalyzes the reduction of dihydrodipicolinate in the !1presence of NADH or NADPH !$#pathway diaminopimelate-lysine biosynthesis !$#note second step of diaminopimelate-lysine biosynthesis pathway CLASSIFICATION #superfamily dihydrodipicolinate reductase KEYWORDS diaminopimelate-lysine biosynthesis; homotetramer; NAD; !1oxidoreductase FEATURE !$159-163 #region substrate binding #status predicted SUMMARY #length 273 #molecular-weight 28756 #checksum 6444 SEQUENCE /// ENTRY JT0601 #type complete TITLE protochlorophyllide reductase (EC 1.3.1.33) chain chlN [similarity] - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES ORF465 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 16-Jun-2000 ACCESSIONS JT0601; S76834 REFERENCE JT0600 !$#authors Ogura, Y.; Takemura, M.; Oda, K.; Yamato, K.; Ohta, E.; !1Fukuzawa, H.; Ohyama, K. !$#journal Biosci. Biotechnol. Biochem. (1992) 56:788-793 !$#title Cloning and nucleotide sequence of a frxC-ORF469 gene !1cluster of Synechocystis PCC6803: conservation with !1liverwort chloroplast frxC-ORF465 and nif operon. !$#cross-references MUID:92330029; PMID:1368342 !$#accession JT0601 !'##molecule_type DNA !'##residues 1-469 ##label OGU !'##cross-references DDBJ:D10474; NID:g217090; PIDN:BAA01276.1; !1PID:g217094 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76834 !'##molecule_type DNA !'##residues 1-469 ##label KAN !'##cross-references EMBL:D90916; GB:AB001339; NID:g1653715; !1PIDN:BAA18746.1; PID:g1653835 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily protochlorophyllide reductase chain chlN KEYWORDS chlorophyll biosynthesis; oxidoreductase; photosynthesis SUMMARY #length 469 #molecular-weight 52474 #checksum 3652 SEQUENCE /// ENTRY S36669 #type complete TITLE protochlorophyllide reductase (EC 1.3.1.33) chain chlN [similarity] - Plectonema boryanum ORGANISM #formal_name Plectonema boryanum DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 16-Jun-2000 ACCESSIONS S36669 REFERENCE S36668 !$#authors Fujita, Y.; Matsumoto, H.; Takahashi, Y.; Matsubara, H. !$#submission submitted to the EMBL Data Library, August 1992 !$#description Identification of the nifDK-like gene (ORF467) involved in !1the biosynthesis of chlorophyll in the cyanobacterium !1Plectonema boryanum. !$#accession S36669 !'##molecule_type DNA !'##residues 1-467 ##label FUJ !'##cross-references EMBL:D12973; NID:g216810; PIDN:BAA02349.1; !1PID:g216812 CLASSIFICATION #superfamily protochlorophyllide reductase chain chlN KEYWORDS chlorophyll biosynthesis; oxidoreductase; photosynthesis SUMMARY #length 467 #molecular-weight 52795 #checksum 365 SEQUENCE /// ENTRY A36904 #type complete TITLE protochlorophyllide reductase (EC 1.3.1.33) [similarity] - Synechococcus sp. (PCC 7942) ORGANISM #formal_name Synechococcus sp. #variety PCC 7942 DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS S25621; A36904 REFERENCE S25616 !$#authors Lieman-Hurwitz, J.; Ronen-Tarazi, M.; Gabai, C.; Hassidim, !1M.; Schwarz, R.; Kaplan, A. !$#submission submitted to the EMBL Data Library, August 1992 !$#accession S25621 !'##molecule_type DNA !'##residues 1-466 ##label LIE !'##cross-references EMBL:X67694; NID:g312508; PIDN:CAA47924.1; !1PID:g46847 REFERENCE A36904 !$#authors Price, G.D.; Howitt, S.M.; Harrison, K.; Badger, M.R. !$#journal J. Bacteriol. (1993) 175:2871-2879 !$#title Analysis of a genomic DNA region from the cyanobacterium !1Synechococcus sp. strain PCC7942 involved in carboxysome !1assembly and function. !$#cross-references MUID:93259930; PMID:8491708 !$#accession A36904 !'##molecule_type DNA !'##residues 388-466 ##label PRI !'##experimental_source PCC 7942 !'##note sequence extracted from NCBI backbone (NCBIN:131726, !1NCBIP:131727) CLASSIFICATION #superfamily protochlorophyllide reductase chain chlN KEYWORDS chlorophyll biosynthesis; oxidoreductase; photosynthesis SUMMARY #length 466 #molecular-weight 51540 #checksum 7627 SEQUENCE /// ENTRY T07310 #type complete TITLE protochlorophyllide reductase (EC 1.3.1.33) chain chlN [similarity] - Chlorella vulgaris chloroplast ORGANISM #formal_name chloroplast Chlorella vulgaris DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 21-Jul-2000 ACCESSIONS T07310 REFERENCE Z15985 !$#authors Wakasugi, T.; Nagai, T.; Kapoor, M.; Sugita, M.; Ito, M.; !1Ito, S.; Tsudzuki, J.; Nakashima, K.; Tsudzuki, T.; Suzuki, !1Y.; Hamada, A.; Ohta, T.; Inamura, A.; Yoshinaga, K.; !1Sugiura, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1997) 94:5967-5972 !$#title Complete nucleotide sequence of the chloroplast genome from !1the green alga Chlorella vulgaris: the existence of genes !1possibly involved in chloroplast division. !$#cross-references MUID:97303241; PMID:9159184 !$#accession T07310 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-435 ##label WAK !'##cross-references EMBL:AB001684; NID:g2224352; PIDN:BAA57958.1; !1PID:g2224474 GENETICS !$#gene chlN !$#genome chloroplast CLASSIFICATION #superfamily protochlorophyllide reductase chain chlN KEYWORDS chlorophyll biosynthesis; chloroplast; oxidoreductase; !1photosynthesis SUMMARY #length 435 #molecular-weight 49421 #checksum 1141 SEQUENCE /// ENTRY T07565 #type complete TITLE probable protochlorophyllide reductase (EC 1.3.1.33) [similarity] - Japanese black pine chloroplast ORGANISM #formal_name chloroplast Pinus thunbergiana #common_name Japanese black pine DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 18-Aug-2000 ACCESSIONS T07565 REFERENCE Z16030 !$#authors Wakasugi, T.; Tsudzuki, J.; Ito, S.; Nakashima, K.; !1Tsudzuki, T.; Sugiura, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1994) 91:9794-9798 !$#title Loss of all ndh genes as determined by sequencing the entire !1chloroplast genome of the black pine Pinus thunbergii. !$#cross-references MUID:95024047; PMID:7937893 !$#accession T07565 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-467 ##label WAK !'##cross-references EMBL:D17510; NID:g529643; PIDN:BAA04441.1; !1PID:g1262726 GENETICS !$#gene chlN !$#genome chloroplast FUNCTION !$#description catalyzes the light-dependent reduction of !1protochlorophyllide to chlorophyllide in the biosynthesis of !1chlorophyll CLASSIFICATION #superfamily protochlorophyllide reductase chain chlN KEYWORDS chlorophyll biosynthesis; chloroplast; oxidoreductase; !1photosynthesis SUMMARY #length 467 #molecular-weight 53012 #checksum 3296 SEQUENCE /// ENTRY T06974 #type complete TITLE protochlorophyllide reductase (EC 1.3.1.33) [similarity] - Cyanophora paradoxa cyanelle ORGANISM #formal_name cyanelle Cyanophora paradoxa DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS T06974 REFERENCE Z15840 !$#authors Stirewalt, V.L.; Michalowski, C.B.; Luffelhardt, W.; !1Bohnert, H.J.; Bryant, D.A. !$#submission submitted to the EMBL Data Library, July 1995 !$#description Nucleotide sequence of the cyanelle genome from Cyanophora !1paradoxa. !$#accession T06974 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-460 ##label STI !'##cross-references EMBL:U30821; NID:g1016083; PIDN:AAA81317.1; !1PID:g1016230 !'##experimental_source strain Pringsheim LB555 GENETICS !$#gene chlN !$#genome cyanelle CLASSIFICATION #superfamily protochlorophyllide reductase chain chlN KEYWORDS chlorophyll biosynthesis; cyanelle; oxidoreductase; !1photosynthesis SUMMARY #length 460 #molecular-weight 52449 #checksum 528 SEQUENCE /// ENTRY B49851 #type complete TITLE protochlorophyllide reductase (EC 1.3.1.33) 46K chain [similarity] - Rhodobacter capsulatus ALTERNATE_NAMES chlorin reductase subunit bchN ORGANISM #formal_name Rhodobacter capsulatus DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS B49851; S17810 REFERENCE A49851 !$#authors Burke, D.H.; Alberti, M.; Hearst, J.E. !$#journal J. Bacteriol. (1993) 175:2414-2422 !$#title bchFNBH bacteriochlorophyll synthesis genes of Rhodobacter !1capsulatus and identification of the third subunit of !1light-independent protochlorophyllide reductase in bacteria !1and plants. !$#cross-references MUID:93224465; PMID:8385667 !$#accession B49851 !'##molecule_type DNA !'##residues 1-424 ##label BUR !'##cross-references EMBL:Z11165; NID:g46097; PIDN:CAA77526.1; !1PID:g46109 !'##experimental_source SB1003 !'##note sequence extracted from NCBI backbone (NCBIN:129238, !1NCBIP:129240) GENETICS !$#gene bchN CLASSIFICATION #superfamily protochlorophyllide reductase chain chlN KEYWORDS chlorophyll biosynthesis; oxidoreductase; photosynthesis SUMMARY #length 424 #molecular-weight 45829 #checksum 3396 SEQUENCE /// ENTRY T07268 #type complete TITLE protochlorophyllide reductase (EC 1.3.1.33) chain chlB [similarity] - Chlorella vulgaris chloroplast ORGANISM #formal_name chloroplast Chlorella vulgaris DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 21-Jul-2000 ACCESSIONS T07268 REFERENCE Z15985 !$#authors Wakasugi, T.; Nagai, T.; Kapoor, M.; Sugita, M.; Ito, M.; !1Ito, S.; Tsudzuki, J.; Nakashima, K.; Tsudzuki, T.; Suzuki, !1Y.; Hamada, A.; Ohta, T.; Inamura, A.; Yoshinaga, K.; !1Sugiura, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1997) 94:5967-5972 !$#title Complete nucleotide sequence of the chloroplast genome from !1the green alga Chlorella vulgaris: the existence of genes !1possibly involved in chloroplast division. !$#cross-references MUID:97303241; PMID:9159184 !$#accession T07268 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-510 ##label WAK !'##cross-references EMBL:AB001684; NID:g2224352; PIDN:BAA57916.1; !1PID:g2224432 GENETICS !$#gene chlB !$#genome chloroplast CLASSIFICATION #superfamily protochlorophyllide reductase chain chlB KEYWORDS chlorophyll biosynthesis; chloroplast; oxidoreductase; !1photosynthesis SUMMARY #length 510 #molecular-weight 57538 #checksum 4388 SEQUENCE /// ENTRY S76262 #type complete TITLE protochlorophyllide reductase (EC 1.3.1.33) 57K chain [similarity] - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 16-Jun-2000 ACCESSIONS S76262 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76262 !'##molecule_type DNA !'##residues 1-508 ##label KAN !'##cross-references EMBL:D64000; GB:AB001339; NID:g1001484; !1PIDN:BAA10114.1; PID:g1001489 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily protochlorophyllide reductase chain chlB KEYWORDS chlorophyll biosynthesis; oxidoreductase; photosynthesis SUMMARY #length 508 #molecular-weight 56952 #checksum 5874 SEQUENCE /// ENTRY T06837 #type complete TITLE protochlorophyllide reductase (EC 1.3.1.33) chain chlB [similarity] - Cyanophora paradoxa cyanelle ORGANISM #formal_name cyanelle Cyanophora paradoxa DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS T06837 REFERENCE Z15840 !$#authors Stirewalt, V.L.; Michalowski, C.B.; Luffelhardt, W.; !1Bohnert, H.J.; Bryant, D.A. !$#submission submitted to the EMBL Data Library, July 1995 !$#description Nucleotide sequence of the cyanelle genome from Cyanophora !1paradoxa. !$#accession T06837 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-440 ##label STI !'##cross-references EMBL:U30821; NID:g1016083; PIDN:AAA81180.1; !1PID:g1016093 !'##experimental_source strain Pringsheim LB555 GENETICS !$#gene chlB !$#genome cyanelle FUNCTION !$#description catalyzes the light-dependent reduction of !1protochlorophyllide to chlorophyllid CLASSIFICATION #superfamily protochlorophyllide reductase chain chlB KEYWORDS chlorophyll biosynthesis; cyanelle; oxidoreductase; !1photosynthesis SUMMARY #length 440 #molecular-weight 50284 #checksum 2486 SEQUENCE /// ENTRY C49851 #type complete TITLE protochlorophyllide reductase (EC 1.3.1.33) 57K chain [similarity] - Rhodobacter capsulatus ALTERNATE_NAMES chlorin reductase subunit bchB ORGANISM #formal_name Rhodobacter capsulatus DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS C49851; S17809 REFERENCE A49851 !$#authors Burke, D.H.; Alberti, M.; Hearst, J.E. !$#journal J. Bacteriol. (1993) 175:2414-2422 !$#title bchFNBH bacteriochlorophyll synthesis genes of Rhodobacter !1capsulatus and identification of the third subunit of !1light-independent protochlorophyllide reductase in bacteria !1and plants. !$#cross-references MUID:93224465; PMID:8385667 !$#accession C49851 !'##molecule_type DNA !'##residues 1-525 ##label BUR !'##cross-references EMBL:Z11165; NID:g46097; PIDN:CAA77525.1; !1PID:g46108 !'##experimental_source SB1003 !'##note sequence extracted from NCBI backbone (NCBIN:129238, !1NCBIP:129241) GENETICS !$#gene bchB CLASSIFICATION #superfamily protochlorophyllide reductase chain chlB KEYWORDS chlorophyll biosynthesis; oxidoreductase; photosynthesis SUMMARY #length 525 #molecular-weight 57191 #checksum 7390 SEQUENCE /// ENTRY PC1219 #type complete TITLE dihydroorotate oxidase (EC 1.3.3.1) precursor - human ALTERNATE_NAMES dihydroorotate dehydrogenase ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1993 #sequence_revision 17-Apr-1998 #text_change 11-Jun-1999 ACCESSIONS PC1219; S62653; S68018; S74083 REFERENCE PC1219 !$#authors Minet, M.; Dufour, M.E.; Lacroute, F. !$#journal Gene (1992) 121:393-396 !$#title Cloning and sequencing of a human cDNA coding for !1dihydroorotate dehydrogenase by complementation of the !1corresponding yeast mutant. !$#cross-references MUID:93077060; PMID:1446837 !$#accession PC1219 !'##molecule_type mRNA !'##residues 2-397 ##label MIN !'##cross-references GB:M94065 REFERENCE S62653 !$#authors Minet, M. !$#submission submitted to the EMBL Data Library, October 1992 !$#accession S62653 !'##status preliminary !'##molecule_type mRNA !'##residues 2-229,'EL',232-341,'D',343-360,'T',362-397 ##label MI2 !'##cross-references EMBL:M94065; NID:g555593; PIDN:AAA50163.1; !1PID:g555594 REFERENCE S68018 !$#authors Copeland, R.A.; Davis, J.P.; Dowling, R.L.; Lombardo, D.; !1Murphy, K.B.; Patterson, T.A. !$#journal Arch. Biochem. Biophys. (1995) 323:79-86 !$#title Recombinant human dihydroorotate dehydrogenase: expression, !1purification, and characterization of a catalytically !1functional truncated enzyme. !$#cross-references MUID:96019950; PMID:7487077 !$#accession S68018 !'##molecule_type DNA !'##residues 2-229,'EL',232-341,'D',343-360,'T',362-397 ##label COP REFERENCE S74083 !$#authors Knecht, W.; Bergjohann, U.; Gonski, S.; Kirschbaum, B.; !1Loeffler, M. !$#journal Eur. J. Biochem. (1996) 240:292-301 !$#title Functional expression of a fragment of human dihydroorotate !1dehydrogenase by means of the baculovirus expression vector !1system, and kinetic investigation of the purified !1recombinant enzyme. !$#cross-references MUID:97025338; PMID:8925840 !$#accession S74083 !'##molecule_type protein !'##residues 1-13,'A' ##label KNE GENETICS !$#gene GDB:DHODH !'##cross-references GDB:136780 !$#map_position 16q22-16q22 !$#genome nuclear CLASSIFICATION #superfamily dihydroorotate oxidase KEYWORDS FAD; flavoprotein; mitochondrial inner membrane; !1mitochondrion; oxidoreductase; pyrimidine nucleotide !1biosynthesis FEATURE !$1-11 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$12-397 #product dihydroorotate oxidase #status predicted !8#label MAT SUMMARY #length 397 #molecular-weight 43101 #checksum 1495 SEQUENCE /// ENTRY JN0500 #type complete TITLE dihydroorotate oxidase (EC 1.3.3.1), mitochondrial - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES dihydroorotate dehydrogenase ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JN0500; S34967 REFERENCE JN0500 !$#authors Rawls, J.; Kirkpatrick, R.; Yang, J.; Lacy, L. !$#journal Gene (1993) 124:191-197 !$#title The dhod gene and deduced structure of mitochondrial !1dihydroorotate dehydrogenase in Drosophila melanogaster. !$#cross-references MUID:93185923; PMID:8444342 !$#accession JN0500 !'##molecule_type DNA !'##residues 1-405 ##label RAW !'##cross-references EMBL:L00964 REFERENCE S34967 !$#authors Rawls, J.; Kirkpatrick, R.; Yang, J.; Lacy, L. !$#submission submitted to the EMBL Data Library, September 1992 !$#description The dhod gene and the deduced structure of mitochondrial !1dihydroorotate dehydrogenase in Drosophila melanogaster. !$#accession S34967 !'##molecule_type DNA !'##residues 1-377,'GAVGADHTA',387,'SH' ##label RA2 !'##cross-references EMBL:L00964; NID:g157227; PIDN:AAB59185.1; !1PID:g157228 GENETICS !$#gene dhod !'##cross-references FlyBase:FBgn0000447 !$#introns 16/3 CLASSIFICATION #superfamily dihydroorotate oxidase KEYWORDS flavoprotein; mitochondrion; oxidoreductase; pyrimidine !1nucleotide biosynthesis SUMMARY #length 405 #molecular-weight 44342 #checksum 5650 SEQUENCE /// ENTRY A46248 #type complete TITLE dihydroorotate oxidase (EC 1.3.3.1) - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES dihydroorotate dehydrogenase ORGANISM #formal_name Schizosaccharomyces pombe DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 10-Dec-1999 ACCESSIONS A46248; T38939; S19995 REFERENCE A46248 !$#authors Nagy, M.; Lacroute, F.; Thomas, D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:8966-8970 !$#title Divergent evolution of pyrimidine biosynthesis between !1anaerobic and aerobic yeasts. !$#cross-references MUID:93028386; PMID:1409592 !$#accession A46248 !'##molecule_type mRNA !'##residues 1-443 ##label NAG !'##cross-references EMBL:X65114; NID:g5131; PIDN:CAA46230.1; PID:g5132 !'##note sequence extracted from NCBI backbone (NCBIP:115364) REFERENCE Z21818 !$#authors Badcock, K.; Churcher, C.M.; Wood, V.; Barrell, B.G.; !1Rajandream, M.A. !$#submission submitted to the EMBL Data Library, April 1997 !$#accession T38939 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-443 ##label BAD !'##cross-references EMBL:Z94864; PIDN:CAB08175.1; GSPDB:GN00066; !1SPDB:SPAC57A10.12c !'##experimental_source strain 972h-; cosmid c57A10 GENETICS !$#gene SPAC57A10.12c !$#map_position 1 CLASSIFICATION #superfamily dihydroorotate oxidase KEYWORDS flavoprotein; oxidoreductase; pyrimidine nucleotide !1biosynthesis SUMMARY #length 443 #molecular-weight 48295 #checksum 9424 SEQUENCE /// ENTRY DEECDO #type complete TITLE dihydroorotate oxidase (EC 1.3.3.1) - Escherichia coli (strain K-12) ALTERNATE_NAMES dihydroorotate dehydrogenase ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 01-Mar-2002 ACCESSIONS A23109; H64834 REFERENCE A23109 !$#authors Larsen, J.N.; Jensen, K.F. !$#journal Eur. J. Biochem. (1985) 151:59-65 !$#title Nucleotide sequence of the pyrD gene of Escherichia coli and !1characterization of the flavoprotein dihydroorotate !1dehydrogenase. !$#cross-references MUID:85285014; PMID:2992959 !$#accession A23109 !'##molecule_type DNA !'##residues 1-336 ##label LAR !'##cross-references GB:X02826; NID:g42608; PIDN:CAA26594.1; PID:g42609 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64834 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-336 ##label BLAT !'##cross-references GB:AE000196; GB:U00096; NID:g1787169; !1PIDN:AAC74031.1; PID:g1787177; UWGP:b0945 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene pyrD !$#map_position 21 min FUNCTION !$#description catalyzes the oxidation of dihydroorotate to orotate using !1molecular oxygen and produces hydrogen peroxide !$#pathway pyrimidine nucleotide biosynthesis !$#note it contains one mole of FMN per monome; location on the !1inner side of the cytosolic membrane CLASSIFICATION #superfamily dihydroorotate oxidase KEYWORDS flavoprotein; FMN; homodimer; oxidoreductase; pyrimidine !1nucleotide biosynthesis FEATURE !$292-312 #region FMN binding SUMMARY #length 336 #molecular-weight 36774 #checksum 5800 SEQUENCE /// ENTRY S13824 #type complete TITLE dihydroorotate oxidase (EC 1.3.3.1) - Salmonella typhimurium ALTERNATE_NAMES dihydroorotate dehydrogenase ORGANISM #formal_name Salmonella typhimurium DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 11-Sep-1998 ACCESSIONS S13824 REFERENCE S13824 !$#authors Frick, M.M.; Neuhard, J.; Kelln, R.A. !$#journal Eur. J. Biochem. (1990) 194:573-578 !$#title Cloning, nucleotide sequence and regulation of the !1Salmonella typhimurium pyrD gene encoding dihydroorotate !1dehydrogenase. !$#cross-references MUID:91099333; PMID:2269282 !$#accession S13824 !'##molecule_type DNA !'##residues 1-336 ##label FRI GENETICS !$#gene pyrD !$#map_position 20 min FUNCTION !$#description catalyzes the oxidation of dihydroorotate to orotate using !1molecular oxygen and produces hydrogen peroxide !$#pathway pyrimidine nucleotide biosynthesis !$#note it contains one mole of FMN per monome; location on the !1inner side of the cytosolic membrane CLASSIFICATION #superfamily dihydroorotate oxidase KEYWORDS flavoprotein; FMN; homodimer; oxidoreductase; pyrimidine !1nucleotide biosynthesis FEATURE !$292-312 #region FMN binding SUMMARY #length 336 #molecular-weight 36794 #checksum 7615 SEQUENCE /// ENTRY I40171 #type complete TITLE dihydroorotate oxidase (EC 1.3.3.1) - Bacillus caldolyticus ALTERNATE_NAMES dihydroorotate dehydrogenase ORGANISM #formal_name Bacillus caldolyticus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS I40171; S34323 REFERENCE I40166 !$#authors Ghim, S.Y.; Neuhard, J. !$#journal J. Bacteriol. (1994) 176:3698-3707 !$#title The pyrimidine biosynthesis operon of the thermophile !1Bacillus caldolyticus includes genes for uracil !1phosphoribosyltransferase and uracil permease. !$#cross-references MUID:94266723; PMID:8206848 !$#accession I40171 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-313 ##label RES !'##cross-references EMBL:X73308; NID:g312439; PIDN:CAA51741.1; !1PID:g312445 GENETICS !$#gene pyrD CLASSIFICATION #superfamily dihydroorotate oxidase KEYWORDS flavoprotein; oxidoreductase; pyrimidine nucleotide !1biosynthesis SUMMARY #length 313 #molecular-weight 32857 #checksum 6574 SEQUENCE /// ENTRY JN0453 #type complete TITLE dihydroorotate oxidase (EC 1.3.3.1) - gill mushroom (Agrocybe aegerita) ALTERNATE_NAMES dihydroorotate dehydrogenase ORGANISM #formal_name Agrocybe aegerita DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JN0453 REFERENCE JN0453 !$#authors Noeel, T.; Labarere, J. !$#journal Gene (1992) 122:233-234 !$#title Sequence of the URA1 gene encoding dihydroorotate !1dehydrogenase from the basidiomycete fungus Agrocybe !1aegerita. !$#cross-references MUID:93083991; PMID:1452035 !$#accession JN0453 !'##molecule_type DNA !'##residues 1-328 ##label NOE !'##cross-references GB:M90295; NID:g166337; PIDN:AAA32636.1; !1PID:g166338 GENETICS !$#gene URA1 CLASSIFICATION #superfamily dihydroorotate oxidase KEYWORDS flavoprotein; oxidoreductase; pyrimidine nucleotide !1biosynthesis SUMMARY #length 328 #molecular-weight 35085 #checksum 6956 SEQUENCE /// ENTRY JC1276 #type complete TITLE dihydroorotate oxidase (EC 1.3.3.1) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein A314; protein YKL216w ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 21-Jul-2000 ACCESSIONS JC1276; S38059; S44322; S17008 REFERENCE JC1276 !$#authors Roy, A. !$#journal Gene (1992) 118:149-150 !$#title Nucleotide sequence of the URA1 gene of Saccharomyces !1cerevisiae. !$#cross-references MUID:92380485; PMID:1511880 !$#accession JC1276 !'##molecule_type DNA !'##residues 1-314 ##label ROY !'##cross-references GB:M83295; NID:g171393; PIDN:AAA34566.1; !1PID:g171394 REFERENCE S38054 !$#authors Alexandraki, D.; Tzermia, M. !$#submission submitted to the Protein Sequence Database, March 1994 !$#accession S38059 !'##molecule_type DNA !'##residues 1-314 ##label ALE !'##cross-references EMBL:Z28216; NID:g486386; PIDN:CAA82061.1; !1PID:g486387; GSPDB:GN00011; MIPS:YKL216w !'##experimental_source strain S288C REFERENCE S44319 !$#authors Tzermia, M.; Horaitis, O.; Alexandraki, D. !$#journal Yeast (1994) 10:663-679 !$#title The complete sequencing of a 24.6 kb segment of yeast !1chromosome XI identified the known loci URA1, SAC1 and TRP3, !1and revealed 6 new open reading frames including homologues !1to the threonine dehydratases, membrane transporters, !1hydantoinases and the phospholipase A(2)-activating protein. !$#cross-references MUID:95028164; PMID:7941750 !$#accession S44322 !'##status translation not shown !'##molecule_type DNA !'##residues 1-314 ##label TZE !'##cross-references EMBL:X75951; NID:g473130; PIDN:CAA53557.1; !1PID:g473134 GENETICS !$#gene SGD:URA1; MIPS:YKL216w !'##cross-references SGD:S0001699; MIPS:YKL216w !$#map_position 11L CLASSIFICATION #superfamily dihydroorotate oxidase KEYWORDS flavoprotein; FMN; oxidoreductase; pyrimidine nucleotide !1biosynthesis SUMMARY #length 314 #molecular-weight 34801 #checksum 8632 SEQUENCE /// ENTRY H39845 #type complete TITLE dihydroorotate oxidase (EC 1.3.3.1) pyrD - Bacillus subtilis ALTERNATE_NAMES dihydroorotate dehydrogenase ORGANISM #formal_name Bacillus subtilis DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 21-Jul-2000 ACCESSIONS H39845; E69686 REFERENCE A39845 !$#authors Quinn, C.L.; Stephenson, B.T.; Switzer, R.L. !$#journal J. Biol. Chem. (1991) 266:9113-9127 !$#title Functional organization and nucleotide sequence of the !1Bacillus subtilis pyrimidine biosynthetic operon. !$#cross-references MUID:91225016; PMID:1709162 !$#accession H39845 !'##molecule_type DNA !'##residues 1-311 ##label QUI !'##cross-references GB:M59757; NID:g4887706; PIDN:AAA21272.1; !1PID:g143392 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69686 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-311 ##label KUN !'##cross-references GB:Z99112; GB:AL009126; NID:g2633902; !1PIDN:CAB13428.1; PID:g2633927 !'##experimental_source strain 168 GENETICS !$#gene pyrD CLASSIFICATION #superfamily dihydroorotate oxidase KEYWORDS flavoprotein; oxidoreductase; pyrimidine nucleotide !1biosynthesis SUMMARY #length 311 #molecular-weight 33091 #checksum 3542 SEQUENCE /// ENTRY A23559 #type complete TITLE dihydroorotate oxidase (EC 1.3.3.1) - slime mold (Dictyostelium discoideum) ALTERNATE_NAMES dihydroorotate dehydrogenase ORGANISM #formal_name Dictyostelium discoideum DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 30-Sep-1993 ACCESSIONS A23559 REFERENCE A23559 !$#authors Jacquet, M.; Kalekine, M.; Boy-Marcotte, E. !$#journal Biochimie (1985) 67:583-588 !$#title Sequence analysis of a Dictyostelium discoideum gene coding !1for an active dihydroorotate dehydrogenase in yeast. !$#cross-references MUID:86026489; PMID:2996629 !$#accession A23559 !'##molecule_type DNA !'##residues 1-369 ##label JAC !'##cross-references GB:X02917 CLASSIFICATION #superfamily slime mold dihydroorotate oxidase KEYWORDS flavoprotein; oxidoreductase; pyrimidine nucleotide !1biosynthesis SUMMARY #length 369 #molecular-weight 40370 #checksum 5307 SEQUENCE /// ENTRY DEBYCH #type complete TITLE coproporphyrinogen oxidase (EC 1.3.3.3) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES coproporphyrinogenase; protein YD5112.02; protein YDR044w ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1989 #sequence_revision 12-Apr-1996 #text_change 05-Nov-1999 ACCESSIONS S55079; A28090 REFERENCE S55078 !$#authors Oliver, K.; Harris, D. !$#submission submitted to the EMBL Data Library, June 1995 !$#accession S55079 !'##molecule_type DNA !'##residues 1-328 ##label OLI !'##cross-references EMBL:Z49812; NID:g1204147; PIDN:CAA89966.1; !1PID:g854428; GSPDB:GN00004; MIPS:YDR044w !'##experimental_source strain AB972 REFERENCE A28090 !$#authors Zagorec, M.; Buhler, J.M.; Treich, I.; Keng, T.; Guarente, !1L.; Labbe-Bois, R. !$#journal J. Biol. Chem. (1988) 263:9718-9724 !$#title Isolation, sequence, and regulation by oxygen of the yeast !1HEM13 gene coding for coproporphyrinogen oxidase. !$#cross-references MUID:88257098; PMID:2838478 !$#accession A28090 !'##molecule_type DNA !'##residues 1-225,'N',227-328 ##label ZAG !'##cross-references EMBL:J03873; NID:g171315; PIDN:AAA34529.1; !1PID:g171316 GENETICS !$#gene SGD:HEM13; MIPS:YDR044w !'##cross-references SGD:S0002451; MIPS:YDR044w !$#map_position 4R COMPLEX homodimer FUNCTION !$#description catalyzes the oxygen-requiring oxidative decarboxylation of !1the two carboxyethyl side chains of coproporphyrinogen III !1to two vinyl groups of the protoporphyrinogen IX CLASSIFICATION #superfamily coproporphyrinogen oxidase KEYWORDS cytosol; homodimer; iron; metalloprotein; oxidative !1decarboxylation; oxidoreductase SUMMARY #length 328 #molecular-weight 37711 #checksum 3648 SEQUENCE /// ENTRY I52444 #type complete TITLE coproporphyrinogen oxidase (EC 1.3.3.3) precursor, mitochondrial - human ORGANISM #formal_name Homo sapiens #common_name man DATE 28-Jan-2000 #sequence_revision 28-Jan-2000 #text_change 28-Jan-2000 ACCESSIONS I52444; I37259; I37257; S39243 REFERENCE I52444 !$#authors Taketani, S.; Kohno, H.; Furukawa, T.; Yoshinaga, T.; !1Tokunaga, R. !$#journal Biochim. Biophys. Acta (1994) 1183:547-549 !$#title Molecular cloning, sequencing and expression of cDNA !1encoding human coproporphyrinogen oxidase. !$#cross-references MUID:94114558; PMID:8286403 !$#accession I52444 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-354 ##label TAK !'##cross-references GB:D16611; NID:g469488; PIDN:BAA04033.1; !1PID:g840693 !'##note the amino-terminal of the mature form is predicted from a !1bovine sequence determination REFERENCE A54939 !$#authors Martasek, P.; Camadro, J.M.; Delfau-Larue, M.H.; Dumas, !1J.B.; Montagne, J.J.; de Verneuil, H.; Labbe, P.; !1Grandchamp, B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1994) 91:3024-3028 !$#title Molecular cloning, sequencing, and functional expression of !1a cDNA encoding human coproporphyrinogen oxidase. !$#cross-references MUID:94211794; PMID:8159699 !$#accession I37259 !'##status preliminary !'##molecule_type mRNA !'##residues 1-146,'T',148-171,'H',173-354 ##label MAR !'##cross-references EMBL:Z28409; NID:g433887; PIDN:CAA82250.1; !1PID:g433888 REFERENCE I37257 !$#authors Delfau-Larue, M.H.; Martasek, P.; Grandchamp, B. !$#journal Hum. Mol. Genet. (1994) 3:1325-1330 !$#title Coproporphyrinogen oxidase: gene organization and !1description of a mutation leading to exon 6 skipping. !$#cross-references MUID:95078835; PMID:7987309 !$#accession I37257 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 'MALQLGRLSSGPCWLVARGGCGGPRAWSQCGGGGLRAWSQ', !1'RSAAGRVCRPPGPAGTEQSRGLGHGSTSRGGPWVGTGLAA', !1'ALAGLVGLATAAFGHVQRAE',1-354 ##label DEL !'##cross-references EMBL:Z34531; NID:g505586; PIDN:CAA84292.1; !1PID:g825648 !'##note an incorrect initiation codon was used GENETICS !$#gene GDB:CPO; CPX !'##cross-references GDB:119070; OMIM:121300 !$#map_position 9pter-9qter !$#introns 86/1; 134/1; 171/1; 218/2; 291/2; 326/2 CLASSIFICATION #superfamily coproporphyrinogen oxidase KEYWORDS heme biosynthesis; iron; metalloprotein; mitochondrion; !1oxidoreductase FEATURE !$1-31 #domain transit peptide (mitochondrion) #status !8predicted #label TRP\ !$32-354 #product coproporphyrinogen oxidase, mitochondrial !8#status predicted #label MAT SUMMARY #length 354 #molecular-weight 40291 #checksum 7684 SEQUENCE /// ENTRY A48049 #type complete TITLE coproporphyrinogen oxidase (EC 1.3.3.3) precursor, mitochondrial - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A48049; A54939 REFERENCE A48049 !$#authors Kohno, H.; Furukawa, T.; Yoshinaga, T.; Tokunaga, R.; !1Taketani, S. !$#journal J. Biol. Chem. (1993) 268:21359-21363 !$#title Coproporphyrinogen oxidase. Purification, molecular cloning, !1and induction of mRNA during erythroid differentiation. !$#cross-references MUID:94012692; PMID:8407975 !$#accession A48049 !'##status preliminary !'##molecule_type mRNA; protein !'##residues 1-354 ##label KOH !'##cross-references GB:D16333; NID:g436576; PIDN:BAA03840.1; !1PID:g436577 !'##experimental_source MEL, erythroleukemia cells !'##note sequence extracted from NCBI backbone (NCBIN:138527, !1NCBIP:138528) REFERENCE A54939 !$#authors Martasek, P.; Camadro, J.M.; Delfau-Larue, M.H.; Dumas, !1J.B.; Montagne, J.J.; de Verneuil, H.; Labbe, P.; !1Grandchamp, B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1994) 91:3024-3028 !$#title Molecular cloning, sequencing, and functional expression of !1a cDNA encoding human coproporphyrinogen oxidase. !$#cross-references MUID:94211794; PMID:8159699 !$#accession A54939 !'##molecule_type protein !'##residues 'X',11,'X',13-26,'SD',29-32,'XTFMST',34,'P',36;159-169 !1##label RES CLASSIFICATION #superfamily coproporphyrinogen oxidase KEYWORDS heme biosynthesis; iron; metalloprotein; mitochondrion; !1oxidoreductase FEATURE !$1-9 #domain transit peptide (mitochondrion) #status !8predicted #label TRP\ !$10-354 #product coproporphyrinogen oxidase, mitochondrial !8#status experimental #label MAT SUMMARY #length 354 #molecular-weight 40648 #checksum 2313 SEQUENCE /// ENTRY B53302 #type complete TITLE coproporphyrinogen oxidase (EC 1.3.3.3) - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B53302 REFERENCE A53302 !$#authors Xu, K.; Elliott, T. !$#journal J. Bacteriol. (1993) 175:4990-4999 !$#title An oxygen-dependent coproporphyrinogen oxidase encoded by !1the hemF gene of Salmonella typhimurium. !$#cross-references MUID:93352403; PMID:8349542 !$#accession B53302 !'##status preliminary !'##molecule_type DNA !'##residues 1-299 ##label XUA !'##cross-references GB:L19503; NID:g310640; PIDN:AAA27139.1; !1PID:g310642 CLASSIFICATION #superfamily coproporphyrinogen oxidase KEYWORDS oxidoreductase SUMMARY #length 299 #molecular-weight 34429 #checksum 9284 SEQUENCE /// ENTRY B36964 #type complete TITLE coproporphyrinogen oxidase (EC 1.3.3.3) III, aerobic - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS B36964; C65018 REFERENCE A36964 !$#authors Troup, B.; Jahn, M.; Hungerer, C.; Jahn, D. !$#journal J. Bacteriol. (1994) 176:673-680 !$#title Isolation of the hemF operon containing the gene for the !1Escherichia coli aerobic coproporphyrinogen III oxidase by !1in vivo complementation of a yeast HEM13 mutant. !$#cross-references MUID:94131946; PMID:8300522 !$#accession B36964 !'##status preliminary !'##molecule_type DNA !'##residues 1-299 ##label TRO !'##cross-references GB:X75413; NID:g453967; PIDN:CAA53167.1; !1PID:g453969 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65018 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-299 ##label BLAT !'##cross-references GB:AE000331; GB:U00096; NID:g1788775; !1PIDN:AAC75489.1; PID:g1788777; UWGP:b2436 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene hemF CLASSIFICATION #superfamily coproporphyrinogen oxidase KEYWORDS oxidoreductase SUMMARY #length 299 #molecular-weight 34322 #checksum 8771 SEQUENCE /// ENTRY S52924 #type complete TITLE coproporphyrinogen oxidase (EC 1.3.3.3) oxygen-dependent - Pseudomonas aeruginosa ALTERNATE_NAMES coproporphyrinogen III oxidase, aerobic ORGANISM #formal_name Pseudomonas aeruginosa DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 31-Dec-2000 ACCESSIONS S52924; F83641 REFERENCE S52923 !$#authors Hungerer, C.; Troup, B.; Jahn, D. !$#submission submitted to the EMBL Data Library, February 1995 !$#description Cloning and regulation of the Pseudomonas aeruginosa hemF !1gene encoding oxygen-dependent coproporphyrinogen III !1oxidase. !$#accession S52924 !'##status preliminary !'##molecule_type DNA !'##residues 1-305 ##label HUN !'##cross-references EMBL:X85015; NID:g747872; PIDN:CAA59376.1; !1PID:g695693 REFERENCE A82950 !$#authors Stover, C.K.; Pham, X.Q.; Erwin, A.L.; Mizoguchi, S.D.; !1Warrener, P.; Hickey, M.J.; Brinkman, F.S.L.; Hufnagle, !1W.O.; Kowalik, D.J.; Lagrou, M.; Garber, R.L.; Goltry, L.; !1Tolentino, E.; Westbrook-Wadman, S.; Yuan, Y.; Brody, L.L.; !1Coulter, S.N.; Folger, K.R.; Kas, A.; Larbig, K.; Lim, R.M.; !1Smith, K.A.; Spencer, D.H.; Wong, G.K.S.; Wu, Z.; Paulsen, !1I.T.; Reizer, J.; Saier, M.H.; Hancock, R.E.W.; Lory, S.; !1Olson, M.V. !$#journal Nature (2000) 406:959-964 !$#title Complete genome sequence of Pseudomonas aeruginosa PA01, an !1opportunistic pathogen. !$#cross-references MUID:20437337; PMID:10984043 !$#accession F83641 !'##status preliminary !'##molecule_type DNA !'##residues 1-305 ##label STO !'##cross-references GB:AE004442; GB:AE004091; NID:g9945843; !1PIDN:AAG03414.1; GSPDB:GN00131; PASP:PA0024 !'##experimental_source strain PAO1 GENETICS !$#gene hemF; PA0024 !$#start_codon GTG CLASSIFICATION #superfamily coproporphyrinogen oxidase KEYWORDS oxidoreductase SUMMARY #length 305 #molecular-weight 34806 #checksum 237 SEQUENCE /// ENTRY S39523 #type complete TITLE coproporphyrinogen oxidase (EC 1.3.3.3) precursor - soybean ORGANISM #formal_name Glycine max #common_name soybean DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S39523; S39905; S39524 REFERENCE S39523 !$#authors Madsen, O.; Sandal, L.; Sandal, N.N.; Marcker, K.A. !$#journal Plant Mol. Biol. (1993) 23:35-43 !$#title A soybean coproporphyrinogen oxidase gene is highly !1expressed in root nodules. !$#cross-references MUID:94033295; PMID:8219054 !$#accession S39523 !'##molecule_type DNA !'##residues 1-385 ##label MAD !'##cross-references EMBL:X71083 REFERENCE S39905 !$#authors Sandal, N.N. !$#submission submitted to the EMBL Data Library, March 1993 !$#accession S39905 !'##molecule_type DNA !'##residues 1-46,'V',48-385 ##label SAN !'##cross-references EMBL:X71083; NID:g414665; PIDN:CAA50400.1; !1PID:g414666 GENETICS !$#genome nuclear !$#introns 174/3; 200/1; 231/3; 259/3; 289/1; 330/3; 363/3 CLASSIFICATION #superfamily coproporphyrinogen oxidase KEYWORDS chloroplast; iron; oxidative decarboxylation; oxidoreductase FEATURE !$1-67 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$68-385 #product coproporphyrinogen oxidase #status predicted !8#label MAT SUMMARY #length 385 #molecular-weight 43279 #checksum 5213 SEQUENCE /// ENTRY B69640 #type complete TITLE coproporphyrinogen oxidase (EC 1.3.3.3) III, oxygen-independent hemN - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS B69640 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69640 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-366 ##label KUN !'##cross-references GB:Z99117; GB:AL009126; NID:g2634966; !1PIDN:CAB14492.1; PID:g2634996 !'##experimental_source strain 168 GENETICS !$#gene hemN CLASSIFICATION #superfamily oxygen-independent coproporphyrinogen oxidase KEYWORDS oxidoreductase SUMMARY #length 366 #molecular-weight 41562 #checksum 5900 SEQUENCE /// ENTRY S75358 #type complete TITLE coproporphyrinogen oxidase (EC 1.3.3.3) III, oxygen-independent - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S75358 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75358 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-412 ##label KAN !'##cross-references EMBL:D90904; GB:AB001339; NID:g1652225; !1PIDN:BAA17272.1; PID:g1652349 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily oxygen-independent coproporphyrinogen oxidase KEYWORDS oxidoreductase SUMMARY #length 412 #molecular-weight 46446 #checksum 8675 SEQUENCE /// ENTRY B64070 #type complete TITLE coproporphyrinogen oxidase (EC 1.3.3.3) III, oxygen-independent HI0463 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B64070 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession B64070 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-383 ##label TIGR !'##cross-references GB:U32729; GB:L42023; NID:g1573439; !1PIDN:AAC22122.1; PID:g1573441; TIGR:HI0463 CLASSIFICATION #superfamily oxygen-independent coproporphyrinogen oxidase KEYWORDS oxidoreductase SUMMARY #length 383 #molecular-weight 44105 #checksum 1257 SEQUENCE /// ENTRY B64673 #type complete TITLE coproporphyrinogen oxidase (EC 1.3.3.3) III, oxygen-independent - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B64673 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession B64673 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-352 ##label TOM !'##cross-references GB:AE000628; GB:AE000511; NID:g2314386; !1PIDN:AAD08271.1; PID:g2314389; TIGR:HP1226 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily oxygen-independent coproporphyrinogen oxidase KEYWORDS oxidoreductase SUMMARY #length 352 #molecular-weight 40196 #checksum 7296 SEQUENCE /// ENTRY F65191 #type complete TITLE coproporphyrinogen oxidase (EC 1.3.3.3) III, oxygen-independent - Escherichia coli (strain K-12) ALTERNATE_NAMES hypothetical protein o459 ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS F65191; S40812; A57252; S49373 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65191 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-459 ##label BLAT !'##cross-references GB:AE000462; GB:U00096; NID:g1790295; !1PIDN:AAC76864.1; PID:g1790298; UWGP:b3867 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S40802 !$#authors Plunkett III, G.; Burland, V.; Daniels, D.L.; Blattner, F.R. !$#journal Nucleic Acids Res. (1993) 21:3391-3398 !$#title Analysis of the Escherichia coli genome. III. DNA sequence !1of the region from 87.2 to 89.2 minutes. !$#cross-references MUID:93347969; PMID:8346018 !$#accession S40812 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-232,'XX',235-459 ##label PLU !'##cross-references EMBL:L19201; NID:g304961; PIDN:AAB03001.1; !1PID:g304972 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1993 REFERENCE A57252 !$#authors Troup, B.; Hungerer, C.; Jahn, D. !$#journal J. Bacteriol. (1995) 177:3326-3331 !$#title Cloning and characterization of the Escherichia coli hemN !1gene encoding the oxygen-independent coproporphyrinogen III !1oxidase. !$#cross-references MUID:95286520; PMID:7768836 !$#accession A57252 !'##status preliminary !'##molecule_type DNA !'##residues 3-233,'V',235-459 ##label TRO !'##cross-references EMBL:X82073; NID:g557232; PIDN:CAA57578.1; !1PID:g557233 GENETICS !$#gene hemN !$#start_codon GTG CLASSIFICATION #superfamily oxygen-independent coproporphyrinogen oxidase KEYWORDS oxidoreductase SUMMARY #length 459 #molecular-weight 52947 #checksum 1741 SEQUENCE /// ENTRY OXCKP2 #type complete TITLE acyl-CoA oxidase (EC 1.3.3.6) PXP2, peroxisomal - yeast (Candida tropicalis) ORGANISM #formal_name Candida tropicalis DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 11-Jun-1999 ACCESSIONS A27331 REFERENCE A27331 !$#authors Okazaki, K.; Tan, H.; Fukui, S.; Kubota, I.; Kamiryo, T. !$#journal Gene (1987) 58:37-44 !$#title Peroxisomal acyl-coenzyme A oxidase multigene family of the !1yeast Candida tropicalis; nucleotide sequence of a third !1gene and its protein product. !$#cross-references MUID:88084444; PMID:3692174 !$#accession A27331 !'##molecule_type DNA !'##residues 1-724 ##label OKA !'##cross-references GB:M18259; NID:g170909; PIDN:AAA34361.1; !1PID:g170910 COMMENT This enzyme, located in peroxisomes, catalyzes the !1oxygen-specific oxidation of long-chain (8 and up) acyl-CoA !1to trans-2,3-dehydroacyl-CoA with oxygen being converted to !1hydrogen peroxide; this reaction is the initial step of the !1peroxisomal beta-oxidation system. In C. tropicalis, the !1active enzyme is an octamer of identical FAD-containing !1chains, encoded by nuclear genes of a multigene family. COMMENT The peroxisomes are eukaryote subcellular organelles that !1generate and degrade hydrogen peroxide. They therefore !1contain various oxidases, catalases, and other related !1enzymes. The metabolic reactions as well as the enzymes !1involved are usually different from the mitochondrial !1equivalents. GENETICS !$#gene POX2 CLASSIFICATION #superfamily acyl-CoA oxidase KEYWORDS FAD; fatty acid oxidation; flavoprotein; oxidoreductase; !1peroxisome SUMMARY #length 724 #molecular-weight 81935 #checksum 4180 SEQUENCE /// ENTRY OXCKX4 #type complete TITLE acyl-CoA oxidase (EC 1.3.3.6) POX4, peroxisomal - yeast (Candida tropicalis) ALTERNATE_NAMES acyl-CoA oxidase II ORGANISM #formal_name Candida tropicalis DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 11-Jun-1999 ACCESSIONS A25123 REFERENCE A94084 !$#authors Okazaki, K.; Takechi, T.; Kambara, N.; Fukui, S.; Kubota, !1I.; Kamiryo, T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:1232-1236 !$#title Two acyl-coenzyme A oxidases in peroxisomes of the yeast !1Candida tropicalis: primary structures deduced from genomic !1DNA sequence. !$#cross-references MUID:86149279; PMID:3456583 !$#accession A25123 !'##molecule_type DNA !'##residues 1-709 ##label OKA !'##cross-references GB:M12160; NID:g170911; PIDN:AAA34362.1; !1PID:g170912 !'##experimental_source strain pK233, ATCC 20336 COMMENT This enzyme, located in peroxisomes, catalyzes the !1oxygen-specific oxidation of long-chain (8 and up) acyl-CoA !1to trans-2,3-dehydroacyl-CoA with oxygen being converted to !1hydrogen peroxide; this reaction is the initial step of the !1peroxisomal beta-oxidation system. In C. tropicalis, the !1active enzyme is an octamer of identical FAD-containing !1chains, encoded by nuclear genes of a multigene family. COMMENT The peroxisomes are eukaryote subcellular organelles that !1generate and degrade hydrogen peroxide. They therefore !1contain various oxidases, catalases, and other related !1enzymes. The metabolic reactions as well as the enzymes !1involved are usually different from the mitochondrial !1equivalents. GENETICS !$#gene POX4 CLASSIFICATION #superfamily acyl-CoA oxidase KEYWORDS FAD; fatty acid oxidation; flavoprotein; oxidoreductase; !1peroxisome SUMMARY #length 709 #molecular-weight 78774 #checksum 4824 SEQUENCE /// ENTRY OXCKAX #type fragment TITLE acyl-CoA oxidase (EC 1.3.3.6) POX4-2, peroxisomal - yeast (Candida tropicalis) (fragment) ALTERNATE_NAMES acyl-CoA oxidase II-2 ORGANISM #formal_name Candida tropicalis DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 11-Jun-1999 ACCESSIONS A28584 REFERENCE A28584 !$#authors Small, G.M.; Lazarow, P.B. !$#journal J. Cell Biol. (1987) 105:247-250 !$#title Import of the carboxy-terminal portion of acyl-CoA oxidase !1into peroxisomes of Candida tropicalis. !$#cross-references MUID:87280361; PMID:3611187 !$#accession A28584 !'##molecule_type mRNA !'##residues 1-502 ##label SMA !'##cross-references GB:Y00623; NID:g2672; PIDN:CAA68660.1; PID:g2673 GENETICS !$#gene POX4-2 CLASSIFICATION #superfamily acyl-CoA oxidase KEYWORDS FAD; fatty acid oxidation; flavoprotein; oxidoreductase; !1peroxisome SUMMARY #length 502 #checksum 6643 SEQUENCE /// ENTRY OXCKX #type complete TITLE acyl-CoA oxidase (EC 1.3.3.6) AOx, peroxisomal - yeast (Candida tropicalis) ORGANISM #formal_name Candida tropicalis DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 30-Sep-1993 ACCESSIONS A29047 REFERENCE A29047 !$#authors Murray, W.W.; Rachubinski, R.A. !$#journal Gene (1987) 51:119-128 !$#title The primary structure of a peroxisomal fatty acyl-CoA !1oxidase from the yeast Candida tropicalis pK233. !$#cross-references MUID:87248070; PMID:3596241 !$#accession A29047 !'##molecule_type DNA !'##residues 1-709 ##label MUR !'##experimental_source strain pK233, ATCC 20336 GENETICS !$#gene AOx CLASSIFICATION #superfamily acyl-CoA oxidase KEYWORDS FAD; fatty acid oxidation; flavoprotein; oxidoreductase; !1peroxisome SUMMARY #length 709 #molecular-weight 79146 #checksum 2978 SEQUENCE /// ENTRY OXCKPM #type complete TITLE acyl-CoA oxidase (EC 1.3.3.6) PXP4, peroxisomal - yeast (Candida maltosa) ORGANISM #formal_name Candida maltosa DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 17-Feb-1995 ACCESSIONS A29441 REFERENCE A29441 !$#authors Hill, D.E.; Boulay, R.; Rogers, D. !$#journal Nucleic Acids Res. (1988) 16:365-366 !$#title Complete nucleotide sequence of the peroxisomal acyl CoA !1oxidase from the alkane-utilizing yeast Candida maltosa. !$#cross-references MUID:88124223; PMID:3340538 !$#accession A29441 !'##molecule_type DNA !'##residues 1-709 ##label HIL !'##experimental_source ATCC 20184 GENETICS !$#gene POX4 CLASSIFICATION #superfamily acyl-CoA oxidase KEYWORDS FAD; fatty acid oxidation; flavoprotein; oxidoreductase; !1peroxisome SUMMARY #length 709 #molecular-weight 78277 #checksum 8367 SEQUENCE /// ENTRY OXCKX5 #type complete TITLE acyl-CoA oxidase (EC 1.3.3.6) POX5, peroxisomal - yeast (Candida tropicalis) ALTERNATE_NAMES acyl-CoA oxidase I ORGANISM #formal_name Candida tropicalis DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 11-Jun-1999 ACCESSIONS B25123 REFERENCE A94084 !$#authors Okazaki, K.; Takechi, T.; Kambara, N.; Fukui, S.; Kubota, !1I.; Kamiryo, T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:1232-1236 !$#title Two acyl-coenzyme A oxidases in peroxisomes of the yeast !1Candida tropicalis: primary structures deduced from genomic !1DNA sequence. !$#cross-references MUID:86149279; PMID:3456583 !$#accession B25123 !'##molecule_type DNA !'##residues 1-662 ##label OKA !'##cross-references GB:M12161; NID:g170913; PIDN:AAA34363.1; !1PID:g170914 COMMENT This enzyme, located in peroxisomes, catalyzes the !1oxygen-specific oxidation of long-chain (8 and up) acyl-CoA !1to trans-2,3-dehydroacyl-CoA with oxygen being converted to !1hydrogen peroxide; this reaction is the initial step of the !1peroxisomal beta-oxidation system. In C. tropicalis, the !1active enzyme is an octamer of identical FAD-containing !1chains, encoded by nuclear genes of a multigene family. COMMENT The peroxisomes are eukaryote subcellular organelles that !1generate and degrade hydrogen peroxide. They therefore !1contain various oxidases, catalases, and other related !1enzymes. The metabolic reactions as well as the enzymes !1involved are usually different from the mitochondrial !1equivalents. GENETICS !$#gene POX5 CLASSIFICATION #superfamily acyl-CoA oxidase KEYWORDS FAD; fatty acid oxidation; flavoprotein; oxidoreductase; !1peroxisome SUMMARY #length 662 #molecular-weight 74263 #checksum 3893 SEQUENCE /// ENTRY OXRTA1 #type complete TITLE acyl-CoA oxidase (EC 1.3.3.6) chain A, peroxisomal splice form I - rat CONTAINS acyl-CoA oxidase component B; acyl-CoA oxidase component C ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 10-Dec-1999 ACCESSIONS A29328 REFERENCE A92649 !$#authors Miyazawa, S.; Hayashi, H.; Hijikata, M.; Ishii, N.; Furuta, !1S.; Kagamiyama, H.; Osumi, T.; Hashimoto, T. !$#journal J. Biol. Chem. (1987) 262:8131-8137 !$#title Complete nucleotide sequence of cDNA and predicted amino !1acid sequence of rat acyl-CoA oxidase. !$#cross-references MUID:87250404; PMID:3036800 !$#accession A29328 !'##molecule_type mRNA !'##residues 1-661 ##label MIY !'##cross-references GB:J02752; NID:g202677; PIDN:AAA40666.1; !1PID:g202678 COMMENT This FAD enzyme, located in peroxisomes, catalyzes the !1oxygen-specific oxidation of long-chain (8 and up) acyl-CoA !1to trans-2,3-dehydroacyl-CoA with oxygen being converted to !1hydrogen peroxide. COMMENT This enzyme is a mixture of different combinations of three !1polypeptide chains, A, B, and C, with the B and C chains !1derived from proteolytic cleavage of the A chain. For splice !1form II, see PIR:OXRTA2. COMMENT The peroxisomes are eukaryote subcellular organelles that !1generate and degrade hydrogen peroxide. They therefore !1contain various oxidases, catalases, and other related !1enzymes. The metabolic reactions as well as the enzymes !1involved are biochemically and immunologically different !1from the mitochondrial counterparts. CLASSIFICATION #superfamily acyl-CoA oxidase KEYWORDS alternative splicing; FAD; fatty acid oxidation; !1flavoprotein; oxidoreductase; peroxisome FEATURE !$1-438 #product acyl-CoA oxidase, peroxisomal splice form I, !8chain B #status predicted #label BCH\ !$439-661 #product acyl-CoA oxidase, peroxisomal, chain C !8#status predicted #label CCH\ !$659-661 #region peroxisome/glyoxysome location signal !8(S-[RKH]-L) motif SUMMARY #length 661 #molecular-weight 74678 #checksum 9112 SEQUENCE /// ENTRY OXRTA2 #type complete TITLE acyl-CoA oxidase (EC 1.3.3.6) chain A, peroxisomal splice form II - rat CONTAINS acyl-CoA oxidase component B; acyl-CoA oxidase component C ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 10-Dec-1999 ACCESSIONS B29328; I55261 REFERENCE A92649 !$#authors Miyazawa, S.; Hayashi, H.; Hijikata, M.; Ishii, N.; Furuta, !1S.; Kagamiyama, H.; Osumi, T.; Hashimoto, T. !$#journal J. Biol. Chem. (1987) 262:8131-8137 !$#title Complete nucleotide sequence of cDNA and predicted amino !1acid sequence of rat acyl-CoA oxidase. !$#cross-references MUID:87250404; PMID:3036800 !$#accession B29328 !'##molecule_type mRNA !'##residues 1-661 ##label MIY REFERENCE I55261 !$#authors Osumi, T.; Ishii, N.; Miyazawa, S.; Hashimoto, T. !$#journal J. Biol. Chem. (1987) 262:8138-8143 !$#title Isolation and structural characterization of the rat !1acyl-CoA oxidase gene. !$#cross-references MUID:87250405; PMID:3036801 !$#accession I55261 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-36 ##label RES !'##cross-references GB:J02753; NID:g202679; PIDN:AAA40667.1; !1PID:g554410 COMMENT This FAD enzyme, located in peroxisomes, catalyzes the !1oxygen-specific oxidation of long-chain (8 and up) acyl-CoA !1to trans-2,3-dehydroacyl-CoA with oxygen being converted to !1hydrogen peroxide. COMMENT This enzyme is a mixture of different combinations of three !1polypeptide chains, A, B, and C, with the B and C chains !1derived from proteolytic cleavage of the A chain. For splice !1form I, see PIR:OXRTA1. COMMENT The peroxisomes are eukaryote subcellular organelles that !1generate and degrade hydrogen peroxide. They therefore !1contain various oxidases, catalases, and other related !1enzymes. The metabolic reactions as well as the enzymes !1involved are biochemically and immunologically different !1from the mitochondrial counterparts. GENETICS !$#gene aCoA CLASSIFICATION #superfamily acyl-CoA oxidase KEYWORDS alternative splicing; FAD; fatty acid oxidation; !1flavoprotein; oxidoreductase; peroxisome FEATURE !$1-438 #product acyl-CoA oxidase, peroxisomal splice form !8II, chain B #status predicted #label BCH\ !$439-661 #product acyl-CoA oxidase, peroxisomal, chain C !8#status predicted #label CCH\ !$659-661 #region peroxisome/glyoxysome location signal !8(S-[RKH]-L) motif SUMMARY #length 661 #molecular-weight 74690 #checksum 6914 SEQUENCE /// ENTRY A54942 #type complete TITLE acyl-CoA oxidase (EC 1.3.3.6), peroxisomal splice form I - human ALTERNATE_NAMES peroxisomal acyl-coenzyme A oxidase ORGANISM #formal_name Homo sapiens #common_name man DATE 18-Nov-1994 #sequence_revision 11-Aug-1995 #text_change 31-Dec-2000 ACCESSIONS A54942; JC2066; G01400 REFERENCE A54942 !$#authors Varanasi, U.; Chu, R.; Chu, S.; Espinosa, R.; LeBeau, M.M.; !1Reddy, J.K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1994) 91:3107-3111 !$#title Isolation of the human peroxisomal acyl-CoA oxidase gene: !1organization, promoter analysis, and chromosomal !1localization. !$#cross-references MUID:94211811; PMID:8159712 !$#accession A54942 !'##molecule_type DNA !'##residues 1-660 ##label VAR !'##cross-references GB:U03254; GB:U03255; GB:U03256; GB:U03258; !1GB:U03259; GB:U03260; GB:U03261; GB:U03262; GB:U03263; !1GB:U03264; GB:U03265; GB:U03266; GB:U03267; GB:U03268; !1NID:g458117; PIDN:AAA19113.1; PID:g458119 REFERENCE JC2066 !$#authors Aoyama, T.; Tsushima, K.; Souri, M.; Kamijo, T.; Suzuki, Y.; !1Shimozawa, N.; Orii, T.; Hashimoto, T. !$#journal Biochem. Biophys. Res. Commun. (1994) 198:1113-1118 !$#title Molecular cloning and functional expression of a human !1peroxisomal acyl-coenzyme A oxidase. !$#cross-references MUID:94161722; PMID:8117268 !$#accession JC2066 !'##molecule_type mRNA !'##residues 1-118,'E',120-211,'IG',214-263,'T',265-311,'M',313-530,'C', !1532-533,'VV',536-650,'H',651-660 ##label AOY !'##cross-references GB:S69189; NID:g545593; PIDN:AAB30019.1; !1PID:g545594 !'##note the authors translated the codon GAG for residue 119 as Gln REFERENCE G06858 !$#authors Reddy, J.K. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession G01400 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-199,'H',201-331,'L',333-448,'R',450-660 ##label RED !'##cross-references EMBL:U07866; NID:g495474; PIDN:AAA18595.1; !1PID:g495475 COMMENT For splice form II, see PIR:B54942. GENETICS !$#gene GDB:ACOX !'##cross-references GDB:282672; OMIM:264470 !$#map_position 17q24-17q25 FUNCTION !$#description catalyzes the dehydrogenation of acyl-CoA by dioxygen to !1(E)-2-enoyl-CoA and hydrogen peroxide !$#pathway fatty acid beta-oxidation CLASSIFICATION #superfamily acyl-CoA oxidase KEYWORDS alternative splicing; fatty acid beta-oxidation; !1oxidoreductase; peroxisome FEATURE !$658-660 #region peroxisome/glyoxysome location signal !8(S-[RKH]-L) motif SUMMARY #length 660 #molecular-weight 74501 #checksum 4225 SEQUENCE /// ENTRY B54942 #type complete TITLE acyl-CoA oxidase (EC 1.3.3.6), peroxisomal splice form II - human ORGANISM #formal_name Homo sapiens #common_name man DATE 18-Nov-1994 #sequence_revision 11-Aug-1995 #text_change 31-Dec-2000 ACCESSIONS B54942 REFERENCE A54942 !$#authors Varanasi, U.; Chu, R.; Chu, S.; Espinosa, R.; LeBeau, M.M.; !1Reddy, J.K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1994) 91:3107-3111 !$#title Isolation of the human peroxisomal acyl-CoA oxidase gene: !1organization, promoter analysis, and chromosomal !1localization. !$#cross-references MUID:94211811; PMID:8159712 !$#accession B54942 !'##molecule_type DNA !'##residues 1-660 ##label VAR !'##cross-references GB:U03254; GB:U03255; GB:U03257; GB:U03258; !1GB:U03259; GB:U03260; GB:U03261; GB:U03262; GB:U03263; !1GB:U03264; GB:U03265; GB:U03266; GB:U03267; GB:U03268; !1NID:g458117; PIDN:AAA19114.1; PID:g458120 COMMENT For splice form I, see PIR:A54942. GENETICS !$#gene GDB:ACOX !'##cross-references GDB:282672; OMIM:264470 !$#map_position 17q24-17q25 FUNCTION !$#description catalyzes the dehydrogenation of acyl-CoA by dioxygen to !1(E)-2-enoyl-CoA and hydrogen peroxide !$#pathway fatty acid beta-oxidation CLASSIFICATION #superfamily acyl-CoA oxidase KEYWORDS alternative splicing; fatty acid beta-oxidation; !1oxidoreductase; peroxisome FEATURE !$658-660 #region peroxisome/glyoxysome location signal !8(S-[RKH]-L) motif SUMMARY #length 660 #molecular-weight 74745 #checksum 1714 SEQUENCE /// ENTRY DEECS2 #type complete TITLE succinate dehydrogenase (EC 1.3.99.1) 13K protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 01-Mar-2002 ACCESSIONS B28836; I62456; A64808 REFERENCE A94642 !$#authors Wood, D.; Darlison, M.G.; Wilde, R.J.; Guest, J.R. !$#journal Biochem. J. (1984) 222:519-534 !$#title Nucleotide sequence encoding the flavoprotein and !1hydrophobic subunits of the succinate dehydrogenase of !1Escherichia coli. !$#cross-references MUID:84307466; PMID:6383359 !$#accession B28836 !'##molecule_type DNA !'##residues 1-115 ##label WOO !'##cross-references GB:X00980; NID:g42921; PIDN:CAA25486.1; PID:g42924 REFERENCE I41112 !$#authors Wilde, R.J.; Guest, J.R. !$#journal J. Gen. Microbiol. (1986) 132:3239-3251 !$#title Transcript analysis of the citrate synthase and succinate !1dehydrogenase genes of Escherichia coli k-12. !$#cross-references MUID:88009821; PMID:3309132 !$#accession I62456 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-6 ##label RES !'##cross-references GB:M28989; NID:g342042; PIDN:AAA24617.1; !1PID:g495785 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64808 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-115 ##label BLAT !'##cross-references GB:AE000175; GB:U00096; NID:g1786934; !1PIDN:AAC73816.1; PID:g1786941; UWGP:b0722 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene sdhD !$#map_position 17 min COMPLEX one of two hydrophobic anchor components of the succinate !1dehydrogenase complex FUNCTION !$#pathway tricarboxylic acid cycle CLASSIFICATION #superfamily succinate dehydrogenase 13K hydrophobic protein KEYWORDS oxidoreductase; transmembrane protein; tricarboxylic acid !1cycle FEATURE !$16-36 #domain transmembrane #status predicted #label TM1\ !$37-57 #domain transmembrane #status predicted #label TM2\ !$59-79 #domain transmembrane #status predicted #label TM3\ !$95-115 #domain transmembrane #status predicted #label TM4 SUMMARY #length 115 #molecular-weight 12867 #checksum 6993 SEQUENCE /// ENTRY DEBSSC #type complete TITLE succinate dehydrogenase (EC 1.3.99.1) cytochrome b558 - Bacillus subtilis ALTERNATE_NAMES fumarate reductase C protein ORGANISM #formal_name Bacillus subtilis DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 16-Jun-2000 ACCESSIONS A29843; I39972; E69704 REFERENCE A29843 !$#authors Magnusson, K.; Philips, M.K.; Guest, J.R.; Rutberg, L. !$#journal J. Bacteriol. (1986) 166:1067-1071 !$#title Nucleotide sequence of the gene for cytochrome b-558 of the !1Bacillus subtilis succinate dehydrogenase complex. !$#cross-references MUID:86223767; PMID:3086287 !$#accession A29843 !'##molecule_type DNA !'##residues 1-202 ##label MAG !'##cross-references GB:M13470; GB:M15107; NID:g143524; PIDN:AAA22745.1; !1PID:g143525 REFERENCE I39971 !$#authors Melin, L.; Magnusson, K.; Rutberg, L. !$#journal J. Bacteriol. (1987) 169:3232-3236 !$#title Identification of the promoter of the Bacillus subtilis sdh !1operon. !$#cross-references MUID:87250294; PMID:3036777 !$#accession I39972 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-13 ##label RES !'##cross-references GB:M16753; NID:g143528; PIDN:AAA22749.1; !1PID:g143530 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69704 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-202 ##label KUN !'##cross-references GB:Z99118; GB:AL009126; NID:g2635200; !1PIDN:CAB14805.1; PID:g2635310 !'##experimental_source strain 168 COMMENT This transmembrane electron transport protein is one of the !1three components of the B. subtilis succinate dehydrogenanse !1complex. It is required for binding the other two !1components, the flavoprotein and the iron-sulfur protein, to !1the membrane. However, the mode of electron transfer is not !1clear. GENETICS !$#gene sdhC; sdhA !$#map_position 70 !$#note formerly sdhA; renamed sdhC for better compatibility with !1gene names in E. coli CLASSIFICATION #superfamily succinate dehydrogenase cytochrome b558 KEYWORDS electron transfer; oxidoreductase; transmembrane protein; !1tricarboxylic acid cycle FEATURE !$12-31 #domain transmembrane #status predicted #label TM1\ !$60-79 #domain transmembrane #status predicted #label TM2\ !$93-113 #domain transmembrane #status predicted #label TM3\ !$135-155 #domain transmembrane #status predicted #label TM4\ !$178-196 #domain transmembrane #status predicted #label TM5 SUMMARY #length 202 #molecular-weight 22931 #checksum 8977 SEQUENCE /// ENTRY JX0336 #type complete TITLE succinate dehydrogenase (ubiquinone) (EC 1.3.5.1) flavoprotein chain precursor, mitochondrial - human CONTAINS fumarate reductase (EC 1.3.99.1) flavoprotein ORGANISM #formal_name Homo sapiens #common_name man DATE 28-Oct-1994 #sequence_revision 19-Jul-1996 #text_change 16-Jun-2000 ACCESSIONS JX0336; I52450 REFERENCE JX0336 !$#authors Hirawake, H.; Wang, H.; Kuramochi, T.; Kojima, S.; Kita, K. !$#journal J. Biochem. (1994) 116:221-227 !$#title Human complex II (succinate-ubiquinone oxidoreductase): cDNA !1cloning of the flavoprotein (Fp) subunit of liver !1mitochondria. !$#cross-references MUID:95096020; PMID:7798181 !$#accession JX0336 !'##molecule_type mRNA !'##residues 1-664 ##label HIR !'##cross-references DDBJ:D30648; NID:g506337; PIDN:BAA06332.1; !1PID:g506338 !'##experimental_source liver REFERENCE I52450 !$#authors Morris, A.A.; Farnsworth, L.; Ackrell, B.A.; Turnbull, D.M.; !1Birch-Machin, M.A. !$#journal Biochim. Biophys. Acta (1994) 1185:125-128 !$#title The cDNA sequence of the flavoprotein subunit of human heart !1succinate dehydrogenase. !$#cross-references MUID:94190953; PMID:8142412 !$#accession I52450 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-628,'F',630-656,'I',658-664 ##label MOR !'##cross-references GB:L21936; NID:g347133; PIDN:AAA20683.1; !1PID:g347134 GENETICS !$#gene GDB:SDH2 !'##cross-references GDB:378037; OMIM:600857 !$#map_position 5p15-5p15 COMPLEX heterotetramer of two flavoprotein chains and two !1iron-sulfur protein chains (see PIR:I38895) FUNCTION !$#description catalyzes the reversible oxidation of succinate to fumarate !1by ubiquinone !$#pathway tricarboxylic acid cycle CLASSIFICATION #superfamily fumarate reductase flavoprotein; 3-oxosteroid !11-dehydrogenase homology; fumarate reductase flavoprotein !1homology KEYWORDS FAD; flavoprotein; mitochondrion; oxidoreductase; !1phosphoprotein; tricarboxylic acid cycle FEATURE !$1-43 #domain transit peptide (mitochondrion) #status !8predicted #label TPP\ !$44-664 #product succinate dehydrogenase (ubiquinone) !8flavoprotein chain #status predicted #label MAT\ !$63-331 #domain fumarate reductase flavoprotein homology !8#label FRF\ !$362-463 #domain 3-oxosteroid 1-dehydrogenase homology #label !8OXD\ !$99 #modified_site 3'-FAD-histidine (His) #status !8predicted\ !$311 #active_site Cys #status predicted SUMMARY #length 664 #molecular-weight 72691 #checksum 5293 SEQUENCE /// ENTRY A42792 #type complete TITLE succinate dehydrogenase (ubiquinone) (EC 1.3.5.1) flavoprotein chain precursor, mitochondrial - bovine CONTAINS fumarate reductase (EC 1.3.99.1) flavoprotein ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Dec-1993 #sequence_revision 19-Jul-1996 #text_change 09-Apr-1999 ACCESSIONS A42792 REFERENCE A42792 !$#authors Birch-Machin, M.A.; Farnsworth, L.; Ackrell, B.A.; Cochran, !1B.; Jackson, S.; Bindoff, L.A.; Aitken, A.; Diamond, A.G.; !1Turnbull, D.M. !$#journal J. Biol. Chem. (1992) 267:11553-11558 !$#title The sequence of the flavoprotein subunit of bovine heart !1succinate dehydrogenase. !$#cross-references MUID:92283874; PMID:1375942 !$#accession A42792 !'##molecule_type mRNA; protein !'##residues 1-665 ##label BIR !'##cross-references GB:M60879; NID:g387583 !'##experimental_source heart !'##note sequence extracted from NCBI backbone (NCBIP:104758) COMPLEX heterotetramer of two flavoprotein chains and two !1iron-sulfur protein chains FUNCTION !$#description catalyzes the reversible oxidation of succinate to fumarate !1by ubiquinone !$#pathway tricarboxylic acid cycle CLASSIFICATION #superfamily fumarate reductase flavoprotein; 3-oxosteroid !11-dehydrogenase homology; fumarate reductase flavoprotein !1homology KEYWORDS FAD; flavoprotein; heterotetramer; mitochondrion; !1oxidoreductase; phosphoprotein; tricarboxylic acid cycle FEATURE !$1-43 #domain transit peptide (mitochondrion) #status !8predicted #label TPP\ !$44-664 #product succinate dehydrogenase (ubiquinone) !8flavoprotein chain #status predicted #label MAT\ !$64-332 #domain fumarate reductase flavoprotein homology !8#label FRF\ !$64-92 #region beta-alpha-beta FAD nucleotide-binding fold\ !$363-464 #domain 3-oxosteroid 1-dehydrogenase homology #label !8OXD\ !$100 #modified_site 3'-FAD-histidine (His) #status !8predicted\ !$312 #active_site Cys #status predicted SUMMARY #length 665 #molecular-weight 72857 #checksum 8959 SEQUENCE /// ENTRY DEECSF #type complete TITLE succinate dehydrogenase (EC 1.3.99.1) flavoprotein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1988 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS B64808; C28836 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64808 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-588 ##label BLAT !'##cross-references GB:AE000175; GB:U00096; NID:g1786934; !1PIDN:AAC73817.1; PID:g1786942; UWGP:b0723 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A94642 !$#authors Wood, D.; Darlison, M.G.; Wilde, R.J.; Guest, J.R. !$#journal Biochem. J. (1984) 222:519-534 !$#title Nucleotide sequence encoding the flavoprotein and !1hydrophobic subunits of the succinate dehydrogenase of !1Escherichia coli. !$#cross-references MUID:84307466; PMID:6383359 !$#accession C28836 !'##molecule_type DNA !'##residues 1-19,'IAR',23-588 ##label WOO !'##cross-references GB:X00980; NID:g42921; PIDN:CAA25487.1; PID:g42925 COMMENT In E. coli, two distinct, membrane-bound, FAD-containing !1enzymes are responsible for the catalysis of fumarate and !1succinate interconversion; fumarate reductase is used in !1anaerobic growth and succinate dehydrogenase in aerobic !1growth. The protein shown, which covalently binds FAD and !1contains an iron-sulfur center, is one of two catalytic !1components constituting the functional succinate !1dehydrogenase; the other component is an iron-sulfur !1protein. GENETICS !$#gene sdhA !$#map_position 17 min CLASSIFICATION #superfamily fumarate reductase flavoprotein; 3-oxosteroid !11-dehydrogenase homology; fumarate reductase flavoprotein !1homology KEYWORDS FAD; flavoprotein; oxidoreductase; phosphoprotein; !1tricarboxylic acid cycle FEATURE !$9-277 #domain fumarate reductase flavoprotein homology !8#label FRF\ !$9-37 #region beta-alpha-beta FAD nucleotide-binding fold\ !$309-411 #domain 3-oxosteroid 1-dehydrogenase homology #label !8OXD\ !$45 #modified_site 3'-FAD-histidine (His) #status !8predicted\ !$257 #active_site Cys #status predicted SUMMARY #length 588 #molecular-weight 64421 #checksum 4157 SEQUENCE /// ENTRY RDECFF #type complete TITLE fumarate reductase (EC 1.3.99.1) flavoprotein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 01-Mar-2002 ACCESSIONS A00376; S56382; H65225 REFERENCE A91118 !$#authors Cole, S.T. !$#journal Eur. J. Biochem. (1982) 122:479-484 !$#title Nucleotide sequence coding for the flavoprotein subunit of !1the fumarate reductase of Escherichia coli. !$#cross-references MUID:82138876; PMID:7037404 !$#accession A00376 !'##molecule_type DNA !'##residues 1-602 ##label COL !'##note the authors translated the codon CTG for residue 285 as Glu REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56382 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-602 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97053.1; !1PID:g536998 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65225 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-602 ##label BLAT !'##cross-references GB:AE000487; GB:U00096; NID:g1790582; !1PIDN:AAC77114.1; PID:g1790597; UWGP:b4154 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene frdA !$#map_position 94 min !$#start_codon GTG COMPLEX heterotetramer (FAD linked flavoprotein, iron-sulfur !1protein, 13K and 15K membrane anchor protein) FUNCTION !$#description in E. coli, two distinct, membrane-bound, FAD-containing !1enzymes are responsible for the catalysis of fumarate and !1succinate interconversion; the fumarate reductase is used in !1anaerobic growth, and the succinate dehydrogenase is used in !1aerobic growth CLASSIFICATION #superfamily fumarate reductase flavoprotein; 3-oxosteroid !11-dehydrogenase homology; fumarate reductase flavoprotein !1homology KEYWORDS FAD; flavoprotein; heterotetramer; oxidoreductase; !1phosphoprotein FEATURE !$7-268 #domain fumarate reductase flavoprotein homology !8#label FRF\ !$311-403 #domain 3-oxosteroid 1-dehydrogenase homology #label !8OXD\ !$45 #modified_site 3'-FAD-histidine (His) #status !8experimental\ !$248 #active_site Cys #status predicted SUMMARY #length 602 #molecular-weight 65971 #checksum 8771 SEQUENCE /// ENTRY RDEBFV #type complete TITLE fumarate reductase (EC 1.3.99.1) flavoprotein - Proteus vulgaris ALTERNATE_NAMES fumarate reductase chain A; succinate dehydrogenase flavoprotein ORGANISM #formal_name Proteus vulgaris DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 11-Jun-1999 ACCESSIONS S00107 REFERENCE S00107 !$#authors Cole, S.T. !$#journal Eur. J. Biochem. (1987) 167:481-488 !$#title Nucleotide sequence and comparative analysis of the frd !1operon encoding the fumarate reductase of Proteus vulgaris. !1Extensive sequence divergence of the membrane anchors and !1absence of an frd-linked ampC cephalosporinase gene. !$#cross-references MUID:88004470; PMID:3308458 !$#accession S00107 !'##molecule_type DNA !'##residues 1-598 ##label COL !'##cross-references EMBL:X06144; NID:g45917; PIDN:CAA29501.1; !1PID:g581487 GENETICS !$#gene frdA !$#start_codon GTG CLASSIFICATION #superfamily fumarate reductase flavoprotein; 3-oxosteroid !11-dehydrogenase homology; fumarate reductase flavoprotein !1homology KEYWORDS FAD; flavoprotein; heterotetramer; oxidoreductase; !1phosphoprotein FEATURE !$7-268 #domain fumarate reductase flavoprotein homology !8#label FRF\ !$9-23 #region AMP binding #status predicted\ !$311-403 #domain 3-oxosteroid 1-dehydrogenase homology #label !8OXD\ !$45 #modified_site 3'-FAD-histidine (His) #status !8experimental\ !$248 #active_site Cys #status predicted SUMMARY #length 598 #molecular-weight 66141 #checksum 327 SEQUENCE /// ENTRY OXECLD #type complete TITLE L-aspartate oxidase (EC 1.4.3.16) nadB [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES quinolinate synthetase B ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS E65035; S01132; S09000 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65035 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-540 ##label BLAT !'##cross-references GB:AE000344; GB:U00096; NID:g1788927; !1PIDN:AAC75627.1; PID:g1788928; UWGP:b2574 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S01131 !$#authors Flachmann, R.; Kunz, N.; Seifert, J.; Guetlich, M.; !1Wientjes, F.J.; Laeufer, A.; Gassen, H.G. !$#journal Eur. J. Biochem. (1988) 175:221-228 !$#title Molecular biology of pyridine nucleotide biosynthesis in !1Escherichia coli: cloning and characterization of !1quinolinate synthesis genes nadA and nadB. !$#cross-references MUID:88296484; PMID:2841129 !$#accession S01132 !'##molecule_type DNA !'##residues 1-159,'T',161-290,'H',292-484,'D',486-540 ##label FLA !'##cross-references EMBL:X12714 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE S09000 !$#authors Seifert, J.; Kunz, N.; Flachmann, R.; Laeufer, A.; Jany, !1K.D.; Gassen, H.G. !$#journal Biol. Chem. Hoppe-Seyler (1990) 371:239-248 !$#title Expression of the E. coli nadB gene and characterization of !1the gene product L-aspartate oxidase. !$#cross-references MUID:90253646; PMID:2187483 !$#accession S09000 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-159,'T',161-290,'H',292-484,'D',486-540 ##label SEI !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing GENETICS !$#gene nadB !$#map_position 56 min FUNCTION !$#description EC 1.4.3.16 [validated, MUID:90253646]; catalyzes the !1FAD-dependent oxidation of L-aspartate to iminoaspartate, !1the intermediate that leads to the formation of quinolinate, !1catalyzed by nadA (PIR:SYECQA) !$#note one of two components of the quinolinate synthetase complex, !1consisting of nadA and nadB !$#note quinolinate (pyridine-2,3-dicarboxylate) is the biosynthetic !1precursor of the pyridine ring of NAD CLASSIFICATION #superfamily fumarate reductase flavoprotein; 3-oxosteroid !11-dehydrogenase homology; fumarate reductase flavoprotein !1homology KEYWORDS FAD; flavoprotein; oxidoreductase; pyridine nucleotide !1biosynthesis FEATURE !$2-540 #product L-aspartate oxidase #status experimental !8#label MAT\ !$10-282 #domain fumarate reductase flavoprotein homology !8#label FRF\ !$10-37 #region beta-alpha-beta FAD nucleotide-binding fold\ !$307-398 #domain 3-oxosteroid 1-dehydrogenase homology #label !8OXD SUMMARY #length 540 #molecular-weight 60337 #checksum 9218 SEQUENCE /// ENTRY B44954 #type complete TITLE fumarate reductase (EC 1.3.99.1) flavoprotein - Wolinella succinogenes ALTERNATE_NAMES fumarate reductase chain A ORGANISM #formal_name Wolinella succinogenes DATE 03-Jun-1993 #sequence_revision 19-Jul-1996 #text_change 11-Jun-1999 ACCESSIONS B44954; S10165 REFERENCE A44954 !$#authors Lauterbach, F.; Koertner, C.; Albracht, S.P.J.; Unden, G.; !1Kroeger, A. !$#journal Arch. Microbiol. (1990) 154:386-393 !$#title The fumarate reductase operon of Wolinella succinogenes. !1Sequence and expression of the frdA and frdB genes. !$#cross-references MUID:91058386; PMID:2244791 !$#accession B44954 !'##status preliminary !'##molecule_type DNA !'##residues 1-656 ##label LAU !'##cross-references GB:X51509; NID:g48511; PIDN:CAA35875.1; PID:g48513 REFERENCE S10164 !$#authors Koertner, C.; Lauterbach, F.; Tripier, D.; Unden, G.; !1Kroeger, A. !$#journal Mol. Microbiol. (1990) 4:855-860 !$#title Wolinella succinogenes fumarate reductase contains a dihaem !1cytochrome b. !$#cross-references MUID:90355847; PMID:2388563 !$#accession S10165 !'##status preliminary; translation not shown !'##molecule_type DNA !'##residues 1-656 ##label KOE !'##cross-references EMBL:X51509; NID:g48511; PIDN:CAA35875.1; !1PID:g48513 GENETICS !$#gene frdA COMPLEX part of an enzyme complex containing a heterotrimer !1(flavoprotein, iron-sulfer protein and a cytochrome B) FUNCTION !$#description catalyzes the oxidation of succinate to fumarate and !1transfers its reducing equivalents to ubiquinone; it is the !1site of succinate-fumarate conversion and forms the !1catalytic portion of the complex together with the iron !1sulfur subunit CLASSIFICATION #superfamily fumarate reductase flavoprotein; 3-oxosteroid !11-dehydrogenase homology; fumarate reductase flavoprotein !1homology KEYWORDS FAD; flavoprotein; oxidoreductase; phosphoprotein; !1tricarboxylic acid cycle FEATURE !$7-292 #domain fumarate reductase flavoprotein homology !8#label FRF\ !$324-416 #domain 3-oxosteroid 1-dehydrogenase homology #label !8OXD\ !$43 #modified_site 3'-FAD-histidine (His) #status !8predicted\ !$272 #active_site Cys #status predicted SUMMARY #length 656 #molecular-weight 72801 #checksum 8645 SEQUENCE /// ENTRY S25968 #type complete TITLE succinate dehydrogenase (ubiquinone) (EC 1.3.5.1) chain 3 - liverwort (Marchantia polymorpha) mitochondrion ALTERNATE_NAMES hypothetical protein 137 ORGANISM #formal_name mitochondrion Marchantia polymorpha DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S25968 REFERENCE S25941 !$#authors Oda, K.; Yamato, K.; Ohta, E.; Nakamura, Y.; Takemura, M.; !1Nozato, N.; Akashi, K.; Kanegae, T.; Ogura, Y.; Kohchi, T.; !1Ohyama, K. !$#journal J. Mol. Biol. (1992) 223:1-7 !$#title Gene organization deduced from the complete sequence of !1liverwort Marchantia polymorpha mitochondrial DNA. A !1primitive form of plant mitochondrial genome. !$#cross-references MUID:92114051; PMID:1731062 !$#accession S25968 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-137 ##label ODA !'##cross-references EMBL:M68929; NID:g786182; PIDN:AAC09406.1; !1PID:g786193 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1February 1992 GENETICS !$#genome mitochondrion CLASSIFICATION #superfamily succinate dehydrogenase chain 3 KEYWORDS mitochondrion; oxidoreductase; transmembrane protein SUMMARY #length 137 #molecular-weight 16173 #checksum 4667 SEQUENCE /// ENTRY D64311 #type complete TITLE fumarate reductase (EC 1.3.99.1) - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS D64311 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession D64311 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-489 ##label BUL !'##cross-references GB:U67466; GB:L77117; NID:g1590867; !1PIDN:AAB98073.1; PID:g1498856; TIGR:MJ0092 GENETICS !$#map_position FOR86613-88082 CLASSIFICATION #superfamily Methanococcus fumarate reductase; ferredoxin !1[2Fe-2S] homology KEYWORDS 2Fe-2S; metalloprotein; oxidoreductase FEATURE !$27-69 #domain ferredoxin [2Fe-2S] homology #label FER1\ !$48,53,56,68 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 489 #molecular-weight 56128 #checksum 2284 SEQUENCE /// ENTRY E69114 #type complete TITLE fumarate reductase (EC 1.3.99.1) - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS E69114 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession E69114 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-492 ##label MTH !'##cross-references GB:AE000937; GB:AE000666; NID:g2622974; !1PIDN:AAB86316.1; PID:g2622985 !'##experimental_source strain Delta H GENETICS !$#gene MTH1850 CLASSIFICATION #superfamily Methanococcus fumarate reductase; ferredoxin !1[2Fe-2S] homology KEYWORDS 2Fe-2S; metalloprotein; oxidoreductase FEATURE !$36-78 #domain ferredoxin [2Fe-2S] homology #label FER1\ !$57,62,65,77 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 492 #molecular-weight 54780 #checksum 6620 SEQUENCE /// ENTRY S46591 #type complete TITLE fumarate reductase (EC 1.3.99.1) homolog OSM1 precursor - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES osmotic growth protein 1; protein GTB501; protein J1659; protein YJR051w ORGANISM #formal_name Saccharomyces cerevisiae DATE 13-Jan-1995 #sequence_revision 26-Jul-1996 #text_change 21-Jul-2000 ACCESSIONS S46591; JH0106; S57070; S63776 REFERENCE S46588 !$#authors Huang, M.E.; Manus, V.; Chuat, J.C.; Galibert, F. !$#journal Yeast (1994) 10:811-818 !$#title Revised nucleotide sequence of the COR region of yeast !1Saccharomyces cerevisiae chromosome X. !$#cross-references MUID:95066383; PMID:7975898 !$#accession S46591 !'##status translation not shown !'##molecule_type DNA !'##residues 1-501 ##label HUA !'##cross-references EMBL:L26347; NID:g508621; PIDN:AAA62859.1; !1PID:g695798 REFERENCE JH0104 !$#authors Melnick, L.; Sherman, F. !$#journal Gene (1990) 87:157-166 !$#title Nucleotide sequence of the COR region: a cluster of six !1genes in the yeast Saccharomyces cerevisiae. !$#cross-references MUID:90236305; PMID:2158927 !$#accession JH0106 !'##molecule_type DNA !'##residues 1-105,'FD',108-170,'R',171-190,193-281, !1'LPASLIQMTVKITGSFWLQRH' ##label MEL !'##cross-references EMBL:M37696; NID:g171257; PIDN:AAB59346.1; !1PID:g171260 REFERENCE S57052 !$#authors Huang, M.E.; Chuat, J.C.; Galibert, F. !$#submission submitted to the Protein Sequence Database, September 1995 !$#accession S57070 !'##molecule_type DNA !'##residues 1-501 ##label MAN !'##cross-references EMBL:Z49551; NID:g1015712; PIDN:CAA89579.1; !1PID:g1015713; GSPDB:GN00010; MIPS:YJR051w REFERENCE S63757 !$#authors Huang, M.E.; Chuat, J.C.; Galibert, F. !$#journal Yeast (1995) 11:775-781 !$#title Analysis of a 42.5 kb DNA sequence of chromosome X reveals !1three tRNA genes and 14 new open reading frames including a !1gene most probably belonging to the family of !1ubiquitin-protein ligases. !$#cross-references MUID:95397595; PMID:7668047 !$#accession S63776 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-501 ##label HUW !'##cross-references EMBL:L36344; NID:g1197060; PIDN:AAA88754.1; !1PID:g1197080 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1February 1996 GENETICS !$#gene SGD:OSM1; MIPS:YJR051w !'##cross-references SGD:S0003812; MIPS:YJR051w !$#map_position 10R FUNCTION !$#description may have fumarate reductase and/or succinate dehydrogenase !1activity CLASSIFICATION #superfamily osmotic growth protein 1; 3-oxosteroid !11-dehydrogenase homology; fumarate reductase flavoprotein !1homology KEYWORDS oxidoreductase FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-501 #product OSM1 protein #status predicted #label OSM\ !$26-55 #region nucleotide binding #status predicted\ !$36-324 #domain fumarate reductase flavoprotein homology !8#label FRF\ !$36-65 #region beta-alpha-beta FAD nucleotide-binding fold\ !$390-489 #domain 3-oxosteroid 1-dehydrogenase homology #label !8OXD\ !$281,304 #active_site His, Arg #status predicted SUMMARY #length 501 #molecular-weight 55065 #checksum 5607 SEQUENCE /// ENTRY S30830 #type complete TITLE fumarate reductase (EC 1.3.99.1) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YEL047c ORGANISM #formal_name Saccharomyces cerevisiae DATE 28-May-1993 #sequence_revision 26-Jul-1996 #text_change 19-Apr-2002 ACCESSIONS S30830; S50497; JC5123; PC4235 REFERENCE S30812 !$#authors Mulligan, J.T.; Dietrich, F.S.; Hennessey, K.M.; Sehl, P.; !1Komp, C.; Wei, Y.; Taylor, P.; Nakahara, K.; Roberts, D.; !1Davis, R.W. !$#submission submitted to the EMBL Data Library, February 1993 !$#accession S30830 !'##molecule_type DNA !'##residues 1-470 ##label MUL !'##cross-references GB:U18779; EMBL:L10830; NID:g603625; !1PIDN:AAB64995.1; PID:g603632 REFERENCE S50429 !$#authors Dietrich, F.S. !$#submission submitted to the EMBL Data Library, December 1994 !$#description The sequence of S. cerevisiae cosmids 8199, 8334, and 9871. !$#accession S50497 !'##molecule_type DNA !'##residues 1-470 ##label DIE !'##cross-references EMBL:U18779; NID:g603625; PIDN:AAB64995.1; !1PID:g603632; GSPDB:GN00005; MIPS:YEL047c REFERENCE JC5123 !$#authors Enomoto, K.; Ohki, R.; Muratsubaki, H. !$#journal DNA Res. (1996) 3:263-267 !$#title Cloning and sequencing of the gene encoding the soluble !1fumarate reductase from Saccharomyces cerevisiae. !$#cross-references MUID:97101648; PMID:8946166 !$#accession JC5123 !'##status preliminary !'##molecule_type DNA !'##residues 1-32,'RQ',35-284,'K',286-470 ##label ENO !$#accession PC4235 !'##status preliminary !'##molecule_type protein !'##residues 89-106;245-253;322-327;409-423 ##label EN2 GENETICS !$#gene FRDS; MIPS:YEL047c !'##cross-references SGD:S0000773 !$#map_position 5L CLASSIFICATION #superfamily osmotic growth protein 1; 3-oxosteroid !11-dehydrogenase homology; fumarate reductase flavoprotein !1homology KEYWORDS FAD; flavoprotein; oxidoreductase FEATURE !$5-292 #domain fumarate reductase flavoprotein homology !8#label FRF\ !$5-34 #region beta-alpha-beta FAD nucleotide-binding fold\ !$358-457 #domain 3-oxosteroid 1-dehydrogenase homology #label !8OXD\ !$401-448 #region AMP-binding #status predicted\ !$249,272 #active_site His, Arg #status predicted SUMMARY #length 470 #molecular-weight 50844 #checksum 999 SEQUENCE /// ENTRY B44238 #type complete TITLE fumarate reductase (EC 1.3.99.1) flavocytochrome precursor - Shewanella putrefaciens ALTERNATE_NAMES flavocytochrome c ORGANISM #formal_name Shewanella putrefaciens DATE 10-Jun-1993 #sequence_revision 26-Jul-1996 #text_change 03-Mar-2000 ACCESSIONS B44238 REFERENCE A44238 !$#authors Pealing, S.L.; Black, A.C.; Manson, F.D.; Ward, F.B.; !1Chapman, S.K.; Reid, G.A. !$#journal Biochemistry (1992) 31:12132-12140 !$#title Sequence of the gene encoding flavocytochrome c from !1Shewanella putrefaciens: a tetraheme flavoenzyme that is a !1soluble fumarate reductase related to the membrane-bound !1enzymes from other bacteria. !$#cross-references MUID:93090746; PMID:1333793 !$#accession B44238 !'##molecule_type DNA; protein !'##residues 1-596 ##label PEA !'##cross-references GB:L04283; NID:g152718; PIDN:AAA70385.1; !1PID:g152719 !'##experimental_source strain NCMB400 !'##note sequence extracted from NCBI backbone (NCBIN:119892, !1NCBIP:119894) !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing FUNCTION !$#description catalyzes the reductive hydrogenation of fumarate to !1succinate !$#pathway anaerobic respiratory chain !$#note does not catalyze the reverse (succinate dehydrogenase) !1reaction CLASSIFICATION #superfamily Shewanella fumarate reductase flavocytochrome; !13-oxosteroid 1-dehydrogenase homology; fumarate reductase !1flavoprotein homology KEYWORDS chromoprotein; electron transfer; FAD; flavoprotein; heme; !1iron; metalloprotein; monomer; oxidoreductase; periplasmic !1space FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-596 #product fumarate reductase flavocytochrome #status !8predicted #label MAT\ !$153-425 #domain fumarate reductase flavoprotein homology !8#label FRF\ !$153-181 #region beta-alpha-beta FAD nucleotide-binding fold\ !$482-581 #domain 3-oxosteroid 1-dehydrogenase homology #label !8OXD\ !$39,42 #binding_site heme (Cys) (covalent) #status !8predicted\ !$43 #binding_site heme iron (His) (axial ligand) #status !8predicted\ !$61,64 #binding_site heme (Cys) (covalent) #status !8predicted\ !$65 #binding_site heme iron (His) (axial ligand) #status !8predicted\ !$93,96 #binding_site heme (Cys) (covalent) #status !8predicted\ !$97 #binding_site heme iron (His) (axial ligand) #status !8predicted\ !$107,110 #binding_site heme (Cys) (covalent) #status !8predicted\ !$111 #binding_site heme iron (His) (axial ligand) #status !8predicted\ !$390,406 #active_site His, Arg #status predicted SUMMARY #length 596 #molecular-weight 63027 #checksum 4134 SEQUENCE /// ENTRY RDECFS #type complete TITLE fumarate reductase (EC 1.3.99.1) iron-sulfur protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 15-Oct-1982 #sequence_revision 15-Oct-1982 #text_change 01-Mar-2002 ACCESSIONS A00377; S56381; G65225 REFERENCE A00377 !$#authors Cole, S.T.; Grundstrom, T.; Jaurin, B.; Robinson, J.J.; !1Weiner, J.H. !$#journal Eur. J. Biochem. (1982) 126:211-216 !$#title Location and nucleotide sequence of frdB, the gene coding !1for the iron-sulphur protein subunit of the fumarate !1reductase of Escherichia coli. !$#cross-references MUID:83027298; PMID:6751816 !$#accession A00377 !'##molecule_type DNA !'##residues 1-244 ##label COL !'##cross-references GB:J01611; GB:J01583; NID:g145261; PIDN:AAA23438.1; !1PID:g145264 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56381 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-244 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97052.1; !1PID:g536997 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65225 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-244 ##label BLAT !'##cross-references GB:AE000487; GB:U00096; NID:g1790582; !1PIDN:AAC77113.1; PID:g1790596; UWGP:b4153 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene frdB !$#map_position 94 min COMPLEX heterotetramer (FAD linked flavoprotein, iron-sulfur !1protein, 13K and 15K membrane anchor protein) FUNCTION !$#description in E. coli, two distinct, membrane-bound, FAD-containing !1enzymes are responsible for the catalysis of fumarate and !1succinate interconversion; the fumarate reductase is used in !1anaerobic growth, and the succinate dehydrogenase is used in !1aerobic growth CLASSIFICATION #superfamily fumarate reductase iron-sulfur protein; !1ferredoxin 2[4Fe-4S] homology; ferredoxin [2Fe-2S] homology KEYWORDS 2Fe-2S; 3Fe-4S; 4Fe-4S; heterotetramer; iron-sulfur protein; !1metalloprotein; oxidoreductase FEATURE !$2-244 #product fumarate reductase iron-sulfur protein !8#status predicted #label MAT\ !$37-79 #domain ferredoxin [2Fe-2S] homology #label FER1\ !$142-223 #domain ferredoxin 2[4Fe-4S] homology #label FER2\ !$58,63,66,78 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8experimental\ !$149,152,155,215 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$159,205,211 #binding_site 3Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 244 #molecular-weight 27123 #checksum 1006 SEQUENCE /// ENTRY RDEBIV #type complete TITLE fumarate reductase (EC 1.3.99.1) iron-sulfur protein - Proteus vulgaris ALTERNATE_NAMES fumarate reductase chain B; succinate dehydrogenase iron-sulfur protein ORGANISM #formal_name Proteus vulgaris DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 11-Jun-1999 ACCESSIONS S00108 REFERENCE S00107 !$#authors Cole, S.T. !$#journal Eur. J. Biochem. (1987) 167:481-488 !$#title Nucleotide sequence and comparative analysis of the frd !1operon encoding the fumarate reductase of Proteus vulgaris. !1Extensive sequence divergence of the membrane anchors and !1absence of an frd-linked ampC cephalosporinase gene. !$#cross-references MUID:88004470; PMID:3308458 !$#accession S00108 !'##molecule_type DNA !'##residues 1-245 ##label COL !'##cross-references EMBL:X06144; NID:g45917; PIDN:CAA29502.1; !1PID:g45919 GENETICS !$#gene frdB CLASSIFICATION #superfamily fumarate reductase iron-sulfur protein; !1ferredoxin 2[4Fe-4S] homology; ferredoxin [2Fe-2S] homology KEYWORDS 2Fe-2S; 3Fe-4S; 4Fe-4S; heterotetramer; iron-sulfur protein; !1metalloprotein; oxidoreductase FEATURE !$38-80 #domain ferredoxin [2Fe-2S] homology #label FER1\ !$143-224 #domain ferredoxin 2[4Fe-4S] homology #label FER2\ !$59,64,67,79 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted\ !$150,153,156,216 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$160,206,212 #binding_site 3Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 245 #molecular-weight 27331 #checksum 2754 SEQUENCE /// ENTRY S26978 #type complete TITLE succinate dehydrogenase (ubiquinone) (EC 1.3.5.1) iron-sulfur protein precursor - smut fungus (Ustilago maydis) ORGANISM #formal_name Ustilago maydis #common_name corn smut DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 11-Jun-1999 ACCESSIONS S26978; S32824 REFERENCE S26978 !$#authors Broomfield, P.L.E.; Hargreaves, J.A. !$#journal Curr. Genet. (1992) 22:117-121 !$#title A single amino acid change in the iron-sulphur protein !1subunit of succinate dehydrogenase confers resistance to !1carboxin in Ustilago maydis. !$#cross-references MUID:93046793; PMID:1423716 !$#accession S26978 !'##molecule_type DNA !'##residues 1-295 ##label BRO !'##cross-references EMBL:Z11738; NID:g5230; PIDN:CAA77798.1; PID:g5231 !'##note the authors translated the codon AAG for residue 56 as Leu and !1GAG for residue 288 as Gln REFERENCE S32824 !$#authors Keon, J.P.R.; White, G.A.; Hargreaves, J.A. !$#journal Curr. Genet. (1991) 19:475-481 !$#title Isolation, characterization and sequence of a gene !1conferring resistance to the systemic fungicide carboxin !1from the maize smut pathogen, Ustilago maydis. !$#cross-references MUID:91347409; PMID:1879000 !$#accession S32824 !'##molecule_type DNA !'##residues 1-252,'L',254-295 ##label KEO !'##cross-references EMBL:X62762; NID:g5216; PIDN:CAA44612.1; PID:g5217 FUNCTION !$#description catalyzes the oxidation/reduction reaction of succinate and !1ubiquinone to fumarate and ubiquinol CLASSIFICATION #superfamily fumarate reductase iron-sulfur protein; !1ferredoxin 2[4Fe-4S] homology; ferredoxin [2Fe-2S] homology KEYWORDS 2Fe-2S; 3Fe-4S; 4Fe-4S; heterotetramer; iron-sulfur protein; !1metalloprotein; mitochondrion; oxidoreductase; tricarboxylic !1acid cycle FEATURE !$85-127 #domain ferredoxin [2Fe-2S] homology #label FER1\ !$188-270 #domain ferredoxin 2[4Fe-4S] homology #label FER2\ !$106,111,114,126 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted\ !$195,198,201,262 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$205,252,258 #binding_site 3Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 295 #molecular-weight 33282 #checksum 6403 SEQUENCE /// ENTRY RDBYIS #type complete TITLE succinate dehydrogenase (ubiquinone) (EC 1.3.5.1) iron-sulfur protein precursor - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein L0745; protein YLL041c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 21-Jul-2000 ACCESSIONS A35435; F32394; S64793; S11164 REFERENCE A35435 !$#authors Lombardo, A.; Carine, K.; Scheffler, I.E. !$#journal J. Biol. Chem. (1990) 265:10419-10423 !$#title Cloning and characterization of the iron-sulfur subunit gene !1of succinate dehydrogenase from Saccharomyces cerevisiae. !$#cross-references MUID:90285165; PMID:2191948 !$#accession A35435 !'##molecule_type DNA !'##residues 1-266 ##label LOM !'##cross-references EMBL:J05487; NID:g172548; PIDN:AAA35021.1; !1PID:g172549 REFERENCE A32394 !$#authors Gould, S.J.; Subramani, S.; Scheffler, I.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:1934-1938 !$#title Use of the DNA polymerase chain reaction for homology !1probing: isolation of partial cDNA or genomic clones !1encoding the iron-sulfur protein of succinate dehydrogenase !1from several species. !$#cross-references MUID:89184541; PMID:2494655 !$#accession F32394 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type DNA !'##residues 101-242 ##label GOU REFERENCE S64792 !$#authors Wedler, H.; Wedler, E.; Scharfe, M.; Wambutt, R. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64793 !'##molecule_type DNA !'##residues 1-266 ##label WED !'##cross-references EMBL:Z73146; NID:g1360234; PIDN:CAA97492.1; !1PID:g1360235; GSPDB:GN00012; MIPS:YLL041c !'##note experimental_source strain S288C GENETICS !$#gene SGD:SDH2; MIPS:YLL041c !'##cross-references SGD:S0003964; MIPS:YLL041c !$#map_position 12L !$#genome nuclear FUNCTION !$#description catalyzes the oxidation/reduction reaction of succinate and !1ubiquinone to fumarate and ubiquinol CLASSIFICATION #superfamily fumarate reductase iron-sulfur protein; !1ferredoxin 2[4Fe-4S] homology; ferredoxin [2Fe-2S] homology KEYWORDS 2Fe-2S; 3Fe-4S; 4Fe-4S; iron-sulfur protein; metalloprotein; !1mitochondrion; oxidoreductase; tricarboxylic acid cycle FEATURE !$1-20 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$21-266 #product succinate dehydrogenase (ubiquinone) !8iron-sulfur protein #status predicted #label MAT\ !$66-108 #domain ferredoxin [2Fe-2S] homology #label FER1\ !$172-254 #domain ferredoxin 2[4Fe-4S] homology #label FER2\ !$87,92,95,107 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted\ !$179,182,185,246 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$189,236,242 #binding_site 3Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 266 #molecular-weight 30231 #checksum 2329 SEQUENCE /// ENTRY DEECSI #type complete TITLE succinate dehydrogenase (EC 1.3.99.1) iron-sulfur protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 01-Mar-2002 ACCESSIONS A28837; C64808 REFERENCE A28837 !$#authors Darlison, M.G.; Guest, J.R. !$#journal Biochem. J. (1984) 223:507-517 !$#title Nucleotide sequence encoding the iron-sulphur protein !1subunit of the succinate dehydrogenase of Escherichia coli. !$#cross-references MUID:85046453; PMID:6388571 !$#accession A28837 !'##molecule_type DNA !'##residues 1-238 ##label DAR !'##cross-references GB:X01070; NID:g42926; PIDN:CAA25534.1; PID:g42928 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64808 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-238 ##label BLAT !'##cross-references GB:AE000175; GB:U00096; NID:g1786934; !1PIDN:AAC73818.1; PID:g1786943; UWGP:b0724 !'##experimental_source strain K-12, substrain MG1655 COMMENT In E. coli, two distinct, membrane-bound, FAD-containing !1enzymes are responsible for the catalysis of fumarate and !1succinate interconversion; fumarate reductase is used in !1anaerobic growth and succinate dehydrogenase in aerobic !1growth. The protein shown, which contains iron-sulfur !1centers, is one of two catalytic components of the !1functional succinate dehydrogenase; the other component is a !1flavoprotein also containing iron-sulfur centers. GENETICS !$#gene sdhB !$#map_position 17 min CLASSIFICATION #superfamily fumarate reductase iron-sulfur protein; !1ferredoxin 2[4Fe-4S] homology; ferredoxin [2Fe-2S] homology KEYWORDS 2Fe-2S; 3Fe-4S; 4Fe-4S; iron-sulfur protein; metalloprotein; !1oxidoreductase; tricarboxylic acid cycle FEATURE !$35-76 #domain ferredoxin [2Fe-2S] homology #label FER1\ !$142-224 #domain ferredoxin 2[4Fe-4S] homology #label FER2\ !$55,60,75 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted\ !$149,152,155,216 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$159,206,212 #binding_site 3Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 238 #molecular-weight 26770 #checksum 6209 SEQUENCE /// ENTRY C44954 #type complete TITLE fumarate reductase (EC 1.3.99.1) iron-sulfur protein - Wolinella succinogenes ALTERNATE_NAMES fumarate reductase chain B ORGANISM #formal_name Wolinella succinogenes DATE 03-Jun-1993 #sequence_revision 19-Jul-1996 #text_change 11-Jun-1999 ACCESSIONS C44954; S10166 REFERENCE A44954 !$#authors Lauterbach, F.; Koertner, C.; Albracht, S.P.J.; Unden, G.; !1Kroeger, A. !$#journal Arch. Microbiol. (1990) 154:386-393 !$#title The fumarate reductase operon of Wolinella succinogenes. !1Sequence and expression of the frdA and frdB genes. !$#cross-references MUID:91058386; PMID:2244791 !$#accession C44954 !'##status preliminary !'##molecule_type DNA !'##residues 1-239 ##label LAU !'##cross-references GB:X51509; NID:g48511; PIDN:CAA35876.1; PID:g48514 REFERENCE S10164 !$#authors Koertner, C.; Lauterbach, F.; Tripier, D.; Unden, G.; !1Kroeger, A. !$#journal Mol. Microbiol. (1990) 4:855-860 !$#title Wolinella succinogenes fumarate reductase contains a dihaem !1cytochrome b. !$#cross-references MUID:90355847; PMID:2388563 !$#accession S10166 !'##status preliminary; translation not shown !'##molecule_type DNA !'##residues 1-239 ##label KOE !'##cross-references EMBL:X51509; NID:g48511; PIDN:CAA35876.1; !1PID:g48514 GENETICS !$#gene frdB COMPLEX part of an enzyme complex containing a heterotrimer !1(flavoprotein, iron-sulfer protein and a cytochrome B) FUNCTION !$#description catalyzes the oxidation of succinate to fumarate and !1transfers its reducing equivalents to ubiquinone; it is the !1site of succinate-fumarate conversion and forms the !1catalytic portion of the complex together with the iron !1sulfur subunit CLASSIFICATION #superfamily fumarate reductase iron-sulfur protein; !1ferredoxin 2[4Fe-4S] homology; ferredoxin [2Fe-2S] homology KEYWORDS 2Fe-2S; 3Fe-4S; 4Fe-4S; heterotetramer; iron-sulfur protein; !1metalloprotein; oxidoreductase FEATURE !$38-78 #domain ferredoxin [2Fe-2S] homology #label FER1\ !$144-226 #domain ferredoxin 2[4Fe-4S] homology #label FER2\ !$57,62,65,77 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted\ !$151,154,157,218 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$161,208,214 #binding_site 3Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 239 #molecular-weight 27165 #checksum 684 SEQUENCE /// ENTRY T50537 #type complete TITLE succinate dehydrogenase (EC 1.3.99.1) chain B [validated] - Acidianus ambivalens ALTERNATE_NAMES succinate dehydrogenase / fumarate reductase iron-sulfur protein ORGANISM #formal_name Acidianus ambivalens DATE 15-Jun-2001 #sequence_revision 15-Jun-2001 #text_change 15-Jun-2001 ACCESSIONS T50537 REFERENCE Z25105 !$#authors Gomes, C.M.; Lemos, R.S.; Teixeira, M.; Kletzin, A.; Huber, !1H.; Stetter, K.O.; Schaefer, G.; Anemueller, S. !$#journal Biochim. Biophys. Acta (1999) 1411:134-141 !$#title The unusual iron sulfur composition of the Acidianus !1ambivalens succinate dehydrogenase complex. !$#cross-references PMID:10216159 !$#accession T50537 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-314 ##label GOM !'##cross-references EMBL:AJ005961; PIDN:CAA06781.1 !'##experimental_source isolate Lei 10 COMMENT This succinate dehydrogenase has one 2Fe-2S center and two !14Fe-4S centers. GENETICS !$#gene sdhB FUNCTION !$#description EC 1.3.99.1 [validated, MUID:99233616]; catalyzes the !1oxidation/reduction reaction of succinate and ubiquinone to !1fumarate and ubiquinol CLASSIFICATION #superfamily fumarate reductase iron-sulfur protein; !1ferredoxin 2[4Fe-4S] homology; ferredoxin [2Fe-2S] homology KEYWORDS 2Fe-2S; 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein; membrane-associated complex; oxidoreductase FEATURE !$39-78 #domain ferredoxin [2Fe-2S] homology #label FDX\ !$57,62,65,77 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted\ !$152-226 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$154,157,160,218 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$164,208,211,214 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 314 #molecular-weight 36378 #checksum 1052 SEQUENCE /// ENTRY G90406 #type complete TITLE succinate dehydrogenase (EC 1.3.99.1) chain B [similarity] - Sulfolobus solfataricus ALTERNATE_NAMES succinate dehydrogenase / fumarate reductase iron-sulfur protein ORGANISM #formal_name Sulfolobus solfataricus DATE 15-Jun-2001 #sequence_revision 15-Jun-2001 #text_change 30-Jun-2001 ACCESSIONS G90406 REFERENCE A99139 !$#authors She, Q.; Singh, R.K.; Confalonieri, F.; Zivanovic, Y.; !1Allard, G.; Awayez, M.J.; Chan-Weiher, C.C.Y.; Clausen, !1I.G.; Curtis, B.A.; De Moors, A.; Erauso, G.; Fletcher, C.; !1Gordon, P.M.K.; Heikamp-de Jong, I.; Jeffries, A.C.; Kozera, !1C.J.; Medina, N.; Peng, X.; Thi-Ngoc, H.P.; Redder, P.; !1Schenk, M.E.; Theriault, C.; Tolstrup, N.; Charlebois, R.L.; !1Doolittle, W.F.; Duguet, M.; Gaasterland, T.; Garrett, R.A.; !1Ragan, M.A.; Sensen, C.W.; Van der Oost, J. !$#submission submitted to GenBank, April 2001 !$#description Sulfolobus solfataricus complete genome. !$#accession G90406 !'##status preliminary !'##molecule_type DNA !'##residues 1-316 ##label KUR !'##cross-references GB:AE006641; NID:g13815660; PIDN:AAK42510.1; !1GSPDB:GN00155 GENETICS !$#gene sdhB CLASSIFICATION #superfamily fumarate reductase iron-sulfur protein; !1ferredoxin 2[4Fe-4S] homology; ferredoxin [2Fe-2S] homology KEYWORDS 2Fe-2S; 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein; membrane-associated complex; oxidoreductase FEATURE !$58,63,66,78 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 316 #molecular-weight 36792 #checksum 8153 SEQUENCE /// ENTRY T45163 #type complete TITLE succinate dehydrogenase (EC 1.3.99.1) chain B [validated] - Sulfolobus acidocaldarius ALTERNATE_NAMES succinate dehydrogenase iron-sulfur protein ORGANISM #formal_name Sulfolobus acidocaldarius DATE 15-Jun-2001 #sequence_revision 15-Jun-2001 #text_change 15-Jun-2001 ACCESSIONS T45163 REFERENCE Z22936 !$#authors Janssen, S.; Schaefer, G.; Anemueller, S.; Moll, R. !$#journal J. Bacteriol. (1997) 179:5560-5569 !$#title A succinate dehydrogenase with novel structure and !1properties from the hyperthermophilic archaeon Sulfolobus !1acidocaldarius: genetic and biophysical characterization. !$#cross-references MUID:97431508; PMID:9287013 !$#accession T45163 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-317 ##label JAN !'##cross-references EMBL:Y09041; PIDN:CAA70250.1 !'##experimental_source DSM 639 COMMENT This succinate dehydrogenase has one 2Fe-2S center and two !14Fe-4S centers. GENETICS !$#gene sdhB FUNCTION !$#description EC 1.3.99.1 [validated, PMID:1935955]; catalyzes the !1oxidative dehydrogenation of succinate to fumarate CLASSIFICATION #superfamily fumarate reductase iron-sulfur protein; !1ferredoxin 2[4Fe-4S] homology; ferredoxin [2Fe-2S] homology KEYWORDS 2Fe-2S; 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein; membrane-associated complex; oxidoreductase FEATURE !$41-80 #domain ferredoxin [2Fe-2S] homology #label FDX\ !$59,64,67,79 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted\ !$154-228 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$156,159,162,220 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$166,210,213,216 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 317 #molecular-weight 36470 #checksum 1841 SEQUENCE /// ENTRY S10164 #type complete TITLE fumarate reductase (EC 1.3.99.1) cytochrome b component - Wolinella succinogenes ALTERNATE_NAMES fumarate reductase chain C ORGANISM #formal_name Wolinella succinogenes DATE 21-Nov-1993 #sequence_revision 19-Jul-1996 #text_change 11-Jun-1999 ACCESSIONS S10164; A44954 REFERENCE S10164 !$#authors Koertner, C.; Lauterbach, F.; Tripier, D.; Unden, G.; !1Kroeger, A. !$#journal Mol. Microbiol. (1990) 4:855-860 !$#title Wolinella succinogenes fumarate reductase contains a dihaem !1cytochrome b. !$#cross-references MUID:90355847; PMID:2388563 !$#accession S10164 !'##status preliminary; translation not shown !'##molecule_type DNA !'##residues 1-256 ##label KOE !'##cross-references EMBL:X51509; NID:g48511; PIDN:CAA35874.1; !1PID:g48512 REFERENCE A44954 !$#authors Lauterbach, F.; Koertner, C.; Albracht, S.P.J.; Unden, G.; !1Kroeger, A. !$#journal Arch. Microbiol. (1990) 154:386-393 !$#title The fumarate reductase operon of Wolinella succinogenes. !1Sequence and expression of the frdA and frdB genes. !$#cross-references MUID:91058386; PMID:2244791 !$#accession A44954 !'##status preliminary !'##molecule_type DNA !'##residues 205-256 ##label LAU !'##cross-references GB:X51509 GENETICS !$#gene frdC COMPLEX part of an enzyme complex containing a heterotrimer !1(flavoprotein, iron-sulfer protein and a cytochrome b) FUNCTION !$#description catalyzes the oxidation of succinate to fumarate and !1transfers its reducing equivalents to ubiquinone; it is the !1site of succinate-fumarate conversion and forms the !1catalytic portion of the complex together with the iron !1sulfur subunit CLASSIFICATION #superfamily fumarate reductase cytochrome b KEYWORDS oxidoreductase; transmembrane protein; tricarboxylic acid !1cycle SUMMARY #length 256 #molecular-weight 29723 #checksum 8740 SEQUENCE /// ENTRY DEECS4 #type complete TITLE succinate dehydrogenase (EC 1.3.99.1) cytochrome b556 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 01-Mar-2002 ACCESSIONS A28836; I84546; H64807 REFERENCE A94642 !$#authors Wood, D.; Darlison, M.G.; Wilde, R.J.; Guest, J.R. !$#journal Biochem. J. (1984) 222:519-534 !$#title Nucleotide sequence encoding the flavoprotein and !1hydrophobic subunits of the succinate dehydrogenase of !1Escherichia coli. !$#cross-references MUID:84307466; PMID:6383359 !$#accession A28836 !'##molecule_type DNA !'##residues 1-129 ##label WOO !'##cross-references GB:X00980; NID:g42921; PIDN:CAA25485.1; PID:g42923 REFERENCE I41112 !$#authors Wilde, R.J.; Guest, J.R. !$#journal J. Gen. Microbiol. (1986) 132:3239-3251 !$#title Transcript analysis of the citrate synthase and succinate !1dehydrogenase genes of Escherichia coli k-12. !$#cross-references MUID:88009821; PMID:3309132 !$#accession I84546 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-129 ##label RES !'##cross-references GB:M28989; NID:g342042; PIDN:AAA24616.1; !1PID:g495784 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64807 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-129 ##label BLAT !'##cross-references GB:AE000175; GB:U00096; NID:g1786934; !1PIDN:AAC73815.1; PID:g1786940; UWGP:b0721 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene sdhC; cybA !$#map_position 17 min COMPLEX one of two hydrophobic anchor components of the succinate !1dehydrogenase complex FUNCTION !$#pathway tricarboxylic acid cycle CLASSIFICATION #superfamily succinate dehydrogenase 14K hydrophobic protein KEYWORDS heme; oxidoreductase; transmembrane protein; tricarboxylic !1acid cycle FEATURE !$32-48 #domain transmembrane #status predicted #label TM1\ !$73-89 #domain transmembrane #status predicted #label TM2\ !$112-128 #domain transmembrane #status predicted #label TM3 SUMMARY #length 129 #molecular-weight 14299 #checksum 1478 SEQUENCE /// ENTRY WMEC13 #type complete TITLE fumarate reductase (EC 1.3.99.1) 13K membrane anchor protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 15-Oct-1982 #sequence_revision 15-Oct-1982 #text_change 01-Mar-2002 ACCESSIONS A04431; S56379; B21197; I41130; E65225 REFERENCE A04431 !$#authors Grundstrom, T.; Jaurin, B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:1111-1115 !$#title Overlap between ampC and frd operons on the Escherichia coli !1chromosome. !$#cross-references MUID:82174546; PMID:7041115 !$#accession A04431 !'##molecule_type DNA !'##residues 1-119 ##label GRU !'##cross-references GB:V00277; NID:g41482; PIDN:CAA23536.1; PID:g41484 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56379 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-119 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97050.1; !1PID:g536995 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A21197 !$#authors Olsson, O.; Bergstroem, S.; Lindberg, F.P.; Normark, S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:7556-7560 !$#title ampC beta-lactamase hyperproduction in Escherichia coli: !1natural ampicillin resistance generated by horizontal !1chromosomal DNA transfer from Shigella. !$#cross-references MUID:84170267; PMID:6369321 !$#accession B21197 !'##status preliminary !'##molecule_type DNA !'##residues 82-119 ##label OLS REFERENCE I41130 !$#authors Jones, H.M.; Gunsalus, R.P. !$#journal J. Bacteriol. (1985) 164:1100-1109 !$#title Transcription of the Escherichia coli fumarate reductase !1genes (frdABCD) and their coordinate regulation by oxygen, !1nitrate, and fumarate. !$#cross-references MUID:86059201; PMID:2999070 !$#accession I41130 !'##status preliminary !'##molecule_type DNA !'##residues 109-119 ##label RES !'##cross-references GB:M11979; NID:g145255; PIDN:AAA23434.1; !1PID:g145257 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65225 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-119 ##label BLAT !'##cross-references GB:AE000487; GB:U00096; NID:g1790582; !1PIDN:AAC77111.1; PID:g1790594; UWGP:b4151 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene frdD !$#map_position 94 min COMPLEX heterotetramer (FAD linked flavoprotein, iron-sulfur !1protein, 13K and 15K membrane anchor protein) FUNCTION !$#description in E. coli, two distinct, membrane-bound, FAD-containing !1enzymes are responsible for the catalysis of fumarate and !1succinate interconversion; the fumarate reductase is used in !1anaerobic growth, and the succinate dehydrogenase is used in !1aerobic growth CLASSIFICATION #superfamily fumarate reductase 13K protein KEYWORDS heterotetramer; membrane protein; oxidoreductase FEATURE !$13-40 #domain transmembrane #status predicted #label TM1\ !$55-80 #domain transmembrane #status predicted #label TM2\ !$99-119 #domain transmembrane #status predicted #label TM3\ !$81 #active_site His #status predicted SUMMARY #length 119 #molecular-weight 13107 #checksum 2068 SEQUENCE /// ENTRY RDEB13 #type complete TITLE fumarate reductase (EC 1.3.99.1) 13K protein - Proteus vulgaris ALTERNATE_NAMES fumarate reductase chain D; succinate dehydrogenase 13K protein ORGANISM #formal_name Proteus vulgaris DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 09-Sep-1994 ACCESSIONS S00110 REFERENCE S00107 !$#authors Cole, S.T. !$#journal Eur. J. Biochem. (1987) 167:481-488 !$#title Nucleotide sequence and comparative analysis of the frd !1operon encoding the fumarate reductase of Proteus vulgaris. !1Extensive sequence divergence of the membrane anchors and !1absence of an frd-linked ampC cephalosporinase gene. !$#cross-references MUID:88004470; PMID:3308458 !$#accession S00110 !'##molecule_type DNA !'##residues 1-119 ##label COL !'##cross-references EMBL:X06144 COMMENT Succinate dehydrogenase consists of four subunits: the !1flavoprotein, the iron-sulfur protein, the 15K protein, and !1the 13K protein. GENETICS !$#gene frdD CLASSIFICATION #superfamily fumarate reductase 13K protein KEYWORDS heterotetramer; oxidoreductase; transmembrane protein FEATURE !$27-47 #domain transmembrane #status predicted #label TM1\ !$55-81 #domain transmembrane #status predicted #label TM2\ !$99-119 #domain transmembrane #status predicted #label TM3\ !$81 #active_site His #status predicted SUMMARY #length 119 #molecular-weight 13201 #checksum 8812 SEQUENCE /// ENTRY E64097 #type complete TITLE fumarate reductase (EC 1.3.99.1) 13K protein - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS E64097 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession E64097 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-114 ##label TIGR !'##cross-references GB:U32765; GB:L42023; NID:g1573838; !1PIDN:AAC22490.1; PID:g1573846; TIGR:HI0832 CLASSIFICATION #superfamily fumarate reductase 13K protein KEYWORDS oxidoreductase; transmembrane protein FEATURE !$26-46 #domain transmembrane #status predicted #label TM1\ !$94-114 #domain transmembrane #status predicted #label TM3\ !$76 #active_site His #status predicted SUMMARY #length 114 #molecular-weight 12636 #checksum 3528 SEQUENCE /// ENTRY RDEB15 #type complete TITLE fumarate reductase (EC 1.3.99.1) 15K protein - Proteus vulgaris ALTERNATE_NAMES fumarate reductase chain C; succinate dehydrogenase 15K protein ORGANISM #formal_name Proteus vulgaris DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 09-Sep-1994 ACCESSIONS S00109 REFERENCE S00107 !$#authors Cole, S.T. !$#journal Eur. J. Biochem. (1987) 167:481-488 !$#title Nucleotide sequence and comparative analysis of the frd !1operon encoding the fumarate reductase of Proteus vulgaris. !1Extensive sequence divergence of the membrane anchors and !1absence of an frd-linked ampC cephalosporinase gene. !$#cross-references MUID:88004470; PMID:3308458 !$#accession S00109 !'##molecule_type DNA !'##residues 1-131 ##label COL !'##cross-references EMBL:X06144 GENETICS !$#gene frdC CLASSIFICATION #superfamily fumarate reductase 15K protein KEYWORDS heterotetramer; oxidoreductase; transmembrane protein FEATURE !$31-50 #domain transmembrane #status predicted #label TM1\ !$68-87 #domain transmembrane #status predicted #label TM2\ !$112-131 #domain transmembrane #status predicted #label TM3\ !$83 #active_site His #status predicted SUMMARY #length 131 #molecular-weight 14822 #checksum 7437 SEQUENCE /// ENTRY A47011 #type complete TITLE glycine reductase (EC 1.4.99.-) selenoprotein A - Clostridium sticklandii ALTERNATE_NAMES glycine reductase selenocysteine-containing protein ORGANISM #formal_name Clostridium sticklandii DATE 21-Sep-1993 #sequence_revision 08-Nov-1996 #text_change 11-Jun-1999 ACCESSIONS A47011; A28115 REFERENCE A47011 !$#authors Garcia, G.E.; Stadtman, T.C. !$#journal J. Bacteriol. (1992) 174:7080-7089 !$#title Clostridium sticklandii glycine reductase selenoprotein A !1gene: cloning, sequencing, and expression in Escherichia !1coli. !$#cross-references MUID:93054316; PMID:1429431 !$#accession A47011 !'##molecule_type DNA !'##residues 1-158 ##label GAR !'##cross-references GB:M60399; NID:g144821; PIDN:AAB02347.1; !1PID:g1374788 !'##note sequence extracted from NCBI backbone (NCBIN:117995, !1NCBIP:117996) !'##note in Genbank entry CLOGRDA, release 106.0, PID:g1374788 the !1selenocysteine UGA codon for residue 44 is translated as 'X' REFERENCE A28115 !$#authors Sliwkowski, M.X.; Stadtman, T.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:368-371 !$#title Selenoprotein A of the clostridial glycine reductase !1complex: purification and amino acid sequence of the !1selenocysteine-containing peptide. !$#cross-references MUID:88124843; PMID:2963330 !$#accession A28115 !'##molecule_type protein !'##residues 41-54,'E',56 ##label SLI GENETICS !$#gene grdA FUNCTION !$#description glycine reductase complex catalyzes the reductive !1deamination of glycine to acetic acid and ammonia coupled to !1the formation of ATP from ADP and phosphate CLASSIFICATION #superfamily glycine reductase complex selenoprotein A KEYWORDS ATP; blocked amino end; glycoprotein; oxidoreductase; !1selenocysteine FEATURE !$44 #modified_site selenocysteine #status experimental SUMMARY #length 158 #molecular-weight 17093 #checksum 9092 SEQUENCE /// ENTRY A38540 #type complete TITLE glycine reductase (EC 1.4.99.-) selenoprotein A - Clostridium purinolyticum ORGANISM #formal_name Clostridium purinolyticum DATE 31-Jul-1991 #sequence_revision 08-Nov-1996 #text_change 11-Jun-1999 ACCESSIONS A38540 REFERENCE A38540 !$#authors Garcia, G.E.; Stadtman, T.C. !$#journal J. Bacteriol. (1991) 173:2093-2098 !$#title Selenoprotein A component of the glycine reductase complex !1from Clostridium purinolyticum: nucleotide sequence of the !1gene shows that selenocysteine is encoded by UGA. !$#cross-references MUID:91161528; PMID:1825826 !$#accession A38540 !'##molecule_type DNA !'##residues 1-150 ##label GAR !'##cross-references GB:M64374; GB:M55254; NID:g144823; PIDN:AAB02121.1; !1PID:g144824 !'##note in Genbank entry CLOGRDA1, release 106.0, PID:g144824 the !1selenocysteine UGA codon for residue 43 is translated as 'X' GENETICS !$#gene grdA FUNCTION !$#description glycine reductase complex catalyzes the reductive !1deamination of glycine to acetic acid and ammonia coupled to !1the formation of ATP from ADP and phosphate CLASSIFICATION #superfamily glycine reductase complex selenoprotein A KEYWORDS ATP; oxidoreductase; selenocysteine FEATURE !$43 #modified_site selenocysteine #status predicted SUMMARY #length 150 #molecular-weight 15715 #checksum 8069 SEQUENCE /// ENTRY S38990 #type complete TITLE glycine reductase (EC 1.4.99.-) selenoprotein A - Eubacterium acidaminophilum ORGANISM #formal_name Eubacterium acidaminophilum DATE 07-Oct-1994 #sequence_revision 08-Nov-1996 #text_change 11-Jun-1999 ACCESSIONS S38990; B38157 REFERENCE S38988 !$#authors Luebbers, M.; Andreesen, J.R. !$#journal Eur. J. Biochem. (1993) 217:791-798 !$#title Components of glycine reductase from Eubacterium !1acidaminophilum. Cloning, sequencing and identification of !1the genes for thioredoxin reductase, thioredoxin and !1selenoprotein P(A). !$#cross-references MUID:94039119; PMID:8223622 !$#accession S38990 !'##molecule_type DNA !'##residues 1-158 ##label LUE !'##cross-references GB:L04500; NID:g2708733; PIDN:AAB93305.1; !1PID:g388296 !'##note in Genbank entry EUBTHIORED, release 106.0, PID:g388296 the !1selenocysteine UGA codon for residue 44 is translated as 'X' REFERENCE A38157 !$#authors Dietrichs, D.; Meyer, M.; Rieth, M.; Andreesen, J.R. !$#journal J. Bacteriol. (1991) 173:5983-5991 !$#title Interaction of selenoprotein P-A and the thioredoxin system, !1components of the NADPH-dependent reduction of glycine in !1Eubacterium acidaminophilum and Clostridium litoralis. !$#cross-references MUID:92011354; PMID:1917832 !$#accession B38157 !'##molecule_type protein !'##residues 2-25,'X',27-40,'X',42-43,'XD',46,'XLF' ##label DIE GENETICS !$#gene grdA FUNCTION !$#description glycine reductase complex catalyzes the reductive !1deamination of glycine to acetic acid and ammonia coupled to !1the formation of ATP from ADP and phosphate CLASSIFICATION #superfamily glycine reductase complex selenoprotein A KEYWORDS ATP; oxidoreductase; selenocysteine FEATURE !$44 #modified_site selenocysteine #status experimental SUMMARY #length 158 #molecular-weight 16609 #checksum 9227 SEQUENCE /// ENTRY DEHUCM #type complete TITLE acyl-CoA dehydrogenase (EC 1.3.99.3) precursor, medium-chain-specific, mitochondrial [validated] - human ALTERNATE_NAMES acyl dehydrogenase, medium-chain-specific ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 01-Dec-2000 ACCESSIONS A29031; I52240 REFERENCE A29031 !$#authors Kelly, D.P.; Kim, J.J.; Billadello, J.J.; Hainline, B.E.; !1Chu, T.W.; Strauss, A.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:4068-4072 !$#title Nucleotide sequence of medium-chain acyl-CoA dehydrogenase !1mRNA and its expression in enzyme-deficient human tissue. !$#cross-references MUID:87231952; PMID:3035565 !$#accession A29031 !'##molecule_type mRNA !'##residues 1-421 ##label KEL !'##cross-references GB:M16827; GB:J05355; NID:g177963; PIDN:AAA51566.1; !1PID:g177964 REFERENCE I52240 !$#authors Matsubara, Y.; Narisawa, K.; Miyabayashi, S.; Tada, K.; !1Coates, P.M.; Bachmann, C.; Elsas, L.J. !$#journal Biochem. Biophys. Res. Commun. (1990) 171:498-505 !$#title Identification of a common mutation in patients with !1medium-chain acyl-CoA dehydrogenase deficiency. !$#cross-references MUID:90365752; PMID:2393404 !$#accession I52240 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 314-342 ##label RES !'##cross-references GB:M60505; NID:g187418; PIDN:AAB59625.1; !1PID:g553529 COMMENT Three straight-chain acyl-CoA dehydrogenases of different !1substrate specificities are present in mammalian tissues. GENETICS !$#gene GDB:ACADM !'##cross-references GDB:118958; OMIM:201450 !$#map_position 1p31-1p31 FUNCTION !$#description EC 1.3.99.3 [validated, MUID:90365752]; catalyzes the 1, !12-oxidation of acyl-CoA thioester with formation of !1trans-2-enoyl-CoA !$#pathway fatty acid beta-oxidation !$#note specific for acyl chain lengths of 4 to 16 !$#note medium-chain acyl-CoA dehydrogenase deficiency is one of the !1most common recessively inherited metabolic diseases in man CLASSIFICATION #superfamily acyl-CoA dehydrogenase KEYWORDS fatty acid beta-oxidation; fatty acid metabolism; !1flavoprotein; mitochondrion; oxidoreductase FEATURE !$1-25 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$26-421 #product acyl-CoA dehydrogenase, !8medium-chain-specific #status predicted #label MAT SUMMARY #length 421 #molecular-weight 46588 #checksum 8165 SEQUENCE /// ENTRY DERTCM #type complete TITLE acyl-CoA dehydrogenase (EC 1.3.99.3) precursor, medium-chain-specific, mitochondrial - rat ALTERNATE_NAMES acyl dehydrogenase, medium-chain-specific ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 01-Dec-2000 ACCESSIONS A28436; S15128 REFERENCE A28436 !$#authors Matsubara, Y.; Kraus, J.P.; Ozasa, H.; Glassberg, R.; !1Finocchiaro, G.; Ikeda, Y.; Mole, J.; Rosenberg, L.E.; !1Tanaka, K. !$#journal J. Biol. Chem. (1987) 262:10104-10108 !$#title Molecular cloning and nucleotide sequence of cDNA encoding !1the entire precursor of rat liver medium chain acyl coenzyme !1A dehydrogenase. !$#cross-references MUID:87280028; PMID:3611054 !$#accession A28436 !'##molecule_type mRNA !'##residues 1-421 ##label RF1 !'##cross-references GB:J02791; NID:g202688; PIDN:AAA40670.1; !1PID:g202689 REFERENCE S15128 !$#authors Inagaki, T.; Ohishi, N.; Tsukagoshi, N.; Udaka, S.; Ghisla, !1S.; Yagi, K. !$#journal Biochim. Biophys. Acta (1991) 1077:285-290 !$#title Structurally different rat liver medium-chain acyl CoA !1dehydrogenases directed by complementary DNAs differing in !1their 5'-region. !$#cross-references MUID:91230137; PMID:2029527 !$#accession S15128 !'##status preliminary !'##molecule_type protein !'##residues 11-81 ##label BIO CLASSIFICATION #superfamily acyl-CoA dehydrogenase KEYWORDS fatty acid beta-oxidation; fatty acid metabolism; !1flavoprotein; mitochondrion; oxidoreductase FEATURE !$1-25 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$26-421 #product acyl-CoA dehydrogenase, !8medium-chain-specific #status predicted #label MAT SUMMARY #length 421 #molecular-weight 46555 #checksum 2103 SEQUENCE /// ENTRY B34252 #type complete TITLE acyl-CoA dehydrogenase (EC 1.3.99.3) short-chain-specific precursor, hepatic - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B34252 REFERENCE A34252 !$#authors Matsubara, Y.; Indo, Y.; Naito, E.; Ozasa, H.; Glassberg, !1R.; Vockley, J.; Ikeda, Y.; Kraus, J.; Tanaka, K. !$#journal J. Biol. Chem. (1989) 264:16321-16331 !$#title Molecular cloning and nucleotide sequence of cDNAs encoding !1the precursors of rat long chain acyl-coenzyme A, short !1chain acyl-coenzyme A, and isovaleryl-coenzyme A !1dehydrogenases. Sequence homology of four enzymes of the !1acyl-CoA dehydrogenase family. !$#cross-references MUID:89380240; PMID:2777793 !$#accession B34252 !'##status preliminary !'##molecule_type mRNA !'##residues 1-414 ##label MAT !'##cross-references GB:J05030; NID:g202686; PIDN:AAA40669.1; !1PID:g202687 CLASSIFICATION #superfamily acyl-CoA dehydrogenase KEYWORDS liver; mitochondrion; oxidoreductase SUMMARY #length 414 #molecular-weight 44967 #checksum 2847 SEQUENCE /// ENTRY C34252 #type complete TITLE isovaleryl-CoA dehydrogenase (EC 1.3.99.10) precursor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C34252; A29490 REFERENCE A34252 !$#authors Matsubara, Y.; Indo, Y.; Naito, E.; Ozasa, H.; Glassberg, !1R.; Vockley, J.; Ikeda, Y.; Kraus, J.; Tanaka, K. !$#journal J. Biol. Chem. (1989) 264:16321-16331 !$#title Molecular cloning and nucleotide sequence of cDNAs encoding !1the precursors of rat long chain acyl-coenzyme A, short !1chain acyl-coenzyme A, and isovaleryl-coenzyme A !1dehydrogenases. Sequence homology of four enzymes of the !1acyl-CoA dehydrogenase family. !$#cross-references MUID:89380240; PMID:2777793 !$#accession C34252 !'##status preliminary !'##molecule_type mRNA !'##residues 1-424 ##label MAT1 !'##cross-references GB:J05031; NID:g204981; PIDN:AAA41454.1; !1PID:g204982 !'##experimental_source hepatic REFERENCE A29490 !$#authors Kraus, J.P.; Matsubara, Y.; Barton, D.; Yang-Feng, T.L.; !1Glassberg, R.; Ito, M.; Ikeda, Y.; Mole, J.; Francke, U.; !1Tanaka, K. !$#journal Genomics (1987) 1:264-269 !$#title Isolation of cDNA clones coding for rat isovaleryl-CoA !1dehydrogenase and assignment of the gene to human chromosome !115. !$#cross-references MUID:88186060; PMID:3446585 !$#accession A29490 !'##molecule_type mRNA !'##residues 1-48 ##label KRA !'##cross-references GB:M19867; NID:g204991; PIDN:AAA41459.1; !1PID:g204992 !'##experimental_source mitochondrion CLASSIFICATION #superfamily acyl-CoA dehydrogenase KEYWORDS mitochondrion; oxidoreductase FEATURE !$1-30 #domain transit peptide (mitochondrion) #status !8predicted #label SIG\ !$31-48 #product isovaleryl-CoA dehydrogenase #status !8predicted #label MAT SUMMARY #length 424 #molecular-weight 46435 #checksum 3174 SEQUENCE /// ENTRY A55680 #type complete TITLE acyl-CoA dehydrogenase (EC 1.3.99.-) short/branched chain specific precursor - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A55680 REFERENCE A55680 !$#authors Rozen, R.; Vockley, J.; Zhou, L.; Milos, R.; Willard, J.; !1Fu, K.; Vicanek, C.; Low-Nang, L.; Torban, E.; Fournier, B. !$#journal Genomics (1994) 24:280-287 !$#title Isolation and expression of a cDNA encoding the precursor !1for a novel member (ACADSB) of the Acyl-CoA dehydrogenase !1gene family. !$#cross-references MUID:95213018; PMID:7698750 !$#accession A55680 !'##status preliminary !'##molecule_type mRNA !'##residues 1-432 ##label ROZ !'##cross-references GB:U12778; NID:g531390; PIDN:AAA74424.1; !1PID:g531391 GENETICS !$#gene GDB:ACADSB !'##cross-references GDB:388699; OMIM:600301 !$#map_position 10q25-10q26 CLASSIFICATION #superfamily acyl-CoA dehydrogenase KEYWORDS mitochondrion; oxidoreductase SUMMARY #length 432 #molecular-weight 47485 #checksum 4172 SEQUENCE /// ENTRY S55421 #type complete TITLE acyl-CoA dehydrogenase (EC 1.3.99.3) acdA - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S55421; B69581 REFERENCE S55414 !$#authors Glaser, P.; Danchin, A. !$#submission submitted to the EMBL Data Library, May 1995 !$#description Cloning and sequencing of the Bacillus subtilis chromosomal !1region from 320 degrees to 321 degrees. !$#accession S55421 !'##status preliminary !'##molecule_type DNA !'##residues 1-379 ##label GLA !'##cross-references EMBL:Z49782; NID:g853752; PIDN:CAA89868.1; !1PID:g853760 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69581 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-379 ##label KUN !'##cross-references GB:Z99123; GB:AL009126; NID:g2636240; !1PIDN:CAB15745.1; PID:g2636254 !'##experimental_source strain 168 GENETICS !$#gene acdA CLASSIFICATION #superfamily acyl-CoA dehydrogenase KEYWORDS oxidoreductase SUMMARY #length 379 #molecular-weight 41446 #checksum 220 SEQUENCE /// ENTRY A34252 #type complete TITLE long-chain-acyl-CoA dehydrogenase (EC 1.3.99.13) precursor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A34252; S39802 REFERENCE A34252 !$#authors Matsubara, Y.; Indo, Y.; Naito, E.; Ozasa, H.; Glassberg, !1R.; Vockley, J.; Ikeda, Y.; Kraus, J.; Tanaka, K. !$#journal J. Biol. Chem. (1989) 264:16321-16331 !$#title Molecular cloning and nucleotide sequence of cDNAs encoding !1the precursors of rat long chain acyl-coenzyme A, short !1chain acyl-coenzyme A, and isovaleryl-coenzyme A !1dehydrogenases. Sequence homology of four enzymes of the !1acyl-CoA dehydrogenase family. !$#cross-references MUID:89380240; PMID:2777793 !$#accession A34252 !'##status preliminary !'##molecule_type mRNA !'##residues 1-430 ##label MAT !'##cross-references GB:J05029; NID:g202684; PIDN:AAA40668.1; !1PID:g202685; GB:M26200 !'##experimental_source hepatic REFERENCE S39802 !$#authors Hainline, B.E.; Kahlenbeck, D.J.; Grant, J.; Strauss, A.W. !$#journal Biochim. Biophys. Acta (1993) 1216:460-468 !$#title Tissue specific and developmental expression of rat long- !1and medium-chain acyl-CoA dehydrogenases. !$#cross-references MUID:94092740; PMID:8268228 !$#accession S39802 !'##status preliminary !'##molecule_type mRNA !'##residues 1-430 ##label HAI !'##cross-references EMBL:L11276; NID:g205144; PIDN:AAA41514.1; !1PID:g205145 CLASSIFICATION #superfamily acyl-CoA dehydrogenase KEYWORDS mitochondrion; oxidoreductase FEATURE !$1-30 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$31-430 #product long-chain-acyl-CoA dehydrogenase #status !8predicted #label MATP SUMMARY #length 430 #molecular-weight 47872 #checksum 2261 SEQUENCE /// ENTRY I41011 #type complete TITLE probable acyl-CoA dehydrogenase (EC 1.3.99.-) carnitine operon caiA - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS G64724; I41011; S40560 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64724 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-380 ##label BLAT !'##cross-references GB:AE000114; GB:U00096; NID:g1786217; !1PIDN:AAC73150.1; PID:g1786223; UWGP:b0039 !'##experimental_source strain K-12, substrain MG1655 REFERENCE I41010 !$#authors Eichler, K.; Bourgis, F.; Buchet, A.; Kleber, H.P.; !1Mandrand-Berthelot, M.A. !$#journal Mol. Microbiol. (1994) 13:775-786 !$#title Molecular characterization of the cai operon necessary for !1carnitine metabolism in Escherichia coli. !$#cross-references MUID:95115548; PMID:7815937 !$#accession I41011 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-380 ##label RES !'##cross-references EMBL:X73904; NID:g563860; PIDN:CAA52111.1; !1PID:g563862 !'##experimental_source strain 044 K74 REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40560 !'##molecule_type DNA !'##residues 1-142,'K',144-181,'G',183-380 ##label YUR !'##cross-references EMBL:D10483; NID:g216434; PIDN:BAA01315.1; !1PID:g216464 GENETICS !$#gene caiA CLASSIFICATION #superfamily acyl-CoA dehydrogenase KEYWORDS FAD; flavoprotein; oxidoreductase SUMMARY #length 380 #molecular-weight 42558 #checksum 2633 SEQUENCE /// ENTRY A43830 #type complete TITLE alanine dehydrogenase (EC 1.4.1.1) ald - Mycobacterium tuberculosis ORGANISM #formal_name Mycobacterium tuberculosis DATE 30-Jun-1993 #sequence_revision 24-Jul-1998 #text_change 16-Jun-2000 ACCESSIONS C70883; A43830; B43830; S18864 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession C70883 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-371 ##label COL !'##cross-references GB:AL008967; GB:AL123456; NID:g3261491; !1PIDN:CAA15575.1; PID:g2624302 !'##experimental_source strain H37Rv REFERENCE A43830 !$#authors Andersen, A.B.; Andersen, P.; Ljungqvist, L. !$#journal Infect. Immun. (1992) 60:2317-2323 !$#title Structure and function of a 40,000-molecular-weight protein !1antigen of Mycobacterium tuberculosis. !$#cross-references MUID:92267644; PMID:1587598 !$#accession A43830 !'##molecule_type DNA !'##residues 1-14,'QF',15-371 ##label AND !'##cross-references EMBL:X63069; NID:g44565; PIDN:CAA44791.1; !1PID:g44566 !$#accession B43830 !'##molecule_type protein !'##residues 1,'X',3-5,'X',7,'XX',10 ##label AND2 COMMENT This enzyme may be important in synthesis of peptidoglycan !1in the cell wall. Although it lacks a cleaved signal !1sequence, the enzyme is secreted across the cell membrane. GENETICS !$#gene ald CLASSIFICATION #superfamily alanine dehydrogenase; alanine dehydrogenase !1homology KEYWORDS NAD; oxidoreductase FEATURE !$1-278 #domain alanine dehydrogenase homology #label ALA\ !$170-198 #region beta-alpha-beta NAD nucleotide-binding fold SUMMARY #length 371 #molecular-weight 38713 #checksum 7340 SEQUENCE /// ENTRY DENCED #type fragments TITLE glutamate dehydrogenase (EC 1.4.1.2) - Neurospora crassa (tentative sequence) (fragments) ALTERNATE_NAMES glutamic dehydrogenase; NAD-specific glutamate dehydrogenase ORGANISM #formal_name Neurospora crassa DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 31-Mar-2000 ACCESSIONS A92284; A92215; A32204; A00378 REFERENCE A92284 !$#authors Haberland, M.E.; Smith, E.L. !$#journal J. Biol. Chem. (1980) 255:7984-7992 !$#title Nicotinamide adenine dinucleotide-specific glutamate !1dehydrogenase of Neurospora crassa. Isolation and sequences !1of several cyanogen bromide peptides from the NH-2-terminal !1portion of the peptide chain. !$#cross-references MUID:80249569; PMID:6447150 !$#accession A92284 !'##molecule_type protein !'##residues 1-356 ##label HAB REFERENCE A92215 !$#authors Austen, B.M.; Haberland, M.E.; Nyc, J.F.; Smith, E.L. !$#journal J. Biol. Chem. (1977) 252:8142-8149 !$#title Nicotinamide adenine dinucleotide-specific glutamate !1dehydrogenase of Neurospora. IV. The COOH-terminal 669 !1residues of the peptide chain; comparison with other !1glutamate dehydrogenases. !$#cross-references MUID:78026588; PMID:21191 !$#accession A92215 !'##molecule_type protein !'##residues 357-1025 ##label AUS !'##note this is the final paper in a series REFERENCE A32204 !$#authors Vierula, P.J.; Kapoor, M. !$#journal J. Biol. Chem. (1989) 264:1108-1114 !$#title NAD-specific glutamate dehydrogenase of Neurospora crassa. !1cDNA cloning and gene expression during derepression. !$#cross-references MUID:89093096; PMID:2521336 !$#accession A32204 !'##molecule_type mRNA !'##residues 618-728,'N',730-763,'N',765-774,'V',776,'H',777-819,'ST', !1822-883,'D',885-923 ##label VIE !'##cross-references GB:M23436; NID:g168845; PIDN:AAA33601.1; !1PID:g168846; GB:M21816 CLASSIFICATION #superfamily glutamate dehydrogenase KEYWORDS NAD; oxidoreductase FEATURE !$481,570 #binding_site substrate (Lys) #status predicted SUMMARY #length 1025 #checksum 3887 SEQUENCE /// ENTRY S37676 #type complete TITLE glutamate dehydrogenase (EC 1.4.1.2) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES glutamic dehydrogenase; NAD-specific glutamate dehydrogenase; protein D0892; protein YDL215c ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Dec-1993 #sequence_revision 23-Mar-1995 #text_change 21-Jul-2000 ACCESSIONS S37676; S22282; S67774; S67778 REFERENCE S37676 !$#authors Boles, E.; Lehnert, W.; Zimmermann, F.K. !$#journal Eur. J. Biochem. (1993) 217:469-477 !$#title The role of the NAD-dependent glutamate dehydrogenase in !1restoring growth on glucose of a Saccharomyces cerevisiae !1phosphoglucose isomerase mutant. !$#cross-references MUID:94039072; PMID:7901008 !$#accession S37676 !'##molecule_type DNA !'##residues 1-1092 ##label BOL !'##cross-references EMBL:X72015; NID:g396750; PIDN:CAA50894.1; !1PID:g396751 REFERENCE S22282 !$#authors Miller, S.M.; Magasanik, B. !$#journal Mol. Cell. Biol. (1991) 11:6229-6247 !$#title Role of the complex upstream region of the GDH2 gene in !1nitrogen regulation of the NAD-linked glutamate !1dehydrogenase in Saccharomyces cerevisiae. !$#cross-references MUID:92049354; PMID:1682801 !$#accession S22282 !'##molecule_type DNA !'##residues 1-79 ##label MIL !'##cross-references GB:S66436; NID:g238959; PIDN:AAB20327.1; !1PID:g238960 REFERENCE S67756 !$#authors Schmidt, E.R.; Bahr, A.; Kraemer, C.; Hankeln, T.; !1Moeller-Rieker, S. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67774 !'##molecule_type DNA !'##residues 1-1092 ##label SCH !'##cross-references EMBL:Z74263; NID:g1431359; PIDN:CAA98793.1; !1PID:g1431360; GSPDB:GN00004; MIPS:YDL215c !'##experimental_source strain S288C REFERENCE S67778 !$#authors Rasmussen, S.W. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67778 !'##molecule_type DNA !'##residues 849-1092 ##label RAS !'##cross-references EMBL:Z74263; GSPDB:GN00004; MIPS:YDL215c !'##experimental_source strain S288C GENETICS !$#gene SGD:GDH2; MIPS:YDL215c !'##cross-references SGD:S0002374; MIPS:YDL215c !$#map_position 4L CLASSIFICATION #superfamily glutamate dehydrogenase KEYWORDS NAD; oxidoreductase FEATURE !$536,626 #binding_site substrate (Lys) #status predicted SUMMARY #length 1092 #molecular-weight 124331 #checksum 5575 SEQUENCE /// ENTRY DEHUE #type complete TITLE glutamate dehydrogenase [NAD(P)] (EC 1.4.1.3) precursor - human ALTERNATE_NAMES glutamic dehydrogenase ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 03-Jun-2002 ACCESSIONS A28208; A27697; A27881; A27481; S00958; C46125; A46125; !1B46125; S10769; A00379; S29932 REFERENCE A94195 !$#authors Mavrothalassitis, G.; Tzimagiorgis, G.; Mitsialis, A.; !1Zannis, V.; Plaitakis, A.; Papamatheakis, J.; Moschonas, N. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:3494-3498 !$#title Isolation and characterization of cDNA clones encoding human !1liver glutamate dehydrogenase: evidence for a small gene !1family. !$#cross-references MUID:88217927; PMID:3368458 !$#accession A28208 !'##molecule_type mRNA !'##residues 1-558 ##label MAV !'##cross-references GB:J03248; NID:g183053; PIDN:AAA52523.1; !1PID:g183054 !'##experimental_source liver REFERENCE A90143 !$#authors Amuro, N.; Yamaura, M.; Goto, Y.; Okazaki, T. !$#journal Biochem. Biophys. Res. Commun. (1988) 152:1395-1400 !$#title Molecular cloning and nucleotide sequence of the cDNA for !1human liver glutamate dehydrogenase precursor. !$#cross-references MUID:88240360; PMID:3377777 !$#accession A27697 !'##molecule_type mRNA !'##residues 1-558 ##label AMU1 !'##cross-references GB:M20867; NID:g183059; PIDN:AAA52526.1; !1PID:g183060 !'##experimental_source liver !'##note the authors translated the codon AUC for residue 380 as Gly REFERENCE A92973 !$#authors Banner, C.; Silverman, S.; Thomas, J.W.; Lampel, K.A.; !1Vitkovic, L.; Huie, D.; Wenthold, R.J. !$#journal J. Neurochem. (1987) 49:246-252 !$#title Isolation of a human brain cDNA for glutamate dehydrogenase. !$#cross-references MUID:87224937; PMID:3585334 !$#accession A27881 !'##molecule_type mRNA !'##residues 301-558 ##label BAN !'##experimental_source brain REFERENCE A90138 !$#authors Nakatani, Y.; Banner, C.; von Herrath, M.; Schneider, M.E.; !1Smith, H.H.; Freese, E. !$#journal Biochem. Biophys. Res. Commun. (1987) 149:405-410 !$#title Comparison of human brain and liver glutamate dehydrogenase !1cDNAs. !$#cross-references MUID:88106451; PMID:3426581 !$#accession A27481 !'##molecule_type mRNA !'##residues 131-558 ##label NAK1 !'##cross-references GB:X07674; GB:M18377; NID:g31706; PIDN:CAA30521.1; !1PID:g31707 !'##note the complete sequence and translation are not shown; the !1complete submitted sequence is shown in GenBank entry !1HSGDHR, release 113.0 REFERENCE S00958 !$#authors Nakatani, Y.; Schneider, M.; Banner, C.; Freese, E. !$#journal Nucleic Acids Res. (1988) 16:6237 !$#title Complete nucleotide sequence of human glutamate !1dehydrogenase cDNA. !$#cross-references MUID:88289377; PMID:3399399 !$#accession S00958 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-558 ##label NAK2 !'##cross-references GB:M37154; NID:g183057; PIDN:AAA52525.1; !1PID:g183058; EMBL:X07769; NID:g31798; PIDN:CAA30598.1; !1PID:g31799 REFERENCE A46125 !$#authors Michaelidis, T.M.; Tzimagiorgis, G.; Moschonas, N.K.; !1Papamatheakis, J. !$#journal Genomics (1993) 16:150-160 !$#title The human glutamate dehydrogenase gene family: gene !1organization and structural characterization. !$#cross-references MUID:93252371; PMID:8486350 !$#accession C46125 !'##molecule_type DNA !'##residues 1-1 ##label MIC1 !'##cross-references GB:S60495; NID:g300129; PIDN:AAD14931.1; !1PID:g4262783 !$#accession A46125 !'##molecule_type DNA !'##residues 150-215 ##label MIC2 !'##cross-references GB:S60498; NID:g300124; PIDN:AAC60587.1; !1PID:g300125 !'##note sequence extracted from NCBI backbone (NCBIN:131434, !1NCBIN:131436, NCBIN:131438, NCBIP:131439) !$#accession B46125 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 420-558 ##label MIC3 !'##note this translation from Fig. 6 is not annotated in GenBank, !1release 113.0 REFERENCE S10769 !$#authors Amuro, N.; Goto, Y.; Okazaki, T. !$#journal Biochim. Biophys. Acta (1990) 1049:216-218 !$#title Isolation and characterization of the two distinct genes for !1human glutamate dehydrogenase. !$#cross-references MUID:90304226; PMID:2364112 !$#accession S10769 !'##molecule_type DNA !'##residues 150-215 ##label AMU2 !'##cross-references EMBL:X53144; NID:g31700; EMBL:X53145; NID:g31701; !1EMBL:X53146; NID:g31702; GB:X66301; NID:g31807; GB:X66302; !1NID:g31808 !'##note this translation is not annotated in the cross-referenced !1GenBank entries REFERENCE A92250 !$#authors Julliard, J.H.; Smith, E.L. !$#journal J. Biol. Chem. (1979) 254:3427-3438 !$#title Partial amino acid sequence of the glutamate dehydrogenase !1of human liver and a revision of the sequence of the bovine !1enzyme. !$#cross-references MUID:79151102; PMID:429360 !$#contents annotation; partial sequence GENETICS !$#gene GDB:GLUD1; GLUD; GDH1 !'##cross-references GDB:119994; OMIM:138130 !$#map_position 10q23.3-10q23.3 !$#introns 149/1; 176/1; 194/3; 216/1; 247/3; 307/3; 353/3; 399/3; 426/ !13; 468/1; 498/3; 519/3 !$#note the list of introns may be incomplete COMPLEX homohexamer FUNCTION !$#description catalyzes the reversible reaction of L-glutamate, water and !1NAD (or NADP) to form alpha-ketoglutarate, ammonia and NADH !1(or NADPH) CLASSIFICATION #superfamily glutamate dehydrogenase (NAD(P)+) KEYWORDS homohexamer; mitochondrion; NAD; NADP; oxidoreductase FEATURE !$1-53 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$54-558 #product glutamate dehydrogenase (NAD(P)+) #status !8predicted #label MAT\ !$84,183 #binding_site substrate (Lys) #status predicted SUMMARY #length 558 #molecular-weight 61397 #checksum 6214 SEQUENCE /// ENTRY A53719 #type complete TITLE glutamate dehydrogenase [NAD(P)] (EC 1.4.1.3) 2 precursor - human ORGANISM #formal_name Homo sapiens #common_name man DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 03-Jun-2002 ACCESSIONS A53719; S31838 REFERENCE A53719 !$#authors Shashidharan, P.; Michaelidis, T.M.; Robakis, N.K.; !1Kresovali, A.; Papamatheakis, J.; Plaitakis, A. !$#journal J. Biol. Chem. (1994) 269:16971-16976 !$#title Novel human glutamate dehydrogenase expressed in neural and !1testicular tissues and encoded by an X-linked intronless !1gene. !$#cross-references MUID:94266921; PMID:8207021 !$#accession A53719 !'##molecule_type DNA !'##residues 1-558 ##label SHA !'##cross-references GB:U08997; NID:g478987; PIDN:AAA20969.1; !1PID:g478988 !'##note several cDNA clones to mRNA from this gene were also found REFERENCE S29331 !$#authors Michaelidis, T. !$#submission submitted to the EMBL Data Library, May 1992 !$#accession S31838 !'##molecule_type DNA !'##residues 1-558 ##label MIC !'##cross-references EMBL:X66310; NID:g31814; PIDN:CAA46995.1; !1PID:g31815 GENETICS !$#gene GDB:GLUD2; GDB:GLUDP1 !'##cross-references GDB:9954793; OMIM:300144; GDB:119274; OMIM:305910 !$#map_position Xq24-Xq25 !$#note this apparently processed (retroposon), intronless gene is !1expressed in neural and testicular tissues and encodes a !1functional protein FUNCTION !$#description catalyzes the reversible reaction of L-glutamate, water and !1NAD (or NADP) to form alpha-ketoglutarate, ammonia and NADH !1(or NADPH) CLASSIFICATION #superfamily glutamate dehydrogenase (NAD(P)+) KEYWORDS mitochondrion; NAD; NADP; oxidoreductase FEATURE !$1-53 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$54-558 #product glutamate dehydrogenase (NAD(P)+) #status !8predicted #label MAT\ !$84,183 #binding_site substrate (Lys) #status predicted SUMMARY #length 558 #molecular-weight 61432 #checksum 8219 SEQUENCE /// ENTRY DEBOE #type complete TITLE glutamate dehydrogenase [NAD(P)] (EC 1.4.1.3) - bovine (tentative sequence) ALTERNATE_NAMES glutamic dehydrogenase ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 22-May-1981 #sequence_revision 22-May-1981 #text_change 03-Jun-2002 ACCESSIONS A92129; A92250; S03861; A00379 REFERENCE A92129 !$#authors Moon, K.; Smith, E.L. !$#journal J. Biol. Chem. (1973) 248:3082-3088 !$#title Sequence of bovine liver glutmate dehydrogenase. VIII. !1Peptides produced by specific chemical cleavages; the !1complete sequence of the protein. !$#cross-references MUID:73166548; PMID:4735572 !$#accession A92129 !'##molecule_type protein !'##residues 1-383,'Z',386-501 ##label MOO !'##experimental_source liver !'##note this is the final paper in a series giving the experimental !1details REFERENCE A92250 !$#authors Julliard, J.H.; Smith, E.L. !$#journal J. Biol. Chem. (1979) 254:3427-3438 !$#title Partial amino acid sequence of the glutamate dehydrogenase !1of human liver and a revision of the sequence of the bovine !1enzyme. !$#cross-references MUID:79151102; PMID:429360 !$#accession A92250 !'##molecule_type protein !'##residues 1-501 ##label JUL REFERENCE A91217 !$#authors Rasched, I.; Jornvall, H.; Sund, H. !$#journal Eur. J. Biochem. (1974) 41:603-606 !$#title Studies of glutamate dehydrogenase. Identification of an !1amino group involved in the substrate binding. !$#cross-references MUID:74125870; PMID:4856315 !$#contents annotation; substrate-binding site REFERENCE S03861 !$#authors Batra, S.P.; Lark, R.H.; Colman, R.F. !$#journal Arch. Biochem. Biophys. (1989) 270:277-285 !$#title Identification of histidyl peptide labeled by 2-(4-bromo-2, !13-dioxobutylthio)adenosine 5'-monophosphate in an ADP !1regulatory site of glutamate dehydrogenase. !$#cross-references MUID:89192378; PMID:2930190 !$#accession S03861 !'##molecule_type protein !'##residues 156-167,'D',169-173;218-220,'HG',223-225;343-354,'E', !1356-358 ##label BAT CLASSIFICATION #superfamily glutamate dehydrogenase (NAD(P)+) KEYWORDS homohexamer; mitochondrion; NAD; NADP; oxidoreductase FEATURE !$27,126 #binding_site substrate (Lys) #status experimental SUMMARY #length 501 #molecular-weight 55561 #checksum 5335 SEQUENCE /// ENTRY S03707 #type complete TITLE glutamate dehydrogenase [NAD(P)] (EC 1.4.1.3) precursor - rat ALTERNATE_NAMES glutamic dehydrogenase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 01-Dec-1989 #sequence_revision 23-Mar-1995 #text_change 03-Jun-2002 ACCESSIONS S03707; S03704; S29786; S29335; S19282 REFERENCE S03707 !$#authors Amuro, N.; Ooki, K.; Ito, A.; Goto, Y.; Okazaki, T. !$#journal Nucleic Acids Res. (1989) 17:2356 !$#title Nucleotide sequence of rat liver glutamate dehydrogenase !1cDNA. !$#cross-references MUID:89202049; PMID:2704625 !$#accession S03707 !'##molecule_type mRNA !'##residues 1-558 ##label AMU !'##cross-references EMBL:X14223; NID:g56199; PIDN:CAA32441.1; !1PID:g56200 REFERENCE S03704 !$#authors Das, A.T.; Moerer, P.; Charles, R.; Moorman, A.F.M.; Lamers, !1W.H. !$#journal Nucleic Acids Res. (1989) 17:2355 !$#title Nucleotide sequence of rat liver glutamate dehydrogenase !1cDNA. !$#cross-references MUID:89202048; PMID:2704624 !$#accession S03704 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-55,'AA',57-558 ##label DAS !'##cross-references EMBL:X14044 !'##experimental_source liver REFERENCE S29786 !$#authors Das, A.T.; Arnberg, A.C.; Malingre, H.; Moerer, P.; Charles, !1R.; Moorman, A.F.M.; Lamers, W.H. !$#journal Eur. J. Biochem. (1993) 211:795-803 !$#title Isolation and characterization of the rat gene encoding !1glutamate dehydrogenase. !$#cross-references MUID:93170315; PMID:8094669 !$#accession S29786 !'##status preliminary !'##molecule_type DNA !'##residues 1-30 ##label DA2 !'##cross-references EMBL:X64365; NID:g297520; PIDN:CAA45717.1; !1PID:g57905 REFERENCE S29335 !$#authors Das, A.T. !$#submission submitted to the EMBL Data Library, February 1992 !$#accession S29335 !'##status preliminary !'##molecule_type DNA !'##residues 1-30 ##label DA3 !'##cross-references EMBL:X64365; NID:g297520; PIDN:CAA45717.1; !1PID:g57905 REFERENCE S19282 !$#authors Schwerdt, G.; Moeller, U.; Huth, W. !$#journal Biochem. J. (1991) 280:353-357 !$#title Identification of the CoA-modified forms of mitochondrial !1acetyl-CoA acetyltransferase and of glutamate dehydrogenase !1as nearest-neighbour proteins. !$#cross-references MUID:92082470; PMID:1684101 !$#accession S19282 !'##molecule_type protein !'##residues 161-171,'S',173-175,'X',177-190 ##label SCH CLASSIFICATION #superfamily glutamate dehydrogenase (NAD(P)+) KEYWORDS mitochondrion; NAD; NADP; oxidoreductase FEATURE !$1-53 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$54-558 #product glutamate dehydrogenase #status predicted !8#label MAT\ !$84,183 #binding_site substrate (Lys) #status predicted SUMMARY #length 558 #molecular-weight 61427 #checksum 585 SEQUENCE /// ENTRY DECHE #type complete TITLE glutamate dehydrogenase [NAD(P)] (EC 1.4.1.3) - chicken (tentative sequence) ALTERNATE_NAMES glutamic dehydrogenase ORGANISM #formal_name Gallus gallus #common_name chicken DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 03-Jun-2002 ACCESSIONS A00380 REFERENCE A00380 !$#authors Moon, K.; Piszkiewicz, D.; Smith, E.L. !$#journal J. Biol. Chem. (1973) 248:3093-3107 !$#title Amino acid sequence of chicken liver glutamate !1dehydrogenase. !$#cross-references MUID:73166550; PMID:4735574 !$#accession A00380 !'##molecule_type protein !'##residues 1-503 ##label MOO !'##note the authors indicate that the amidation states of residues 9, !1247, 311, 365, 367, 373, 439, 440, and 465 were !1experimentally determined. Residue 150 was not isolated or !1identified !'##note Lys-129 covalently binds pyridoxal 5'-phosphate with !1concomitant loss of enzymatic activity COMMENT The enzyme molecule is a hexamer of identical chains !1isolated from liver mitochondria. CLASSIFICATION #superfamily glutamate dehydrogenase (NAD(P)+) KEYWORDS homohexamer; mitochondrion; NAD; NADP; oxidoreductase FEATURE !$30,129 #binding_site substrate (Lys) #status predicted SUMMARY #length 503 #molecular-weight 55711 #checksum 8434 SEQUENCE /// ENTRY S16239 #type complete TITLE glutamate dehydrogenase [NAD(P)] (EC 1.4.1.3) precursor - mouse ALTERNATE_NAMES glutamic dehydrogenase ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Jun-1992 #sequence_revision 23-Mar-1995 #text_change 03-Jun-2002 ACCESSIONS S16239 REFERENCE S16239 !$#authors Tzimagiorgis, G.; Moschonas, N.K. !$#journal Biochim. Biophys. Acta (1991) 1089:250-253 !$#title Molecular cloning, structure and expression analysis of a !1full-length mouse brain glutamate dehydrogenase cDNA. !$#cross-references MUID:91274358; PMID:1711373 !$#accession S16239 !'##molecule_type mRNA !'##residues 1-558 ##label TZI !'##cross-references EMBL:X57024; NID:g51081; PIDN:CAA40341.1; !1PID:g51082 GENETICS !$#gene GLUD CLASSIFICATION #superfamily glutamate dehydrogenase (NAD(P)+) KEYWORDS mitochondrion; NAD; NADP; oxidoreductase FEATURE !$1-53 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$54-558 #product glutamate dehydrogenase (NAD(P)+) #status !8predicted #label MAT\ !$84,183 #binding_site substrate (Lys) #status predicted SUMMARY #length 558 #molecular-weight 61336 #checksum 8468 SEQUENCE /// ENTRY DENCEN #type complete TITLE glutamate dehydrogenase (NADP) (EC 1.4.1.4) - Neurospora crassa ALTERNATE_NAMES glutamic dehydrogenase; NADP-specific glutamate dehydrogenase ORGANISM #formal_name Neurospora crassa DATE 24-Apr-1984 #sequence_revision 20-Sep-1984 #text_change 03-Jun-2002 ACCESSIONS A91506; A90288; T47238; A00381 REFERENCE A91506 !$#authors Kinnaird, J.H.; Fincham, J.R.S. !$#journal Gene (1983) 26:253-260 !$#title The complete nucleotide sequence of the Neurospora crassa am !1(NADP-specific glutamate dehydrogenase) gene. !$#cross-references MUID:84159508; PMID:6231215 !$#accession A91506 !'##molecule_type DNA !'##residues 1-454 ##label KIN !'##cross-references GB:K01409; NID:g168752; PIDN:AAA33558.1; !1PID:g168753 REFERENCE A90288 !$#authors Holder, A.A.; Wootton, J.C.; Baron, A.J.; Chambers, G.K.; !1Fincham, J.R.S. !$#journal Biochem. J. (1975) 149:757-773 !$#title The amino acid sequence of Neurospora NADP-specific !1glutamate dehydrogenase. Peptic and chymotryptic peptides !1and the complete sequence. !$#cross-references MUID:76087806; PMID:1002 !$#accession A90288 !'##molecule_type protein !'##residues 2-56,'D',58-313,'ED',316-450,452-454 ##label HOL !'##note this is the final paper in a series REFERENCE Z24414 !$#authors Rambosek, J.A.; Kinsey, J.A. !$#journal Gene (1984) 27:101-107 !$#title An unstable mutant gene of the am locus of Neurospora !1results from a small duplication. !$#cross-references MUID:84183602; PMID:6325296 !$#accession T47238 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-25 ##label RAM !'##cross-references EMBL:K02468; NID:g168754; PIDN:AAA33559.1; !1PID:g168755 GENETICS !$#gene am !$#introns 16/1; 108/1 CLASSIFICATION #superfamily glutamate dehydrogenase (NAD(P)+) KEYWORDS acetylated amino end; NADP; oxidoreductase FEATURE !$2-454 #product glutamate dehydrogenase (NADP+) #status !8experimental #label MAT\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental\ !$114 #binding_site substrate (Lys) #status predicted SUMMARY #length 454 #molecular-weight 48853 #checksum 1037 SEQUENCE /// ENTRY S04904 #type complete TITLE glutamate dehydrogenase (NADP) (EC 1.4.1.4) - Emericella nidulans ALTERNATE_NAMES glutamic dehydrogenase; NADP-specific glutamate dehydrogenase ORGANISM #formal_name Emericella nidulans, Aspergillus nidulans DATE 28-Feb-1990 #sequence_revision 23-Mar-1995 #text_change 03-Jun-2002 ACCESSIONS S04904 REFERENCE S04904 !$#authors Hawkins, A.R.; Gurr, S.J.; Montague, P.; Kinghorn, J.R. !$#journal Mol. Gen. Genet. (1989) 218:105-111 !$#title Nucleotide sequence and regulation of expression of the !1Aspergillus nidulans gdhA gene encoding NADP dependent !1glutamate dehydrogenase. !$#cross-references MUID:89384423; PMID:2550758 !$#accession S04904 !'##molecule_type DNA !'##residues 1-459 ##label HAW !'##cross-references EMBL:X16121; NID:g2347; PIDN:CAA34252.1; PID:g2348 !'##note the authors translated the codon CTT for residue 150 as Val GENETICS !$#gene gdhA !$#introns 16/1; 108/1 CLASSIFICATION #superfamily glutamate dehydrogenase (NAD(P)+) KEYWORDS NADP; oxidoreductase FEATURE !$114 #binding_site substrate (Lys) #status predicted SUMMARY #length 459 #molecular-weight 49622 #checksum 3150 SEQUENCE /// ENTRY A25275 #type complete TITLE glutamate dehydrogenase (NADP) (EC 1.4.1.4) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES glutamic dehydrogenase; NADP-specific glutamate dehydrogenase; protein O6734; protein YOR375c ORGANISM #formal_name Saccharomyces cerevisiae DATE 23-Aug-1987 #sequence_revision 16-Aug-1996 #text_change 03-Jun-2002 ACCESSIONS S67287; A25275; A23976 REFERENCE S67261 !$#authors Delius, H.; Hebling, U.; Hofmann, B. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67287 !'##molecule_type DNA !'##residues 1-454 ##label DEL !'##cross-references EMBL:Z75283; NID:g1420809; PIDN:CAA99706.1; !1PID:g1420810; GSPDB:GN00015; MIPS:YOR375c !'##experimental_source strain S288C REFERENCE A25275 !$#authors Moye, W.S.; Amuro, N.; Rao, J.K.M.; Zalkin, H. !$#journal J. Biol. Chem. (1985) 260:8502-8508 !$#title Nucleotide sequence of yeast GDH1 encoding nicotinamide !1adenine dinucleotide phosphate-dependent glutamate !1dehydrogenase. !$#cross-references MUID:85234567; PMID:2989290 !$#accession A25275 !'##molecule_type DNA !'##residues 1-82,'G',84-197,'L',199-254,'L',256-265,'V',267-454 ##label !1MOY !'##cross-references EMBL:M11297; NID:g1431821; PIDN:AAB03898.1; !1PID:g171592 REFERENCE A23976 !$#authors Nagasu, T.; Hall, B.D. !$#journal Gene (1985) 37:247-253 !$#title Nucleotide sequence of the GDH gene coding for the !1NADP-specific glutamate dehydrogenase of Saccharomyces !1cerevisiae. !$#cross-references MUID:86031359; PMID:2932370 !$#accession A23976 !'##molecule_type DNA !'##residues 1-357;'PLDQAT',368-454 ##label NAG !'##cross-references EMBL:M10590 GENETICS !$#gene SGD:GDH1; MIPS:YOR375c !'##cross-references SGD:S0005902; MIPS:YOR375c !$#map_position 15R CLASSIFICATION #superfamily glutamate dehydrogenase (NAD(P)+) KEYWORDS NADP; oxidoreductase FEATURE !$110 #binding_site substrate (Lys) #status predicted SUMMARY #length 454 #molecular-weight 49570 #checksum 9634 SEQUENCE /// ENTRY DEECEN #type complete TITLE glutamate dehydrogenase (NADP) (EC 1.4.1.4) - Escherichia coli (strain K-12) ALTERNATE_NAMES glutamic dehydrogenase; NADP-specific glutamate dehydrogenase ORGANISM #formal_name Escherichia coli DATE 03-Aug-1984 #sequence_revision 20-Sep-1984 #text_change 03-Jun-2002 ACCESSIONS A00382; A22413; A64936 REFERENCE A00382 !$#authors McPherson, M.J.; Wootton, J.C. !$#journal Nucleic Acids Res. (1983) 11:5257-5266 !$#title Complete nucleotide sequence of the Escherichia coli gdhA !1gene. !$#cross-references MUID:83272967; PMID:6308576 !$#accession A00382 !'##molecule_type DNA !'##residues 1-447 ##label MCP !'##cross-references GB:X00988; GB:J01615; GB:K00565; NID:g41543; !1PIDN:CAA25495.1; PID:g41544 REFERENCE A22413 !$#authors Valle, F.; Becerril, B.; Chen, E.; Seeburg, P.; Heyneker, !1H.; Bolivar, F. !$#journal Gene (1984) 27:193-199 !$#title Complete nucleotide sequence of the glutamate dehydrogenase !1gene from Escherichia coli K-12. !$#cross-references MUID:84209849; PMID:6373501 !$#accession A22413 !'##molecule_type DNA !'##residues 1-447 ##label VAL !'##experimental_source strain K12 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64936 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-447 ##label BLAT !'##cross-references GB:AE000271; GB:U00096; NID:g1788058; !1PIDN:AAC74831.1; PID:g1788059; UWGP:b1761 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene gdhA !$#map_position 27 min CLASSIFICATION #superfamily glutamate dehydrogenase (NAD(P)+) KEYWORDS homohexamer; NADP; oxidoreductase FEATURE !$128 #binding_site substrate (Lys) #status predicted SUMMARY #length 447 #molecular-weight 48581 #checksum 2843 SEQUENCE /// ENTRY A33504 #type complete TITLE glutamate dehydrogenase (NADP) (EC 1.4.1.4) - Salmonella typhimurium ALTERNATE_NAMES glutamic dehydrogenase; NADP-specific glutamate dehydrogenase ORGANISM #formal_name Salmonella typhimurium DATE 08-Dec-1989 #sequence_revision 23-Mar-1995 #text_change 03-Jun-2002 ACCESSIONS A33504 REFERENCE A33504 !$#authors Bansal, A.; Dayton, M.A.; Zalkin, H.; Colman, R.F. !$#journal J. Biol. Chem. (1989) 264:9827-9835 !$#title Affinity labeling of a glutamyl peptide in the coenzyme !1binding site of NADP(+)-specific glutamate dehydrogenase of !1Salmonella typhimurium by 2-[(4-bromo-2,3-dioxobutyl)thio] !1-1,N(6)-ethenoadenosine 2',5'-bisphosphate. !$#cross-references MUID:89255551; PMID:2656714 !$#accession A33504 !'##molecule_type DNA !'##residues 1-447 ##label BAN !'##cross-references GB:M24021; GB:J04814 GENETICS !$#gene gdh !$#map_position 27 min CLASSIFICATION #superfamily glutamate dehydrogenase (NAD(P)+) KEYWORDS homohexamer; NADP; oxidoreductase FEATURE !$128 #binding_site substrate (Lys) #status predicted SUMMARY #length 447 #molecular-weight 48574 #checksum 5173 SEQUENCE /// ENTRY A42489 #type complete TITLE glutamate dehydrogenase (NADP) (EC 1.4.1.4) - Giardia lamblia ALTERNATE_NAMES glutamic dehydrogenase; NADP-specific glutamate dehydrogenase ORGANISM #formal_name Giardia lamblia DATE 31-Dec-1993 #sequence_revision 23-Mar-1995 #text_change 03-Jun-2002 ACCESSIONS A42489 REFERENCE A42489 !$#authors Yee, J.; Dennis, P.P. !$#journal J. Biol. Chem. (1992) 267:7539-7544 !$#title Isolation and characterization of a NADP-dependent glutamate !1dehydrogenase gene from the primitive eucaryote Giardia !1lamblia. !$#cross-references MUID:92218410; PMID:1559991 !$#accession A42489 !'##molecule_type DNA !'##residues 1-449 ##label YEE !'##cross-references GB:M84604; NID:g159108; PIDN:AAA29155.1; !1PID:g159109 !'##note sequence extracted from NCBI backbone (NCBIN:94071, !1NCBIP:94074) CLASSIFICATION #superfamily glutamate dehydrogenase (NAD(P)+) KEYWORDS NADP; oxidoreductase FEATURE !$125 #binding_site substrate (Lys) #status predicted SUMMARY #length 449 #molecular-weight 49766 #checksum 4132 SEQUENCE /// ENTRY S17949 #type fragment TITLE glutamate dehydrogenase (NADP) (EC 1.4.1.4) precursor - Chlorella sorokiniana (fragment) ALTERNATE_NAMES glutamic dehydrogenase; NADP-specific glutamate dehydrogenase ORGANISM #formal_name Chlorella sorokiniana DATE 30-Jun-1992 #sequence_revision 23-Mar-1995 #text_change 03-Jun-2002 ACCESSIONS S17949; S17950; S19030 REFERENCE S17949 !$#authors Cock, J.M.; Kim, K.D.; Miller, P.W.; Hutson, R.G.; Schmidt, !1R.R. !$#journal Plant Mol. Biol. (1991) 17:1023-1044 !$#title A nuclear gene with many introns encoding ammonium-inducible !1chloroplastic NADP-specific glutamate dehydrogenase(s) in !1Chlorella sorokiniana. !$#cross-references MUID:92032762; PMID:1718478 !$#accession S17949 !'##molecule_type DNA !'##residues 1-523 ##label COC !'##cross-references EMBL:X58831 !$#accession S17950 !'##molecule_type mRNA !'##residues 1-523 ##label COC2 !'##cross-references EMBL:X58832; NID:g18272; PIDN:CAA41636.1; !1PID:g18273 REFERENCE S19030 !$#authors Schmidt, R.R. !$#submission submitted to the EMBL Data Library, April 1991 !$#accession S19030 !'##molecule_type DNA !'##residues 1-219,'LW',222-523 ##label SCH !'##cross-references EMBL:X58831 GENETICS !$#genome nuclear !$#introns 6/2; 29/1; 40/3; 56/3; 85/3; 127/3; 149/3; 175/1; 183/3; !1211/1; 246/1; 272/2; 305/3; 344/3; 372/3; 401/3; 438/3; 466/ !13; 484/3; 503/1; 509/1 CLASSIFICATION #superfamily glutamate dehydrogenase (NAD(P)+) KEYWORDS chloroplast; hexamer; NADP; oxidoreductase FEATURE !$202 #binding_site substrate (Lys) #status predicted SUMMARY #length 523 #checksum 3338 SEQUENCE /// ENTRY S18609 #type complete TITLE glutamate dehydrogenase (NADP) (EC 1.4.1.4) - Halobacterium salinarum ALTERNATE_NAMES glutamic dehydrogenase; NADP-specific glutamate dehydrogenase ORGANISM #formal_name Halobacterium salinarum DATE 13-Jan-1995 #sequence_revision 23-Mar-1995 #text_change 03-Jun-2002 ACCESSIONS S18609 REFERENCE S18609 !$#authors Benachenhou, N.; Baldacci, G. !$#journal Mol. Gen. Genet. (1991) 230:345-352 !$#title The gene for a halophilic glutamate dehydrogenase: sequence, !1transcription analysis and phylogenetic implications. !$#cross-references MUID:92114863; PMID:1766432 !$#accession S18609 !'##molecule_type DNA !'##residues 1-435 ##label BEN !'##cross-references EMBL:X63837; NID:g49045; PIDN:CAA45327.1; !1PID:g49046 !'##note the source is designated as Halobacterium salinarium CLASSIFICATION #superfamily glutamate dehydrogenase (NAD(P)+) KEYWORDS NADP; oxidoreductase FEATURE !$126 #binding_site substrate (Lys) #status predicted SUMMARY #length 435 #molecular-weight 47458 #checksum 1053 SEQUENCE /// ENTRY A38168 #type complete TITLE glutamate dehydrogenase (EC 1.4.1.2) - Peptostreptococcus asaccharolyticus ALTERNATE_NAMES glutamic dehydrogenase; NAD-specific glutamate dehydrogenase ORGANISM #formal_name Peptostreptococcus asaccharolyticus DATE 16-Oct-1992 #sequence_revision 23-Mar-1995 #text_change 11-Jun-1999 ACCESSIONS A38168 REFERENCE A38168 !$#authors Snedecor, B.; Chu, H.; Chen, E. !$#journal J. Bacteriol. (1991) 173:6162-6167 !$#title Selection, expression, and nucleotide sequencing of the !1glutamate dehydrogenase gene of Peptostreptococcus !1asaccharolyticus. !$#cross-references MUID:92011378; PMID:1917850 !$#accession A38168 !'##molecule_type DNA !'##residues 1-421 ##label SNE !'##cross-references GB:M76403; NID:g150669; PIDN:AAA25611.1; !1PID:g150670 CLASSIFICATION #superfamily glutamate dehydrogenase (NAD(P)+) KEYWORDS NAD; oxidoreductase FEATURE !$106 #binding_site substrate (Lys) #status predicted SUMMARY #length 421 #molecular-weight 46514 #checksum 4544 SEQUENCE /// ENTRY JN0854 #type complete TITLE glutamate dehydrogenase (EC 1.4.1.2) - Pyrococcus furiosus ALTERNATE_NAMES glutamic dehydrogenase; NAD-specific glutamate dehydrogenase ORGANISM #formal_name Pyrococcus furiosus DATE 10-Mar-1994 #sequence_revision 05-May-2000 #text_change 05-May-2000 ACCESSIONS T46971; JN0854 REFERENCE Z24328 !$#authors de Vos, W.M.; van der Oost, J. !$#submission submitted to the EMBL Data Library, March 1999 !$#accession T46971 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-420 ##label DEV !'##cross-references EMBL:M97860; PIDN:AAA83390.1 !'##experimental_source DSM 3638 REFERENCE JN0854 !$#authors Eggen, R.I.L.; Geerling, A.C.M.; Waldkoetter, K.; !1Antranikian, G.; de Vos, W.M. !$#journal Gene (1993) 132:143-148 !$#title The glutamate dehydrogenase-encoding gene of the !1hyperthermophilic archaeon Pyrococcus furiosus: Sequence, !1transcription and analysis of the deduced amino acid !1sequence. !$#cross-references MUID:94010338; PMID:8406037 !$#accession JN0854 !'##molecule_type DNA !'##residues 1-281,'K',283-420 ##label EGG GENETICS !$#gene gdh CLASSIFICATION #superfamily glutamate dehydrogenase (NAD(P)+) KEYWORDS NAD; oxidoreductase FEATURE !$105 #binding_site substrate (Lys) #status predicted SUMMARY #length 420 #molecular-weight 47114 #checksum 5304 SEQUENCE /// ENTRY F65112 #type complete TITLE glutamate synthase (NADPH) (EC 1.4.1.13) large chain precursor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 18-Feb-2000 #sequence_revision 18-Feb-2000 #text_change 08-Sep-2002 ACCESSIONS F65112; A29617; I41239; I41240 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65112 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1517 ##label BLAT !'##cross-references GB:AE000400; GB:U00096; NID:g2367203; !1PIDN:AAC76244.1; PID:g1789605; UWGP:b3212 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A91585 !$#authors Oliver, G.; Gosset, G.; Sanchez-Pescador, R.; Lozoya, E.; !1Ku, L.M.; Flores, N.; Becerril, B.; Valle, F.; Bolivar, F. !$#journal Gene (1987) 60:1-11 !$#title Determination of the nucleotide sequence for the glutamate !1synthase structural genes of Escherichia coli K-12. !$#cross-references MUID:88152492; PMID:3326786 !$#accession A29617 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-104,'LAFR',110-139,'N',141-219,221,'VCRRIC',228, !1'VLSGSCGPASGM',241-258,'WRNRSAIWRITVKSTPSPVTANG',283-459, !1'K',461-573,'T',575-862,'H',864-1285,'DARRS',1291-1372,'A', !11374-1375,'R',1377-1517 ##label OLI !'##cross-references GB:M18747; NID:g146207; PIDN:AAA23904.1; !1PID:g146208 !'##experimental_source strain K-12 REFERENCE I41239 !$#authors Velazquez, L.; Camarena, L.; Reyes, J.L.; Bastarrachea, F. !$#journal J. Bacteriol. (1991) 173:3261-3264 !$#title Mutations affecting the Shine-Dalgarno sequences of the !1untranslated region of the Escherichia coli gltBDF operon. !$#cross-references MUID:91217005; PMID:1673677 !$#accession I41239 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-258,'WRNRSAIWRITVKSTPSPVTANG',283-304 ##label VEL1 !'##cross-references GB:M68876; NID:g146210; PIDN:AAA23906.1; !1PID:g146211 !$#accession I41240 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 32-258,'WRNRSAIWRITVKSTPSPVTANG',283-304 ##label VEL2 !'##cross-references GB:M68876; NID:g146210; PIDN:AAA23907.1; !1PID:g146212 GENETICS !$#gene gltB !$#map_position 69 min CLASSIFICATION #superfamily glutamate synthase (NADPH) KEYWORDS 3Fe-4S; flavoprotein; glutamate biosynthesis; iron-sulfur !1protein; metalloprotein; NADP; oxidoreductase FEATURE !$1-42 #domain propeptide #status predicted #label PRO\ !$43-1517 #product glutamate synthase (NADPH) large chain !8#status predicted #label MAT\ !$43 #active_site Cys #status predicted\ !$1133,1139,1144 #binding_site 3Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 1517 #molecular-weight 166708 #checksum 6315 SEQUENCE /// ENTRY JQ1977 #type complete TITLE glutamate synthase (NADH2) (EC 1.4.1.14) precursor [validated] - alfalfa ORGANISM #formal_name Medicago sativa #common_name alfalfa DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS JQ1977; PQ0551 REFERENCE JQ1977 !$#authors Gregerson, R.G.; Miller, S.S.; Twary, S.N.; Gantt, J.S.; !1Vance, C.P. !$#journal Plant Cell (1993) 5:215-226 !$#title Molecular characterization of NADH-dependent glutamate !1synthase from alfalfa nodules. !$#cross-references MUID:93200806; PMID:8453303 !$#accession JQ1977 !'##molecule_type mRNA !'##residues 1-2194 ##label GRE !'##cross-references GB:L01660; NID:g166411; PIDN:AAB46617.1; !1PID:g166412 !$#accession PQ0551 !'##molecule_type protein !'##residues 102-114 ##label GR2 COMMENT This enzyme catalyzes the reductive transfer of the amido !1group of glutamine to the alpha-keto position of !12-oxoglutarate, resulting in the formation of two molecules !1of glutamate. CLASSIFICATION #superfamily glutamate synthase (NADH) KEYWORDS 3Fe-4S; chloroplast; iron-sulfur protein; metalloprotein; !1NAD; oxidoreductase FEATURE !$1-101 #domain propeptide #status predicted #label PRO\ !$102-2194 #product glutamate synthase (NADH) #status !8experimental #label MAT\ !$102 #active_site Cys #status predicted\ !$1246,1252,1257 #binding_site 3Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 2194 #molecular-weight 240372 #checksum 1127 SEQUENCE /// ENTRY B69962 #type complete TITLE probable leucine dehydrogenase (EC 1.4.1.9) yqiT - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS B69962 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69962 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-364 ##label KUN !'##cross-references GB:Z99116; GB:AL009126; NID:g2634723; !1PIDN:CAB14339.1; PID:g2634842 !'##experimental_source strain 168 GENETICS !$#gene yqiT CLASSIFICATION #superfamily leucine dehydrogenase KEYWORDS oxidoreductase SUMMARY #length 364 #molecular-weight 39992 #checksum 4999 SEQUENCE /// ENTRY A31950 #type complete TITLE leucine dehydrogenase (EC 1.4.1.9) - Bacillus stearothermophilus ORGANISM #formal_name Bacillus stearothermophilus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A31950 REFERENCE A31950 !$#authors Nagata, S.; Tanizawa, K.; Esaki, N.; Sakamoto, Y.; Ohshima, !1T.; Tanaka, H.; Soda, K. !$#journal Biochemistry (1988) 27:9056-9062 !$#title Gene cloning and sequence determination of leucine !1dehydrogenase from Bacillus stearothermophilus and !1structural comparison with other NAD(P)+-dependent !1dehydrogenases. !$#cross-references MUID:89166517; PMID:3069133 !$#accession A31950 !'##molecule_type DNA !'##residues 1-429 ##label NAG !'##cross-references GB:M22977; GB:M21477; NID:g143145; PIDN:AAA22570.1; !1PID:g143146 CLASSIFICATION #superfamily leucine dehydrogenase KEYWORDS oxidoreductase SUMMARY #length 429 #molecular-weight 46903 #checksum 3371 SEQUENCE /// ENTRY A54038 #type complete TITLE phenylalanine dehydrogenase (EC 1.4.1.20) - Rhodococcus sp. ORGANISM #formal_name Rhodococcus sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A54038 REFERENCE A54038 !$#authors Brunhuber, N.M.W.; Banerjee, A.; Jacobs Jr., W.R.; !1Blanchard, J.S. !$#journal J. Biol. Chem. (1994) 269:16203-16211 !$#title Cloning, sequencing, and expression of Rhodococcus !1L-phenylalanine dehydrogenase. Sequence comparisons to !1amino-acid dehydrogenases. !$#cross-references MUID:94266809; PMID:8206922 !$#accession A54038 !'##status preliminary !'##molecule_type mRNA !'##residues 1-356 ##label BRU !'##cross-references GB:U08381; NID:g475595; PIDN:AAA21461.1; !1PID:g475596 CLASSIFICATION #superfamily leucine dehydrogenase KEYWORDS NAD; oxidoreductase SUMMARY #length 356 #molecular-weight 36609 #checksum 344 SEQUENCE /// ENTRY S20286 #type complete TITLE glutamate dehydrogenase [NAD(P)] (EC 1.4.1.3) - Sulfolobus solfataricus ORGANISM #formal_name Sulfolobus solfataricus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S20286 REFERENCE S20286 !$#authors Maras, B.; Consalvi, V.; Chiaraluce, R.; Politi, L.; de !1Rosa, M.; Bossa, F.; Scandurra, R.; Barra, D. !$#journal Eur. J. Biochem. (1992) 203:81-87 !$#title The protein sequence of glutamate dehydrogenase from !1Sulfolobus solfataricus, a thermoacidophilic !1archaebacterium. Is the presence of N-epsilon-methyllysine !1related to thermostability? !$#cross-references MUID:92111588; PMID:1730244 !$#accession S20286 !'##molecule_type protein !'##residues 1-421 ##label MAR !'##note the sequence from Fig. 3 is inconsistent with that from Fig. 1 !1in having an additional Ala after 415-Met CLASSIFICATION #superfamily leucine dehydrogenase KEYWORDS methylated amino acid; NAD; oxidoreductase FEATURE !$254,260,372,391, !$392,393 #modified_site N6-methyllysine (Lys) #status !8predicted SUMMARY #length 421 #molecular-weight 46157 #checksum 7702 SEQUENCE /// ENTRY OXPGDA #type complete TITLE D-amino-acid oxidase (EC 1.4.3.3) - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 13-Aug-1999 ACCESSIONS A29598; B29598; A27209; A92383; S02656; A00383 REFERENCE A29598 !$#authors Jacobs, P.; Brockly, F.; Massaer, M.; Loriau, R.; Guillaume, !1J.P.; Ciccarelli, E.; Heinderyckx, M.; Cravador, A.; !1Biemans, R.; van Elsen, A.; Herzog, A.; Bollen, A. !$#journal Gene (1987) 59:55-61 !$#title Porcine D-amino acid oxidase: determination of the mRNA !1nucleotide sequence by the characterization of genomic and !1cDNA clones. !$#cross-references MUID:88137946; PMID:2893757 !$#accession A29598 !'##molecule_type DNA !'##residues 1-151 ##label JAC !$#accession B29598 !'##molecule_type mRNA !'##residues 100-347 ##label JA2 REFERENCE A27209 !$#authors Fukui, K.; Watanabe, F.; Shibata, T.; Miyake, Y. !$#journal Biochemistry (1987) 26:3612-3618 !$#title Molecular cloning and sequence analysis of cDNAs encoding !1porcine kidney D-amino acid oxidase. !$#cross-references MUID:88000568; PMID:2888479 !$#accession A27209 !'##molecule_type mRNA !'##residues 1-347 ##label FUK REFERENCE A92383 !$#authors Ronchi, S.; Minchiotti, L.; Galliano, M.; Curti, B.; !1Swenson, R.P.; Williams Jr., C.H.; Massey, V. !$#journal J. Biol. Chem. (1982) 257:8824-8834 !$#title The primary structure of D-amino acid oxidase from pig !1kidney. II. Isolation and sequence of overlap peptides and !1the complete sequence. !$#cross-references MUID:82239363; PMID:6124543 !$#accession A92383 !'##molecule_type protein !'##residues 1-347 ##label RON !'##experimental_source kidney REFERENCE S02656 !$#authors Nicholson, B.H.; Batra, S.P. !$#journal Biochem. J. (1988) 255:907-912 !$#title Structural interpretation of the binding of 9-azidoacridine !1to D-amino acid oxidase. !$#cross-references MUID:89105024; PMID:2905598 !$#accession S02656 !'##molecule_type protein !'##residues 1-45,'A',47-191,'D',193-347 ##label NIC REFERENCE A92359 !$#authors Swenson, R.P.; Williams Jr., C.H.; Massey, V. !$#journal J. Biol. Chem. (1982) 257:1937-1944 !$#title Chemical modification of D-amino acid oxidase. Amino acid !1sequence of the tryptic peptides containing tyrosine and !1lysine residues modified by fluorodinitrobenzene. !$#cross-references MUID:82120157; PMID:6120171 !$#contents annotation; active site REFERENCE A92423 !$#authors Swenson, R.P.; Williams Jr., C.H.; Massey, V. !$#journal J. Biol. Chem. (1983) 258:497-502 !$#title Identification of the histidine residue in D-amino acid !1oxidase that is covalently modified during inactivation by !15-dimethylaminonaphthalene-1-sulfonyl chloride. !$#cross-references MUID:83082913; PMID:6129252 !$#contents annotation; active site COMMENT The active enzyme contains a noncovalently bound FAD; it !1catalyzes the oxidation of a number of D-amino acids to the !1corresponding imino acids, which are than hydrolyzed !1nonenzymatically to alpha-keto acids. Oxygen, the electron !1acceptor, is converted to hydrogen peroxide. GENETICS !$#gene DAO !$#introns 65/2; 103/3; 129/2; 151/2 CLASSIFICATION #superfamily D-amino-acid oxidase KEYWORDS oxidoreductase FEATURE !$345-347 #region peroxisome/glyoxysome location signal !8(S-[RKH]-L) motif\ !$55,204,217 #active_site Tyr, Lys, His #status experimental SUMMARY #length 347 #molecular-weight 39335 #checksum 2700 SEQUENCE /// ENTRY S01340 #type complete TITLE D-amino-acid oxidase (EC 1.4.3.3) - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S01340 REFERENCE S01340 !$#authors Momoi, K.; Fukui, K.; Watanabe, F.; Miyake, Y. !$#journal FEBS Lett. (1988) 238:180-184 !$#title Molecular cloning and sequence analysis of cDNA encoding !1human kidney D-amino acid oxidase. !$#cross-references MUID:89005666; PMID:2901986 !$#accession S01340 !'##molecule_type mRNA !'##residues 1-347 ##label MOM !'##cross-references EMBL:X13227 GENETICS !$#gene GDB:DAO !'##cross-references GDB:135365; OMIM:124050 !$#map_position 12q24-12q24 CLASSIFICATION #superfamily D-amino-acid oxidase KEYWORDS oxidoreductase FEATURE !$345-347 #region peroxisome/glyoxysome location signal !8(S-[RKH]-L) motif\ !$55,204,217 #active_site Tyr, Lys, His #status predicted SUMMARY #length 347 #molecular-weight 39389 #checksum 7827 SEQUENCE /// ENTRY JX0132 #type complete TITLE D-amino-acid oxidase (EC 1.4.3.3) - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS JX0132 REFERENCE JX0132 !$#authors Momoi, K.; Fukui, K.; Tada, M.; Miyake, Y. !$#journal J. Biochem. (1990) 108:406-413 !$#title Gene expression of D-amino acid oxidase in rabbit kidney. !$#cross-references MUID:91115787; PMID:1980495 !$#accession JX0132 !'##status preliminary !'##molecule_type mRNA !'##residues 1-347 ##label MOM !'##cross-references GB:D12494; NID:g217719; PIDN:BAA02058.1; !1PID:g217720 CLASSIFICATION #superfamily D-amino-acid oxidase KEYWORDS oxidoreductase FEATURE !$345-347 #region peroxisome/glyoxysome location signal !8(S-[RKH]-L) motif\ !$55,204,217 #active_site Tyr, Lys, His #status predicted SUMMARY #length 347 #molecular-weight 38590 #checksum 29 SEQUENCE /// ENTRY JH0185 #type complete TITLE D-amino-acid oxidase (EC 1.4.3.3) - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JH0185 REFERENCE JH0185 !$#authors Tada, M.; Fukui, K.; Momoi, K.; Miyake, Y. !$#journal Gene (1990) 90:293-297 !$#title Cloning and expression of a cDNA encoding mouse kidney !1D-amino acid oxidase. !$#cross-references MUID:90382679; PMID:1976103 !$#accession JH0185 !'##molecule_type mRNA !'##residues 1-345 ##label TAD !'##cross-references GB:M32299; NID:g198571; PIDN:AAA39367.1; !1PID:g198572 !'##experimental_source kidney, strain BALB/c COMMENT D-Amino-acid oxidase is a flavoprotein associated with FAD !1which catalyzes the oxidative deamination of D-amino acid. CLASSIFICATION #superfamily D-amino-acid oxidase KEYWORDS oxidoreductase FEATURE !$7-12 #domain FAD binding #status predicted #label FAD\ !$343-345 #region peroxisome/glyoxysome location signal !8(S-[RKH]-L) motif\ !$54,209,215 #active_site Tyr, Lys, His #status predicted SUMMARY #length 345 #molecular-weight 38699 #checksum 8704 SEQUENCE /// ENTRY S75844 #type complete TITLE pyridoxamine-phosphate oxidase (EC 1.4.3.5) - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES flavin-associated protein A ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S75844; S52649 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75844 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-230 ##label KAN !'##cross-references EMBL:D90913; GB:AB001339; NID:g1653348; !1PIDN:BAA18303.1; PID:g1653389 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 REFERENCE S52649 !$#authors Sakamoto, T.; Los, D.A.; Higashi, S.; Wada, H.; Nishida, I.; !1Ohmori, M.; Murata, N. !$#journal Plant Mol. Biol. (1994) 26:249-263 !$#title Cloning of omega-3 desaturase from cyanobacteria and its use !1in altering the degree of membrane-lipid unsaturation. !$#cross-references MUID:95035996; PMID:7524725 !$#accession S52649 !'##status preliminary; translation not shown !'##molecule_type DNA !'##residues 194-230 ##label SAK !'##cross-references GB:D13780; NID:g600596; PIDN:BAA02923.1; !1PID:g600597 CLASSIFICATION #superfamily pyridoxamine-phosphate oxidase KEYWORDS oxidoreductase SUMMARY #length 230 #molecular-weight 26404 #checksum 2581 SEQUENCE /// ENTRY S41301 #type complete TITLE pyridoxamine-phosphate oxidase (EC 1.4.3.5) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YBR0321; protein YBR035c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-Nov-1999 ACCESSIONS S41301; S46564; S45891; S45893; A56147 REFERENCE S41301 !$#authors Loubbardi, A.; Karst, F.; Guilloton, M. !$#submission submitted to the EMBL Data Library, December 1993 !$#description Cloning and sequencing the PDX3 gene encoding pyridoxine !1(pyridoxamine) phosphate oxidase in Saccharomyces !1cerevisiae. !$#accession S41301 !'##molecule_type DNA !'##residues 1-228 ##label LOU !'##cross-references EMBL:X76992; NID:g440579; PIDN:CAA54295.1; !1PID:g440580 REFERENCE S46551 !$#authors Smits, P.H.M.; de Haan, M.; Maat, C.; Grivell, L.A. !$#journal Yeast (1994) 10(Suppl.A):S75-S80 !$#title The complete sequence of a 33 kb fragment on the right arm !1of chromosome II from Saccharomyces cerevisiae reveals 16 !1open reading frames, including ten new open reading frames, !1five previously identified genes and a homologue of the SCO1 !1gene. !$#cross-references MUID:94378725; PMID:8091864 !$#accession S46564 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-228 ##label SMI !'##cross-references EMBL:X76078; NID:g498748; PIDN:CAA53690.1; !1PID:g498762 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1993 REFERENCE S45875 !$#authors Grivell, L.A.; de Haan, M.; Maat, M.J.; Smits, P.H.M. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S45891 !'##molecule_type DNA !'##residues 1-228 ##label GRI !'##cross-references EMBL:Z35904; NID:g536251; PIDN:CAA84977.1; !1PID:g536252; GSPDB:GN00002; MIPS:YBR035c REFERENCE S45893 !$#authors Andre, B.; Cziepluch, C.; Hein, C.; Jauniaux, J.C.; !1Urrestarazu, A.; Vissers, S. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S45893 !'##molecule_type DNA !'##residues 1-228 ##label AND !'##cross-references EMBL:Z35904; NID:g536251; PIDN:CAA84977.1; !1PID:g536252; GSPDB:GN00002; MIPS:YBR035c REFERENCE A56147 !$#authors Loubbardi, A.; Marcireau, C.; Karst, F.; Guilloton, M. !$#journal J. Bacteriol. (1995) 177:1817-1823 !$#title Sterol uptake induced by an impairment of pyridoxal !1phosphate synthesis in Saccharomyces cerevisiae: cloning and !1sequencing of the PDX3 gene encoding pyridoxine !1(pyridoxamine) phosphate oxidase. !$#cross-references MUID:95204349; PMID:7896706 !$#accession A56147 !'##molecule_type DNA !'##residues 1-228 ##label LOW !'##cross-references GB:X76992; NID:g440579; PIDN:CAA54295.1; !1PID:g440580 GENETICS !$#gene SGD:PDX3; MIPS:YBR035c !'##cross-references SGD:S0000239; MIPS:YBR035c !$#map_position 2R !$#note YBR035c CLASSIFICATION #superfamily pyridoxamine-phosphate oxidase KEYWORDS oxidoreductase SUMMARY #length 228 #molecular-weight 26908 #checksum 4734 SEQUENCE /// ENTRY H64098 #type complete TITLE probable pyridoxamine-phosphate oxidase (EC 1.4.3.5) HI0863 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS H64098 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession H64098 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-229 ##label TIGR !'##cross-references GB:U32768; GB:L42023; NID:g1573878; !1PIDN:AAC22522.1; PID:g1573880; TIGR:HI0863 CLASSIFICATION #superfamily pyridoxamine-phosphate oxidase KEYWORDS oxidoreductase SUMMARY #length 229 #molecular-weight 26766 #checksum 8312 SEQUENCE /// ENTRY S36092 #type complete TITLE pyridoxamine-phosphate oxidase (EC 1.4.3.5) fprA - Myxococcus xanthus ALTERNATE_NAMES fprA protein ORGANISM #formal_name Myxococcus xanthus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S36092 REFERENCE S36091 !$#authors Hagen, T.J.; Shimkets, L.J. !$#journal J. Bacteriol. (1990) 172:15-23 !$#title Nucleotide sequence and transcriptional products of the csg !1locus of Myxococcus xanthus. !$#cross-references MUID:90094211; PMID:2152896 !$#accession S36092 !'##molecule_type DNA !'##residues 1-220 ##label HAG !'##cross-references EMBL:M29288 GENETICS !$#gene fprA !$#start_codon GTG CLASSIFICATION #superfamily pyridoxamine-phosphate oxidase KEYWORDS oxidoreductase SUMMARY #length 220 #molecular-weight 25284 #checksum 1274 SEQUENCE /// ENTRY B43261 #type complete TITLE pyridoxamine-phosphate oxidase (EC 1.4.3.5) pdxH - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS B43261; H64920 REFERENCE A43261 !$#authors Lam, H.M.; Winkler, M.E. !$#journal J. Bacteriol. (1992) 174:6033-6045 !$#title Characterization of the complex pdxH-tyrS operon of !1Escherichia coli K-12 and pleiotropic phenotypes caused by !1pdxH insertion mutations. !$#cross-references MUID:93015640; PMID:1356963 !$#accession B43261 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-218 ##label LAM !'##cross-references GB:M92351; NID:g148095; PIDN:AAA24709.1; !1PID:g148097 !'##experimental_source K-12 !'##note sequence extracted from NCBI backbone (NCBIP:115106) REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64920 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-218 ##label BLAT !'##cross-references GB:AE000259; GB:U00096; NID:g1787921; !1PIDN:AAC74710.1; PID:g1787926; UWGP:b1638 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene pdxH FUNCTION !$#description catalyzes the oxidation of pyridoxamine-5-phosphate to !1pyridoxal-5-phosphate and ammonia !$#pathway vitamin b6 metabolism CLASSIFICATION #superfamily pyridoxamine-phosphate oxidase KEYWORDS flavoprotein; oxidoreductase SUMMARY #length 218 #molecular-weight 25545 #checksum 5260 SEQUENCE /// ENTRY OXHUL #type complete TITLE protein-lysine 6-oxidase (EC 1.4.3.13) precursor - human ALTERNATE_NAMES lysyl oxidase ORGANISM #formal_name Homo sapiens #common_name man DATE 05-Jun-1992 #sequence_revision 06-Sep-1996 #text_change 11-Jun-1999 ACCESSIONS A47529; A40557; S23515; A56113; I55361 REFERENCE A47529 !$#authors Haemaelaeinen, E.R.; Kemppainen, R.; Pihlajaniemi, T.; !1Kivirikko, K.I. !$#journal Genomics (1993) 17:544-548 !$#title Structure of the human lysyl oxidase gene. !$#cross-references MUID:94063892; PMID:7902322 !$#accession A47529 !'##molecule_type DNA !'##residues 1-213 ##label HAE !'##cross-references GB:L16895; NID:g292923; PIDN:AAA16870.1; !1PID:g292924 !'##experimental_source leukocyte !'##note sequence extracted from NCBI backbone (NCBIN:139692, !1NCBIP:140196) REFERENCE A40557 !$#authors Haemaelaeinen, E.R.; Jones, T.A.; Sheer, D.; Taskinen, K.; !1Pihlajaniemi, T.; Kivirikko, K.I. !$#journal Genomics (1991) 11:508-516 !$#title Molecular cloning of human lysyl oxidase and assignment of !1the gene to chromosome 5q23.3-31.2. !$#cross-references MUID:92128932; PMID:1685472 !$#accession A40557 !'##molecule_type mRNA !'##residues 1-303,'LY',306-314,'W',316-417 ##label HA2 !'##cross-references GB:S78694; NID:g244145; PIDN:AAB21243.1; !1PID:g244146 REFERENCE S23515 !$#authors Mariani, T.J.; Trackman, P.C.; Kagan, H.M.; Eddy, R.L.; !1Shows, T.B.; Boyd, C.D.; Deak, S.B. !$#journal Matrix (1992) 12:242-248 !$#title The complete derived amino acid sequence of human lysyl !1oxidase and assignment of the gene to chromosome 5. !1(Extensive sequence homology with the murine RAS recision !1gene). !$#cross-references MUID:93024096; PMID:1357535 !$#accession S23515 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-101,'A',103-136,'R',138,'A',140-417 ##label MAR !'##cross-references GB:S45875; NID:g257064; PIDN:AAB23549.1; !1PID:g257065 REFERENCE A56113 !$#authors Kim, Y.; Boyd, C.D.; Csiszar, K. !$#journal J. Biol. Chem. (1995) 270:7176-7182 !$#title A new gene with sequence and structural similarity to the !1gene encoding human lysyl oxidase. !$#cross-references MUID:95221367; PMID:7706256 !$#accession A56113 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 201-417 ##label KIM !'##cross-references GB:S77920; NID:g998583 REFERENCE I55361 !$#authors Svinarich, D.M.; Twomey, T.A.; Macauley, S.P.; Krebs, C.J.; !1Yang, T.P.; Krawetz, S.A. !$#journal J. Biol. Chem. (1992) 267:14382-14387 !$#title Characterization of the human lysyl oxidase gene locus. !$#cross-references MUID:92332554; PMID:1352776 !$#accession I55361 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 55-101,'A',103-138,'A',140-216 ##label RES !'##cross-references GB:M84150; NID:g187277; PIDN:AAA59541.1; !1PID:g187278 GENETICS !$#gene GDB:LOX !'##cross-references GDB:119367; OMIM:153455 !$#map_position 5q23.3-5q31.2 !$#introns 211/1; 247/2; 293/2; 345/3; 377/3; 416/2 FUNCTION !$#description using molecular oxygen catalyzes the oxidative deamination !1of peptidyl-lysine to peptidyl-allysine, ammonium and !1hydrogen peroxide !$#pathway collagen biosynthesis; elastin biosynthesis CLASSIFICATION #superfamily protein-lysine 6-oxidase KEYWORDS blocked amino end; copper; extracellular protein; !1glycoprotein; oxidoreductase; quinoprotein; topaquinone FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-168 #domain propeptide #status predicted #label PRO\ !$169-417 #product protein-lysine 6-oxidase #status predicted !8#label MAT\ !$81,97,144 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$169 #modified_site blocked amino end (Asp) (in mature !8form) #status predicted\ !$320-355 #cross-link lysine-topaquinone (Lys-Tyr) #status !8predicted\ !$355 #modified_site topaquinone (Tyr) #status predicted SUMMARY #length 417 #molecular-weight 46956 #checksum 6652 SEQUENCE /// ENTRY A48501 #type complete TITLE probable protein-lysine 6-oxidase (EC 1.4.3.13) precursor - human ALTERNATE_NAMES lysyl oxidase homolog ORGANISM #formal_name Homo sapiens #common_name man DATE 21-Jan-2000 #sequence_revision 21-Jan-2000 #text_change 21-Jan-2000 ACCESSIONS A48501 REFERENCE A48501 !$#authors Kenyon, K.; Modi, W.S.; Contente, S.; Friedman, R.M. !$#journal J. Biol. Chem. (1993) 268:18435-18437 !$#title A novel human cDNA with a predicted protein similar to lysyl !1oxidase maps to chromosome 15q24-q25. !$#cross-references MUID:93366738; PMID:7689553 !$#accession A48501 !'##molecule_type mRNA !'##residues 1-574 ##label KEN !'##cross-references GB:L21186; NID:g307145; PIDN:AAA50162.1; !1PID:g307146 !'##experimental_source umbilical artery GENETICS !$#gene GDB:LOXL !'##cross-references GDB:228067; OMIM:153456 !$#map_position 15q24-15q25 CLASSIFICATION #superfamily protein-lysine 6-oxidase KEYWORDS oxidoreductase; quinoprotein; topaquinone FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$477-512 #cross-link lysine-topaquinone (Lys-Tyr) #status !8predicted\ !$512 #modified_site topaquinone (Tyr) #status predicted SUMMARY #length 574 #molecular-weight 63066 #checksum 2979 SEQUENCE /// ENTRY OXMSL #type complete TITLE protein-lysine 6-oxidase (EC 1.4.3.13) precursor - mouse ALTERNATE_NAMES lysyl oxidase ORGANISM #formal_name Mus musculus #common_name house mouse DATE 02-Jul-1996 #sequence_revision 06-Sep-1996 #text_change 11-Jun-1999 ACCESSIONS A47005; I59555 REFERENCE A47005 !$#authors Contente, S.; Csiszar, K.; Kenyon, K.; Friedman, R.M. !$#journal Genomics (1993) 16:395-400 !$#title Structure of the mouse lysyl oxidase gene. !$#cross-references MUID:93300513; PMID:8100214 !$#accession A47005 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-411 ##label RES !'##cross-references GB:L04262; NID:g198956; PIDN:AAA99899.1; !1PID:g459877 REFERENCE I59555 !$#authors Kenyon, K.; Contente, S.; Trackman, P.C.; Tang, J.; Kagan, !1H.M.; Friedman, R.M. !$#journal Science (1991) 253:802 !$#title Lysyl oxidase and rrg messenger RNA. !$#cross-references MUID:91343916; PMID:1678898 !$#accession I59555 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 294-332,'A',334-411 ##label RE2 !'##cross-references GB:M65143; NID:g500626; PIDN:AAA20185.1; !1PID:g198958 GENETICS !$#introns 205/1; 241/2; 287/2; 339/3; 371/3; 410/2 FUNCTION !$#description using molecular oxygen catalyzes the oxidative deamination !1of peptidyl-lysine to peptidyl-allysine, ammonium and !1hydrogen peroxide !$#pathway collagen biosynthesis; elastin biosynthesis CLASSIFICATION #superfamily protein-lysine 6-oxidase KEYWORDS blocked amino end; copper; extracellular protein; !1glycoprotein; oxidoreductase; quinoprotein; topaquinone FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-162 #domain propeptide #status predicted #label PRO\ !$163-411 #product protein-lysine 6-oxidase #status predicted !8#label MAT\ !$91,138 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$163 #modified_site blocked amino end (Asp) (in mature !8form) #status predicted\ !$314-349 #cross-link lysine-topaquinone (Lys-Tyr) #status !8predicted\ !$349 #modified_site topaquinone (Tyr) #status predicted SUMMARY #length 411 #molecular-weight 46686 #checksum 5206 SEQUENCE /// ENTRY OXRTL #type complete TITLE protein-lysine 6-oxidase (EC 1.4.3.13) precursor - rat ALTERNATE_NAMES lysyl oxidase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 03-Aug-1992 #sequence_revision 06-Sep-1996 #text_change 21-Jan-2000 ACCESSIONS B40557; A30352; A40290 REFERENCE A40557 !$#authors Haemaelaeinen, E.R.; Jones, T.A.; Sheer, D.; Taskinen, K.; !1Pihlajaniemi, T.; Kivirikko, K.I. !$#journal Genomics (1991) 11:508-516 !$#title Molecular cloning of human lysyl oxidase and assignment of !1the gene to chromosome 5q23.3-31.2. !$#cross-references MUID:92128932; PMID:1685472 !$#accession B40557 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type mRNA !'##residues 1-411 ##label HAE REFERENCE A30352 !$#authors Trackman, P.C.; Pratt, A.M.; Wolanski, A.; Tang, S.S.; !1Offner, G.D.; Troxler, R.F.; Kagan, H.M. !$#journal Biochemistry (1990) 29:4863-4870 !$#title Cloning of rat aorta lysyl oxidase cDNA: complete codons and !1predicted amino acid sequence. !$#cross-references MUID:90304121; PMID:1973052 !$#accession A30352 !'##molecule_type mRNA !'##residues 1-74,'ATLQHSHARPFCCCVTTALPLPVRGLQAHLGSPRVVPGP', !1'QPATGSKLVSRRRGPAMEPQGAQ',138-161, !1'ATTPTIPTSTPTTTPIITTMTLMRD',188-411 ##label TRA !'##cross-references GB:J02903 !'##note this sequence has been corrected in reference A40290 REFERENCE A40290 !$#authors Trackman, P.C.; Pratt, A.M.; Wolanski, A.; Tang, S.S.; !1Offner, G.D.; Troxler, R.F.; Kagan, H.M. !$#journal Biochemistry (1991) 30:8282 !$#cross-references MUID:91329411; PMID:1678281 !$#contents erratum !$#accession A40290 !'##molecule_type mRNA !'##residues 1-210 ##label TR2 !'##cross-references GB:J02903; NID:g205226; PIDN:AAA41537.1; !1PID:g205227 !'##note the sequence was redetermined for only the residues indicated; !1in GenBank entry RATLOX, release 113.0, PIDN:AAA41537.1 !1applies to the complete, corrected sequence FUNCTION !$#description using molecular oxygen catalyzes the oxidative deamination !1of peptidyl-lysine to peptidyl-allysine, ammonium and !1hydrogen peroxide !$#pathway collagen biosynthesis; elastin biosynthesis CLASSIFICATION #superfamily protein-lysine 6-oxidase KEYWORDS blocked amino end; copper; extracellular protein; !1glycoprotein; oxidoreductase; quinoprotein; topaquinone FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-162 #domain propeptide #status predicted #label PRO\ !$163-411 #product protein-lysine 6-oxidase #status predicted !8#label MAT\ !$91,138 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$163 #modified_site blocked amino end (Asp) (in mature !8form) #status predicted\ !$314-349 #cross-link lysine-topaquinone (Lys-Tyr) #status !8predicted\ !$349 #modified_site topaquinone (Tyr) #status predicted SUMMARY #length 411 #molecular-weight 46558 #checksum 3802 SEQUENCE /// ENTRY DEPSNL #type complete TITLE amine dehydrogenase (EC 1.4.99.3) light chain - Methylobacterium extorquens ALTERNATE_NAMES methylamine dehydrogenase light chain ORGANISM #formal_name Methylobacterium extorquens DATE 14-Nov-1983 #sequence_revision 17-Nov-1995 #text_change 11-Jun-1999 ACCESSIONS A36676; A00384; B38123 REFERENCE A36676 !$#authors Chistoserdov, A.Y.; Tsygankov, Y.D.; Lidstrom, M.E. !$#journal Biochem. Biophys. Res. Commun. (1990) 172:211-216 !$#title Cloning and sequencing of the structural gene for the small !1subunit of methylamine dehydrogenase from Methylobacterium !1extorquens AM1: evidence for two tryptophan residues !1involved in the active center. !$#cross-references MUID:91025043; PMID:2121141 !$#accession A36676 !'##molecule_type DNA !'##residues 58-186 ##label CH3 !'##cross-references GB:M58517; NID:g150012; PIDN:AAA25379.1; !1PID:g150013; GB:M38387 REFERENCE A00384 !$#authors Ishii, Y.; Hase, T.; Fukumori, Y.; Matsubara, H.; Tobari, J. !$#journal J. Biochem. (1983) 93:107-119 !$#title Amino acid sequence studies of the light subunit of !1methylamine dehydrogenase from Pseudomonas AM1: existence of !1two residues binding the prosthetic group. !$#cross-references MUID:83186062; PMID:6841324 !$#accession A00384 !'##molecule_type protein !'##residues 58-73,'N',75-105,'L',107-111,'X',113-162,'X',164-186 !1##label IS2 !'##experimental_source AM1 !'##note 106-Lys was also found REFERENCE A38123 !$#authors Chistoserdov, A.Y.; Lidstrom, M.E. !$#journal J. Bacteriol. (1991) 173:5909-5913 !$#title The small-subunit polypeptide of methylamine dehydrogenase !1from Methylobacterium extorquens AM1 has an unusual leader !1sequence. !$#cross-references MUID:91358386; PMID:1885555 !$#accession B38123 !'##molecule_type DNA !'##residues 1-59 ##label CH2 !'##cross-references GB:M57963 COMMENT The active enzyme is a tetramer of two light and two heavy !1chains. CLASSIFICATION #superfamily amine dehydrogenase light chain KEYWORDS oxidoreductase; quinoprotein FEATURE !$112-163 #cross-link tryptophan-tryptophyl quinone (Trp-Trp) !8#status predicted\ !$112 #modified_site tryptophyl quinone (Trp) #status !8predicted SUMMARY #length 186 #molecular-weight 20084 #checksum 4765 SEQUENCE /// ENTRY JH0661 #type complete TITLE amine dehydrogenase (EC 1.4.99.3) small chain precursor - Paracoccus denitrificans ALTERNATE_NAMES methylamine dehydrogenase small chain precursor ORGANISM #formal_name Paracoccus denitrificans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JH0661; S12971 REFERENCE PH0856 !$#authors Chistoserdov, A.Y.; Boyd, J.; Mathews, F.S.; Lidstrom, M.E. !$#journal Biochem. Biophys. Res. Commun. (1992) 184:1181-1189 !$#title The genetic organization of the mau gene cluster of the !1facultative autotroph Paracoccus denitrificans. !$#cross-references MUID:92272706; PMID:1590782 !$#accession JH0661 !'##molecule_type DNA !'##residues 1-188 ##label CHI !'##cross-references GB:M90098; NID:g150580; PIDN:AAA25578.1; !1PID:g150582 REFERENCE S12971 !$#authors van Spanning, R.J.M.; Wansell, C.W.; Reijnders, W.N.M.; !1Oltmann, L.F.; Stouthamer, A.H. !$#journal FEBS Lett. (1990) 275:217-220 !$#title Mutagenesis of the gene encoding amicyanin of Paracoccus !1denitrificans and the resultant effect on methylamine !1oxidation. !$#cross-references MUID:91085564; PMID:2261991 !$#accession S12971 !'##status preliminary !'##molecule_type DNA !'##residues 158-188 ##label SPA !'##cross-references EMBL:X55665; NID:g45458; PIDN:CAA39198.1; !1PID:g45459 GENETICS !$#gene mauA CLASSIFICATION #superfamily amine dehydrogenase light chain KEYWORDS oxidoreductase; quinoprotein FEATURE !$1-57 #domain signal sequence #status predicted #label SIG\ !$58-188 #product amine dehydrogenase small chain #status !8predicted #label AMI\ !$80-145,86-118, !$93-178,95-143, !$103-134 #disulfide_bonds #status experimental\ !$114-165 #cross-link tryptophan-tryptophyl quinone (Trp-Trp) !8#status experimental\ !$114 #modified_site tryptophyl quinone (Trp) #status !8experimental SUMMARY #length 188 #molecular-weight 20393 #checksum 7572 SEQUENCE /// ENTRY RDECC #type complete TITLE pyrroline-5-carboxylate reductase (EC 1.5.1.2) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 01-Mar-2002 ACCESSIONS A00385; B64767 REFERENCE A00385 !$#authors Deutch, A.H.; Smith, C.J.; Rushlow, K.E.; Kretschmer, P.J. !$#journal Nucleic Acids Res. (1982) 10:7701-7714 !$#title Escherichia coli delta(1)-pyrroline-5-carboxylate reductase: !1gene sequence, protein overproduction and purification. !$#cross-references MUID:83116986; PMID:6296787 !$#accession A00385 !'##molecule_type DNA !'##residues 1-269 ##label DEU !'##cross-references GB:J01665; NID:g147358; PIDN:AAA86433.1; !1PID:g147359 !'##note parts of this sequence, including the amino and carboxyl ends !1of the mature protein, were confirmed by protein sequencing REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64767 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-269 ##label BLAT !'##cross-references GB:AE000145; GB:U00096; NID:g1786580; !1PIDN:AAC73489.1; PID:g1786585; UWGP:b0386 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene proC !$#map_position 9 min FUNCTION !$#description catalyzes reduction of pyrroline-5-carboxylate to proline !$#pathway proline biosynthesis !$#note third enzyme in the proline biosynthetic pathway CLASSIFICATION #superfamily pyrroline-5-carboxylate reductase KEYWORDS oxidoreductase; proline biosynthesis SUMMARY #length 269 #molecular-weight 28145 #checksum 442 SEQUENCE /// ENTRY F69602 #type complete TITLE pyrroline-5-carboxylate reductase homolog comER - Bacillus subtilis ALTERNATE_NAMES non-essential gene for competence comER CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS F69602; S39862 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69602 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-273 ##label KUN !'##cross-references GB:Z99117; GB:AL009126; NID:g2634966; !1PIDN:CAB14502.1; PID:g2635006 !'##experimental_source strain 168 REFERENCE S39862 !$#authors Hahn, J.; Inamine, G.; Kozlov, Y.; Dubnau, D. !$#journal Mol. Microbiol. (1993) 10:99-111 !$#title Characterization of comE, a late competence operon of !1Bacillus subtilis required for the binding and uptake of !1transforming DNA. !$#cross-references MUID:95058187; PMID:7968523 !$#accession S39862 !'##status preliminary !'##molecule_type DNA !'##residues 'MLSYADSTNSSCMFPAFVIFYFHNTYGLEDNSSKEGKPL',2-152,'QA', !1155-273 ##label HAH !'##cross-references EMBL:L15202; NID:g289258; PIDN:AAC36904.1; !1PID:g289259 GENETICS !$#gene comER CLASSIFICATION #superfamily pyrroline-5-carboxylate reductase KEYWORDS oxidoreductase SUMMARY #length 273 #molecular-weight 30239 #checksum 4780 SEQUENCE /// ENTRY F69855 #type complete TITLE pyrroline-5-carboxylate reductase homolog ykeA - Bacillus subtilis ALTERNATE_NAMES hypothetical protein X (dciAA 5' region) CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS F69855; S16646 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69855 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-272 ##label KUN !'##cross-references GB:Z99110; GB:AL009126; NID:g2633472; !1PIDN:CAB13148.1; PID:g2633645 !'##experimental_source strain 168 REFERENCE S16646 !$#authors Mathiopoulos, C.; Mueller, J.P.; Slack, F.J.; Murphy, C.G.; !1Patankar, S.; Bukusoglu, G.; Sonenshein, A.L. !$#journal Mol. Microbiol. (1991) 5:1903-1913 !$#title A Bacillus subtilis dipeptide transport system expressed !1early during sporulation. !$#cross-references MUID:92114768; PMID:1766370 !$#accession S16646 !'##status preliminary !'##molecule_type DNA !'##residues 247-272 ##label MAT !'##cross-references EMBL:X56678; NID:g48802; PIDN:CAA40001.1; !1PID:g48803 GENETICS !$#gene ykeA CLASSIFICATION #superfamily pyrroline-5-carboxylate reductase KEYWORDS oxidoreductase SUMMARY #length 272 #molecular-weight 30202 #checksum 9104 SEQUENCE /// ENTRY G69964 #type complete TITLE pyrroline-5-carboxylate reductase homolog yqjO - Bacillus subtilis CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS G69964 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69964 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-278 ##label KUN !'##cross-references GB:Z99116; GB:AL009126; NID:g2634723; !1PIDN:CAB14312.1; PID:g2634815 !'##experimental_source strain 168 GENETICS !$#gene yqjO CLASSIFICATION #superfamily pyrroline-5-carboxylate reductase KEYWORDS oxidoreductase SUMMARY #length 278 #molecular-weight 30396 #checksum 1554 SEQUENCE /// ENTRY S10186 #type complete TITLE pyrroline-5-carboxylate reductase (EC 1.5.1.2) - soybean ORGANISM #formal_name Glycine max #common_name soybean DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S10186 REFERENCE S10186 !$#authors Delauney, A.J.; Verma, D.P.S. !$#journal Mol. Gen. Genet. (1990) 221:299-305 !$#title A soybean gene encoding Delta1-pyrroline-5-carboxylate !1reductase was isolated by functional complementation in !1Escherichia coli and is found to be osmoregulated. !$#cross-references MUID:90340278; PMID:2199815 !$#accession S10186 !'##molecule_type mRNA !'##residues 1-274 ##label DEL !'##cross-references EMBL:X16352; NID:g18723; PIDN:CAA34401.1; !1PID:g18724 !'##note the authors translated the codon GAA for residue 115 as Pro and !1GTG for residue 125 as Pro CLASSIFICATION #superfamily pyrroline-5-carboxylate reductase KEYWORDS oxidoreductase; proline biosynthesis SUMMARY #length 274 #molecular-weight 28586 #checksum 3980 SEQUENCE /// ENTRY JQ2334 #type complete TITLE pyrroline-5-carboxylate reductase (EC 1.5.1.2) [similarity] - Arabidopsis thaliana ALTERNATE_NAMES protein T9L3_100 ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Sep-2000 ACCESSIONS JQ2334; T51425 REFERENCE JQ2334 !$#authors Verbruggen, N.; Villarroel, R.; Van Montagu, M. !$#journal Plant Physiol. (1993) 103:771-781 !$#title Osmoregulation of a pyrroline-5-carboxylate reductase gene !1in Arabidopsis thaliana. !$#cross-references MUID:94294559; PMID:8022935 !$#accession JQ2334 !'##molecule_type DNA !'##residues 1-276 ##label VER !'##cross-references GB:M76538; NID:g166814; PIDN:AAA61346.1; !1PID:g166815 REFERENCE Z25394 !$#authors Sato, S.; Nakamura, Y.; Kaneko, T.; Kato, T.; Asamizu, E.; !1Kotani, H.; Tabata, S.; Mewes, H.W.; Rudd, S.; Lemcke, K.; !1Mayer, K.F.X. !$#submission submitted to the Protein Sequence Database, August 2000 !$#accession T51425 !'##status preliminary !'##molecule_type DNA !'##residues 1-276 ##label SAT !'##cross-references EMBL:AL391149 !'##experimental_source cultivar Columbia; BAC clone T9L3 COMMENT This enzyme is involved in the last step of the proline !1biosynthetic pathway. GENETICS !$#map_position 5 !$#introns 67/3; 84/1; 114/3; 139/1; 179/2; 214/3 !$#note T9L3_100 CLASSIFICATION #superfamily pyrroline-5-carboxylate reductase KEYWORDS oxidoreductase; proline biosynthesis SUMMARY #length 276 #molecular-weight 28624 #checksum 8609 SEQUENCE /// ENTRY A41770 #type complete TITLE pyrroline-5-carboxylate reductase (EC 1.5.1.2) - human ALTERNATE_NAMES P5C reductase ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A41770 REFERENCE A41770 !$#authors Dougherty, K.M.; Brandriss, M.C.; Valle, D. !$#journal J. Biol. Chem. (1992) 267:871-875 !$#title Cloning human pyrroline-5-carboxylate reductase cDNA by !1complementation in Saccharomyces cerevisiae. !$#cross-references MUID:92112821; PMID:1730675 !$#accession A41770 !'##molecule_type mRNA !'##residues 1-319 ##label DOU !'##cross-references GB:M77836; NID:g189497; PIDN:AAA36407.1; !1PID:g189498 !'##note sequence extracted from NCBI backbone (NCBIN:75606, !1NCBIP:75608) GENETICS !$#gene GDB:PYCR1; P5C; PYCR !'##cross-references GDB:135716; OMIM:179035 !$#map_position 17pter-17qter CLASSIFICATION #superfamily pyrroline-5-carboxylate reductase KEYWORDS oxidoreductase; proline biosynthesis SUMMARY #length 319 #molecular-weight 33374 #checksum 6728 SEQUENCE /// ENTRY RDHUD #type complete TITLE dihydrofolate reductase (EC 1.5.1.3) [validated] - human ALTERNATE_NAMES DHFR ORGANISM #formal_name Homo sapiens #common_name man DATE 19-Feb-1984 #sequence_revision 23-Mar-1995 #text_change 15-Sep-2000 ACCESSIONS A22551; I37287; A00386 REFERENCE A22551 !$#authors Chen, M.J.; Shimada, T.; Moulton, A.D.; Cline, A.; !1Humphries, R.K.; Maizel, J.; Nienhuis, A.W. !$#journal J. Biol. Chem. (1984) 259:3933-3943 !$#title The functional human dihydrofolate reductase gene. !$#cross-references MUID:84162075; PMID:6323448 !$#accession A22551 !'##molecule_type DNA !'##residues 1-187 ##label CHE !'##cross-references GB:K01612; GB:M10235; NID:g182711 REFERENCE I37287 !$#authors Yang, J.K.; Masters, J.N.; Attardi, G. !$#journal J. Mol. Biol. (1984) 176:169-187 !$#title Human dihydrofolate reductase gene organization. Extensive !1conservation of the G + C-rich 5' non-coding sequence and !1strong intron size divergence from homologous mammalian !1genes. !$#cross-references MUID:84267838; PMID:6235374 !$#accession I37287 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-45 ##label YAN !'##cross-references EMBL:X00855; NID:g30776; PIDN:CAA25409.1; !1PID:g1617080 REFERENCE A00386 !$#authors Masters, J.N.; Attardi, G. !$#journal Gene (1983) 21:59-63 !$#title The nucleotide sequence of the cDNA coding for the human !1dihydrofolic acid reductase. !$#cross-references MUID:83183667; PMID:6687716 !$#accession A00386 !'##molecule_type mRNA !'##residues 2-187 ##label MAS !'##cross-references GB:V00507; NID:g30774; PIDN:CAA23765.1; PID:g30775 REFERENCE A50112 !$#authors Oefner, C.; D'Arcy, A.; Winkler, F.K. !$#submission submitted to the Brookhaven Protein Data Bank, August 1990 !$#cross-references PDB:1DRF !$#contents annotation; X-ray crystallography, 2.0 angstroms, residues !12-187 REFERENCE A44685 !$#authors Oefner, C.; D'Arcy, A.; Winkler, F.K. !$#journal Eur. J. Biochem. (1988) 174:377-385 !$#title Crystal structure of human dihydrofolate reductase complexed !1with folate. !$#cross-references MUID:88254806; PMID:3383852 !$#contents annotation; X-ray crystallography, 2.0 angstroms REFERENCE A44686 !$#authors Davies II, J.F.; Delcamp, T.V.; Prendergast, N.J.; Ashford, !1V.A.; Freisheim, J.H.; Kraut, J. !$#journal Biochemistry (1990) 29:9467-9479 !$#title Crystal structures of recombinant human dihydrofolate !1reductase complexed with folate and 5-deazafolate. !$#cross-references MUID:91064350; PMID:2248959 !$#contents annotation; X-ray crystallography, 2.3 angstroms GENETICS !$#gene GDB:DHFR !'##cross-references GDB:119845; OMIM:126060 !$#map_position 5q12-5q14 !$#introns 29/2; 46/1; 81/2; 123/3; 162/2 FUNCTION !$#description catalyzes the reduction of dihydrofolic acid to !1tetrahydrofolic acid with NADPH; oxidoreductase !$#pathway tetrahydrofolate synthesis CLASSIFICATION #superfamily type I dihydrofolate reductase; type I !1dihydrofolate reductase homology KEYWORDS NADP; oxidoreductase FEATURE !$2-187 #product dihydrofolate reductase #status experimental !8#label MAT\ !$4-126 #domain type I dihydrofolate reductase homology !8#label DFR\ !$31,35,65,71 #binding_site substrate (Glu, Phe, Asn, Arg) #status !8experimental SUMMARY #length 187 #molecular-weight 21453 #checksum 1737 SEQUENCE /// ENTRY RDMSD #type complete TITLE dihydrofolate reductase (EC 1.5.1.3), methotrexate-resistant - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 24-Apr-1984 #sequence_revision 13-Mar-1997 #text_change 16-Jun-2000 ACCESSIONS S13096; S13880; I48328; I49672; A92253; A90792; I49632; !1I49633; A21119; A00387 REFERENCE S13096 !$#authors McIvor, R.S.; Simonsen, C.C. !$#journal Nucleic Acids Res. (1990) 18:7025-7032 !$#title Isolation and characterization of a variant dihydrofolate !1reductase cDNA from methotrexate-resistant murine L5178Y !1cells. !$#cross-references MUID:91088280; PMID:2263462 !$#accession S13096 !'##molecule_type mRNA !'##residues 1-187 ##label MCI !'##cross-references EMBL:X56066 !'##note the authors did not translate the codon for residue 1 REFERENCE S13880 !$#authors Simonsen, C.C. !$#submission submitted to the EMBL Data Library, October 1990 !$#accession S13880 !'##molecule_type mRNA !'##residues 1-13,'D',15-187 ##label SIM !'##cross-references EMBL:X56066; NID:g50710; PIDN:CAA39544.1; !1PID:g50711 REFERENCE I48328 !$#authors Crouse, G.F.; Simonsen, C.C.; McEwan, R.N.; Schimke, R.T. !$#journal J. Biol. Chem. (1982) 257:7887-7897 !$#title Structure of amplified normal and variant dihydrofolate !1reductase genes in mouse sarcoma S180 cells. !$#cross-references MUID:82213979; PMID:6282858 !$#accession I48328 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-28 ##label RES !'##cross-references EMBL:V00735; NID:g50701; PIDN:CAA24113.1; !1PID:g1619305 REFERENCE I49672 !$#authors McGrogan, M.; Simonsen, C.C.; Smouse, D.T.; Farnham, P.J.; !1Schimke, R.T. !$#journal J. Biol. Chem. (1985) 260:2307-2314 !$#title Heterogeneity at the 5' termini of mouse dihydrofolate !1reductase mRNAs: Evidence for multiple promoter regions. !$#cross-references MUID:85130969; PMID:2982814 !$#accession I49672 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-3,'A',5-28 ##label RE2 !'##cross-references GB:M10071; NID:g193331; PIDN:AAA37637.1; !1PID:g553915 REFERENCE A92253 !$#authors Stone, D.; Paterson, S.J.; Raper, J.H.; Phillips, A.W. !$#journal J. Biol. Chem. (1979) 254:480-488 !$#title The amino acid sequence of dihydrofolate reductase from the !1mouse lymphoma L1210. !$#cross-references MUID:79109591; PMID:762074 !$#accession A92253 !'##molecule_type protein !'##residues 2-31,'F',33-122,'EQ',125-127,'E',129-173,'D',175-187 !1##label STO !'##experimental_source lymphoma L1210 cells REFERENCE A90792 !$#authors Nunberg, J.H.; Kaufman, R.J.; Chang, A.C.Y.; Cohen, S.N.; !1Schimke, R.T. !$#journal Cell (1980) 19:355-364 !$#title Structure and genomic organization of the mouse !1dihydrofolate reductase gene. !$#cross-references MUID:80132485; PMID:6244105 !$#accession A90792 !'##molecule_type mRNA !'##residues 2-24;50-127;154-187 ##label NUN !'##note the authors translated the codon GAG for residue 169 as Gly REFERENCE I49632 !$#authors Chang, A.C.Y.; Nunberg, J.; Kaufman, R.J.; Erlich, H.A.; !1Schimke, R.T.; Cohen, S.N. !$#journal Nature (1978) 275:617-624 !$#title Phenotypic expression in E.coli of a DNA sequence coding for !1mouse dihydrofolate reductase. !$#cross-references MUID:79032141; PMID:360074 !$#accession I49632 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-24 ##label RE3 !'##cross-references GB:M10722; NID:g192946; PIDN:AAA37524.1; !1PID:g192949 !$#accession I49633 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 50-122,'E',124-127 ##label RE4 !'##cross-references GB:M10811; NID:g192947; PIDN:AAA37525.1; !1PID:g192950 REFERENCE A21119 !$#authors Simonsen, C.C.; Levinson, A.D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:2495-2499 !$#title Isolation and expression of an altered mouse dihydrofolate !1reductase cDNA. !$#cross-references MUID:83195084; PMID:6573667 !$#accession A21119 !'##status preliminary !'##molecule_type mRNA !'##residues 2-22,'R',24-31,'F',33-187 ##label SI2 !'##cross-references GB:V00734; NID:g50699; PIDN:CAA24112.1; PID:g50700 CLASSIFICATION #superfamily type I dihydrofolate reductase; type I !1dihydrofolate reductase homology KEYWORDS methotrexate resistance; NADP; one-carbon metabolism; !1oxidoreductase FEATURE !$4-126 #domain type I dihydrofolate reductase homology !8#label DFR\ !$31,35,65,71 #binding_site substrate (Glu, Phe, Asn, Arg) #status !8predicted SUMMARY #length 187 #molecular-weight 21645 #checksum 2035 SEQUENCE /// ENTRY RDHY75 #type complete TITLE dihydrofolate reductase (EC 1.5.1.3) (antifolate-resistant variant) - Chinese hamster ORGANISM #formal_name Cricetulus griseus #common_name Chinese hamster DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 11-Jun-1999 ACCESSIONS A28274; I48104 REFERENCE A28274 !$#authors Melera, P.W.; Davide, J.P.; Oen, H. !$#journal J. Biol. Chem. (1988) 263:1978-1990 !$#title Antifolate-resistant Chinese hamster cells. Molecular basis !1for the biochemical and structural heterogeneity among !1dihydrofolate reductases produced by drug-sensitive and !1drug-resistant cell lines. !$#cross-references MUID:88115326; PMID:3339001 !$#accession A28274 !'##molecule_type mRNA !'##residues 1-186 ##label MEL !'##experimental_source antifolate-resistant cell line DC-3F/A75 REFERENCE I48104 !$#authors Mitchell, P.J.; Urlaub, G.; Chasin, L. !$#journal Mol. Cell. Biol. (1986) 6:1926-1935 !$#title Spontaneous splicing mutations at the dihydrofolate !1reductase locus in Chinese hamster ovary cells. !$#cross-references MUID:87064481; PMID:3023911 !$#accession I48104 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 88-160 ##label RES !'##cross-references GB:M13477; NID:g191049; PIDN:AAA36973.1; !1PID:g553838 COMMENT This enzyme catalyzes the NADPH-dependent reduction of 7, !18-dihydrofolate to 5,6,7,8-tetrahydrofolate, which is !1involved in the synthesis of thymidylate, purines, and some !1amino acids. GENETICS !$#introns 122/3 !$#note the list of introns may be incomplete CLASSIFICATION #superfamily type I dihydrofolate reductase; type I !1dihydrofolate reductase homology KEYWORDS methotrexate resistance; NADP; oxidoreductase; trimethoprim !1resistance FEATURE !$3-125 #domain type I dihydrofolate reductase homology !8#label DFR\ !$30,34,64,70 #binding_site substrate (Glu, Phe, Asn, Arg) #status !8predicted SUMMARY #length 186 #molecular-weight 21501 #checksum 8909 SEQUENCE /// ENTRY RDBOD #type complete TITLE dihydrofolate reductase (EC 1.5.1.3) - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 15-Oct-1982 #sequence_revision 15-Oct-1982 #text_change 11-Nov-1996 ACCESSIONS A00388 REFERENCE A00388 !$#authors Lai, P.H.; Pan, Y.C.E.; Gleisner, J.M.; Peterson, D.L.; !1Williams, K.R.; Blakley, R.L. !$#journal Biochemistry (1982) 21:3284-3294 !$#title Structure of dihydrofolate reductase: primary sequence of !1the bovine liver enzyme. !$#cross-references MUID:83000246; PMID:7115669 !$#accession A00388 !'##molecule_type protein !'##residues 1-186 ##label LAI !'##experimental_source liver CLASSIFICATION #superfamily type I dihydrofolate reductase; type I !1dihydrofolate reductase homology KEYWORDS NADP; oxidoreductase FEATURE !$3-125 #domain type I dihydrofolate reductase homology !8#label DFR\ !$30,34,64,70 #binding_site substrate (Glu, Phe, Asn, Arg) #status !8predicted SUMMARY #length 186 #molecular-weight 21472 #checksum 9961 SEQUENCE /// ENTRY RDPGD #type complete TITLE dihydrofolate reductase (EC 1.5.1.3) - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 28-Feb-1980 #sequence_revision 28-Feb-1980 #text_change 11-Nov-1996 ACCESSIONS A00389 REFERENCE A00389 !$#authors Smith, S.L.; Patrick, P.; Stone, D.; Phillips, A.W.; !1Burchall, J.J. !$#journal J. Biol. Chem. (1979) 254:11475-11484 !$#title Porcine liver dihydrofolate reductase. Purification, !1properties, and amino acid sequence. !$#cross-references MUID:80049777; PMID:500653 !$#accession A00389 !'##molecule_type protein !'##residues 1-186 ##label SMI !'##experimental_source liver !'##note Cys-162 may be modified in approximately 30% of the molecules CLASSIFICATION #superfamily type I dihydrofolate reductase; type I !1dihydrofolate reductase homology KEYWORDS NADP; oxidoreductase FEATURE !$3-125 #domain type I dihydrofolate reductase homology !8#label DFR\ !$30,34,64,70 #binding_site substrate (Glu, Phe, Asn, Arg) #status !8predicted SUMMARY #length 186 #molecular-weight 21455 #checksum 9854 SEQUENCE /// ENTRY RDBE11 #type complete TITLE dihydrofolate reductase (EC 1.5.1.3) - saimiriine herpesvirus 1 (strain 11) ORGANISM #formal_name saimiriine herpesvirus 1 #note host Saimiri sciureus (common squirrel monkey) DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 11-Jun-1999 ACCESSIONS A29954; B36806 REFERENCE A29954 !$#authors Trimble, J.J.; Murthy, S.C.S.; Bakker, A.; Grassmann, R.; !1Desrosiers, R.C. !$#journal Science (1988) 239:1145-1147 !$#title A gene for dihydrofolate reductase in a herpesvirus. !$#cross-references MUID:88145671; PMID:2830673 !$#accession A29954 !'##molecule_type DNA !'##residues 1-187 ##label TRI !'##cross-references GB:M19237; NID:g331031; PIDN:AAA46154.1; !1PID:g331032 REFERENCE A36806 !$#authors Albrecht, J. !$#submission submitted to the EMBL Data Library, January 1992 !$#description Primary structure of the herpesvirus saimiri genome. !$#accession B36806 !'##molecule_type DNA !'##residues 1-187 ##label ALB !'##cross-references GB:X64346; NID:g60320; PIDN:CAA45624.1; PID:g60322 REFERENCE A37309 !$#authors Albrecht, J.C.; Nicholas, J.; Biller, D.; Cameron, K.R.; !1Biesinger, B.; Newman, C.; Wittmann, S.; Craxton, M.A.; !1Coleman, H.; Fleckenstein, B.; Honess, R.W. !$#journal J. Virol. (1992) 66:5047-5058 !$#title Primary structure of the herpesvirus saimiri genome. !$#cross-references MUID:92333688; PMID:1321287 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given COMMENT This enzyme catalyzes the reduction of dihydrofolate to !1tetrahydrofolate. GENETICS !$#gene 2 CLASSIFICATION #superfamily type I dihydrofolate reductase; type I !1dihydrofolate reductase homology KEYWORDS methotrexate resistance; NADP; oxidoreductase; trimethoprim !1resistance FEATURE !$4-126 #domain type I dihydrofolate reductase homology !8#label DFR\ !$31,35,65,71 #binding_site substrate (Asp, Phe, Asn, Arg) #status !8predicted SUMMARY #length 187 #molecular-weight 21719 #checksum 794 SEQUENCE /// ENTRY RDBEHS #type complete TITLE dihydrofolate reductase (EC 1.5.1.3) - saimiriine herpesvirus 1 (strain 488) ORGANISM #formal_name saimiriine herpesvirus 1 DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 11-Jun-1999 ACCESSIONS E34770 REFERENCE A34770 !$#authors Biesinger, B.; Trimble, J.J.; Desrosiers, R.C.; !1Fleckenstein, B. !$#journal Virology (1990) 176:505-514 !$#title The divergence between two oncogenic Herpesvirus saimiri !1strains in a genomic region related to the transforming !1phenotype. !$#cross-references MUID:90266466; PMID:2161148 !$#accession E34770 !'##molecule_type DNA !'##residues 1-213 ##label BIE !'##cross-references EMBL:M55264; NID:g331005; PIDN:AAA72932.1; !1PID:g331010 CLASSIFICATION #superfamily type I dihydrofolate reductase; type I !1dihydrofolate reductase homology KEYWORDS methotrexate resistance; NADP; oxidoreductase; trimethoprim !1resistance FEATURE !$4-125 #domain type I dihydrofolate reductase homology !8#label DFR\ !$31,35,64,70 #binding_site substrate (Asp, Phe, Asn, Arg) #status !8predicted SUMMARY #length 213 #molecular-weight 24577 #checksum 1227 SEQUENCE /// ENTRY RDCHD #type complete TITLE dihydrofolate reductase (EC 1.5.1.3) - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 31-Jul-1980 #sequence_revision 31-Jul-1980 #text_change 07-May-1999 ACCESSIONS A00390; S66557 REFERENCE A00390 !$#authors Kumar, A.A.; Blankenship, D.T.; Kaufman, B.T.; Freisheim, !1J.H. !$#journal Biochemistry (1980) 19:667-678 !$#title Primary structure of chicken liver dihydrofolate reductase. !$#cross-references MUID:80130564; PMID:6766736 !$#accession A00390 !'##molecule_type protein !'##residues 1-189 ##label KUM REFERENCE S66557 !$#authors Fan, Y.; Ju, M.; Zhou, J.; Tsou, C. !$#journal Biochem. J. (1996) 315:97-102 !$#title Activation of chicken liver dihydrofolate reductase by urea !1and guanidine hydrochloride is accompanied by conformational !1change at the active site. !$#cross-references MUID:96207568; PMID:8670138 !$#accession S66557 !'##molecule_type protein !'##residues 19-22;138-140,'Q';158-161 ##label FAN CLASSIFICATION #superfamily type I dihydrofolate reductase; type I !1dihydrofolate reductase homology KEYWORDS NADP; oxidoreductase FEATURE !$3-125 #domain type I dihydrofolate reductase homology !8#label DFR\ !$30,34,64,70 #binding_site substrate (Glu, Phe, Asn, Arg) #status !8predicted SUMMARY #length 189 #molecular-weight 21650 #checksum 1926 SEQUENCE /// ENTRY RDBYD #type complete TITLE dihydrofolate reductase (EC 1.5.1.3) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein O5231; protein YOR236w ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 21-Jul-2000 ACCESSIONS JT0269; JT0274; S06312; S67129 REFERENCE A91592 !$#authors Fling, M.E.; Kopf, J.; Richards, C.A. !$#journal Gene (1988) 63:165-174 !$#title Nucleotide sequence of the dihydrofolate reductase gene of !1Saccharomyces cerevisiae. !$#cross-references MUID:88255864; PMID:2838385 !$#accession JT0269 !'##molecule_type DNA !'##residues 1-211 ##label FLI !'##cross-references GB:M18578; EMBL:M26667; NID:g171396; !1PIDN:AAB59331.1; PID:g171397 REFERENCE A91593 !$#authors Barclay, B.J.; Huang, T.; Nagel, M.G.; Misener, V.L.; Game, !1J.C.; Wahl, G.M. !$#journal Gene (1988) 63:175-185 !$#title Mapping and sequencing of the dihydrofolate reductase gene !1(DFR1) of Saccharomyces cerevisiae. !$#cross-references MUID:88255865; PMID:2838386 !$#accession JT0274 !'##molecule_type DNA !'##residues 1-211 ##label BAR !'##cross-references EMBL:M26668; NID:g295603; PIDN:AAA34564.1; !1PID:g295604 REFERENCE S06312 !$#authors Lagosky, P.A.; Taylor, G.R.; Haynes, R.H. !$#journal Nucleic Acids Res. (1987) 15:10355-10371 !$#title Molecular characterization of the Saccharomyces cerevisiae !1dihydrofolate reductase gene (DFR1). !$#cross-references MUID:88096572; PMID:2827121 !$#accession S06312 !'##molecule_type DNA !'##residues 1-211 ##label LAG !'##cross-references EMBL:Y00887 !'##note the authors translated the codon GTA for residue 27 as Leu; the !1sequence shown follows the authors' translation REFERENCE S67104 !$#authors Boyer, J.; Fairhead, C.; Gaillon, L.; Galisson, F.; Michaux, !1G.; Thierry, A.; Dujon, B. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67129 !'##molecule_type DNA !'##residues 1-211 ##label BOY !'##cross-references EMBL:Z75144; NID:g1420540; PIDN:CAA99456.1; !1PID:g1420541; GSPDB:GN00015; MIPS:YOR236w !'##experimental_source strain S288C COMMENT This enzyme catalyzes the NADPH-dependent reduction of !1dihydrofolate to tetrahydrofolate. GENETICS !$#gene SGD:DFR1; MIPS:YOR236w !'##cross-references SGD:S0005762; MIPS:YOR236w !$#map_position 15R CLASSIFICATION #superfamily type I dihydrofolate reductase; type I !1dihydrofolate reductase homology KEYWORDS NADP; oxidoreductase FEATURE !$8-132 #domain type I dihydrofolate reductase homology !8#label DFR\ !$34,38,68,74 #binding_site substrate (Glu, Phe, Phe, Arg) #status !8predicted SUMMARY #length 211 #molecular-weight 24261 #checksum 8536 SEQUENCE /// ENTRY RDECD #type complete TITLE dihydrofolate reductase (EC 1.5.1.3) type I - Escherichia coli (strain K-12) ALTERNATE_NAMES tetrahydrofolate dehydrogenase ORGANISM #formal_name Escherichia coli DATE 30-Apr-1982 #sequence_revision 30-Apr-1982 #text_change 01-Mar-2002 ACCESSIONS A93704; A91181; A91244; A92301; A90409; S40569; H64725; !1A00391; A29070 REFERENCE A93704 !$#authors Smith, D.R.; Calvo, J.M. !$#journal Nucleic Acids Res. (1980) 8:2255-2274 !$#title Nucleotide sequence of the Escherichia coli gene coding for !1dihydrofolate reductase. !$#cross-references MUID:81053692; PMID:6159575 !$#accession A93704 !'##molecule_type DNA !'##residues 1-159 ##label SMI !'##cross-references GB:D10483; GB:J01597; GB:J01683; GB:J01706; !1GB:K01298; GB:K01990; GB:M10420; GB:M10611; GB:M12544; !1GB:V00259; GB:X04711; GB:X54847; GB:X54945; GB:X55034; !1GB:X56742; NID:g216434; PIDN:BAA01324.1; PID:g216473 !'##experimental_source strain K-12 REFERENCE A91181 !$#authors Flensburg, J.; Skold, O. !$#journal Eur. J. Biochem. (1987) 162:473-476 !$#title Massive overproduction of dihydrofolate reductase in !1bacteria as a response to the use of trimethoprim. !$#cross-references MUID:87161813; PMID:3549289 !$#accession A91181 !'##molecule_type DNA !'##residues 1-29,'G',31-153,'Q',155-159 ##label FLE !'##cross-references GB:X05108; NID:g41264; PIDN:CAA28755.1; PID:g41265 !'##experimental_source strain 1810 REFERENCE A91244 !$#authors Stone, D.; Phillips, A.W.; Burchall, J.J. !$#journal Eur. J. Biochem. (1977) 72:613-624 !$#title The amino-acid sequence of the dihydrofolate reductase of a !1trimethoprim-resistant strain of Escherichia coli. !$#cross-references MUID:77115802; PMID:320005 !$#accession A91244 !'##molecule_type protein !'##residues 1-36,'D',38-86,'N',88-117,'Q',119-159 ##label STO !'##experimental_source strain B [RT500] isozyme 1 REFERENCE A92301 !$#authors Baccanari, D.P.; Stone, D.; Kuyper, L. !$#journal J. Biol. Chem. (1981) 256:1738-1747 !$#title Effect of a single amino acid substitution on Escherichia !1coli dihydrofolate reductase catalysis and ligand binding. !$#cross-references MUID:81117257; PMID:7007370 !$#accession A92301 !'##molecule_type protein !'##residues 1-27,'R',29-36,'D',38-86,'N',88-117,'Q',119-159 ##label BAC !'##experimental_source strain B [RT500] isozyme 2 !'##note this strain is resistant to 500 micrograms per milliliter of !1trimethoprim REFERENCE A90409 !$#authors Bennett, C.D.; Rodkey, J.A.; Sondey, J.M.; Hirschmann, R. !$#journal Biochemistry (1978) 17:1328-1337 !$#title Dihydrofolate reductase: the amino acid sequence of the !1enzyme from a methotrexate-resistant mutant of Escherichia !1coli. !$#cross-references MUID:78187252; PMID:350268 !$#accession A90409 !'##molecule_type protein !'##residues 1-36,'D',38-86,'N',88-141,'N',143-153,'K',155-159 ##label !1BEN !'##experimental_source strain B [MB1428] !'##note this strain is methotrexate-resistant REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40569 !'##molecule_type DNA !'##residues 1-159 ##label YUR !'##cross-references EMBL:D10483; NID:g216434; PIDN:BAA01324.1; !1PID:g216473 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64725 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-159 ##label BLAT !'##cross-references GB:AE000115; GB:U00096; NID:g1786230; !1PIDN:AAC73159.1; PID:g1786233; UWGP:b0048 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene folA !$#map_position 1 min FUNCTION !$#pathway one-carbon metabolism; folate biosynthesis CLASSIFICATION #superfamily type I dihydrofolate reductase; type I !1dihydrofolate reductase homology KEYWORDS folate biosynthesis; methotrexate resistance; NADP; !1one-carbon metabolism; oxidoreductase; trimethoprim !1resistance FEATURE !$1-104 #domain type I dihydrofolate reductase homology !8#label DFR\ !$27,31,51,57 #binding_site substrate (Asp, Phe, Gly, Arg) #status !8predicted SUMMARY #length 159 #molecular-weight 17999 #checksum 851 SEQUENCE /// ENTRY RDKBD #type complete TITLE dihydrofolate reductase (EC 1.5.1.3) - Klebsiella pneumoniae ORGANISM #formal_name Klebsiella pneumoniae DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jun-2000 ACCESSIONS A42379 REFERENCE A42379 !$#authors Azakami, H.; Sugino, H.; Murooka, Y. !$#journal J. Bacteriol. (1992) 174:2344-2351 !$#title Cloning and nucleotide sequence of a negative regulator gene !1for Klebsiella aerogenes arylsulfatase synthesis and !1identification of the gene as folA. !$#cross-references MUID:92202165; PMID:1551851 !$#accession A42379 !'##molecule_type DNA !'##residues 1-159 ##label AZA !'##cross-references GB:D10358; NID:g216718; PIDN:BAA01187.1; !1PID:g216719 !'##note the source is designated as Klebsiella aerogenes W70 GENETICS !$#gene folA CLASSIFICATION #superfamily type I dihydrofolate reductase; type I !1dihydrofolate reductase homology KEYWORDS methotrexate resistance; NADP; oxidoreductase; trimethoprim !1resistance FEATURE !$1-104 #domain type I dihydrofolate reductase homology !8#label DFR\ !$27,31,51,57 #binding_site substrate (Asp, Phe, Gly, Arg) #status !8predicted SUMMARY #length 159 #molecular-weight 18112 #checksum 942 SEQUENCE /// ENTRY RDEBDT #type complete TITLE dihydrofolate reductase (EC 1.5.1.3) type III - Salmonella typhimurium plasmid pAZ1 ORGANISM #formal_name Salmonella typhimurium DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 28-May-1999 ACCESSIONS JT0266; A22241 REFERENCE JT0266 !$#authors Fling, M.E.; Kopf, J.; Richards, C. !$#journal Plasmid (1988) 19:30-38 !$#title Characterization of plasmid pAZ1 and the type III !1dihydrofolate reductase gene. !$#cross-references MUID:88289861; PMID:2840679 !$#accession JT0266 !'##molecule_type DNA !'##residues 1-162 ##label FLI !'##cross-references GB:J03306; NID:g150519; PIDN:AAA25550.1; !1PID:g150520 REFERENCE A92480 !$#authors Joyner, S.S.; Fling, M.E.; Stone, D.; Baccanari, D.P. !$#journal J. Biol. Chem. (1984) 259:5851-5856 !$#title Characterization of an R-plasmid dihydrofolate reductase !1with a monomeric structure. !$#cross-references MUID:84185739; PMID:6371010 !$#accession A22241 !'##molecule_type protein !'##residues 1-7,'S',9-20 ##label JOY COMMENT This enzyme catalyzes the NADPH-dependent reduction of !1dihydrofolate to tetrahydrofolate. COMMENT The plasmid pAZ1 determines trimethoprim and sulphonamide !1resistance. GENETICS !$#genome plasmid CLASSIFICATION #superfamily type I dihydrofolate reductase; type I !1dihydrofolate reductase homology KEYWORDS NADP; oxidoreductase; sulfonamide resistance; trimethoprim !1resistance FEATURE !$2-106 #domain type I dihydrofolate reductase homology !8#label DFR\ !$28,32,52,58 #binding_site substrate (Asp, Phe, Gly, Arg) #status !8predicted SUMMARY #length 162 #molecular-weight 18032 #checksum 9761 SEQUENCE /// ENTRY RDBSD #type complete TITLE dihydrofolate reductase (EC 1.5.1.3) - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jun-2000 ACCESSIONS JT0291; A38062; F69614 REFERENCE A91594 !$#authors Iwakura, M.; Kawata, M.; Tsuda, K.; Tanaka, T. !$#journal Gene (1988) 64:9-20 !$#title Nucleotide sequence of the thymidylate synthase B and !1dihydrofolate reductase genes contained in one Bacillus !1subtilis operon. !$#cross-references MUID:88284366; PMID:2840350 !$#accession JT0291 !'##molecule_type DNA !'##residues 1-168 ##label IWA1 !'##cross-references GB:M20012; NID:g143740; PIDN:AAA22853.1; !1PID:g143742 !'##experimental_source strain MI112 !$#accession A38062 !'##molecule_type protein !'##residues 1-8;166-168 ##label IWA2 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69614 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-164,'A',166-168 ##label KUN !'##cross-references GB:Z99115; GB:AL009126; NID:g2634478; !1PIDN:CAB14099.1; PID:g2634601 !'##experimental_source strain 168 COMMENT The dfrA gene is 3' to the thyB gene and overlaps it by one !1nucleotide. GENETICS !$#gene dfrA !$#map_position 200 (degrees) FUNCTION !$#description catalyzes the reduction of dihydrofolic acid to !1tetrahydrofolic acid by NADPH !$#pathway tetrahydrofolate synthesis CLASSIFICATION #superfamily type I dihydrofolate reductase; type I !1dihydrofolate reductase homology KEYWORDS NADP; oxidoreductase FEATURE !$1-105 #domain type I dihydrofolate reductase homology !8#label DFR\ !$27,31,51,57 #binding_site substrate (Asp, Phe, Gly, Arg) #status !8predicted SUMMARY #length 168 #molecular-weight 19204 #checksum 5822 SEQUENCE /// ENTRY RDSODF #type complete TITLE dihydrofolate reductase (EC 1.5.1.3) - Enterococcus faecium ORGANISM #formal_name Enterococcus faecium DATE 29-Jul-1981 #sequence_revision 29-Jul-1981 #text_change 18-Jul-1997 ACCESSIONS A00392 REFERENCE A00392 !$#authors Peterson, D.L.; Gleisner, J.M.; Blakley, R.L. !$#journal J. Biol. Chem. (1975) 250:4945-4954 !$#title The structure of the mutant dihydrofolate reductase from !1Streptococcus faecium. Amino acid sequence of peptide CNBr 7 !1and complete sequence of the protein. !$#cross-references MUID:75211261; PMID:1097435 !$#accession A00392 !'##molecule_type protein !'##residues 1-167 ##label PET !'##experimental_source strain A, var. Durans CLASSIFICATION #superfamily type I dihydrofolate reductase; type I !1dihydrofolate reductase homology KEYWORDS NADP; oxidoreductase FEATURE !$1-108 #domain type I dihydrofolate reductase homology !8#label DFR\ !$27,31,51,58 #binding_site substrate (Asp, Phe, Gly, Arg) #status !8predicted SUMMARY #length 167 #molecular-weight 19582 #checksum 1992 SEQUENCE /// ENTRY RDNHD #type complete TITLE dihydrofolate reductase (EC 1.5.1.3) - Neisseria gonorrhoeae ORGANISM #formal_name Neisseria gonorrhoeae DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 18-Jul-1997 ACCESSIONS A00393 REFERENCE A00393 !$#authors Baccanari, D.P.; Tansik, R.L.; Paterson, S.J.; Stone, D. !$#journal J. Biol. Chem. (1984) 259:12291-12298 !$#title Characterization and amino acid sequence of Neisseria !1gonorrhoeae dihydrofolate reductase. !$#cross-references MUID:85006974; PMID:6434541 !$#accession A00393 !'##molecule_type protein !'##residues 1-162 ##label BAC CLASSIFICATION #superfamily type I dihydrofolate reductase; type I !1dihydrofolate reductase homology KEYWORDS methotrexate resistance; NADP; oxidoreductase; trimethoprim !1resistance FEATURE !$3-108 #domain type I dihydrofolate reductase homology !8#label DFR\ !$29,33,60 #binding_site substrate (Asp, Phe, Arg) #status !8predicted SUMMARY #length 162 #molecular-weight 17730 #checksum 9225 SEQUENCE /// ENTRY RDLBD #type complete TITLE dihydrofolate reductase (EC 1.5.1.3) [validated] - Lactobacillus casei ORGANISM #formal_name Lactobacillus casei DATE 31-May-1979 #sequence_revision 17-Sep-1997 #text_change 15-Sep-2000 ACCESSIONS A24036; A00394; A12987 REFERENCE A24036 !$#authors Andrews, J.; Clore, G.M.; Davies, R.W.; Gronenborn, A.M.; !1Gronenborn, B.; Kalderon, D.; Papadopoulos, P.C.; Schafer, !1S.; Sims, P.F.G.; Stancombe, R. !$#journal Gene (1985) 35:217-222 !$#title Nucleotide sequence of the dihydrofolate reductase gene of !1methotrexate-resistant Lactobacillus casei. !$#cross-references MUID:85286353; PMID:3928445 !$#accession A24036 !'##molecule_type DNA !'##residues 1-163 ##label AND !'##cross-references GB:M10922; NID:g149539; PIDN:AAA25237.1; !1PID:g149540 !'##experimental_source clone pWDLcB1 !'##note sequence from a methotrexate-resistant strain REFERENCE A00394 !$#authors Freisheim, J.H.; Bitar, K.G.; Reddy, A.V.; Blankenship, D.T. !$#journal J. Biol. Chem. (1978) 253:6437-6444 !$#title Dihydrofolate reductase from amethopterin-resistant !1Lactobacillus casei. Sequences of the cyanogen bromide !1peptides and complete sequence of the enzyme. !$#cross-references MUID:78242349; PMID:98527 !$#accession A00394 !'##molecule_type protein !'##residues 2-8,'N',10-90,'L',92-163 ##label FRE !'##note sequence from a strain resistant to the folic acid analog !1methotrexate (amethopterin); it is not clear whether the !1differences reflect strain variations REFERENCE A12987 !$#authors Batley, K.E.; Morris, H.R. !$#journal Biochem. Biophys. Res. Commun. (1977) 75:1010-1014 !$#title Dihydrofolate reductase from Lactobacillus casei: N-terminal !1sequence and comparison with the substrate binding region of !1other reductases. !$#cross-references MUID:77181453; PMID:405008 !$#accession A12987 !'##molecule_type protein !'##residues 2-52 ##label BAT !'##note sequence from a methotrexate-resistant strain REFERENCE A50583 !$#authors Filman, D.J.; Matthews, D.A.; Bolin, J.T.; Kraut, J. !$#submission submitted to the Brookhaven Protein Data Bank, June 1982 !$#cross-references PDB:3DFR !$#contents annotation; X-ray crystallography, 1.7 angstroms, 2-8,'N', !110,'N',12-90,'L',92-163 !$#note dichloromethotrexate-resistant strain !$#note strain methotrexate-resistant, expressed in Escherichia coli REFERENCE A65422 !$#authors Morgan, W.D.; Birdsall, B.; Polshakov, V.I.; Sali, D.; !1Kompis, I.; Feeney, J. !$#submission submitted to the Brookhaven Protein Data Bank, August 1995 !$#cross-references PDB:1DIS !$#contents annotation; conformation by NMR, residues 2-163 REFERENCE A58587 !$#authors Morgan, W.D.; Birdsall, B.; Polshakov, V.I.; Sali, D.; !1Kompis, I.; Feeney, J. !$#journal Biochemistry (1995) 34:11690-11702 !$#title Solution structure of a brodimoprim analogue in its complex !1with Lactobacillus casei dihydrofolate reductase. !$#cross-references MUID:96018856; PMID:7547901 !$#contents annotation; conformation by (1)H-NMR FUNCTION !$#description catalyzes the reduction of dihydrofolic acid to !1tetrahydrofolic acid with NADPH; oxidoreductase !$#pathway tetrahydrofolate synthesis CLASSIFICATION #superfamily type I dihydrofolate reductase; type I !1dihydrofolate reductase homology KEYWORDS NADP; oxidoreductase FEATURE !$2-163 #product dihydrofolate reductase #status experimental !8#label MAT\ !$2-108 #domain type I dihydrofolate reductase homology !8#label DFR\ !$27,31,58 #binding_site substrate (Asp, Phe, Arg) #status !8predicted SUMMARY #length 163 #molecular-weight 18439 #checksum 5898 SEQUENCE /// ENTRY RDECD7 #type complete TITLE dihydrofolate reductase (EC 1.5.1.3) type I - Escherichia coli plasmid ORGANISM #formal_name Escherichia coli DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 16-Jun-2000 ACCESSIONS S03651; A21038; A00395; S11702 REFERENCE S03651 !$#authors Simonsen, C.C.; Walter, M.; Levinson, A.D. !$#journal Nucleic Acids Res. (1988) 16:2235-2246 !$#title Expression of the plasmid-encoded type I dihydrofolate !1reductase gene in cultured mammalian cells: a novel !1selectable marker. !$#cross-references MUID:88189815; PMID:3357775 !$#accession S03651 !'##molecule_type DNA !'##residues 1-157 ##label SIM REFERENCE A21038 !$#authors Novak, P.; Stone, D.; Burchall, J.J. !$#journal J. Biol. Chem. (1983) 258:10956-10959 !$#title R plasmid dihydrofolate reductase with a dimeric subunit !1structure. !$#cross-references MUID:83291046; PMID:6350298 !$#accession A21038 !'##molecule_type protein !'##residues 1-34 ##label NOV REFERENCE A00395 !$#authors Fling, M.E.; Richards, C. !$#journal Nucleic Acids Res. (1983) 11:5147-5158 !$#title The nucleotide sequence of the trimethoprim-resistant !1dihydrofolate reductase gene harbored by Tn7. !$#cross-references MUID:83272957; PMID:6308574 !$#accession A00395 !'##molecule_type DNA !'##residues 1-157 ##label FLI !'##cross-references GB:X00926; GB:K00970; NID:g41266; PIDN:CAA25445.1; !1PID:g581066 REFERENCE S11701 !$#authors Sundstroem, L.; Skoeld, O. !$#journal Antimicrob. Agents Chemother. (1990) 34:642-650 !$#title The dhfrI trimethoprim resistance gene of Tn7 can be found !1at specific sites in other genetic surroundings. !$#cross-references MUID:90262183; PMID:2188588 !$#accession S11702 !'##status preliminary !'##molecule_type DNA !'##residues 1-157 ##label SUN !'##cross-references EMBL:X17477; NID:g45578; PIDN:CAA35509.1; !1PID:g1333726 GENETICS !$#genome plasmid !$#start_codon GTG !$#note the protein is encoded by genes from plasmid pLMO150 and !1plasmid R438 CLASSIFICATION #superfamily type I dihydrofolate reductase; type I !1dihydrofolate reductase homology KEYWORDS homodimer; methotrexate resistance; NADP; oxidoreductase; !1trimethoprim resistance FEATURE !$2-107 #domain type I dihydrofolate reductase homology !8#label DFR\ !$28,32,52,57 #binding_site substrate (Glu, Phe, Gly, Arg) #status !8predicted SUMMARY #length 157 #molecular-weight 17575 #checksum 6601 SEQUENCE /// ENTRY S04810 #type complete TITLE dihydrofolate reductase (EC 1.5.1.3) type V [similarity] - Escherichia coli plasmid pLMO20 ORGANISM #formal_name Escherichia coli DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 16-Jun-2000 ACCESSIONS S04810 REFERENCE S04809 !$#authors Sundstroem, L.; Radstroem, P.; Swedberg, G.; Skoeld, O. !$#journal Mol. Gen. Genet. (1988) 213:191-201 !$#title Site-specific recombination promotes linkage between !1trimethoprim- and sulfonamide resistance genes. Sequence !1characterization of dhfrV and sulI and a recombination !1active locus of Tn21. !$#cross-references MUID:89039710; PMID:3054482 !$#accession S04810 !'##molecule_type DNA !'##residues 1-157 ##label SUN !'##cross-references EMBL:X12868; NID:g45672; PIDN:CAA31356.1; !1PID:g1333796 GENETICS !$#gene dhfrV !$#genome plasmid pLMO20 !$#start_codon GTG CLASSIFICATION #superfamily type I dihydrofolate reductase; type I !1dihydrofolate reductase homology KEYWORDS antibiotic resistance; NADP; oxidoreductase FEATURE !$2-107 #domain type I dihydrofolate reductase homology !8#label DFR SUMMARY #length 157 #molecular-weight 17531 #checksum 5492 SEQUENCE /// ENTRY RDBPT4 #type complete TITLE dihydrofolate reductase (EC 1.5.1.3) - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 01-Dec-2000 ACCESSIONS A00396; T10128 REFERENCE A00396 !$#authors Purohit, S.; Mathews, C.K. !$#journal J. Biol. Chem. (1984) 259:6261-6266 !$#title Nucleotide sequence reveals overlap between T4 phage genes !1encoding dihydrofolate reductase and thymidylate synthase. !$#cross-references MUID:84212439; PMID:6327673 !$#accession A00396 !'##molecule_type DNA !'##residues 1-193 ##label PUR !'##cross-references GB:K01804; GB:K02034; NID:g215849; PIDN:AAA32491.1; !1PID:g215852 REFERENCE Z16963 !$#authors Chu, F. !$#submission submitted to the EMBL Data Library, April 1998 !$#accession T10128 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 123-193 ##label CHU !'##cross-references EMBL:M12742; NID:g3033366; PID:g1196771 !'##experimental_source strain alc4 GENETICS !$#gene frd CLASSIFICATION #superfamily type I dihydrofolate reductase; type I !1dihydrofolate reductase homology KEYWORDS methotrexate resistance; NADP; oxidoreductase; trimethoprim !1resistance FEATURE !$9-137 #domain type I dihydrofolate reductase homology !8#label DFR SUMMARY #length 193 #molecular-weight 21713 #checksum 9895 SEQUENCE /// ENTRY G75250 #type complete TITLE dihydrofolate reductase (EC 1.5.1.3) [similarity] - Deinococcus radiodurans (strain R1) ORGANISM #formal_name Deinococcus radiodurans DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS G75250 REFERENCE A75250 !$#authors White, O.; Eisen, J.A.; Heidelberg, J.F.; Hickey, E.K.; !1Peterson, J.D.; Dodson, R.J.; Haft, D.H.; Gwinn, M.L.; !1Nelson, W.C.; Richardson, D.L.; Moffat, K.S.; Qin, H.; !1Jiang, L.; Pamphile, W.; Crosby, M.; Shen, M.; Vamathevan, !1J.J.; Lam, P.; McDonald, L.; Utterback, T.; Zalewski, C.; !1Makarova, K.S.; Aravind, L.; Daly, M.J.; Minton, K.W.; !1Fleischmann, R.D.; Ketchum, K.A.; Nelson, K.E.; Salzberg, !1S.; Smith, H.O.; Venter, J.C.; Fraser, C.M. !$#journal Science (1999) 286:1571-1577 !$#title Genome sequence of the radioresistant bacterium Deinococcus !1radiodurans R1. !$#cross-references MUID:20036896; PMID:10567266 !$#accession G75250 !'##molecule_type DNA !'##residues 1-180 ##label WHI !'##cross-references GB:AE002092; GB:AE000513; NID:g6460455; !1PIDN:AAF12168.1; PID:g6460461; TIGR:DR2632; GSPDB:GN00077 !'##experimental_source strain R1 GENETICS !$#gene DR2632 !$#map_position 1 CLASSIFICATION #superfamily type I dihydrofolate reductase; type I !1dihydrofolate reductase homology KEYWORDS NADP; oxidoreductase SUMMARY #length 180 #molecular-weight 20400 #checksum 3439 SEQUENCE /// ENTRY H71493 #type complete TITLE dihydrofolate reductase [similarity] - Chlamydia trachomatis (serotype D, strain UW3/Cx) ORGANISM #formal_name Chlamydia trachomatis DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS H71493 REFERENCE A71570 !$#authors Stephens, R.S.; Kalman, S.; Lammel, C.J.; Fan, J.; Marathe, !1R.; Aravind, L.; Mitchell, W.P.; Olinger, L.; Tatusov, R.L.; !1Zhao, Q.; Koonin, E.V.; Davis, R.W. !$#journal Science (1998) 282:754-759 !$#title Genome sequence of an obligate intracellular pathogen of !1humans: Chlamydia trachomatis. !$#cross-references MUID:99000809; PMID:9784136 !$#accession H71493 !'##molecule_type DNA !'##residues 1-159 ##label ARN !'##cross-references GB:AE001331; GB:AE001273; NID:g3329046; !1PIDN:AAC68215.1; PID:g3329057 !'##experimental_source serotype D, strain UW-3/Cx GENETICS !$#gene folA CLASSIFICATION #superfamily type I dihydrofolate reductase; type I !1dihydrofolate reductase homology SUMMARY #length 159 #molecular-weight 18381 #checksum 385 SEQUENCE /// ENTRY A49790 #type complete TITLE dihydrofolate reductase (EC 1.5.1.3) type X [similarity] - Escherichia coli plasmid pDGO100 ORGANISM #formal_name Escherichia coli DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 18-Aug-2000 ACCESSIONS A49790; T45125 REFERENCE A49790 !$#authors Parsons, Y.; Hall, R.M.; Stokes, H.W. !$#journal Antimicrob. Agents Chemother. (1991) 35:2436-2439 !$#title A new trimethoprim resistance gene, dhfrX, in the In7 !1integron of plasmid pDGO100. !$#cross-references MUID:92206862; PMID:1804022 !$#accession A49790 !'##molecule_type DNA !'##residues 1-187 ##label PAR !'##cross-references GB:M69220; NID:g150624; PIDN:AAA99497.1; !1PID:g150625 REFERENCE Z22920 !$#authors Stokes, H.W.; Tomaras, C.; Parsons, Y.; Hall, R.M. !$#journal Plasmid (1993) 30:39-50 !$#title The partial 3'-conserved segment duplications in the !1integrons In6 from pSa and In7 from pDGO100 have a common !1origin. !$#cross-references MUID:93391548; PMID:8378445 !$#accession T45125 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-187 ##label STO !'##cross-references EMBL:L06418; NID:g149116; PIDN:AAA92749.1; !1PID:g149122 GENETICS !$#gene dhfrX !$#genome plasmid pDGO100 FUNCTION !$#description confers resistance to trimethoprim CLASSIFICATION #superfamily type I dihydrofolate reductase; type I !1dihydrofolate reductase homology KEYWORDS NADP; oxidoreductase FEATURE !$2-113 #domain type I dihydrofolate reductase homology !8#label DFR SUMMARY #length 187 #molecular-weight 21219 #checksum 2123 SEQUENCE /// ENTRY T43248 #type complete TITLE dihydrofolate reductase (EC 1.5.1.3) [similarity] - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES dihydropteridine reductase ORGANISM #formal_name Schizosaccharomyces pombe DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 21-Jul-2000 ACCESSIONS T43248; T40868 REFERENCE Z22365 !$#authors Bertani, L.E.; Campbell, J.L. !$#journal Gene (1994) 147:131-135 !$#title The isolation and characterization of the gene (dfr1) !1encoding dihydrofolate reductase (DHFR) in !1Schizosaccharomyces pombe. !$#cross-references MUID:94374697; PMID:8088538 !$#accession T43248 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-461 ##label BER !'##cross-references EMBL:L13703; NID:g404818; PIDN:AAA57051.1; !1PID:g404819 REFERENCE Z21953 !$#authors Wedler, H.; Wambutt, R.; Lyne, M.; Rajandream, M.A.; !1Barrell, B.G. !$#submission submitted to the EMBL Data Library, September 1998 !$#accession T40868 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-125,'QP',128-461 ##label WED !'##cross-references EMBL:AL031579; PIDN:CAA20877.1; GSPDB:GN00068; !1SPDB:SPCC1223.08c !'##experimental_source strain 972h(-); cosmid c1223 GENETICS !$#gene dfr1; SPCC1223.08c !$#map_position 3 !$#introns 12/1 FUNCTION !$#description catalyzes the reduction of dihydrofolate to tetrahydrofolate CLASSIFICATION #superfamily fission yeast dihydrofolate reductase; type I !1dihydrofolate reductase homology KEYWORDS NADP; oxidoreductase SUMMARY #length 461 #molecular-weight 51505 #checksum 2547 SEQUENCE /// ENTRY T38146 #type complete TITLE dihydrofolate reductase [similarity] - fission yeast (Schizosaccharomyces pombe) ORGANISM #formal_name Schizosaccharomyces pombe DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS T38146 REFERENCE Z21774 !$#authors Pearson, D.; Churcher, C.M.; Barrell, B.G.; Rajandream, !1M.A.; Wood, V. !$#submission submitted to the EMBL Data Library, September 1997 !$#accession T38146 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-429 ##label PEA !'##cross-references EMBL:Z99295; PIDN:CAB16576.1; GSPDB:GN00066; !1SPDB:SPAC22A12.06c !'##experimental_source strain 972h(-); cosmid c22A12 GENETICS !$#gene SPAC22A12.06c !$#map_position 1 CLASSIFICATION #superfamily fission yeast dihydrofolate reductase; type I !1dihydrofolate reductase homology SUMMARY #length 429 #molecular-weight 48231 #checksum 3842 SEQUENCE /// ENTRY F70021 #type complete TITLE proline dehydrogenase homolog yusM - Bacillus subtilis CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 23-Dec-2002 ACCESSIONS F70021 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F70021 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-302 ##label KUN !'##cross-references GB:Z99120; GB:AL009126; NID:g2635613; !1PIDN:CAB15274.1; PID:g2635781 !'##experimental_source strain 168 GENETICS !$#gene yusM CLASSIFICATION #superfamily proline dehydrogenase KEYWORDS oxidoreductase SUMMARY #length 302 #molecular-weight 34451 #checksum 8930 SEQUENCE /// ENTRY H69758 #type complete TITLE proline dehydrohenase homolog ycgM - Bacillus subtilis CONTAINS oxidoreductase (EC 1.-.-.-) ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 23-Dec-2002 ACCESSIONS H69758 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69758 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-303 ##label KUN !'##cross-references GB:Z99105; GB:AL009126; NID:g2632457; !1PIDN:CAB12114.1; PID:g2632606 !'##experimental_source strain 168 GENETICS !$#gene ycgM CLASSIFICATION #superfamily proline dehydrogenase KEYWORDS oxidoreductase SUMMARY #length 303 #molecular-weight 35046 #checksum 7063 SEQUENCE /// ENTRY I53597 #type complete TITLE proline dehydrogenase (EC 1.5.99.8) / 1-pyrroline-5-carboxylate dehydrogenase (EC 1.5.1.12) [similarity] - Escherichia coli CONTAINS 1-pyrroline-5-carboxylate dehydrogenase (EC 1.5.1.12); proline dehydrogenase (EC 1.5.99.8) ORGANISM #formal_name Escherichia coli DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS I53597; S43126 REFERENCE I53597 !$#authors Xia, M.; Zhu, Y.; Cao, X.; You, L.; Chen, Z. !$#journal FEMS Microbiol. Lett. (1995) 127:235-242 !$#title Cloning, sequencing and analysis of a gene encoding !1Escherichia coli proline dehydrogenase. !$#cross-references MUID:95278725; PMID:7758938 !$#accession I53597 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-1310 ##label XIA !'##cross-references EMBL:X78340; NID:g467735; PIDN:CAA55136.1; !1PID:g467736 !'##experimental_source strain K-12, substrain CSH4 GENETICS !$#gene putA CLASSIFICATION #superfamily bifunctional protein putA KEYWORDS FAD; flavoprotein; NAD; oxidoreductase FEATURE !$877 #active_site Glu #status predicted\ !$911 #active_site Cys #status predicted SUMMARY #length 1310 #molecular-weight 145190 #checksum 6784 SEQUENCE /// ENTRY S66279 #type complete TITLE proline dehydrogenase (EC 1.5.99.8) / 1-pyrroline-5-carboxylate dehydrogenase (EC 1.5.1.12) [validated] - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 15-Sep-2000 ACCESSIONS S66279; S33716; B39192; S03817; S31910 REFERENCE S66279 !$#authors Maloy, S.R. !$#submission submitted to the EMBL Data Library, April 1994 !$#accession S66279 !'##molecule_type DNA !'##residues 1-1320 ##label MAL !'##cross-references EMBL:X70843; NID:g470179; PIDN:CAA50193.1; !1PID:g470180 !'##experimental_source strain LT2 !'##note this is a revision to the sequence from reference S33716 REFERENCE S33716 !$#authors Allen, S.W.; Senti-Willis, A.; Maloy, S.R. !$#journal Nucleic Acids Res. (1993) 21:1676 !$#title DNA sequence of the putA gene from Salmonella typhimurium: a !1bifunctional membrane-associated dehydrogenase that binds !1DNA. !$#cross-references MUID:93241961; PMID:8479928 !$#accession S33716 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-19,'WPRRVSIA',28-272,'ENWKR',278-279,'SAILTICWAN', !1290-368,'APKRRIVWRSRSICWKNSASNPNWRAGTC',398-592, !1'RKVRLAYRIRKFRCRAICTA',613-907,'CFRQRRTTLFR',919-1034,'DV', !11037-1152, !1'RRYRRSADNSPIWPRPARSACYRGRPASAIPGRCCRVNGYYAWLMMNRTR' ##label !1ALL !'##cross-references EMBL:X70843 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1993 !'##note this sequence has been revised in reference S66279 REFERENCE S53664 !$#authors Ling, M.; Allen, S.W.; Wood, J.M. !$#journal J. Mol. Biol. (1994) 243:950-956 !$#title Sequence analysis identifies the proline dehydrogenase and !1Delta(1)-pyrroline-5-carboxylate dehydrogenase domains of !1the multifunctional Escherichia coli PutA protein. !$#cross-references MUID:95055736; PMID:7966312 !$#contents annotation REFERENCE A39192 !$#authors Ostrovsky de Spicer, P.; O'Brien, K.; Maloy, S. !$#journal J. Bacteriol. (1991) 173:211-219 !$#title Regulation of proline utilization in Salmonella typhimurium: !1a membrane-associated dehydrogenase binds DNA in vitro. !$#cross-references MUID:91100285; PMID:1987118 !$#accession B39192 !'##status preliminary !'##molecule_type DNA !'##residues 1-26 ##label OST !'##note the authors translated the codon CGT for residue 24 as Gly REFERENCE S03816 !$#authors Hahn, D.R.; Myers, R.S.; Kent, C.R.; Maloy, S.R. !$#journal Mol. Gen. Genet. (1988) 213:125-133 !$#title Regulation of proline utilization in Salmonella typhimurium: !1molecular characterization of the put operon, and DNA !1sequence of the put control region. !$#cross-references MUID:89127131; PMID:2851701 !$#accession S03817 !'##molecule_type DNA !'##residues 1-13,'HARTDQ',20-26 ##label HAH !'##cross-references EMBL:X12569 GENETICS !$#gene putA !$#map_position 22 min FUNCTION !$#description transfers eletrons from proline to the respiratory chain; !1catalyzes proline oxidation to 1-pyrroline-5-carboxylate !$#pathway proline utilization !$#note membrane-bound with proline FUNCTION HPC !$#description catalyzes hydrolysis of 1-pyrroline-5-carboxylate to !1gamma-glutamic semialdehyde !$#pathway proline utilization FUNCTION RPA !$#description transcriptional repressor controls expression of genes putP !1and putA in response to proline supply CLASSIFICATION #superfamily bifunctional protein putA KEYWORDS DNA binding; FAD; flavoprotein; membrane-associated protein; !1NAD; oxidoreductase; transcription regulation FEATURE !$883,917 #active_site Glu, Cys #status predicted SUMMARY #length 1320 #molecular-weight 144187 #checksum 3619 SEQUENCE /// ENTRY D64843 #type complete TITLE proline dehydrogenase (EC 1.5.99.8) / 1-pyrroline-5-carboxylate dehydrogenase (EC 1.5.1.12) [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES proline oxidase CONTAINS 1-pyrroline-5-carboxylate dehydrogenase (EC 1.5.1.12); proline dehydrogenase (EC 1.5.99.8) ORGANISM #formal_name Escherichia coli DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 01-Mar-2002 ACCESSIONS D64843; S53665; S53664; S07035 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64843 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1320 ##label BLAT !'##cross-references GB:AE000203; GB:U00096; NID:g1787248; !1PIDN:AAC74099.1; PID:g1787250; UWGP:b1014 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S53665 !$#authors Ling, M. !$#submission submitted to the EMBL Data Library, January 1994 !$#accession S53665 !'##molecule_type DNA !'##residues 1-530,'A',532-1320 ##label LIN !'##cross-references EMBL:U05212; NID:g468874; PIDN:AAB59985.1; !1PID:g468875 !'##experimental_source strain K-12 REFERENCE S53664 !$#authors Ling, M.; Allen, S.W.; Wood, J.M. !$#journal J. Mol. Biol. (1994) 243:950-956 !$#title Sequence analysis identifies the proline dehydrogenase and !1Delta(1)-pyrroline-5-carboxylate dehydrogenase domains of !1the multifunctional Escherichia coli PutA protein. !$#cross-references MUID:95055736; PMID:7966312 !$#accession S53664 !'##molecule_type DNA !'##residues 228-358;404-446;540-561;651-1135 ##label LIW !'##cross-references EMBL:U05212 REFERENCE S06385 !$#authors Nakao, T.; Yamato, I.; Anraku, Y. !$#journal Mol. Gen. Genet. (1987) 210:364-368 !$#title Nucleotide sequence of putC, the regulatory region for the !1put regulon of Escherichia coli K12. !$#cross-references MUID:88142554; PMID:3325781 !$#accession S07035 !'##molecule_type DNA !'##residues 1-19,'F',21-40,'AR',43-44,'GKQRYSAGATCAAFWR' ##label NAK !'##cross-references EMBL:X05653; NID:g42599; PIDN:CAA29141.1; !1PID:g42600 GENETICS !$#gene putA; poaA !$#map_position 23 min FUNCTION PDH !$#description EC 1.5.99.8 [validated, MUID:95055736]; transfers eletrons !1from proline to the respiratory chain !$#pathway proline utilization !$#note membrane-bound with proline FUNCTION PCD !$#description EC 1.5.1.12 [validated, MUID:95055736]; catalyzes the !1hydrolysis of 1-pyrroline-5-carboxylate to gamma-glutamic !1semialdehyde !$#pathway proline utilization FUNCTION PREP !$#description controls the expression of the genes putP and putA in !1response to proline supply [validated, MUID:95055736] CLASSIFICATION #superfamily bifunctional protein putA KEYWORDS DNA binding; FAD; flavoprotein; membrane-associated protein; !1NAD; oxidoreductase; transcription regulation FEATURE !$883 #active_site Glu #status predicted\ !$917 #active_site Cys #status predicted SUMMARY #length 1320 #molecular-weight 143814 #checksum 5109 SEQUENCE /// ENTRY JC4661 #type complete TITLE proline dehydrogenase (EC 1.5.99.8) - Photobacterium leiognathi ALTERNATE_NAMES putA protein ORGANISM #formal_name Photobacterium leiognathi DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JC4661 REFERENCE JC4661 !$#authors Liu, J.; Yu, K.; Chen, H.; Weng, S. !$#journal Biochem. Biophys. Res. Commun. (1996) 219:868-875 !$#title Regulatory region with putA gene of proline dehydrogenase !1that links to the Lum and the Lux operons in Photobacterium !1leiognathi. !$#cross-references MUID:96216743; PMID:8645272 !$#accession JC4661 !'##molecule_type DNA !'##residues 1-314 ##label LIU !'##cross-references GB:U39227; NID:g1236800; PIDN:AAC43866.1; !1PID:g1236801 !'##experimental_source PL741 COMMENT This enzyme is a multifunctional membrane-associated !1dehydrogenase. GENETICS !$#gene putA CLASSIFICATION #superfamily proline dehydrogenase KEYWORDS oxidoreductase SUMMARY #length 314 #molecular-weight 35213 #checksum 2213 SEQUENCE /// ENTRY RDECD6 #type complete TITLE dihydrofolate reductase (EC 1.5.1.3) type II - Escherichia coli plasmid R67 ORGANISM #formal_name Escherichia coli DATE 31-Mar-1980 #sequence_revision 29-Jul-1981 #text_change 28-May-1999 ACCESSIONS A91512; A92244; A00397; A24948 REFERENCE A91512 !$#authors Brisson, N.; Hohn, T. !$#journal Gene (1984) 28:271-274 !$#title Nucleotide sequence of the dihydrofolate-reductase gene !1borne by the plasmid R67 and conferring methotrexate !1resistance. !$#cross-references MUID:84237581; PMID:6735180 !$#accession A91512 !'##molecule_type DNA !'##residues 1-78 ##label BRI !'##cross-references GB:K02118; GB:M27532; NID:g151839; PIDN:AAA26083.1; !1PID:g151840 REFERENCE A92244 !$#authors Stone, D.; Smith, S.L. !$#journal J. Biol. Chem. (1979) 254:10857-10861 !$#title The amino acid sequence of the trimethoprim-resistant !1dihydrofolate reductase specified in Escherichia coli by !1R-plasmid R67. !$#cross-references MUID:80049683; PMID:387758 !$#accession A92244 !'##molecule_type protein !'##residues 1-78 ##label STO !'##note this protein is specified by plasmid R67 expressed in !1Escherichia coli COMMENT Type II plasmid-specified enzyme is practically insensitive !1to trimethoprim and methotrexate. GENETICS !$#genome plasmid CLASSIFICATION #superfamily type II dihydrofolate reductase KEYWORDS NADP; oxidoreductase SUMMARY #length 78 #molecular-weight 8446 #checksum 5327 SEQUENCE /// ENTRY RDECD8 #type complete TITLE dihydrofolate reductase (EC 1.5.1.3) type II - Escherichia coli plasmid R388 ORGANISM #formal_name Escherichia coli DATE 29-Jul-1981 #sequence_revision 29-Jul-1981 #text_change 11-Jun-1999 ACCESSIONS A00398 REFERENCE A00398 !$#authors Zolg, J.W.; Hanggi, U.J. !$#journal Nucleic Acids Res. (1981) 9:697-710 !$#title Characterization of a R plasmid-associated, !1trimethoprim-resistant dihydrofolate reductase and !1determination of the nucleotide sequence of the reductase !1gene. !$#cross-references MUID:81174731; PMID:6261228 !$#accession A00398 !'##molecule_type DNA !'##residues 1-78 ##label ZOL !'##cross-references GB:V00252; GB:J01774; NID:g40870; PIDN:CAA23503.1; !1PID:g40871 !'##note this protein is specified by plasmid R388 expressed in !1Escherichia coli COMMENT Type II plasmid-specified enzyme is practically insensitive !1to trimethoprim and methotrexate. GENETICS !$#genome plasmid CLASSIFICATION #superfamily type II dihydrofolate reductase KEYWORDS NADP; oxidoreductase SUMMARY #length 78 #molecular-weight 8195 #checksum 5118 SEQUENCE /// ENTRY RDECD5 #type complete TITLE dihydrofolate reductase (EC 1.5.1.3) type II - Escherichia coli plasmid R751 ALTERNATE_NAMES tetrahydrofolate dehydrogenase ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 11-Jun-1999 ACCESSIONS A23598 REFERENCE A23598 !$#authors Flensburg, J.; Steen, R. !$#journal Nucleic Acids Res. (1986) 14:5933 !$#title Nucleotide sequence analysis of the trimethoprim resistant !1dihydrofolate reductase encoded by R plasmid R751. !$#cross-references MUID:86286598; PMID:3526286 !$#accession A23598 !'##molecule_type DNA !'##residues 1-78 ##label FLE !'##cross-references GB:X04128; NID:g41268; PIDN:CAA27740.1; PID:g41269 !'##note the authors translated the codon TGC for residue 47 as Lys GENETICS !$#genome plasmid CLASSIFICATION #superfamily type II dihydrofolate reductase KEYWORDS NADP; oxidoreductase; trimethoprim resistance SUMMARY #length 78 #molecular-weight 8328 #checksum 5385 SEQUENCE /// ENTRY DEHUMT #type complete TITLE methylenetetrahydrofolate dehydrogenase (NAD) (EC 1.5.1.15) / methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9) precursor - human ALTERNATE_NAMES methylenetetrahydrofolate dehydrogenase-cyclohydrolase, NAD-dependent ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 03-Jun-2002 ACCESSIONS S14902; S06679 REFERENCE S14902 !$#authors Peri, K.G.; Belanger, C.; Mackenzie, R.E. !$#journal Nucleic Acids Res. (1989) 17:8853 !$#title Nucleotide sequence of the human NAD-dependent methylene !1tetrahydrofolate dehydrogenase-cyclohydrolase. !$#cross-references MUID:90067849; PMID:2587219 !$#accession S14902 !'##molecule_type mRNA !'##residues 1-344 ##label PER !'##cross-references EMBL:X16396; NID:g35070; PIDN:CAA34431.1; !1PID:g35071 COMMENT This NAD-dependent enzyme catalyzes the oxidation of 5, !110-methylenetetrahydrofolate and the subsequent hydrolysis, !1which results in the formation of 10-formyltetrahydrofolate. !1It is homologous to the NADP-dependent !1methylenetetrahydrofolate dehydrogenase-cyclohydrolase. !1However, the two enzymes are immunologically and kinetically !1distinct. CLASSIFICATION #superfamily methylenetetrahydrofolate dehydrogenase (NAD+); !1methylenetetrahydrofolate dehydrogenase (NAD+) homology KEYWORDS homodimer; hydrolase; mitochondrion; multifunctional enzyme; !1NAD; oxidoreductase FEATURE !$1-29 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$30-344 #product methylenetetrahydrofolate dehydrogenase !8(NAD+) / methenyltetrahydrofolate cyclohydrolase !8#status predicted #label MAT\ !$33-323 #domain methylenetetrahydrofolate dehydrogenase !8(NAD+) homology #label MTFD SUMMARY #length 344 #molecular-weight 37320 #checksum 5347 SEQUENCE /// ENTRY A33267 #type complete TITLE methylenetetrahydrofolate dehydrogenase (NAD) (EC 1.5.1.15) / methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9) precursor - mouse ALTERNATE_NAMES methylenetetrahydrofolate dehydrogenase-cyclohydrolase, NAD-dependent ORGANISM #formal_name Mus musculus #common_name house mouse DATE 22-Nov-1989 #sequence_revision 05-Apr-1995 #text_change 03-Jun-2002 ACCESSIONS A33267; B33267; S70754 REFERENCE A33267 !$#authors Belanger, C.; MacKenzie, R.E. !$#journal J. Biol. Chem. (1989) 264:4837-4843 !$#title Isolation and characterization of cDNA clones encoding the !1murine NAD-dependent methylenetetrahydrofolate !1dehydrogenase-methenyltetrahydrofolate cyclohydrolase. !$#cross-references MUID:89174757; PMID:2647744 !$#accession A33267 !'##molecule_type mRNA !'##residues 1-350 ##label BEL1 !'##cross-references GB:J04627; NID:g200070; PIDN:AAA39827.1; !1PID:g200071 !$#accession B33267 !'##molecule_type protein !'##residues 35-54 ##label BEL2 REFERENCE S70754 !$#authors Belanger, C.; Peri, K.; MacKenzie, R.E. !$#journal Nucleic Acids Res. (1991) 19:4341-4345 !$#title Analysis of the promoter region of the gene encoding !1NAD-dependent methylenetetrahydrofolate !1dehydrogenase-methenyltetrahydrofolate cyclohydrolase. !$#cross-references MUID:91360330; PMID:1843253 !$#accession S70754 !'##status preliminary; translation not shown !'##molecule_type DNA !'##residues 1-33 ##label BEL !'##cross-references EMBL:M74185 COMMENT This NAD-dependent enzyme catalyzes the oxidation of 5, !110-methylenetetrahydrofolate and the subsequent hydrolysis, !1which results in the formation of 10-formyltetrahydrofolate. !1It is homologous to the NADP-dependent !1methylenetetrahydrofolate dehydrogenase-cyclohydrolase. !1However, the two enzymes are immunologically and kinetically !1distinct. CLASSIFICATION #superfamily methylenetetrahydrofolate dehydrogenase (NAD+); !1methylenetetrahydrofolate dehydrogenase (NAD+) homology KEYWORDS homodimer; hydrolase; mitochondrion; multifunctional enzyme; !1NAD; oxidoreductase FEATURE !$1-34 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$35-350 #product methylenetetrahydrofolate dehydrogenase !8(NAD+) / methenyltetrahydrofolate cyclohydrolase !8#status experimental #label MAT\ !$39-329 #domain methylenetetrahydrofolate dehydrogenase !8(NAD+) homology #label MTFD SUMMARY #length 350 #molecular-weight 37863 #checksum 7217 SEQUENCE /// ENTRY S32562 #type complete TITLE methylenetetrahydrofolate dehydrogenase (NAD) (EC 1.5.1.15) / methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9) precursor - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES methylenetetrahydrofolate dehydrogenase-cyclohydrolase, NAD-dependent ORGANISM #formal_name Drosophila melanogaster DATE 22-Nov-1993 #sequence_revision 05-Apr-1995 #text_change 03-Jun-2002 ACCESSIONS S32562 REFERENCE S32562 !$#authors Price, B.D.; Laughon, A. !$#journal Biochim. Biophys. Acta (1993) 1173:94-98 !$#title The isolation and characterization of a Drosophila gene !1encoding a putative NAD-dependent methylenetetrahydrofolate !1dehydrogenase-methenyltetrahydrofolate cyclohydrolase. !$#cross-references MUID:93250056; PMID:8485162 !$#accession S32562 !'##molecule_type mRNA !'##residues 1-357 ##label PRI !'##cross-references EMBL:L07958; NID:g157971; PIDN:AAB41352.1; !1PID:g157972 COMMENT This NAD-dependent enzyme catalyzes the oxidation of 5, !110-methylenetetrahydrofolate and the subsequent hydrolysis, !1which results in the formation of 10-formyltetrahydrofolate. !1It is homologous to the NADP-dependent !1methylenetetrahydrofolate dehydrogenase-cyclohydrolase. !1However, the two enzymes are immunologically and kinetically !1distinct. GENETICS !$#gene FlyBase:Nmdmc !'##cross-references FlyBase:FBgn0010222 CLASSIFICATION #superfamily methylenetetrahydrofolate dehydrogenase (NAD+); !1methylenetetrahydrofolate dehydrogenase (NAD+) homology KEYWORDS homodimer; hydrolase; mitochondrion; multifunctional enzyme; !1NAD; oxidoreductase FEATURE !$1-53 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$54-357 #product methylenetetrahydrofolate dehydrogenase !8(NAD+) / methenyltetrahydrofolate cyclohydrolase !8#status predicted #label MAT\ !$58-348 #domain methylenetetrahydrofolate dehydrogenase !8(NAD+) homology #label MTFD SUMMARY #length 357 #molecular-weight 38759 #checksum 8219 SEQUENCE /// ENTRY JS0662 #type complete TITLE methylenetetrahydrofolate dehydrogenase (NADP) (EC 1.5.1.5) / methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9) [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES bifunctional enzyme folD ORGANISM #formal_name Escherichia coli DATE 17-Jul-1992 #sequence_revision 31-Oct-1997 #text_change 03-Jun-2002 ACCESSIONS H64784; JS0662; PS0334; S35893; I41117 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64784 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-288 ##label BLAT !'##cross-references GB:AE000159; GB:U00096; NID:g1786739; !1PIDN:AAC73631.1; PID:g1786741; UWGP:b0529 !'##experimental_source strain K-12, substrain MG1655 REFERENCE JS0662 !$#authors D'Ari, L.; Rabinowitz, J.C. !$#journal J. Biol. Chem. (1991) 266:23953-23958 !$#title Purification, characterization, cloning, and amino acid !1sequence of the bifunctional enzyme 5, !110-methylenetetrahydrofolate dehydrogenase/5, !110-methenyltetrahydrofolate cyclohydrolase from Escherichia !1coli. !$#cross-references MUID:92084696; PMID:1748668 !$#accession JS0662 !'##molecule_type DNA !'##residues 1-199,'L',201-288 ##label DAR !'##cross-references GB:M74789; NID:g146010; PIDN:AAA23803.1; !1PID:g146011 !$#accession PS0334 !'##molecule_type protein !'##residues 2-36 ##label DAR1 REFERENCE S35893 !$#authors Yonetani, Y.; Sanpei, G.; Mizobuchi, K. !$#submission submitted to the EMBL Data Library, July 1992 !$#description Cloning and nucleotide sequence ananlysis of a novel !1adeninesensitive mutation of Escherichia coli strain K12 !1W3110. !$#accession S35893 !'##molecule_type DNA !'##residues 1-288 ##label YON !'##cross-references EMBL:D10588; NID:g216520; PIDN:BAA01445.1; !1PID:g216521 REFERENCE I41117 !$#authors Rossolini, G.M.; Muscas, P.; Chiesurin, A.; Satta, G. !$#journal FEMS Microbiol. Lett. (1994) 119:321-328 !$#title fimA-folD genes linkage in Salmonella identifies a putative !1junctional site of chromosomal rearrangement in the !1enterobacterial genome. !$#cross-references MUID:94327079; PMID:8050713 !$#accession I41117 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-288 ##label RES !'##cross-references GB:D10588; NID:g216520; PIDN:BAA01445.1; !1PID:g216521 GENETICS !$#gene folD; ads !$#map_position 12 min COMPLEX homodimer FUNCTION !$#description EC 1.5.1.5 / EC 3.5.4.9 [validated, MUID:92084696] !$#note homologous to the NAD-dependent methylenetetrahydrofolate !1dehydrogenase-cyclohydrolase; however, the two enzymes are !1immunologically and kinetically distinct CLASSIFICATION #superfamily methylenetetrahydrofolate dehydrogenase (NAD+); !1methylenetetrahydrofolate dehydrogenase (NAD+) homology KEYWORDS homodimer; hydrolase; multifunctional enzyme; NADP; !1oxidoreductase FEATURE !$2-288 #product methylenetetrahydrofolate dehydrogenase !8(NADP+) / methenyltetrahydrofolate cyclohydrolase !8#status experimental #label MAT\ !$5-280 #domain methylenetetrahydrofolate dehydrogenase !8(NAD+) homology #label MTFD SUMMARY #length 288 #molecular-weight 31043 #checksum 9732 SEQUENCE /// ENTRY A64081 #type complete TITLE methylenetetrahydrofolate dehydrogenase (NADP) (EC 1.5.1.5) / methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9) - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS A64081 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession A64081 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-282 ##label TIGR !'##cross-references GB:U32743; GB:L42023; NID:g1573597; !1PIDN:AAC22268.1; PID:g1573602; TIGR:HI0609 CLASSIFICATION #superfamily methylenetetrahydrofolate dehydrogenase (NAD+); !1methylenetetrahydrofolate dehydrogenase (NAD+) homology KEYWORDS hydrolase; multifunctional enzyme; NADP; oxidoreductase FEATURE !$5-279 #domain methylenetetrahydrofolate dehydrogenase !8(NAD+) homology #label MTFD SUMMARY #length 282 #molecular-weight 30460 #checksum 5924 SEQUENCE /// ENTRY S36633 #type complete TITLE methylenetetrahydrofolate dehydrogenase (NADP) (EC 1.5.1.5) / methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9) - Salmonella typhi ORGANISM #formal_name Salmonella typhi DATE 09-Dec-1993 #sequence_revision 05-Apr-1995 #text_change 03-Jun-2002 ACCESSIONS S36633 REFERENCE S36632 !$#authors Rossolini, G.M.; Muscas, P.; Chiesurin, A.; Satta, G. !$#submission submitted to the EMBL Data Library, August 1993 !$#accession S36633 !'##molecule_type DNA !'##residues 1-288 ##label ROS !'##cross-references EMBL:X74603; NID:g397534; PIDN:CAA52683.1; !1PID:g397535 COMMENT This NADH-dependent enzyme catalyzes the oxidation of 5, !110-methylenetetrahydrofolate and the subsequent hydrolysis, !1which results in the formation of 10-formyltetrahydrofolate. !1It is homologous to the NAD-dependent !1methylenetetrahydrofolate dehydrogenase-cyclohydrolase. !1However, the two enzymes are immunologically and kinetically !1distinct. CLASSIFICATION #superfamily methylenetetrahydrofolate dehydrogenase (NAD+); !1methylenetetrahydrofolate dehydrogenase (NAD+) homology KEYWORDS homodimer; hydrolase; multifunctional enzyme; NADP; !1oxidoreductase FEATURE !$2-288 #product methylenetetrahydrofolate dehydrogenase !8(NADP+) / methenyltetrahydrofolate cyclohydrolase !8#status predicted #label MAT\ !$5-280 #domain methylenetetrahydrofolate dehydrogenase !8(NAD+) homology #label MTFD SUMMARY #length 288 #molecular-weight 30824 #checksum 9465 SEQUENCE /// ENTRY S31254 #type complete TITLE methylenetetrahydrofolate dehydrogenase (NAD) (EC 1.5.1.15) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YKR080w; protein YKR400 ORGANISM #formal_name Saccharomyces cerevisiae DATE 28-May-1993 #sequence_revision 05-Apr-1995 #text_change 03-Jun-2002 ACCESSIONS S31254; S31466; S38157; S38158; S42009; S39121 REFERENCE S31254 !$#authors West, M.G.; Barlowe, C.K.; Appling, D.R. !$#journal J. Biol. Chem. (1993) 268:153-160 !$#title Cloning and characterization of the Saccharomyces cerevisiae !1gene encoding NAD-dependent 5,10-methylenetetrahydrofolate !1dehydrogenase. !$#cross-references MUID:93106993; PMID:8416923 !$#accession S31254 !'##molecule_type DNA !'##residues 1-320 ##label WES !'##cross-references EMBL:L02934; NID:g172015; PIDN:AAB00323.1; !1PID:g172016 !$#accession S31466 !'##molecule_type protein !'##residues 72-86;146-160 ##label WE2 REFERENCE S37897 !$#authors Pohl, T.M.; Pohl, F.M. !$#submission submitted to the Protein Sequence Database, March 1994 !$#accession S38157 !'##molecule_type DNA !'##residues 1-254 ##label POH !'##cross-references EMBL:Z28305; GSPDB:GN00011; MIPS:YKR080w !'##experimental_source strain S288C REFERENCE S38158 !$#authors Baladron, V.; Ballesta, J.P.G.; Bou, G.; del Rey, F.; !1Esteban, P.F.; Garcia-Cantalejo, J.M.; Garcia-Ramirez, J.J.; !1Gonzalez, A.; Jimenez, A.; Revuelta, J.L.; Santos, M.A. !$#submission submitted to the Protein Sequence Database, March 1994 !$#accession S38158 !'##molecule_type DNA !'##residues 107-320 ##label BAL !'##cross-references EMBL:Z28305; GSPDB:GN00011; MIPS:YKR080w REFERENCE S42009 !$#authors Garcia-Cantalejo, J.; Baladron, V.; Esteban, P.F.; Santos, !1M.A.; Bou, G.; Remacha, M.A.; Revuelta, J.L.; Ballesta, !1J.P.G.; Jimenez, A.; del Rey, F. !$#journal Yeast (1994) 10:231-245 !$#title The complete sequence of an 18,002 bp segment of !1Saccharomyces cerevisiae chromosome XI contains the HBS1, !1MRP-L20 and PRP16 genes, and six new open reading frames. !$#cross-references MUID:94262327; PMID:8203164 !$#accession S42009 !'##status translation not shown !'##molecule_type DNA !'##residues 1-161 ##label GAR !'##cross-references EMBL:Z27116 COMMENT This NAD-dependent enzyme catalyzes the oxidation of 5, !110-methylenetetrahydrofolate; it is a monofunctional !1cytoplasmic enzyme. GENETICS !$#gene SGD:MTD1; MIPS:YKR080w !'##cross-references SGD:S0001788; MIPS:YKR080w !$#map_position 11R CLASSIFICATION #superfamily methylenetetrahydrofolate dehydrogenase (NAD+); !1methylenetetrahydrofolate dehydrogenase (NAD+) homology KEYWORDS homodimer; hydrolase; NAD; oxidoreductase FEATURE !$8-312 #domain methylenetetrahydrofolate dehydrogenase !8(NAD+) homology #label MTFD SUMMARY #length 320 #molecular-weight 36239 #checksum 9893 SEQUENCE /// ENTRY DEAGLT #type complete TITLE D-octopine dehydrogenase (EC 1.5.1.11) - Agrobacterium tumefaciens plasmids ALTERNATE_NAMES D-lysopine synthase; octopine synthase CONTAINS D-lysopine dehydrogenase (EC 1.5.1.16) ORGANISM #formal_name Agrobacterium tumefaciens DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 11-Jun-1999 ACCESSIONS A00399; S28694 REFERENCE A00399 !$#authors De Greve, H.; Dhaese, P.; Seurinck, J.; Lemmers, M.; Van !1Montagu, M.; Schell, J. !$#journal J. Mol. Appl. Genet. (1982) 1:499-511 !$#title Nucleotide sequence and transcript map of the Agrobacterium !1tumefaciens Ti plasmid-encoded octopine synthase gene. !$#cross-references MUID:83110646; PMID:7153687 !$#accession A00399 !'##molecule_type DNA !'##residues 1-358 ##label DEG !'##cross-references GB:V00088; GB:J01820; NID:g39109; PIDN:CAA23428.1; !1PID:g39110 !'##experimental_source plasmid pTiAch5 REFERENCE S28683 !$#authors Barker, R.F.; Idler, K.B.; Thompson, D.V.; Kemp, J.D. !$#journal Plant Mol. Biol. (1983) 2:335-350 !$#title Nucleotide sequence of the T-DNA region from the !1Agrobacterium tumefaciens octopine Ti plasmid pTi15955. !$#accession S28694 !'##status translation not shown !'##molecule_type DNA !'##residues 1-358 ##label BAR !'##cross-references EMBL:X00493; NID:g39062; PIDN:CAA25174.1; !1PID:g39074 !'##experimental_source plasmid pTi15955 GENETICS !$#genome plasmid !$#note the Agrobacterium Ti plasmid induces tumor (crown gall) in !1dicotyledonous plants by transferring a plasmid segment from !1the bacteria to the plant cell; two or more functions !1encoded by this DNA segment (T-DNA) are specifically !1expressed in the plant cell nucleus FUNCTION !$#description catalyzes the reductive condensation of pyruvate and !1arginine, lysine, histidine, or ornithine to form octopine, !1lysopine, histopine, or octopinic acid, respectively, using !1NADPH !$#note 2-oxobutanoate and glyoxylate can be used as alternative !1alpha-ketoacids; NADH can be used as an alternative cofactor CLASSIFICATION #superfamily D-octopine dehydrogenase KEYWORDS crown gall tumor; oxidoreductase SUMMARY #length 358 #molecular-weight 38797 #checksum 8633 SEQUENCE /// ENTRY S30109 #type complete TITLE D-vitopine dehydrogenase (EC 1.5.1.-) - Agrobacterium vitis plasmid pTiS4 ALTERNATE_NAMES vitopine synthase ORGANISM #formal_name Agrobacterium vitis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S30109 REFERENCE S30104 !$#authors Canaday, J.; Gerard, J.C.; Crouzet, P.; Otten, L. !$#journal Mol. Gen. Genet. (1992) 235:292-303 !$#title Organization and functional analysis of three T-DNAs from !1the vitopine Ti plasmid pTiS4. !$#cross-references MUID:93101133; PMID:1465104 !$#accession S30109 !'##molecule_type DNA !'##residues 1-360 ##label CAN !'##cross-references EMBL:M91608; NID:g149132; PIDN:AAA25044.1; !1PID:g149134 GENETICS !$#genome plasmid CLASSIFICATION #superfamily D-octopine dehydrogenase KEYWORDS crown gall tumor; oxidoreductase SUMMARY #length 360 #molecular-weight 39700 #checksum 7775 SEQUENCE /// ENTRY DEAGNT #type complete TITLE D-nopaline dehydrogenase (EC 1.5.1.19) - Agrobacterium tumefaciens plasmid pTiT37 ALTERNATE_NAMES D-nopaline synthase ORGANISM #formal_name Agrobacterium tumefaciens DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 28-May-1999 ACCESSIONS A92833; A93471; A00400 REFERENCE A92833 !$#authors Depicker, A.; Stachel, S.; Dhaese, P.; Zambryski, P.; !1Goodman, H.M. !$#journal J. Mol. Appl. Genet. (1982) 1:561-573 !$#title Nopaline synthase: transcript mapping and DNA sequence. !$#cross-references MUID:83110651; PMID:7153689 !$#accession A92833 !'##molecule_type DNA !'##residues 1-413 ##label DEP !'##cross-references GB:V00087; GB:J01541; NID:g39105; PIDN:CAA23427.1; !1PID:g39106 REFERENCE A93471 !$#authors Bevan, M.; Barnes, W.M.; Chilton, M.D. !$#journal Nucleic Acids Res. (1983) 11:369-385 !$#title Structure and transcription of the nopaline synthase gene !1region of T-DNA. !$#cross-references MUID:83143308; PMID:6298724 !$#accession A93471 !'##molecule_type DNA !'##residues 1-221,'Y',223-358,'K',360-361,'I',363-413 ##label BEV COMMENT This enzyme catalyzes the formation of nopaline by the !1reductive condensation of alpha-ketoglutaric acid and !1arginine. COMMENT The Ti plasmid in Agrobacterium induces tumor (crown gall) !1in dicotyledonous plants by transferring a plasmid segment !1from the bacteria to the plant cell. Two or more functions !1encoded by this DNA segment (T-DNA) are specifically !1expressed in the plant cell nucleus. GENETICS !$#gene nos !$#genome plasmid CLASSIFICATION #superfamily D-octopine dehydrogenase KEYWORDS crown gall tumor; oxidoreductase SUMMARY #length 413 #molecular-weight 45386 #checksum 3469 SEQUENCE /// ENTRY S46512 #type complete TITLE D-nopaline dehydrogenase (EC 1.5.1.19) [similarity] - Agrobacterium tumefaciens ALTERNATE_NAMES nopaline synthase ORGANISM #formal_name Agrobacterium tumefaciens DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS S46512 REFERENCE S46509 !$#authors Drevet, C.; Brasileiro, A.C.M.; Jouanin, L. !$#journal Plant Mol. Biol. (1994) 25:83-90 !$#title Oncogene arrangement in a shooty strain of Agrobacterium !1tumefaciens. !$#cross-references MUID:94272016; PMID:8003699 !$#accession S46512 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-412 ##label DRE !'##cross-references EMBL:X74123; NID:g510732; PIDN:CAA52223.1; !1PID:g510736 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1993 CLASSIFICATION #superfamily D-octopine dehydrogenase KEYWORDS crown gall tumor; oxidoreductase SUMMARY #length 412 #molecular-weight 45306 #checksum 6301 SEQUENCE /// ENTRY S41895 #type complete TITLE D-nopaline dehydrogenase (EC 1.5.1.19) - Agrobacterium vitis ALTERNATE_NAMES nopaline synthase ORGANISM #formal_name Agrobacterium vitis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S41895 REFERENCE S41891 !$#authors Otten, L.; Ruffray, P. !$#submission submitted to the EMBL Data Library, January 1994 !$#description Agrobacterium vitis nopaline Ti plasmid pTiAB4: relationship !1to other Ti plasmids and T-DNA analysis. !$#accession S41895 !'##status preliminary !'##molecule_type DNA !'##residues 1-412 ##label OTT !'##cross-references EMBL:X77327; NID:g452715; PIDN:CAA54543.1; !1PID:g452720 CLASSIFICATION #superfamily D-octopine dehydrogenase KEYWORDS crown gall tumor; oxidoreductase SUMMARY #length 412 #molecular-weight 45278 #checksum 6083 SEQUENCE /// ENTRY DEIQHN #type complete TITLE (R)-6-hydroxynicotine oxidase (EC 1.5.3.6) - Arthrobacter oxydans ALTERNATE_NAMES 6-hydroxy-D-nicotine oxidase ORGANISM #formal_name Arthrobacter oxydans DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 09-Apr-1999 ACCESSIONS S00087; S00017 REFERENCE S00087 !$#authors Brandsch, R.; Hinkkanen, A.E.; Mauch, L.; Nagursky, H.; !1Decker, K. !$#journal Eur. J. Biochem. (1987) 167:315-320 !$#title 6-Hydroxy-D-nicotine oxidase of Arthrobacter oxidans. Gene !1structure of the flavoenzyme and its relationship to !16-hydroxy-L-nicotine oxidase. !$#cross-references MUID:87304263; PMID:3622516 !$#accession S00087 !'##molecule_type DNA !'##residues 1-443 ##label BRA !'##cross-references EMBL:X05999 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily (R)-6-hydroxynicotine oxidase KEYWORDS FAD; flavoprotein; oxidoreductase; phosphoprotein FEATURE !$71 #modified_site 3'-FAD-histidine (His) #status !8experimental SUMMARY #length 443 #molecular-weight 48161 #checksum 3217 SEQUENCE /// ENTRY DEECXA #type complete TITLE NAD(P) transhydrogenase (B-specific) (EC 1.6.1.1) alpha chain - Escherichia coli (strain K-12) ALTERNATE_NAMES pyridine nucleotide transhydrogenase alpha chain ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 19-May-1995 #text_change 03-Jun-2002 ACCESSIONS S24380; A25012; E64916; S18355; S23833 REFERENCE S24380 !$#authors Ahmad, S.; Glavas, N.A.; Bragg, P.D. !$#journal Eur. J. Biochem. (1992) 207:733-739 !$#title A mutation at Gly314 of the beta subunit of the Escherichia !1coli pyridine nucleotide transhydrogenase abolishes activity !1and affects the NADP(H)-induced conformational change. !$#cross-references MUID:92339464; PMID:1633824 !$#accession S24380 !'##molecule_type DNA !'##residues 1-510 ##label AHM !'##cross-references EMBL:X66086; NID:g42455; PIDN:CAA46884.1; !1PID:g42456 REFERENCE A91172 !$#authors Clarke, D.M.; Loo, T.W.; Gillam, S.; Bragg, P.D. !$#journal Eur. J. Biochem. (1986) 158:647-653 !$#title Nucleotide sequence of the pntA and pntB genes encoding the !1pyridine nucleotide transhydrogenase of Escherichia coli. !$#cross-references MUID:86274751; PMID:3525165 !$#accession A25012 !'##molecule_type DNA !'##residues 1-39,'VNWQVLTIKRLCSG',56-328,'R',330-502 ##label CLA REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64916 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-510 ##label BLAT !'##cross-references GB:AE000255; GB:U00096; NID:g1787875; !1PIDN:AAC74675.1; PID:g1787887; UWGP:b1603 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S18355 !$#authors Tong, R.C.W.; Glavas, N.A.; Bragg, P.D. !$#journal Biochim. Biophys. Acta (1991) 1080:19-28 !$#title Topological analysis of the pyridine nucleotide !1transhydrogenase of Escherichia coli using proteolytic !1enzymes. !$#cross-references MUID:92031646; PMID:1932078 !$#accession S18355 !'##molecule_type protein !'##residues 1-10;16-25;'XF','ISV',136-138,225,'FGT';229-238;270-273, !1'X',275-278;'AG',279-285 ##label TON GENETICS !$#gene pntA !$#map_position 35 min COMPLEX heterotetramer; two alpha and two beta chains FUNCTION !$#description catalyzes the reversible hydride ion transfer between NAD !1and NADP; this transhydrogenation is coupled to respiration !1and ATP hydrolysis and functions as a proton pump across the !1membrane !$#pathway NAD phosphorylation and dephosphorylation CLASSIFICATION #superfamily NAD(P)+ transhydrogenase (B-specific) alpha !1chain; alanine dehydrogenase homology; NAD(P)+ !1transhydrogenase (B-specific) alpha chain homology KEYWORDS heterotetramer; inner membrane; transmembrane protein; NAD; !1NADP; oxidoreductase FEATURE !$1-509 #domain NAD(P)+ transhydrogenase (B-specific) alpha !8chain homology #label TBA\ !$1-295 #domain alanine dehydrogenase homology #label ALA\ !$167-195 #region beta-alpha-beta NAD nucleotide-binding fold\ !$404-420 #domain transmembrane #status predicted #label TM1\ !$429-445 #domain transmembrane #status predicted #label TM2\ !$453-469 #domain transmembrane #status predicted #label TM3\ !$478-494 #domain transmembrane #status predicted #label TM4 SUMMARY #length 510 #molecular-weight 54623 #checksum 4889 SEQUENCE /// ENTRY DEECXB #type complete TITLE NAD(P) transhydrogenase (B-specific) (EC 1.6.1.1) beta chain - Escherichia coli (strain K-12) ALTERNATE_NAMES pyridine nucleotide transhydrogenase beta chain ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 03-Nov-1995 #text_change 03-Jun-2002 ACCESSIONS S24381; B25012; S18427; D64916; S23834 REFERENCE S24380 !$#authors Ahmad, S.; Glavas, N.A.; Bragg, P.D. !$#journal Eur. J. Biochem. (1992) 207:733-739 !$#title A mutation at Gly314 of the beta subunit of the Escherichia !1coli pyridine nucleotide transhydrogenase abolishes activity !1and affects the NADP(H)-induced conformational change. !$#cross-references MUID:92339464; PMID:1633824 !$#accession S24381 !'##molecule_type DNA !'##residues 1-462 ##label AHM !'##cross-references EMBL:X66086; NID:g42455; PIDN:CAA46885.1; !1PID:g42457 REFERENCE A91172 !$#authors Clarke, D.M.; Loo, T.W.; Gillam, S.; Bragg, P.D. !$#journal Eur. J. Biochem. (1986) 158:647-653 !$#title Nucleotide sequence of the pntA and pntB genes encoding the !1pyridine nucleotide transhydrogenase of Escherichia coli. !$#cross-references MUID:86274751; PMID:3525165 !$#accession B25012 !'##molecule_type DNA !'##residues 1-220,'AELVLRLGGCGCGLYAQQRPV',242-462 ##label CLA !'##cross-references GB:D10005; GB:D00008; GB:X04195; NID:g216613; !1PIDN:BAA00896.1; PID:g216615 REFERENCE S18355 !$#authors Tong, R.C.W.; Glavas, N.A.; Bragg, P.D. !$#journal Biochim. Biophys. Acta (1991) 1080:19-28 !$#title Topological analysis of the pyridine nucleotide !1transhydrogenase of Escherichia coli using proteolytic !1enzymes. !$#cross-references MUID:92031646; PMID:1932078 !$#accession S18427 !'##molecule_type protein !'##residues 266-277;364-373 ##label TON REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64916 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-462 ##label BLAT !'##cross-references GB:AE000255; GB:U00096; NID:g1787875; !1PIDN:AAC74674.1; PID:g1787886; UWGP:b1602 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene pntB !$#map_position 35 min COMPLEX heterotetramer; two alpha and two beta chains FUNCTION !$#description catalyzes the reversible hydride ion transfer between NAD !1and NADP; this transhydrogenation is coupled to respiration !1and ATP hydrolysis and functions as a proton pump across the !1membrane !$#pathway NAD phosphorylation and dephosphorylation CLASSIFICATION #superfamily NAD(P)+ transhydrogenase (B-specific) beta !1chain; NAD(P)+ transhydrogenase (B-specific) beta chain !1homology KEYWORDS heterotetramer; inner membrane; transmembrane protein; NAD; !1NADP; oxidoreductase FEATURE !$5-21 #domain transmembrane #status predicted #label TM1\ !$21-462 #domain NAD(P)+ transhydrogenase (B-specific) beta !8chain homology #label TBB\ !$36-52 #domain transmembrane #status predicted #label TM2\ !$59-75 #domain transmembrane #status predicted #label TM3\ !$86-102 #domain transmembrane #status predicted #label TM4\ !$125-141 #domain transmembrane #status predicted #label TM5\ !$163-179 #domain transmembrane #status predicted #label TM6\ !$184-200 #domain transmembrane #status predicted #label TM7\ !$205-221 #domain transmembrane #status predicted #label TM8\ !$240-256 #domain transmembrane #status predicted #label TM9 SUMMARY #length 462 #molecular-weight 48723 #checksum 1046 SEQUENCE /// ENTRY DEBOXM #type complete TITLE NAD(P) transhydrogenase (B-specific) (EC 1.6.1.1) precursor, mitochondrial - bovine ALTERNATE_NAMES nicotinamide nucleotide transhydrogenase; pyridine nucleotide transhydrogenase ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Mar-1989 #sequence_revision 22-Apr-1995 #text_change 03-Jun-2002 ACCESSIONS A31670; A29925; B29925; A47484; A54044; S02205 REFERENCE A31670 !$#authors Yamaguchi, M.; Hatefi, Y.; Trach, K.; Hoch, J.A. !$#journal Biochem. Biophys. Res. Commun. (1988) 157:24-29 !$#title Amino acid sequence of the signal peptide of mitochondrial !1nicotinamide nucleotide transhydrogenase as determined from !1the sequence of its messenger RNA. !$#cross-references MUID:89061718; PMID:3196335 !$#accession A31670 !'##molecule_type mRNA !'##residues 1-75 ##label YA3 !'##cross-references GB:M22754; NID:g163557; PIDN:AAA30717.1; !1PID:g163558 REFERENCE A29925 !$#authors Yamaguchi, M.; Hatefi, Y.; Trach, K.; Hoch, J.A. !$#journal J. Biol. Chem. (1988) 263:2761-2767 !$#title The primary structure of the mitochondrial energy-linked !1nicotinamide nucleotide transhydrogenase deduced from the !1sequence of cDNA clones. !$#cross-references MUID:88139323; PMID:3277960 !$#accession A29925 !'##molecule_type protein !'##residues 'S',45-58 ##label YAM !$#accession B29925 !'##molecule_type mRNA !'##residues 52-1086 ##label YA2 !'##cross-references GB:J03534 REFERENCE A47484 !$#authors Wakabayashi, S.; Hatefi, Y. !$#journal Biochem. Int. (1987) 15:915-924 !$#title Characterization of the substrate-binding sites of the !1mitochondrial nicotinamide nucleotide transhydrogenase. !$#cross-references MUID:88134323; PMID:3325062 !$#accession A47484 !'##molecule_type protein !'##residues 280-287,'X',289-290;1044-1049 ##label WA2 REFERENCE A54044 !$#authors Holmberg, E.; Olausson, T.; Hultman, T.; Rydstroem, J.; !1Ahmad, S.; Glavas, N.A.; Bragg, P.D. !$#journal Biochemistry (1994) 33:7691-7700 !$#title Prediction and site-specific mutagenesis of residues in !1transmembrane alpha-helices of proton-pumping nicotinamide !1nucleotide transhydrogenases from Escherichia coli and !1bovine heart mitochondria. !$#cross-references MUID:94281199; PMID:8011636 !$#accession A54044 !'##status preliminary !'##molecule_type mRNA !'##residues 444-633,'A',635-662,'I',664-819,'V',821-824,'A',826-893 !1##label HHO !'##cross-references GB:L02543 REFERENCE S02205 !$#authors Wakabayashi, S.; Hatefi, Y. !$#journal Biochem. Int. (1987) 15:667-675 !$#title Amino acid sequence of the NAD(H)-binding region of the !1mitochondrial nicotinamide nucleotide transhydrogenase !1modified by N,N'-dicyclohexylcarbodiimide. !$#cross-references MUID:88106658; PMID:3426633 !$#accession S02205 !'##molecule_type protein !'##residues 291-302 ##label WAK !'##experimental_source heart mitochondria GENETICS !$#genome nuclear FUNCTION !$#description catalyzes the reversible hydride ion transfer between NAD !1and NADP; this transhydrogenation is coupled to respiration !1and ATP hydrolysis and functions as a proton pump across the !1mitochondrial inner membrane. CLASSIFICATION #superfamily NAD(P)+ transhydrogenase (B-specific); alanine !1dehydrogenase homology; NAD(P)+ transhydrogenase !1(B-specific) alpha chain homology; NAD(P)+ transhydrogenase !1(B-specific) beta chain homology KEYWORDS homodimer; membrane protein; mitochondrion; NAD; NADP; !1oxidoreductase FEATURE !$1-43 #domain transit peptide (mitochondrion) #status !8predicted #label SIG\ !$44-1086 #product NAD(P)+transhydrogenase (B-specific), !8mitochondrial #status predicted #label MAT\ !$57-587 #domain NAD(P)+ transhydrogenase (B-specific) alpha !8chain homology #label TBA\ !$57-357 #domain alanine dehydrogenase homology #label ALA\ !$229-257 #region beta-alpha-beta NAD nucleotide-binding fold\ !$635-1080 #domain NAD(P)+ transhydrogenase (B-specific) beta !8chain homology #label TBB\ !$288 #binding_site NAD (Tyr) #status predicted\ !$1049 #binding_site NADP (Tyr) #status predicted SUMMARY #length 1086 #molecular-weight 114044 #checksum 7879 SEQUENCE /// ENTRY RDHUB5 #type complete TITLE cytochrome-b5 reductase (EC 1.6.2.2) [validated] - human ALTERNATE_NAMES NADH-cytochrome b5 reductase; NADH-ferricytochrome b5 oxidoreductase ORGANISM #formal_name Homo sapiens #common_name man DATE 25-Feb-1985 #sequence_revision 30-Sep-1993 #text_change 08-Dec-2000 ACCESSIONS JS0468; A60813; A26616; B26616; PX0015; JS0003; A00401 REFERENCE JS0468 !$#authors Tomatsu, S.; Kobayashi, Y.; Fukumaki, Y.; Yubisui, T.; Orii, !1T.; Sakaki, Y. !$#journal Gene (1989) 80:353-361 !$#title The organization and the complete nucleotide sequence of the !1human NADH-cytochrome b5 reductase gene. !$#cross-references MUID:90060784; PMID:2479590 !$#accession JS0468 !'##molecule_type DNA !'##residues 1-301 ##label TOM !'##cross-references GB:M28705; NID:g341971 !'##note the authors' translation is shown for the codon CCA at residue !166-Ser !'##note this translation is not annotated in GenBank entry HUMNADHCY1, !1release 109.0 REFERENCE A60813 !$#authors Bull, P.C.; Shephard, E.A.; Povey, S.; Santisteban, I.; !1Phillips, I.R. !$#journal Ann. Hum. Genet. (1988) 52:263-268 !$#title Cloning and chromosomal mapping of human cytochrome b-5 !1reductase (DIA1). !$#cross-references MUID:90024910; PMID:3268037 !$#accession A60813 !'##molecule_type mRNA !'##residues 188-301 ##label BUL REFERENCE A94154 !$#authors Yubisui, T.; Naitoh, Y.; Zenno, S.; Tamura, M.; Takeshita, !1M.; Sakaki, Y. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:3609-3613 !$#title Molecular cloning of cDNAs of human liver and placenta !1NADH-cytochrome b-5 reductase. !$#cross-references MUID:87231867; PMID:3035541 !$#accession A26616 !'##molecule_type mRNA !'##residues 8-240 ##label YUB !'##cross-references GB:M16461 !$#accession B26616 !'##molecule_type mRNA !'##residues 'RWPRAALA',36-65,'P',67-301 ##label YU3 !'##cross-references GB:M16462; NID:g181556; PIDN:AAA52307.1; !1PID:g181557 !'##note the authors translated the codon CCA for residue 39 as Ser !'##note the initial sequence differences may be a cloning artifact REFERENCE PX0016 !$#authors Murakami, K.; Yubisui, T.; Takeshita, M.; Miyata, T. !$#journal J. Biochem. (1989) 105:312-317 !$#title The NH2-terminal structures of human and rat liver !1microsomal NADH-cytochrome b5 reductases. !$#cross-references MUID:89255181; PMID:2498303 !$#accession PX0015 !'##molecule_type protein !'##residues 2-25 ##label MUR !'##experimental_source liver !'##note amino-terminal myristylation was observed REFERENCE A92007 !$#authors Yubisui, T.; Miyata, T.; Iwanaga, S.; Tamura, M.; Takeshita, !1M. !$#journal J. Biochem. (1986) 99:407-422 !$#title Complete amino acid sequence of NADH-cytochrome b5 reductase !1purified from human erythrocytes. !$#cross-references MUID:86195916; PMID:3700359 !$#accession JS0003 !'##molecule_type protein !'##residues 27-301 ##label YU1 !'##experimental_source erythrocyte REFERENCE A91986 !$#authors Yubisui, T.; Miyata, T.; Iwanaga, S.; Tamura, M.; Yoshida, !1S.; Takeshita, M.; Nakajima, H. !$#journal J. Biochem. (1984) 96:579-582 !$#title Amino acid sequence of NADH-cytochrome b5 reductase of human !1erythrocytes. !$#cross-references MUID:85054726; PMID:6389526 !$#accession A00401 !'##molecule_type protein !'##residues 27-301 ##label YU2 !'##experimental_source erythrocyte !'##note some of the chains began with residue 30 COMMENT Cytochrome b5 reductase exists in two forms arising from !1different posttranslational processing and possibly also !1alternative translation initiation. The longer myristylated !1form is found bound in microsome membranes. The shorter !1unmyristylated form is found in the cytoplasm of !1erythrocytes. GENETICS !$#gene GDB:DIA1 !'##cross-references GDB:119848; OMIM:250800 !$#map_position 22q13.31-22qter !$#introns 7/3; 51/3; 76/1; 111/3; 155/1; 183/1; 211/3; 245/1 FUNCTION !$#description catalyzes the reduction of 2 molecules of ferricytochrome b5 !1to ferrocytochrome b5 with 1 molecule of NADH !$#note a deficiency in this enzyme is one cause of hereditary !1methemoglobinemia CLASSIFICATION #superfamily cytochrome-b5 reductase; cytochrome-b5 !1reductase homology KEYWORDS blocked amino end; endoplasmic reticulum; FAD; lipoprotein; !1membrane protein; myristylation; NAD; oxidoreductase FEATURE !$2-301 #product cytochrome-b5 reductase, microsomal form !8#status predicted #label MATM\ !$27-301 #product cytochrome-b5 reductase, erythrocyte form !8#status experimental #label MATE\ !$47-301 #domain cytochrome-b5 reductase homology #label CBR\ !$67-97 #region FAD/NAD binding #status predicted\ !$132-162 #region FAD/NAD binding #status predicted\ !$171-206 #region FAD/NAD binding #status predicted\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status experimental SUMMARY #length 301 #molecular-weight 34235 #checksum 397 SEQUENCE /// ENTRY RDBOB5 #type complete TITLE cytochrome-b5 reductase (EC 1.6.2.2) - bovine ALTERNATE_NAMES NADH-cytochrome b5 reductase ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 08-Aug-1987 #sequence_revision 05-Apr-1995 #text_change 11-Jun-1999 ACCESSIONS A42328; A23896; A26922; A22182; A23193 REFERENCE A42328 !$#authors Strittmatter, P.; Kittler, J.M.; Coghill, J.E.; Ozols, J. !$#journal J. Biol. Chem. (1992) 267:2519-2523 !$#title Characterization of lysyl residues of NADH-cytochrome b5 !1reductase implicated in charge-pairing with active-site !1carboxyl residues of cytochrome b5 by site-directed !1mutagenesis of an expression vector for the flavoprotein. !$#cross-references MUID:92129336; PMID:1370824 !$#accession A42328 !'##molecule_type mRNA !'##residues 1-14,'V',16-133,'K',135-161,'K',163-225,'N',227-300 ##label !1STR !'##cross-references GB:M83104; GB:M81759; NID:g162940; PIDN:AAA30483.1; !1PID:g162941 !'##note sequence extracted from NCBI backbone (NCBIN:78450, !1NCBIP:78451) !'##note initiator Met not shown REFERENCE A23896 !$#authors Ozols, J.; Korza, G.; Heinemann, F.S.; Hediger, M.A.; !1Strittmatter, P. !$#journal J. Biol. Chem. (1985) 260:11953-11961 !$#title Complete amino acid sequence of steer liver microsomal !1NADH-cytochrome b5 reductase. !$#cross-references MUID:86008250; PMID:3900065 !$#accession A23896 !'##molecule_type protein !'##residues 1-300 ##label OZO !'##experimental_source Black Angus REFERENCE A26922 !$#authors Tamura, M.; Yubisui, T.; Takeshita, M.; Kawabata, S.; !1Miyata, T.; Iwanaga, S. !$#journal J. Biochem. (1987) 101:1147-1159 !$#title Structural comparison of bovine erythrocyte, brain, and !1liver NADH-cytochrome b-5 reductase by HPLC mapping. !$#cross-references MUID:88007457; PMID:3654589 !$#accession A26922 !'##molecule_type protein !'##residues 26-52 ##label TAM REFERENCE A22182 !$#authors Ozols, J.; Carr, S.A.; Strittmatter, P. !$#journal J. Biol. Chem. (1984) 259:13349-13354 !$#title Identification of the NH2-terminal blocking group of !1NADH-cytochrome b5 reductase as myristic acid and the !1complete amino acid sequence of the membrane-binding domain. !$#cross-references MUID:85030460; PMID:6436247 !$#accession A22182 !'##molecule_type protein !'##residues 1-36 ##label OZ2 !'##note identification of myristylated amino end REFERENCE A23193 !$#authors Kensil, C.R.; Hediger, M.A.; Ozols, J.; Strittmatter, P. !$#journal J. Biol. Chem. (1983) 258:14656-14663 !$#title Isolation and partial characterization of the NH2-terminal !1membrane-binding domain of NADH-cytochrome b5 reductase. !$#cross-references MUID:84061926; PMID:6643503 !$#accession A23193 !'##molecule_type protein !'##residues 16-43 ##label KEN COMMENT Cytochrome b5 reductase exists in two forms arising from !1different posttranslational processing and possibly also !1alternative translation initiation. The longer myristylated !1form is found bound in microsome membranes. The shorter !1unmyristylated form is found in the cytoplasm of !1erythrocytes. FUNCTION !$#description catalyzes the reduction of 2 molecules of ferricytochrome b5 !1to ferrocytochrome b5 with 1 molecule of NADH CLASSIFICATION #superfamily cytochrome-b5 reductase; cytochrome-b5 !1reductase homology KEYWORDS blocked amino end; endoplasmic reticulum; FAD; lipoprotein; !1membrane protein; myristylation; NAD; oxidoreductase FEATURE !$1-300 #product cytochrome-b5 reductase, microsomal form !8#status experimental #label MATM\ !$26-300 #product cytochrome-b5 reductase, erythrocyte form !8#status predicted #label MATE\ !$46-300 #domain cytochrome-b5 reductase homology #label CBR\ !$1 #modified_site myristylated amino end (Gly) #status !8experimental SUMMARY #length 300 #molecular-weight 33893 #checksum 8943 SEQUENCE /// ENTRY RDRTB5 #type complete TITLE cytochrome-b5 reductase (EC 1.6.2.2), microsomal form - rat ALTERNATE_NAMES NADH-cytochrome b5 reductase CONTAINS cytochrome-b5 reductase, erythrocyte shorter form ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1992 #sequence_revision 05-Apr-1995 #text_change 16-Jun-2000 ACCESSIONS A40495; JX0119; PX0016 REFERENCE A40495 !$#authors Pietrini, G.; Carrera, P.; Borgese, N. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:7246-7250 !$#title Two transcripts encode rat cytochrome b-5 reductase. !$#cross-references MUID:89017174; PMID:3174630 !$#accession A40495 !'##molecule_type mRNA !'##residues 1-301 ##label PIE !'##cross-references GB:J03867; NID:g203696; PIDN:AAA41008.1; !1PID:g203697 REFERENCE JX0119 !$#authors Zenno, S.; Hattori, M.; Misumi, Y.; Yubisui, T.; Sakaki, Y. !$#journal J. Biochem. (1990) 107:810-816 !$#title Molecular cloning of a cDNA encoding rat NADH-cytochrome b5 !1reductase and the corresponding gene. !$#cross-references MUID:90361681; PMID:2391344 !$#accession JX0119 !'##molecule_type mRNA !'##residues 1-104,'F',106-301 ##label ZEN !'##cross-references GB:D00636; NID:g2959435; PIDN:BAA00530.1; !1PID:g220674 REFERENCE PX0016 !$#authors Murakami, K.; Yubisui, T.; Takeshita, M.; Miyata, T. !$#journal J. Biochem. (1989) 105:312-317 !$#title The NH2-terminal structures of human and rat liver !1microsomal NADH-cytochrome b5 reductases. !$#cross-references MUID:89255181; PMID:2498303 !$#accession PX0016 !'##molecule_type protein !'##residues 2-25 ##label MUR COMMENT Cytochrome b5 reductase exists in several forms arising from !1alternative translation initiation and different !1posttranslational processing. The myristylated form is found !1in microsome membranes. Unmyristylated forms are found in !1the cytoplasm of erythrocytes. GENETICS !$#gene b5R FUNCTION !$#description catalyzes the reduction of 2 molecules of ferricytochrome b5 !1to ferrocytochrome b5 with 1 molecule of NADH CLASSIFICATION #superfamily cytochrome-b5 reductase; cytochrome-b5 !1reductase homology KEYWORDS alternative initiators; blocked amino end; endoplasmic !1reticulum; FAD; lipoprotein; membrane protein; !1myristylation; NAD; oxidoreductase FEATURE !$2-301 #product cytochrome-b5 reductase, microsomal form !8#status predicted #label MATM\ !$27-301 #product cytochrome-b5 reductase, erythrocyte shorter !8form #status predicted #label MATE\ !$47-301 #domain cytochrome-b5 reductase homology #label CBR\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status experimental SUMMARY #length 301 #molecular-weight 34140 #checksum 1724 SEQUENCE /// ENTRY A34231 #type complete TITLE sulfite reductase (NADPH2) (EC 1.8.1.2) flavoprotein - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS A34231 REFERENCE A92735 !$#authors Ostrowski, J.; Barber, M.J.; Rueger, D.C.; Miller, B.E.; !1Siegel, L.M.; Kredich, N.M. !$#journal J. Biol. Chem. (1989) 264:15796-15808 !$#title Characterization of the flavoprotein moieties of !1NADPH-sulfite reductase from Salmonella typhimurium and !1Escherichia coli. Physicochemical and catalytic properties, !1amino acid sequence deduced from DNA sequence of cysJ, and !1comparison with NADPH-cytochrome P-450 reductase. !$#cross-references MUID:89380164; PMID:2550423 !$#accession A34231 !'##molecule_type DNA !'##residues 1-599 ##label OST !'##cross-references GB:M23007; GB:J05009; GB:J05025; GB:M27145; !1NID:g153928; PIDN:AAA27046.1; PID:g153929 GENETICS !$#gene cysJ CLASSIFICATION #superfamily sulfite reductase (NADPH); flavodoxin homology; !1NADPH-ferrihemoprotein reductase homology KEYWORDS flavoprotein; NADP; oxidoreductase FEATURE !$64-598 #domain NADPH-ferrihemoprotein reductase homology !8#label FEH\ !$66-205 #domain flavodoxin homology #label FLX SUMMARY #length 599 #molecular-weight 66484 #checksum 3026 SEQUENCE /// ENTRY H65057 #type complete TITLE sulfite reductase (NADPH2) (EC 1.8.1.2) flavoprotein beta chain - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS H65057; B34231; I41185 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65057 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-599 ##label BLAT !'##cross-references GB:AE000360; GB:U00096; NID:g2367157; !1PIDN:AAC75806.1; PID:g1789123; UWGP:b2764 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A92735 !$#authors Ostrowski, J.; Barber, M.J.; Rueger, D.C.; Miller, B.E.; !1Siegel, L.M.; Kredich, N.M. !$#journal J. Biol. Chem. (1989) 264:15796-15808 !$#title Characterization of the flavoprotein moieties of !1NADPH-sulfite reductase from Salmonella typhimurium and !1Escherichia coli. Physicochemical and catalytic properties, !1amino acid sequence deduced from DNA sequence of cysJ, and !1comparison with NADPH-cytochrome P-450 reductase. !$#cross-references MUID:89380164; PMID:2550423 !$#accession B34231 !'##molecule_type DNA !'##residues 1-155,'T',157-267,'L',269-507,'E',509-599 ##label OST !'##cross-references GB:M23008; NID:g145679; PIDN:AAA23650.1; !1PID:g145680; GB:J05025; GB:J05057; GB:M27144 REFERENCE I41185 !$#authors Loudon, J.A.; Loughlin, R.E. !$#journal Gene (1992) 122:17-25 !$#title Mutagenesis and regulation of the cysJ promoter of !1Escherichia coli K-12. !$#cross-references MUID:93083978; PMID:1452024 !$#accession I41185 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-29 ##label RES !'##cross-references GB:M65058; NID:g145677; PIDN:AAA23649.1; !1PID:g145678 GENETICS !$#gene cysJ CLASSIFICATION #superfamily sulfite reductase (NADPH); flavodoxin homology; !1NADPH-ferrihemoprotein reductase homology KEYWORDS flavoprotein; NADP; oxidoreductase FEATURE !$64-598 #domain NADPH-ferrihemoprotein reductase homology !8#label FEH\ !$66-205 #domain flavodoxin homology #label FLX SUMMARY #length 599 #molecular-weight 66269 #checksum 599 SEQUENCE /// ENTRY S34190 #type complete TITLE sulfite reductase (NADPH2) (EC 1.8.1.2) flavoprotein - Thiocapsa roseopersicina ORGANISM #formal_name Thiocapsa roseopersicina DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S34190 REFERENCE S34190 !$#authors Haverkamp, T.; Gisselmann, G.; Schwenn, J.D. !$#submission submitted to the EMBL Data Library, July 1993 !$#description Structure and function of genes involved in the metabolism !1of sulfite from the sulfur oxidizing purple bacterium !1Thiocapsa roseopersicina. !$#accession S34190 !'##molecule_type DNA !'##residues 1-522 ##label HAV !'##cross-references EMBL:Z23169; NID:g1518424; PIDN:CAA80687.1; !1PID:g313351 CLASSIFICATION #superfamily sulfite reductase (NADPH); flavodoxin homology; !1NADPH-ferrihemoprotein reductase homology KEYWORDS flavoprotein; NADP; oxidoreductase FEATURE !$47-522 #domain NADPH-ferrihemoprotein reductase homology !8#status atypical #label FEH\ !$62-201 #domain flavodoxin homology #label FLX SUMMARY #length 522 #molecular-weight 57784 #checksum 1317 SEQUENCE /// ENTRY G70040 #type complete TITLE sulfite reductase (NADPH2) (EC 1.8.1.2) flavoprotein yvgR - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS G70040 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G70040 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-605 ##label KUN !'##cross-references GB:Z99121; GB:AL009126; NID:g2635827; !1PIDN:CAB15349.1; PID:g2635857 !'##experimental_source strain 168 GENETICS !$#gene yvgR CLASSIFICATION #superfamily sulfite reductase (NADPH); flavodoxin homology; !1NADPH-ferrihemoprotein reductase homology KEYWORDS flavoprotein; NADP; oxidoreductase FEATURE !$68-604 #domain NADPH-ferrihemoprotein reductase homology !8#label FEH\ !$70-209 #domain flavodoxin homology #label FLX SUMMARY #length 605 #molecular-weight 67259 #checksum 3504 SEQUENCE /// ENTRY RDRTO4 #type complete TITLE NADPH-ferrihemoprotein reductase (EC 1.6.2.4) - rat ALTERNATE_NAMES NADP-cytochrome P450 reductase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 03-Jun-2002 ACCESSIONS A36073; A00402; A25813 REFERENCE A36073 !$#authors Porter, T.D.; Beck, T.W.; Kasper, C.B. !$#journal Biochemistry (1990) 29:9814-9818 !$#title NADPH-cytochrome P-450 oxidoreductase gene organization !1correlates with structural domains of the protein. !$#cross-references MUID:91104888; PMID:2125483 !$#accession A36073 !'##molecule_type DNA !'##residues 1-678 ##label PO2 !'##cross-references GB:J05291 REFERENCE A00402 !$#authors Porter, T.D.; Kasper, C.B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:973-977 !$#title Coding nucleotide sequence of rat NADPH-cytochrome P-450 !1oxidoreductase cDNA and identification of flavin-binding !1domains. !$#cross-references MUID:85140278; PMID:3919392 !$#accession A00402 !'##molecule_type mRNA !'##residues 1-678 ##label POR !'##cross-references GB:M10068; NID:g203872; PIDN:AAA41064.1; !1PID:g203873 REFERENCE A25813 !$#authors Murakami, H.; Yabusaki, Y.; Ohkawa, H. !$#journal DNA (1986) 5:1-10 !$#title Expression of rat NADPH-cytochrome P-450 reductase cDNA in !1Saccharomyces cerevisiae. !$#cross-references MUID:86163762; PMID:3082610 !$#accession A25813 !'##molecule_type mRNA !'##residues 1-678 ##label MUR !'##cross-references GB:M12516; NID:g203878; PIDN:AAA41067.1; !1PID:g203879 COMMENT This enzyme, a membrane-bound flavoprotein containing one !1molecule each of FMN and FAD, is required for electron !1transfer to cytochrome P450 in microsomes; the FMN-binding !1domain is related to bacterial flavodoxins. GENETICS !$#introns 60/2; 76/3; 119/3; 169/3; 211/2; 241/2; 274/2; 313/2; 353/1; !1413/3; 463/3; 554/1; 602/3; 631/2 CLASSIFICATION #superfamily NADPH-ferrihemoprotein reductase; flavodoxin !1homology; NADPH-ferrihemoprotein reductase homology KEYWORDS electron transfer; endoplasmic reticulum; FAD; flavoprotein; !1FMN; membrane protein; NADP; oxidoreductase FEATURE !$1-56 #domain membrane-bound #status predicted #label MEM\ !$77-227 #domain FMN binding #status predicted #label FMN\ !$80-676 #domain NADPH-ferrihemoprotein reductase homology !8#label FEH\ !$82-224 #domain flavodoxin homology #label FLX\ !$84-95 #region FMN-phosphate binding #status predicted\ !$267-326,452-477 #domain FAD binding #status predicted #label FAD\ !$293-296 #region FAD-pyrophosphate binding #status predicted SUMMARY #length 678 #molecular-weight 76962 #checksum 4992 SEQUENCE /// ENTRY RDPGO4 #type complete TITLE NADPH-ferrihemoprotein reductase (EC 1.6.2.4) - pig ALTERNATE_NAMES NADP-cytochrome P450 reductase ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 04-Dec-1986 #sequence_revision 03-Feb-1994 #text_change 03-Jun-2002 ACCESSIONS A25584; A00403 REFERENCE A25584 !$#authors Haniu, M.; Iyanagi, T.; Miller, P.; Lee, T.D.; Shively, J.E. !$#journal Biochemistry (1986) 25:7906-7911 !$#title Complete amino acid sequence of NADPH-cytochrome P-450 !1reductase from porcine hepatic microsomes. !$#cross-references MUID:87101085; PMID:3099837 !$#accession A25584 !'##molecule_type protein !'##residues 1-677 ##label HAN REFERENCE A00403 !$#authors Vogel, F.; Lumper, L. !$#journal Biochem. J. (1986) 236:871-878 !$#title Complete structure of the hydrophilic domain in the porcine !1NADPH-cytochrome P-450 reductase. !$#cross-references MUID:87075664; PMID:3098240 !$#accession A00403 !'##molecule_type protein !'##residues 56-162,'S',164-173,'D',175-338,'A',340-377,'D',379-399,'E', !1401-445,'L',447-501,'D',503-673,'N',675-677 ##label VOG CLASSIFICATION #superfamily NADPH-ferrihemoprotein reductase; flavodoxin !1homology; NADPH-ferrihemoprotein reductase homology KEYWORDS acetylated amino end; electron transfer; endoplasmic !1reticulum; FAD; flavoprotein; FMN; membrane protein; NADP; !1oxidoreductase FEATURE !$76-126 #domain FMN binding #label FMN\ !$79-675 #domain NADPH-ferrihemoprotein reductase homology !8#label FEH\ !$81-223 #domain flavodoxin homology #label FLX\ !$451-476 #domain FAD binding #label FAD\ !$1 #modified_site acetylated amino end (Gly) #status !8experimental SUMMARY #length 677 #molecular-weight 76701 #checksum 3759 SEQUENCE /// ENTRY S31502 #type complete TITLE NADPH-ferrihemoprotein reductase (EC 1.6.2.4) - Madagascar periwinkle ORGANISM #formal_name Catharanthus roseus #common_name Madagascar periwinkle DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S31502 REFERENCE S31502 !$#authors Meijer, A.H.; Lopes Cardoso, M.I.; Voskuilen, J.T.; de Waal, !1A.; Verpoorte, R.; Hoge, J.H.C. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Isolation and characterization of a cDNA clone from !1Catharanthus roseus encoding NADPH:cytochrome P-450 !1reductase an enzyme essential for reactions catalysed by !1cytochrome P-450 monooxygenases in plants. !$#accession S31502 !'##status preliminary !'##molecule_type mRNA !'##residues 1-714 ##label MEI !'##cross-references EMBL:X69791; NID:g18138; PIDN:CAA49446.1; !1PID:g18139 CLASSIFICATION #superfamily NADPH-ferrihemoprotein reductase; flavodoxin !1homology; NADPH-ferrihemoprotein reductase homology KEYWORDS flavoprotein; NADP; oxidoreductase FEATURE !$104-713 #domain NADPH-ferrihemoprotein reductase homology !8#label FEH\ !$106-254 #domain flavodoxin homology #label FLX SUMMARY #length 714 #molecular-weight 78958 #checksum 8457 SEQUENCE /// ENTRY S38427 #type complete TITLE NADPH-ferrihemoprotein reductase (EC 1.6.2.4) - Aspergillus niger ALTERNATE_NAMES NADPH-cytochrome P450 oxidoreductase ORGANISM #formal_name Aspergillus niger DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S38427 REFERENCE S38427 !$#authors van den Brink, J.; van Zeijl, C.; van den Hondel, C.; van !1Gorcom, R. !$#submission submitted to the EMBL Data Library, October 1993 !$#description Cloning and characterization of the NADPH cytochrome P450 !1oxidoreductase (cprA) gene of Aspergillus niger. !$#accession S38427 !'##status preliminary !'##molecule_type DNA !'##residues 1-693 ##label VAN !'##cross-references EMBL:Z26938; NID:g408110; PIDN:CAA81550.1; !1PID:g408111 GENETICS !$#introns 595/3 CLASSIFICATION #superfamily NADPH-ferrihemoprotein reductase; flavodoxin !1homology; NADPH-ferrihemoprotein reductase homology KEYWORDS flavoprotein; NADP; oxidoreductase FEATURE !$66-691 #domain NADPH-ferrihemoprotein reductase homology !8#label FEH\ !$68-220 #domain flavodoxin homology #label FLX SUMMARY #length 693 #molecular-weight 77072 #checksum 9219 SEQUENCE /// ENTRY S46735 #type complete TITLE NADPH-ferrihemoprotein reductase (EC 1.6.2.4) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES NADP-cytochrome P450 reductase; protein H8179.8; protein YHR042w ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S46735; A41447; B41447 REFERENCE S46732 !$#authors Du, Z. !$#submission submitted to the EMBL Data Library, May 1994 !$#description The sequence of S. cerevisiae cosmid 8179. !$#accession S46735 !'##molecule_type DNA !'##residues 1-691 ##label DUZ !'##cross-references EMBL:U00062; NID:g488162; PIDN:AAB68904.1; !1PID:g488169; GSPDB:GN00008; MIPS:YHR042w REFERENCE A41447 !$#authors Yabusaki, Y.; Murakami, H.; Ohkawa, H. !$#journal J. Biochem. (1988) 103:1004-1010 !$#title Primary structure of Saccharomyces cerevisiae !1NADPH-cytochrome P450 reductase deduced from nucleotide !1sequence of its cloned gene. !$#cross-references MUID:89008184; PMID:3139648 !$#accession A41447 !'##molecule_type DNA !'##residues 1-422,'N',424-473,'G',475-691 ##label YAB !'##cross-references GB:D13788; GB:D00316; NID:g218452; PIDN:BAA02936.1; !1PID:g218453 !$#accession B41447 !'##molecule_type protein !'##residues 2-13;45-62 ##label YA2 GENETICS !$#gene SGD:NCP1; PRD1; SGD:S0001084 !'##cross-references MIPS:YHR042w; SGD:S0001084 !$#map_position 8R FUNCTION !$#description electron transfer; oxidoreductase CLASSIFICATION #superfamily NADPH-ferrihemoprotein reductase; flavodoxin !1homology; NADPH-ferrihemoprotein reductase homology KEYWORDS electron transfer; endoplasmic reticulum; flavoprotein; !1NADP; oxidoreductase FEATURE !$61-690 #domain NADPH-ferrihemoprotein reductase homology !8#label FEH\ !$63-204 #domain flavodoxin homology #label FLX SUMMARY #length 691 #molecular-weight 76771 #checksum 8413 SEQUENCE /// ENTRY S29123 #type complete TITLE NADPH-ferrihemoprotein reductase (EC 1.6.2.4) - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES NADP-cytochrome P450 reductase ORGANISM #formal_name Schizosaccharomyces pombe DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S29123; T40324; S20814 REFERENCE S29123 !$#authors Miles, J.S. !$#journal Biochem. J. (1992) 287:195-200 !$#title Structurally and functionally conserved regions of !1cytochrome P-450 reductase as targets for DNA amplification !1by the polymerase chain reaction. Cloning and nucleotide !1sequence of the Schizosaccharomyces pombe cDNA. !$#cross-references MUID:93038553; PMID:1417773 !$#accession S29123 !'##molecule_type mRNA !'##residues 1-678 ##label MIL !'##cross-references EMBL:X64702; NID:g4943; PIDN:CAA45956.1; PID:g4944 REFERENCE Z21920 !$#authors Wood, V.; Rajandream, M.A.; Barrell, B.G.; Lelaure, V.; !1Galibert, F. !$#submission submitted to the EMBL Data Library, June 1999 !$#accession T40324 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-678 ##label WOO !'##cross-references EMBL:AL078627; PIDN:CAB44769.1; GSPDB:GN00067; !1SPDB:SPBC365.17 !'##experimental_source strain 972h-; cosmid c365 GENETICS !$#gene SPBC365.17 !$#map_position 2 CLASSIFICATION #superfamily NADPH-ferrihemoprotein reductase; flavodoxin !1homology; NADPH-ferrihemoprotein reductase homology KEYWORDS electron transfer; endoplasmic reticulum; FAD; flavoprotein; !1FMN; membrane protein; NADP; oxidoreductase FEATURE !$53-677 #domain NADPH-ferrihemoprotein reductase homology !8#label FEH\ !$55-208 #domain flavodoxin homology #label FLX SUMMARY #length 678 #molecular-weight 76774 #checksum 6588 SEQUENCE /// ENTRY A34286 #type complete TITLE NADPH-ferrihemoprotein reductase (EC 1.6.2.4) - Bacillus megaterium CONTAINS NADPH-ferrihemoprotein reductase (EC 1.6.2.4); unspecific monooxygenase (EC 1.14.14.1) ORGANISM #formal_name Bacillus megaterium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS A34286; S43653 REFERENCE A34286 !$#authors Ruettinger, R.T.; Wen, L.P.; Fulco, A.J. !$#journal J. Biol. Chem. (1989) 264:10987-10995 !$#title Coding nucleotide, 5' regulatory, and deduced amino acid !1sequences of P-450-BM-3, a single peptide cytochrome !1P-450:NADPH-P-450 reductase from Bacillus megaterium. !$#cross-references MUID:89291834; PMID:2544578 !$#accession A34286 !'##molecule_type DNA !'##residues 1-1049 ##label RUE !'##cross-references GB:J04832; NID:g142797; PIDN:AAA87602.1; !1PID:g142798 REFERENCE S43653 !$#authors Munro, A.W.; Lindsay, J.G.; Coggins, J.R.; Kelly, S.M.; !1Price, N.C. !$#journal FEBS Lett. (1994) 343:70-74 !$#title Structural and enzymological analysis of the interaction of !1isolated domains of cytochrome P-450 BM3. !$#cross-references MUID:94215710; PMID:8163021 !$#accession S43653 !'##molecule_type protein !'##residues 430-439;441-496 ##label MUN GENETICS !$#gene CYP102 CLASSIFICATION #superfamily P450 bifunctional enzyme CYP102; cytochrome !1P450 homology; flavodoxin homology; NADPH-ferrihemoprotein !1reductase homology KEYWORDS chromoprotein; electron transfer; FAD; flavoprotein; FMN; !1heme; iron; metalloprotein; monooxygenase; multifunctional !1enzyme; oxidoreductase FEATURE !$262-423 #domain cytochrome P450 homology #label P45\ !$483-1046 #domain NADPH-ferrihemoprotein reductase homology !8#label FEH\ !$485-622 #domain flavodoxin homology #label FLX\ !$401 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 1049 #molecular-weight 117780 #checksum 7647 SEQUENCE /// ENTRY A69975 #type complete TITLE NADPH-ferrihemoprotein reductase (EC 1.6.2.4) - Bacillus subtilis CONTAINS NADPH-ferrihemoprotein reductase (EC 1.6.2.4); unspecific monooxygenase (EC 1.14.14.1) ORGANISM #formal_name Bacillus subtilis DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 03-Jun-2002 ACCESSIONS A69975 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69975 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1054 ##label KUN !'##cross-references GB:Z99117; GB:AL009126; NID:g2634966; PID:g2635162 !'##experimental_source strain 168 GENETICS !$#gene yrhJ CLASSIFICATION #superfamily P450 bifunctional enzyme CYP102; cytochrome !1P450 homology; flavodoxin homology; NADPH-ferrihemoprotein !1reductase homology KEYWORDS chromoprotein; flavoprotein; heme; iron; metalloprotein; !1monooxygenase; oxidoreductase FEATURE !$486-1050 #domain NADPH-ferrihemoprotein reductase homology !8#label FEH\ !$488-625 #domain flavodoxin homology #label FLX\ !$403 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 1054 #molecular-weight 118675 #checksum 3800 SEQUENCE /// ENTRY RDHUU #type complete TITLE glutathione-disulfide reductase (EC 1.8.1.7) - human ORGANISM #formal_name Homo sapiens #common_name man DATE 02-Apr-1982 #sequence_revision 22-Apr-1995 #text_change 03-Jun-2002 ACCESSIONS S08979; A00404; S10730 REFERENCE S08979 !$#authors Tutic, M.; Lu, X.; Schirmer, R.H.; Werner, D. !$#journal Eur. J. Biochem. (1990) 188:523-528 !$#title Cloning and sequencing of mammalian glutathione reductase !1cDNA. !$#cross-references MUID:90235822; PMID:2185014 !$#accession S08979 !'##molecule_type mRNA !'##residues 1-479 ##label TUT !'##cross-references EMBL:X15722; NID:g31824; PIDN:CAA33744.1; !1PID:g31825 REFERENCE A91112 !$#authors Krauth-Siegel, R.L.; Blatterspiel, R.; Saleh, M.; Schiltz, !1E.; Schirmer, R.H.; Untucht-Grau, R. !$#journal Eur. J. Biochem. (1982) 121:259-267 !$#title Glutathione reductase from human erythrocytes. The sequences !1of the NADPH domain and of the interface domain. !$#cross-references MUID:82138780; PMID:7060551 !$#accession A00404 !'##molecule_type protein !'##residues 2-479 ##label KRA !'##note this is the final paper in a series REFERENCE A92874 !$#authors Thieme, R.; Pai, E.F.; Schirmer, R.H.; Schulz, G.E. !$#journal J. Mol. Biol. (1981) 152:763-782 !$#title Three-dimensional structure of glutathione reductase at 2 !1angstrom resolution. !$#cross-references MUID:82145544; PMID:7334521 !$#contents annotation; X-ray crystallography, 2 angstroms REFERENCE S10730 !$#authors Arnold, H.H.; Heinze, H. !$#journal FEBS Lett. (1990) 267:189-192 !$#title Treatment of human peripheral lymphocytes with concanavalin !1A activates expression of glutathione reductase. !$#cross-references MUID:90336771; PMID:2379581 !$#accession S10730 !'##molecule_type mRNA !'##residues !178-96;98-116;118-136;138-156;158-176;178-196;198-216; !1218-236;238-256;258-276;278-296;298-316;318-319 ##label ARN !'##cross-references GB:X54507; NID:g31828; PIDN:CAA38367.1; PID:g31829 !'##note in the displayed figure the last codon of the sequence plus !1amino acid are skipped in every line; therefore 12 internal !1amino acids are missing GENETICS !$#gene GDB:GSR !'##cross-references GDB:119288; OMIM:138300 !$#map_position 8p21.1-8p21.1 COMPLEX homodimer FUNCTION !$#description catalyzes the reduction of glutathione by NADPH !$#note responsible for maintaining high levels of reduced !1glutathione in the cytoplasm CLASSIFICATION #superfamily dihydrolipoamide dehydrogenase; !1dihydrolipoamide dehydrogenase homology KEYWORDS acetylated amino end; FAD; flavoprotein; homodimer; NADP; !1oxidoreductase; redox-active disulfide FEATURE !$23-51 #region beta-alpha-beta FAD nucleotide-binding fold\ !$25-475 #domain dihydrolipoamide dehydrogenase homology !8#label DLD\ !$190-221 #region beta-alpha-beta NADP nucleotide-binding fold\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental\ !$59-64 #disulfide_bonds redox-active #status experimental\ !$91 #disulfide_bonds interchain #status experimental\ !$468 #active_site His #status experimental SUMMARY #length 479 #molecular-weight 51700 #checksum 4262 SEQUENCE /// ENTRY RDECU #type complete TITLE glutathione-disulfide reductase (EC 1.8.1.7) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 03-Jun-2002 ACCESSIONS A24409; S47720; G65147 REFERENCE A24409 !$#authors Greer, S.; Perham, R.N. !$#journal Biochemistry (1986) 25:2736-2742 !$#title Glutathione reductase from Escherichia coli: cloning and !1sequence analysis of the gene and relationship to other !1flavoprotein disulfide oxidoreductases. !$#cross-references MUID:86243410; PMID:3521741 !$#accession A24409 !'##molecule_type DNA !'##residues 1-450 ##label GRE !'##cross-references GB:M13141; NID:g146247; PIDN:AAA23926.1; !1PID:g146248 !'##experimental_source strain K12 REFERENCE S47666 !$#authors Plunkett, G. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S47720 !'##molecule_type DNA !'##residues 1-450 ##label PLU !'##cross-references EMBL:U00039; NID:g466582; PIDN:AAB18476.1; !1PID:g466637 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65147 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-450 ##label BLAT !'##cross-references GB:AE000426; GB:U00096; NID:g1789910; !1PIDN:AAC76525.1; PID:g1789915; UWGP:b3500 !'##experimental_source strain K-12, substrain MG1655 COMMENT This ubiquitous FAD-containing enzyme catalyzes the !1reduction of oxidized glutathione by NADPH. Glutathione is !1not an essential metabolite in E. coli; mutants (gor) !1lacking glutathione reductase have been shown to have !1unimpaired growth. GENETICS !$#gene gor !$#map_position 78 min CLASSIFICATION #superfamily dihydrolipoamide dehydrogenase; !1dihydrolipoamide dehydrogenase homology KEYWORDS FAD; flavoprotein; NADP; oxidoreductase; redox-active !1disulfide FEATURE !$6-34 #region beta-alpha-beta FAD nucleotide-binding fold\ !$8-446 #domain dihydrolipoamide dehydrogenase homology !8#label DLD\ !$42-47 #disulfide_bonds redox-active #status predicted\ !$439 #active_site His #status predicted SUMMARY #length 450 #molecular-weight 48772 #checksum 7782 SEQUENCE /// ENTRY S66677 #type complete TITLE thioredoxin-disulfide reductase (EC 1.8.1.9) [validated] - human CONTAINS thioredoxin reductase (NADPH), placental form; thioredoxin reductase (NADPH), T-cell form ORGANISM #formal_name Homo sapiens #common_name man DATE 28-Oct-1996 #sequence_revision 10-Oct-1997 #text_change 03-Jun-2002 ACCESSIONS S66677; S74270; A43122; G01120 REFERENCE S66677 !$#authors Gasdaska, P.Y.; Gasdaska, J.R.; Cochran, S.; Powis, G. !$#journal FEBS Lett. (1995) 373:5-9 !$#title Cloning and sequencing of a human thioredoxin reductase. !$#cross-references MUID:96013875; PMID:7589432 !$#accession S66677 !'##molecule_type mRNA !'##residues 1-497 ##label GAS1 !'##cross-references EMBL:X91247; NID:g1237037; PIDN:CAA62629.1; !1PID:g1237038; GB:S79851; NID:g1184536; PID:g1184537 !$#accession S74270 !'##molecule_type protein !'##residues 3-11;157-165;435-457 ##label GAS2 REFERENCE A43122 !$#authors Gladyshev, V.N.; Jeang, K.T.; Stadtman, T.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1996) 93:6146-6151 !$#title Selenocysteine, identified as the penultimate C-terminal !1residue in human T-cell thioredoxin reductase, corresponds !1to TGA in the human placental gene. !$#cross-references MUID:96234105; PMID:8650234 !$#accession A43122 !'##molecule_type protein !'##residues 488-497,'X',499 ##label GLA !'##note the residue designated 'X' was determined to be selenocysteine; !1we have shown the residue as Cys COMMENT In most tissues, such as placenta, the UGA codon is used as !1the terminator. In the T-cell at least the UGA codon is !1translated with selenocysteine, and termination occurs at a !1UAA codon two codons further along. GENETICS !$#gene GDB:TXNRD1; TXNR !'##cross-references GDB:683567; OMIM:601112 !$#map_position 12q23-12q24.1 COMPLEX homodimer FUNCTION !$#description catalyzes the reduction of thioredoxin by NADPH !$#note the T-cell form also has peroxidase activity CLASSIFICATION #superfamily dihydrolipoamide dehydrogenase; !1dihydrolipoamide dehydrogenase homology KEYWORDS alternative termination; FAD; flavoprotein; homodimer; NADP; !1oxidoreductase; redox-active disulfide; selenocysteine FEATURE !$3-499 #product thioredoxin reductase (NADPH), T-cell form !8#status experimental #label MAT1\ !$3-497 #product thioredoxin reductase (NADPH), placental !8form #status experimental #label MAT2\ !$14-42 #region beta-alpha-beta FAD nucleotide-binding fold\ !$16-479 #domain dihydrolipoamide dehydrogenase homology !8#label DLD\ !$192-222 #region beta-alpha-beta NADP nucleotide-binding fold\ !$59-64 #disulfide_bonds redox-active #status predicted\ !$472 #active_site His #status predicted\ !$498 #modified_site selenocysteine #status experimental SUMMARY #length 499 #molecular-weight 54579 #checksum 4319 SEQUENCE /// ENTRY S28002 #type complete TITLE trypanothione-disulfide reductase (EC 1.8.1.12) - Crithidia fasciculata ORGANISM #formal_name Crithidia fasciculata DATE 17-Apr-1993 #sequence_revision 02-Jun-1994 #text_change 03-Jun-2002 ACCESSIONS S28002; A45647; S22724 REFERENCE S28002 !$#authors Aboagye-Kwarteng, T.; Smith, K.; Fairlamb, A.H. !$#journal Mol. Microbiol. (1992) 6:3089-3099 !$#title Molecular characterization of the trypanothione reductase !1gene from Crithidia fasciculata and Trypanosoma brucei: !1comparison with other flavoprotein disulphide !1oxidoreductases with respect to substrate specificity and !1catalytic machanism. !$#cross-references MUID:93086418; PMID:1453951 !$#accession S28002 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-491 ##label ABO !'##cross-references EMBL:Z12618; NID:g6995; PIDN:CAA78264.1; PID:g6996 REFERENCE A45647 !$#authors Field, H.; Cerami, A.; Henderson, G.B. !$#journal Mol. Biochem. Parasitol. (1992) 50:47-56 !$#title Cloning, sequencing, and demonstration of polymorphism in !1trypanothione reductase from Crithidia fasciculata. !$#cross-references MUID:92178290; PMID:1542316 !$#accession A45647 !'##molecule_type DNA !'##residues 1-296,'E',298-453,'V',455-491 ##label FIE !'##note this sequence is inconsistent with the nucleotide translation !'##note sequence extracted from NCBI backbone (NCBIN:85191, !1NCBIP:85193) CLASSIFICATION #superfamily dihydrolipoamide dehydrogenase; !1dihydrolipoamide dehydrogenase homology KEYWORDS FAD; flavoprotein; oxidoreductase; redox-active disulfide FEATURE !$8-468 #domain dihydrolipoamide dehydrogenase homology !8#label DLD\ !$52-57 #disulfide_bonds redox-active #status predicted SUMMARY #length 491 #molecular-weight 53229 #checksum 8923 SEQUENCE /// ENTRY S34376 #type complete TITLE trypanothione-disulfide reductase (EC 1.8.1.12) - Leishmania donovani ORGANISM #formal_name Leishmania donovani DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S34376 REFERENCE S34376 !$#authors Taylor, M.C.; Chapman, C.J.; Kelly, J.M.; Fairlamb, A.H.; !1Miles, M.A. !$#submission submitted to the EMBL Data Library, June 1993 !$#description The trypanothione reductase gene of Leishmania donovani. !$#accession S34376 !'##molecule_type DNA !'##residues 1-491 ##label TAY !'##cross-references EMBL:Z23135; NID:g312820; PIDN:CAA80668.1; !1PID:g312821 CLASSIFICATION #superfamily dihydrolipoamide dehydrogenase; !1dihydrolipoamide dehydrogenase homology KEYWORDS oxidoreductase; redox-active disulfide FEATURE !$8-468 #domain dihydrolipoamide dehydrogenase homology !8#label DLD\ !$52-57 #disulfide_bonds redox-active #status predicted SUMMARY #length 491 #molecular-weight 52933 #checksum 4751 SEQUENCE /// ENTRY S68968 #type complete TITLE trypanothione-disulfide reductase (EC 1.8.1.12) - Trypanosoma cruzi ORGANISM #formal_name Trypanosoma cruzi DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S68968; S24243; S30204 REFERENCE S68968 !$#authors Borges, A.; Cunningham, M.L.; Tovar, J.; Fairlamb, A.H. !$#journal Eur. J. Biochem. (1995) 228:745-752 !$#title Site-directed mutagenesis of the redox-active cysteines of !1Trypanosoma cruzi trypanothione reductase. !$#cross-references MUID:95255281; PMID:7737173 !$#accession S68968 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-492 ##label BOR !'##cross-references EMBL:Z13958; NID:g624037; PIDN:CAA78360.1; !1PID:g624038 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1995 REFERENCE S24243 !$#authors Borges, A.; Fairlamb, A. !$#submission submitted to the EMBL Data Library, June 1992 !$#description Mutagenesis of the redox-active cysteines in the !1trypanothione reductase from Trypanosoma cruzi. Implications !1for the mechanism of catalysis. !$#accession S24243 !'##status preliminary !'##molecule_type DNA !'##residues 1-111,'E',113-139,'A',141-155,'N',157-492 ##label BO2 !'##cross-references EMBL:Z13958 REFERENCE S30204 !$#authors Sullivan, F.X.; Walsh, C.T. !$#journal Mol. Biochem. Parasitol. (1991) 44:145-148 !$#title Cloning, sequencing, overproduction and purification of !1trypanothione reductase from Trypanosoma cruzi. !$#cross-references MUID:91187059; PMID:2011150 !$#accession S30204 !'##status preliminary !'##molecule_type DNA !'##residues 1-94,'K',96-111,'E',113-155,'N',157-352,'N',354-401,'NI', !1404-440,'V',442-492 ##label SUL !'##cross-references EMBL:M38051; NID:g162316; PIDN:AAA63547.1; !1PID:g162317 CLASSIFICATION #superfamily dihydrolipoamide dehydrogenase; !1dihydrolipoamide dehydrogenase homology KEYWORDS NADP; oxidoreductase; redox-active disulfide FEATURE !$9-468 #domain dihydrolipoamide dehydrogenase homology !8#label DLD\ !$53-58 #disulfide_bonds redox-active #status predicted SUMMARY #length 492 #molecular-weight 53863 #checksum 8597 SEQUENCE /// ENTRY A27727 #type complete TITLE trypanothione-disulfide reductase (EC 1.8.1.12) - Trypanosoma congolense ORGANISM #formal_name Trypanosoma congolense DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS A27727 REFERENCE A27727 !$#authors Shames, S.L.; Kimmel, B.E.; Peoples, O.P.; Agabian, N.; !1Walsh, C.T. !$#journal Biochemistry (1988) 27:5014-5019 !$#title Trypanothione reductase of Trypanosoma congolense: gene !1isolation, primary sequence determination, and comparison to !1glutathione reductase. !$#cross-references MUID:89000712; PMID:3167026 !$#accession A27727 !'##molecule_type DNA !'##residues 1-492 ##label SHA !'##cross-references GB:M21122; NID:g162310; PIDN:AAA30258.1; !1PID:g162311 CLASSIFICATION #superfamily dihydrolipoamide dehydrogenase; !1dihydrolipoamide dehydrogenase homology KEYWORDS flavoprotein; oxidoreductase; redox-active disulfide FEATURE !$8-468 #domain dihydrolipoamide dehydrogenase homology !8#label DLD\ !$52-57 #disulfide_bonds redox-active #status predicted SUMMARY #length 492 #molecular-weight 53443 #checksum 5448 SEQUENCE /// ENTRY S28003 #type complete TITLE trypanothione-disulfide reductase (EC 1.8.1.12) - Trypanosoma brucei ORGANISM #formal_name Trypanosoma brucei DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S28003; S22725 REFERENCE S28002 !$#authors Aboagye-Kwarteng, T.; Smith, K.; Fairlamb, A.H. !$#journal Mol. Microbiol. (1992) 6:3089-3099 !$#title Molecular characterization of the trypanothione reductase !1gene from Crithidia fasciculata and Trypanosoma brucei: !1comparison with other flavoprotein disulphide !1oxidoreductases with respect to substrate specificity and !1catalytic machanism. !$#cross-references MUID:93086418; PMID:1453951 !$#accession S28003 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-492 ##label ABO !'##cross-references EMBL:X63188; NID:g10544; PIDN:CAA44870.1; !1PID:g10545 CLASSIFICATION #superfamily dihydrolipoamide dehydrogenase; !1dihydrolipoamide dehydrogenase homology KEYWORDS FAD; flavoprotein; oxidoreductase; redox-active disulfide FEATURE !$8-468 #domain dihydrolipoamide dehydrogenase homology !8#label DLD\ !$52-57 #disulfide_bonds redox-active #status predicted SUMMARY #length 492 #molecular-weight 53284 #checksum 7215 SEQUENCE /// ENTRY DEHULP #type complete TITLE dihydrolipoamide dehydrogenase (EC 1.8.1.4) precursor - human ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 11-Jun-1999 ACCESSIONS A92622; A94190; I59212; A28961; B28448 REFERENCE A92622 !$#authors Otulakowski, G.; Robinson, B.H. !$#journal J. Biol. Chem. (1987) 262:17313-17318 !$#title Isolation and sequence determination of cDNA clones for !1porcine and human lipoamide dehydrogenase. Homology to other !1disulfide oxidoreductases. !$#cross-references MUID:88087005; PMID:3693355 !$#accession A92622 !'##molecule_type mRNA !'##residues 1-509 ##label OTU !'##cross-references GB:J03490; NID:g187207; PIDN:AAA59527.1; !1PID:g307137 REFERENCE A94190 !$#authors Pons, G.; Raefsky-Estrin, C.; Carothers, D.J.; Pepin, R.A.; !1Javed, A.A.; Jesse, B.W.; Ganapathi, M.K.; Samols, D.; !1Patel, M.S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:1422-1426 !$#title Cloning and cDNA sequence of the dihydrolipoamide !1dehydrogenase component of human alpha-ketoacid !1dehydrogenase complexes. !$#cross-references MUID:88144449; PMID:3278312 !$#accession A94190 !'##molecule_type mRNA !'##residues 1-103,'K',105-153,'R',155-509 ##label PON !'##cross-references GB:J03620; NID:g181574; PIDN:AAA35764.1; !1PID:g181575 REFERENCE I59212 !$#authors Johanning, G.L.; Morris, J.I.; Madhusudhan, K.T.; Samols, !1D.; Patel, M.S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:10964-10968 !$#title Characterization of the transcriptional regulatory region of !1the human dihydrolipoamide dehydrogenase gene. !$#cross-references MUID:93066364; PMID:1332063 !$#accession I59212 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-13 ##label RES !'##cross-references GB:M99384; NID:g181550; PIDN:AAA35759.1; !1PID:g181551 COMMENT The active enzyme is a dimer of identical chains containing !1a noncovalently bound FAD and a redox-active disulfide bond. !1The precursor is encoded by a nuclear gene and converted to !1mature protein when it is transported to the mitochondrial !1matrix. COMMENT This enzyme is the component (E3) shared by three !1multienzyme complexes that catalyze the overall oxidative !1decarboxylation of pyruvate, 2-oxoglutarate, and !1branched-chain alpha-keto acid with the formation of !1corresponding acyl-CoAs. The other complex-specific !1components are the oxidative decarboxylase components (E1) !1and the dihydrolipoamide acyltransferase components (E2). GENETICS !$#gene GDB:DLD; DLDH; LAD !'##cross-references GDB:120608; OMIM:246900 !$#map_position 7q31-7q32 CLASSIFICATION #superfamily dihydrolipoamide dehydrogenase; !1dihydrolipoamide dehydrogenase homology KEYWORDS FAD; flavoprotein; lipoamide; mitochondrial matrix; !1mitochondrion; NAD; oxidoreductase; redox-active disulfide; !1tricarboxylic acid cycle FEATURE !$1-35 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$36-509 #product dihydrolipoamide dehydrogenase #status !8predicted #label MAT\ !$43-71 #region beta-alpha-beta FAD nucleotide-binding fold\ !$45-494 #domain dihydrolipoamide dehydrogenase homology !8#label DLD\ !$215-243 #region beta-alpha-beta NAD nucleotide-binding fold\ !$80-85 #disulfide_bonds redox-active #status predicted SUMMARY #length 509 #molecular-weight 54150 #checksum 9280 SEQUENCE /// ENTRY DEPGLP #type complete TITLE dihydrolipoamide dehydrogenase (EC 1.8.1.4) precursor - pig ALTERNATE_NAMES diaphorase; lipoamide reductase (NADH) ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 11-Jun-1999 ACCESSIONS A28448; A21524; A05101 REFERENCE A92622 !$#authors Otulakowski, G.; Robinson, B.H. !$#journal J. Biol. Chem. (1987) 262:17313-17318 !$#title Isolation and sequence determination of cDNA clones for !1porcine and human lipoamide dehydrogenase. Homology to other !1disulfide oxidoreductases. !$#cross-references MUID:88087005; PMID:3693355 !$#accession A28448 !'##molecule_type mRNA !'##residues 1-509 ##label OTU !'##cross-references GB:J03489; NID:g164538; PIDN:AAA31069.1; !1PID:g164539 REFERENCE A93908 !$#authors Williams Jr., C.H.; Arscott, L.D.; Schulz, G.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:2199-2201 !$#title Amino acid sequence homology between pig heart lipoamide !1dehydrogenase and human erythrocyte glutathione reductase. !$#cross-references MUID:82247969; PMID:6954534 !$#accession A21524 !'##molecule_type protein !'##residues 36-59;60-66;67-89;91-94,'G',96,'AX',99,'X',101-102,'X', !1104;317-331,'R';347-350,'A',352-360;388-404;405-417;418, !1451-482 ##label WIL CLASSIFICATION #superfamily dihydrolipoamide dehydrogenase; !1dihydrolipoamide dehydrogenase homology KEYWORDS FAD; flavoprotein; lipoamide; mitochondrial matrix; !1mitochondrion; NAD; oxidoreductase; redox-active disulfide; !1tricarboxylic acid cycle FEATURE !$1-35 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$36-509 #product dihydrolipoamide dehydrogenase #status !8predicted #label MAT\ !$43-71 #region beta-alpha-beta FAD nucleotide-binding fold\ !$45-494 #domain dihydrolipoamide dehydrogenase homology !8#label DLD\ !$215-243 #region beta-alpha-beta NAD nucleotide-binding fold\ !$80-85 #disulfide_bonds redox-active #status predicted SUMMARY #length 509 #molecular-weight 54185 #checksum 8760 SEQUENCE /// ENTRY JC4241 #type complete TITLE dihydrolipoamide dehydrogenase (EC 1.8.1.4) precursor - dog ALTERNATE_NAMES dihydrolipoamide:NAD+ oxidoreductase; lipoyl dehydrogenase ORGANISM #formal_name Canis lupus familiaris #common_name dog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JC4241 REFERENCE JC4241 !$#authors Martins, A.S.; Greene, L.J.; Yoho, L.L.; Milsted, A. !$#journal Gene (1995) 161:253-257 !$#title The cDNA encoding canine dihydrolipoamide dehydrogenase !1contains multiple termination signals. !$#cross-references MUID:95394366; PMID:7665089 !$#accession JC4241 !'##molecule_type mRNA !'##residues 1-509 ##label MAR !'##cross-references GB:U19872; NID:g642069; PIDN:AAA87174.1; !1PID:g642070 !'##experimental_source skeletal muscle COMMENT This enzyme is a flavoprotein common to three multi-enzyme !1alpha-keto-acid dehydrogenase complexes involved in !1oxidative decarboxylation of pyruvate, alpha-ketoglutarate !1and the branched-chain keto acids. GENETICS !$#gene dldh CLASSIFICATION #superfamily dihydrolipoamide dehydrogenase; !1dihydrolipoamide dehydrogenase homology KEYWORDS FAD; flavoprotein; lipoamide; NAD; oxidoreductase; !1redox-active disulfide; skeletal muscle FEATURE !$1-35 #domain signal sequence #status predicted #label SIG\ !$36-509 #product dihydrolipoamide dehydrogenase #status !8predicted #label MAT\ !$43-71 #region beta-alpha-beta FAD nucleotide-binding fold\ !$45-494 #domain dihydrolipoamide dehydrogenase homology !8#label DLD\ !$215-243 #region beta-alpha-beta NAD nucleotide-binding fold\ !$80-85 #disulfide_bonds redox-active #status predicted\ !$485,487 #active_site His #status predicted SUMMARY #length 509 #molecular-weight 54153 #checksum 48 SEQUENCE /// ENTRY DEECLP #type complete TITLE dihydrolipoamide dehydrogenase (EC 1.8.1.4) - Escherichia coli (strain K-12) ALTERNATE_NAMES 2-oxoglutarate dehydrogenase complex E3 component; alpha-ketoacid dehydrogenase complex E3 component; diaphorase; glycine cleavage system L protein; lipoamide reductase ORGANISM #formal_name Escherichia coli DATE 25-Feb-1985 #sequence_revision 01-Mar-1996 #text_change 01-Mar-2002 ACCESSIONS S45195; D64734; A00405 REFERENCE S45181 !$#authors Fujita, N. !$#submission submitted to the EMBL Data Library, January 1994 !$#accession S45195 !'##molecule_type DNA !'##residues 1-474 ##label FUJ !'##cross-references EMBL:D26562; NID:g473770; PIDN:BAA05574.1; !1PID:g473785 !'##experimental_source strain K-12 substrain W3110 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64734 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-474 ##label BLAT !'##cross-references GB:AE000121; GB:U00096; NID:g1786306; !1PIDN:AAC73227.1; PID:g1786307; UWGP:b0116 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A00405 !$#authors Stephens, P.E.; Lewis, H.M.; Darlison, M.G.; Guest, J.R. !$#journal Eur. J. Biochem. (1983) 135:519-527 !$#title Nucleotide sequence of the lipoamide dehydrogenase gene of !1Escherichia coli K12. !$#cross-references MUID:84004369; PMID:6352260 !$#accession A00405 !'##molecule_type DNA !'##residues 2-474 ##label STE !'##cross-references GB:V01498; NID:g431915; PIDN:CAA24742.1; !1PID:g434012 !'##note the initiator Met removed after translation is not shown; the !1GenBank translation with PID:g434012 shows a Met immediately !1preceeding the initiator Met COMMENT This enzyme is a component of at least three multienzyme !1complexes, the pyruvate dehydrogenase complex, the !12-oxoglutarate dehydrogenase complex and the glycine !1cleavage complex. GENETICS !$#gene lpdA; lpd !$#map_position 3 min COMPLEX homodimer COMPLEX in 2-oxoglutarate dehydrogenase complex approximately 12 !1monomeric chains associate with 24 chains of the E2 !1component FUNCTION !$#description catalyzes the oxidation of dihydrolipoamide to lipoamide by !1NAD !$#note the 2-oxoglutarate dehydrogenase complex, including !12-oxoglutarate dehydrogenase (E1), dihydrolipoamide !1succinyltransferase (E2) and lipoamide dehydrogenase (E3), !1catalyzes the oxidative decarboxylation of 2-oxoglutarate to !1succinyl-CoA and carbon dioxide CLASSIFICATION #superfamily dihydrolipoamide dehydrogenase; !1dihydrolipoamide dehydrogenase homology KEYWORDS FAD; flavoprotein; homodimer; lipoamide; NAD; !1oxidoreductase; redox-active disulfide; tricarboxylic acid !1cycle FEATURE !$8-36 #region beta-alpha-beta FAD nucleotide-binding fold\ !$10-452 #domain dihydrolipoamide dehydrogenase homology !8#label DLD\ !$177-205 #region beta-alpha-beta NAD nucleotide-binding fold\ !$45-50 #disulfide_bonds redox-active #status predicted SUMMARY #length 474 #molecular-weight 50688 #checksum 3443 SEQUENCE /// ENTRY H64111 #type complete TITLE dihydrolipoamide dehydrogenase (EC 1.8.1.4) - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 18-Aug-1995 #sequence_revision 10-May-1996 #text_change 11-Jun-1999 ACCESSIONS H64111 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession H64111 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-478 ##label TIGR !'##cross-references GB:U32802; GB:L42023; NID:g1574151; !1PIDN:AAC22884.1; PID:g1574161; TIGR:HI1231 !'##note named according to sequence homology to a protein from !1Escherichia coli CLASSIFICATION #superfamily dihydrolipoamide dehydrogenase; !1dihydrolipoamide dehydrogenase homology KEYWORDS FAD; flavoprotein; lipoamide; NAD; oxidoreductase; !1redox-active disulfide; tricarboxylic acid cycle FEATURE !$8-36 #region beta-alpha-beta FAD nucleotide-binding fold\ !$10-452 #domain dihydrolipoamide dehydrogenase homology !8#label DLD\ !$178-206 #region beta-alpha-beta NAD nucleotide-binding fold\ !$45-50 #disulfide_bonds redox-active #status predicted SUMMARY #length 478 #molecular-weight 51154 #checksum 1521 SEQUENCE /// ENTRY S13839 #type complete TITLE dihydrolipoamide dehydrogenase (EC 1.8.1.4) [validated] - Bacillus stearothermophilus ALTERNATE_NAMES 2-oxoglutarate dehydrogenase complex chain E3; branched-chain 2-oxoacid dehydrogenase complex chain E3; lipoamide dehydrogenase; pyruvate dehydrogenase complex chain E3; S-complex 50K chain ORGANISM #formal_name Bacillus stearothermophilus DATE 21-Nov-1993 #sequence_revision 10-May-1996 #text_change 21-Jul-2000 ACCESSIONS S13839; S62229; T46892; A28514; S14231 REFERENCE S13838 !$#authors Borges, A.; Hawkins, C.F.; Packman, L.C.; Perham, R.N. !$#journal Eur. J. Biochem. (1990) 194:95-102 !$#title Cloning and sequence analysis of the genes encoding the !1dihydrolipoamide acetyltransferase and dihydrolipoamide !1dehydrogenase components of the pyruvate dehydrogenase !1multienzyme complex of Bacillus stearothermophilus. !$#cross-references MUID:91071217; PMID:2253629 !$#accession S13839 !'##molecule_type DNA !'##residues 1-470 ##label BOR !'##cross-references EMBL:X53560; NID:g40038; PIDN:CAA37631.1; !1PID:g40044 !$#accession S62229 !'##molecule_type protein !'##residues 2-32;41-64;142-150;227-241;294-298;371-379;388-394;400-403 !1##label BOW !$#accession T46892 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-470 ##label BO2 !'##cross-references EMBL:X53560; NID:g40038; PIDN:CAA37631.1; !1PID:g40044 !'##experimental_source strain NCA1503 REFERENCE A28514 !$#authors Packman, L.C.; Perham, R.N. !$#journal FEBS Lett. (1982) 139:155-158 !$#title An amino acid sequence in the active site of lipoamide !1dehydrogenase from Bacillus stearothermophilus. !$#cross-references MUID:82187191; PMID:6896188 !$#accession A28514 !'##molecule_type protein !'##residues 41-56 ##label PAC GENETICS !$#gene pdhD !$#note member of gene cluster pdhABCD COMPLEX homodimer COMPLEX component of the pyruvate dehydrogenase complex; components !1are pyruvate dehydrogenase, dihydrolipoamide !1acetyltransferase, and dihydrolipoamide dehydrogenase !1(PIR:S13839) FUNCTION !$#description EC 1.8.1.4 [validated, MUID:88339820]; dihydrolipoamide !1dehydrogenase; catalyzes the oxidation of dihydrolipoamide !1to lipoamide using NAD as acceptor; it is a component of the !1multienzyme complexes that catalyze the oxidative !1decarboxylation of 2-oxoglutarate and pyruvate with the !1formation of succinyl-CoA and acetyl-CoA, respectively CLASSIFICATION #superfamily dihydrolipoamide dehydrogenase; !1dihydrolipoamide dehydrogenase homology KEYWORDS FAD; flavoprotein; lipoamide; NAD; oxidoreductase; !1redox-active disulfide; tricarboxylic acid cycle FEATURE !$11-39 #region beta-alpha-beta FAD nucleotide-binding fold\ !$13-453 #domain dihydrolipoamide dehydrogenase homology !8#label DLD\ !$178-206 #region beta-alpha-beta NAD nucleotide-binding fold\ !$47-52 #disulfide_bonds redox-active #status predicted SUMMARY #length 470 #molecular-weight 49355 #checksum 5326 SEQUENCE /// ENTRY E36718 #type complete TITLE dihydrolipoamide dehydrogenase (EC 1.8.1.4) - Bacillus subtilis ALTERNATE_NAMES 2-oxoglutarate dehydrogenase complex chain E3; branched-chain 2-oxoacid dehydrogenase complex chain E3; lipoamide dehydrogenase; pyruvate dehydrogenase complex chain E3; S-complex 50K chain ORGANISM #formal_name Bacillus subtilis DATE 12-Apr-1991 #sequence_revision 10-May-1996 #text_change 16-Jun-2000 ACCESSIONS E36718; C54546; C69674 REFERENCE A36718 !$#authors Hemilae, H.; Palva, A.; Paulin, L.; Arvidson, S.; Palva, I. !$#journal J. Bacteriol. (1990) 172:5052-5063 !$#title Secretory S complex of Bacillus subtilis: sequence analysis !1and identity to pyruvate dehydrogenase. !$#cross-references MUID:90368558; PMID:1697575 !$#accession E36718 !'##molecule_type DNA !'##residues 1-470 ##label HEM !'##cross-references GB:M57435; GB:M31542; NID:g143375; PIDN:AAA62684.1; !1PID:g143380 REFERENCE A54546 !$#authors Hemilae, H. !$#journal FEMS Microbiol. Lett. (1991) 66:37-41 !$#title Sequence of a PAL-related lipoprotein from Bacillus !1subtilis. !$#cross-references MUID:92038903; PMID:1936936 !$#accession C54546 !'##molecule_type DNA !'##residues 461-470 ##label HE2 !'##experimental_source 168 strain BRB1 !'##note sequence extracted from NCBI backbone (NCBIN:63826, !1NCBIP:63830) REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69674 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-470 ##label KUN !'##cross-references GB:Z99111; GB:AL009126; NID:g2633699; !1PIDN:CAB13334.1; PID:g2633832 !'##experimental_source strain 168 GENETICS !$#gene pdhD COMPLEX dimer of identical chains containing a noncovalently bound !1FAD and a redox-active disulfide bond; it is a component of !1two multienzyme complexes: pyruvate dehydrogenase complex !1(other components are pyruvate dehydrogenase and !1dihydrolipoamide acetyltransferase) and oxoglutarate !1dehydrogenase complex (other components are oxoglutarate !1dehydrogenase and dihydrolipoamide succinyltransferase) FUNCTION !$#description catalyzes the oxidation dihydrolipoamide to lipoamide using !1NAD acceptor; it is a component of the multienzyme complexes !1that catalyze the oxidative decarboxylation of !12-oxoglutarate and pyruvate with the formation of !1succinyl-CoA and acetyl-CoA, respectively CLASSIFICATION #superfamily dihydrolipoamide dehydrogenase; !1dihydrolipoamide dehydrogenase homology KEYWORDS FAD; flavoprotein; lipoamide; NAD; oxidoreductase; !1redox-active disulfide; tricarboxylic acid cycle FEATURE !$11-39 #region beta-alpha-beta FAD nucleotide-binding fold\ !$13-454 #domain dihydrolipoamide dehydrogenase homology !8#label DLD\ !$178-206 #region beta-alpha-beta NAD nucleotide-binding fold\ !$47-52 #disulfide_bonds redox-active #status predicted SUMMARY #length 470 #molecular-weight 49732 #checksum 3042 SEQUENCE /// ENTRY S19723 #type complete TITLE dihydrolipoamide dehydrogenase (EC 1.8.1.4) - Staphylococcus aureus ALTERNATE_NAMES pyruvate dehydrogenase complex chain E3 ORGANISM #formal_name Staphylococcus aureus DATE 13-Jan-1995 #sequence_revision 10-May-1996 #text_change 11-Jun-1999 ACCESSIONS S19723 REFERENCE S19721 !$#authors Hemilae, H. !$#journal Biochim. Biophys. Acta (1991) 1129:119-123 !$#title Lipoamide dehydrogenase of Staphylococcus aureus: nucleotide !1sequence and sequence analysis. !$#cross-references MUID:92096451; PMID:1756171 !$#accession S19723 !'##status preliminary !'##molecule_type DNA !'##residues 1-468 ##label HEM !'##cross-references EMBL:X58434; NID:g48871; PIDN:CAA41340.1; !1PID:g48874 GENETICS !$#gene pdhD COMPLEX dimer of identical chains containing a noncovalently bound !1FAD and a redox-active disulfide bond; it is a component of !1two multienzyme complexes: pyruvate dehydrogenase complex !1(other components are pyruvate dehydrogenase and !1dihydrolipoamide acetyltransferase) and oxoglutarate !1dehydrogenase complex (other components are oxoglutarate !1dehydrogenase and dihydrolipoamide succinyltransferase) FUNCTION !$#description catalyzes the oxidation dihydrolipoamide to lipoamide using !1NAD acceptor; it is a component of the multienzyme complexes !1that catalyze the oxidative decarboxylation of !12-oxoglutarate and pyruvate with the formation of !1succinyl-CoA and acetyl-CoA, respectively CLASSIFICATION #superfamily dihydrolipoamide dehydrogenase; !1dihydrolipoamide dehydrogenase homology KEYWORDS FAD; flavoprotein; lipoamide; NAD; oxidoreductase; !1redox-active disulfide; tricarboxylic acid cycle FEATURE !$11-39 #region beta-alpha-beta FAD nucleotide-binding fold\ !$13-453 #domain dihydrolipoamide dehydrogenase homology !8#label DLD\ !$178-206 #region beta-alpha-beta NAD nucleotide-binding fold\ !$47-52 #disulfide_bonds redox-active #status predicted SUMMARY #length 468 #molecular-weight 49451 #checksum 8131 SEQUENCE /// ENTRY A56824 #type complete TITLE dihydrolipoamide dehydrogenase (EC 1.8.1.4) - Haloferax volcanii ORGANISM #formal_name Haloferax volcanii DATE 18-Aug-1995 #sequence_revision 10-May-1996 #text_change 11-Jun-1999 ACCESSIONS A56824 REFERENCE A56824 !$#authors Vettakkorumakankav, N.N.; Stevenson, K.J. !$#journal Biochem. Cell Biol. (1992) 70:656-663 !$#title Dihydrolipoamide dehydrogenase from Haloferax volcanii: gene !1cloning, complete primary structure, and comparison to other !1dihydrolipoamide dehydrogenases. !$#cross-references MUID:93119588; PMID:1339281 !$#accession A56824 !'##status preliminary !'##molecule_type DNA !'##residues 1-475 ##label VET !'##cross-references GB:L09733; NID:g149019; PIDN:AAA72340.1; !1PID:g149020 !'##note sequence extracted from NCBI backbone (NCBIN:122030, !1NCBIP:122031) COMPLEX dimer of identical chains containing a noncovalently bound !1FAD and a redox-active disulfide bond; it is a component of !1two multienzyme complexes: pyruvate dehydrogenase complex !1(other components are pyruvate dehydrogenase and !1dihydrolipoamide acetyltransferase) and oxoglutarate !1dehydrogenase complex (other components are oxoglutarate !1dehydrogenase and dihydrolipoamide succinyltransferase) FUNCTION !$#description catalyzes the oxidation dihydrolipoamide to lipoamide using !1NAD acceptor; it is a component of the multienzyme complexes !1that catalyze the oxidative decarboxylation of !12-oxoglutarate and pyruvate with the formation of !1succinyl-CoA and acetyl-CoA, respectively CLASSIFICATION #superfamily dihydrolipoamide dehydrogenase; !1dihydrolipoamide dehydrogenase homology KEYWORDS FAD; flavoprotein; lipoamide; NAD; oxidoreductase; !1redox-active disulfide; tricarboxylic acid cycle FEATURE !$11-39 #region beta-alpha-beta FAD nucleotide-binding fold\ !$13-458 #domain dihydrolipoamide dehydrogenase homology !8#label DLD\ !$181-209 #region beta-alpha-beta NAD nucleotide-binding fold\ !$47-52 #disulfide_bonds redox-active #status predicted SUMMARY #length 475 #molecular-weight 49987 #checksum 2181 SEQUENCE /// ENTRY DEAVHL #type complete TITLE dihydrolipoamide dehydrogenase (EC 1.8.1.4) - Azotobacter vinelandii ALTERNATE_NAMES lipoamide reductase ORGANISM #formal_name Azotobacter vinelandii DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 05-May-2000 ACCESSIONS S00360 REFERENCE S00360 !$#authors Westphal, A.H.; de Kok, A. !$#journal Eur. J. Biochem. (1988) 172:299-305 !$#title Lipoamide dehydrogenase from Azotobacter vinelandii. !1Molecular cloning, organization and sequence analysis of the !1gene. !$#cross-references MUID:88166699; PMID:2832161 !$#accession S00360 !'##molecule_type DNA !'##residues 1-477 ##label WES !'##cross-references EMBL:M37307; NID:g142323; PIDN:AAA22139.1; !1PID:g142325 REFERENCE A58151 !$#authors Mattevi, A.; Schierbeek, A.J.; Hol, W.G.J. !$#journal J. Mol. Biol. (1991) 220:975-994 !$#title Refined crystal structure of lipoamide dehydrogenase from !1Azotobacter vinelandii at 2.2 Angstrom resolution. A !1comparison with the structure of glutathione reductase. !$#cross-references MUID:91350192; PMID:1880807 !$#contents annotation COMMENT This protein is a component of the oxoglutarate !1dehydrogenase and pyruvate dehydrogenase multienzyme !1complexes. GENETICS !$#gene lpd CLASSIFICATION #superfamily dihydrolipoamide dehydrogenase; !1dihydrolipoamide dehydrogenase homology KEYWORDS FAD; flavoprotein; homodimer; lipoamide; NAD; !1oxidoreductase; redox-active disulfide; tricarboxylic acid !1cycle FEATURE !$2-477 #product dihydrolipoamide dehydrogenase #status !8experimental #label MAT\ !$2-151 #domain FAD-binding #label FAD\ !$6-34 #region beta-alpha-beta FAD nucleotide-binding fold !8#status experimental\ !$8-458 #domain dihydrolipoamide dehydrogenase homology !8#label DLD\ !$152-281 #domain NAD binding #status experimental #label NAD\ !$183-211 #region beta-alpha-beta NAD nucleotide-binding fold !8#status experimental\ !$282-350 #domain central #label CEN\ !$351-467 #domain dimer interface #label DIM\ !$49-54 #disulfide_bonds redox-active #status experimental\ !$451 #active_site His #status experimental SUMMARY #length 477 #molecular-weight 49567 #checksum 1827 SEQUENCE /// ENTRY DEPSLP #type complete TITLE dihydrolipoamide dehydrogenase (EC 1.8.1.4) - Pseudomonas putida ALTERNATE_NAMES branched-chain-oxoacid dehydrogenase chain E3; lipoamide reductase ORGANISM #formal_name Pseudomonas putida DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 05-May-2000 ACCESSIONS S02139; S03011 REFERENCE S02139 !$#authors Burns, G.; Brown, T.; Hatter, K.; Sokatch, J.R. !$#journal Eur. J. Biochem. (1989) 179:61-69 !$#title Sequence analysis of the lpdV gene for lipoamide !1dehydrogenase of branched-chain-oxoacid dehydrogenase of !1Pseudomonas putida. !$#cross-references MUID:89137095; PMID:2917566 !$#accession S02139 !'##molecule_type DNA !'##residues 1-459 ##label BUR !'##cross-references GB:M57613; EMBL:X14692; NID:g790512; !1PIDN:AAA65618.1; PID:g790518 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing GENETICS !$#gene lpdV CLASSIFICATION #superfamily dihydrolipoamide dehydrogenase; !1dihydrolipoamide dehydrogenase homology KEYWORDS FAD; flavoprotein; homodimer; lipoamide; NAD; !1oxidoreductase; redox-active disulfide; tricarboxylic acid !1cycle FEATURE !$4-143 #domain FAD-binding #label FAD\ !$8-36 #region beta-alpha-beta FAD nucleotide-binding fold\ !$10-445 #domain dihydrolipoamide dehydrogenase homology !8#label DLD\ !$144-269 #domain NAD binding #status predicted #label NAD\ !$174-202 #region beta-alpha-beta NAD nucleotide-binding fold\ !$270-337 #domain central #label CEN\ !$338-454 #domain dimer interface #label DIM\ !$44-49 #disulfide_bonds redox-active #status predicted\ !$438 #active_site His #status predicted SUMMARY #length 459 #molecular-weight 48158 #checksum 2706 SEQUENCE /// ENTRY D55514 #type complete TITLE dihydrolipoamide dehydrogenase (EC 1.8.1.4) [validated] - Alcaligenes eutrophus ORGANISM #formal_name Alcaligenes eutrophus DATE 18-Aug-1995 #sequence_revision 10-May-1996 #text_change 01-Sep-2000 ACCESSIONS D55514 REFERENCE A55514 !$#authors Hein, S.; Steinbuechel, A. !$#journal J. Bacteriol. (1994) 176:4394-4408 !$#title Biochemical and molecular characterization of the !1Alcaligenes eutrophus pyruvate dehydrogenase complex and !1identification of a new type of dihydrolipoamide !1dehydrogenase. !$#cross-references MUID:94292470; PMID:8021225 !$#accession D55514 !'##status preliminary !'##molecule_type DNA !'##residues 1-594 ##label HEI !'##cross-references GB:U09865; NID:g497263; PIDN:AAA21600.1; !1PID:g497266 GENETICS !$#gene pdhL CLASSIFICATION #superfamily Alcaligenes dihydrolipoamide dehydrogenase; !1dihydrolipoamide dehydrogenase homology; lipoyl/ !1biotin-binding homology KEYWORDS FAD; flavoprotein; lipoamide; NAD; oxidoreductase; !1redox-active disulfide FEATURE !$5-77 #domain lipoyl/biotin-binding homology #label LPB\ !$122-150 #region beta-alpha-beta FAD nucleotide-binding fold\ !$124-574 #domain dihydrolipoamide dehydrogenase homology !8#label DLD\ !$298-326 #region beta-alpha-beta NAD nucleotide-binding fold\ !$43 #binding_site lipoamide (Lys) (covalent) #status !8predicted\ !$159-164 #disulfide_bonds redox-active #status predicted SUMMARY #length 594 #molecular-weight 62110 #checksum 2506 SEQUENCE /// ENTRY S42920 #type complete TITLE dihydrolipoamide dehydrogenase (EC 1.8.1.4) NMB1344 [similarity] - Neisseria meningitidis (strain MC58 serogroup B, strain B:4:P1.15) ALTERNATE_NAMES outer membrane protein p64k (PM-6); pyruvate dehydrogenase, E3 component ORGANISM #formal_name Neisseria meningitidis DATE 06-Jan-1995 #sequence_revision 21-Jul-2000 #text_change 19-Jan-2001 ACCESSIONS H81094; S42920 REFERENCE A81000 !$#authors Tettelin, H.; Saunders, N.J.; Heidelberg, J.; Jeffries, !1A.C.; Nelson, K.E.; Eisen, J.A.; Ketchum, K.A.; Hood, D.W.; !1Peden, J.F.; Dodson, R.J.; Nelson, W.C.; Gwinn, M.L.; DeBoy, !1R.; Peterson, J.D.; Hickey, E.K.; Haft, D.H.; Salzberg, !1S.L.; White, O.; Fleischmann, R.D.; Dougherty, B.A.; Mason, !1T.; Ciecko, A.; Parksey, D.S.; Blair, E.; Cittone, H.; !1Clark, E.B.; Cotton, M.D.; Utterback, T.R.; Khouri, H.; Qin, !1H.; Vamathevan, J.; Gill, J.; Scarlato, V.; Masignani, V.; !1Pizza, M.; Grandi, G.; Sun, L.; Smith, H.O.; Fraser, C.M.; !1Moxon, E.R.; Rappuoli, R.; Venter, J.C. !$#journal Science (2000) 287:1809-1815 !$#title Complete genome sequence of Neisseria meningitidis serogroup !1B strain MC58. !$#cross-references MUID:20175755; PMID:10710307 !$#accession H81094 !'##status preliminary !'##molecule_type DNA !'##residues 1-594 ##label TET !'##cross-references GB:AE002482; GB:AE002098; NID:g7226577; !1PIDN:AAF41719.1; PID:g7226588; GSPDB:GN00119; TIGR:NMB1344 !'##experimental_source serogroup B, strain MC58 REFERENCE S42920 !$#authors Silva, R.; Selman, M.; Guillen, G.; Herrera, L.S.; !1Fernandez, J.R.; Novoa, L.I.; Morales, J.; Morera, V.; !1Gonzalez, S.; Tamargo, B.; del Valle, J.A.; Caballero, E.; !1Alvarez, A.; Couzeau, E.; Cruz, S.; Musacchio, A. !$#submission submitted to the EMBL Data Library, February 1994 !$#description Nucleotide sequence for an outer membrane protein from N. !1meningitidis and use of said protein in vaccine !1preparations. !$#accession S42920 !'##molecule_type DNA !'##residues 1-515,'KP',518-594 ##label SIL !'##cross-references EMBL:X77920; NID:g534954; PIDN:CAA54878.1; !1PID:g458843 !'##experimental_source strain B:4:P1.15 GENETICS !$#gene NMB1344; m-6 CLASSIFICATION #superfamily Alcaligenes dihydrolipoamide dehydrogenase; !1dihydrolipoamide dehydrogenase homology; lipoyl/ !1biotin-binding homology KEYWORDS FAD; flavoprotein; lipoamide; NAD; oxidoreductase; !1redox-active disulfide FEATURE !$5-77 #domain lipoyl/biotin-binding homology #label LPB\ !$119-147 #region beta-alpha-beta FAD nucleotide-binding fold\ !$121-574 #domain dihydrolipoamide dehydrogenase homology !8#label DLD\ !$298-326 #region beta-alpha-beta NAD nucleotide-binding fold\ !$43 #binding_site lipoamide (Lys) (covalent) #status !8predicted\ !$156-161 #disulfide_bonds redox-active #status predicted SUMMARY #length 594 #molecular-weight 61828 #checksum 7651 SEQUENCE /// ENTRY G81847 #type complete TITLE dihydrolipoamide dehydrogenase (EC 1.8.1.4) NMA1556 [similarity] - Neisseria meningitidis (strain Z2491 serogroup A) ALTERNATE_NAMES outer membrane protein p64k (PM-6); pyruvate dehydrogenase, E3 component ORGANISM #formal_name Neisseria meningitidis DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 02-Feb-2001 ACCESSIONS G81847 REFERENCE A81775 !$#authors Parkhill, J.; Achtman, M.; James, K.D.; Bentley, S.D.; !1Churcher, C.; Klee, S.R.; Morelli, G.; Basham, D.; Brown, !1D.; Chillingworth, T.; Davies, R.M.; Davis, P.; Devlin, K.; !1Feltwell, T.; Hamlin, N.; Holroyd, S.; Jagels, K.; Leather, !1S.; Moule, S.; Mungall, K.; Quail, M.A.; Rajandream, M.A.; !1Rutherford, K.M.; Simmonds, M.; Skelton, J.; Whitehead, S.; !1Spratt, B.G.; Barrell, B.G. !$#journal Nature (2000) 404:502-506 !$#title Complete DNA sequence of a serogroup A strain of Neisseria !1menigitidis Z2491. !$#cross-references MUID:20222556; PMID:10761919 !$#accession G81847 !'##status preliminary !'##molecule_type DNA !'##residues 1-594 ##label PAR !'##cross-references GB:AL162756; GB:AL157959; NID:g7380091; !1PIDN:CAB84783.1; PID:g7380197; GSPDB:GN00124; NMASP:NMA1556 !'##experimental_source serogroup A, strain Z2491 GENETICS !$#gene lpdA; NMA1556 CLASSIFICATION #superfamily Alcaligenes dihydrolipoamide dehydrogenase; !1dihydrolipoamide dehydrogenase homology; lipoyl/ !1biotin-binding homology KEYWORDS FAD; flavoprotein; lipoamide; NAD; oxidoreductase; !1redox-active disulfide FEATURE !$5-77 #domain lipoyl/biotin-binding homology #label LPB\ !$119-147 #region beta-alpha-beta FAD nucleotide-binding fold\ !$121-574 #domain dihydrolipoamide dehydrogenase homology !8#label DLD\ !$298-326 #region beta-alpha-beta NAD nucleotide-binding fold\ !$43 #binding_site lipoamide (Lys) (covalent) #status !8predicted\ !$156-161 #disulfide_bonds redox-active #status predicted SUMMARY #length 594 #molecular-weight 62105 #checksum 8557 SEQUENCE /// ENTRY I40794 #type complete TITLE dihydrolipoamide dehydrogenase (EC 1.8.1.4) [validated] - Clostridium magnum ALTERNATE_NAMES 2-oxoglutarate dehydrogenase complex chain E3; acetoin dehydrogenase complex chain E3; branched-chain 2-oxoacid dehydrogenase complex chain E3; lipoamide dehydrogenase; pyruvate dehydrogenase complex chain E3; S-complex 50K chain ORGANISM #formal_name Clostridium magnum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS I40794 REFERENCE I40789 !$#authors Kruger, N.; Oppermann, F.B.; Lorenzl, H.; Steinbuchel, A. !$#journal J. Bacteriol. (1994) 176:3614-3630 !$#title Biochemical and molecular characterization of the !1Clostridium magnum acetoin dehydrogenase enzyme system. !$#cross-references MUID:94266715; PMID:8206840 !$#accession I40794 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-578 ##label KRU !'##cross-references GB:L31844; NID:g472324; PIDN:AAA21748.1; !1PID:g472330 FUNCTION !$#description catalyzes the oxidation of dihydrolipoamide to lipoamide !1using NAD !$#pathway acetoin dehydrogenase enzyme system CLASSIFICATION #superfamily Alcaligenes dihydrolipoamide dehydrogenase; !1dihydrolipoamide dehydrogenase homology; lipoyl/ !1biotin-binding homology KEYWORDS FAD; flavoprotein; lipoamide; NAD; oxidoreductase; !1redox-active disulfide FEATURE !$5-77 #domain lipoyl/biotin-binding homology #label LPB\ !$117-145 #region beta-alpha-beta FAD nucleotide-binding fold\ !$119-561 #domain dihydrolipoamide dehydrogenase homology !8#label DLD\ !$287-315 #region beta-alpha-beta NAD nucleotide-binding fold\ !$153-158 #disulfide_bonds redox-active #status predicted SUMMARY #length 578 #molecular-weight 61342 #checksum 930 SEQUENCE /// ENTRY S44026 #type fragment TITLE thioredoxin-disulfide reductase (EC 1.8.1.9) 2 - Arabidopsis thaliana (fragment) ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 06-Nov-1998 #sequence_revision 06-Nov-1998 #text_change 03-Jun-2002 ACCESSIONS S44026 REFERENCE S44026 !$#authors Jacquot, J.P.; Rivera-Madrid, R.; Marinho, P.; Kollarova, !1M.; le Marechal, P.; Miginiac-Maslow, M.; Meyer, Y. !$#journal J. Mol. Biol. (1994) 235:1357-1363 !$#title Arabidopsis thaliana NAPHP thioredoxin reductase. cDNA !1characterization and expression of the recombinant protein !1in Escherichia coli. !$#cross-references MUID:94141931; PMID:8308900 !$#accession S44026 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type mRNA !'##residues 1-302 ##label JAC !'##cross-references EMBL:Z23108; NID:g468523; PIDN:CAA80655.1; !1PID:g468524 !'##experimental_source tissue type siliques !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1993 COMPLEX homodimer; each chain has a tightly associated but !1noncovalently bound FAD FUNCTION !$#description catalyzes the reversible reduction of oxidized thioredoxin !1by NADPH CLASSIFICATION #superfamily thioredoxin reductase; thioredoxin reductase !1homology KEYWORDS FAD; flavoprotein; homodimer; NADP; oxidoreductase; !1redox-active disulfide FEATURE !$1-291 #domain thioredoxin reductase homology (fragment) !8#label TRXB\ !$1-15 #region beta-alpha-beta FAD nucleotide-binding fold !8(fragment)\ !$130-157 #region beta-alpha-beta NADP nucleotide-binding fold\ !$116-119 #disulfide_bonds redox-active #status predicted SUMMARY #length 302 #checksum 8478 SEQUENCE /// ENTRY RDECT #type complete TITLE thioredoxin-disulfide reductase (EC 1.8.1.9) [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 03-Jun-2002 ACCESSIONS A28074; JN0286; A40632; G64827; S71495 REFERENCE A28074 !$#authors Russel, M.; Model, P. !$#journal J. Biol. Chem. (1988) 263:9015-9019 !$#title Sequence of thioredoxin reductase from Escherichia coli. !1Relationship to other flavoprotein disulfide !1oxidoreductases. !$#cross-references MUID:88243771; PMID:3288628 !$#accession A28074 !'##molecule_type DNA !'##residues 1-321 ##label RUS !'##cross-references GB:J03762; NID:g148072; PIDN:AAA24697.1; !1PID:g148073 REFERENCE JN0286 !$#authors Ueshima, R.; Fujita, N.; Ishihama, A. !$#journal Biochem. Biophys. Res. Commun. (1992) 184:634-639 !$#title Identification of Escherichia coli proteins cross-reacting !1with antibodies against region 2.2 peptide of RNA polymerase !1sigma subunit. !$#cross-references MUID:92246944; PMID:1575737 !$#accession JN0286 !'##molecule_type protein !'##residues 'M',3-26 ##label UES REFERENCE A40632 !$#authors Delaney, J.M.; Wall, D.; Georgopoulos, C. !$#journal J. Bacteriol. (1993) 175:166-175 !$#title Molecular characterization of the Escherichia coli htrD !1gene: cloning, sequence, regulation, and involvement with !1cytochrome d oxidase. !$#cross-references MUID:93106951; PMID:8380150 !$#accession A40632 !'##molecule_type DNA !'##residues 257-321 ##label DEL !'##cross-references GB:M95935; NID:g146415 !'##note sequence extracted from NCBI backbone (NCBIN:121156, !1NCBIP:121157); this ORF is not annotated in GenBank entry !1ECOHTRD, release 106.0 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64827 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-321 ##label BLAT !'##cross-references GB:AE000190; GB:U00096; NID:g1787106; !1PIDN:AAC73974.1; PID:g1787114; UWGP:b0888 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S39635 !$#authors Poole, R.K.; Hatch, L.; Cleeter, M.W.J.; Gibson, F.; Cox, !1G.B.; Wu, G. !$#journal Mol. Microbiol. (1993) 10:421-430 !$#title Cytochrome bd biosynthesis in Escherichia coli: the !1sequences of the cydC and cydD genes suggest that they !1encode the components of an ABC membrane transporter. !$#cross-references MUID:95020541; PMID:7934832 !$#accession S71495 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 244-321 ##label POO !'##cross-references EMBL:L21749; NID:g347238; PIDN:AAA66170.1; !1PID:g347239 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1993 REFERENCE A52848 !$#authors Waksman, G.; Krishna, T.S.R.; Williams Jr., C.H.; Kuriyan, !1J. !$#submission submitted to the Brookhaven Protein Data Bank, January 1994 !$#cross-references PDB:1TDE !$#contents annotation; X-ray crystallography, 2.1 angstroms, residues !12-317 REFERENCE A58895 !$#authors Waksman, G.; Krishna, T.S.R.; Williams Jr., C.H.; Kuriyan, !1J. !$#journal J. Mol. Biol. (1994) 236:800-816 !$#title Crystal structure of Escherichia coli thioredoxin reductase !1refined at 2 angstroms resolution: implications for a large !1conformational change during catalysis. !$#cross-references MUID:94157914; PMID:8114095 !$#contents annotation; X-ray crystallography, 2.0 angstroms GENETICS !$#gene trxB !$#map_position 20 min COMPLEX homodimer; each chain has a tightly associated but !1noncovalently bound FAD FUNCTION !$#description EC 1.6.4.5 [validated, PMID:8114095]; catalyzes the !1reversible reduction of oxidized thioredoxin by NADPH CLASSIFICATION #superfamily thioredoxin reductase; thioredoxin reductase !1homology KEYWORDS FAD; flavoprotein; homodimer; NADP; oxidoreductase; !1redox-active disulfide FEATURE !$2-321 #product thioredoxin reductase #status experimental !8#label MAT\ !$3-314 #domain thioredoxin reductase homology #label TRXB\ !$8-39 #region beta-alpha-beta FAD nucleotide-binding fold\ !$148-175 #region beta-alpha-beta NADP nucleotide-binding fold\ !$136-139 #disulfide_bonds redox-active #status experimental SUMMARY #length 321 #molecular-weight 34623 #checksum 4752 SEQUENCE /// ENTRY G64186 #type complete TITLE thioredoxin-disulfide reductase (EC 1.8.1.9) - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 18-Aug-1995 #sequence_revision 18-Oct-1996 #text_change 03-Jun-2002 ACCESSIONS G64186 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession G64186 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-318 ##label TIGR !'##cross-references GB:U32795; GB:L42023; NID:g1574708; !1PIDN:AAC22813.1; PID:g1574715; TIGR:HI1158 !'##note named as homolog to a protein from Escherichia coli COMPLEX homodimer; each chain has a tightly associated but !1noncovalently bound FAD FUNCTION !$#description catalyzes the reversible reduction of oxidized thioredoxin !1by NADPH CLASSIFICATION #superfamily thioredoxin reductase; thioredoxin reductase !1homology KEYWORDS FAD; flavoprotein; homodimer; NADP; oxidoreductase; !1redox-active disulfide FEATURE !$3-313 #domain thioredoxin reductase homology #label TRXB\ !$8-39 #region beta-alpha-beta FAD nucleotide-binding fold\ !$148-175 #region beta-alpha-beta NADP nucleotide-binding fold\ !$136-139 #disulfide_bonds redox-active #status predicted SUMMARY #length 318 #molecular-weight 34395 #checksum 5444 SEQUENCE /// ENTRY S43131 #type complete TITLE thioredoxin-disulfide reductase (EC 1.8.1.9) - Coxiella burnetii ORGANISM #formal_name Coxiella burnetii DATE 25-Dec-1994 #sequence_revision 18-Oct-1996 #text_change 03-Jun-2002 ACCESSIONS S43131 REFERENCE S43131 !$#authors Oswald, W. !$#submission submitted to the EMBL Data Library, November 1993 !$#accession S43131 !'##molecule_type DNA !'##residues 1-321 ##label OSW !'##cross-references EMBL:X75627; NID:g468527; PIDN:CAA53288.1; !1PID:g468528 COMPLEX homodimer; each chain has a tightly associated but !1noncovalently bound FAD FUNCTION !$#description catalyzes the reversible reduction of oxidized thioredoxin !1by NADPH CLASSIFICATION #superfamily thioredoxin reductase; thioredoxin reductase !1homology KEYWORDS FAD; flavoprotein; homodimer; NADP; oxidoreductase; !1redox-active disulfide FEATURE !$3-315 #domain thioredoxin reductase homology #label TRXB\ !$8-39 #region beta-alpha-beta FAD nucleotide-binding fold\ !$149-176 #region beta-alpha-beta NADP nucleotide-binding fold\ !$137-140 #disulfide_bonds redox-active #status predicted SUMMARY #length 321 #molecular-weight 34660 #checksum 4355 SEQUENCE /// ENTRY A53307 #type complete TITLE thioredoxin-disulfide reductase (EC 1.8.1.9) - Streptomyces clavuligerus ORGANISM #formal_name Streptomyces clavuligerus DATE 08-Sep-1995 #sequence_revision 18-Oct-1996 #text_change 03-Jun-2002 ACCESSIONS A53307 REFERENCE A53307 !$#authors Cohen, G.; Yanko, M.; Mislovati, M.; Argaman, A.; Schreiber, !1R.; Av-Gay, Y.; Aharonowitz, Y. !$#journal J. Bacteriol. (1993) 175:5159-5167 !$#title Thioredoxin-thioredoxin reductase system of Streptomyces !1clavuligerus: sequences, expression, and organization of the !1genes. !$#cross-references MUID:93352422; PMID:8349555 !$#accession A53307 !'##molecule_type DNA !'##residues 1-322 ##label COH !'##cross-references GB:Z21946; NID:g287916; PIDN:CAA79940.1; !1PID:g581639 !'##note this publication is not cited in GenBank entry SCTRXABA, !1release 106.0 GENETICS !$#gene trxB !$#start_codon GTG COMPLEX homodimer; each chain has a tightly associated but !1noncovalently bound FAD FUNCTION !$#description catalyzes the reversible reduction of oxidized thioredoxin !1by NADPH CLASSIFICATION #superfamily thioredoxin reductase; thioredoxin reductase !1homology KEYWORDS FAD; flavoprotein; homodimer; NADP; oxidoreductase; !1redox-active disulfide FEATURE !$1-306 #domain thioredoxin reductase homology #label TRXB\ !$6-37 #region beta-alpha-beta FAD nucleotide-binding fold\ !$148-175 #region beta-alpha-beta NADP nucleotide-binding fold\ !$136-139 #disulfide_bonds redox-active #status predicted SUMMARY #length 322 #molecular-weight 34146 #checksum 7851 SEQUENCE /// ENTRY S63990 #type complete TITLE thioredoxin-disulfide reductase (EC 1.8.1.9) - Clostridium litorale ALTERNATE_NAMES glycine reductase complex thioredoxin reductase subunit ORGANISM #formal_name Clostridium litorale DATE 06-Nov-1998 #sequence_revision 06-Nov-1998 #text_change 03-Jun-2002 ACCESSIONS S63990; S63989 REFERENCE S63990 !$#authors Kreimer, S.; Andreesen, J.R. !$#submission submitted to the EMBL Data Library, April 1995 !$#accession S63990 !'##molecule_type DNA !'##residues 1-315 ##label KRE !'##cross-references EMBL:U24268; NID:g1171124; PIDN:AAC43575.1; !1PID:g1171125 REFERENCE S63987 !$#authors Kreimer, S.; Andreesen, J.R. !$#journal Eur. J. Biochem. (1995) 234:192-199 !$#title Glycine reductase of Clostridium litorale. Cloning, !1sequencing, and molecular analysis of the grdAB operon that !1contains two in-frame TGA codons for selenium incorporation. !$#cross-references MUID:96096738; PMID:8529640 !$#accession S63989 !'##molecule_type DNA !'##residues 1-117 ##label KRW !'##cross-references EMBL:U24268; NID:g1171124 GENETICS !$#gene trxB !$#start_codon GTG COMPLEX homodimer; each chain has a tightly associated but !1noncovalently bound FAD FUNCTION !$#description catalyzes the reversible reduction of oxidized thioredoxin !1by NADPH CLASSIFICATION #superfamily thioredoxin reductase; thioredoxin reductase !1homology KEYWORDS FAD; flavoprotein; homodimer; NADP; oxidoreductase; !1redox-active disulfide FEATURE !$1-309 #domain thioredoxin reductase homology #label TRXB\ !$6-34 #region beta-alpha-beta FAD nucleotide-binding fold\ !$146-173 #region beta-alpha-beta NADP nucleotide-binding fold\ !$134-137 #disulfide_bonds redox-active #status predicted SUMMARY #length 315 #molecular-weight 33946 #checksum 4791 SEQUENCE /// ENTRY D35156 #type complete TITLE thioredoxin-disulfide reductase (EC 1.8.1.9) - Eubacterium acidaminophilum ALTERNATE_NAMES dihydrolipoamide dehydrogenase [misidentification] ORGANISM #formal_name Eubacterium acidaminophilum DATE 06-Nov-1998 #sequence_revision 06-Nov-1998 #text_change 03-Jun-2002 ACCESSIONS S38988; D35156 REFERENCE S38988 !$#authors Luebbers, M.; Andreesen, J.R. !$#journal Eur. J. Biochem. (1993) 217:791-798 !$#title Components of glycine reductase from Eubacterium !1acidaminophilum. Cloning, sequencing and identification of !1the genes for thioredoxin reductase, thioredoxin and !1selenoprotein P(A). !$#cross-references MUID:94039119; PMID:8223622 !$#accession S38988 !'##molecule_type DNA !'##residues 1-315 ##label LUE !'##cross-references GB:L04500; NID:g2708733 REFERENCE A35156 !$#authors Dietrichs, D.; Meyer, M.; Schmidt, B.; Andreesen, J.R. !$#journal J. Bacteriol. (1990) 172:2088-2095 !$#title Purification of NADPH-dependent electron-transferring !1flavoproteins and N-terminal protein sequence data of !1dihydrolipoamide dehydrogenases from anaerobic, !1glycine-utilizing bacteria. !$#cross-references MUID:90202731; PMID:2318809 !$#accession D35156 !'##molecule_type protein !'##residues 1-33,'X',35-46,'X',48,'D',50-55 ##label DIE !'##note the designation "atypically small dihydrolipoamide !1dehydrogenase" was revised in refenece S38988 GENETICS !$#gene trxB !$#start_codon GTG COMPLEX homodimer; each chain has a tightly associated but !1noncovalently bound FAD FUNCTION !$#description catalyzes the reversible reduction of oxidized thioredoxin !1by NADPH CLASSIFICATION #superfamily thioredoxin reductase; thioredoxin reductase !1homology KEYWORDS FAD; flavoprotein; homodimer; NADP; oxidoreductase; !1redox-active disulfide FEATURE !$1-309 #domain thioredoxin reductase homology #label TRXB\ !$6-34 #region beta-alpha-beta FAD nucleotide-binding fold\ !$146-173 #region beta-alpha-beta NADP nucleotide-binding fold\ !$134-137 #disulfide_bonds redox-active #status predicted SUMMARY #length 315 #molecular-weight 34019 #checksum 4464 SEQUENCE /// ENTRY A69727 #type complete TITLE thioredoxin-disulfide reductase (EC 1.8.1.9) - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 06-Nov-1998 #sequence_revision 06-Nov-1998 #text_change 03-Jun-2002 ACCESSIONS A69727 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69727 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-316 ##label KUN !'##cross-references GB:Z99121; GB:AL009126; NID:g2635827; !1PIDN:CAB15484.1; PID:g2635992 !'##experimental_source strain 168 GENETICS !$#gene trxB COMPLEX homodimer; each chain has a tightly associated but !1noncovalently bound FAD FUNCTION !$#description catalyzes the reversible reduction of oxidized thioredoxin !1by NADPH CLASSIFICATION #superfamily thioredoxin reductase; thioredoxin reductase !1homology KEYWORDS FAD; flavoprotein; homodimer; NADP; oxidoreductase; !1redox-active disulfide FEATURE !$3-305 #domain thioredoxin reductase homology #label TRXB\ !$8-36 #region beta-alpha-beta FAD nucleotide-binding fold\ !$147-174 #region beta-alpha-beta NADP nucleotide-binding fold\ !$135-138 #disulfide_bonds redox-active #status predicted SUMMARY #length 316 #molecular-weight 34519 #checksum 1280 SEQUENCE /// ENTRY S29117 #type complete TITLE thioredoxin-disulfide reductase (EC 1.8.1.9) - Clostridium pasteurianum ORGANISM #formal_name Clostridium pasteurianum DATE 06-Nov-1998 #sequence_revision 06-Nov-1998 #text_change 03-Jun-2002 ACCESSIONS S29117 REFERENCE S29117 !$#authors Mathieu, I.; Meyer, J.; Moulis, J.M. !$#journal Biochem. J. (1992) 285:255-262 !$#title Cloning, sequencing and expression in Escherichia coli of !1the rubredoxin gene from Clostridium pasteurianum. !$#cross-references MUID:92344580; PMID:1637309 !$#accession S29117 !'##molecule_type DNA !'##residues 1-308 ##label MAT !'##cross-references EMBL:M60116; NID:g144905; PIDN:AAA23276.1; !1PID:g144906 COMPLEX homodimer; each chain has a tightly associated but !1noncovalently bound FAD FUNCTION !$#description catalyzes the reversible reduction of oxidized thioredoxin !1by NADPH CLASSIFICATION #superfamily thioredoxin reductase; thioredoxin reductase !1homology KEYWORDS FAD; flavoprotein; homodimer; NADP; oxidoreductase; !1redox-active disulfide FEATURE !$3-305 #domain thioredoxin reductase homology #label TRXB\ !$8-36 #region beta-alpha-beta FAD nucleotide-binding fold\ !$148-175 #region beta-alpha-beta NADP nucleotide-binding fold\ !$136-139 #disulfide_bonds redox-active #status predicted SUMMARY #length 308 #molecular-weight 34215 #checksum 6017 SEQUENCE /// ENTRY B70164 #type complete TITLE thioredoxin-disulfide reductase (EC 1.8.1.9) - Lyme disease spirochete ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 06-Nov-1998 #sequence_revision 06-Nov-1998 #text_change 03-Jun-2002 ACCESSIONS B70164 REFERENCE A70100 !$#authors Fraser, C.M.; Casjens, S.; Huang, W.M.; Sutton, G.G.; !1Clayton, R.; Lathigra, R.; White, O.; Ketchum, K.A.; Dodson, !1R.; Hickey, E.K.; Gwinn, M.; Dougherty, B.; Tomb, J.F.; !1Fleischmann, R.D.; Richardson, D.; Peterson, J.; Kerlavage, !1A.R.; Quackenbush, J.; Salzberg, S.; Hanson, M.; Vugt, R.V.; !1Palmer, N.; Adams, M.D.; Gocayne, J.; Weidman, J.; !1Utterback, T.; Watthey, L.; McDonald, L.; Artiach, P.; !1Bowman, C.; Garland, S.; Fujii, C.; Cotton, M.D.; Horst, K.; !1Roberts, K.; Hatch, B.; Smith, H.O.; Venter, J.C. !$#journal Nature (1997) 390:580-586 !$#title Genomic sequence of a Lyme disease spirochaete, Borrelia !1burgdorferi. !$#cross-references MUID:98065943; PMID:9403685 !$#accession B70164 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-326 ##label KLE !'##cross-references GB:AE001154; GB:AE000783; NID:g2688431; !1PIDN:AAC66890.1; PID:g2688441; TIGR:BB0515 !'##experimental_source strain B31 COMPLEX homodimer; each chain has a tightly associated but !1noncovalently bound FAD FUNCTION !$#description catalyzes the reversible reduction of oxidized thioredoxin !1by NADPH CLASSIFICATION #superfamily thioredoxin reductase; thioredoxin reductase !1homology KEYWORDS FAD; flavoprotein; homodimer; NADP; oxidoreductase; !1redox-active disulfide FEATURE !$22-325 #domain thioredoxin reductase homology #label TRXB\ !$27-55 #region beta-alpha-beta FAD nucleotide-binding fold\ !$168-195 #region beta-alpha-beta NADP nucleotide-binding fold\ !$156-159 #disulfide_bonds redox-active #status predicted SUMMARY #length 326 #molecular-weight 35673 #checksum 1273 SEQUENCE /// ENTRY B70345 #type complete TITLE thioredoxin-disulfide reductase (EC 1.8.1.9) - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 06-Nov-1998 #sequence_revision 06-Nov-1998 #text_change 03-Jun-2002 ACCESSIONS B70345 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession B70345 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-323 ##label AQF !'##cross-references GB:AE000693; NID:g2983148; PIDN:AAC06756.1; !1PID:g2983154; GB:AE000657 !'##experimental_source strain VF5 GENETICS !$#gene trxB COMPLEX homodimer; each chain has a tightly associated but !1noncovalently bound FAD FUNCTION !$#description catalyzes the reversible reduction of oxidized thioredoxin !1by NADPH CLASSIFICATION #superfamily thioredoxin reductase; thioredoxin reductase !1homology KEYWORDS FAD; flavoprotein; homodimer; NADP; oxidoreductase; !1redox-active disulfide FEATURE !$9-313 #domain thioredoxin reductase homology #label TRXB\ !$14-42 #region beta-alpha-beta FAD nucleotide-binding fold\ !$155-182 #region beta-alpha-beta NADP nucleotide-binding fold\ !$143-146 #disulfide_bonds redox-active #status predicted SUMMARY #length 323 #molecular-weight 35101 #checksum 6169 SEQUENCE /// ENTRY C64211 #type complete TITLE thioredoxin-disulfide reductase (EC 1.8.1.9) - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 06-Nov-1998 #sequence_revision 06-Nov-1998 #text_change 03-Jun-2002 ACCESSIONS C64211 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession C64211 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-315 ##label TIGR !'##cross-references GB:U39689; GB:L43967; NID:g1045773; PID:g1045780; !1TIGR:MG102 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 COMPLEX homodimer; each chain has a tightly associated but !1noncovalently bound FAD FUNCTION !$#description catalyzes the reversible reduction of oxidized thioredoxin !1by NADPH CLASSIFICATION #superfamily thioredoxin reductase; thioredoxin reductase !1homology KEYWORDS FAD; flavoprotein; homodimer; NADP; oxidoreductase; !1redox-active disulfide FEATURE !$13-315 #domain thioredoxin reductase homology #label TRXB\ !$17-48 #region beta-alpha-beta FAD nucleotide-binding fold\ !$157-184 #region beta-alpha-beta NADP nucleotide-binding fold\ !$145-148 #disulfide_bonds redox-active #status predicted SUMMARY #length 315 #molecular-weight 34674 #checksum 2395 SEQUENCE /// ENTRY S73917 #type complete TITLE thioredoxin-disulfide reductase (EC 1.8.1.9) - Mycoplasma pneumoniae (strain ATCC 29342) ALTERNATE_NAMES hypothetical protein K04_orf315 ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 06-Nov-1998 #sequence_revision 06-Nov-1998 #text_change 03-Jun-2002 ACCESSIONS S73917 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73917 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-315 ##label HIM !'##cross-references EMBL:AE000058; GB:U00089; NID:g1674291; !1PIDN:AAB96239.1; PID:g1674293 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#gene trxB !$#genetic_code SGC3 COMPLEX homodimer; each chain has a tightly associated but !1noncovalently bound FAD FUNCTION !$#description catalyzes the reversible reduction of oxidized thioredoxin !1by NADPH CLASSIFICATION #superfamily thioredoxin reductase; thioredoxin reductase !1homology KEYWORDS FAD; flavoprotein; homodimer; NADP; oxidoreductase; !1redox-active disulfide FEATURE !$13-315 #domain thioredoxin reductase homology #label TRXB\ !$17-48 #region beta-alpha-beta FAD nucleotide-binding fold\ !$157-184 #region beta-alpha-beta NADP nucleotide-binding fold\ !$145-148 #disulfide_bonds redox-active #status predicted SUMMARY #length 315 #molecular-weight 34532 #checksum 1333 SEQUENCE /// ENTRY A64623 #type complete TITLE thioredoxin-disulfide reductase (EC 1.8.1.9) - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 06-Nov-1998 #sequence_revision 06-Nov-1998 #text_change 03-Jun-2002 ACCESSIONS A64623 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession A64623 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-311 ##label TOM !'##cross-references GB:AE000594; GB:AE000511; NID:g2313957; !1PIDN:AAD07875.1; PID:g2313959; TIGR:HP0825 COMPLEX homodimer; each chain has a tightly associated but !1noncovalently bound FAD FUNCTION !$#description catalyzes the reversible reduction of oxidized thioredoxin !1by NADPH CLASSIFICATION #superfamily thioredoxin reductase; thioredoxin reductase !1homology KEYWORDS FAD; flavoprotein; homodimer; NADP; oxidoreductase; !1redox-active disulfide FEATURE !$1-308 #domain thioredoxin reductase homology #label TRXB\ !$3-32 #region beta-alpha-beta FAD nucleotide-binding fold\ !$145-172 #region beta-alpha-beta NADP nucleotide-binding fold\ !$133-136 #disulfide_bonds redox-active #status predicted SUMMARY #length 311 #molecular-weight 33538 #checksum 1795 SEQUENCE /// ENTRY A69444 #type complete TITLE thioredoxin-disulfide reductase (EC 1.8.1.9) - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 06-Nov-1998 #sequence_revision 06-Nov-1998 #text_change 03-Jun-2002 ACCESSIONS A69444 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession A69444 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-300 ##label KLE !'##cross-references GB:AE000995; GB:AE000782; NID:g2689318; !1PIDN:AAB89692.1; PID:g2649006; TIGR:AF1554 COMPLEX homodimer; each chain has a tightly associated but !1noncovalently bound FAD FUNCTION !$#description catalyzes the reversible reduction of oxidized thioredoxin !1by NADPH CLASSIFICATION #superfamily thioredoxin reductase; thioredoxin reductase !1homology KEYWORDS FAD; flavoprotein; homodimer; NADP; oxidoreductase; !1redox-active disulfide FEATURE !$1-298 #domain thioredoxin reductase homology #label TRXB\ !$3-31 #region beta-alpha-beta FAD nucleotide-binding fold\ !$141-168 #region beta-alpha-beta NADP nucleotide-binding fold\ !$129-132 #disulfide_bonds redox-active #status predicted SUMMARY #length 300 #molecular-weight 32391 #checksum 8995 SEQUENCE /// ENTRY E69194 #type complete TITLE thioredoxin-disulfide reductase (EC 1.8.1.9) - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 06-Nov-1998 #sequence_revision 06-Nov-1998 #text_change 03-Jun-2002 ACCESSIONS E69194 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession E69194 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-303 ##label MTH !'##cross-references GB:AE000850; GB:AE000666; NID:g2621794; !1PIDN:AAB85213.1; PID:g2621795 !'##experimental_source strain Delta H GENETICS !$#gene MTH708 COMPLEX homodimer; each chain has a tightly associated but !1noncovalently bound FAD FUNCTION !$#description catalyzes the reversible reduction of oxidized thioredoxin !1by NADPH CLASSIFICATION #superfamily thioredoxin reductase; thioredoxin reductase !1homology KEYWORDS FAD; flavoprotein; homodimer; NADP; oxidoreductase; !1redox-active disulfide FEATURE !$1-300 #domain thioredoxin reductase homology #label TRXB\ !$6-34 #region beta-alpha-beta FAD nucleotide-binding fold\ !$144-171 #region beta-alpha-beta NADP nucleotide-binding fold\ !$132-135 #disulfide_bonds redox-active #status predicted SUMMARY #length 303 #molecular-weight 32768 #checksum 1436 SEQUENCE /// ENTRY G64491 #type complete TITLE thioredoxin-disulfide reductase (EC 1.8.1.9) - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 06-Nov-1998 #sequence_revision 06-Nov-1998 #text_change 03-Jun-2002 ACCESSIONS G64491 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession G64491 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-301 ##label BUL !'##cross-references GB:U67594; GB:L77117; NID:g1592160; !1PIDN:AAB99556.1; PID:g1592167; TIGR:MJ1536 GENETICS !$#map_position REV1514708-1513803 COMPLEX homodimer; each chain has a tightly associated but !1noncovalently bound FAD FUNCTION !$#description catalyzes the reversible reduction of oxidized thioredoxin !1by NADPH CLASSIFICATION #superfamily thioredoxin reductase; thioredoxin reductase !1homology KEYWORDS FAD; flavoprotein; homodimer; NADP; oxidoreductase; !1redox-active disulfide FEATURE !$1-298 #domain thioredoxin reductase homology #label TRXB\ !$4-32 #region beta-alpha-beta FAD nucleotide-binding fold\ !$142-169 #region beta-alpha-beta NADP nucleotide-binding fold\ !$130-133 #disulfide_bonds redox-active #status predicted SUMMARY #length 301 #molecular-weight 33034 #checksum 53 SEQUENCE /// ENTRY S76954 #type complete TITLE probable thioredoxin-disulfide reductase (EC 1.8.1.9) - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 06-Nov-1998 #sequence_revision 06-Nov-1998 #text_change 03-Jun-2002 ACCESSIONS S76954 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76954 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-326 ##label KAN !'##cross-references EMBL:D90917; GB:AB001339; NID:g1653836; !1PIDN:BAA18866.1; PID:g1653956 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#start_codon GTG COMPLEX homodimer; each chain has a tightly associated but !1noncovalently bound FAD FUNCTION !$#description catalyzes the reversible reduction of oxidized thioredoxin !1by NADPH CLASSIFICATION #superfamily thioredoxin reductase; thioredoxin reductase !1homology KEYWORDS FAD; flavoprotein; homodimer; NADP; oxidoreductase; !1redox-active disulfide FEATURE !$11-315 #domain thioredoxin reductase homology #label TRXB\ !$18-45 #region beta-alpha-beta FAD nucleotide-binding fold\ !$165-192 #region beta-alpha-beta NADP nucleotide-binding fold\ !$153-156 #disulfide_bonds redox-active #status predicted SUMMARY #length 326 #molecular-weight 35993 #checksum 401 SEQUENCE /// ENTRY B49888 #type complete TITLE thioredoxin-disulfide reductase (EC 1.8.1.9) - Penicillium chrysogenum ALTERNATE_NAMES 72K broad-range disulfide reductase ORGANISM #formal_name Penicillium chrysogenum DATE 06-Nov-1998 #sequence_revision 06-Nov-1998 #text_change 03-Jun-2002 ACCESSIONS B49888 REFERENCE A49888 !$#authors Cohen, G.; Argaman, A.; Schreiber, R.; Mislovati, M.; !1Aharonowitz, Y. !$#journal J. Bacteriol. (1994) 176:973-984 !$#title The thioredoxin system of Penicillium chrysogenum and its !1possible role in penicillin biosynthesis. !$#cross-references MUID:94148789; PMID:8106340 !$#accession B49888 !'##status preliminary !'##molecule_type DNA !'##residues 1-334 ##label COH !'##cross-references GB:X76119; NID:g426467; PIDN:CAA53725.1; !1PID:g4379348 !'##note the translation is not provided in GenBank entry PCTRXB, !1release 106.0 !'##note authors translated the codon GCT for residue 13 as Pro GENETICS !$#gene trxB !$#introns 8/1; 308/1 COMPLEX homodimer; each chain has a tightly associated but !1noncovalently bound FAD FUNCTION !$#description catalyzes the reversible reduction of oxidized thioredoxin !1by NADPH CLASSIFICATION #superfamily thioredoxin reductase; thioredoxin reductase !1homology KEYWORDS FAD; flavoprotein; NADP; oxidoreductase; redox-active !1disulfide FEATURE !$1-321 #domain thioredoxin reductase homology #label TRXB\ !$5-41 #region beta-alpha-beta FAD nucleotide-binding fold\ !$159-186 #region beta-alpha-beta NADP nucleotide-binding fold\ !$145-148 #disulfide_bonds redox-active #status predicted SUMMARY #length 334 #molecular-weight 35701 #checksum 8264 SEQUENCE /// ENTRY S44027 #type complete TITLE thioredoxin-disulfide reductase (EC 1.8.1.9) 2 [validated] - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 06-Nov-1998 #sequence_revision 06-Nov-1998 #text_change 03-Jun-2002 ACCESSIONS S44027; S50882 REFERENCE S44026 !$#authors Jacquot, J.P.; Rivera-Madrid, R.; Marinho, P.; Kollarova, !1M.; le Marechal, P.; Miginiac-Maslow, M.; Meyer, Y. !$#journal J. Mol. Biol. (1994) 235:1357-1363 !$#title Arabidopsis thaliana NAPHP thioredoxin reductase. cDNA !1characterization and expression of the recombinant protein !1in Escherichia coli. !$#cross-references MUID:94141931; PMID:8308900 !$#accession S44027 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-333 ##label JAC !'##cross-references EMBL:Z23109 REFERENCE S50882 !$#authors Meyer, Y. !$#submission submitted to the EMBL Data Library, June 1993 !$#accession S50882 !'##molecule_type mRNA !'##residues 1-51,'NQPPR',58-333 ##label MEY !'##cross-references EMBL:Z23109; NID:g468525; PIDN:CAA80656.1; !1PID:g468526 !'##experimental_source tissue type siliques REFERENCE A66845 !$#authors Dai, S.; Eklund, H. !$#submission submitted to the Brookhaven Protein Data Bank, September !11996 !$#cross-references PDB:1VDC !$#contents annotation; X-ray crystallography, 2.5 angstroms, residues !14-125,'R',127-138,'F',140-188,'H',190-325 REFERENCE A58899 !$#authors Dai, S.; Saarinen, M.; Ramaswamy, S.; Meyer, Y.; Jacquot, !1J.P.; Eklund, H. !$#journal J. Mol. Biol. (1996) 264:1044-1057 !$#title Crystal structure of Arabidopsis thaliana NADPH dependent !1thioredoxin reductase at 2.5 Angstroms resolution. !$#cross-references MUID:97153339; PMID:9000629 !$#contents annotation; X-ray crystallography, 2.5 angstroms COMPLEX homodimer; each chain has a tightly associated but !1noncovalently bound FAD FUNCTION !$#description catalyzes the reversible reduction of oxidized thioredoxin !1by NADPH CLASSIFICATION #superfamily thioredoxin reductase; thioredoxin reductase !1homology KEYWORDS FAD; flavoprotein; homodimer; NADP; oxidoreductase; !1redox-active disulfide FEATURE !$6-322 #domain thioredoxin reductase homology #label TRXB\ !$10-46 #region beta-alpha-beta FAD nucleotide-binding fold\ !$161-188 #region beta-alpha-beta NADP nucleotide-binding fold\ !$147-150 #disulfide_bonds redox-active #status experimental SUMMARY #length 333 #molecular-weight 35354 #checksum 2553 SEQUENCE /// ENTRY S48948 #type complete TITLE thioredoxin-disulfide reductase (EC 1.8.1.9) TRR2 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YHR106w ORGANISM #formal_name Saccharomyces cerevisiae DATE 06-Nov-1998 #sequence_revision 06-Nov-1998 #text_change 03-Jun-2002 ACCESSIONS S48948 REFERENCE S46676 !$#authors Latreille, P. !$#submission submitted to the EMBL Data Library, May 1994 !$#description The sequence of S. cerevisiae cosmid 8263. !$#accession S48948 !'##molecule_type DNA !'##residues 1-342 ##label LAT !'##cross-references EMBL:U00059; NID:g529116; PIDN:AAB68856.1; !1PID:g529123; GSPDB:GN00008; MIPS:YHR106w GENETICS !$#gene SGD:TRR2; MIPS:YHR106w !'##cross-references MIPS:YHR106w; SGD:S0001148 !$#map_position 8R COMPLEX homodimer; each chain has a tightly associated but !1noncovalently bound FAD FUNCTION !$#description catalyzes the reversible reduction of oxidized thioredoxin !1by NADPH CLASSIFICATION #superfamily thioredoxin reductase; thioredoxin reductase !1homology KEYWORDS FAD; flavoprotein; NADP; oxidoreductase; redox-active !1disulfide FEATURE !$24-338 #domain thioredoxin reductase homology #label TRXB\ !$28-64 #region beta-alpha-beta FAD nucleotide-binding fold\ !$179-206 #region beta-alpha-beta NADP nucleotide-binding fold\ !$165-168 #disulfide_bonds redox-active #status predicted SUMMARY #length 342 #molecular-weight 37087 #checksum 579 SEQUENCE /// ENTRY S61150 #type complete TITLE thioredoxin-disulfide reductase (EC 1.8.1.9) TRR1 [validated] - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES peroxide reductase, thioredoxin-dependent; protector 35K protein; protein D9476.5; protein YDR353w ORGANISM #formal_name Saccharomyces cerevisiae DATE 06-Nov-1998 #sequence_revision 06-Nov-1998 #text_change 03-Jun-2002 ACCESSIONS S61150; S47907; A55468; PC2244 REFERENCE S61148 !$#authors Du, Z. !$#submission submitted to the EMBL Data Library, June 1995 !$#description The sequence of S. cerevisiae cosmid 9476. !$#accession S61150 !'##molecule_type DNA !'##residues 1-319 ##label DUZ !'##cross-references EMBL:U28372; NID:g849170; PIDN:AAB64789.1; !1PID:g849175; GSPDB:GN00004; MIPS:YDR353w REFERENCE S47907 !$#authors Chae, H.; Chung, S.; Rhee, S. !$#submission submitted to the EMBL Data Library, June 1994 !$#description Thioredoxin-dependent peroxide reductase from yeast. !$#accession S47907 !'##molecule_type DNA !'##residues 1-17,'V',19-100,'A',102-110,'A',112-179,'CLC',183,'SE',186, !1'TICVLLPLCK',197-319 ##label CHA !'##cross-references EMBL:U10274; NID:g520500; PIDN:AAA64747.1; !1PID:g520501 REFERENCE A55468 !$#authors Chae, H.Z.; Chung, S.J.; Rhee, S.G. !$#journal J. Biol. Chem. (1994) 269:27670-27678 !$#title Thioredoxin-dependent peroxide reductase from yeast. !$#cross-references MUID:95050519; PMID:7961686 !$#accession A55468 !'##molecule_type DNA !'##residues 1-100,'A',102-110,'A',112-179,'CLC',183,'SE',186, !1'TICVLLPLCK',197-319 ##label CHF !'##cross-references GB:U10274; NID:g520500; PIDN:AAA64747.1; !1PID:g520501 !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing REFERENCE PC2231 !$#authors Kwon, S.J.; Park, J.W.; Choi, W.K.; Kim, I.H.; Kim, K. !$#journal Biochem. Biophys. Res. Commun. (1994) 201:8-15 !$#title Inhibition of metal-catalyzed oxidation systems by a yeast !1protector protein in the presence of thioredoxin. !$#cross-references MUID:94257026; PMID:7911017 !$#accession PC2244 !'##molecule_type protein !'##residues 2-4,'I',6-9,'X',11,'X',13-16 ##label KWO !'##experimental_source strain BJ926 GENETICS !$#gene SGD:TRR1; MIPS:YDR353w !'##cross-references MIPS:YDR353w; SGD:S0002761 !$#map_position 4R COMPLEX homodimer; each chain has a tightly associated but !1noncovalently bound FAD [validated, MUID:95050519] FUNCTION !$#description EC 1.6.4.5 [validated, MUID:95050519]; catalyzes the !1reversible reduction of oxidized thioredoxin by NADPH CLASSIFICATION #superfamily thioredoxin reductase; thioredoxin reductase !1homology KEYWORDS FAD; flavoprotein; NADP; oxidoreductase; redox-active !1disulfide FEATURE !$1-315 #domain thioredoxin reductase homology #label TRXB\ !$2-319 #product thioredoxin reductase #status experimental !8#label MAT\ !$5-41 #region beta-alpha-beta FAD nucleotide-binding fold\ !$156-183 #region beta-alpha-beta NADP nucleotide-binding fold\ !$142-145 #disulfide_bonds redox-active #status predicted SUMMARY #length 319 #molecular-weight 34238 #checksum 5697 SEQUENCE /// ENTRY G69759 #type complete TITLE thioredoxin reductase homolog ycgT - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS G69759 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69759 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-336 ##label KUN !'##cross-references GB:Z99105; GB:AL009126; NID:g2632457; !1PIDN:CAB12121.1; PID:g2632613 !'##experimental_source strain 168 GENETICS !$#gene ycgT CLASSIFICATION #superfamily thioredoxin reductase; thioredoxin reductase !1homology SUMMARY #length 336 #molecular-weight 36967 #checksum 7992 SEQUENCE /// ENTRY B70015 #type complete TITLE thioredoxin reductase homolog yumC - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS B70015 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B70015 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-332 ##label KUN !'##cross-references GB:Z99120; GB:AL009126; NID:g2635613; !1PIDN:CAB15201.1; PID:g2635708 !'##experimental_source strain 168 GENETICS !$#gene yumC CLASSIFICATION #superfamily thioredoxin reductase; thioredoxin reductase !1homology SUMMARY #length 332 #molecular-weight 36840 #checksum 335 SEQUENCE /// ENTRY S77662 #type complete TITLE thioredoxin-disulfide reductase (EC 1.8.1.9) / thioredoxin - Mycobacterium leprae ALTERNATE_NAMES TR/Trx hybrid protein ORGANISM #formal_name Mycobacterium leprae DATE 06-Nov-1998 #sequence_revision 06-Nov-1998 #text_change 03-Jun-2002 ACCESSIONS S77662 REFERENCE S77662 !$#authors Wieles, B.; van Soolingen, D.; Holmgren, A.; Offringa, R.; !1Ottenhoff, T.; Thole, J. !$#journal Mol. Microbiol. (1995) 16:921-929 !$#title Unique gene organization of thioredoxin and thioredoxin !1reductase in Mycobacterium leprae. !$#cross-references MUID:96059638; PMID:7476189 !$#accession S77662 !'##molecule_type DNA !'##residues 1-458 ##label WIE !'##cross-references EMBL:X87899; NID:g871418; PIDN:CAA61150.1; !1PID:g871419 GENETICS !$#gene tr/trx FUNCTION !$#description catalyzes the reversible reduction of oxidized thioredoxin !1by NADPH !$#note in this organism this protein functions as both enzyme and !1substrate CLASSIFICATION #superfamily Mycobacterium leprae thioredoxin reductase / !1thioredoxin; thioredoxin homology; thioredoxin reductase !1homology KEYWORDS FAD; flavoprotein; NADP; oxidoreductase; redox-active !1disulfide FEATURE !$1-321 #domain thioredoxin reductase (NADPH) #status !8predicted #label TRR\ !$14-312 #domain thioredoxin reductase homology #label TRXB\ !$14-42 #region beta-alpha-beta FAD nucleotide-binding fold\ !$155-168 #region beta-alpha-beta NADP nucleotide-binding fold\ !$322-341 #region linker\ !$342-458 #domain thioredoxin #status predicted #label TRX\ !$357-440 #domain thioredoxin homology #label THR\ !$142-145,379-382 #disulfide_bonds redox-active #status predicted SUMMARY #length 458 #molecular-weight 49046 #checksum 6642 SEQUENCE /// ENTRY DNHUN1 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 1 - human mitochondrion ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 1 ORGANISM #formal_name mitochondrion Homo sapiens #common_name man DATE 22-May-1981 #sequence_revision 23-Oct-1981 #text_change 03-Jun-2002 ACCESSIONS A00407 REFERENCE A00151 !$#authors Anderson, S.; Bankier, A.T.; Barrell, B.G.; de Bruijn, !1M.H.L.; Coulson, A.R.; Drouin, J.; Eperon, I.C.; Nierlich, !1D.P.; Roe, B.A.; Sanger, F.; Schreier, P.H.; Smith, A.J.H.; !1Staden, R.; Young, I.G. !$#journal Nature (1981) 290:457-465 !$#title Sequence and organization of the human mitochondrial genome. !$#cross-references MUID:81173052; PMID:7219534 !$#accession A00407 !'##molecule_type DNA !'##residues 1-318 ##label AND !'##cross-references GB:J01415; GB:M12548; GB:M58503; GB:M63932; !1GB:M63933; NID:g1944628; PIDN:AAB58943.1; PID:g337189; !1EMBL:V00662; NID:g13003; PID:g13004; GSPDB:GN00100 GENETICS !$#gene GDB:MTND1 !'##cross-references GDB:118911; OMIM:516000 !$#map_position MTH3307-4262 !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 1 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 318 #molecular-weight 35660 #checksum 9373 SEQUENCE /// ENTRY QXBO1M #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 1 - bovine mitochondrion ALTERNATE_NAMES NADH dehydrogenase (ubiquinone) 29K chain; NADH-ubiquinone oxidoreductase chain 1 ORGANISM #formal_name mitochondrion Bos primigenius taurus #common_name cattle DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 03-Jun-2002 ACCESSIONS A00408; A31910 REFERENCE A00152 !$#authors Anderson, S.; de Bruijn, M.H.L.; Coulson, A.R.; Eperon, !1I.C.; Sanger, F.; Young, I.G. !$#journal J. Mol. Biol. (1982) 156:683-717 !$#title Complete sequence of bovine mitochondrial DNA. Conserved !1features of the mammalian mitochondrial genome. !$#cross-references MUID:83010260; PMID:7120390 !$#accession A00408 !'##molecule_type DNA !'##residues 1-318 ##label AND !'##cross-references GB:J01394; NID:g336430; PIDN:AAB59268.1; !1PID:g336431; EMBL:V00654; NID:g12800; PID:g12801 REFERENCE A31910 !$#authors Yagi, T.; Hatefi, Y. !$#journal J. Biol. Chem. (1988) 263:16150-16155 !$#title Identification of the dicyclohexylcarbodiimide-binding !1subunit of NADH-ubiquinone oxidoreductase (complex I). !$#cross-references MUID:89034077; PMID:3141400 !$#accession A31910 !'##molecule_type protein !'##residues 1-15 ##label YAG GENETICS !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 1 KEYWORDS blocked amino end; membrane-associated complex; !1mitochondrion; NAD; oxidative phosphorylation; !1oxidoreductase; respiratory chain FEATURE !$1 #modified_site N-formylmethionine #status !8experimental SUMMARY #length 318 #molecular-weight 35670 #checksum 7533 SEQUENCE /// ENTRY QXMS1M #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 1 - mouse mitochondrion ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 1 ORGANISM #formal_name mitochondrion Mus musculus #common_name house mouse DATE 02-Apr-1982 #sequence_revision 17-Jul-1998 #text_change 03-Jun-2002 ACCESSIONS A00409 REFERENCE A00153 !$#authors Bibb, M.J.; Van Etten, R.A.; Wright, C.T.; Walberg, M.W.; !1Clayton, D.A. !$#journal Cell (1981) 26:167-180 !$#title Sequence and gene organization of mouse mitochondrial DNA. !$#cross-references MUID:82137051; PMID:7332926 !$#accession A00409 !'##molecule_type DNA !'##residues 1-315 ##label BIB !'##cross-references GB:J01420; NID:g342520; PIDN:AAB48644.1; !1PID:g896295 !'##note the authors translated the initiation codon ATT for residue 1 !1as Ile GENETICS !$#gene ND1 !$#genome mitochondrion !$#genetic_code SGC1 !$#start_codon ATT CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 1 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 315 #molecular-weight 35651 #checksum 782 SEQUENCE /// ENTRY QQRT1M #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 1 - rat mitochondrion ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 1 ORGANISM #formal_name mitochondrion Rattus norvegicus #common_name Norway rat DATE 02-Apr-1982 #sequence_revision 15-Oct-1994 #text_change 03-Jun-2002 ACCESSIONS S04747; A00410; S16157; S16887; I48222; S01954 REFERENCE S04747 !$#authors Gadaleta, G.; Pepe, G.; De Candia, G.; Quagliariello, C.; !1Sbisa, E.; Saccone, C. !$#journal J. Mol. Evol. (1989) 28:497-516 !$#title The complete nucleotide sequence of the Rattus norvegicus !1mitochondrial genome: cryptic signals revealed by !1comparative analysis between vertebrates. !$#cross-references MUID:89362487; PMID:2504926 !$#accession S04747 !'##molecule_type DNA !'##residues 1-318 ##label GAD !'##cross-references EMBL:X14848; NID:g854269; PIDN:CAA32954.1; !1PID:g578783 !'##note the authors translated the initiation codon GTG for residue 1 !1as Val REFERENCE A00410 !$#authors Saccone, C.; Cantatore, P.; Gadaleta, G.; Gallerani, R.; !1Lanave, C.; Pepe, G.; Kroon, A.M. !$#journal Nucleic Acids Res. (1981) 9:4139-4148 !$#title The nucleotide sequence of the large ribosomal RNA gene and !1the adjacent tRNA genes from rat mitochondria. !$#cross-references MUID:82059452; PMID:6913863 !$#accession A00410 !'##molecule_type DNA !'##residues 4-86 ##label SAC REFERENCE S16157 !$#authors Davies, J.D.; Wilson, D.H.; Hermel, E.; Fischer-Lindahl, K.; !1Butcher, G.W.; Wilson, D.B. !$#journal J. Exp. Med. (1991) 173:823-832 !$#title Generation of T cells with lytic specificity for atypical !1antigens. I. A mitochondrial antigen in the rat. !$#cross-references MUID:91178443; PMID:1672544 !$#accession S16157 !'##molecule_type DNA !'##residues 1-17,'AF',20-72 ##label DAV !'##cross-references EMBL:X56833 REFERENCE S16887 !$#authors Hermel, E. !$#submission submitted to the EMBL Data Library, December 1990 !$#accession S16887 !'##molecule_type DNA !'##residues 1-17,'AF',20-32,'S',34-72 ##label HER !'##cross-references EMBL:X56833; NID:g13473; PIDN:CAA40164.1; !1PID:g578782 REFERENCE I48222 !$#authors Gadaleta, G.; Pepe, G.; De Candia, G.; Quagliariello, C.; !1Sbisa, E.; Saccone, C. !$#journal Nucleic Acids Res. (1988) 16:6233 !$#title Nucleotide sequence of rat mitochondrial NADH dehydrogenase !1subunit 1. GTG, a new initiator codon in vertebrate !1mitochondrial genome. !$#cross-references MUID:88289373; PMID:3399396 !$#accession I48222 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-318 ##label GA2 !'##cross-references EMBL:X07479; NID:g13472; PIDN:CAB50772.1; !1PID:g5514772 !'##note sequence modified relative to PID:g929676 (GTG start codon !1interpreted as Met) GENETICS !$#gene nd1 !$#genome mitochondrion !$#genetic_code SGC1 !$#start_codon GTG CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 1 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 318 #molecular-weight 36177 #checksum 8676 SEQUENCE /// ENTRY QXXL1M #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 1 - African clawed frog mitochondrion ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 1 ORGANISM #formal_name mitochondrion Xenopus laevis #common_name African clawed frog DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 03-Jun-2002 ACCESSIONS A00411 REFERENCE A00155 !$#authors Roe, B.A.; Ma, D.P.; Wilson, R.K.; Wong, J.F.H. !$#journal J. Biol. Chem. (1985) 260:9759-9774 !$#title The complete nucleotide sequence of the Xenopus laevis !1mitochondrial genome. !$#cross-references MUID:85261388; PMID:4019494 !$#accession A00411 !'##molecule_type DNA !'##residues 1-323 ##label ROE !'##cross-references GB:M10217; GB:X01600; GB:X01601; GB:X02890; !1NID:g343717; PIDN:AAA66458.1; PID:g807683 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 1 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 323 #molecular-weight 35861 #checksum 7778 SEQUENCE /// ENTRY DNWTU1 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 1 - wheat mitochondrion ORGANISM #formal_name mitochondrion Triticum aestivum #common_name common wheat DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 03-Jun-2002 ACCESSIONS A38489; C38489 REFERENCE A38489 !$#authors Chapdelaine, Y.; Bonen, L. !$#journal Cell (1991) 65:465-472 !$#title The wheat mitochondrial gene for subunit I of the NADH !1dehydrogenase complex: a trans-splicing model for this !1gene-in-pieces. !$#cross-references MUID:91208683; PMID:1902143 !$#accession A38489 !'##molecule_type mRNA !'##residues 1-325 ##label CHA !'##cross-references EMBL:X57968 !$#accession C38489 !'##molecule_type DNA !'##residues 'T',2-71,'S',73-102,'P',104-145,'P',147-163,'P',165-166, !1'S',168-178,'S',180-190,'L',192,'PR',195-202,'S',204-224, !1'S',226-244,'S',246-247,'P',249-325 ##label CHA2 !'##cross-references EMBL:X57968; NID:g14277; PIDN:CAA41034.1; !1PID:g1334612 GENETICS !$#gene nad1 !$#genome mitochondrion !$#introns 129/2; 156/3; 220/3; 240/2 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 1 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain; RNA !1editing SUMMARY #length 325 #molecular-weight 35932 #checksum 4363 SEQUENCE /// ENTRY S49576 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 1 - Arabidopsis thaliana mitochondrion ORGANISM #formal_name mitochondrion Arabidopsis thaliana #common_name mouse-ear cress DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S49576 REFERENCE S49576 !$#authors Schuster, W. !$#submission submitted to the EMBL Data Library, November 1994 !$#accession S49576 !'##molecule_type mRNA !'##residues 1-325 ##label SCH !'##cross-references EMBL:X82618; NID:g572520; PIDN:CAA57940.1; !1PID:g572521 GENETICS !$#gene NAD1 !$#genome mitochondrion CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 1 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 325 #molecular-weight 36030 #checksum 3409 SEQUENCE /// ENTRY B40358 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 1 - garden petunia mitochondrion ORGANISM #formal_name mitochondrion Petunia x hybrida #common_name garden petunia DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS B40358; A40358 REFERENCE A40358 !$#authors Conklin, P.L.; Wilson, R.K.; Hanson, M.R. !$#journal Genes Dev. (1991) 5:1407-1415 !$#title Multiple trans-splicing events are required to produce a !1mature nad1 transcript in a plant mitochondrion. !$#cross-references MUID:91331312; PMID:1869047 !$#accession B40358 !'##molecule_type mRNA !'##residues 1-325 ##label CON !$#accession A40358 !'##molecule_type DNA !'##residues 1-71,'S',73-88,'R',90-102,'P',104-145,'P',147-164,'R',166, !1'S',168-178,'S',180-193,'R',195-211,'S',213-224,'S',226-227, !1'S',229-246,'SP',249-251,'P',253-259,'S',261-274,'L', !1276-299,'R',301-309,'R',311-312,'P',314-325 ##label CO2 !'##cross-references GB:X60402 GENETICS !$#genome mitochondrion CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 1 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain; RNA !1editing SUMMARY #length 325 #molecular-weight 35956 #checksum 3818 SEQUENCE /// ENTRY S25993 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 1 - liverwort (Marchantia polymorpha) mitochondrion ORGANISM #formal_name mitochondrion Marchantia polymorpha DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S25993 REFERENCE S25941 !$#authors Oda, K.; Yamato, K.; Ohta, E.; Nakamura, Y.; Takemura, M.; !1Nozato, N.; Akashi, K.; Kanegae, T.; Ogura, Y.; Kohchi, T.; !1Ohyama, K. !$#journal J. Mol. Biol. (1992) 223:1-7 !$#title Gene organization deduced from the complete sequence of !1liverwort Marchantia polymorpha mitochondrial DNA. A !1primitive form of plant mitochondrial genome. !$#cross-references MUID:92114051; PMID:1731062 !$#accession S25993 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-328 ##label ODA !'##cross-references EMBL:M68929; NID:g786182; PIDN:AAC09438.1; !1PID:g786224 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1February 1992 GENETICS !$#gene nad1 !$#genome mitochondrion CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 1 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 328 #molecular-weight 36518 #checksum 2653 SEQUENCE /// ENTRY DNOBU1 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 1 - evening primrose mitochondrion ORGANISM #formal_name mitochondrion Oenothera villaricae #common_name evening primrose DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 03-Jun-2002 ACCESSIONS C38490; A38490 REFERENCE A38490 !$#authors Wissinger, B.; Schuster, W.; Brennicke, A. !$#journal Cell (1991) 65:473-482 !$#title Trans splicing in Oenothera mitochondria: nad1 mRNAs are !1edited in exon and trans-splicing group II intron sequences. !$#cross-references MUID:91208684; PMID:1850322 !$#accession C38490 !'##molecule_type mRNA !'##residues 1-331 ##label WIS !'##cross-references GB:M63033 !$#accession A38490 !'##molecule_type DNA !'##residues 1-6,'T',8-94,'R',97-108,'P',110-128,'T',130-131,'R', !1133-169,'PR',172,'S',174-184,'S',186-199,'R',201-217,'S', !1219-230,'S',232-250,'S',252,'SP',255-257,'P',259-280,'L', !1282-305,'R',307-315,'R',317-318,'P',320-331 ##label WIS2 !'##cross-references GB:M63033 !'##note it is uncertain whether Met-1 or Met-7 is the initiator GENETICS !$#gene nad1 !$#genome mitochondrion !$#introns 135/1; 162/3; 226/3; 246/2 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 1 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain; RNA !1editing SUMMARY #length 331 #molecular-weight 36667 #checksum 5437 SEQUENCE /// ENTRY DENTN1 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 1 - common tobacco chloroplast ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 1; ndh1 protein ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 03-Jun-2002 ACCESSIONS A00412 REFERENCE A00149 !$#authors Sugiura, M. !$#submission submitted to the EMBL Data Library, August 1986 !$#accession A00412 !'##molecule_type DNA !'##residues 1-333 ##label SUG !'##experimental_source cv. Bright Yellow 4 REFERENCE A38013 !$#authors Shinozaki, K.; Ohme, M.; Tanaka, M.; Wakasugi, T.; !1Hayashida, N.; Matsubayashi, T.; Zaita, N.; Chunwongse, J.; !1Obokata, J.; Yamaguchi-Shinozaki, K.; Ohto, C.; Torazawa, !1K.; Meng, B.Y.; Sugita, M.; Deno, H.; Kamogashira, T.; !1Yamada, K.; Kusuda, J.; Takaiwa, F.; Kato, A.; Tohdoh, N.; !1Shimada, H.; Sugiura, M. !$#journal EMBO J. (1986) 5:2043-2049 !$#title The complete nucleotide sequence of the tobacco chloroplast !1genome: its gene organization and expression. !$#contents annotation; gene organization, sites, features GENETICS !$#gene ndh1; ndhA !$#genome chloroplast !$#introns 185/2 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 1 KEYWORDS chloroplast; membrane-associated complex; NAD; !1oxidoreductase SUMMARY #length 333 #molecular-weight 37049 #checksum 8110 SEQUENCE /// ENTRY DELVN1 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 1 - liverwort (Marchantia polymorpha) chloroplast ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 1; ndh1 protein ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 03-Jun-2002 ACCESSIONS A00413; S01523 REFERENCE A00150 !$#authors Ohyama, K. !$#submission submitted to the EMBL Data Library, October 1986 !$#accession A00413 !'##molecule_type DNA !'##residues 1-368 ##label OHY REFERENCE S01512 !$#authors Kohchi, T.; Shirai, H.; Fukuzawa, H.; Sano, T.; Komano, T.; !1Umesono, K.; Inokuchi, H.; Ozeki, H.; Ohyama, K. !$#journal J. Mol. Biol. (1988) 203:353-372 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. IV. Inverted repeat and small single !1copy regions. !$#cross-references MUID:89068688; PMID:3199437 !$#accession S01523 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-368 ##label KOH !'##cross-references GB:X04465; GB:Y00686; NID:g11640; PIDN:CAA28139.1; !1PID:g456521 REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features GENETICS !$#gene ndh1; ndhA !$#genome chloroplast !$#introns 186/1 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 1 KEYWORDS chloroplast; membrane-associated complex; NAD; !1oxidoreductase SUMMARY #length 368 #molecular-weight 41510 #checksum 6337 SEQUENCE /// ENTRY DERZN1 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 1 - rice chloroplast ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 1; ndh1 protein ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 03-Jun-2002 ACCESSIONS JQ0293; S05173 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0293 !'##molecule_type DNA !'##residues 1-362 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05173 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-362 ##label HIR !'##cross-references EMBL:X15901; NID:g11957; PIDN:CAA33910.1; !1PID:g669087 !'##experimental_source cv. Nihonbare GENETICS !$#gene ndhA !$#map_position CP112706-112157,111169-110631 !$#genome chloroplast !$#introns 184/1 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 1 KEYWORDS chloroplast; membrane-associated complex; NAD; !1oxidoreductase SUMMARY #length 362 #molecular-weight 40355 #checksum 9402 SEQUENCE /// ENTRY QXYB1 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 1 - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 31-Mar-1992 #sequence_revision 30-Jun-1993 #text_change 03-Jun-2002 ACCESSIONS S27972; S18046; S76038 REFERENCE S27972 !$#authors Ellersiek, U.; Steinmueller, K. !$#journal Plant Mol. Biol. (1992) 20:1097-1110 !$#title Cloning and transcription analysis of the ndh(A-I-G-E) gene !1cluster and the ndhD gene of the cyanobacterium !1Synechocystis sp. PCC6803. !$#cross-references MUID:93099260; PMID:1463844 !$#accession S27972 !'##molecule_type DNA !'##residues 1-372 ##label ELL !'##cross-references EMBL:X62517; NID:g47554; PIDN:CAA44374.1; !1PID:g47555 !'##note the authors did not translate the codons for residues 342-361 REFERENCE S18046 !$#authors Ellersiek, U.; Steinmueller, K. !$#submission submitted to the EMBL Data Library, October 1991 !$#description Nucleotide sequence of the ndhA/I/G/E genes from !1Synechocystis sp. PCC 6803. !$#accession S18046 !'##molecule_type DNA !'##residues 1-367 ##label EL2 !'##cross-references EMBL:X62517 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76038 !'##status preliminary !'##molecule_type DNA !'##residues 1-372 ##label KAN !'##cross-references EMBL:D64006; GB:AB001339; NID:g1001291; !1PIDN:BAA10885.1; PID:g1001395 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene ndhA CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 1 KEYWORDS membrane-associated complex; NAD; oxidoreductase SUMMARY #length 372 #molecular-weight 40548 #checksum 6506 SEQUENCE /// ENTRY A30113 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) 24K chain precursor - human ORGANISM #formal_name Homo sapiens #common_name man DATE 14-May-1999 #sequence_revision 14-May-1999 #text_change 03-Jun-2002 ACCESSIONS A30113; B30863 REFERENCE A90542 !$#authors Pilkington, S.J.; Walker, J.E. !$#journal Biochemistry (1989) 28:3257-3264 !$#title Mitochondrial NADH-ubiquinone reductase: complementary DNA !1sequences of import precursors of the bovine and human !124-kDa subunit. !$#cross-references MUID:89302922; PMID:2500970 !$#accession A30113 !'##molecule_type mRNA !'##residues 1-249 ##label PIL !'##cross-references GB:M22538; NID:g986883; PIDN:AAA75390.1; !1PID:g188852; GB:M25484 GENETICS !$#gene GDB:NDUFV2 !'##cross-references GDB:383612; OMIM:600532 !$#map_position 18p11.31-18p11.2 COMPLEX heteromultimer of chains encoded by nuclear and !1mitochondrial genes FUNCTION !$#description the complex catalyzes the reduction of ubiquinone to !1ubiquinol by NADH, accompanied by proton translocation !1across the mitochondrial inner membrane CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) I chain E; NADH !1dehydrogenase (ubiquinone) I chain E homology KEYWORDS 2Fe-2S; iron-sulfur protein; metalloprotein; mitochondrial !1inner membrane; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase FEATURE !$1-32 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$33-249 #product NADH dehydrogenase (ubiquinone) 24K chain, !8mitochondrial #status predicted #label MAT\ !$67-208 #domain NADH dehydrogenase (ubiquinone) I chain E !8homology #label NUOE\ !$135,140,176,180 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 249 #molecular-weight 27363 #checksum 9676 SEQUENCE /// ENTRY B30113 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) 24K chain precursor - bovine ALTERNATE_NAMES NADH2 dehydrogenase chain II CONTAINS NADH2 dehydrogenase (EC 1.6.99.3) 24K chain ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 14-May-1999 #sequence_revision 14-May-1999 #text_change 19-Jul-2002 ACCESSIONS B30113; A30863; S06180; A05099 REFERENCE A90542 !$#authors Pilkington, S.J.; Walker, J.E. !$#journal Biochemistry (1989) 28:3257-3264 !$#title Mitochondrial NADH-ubiquinone reductase: complementary DNA !1sequences of import precursors of the bovine and human !124-kDa subunit. !$#cross-references MUID:89302922; PMID:2500970 !$#accession B30113 !'##molecule_type mRNA !'##residues 1-249 ##label WA1 !'##cross-references GB:M22539; GB:M25485; NID:g986869; PIDN:AAA87358.1; !1PID:g163399 REFERENCE A30863 !$#authors Pilkington, S.J.; Walker, J.E. !$#submission submitted to GenBank, February 1989 !$#accession A30863 !'##molecule_type mRNA !'##residues 1-249 ##label WA2 REFERENCE S06180 !$#authors Chomyn, A.; Tsai Lai, S.S.A. !$#journal Curr. Genet. (1989) 16:117-125 !$#title cDNA of the 24 kDa subunit of the bovine respiratory chain !1NADH dehydrogenase: high sequence conservation in mammals !1and tissue-specific and growth-dependent expression. !$#cross-references MUID:90090682; PMID:2598272 !$#accession S06180 !'##molecule_type mRNA !'##residues 38-249 ##label CHO !'##cross-references GB:X14724; NID:g1840; PIDN:CAA32848.1; PID:g1364245 REFERENCE A05099 !$#authors von Bahr-Lindstrom, H.; Galante, Y.M.; Persson, M.; !1Jornvall, H. !$#journal Eur. J. Biochem. (1983) 134:145-150 !$#title The primary structure of subunit II of NADH dehydrogenase !1from bovine-heart mitochondria. !$#cross-references MUID:83234474; PMID:6861757 !$#accession A05099 !'##molecule_type protein !'##residues 33-88,'SS',91,'TSYPDVLKBZZZPPGGAAI',95,'LW',98-249 ##label !1VON !'##experimental_source heart mitochondria !'##note tentative sequence COMMENT This NADH dehydrogenase, also called complex I of the !1respiratory chain, consists of at least 26 different !1polypeptide chains. It binds FMN and six or seven different !1iron-sulfur clusters. COMPLEX heteromultimer of chains encoded by nuclear and !1mitochondrial genes FUNCTION !$#description the complex catalyzes the reduction of ubiquinone to !1ubiquinol by NADH, accompanied by proton translocation !1across the mitochondrial inner membrane CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) I chain E; NADH !1dehydrogenase (ubiquinone) I chain E homology KEYWORDS 2Fe-2S; iron-sulfur protein; metalloprotein; mitochondrial !1inner membrane; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase FEATURE !$1-32 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$33-249 #product NADH dehydrogenase (ubiquinone) 24K chain, !8mitochondrial #status experimental #label MAT\ !$67-208 #domain NADH dehydrogenase (ubiquinone) I chain E !8homology #label NUOE\ !$135,140,176,180 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 249 #molecular-weight 27307 #checksum 9097 SEQUENCE /// ENTRY A31868 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) 24K chain precursor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 14-May-1999 #sequence_revision 14-May-1999 #text_change 03-Jun-2002 ACCESSIONS A31868 REFERENCE A31868 !$#authors Nishikimi, M.; Hosokawa, Y.; Toda, H.; Suzuki, H.; Ozawa, T. !$#journal Biochem. Biophys. Res. Commun. (1988) 157:914-920 !$#title The amino acid sequence of the 24-kDa subunit, an !1iron-sulfur protein, of rat liver mitochondrial NADH !1dehydrogenase deduced from cDNA sequence. !$#cross-references MUID:89087482; PMID:2974699 !$#accession A31868 !'##molecule_type mRNA !'##residues 1-241 ##label NIS !'##cross-references GB:M22756; NID:g205627; PIDN:AAA41669.1; !1PID:g205628 !'##note the authors translated the codon CCA for residue 238 as Gln COMPLEX heteromultimer of chains encoded by nuclear and !1mitochondrial genes FUNCTION !$#description the complex catalyzes the reduction of ubiquinone to !1ubiquinol by NADH, accompanied by proton translocation !1across the mitochondrial inner membrane CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) I chain E; NADH !1dehydrogenase (ubiquinone) I chain E homology KEYWORDS 2Fe-2S; iron-sulfur protein; metalloprotein; mitochondrial !1inner membrane; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase FEATURE !$1-24 #domain transit peptide (mitochondrion) (fragment) !8#status predicted #label TRP\ !$25-241 #product NADH dehydrogenase (ubiquinone) #status !8predicted #label MAT\ !$59-200 #domain NADH dehydrogenase (ubiquinone) I chain E !8homology #label NUOE\ !$127,132,168,172 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 241 #molecular-weight 26528 #checksum 9914 SEQUENCE /// ENTRY T01091 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) 24K chain homolog - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 14-May-1999 #sequence_revision 14-May-1999 #text_change 03-Jun-2002 ACCESSIONS T01091 REFERENCE Z14248 !$#authors Kaplan, N.; Johnson, D.; Schutz, K.; Gnoj, L.; Hoffman, J.; !1Till, S.; de la Bastide, M.; Granat, S.; Hameed, A.; !1Gottesman, T.; Hasegawa, A.; Shohdy, N.; Parnell, L.; !1Dedhia, N.; Johnson, A.F.; Lodhi, M.; Martienssen, R.; Chen, !1E.Y.; Wilson, R.; McCombie, W.R. !$#submission submitted to the EMBL Data Library, November 1998 !$#description Sequence of A. thaliana BAC T10P11 from chromosome IV. !$#accession T01091 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-244 ##label KAP !'##cross-references EMBL:AC002330; NID:g2262135; PIDN:AAC78260.1; !1PID:g3892051 GENETICS !$#map_position IV !$#introns 23/3; 45/3; 84/3; 110/3; 146/1; 161/3; 187/3; 209/3 !$#note T10P11.14 COMPLEX heteromultimer of chains encoded by nuclear and !1mitochondrial genes FUNCTION !$#description the complex catalyzes the reduction of ubiquinone to !1ubiquinol by NADH, accompanied by proton translocation !1across the mitochondrial inner membrane CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) I chain E; NADH !1dehydrogenase (ubiquinone) I chain E homology KEYWORDS 2Fe-2S; iron-sulfur protein; metalloprotein; NAD; oxidative !1phosphorylation; oxidoreductase FEATURE !$50-190 #domain NADH dehydrogenase (ubiquinone) I chain E !8homology #label NUOE\ !$119,124,160,164 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 244 #molecular-weight 27182 #checksum 6998 SEQUENCE /// ENTRY A40296 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) 25K chain - Paracoccus denitrificans ORGANISM #formal_name Paracoccus denitrificans DATE 14-May-1999 #sequence_revision 14-May-1999 #text_change 03-Jun-2002 ACCESSIONS A40296; G42573 REFERENCE A40296 !$#authors Xu, X.; Matsuno-Yagi, A.; Yagi, T. !$#journal Biochemistry (1991) 30:8678-8684 !$#title Characterization of the 25-kilodalton subunit of the !1energy-transducing NADH-ubiquinone oxidoreductase of !1Paracoccus denitrificans: sequence similarity to the !124-kilodalton subunit of the flavoprotein fraction of !1mammalian complex I. !$#cross-references MUID:91363357; PMID:1909571 !$#accession A40296 !'##molecule_type DNA !'##residues 1-239 ##label XUA !'##cross-references GB:M74171; GB:J05337; NID:g150602; PIDN:AAA25588.1; !1PID:g150603 !'##note part of this sequence, including the amino end of the mature !1protein, was determined by protein sequencing REFERENCE A42573 !$#authors Xu, X.; Matsuno-Yagi, A.; Yagi, T. !$#journal Biochemistry (1992) 31:6925-6932 !$#title Gene cluster of the energy-transducing NADH-quinone !1oxidoreductase of Paracoccus denitrificans: characterization !1of four structural gene products. !$#cross-references MUID:92345253; PMID:1637825 !$#accession G42573 !'##molecule_type DNA !'##residues 1-16 ##label XU1 !'##experimental_source ATCC 13543 !'##note sequence extracted from NCBI backbone (NCBIN:110121, !1NCBIP:110128) REFERENCE A57971 !$#authors Yano, T.; Sled, V.D.; Ohnishi, T.; Yagi, T. !$#journal FEBS Lett. (1994) 354:160-164 !$#title Identification of amino acid residues associated with the !1[2Fe-2S] cluster of the 25 kDa (NQO2) subunit of the !1proton-translocating NADH-quinone oxidoreductase of !1Paracoccus denitrificans. !$#cross-references MUID:95046324; PMID:7957917 !$#contents annotation; identification of iron-sulfur cluster ligands GENETICS !$#gene NQO2 FUNCTION !$#description the complex catalyzes the reduction of ubiquinone to !1ubiquinol by NADH CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) I chain E; NADH !1dehydrogenase (ubiquinone) I chain E homology KEYWORDS 2Fe-2S; iron-sulfur protein; metalloprotein; NAD; oxidative !1phosphorylation; oxidoreductase FEATURE !$1-239 #product NADH dehydrogenase (ubiquinone) 25K chain !8#status predicted #label MAT\ !$27-169 #domain NADH dehydrogenase (ubiquinone) I chain E !8homology #label NUOE\ !$96,101,137,141 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8experimental SUMMARY #length 239 #molecular-weight 26122 #checksum 723 SEQUENCE /// ENTRY C71692 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) I chain E RP353 - Rickettsia prowazekii ORGANISM #formal_name Rickettsia prowazekii DATE 14-May-1999 #sequence_revision 14-May-1999 #text_change 03-Jun-2002 ACCESSIONS C71692 REFERENCE A71630 !$#authors Andersson, S.G.E.; Zomorodipour, A.; Andersson, J.O.; !1Sicheritz-Ponten, T.; Alsmark, U.C.M.; Podowski, R.M.; !1Naeslund, A.K.; Eriksson, A.S.; Winkler, H.H.; Kurland, C.G. !$#journal Nature (1998) 396:133-140 !$#title The genome sequence of Rickettsia prowazekii and the origin !1of mitochondria. !$#cross-references MUID:99039499; PMID:9823893 !$#accession C71692 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-177 ##label AND !'##cross-references GB:AJ235271; GB:AJ235269; NID:g3868717; !1PIDN:CAA14813.1; PID:g3860913; GSPDB:GN00081 !'##experimental_source strain Madrid E GENETICS !$#gene nuoE; RP353 FUNCTION !$#description the complex catalyzes the reduction of ubiquinone to !1ubiquinol by NADH CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) I chain E; NADH !1dehydrogenase (ubiquinone) I chain E homology KEYWORDS 2Fe-2S; iron-sulfur protein; metalloprotein; NAD; oxidative !1phosphorylation; oxidoreductase FEATURE !$24-166 #domain NADH dehydrogenase (ubiquinone) I chain E !8homology #label NUOE\ !$93,98,134,138 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 177 #molecular-weight 20462 #checksum 6967 SEQUENCE /// ENTRY C65000 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) I chain E - Escherichia coli (strain K-12) ALTERNATE_NAMES complex 1 dehydrogenase, chain E; NADH dehydrogenase I, chain E; type 1 dehydrogenase, chain E; ubiquinone reductase, chain K ORGANISM #formal_name Escherichia coli DATE 14-May-1999 #sequence_revision 14-May-1999 #text_change 03-Jun-2002 ACCESSIONS C65000; S38314; S65636; S37062 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65000 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-166 ##label BLAT !'##cross-references GB:AE000317; GB:U00096; NID:g1788605; !1PIDN:AAC75345.1; PID:g1788621; UWGP:b2285 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S38310 !$#authors Weidner, U.; Geier, S.; Ptock, A.; Friedrich, T.; Leif, H.; !1Weiss, H. !$#journal J. Mol. Biol. (1993) 233:109-122 !$#title The gene locus of the proton-translocating NADH:ubiquinone !1oxidoreductase in Escherichia coli. Organization of the 14 !1genes and relationship between the derived proteins and !1subunits of mitochondrial complex I. !$#cross-references MUID:93389724; PMID:7690854 !$#accession S38314 !'##status preliminary !'##molecule_type DNA !'##residues 1-21,'V',23-166 ##label WEI !'##cross-references EMBL:X68301; NID:g444012; PIDN:CAA48364.1; !1PID:g397902 !'##experimental_source strain AN387 REFERENCE S65633 !$#authors Leif, H.; Sled, V.D.; Ohnishi, T.; Weiss, H.; Friedrich, T. !$#journal Eur. J. Biochem. (1995) 230:538-548 !$#title Isolation and characterization of the proton-translocating !1NADH:ubiquinone oxidoreductase from Escherichia coli. !$#cross-references MUID:95331291; PMID:7607227 !$#accession S65636 !'##molecule_type protein !'##residues 1-5 ##label LEI GENETICS !$#gene nuoE !$#map_position 49 min FUNCTION !$#description the complex catalyzes the reduction of ubiquinone to !1ubiquinol by NADH CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) I chain E; NADH !1dehydrogenase (ubiquinone) I chain E homology KEYWORDS 2Fe-2S; iron-sulfur protein; metalloprotein; NAD; oxidative !1phosphorylation; oxidoreductase FEATURE !$26-165 #domain NADH dehydrogenase (ubiquinone) I chain E !8homology #label NUOE\ !$92,97,133,137 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 166 #molecular-weight 18590 #checksum 1682 SEQUENCE /// ENTRY F70351 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) I chain nuoE - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 14-May-1999 #sequence_revision 14-May-1999 #text_change 03-Jun-2002 ACCESSIONS F70351 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession F70351 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-160 ##label AQF !'##cross-references GB:AE000696; NID:g2983196; PIDN:AAC06799.1; !1PID:g2983200; GB:AE000657 !'##experimental_source strain VF5 GENETICS !$#gene nuoE FUNCTION !$#description the complex catalyzes the reduction of ubiquinone to !1ubiquinol by NADH CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) I chain E; NADH !1dehydrogenase (ubiquinone) I chain E homology KEYWORDS 2Fe-2S; iron-sulfur protein; metalloprotein; NAD; oxidative !1phosphorylation; oxidoreductase FEATURE !$20-159 #domain NADH dehydrogenase (ubiquinone) I chain E !8homology #label NUOE\ !$86,91,127,131 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 160 #molecular-weight 18550 #checksum 3195 SEQUENCE /// ENTRY E69073 #type complete TITLE NADP-reducing hydrogenase (EC 1.-.-.-) chain A - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 14-May-1999 #sequence_revision 14-May-1999 #text_change 20-Oct-2000 ACCESSIONS E69073 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession E69073 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-149 ##label MTH !'##cross-references GB:AE000915; GB:AE000666; NID:g2622664; !1PIDN:AAB86022.1; PID:g2622669 !'##experimental_source strain Delta H GENETICS !$#gene MTH1548 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) I chain E; NADH !1dehydrogenase (ubiquinone) I chain E homology KEYWORDS 2Fe-2S; iron-sulfur protein; metalloprotein; NADP; !1oxidoreductase FEATURE !$9-148 #domain NADH dehydrogenase (ubiquinone) I chain E !8homology #label NUOE\ !$75,80,116,120 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 149 #molecular-weight 16433 #checksum 8486 SEQUENCE /// ENTRY A57150 #type complete TITLE NADP-reducing hydrogenase (EC 1.-.-.-) chain A - Desulfovibrio fructosovorans ORGANISM #formal_name Desulfovibrio fructosovorans DATE 14-May-1999 #sequence_revision 14-May-1999 #text_change 20-Oct-2000 ACCESSIONS A57150 REFERENCE A57150 !$#authors Malki, S.; Saimmaime, I.; De Luca, G.; Rousset, M.; Dermoun, !1Z.; Belaich, J.P. !$#journal J. Bacteriol. (1995) 177:2628-2636 !$#title Characterization of an operon encoding an NADP-reducing !1hydrogenase in Desulfovibrio fructosovorans. !$#cross-references MUID:95270577; PMID:7751270 !$#accession A57150 !'##status preliminary !'##molecule_type DNA !'##residues 1-171 ##label MAL !'##cross-references GB:U07229; NID:g466362; PIDN:AAA87054.1; !1PID:g466363 !'##note authors failed to translated the codon TGC for residue 6 as Cys GENETICS !$#gene hndA CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) I chain E; NADH !1dehydrogenase (ubiquinone) I chain E homology KEYWORDS 2Fe-2S; iron-sulfur protein; metalloprotein; NADP; !1oxidoreductase FEATURE !$32-171 #domain NADH dehydrogenase (ubiquinone) I chain E !8homology #label NUOE\ !$98,103,139,143 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 171 #molecular-weight 18807 #checksum 916 SEQUENCE /// ENTRY S75537 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) I chain E - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein sll1220 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 14-May-1999 #sequence_revision 14-May-1999 #text_change 03-Jun-2002 ACCESSIONS S75537 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75537 !'##status preliminary !'##molecule_type DNA !'##residues 1-173 ##label KAN !'##cross-references EMBL:D90911; GB:AB001339; NID:g1653083; !1PIDN:BAA18098.1; PID:g1653182 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 FUNCTION !$#description the complex catalyzes the reduction of ubiquinone to !1ubiquinol by NADH CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) I chain E; NADH !1dehydrogenase (ubiquinone) I chain E homology KEYWORDS 2Fe-2S; iron-sulfur protein; metalloprotein; NAD; oxidative !1phosphorylation; oxidoreductase FEATURE !$30-169 #domain NADH dehydrogenase (ubiquinone) I chain E !8homology #label NUOE\ !$96,101,137,141 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 173 #molecular-weight 18760 #checksum 2819 SEQUENCE /// ENTRY F70647 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) I chain E - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 14-May-1999 #sequence_revision 14-May-1999 #text_change 03-Jun-2002 ACCESSIONS F70647 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession F70647 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-252 ##label COL !'##cross-references GB:Z83867; GB:AL123456; NID:g3261695; !1PIDN:CAB06290.1; PID:g1781219 !'##experimental_source strain H37Rv GENETICS !$#gene nuoE FUNCTION !$#description the complex catalyzes the reduction of ubiquinone to !1ubiquinol by NADH CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) I chain E; NADH !1dehydrogenase (ubiquinone) I chain E homology KEYWORDS 2Fe-2S; iron-sulfur protein; metalloprotein; NAD; oxidative !1phosphorylation; oxidoreductase FEATURE !$48-187 #domain NADH dehydrogenase (ubiquinone) I chain E !8homology #label NUOE\ !$114,119,155,159 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 252 #molecular-weight 27197 #checksum 5855 SEQUENCE /// ENTRY JE0092 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) flavoprotein 1 precursor [validated] - human ALTERNATE_NAMES mitochondrial complex I 51K chain; NADH dehydrogenase (ubiquinone) 51K chain; NDUFV1 protein ORGANISM #formal_name Homo sapiens #common_name man DATE 14-May-1999 #sequence_revision 14-May-1999 #text_change 03-Jun-2002 ACCESSIONS JE0092; A44362; A48922 REFERENCE JE0092 !$#authors Schuelke, M.; Loeffen, J.; Mariman, E.; Smeitink, J.; van !1den Heuvel, L. !$#journal Biochem. Biophys. Res. Commun. (1998) 245:599-606 !$#title Cloning of the human mitochondrial 51 kDa subunit (NDUFV1) !1reveals a 100% antisense homology of its 3'UTR with 5'UTR of !1the gamma-interferon inducible protein (IP-30) precursor: Is !1this a link between mitochondrial myopathy and !1inflammation?. !$#cross-references MUID:98238687; PMID:9571201 !$#accession JE0092 !'##molecule_type mRNA !'##residues 1-464 ##label SCH !'##cross-references GB:AF053070 REFERENCE A44362 !$#authors Spencer, S.R.; Taylor, J.B.; Cowell, I.G.; Xia, C.L.; !1Pemble, S.E.; Ketterer, B. !$#journal Genomics (1992) 14:1116-1118 !$#title The human mitochondrial NADH: ubiquinone oxidoreductase !151-kDa subunit maps adjacent to the glutathione !1S-transferase P1-1 gene on chromosome 11q13. !$#cross-references MUID:93122785; PMID:1478657 !$#accession A44362 !'##status preliminary !'##molecule_type DNA !'##residues 1-79,'V',81-130 ##label SPE !'##cross-references GB:S52526; NID:g263363; PIDN:AAB24883.1; !1PID:g263364 !'##note sequence extracted from NCBI backbone (NCBIN:122417, !1NCBIN:122420, NCBIP:122421) REFERENCE A48922 !$#authors Ali, S.T.; Duncan, A.M.; Schappert, K.; Heng, H.H.; Tsui, !1L.C.; Chow, W.; Robinson, B.H. !$#journal Genomics (1993) 18:435-439 !$#title Chromosomal localization of the human gene encoding the !151-kDa subunit of mitochondrial complex I (NDUFV1) to 11q13. !$#cross-references MUID:94117021; PMID:8288251 !$#accession A48922 !'##molecule_type mRNA !'##residues 87-149,'A',151-305 ##label ALI !'##cross-references GB:S67973; NID:g461139; PIDN:AAB29698.1; !1PID:g461140 !'##experimental_source kidney !'##note sequence extracted from NCBI backbone (NCBIN:142158, !1NCBIP:142159) GENETICS !$#gene GDB:NDUFV1 !'##cross-references GDB:136409; OMIM:161015 !$#map_position 11q13-11q13 COMPLEX heteromultimer of chains encoded by nuclear and !1mitochondrial genes FUNCTION !$#description the complex catalyzes the reduction of ubiquinone to !1ubiquinol by NADH, accompanied by proton translocation !1across the mitochondrial inner membrane !$#pathway oxidative phosphorylation CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain F; NADH !1dehydrogenase (ubiquinone) I chain F homology KEYWORDS 4Fe-4S; flavoprotein; FMN; iron-sulfur protein; !1membrane-associated complex; metalloprotein; mitochondrial !1inner membrane; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase FEATURE !$1-20 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$21-464 #product NADH dehydrogenase (ubiquinone) 51K chain !8#status experimental #label MAT\ !$69-447 #domain NADH dehydrogenase (ubiquinone) I chain F !8homology #label NUOF\ !$87-96 #region NAD binding motif\ !$200-215 #region FMN binding motif\ !$379,382,385,425 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 464 #molecular-weight 50817 #checksum 5954 SEQUENCE /// ENTRY A39362 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) flavoprotein 1 precursor - bovine ALTERNATE_NAMES mitochondrial complex I 51K chain; NADH dehydrogenase (ubiquinone) 51K chain; NDUFV1 protein ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 14-May-1999 #sequence_revision 14-May-1999 #text_change 03-Jun-2002 ACCESSIONS A39362; A37941 REFERENCE A39362 !$#authors Patel, S.D.; Aebersold, R.; Attardi, G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:4225-4229 !$#title cDNA-derived amino acid sequence of the NADH-binding 51-kDa !1subunit of the bovine respiratory NADH dehydrogenase reveals !1striking similarities to a bacterial NAD(+)-reducing !1hydrogenase. !$#cross-references MUID:91239540; PMID:2034666 !$#accession A39362 !'##molecule_type mRNA !'##residues 1-464 ##label PAT !'##cross-references GB:M63009 !'##note parts of this sequence were confirmed by protein sequencing REFERENCE A37941 !$#authors Pilkington, S.J.; Skehel, J.M.; Gennis, R.B.; Walker, J.E. !$#journal Biochemistry (1991) 30:2166-2175 !$#title Relationship between mitochondrial NADH-ubiquinone reductase !1and a bacterial NAD-reducing hydrogenase. !$#cross-references MUID:91152030; PMID:1900194 !$#accession A37941 !'##molecule_type mRNA !'##residues 1-412,'C',414-464 ##label PIL !'##cross-references GB:M58607; GB:J05316; NID:g162863; PIDN:AAA30450.1; !1PID:g162864 !'##note parts of this sequence, including the amino end of the mature !1protein, were confirmed by protein sequencing COMPLEX heteromultimer of chains encoded by nuclear and !1mitochondrial genes FUNCTION !$#description the complex catalyzes the reduction of ubiquinone to !1ubiquinol by NADH, accompanied by proton translocation !1across the mitochondrial inner membrane !$#pathway oxidative phosphorylation CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain F; NADH !1dehydrogenase (ubiquinone) I chain F homology KEYWORDS 4Fe-4S; flavoprotein; FMN; iron-sulfur protein; !1membrane-associated complex; metalloprotein; mitochondrial !1inner membrane; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase FEATURE !$1-20 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$21-464 #product NADH dehydrogenase (ubiquinone) 51K chain !8#status predicted #label MAT\ !$69-447 #domain NADH dehydrogenase (ubiquinone) I chain F !8homology #label NUOF\ !$87-96 #region NAD binding motif\ !$200-215 #region FMN binding motif\ !$379,382,385,425 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 464 #molecular-weight 50651 #checksum 5483 SEQUENCE /// ENTRY S17663 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) flavoprotein 1 precursor - Neurospora crassa ALTERNATE_NAMES mitochondrial complex I 51K chain; NADH dehydrogenase (ubiquinone) 51K chain ORGANISM #formal_name Neurospora crassa DATE 14-May-1999 #sequence_revision 14-May-1999 #text_change 03-Jun-2002 ACCESSIONS S17663; S20223; S16743 REFERENCE S17663 !$#authors Preis, D.; Weidner, U.; Conzen, C.; Azevedo, J.E.; Nehls, !1U.; Roehlen, D.; van der Pas, J.; Sackmann, U.; Schneider, !1R.; Werner, S.; Weiss, H. !$#journal Biochim. Biophys. Acta (1991) 1090:133-138 !$#title Primary structures of two subunits of NADH:ubiquinone !1reductase from Neurospora crassa concerned with !1NADH-oxidation. Relationship to a soluble NAD-reducing !1hydrogenase of Alcaligenes eutrophus. !$#cross-references MUID:91355223; PMID:1832016 !$#accession S17663 !'##molecule_type mRNA !'##residues 1-493 ##label PRE !'##cross-references EMBL:X56227; NID:g3031; PIDN:CAA39676.1; PID:g3032 !$#accession S20223 !'##molecule_type protein !'##residues 28-38 ##label PRA2 COMPLEX heteromultimer of chains encoded by nuclear and !1mitochondrial genes FUNCTION !$#description the complex catalyzes the reduction of ubiquinone to !1ubiquinol by NADH, accompanied by proton translocation !1across the mitochondrial inner membrane !$#pathway oxidative phosphorylation CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain F; NADH !1dehydrogenase (ubiquinone) I chain F homology KEYWORDS 4Fe-4S; flavoprotein; FMN; iron-sulfur protein; !1membrane-associated complex; metalloprotein; mitochondrial !1inner membrane; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase FEATURE !$1-27 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$29-493 #product NADH dehydrogenase (ubiquinone) 51K chain !8#status experimental #label MAT\ !$78-459 #domain NADH dehydrogenase (ubiquinone) I chain F !8homology #label NUOF\ !$96-105 #region NAD binding motif\ !$212-227 #region FMN binding motif\ !$391,394,397,437 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 493 #molecular-weight 54326 #checksum 2896 SEQUENCE /// ENTRY S52261 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) flavoprotein 1 precursor - potato ALTERNATE_NAMES mitochondrial complex I 51K chain; NADH dehydrogenase (ubiquinone) 51K chain ORGANISM #formal_name Solanum tuberosum #common_name potato DATE 14-May-1999 #sequence_revision 14-May-1999 #text_change 03-Jun-2002 ACCESSIONS S52261 REFERENCE S52261 !$#authors Grohmann, L.; Thieck, O. !$#submission submitted to the EMBL Data Library, January 1995 !$#accession S52261 !'##molecule_type mRNA !'##residues 1-487 ##label GRO !'##cross-references EMBL:X83999; NID:g639833; PIDN:CAA58823.1; !1PID:g639834 FUNCTION !$#description catalyzes the reduction of ubiquinone to ubiquinol by NADH !$#pathway oxidative phosphorylation CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain F; NADH !1dehydrogenase (ubiquinone) I chain F homology KEYWORDS 4Fe-4S; flavoprotein; FMN; iron-sulfur protein; !1membrane-associated complex; metalloprotein; mitochondrial !1inner membrane; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase FEATURE !$92-470 #domain NADH dehydrogenase (ubiquinone) I chain F !8homology #label NUOF\ !$110-119 #region NAD binding motif\ !$223-238 #region FMN binding motif\ !$402,405,408,448 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 487 #molecular-weight 53618 #checksum 7949 SEQUENCE /// ENTRY A39588 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) I chain 1 - Paracoccus denitrificans ALTERNATE_NAMES NADH dehydrogenase (ubiquinone) 50K chain; NADH dehydrogenase (ubiquinone) NADH-binding chain NQO1 ORGANISM #formal_name Paracoccus denitrificans DATE 14-May-1999 #sequence_revision 14-May-1999 #text_change 03-Jun-2002 ACCESSIONS A39588; S23946; D40296 REFERENCE A39588 !$#authors Xu, X.; Matsuno-Yagi, A.; Yagi, T. !$#journal Biochemistry (1991) 30:6422-6428 !$#title The NADH-binding subunit of the energy-transducing !1NADH-ubiquinone oxidoreductase of Paracoccus denitrificans: !1gene cloning and deduced primary structure. !$#cross-references MUID:91274292; PMID:1905152 !$#accession A39588 !'##molecule_type DNA !'##residues 1-431 ##label XUA !'##cross-references GB:M64432; NID:g150597; PIDN:AAA25585.1; !1PID:g150598 !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing REFERENCE S23946 !$#authors Xu, X.; Matsuno-Yagi, A.; Yagi, T. !$#journal Arch. Biochem. Biophys. (1992) 296:40-48 !$#title Structural features of the 66-kDa subunit of the !1energy-transducing NADH-ubiquinone oxidoreductase (NDH-1) of !1Paracoccus denitrificans. !$#cross-references MUID:92296779; PMID:1605643 !$#accession S23946 !'##status preliminary !'##molecule_type DNA !'##residues 416-431 ##label XU2 REFERENCE A40296 !$#authors Xu, X.; Matsuno-Yagi, A.; Yagi, T. !$#journal Biochemistry (1991) 30:8678-8684 !$#title Characterization of the 25-kilodalton subunit of the !1energy-transducing NADH-ubiquinone oxidoreductase of !1Paracoccus denitrificans: sequence similarity to the !124-kilodalton subunit of the flavoprotein fraction of !1mammalian complex I. !$#cross-references MUID:91363357; PMID:1909571 !$#accession D40296 !'##molecule_type DNA !'##residues 1-8 ##label XU3 !'##cross-references GB:J05337 GENETICS !$#gene NQO1 COMPLEX heteromultimer containing about 10 types of chains FUNCTION !$#description catalyzes the reduction of ubiquinone to ubiquinol by NADH !$#pathway oxidative phosphorylation CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain F; NADH !1dehydrogenase (ubiquinone) I chain F homology KEYWORDS 4Fe-4S; flavoprotein; FMN; iron-sulfur protein; !1metalloprotein; NAD; oxidative phosphorylation; !1oxidoreductase FEATURE !$36-414 #domain NADH dehydrogenase (ubiquinone) I chain F !8homology #label NUOF\ !$54-63 #region NAD binding motif\ !$167-182 #region FMN binding motif\ !$346,349,352,392 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 431 #molecular-weight 47191 #checksum 5247 SEQUENCE /// ENTRY A71721 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) I chain F RP115 - Rickettsia prowazekii ORGANISM #formal_name Rickettsia prowazekii DATE 14-May-1999 #sequence_revision 14-May-1999 #text_change 03-Jun-2002 ACCESSIONS A71721 REFERENCE A71630 !$#authors Andersson, S.G.E.; Zomorodipour, A.; Andersson, J.O.; !1Sicheritz-Ponten, T.; Alsmark, U.C.M.; Podowski, R.M.; !1Naeslund, A.K.; Eriksson, A.S.; Winkler, H.H.; Kurland, C.G. !$#journal Nature (1998) 396:133-140 !$#title The genome sequence of Rickettsia prowazekii and the origin !1of mitochondria. !$#cross-references MUID:99039499; PMID:9823893 !$#accession A71721 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-421 ##label AND !'##cross-references GB:AJ235270; GB:AJ235269; NID:g3860572; !1PIDN:CAA14584.1; PID:g3860683; GSPDB:GN00081 !'##experimental_source strain Madrid E GENETICS !$#gene nuoF; RP115 FUNCTION !$#description catalyzes the reduction of ubiquinone to ubiquinol by NADH !$#pathway oxidative phosphorylation CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain F; NADH !1dehydrogenase (ubiquinone) I chain F homology KEYWORDS 4Fe-4S; flavoprotein; FMN; iron-sulfur protein; !1metalloprotein; NAD; oxidative phosphorylation; !1oxidoreductase FEATURE !$36-412 #domain NADH dehydrogenase (ubiquinone) I chain F !8homology #label NUOF\ !$54-63 #region NAD binding motif\ !$166-181 #region FMN binding motif\ !$344,347,350,390 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 421 #molecular-weight 46291 #checksum 8968 SEQUENCE /// ENTRY G70647 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) I chain F - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 14-May-1999 #sequence_revision 14-May-1999 #text_change 03-Jun-2002 ACCESSIONS G70647 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession G70647 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-445 ##label COL !'##cross-references GB:Z83867; GB:AL123456; NID:g3261695; !1PIDN:CAB06289.1; PID:g1781218 !'##experimental_source strain H37Rv GENETICS !$#gene nuoF FUNCTION !$#description catalyzes the reduction of ubiquinone to ubiquinol by NADH !$#pathway oxidative phosphorylation CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain F; NADH !1dehydrogenase (ubiquinone) I chain F homology KEYWORDS 4Fe-4S; flavoprotein; FMN; iron-sulfur protein; !1metalloprotein; NAD; oxidative phosphorylation; !1oxidoreductase FEATURE !$43-421 #domain NADH dehydrogenase (ubiquinone) I chain F !8homology #label NUOF\ !$61-70 #region NAD binding motif\ !$177-192 #region FMN binding motif\ !$353,356,359,399 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 445 #molecular-weight 48101 #checksum 8666 SEQUENCE /// ENTRY B65000 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) I chain F - Escherichia coli (strain K-12) ALTERNATE_NAMES NADH dehydrogenase (ubiquinone) I NADH-binding chain ORGANISM #formal_name Escherichia coli DATE 14-May-1999 #sequence_revision 14-May-1999 #text_change 03-Jun-2002 ACCESSIONS B65000; S38315; S65637; B48643; S37063 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65000 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-445 ##label BLAT !'##cross-references GB:AE000317; GB:U00096; NID:g1788605; !1PIDN:AAC75344.1; PID:g1788620; UWGP:b2284 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S38310 !$#authors Weidner, U.; Geier, S.; Ptock, A.; Friedrich, T.; Leif, H.; !1Weiss, H. !$#journal J. Mol. Biol. (1993) 233:109-122 !$#title The gene locus of the proton-translocating NADH:ubiquinone !1oxidoreductase in Escherichia coli. Organization of the 14 !1genes and relationship between the derived proteins and !1subunits of mitochondrial complex I. !$#cross-references MUID:93389724; PMID:7690854 !$#accession S38315 !'##molecule_type DNA !'##residues 1-25,'R',27-40,'R',42-369,'R',371-445 ##label WEI !'##cross-references EMBL:X68301; NID:g444012; PIDN:CAA48365.1; !1PID:g397903 !'##experimental_source strain AN387 REFERENCE S65633 !$#authors Leif, H.; Sled, V.D.; Ohnishi, T.; Weiss, H.; Friedrich, T. !$#journal Eur. J. Biochem. (1995) 230:538-548 !$#title Isolation and characterization of the proton-translocating !1NADH:ubiquinone oxidoreductase from Escherichia coli. !$#cross-references MUID:95331291; PMID:7607227 !$#accession S65637 !'##status preliminary !'##molecule_type protein !'##residues 1-9 ##label LEI REFERENCE A48643 !$#authors Zambrano, M.M.; Kolter, R. !$#journal J. Bacteriol. (1993) 175:5642-5647 !$#title Escherichia coli mutants lacking NADH dehydrogenase I have a !1competitive disadvantage in stationary phase. !$#cross-references MUID:93374861; PMID:8366049 !$#accession B48643 !'##status preliminary !'##molecule_type DNA !'##residues 25-37,'R',39-50,'I',52-114 ##label ZAM !'##cross-references GB:L19569 GENETICS !$#gene nuoF FUNCTION !$#description catalyzes the reduction of ubiquinone to ubiquinol by NADH !$#pathway oxidative phosphorylation CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain F; NADH !1dehydrogenase (ubiquinone) I chain F homology KEYWORDS 4Fe-4S; flavoprotein; FMN; iron-sulfur protein; !1metalloprotein; NAD; oxidative phosphorylation; !1oxidoreductase FEATURE !$43-420 #domain NADH dehydrogenase (ubiquinone) I chain F !8homology #label NUOF\ !$61-70 #region NAD binding motif\ !$174-189 #region FMN binding motif\ !$351,354,357,398 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 445 #molecular-weight 49292 #checksum 4598 SEQUENCE /// ENTRY E70351 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) I chain nuoF - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 14-May-1999 #sequence_revision 14-May-1999 #text_change 03-Jun-2002 ACCESSIONS E70351 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession E70351 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-426 ##label AQF !'##cross-references GB:AE000696; NID:g2983196; PIDN:AAC06800.1; !1PID:g2983201; GB:AE000657 !'##experimental_source strain VF5 GENETICS !$#gene nuoF FUNCTION !$#description catalyzes the reduction of ubiquinone to ubiquinol by NADH !$#pathway oxidative phosphorylation CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain F; NADH !1dehydrogenase (ubiquinone) I chain F homology KEYWORDS 4Fe-4S; flavoprotein; FMN; iron-sulfur protein; !1metalloprotein; NAD; oxidative phosphorylation; !1oxidoreductase FEATURE !$47-415 #domain NADH dehydrogenase (ubiquinone) I chain F !8homology #label NUOF\ !$65-74 #region NAD binding motif\ !$176-191 #region FMN binding motif\ !$347,350,353,393 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 426 #molecular-weight 47508 #checksum 2903 SEQUENCE /// ENTRY S75536 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) I chain F homolog - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein sll1221 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 14-May-1999 #sequence_revision 14-May-1999 #text_change 03-Jun-2002 ACCESSIONS S75536 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75536 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-533 ##label KAN !'##cross-references EMBL:D90911; GB:AB001339; NID:g1653083; !1PIDN:BAA18097.1; PID:g1653181 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene hoxF CLASSIFICATION #superfamily Synechocystis NADH dehydrogenase (ubiquinone) !1chain F homolog; NADH dehydrogenase (ubiquinone) I chain F !1homology KEYWORDS 4Fe-4S; flavoprotein; FMN; iron-sulfur protein; !1metalloprotein; NAD; oxidoreductase FEATURE !$1-104 #region Desulfovibrio NADP-reducing hydrogenase chain !8B similarity\ !$153-528 #domain NADH dehydrogenase (ubiquinone) I chain F !8homology #label NUOF\ !$171-180 #region NAD binding motif\ !$283-298 #region FMN binding motif\ !$460,463,466,506 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 533 #molecular-weight 57774 #checksum 2646 SEQUENCE /// ENTRY I39730 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) I chain F homolog - Anabaena variabilis ALTERNATE_NAMES bidirectional NAD(P)-dependent hydrogenase ORGANISM #formal_name Anabaena variabilis DATE 14-May-1999 #sequence_revision 14-May-1999 #text_change 03-Jun-2002 ACCESSIONS S68182; I39730 REFERENCE I39730 !$#authors Schmitz, O.; Boison, G.; Hilscher, R.; Hundeshagen, B.; !1Zimmer, W.; Lottspeich, F.; Bothe, H. !$#journal Eur. J. Biochem. (1995) 233:266-276 !$#title Molecular biological analysis of a bidirectional hydrogenase !1from cyanobacteria. !$#cross-references MUID:96061958; PMID:7588754 !$#accession S68182 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-535 ##label SCH !'##cross-references EMBL:X79285; NID:g1032475; PIDN:CAA55873.1; !1PID:g1032476 !'##experimental_source ATCC 29413 GENETICS !$#gene hoxF CLASSIFICATION #superfamily Synechocystis NADH dehydrogenase (ubiquinone) !1chain F homolog; NADH dehydrogenase (ubiquinone) I chain F !1homology KEYWORDS 4Fe-4S; flavoprotein; FMN; iron-sulfur protein; !1metalloprotein; NAD; oxidoreductase FEATURE !$1-108 #region Desulfovibrio NADP-reducing hydrogenase chain !8B similarity\ !$155-530 #domain NADH dehydrogenase (ubiquinone) I chain F !8homology #label NUOF\ !$173-182 #region NAD binding motif\ !$285-300 #region FMN binding motif\ !$25,30,62,66 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$462,465,468,508 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 535 #molecular-weight 57294 #checksum 5221 SEQUENCE /// ENTRY C57150 #type complete TITLE NADP-reducing hydrogenase (EC 1.-.-.-) chain C - Desulfovibrio fructosovorans ORGANISM #formal_name Desulfovibrio fructosovorans DATE 14-May-1999 #sequence_revision 14-May-1999 #text_change 11-Jun-1999 ACCESSIONS C57150 REFERENCE A57150 !$#authors Malki, S.; Saimmaime, I.; De Luca, G.; Rousset, M.; Dermoun, !1Z.; Belaich, J.P. !$#journal J. Bacteriol. (1995) 177:2628-2636 !$#title Characterization of an operon encoding an NADP-reducing !1hydrogenase in Desulfovibrio fructosovorans. !$#cross-references MUID:95270577; PMID:7751270 !$#accession C57150 !'##molecule_type DNA !'##residues 1-490 ##label MAL !'##cross-references GB:U07229; NID:g466362; PIDN:AAA87056.1; !1PID:g466365 GENETICS !$#gene hndC CLASSIFICATION #superfamily Desulfovibrio NADP-reducing hydrogenase chain !1C; ferredoxin 2[4Fe-4S] homology; NADH dehydrogenase !1(ubiquinone) I chain F homology KEYWORDS 4Fe-4S; flavoprotein; FMN; iron-sulfur protein; !1metalloprotein; NAD; oxidoreductase FEATURE !$42-416 #domain NADH dehydrogenase (ubiquinone) I chain F !8homology #label NUOF\ !$60-69 #region NAD binding motif\ !$171-186 #region FMN binding motif\ !$435-490 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$348,351,354,394 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$442,445,448,482 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$452,472,475,478 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 490 #molecular-weight 52585 #checksum 4458 SEQUENCE /// ENTRY F69073 #type complete TITLE NADP-reducing hydrogenase (EC 1.-.-.-) chain B/C - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 14-May-1999 #sequence_revision 14-May-1999 #text_change 31-Mar-2000 ACCESSIONS F69073 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession F69073 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-630 ##label MTH !'##cross-references GB:AE000915; GB:AE000666; NID:g2622664; !1PIDN:AAB86023.1; PID:g2622670 !'##experimental_source strain Delta H COMMENT This gene is identified by similarity with two adjacent !1genes of the hnd operon in Desulfovibrio fructosovorans (see !1PIR:B57150 and PIR:C57150). GENETICS !$#gene MTH1549 CLASSIFICATION #superfamily NADP-reducing hydrogenase chain B/C homolog; !1ferredoxin 2[4Fe-4S] homology; NADH dehydrogenase !1(ubiquinone) I chain F homology KEYWORDS 4Fe-4S; flavoprotein; FMN; iron-sulfur protein; !1metalloprotein; NAD; oxidoreductase FEATURE !$1-116 #region Desulfovibrio NADP-reducing hydrogenase chain !8B similarity\ !$164-538 #domain NADH dehydrogenase (ubiquinone) I chain F !8homology #label NUOF\ !$182-191 #region NAD binding motif\ !$294-309 #region FMN binding motif\ !$556-611 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$470,473,476,516 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$563,566,569,603 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$573,593,596,599 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 630 #molecular-weight 68594 #checksum 2354 SEQUENCE /// ENTRY A32667 #type complete TITLE NAD(P)H2 dehydrogenase (quinone) (EC 1.6.99.2) 2 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS A32667; A54055 REFERENCE A32667 !$#authors Jaiswal, A.K.; Burnett, P.; Adesnik, M.; McBride, O.W. !$#journal Biochemistry (1990) 29:1899-1906 !$#title Nucleotide and deduced amino acid sequence of a human cDNA !1(NQO-2) corresponding to a second member of the NAD !1(P)H:quinone oxidoreductase gene family. Extensive !1polymorphism at the NQO-2 gene locus on chromosome 6. !$#cross-references MUID:90234709; PMID:1691923 !$#accession A32667 !'##molecule_type mRNA !'##residues 1-231 ##label JAI !'##cross-references GB:J02888; NID:g190817; PIDN:AAA60239.1; !1PID:g190818 REFERENCE A54055 !$#authors Jaiswal, A.K. !$#journal J. Biol. Chem. (1994) 269:14502-14508 !$#title Human NAD(P)H:quinone oxidoreductase-2. Gene structure, !1activity, and tissue-specific expression. !$#cross-references MUID:94237859; PMID:8182056 !$#accession A54055 !'##molecule_type DNA !'##residues 1-139,'C',141-231 ##label JA2 !'##cross-references GB:U07729 !'##note authors translated the codon TGT for residue 140 as Gly GENETICS !$#gene GDB:NMOR2 !'##cross-references GDB:128074; OMIM:160998 !$#map_position 6pter-6q12 CLASSIFICATION #superfamily NAD(P)H dehydrogenase (quinone) 2 KEYWORDS flavoprotein; NAD; oxidoreductase SUMMARY #length 231 #molecular-weight 25952 #checksum 6341 SEQUENCE /// ENTRY I52851 #type complete TITLE NAD(P)H2 dehydrogenase (quinone) (EC 1.6.99.2) 1 [similarity] - mouse ALTERNATE_NAMES NAD(P)H oxidoreductase ORGANISM #formal_name Mus musculus #common_name house mouse DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 03-Jun-2002 ACCESSIONS I52851 REFERENCE I52851 !$#authors Robertson, J.A.; Nebert, D.W. !$#journal Chem. Scr. (1987) 27:83-87 !$#title Autoregulation plus positive and negative elements !1controlling transcription of genes in the [Ah] battery. !$#accession I52851 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-274 ##label RES !'##cross-references GB:M36660; NID:g200083; PIDN:AAA39829.1; !1PID:g200084 CLASSIFICATION #superfamily NAD(P)H dehydrogenase (quinone) 2 KEYWORDS NAD; oxidoreductase SUMMARY #length 274 #molecular-weight 30946 #checksum 8851 SEQUENCE /// ENTRY A34162 #type complete TITLE NAD(P)H2 dehydrogenase (quinone) (EC 1.6.99.2) - rat ALTERNATE_NAMES DT-diaphorase; menadione reductase; NAD(P)H-menadione oxidoreductase; phylloquinone reductase; quinone reductase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS A34162; A26140; A35607; A24607; A37380; A28950; A60561; !1A60821; S13883; I52085 REFERENCE A34162 !$#authors Bayney, R.M.; Morton, M.R.; Favreau, L.V.; Pickett, C.B. !$#journal J. Biol. Chem. (1989) 264:21793-21797 !$#title Rat liver NAD(P)H:quinone reductase. Regulation of quinone !1reductase gene expression by planar aromatic compounds and !1determination of the exon structure of the quinone reductase !1structural gene. !$#cross-references MUID:90094356; PMID:2480957 !$#accession A34162 !'##molecule_type DNA !'##residues 1-274 ##label BAY !'##cross-references GB:M31801; GB:M31802; GB:M31803; GB:M31804; !1GB:M31805; NID:g206520; PIDN:AAA41989.1; PID:g206522 REFERENCE A26140 !$#authors Bayney, R.M.; Rodkey, J.A.; Bennett, C.D.; Lu, A.Y.H.; !1Pickett, C.B. !$#journal J. Biol. Chem. (1987) 262:572-575 !$#title Rat liver NAD(P)H:quinone reductase nucleotide sequence !1analysis of a quinone reductase cDNA clone and prediction of !1the amino acid sequence of the corresponding protein. !$#cross-references MUID:87109147; PMID:3100515 !$#accession A26140 !'##molecule_type mRNA !'##residues 22-134,'Q',136-274 ##label BA2 !'##cross-references GB:J02640; NID:g206514; PIDN:AAA41988.1; !1PID:g206515 REFERENCE A35607 !$#authors Forrest, G.L.; Qian, J.; Ma, J.X.; Kaplan, W.D.; Akman, S.; !1Doroshow, J.; Chen, S. !$#journal Biochem. Biophys. Res. Commun. (1990) 169:1087-1093 !$#title Rat liver NAD(P)H:quinone oxidoreductase: cDNA expression !1and site-directed mutagenesis. !$#cross-references MUID:90303294; PMID:2141979 !$#accession A35607 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type mRNA !'##residues 2-274 ##label FOR REFERENCE A24607 !$#authors Robertson, J.A.; Chen, H.C.; Nebert, D.W. !$#journal J. Biol. Chem. (1986) 261:15794-15799 !$#title NAD(P)H:Menadione oxidoreductase. Novel purification of !1enzyme, cDNA and complete amino acid sequence, and gene !1regulation. !$#cross-references MUID:87057224; PMID:3536915 !$#accession A24607 !'##molecule_type mRNA !'##residues 1-274 ##label ROB !'##cross-references GB:J02608; NID:g205743; PIDN:AAA41716.1; !1PID:g205744 REFERENCE A37380 !$#authors Dear, T.N.; McDonald, D.A.; Kefford, R.F. !$#journal Cancer Res. (1989) 49:5323-5328 !$#title Transcriptional down-regulation of a rat gene, WDNM2, in !1metastatic DMBA-8 cells. !$#cross-references MUID:89354323; PMID:2504488 !$#accession A37380 !'##molecule_type mRNA !'##residues 'G',81-274 ##label DEA !'##cross-references GB:X17464 REFERENCE A28950 !$#authors Haniu, M.; Yuan, H.; Chen, S.; Iyanagi, T.; Lee, T.D.; !1Shively, J.E. !$#journal Biochemistry (1988) 27:6877-6883 !$#title Structure-function relationship of NAD(P)H:quinone !1reductase: characterization of NH2-terminal blocking group !1and essential tyrosine and lysine residues. !$#cross-references MUID:89062419; PMID:3143406 !$#accession A28950 !'##molecule_type protein !'##residues 2-274 ##label HAN REFERENCE A60561 !$#authors Liu, X.F.; Yuan, H.; Haniu, M.; Iyanagi, T.; Shively, J.E.; !1Chen, S. !$#journal Mol. Pharmacol. (1989) 35:818-822 !$#title Reaction of rat liver DT-diaphorase (NAD(P)H:quinone !1acceptor reductase) with 5'-[p-(fluorosulfonyl)benzoyl] !1-adenosine. !$#cross-references MUID:89281507; PMID:2499768 !$#accession A60561 !'##molecule_type protein !'##residues 147-157;264-268,'E',270-271 ##label LIU !'##note these peptides were radiolabeled by an affinity label for the !1NADH or NADPH binding site REFERENCE A60821 !$#authors Knox, R.J.; Boland, M.P.; Friedlos, F.; Coles, B.; Southan, !1C.; Roberts, J.J. !$#journal Biochem. Pharmacol. (1988) 37:4671-4677 !$#title The nitroreductase enzyme in Walker cells that activates 5- !1(aziridin-1-yl)-2,4-dinitrobenzamide (CB 1954) to 5- !1(aziridin-1-yl)-4-hydroxylamino-2-nitrobenzamide is a form !1of NAD(P)H dehydrogenase (quinone) (EC 1.6.99.2). !$#cross-references MUID:89076397; PMID:3144286 !$#accession A60821 !'##molecule_type protein !'##residues 24-32,34,'X',36-37,'X',39,'X',41-81,'X',83-105,'X',107-115, !1'X',117-131;156,'X',158-169,'X',171-207,'X',209-215,'E', !1217-226,'E',228-239,'XXXX',244-262,'I',264-270 ##label KNO REFERENCE S13883 !$#authors Ma, Q.; Wang, R.; Yang, C.S.; Lu, A.Y.H. !$#journal Arch. Biochem. Biophys. (1990) 283:311-317 !$#title Expression of mammalian DT-Diaphorase in Escherichia coli: !1purification and characterization of the expressed protein. !$#cross-references MUID:91112743; PMID:1703398 !$#accession S13883 !'##molecule_type protein !'##residues 2-21 ##label MAQ REFERENCE I52085 !$#authors Bayney, R.M.; Pickett, C.B. !$#journal Arch. Biochem. Biophys. (1988) 260:847-850 !$#title Rat liver NAD(P)H:quinone reductase: Isolation of a quinone !1reductase structural gene and prediction of the NH2 terminal !1sequence of the protein by double-stranded sequencing of !1exons 1 and 2. !$#cross-references MUID:88132903; PMID:2963593 !$#accession I52085 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-57 ##label RES !'##cross-references GB:M33039; NID:g206524; PIDN:AAA41990.1; !1PID:g554502 GENETICS !$#introns 3/1 CLASSIFICATION #superfamily NAD(P)H dehydrogenase (quinone) 2 KEYWORDS FAD; flavoprotein; homodimer; NAD; oxidoreductase SUMMARY #length 274 #molecular-weight 30946 #checksum 8851 SEQUENCE /// ENTRY A57691 #type complete TITLE NAD(P)H2 dehydrogenase (quinone) (EC 1.6.99.2) 2 [similarity] - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 03-Jun-2002 ACCESSIONS A57691 REFERENCE A57691 !$#authors Chen, S.; Clarke, P.E.; Martino, P.A.; Deng, P.S.K.; Yeh, !1C.H.; Lee, T.D.; Prochaska, H.J.; Talalay, P. !$#journal Protein Sci. (1994) 3:1296-1304 !$#title Mouse liver NAD(P)H:quinone acceptor oxidoreductase: protein !1sequence analysis by tandem mass spectrometry, cDNA cloning, !1expression in Escherichia coli, and enzyme activity !1analysis. !$#cross-references MUID:95078737; PMID:7527260 !$#accession A57691 !'##molecule_type mRNA !'##residues 1-274 ##label CHE !'##cross-references GB:S75951; NID:g913782; PIDN:AAB32718.1; !1PID:g913783 CLASSIFICATION #superfamily NAD(P)H dehydrogenase (quinone) 2 KEYWORDS NAD; oxidoreductase SUMMARY #length 274 #molecular-weight 30959 #checksum 7028 SEQUENCE /// ENTRY A30879 #type complete TITLE NAD(P)H2 dehydrogenase (quinone) (EC 1.6.99.2) 1 - human ALTERNATE_NAMES menadione reductase; phylloquinone reductase; quinone reductase ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS A41135; A30879 REFERENCE A41135 !$#authors Jaiswal, A.K. !$#journal Biochemistry (1991) 30:10647-10653 !$#title Human NAD(P)H:quinone oxidoreductase (NQO-1) gene structure !1and induction by dioxin. !$#cross-references MUID:92031511; PMID:1657151 !$#accession A41135 !'##molecule_type DNA !'##residues 1-274 ##label JAI !'##cross-references GB:M81600; GB:J05348; NID:g189290; PIDN:AAB60701.1; !1PID:g189292 REFERENCE A30879 !$#authors Jaiswal, A.K.; McBride, O.W.; Adesnik, M.; Nebert, D.W. !$#journal J. Biol. Chem. (1988) 263:13572-13578 !$#title Human dioxin-inducible cytosolic NAD(P)H:menadione !1oxidoreductase. cDNA sequence and localization of gene to !1chromosome 16. !$#cross-references MUID:88330879; PMID:2843525 !$#accession A30879 !'##molecule_type mRNA !'##residues 1-274 ##label JA2 !'##cross-references GB:J03934; NID:g189245; PIDN:AAA59940.1; !1PID:g189246 GENETICS !$#gene GDB:NMOR1 !'##cross-references GDB:120238; OMIM:125860 !$#map_position 16q22.1-16q22.1 !$#introns 3/1; 58/1; 101/3; 139/3; 173/3 CLASSIFICATION #superfamily NAD(P)H dehydrogenase (quinone) 2 KEYWORDS flavoprotein; NAD; oxidoreductase SUMMARY #length 274 #molecular-weight 30867 #checksum 4376 SEQUENCE /// ENTRY G64128 #type complete TITLE probable NAD(P)H2 dehydrogenase (quinone) (EC 1.6.99.2) - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS G64128 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession G64128 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-202 ##label TIGR !'##cross-references GB:U32829; GB:L42023; NID:g1574375; !1PIDN:AAC23194.1; PID:g1574386; TIGR:HI1544 CLASSIFICATION #superfamily NAD(P)H dehydrogenase (quinone) 2 KEYWORDS NAD; oxidoreductase SUMMARY #length 202 #molecular-weight 23159 #checksum 9888 SEQUENCE /// ENTRY B65129 #type complete TITLE probable NAD(P)H2 dehydrogenase (quinone) (EC 1.6.99.2) - Escherichia coli (strain K-12) ALTERNATE_NAMES hypothetical protein kifB-prkB intergenic region ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS B65129 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65129 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-184 ##label BLAT !'##cross-references GB:AE000411; GB:U00096; NID:g2367213; !1PIDN:AAC76376.1; PID:g1789750; UWGP:b3351 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yheR CLASSIFICATION #superfamily NAD(P)H dehydrogenase (quinone) 2 KEYWORDS flavoprotein; NAD; oxidoreductase SUMMARY #length 184 #molecular-weight 20958 #checksum 6762 SEQUENCE /// ENTRY F64725 #type complete TITLE probable NAD(P)H2 dehydrogenase (quinone) (EC 1.6.99.2) yabF - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS F64725; S40567 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64725 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-176 ##label BLAT !'##cross-references GB:AE000115; GB:U00096; NID:g1786230; !1PIDN:AAC73157.1; PID:g1786231; UWGP:b0046 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40567 !'##status preliminary !'##molecule_type DNA !'##residues 1-78,'N',80-122,'G',124-176 ##label YUR !'##cross-references EMBL:D10483; NID:g216434; PIDN:BAA01322.1; !1PID:g216471 GENETICS !$#gene yabF CLASSIFICATION #superfamily NAD(P)H dehydrogenase (quinone) 2 KEYWORDS flavoprotein; NAD; oxidoreductase SUMMARY #length 176 #molecular-weight 20170 #checksum 4522 SEQUENCE /// ENTRY DNHUN2 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 2 - human mitochondrion ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 2 ORGANISM #formal_name mitochondrion Homo sapiens #common_name man DATE 22-May-1981 #sequence_revision 17-Jul-1998 #text_change 03-Jun-2002 ACCESSIONS A00414; A38016; I52262; I65212 REFERENCE A00151 !$#authors Anderson, S.; Bankier, A.T.; Barrell, B.G.; de Bruijn, !1M.H.L.; Coulson, A.R.; Drouin, J.; Eperon, I.C.; Nierlich, !1D.P.; Roe, B.A.; Sanger, F.; Schreier, P.H.; Smith, A.J.H.; !1Staden, R.; Young, I.G. !$#journal Nature (1981) 290:457-465 !$#title Sequence and organization of the human mitochondrial genome. !$#cross-references MUID:81173052; PMID:7219534 !$#accession A00414 !'##molecule_type DNA !'##residues 1-347 ##label AND !'##cross-references GB:V00662; NID:g13003; PIDN:CAA24027.1; !1PID:g578710; GSPDB:GN00100 !'##note the authors translated the initiation codon ATT for residue 1 !1as Ile REFERENCE A38016 !$#authors Sanger, F.; Coulson, A.R.; Barrell, B.G.; Smith, A.J.H.; !1Roe, B.A. !$#journal J. Mol. Biol. (1980) 143:161-178 !$#title Cloning in single-stranded bacteriophage as an aid to rapid !1DNA sequencing. !$#cross-references MUID:81170577; PMID:6260957 !$#accession A38016 !'##molecule_type DNA !'##residues 37-347 ##label SAN !'##cross-references GB:M10546; NID:g337297; PIDN:AAA65502.1; !1PID:g786121 !'##note the authors do not show a translation for 1-36 and use 37-Met !1as the start codon REFERENCE I52262 !$#authors Lin, F.H.; Lin, R.; Wisniewski, H.M.; Hwang, Y.W.; !1Grundke-Iqbal, I.; Healy-Louie, G.; Iqbal, K. !$#journal Biochem. Biophys. Res. Commun. (1992) 182:238-246 !$#title Detection of point mutations in codon 331 of mitochondrial !1NADH dehydrogenase subunit 2 in Alzheimer's brains. !$#cross-references MUID:92118019; PMID:1370613 !$#accession I52262 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 269-330,'T',332-347 ##label LIN1 !'##cross-references GB:S75895; NID:g242496; PIDN:AAB20905.1; !1PID:g242497 !'##experimental_source mutation, Alzheimer's disease, clone 82-2 !$#accession I65212 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 269-270,278-330,'S',332,'LDSVFLWLT',342 ##label LIN2 !'##cross-references GB:S75896; NID:g242498; PIDN:AAB20906.1; !1PID:g242499 GENETICS !$#gene GDB:MTND2 !'##cross-references GDB:118912; OMIM:516001 !$#map_position MTH4470-5511 !$#genome mitochondrion !$#genetic_code SGC1 !$#start_codon ATT CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 2 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 347 #molecular-weight 38960 #checksum 6734 SEQUENCE /// ENTRY QXXL2M #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 2 - African clawed frog mitochondrion ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 2 ORGANISM #formal_name mitochondrion Xenopus laevis #common_name African clawed frog DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 03-Jun-2002 ACCESSIONS A00417 REFERENCE A00155 !$#authors Roe, B.A.; Ma, D.P.; Wilson, R.K.; Wong, J.F.H. !$#journal J. Biol. Chem. (1985) 260:9759-9774 !$#title The complete nucleotide sequence of the Xenopus laevis !1mitochondrial genome. !$#cross-references MUID:85261388; PMID:4019494 !$#accession A00417 !'##molecule_type DNA !'##residues 1-345 ##label ROE !'##cross-references GB:M10217; GB:X01600; GB:X01601; GB:X02890; !1NID:g343717; PIDN:AAA66459.1; PID:g807684 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 2 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 345 #molecular-weight 37671 #checksum 3982 SEQUENCE /// ENTRY QXBO2M #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 2 - bovine mitochondrion ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 2 ORGANISM #formal_name mitochondrion Bos primigenius taurus #common_name cattle DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 03-Jun-2002 ACCESSIONS A00415 REFERENCE A00152 !$#authors Anderson, S.; de Bruijn, M.H.L.; Coulson, A.R.; Eperon, !1I.C.; Sanger, F.; Young, I.G. !$#journal J. Mol. Biol. (1982) 156:683-717 !$#title Complete sequence of bovine mitochondrial DNA. Conserved !1features of the mammalian mitochondrial genome. !$#cross-references MUID:83010260; PMID:7120390 !$#accession A00415 !'##molecule_type DNA !'##residues 1-347 ##label AND !'##cross-references GB:J01394; NID:g336430; PIDN:AAB59269.1; !1PID:g336432; EMBL:V00654; NID:g12800; PID:g12802 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 2 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 347 #molecular-weight 39254 #checksum 7342 SEQUENCE /// ENTRY QXFG2B #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 2 - bullfrog mitochondrion ORGANISM #formal_name mitochondrion Rana catesbeiana #common_name bullfrog DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 03-Jun-2002 ACCESSIONS A41451; I50501; JT0265 REFERENCE A41451 !$#authors Fujii, H.; Shimada, T.; Goto, Y.; Okazaki, T. !$#journal J. Biochem. (1988) 103:474-481 !$#title Cloning of the mitochondrial genome of Rana catesbeiana and !1the nucleotide sequences of the ND2 and five tRNA genes. !$#cross-references MUID:88273072; PMID:3260590 !$#accession A41451 !'##molecule_type DNA !'##residues 1-344 ##label FUJ !'##cross-references GB:D00197 REFERENCE I50500 !$#authors Yoneyama, Y. !$#journal Nippon Ika Daigaku Zasshi (1987) 54:429-440 !$#title The nucleotide sequences of the heavy and light strand !1replication origins of the Rana catesbeiana mitochondrial !1genome. !$#cross-references MUID:88033615; PMID:2444617 !$#accession I50501 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 325-344 ##label YON !'##cross-references GB:D12695; NID:g343989; PIDN:BAA02192.1; !1PID:g343990 REFERENCE JT0265 !$#authors Fujii, H. !$#journal Nichiidaishi (1987) 54:59-71 !$#title Cloning of the entire mitochondrial genome of Rana !1catesbeiana and nucleotide sequencing of the URF2 and its !1flanking genes. !$#accession JT0265 !'##molecule_type DNA !'##residues 'I',2-344 ##label FU2 !'##note article in Japanese with English abstract GENETICS !$#genome mitochondrion !$#genetic_code SGC1 !$#start_codon ATT !$#introns #status absent CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 2 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 344 #molecular-weight 37624 #checksum 412 SEQUENCE /// ENTRY QXMS2M #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 2 - mouse mitochondrion ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 2 ORGANISM #formal_name mitochondrion Mus musculus #common_name house mouse DATE 02-Apr-1982 #sequence_revision 02-Apr-1982 #text_change 03-Jun-2002 ACCESSIONS A00416 REFERENCE A00153 !$#authors Bibb, M.J.; Van Etten, R.A.; Wright, C.T.; Walberg, M.W.; !1Clayton, D.A. !$#journal Cell (1981) 26:167-180 !$#title Sequence and gene organization of mouse mitochondrial DNA. !$#cross-references MUID:82137051; PMID:7332926 !$#accession A00416 !'##molecule_type DNA !'##residues 1-345 ##label BIB !'##cross-references GB:J01420; NID:g342520; PIDN:AAB48645.1; !1PID:g488491; EMBL:V00711; NID:g13838; PID:g13840 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 2 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 345 #molecular-weight 38764 #checksum 238 SEQUENCE /// ENTRY S35463 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 2 - hillstream loach (Crossostoma lacustre) mitochondrion ORGANISM #formal_name mitochondrion Crossostoma lacustre DATE 14-Aug-1998 #sequence_revision 14-Aug-1998 #text_change 03-Jun-2002 ACCESSIONS S35463; S60272 REFERENCE S35462 !$#authors Tzeng, C.S.; Hui, C.F.; Shen, S.C.; Huang, P.C. !$#journal Nucleic Acids Res. (1992) 20:4853-4858 !$#title The complete nucleotide sequence of the Crossostoma lacustre !1mitochondrial genome: conservation and variations among !1vertebrates. !$#cross-references MUID:93027205; PMID:1408800 !$#accession S35463 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-348 ##label TZE1 !'##cross-references EMBL:M91245; NID:g1381122; PIDN:AAB96812.1; !1PID:g336705 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1992 REFERENCE S60271 !$#authors Tzeng, C.S.; Shen, S.C.; Huang, P.C. !$#journal Bull. Inst. Zool. Acad. Sin. (1990) 29:11-19 !$#title Mitochondrial DNA identity of Crossostoma (Homalopteridae, !1Pisces) from two river systems of the same geographical !1origin. !$#accession S60272 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-348 ##label TZE2 !'##cross-references GB:M91245; NID:g1381122; PIDN:AAB96812.1; !1PID:g336705 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 2 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 348 #molecular-weight 37925 #checksum 8427 SEQUENCE /// ENTRY S45350 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 2 - Atlantic cod mitochondrion ORGANISM #formal_name mitochondrion Gadus morhua #common_name Atlantic cod DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S45350; T11821 REFERENCE S45350 !$#authors Johansen, S.; Johansen, T. !$#journal Biochim. Biophys. Acta (1994) 1218:213-217 !$#title Sequence analysis of 12 structural genes and a novel !1non-coding region from mitochondrial DNA of Atlantic cod, !1Gadus morhua. !$#cross-references MUID:94289483; PMID:8018725 !$#accession S45350 !'##molecule_type DNA !'##residues 1-348 ##label JOH !'##cross-references EMBL:X76363; NID:g525245; PIDN:CAA53964.1; !1PID:g525246 REFERENCE Z17351 !$#authors Johansen, S.; Bakke, I. !$#journal Mol. Marine Biol. Biotechnol. (1996) 5:203-214 !$#title The complete mitochondrial DNA sequence of Atlantic cod, !1Gadus morhua: Relevance to taxonomic studies among !1cod-fishes. !$#cross-references MUID:96414925; PMID:8817926 !$#accession T11821 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-348 ##label JO2 !'##cross-references EMBL:X99772; PIDN:CAA68107.1 !'##experimental_source norwegian coastal stock (NC-1) GENETICS !$#gene nd2 !$#genome mitochondrion !$#genetic_code SGC1 !$#note ND2 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 2 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 348 #molecular-weight 37893 #checksum 1295 SEQUENCE /// ENTRY S36003 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 2 - common carp mitochondrion ORGANISM #formal_name mitochondrion Cyprinus carpio #common_name common carp DATE 24-Jul-1998 #sequence_revision 24-Jul-1998 #text_change 03-Jun-2002 ACCESSIONS S36003; B44650 REFERENCE S21910 !$#authors Chang, Y.S.; Huang, F.L. !$#submission submitted to the EMBL Data Library, July 1991 !$#description The cDNA and primary structure of pregrowth hormones of !1three species of Cyprinadae: silver carp, bighead carp and !1grass carp. !$#accession S36003 !'##molecule_type DNA !'##residues 1-348 ##label CHA1 !'##cross-references EMBL:X61010; NID:g436882; PIDN:CAA43333.1; !1PID:g12835 REFERENCE A44650 !$#authors Chang, Y.S.; Huang, F.L.; Lo, T.B. !$#journal J. Mol. Evol. (1994) 38:138-155 !$#title The complete nucleotide sequence and gene organization of !1carp (Cyprinus carpio) mitochondrial genome. !$#cross-references MUID:94223691; PMID:8169959 !$#accession B44650 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type DNA !'##residues 1-348 ##label CHA2 !'##cross-references EMBL:X61010; NID:g436882; PIDN:CAA43333.1; !1PID:g12835 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 2 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 348 #molecular-weight 37851 #checksum 9032 SEQUENCE /// ENTRY QXFF2Y #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 2 - fruit fly (Drosophila yakuba) mitochondrion ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 2 ORGANISM #formal_name mitochondrion Drosophila yakuba DATE 18-Apr-1984 #sequence_revision 18-Apr-1984 #text_change 03-Jun-2002 ACCESSIONS B93488; A93445; A25797; A00418 REFERENCE A93488 !$#authors Clary, D.O.; Wolstenholme, D.R. !$#journal Nucleic Acids Res. (1983) 11:6859-6872 !$#title Genes for cytochrome c oxidase subunit I, URF2, and three !1tRNAs in Drosophila mitochondrial DNA. !$#cross-references MUID:84041489; PMID:6314262 !$#accession B93488 !'##molecule_type DNA !'##residues 1-341 ##label CL1 !'##cross-references GB:X03240; GB:J01400; GB:J01402; GB:J01403; !1GB:J01406; GB:J01408; GB:V01521; GB:X00563; NID:g12923; !1PIDN:CAA26985.1; PID:g529255 !'##note the authors translated the initiation codon ATT for residue 1 !1as Ile REFERENCE A93445 !$#authors Clary, D.O.; Goddard, J.M.; Martin, S.C.; Fauron, C.M.R.; !1Wolstenholme, D.R. !$#journal Nucleic Acids Res. (1982) 10:6619-6637 !$#title Drosophila mitochondrial DNA: a novel gene order. !$#cross-references MUID:83090428; PMID:6294611 !$#accession A93445 !'##molecule_type DNA !'##residues 1-56 ##label CL2 !'##note the authors translated the initiation codon ATT for residue 1 !1as Ile REFERENCE A92962 !$#authors Clary, D.O.; Wolstenholme, D.R. !$#journal J. Mol. Evol. (1985) 22:252-271 !$#title The mitochondrial DNA molecule of Drosophila yakuba: !1nucleotide sequence, gene organization, and genetic code. !$#cross-references MUID:86089137; PMID:3001325 !$#accession A25797 !'##molecule_type DNA !'##residues 1-341 ##label CLA !'##cross-references GB:X03240; GB:J01400; GB:J01402; GB:J01403; !1GB:J01406; GB:J01408; GB:V01521; GB:X00563; NID:g12923; !1PIDN:CAA26985.1; PID:g529255 GENETICS !$#gene FlyBase:Dyak/mt:ND2 !'##cross-references FlyBase:FBgn0013184 !$#genome mitochondrion !$#genetic_code SGC4 !$#start_codon ATT CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 2 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 341 #molecular-weight 39495 #checksum 4251 SEQUENCE /// ENTRY QXFF2M #type fragment TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 2 - fruit fly (Drosophila melanogaster) mitochondrion (fragment) ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 2 ORGANISM #formal_name mitochondrion Drosophila melanogaster DATE 18-Apr-1984 #sequence_revision 18-Apr-1984 #text_change 03-Jun-2002 ACCESSIONS A00419 REFERENCE A93307 !$#authors de Bruijn, M.H.L. !$#journal Nature (1983) 304:234-241 !$#title Drosophila melanogaster mitochondrial DNA, a novel !1organization and genetic code. !$#cross-references MUID:83245048; PMID:6408489 !$#accession A00419 !'##molecule_type DNA !'##residues 1-286 ##label DEB !'##cross-references GB:J01404; GB:J01405; GB:J01407; NID:g336811; !1PIDN:AAB59238.1; PID:g472806 GENETICS !$#gene FlyBase:mt:ND2 !'##cross-references FlyBase:FBgn0013680 !$#genome mitochondrion !$#genetic_code SGC4 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 2 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 286 #checksum 2527 SEQUENCE /// ENTRY DNETU2 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 2 - sugar beet mitochondrion ORGANISM #formal_name mitochondrion Beta vulgaris var. altissima #common_name sugar beet DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 03-Jun-2002 ACCESSIONS S12804 REFERENCE S12804 !$#authors Xue, Y.; Davies, D.R.; Thomas, C.M. !$#journal Mol. Gen. Genet. (1990) 221:195-198 !$#title Sugarbeet mitochondria contain an open reading frame showing !1extensive sequence homology to the subunit 2 gene of the !1NADH:ubiquinone reductase complex. !$#cross-references MUID:90318317; PMID:2115110 !$#accession S12804 !'##molecule_type DNA !'##residues 1-515 ##label XUE !'##cross-references EMBL:X16828; NID:g12821; PIDN:CAA34728.1; !1PID:g12822 !'##note it is uncertain whether Met-1 or Met-52 is the initiator GENETICS !$#gene nad2 !$#genome mitochondrion CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 2 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 515 #molecular-weight 56274 #checksum 49 SEQUENCE /// ENTRY S26018 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 2 - pig roundworm mitochondrion ORGANISM #formal_name mitochondrion Ascaris suum #common_name pig roundworm DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S26018; S25791 REFERENCE S26014 !$#authors Okimoto, R.; Macfarlane, J.L.; Clary, D.O.; Wolstenholme, !1D.R. !$#journal Genetics (1992) 130:471-498 !$#title The mitochondrial genomes of two nematodes, Caenorhabditis !1elegans and Ascaris suum. !$#cross-references MUID:92201635; PMID:1551572 !$#accession S26018 !'##molecule_type DNA !'##residues 1-281 ##label OKI !'##cross-references EMBL:X54253 !'##note the authors translated the initiation codon TTG for residue 1 !1as Leu REFERENCE S13139 !$#authors Okimoto, R.; Macfarlane, J.L.; Wolstenholme, D.R. !$#journal Nucleic Acids Res. (1990) 18:6113-6118 !$#title Evidence for the frequent use of TTG as the translation !1initiation codon of mitochondrial protein genes in the !1nematodes, Ascaris suum and Caenorhabditis elegans. !$#cross-references MUID:91045077; PMID:2235493 !$#accession S25791 !'##molecule_type DNA !'##residues 1-25 ##label OK2 !'##cross-references EMBL:X54253 !'##note the authors translated the initiation codon TTG for residue 1 !1as Leu GENETICS !$#gene ND2 !$#genome mitochondrion !$#genetic_code SGC4 !$#start_codon TTG CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 2 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 281 #molecular-weight 33135 #checksum 4766 SEQUENCE /// ENTRY DENTN2 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 2 - common tobacco chloroplast ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 2; ndh2 protein ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 03-Jun-2002 ACCESSIONS A00420 REFERENCE A00149 !$#authors Sugiura, M. !$#submission submitted to the EMBL Data Library, August 1986 !$#accession A00420 !'##molecule_type DNA !'##residues 1-361 ##label SUG !'##experimental_source cv. Bright Yellow 4 REFERENCE A38013 !$#authors Shinozaki, K.; Ohme, M.; Tanaka, M.; Wakasugi, T.; !1Hayashida, N.; Matsubayashi, T.; Zaita, N.; Chunwongse, J.; !1Obokata, J.; Yamaguchi-Shinozaki, K.; Ohto, C.; Torazawa, !1K.; Meng, B.Y.; Sugita, M.; Deno, H.; Kamogashira, T.; !1Yamada, K.; Kusuda, J.; Takaiwa, F.; Kato, A.; Tohdoh, N.; !1Shimada, H.; Sugiura, M. !$#journal EMBO J. (1986) 5:2043-2049 !$#title The complete nucleotide sequence of the tobacco chloroplast !1genome: its gene organization and expression. !$#contents annotation; gene organization, sites, features GENETICS !$#gene ndh2; ndhB !$#genome chloroplast !$#introns 136/3 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 2 KEYWORDS chloroplast; membrane-associated complex; NAD; !1oxidoreductase SUMMARY #length 361 #molecular-weight 39655 #checksum 3657 SEQUENCE /// ENTRY DELVN2 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 2 - liverwort (Marchantia polymorpha) chloroplast ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 2 ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 03-Jun-2002 ACCESSIONS S01569; A00421 REFERENCE S01567 !$#authors Umesono, K.; Inokuchi, H.; Shiki, Y.; Takeuchi, M.; Chang, !1Z.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Ohyama, K.; Ozeki, !1H. !$#journal J. Mol. Biol. (1988) 203:299-331 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. II. Gene organization of the large !1single copy region from rps'12 to atpB. !$#cross-references MUID:89068686; PMID:2974085 !$#accession S01569 !'##molecule_type DNA !'##residues 1-501 ##label UME !'##cross-references EMBL:X04465; NID:g11640; PIDN:CAA28058.1; !1PID:g453589 REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features GENETICS !$#gene ndh2 !$#genome chloroplast !$#introns 242/3 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 2 KEYWORDS chloroplast; membrane-associated complex; NAD; !1oxidoreductase SUMMARY #length 501 #molecular-weight 56189 #checksum 5569 SEQUENCE /// ENTRY DERZN2 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 2 - rice chloroplast ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 2; ndh2 protein ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 03-Jun-2002 ACCESSIONS JQ0275; S05155 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0275 !'##molecule_type DNA !'##residues 1-510 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05155 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-510 ##label HIR !'##cross-references EMBL:X15901; NID:g11957; PIDN:CAA33941.1; !1PID:g669085 !'##experimental_source cv. Nihonbare GENETICS !$#gene ndhB !$#map_position CP87639-86863,86150-85395 !$#genome chloroplast !$#introns 259/3 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 2 KEYWORDS chloroplast; membrane-associated complex; NAD; !1oxidoreductase SUMMARY #length 510 #molecular-weight 56768 #checksum 4352 SEQUENCE /// ENTRY DNYC27 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 2 - Synechococcus sp. (strain PCC 7942) ORGANISM #formal_name Synechococcus sp. DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 03-Jun-2002 ACCESSIONS S19921 REFERENCE S19921 !$#authors Kaplan, A. !$#submission submitted to the EMBL Data Library, March 1992 !$#accession S19921 !'##molecule_type DNA !'##residues 1-521 ##label KAP !'##cross-references EMBL:X65027; NID:g46484; PIDN:CAA46161.1; !1PID:g46485 GENETICS !$#gene ndhB CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 2 KEYWORDS membrane-associated complex; NAD; oxidoreductase SUMMARY #length 521 #molecular-weight 55069 #checksum 9742 SEQUENCE /// ENTRY S07734 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 2 - Paramecium tetraurelia mitochondrion ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 2 ORGANISM #formal_name mitochondrion Paramecium tetraurelia DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S07734; JS0233 REFERENCE S07725 !$#authors Pritchard, A.E.; Seilhamer, J.J.; Mahalingam, R.; Sable, !1C.L.; Venuti, S.E.; Cummings, D.J. !$#journal Nucleic Acids Res. (1990) 18:173-180 !$#title Nucleotide sequence of the mitochondrial genome of !1Paramecium. !$#cross-references MUID:90174913; PMID:2308823 !$#accession S07734 !'##status translation not shown !'##molecule_type DNA !'##residues 1-193 ##label PRI1 !'##cross-references EMBL:X15917; NID:g13256; PIDN:CAA34043.1; !1PID:g515876 REFERENCE JS0231 !$#authors Pritchard, A.E.; Venuti, S.E.; Ghalambor, M.A.; Sable, C.L.; !1Cummings, D.J. !$#journal Gene (1989) 78:121-134 !$#title An unusual region of Paramecium mitochondrial DNA containing !1chloroplast-like genes. !$#cross-references MUID:89357489; PMID:2670676 !$#accession JS0233 !'##molecule_type DNA !'##residues 'L',2-193 ##label PRI2 !'##cross-references GB:M26930; NID:g341550; PIDN:AAA79255.1; !1PID:g1019630 !'##experimental_source strain sp. 4.51 !'##note the authors translated the initiation codon TTG for residue 1 !1as Leu GENETICS !$#gene ndh2 !$#genome mitochondrion !$#genetic_code SGC6 !$#start_codon TTG CLASSIFICATION #superfamily Paramecium NADH dehydrogenase (ubiquinone) !1chain 2 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 193 #molecular-weight 23181 #checksum 9281 SEQUENCE /// ENTRY S17854 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) 75K chain precursor - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S17854; S16382 REFERENCE S17854 !$#authors Chow, W.; Ragan, I.; Robinson, B.H. !$#journal Eur. J. Biochem. (1991) 201:547-550 !$#title Determination of the cDNA sequence for the human !1mitochondrial 75-kDa Fe-S protein of NADH-coenzyme Q !1reductase. !$#cross-references MUID:92037608; PMID:1935949 !$#accession S17854 !'##molecule_type mRNA !'##residues 1-727 ##label CHO !'##cross-references EMBL:X61100; NID:g38078; PIDN:CAA43412.1; !1PID:g38079 GENETICS !$#gene GDB:NDUFS1 !'##cross-references GDB:132062; OMIM:157655 !$#map_position 2q33-2q34 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 11 KEYWORDS iron-sulfur protein; membrane-associated complex; !1metalloprotein; mitochondrion; NAD; oxidoreductase FEATURE !$1-23 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$24-727 #product NADH dehydrogenase (ubiquinone) 75K chain !8#status predicted #label MAT SUMMARY #length 727 #molecular-weight 79573 #checksum 8774 SEQUENCE /// ENTRY DNHUN3 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 3 - human mitochondrion ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 3 ORGANISM #formal_name mitochondrion Homo sapiens #common_name man DATE 22-May-1981 #sequence_revision 23-Oct-1981 #text_change 03-Jun-2002 ACCESSIONS A00422 REFERENCE A00151 !$#authors Anderson, S.; Bankier, A.T.; Barrell, B.G.; de Bruijn, !1M.H.L.; Coulson, A.R.; Drouin, J.; Eperon, I.C.; Nierlich, !1D.P.; Roe, B.A.; Sanger, F.; Schreier, P.H.; Smith, A.J.H.; !1Staden, R.; Young, I.G. !$#journal Nature (1981) 290:457-465 !$#title Sequence and organization of the human mitochondrial genome. !$#cross-references MUID:81173052; PMID:7219534 !$#accession A00422 !'##molecule_type DNA !'##residues 1-115 ##label AND !'##cross-references GB:J01415; GB:M12548; GB:M58503; GB:M63932; !1GB:M63933; NID:g1944628; PIDN:AAB58950.1; PID:g506832; !1EMBL:V00662; NID:g13003; PID:g13011; GSPDB:GN00100 GENETICS !$#gene GDB:MTND3 !'##cross-references GDB:118913; OMIM:516002 !$#map_position MTH10059-10404 !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 3 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 115 #molecular-weight 13186 #checksum 3614 SEQUENCE /// ENTRY QXBO3M #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 3 - bovine mitochondrion ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 3 ORGANISM #formal_name mitochondrion Bos primigenius taurus #common_name cattle DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 03-Jun-2002 ACCESSIONS A00423 REFERENCE A00152 !$#authors Anderson, S.; de Bruijn, M.H.L.; Coulson, A.R.; Eperon, !1I.C.; Sanger, F.; Young, I.G. !$#journal J. Mol. Biol. (1982) 156:683-717 !$#title Complete sequence of bovine mitochondrial DNA. Conserved !1features of the mammalian mitochondrial genome. !$#cross-references MUID:83010260; PMID:7120390 !$#accession A00423 !'##molecule_type DNA !'##residues 1-115 ##label AND !'##cross-references GB:J01394; NID:g336430; PIDN:AAB59275.1; !1PID:g506805; EMBL:V00654; NID:g12800; PID:g12808 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 3 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 115 #molecular-weight 13054 #checksum 3024 SEQUENCE /// ENTRY QXMS3M #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 3 - mouse mitochondrion ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 3 ORGANISM #formal_name mitochondrion Mus musculus #common_name house mouse DATE 02-Apr-1982 #sequence_revision 05-Apr-1995 #text_change 03-Jun-2002 ACCESSIONS B55746; A00424 REFERENCE A55746 !$#authors Nachman, M.W.; Boyer, S.N.; Aquadro, C.F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1994) 91:6364-6368 !$#title Nonneutral evolution at the mitochondrial NADH dehydrogenase !1subunit 3 gene in mice. !$#cross-references MUID:94294382; PMID:8022788 !$#accession B55746 !'##molecule_type DNA !'##residues 'I',2-115 ##label NAC !'##cross-references GB:U09638; NID:g495201; PIDN:AAA19255.1; !1PID:g495202 !'##note the authors translated the initiation codon ATC for residue 1 !1as Ile REFERENCE A00153 !$#authors Bibb, M.J.; Van Etten, R.A.; Wright, C.T.; Walberg, M.W.; !1Clayton, D.A. !$#journal Cell (1981) 26:167-180 !$#title Sequence and gene organization of mouse mitochondrial DNA. !$#cross-references MUID:82137051; PMID:7332926 !$#accession A00424 !'##molecule_type DNA !'##residues 1-15,'T',17-32,34-115 ##label BIB !'##cross-references GB:J01420; NID:g342520; PIDN:AAB48651.1; !1PID:g896298 !'##note the authors translated the initiation codon ATC for residue 1 !1as Ile GENETICS !$#gene ND3 !$#genome mitochondrion !$#genetic_code SGC1 !$#start_codon ATC CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 3 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 115 #molecular-weight 13189 #checksum 3246 SEQUENCE /// ENTRY QXXL3M #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 3 - African clawed frog mitochondrion ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 3 ORGANISM #formal_name mitochondrion Xenopus laevis #common_name African clawed frog DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 03-Jun-2002 ACCESSIONS A00425 REFERENCE A00155 !$#authors Roe, B.A.; Ma, D.P.; Wilson, R.K.; Wong, J.F.H. !$#journal J. Biol. Chem. (1985) 260:9759-9774 !$#title The complete nucleotide sequence of the Xenopus laevis !1mitochondrial genome. !$#cross-references MUID:85261388; PMID:4019494 !$#accession A00425 !'##molecule_type DNA !'##residues 1-114 ##label ROE !'##cross-references GB:M10217; GB:X01600; GB:X01601; GB:X02890; !1NID:g343717; PIDN:AAA66465.1; PID:g807689 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 3 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 114 #molecular-weight 12923 #checksum 1117 SEQUENCE /// ENTRY DNWTU3 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 3 - wheat mitochondrion ORGANISM #formal_name mitochondrion Triticum aestivum #common_name common wheat DATE 30-Jun-1992 #sequence_revision 14-Aug-1998 #text_change 03-Jun-2002 ACCESSIONS JQ1374; S03609 REFERENCE JQ1374 !$#authors Gualberto, J.M.; Bonnard, G.; Lamattina, L.; Grienenberger, !1J.M. !$#journal Plant Cell (1991) 3:1109-1120 !$#title Expression of the wheat mitochondrial nad3-rps12 !1transcription unit: correlation between editing and mRNA !1maturation. !$#cross-references MUID:92338836; PMID:1726558 !$#accession JQ1374 !'##molecule_type mRNA !'##residues 1-118 ##label GUA !'##cross-references GB:X59153; GB:S40874; NID:g433681 !'##note in plant mitochondria, RNA editing involves the conversion of C !1in the primary transcript into U in the final mRNA !'##note this sequence is the translation of the consensus sequence of !1three cDNA clones REFERENCE S03609 !$#authors Gualberto, J.M.; Wintz, H.; Weil, J.H.; Grienenberger, J.M. !$#journal Mol. Gen. Genet. (1988) 215:118-127 !$#title The genes coding for subunit 3 of NADH dehydrogenase and for !1ribosomal protein S12 are present in the wheat and maize !1mitochondrial genomes and are co-transcribed. !$#cross-references MUID:89201232; PMID:2853827 !$#accession S03609 !'##molecule_type DNA !'##residues 1,'S',3-14,'P',16-20,'P',22-26,'P',28-45,'S',47-48,'S', !150-63,'P',65-69,'P',71,'P',73-76,'S',78-82,'PP',85-91,'S', !193-105,'S',107-114,'S',116,'R',118 ##label GU2 !'##cross-references EMBL:X14262; NID:g13703; PIDN:CAA32475.1; !1PID:g13704 GENETICS !$#gene nad3 !$#genome mitochondrion CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 3 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain; RNA !1editing SUMMARY #length 118 #molecular-weight 13725 #checksum 70 SEQUENCE /// ENTRY DNZMU3 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 3 - maize mitochondrion ORGANISM #formal_name mitochondrion Zea mays #common_name maize DATE 30-Jun-1992 #sequence_revision 28-Aug-1998 #text_change 03-Jun-2002 ACCESSIONS S70025; S70024; S05952 REFERENCE S70024 !$#authors Grosskopf, D.; Mulligan, R.M. !$#journal Curr. Genet. (1996) 29:556-563 !$#title Developmental- and tissue-specificity of RNA editing in !1mitochondria of suspension-cultured maize cells and !1seedlings. !$#cross-references MUID:96269915; PMID:8662195 !$#accession S70025 !'##molecule_type mRNA !'##residues 1-118 ##label GRO !'##experimental_source cultivar Black Mexican Sweet !'##note in plant mitochondria, RNA editing involves the conversion of C !1in the primary transcript into U in the final mRNA !$#accession S70024 !'##molecule_type DNA !'##residues 1,'S',3-14,'P',16-20,'P',22-26,'P',28-45,'L',47-48,'S', !150-61,'P',63,'P',65-69,'P',71,'P',73-76,'S',78-82,'PP', !185-91,'S',93-102,'T',104-114,'S',116,'R',118 ##label GR2 !'##experimental_source cultivar Black Mexican Sweet REFERENCE S03609 !$#authors Gualberto, J.M.; Wintz, H.; Weil, J.H.; Grienenberger, J.M. !$#journal Mol. Gen. Genet. (1988) 215:118-127 !$#title The genes coding for subunit 3 of NADH dehydrogenase and for !1ribosomal protein S12 are present in the wheat and maize !1mitochondrial genomes and are co-transcribed. !$#cross-references MUID:89201232; PMID:2853827 !$#accession S05952 !'##molecule_type DNA !'##residues 1,'S',3-14,'P',16-20,'P',22-26,'P',28-45,'S',47-48,'S', !150-61,'P',63,'P',65-69,'P',71,'P',73-76,'S',78-82,'PP', !185-91,'S',93-102,'T',104-114,'S',116,'R',118 ##label GUA !'##cross-references EMBL:X14709; NID:g13913; PIDN:CAA32833.1; !1PID:g13914 !'##experimental_source strain WF9-N !'##note the authors translated the codon CCG for residue 62 as Leu GENETICS !$#gene nad3 !$#genome mitochondrion FUNCTION !$#pathway respiratory chain !$#note FAD cofactor CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 3 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain; RNA !1editing SUMMARY #length 118 #molecular-weight 13711 #checksum 63 SEQUENCE /// ENTRY DNOBU3 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 3 - evening primrose mitochondrion ORGANISM #formal_name mitochondrion Oenothera villaricae #common_name evening primrose DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 03-Jun-2002 ACCESSIONS S12781; S12779 REFERENCE S12778 !$#authors Schuster, W.; Wissinger, B.; Unseld, M.; Brennicke, A. !$#journal EMBO J. (1990) 9:263-269 !$#title Transcripts of the NADH-dehydrogenase subunit 3 gene are !1differentially edited in Oenothera mitochondria. !$#cross-references MUID:90107953; PMID:1688531 !$#accession S12781 !'##molecule_type mRNA !'##residues 1-118 ##label SCH !'##cross-references EMBL:X52200; NID:g13178; PIDN:CAA36454.1; !1PID:g13179 !'##note in plant mitochondria, RNA editing involves the conversion of C !1in the primary transcript into U in the final mRNA !$#accession S12779 !'##molecule_type DNA !'##residues 1,'S',3-14,'P',16-48,'S',50-69,'P',71,'P',73-82,'PL',85-88, !1'P',90-91,'S',93-105,'S',107-114,'S',116,'R',118 ##label !1SCH2 !'##cross-references EMBL:X52199; NID:g13175; PIDN:CAA36452.1; !1PID:g13177 GENETICS !$#gene nad3 !$#genome mitochondrion CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 3 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain; RNA !1editing SUMMARY #length 118 #molecular-weight 13755 #checksum 545 SEQUENCE /// ENTRY DENTN3 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 3 - common tobacco chloroplast ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 3; ndh3 protein ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 03-Jun-2002 ACCESSIONS A00426 REFERENCE A00149 !$#authors Sugiura, M. !$#submission submitted to the EMBL Data Library, August 1986 !$#accession A00426 !'##molecule_type DNA !'##residues 1-120 ##label SUG !'##experimental_source cv. Bright Yellow 4 REFERENCE A38013 !$#authors Shinozaki, K.; Ohme, M.; Tanaka, M.; Wakasugi, T.; !1Hayashida, N.; Matsubayashi, T.; Zaita, N.; Chunwongse, J.; !1Obokata, J.; Yamaguchi-Shinozaki, K.; Ohto, C.; Torazawa, !1K.; Meng, B.Y.; Sugita, M.; Deno, H.; Kamogashira, T.; !1Yamada, K.; Kusuda, J.; Takaiwa, F.; Kato, A.; Tohdoh, N.; !1Shimada, H.; Sugiura, M. !$#journal EMBO J. (1986) 5:2043-2049 !$#title The complete nucleotide sequence of the tobacco chloroplast !1genome: its gene organization and expression. !$#contents annotation; gene organization, sites, features GENETICS !$#gene ndh3; ndhC !$#genome chloroplast CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 3 KEYWORDS chloroplast; membrane-associated complex; NAD; !1oxidoreductase SUMMARY #length 120 #molecular-weight 13916 #checksum 3923 SEQUENCE /// ENTRY DERZN3 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 3 - rice chloroplast ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 3; ndh3 protein ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 03-Jun-2002 ACCESSIONS JQ0228; S05108 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0228 !'##molecule_type DNA !'##residues 1-120 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05108 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-120 ##label HIR !'##cross-references EMBL:X15901; NID:g11957; PIDN:CAA34001.1; !1PID:g11989 !'##experimental_source cv. Nihonbare GENETICS !$#gene ndhC !$#map_position CP49662-49300 !$#genome chloroplast CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 3 KEYWORDS chloroplast; membrane-associated complex; NAD; !1oxidoreductase SUMMARY #length 120 #molecular-weight 13899 #checksum 4417 SEQUENCE /// ENTRY DELVN3 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 3 - liverwort (Marchantia polymorpha) chloroplast ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 3; ndh3 protein ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 03-Jun-2002 ACCESSIONS A00427; S01599 REFERENCE A00150 !$#authors Ohyama, K. !$#submission submitted to the EMBL Data Library, October 1986 !$#accession A00427 !'##molecule_type DNA !'##residues 1-120 ##label OHY REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features REFERENCE S01567 !$#authors Umesono, K.; Inokuchi, H.; Shiki, Y.; Takeuchi, M.; Chang, !1Z.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Ohyama, K.; Ozeki, !1H. !$#journal J. Mol. Biol. (1988) 203:299-331 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. II. Gene organization of the large !1single copy region from rps'12 to atpB. !$#cross-references MUID:89068686; PMID:2974085 !$#accession S01599 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-120 ##label UME !'##cross-references GB:X04465; GB:Y00686; NID:g11640; PIDN:CAA28089.1; !1PID:g11677 GENETICS !$#gene ndh3; ndhC !$#genome chloroplast CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 3 KEYWORDS chloroplast; membrane-associated complex; NAD; !1oxidoreductase SUMMARY #length 120 #molecular-weight 14189 #checksum 1840 SEQUENCE /// ENTRY DNHUNL #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 4L - human mitochondrion ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 4L ORGANISM #formal_name mitochondrion Homo sapiens #common_name man DATE 22-May-1981 #sequence_revision 23-Oct-1981 #text_change 03-Jun-2002 ACCESSIONS A00428; S24587; I80238 REFERENCE A00151 !$#authors Anderson, S.; Bankier, A.T.; Barrell, B.G.; de Bruijn, !1M.H.L.; Coulson, A.R.; Drouin, J.; Eperon, I.C.; Nierlich, !1D.P.; Roe, B.A.; Sanger, F.; Schreier, P.H.; Smith, A.J.H.; !1Staden, R.; Young, I.G. !$#journal Nature (1981) 290:457-465 !$#title Sequence and organization of the human mitochondrial genome. !$#cross-references MUID:81173052; PMID:7219534 !$#accession A00428 !'##molecule_type DNA !'##residues 1-98 ##label AND !'##cross-references GB:J01415; GB:M12548; GB:M58503; GB:M63932; !1GB:M63933; NID:g1944628; PIDN:AAB58951.1; PID:g337197; !1EMBL:V00662; NID:g13003; PID:g13012; GSPDB:GN00100 REFERENCE S24587 !$#authors Marzuki, S. !$#submission submitted to the EMBL Data Library, October 1991 !$#accession S24587 !'##molecule_type DNA !'##residues 1-98 ##label MAR !'##cross-references EMBL:X62996; NID:g13000; PIDN:CAA44730.1; !1PID:g13001 REFERENCE I59384 !$#authors Horai, S.; Hayasaka, K.; Kondo, R.; Tsugane, K.; Takahata, !1N. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1995) 92:532-536 !$#title Recent African origin of modern humans revealed by complete !1sequences of hominoid mitochondrial DNAs. !$#cross-references MUID:95132634; PMID:7530363 !$#accession I80238 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-98 ##label RES !'##cross-references GB:D38112; NID:g644480; PIDN:BAA07296.1; !1PID:g704446 GENETICS !$#gene GDB:MTND4L !'##cross-references GDB:118915; OMIM:516004 !$#map_position MTH10470-10766 !$#genome mitochondrion !$#genetic_code SGC1 FUNCTION !$#description catalyzes the reduction of ubiquinone by NADH CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 4L KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 98 #molecular-weight 10741 #checksum 2373 SEQUENCE /// ENTRY T14198 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 4L - chimpanzee mitochondrion ORGANISM #formal_name mitochondrion Pan troglodytes #common_name chimpanzee DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Jun-2002 ACCESSIONS T14198; T11273 REFERENCE I59384 !$#authors Horai, S.; Hayasaka, K.; Kondo, R.; Tsugane, K.; Takahata, !1N. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1995) 92:532-536 !$#title Recent African origin of modern humans revealed by complete !1sequences of hominoid mitochondrial DNAs. !$#cross-references MUID:95132634; PMID:7530363 !$#accession T14198 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-98 ##label HOR !'##cross-references EMBL:D38113; PIDN:BAA07301.1 REFERENCE Z17257 !$#authors Arnason, U.; Xu, X.; Gullberg, A. !$#journal J. Mol. Evol. (1996) 42:145-152 !$#title Comparison between the complete mitochondrial DNA sequences !1of Homo and the common chimpanzee based on non-chimaeric !1sequences. !$#cross-references MUID:9707729; PMID:8919866 !$#accession T11273 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-98 ##label ARN !'##cross-references EMBL:X93335; NID:g1262390; PIDN:CAA63722.1 !'##experimental_source sub_species verus; isolate Jenny GENETICS !$#gene NADH4L !$#genome mitochondrion !$#genetic_code SGC1 FUNCTION !$#description catalyzes the reduction of ubiquinone by NADH CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 4L KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 98 #molecular-weight 10771 #checksum 2468 SEQUENCE /// ENTRY T14148 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 4L - pygmy chimpanzee mitochondrion ORGANISM #formal_name mitochondrion Pan paniscus #common_name pygmy chimpanzee, bonobo DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Jun-2002 ACCESSIONS T14148 REFERENCE I59384 !$#authors Horai, S.; Hayasaka, K.; Kondo, R.; Tsugane, K.; Takahata, !1N. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1995) 92:532-536 !$#title Recent African origin of modern humans revealed by complete !1sequences of hominoid mitochondrial DNAs. !$#cross-references MUID:95132634; PMID:7530363 !$#accession T14148 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-98 ##label HOR !'##cross-references EMBL:D38116; PIDN:BAA07314.1 GENETICS !$#gene NADH4L !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 4L KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 98 #molecular-weight 10801 #checksum 3304 SEQUENCE /// ENTRY T11415 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 4L [similarity] - western lowland gorilla mitochondrion ORGANISM #formal_name mitochondrion Gorilla gorilla gorilla #common_name western lowland gorilla DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 03-Jun-2002 ACCESSIONS T11415 REFERENCE Z17269 !$#authors Xu, X.; Arnason, U. !$#journal Mol. Biol. Evol. (1996) 13:691-698 !$#title A complete sequence of the mitochondrial genome of the !1Western lowland gorilla. !$#cross-references MUID:96212991; PMID:8676744 !$#accession T11415 !'##molecule_type DNA !'##residues 1-98 ##label XUX !'##cross-references GB:X93347; NID:g1304307; PIDN:CAA63723.1; !1PID:g1304308; GSPDB:GN00106 !'##note submitted to GenBank, November 1995 GENETICS !$#gene NADH4L !$#genome mitochondrion !$#genetic_code SGC1 FUNCTION !$#description catalyzes the reduction of ubiquinone by NADH CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 4L KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 98 #molecular-weight 10762 #checksum 2774 SEQUENCE /// ENTRY T14144 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 4L - orangutan mitochondrion ORGANISM #formal_name mitochondrion Pongo pygmaeus #common_name orangutan DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Jun-2002 ACCESSIONS T14144 REFERENCE I59384 !$#authors Horai, S.; Hayasaka, K.; Kondo, R.; Tsugane, K.; Takahata, !1N. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1995) 92:532-536 !$#title Recent African origin of modern humans revealed by complete !1sequences of hominoid mitochondrial DNAs. !$#cross-references MUID:95132634; PMID:7530363 !$#accession T14144 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-98 ##label HOR !'##cross-references EMBL:D38115; PIDN:BAA07310.1 GENETICS !$#gene NADH4L !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 4L KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 98 #molecular-weight 10782 #checksum 2663 SEQUENCE /// ENTRY T17351 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 4L - Trachypithecus leucocephalus mitochondrion ORGANISM #formal_name mitochondrion Trachypithecus leucocephalus DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Jun-2002 ACCESSIONS T17351; T17354; T17357 REFERENCE Z18709 !$#authors Wang, W.; Forstner, M.R.J.; Zhang, Y.P.; Lui, Z.M.; Wei, Y.; !1Huang, H.Q.; Hu, H.G.; Xie, Y.X.; Wu, D.H.; Melnick, D.J. !$#journal Int. J. Primatol. (1997) 18:305-320 !$#title A phylogeny of Chinese leaf monkeys using mitochondrial !1ND3-ND4 gene sequences. !$#accession T17351 !'##molecule_type DNA !'##residues 1-98 ##label WAN1 !'##cross-references EMBL:U92966; NID:g2290477; PID:g2290479; !1PIDN:AAD04697.1 !'##experimental_source isolate BTY1 !$#accession T17354 !'##molecule_type DNA !'##residues 1-98 ##label WAN2 !'##cross-references EMBL:U92967; NID:g2290481; PID:g2290483; !1PIDN:AAD04700.1 !'##experimental_source isolate BTY2 !$#accession T17357 !'##molecule_type DNA !'##residues 1-98 ##label WAN3 !'##cross-references EMBL:U92968; NID:g2290485; PID:g2290487; !1PIDN:AAD04703.1 !'##experimental_source isolate BTY3 GENETICS !$#gene ND4L !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 4L KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 98 #molecular-weight 10823 #checksum 602 SEQUENCE /// ENTRY T11841 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 4L - common gibbon mitochondrion ORGANISM #formal_name mitochondrion Hylobates lar #common_name common gibbon, white-handed gibbon DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Jun-2002 ACCESSIONS T11841 REFERENCE Z17353 !$#authors Arnason, U.; Gullberg, A.; Xu, X. !$#journal Hereditas (1996) 124:185-189 !$#title A complete mitochondrial DNA molecule of the white-handed !1gibbon, Hylobates lar, and comparison among individual !1mitochondrial genes of all hominoid genera. !$#accession T11841 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-98 ##label ARN !'##cross-references EMBL:X99256; PIDN:CAA67636.1 !'##experimental_source isolate Ester GENETICS !$#gene NADH4L !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 4L KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 98 #molecular-weight 10739 #checksum 1404 SEQUENCE /// ENTRY QXBO4L #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 4L - bovine mitochondrion ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 4L ORGANISM #formal_name mitochondrion Bos primigenius taurus #common_name cattle DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 03-Jun-2002 ACCESSIONS A00429 REFERENCE A00152 !$#authors Anderson, S.; de Bruijn, M.H.L.; Coulson, A.R.; Eperon, !1I.C.; Sanger, F.; Young, I.G. !$#journal J. Mol. Biol. (1982) 156:683-717 !$#title Complete sequence of bovine mitochondrial DNA. Conserved !1features of the mammalian mitochondrial genome. !$#cross-references MUID:83010260; PMID:7120390 !$#accession A00429 !'##molecule_type DNA !'##residues 1-98 ##label AND !'##cross-references GB:J01394; NID:g336430; PIDN:AAB59276.1; !1PID:g336439; EMBL:V00654; NID:g12800; PID:g12809 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 4L KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 98 #molecular-weight 10797 #checksum 2979 SEQUENCE /// ENTRY QXMS4L #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 4L - mouse mitochondrion ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 4L ORGANISM #formal_name mitochondrion Mus musculus #common_name house mouse DATE 02-Apr-1982 #sequence_revision 02-Apr-1982 #text_change 03-Jun-2002 ACCESSIONS A00430 REFERENCE A00153 !$#authors Bibb, M.J.; Van Etten, R.A.; Wright, C.T.; Walberg, M.W.; !1Clayton, D.A. !$#journal Cell (1981) 26:167-180 !$#title Sequence and gene organization of mouse mitochondrial DNA. !$#cross-references MUID:82137051; PMID:7332926 !$#accession A00430 !'##molecule_type DNA !'##residues 1-97 ##label BIB !'##cross-references GB:J01420; NID:g342520; PIDN:AAB48652.1; !1PID:g896299; EMBL:V00711; NID:g13838; PID:g13847 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 4L KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 97 #molecular-weight 10493 #checksum 3116 SEQUENCE /// ENTRY QXXL4L #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 4L - African clawed frog mitochondrion ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 4L ORGANISM #formal_name mitochondrion Xenopus laevis #common_name African clawed frog DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 03-Jun-2002 ACCESSIONS A00431 REFERENCE A00155 !$#authors Roe, B.A.; Ma, D.P.; Wilson, R.K.; Wong, J.F.H. !$#journal J. Biol. Chem. (1985) 260:9759-9774 !$#title The complete nucleotide sequence of the Xenopus laevis !1mitochondrial genome. !$#cross-references MUID:85261388; PMID:4019494 !$#accession A00431 !'##molecule_type DNA !'##residues 1-98 ##label ROE !'##cross-references GB:M10217; GB:X01600; GB:X01601; GB:X02890; !1NID:g343717; PIDN:AAA66466.1; PID:g807690 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 4L KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 98 #molecular-weight 10710 #checksum 2024 SEQUENCE /// ENTRY DENTNL #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 4L - common tobacco chloroplast ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 4L; ndh4L protein ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 03-Jun-2002 ACCESSIONS A00433 REFERENCE A00149 !$#authors Sugiura, M. !$#submission submitted to the EMBL Data Library, August 1986 !$#accession A00433 !'##molecule_type DNA !'##residues 1-101 ##label SUG !'##experimental_source cv. Bright Yellow 4 REFERENCE A38013 !$#authors Shinozaki, K.; Ohme, M.; Tanaka, M.; Wakasugi, T.; !1Hayashida, N.; Matsubayashi, T.; Zaita, N.; Chunwongse, J.; !1Obokata, J.; Yamaguchi-Shinozaki, K.; Ohto, C.; Torazawa, !1K.; Meng, B.Y.; Sugita, M.; Deno, H.; Kamogashira, T.; !1Yamada, K.; Kusuda, J.; Takaiwa, F.; Kato, A.; Tohdoh, N.; !1Shimada, H.; Sugiura, M. !$#journal EMBO J. (1986) 5:2043-2049 !$#title The complete nucleotide sequence of the tobacco chloroplast !1genome: its gene organization and expression. !$#contents annotation; gene organization, sites, features GENETICS !$#gene ndh4L; ndhE !$#genome chloroplast CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 4L KEYWORDS chloroplast; membrane-associated complex; NAD; !1oxidoreductase SUMMARY #length 101 #molecular-weight 11270 #checksum 2083 SEQUENCE /// ENTRY DERZNL #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 4L - rice chloroplast ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 4L; ndh4L protein ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 03-Jun-2002 ACCESSIONS JQ0291; S05170 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0291 !'##molecule_type DNA !'##residues 1-101 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05170 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-101 ##label HIR !'##cross-references EMBL:X15901; NID:g11957; PIDN:CAA33955.1; !1PID:g12052 !'##experimental_source cv. Nihonbare GENETICS !$#gene ndhE !$#map_position CP109017-108712 !$#genome chloroplast CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 4L KEYWORDS chloroplast; membrane-associated complex; NAD; !1oxidoreductase SUMMARY #length 101 #molecular-weight 11337 #checksum 2572 SEQUENCE /// ENTRY QXZM4L #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 4L - maize chloroplast ORGANISM #formal_name chloroplast Zea mays #common_name maize DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 03-Jun-2002 ACCESSIONS JU0010; S58617 REFERENCE JU0008 !$#authors Schantz, R.; Bogorad, L. !$#journal Plant Mol. Biol. (1988) 11:239-247 !$#title Maize chloroplast genes ndhD, ndhE, and psaC. Sequences, !1transcripts and transcript pools. !$#accession JU0010 !'##molecule_type DNA !'##residues 1-101 ##label SCH !'##cross-references GB:X13159; NID:g12421; PIDN:CAA31556.1; PID:g12422 REFERENCE S58531 !$#authors Maier, R.M.; Neckermann, K.; Igloi, G.L.; Koessel, H. !$#journal J. Mol. Biol. (1995) 251:614-628 !$#title Complete sequence of the maize chloroplast genome: gene !1content, hotspots of divergence and fine tuning of genetic !1information by transcript editing. !$#cross-references MUID:95395841; PMID:7666415 !$#accession S58617 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-101 ##label MAI !'##cross-references EMBL:X86563; NID:g902200; PIDN:CAA60350.1; !1PID:g902286 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1995 GENETICS !$#gene ndhE !$#genome chloroplast CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 4L KEYWORDS chloroplast; membrane-associated complex; NAD; !1oxidoreductase SUMMARY #length 101 #molecular-weight 11356 #checksum 2622 SEQUENCE /// ENTRY DELVNL #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 4L - liverwort (Marchantia polymorpha) chloroplast ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 4L; ndh4L protein ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 03-Jun-2002 ACCESSIONS A00432; S01526 REFERENCE A00150 !$#authors Ohyama, K. !$#submission submitted to the EMBL Data Library, October 1986 !$#accession A00432 !'##molecule_type DNA !'##residues 1-100 ##label OHY REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features REFERENCE S01512 !$#authors Kohchi, T.; Shirai, H.; Fukuzawa, H.; Sano, T.; Komano, T.; !1Umesono, K.; Inokuchi, H.; Ozeki, H.; Ohyama, K. !$#journal J. Mol. Biol. (1988) 203:353-372 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. IV. Inverted repeat and small single !1copy regions. !$#cross-references MUID:89068688; PMID:3199437 !$#accession S01526 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-100 ##label KOH !'##cross-references GB:X04465; GB:Y00686; NID:g11640; PIDN:CAA28136.1; !1PID:g11725 GENETICS !$#gene ndh4L; ndhE !$#genome chloroplast CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 4L KEYWORDS chloroplast; membrane-associated complex; NAD; !1oxidoreductase SUMMARY #length 100 #molecular-weight 11197 #checksum 7187 SEQUENCE /// ENTRY QXYB4L #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 4L - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Jun-2002 ACCESSIONS S27975; S76035; S14966; S18049 REFERENCE S27972 !$#authors Ellersiek, U.; Steinmueller, K. !$#journal Plant Mol. Biol. (1992) 20:1097-1110 !$#title Cloning and transcription analysis of the ndh(A-I-G-E) gene !1cluster and the ndhD gene of the cyanobacterium !1Synechocystis sp. PCC6803. !$#cross-references MUID:93099260; PMID:1463844 !$#accession S27975 !'##molecule_type DNA !'##residues 1-103 ##label ELL !'##cross-references EMBL:X62517; NID:g47554; PIDN:CAA44377.1; !1PID:g47558 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76035 !'##status preliminary !'##molecule_type DNA !'##residues 1-103 ##label KAN !'##cross-references EMBL:D64006; GB:AB001339; NID:g1001291; !1PIDN:BAA10882.1; PID:g1001392 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 REFERENCE S14966 !$#authors Anderson, S.L.; McIntosh, L. !$#journal Plant Mol. Biol. (1991) 16:487-499 !$#title Partial conservation of the 5' ndhE-psaC-ndhD 3' gene !1arrangement of chloroplasts in the cyanobacterium !1Synechocystis sp. PCC 6803: implications for NDH-D function !1in cyanobacteria and chloroplasts. !$#cross-references MUID:91329685; PMID:1907869 !$#accession S14966 !'##molecule_type DNA !'##residues 'R',24-28,'M',30-31,'A',33-34,'CL',37-38,'I',40-44,'M',46, !1'FVT',50-51,'DFF',55,'N',57,'QLK',61,'EI',64,'C',66-69,'A', !171-77,'I',79-83,'SS',86-90,'KSIRIN',97,'ST',100-101,'NK' !1##label AND !'##cross-references EMBL:X53842; NID:g47594; PIDN:CAA37835.1; !1PID:g47595 !'##experimental_source PCC 6803 !'##note this sequence was not reported in the complete genome; the !1sequence is similar to a sequence translated from the common !1tobacco chloroplast (see PIR:DENTNL) GENETICS !$#gene ndhE CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 4L KEYWORDS membrane-associated complex; NAD; oxidoreductase SUMMARY #length 103 #molecular-weight 11463 #checksum 8762 SEQUENCE /// ENTRY DNHUN4 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 4 - human mitochondrion ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 4 ORGANISM #formal_name mitochondrion Homo sapiens #common_name man DATE 22-May-1981 #sequence_revision 23-Oct-1981 #text_change 03-Jun-2002 ACCESSIONS A00434; B00435 REFERENCE A00151 !$#authors Anderson, S.; Bankier, A.T.; Barrell, B.G.; de Bruijn, !1M.H.L.; Coulson, A.R.; Drouin, J.; Eperon, I.C.; Nierlich, !1D.P.; Roe, B.A.; Sanger, F.; Schreier, P.H.; Smith, A.J.H.; !1Staden, R.; Young, I.G. !$#journal Nature (1981) 290:457-465 !$#title Sequence and organization of the human mitochondrial genome. !$#cross-references MUID:81173052; PMID:7219534 !$#accession A00434 !'##molecule_type DNA !'##residues 1-459 ##label AND !'##cross-references GB:J01415; GB:M12548; GB:M58503; GB:M63932; !1GB:M63933; NID:g1944628; PIDN:AAB58952.1; PID:g506833; !1GB:V00662; NID:g13003; GSPDB:GN00100 REFERENCE A00435 !$#authors Brown, W.M.; Prager, E.M.; Wang, A.; Wilson, A.C. !$#journal J. Mol. Evol. (1982) 18:225-239 !$#title Mitochondrial DNA sequences of primates: tempo and mode of !1evolution. !$#cross-references MUID:82242101; PMID:6284948 !$#accession B00435 !'##molecule_type DNA !'##residues 308-459 ##label BRO !'##cross-references GB:L00016; EMBL:V00658; NID:g337302 !'##note this ORF is not annotated in GenBank entry HUMMTTRPR, release !1106 GENETICS !$#gene GDB:MTND4 !'##cross-references GDB:118914; OMIM:516003 !$#map_position MTH10760-12137 !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 4 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 459 #molecular-weight 51580 #checksum 1574 SEQUENCE /// ENTRY QXGI4M #type fragment TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 4 - common gibbon mitochondrion (fragment) ORGANISM #formal_name mitochondrion Hylobates lar #common_name common gibbon, white-handed gibbon DATE 17-Dec-1982 #sequence_revision 26-Aug-1999 #text_change 03-Jun-2002 ACCESSIONS T11842; A00438 REFERENCE Z17353 !$#authors Arnason, U.; Gullberg, A.; Xu, X. !$#journal Hereditas (1996) 124:185-189 !$#title A complete mitochondrial DNA molecule of the white-handed !1gibbon, Hylobates lar, and comparison among individual !1mitochondrial genes of all hominoid genera. !$#accession T11842 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-459 ##label ARN !'##cross-references EMBL:X99256; PIDN:CAA67637.1 !'##experimental_source isolate Ester REFERENCE A00435 !$#authors Brown, W.M.; Prager, E.M.; Wang, A.; Wilson, A.C. !$#journal J. Mol. Evol. (1982) 18:225-239 !$#title Mitochondrial DNA sequences of primates: tempo and mode of !1evolution. !$#cross-references MUID:82242101; PMID:6284948 !$#accession A00438 !'##molecule_type DNA !'##residues 308-459 ##label BRO !'##cross-references GB:V00659; NID:g12996; PIDN:CAB51360.1; !1PID:g5579007 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 !$#note NADH4 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 4 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 459 #checksum 9688 SEQUENCE /// ENTRY QXBO4M #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 4 - bovine mitochondrion ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 4 ORGANISM #formal_name mitochondrion Bos primigenius taurus #common_name cattle DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 03-Jun-2002 ACCESSIONS A00439 REFERENCE A00152 !$#authors Anderson, S.; de Bruijn, M.H.L.; Coulson, A.R.; Eperon, !1I.C.; Sanger, F.; Young, I.G. !$#journal J. Mol. Biol. (1982) 156:683-717 !$#title Complete sequence of bovine mitochondrial DNA. Conserved !1features of the mammalian mitochondrial genome. !$#cross-references MUID:83010260; PMID:7120390 !$#accession A00439 !'##molecule_type DNA !'##residues 1-459 ##label AND !'##cross-references GB:J01394; NID:g336430; PIDN:AAB59277.1; !1PID:g506806; EMBL:V00654; NID:g12800; PID:g12810 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 4 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 459 #molecular-weight 52098 #checksum 7669 SEQUENCE /// ENTRY QXMS4M #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 4 - mouse mitochondrion ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 4 ORGANISM #formal_name mitochondrion Mus musculus #common_name house mouse DATE 02-Apr-1982 #sequence_revision 02-Apr-1982 #text_change 03-Jun-2002 ACCESSIONS A00440 REFERENCE A00153 !$#authors Bibb, M.J.; Van Etten, R.A.; Wright, C.T.; Walberg, M.W.; !1Clayton, D.A. !$#journal Cell (1981) 26:167-180 !$#title Sequence and gene organization of mouse mitochondrial DNA. !$#cross-references MUID:82137051; PMID:7332926 !$#accession A00440 !'##molecule_type DNA !'##residues 1-459 ##label BIB !'##cross-references GB:J01420; NID:g342520; PIDN:AAB48653.1; !1PID:g488495; EMBL:V00711; NID:g13838; PID:g13848 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 4 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 459 #molecular-weight 51881 #checksum 8265 SEQUENCE /// ENTRY QXXL4M #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 4 - African clawed frog mitochondrion ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 4 ORGANISM #formal_name mitochondrion Xenopus laevis #common_name African clawed frog DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 03-Jun-2002 ACCESSIONS A00441 REFERENCE A00155 !$#authors Roe, B.A.; Ma, D.P.; Wilson, R.K.; Wong, J.F.H. !$#journal J. Biol. Chem. (1985) 260:9759-9774 !$#title The complete nucleotide sequence of the Xenopus laevis !1mitochondrial genome. !$#cross-references MUID:85261388; PMID:4019494 !$#accession A00441 !'##molecule_type DNA !'##residues 1-461 ##label ROE !'##cross-references GB:M10217; GB:X01600; GB:X01601; GB:X02890; !1NID:g343717; PIDN:AAA66467.1; PID:g807691 !'##note the authors translated the codon ATC for residue 186 as Thr GENETICS !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 4 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 461 #molecular-weight 52043 #checksum 1640 SEQUENCE /// ENTRY QXASM4 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 4 - Aspergillus amstelodami mitochondrion ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 4 ORGANISM #formal_name mitochondrion Aspergillus amstelodami DATE 14-Nov-1983 #sequence_revision 03-Aug-1984 #text_change 03-Jun-2002 ACCESSIONS A00442 REFERENCE A94634 !$#authors Lazarus, C.M.; Kuntzel, H. !$#submission submitted to the Protein Sequence Database, March 1984 !$#accession A00442 !'##molecule_type DNA !'##residues 1-488 ##label LAZ GENETICS !$#genome mitochondrion !$#genetic_code SGC3 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 4 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 488 #molecular-weight 54298 #checksum 7450 SEQUENCE /// ENTRY S02153 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 4 - Podospora anserina mitochondrion ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 4 ORGANISM #formal_name mitochondrion Podospora anserina DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S02153 REFERENCE S02153 !$#authors Cummings, D.J.; Domenico, J.M. !$#journal J. Mol. Biol. (1988) 204:815-839 !$#title Sequence analysis of mitochondrial DNA from Podospora !1anserina. Pervasiveness of a class I intron in three !1separate genes. !$#cross-references MUID:89125610; PMID:2975708 !$#accession S02153 !'##molecule_type DNA !'##residues 1-519 ##label CUM !'##cross-references EMBL:X14484; NID:g13300; PIDN:CAA32645.1; !1PID:g295784 GENETICS !$#gene ND4 !$#genome mitochondrion !$#genetic_code SGC3 !$#introns 203/1 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 4 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 519 #molecular-weight 57611 #checksum 1294 SEQUENCE /// ENTRY QXAS4M #type fragment TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 4 - Emericella nidulans mitochondrion (fragment) ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 4 ORGANISM #formal_name mitochondrion Emericella nidulans, Aspergillus nidulans DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 03-Jun-2002 ACCESSIONS A00443 REFERENCE A93436 !$#authors Netzker, R.; Kochel, H.G.; Basak, N.; Kuntzel, H. !$#journal Nucleic Acids Res. (1982) 10:4783-4794 !$#title Nucleotide sequence of Aspergillus nidulans mitochondrial !1genes coding for ATPase subunit 6, cytochrome oxidase !1subunit 3, seven unidentified proteins, four tRNAs and !1L-rRNA. !$#cross-references MUID:83038633; PMID:6290989 !$#accession A00443 !'##molecule_type DNA !'##residues 1-221 ##label NET !'##cross-references GB:J01390; NID:g336905; PIDN:AAA99203.1; !1PID:g472819 !'##experimental_source imperfect stage GENETICS !$#genome mitochondrion !$#genetic_code SGC3 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 4 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 221 #checksum 9648 SEQUENCE /// ENTRY DENTN4 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 4 - common tobacco chloroplast ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 4; ndh4 protein ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 03-Jun-2002 ACCESSIONS A00444 REFERENCE A00149 !$#authors Sugiura, M. !$#submission submitted to the EMBL Data Library, August 1986 !$#accession A00444 !'##molecule_type DNA !'##residues 1-509 ##label SUG !'##experimental_source cv. Bright Yellow 4 REFERENCE A38013 !$#authors Shinozaki, K.; Ohme, M.; Tanaka, M.; Wakasugi, T.; !1Hayashida, N.; Matsubayashi, T.; Zaita, N.; Chunwongse, J.; !1Obokata, J.; Yamaguchi-Shinozaki, K.; Ohto, C.; Torazawa, !1K.; Meng, B.Y.; Sugita, M.; Deno, H.; Kamogashira, T.; !1Yamada, K.; Kusuda, J.; Takaiwa, F.; Kato, A.; Tohdoh, N.; !1Shimada, H.; Sugiura, M. !$#journal EMBO J. (1986) 5:2043-2049 !$#title The complete nucleotide sequence of the tobacco chloroplast !1genome: its gene organization and expression. !$#contents annotation; gene organization, sites, features GENETICS !$#gene ndh4; ndhD !$#genome chloroplast CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 4 KEYWORDS chloroplast; membrane-associated complex; NAD; !1oxidoreductase SUMMARY #length 509 #molecular-weight 57401 #checksum 8354 SEQUENCE /// ENTRY DELVN4 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 4 - liverwort (Marchantia polymorpha) chloroplast ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 4; ndh4 protein ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 03-Jun-2002 ACCESSIONS A00445; S01528 REFERENCE A00150 !$#authors Ohyama, K. !$#submission submitted to the EMBL Data Library, October 1986 !$#accession A00445 !'##molecule_type DNA !'##residues 1-499 ##label OHY REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features REFERENCE S01512 !$#authors Kohchi, T.; Shirai, H.; Fukuzawa, H.; Sano, T.; Komano, T.; !1Umesono, K.; Inokuchi, H.; Ozeki, H.; Ohyama, K. !$#journal J. Mol. Biol. (1988) 203:353-372 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. IV. Inverted repeat and small single !1copy regions. !$#cross-references MUID:89068688; PMID:3199437 !$#accession S01528 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-499 ##label KOH !'##cross-references GB:X04465; GB:Y00686; NID:g11640; PIDN:CAA28134.1; !1PID:g11723 GENETICS !$#gene ndh4; ndhD !$#genome chloroplast CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 4 KEYWORDS chloroplast; membrane-associated complex; NAD; !1oxidoreductase SUMMARY #length 499 #molecular-weight 56666 #checksum 9726 SEQUENCE /// ENTRY DERZN4 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 4 - rice chloroplast ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 4; ndh4 protein ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 03-Jun-2002 ACCESSIONS JQ0289; S05168 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0289 !'##molecule_type DNA !'##residues 1-500 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05168 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-500 ##label HIR !'##cross-references EMBL:X15901; NID:g11957; PIDN:CAA33953.1; !1PID:g12050 !'##experimental_source cv. Nihonbare GENETICS !$#gene ndhD !$#map_position CP107900-106398 !$#genome chloroplast CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 4 KEYWORDS chloroplast; membrane-associated complex; NAD; !1oxidoreductase SUMMARY #length 500 #molecular-weight 56506 #checksum 4858 SEQUENCE /// ENTRY QXZM4 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 4 - maize chloroplast ALTERNATE_NAMES ndhD protein ORGANISM #formal_name chloroplast Zea mays #common_name maize DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 03-Jun-2002 ACCESSIONS JU0009; S58615; S58616 REFERENCE JU0008 !$#authors Schantz, R.; Bogorad, L. !$#journal Plant Mol. Biol. (1988) 11:239-247 !$#title Maize chloroplast genes ndhD, ndhE, and psaC. Sequences, !1transcripts and transcript pools. !$#accession JU0009 !'##molecule_type DNA !'##residues 1-515 ##label SCH !'##cross-references GB:X13159; NID:g12421; PIDN:CAA31558.1; PID:g12424 REFERENCE S58531 !$#authors Maier, R.M.; Neckermann, K.; Igloi, G.L.; Koessel, H. !$#journal J. Mol. Biol. (1995) 251:614-628 !$#title Complete sequence of the maize chloroplast genome: gene !1content, hotspots of divergence and fine tuning of genetic !1information by transcript editing. !$#cross-references MUID:95395841; PMID:7666415 !$#accession S58615 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 16-223,'W',225-486,'V',488-515 ##label MAI !'##cross-references EMBL:X86563; NID:g902200; PIDN:CAA60349.1; !1PID:g902285 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1995 GENETICS !$#gene ndhD !$#genome chloroplast CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 4 KEYWORDS chloroplast; membrane-associated complex; NAD; !1oxidoreductase SUMMARY #length 515 #molecular-weight 58166 #checksum 9562 SEQUENCE /// ENTRY S28891 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 4 - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 03-Jun-2002 ACCESSIONS S28891; S76059; S20681 REFERENCE S27972 !$#authors Ellersiek, U.; Steinmueller, K. !$#journal Plant Mol. Biol. (1992) 20:1097-1110 !$#title Cloning and transcription analysis of the ndh(A-I-G-E) gene !1cluster and the ndhD gene of the cyanobacterium !1Synechocystis sp. PCC6803. !$#cross-references MUID:93099260; PMID:1463844 !$#accession S28891 !'##molecule_type DNA !'##residues 1-525 ##label ELL !'##cross-references EMBL:X65170; NID:g47600; PIDN:CAA46289.1; !1PID:g47602 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76059 !'##status preliminary !'##molecule_type DNA !'##residues 1-525 ##label KAN !'##cross-references EMBL:D63999; GB:AB001339; NID:g1001396; !1PIDN:BAA10037.1; PID:g1001415 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 4 KEYWORDS membrane-associated complex; NAD; oxidoreductase SUMMARY #length 525 #molecular-weight 57510 #checksum 1636 SEQUENCE /// ENTRY S53834 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 4 - Acanthamoeba castellanii mitochondrion ORGANISM #formal_name mitochondrion Acanthamoeba castellanii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S53834 REFERENCE S53825 !$#authors Burger, G.; Plante, I.; Lonergan, K.M.; Gray, M.W. !$#journal J. Mol. Biol. (1995) 245:522-537 !$#title The mitochondrial DNA of the amoeboid protozoon, !1Acanthamoeba castellanii: complete sequence, gene content !1and genome organization. !$#cross-references MUID:95147275; PMID:7844823 !$#accession S53834 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-497 ##label BUR !'##cross-references GB:U12386; NID:g562028; PIDN:AAD11826.1; !1PID:g562038 !'##experimental_source strain Neff; ATCC 30010 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1994 GENETICS !$#genome mitochondrion !$#genetic_code SGC6 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 4 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 497 #molecular-weight 57768 #checksum 316 SEQUENCE /// ENTRY S16447 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 4 - wheat mitochondrion ALTERNATE_NAMES mitochondrial complex I subunit IV ORGANISM #formal_name mitochondrion Triticum aestivum #common_name common wheat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S16447; S16448; S06835 REFERENCE S16447 !$#authors Lamattina, L.; Grienenberger, J.M. !$#journal Nucleic Acids Res. (1991) 19:3275-3282 !$#title RNA editing of the transcript coding for subunit 4 of NADH !1dehydrogenase in wheat mitochondria: uneven distribution of !1the editing sites among the four exons. !$#cross-references MUID:91288205; PMID:1712098 !$#accession S16447 !'##molecule_type mRNA !'##residues 1-495 ##label LAM !'##cross-references EMBL:X57163 !'##note the authors translated the codon CGT for residue 418 as Ala !$#accession S16448 !'##molecule_type DNA !'##residues 1-14,'P',16-24,'TP',27-35,'P',37-51,'PP',54,'PR',57-65,'S', !167-105,'S',107-120,'T',122-125,'R',127-133,'S',135-138,'P', !1140-144,'LS',147-149,'P',151-325,'P',327-457,'S',459-468, !1'R',470-472,'H',474-477,'P',479-495 ##label LAF !'##cross-references EMBL:X57164; NID:g21823; PIDN:CAA40453.1; !1PID:g21824 !'##note the authors translated the codon CGT for residue 418 as Ala !'##note 15-P, 25-Thr, 26-Pro, 36-Pro, 52-Pro, 53-Pro, 55-Pro, 56-Arg, !166-Ser, 106-Ser, 121-Thr, 126-Arg, 134-Ser, 139-Pro, !1145-Leu, 146-Ser, 150-Pro, 326-Pro, 458-Ser, 469-Arg, !1473-His, and 478-Pro are due to RNA editing REFERENCE S06835 !$#authors Lamattina, L.; Weil, J.H.; Grienenberger, J.M. !$#journal FEBS Lett. (1989) 258:79-83 !$#title RNA editing at a splicing site of NADH dehydrogenase subunit !1IV gene transcript in wheat mitochondria. !$#cross-references MUID:90076495; PMID:2687023 !$#accession S06835 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 295-346 ##label LAW GENETICS !$#gene nad4 !$#genome mitochondrion !$#introns 154/2; 326/1; 467/1 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 4 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain; RNA !1editing SUMMARY #length 495 #molecular-weight 55897 #checksum 3012 SEQUENCE /// ENTRY S25942 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 4 - liverwort (Marchantia polymorpha) mitochondrion ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 4 ORGANISM #formal_name mitochondrion Marchantia polymorpha DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S25942; S31172 REFERENCE S25941 !$#authors Oda, K.; Yamato, K.; Ohta, E.; Nakamura, Y.; Takemura, M.; !1Nozato, N.; Akashi, K.; Kanegae, T.; Ogura, Y.; Kohchi, T.; !1Ohyama, K. !$#journal J. Mol. Biol. (1992) 223:1-7 !$#title Gene organization deduced from the complete sequence of !1liverwort Marchantia polymorpha mitochondrial DNA. A !1primitive form of plant mitochondrial genome. !$#cross-references MUID:92114051; PMID:1731062 !$#accession S25942 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-495 ##label ODA !'##cross-references EMBL:M68929; NID:g786182; PIDN:AAC09398.1; !1PID:g786185 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1February 1992 REFERENCE S31171 !$#authors Nozato, N.; Oda, K.; Yamato, K.; Ohta, E.; Takemura, M.; !1Akashi, K.; Fukuzawa, H.; Ohyama, K. !$#journal Mol. Gen. Genet. (1993) 237:343-350 !$#title Cotranscriptional expression of mitochondrial genes for !1subunits of NADH dehydrogenase, nad5, nad4, nad2, in !1Marchantia polymorpha. !$#cross-references MUID:93247547; PMID:8483448 !$#accession S31172 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-495 ##label NOZ !'##cross-references EMBL:M68929; NID:g786182; PIDN:AAC09398.1; !1PID:g786185 GENETICS !$#gene nad4 !$#genome mitochondrion !$#introns 183/2 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 4 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 495 #molecular-weight 56311 #checksum 4541 SEQUENCE /// ENTRY S26870 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 4 - field mustard mitochondrion ORGANISM #formal_name mitochondrion Brassica campestris #common_name field mustard DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S26870; S21869 REFERENCE S26870 !$#authors Gass, D.A.; Makaroff, C.A.; Palmer, J.D. !$#journal Curr. Genet. (1992) 21:423-430 !$#title Variable intron content of the NADH dehydrogenase subunit 4 !1gene of plant mitochondria. !$#cross-references MUID:92405241; PMID:1525869 !$#accession S26870 !'##molecule_type DNA !'##residues 1-495 ##label GAS !'##cross-references EMBL:X60794; NID:g12769; PIDN:CAA43207.1; !1PID:g12770 !'##note the authors translated the codon CTC for residue 467 as Val GENETICS !$#gene nad4 !$#genome mitochondrion !$#introns 154/2; 326/1; 466/3 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 4 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 495 #molecular-weight 55200 #checksum 5160 SEQUENCE /// ENTRY DNHUN5 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 5 - human mitochondrion ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 5 ORGANISM #formal_name mitochondrion Homo sapiens #common_name man DATE 22-May-1981 #sequence_revision 23-Oct-1981 #text_change 03-Jun-2002 ACCESSIONS A00446; C00435; I80239 REFERENCE A00151 !$#authors Anderson, S.; Bankier, A.T.; Barrell, B.G.; de Bruijn, !1M.H.L.; Coulson, A.R.; Drouin, J.; Eperon, I.C.; Nierlich, !1D.P.; Roe, B.A.; Sanger, F.; Schreier, P.H.; Smith, A.J.H.; !1Staden, R.; Young, I.G. !$#journal Nature (1981) 290:457-465 !$#title Sequence and organization of the human mitochondrial genome. !$#cross-references MUID:81173052; PMID:7219534 !$#accession A00446 !'##molecule_type DNA !'##residues 1-603 ##label AND !'##cross-references GB:J01415; NID:g1944628; PIDN:AAB58953.1; !1PID:g2052366; EMBL:V00662; NID:g13003; PID:g13014; !1GSPDB:GN00100 REFERENCE A00435 !$#authors Brown, W.M.; Prager, E.M.; Wang, A.; Wilson, A.C. !$#journal J. Mol. Evol. (1982) 18:225-239 !$#title Mitochondrial DNA sequences of primates: tempo and mode of !1evolution. !$#cross-references MUID:82242101; PMID:6284948 !$#accession C00435 !'##molecule_type DNA !'##residues 1-79 ##label BRO !'##cross-references GB:L00016; EMBL:V00658; NID:g337302 !'##note this ORF is not annotated in GenBank entry HUMMTTRPR, release !1106 REFERENCE I59384 !$#authors Horai, S.; Hayasaka, K.; Kondo, R.; Tsugane, K.; Takahata, !1N. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1995) 92:532-536 !$#title Recent African origin of modern humans revealed by complete !1sequences of hominoid mitochondrial DNAs. !$#cross-references MUID:95132634; PMID:7530363 !$#accession I80239 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-210,'P',212-256,'V',258-313,'V',315-455,'R',457-603 !1##label HOR !'##cross-references DDBJ:D38112; NID:g644480; PIDN:BAA07297.1; !1PID:g704447 !'##experimental_source African isolate SB17 GENETICS !$#gene GDB:MTND5 !'##cross-references GDB:118916; OMIM:516005 !$#map_position MTH12337-14148 !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 5 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 603 #molecular-weight 66927 #checksum 6628 SEQUENCE /// ENTRY QXBO5M #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 5 - bovine mitochondrion ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 5 ORGANISM #formal_name mitochondrion Bos primigenius taurus #common_name cattle DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 03-Jun-2002 ACCESSIONS A00450 REFERENCE A00152 !$#authors Anderson, S.; de Bruijn, M.H.L.; Coulson, A.R.; Eperon, !1I.C.; Sanger, F.; Young, I.G. !$#journal J. Mol. Biol. (1982) 156:683-717 !$#title Complete sequence of bovine mitochondrial DNA. Conserved !1features of the mammalian mitochondrial genome. !$#cross-references MUID:83010260; PMID:7120390 !$#accession A00450 !'##molecule_type DNA !'##residues 1-606 ##label AND !'##cross-references GB:J01394; NID:g336430; PIDN:AAB59278.1; !1PID:g336441; EMBL:V00654; NID:g12800; PID:g12811 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 5 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 606 #molecular-weight 68313 #checksum 2794 SEQUENCE /// ENTRY QXMS5M #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 5 - mouse mitochondrion ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 5 ORGANISM #formal_name mitochondrion Mus musculus #common_name house mouse DATE 02-Apr-1982 #sequence_revision 30-Sep-1989 #text_change 03-Jun-2002 ACCESSIONS A00451 REFERENCE A00153 !$#authors Bibb, M.J.; Van Etten, R.A.; Wright, C.T.; Walberg, M.W.; !1Clayton, D.A. !$#journal Cell (1981) 26:167-180 !$#title Sequence and gene organization of mouse mitochondrial DNA. !$#cross-references MUID:82137051; PMID:7332926 !$#accession A00451 !'##molecule_type DNA !'##residues 1-607 ##label BIB !'##cross-references GB:J01420; NID:g342520; PIDN:AAB48654.1; !1PID:g896300; EMBL:V00711; NID:g13838; PID:g578833 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 !$#start_codon ATC CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 5 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 607 #molecular-weight 68440 #checksum 6873 SEQUENCE /// ENTRY QXXL5M #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 5 - African clawed frog mitochondrion ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 5 ORGANISM #formal_name mitochondrion Xenopus laevis #common_name African clawed frog DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 03-Jun-2002 ACCESSIONS A00452 REFERENCE A00155 !$#authors Roe, B.A.; Ma, D.P.; Wilson, R.K.; Wong, J.F.H. !$#journal J. Biol. Chem. (1985) 260:9759-9774 !$#title The complete nucleotide sequence of the Xenopus laevis !1mitochondrial genome. !$#cross-references MUID:85261388; PMID:4019494 !$#accession A00452 !'##molecule_type DNA !'##residues 1-604 ##label ROE !'##cross-references GB:M10217; GB:X01600; GB:X01601; GB:X02890; !1NID:g343717; PIDN:AAA66468.1; PID:g807692 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 5 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 604 #molecular-weight 67155 #checksum 3850 SEQUENCE /// ENTRY DNMUU5 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 5 - Arabidopsis thaliana mitochondrion ORGANISM #formal_name mitochondrion Arabidopsis thaliana #common_name mouse-ear cress DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 03-Jun-2002 ACCESSIONS S20234; S17797 REFERENCE S17797 !$#authors Knoop, V.; Schuster, W.; Wissinger, B.; Brennicke, A. !$#journal EMBO J. (1991) 10:3483-3493 !$#title Trans splicing integrates an exon of 22 nucleotides into the !1nad5 mRNA in higher plant mitochondria. !$#cross-references MUID:92007799; PMID:1915303 !$#accession S20234 !'##molecule_type mRNA !'##residues 1-669 ##label KNO1 !'##cross-references EMBL:X60047 !$#accession S17797 !'##molecule_type DNA !'##residues 1-497,'P',499-516,'T',518-526,'S',528-631,'S',633-638,'SR', !1641-652,'S',654-669 ##label KNO2 !'##cross-references EMBL:X60047 !'##note differences from the sequence translated from mRNA are due to !1RNA editing GENETICS !$#gene nad5 !$#genome mitochondrion !$#introns 77/2; 482/3; 490/1; 621/3 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 5 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain; RNA !1editing SUMMARY #length 669 #molecular-weight 74021 #checksum 8623 SEQUENCE /// ENTRY S25941 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 5 - liverwort (Marchantia polymorpha) mitochondrion ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 5 ORGANISM #formal_name mitochondrion Marchantia polymorpha DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S25941; S31171 REFERENCE S25941 !$#authors Oda, K.; Yamato, K.; Ohta, E.; Nakamura, Y.; Takemura, M.; !1Nozato, N.; Akashi, K.; Kanegae, T.; Ogura, Y.; Kohchi, T.; !1Ohyama, K. !$#journal J. Mol. Biol. (1992) 223:1-7 !$#title Gene organization deduced from the complete sequence of !1liverwort Marchantia polymorpha mitochondrial DNA. A !1primitive form of plant mitochondrial genome. !$#cross-references MUID:92114051; PMID:1731062 !$#accession S25941 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-669 ##label ODA !'##cross-references EMBL:M68929; NID:g786182; PIDN:AAC09397.1; !1PID:g786184 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1February 1992 REFERENCE S31171 !$#authors Nozato, N.; Oda, K.; Yamato, K.; Ohta, E.; Takemura, M.; !1Akashi, K.; Fukuzawa, H.; Ohyama, K. !$#journal Mol. Gen. Genet. (1993) 237:343-350 !$#title Cotranscriptional expression of mitochondrial genes for !1subunits of NADH dehydrogenase, nad5, nad4, nad2, in !1Marchantia polymorpha. !$#cross-references MUID:93247547; PMID:8483448 !$#accession S31171 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-669 ##label NOZ !'##cross-references EMBL:M68929; NID:g786182; PIDN:AAC09397.1; !1PID:g786184 GENETICS !$#gene nad5 !$#genome mitochondrion !$#introns 251/3 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 5 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 669 #molecular-weight 74678 #checksum 2039 SEQUENCE /// ENTRY DNOBU5 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 5 - evening primrose mitochondrion ORGANISM #formal_name mitochondrion Oenothera villaricae #common_name evening primrose DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 03-Jun-2002 ACCESSIONS S20236; S20237; S20235; S17798; S03125 REFERENCE S03125 !$#authors Wissinger, B.; Hiesel, R.; Schuster, W.; Brennicke, A. !$#journal Mol. Gen. Genet. (1988) 212:56-65 !$#title The NADH-dehydrogenase subunit 5 gene in Oenothera !1mitochondria contains two introns and is co-transcribed with !1the 5 S rRNA gene. !$#cross-references MUID:88232433; PMID:3163767 !$#accession S20236 !'##molecule_type mRNA !'##residues 1-482 ##label WIS1 !'##cross-references EMBL:X07566 !$#accession S20237 !'##molecule_type DNA !'##residues 1-51,'P',53-80,'P',82-90,'S',92-119,'L',121-132,'S', !1134-164,'T',166-168,'P',170-179,'P',181-182,'S',184,'R', !1186-199,'R',201-237,'S',239-241,'S',243-278,'P',280-287,'S', !1289-291,'T',293-466,'S',468-482 ##label WIS2 !'##note the authors translated the codon CGG for residue 366 as Trp, !1assuming a special genetic code for plant mitochondria !'##note the carboxyl end of the sequence shown in reference S03125 has !1been revised in reference S17797 REFERENCE S17797 !$#authors Knoop, V.; Schuster, W.; Wissinger, B.; Brennicke, A. !$#journal EMBO J. (1991) 10:3483-3493 !$#title Trans splicing integrates an exon of 22 nucleotides into the !1nad5 mRNA in higher plant mitochondria. !$#cross-references MUID:92007799; PMID:1915303 !$#accession S20235 !'##molecule_type mRNA !'##residues 483-670 ##label KNO1 !'##cross-references EMBL:X60046 !$#accession S17798 !'##molecule_type DNA !'##residues 483-492,'PL',495-516,'T',518-522,'P',524-526,'S',528-529, !1'S',531-536,'P',538-638,'SR',641-670 ##label KNO2 GENETICS !$#gene nad5; ndh5 !$#genome mitochondrion !$#introns 76/3; 482/3; 490/1; 621/3 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 5 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain; RNA !1editing SUMMARY #length 670 #molecular-weight 74583 #checksum 8877 SEQUENCE /// ENTRY DENTN5 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 5 - common tobacco chloroplast ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 5; ndh5 protein ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 30-Jun-1987 #sequence_revision 14-Aug-1998 #text_change 03-Jun-2002 ACCESSIONS S37352; A00454 REFERENCE S37352 !$#authors Olmstead, R.G.; Sweere, J.A.; Wolfe, K.H. !$#journal Plant Mol. Biol. (1993) 22:1191-1193 !$#title Ninety extra nucleotide in ndhF gene of tobacco chloroplast !1DNA: a summary of revisions to the 1986 genome sequence. !$#cross-references MUID:94003079; PMID:8400137 !$#accession S37352 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-740 ##label OLM !'##cross-references GB:L14953; NID:g295333; PIDN:AAA84685.1; !1PID:g295334 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1993 REFERENCE A00149 !$#authors Sugiura, M. !$#submission submitted to the EMBL Data Library, August 1986 !$#accession A00454 !'##molecule_type DNA !'##residues 1-578,609-691,'TD',694-740 ##label SUG !'##experimental_source cv. Bright Yellow 4 REFERENCE A38013 !$#authors Shinozaki, K.; Ohme, M.; Tanaka, M.; Wakasugi, T.; !1Hayashida, N.; Matsubayashi, T.; Zaita, N.; Chunwongse, J.; !1Obokata, J.; Yamaguchi-Shinozaki, K.; Ohto, C.; Torazawa, !1K.; Meng, B.Y.; Sugita, M.; Deno, H.; Kamogashira, T.; !1Yamada, K.; Kusuda, J.; Takaiwa, F.; Kato, A.; Tohdoh, N.; !1Shimada, H.; Sugiura, M. !$#journal EMBO J. (1986) 5:2043-2049 !$#title The complete nucleotide sequence of the tobacco chloroplast !1genome: its gene organization and expression. !$#contents annotation; gene organization, sites, features GENETICS !$#gene ndh5; ndhF !$#genome chloroplast CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 5 KEYWORDS chloroplast; membrane-associated complex; NAD; !1oxidoreductase SUMMARY #length 740 #molecular-weight 83717 #checksum 3049 SEQUENCE /// ENTRY DERZN5 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 5 - rice chloroplast ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 3; ndh3 protein ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 03-Jun-2002 ACCESSIONS JQ0286; S05165 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0286 !'##molecule_type DNA !'##residues 1-734 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05165 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-734 ##label HIR !'##cross-references EMBL:X15901; NID:g11957; PIDN:CAA33950.1; !1PID:g12047 !'##experimental_source cv. Nihonbare GENETICS !$#gene ndhF !$#map_position CP103637-101433 !$#genome chloroplast CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 5 KEYWORDS chloroplast; membrane-associated complex; NAD; !1oxidoreductase SUMMARY #length 734 #molecular-weight 82597 #checksum 5032 SEQUENCE /// ENTRY DELVN5 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 5 - liverwort (Marchantia polymorpha) chloroplast ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 5; ndh5 protein ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 03-Jun-2002 ACCESSIONS A00453; S01512 REFERENCE A00150 !$#authors Ohyama, K. !$#submission submitted to the EMBL Data Library, October 1986 !$#accession A00453 !'##molecule_type DNA !'##residues 1-692 ##label OHY REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features REFERENCE S01512 !$#authors Kohchi, T.; Shirai, H.; Fukuzawa, H.; Sano, T.; Komano, T.; !1Umesono, K.; Inokuchi, H.; Ozeki, H.; Ohyama, K. !$#journal J. Mol. Biol. (1988) 203:353-372 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. IV. Inverted repeat and small single !1copy regions. !$#cross-references MUID:89068688; PMID:3199437 !$#accession S01512 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-692 ##label KOH !'##cross-references GB:X04465; GB:Y00686; NID:g11640; PIDN:CAA28129.1; !1PID:g11718 GENETICS !$#gene ndh5; ndhF !$#genome chloroplast CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 5 KEYWORDS chloroplast; membrane-associated complex; NAD; !1oxidoreductase SUMMARY #length 692 #molecular-weight 79278 #checksum 5386 SEQUENCE /// ENTRY QQUTC5 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 5 - Trypanosoma brucei mitochondrion ORGANISM #formal_name mitochondrion Trypanosoma brucei DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 03-Jun-2002 ACCESSIONS A04519; D22845 REFERENCE A93537 !$#authors Hensgens, L.A.M.; Brakenhoff, J.; De Vries, B.F.; Sloof, P.; !1Tromp, M.C.; Van Boom, J.H.; Benne, R. !$#journal Nucleic Acids Res. (1984) 12:7327-7344 !$#title The sequence of the gene for cytochrome c oxidase subunit I, !1a frameshift containing gene for cytochrome c oxidase !1subunit II and seven unassigned reading frames in !1Trypanosoma brucei mitochondrial maxi-circle DNA. !$#cross-references MUID:85037915; PMID:6093040 !$#accession A04519 !'##molecule_type DNA !'##residues 1-590 ##label HEN !'##cross-references GB:M94286; NID:g343546 !'##note this translation is not annotated in GenBank entry TRBKPGEN, !1release 109.0 COMMENT The DNA sequence is from a segment of the 20-kb maxicircle, !1which is believed to be the trypanosome mitochondrial !1genome. GENETICS !$#genome mitochondrion !$#genetic_code SGC6 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 5 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 590 #molecular-weight 71493 #checksum 7193 SEQUENCE /// ENTRY S34960 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 5 - Crithidia oncopelti mitochondrion ORGANISM #formal_name mitochondrion Crithidia oncopelti DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S34960 REFERENCE S34958 !$#authors Maslov, D.A.; Horvath, A.; Gwang II, K.; Kolesnikov, A.A. !$#submission submitted to the EMBL Data Library, October 1990 !$#accession S34960 !'##molecule_type DNA !'##residues 1-590 ##label MAS !'##cross-references EMBL:X56015; NID:g12879; PIDN:CAA39492.1; !1PID:g12882 GENETICS !$#gene ND5 !$#genome mitochondrion !$#genetic_code SGC6 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 5 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 590 #molecular-weight 71650 #checksum 5000 SEQUENCE /// ENTRY I30010 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 5 - Leishmania tarentolae mitochondrion ORGANISM #formal_name mitochondrion Leishmania tarentolae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS I30010 REFERENCE A22848 !$#authors de la Cruz, V.F.; Neckelmann, N.; Simpson, L. !$#journal J. Biol. Chem. (1984) 259:15136-15147 !$#title Sequences of six genes and several open reading frames in !1the kinetoplast maxicircle DNA of Leishmania tarentolae. !$#cross-references MUID:85079995; PMID:6096360 !$#accession I30010 !'##molecule_type DNA !'##residues 1-502 ##label DEL !'##cross-references GB:M30010 GENETICS !$#genome mitochondrion !$#genetic_code SGC6 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 5 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 502 #molecular-weight 60538 #checksum 3254 SEQUENCE /// ENTRY B24707 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 5 - Chlamydomonas reinhardtii mitochondrion ORGANISM #formal_name mitochondrion Chlamydomonas reinhardtii DATE 25-Jan-1988 #sequence_revision 10-Oct-1997 #text_change 03-Jun-2002 ACCESSIONS B24707; A24611; S28107; S41639; S37610 REFERENCE A24707 !$#authors Boer, P.H.; Gray, M.W. !$#journal Nucleic Acids Res. (1986) 14:7506-7507 !$#title Nucleotide sequence of a protein coding region in !1Chlamydomonas reinhardtii mitochondrial DNA. !$#cross-references MUID:87016388; PMID:3020517 !$#accession B24707 !'##molecule_type DNA !'##residues 1-546 ##label BOE !'##note the assignment of Met-1 as the initiator, rather than some !1codon upstream of Met-1, was based on detailed transcript !1mapping REFERENCE A24611 !$#authors Boer, P.H.; Gray, M.W. !$#journal EMBO J. (1986) 5:21-28 !$#title The URF 5 gene of Chlamydomonas reinhardtii mitochondria: !1DNA sequence and mode of transcription. !$#cross-references MUID:86164259; PMID:3007117 !$#accession A24611 !'##molecule_type DNA !'##residues 1-505,'A',507-546 ##label BO2 REFERENCE S28106 !$#authors Gray, M.W. !$#submission submitted to the EMBL Data Library, October 1990 !$#accession S28107 !'##status preliminary !'##molecule_type DNA !'##residues 'P',1-546 ##label GRA !'##cross-references EMBL:X54860; NID:g12503; PIDN:CAA38641.1; !1PID:g1334383 REFERENCE S41639 !$#authors Michaelis, G. !$#submission submitted to the EMBL Data Library, September 1991 !$#accession S41639 !'##molecule_type DNA !'##residues 'MSSSLVQINELANREISLLFP',1-205,'G',207-291,'I',293-546 !1##label MIC !'##cross-references EMBL:X66484; NID:g12510; PIDN:CAA47113.1; !1PID:g12513 REFERENCE S37609 !$#authors Vahrenholz, C.; Pratje, E.; Michaelis, G.; Dujon, B. !$#journal Mol. Gen. Genet. (1985) 201:213-224 !$#title Mitochondrial DNA of Chlamydomonas reinhardtii: sequence and !1arrangement of URF5 and the gene for cytochrome oxidase !1subunit I. !$#accession S37610 !'##molecule_type DNA !'##residues 'MSSSLVQINELANREISLLFP',1-205,'G',207-291,'I',293-508, !1'GVSINCSLAVQ' ##label VAH !'##cross-references EMBL:X66484 GENETICS !$#gene nad5 !$#genome mitochondrion CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 5 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 546 #molecular-weight 59035 #checksum 2348 SEQUENCE /// ENTRY DEHUN6 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 6 - human mitochondrion ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 6 ORGANISM #formal_name mitochondrion Homo sapiens #common_name man DATE 22-May-1981 #sequence_revision 23-Oct-1981 #text_change 03-Jun-2002 ACCESSIONS A00455; I80240 REFERENCE A00151 !$#authors Anderson, S.; Bankier, A.T.; Barrell, B.G.; de Bruijn, !1M.H.L.; Coulson, A.R.; Drouin, J.; Eperon, I.C.; Nierlich, !1D.P.; Roe, B.A.; Sanger, F.; Schreier, P.H.; Smith, A.J.H.; !1Staden, R.; Young, I.G. !$#journal Nature (1981) 290:457-465 !$#title Sequence and organization of the human mitochondrial genome. !$#cross-references MUID:81173052; PMID:7219534 !$#accession A00455 !'##molecule_type DNA !'##residues 1-174 ##label AND !'##cross-references GB:J01415; NID:g1944628; PIDN:AAB58954.1; !1PID:g2052367; EMBL:V00662; NID:g13003; PID:g13015; !1GSPDB:GN00100 REFERENCE I59384 !$#authors Horai, S.; Hayasaka, K.; Kondo, R.; Tsugane, K.; Takahata, !1N. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1995) 92:532-536 !$#title Recent African origin of modern humans revealed by complete !1sequences of hominoid mitochondrial DNAs. !$#cross-references MUID:95132634; PMID:7530363 !$#accession I80240 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-101,'L',103-133,'L',135-158,'T',160-174 ##label HOR !'##cross-references GB:D38112; NID:g644480; PIDN:BAA07298.1; !1PID:g704448 !'##experimental_source African isolate SB17 GENETICS !$#gene GDB:MTND6 !'##cross-references GDB:118917; OMIM:516006 !$#map_position MTL14673-14149 !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 6 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 174 #molecular-weight 18686 #checksum 4033 SEQUENCE /// ENTRY DEBON6 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 6 - bovine mitochondrion ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 6 ORGANISM #formal_name mitochondrion Bos primigenius taurus #common_name cattle DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 03-Jun-2002 ACCESSIONS A00456 REFERENCE A00152 !$#authors Anderson, S.; de Bruijn, M.H.L.; Coulson, A.R.; Eperon, !1I.C.; Sanger, F.; Young, I.G. !$#journal J. Mol. Biol. (1982) 156:683-717 !$#title Complete sequence of bovine mitochondrial DNA. Conserved !1features of the mammalian mitochondrial genome. !$#cross-references MUID:83010260; PMID:7120390 !$#accession A00456 !'##molecule_type DNA !'##residues 1-175 ##label AND !'##cross-references GB:J01394; NID:g336430; PIDN:AAB59279.1; !1PID:g336442; EMBL:V00654; NID:g12800; PID:g12812 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 6 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 175 #molecular-weight 19078 #checksum 1072 SEQUENCE /// ENTRY DEMSN6 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 6 - mouse mitochondrion ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 6 ORGANISM #formal_name mitochondrion Mus musculus #common_name house mouse DATE 02-Apr-1982 #sequence_revision 02-Apr-1982 #text_change 03-Jun-2002 ACCESSIONS A00457 REFERENCE A00153 !$#authors Bibb, M.J.; Van Etten, R.A.; Wright, C.T.; Walberg, M.W.; !1Clayton, D.A. !$#journal Cell (1981) 26:167-180 !$#title Sequence and gene organization of mouse mitochondrial DNA. !$#cross-references MUID:82137051; PMID:7332926 !$#accession A00457 !'##molecule_type DNA !'##residues 1-172 ##label BIB !'##cross-references GB:J01420; NID:g342520; PIDN:AAB48655.1; !1PID:g896301; EMBL:V00711; NID:g13838; PID:g13850 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 6 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 172 #molecular-weight 18626 #checksum 7864 SEQUENCE /// ENTRY DERTN6 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 6 - rat mitochondrion ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 6 ORGANISM #formal_name mitochondrion Rattus norvegicus #common_name Norway rat DATE 14-Nov-1983 #sequence_revision 12-Feb-1999 #text_change 03-Jun-2002 ACCESSIONS S04758; B00154; A94555; I48220; I77965; A00458 REFERENCE S04747 !$#authors Gadaleta, G.; Pepe, G.; De Candia, G.; Quagliariello, C.; !1Sbisa, E.; Saccone, C. !$#journal J. Mol. Evol. (1989) 28:497-516 !$#title The complete nucleotide sequence of the Rattus norvegicus !1mitochondrial genome: cryptic signals revealed by !1comparative analysis between vertebrates. !$#cross-references MUID:89362487; PMID:2504926 !$#accession S04758 !'##molecule_type DNA !'##residues 1-79,'A',81,'Y',83-172 ##label GAD1 !'##cross-references EMBL:X14848; NID:g854269 REFERENCE A00154 !$#authors Koike, K.; Kobayashi, M.; Yaginuma, K.; Taira, M.; Yoshida, !1E.; Imai, M. !$#journal Gene (1982) 20:177-185 !$#title Nucleotide sequence and evolution of the rat mitochondrial !1cytochrome b gene containing the ochre termination codon. !$#cross-references MUID:83158755; PMID:6299885 !$#accession B00154 !'##molecule_type DNA !'##residues 1-79 ##label KOI !'##cross-references GB:J01436; NID:g343168 REFERENCE A94555 !$#authors Koike, K. !$#submission submitted to the Atlas, April 1984 !$#accession A94555 !'##molecule_type DNA !'##residues 'R' ##label KO2 REFERENCE I48220 !$#authors Goertz, G.; Feldmann, H. !$#journal Curr. Genet. (1982) 5:221-225 !$#title Nucleotide sequence of the cytochrome b gene and adjacent !1regions from rat liver mitochondrial DNA. !$#accession I48220 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1,'L',3-79 ##label GOE !'##cross-references EMBL:V01556; NID:g13467; PIDN:CAA24881.1; !1PID:g13468 REFERENCE I58004 !$#authors Gadaleta, M.N.; Rainaldi, G.; Lezza, A.M.; Milella, F.; !1Fracasso, F.; Cantatore, P. !$#journal Mutat. Res. (1992) 275:181-193 !$#title Mitochondrial DNA copy number and mitochondrial DNA deletion !1in adult and senescent rats. !$#cross-references MUID:93024615; PMID:1383760 !$#accession I77965 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 80-158,'M',160-163 ##label GAD2 !'##cross-references GB:S46798; NID:g258278; PIDN:AAB23820.1; !1PID:g258280 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 6 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 172 #molecular-weight 18956 #checksum 5992 SEQUENCE /// ENTRY DEXLN6 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 6 - African clawed frog mitochondrion ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 6 ORGANISM #formal_name mitochondrion Xenopus laevis #common_name African clawed frog DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 03-Jun-2002 ACCESSIONS A00459 REFERENCE A00155 !$#authors Roe, B.A.; Ma, D.P.; Wilson, R.K.; Wong, J.F.H. !$#journal J. Biol. Chem. (1985) 260:9759-9774 !$#title The complete nucleotide sequence of the Xenopus laevis !1mitochondrial genome. !$#cross-references MUID:85261388; PMID:4019494 !$#accession A00459 !'##molecule_type DNA !'##residues 1-170 ##label ROE !'##cross-references GB:M10217; GB:X01600; GB:X01601; GB:X02890; !1NID:g343717; PIDN:AAA66469.1; PID:g807693 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 6 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 170 #molecular-weight 18768 #checksum 1529 SEQUENCE /// ENTRY DELVN6 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 6 - liverwort (Marchantia polymorpha) chloroplast ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 6; ndh6 protein ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 03-Jun-2002 ACCESSIONS A00460; S01525 REFERENCE A00150 !$#authors Ohyama, K. !$#submission submitted to the EMBL Data Library, October 1986 !$#accession A00460 !'##molecule_type DNA !'##residues 1-191 ##label OHY REFERENCE S01512 !$#authors Kohchi, T.; Shirai, H.; Fukuzawa, H.; Sano, T.; Komano, T.; !1Umesono, K.; Inokuchi, H.; Ozeki, H.; Ohyama, K. !$#journal J. Mol. Biol. (1988) 203:353-372 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. IV. Inverted repeat and small single !1copy regions. !$#cross-references MUID:89068688; PMID:3199437 !$#accession S01525 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-191 ##label KOH !'##cross-references GB:X04465; GB:Y00686; NID:g11640; PIDN:CAA28137.1; !1PID:g11726 REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features GENETICS !$#gene ndh6 !$#genome chloroplast CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 6 KEYWORDS chloroplast; membrane-associated complex; NAD; !1oxidoreductase SUMMARY #length 191 #molecular-weight 21607 #checksum 2256 SEQUENCE /// ENTRY DERZN6 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 6 - rice chloroplast ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 6; ndh6 protein ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 03-Jun-2002 ACCESSIONS JQ0292; S05171 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0292 !'##molecule_type DNA !'##residues 1-176 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05171 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-176 ##label HIR !'##cross-references EMBL:X15901; NID:g11957; PIDN:CAA33908.1; !1PID:g12053 !'##experimental_source cv. Nihonbare GENETICS !$#gene ndhG !$#map_position CP109757-109227 !$#genome chloroplast CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 6 KEYWORDS chloroplast; membrane-associated complex; NAD; !1oxidoreductase SUMMARY #length 176 #molecular-weight 19349 #checksum 1505 SEQUENCE /// ENTRY QXYB6 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 6 - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein sll0521 ORGANISM #formal_name Synechocystis sp. #variety strain PCC 6803 DATE 31-Mar-1992 #sequence_revision 24-Apr-1998 #text_change 03-Jun-2002 ACCESSIONS S76036; S27974; S18048 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76036 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-198 ##label KAN !'##cross-references EMBL:D64006; GB:AB001339; NID:g1001291; !1PIDN:BAA10883.1; PID:g1001393 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 REFERENCE S27972 !$#authors Ellersiek, U.; Steinmueller, K. !$#journal Plant Mol. Biol. (1992) 20:1097-1110 !$#title Cloning and transcription analysis of the ndh(A-I-G-E) gene !1cluster and the ndhD gene of the cyanobacterium !1Synechocystis sp. PCC6803. !$#cross-references MUID:93099260; PMID:1463844 !$#accession S27974 !'##molecule_type DNA !'##residues 1-167,'PG',170,'NSRIVRGKQ',178,'RHGPDFARASPGVN',193, !1'RFQIDAA' ##label ELL !'##cross-references EMBL:X62517; NID:g47554; PIDN:CAA44376.1; !1PID:g581746 !'##note the authors translated the initiation codon GTG for residue 1 !1as Val GENETICS !$#gene ndhG !$#start_codon GTG CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 6 KEYWORDS membrane-associated complex; NAD; oxidoreductase SUMMARY #length 198 #molecular-weight 21522 #checksum 5543 SEQUENCE /// ENTRY JQ2137 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 6 - Plectonema boryanum ORGANISM #formal_name Plectonema boryanum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS JQ2137 REFERENCE JQ2135 !$#authors Takahashi, Y.; Shonai, F.; Fujita, Y.; Kohchi, T.; Ohyama, !1K.; Matsubara, H. !$#journal Plant Cell Physiol. (1991) 32:969-981 !$#title Structure of a co-transcribed gene cluster, !1ndh1-frxB-ndh6-ndh4L, cloned from the filamentous !1cyanobacterium Plectonema boryanum. !$#accession JQ2137 !'##molecule_type DNA !'##residues 1-199 ##label TAK !'##cross-references DDBJ:D01014; NID:g216817; PIDN:BAA00816.1; !1PID:g441181 !'##experimental_source strain M101 GENETICS !$#gene ndh6 !$#start_codon GTG CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 6 KEYWORDS membrane-associated complex; NAD; oxidoreductase SUMMARY #length 199 #molecular-weight 21299 #checksum 2110 SEQUENCE /// ENTRY S25967 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 6 - liverwort (Marchantia polymorpha) mitochondrion ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 6 ORGANISM #formal_name mitochondrion Marchantia polymorpha DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S25967; S32196 REFERENCE S25941 !$#authors Oda, K.; Yamato, K.; Ohta, E.; Nakamura, Y.; Takemura, M.; !1Nozato, N.; Akashi, K.; Kanegae, T.; Ogura, Y.; Kohchi, T.; !1Ohyama, K. !$#journal J. Mol. Biol. (1992) 223:1-7 !$#title Gene organization deduced from the complete sequence of !1liverwort Marchantia polymorpha mitochondrial DNA. A !1primitive form of plant mitochondrial genome. !$#cross-references MUID:92114051; PMID:1731062 !$#accession S25967 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-199 ##label ODA !'##cross-references EMBL:M68929; NID:g786182; PIDN:AAC09405.1; !1PID:g786192 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1February 1992 REFERENCE S32195 !$#authors Yamato, K.; Nozato, N.; Oda, K.; Ohta, E.; Takemura, M.; !1Akashi, K.; Ohyama, K. !$#journal Curr. Genet. (1993) 23:526-531 !$#title Occurrence and transcription of genes for nad1, nad3, nad4L, !1and nad6, coding for NADH dehydrogenase subunits 1, 3, 4L, !1and 6, in liverwort mitochondria. !$#cross-references MUID:93306762; PMID:7916672 !$#contents annotation GENETICS !$#gene nad6 !$#genome mitochondrion CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 6 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 199 #molecular-weight 22539 #checksum 9945 SEQUENCE /// ENTRY F45456 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 6 - Paracoccus denitrificans ALTERNATE_NAMES NADH-ubiquinone oxidoreductase chain 6 ORGANISM #formal_name Paracoccus denitrificans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS F45456 REFERENCE A45456 !$#authors Xu, X.; Matsuno-Yagi, A.; Yagi, T. !$#journal Biochemistry (1993) 32:968-981 !$#title DNA sequencing of the seven remaining structural genes of !1the gene cluster encoding the energy-transducing !1NADH-quinone oxidoreductase of Paracoccus denitrificans. !$#cross-references MUID:93136200; PMID:8422400 !$#accession F45456 !'##status preliminary !'##molecule_type DNA !'##residues 1-200 ##label XU1 !'##cross-references GB:L02354; GB:L01096; NID:g150606; PIDN:AAA25596.1; !1PID:g150612 !'##note sequence extracted from NCBI backbone (NCBIN:123409, !1NCBIP:123416) CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 6 KEYWORDS membrane-associated complex; NAD; oxidoreductase; !1transmembrane protein SUMMARY #length 200 #molecular-weight 21819 #checksum 9819 SEQUENCE /// ENTRY QXASC #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 6 - Emericella nidulans mitochondrion ORGANISM #formal_name mitochondrion Emericella nidulans, Aspergillus nidulans DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 03-Jun-2002 ACCESSIONS E93436; C94593; A04516 REFERENCE A93436 !$#authors Netzker, R.; Kochel, H.G.; Basak, N.; Kuntzel, H. !$#journal Nucleic Acids Res. (1982) 10:4783-4794 !$#title Nucleotide sequence of Aspergillus nidulans mitochondrial !1genes coding for ATPase subunit 6, cytochrome oxidase !1subunit 3, seven unidentified proteins, four tRNAs and !1L-rRNA. !$#cross-references MUID:83038633; PMID:6290989 !$#accession E93436 !'##molecule_type DNA !'##residues 1-46,'P',48-194,'E',196-228 ##label NET !'##experimental_source imperfect stage !'##note this sequence has been revised in reference A94593 REFERENCE A94593 !$#authors Lazarus, C.M.; Kuntzel, H. !$#submission submitted to the Atlas, March 1984 !$#accession C94593 !'##molecule_type DNA !'##residues 1-228 ##label LAZ COMMENT Residues 25-228 may be very distantly related to !1hypothetical protein 6 of the animal mitochondria. GENETICS !$#genome mitochondrion !$#genetic_code SGC3 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 6 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 228 #molecular-weight 25381 #checksum 1909 SEQUENCE /// ENTRY S65033 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 6 - dermatophytic fungus (Trichophyton rubrum) mitochondrion ORGANISM #formal_name mitochondrion Trichophyton rubrum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S65033 REFERENCE S65031 !$#authors de Bievre, C.; Dujon, B. !$#journal Curr. Genet. (1995) 28:553-559 !$#title Organisation of the mitochondrial genome of Trichophyton !1rubrum. DNA sequence analysis of the ND4 gene, the ATPase !1subunit-6 gene, the ribosomal RNA small-subunit gene, the !1ND6 gene, the COXIII gene, the ATPase subunit-8 gene and six !1tRNA genes that correspond respectively to the tyrosine, !1lysine, glutamine, asparagine, isoleucine and tryptophan !1isoacceptors. !$#cross-references MUID:96132111; PMID:8593686 !$#accession S65033 !'##status preliminary !'##molecule_type DNA !'##residues 1-203 ##label DEB !'##cross-references EMBL:X88896; NID:g1017446; PIDN:CAA61356.1; !1PID:g1017449 !'##note the authors translated the codon CCT for residue 39 as Ala and !1CCT for residue 104 as Ala GENETICS !$#genome mitochondrion !$#genetic_code SGC3 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 6 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 203 #molecular-weight 22656 #checksum 4345 SEQUENCE /// ENTRY S02156 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain 6 - Podospora anserina mitochondrion ORGANISM #formal_name mitochondrion Podospora anserina DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S02156 REFERENCE S02153 !$#authors Cummings, D.J.; Domenico, J.M. !$#journal J. Mol. Biol. (1988) 204:815-839 !$#title Sequence analysis of mitochondrial DNA from Podospora !1anserina. Pervasiveness of a class I intron in three !1separate genes. !$#cross-references MUID:89125610; PMID:2975708 !$#accession S02156 !'##molecule_type DNA !'##residues 1-221 ##label CUM !'##cross-references EMBL:X14486; NID:g13303; PIDN:CAA32648.1; !1PID:g13304 GENETICS !$#genome mitochondrion !$#genetic_code SGC3 CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) chain 6 KEYWORDS membrane-associated complex; mitochondrion; NAD; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 221 #molecular-weight 25357 #checksum 542 SEQUENCE /// ENTRY DERZ49 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) 49K protein - rice chloroplast ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 03-Jun-2002 ACCESSIONS JQ0295; S05174 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0295 !'##molecule_type DNA !'##residues 1-393 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05174 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-393 ##label HIR !'##cross-references EMBL:X15901; NID:g11957; PIDN:CAA33911.1; !1PID:g12056 !'##experimental_source cv. Nihonbare GENETICS !$#gene ndhH; rps15 !$#map_position CP113889-112708 !$#genome chloroplast CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) 49K protein KEYWORDS chloroplast; membrane-associated complex; NAD; !1oxidoreductase SUMMARY #length 393 #molecular-weight 45685 #checksum 3367 SEQUENCE /// ENTRY QXYBNH #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain ndhH - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES NADH dehydrogenase chain 7 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 03-Jun-2002 ACCESSIONS S19118; S34477; S75077; S16045 REFERENCE S19118 !$#authors Steinmueller, K. !$#journal Plant Mol. Biol. (1992) 18:135-137 !$#title Nucleotide sequence and expression of the ndhH gene of the !1cyanobacterium Synechocystis sp. PCC6803. !$#cross-references MUID:92119222; PMID:1731965 !$#accession S19118 !'##molecule_type DNA !'##residues 1-394 ##label STE !'##cross-references EMBL:X60650; NID:g48041; PIDN:CAA43057.1; !1PID:g48042 REFERENCE S34477 !$#authors Berger, S.; Ellersiek, U.; Kinzelt, D.; Steinmueller, K. !$#journal FEBS Lett. (1993) 326:246-250 !$#title Immunopurification of a subcomplex of the NAD !1(P)H-plastoquinone-oxidoreductase from the cyanobacterium !1Synechocystis sp. PCC6803. !$#cross-references MUID:93314795; PMID:8325373 !$#accession S34477 !'##status preliminary !'##molecule_type protein !'##residues 2-18 ##label BER REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75077 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-394 ##label KAN !'##cross-references EMBL:D90910; GB:AB001339; NID:g1652956; !1PIDN:BAA17939.1; PID:g1653022 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene ndhH CLASSIFICATION #superfamily NADH dehydrogenase (ubiquinone) 49K protein KEYWORDS membrane-associated complex; NAD; oxidoreductase SUMMARY #length 394 #molecular-weight 45534 #checksum 7750 SEQUENCE /// ENTRY D65000 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) I, chain C-D - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS D65000; S38313; S38312; S65634; S65635; S37060; S37061 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65000 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-600 ##label BLAT !'##cross-references GB:AE000317; GB:U00096; NID:g1788605; !1PIDN:AAC75346.1; PID:g1788622; UWGP:b2286 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S38310 !$#authors Weidner, U.; Geier, S.; Ptock, A.; Friedrich, T.; Leif, H.; !1Weiss, H. !$#journal J. Mol. Biol. (1993) 233:109-122 !$#title The gene locus of the proton-translocating NADH:ubiquinone !1oxidoreductase in Escherichia coli. Organization of the 14 !1genes and relationship between the derived proteins and !1subunits of mitochondrial complex I. !$#cross-references MUID:93389724; PMID:7690854 !$#accession S38313 !'##status preliminary !'##molecule_type DNA !'##residues 194-224,'RR',227,'D',229-232,'T',234-368,'RRPAA',374, !1'LGSPAA',382-412,'PMAR',417-474,'G',476-493,'NR',496-600 !1##label WEI !'##cross-references EMBL:X68301; NID:g444012; PIDN:CAA48363.1; !1PID:g444013 !'##experimental_source strain K-12, substrain AN387 !$#accession S38312 !'##status preliminary !'##molecule_type DNA !'##residues 1-174,'RARYRILAV' ##label WE2 !'##cross-references EMBL:X68301; NID:g444012; PIDN:CAA48362.1; !1PID:g397900 !'##experimental_source strain K-12, substrain AN387 REFERENCE S65633 !$#authors Leif, H.; Sled, V.D.; Ohnishi, T.; Weiss, H.; Friedrich, T. !$#journal Eur. J. Biochem. (1995) 230:538-548 !$#title Isolation and characterization of the proton-translocating !1NADH:ubiquinone oxidoreductase from Escherichia coli. !$#cross-references MUID:95331291; PMID:7607227 !$#accession S65634 !'##molecule_type protein !'##residues 1-4 ##label LEI !$#accession S65635 !'##molecule_type protein !'##residues 'T',234-236 ##label LEW GENETICS !$#gene nuoC; nuoD !$#map_position 49.5 min CLASSIFICATION #superfamily Escherichia coli NADH dehydrogenase !1(ubiquinone) I, chain C-D KEYWORDS NAD; oxidoreductase SUMMARY #length 600 #molecular-weight 68694 #checksum 7130 SEQUENCE /// ENTRY F70349 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) I chain nuoD1 [similarity] - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 03-Jun-2002 ACCESSIONS F70349 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession F70349 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-593 ##label AQF !'##cross-references GB:AE000695; NID:g2983180; PIDN:AAC06787.1; !1PID:g2983187; GB:AE000657 !'##experimental_source strain VF5 GENETICS !$#gene nuoD1 CLASSIFICATION #superfamily Escherichia coli NADH dehydrogenase !1(ubiquinone) I, chain C-D KEYWORDS NAD; oxidoreductase SUMMARY #length 593 #molecular-weight 68691 #checksum 3056 SEQUENCE /// ENTRY D70413 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) I chain nuoD2 [similarity] - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 03-Jun-2002 ACCESSIONS D70413 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession D70413 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-586 ##label AQF !'##cross-references GB:AE000734; NID:g2983733; PIDN:AAC07298.1; !1PID:g2983737; GB:AE000657 !'##experimental_source strain VF5 GENETICS !$#gene nuoD2 CLASSIFICATION #superfamily Escherichia coli NADH dehydrogenase !1(ubiquinone) I, chain C-D KEYWORDS NAD; oxidoreductase SUMMARY #length 586 #molecular-weight 67892 #checksum 1027 SEQUENCE /// ENTRY I67685 #type complete TITLE nitroreductase (EC 1.6.6.-) IB1 - Escherichia coli (strain K-12) ALTERNATE_NAMES oxygen-insensitive NAD(P)H nitroreductase ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS I67685; JC4941; H64790; B48986; A48986 REFERENCE I53585 !$#authors Michael, N.P.; Brehm, J.K.; Anlezark, G.M.; Minton, N.P. !$#journal FEMS Microbiol. Lett. (1994) 124:195-202 !$#title Physical characterisation of the Escherichia coli B gene !1encoding nitroreductase and its over-expression in !1Escherichia coli K12. !$#cross-references MUID:95113294; PMID:7813889 !$#accession I67685 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-217 ##label RES !'##cross-references EMBL:U07860; NID:g533420; PIDN:AAC43263.1; !1PID:g533421 REFERENCE JC4941 !$#authors Zenno, S.; Koike, H.; Tanokura, M.; Saigo, K. !$#journal J. Biochem. (1996) 120:736-744 !$#title Gene cloning, purification, and characterization of NfsB, a !1minor oxygen-insensitive nitroreductase from Escherichia !1coli, similar in biochemical properties to FRase I, the !1major flavin reductase in Vibrio fischeri. !$#cross-references MUID:97103464; PMID:8947835 !$#accession JC4941 !'##status preliminary !'##molecule_type DNA !'##residues 1-217 ##label ZEN !'##cross-references DDBJ:D25414; NID:g538226; PIDN:BAA05004.1; !1PID:g538227 !'##experimental_source strain K12 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64790 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-217 ##label BLAT !'##cross-references GB:AE000163; GB:U00096; NID:g1786790; !1PIDN:AAC73679.1; PID:g1786792; UWGP:b0578 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A48986 !$#authors Anlezark, G.M.; Melton, R.G.; Sherwood, R.F.; Coles, B.; !1Friedlos, F.; Knox, R.J. !$#journal Biochem. Pharmacol. (1992) 44:2289-2295 !$#title The bioactivation of 5-(aziridin-1-yl)-2,4-dinitrobenzamide !1(CB1954)--I. Purification and properties of a nitroreductase !1enzyme from Escherichia coli--a potential enzyme for !1antibody-directed enzyme prodrug therapy (ADEPT). !$#cross-references MUID:93112106; PMID:1472094 !$#accession B48986 !'##status preliminary !'##molecule_type protein !'##residues 139-179,'I' ##label ANL !'##experimental_source B !'##note sequence extracted from NCBI backbone (NCBIP:121770) !$#accession A48986 !'##status preliminary !'##molecule_type protein !'##residues 1-20,22-27,'D',29-31 ##label AN2 !'##note sequence extracted from NCBI backbone (NCBIP:121766) COMMENT This enzyme belongs to the type I nitroreductases. It is a !1flavoprotein associated with a low level of FMN/FAD !1reductase activity. GENETICS !$#gene nfnB; nfsB COMPLEX homodimer CLASSIFICATION #superfamily nitroreductase KEYWORDS flavoprotein; homodimer; oxidoreductase SUMMARY #length 217 #molecular-weight 23905 #checksum 6270 SEQUENCE /// ENTRY S08397 #type complete TITLE nitroreductase (EC 1.6.6.-) - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S08397 REFERENCE S08397 !$#authors Watanabe, M.; Ishidate Jr., M.; Nohmi, T. !$#journal Nucleic Acids Res. (1990) 18:1059 !$#title Nucleotide sequence of Salmonella typhimurium nitroreductase !1gene. !$#cross-references MUID:90192100; PMID:2179862 !$#accession S08397 !'##molecule_type DNA !'##residues 1-217 ##label WAT !'##cross-references EMBL:X17250; NID:g47792; PIDN:CAA35113.1; !1PID:g47793 CLASSIFICATION #superfamily nitroreductase KEYWORDS oxidoreductase SUMMARY #length 217 #molecular-weight 23955 #checksum 6660 SEQUENCE /// ENTRY A38686 #type complete TITLE nitroreductase (EC 1.6.6.-) - Enterobacter cloacae ORGANISM #formal_name Enterobacter cloacae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A38686 REFERENCE A38686 !$#authors Bryant, C.; Hubbard, L.; McElroy, W.D. !$#journal J. Biol. Chem. (1991) 266:4126-4130 !$#title Cloning, nucleotide sequence, and expression of the !1nitroreductase gene from Enterobacter cloacae. !$#cross-references MUID:91154203; PMID:1999406 !$#accession A38686 !'##status preliminary !'##molecule_type DNA !'##residues 1-217 ##label BRY !'##cross-references GB:M63808; GB:M37085; NID:g148361; PIDN:AAA62801.1; !1PID:g148362 CLASSIFICATION #superfamily nitroreductase KEYWORDS oxidoreductase SUMMARY #length 217 #molecular-weight 23950 #checksum 5913 SEQUENCE /// ENTRY B64600 #type complete TITLE NAD(P)H-flavin oxidoreductase (EC 1.6.6.-) - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B64600 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession B64600 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-217 ##label TOM !'##cross-references GB:AE000578; GB:AE000511; NID:g2313759; !1PIDN:AAD07703.1; PID:g2313762; TIGR:HP0642 CLASSIFICATION #superfamily nitroreductase KEYWORDS oxidoreductase SUMMARY #length 217 #molecular-weight 25293 #checksum 1959 SEQUENCE /// ENTRY B64114 #type complete TITLE probable NAD(P)H-flavin oxidoreductase (EC 1.6.6.-) - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B64114 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession B64114 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-220 ##label TIGR !'##cross-references GB:U32807; GB:L42023; NID:g1574725; !1PIDN:AAC22926.1; PID:g1574733; TIGR:HI1278 !'##note named as homolog to a protein from Vibrio fischeri CLASSIFICATION #superfamily nitroreductase KEYWORDS NAD; oxidoreductase SUMMARY #length 220 #molecular-weight 25189 #checksum 189 SEQUENCE /// ENTRY RDMUNH #type complete TITLE nitrate reductase (NADH) (EC 1.7.1.1) 2 - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Jun-2002 ACCESSIONS A31821; S01641 REFERENCE A31821 !$#authors Crawford, N.M.; Smith, M.; Bellissimo, D.; Davis, R.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:5006-5010 !$#title Sequence and nitrate regulation of the Arabidopsis thaliana !1mRNA encoding nitrate reductase, a metalloflavoprotein with !1three functional domains. !$#cross-references MUID:88276888; PMID:3393528 !$#accession A31821 !'##molecule_type mRNA !'##residues 1-917 ##label CRA !'##cross-references GB:J03240; NID:g166781; PIDN:AAA32830.1; !1PID:g166782 REFERENCE S01640 !$#authors Cheng, C.; Dewdney, J.; Nam, H.; den Boer, B.G.W.; Goodman, !1H.M. !$#journal EMBO J. (1988) 7:3309-3314 !$#title A new locus (NIA1) in Arabidopsis thaliana encoding nitrate !1reductase. !$#cross-references MUID:89091069; PMID:2905260 !$#accession S01641 !'##molecule_type mRNA !'##residues 522-917 ##label CHE !'##cross-references EMBL:X13435; NID:g16403; PIDN:CAA31787.1; !1PID:g930002 !'##note the translation of the nucleotide sequence is not complete COMMENT This enzyme catalyzes the reduction of nitrate to nitrite in !1cytoplasm; each chain contains one equivalent of FAD, heme !1iron, and molybdenum-pterin as prosthetic groups. This is a !1key enzyme involved in the first step of nitrate !1assimilation in plants, fungi, and bacteria. GENETICS !$#gene NIA2 !$#map_position 1 COMPLEX homodimer CLASSIFICATION #superfamily nitrate reductase (NADH); cytochrome b5 core !1homology; cytochrome-b5 reductase homology; !1molybdopterin-binding domain homology KEYWORDS chromoprotein; electron transfer; FAD; flavoprotein; heme; !1homodimer; iron; metalloprotein; molybdenum; molybdopterin; !1NAD; nitrate assimilation; oxidoreductase; phosphoprotein FEATURE !$87-482 #domain molybdopterin-binding domain homology #label !8PCO\ !$542-616 #domain cytochrome b5 core homology #label CB5\ !$667-917 #domain cytochrome-b5 reductase homology #label CBR\ !$191 #binding_site molybdopterin (Cys) (covalent) #status !8predicted\ !$433 #disulfide_bonds interchain #status predicted\ !$577,600 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$731,889 #binding_site NAD (Lys, Cys) #status predicted\ !$771 #binding_site FAD (Tyr) #status predicted SUMMARY #length 917 #molecular-weight 102844 #checksum 5640 SEQUENCE /// ENTRY RDTONH #type complete TITLE nitrate reductase (NADH) (EC 1.7.1.1) - tomato ORGANISM #formal_name Lycopersicon esculentum #common_name tomato DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Jun-2002 ACCESSIONS JQ0373 REFERENCE JQ0373 !$#authors Daniel-Vedele, F.; Dorbe, M.F.; Caboche, M.; Rouze, P. !$#journal Gene (1989) 85:371-380 !$#title Cloning and analysis of the tomato nitrate !1reductase-encoding gene: protein domain structure and amino !1acid homologies in higher plants. !$#cross-references MUID:90185211; PMID:2628174 !$#accession JQ0373 !'##molecule_type DNA !'##residues 1-911 ##label DAN !'##cross-references GB:X14060; NID:g19282; PIDN:CAA32218.1; PID:g19283 COMMENT This enzyme catalyzes the reduction of nitrate to nitrite in !1cytoplasm; each chain contains one equivalent of FAD, heme !1iron, and molybdenum-pterin as prosthetic groups. This is a !1key enzyme involved in the first step of nitrate !1assimilation in plants, fungi, and bacteria. GENETICS !$#gene nia !$#introns 343/1; 390/1; 467/3 CLASSIFICATION #superfamily nitrate reductase (NADH); cytochrome b5 core !1homology; cytochrome-b5 reductase homology; !1molybdopterin-binding domain homology KEYWORDS chromoprotein; electron transfer; FAD; flavoprotein; heme; !1homodimer; iron; metalloprotein; molybdenum; molybdopterin; !1NAD; nitrate assimilation; oxidoreductase; phosphoprotein FEATURE !$84-476 #domain molybdopterin-binding domain homology #label !8PCO\ !$536-610 #domain cytochrome b5 core homology #label CB5\ !$661-911 #domain cytochrome-b5 reductase homology #label CBR\ !$188 #binding_site molybdopterin (Cys) (covalent) #status !8predicted\ !$427 #disulfide_bonds interchain #status predicted\ !$571,594 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$725,883 #binding_site NAD (Lys, Cys) #status predicted\ !$765 #binding_site FAD (Tyr) #status predicted SUMMARY #length 911 #molecular-weight 102452 #checksum 3686 SEQUENCE /// ENTRY RDNTNT #type complete TITLE nitrate reductase (NADH) (EC 1.7.1.1) nia-1 - common tobacco ORGANISM #formal_name Nicotiana tabacum #common_name common tobacco DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 03-Jun-2002 ACCESSIONS S04838; S05696 REFERENCE S04838 !$#authors Vaucheret, H.; Kronenberger, J.; Rouze, P.; Caboche, M. !$#journal Plant Mol. Biol. (1989) 12:597-600 !$#title Complete nucleotide sequence of the two homeologous tobacco !1nitrate reductase genes. !$#accession S04838 !'##molecule_type DNA !'##residues 1-904 ##label VAU !'##cross-references EMBL:X14058 REFERENCE S05696 !$#authors Rouze, P. !$#submission submitted to the EMBL Data Library, January 1989 !$#accession S05696 !'##molecule_type DNA !'##residues 1-35,'P',37-904 ##label ROU !'##cross-references EMBL:X14058; NID:g19888; PIDN:CAA32216.1; !1PID:g19889 GENETICS !$#gene nia-1 !$#introns 338/1; 385/1; 462/3 COMPLEX homodimer CLASSIFICATION #superfamily nitrate reductase (NADH); cytochrome b5 core !1homology; cytochrome-b5 reductase homology; !1molybdopterin-binding domain homology KEYWORDS chromoprotein; electron transfer; FAD; flavoprotein; heme; !1homodimer; iron; metalloprotein; molybdenum; molybdopterin; !1NAD; nitrate assimilation; oxidoreductase; phosphoprotein FEATURE !$79-471 #domain molybdopterin-binding domain homology #label !8PCO\ !$531-605 #domain cytochrome b5 core homology #label CB5\ !$654-904 #domain cytochrome-b5 reductase homology #label CBR\ !$183 #binding_site molybdopterin (Cys) (covalent) #status !8predicted\ !$422 #disulfide_bonds interchain #status predicted\ !$566,589 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$718,876 #binding_site NAD (Lys, Cys) #status predicted\ !$758 #binding_site FAD (Tyr) #status predicted SUMMARY #length 904 #molecular-weight 101897 #checksum 4005 SEQUENCE /// ENTRY RDNTNS #type complete TITLE nitrate reductase (NADH) (EC 1.7.1.1) nia-2 - common tobacco ORGANISM #formal_name Nicotiana tabacum #common_name common tobacco DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 03-Jun-2002 ACCESSIONS S04839; S25375; S22779 REFERENCE S04838 !$#authors Vaucheret, H.; Kronenberger, J.; Rouze, P.; Caboche, M. !$#journal Plant Mol. Biol. (1989) 12:597-600 !$#title Complete nucleotide sequence of the two homeologous tobacco !1nitrate reductase genes. !$#accession S04839 !'##molecule_type DNA !'##residues 1-904 ##label VAU !'##cross-references EMBL:X14059; NID:g19890; PIDN:CAA32217.1; !1PID:g19891 REFERENCE S25375 !$#authors Galangau, F.; Cherel, I.; Deng, M.; Meyer, C.; Moureaux, T.; !1Rouze, P.; Vaucheret, H.; Vedele, F.; Vincentz, M.; Caboche, !1M. !$#journal Curr. Top. Plant Biochem. Physiol. (1988) 7:26-34 !$#title Nitrate reductase expression in tobacco and tomato. !$#accession S25375 !'##molecule_type DNA !'##residues 1-904 ##label GAL REFERENCE S22779 !$#authors Calza, R.; Huttner, E.; Vincentz, M.; Rouze, P.; Galangau, !1F.; Vaucheret, H.; Cherel, I.; Meyer, C.; Kronenberger, J.; !1Caboche, M. !$#journal Mol. Gen. Genet. (1987) 209:552-562 !$#title Cloning of DNA fragments complementary to tobacco nitrate !1reductase mRNA and encoding epitopes common to the nitrate !1reductases from higher plants. !$#accession S22779 !'##molecule_type mRNA !'##residues 171-724 ##label CAL !'##cross-references EMBL:X06134; NID:g19894; PIDN:CAA29497.1; !1PID:g929750 GENETICS !$#gene nia-2 !$#introns 338/1; 385/1; 462/3 COMPLEX homodimer CLASSIFICATION #superfamily nitrate reductase (NADH); cytochrome b5 core !1homology; cytochrome-b5 reductase homology; !1molybdopterin-binding domain homology KEYWORDS chromoprotein; electron transfer; FAD; flavoprotein; heme; !1homodimer; iron; metalloprotein; molybdenum; molybdopterin; !1NAD; nitrate assimilation; oxidoreductase; phosphoprotein FEATURE !$79-471 #domain molybdopterin-binding domain homology #label !8PCO\ !$531-605 #domain cytochrome b5 core homology #label CB5\ !$654-904 #domain cytochrome-b5 reductase homology #label CBR\ !$183 #binding_site molybdopterin (Cys) (covalent) #status !8predicted\ !$422 #disulfide_bonds interchain #status predicted\ !$566,589 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$718,876 #binding_site NAD (Lys, Cys) #status predicted\ !$758 #binding_site FAD (Tyr) #status predicted SUMMARY #length 904 #molecular-weight 101957 #checksum 3551 SEQUENCE /// ENTRY RDSPNH #type complete TITLE nitrate reductase (NADH) (EC 1.7.1.1) - spinach ORGANISM #formal_name Spinacia oleracea #common_name spinach DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 03-Jun-2002 ACCESSIONS S11868; PQ0694; PQ0695; S62777; A45589; B45589; S68383 REFERENCE S11868 !$#authors Prosser, I.M.; Lazarus, C.M. !$#journal Plant Mol. Biol. (1990) 15:187-190 !$#title Nucleotide sequence of a spinach nitrate reductase cDNA. !$#cross-references MUID:91355858; PMID:2103436 !$#accession S11868 !'##molecule_type mRNA !'##residues 1-926 ##label PRO !'##cross-references GB:M32600; NID:g170118; PIDN:AAA34033.1; !1PID:g170119 REFERENCE PQ0694 !$#authors Shiraishi, N.; Kubo, Y.; Takeba, G.; Kiyota, S.; Sakano, K.; !1Nakagawa, H. !$#journal Plant Cell Physiol. (1991) 32:1031-1038 !$#title Sequence analysis of cloned cDNA and proteolytic fragments !1for nitrate reductase from Spinacia oleracea L. !$#accession PQ0694 !'##molecule_type mRNA !'##residues 287-926 ##label SHI !'##experimental_source cv. Hoyo !$#accession PQ0695 !'##molecule_type protein !'##residues 541-550;659-667 ##label SH2 REFERENCE S62777 !$#authors Quinn, G.B.; Trimboli, A.J.; Prosser, I.M.; Barber, M.J. !$#journal Arch. Biochem. Biophys. (1996) 327:151-160 !$#title Spectroscopic and kinetic properties of a recombinant form !1of the flavin domain of spinach NADH:nitrate reductase. !$#cross-references MUID:96201358; PMID:8615685 !$#accession S62777 !'##molecule_type protein !'##residues !1659-673;722-731;758-766;789-798;802-814;829-833;846-852; !1853-858;859-864;874-879;904-914;916-926 ##label QUI REFERENCE A45589 !$#authors Fido, R.J. !$#journal Phytochemistry (1991) 30:3519-3523 !$#title Isolation and partial amino acid sequence of domains of !1nitrate reductase from spinach. !$#cross-references MUID:92134724; PMID:1367837 !$#accession A45589 !'##molecule_type protein !'##residues 659-701 ##label FID !'##note sequence extracted from NCBI backbone (NCBIP:79483) !$#accession B45589 !'##molecule_type protein !'##residues 'A',533-564 ##label FI2 !'##note sequence extracted from NCBI backbone (NCBIP:79485) REFERENCE S68382 !$#authors Douglas, P.; Morrice, N.; MacKintosh, C. !$#journal FEBS Lett. (1995) 377:113-117 !$#title Identification of a regulatory phosphorylation site in the !1hinge 1 region of nitrate reductase from spinach (Spinacea !1oleracea) leaves. !$#cross-references MUID:96128209; PMID:8543031 !$#accession S68383 !'##molecule_type protein !'##residues 25-33;46-60;541-552 ##label DOU COMPLEX homodimer CLASSIFICATION #superfamily nitrate reductase (NADH); cytochrome b5 core !1homology; cytochrome-b5 reductase homology; !1molybdopterin-binding domain homology KEYWORDS chromoprotein; electron transfer; FAD; flavoprotein; heme; !1homodimer; iron; metalloprotein; molybdenum; molybdopterin; !1NAD; nitrate assimilation; oxidoreductase; phosphoprotein FEATURE !$100-492 #domain molybdopterin-binding domain homology #label !8PCO\ !$551-625 #domain cytochrome b5 core homology #label CB5\ !$677-926 #domain cytochrome-b5 reductase homology #label CBR\ !$204 #binding_site molybdopterin (Cys) (covalent) #status !8predicted\ !$443 #disulfide_bonds interchain #status predicted\ !$543 #binding_site phosphate (Ser) (covalent) (by nitrate !8reductase-inactivating kinase) #status experimental\ !$586,609 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$741,898 #binding_site NAD (Lys, Cys) #status predicted\ !$781 #binding_site FAD (Tyr) #status predicted SUMMARY #length 926 #molecular-weight 103970 #checksum 1366 SEQUENCE /// ENTRY RDBJNH #type complete TITLE nitrate reductase [NAD(P)H] (EC 1.7.1.2) - European white birch ORGANISM #formal_name Betula pendula #common_name European white birch DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 03-Jun-2002 ACCESSIONS S15959 REFERENCE S15959 !$#authors Friemann, A.; Brinkmann, K.; Hachtel, W. !$#journal Mol. Gen. Genet. (1991) 227:97-105 !$#title Sequence of a cDNA encoding the bi-specific NAD(P)H-nitrate !1reductase from the tree Betula pendula and identification of !1conserved protein regions. !$#cross-references MUID:91260687; PMID:1675424 !$#accession S15959 !'##molecule_type mRNA !'##residues 1-898 ##label FRI !'##cross-references EMBL:X54097; NID:g17924; PIDN:CAA38031.1; !1PID:g17925 !'##note the authors translated the codon CAC for residue 31 as Arg and !1CGG for residue 32 as His CLASSIFICATION #superfamily nitrate reductase (NADH); cytochrome b5 core !1homology; cytochrome-b5 reductase homology; !1molybdopterin-binding domain homology KEYWORDS chromoprotein; electron transfer; FAD; flavoprotein; heme; !1homodimer; iron; metalloprotein; molybdenum; molybdopterin; !1NAD; NADP; nitrate assimilation; oxidoreductase; !1phosphoprotein FEATURE !$76-468 #domain molybdopterin-binding domain homology #label !8PCO\ !$528-602 #domain cytochrome b5 core homology #label CB5\ !$649-898 #domain cytochrome-b5 reductase homology #label CBR\ !$180 #binding_site molybdopterin (Cys) (covalent) #status !8predicted\ !$419 #disulfide_bonds interchain #status predicted\ !$563,586 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$713,870 #binding_site NAD(P) (Lys, Cys) #status predicted\ !$753 #binding_site FAD (Tyr) #status predicted SUMMARY #length 898 #molecular-weight 101001 #checksum 9371 SEQUENCE /// ENTRY RDBHNH #type complete TITLE nitrate reductase (NADH) (EC 1.7.1.1) - barley (cv. Himalaya) ORGANISM #formal_name Hordeum vulgare #common_name barley DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 03-Jun-2002 ACCESSIONS S17453 REFERENCE S17453 !$#authors Schnorr, K.M.; Juricek, M.; Huang, C.; Culley, D.; !1Kleinhofs, A. !$#journal Mol. Gen. Genet. (1991) 227:411-416 !$#title Analysis of barley nitrate reductase cDNA and genomic !1clones. !$#cross-references MUID:91326031; PMID:1865878 !$#accession S17453 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-915 ##label SCH !'##cross-references EMBL:X57845; NID:g18993; PIDN:CAA40976.1; !1PID:g18994 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1February 1991 GENETICS !$#map_position 6 !$#introns 391/1 CLASSIFICATION #superfamily nitrate reductase (NADH); cytochrome b5 core !1homology; cytochrome-b5 reductase homology; !1molybdopterin-binding domain homology KEYWORDS chromoprotein; electron transfer; FAD; flavoprotein; heme; !1homodimer; iron; metalloprotein; molybdenum; molybdopterin; !1NAD; nitrate assimilation; oxidoreductase; phosphoprotein FEATURE !$85-477 #domain molybdopterin-binding domain homology #label !8PCO\ !$538-612 #domain cytochrome b5 core homology #label CB5\ !$661-915 #domain cytochrome-b5 reductase homology #label CBR\ !$189 #binding_site molybdopterin (Cys) (covalent) #status !8predicted\ !$428 #disulfide_bonds interchain #status predicted\ !$573,596 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$725,887 #binding_site NAD (Lys, Cys) #status predicted\ !$766 #binding_site FAD (Tyr) #status predicted SUMMARY #length 915 #molecular-weight 101770 #checksum 3558 SEQUENCE /// ENTRY RDBHNS #type fragment TITLE nitrate reductase (NADH) (EC 1.7.1.1) - barley (cv. Steptoe) (fragment) ORGANISM #formal_name Hordeum vulgare #common_name barley DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 03-Jun-2002 ACCESSIONS S17454 REFERENCE S17453 !$#authors Schnorr, K.M.; Juricek, M.; Huang, C.; Culley, D.; !1Kleinhofs, A. !$#journal Mol. Gen. Genet. (1991) 227:411-416 !$#title Analysis of barley nitrate reductase cDNA and genomic !1clones. !$#cross-references MUID:91326031; PMID:1865878 !$#accession S17454 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type mRNA !'##residues 1-912 ##label SCH !'##cross-references EMBL:X57844; NID:g19044; PIDN:CAA40975.1; !1PID:g19045 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1February 1991 GENETICS !$#map_position 6 CLASSIFICATION #superfamily nitrate reductase (NADH); cytochrome b5 core !1homology; cytochrome-b5 reductase homology; !1molybdopterin-binding domain homology KEYWORDS chromoprotein; electron transfer; FAD; flavoprotein; heme; !1homodimer; iron; metalloprotein; molybdenum; molybdopterin; !1NAD; nitrate assimilation; oxidoreductase; phosphoprotein FEATURE !$82-474 #domain molybdopterin-binding domain homology #label !8PCO\ !$535-609 #domain cytochrome b5 core homology #label CB5\ !$658-912 #domain cytochrome-b5 reductase homology #label CBR\ !$186 #binding_site molybdopterin (Cys) (covalent) #status !8predicted\ !$425 #disulfide_bonds interchain #status predicted\ !$570,593 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$722,884 #binding_site NAD (Lys, Cys) #status predicted\ !$763 #binding_site FAD (Tyr) #status predicted SUMMARY #length 912 #checksum 1642 SEQUENCE /// ENTRY RDBHNP #type complete TITLE nitrate reductase [NAD(P)H] (EC 1.7.1.2) - barley ORGANISM #formal_name Hordeum vulgare #common_name barley DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 03-Jun-2002 ACCESSIONS S16895 REFERENCE S16895 !$#authors Miyazaki, J.; Juricek, M.; Angelis, K.; Schnorr, K.M.; !1Kleinhofs, A.; Warner, R.L. !$#journal Mol. Gen. Genet. (1991) 228:329-334 !$#title Characterization and sequence of a novel nitrate reductase !1from barley. !$#cross-references MUID:91375416; PMID:1896007 !$#accession S16895 !'##molecule_type DNA !'##residues 1-891 ##label MIY !'##cross-references EMBL:X60173; NID:g19064; PIDN:CAA42739.1; !1PID:g19065 GENETICS !$#gene Nar-7 !$#introns 321/3; 368/3 CLASSIFICATION #superfamily nitrate reductase (NADH); cytochrome b5 core !1homology; cytochrome-b5 reductase homology; !1molybdopterin-binding domain homology KEYWORDS chromoprotein; electron transfer; FAD; flavoprotein; heme; !1homodimer; iron; metalloprotein; molybdenum; molybdopterin; !1NAD; NADP; nitrate assimilation; oxidoreductase; !1phosphoprotein FEATURE !$64-455 #domain molybdopterin-binding domain homology #label !8PCO\ !$515-589 #domain cytochrome b5 core homology #label CB5\ !$637-891 #domain cytochrome-b5 reductase homology #label CBR\ !$168 #binding_site molybdopterin (Cys) (covalent) #status !8predicted\ !$406 #disulfide_bonds interchain #status predicted\ !$550,573 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$701,863 #binding_site NAD(P) (Lys, Cys) #status predicted\ !$741 #binding_site FAD (Tyr) #status predicted SUMMARY #length 891 #molecular-weight 98630 #checksum 4122 SEQUENCE /// ENTRY JN0803 #type complete TITLE nitrate reductase (NADPH) (EC 1.7.1.3) - fungus (Fusarium oxysporum) ORGANISM #formal_name Fusarium oxysporum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS JN0803; S35748 REFERENCE JN0803 !$#authors Diolez, A.; Langin, T.; Gerlinger, C.; Brygoo, Y.; Daboussi, !1M.J. !$#journal Gene (1993) 131:61-67 !$#title The nia gene of Fusarium oxysporum: Isolation, sequence and !1development of a homologous transformation system. !$#cross-references MUID:93380674; PMID:8370541 !$#accession JN0803 !'##molecule_type DNA !'##residues 1-905 ##label DIO !'##cross-references EMBL:Z22549; NID:g296098; PIDN:CAA80270.1; !1PID:g296099 !'##note the authors translated the codon AAC for residue 472 as Met GENETICS !$#gene nia !$#introns 604/1 COMPLEX homodimer CLASSIFICATION #superfamily nitrate reductase (NADH); cytochrome b5 core !1homology; cytochrome-b5 reductase homology; !1molybdopterin-binding domain homology KEYWORDS chromoprotein; electron transfer; FAD; flavoprotein; heme; !1homodimer; iron; metalloprotein; molybdenum; molybdopterin; !1NADP; nitrate assimilation; oxidoreductase; phosphoprotein FEATURE !$72-477 #domain molybdopterin-binding domain homology #label !8PCO\ !$546-620 #domain cytochrome b5 core homology #label CB5\ !$655-905 #domain cytochrome-b5 reductase homology #label CBR\ !$179 #binding_site molybdopterin (Cys) (covalent) #status !8predicted\ !$428 #disulfide_bonds interchain #status predicted\ !$581,604 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$721,879 #binding_site NADP (Lys, Cys) #status predicted\ !$758 #binding_site FAD (Tyr) #status predicted SUMMARY #length 905 #molecular-weight 101898 #checksum 1734 SEQUENCE /// ENTRY JH0182 #type complete TITLE nitrate reductase (NADPH) (EC 1.7.1.3) - Emericella nidulans ORGANISM #formal_name Emericella nidulans, Aspergillus nidulans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS JH0182; PS0300 REFERENCE JH0181 !$#authors Johnstone, I.L.; McCabe, P.C.; Greaves, P.; Gurr, S.J.; !1Cole, G.E.; Brow, M.A.D.; Unkles, S.E.; Clutterbuck, A.J.; !1Kinghorn, J.R.; Innis, M.A. !$#journal Gene (1990) 90:181-192 !$#title Isolation and characterisation of the crnA-niiA-niaD gene !1cluster for nitrate assimilation in Aspergillus nidulans. !$#cross-references MUID:90382664; PMID:2205530 !$#accession JH0182 !'##molecule_type DNA !'##residues 1-873 ##label JOH !'##cross-references GB:M58291; NID:g168061; PIDN:AAA33314.1; !1PID:g168062 !$#accession PS0300 !'##molecule_type mRNA !'##residues 1-873 ##label JO2 !'##cross-references GB:M58291; NID:g168061; PIDN:AAA33314.1; !1PID:g168062 GENETICS !$#gene niaD !$#introns 89/1; 122/2; 208/3; 287/2; 362/1; 570/1 COMPLEX homodimer CLASSIFICATION #superfamily nitrate reductase (NADH); cytochrome b5 core !1homology; cytochrome-b5 reductase homology; !1molybdopterin-binding domain homology KEYWORDS chromoprotein; electron transfer; FAD; flavoprotein; heme; !1homodimer; iron; metalloprotein; molybdenum; molybdopterin; !1NADP; nitrate assimilation; oxidoreductase; phosphoprotein FEATURE !$43-446 #domain molybdopterin-binding domain homology #label !8PCO\ !$512-586 #domain cytochrome b5 core homology #label CB5\ !$623-873 #domain cytochrome-b5 reductase homology #label CBR\ !$150 #binding_site molybdopterin (Cys) (covalent) #status !8predicted\ !$397 #disulfide_bonds interchain #status predicted\ !$547,570 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$691,847 #binding_site NADP (Lys, Cys) #status predicted\ !$728 #binding_site FAD (Tyr) #status predicted SUMMARY #length 873 #molecular-weight 97559 #checksum 5435 SEQUENCE /// ENTRY JQ1525 #type complete TITLE nitrate reductase (NADPH) (EC 1.7.1.3) - Aspergillus niger ORGANISM #formal_name Aspergillus niger DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS JQ1525 REFERENCE JQ1525 !$#authors Unkles, S.E.; Campbell, E.I.; Punt, P.J.; Hawker, K.L.; !1Contreras, R.; Hawkins, A.R.; Van den Hondel, C.A.M.J.J.; !1Kinghorn, J.R. !$#journal Gene (1992) 111:149-155 !$#title The Aspergillus niger niaD gene encoding nitrate reductase: !1upstream nucleotide and amino acid sequence comparisons. !$#cross-references MUID:92175518; PMID:1541396 !$#accession JQ1525 !'##molecule_type DNA !'##residues 1-867 ##label UNK !'##cross-references GB:M77022 GENETICS !$#gene niaD !$#introns 91/1; 124/2; 210/3; 289/2; 364/1; 572/1 COMPLEX homodimer CLASSIFICATION #superfamily nitrate reductase (NADH); cytochrome b5 core !1homology; cytochrome-b5 reductase homology; !1molybdopterin-binding domain homology KEYWORDS chromoprotein; electron transfer; FAD; flavoprotein; heme; !1homodimer; iron; metalloprotein; molybdenum; molybdopterin; !1NADP; nitrate assimilation; oxidoreductase; phosphoprotein FEATURE !$45-448 #domain molybdopterin-binding domain homology #label !8PCO\ !$514-588 #domain cytochrome b5 core homology #label CB5\ !$622-867 #domain cytochrome-b5 reductase homology #label CBR\ !$152 #binding_site molybdopterin (Cys) (covalent) #status !8predicted\ !$399 #disulfide_bonds interchain #status predicted\ !$549,572 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$688,841 #binding_site NADP (Lys, Cys) #status predicted\ !$725 #binding_site FAD (Tyr) #status predicted SUMMARY #length 867 #molecular-weight 97188 #checksum 4803 SEQUENCE /// ENTRY S16292 #type complete TITLE nitrate reductase (NADPH) (EC 1.7.1.3) - Neurospora crassa ORGANISM #formal_name Neurospora crassa DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S16292; S07176; S34796; S37298 REFERENCE S16292 !$#authors Okamoto, P.M.; Fu, Y.H.; Marzluf, G.A. !$#journal Mol. Gen. Genet. (1991) 227:213-223 !$#title Nit-3, the structural gene of nitrate reductase in !1Neurospora crassa: nucleotide sequence and regulation of !1mRNA synthesis and turnover. !$#cross-references MUID:91287699; PMID:1829499 !$#accession S16292 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-982 ##label MOL !'##note the authors translated the codon CGC for residue 140 as Pro REFERENCE S07176 !$#authors Le, K.H.D.; Lederer, F. !$#journal EMBO J. (1983) 2:1909-1914 !$#title On the presence of a heme-binding domain homologous to !1cytochrome b5 in Neurospora crassa assimilatory nitrate !1reductase. !$#accession S07176 !'##molecule_type protein !'##residues 'D',622-623,'Y',624,'IK',627,'Y',628,'XNXKXT',635, !1'LILHYKX',643,'DL',646,'K',648,'XXX',652-655,'XE' ##label !1LEK GENETICS !$#gene nit-3 !$#introns 675/1 COMPLEX homodimer CLASSIFICATION #superfamily nitrate reductase (NADH); cytochrome b5 core !1homology; cytochrome-b5 reductase homology; !1molybdopterin-binding domain homology KEYWORDS chromoprotein; electron transfer; FAD; flavoprotein; heme; !1homodimer; iron; metalloprotein; molybdenum; molybdopterin; !1NADP; nitrate assimilation; oxidoreductase; phosphoprotein FEATURE !$121-548 #domain molybdopterin-binding domain homology #label !8PCO\ !$617-691 #domain cytochrome b5 core homology #label CB5\ !$728-982 #domain cytochrome-b5 reductase homology #label CBR\ !$240 #binding_site molybdopterin (Cys) (covalent) #status !8predicted\ !$499 #disulfide_bonds interchain #status predicted\ !$652,675 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$796,956 #binding_site NADP (Lys, Cys) #status predicted\ !$835 #binding_site FAD (Tyr) #status predicted SUMMARY #length 982 #molecular-weight 108457 #checksum 8267 SEQUENCE /// ENTRY JC4283 #type complete TITLE nitrate reductase (NADPH) (EC 1.7.1.3) - Aspergillus oryzae ORGANISM #formal_name Aspergillus oryzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS JC4283 REFERENCE JC4283 !$#authors Kitamoto, N.; Kimura, T.; Kito, Y.; Ohmiya, K.; Tsukagoshi, !1N. !$#journal Biosci. Biotechnol. Biochem. (1995) 59:1795-1797 !$#title The nitrate reductase gene from a shoyu koji mold, !1Aspergillus oryzae KBN616. !$#cross-references MUID:96014424; PMID:8520125 !$#accession JC4283 !'##molecule_type DNA !'##residues 1-868 ##label KIT !'##cross-references DDBJ:D49701; NID:g1136628; PIDN:BAA08551.1; !1PID:g1136629 !'##experimental_source strain KBN616 transformed with plasmid pND300 GENETICS !$#gene niaD !$#introns 91/1; 124/2; 210/3; 289/2; 364/1; 572/1 CLASSIFICATION #superfamily nitrate reductase (NADH); cytochrome b5 core !1homology; cytochrome-b5 reductase homology; !1molybdopterin-binding domain homology KEYWORDS heme; iron; metalloprotein; molybdenum; molybdopterin; NADP; !1oxidoreductase; phosphoprotein FEATURE !$45-448 #domain molybdopterin-binding domain homology #label !8PCO\ !$514-588 #domain cytochrome b5 core homology #label CB5\ !$622-868 #domain cytochrome-b5 reductase homology #label CBR\ !$152 #binding_site molybdopterin (Cys) (covalent) #status !8predicted\ !$549,572 #binding_site heme iron (His) (axial ligands) #status !8predicted SUMMARY #length 868 #molecular-weight 97530 #checksum 87 SEQUENCE /// ENTRY S57199 #type complete TITLE nitrate reductase (NADPH) (EC 1.7.1.3) - Phytophthora infestans ORGANISM #formal_name Phytophthora infestans #common_name potato late blight agent DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S57199 REFERENCE S57199 !$#authors Pieterse, C.M.J.; van't Klooster, J.; van den Berg-Velthuis, !1G.C.M.; Govers, F. !$#journal Curr. Genet. (1995) 27:359-366 !$#title NiaA, the structural nitrate reductase gene of Phytophthora !1infestans: isolation, characterization and expression !1analysis in Aspergillus nidulans. !$#cross-references MUID:95339410; PMID:7614559 !$#accession S57199 !'##status preliminary !'##molecule_type DNA !'##residues 1-902 ##label PIE !'##cross-references EMBL:U14405; NID:g1176368; PIDN:AAA86681.1; !1PID:g538158 GENETICS !$#introns 67/3 CLASSIFICATION #superfamily nitrate reductase (NADH); cytochrome b5 core !1homology; cytochrome-b5 reductase homology; !1molybdopterin-binding domain homology KEYWORDS heme; iron; metalloprotein; molybdenum; molybdopterin; !1oxidoreductase; phosphoprotein FEATURE !$78-468 #domain molybdopterin-binding domain homology #label !8PCO\ !$537-611 #domain cytochrome b5 core homology #label CB5\ !$644-902 #domain cytochrome-b5 reductase homology #label CBR\ !$182 #binding_site molybdopterin (Cys) (covalent) #status !8predicted\ !$572,595 #binding_site heme iron (His) (axial ligands) #status !8predicted SUMMARY #length 902 #molecular-weight 101074 #checksum 8433 SEQUENCE /// ENTRY S65938 #type complete TITLE nitrate reductase [NAD(P)H] (EC 1.7.1.2) - yeast (Pichia angusta) ALTERNATE_NAMES assimilatory nitrate reductase ORGANISM #formal_name Pichia angusta DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S65938; T43157 REFERENCE S65938 !$#authors Avila, J.; Perez, M.D.; Brito, N.; Gonzalez, C.; Siverio, !1J.M. !$#journal FEBS Lett. (1995) 366:137-142 !$#title Cloning and disruption of the YNR1 gene encoding the nitrate !1reductase apoenzyme of the yeast Hansenula polymorpha. !$#cross-references MUID:95309418; PMID:7789531 !$#accession S65938 !'##status preliminary !'##molecule_type DNA !'##residues 1-859 ##label AVI !'##cross-references EMBL:Z49110; NID:g902625; PIDN:CAA88925.1; !1PID:g902626 REFERENCE Z22318 !$#authors Siverio, J.M. !$#submission submitted to the EMBL Data Library, January 1998 !$#accession T43157 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-859 ##label SIV !'##cross-references EMBL:AJ223294; PIDN:CAA11232.1 GENETICS !$#gene YNR1 CLASSIFICATION #superfamily nitrate reductase (NADH); cytochrome b5 core !1homology; cytochrome-b5 reductase homology; !1molybdopterin-binding domain homology KEYWORDS heme; iron; metalloprotein; molybdenum; molybdopterin; NADP; !1oxidoreductase; phosphoprotein FEATURE !$30-432 #domain molybdopterin-binding domain homology #label !8PCO\ !$504-577 #domain cytochrome b5 core homology #label CB5\ !$609-859 #domain cytochrome-b5 reductase homology #label CBR\ !$137 #binding_site molybdopterin (Cys) (covalent) #status !8predicted\ !$538,561 #binding_site heme iron (His) (axial ligands) #status !8predicted SUMMARY #length 859 #molecular-weight 98533 #checksum 7716 SEQUENCE /// ENTRY JN0804 #type complete TITLE nitrate reductase (NADPH) (EC 1.7.1.3) - smut fungus (Ustilago maydis) ORGANISM #formal_name Ustilago maydis #common_name corn smut DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS JN0804; S25516 REFERENCE JN0804 !$#authors Banks, G.R.; Shelton, P.A.; Kanuga, N.; Holden, D.W.; !1Spanos, A. !$#journal Gene (1993) 131:69-78 !$#title The Ustilago maydis nar1 gene encoding nitrate reductase !1activity: Sequence and transcriptional regulation. !$#cross-references MUID:93380675; PMID:8370542 !$#accession JN0804 !'##molecule_type DNA !'##residues 1-908 ##label BAN !'##cross-references EMBL:X67687; NID:g5226; PIDN:CAA47918.1; PID:g5227 GENETICS !$#gene nar1 CLASSIFICATION #superfamily nitrate reductase (NADH); cytochrome b5 core !1homology; cytochrome-b5 reductase homology; !1molybdopterin-binding domain homology KEYWORDS electron transfer; FAD; flavoprotein; heme; iron; !1metalloprotein; molybdenum; molybdopterin; NADP; nitrate !1assimilation; oxidoreductase; phosphoprotein FEATURE !$8-435 #domain molybdopterin-binding domain homology #label !8PCO\ !$516-591 #domain cytochrome b5 core homology #label CB5\ !$624-908 #domain cytochrome-b5 reductase homology #label CBR\ !$116 #binding_site molybdopterin (Cys) (covalent) #status !8predicted\ !$551,575 #binding_site heme iron (His) (axial ligands) #status !8predicted SUMMARY #length 908 #molecular-weight 101524 #checksum 9196 SEQUENCE /// ENTRY JC1422 #type complete TITLE nitrate reductase (NADH) (EC 1.7.1.1) - Volvox carteri ORGANISM #formal_name Volvox carteri DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS JC1422; S22192 REFERENCE JC1422 !$#authors Gruber, H.; Goetinck, S.D.; Kirk, D.L.; Schmitt, R. !$#journal Gene (1992) 120:75-83 !$#title The nitrate reductase-encoding gene of Volvox carteri: Map !1location, sequence and induction kinetics. !$#cross-references MUID:93013022; PMID:1398126 !$#accession JC1422 !'##molecule_type DNA !'##residues 1-864 ##label GR2 !'##cross-references EMBL:X64136; NID:g21993; PIDN:CAA45497.1; !1PID:g21994 !'##note submitted to the EMBL Data Library, January 1992 GENETICS !$#gene nitA !$#map_position linkage group IX !$#introns 183/3; 234/2; 295/1; 339/1; 372/1; 425/2; 521/3; 593/3; 677/ !13; 797/2 FUNCTION !$#description catalyzes the reduction of nitrate to nitrite CLASSIFICATION #superfamily nitrate reductase (NADH); cytochrome b5 core !1homology; cytochrome-b5 reductase homology; !1molybdopterin-binding domain homology KEYWORDS dimer; electron transfer; FAD; flavoprotein; heme; iron; !1metalloprotein; molybdenum; molybdopterin; NAD; nitrate !1assimilation; oxidoreductase; phosphoprotein FEATURE !$36-425 #domain molybdopterin-binding domain homology #label !8PCO\ !$497-571 #domain cytochrome b5 core homology #label CB5\ !$613-864 #domain cytochrome-b5 reductase homology #label CBR\ !$139 #binding_site molybdopterin (Cys) (covalent) #status !8predicted\ !$532,555 #binding_site heme iron (His) (axial ligands) #status !8predicted SUMMARY #length 864 #molecular-weight 96401 #checksum 6412 SEQUENCE /// ENTRY S05441 #type complete TITLE cytochrome b5-related protein TU-36B - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S05441 REFERENCE S05441 !$#authors Levin, R.J.; Boychuk, P.L.; Croniger, C.M.; Kazzaz, J.A.; !1Rozek, C.E. !$#journal Nucleic Acids Res. (1989) 17:6349-6367 !$#title Structure and expression of a muscle specific gene which is !1adjacent to the Drosophila myosin heavy-chain gene and can !1encode a cytochrome b related protein. !$#cross-references MUID:89366661; PMID:2549511 !$#accession S05441 !'##molecule_type DNA !'##residues 1-414 ##label LEV !'##cross-references EMBL:X15008; NID:g8748; PIDN:CAA33113.1; !1PID:g295756 !'##note 202-Ala, 213-Ile, and 344-Arg were also found GENETICS !$#gene FlyBase:Cyt-b5 !'##cross-references FlyBase:FBgn0000406 !$#map_position 2 36B !$#introns 138/3 CLASSIFICATION #superfamily fruit fly protein TU-36B; cytochrome b5 core !1homology KEYWORDS heme; iron; metalloprotein FEATURE !$25-99 #domain cytochrome b5 core homology #label CB5\ !$59,82 #binding_site heme iron (His) (axial ligands) #status !8predicted SUMMARY #length 414 #molecular-weight 47147 #checksum 3576 SEQUENCE /// ENTRY B32902 #type complete TITLE GMP reductase (EC 1.7.1.7) - human ALTERNATE_NAMES guanosine monophosphate reductase ORGANISM #formal_name Homo sapiens #common_name man DATE 04-Jun-1999 #sequence_revision 04-Jun-1999 #text_change 03-Jun-2002 ACCESSIONS B32902; A55285 REFERENCE A32902 !$#authors Kanno, H.; Huang, I.Y.; Kan, Y.W.; Yoshida, A. !$#journal Cell (1989) 58:595-606 !$#title Two structural genes on different chromosomes are required !1for encoding the major subunit of human red cell !1glucose-6-phosphate dehydrogenase. !$#cross-references MUID:89336791; PMID:2758468 !$#accession B32902 !'##molecule_type mRNA !'##residues 1-345 ##label KAN !'##cross-references GB:M24470; NID:g182866; PIDN:AAA52498.1; !1PID:g182867; GB:M27958 REFERENCE A55285 !$#authors Kondoh, T.; Kanno, H.; Chang, L.; Yoshida, A. !$#journal Hum. Genet. (1991) 88:219-224 !$#title Genomic structure and expression of human guanosine !1monophosphate reductase. !$#cross-references MUID:92098099; PMID:1661705 !$#accession A55285 !'##status preliminary; translation not shown !'##molecule_type DNA !'##residues 1-233,'A',235-255,'F',257-345 ##label KON !'##cross-references GB:S73035 REFERENCE A55176 !$#authors Henikoff, S.; Smith, J.M. !$#journal Cell (1989) 58:1021-1022 !$#title The human mRNA that provides the N-terminus of chimeric G6PD !1encodes GMP reductase. !$#cross-references MUID:89376552; PMID:2570640 !$#contents annotation REFERENCE A55177 !$#authors Yoshida, A.; Kan, Y.W. !$#journal Cell (1990) 62:11-12 !$#title Origin of "fused" glucose-6-phosphate dehydrogenase. !$#cross-references MUID:90304899; PMID:1694726 !$#contents annotation GENETICS !$#gene GDB:GMPR !'##cross-references GDB:127058; OMIM:139265 !$#map_position 6pter-6qter FUNCTION !$#description catalyzes the reductive deamination of GMP into IMP using !1NADPH !$#pathway purine catabolism CLASSIFICATION #superfamily GMP reductase; IMP dehydrogenase amino-terminal !1homology; IMP dehydrogenase catalytic homology KEYWORDS NADP; oxidoreductase; purine catabolism FEATURE !$10-81 #domain IMP dehydrogenase amino-terminal homology !8#label IDHN\ !$88-324 #domain IMP dehydrogenase catalytic homology #label !8IDHC\ !$186 #active_site Cys #status predicted SUMMARY #length 345 #molecular-weight 37415 #checksum 4889 SEQUENCE /// ENTRY T03917 #type complete TITLE GMP reductase (EC 1.7.1.7) F32D1.5 - Caenorhabditis elegans ALTERNATE_NAMES guanosine monophosphate reductase ORGANISM #formal_name Caenorhabditis elegans DATE 04-Jun-1999 #sequence_revision 04-Jun-1999 #text_change 03-Jun-2002 ACCESSIONS T03917 REFERENCE Z15134 !$#authors Becker, M.; Bradshaw, H.; Kramer, J. !$#submission submitted to the EMBL Data Library, July 1997 !$#description The sequence of C. elegans cosmid F32D1. !$#accession T03917 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-358 ##label BEC !'##cross-references EMBL:AF016427; NID:g2291228; PIDN:AAB65350.1; !1PID:g2291231 GENETICS !$#map_position V !$#introns 81/3; 262/3 !$#note F32D1.5 FUNCTION !$#description catalyzes the reductive deamination of GMP into IMP using !1NADPH !$#pathway purine catabolism CLASSIFICATION #superfamily GMP reductase; IMP dehydrogenase amino-terminal !1homology; IMP dehydrogenase catalytic homology KEYWORDS NADP; oxidoreductase; purine catabolism FEATURE !$10-81 #domain IMP dehydrogenase amino-terminal homology !8#label IDHN\ !$89-325 #domain IMP dehydrogenase catalytic homology #label !8IDHC\ !$187 #active_site Cys #status predicted SUMMARY #length 358 #molecular-weight 38806 #checksum 4053 SEQUENCE /// ENTRY H64732 #type complete TITLE GMP reductase (EC 1.7.1.7) guaC [similarity] - Escherichia coli (strain K-12) ALTERNATE_NAMES guanosine monophosphate reductase ORGANISM #formal_name Escherichia coli DATE 04-Jun-1999 #sequence_revision 04-Jun-1999 #text_change 03-Jun-2002 ACCESSIONS H64732; S01671; S45182 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64732 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-347 ##label BLAT !'##cross-references GB:AE000119; GB:U00096; NID:g1786283; !1PIDN:AAC73215.1; PID:g1786293; UWGP:b0104 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S01671 !$#authors Andrews, S.C.; Guest, J.R. !$#journal Biochem. J. (1988) 255:35-43 !$#title Nucleotide sequence of the gene encoding the GMP reductase !1of Escherichia coli K12. !$#cross-references MUID:89061679; PMID:2904262 !$#accession S01671 !'##molecule_type DNA !'##residues 1-232,'AR',236-347 ##label AND !'##cross-references EMBL:X07917; NID:g42615; PIDN:CAA30751.1; !1PID:g42616 !'##experimental_source strain K-12 JM101 REFERENCE S45181 !$#authors Fujita, N. !$#submission submitted to the EMBL Data Library, January 1994 !$#accession S45182 !'##molecule_type DNA !'##residues 1-232,'AR',236-347 ##label FUJ !'##cross-references EMBL:D26562; NID:g473770; PIDN:BAA05561.1; !1PID:g473772 GENETICS !$#gene guaC !$#map_position 3 min FUNCTION !$#description catalyzes the reductive deamination of GMP into IMP using !1NADPH !$#pathway purine catabolism CLASSIFICATION #superfamily GMP reductase; IMP dehydrogenase amino-terminal !1homology; IMP dehydrogenase catalytic homology KEYWORDS NADP; oxidoreductase; purine catabolism FEATURE !$9-80 #domain IMP dehydrogenase amino-terminal homology !8#label IDHN\ !$88-324 #domain IMP dehydrogenase catalytic homology #label !8IDHC\ !$186 #active_site Cys #status predicted SUMMARY #length 347 #molecular-weight 37383 #checksum 5330 SEQUENCE /// ENTRY F64626 #type complete TITLE probable GMP reductase (EC 1.7.1.7) - Helicobacter pylori (strain 26695) ALTERNATE_NAMES guanosine monophosphate reductase ORGANISM #formal_name Helicobacter pylori DATE 04-Jun-1999 #sequence_revision 04-Jun-1999 #text_change 03-Jun-2002 ACCESSIONS F64626 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession F64626 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-327 ##label TOM !'##cross-references GB:AE000596; GB:AE000511; NID:g2313982; !1PIDN:AAD07901.1; PID:g2313987; TIGR:HP0854 FUNCTION !$#description catalyzes the reductive deamination of GMP into IMP using !1NADPH !$#pathway purine catabolism CLASSIFICATION #superfamily GMP reductase; IMP dehydrogenase amino-terminal !1homology; IMP dehydrogenase catalytic homology KEYWORDS NADP; oxidoreductase; purine catabolism FEATURE !$6-72 #domain IMP dehydrogenase amino-terminal homology !8#label IDHN\ !$76-306 #domain IMP dehydrogenase catalytic homology #label !8IDHC\ !$176 #active_site Cys #status predicted SUMMARY #length 327 #molecular-weight 36038 #checksum 7430 SEQUENCE /// ENTRY A71887 #type complete TITLE probable GMP reductase (EC 1.7.1.7) - Helicobacter pylori (strain J99) ALTERNATE_NAMES guanosine monophosphate reductase ORGANISM #formal_name Helicobacter pylori #variety strain J99 DATE 04-Jun-1999 #sequence_revision 04-Jun-1999 #text_change 03-Jun-2002 ACCESSIONS A71887 REFERENCE A71800 !$#authors Alm, R.A.; Ling, L.S.L.; Moir, D.T.; King, B.L.; Brown, !1E.D.; Doig, P.C.; Smith, D.R.; Noonan, B.; Guild, B.C.; !1deJonge, B.L.; Carmel, G.; Tummino, P.J.; Caruso, A.; !1Uria-Nickelsen, M.; Mills, D.M.; Ives, C.; Gibson, R.; !1Merberg, D.; Mills, S.D.; Jiang, Q.; Taylor, D.E.; Vovis, !1G.F.; Trust, T.J. !$#journal Nature (1999) 397:176-180 !$#title Genomic sequence comparison of two unrelated isolates of the !1human gastric pathogen Helicobacter pylori. !$#cross-references MUID:99120557; PMID:9923682 !$#accession A71887 !'##molecule_type DNA !'##residues 1-325 ##label ARN !'##cross-references GB:AE001509; GB:AE001439; NID:g4155350; !1PIDN:AAD06382.1; PID:g4155370 !'##experimental_source strain J99 GENETICS !$#gene guaC FUNCTION !$#description catalyzes the reductive deamination of GMP into IMP using !1NADPH !$#pathway purine catabolism CLASSIFICATION #superfamily GMP reductase; IMP dehydrogenase amino-terminal !1homology; IMP dehydrogenase catalytic homology KEYWORDS NADP; oxidoreductase; purine catabolism FEATURE !$4-70 #domain IMP dehydrogenase amino-terminal homology !8#label IDHN\ !$74-304 #domain IMP dehydrogenase catalytic homology #label !8IDHC\ !$174 #active_site Cys #status predicted SUMMARY #length 325 #molecular-weight 35845 #checksum 3284 SEQUENCE /// ENTRY C70015 #type complete TITLE probable GMP reductase (EC 1.7.1.7) yumD - Bacillus subtilis ALTERNATE_NAMES guanosine monophosphate reductase ORGANISM #formal_name Bacillus subtilis DATE 04-Jun-1999 #sequence_revision 04-Jun-1999 #text_change 03-Jun-2002 ACCESSIONS C70015 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C70015 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-326 ##label KUN !'##cross-references GB:Z99120; GB:AL009126; NID:g2635613; !1PIDN:CAB15203.1; PID:g2635710 !'##experimental_source strain 168 GENETICS !$#gene yumD FUNCTION !$#description catalyzes the reductive deamination of GMP into IMP using !1NADPH !$#pathway purine catabolism CLASSIFICATION #superfamily GMP reductase; IMP dehydrogenase amino-terminal !1homology; IMP dehydrogenase catalytic homology KEYWORDS NADP; oxidoreductase; purine catabolism FEATURE !$5-71 #domain IMP dehydrogenase amino-terminal homology !8#label IDHN\ !$75-305 #domain IMP dehydrogenase catalytic homology #label !8IDHC\ !$175 #active_site Cys #status predicted SUMMARY #length 326 #molecular-weight 35819 #checksum 7996 SEQUENCE /// ENTRY S57699 #type complete TITLE flavohemoglobin - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES flavohemoprotein; protein 399; protein G8572; protein YGR234w ORGANISM #formal_name Saccharomyces cerevisiae DATE 19-Oct-1995 #sequence_revision 03-Nov-1995 #text_change 23-Mar-2001 ACCESSIONS S57699; B45383; A45383; S64558; S63915 REFERENCE S57680 !$#authors van der Aart, Q.J.M.; Kleine, K.; Steensma, H.Y. !$#submission submitted to the EMBL Data Library, June 1995 !$#description Sequence analysis of the 43 KB !1CRM1-YLM9-PET54-SMI1-PHO81-YHB4-PFK1 region from the right !1arm of Saccharomyces cerevisiae chromosome VII. !$#accession S57699 !'##molecule_type DNA !'##residues 1-399 ##label VAN !'##cross-references EMBL:X87941; NID:g886908; PIDN:CAA61184.1; !1PID:g886928 !'##experimental_source strain S288C REFERENCE A45383 !$#authors Zhu, H.; Riggs, A.F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:5015-5019 !$#title Yeast flavohemoglobin is an ancient protein related to !1globins and a reductase family. !$#cross-references MUID:92279256; PMID:1594608 !$#accession B45383 !'##molecule_type DNA !'##residues 1-399 ##label ZHU !'##cross-references GB:L07071; NID:g171515 !'##experimental_source strain DBY939 !'##note this translation is not annotated in GenBank entry YSCFLAHBG, !1release 109.0 !$#accession A45383 !'##molecule_type mRNA !'##residues 1-152,'E',154-344,'D',346-364,'V',366-399 ##label ZHW !'##cross-references GB:L07070; NID:g484239 !'##experimental_source strain JM43 !'##note sequence extracted from NCBI backbone (NCBIP:104352) !'##note this translation is not annotated in GenBank entry YSCFLAVHBC, !1release 109.0 REFERENCE S64541 !$#authors van der Aart, Q.J.M.; Steensma, H.Y. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64558 !'##molecule_type DNA !'##residues 1-399 ##label VAW !'##cross-references EMBL:Z73019; NID:g1323422; PIDN:CAA97262.1; !1PID:g1323423; GSPDB:GN00007; MIPS:YGR234w !'##experimental_source strain S288C REFERENCE S63896 !$#authors van der Aart, Q.J.M.; Kleine, K.; Steensma, H.Y. !$#journal Yeast (1996) 12:385-390 !$#title Sequence analysis of the 43 kb !1CRM1-YLM9-PET54-DIE2-SMI1-PHO81-YHB4-PFK1 region from the !1right arm of Saccharomyces cerevisiae chromosome VII. !$#cross-references MUID:96267763; PMID:8701610 !$#accession S63915 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-399 ##label VAF !'##cross-references EMBL:X87941; NID:g886908; PIDN:CAA61184.1; !1PID:g886928 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1995 GENETICS !$#gene SGD:YHB1; YHB4; MIPS:YGR234w !'##cross-references SGD:S0003466; MIPS:YGR234w !$#map_position 7R CLASSIFICATION #superfamily flavohemoglobin; cytochrome-b5 reductase !1homology; globin homology KEYWORDS chromoprotein; flavoprotein; heme; iron; metalloprotein; !1monomer FEATURE !$2-138 #domain globin homology #label GLB\ !$155-390 #domain cytochrome-b5 reductase homology #label CBR\ !$53 #binding_site oxygen (Gln) (distal axial ligand) !8#status predicted\ !$85 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 399 #molecular-weight 44646 #checksum 8586 SEQUENCE /// ENTRY S15992 #type complete TITLE flavohemoglobin hmp - Escherichia coli (strain K-12) ALTERNATE_NAMES ferrisiderophore reductase fsrB; flavohemoprotein ORGANISM #formal_name Escherichia coli DATE 13-Jan-1995 #sequence_revision 13-Jan-1995 #text_change 01-Mar-2002 ACCESSIONS S15992; S21161; S25241; G65032 REFERENCE S15991 !$#authors Vasudevan, S.G.; Armarego, W.L.F.; Shaw, D.C.; Lilley, P.E.; !1Dixon, N.E.; Poole, R.K. !$#journal Mol. Gen. Genet. (1991) 226:49-58 !$#title Isolation and nucleotide sequence of the hmp gene that !1encodes a haemoglobin-like protein in Escherichia coli K-12. !$#cross-references MUID:91238719; PMID:2034230 !$#accession S15992 !'##molecule_type DNA !'##residues 1-396 ##label VAS !'##cross-references EMBL:X58872; NID:g41730; PIDN:CAA41682.1; !1PID:g41731 REFERENCE S21161 !$#authors Andrews, S.C.; Shipley, D.; Keen, J.N.; Findlay, J.B.C.; !1Harrison, P.M.; Guest, J.R. !$#journal FEBS Lett. (1992) 302:247-252 !$#title The haemoglobin-like protein (HMP) of Escherichia coli has !1ferrisiderophore reductase activity and its C-terminal !1domain shares homology with ferredoxin NADP(+) reductases. !$#cross-references MUID:92290008; PMID:1601132 !$#accession S21161 !'##status preliminary !'##molecule_type DNA !'##residues 1-37,'Q',39-64;359-396 ##label AND REFERENCE S25241 !$#authors Plamann, M.D.; Stauffer, G.V. !$#journal Gene (1983) 22:9-18 !$#title Characterization of the Escherichia coli gene for serine !1hydroxymethyltransferase. !$#cross-references MUID:83235562; PMID:6190704 !$#accession S25241 !'##molecule_type DNA !'##residues 1-10 ##label PLA !'##cross-references EMBL:X58872 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65032 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-396 ##label BLAT !'##cross-references GB:AE000341; GB:U00096; NID:g1788899; !1PIDN:AAC75605.1; PID:g1788903; UWGP:b2552 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene hmpA (hmp) CLASSIFICATION #superfamily flavohemoglobin; cytochrome-b5 reductase !1homology; globin homology KEYWORDS chromoprotein; flavoprotein; heme; iron; metalloprotein; !1monomer FEATURE !$2-136 #domain globin homology #label GLB\ !$157-390 #domain cytochrome-b5 reductase homology #label CBR\ !$53 #binding_site oxygen (Gln) (distal axial ligand) !8#status predicted\ !$85 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 396 #molecular-weight 43867 #checksum 1909 SEQUENCE /// ENTRY S44277 #type complete TITLE flavohemoglobin hmpX - Erwinia chrysanthemi ALTERNATE_NAMES flavohemoprotein ORGANISM #formal_name Erwinia chrysanthemi DATE 13-Jan-1995 #sequence_revision 13-Jan-1995 #text_change 03-Mar-2000 ACCESSIONS S44277 REFERENCE S44277 !$#authors Favey, S.; Labesse, G.; Vouille, V.; Boccara, M. !$#submission submitted to the EMBL Data Library, January 1994 !$#description The flavohemoprotein HmpX: a new determinant of Erwinia !1chrysanthemi strain 3937 virulence. !$#accession S44277 !'##molecule_type DNA !'##residues 1-395 ##label FAV !'##cross-references EMBL:X75893; NID:g479142; PIDN:CAA53500.1; !1PID:g479143 CLASSIFICATION #superfamily flavohemoglobin; cytochrome-b5 reductase !1homology; globin homology KEYWORDS chromoprotein; flavoprotein; heme; iron; metalloprotein; !1monomer FEATURE !$2-136 #domain globin homology #label GLB\ !$157-389 #domain cytochrome-b5 reductase homology #label CBR\ !$53 #binding_site oxygen (Gln) (distal axial ligand) !8#status predicted\ !$85 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 395 #molecular-weight 44315 #checksum 5404 SEQUENCE /// ENTRY A53396 #type complete TITLE flavohemoglobin - Alcaligenes eutrophus ALTERNATE_NAMES flavohemoprotein ORGANISM #formal_name Alcaligenes eutrophus DATE 12-May-1994 #sequence_revision 12-May-1994 #text_change 03-Mar-2000 ACCESSIONS A53396; S42483 REFERENCE A53396 !$#authors Cramm, R.; Siddiqui, R.A.; Friedrich, B. !$#journal J. Biol. Chem. (1994) 269:7349-7354 !$#title Primary sequence and evidence for a physiological function !1of the flavohemoprotein of Alcaligenes eutrophus. !$#cross-references MUID:94171753; PMID:8125952 !$#accession A53396 !'##molecule_type DNA !'##residues 1-403 ##label CRA !'##cross-references GB:X74334; NID:g460998; PIDN:CAA52381.1; !1PID:g460999 COMMENT Both FAD and protoheme IX were bound as cofactors. COMMENT Fhp-negative mutants, unlike the wild type, failed to !1accumulate nitrous oxide during denitrification with nitrite !1as the electron receptor. GENETICS !$#gene fhp CLASSIFICATION #superfamily flavohemoglobin; cytochrome-b5 reductase !1homology; globin homology KEYWORDS chromoprotein; FAD; flavoprotein; heme; iron; !1metalloprotein; monomer FEATURE !$2-138 #domain globin homology #label GLB\ !$159-396 #domain cytochrome-b5 reductase homology #label CBR\ !$53 #binding_site oxygen (Gln) (distal axial ligand) !8#status predicted\ !$85 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 403 #molecular-weight 44796 #checksum 968 SEQUENCE /// ENTRY DEECR #type complete TITLE NADH2 dehydrogenase (EC 1.6.99.3) [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 15-Oct-1982 #sequence_revision 15-Oct-1982 #text_change 03-Jun-2002 ACCESSIONS A00461; B64855 REFERENCE A00461 !$#authors Young, I.G.; Rogers, B.L.; Campbell, H.D.; Jaworowski, A.; !1Shaw, D.C. !$#journal Eur. J. Biochem. (1981) 116:165-170 !$#title Nucleotide sequence coding for the respiratory NADH !1dehydrogenase of Escherichia coli. !$#cross-references MUID:81236546; PMID:6265208 !$#accession A00461 !'##molecule_type DNA !'##residues 1-434 ##label YOU !'##cross-references GB:V00306; GB:J01653; NID:g42112; PIDN:CAA23586.1; !1PID:g581140 !'##experimental_source strain K-12 !'##note part of this sequence, including the amino end, was confirmed !1by protein sequencing REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64855 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-434 ##label BLAT !'##cross-references GB:AE000211; GB:U00096; NID:g1787345; !1PIDN:AAC74193.1; PID:g1787352; UWGP:b1109 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ndh !$#map_position 22 min !$#start_codon TTG FUNCTION !$#description EC 1.6.99.3 [validated, MUID:81236546]; catalyzes the !1transfer of electrons from NADH to the respiratory chain !$#note the immediate electron acceptor for the enzyme is believed !1to be ubiquinone; membrane enzyme containing one !1noncovalently bound FAD per polypeptide chain CLASSIFICATION #superfamily NADH dehydrogenase KEYWORDS electron transfer; FAD; flavoprotein; NAD; oxidoreductase FEATURE !$2-434 #product NADH dehydrogenase #status predicted #label !8MAT\ !$6-41 #region FAD binding #status predicted\ !$170-207 #region NAD binding #status predicted\ !$177-182 #region NADH-binding motif SUMMARY #length 434 #molecular-weight 47358 #checksum 1521 SEQUENCE /// ENTRY B69852 #type complete TITLE probable NADH2 dehydrogenase (EC 1.6.99.3) yjlD - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS B69852 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69852 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-392 ##label KUN !'##cross-references GB:Z99110; GB:AL009126; NID:g2633472; !1PIDN:CAB13086.1; PID:g2633583 !'##experimental_source strain 168 GENETICS !$#gene yjlD CLASSIFICATION #superfamily NADH dehydrogenase KEYWORDS electron transfer; FAD; flavoprotein; NAD; oxidoreductase SUMMARY #length 392 #molecular-weight 41953 #checksum 4888 SEQUENCE /// ENTRY A70015 #type complete TITLE probable NADH2 dehydrogenase (EC 1.6.99.3) yumB - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS A70015 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A70015 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-406 ##label KUN !'##cross-references GB:Z99120; GB:AL009126; NID:g2635613; !1PIDN:CAB15200.1; PID:g2635707 !'##experimental_source strain 168 GENETICS !$#gene yumB CLASSIFICATION #superfamily NADH dehydrogenase KEYWORDS electron transfer; FAD; flavoprotein; NAD; oxidoreductase SUMMARY #length 406 #molecular-weight 44932 #checksum 2045 SEQUENCE /// ENTRY S74826 #type complete TITLE NADH2 dehydrogenase (EC 1.6.99.3) - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein slr0851 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S74826 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74826 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-445 ##label KAN !'##cross-references EMBL:D90909; GB:AB001339; NID:g1652844; !1PIDN:BAA17787.1; PID:g1652869 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene ndh CLASSIFICATION #superfamily NADH dehydrogenase KEYWORDS electron transfer; FAD; flavoprotein; NAD; oxidoreductase SUMMARY #length 445 #molecular-weight 49133 #checksum 886 SEQUENCE /// ENTRY S76810 #type complete TITLE probable NADH2 dehydrogenase (EC 1.6.99.3) - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S76810 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76810 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-524 ##label KAN !'##cross-references EMBL:D90916; GB:AB001339; NID:g1653715; !1PIDN:BAA18722.1; PID:g1653811 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily NADH dehydrogenase KEYWORDS electron transfer; FAD; flavoprotein; NAD; oxidoreductase SUMMARY #length 524 #molecular-weight 56862 #checksum 7185 SEQUENCE /// ENTRY A49911 #type complete TITLE NADH oxidase (hydrogen peroxide-forming) (EC 1.6.-.-) - Amphibacillus xylanus ORGANISM #formal_name Amphibacillus xylanus DATE 18-Nov-1994 #sequence_revision 18-Nov-1994 #text_change 16-Jun-2000 ACCESSIONS A49911 REFERENCE A49911 !$#authors Niimura, Y.; Ohnishi, K.; Yarita, Y.; Hidaka, M.; Masaki, !1H.; Uchimura, T.; Suzuki, H.; Kozaki, M.; Uozumi, T. !$#journal J. Bacteriol. (1993) 175:7945-7950 !$#title A flavoprotein functional as NADH oxidase from Amphibacillus !1xylanus Ep01: purification and characterization of the !1enzyme and structural analysis of its gene. !$#cross-references MUID:94075233; PMID:8253683 !$#accession A49911 !'##molecule_type DNA !'##residues 1-509 ##label NII !'##cross-references GB:D13563; NID:g216219; PIDN:BAA33809.1; !1PID:g216220 !'##note parts of this sequence were confirmed by protein sequencing COMMENT This enzyme, a homotetramer containing one FAD per chain, !1catalyzes the reduction of oxygen to hydrogen peroxide with !1beta-NADH as the preferred electron donor; it exhibits no !1activity with NADPH. CLASSIFICATION #superfamily NADH oxidase (hydrogen peroxide-forming); !1thioredoxin reductase homology KEYWORDS FAD; flavoprotein; homotetramer; oxidoreductase; !1redox-active disulfide FEATURE !$205-506 #domain thioredoxin reductase homology #label TRXB\ !$210-239 #region beta-alpha-beta FAD nucleotide-binding fold\ !$349-377 #region beta-alpha-beta NAD nucleotide-binding fold\ !$461-479 #region FAD binding #status predicted\ !$337-340 #disulfide_bonds redox-active #status predicted SUMMARY #length 509 #molecular-weight 54977 #checksum 8619 SEQUENCE /// ENTRY JC2311 #type complete TITLE NADH oxidase (hydrogen peroxide-forming) (EC 1.6.-.-) precursor - Streptococcus mutans ORGANISM #formal_name Streptococcus mutans DATE 18-Nov-1994 #sequence_revision 18-Nov-1994 #text_change 16-Jun-2000 ACCESSIONS JC2311; PC2207 REFERENCE JC2311 !$#authors Higuchi, M.; Shimada, M.; Matsumoto, J.; Yamamoto, Y.; !1Rhaman, A.; Kamio, Y. !$#journal Biosci. Biotechnol. Biochem. (1994) 58:1603-1607 !$#title Molecular cloning and sequence analysis of the gene encoding !1the H2O2-forming NADH oxidase from Streptococcus mutans. !$#cross-references MUID:95036869; PMID:7765479 !$#accession JC2311 !'##molecule_type DNA !'##residues 1-510 ##label HIG1 !'##cross-references DDBJ:D21803; NID:g415613; PIDN:BAA04825.1; !1PID:g464216 !$#accession PC2207 !'##molecule_type protein !'##residues 2-17 ##label HIG2 GENETICS !$#gene nox-1 CLASSIFICATION #superfamily NADH oxidase (hydrogen peroxide-forming); !1thioredoxin reductase homology KEYWORDS FAD; flavoprotein; oxidoreductase; redox-active disulfide FEATURE !$2-510 #product NADH peroxidase #status experimental #label !8MAT\ !$205-507 #domain thioredoxin reductase homology #label TRXB\ !$210-239 #region beta-alpha-beta FAD nucleotide-binding fold\ !$349-377 #region beta-alpha-beta NAD nucleotide-binding fold\ !$461-479 #region FAD binding #status predicted\ !$337-340 #disulfide_bonds redox-active #status predicted SUMMARY #length 510 #molecular-weight 55188 #checksum 6130 SEQUENCE /// ENTRY B35441 #type complete TITLE alkyl hydroperoxide reductase (EC 1.6.-.-) F52a protein - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 07-Sep-1990 #sequence_revision 18-Nov-1994 #text_change 11-Jun-1999 ACCESSIONS B35441 REFERENCE A35441 !$#authors Tartaglia, L.A.; Storz, G.; Brodsky, M.H.; Lai, A.; Ames, !1B.N. !$#journal J. Biol. Chem. (1990) 265:10535-10540 !$#title Alkyl hydroperoxide reductase from Salmonella typhimurium. !1Sequence and homology to thioredoxin reductase and other !1flavoprotein disulfide oxidoreductases. !$#cross-references MUID:90285183; PMID:2191951 !$#accession B35441 !'##molecule_type DNA !'##residues 1-521 ##label TAR !'##cross-references GB:J05478; NID:g457175; PIDN:AAA16432.1; !1PID:g153863 COMMENT This protein is the catalytic component (composed of two !1identical chains) of the active enzyme. It can use NADH or !1NADPH as electron donors for the direct reduction of alkyl !1hydroperoxides when combined with the other component, C22 !1protein. GENETICS !$#gene ahpF !$#map_position 13 min CLASSIFICATION #superfamily NADH oxidase (hydrogen peroxide-forming); !1thioredoxin reductase homology KEYWORDS FAD; flavoprotein; homodimer; oxidoreductase; redox-active !1disulfide FEATURE !$209-515 #domain thioredoxin reductase homology #label TRXB\ !$214-243 #region beta-alpha-beta FAD nucleotide-binding fold\ !$357-385 #region beta-alpha-beta NAD(P) nucleotide-binding !8fold\ !$470-488 #region FAD binding #status predicted\ !$345-348 #disulfide_bonds redox-active #status predicted SUMMARY #length 521 #molecular-weight 55949 #checksum 2526 SEQUENCE /// ENTRY JX0166 #type complete TITLE NADH oxidase (hydrogen peroxide-forming) (EC 1.6.-.-) - Bacillus sp. (strain YN-1) ALTERNATE_NAMES type I dehydrogenase ORGANISM #formal_name Bacillus sp. DATE 30-Sep-1991 #sequence_revision 18-Nov-1994 #text_change 16-Jun-2000 ACCESSIONS JX0166; PX0020 REFERENCE JX0166 !$#authors Xu, X.; Koyama, N.; Cui, M.; Yamagishi, A.; Nosoh, Y.; !1Oshima, T. !$#journal J. Biochem. (1991) 109:678-683 !$#title Nucleotide sequence of the gene encoding NADH dehydrogenase !1from an alkalophile, Bacillus sp. strain YN-1. !$#cross-references MUID:92011449; PMID:1917890 !$#accession JX0166 !'##molecule_type DNA !'##residues 1-519 ##label XUX !'##cross-references GB:D10701; NID:g216302; PIDN:BAA01545.1; !1PID:g216304 !'##experimental_source strain YN-1 REFERENCE PX0020 !$#authors Xu, X.; Kanaya, S.; Koyama, N.; Sekiguchi, T.; Nosoh, Y.; !1Ohashi, S.; Tsuda, K. !$#journal J. Biochem. (1989) 105:626-632 !$#title Tryptic digestion of NADH dehydrogenase from alkalophilic !1Bacillus. !$#cross-references MUID:89340392; PMID:2760020 !$#contents annotation !$#accession PX0020 !'##molecule_type protein !'##residues 1-34;185-223;517-519 ##label XU2 COMMENT This enzyme catalyzes the electron transfer from NADH to the !1respiratory chain; it is loosely bound to the cytoplasmic !1membrane. COMMENT The sequence of this protein is homologous to the catalytic !1component of alkylhydroperoxide reductase. However, it is !1not clear whether functionally they are equivalent. GENETICS !$#gene ndh CLASSIFICATION #superfamily NADH oxidase (hydrogen peroxide-forming); !1thioredoxin reductase homology KEYWORDS FAD; flavoprotein; homodimer; oxidoreductase; redox-active !1disulfide FEATURE !$205-506 #domain thioredoxin reductase homology #label TRXB\ !$210-239 #region beta-alpha-beta FAD nucleotide-binding fold\ !$349-377 #region beta-alpha-beta NAD nucleotide-binding fold\ !$461-479 #region FAD binding #status predicted\ !$337-340 #disulfide_bonds redox-active #status predicted SUMMARY #length 519 #molecular-weight 55830 #checksum 7942 SEQUENCE /// ENTRY A35441 #type complete TITLE alkyl hydroperoxide reductase (EC 1.6.-.-) C22 protein - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 07-Sep-1990 #sequence_revision 18-Nov-1994 #text_change 19-Oct-1995 ACCESSIONS A35441; S07525 REFERENCE A35441 !$#authors Tartaglia, L.A.; Storz, G.; Brodsky, M.H.; Lai, A.; Ames, !1B.N. !$#journal J. Biol. Chem. (1990) 265:10535-10540 !$#title Alkyl hydroperoxide reductase from Salmonella typhimurium. !1Sequence and homology to thioredoxin reductase and other !1flavoprotein disulfide oxidoreductases. !$#cross-references MUID:90285183; PMID:2191951 !$#accession A35441 !'##molecule_type DNA !'##residues 1-184 ##label TAR !'##cross-references GB:J05478 !'##note the nucleotide sequence given is inconsistent with Genbank !1accession J05478 REFERENCE S07525 !$#authors Tartaglia, L.A.; Storz, G.; Ames, B.N. !$#journal J. Mol. Biol. (1989) 210:709-719 !$#title Identification and molecular analysis of oxyR-regulated !1promoters important for the bacterial adaptation to !1oxidative stress. !$#cross-references MUID:90133925; PMID:2693740 !$#accession S07525 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-21 ##label TA2 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing GENETICS !$#gene ahpC !$#map_position 13 min FUNCTION !$#description noncatalytic component of the active enzyme, which protects !1the cell against DNA damage by reducing alkyl !1hydroperoxides; it probably plays a role in substrate !1binding CLASSIFICATION #superfamily alkyl hydroperoxide reductase C22 protein; !1alkyl hydroperoxidase c22 protein homology KEYWORDS oxidoreductase FEATURE !$11-146 #domain alkyl hydroperoxidase c22 protein homology !8#label C22 SUMMARY #length 184 #molecular-weight 20846 #checksum 4701 SEQUENCE /// ENTRY RDHUP #type complete TITLE dihydropteridine reductase (EC 1.6.99.7) [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 15-Sep-2000 ACCESSIONS A93655; A94152; A26566 REFERENCE A93655 !$#authors Dahl, H.H.M.; Hutchison, W.; McAdam, W.; Wake, S.; Morgan, !1F.J.; Cotton, R.G.H. !$#journal Nucleic Acids Res. (1987) 15:1921-1932 !$#title Human dihydropteridine reductase: characterisation of a cDNA !1clone and its use in analysis of patients with !1dihydropteridine reductase deficiency. !$#cross-references MUID:87174727; PMID:3031582 !$#accession A93655 !'##molecule_type mRNA !'##residues 1-244 ##label DAH !'##cross-references GB:X04882; NID:g30818; PIDN:CAA28571.1; PID:g30819 REFERENCE A94152 !$#authors Lockyer, J.; Cook, R.G.; Milstien, S.; Kaufman, S.; Woo, !1S.L.C.; Ledley, F.D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:3329-3333 !$#title Structure and expression of human dihydropteridine !1reductase. !$#cross-references MUID:87204131; PMID:3033643 !$#accession A94152 !'##molecule_type mRNA !'##residues 1-50,'T',52-244 ##label LOC !'##cross-references GB:M16447; NID:g181552; PIDN:AAA52305.1; !1PID:g181553 REFERENCE A52588 !$#authors Varughese, K.I.; Su, Y.; Xuong, N.H.; Whiteley, J.M. !$#submission submitted to the Brookhaven Protein Data Bank, August 1993 !$#cross-references PDB:1HDR !$#contents annotation; X-ray crystallography, 2.5 angstroms, residues !19-244 REFERENCE A57129 !$#authors Su, Y.; Varughese, K.I.; Xuong, N.H.; Bray, T.L.; Roche, !1D.J.; Whiteley, J.M. !$#journal J. Biol. Chem. (1993) 268:26836-26841 !$#title The crystallographic structure of a human dihydropteridine !1reductase NADH binary complex expressed in Escherichia coli !1by a cDNA constructed from its rat homologue. !$#cross-references MUID:94086485; PMID:8262916 !$#contents annotation; X-ray crystallography, 2.5 angstroms GENETICS !$#gene GDB:QDPR !'##cross-references GDB:120331; OMIM:261630 !$#map_position 4p15.31-4p15.31 !$#note a defect in this gene may cause hyperphenylalaninemia, !1phenylketonuria and neurological disturbances and is !1generally lethal if untreated FUNCTION !$#description catalyzes the reduction of quinoid 7,8-dihydrobiopterin to !1tetrahydrobiopterin by NADH !$#note tetrahydrobiopterin (BH-4) is an essential cofactor for !1phenylalanine, tyrosine, and tryptophan hydroxylases CLASSIFICATION #superfamily dihydropteridine reductase KEYWORDS biopterin; NAD; oxidoreductase FEATURE !$2-244 #product dihydropteridine reductase #status predicted !8#label MAT\ !$12-41 #region beta-alpha-beta NAD nucleotide-binding fold\ !$90,150 #binding_site substrate (Trp, Tyr) #status predicted SUMMARY #length 244 #molecular-weight 25789 #checksum 2891 SEQUENCE /// ENTRY RDRTP #type complete TITLE dihydropteridine reductase (EC 1.6.99.7) - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 03-Dec-1999 ACCESSIONS A28473; A29415 REFERENCE A28473 !$#authors Shahbaz, M.; Hoch, J.A.; Trach, K.A.; Hural, J.A.; Webber, !1S.; Whiteley, J.M. !$#journal J. Biol. Chem. (1987) 262:16412-16416 !$#title Structural studies and isolation of cDNA clones providing !1the complete sequence of rat liver dihydropteridine !1reductase. !$#cross-references MUID:88059018; PMID:3680258 !$#accession A28473 !'##molecule_type mRNA !'##residues 1-241 ##label SHA !'##cross-references GB:J03481; NID:g203978; PIDN:AAA41099.1; !1PID:g203979 !'##note parts of the sequence were confirmed by protein sequencing REFERENCE A29415 !$#authors Webber, S.; Hural, J.; Whiteley, J.M. !$#journal Biochem. Biophys. Res. Commun. (1987) 143:582-586 !$#title Preliminary studies on the primary structure of rat liver !1dihydropteridine reductase. !$#cross-references MUID:87184542; PMID:3566737 !$#accession A29415 !'##molecule_type protein !'##residues 'IG',13-14;105-124,'Z',126-128;192-217,'G',219-220;236-241 !1##label WEB FUNCTION !$#description catalyzes the reduction, utilizing NADH, of quinoid 7, !18-dihydrobiopterin to tetrahydrobiopterin (BH-4), an !1essential cofactor for phenylalanine, tyrosine, and !1tryptophan hydroxylases CLASSIFICATION #superfamily dihydropteridine reductase KEYWORDS acetylated amino end; biopterin; NAD; oxidoreductase FEATURE !$2-241 #product dihydropteridine reductase #status predicted !8#label MAT\ !$9-38 #region beta-alpha-beta NAD nucleotide-binding fold\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status predicted\ !$87,147 #binding_site substrate (Trp, Tyr) #status predicted SUMMARY #length 241 #molecular-weight 25552 #checksum 1907 SEQUENCE /// ENTRY T24395 #type complete TITLE dihydropteridine reductase (EC 1.6.99.7) - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 02-Jun-2000 #sequence_revision 02-Jun-2000 #text_change 02-Jun-2000 ACCESSIONS T24395 REFERENCE Z19886 !$#authors Wilkinson, J. !$#submission submitted to the EMBL Data Library, October 1996 !$#accession T24395 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-236 ##label WIL !'##cross-references EMBL:Z81113; PIDN:CAB03278.1; GSPDB:GN00021; !1CESP:T03F6.1 !'##experimental_source clone T03F6 GENETICS !$#gene CESP:T03F6.1 !$#map_position 3 !$#introns 28/3; 63/2; 104/3; 194/2 FUNCTION !$#description catalyzes the reduction of quinoid 7,8-dihydrobiopterin to !1tetrahydrobiopterin by NADH !$#note tetrahydrobiopterin (BH-4) is an essential cofactor for !1phenylalanine, tyrosine, and tryptophan hydroxylases CLASSIFICATION #superfamily dihydropteridine reductase KEYWORDS biopterin; NAD; oxidoreductase FEATURE !$2-236 #product dihydropteridine reductase #status predicted !8#label MAT\ !$5-34 #region beta-alpha-beta NAD nucleotide-binding fold\ !$83,143 #binding_site substrate (Trp, Tyr) #status predicted SUMMARY #length 236 #molecular-weight 24713 #checksum 5680 SEQUENCE /// ENTRY RDRTU #type complete TITLE urate oxidase (EC 1.7.3.3) - rat ALTERNATE_NAMES uricase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1991 #sequence_revision 21-Feb-1997 #text_change 13-Aug-1999 ACCESSIONS I54070; A61606; A32267; A31261; A31774; S00496; A37533; !1S09670 REFERENCE I54070 !$#authors Wang, X.D.; Kawano, H.; Alvares, K.; Reddy, P.G.; Getto, H.; !1Rao, M.S.; Reddy, J.K. !$#journal Gene (1991) 97:223-229 !$#title Rat urate oxidase: cloning and structural analysis of the !1gene and 5'-flanking region. !$#cross-references MUID:91153651; PMID:1999285 !$#accession I54070 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-303 ##label RES !'##cross-references GB:M63593; NID:g207615; PIDN:AAA61699.1; !1PID:g207617 REFERENCE A61606 !$#authors Ito, M.; Nakamura, M.; Ogawa, H.; Kato, S.; Takagi, Y. !$#journal Genomics (1991) 11:905-913 !$#title Structural analysis of the gene encoding rat uricase. !$#cross-references MUID:92147134; PMID:1783398 !$#accession A61606 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-54,'D',56-110,'H',112-303 ##label IT1 REFERENCE A32267 !$#authors Alvares, K.; Nemali, M.R.; Reddy, P.G.; Wang, X.; Rao, M.S.; !1Reddy, J.K. !$#journal Biochem. Biophys. Res. Commun. (1989) 158:991-995 !$#title The nucleotide sequence of a full length cDNA clone encoding !1rat liver urate oxidase. !$#cross-references MUID:89149825; PMID:2920046 !$#accession A32267 !'##molecule_type mRNA !'##residues 1-110,'H',112-303 ##label ALV !'##cross-references GB:M24396; NID:g207606; PIDN:AAA42317.1; !1PID:g207607 !'##note the authors note the substantial differences in the published !1rat sequences REFERENCE A31261 !$#authors Reddy, P.G.; Nemali, M.R.; Reddy, M.K.; Reddy, M.N.; Yuan, !1P.M.; Yuen, S.; Laffler, T.G.; Shiroza, T.; Kuramitsu, H.K.; !1Usuda, N.; Chisholm, R.L.; Rao, M.S.; Reddy, J.K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:9081-9085 !$#title Isolation and sequence determination of a cDNA clone for rat !1peroxisomal urate oxidase: liver-specific expression in the !1rat. !$#cross-references MUID:89057880; PMID:3194410 !$#accession A31261 !'##molecule_type mRNA !'##residues 11-303 ##label RED REFERENCE A31774 !$#authors Motojima, K.; Kanaya, S.; Goto, S. !$#journal J. Biol. Chem. (1988) 263:16677-16681 !$#title Cloning and sequence analysis of cDNA for rat liver uricase. !$#cross-references MUID:89034153; PMID:3182808 !$#accession A31774 !'##molecule_type mRNA !'##residues 2-287,'TA',290 ##label MOT !'##cross-references GB:J03959; NID:g207618; PIDN:AAA42318.1; !1PID:g207619 REFERENCE S00496 !$#authors Ito, M.; Suzuki, M.; Takagi, Y. !$#journal Eur. J. Biochem. (1988) 173:459-463 !$#title Nucleotide sequence of cDNA and predicted amino acid !1sequence of rat liver uricase. !$#cross-references MUID:88196136; PMID:3267221 !$#accession S00496 !'##molecule_type mRNA !'##residues 'MMKWSLSELAM',22,'RTWS',27,'L',29-136,'ELTSVTWSR',146-211, !1'RCP',215-257,'AFQTFTTLTSTCP',271,'W',273,'S',275-287,'TA', !1290 ##label IT2 !'##cross-references EMBL:X07497; NID:g57458; PIDN:CAA30378.1; !1PID:g57459 !$#accession A37533 !'##molecule_type protein !'##residues 165-174;176-185;221-245;247-252 ##label IT3 !'##note the authors translated the codon CAA for residue 250 as Gly REFERENCE A35892 !$#authors Yeldandi, A.V.; Wang, X.; Alvares, K.; Kumar, S.; Rao, M.S.; !1Reddy, J.K. !$#journal Biochem. Biophys. Res. Commun. (1990) 171:641-646 !$#title Human urate oxidase gene: cloning and partial sequence !1analysis reveal a stop codon within the fifth exon. !$#cross-references MUID:90386634; PMID:2403354 !$#contents annotation !$#note compares the rat sequence with the human which has a stop !1codon in exon 5 REFERENCE S04332 !$#authors Motojima, K.; Goto, S. !$#journal Biochim. Biophys. Acta (1989) 1008:116-118 !$#title Cloning of rabbit uricase cDNA reveals a conserved !1carboxy-terminal tripeptide in three species. !$#cross-references MUID:89247439; PMID:2719958 !$#accession S09670 !'##molecule_type mRNA !'##residues 2-303 ##label MOW GENETICS !$#gene UOX !$#introns 10/3; 83/3; 122/3; 149/1; 210/2; 251/3; 279/3 FUNCTION !$#description copper-containing oxidase responsible for the hydrolysis of !1uric acid to allantoin !$#pathway purine metabolism !$#note present in most mammals, but absent in humans and certain !1primates CLASSIFICATION #superfamily urate oxidase KEYWORDS copper binding; liver; oxidoreductase; peroxisome FEATURE !$301-303 #region peroxisome/glyoxysome location signal !8(S-[RKH]-L) motif\ !$127,129 #binding_site copper (His) (type 2) #status predicted SUMMARY #length 303 #molecular-weight 34934 #checksum 5301 SEQUENCE /// ENTRY B36227 #type complete TITLE urate oxidase (EC 1.7.3.3) - mouse ALTERNATE_NAMES uricase ORGANISM #formal_name Mus musculus #common_name house mouse DATE 04-Oct-1991 #sequence_revision 27-Jun-1994 #text_change 13-Aug-1999 ACCESSIONS B36227 REFERENCE A36227 !$#authors Wu, X.; Lee, C.C.; Muzny, D.M.; Caskey, C.T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:9412-9416 !$#title Urate oxidase: primary structure and evolutionary !1implications. !$#cross-references MUID:90083277; PMID:2594778 !$#accession B36227 !'##molecule_type mRNA !'##residues 1-303 ##label WUA !'##cross-references GB:M27695; NID:g202294; PIDN:AAA40538.1; !1PID:g202295 CLASSIFICATION #superfamily urate oxidase KEYWORDS copper binding; liver; oxidoreductase; peroxisome FEATURE !$301-303 #region peroxisome/glyoxysome location signal !8(S-[RKH]-L) motif\ !$127,129 #binding_site copper (His) (type 2) #status predicted SUMMARY #length 303 #molecular-weight 35039 #checksum 5115 SEQUENCE /// ENTRY C36227 #type complete TITLE urate oxidase (EC 1.7.3.3) - pig ALTERNATE_NAMES uricase ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 04-Oct-1991 #sequence_revision 27-Jun-1994 #text_change 13-Aug-1999 ACCESSIONS C36227; A47600; B47600 REFERENCE A36227 !$#authors Wu, X.; Lee, C.C.; Muzny, D.M.; Caskey, C.T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:9412-9416 !$#title Urate oxidase: primary structure and evolutionary !1implications. !$#cross-references MUID:90083277; PMID:2594778 !$#accession C36227 !'##molecule_type mRNA !'##residues 1-304 ##label WUA !'##cross-references GB:M27697; NID:g164723; PIDN:AAA31141.1; !1PID:g164724 REFERENCE A47600 !$#authors Lee, C.C.; Wu, X.; Gibbs, R.A.; Cook, R.G.; Muzny, D.M.; !1Caskey, C.T. !$#journal Science (1988) 239:1288-1291 !$#title Generation of cDNA probes directed by amino acid sequence: !1cloning of urate oxidase. !$#cross-references MUID:88145684; PMID:3344434 !$#accession A47600 !'##molecule_type mRNA !'##residues 1-108 ##label LEE1 !'##cross-references GB:M19733; NID:g164721; PIDN:AAA31140.1; !1PID:g164722 !'##note nucleotide sequence is not complete !$#accession B47600 !'##molecule_type protein !'##residues 7-38 ##label LEE2 CLASSIFICATION #superfamily urate oxidase KEYWORDS copper binding; liver; oxidoreductase; peroxisome FEATURE !$302-304 #region peroxisome/glyoxysome location signal !8(S-[RKH]-L) motif\ !$127,129 #binding_site copper (His) (type 2) #status predicted SUMMARY #length 304 #molecular-weight 35008 #checksum 9323 SEQUENCE /// ENTRY A36227 #type complete TITLE urate oxidase (EC 1.7.3.3) - baboon ALTERNATE_NAMES uricase ORGANISM #formal_name Papio sp. #common_name baboon DATE 04-Oct-1991 #sequence_revision 27-Jun-1994 #text_change 13-Aug-1999 ACCESSIONS A36227 REFERENCE A36227 !$#authors Wu, X.; Lee, C.C.; Muzny, D.M.; Caskey, C.T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:9412-9416 !$#title Urate oxidase: primary structure and evolutionary !1implications. !$#cross-references MUID:90083277; PMID:2594778 !$#accession A36227 !'##molecule_type mRNA !'##residues 1-304 ##label WUA !'##cross-references GB:M27694 CLASSIFICATION #superfamily urate oxidase KEYWORDS copper binding; liver; oxidoreductase; peroxisome FEATURE !$302-304 #region peroxisome/glyoxysome location signal !8(S-[RKH]-L) motif\ !$127,129 #binding_site copper (His) (type 2) #status predicted SUMMARY #length 304 #molecular-weight 34978 #checksum 7747 SEQUENCE /// ENTRY S04332 #type complete TITLE urate oxidase (EC 1.7.3.3) - rabbit ALTERNATE_NAMES uricase ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 28-Feb-1990 #sequence_revision 27-Jun-1994 #text_change 13-Aug-1999 ACCESSIONS S04332; I46540; I46541 REFERENCE S04332 !$#authors Motojima, K.; Goto, S. !$#journal Biochim. Biophys. Acta (1989) 1008:116-118 !$#title Cloning of rabbit uricase cDNA reveals a conserved !1carboxy-terminal tripeptide in three species. !$#cross-references MUID:89247439; PMID:2719958 !$#accession S04332 !'##molecule_type mRNA !'##residues 1-300 ##label MOT !'##cross-references EMBL:X14522; NID:g1769; PIDN:CAA32664.1; PID:g1770 REFERENCE I46540 !$#authors Motojima, K.; Goto, S. !$#journal FEBS Lett. (1990) 277:26-28 !$#title Two rabbit uricase mRNAs and their tissue-specific !1expression. !$#cross-references MUID:91099512; PMID:2269363 !$#accession I46540 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-35 ##label MO2 !'##cross-references EMBL:X57776; NID:g1765; PIDN:CAA40922.1; PID:g1766 !$#accession I46541 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-35 ##label MO3 !'##cross-references EMBL:X57777; NID:g1767; PIDN:CAA40923.1; PID:g1768 CLASSIFICATION #superfamily urate oxidase KEYWORDS copper binding; liver; oxidoreductase; peroxisome FEATURE !$298-300 #region peroxisome/glyoxysome location signal !8(S-[RKH]-L) motif\ !$123,125 #binding_site copper (His) (type 2) #status predicted SUMMARY #length 300 #molecular-weight 34500 #checksum 5785 SEQUENCE /// ENTRY S29133 #type complete TITLE urate oxidase (EC 1.7.3.3) - fruit fly (Drosophila virilis) ALTERNATE_NAMES uricase ORGANISM #formal_name Drosophila virilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S29133 REFERENCE S29133 !$#authors Wallrath, L.L.; Burnett, J.B.; Friedman, T.B. !$#submission submitted to the EMBL Data Library, January 1991 !$#accession S29133 !'##molecule_type DNA !'##residues 1-342 ##label WAL !'##cross-references EMBL:X57114; NID:g9211; PIDN:CAA40397.1; PID:g9212 GENETICS !$#gene FlyBase:Dvir/Uro !'##cross-references FlyBase:FBgn0013101 !$#introns 182/1 CLASSIFICATION #superfamily urate oxidase KEYWORDS copper binding; oxidoreductase; peroxisome FEATURE !$340-342 #region peroxisome/glyoxysome location signal !8(S-[RKH]-L) motif\ !$160,162 #binding_site copper (His) (type 2) #status predicted SUMMARY #length 342 #molecular-weight 38724 #checksum 2138 SEQUENCE /// ENTRY S29760 #type complete TITLE urate oxidase (EC 1.7.3.3) - fruit fly (Drosophila pseudoobscura) ALTERNATE_NAMES uricase ORGANISM #formal_name Drosophila pseudoobscura DATE 22-Nov-1993 #sequence_revision 27-Jun-1994 #text_change 13-Aug-1999 ACCESSIONS S29760 REFERENCE S29760 !$#authors Friedman, T.B.; Burnett, J.B.; Lootens, S.; Steinman, R.; !1Wallrath, L.L. !$#journal J. Mol. Evol. (1992) 34:62-77 !$#title The urate oxidase gene of Drosophila pseudoobscura and !1Drosophila melanogaster: evolutionary changes of sequence !1and regulation. !$#cross-references MUID:92211723; PMID:1556745 !$#accession S29760 !'##molecule_type DNA !'##residues 1-346 ##label FRI !'##cross-references EMBL:X57113 GENETICS !$#gene UO !'##cross-references FlyBase:FBgn0012716 !$#introns 186/1 CLASSIFICATION #superfamily urate oxidase KEYWORDS copper binding; oxidoreductase; peroxisome FEATURE !$344-346 #region peroxisome/glyoxysome location signal !8(S-[RKH]-L) motif\ !$164,166 #binding_site copper (His) (type 2) #status predicted SUMMARY #length 346 #molecular-weight 39310 #checksum 5125 SEQUENCE /// ENTRY A35920 #type complete TITLE urate oxidase (EC 1.7.3.3) - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES uricase ORGANISM #formal_name Drosophila melanogaster DATE 09-Nov-1990 #sequence_revision 27-Jun-1994 #text_change 13-Aug-1999 ACCESSIONS A35920; S08676 REFERENCE A35920 !$#authors Wallrath, L.L.; Burnett, J.B.; Friedman, T.B. !$#journal Mol. Cell. Biol. (1990) 10:5114-5127 !$#title Molecular characterization of the Drosophila melanogaster !1urate oxidase gene, an ecdysone-repressible gene expressed !1only in the malpighian tubules. !$#cross-references MUID:90377201; PMID:2118989 !$#accession A35920 !'##molecule_type DNA !'##residues 1-352 ##label WAL !'##cross-references EMBL:X51940; NID:g8798; PIDN:CAA36203.1; PID:g8799 GENETICS !$#gene UO !'##cross-references FlyBase:FBgn0003961 !$#introns 192/1 CLASSIFICATION #superfamily urate oxidase KEYWORDS copper binding; oxidoreductase; peroxisome FEATURE !$350-352 #region peroxisome/glyoxysome location signal !8(S-[RKH]-L) motif\ !$170,172 #binding_site copper (His) (type 2) #status predicted SUMMARY #length 352 #molecular-weight 40034 #checksum 5711 SEQUENCE /// ENTRY A38097 #type complete TITLE urate oxidase (EC 1.7.3.3) - Aspergillus flavus ALTERNATE_NAMES uricase ORGANISM #formal_name Aspergillus flavus DATE 07-Apr-1994 #sequence_revision 27-Jun-1994 #text_change 13-Aug-1999 ACCESSIONS A38097; S22867; S22868 REFERENCE A38097 !$#authors Legoux, R.; Delpech, B.; Dumont, X.; Guillemot, J.C.; !1Ramond, P.; Shire, D.; Caput, D.; Ferrara, P.; Loison, G. !$#journal J. Biol. Chem. (1992) 267:8565-8570 !$#title Cloning and expression in Escherichia coli of the gene !1encoding Aspergillus flavus urate oxidase. !$#cross-references MUID:92235086; PMID:1339455 !$#accession A38097 !'##molecule_type DNA; mRNA !'##residues 1-302 ##label LEG !'##cross-references GB:X61765; NID:g2299; PIDN:CAA43895.1; PID:g2300; !1GB:X61766; NID:g2301; PID:g2302 COMMENT This is a copper-containing oxidase involved in the purine !1breakdown pathway. It is responsible for the oxidation of !1uric acid to allantoin. GENETICS !$#gene uaZ !$#introns 46/2; 262/1 CLASSIFICATION #superfamily urate oxidase KEYWORDS copper binding; oxidoreductase; peroxisome FEATURE !$300-302 #region peroxisome/glyoxysome location signal !8(S-[RKH]-L) motif\ !$117,119 #binding_site copper (His) (type 2) #status predicted SUMMARY #length 302 #molecular-weight 34241 #checksum 6039 SEQUENCE /// ENTRY A25776 #type complete TITLE urate oxidase (EC 1.7.3.3) - soybean ALTERNATE_NAMES nodulin-35 protein; uricase II ORGANISM #formal_name Glycine max #common_name soybean DATE 29-Aug-1987 #sequence_revision 27-Jun-1994 #text_change 13-Aug-1999 ACCESSIONS A25776 REFERENCE A25776 !$#authors Nguyen, T.; Zelechowska, M.; Foster, V.; Bergmann, H.; !1Verma, D.P.S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:5040-5044 !$#title Primary structure of the soybean nodulin-35 gene encoding !1uricase II localized in the peroxisome of uninfected cells !1of nodules. !$#accession A25776 !'##molecule_type DNA !'##residues 1-309 ##label NGU GENETICS !$#introns 70/3; 101/3; 127/1; 163/3; 194/2; 252/2; 282/3 CLASSIFICATION #superfamily urate oxidase KEYWORDS copper binding; oxidoreductase; peroxisome FEATURE !$307-309 #region peroxisome/glyoxysome location signal !8(S-[RKH]-L) motif\ !$124,126 #binding_site copper (His) (type 2) #status predicted SUMMARY #length 309 #molecular-weight 35171 #checksum 9323 SEQUENCE /// ENTRY A36954 #type complete TITLE hydroxylamine oxidase (EC 1.7.3.4) precursor [validated] - Nitrosomonas europaea ALTERNATE_NAMES hydroxylamine oxidoreductase ORGANISM #formal_name Nitrosomonas europaea DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 23-Mar-2001 ACCESSIONS A36954; A55000 REFERENCE A36954 !$#authors Sayavedra-Soto, L.A.; Hommes, N.G.; Arp, D.J. !$#journal J. Bacteriol. (1994) 176:504-510 !$#title Characterization of the gene encoding hydroxylamine !1oxidoreductase in Nitrosomonas europaea. !$#cross-references MUID:94117386; PMID:8288544 !$#accession A36954 !'##molecule_type DNA !'##residues 1-570 ##label SAY !'##cross-references GB:U04053; NID:g433392; PIDN:AAC43216.1; !1PID:g433393 !'##experimental_source strain ATCC 19178 REFERENCE A55000 !$#authors Arciero, D.M.; Hooper, A.B. !$#journal J. Biol. Chem. (1993) 268:14645-14654 !$#title Hydroxylamine oxidoreductase from Nitrosomonas europaea is a !1multimer of an octa-heme subunit. !$#cross-references MUID:93315429; PMID:8325841 !$#accession A55000 !'##molecule_type protein !'##residues !125-48;93-115;165-179;252-272;273-291;325-350;377-391; !1481-490,'X',492-499 ##label ARC !'##cross-references PIDN:AAB27473.1; PID:g398454; PIDN:AAB27476.1; !1PID:g398457; PIDN:AAB27477.1; PID:g398458; PIDN:AAB27479.1; !1PID:g398460; PIDN:AAB27474.1; PID:g398455; PIDN:AAB27475.1; !1PID:g398456; PIDN:AAB27478.1; PID:g398459; PIDN:AAB27480.1; !1PID:g398461 !'##note sequence extracted from NCBI backbone (NCBIP:134967, !1NCBIP:134970, NCBIP:134971, NCBIP:134973, NCBIP:134968, !1NCBIP:134969, NCBIP:134972, NCBIP:134974) !'##note sequence modified after extraction from NCBI backbone REFERENCE A73171 !$#authors Tanaka, N.; Igarashi, N.; Moriyama, H. !$#submission submitted to the Brookhaven Protein Data Bank, March 1997 !$#cross-references PDB:1FGJ !$#contents annotation; X-ray crystallography, 2.8 angstroms, residues !125-523 REFERENCE A59035 !$#authors Igarashi, N.; Moriyama, H.; Fujiwara, T.; Fukumori, Y.; !1Tanaka, N. !$#journal Nat. Struct. Biol. (1997) 4:276-284 !$#title The 2.8 A structure of hydroxylamine oxidoreductase from a !1nitrifying chemoautotrophic bacterium, Nitrosomonas !1europaea. !$#cross-references MUID:97249290; PMID:9095195 !$#contents annotation; X-ray crystallography, 2.8 angstroms COMMENT For cytochrome c554, see PIR:A59036. COMMENT The heme moiety has an unusual third covalent linkage as !1does the heme P460 of cytochrome P460 (see PIR:S48749). GENETICS !$#gene hao COMPLEX homotrimer FUNCTION !$#description catalyzes the oxidation of hydroxyl amine and water by 2 !1molecules of cytochrome c554 to nitrous acid and four !1protons !$#pathway ammonia oxidation !$#note the reaction involves two two-electron reductions of the !1tetraheme cytochrome c554; the Enzyme Commission defined !1activity applies to the combination of this reaction with !1the subsequent reoxidation of cytochrome c554 and the !1eventual reduction of oxygen CLASSIFICATION #superfamily Nitrosomonas europaea hydroxylamine oxidase KEYWORDS ammonia oxidation; chromoprotein; electron transfer; heme; !1homotrimer; iron; metalloprotein; oxidoreductase FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-570 #product hydroxylamine oxidase #status experimental !8#label MAT\ !$103,106 #binding_site heme (Cys) (covalent) #status !8experimental\ !$107,184 #binding_site heme iron (His) (axial ligands) #status !8experimental\ !$123,200 #binding_site heme iron (His) (axial ligands) #status !8experimental\ !$169,172 #binding_site heme (Cys) (covalent) #status !8experimental\ !$173,270 #binding_site heme iron (His) (axial ligands) #status !8experimental\ !$196,199 #binding_site heme (Cys) (covalent) #status !8experimental\ !$228,287 #binding_site heme iron (His) (axial ligands) #status !8experimental\ !$253,256 #cross-link heme P460 (Cys-Cys) (interchain to !8Tyr-491 in trimeric partner 1) #status experimental\ !$257 #binding_site heme P460 iron (His) (axial ligand) !8#status experimental\ !$263,266 #binding_site heme (Cys) (covalent) #status !8experimental\ !$267,347 #binding_site heme iron (His) (axial ligands) #status !8experimental\ !$283,286 #binding_site heme (Cys) (covalent) #status !8experimental\ !$303,388 #binding_site heme iron (His) (axial ligands) #status !8experimental\ !$334,337 #binding_site heme (Cys) (covalent) #status !8experimental\ !$338,483 #binding_site heme iron (His) (axial ligands) #status !8experimental\ !$384,387 #binding_site heme (Cys) (covalent) #status !8experimental\ !$491 #cross-link heme P460 (Tyr) (interchain to Cys-253 !8and Cys-256 in trimeric partner 2) #status !8experimental SUMMARY #length 570 #molecular-weight 64274 #checksum 4648 SEQUENCE /// ENTRY S39590 #type complete TITLE formate-dependent nitrite reductase (EC 1.7.-.-) cytochrome c552 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 13-Jan-1995 #sequence_revision 26-Jul-1996 #text_change 01-Mar-2002 ACCESSIONS S39590; E65215; S34283 REFERENCE S39590 !$#authors Darwin, A.; Hussain, H.; Griffiths, L.; Grove, J.; Sambongi, !1Y.; Busby, S.; Cole, J. !$#journal Mol. Microbiol. (1993) 9:1255-1265 !$#title Regulation and sequence of the structural gene for !1cytochrome c(552) from Escherichia coli: not a hexahaem but !1a 50kDa tetrahaem nitrite reductase. !$#cross-references MUID:95020657; PMID:7934939 !$#accession S39590 !'##molecule_type DNA !'##residues 1-478 ##label DAR !'##cross-references EMBL:X72298; NID:g404302; PIDN:CAA51048.1; !1PID:g853826 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65215 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-478 ##label BLAT !'##cross-references GB:AE000480; GB:U00096; NID:g2367344; !1PIDN:AAC77040.1; PID:g1790506; UWGP:b4070 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene nrfA !$#note this is one of the seven gene operon (nrf) essential for !1formate-dependent nitrite reduction to ammonia FUNCTION !$#description this nitrite reductase is a c-type cytochrome (c552) that is !1the final component of an energy-conserving chain, !1transforming electrons from formate to nitrite CLASSIFICATION #superfamily formate-dependent nitrite reductase cytochrome !1c552 KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; oxidoreductase; periplasmic space FEATURE !$160,163 #binding_site heme (Cys) (covalent) #status !8predicted\ !$164 #binding_site heme iron (His) (axial ligand) #status !8predicted\ !$209,212 #binding_site heme (Cys) (covalent) #status !8predicted\ !$213 #binding_site heme iron (His) (axial ligand) #status !8predicted\ !$282,285 #binding_site heme (Cys) (covalent) #status !8predicted\ !$286 #binding_site heme iron (His) (axial ligand) #status !8predicted\ !$314,317 #binding_site heme (Cys) (covalent) #status !8predicted\ !$318 #binding_site heme iron (His) (axial ligand) #status !8predicted SUMMARY #length 478 #molecular-weight 53703 #checksum 1596 SEQUENCE /// ENTRY C64181 #type complete TITLE formate-dependent nitrite reductase (EC 1.7.-.-) cytochrome c552 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 18-Aug-1995 #sequence_revision 26-Jul-1996 #text_change 03-Mar-2000 ACCESSIONS C64181 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession C64181 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-538 ##label TIGR !'##cross-references GB:U32787; GB:L42023; NID:g1574619; !1PIDN:AAC22727.1; PID:g1574623; TIGR:HI1069 !'##note named as homolog to a protein from Escherichia coli FUNCTION !$#description this nitrite reductase is a c-type cytochrome (c552) that is !1the final component of an energy-conserving chain, !1transforming electrons from formate to nitrite CLASSIFICATION #superfamily formate-dependent nitrite reductase cytochrome !1c552 KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; oxidoreductase; periplasmic space FEATURE !$199,202 #binding_site heme (Cys) (covalent) #status !8predicted\ !$203 #binding_site heme iron (His) (axial ligand) #status !8predicted\ !$264,267 #binding_site heme (Cys) (covalent) #status !8predicted\ !$268 #binding_site heme iron (His) (axial ligand) #status !8predicted\ !$337,340 #binding_site heme (Cys) (covalent) #status !8predicted\ !$341 #binding_site heme iron (His) (axial ligand) #status !8predicted\ !$369,372 #binding_site heme (Cys) (covalent) #status !8predicted\ !$373 #binding_site heme iron (His) (axial ligand) #status !8predicted SUMMARY #length 538 #molecular-weight 60399 #checksum 5077 SEQUENCE /// ENTRY JC4395 #type complete TITLE ferredoxin-nitrite reductase (EC 1.7.7.1) precursor - rice ORGANISM #formal_name Oryza sativa #common_name rice DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 03-Jun-2002 ACCESSIONS JC4395; PS0153 REFERENCE JC4395 !$#authors Terada, Y.; Aoki, H.; Tanaka, T.; Morikawa, H.; Ida, S. !$#journal Biosci. Biotechnol. Biochem. (1995) 59:2183-2185 !$#title Cloning and nucleotide sequence of a leaf ferredoxin-nitrite !1reductase cDNA of rice. !$#cross-references MUID:96100954; PMID:8541663 !$#accession JC4395 !'##molecule_type mRNA !'##residues 1-596 ##label TER !'##cross-references DDBJ:D50556; NID:g809513; PIDN:BAA09122.1; !1PID:g809514 !'##experimental_source leaf REFERENCE PS0153 !$#authors Matsui, J.; Takeba, G.; Ida, S. !$#journal Agric. Biol. Chem. (1990) 54:3069-3071 !$#title Molecular cloning and partial amino acid sequence of rice !1ferredoxin-nitrite reductase. !$#cross-references MUID:91248477; PMID:1368656 !$#accession PS0153 !'##molecule_type mRNA !'##residues 501-530,'A',532-560,'DV',563-596 ##label MAS CLASSIFICATION #superfamily ferredoxin-nitrite reductase KEYWORDS 4Fe-4S; chloroplast; iron-sulfur protein; metalloprotein; !1oxidoreductase FEATURE !$1-30 #domain transit peptide (chloroplast) #status !8predicted #label TRP\ !$31-596 #product ferredoxin-nitrite reductase #status !8predicted #label MAT\ !$128-138 #region ferredoxin binding #status predicted\ !$474,480,515,519 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 596 #molecular-weight 66142 #checksum 5038 SEQUENCE /// ENTRY S51945 #type complete TITLE ferredoxin-nitrite reductase (EC 1.7.7.1) precursor - kidney bean ORGANISM #formal_name Phaseolus vulgaris #common_name kidney bean DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 03-Jun-2002 ACCESSIONS S51945 REFERENCE S51945 !$#authors Sander, L.; Jensen, P.E.; Back, L.F.; Stummann, B.M.; !1Henningsen, K.W. !$#journal Plant Mol. Biol. (1995) 27:165-177 !$#title Structure and expression of a nitrite reductase gene from !1bean (Phaseolus vulgaris) and promoter analysis in !1transgenic tobacco. !$#cross-references MUID:95169998; PMID:7865786 !$#accession S51945 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-582 ##label SAN !'##cross-references EMBL:U10419; NID:g500752; PIDN:AAA74456.1; !1PID:g500753 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1994 !'##note only a part of the translation is shown GENETICS !$#gene NiR !$#genome nuclear !$#introns 122/1; 240/2; 337/3 CLASSIFICATION #superfamily ferredoxin-nitrite reductase KEYWORDS 4Fe-4S; chloroplast; iron-sulfur protein; metalloprotein; !1oxidoreductase FEATURE !$1-18 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$19-582 #product ferredoxin-nitrite reductase #status !8predicted #label MAT\ !$460,466,501,505 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 582 #molecular-weight 64994 #checksum 5084 SEQUENCE /// ENTRY S20495 #type complete TITLE ferredoxin-nitrite reductase (EC 1.7.7.1) precursor - European white birch ORGANISM #formal_name Betula pendula #common_name European white birch DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 03-Jun-2002 ACCESSIONS S20495 REFERENCE S20495 !$#authors Friemann, A.; Brinkmann, K.; Hachtel, W. !$#journal Mol. Gen. Genet. (1992) 231:411-416 !$#title Sequence of a cDNA encoding nitrite reductase from the tree !1Betula pendula and identification of conserved protein !1regions. !$#cross-references MUID:92167960; PMID:1347145 !$#accession S20495 !'##molecule_type mRNA !'##residues 1-583 ##label FRI !'##cross-references EMBL:X60093; NID:g17926; PIDN:CAA42690.1; !1PID:g17927 CLASSIFICATION #superfamily ferredoxin-nitrite reductase KEYWORDS 4Fe-4S; chloroplast; iron-sulfur protein; metalloprotein; !1oxidoreductase FEATURE !$1-22 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$23-583 #product nitrite reductase #status predicted #label !8MAT\ !$461,467,502,506 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 583 #molecular-weight 65229 #checksum 6269 SEQUENCE /// ENTRY S16603 #type complete TITLE ferredoxin-nitrite reductase (EC 1.7.7.1) precursor - spinach ORGANISM #formal_name Spinacia oleracea #common_name spinach DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 03-Jun-2002 ACCESSIONS S16603; S00896 REFERENCE S16603 !$#authors Back, E.; Dunne, W.; Schneiderbauer, A.; de Framond, A.; !1Rastogi, R.; Rothstein, S.J. !$#journal Plant Mol. Biol. (1991) 17:9-18 !$#title Isolation of the spinach nitrite reductase gene promoter !1which confers nitrate inducibility on GUS gene expression in !1transgenic tobacco. !$#cross-references MUID:91329742; PMID:1868226 !$#accession S16603 !'##molecule_type DNA !'##residues 1-594 ##label BAC !'##cross-references EMBL:X17031; NID:g21255; PIDN:CAA34893.1; !1PID:g21256 REFERENCE S00896 !$#authors Back, E.; Burkhart, W.; Moyer, M.; Privalle, L.; Rothstein, !1S. !$#journal Mol. Gen. Genet. (1988) 212:20-26 !$#title Isolation of cDNA clones coding for spinach nitrite !1reductase: complete sequence and nitrate induction. !$#cross-references MUID:88232431; PMID:3163766 !$#accession S00896 !'##molecule_type mRNA !'##residues 1-594 ##label BA2 !'##cross-references EMBL:X07568; NID:g21257; PIDN:CAA30453.1; !1PID:g21258 GENETICS !$#gene NiR !$#introns 135/1; 253/2; 349/3 CLASSIFICATION #superfamily ferredoxin-nitrite reductase KEYWORDS 4Fe-4S; chloroplast; iron-sulfur protein; metalloprotein; !1oxidoreductase FEATURE !$1-32 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$33-594 #product ferredoxin-nitrite reductase #status !8predicted #label MAT\ !$473,479,514,518 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 594 #molecular-weight 66394 #checksum 27 SEQUENCE /// ENTRY S75713 #type complete TITLE ferredoxin-nitrate reductase (EC 1.7.7.2) - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein slr0898 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 03-Jun-2002 ACCESSIONS S75713 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75713 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-502 ##label KAN !'##cross-references EMBL:D64003; GB:AB001339; NID:g1001200; !1PIDN:BAA10448.1; PID:g1001208 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene nirA !$#start_codon GTG CLASSIFICATION #superfamily ferredoxin-nitrite reductase KEYWORDS 4Fe-4S; iron-sulfur protein; metalloprotein; oxidoreductase FEATURE !$388,394,429,433 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 502 #molecular-weight 55927 #checksum 2163 SEQUENCE /// ENTRY PQ0646 #type complete TITLE ferredoxin-nitrite reductase (EC 1.7.7.1) - Synechococcus sp. (strain PCC 7942) ORGANISM #formal_name Synechococcus sp. #variety PCC 7942 DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 03-Jun-2002 ACCESSIONS S33530; PQ0646; S32143 REFERENCE S33530 !$#authors Luque, I.; Flores, E.; Herrero, A. !$#journal Plant Mol. Biol. (1993) 21:1201-1205 !$#title Nitrite reductase gene from Synechococcus sp. PCC 7942: !1homology between cyanobacterial and higher-plant nitrite !1reductases. !$#cross-references MUID:93257637; PMID:8490140 !$#accession S33530 !'##molecule_type DNA !'##residues 1-512 ##label LUQ !'##cross-references EMBL:X67680; NID:g288053; PIDN:CAA47912.1; !1PID:g288054 REFERENCE PQ0646 !$#authors Omata, T. !$#journal Plant Cell Physiol. (1991) 32:151-157 !$#title Cloning and characterization of the nrtA gene that encodes a !145-kDa protein involved in nitrate transport in the !1cyanobacterium Synechococcus PCC 7942. !$#accession PQ0646 !'##molecule_type DNA !'##residues 468-512 ##label OMA !'##cross-references DDBJ:D00677 GENETICS !$#gene nir CLASSIFICATION #superfamily ferredoxin-nitrite reductase KEYWORDS 4Fe-4S; iron-sulfur protein; metalloprotein; oxidoreductase FEATURE !$396,402,437,441 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 512 #molecular-weight 56541 #checksum 4054 SEQUENCE /// ENTRY S56640 #type complete TITLE ferredoxin-nitrite reductase (EC 1.7.7.1) [similarity] - Phormidium laminosum ORGANISM #formal_name Phormidium laminosum #note oscillatoriacean cyanobacterium DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 03-Jun-2002 ACCESSIONS S56640 REFERENCE S56640 !$#authors Merchan, F.; Prieto, R.; Kindle, K.L.; Llama, M.J.; Serra, !1J.L.; Fernandez, E. !$#journal Plant Mol. Biol. (1995) 27:1037-1042 !$#title Isolation, sequence and expression in Escherichia coli of !1the nitrite reductase gene from the filamentous, !1thermophilic cyanobacterium Phormidium laminosum. !$#cross-references MUID:95284340; PMID:7766873 !$#accession S56640 !'##molecule_type DNA !'##residues 1-510 ##label MER !'##cross-references EMBL:Z19598; NID:g1154890; PID:g887565; !1PIDN:CAA79655.1 CLASSIFICATION #superfamily ferredoxin-nitrite reductase KEYWORDS 4Fe-4S; iron-sulfur protein; metalloprotein; oxidoreductase FEATURE !$396,402,437,441 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 510 #molecular-weight 56709 #checksum 3906 SEQUENCE /// ENTRY B57987 #type complete TITLE formate-dependent nitrite reductase precursor NrfB [imported] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 26-Jul-1996 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS F65215; B57987 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65215 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-190 ##label BLAT !'##cross-references GB:AE000480; GB:U00096; NID:g2367344; !1PIDN:AAC77041.1; PID:g1790507; UWGP:b4071 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A57987 !$#authors Hussain, H.; Grove, J.; Griffiths, L.; Busby, S.; Cole, J. !$#journal Mol. Microbiol. (1994) 12:153-163 !$#title A seven-gene operon essential for formate-dependent nitrite !1reduction to ammonia by enteric bacteria. !$#cross-references MUID:94335626; PMID:8057835 !$#accession B57987 !'##status preliminary !'##molecule_type DNA !'##residues 3-190 ##label HUS !'##cross-references EMBL:X72298; NID:g404302; PIDN:CAA51042.1; !1PID:g404303 GENETICS !$#gene nrfB !$#note this is one of the seven gene operon (nrf) essential for !1formate-dependent nitrite reduction to ammonia FUNCTION !$#description a cytochrome c type protein; essential for the !1formate-dependent nitrite reductase activity CLASSIFICATION #superfamily nrfB protein KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; periplasmic space FEATURE !$1-33 #domain signal sequence #status predicted #label SIG\ !$34-190 #product nrfB protein #status predicted #label MAT\ !$51,54 #binding_site heme (Cys) (covalent) #status !8predicted\ !$55 #binding_site heme iron (His) (axial ligand) #status !8predicted\ !$80,83 #binding_site heme (Cys) (covalent) #status !8predicted\ !$84 #binding_site heme iron (His) (axial ligand) #status !8predicted\ !$115,118 #binding_site heme (Cys) (covalent) #status !8predicted\ !$119 #binding_site heme iron (His) (axial ligand) #status !8predicted\ !$140,143 #binding_site heme (Cys) (covalent) #status !8predicted\ !$144 #binding_site heme iron (His) (axial ligand) #status !8predicted\ !$165,168 #binding_site heme (Cys) (covalent) #status !8predicted\ !$169 #binding_site heme iron (His) (axial ligand) #status !8predicted SUMMARY #length 190 #molecular-weight 20960 #checksum 2122 SEQUENCE /// ENTRY B64181 #type complete TITLE nrfB protein - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 18-Aug-1995 #sequence_revision 26-Jul-1996 #text_change 03-Mar-2000 ACCESSIONS B64181 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession B64181 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-226 ##label TIGR !'##cross-references GB:U32787; GB:L42023; NID:g1574619; !1PIDN:AAC22726.1; PID:g1574622; TIGR:HI1068 !'##note named as homolog to a protein from Escherichia coli GENETICS !$#gene nrfB !$#start_codon GTG FUNCTION !$#description a cytochrome c type protein; essential for the !1formate-dependent nitrite reductase activity CLASSIFICATION #superfamily nrfB protein KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; periplasmic space FEATURE !$65,68 #binding_site heme (Cys) (covalent) #status !8predicted\ !$69 #binding_site heme iron (His) (axial ligand) #status !8predicted\ !$110,113 #binding_site heme (Cys) (covalent) #status !8predicted\ !$114 #binding_site heme iron (His) (axial ligand) #status !8predicted\ !$152,155 #binding_site heme (Cys) (covalent) #status !8predicted\ !$156 #binding_site heme iron (His) (axial ligand) #status !8predicted\ !$177,180 #binding_site heme (Cys) (covalent) #status !8predicted\ !$181 #binding_site heme iron (His) (axial ligand) #status !8predicted\ !$202,205 #binding_site heme (Cys) (covalent) #status !8predicted\ !$206 #binding_site heme iron (His) (axial ligand) #status !8predicted SUMMARY #length 226 #molecular-weight 25663 #checksum 6253 SEQUENCE /// ENTRY C57987 #type complete TITLE formate-dependent nitrite reductase NrfC [imported] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 26-Jul-1996 #sequence_revision 26-Jul-1996 #text_change 01-Mar-2002 ACCESSIONS C57987; G65215 REFERENCE A57987 !$#authors Hussain, H.; Grove, J.; Griffiths, L.; Busby, S.; Cole, J. !$#journal Mol. Microbiol. (1994) 12:153-163 !$#title A seven-gene operon essential for formate-dependent nitrite !1reduction to ammonia by enteric bacteria. !$#cross-references MUID:94335626; PMID:8057835 !$#accession C57987 !'##status preliminary !'##molecule_type DNA !'##residues 1-223 ##label HUS !'##cross-references EMBL:X72298; NID:g404302; PIDN:CAA51043.1; !1PID:g404304 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65215 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-223 ##label BLAT !'##cross-references GB:AE000480; GB:U00096; NID:g2367344; !1PIDN:AAC77042.1; PID:g2367345; UWGP:b4072 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene nrfC !$#note this is one of the seven gene operon (nrf) essential for !1formate-dependent nitrite reduction to ammonia FUNCTION !$#description probably involved in the transfer of electrons from the !1quinone pool to the type-c cytochromes; essential for the !1formate-dependent nitrite reductase activity CLASSIFICATION #superfamily nrfC protein; ferredoxin 2[4Fe-4S] homology KEYWORDS 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$39-112 #domain ferredoxin 2[4Fe-4S] homology #label FER1\ !$118-180 #domain ferredoxin 2[4Fe-4S] homology #status !8atypical #label FER2\ !$46,49,52,104 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$56,92,95,100 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$125,128,131,172 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$135,152,155,168 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 223 #molecular-weight 24567 #checksum 8529 SEQUENCE /// ENTRY A64181 #type complete TITLE nrfC protein - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 18-Aug-1995 #sequence_revision 26-Jul-1996 #text_change 20-Apr-2000 ACCESSIONS A64181 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession A64181 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-225 ##label TIGR !'##cross-references GB:U32787; GB:L42023; NID:g1574619; !1PIDN:AAC22725.1; PID:g1574621; TIGR:HI1067 !'##note named as homolog to a protein from Escherichia coli GENETICS !$#gene nrfC FUNCTION !$#description probably involved in the transfer of electrons from the !1quinone pool to the type-c cytochromes; essential for the !1formate-dependent nitrite reductase activity CLASSIFICATION #superfamily nrfC protein; ferredoxin 2[4Fe-4S] homology KEYWORDS 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein FEATURE !$41-114 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$120-182 #domain ferredoxin 2[4Fe-4S] homology #status !8atypical #label FER2\ !$48,51,54,106 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$58,94,97,102 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$127,130,133,174 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$137,154,157,170 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 225 #molecular-weight 25105 #checksum 5660 SEQUENCE /// ENTRY S23458 #type complete TITLE polysulfide reductase (EC 1.-.-.-) iron-sulfur protein psrB - Wolinella succinogenes ORGANISM #formal_name Wolinella succinogenes DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S23458 REFERENCE S23457 !$#authors Krafft, T.; Bokranz, M.; Klimmek, O.; Schroeder, I.; !1Fahrenholz, F.; Kojro, E.; Kroeger, A. !$#journal Eur. J. Biochem. (1992) 206:503-510 !$#title Cloning and nucleotide sequence of the psrA gene of !1Wolinella succinogenes polysulphide reductase. !$#cross-references MUID:92283277; PMID:1597189 !$#accession S23458 !'##molecule_type DNA !'##residues 1-191 ##label KRA !'##cross-references EMBL:X65042; NID:g48525; PIDN:CAA46177.1; !1PID:g48527 GENETICS !$#gene psrB CLASSIFICATION #superfamily nrfC protein; ferredoxin 2[4Fe-4S] homology KEYWORDS 4Fe-4S; iron-sulfur protein; metalloprotein; oxidoreductase FEATURE !$7-81 #domain ferredoxin 2[4Fe-4S] homology #label FER1\ !$86-148 #domain ferredoxin 2[4Fe-4S] homology #status !8atypical #label FER2\ !$14,17,20,73 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$24,61,64,69 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$93,96,99,140 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$103,120,123,136 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 191 #molecular-weight 20945 #checksum 7102 SEQUENCE /// ENTRY B57143 #type complete TITLE thiosulfate-dithiol sulfurtransferase (EC 2.8.1.5) phsB chain - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS B57143 REFERENCE A57143 !$#authors Heinzinger, N.K.; Fujimoto, S.Y.; Clark, M.A.; Moreno, M.S.; !1Barrett, E.L. !$#journal J. Bacteriol. (1995) 177:2813-2820 !$#title Sequence analysis of the phs operon in Salmonella !1typhimurium and the contribution of thiosulfate reduction to !1anaerobic energy metabolism. !$#cross-references MUID:95270599; PMID:7751291 !$#accession B57143 !'##status preliminary !'##molecule_type DNA !'##residues 1-192 ##label HEI !'##cross-references GB:L32188; NID:g755675; PIDN:AAC36935.1; !1PID:g755677 CLASSIFICATION #superfamily nrfC protein; ferredoxin 2[4Fe-4S] homology KEYWORDS sulfurtransferase FEATURE !$57-114 #domain ferredoxin 2[4Fe-4S] homology #label FER SUMMARY #length 192 #molecular-weight 21320 #checksum 5653 SEQUENCE /// ENTRY D57987 #type complete TITLE nrfD protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 26-Jul-1996 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS H65215; D57987 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65215 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-318 ##label BLAT !'##cross-references GB:AE000480; GB:U00096; NID:g2367344; !1PIDN:AAC77043.1; PID:g1790509; UWGP:b4073 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A57987 !$#authors Hussain, H.; Grove, J.; Griffiths, L.; Busby, S.; Cole, J. !$#journal Mol. Microbiol. (1994) 12:153-163 !$#title A seven-gene operon essential for formate-dependent nitrite !1reduction to ammonia by enteric bacteria. !$#cross-references MUID:94335626; PMID:8057835 !$#accession D57987 !'##molecule_type DNA !'##residues 1-140,'V',142-201,'R',203-318 ##label HUS !'##cross-references EMBL:X72298; NID:g404302; PIDN:CAA51044.1; !1PID:g404305 GENETICS !$#gene nrfD !$#note this is one of the seven gene operon (nrf) essential for !1formate-dependent nitrite reduction to ammonia FUNCTION !$#description probably involved in the transfer of electrons from the !1quinone pool to the type-c cytochromes; essential for the !1pathway of formate-dependent nitrite reduction to ammonia CLASSIFICATION #superfamily nrfD protein KEYWORDS transmembrane protein FEATURE !$128-144 #domain transmembrane #status predicted #label TMM1\ !$302-318 #domain transmembrane #status predicted #label TMM2 SUMMARY #length 318 #molecular-weight 35042 #checksum 587 SEQUENCE /// ENTRY I64180 #type complete TITLE nrfD protein - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 18-Aug-1995 #sequence_revision 26-Jul-1996 #text_change 11-Jun-1999 ACCESSIONS I64180 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession I64180 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-321 ##label TIGR !'##cross-references GB:U32787; GB:L42023; NID:g1574619; !1PIDN:AAC22724.1; PID:g1574620; TIGR:HI1066 !'##note named as homolog to a protein from Escherichia coli GENETICS !$#gene nrfD FUNCTION !$#description probably involved in the transfer of electrons from the !1quinone pool to the type-c cytochromes; essential for the !1pathway of formate-dependent nitrite reduction to ammonia CLASSIFICATION #superfamily nrfD protein KEYWORDS transmembrane protein FEATURE !$130-146 #domain transmembrane #status predicted #label TMM1\ !$305-321 #domain transmembrane #status predicted #label TMM2 SUMMARY #length 321 #molecular-weight 35944 #checksum 845 SEQUENCE /// ENTRY E57987 #type complete TITLE cytochrome c-type biogenesis protein nrfE - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 26-Jul-1996 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS A65216; E57987 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65216 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-552 ##label BLAT !'##cross-references GB:AE000481; GB:U00096; NID:g2367346; !1PIDN:AAD13457.1; PID:g1790511; UWGP:b4074 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A57987 !$#authors Hussain, H.; Grove, J.; Griffiths, L.; Busby, S.; Cole, J. !$#journal Mol. Microbiol. (1994) 12:153-163 !$#title A seven-gene operon essential for formate-dependent nitrite !1reduction to ammonia by enteric bacteria. !$#cross-references MUID:94335626; PMID:8057835 !$#accession E57987 !'##molecule_type DNA !'##residues 1-31,'V',33-37,'A',39-189,'S',191-217,'L',219,'RLVVLGS', !1227-454,'A',456-480,'A',482-552 ##label HUS !'##cross-references EMBL:X72298; NID:g404302; PIDN:CAA51045.1; !1PID:g581146 GENETICS !$#gene nrfE !$#note this is one of the seven gene operon (nrf) essential for !1formate-dependent nitrite reduction to ammonia FUNCTION !$#description an inner membrane protein, possible component of a heme !1lyase, which is required for the biosythesis of the !1cytochrome c type proteins (nrfA and nrfB); essential for !1the formate-dependent nitrite reductase activity CLASSIFICATION #superfamily nrfE protein KEYWORDS membrane protein SUMMARY #length 552 #molecular-weight 61294 #checksum 8574 SEQUENCE /// ENTRY A64167 #type complete TITLE cytochrome c-type synthesis protein HI1094 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A64167 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession A64167 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-648 ##label TIGR !'##cross-references GB:U32789; GB:L42023; NID:g1574642; !1PIDN:AAC22751.1; PID:g1574649; TIGR:HI1094 CLASSIFICATION #superfamily nrfE protein SUMMARY #length 648 #molecular-weight 72353 #checksum 6169 SEQUENCE /// ENTRY A64162 #type complete TITLE cytochrome c-type synthesis protein HI0936 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A64162 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession A64162 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-635 ##label TIGR !'##cross-references GB:U32775; GB:L42023; NID:g1573951; !1PIDN:AAC22594.1; PID:g1573957; TIGR:HI0936 CLASSIFICATION #superfamily nrfE protein SUMMARY #length 635 #molecular-weight 71273 #checksum 5963 SEQUENCE /// ENTRY S54750 #type complete TITLE cytochrome c-type synthesis protein cycK - Rhizobium meliloti ORGANISM #formal_name Rhizobium meliloti DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S54750; S49616 REFERENCE S54748 !$#authors Kereszt, A.; Slaska-Kiss, K.; Putnoky, P.; Banfalvi, Z.; !1Kondorosi, A. !$#journal Mol. Gen. Genet. (1995) 247:39-47 !$#title The cycHJKL genes of Rhizobium meliloti involved in !1cytochrome c biogenesis are required for "respiratory" !1nitrate reduction ex planta and for nitrogen fixation during !1symbiosis. !$#cross-references MUID:95231514; PMID:7715602 !$#accession S54750 !'##status preliminary; nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-676 ##label KER !'##cross-references EMBL:X82560; NID:g575369; PIDN:CAA57906.1; !1PID:g575372 GENETICS !$#gene cycK CLASSIFICATION #superfamily nrfE protein SUMMARY #length 676 #molecular-weight 72643 #checksum 6524 SEQUENCE /// ENTRY S23667 #type complete TITLE cytochrome c-type synthesis protein ccl1 - Rhodobacter capsulatus ORGANISM #formal_name Rhodobacter capsulatus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S23667 REFERENCE S23662 !$#authors Beckman, D.L.; Trawick, D.R.; Kranz, R.G. !$#journal Genes Dev. (1992) 6:268-283 !$#title Bacterial cytochromes c biogenesis. !$#cross-references MUID:92146961; PMID:1310666 !$#accession S23667 !'##status preliminary !'##molecule_type DNA !'##residues 1-653 ##label BEC !'##cross-references EMBL:X63461; NID:g45993; PIDN:CAA45058.1; !1PID:g45994 CLASSIFICATION #superfamily nrfE protein KEYWORDS transmembrane protein SUMMARY #length 653 #molecular-weight 70551 #checksum 2310 SEQUENCE /// ENTRY S54746 #type complete TITLE cytochrome c-type synthesis protein cycK - Bradyrhizobium japonicum ORGANISM #formal_name Bradyrhizobium japonicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S54746 REFERENCE S54745 !$#authors Ritz, D.; Thoeny-Meyer, L.; Hennecke, H. !$#journal Mol. Gen. Genet. (1995) 247:27-38 !$#title The cycHJKL gene cluster plays an essential role in the !1biogenesis of c-type cytochromes in Bradyrhizobium !1japonicum. !$#cross-references MUID:95231513; PMID:7715601 !$#accession S54746 !'##status preliminary; nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-660 ##label RIT !'##cross-references EMBL:Z46607; NID:g572600; PIDN:CAA86575.1; !1PID:g572603 GENETICS !$#gene cycK !$#start_codon GTG CLASSIFICATION #superfamily nrfE protein SUMMARY #length 660 #molecular-weight 71083 #checksum 2154 SEQUENCE /// ENTRY S58614 #type complete TITLE cytochrome c-type synthesis protein homolog - maize chloroplast ALTERNATE_NAMES hypothetical protein 321 ORGANISM #formal_name chloroplast Zea mays #common_name maize DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S58614 REFERENCE S58531 !$#authors Maier, R.M.; Neckermann, K.; Igloi, G.L.; Koessel, H. !$#journal J. Mol. Biol. (1995) 251:614-628 !$#title Complete sequence of the maize chloroplast genome: gene !1content, hotspots of divergence and fine tuning of genetic !1information by transcript editing. !$#cross-references MUID:95395841; PMID:7666415 !$#accession S58614 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-321 ##label MAI !'##cross-references EMBL:X86563; NID:g902200; PIDN:CAA60348.1; !1PID:g902283 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1995 GENETICS !$#genome chloroplast CLASSIFICATION #superfamily cytochrome c-type synthesis protein KEYWORDS chloroplast SUMMARY #length 321 #molecular-weight 36693 #checksum 974 SEQUENCE /// ENTRY JQ0288 #type complete TITLE cytochrome c-type synthesis protein protein homolog - rice chloroplast ALTERNATE_NAMES hypothetical 36.7K protein (trnL-trnN intergenic region) ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JQ0288; S05167 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0288 !'##molecule_type DNA !'##residues 1-321 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05167 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-321 ##label HIR !'##cross-references GB:X15901; NID:g11957; PIDN:CAA33952.1; PID:g12049 !'##experimental_source cv. Nihonbare GENETICS !$#genome chloroplast CLASSIFICATION #superfamily cytochrome c-type synthesis protein KEYWORDS chloroplast SUMMARY #length 321 #molecular-weight 36702 #checksum 7954 SEQUENCE /// ENTRY A05213 #type complete TITLE cytochrome c-type synthesis protein homolog - common tobacco chloroplast ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A05213 REFERENCE A00149 !$#authors Sugiura, M. !$#submission submitted to the EMBL Data Library, August 1986 !$#accession A05213 !'##molecule_type DNA !'##residues 1-313 ##label SUG !'##experimental_source cv. Bright Yellow 4 REFERENCE A38013 !$#authors Shinozaki, K.; Ohme, M.; Tanaka, M.; Wakasugi, T.; !1Hayashida, N.; Matsubayashi, T.; Zaita, N.; Chunwongse, J.; !1Obokata, J.; Yamaguchi-Shinozaki, K.; Ohto, C.; Torazawa, !1K.; Meng, B.Y.; Sugita, M.; Deno, H.; Kamogashira, T.; !1Yamada, K.; Kusuda, J.; Takaiwa, F.; Kato, A.; Tohdoh, N.; !1Shimada, H.; Sugiura, M. !$#journal EMBO J. (1986) 5:2043-2049 !$#title The complete nucleotide sequence of the tobacco chloroplast !1genome: its gene organization and expression. !$#contents annotation; gene organization, sites, features GENETICS !$#genome chloroplast CLASSIFICATION #superfamily cytochrome c-type synthesis protein KEYWORDS chloroplast SUMMARY #length 313 #molecular-weight 35558 #checksum 6803 SEQUENCE /// ENTRY A05023 #type complete TITLE cytochrome c-type synthesis protein homolog - liverwort (Marchantia polymorpha) chloroplast ALTERNATE_NAMES hypothetical protein 320 ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S01516; A05023 REFERENCE S01512 !$#authors Kohchi, T.; Shirai, H.; Fukuzawa, H.; Sano, T.; Komano, T.; !1Umesono, K.; Inokuchi, H.; Ozeki, H.; Ohyama, K. !$#journal J. Mol. Biol. (1988) 203:353-372 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. IV. Inverted repeat and small single !1copy regions. !$#cross-references MUID:89068688; PMID:3199437 !$#accession S01516 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-320 ##label KOH !'##cross-references EMBL:X04465; NID:g11640; PIDN:CAA28133.1; !1PID:g11722 REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features GENETICS !$#genome chloroplast CLASSIFICATION #superfamily cytochrome c-type synthesis protein KEYWORDS chloroplast SUMMARY #length 320 #molecular-weight 37170 #checksum 3085 SEQUENCE /// ENTRY S73290 #type complete TITLE cytochrome c-type synthesis protein homolog - red alga (Porphyra purpurea) chloroplast ORGANISM #formal_name chloroplast Porphyra purpurea DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S73290 REFERENCE S73108 !$#authors Reith, M.; Munholland, J. !$#journal Plant Mol. Biol. Rep. (1995) 13:333-335 !$#title Complete nucleotide sequence of the Porphyra purpurea !1chloroplast genome. !$#accession S73290 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-319 ##label REI !'##cross-references EMBL:U38804; NID:g1276652; PIDN:AAC08255.1; !1PID:g1276835 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1995 GENETICS !$#gene ycf5 !$#genome chloroplast CLASSIFICATION #superfamily cytochrome c-type synthesis protein KEYWORDS chloroplast SUMMARY #length 319 #molecular-weight 35213 #checksum 9725 SEQUENCE /// ENTRY S25309 #type complete TITLE cytochrome c-type synthesis protein homolog - red alga (Cyanidium caldarium) chloroplast ALTERNATE_NAMES hypothetical protein (cpcL 3' region) ORGANISM #formal_name chloroplast Cyanidium caldarium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S25309; S14520 REFERENCE S25306 !$#authors Valentin, K.; Maid, U.; Emich, A.; Zetsche, K. !$#journal Plant Mol. Biol. (1992) 20:267-276 !$#title Organization and expression of a phycobiliprotein gene !1cluster from the unicellular red alga Cyanidium caldarium. !$#cross-references MUID:93004479; PMID:1391770 !$#accession S25309 !'##molecule_type DNA !'##residues 1-306 ##label VAL !'##cross-references EMBL:X57150; NID:g11344; PIDN:CAA40439.1; !1PID:g11345 GENETICS !$#genome chloroplast CLASSIFICATION #superfamily cytochrome c-type synthesis protein KEYWORDS chloroplast SUMMARY #length 306 #molecular-weight 35263 #checksum 8924 SEQUENCE /// ENTRY S10456 #type complete TITLE cytochrome c-type synthesis protein homolog - Cryptomonas sp. chloroplast ALTERNATE_NAMES hypothetical protein (cpeB 3' region) ORGANISM #formal_name chloroplast Cryptomonas sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S10456 REFERENCE S10455 !$#authors Reith, M.; Douglas, S. !$#submission submitted to the EMBL Data Library, March 1990 !$#accession S10456 !'##molecule_type DNA !'##residues 1-301 ##label REI !'##cross-references EMBL:X52159; NID:g11374; PIDN:CAA36413.1; !1PID:g11376 GENETICS !$#genome chloroplast CLASSIFICATION #superfamily cytochrome c-type synthesis protein KEYWORDS chloroplast SUMMARY #length 301 #molecular-weight 34193 #checksum 5421 SEQUENCE /// ENTRY S74957 #type complete TITLE cytochrome c-type synthesis protein - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein sll1513 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S74957 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74957 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-334 ##label KAN !'##cross-references EMBL:D90902; GB:AB001339; NID:g1652027; !1PIDN:BAA16997.1; PID:g1652072 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene ccsA CLASSIFICATION #superfamily cytochrome c-type synthesis protein SUMMARY #length 334 #molecular-weight 36077 #checksum 6583 SEQUENCE /// ENTRY S72913 #type complete TITLE cytochrome c-type synthesis protein homolog - Mycobacterium leprae ALTERNATE_NAMES hypothetical protein B2168_C3_281 ORGANISM #formal_name Mycobacterium leprae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 23-Mar-2001 ACCESSIONS S72913 REFERENCE S72586 !$#authors Smith, D.R.; Robison, K. !$#submission submitted to the EMBL Data Library, November 1993 !$#description Mycobacterium leprae cosmid B2168. !$#accession S72913 !'##status preliminary !'##molecule_type DNA !'##residues 1-327 ##label SMI !'##cross-references EMBL:U00018; NID:g467037; PIDN:AAA17249.1; !1PID:g467065 CLASSIFICATION #superfamily cytochrome c-type synthesis protein SUMMARY #length 327 #molecular-weight 35844 #checksum 5263 SEQUENCE /// ENTRY F57987 #type complete TITLE cytochrome c-type biogenesis protein nrfF precursor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 26-Jul-1996 #sequence_revision 26-Jul-1996 #text_change 01-Mar-2002 ACCESSIONS F57987; B65216 REFERENCE A57987 !$#authors Hussain, H.; Grove, J.; Griffiths, L.; Busby, S.; Cole, J. !$#journal Mol. Microbiol. (1994) 12:153-163 !$#title A seven-gene operon essential for formate-dependent nitrite !1reduction to ammonia by enteric bacteria. !$#cross-references MUID:94335626; PMID:8057835 !$#accession F57987 !'##status preliminary !'##molecule_type DNA !'##residues 1-127 ##label HUS !'##cross-references EMBL:X72298; NID:g404302; PIDN:CAA51046.1; !1PID:g404307 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65216 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-127 ##label BLAT !'##cross-references GB:AE000481; GB:U00096; NID:g2367346; !1PIDN:AAD13458.1; PID:g1790512; UWGP:b4075 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene nrfF !$#note this is one of the seven gene operon (nrf) essential for !1formate-dependent nitrite reduction to ammonia FUNCTION !$#description possible component of a heme lyase, which is required for !1the biosythesis of the cytochrome c type proteins (nrfA and !1nrfB); essential for the pathway of formate-dependent !1nitrite reduction to ammonia CLASSIFICATION #superfamily nrfF protein FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-127 #product nrfB protein #status predicted #label MAT SUMMARY #length 127 #molecular-weight 14523 #checksum 2922 SEQUENCE /// ENTRY A57987 #type complete TITLE nrfG protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 26-Jul-1996 #sequence_revision 26-Jul-1996 #text_change 01-Mar-2002 ACCESSIONS A57987; C65216 REFERENCE A57987 !$#authors Hussain, H.; Grove, J.; Griffiths, L.; Busby, S.; Cole, J. !$#journal Mol. Microbiol. (1994) 12:153-163 !$#title A seven-gene operon essential for formate-dependent nitrite !1reduction to ammonia by enteric bacteria. !$#cross-references MUID:94335626; PMID:8057835 !$#accession A57987 !'##status preliminary !'##molecule_type DNA !'##residues 1-198 ##label HUS !'##cross-references EMBL:X72298; NID:g404302; PIDN:CAA51047.1; !1PID:g404308 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65216 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-198 ##label BLAT !'##cross-references GB:AE000481; GB:U00096; NID:g2367346; !1PIDN:AAD13459.1; PID:g1790513; UWGP:b4076 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene nrfG !$#note this is one of the seven gene operon (nrf) essential for !1formate-dependent nitrite reduction to ammonia FUNCTION !$#description essential for the formate-dependent nitrite reductase !1activity CLASSIFICATION #superfamily nrfG protein SUMMARY #length 198 #molecular-weight 22784 #checksum 6617 SEQUENCE /// ENTRY RDECNA #type complete TITLE nitrate reductase (EC 1.7.99.4) 1 alpha chain - Escherichia coli (strain K-12) ALTERNATE_NAMES respiratory nitrate reductase alpha chain ORGANISM #formal_name Escherichia coli DATE 30-Sep-1990 #sequence_revision 21-Nov-1997 #text_change 01-Mar-2002 ACCESSIONS E64869; JV0037; A24610; S05253; A31911; I41103 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64869 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1247 ##label BLAT !'##cross-references GB:AE000221; GB:U00096; NID:g1787476; !1PIDN:AAC74308.1; PID:g1787477; UWGP:b1224 !'##experimental_source strain K-12, substrain MG1655 REFERENCE JV0037 !$#authors Blasco, F.; Iobbi, C.; Giordano, G.; Chippaux, M.; Bonnefoy, !1V. !$#journal Mol. Gen. Genet. (1989) 218:249-256 !$#title Nitrate reductase of Escherichia coli: completion of the !1nucleotide sequence of the nar operon and reassessment of !1the role of the alpha and beta subunits in iron binding and !1electron transfer. !$#cross-references MUID:89384449; PMID:2674654 !$#accession JV0037 !'##molecule_type DNA !'##residues 1-149,'NAGAWTR',157-309,'GIPPRATQASISGLCACTRHADAGDAGRT', !1311,348-1247 ##label BLA !'##experimental_source strain TG1 REFERENCE A24610 !$#authors Li, S.; Rabi, T.; DeMoss, J.A. !$#journal J. Bacteriol. (1985) 164:25-32 !$#title Delineation of two distinct regulatory domains in the 5' !1region of the nar operon of Escherichia coli. !$#cross-references MUID:86008060; PMID:2995309 !$#accession A24610 !'##molecule_type DNA !'##residues 1-21 ##label LIS !'##experimental_source strain PK27 REFERENCE S05239 !$#authors Noji, S.; Nohno, T.; Saito, T.; Taniguchi, S. !$#journal FEBS Lett. (1989) 252:139-143 !$#title The narK gene product participates in nitrate transport !1induced in Escherichia coli nitrate-respiring cells. !$#cross-references MUID:89338707; PMID:2668029 !$#accession S05253 !'##molecule_type DNA !'##residues 1-23 ##label NOJ !'##cross-references EMBL:X15996; NID:g42089; PIDN:CAA34127.1; !1PID:g42092 !'##experimental_source strain K-12 REFERENCE A92678 !$#authors Sodergren, E.J.; Hsu, P.Y.; DeMoss, J.A. !$#journal J. Biol. Chem. (1988) 263:16156-16162 !$#title Roles of the narJ and narI gene products in the expression !1of nitrate reductase in Escherichia coli. !$#cross-references MUID:89034078; PMID:3053688 !$#accession A31911 !'##molecule_type protein !'##residues 2-9,'K',11 ##label SOD REFERENCE I41103 !$#authors McPherson, M.J.; Baron, A.J.; Pappin, D.J.; Wootton, J.C. !$#journal FEBS Lett. (1984) 177:260-264 !$#title Respiratory nitrate reductase of Escherichia coli. Sequence !1identification of the large subunit gene. !$#cross-references MUID:85051857; PMID:6094247 !$#accession I41103 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-148 ##label RES !'##cross-references EMBL:X01164; NID:g42083; PIDN:CAA25611.1; !1PID:g42084 GENETICS !$#gene narG; narC; bisD !$#map_position 27 min COMPLEX heterotetramer of one alpha, one beta (see PIR:RDECNB), and !1two gamma chains(see PIR:RDECNG) FUNCTION !$#description catalyzes the reversible reduction of nitrate to nitrite CLASSIFICATION #superfamily nitrate reductase alpha chain KEYWORDS 4Fe-4S; electron transfer; iron-sulfur protein; !1membrane-associated complex; metalloprotein; molybdenum; !1oxidoreductase FEATURE !$54,58,93 #binding_site iron-sulfur clusters (Cys) (covalent) !8#status predicted SUMMARY #length 1247 #molecular-weight 140488 #checksum 6063 SEQUENCE /// ENTRY RDECNB #type complete TITLE nitrate reductase (EC 1.7.99.4) 1 beta chain - Escherichia coli (strain K-12) ALTERNATE_NAMES respiratory nitrate reductase beta chain ORGANISM #formal_name Escherichia coli DATE 31-Mar-1989 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS F64869; JV0038; A27737; B31911 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64869 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-512 ##label BLAT !'##cross-references GB:AE000221; GB:U00096; NID:g1787476; !1PIDN:AAC74309.1; PID:g1787478; UWGP:b1225 !'##experimental_source strain K-12, substrain MG1655 REFERENCE JV0037 !$#authors Blasco, F.; Iobbi, C.; Giordano, G.; Chippaux, M.; Bonnefoy, !1V. !$#journal Mol. Gen. Genet. (1989) 218:249-256 !$#title Nitrate reductase of Escherichia coli: completion of the !1nucleotide sequence of the nar operon and reassessment of !1the role of the alpha and beta subunits in iron binding and !1electron transfer. !$#cross-references MUID:89384449; PMID:2674654 !$#accession JV0038 !'##molecule_type DNA !'##residues 1-397,'EYQTGTARTETYAGDASLQT',418-512 ##label BLA !'##experimental_source strain TG1 !'##note the sequence of residues 1-10 was confirmed by protein !1sequencing REFERENCE A91868 !$#authors Sodergren, E.J.; DeMoss, J.A. !$#journal J. Bacteriol. (1988) 170:1721-1729 !$#title narI region of the Escherichia coli nitrate reductase (nar) !1operon contains two genes. !$#cross-references MUID:88169497; PMID:2832376 !$#accession A27737 !'##molecule_type DNA !'##residues 365-397,'EYQTGTARTETYAGDASLQT',418-512 ##label SOD !'##cross-references GB:M20147; NID:g146918; PIDN:AAA24195.1; !1PID:g146919 REFERENCE A92678 !$#authors Sodergren, E.J.; Hsu, P.Y.; DeMoss, J.A. !$#journal J. Biol. Chem. (1988) 263:16156-16162 !$#title Roles of the narJ and narI gene products in the expression !1of nitrate reductase in Escherichia coli. !$#cross-references MUID:89034078; PMID:3053688 !$#accession B31911 !'##molecule_type protein !'##residues 1-6,'Y',8-10 ##label SO2 GENETICS !$#gene narH !$#map_position 27 min COMPLEX heterotetramer of one alpha (see PIR:RDECNA), one beta, and !1two gamma chains(see PIR:RDECNG) FUNCTION !$#description catalyzes the reversible reduction of nitrate to nitrite CLASSIFICATION #superfamily nitrate reductase beta chain; ferredoxin !12[4Fe-4S] homology KEYWORDS 4Fe-4S; electron transfer; iron-sulfur protein; membrane !1bound; metalloprotein; oxidoreductase FEATURE !$177-235 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$184,187,192,227 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$196,213,217,223 #binding_site 4Fe-4S cluster (Cys, Asp, Cys, Cys) !8(covalent) #status predicted SUMMARY #length 512 #molecular-weight 58066 #checksum 585 SEQUENCE /// ENTRY RDECNG #type complete TITLE nitrate reductase (EC 1.7.99.4) 1 gamma chain - Escherichia coli (strain K-12) ALTERNATE_NAMES cytochrome b-NR; respiratory nitrate reductase gamma chain ORGANISM #formal_name Escherichia coli DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 01-Mar-2002 ACCESSIONS C27737; C31911; H64869 REFERENCE A91868 !$#authors Sodergren, E.J.; DeMoss, J.A. !$#journal J. Bacteriol. (1988) 170:1721-1729 !$#title narI region of the Escherichia coli nitrate reductase (nar) !1operon contains two genes. !$#cross-references MUID:88169497; PMID:2832376 !$#accession C27737 !'##molecule_type DNA !'##residues 1-225 ##label SOD !'##cross-references GB:M20147; NID:g146918; PIDN:AAA24197.1; !1PID:g146921 REFERENCE A92678 !$#authors Sodergren, E.J.; Hsu, P.Y.; DeMoss, J.A. !$#journal J. Biol. Chem. (1988) 263:16156-16162 !$#title Roles of the narJ and narI gene products in the expression !1of nitrate reductase in Escherichia coli. !$#cross-references MUID:89034078; PMID:3053688 !$#accession C31911 !'##molecule_type protein !'##residues 1-5,'F',7-8,'D' ##label SO2 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64869 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-225 ##label BLAT !'##cross-references GB:AE000221; GB:U00096; NID:g1787476; !1PIDN:AAC74311.1; PID:g1787480; UWGP:b1227 !'##experimental_source strain K-12, substrain MG1655 COMMENT This form of the enzyme is induced by nitrate. GENETICS !$#gene narI; chlI !$#map_position 27 min COMPLEX heterotetramer of one alpha (see PIR:RDECNA), one beta (see !1PIR:RDECNB), and two gamma chains FUNCTION !$#description catalyzes the reversible reduction of nitrate to nitrite CLASSIFICATION #superfamily nitrate reductase gamma chain KEYWORDS chromoprotein; electron transfer; heme; iron; !1membrane-associated complex; metalloprotein; oxidoreductase; !1transmembrane protein FEATURE !$6-22 #domain transmembrane #status predicted #label TM1\ !$54-70 #domain transmembrane #status predicted #label TM2\ !$93-109 #domain transmembrane #status predicted #label TM3\ !$128-144 #domain transmembrane #status predicted #label TM4\ !$182-198 #domain transmembrane #status predicted #label TM5\ !$56,205 #binding_site heme iron (His) (axial ligands) (high !8potential) #status predicted\ !$66,187 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted SUMMARY #length 225 #molecular-weight 25497 #checksum 3511 SEQUENCE /// ENTRY RDECMH #type complete TITLE 5,10-methylenetetrahydrofolate reductase (FADH2) (EC 1.7.99.5) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 01-Mar-2002 ACCESSIONS A00462; S40884; H65200 REFERENCE A00462 !$#authors Saint-Girons, I.; Duchange, N.; Zakin, M.M.; Park, I.; !1Margarita, D.; Ferrara, P.; Cohen, G.N. !$#journal Nucleic Acids Res. (1983) 11:6723-6732 !$#title Nucleotide sequence of metF, the Escherichia coli structural !1gene for 5-10 methylene tetrahydrofolate reductase and of !1its control reigon. !$#cross-references MUID:84041480; PMID:6356036 !$#accession A00462 !'##molecule_type DNA !'##residues 1-296 ##label SAI !'##cross-references GB:V01502; NID:g41999; PIDN:CAA24747.1; PID:g42000 REFERENCE S40802 !$#authors Plunkett III, G.; Burland, V.; Daniels, D.L.; Blattner, F.R. !$#journal Nucleic Acids Res. (1993) 21:3391-3398 !$#title Analysis of the Escherichia coli genome. III. DNA sequence !1of the region from 87.2 to 89.2 minutes. !$#cross-references MUID:93347969; PMID:8346018 !$#accession S40884 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-296 ##label PLU !'##cross-references EMBL:L19201; NID:g304961; PIDN:AAB03073.1; !1PID:g305044 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1993 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65200 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-296 ##label BLAT !'##cross-references GB:AE000468; GB:U00096; NID:g1790374; !1PIDN:AAC76923.1; PID:g1790377; UWGP:b3941 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene metF !$#map_position 89 min FUNCTION !$#description in the presence of reduced FAD, catalyzes the formation of !15-N-methyltetrahydrofolate, which is the methyl donor for !1methionine biosynthesis !$#pathway methionine biosynthesis CLASSIFICATION #superfamily 5,10-methylenetetrahydrofolate reductase !1(FADH2) KEYWORDS methionine biosynthesis; oxidoreductase SUMMARY #length 296 #molecular-weight 33102 #checksum 1239 SEQUENCE /// ENTRY S03169 #type complete TITLE 5,10-methylenetetrahydrofolate reductase (FADH2) (EC 1.7.99.5) - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S03169 REFERENCE S03169 !$#authors Stauffer, G.V.; Stauffer, L.T. !$#journal Mol. Gen. Genet. (1988) 212:246-251 !$#title Cloning and nucleotide sequence of the Salmonella !1typhimurium LT2 metF gene and its homology with the !1corresponding sequence of Escherichia coli. !$#cross-references MUID:88302115; PMID:2841568 !$#accession S03169 !'##molecule_type DNA !'##residues 1-296 ##label STA !'##cross-references EMBL:X07689 GENETICS !$#gene metF CLASSIFICATION #superfamily 5,10-methylenetetrahydrofolate reductase !1(FADH2) KEYWORDS oxidoreductase SUMMARY #length 296 #molecular-weight 33173 #checksum 1242 SEQUENCE /// ENTRY H64123 #type complete TITLE 5,10-methylenetetrahydrofolate reductase (FADH2) (EC 1.7.99.5) - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS H64123 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession H64123 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-292 ##label TIGR !'##cross-references GB:U32823; GB:L42023; NID:g1574281; !1PIDN:AAC23094.1; PID:g1574284; TIGR:HI1444 CLASSIFICATION #superfamily 5,10-methylenetetrahydrofolate reductase !1(FADH2) KEYWORDS methionine biosynthesis; oxidoreductase SUMMARY #length 292 #molecular-weight 33020 #checksum 950 SEQUENCE /// ENTRY A31845 #type complete TITLE nitrous-oxide reductase (EC 1.7.99.6) precursor [similarity] - Pseudomonas stutzeri ORGANISM #formal_name Pseudomonas stutzeri DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS A31845; S28447; B42953; S13582 REFERENCE A31845 !$#authors Viebrock, A.; Zumft, W.G. !$#journal J. Bacteriol. (1988) 170:4658-4668 !$#title Molecular cloning, heterologous expression, and primary !1structure of the structural gene for the copper enzyme !1nitrous oxide reductase from denitrifying Pseudomonas !1stutzeri. !$#cross-references MUID:89008083; PMID:3049543 !$#accession A31845 !'##molecule_type DNA !'##residues 1-638 ##label VIE !'##cross-references GB:M22628; NID:g340729; PIDN:AAA25907.1; !1PID:g387863 REFERENCE S28446 !$#authors Zumft, W.G. !$#submission submitted to the EMBL Data Library, July 1992 !$#accession S28447 !'##molecule_type DNA !'##residues 1-27 ##label ZUM !'##cross-references EMBL:Z13988; NID:g45857; PIDN:CAA78381.1; !1PID:g45859 REFERENCE A42953 !$#authors Cuypers, H.; Viebrock-Sambale, A.; Zumft, W.G. !$#journal J. Bacteriol. (1992) 174:5332-5339 !$#title NosR, a membrane-bound regulatory component necessary for !1expression of nitrous oxide reductase in denitrifying !1Pseudomonas stutzeri. !$#cross-references MUID:92355508; PMID:1644760 !$#accession B42953 !'##molecule_type DNA !'##residues 1-14,'E',15-26 ##label CUY !'##experimental_source ZoBell, ATCC 14405 !'##note sequence is inconsistent with the nucleotide translation !'##note sequence extracted from NCBI backbone (NCBIN:110502, !1NCBIP:110504) REFERENCE S13582 !$#authors Zumft, W.G.; Viebrock-Sambale, A.; Braun, C. !$#journal Eur. J. Biochem. (1990) 192:591-599 !$#title Nitrous oxide reductase from denitrifying Pseudomonas !1stutzeri. Genes for copper-processing and properties of the !1deduced products, including a new member of the family of !1ATP/GTP-binding proteins. !$#cross-references MUID:91006150; PMID:2170125 !$#accession S13582 !'##molecule_type DNA !'##residues 618-638 ##label ZU2 !'##cross-references EMBL:X53676; NID:g45844; PIDN:CAA37714.1; !1PID:g747877 GENETICS !$#gene nosZ CLASSIFICATION #superfamily nitrous-oxide reductase KEYWORDS copper; metalloprotein; oxidoreductase FEATURE !$583,618,622 #binding_site copper 1 (His, Cys, Cys) #status !8predicted\ !$618,620,622,626 #binding_site copper 2 (Cys, Trp, Cys, His) #status !8predicted SUMMARY #length 638 #molecular-weight 70822 #checksum 4964 SEQUENCE /// ENTRY S24384 #type complete TITLE nitrous-oxide reductase (EC 1.7.99.6) [similarity] - Pseudomonas stutzeri ORGANISM #formal_name Pseudomonas stutzeri DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS S24384 REFERENCE S24382 !$#authors Zumft, W.G.; Dreusch, A.; Loechelt, S.; Cuypers, H.; !1Friedrich, B.; Schneider, B. !$#journal Eur. J. Biochem. (1992) 208:31-40 !$#title Derived amino acid sequences of the nosZ gene (respiratory N !1(2)O reductase) from Alcaligenes eutrophus, Pseudomonas !1aeruginosa and Pseudomonas stutzeri reveal potential !1copper-binding residues. Implications for the Cu(A) site of !1N(2)O reductase and cytochrome-c oxidase. !$#cross-references MUID:92380183; PMID:1324835 !$#accession S24384 !'##molecule_type DNA !'##residues 1-634 ##label ZUM !'##cross-references EMBL:X65277; NID:g45853; PIDN:CAA46381.1; !1PID:g45855 CLASSIFICATION #superfamily nitrous-oxide reductase KEYWORDS copper; metalloprotein; oxidoreductase FEATURE !$579,614,618 #binding_site copper 1 (His, Cys, Cys) #status !8predicted\ !$614,616,618,622 #binding_site copper 2 (Cys, Trp, Cys, His) #status !8predicted SUMMARY #length 634 #molecular-weight 70695 #checksum 5419 SEQUENCE /// ENTRY S39409 #type complete TITLE nitrous-oxide reductase (EC 1.7.99.6) precursor - Paracoccus denitrificans ORGANISM #formal_name Paracoccus denitrificans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S39409 REFERENCE S39409 !$#authors Hoeren, F.U.; Berks, B.C.; Ferguson, S.J.; McCarthy, J.E.G. !$#journal Eur. J. Biochem. (1993) 218:49-57 !$#title Sequence and expression of the gene encoding the respiratory !1nitrous-oxide reductase from Paracoccus denitrificans. New !1and conserved structural and regulatory motifs. !$#cross-references MUID:94062841; PMID:8243476 !$#accession S39409 !'##status preliminary !'##molecule_type DNA !'##residues 1-652 ##label HOE !'##cross-references EMBL:X74792; NID:g398932; PIDN:CAA52798.1; !1PID:g398933 CLASSIFICATION #superfamily nitrous-oxide reductase KEYWORDS copper; metalloprotein; oxidoreductase FEATURE !$1-57 #domain signal sequence #status predicted #label SIG\ !$58-652 #product nitrous-oxide reductase #status predicted !8#label MAT\ !$595,630,634 #binding_site copper 1 (His, Cys, Cys) #status !8predicted\ !$630,632,634,638 #binding_site copper 2 (Cys, Trp, Cys, His) #status !8predicted SUMMARY #length 652 #molecular-weight 71413 #checksum 486 SEQUENCE /// ENTRY S24382 #type complete TITLE nitrous-oxide reductase (EC 1.7.99.6) - Alcaligenes eutrophus ORGANISM #formal_name Alcaligenes eutrophus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S24382 REFERENCE S24382 !$#authors Zumft, W.G.; Dreusch, A.; Loechelt, S.; Cuypers, H.; !1Friedrich, B.; Schneider, B. !$#journal Eur. J. Biochem. (1992) 208:31-40 !$#title Derived amino acid sequences of the nosZ gene (respiratory N !1(2)O reductase) from Alcaligenes eutrophus, Pseudomonas !1aeruginosa and Pseudomonas stutzeri reveal potential !1copper-binding residues. Implications for the Cu(A) site of !1N(2)O reductase and cytochrome-c oxidase. !$#cross-references MUID:92380183; PMID:1324835 !$#accession S24382 !'##molecule_type DNA !'##residues 1-643 ##label ZUM !'##cross-references EMBL:X65278; NID:g38781; PIDN:CAA46383.1; !1PID:g38782 CLASSIFICATION #superfamily nitrous-oxide reductase KEYWORDS copper; metalloprotein; oxidoreductase FEATURE !$589,624,628 #binding_site copper 1 (His, Cys, Cys) #status !8predicted\ !$624,626,628,632 #binding_site copper 2 (Cys, His, Cys, His) #status !8predicted SUMMARY #length 643 #molecular-weight 70084 #checksum 4448 SEQUENCE /// ENTRY T46965 #type complete TITLE sulfite dehydrogenase (EC 1.8.2.1) precursor [validated] - Paracoccus denitrificans ORGANISM #formal_name Paracoccus denitrificans DATE 17-Mar-2000 #sequence_revision 17-Mar-2000 #text_change 22-Oct-2001 ACCESSIONS T46965 REFERENCE Z24324 !$#authors Wodara, C.; Bardischewsky, F.; Friedrich, C.G. !$#journal J. Bacteriol. (1997) 179:5014-5023 !$#title Cloning and characterization of sulfite dehydrogenase, two !1c-type cytochromes, and a flavoprotein of Paracoccus !1denitrificans GB17: Essential role of of sulfite !1dehydrogenase in lithotrophic sulfur oxidation. !$#cross-references MUID:97405897; PMID:9260941 !$#accession T46965 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-430 ##label WOD !'##cross-references EMBL:X79242; NID:g2253074; PIDN:CAA55829.1; !1PID:g1550793 !'##experimental_source strain GB17 GENETICS !$#gene soxC FUNCTION !$#description EC 1.8.2.1 [validated, MUID:97405897] !$#note essential for growth with thiosulfate; may have molybdenum !1cofactor, as molybdenum is also required CLASSIFICATION #superfamily Paracoccus denitrificans sulfite dehydrogenase; !1molybdopterin-binding domain homology KEYWORDS molybdenum; oxidoreductase FEATURE !$1-40 #domain signal sequence #status predicted #label SIG\ !$41-430 #product sulfite dehydrogenase #status predicted !8#label MAT\ !$78-410 #domain molybdopterin-binding domain homology #status !8atypical #label PCO SUMMARY #length 430 #molecular-weight 47341 #checksum 7974 SEQUENCE /// ENTRY S55874 #type complete TITLE sulfite oxidase (EC 1.8.3.1) precursor, mitochondrial [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Oct-1995 #sequence_revision 03-Nov-1995 #text_change 20-Apr-2000 ACCESSIONS S55874; S55875 REFERENCE S55874 !$#authors Garrett, R.M.; Bellissimo, D.B.; Rajagopalan, K.V. !$#submission submitted to the EMBL Data Library, July 1994 !$#description Molecular cloning of human sulfite oxidase. !$#accession S55874 !'##molecule_type mRNA !'##residues 1-488 ##label GAR1 !'##cross-references EMBL:L31573; NID:g508501; PIDN:AAA74886.1; !1PID:g508502 !'##experimental_source liver REFERENCE S55875 !$#authors Garrett, R.M.; Bellissimo, D.B.; Rajagopalan, K.V. !$#journal Biochim. Biophys. Acta (1995) 1262:147-149 !$#title Molecular cloning of human liver sulfite oxidase. !$#cross-references MUID:95322455; PMID:7599189 !$#accession S55875 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 101-356 ##label GAR2 !'##cross-references EMBL:L31573; NID:g508501 !'##experimental_source liver GENETICS !$#gene GDB:SUOX !'##cross-references GDB:5584405; OMIM:272300 COMPLEX homodimer FUNCTION !$#description EC 1.8.3.1 [validated, MUID:95322455]; sulfite oxidase; !1catalyzes the oxidation of sulfite and water to sulfate and !1hydrogen peroxide by dioxygen CLASSIFICATION #superfamily sulfite oxidase; cytochrome b5 core homology; !1molybdopterin-binding domain homology KEYWORDS chromoprotein; heme; homodimer; iron; metalloprotein; !1mitochondrion; molybdenum; molybdopterin; oxidoreductase; !1phosphoprotein FEATURE !$1-22 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$25-103 #domain cytochrome b5 core homology #label CB5\ !$107-481 #domain molybdopterin-binding domain homology #label !8PCO\ !$61,86 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$207 #binding_site molybdopterin (Cys) (covalent) #status !8predicted SUMMARY #length 488 #molecular-weight 53884 #checksum 5429 SEQUENCE /// ENTRY A53107 #type complete TITLE sulfite oxidase (EC 1.8.3.1) precursor, mitochondrial [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 02-Jun-1995 #sequence_revision 02-Jun-1995 #text_change 05-May-2000 ACCESSIONS A53107; A38328 REFERENCE A53107 !$#authors Garrett, R.M.; Rajagopalan, K.V. !$#journal J. Biol. Chem. (1994) 269:272-276 !$#title Molecular cloning of rat liver sulfite oxidase. Expression !1of a eukaryotic Mo-pterin-containing enzyme in Escherichia !1coli. !$#cross-references MUID:94103222; PMID:8276806 !$#accession A53107 !'##status preliminary !'##molecule_type mRNA !'##residues 1-488 ##label GAR !'##cross-references GB:L05084; NID:g294638; PIDN:AAA16618.1; !1PID:g294639 REFERENCE A38328 !$#authors Barber, M.J.; Neame, P.J. !$#journal J. Biol. Chem. (1990) 265:20912-20915 !$#title A conserved cysteine in molybdenum oxotransferases. !$#cross-references MUID:91065892; PMID:2249998 !$#accession A38328 !'##status preliminary !'##molecule_type protein !'##residues 41-119,'T',121-195;199-217;223-235,'R',237-259,'Q',261-270, !1272-279,'G',281-303,'S',305-319;323-335,'HYL', !1339-342;345-371,'X',373,'V',375;428-437;446-455,'A',457-468, !1'A',470-479 ##label BAR !'##experimental_source hepatic COMPLEX homodimer FUNCTION !$#description EC 1.8.3.1 [validated, MUID: 94103222]; sulfite oxidase; !1catalyzes the oxidation of sulfite and water to sulfate and !1hydrogen peroxide by dioxygen CLASSIFICATION #superfamily sulfite oxidase; cytochrome b5 core homology; !1molybdopterin-binding domain homology KEYWORDS heme; homodimer; iron; metalloprotein; mitochondrion; !1molybdenum; molybdopterin; oxidoreductase; phosphoprotein FEATURE !$1-22 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$25-103 #domain cytochrome b5 core homology #label CB5\ !$107-481 #domain molybdopterin-binding domain homology #label !8PCO\ !$61,86 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$207 #binding_site molybdopterin (Cys) (covalent) #status !8predicted SUMMARY #length 488 #molecular-weight 54354 #checksum 3323 SEQUENCE /// ENTRY A34180 #type complete TITLE sulfite oxidase (EC 1.8.3.1), hepatic - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 07-Jun-1990 #sequence_revision 07-Jun-1990 #text_change 16-Jul-1999 ACCESSIONS A34180; S10446; S07219 REFERENCE A34180 !$#authors Neame, P.J.; Barber, M.J. !$#journal J. Biol. Chem. (1989) 264:20894-20901 !$#title Conserved domains in molybdenum hydroxylases. The amino acid !1sequence of chicken hepatic sulfite oxidase. !$#cross-references MUID:90078175; PMID:2687265 !$#accession A34180 !'##molecule_type protein !'##residues 1-460 ##label NEA REFERENCE S10446 !$#authors Binder, C.M.; Irminger, J.C.; Jaussi, R. !$#submission submitted to the EMBL Data Library, March 1990 !$#accession S10446 !'##molecule_type mRNA !'##residues 16-96 ##label BIN !'##cross-references EMBL:X52559; NID:g62987; PIDN:CAA36793.1; !1PID:g860935 REFERENCE S07219 !$#authors Guiard, B.; Lederer, F. !$#journal Eur. J. Biochem. (1979) 100:441-453 !$#title Amino acid sequence of the 'b5-like' heme-binding domain !1from chicken sulfite oxidase. !$#cross-references MUID:80068877; PMID:510290 !$#accession S07219 !'##molecule_type protein !'##residues 1-97 ##label GUI REFERENCE A58730 !$#authors Kisker, C.; Schindelin, H.; Pacheco, A.; Wehbi, W.A.; !1Garrett, R.M.; Rajagopalan, K.V.; Enemark, J.H.; Rees, D.C. !$#journal Cell (1997) 91:973-983 !$#title Molecular basis of sulfite oxidase deficiency from the !1structure of sulfite oxidase. !$#cross-references MUID:98088796; PMID:9428520 !$#contents annotation; X-ray crystallography, 1.9 angstroms FUNCTION !$#description catalyzes the oxidation of sulfite and water to sulfate and !1hydrogen peroxide by dioxygen CLASSIFICATION #superfamily sulfite oxidase; cytochrome b5 core homology; !1molybdopterin-binding domain homology KEYWORDS chromoprotein; heme; homodimer; iron; liver; metalloprotein; !1mitochondrion; molybdenum; molybdopterin; oxidoreductase; !1phosphoprotein FEATURE !$4-82 #domain cytochrome b5 core homology #label CB5\ !$85-460 #domain molybdopterin-binding domain homology #label !8PCO\ !$40,65 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$186 #binding_site molybdopterin (Cys) (covalent) #status !8experimental SUMMARY #length 460 #molecular-weight 50360 #checksum 3503 SEQUENCE /// ENTRY F64864 #type complete TITLE protein-disulfide oxidoreductase (EC 1.8.4.-) dsbB [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES disulfide bond formation protein B ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS F64864; A48288; JC1109 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64864 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-176 ##label BLAT !'##cross-references GB:AE000216; GB:U00096; NID:g1787417; !1PIDN:AAC74269.1; PID:g1787433; UWGP:b1185 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A48288 !$#authors Missiakas, D.; Georgopoulos, C.; Raina, S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:7084-7088 !$#title Identification and characterization of the Escherichia coli !1gene dsbB, whose product is involved in the formation of !1disulfide bonds in vivo. !$#cross-references MUID:93348217; PMID:7688471 !$#accession A48288 !'##status preliminary !'##molecule_type DNA !'##residues 'MI',1-176 ##label MIS !'##cross-references GB:L03721; NID:g398017; PIDN:AAA23711.1; !1PID:g398018 REFERENCE JC1108 !$#authors Pinner, E.; Padan, E.; Schuldiner, S. !$#journal J. Biol. Chem. (1992) 267:11064-11068 !$#title Cloning, sequencing, and expression of the nhaB gene, !1encoding a Na+/H+ antiporter in Escherichia coli. !$#cross-references MUID:92283803; PMID:1317851 !$#accession JC1109 !'##status translation not shown !'##molecule_type DNA !'##residues 'MI',1-129,'LRRASVGFFRSGNAAVAARYFYRLPDCRSAGG',136-137,'PAV' !1##label PIN !'##cross-references GB:M83655 !'##experimental_source strain K-12, substrain W1333 GENETICS !$#gene dsbB; roxB !$#map_position 25.5 min FUNCTION !$#description reoxidizes dsbA protein specifically !$#note reaction depends on the presence of oxygen CLASSIFICATION #superfamily protein-disulfide oxidoreductase dsbB KEYWORDS oxidoreductase; redox-active disulfide; transmembrane !1protein FEATURE !$16-32 #domain transmembrane #status predicted #label TM1\ !$49-65 #domain transmembrane #status predicted #label TM2\ !$146-162 #domain transmembrane #status predicted #label TM3\ !$41-44 #disulfide_bonds redox-active #status predicted SUMMARY #length 176 #molecular-weight 20142 #checksum 9116 SEQUENCE /// ENTRY C64067 #type complete TITLE probable protein-disulfide oxidoreductase (EC 1.8.4.-) - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C64067 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession C64067 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-177 ##label TIGR !'##cross-references GB:U32726; GB:L42023; NID:g1573399; !1PIDN:AAC22087.1; PID:g1573403; TIGR:HI0428 CLASSIFICATION #superfamily protein-disulfide oxidoreductase dsbB KEYWORDS oxidoreductase; redox-active disulfide; transmembrane !1protein FEATURE !$41-57 #domain transmembrane #status predicted #label TM2\ !$67-83 #domain transmembrane #status predicted #label TM3\ !$147-163 #domain transmembrane #status predicted #label TM4\ !$41-44 #disulfide_bonds redox-active #status predicted SUMMARY #length 177 #molecular-weight 20442 #checksum 1735 SEQUENCE /// ENTRY JQ0144 #type complete TITLE probable protein-disulfide oxidoreductase (EC 1.8.4.-) - Pseudomonas aeruginosa ORGANISM #formal_name Pseudomonas aeruginosa DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JQ0144 REFERENCE JQ0132 !$#authors Kato, J.; Chu, L.; Kitano, K.; DeVault, J.D.; Kimbara, K.; !1Chakrabarty, A.M.; Misra, T.K. !$#journal Gene (1989) 84:31-38 !$#title Nucleotide sequence of a regulatory region controlling !1alginate synthesis in Pseudomonas aeruginosa: !1characterization of the algR2 gene. !$#cross-references MUID:90108714; PMID:2514124 !$#accession JQ0144 !'##status translation not shown !'##molecule_type DNA !'##residues 1-163 ##label KAT CLASSIFICATION #superfamily protein-disulfide oxidoreductase dsbB KEYWORDS oxidoreductase; redox-active disulfide; transmembrane !1protein FEATURE !$9-25 #domain transmembrane #status predicted #label TM1\ !$38-54 #domain transmembrane #status predicted #label TM2\ !$68-84 #domain transmembrane #status predicted #label TM3\ !$144-160 #domain transmembrane #status predicted #label TM4\ !$36-39 #disulfide_bonds redox-active #status predicted SUMMARY #length 163 #molecular-weight 17794 #checksum 3791 SEQUENCE /// ENTRY T12787 #type complete TITLE probable protein-disulfide oxidoreductase (EC 1.8.4.-) [similarity] - Bacillus subtilis phage SPBc2 ORGANISM #formal_name Bacillus subtilis phage SPBc2 DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 16-Jun-2000 ACCESSIONS T12787; H69909 REFERENCE Z17583 !$#authors Lazarevic, V.; Duesterhoeft, A.; Soldo, B.; Hilbert, H.; !1Mauel, C.; Karamata, D. !$#submission submitted to the EMBL Data Library, August 1997 !$#description The complete nucleotide sequence of the Bacillus subtilis !1SPbetac2 prophage. !$#accession T12787 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-148 ##label LAZ !'##cross-references EMBL:AF020713; NID:g3025478; PID:g3025501; !1PIDN:AAC12996.1 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69909 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-148 ##label KUN !'##cross-references GB:Z99115; GB:AL009126; NID:g2634478; !1PIDN:CAB14062.1; PID:g2634564 !'##experimental_source strain 168 GENETICS !$#gene yolK CLASSIFICATION #superfamily protein-disulfide oxidoreductase dsbB KEYWORDS oxidoreductase; redox-active disulfide; transmembrane !1protein FEATURE !$9-25 #domain transmembrane #status predicted #label TM1\ !$44-60 #domain transmembrane #status predicted #label TM2\ !$64-80 #domain transmembrane #status predicted #label TM3\ !$119-135 #domain transmembrane #status predicted #label TM4\ !$36-39 #disulfide_bonds redox-active #status predicted SUMMARY #length 148 #molecular-weight 17139 #checksum 8402 SEQUENCE /// ENTRY B70041 #type complete TITLE probable protein-disulfide oxidoreductase (EC 1.8.4.-) yvgU - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS B70041 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B70041 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-138 ##label KUN !'##cross-references GB:Z99121; GB:AL009126; NID:g2635827; !1PIDN:CAB15352.1; PID:g2635860 !'##experimental_source strain 168 GENETICS !$#gene yvgU CLASSIFICATION #superfamily protein-disulfide oxidoreductase dsbB KEYWORDS oxidoreductase; redox-active disulfide; transmembrane !1protein FEATURE !$5-21 #domain transmembrane #status predicted #label TM1\ !$42-58 #domain transmembrane #status predicted #label TM2\ !$66-82 #domain transmembrane #status predicted #label TM3\ !$116-132 #domain transmembrane #status predicted #label TM4\ !$34-37 #disulfide_bonds redox-active #status predicted SUMMARY #length 138 #molecular-weight 15714 #checksum 5350 SEQUENCE /// ENTRY G71547 #type complete TITLE probable protein-disulfide oxidoreductase (EC 1.8.4.-) - Chlamydia trachomatis (serotype D, strain UW3/Cx) ORGANISM #formal_name Chlamydia trachomatis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS G71547 REFERENCE A71570 !$#authors Stephens, R.S.; Kalman, S.; Lammel, C.J.; Fan, J.; Marathe, !1R.; Aravind, L.; Mitchell, W.P.; Olinger, L.; Tatusov, R.L.; !1Zhao, Q.; Koonin, E.V.; Davis, R.W. !$#journal Science (1998) 282:754-759 !$#title Genome sequence of an obligate intracellular pathogen of !1humans: Chlamydia trachomatis. !$#cross-references MUID:99000809; PMID:9784136 !$#accession G71547 !'##status preliminary !'##molecule_type DNA !'##residues 1-135 ##label ARN !'##cross-references GB:AE001291; GB:AE001273; NID:g3328573; !1PIDN:AAC67767.1; PID:g3328580 !'##experimental_source serotype D, strain UW-3/Cx GENETICS !$#gene dsbB CLASSIFICATION #superfamily protein-disulfide oxidoreductase dsbB KEYWORDS oxidoreductase; redox-active disulfide; transmembrane !1protein FEATURE !$9-25 #domain transmembrane #status predicted #label TM1\ !$37-53 #domain transmembrane #status predicted #label TM2\ !$69-85 #domain transmembrane #status predicted #label TM3\ !$115-131 #domain transmembrane #status predicted #label TM4\ !$36-39 #disulfide_bonds redox-active #status predicted SUMMARY #length 135 #molecular-weight 15005 #checksum 9558 SEQUENCE /// ENTRY RDYCS7 #type complete TITLE sulfite reductase (ferredoxin) (EC 1.8.7.1) - Synechococcus sp. ORGANISM #formal_name Synechococcus sp. DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 11-Jun-1999 ACCESSIONS S19860; I39640 REFERENCE S19860 !$#authors Gisselmann, G.; Schwenn, J.D. !$#submission submitted to the EMBL Data Library, February 1992 !$#description Identification and characterization of the gene encoding !1ferredoxin:sulfite reductase from the cyanobacterium !1Synechococcus PCC 7942. !$#accession S19860 !'##molecule_type DNA !'##residues 1-624 ##label GIS !'##cross-references EMBL:Z11755; NID:g38929; PIDN:CAA77809.1; !1PID:g38930 !'##experimental_source PCC 7942 !'##note the source is designated as Anacystis nidulans (PCC 7942) REFERENCE I39639 !$#authors Gisselmann, G.; Klausmeier, P.; Schwenn, J.D. !$#journal Biochim. Biophys. Acta (1993) 1144:102-106 !$#title The ferredoxin:sulphite reductase gene from Synechococcus !1PCC7942. !$#cross-references MUID:93349955; PMID:8347657 !$#accession I39640 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-624 ##label RES !'##cross-references EMBL:Z11755; NID:g38929; PIDN:CAA77809.1; !1PID:g38930 !'##experimental_source PCC 6301 GENETICS !$#gene sir CLASSIFICATION #superfamily sulfite reductase (ferredoxin) KEYWORDS 4Fe-4S; chromoprotein; heme; iron; iron-sulfur protein; !1metalloprotein; oxidoreductase FEATURE !$446,452,491,495 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$495 #binding_site siroheme iron (Cys) (axial ligand) !8#status predicted SUMMARY #length 624 #molecular-weight 70031 #checksum 2403 SEQUENCE /// ENTRY RDECSH #type complete TITLE sulfite reductase (NADPH2) (EC 1.8.1.2) hemoprotein - Escherichia coli (strain K-12) ALTERNATE_NAMES sulfite reductase (NADPH) alpha chain ORGANISM #formal_name Escherichia coli DATE 31-Dec-1993 #sequence_revision 17-Oct-1997 #text_change 03-Jun-2002 ACCESSIONS G65057; B34354; S14220 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65057 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-570 ##label BLAT !'##cross-references GB:AE000360; GB:U00096; NID:g2367157; !1PIDN:AAC75805.1; PID:g1789122; UWGP:b2763 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A34354 !$#authors Ostrowski, J.; Wu, J.Y.; Rueger, D.C.; Miller, B.E.; Siegel, !1L.M.; Kredich, N.M. !$#journal J. Biol. Chem. (1989) 264:15726-15737 !$#title Characterization of the cysJIH regions of Salmonella !1typhimurium and Escherichia coli B. DNA sequences of cysI !1and cysH and a model for the siroheme-Fe-4S-4 active center !1of sulfite reductase hemoprotein based on amino acid !1homology with spinach nitrite reductase. !$#cross-references MUID:89359425; PMID:2670946 !$#accession B34354 !'##molecule_type DNA !'##residues 1-22,'L',24-570 ##label OST !'##cross-references GB:J05057 !'##note the authors translated the codon AAC for residue 355 as Gln !'##note parts of this sequence, including the amino end of the mature !1protein, were confirmed by protein sequencing REFERENCE S14220 !$#authors Krone, F.A.; Westphal, G.; Schwenn, J.D. !$#journal Mol. Gen. Genet. (1991) 225:314-319 !$#title Characterization of the gene cysH and of its product !1phospho-adenylylsulphate reductase from Escherichia coli. !$#cross-references MUID:91172132; PMID:2005873 !$#accession S14220 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 'RPV',344-570 ##label KRO !'##cross-references EMBL:Y07525; NID:g41197; PIDN:CAA68816.1; !1PID:g809673 !'##note this sequence was submitted to the EMBL Data Library, April !11990 GENETICS !$#gene cysI; cysQ !$#map_position 59 min CLASSIFICATION #superfamily sulfite reductase (ferredoxin) KEYWORDS 4Fe-4S; chromoprotein; cysteine biosynthesis; heme; iron; !1iron-sulfur protein; metalloprotein; NADP; oxidoreductase FEATURE !$2-570 #product sulfite reductase (NADPH) hemoprotein !8#status experimental #label MAT\ !$434,440,479,483 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$483 #binding_site siroheme iron (Cys) (axial ligand) !8#status predicted SUMMARY #length 570 #molecular-weight 63998 #checksum 9740 SEQUENCE /// ENTRY A34354 #type complete TITLE sulfite reductase (NADPH2) (EC 1.8.1.2) hemoprotein - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS A34354 REFERENCE A34354 !$#authors Ostrowski, J.; Wu, J.Y.; Rueger, D.C.; Miller, B.E.; Siegel, !1L.M.; Kredich, N.M. !$#journal J. Biol. Chem. (1989) 264:15726-15737 !$#title Characterization of the cysJIH regions of Salmonella !1typhimurium and Escherichia coli B. DNA sequences of cysI !1and cysH and a model for the siroheme-Fe-4S-4 active center !1of sulfite reductase hemoprotein based on amino acid !1homology with spinach nitrite reductase. !$#cross-references MUID:89359425; PMID:2670946 !$#accession A34354 !'##status preliminary !'##molecule_type DNA !'##residues 1-570 ##label OST !'##cross-references GB:M23007; GB:J05009; GB:J05025; GB:M27145 CLASSIFICATION #superfamily sulfite reductase (ferredoxin) KEYWORDS 4Fe-4S; chromoprotein; cysteine biosynthesis; heme; iron; !1iron-sulfur protein; metalloprotein; NADP; oxidoreductase FEATURE !$434,440,479,483 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$483 #binding_site siroheme iron (Cys) (axial ligand) !8#status predicted SUMMARY #length 570 #molecular-weight 64023 #checksum 9303 SEQUENCE /// ENTRY S34191 #type complete TITLE sulfite reductase (NADPH2) (EC 1.8.1.2) hemoprotein - Thiocapsa roseopersicina ORGANISM #formal_name Thiocapsa roseopersicina DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S34191 REFERENCE S34190 !$#authors Haverkamp, T.; Gisselmann, G.; Schwenn, J.D. !$#submission submitted to the EMBL Data Library, July 1993 !$#description Structure and function of genes involved in the metabolism !1of sulfite from the sulfur oxidizing purple bacterium !1Thiocapsa roseopersicina. !$#accession S34191 !'##molecule_type DNA !'##residues 1-561 ##label HAV !'##cross-references EMBL:Z23169 CLASSIFICATION #superfamily sulfite reductase (ferredoxin) KEYWORDS 4Fe-4S; chromoprotein; cysteine biosynthesis; heme; iron; !1iron-sulfur protein; metalloprotein; NADP; oxidoreductase FEATURE !$423,429,468,472 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$472 #binding_site siroheme iron (Cys) (axial ligand) !8#status predicted SUMMARY #length 561 #molecular-weight 62455 #checksum 1247 SEQUENCE /// ENTRY RDSPTB #type complete TITLE ferredoxin-thioredoxin reductase (EC 1.18.-.-) chain B precursor - spinach ALTERNATE_NAMES ferredoxin-thioredoxin reductase catalytic chain; FTR-B ORGANISM #formal_name Spinacia oleracea #common_name spinach DATE 24-Aug-1996 #sequence_revision 04-Oct-1996 #text_change 16-Jun-2000 ACCESSIONS S65943; S41162; JT0772; S17460; S65942; S44048 REFERENCE S65943 !$#authors Chow, L.P.; Iwadate, H.; Yano, K.; Kamo, M.; Tsugita, A.; !1Gardet-Salvi, L.; Stritt-Etter, A.L.; Schuermann, P. !$#submission submitted to the EMBL Data Library, November 1995 !$#description Amino acid sequence of spinach ferredoxin: thioredoxin !1reductase catalytic subunit and identification of thiol !1groups constituting a redox-active disulfide and a [4Fe-4S] !1cluster. !$#accession S65943 !'##molecule_type mRNA !'##residues 1-144 ##label CHO !'##cross-references EMBL:X74881; NID:g1103725; PIDN:CAA52867.1; !1PID:g1103726 REFERENCE S41162 !$#authors Gaymard, E.; Spielmann, A.; Stutz, E.; Schuermann, P. !$#submission submitted to the EMBL Data Library, September 1993 !$#description Nucleotide sequence of a cDNA encoding the entire precursor !1polypeptide of the catalytic subunit of !1ferredoxin-thioredoxin reductase from spinach cloroplasts. !$#accession S41162 !'##status preliminary !'##molecule_type mRNA !'##residues 1-25,27-144 ##label GAY !'##cross-references EMBL:X74881 REFERENCE JT0772 !$#authors Chow, L.P.; Iwadate, H.; Yano, K.; Kamo, M.; Salvi, L.G.; !1Schuermann, P.; Tsugita, A. !$#submission submitted to JIPID, June 1994 !$#description Amino acid sequence of spinach ferredoxin thioredoxin !1reductase catalytic subunit and identification of thiol !1groups constituting a redox active site and Fe-S cluster. !$#accession JT0772 !'##molecule_type protein !'##residues 32-144 ##label CH2 REFERENCE S16921 !$#authors Tsugita, A.; Yano, K.; Gardet-Salvi, L.; Schuermann, P. !$#journal Protein Seq. Data Anal. (1991) 4:9-13 !$#title Characterization of spinach ferredoxin-thioredoxin !1reductase. !$#cross-references MUID:92020817; PMID:1924273 !$#accession S17460 !'##molecule_type protein !'##residues 32-53;139-144 ##label TSU REFERENCE A58085 !$#authors Staples, C.R.; Ameyibor, E.; Fu, W.; Gardet-Salvi, L.; !1Stritt-Etter, A.L.; Schuermann, P.; Knaff, D.B.; Johnson, !1M.K. !$#journal Biochemistry (1996) 35:11425-11434 !$#title The function and properties of the iron-sulfur center in !1spinach ferredoxin:thioredoxin reductase: a new biological !1role for iron-sulfur clusters. !$#cross-references MUID:96378635; PMID:8784198 !$#contents annotation; investigation of active site mechanism REFERENCE S65942 !$#authors Chow, L.P.; Iwadate, H.; Yano, K.; Kamo, M.; Tsugita, A.; !1Gardet-Salvi, L.; Stritt-Etter, A.L.; Schuermann, P. !$#journal Eur. J. Biochem. (1995) 231:149-156 !$#title Amino acid sequence of spinach ferredoxin:thioredoxin !1reductase catalytic subunit and identification of thiol !1groups constituting a redox-active disulfide and a [4Fe-4S] !1cluster. !$#cross-references MUID:95354683; PMID:7628465 !$#accession S65942 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 32-144 ##label CHA !'##cross-references EMBL:X74881 COMMENT The B chain binds a 4Fe-4S cluster and has the redox-active !1disulfide. After the first step of reduction, it is !1predicted that Cys-85 becomes a ligand of the iron-sulfur !1cluster, and Cys-115 forms a disulfide bond with !1thioredoxin. GENETICS !$#gene ftrB FUNCTION !$#description catalyzes the reversible oxidation of ferredoxin by !1thioredoxin !$#pathway photosynthesis CLASSIFICATION #superfamily ferredoxin-thioredoxin reductase chain B KEYWORDS 4Fe-4S; chloroplast; heterodimer; iron-sulfur protein; !1metalloprotein; oxidoreductase; phosphoprotein; !1photosynthesis; redox-active disulfide FEATURE !$1-31 #domain transit peptide (chloroplast) #status !8predicted #label TRP\ !$32-144 #product ferredoxin-thioredoxin reductase chain B !8#status experimental #label MAT\ !$83,102,104,113 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8experimental\ !$85-115 #disulfide_bonds redox-active #status experimental SUMMARY #length 144 #molecular-weight 16349 #checksum 5151 SEQUENCE /// ENTRY RDSPTA #type complete TITLE ferredoxin-thioredoxin reductase (EC 1.18.-.-) chain A precursor - spinach ALTERNATE_NAMES ferredoxin-thioredoxin reductase variable chain; FTR-A ORGANISM #formal_name Spinacia oleracea #common_name spinach DATE 13-Jan-1995 #sequence_revision 04-Oct-1996 #text_change 11-Jun-1999 ACCESSIONS S44200; S45672; JT0771; S16921; JT0661 REFERENCE S44200 !$#authors Schuermann, P. !$#submission submitted to the EMBL Data Library, April 1994 !$#accession S44200 !'##status preliminary !'##molecule_type mRNA !'##residues 1-174 ##label SCH !'##cross-references EMBL:X78880; NID:g1405818; PIDN:CAA55480.1; !1PID:g474766 REFERENCE S45672 !$#authors Iwadate, H.; Yano, K.; Kamo, M.; Gardet-Salvi, L.; !1Schuermann, P.; Tsugita, A. !$#journal Eur. J. Biochem. (1994) 223:465-471 !$#title Amino acid sequence of spinach ferredoxin: thioredoxin !1reductase variable subunit. !$#cross-references MUID:94333335; PMID:8055915 !$#accession S45672 !'##molecule_type protein !'##residues 63-174 ##label IWA REFERENCE JT0771 !$#authors Iwadate, H.; Yano, K.; Kamo, M.; Gardet-Salvi, L.; !1Schuermann, P.; Tsugita, A. !$#submission submitted to JIPID, April 1994 !$#description Amino acid sequence of spinach ferredoxin: thioredoxin !1reductase variable subunit. !$#accession JT0771 !'##molecule_type protein !'##residues 63-99,'F',101-174 ##label IW2 REFERENCE S16921 !$#authors Tsugita, A.; Yano, K.; Gardet-Salvi, L.; Schuermann, P. !$#journal Protein Seq. Data Anal. (1991) 4:9-13 !$#title Characterization of spinach ferredoxin-thioredoxin !1reductase. !$#cross-references MUID:92020817; PMID:1924273 !$#accession S16921 !'##molecule_type protein !'##residues 63-78,'D',80,'SEPPPVVKSPPP';'ESGK' ##label TSU COMMENT The A chain does not bind the iron-sulfur cluster and does !1not appear to be catalytically competent. GENETICS !$#gene ftrA FUNCTION !$#description catalyzes the reversible oxidation of ferredoxin by !1thioredoxin !$#pathway photosynthesis CLASSIFICATION #superfamily ferredoxin-thioredoxin reductase chain A KEYWORDS chloroplast; heterodimer; oxidoreductase; phosphoprotein; !1photosynthesis FEATURE !$1-62 #domain transit peptide (chloroplast) #status !8predicted #label TRP\ !$63-174 #product ferredoxin-thioredoxin reductase A #status !8experimental #label FE1\ !$68-174 #product ferredoxin-thioredoxin reductase A' #status !8experimental #label FE2\ !$78-174 #product ferredoxin-thioredoxin reductase A'' #status !8experimental #label FE3\ !$70,71 #binding_site phosphate (Ser) (covalent) #status !8experimental SUMMARY #length 174 #molecular-weight 19075 #checksum 3988 SEQUENCE /// ENTRY E28544 #type complete TITLE methyl coenzyme M reductase (EC 1.8.-.-) I alpha chain - Methanobacterium thermoautotrophicum (strain Marburg) ORGANISM #formal_name Methanobacterium thermoautotrophicum #variety strain Marburg DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 15-Oct-1999 ACCESSIONS E28544; S78576 REFERENCE A91891 !$#authors Bokranz, M.; Baeumner, G.; Allmansberger, R.; Ankel-Fuchs, !1D.; Klein, A. !$#journal J. Bacteriol. (1988) 170:568-577 !$#title Cloning and characterization of the methyl coenzyme M !1reductase genes from Methanobacterium thermoautotrophicum. !$#cross-references MUID:88115150; PMID:2448287 !$#accession E28544 !'##molecule_type DNA !'##residues 1-550 ##label BOK !'##cross-references GB:X07794; GB:M18969; NID:g44607; PIDN:CAA30639.1; !1PID:g44612 !'##experimental_source strain Marburg REFERENCE S13864 !$#authors Rospert, S.; Linder, D.; Ellermann, J.; Thauer, R.K. !$#journal Eur. J. Biochem. (1990) 194:871-877 !$#title Two genetically distinct methyl-coenzyme M reductases in !1Methanobacterium thermoautotrophicum strain Marburg and !1Delta-H. !$#cross-references MUID:91099370; PMID:2269306 !$#accession S78576 !'##molecule_type protein !'##residues 2-19 ##label ROS !'##experimental_source strain Marburg REFERENCE A58866 !$#authors Ermler, U.; Grabarse, W.; Shima, S.; Goubeaud, M.; Thauer, !1R.K. !$#journal Science (1997) 278:1457-1462 !$#title Crystal structure of methyl-coenzyme M reductase: the key !1enzyme of biological methane formation. !$#cross-references MUID:98035783; PMID:9367957 !$#contents annotation; X-ray crystallography, 1.45 angstroms !$#note the modified residue designated as N1-methylhistidine is !1correctly named 3'-methylhistidine; the modified residue !1designated as delta- or 4-methylarginine is correctly named !15-methylarginine COMPLEX heterohexamer of two alpha, two beta (see PIR:A28544) and !1two gamma (see PIR:D28544) chains FUNCTION !$#description catalyzes the reaction of methyl coenzyme M (2- !1(methylthio)enthanesulfonic acid) with coenzyme B (N- !1(7-thioheptanoyl)threonine-O3-phosphate) to form coenzyme !1M-coenzyme B heterodisulfide and methane !$#pathway methanogenesis CLASSIFICATION #superfamily methyl coenzyme M reductase alpha chain KEYWORDS heterohexamer; metalloprotein; methanogenesis; methylated !1amino acid; nickel; oxidoreductase FEATURE !$2-550 #product methyl coenzyme M reductase I alpha chain !8#status experimental #label MAT\ !$147 #binding_site coenzyme F430 nickel (Gln) (axial !8ligand) #status experimental\ !$257 #modified_site 3'-methylhistidine (His) #status !8experimental\ !$271 #modified_site 5-methylarginine (Arg) #status !8experimental\ !$333 #active_site Tyr #status predicted\ !$400 #modified_site 2-methylglutamine (Gln) #status !8experimental\ !$444 #binding_site coenzyme M (Tyr) #status experimental\ !$445 #modified_site 1-thioglycine (Gly) #status !8experimental\ !$452 #binding_site methyl (Cys) (covalent) #status !8experimental\ !$481 #binding_site coenzyme B (Asn) #status experimental SUMMARY #length 550 #molecular-weight 60510 #checksum 4352 SEQUENCE /// ENTRY G69017 #type complete TITLE methyl coenzyme M reductase (EC 1.8.-.-) II beta chain - Methanobacterium thermoautotrophicum (strains Delta H and Marburg) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS G69017; S13969; S13966; I30315 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession G69017 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 'MNT',1-443 ##label MTH !'##cross-references GB:AE000883; GB:AE000666; NID:g2622231; !1PIDN:AAB85621.1; PID:g2622236 !'##experimental_source strain Delta H !'##note an incorrect initiation codon was used REFERENCE S13864 !$#authors Rospert, S.; Linder, D.; Ellermann, J.; Thauer, R.K. !$#journal Eur. J. Biochem. (1990) 194:871-877 !$#title Two genetically distinct methyl-coenzyme M reductases in !1Methanobacterium thermoautotrophicum strain Marburg and !1Delta-H. !$#cross-references MUID:91099370; PMID:2269306 !$#accession S13969 !'##molecule_type protein !'##residues 2-20 ##label ROS !'##experimental_source strain Delta H !$#accession S13966 !'##molecule_type protein !'##residues 2-15 ##label ROW !'##experimental_source strain Marburg REFERENCE A30315 !$#authors Reeve, J.N.; Beckler, G.S.; Cram, D.S.; Hamilton, P.T.; !1Brown, J.W.; Krzycki, J.A.; Kolodziej, A.F.; Alex, L.; !1Orme-Johnson, W.H.; Walsh, C.T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:3031-3035 !$#title A hydrogenase-linked gene in Methanobacterium !1thermoautotrophicum strain delta-H encodes a polyferredoxin. !$#cross-references MUID:89240669; PMID:2654933 !$#accession I30315 !'##molecule_type DNA !'##residues 1-146 ##label REE !'##cross-references GB:J04540; NID:g149730; PIDN:AAB02353.1; !1PID:g1196494 !'##experimental_source strain Delta H !'##note the authors translated the codon ATG for residue 121 as Asn GENETICS !$#gene MTH1132 !$#start_codon GTG COMPLEX heterohexamer of two alpha (see PIR:C69017), two beta and !1two gamma (see PIR:E69017) chains FUNCTION !$#description catalyzes the reaction of methyl coenzyme M (2- !1(methylthio)enthanesulfonic acid) with coenzyme B (N- !1(7-thioheptanoyl)threonine-O3-phosphate) to form coenzyme !1M-coenzyme B heterodisulfide and methane !$#pathway methanogenesis CLASSIFICATION #superfamily methyl coenzyme M reductase beta chain KEYWORDS methanogenesis; oxidoreductase FEATURE !$2-443 #product methyl coenzyme M reductase II beta chain !8#status experimental #label MAT\ !$367 #active_site Tyr #status predicted SUMMARY #length 443 #molecular-weight 47133 #checksum 2799 SEQUENCE /// ENTRY D28544 #type complete TITLE methyl coenzyme M reductase (EC 1.8.-.-) I gamma chain - Methanobacterium thermoautotrophicum (strain Marburg) ORGANISM #formal_name Methanobacterium thermoautotrophicum #variety strain Marburg DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS D28544; S78578 REFERENCE A91891 !$#authors Bokranz, M.; Baeumner, G.; Allmansberger, R.; Ankel-Fuchs, !1D.; Klein, A. !$#journal J. Bacteriol. (1988) 170:568-577 !$#title Cloning and characterization of the methyl coenzyme M !1reductase genes from Methanobacterium thermoautotrophicum. !$#cross-references MUID:88115150; PMID:2448287 !$#accession D28544 !'##molecule_type DNA !'##residues 1-249 ##label BOK !'##cross-references GB:X07794; GB:M18969; NID:g44607; PIDN:CAA30638.1; !1PID:g44611 !'##experimental_source strain Marburg REFERENCE S13864 !$#authors Rospert, S.; Linder, D.; Ellermann, J.; Thauer, R.K. !$#journal Eur. J. Biochem. (1990) 194:871-877 !$#title Two genetically distinct methyl-coenzyme M reductases in !1Methanobacterium thermoautotrophicum strain Marburg and !1Delta-H. !$#cross-references MUID:91099370; PMID:2269306 !$#accession S78578 !'##molecule_type protein !'##residues 2-18,'X',20-21 ##label ROS !'##experimental_source strain Marburg REFERENCE A58866 !$#authors Ermler, U.; Grabarse, W.; Shima, S.; Goubeaud, M.; Thauer, !1R.K. !$#journal Science (1997) 278:1457-1462 !$#title Crystal structure of methyl-coenzyme M reductase: the key !1enzyme of biological methane formation. !$#cross-references MUID:98035783; PMID:9367957 !$#contents annotation; X-ray crystallography, 1.45 angstroms COMPLEX heterohexamer of two alpha (see PIR:E28544), two beta (see !1PIR:A28544) and two gamma chains FUNCTION !$#description catalyzes the reaction of methyl coenzyme M (2- !1(methylthio)enthanesulfonic acid) with coenzyme B (N- !1(7-thioheptanoyl)threonine-O3-phosphate) to form coenzyme !1M-coenzyme B heterodisulfide and methane !$#pathway methanogenesis CLASSIFICATION #superfamily methyl coenzyme M reductase gamma chain KEYWORDS heterohexamer; methanogenesis; oxidoreductase FEATURE !$2-249 #product methyl coenzyme M reductase I gamma chain !8#status experimental #label MAT\ !$120 #binding_site substrate (Arg) #status experimental SUMMARY #length 249 #molecular-weight 28758 #checksum 8754 SEQUENCE /// ENTRY ODHU1 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain I - human mitochondrion ALTERNATE_NAMES cytochrome a3; cytochrome aa3 ORGANISM #formal_name mitochondrion Homo sapiens #common_name man DATE 22-May-1981 #sequence_revision 23-Oct-1981 #text_change 31-Mar-2000 ACCESSIONS A00463; B38016 REFERENCE A00151 !$#authors Anderson, S.; Bankier, A.T.; Barrell, B.G.; de Bruijn, !1M.H.L.; Coulson, A.R.; Drouin, J.; Eperon, I.C.; Nierlich, !1D.P.; Roe, B.A.; Sanger, F.; Schreier, P.H.; Smith, A.J.H.; !1Staden, R.; Young, I.G. !$#journal Nature (1981) 290:457-465 !$#title Sequence and organization of the human mitochondrial genome. !$#cross-references MUID:81173052; PMID:7219534 !$#accession A00463 !'##molecule_type DNA !'##residues 1-513 ##label AND !'##cross-references GB:J01415; NID:g1944628; PIDN:AAB58945.1; !1PID:g506829; EMBL:V00662; NID:g13003; PID:g13006; !1GSPDB:GN00100 REFERENCE A38016 !$#authors Sanger, F.; Coulson, A.R.; Barrell, B.G.; Smith, A.J.H.; !1Roe, B.A. !$#journal J. Mol. Biol. (1980) 143:161-178 !$#title Cloning in single-stranded bacteriophage as an aid to rapid !1DNA sequencing. !$#cross-references MUID:81170577; PMID:6260957 !$#accession B38016 !'##molecule_type DNA !'##residues 1-185 ##label SAN !'##cross-references GB:M10546 GENETICS !$#gene GDB:MTCO1 !'##cross-references GDB:118900; OMIM:516030 !$#map_position MTH5904-7444 !$#genome mitochondrion !$#genetic_code SGC1 COMPLEX part of a 13 chain complex spanning the inner mitochondrial !1membrane and consisting of one each of chains I, II (see !1PIR:OBHU2), III (see PIR:OTHU3), IV (see PIR:OLHU4), Va (see !1PIR:OTHU5A), Vb (see PIR:OTHU5B), VIa (see PIR:OGHU6A), VIb !1(see PIR:OGHU6B), VIc (see PIR:OGHU6C), VIIa (see !1PIR:OSHU7A), VIIb (see PIR:OSHU7B), VIIc (see PIR:OSHU7C), !1VIII (see PIR:OSHU8); the complex may form dimers within the !1mitochondrial inner-membrane FUNCTION !$#description the cytochrome-c oxidase complex catalyzes the oxidation of !1four molecules of reduced cytochrome c in the intracristal !1(or intermembrane) space using one oxygen molecule and four !1protons from the mitochondrial matrix producing two !1molecules of water and lowering the concentration of protons !1in the mitochondrial matrix !$#pathway oxidative phosphorylation; respiratory chain !$#note chain I directly reduces oxygen on the mitochondrial matrix !1side of the inner-membrane; the oxygen is bound between the !1heme a3 iron atom and the copper atom, referred to as copper !1B CLASSIFICATION #superfamily cytochrome-c oxidase chain I; cytochrome-c !1oxidase chain I homology KEYWORDS chromoprotein; copper; electron transfer; heme; iron; !1magnesium; membrane-associated complex; metalloprotein; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$11-457 #domain cytochrome-c oxidase chain I homology #label !8CO1\ !$12-40 #domain transmembrane helix #status predicted #label !8TR01\ !$51-86 #domain transmembrane helix #status predicted #label !8TR02\ !$95-117 #domain transmembrane helix #status predicted #label !8TR03\ !$141-170 #domain transmembrane helix #status predicted #label !8TR04\ !$183-212 #domain transmembrane helix #status predicted #label !8TR05\ !$228-261 #domain transmembrane helix #status predicted #label !8TR06\ !$270-286 #domain transmembrane helix #status predicted #label !8TR07\ !$299-327 #domain transmembrane helix #status predicted #label !8TR08\ !$336-356 #domain transmembrane helix #status predicted #label !8TR09\ !$371-400 #domain transmembrane helix #status predicted #label !8TR10\ !$407-433 #domain transmembrane helix #status predicted #label !8TR11\ !$447-478 #domain transmembrane helix #status predicted #label !8TR12\ !$1 #modified_site N-formylmethionine #status predicted\ !$61,378 #binding_site heme a iron (His) (axial ligands) !8#status predicted\ !$240,290,291 #binding_site copper (His) #status predicted\ !$240-244 #cross-link 1'-histidyl-3'-tyrosine (His-Tyr) #status !8predicted\ !$244 #binding_site oxygen (Tyr) #status predicted\ !$368 #binding_site magnesium (His) (shared with chain II) !8#status predicted\ !$376 #binding_site heme a3 iron (His) (axial ligand) !8#status predicted SUMMARY #length 513 #molecular-weight 57041 #checksum 8809 SEQUENCE /// ENTRY ODBO1 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain I [validated] - bovine mitochondrion ALTERNATE_NAMES cytochrome a3; cytochrome aa3 ORGANISM #formal_name mitochondrion Bos primigenius taurus #common_name cattle DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 15-Sep-2000 ACCESSIONS A00464; S09684 REFERENCE A00152 !$#authors Anderson, S.; de Bruijn, M.H.L.; Coulson, A.R.; Eperon, !1I.C.; Sanger, F.; Young, I.G. !$#journal J. Mol. Biol. (1982) 156:683-717 !$#title Complete sequence of bovine mitochondrial DNA. Conserved !1features of the mammalian mitochondrial genome. !$#cross-references MUID:83010260; PMID:7120390 !$#accession A00464 !'##molecule_type DNA !'##residues 1-514 ##label AND !'##cross-references GB:J01394; NID:g336430; PIDN:AAB59270.1; !1PID:g336433; EMBL:V00654; NID:g12800; PID:g12803 REFERENCE S09684 !$#authors Hensel, S.; Buse, G. !$#journal Biol. Chem. Hoppe-Seyler (1990) 371:411-422 !$#title Studies on cytochrome-c oxidase, XIV[1]. The amino-acid !1sequence of subunit I - proteinchemical methods for the !1analysis of a large hydrophobic membrane protein. !$#cross-references MUID:90334744; PMID:2165784 !$#accession S09684 !'##molecule_type protein !'##residues 1-514 ##label HEN !'##experimental_source heart REFERENCE A67451 !$#authors Tsukihara, T.; Aoyama, H.; Yamashita, E.; Tomizaki, T.; !1Yamaguchi, H.; Shinzawa-itoh, K.; Nakashima, R.; Yaono, R.; !1Yoshikawa, S. !$#submission submitted to the Brookhaven Protein Data Bank, April 1996 !$#cross-references PDB:1OCC !$#contents annotation; X-ray crystallography, 2.8 angstroms, residues !11-514 REFERENCE A57981 !$#authors Tsukihara, T.; Aoyama, H.; Yamashita, E.; Tomizaki, T.; !1Yamaguchi, H.; Sinzawa-Itoh, K.; Nakashima, R.; Yaono, R.; !1Yoshikawa, S. !$#journal Science (1996) 272:1136-1144 !$#title The whole structure of the 13-subunit oxidized cytochrome c !1oxidase at 2.8 angstroms. !$#cross-references MUID:96216288; PMID:8638158 !$#contents annotation; X-ray crystallography, 2.8 angstroms REFERENCE A58960 !$#authors Buse, G.; Soulimane, T.; Dewor, M.; Meyer, H.E.; Blueggel, !1M. !$#journal Protein Sci. (1999) 8:985-990 !$#title Evidence for a copper-coordinated histidine-tyrosine !1cross-link in the active site of cytochrome oxidase. !$#cross-references MUID:99268331; PMID:10338009 !$#contents annotation !$#note mass spectrographic and chemical characterization of !1histidyl-tyrosine cross-link GENETICS !$#gene coI !$#genome mitochondrion !$#genetic_code SGC1 COMPLEX part of a 13 chain complex spanning the inner mitochondrial !1membrane and consisting of one each of chains I, II (see !1PIR:OBBO2), III (see PIR:OTBO3), IV (see PIR:OLBO4), Va (see !1PIR:CABO), Vb (see PIR:OGBO6A), VIa (see PIR:OGBO6), VIb !1(see PIR:OGBO7), VIc (see PIR:OGBO6C), VIIa (see !1PIR:OSBO7A), VIIb (see PIR:OSBO7B), VIIc (see PIR:OSBO8A), !1VIII (see PIR:OSBO8); the complex may form dimers within the !1mitochondrial inner-membrane FUNCTION !$#description the cytochrome-c oxidase complex catalyzes the oxidation of !1four molecules of reduced cytochrome c in the intracristal !1(or intermembrane) space using one oxygen molecule and four !1protons from the mitochondrial matrix producing two !1molecules of water and lowering the concentration of protons !1in the mitochondrial matrix !$#pathway oxidative phosphorylation; respiratory chain !$#note chain I directly reduces oxygen on the mitochondrial matrix !1side of the inner-membrane; the oxygen is bound between the !1heme a3 iron atom and the copper atom, referred to as copper !1B CLASSIFICATION #superfamily cytochrome-c oxidase chain I; cytochrome-c !1oxidase chain I homology KEYWORDS chromoprotein; copper; electron transfer; heme; iron; !1magnesium; membrane-associated complex; metalloprotein; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$1-11 #domain mitochondrial matrix #status experimental !8#label MM1\ !$11-457 #domain cytochrome-c oxidase chain I homology #label !8CO1\ !$12-40 #domain transmembrane helix #status experimental !8#label TR01\ !$41-50 #domain intracristal #status experimental #label !8ITC1\ !$51-86 #domain transmembrane helix #status experimental !8#label TR02\ !$87-94 #domain mitochondrial matrix #status experimental !8#label MM2\ !$95-117 #domain transmembrane helix #status experimental !8#label TR03\ !$118-140 #domain intracristal #status experimental #label !8ITC2\ !$141-170 #domain transmembrane helix #status experimental !8#label TR04\ !$171-182 #domain mitochondrial matrix #status experimental !8#label MM3\ !$183-212 #domain transmembrane helix #status experimental !8#label TR05\ !$213-227 #domain intracristal #status experimental #label !8ITC3\ !$228-261 #domain transmembrane helix #status experimental !8#label TR06\ !$262-269 #domain mitochondrial matrix #status experimental !8#label MM4\ !$270-286 #domain transmembrane helix #status experimental !8#label TR07\ !$287-298 #domain intracristal #status experimental #label !8ITC4\ !$299-327 #domain transmembrane helix #status experimental !8#label TR08\ !$326-335 #domain mitochondrial matrix #status experimental !8#label MM5\ !$336-356 #domain transmembrane helix #status experimental !8#label TR09\ !$357-370 #domain intracristal #status experimental #label !8ITC5\ !$371-400 #domain transmembrane helix #status experimental !8#label TR10\ !$401-406 #domain mitochondrial matrix #status experimental !8#label MM6\ !$407-433 #domain transmembrane helix #status experimental !8#label TR11\ !$432-446 #domain intracristal #status experimental #label !8ITC6\ !$447-478 #domain transmembrane helix #status experimental !8#label TR12\ !$479-514 #domain mitochondrial matrix #status experimental !8#label MM7\ !$1 #modified_site N-formylmethionine #status !8experimental\ !$61,378 #binding_site heme a iron (His) (axial ligands) !8#status experimental\ !$240,290,291 #binding_site copper (His) #status experimental\ !$240-244 #cross-link 1'-histidyl-3'-tyrosine (His-Tyr) #status !8experimental\ !$244 #binding_site oxygen (Tyr) #status predicted\ !$368 #binding_site magnesium (His) (shared with chain II) !8#status experimental\ !$376 #binding_site heme a3 iron (His) (axial ligand) !8#status experimental SUMMARY #length 514 #molecular-weight 57032 #checksum 8865 SEQUENCE /// ENTRY ODMS1 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain I - mouse mitochondrion ORGANISM #formal_name mitochondrion Mus musculus #common_name house mouse DATE 02-Apr-1982 #sequence_revision 02-Apr-1982 #text_change 07-Dec-1999 ACCESSIONS A00465 REFERENCE A00153 !$#authors Bibb, M.J.; Van Etten, R.A.; Wright, C.T.; Walberg, M.W.; !1Clayton, D.A. !$#journal Cell (1981) 26:167-180 !$#title Sequence and gene organization of mouse mitochondrial DNA. !$#cross-references MUID:82137051; PMID:7332926 !$#accession A00465 !'##molecule_type DNA !'##residues 1-514 ##label BIB !'##cross-references GB:J01420; NID:g342520; PIDN:AAB48646.1; !1PID:g342521; EMBL:V00711; NID:g13838; PID:g13841 GENETICS !$#gene coI !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily cytochrome-c oxidase chain I; cytochrome-c !1oxidase chain I homology KEYWORDS chromoprotein; copper; electron transfer; heme; iron; !1magnesium; membrane-associated complex; metalloprotein; !1mitochondrion; oxidative phosphorylation; oxidoreductase; !1respiratory chain; transmembrane protein FEATURE !$11-457 #domain cytochrome-c oxidase chain I homology #label !8CO1\ !$61,378 #binding_site heme a iron (His) (axial ligands) !8#status predicted\ !$240,290,291 #binding_site copper (His) #status predicted\ !$240-244 #cross-link 1'-histidyl-3'-tyrosine (His-Tyr) #status !8predicted\ !$244 #binding_site oxygen (Tyr) #status predicted\ !$368 #binding_site magnesium (His) (shared with chain II) !8#status predicted\ !$376 #binding_site heme a3 iron (His) (axial ligand) !8#status predicted SUMMARY #length 514 #molecular-weight 56862 #checksum 8596 SEQUENCE /// ENTRY ODXL1 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain I - African clawed frog mitochondrion ALTERNATE_NAMES cytochrome a3 polypeptide I; cytochrome aa3 polypeptide I ORGANISM #formal_name mitochondrion Xenopus laevis #common_name African clawed frog DATE 28-Feb-1986 #sequence_revision 17-Jul-1998 #text_change 07-Dec-1999 ACCESSIONS A00466 REFERENCE A00155 !$#authors Roe, B.A.; Ma, D.P.; Wilson, R.K.; Wong, J.F.H. !$#journal J. Biol. Chem. (1985) 260:9759-9774 !$#title The complete nucleotide sequence of the Xenopus laevis !1mitochondrial genome. !$#cross-references MUID:85261388; PMID:4019494 !$#accession A00466 !'##molecule_type DNA !'##residues 1-518 ##label ROE !'##cross-references GB:M10217; GB:X01600; GB:X01601; GB:X02890; !1NID:g343717; PIDN:AAA66460.1; PID:g807685 !'##note RNA processing and polyadenylation converts the codon after !1518-Lys from UCG to the UAA termination codon GENETICS !$#gene coI !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily cytochrome-c oxidase chain I; cytochrome-c !1oxidase chain I homology KEYWORDS chromoprotein; copper; electron transfer; heme; iron; !1magnesium; membrane-associated complex; metalloprotein; !1mitochondrion; oxidative phosphorylation; oxidoreductase; !1respiratory chain; transmembrane protein FEATURE !$11-457 #domain cytochrome-c oxidase chain I homology #label !8CO1\ !$61,378 #binding_site heme a iron (His) (axial ligands) !8#status predicted\ !$240,290,291 #binding_site copper (His) #status predicted\ !$240-244 #cross-link 1'-histidyl-3'-tyrosine (His-Tyr) #status !8predicted\ !$244 #binding_site oxygen (Tyr) #status predicted\ !$368 #binding_site magnesium (His) (shared with chain II) !8#status predicted\ !$376 #binding_site heme a3 iron (His) (axial ligand) !8#status predicted SUMMARY #length 518 #molecular-weight 57352 #checksum 9462 SEQUENCE /// ENTRY ODFF1 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain I - fruit fly (Drosophila melanogaster) mitochondrion ORGANISM #formal_name mitochondrion Drosophila melanogaster DATE 18-Apr-1984 #sequence_revision 18-Apr-1984 #text_change 07-Dec-1999 ACCESSIONS A93307; A00467 REFERENCE A93307 !$#authors de Bruijn, M.H.L. !$#journal Nature (1983) 304:234-241 !$#title Drosophila melanogaster mitochondrial DNA, a novel !1organization and genetic code. !$#cross-references MUID:83245048; PMID:6408489 !$#accession A93307 !'##molecule_type DNA !'##residues 1-512 ##label DEB !'##cross-references GB:U37541; NID:g1166529; PIDN:AAC47812.1; !1PID:g1166531 !'##note the nucleotide sequence corresponding to residue 1 is ATAA; the !1authors translated this sequence as Met GENETICS !$#gene coI !'##cross-references FlyBase:FBgn0013674 !$#genome mitochondrion !$#genetic_code SGC4 CLASSIFICATION #superfamily cytochrome-c oxidase chain I; cytochrome-c !1oxidase chain I homology KEYWORDS chromoprotein; copper; electron transfer; heme; iron; !1magnesium; membrane-associated complex; metalloprotein; !1mitochondrion; oxidative phosphorylation; oxidoreductase; !1respiratory chain; transmembrane protein FEATURE !$10-456 #domain cytochrome-c oxidase chain I homology #label !8CO1\ !$60,377 #binding_site heme a iron (His) (axial ligands) !8#status predicted\ !$239,289,290 #binding_site copper (His) #status predicted\ !$239-243 #cross-link 1'-histidyl-3'-tyrosine (His-Tyr) #status !8predicted\ !$243 #binding_site oxygen (Tyr) #status predicted\ !$367 #binding_site magnesium (His) (shared with chain II) !8#status predicted\ !$375 #binding_site heme a3 iron (His) (axial ligand) !8#status predicted SUMMARY #length 512 #molecular-weight 56503 #checksum 2399 SEQUENCE /// ENTRY ODFF1Y #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain I - fruit fly (Drosophila yakuba) mitochondrion ORGANISM #formal_name mitochondrion Drosophila yakuba DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 07-Dec-1999 ACCESSIONS A93488; B25797; A00467 REFERENCE A93488 !$#authors Clary, D.O.; Wolstenholme, D.R. !$#journal Nucleic Acids Res. (1983) 11:6859-6872 !$#title Genes for cytochrome c oxidase subunit I, URF2, and three !1tRNAs in Drosophila mitochondrial DNA. !$#cross-references MUID:84041489; PMID:6314262 !$#accession A93488 !'##molecule_type DNA !'##residues 1-512 ##label CL1 !'##cross-references GB:X03240; NID:g12923; PIDN:CAA26986.1; PID:g809039 !'##note the nucleotide sequence corresponding to residue 1 is ATAA, !1which was not translated by the authors REFERENCE A92962 !$#authors Clary, D.O.; Wolstenholme, D.R. !$#journal J. Mol. Evol. (1985) 22:252-271 !$#title The mitochondrial DNA molecule of Drosophila yakuba: !1nucleotide sequence, gene organization, and genetic code. !$#cross-references MUID:86089137; PMID:3001325 !$#accession B25797 !'##molecule_type DNA !'##residues 1-512 ##label CL2 !'##cross-references GB:X03240; GB:J01400; GB:J01402; GB:J01403; !1GB:J01406; GB:J01408; GB:V01521; GB:X00563; NID:g12923; !1PIDN:CAA26986.1; PID:g809039 GENETICS !$#gene COI !'##cross-references FlyBase:FBgn0013179 !$#genome mitochondrion !$#genetic_code SGC4 !$#start_codon ATAA CLASSIFICATION #superfamily cytochrome-c oxidase chain I; cytochrome-c !1oxidase chain I homology KEYWORDS chromoprotein; copper; electron transfer; heme; iron; !1magnesium; membrane-associated complex; metalloprotein; !1mitochondrion; oxidative phosphorylation; oxidoreductase; !1respiratory chain; transmembrane protein FEATURE !$10-456 #domain cytochrome-c oxidase chain I homology #label !8CO1\ !$60,377 #binding_site heme a iron (His) (axial ligands) !8#status predicted\ !$239,289,290 #binding_site copper (His) #status predicted\ !$239-243 #cross-link 1'-histidyl-3'-tyrosine (His-Tyr) #status !8predicted\ !$243 #binding_site oxygen (Tyr) #status predicted\ !$367 #binding_site magnesium (His) (shared with chain II) !8#status predicted\ !$375 #binding_site heme a3 iron (His) (axial ligand) !8#status predicted SUMMARY #length 512 #molecular-weight 56526 #checksum 3786 SEQUENCE /// ENTRY ODBY1 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain I - yeast (Saccharomyces cerevisiae) mitochondrion ORGANISM #formal_name mitochondrion Saccharomyces cerevisiae DATE 30-Apr-1981 #sequence_revision 19-Feb-1984 #text_change 19-Apr-2002 ACCESSIONS A00468; S22218; S22217; S43945 REFERENCE A92267 !$#authors Bonitz, S.G.; Coruzzi, G.; Thalenfeld, B.E.; Tzagoloff, A.; !1Macino, G. !$#journal J. Biol. Chem. (1980) 255:11927-11941 !$#title Assembly of the mitochondrial membrane system. Structure and !1nucleotide sequence of the gene coding for subunit 1 of !1yeast cytochrome oxidase. !$#cross-references MUID:81069885; PMID:6254986 !$#accession A00468 !'##molecule_type DNA !'##residues 1-512 ##label BON !'##cross-references EMBL:V00694 !'##experimental_source strain D273-10B !'##note we have reassigned the boundaries of introns 1, 2, and 5 by !1homology with other cytochrome-c oxidase chain I sequences; !1the authors' translation differs from the sequence shown in !1lacking 57-Val, in having 69-Cys and 378-Tyr, and in having !1an additional Thr after 69-Cys !'##note the authors translated the codon ATA for residue 87 according !1to the standard code REFERENCE S22218 !$#authors Seraphin, B.; Simon, M.; Jacq, C.; Faye, G. !$#journal Nucleic Acids Res. (1989) 17:4886 !$#title Sequence of the yeast mitochondrial OXI3/OLI2 promoter !1region. !$#cross-references MUID:89315236; PMID:2664712 !$#accession S22218 !'##status translation not shown !'##molecule_type DNA !'##residues 1-56 ##label SER !'##cross-references EMBL:X14910; NID:g13584; PIDN:CAA33036.1; !1PID:g13585 REFERENCE S05820 !$#authors Simon, M.; Faye, G. !$#journal Mol. Gen. Genet. (1984) 196:266-274 !$#title Organization and processing of the mitochondrial oxi3/oli2 !1multigenic transcript in yeast. !$#cross-references MUID:85035872; PMID:6387398 !$#accession S22217 !'##molecule_type DNA !'##residues 493-512 ##label SIM !'##cross-references EMBL:X00960; NID:g13563; PIDN:CAA25472.1; !1PID:g13564 REFERENCE S43945 !$#authors Novitski, C.E.; Macreadie, I.G.; Maxwell, R.J.; Lukins, !1H.B.; Linnane, A.W.; Nagley, P. !$#journal Curr. Genet. (1984) 8:135-146 !$#title Biogenesis of mitochondria: genetic and molecular analysis !1of the oli2 region of mitochondrial DNA in Saccharomyces !1cerevisiae. !$#accession S43945 !'##molecule_type DNA !'##residues 493-512 ##label NOV !'##cross-references EMBL:M36379; NID:g343760; PIDN:AAA32147.1; !1PID:g343761 GENETICS !$#gene SGD:COX1; cox1; oxi3 !'##cross-references SGD:S0007260 !$#map_position 43.7-57.6 !$#genome mitochondrion !$#genetic_code SGC2 !$#introns 57/1; 69/1; 81/3; 240/3; 378/1; 478/3; 488/3 CLASSIFICATION #superfamily cytochrome-c oxidase chain I; cytochrome-c !1oxidase chain I homology KEYWORDS chromoprotein; copper; electron transfer; heme; iron; !1magnesium; membrane-associated complex; metalloprotein; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$10-457 #domain cytochrome-c oxidase chain I homology #label !8CO1\ !$62,378 #binding_site heme a iron (His) (axial ligands) !8#status predicted\ !$241,290,291 #binding_site copper (His) #status predicted\ !$241-245 #cross-link 1'-histidyl-3'-tyrosine (His-Tyr) #status !8predicted\ !$245 #binding_site oxygen (Tyr) #status predicted\ !$368 #binding_site magnesium (His) (shared with chain II) !8#status predicted\ !$376 #binding_site heme a3 iron (His) (axial ligand) !8#status predicted SUMMARY #length 512 #molecular-weight 56302 #checksum 2835 SEQUENCE /// ENTRY ODNC1 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain I - Neurospora crassa mitochondrion ALTERNATE_NAMES cytochrome a3 polypeptide I; cytochrome aa3 polypeptide I ORGANISM #formal_name mitochondrion Neurospora crassa DATE 13-Aug-1986 #sequence_revision 13-Aug-1986 #text_change 07-Dec-1999 ACCESSIONS A00469; S07650; S07651 REFERENCE A00469 !$#authors Burger, G.; Scriven, C.; Machleidt, W.; Werner, S. !$#journal EMBO J. (1982) 1:1385-1391 !$#title Subunit 1 of cytochrome oxidase from Neurospora crassa: !1nucleotide sequence of the coding gene and partial amino !1acid sequence of the protein. !$#cross-references MUID:84207889; PMID:6327266 !$#accession A00469 !'##molecule_type DNA !'##residues 1-557 ##label BUR !'##cross-references EMBL:X01850; NID:g13119; PIDN:CAA25976.1; !1PID:g762976 !'##note the amino end of the mature protein may be 3-Ser REFERENCE S07649 !$#authors Field, D.J.; Sommerfield, A.; Saville, B.J.; Collins, R.A. !$#journal Nucleic Acids Res. (1989) 17:9087-9099 !$#title A group II intron in the Neurospora mitochondrial coI gene: !1nucleotide sequence and implications for splicing and !1molecular evolution. !$#cross-references MUID:90067912; PMID:2531370 !$#accession S07650 !'##molecule_type DNA !'##residues 1-73 ##label FIE !'##cross-references EMBL:X14669; NID:g13123 REFERENCE S07651 !$#authors Collins, R.A. !$#submission submitted to the EMBL Data Library, March 1989 !$#accession S07651 !'##molecule_type DNA !'##residues 1-526,'V',528-540 ##label COL !'##cross-references EMBL:X14669; NID:g13123 REFERENCE A43101 !$#authors Vassilev, A.O.; Plesofsky-Vig, N.; Brambl, R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1995) 92:8680-8684 !$#title Cytochrome c oxidase in Neurospora crassa contains myristic !1acid covalently linked to subunit 1. !$#cross-references MUID:96004602; PMID:7567996 !$#contents annotation; modified site GENETICS !$#gene COI !$#genome mitochondrion !$#genetic_code SGC3 !$#introns 72/1; 99/2; 210/3; 249/2 FUNCTION !$#description the cytochrome-c oxidase complex catalyzes the oxidation of !1four molecules of reduced cytochrome c in the intracristal !1(or intermembrane) space using one oxygen molecule and four !1protons from the mitochondrial matrix producing two !1molecules of water and lowering the concentration of protons !1in the mitochondrial matrix !$#pathway oxidative phosphorylation; respiratory chain !$#note chain I directly reduces oxygen on the mitochondrial matrix !1side of the inner-membrane; the oxygen is bound between the !1heme a3 iron atom and the copper atom, referred to as copper !1B CLASSIFICATION #superfamily cytochrome-c oxidase chain I; cytochrome-c !1oxidase chain I homology KEYWORDS chromoprotein; copper; electron transfer; heme; iron; !1lipoprotein; magnesium; membrane-associated complex; !1metalloprotein; mitochondrion; myristylation; oxidative !1phosphorylation; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$16-462 #domain cytochrome-c oxidase chain I homology #label !8CO1\ !$67,383 #binding_site heme a iron (His) (axial ligands) !8#status predicted\ !$246,295,296 #binding_site copper (His) #status predicted\ !$246-250 #cross-link 1'-histidyl-3'-tyrosine (His-Tyr) #status !8predicted\ !$250 #binding_site oxygen (Tyr) #status predicted\ !$324 #binding_site myristate (Lys) (covalent) #status !8experimental\ !$373 #binding_site magnesium (His) (shared with chain II) !8#status predicted\ !$381 #binding_site heme a3 iron (His) (axial ligand) !8#status predicted SUMMARY #length 557 #molecular-weight 61493 #checksum 9740 SEQUENCE /// ENTRY ODAS1 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain I - Emericella nidulans mitochondrion ORGANISM #formal_name mitochondrion Emericella nidulans, Aspergillus nidulans DATE 22-Nov-1983 #sequence_revision 12-Apr-1996 #text_change 07-Dec-1999 ACCESSIONS A22735; A00470; S05630 REFERENCE A90991 !$#authors Waring, R.B.; Brown, T.A.; Ray, J.A.; Scazzocchio, C.; !1Davies, R.W. !$#journal EMBO J. (1984) 3:2121-2128 !$#title Three variant introns of the same general class in the !1mitochondrial gene for cytochrome oxidase subunit 1 in !1Aspergillus nidulans. !$#cross-references MUID:85027165; PMID:6092056 !$#accession A22735 !'##molecule_type DNA !'##residues 1-567 ##label WAR REFERENCE A93436 !$#authors Netzker, R.; Kochel, H.G.; Basak, N.; Kuntzel, H. !$#journal Nucleic Acids Res. (1982) 10:4783-4794 !$#title Nucleotide sequence of Aspergillus nidulans mitochondrial !1genes coding for ATPase subunit 6, cytochrome oxidase !1subunit 3, seven unidentified proteins, four tRNAs and !1L-rRNA. !$#cross-references MUID:83038633; PMID:6290989 !$#accession A00470 !'##molecule_type DNA !'##residues 44-133 ##label NET !'##experimental_source imperfect stage GENETICS !$#gene cox1; oxiA !$#genome mitochondrion !$#genetic_code SGC3 !$#introns 133/3; 245/3; 284/3 CLASSIFICATION #superfamily cytochrome-c oxidase chain I; cytochrome-c !1oxidase chain I homology KEYWORDS chromoprotein; copper; electron transfer; heme; iron; !1magnesium; membrane-associated complex; metalloprotein; !1mitochondrion; oxidative phosphorylation; oxidoreductase; !1respiratory chain; transmembrane protein FEATURE !$50-496 #domain cytochrome-c oxidase chain I homology #label !8CO1\ !$101,417 #binding_site heme a iron (His) (axial ligands) !8#status predicted\ !$280,329,330 #binding_site copper (His) #status predicted\ !$280-284 #cross-link 1'-histidyl-3'-tyrosine (His-Tyr) #status !8predicted\ !$284 #binding_site oxygen (Tyr) #status predicted\ !$407 #binding_site magnesium (His) (shared with chain II) !8#status predicted\ !$415 #binding_site heme a3 iron (His) (axial ligand) !8#status predicted SUMMARY #length 567 #molecular-weight 62602 #checksum 5416 SEQUENCE /// ENTRY OBSY1 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain I - soybean mitochondrion ORGANISM #formal_name mitochondrion Glycine max #common_name soybean DATE 30-Sep-1988 #sequence_revision 30-Jun-1992 #text_change 23-Jul-1999 ACCESSIONS JA0001 REFERENCE JA0001 !$#authors Grabau, E.A. !$#journal Plant Mol. Biol. (1986) 7:377-384 !$#title Nucleotide sequence of the cytochrome oxidase subunit I gene !1from soybean mitochondria. !$#accession JA0001 !'##molecule_type DNA !'##residues 1-527 ##label GRA !'##cross-references EMBL:M16884; NID:g343345; PIDN:AAA70318.1; !1PID:g903881 !'##note the authors translated the codon CGG for residues 239 and 405 !1as Trp, assuming a special genetic code for plant !1mitochondria GENETICS !$#gene COI !$#genome mitochondrion CLASSIFICATION #superfamily cytochrome-c oxidase chain I; cytochrome-c !1oxidase chain I homology KEYWORDS chromoprotein; copper; electron transfer; heme; iron; !1magnesium; membrane-associated complex; metalloprotein; !1mitochondrion; oxidative phosphorylation; oxidoreductase; !1respiratory chain; transmembrane protein FEATURE !$12-459 #domain cytochrome-c oxidase chain I homology #label !8CO1\ !$64,380 #binding_site heme a iron (His) (axial ligands) !8#status predicted\ !$243,292,293 #binding_site copper (His) #status predicted\ !$243-247 #cross-link 1'-histidyl-3'-tyrosine (His-Tyr) #status !8predicted\ !$247 #binding_site oxygen (Tyr) #status predicted\ !$370 #binding_site magnesium (His) (shared with chain II) !8#status predicted\ !$378 #binding_site heme a3 iron (His) (axial ligand) !8#status predicted SUMMARY #length 527 #molecular-weight 57477 #checksum 9678 SEQUENCE /// ENTRY ODRZ1 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain I - rice mitochondrion ORGANISM #formal_name mitochondrion Oryza sativa #common_name rice DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 23-Jul-1999 ACCESSIONS S06761; S17914 REFERENCE S06761 !$#authors Kadowaki, K.I.; Suzuki, T.; Kazama, S.; Oh-fuchi, T.; !1Sakamoto, W. !$#journal Nucleic Acids Res. (1989) 17:7519 !$#title Nucleotide sequence of the cytochrome oxidase subunit I gene !1from rice mitochondria. !$#cross-references MUID:90016815; PMID:2552410 !$#accession S06761 !'##molecule_type DNA !'##residues 1-524 ##label KAD !'##cross-references EMBL:X15990; NID:g13218; PIDN:CAA34122.1; !1PID:g13219 !'##note the authors translated the codon CGG for residue 405 as Trp, !1assuming a special genetic code for plant mitochondria REFERENCE S17912 !$#authors Suzuki, T.; Kazama, S.; Hirai, A.; Akihama, T.; Kadowaki, K. !$#journal Curr. Genet. (1991) 20:331-337 !$#title The rice mitochondrial nad3 gene has an extended reading !1frame at its 5' end: nucleotide sequence analysis of rice !1trnS, nad3, and rps12 genes. !$#cross-references MUID:92035104; PMID:1718614 !$#accession S17914 !'##molecule_type DNA !'##residues 1-57 ##label SUZ !'##cross-references EMBL:M57903; NID:g343217; PIDN:AAA70312.1; !1PID:g343222 GENETICS !$#gene coxI !$#genome mitochondrion FUNCTION !$#description the cytochrome-c oxidase complex catalyzes the oxidation of !1four molecules of reduced cytochrome c in the intracristal !1(or intermembrane) space using one oxygen molecule and four !1protons from the mitochondrial matrix producing two !1molecules of water and lowering the concentration of protons !1in the mitochondrial matrix !$#pathway oxidative phosphorylation; respiratory chain !$#note chain I directly reduces oxygen on the mitochondrial matrix !1side of the inner-membrane; the oxygen is bound between the !1heme a3 iron atom and the copper atom, referred to as copper !1B CLASSIFICATION #superfamily cytochrome-c oxidase chain I; cytochrome-c !1oxidase chain I homology KEYWORDS chromoprotein; copper; electron transfer; heme; iron; !1magnesium; membrane-associated complex; metalloprotein; !1mitochondrion; oxidative phosphorylation; oxidoreductase; !1respiratory chain; transmembrane protein FEATURE !$12-459 #domain cytochrome-c oxidase chain I homology #label !8CO1\ !$64,380 #binding_site heme a iron (His) (axial ligands) !8#status predicted\ !$243,292,293 #binding_site copper (His) #status predicted\ !$243-247 #cross-link 1'-histidyl-3'-tyrosine (His-Tyr) #status !8predicted\ !$247 #binding_site oxygen (Tyr) #status predicted\ !$370 #binding_site magnesium (His) (shared with chain II) !8#status predicted\ !$378 #binding_site heme a3 iron (His) (axial ligand) !8#status predicted SUMMARY #length 524 #molecular-weight 57766 #checksum 3856 SEQUENCE /// ENTRY ODZM1 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain I - maize mitochondrion ORGANISM #formal_name mitochondrion Zea mays #common_name maize DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 23-Jul-1999 ACCESSIONS A22840 REFERENCE A22840 !$#authors Issac, P.G.; Jones, V.P.; Leaver, C.J. !$#journal EMBO J. (1985) 4:1617-1623 !$#title The maize cytochrome c oxidase subunit I gene: sequence, !1expression and rearrangement in cytoplasmic male sterile !1plants. !$#accession A22840 !'##molecule_type DNA !'##residues 1-528 ##label ISS !'##cross-references EMBL:X02660; NID:g12888; PIDN:CAA26496.1; !1PID:g12889 !'##note the authors translated the codon CGG for residue 405 as Trp, !1assuming a special genetic code for plant mitochondria GENETICS !$#gene COXI !$#genome mitochondrion CLASSIFICATION #superfamily cytochrome-c oxidase chain I; cytochrome-c !1oxidase chain I homology KEYWORDS chromoprotein; copper; electron transfer; heme; iron; !1magnesium; membrane-associated complex; metalloprotein; !1mitochondrion; oxidative phosphorylation; oxidoreductase; !1respiratory chain; transmembrane protein FEATURE !$12-459 #domain cytochrome-c oxidase chain I homology #label !8CO1\ !$64,380 #binding_site heme a iron (His) (axial ligands) !8#status predicted\ !$243,292,293 #binding_site copper (His) #status predicted\ !$243-247 #cross-link 1'-histidyl-3'-tyrosine (His-Tyr) #status !8predicted\ !$247 #binding_site oxygen (Tyr) #status predicted\ !$370 #binding_site magnesium (His) (shared with chain II) !8#status predicted\ !$378 #binding_site heme a3 iron (His) (axial ligand) !8#status predicted SUMMARY #length 528 #molecular-weight 58257 #checksum 8184 SEQUENCE /// ENTRY ODOB1M #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain I - Bertero's evening primrose mitochondrion ALTERNATE_NAMES cytochrome a3 polypeptide I; cytochrome aa3 polypeptide I ORGANISM #formal_name mitochondrion Oenothera berteriana #common_name Bertero's evening primrose DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 01-Dec-2000 ACCESSIONS A26170 REFERENCE A91078 !$#authors Hiesel, R.; Schobel, W.; Schuster, W.; Brennicke, A. !$#journal EMBO J. (1987) 6:29-34 !$#title The cytochrome oxidase subunit I and subunit III genes in !1Oenothera mitochondria are transcribed from identical !1promoter sequences. !$#accession A26170 !'##molecule_type mRNA !'##residues 1-527 ##label HIE !'##cross-references EMBL:X05465; NID:g13166; PIDN:CAA29025.1; !1PID:g13167 !'##note the authors translated the codon CGG for residues 239 and 405 !1as Trp, assuming a special genetic code for plant !1mitochondria !'##note the source species is not specified; see GenBank entry !1MIOBCOX1, release 117.0 GENETICS !$#gene coI !$#genome mitochondrion CLASSIFICATION #superfamily cytochrome-c oxidase chain I; cytochrome-c !1oxidase chain I homology KEYWORDS chromoprotein; copper; electron transfer; heme; iron; !1magnesium; membrane-associated complex; metalloprotein; !1mitochondrion; oxidative phosphorylation; oxidoreductase; !1respiratory chain; transmembrane protein FEATURE !$12-459 #domain cytochrome-c oxidase chain I homology #label !8CO1\ !$64,380 #binding_site heme a iron (His) (axial ligands) !8#status predicted\ !$243,292,293 #binding_site copper (His) #status predicted\ !$243-247 #cross-link 1'-histidyl-3'-tyrosine (His-Tyr) #status !8predicted\ !$247 #binding_site oxygen (Tyr) #status predicted\ !$370 #binding_site magnesium (His) (shared with chain II) !8#status predicted\ !$378 #binding_site heme a3 iron (His) (axial ligand) !8#status predicted SUMMARY #length 527 #molecular-weight 57241 #checksum 9095 SEQUENCE /// ENTRY ODZJ1 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain I - Bradyrhizobium japonicum ORGANISM #formal_name Bradyrhizobium japonicum DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 23-Jul-1999 ACCESSIONS S13076; S12101 REFERENCE S13076 !$#authors Bott, M.; Bolliger, M.; Hennecke, H. !$#journal Mol. Microbiol. (1990) 4:2147-2157 !$#title Genetic analysis of the cytochrome c-aa(3) branch of the !1Bradyrhizobium japonicum respiratory chain. !$#cross-references MUID:91211625; PMID:1965217 !$#accession S13076 !'##molecule_type DNA !'##residues 1-541 ##label BOT !'##cross-references EMBL:X54800; NID:g39502; PIDN:CAA38570.1; !1PID:g39503 REFERENCE S12101 !$#authors Gabel, C.; Maier, R.J. !$#journal Nucleic Acids Res. (1990) 18:6143 !$#title Nucleotide sequence of the coxA gene encoding subunit I of !1cytochrome aa(3) of Bradyrhizobium japonicum. !$#cross-references MUID:91045095; PMID:2172930 !$#accession S12101 !'##molecule_type DNA !'##residues 1-541 ##label GAB !'##cross-references EMBL:X54318; NID:g39505; PIDN:CAA38216.1; !1PID:g39506 GENETICS !$#gene coxA CLASSIFICATION #superfamily cytochrome-c oxidase chain I; cytochrome-c !1oxidase chain I homology KEYWORDS chromoprotein; copper; electron transfer; heme; iron; !1magnesium; membrane-associated complex; metalloprotein; !1oxidative phosphorylation; oxidoreductase; respiratory !1chain; transmembrane protein FEATURE !$34-484 #domain cytochrome-c oxidase chain I homology #label !8CO1\ !$41-60 #domain transmembrane #status predicted #label TM01\ !$87-107 #domain transmembrane #status predicted #label TM02\ !$124-142 #domain transmembrane #status predicted #label TM03\ !$173-193 #domain transmembrane #status predicted #label TM04\ !$211-231 #domain transmembrane #status predicted #label TM05\ !$262-282 #domain transmembrane #status predicted #label TM06\ !$294-315 #domain transmembrane #status predicted #label TM07\ !$331-352 #domain transmembrane #status predicted #label TM08\ !$365-385 #domain transmembrane #status predicted #label TM09\ !$404-424 #domain transmembrane #status predicted #label TM10\ !$441-460 #domain transmembrane #status predicted #label TM11\ !$483-503 #domain transmembrane #status predicted #label TM12\ !$85,405 #binding_site heme a iron (His) (axial ligands) !8#status predicted\ !$268,317,318 #binding_site copper (His) #status predicted\ !$268-272 #cross-link 1'-histidyl-3'-tyrosine (His-Tyr) #status !8predicted\ !$272 #binding_site oxygen (Tyr) #status predicted\ !$403 #binding_site heme a3 iron (His) (axial ligand) !8#status predicted SUMMARY #length 541 #molecular-weight 59265 #checksum 9006 SEQUENCE /// ENTRY ODUTMB #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain I - Trypanosoma brucei mitochondrion ORGANISM #formal_name mitochondrion Trypanosoma brucei DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 11-May-2000 ACCESSIONS A00471 REFERENCE A93537 !$#authors Hensgens, L.A.M.; Brakenhoff, J.; De Vries, B.F.; Sloof, P.; !1Tromp, M.C.; Van Boom, J.H.; Benne, R. !$#journal Nucleic Acids Res. (1984) 12:7327-7344 !$#title The sequence of the gene for cytochrome c oxidase subunit I, !1a frameshift containing gene for cytochrome c oxidase !1subunit II and seven unassigned reading frames in !1Trypanosoma brucei mitochondrial maxi-circle DNA. !$#cross-references MUID:85037915; PMID:6093040 !$#accession A00471 !'##molecule_type DNA !'##residues 1-549 ##label HEN !'##cross-references GB:M94286; NID:g343546 !'##note this translation is not annotated in GenBank entry TRBKPGEN, !1release 109.0 COMMENT The DNA sequence is from a segment of the 20-kb maxicircle, !1which is believed to be the trypanosome mitochondrial !1genome. GENETICS !$#gene coxI !$#genome mitochondrion !$#genetic_code SGC6 CLASSIFICATION #superfamily cytochrome-c oxidase chain I; cytochrome-c !1oxidase chain I homology KEYWORDS chromoprotein; copper; electron transfer; heme; iron; !1magnesium; membrane-associated complex; metalloprotein; !1mitochondrion; oxidative phosphorylation; oxidoreductase; !1respiratory chain; transmembrane protein FEATURE !$12-459 #domain cytochrome-c oxidase chain I homology #label !8CO1\ !$64,380 #binding_site heme a iron (His) (axial ligands) !8#status predicted\ !$243,292,293 #binding_site copper (His) #status predicted\ !$243-247 #cross-link 1'-histidyl-3'-tyrosine (His-Tyr) #status !8predicted\ !$247 #binding_site oxygen (Tyr) #status predicted\ !$370 #binding_site magnesium (His) (shared with chain II) !8#status predicted\ !$378 #binding_site heme a3 iron (His) (axial ligand) !8#status predicted SUMMARY #length 549 #molecular-weight 63348 #checksum 6196 SEQUENCE /// ENTRY D30010 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain I - Leishmania tarentolae mitochondrion ORGANISM #formal_name mitochondrion Leishmania tarentolae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 07-Dec-1999 ACCESSIONS D30010 REFERENCE A22848 !$#authors de la Cruz, V.F.; Neckelmann, N.; Simpson, L. !$#journal J. Biol. Chem. (1984) 259:15136-15147 !$#title Sequences of six genes and several open reading frames in !1the kinetoplast maxicircle DNA of Leishmania tarentolae. !$#cross-references MUID:85079995; PMID:6096360 !$#accession D30010 !'##molecule_type DNA !'##residues 1-549 ##label DEL !'##cross-references GB:M10126 GENETICS !$#genome mitochondrion !$#genetic_code SGC6 CLASSIFICATION #superfamily cytochrome-c oxidase chain I; cytochrome-c !1oxidase chain I homology KEYWORDS chromoprotein; copper; electron transfer; heme; iron; !1magnesium; membrane-associated complex; metalloprotein; !1mitochondrion; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$12-459 #domain cytochrome-c oxidase chain I homology #label !8CO1\ !$64,380 #binding_site heme a iron (His) (axial ligands) !8#status predicted\ !$243,292,293 #binding_site copper (His) #status predicted\ !$243-247 #cross-link 1'-histidyl-3'-tyrosine (His-Tyr) #status !8predicted\ !$247 #binding_site oxygen (Tyr) #status predicted\ !$370 #binding_site magnesium (His) (shared with chain II) !8#status predicted\ !$378 #binding_site heme a3 iron (His) (axial ligand) !8#status predicted SUMMARY #length 549 #molecular-weight 63271 #checksum 8865 SEQUENCE /// ENTRY ODPP1 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain I - Paramecium sp. mitochondrion ALTERNATE_NAMES cytochrome a3 polypeptide I; cytochrome aa3 polypeptide I ORGANISM #formal_name mitochondrion Paramecium sp. DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 07-Dec-1999 ACCESSIONS A24988 REFERENCE A91555 !$#authors Pritchard, A.E.; Seilhamer, J.J.; Cummings, D.J. !$#journal Gene (1986) 44:243-253 !$#title Paramecium mitochondrial DNA sequences and RNA transcripts !1for cytochrome oxidase subunit I, URF1, and three ORFs !1adjacent to the replication origin. !$#cross-references MUID:87055241; PMID:3023187 !$#accession A24988 !'##molecule_type DNA !'##residues 1-645 ##label PRI !'##cross-references GB:M15281; NID:g342944; PIDN:AAA79251.1; !1PID:g1019626 !'##note in GenBank entry ODPP1, release 109.0, PID:g1019626 assumes !1special genetic code 4 with a translation exception rather !1than special genetic code 6 GENETICS !$#gene COI !$#genome mitochondrion !$#genetic_code SGC6 !$#start_codon ATA CLASSIFICATION #superfamily cytochrome-c oxidase chain I; cytochrome-c !1oxidase chain I homology KEYWORDS chromoprotein; copper; electron transfer; heme; iron; !1magnesium; membrane-associated complex; metalloprotein; !1mitochondrion; oxidative phosphorylation; oxidoreductase; !1respiratory chain; transmembrane protein FEATURE !$2-559 #domain cytochrome-c oxidase chain I homology #label !8CO1\ !$54,480 #binding_site heme a iron (His) (axial ligands) !8#status predicted\ !$343,392,393 #binding_site copper (His) #status predicted\ !$343-347 #cross-link 1'-histidyl-3'-tyrosine (His-Tyr) #status !8predicted\ !$347 #binding_site oxygen (Tyr) #status predicted\ !$470 #binding_site magnesium (His) (shared with chain II) !8#status predicted\ !$478 #binding_site heme a3 iron (His) (axial ligand) !8#status predicted SUMMARY #length 645 #molecular-weight 74072 #checksum 2904 SEQUENCE /// ENTRY S07751 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain I - Paramecium tetraurelia mitochondrion ORGANISM #formal_name mitochondrion Paramecium tetraurelia DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 07-Dec-1999 ACCESSIONS S07751 REFERENCE S07725 !$#authors Pritchard, A.E.; Seilhamer, J.J.; Mahalingam, R.; Sable, !1C.L.; Venuti, S.E.; Cummings, D.J. !$#journal Nucleic Acids Res. (1990) 18:173-180 !$#title Nucleotide sequence of the mitochondrial genome of !1Paramecium. !$#cross-references MUID:90174913; PMID:2308823 !$#accession S07751 !'##status translation not shown !'##molecule_type DNA !'##residues 1-645 ##label PRI !'##cross-references EMBL:X15917; NID:g13256; PIDN:CAA34030.1; !1PID:g578766 GENETICS !$#gene COI !$#genome mitochondrion !$#genetic_code SGC6 !$#start_codon ATA CLASSIFICATION #superfamily cytochrome-c oxidase chain I; cytochrome-c !1oxidase chain I homology KEYWORDS chromoprotein; copper; electron transfer; heme; iron; !1magnesium; membrane-associated complex; metalloprotein; !1mitochondrion; oxidative phosphorylation; oxidoreductase; !1respiratory chain; transmembrane protein FEATURE !$2-559 #domain cytochrome-c oxidase chain I homology #label !8CO1\ !$54,480 #binding_site heme a iron (His) (axial ligands) !8#status predicted\ !$343,392,393 #binding_site copper (His) #status predicted\ !$343-347 #cross-link 1'-histidyl-3'-tyrosine (His-Tyr) #status !8predicted\ !$347 #binding_site oxygen (Tyr) #status predicted\ !$470 #binding_site magnesium (His) (shared with chain II) !8#status predicted\ !$478 #binding_site heme a3 iron (His) (axial ligand) !8#status predicted SUMMARY #length 645 #molecular-weight 74036 #checksum 2608 SEQUENCE /// ENTRY S00742 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain I - Tetrahymena pyriformis mitochondrion ORGANISM #formal_name mitochondrion Tetrahymena pyriformis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 07-Dec-1999 ACCESSIONS S00742 REFERENCE S00742 !$#authors Ziaie, Z.; Suyama, Y. !$#journal Curr. Genet. (1987) 12:357-368 !$#title The cytochrome oxidase subunit I gene of Tetrahymena: a 57 !1amino acid NH2-terminal extension and a 108 amino acid !1insert. !$#cross-references MUID:88184706; PMID:2833363 !$#accession S00742 !'##molecule_type DNA !'##residues 1-698 ##label ZIA !'##cross-references EMBL:X06133 GENETICS !$#genome mitochondrion !$#genetic_code SGC6 !$#start_codon ATA CLASSIFICATION #superfamily cytochrome-c oxidase chain I; cytochrome-c !1oxidase chain I homology KEYWORDS chromoprotein; copper; electron transfer; heme; iron; !1magnesium; membrane-associated complex; metalloprotein; !1mitochondrion; oxidative phosphorylation; oxidoreductase; !1respiratory chain; transmembrane protein FEATURE !$59-617 #domain cytochrome-c oxidase chain I homology #label !8CO1\ !$111,538 #binding_site heme a iron (His) (axial ligands) !8#status predicted\ !$401,450,451 #binding_site copper (His) #status predicted\ !$401-405 #cross-link 1'-histidyl-3'-tyrosine (His-Tyr) #status !8predicted\ !$405 #binding_site oxygen (Tyr) #status predicted\ !$528 #binding_site magnesium (His) (shared with chain II) !8#status predicted\ !$536 #binding_site heme a3 iron (His) (axial ligand) !8#status predicted SUMMARY #length 698 #molecular-weight 81746 #checksum 4835 SEQUENCE /// ENTRY S75272 #type complete TITLE cytochrome d ubiquinol oxidase (EC 1.10.3.-) chain II - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein slr1380 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S75272 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75272 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-336 ##label KAN !'##cross-references EMBL:D90904; GB:AB001339; NID:g1652225; !1PIDN:BAA17186.1; PID:g1652263 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene cydB CLASSIFICATION #superfamily cytochrome d ubiquinol oxidase KEYWORDS electron transfer; heme; oxidoreductase; respiratory chain; !1transmembrane protein SUMMARY #length 336 #molecular-weight 37225 #checksum 790 SEQUENCE /// ENTRY B28940 #type complete TITLE cytochrome d ubiquinol oxidase (EC 1.10.3.-) chain II - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS B28940; E64809 REFERENCE A92666 !$#authors Green, G.N.; Fang, H.; Lin, R.J.; Newton, G.; Mather, M.; !1Georgiou, C.D.; Gennis, R.B. !$#journal J. Biol. Chem. (1988) 263:13138-13143 !$#title The nucleotide sequence of the cyd locus encoding the two !1subunits of the cytochrome d terminal oxidase complex of !1Escherichia coli. !$#cross-references MUID:88330812; PMID:2843510 !$#accession B28940 !'##molecule_type DNA !'##residues 1-379 ##label GRE !'##cross-references GB:J03939; NID:g145638; PIDN:AAA18805.1; !1PID:g145640 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64809 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-379 ##label BLAT !'##cross-references GB:AE000176; GB:U00096; NID:g1786947; !1PIDN:AAC73828.1; PID:g1786954; UWGP:b0734 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene cydB; cyd-2 !$#map_position 17 min COMPLEX heterodimer; chain I and chain II FUNCTION !$#description the cytochrome d complex catalyzes the two-eletron oxidation !1of ubiquinol-8 and the four-eletron reduction of molecular !1oxygen to water CLASSIFICATION #superfamily cytochrome d ubiquinol oxidase KEYWORDS electron transfer; heme; heterodimer; oxidoreductase; !1respiratory chain; transmembrane protein FEATURE !$9-25 #domain transmembrane #status predicted #label TM1\ !$62-78 #domain transmembrane #status predicted #label TM2\ !$83-99 #domain transmembrane #status predicted #label TM3\ !$122-138 #domain transmembrane #status predicted #label TM4\ !$165-181 #domain transmembrane #status predicted #label TM5\ !$206-222 #domain transmembrane #status predicted #label TM6\ !$264-280 #domain transmembrane #status predicted #label TM7\ !$299-315 #domain transmembrane #status predicted #label TM8\ !$337-353 #domain transmembrane #status predicted #label TM9 SUMMARY #length 379 #molecular-weight 42453 #checksum 6292 SEQUENCE /// ENTRY B69611 #type complete TITLE cytochrome d ubiquinol oxidase (EC 1.10.3.-) chain II cydB - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS B69611 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69611 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-338 ##label KUN !'##cross-references GB:Z99123; GB:AL009126; NID:g2636240; !1PIDN:CAB15901.1; PID:g2636410 !'##experimental_source strain 168 GENETICS !$#gene cydB CLASSIFICATION #superfamily cytochrome d ubiquinol oxidase KEYWORDS oxidoreductase SUMMARY #length 338 #molecular-weight 37861 #checksum 3202 SEQUENCE /// ENTRY S53828 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain 1/2 [validated] - Acanthamoeba castellanii mitochondrion ORGANISM #formal_name mitochondrion Acanthamoeba castellanii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 08-Sep-2000 ACCESSIONS S53828; S68552 REFERENCE S53825 !$#authors Burger, G.; Plante, I.; Lonergan, K.M.; Gray, M.W. !$#journal J. Mol. Biol. (1995) 245:522-537 !$#title The mitochondrial DNA of the amoeboid protozoon, !1Acanthamoeba castellanii: complete sequence, gene content !1and genome organization. !$#cross-references MUID:95147275; PMID:7844823 !$#accession S53828 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-873 ##label BUR !'##cross-references GB:U12386; NID:g562028; PIDN:AAD11820.1; !1PID:g562032 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1994 REFERENCE S68552 !$#authors Lonergan, K.M.; Gray, M.W. !$#journal J. Mol. Biol. (1996) 257:1019-1030 !$#title Expression of a continuous open reading frame encoding !1subunits 1 and 2 of cytochrome c oxidase in the !1mitochondrial DNA of Acanthamoeba castellanii. !$#cross-references MUID:96192086; PMID:8632465 !$#accession S68552 !'##molecule_type DNA !'##residues 1-873 ##label LON !'##cross-references GB:U12386; NID:g562028; PIDN:AAD11820.1; !1PID:g562032 !'##experimental_source ATCC 30010 GENETICS !$#gene cox1/2 !$#genome mitochondrion !$#genetic_code SGC6 CLASSIFICATION #superfamily Acanthamoeba cytochrome-c oxidase chain I/II; !1cytochrome-c oxidase chain I homology; cytochrome-c oxidase !1chain II homology KEYWORDS chromoprotein; copper; electron transfer; heme; iron; !1magnesium; membrane-associated complex; metalloprotein; !1mitochondrion; oxidative phosphorylation; oxidoreductase; !1respiratory chain; transmembrane protein FEATURE !$23-470 #domain cytochrome-c oxidase chain I homology #label !8CO1\ !$568-854 #domain cytochrome-c oxidase chain II homology #label !8CO2\ !$75,391 #binding_site heme a iron (His) (axial ligands) !8#status predicted\ !$254,303,304 #binding_site copper (His) (B site) #status !8predicted\ !$254-258 #cross-link 1'-histidyl-3'-tyrosine (His-Tyr) #status !8predicted\ !$258 #binding_site oxygen (Tyr) #status predicted\ !$381,838 #binding_site magnesium (His, Glu) #status predicted\ !$389 #binding_site heme a3 iron (His) (axial ligand) !8#status predicted\ !$801,836,840,847 #binding_site copper 1 (His, Cys, Cys, Met) (A site) !8#status predicted\ !$836,838,840,844 #binding_site copper 2 (Cys, Glu, Cys, His) (A site) !8#status predicted SUMMARY #length 873 #molecular-weight 99213 #checksum 9073 SEQUENCE /// ENTRY A49872 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain II - Trypanosoma cruzi mitochondrion (strain Tulahuen) ORGANISM #formal_name mitochondrion Trypanosoma cruzi DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jan-2000 ACCESSIONS A49872 REFERENCE A49872 !$#authors Kim, K.S.; Teixeira, S.M.R.; Kirchhoff, L.V.; Donelson, J.E. !$#journal J. Biol. Chem. (1994) 269:1206-1211 !$#title Transcription and editing of cytochrome oxidase II RNAs in !1Trypanosoma cruzi. !$#cross-references MUID:94117429; PMID:8288582 !$#accession A49872 !'##status preliminary !'##molecule_type mRNA !'##residues 1-210 ##label KIM !'##cross-references GB:L22643; NID:g349146; PIDN:AAA16806.1; !1PID:g349147 GENETICS !$#gene COII !$#genome mitochondrion !$#genetic_code SGC6 CLASSIFICATION #superfamily cytochrome-c oxidase chain II; cytochrome-c !1oxidase chain II homology KEYWORDS copper; electron transfer; membrane-associated complex; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain; RNA !1editing; transmembrane protein FEATURE !$7-210 #domain cytochrome-c oxidase chain II homology #label !8CO2\ !$157,192,196,203 #binding_site copper 1 (His, Cys, Cys, Met) #status !8predicted\ !$192,194,196,200 #binding_site copper 2 (Cys, Glu, Cys, His) #status !8predicted\ !$194 #binding_site magnesium (Glu) (shared with chain I) !8#status predicted SUMMARY #length 210 #molecular-weight 24145 #checksum 1856 SEQUENCE /// ENTRY OBUTMB #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain II - Trypanosoma brucei mitochondrion ORGANISM #formal_name mitochondrion Trypanosoma brucei DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 11-May-2000 ACCESSIONS A00477 REFERENCE A93537 !$#authors Hensgens, L.A.M.; Brakenhoff, J.; De Vries, B.F.; Sloof, P.; !1Tromp, M.C.; Van Boom, J.H.; Benne, R. !$#journal Nucleic Acids Res. (1984) 12:7327-7344 !$#title The sequence of the gene for cytochrome c oxidase subunit I, !1a frameshift containing gene for cytochrome c oxidase !1subunit II and seven unassigned reading frames in !1Trypanosoma brucei mitochondrial maxi-circle DNA. !$#cross-references MUID:85037915; PMID:6093040 !$#accession A00477 !'##molecule_type DNA !'##residues 1-209 ##label HEN !'##cross-references GB:M94286; NID:g343546 !'##note this translation is not annotated in GenBank entry TRBKPGEN, !1release 109.0 COMMENT The DNA sequence is from a segment of the 20-kb maxicircle, !1which is believed to be the trypanosome mitochondrial !1genome. GENETICS !$#gene coxII !$#genome mitochondrion !$#genetic_code SGC6 CLASSIFICATION #superfamily cytochrome-c oxidase chain II; cytochrome-c !1oxidase chain II homology KEYWORDS copper; electron transfer; membrane-associated complex; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$7-209 #domain cytochrome-c oxidase chain II homology #label !8CO2\ !$157,191,195,202 #binding_site copper 1 (His, Cys, Cys, Met) #status !8predicted\ !$191,193,195,199 #binding_site copper 2 (Cys, Glu, Cys, His) #status !8predicted\ !$193 #binding_site magnesium (Glu) (shared with chain I) !8#status predicted SUMMARY #length 209 #molecular-weight 24132 #checksum 8937 SEQUENCE /// ENTRY I22848 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain II - Leishmania tarentolae mitochondrion ORGANISM #formal_name mitochondrion Leishmania tarentolae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 07-Dec-1999 ACCESSIONS I22848 REFERENCE A22848 !$#authors de la Cruz, V.F.; Neckelmann, N.; Simpson, L. !$#journal J. Biol. Chem. (1984) 259:15136-15147 !$#title Sequences of six genes and several open reading frames in !1the kinetoplast maxicircle DNA of Leishmania tarentolae. !$#cross-references MUID:85079995; PMID:6096360 !$#accession I22848 !'##molecule_type DNA !'##residues 1-176 ##label DEL !'##cross-references GB:M10126 GENETICS !$#genome mitochondrion !$#genetic_code SGC6 CLASSIFICATION #superfamily cytochrome-c oxidase chain II; cytochrome-c !1oxidase chain II homology KEYWORDS copper; electron transfer; heme; membrane-associated !1complex; mitochondrial inner membrane; mitochondrion; !1oxidative phosphorylation; oxidoreductase; respiratory !1chain; transmembrane protein SUMMARY #length 176 #molecular-weight 20315 #checksum 4015 SEQUENCE /// ENTRY OBHU2 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain II - human mitochondrion ORGANISM #formal_name mitochondrion Homo sapiens #common_name man DATE 30-Nov-1980 #sequence_revision 23-Oct-1981 #text_change 31-Mar-2000 ACCESSIONS A00472; I58025; S05493; I38732; I38735; I59384 REFERENCE A00151 !$#authors Anderson, S.; Bankier, A.T.; Barrell, B.G.; de Bruijn, !1M.H.L.; Coulson, A.R.; Drouin, J.; Eperon, I.C.; Nierlich, !1D.P.; Roe, B.A.; Sanger, F.; Schreier, P.H.; Smith, A.J.H.; !1Staden, R.; Young, I.G. !$#journal Nature (1981) 290:457-465 !$#title Sequence and organization of the human mitochondrial genome. !$#cross-references MUID:81173052; PMID:7219534 !$#accession A00472 !'##molecule_type DNA !'##residues 1-227 ##label AND !'##cross-references GB:J01415; NID:g1944628; PIDN:AAB58946.1; !1PID:g337192; EMBL:V00662; NID:g13003; PID:g13007; !1GSPDB:GN00100 REFERENCE I58025 !$#authors Barrell, B.G.; Bankier, A.T.; Drouin, J. !$#journal Nature (1979) 282:189-194 !$#title A different genetic code in human mitochondria. !$#cross-references MUID:80032938; PMID:226894 !$#accession I58025 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-227 ##label BAR !'##cross-references GB:M25171; NID:g337186; PIDN:AAA31850.1; !1PID:g337187 REFERENCE S05493 !$#authors Power, M.D.; Kiefer, M.C.; Barr, P.J.; Reeves, R. !$#journal Nucleic Acids Res. (1989) 17:6734 !$#title Nucleotide sequence of human mitochondrial cytochrome c !1oxidase II cDNA. !$#cross-references MUID:89386008; PMID:2550900 !$#accession S05493 !'##molecule_type mRNA !'##residues 1-227 ##label POW !'##cross-references EMBL:X15759; NID:g12583; PIDN:CAA33766.1; !1PID:g12584 !'##note the authors translated the codon TAC for residue 105 as Thr REFERENCE I38732 !$#authors Ruvolo, M.; Zehr, S.; von Dornum, M.; Pan, D.; Chang, B.; !1Lin, J. !$#journal Mol. Biol. Evol. (1993) 10:1115-1135 !$#title Mitochondrial COII sequences and modern human origins. !$#cross-references MUID:94104475; PMID:8277847 !$#accession I38732 !'##status translation not shown !'##molecule_type DNA !'##residues 1-227 ##label RES !'##cross-references EMBL:U12690; NID:g530068; PIDN:AAA20843.1; !1PID:g530069; EMBL:U12691; NID:g530070; PID:g530071; !1EMBL:U12692; NID:g530072; PID:g530073; EMBL:U12694; !1NID:g530076; PID:g530077 !'##experimental_source Hsa2, Asian, Taiwan; Hsa3, Mbuti pygmy, Zaire; !1Hsa4, Biaka pygmy, Central African Republic; Hsa6, !Kung, !1Republic of South African !$#accession I38735 !'##status translation not shown !'##molecule_type DNA !'##residues 1-29,'V',31-147,'T',149-227 ##label RE2 !'##cross-references EMBL:U12693; NID:g530074; PIDN:AAA20846.1; !1PID:g530075 !'##experimental_source Hsa5, Biaka pygmy, Central African Republic REFERENCE I59384 !$#authors Horai, S.; Hayasaka, K.; Kondo, R.; Tsugane, K.; Takahata, !1N. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1995) 92:532-536 !$#title Recent African origin of modern humans revealed by complete !1sequences of hominoid mitochondrial DNAs. !$#cross-references MUID:95132634; PMID:7530363 !$#accession I59384 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-227 ##label RE3 !'##cross-references GB:D38112; NID:g644480; PIDN:BAA07293.1; !1PID:g704444 GENETICS !$#gene GDB:MTCO2 !'##cross-references GDB:118901; OMIM:516040 !$#map_position MTH7586-8262 !$#genome mitochondrion !$#genetic_code SGC1 COMPLEX part of a 13 chain complex spanning the inner mitochondrial !1membrane and consisting of one each of chains I (see !1PIR:ODHU1), II, III (see PIR:OTHU3), IV (see PIR:OLHU4), Va !1(see PIR:OTHU5A), Vb (see PIR:OTHU5B), VIa (see PIR:OGHU6A), !1VIb (see PIR:OGHU6B), VIc (see PIR:OGHU6C), VIIa (see !1PIR:OSHU7A), VIIb (see PIR:OSHU7B), VIIc (see PIR:OSHU7C), !1VIII (see PIR:OSHU8); the complex may form dimers within the !1mitochondrial inner-membrane FUNCTION !$#description the cytochrome-c oxidase complex catalyzes the oxidation of !1four molecules of reduced cytochrome c in the intracristal !1(or intermembrane) space using one oxygen molecule and four !1protons from the mitochondrial matrix producing two !1molecules of water and lowering the concentration of protons !1in the mitochondrial matrix !$#pathway oxidative phosphorylation; respiratory chain !$#note chain II directly oxidizes cytochrome c on the intracristal !1side of the inner-membrane; two copper atoms are bound at !1what is referred to as the copper A site CLASSIFICATION #superfamily cytochrome-c oxidase chain II; cytochrome-c !1oxidase chain II homology KEYWORDS copper; electron transfer; magnesium; membrane-associated !1complex; metalloprotein; mitochondrial inner membrane; !1mitochondrion; oxidative phosphorylation; oxidoreductase; !1respiratory chain; transmembrane protein FEATURE !$9-214 #domain cytochrome-c oxidase chain II homology #label !8CO2\ !$15-35 #domain transmembrane helix #status predicted #label !8TR01\ !$60-87 #domain transmembrane helix #status predicted #label !8TR02\ !$1 #modified_site N-formylmethionine #status predicted\ !$161,196,200,207 #binding_site copper 1 (His, Cys, Cys, Met) #status !8predicted\ !$196,198,200,204 #binding_site copper 2 (Cys, Glu, Cys, His) #status !8predicted\ !$198 #binding_site magnesium (Glu) (shared with chain I) !8#status predicted SUMMARY #length 227 #molecular-weight 25565 #checksum 4983 SEQUENCE /// ENTRY OBMS2 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain II - mouse mitochondrion ORGANISM #formal_name mitochondrion Mus musculus #common_name house mouse DATE 02-Apr-1982 #sequence_revision 02-Apr-1982 #text_change 07-Dec-1999 ACCESSIONS A00474; I57011 REFERENCE A00153 !$#authors Bibb, M.J.; Van Etten, R.A.; Wright, C.T.; Walberg, M.W.; !1Clayton, D.A. !$#journal Cell (1981) 26:167-180 !$#title Sequence and gene organization of mouse mitochondrial DNA. !$#cross-references MUID:82137051; PMID:7332926 !$#accession A00474 !'##molecule_type DNA !'##residues 1-227 ##label BIB !'##cross-references GB:J01420; NID:g342520; PIDN:AAB48647.1; !1PID:g342522; EMBL:V00711; NID:g13838; PID:g13842 !'##note the nucleotide sequence corresponding to residue 1 is ATAA, !1which was not translated by the authors REFERENCE I57011 !$#authors Nelson, I.; Gerasimov, S.; Marsac, C.; Lestienne, P.; !1Boursot, P. !$#journal Mamm. Genome (1993) 4:680-683 !$#title Sequence analysis of a deleted mitochondrial DNA molecule in !1heteroplasmic mice. !$#cross-references MUID:94108239; PMID:8281018 !$#accession I57011 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 57-63 ##label RES !'##cross-references GB:S68119; NID:g544777 GENETICS !$#gene coII !$#map_position 43.0-47.2 !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily cytochrome-c oxidase chain II; cytochrome-c !1oxidase chain II homology KEYWORDS copper; electron transfer; membrane-associated complex; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$9-214 #domain cytochrome-c oxidase chain II homology #label !8CO2\ !$161,196,200,207 #binding_site copper 1 (His, Cys, Cys, Met) #status !8predicted\ !$196,198,200,204 #binding_site copper 2 (Cys, Glu, Cys, His) #status !8predicted\ !$198 #binding_site magnesium (Glu) (shared with chain I) !8#status predicted SUMMARY #length 227 #molecular-weight 25976 #checksum 9405 SEQUENCE /// ENTRY OBRT2 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain II - rat mitochondrion ALTERNATE_NAMES gene C1-13 protein [misidentification] ORGANISM #formal_name mitochondrion Rattus norvegicus #common_name Norway rat DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 04-Feb-2000 ACCESSIONS A93914; S04750; I52411; I73678; A00474 REFERENCE A93914 !$#authors Brown, G.G.; Simpson, M.V. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:3246-3250 !$#title Novel features of animal mtDNA evolution as shown by !1sequences of two rat cytochrome oxidase subunit II genes. !$#cross-references MUID:82247832; PMID:6285344 !$#accession A93914 !'##molecule_type DNA !'##residues 1-227 ##label BRO !'##cross-references GB:J01435 REFERENCE S04747 !$#authors Gadaleta, G.; Pepe, G.; De Candia, G.; Quagliariello, C.; !1Sbisa, E.; Saccone, C. !$#journal J. Mol. Evol. (1989) 28:497-516 !$#title The complete nucleotide sequence of the Rattus norvegicus !1mitochondrial genome: cryptic signals revealed by !1comparative analysis between vertebrates. !$#cross-references MUID:89362487; PMID:2504926 !$#accession S04750 !'##molecule_type DNA !'##residues 1-227 ##label GAD !'##cross-references EMBL:X14848; NID:g854269; PIDN:CAA32957.1; !1PID:g13481 REFERENCE I52411 !$#authors Cao, J.L.; Revzin, A.; Ferguson-Miller, S. !$#journal Biochemistry (1991) 30:2642-2650 !$#title Conversion of a mitochondrial gene for mammalian cytochrome !1c oxidase subunit II into its universal codon equivalent and !1expression in vivo and in vitro. !$#cross-references MUID:91159394; PMID:1848093 !$#accession I52411 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-58,'H',60-129,'L',131-163,'P',165-178,'P',180-188,'L', !1190-207,'L',209-227 ##label RES !'##cross-references GB:M64496; NID:g343166; PIDN:AAA67314.1; !1PID:g829018 REFERENCE I56602 !$#authors Law, S.W.; Apostolakis, E.M.; Samora, P.J.; O'Malley, B.W.; !1Clark, J.H. !$#journal J. Steroid Biochem. Mol. Biol. (1994) 51:131-136 !$#title Hormonal regulation of hypothalamic gene expression: !1identification of multiple novel estrogen induced genes. !$#cross-references MUID:95071919; PMID:7981121 !$#accession I73678 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 7-16,'I',18-28,'I',30-44,'I',46-55,'I' ##label LAW !'##cross-references GB:S74342; NID:g786415 !'##note the authors' translation used the standard genetic code rather !1than SGC1 GENETICS !$#gene coII !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily cytochrome-c oxidase chain II; cytochrome-c !1oxidase chain II homology KEYWORDS copper; electron transfer; membrane-associated complex; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$9-214 #domain cytochrome-c oxidase chain II homology #label !8CO2\ !$15-35 #domain transmembrane helix #status predicted #label !8TR01\ !$60-87 #domain transmembrane helix #status predicted #label !8TR02\ !$161,196,200,207 #binding_site copper 1 (His, Cys, Cys, Met) #status !8predicted\ !$196,198,200,204 #binding_site copper 2 (Cys, Glu, Cys, His) #status !8predicted\ !$198 #binding_site magnesium (Glu) (shared with chain I) !8#status predicted SUMMARY #length 227 #molecular-weight 25942 #checksum 8871 SEQUENCE /// ENTRY OBRT2B #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain II - black rat mitochondrion ORGANISM #formal_name mitochondrion Rattus rattus #common_name black rat, roof rat #note this sequence is derived from an apparently genuine specimen of this problematically identified species DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jun-2000 ACCESSIONS B93914; A00474 REFERENCE A93914 !$#authors Brown, G.G.; Simpson, M.V. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:3246-3250 !$#title Novel features of animal mtDNA evolution as shown by !1sequences of two rat cytochrome oxidase subunit II genes. !$#cross-references MUID:82247832; PMID:6285344 !$#accession B93914 !'##molecule_type DNA !'##residues 1-227 ##label BRO !'##cross-references GB:J01434; NID:g343170; PIDN:AAA67374.1; !1PID:g829021 GENETICS !$#gene coII !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily cytochrome-c oxidase chain II; cytochrome-c !1oxidase chain II homology KEYWORDS copper; electron transfer; membrane-associated complex; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$9-214 #domain cytochrome-c oxidase chain II homology #label !8CO2\ !$161,196,200,207 #binding_site copper 1 (His, Cys, Cys, Met) #status !8predicted\ !$196,198,200,204 #binding_site copper 2 (Cys, Glu, Cys, His) #status !8predicted\ !$198 #binding_site magnesium (Glu) (shared with chain I) !8#status predicted SUMMARY #length 227 #molecular-weight 25932 #checksum 8588 SEQUENCE /// ENTRY OBBO2 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain II [validated] - bovine mitochondrion ORGANISM #formal_name mitochondrion Bos primigenius taurus #common_name cattle DATE 31-Aug-1979 #sequence_revision 23-Oct-1981 #text_change 15-Sep-2000 ACCESSIONS B00152; A91476; A91686; A00473 REFERENCE A00152 !$#authors Anderson, S.; de Bruijn, M.H.L.; Coulson, A.R.; Eperon, !1I.C.; Sanger, F.; Young, I.G. !$#journal J. Mol. Biol. (1982) 156:683-717 !$#title Complete sequence of bovine mitochondrial DNA. Conserved !1features of the mammalian mitochondrial genome. !$#cross-references MUID:83010260; PMID:7120390 !$#accession B00152 !'##molecule_type DNA !'##residues 1-227 ##label AND !'##cross-references GB:J01394; NID:g336430; PIDN:AAB59271.1; !1PID:g336434; EMBL:V00654; NID:g12800; PID:g12804 REFERENCE A91476 !$#authors Young, I.G.; Anderson, S. !$#journal Gene (1980) 12:257-265 !$#title The genetic code in bovine mitochondria: sequence of genes !1for the cytochrome oxidase subunit II and two tRNAs. !$#cross-references MUID:81237788; PMID:6265319 !$#accession A91476 !'##molecule_type DNA !'##residues 1-227 ##label YOU !'##cross-references GB:M10544 REFERENCE A91686 !$#authors Steffens, G.J.; Buse, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1979) 360:613-619 !$#title Studies on cytochrome c oxidase, IV[1-3]. Primary structure !1and function of subunit II. !$#cross-references MUID:79171281; PMID:220175 !$#accession A91686 !'##molecule_type protein !'##residues 1-227 ##label STE !'##experimental_source heart REFERENCE A67451 !$#authors Tsukihara, T.; Aoyama, H.; Yamashita, E.; Tomizaki, T.; !1Yamaguchi, H.; Shinzawa-itoh, K.; Nakashima, R.; Yaono, R.; !1Yoshikawa, S. !$#submission submitted to the Brookhaven Protein Data Bank, April 1996 !$#cross-references PDB:1OCC !$#contents annotation; X-ray crystallography, 2.8 angstroms, residues !11-227 REFERENCE A57981 !$#authors Tsukihara, T.; Aoyama, H.; Yamashita, E.; Tomizaki, T.; !1Yamaguchi, H.; Sinzawa-Itoh, K.; Nakashima, R.; Yaono, R.; !1Yoshikawa, S. !$#journal Science (1996) 272:1136-1144 !$#title The whole structure of the 13-subunit oxidized cytochrome c !1oxidase at 2.8 angstroms. !$#cross-references MUID:96216288; PMID:8638158 !$#contents annotation; X-ray crystallography, 2.8 angstroms GENETICS !$#gene coII !$#genome mitochondrion !$#genetic_code SGC1 COMPLEX part of a 13 chain complex spanning the inner mitochondrial !1membrane and consisting of one each of chains I (see !1PIR:ODBO1), II, III (see PIR:OTBO3), IV (see PIR:OLBO4), Va !1(see PIR:CABO), Vb (see PIR:OGBO6A), VIa (see PIR:OGBO6), !1VIb (see PIR:OGBO7), VIc (see PIR:OGBO6C), VIIa (see !1PIR:OSBO7A), VIIb (see PIR:OSBO7B), VIIc (see PIR:OSBO8A), !1VIII (see PIR:OSBO8); the complex may form dimers within the !1mitochondrial inner-membrane FUNCTION !$#description the cytochrome-c oxidase complex catalyzes the oxidation of !1four molecules of reduced cytochrome c in the intracristal !1(or intermembrane) space using one oxygen molecule and four !1protons from the mitochondrial matrix producing two !1molecules of water and lowering the concentration of protons !1in the mitochondrial matrix !$#pathway oxidative phosphorylation; respiratory chain !$#note chain II directly oxidizes cytochrome c on the intracristal !1side of the inner-membrane; two copper atoms are bound at !1what is referred to as the copper A site CLASSIFICATION #superfamily cytochrome-c oxidase chain II; cytochrome-c !1oxidase chain II homology KEYWORDS copper; electron transfer; magnesium; membrane-associated !1complex; metalloprotein; mitochondrial inner membrane; !1mitochondrion; oxidative phosphorylation; oxidoreductase; !1respiratory chain; transmembrane protein FEATURE !$1-14 #domain intracristal #status experimental #label !8ITC1\ !$9-214 #domain cytochrome-c oxidase chain II homology #label !8CO2\ !$15-35 #domain transmembrane helix #status experimental !8#label TR01\ !$36-59 #domain mitochondrial matrix #status experimental !8#label MM1\ !$60-87 #domain transmembrane helix #status experimental !8#label TR02\ !$88-227 #domain intracristal #status experimental #label !8ITC2\ !$1 #modified_site N-formylmethionine #status !8experimental\ !$161,196,200,207 #binding_site copper 1 (His, Cys, Cys, Met) #status !8experimental\ !$196,198,200,204 #binding_site copper 2 (Cys, Glu, Cys, His) #status !8experimental\ !$198 #binding_site magnesium (Glu) (shared with chain I) !8#status experimental SUMMARY #length 227 #molecular-weight 26021 #checksum 173 SEQUENCE /// ENTRY OBXL2 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain II - African clawed frog mitochondrion ALTERNATE_NAMES cytochrome a3 polypeptide II; cytochrome aa3 polypeptide II ORGANISM #formal_name mitochondrion Xenopus laevis #common_name African clawed frog DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 07-Dec-1999 ACCESSIONS A00475 REFERENCE A00155 !$#authors Roe, B.A.; Ma, D.P.; Wilson, R.K.; Wong, J.F.H. !$#journal J. Biol. Chem. (1985) 260:9759-9774 !$#title The complete nucleotide sequence of the Xenopus laevis !1mitochondrial genome. !$#cross-references MUID:85261388; PMID:4019494 !$#accession A00475 !'##molecule_type DNA !'##residues 1-229 ##label ROE !'##cross-references GB:M10217; GB:X01600; GB:X01601; GB:X02890; !1NID:g343717; PIDN:AAA66461.1; PID:g807686 GENETICS !$#gene coII !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily cytochrome-c oxidase chain II; cytochrome-c !1oxidase chain II homology KEYWORDS copper; electron transfer; membrane-associated complex; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$9-214 #domain cytochrome-c oxidase chain II homology #label !8CO2\ !$161,196,200,207 #binding_site copper 1 (His, Cys, Cys, Met) #status !8predicted\ !$196,198,200,204 #binding_site copper 2 (Cys, Glu, Cys, His) #status !8predicted\ !$198 #binding_site magnesium (Glu) (shared with chain I) !8#status predicted SUMMARY #length 229 #molecular-weight 25956 #checksum 1874 SEQUENCE /// ENTRY OBFF2 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain II - fruit fly (Drosophila melanogaster) mitochondrion ORGANISM #formal_name mitochondrion Drosophila melanogaster DATE 18-Apr-1984 #sequence_revision 18-Apr-1984 #text_change 07-Dec-1999 ACCESSIONS A00476 REFERENCE A93307 !$#authors de Bruijn, M.H.L. !$#journal Nature (1983) 304:234-241 !$#title Drosophila melanogaster mitochondrial DNA, a novel !1organization and genetic code. !$#cross-references MUID:83245048; PMID:6408489 !$#accession A00476 !'##molecule_type DNA !'##residues 1-228 ##label DEB !'##cross-references GB:J01404; GB:J01405; GB:J01407; NID:g336811; !1PIDN:AAB59240.1; PID:g895683 GENETICS !$#gene coII !'##cross-references FlyBase:FBgn0013675 !$#genome mitochondrion !$#genetic_code SGC4 CLASSIFICATION #superfamily cytochrome-c oxidase chain II; cytochrome-c !1oxidase chain II homology KEYWORDS copper; electron transfer; membrane-associated complex; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$9-214 #domain cytochrome-c oxidase chain II homology #label !8CO2\ !$161,196,200,207 #binding_site copper 1 (His, Cys, Cys, Met) #status !8predicted\ !$196,198,200,204 #binding_site copper 2 (Cys, Glu, Cys, His) #status !8predicted\ !$198 #binding_site magnesium (Glu) (shared with chain I) !8#status predicted SUMMARY #length 228 #molecular-weight 26190 #checksum 1900 SEQUENCE /// ENTRY OBFF2Y #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain II - fruit fly (Drosophila yakuba) mitochondrion ORGANISM #formal_name mitochondrion Drosophila yakuba DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 07-Dec-1999 ACCESSIONS A93477; C25797; A00476 REFERENCE A93477 !$#authors Clary, D.O.; Wolstenholme, D.R. !$#journal Nucleic Acids Res. (1983) 11:4211-4227 !$#title Nucleotide sequence of a segment of Drosophila mitochondrial !1DNA that contains the genes for cytochrome c oxidase !1subunits II and III and ATPase subunit 6. !$#cross-references MUID:83246544; PMID:6306579 !$#accession A93477 !'##molecule_type DNA !'##residues 1-228 ##label CLA !'##cross-references GB:X03240; NID:g12923; PIDN:CAA26987.1; PID:g12926; !1GB:X00924; NID:g12918; PID:g12919 !'##note the authors translated the codon AGA for residues 12 and 225 as !1Arg REFERENCE A92962 !$#authors Clary, D.O.; Wolstenholme, D.R. !$#journal J. Mol. Evol. (1985) 22:252-271 !$#title The mitochondrial DNA molecule of Drosophila yakuba: !1nucleotide sequence, gene organization, and genetic code. !$#cross-references MUID:86089137; PMID:3001325 !$#accession C25797 !'##molecule_type DNA !'##residues 1-228 ##label CL2 !'##cross-references GB:X03240; GB:J01400; GB:J01402; GB:J01403; !1GB:J01406; GB:J01408; GB:V01521; GB:X00563; NID:g12923; !1PIDN:CAA26987.1; PID:g12926 GENETICS !$#gene coII !'##cross-references FlyBase:FBgn0013180 !$#genome mitochondrion !$#genetic_code SGC4 !$#start_codon ATA CLASSIFICATION #superfamily cytochrome-c oxidase chain II; cytochrome-c !1oxidase chain II homology KEYWORDS copper; electron transfer; membrane-associated complex; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$9-214 #domain cytochrome-c oxidase chain II homology #label !8CO2\ !$161,196,200,207 #binding_site copper 1 (His, Cys, Cys, Met) #status !8predicted\ !$196,198,200,204 #binding_site copper 2 (Cys, Glu, Cys, His) #status !8predicted\ !$198 #binding_site magnesium (Glu) (shared with chain I) !8#status predicted SUMMARY #length 228 #molecular-weight 26107 #checksum 650 SEQUENCE /// ENTRY OBBY2 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain II precursor - yeast (Saccharomyces cerevisiae) mitochondrion ALTERNATE_NAMES protein Q0250 ORGANISM #formal_name mitochondrion Saccharomyces cerevisiae DATE 28-Feb-1980 #sequence_revision 19-Feb-1984 #text_change 19-Apr-2002 ACCESSIONS A00478; A93838; S59345; S78682; S78683 REFERENCE A92261 !$#authors Coruzzi, G.; Tzagoloff, A. !$#journal J. Biol. Chem. (1979) 254:9324-9330 !$#title Assembly of the mitochondrial membrane system. DNA sequence !1of subunit 2 of yeast cytochrome oxidase. !$#cross-references MUID:80006652; PMID:225327 !$#accession A00478 !'##molecule_type DNA !'##residues 1-251 ##label COR !'##cross-references GB:J01481 !'##experimental_source strain DS200/A1 !'##note the authors translated the codon ATA for residues 63, 115, and !1167 according to the standard code REFERENCE A93838 !$#authors Fox, T.D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1979) 76:6534-6538 !$#title Five TGA "stop" codons occur within the translated sequence !1of the yeast mitochondrial gene for cytochrome c oxidase !1subunit II. !$#cross-references MUID:80101645; PMID:230513 !$#accession A93838 !'##molecule_type DNA !'##residues 1-251 ##label FOX !'##cross-references EMBL:V00685; NID:g13511; PIDN:CAA24056.1; !1PID:g13512 !'##experimental_source strain D273-10B, ATCC 25657 !'##note the authors translated the codon ATA for residues 63, 115, and !1167 according to the standard code REFERENCE S59345 !$#authors Nakagawa, Y. !$#submission submitted to the EMBL Data Library, June 1995 !$#description Amplification and sequencing of cytochrome c oxidase subunit !1II gene for phylogenetic analysis of yeast mitochondria. !$#accession S59345 !'##molecule_type DNA !'##residues 46-200 ##label NAK !'##cross-references EMBL:D55725; NID:g1001842; PIDN:BAA09539.1; !1PID:g2160325 REFERENCE S78634 !$#authors Foury, F.; Roganti, T.; Lecrenier, N.; Purnelle, B. !$#submission submitted to the Protein Sequence Database, December 1998 !$#accession S78682 !'##molecule_type DNA !'##residues 1-251 ##label FOU1 !'##cross-references EMBL:AJ011856; MIPS:Q0250 !'##experimental_source strain FY1679, isogenic derivative of strain !1S288C REFERENCE Z13743 !$#authors Foury, F.; Roganti, T.; Lecrenier, N.; Purnelle, B. !$#journal FEBS Lett. (1998) 440:325-331 !$#title The complete sequence of the mitochondrial genome of !1Saccharomyces cerevisiae. !$#cross-references MUID:99087401; PMID:9872396 !$#accession S78683 !'##molecule_type DNA !'##residues 1-251 ##label FOU2 !'##cross-references EMBL:AJ011856; NID:g4160362; PIDN:CAA09845.1; !1PID:g4160387 !'##experimental_source strain FY1679, isogenic derivative of strain !1S288C GENETICS !$#gene SGD:COX2; cox2; oxi1 !'##cross-references SGD:S0007281 !$#map_position 13.8-15.0 !$#genome mitochondrion !$#genetic_code SGC2 CLASSIFICATION #superfamily cytochrome-c oxidase chain II; cytochrome-c !1oxidase chain II homology KEYWORDS copper; electron transfer; membrane-associated complex; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$1-15 #domain propeptide #status predicted #label PRO\ !$16-251 #product cytochrome-c oxidase chain II #status !8predicted #label MAT\ !$25-239 #domain cytochrome-c oxidase chain II homology #label !8CO2\ !$47-63 #domain transmembrane #status predicted #label TM1\ !$91-107 #domain transmembrane #status predicted #label TM2\ !$186,221,225,232 #binding_site copper 1 (His, Cys, Cys, Met) #status !8predicted\ !$221,223,225,229 #binding_site copper 2 (Cys, Glu, Cys, His) #status !8predicted\ !$223 #binding_site magnesium (Glu) (shared with chain I) !8#status predicted SUMMARY #length 251 #molecular-weight 28567 #checksum 6195 SEQUENCE /// ENTRY OBVK2M #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain II precursor - yeast (Kluyveromyces marxianus var. lactis) mitochondrion ORGANISM #formal_name mitochondrion Kluyveromyces marxianus var. lactis, Candida sphaerica DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 07-Dec-1999 ACCESSIONS S11171 REFERENCE S11171 !$#authors Hardy, C.M.; Clark-Walker, G.D. !$#journal Yeast (1990) 6:403-410 !$#title Nucleotide sequence of the cytochrome oxidase subunit 2 and !1val-tRNA genes and surrounding sequences from Kluyveromyces !1lactis K8 mitochondrial DNA. !$#cross-references MUID:91021490; PMID:2171241 !$#accession S11171 !'##molecule_type DNA !'##residues 1-247 ##label HAR !'##cross-references EMBL:X15999; NID:g13025; PIDN:CAA34129.1; !1PID:g13026 GENETICS !$#gene cox2 !$#genome mitochondrion !$#genetic_code SGC2 CLASSIFICATION #superfamily cytochrome-c oxidase chain II; cytochrome-c !1oxidase chain II homology KEYWORDS copper; electron transfer; membrane-associated complex; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$12-247 #product cytochrome-c oxidase chain II #status !8predicted #label MAT\ !$21-235 #domain cytochrome-c oxidase chain II homology #label !8CO2\ !$39-59 #domain transmembrane #status predicted #label TM1\ !$79-101 #domain transmembrane #status predicted #label TM2\ !$182,217,221,228 #binding_site copper 1 (His, Cys, Cys, Met) #status !8predicted\ !$217,219,221,225 #binding_site copper 2 (Cys, Glu, Cys, His) #status !8predicted\ !$219 #binding_site magnesium (Glu) (shared with chain I) !8#status predicted SUMMARY #length 247 #molecular-weight 28048 #checksum 7875 SEQUENCE /// ENTRY OBHQMS #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain II - yeast (Hansenula saturnus) mitochondrion ORGANISM #formal_name mitochondrion Hansenula saturnus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 07-Dec-1999 ACCESSIONS S07165 REFERENCE S07165 !$#authors Lawson, J.E.; Deters, D.W. !$#journal Curr. Genet. (1985) 9:351-360 !$#title Nucleotide sequence of the mitochondrial cytochrome oxidase !1subunit II gene in the yeast Hansenula saturnus. !$#cross-references MUID:88223501; PMID:2836090 !$#accession S07165 !'##molecule_type DNA !'##residues 1-247 ##label LAW !'##cross-references EMBL:X02439; NID:g12594; PIDN:CAA26284.1; !1PID:g12595 !'##note the authors used the standard genetic code in their translation GENETICS !$#gene coxII !$#genome mitochondrion !$#genetic_code SGC2 CLASSIFICATION #superfamily cytochrome-c oxidase chain II; cytochrome-c !1oxidase chain II homology KEYWORDS copper; electron transfer; membrane-associated complex; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$21-235 #domain cytochrome-c oxidase chain II homology #label !8CO2\ !$39-59 #domain transmembrane #status predicted #label TM1\ !$79-101 #domain transmembrane #status predicted #label TM2\ !$182,217,221,228 #binding_site copper 1 (His, Cys, Cys, Met) #status !8predicted\ !$217,219,221,225 #binding_site copper 2 (Cys, Glu, Cys, His) #status !8predicted\ !$219 #binding_site magnesium (Glu) (shared with chain I) !8#status predicted SUMMARY #length 247 #molecular-weight 27927 #checksum 1401 SEQUENCE /// ENTRY OBNC2 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain II - Neurospora crassa mitochondrion ORGANISM #formal_name mitochondrion Neurospora crassa DATE 18-Apr-1984 #sequence_revision 18-Apr-1984 #text_change 07-Dec-1999 ACCESSIONS A00479; S10082; A19032 REFERENCE A00479 !$#authors Macino, G.; Morelli, G. !$#journal J. Biol. Chem. (1983) 258:13230-13235 !$#title Cytochrome oxidase subunit 2 gene in Neurospora crassa !1mitochondria. !$#cross-references MUID:84032555; PMID:6313689 !$#accession A00479 !'##molecule_type DNA !'##residues 1-250 ##label MAC REFERENCE S10081 !$#authors Almasan, A.; Mishra, N.C. !$#journal Genetics (1988) 120:935-945 !$#title Molecular characterization of the mitochondrial DNA of a new !1stopper mutant ER-3 of Neurospora crassa. !$#cross-references MUID:89137935; PMID:2976009 !$#accession S10082 !'##molecule_type DNA !'##residues 1-65 ##label ALM !'##cross-references EMBL:X14681; NID:g14021; PIDN:CAA32813.1; !1PID:g14023 REFERENCE A19032 !$#authors van den Boogaart, P.; van Dijk, S.; Agsteribbe, E. !$#journal FEBS Lett. (1982) 147:97-100 !$#title The mitochondrially made subunit 2 of Neurospora crassa !1cytochrome aa-3 is synthesized as a precursor protein. !$#cross-references MUID:83054012; PMID:6291999 !$#accession A19032 !'##molecule_type DNA !'##residues 1-49,'G',51-54 ##label VAN !'##note the authors translated the codon TAA for residue 33 as Leu GENETICS !$#gene coII; oxi1 !$#genome mitochondrion !$#genetic_code SGC3 CLASSIFICATION #superfamily cytochrome-c oxidase chain II; cytochrome-c !1oxidase chain II homology KEYWORDS copper; electron transfer; membrane-associated complex; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$22-238 #domain cytochrome-c oxidase chain II homology #label !8CO2\ !$185,220,224,231 #binding_site copper 1 (His, Cys, Cys, Met) #status !8predicted\ !$220,222,224,228 #binding_site copper 2 (Cys, Glu, Cys, His) #status !8predicted\ !$222 #binding_site magnesium (Glu) (shared with chain I) !8#status predicted SUMMARY #length 250 #molecular-weight 28724 #checksum 5291 SEQUENCE /// ENTRY OBJJMP #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain II - Podospora anserina mitochondrion ORGANISM #formal_name mitochondrion Podospora anserina DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 07-Dec-1999 ACCESSIONS S09135 REFERENCE S09135 !$#authors Cummings, D.J.; Michel, F.; Domenico, J.M.; McNally, K.L. !$#journal J. Mol. Biol. (1990) 212:287-294 !$#title Mitochondrial DNA sequence analysis of the cytochrome !1oxidase subunit II gene from Podospora anserina. A group IA !1intron with a putative alternative splice site. !$#cross-references MUID:90204556; PMID:2157023 !$#accession S09135 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-250 ##label CUM !'##cross-references GB:X55026; GB:M30937; GB:M61734; NID:g14030; !1PIDN:CAA38803.1; PID:g1334558 !'##note the sequence from Fig. 2 is inconsistent with that from Fig. 1 !1in having 69-Lys GENETICS !$#gene CoII !$#genome mitochondrion !$#genetic_code SGC3 CLASSIFICATION #superfamily cytochrome-c oxidase chain II; cytochrome-c !1oxidase chain II homology KEYWORDS copper; electron transfer; membrane-associated complex; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$22-238 #domain cytochrome-c oxidase chain II homology #label !8CO2\ !$40-60 #domain transmembrane #status predicted #label TM1\ !$82-104 #domain transmembrane #status predicted #label TM2\ !$185,220,224,231 #binding_site copper 1 (His, Cys, Cys, Met) #status !8predicted\ !$220,222,224,228 #binding_site copper 2 (Cys, Glu, Cys, His) #status !8predicted\ !$222 #binding_site magnesium (Glu) (shared with chain I) !8#status predicted SUMMARY #length 250 #molecular-weight 28541 #checksum 4118 SEQUENCE /// ENTRY OBUNMP #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain II - Pneumocystis carinii mitochondrion ORGANISM #formal_name mitochondrion Pneumocystis carinii DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 20-Aug-1999 ACCESSIONS S16283 REFERENCE S16283 !$#authors Pixley, F.J.; Wakefield, A.E.; Banerji, S.; Hopkin, J.M. !$#journal Mol. Microbiol. (1991) 5:1347-1351 !$#title Mitochondrial gene sequences show fungal homology for !1Pneumocystis carinii. !$#cross-references MUID:92157861; PMID:1664905 !$#accession S16283 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type DNA !'##residues 1-243 ##label MOL GENETICS !$#genome mitochondrion CLASSIFICATION #superfamily cytochrome-c oxidase chain II; cytochrome-c !1oxidase chain II homology KEYWORDS copper; electron transfer; membrane-associated complex; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$17-231 #domain cytochrome-c oxidase chain II homology #label !8CO2\ !$35-55 #domain transmembrane #status predicted #label TM1\ !$75-97 #domain transmembrane #status predicted #label TM2\ !$178,213,217,224 #binding_site copper 1 (His, Cys, Cys, Met) #status !8predicted\ !$213,215,217,221 #binding_site copper 2 (Cys, Glu, Cys, His) #status !8predicted\ !$215 #binding_site magnesium (Glu) (shared with chain I) !8#status predicted SUMMARY #length 243 #molecular-weight 27635 #checksum 9199 SEQUENCE /// ENTRY OBZM2 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain II - maize mitochondrion ORGANISM #formal_name mitochondrion Zea mays #common_name maize DATE 02-Apr-1982 #sequence_revision 15-Oct-1994 #text_change 17-Nov-2000 ACCESSIONS B41260; A00480; T01704 REFERENCE A41260 !$#authors Yang, A.J.; Mulligan, R.M. !$#journal Mol. Cell. Biol. (1991) 11:4278-4281 !$#title RNA editing intermediates of cox2 transcripts in maize !1mitochondria. !$#cross-references MUID:91304421; PMID:1712908 !$#accession B41260 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-260 ##label YAN REFERENCE A00480 !$#authors Fox, T.D.; Leaver, C.J. !$#journal Cell (1981) 26:315-323 !$#title The Zea mays mitochondrial gene coding cytochrome oxidase !1subunit II has an intervening sequence and does not contain !1TGA codons. !$#cross-references MUID:82115309; PMID:6276012 !$#accession A00480 !'##molecule_type DNA !'##residues 1-4,'S',6-10,'L',12-25,'S',27-55,'SR',58-86,'R',88-94,'P', !196-128,'RS',131-149,'T',151-155,'P',157-160,'S',162-183,'P', !1185-187,'P',189-195,'S',197-206,'S',208-212,'S',214-234,'T', !1236-260 ##label FOX !'##cross-references EMBL:V00712; NID:g13908; PIDN:CAA24094.1; !1PID:g13910 !'##note the initiation codon was assigned by homology with yeast; there !1is an alternative start codon that would increase the length !1of the protein by 14 residues GENETICS !$#gene mox1; coII !$#genome mitochondrion !$#introns 130/3 CLASSIFICATION #superfamily cytochrome-c oxidase chain II; cytochrome-c !1oxidase chain II homology KEYWORDS copper; electron transfer; membrane-associated complex; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain; RNA !1editing; transmembrane protein FEATURE !$26-242 #domain cytochrome-c oxidase chain II homology #label !8CO2\ !$44-66 #domain transmembrane #status predicted #label TM1\ !$85-107 #domain transmembrane #status predicted #label TM2\ !$189,224,228,235 #binding_site copper 1 (His, Cys, Cys, Met) #status !8predicted\ !$224,226,228,232 #binding_site copper 2 (Cys, Glu, Cys, His) #status !8predicted\ !$226 #binding_site magnesium (Glu) (shared with chain I) !8#status predicted SUMMARY #length 260 #molecular-weight 29679 #checksum 7153 SEQUENCE /// ENTRY OBRZ2 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain II - rice mitochondrion ORGANISM #formal_name mitochondrion Oryza sativa #common_name rice DATE 31-Mar-1989 #sequence_revision 30-Jun-1992 #text_change 20-Aug-1999 ACCESSIONS A93536; A00480; JR0003 REFERENCE A93536 !$#authors Kao, T.; Moon, E.; Wu, R. !$#journal Nucleic Acids Res. (1984) 12:7305-7315 !$#title Cytochrome oxidase subunit II gene of rice has an insertion !1sequence within the intron. !$#cross-references MUID:85037913; PMID:6093039 !$#accession A93536 !'##molecule_type DNA !'##residues 1-260 ##label KAO !'##cross-references EMBL:X01088; NID:g13200; PIDN:CAA25566.1; !1PID:g600446 COMMENT RNA editing in the maize mitochondrion results in a Met !1rather than a Thr at the position for the fourth ligand of !1copper 1 (see PIR:OBZM2). RNA editing may restore the !1missing ligand in this translation. GENETICS !$#gene mox1; coII !$#genome mitochondrion !$#introns 130/3 CLASSIFICATION #superfamily cytochrome-c oxidase chain II; cytochrome-c !1oxidase chain II homology KEYWORDS copper; electron transfer; membrane-associated complex; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$26-242 #domain cytochrome-c oxidase chain II homology #label !8CO2\ !$44-66 #domain transmembrane #status predicted #label TM1\ !$85-107 #domain transmembrane #status predicted #label TM2\ !$189,224,228 #binding_site copper 1 (His, Cys, Cys) #status !8predicted\ !$224,226,228,232 #binding_site copper 2 (Cys, Glu, Cys, His) #status !8predicted\ !$226 #binding_site magnesium (Glu) (shared with chain I) !8#status predicted SUMMARY #length 260 #molecular-weight 29242 #checksum 9090 SEQUENCE /// ENTRY OBWT2 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain II - wheat mitochondrion ALTERNATE_NAMES cytochrome oxidase subunit II ORGANISM #formal_name mitochondrion Triticum aestivum #common_name common wheat DATE 28-May-1986 #sequence_revision 30-Jun-1992 #text_change 20-Aug-1999 ACCESSIONS A00481 REFERENCE A00481 !$#authors Bonen, L.; Boer, P.H.; Gray, M.W. !$#journal EMBO J. (1984) 3:2531-2536 !$#title The wheat cytochrome oxidase subunit II gene has an intron !1insert and three radical amino acid changes relative to !1maize. !$#accession A00481 !'##molecule_type DNA !'##residues 1-260 ##label BON !'##cross-references EMBL:X01108; NID:g13690; PIDN:CAA25581.1; !1PID:g13691 !'##note the authors translated the codon CGG for residues 57, 87 and !1129 as Trp, assuming a special genetic code for plant !1mitochondria COMMENT RNA editing in the maize mitochondrion results in a Met !1rather than a Thr at the position for the fourth ligand of !1copper 1 (see PIR:OBZM2). RNA editing may restore the !1missing ligands in this translation. GENETICS !$#gene coII !$#genome mitochondrion !$#introns 130/3 CLASSIFICATION #superfamily cytochrome-c oxidase chain II; cytochrome-c !1oxidase chain II homology KEYWORDS copper; electron transfer; membrane-associated complex; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$26-242 #domain cytochrome-c oxidase chain II homology #label !8CO2\ !$44-66 #domain transmembrane #status predicted #label TM1\ !$85-107 #domain transmembrane #status predicted #label TM2\ !$189,224 #binding_site copper 1 (His, Cys) #status predicted\ !$224,226,232 #binding_site copper 2 (Cys, Glu, His) #status !8predicted SUMMARY #length 260 #molecular-weight 29253 #checksum 9959 SEQUENCE /// ENTRY OBPM2 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain II - garden pea mitochondrion ORGANISM #formal_name mitochondrion Pisum sativum #common_name garden pea DATE 31-Dec-1989 #sequence_revision 30-Jun-1992 #text_change 20-Aug-1999 ACCESSIONS A23012 REFERENCE A23012 !$#authors Moon, E.; Kao, T.; Wu, R. !$#journal Nucleic Acids Res. (1985) 13:3195-3212 !$#title Pea cytochrome oxidase subunit II gene has no intron and !1generates two mRNA transcripts with different 5'-termini. !$#cross-references MUID:85215679; PMID:2987876 !$#accession A23012 !'##molecule_type DNA !'##residues 1-258 ##label MOO !'##cross-references EMBL:X02433; NID:g13386; PIDN:CAA26282.1; !1PID:g13387 !'##note the authors translated the codon CGG for residues 54, 84, 126, !1and 246 as Trp, assuming a special genetic code for plant !1mitochondria COMMENT RNA editing in the maize mitochondrion results in a Met !1rather than a Thr at the position for the fourth ligand of !1copper 1 (see PIR:OBZM2). RNA editing may restore the !1missing ligand in this translation. GENETICS !$#gene coII !$#genome mitochondrion CLASSIFICATION #superfamily cytochrome-c oxidase chain II; cytochrome-c !1oxidase chain II homology KEYWORDS copper; electron transfer; membrane-associated complex; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$23-238 #domain cytochrome-c oxidase chain II homology #label !8CO2\ !$41-63 #domain transmembrane #status predicted #label TM1\ !$82-104 #domain transmembrane #status predicted #label TM2\ !$186,221,225 #binding_site copper 1 (His, Cys, Cys) #status !8predicted\ !$221,223,225,229 #binding_site copper 2 (Cys, Glu, Cys, His) #status !8predicted\ !$223 #binding_site magnesium (Glu) (shared with chain I) !8#status predicted SUMMARY #length 258 #molecular-weight 29001 #checksum 1524 SEQUENCE /// ENTRY OBPZ2M #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain II - carrot mitochondrion ORGANISM #formal_name mitochondrion Daucus carota #common_name carrot DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 20-Aug-1999 ACCESSIONS S20464; S19858 REFERENCE S20464 !$#authors Lippok, B.; Brennicke, A.; Wissinger, B. !$#journal Mol. Gen. Genet. (1992) 232:322-327 !$#title The coxII gene in carrot mitochondria contains two introns. !$#cross-references MUID:92212297; PMID:1372953 !$#accession S20464 !'##molecule_type DNA !'##residues 1-261 ##label LIP !'##cross-references EMBL:X63625; NID:g18331; PIDN:CAA45171.1; !1PID:g18332 COMMENT RNA editing in the maize mitochondrion results in a Met !1rather than a Thr at the position for the fourth ligand of !1copper 1 (see PIR:OBZM2). RNA editing may restore the !1missing ligand in this translation. GENETICS !$#gene coxII !$#genome mitochondrion !$#introns 129/1; 235/1 CLASSIFICATION #superfamily cytochrome-c oxidase chain II; cytochrome-c !1oxidase chain II homology KEYWORDS copper; electron transfer; membrane-associated complex; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$25-241 #domain cytochrome-c oxidase chain II homology #label !8CO2\ !$43-63 #domain transmembrane #status predicted #label TM1\ !$84-106 #domain transmembrane #status predicted #label TM2\ !$188,223,227 #binding_site copper 1 (His, Cys, Cys) #status !8predicted\ !$223,225,227,231 #binding_site copper 2 (Cys, Glu, Cys, His) #status !8predicted\ !$225 #binding_site magnesium (Glu) (shared with chain I) !8#status predicted SUMMARY #length 261 #molecular-weight 29301 #checksum 600 SEQUENCE /// ENTRY OBOB2M #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain II - evening primrose mitochondrion ORGANISM #formal_name mitochondrion Oenothera villaricae #common_name evening primrose DATE 30-Jun-1992 #sequence_revision 14-Aug-1998 #text_change 20-Aug-1999 ACCESSIONS S20147; S14124; S07177 REFERENCE S14124 !$#authors Hiesel, R.; Wissinger, B.; Brennicke, A. !$#journal Curr. Genet. (1990) 18:371-375 !$#title Cytochrome oxidase subunit II mRNAs in Oenothera !1mitochondria are edited at 24 sites. !$#cross-references MUID:91070624; PMID:2174746 !$#accession S20147 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-258 ##label HIE1 !$#accession S14124 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-8,'L',10-12,'P',14-23,'S',25-42,'F',44-53,'SR',56-64,'H', !166-84,'R',86-92,'P',94-126,'R',128-147,'T',149-158,'S', !1160-181,'P',183-185,'P',187-193,'S',195-210,'S',212-247,'R', !1249-258 ##label HIE2 REFERENCE S07177 !$#authors Hiesel, R.; Brennicke, A. !$#journal EMBO J. (1983) 2:2173-2178 !$#title Cytochrome oxidase subunit II gene in mitochondria of !1Oenothera has no intron. !$#accession S07177 !'##molecule_type DNA !'##residues 1-8,'L',10-12,'P',14-23,'S',25-42,'F',44-53,'SR',56-64,'H', !166-84,'R',86-92,'P',94-126,'RS',129-147,'T',149-158,'S', !1160-181,'P',183-185,'P',187-193,'S',195-210,'S',212-247,'R', !1249-258 ##label HIE !'##cross-references EMBL:X00212; NID:g13226; PIDN:CAA25038.1; !1PID:g13227 !'##note the authors translated the codon CGG for residues 55, 85, 127, !1and 248 as Trp, assuming a special genetic code for plant !1mitochondria GENETICS !$#gene coxII !$#genome mitochondrion FUNCTION !$#description cytochrome-c oxidase complex catalyzes the oxidation of four !1molecules of reduced cytochrome c in the intracristal (or !1intermembrane) space using one oxygen molecule and four !1protons from the mitochondrial matrix producing two !1molecules of water and lowering the concentration of protons !1in the mitochondrial matrix !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome-c oxidase chain II; cytochrome-c !1oxidase chain II homology KEYWORDS copper; electron transfer; heme; membrane-associated !1complex; mitochondrial inner membrane; mitochondrion; !1oxidative phosphorylation; oxidoreductase; respiratory !1chain; RNA editing; transmembrane protein FEATURE !$24-240 #domain cytochrome-c oxidase chain II homology #label !8CO2\ !$42-62 #domain transmembrane #status predicted #label TM1\ !$83-105 #domain transmembrane #status predicted #label TM2\ !$187,222,226,233 #binding_site copper 1 (His, Cys, Cys, Met) #status !8predicted\ !$222,224,226,230 #binding_site copper 2 (Cys, Glu, Cys, His) #status !8predicted\ !$224 #binding_site magnesium (Glu) (shared with chain I) !8#status predicted SUMMARY #length 258 #molecular-weight 29457 #checksum 3446 SEQUENCE /// ENTRY OBPC2N #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain II precursor - Paracoccus denitrificans ORGANISM #formal_name Paracoccus denitrificans DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 23-Jul-1999 ACCESSIONS S00106; S20231; S03803 REFERENCE S00106 !$#authors Steinruecke, P.; Steffens, G.C.M.; Panskus, G.; Buse, G.; !1Ludwig, B. !$#journal Eur. J. Biochem. (1987) 167:431-439 !$#title Subunit II of cytochrome c oxidase from Paracoccus !1denitrificans. DNA sequence, gene expression and the !1protein. !$#cross-references MUID:88004464; PMID:2820725 !$#accession S00106 !'##molecule_type DNA !'##residues 1-297 ##label STE !'##cross-references EMBL:X05934; NID:g45483; PIDN:CAA29372.1; !1PID:g45484 !$#accession S20231 !'##molecule_type protein !'##residues 29,'B';261-280 ##label STE2 REFERENCE S03803 !$#authors Raitio, M.; Jalli, T.; Saraste, M. !$#journal EMBO J. (1987) 6:2825-2833 !$#title Isolation and analysis of the genes for cytochrome c oxidase !1in Paracoccus denitrificans. !$#accession S03803 !'##molecule_type DNA !'##residues 1-158,'GV',161-297 ##label RAI !'##cross-references EMBL:X05828; NID:g45468; PIDN:CAA29268.1; !1PID:g45469 GENETICS !$#gene COII CLASSIFICATION #superfamily cytochrome-c oxidase chain II; cytochrome-c !1oxidase chain II homology KEYWORDS copper; electron transfer; membrane-associated complex; !1oxidoreductase; pyroglutamic acid; respiratory chain; !1transmembrane protein FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-280 #product cytochrome-c oxidase chain II #status !8experimental #label MAT\ !$29-54 #domain periplasmic #status predicted #label PER1\ !$48-262 #domain cytochrome-c oxidase chain II homology #label !8CO2\ !$55-87 #domain transmembrane #status experimental #label !8TM1\ !$102-133 #domain transmembrane #status experimental #label !8TM2\ !$134-280 #domain periplasmic #status predicted #label PER2\ !$281-297 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$29 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$209,244,248,255 #binding_site copper 1 (His, Cys, Cys, Met) #status !8experimental\ !$244,246,248,252 #binding_site copper 2 (Cys, Glu, Cys, His) #status !8experimental\ !$246 #binding_site magnesium (Glu) (shared with chain I) !8#status predicted SUMMARY #length 297 #molecular-weight 32469 #checksum 2331 SEQUENCE /// ENTRY A23711 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain II/c precursor - Thermus aquaticus ALTERNATE_NAMES cytochrome c1 aa3 33K chain; cytochrome-c oxidase bifunctional chain II; cytochrome-c oxidase C chain; cytochrome-c oxidase small chain ORGANISM #formal_name Thermus aquaticus DATE 21-Feb-1992 #sequence_revision 02-Jul-1998 #text_change 03-Mar-2000 ACCESSIONS A23711; S03950 REFERENCE A23711 !$#authors Mather, M.W.; Springer, P.; Fee, J.A. !$#journal J. Biol. Chem. (1991) 266:5025-5035 !$#title Cytochrome oxidase genes from Thermus thermophilus. !1Nucleotide sequence and analysis of the deduced primary !1structure of subunit IIc of cytochrome caa-3. !$#cross-references MUID:91161592; PMID:1848234 !$#accession A23711 !'##molecule_type DNA !'##residues 1-337 ##label MATH !'##cross-references GB:M59180; NID:g155080; PIDN:AAA27484.1; !1PID:g155081 !'##note the authors translated the codon GAA for residue 285 as Gly REFERENCE S03949 !$#authors Buse, G.; Hensel, S.; Fee, J.A. !$#journal Eur. J. Biochem. (1989) 181:261-268 !$#title Evidence for cytochrome oxidase subunit I and a cytochrome c !1- subunit II fused protein in the cytochrome 'c1aa3' of !1Thermus thermophilus. How old is cytochrome oxidase? !$#cross-references MUID:89231697; PMID:2540968 !$#accession S03950 !'##molecule_type protein !'##residues 118-130,'X',132-133,'X',135-136;155-164,'X', !1166-185;209-210,'X',212-216,'LGL',220,'G',223-224,'S', !1226-231,'H',233-254,'XX',257-265;304-314 ##label BUS !'##experimental_source strain HB8, ATCC 27634 !'##note the source is designated as Thermus thermophilus; the amino end !1of the mature protein is blocked COMPLEX heterodimer with chain I (see PIR:A46616) FUNCTION !$#description the cytochrome-c oxidase complex catalyzes the oxidation of !1four molecules of reduced cytochrome c using one oxygen !1molecule and four protons producing two molecules of water !$#pathway respiratory chain CLASSIFICATION #superfamily Thermus aquaticus cytochrome-c oxidase !1bifunctional chain II; cytochrome c6 homology; cytochrome-c !1oxidase chain II homology KEYWORDS chromoprotein; copper; electron transfer; heme; iron; !1membrane-associated complex; metalloprotein; oxidoreductase; !1pyroglutamic acid; respiratory chain; transmembrane protein FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-337 #product cytochrome-c oxidase chain II/c #status !8predicted #label MAT\ !$31-215 #domain cytochrome-c oxidase chain II homology #label !8CO2\ !$37-53 #domain transmembrane #status predicted #label TM1\ !$85-101 #domain transmembrane #status predicted #label TM2\ !$236-324 #domain cytochrome c6 homology #label CYC\ !$17 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status predicted\ !$162,197,201,208 #binding_site copper 1 (His, Cys, Cys, Met) #status !8predicted\ !$197,199,201,205 #binding_site copper 2 (Cys, Glu, Cys, His) #status !8predicted\ !$199 #binding_site magnesium (Glu) (shared with chain I) !8#status predicted\ !$247,250 #binding_site heme (Cys) (covalent) #status !8experimental\ !$251,303 #binding_site heme iron (His, Met) (axial ligands) !8#status predicted SUMMARY #length 337 #molecular-weight 37351 #checksum 133 SEQUENCE /// ENTRY OTHU3 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain III - human mitochondrion ORGANISM #formal_name mitochondrion Homo sapiens #common_name man DATE 22-May-1981 #sequence_revision 23-Oct-1981 #text_change 31-Mar-2000 ACCESSIONS A00482 REFERENCE A00151 !$#authors Anderson, S.; Bankier, A.T.; Barrell, B.G.; de Bruijn, !1M.H.L.; Coulson, A.R.; Drouin, J.; Eperon, I.C.; Nierlich, !1D.P.; Roe, B.A.; Sanger, F.; Schreier, P.H.; Smith, A.J.H.; !1Staden, R.; Young, I.G. !$#journal Nature (1981) 290:457-465 !$#title Sequence and organization of the human mitochondrial genome. !$#cross-references MUID:81173052; PMID:7219534 !$#accession A00482 !'##molecule_type DNA !'##residues 1-261 ##label AND !'##cross-references GB:J01415; EMBL:V00662; NID:g13003; !1PIDN:CAA24032.1; PID:g13010; GSPDB:GN00100 GENETICS !$#gene GDB:MTCO3 !'##cross-references GDB:118902; OMIM:516050 !$#map_position MTH9207-9990 !$#genome mitochondrion !$#genetic_code SGC1 COMPLEX part of a 13 chain complex spanning the inner mitochondrial !1membrane and consisting of one each of chains I (see !1PIR:ODHU1), II (see PIR:OBHU2), III, IV (see PIR:OLHU4), Va !1(see PIR:OTHU5A), Vb (see PIR:OTHU5B), VIa (see PIR:OGHU6A), !1VIb (see PIR:OGHU6B), VIc (see PIR:OGHU6C), VIIa (see !1PIR:OSHU7A), VIIb (see PIR:OSHU7B), VIIc (see PIR:OSHU7C), !1VIII (see PIR:OSHU8); the complex may form dimers within the !1mitochondrial inner-membrane FUNCTION !$#description the cytochrome-c oxidase complex catalyzes the oxidation of !1four molecules of reduced cytochrome c in the intracristal !1(or intermembrane) space using one oxygen molecule and four !1protons from the mitochondrial matrix producing two !1molecules of water and lowering the concentration of protons !1in the mitochondrial matrix !$#pathway oxidative phosphorylation; respiratory chain !$#note chain III may help bind cytochrome c on the intracristal !1side of the inner-membrane CLASSIFICATION #superfamily cytochrome-c oxidase chain III KEYWORDS electron transfer; membrane-associated complex; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$16-34 #domain transmembrane helix #status predicted #label !8TR01\ !$41-66 #domain transmembrane helix #status predicted #label !8TR02\ !$73-105 #domain transmembrane helix #status predicted #label !8TR03\ !$129-152 #domain transmembrane helix #status predicted #label !8TR04\ !$156-183 #domain transmembrane helix #status predicted #label !8TR05\ !$191-223 #domain transmembrane helix #status predicted #label !8TR06\ !$233-256 #domain transmembrane helix #status predicted #label !8TR07 SUMMARY #length 261 #molecular-weight 30010 #checksum 1450 SEQUENCE /// ENTRY OTBO3 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain III [validated] - bovine mitochondrion ORGANISM #formal_name mitochondrion Bos primigenius taurus #common_name cattle DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 15-Sep-2000 ACCESSIONS A00483 REFERENCE A00152 !$#authors Anderson, S.; de Bruijn, M.H.L.; Coulson, A.R.; Eperon, !1I.C.; Sanger, F.; Young, I.G. !$#journal J. Mol. Biol. (1982) 156:683-717 !$#title Complete sequence of bovine mitochondrial DNA. Conserved !1features of the mammalian mitochondrial genome. !$#cross-references MUID:83010260; PMID:7120390 !$#accession A00483 !'##molecule_type DNA !'##residues 1-261 ##label AND !'##cross-references GB:J01394; NID:g336430; EMBL:V00654; NID:g12800; !1PID:g12807 REFERENCE A67451 !$#authors Tsukihara, T.; Aoyama, H.; Yamashita, E.; Tomizaki, T.; !1Yamaguchi, H.; Shinzawa-itoh, K.; Nakashima, R.; Yaono, R.; !1Yoshikawa, S. !$#submission submitted to the Brookhaven Protein Data Bank, April 1996 !$#cross-references PDB:1OCC !$#contents annotation; X-ray crystallography, 2.8 angstroms, residues !11-261 REFERENCE A57981 !$#authors Tsukihara, T.; Aoyama, H.; Yamashita, E.; Tomizaki, T.; !1Yamaguchi, H.; Sinzawa-Itoh, K.; Nakashima, R.; Yaono, R.; !1Yoshikawa, S. !$#journal Science (1996) 272:1136-1144 !$#title The whole structure of the 13-subunit oxidized cytochrome c !1oxidase at 2.8 angstroms. !$#cross-references MUID:96216288; PMID:8638158 !$#contents annotation; X-ray crystallography, 2.8 angstroms GENETICS !$#gene coIII !$#genome mitochondrion !$#genetic_code SGC1 COMPLEX part of a 13 chain complex spanning the inner mitochondrial !1membrane and consisting of one each of chains I (see !1PIR:ODBO1), II (see PIR:OBBO2), III, IV (see PIR:OLBO4), Va !1(see PIR:CABO), Vb (see PIR:OGBO6A), VIa (see PIR:OGBO6), !1VIb (see PIR:OGBO7), VIc (see PIR:OGBO6C), VIIa (see !1PIR:OSBO7A), VIIb (see PIR:OSBO7B), VIIc (see PIR:OSBO8A), !1VIII (see PIR:OSBO8); the complex may form dimers within the !1mitochondrial inner-membrane FUNCTION !$#description the cytochrome-c oxidase complex catalyzes the oxidation of !1four molecules of reduced cytochrome c in the intracristal !1(or intermembrane) space using one oxygen molecule and four !1protons from the mitochondrial matrix producing two !1molecules of water and lowering the concentration of protons !1in the mitochondrial matrix !$#pathway oxidative phosphorylation; respiratory chain !$#note chain III may help bind cytochrome c on the intracristal !1side of the inner-membrane CLASSIFICATION #superfamily cytochrome-c oxidase chain III KEYWORDS electron transfer; membrane-associated complex; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$1-15 #domain mitochondrial matrix #status experimental !8#label MM1\ !$16-34 #domain transmembrane helix #status experimental !8#label TR01\ !$35-40 #domain intracristal #status experimental #label !8ITC1\ !$41-66 #domain transmembrane helix #status experimental !8#label TR02\ !$67-72 #domain mitochondrial matrix #status experimental !8#label MM2\ !$73-105 #domain transmembrane helix #status experimental !8#label TR03\ !$106-128 #domain intracristal #status experimental #label !8ITC2\ !$129-152 #domain transmembrane helix #status experimental !8#label TR04\ !$153-155 #domain mitochondrial matrix #status experimental !8#label MM3\ !$156-183 #domain transmembrane helix #status experimental !8#label TR05\ !$184-190 #domain intracristal #status experimental #label !8ITC3\ !$191-223 #domain transmembrane helix #status experimental !8#label TR06\ !$224-232 #domain mitochondrial matrix #status experimental !8#label MM4\ !$233-256 #domain transmembrane helix #status experimental !8#label TR07\ !$257-261 #domain intracristal #status experimental #label ITC4 SUMMARY #length 261 #molecular-weight 29919 #checksum 1342 SEQUENCE /// ENTRY OTMS3 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain III - mouse mitochondrion ORGANISM #formal_name mitochondrion Mus musculus #common_name house mouse DATE 02-Apr-1982 #sequence_revision 02-Apr-1982 #text_change 07-Dec-1999 ACCESSIONS A00484 REFERENCE A00153 !$#authors Bibb, M.J.; Van Etten, R.A.; Wright, C.T.; Walberg, M.W.; !1Clayton, D.A. !$#journal Cell (1981) 26:167-180 !$#title Sequence and gene organization of mouse mitochondrial DNA. !$#cross-references MUID:82137051; PMID:7332926 !$#accession A00484 !'##molecule_type DNA !'##residues 1-261 ##label BIB !'##cross-references GB:J01420; NID:g342520; PIDN:AAB48650.1; !1PID:g896297; EMBL:V00711; NID:g13838; PID:g13845 GENETICS !$#gene coIII !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily cytochrome-c oxidase chain III KEYWORDS electron transfer; membrane-associated complex; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$16-34 #domain transmembrane helix #status predicted #label !8TR01\ !$41-66 #domain transmembrane helix #status predicted #label !8TR02\ !$73-105 #domain transmembrane helix #status predicted #label !8TR03\ !$129-152 #domain transmembrane helix #status predicted #label !8TR04\ !$156-183 #domain transmembrane helix #status predicted #label !8TR05\ !$191-223 #domain transmembrane helix #status predicted #label !8TR06\ !$233-256 #domain transmembrane helix #status predicted #label !8TR07 SUMMARY #length 261 #molecular-weight 29937 #checksum 1649 SEQUENCE /// ENTRY OTFF3 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain III - fruit fly (Drosophila melanogaster) mitochondrion ORGANISM #formal_name mitochondrion Drosophila melanogaster DATE 18-Apr-1984 #sequence_revision 18-Apr-1984 #text_change 07-Dec-1999 ACCESSIONS A00485; A93463; S02250 REFERENCE A93307 !$#authors de Bruijn, M.H.L. !$#journal Nature (1983) 304:234-241 !$#title Drosophila melanogaster mitochondrial DNA, a novel !1organization and genetic code. !$#cross-references MUID:83245048; PMID:6408489 !$#accession A00485 !'##molecule_type DNA !'##residues 1-179 ##label DEB REFERENCE A93463 !$#authors Clary, D.O.; Wahleithner, J.A.; Wolstenholme, D.R. !$#journal Nucleic Acids Res. (1983) 11:2411-2425 !$#title Transfer RNA genes in Drosophila mitochondrial DNA: related !15' flanking sequences and comparisons to mammalian !1mitochondrial tRNA genes. !$#cross-references MUID:83220794; PMID:6304652 !$#accession A93463 !'##molecule_type DNA !'##residues 179-262 ##label CLA REFERENCE S01185 !$#authors Garesse, R. !$#journal Genetics (1988) 118:649-663 !$#title Drosophila melanogaster mitochondrial DNA: gene organization !1and evolutionary considerations. !$#cross-references MUID:88212147; PMID:3130291 !$#accession S02250 !'##molecule_type DNA !'##residues 179-262 ##label GAR !'##cross-references GB:M37275; EMBL:Y00610; NID:g336819; !1PIDN:AAA69708.1; PID:g336820 GENETICS !$#gene coIII !'##cross-references FlyBase:FBgn0013676 !$#genome mitochondrion !$#genetic_code SGC4 CLASSIFICATION #superfamily cytochrome-c oxidase chain III KEYWORDS electron transfer; membrane-associated complex; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$17-35 #domain transmembrane helix #status predicted #label !8TR01\ !$42-67 #domain transmembrane helix #status predicted #label !8TR02\ !$74-106 #domain transmembrane helix #status predicted #label !8TR03\ !$130-153 #domain transmembrane helix #status predicted #label !8TR04\ !$157-184 #domain transmembrane helix #status predicted #label !8TR05\ !$192-224 #domain transmembrane helix #status predicted #label !8TR06\ !$234-257 #domain transmembrane helix #status predicted #label !8TR07 SUMMARY #length 262 #molecular-weight 30064 #checksum 3508 SEQUENCE /// ENTRY OTFF3Y #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain III - fruit fly (Drosophila yakuba) mitochondrion ORGANISM #formal_name mitochondrion Drosophila yakuba DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 07-Dec-1999 ACCESSIONS B93477; F25797; A00485 REFERENCE A93477 !$#authors Clary, D.O.; Wolstenholme, D.R. !$#journal Nucleic Acids Res. (1983) 11:4211-4227 !$#title Nucleotide sequence of a segment of Drosophila mitochondrial !1DNA that contains the genes for cytochrome c oxidase !1subunits II and III and ATPase subunit 6. !$#cross-references MUID:83246544; PMID:6306579 !$#accession B93477 !'##molecule_type DNA !'##residues 1-262 ##label CLA !'##cross-references GB:X03240; NID:g12923; PIDN:CAA26990.1; PID:g12929; !1GB:X00924; NID:g12918; PID:g12922 !'##note the authors translated the codon AGA for residues 97, 105, 151, !1and 155 as Arg REFERENCE A92962 !$#authors Clary, D.O.; Wolstenholme, D.R. !$#journal J. Mol. Evol. (1985) 22:252-271 !$#title The mitochondrial DNA molecule of Drosophila yakuba: !1nucleotide sequence, gene organization, and genetic code. !$#cross-references MUID:86089137; PMID:3001325 !$#accession F25797 !'##molecule_type DNA !'##residues 1-262 ##label CL2 !'##cross-references GB:X03240; GB:J01400; GB:J01402; GB:J01403; !1GB:J01406; GB:J01408; GB:V01521; GB:X00563; NID:g12923; !1PIDN:CAA26990.1; PID:g12929 GENETICS !$#gene COIII !'##cross-references FlyBase:FBgn0013181 !$#genome mitochondrion !$#genetic_code SGC4 CLASSIFICATION #superfamily cytochrome-c oxidase chain III KEYWORDS electron transfer; membrane-associated complex; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$17-35 #domain transmembrane helix #status predicted #label !8TR01\ !$42-67 #domain transmembrane helix #status predicted #label !8TR02\ !$74-106 #domain transmembrane helix #status predicted #label !8TR03\ !$130-153 #domain transmembrane helix #status predicted #label !8TR04\ !$157-184 #domain transmembrane helix #status predicted #label !8TR05\ !$192-224 #domain transmembrane helix #status predicted #label !8TR06\ !$234-257 #domain transmembrane helix #status predicted #label !8TR07 SUMMARY #length 262 #molecular-weight 30039 #checksum 4549 SEQUENCE /// ENTRY OTXL3 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain III - African clawed frog mitochondrion ALTERNATE_NAMES cytochrome a3 polypeptide III; cytochrome aa3 polypeptide III ORGANISM #formal_name mitochondrion Xenopus laevis #common_name African clawed frog DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 07-Dec-1999 ACCESSIONS A00486 REFERENCE A00155 !$#authors Roe, B.A.; Ma, D.P.; Wilson, R.K.; Wong, J.F.H. !$#journal J. Biol. Chem. (1985) 260:9759-9774 !$#title The complete nucleotide sequence of the Xenopus laevis !1mitochondrial genome. !$#cross-references MUID:85261388; PMID:4019494 !$#accession A00486 !'##molecule_type DNA !'##residues 1-260 ##label ROE !'##cross-references GB:M10217; GB:X01600; GB:X01601; GB:X02890; !1NID:g343717; PIDN:AAA66464.1; PID:g807688 GENETICS !$#gene coIII !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily cytochrome-c oxidase chain III KEYWORDS electron transfer; membrane-associated complex; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$16-34 #domain transmembrane helix #status predicted #label !8TR01\ !$41-66 #domain transmembrane helix #status predicted #label !8TR02\ !$73-105 #domain transmembrane helix #status predicted #label !8TR03\ !$129-152 #domain transmembrane helix #status predicted #label !8TR04\ !$156-183 #domain transmembrane helix #status predicted #label !8TR05\ !$191-223 #domain transmembrane helix #status predicted #label !8TR06\ !$233-255 #domain transmembrane helix #status predicted #label !8TR07 SUMMARY #length 260 #molecular-weight 29593 #checksum 8367 SEQUENCE /// ENTRY OTCA3 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain III - common carp mitochondrion ORGANISM #formal_name mitochondrion Cyprinus carpio #common_name common carp DATE 31-Dec-1991 #sequence_revision 30-Sep-1993 #text_change 23-Mar-2001 ACCESSIONS S36010; S14918; G44650; S08070 REFERENCE S21910 !$#authors Chang, Y.S.; Huang, F.L. !$#submission submitted to the EMBL Data Library, July 1991 !$#description The cDNA and primary structure of pregrowth hormones of !1three species of Cyprinadae: silver carp, bighead carp and !1grass carp. !$#accession S36010 !'##molecule_type DNA !'##residues 1-261 ##label CHA1 !'##cross-references EMBL:X61010; NID:g436882; PIDN:CAA43341.1; !1PID:g12843 REFERENCE S14918 !$#authors Huang, C.J.; Huang, F.L.; Chang, Y.S.; Tsai, Y.J.; Lo, T.B. !$#journal Nucleic Acids Res. (1990) 18:1056 !$#title Nucleotide sequence of carp mitochondrial cytochrome C !1oxidase III. !$#cross-references MUID:90192097; PMID:2156223 !$#accession S14918 !'##molecule_type mRNA !'##residues 1-120,'M',122-261 ##label HUA !'##cross-references EMBL:X17006; NID:g12847; PIDN:CAA34866.1; !1PID:g12848 !'##note the authors translated the codon GAA for residue 155 as Asp and !1the codon ATA for residues 27 and 43 according to the !1standard genetic code REFERENCE A44650 !$#authors Chang, Y.S.; Huang, F.L.; Lo, T.B. !$#journal J. Mol. Evol. (1994) 38:138-155 !$#title The complete nucleotide sequence and gene organization of !1carp (Cyprinus carpio) mitochondrial genome. !$#cross-references MUID:94223691; PMID:8169959 !$#accession G44650 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type DNA !'##residues 1-261 ##label CHA2 !'##cross-references EMBL:X61010; NID:g436882; PIDN:CAA43341.1; !1PID:g12843 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily cytochrome-c oxidase chain III KEYWORDS electron transfer; membrane-associated complex; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$16-34 #domain transmembrane helix #status predicted #label !8TR01\ !$41-66 #domain transmembrane helix #status predicted #label !8TR02\ !$73-105 #domain transmembrane helix #status predicted #label !8TR03\ !$129-152 #domain transmembrane helix #status predicted #label !8TR04\ !$156-183 #domain transmembrane helix #status predicted #label !8TR05\ !$191-223 #domain transmembrane helix #status predicted #label !8TR06\ !$233-256 #domain transmembrane helix #status predicted #label !8TR07 SUMMARY #length 261 #molecular-weight 29640 #checksum 9548 SEQUENCE /// ENTRY OTWT3M #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain III - wheat mitochondrion ORGANISM #formal_name mitochondrion Triticum aestivum #common_name common wheat DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 20-Aug-1999 ACCESSIONS S10331; S20233; S08212 REFERENCE S10331 !$#authors Gualberto, J.M.; Weil, J.H.; Grienenberger, J.M. !$#journal Nucleic Acids Res. (1990) 18:3771-3776 !$#title Editing of the wheat coxIII transcript: evidence for twelve !1C to U and one U to C conversions and for sequence !1similarities around editing sites. !$#cross-references MUID:90326496; PMID:1695731 !$#accession S10331 !'##molecule_type mRNA !'##residues 1-265 ##label GUA1 !'##cross-references EMBL:X52539; NID:g13692; PIDN:CAA36775.1; !1PID:g13693 !$#accession S20233 !'##molecule_type DNA !'##residues 1-81,'P',83-96,'L',98-103,'SS',106-137,'P',139-140,'P', !1142-170,'S',172-175,'S',177-188,'S',190-251,'R',253-254,'P', !1256-265 ##label GUA2 !'##cross-references EMBL:X52539 REFERENCE S08212 !$#authors Gualberto, J.M.; Domon, C.; Weil, J.H.; Grienenberger, J.M. !$#journal Curr. Genet. (1990) 17:41-47 !$#title Structure and transcription of the gene coding for subunit 3 !1of cytochrome oxidase in wheat mitochondria. !$#cross-references MUID:90182728; PMID:2155710 !$#accession S08212 !'##molecule_type DNA !'##residues 1-81,'P',83-96,'L',98-103,'SS',106-137,'P',139-140,'P', !1142-170,'S',172-175,'S',177-188,'S',190-251,'R',253-254,'P', !1256-265 ##label GUA3 !'##cross-references EMBL:X15944 GENETICS !$#gene coxIII; cox3 !$#genome mitochondrion CLASSIFICATION #superfamily cytochrome-c oxidase chain III KEYWORDS electron transfer; membrane-associated complex; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain; RNA !1editing; transmembrane protein FEATURE !$17-35 #domain transmembrane helix #status predicted #label !8TR01\ !$44-69 #domain transmembrane helix #status predicted #label !8TR02\ !$76-108 #domain transmembrane helix #status predicted #label !8TR03\ !$132-155 #domain transmembrane helix #status predicted #label !8TR04\ !$159-186 #domain transmembrane helix #status predicted #label !8TR05\ !$194-226 #domain transmembrane helix #status predicted #label !8TR06\ !$236-259 #domain transmembrane helix #status predicted #label !8TR07 SUMMARY #length 265 #molecular-weight 29796 #checksum 7553 SEQUENCE /// ENTRY OTRZ3M #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain III - rice mitochondrion ORGANISM #formal_name mitochondrion Oryza sativa #common_name rice DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 20-Aug-1999 ACCESSIONS JQ0166; S29748; S07875 REFERENCE JQ0166 !$#authors Kaleikau, E.K.; Andre, C.P.; Walbot, V. !$#journal Nucleic Acids Res. (1990) 18:371 !$#title Sequence of the rice mitochondrial gene for cytochrome !1oxidase subunit 3. !$#cross-references MUID:90221829; PMID:2158075 !$#accession JQ0166 !'##molecule_type DNA !'##residues 1-265 ##label KAL !'##cross-references EMBL:X17040; NID:g13216; PIDN:CAA34898.1; !1PID:g13217 REFERENCE S26876 !$#authors Liu, A.W.; Narayanan, K.K.; Andre, C.P.; Kaleikau, E.K.; !1Walbot, V. !$#journal Curr. Genet. (1992) 21:507-513 !$#title Co-transcription of orf25 and coxIII in rice mitochondria. !$#cross-references MUID:92315351; PMID:1617739 !$#accession S29748 !'##status translation not shown !'##molecule_type DNA !'##residues 1-265 ##label LIU !'##cross-references EMBL:M74241; NID:g343214; PIDN:AAA66048.1; !1PID:g804815 GENETICS !$#gene cox3 !$#genome mitochondrion CLASSIFICATION #superfamily cytochrome-c oxidase chain III KEYWORDS electron transfer; membrane-associated complex; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$17-35 #domain transmembrane helix #status predicted #label !8TR01\ !$44-69 #domain transmembrane helix #status predicted #label !8TR02\ !$76-108 #domain transmembrane helix #status predicted #label !8TR03\ !$132-155 #domain transmembrane helix #status predicted #label !8TR04\ !$159-186 #domain transmembrane helix #status predicted #label !8TR05\ !$194-226 #domain transmembrane helix #status predicted #label !8TR06\ !$236-259 #domain transmembrane helix #status predicted #label !8TR07 SUMMARY #length 265 #molecular-weight 29358 #checksum 144 SEQUENCE /// ENTRY OTSY3M #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain III - soybean mitochondrion ORGANISM #formal_name mitochondrion Glycine max #common_name soybean DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 20-Aug-1999 ACCESSIONS S07468 REFERENCE S07468 !$#authors Grabau, E.A.; Gengenbach, B.G. !$#journal Plant Mol. Biol. (1989) 13:595-597 !$#title Cytochrome oxidase subunit III gene from soybean !1mitochondria. !$#cross-references MUID:91370841; PMID:2562384 !$#accession S07468 !'##molecule_type DNA !'##residues 1-265 ##label GRA !'##cross-references EMBL:X15131; NID:g12976; PIDN:CAA33227.1; !1PID:g12977 !'##note the authors translated the codon CGG for residues 102, 130 and !1252 as Trp, assuming a special genetic code for plant !1mitochondria GENETICS !$#gene coxIII !$#genome mitochondrion CLASSIFICATION #superfamily cytochrome-c oxidase chain III KEYWORDS electron transfer; membrane-associated complex; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$17-35 #domain transmembrane helix #status predicted #label !8TR01\ !$44-69 #domain transmembrane helix #status predicted #label !8TR02\ !$76-108 #domain transmembrane helix #status predicted #label !8TR03\ !$132-155 #domain transmembrane helix #status predicted #label !8TR04\ !$159-186 #domain transmembrane helix #status predicted #label !8TR05\ !$194-226 #domain transmembrane helix #status predicted #label !8TR06\ !$236-259 #domain transmembrane helix #status predicted #label !8TR07 SUMMARY #length 265 #molecular-weight 29599 #checksum 9505 SEQUENCE /// ENTRY OTOB3M #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain III - Bertero's evening primrose mitochondrion ALTERNATE_NAMES cytochrome a3 polypeptide III; cytochrome aa3 polypeptide III ORGANISM #formal_name mitochondrion Oenothera berteriana #common_name Bertero's evening primrose DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 01-Dec-2000 ACCESSIONS B26170; T09853 REFERENCE A91078 !$#authors Hiesel, R.; Schobel, W.; Schuster, W.; Brennicke, A. !$#journal EMBO J. (1987) 6:29-34 !$#title The cytochrome oxidase subunit I and subunit III genes in !1Oenothera mitochondria are transcribed from identical !1promoter sequences. !$#accession B26170 !'##molecule_type mRNA !'##residues 1-265 ##label HIE !'##cross-references EMBL:X04764; NID:g13169; PIDN:CAA28459.1; !1PID:g13172 !'##note the authors translated the codon AGG for residue 6 as Lys, CTC !1for residue 23 as Ser, GGA for residue 24 as Leu, GGA for !1residue 144 as Glu, GTA for residue 147 as Ala, TTT for !1residue 209 as Thr, and GTA for residue 257 as Leu !'##note the authors translated the codon CGG for residues 102 and 252 !1as Trp, assuming a special genetic code for plant !1mitochondria !'##note the source species is not specified; see GenBank entry !1MIOBCOX1, release 117.0 REFERENCE Z16887 !$#authors Karlovsky, P.; Fartmann, B. !$#journal J. Mol. Evol. (1992) 34:254-258 !$#title Genetic code and phylogenetic origin of oomycetous !1mitochondria. !$#cross-references MUID:92269300; PMID:1588598 !$#accession T09853 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-265 ##label KAR !'##cross-references EMBL:X04764; NID:g13169; PIDN:CAA28459.1; !1PID:g13172 GENETICS !$#gene coxIII !$#genome mitochondrion CLASSIFICATION #superfamily cytochrome-c oxidase chain III KEYWORDS electron transfer; membrane-associated complex; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$17-35 #domain transmembrane helix #status predicted #label !8TR01\ !$44-69 #domain transmembrane helix #status predicted #label !8TR02\ !$76-108 #domain transmembrane helix #status predicted #label !8TR03\ !$132-155 #domain transmembrane helix #status predicted #label !8TR04\ !$159-186 #domain transmembrane helix #status predicted #label !8TR05\ !$194-226 #domain transmembrane helix #status predicted #label !8TR06\ !$236-259 #domain transmembrane helix #status predicted #label !8TR07 SUMMARY #length 265 #molecular-weight 29497 #checksum 292 SEQUENCE /// ENTRY OTBY3 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain III - yeast (Saccharomyces cerevisiae) mitochondrion (strain D273-10B/ A48) ORGANISM #formal_name mitochondrion Saccharomyces cerevisiae #variety strain D273-10B/A48 DATE 31-Oct-1980 #sequence_revision 19-Feb-1984 #text_change 19-Apr-2002 ACCESSIONS A00487 REFERENCE A00487 !$#authors Thalenfeld, B.E.; Tzagoloff, A. !$#journal J. Biol. Chem. (1980) 255:6173-6180 !$#title Assembly of the mitochondrial system. Sequence of the oxi2 !1gene of yeast mitochondrial DNA. !$#cross-references MUID:80227739; PMID:6248512 !$#accession A00487 !'##molecule_type DNA !'##residues 1-269 ##label THA !'##experimental_source strain D273-10B/A48 !'##note the authors translated the codon ATA for residue 81 according !1to the standard code GENETICS !$#gene SGD:COX3; cox3; oxi2 !'##cross-references SGD:S0007283 !$#map_position 20.2-20.4 !$#genome mitochondrion !$#genetic_code SGC2 CLASSIFICATION #superfamily cytochrome-c oxidase chain III KEYWORDS electron transfer; membrane-associated complex; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$22-40 #domain transmembrane helix #status predicted #label !8TR01\ !$49-74 #domain transmembrane helix #status predicted #label !8TR02\ !$81-113 #domain transmembrane helix #status predicted #label !8TR03\ !$137-160 #domain transmembrane helix #status predicted #label !8TR04\ !$164-191 #domain transmembrane helix #status predicted #label !8TR05\ !$199-231 #domain transmembrane helix #status predicted #label !8TR06\ !$241-264 #domain transmembrane helix #status predicted #label !8TR07 SUMMARY #length 269 #molecular-weight 30262 #checksum 3875 SEQUENCE /// ENTRY OTAS3 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain III - Emericella nidulans mitochondrion ORGANISM #formal_name mitochondrion Emericella nidulans, Aspergillus nidulans DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 07-Dec-1999 ACCESSIONS B93436; A94593; A00488 REFERENCE A93436 !$#authors Netzker, R.; Kochel, H.G.; Basak, N.; Kuntzel, H. !$#journal Nucleic Acids Res. (1982) 10:4783-4794 !$#title Nucleotide sequence of Aspergillus nidulans mitochondrial !1genes coding for ATPase subunit 6, cytochrome oxidase !1subunit 3, seven unidentified proteins, four tRNAs and !1L-rRNA. !$#cross-references MUID:83038633; PMID:6290989 !$#accession B93436 !'##molecule_type DNA !'##residues 1-10,'L',12-18,'E',20-122,'X',124-248,'Q',250-269 ##label !1NET !'##experimental_source imperfect stage !'##note this sequence has been revised in reference A94593 REFERENCE A94593 !$#authors Lazarus, C.M.; Kuntzel, H. !$#submission submitted to the Atlas, March 1984 !$#accession A94593 !'##molecule_type DNA !'##residues 1-269 ##label LAZ GENETICS !$#gene cox3 !$#genome mitochondrion !$#genetic_code SGC3 !$#start_codon GTG CLASSIFICATION #superfamily cytochrome-c oxidase chain III KEYWORDS electron transfer; membrane-associated complex; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$22-40 #domain transmembrane helix #status predicted #label !8TR01\ !$49-74 #domain transmembrane helix #status predicted #label !8TR02\ !$81-113 #domain transmembrane helix #status predicted #label !8TR03\ !$137-160 #domain transmembrane helix #status predicted #label !8TR04\ !$164-191 #domain transmembrane helix #status predicted #label !8TR05\ !$199-231 #domain transmembrane helix #status predicted #label !8TR06\ !$241-264 #domain transmembrane helix #status predicted #label !8TR07 SUMMARY #length 269 #molecular-weight 30360 #checksum 2973 SEQUENCE /// ENTRY OTNC3 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain III - Neurospora crassa mitochondrion ALTERNATE_NAMES ferrocytochrome c ORGANISM #formal_name mitochondrion Neurospora crassa DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 07-Dec-1999 ACCESSIONS A00489 REFERENCE A92371 !$#authors Browning, K.S.; RajBhandary, U.L. !$#journal J. Biol. Chem. (1982) 257:5253-5256 !$#title Cytochrome oxidase subunit III gene in Neurospora crassa !1mitochondrial. Location and sequence. !$#cross-references MUID:82167655; PMID:6279664 !$#accession A00489 !'##molecule_type DNA !'##residues 1-269 ##label BRO !'##cross-references GB:V00668; GB:J01430; NID:g13125; PIDN:CAA24041.1; !1PID:g13126 REFERENCE A91210 !$#authors Sebald, W.; Machleidt, W.; Otto, J. !$#journal Eur. J. Biochem. (1973) 38:311-324 !$#title Products of mitochondrial protein synthesis in Neurospora !1crassa. Determination of equimolar amounts of three products !1in cytochrome oxidase on the basis of amino-acid analysis. !$#cross-references MUID:74086110; PMID:4359388 !$#contents annotation; composition GENETICS !$#gene oxi2 !$#genome mitochondrion !$#genetic_code SGC3 CLASSIFICATION #superfamily cytochrome-c oxidase chain III KEYWORDS electron transfer; membrane-associated complex; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$22-40 #domain transmembrane helix #status predicted #label !8TR01\ !$49-74 #domain transmembrane helix #status predicted #label !8TR02\ !$81-113 #domain transmembrane helix #status predicted #label !8TR03\ !$137-160 #domain transmembrane helix #status predicted #label !8TR04\ !$164-191 #domain transmembrane helix #status predicted #label !8TR05\ !$199-231 #domain transmembrane helix #status predicted #label !8TR06\ !$241-264 #domain transmembrane helix #status predicted #label !8TR07 SUMMARY #length 269 #molecular-weight 30089 #checksum 7369 SEQUENCE /// ENTRY OLHU4 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain IV precursor - human ORGANISM #formal_name Homo sapiens #common_name man DATE 13-Jan-1995 #sequence_revision 07-Jun-1996 #text_change 11-Jun-1999 ACCESSIONS S47012; I54009; S21077 REFERENCE S47012 !$#authors Park, S.J.; Modica-Napolitano, J.; Gross, A.; Ernst, S.G.; !1Aprille, J.R. !$#submission submitted to the EMBL Data Library, October 1990 !$#accession S47012 !'##status preliminary !'##molecule_type mRNA !'##residues 1-169 ##label PAR !'##cross-references EMBL:X54802; NID:g517251; PIDN:CAA38573.1; !1PID:g517252 REFERENCE I54009 !$#authors Zeviani, M.; Nakagawa, M.; Herbert, J.; Lomax, M.I.; !1Grossman, L.I.; Sherbany, A.A.; Miranda, A.F.; DiMauro, S.; !1Schon, E.A. !$#journal Gene (1987) 55:205-217 !$#title Isolation of a cDNA clone encoding subunit IV of human !1cytochrome c oxidase. !$#cross-references MUID:88030687; PMID:2444497 !$#accession I54009 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-169 ##label ZEV !'##cross-references GB:M21575; NID:g1311702; PIDN:AAA99312.1; !1PID:g180933 REFERENCE S21077 !$#authors van Kuilenburg, A.B.P.; van Beeumen, J.J.; Demol, H.; van !1den Bogert, C.; Schouten, I.; Muijsers, A.O. !$#journal Biochim. Biophys. Acta (1992) 1119:218-224 !$#title Subunit IV of human cytochrome c oxidase, polymorphism and a !1putative isoform. !$#cross-references MUID:92172943; PMID:1311608 !$#accession S21077 !'##status preliminary !'##molecule_type protein !'##residues 23-52 ##label KUI GENETICS !$#gene GDB:COX4 !'##cross-references GDB:119068; OMIM:123864 !$#map_position 16q24.1-16q24.1 COMPLEX part of a 13 chain complex spanning the inner mitochondrial !1membrane and consisting of one each of chains I (see !1PIR:ODHU1), II (see PIR:OBHU2), III (see PIR:OTHU3), IV, Va !1(see PIR:OTHU5A), Vb (see PIR:OTHU5B), VIa (see PIR:OGHU6A), !1VIb (see PIR:OGHU6B), VIc (see PIR:OGHU6C), VIIa (see !1PIR:OSHU7A), VIIb (see PIR:OSHU7B), VIIc (see PIR:OSHU7C), !1VIII (see PIR:OSHU8); the complex may form dimers within the !1mitochondrial inner-membrane FUNCTION !$#description the cytochrome-c oxidase complex catalyzes the oxidation of !1four molecules of reduced cytochrome c in the intracristal !1(or intermembrane) space using one oxygen molecule and four !1protons from the mitochondrial matrix producing two !1molecules of water and lowering the concentration of protons !1in the mitochondrial matrix !$#pathway oxidative phosphorylation; respiratory chain !$#note the role of chain IV is not clear CLASSIFICATION #superfamily cytochrome-c oxidase chain IV KEYWORDS electron transfer; membrane-associated complex; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$1-22 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$23-169 #product cytochrome-c oxidase chain IV #status !8predicted #label MAT\ !$77-103 #domain transmembrane helix #status predicted #label !8TR01 SUMMARY #length 169 #molecular-weight 19577 #checksum 9666 SEQUENCE /// ENTRY OLBO4 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain IV precursor [validated] - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 28-Feb-1980 #sequence_revision 07-Jun-1996 #text_change 15-Sep-2000 ACCESSIONS A30618; A91681; A29968; A00490 REFERENCE A30618 !$#authors Lomax, M.I.; Bachman, N.J.; Nasoff, M.S.; Caruthers, M.H.; !1Grossman, L.I. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:6295-6299 !$#title Isolation and characterization of a cDNA clone for bovine !1cytochrome c oxidase subunit IV. !$#cross-references MUID:85038504; PMID:6093095 !$#accession A30618 !'##molecule_type mRNA !'##residues 1-128 ##label LOM !'##cross-references EMBL:K02064; NID:g162892; PIDN:AAA30463.1; !1PID:g162893 REFERENCE A91681 !$#authors Sacher, R.; Steffens, G.J.; Buse, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1979) 360:1385-1392 !$#title Studies on cytochrome c oxidase, VI. Polypeptide IV: the !1complete primary structure. !$#cross-references MUID:80048318; PMID:227780 !$#accession A91681 !'##molecule_type protein !'##residues 23-169 ##label SAC !'##experimental_source heart REFERENCE A90531 !$#authors Yanamura, W.; Zhang, Y.Z.; Takamiya, S.; Capaldi, R.A. !$#journal Biochemistry (1988) 27:4909-4914 !$#title Tissue-specific differences between heart and liver !1cytochrome c oxidase. !$#cross-references MUID:89000697; PMID:2844245 !$#accession A29968 !'##molecule_type protein !'##residues 23-43;108-138;148-169 ##label YAN !'##experimental_source liver REFERENCE A91680 !$#authors Sacher, R.; Buse, G.; Steffens, G.J. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1979) 360:1377-1383 !$#title Studies on cytochrome c oxidase, V. Polypeptide IV: !1alignment and amino acid sequences of cyanogen bromide !1fragments. !$#cross-references MUID:80048317; PMID:227779 !$#contents annotation; partial sequence REFERENCE A67451 !$#authors Tsukihara, T.; Aoyama, H.; Yamashita, E.; Tomizaki, T.; !1Yamaguchi, H.; Shinzawa-itoh, K.; Nakashima, R.; Yaono, R.; !1Yoshikawa, S. !$#submission submitted to the Brookhaven Protein Data Bank, April 1996 !$#cross-references PDB:1OCC !$#contents annotation; X-ray crystallography, 2.8 angstroms, residues !126-169 REFERENCE A57981 !$#authors Tsukihara, T.; Aoyama, H.; Yamashita, E.; Tomizaki, T.; !1Yamaguchi, H.; Sinzawa-Itoh, K.; Nakashima, R.; Yaono, R.; !1Yoshikawa, S. !$#journal Science (1996) 272:1136-1144 !$#title The whole structure of the 13-subunit oxidized cytochrome c !1oxidase at 2.8 angstroms. !$#cross-references MUID:96216288; PMID:8638158 !$#contents annotation; X-ray crystallography, 2.8 angstroms GENETICS !$#genome nuclear COMPLEX part of a 13 chain complex spanning the inner mitochondrial !1membrane and consisting of one each of chains I (see !1PIR:ODBO1), II (see PIR:OBBO2), III (see PIR:OTBO3), IV, Va !1(see PIR:CABO), Vb (see PIR:OGBO6A), VIa (see PIR:OGBO6), !1VIb (see PIR:OGBO7), VIc (see PIR:OGBO6C), VIIa (see !1PIR:OSBO7A), VIIb (see PIR:OSBO7B), VIIc (see PIR:OSBO8A), !1VIII (see PIR:OSBO8); the complex may form dimers within the !1mitochondrial inner-membrane FUNCTION !$#description the cytochrome-c oxidase complex catalyzes the oxidation of !1four molecules of reduced cytochrome c in the intracristal !1(or intermembrane) space using one oxygen molecule and four !1protons from the mitochondrial matrix producing two !1molecules of water and lowering the concentration of protons !1in the mitochondrial matrix !$#pathway oxidative phosphorylation; respiratory chain !$#note the role of chain IV is not clear CLASSIFICATION #superfamily cytochrome-c oxidase chain IV KEYWORDS electron transfer; membrane-associated complex; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$1-22 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$23-169 #product cytochrome-c oxidase chain IV #status !8experimental #label MAT\ !$23-76 #domain mitochondrial matrix #status experimental !8#label MM1\ !$77-103 #domain transmembrane helix #status experimental !8#label TR01\ !$104-169 #domain intracristal #status experimental #label ITC1 SUMMARY #length 169 #molecular-weight 19571 #checksum 741 SEQUENCE /// ENTRY A35209 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain IV precursor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Aug-1990 #sequence_revision 10-Aug-1990 #text_change 11-Jun-1999 ACCESSIONS A35209; S12724; S04070; S04593; S14190; S65373 REFERENCE A35209 !$#authors Yamada, M.; Amuro, N.; Goto, Y.; Okazaki, T. !$#journal J. Biol. Chem. (1990) 265:7687-7692 !$#title Structural organization of the rat cytochrome c oxidase !1subunit IV gene. !$#cross-references MUID:90237079; PMID:2159010 !$#accession A35209 !'##status preliminary !'##molecule_type DNA !'##residues 1-169 ##label YAM !'##cross-references GB:J05425; NID:g203516; PIDN:AAA40949.1; !1PID:g203517 REFERENCE S12724 !$#authors Amuro, N.; Yamada, M.; Goto, Y.; Okazaki, T. !$#journal Nucleic Acids Res. (1990) 18:3992 !$#title Complete nucleotide sequence of the gene encoding rat !1cytochrome c oxidase subunit IV. !$#cross-references MUID:90326528; PMID:2165254 !$#accession S12724 !'##status preliminary !'##molecule_type DNA !'##residues 1-169 ##label AMU !'##cross-references EMBL:J05425; NID:g203516; PIDN:AAA40949.1; !1PID:g203517 REFERENCE S04070 !$#authors Goto, Y.; Amuro, N.; Okazaki, T. !$#journal Nucleic Acids Res. (1989) 17:2851 !$#title Nucleotide sequence of cDNA for rat brain and liver !1cytochrome c oxidase subunit IV. !$#cross-references MUID:89240039; PMID:2541414 !$#accession S04070 !'##molecule_type mRNA !'##residues 1-169 ##label GOT !'##cross-references EMBL:X14209; NID:g55989; PIDN:CAA32426.1; !1PID:g55990 REFERENCE S04593 !$#authors Gopalan, G.; Droste, M.; Kadenbach, B. !$#journal Nucleic Acids Res. (1989) 17:4376 !$#title Nucleotide sequence of cDNA encoding subunit IV of !1cytochrome c oxidase from fetal rat liver. !$#cross-references MUID:89296488; PMID:2544859 !$#accession S04593 !'##molecule_type mRNA !'##residues 1-169 ##label GOP !'##cross-references EMBL:X15029; NID:g55980; PIDN:CAA33133.1; !1PID:g55981 REFERENCE S14190 !$#authors Virbasius, J.V.; Scarpulla, R.C. !$#journal Nucleic Acids Res. (1990) 18:6581-6586 !$#title The rat cytochrome c oxidase subunit IV gene family: !1tissue-specific and hormonal differences in subunit IV and !1cytochrome c mRNA expression. !$#cross-references MUID:91067442; PMID:2174541 !$#accession S14190 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type mRNA !'##residues 1-169 ##label VIR !'##cross-references EMBL:X54081; NID:g57030; PIDN:CAA38018.1; !1PID:g57031 !'##experimental_source strain Sprague Dawley !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1990 REFERENCE S65372 !$#authors Schaegger, H.; Noack, H.; Halangk, W.; Brandt, U.; von !1Jagow, G. !$#journal Eur. J. Biochem. (1995) 230:235-241 !$#title Cytochrome-c oxidase in developing rat heart. Enzymic !1properties and amino-terminal sequences suggest identity of !1the fetal heart and the adult liver isoform. !$#cross-references MUID:95324529; PMID:7601105 !$#accession S65373 !'##status preliminary !'##molecule_type protein !'##residues 23-45 ##label SCH GENETICS !$#gene RCO4-1 !$#introns 25/1; 81/1; 125/1 FUNCTION !$#description the cytochrome-c oxidase complex catalyzes the oxidation of !1four molecules of reduced cytochrome c in the intracristal !1(or intermembrane) space using one oxygen molecule and four !1protons from the mitochondrial matrix producing two !1molecules of water and lowering the concentration of protons !1in the mitochondrial matrix !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily cytochrome-c oxidase chain IV KEYWORDS electron transfer; membrane-associated complex; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$1-22 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$23-169 #product cytochrome-c oxidase chain IV #status !8experimental #label MAT\ !$77-103 #domain transmembrane helix #status predicted #label !8TR01 SUMMARY #length 169 #molecular-weight 19514 #checksum 1878 SEQUENCE /// ENTRY S12142 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain IV precursor - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S12142; S16114 REFERENCE S12142 !$#authors Grossman, L.I.; Akamatsu, M. !$#journal Nucleic Acids Res. (1990) 18:6454 !$#title Nucleotide sequence of a mouse cDNA for subunit IV of !1cytochrome c oxidase. !$#cross-references MUID:91057158; PMID:2173832 !$#accession S12142 !'##molecule_type mRNA !'##residues 1-169 ##label GRO !'##cross-references EMBL:X54691; NID:g50518; PIDN:CAA38507.1; !1PID:g50519 !'##experimental_source strain Balb/c REFERENCE S16114 !$#authors Carter, R.S.; Avadhani, N.G. !$#journal Arch. Biochem. Biophys. (1991) 288:97-106 !$#title Cloning and characterization of the mouse cytochrome c !1oxidase subunit IV gene. !$#cross-references MUID:91378465; PMID:1654830 !$#accession S16114 !'##molecule_type mRNA !'##residues 1-169 ##label ARC GENETICS !$#gene COXIV !$#genome nuclear CLASSIFICATION #superfamily cytochrome-c oxidase chain IV KEYWORDS membrane-associated complex; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain FEATURE !$1-22 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$23-169 #product cytochrome-c oxidase chain IV #status !8predicted #label MAT SUMMARY #length 169 #molecular-weight 19530 #checksum 482 SEQUENCE /// ENTRY S19718 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain V - slime mold (Dictyostelium discoideum) ORGANISM #formal_name Dictyostelium discoideum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S19718; S34106; S30445 REFERENCE S19718 !$#authors Rizzuto, R.; Sandona, D.; Brini, M.; Capaldi, R.A.; Bisson, !1R. !$#journal Biochim. Biophys. Acta (1991) 1129:100-104 !$#title The most conserved nuclear-encoded polypeptide of cytochrome !1c oxidase is the putative zinc-binding subunit: primary !1structure of subunit V from the slime mold Dictyostelium !1discoideum. !$#cross-references MUID:92096446; PMID:1661610 !$#accession S19718 !'##molecule_type mRNA !'##residues 1-120 ##label RIZ !'##cross-references EMBL:X55671; NID:g10925; PIDN:CAA39206.1; !1PID:g10926 !$#accession S34106 !'##molecule_type protein !'##residues 41-60 ##label RI2 REFERENCE S30445 !$#authors Rizzuto, R.; Brini, M.; Sandona, D.; Bisson, R.; Marschalek, !1R.; Dingermann, T. !$#journal Eur. J. Biochem. (1993) 211:411-414 !$#title Structure of the promoter region of the gene encoding !1cytochrome c oxidase subunit V in Dictyostelium. !$#cross-references MUID:93170268; PMID:8382151 !$#accession S30445 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type mRNA !'##residues 1-32 ##label RI3 !'##cross-references EMBL:X64771; NID:g296579; PIDN:CAA46018.1; !1PID:g296580 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1February 1992 CLASSIFICATION #superfamily Dictyostelium cytochrome-c oxidase chain V KEYWORDS electron transfer; mitochondrion; oxidoreductase; !1respiratory chain SUMMARY #length 120 #molecular-weight 13497 #checksum 8280 SEQUENCE /// ENTRY OTBY5A #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain V.A precursor - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein N2474; protein YNL052w; protein YNL1628 ORGANISM #formal_name Saccharomyces cerevisiae DATE 27-Nov-1985 #sequence_revision 30-Sep-1991 #text_change 21-Jul-2000 ACCESSIONS S05833; S07606; A23906; A05018; A05013; S58724; S62980; !1S42149; A00491 REFERENCE S05831 !$#authors Seraphin, B.; Simon, M.; Faye, G. !$#journal Curr. Genet. (1985) 9:435-439 !$#title Primary structure of a gene for subunit V of the cytochrome !1c oxidase from Saccharomyces cerevisiae. !$#cross-references MUID:88223509; PMID:2836092 !$#accession S05833 !'##molecule_type DNA !'##residues 1-153 ##label SER !'##cross-references EMBL:X02561; NID:g3568; PIDN:CAA26403.1; PID:g3570 REFERENCE S05755 !$#authors Cumsky, M.G.; Trueblood, C.E.; Ko, C.; Poyton, R.O. !$#journal Mol. Cell. Biol. (1987) 7:3511-3519 !$#title Structural analysis of two genes encoding divergent forms of !1yeast cytochrome c oxidase subunit V. !$#cross-references MUID:88065487; PMID:2824989 !$#accession S07606 !'##molecule_type DNA !'##residues 1-153 ##label CUM !'##cross-references EMBL:M17800; NID:g171288; PIDN:AAA34520.1; !1PID:g171289 REFERENCE A23906 !$#authors Koerner, T.J.; Hill, J.; Tzagoloff, A. !$#journal J. Biol. Chem. (1985) 260:9513-9515 !$#title Cloning and characterization of the yeast nuclear gene for !1subunit 5 of cytochrome oxidase. !$#cross-references MUID:85261346; PMID:2991248 !$#accession A23906 !'##molecule_type DNA !'##residues 1-153 ##label KOE !'##cross-references GB:M11770; NID:g171282; PIDN:AAA34518.1; !1PID:g171283 REFERENCE A05016 !$#authors Power, S.D.; Lochrie, M.A.; Poyton, R.O. !$#journal J. Biol. Chem. (1984) 259:6575-6578 !$#title The nuclear-coded subunits of yeast cytochrome c oxidase. !1III. Identification of homologous subunits in yeast, bovine !1heart, and Neurospora crassa cytochrome c oxidases. !$#cross-references MUID:84212484; PMID:6327686 !$#accession A05018 !'##molecule_type protein !'##residues 21-50,'X',52-88 ##label POW REFERENCE A05013 !$#authors Cerletti, N.; Bohni, P.C.; Suda, K. !$#journal J. Biol. Chem. (1983) 258:4944-4949 !$#title Import of proteins into mitochondria. Isolated yeast !1mitochondria and a solubilized matrix protease correctly !1process cytochrome c oxidase subunit V precursor at the NH !1(2) terminus. !$#cross-references MUID:83161105; PMID:6300105 !$#accession A05013 !'##molecule_type protein !'##residues 21-35 ##label CER REFERENCE S58711 !$#authors Bergez, P.; Doignon, F.; Crouzet, M. !$#journal Yeast (1995) 11:967-974 !$#title The sequence of a 44 420 bp fragment located on the left arm !1of chromosome XIV from Saccharomyces cerevisiae. !$#cross-references MUID:96021608; PMID:8533472 !$#accession S58724 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-153 ##label BER !'##cross-references EMBL:U12141; NID:g1314216; PIDN:AAA99660.1; !1PID:g994833 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1994 REFERENCE S62975 !$#authors Bergez, P.; Doignon, F.; Crouzet, M. !$#submission submitted to the Protein Sequence Database, April 1996 !$#accession S62980 !'##molecule_type DNA !'##residues 1-153 ##label BEW !'##cross-references EMBL:Z71328; NID:g2253171; PIDN:CAA95921.1; !1PID:g1301915; GSPDB:GN00014; MIPS:YNL052w !'##experimental_source strain S288C REFERENCE A94032 !$#authors Cumsky, M.G.; Ko, C.; Trueblood, C.E.; Poyton, R.O. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:2235-2239 !$#title Two nonidentical forms of subunit V are functional in yeast !1cytochrome c oxidase. !$#cross-references MUID:85190471; PMID:2986105 !$#accession S42149 !'##molecule_type DNA !'##residues 21-88 ##label CUW !'##cross-references EMBL:M11141; NID:g171284; PIDN:AAA34519.1; !1PID:g171285 GENETICS !$#gene SGD:COX5A; MIPS:YNL052w !'##cross-references SGD:S0004997; MIPS:YNL052w !$#map_position 14L !$#genome nuclear CLASSIFICATION #superfamily yeast cytochrome-c oxidase chain V KEYWORDS membrane-associated complex; mitochondrial inner membrane; !1mitochondrion; oxidative phosphorylation; oxidoreductase; !1respiratory chain FEATURE !$1-20 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$21-153 #product cytochrome-c oxidase chain V.A #status !8experimental #label MAT SUMMARY #length 153 #molecular-weight 17140 #checksum 5621 SEQUENCE /// ENTRY OTBY5B #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain V.B precursor - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YIL111w ORGANISM #formal_name Saccharomyces cerevisiae DATE 27-Nov-1985 #sequence_revision 30-Sep-1991 #text_change 21-Jul-2000 ACCESSIONS S05755; A38762; S48461; S42148; A00492 REFERENCE S05755 !$#authors Cumsky, M.G.; Trueblood, C.E.; Ko, C.; Poyton, R.O. !$#journal Mol. Cell. Biol. (1987) 7:3511-3519 !$#title Structural analysis of two genes encoding divergent forms of !1yeast cytochrome c oxidase subunit V. !$#cross-references MUID:88065487; PMID:2824989 !$#accession S05755 !'##molecule_type DNA !'##residues 1-151 ##label CUM !'##cross-references EMBL:M17799; NID:g171292; PIDN:AAA96310.1; !1PID:g171293 !$#accession A38762 !'##molecule_type mRNA !'##residues 1-36 ##label CUM2 REFERENCE S48455 !$#authors Bowman, S.; Churcher, C. !$#submission submitted to the EMBL Data Library, September 1994 !$#accession S48461 !'##molecule_type DNA !'##residues 1-151 ##label BOW !'##cross-references GB:Z47047; EMBL:Z38125; NID:g603997; PID:g763235; !1GSPDB:GN00009; MIPS:YIL111w REFERENCE A94032 !$#authors Cumsky, M.G.; Ko, C.; Trueblood, C.E.; Poyton, R.O. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:2235-2239 !$#title Two nonidentical forms of subunit V are functional in yeast !1cytochrome c oxidase. !$#cross-references MUID:85190471; PMID:2986105 !$#accession S42148 !'##molecule_type DNA !'##residues 18-85 ##label CUW !'##cross-references EMBL:M11140; NID:g171290; PIDN:AAA34521.1; !1PID:g171291 GENETICS !$#gene SGD:COX5b; MIPS:YIL111w !'##cross-references SGD:S0001373; MIPS:YIL111w !$#map_position 9L !$#genome nuclear !$#introns 1/1 CLASSIFICATION #superfamily yeast cytochrome-c oxidase chain V KEYWORDS membrane-associated complex; mitochondrial inner membrane; !1mitochondrion; oxidative phosphorylation; oxidoreductase; !1respiratory chain FEATURE !$1-17 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$18-151 #product cytochrome-c oxidase chain V.B #status !8predicted #label MAT SUMMARY #length 151 #molecular-weight 17197 #checksum 6065 SEQUENCE /// ENTRY OTNCV #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain V precursor [similarity] - Neurospora crassa ALTERNATE_NAMES protein B8B20.30 ORGANISM #formal_name Neurospora crassa DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 09-Jun-2000 ACCESSIONS A30134; A38751; B25629; T49649 REFERENCE A30134 !$#authors Sachs, M.S.; Bertrand, H.; Metzenberg, R.L.; Rajbhandary, !1U.L. !$#journal Mol. Cell. Biol. (1989) 9:566-577 !$#title Cytochrome oxidase subunit V gene of Neurospora crassa: DNA !1sequences, chromosomal mapping, and evidence that the cya-4 !1locus specifies the structural gene for subunit V. !$#cross-references MUID:89219050; PMID:2540423 !$#accession A30134 !'##molecule_type DNA !'##residues 1-171 ##label SAC !'##cross-references GB:M24389; NID:g341160 !'##note the translated sequence in GenBank entry NEUCOXV, release 114, !1(PIDN:AAA31957.1) differs from the published sequence in !1having 44-Ser !$#accession A38751 !'##molecule_type mRNA !'##residues 1-171 ##label SA1 REFERENCE A92592 !$#authors Sachs, M.S.; David, M.; Werner, S.; RajBhandary, U.L. !$#journal J. Biol. Chem. (1986) 261:869-873 !$#title Nuclear genes for cytochrome c oxidase subunits of !1Neurospora crassa. !$#cross-references MUID:86085927; PMID:3001085 !$#accession B25629 !'##molecule_type mRNA !'##residues 1-67 ##label SA2 !'##cross-references GB:M12117; NID:g168788; PIDN:AAA33575.1; !1PID:g168789 REFERENCE Z25022 !$#authors Schulte, U.; Aign, V.; Hoheisel, J.; Brandt, P.; Fartmann, !1B.; Holland, R.; Nyakatura, G.; Mewes, H.W.; Mannhaupt, G. !$#submission submitted to the Protein Sequence Database, May 2000 !$#accession T49649 !'##status preliminary !'##molecule_type DNA !'##residues 1-171 ##label SCH !'##cross-references EMBL:AL355933; GSPDB:GN00116; NCSP:B8B20.30 !'##experimental_source BAC clone B8B20; strain OR74A GENETICS !$#gene NCSP:B8B20.30 !$#map_position 6 !$#introns 79/1; 143/3 CLASSIFICATION #superfamily yeast cytochrome-c oxidase chain V KEYWORDS membrane-associated complex; mitochondrial inner membrane; !1mitochondrion; oxidative phosphorylation; oxidoreductase; !1respiratory chain; transmembrane protein FEATURE !$1-27 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$28-171 #product cytochrome-c oxidase chain V #status !8predicted #label MAT\ !$101-119 #domain transmembrane #status predicted #label TMM SUMMARY #length 171 #molecular-weight 18804 #checksum 9373 SEQUENCE /// ENTRY OTHU5A #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain Va precursor - human ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 11-Jun-1999 ACCESSIONS JT0342 REFERENCE JT0342 !$#authors Rizzuto, R.; Nakase, H.; Zeviani, M.; DiMauro, S.; Schon, !1E.A. !$#journal Gene (1988) 69:245-256 !$#title Subunit Va of human and bovine cytochrome c oxidase is !1highly conserved. !$#cross-references MUID:89172069; PMID:2853101 !$#accession JT0342 !'##molecule_type mRNA !'##residues 1-150 ##label RIZ !'##cross-references GB:M22760; NID:g695359; PIDN:AAA99220.1; !1PID:g695360 GENETICS !$#gene COX5A !$#genome nuclear COMPLEX part of a 13 chain complex spanning the inner mitochondrial !1membrane and consisting of one each of chains I (see !1PIR:ODHU1), II (see PIR:OBHU2), III (see PIR:OTHU3), IV (see !1PIR:OLHU4), Va, Vb (see PIR:OTHU5B), VIa (see PIR:OGHU6A), !1VIb (see PIR:OGHU6B), VIc (see PIR:OGHU6C), VIIa (see !1PIR:OSHU7A), VIIb (see PIR:OSHU7B), VIIc (see PIR:OSHU7C), !1VIII (see PIR:OSHU8); the complex may form dimers within the !1mitochondrial inner-membrane FUNCTION !$#description the cytochrome-c oxidase complex catalyzes the oxidation of !1four molecules of reduced cytochrome c in the intracristal !1(or intermembrane) space using one oxygen molecule and four !1protons from the mitochondrial matrix producing two !1molecules of water and lowering the concentration of protons !1in the mitochondrial matrix !$#pathway oxidative phosphorylation; respiratory chain !$#note the role of chain Va is not clear CLASSIFICATION #superfamily mammalian cytochrome-c oxidase chain Va KEYWORDS electron transfer; membrane-associated complex; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain FEATURE !$1-41 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$42-150 #product cytochrome-c oxidase chain Va #status !8predicted #label MAT\ !$42-150 #domain mitochondrial matrix #status predicted #label !8MM1 SUMMARY #length 150 #molecular-weight 16774 #checksum 1976 SEQUENCE /// ENTRY CABO #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain Va [validated] - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Nov-1979 #sequence_revision 08-Oct-1981 #text_change 15-Sep-2000 ACCESSIONS A00493; D29968 REFERENCE A00493 !$#authors Tanaka, M.; Haniu, M.; Yasunobu, K.T.; Yu, C.A.; Yu, L.; !1Wei, Y.H.; King, T.E. !$#journal J. Biol. Chem. (1979) 254:3879-3885 !$#title Amino acid sequence of subunit V of bovine heart cytochrome !1oxidase, the heme a-containing subunit. !$#cross-references MUID:79173095; PMID:220224 !$#accession A00493 !'##molecule_type protein !'##residues 1-109 ##label TAN !'##experimental_source heart REFERENCE A90531 !$#authors Yanamura, W.; Zhang, Y.Z.; Takamiya, S.; Capaldi, R.A. !$#journal Biochemistry (1988) 27:4909-4914 !$#title Tissue-specific differences between heart and liver !1cytochrome c oxidase. !$#cross-references MUID:89000697; PMID:2844245 !$#accession D29968 !'##molecule_type protein !'##residues 1-34 ##label YAN !'##experimental_source liver REFERENCE A67451 !$#authors Tsukihara, T.; Aoyama, H.; Yamashita, E.; Tomizaki, T.; !1Yamaguchi, H.; Shinzawa-itoh, K.; Nakashima, R.; Yaono, R.; !1Yoshikawa, S. !$#submission submitted to the Brookhaven Protein Data Bank, April 1996 !$#cross-references PDB:1OCC !$#contents annotation; X-ray crystallography, 2.8 angstroms, residues !11-109 REFERENCE A57981 !$#authors Tsukihara, T.; Aoyama, H.; Yamashita, E.; Tomizaki, T.; !1Yamaguchi, H.; Sinzawa-Itoh, K.; Nakashima, R.; Yaono, R.; !1Yoshikawa, S. !$#journal Science (1996) 272:1136-1144 !$#title The whole structure of the 13-subunit oxidized cytochrome c !1oxidase at 2.8 angstroms. !$#cross-references MUID:96216288; PMID:8638158 !$#contents annotation; X-ray crystallography, 2.8 angstroms GENETICS !$#genome nuclear COMPLEX part of a 13 chain complex spanning the inner mitochondrial !1membrane and consisting of one each of chains I (see !1PIR:ODBO1), II (see PIR:OBBO2), III (see PIR:OTBO3), IV (see !1PIR:OLBO4), Va, Vb (see PIR:OGBO6A), VIa (see PIR:OGBO6), !1VIb (see PIR:OGBO7), VIc (see PIR:OGBO6C), VIIa (see !1PIR:OSBO7A), VIIb (see PIR:OSBO7B), VIIc (see PIR:OSBO8A), !1VIII (see PIR:OSBO8); the complex may form dimers within the !1mitochondrial inner-membrane FUNCTION !$#description the cytochrome-c oxidase complex catalyzes the oxidation of !1four molecules of reduced cytochrome c in the intracristal !1(or intermembrane) space using one oxygen molecule and four !1protons from the mitochondrial matrix producing two !1molecules of water and lowering the concentration of protons !1in the mitochondrial matrix !$#pathway oxidative phosphorylation; respiratory chain !$#note the role of chain Va is not clear CLASSIFICATION #superfamily mammalian cytochrome-c oxidase chain Va KEYWORDS electron transfer; membrane-associated complex; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain FEATURE !$1-109 #product cytochrome-c oxidase chain Va #status !8experimental #label MAT\ !$1-109 #domain mitochondrial matrix #status experimental !8#label MM1 SUMMARY #length 109 #molecular-weight 12436 #checksum 9720 SEQUENCE /// ENTRY S05495 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain Va precursor - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S05495 REFERENCE S05495 !$#authors Nielsen, P.J.; Ayane, M.; Koehler, G. !$#journal Nucleic Acids Res. (1989) 17:6723 !$#title Nucleotide sequence of cDNA encoding mouse cytochrome c !1oxidase subunit Va. !$#cross-references MUID:89385997; PMID:2550898 !$#accession S05495 !'##molecule_type mRNA !'##residues 1-145 ##label NIE !'##cross-references EMBL:X15963; NID:g50526; PIDN:CAA34085.1; !1PID:g50527 CLASSIFICATION #superfamily mammalian cytochrome-c oxidase chain Va KEYWORDS membrane-associated complex; mitochondrial inner membrane; !1mitochondrion; oxidative phosphorylation; oxidoreductase; !1respiratory chain FEATURE !$1-36 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$37-145 #product cytochrome-c oxidase chain Va #status !8predicted #label MAT SUMMARY #length 145 #molecular-weight 16030 #checksum 6297 SEQUENCE /// ENTRY S04592 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain Va precursor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S04592; S65376 REFERENCE S04592 !$#authors Droste, M.; Schon, E.; Kadenbach, B. !$#journal Nucleic Acids Res. (1989) 17:4375 !$#title Nucleotide sequence of cDNA encoding subunit Va from rat !1heart cytochrome c oxidase. !$#cross-references MUID:89296487; PMID:2544858 !$#accession S04592 !'##molecule_type mRNA !'##residues 1-146 ##label DRO !'##cross-references EMBL:X15030; NID:g55970; PIDN:CAA33134.1; !1PID:g55971 REFERENCE S65372 !$#authors Schaegger, H.; Noack, H.; Halangk, W.; Brandt, U.; von !1Jagow, G. !$#journal Eur. J. Biochem. (1995) 230:235-241 !$#title Cytochrome-c oxidase in developing rat heart. Enzymic !1properties and amino-terminal sequences suggest identity of !1the fetal heart and the adult liver isoform. !$#cross-references MUID:95324529; PMID:7601105 !$#accession S65376 !'##status preliminary !'##molecule_type protein !'##residues 38-47 ##label SCH CLASSIFICATION #superfamily mammalian cytochrome-c oxidase chain Va KEYWORDS membrane-associated complex; mitochondrial inner membrane; !1mitochondrion; oxidative phosphorylation; oxidoreductase; !1respiratory chain FEATURE !$1-37 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$38-146 #product cytochrome-c oxidase chain Va #status !8experimental #label MAT SUMMARY #length 146 #molecular-weight 16129 #checksum 9266 SEQUENCE /// ENTRY OTBY6 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain VI precursor - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein H8179.2; protein YHR051w ORGANISM #formal_name Saccharomyces cerevisiae DATE 13-Jun-1983 #sequence_revision 31-Dec-1992 #text_change 23-Mar-2001 ACCESSIONS A22853; S46730; A00494; S48874 REFERENCE A92466 !$#authors Wright, R.M.; Ko, C.; Cumsky, M.G.; Poyton, R.O. !$#journal J. Biol. Chem. (1984) 259:15401-15407 !$#title Isolation and sequence of the structural gene for cytochrome !1c oxidase subunit VI from Saccharomyces cerevisiae. !$#cross-references MUID:85080033; PMID:6210289 !$#accession A22853 !'##molecule_type DNA !'##residues 1-148 ##label WRI !'##cross-references EMBL:M10138; NID:g171294; PIDN:AAA66900.1; !1PID:g171295 REFERENCE S46732 !$#authors Du, Z. !$#submission submitted to the EMBL Data Library, May 1994 !$#description The sequence of S. cerevisiae cosmid 8179. !$#accession S46730 !'##molecule_type DNA !'##residues 1-148 ##label DUZ !'##cross-references EMBL:U00062; NID:g488162; PIDN:AAB68899.1; !1PID:g488164; GSPDB:GN00008; MIPS:YHR051w REFERENCE A00494 !$#authors Gregor, I.; Tsugita, A. !$#journal J. Biol. Chem. (1982) 257:13081-13087 !$#title The amino acid sequence of cytochrome c oxidase subunit VI !1from Saccharomyces cerevisiae. !$#cross-references MUID:83030850; PMID:6290493 !$#accession A00494 !'##molecule_type protein !'##residues 41-148 ##label GRE REFERENCE S48872 !$#authors Wright, R.M.; Rosenzweig, B.; Poyton, R.O. !$#journal Nucleic Acids Res. (1989) 17:1103-1120 !$#title Organization and expression of the COX6 genetic locus in !1Saccharomyces cerevisiae: multiple mRNAs with different 3' !1termini are transcribed from COX6 and regulated !1differentially. !$#cross-references MUID:89160242; PMID:2537949 !$#accession S48874 !'##molecule_type DNA !'##residues 1-23 ##label WRW !'##cross-references EMBL:X14452; NID:g3573; PIDN:CAA32622.1; PID:g3576 COMMENT Cytochrome-c oxidase is the terminal component of the !1respiratory chain; it transfers electrons from cytochrome c !1to molecular oxygen. GENETICS !$#gene SGD:COX6; MIPS:YHR051w !'##cross-references SGD:S0001093; MIPS:YHR051w !$#map_position 8R !$#genome nuclear FUNCTION !$#description oxidoreductase !$#pathway oxidative phosphorylation; respiratory chain CLASSIFICATION #superfamily mammalian cytochrome-c oxidase chain Va KEYWORDS membrane-associated complex; mitochondrial inner membrane; !1mitochondrion; oxidative phosphorylation; oxidoreductase; !1respiratory chain FEATURE !$1-40 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$41-148 #product cytochrome-c oxidase chain VI #status !8experimental #label MAT SUMMARY #length 148 #molecular-weight 17341 #checksum 6173 SEQUENCE /// ENTRY OTHU5B #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain Vb precursor - human ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1992 #sequence_revision 07-Jun-1996 #text_change 11-Jun-1999 ACCESSIONS JT0324; A39063; S74198; A28817 REFERENCE JT0324 !$#authors Zeviani, M.; Sakoda, S.; Sherbany, A.A.; Nakase, H.; !1Rizzuto, R.; Samitt, C.E.; DiMauro, S.; Schon, E.A. !$#journal Gene (1988) 65:1-11 !$#title Sequence of cDNAs encoding subunit Vb of human and bovine !1cytochrome c oxidase. !$#cross-references MUID:88284368; PMID:2840351 !$#accession JT0324 !'##molecule_type mRNA !'##residues 1-129 ##label ZEV !'##cross-references EMBL:M19961; NID:g180940; PIDN:AAA52061.1; !1PID:g180941 REFERENCE A39063 !$#authors Lomax, M.I.; Hsieh, C.L.; Darras, B.T.; Francke, U. !$#journal Genomics (1991) 10:1-9 !$#title Structure of the human cytochrome c oxidase subunit Vb gene !1and chromosomal mapping of the coding gene and of seven !1pseudogenes. !$#cross-references MUID:91257815; PMID:1646156 !$#accession A39063 !'##status preliminary !'##molecule_type DNA !'##residues 1-108,'E',110-129 ##label LOM !'##cross-references EMBL:M59250 !'##note the authors translated the codon GGC for residue 21 as His REFERENCE S74198 !$#authors Bachman, N.J.; Yang, T.L.; Dasen, J.S.; Ernst, R.E.; Lomax, !1M.I. !$#journal Arch. Biochem. Biophys. (1996) 333:152-162 !$#title Phylogenetic footprinting of the human cytochrome c oxidase !1subunit Vb promoter. !$#cross-references MUID:96400390; PMID:8806766 !$#accession S74198 !'##status translation not shown !'##molecule_type DNA !'##residues 1-35,'TR' ##label BAC !'##cross-references EMBL:U41284; NID:g1679627; PIDN:AAB19185.1; !1PID:g1679628 GENETICS !$#gene GDB:COX5B !'##cross-references GDB:127530; OMIM:123866 !$#map_position 2cen-2q13 !$#genome nuclear COMPLEX part of a 13 chain complex spanning the inner mitochondrial !1membrane and consisting of one each of chains I (see !1PIR:ODHU1), II (see PIR:OBHU2), III (see PIR:OTHU3), IV (see !1PIR:OLHU4), Va (see PIR:OTHU5A), Vb, VIa (see PIR:OGHU6A), !1VIb (see PIR:OGHU6B), VIc (see PIR:OGHU6C), VIIa (see !1PIR:OSHU7A), VIIb (see PIR:OSHU7B), VIIc (see PIR:OSHU7C), !1VIII (see PIR:OSHU8); the complex may form dimers within the !1mitochondrial inner-membrane FUNCTION !$#description the cytochrome-c oxidase complex catalyzes the oxidation of !1four molecules of reduced cytochrome c in the intracristal !1(or intermembrane) space using one oxygen molecule and four !1protons from the mitochondrial matrix producing two !1molecules of water and lowering the concentration of protons !1in the mitochondrial matrix !$#note the role of chain Vb is not clear CLASSIFICATION #superfamily mammalian cytochrome-c oxidase chain Vb KEYWORDS electron transfer; membrane-associated complex; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain; zinc FEATURE !$1-31 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$32-129 #product cytochrome-c oxidase chain Vb #status !8predicted #label MAT\ !$91,93,113,116 #binding_site zinc (Cys) #status predicted SUMMARY #length 129 #molecular-weight 13695 #checksum 8000 SEQUENCE /// ENTRY A39425 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain Vb precursor - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A39425; S11389 REFERENCE A39425 !$#authors Basu, A.; Avadhani, N.G. !$#journal J. Biol. Chem. (1991) 266:15450-15456 !$#title Structural organization of nuclear gene for subunit Vb of !1mouse mitochondrial cytochrome c oxidase. !$#cross-references MUID:91332074; PMID:1651332 !$#accession A39425 !'##status preliminary !'##molecule_type DNA !'##residues 1-128 ##label BAS !'##cross-references GB:M77040; GB:M38201; NID:g192923; PIDN:AAA37515.1; !1PID:g192924 REFERENCE S11389 !$#authors Basu, A.; Avadhani, N.G. !$#journal Biochim. Biophys. Acta (1990) 1087:98-100 !$#title Nucleotide sequence of cDNA for nuclear encoded subunit Vb !1of mouse cytochrome-c oxidase. !$#cross-references MUID:90381323; PMID:2169317 !$#accession S11389 !'##molecule_type mRNA !'##residues 1-128 ##label BA2 !'##cross-references EMBL:X53157; NID:g50530; PIDN:CAA37313.1; !1PID:g50531 CLASSIFICATION #superfamily mammalian cytochrome-c oxidase chain Vb KEYWORDS membrane-associated complex; mitochondrial inner membrane; !1mitochondrion; oxidative phosphorylation; oxidoreductase; !1respiratory chain FEATURE !$1-30 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$31-128 #product cytochrome-c oxidase chain Vb #status !8predicted #label MAT SUMMARY #length 128 #molecular-weight 13813 #checksum 6739 SEQUENCE /// ENTRY JC2254 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain Vb precursor - rat ALTERNATE_NAMES cytochrome-c oxidase (EC 1.9.3.1) chain VIa* ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 28-Oct-1994 #sequence_revision 26-May-1995 #text_change 16-Jun-2000 ACCESSIONS JC2254; JC2255; S05318; S65375 REFERENCE JC2254 !$#authors Hoshinaga, H.; Amuro, N.; Goto, Y.; Okazaki, T. !$#journal J. Biochem. (1994) 115:194-201 !$#title Molecular cloning and characterization of the rat cytochrome !1c oxidase subunit Vb gene. !$#cross-references MUID:94266742; PMID:8206867 !$#accession JC2254 !'##molecule_type mRNA !'##residues 1-129 ##label HOS !'##cross-references DDBJ:D10952; NID:g493694; PIDN:BAA01744.1; !1PID:g493695 !'##experimental_source liver !$#accession JC2255 !'##molecule_type DNA !'##residues 1-129 ##label HO2 !'##cross-references DDBJ:D10951 !'##experimental_source lambda COXVb741 REFERENCE S05318 !$#authors Goto, Y.; Amuro, N.; Okazaki, T. !$#journal Nucleic Acids Res. (1989) 17:6388 !$#title Nucleotide sequence of cDNA for rat liver and brain !1cytochrome c oxidase subunit VIa* (Vb). !$#cross-references MUID:89366668; PMID:2549512 !$#accession S05318 !'##molecule_type mRNA !'##residues 31-129 ##label GOT !'##cross-references EMBL:X14208 REFERENCE S65372 !$#authors Schaegger, H.; Noack, H.; Halangk, W.; Brandt, U.; von !1Jagow, G. !$#journal Eur. J. Biochem. (1995) 230:235-241 !$#title Cytochrome-c oxidase in developing rat heart. Enzymic !1properties and amino-terminal sequences suggest identity of !1the fetal heart and the adult liver isoform. !$#cross-references MUID:95324529; PMID:7601105 !$#accession S65375 !'##molecule_type protein !'##residues 32-41 ##label SCH !'##experimental_source liver GENETICS !$#gene COXVb-1 !$#introns 35/1; 59/3; 93/1 !$#note intronless gene COXVb-2 apparently a nonfunctional processed !1pseudogene CLASSIFICATION #superfamily mammalian cytochrome-c oxidase chain Vb KEYWORDS membrane-associated complex; mitochondrial inner membrane; !1mitochondrion; oxidative phosphorylation; oxidoreductase; !1respiratory chain FEATURE !$1-31 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$32-129 #product cytochrome-c oxidase chain Vb #status !8predicted #label MAT SUMMARY #length 129 #molecular-weight 13915 #checksum 9143 SEQUENCE /// ENTRY OGBO6A #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain Vb [validated] - bovine ALTERNATE_NAMES cytochrome-c oxidase chain VIa ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 15-Sep-2000 ACCESSIONS A00495; E29968; JT0325; B28817 REFERENCE A00495 !$#authors Biewald, R.; Buse, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1982) 363:1141-1153 !$#title Studies on cytochrome c oxidase, IX. The primary structure !1of polypeptide VIa. !$#cross-references MUID:83055083; PMID:6292069 !$#accession A00495 !'##molecule_type protein !'##residues 1-98 ##label BIE !'##experimental_source heart REFERENCE A90531 !$#authors Yanamura, W.; Zhang, Y.Z.; Takamiya, S.; Capaldi, R.A. !$#journal Biochemistry (1988) 27:4909-4914 !$#title Tissue-specific differences between heart and liver !1cytochrome c oxidase. !$#cross-references MUID:89000697; PMID:2844245 !$#accession E29968 !'##molecule_type protein !'##residues 1-26 ##label YAN !'##experimental_source liver REFERENCE JT0324 !$#authors Zeviani, M.; Sakoda, S.; Sherbany, A.A.; Nakase, H.; !1Rizzuto, R.; Samitt, C.E.; DiMauro, S.; Schon, E.A. !$#journal Gene (1988) 65:1-11 !$#title Sequence of cDNAs encoding subunit Vb of human and bovine !1cytochrome c oxidase. !$#cross-references MUID:88284368; PMID:2840351 !$#accession JT0325 !'##molecule_type mRNA !'##residues 20-98 ##label ZEV !'##cross-references GB:M19962; NID:g162896; PIDN:AAA30465.1; !1PID:g162897 !'##experimental_source brain REFERENCE A67451 !$#authors Tsukihara, T.; Aoyama, H.; Yamashita, E.; Tomizaki, T.; !1Yamaguchi, H.; Shinzawa-itoh, K.; Nakashima, R.; Yaono, R.; !1Yoshikawa, S. !$#submission submitted to the Brookhaven Protein Data Bank, April 1996 !$#cross-references PDB:1OCC !$#contents annotation; X-ray crystallography, 2.8 angstroms, residues !11-98 REFERENCE A57981 !$#authors Tsukihara, T.; Aoyama, H.; Yamashita, E.; Tomizaki, T.; !1Yamaguchi, H.; Sinzawa-Itoh, K.; Nakashima, R.; Yaono, R.; !1Yoshikawa, S. !$#journal Science (1996) 272:1136-1144 !$#title The whole structure of the 13-subunit oxidized cytochrome c !1oxidase at 2.8 angstroms. !$#cross-references MUID:96216288; PMID:8638158 !$#contents annotation; X-ray crystallography, 2.8 angstroms GENETICS !$#gene COX Vb COMPLEX part of a 13 chain complex spanning the inner mitochondrial !1membrane and consisting of one each of chains I (see !1PIR:ODBO1), II (see PIR:OBBO2), III (see PIR:OTBO3), IV (see !1PIR:OLBO4), Va (see PIR:CABO), Vb, VIa (see PIR:OGBO6), VIb !1(see PIR:OGBO7), VIc (see PIR:OGBO6C), VIIa (see !1PIR:OSBO7A), VIIb (see PIR:OSBO7B), VIIc (see PIR:OSBO8A), !1VIII (see PIR:OSBO8); the complex may form dimers within the !1mitochondrial inner-membrane FUNCTION !$#description the cytochrome-c oxidase complex catalyzes the oxidation of !1four molecules of reduced cytochrome c in the intracristal !1(or intermembrane) space using one oxygen molecule and four !1protons from the mitochondrial matrix producing two !1molecules of water and lowering the concentration of protons !1in the mitochondrial matrix !$#pathway oxidative phosphorylation; respiratory chain !$#note the role of chain Vb is not clear CLASSIFICATION #superfamily mammalian cytochrome-c oxidase chain Vb KEYWORDS electron transfer; membrane-associated complex; !1metalloprotein; mitochondrial inner membrane; mitochondrion; !1oxidative phosphorylation; oxidoreductase; respiratory !1chain; zinc FEATURE !$1-98 #product cytochrome-c oxidase chain Vb #status !8experimental #label MAT\ !$1-98 #domain mitochondrial matrix #status experimental !8#label MM1\ !$60,62,82,85 #binding_site zinc (Cys) #status experimental SUMMARY #length 98 #molecular-weight 10670 #checksum 2005 SEQUENCE /// ENTRY OLBY4 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain IV precursor - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein G1362; protein YGL187c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1991 #sequence_revision 26-May-1995 #text_change 21-Jul-2000 ACCESSIONS A22786; A05016; S61130; S64204 REFERENCE A22786 !$#authors Maarse, A.C.; Van Loon, A.P.G.M.; Riezman, H.; Gregor, I.; !1Schatz, G.; Grivell, L.A. !$#journal EMBO J. (1984) 3:2831-2837 !$#title Subunit IV of yeast cytochrome c oxidase: cloning and !1nucleotide sequencing of the gene and partial amino acid !1sequencing of the mature protein. !$#cross-references MUID:85126878; PMID:6098449 !$#accession A22786 !'##molecule_type DNA !'##residues 1-155 ##label MAA !'##cross-references EMBL:X01418; NID:g3581; PIDN:CAA25665.1; PID:g3582 !'##note most of the sequence confirmed by amino acid sequencing REFERENCE A05016 !$#authors Power, S.D.; Lochrie, M.A.; Poyton, R.O. !$#journal J. Biol. Chem. (1984) 259:6575-6578 !$#title The nuclear-coded subunits of yeast cytochrome c oxidase. !1III. Identification of homologous subunits in yeast, bovine !1heart, and Neurospora crassa cytochrome c oxidases. !$#cross-references MUID:84212484; PMID:6327686 !$#accession A05016 !'##molecule_type protein !'##residues 'E',27-72,'C',74-79 ##label POW REFERENCE S61128 !$#authors Bertani, I.; Coglievina, M.; Zaccaria, P.; Klima, R.; !1Bruschi, C.V. !$#submission submitted to the EMBL Data Library, September 1995 !$#description The sequence analysis of a 7.9 kb DNA fragment from the left !1arm of S.cerevisiae chromosome VII reveals five ORF's !1including part of the CDC55, the entire COX4 and RPS26, and !1two putative new genes. !$#accession S61130 !'##molecule_type DNA !'##residues 1-155 ##label BER !'##cross-references EMBL:X91489; NID:g1143557; PIDN:CAA62787.1; !1PID:g1143560 REFERENCE S64183 !$#authors Bruschi, C.V.; Coglievina, M.; Bertani, I.; Klima, R.; !1Zaccaria, P.; Delneri, D. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64204 !'##molecule_type DNA !'##residues 1-155 ##label BRU !'##cross-references EMBL:Z72709; NID:g1322804; PIDN:CAA96899.1; !1PID:g1322805; GSPDB:GN00007; MIPS:YGL187c !'##experimental_source strain S288C GENETICS !$#gene SGD:COX4; MIPS:YGL187c !'##cross-references SGD:S0003155; MIPS:YGL187c !$#map_position 7L CLASSIFICATION #superfamily mammalian cytochrome-c oxidase chain Vb KEYWORDS membrane-associated complex; mitochondrial inner membrane; !1mitochondrion; oxidative phosphorylation; oxidoreductase; !1respiratory chain FEATURE !$1-25 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$25-155 #product cytochrome-c oxidase chain IV #status !8experimental #label MAT SUMMARY #length 155 #molecular-weight 17142 #checksum 9611 SEQUENCE /// ENTRY OGHU6L #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain VIa, hepatic - human ORGANISM #formal_name Homo sapiens #common_name man DATE 01-Dec-1989 #sequence_revision 07-Jun-1996 #text_change 16-Jun-2000 ACCESSIONS S05304; T09475 REFERENCE S05304 !$#authors Fabrizi, G.M.; Rizzuto, R.; Nakase, H.; Mita, S.; Kadenbach, !1B.; Schon, E.A. !$#journal Nucleic Acids Res. (1989) 17:6409 !$#title Sequence of a cDNA specifying subunit VIa of human !1cytochrome c oxidase. !$#cross-references MUID:89366687; PMID:2549515 !$#accession S05304 !'##molecule_type mRNA !'##residues 1-86 ##label FAB !'##cross-references EMBL:X15341; NID:g1197215; PIDN:CAA33392.1; !1PID:g30153 !'##note the authors translated the codon AAT for residue 33 as Asp and !1TTC for residue 71 as Leu REFERENCE Z16683 !$#authors Murphy, L. !$#submission submitted to the EMBL Data Library, January 1998 !$#accession T09475 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 'MAVVGVSSVSRLLGRSRPQLGRP',1-86 ##label MUR !'##cross-references EMBL:AL021546 !'##note the gene is misidentified as COX6A2 COMMENT This form is found in adult liver and brain, as a minor form !1in fetal cardiac and skeletal muscle, and in small amounts !1in adult cardiac muscle. GENETICS !$#gene GDB:COX6A1; COX6A !'##cross-references GDB:118774 !$#map_position 22pter-22qter !$#introns 12/1; 59/3 COMPLEX part of a 13 chain complex spanning the inner mitochondrial !1membrane and consisting of one each of chains I (see !1PIR:ODHU1), II (see PIR:OBHU2), III (see PIR:OTHU3), IV (see !1PIR:OLHU4), Va (see PIR:OTHU5A), Vb (see PIR:OTHU5B), VIa !1(see also PIR:OGHU6A), VIb (see PIR:OGHU6B), VIc (see !1PIR:OGHU6C), VIIa (see PIR:OSHU7A), VIIb (see PIR:OSHU7B), !1VIIc (see PIR:OSHU7C), VIII (see PIR:OSHU8); the complex may !1form dimers within the mitochondrial inner-membrane FUNCTION !$#description the cytochrome-c oxidase complex catalyzes the oxidation of !1four molecules of reduced cytochrome c in the intracristal !1(or intermembrane) space using one oxygen molecule and four !1protons from the mitochondrial matrix producing two !1molecules of water and lowering the concentration of protons !1in the mitochondrial matrix !$#pathway oxidative phosphorylation; respiratory chain !$#note the role of chain VIa is not clear CLASSIFICATION #superfamily mammalian cytochrome-c oxidase chain VIa KEYWORDS electron transfer; membrane-associated complex; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$2-86 #product cytochrome-c oxidase chain VIa, hepatic !8#status predicted #label MAT\ !$12-36 #domain transmembrane helix #status predicted #label !8TR01 SUMMARY #length 86 #molecular-weight 9750 #checksum 9264 SEQUENCE /// ENTRY S18314 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain VIa, hepatic [similarity] - bovine ALTERNATE_NAMES cytochrome-c oxidase chain SSG; cytochrome-c oxidase chain VIa, hepatic ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS S18314; B29968; S13001 REFERENCE S18314 !$#authors Ewart, G.D.; Zhang, Y.Z.; Capaldi, R.A. !$#journal FEBS Lett. (1991) 292:79-84 !$#title Switching of bovine cytochrome c oxidase subunit VIa !1isoforms in skeletal muscle during development. !$#cross-references MUID:92070527; PMID:1720401 !$#accession S18314 !'##molecule_type mRNA !'##residues 1-85 ##label EWA !'##cross-references EMBL:M38520; NID:g162816; PIDN:AAA30437.1; !1PID:g162817 !'##experimental_source liver REFERENCE A90531 !$#authors Yanamura, W.; Zhang, Y.Z.; Takamiya, S.; Capaldi, R.A. !$#journal Biochemistry (1988) 27:4909-4914 !$#title Tissue-specific differences between heart and liver !1cytochrome c oxidase. !$#cross-references MUID:89000697; PMID:2844245 !$#accession B29968 !'##molecule_type protein !'##residues 1-18,'Y',20-27,'L',29,'T',31-32 ##label YAN !'##experimental_source liver REFERENCE S13001 !$#authors Anthony, G.; Stroh, A.; Lottspeich, F.; Kadenbach, B. !$#journal FEBS Lett. (1990) 277:97-100 !$#title Different isozymes of cytochrome c oxidase are expressed in !1bovine smooth muscle and skeletal or heart muscle. !$#cross-references MUID:91099535; PMID:2176624 !$#accession S13001 !'##molecule_type protein !'##residues 1-6 ##label ANT !'##experimental_source smooth muscle COMMENT This is the only form found in adult liver and brain; it is !1also found as a minor form in fetal heart and skeletal !1muscle and in small amounts in adult heart. CLASSIFICATION #superfamily mammalian cytochrome-c oxidase chain VIa KEYWORDS liver; membrane-associated complex; mitochondrial inner !1membrane; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain SUMMARY #length 85 #molecular-weight 9507 #checksum 7296 SEQUENCE /// ENTRY S01156 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain VIa, hepatic [similarity] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS S01156; S65380 REFERENCE S01156 !$#authors Schlerf, A.; Droste, M.; Winter, M.; Kadenbach, B. !$#journal EMBO J. (1988) 7:2387-2391 !$#title Characterization of two different genes (cDNA) for !1cytochrome c oxidase subunit VIa from heart and liver of the !1rat. !$#cross-references MUID:89052650; PMID:2461293 !$#accession S01156 !'##molecule_type mRNA !'##residues 1-85 ##label SCH !'##cross-references EMBL:X12553; NID:g55986; PIDN:CAA31067.1; !1PID:g818021 !'##experimental_source tissue liver REFERENCE S65372 !$#authors Schaegger, H.; Noack, H.; Halangk, W.; Brandt, U.; von !1Jagow, G. !$#journal Eur. J. Biochem. (1995) 230:235-241 !$#title Cytochrome-c oxidase in developing rat heart. Enzymic !1properties and amino-terminal sequences suggest identity of !1the fetal heart and the adult liver isoform. !$#cross-references MUID:95324529; PMID:7601105 !$#accession S65380 !'##molecule_type protein !'##residues 1-23 ##label SCW COMMENT This is the only form found in adult liver and brain; it is !1also found as a minor form in fetal heart and skeletal !1muscle and in small amounts in adult heart. CLASSIFICATION #superfamily mammalian cytochrome-c oxidase chain VIa KEYWORDS liver; membrane-associated complex; mitochondrial inner !1membrane; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain SUMMARY #length 85 #molecular-weight 9666 #checksum 7777 SEQUENCE /// ENTRY OGHU6A #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain VIa precursor, cardiac - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1993 #sequence_revision 07-Jun-1996 #text_change 16-Jul-1999 ACCESSIONS JC1304 REFERENCE JC1304 !$#authors Fabrizi, G.M.; Sadlock, J.; Hirano, M.; Mita, S.; Koga, Y.; !1Rizzuto, R.; Zeviani, M.; Schon, E.A. !$#journal Gene (1992) 119:307-312 !$#title Differential expression of genes specifying two isoforms of !1subunit VIa of human cytochrome c oxidase. !$#cross-references MUID:93013003; PMID:1327966 !$#accession JC1304 !'##molecule_type mRNA !'##residues 1-97 ##label FAB !'##cross-references GB:M83308 !'##note the authors translated the codon ACC for residue 9 as Ser COMMENT This form is expressed in fetal and adult cardiac and !1skeletal muscle. GENETICS !$#gene GDB:COX6A2 !'##cross-references GDB:136189 !$#map_position 22pter-22qter COMPLEX part of a 13 chain complex spanning the inner mitochondrial !1membrane and consisting of one each of chains I (see !1PIR:ODHU1), II (see PIR:OBHU2), III (see PIR:OTHU3), IV (see !1PIR:OLHU4), Va (see PIR:OTHU5A), Vb (see PIR:OTHU5B), VIa !1(see also PIR:OGHU6L), VIb (see PIR:OGHU6B), VIc (see !1PIR:OGHU6C), VIIa (see PIR:OSHU7A), VIIb (see PIR:OSHU7B), !1VIIc (see PIR:OSHU7C), VIII (see PIR:OSHU8); the complex may !1form dimers within the mitochondrial inner-membrane FUNCTION !$#description the cytochrome-c oxidase complex catalyzes the oxidation of !1four molecules of reduced cytochrome c in the intracristal !1(or intermembrane) space using one oxygen molecule and four !1protons from the mitochondrial matrix producing two !1molecules of water and lowering the concentration of protons !1in the mitochondrial matrix !$#pathway oxidative phosphorylation; respiratory chain !$#note the role of chain VIa is not clear CLASSIFICATION #superfamily mammalian cytochrome-c oxidase chain VIa KEYWORDS cardiac muscle; electron transfer; heart; !1membrane-associated complex; mitochondrial inner membrane; !1mitochondrion; oxidative phosphorylation; oxidoreductase; !1respiratory chain; transmembrane protein FEATURE !$1-12 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$13-97 #product cytochrome-c oxidase chain VIa, cardiac !8#status predicted #label MAT\ !$25-49 #domain transmembrane helix #status predicted #label !8TR01 SUMMARY #length 97 #molecular-weight 10815 #checksum 694 SEQUENCE /// ENTRY OGBO6 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain VIa precursor, cardiac [validated] - bovine ALTERNATE_NAMES cytochrome-c oxidase chain VIb ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 10-Dec-1993 #sequence_revision 07-Jun-1996 #text_change 15-Sep-2000 ACCESSIONS S35702; S16242; A24659 REFERENCE S35702 !$#authors Smith, E.O.; Lomax, M.I. !$#journal Biochim. Biophys. Acta (1993) 1174:63-71 !$#title Structural organization of the bovine gene for the heart/ !1muscle isoform of cytochrome c oxidase subunit VIa. !$#cross-references MUID:93326637; PMID:7687470 !$#accession S35702 !'##molecule_type DNA !'##residues 1-97 ##label SM2 !'##cross-references GB:S64127; NID:g404386; PIDN:AAB27605.1; !1PID:g404387 REFERENCE S16242 !$#authors Smith, E.O.; BeMent, D.M.; Grossman, L.I.; Lomax, M.I. !$#journal Biochim. Biophys. Acta (1991) 1089:266-268 !$#title The cDNA for the heart/ muscle isoform of bovine cytochrome !1c oxidase subunit VIa encodes a presequence. !$#cross-references MUID:91274363; PMID:1647214 !$#accession S16242 !'##molecule_type mRNA !'##residues 1-97 ##label SMI !'##cross-references EMBL:X56857; NID:g269; PIDN:CAA40183.1; PID:g270 !'##experimental_source heart REFERENCE A24659 !$#authors Meinecke, L.; Buse, G. !$#journal Biol. Chem. Hoppe-Seyler (1985) 366:687-694 !$#title Studies on cytochrome c oxidase. XII. Isolation and primary !1structure of polypeptide VIb from bovine heart. !$#cross-references MUID:86000134; PMID:2994692 !$#accession A24659 !'##molecule_type protein !'##residues 13-96 ##label MEI !'##experimental_source heart REFERENCE A67451 !$#authors Tsukihara, T.; Aoyama, H.; Yamashita, E.; Tomizaki, T.; !1Yamaguchi, H.; Shinzawa-itoh, K.; Nakashima, R.; Yaono, R.; !1Yoshikawa, S. !$#submission submitted to the Brookhaven Protein Data Bank, April 1996 !$#cross-references PDB:1OCC !$#contents annotation; X-ray crystallography, 2.8 angstroms, residues !113-96 REFERENCE A57981 !$#authors Tsukihara, T.; Aoyama, H.; Yamashita, E.; Tomizaki, T.; !1Yamaguchi, H.; Sinzawa-Itoh, K.; Nakashima, R.; Yaono, R.; !1Yoshikawa, S. !$#journal Science (1996) 272:1136-1144 !$#title The whole structure of the 13-subunit oxidized cytochrome c !1oxidase at 2.8 angstroms. !$#cross-references MUID:96216288; PMID:8638158 !$#contents annotation; X-ray crystallography, 2.8 angstroms COMMENT This form is expressed in fetal and adult cardiac and !1skeletal muscle. GENETICS !$#gene COX6A1 !$#introns 25/1; 70/3 COMPLEX part of a 13 chain complex spanning the inner mitochondrial !1membrane and consisting of one each of chains I (see !1PIR:ODBO1), II (see PIR:OBBO2), III (see PIR:OTBO3), IV, Va !1(see PIR:CABO), Vb (see PIR:OGBO6A), VIa, VIb (see !1PIR:OGBO7), VIc (see PIR:OGBO6C), VIIa (see PIR:OSBO7A), !1VIIb (see PIR:OSBO7B), VIIc (see PIR:OSBO8A), VIII (see !1PIR:OSBO8); the complex may form dimers within the !1mitochondrial inner-membrane FUNCTION !$#description the cytochrome-c oxidase complex catalyzes the oxidation of !1four molecules of reduced cytochrome c in the intracristal !1(or intermembrane) space using one oxygen molecule and four !1protons from the mitochondrial matrix producing two !1molecules of water and lowering the concentration of protons !1in the mitochondrial matrix !$#pathway oxidative phosphorylation; respiratory chain !$#note the role of chain VIa is not clear CLASSIFICATION #superfamily mammalian cytochrome-c oxidase chain VIa KEYWORDS cardiac muscle; electron transfer; heart; !1membrane-associated complex; mitochondrial inner membrane; !1mitochondrion; oxidative phosphorylation; oxidoreductase; !1respiratory chain; transmembrane protein FEATURE !$1-12 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$13-96 #product cytochrome-c oxidase chain VIa, cardiac !8#status experimental #label MAT\ !$13-24 #domain mitochondrial matrix #status experimental !8#label MM1\ !$25-49 #domain transmembrane helix #status experimental !8#label TR01\ !$50-96 #domain intracristal #status experimental #label ITC1 SUMMARY #length 97 #molecular-weight 10800 #checksum 9780 SEQUENCE /// ENTRY A48520 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain VIa precursor - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein G1341; protein YGL191w ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A48520; S62054; S64208; S33198 REFERENCE A48520 !$#authors Taanman, J.W.; Capaldi, R.A. !$#journal J. Biol. Chem. (1993) 268:18754-18761 !$#title Subunit VIa of yeast cytochrome c oxidase is not necessary !1for assembly of the enzyme complex but modulates the enzyme !1activity. Isolation and characterization of the !1nuclear-coded gene. !$#cross-references MUID:93366789; PMID:8395517 !$#accession A48520 !'##molecule_type DNA !'##residues 1-129 ##label TAA !'##cross-references EMBL:X72970; NID:g296077; PIDN:CAA51479.1; !1PID:g296078 REFERENCE S62051 !$#authors Coglievina, M.; Delneri, D.; Zaccaria, P.; Klima, R.; !1Bertani, I.; Bruschi, C.V. !$#submission submitted to the EMBL Data Library, September 1995 !$#description A 6.7 Kb fragment from chromosome VII of Saccharomyces !1cerevisiae contains the SPO8, COX13 and CDC55 genes as well !1as a new putative transcriptional regulatory protein. !$#accession S62054 !'##molecule_type DNA !'##residues 1-129 ##label COG !'##cross-references EMBL:X91837; NID:g1177627; PIDN:CAA62953.1; !1PID:g1177637 !'##experimental_source strain FY1679 REFERENCE S64183 !$#authors Bruschi, C.V.; Coglievina, M.; Bertani, I.; Klima, R.; !1Zaccaria, P.; Delneri, D. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64208 !'##molecule_type DNA !'##residues 1-129 ##label BRU !'##cross-references EMBL:Z72713; NID:g1322812; PIDN:CAA96903.1; !1PID:g1322813; GSPDB:GN00007; MIPS:YGL191w !'##experimental_source strain S288C GENETICS !$#gene SGD:COX13; MIPS:YGL191w !'##cross-references SGD:S0003159; MIPS:YGL191w !$#map_position 7L !$#genome nuclear CLASSIFICATION #superfamily mammalian cytochrome-c oxidase chain VIa KEYWORDS membrane-associated complex; mitochondrial inner membrane; !1mitochondrion; oxidative phosphorylation; oxidoreductase; !1respiratory chain FEATURE !$1-9 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$10-129 #product cytochrome-c oxidase chain VIa #status !8predicted #label MAT SUMMARY #length 129 #molecular-weight 15021 #checksum 667 SEQUENCE /// ENTRY OGHU6B #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain VIb - human ORGANISM #formal_name Homo sapiens #common_name man DATE 01-Dec-1989 #sequence_revision 07-Jun-1996 #text_change 11-Jun-1999 ACCESSIONS S03287; JS0677; JQ0765; S16245; S14653; S18747 REFERENCE S03287 !$#authors Taanman, J.W.; Schrage, C.; Ponne, N.; Bolhuis, P.; de !1Vries, H.; Agsteribbe, E. !$#journal Nucleic Acids Res. (1989) 17:1766 !$#title Nucleotide sequence of cDNA encoding subunit VIb of human !1cytochrome c oxidase. !$#cross-references MUID:89160337; PMID:2537962 !$#accession S03287 !'##molecule_type mRNA !'##residues 1-86 ##label TAA !'##cross-references EMBL:X13923; NID:g30294; PIDN:CAA32114.1; !1PID:g30295 REFERENCE JS0677 !$#authors Carrero-Valenzuela, R.D.; Quan, F.; Lightowlers, R.; !1Kennaway, N.G.; Litt, M.; Forte, M. !$#journal Gene (1991) 102:229-236 !$#title Human cytochrome c oxidase subunit VIb: characterization and !1mapping of a multigene family. !$#cross-references MUID:91340157; PMID:1651883 !$#accession JS0677 !'##molecule_type mRNA !'##residues 1-86 ##label CAR !'##cross-references EMBL:X54473; NID:g311347; PIDN:CAA38352.1; !1PID:g30381 REFERENCE JQ0765 !$#authors Taanman, J.W.; Schrage, C.; Ponne, N.J.; Das, A.T.; Bolhuis, !1P.A.; de Vries, H.; Agsteribbe, E. !$#journal Gene (1990) 93:285-291 !$#title Isolation of cDNAs encoding subunit VIb of human cytochrome !1c oxidase and steady-state levels of coxVIb mRNA in !1different tissues. !$#cross-references MUID:91033040; PMID:2172092 !$#accession JQ0765 !'##molecule_type mRNA !'##residues 1-86 ##label TA2 !'##cross-references GB:X13923; NID:g30294; PIDN:CAA32114.1; PID:g30295 !'##experimental_source skeletal muscle REFERENCE S16245 !$#authors Taanman, J.W.; Schrage, C.; Bokma, E.; Reuvekamp, P.; !1Agsteribbe, E.; de Vries, H. !$#journal Biochim. Biophys. Acta (1991) 1089:283-285 !$#title Nucleotide sequence of the last exon of the gene for human !1cytochrome c oxidase subunit VIb and its flanking regions. !$#cross-references MUID:91274368; PMID:1647217 !$#accession S16245 !'##molecule_type DNA !'##residues 70-86 ##label TA3 !'##cross-references EMBL:X58139; NID:g30144; PIDN:CAA41147.1; !1PID:g30145 GENETICS !$#gene GDB:COX6B !'##cross-references GDB:128117; OMIM:124089 !$#map_position 19q13.1-19q13.1 COMPLEX part of a 13 chain complex spanning the inner mitochondrial !1membrane and consisting of one each of chains I (see !1PIR:ODHU1), II (see PIR:OBHU2), III (see PIR:OTHU3), IV (see !1PIR:OLHU4), Va (see PIR:OTHU5A), Vb (see PIR:OTHU5B), VIa !1(see PIR:OGHU6A), VIb, VIc (see PIR:OGHU6C), VIIa (see !1PIR:OSHU7A), VIIb (see PIR:OSHU7B), VIIc (see PIR:OSHU7C), !1VIII (see PIR:OSHU8); the complex may form dimers within the !1mitochondrial inner-membrane FUNCTION !$#description the cytochrome-c oxidase complex catalyzes the oxidation of !1four molecules of reduced cytochrome c in the intracristal !1(or intermembrane) space using one oxygen molecule and four !1protons from the mitochondrial matrix producing two !1molecules of water and lowering the concentration of protons !1in the mitochondrial matrix !$#pathway oxidative phosphorylation; respiratory chain !$#note chain VIb may be responsible for dimeric association of the !1complex within the mitochondrial inner-membrane CLASSIFICATION #superfamily mammalian cytochrome-c oxidase chain VIb KEYWORDS acetylated amino end; electron transfer; membrane-associated !1complex; mitochondrial inner membrane; mitochondrion; !1oxidative phosphorylation; oxidoreductase; respiratory chain FEATURE !$2-86 #product cytochrome-c oxidase chain VIb #status !8predicted #label MAT\ !$2-86 #domain intracristal #status predicted #label ITC1\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status predicted\ !$30-65,40-54 #disulfide_bonds #status predicted SUMMARY #length 86 #molecular-weight 10192 #checksum 9421 SEQUENCE /// ENTRY OGBO7 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain VIb [validated] - bovine ALTERNATE_NAMES cytochrome-c oxidase (EC 1.9.3.1) chain VII; cytochrome-c oxidase chain AED ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 28-Feb-1980 #sequence_revision 05-Apr-1995 #text_change 15-Sep-2000 ACCESSIONS S05432; A91683; A92321; I29968; A00497 REFERENCE S05432 !$#authors Lightowlers, R.N.; Capaldi, R.A. !$#journal Nucleic Acids Res. (1989) 17:5845 !$#title Nucleotide sequence of the cDNA encoding subunit AED (VIB) !1of beef heart cytochrome c oxidase. !$#cross-references MUID:89345180; PMID:2548168 !$#accession S05432 !'##molecule_type mRNA !'##residues 1-86 ##label LIG !'##cross-references EMBL:X15112; NID:g267; PIDN:CAA33211.1; PID:g268 !'##experimental_source heart REFERENCE A91683 !$#authors Steffens, G.C.M.; Steffens, G.J.; Buse, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1979) 360:1641-1650 !$#title Studies on cytochrome c oxidase, VIII[1-7]. !$#cross-references MUID:80070615; PMID:229067 !$#accession A91683 !'##molecule_type protein !'##residues 2-86 ##label STE !'##experimental_source heart REFERENCE A92321 !$#authors Tanaka, M.; Yasunobu, K.T.; Wei, Y.H.; King, T.E. !$#journal J. Biol. Chem. (1981) 256:4832-4837 !$#title The complete amino acid sequence of bovine heart cytochrome !1oxidase subunit VI. !$#cross-references MUID:81191870; PMID:6262305 !$#accession A92321 !'##molecule_type protein !'##residues 2-86 ##label TAN !'##experimental_source heart REFERENCE A90531 !$#authors Yanamura, W.; Zhang, Y.Z.; Takamiya, S.; Capaldi, R.A. !$#journal Biochemistry (1988) 27:4909-4914 !$#title Tissue-specific differences between heart and liver !1cytochrome c oxidase. !$#cross-references MUID:89000697; PMID:2844245 !$#accession I29968 !'##molecule_type protein !'##residues 45-67 ##label YAN !'##experimental_source liver REFERENCE A67451 !$#authors Tsukihara, T.; Aoyama, H.; Yamashita, E.; Tomizaki, T.; !1Yamaguchi, H.; Shinzawa-itoh, K.; Nakashima, R.; Yaono, R.; !1Yoshikawa, S. !$#submission submitted to the Brookhaven Protein Data Bank, April 1996 !$#cross-references PDB:1OCC !$#contents annotation; X-ray crystallography, 2.8 angstroms, residues !112-86 REFERENCE A57981 !$#authors Tsukihara, T.; Aoyama, H.; Yamashita, E.; Tomizaki, T.; !1Yamaguchi, H.; Sinzawa-Itoh, K.; Nakashima, R.; Yaono, R.; !1Yoshikawa, S. !$#journal Science (1996) 272:1136-1144 !$#title The whole structure of the 13-subunit oxidized cytochrome c !1oxidase at 2.8 angstroms. !$#cross-references MUID:96216288; PMID:8638158 !$#contents annotation; X-ray crystallography, 2.8 angstroms GENETICS !$#genome nuclear COMPLEX part of a 13 chain complex spanning the inner mitochondrial !1membrane and consisting of one each of chains I (see !1PIR:ODBO1), II (see PIR:OBBO2), III (see PIR:OTBO3), IV (see !1PIR:OLBO4), Va (see PIR:CABO), Vb (see PIR:OGBO6A), VIa (see !1PIR:OGBO6), VIb, VIc (see PIR:OGBO6C), VIIa (see !1PIR:OSBO7A), VIIb (see PIR:OSBO7B), VIIc (see PIR:OSBO8A), !1VIII (see PIR:OSBO8); the complex may form dimers within the !1mitochondrial inner-membrane FUNCTION !$#description the cytochrome-c oxidase complex catalyzes the oxidation of !1four molecules of reduced cytochrome c in the intracristal !1(or intermembrane) space using one oxygen molecule and four !1protons from the mitochondrial matrix producing two !1molecules of water and lowering the concentration of protons !1in the mitochondrial matrix !$#pathway oxidative phosphorylation; respiratory chain !$#note chain VIb may be responsible for dimeric association of the !1complex within the mitochondrial inner-membrane CLASSIFICATION #superfamily mammalian cytochrome-c oxidase chain VIb KEYWORDS acetylated amino end; electron transfer; membrane-associated !1complex; mitochondrial inner membrane; mitochondrion; !1oxidative phosphorylation; oxidoreductase; respiratory chain FEATURE !$2-86 #product cytochrome-c oxidase chain VIb #status !8predicted #label MAT\ !$2-86 #domain intracristal #status experimental #label !8ITC1\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental\ !$30-65,40-54 #disulfide_bonds #status experimental SUMMARY #length 86 #molecular-weight 10156 #checksum 9677 SEQUENCE /// ENTRY S31256 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain VIb - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein L1913; protein YLR038c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S31256; S64865 REFERENCE S31256 !$#authors LaMarche, A.E.P.; Abate, M.I.; Chan, S.H.P.; Trumpower, B.L. !$#journal J. Biol. Chem. (1992) 267:22473-22480 !$#title Isolation and characterization of COX12, the nuclear gene !1for a previously unrecognized subunit of Saccharomyces !1cerevisiae cytochrome c oxidase. !$#cross-references MUID:93054541; PMID:1331057 !$#accession S31256 !'##molecule_type DNA !'##residues 1-83 ##label LAM !'##cross-references EMBL:M98332; NID:g171266; PIDN:AAA34510.1; !1PID:g171267 REFERENCE S64863 !$#authors Koetter, P.; Rose, M.; Entian, K.D. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64865 !'##molecule_type DNA !'##residues 1-83 ##label KOE !'##cross-references EMBL:Z73210; NID:g1360363; PIDN:CAA97566.1; !1PID:g1360364; GSPDB:GN00012; MIPS:YLR038c !'##experimental_source strain S288C GENETICS !$#gene SGD:COX12; MIPS:YLR038c !'##cross-references SGD:S0004028; MIPS:YLR038c !$#map_position 12R !$#genome nuclear CLASSIFICATION #superfamily mammalian cytochrome-c oxidase chain VIb KEYWORDS membrane-associated complex; mitochondrial inner membrane; !1mitochondrion; oxidative phosphorylation; oxidoreductase; !1respiratory chain SUMMARY #length 83 #molecular-weight 9788 #checksum 2319 SEQUENCE /// ENTRY OGBO6C #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain VIc [validated] - bovine ALTERNATE_NAMES cytochrome-c oxidase chain STA, hepatic ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 15-Sep-2000 ACCESSIONS A00496; F29968 REFERENCE A00496 !$#authors Erdweg, M.; Buse, G. !$#journal Biol. Chem. Hoppe-Seyler (1985) 366:257-263 !$#title Studies on cytochrome c oxidase, XI. The amino-acid sequence !1of bovine heart polypeptide VIc. !$#cross-references MUID:85225955; PMID:2988583 !$#accession A00496 !'##molecule_type protein !'##residues 1-73 ##label ERD !'##experimental_source heart REFERENCE A90531 !$#authors Yanamura, W.; Zhang, Y.Z.; Takamiya, S.; Capaldi, R.A. !$#journal Biochemistry (1988) 27:4909-4914 !$#title Tissue-specific differences between heart and liver !1cytochrome c oxidase. !$#cross-references MUID:89000697; PMID:2844245 !$#accession F29968 !'##molecule_type protein !'##residues 1-20 ##label YAN !'##experimental_source liver REFERENCE A67451 !$#authors Tsukihara, T.; Aoyama, H.; Yamashita, E.; Tomizaki, T.; !1Yamaguchi, H.; Shinzawa-itoh, K.; Nakashima, R.; Yaono, R.; !1Yoshikawa, S. !$#submission submitted to the Brookhaven Protein Data Bank, April 1996 !$#cross-references PDB:1OCC !$#contents annotation; X-ray crystallography, 2.8 angstroms, residues !11-73 REFERENCE A57981 !$#authors Tsukihara, T.; Aoyama, H.; Yamashita, E.; Tomizaki, T.; !1Yamaguchi, H.; Sinzawa-Itoh, K.; Nakashima, R.; Yaono, R.; !1Yoshikawa, S. !$#journal Science (1996) 272:1136-1144 !$#title The whole structure of the 13-subunit oxidized cytochrome c !1oxidase at 2.8 angstroms. !$#cross-references MUID:96216288; PMID:8638158 !$#contents annotation; X-ray crystallography, 2.8 angstroms GENETICS !$#genome nuclear COMPLEX part of a 13 chain complex spanning the inner mitochondrial !1membrane and consisting of one each of chains I (see !1PIR:ODBO1), II (see PIR:OBBO2), III (see PIR:OTBO3), IV (see !1PIR:OLBO4), Va (see PIR:CABO), Vb (see PIR:OGBO6A), VIa (see !1PIR:OGBO6), VIb (see PIR:OGBO7), VIc, VIIa (see PIR:OSBO7A), !1VIIb (see PIR:OSBO7B), VIIc (see PIR:OSBO8A), VIII (see !1PIR:OSBO8); the complex may form dimers within the !1mitochondrial inner-membrane FUNCTION !$#description the cytochrome-c oxidase complex catalyzes the oxidation of !1four molecules of reduced cytochrome c in the intracristal !1(or intermembrane) space using one oxygen molecule and four !1protons from the mitochondrial matrix producing two !1molecules of water and lowering the concentration of protons !1in the mitochondrial matrix !$#pathway oxidative phosphorylation; respiratory chain !$#note the role of chain VIc is not clear CLASSIFICATION #superfamily cytochrome-c oxidase chain VIc KEYWORDS electron transfer; membrane-associated complex; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$1-11 #domain mitochondrial matrix #status experimental !8#label MM1\ !$12-52 #domain transmembrane helix #status experimental !8#label TR01\ !$53-73 #domain intracristal #status experimental #label ITC1 SUMMARY #length 73 #molecular-weight 8479 #checksum 5329 SEQUENCE /// ENTRY S00114 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain VIc [validated] - rat ALTERNATE_NAMES cytochrome a3; cytochrome aa3; cytochrome oxidase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS S00114; S20192; A32741; A29907; I64890; I64889; S65382 REFERENCE S00114 !$#authors Suske, G.; Mengel, T.; Cordingley, M.; Kadenbach, B. !$#journal Eur. J. Biochem. (1987) 168:233-237 !$#title Molecular cloning and further characterization of cDNAs for !1rat nuclear-encoded cytochrome c oxidase subunits VIc and !1VIII. !$#cross-references MUID:88029422; PMID:2822403 !$#accession S00114 !'##molecule_type mRNA !'##residues 1-76 ##label SUS !$#accession S20192 !'##molecule_type DNA !'##residues 1-39 ##label SUS2 !'##cross-references EMBL:M28257; NID:g203740; PIDN:AAA41019.1; !1PID:g203742 REFERENCE A32741 !$#authors Parimoo, S.; Seelan, R.S.; Desai, S.; Buse, G.; Padmanaban, !1G. !$#journal Biochem. Biophys. Res. Commun. (1984) 118:902-909 !$#title Construction of a cDNA clone for a nuclear-coded subunit of !1cytochrome c oxidase from rat liver. !$#cross-references MUID:84153873; PMID:6200111 !$#accession A32741 !'##molecule_type mRNA !'##residues 44-76 ##label PAR !'##cross-references GB:K01565; NID:g203713; PIDN:AAA41013.1; !1PID:g203714 REFERENCE A29907 !$#authors Suske, G.; Enders, C.; Schlerf, A.; Kadenbach, B. !$#journal DNA (1988) 7:163-171 !$#title Organization and nucleotide sequence of two chromosomal !1genes for rat cytochrome c oxidase subunit VIc: a structural !1and a processed gene. !$#cross-references MUID:88224561; PMID:2836143 !$#accession A29907 !'##molecule_type DNA !'##residues 1-76 ##label SUS3 !'##cross-references GB:M20152; GB:M20153; NID:g203708; PIDN:AAA41011.1; !1PID:g203710 !'##experimental_source liver REFERENCE I51956 !$#authors Cao, X.N.; Hengst, L.; Schlerf, A.; Droste, M.; Mengel, T.; !1Kadenbach, B. !$#journal Ann. N. Y. Acad. Sci. (1988) 550:337-347 !$#title Complexity of nucleus-encoded genes of mammalian cytochrome !1c oxidase. !$#cross-references MUID:89226785; PMID:2854406 !$#accession I64890 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-76 ##label RES !'##cross-references GB:M27466; NID:g203518; PIDN:AAA79271.1; !1PID:g203519 !$#accession I64889 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 12-28,'A',30-76 ##label RE2 !'##cross-references GB:M27467; NID:g203514; PIDN:AAA79270.1; !1PID:g203515 REFERENCE S65372 !$#authors Schaegger, H.; Noack, H.; Halangk, W.; Brandt, U.; von !1Jagow, G. !$#journal Eur. J. Biochem. (1995) 230:235-241 !$#title Cytochrome-c oxidase in developing rat heart. Enzymic !1properties and amino-terminal sequences suggest identity of !1the fetal heart and the adult liver isoform. !$#cross-references MUID:95324529; PMID:7601105 !$#accession S65382 !'##molecule_type protein !'##residues 2-11 ##label SCH GENETICS !$#gene COX-VIc !$#introns 39/3 CLASSIFICATION #superfamily cytochrome-c oxidase chain VIc KEYWORDS electron transfer; membrane-associated complex; !1mitochondrion; oxidative phosphorylation; oxidoreductase; !1respiratory chain; transmembrane protein FEATURE !$2-76 #product cytochrome-c oxidase chain VIc #status !8predicted #label MAT\ !$22-38 #domain transmembrane #status predicted #label TMM SUMMARY #length 76 #molecular-weight 8455 #checksum 9643 SEQUENCE /// ENTRY OGHU6C #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain VIc - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1989 #sequence_revision 07-Jun-1996 #text_change 22-May-1998 ACCESSIONS S01960 REFERENCE S01960 !$#authors Otsuka, M.; Mizuno, Y.; Yoshida, M.; Kagawa, Y.; Ohta, S. !$#journal Nucleic Acids Res. (1988) 16:10916 !$#title Nucleotide sequence of cDNA encoding human cytochrome c !1oxidase subunit VIc. !$#cross-references MUID:89083509; PMID:2849755 !$#accession S01960 !'##molecule_type mRNA !'##residues 1-75 ##label OTS !'##cross-references EMBL:X13238 GENETICS !$#gene GDB:COX6C !'##cross-references GDB:118775; OMIM:124090 !$#map_position 19q13.1-19q13.1 COMPLEX part of a 13 chain complex spanning the inner mitochondrial !1membrane and consisting of one each of chains I (see !1PIR:ODHU1), II (see PIR:OBHU2), III (see PIR:OTHU3), IV (see !1PIR:OLHU4), Va (see PIR:OTHU5A), Vb (see PIR:OTHU5B), VIa !1(see PIR:OGHU6A), VIb (see PIR:OGHU6B), VIc, VIIa (see !1PIR:OSHU7A), VIIb (see PIR:OSHU7B), VIIc (see PIR:OSHU7C), !1VIII (see PIR:OSHU8); the complex may form dimers within the !1mitochondrial inner-membrane FUNCTION !$#description the cytochrome-c oxidase complex catalyzes the oxidation of !1four molecules of reduced cytochrome c in the intracristal !1(or intermembrane) space using one oxygen molecule and four !1protons from the mitochondrial matrix producing two !1molecules of water and lowering the concentration of protons !1in the mitochondrial matrix !$#pathway oxidative phosphorylation; respiratory chain !$#note the role of chain VIc is not clear CLASSIFICATION #superfamily cytochrome-c oxidase chain VIc KEYWORDS electron transfer; membrane-associated complex; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$2-75 #product cytochrome-c oxidase chain VIc #status !8predicted #label MAT\ !$14-54 #domain transmembrane helix #status predicted #label !8TR01 SUMMARY #length 75 #molecular-weight 8721 #checksum 9644 SEQUENCE /// ENTRY B29907 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain VIc-1 [similarity] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS B29907 REFERENCE A29907 !$#authors Suske, G.; Enders, C.; Schlerf, A.; Kadenbach, B. !$#journal DNA (1988) 7:163-171 !$#title Organization and nucleotide sequence of two chromosomal !1genes for rat cytochrome c oxidase subunit VIc: a structural !1and a processed gene. !$#cross-references MUID:88224561; PMID:2836143 !$#accession B29907 !'##molecule_type DNA !'##residues 1-76 ##label SUS !'##cross-references GB:M20183; NID:g203711; PIDN:AAA41012.1; !1PID:g203712 CLASSIFICATION #superfamily cytochrome-c oxidase chain VIc KEYWORDS membrane-associated complex; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain SUMMARY #length 76 #molecular-weight 8553 #checksum 7740 SEQUENCE /// ENTRY OGDO6 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain VI - slime mold (Dictyostelium discoideum) ORGANISM #formal_name Dictyostelium discoideum DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 11-Jun-1999 ACCESSIONS S17190; S18849 REFERENCE S17190 !$#authors Rizzuto, R.; Sandona, D.; Capaldi, R.A.; Bisson, R. !$#journal Biochim. Biophys. Acta (1991) 1089:386-388 !$#title Characterization of a cDNA encoding subunit VI of cytochrome !1c oxidase from the slime mold Dictyostelium discoideum. !$#cross-references MUID:91316139; PMID:1650252 !$#accession S17190 !'##molecule_type mRNA !'##residues 1-93 ##label RIZ !'##cross-references EMBL:X55672; NID:g7229; PIDN:CAA39207.1; PID:g7230 !$#accession S18849 !'##molecule_type protein !'##residues 2-18 ##label RIZ1 CLASSIFICATION #superfamily Dictyostelium cytochrome-c oxidase chain VI KEYWORDS mitochondrion; oxidative phosphorylation; oxidoreductase; !1respiratory chain; transmembrane protein FEATURE !$2-93 #product cytochrome-c oxidase chain VI #status !8experimental #label MAT\ !$34-53 #domain transmembrane #status predicted #label TMM SUMMARY #length 93 #molecular-weight 10666 #checksum 9130 SEQUENCE /// ENTRY OSHU7A #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain VIIa precursor, cardiac and skeletal muscle [validated] - human ALTERNATE_NAMES cytochrome-c oxidase chain VIIa-M; cytochrome-c oxidase chain VIIa.1, skeletal muscle; cytochrome-c oxidase chain VIIa.H, cardiac muscle ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1993 #sequence_revision 07-Jun-1996 #text_change 08-Dec-2000 ACCESSIONS JC1303; S09724; S20290 REFERENCE JC1303 !$#authors Arnaudo, E.; Hirano, M.; Seelan, R.S.; Milatovich, A.; !1Hsieh, C.L.; Fabrizi, G.M.; Grossman, L.I.; Franck, U.; !1Schon, E.A. !$#journal Gene (1992) 119:299-305 !$#title Tissue-specific expression and chromosome assignment of !1genes specifying two isoforms of subunit VIIa of human !1cytochrome c oxidase. !$#cross-references MUID:93013002; PMID:1327965 !$#accession JC1303 !'##molecule_type mRNA !'##residues 1-79 ##label ARN !'##cross-references GB:M83186; NID:g181404; PIDN:AAA52166.1; !1PID:g181405 REFERENCE S09724 !$#authors van Beeumen, J.J.; van Kuilenburg, A.B.P.; van Bun, S.; van !1den Bogert, C.; Tager, J.M.; Muijsers, A.O. !$#journal FEBS Lett. (1990) 263:213-216 !$#title Demonstration of two isoforms of subunit VIIa of cytochrome !1c oxidase from human skeletal muscle. Implications for !1mitochondrial myopathies. !$#cross-references MUID:90242975; PMID:2159420 !$#accession S09724 !'##molecule_type protein !'##residues 22-59 ##label VAN REFERENCE S20288 !$#authors van Kuilenburg, A.B.P.; van Beeumen, J.J.; van der Meer, !1N.M.; Muijsers, A.O. !$#journal Eur. J. Biochem. (1992) 203:193-199 !$#title Subunits VIIa,b,c of human cytochrome c oxidase. !1Identification of both 'heart-type' and 'liver-type' !1isoforms of subunit VIIa in human heart. !$#cross-references MUID:92111565; PMID:1309697 !$#accession S20290 !'##molecule_type protein !'##residues 22-51 ##label KUI COMMENT This is the principal form expressed in cardiac and skeletal !1muscle. GENETICS !$#gene GDB:COX7A1; COX7A !'##cross-references GDB:118776; OMIM:123995 !$#map_position 19q13.1-19q13.1 COMPLEX part of a 13 chain complex spanning the inner mitochondrial !1membrane and consisting of one each of chains I (see !1PIR:ODHU1), II (see PIR:OBHU2), III (see PIR:OTHU3), IV (see !1PIR:OLHU4), Va (see PIR:OTHU5A), Vb (see PIR:OTHU5B), VIa !1(see PIR:OGHU6A), VIb (see PIR:OGHU6B), VIc (see !1PIR:OGHU6C), VIIa (see also PIR:OSHU7L), VIIb (see !1PIR:OSHU7B), VIIc (see PIR:OSHU7C), VIII (see PIR:OSHU8); !1the complex may form dimers within the mitochondrial !1inner-membrane FUNCTION !$#description the cytochrome-c oxidase complex catalyzes the oxidation of !1four molecules of reduced cytochrome c in the intracristal !1(or intermembrane) space using one oxygen molecule and four !1protons from the mitochondrial matrix producing two !1molecules of water and lowering the concentration of protons !1in the mitochondrial matrix !$#pathway oxidative phosphorylation; respiratory chain !$#note the role of chain VIIa is not clear CLASSIFICATION #superfamily mammalian cytochrome-c oxidase chain VIIa KEYWORDS cardiac muscle; electron transfer; heart; !1membrane-associated complex; mitochondrial inner membrane; !1mitochondrion; oxidative phosphorylation; oxidoreductase; !1respiratory chain; transmembrane protein FEATURE !$1-21 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$22-79 #product cytochrome-c oxidase chain VIIa #status !8experimental #label MAT\ !$47-78 #domain transmembrane helix #status predicted #label !8TR01 SUMMARY #length 79 #molecular-weight 9117 #checksum 7825 SEQUENCE /// ENTRY OSBO7A #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain VIIa precursor, cardiac [validated] - bovine ALTERNATE_NAMES cytochrome-c oxidase chain VIIa, isoform H; cytochrome-c oxidase chain VIIIc ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Sep-1993 #sequence_revision 07-Jun-1996 #text_change 15-Sep-2000 ACCESSIONS A41852; S18187; A25879; S13002; A41034 REFERENCE A41852 !$#authors Seelan, R.S.; Grossman, L.I. !$#journal Biochemistry (1992) 31:4696-4704 !$#title Structure and organization of the heart isoform gene for !1bovine cytochrome c oxidase subunit VIIa. !$#cross-references MUID:92256407; PMID:1316159 !$#accession A41852 !'##molecule_type DNA !'##residues 1-80 ##label SEE !'##cross-references GB:M83299; NID:g162894; PIDN:AAA30464.1; !1PID:g162895 REFERENCE S18187 !$#authors Seelan, R.S.; Grossman, L.I. !$#journal J. Biol. Chem. (1991) 266:19752-19757 !$#title Cytochrome c oxidase subunit VIIa isoforms. Characterization !1and expression of bovine cDNAs. !$#cross-references MUID:92011781; PMID:1717471 !$#accession S18187 !'##molecule_type mRNA !'##residues 1-80 ##label SE2 !'##cross-references GB:X56739; NID:g271; PIDN:CAA40063.1; PID:g272 REFERENCE A25879 !$#authors Meinecke, L.; Buse, G. !$#journal Biol. Chem. Hoppe-Seyler (1986) 367:67-73 !$#title Studies on cytochrome-c oxidase, XIII. Amino-acid sequence !1of the small membrane polypeptide VIIIc from bovine heart !1respiratory complex IV. !$#cross-references MUID:86159303; PMID:3006725 !$#accession A25879 !'##molecule_type protein !'##residues 22-72,'H',74-75,'KK' ##label MEI !'##experimental_source heart REFERENCE S13001 !$#authors Anthony, G.; Stroh, A.; Lottspeich, F.; Kadenbach, B. !$#journal FEBS Lett. (1990) 277:97-100 !$#title Different isozymes of cytochrome c oxidase are expressed in !1bovine smooth muscle and skeletal or heart muscle. !$#cross-references MUID:91099535; PMID:2176624 !$#accession S13002 !'##molecule_type protein !'##residues 22-27 ##label ANT !'##experimental_source smooth muscle REFERENCE A67451 !$#authors Tsukihara, T.; Aoyama, H.; Yamashita, E.; Tomizaki, T.; !1Yamaguchi, H.; Shinzawa-itoh, K.; Nakashima, R.; Yaono, R.; !1Yoshikawa, S. !$#submission submitted to the Brookhaven Protein Data Bank, April 1996 !$#cross-references PDB:1OCC !$#contents annotation; X-ray crystallography, 2.8 angstroms, residues !122-77 REFERENCE A57981 !$#authors Tsukihara, T.; Aoyama, H.; Yamashita, E.; Tomizaki, T.; !1Yamaguchi, H.; Sinzawa-Itoh, K.; Nakashima, R.; Yaono, R.; !1Yoshikawa, S. !$#journal Science (1996) 272:1136-1144 !$#title The whole structure of the 13-subunit oxidized cytochrome c !1oxidase at 2.8 angstroms. !$#cross-references MUID:96216288; PMID:8638158 !$#contents annotation; X-ray crystallography, 2.8 angstroms GENETICS !$#gene COX7aH !$#introns 5/3; 34/3; 63/1 COMPLEX part of a 13 chain complex spanning the inner mitochondrial !1membrane and consisting of one each of chains I (see !1PIR:ODBO1), II (see PIR:OBBO2), III (see PIR:OTBO3), IV (see !1PIR:OLBO4), Va (see PIR:CABO), Vb (see PIR:OGBO6A), VIa (see !1PIR:OGBO6), VIb (see PIR:OGBO7), VIc (see PIR:OGBO6C), VIIa, !1VIIb (see PIR:OSBO7B), VIIc (see PIR:OSBO8A), VIII (see !1PIR:OSBO8); the complex may form dimers within the !1mitochondrial inner-membrane FUNCTION !$#description the cytochrome-c oxidase complex catalyzes the oxidation of !1four molecules of reduced cytochrome c in the intracristal !1(or intermembrane) space using one oxygen molecule and four !1protons from the mitochondrial matrix producing two !1molecules of water and lowering the concentration of protons !1in the mitochondrial matrix !$#pathway oxidative phosphorylation; respiratory chain !$#note the role of chain VIIa is not clear CLASSIFICATION #superfamily mammalian cytochrome-c oxidase chain VIIa KEYWORDS cardiac muscle; electron transfer; heart; !1membrane-associated complex; mitochondrial inner membrane; !1mitochondrion; oxidative phosphorylation; oxidoreductase; !1respiratory chain; transmembrane protein FEATURE !$1-21 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$22-80 #product cytochrome-c oxidase chain VIIa #status !8experimental #label MAT\ !$22-46 #domain mitochondrial matrix #status experimental !8#label MM1\ !$47-78 #domain transmembrane helix #status experimental !8#label TR01\ !$79-80 #domain intracristal #status experimental #label ITC1 SUMMARY #length 80 #molecular-weight 9062 #checksum 7851 SEQUENCE /// ENTRY OSHU7L #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain VIIa precursor, hepatic [validated] - human ALTERNATE_NAMES cytochrome-c oxidase chain VIIa.2, skeletal muscle; cytochrome-c oxidase chain VIIa.L, cardiac muscle ORGANISM #formal_name Homo sapiens #common_name man DATE 28-Feb-1990 #sequence_revision 07-Jun-1996 #text_change 08-Dec-2000 ACCESSIONS S06897; S09725; S20374 REFERENCE S06897 !$#authors Fabrizi, G.M.; Rizzuto, R.; Nakase, H.; Mita, S.; Lomax, !1M.I.; Grossman, L.I.; Schon, E.A. !$#journal Nucleic Acids Res. (1989) 17:7107 !$#title Sequence of a cDNA specifying subunit VIIa of human !1cytochrome c oxidase. !$#cross-references MUID:89386065; PMID:2550906 !$#accession S06897 !'##molecule_type mRNA !'##residues 1-83 ##label FAB !'##cross-references EMBL:X15822; NID:g30146; PIDN:CAA33820.1; !1PID:g30147 REFERENCE S09724 !$#authors van Beeumen, J.J.; van Kuilenburg, A.B.P.; van Bun, S.; van !1den Bogert, C.; Tager, J.M.; Muijsers, A.O. !$#journal FEBS Lett. (1990) 263:213-216 !$#title Demonstration of two isoforms of subunit VIIa of cytochrome !1c oxidase from human skeletal muscle. Implications for !1mitochondrial myopathies. !$#cross-references MUID:90242975; PMID:2159420 !$#accession S09725 !'##molecule_type protein !'##residues 24-45 ##label VAN REFERENCE S20288 !$#authors van Kuilenburg, A.B.P.; van Beeumen, J.J.; van der Meer, !1N.M.; Muijsers, A.O. !$#journal Eur. J. Biochem. (1992) 203:193-199 !$#title Subunits VIIa,b,c of human cytochrome c oxidase. !1Identification of both 'heart-type' and 'liver-type' !1isoforms of subunit VIIa in human heart. !$#cross-references MUID:92111565; PMID:1309697 !$#accession S20374 !'##molecule_type protein !'##residues 24-53 ##label KUI COMMENT This form may be expressed in all tissue types; it is the !1principal form in liver and other tissues, a minor form in !1skeletal muscle, and equally expressed with the muscle form !1in cardiac muscle. GENETICS !$#gene GDB:COX7A2 !'##cross-references GDB:135979; OMIM:123996 !$#map_position 4q31-4q35 COMPLEX part of a 13 chain complex spanning the inner mitochondrial !1membrane and consisting of one each of chains I (see !1PIR:ODHU1), II (see PIR:OBHU2), III (see PIR:OTHU3), IV (see !1PIR:OLHU4), Va (see PIR:OTHU5A), Vb (see PIR:OTHU5B), VIa !1(see PIR:OGHU6A), VIb (see PIR:OGHU6B), VIc (see !1PIR:OGHU6C), VIIa (see PIR:OSHU7A), VIIb (see PIR:OSHU7B), !1VIIc (see PIR:OSHU7C), VIII (see PIR:OSHU8); the complex may !1form dimers within the mitochondrial inner-membrane FUNCTION !$#description the cytochrome-c oxidase complex catalyzes the oxidation of !1four molecules of reduced cytochrome c in the intracristal !1(or intermembrane) space using one oxygen molecule and four !1protons from the mitochondrial matrix producing two !1molecules of water and lowering the concentration of protons !1in the mitochondrial matrix !$#pathway oxidative phosphorylation; respiratory chain !$#note the role of chain VIIa is not clear CLASSIFICATION #superfamily mammalian cytochrome-c oxidase chain VIIa KEYWORDS cardiac muscle; electron transfer; heart; !1membrane-associated complex; mitochondrial inner membrane; !1mitochondrion; oxidative phosphorylation; oxidoreductase; !1respiratory chain; transmembrane protein FEATURE !$1-23 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$24-83 #product cytochrome-c oxidase chain VIIa #status !8experimental #label MAT\ !$49-80 #domain transmembrane helix #status predicted #label !8TR01 SUMMARY #length 83 #molecular-weight 9396 #checksum 1098 SEQUENCE /// ENTRY OBBY7 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain VII - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YM9920.10c; protein YMR256c ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Dec-1989 #sequence_revision 31-Dec-1992 #text_change 12-Nov-1999 ACCESSIONS S22248; S11181; A24809; S53078 REFERENCE S22248 !$#authors Calder, K.M.; McEwen, J.E. !$#journal Nucleic Acids Res. (1990) 18:1632 !$#title Nucleotide sequence of the gene encoding cytochrome c !1oxidase subunit VII from Saccharomyces cerevisiae. !$#cross-references MUID:90221896; PMID:2158084 !$#accession S22248 !'##molecule_type DNA !'##residues 1-60 ##label CAL !'##cross-references EMBL:X51506; NID:g3584; PIDN:CAA35871.1; PID:g3585 REFERENCE S11181 !$#authors Aggeler, R.; Capaldi, R.A. !$#journal J. Biol. Chem. (1990) 265:16389-16393 !$#title Yeast cytochrome c oxidase subunit VII is essential for !1assembly of an active enzyme. Cloning, sequencing, and !1characterization of the nuclear-encoded gene. !$#cross-references MUID:90375505; PMID:2168889 !$#accession S11181 !'##molecule_type DNA !'##residues 1-60 ##label AGG !'##cross-references GB:M31620; NID:g171363; PIDN:AAA34550.1; !1PID:g171364 REFERENCE A92593 !$#authors Power, S.D.; Lochrie, M.A.; Poyton, R.O. !$#journal J. Biol. Chem. (1986) 261:9206-9209 !$#title The nuclear-coded subunits of yeast cytochrome c oxidase. !1The amino acid sequences of subunits VII and VIIa, !1structural similarities between the three smallest !1polypeptides of the holoenzyme, and implications for !1biogenesis. !$#cross-references MUID:86250863; PMID:3013877 !$#accession A24809 !'##molecule_type protein !'##residues 2-58 ##label POW REFERENCE S53069 !$#authors Hunt, S.; Bowman, S. !$#submission submitted to the EMBL Data Library, March 1995 !$#accession S53078 !'##molecule_type DNA !'##residues 1-60 ##label HUN !'##cross-references EMBL:Z48639; NID:g732924; PIDN:CAA88583.1; !1PID:g732934; GSPDB:GN00013; MIPS:YMR256c GENETICS !$#gene SGD:COX7; MIPS:YMR256c !'##cross-references SGD:S0004869; MIPS:YMR256c !$#map_position 13R !$#genome nuclear CLASSIFICATION #superfamily yeast cytochrome-c oxidase chain VII KEYWORDS membrane-associated complex; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$2-58 #product cytochrome-c oxidase chain VII #status !8experimental #label MAT\ !$31-51 #domain transmembrane #status predicted #label TMM SUMMARY #length 60 #molecular-weight 6932 #checksum 7664 SEQUENCE /// ENTRY OBBY7A #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain VIIa - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein D2520; protein YDL067c ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Dec-1989 #sequence_revision 17-Feb-1995 #text_change 21-Jul-2000 ACCESSIONS JQ0325; A25352; B24809; S42147; S67602 REFERENCE JQ0325 !$#authors Forsbach, V.; Pillar, T.; Gottenoef, T.; Roedel, G. !$#journal Mol. Gen. Genet. (1989) 218:57-63 !$#title Chromosomal localization and expression of CBS1, a !1translational activator of cytochrome b in yeast. !$#cross-references MUID:89384437; PMID:2550765 !$#accession JQ0325 !'##molecule_type DNA !'##residues 1-59 ##label FOR !'##cross-references GB:X16120; NID:g3465; PIDN:CAA34250.1; PID:g3466 REFERENCE A25352 !$#authors Wright, R.M.; Dircks, L.K.; Poyton, R.O. !$#journal J. Biol. Chem. (1986) 261:17183-17191 !$#title Characterization of COX9, the nuclear gene encoding the !1yeast mitochondrial protein cytochrome c oxidase subunit !1VIIa. Subunit VIIa lacks a leader peptide and is an !1essential component of the holoenzyme. !$#cross-references MUID:87057443; PMID:3023385 !$#accession A25352 !'##molecule_type DNA !'##residues 1-59 ##label WRI !'##cross-references EMBL:J02633; NID:g1431804; PIDN:AAB03896.1; !1PID:g171299 REFERENCE A92593 !$#authors Power, S.D.; Lochrie, M.A.; Poyton, R.O. !$#journal J. Biol. Chem. (1986) 261:9206-9209 !$#title The nuclear-coded subunits of yeast cytochrome c oxidase. !1The amino acid sequences of subunits VII and VIIa, !1structural similarities between the three smallest !1polypeptides of the holoenzyme, and implications for !1biogenesis. !$#cross-references MUID:86250863; PMID:3013877 !$#contents Sequence !$#accession B24809 !'##molecule_type protein !'##residues 'A',3-55 ##label POW REFERENCE A35189 !$#authors Duhl, D.M.; Powell, T.; Poyton, R.O. !$#journal J. Biol. Chem. (1990) 265:7273-7277 !$#title Mitochondrial import of cytochrome c oxidase subunit VIIa in !1Saccharomyces cerevisiae. Identification of sequences !1required for mitochondrial localization in vivo. !$#cross-references MUID:90237020; PMID:2158998 !$#accession S42147 !'##molecule_type DNA !'##residues 1-59 ##label DUH !'##cross-references EMBL:M35260; NID:g171300; PIDN:AAA34523.1; !1PID:g171301 REFERENCE S67587 !$#authors Bloecker, H.; Brandt, P. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67602 !'##molecule_type DNA !'##residues 1-59 ##label BLO !'##cross-references EMBL:Z74115; NID:g1431075; PIDN:CAA98632.1; !1PID:g1431076; GSPDB:GN00004; MIPS:YDL067c !'##experimental_source strain S288C COMMENT This protein, along with polypeptides VII and VIII, belong !1to the group of nuclear-coded short polypeptide chains of !1cytochrome-c oxidase. They have a higher content of !1hydrophobic amino acids than the nuclear-coded long chains !1and are insoluble in aqueous buffers. GENETICS !$#gene SGD:COX9; MIPS:YDL067c !'##cross-references SGD:S0002225; MIPS:YDL067c !$#map_position 4L CLASSIFICATION #superfamily yeast cytochrome-c oxidase chain VIIa KEYWORDS membrane-associated complex; mitochondrial inner membrane; !1mitochondrion; oxidative phosphorylation; oxidoreductase; !1respiratory chain; transmembrane protein FEATURE !$14-36 #domain transmembrane #status predicted #label TMM SUMMARY #length 59 #molecular-weight 6963 #checksum 5453 SEQUENCE /// ENTRY OSHU7B #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain VIIb precursor - human ORGANISM #formal_name Homo sapiens #common_name man DATE 08-Dec-1993 #sequence_revision 07-Jun-1996 #text_change 16-Jul-1999 ACCESSIONS S29856 REFERENCE S29856 !$#authors Sadlock, J.E.; Lightowlers, R.N.; Capaldi, R.A.; Schon, E.A. !$#journal Biochim. Biophys. Acta (1993) 1172:223-225 !$#title Isolation of a cDNA specifying subunit VIIb of human !1cytochrome c oxidase. !$#cross-references MUID:93176819; PMID:8382530 !$#accession S29856 !'##molecule_type mRNA !'##residues 1-80 ##label SAD !'##cross-references EMBL:Z14244; NID:g30150; PIDN:CAA78613.1; !1PID:g30151 GENETICS !$#gene GDB:COX7B !'##cross-references GDB:138315 !$#map_position 14pter-14qter COMPLEX part of a 13 chain complex spanning the inner mitochondrial !1membrane and consisting of one each of chains I (see !1PIR:ODHU1), II (see PIR:OBHU2), III (see PIR:OTHU3), IV (see !1PIR:OLHU4), Va (see PIR:OTHU5A), Vb (see PIR:OTHU5B), VIa !1(see PIR:OGHU6A), VIb (see PIR:OGHU6B), VIc (see !1PIR:OGHU6C), VIIa (see PIR:OSHU7A), VIIb, VIIc (see !1PIR:OSHU7C), VIII (see PIR:OSHU8); the complex may form !1dimers within the mitochondrial inner-membrane FUNCTION !$#description the cytochrome-c oxidase complex catalyzes the oxidation of !1four molecules of reduced cytochrome c in the intracristal !1(or intermembrane) space using one oxygen molecule and four !1protons from the mitochondrial matrix producing two !1molecules of water and lowering the concentration of protons !1in the mitochondrial matrix !$#pathway oxidative phosphorylation; respiratory chain !$#note the role of chain VIIb is not clear CLASSIFICATION #superfamily cytochrome-c oxidase chain VIIb KEYWORDS electron transfer; membrane-associated complex; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$1-23 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$24-80 #product cytochrome-c oxidase chain VIIb #status !8predicted #label MAT\ !$33-59 #domain transmembrane helix #status predicted #label !8TR01 SUMMARY #length 80 #molecular-weight 9160 #checksum 9790 SEQUENCE /// ENTRY OSBO7B #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain VIIb precursor [validated] - bovine ALTERNATE_NAMES cytochrome-c oxidase chain IHQ ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 07-Sep-1990 #sequence_revision 07-Jun-1996 #text_change 15-Sep-2000 ACCESSIONS A34410; G29968 REFERENCE A34410 !$#authors Lightowlers, R.; Takamiya, S.; Wessling, R.; Lindorfer, M.; !1Capaldi, R.A. !$#journal J. Biol. Chem. (1989) 264:16858-16861 !$#title Cloning and sequencing of the cDNA for a 13th different !1subunit (IHQ) of beef heart cytochrome c oxidase. !$#cross-references MUID:89380319; PMID:2550462 !$#accession A34410 !'##molecule_type mRNA !'##residues 1-88 ##label LIG !'##cross-references GB:J05058; NID:g162958; PIDN:AAA30489.1; !1PID:g162959 !'##experimental_source heart !'##note the authors were uncertain whether Met-1 or Met-6 is the !1initiator REFERENCE A90531 !$#authors Yanamura, W.; Zhang, Y.Z.; Takamiya, S.; Capaldi, R.A. !$#journal Biochemistry (1988) 27:4909-4914 !$#title Tissue-specific differences between heart and liver !1cytochrome c oxidase. !$#cross-references MUID:89000697; PMID:2844245 !$#accession G29968 !'##molecule_type protein !'##residues 33-54 ##label YAN !'##experimental_source liver REFERENCE A67451 !$#authors Tsukihara, T.; Aoyama, H.; Yamashita, E.; Tomizaki, T.; !1Yamaguchi, H.; Shinzawa-itoh, K.; Nakashima, R.; Yaono, R.; !1Yoshikawa, S. !$#submission submitted to the Brookhaven Protein Data Bank, April 1996 !$#cross-references PDB:1OCC !$#contents annotation; X-ray crystallography, 2.8 angstroms, residues !138-86 REFERENCE A57981 !$#authors Tsukihara, T.; Aoyama, H.; Yamashita, E.; Tomizaki, T.; !1Yamaguchi, H.; Sinzawa-Itoh, K.; Nakashima, R.; Yaono, R.; !1Yoshikawa, S. !$#journal Science (1996) 272:1136-1144 !$#title The whole structure of the 13-subunit oxidized cytochrome c !1oxidase at 2.8 angstroms. !$#cross-references MUID:96216288; PMID:8638158 !$#contents annotation; X-ray crystallography, 2.8 angstroms GENETICS !$#genome nuclear COMPLEX part of a 13 chain complex spanning the inner mitochondrial !1membrane and consisting of one each of chains I (see !1PIR:ODBO1), II (see PIR:OBBO2), III (see PIR:OTBO3), IV (see !1PIR:OLBO4), Va (see PIR:CABO), Vb (see PIR:OGBO6A), VIa (see !1PIR:OGBO6), VIb (see PIR:OGBO7), VIc (see PIR:OGBO6C), VIIa !1(see PIR:OSBO7A), VIIb, VIIc (see PIR:OSBO8A), VIII (see !1PIR:OSBO8); the complex may form dimers within the !1mitochondrial inner-membrane FUNCTION !$#description the cytochrome-c oxidase complex catalyzes the oxidation of !1four molecules of reduced cytochrome c in the intracristal !1(or intermembrane) space using one oxygen molecule and four !1protons from the mitochondrial matrix producing two !1molecules of water and lowering the concentration of protons !1in the mitochondrial matrix !$#pathway oxidative phosphorylation; respiratory chain !$#note the role of chain VIIb is not clear CLASSIFICATION #superfamily cytochrome-c oxidase chain VIIb KEYWORDS electron transfer; membrane-associated complex; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$1-32 #domain (or 6-32) transit peptide (mitochondrion) !8#status predicted #label TNP\ !$33-88 #product cytochrome-c oxidase chain VIIb #status !8experimental #label MAT\ !$33-40 #domain mitochondrial matrix #status experimental !8#label MM1\ !$41-67 #domain transmembrane helix #status experimental !8#label TR01\ !$68-88 #domain intracristal #status experimental #label ITC1 SUMMARY #length 88 #molecular-weight 10026 #checksum 3255 SEQUENCE /// ENTRY OSHU7C #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain VIIc precursor - human ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 11-Jun-1999 ACCESSIONS S15763; S20288; S08217 REFERENCE S15763 !$#authors Koga, Y.; Fabrizi, G.M.; Mita, S.; Arnaudo, E.; Lomax, M.I.; !1Aqua, M.S.; Grossman, L.I.; Schon, E.A. !$#journal Nucleic Acids Res. (1990) 18:684 !$#title Sequence of a cDNA specifying subunit VIIc of human !1cytochrome c oxidase. !$#cross-references MUID:90175022; PMID:2155413 !$#accession S15763 !'##molecule_type mRNA !'##residues 1-63 ##label KOG !'##cross-references EMBL:X16560; NID:g30154; PIDN:CAA34559.1; !1PID:g30155 REFERENCE S20288 !$#authors van Kuilenburg, A.B.P.; van Beeumen, J.J.; van der Meer, !1N.M.; Muijsers, A.O. !$#journal Eur. J. Biochem. (1992) 203:193-199 !$#title Subunits VIIa,b,c of human cytochrome c oxidase. !1Identification of both 'heart-type' and 'liver-type' !1isoforms of subunit VIIa in human heart. !$#cross-references MUID:92111565; PMID:1309697 !$#accession S20288 !'##molecule_type protein !'##residues 17-40 ##label KUI GENETICS !$#gene GDB:COX7C !'##cross-references GDB:128569 !$#map_position 14pter-14qter COMPLEX part of a 13 chain complex spanning the inner mitochondrial !1membrane and consisting of one each of chains I (see !1PIR:ODHU1), II (see PIR:OBHU2), III (see PIR:OTHU3), IV (see !1PIR:OLHU4), Va (see PIR:OTHU5A), Vb (see PIR:OTHU5B), VIa !1(see PIR:OGHU6A), VIb (see PIR:OGHU6B), VIc (see !1PIR:OGHU6C), VIIa (see PIR:OSHU7A), VIIb (see PIR:OSHU7B), !1VIIc, VIII (see PIR:OSHU8); the complex may form dimers !1within the mitochondrial inner-membrane FUNCTION !$#description the cytochrome-c oxidase complex catalyzes the oxidation of !1four molecules of reduced cytochrome c in the intracristal !1(or intermembrane) space using one oxygen molecule and four !1protons from the mitochondrial matrix producing two !1molecules of water and lowering the concentration of protons !1in the mitochondrial matrix !$#pathway oxidative phosphorylation; respiratory chain !$#note the role of chain VIIc is not clear CLASSIFICATION #superfamily cytochrome-c oxidase chain VIIc KEYWORDS electron transfer; membrane-associated complex; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$1-16 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$17-63 #product cytochrome-c oxidase chain VIIc #status !8predicted #label MAT\ !$34-60 #domain transmembrane helix #status predicted #label !8TR01 SUMMARY #length 63 #molecular-weight 7245 #checksum 8812 SEQUENCE /// ENTRY OSBO8A #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain VIIc precursor [validated] - bovine ALTERNATE_NAMES cytochrome-c oxidase chain VIIIa ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-May-1979 #sequence_revision 31-Dec-1992 #text_change 15-Sep-2000 ACCESSIONS JH0473; S06597; A00498; H29968; S18834 REFERENCE JH0473 !$#authors Aqua, M.S.; Bachman, N.J.; Lomax, M.I.; Grossman, L.I. !$#journal Gene (1991) 104:211-217 !$#title Characterization and expression of a cDNA specifying subunit !1VIIc of bovine cytochrome c oxidase. !$#cross-references MUID:92009215; PMID:1655579 !$#accession JH0473 !'##molecule_type DNA !'##residues 1-63 ##label AQU1 !'##cross-references GB:X58823 REFERENCE S06597 !$#authors Aqua, M.S.; Lomax, M.I.; Schon, E.A.; Grossman, L.I. !$#journal Nucleic Acids Res. (1989) 17:8376 !$#title Nucleotide sequence of a cDNA for bovine cytochrome c !1oxidase subunit VIIc. !$#cross-references MUID:90045968; PMID:2554257 !$#accession S06597 !'##molecule_type mRNA !'##residues 1-63 ##label AQU2 !'##cross-references EMBL:X15725; NID:g277; PIDN:CAB57793.1; !1PID:g6015488 REFERENCE A00498 !$#authors Buse, G.; Steffens, G.J. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1978) 359:1005-1009 !$#title Studies on cytochrome c oxidase, II. The chemical !1constitution of a short polypeptide from the beef heart !1enzyme. !$#cross-references MUID:79046803; PMID:213363 !$#accession A00498 !'##molecule_type protein !'##residues 17-63 ##label BUS !'##experimental_source heart REFERENCE A90531 !$#authors Yanamura, W.; Zhang, Y.Z.; Takamiya, S.; Capaldi, R.A. !$#journal Biochemistry (1988) 27:4909-4914 !$#title Tissue-specific differences between heart and liver !1cytochrome c oxidase. !$#cross-references MUID:89000697; PMID:2844245 !$#accession H29968 !'##molecule_type protein !'##residues 17-42 ##label YAN !'##experimental_source liver REFERENCE A67451 !$#authors Tsukihara, T.; Aoyama, H.; Yamashita, E.; Tomizaki, T.; !1Yamaguchi, H.; Shinzawa-itoh, K.; Nakashima, R.; Yaono, R.; !1Yoshikawa, S. !$#submission submitted to the Brookhaven Protein Data Bank, April 1996 !$#cross-references PDB:1OCC !$#contents annotation; X-ray crystallography, 2.8 angstroms, residues !117-63 REFERENCE A57981 !$#authors Tsukihara, T.; Aoyama, H.; Yamashita, E.; Tomizaki, T.; !1Yamaguchi, H.; Sinzawa-Itoh, K.; Nakashima, R.; Yaono, R.; !1Yoshikawa, S. !$#journal Science (1996) 272:1136-1144 !$#title The whole structure of the 13-subunit oxidized cytochrome c !1oxidase at 2.8 angstroms. !$#cross-references MUID:96216288; PMID:8638158 !$#contents annotation; X-ray crystallography, 2.8 angstroms GENETICS !$#genome nuclear COMPLEX part of a 13 chain complex spanning the inner mitochondrial !1membrane and consisting of one each of chains I (see !1PIR:ODBO1), II (see PIR:OBBO2), III (see PIR:OTBO3), IV (see !1PIR:OLBO4), Va (see PIR:CABO), Vb (see PIR:OGBO6A), VIa (see !1PIR:OGBO6), VIb (see PIR:OGBO7), VIc (see PIR:OGBO6C), VIIa !1(see PIR:OSBO7A), VIIb (see PIR:OSBO7B), VIIc, VIII (see !1PIR:OSBO8); the complex may form dimers within the !1mitochondrial inner-membrane FUNCTION !$#description the cytochrome-c oxidase complex catalyzes the oxidation of !1four molecules of reduced cytochrome c in the intracristal !1(or intermembrane) space using one oxygen molecule and four !1protons from the mitochondrial matrix producing two !1molecules of water and lowering the concentration of protons !1in the mitochondrial matrix !$#pathway oxidative phosphorylation; respiratory chain !$#note the role of chain VIIc is not clear CLASSIFICATION #superfamily cytochrome-c oxidase chain VIIc KEYWORDS electron transfer; membrane-associated complex; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$1-16 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$17-63 #product cytochrome-c oxidase chain VIIc #status !8experimental #label MAT\ !$17-33 #domain mitochondrial matrix #status experimental !8#label MM1\ !$34-60 #domain transmembrane helix #status experimental !8#label TR01\ !$61-63 #domain intracristal #status experimental #label ITC1 SUMMARY #length 63 #molecular-weight 7331 #checksum 6879 SEQUENCE /// ENTRY OSHU8 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain VIII precursor [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Mar-1990 #sequence_revision 07-Jun-1996 #text_change 08-Dec-2000 ACCESSIONS A34103; S01785 REFERENCE A34103 !$#authors Rizzuto, R.; Nakase, H.; Darras, B.; Francke, U.; Fabrizi, !1G.M.; Mengel, T.; Walsh, F.; Kadenbach, B.; DiMauro, S.; !1Schon, E.A. !$#journal J. Biol. Chem. (1989) 264:10595-10600 !$#title A gene specifying subunit VIII of human cytochrome c oxidase !1is localized to chromosome 11 and is expressed in both !1muscle and non-muscle tissues. !$#cross-references MUID:89278125; PMID:2543673 !$#accession A34103 !'##status preliminary !'##molecule_type mRNA !'##residues 1-69 ##label RIZ !'##cross-references GB:J04823; NID:g1311703; PIDN:AAA99313.1; !1PID:g180939 REFERENCE S01785 !$#authors van Kuilenburg, A.B.P.; Muijsers, A.O.; Demol, H.; Dekker, !1H.L.; van Beeumen, J.J. !$#journal FEBS Lett. (1988) 240:127-132 !$#title Human heart cytochrome c oxidase subunit VIII. Purification !1and determination of the complete amino acid sequence. !$#cross-references MUID:89052871; PMID:2847943 !$#accession S01785 !'##molecule_type protein !'##residues 26-69 ##label VAN GENETICS !$#gene GDB:COX8 !'##cross-references GDB:119796; OMIM:123870 !$#map_position 11q12-11q13 COMPLEX part of a 13 chain complex spanning the inner mitochondrial !1membrane and consisting of one each of chains I (see !1PIR:ODHU1), II (see PIR:OBHU2), III (see PIR:OTHU3), IV (see !1PIR:OLHU4), Va (see PIR:OTHU5A), Vb (see PIR:OTHU5B), VIa !1(see PIR:OGHU6A), VIb (see PIR:OGHU6B), VIc (see !1PIR:OGHU6C), VIIa (see PIR:OSHU7A), VIIb (see PIR:OSHU7B), !1VIIc (see PIR:OSHU7C), VIII; the complex may form dimers !1within the mitochondrial inner-membrane FUNCTION !$#description the cytochrome-c oxidase complex catalyzes the oxidation of !1four molecules of reduced cytochrome c in the intracristal !1(or intermembrane) space using one oxygen molecule and four !1protons from the mitochondrial matrix producing two !1molecules of water and lowering the concentration of protons !1in the mitochondrial matrix !$#pathway oxidative phosphorylation; respiratory chain !$#note the role of chain VIII is not clear CLASSIFICATION #superfamily cytochrome-c oxidase chain VIII KEYWORDS electron transfer; membrane-associated complex; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain; !1transmembrane protein FEATURE !$1-25 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$26-69 #product cytochrome-c oxidase chain VIII #status !8experimental #label MAT\ !$37-60 #domain transmembrane helix #status predicted #label !8TR01 SUMMARY #length 69 #molecular-weight 7579 #checksum 1836 SEQUENCE /// ENTRY B35537 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain VIII precursor, isoform L - bovine ALTERNATE_NAMES cytochrome-c oxidase chain IX, hepatic; cytochrome-c oxidase chain VIII.2 ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B35537; A28969; C60181; D60181; S13004 REFERENCE A35537 !$#authors Lightowlers, R.; Ewart, G.; Aggeler, R.; Zhang, Y.Z.; !1Calavetta, L.; Capaldi, R.A. !$#journal J. Biol. Chem. (1990) 265:2677-2681 !$#title Isolation and characterization of the cDNAs encoding two !1isoforms of subunit C-IX of bovine cytochrome c oxidase. !$#cross-references MUID:90153890; PMID:1689292 !$#accession B35537 !'##molecule_type mRNA !'##residues 1-69 ##label LIG !'##cross-references GB:J05201; NID:g162900; PIDN:AAA30467.1; !1PID:g162901 !'##experimental_source liver !'##note the authors suggest that the differences at residue 39 are due !1to polymorphism REFERENCE A90531 !$#authors Yanamura, W.; Zhang, Y.Z.; Takamiya, S.; Capaldi, R.A. !$#journal Biochemistry (1988) 27:4909-4914 !$#title Tissue-specific differences between heart and liver !1cytochrome c oxidase. !$#cross-references MUID:89000697; PMID:2844245 !$#accession A28969 !'##molecule_type protein !'##residues 26-38,'E',40-49,'D',62-69 ##label YAN !'##experimental_source liver REFERENCE A60181 !$#authors Kennaway, N.G.; Carrero-Valenzuela, R.D.; Ewart, G.; Balan, !1V.K.; Lightowlers, R.; Zhang, Y.Z.; Powell, B.R.; Capaldi, !1R.A.; Buist, N.R.M. !$#journal Pediatr. Res. (1990) 28:529-535 !$#title Isoforms of mammalian cytochrome c oxidase: correlation with !1human cytochrome c oxidase deficiency. !$#cross-references MUID:91074608; PMID:2175025 !$#accession C60181 !'##molecule_type protein !'##residues 26-38,'E',40-45 ##label KEN !'##experimental_source liver !$#accession D60181 !'##molecule_type protein !'##residues 26-43 ##label KE2 !'##experimental_source brain REFERENCE S13001 !$#authors Anthony, G.; Stroh, A.; Lottspeich, F.; Kadenbach, B. !$#journal FEBS Lett. (1990) 277:97-100 !$#title Different isozymes of cytochrome c oxidase are expressed in !1bovine smooth muscle and skeletal or heart muscle. !$#cross-references MUID:91099535; PMID:2176624 !$#accession S13004 !'##molecule_type protein !'##residues 26-31 ##label ANT !'##experimental_source smooth muscle CLASSIFICATION #superfamily cytochrome-c oxidase chain VIII KEYWORDS liver; mitochondrion; oxidoreductase; polymorphism FEATURE !$1-25 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$26-69 #product cytochrome-c oxidase chain VIII, isoform L !8#status experimental #label MAT SUMMARY #length 69 #molecular-weight 7743 #checksum 1683 SEQUENCE /// ENTRY OSBO8 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) chain VIII precursor, cardiac [validated] - bovine ALTERNATE_NAMES cytochrome-c oxidase chain IX, cardiac; cytochrome-c oxidase chain VIII.1; cytochrome-c oxidase chain VIIIb ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 07-Sep-1990 #sequence_revision 07-Jun-1996 #text_change 15-Sep-2000 ACCESSIONS A35537; A29180; B60181; S13003 REFERENCE A35537 !$#authors Lightowlers, R.; Ewart, G.; Aggeler, R.; Zhang, Y.Z.; !1Calavetta, L.; Capaldi, R.A. !$#journal J. Biol. Chem. (1990) 265:2677-2681 !$#title Isolation and characterization of the cDNAs encoding two !1isoforms of subunit C-IX of bovine cytochrome c oxidase. !$#cross-references MUID:90153890; PMID:1689292 !$#accession A35537 !'##molecule_type mRNA !'##residues 1-70 ##label LIG !'##cross-references GB:J05202; NID:g162898; PIDN:AAA30466.1; !1PID:g162899 !'##experimental_source heart !'##note the authors suggest that the differences at residue 31 are due !1to polymorphism REFERENCE A29180 !$#authors Meinecke, L.; Steffens, G.J.; Buse, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1984) 365:313-320 !$#title Studies on cytochrome c oxidase, X. Isolation and amino-acid !1sequence of polypeptide VIIIb. !$#cross-references MUID:84210427; PMID:6327490 !$#accession A29180 !'##molecule_type protein !'##residues 25-30,'K',32-70 ##label MEI !'##experimental_source heart REFERENCE A60181 !$#authors Kennaway, N.G.; Carrero-Valenzuela, R.D.; Ewart, G.; Balan, !1V.K.; Lightowlers, R.; Zhang, Y.Z.; Powell, B.R.; Capaldi, !1R.A.; Buist, N.R.M. !$#journal Pediatr. Res. (1990) 28:529-535 !$#title Isoforms of mammalian cytochrome c oxidase: correlation with !1human cytochrome c oxidase deficiency. !$#cross-references MUID:91074608; PMID:2175025 !$#accession B60181 !'##molecule_type protein !'##residues 25-30,'K',32-44 ##label KEN REFERENCE S13001 !$#authors Anthony, G.; Stroh, A.; Lottspeich, F.; Kadenbach, B. !$#journal FEBS Lett. (1990) 277:97-100 !$#title Different isozymes of cytochrome c oxidase are expressed in !1bovine smooth muscle and skeletal or heart muscle. !$#cross-references MUID:91099535; PMID:2176624 !$#accession S13003 !'##molecule_type protein !'##residues 25-30 ##label ANT !'##experimental_source smooth muscle REFERENCE A67451 !$#authors Tsukihara, T.; Aoyama, H.; Yamashita, E.; Tomizaki, T.; !1Yamaguchi, H.; Shinzawa-itoh, K.; Nakashima, R.; Yaono, R.; !1Yoshikawa, S. !$#submission submitted to the Brookhaven Protein Data Bank, April 1996 !$#cross-references PDB:1OCC !$#contents annotation; X-ray crystallography, 2.8 angstroms, residues !125-30,'K',32-77 REFERENCE A57981 !$#authors Tsukihara, T.; Aoyama, H.; Yamashita, E.; Tomizaki, T.; !1Yamaguchi, H.; Sinzawa-Itoh, K.; Nakashima, R.; Yaono, R.; !1Yoshikawa, S. !$#journal Science (1996) 272:1136-1144 !$#title The whole structure of the 13-subunit oxidized cytochrome c !1oxidase at 2.8 angstroms. !$#cross-references MUID:96216288; PMID:8638158 !$#contents annotation; X-ray crystallography, 2.8 angstroms GENETICS !$#genome nuclear COMPLEX part of a 13 chain complex spanning the inner mitochondrial !1membrane and consisting of one each of chains I (see !1PIR:ODBO1), II (see PIR:OBBO2), III (see PIR:OTBO3), IV (see !1PIR:OLBO4), Va (see PIR:CABO), Vb (see PIR:OGBO6A), VIa (see !1PIR:OGBO6), VIb (see PIR:OGBO7), VIc (see PIR:OGBO6C), VIIa !1(see PIR:OSBO7A), VIIb (see PIR:OSBO7B), VIIc (see !1PIR:OSBO8A), VIII; the complex may form dimers within the !1mitochondrial inner-membrane FUNCTION !$#description the cytochrome-c oxidase complex catalyzes the oxidation of !1four molecules of reduced cytochrome c in the intracristal !1(or intermembrane) space using one oxygen molecule and four !1protons from the mitochondrial matrix producing two !1molecules of water and lowering the concentration of protons !1in the mitochondrial matrix !$#pathway oxidative phosphorylation; respiratory chain !$#note the role of chain VIII is not clear CLASSIFICATION #superfamily cytochrome-c oxidase chain VIII KEYWORDS cardiac muscle; electron transfer; heart; !1membrane-associated complex; mitochondrial inner membrane; !1mitochondrion; oxidative phosphorylation; oxidoreductase; !1respiratory chain; transmembrane protein FEATURE !$1-24 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$25-70 #product cytochrome-c oxidase chain VIII, cardiac !8#status experimental #label MAT\ !$25-35 #domain mitochondrial matrix #status experimental !8#label MM1\ !$36-59 #domain transmembrane helix #status experimental !8#label TR01\ !$60-70 #domain intracristal #status experimental #label ITC1 SUMMARY #length 70 #molecular-weight 7695 #checksum 4303 SEQUENCE /// ENTRY A64538 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) fixO chain - Helicobacter pylori (strain 26695) ALTERNATE_NAMES cb-type cytochrome-c oxidase 28K chain; cytochrome b410; fixO protein ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A64538 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession A64538 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-232 ##label TOM !'##cross-references GB:AE000536; GB:AE000511; NID:g2313230; !1PIDN:AAD07215.1; PID:g2313232; TIGR:HP0145 CLASSIFICATION #superfamily Rhizobium cytochrome-c oxidase fixO chain KEYWORDS electron transfer; membrane-associated complex; !1oxidoreductase; respiratory chain SUMMARY #length 232 #molecular-weight 26548 #checksum 5579 SEQUENCE /// ENTRY B55582 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) fixO chain - Azorhizobium caulinodans ALTERNATE_NAMES cb-type cytochrome-c oxidase 28K chain; cytochrome b410; fixO protein ORGANISM #formal_name Azorhizobium caulinodans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B55582; S42230 REFERENCE A55582 !$#authors Mandon, K.; Kaminski, P.A.; Elmerich, C. !$#journal J. Bacteriol. (1994) 176:2560-2568 !$#title Functional analysis of the fixNOQP region of Azorhizobium !1caulinodans. !$#cross-references MUID:94222833; PMID:8169204 !$#accession B55582 !'##status preliminary; nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-246 ##label MAN1 !'##cross-references GB:X74410; NID:g456310; PIDN:CAA52430.1; !1PID:g456312 REFERENCE S42229 !$#authors Mandon, K.; Kaminski, P.A.; Mougel, C.; Desnoues, N.; !1Dreyfus, B.; Elmerich, C. !$#journal FEMS Microbiol. Lett. (1993) 114:185-190 !$#title Role of the fixGHI region of Azorhizobium caulinodans in !1free-living and symbiotic nitrogen fixation. !$#cross-references MUID:94109675; PMID:8282187 !$#accession S42230 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-246 ##label MAN2 !'##cross-references EMBL:X74410; NID:g456310; PIDN:CAA52430.1; !1PID:g456312 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1993 CLASSIFICATION #superfamily Rhizobium cytochrome-c oxidase fixO chain KEYWORDS electron transfer; membrane-associated complex; !1oxidoreductase; respiratory chain SUMMARY #length 246 #molecular-weight 27641 #checksum 5848 SEQUENCE /// ENTRY B47468 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) fixO chain - Bradyrhizobium japonicum ALTERNATE_NAMES cb-type cytochrome-c oxidase 28K chain; cytochrome b410; fixO protein; membrane-anchored monoheme cytochrome c ORGANISM #formal_name Bradyrhizobium japonicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B47468 REFERENCE A47468 !$#authors Preisig, O.; Anthamatten, D.; Hennecke, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:3309-3313 !$#title Genes for a microaerobically induced oxidase complex in !1Bradyrhizobium japonicum are essential for a nitrogen-fixing !1endosymbiosis. !$#cross-references MUID:93234486; PMID:8386371 !$#accession B47468 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-244 ##label PRE !'##cross-references GB:L07487; NID:g152196; PIDN:AAA26204.1; !1PID:g152200 !'##experimental_source 110spc4 !'##note sequence extracted from NCBI backbone (NCBIP:129654) CLASSIFICATION #superfamily Rhizobium cytochrome-c oxidase fixO chain KEYWORDS electron transfer; membrane-associated complex; !1oxidoreductase; respiratory chain SUMMARY #length 244 #molecular-weight 27352 #checksum 6898 SEQUENCE /// ENTRY S39989 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) fixO chain - Rhizobium meliloti ALTERNATE_NAMES cb-type cytochrome-c oxidase 28K chain; cytochrome b410; fixO protein ORGANISM #formal_name Rhizobium meliloti DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S39989; S32842 REFERENCE S32837 !$#authors Kahn, D.D. !$#submission submitted to the EMBL Data Library, March 1993 !$#accession S39989 !'##status preliminary !'##molecule_type DNA !'##residues 1-243 ##label KAH !'##cross-references EMBL:Z21854; NID:g49403; PIDN:CAA79902.1; !1PID:g49409 CLASSIFICATION #superfamily Rhizobium cytochrome-c oxidase fixO chain KEYWORDS electron transfer; membrane-associated complex; !1oxidoreductase; respiratory chain SUMMARY #length 243 #molecular-weight 27126 #checksum 4551 SEQUENCE /// ENTRY S49346 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) fixO chain - Rhodobacter capsulatus ALTERNATE_NAMES cb-type cytochrome-c oxidase 28K chain; ccoO protein; cytochrome b410; fixO protein homolog ORGANISM #formal_name Rhodobacter capsulatus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S65859; C54235; D54235; E54235; F54235; S49346 REFERENCE S65858 !$#authors Thoeny-Meyer, L.; Beck, C.; Preisig, O.; Hennecke, H. !$#journal Mol. Microbiol. (1994) 14:705-716 !$#title The ccoNOQP gene cluster codes for a cb-type cytochrome !1oxidase that functions in aerobic respiration of Rhodobacter !1capsulatus. !$#cross-references MUID:95198544; PMID:7891558 !$#accession S65859 !'##status preliminary; nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-242 ##label THO !'##cross-references EMBL:X80134; NID:g556812; PIDN:CAA56434.1; !1PID:g556814 REFERENCE A54235 !$#authors Gray, K.A.; Grooms, M.; Myllykallio, H.; Moomaw, C.; !1Slaughter, C.; Daldal, F. !$#journal Biochemistry (1994) 33:3120-3127 !$#title Rhodobacter capsulatus contains a novel cb-type cytochrome c !1oxidase without a CuA center. !$#cross-references MUID:94176508; PMID:8130227 !$#accession C54235 !'##molecule_type protein !'##residues 'XX',3-6,'XX',9-20 ##label GRA1 !'##experimental_source pMT0-404/MT-RBC1 cells !'##note sequence extracted from NCBI backbone (NCBIP:144512) !$#accession D54235 !'##molecule_type protein !'##residues 119,'H',121-128,'S',130-132,'XSG',136,'F' ##label GRA2 !'##experimental_source pMT0-404/MT-RBC1 cells !'##note sequence extracted from NCBI backbone (NCBIP:144514) !$#accession E54235 !'##molecule_type protein !'##residues 160-164,'L',166-170,'YDAPFQAN' ##label GRA3 !'##experimental_source pMT0-404/MT-RBC1 cells !'##note sequence extracted from NCBI backbone (NCBIP:144517) !$#accession F54235 !'##molecule_type protein !'##residues 180-192,'A',194,'XAN' ##label GRA4 !'##experimental_source pMT0-404/MT-RBC1 cells !'##note sequence extracted from NCBI backbone (NCBIP:144519) GENETICS !$#gene ccoO FUNCTION !$#description this cytochrome-c oxidase complex catalyzes the oxidation of !1four molecules of reduced cytochrome c2 using one oxygen !1molecule and four protons producing two molecules of water !$#pathway respiratory chain CLASSIFICATION #superfamily Rhizobium cytochrome-c oxidase fixO chain KEYWORDS electron transfer; membrane-associated complex; !1oxidoreductase; respiratory chain SUMMARY #length 242 #molecular-weight 27069 #checksum 6838 SEQUENCE /// ENTRY A55582 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) fixN chain - Azorhizobium caulinodans ALTERNATE_NAMES cb-type cytochrome-c oxidase 45K chain; cytochrome b410; fixN protein ORGANISM #formal_name Azorhizobium caulinodans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A55582; S42229 REFERENCE A55582 !$#authors Mandon, K.; Kaminski, P.A.; Elmerich, C. !$#journal J. Bacteriol. (1994) 176:2560-2568 !$#title Functional analysis of the fixNOQP region of Azorhizobium !1caulinodans. !$#cross-references MUID:94222833; PMID:8169204 !$#accession A55582 !'##status preliminary; nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-551 ##label MAN1 !'##cross-references GB:X74410; NID:g456310; PIDN:CAA52429.1; !1PID:g456311 REFERENCE S42229 !$#authors Mandon, K.; Kaminski, P.A.; Mougel, C.; Desnoues, N.; !1Dreyfus, B.; Elmerich, C. !$#journal FEMS Microbiol. Lett. (1993) 114:185-190 !$#title Role of the fixGHI region of Azorhizobium caulinodans in !1free-living and symbiotic nitrogen fixation. !$#cross-references MUID:94109675; PMID:8282187 !$#accession S42229 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-551 ##label MAN2 !'##cross-references EMBL:X74410; NID:g456310; PIDN:CAA52429.1; !1PID:g456311 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1993 CLASSIFICATION #superfamily Rhizobium cytochrome-c oxidase fixN chain; !1cytochrome-c oxidase chain I homology KEYWORDS chromoprotein; copper; electron transfer; heme; iron; !1magnesium; membrane-associated complex; metalloprotein; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$73-502 #domain cytochrome-c oxidase chain I homology #label !8CO1\ !$132,421 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$281,331,332 #binding_site copper (His) #status predicted\ !$419 #binding_site heme iron (His) (axial ligand) #status !8predicted SUMMARY #length 551 #molecular-weight 61842 #checksum 4702 SEQUENCE /// ENTRY S39988 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) fixN chain - Rhizobium meliloti ALTERNATE_NAMES cb-type cytochrome-c oxidase 45K chain; cytochrome b410; fixN protein ORGANISM #formal_name Rhizobium meliloti DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S39988; S32841 REFERENCE S32837 !$#authors Kahn, D.D. !$#submission submitted to the EMBL Data Library, March 1993 !$#accession S39988 !'##status preliminary !'##molecule_type DNA !'##residues 1-539 ##label KAH !'##cross-references EMBL:Z21854; NID:g49403; PIDN:CAA79901.1; !1PID:g49408 CLASSIFICATION #superfamily Rhizobium cytochrome-c oxidase fixN chain; !1cytochrome-c oxidase chain I homology KEYWORDS chromoprotein; copper; electron transfer; heme; iron; !1magnesium; membrane-associated complex; metalloprotein; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$59-487 #domain cytochrome-c oxidase chain I homology #label !8CO1\ !$117,406 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$266,316,317 #binding_site copper (His) #status predicted\ !$404 #binding_site heme iron (His) (axial ligand) #status !8predicted SUMMARY #length 539 #molecular-weight 60868 #checksum 8067 SEQUENCE /// ENTRY A47468 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) fixN chain - Bradyrhizobium japonicum ALTERNATE_NAMES cb-type cytochrome-c oxidase 45K chain; cytochrome b410; fixN protein homolog; heme b/copper-binding oxidase subunit ORGANISM #formal_name Bradyrhizobium japonicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A47468 REFERENCE A47468 !$#authors Preisig, O.; Anthamatten, D.; Hennecke, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:3309-3313 !$#title Genes for a microaerobically induced oxidase complex in !1Bradyrhizobium japonicum are essential for a nitrogen-fixing !1endosymbiosis. !$#cross-references MUID:93234486; PMID:8386371 !$#accession A47468 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-549 ##label PRE !'##cross-references GB:L07487; NID:g152196; PIDN:AAA26203.1; !1PID:g152199 !'##experimental_source 110spc4 !'##note sequence extracted from NCBI backbone (NCBIP:129651) CLASSIFICATION #superfamily Rhizobium cytochrome-c oxidase fixN chain; !1cytochrome-c oxidase chain I homology KEYWORDS chromoprotein; copper; electron transfer; heme; iron; !1magnesium; membrane-associated complex; metalloprotein; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$72-501 #domain cytochrome-c oxidase chain I homology #label !8CO1\ !$131,420 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$280,330,331 #binding_site copper (His) #status predicted\ !$418 #binding_site heme iron (His) (axial ligand) #status !8predicted SUMMARY #length 549 #molecular-weight 61273 #checksum 6191 SEQUENCE /// ENTRY S49495 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) fixN chain - Agrobacterium tumefaciens ALTERNATE_NAMES cb-type cytochrome-c oxidase 45K chain; cytochrome b410; fixN protein ORGANISM #formal_name Agrobacterium tumefaciens DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S54758; S49495 REFERENCE S54758 !$#authors Schlueter, A.; Rueberg, S.; Kraemer, M.; Weidner, S.; !1Priefer, U.B. !$#journal Mol. Gen. Genet. (1995) 247:206-215 !$#title A homolog of the Rhizobium meliloti nitrogen fixation gene !1fixN is involved in the production of a microaerobically !1induced oxidase activity in the phytopathogenic bacterium !1Agrobacterium tumefaciens. !$#cross-references MUID:95272530; PMID:7753030 !$#accession S54758 !'##status preliminary !'##molecule_type DNA !'##residues 1-539 ##label SC2 !'##cross-references EMBL:Z46239; NID:g559396; PIDN:CAA86308.1; !1PID:g559397 GENETICS !$#gene fixN CLASSIFICATION #superfamily Rhizobium cytochrome-c oxidase fixN chain; !1cytochrome-c oxidase chain I homology KEYWORDS chromoprotein; copper; electron transfer; heme; iron; !1magnesium; membrane-associated complex; metalloprotein; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$59-487 #domain cytochrome-c oxidase chain I homology #label !8CO1\ !$117,406 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$266,316,317 #binding_site copper (His) #status predicted\ !$404 #binding_site heme iron (His) (axial ligand) #status !8predicted SUMMARY #length 539 #molecular-weight 60651 #checksum 386 SEQUENCE /// ENTRY S49345 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) fixN chain - Rhodobacter capsulatus ALTERNATE_NAMES cb-type cytochrome-c oxidase 45K chain; ccoN protein; cytochrome b410; fixN protein homolog ORGANISM #formal_name Rhodobacter capsulatus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S65858; A54235; B54235; B59014; S49345 REFERENCE S65858 !$#authors Thoeny-Meyer, L.; Beck, C.; Preisig, O.; Hennecke, H. !$#journal Mol. Microbiol. (1994) 14:705-716 !$#title The ccoNOQP gene cluster codes for a cb-type cytochrome !1oxidase that functions in aerobic respiration of Rhodobacter !1capsulatus. !$#cross-references MUID:95198544; PMID:7891558 !$#accession S65858 !'##status preliminary; nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-532 ##label TH2 !'##cross-references EMBL:X80134; NID:g556812; PIDN:CAA56433.1; !1PID:g556813 REFERENCE A54235 !$#authors Gray, K.A.; Grooms, M.; Myllykallio, H.; Moomaw, C.; !1Slaughter, C.; Daldal, F. !$#journal Biochemistry (1994) 33:3120-3127 !$#title Rhodobacter capsulatus contains a novel cb-type cytochrome c !1oxidase without a CuA center. !$#cross-references MUID:94176508; PMID:8130227 !$#accession A54235 !'##molecule_type protein !'##residues 'X',386-387,'E',389-390,'XXTXLRXQX' ##label GRA1 !'##experimental_source pMT0-404/MT-RBC1 cells !'##note sequence extracted from NCBI backbone (NCBIP:144508) !$#accession B54235 !'##molecule_type protein !'##residues 'XXXA',373-374,'APA',378,'SXIE' ##label GRA2 !'##experimental_source pMT0-404/MT-RBC1 cells !'##note sequence extracted from NCBI backbone (NCBIP:144511) !$#accession B59014 !'##molecule_type protein !'##residues 'D',169-171,'ITL' ##label GRA3 !'##experimental_source pMT0-404/MT-RBC1 cells GENETICS !$#gene ccoN FUNCTION !$#description this cytochrome-c oxidase complex catalyzes the oxidation of !1four molecules of reduced cytochrome c2 using one oxygen !1molecule and four protons producing two molecules of water !$#pathway respiratory chain CLASSIFICATION #superfamily Rhizobium cytochrome-c oxidase fixN chain; !1cytochrome-c oxidase chain I homology KEYWORDS chromoprotein; copper; electron transfer; heme; iron; !1magnesium; membrane-associated complex; metalloprotein; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$53-485 #domain cytochrome-c oxidase chain I homology #label !8CO1\ !$114,404 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$264,314,315 #binding_site copper (His) #status predicted\ !$402 #binding_site heme iron (His) (axial ligand) #status !8predicted SUMMARY #length 532 #molecular-weight 58955 #checksum 9212 SEQUENCE /// ENTRY H64537 #type complete TITLE cytochrome-c oxidase (EC 1.9.3.1) fixN chain - Helicobacter pylori (strain 26695) ALTERNATE_NAMES cb-type cytochrome-c oxidase 45K chain; cytochrome b410; fixN protein ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS H64537 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession H64537 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-488 ##label TOM !'##cross-references GB:AE000536; GB:AE000511; NID:g2313230; !1PIDN:AAD07214.1; PID:g2313231; TIGR:HP0144 CLASSIFICATION #superfamily Rhizobium cytochrome-c oxidase fixN chain; !1cytochrome-c oxidase chain I homology KEYWORDS chromoprotein; copper; electron transfer; heme; iron; !1magnesium; membrane-associated complex; metalloprotein; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$1-439 #domain cytochrome-c oxidase chain I homology #label !8CO1\ !$61,359 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$219,269,270 #binding_site copper (His) #status predicted\ !$357 #binding_site heme iron (His) (axial ligand) #status !8predicted SUMMARY #length 488 #molecular-weight 56058 #checksum 6212 SEQUENCE /// ENTRY OSPSZ #type complete TITLE Pseudomonas cytochrome oxidase (EC 1.9.3.2) precursor - Pseudomonas stutzeri ALTERNATE_NAMES cytochrome cd1 ORGANISM #formal_name Pseudomonas stutzeri DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 21-Jul-2000 ACCESSIONS S13613; A38056 REFERENCE S13613 !$#authors Juengst, A.; Wakabayashi, S.; Matsubara, H.; Zumft, W.G. !$#journal FEBS Lett. (1991) 279:205-209 !$#title The nirSTBM region coding for cytochrome cd(1)-dependent !1nitrite respiration of Pseudomonas stutzeri consists of a !1cluster of mono-, di-, and tetraheme proteins. !$#cross-references MUID:91160715; PMID:2001732 !$#accession S13613 !'##molecule_type DNA !'##residues 1-560 ##label JUE !'##cross-references EMBL:X56813 !$#accession A38056 !'##molecule_type protein !'##residues !127-45;89-102;119-127;137-143;383-396;506-512;519-527; !1537-545;550-560 ##label JUE1 GENETICS !$#gene nirS CLASSIFICATION #superfamily Pseudomonas cytochrome oxidase; cytochrome c6 !1homology KEYWORDS chromoprotein; electron transfer; heme; heterodimer; iron; !1metalloprotein; oxidoreductase FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-560 #product Pseudomonas cytochrome oxidase #status !8experimental #label MAT\ !$37-120 #domain cytochrome c6 homology #label CY6\ !$47,50 #binding_site heme (Cys) (covalent) #status !8predicted\ !$51 #binding_site heme iron (His) (axial ligand) #status !8predicted SUMMARY #length 560 #molecular-weight 61986 #checksum 2566 SEQUENCE /// ENTRY OSPSA #type complete TITLE Pseudomonas cytochrome oxidase (EC 1.9.3.2) precursor - Pseudomonas aeruginosa ALTERNATE_NAMES cytochrome c551; cytochrome cd1; nitrite reductase (cytochrome) ORGANISM #formal_name Pseudomonas aeruginosa DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 31-Dec-2000 ACCESSIONS A32975; A38752; A34255; A34141; C83582 REFERENCE A32975 !$#authors Silvestrini, M.C.; Galeotti, C.L.; Gervais, M.; Schinina, !1E.; Barra, D.; Bossa, F.; Brunori, M. !$#journal FEBS Lett. (1989) 254:33-38 !$#title Nitrite reductase from Pseudomonas aeruginosa: sequence of !1the gene and the protein. !$#cross-references MUID:89378234; PMID:2506077 !$#accession A32975 !'##molecule_type DNA !'##residues 1-568 ##label SIL !'##cross-references GB:X16452; NID:g45357; PIDN:CAA34471.1; PID:g45358 !$#accession A38752 !'##molecule_type protein !'##residues 26-70 ##label SIL2 REFERENCE A34255 !$#authors Arai, H.; Sanbongi, Y.; Igarashi, Y.; Kodama, T. !$#journal FEBS Lett. (1990) 261:196-198 !$#title Cloning and sequencing of the gene encoding cytochrome c-551 !1from Pseudomonas aeruginosa. !$#cross-references MUID:90169115; PMID:2155133 !$#accession A34255 !'##molecule_type DNA !'##residues 462-568 ##label ARA !'##cross-references GB:X51631; NID:g45316; PIDN:CAA35957.1; PID:g45317 REFERENCE A34141 !$#authors Nordling, M.; Young, S.; Karlsson, B.G.; Lundberg, L.G. !$#journal FEBS Lett. (1990) 259:230-232 !$#title The structural gene for cytochrome c-551 from Pseudomonas !1aeruginosa. The nucleotide sequence shows a location !1downstream of the nitrite reductase gene. !$#cross-references MUID:90092552; PMID:2152881 !$#accession A34141 !'##molecule_type DNA !'##residues 462-568 ##label NOR !'##cross-references EMBL:X51319; NID:g45305; PIDN:CAA35702.1; !1PID:g45306 REFERENCE A82950 !$#authors Stover, C.K.; Pham, X.Q.; Erwin, A.L.; Mizoguchi, S.D.; !1Warrener, P.; Hickey, M.J.; Brinkman, F.S.L.; Hufnagle, !1W.O.; Kowalik, D.J.; Lagrou, M.; Garber, R.L.; Goltry, L.; !1Tolentino, E.; Westbrook-Wadman, S.; Yuan, Y.; Brody, L.L.; !1Coulter, S.N.; Folger, K.R.; Kas, A.; Larbig, K.; Lim, R.M.; !1Smith, K.A.; Spencer, D.H.; Wong, G.K.S.; Wu, Z.; Paulsen, !1I.T.; Reizer, J.; Saier, M.H.; Hancock, R.E.W.; Lory, S.; !1Olson, M.V. !$#journal Nature (2000) 406:959-964 !$#title Complete genome sequence of Pseudomonas aeruginosa PA01, an !1opportunistic pathogen. !$#cross-references MUID:20437337; PMID:10984043 !$#accession C83582 !'##status preliminary !'##molecule_type DNA !'##residues 1-568 ##label STO !'##cross-references GB:AE004488; GB:AE004091; NID:g9946372; !1PIDN:AAG03908.1; GSPDB:GN00131; PASP:PA0519 !'##experimental_source strain PAO1 GENETICS !$#gene nirS; PA0519 CLASSIFICATION #superfamily Pseudomonas cytochrome oxidase; cytochrome c6 !1homology KEYWORDS chromoprotein; electron transfer; heme; homodimer; iron; !1metalloprotein; oxidoreductase FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-568 #product Pseudomonas cytochrome oxidase #status !8predicted #label MAT\ !$62-134 #domain cytochrome c6 homology #label CY6\ !$72,75 #binding_site heme (Cys) (covalent) #status !8predicted\ !$76 #binding_site heme iron (His) (axial ligand) #status !8predicted SUMMARY #length 568 #molecular-weight 62653 #checksum 4963 SEQUENCE /// ENTRY S33543 #type complete TITLE catechol oxidase (EC 1.10.3.1) E, precursor [similarity] - tomato ALTERNATE_NAMES polyphenoloxidase ORGANISM #formal_name Lycopersicon esculentum #common_name tomato DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS S33543; JQ1672; S22969 REFERENCE S33539 !$#authors Newman, S.M.; Eannetta, N.T.; Yu, H.; Prince, J.P.; de !1Vicente, C.; Tanksley, S.D.; Steffens, J.C. !$#journal Plant Mol. Biol. (1993) 21:1035-1051 !$#title Organisation of the tomato polyphenol oxidase gene family. !$#cross-references MUID:93257620; PMID:8098228 !$#accession S33543 !'##molecule_type DNA !'##residues 1-587 ##label NEW !'##cross-references EMBL:Z12837; NID:g1403354; PIDN:CAA78299.1; !1PID:g22733 REFERENCE JQ1672 !$#authors Shahar, T.; Hennig, N.; Gutfinger, T.; Hareven, D.; !1Lifschitz, E. !$#journal Plant Cell (1992) 4:135-147 !$#title The tomato 66.3-kD polyphenoloxidase gene: molecular !1identification and developmental expression. !$#cross-references MUID:92338844; PMID:1633491 !$#accession JQ1672 !'##molecule_type DNA !'##residues 1-310,'LWVLN',316-409,'V',411-540,'V',542-566,'I',568-573, !1'G',575-587 ##label SHA !'##cross-references GB:S40548; NID:g251894; PIDN:AAB22610.1; !1PID:g251895 !'##experimental_source tomato flowers cv Tiny Tim LA154 GENETICS !$#gene P2 CLASSIFICATION #superfamily catechol oxidase KEYWORDS copper; oxidoreductase FEATURE !$197,206 #binding_site copper (His) #status predicted\ !$328,332,363 #binding_site copper (His) #status predicted SUMMARY #length 587 #molecular-weight 66236 #checksum 3052 SEQUENCE /// ENTRY S33544 #type complete TITLE catechol oxidase (EC 1.10.3.1) precursor [similarity] - tomato ALTERNATE_NAMES polyphenol oxidase precursor ORGANISM #formal_name Lycopersicon esculentum #common_name tomato DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS S33544; S22970 REFERENCE S33539 !$#authors Newman, S.M.; Eannetta, N.T.; Yu, H.; Prince, J.P.; de !1Vicente, C.; Tanksley, S.D.; Steffens, J.C. !$#journal Plant Mol. Biol. (1993) 21:1035-1051 !$#title Organisation of the tomato polyphenol oxidase gene family. !$#cross-references MUID:93257620; PMID:8098228 !$#accession S33544 !'##molecule_type DNA !'##residues 1-585 ##label NEW !'##cross-references EMBL:Z12838; NID:g1403355; PIDN:CAA78300.1; !1PID:g22735 REFERENCE S22965 !$#authors Newman, S.M.; Eannetta, N.T.; Yu, H.; Prince, J.P.; de !1Vicente, C.; Tanksley, S.D.; Steffens, J.C. !$#submission submitted to the EMBL Data Library, June 1992 !$#description Organization of the tomato polyphenol oxidase gene family. !$#accession S22970 !'##molecule_type DNA !'##residues 1-582,'DLKLGIYLDLDLYLDLKLDLNFILMLNIILILTSS' ##label NE2 !'##cross-references EMBL:Z12838 CLASSIFICATION #superfamily catechol oxidase KEYWORDS oxidoreductase FEATURE !$197,206 #binding_site copper (His) #status predicted\ !$326,330,361 #binding_site copper (His) #status predicted SUMMARY #length 585 #molecular-weight 66182 #checksum 8603 SEQUENCE /// ENTRY S33540 #type complete TITLE catechol oxidase (EC 1.10.3.1) B precursor [similarity] - tomato ORGANISM #formal_name Lycopersicon esculentum #common_name tomato DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS S33540; S22966 REFERENCE S33539 !$#authors Newman, S.M.; Eannetta, N.T.; Yu, H.; Prince, J.P.; de !1Vicente, C.; Tanksley, S.D.; Steffens, J.C. !$#journal Plant Mol. Biol. (1993) 21:1035-1051 !$#title Organisation of the tomato polyphenol oxidase gene family. !$#cross-references MUID:93257620; PMID:8098228 !$#accession S33540 !'##molecule_type DNA !'##residues 1-596 ##label NEW !'##cross-references EMBL:Z12834; NID:g1403351; PIDN:CAA78296.1; !1PID:g22727 CLASSIFICATION #superfamily catechol oxidase KEYWORDS oxidoreductase FEATURE !$199,208 #binding_site copper (His) #status predicted\ !$329,333,371 #binding_site copper (His) #status predicted SUMMARY #length 596 #molecular-weight 67227 #checksum 1552 SEQUENCE /// ENTRY S33539 #type complete TITLE catechol oxidase (EC 1.10.3.1) A/A' precursor [similarity] - tomato ORGANISM #formal_name Lycopersicon esculentum #common_name tomato DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS S33539; S22965 REFERENCE S33539 !$#authors Newman, S.M.; Eannetta, N.T.; Yu, H.; Prince, J.P.; de !1Vicente, C.; Tanksley, S.D.; Steffens, J.C. !$#journal Plant Mol. Biol. (1993) 21:1035-1051 !$#title Organisation of the tomato polyphenol oxidase gene family. !$#cross-references MUID:93257620; PMID:8098228 !$#accession S33539 !'##molecule_type DNA !'##residues 1-630 ##label NEW !'##cross-references EMBL:Z12833; NID:g1403350; PIDN:CAA78295.1; !1PID:g22725 CLASSIFICATION #superfamily catechol oxidase KEYWORDS oxidoreductase FEATURE !$198,207 #binding_site copper (His) #status predicted\ !$328,332,370 #binding_site copper (His) #status predicted SUMMARY #length 630 #molecular-weight 70616 #checksum 1243 SEQUENCE /// ENTRY S24758 #type complete TITLE catechol oxidase (EC 1.10.3.1) precursor - fava bean ALTERNATE_NAMES polyphenol oxidase ORGANISM #formal_name Vicia faba #common_name fava bean DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S24758; S19805 REFERENCE S24758 !$#authors Cary, J.W.; Lax, A.R.; Flurkey, W.H. !$#journal Plant Mol. Biol. (1992) 20:245-253 !$#title Cloning and characterization of cDNAs coding for Vicia faba !1polyphenol oxidase. !$#cross-references MUID:93004477; PMID:1391768 !$#accession S24758 !'##molecule_type mRNA !'##residues 1-606 ##label CAR !'##cross-references EMBL:Z11702 REFERENCE S19805 !$#authors Cary, J. !$#submission submitted to the EMBL Data Library, February 1992 !$#accession S19805 !'##molecule_type mRNA !'##residues 1-247,'T',249-250,'A',252-278,'IG',281-283,286,'RN',287-606 !1##label CA2 !'##cross-references EMBL:Z11702; NID:g22028; PIDN:CAA77764.1; !1PID:g22029 CLASSIFICATION #superfamily catechol oxidase KEYWORDS chloroplast; copper; metalloprotein; oxidoreductase FEATURE !$1-92 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$93-606 #product catechol oxidase #status predicted #label !8MAT\ !$202,211 #binding_site copper (His) #status predicted\ !$333,337,367 #binding_site copper (His) #status predicted SUMMARY #length 606 #molecular-weight 68512 #checksum 5684 SEQUENCE /// ENTRY S52984 #type complete TITLE catechol oxidase (EC 1.10.3.1) precursor - apple tree ALTERNATE_NAMES polyphenol oxidase ORGANISM #formal_name Malus domestica #common_name apple tree DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S52984 REFERENCE S52984 !$#authors Boss, P.K.; Gardner, R.C.; Janssen, B.J.; Ross, G.S. !$#journal Plant Mol. Biol. (1995) 27:429-433 !$#title An apple polyphenol oxidase cDNA is up-regulated in wounded !1tissues. !$#cross-references MUID:95195170; PMID:7888632 !$#accession S52984 !'##status preliminary !'##molecule_type mRNA !'##residues 1-593 ##label BOS !'##cross-references EMBL:L29450; NID:g507279; PIDN:AAA69902.1; !1PID:g507280 CLASSIFICATION #superfamily catechol oxidase KEYWORDS chloroplast; copper; metalloprotein; oxidoreductase FEATURE !$196,205 #binding_site copper (His) #status predicted\ !$327,331,361 #binding_site copper (His) #status predicted SUMMARY #length 593 #molecular-weight 65720 #checksum 3092 SEQUENCE /// ENTRY S52629 #type complete TITLE catechol oxidase (EC 1.10.3.1) precursor - grape ALTERNATE_NAMES polyphenol oxidase ORGANISM #formal_name Vitis sp. #common_name grape DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S52629; S56164; S49167 REFERENCE S52629 !$#authors Dry, I.B.; Robinson, S.P. !$#journal Plant Mol. Biol. (1994) 26:495-502 !$#title Molecular cloning and characterisation of grape berry !1polyphenol oxidase. !$#cross-references MUID:95036022; PMID:7948897 !$#accession S52629 !'##molecule_type mRNA !'##residues 1-607 ##label DRY1 !'##cross-references EMBL:Z27411; NID:g510233; PIDN:CAA81798.1; !1PID:g510234 !$#accession S56164 !'##molecule_type protein !'##residues 105-115 ##label DRY2 GENETICS !$#genome nuclear CLASSIFICATION #superfamily catechol oxidase KEYWORDS chloroplast; copper; metalloprotein; oxidoreductase FEATURE !$1-103 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$104-463 #product catechol oxidase #status experimental #label !8MAT\ !$464-607 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$211,220 #binding_site copper (His) #status predicted\ !$342,346,375 #binding_site copper (His) #status predicted SUMMARY #length 607 #molecular-weight 67346 #checksum 3667 SEQUENCE /// ENTRY KSNCLO #type complete TITLE laccase (EC 1.10.3.2) precursor - Neurospora crassa (strain OR) ALTERNATE_NAMES urishiol oxidase ORGANISM #formal_name Neurospora crassa DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 11-Jun-1999 ACCESSIONS A28523; A29762 REFERENCE A28523 !$#authors Germann, U.A.; Mueller, G.; Hunziker, P.E.; Lerch, K. !$#journal J. Biol. Chem. (1988) 263:885-896 !$#title Characterization of two allelic forms of Neurospora crassa !1laccase. Amino- and carboxyl-terminal processing of a !1precursor. !$#cross-references MUID:88087214; PMID:2961749 !$#accession A28523 !'##molecule_type DNA !'##residues 1-619 ##label GER !'##cross-references EMBL:M14554 REFERENCE A29762 !$#authors Germann, U.A.; Lerch, K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:8854-8858 !$#title Isolation and partial nucleotide sequence of the laccase !1gene from Neurospora crassa: amino acid sequence homology of !1the protein to human ceruloplasmin. !$#cross-references MUID:87067412; PMID:2947240 !$#accession A29762 !'##molecule_type DNA !'##residues 379-619 ##label GE2 !'##cross-references GB:M14554; NID:g168823; PIDN:AAA33590.1; !1PID:g168824 COMMENT This enzyme, which catalyzes the oxidation of benzendiol to !1benzosemiquinone by molecular oxygen, is a multicopper !1oxidase containing type 1, type 2, and type 3 copper !1centers. GENETICS !$#introns 86/3 CLASSIFICATION #superfamily laccase KEYWORDS copper; glycoprotein; oxidoreductase FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-49 #domain propeptide #status predicted #label PRO\ !$50-619 #product laccase #status predicted #label MAT\ !$84-215 #domain amino-terminal beta-barrel #status predicted !8#label BB1\ !$216-372 #domain middle beta-barrel #status predicted #label !8BB2\ !$431-580 #domain carboxyl-terminal beta-barrel #status !8predicted #label BB3\ !$139,282,295,340, !$422,444 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$144,480 #binding_site copper (His) (type 2) #status !8predicted\ !$146,189,191,482, !$548,550 #binding_site 2Cu-O cluster (His) (copper type 3) !8#status predicted\ !$477,549,554 #binding_site copper (His, Cys, His) (type 1) #status !8predicted SUMMARY #length 619 #molecular-weight 68173 #checksum 5508 SEQUENCE /// ENTRY KSNCLT #type complete TITLE laccase (EC 1.10.3.2) precursor - Neurospora crassa (strain TS) ALTERNATE_NAMES urishiol oxidase ORGANISM #formal_name Neurospora crassa DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 11-Jun-1999 ACCESSIONS B28523 REFERENCE A28523 !$#authors Germann, U.A.; Mueller, G.; Hunziker, P.E.; Lerch, K. !$#journal J. Biol. Chem. (1988) 263:885-896 !$#title Characterization of two allelic forms of Neurospora crassa !1laccase. Amino- and carboxyl-terminal processing of a !1precursor. !$#cross-references MUID:88087214; PMID:2961749 !$#accession B28523 !'##molecule_type DNA !'##residues 1-619 ##label GER !'##cross-references EMBL:M18334; NID:g168827; PIDN:AAA33592.1; !1PID:g168828 COMMENT This enzyme, which catalyzes the oxidation of benzendiol to !1benzosemiquinone by molecular oxygen, is a multicopper !1oxidase containing type 1, type 2, and type 3 copper !1centers. GENETICS !$#introns 86/3 CLASSIFICATION #superfamily laccase KEYWORDS copper; glycoprotein; oxidoreductase FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-49 #domain propeptide #status predicted #label PRO\ !$50-619 #product laccase #status predicted #label MAT\ !$84-215 #domain amino-terminal beta-barrel #status predicted !8#label BB1\ !$216-372 #domain middle beta-barrel #status predicted #label !8BB2\ !$431-580 #domain carboxyl-terminal beta-barrel #status !8predicted #label BB3\ !$139,282,295,340, !$422,444 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$144,480 #binding_site copper (His) (type 2) #status !8predicted\ !$146,189,191,482, !$548,550 #binding_site 2Cu-O cluster (His) (copper type 3) !8#status predicted\ !$477,549,554 #binding_site copper (His, Cys, His) (type 1) #status !8predicted SUMMARY #length 619 #molecular-weight 68120 #checksum 5342 SEQUENCE /// ENTRY KSASL1 #type complete TITLE laccase (EC 1.10.3.2) I precursor - Emericella nidulans ORGANISM #formal_name Emericella nidulans, Aspergillus nidulans DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 14-Nov-1997 ACCESSIONS S10149 REFERENCE S10149 !$#authors Aramayo, R.; Timberlake, W.E. !$#journal Nucleic Acids Res. (1990) 18:3415 !$#title Sequence and molecular structure of the Aspergillus nidulans !1yA (laccase I) gene. !$#cross-references MUID:90287738; PMID:2192364 !$#accession S10149 !'##molecule_type DNA !'##residues 1-609 ##label ARA !'##cross-references EMBL:X52552 COMMENT This enzyme is a multicopper oxidase containing type 1, type !12, and type 3 copper centers. GENETICS !$#gene yA !$#introns 65/3; 84/2; 141/2; 198/2; 240/2 FUNCTION !$#description catalyzes the oxidation of benzendiol to benzosemiquinone by !1molecular oxygen CLASSIFICATION #superfamily laccase KEYWORDS copper; glycoprotein; oxidoreductase FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-49 #domain propeptide #status predicted #label PRO\ !$50-609 #product laccase I #status predicted #label MAT\ !$75,257,268,403,443, !$486,531,546 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$79,511 #binding_site copper (His) (type 2) #status !8predicted\ !$81,123,125,513,585, !$587 #binding_site 2Cu-O cluster (His) (copper type 3) !8#status predicted\ !$508,586,591,596 #binding_site copper (His, Cys, His, Met) (type 1) !8#status predicted SUMMARY #length 609 #molecular-weight 68011 #checksum 1894 SEQUENCE /// ENTRY KSKVAO #type complete TITLE L-ascorbate oxidase (EC 1.10.3.3) precursor - cucumber ALTERNATE_NAMES ascorbase ORGANISM #formal_name Cucumis sativus #common_name cucumber DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 11-Jun-1999 ACCESSIONS A30094 REFERENCE A30094 !$#authors Ohkawa, J.; Okada, N.; Shinmyo, A.; Takano, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:1239-1243 !$#title Primary structure of cucumber (Cucumis sativus) ascorbate !1oxidase deduced from cDNA sequence: homology with blue !1copper proteins and tissue-specific expression. !$#cross-references MUID:89145218; PMID:2919172 !$#accession A30094 !'##molecule_type mRNA !'##residues 1-587 ##label OHK !'##cross-references GB:J04494; NID:g167512; PIDN:AAA33119.1; !1PID:g167513 COMMENT This enzyme, which catalyzes the oxidation of L-ascorbate to !1dehydroascorbate by molecular oxygen, is a multicopper !1oxidase containing type 1, type 2, and type 3 copper !1centers. CLASSIFICATION #superfamily laccase KEYWORDS copper; glycoprotein; oxidoreductase FEATURE !$1-33 #domain signal sequence #status predicted #label SIG\ !$34-587 #product L-ascorbate oxidase #status predicted #label !8MAT\ !$38-168 #domain amino-terminal beta-barrel #status predicted !8#label BB1\ !$169-346 #domain middle beta-barrel #status predicted #label !8BB2\ !$379-574 #domain carboxyl-terminal beta-barrel #status !8predicted #label BB3\ !$54-236,116-574, !$215-228 #disulfide_bonds #status predicted\ !$95,483 #binding_site copper (His) (type 2) #status !8predicted\ !$97,139,141,485,542, !$544 #binding_site 2Cu-O cluster (His) (copper type 3) !8#status predicted\ !$360,401,475 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$480,543,548,553 #binding_site copper (His, Cys, His, Met) (type 1) !8#status predicted SUMMARY #length 587 #molecular-weight 65875 #checksum 6009 SEQUENCE /// ENTRY KSPSCY #type complete TITLE copper resistance protein precursor A - Pseudomonas syringae pv. tomato ORGANISM #formal_name Pseudomonas syringae pv. tomato DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 11-Jun-1999 ACCESSIONS A32018 REFERENCE A32018 !$#authors Mellano, M.A.; Cooksey, D.A. !$#journal J. Bacteriol. (1988) 170:2879-2883 !$#title Nucleotide sequence and organization of copper resistance !1genes from Pseudomonas syringae pv. tomato. !$#cross-references MUID:88227880; PMID:3372485 !$#accession A32018 !'##molecule_type DNA !'##residues 1-609 ##label MEL !'##cross-references GB:M19930; NID:g151187; PIDN:AAA25806.1; !1PID:g151188 GENETICS !$#gene copA CLASSIFICATION #superfamily laccase KEYWORDS copper; tandem repeat FEATURE !$1-32 #domain signal sequence #status predicted #label SIG\ !$33-609 #product copper resistance protein A #status !8predicted #label MAT\ !$367-434 #region 8-residue repeats (D-H-X-X-M-X-G-M)\ !$542,591,596,601 #binding_site copper (His, Cys, His, Met) (type 1) !8#status predicted SUMMARY #length 609 #molecular-weight 67354 #checksum 9679 SEQUENCE /// ENTRY A42226 #type complete TITLE bo-type ubiquinol oxidase (EC 1.10.3.-) chain II precursor - Escherichia coli (strain K-12) ALTERNATE_NAMES cytochrome o chain II ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS A42226; A42227; S37392; A42572; H64772 REFERENCE A42226 !$#authors Chepuri, V.; Lemieux, L.; Au, D.C.T.; Gennis, R.B. !$#journal J. Biol. Chem. (1990) 265:11185-11192 !$#title The sequence of the cyo operon indicates substantial !1structural similarities between the cytochrome o ubiquinol !1oxidase of Escherichia coli and the aa-3-type family of !1cytochrome c oxidases. !$#cross-references MUID:90293062; PMID:2162835 !$#accession A42226 !'##status preliminary !'##molecule_type DNA !'##residues 1-315 ##label CHE !'##cross-references GB:J05492; NID:g145651; PIDN:AAA23631.1; !1PID:g145652 REFERENCE A42227 !$#authors Minagawa, J.; Nakamura, H.; Yamato, I.; Mogi, T.; Anraku, Y. !$#journal J. Biol. Chem. (1990) 265:11198-11203 !$#title Transcriptional regulation of the cytochrome b-562-o complex !1in Escherichia coli. Gene expression and molecular !1characterization of the promoter. !$#cross-references MUID:90293064; PMID:2162837 !$#accession A42227 !'##status preliminary !'##molecule_type DNA !'##residues 1-80 ##label MIN !'##cross-references GB:M55258; GB:M37917; NID:g145649; PIDN:AAA23630.1; !1PID:g145650 REFERENCE S37389 !$#authors Lindquist, S.; Weston-Hafer, K.; Schmidt, H.; Pul, C.; !1Korfmann, G.; Erickson, J.; Sanders, C.; Martin, H.H.; !1Normark, S. !$#journal Mol. Microbiol. (1993) 9:703-715 !$#title AmpG, a signal transducer in chromosomal beta-lactamase !1induction. !$#cross-references MUID:94049112; PMID:8231804 !$#accession S37392 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-66 ##label LIN !'##cross-references GB:S67816; NID:g459274; PIDN:AAB28885.1; !1PID:g459278 REFERENCE A42572 !$#authors Minghetti, K.C.; Goswitz, V.C.; Gabriel, N.E.; Hill, J.J.; !1Barassi, C.A.; Georgiou, C.D.; Chan, S.I.; Gennis, R.B. !$#journal Biochemistry (1992) 31:6917-6924 !$#title Modified, large-scale purification of the cytochrome o !1complex (bo-type oxidase) of Escherichia coli yields a two !1heme/one copper terminal oxidase with high specific !1activity. !$#cross-references MUID:92345252; PMID:1322173 !$#accession A42572 !'##status preliminary !'##molecule_type protein !'##residues 153-171 ##label MI2 !'##note sequence extracted from NCBI backbone (NCBIP:110120) REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64772 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-315 ##label BLAT !'##cross-references GB:AE000149; GB:U00096; NID:g1786628; !1PIDN:AAC73535.1; PID:g1786635; UWGP:b0432 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene cyoA !$#map_position 10 min COMPLEX heterooligomer; the cyoABCDE gene products are required for !1bo-type ubiquinol oxidase; the oxidase complex contains !1subunits I, II, III and IV and heme O synthase (cyoE) as !1polypeptides; subunits II, III and IV may be required for !1the assembly of the metal centers in subunit I FUNCTION !$#description the cytochrome o complex catalyzes the two-eletron oxidation !1of ubiquinol-8 and the four-eletron reduction of molecular !1oxygen to water CLASSIFICATION #superfamily bo-type ubiquinol oxidase chain II precursor; !1cytochrome-c oxidase chain II homology KEYWORDS copper; electron transfer; membrane-associated complex; !1oxidoreductase; respiratory chain; transmembrane protein FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-315 #product bo-type ubiquinol oxidase chain II #status !8predicted #label MAT\ !$47-63 #domain transmembrane #status predicted #label TM1\ !$90-106 #domain transmembrane #status predicted #label TM2 SUMMARY #length 315 #molecular-weight 34911 #checksum 5505 SEQUENCE /// ENTRY A36885 #type complete TITLE bo-type ubiquinol oxidase (EC 1.10.3.-) chain II precursor - Acetobacter aceti ALTERNATE_NAMES cytochrome a1 chain II ORGANISM #formal_name Acetobacter aceti DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A36885 REFERENCE A36885 !$#authors Fukaya, M.; Tayama, K.; Tamaki, T.; Ebisuya, H.; Okumura, !1H.; Kawamura, Y.; Horinouchi, S.; Beppu, T. !$#journal J. Bacteriol. (1993) 175:4307-4314 !$#title Characterization of a cytochrome a-1 that functions as a !1ubiquinol oxidase in Acetobacter aceti. !$#cross-references MUID:93322308; PMID:8392509 !$#accession A36885 !'##status preliminary !'##molecule_type DNA !'##residues 1-307 ##label FUK !'##cross-references GB:D13185; NID:g409064; PIDN:BAA02480.1; !1PID:g433186 !'##experimental_source isolate 1023 GENETICS !$#gene cyaB COMPLEX heterotetramer; chains I, II, III and IV FUNCTION !$#description terminal oxidase for ethanol oxidation CLASSIFICATION #superfamily bo-type ubiquinol oxidase chain II precursor; !1cytochrome-c oxidase chain II homology KEYWORDS copper; electron transfer; heterotetramer; !1membrane-associated complex; oxidoreductase; respiratory !1chain; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-307 #product bo-type ubiquinol oxidase chain II #status !8predicted #label MAT\ !$48-64 #domain transmembrane #status predicted #label TM1\ !$89-105 #domain transmembrane #status predicted #label TM2 SUMMARY #length 307 #molecular-weight 33921 #checksum 4431 SEQUENCE /// ENTRY E69687 #type complete TITLE bo-type ubiquinol oxidase (EC 1.10.3.-) chain II qoxA - Bacillus subtilis ALTERNATE_NAMES quinol oxidase aa3-600 chain qoxA ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS E69687; A38129; S39692 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69687 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-321 ##label KUN !'##cross-references GB:Z99123; GB:AL009126; NID:g2636240; !1PIDN:CAB15843.1; PID:g2636352 !'##experimental_source strain 168 REFERENCE A38129 !$#authors Santana, M.; Kunst, F.; Hullo, M.F.; Rapoport, G.; Danchin, !1A.; Glaser, P. !$#journal J. Biol. Chem. (1992) 267:10225-10231 !$#title Molecular cloning, sequencing, and physiological !1characterization of the qox operon from Bacillus subtilis !1encoding the aa3-600 quinol oxidase. !$#cross-references MUID:92268053; PMID:1316894 !$#accession A38129 !'##molecule_type DNA !'##residues 'MHFRFITSIGRMV',2-38,'D',39-321 ##label SAN !'##cross-references GB:M86548; NID:g143395; PIDN:AAA22686.1; !1PID:g143396 !'##note sequence extracted from NCBI backbone (NCBIN:103632, !1NCBIP:103599) REFERENCE S39655 !$#authors Glaser, P.; Kunst, F.; Arnaud, M.; Coudart, M.P.; Gonzales, !1W.; Hullo, M.F.; Ionescu, M.; Lubochinsky, B.; Marcelino, !1L.; Moszer, I.; Presecan, E.; Santana, M.; Schneider, E.; !1Schweizer, J.; Vertes, A.; Rapoport, G.; Danchin, A. !$#journal Mol. Microbiol. (1993) 10:371-384 !$#title Bacillus subtilis genome project: cloning and sequencing of !1the 97 kb region from 325 degrees to 333 degrees. !$#cross-references MUID:95020537; PMID:7934828 !$#accession S39692 !'##molecule_type DNA !'##residues 'V',2-38,'D',39-321 ##label GLA !'##cross-references EMBL:X73124 GENETICS !$#gene qoxA CLASSIFICATION #superfamily bo-type ubiquinol oxidase chain II precursor; !1cytochrome-c oxidase chain II homology KEYWORDS copper; electron transfer; membrane-associated complex; !1oxidoreductase; respiratory chain FEATURE !$31-229 #domain cytochrome-c oxidase chain II homology #label !8CO2 SUMMARY #length 321 #molecular-weight 36253 #checksum 2559 SEQUENCE /// ENTRY JC5900 #type complete TITLE bo-type ubiquinol oxidase (EC 1.10.3.-) chain II - Bradyrhizobium japonicum ORGANISM #formal_name Bradyrhizobium japonicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JC5900 REFERENCE JC5900 !$#authors Surpin, M.A.; Luebben, M.; Maier, R.J. !$#journal Gene (1996) 183:201-206 !$#title The Bradyrhizobium japonicum coxWXYZ gene cluster encodes a !1bb3-type ubiquinol oxidase. !$#cross-references MUID:97149299; PMID:8996107 !$#accession JC5900 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-277 ##label SUR GENETICS !$#gene coxW CLASSIFICATION #superfamily bo-type ubiquinol oxidase chain II precursor; !1cytochrome-c oxidase chain II homology KEYWORDS copper; electron transfer; membrane-associated complex; !1oxidoreductase; respiratory chain SUMMARY #length 277 #molecular-weight 30294 #checksum 1157 SEQUENCE /// ENTRY OPBYC #type complete TITLE cytochrome-c peroxidase (EC 1.11.1.5) precursor - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YKR066c ORGANISM #formal_name Saccharomyces cerevisiae DATE 22-May-1981 #sequence_revision 02-May-1994 #text_change 21-Jul-2000 ACCESSIONS S19064; S38142; A00499; A90066; A92345; C23116 REFERENCE S19064 !$#authors Piattoni, M.; Miyazaki, W.; Jayaraman, K.; Kaput, J. !$#submission submitted to the EMBL Data Library, October 1991 !$#description Isolation and sequence analysis of a second allele of the !1yeast nuclear gene cytochrome c peroxidase. !$#accession S19064 !'##molecule_type DNA !'##residues 1-361 ##label PIA !'##cross-references EMBL:X62422; NID:g3471; PIDN:CAA44288.1; PID:g3472 REFERENCE S38130 !$#authors van Vliet-Reedijk, J.C.; Planta, R.J. !$#submission submitted to the Protein Sequence Database, March 1994 !$#accession S38142 !'##molecule_type DNA !'##residues 1-361 ##label VAN !'##cross-references EMBL:Z28291; NID:g486534; PIDN:CAA82145.1; !1PID:g486535; GSPDB:GN00011; MIPS:YKR066c !'##experimental_source strain S288C REFERENCE A92358 !$#authors Kaput, J.; Goltz, S.; Blobel, G. !$#journal J. Biol. Chem. (1982) 257:15054-15058 !$#title Nucleotide sequence of the yeast nuclear gene for cytochrome !1c peroxidase precursor. Functional implications of the !1presequence for protein transport into mitochondria. !$#cross-references MUID:83082819; PMID:6294090 !$#accession A00499 !'##molecule_type DNA !'##residues 1-33,'A',34-40,'H',42-119,'I',121-218,'G',220-361 ##label !1KAP !'##cross-references EMBL:J01468 REFERENCE A90066 !$#authors Takio, K.; Titani, K.; Ericsson, L.H.; Yonetani, T. !$#journal Arch. Biochem. Biophys. (1980) 203:615-629 !$#title Primary structure of yeast cytochrome c peroxidase. II. The !1complete amino acid sequence. !$#cross-references MUID:81108305; PMID:6257176 !$#accession A90066 !'##molecule_type protein !'##residues 68-144,'DN',147-230,232-361 ##label TAK !'##note this enzyme forms a one-to-one complex with cytochrome-c !'##note Arg-115, Trp-118, His-119, and His-242 are essential and may be !1at the active site REFERENCE A92345 !$#authors Goltz, S.; Kaput, J.; Blobel, G. !$#journal J. Biol. Chem. (1982) 257:11186-11190 !$#title Isolation of the yeast nuclear gene encoding the !1mitochondrial protein, cytochrome c peroxidase. !$#cross-references MUID:82265845; PMID:6286684 !$#accession A92345 !'##molecule_type mRNA !'##residues 253-332 ##label GOL !'##cross-references EMBL:J01321; NID:g171351; PIDN:AAA88710.1; !1PID:g171352 GENETICS !$#gene SGD:CCP1; CYPX; MIPS:YKR066c !'##cross-references SGD:S0001774; MIPS:YKR066c !$#map_position 11R !$#genome nuclear CLASSIFICATION #superfamily cytochrome-c peroxidase KEYWORDS chromoprotein; heme; iron; metalloprotein; mitochondrion; !1oxidoreductase FEATURE !$1-67 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$68-361 #product cytochrome-c peroxidase #status experimental !8#label MAT\ !$119 #active_site His (distal axial ligand) #status !8predicted\ !$242 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted\ !$258 #active_site Trp (tryptophyl radical intermediate) !8#status experimental SUMMARY #length 361 #molecular-weight 40353 #checksum 6641 SEQUENCE /// ENTRY I53515 #type complete TITLE cytochrome-c peroxidase (EC 1.11.1.5) precursor PA4587 [validated] - Pseudomonas aeruginosa (strains PAO1 and NTCC 6750) ALTERNATE_NAMES cytochrome c551 peroxidase ORGANISM #formal_name Pseudomonas aeruginosa DATE 02-Aug-1996 #sequence_revision 02-Aug-1996 #text_change 20-Oct-2000 ACCESSIONS I53515; S05001; S68397; G83072; S65930 REFERENCE I53515 !$#authors Ridout, C.J.; James, R.; Greenwood, C. !$#journal FEBS Lett. (1995) 365:152-154 !$#title Nucleotide sequence encoding the di-haem cytochrome c551 !1peroxidase from Pseudomonas aeruginosa. !$#cross-references MUID:95300964; PMID:7781769 !$#accession I53515 !'##molecule_type DNA !'##residues 1-346 ##label RID !'##cross-references EMBL:U23766; NID:g887790; PIDN:AAC43378.1; !1PID:g887791 !'##experimental_source NTCC 6750 REFERENCE S05001 !$#authors Roennberg, M.; Kalkkinen, N.; Ellfolk, N. !$#journal FEBS Lett. (1989) 250:175-178 !$#title The primary structure of Pseudomonas cytochrome c !1peroxidase. !$#cross-references MUID:89325562; PMID:2546794 !$#accession S05001 !'##molecule_type protein !'##residues 24-80,'D',82,'D',84-85,'G',87-92,94-95,'G',97-101,121-136, !1'Q',138-163,'A',165-197,'I',199-227,229-285,'QG',288-289, !1'Q',291-346 ##label ROE !'##note 81-Gly, 83-Gly, 152-Val, 164-Pro, 198-Lys, and 334-Trp were !1also found REFERENCE S68397 !$#authors Samyn, B.; van Craenenbroeck, K.; de Smet, L.; Vandenberghe, !1I.; Pettigrew, G.; van Beeumen, J. !$#journal FEBS Lett. (1995) 377:145-149 !$#title A reinvestigation of the covalent structure of Pseudomonas !1aeruginosa cytochrome c peroxidase. !$#cross-references MUID:96128216; PMID:8543038 !$#accession S68397 !'##molecule_type protein !'##residues 24-174,'V',176-346 ##label SAM REFERENCE A82950 !$#authors Stover, C.K.; Pham, X.Q.; Erwin, A.L.; Mizoguchi, S.D.; !1Warrener, P.; Hickey, M.J.; Brinkman, F.S.L.; Hufnagle, !1W.O.; Kowalik, D.J.; Lagrou, M.; Garber, R.L.; Goltry, L.; !1Tolentino, E.; Westbrook-Wadman, S.; Yuan, Y.; Brody, L.L.; !1Coulter, S.N.; Folger, K.R.; Kas, A.; Larbig, K.; Lim, R.M.; !1Smith, K.A.; Spencer, D.H.; Wong, G.K.S.; Wu, Z.; Paulsen, !1I.T.; Reizer, J.; Saier, M.H.; Hancock, R.E.W.; Lory, S.; !1Olson, M.V. !$#journal Nature (2000) 406:959-964 !$#title Complete genome sequence of Pseudomonas aeruginosa PA01, an !1opportunistic pathogen. !$#cross-references MUID:20437337; PMID:10984043 !$#accession G83072 !'##molecule_type DNA !'##residues 1-346 ##label STO !'##cross-references GB:AE004872; GB:AE004091; NID:g9950829; !1PIDN:AAG07975.1; GSPDB:GN00131; PASP:PA4587 !'##experimental_source strain PAO1 GENETICS !$#gene ccpR; PA4587 CLASSIFICATION #superfamily Pseudomonas cytochrome-c peroxidase; !1Pseudomonas cytochrome-c peroxidase homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; oxidoreductase FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-346 #product cytochrome-c peroxidase #status experimental !8#label MAT\ !$48-295 #domain Pseudomonas cytochrome-c peroxidase homology !8#label PCCP\ !$74,77 #binding_site heme (Cys) (covalent) (low potential) !8#status predicted\ !$78,284 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$220,223 #binding_site heme (Cys) (covalent) (high potential) !8#status predicted\ !$224,298 #binding_site heme iron (His, Met) (axial ligands) !8(high potential) #status predicted SUMMARY #length 346 #molecular-weight 37403 #checksum 4589 SEQUENCE /// ENTRY S47738 #type complete TITLE cytochrome-c peroxidase (EC 1.11.1.5) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 27-Jan-1995 #sequence_revision 02-Aug-1996 #text_change 01-Mar-2002 ACCESSIONS S47738; A65150 REFERENCE S47666 !$#authors Plunkett, G. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S47738 !'##molecule_type DNA !'##residues 1-465 ##label PLU !'##cross-references EMBL:U00039; NID:g466582; PIDN:AAB18494.1; !1PID:g466655 !'##note this sequence contains three cytochrome c-type heme-binding !1motifs REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65150 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-465 ##label BLAT !'##cross-references GB:AE000428; GB:U00096; NID:g1789931; !1PIDN:AAC76543.1; PID:g1789935; UWGP:b3518 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yhjA CLASSIFICATION #superfamily Escherichia coli cytochrome-c peroxidase; !1Pseudomonas cytochrome-c peroxidase homology KEYWORDS chromoprotein; electron transfer; heme; iron; !1metalloprotein; oxidoreductase FEATURE !$181-426 #domain Pseudomonas cytochrome-c peroxidase homology !8#label PCCP\ !$59,62 #binding_site heme (Cys) (covalent) #status !8predicted\ !$63,195 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$207,210 #binding_site heme (Cys) (covalent) (low potential) !8#status predicted\ !$211,415 #binding_site heme iron (His) (axial ligands) (low !8potential) #status predicted\ !$351,354 #binding_site heme (Cys) (covalent) (high potential) !8#status predicted\ !$355,429 #binding_site heme iron (His, Met) (axial ligands) !8(high potential) #status predicted SUMMARY #length 465 #molecular-weight 51570 #checksum 664 SEQUENCE /// ENTRY CSHU #type complete TITLE catalase (EC 1.11.1.6) precursor [validated] - human ALTERNATE_NAMES hydrogen peroxidase; hydrogen peroxide oxidoreductase ORGANISM #formal_name Homo sapiens #common_name man DATE 17-Mar-1987 #sequence_revision 18-Aug-1995 #text_change 08-Dec-2000 ACCESSIONS A23646; A23651; A00501; I55606 REFERENCE A23646 !$#authors Quan, F.; Korneluk, R.G.; Tropak, M.B.; Gravel, R.A. !$#journal Nucleic Acids Res. (1986) 14:5321-5335 !$#title Isolation and characterization of the human catalase gene. !$#cross-references MUID:86286546; PMID:3755525 !$#accession A23646 !'##molecule_type DNA !'##residues 1-527 ##label QUA !'##cross-references GB:X04085; NID:g29682; PIDN:CAA27721.1; !1PID:g1228085 REFERENCE A23651 !$#authors Bell, G.I.; Najarian, R.C.; Mullenbach, G.T.; Hallewell, !1R.A. !$#journal Nucleic Acids Res. (1986) 14:5561-5562 !$#title cDNA sequence coding for human kidney catalase. !$#cross-references MUID:86286565; PMID:3755526 !$#accession A23651 !'##molecule_type mRNA !'##residues 1-527 ##label BEL !'##cross-references GB:X04076; NID:g29720; PIDN:CAA27717.1; PID:g29721 REFERENCE A00501 !$#authors Korneluk, R.G.; Quan, F.; Lewis, W.H.; Guise, K.S.; Willard, !1H.F.; Holmes, M.T.; Gravel, R.A. !$#journal J. Biol. Chem. (1984) 259:13819-13823 !$#title Isolation of human fibroblast catalase cDNA clones. Sequence !1of clones derived from spliced and unspliced mRNA. !$#cross-references MUID:85054813; PMID:6548744 !$#accession A00501 !'##molecule_type mRNA !'##residues 77-527 ##label KOR !'##cross-references GB:K02400; NID:g940256; PIDN:AAB59522.1; !1PID:g179950 !'##experimental_source fibroblast !'##note the carboxyl-terminal may be subject to tissue specific !1processing REFERENCE I55606 !$#authors Yoo, J.H.; Erzurum, S.C.; Hay, J.G.; Lemarchand, P.; !1Crystal, R.G. !$#journal J. Clin. Invest. (1994) 93:297-302 !$#title Vulnerability of the human airway epithelium to hyperoxia. !1Constitutive expression of the catalase gene in human !1bronchial epithelial cells despite oxidant stress. !$#cross-references MUID:94110338; PMID:8282800 !$#accession I55606 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-22 ##label RES !'##cross-references GB:L13609; NID:g388711; PIDN:AAA16651.1; !1PID:g388712 REFERENCE A44717 !$#authors Schroeder, W.A.; Shelton, J.R.; Shelton, J.B.; Apell, G.; !1Evans, L.; Bonaventura, J.; Fang, R.S. !$#journal Arch. Biochem. Biophys. (1982) 214:422-424 !$#title The partial amino acid sequence of human erythrocyte !1catalase. !$#cross-references MUID:82205126; PMID:7082010 !$#contents annotation; sequence of peptides differing in composition !1from bovine COMMENT Catalase occurs in almost all aerobically respiring !1organisms and serves to protect cells from the toxic effects !1of hydrogen peroxide. GENETICS !$#gene GDB:CAT !'##cross-references GDB:119049; OMIM:115500 !$#map_position 11p13-11p13 !$#introns 22/3; 80/1; 117/1; 160/3; 195/3; 237/3; 301/3; 352/3; 399/1; !1442/3; 478/3; 506/3 COMPLEX homotetramer FUNCTION !$#description catalyzes the conversion of two of molecules of hydrogen !1peroxide to two molecules of water and dioxygen CLASSIFICATION #superfamily catalase KEYWORDS blocked amino end; chromoprotein; heme; homotetramer; iron; !1metalloprotein; oxidoreductase; peroxisome FEATURE !$2-527 #product catalase #status experimental #label MAT\ !$2-519 #product catalase, peroxisomal form #status predicted !8#label MAT2\ !$517-519 #region peroxisome/glyoxysome location signal !8(S-[RKH]-L) motif\ !$2 #modified_site blocked amino end (Ala) (in mature !8form) (probably acetylated) #status experimental\ !$75,114,148 #active_site His, Ser, Asn #status predicted\ !$358 #binding_site heme iron (Tyr) (axial ligand) #status !8predicted SUMMARY #length 527 #molecular-weight 59756 #checksum 6366 SEQUENCE /// ENTRY CSRT #type complete TITLE catalase (EC 1.11.1.6) - rat ALTERNATE_NAMES hydrogen peroxidase; hydrogen peroxide oxidoreductase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 03-Mar-2000 ACCESSIONS JU0065; A25965; I52202 REFERENCE JU0065 !$#authors Nakashima, H.; Yamamoto, M.; Goto, K.; Osumi, T.; Hashimoto, !1T.; Endo, H. !$#journal Gene (1989) 79:279-288 !$#title Isolation and characterization of the rat catalase-encoding !1gene. !$#cross-references MUID:90006757; PMID:2792765 !$#accession JU0065 !'##molecule_type DNA !'##residues 1-527 ##label NAK !'##cross-references GB:M25680; GB:M23742; NID:g203333; PIDN:AAB42378.1; !1PID:g203335 REFERENCE A25965 !$#authors Furuta, S.; Hayashi, H.; Hijikata, M.; Miyazawa, S.; Osumi, !1T.; Hashimoto, T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:313-317 !$#title Complete nucleotide sequence of cDNA and deduced amino acid !1sequence of rat liver catalase. !$#cross-references MUID:86094381; PMID:3455767 !$#accession A25965 !'##molecule_type mRNA !'##residues 1-527 ##label FUR !'##cross-references GB:M11670; NID:g203344; PIDN:AAA40884.1; !1PID:g203345 !'##experimental_source liver REFERENCE I52202 !$#authors Osumi, T.; Ozasa, H.; Miyazawa, S.; Hashimoto, T. !$#journal Biochem. Biophys. Res. Commun. (1984) 122:831-837 !$#title Molecular cloning of cDNA for rat liver catalase. !$#cross-references MUID:84280086; PMID:6547842 !$#accession I52202 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 399-433,'N',435-527 ##label RES !'##cross-references GB:K01929; NID:g203346; PIDN:AAA40885.1; !1PID:g203347 GENETICS !$#gene cat !$#introns 22/3; 80/1; 117/1; 160/3; 195/3; 237/3; 301/3; 352/3; 399/1; !1442/3; 478/3; 506/3 COMPLEX homotetramer FUNCTION !$#description catalyzes the conversion of two of molecules of hydrogen !1peroxide to two molecules of water and dioxygen CLASSIFICATION #superfamily catalase KEYWORDS chromoprotein; heme; homotetramer; iron; metalloprotein; !1oxidoreductase; peroxisome FEATURE !$75,114,148 #active_site His, Ser, Asn #status predicted\ !$358 #binding_site heme iron (Tyr) (axial ligand) #status !8predicted SUMMARY #length 527 #molecular-weight 59757 #checksum 6407 SEQUENCE /// ENTRY CSBO #type complete TITLE catalase (EC 1.11.1.6) [validated] - bovine ALTERNATE_NAMES hydrogen peroxidase; hydrogen peroxide oxidoreductase ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 05-Apr-1983 #sequence_revision 05-Apr-1983 #text_change 15-Sep-2000 ACCESSIONS A00500 REFERENCE A90067 !$#authors Schroeder, W.A.; Shelton, J.R.; Shelton, J.B.; Robberson, !1B.; Apell, G.; Fang, R.S.; Bonaventura, J. !$#journal Arch. Biochem. Biophys. (1982) 214:397-421 !$#title The complete amino acid sequence of bovine liver catalase !1and the partial sequence of bovine erythrocyte catalase. !$#cross-references MUID:82205125; PMID:7082009 !$#accession A00500 !'##molecule_type protein !'##residues 1-506 ##label SCH !'##experimental_source liver REFERENCE A92872 !$#authors Murthy, M.R.N.; Reid III, T.J.; Sicignano, A.; Tanaka, N.; !1Rossmann, M.G. !$#journal J. Mol. Biol. (1981) 152:465-499 !$#title Structure of beef liver catalase. !$#cross-references MUID:82122604; PMID:7328661 !$#contents annotation; X-ray crystallography, 2.5 angstroms, residues !13-500 !$#note no disulfide bonds are present REFERENCE A50778 !$#authors Murthy, M.R.N.; Reid III, T.J.; Sicignano, A.; Tanaka, N.; !1Fita, I.; Rossmann, M.G. !$#submission submitted to the Brookhaven Protein Data Bank, November 1984 !$#cross-references PDB:7CAT !$#contents annotation; X-ray crystallography, 2.5 angstroms, residues !13-500 COMPLEX homotetramer FUNCTION !$#description catalyzes the conversion of two of molecules of hydrogen !1peroxide to two molecules of water and dioxygen CLASSIFICATION #superfamily catalase KEYWORDS blocked amino end; chromoprotein; heme; homotetramer; iron; !1metalloprotein; oxidoreductase; peroxisome FEATURE !$1 #modified_site blocked amino end (Ala) (probably !8acetylated) #status experimental\ !$74 #active_site His #status experimental\ !$113,147 #active_site Ser, Asn #status predicted\ !$357 #binding_site heme iron (Tyr) (axial ligand) #status !8experimental SUMMARY #length 506 #molecular-weight 57585 #checksum 9451 SEQUENCE /// ENTRY CSFF #type complete TITLE catalase (EC 1.11.1.6) - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 03-Mar-2000 ACCESSIONS S12725; S69287; S15059 REFERENCE S12725 !$#authors Orr, E.C.; Bewley, G.C.; Orr, W.C. !$#journal Nucleic Acids Res. (1990) 18:3663 !$#title cDNA and deduced amino acid sequence of Drosophila catalase. !$#cross-references MUID:90301508; PMID:2362827 !$#accession S12725 !'##molecule_type mRNA !'##residues 1-506 ##label ORR1 !'##cross-references EMBL:X52286; NID:g7689; PIDN:CAA36529.1; PID:g7690 REFERENCE S69287 !$#authors Orr, W.C.; Orr, E.C.; Legan, S.K.; Sohal, R.S. !$#journal Arch. Biochem. Biophys. (1996) 330:251-258 !$#title Molecular analysis of the Drosophila catalase gene. !$#cross-references MUID:96239139; PMID:8660653 !$#accession S69287 !'##status preliminary !'##molecule_type DNA !'##residues 1-506 ##label ORR !'##cross-references EMBL:U00145; NID:g451307; PIDN:AAC13738.1; !1PID:g451308 GENETICS !$#gene FlyBase:Cat !'##cross-references FlyBase:FBgn0000261 !$#map_position 3L 75D-E1 !$#introns 19/3; 326/3 CLASSIFICATION #superfamily catalase KEYWORDS chromoprotein; heme; iron; metalloprotein; oxidoreductase FEATURE !$73,112,146 #active_site His, Ser, Asn #status predicted\ !$356 #binding_site heme iron (Tyr) (axial ligand) #status !8predicted SUMMARY #length 506 #molecular-weight 57149 #checksum 7909 SEQUENCE /// ENTRY CSRZ #type complete TITLE catalase (EC 1.11.1.6) catA - rice ORGANISM #formal_name Oryza sativa #common_name rice DATE 31-Dec-1992 #sequence_revision 02-Jun-2000 #text_change 16-Jun-2000 ACCESSIONS S70588; S20873; S19823 REFERENCE S70588 !$#authors Higo, K.; Higo, H. !$#journal Plant Mol. Biol. (1996) 30:505-521 !$#title Cloning and characterization of the rice CatA catalase gene, !1a homologue of the maize Cat3 gene. !$#cross-references MUID:96189265; PMID:8605302 !$#accession S70588 !'##status preliminary !'##molecule_type DNA !'##residues 1-491 ##label HIG !'##cross-references EMBL:D29966; NID:g1261857; PIDN:BAA06232.1; !1PID:g1261858 REFERENCE S20873 !$#authors Mori, H.; Higo, K.; Higo, H.; Minobe, Y.; Matsui, H.; Chiba, !1S. !$#journal Plant Mol. Biol. (1992) 18:973-976 !$#title Nucleotide and derived amino acid sequence of a catalase !1cDNA isolated from rice immature seeds. !$#cross-references MUID:92256818; PMID:1581574 !$#accession S20873 !'##molecule_type mRNA !'##residues 1-112,'Q',114-447,'AV',450-491 ##label MOR !'##cross-references EMBL:X61626; NID:g20191; PIDN:CAA43814.1; !1PID:g20192 GENETICS !$#gene cat A !$#introns 5/3; 272/3; 472/3 CLASSIFICATION #superfamily catalase KEYWORDS chromoprotein; heme; iron; metalloprotein; oxidoreductase FEATURE !$65,104,138 #active_site His, Ser, Asn #status predicted\ !$348 #binding_site heme iron (Tyr) (axial ligand) #status !8predicted SUMMARY #length 491 #molecular-weight 56646 #checksum 7027 SEQUENCE /// ENTRY CSSY #type complete TITLE catalase (EC 1.11.1.6) - soybean ORGANISM #formal_name Glycine max #common_name soybean DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 03-Mar-2000 ACCESSIONS S20999 REFERENCE S20999 !$#authors Allen, R. !$#submission submitted to the EMBL Data Library, May 1992 !$#accession S20999 !'##molecule_type DNA !'##residues 1-492 ##label ALL !'##cross-references EMBL:Z12021; NID:g18559; PIDN:CAA78056.1; !1PID:g18560 GENETICS !$#introns 5/3; 38/1; 389/3; 419/3; 442/2; 473/3 CLASSIFICATION #superfamily catalase KEYWORDS chromoprotein; heme; iron; metalloprotein; oxidoreductase FEATURE !$65,104,138 #active_site His, Ser, Asn #status predicted\ !$348 #binding_site heme iron (Tyr) (axial ligand) #status !8predicted SUMMARY #length 492 #molecular-weight 56847 #checksum 9929 SEQUENCE /// ENTRY CSPM #type complete TITLE catalase (EC 1.11.1.6) - garden pea ORGANISM #formal_name Pisum sativum #common_name garden pea DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 03-Mar-2000 ACCESSIONS S18346; S15559 REFERENCE S18346 !$#authors Isin, S.H.; Allen, R.D. !$#journal Plant Mol. Biol. (1991) 17:1263-1265 !$#title Isolation and characterization of a pea catalase cDNA. !$#cross-references MUID:92032793; PMID:1932700 !$#accession S18346 !'##molecule_type mRNA !'##residues 1-494 ##label ISI !'##cross-references EMBL:X60169; NID:g20676; PIDN:CAA42736.1; !1PID:g20677 CLASSIFICATION #superfamily catalase KEYWORDS chromoprotein; heme; iron; metalloprotein; oxidoreductase; !1peroxisome; tetramer FEATURE !$65,104,138 #active_site His, Ser, Asn #status predicted\ !$348 #binding_site heme iron (Tyr) (axial ligand) #status !8predicted SUMMARY #length 494 #molecular-weight 57344 #checksum 6516 SEQUENCE /// ENTRY CSBYT #type complete TITLE catalase (EC 1.11.1.6) T - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein G4628; protein YGR088w ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1988 #sequence_revision 19-Jul-1996 #text_change 21-Jul-2000 ACCESSIONS S64383; S64393; A26117; S48892 REFERENCE S64356 !$#authors Wedler, H.; Scharfe, M.; Wedler, E.; Wambutt, R. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64383 !'##molecule_type DNA !'##residues 1-573 ##label WED !'##cross-references EMBL:Z72873; NID:g1323128; PIDN:CAA97090.1; !1PID:g1323129; GSPDB:GN00007; MIPS:YGR088w !'##experimental_source strain S288C REFERENCE S64392 !$#authors Hernandez, K.; Weber, N.; Wipfli, P.; Schmidheini, T. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64393 !'##molecule_type DNA !'##residues 1-573 ##label HER !'##cross-references EMBL:Z72873; NID:g1323128; PIDN:CAA97090.1; !1PID:g1323129; GSPDB:GN00007; MIPS:YGR088w !'##experimental_source strain S288C REFERENCE A26117 !$#authors Hartig, A.; Ruis, H. !$#journal Eur. J. Biochem. (1986) 160:487-490 !$#title Nucleotide sequence of the Saccharomyces cerevisiae CTT1 !1gene and deduced amino-acid sequence of yeast catalase T. !$#cross-references MUID:87053966; PMID:3536508 !$#accession A26117 !'##molecule_type DNA !'##residues 12-439,'V',441-549,'G',551-573 ##label HAR !'##cross-references EMBL:X04625; NID:g3607; PIDN:CAA28298.1; PID:g3608 REFERENCE S48892 !$#authors Spevak, W.; Hartig, A.; Meindl, P.; Ruis, H. !$#journal Mol. Gen. Genet. (1986) 203:73-78 !$#title Heme control region of the catalase T gene of the yeast !1Saccharomyces cerevisiae. !$#cross-references MUID:86230135; PMID:2423850 !$#accession S48892 !'##molecule_type DNA !'##residues 1-74 ##label SPE !'##cross-references EMBL:M30256; NID:g171335; PIDN:AAA34540.1; !1PID:g553124 GENETICS !$#gene SGD:CTT1; MIPS:YGR088w !'##cross-references SGD:S0003320; MIPS:YGR088w !$#map_position 7R FUNCTION !$#description oxidoreductase CLASSIFICATION #superfamily catalase KEYWORDS chromoprotein; heme; iron; metalloprotein; oxidoreductase FEATURE !$75,114,148 #active_site His, Ser, Asn #status predicted\ !$362 #binding_site heme iron (Tyr) (axial ligand) #status !8predicted SUMMARY #length 573 #molecular-weight 65741 #checksum 350 SEQUENCE /// ENTRY CSCKPT #type complete TITLE catalase (EC 1.11.1.6), peroxisomal - yeast (Candida tropicalis) ORGANISM #formal_name Candida tropicalis DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 03-Mar-2000 ACCESSIONS A29629; S00231; S04086; S00461 REFERENCE A29629 !$#authors Murray, W.W.; Rachubinski, R.A. !$#journal Gene (1987) 61:401-413 !$#title The nucleotide sequence of complementary DNA and the deduced !1amino acid sequence of peroxisomal catalase of the yeast !1Candida tropicalis pK233. !$#cross-references MUID:88185842; PMID:3446581 !$#accession A29629 !'##molecule_type mRNA !'##residues 1-485 ##label MUR !'##cross-references GB:M18832; NID:g170830; PIDN:AAA34327.1; !1PID:g170831 !'##experimental_source strain pK233 REFERENCE S00231 !$#authors Okada, H.; Ueda, M.; Sugaya, T.; Atomi, H.; Mozaffar, S.; !1Hishida, T.; Teranishi, Y.; Okazaki, K.; Takechi, T.; !1Kamiryo, T.; Tanaka, A. !$#journal Eur. J. Biochem. (1987) 170:105-110 !$#title Catalase gene of the yeast Candida tropicalis. Sequence !1analysis and comparison with peroxisomal and cytosolic !1catalases from other sources. !$#cross-references MUID:88082804; PMID:3691514 !$#accession S00231 !'##molecule_type DNA !'##residues 1-165,'T',167-389,'I',391-485 ##label OKA !'##cross-references EMBL:X06660; NID:g2676; PIDN:CAA29859.1; PID:g2677 REFERENCE S04086 !$#authors Murray, W.W.; Rachubinski, R.A. !$#journal Nucleic Acids Res. (1989) 17:3600 !$#title Nucleotide sequence of peroxisomal catalase from the yeast !1Candida tropicalis pK233: identification of an upstream !1BamHI site polymorphism. !$#cross-references MUID:89263811; PMID:2726500 !$#accession S04086 !'##status translation not shown !'##molecule_type DNA !'##residues 1-165,'T',167-389,'I',391-485 ##label MUW !'##cross-references EMBL:X13978; NID:g2655; PIDN:CAA32159.1; PID:g2656 REFERENCE S00461 !$#authors Ueda, M.; Okada, H.; Hishida, T.; Teranishi, Y.; Tanaka, A. !$#journal FEBS Lett. (1987) 220:31-35 !$#title Isolation of several cDNAs encoding yeast peroxisomal !1enzymes. !$#cross-references MUID:87276567; PMID:2440725 !$#accession S00461 !'##molecule_type mRNA !'##residues 2-15,'X',17-18,'X',20,'XX',23-24;109-113;222-236;'NYFXA', !1118,'V';394-451 ##label UED !'##cross-references EMBL:X05886 !'##note part of this sequence, including the amino end of the mature !1protein, was determined by protein sequencing COMMENT This enzyme catalyzes the decomposition of hydrogen peroxide !1to oxygen and water; it is a trimer of identical !1hemin-containing chains. GENETICS !$#gene cat CLASSIFICATION #superfamily catalase KEYWORDS chromoprotein; heme; iron; metalloprotein; oxidoreductase; !1peroxisome FEATURE !$2-485 #product catalase #status experimental #label MAT\ !$53,92,126 #active_site His, Ser, Asn #status predicted\ !$336 #binding_site heme iron (Tyr) (axial ligand) #status !8predicted SUMMARY #length 485 #molecular-weight 54910 #checksum 7872 SEQUENCE /// ENTRY CSBYP #type complete TITLE catalase (EC 1.11.1.6), peroxisomal - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES catalase A; protein YD9302A.06c; protein YDR256c ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Jun-2000 ACCESSIONS S07868; S67313; S67459 REFERENCE S07868 !$#authors Cohen, G.; Rapatz, W.; Ruis, H. !$#journal Eur. J. Biochem. (1988) 176:159-163 !$#title Sequence of the Saccharomyces cerevisiae CTA1 gene and amino !1acid sequence of catalase A derived from it. !$#cross-references MUID:88329055; PMID:3046940 !$#accession S07868 !'##molecule_type DNA !'##residues 1-515 ##label COH !'##cross-references EMBL:X13028; NID:g3604; PIDN:CAA31443.1; PID:g3605 REFERENCE S61117 !$#authors Murphy, L.; Harris, D. !$#submission submitted to the EMBL Data Library, December 1995 !$#accession S67313 !'##molecule_type DNA !'##residues 1-515 ##label MUR !'##cross-references EMBL:Z68329; NID:g1136205; PIDN:CAA92713.1; !1PID:g1136211; MIPS:YDR256c REFERENCE S67454 !$#authors Murphy, L.; Harris, D. !$#submission submitted to the EMBL Data Library, March 1996 !$#accession S67459 !'##molecule_type DNA !'##residues 1-515 ##label MUW !'##cross-references EMBL:Z70202; NID:g1226026; PIDN:CAA94095.1; !1PID:g1226032; GSPDB:GN00004; MIPS:YDR256c GENETICS !$#gene SGD:CTA1; MIPS:YDR256c !'##cross-references SGD:S0002664; MIPS:YDR256c !$#map_position 4R CLASSIFICATION #superfamily catalase KEYWORDS chromoprotein; heme; iron; metalloprotein; oxidoreductase; !1peroxisome FEATURE !$70,109,143 #active_site His, Ser, Asn #status predicted\ !$355 #binding_site heme iron (Tyr) (axial ligand) #status !8predicted SUMMARY #length 515 #molecular-weight 58555 #checksum 1923 SEQUENCE /// ENTRY CSECHP #type complete TITLE catalase (EC 1.11.1.6) HPI - Escherichia coli (strain K-12) ALTERNATE_NAMES catalase-peroxidase; hydroperoxidase I CONTAINS peroxidase (EC 1.11.1.7) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1990 #sequence_revision 10-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS A65201; JS0140; S40885; I58303 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65201 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-726 ##label BLAT !'##cross-references GB:AE000468; GB:U00096; NID:g1790374; !1PIDN:AAC76924.1; PID:g1790378; UWGP:b3942 !'##experimental_source strain K-12, substrain MG1655 REFERENCE JS0140 !$#authors Triggs-Raine, B.L.; Doble, B.W.; Mulvey, M.R.; Sorby, P.A.; !1Loewen, P.C. !$#journal J. Bacteriol. (1988) 170:4415-4419 !$#title Nucleotide sequence of katG, encoding catalase HPI of !1Escherichia coli. !$#cross-references MUID:88314956; PMID:3045098 !$#accession JS0140 !'##molecule_type DNA !'##residues 1-510,'L',512-620,'G',622-726 ##label TRI !'##note parts of this sequence were confirmed by protein sequencing; !1the amino end of the mature protein is blocked !'##note the authors translated the codon CCG for residue 216 as Cys and !1GGC for residue 621 as Ala REFERENCE S40802 !$#authors Plunkett III, G.; Burland, V.; Daniels, D.L.; Blattner, F.R. !$#journal Nucleic Acids Res. (1993) 21:3391-3398 !$#title Analysis of the Escherichia coli genome. III. DNA sequence !1of the region from 87.2 to 89.2 minutes. !$#cross-references MUID:93347969; PMID:8346018 !$#accession S40885 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-339 ##label PLU !'##cross-references EMBL:L19201; NID:g304961; PIDN:AAB03074.1; !1PID:g305045 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1993 REFERENCE I58303 !$#authors Blattner, F.R.; Burland, V.; Plunkett III, G.; Sofia, H.J.; !1Daniels, D.L. !$#journal Nucleic Acids Res. (1993) 21:5408-5417 !$#title Analysis of the Escherichia coli genome. IV. DNA sequence of !1the region from 89.2 to 92.8 minutes. !$#cross-references MUID:94089392; PMID:8265357 !$#accession I58303 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 309-406,'X',408-726 ##label RES !'##cross-references EMBL:U00006; NID:g409785; PIDN:AAC43048.1; !1PID:g396289 COMMENT This catalase is not sensitive to 3-amino-1,2,4-triazole. GENETICS !$#gene katG !$#map_position 89.2 min COMPLEX homotetramer; two non-covalently associated iron protoheme !1IX groups per tetramer FUNCTION CAT !$#description as catalase, catalyzes the dismutation of two molecules of !1hydrogen peroxide to dioxygen and two molecules of water FUNCTION PER !$#description as peroxidase, uses hydrogen peroxide to oxidize donor !1compounds producing water !$#note active with a broad spectrum of donor compounds, including !1larger ones which cannot access the active site of typical !1catalases and peroxidases CLASSIFICATION #superfamily catalase HPI KEYWORDS blocked amino end; chromoprotein; heme; homotetramer; iron; !1metalloprotein; oxidoreductase FEATURE !$106 #active_site His (distal axial ligand) #status !8predicted\ !$267 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted\ !$318 #active_site Trp (tryptophyl radical intermediate) !8#status predicted SUMMARY #length 726 #molecular-weight 80023 #checksum 4514 SEQUENCE /// ENTRY CSEBHT #type complete TITLE catalase (EC 1.11.1.6) HPI - Salmonella typhimurium ALTERNATE_NAMES hydroperoxidase I ORGANISM #formal_name Salmonella typhimurium DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 03-Mar-2000 ACCESSIONS S12039; S11647 REFERENCE S12039 !$#authors Loewen, P.C.; Stauffer, G.V. !$#journal Mol. Gen. Genet. (1990) 224:147-151 !$#title Nucleotide sequence of katG of Salmonella typhimurium LT2 !1and characterization of its product, hydroperoxidase I. !$#cross-references MUID:91117169; PMID:2277629 !$#accession S12039 !'##molecule_type DNA !'##residues 1-727 ##label LOE1 !'##cross-references EMBL:X53001; NID:g47754; PIDN:CAA37187.1; !1PID:g47755 REFERENCE S11647 !$#authors Loewen, P.C.; Stauffer, G.V. !$#submission submitted to the EMBL Data Library, May 1990 !$#description Nucleotide sequence of katG of Salmonella typhimurium and !1characterization of its product, hydroperoxidase I. !$#accession S11647 !'##molecule_type DNA !'##residues 1-370,'XX',371-727 ##label LOE2 !'##cross-references EMBL:X53001 GENETICS !$#gene katG !$#map_position 88 min CLASSIFICATION #superfamily catalase HPI KEYWORDS chromoprotein; heme; iron; metalloprotein; oxidoreductase FEATURE !$107 #active_site His (distal axial ligand) #status !8predicted\ !$268 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted\ !$319 #active_site Trp (tryptophyl radical intermediate) !8#status predicted SUMMARY #length 727 #molecular-weight 80032 #checksum 411 SEQUENCE /// ENTRY JS0520 #type complete TITLE catalase (EC 1.11.1.6) HPI - Bacillus stearothermophilus ALTERNATE_NAMES catalase-peroxidase; hydroperoxidase I CONTAINS peroxidase (EC 1.11.1.7) ORGANISM #formal_name Bacillus stearothermophilus DATE 30-Sep-1991 #sequence_revision 08-Nov-1996 #text_change 03-Mar-2000 ACCESSIONS JS0520; A33955 REFERENCE JS0520 !$#authors Trakulnaleamsai, S.; Aihara, S.; Miyai, K.; Suga, Y.; Yomo, !1T.; Negoro, S.; Urabe, I. !$#submission submitted to JIPID, July 1991 !$#accession JS0520 !'##molecule_type DNA !'##residues 1-735 ##label TRA REFERENCE A33955 !$#authors Loprasert, S.; Negoro, S.; Okada, H. !$#journal J. Bacteriol. (1989) 171:4871-4875 !$#title Cloning, nucleotide sequence, and expression in Escherichia !1coli of the Bacillus stearothermophilus peroxidase gene !1(perA). !$#cross-references MUID:89359121; PMID:2670897 !$#accession A33955 !'##molecule_type DNA !'##residues 1-731 ##label LOP !'##note this sequence has been extensively revised in reference JS0520 GENETICS !$#gene perA COMPLEX homotetramer; two non-covalently associated iron protoheme !1IX groups per tetramer FUNCTION CAT !$#description as catalase, catalyzes the dismutation of two molecules of !1hydrogen peroxide to dioxygen and two molecules of water FUNCTION PER !$#description as peroxidase, uses hydrogen peroxide to oxidize donor !1compounds producing water !$#note active with a broad spectrum of donor compounds, including !1larger ones which cannot access the active site of typical !1catalases and peroxidases CLASSIFICATION #superfamily catalase HPI KEYWORDS chromoprotein; heme; homotetramer; iron; metalloprotein; !1oxidoreductase FEATURE !$101 #active_site His (distal axial ligand) #status !8predicted\ !$264 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted\ !$315 #active_site Trp (tryptophyl radical intermediate) !8#status predicted SUMMARY #length 735 #molecular-weight 82988 #checksum 5822 SEQUENCE /// ENTRY A40662 #type complete TITLE catalase (EC 1.11.1.6) HPI - Mycobacterium tuberculosis (strain H37Rv) ALTERNATE_NAMES catalase-peroxidase; hydroperoxidase I; katG catalase-peroxidase bifunctional enzyme CONTAINS peroxidase (EC 1.11.1.7) ORGANISM #formal_name Mycobacterium tuberculosis DATE 03-May-1994 #sequence_revision 24-Jul-1998 #text_change 16-Jun-2000 ACCESSIONS A70519; A40662; S29071; S34036 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession A70519 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-740 ##label COL !'##cross-references GB:Z97193; GB:AL123456; NID:g3261816; !1PIDN:CAB10056.1; PID:g2225952 !'##experimental_source strain H37Rv REFERENCE A40662 !$#authors Heym, B.; Zhang, Y.; Poulet, S.; Young, D.; Cole, S.T. !$#journal J. Bacteriol. (1993) 175:4255-4259 !$#title Characterization of the katG gene encoding a !1catalase-peroxidase required for the isoniazid !1susceptibility of Mycobacterium tuberculosis. !$#cross-references MUID:93308108; PMID:8320241 !$#accession A40662 !'##molecule_type DNA !'##residues 1-70,'SRL',74-170,'RCARNRWASRRSGSASG',188-192,'T',194-207, !1'DG',210-211,'VS',215-233,'A',235-408,'R',410-446,'TTSSAK', !1'Q',455-512,'SAQGHSHP',522-528,'TRR',534-550,'PL',553-570, !1'PH',573-602,'RCRPSTS',610-711,'APMTR',717,'A',719-721,'TG', !1724-740 ##label HEY !'##cross-references EMBL:X68081; GB:S42739; NID:g581367 REFERENCE S29071 !$#authors Zhang, Y.; Heym, B.; Allen, B.; Young, D.; Cole, S. !$#journal Nature (1992) 358:591-593 !$#title The catalase-peroxidase gene and isoniazid resistance of !1Mycobacterium tuberculosis. !$#cross-references MUID:92365822; PMID:1501713 !$#accession S29071 !'##molecule_type DNA !'##residues 1-70,'SRL',74-80 ##label ZHA !'##cross-references EMBL:X68081 GENETICS !$#gene katG !$#start_codon GTG COMPLEX homotetramer; two non-covalently associated iron protoheme !1IX groups per tetramer FUNCTION CAT !$#description as catalase, catalyzes the dismutation of two molecules of !1hydrogen peroxide to dioxygen and two molecules of water FUNCTION PER !$#description as peroxidase, uses hydrogen peroxide to oxidize donor !1compounds producing water !$#note active with a broad spectrum of donor compounds, including !1larger ones which cannot access the active site of typical !1catalases and peroxidases CLASSIFICATION #superfamily catalase HPI KEYWORDS chromoprotein; heme; homotetramer; iron; metalloprotein; !1oxidoreductase FEATURE !$108 #active_site His (distal axial ligand) #status !8predicted\ !$270 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted\ !$321 #active_site Trp (tryptophyl radical intermediate) !8#status predicted SUMMARY #length 740 #molecular-weight 80604 #checksum 8213 SEQUENCE /// ENTRY A47685 #type complete TITLE catalase (EC 1.11.1.6) HPI - Mycobacterium intracellulare ALTERNATE_NAMES catalase-peroxidase; hydroperoxidase I; MI85 CONTAINS peroxidase (EC 1.11.1.7) ORGANISM #formal_name Mycobacterium intracellulare DATE 19-Dec-1993 #sequence_revision 08-Nov-1996 #text_change 03-Mar-2000 ACCESSIONS A47685 REFERENCE A47685 !$#authors Morris, S.L.; Nair, J.; Rouse, D.A. !$#journal J. Gen. Microbiol. (1992) 138:2363-2370 !$#title The catalase-peroxidase of Mycobacterium intracellulare: !1nucleotide sequence analysis and expression in Escherichia !1coli. !$#cross-references MUID:93123988; PMID:1336034 !$#contents 13950 !$#accession A47685 !'##molecule_type DNA !'##residues 1-746 ##label MOR !'##cross-references GB:M86741; NID:g149937; PIDN:AAA25360.1; !1PID:g149938 !'##note sequence extracted from NCBI backbone (NCBIN:122093, !1NCBIP:122096) GENETICS !$#gene katG COMPLEX homotetramer; two non-covalently associated iron protoheme !1IX groups per tetramer FUNCTION CAT !$#description as catalase, catalyzes the dismutation of two molecules of !1hydrogen peroxide to dioxygen and two molecules of water FUNCTION PER !$#description as peroxidase, uses hydrogen peroxide to oxidize donor !1compounds producing water !$#note active with a broad spectrum of donor compounds, including !1larger ones which cannot access the active site of typical !1catalases and peroxidases CLASSIFICATION #superfamily catalase HPI KEYWORDS chromoprotein; heme; homotetramer; iron; metalloprotein; !1oxidoreductase FEATURE !$114 #active_site His (distal axial ligand) #status !8predicted\ !$277 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted\ !$328 #active_site Trp (tryptophyl radical intermediate) !8#status predicted SUMMARY #length 746 #molecular-weight 81385 #checksum 3493 SEQUENCE /// ENTRY OPRHC #type complete TITLE peroxidase (EC 1.11.1.7) C1A precursor - horseradish ORGANISM #formal_name Armoracia rusticana #common_name horseradish DATE 24-Apr-1984 #sequence_revision 12-Apr-1996 #text_change 01-Dec-2000 ACCESSIONS S00625; S32972; A00502; PC7025 REFERENCE S00625 !$#authors Fujiyama, K.; Takemura, H.; Shibayama, S.; Kobayashi, K.; !1Choi, J.K.; Shinmyo, A.; Takano, M.; Yamada, Y.; Okada, H. !$#journal Eur. J. Biochem. (1988) 173:681-687 !$#title Structure of the horseradish peroxidase isozyme C genes. !$#cross-references MUID:88225087; PMID:3371352 !$#accession S00625 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-353 ##label FUJ REFERENCE S32972 !$#authors Welinder, K.G. !$#journal Eur. J. Biochem. (1979) 96:483-502 !$#title Amino acid sequence studies of horseradish peroxidase. Amino !1and carboxyl termini, cyanogen bromide and tryptic !1fragments, the complete sequence, and some structural !1characteristics of horseradish peroxidase C. !$#cross-references MUID:79236311; PMID:38113 !$#accession S32972 !'##molecule_type protein !'##residues 31-338 ##label WEL REFERENCE A00502 !$#authors Welinder, K.G. !$#journal FEBS Lett. (1976) 72:19-23 !$#title Covalent structure of the glycoprotein horseradish !1peroxidase (EC 1.11.1.7). !$#cross-references MUID:77068850; PMID:1001465 !$#accession A00502 !'##molecule_type protein !'##residues 31-338 ##label WE2 REFERENCE PC7025 !$#authors Gazaryan, I.G.; Chubar, T.A.; Ignatenko, O.V.; Mareeva, !1E.A.; Orlova, M.A.; Kapeliuch, Y.L.; Savitsky, P.A.; !1Rojkova, A.M.; Tishkov, V.I. !$#journal Biochem. Biophys. Res. Commun. (1999) 262:297-301 !$#title Tryptophanless recombinant horseradish peroxidase: Stability !1and catalytic properties. !$#cross-references MUID:99382281; PMID:10448108 !$#accession PC7025 !'##molecule_type DNA !'##residues 31-338 ##label GAZ GENETICS !$#gene prxC1; w117f CLASSIFICATION #superfamily peroxidase KEYWORDS chromoprotein; glycoprotein; heme; iron; metalloprotein; !1oxidoreductase; pyroglutamic acid FEATURE !$1-30 #domain signal sequence #status predicted #label SIG\ !$31-338 #product peroxidase C1 #status experimental #label !8MAT\ !$31 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$41-121,74-79, !$127-331,207-239 #disulfide_bonds #status experimental\ !$43,87,188,216,228, !$244,285,298 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$68 #active_site Arg #status predicted\ !$72,200 #binding_site heme iron (His) (axial ligands) #status !8predicted SUMMARY #length 353 #molecular-weight 38825 #checksum 3471 SEQUENCE /// ENTRY OPNB7 #type complete TITLE peroxidase (EC 1.11.1.7) - turnip ALTERNATE_NAMES hydrogen peroxide oxidoreductase; peroxidase 7 ORGANISM #formal_name Brassica rapa #common_name turnip DATE 31-Oct-1980 #sequence_revision 23-Oct-1981 #text_change 03-Mar-2000 ACCESSIONS A91094; A91246; B23116; PN0612; A00503 REFERENCE A91094 !$#authors Mazza, G.; Welinder, K.G. !$#journal Eur. J. Biochem. (1980) 108:481-489 !$#title Covalent structure of turnip peroxidase 7. Cyanogen bromide !1fragments, complete structure and comparison to horseradish !1peroxidase C. !$#cross-references MUID:81003872; PMID:7408864 !$#accession A91094 !'##molecule_type protein !'##residues 1-296 ##label MAZ !'##experimental_source cv. Blanc dur d'hiver !'##note the protein shown, TP7, is the principal isoperoxidase during !1winter in turnip REFERENCE A91246 !$#authors Welinder, K.G.; Mazza, G. !$#journal Eur. J. Biochem. (1977) 73:353-358 !$#title Amino-acid sequences of heme-linked, histidine-containing !1peptides of five peroxidases from horseradish and turnip. !$#cross-references MUID:77138218; PMID:849740 !$#accession A91246 !'##molecule_type protein !'##residues 32-65;161-175 ##label WEL !'##note these two histidine-containing tryptic peptides are essential !1to the peroxidase activity of the hemoprotein REFERENCE A23116 !$#authors Welinder, K.G. !$#journal Eur. J. Biochem. (1985) 151:497-504 !$#title Plant peroxidases: their primary, secondary and tertiary !1structures, and relation to cytochrome c peroxidase. !$#cross-references MUID:85285060; PMID:2992968 !$#accession B23116 !'##status preliminary !'##molecule_type protein !'##residues 'Z',2-296 ##label WE2 REFERENCE PN0612 !$#authors Diehn, S.H.; Burkhart, W.; Graham, J.S. !$#journal Biochem. Biophys. Res. Commun. (1993) 195:928-934 !$#title Purification and partial amino acid sequence of !1wound-inducible, developmentally regulated anionic !1peroxidase from soybean leaves. !$#cross-references MUID:93384622; PMID:8396932 !$#accession PN0612 !'##molecule_type protein !'##residues 'Z',2-32,'AG',35-88,'D',90-156,'K',158-296 ##label DIE CLASSIFICATION #superfamily peroxidase KEYWORDS chromoprotein; glycoprotein; heme; iron; metalloprotein; !1oxidoreductase; pyroglutamic acid FEATURE !$1 #modified_site pyrrolidone carboxylic acid (Gln) !8#status experimental\ !$11-91,44-49,97-292, !$176-201 #disulfide_bonds #status experimental\ !$38 #active_site Arg #status predicted\ !$42,169 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$185 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 296 #molecular-weight 31086 #checksum 516 SEQUENCE /// ENTRY OPHUM #type complete TITLE myeloperoxidase (EC 1.11.1.7) precursor - human ALTERNATE_NAMES MPO; peroxidase ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1988 #sequence_revision 10-May-1996 #text_change 01-Dec-2000 ACCESSIONS A29467; A28894; S06069; A93657; A92631; A90079; A34650; !1A60797; A45058; I56996; A26551; A26568; A27269 REFERENCE A29467 !$#authors Morishita, K.; Tsuchiya, M.; Asano, S.; Kaziro, Y.; Nagata, !1S. !$#journal J. Biol. Chem. (1987) 262:15208-15213 !$#title Chromosomal gene structure of human myeloperoxidase and !1regulation of its expression by granulocyte !1colony-stimulating factor. !$#cross-references MUID:88033106; PMID:2444596 !$#accession A29467 !'##molecule_type DNA !'##residues 1-745 ##label MOR !'##cross-references GB:M17176; GB:J03456; NID:g188665; PIDN:AAA60346.1; !1PID:g386956 REFERENCE A90533 !$#authors Hashinaka, K.; Nishio, C.; Hur, S.J.; Sakiyama, F.; !1Tsunasawa, S.; Yamada, M. !$#journal Biochemistry (1988) 27:5906-5914 !$#title Multiple species of myeloperoxidase messenger RNAs produced !1by alternative splicing and differential polyadenylation. !$#cross-references MUID:89050930; PMID:2903767 !$#accession A28894 !'##molecule_type mRNA !'##residues 1-745 ##label HAS !'##cross-references GB:M19507; NID:g188657; PIDN:AAA59863.1; !1PID:g188658 !'##experimental_source clone H17 REFERENCE S06069 !$#authors Johnson, K.; Gemperlein, I.; Hudson, S.; Shane, S.; Rovera, !1G. !$#journal Nucleic Acids Res. (1989) 17:7985-7986 !$#title Complete nucleotide sequence of the human myeloperoxidase !1gene. !$#cross-references MUID:90016883; PMID:2552418 !$#accession S06069 !'##status translation not shown !'##molecule_type DNA !'##residues 1-35,'V',37-745 ##label JOH1 !'##cross-references EMBL:X15377; NID:g34718; PIDN:CAA33438.1; !1PID:g34719 REFERENCE A93657 !$#authors Johnson, K.R.; Nauseef, W.M.; Care, A.; Wheelock, M.J.; !1Shane, S.; Hudson, S.; Koeffler, H.P.; Selsted, M.; Miller, !1C.; Rovera, G. !$#journal Nucleic Acids Res. (1987) 15:2013-2028 !$#title Characterization of cDNA clones for human myeloperoxidase: !1predicted amino acid sequence and evidence for multiple mRNA !1species. !$#cross-references MUID:87174733; PMID:3031585 !$#accession A93657 !'##molecule_type mRNA !'##residues 1-35,'V',37-745 ##label JOH2 !'##cross-references GB:X04876; NID:g34720; PIDN:CAA28565.1; PID:g34722 REFERENCE A92631 !$#authors Morishita, K.; Kubota, N.; Asano, S.; Kaziro, Y.; Nagata, S. !$#journal J. Biol. Chem. (1987) 262:3844-3851 !$#title Molecular cloning and characterization of cDNA for human !1myeloperoxidase. !$#cross-references MUID:87137693; PMID:3029127 !$#accession A92631 !'##molecule_type mRNA !'##residues 1-745 ##label MO2 !'##cross-references GB:J02694; NID:g189039; PIDN:AAA59896.1; !1PID:g189040 !'##note the authors translated the codon ACC for residues 710 and 711 !1as Trp REFERENCE A90079 !$#authors Yamada, M.; Hur, S.J.; Hashinaka, K.; Tsuneoka, K.; Saeki, !1T.; Nishio, C.; Sakiyama, F.; Tsunasawa, S. !$#journal Arch. Biochem. Biophys. (1987) 255:147-155 !$#title Isolation and characterization of a cDNA coding for human !1myeloperoxidase. !$#cross-references MUID:87240181; PMID:2884926 !$#accession A90079 !'##molecule_type mRNA !'##residues 588-745 ##label YAM REFERENCE A34650 !$#authors Yamada, M.; Hur, S.J.; Toda, H. !$#journal Biochem. Biophys. Res. Commun. (1990) 166:852-859 !$#title Isolation and characterization of extracellular !1myeloperoxidase precursor in HL-60 cell cultures. !$#cross-references MUID:90147798; PMID:2154223 !$#accession A34650 !'##molecule_type protein !'##residues 49-59,'X',61-66,'XX' ##label YA2 REFERENCE A60797 !$#authors Chang, K.S.; Trujillo, J.M.; Cook, R.G.; Stass, S.A. !$#journal Blood (1986) 68:1411-1414 !$#title Human myeloperoxidase gene: molecular cloning and expression !1in leukemic cells. !$#cross-references MUID:87050063; PMID:3022847 !$#accession A60797 !'##status preliminary !'##molecule_type protein !'##residues 279-308 ##label CHA REFERENCE A45058 !$#authors Taylor, K.L.; Pohl, J.; Kinkade Jr., J.M. !$#journal J. Biol. Chem. (1992) 267:25282-25288 !$#title Unique autolytic cleavage of human myeloperoxidase. !1Implications for the involvement of active site MET409. !$#cross-references MUID:93094240; PMID:1334087 !$#accession A45058 !'##molecule_type protein !'##residues 410-424 ##label TAY !'##note sequence extracted from NCBI backbone (NCBIP:120481) REFERENCE I56996 !$#authors Hosokawa, Y.; Kawaguchi, R.; Hikiji, K.; Yamada, M.; Suzuki, !1K.; Nakagawa, T.; Yoshihara, T.; Yamaguchi, K. !$#journal Leukemia (1993) 7:441-445 !$#title Cloning and characterization of four types of cDNA encoding !1myeloperoxidase from human monocytic leukemia cell line, !1SKM-1. !$#cross-references MUID:93188543; PMID:8383257 !$#accession I56996 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-745 ##label RES !'##cross-references GB:S56200; NID:g266269; PIDN:AAB25582.1; !1PID:g266270 COMMENT This enzyme is a heme-containing glycoprotein found in the !1azurophilic granules (or primary lysosomes) of human !1polymorphonuclear leukocytes. In the presence of hydrogen !1peroxide and the chloride ions in the extracellular matrix, !1myeloperoxidase catalyzes the production of the potent !1microbicidal agent hypochlorous acid. COMMENT The enzyme from human mature granulocytes exists as a !1tetramer of two heavy and two light chains. The enzyme from !1human leukemia cells, however, contains one heavy and one !1light chain, which are both generated from the same !1precursor by a series of proteolytic cleavages. COMMENT The nature of the heme derivative and its covalent !1attachment to glutamate have not been completely !1characterized. GENETICS !$#gene GDB:MPO !'##cross-references GDB:120192; OMIM:254600 !$#map_position 17q23.1-17q23.1 !$#introns 52/1; 83/2; 142/1; 183/2; 226/3; 295/3; 402/1; 455/3; 541/1; !1598/1; 677/2 CLASSIFICATION #superfamily myeloperoxidase; myeloperoxidase homology KEYWORDS alternative splicing; chromoprotein; glycoprotein; heme; !1iron; metalloprotein; oxidoreductase FEATURE !$1-48 #domain signal sequence #status predicted #label SIG\ !$49-164 #domain propeptide #status predicted #label PRO\ !$62-741 #domain myeloperoxidase homology #label MPX\ !$165-272 #product myeloperoxidase light chain precursor !8#status predicted #label LGT\ !$279-745 #product myeloperoxidase heavy chain #status !8predicted #label HVY\ !$139,323 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$167-180,281-291, !$285-309,387-398, !$606-663,704-730 #disulfide_bonds #status predicted\ !$260,408,409 #binding_site hemediol (Asp, Glu, Met) (covalent) !8#status experimental\ !$261 #active_site His (distal axial ligand) #status !8predicted\ !$319 #disulfide_bonds interchain #status predicted\ !$355,391,483 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$405 #active_site Arg #status predicted\ !$502 #binding_site hemediol iron (His) (proximal axial !8ligand) #status experimental SUMMARY #length 745 #molecular-weight 83868 #checksum 1963 SEQUENCE /// ENTRY A35828 #type complete TITLE peroxidase (EC 1.11.1.7) precursor - bovine ALTERNATE_NAMES lactoperoxidase ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Nov-2000 ACCESSIONS A35828; S16103 REFERENCE A35828 !$#authors Dull, T.J.; Uyeda, C.; Strosberg, A.D.; Nedwin, G.; !1Seilhamer, J.J. !$#journal DNA Cell Biol. (1990) 9:499-509 !$#title Molecular cloning of cDNAs encoding bovine and human !1lactoperoxidase. !$#cross-references MUID:91025552; PMID:2222811 !$#accession A35828 !'##molecule_type mRNA !'##residues 1-712 ##label DUL !'##cross-references GB:M58150; NID:g163306; PIDN:AAA62714.1; !1PID:g163307 REFERENCE S16103 !$#authors Cals, M.M.; Mailliart, P.; Brignon, G.; Anglade, P.; Dumas, !1B.R. !$#journal Eur. J. Biochem. (1991) 198:733-739 !$#title Primary structure of bovine lactoperoxidase, a fourth member !1of a mammalian heme peroxidase family. !$#cross-references MUID:91266958; PMID:2050150 !$#accession S16103 !'##molecule_type protein !'##residues 101-108,'B',110-448,'R',450-712 ##label CAL CLASSIFICATION #superfamily myeloperoxidase; myeloperoxidase homology KEYWORDS chromoprotein; glycoprotein; heme; iron; metalloprotein; !1oxidoreductase FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-100 #domain propeptide #status predicted #label PRO\ !$34-707 #domain myeloperoxidase homology #label MPX\ !$101-712 #product peroxidase #status experimental #label MAT\ !$106,212,322,358,449 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$132-145,246-256, !$250-274,354-365, !$573-630,671-696 #disulfide_bonds #status predicted\ !$225,375 #binding_site hemediol (Asp, Glu) (covalent) #status !8predicted\ !$226 #active_site His (distal axial ligand) #status !8predicted\ !$372 #active_site Arg #status predicted\ !$468 #binding_site hemediol iron (His) (proximal axial !8ligand) #status predicted SUMMARY #length 712 #molecular-weight 80642 #checksum 3690 SEQUENCE /// ENTRY OPHUIT #type complete TITLE iodide peroxidase (EC 1.11.1.8) precursor, thyroid - human ALTERNATE_NAMES thyroid microsomal antigen; thyroid peroxidase; thyroperoxidase CONTAINS iodide peroxidase, splice form 2 ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1992 #sequence_revision 05-Nov-1999 #text_change 20-Oct-2000 ACCESSIONS A32413; A27787; A40065; A28574; S06288; I38347; S08221; !1A35415; T01792; T01793 REFERENCE A32413 !$#authors Kimura, S.; Hong, Y.S.; Kotani, T.; Ohtaki, S.; Kikkawa, F. !$#journal Biochemistry (1989) 28:4481-4489 !$#title Structure of the human thyroid peroxidase gene: comparison !1and relationship to the human myeloperoxidase gene. !$#cross-references MUID:89352509; PMID:2548579 !$#accession A32413 !'##molecule_type DNA !'##residues 1-933 ##label KIM1 !'##cross-references GB:M25715; GB:J02856; NID:g339863; PIDN:AAA97517.1; !1PID:g339865 !'##note the authors translated the codon ACT for residue 725 as Pro and !1GTG for residue 847 as Ala REFERENCE A27787 !$#authors Kimura, S.; Kotani, T.; McBride, O.W.; Umeki, K.; Hirai, K.; !1Nakayama, T.; Ohtaki, S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:5555-5559 !$#title Human thyroid peroxidase: complete cDNA and protein !1sequence, chromosome mapping, and identification of two !1alternately spliced mRNAs. !$#cross-references MUID:87289643; PMID:3475693 !$#accession A27787 !'##molecule_type mRNA !'##residues 1-370,'R',372-724,'P',726-846,'A',848-933 ##label KIM2 !'##cross-references GB:J02969; NID:g339866; PIDN:AAA61215.1; !1PID:g339867; GB:J02970 REFERENCE A40065 !$#authors Magnusson, R.P.; Chazenbalk, G.D.; Gestautas, J.; Seto, P.; !1Filetti, S.; DeGroot, L.J.; Rapoport, B. !$#journal Mol. Endocrinol. (1987) 1:856-861 !$#title Molecular cloning of the complementary deoxyribonucleic acid !1for human thyroid peroxidase. !$#cross-references MUID:91042572; PMID:3153466 !$#accession A40065 !'##molecule_type mRNA !'##residues 1-69,'G',71-256,'S',258-353,'G',355-380,'N',382-933 ##label !1MAG !'##cross-references GB:M17755; NID:g4680720; PIDN:AAA61217.2; !1PID:g4680721 REFERENCE A28574 !$#authors Seto, P.; Hirayu, H.; Magnusson, R.P.; Gestautas, J.; !1Portmann, L.; DeGroot, L.J.; Rapoport, B. !$#journal J. Clin. Invest. (1987) 80:1205-1208 !$#title Isolation of a complementary DNA clone for thyroid !1microsomal antigen. Homology with the gene for thyroid !1peroxidase. !$#cross-references MUID:88008367; PMID:3654979 !$#accession A28574 !'##molecule_type mRNA !'##residues 217-256,'S',258-353,'G',355-380,'N',382-496 ##label SET !'##cross-references GB:M17755; NID:g339872; PIDN:AAA61217.1; !1PID:g339873 REFERENCE S06288 !$#authors Libert, F.; Ruel, J.; Ludgate, M.; Swillens, S.; Alexander, !1N.; Vassart, G.; Dinsart, C. !$#journal EMBO J. (1987) 6:4193-4196 !$#title Thyroperoxidase, an auto-antigen with a mosaic structure !1made of nuclear and mitochondrial gene modules. !$#cross-references MUID:88166664; PMID:3443105 !$#accession S06288 !'##molecule_type mRNA !'##residues 1-573,'N',575-724,'P',726-747,'M',749-846,'A',848-871,'K', !1873-933 ##label LIB1 REFERENCE I38347 !$#authors Libert, F.; Ruel, J.; Ludgate, M.; Swillens, S.; Alexander, !1N.; Vassart, G.; Dinsart, C. !$#journal Nucleic Acids Res. (1987) 15:6735 !$#title Complete nucleotide sequence of the human !1thyroperoxidase-microsomal antigen cDNA. !$#cross-references MUID:87316933; PMID:3453124 !$#accession I38347 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-573,'N',575-724,'P',726-747,'M',749-846,'A',848-871,'K', !1873-933 ##label LIB2 !'##cross-references EMBL:Y00406; NID:g37250; PIDN:CAA68467.1; !1PID:g37251 REFERENCE S08221 !$#authors Barnett, P.S.; Banga, J.P.; Watkins, J.; Huang, G.C.; !1Gluckman, D.R.B.; Page, M.J.; McGregor, A.M. !$#journal Nucleic Acids Res. (1990) 18:670 !$#title Nucleotide sequence of the alternatively spliced human !1thyroid peroxidase cDNA, TPO-2. !$#cross-references MUID:90175008; PMID:2308857 !$#accession S08221 !'##molecule_type mRNA !'##residues 1-372,'S',374-397,'T',399-533,591-933 ##label BAR !'##cross-references EMBL:X17358; NID:g28897; PIDN:CAA35235.1; !1PID:g28898 REFERENCE A35415 !$#authors Zanelli, E.; Henry, M.; Charvet, B.; Malthiery, Y. !$#journal Biochem. Biophys. Res. Commun. (1990) 170:735-741 !$#title Evidence for an alternate splicing in the thyroperoxidase !1messenger from patients with Graves' disease. !$#cross-references MUID:90343792; PMID:2383265 !$#accession A35415 !'##status preliminary !'##molecule_type mRNA !'##residues 670-873, !1'RVLGWKAGILTGCREPSEGKVAGHCRTASCSQNHRTTLFQTQANRKSAGRLFSQHG' !1##label ZAN !'##cross-references GB:M55702; NID:g339874; PIDN:AAA61219.1; !1PID:g339875 !'##note mutant splice form from patient with Graves' disease COMMENT This protein is also described by the less specific !1designation peroxidase (EC 1.11.1.7). GENETICS !$#gene GDB:TPO !'##cross-references GDB:120446; OMIM:274500 !$#map_position 2p25-2p24 !$#introns 32/1; 60/2; 117/1; 161/2; 204/3; 273/3; 446/3; 446/3; 553/1; !1590/1; 669/2; 739/1; 796/1; 840/1; 873/2; 916/3 FUNCTION !$#description catalyzes the oxidation by hydrogen peroxide of a tyrosine !1residue and iodide to produce an iodinated tyrosine residue, !1an hydroxyl ion and water CLASSIFICATION #superfamily thyroid peroxidase; complement factor H repeat !1homology; EGF homology; myeloperoxidase homology KEYWORDS alternative splicing; chromoprotein; glycoprotein; heme; !1iron; metalloprotein; oxidoreductase; thyroid gland; thyroid !1hormone biosynthesis; transmembrane protein FEATURE !$1-14 #domain signal sequence #status predicted #label SIG\ !$15-933 #product iodide peroxidase #status predicted #label !8MAT1\ !$15-533,591-933 #product iodide peroxidase, splice form 2 #status !8predicted #label MAT2\ !$39-732 #domain myeloperoxidase homology #label MPX\ !$742-794 #domain complement factor H repeat homology #label !8FHR\ !$800-838 #domain EGF homology #label EGF\ !$854-871 #domain transmembrane #status predicted #label TMM\ !$129,307,342,569 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$142-158,259-269, !$263-286,375-389, !$598-655,696-721 #disulfide_bonds #status predicted\ !$238,399 #binding_site hemediol (Asp, Glu) (covalent) #status !8predicted\ !$239 #active_site His (distal axial ligand) #status !8predicted\ !$240,321,323,325,327 #binding_site calcium (Asp, Thr, Phe, Asp, Ser) !8#status predicted\ !$396 #active_site Arg #status predicted\ !$494 #binding_site hemediol iron (His) (proximal axial !8ligand) #status predicted SUMMARY #length 933 #molecular-weight 102962 #checksum 869 SEQUENCE /// ENTRY OPPGIT #type complete TITLE iodide peroxidase (EC 1.11.1.8) precursor, thyroid - pig ALTERNATE_NAMES thyroid peroxidase ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 01-Dec-2000 ACCESSIONS A27416; A24632; S29051 REFERENCE A27416 !$#authors Magnusson, R.P.; Gestautas, J.; Taurog, A.; Rapoport, B. !$#journal J. Biol. Chem. (1987) 262:13885-13888 !$#title Molecular cloning of the structural gene for porcine thyroid !1peroxidase. !$#cross-references MUID:88007624; PMID:3654642 !$#accession A27416 !'##molecule_type mRNA !'##residues 1-926 ##label MAG !'##cross-references GB:J03463 REFERENCE A24632 !$#authors Magnusson, R.P.; Gestautas, J.; Seto, P.; Taurog, A.; !1Rapoport, B. !$#journal FEBS Lett. (1986) 208:391-396 !$#title Isolation and characterization of a cDNA clone for porcine !1thyroid peroxidase. !$#cross-references MUID:87054611; PMID:3780975 !$#accession A24632 !'##molecule_type mRNA !'##residues 595-926 ##label MA2 !'##cross-references GB:X04645; GB:J03463; NID:g2141; PIDN:CAA28306.1; !1PID:g2142 REFERENCE S29051 !$#authors Rawitch, A.B.; Pollock, G.; Yang, S.X.; Taurog, A. !$#journal Arch. Biochem. Biophys. (1992) 297:321-327 !$#title Thyroid peroxidase glycosylation: the location and nature of !1the N-linked oligosaccharide units in porcine thyroid !1peroxidase. !$#cross-references MUID:92359545; PMID:1497352 !$#accession S29051 !'##molecule_type protein !'##residues 110-115;267-274;301-308;340-351 ##label RAW CLASSIFICATION #superfamily thyroid peroxidase; complement factor H repeat !1homology; EGF homology; myeloperoxidase homology KEYWORDS chromoprotein; glycoprotein; heme; iron; metalloprotein; !1oxidoreductase; thyroid gland; thyroid hormone biosynthesis; !1transmembrane protein FEATURE !$1-14 #domain signal sequence #status predicted #label SIG\ !$15-926 #product iodide peroxidase #status predicted #label !8MAT\ !$39-730 #domain myeloperoxidase homology #label MPX\ !$740-792 #domain complement factor H repeat homology #label !8FHR\ !$798-836 #domain EGF homology #label EGF\ !$852-869 #domain transmembrane #status predicted #label TMM\ !$129,277,307,342 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$142-158,259-269, !$263-286,375-388, !$596-653,694-719 #disulfide_bonds #status predicted\ !$238,398 #binding_site hemediol (Asp, Glu) (covalent) #status !8predicted\ !$239 #active_site His (distal axial ligand) #status !8predicted\ !$240,321,323,325,327 #binding_site calcium (Asp, Thr, Phe, Asp, Ser) !8#status predicted\ !$395 #active_site Arg #status predicted\ !$493 #binding_site hemediol iron (His) (proximal axial !8ligand) #status predicted SUMMARY #length 926 #molecular-weight 100442 #checksum 2698 SEQUENCE /// ENTRY JN0550 #type complete TITLE iodide peroxidase (EC 1.11.1.8) precursor, thyroid - mouse ALTERNATE_NAMES thyroid myeloperoxidase [misnomer] ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS JN0550 REFERENCE JN0550 !$#authors Kotani, T.; Umeki, K.; Yamamoto, I.; Takeuchi, M.; Takechi, !1S.; Nakayama, T.; Ohtaki, S. !$#journal Gene (1993) 123:289-290 !$#title Nucleotide sequence of the cDNA encoding mouse thyroid !1peroxidase. !$#cross-references MUID:93154601; PMID:7916704 !$#accession JN0550 !'##molecule_type mRNA !'##residues 1-914 ##label KOT !'##cross-references EMBL:X60703; NID:g297160; PIDN:CAA43114.1; !1PID:g4539541 COMMENT This protein is a key enzyme in thyroid hormone synthesis. GENETICS !$#gene TPO CLASSIFICATION #superfamily thyroid peroxidase; complement factor H repeat !1homology; EGF homology; myeloperoxidase homology KEYWORDS chromoprotein; glycoprotein; heme; iron; metalloprotein; !1oxidoreductase; transmembrane protein FEATURE !$36-717 #domain myeloperoxidase homology #label MPX\ !$730-782 #domain complement factor H repeat homology #label !8FHR\ !$788-826 #domain EGF homology #label EGF\ !$123,271,299,334,603 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$136-152,253-263, !$257-278,363-377, !$586-643,684-709 #disulfide_bonds #status predicted\ !$232,387 #binding_site hemediol (Asp, Glu) (covalent) #status !8predicted\ !$233 #active_site His (distal axial ligand) #status !8predicted\ !$234,313,315,317,319 #binding_site calcium (Asp, Thr, Phe, Asp, Ser) !8#status predicted\ !$384 #active_site Arg #status predicted\ !$482 #binding_site hemediol iron (His) (proximal axial !8ligand) #status predicted SUMMARY #length 914 #molecular-weight 101342 #checksum 9914 SEQUENCE /// ENTRY S07047 #type complete TITLE iodide peroxidase (EC 1.11.1.8), thyroid - rat ALTERNATE_NAMES thyroid peroxidase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS S07047; A41408 REFERENCE S07047 !$#authors Derwahl, M.; Seto, P.; Rapoport, B. !$#journal Nucleic Acids Res. (1989) 17:8380 !$#title Complete nucleotide sequence of the cDNA for thyroid !1peroxidase in FRTL5 rat thyroid cells. !$#cross-references MUID:90045972; PMID:2813071 !$#accession S07047 !'##molecule_type mRNA !'##residues 1-914 ##label DER !'##cross-references EMBL:X17396; NID:g57382; PIDN:CAA35257.1; !1PID:g57383 REFERENCE A41408 !$#authors Isozaki, O.; Kohn, L.D.; Kozak, C.A.; Kimura, S. !$#journal Mol. Endocrinol. (1989) 3:1681-1692 !$#title Thyroid peroxidase: rat cDNA sequence, chromosomal !1localization in mouse, and regulation of gene expression by !1comparison to thyroglobulin in rat FRTL-5 cells. !$#cross-references MUID:90114171; PMID:2691880 !$#accession A41408 !'##molecule_type mRNA !'##residues 145-197,'S',199-591,'E',593,'P',595-914 ##label ISO !'##cross-references GB:M31655 COMMENT This protein is a key enzyme in thyroid hormone synthesis. GENETICS !$#gene TPO CLASSIFICATION #superfamily thyroid peroxidase; complement factor H repeat !1homology; EGF homology; myeloperoxidase homology KEYWORDS chromoprotein; glycoprotein; heme; iron; metalloprotein; !1oxidoreductase; transmembrane protein FEATURE !$36-717 #domain myeloperoxidase homology #label MPX\ !$730-782 #domain complement factor H repeat homology #label !8FHR\ !$788-826 #domain EGF homology #label EGF\ !$123,271,299,334,603 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$136-152,253-263, !$257-278,363-377, !$586-643,684-709 #disulfide_bonds #status predicted\ !$232,387 #binding_site hemediol (Asp, Glu) (covalent) #status !8predicted\ !$233 #active_site His (distal axial ligand) #status !8predicted\ !$234,313,315,317,319 #binding_site calcium (Asp, Thr, Phe, Asp, Ser) !8#status predicted\ !$384 #active_site Arg #status predicted\ !$482 #binding_site hemediol iron (His) (proximal axial !8ligand) #status predicted SUMMARY #length 914 #molecular-weight 101460 #checksum 2594 SEQUENCE /// ENTRY JC4397 #type complete TITLE peroxinectin precursor - signal crayfish ALTERNATE_NAMES cell adhesion protein CONTAINS peroxidase (EC 1.11.1.7) ORGANISM #formal_name Pacifastacus leniusculus #common_name signal crayfish DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS JC4397; PC4113 REFERENCE JC4397 !$#authors Johansson, M.W.; Lind, M.I.; Holmblad, T.; Thoernqvist, !1P.O.; Soederhaell, K. !$#journal Biochem. Biophys. Res. Commun. (1995) 216:1079-1087 !$#title Peroxinectin, a novel cell adhesion protein from crayfish !1blood. !$#cross-references MUID:96074593; PMID:7488183 !$#accession JC4397 !'##molecule_type mRNA !'##residues 1-818 ##label JOH !'##cross-references EMBL:X91409; NID:g1150531; PIDN:CAA62752.1; !1PID:g1150532 !'##experimental_source Blood cells !$#accession PC4113 !'##molecule_type protein !'##residues 185-188;660;662-667 ##label JO2 COMMENT This protein acts as both cell adhesion ligand and !1peroxidase, and it belongs to a family of proteins that !1includes myeloperoxidase. It also triggers an intracellular !1signaling pathway involving protein kinase C activation and !1protein tyrosine phosphorylation, leading to cell spreading !1and degranulation, stimulates cellular reactions. CLASSIFICATION #superfamily peroxinectin; myeloperoxidase homology KEYWORDS blood; cell adhesion; chromoprotein; glycoprotein; heme; !1iron; metalloprotein; oxidoreductase FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-818 #product peroxinectin #status predicted #label MAT\ !$142-808 #domain myeloperoxidase homology #label MPX\ !$739-741 #region cell adhesion #status predicted\ !$235-254,346-362, !$347-380,453-462, !$672-728,772-798 #disulfide_bonds #status predicted\ !$328,573 #binding_site heme iron (His) (axial ligands) #status !8predicted\ !$349 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$469 #active_site Arg #status predicted SUMMARY #length 818 #molecular-weight 89315 #checksum 1903 SEQUENCE /// ENTRY JN0867 #type complete TITLE peroxinectin-like protein (clone pL04) - squid (Euprymna scolopes) CONTAINS peroxidase (EC 1.11.1.7) ORGANISM #formal_name Euprymna scolopes DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS JN0867 REFERENCE JN0867 !$#authors Tomarev, S.I.; Zinovieva, R.D.; Weis, V.M.; Chepelinsky, !1A.B.; Piatigorsky, J.; McFall-Ngai, M.J. !$#journal Gene (1993) 132:219-226 !$#title Abundant mRNAs in the squid light organ encode proteins with !1a high similarity to mammalian peroxidases. !$#cross-references MUID:94040765; PMID:8224867 !$#accession JN0867 !'##molecule_type mRNA !'##residues 1-891 ##label TOM !'##cross-references GB:L01772; NID:g159007; PIDN:AAA16245.1; !1PID:g159008 !'##experimental_source light organ CLASSIFICATION #superfamily peroxinectin; myeloperoxidase homology KEYWORDS calcium binding; chromoprotein; glycoprotein; heme; iron; !1metalloprotein; oxidoreductase FEATURE !$170-838 #domain myeloperoxidase homology #label MPX\ !$446-452 #domain calcium binding #status predicted #label CAL\ !$209,409,488,711 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$372 #binding_site calcium (Asp) #status predicted\ !$610 #binding_site heme iron (His) (axial ligand) #status !8predicted SUMMARY #length 891 #molecular-weight 93084 #checksum 2550 SEQUENCE /// ENTRY B41659 #type complete TITLE benzoate 1,2-dioxygenase (EC 1.14.12.10) benB - Pseudomonas putida plasmid TOL pWW0 ORGANISM #formal_name Pseudomonas putida DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B41659; S23483 REFERENCE A41659 !$#authors Harayama, S.; Rekik, M.; Bairoch, A.; Neidle, E.L.; Ornston, !1L.N. !$#journal J. Bacteriol. (1991) 173:7540-7548 !$#title Potential DNA slippage structures acquired during !1evolutionary divergence of Acinetobacter calcoaceticus !1chromosomal benABC and Pseudomonas putida TOL pWWO plasmid !1xylXYZ, genes encoding benzoate dioxygenases. !$#cross-references MUID:92041666; PMID:1938949 !$#accession B41659 !'##status preliminary !'##molecule_type DNA !'##residues 1-162 ##label HAR !'##cross-references GB:M64747; NID:g151718; PIDN:AAA26048.1; !1PID:g151720 REFERENCE S23477 !$#authors Neidle, E.L.; Hartnett, C.; Ornston, L.N.; Bairoch, A.; !1Rekik, M.; Harayama, S. !$#journal Eur. J. Biochem. (1992) 204:113-120 !$#title Cis-diol dehydrogenases encoded by the TOL pWW0 plasmid xylL !1gene and the Acinetobacter calcoaceticus chromosomal benD !1gene are members of the short-chain alcohol dehydrogenase !1superfamily. !$#cross-references MUID:92155191; PMID:1740120 !$#accession S23483 !'##status preliminary !'##molecule_type DNA !'##residues 1-162 ##label NEI !'##cross-references EMBL:M64747; NID:g151718; PIDN:AAA26048.1; !1PID:g151720 GENETICS !$#gene xylY !$#genome plasmid CLASSIFICATION #superfamily benB protein KEYWORDS oxidoreductase SUMMARY #length 162 #molecular-weight 19326 #checksum 6435 SEQUENCE /// ENTRY S23478 #type complete TITLE probable benzoate 1,2-dioxygenase (EC 1.14.12.10) benB - Acinetobacter calcoaceticus ORGANISM #formal_name Acinetobacter calcoaceticus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S23478 REFERENCE S23477 !$#authors Neidle, E.L.; Hartnett, C.; Ornston, L.N.; Bairoch, A.; !1Rekik, M.; Harayama, S. !$#journal Eur. J. Biochem. (1992) 204:113-120 !$#title Cis-diol dehydrogenases encoded by the TOL pWW0 plasmid xylL !1gene and the Acinetobacter calcoaceticus chromosomal benD !1gene are members of the short-chain alcohol dehydrogenase !1superfamily. !$#cross-references MUID:92155191; PMID:1740120 !$#accession S23478 !'##status preliminary; translation not shown !'##molecule_type DNA !'##residues 1-169 ##label NEI !'##cross-references EMBL:M76990; NID:g141746; PID:g141748 CLASSIFICATION #superfamily benB protein KEYWORDS oxidoreductase SUMMARY #length 169 #molecular-weight 20073 #checksum 2188 SEQUENCE /// ENTRY OPBOE #type complete TITLE glutathione peroxidase (EC 1.11.1.9) erythrocyte [validated] - bovine ALTERNATE_NAMES cellular glutathione peroxidase ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 17-May-1985 #sequence_revision 23-Mar-1995 #text_change 15-Sep-2000 ACCESSIONS S04872; A00504; S21712 REFERENCE S04872 !$#authors Mullenbach, G.T.; Tabrizi, A.; Irvine, B.D.; Bell, G.; !1Tainer, I.; Hallewell, R.A. !$#submission submitted to the EMBL Data Library, November 1988 !$#accession S04872 !'##molecule_type mRNA !'##residues 1-205 ##label MUL !'##cross-references EMBL:X13684; NID:g398 REFERENCE A00504 !$#authors Gunzler, W.A.; Steffens, G.J.; Grossmann, A.; Kim, S.M.A.; !1Otting, F.; Wendel, A.; Flohe, L. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1984) 365:195-212 !$#title The amino-acid sequence of bovine glutathione peroxidase. !$#cross-references MUID:84184205; PMID:6714945 !$#accession A00504 !'##molecule_type protein !'##residues 8-205 ##label GUN REFERENCE S21712 !$#authors Gettins, P.; Dyal, D.; Crews, B. !$#journal Arch. Biochem. Biophys. (1992) 294:511-518 !$#title Selenium-dependent glutathione peroxidases from ovine and !1bovine erythrocytes occur as longer chain forms than !1previously recognized. !$#cross-references MUID:92231574; PMID:1567207 !$#accession S21712 !'##molecule_type protein !'##residues 8-19 ##label GET !'##experimental_source erythrocyte REFERENCE A50142 !$#authors Epp, O.; Ladenstein, R. !$#submission submitted to the Brookhaven Protein Data Bank, June 1985 !$#cross-references PDB:1GP1 !$#contents annotation; X-ray crystallography, 2.0 angstroms, residues !117-200 REFERENCE A58467 !$#authors Epp, O.; Ladenstein, R.; Wendel, A. !$#journal Eur. J. Biochem. (1983) 133:51-69 !$#title The refined structure of the selenoenzyme glutathione !1peroxidase at 0.2-nm resolution. !$#cross-references MUID:83209650; PMID:6852035 !$#contents annotation; X-ray crystallography, 2.0 angstroms COMMENT The selenocysteine residue is encoded by TGA. GENETICS !$#gene gpx1 COMPLEX homotetramer FUNCTION !$#description catalyzes the reduction of hydrogen peroxide to water by !1glutathione !$#note this activity protects hemoglobin in erythrocytes from !1oxidation CLASSIFICATION #superfamily glutathione peroxidase KEYWORDS erythrocyte; homotetramer; oxidoreductase; selenocysteine FEATURE !$8-205 #product glutathione peroxidase #status experimental !8#label MAT\ !$52 #modified_site selenocysteine #status experimental SUMMARY #length 205 #molecular-weight 22612 #checksum 2216 SEQUENCE /// ENTRY OPHUE #type complete TITLE glutathione peroxidase (EC 1.11.1.9) 1 - human ALTERNATE_NAMES cytosolic glutathione peroxidase; GPx1 ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1988 #sequence_revision 03-May-1996 #text_change 16-Jun-2000 ACCESSIONS A42152; S06304; A26851; A27851; S32453 REFERENCE A42152 !$#authors Moscow, J.A.; Morrow, C.S.; He, R.; Mullenbach, G.T.; Cowan, !1K.H. !$#journal J. Biol. Chem. (1992) 267:5949-5958 !$#title Structure and function of the 5'-flanking sequence of the !1human cytosolic selenium-dependent glutathione peroxidase !1gene (hgpx1). !$#cross-references MUID:92210561; PMID:1556108 !$#accession A42152 !'##molecule_type DNA !'##residues 1-202 ##label MOS !'##cross-references GB:M83094; NID:g806640; PIDN:AAA67540.1; !1PID:g488476 !'##note the codon given for 199-Pro (CTC) is inconsistent with the !1authors' translation !'##note in Genbank entry HUMGLPEX, release 111.0, PID:g488476, the !1selenocysteine UGA codon for residue 48 is translated as 'X' REFERENCE S06304 !$#authors Ishida, K.; Morino, T.; Takagi, K.; Sukenaga, Y. !$#journal Nucleic Acids Res. (1987) 15:10051 !$#title Nucleotide sequence of a human gene for glutathione !1peroxidase. !$#cross-references MUID:88096498; PMID:3697069 !$#accession S06304 !'##molecule_type DNA !'##residues 1-11,13-202 ##label ISH !'##cross-references EMBL:Y00483; NID:g31918; PIDN:CAB37833.1; !1PID:g4467837 REFERENCE A26851 !$#authors Sukenaga, Y.; Ishida, K.; Takeda, T.; Takagi, K. !$#journal Nucleic Acids Res. (1987) 15:7178 !$#title cDNA sequence coding for human glutathione peroxidase. !$#cross-references MUID:88015555; PMID:3658677 !$#accession A26851 !'##molecule_type mRNA !'##residues 1-11,13-202 ##label SUK !'##cross-references EMBL:Y00433; NID:g31917; PIDN:CAA68491.1; !1PID:g577777 !'##note in Genbank entry HSGSHPX, release 111.0, PID:g577777, the !1selenocysteine UGA codon for residue 48 is translated as 'X' REFERENCE A27851 !$#authors Mullenbach, G.T.; Tabrizi, A.; Irvine, B.D.; Bell, G.I.; !1Hallewell, R.A. !$#journal Nucleic Acids Res. (1987) 15:5484 !$#title Sequence of a cDNA coding for human glutathione peroxidase !1confirms TGA encodes active site selenocysteine. !$#cross-references MUID:87260018; PMID:2955287 !$#accession A27851 !'##molecule_type mRNA !'##residues 1-11,13-91,'Q',93-202 ##label MUL !'##cross-references GB:X13709; EMBL:X13430; GB:Y00369; NID:g35389; !1PIDN:CAA31992.1; PID:g577062 !'##note in Genbank entry HSPEROXR, release 111.0, PID:g577062, the !1selenocysteine UGA codon for residue 48 is translated as 'X' GENETICS !$#gene GDB:GPX1; GSHPX !'##cross-references GDB:119282; OMIM:138320 !$#map_position 3q11-3q12 !$#introns 83/3 COMPLEX homotetramer FUNCTION !$#description catalyzes the reduction of hydrogen peroxide to water by !1glutathione CLASSIFICATION #superfamily glutathione peroxidase KEYWORDS homotetramer; oxidoreductase; selenocysteine FEATURE !$48 #modified_site selenocysteine #status predicted SUMMARY #length 202 #molecular-weight 21970 #checksum 3562 SEQUENCE /// ENTRY OPMSE #type complete TITLE glutathione peroxidase (EC 1.11.1.9) - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 16-Jun-2000 ACCESSIONS A25106 REFERENCE A25106 !$#authors Chambers, I.; Frampton, J.; Goldfarb, P.; Affara, N.; !1McBain, W.; Harrison, P.R. !$#journal EMBO J. (1986) 5:1221-1227 !$#title The structure of the mouse glutathione peroxidase gene: the !1selenocysteine in the active site is encoded by the !1'termination' codon, TGA. !$#cross-references MUID:86274624; PMID:3015592 !$#accession A25106 !'##molecule_type DNA !'##residues 1-201 ##label CHA !'##cross-references GB:X03920; NID:g51123; PIDN:CAA27558.1; !1PID:g2673845 CLASSIFICATION #superfamily glutathione peroxidase KEYWORDS erythrocyte; homotetramer; oxidoreductase; selenocysteine FEATURE !$47 #modified_site selenocysteine #status predicted SUMMARY #length 201 #molecular-weight 22282 #checksum 2532 SEQUENCE /// ENTRY OPRTE #type complete TITLE glutathione peroxidase (EC 1.11.1.9) I - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 21-Jul-2000 ACCESSIONS A30793; S03660; S01192; A21598; S21119 REFERENCE A30793 !$#authors Yoshimura, S.; Takekoshi, S.; Watanabe, K.; Fujii-Kuriyama, !1Y. !$#journal Biochem. Biophys. Res. Commun. (1988) 154:1024-1028 !$#title Determination of nucleotide sequence of cDNA coding rat !1glutathione peroxidase and diminished expression of the mRNA !1in selenium deficient rat liver. !$#cross-references MUID:88309078; PMID:3408482 !$#accession A30793 !'##molecule_type mRNA !'##residues 1-201 ##label YOS REFERENCE S03660 !$#authors Reddy, A.P.; Hsu, B.L.; Reddy, P.S.; Li, N.Q.; Thyagaraju, !1K.; Reddy, C.C.; Tam, M.F.; Tu, C.P.D. !$#journal Nucleic Acids Res. (1988) 16:5557-5568 !$#title Expression of glutathione peroxidase I gene in !1selenium-deficient rats. !$#cross-references MUID:88262561; PMID:2838821 !$#accession S03660 !'##molecule_type mRNA !'##residues 1-177,'S',179-201 ##label RED !'##cross-references GB:X12367; NID:g288455; PIDN:CAA30928.1; !1PID:g2654236 REFERENCE S01192 !$#authors Ho, Y.S.; Howard, A.J.; Crapo, J.D. !$#journal Nucleic Acids Res. (1988) 16:5207 !$#title Nucleotide sequence of a rat glutathione peroxidase cDNA. !$#cross-references MUID:88262522; PMID:3387231 !$#accession S01192 !'##molecule_type mRNA !'##residues 1-177,'S',179-201 ##label HO1 !'##cross-references EMBL:X07365; NID:g56328; PIDN:CAB43593.1; !1PID:g4902841 REFERENCE A21598 !$#authors Condell, R.A.; Tappel, A.L. !$#journal Biochim. Biophys. Acta (1982) 709:304-309 !$#title Amino acid sequence around the active-site selenocysteine of !1rat liver glutathione peroxidase. !$#cross-references MUID:83101425; PMID:6217842 !$#accession A21598 !'##molecule_type protein !'##residues 'G',8-52 ##label CON REFERENCE S21119 !$#authors Ho, Y.S.; Howard, A.J. !$#journal FEBS Lett. (1992) 301:5-9 !$#title Cloning and characterization of the rat glutathione !1peroxidase gene. !$#cross-references MUID:93083623; PMID:1451786 !$#accession S21119 !'##molecule_type DNA !'##residues 1-177,'S',179-201 ##label HOY !'##cross-references GB:X07365; GB:S50336; NID:g56328; PIDN:CAB43593.1; !1PID:g4902841 COMMENT Glutathione peroxidase catalyzes the reduction of hydrogen !1peroxide by glutathione and protects the hemoglobin in !1erythrocytes from oxidative breakdown. The selenocysteine !1residue is encoded by TGA. GENETICS !$#introns 82/3 CLASSIFICATION #superfamily glutathione peroxidase KEYWORDS erythrocyte; homotetramer; oxidoreductase; selenocysteine FEATURE !$47 #modified_site selenocysteine #status experimental SUMMARY #length 201 #molecular-weight 22272 #checksum 2949 SEQUENCE /// ENTRY S03723 #type complete TITLE glutathione peroxidase (EC 1.11.1.9) - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S03723 REFERENCE S03723 !$#authors Akasaka, M.; Mizoguch, J.; Yoshimura, S.; Watanabe, K. !$#journal Nucleic Acids Res. (1989) 17:2136 !$#title Nucleotide sequence of cDNA for rabbit glutathione !1peroxidase. !$#cross-references MUID:89183631; PMID:2928123 !$#accession S03723 !'##molecule_type mRNA !'##residues 1-200 ##label AKA !'##cross-references EMBL:X13837; NID:g1564; PIDN:CAB43546.1; !1PID:g4902842 CLASSIFICATION #superfamily glutathione peroxidase KEYWORDS oxidoreductase; selenocysteine FEATURE !$46 #modified_site selenocysteine #status predicted SUMMARY #length 200 #molecular-weight 21836 #checksum 1217 SEQUENCE /// ENTRY A45207 #type complete TITLE glutathione peroxidase (EC 1.11.1.9) 2 - human ALTERNATE_NAMES gastrointestinal glutathione peroxidase (GSHPx-GI); glutathione peroxidase-related protein; hepatic glutathione peroxidase ORGANISM #formal_name Homo sapiens #common_name man DATE 28-May-1999 #sequence_revision 28-May-1999 #text_change 28-May-1999 ACCESSIONS A45207; B45207; S11154 REFERENCE A45207 !$#authors Chu, F.F.; Doroshow, J.H.; Esworthy, R.S. !$#journal J. Biol. Chem. (1993) 268:2571-2576 !$#title Expression, characterization, and tissue distribution of a !1new cellular selenium-dependent glutathione peroxidase, !1GSHPx-GI. !$#cross-references MUID:93155065; PMID:8428933 !$#accession A45207 !'##molecule_type mRNA !'##residues 1-190 ##label CHU1 !'##cross-references EMBL:X68314; NID:g31880; PIDN:CAA48394.1; !1PID:g579930 !'##experimental_source hepatoma HepG2 cells !'##note sequence extracted from NCBI backbone (NCBIP:124151) !'##note in Genbank entry HSGPGI, release 111.0, PID:g579930, the !1selenocysteine UGA codon for residue 40 is translated as 'X' !$#accession B45207 !'##molecule_type mRNA !'##residues 1-36,'L',38-175,'M',177-190 ##label CHU2 !'##experimental_source liver REFERENCE S11154 !$#authors Akasaka, M.; Mizoguchi, J.; Takahashi, K. !$#journal Nucleic Acids Res. (1990) 18:4619 !$#title A human cDNA sequence for a novel glutathione !1peroxidase-related protein. !$#cross-references MUID:90356426; PMID:2388849 !$#accession S11154 !'##status preliminary !'##molecule_type mRNA !'##residues 1-36,'R',38-190 ##label AKA !'##cross-references EMBL:X53463; NID:g31894 !'##note this ORF is not annotated in GenBank entry HSGPLP, release !1111.0; the translation of the revised sequence would have !177-Ser GENETICS !$#gene GDB:GPX2; GSHPX-GI !'##cross-references GDB:138282; OMIM:138319 !$#map_position 14q24.1-14q24.1 COMPLEX homotetramer FUNCTION !$#description catalyzes the reduction of hydrogen peroxide to water by !1glutathione CLASSIFICATION #superfamily glutathione peroxidase KEYWORDS homotetramer; intestine; liver; oxidoreductase; !1selenocysteine; stomach FEATURE !$40 #modified_site selenocysteine #status predicted SUMMARY #length 190 #molecular-weight 21907 #checksum 4589 SEQUENCE /// ENTRY S24328 #type complete TITLE glutathione peroxidase (EC 1.11.1.9) precursor, secretory [similarity] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS S24328; S18913 REFERENCE S24327 !$#authors Perry, A.C.F.; Jones, R.; Niang, L.S.P.; Jackson, R.M.; !1Hall, L. !$#journal Biochem. J. (1992) 285:863-870 !$#title Genetic evidence for an androgen-regulated epididymal !1secretory glutathione peroxidase whose transcript does not !1contain a selenocysteine codon. !$#cross-references MUID:92359957; PMID:1386734 !$#accession S24328 !'##molecule_type mRNA !'##residues 1-221 ##label PER !'##cross-references EMBL:X62404; NID:g57551; PIDN:CAA44274.1; !1PID:g57552 REFERENCE S18912 !$#authors Perry, A.C.F.; Jones, R.; Niang, L.S.P.; Jackson, R.M.; !1Hall, L. !$#submission submitted to the EMBL Data Library, December 1991 !$#accession S18913 !'##molecule_type mRNA !'##residues 1-221 ##label PER2 !'##cross-references EMBL:X62404; NID:g57551; PIDN:CAA44274.1; !1PID:g57552 CLASSIFICATION #superfamily glutathione peroxidase KEYWORDS oxidoreductase SUMMARY #length 221 #molecular-weight 25384 #checksum 7259 SEQUENCE /// ENTRY S24327 #type complete TITLE glutathione peroxidase (EC 1.11.1.9) precursor, epididymal, secretory - crab-eating macaque ORGANISM #formal_name Macaca fascicularis #common_name crab-eating macaque DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S24327; S18912 REFERENCE S24327 !$#authors Perry, A.C.F.; Jones, R.; Niang, L.S.P.; Jackson, R.M.; !1Hall, L. !$#journal Biochem. J. (1992) 285:863-870 !$#title Genetic evidence for an androgen-regulated epididymal !1secretory glutathione peroxidase whose transcript does not !1contain a selenocysteine codon. !$#cross-references MUID:92359957; PMID:1386734 !$#accession S24327 !'##molecule_type mRNA !'##residues 1-221 ##label PER !'##cross-references EMBL:X62403; NID:g38064; PIDN:CAA44273.1; !1PID:g38065 CLASSIFICATION #superfamily glutathione peroxidase KEYWORDS oxidoreductase FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-221 #product glutathione peroxidase, epididymal, !8secretory #status predicted #label MAT SUMMARY #length 221 #molecular-weight 25212 #checksum 4824 SEQUENCE /// ENTRY JX0176 #type complete TITLE glutathione peroxidase (EC 1.11.1.9) precursor [similarity] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 15-Sep-2000 ACCESSIONS JX0176 REFERENCE JX0176 !$#authors Yoshimura, S.; Watanabe, K.; Suemizu, H.; Onozawa, T.; !1Mizoguchi, J.; Tsuda, K.; Hatta, H.; Moriuchi, T. !$#journal J. Biochem. (1991) 109:918-923 !$#title Tissue specific expression of the plasma glutathione !1peroxidase gene in rat kidney. !$#cross-references MUID:92041746; PMID:1939013 !$#accession JX0176 !'##molecule_type mRNA !'##residues 1-226 ##label YOS !'##cross-references GB:D00680; NID:g220843; PIDN:BAA00587.2; !1PID:g6723180 !'##experimental_source kidney CLASSIFICATION #superfamily glutathione peroxidase KEYWORDS oxidoreductase; pyroglutamic acid; selenocysteine FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-226 #product glutathione peroxidase #status predicted !8#label MAT\ !$25 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status predicted\ !$73 #modified_site selenocysteine #status predicted SUMMARY #length 226 #molecular-weight 25393 #checksum 2768 SEQUENCE /// ENTRY A55086 #type complete TITLE glutathione peroxidase (EC 1.11.1.9), plasma, precursor [similarity] - mouse ALTERNATE_NAMES GPX3 protein ORGANISM #formal_name Mus musculus #common_name house mouse DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 15-Sep-2000 ACCESSIONS A55086; JC4550; PC4129 REFERENCE A55086 !$#authors Maser, R.L.; Magenheimer, B.S.; Calvet, J.P. !$#journal J. Biol. Chem. (1994) 269:27066-27073 !$#title Mouse plasma glutathione peroxidase. cDNA sequence analysis !1and renal proximal tubular expression and secretion. !$#cross-references MUID:95014577; PMID:7929449 !$#accession A55086 !'##molecule_type mRNA !'##residues 1-226 ##label MAS !'##cross-references GB:U13705; NID:g536927; PIDN:AAA62283.1; !1PID:g536928 REFERENCE JC4550 !$#authors Schwaab, V.; Baud, E.; Ghyselinck, N.; Mattei, M.G.; !1Dufaure, J.P.; Drevet, J.R. !$#journal Gene (1995) 167:25-31 !$#title Cloning of the mouse gene encoding plasma glutathione !1peroxidase: Organization, sequence and chromosomal !1localization. !$#cross-references MUID:96144244; PMID:8566787 !$#accession JC4550 !'##molecule_type mRNA !'##residues 1-5,'G',8-65,'P',67-100,'C',102-134,'P',136-226 ##label SCH !'##cross-references EMBL:X84742; NID:g683479 !'##experimental_source strain Balb/C, epididymis !'##note this translation is not annotated in GenBank entry MMGPXG, !1release 114 COMMENT This enzyme is a major enzyme in reducing lipid !1hydroperoxides and hydrogen peroxide in plasma, using !1glutathione as the reducing agent, thereby protecting cells !1from oxidative damage resulting from normal oxidative !1metabolism. GENETICS !$#gene gpx3 !$#map_position 11 !$#introns 29/3; 80/3; 120/3; 153/3 CLASSIFICATION #superfamily glutathione peroxidase KEYWORDS epididymis; oxidoreductase; plasma; pyroglutamic acid; !1selenocysteine FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-226 #product plasma glutathione peroxidase #status !8predicted #label MAT\ !$25 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status predicted\ !$73 #modified_site selenocysteine #status predicted SUMMARY #length 226 #molecular-weight 25377 #checksum 4360 SEQUENCE /// ENTRY JQ0476 #type complete TITLE glutathione peroxidase (EC 1.11.1.9) 3, precursor [validated] - human ALTERNATE_NAMES erythrocyte glutathione peroxidase; plasma glutathione peroxidase (GSHPX-P) ORGANISM #formal_name Homo sapiens #common_name man DATE 28-May-1999 #sequence_revision 28-May-1999 #text_change 15-Sep-2000 ACCESSIONS I53822; JQ0476; S15877 REFERENCE I53822 !$#authors Yoshimura, S.; Suemizu, H.; Taniguchi, Y.; Arimori, K.; !1Kawabe, N.; Moriuchi, T. !$#journal Gene (1994) 145:293-297 !$#title The human plasma glutathione peroxidase-encoding gene: !1organization, sequence and localization to chromosome 5q32. !$#cross-references MUID:94333825; PMID:8056346 !$#accession I53822 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-29 ##label YOS !'##cross-references GB:D16360; NID:g303608; PIDN:BAA03862.1; !1PID:g404106 REFERENCE JQ0476 !$#authors Takahashi, K.; Akasaka, M.; Yamamoto, Y.; Kobayashi, C.; !1Mizoguchi, J.; Koyama, J. !$#journal J. Biochem. (1990) 108:145-148 !$#title Primary structure of human plasma glutathione peroxidase !1deduced from cDNA sequences. !$#cross-references MUID:91035338; PMID:2229017 !$#accession JQ0476 !'##molecule_type mRNA !'##residues 1-226 ##label TAK !'##cross-references GB:D00632; NID:g219667; PIDN:BAA00525.1; !1PID:g2160390 !'##note part of this sequence was confirmed by protein sequencing REFERENCE S15877 !$#authors Esworthy, R.S.; Chu, F.F.; Paxton, R.J.; Akman, S.; !1Doroshow, J.H. !$#journal Arch. Biochem. Biophys. (1991) 286:330-336 !$#title Characterization and partial amino acid sequence of human !1plasma glutathione peroxidase. !$#cross-references MUID:91378320; PMID:1897960 !$#accession S15877 !'##molecule_type protein !'##residues 107-138;148-176,'Q',178-197,'RQQ' ##label ARC !'##note the sequence from Fig. 6 is inconsistent with that from Table !1II in having 169-Ile REFERENCE A38863 !$#authors Maddipati, K.R.; Marnett, L.J. !$#journal J. Biol. Chem. (1987) 262:17398-17403 !$#title Characterization of the major hydroperoxide-reducing !1activity of human plasma: purification and properties of a !1selenium-dependent glutathione peroxidase. !$#cross-references MUID:88087018; PMID:3693360 !$#contents annotation GENETICS !$#gene GDB:GPX3 !'##cross-references GDB:138344; OMIM:138321 !$#map_position 5q31.1-5q33.2 FUNCTION !$#description catalyzes the reduction of hydrogen peroxide to water by !1glutathione !$#note protects hemoglobin in erythrocytes from oxidation CLASSIFICATION #superfamily glutathione peroxidase KEYWORDS erythrocyte; oxidoreductase; plasma; pyroglutamic acid; !1selenocysteine FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-226 #product glutathione peroxidase 3 #status predicted !8#label MAT\ !$25 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status predicted\ !$73 #modified_site selenocysteine #status experimental SUMMARY #length 226 #molecular-weight 25505 #checksum 4397 SEQUENCE /// ENTRY JX0280 #type complete TITLE glutathione peroxidase (EC 1.11.1.9), plasma, precursor [similarity] - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 22-Oct-2001 ACCESSIONS JX0280; JQ2271 REFERENCE JX0280 !$#authors Martin-Alonso, J.M.; Ghosh, S.; Coca-Prados, M. !$#journal J. Biochem. (1993) 114:284-291 !$#title Cloning of the bovine plasma selenium-dependent glutathione !1peroxidase (GP) cDNA from the ocular ciliary epithelium: !1Expression of the plasma and cellular forms within the !1mammalian eye. !$#cross-references MUID:94086479; PMID:8262911 !$#accession JX0280 !'##molecule_type mRNA !'##residues 1-226 ##label MA2 !'##cross-references GB:L10325; NID:g163705; PIDN:AAA16579.2; !1PID:g14717817 !'##experimental_source eye !'##note in Genbank entry BOVSELGP, release 117.0, PIDN:AAA16579.1, the !1selenocysteine UGA codon for residue 73 is translated as 'X' CLASSIFICATION #superfamily glutathione peroxidase KEYWORDS erythrocyte; homotetramer; oxidoreductase; pyroglutamic !1acid; selenocysteine FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-226 #product glutathione peroxidase, plasma #status !8predicted #label MAT\ !$25 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status predicted\ !$73 #modified_site selenocysteine #status predicted SUMMARY #length 226 #molecular-weight 25616 #checksum 4471 SEQUENCE /// ENTRY QRECBE #type complete TITLE vitamin B12 transport periplasmic protein btuE - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS F64929; B24498 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64929 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-183 ##label BLAT !'##cross-references GB:AE000266; GB:U00096; NID:g1787997; !1PIDN:AAC74780.1; PID:g1788003; UWGP:b1710 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A24498 !$#authors Friedrich, M.J.; DeVeaux, L.C.; Kadner, R.J. !$#journal J. Bacteriol. (1986) 167:928-934 !$#title Nucleotide sequence of the btuCED genes involved in vitamin !1B12 transport in Escherichia coli and homology with !1components of periplasmic-binding-protein-dependent !1transport systems. !$#cross-references MUID:86304184; PMID:3528129 !$#accession B24498 !'##molecule_type DNA !'##residues 1-183 ##label FRI !'##cross-references GB:M14031; NID:g145441; PIDN:AAA23527.1; !1PID:g145444 COMMENT This protein, thought to be located in the periplasm, is not !1essential for B12 transport; however, it is an auxiliary !1component of the transport system. COMMENT This sequence is homologous with that of bovine glutathione !1peroxidase (41% identity over a region of 156 residues); !1however, the significance of the relationship is not clear. GENETICS !$#gene btuE !$#map_position 37 min CLASSIFICATION #superfamily glutathione peroxidase KEYWORDS vitamin B12 transport FEATURE !$37 #active_site Cys #status predicted SUMMARY #length 183 #molecular-weight 20469 #checksum 4065 SEQUENCE /// ENTRY S48499 #type complete TITLE glutathione peroxidase (EC 1.11.1.9) HYR1 [similarity] - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YIR037w ORGANISM #formal_name Saccharomyces cerevisiae DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 21-Jul-2000 ACCESSIONS S48499; S59420 REFERENCE S48478 !$#authors Rowley, K. !$#submission submitted to the EMBL Data Library, October 1994 !$#accession S48499 !'##molecule_type DNA !'##residues 1-163 ##label ROW !'##cross-references GB:Z47047; EMBL:Z38061; NID:g603997; PID:g763382; !1GSPDB:GN00009; MIPS:YIR037w REFERENCE S59420 !$#authors Budde, E.; Stahl, U. !$#submission submitted to the EMBL Data Library, March 1995 !$#description Cloning and phenotypic characterization of a !1glutathione-peroxidase like gene involved in the oxidative !1stress response of Saccharomyces cerevisiae. !$#accession S59420 !'##molecule_type DNA !'##residues 1-163 ##label BUD !'##cross-references EMBL:U22446; NID:g727366; PIDN:AAA64283.1; !1PID:g727367 !'##experimental_source strain AH22 GENETICS !$#gene SGD:HYR1; MIPS:YIR037w !'##cross-references SGD:S0001476; MIPS:YIR037w !$#map_position 9R FUNCTION !$#description mediates resistance to oxidative stress; oxidoreductase CLASSIFICATION #superfamily glutathione peroxidase KEYWORDS oxidoreductase; selenocysteine FEATURE !$36 #modified_site selenocysteine #status predicted SUMMARY #length 163 #molecular-weight 18641 #checksum 5749 SEQUENCE /// ENTRY S71250 #type complete TITLE glutathione peroxidase (EC 1.11.1.9) precursor - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S71250 REFERENCE S71250 !$#authors Gachotte, D.; Benveniste, P. !$#submission submitted to the EMBL Data Library, July 1995 !$#description Cloning of a glutathione peroxydase homolog in Arabidopsis !1thaliana. !$#accession S71250 !'##molecule_type mRNA !'##residues 1-242 ##label GAC !'##cross-references EMBL:X89866; NID:g1061035; PIDN:CAA61965.1; !1PID:g1061036 GENETICS !$#genome nuclear CLASSIFICATION #superfamily glutathione peroxidase KEYWORDS chloroplast; oxidoreductase; selenocysteine FEATURE !$1-64 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$65-242 #product glutathione peroxidase #status predicted !8#label MAT\ !$111 #modified_site selenocysteine #status predicted SUMMARY #length 242 #molecular-weight 26814 #checksum 9890 SEQUENCE /// ENTRY S33618 #type complete TITLE glutathione peroxidase (EC 1.11.1.9) - sweet orange ALTERNATE_NAMES salt-associated protein csaA ORGANISM #formal_name Citrus sinensis #common_name sweet orange DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S33618; S36373 REFERENCE S33618 !$#authors Holland, D.; Ben-Hayyim, G.; Faltin, Z.; Camoin, L.; !1Strosberg, A.D.; Eshdat, Y. !$#journal Plant Mol. Biol. (1993) 21:923-927 !$#title Molecular characterization of salt-stress-associated protein !1in citrus: protein and cDNA sequence homology to mammalian !1glutathione peroxidases. !$#cross-references MUID:93222490; PMID:8467085 !$#accession S33618 !'##status preliminary; nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-167 ##label HOL !'##cross-references EMBL:X66377 !'##note part of this sequence was confirmed by protein sequencing REFERENCE S36373 !$#authors Holland, D. !$#submission submitted to the EMBL Data Library, May 1992 !$#accession S36373 !'##status preliminary !'##molecule_type mRNA !'##residues 1-52,'Q',54-167 ##label HO2 !'##cross-references EMBL:X66377; NID:g296357; PIDN:CAA47018.1; !1PID:g296358 GENETICS !$#gene csaA CLASSIFICATION #superfamily glutathione peroxidase KEYWORDS oxidoreductase; selenocysteine FEATURE !$41 #modified_site selenocysteine #status predicted SUMMARY #length 167 #molecular-weight 18555 #checksum 9578 SEQUENCE /// ENTRY S20501 #type complete TITLE probable glutathione peroxidase (EC 1.11.1.9) - wood tobacco ORGANISM #formal_name Nicotiana sylvestris #common_name wood tobacco DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S20501 REFERENCE S20501 !$#authors Criqui, M.C.; Jamet, E.; Parmentier, Y.; Marbach, J.; Durr, !1A.; Fleck, J. !$#journal Plant Mol. Biol. (1992) 18:623-627 !$#title Isolation and characterization of a plant cDNA showing !1homology to animal glutathione peroxidases. !$#cross-references MUID:92163033; PMID:1536938 !$#accession S20501 !'##status preliminary !'##molecule_type mRNA !'##residues 1-169 ##label CRI !'##cross-references EMBL:X60219; NID:g19738; PIDN:CAA42780.1; !1PID:g19739 CLASSIFICATION #superfamily glutathione peroxidase KEYWORDS oxidoreductase SUMMARY #length 169 #molecular-weight 18767 #checksum 9415 SEQUENCE /// ENTRY S23062 #type complete TITLE probable glutathione peroxidase (EC 1.11.1.9) precursor - nematode (Brugia pahangi) ALTERNATE_NAMES cuticular glycoprotein gp29 ORGANISM #formal_name Brugia pahangi DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S23062; S34276; S60594 REFERENCE S23062 !$#authors Cookson, E.; Blaxter, M.L.; Selkirk, M.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:5837-5841 !$#title Identification of the major soluble cuticular glycoprotein !1of lymphatic filarial nematode parasites (gp29) as a !1secretory homolog of glutathione peroxidase. !$#cross-references MUID:92335192; PMID:1631065 !$#accession S23062 !'##molecule_type mRNA !'##residues 1-223 ##label COO !'##cross-references EMBL:X63365; NID:g5944; PIDN:CAA44965.1; PID:g5945 REFERENCE S34276 !$#authors Cox-Singh, J.; Paine, M.; Devaney, E. !$#submission submitted to the EMBL Data Library, June 1993 !$#description Differential transcription of gp30 throughout the life cycle !1of brugia pahangi. !$#accession S34276 !'##molecule_type mRNA !'##residues 1-223 ##label COX !'##cross-references EMBL:X73232; NID:g469468; PIDN:CAA51704.1; !1PID:g312033 REFERENCE S60592 !$#authors Cookson, E.; Tang, L.; Selkirk, M.E. !$#journal Mol. Biochem. Parasitol. (1993) 58:155-160 !$#title Conservation of primary sequence of gp29, the major soluble !1cuticular glycoprotein, in three species of lymphatic !1filariae. !$#cross-references MUID:93211443; PMID:8459826 !$#accession S60594 !'##molecule_type DNA !'##residues 1-95,'I',97-223 ##label CO2 !'##cross-references EMBL:X69128; NID:g5946; PIDN:CAA48882.1; !1PID:g296224 !'##note the authors translated the codon ATA for residue 96 as Asn GENETICS !$#gene gp29 !$#introns 22/1; 75/1; 156/3 CLASSIFICATION #superfamily glutathione peroxidase KEYWORDS glycoprotein; oxidoreductase FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-223 #product cuticular glycoprotein gp29 #status !8predicted #label MAT\ !$39,92 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$74 #active_site Cys #status predicted SUMMARY #length 223 #molecular-weight 25883 #checksum 5153 SEQUENCE /// ENTRY S60593 #type complete TITLE probable glutathione peroxidase (EC 1.11.1.9) precursor - nematode (Brugia malayi) ALTERNATE_NAMES cuticular glycoprotein gp29 ORGANISM #formal_name Brugia malayi DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S60593; S30559 REFERENCE S60592 !$#authors Cookson, E.; Tang, L.; Selkirk, M.E. !$#journal Mol. Biochem. Parasitol. (1993) 58:155-160 !$#title Conservation of primary sequence of gp29, the major soluble !1cuticular glycoprotein, in three species of lymphatic !1filariae. !$#cross-references MUID:93211443; PMID:8459826 !$#accession S60593 !'##molecule_type DNA !'##residues 1-223 ##label COO !'##cross-references EMBL:X69127; NID:g5875; PIDN:CAA48881.1; PID:g5876 GENETICS !$#gene gp29 !$#introns 22/1; 75/1; 156/3 CLASSIFICATION #superfamily glutathione peroxidase KEYWORDS glycoprotein; oxidoreductase FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-223 #product glutathione peroxidase, 29K #status !8predicted #label MAT\ !$39,92 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$74 #active_site Cys #status predicted SUMMARY #length 223 #molecular-weight 25883 #checksum 5153 SEQUENCE /// ENTRY S60592 #type complete TITLE probable glutathione peroxidase (EC 1.11.1.9) gp29 - nematode (Wuchereria bancrofti) ORGANISM #formal_name Wuchereria bancrofti DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S60592; S30517 REFERENCE S60592 !$#authors Cookson, E.; Tang, L.; Selkirk, M.E. !$#journal Mol. Biochem. Parasitol. (1993) 58:155-160 !$#title Conservation of primary sequence of gp29, the major soluble !1cuticular glycoprotein, in three species of lymphatic !1filariae. !$#cross-references MUID:93211443; PMID:8459826 !$#accession S60592 !'##molecule_type DNA !'##residues 1-223 ##label COO !'##cross-references EMBL:X69126; NID:g10869; PIDN:CAA48880.1; !1PID:g10870 GENETICS !$#gene gp29 !$#introns 22/1; 75/1; 156/3 CLASSIFICATION #superfamily glutathione peroxidase KEYWORDS glycoprotein; oxidoreductase SUMMARY #length 223 #molecular-weight 25845 #checksum 4297 SEQUENCE /// ENTRY JN0608 #type complete TITLE phospholipid-hydroperoxide glutathione peroxidase (EC 1.11.1.12) - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS JN0608; A53395; A54649 REFERENCE JN0608 !$#authors Sunde, R.A.; Dyer, J.A.; Moran, T.V.; Evenson, J.K.; !1Sugimoto, M. !$#journal Biochem. Biophys. Res. Commun. (1993) 193:905-911 !$#title Phospholipid hydroperoxide glutathione peroxidase: !1full-length pig blastocyst cDNA sequence and regulation by !1selenium status. !$#cross-references MUID:93312346; PMID:8323565 !$#accession JN0608 !'##molecule_type mRNA !'##residues 1-170 ##label SUN !'##cross-references GB:L12743; NID:g294224; PIDN:AAA31099.1; !1PID:g294226 !'##experimental_source blastocyst REFERENCE A53395 !$#authors Brigelius-Flohe, R.; Aumann, K.D.; Bloecker, H.; Gross, G.; !1Kiess, M.; Kloeppel, K.D.; Maiorino, M.; Roveri, A.; !1Schuckelt, R.; Ursini, F.; Wingender, E.; Flohe, L. !$#journal J. Biol. Chem. (1994) 269:7342-7348 !$#title Phospholipid-hydroperoxide glutathione peroxidase. Genomic !1DNA, cDNA, and deduced amino acid sequence. !$#cross-references MUID:94171752; PMID:8125951 !$#accession A53395 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-45,'S',47-170 ##label BRI !'##cross-references GB:X76008; NID:g473358; PIDN:CAA53595.1; !1PID:g2654294; GB:X76009; NID:g483501; PID:g2654295 REFERENCE A54649 !$#authors Schuckelt, R.; Brigelius-Flohe, R.; Maiorino, M.; Roveri, !1A.; Reumkens, J.; Strassburger, W.; Ursini, F.; Wolf, B.; !1Flohe, L. !$#journal Free Radic. Res. Commun. (1991) 14:343-361 !$#title Phospholipid hydroperoxide glutathione peroxidase is a !1selenoenzyme distinct from the classical glutathione !1peroxidase as evident from cDNA and amino acid sequencing. !$#cross-references MUID:92137773; PMID:1778506 !$#accession A54649 !'##status preliminary !'##molecule_type mRNA; protein !'##residues 13-45,47-170 ##label SCH !'##cross-references GB:S80257; NID:g244650; PIDN:AAB21327.1; !1PID:g244651 !'##experimental_source heart !'##note sequence extracted from NCBI backbone (NCBIN:80257, !1NCBIP:80258) CLASSIFICATION #superfamily glutathione peroxidase KEYWORDS oxidoreductase; selenocysteine FEATURE !$46 #modified_site selenocysteine #status predicted SUMMARY #length 170 #molecular-weight 19444 #checksum 1766 SEQUENCE /// ENTRY JC4332 #type complete TITLE phospholipid-hydroperoxide glutathione peroxidase (EC 1.11.1.12) - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JC4332 REFERENCE JC4332 !$#authors Imai, H.; Sumi, D.; Hanamoto, A.; Arai, M.; Sugiyama, A.; !1Chiba, N.; Kuchino, Y.; Nakagawa, Y. !$#journal J. Biochem. (1995) 118:1061-1067 !$#title Molecular cloning and functional expression of a cDNA for !1rat phospholipid hydroperoxide glutathione peroxidase: !13'-untranslated region of the geneis necessary for !1functional expression. !$#cross-references MUID:96318522; PMID:8749327 !$#accession JC4332 !'##molecule_type mRNA !'##residues 1-170 ##label IMA !'##cross-references EMBL:X82679; NID:g1041644; PIDN:CAA57996.1; !1PID:g1041645 !'##experimental_source brain COMMENT This enzyme is a unique enzyme in glutathione peroxidase and !1is a selenoprotein. It interacts directly with peroxidized !1phospholipids and cholesterol and reduces their !1hydroperoxide moieties. It defenses against oxidative !1destruction of biomembranes. GENETICS !$#introns 45/3 CLASSIFICATION #superfamily glutathione peroxidase KEYWORDS brain; oxidoreductase; phospholipid; selenocysteine FEATURE !$46 #modified_site selenocysteine #status experimental SUMMARY #length 170 #molecular-weight 19443 #checksum 2252 SEQUENCE /// ENTRY A28557 #type complete TITLE chloride peroxidase (EC 1.11.1.10) precursor - fungus (Leptoxyphium fumago) ALTERNATE_NAMES chloroperoxidase ORGANISM #formal_name Leptoxyphium fumago DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A28557; A25548; A25936; A60824; A31956 REFERENCE A28557 !$#authors Nuell, M.J.; Fang, G.H.; Axley, M.J.; Kenigsberg, P.; Hager, !1L.P. !$#journal J. Bacteriol. (1988) 170:1007-1011 !$#title Isolation and nucleotide sequence of the chloroperoxidase !1gene from Caldariomyces fumago. !$#cross-references MUID:88115133; PMID:2828306 !$#accession A28557 !'##molecule_type DNA !'##residues 1-321 ##label NUE !'##cross-references GB:M19025; GB:X04486; NID:g167240; PIDN:AAA33026.1; !1PID:g167241 REFERENCE A25548 !$#authors Fang, G.H.; Kenigsberg, P.; Axley, M.J.; Nuell, M.; Hager, !1L.P. !$#journal Nucleic Acids Res. (1986) 14:8061-8071 !$#title Cloning and sequencing of chloroperoxidase cDNA. !$#cross-references MUID:87040773; PMID:3774552 !$#accession A25548 !'##molecule_type mRNA !'##residues 1-321 ##label FAN !'##cross-references GB:X04486; NID:g2555; PIDN:CAA28172.1; PID:g642215 REFERENCE A25936 !$#authors Axley, M.J.; Kenigsberg, P.; Hager, L.P. !$#journal J. Biol. Chem. (1986) 261:15058-15061 !$#title Fructose induces and glucose represses chloroperoxidase mRNA !1levels. !$#cross-references MUID:87033742; PMID:3771564 !$#accession A25936 !'##molecule_type protein !'##residues 1-176 ##label AXL REFERENCE A60824 !$#authors Kenigsberg, P.; Fang, G.H.; Hager, L.P. !$#journal Arch. Biochem. Biophys. (1987) 254:409-415 !$#title Post-translational modifications of chloroperoxidase from !1Caldariomyces fumago. !$#cross-references MUID:87212023; PMID:2883934 !$#accession A60824 !'##molecule_type protein !'##residues 22-24,'A',26-32,'DD',35-40,'A',42-44,'T' ##label KEN !'##note 25-Ser, 33-Asn, and 34-Asn were also found !'##note two Asn residues, including 34-Asn, and one Gln residue were !1deamidated during isolation; inconsistent numbering of !1sequence positions in this reference make it unclear which !1residues were deamidated !'##note 22-Glu appeared to cyclize to pyrrolidone carboxylic acid !1during isolation REFERENCE A31956 !$#authors Blanke, S.R.; Hager, L.P. !$#journal J. Biol. Chem. (1988) 263:18739-18743 !$#title Identification of the fifth axial heme ligand of !1chloroperoxidase. !$#cross-references MUID:89066662; PMID:3198598 !$#accession A31956 !'##molecule_type protein !'##residues 39-54;91-98,'D',100-113,'V',115-124 ##label BLA CLASSIFICATION #superfamily chloride peroxidase KEYWORDS chromoprotein; extracellular protein; glycoprotein; heme; !1iron; metalloprotein; oxidoreductase FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-321 #product chloride peroxidase #status experimental !8#label MAT\ !$33,237 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$50 #binding_site heme iron (Cys) (axial ligand) #status !8experimental\ !$100-108 #disulfide_bonds #status experimental SUMMARY #length 321 #molecular-weight 35203 #checksum 747 SEQUENCE /// ENTRY OPJGAP #type complete TITLE lignin peroxidase (EC 1.11.1.-) LIPA precursor - basidiomycete (Phanerochaete chrysosporium) ALTERNATE_NAMES ligninase LIPA ORGANISM #formal_name Phanerochaete chrysosporium DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 11-Jun-1999 ACCESSIONS S13563 REFERENCE S13563 !$#authors Gaskell, J.; Dieperink, E.; Cullen, D. !$#journal Nucleic Acids Res. (1991) 19:599-603 !$#title Genomic organization of lignin peroxidase genes of !1Phanerochaete chrysosporium. !$#cross-references MUID:91187681; PMID:2011531 !$#accession S13563 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-372 ##label GAS !'##cross-references EMBL:X54257; NID:g3154; PIDN:CAA38177.1; PID:g3155 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1990 GENETICS !$#gene LIPA !$#introns 21/1; 72/2; 91/2; 163/1; 177/1; 203/2; 344/3; 366/2 CLASSIFICATION #superfamily lignin peroxidase KEYWORDS extracellular protein; glycoprotein; heme; oxidoreductase FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-372 #product lignin peroxidase LIPA #status predicted !8#label MAT\ !$285 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 372 #molecular-weight 39393 #checksum 9297 SEQUENCE /// ENTRY OPJGBP #type complete TITLE lignin peroxidase (EC 1.11.1.-) LIPB precursor - basidiomycete (Phanerochaete chrysosporium) ALTERNATE_NAMES ligninase LIPA ORGANISM #formal_name Phanerochaete chrysosporium DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 11-Jun-1999 ACCESSIONS S13564 REFERENCE S13563 !$#authors Gaskell, J.; Dieperink, E.; Cullen, D. !$#journal Nucleic Acids Res. (1991) 19:599-603 !$#title Genomic organization of lignin peroxidase genes of !1Phanerochaete chrysosporium. !$#cross-references MUID:91187681; PMID:2011531 !$#accession S13564 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-372 ##label GAS !'##cross-references EMBL:X54257; NID:g3154; PIDN:CAA38178.1; PID:g3156 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1990 GENETICS !$#gene LIPB !$#introns 21/1; 72/2; 91/2; 163/1; 177/1; 203/2; 344/3; 366/2 CLASSIFICATION #superfamily lignin peroxidase KEYWORDS extracellular protein; glycoprotein; heme; oxidoreductase FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-372 #product lignin peroxidase LIPB #status predicted !8#label MAT\ !$285 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 372 #molecular-weight 39530 #checksum 9006 SEQUENCE /// ENTRY OPJG3P #type complete TITLE lignin peroxidase (EC 1.11.1.-) GLG3 precursor - basidiomycete (Phanerochaete chrysosporium) ALTERNATE_NAMES ligninase LIPA ORGANISM #formal_name Phanerochaete chrysosporium DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 11-Jun-1999 ACCESSIONS S13723 REFERENCE S13723 !$#authors Naidu, P.S.; Reddy, C.A. !$#journal Nucleic Acids Res. (1990) 18:7173 !$#title Nucleotide sequence of a new lignin peroxidase gene GLG3 !1from the white-rot fungus, Phanerochaete chrysosporium. !$#cross-references MUID:91088334; PMID:2129560 !$#accession S13723 !'##molecule_type DNA !'##residues 1-372 ##label NAI !'##cross-references EMBL:X51590; NID:g3135; PIDN:CAA35939.1; PID:g3136 !'##note the authors translated the codon CAG for residue 5 as Glu GENETICS !$#gene GLG3 !$#introns 21/1; 72/2; 91/2; 163/1; 177/1; 203/2; 344/3; 366/2 CLASSIFICATION #superfamily lignin peroxidase KEYWORDS extracellular protein; glycoprotein; heme; oxidoreductase FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-372 #product lignin peroxidase GLG3 #status predicted !8#label MAT\ !$285 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 372 #molecular-weight 39536 #checksum 8638 SEQUENCE /// ENTRY OPJGG5 #type complete TITLE diarylpropane peroxidase (EC 1.11.1.14) H10 precursor - basidiomycete (Phanerochaete chrysosporium) ALTERNATE_NAMES diarylpropane oxygenase; lignin peroxidase GLG5; ligninase ORGANISM #formal_name Phanerochaete chrysosporium DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 11-Jun-1999 ACCESSIONS JN0117; S13565; B29610; E60995 REFERENCE JN0117 !$#authors Zhang, Y.Z.; Reddy, C.A.; Rasooly, A. !$#journal Gene (1991) 97:191-198 !$#title Cloning of several lignin peroxidase (LIP)-encoding genes: !1sequence analysis of the LIP6 gene from the white-rot !1basidiomycete, Phanerochaete chrysosporium. !$#cross-references MUID:91153647; PMID:1999283 !$#accession JN0117 !'##molecule_type DNA !'##residues 1-371 ##label ZHA !'##cross-references GB:M63496; EMBL:M36815; NID:g169279; !1PIDN:AAA33739.1; PID:g169280 !'##experimental_source strain BKMF1767; ATCC 24725 REFERENCE S13563 !$#authors Gaskell, J.; Dieperink, E.; Cullen, D. !$#journal Nucleic Acids Res. (1991) 19:599-603 !$#title Genomic organization of lignin peroxidase genes of !1Phanerochaete chrysosporium. !$#cross-references MUID:91187681; PMID:2011531 !$#accession S13565 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-371 ##label GAS !'##cross-references GB:X55343; EMBL:X54256; NID:g3137; PIDN:CAA39033.1; !1PID:g3138 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1990 REFERENCE A91587 !$#authors de Boer, H.A.; Zhang, Y.Z.; Collins, C.; Reddy, C.A. !$#journal Gene (1987) 60:93-102 !$#title Analysis of nucleotide sequences of two ligninase cDNAs from !1a white-rot filamentous fungus, Phanerochaete chrysosporium. !$#cross-references MUID:88152506; PMID:3440521 !$#accession B29610 !'##molecule_type mRNA !'##residues 1-371 ##label DEB !'##cross-references GB:M18743 REFERENCE A60995 !$#authors Dass, S.B.; Reddy, C.A. !$#journal FEMS Microbiol. Lett. (1990) 69:221-224 !$#title Characterization of extracellular peroxidases produced by !1acetate-buffered cultures of the lignin-degrading !1basidiomycete Phanerochaete chrysosporium. !$#accession E60995 !'##molecule_type protein !'##residues 28-37 ##label DAS !'##experimental_source ATCC 24725 COMMENT Lignin peroxidases play a key role in the initial !1depolymerization and degradation of lignins. GENETICS !$#gene GLG5; LIP6 !$#introns 21/3; 71/2; 90/1; 161/1; 175/1; 201/2; 243/2; 343/3; 365/2 CLASSIFICATION #superfamily lignin peroxidase KEYWORDS extracellular protein; glycoprotein; heme; oxidoreductase FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-27 #domain propeptide #status predicted #label PRO\ !$28-371 #product lignin peroxidase H10 #status experimental !8#label MAT\ !$283 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 371 #molecular-weight 39417 #checksum 9963 SEQUENCE /// ENTRY OPJGH2 #type complete TITLE diarylpropane peroxidase (EC 1.11.1.14) H2 precursor - basidiomycete (Phanerochaete chrysosporium) ALTERNATE_NAMES lignin peroxidase H2; ligninase H2 ORGANISM #formal_name Phanerochaete chrysosporium DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 11-Jun-1999 ACCESSIONS S06043; A29610; B60995; S08200 REFERENCE S06043 !$#authors Naidu, P.S.; Zhang, Y.Z.; Reddy, C.A. !$#submission submitted to the EMBL Data Library, June 1989 !$#description Characterisation of a gene (LIP2) that encodes lignin !1peroxidase H2 of the white-rot basidiomycete Phanerochaete !1chrysosporium BKMF-1767. !$#accession S06043 !'##molecule_type DNA !'##residues 1-372 ##label NAI !'##cross-references EMBL:X15599; NID:g3152; PIDN:CAA33621.1; PID:g3153 REFERENCE A91587 !$#authors de Boer, H.A.; Zhang, Y.Z.; Collins, C.; Reddy, C.A. !$#journal Gene (1987) 60:93-102 !$#title Analysis of nucleotide sequences of two ligninase cDNAs from !1a white-rot filamentous fungus, Phanerochaete chrysosporium. !$#cross-references MUID:88152506; PMID:3440521 !$#accession A29610 !'##molecule_type mRNA !'##residues 1-311,'I',313-372 ##label DEB !'##cross-references GB:M18743; NID:g169263; PIDN:AAA33733.1; !1PID:g169264 REFERENCE A60995 !$#authors Dass, S.B.; Reddy, C.A. !$#journal FEMS Microbiol. Lett. (1990) 69:221-224 !$#title Characterization of extracellular peroxidases produced by !1acetate-buffered cultures of the lignin-degrading !1basidiomycete Phanerochaete chrysosporium. !$#accession B60995 !'##molecule_type protein !'##residues 29-38 ##label DAS !'##experimental_source ATCC 24725 REFERENCE S08200 !$#authors Glumoff, T.; Harvey, P.J.; Molinari, S.; Goble, M.; Frank, !1G.; Palmer, J.M.; Smit, J.D.G.; Leisola, M.S.A. !$#journal Eur. J. Biochem. (1990) 187:515-520 !$#title Lignin peroxidase from Phanerochaete chrysosporium. !1Molecular and kinetic characterization of isozymes. !$#cross-references MUID:90151655; PMID:2303054 !$#accession S08200 !'##molecule_type protein !'##residues 29-30,'X',32-42,'XX',45-59 ##label GLU GENETICS !$#gene LIP2 !$#introns 73/2; 92/2; 178/1; 204/2; 246/2; 285/1; 343/3; 365/2 CLASSIFICATION #superfamily lignin peroxidase KEYWORDS extracellular protein; glycoprotein; heme; manganese; !1oxidoreductase FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-28 #domain propeptide #status predicted #label PRO\ !$29-372 #product lignin peroxidase #status experimental !8#label MAT\ !$286 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 372 #molecular-weight 39522 #checksum 2080 SEQUENCE /// ENTRY HQECL #type complete TITLE hydrogenase (EC 1.18.99.1) (NiFe) 1 large chain - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS C64838; JV0073 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64838 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-597 ##label BLAT !'##cross-references GB:AE000199; GB:U00096; NID:g1787202; !1PIDN:AAC74058.1; PID:g1787207; UWGP:b0973 !'##experimental_source strain K-12, substrain MG1655 REFERENCE JV0072 !$#authors Menon, N.K.; Robbins, J.; Peck Jr., H.D.; Chatelus, C.Y.; !1Choi, E.S.; Przybyla, A.E. !$#journal J. Bacteriol. (1990) 172:1969-1977 !$#title Cloning and sequencing of a putative Escherichia coli [NiFe] !1hydrogenase-1 operon containing six open reading frames. !$#cross-references MUID:90202716; PMID:2180913 !$#accession JV0073 !'##molecule_type DNA !'##residues 1-51,'I',53-68,'R',70-597 ##label MEN !'##cross-references GB:M34825; NID:g146419; PIDN:AAA23998.1; !1PID:g146421 GENETICS !$#gene hyaB !$#map_position 21 min COMPLEX heterodimer; large and small chain FUNCTION !$#description catalyze reactions involving the production or consumption !1of molecular hydrogen coupled with the oxidation or !1reduction of an electron carrier !$#pathway hydrogen metabolism !$#note contains iron-sulfur and nickel; is one of three E. coli !1hydrogenases synthesized in response to different !1physiological conditions CLASSIFICATION #superfamily hydrogenase (NiFe) large chain KEYWORDS heterodimer; hydrogen metabolism; iron; iron-sulfur protein; !1membrane bound; metalloprotein; nickel; oxidoreductase FEATURE !$76,79,576,579 #binding_site nickel (Cys) #status predicted\ !$79,579 #binding_site iron (Cys) #status predicted\ !$83 #active_site His #status predicted SUMMARY #length 597 #molecular-weight 66253 #checksum 3730 SEQUENCE /// ENTRY HQZJUL #type complete TITLE hydrogenase (EC 1.18.99.1) (uptake) large chain - Bradyrhizobium japonicum ORGANISM #formal_name Bradyrhizobium japonicum DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 11-Jun-1999 ACCESSIONS B31341 REFERENCE A31341 !$#authors Sayavedra-Soto, L.A.; Powell, G.K.; Evans, H.J.; Morris, !1R.O. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:8395-8399 !$#title Nucleotide sequence of the genetic loci encoding subunits of !1Bradyrhizobium japonicum uptake hydrogenase. !$#cross-references MUID:89042190; PMID:3054886 !$#accession B31341 !'##molecule_type DNA !'##residues 1-596 ##label SAY !'##cross-references GB:J04114; NID:g152100; PIDN:AAA26219.1; !1PID:g152102 GENETICS !$#gene hupL COMPLEX heterodimer; large and small chain FUNCTION !$#description catalyzes reactions involving the production or consumption !1of molecular hydrogen coupled to the oxidation or reduction !1of an electron carrier !$#pathway hydrogen metabolism !$#note contains iron-sulfur and nickel; selenium increases the !1hydrogen-uptake activity CLASSIFICATION #superfamily hydrogenase (NiFe) large chain KEYWORDS heterodimer; hydrogen metabolism; iron; iron-sulfur protein; !1membrane bound; metalloprotein; nickel; oxidoreductase FEATURE !$75,78,575,578 #binding_site nickel (Cys) #status predicted\ !$78,578 #binding_site iron (Cys) #status predicted\ !$82 #active_site His #status predicted SUMMARY #length 596 #molecular-weight 65923 #checksum 4243 SEQUENCE /// ENTRY B43255 #type complete TITLE hydrogenase (EC 1.18.99.1) large chain - Alcaligenes eutrophus ORGANISM #formal_name Alcaligenes eutrophus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B43255; S03404 REFERENCE A43255 !$#authors Kortluke, C.; Horstmann, K.; Schwartz, E.; Rohde, M.; !1Binsack, R.; Friedrich, B. !$#journal J. Bacteriol. (1992) 174:6277-6289 !$#title A gene complex coding for the membrane-bound hydrogenase of !1Alcaligenes eutrophus H16. !$#cross-references MUID:93015670; PMID:1383192 !$#accession B43255 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-618 ##label KOR !'##cross-references GB:M96433; NID:g141932; PIDN:AAA16462.1; !1PID:g141934 !'##experimental_source strain H16, megaplasmid pHG1 !'##note sequence extracted from NCBI backbone (NCBIP:115451) REFERENCE S03404 !$#authors Lorenz, B.; Schneider, K.; Kratzin, H.; Schlegel, H.G. !$#journal Biochim. Biophys. Acta (1989) 995:1-9 !$#title Immunological comparison of subunits isolated from various !1hydrogenases of aerobic hydrogen bacteria. !$#cross-references MUID:89166625; PMID:2493816 !$#accession S03404 !'##molecule_type protein !'##residues 2-31 ##label LOR GENETICS !$#gene hoxG CLASSIFICATION #superfamily hydrogenase (NiFe) large chain KEYWORDS hydrogen metabolism; iron; iron-sulfur protein; membrane !1bound; metalloprotein; nickel; oxidoreductase FEATURE !$75,78,597,600 #binding_site nickel (Cys) #status predicted\ !$78,600 #binding_site iron (Cys) #status predicted\ !$82 #active_site His #status predicted SUMMARY #length 618 #molecular-weight 68763 #checksum 1458 SEQUENCE /// ENTRY JH0776 #type complete TITLE hydrogenase (EC 1.18.99.1) large chain - Alcaligenes hydrogenophilus ORGANISM #formal_name Alcaligenes hydrogenophilus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JH0776 REFERENCE JH0775 !$#authors Yagi, K.; Seto, T.; Terakado, M.; Umeda, F.; Doi, T.; !1Imanishi, T.; Miura, Y. !$#journal Chem. Pharm. Bull. (1992) 40:3292-3296 !$#title Nucleotide sequences of membrane-bound hydrogenase gene in !1Alcaligenes hydrogenophilus. !$#cross-references MUID:93193199; PMID:1294332 !$#accession JH0776 !'##molecule_type DNA !'##residues 1-619 ##label YAG !'##cross-references GB:S56898; NID:g299291; PIDN:AAB25780.1; !1PID:g299293 GENETICS !$#gene hupL FUNCTION !$#pathway hydrogen metabolism !$#note contains iron-sulfur and nickel CLASSIFICATION #superfamily hydrogenase (NiFe) large chain KEYWORDS hydrogen metabolism; iron; iron-sulfur protein; membrane !1bound; metalloprotein; nickel; oxidoreductase FEATURE !$75,78,603 #binding_site nickel (Cys) #status predicted\ !$78,603 #binding_site iron (Cys) #status predicted\ !$82 #active_site His #status predicted SUMMARY #length 619 #molecular-weight 68531 #checksum 702 SEQUENCE /// ENTRY JQ0806 #type complete TITLE hydrogenase (EC 1.18.99.1) (NiFe) large chain precursor - Azotobacter vinelandii ALTERNATE_NAMES hydrogenlyase; [NiFe]hydrogenase ORGANISM #formal_name Azotobacter vinelandii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JQ0806; S29200 REFERENCE JQ0805 !$#authors Menon, A.L.; Stults, L.W.; Robson, R.L.; Mortenson, L.E. !$#journal Gene (1990) 96:67-74 !$#title Cloning, sequencing and characterization of the [NiFe] !1hydrogenase-encoding structural genes (hoxK and hoxG) from !1Azotobacter vinelandii. !$#cross-references MUID:91092503; PMID:2265761 !$#accession JQ0806 !'##molecule_type DNA !'##residues 1-602 ##label MEN !'##cross-references GB:M33152; NID:g142310; PIDN:AAA82506.1; !1PID:g142312 !'##experimental_source strain OP !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE S29200 !$#authors Gollin, D.J.; Mortenson, L.E.; Robson, R.L. !$#journal FEBS Lett. (1992) 309:371-375 !$#title Carboxyl-terminal processing may be essential for production !1of active NiFe hydrogenase in Azotobacter vinelandii. !$#cross-references MUID:92387391; PMID:1516712 !$#accession S29200 !'##status preliminary !'##molecule_type protein !'##residues 581-602 ##label GOL !'##note hydrogenases purified from nitrogen-fixing microorganisms are !1membrane-bound NiFe-sulfur proteins GENETICS !$#gene hoxG COMPLEX heterodimer; large and small chain FUNCTION !$#pathway hydrogen metabolism !$#note contains iron-sulfur and nickel CLASSIFICATION #superfamily hydrogenase (NiFe) large chain KEYWORDS heterodimer; hydrogen metabolism; iron; iron-sulfur protein; !1membrane bound; metalloprotein; nickel; oxidoreductase FEATURE !$2-602 #product hydrogenase large chain #status experimental !8#label HLH\ !$74,77,581,584 #binding_site nickel (Cys) #status predicted\ !$77,584 #binding_site iron (Cys) #status predicted\ !$81 #active_site His #status predicted SUMMARY #length 602 #molecular-weight 66736 #checksum 9366 SEQUENCE /// ENTRY S11969 #type complete TITLE hydrogenase (EC 1.18.99.1) (uptake) large chain - Rhizobium leguminosarum ORGANISM #formal_name Rhizobium leguminosarum DATE 13-Jan-1995 #sequence_revision 10-May-1996 #text_change 11-Jun-1999 ACCESSIONS S11969; S11278 REFERENCE S11968 !$#authors Hidalgo, E.; Leyva, A.; Ruiz-Argueeso, T. !$#journal Plant Mol. Biol. (1990) 15:367-370 !$#title Nucleotide sequence of the hydrogenase structural genes from !1Rhizobium leguminosarum. !$#cross-references MUID:91355885; PMID:2103457 !$#accession S11969 !'##status preliminary !'##molecule_type DNA !'##residues 1-596 ##label HID !'##cross-references EMBL:X52974; NID:g1167855; PIDN:CAA37149.1; !1PID:g48722 !'##experimental_source strain UPM791 REFERENCE S11277 !$#authors Schneider, C.G.; Schmitt, H.J.; Schild, C.; Tichy, H.V.; !1Lotz, W. !$#journal Nucleic Acids Res. (1990) 18:5285 !$#title DNA sequence encoding the two structural genes for the !1uptake hydrogenase of Rhizobium leguminosarum bv. viciae !1B10. !$#cross-references MUID:90384836; PMID:2402452 !$#accession S11278 !'##status preliminary; translation not shown !'##molecule_type DNA !'##residues 1-509,'R',511-596 ##label SCH !'##cross-references GB:Z36981; EMBL:X53781; NID:g2058351; !1PIDN:CAA85431.1; PID:g536799 !'##experimental_source strain B10 GENETICS !$#gene hupL COMPLEX heterodimer; large and small chain FUNCTION !$#pathway hydrogen metabolism !$#note contains iron-sulfur and nickel CLASSIFICATION #superfamily hydrogenase (NiFe) large chain KEYWORDS heterodimer; hydrogen metabolism; iron; iron-sulfur protein; !1membrane bound; metalloprotein; nickel; oxidoreductase FEATURE !$75,78,575,578 #binding_site nickel (Cys) #status predicted\ !$78,578 #binding_site iron (Cys) #status predicted\ !$82 #active_site His #status predicted SUMMARY #length 596 #molecular-weight 66108 #checksum 2724 SEQUENCE /// ENTRY S11777 #type complete TITLE hydrogenase (EC 1.18.99.1) (uptake) large chain - Azotobacter chroococcum ORGANISM #formal_name Azotobacter chroococcum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S11777 REFERENCE S11776 !$#authors Ford, C.M.; Garg, N.; Garg, R.P.; Tibelius, K.H.; Yates, !1M.G.; Arp, D.J.; Seefeldt, L.C. !$#journal Mol. Microbiol. (1990) 4:999-1008 !$#title The identification, characterization, sequencing and !1mutagenesis of the genes (hupSL) encoding the small and !1large subunits of the H(2)-uptake hydrogenase of Azotobacter !1chroococcum. !$#cross-references MUID:91014699; PMID:2215219 !$#accession S11777 !'##molecule_type DNA !'##residues 1-601 ##label FOR !'##cross-references EMBL:X52961; NID:g38713; PIDN:CAA37134.1; !1PID:g38717 GENETICS !$#gene hupL FUNCTION !$#pathway hydrogen metabolism !$#note contains iron-sulfur and nickel CLASSIFICATION #superfamily hydrogenase (NiFe) large chain KEYWORDS hydrogen metabolism; iron; iron-sulfur protein; membrane !1bound; metalloprotein; nickel; oxidoreductase FEATURE !$74,77,580,583 #binding_site nickel (Cys) #status predicted\ !$77,583 #binding_site iron (Cys) #status predicted SUMMARY #length 601 #molecular-weight 66432 #checksum 7870 SEQUENCE /// ENTRY HQDVLB #type complete TITLE cytochrome-c3 hydrogenase (EC 1.12.2.1) (NiFeSe) large chain - Desulfovibrio baculatus ORGANISM #formal_name Desulfovibrio baculatus DATE 31-Dec-1990 #sequence_revision 31-Dec-1992 #text_change 30-Apr-1999 ACCESSIONS A33101; B28380 REFERENCE A33101 !$#authors Menon, N.K.; Peck Jr., H.D.; Le Gall, J.; Przybyla, A.E. !$#journal J. Bacteriol. (1988) 170:4429 !$#contents erratum !$#accession A33101 !'##molecule_type DNA !'##residues 1-514 ##label MEN !'##cross-references GB:M18271; GB:M22139 REFERENCE A28380 !$#authors Menon, N.K.; Peck Jr., H.D.; Le Gall, J.; Przybyla, A.E. !$#journal J. Bacteriol. (1987) 169:5401-5407 !$#title Cloning and sequencing of the genes encoding the large and !1small subunits of the periplasmic (NiFeSe) hydrogenase of !1Desulfovibrio baculatus. !$#cross-references MUID:88058744; PMID:3316183 !$#contents annotation !$#note this sequence has been extensively revised COMMENT Hydrogenases catalyze reactions involving the production or !1consumption of molecular hydrogen coupled with the oxidation !1or reduction of an electron carrier. Three distinctive !1types, the Fe, NiFe, and NiFeSe hydrogenases, are found in !1the periplasm of sulfate-reducing bacteria. COMMENT The active NiFeSe hydrogenase is a dimer of large and small !1chains, having two [4Fe-4S] clusters, one redox-active Ni !1center, and one selenocysteine. GENETICS !$#start_codon GTG CLASSIFICATION #superfamily hydrogenase (NiFe) large chain KEYWORDS heterodimer; hydrogen metabolism; iron; iron-sulfur protein; !1metalloprotein; nickel; oxidoreductase; periplasmic space; !1selenocysteine FEATURE !$71,74,493,496 #binding_site nickel (Cys) #status predicted\ !$74,496 #binding_site iron (Cys) #status predicted\ !$78 #active_site His #status predicted\ !$493 #modified_site selenocysteine #status predicted SUMMARY #length 514 #molecular-weight 56830 #checksum 8559 SEQUENCE /// ENTRY HQDVLG #type complete TITLE cytochrome-c3 hydrogenase (EC 1.12.2.1) (NiFe) large chain precursor [validated] - Desulfovibrio gigas ALTERNATE_NAMES hydrogenlyase ORGANISM #formal_name Desulfovibrio gigas DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 15-Sep-2000 ACCESSIONS B32315; B27492; S36904; A60485; D27480 REFERENCE A32315 !$#authors Voordouw, G.; Menon, N.K.; LeGall, J.; Choi, E.S.; Peck Jr., !1H.D.; Przybyla, A.E. !$#journal J. Bacteriol. (1989) 171:2894-2899 !$#title Analysis and comparison of nucleotide sequences encoding the !1genes for [NiFe] and [NiFeSe] hydrogenases from !1Desulfovibrio gigas and Desulfovibrio baculatus. !$#cross-references MUID:89213989; PMID:2651421 !$#contents corrections !$#accession B32315 !'##molecule_type DNA !'##residues 1-551 ##label VOO REFERENCE A27492 !$#authors Li, C.; Peck Jr., H.D.; LeGall, J.; Przybyla, A.E. !$#journal DNA (1987) 6:539-551 !$#title Cloning, characterization, and sequencing of the genes !1encoding the large and small subunits of the periplasmic !1[NiFe]hydrogenase of Desulfovibrio gigas. !$#cross-references MUID:88111028; PMID:3322743 !$#accession B27492 !'##status significant sequence differences !'##molecule_type DNA !'##cross-references EMBL:M18083 !'##note this sequence has been extensively revised in B32315 REFERENCE S36904 !$#authors Menon, N.K.; Robbins, J.; der Vartanian, M.; Patil, D.; Peck !1Jr., H.D.; Menon, A.L.; Robson, R.L.; Przybyla, A.E. !$#journal FEBS Lett. (1993) 331:91-95 !$#title Carboxy-terminal processing of the large subunit of [NiFe] !1hydrogenases. !$#cross-references MUID:94009654; PMID:8405419 !$#accession S36904 !'##status preliminary !'##molecule_type protein !'##residues 523-536 ##label MEN REFERENCE A60485 !$#authors Niviere, V.; Forget, N.; Bovier-Lapierre, G.; Bonicel, J.; !1Hatchikian, C. !$#journal Biochimie (1988) 70:267-271 !$#title Isolation, amino acid analysis and N-terminal sequence !1determination of the two subunits of the nickel-containing !1hydrogenase of Desulfovibrio gigas. !$#cross-references MUID:88281536; PMID:3134950 !$#accession A60485 !'##molecule_type protein !'##residues 2-19,'P',21 ##label NIV REFERENCE A27480 !$#authors Prickril, B.C.; He, S.H.; Li, C.; Menon, N.; Choi, E.S.; !1Przybyla, A.E.; DerVartanian, D.V.; Peck Jr., H.D.; Fauque, !1G.; LeGall, J.; Teixeira, M.; Moura, I.; Moura, J.J.G.; !1Patil, D.; Huynh, B.H. !$#journal Biochem. Biophys. Res. Commun. (1987) 149:369-377 !$#title Identification of three classes of hydrogenase in the genus, !1Desulfovibrio. !$#cross-references MUID:88106446; PMID:3322275 !$#accession D27480 !'##molecule_type protein !'##residues 2-30 ##label PRI REFERENCE A65633 !$#authors Volbeda, A.; Frey, M.; Fontecilla-Camps, J.C. !$#submission submitted to the Brookhaven Protein Data Bank, March 1996 !$#cross-references PDB:1FRV !$#contents annotation; X-ray crystallography, 2.85 angstroms, residues !17-536 REFERENCE A57765 !$#authors Volbeda, A.; Charon, M.H.; Piras, C.; Hatchikian, E.C.; !1Frey, M.; Fontecilla-Camps, J.C. !$#journal Nature (1995) 373:580-587 !$#title Crystal structure of the nickel-iron hydrogenase from !1Desulfovibrio gigas. !$#cross-references MUID:95157629; PMID:7854413 !$#contents annotation; X-ray crystallography, 2.85 angstroms COMMENT Three distinct types of hydrogenases, the Fe, NiFe, and !1NiFeSe, are found in the periplasm of sulfate-reducing !1bacteria. COMMENT The complex contains two [4Fe-4S] clusters, one [3Fe-4S] !1cluster, and one redox-active Ni center. COMMENT Evidence suggests that a second metal ion, possibly iron, !1may be bound near the nickel binding site. COMPLEX heterodimer of large and small chains (see PIR:HQDVSG) FUNCTION !$#description catalyze reactions involving the production or consumption !1of molecular hydrogen coupled with the oxidation or !1reduction of an electron carrier CLASSIFICATION #superfamily hydrogenase (NiFe) large chain KEYWORDS heterodimer; hydrogen metabolism; iron; iron-sulfur protein; !1metalloprotein; nickel; oxidoreductase; periplasmic space FEATURE !$2-536 #product hydrogenase (NiFe) large chain #status !8experimental #label MAT\ !$537-551 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$65,68,530,533 #binding_site nickel (Cys) #status experimental\ !$68,533 #binding_site iron (Cys) #status predicted\ !$72 #active_site His #status predicted SUMMARY #length 551 #molecular-weight 61480 #checksum 7212 SEQUENCE /// ENTRY B45865 #type complete TITLE cytochrome-c3 hydrogenase (EC 1.12.2.1) (NiFe) large chain - Desulfovibrio vulgaris (strain Miyazaki) ORGANISM #formal_name Desulfovibrio vulgaris DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Dec-1999 ACCESSIONS B45865 REFERENCE A45865 !$#authors Deckers, H.M.; Wilson, F.R.; Voordouw, G. !$#journal J. Gen. Microbiol. (1990) 136:2021-2028 !$#title Cloning and sequencing of a [NiFe] hydrogenase operon from !1Desulfovibrio vulgaris Miyazaki F. !$#cross-references MUID:91100954; PMID:2269874 !$#accession B45865 !'##status preliminary !'##molecule_type DNA !'##residues 1-567 ##label DEC !'##cross-references GB:M58339; GB:M33174; NID:g145092; PIDN:AAA23370.1; !1PID:g145094 CLASSIFICATION #superfamily hydrogenase (NiFe) large chain KEYWORDS iron; metalloprotein; nickel; oxidoreductase FEATURE !$81,84,546,549 #binding_site nickel (Cys) #status predicted\ !$84,549 #binding_site iron (Cys) #status predicted\ !$88 #active_site His #status predicted SUMMARY #length 567 #molecular-weight 62626 #checksum 3925 SEQUENCE /// ENTRY C55516 #type complete TITLE hydrogenase (EC 1.18.99.1) 2 large chain - Escherichia coli (strain K-12) ALTERNATE_NAMES hybC protein ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS C55516; H65085 REFERENCE A55516 !$#authors Menon, N.K.; Chatelus, C.Y.; Dervartanian, M.; Wendt, J.C.; !1Shanmugam, K.T.; Peck Jr., H.D.; Przybyla, A.E. !$#journal J. Bacteriol. (1994) 176:4416-4423 !$#title Cloning, sequencing, and mutational analysis of the hyb !1operon encoding Escherichia coli hydrogenase 2. !$#cross-references MUID:94292472; PMID:8021226 !$#accession C55516 !'##status preliminary !'##molecule_type DNA !'##residues 1-567 ##label MEN !'##cross-references GB:U09177; NID:g501051; PIDN:AAA21591.1; !1PID:g544485 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65085 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-567 ##label BLAT !'##cross-references GB:AE000382; GB:U00096; NID:g2367182; !1PIDN:AAC76030.1; PID:g1789368; UWGP:b2994 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene hybC CLASSIFICATION #superfamily hydrogenase (NiFe) large chain KEYWORDS iron; metalloprotein; nickel; oxidoreductase FEATURE !$61,64,546,549 #binding_site nickel (Cys) #status predicted\ !$64,549 #binding_site iron (Cys) #status predicted\ !$68 #active_site His #status predicted SUMMARY #length 567 #molecular-weight 62491 #checksum 1991 SEQUENCE /// ENTRY S33853 #type complete TITLE hydrogenase (EC 1.18.99.1) (NiFe) hydB - Wolinella succinogenes ORGANISM #formal_name Wolinella succinogenes DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S33853; S22405; S33064 REFERENCE S33852 !$#authors Dross, F.; Geisler, V.; Lenger, R.; Theis, F.; Krafft, T.; !1Fahrenholz, F.; Kojro, E.; Duchene, A.; Tripier, D.; !1Juvenal, K.; Kroeger, A. !$#journal Eur. J. Biochem. (1993) 214:949-950 !$#title Correction. The quinone-reactive Ni/Fe-hydrogenase of !1Wolinella succinogenes. !$#cross-references MUID:93307313; PMID:8319698 !$#accession S33853 !'##molecule_type DNA !'##residues 1-576 ##label DRO !'##cross-references EMBL:X65189; NID:g296081; PIDN:CAA46303.1; !1PID:g1333732 !'##note this is a revision to the sequence from reference S22405 REFERENCE S22404 !$#authors Dross, F.; Geisler, V.; Lenger, R.; Theis, F.; Krafft, T.; !1Fahrenholz, F.; Kojro, E.; Duchene, A.; Tripier, D.; !1Juvenal, K.; Kroeger, A. !$#journal Eur. J. Biochem. (1992) 206:93-102 !$#title The quinone-reactive Ni/Fe-hydrogenase of Wolinella !1succinogenes. !$#cross-references MUID:92267032; PMID:1587288 !$#accession S22405 !'##molecule_type DNA !'##residues 1-68,'TT',71,'QE',75,'VPWKT',81-82,'NQTS',87-250,'A', !1252-256,'R',258-525,'HEVARSFSAF',539,'DHP',543,'DSL',544-576 !1##label DRW !'##cross-references EMBL:X65189 !'##note this sequence has been revised in reference S33853 GENETICS !$#gene hydB CLASSIFICATION #superfamily hydrogenase (NiFe) large chain KEYWORDS iron; metalloprotein; nickel; oxidoreductase FEATURE !$62,65,547,550 #binding_site nickel (Cys) #status predicted\ !$65,550 #binding_site iron (Cys) #status predicted\ !$69 #active_site His #status predicted SUMMARY #length 576 #molecular-weight 63977 #checksum 490 SEQUENCE /// ENTRY HQDVLV #type complete TITLE cytochrome-c3 hydrogenase (EC 1.12.2.1) (Fe) large chain - Desulfovibrio vulgaris subsp. oxamicus ALTERNATE_NAMES hydrogenase (Fe) alpha chain ORGANISM #formal_name Desulfovibrio vulgaris subsp. oxamicus DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 05-May-2000 ACCESSIONS A32886 REFERENCE A32886 !$#authors Voordouw, G.; Strang, J.D.; Wilson, F.R. !$#journal J. Bacteriol. (1989) 171:3881-3889 !$#title Organization of the genes encoding [Fe] hydrogenase in !1Desulfovibrio vulgaris subsp. oxamicus Monticello. !$#cross-references MUID:89291738; PMID:2661538 !$#accession A32886 !'##molecule_type DNA !'##residues 1-421 ##label VOO !'##cross-references GB:M27212; NID:g145098; PIDN:AAA23373.1; !1PID:g145099 COMMENT Hydrogenases catalyze reactions involving the production or !1consumption of molecular hydrogen coupled with the oxidation !1or reduction of an electron carrier. Three distinctive !1types, the Fe, NiFe, and NiFeSe hydrogenases, are found in !1the periplasm of sulfate-reducing bacteria. COMMENT The active D. vulgaris hydrogenase (Fe) is a dimer of large !1(alpha) and small (beta) chains, binding three [4Fe-4S] !1iron-sulfur clusters. It may be involved in hydrogen uptake !1for the reduction of sulfate to hydrogen sulfide in an !1electron transport chain. Cytochrome c3 is likely to be the !1physiological electron carrier for the enzyme. GENETICS !$#gene hydA CLASSIFICATION #superfamily hydrogenase (Fe) large chain; ferredoxin !12[4Fe-4S] homology KEYWORDS 4Fe-4S; hydrogen metabolism; iron-sulfur protein; !1metalloprotein; oxidoreductase; periplasmic space FEATURE !$28-84 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$35,38,41,76 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$45,66,69,72 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$382 #binding_site diiron cofactor (Cys) #status predicted SUMMARY #length 421 #molecular-weight 46278 #checksum 9948 SEQUENCE /// ENTRY HQDVFL #type complete TITLE cytochrome-c3 hydrogenase (EC 1.12.2.1) (Fe) large chain - Desulfovibrio vulgaris (strain Hildenborough) ALTERNATE_NAMES hydrogenase (Fe) alpha chain ORGANISM #formal_name Desulfovibrio vulgaris DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 05-May-2000 ACCESSIONS A24551; B27480 REFERENCE A24551 !$#authors Voordouw, G.; Brenner, S. !$#journal Eur. J. Biochem. (1985) 148:515-520 !$#title Nucleotide sequence of the gene encoding the hydrogenase !1from Desulfovibrio vulgaris (Hildenborough). !$#cross-references MUID:85203856; PMID:3888621 !$#accession A24551 !'##molecule_type DNA !'##residues 1-421 ##label VOO !'##cross-references GB:X02416; NID:g40829; PIDN:CAA26266.1; PID:g40830 REFERENCE A27480 !$#authors Prickril, B.C.; He, S.H.; Li, C.; Menon, N.; Choi, E.S.; !1Przybyla, A.E.; DerVartanian, D.V.; Peck Jr., H.D.; Fauque, !1G.; LeGall, J.; Teixeira, M.; Moura, I.; Moura, J.J.G.; !1Patil, D.; Huynh, B.H. !$#journal Biochem. Biophys. Res. Commun. (1987) 149:369-377 !$#title Identification of three classes of hydrogenase in the genus, !1Desulfovibrio. !$#cross-references MUID:88106446; PMID:3322275 !$#accession B27480 !'##molecule_type protein !'##residues 1-34,'K' ##label PRI COMMENT Hydrogenases catalyze reactions involving the production or !1consumption of molecular hydrogen coupled with the oxidation !1or reduction of an electron carrier. Three distinctive !1types, the Fe, NiFe, and NiFeSe hydrogenases, are found in !1the periplasm of sulfate-reducing bacteria. COMMENT The active D. vulgaris hydrogenase (Fe) is a dimer of large !1(alpha) and small (beta) chains, binding three [4Fe-4S] !1iron-sulfur clusters. It may be involved in hydrogen uptake !1for the reduction of sulfate to hydrogen sulfide in an !1electron transport chain. Cytochrome c3 is likely to be the !1physiological electron carrier for the enzyme. GENETICS !$#gene hydA CLASSIFICATION #superfamily hydrogenase (Fe) large chain; ferredoxin !12[4Fe-4S] homology KEYWORDS 4Fe-4S; hydrogen metabolism; iron-sulfur protein; !1metalloprotein; oxidoreductase; periplasmic space FEATURE !$28-84 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$35,38,41,76 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$45,66,69,72 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$382 #binding_site diiron cofactor (Cys) #status predicted SUMMARY #length 421 #molecular-weight 45951 #checksum 9186 SEQUENCE /// ENTRY HQCL1P #type complete TITLE hydrogenase (EC 1.18.99.1) (Fe) I, periplasmic [validated] - Clostridium pasteurianum ALTERNATE_NAMES [Fe] hydrogenase ORGANISM #formal_name Clostridium pasteurianum DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 15-Sep-2000 ACCESSIONS A40330 REFERENCE A40330 !$#authors Meyer, J.; Gagnon, J. !$#journal Biochemistry (1991) 30:9697-9704 !$#title Primary structure of hydrogenase I from Clostridium !1pasteurianum. !$#cross-references MUID:92002005; PMID:1911757 !$#accession A40330 !'##molecule_type DNA !'##residues 1-574 ##label MEY !'##cross-references GB:M81737; GB:M62754; NID:g144835; PIDN:AAA23248.1; !1PID:g144836 REFERENCE A59203 !$#authors Peters, J.W.; Lanzilotta, W.N.; Lemon, B.J.; Seefeldt, L.C. !$#journal Science (1998) 282:1853-1858 !$#title X-ray crystal structure of the Fe-only hydrogenase (CpI) !1from Clostridium pasteurianum to 1.8 angstrom resolution. !$#cross-references MUID:99055388; PMID:9836629 !$#contents annotation; X-ray crystallography, 1.80 angstroms REFERENCE A77988 !$#authors Peters, J.W.; Lanzilotta, W.N.; Lemon, B.J.; Seefeldt, L.C. !$#submission submitted to the Protein Data Bank, October 1998 !$#cross-references PDB:1FEH !$#contents annotation; X-ray crystallography, 1.80 angstroms, residues !11-574 COMMENT Three distinct hydrogenases, the Fe, NiFe, and NiFeSe !1hydrogenases, have been found in the periplasm of !1sulfate-reducing bacteria. In C. pasteurianum there are two !1Fe hydrogenases (I and II), each consisting of a single !1polypeptide chain. FUNCTION !$#description catalyzes the reduction of two protons to molecular hydrogen !1by reduced ferredoxin CLASSIFICATION #superfamily hydrogenase (Fe) large chain; ferredoxin !12[4Fe-4S] homology KEYWORDS 2Fe-2S; 4Fe-4S; hydrogen metabolism; iron-sulfur protein; !1metalloprotein; oxidoreductase; periplasmic space FEATURE !$140-208 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$34,46,49,62 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8experimental\ !$94,98,101,107 #binding_site 4Fe-4S cluster (His, Cys, Cys, Cys) !8(covalent) (type N1) #status experimental\ !$147,150,153,200 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8experimental\ !$157,190,193,196 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8experimental\ !$300,355,499,503 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8experimental\ !$503 #binding_site diiron cofactor (Cys) #status !8experimental SUMMARY #length 574 #molecular-weight 63828 #checksum 1439 SEQUENCE /// ENTRY A35385 #type complete TITLE hydrogen dehydrogenase (EC 1.12.1.2) alpha chain - Alcaligenes eutrophus ALTERNATE_NAMES NAD-linked hydrogenase alpha chain ORGANISM #formal_name Alcaligenes eutrophus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 20-Oct-2000 ACCESSIONS A35385; S03942 REFERENCE A35385 !$#authors Tran-Betcke, A.; Warnecke, U.; Boecker, C.; Zaborosch, C.; !1Friedrich, B. !$#journal J. Bacteriol. (1990) 172:2920-2929 !$#title Cloning and nucleotide sequences of the genes for the !1subunits of NAD-reducing hydrogenase of Alcaligenes !1eutrophus H16. !$#cross-references MUID:90264277; PMID:2188945 !$#accession A35385 !'##status preliminary !'##molecule_type DNA !'##residues 1-602 ##label TRA !'##cross-references GB:M55230; NID:g141946; PIDN:AAC06140.1; !1PID:g141947; GB:M37904 REFERENCE S03941 !$#authors Zaborosch, C.; Schneider, K.; Schlegel, H.G.; Kratzin, H. !$#journal Eur. J. Biochem. (1989) 181:175-180 !$#title Comparison of the NH(2)-terminal amino acid sequences of the !1four non-identical subunits of the NAD-linked hydrogenases !1from Nocardia opaca 1b and Alcaligenes eutrophus H16. !$#cross-references MUID:89231684; PMID:2496982 !$#accession S03942 !'##molecule_type protein !'##residues 1-23,'G',25-27 ##label ZAB CLASSIFICATION #superfamily hydrogen dehydrogenase alpha chain; NADH !1dehydrogenase (ubiquinone) I chain E homology; NADH !1dehydrogenase (ubiquinone) I chain F homology KEYWORDS cytosol; oxidoreductase FEATURE !$9-148 #domain NADH dehydrogenase (ubiquinone) I chain E !8homology #label NUOE\ !$201-567 #domain NADH dehydrogenase (ubiquinone) I chain F !8homology #label NUOF SUMMARY #length 602 #molecular-weight 66783 #checksum 7727 SEQUENCE /// ENTRY B35385 #type complete TITLE hydrogen dehydrogenase (EC 1.12.1.2) gamma chain - Alcaligenes eutrophus ALTERNATE_NAMES NAD-linked hydrogenase gamma chain ORGANISM #formal_name Alcaligenes eutrophus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B35385; S03946 REFERENCE A35385 !$#authors Tran-Betcke, A.; Warnecke, U.; Boecker, C.; Zaborosch, C.; !1Friedrich, B. !$#journal J. Bacteriol. (1990) 172:2920-2929 !$#title Cloning and nucleotide sequences of the genes for the !1subunits of NAD-reducing hydrogenase of Alcaligenes !1eutrophus H16. !$#cross-references MUID:90264277; PMID:2188945 !$#accession B35385 !'##status preliminary !'##molecule_type DNA !'##residues 1-234 ##label TRA !'##cross-references GB:M55230; NID:g141946; PIDN:AAC06141.1; !1PID:g141948; GB:M37904 REFERENCE S03941 !$#authors Zaborosch, C.; Schneider, K.; Schlegel, H.G.; Kratzin, H. !$#journal Eur. J. Biochem. (1989) 181:175-180 !$#title Comparison of the NH(2)-terminal amino acid sequences of the !1four non-identical subunits of the NAD-linked hydrogenases !1from Nocardia opaca 1b and Alcaligenes eutrophus H16. !$#cross-references MUID:89231684; PMID:2496982 !$#accession S03946 !'##molecule_type protein !'##residues 2-26 ##label ZAB CLASSIFICATION #superfamily hydrogen dehydrogenase gamma chain; ferredoxin !12[4Fe-4S] homology KEYWORDS oxidoreductase SUMMARY #length 234 #molecular-weight 26173 #checksum 4336 SEQUENCE /// ENTRY HQECSN #type complete TITLE hydrogenase (EC 1.18.99.1) (NiFe) 1 small chain precursor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 01-Mar-2002 ACCESSIONS JV0072; B64838 REFERENCE JV0072 !$#authors Menon, N.K.; Robbins, J.; Peck Jr., H.D.; Chatelus, C.Y.; !1Choi, E.S.; Przybyla, A.E. !$#journal J. Bacteriol. (1990) 172:1969-1977 !$#title Cloning and sequencing of a putative Escherichia coli [NiFe] !1hydrogenase-1 operon containing six open reading frames. !$#cross-references MUID:90202716; PMID:2180913 !$#accession JV0072 !'##molecule_type DNA !'##residues 1-372 ##label MEN !'##cross-references GB:M18271; GB:M22139 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64838 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-372 ##label BLAT !'##cross-references GB:AE000199; GB:U00096; NID:g1787202; !1PIDN:AAC74057.1; PID:g1787206; UWGP:b0972 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene hyaA !$#map_position 21 min COMPLEX heterodimer; large and small chain FUNCTION !$#description catalyze reactions involving the production or consumption !1of molecular hydrogen coupled with the oxidation or !1reduction of an electron carrier !$#pathway hydrogen metabolism !$#note contains iron-sulfur and nickel; is one of three E. coli !1hydrogenases synthesized in response to different !1physiological conditions CLASSIFICATION #superfamily hydrogenase (NiFe) small chain KEYWORDS 3Fe-4S; 4Fe-4S; heterodimer; hydrogen metabolism; !1iron-sulfur protein; membrane bound; metalloprotein; nickel; !1oxidoreductase FEATURE !$1-45 #domain signal sequence #status predicted #label SIG\ !$46-372 #product hydrogenase (NiFe) small chain #status !8predicted #label MAT\ !$62,65,160,194 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$232,235,260,266 #binding_site 4Fe-4S cluster (His, Cys, Cys, Cys) !8(covalent) (type N3) #status predicted\ !$275,294,297 #binding_site 3Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 372 #molecular-weight 40681 #checksum 8477 SEQUENCE /// ENTRY HQZJUS #type complete TITLE hydrogenase (EC 1.18.99.1) (uptake) small chain precursor - Bradyrhizobium japonicum ORGANISM #formal_name Bradyrhizobium japonicum DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 20-Apr-2000 ACCESSIONS A31341 REFERENCE A31341 !$#authors Sayavedra-Soto, L.A.; Powell, G.K.; Evans, H.J.; Morris, !1R.O. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:8395-8399 !$#title Nucleotide sequence of the genetic loci encoding subunits of !1Bradyrhizobium japonicum uptake hydrogenase. !$#cross-references MUID:89042190; PMID:3054886 !$#accession A31341 !'##molecule_type DNA !'##residues 1-363 ##label SAY !'##cross-references GB:J04114; NID:g152100; PIDN:AAA26218.1; !1PID:g152101 GENETICS !$#gene hupS FUNCTION !$#description catalyze reactions involving the production or consumption !1of molecular hydrogen coupled with the oxidation or !1reduction of an electron carrier !$#pathway hydrogen metabolism !$#note contains iron-sulfur and nickel; selenium increases the !1hydrogen-uptake activity CLASSIFICATION #superfamily hydrogenase (NiFe) small chain KEYWORDS 3Fe-4S; 4Fe-4S; heterodimer; hydrogen metabolism; !1iron-sulfur protein; membrane bound; metalloprotein; nickel; !1oxidoreductase FEATURE !$1-46 #domain signal sequence #status predicted #label SIG\ !$47-363 #product hydrogenase (uptake) small chain #status !8predicted #label MAT\ !$63,66,161,195 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$233,236,261,267 #binding_site 4Fe-4S cluster (His, Cys, Cys, Cys) !8(covalent) (type N3) #status predicted\ !$276,295,298 #binding_site 3Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 363 #molecular-weight 39446 #checksum 1726 SEQUENCE /// ENTRY S11776 #type complete TITLE hydrogenase (EC 1.18.99.1) (uptake) small chain precursor - Azotobacter chroococcum ORGANISM #formal_name Azotobacter chroococcum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 20-Apr-2000 ACCESSIONS S11776 REFERENCE S11776 !$#authors Ford, C.M.; Garg, N.; Garg, R.P.; Tibelius, K.H.; Yates, !1M.G.; Arp, D.J.; Seefeldt, L.C. !$#journal Mol. Microbiol. (1990) 4:999-1008 !$#title The identification, characterization, sequencing and !1mutagenesis of the genes (hupSL) encoding the small and !1large subunits of the H(2)-uptake hydrogenase of Azotobacter !1chroococcum. !$#cross-references MUID:91014699; PMID:2215219 !$#accession S11776 !'##molecule_type DNA !'##residues 1-344 ##label FOR !'##cross-references EMBL:X52961; NID:g38713; PIDN:CAA37133.1; !1PID:g38714 !'##experimental_source strain MCD1 GENETICS !$#gene hupS COMPLEX heterodimer; large and small chain FUNCTION !$#pathway hydrogen metabolism !$#note contains iron-sulfur and nickel CLASSIFICATION #superfamily hydrogenase (NiFe) small chain KEYWORDS 3Fe-4S; 4Fe-4S; heterodimer; hydrogen metabolism; !1iron-sulfur protein; membrane bound; metalloprotein; nickel; !1oxidoreductase FEATURE !$1-34 #domain signal sequence #status predicted #label SIG\ !$35-344 #product hydrogenase (uptake) small chain #status !8predicted #label MAT\ !$51,54,146,180 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$218,221,246,252 #binding_site 4Fe-4S cluster (His, Ser, Cys, Cys) !8(covalent) (type N3) #status predicted\ !$261,280,283 #binding_site 3Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 344 #molecular-weight 37953 #checksum 2114 SEQUENCE /// ENTRY S11968 #type complete TITLE hydrogenase (EC 1.18.99.1) (uptake) small chain precursor - Rhizobium leguminosarum ORGANISM #formal_name Rhizobium leguminosarum DATE 13-Jan-1995 #sequence_revision 10-May-1996 #text_change 20-Apr-2000 ACCESSIONS S11968; S11277 REFERENCE S11968 !$#authors Hidalgo, E.; Leyva, A.; Ruiz-Argueeso, T. !$#journal Plant Mol. Biol. (1990) 15:367-370 !$#title Nucleotide sequence of the hydrogenase structural genes from !1Rhizobium leguminosarum. !$#cross-references MUID:91355885; PMID:2103457 !$#accession S11968 !'##molecule_type DNA !'##residues 1-360 ##label HID !'##cross-references EMBL:X52974; NID:g1167855; PIDN:CAA37148.1; !1PID:g48721 !'##experimental_source strain UPM791 REFERENCE S11277 !$#authors Schneider, C.G.; Schmitt, H.J.; Schild, C.; Tichy, H.V.; !1Lotz, W. !$#journal Nucleic Acids Res. (1990) 18:5285 !$#title DNA sequence encoding the two structural genes for the !1uptake hydrogenase of Rhizobium leguminosarum bv. viciae !1B10. !$#cross-references MUID:90384836; PMID:2402452 !$#accession S11277 !'##status translation not shown !'##molecule_type DNA !'##residues 1-159,'S',161-221,'P',223-227,'A',229,'P',231-360 ##label !1SCH !'##cross-references GB:Z36981; EMBL:X53781; NID:g2058351; !1PIDN:CAA85430.1; PID:g536798 !'##experimental_source strain B10 GENETICS !$#gene hupS COMPLEX heterodimer; large and small chain FUNCTION !$#pathway hydrogen metabolism !$#note contains iron-sulfur and nickel CLASSIFICATION #superfamily hydrogenase (NiFe) small chain KEYWORDS 3Fe-4S; 4Fe-4S; heterodimer; hydrogen metabolism; !1iron-sulfur protein; membrane bound; metalloprotein; nickel; !1oxidoreductase FEATURE !$1-45 #domain signal sequence #status predicted #label SIG\ !$46-360 #product hydrogenase (uptake) small chain #status !8predicted #label MAT\ !$62,65,160,194 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$232,235,260,266 #binding_site 4Fe-4S cluster (His, Cys, Cys, Cys) !8(covalent) (type N3) #status predicted\ !$275,294,297 #binding_site 3Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 360 #molecular-weight 39149 #checksum 8319 SEQUENCE /// ENTRY JQ0805 #type complete TITLE hydrogenase (EC 1.18.99.1) small chain precursor - Azotobacter vinelandii ALTERNATE_NAMES hydrogenlyase; [NiFe]hydrogenase ORGANISM #formal_name Azotobacter vinelandii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 20-Apr-2000 ACCESSIONS JQ0805 REFERENCE JQ0805 !$#authors Menon, A.L.; Stults, L.W.; Robson, R.L.; Mortenson, L.E. !$#journal Gene (1990) 96:67-74 !$#title Cloning, sequencing and characterization of the [NiFe] !1hydrogenase-encoding structural genes (hoxK and hoxG) from !1Azotobacter vinelandii. !$#cross-references MUID:91092503; PMID:2265761 !$#accession JQ0805 !'##molecule_type DNA !'##residues 1-358 ##label MEN !'##cross-references GB:M33152; NID:g142310; PIDN:AAA82505.1; !1PID:g142311 !'##experimental_source strain OP !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing GENETICS !$#gene hoxK COMPLEX heterodimer; large and small chain FUNCTION !$#pathway hydrogen metabolism !$#note contains iron-sulfur and nickel CLASSIFICATION #superfamily hydrogenase (NiFe) small chain KEYWORDS 3Fe-4S; 4Fe-4S; heterodimer; hydrogen metabolism; !1iron-sulfur protein; membrane bound; metalloprotein; nickel; !1oxidoreductase FEATURE !$1-45 #domain signal sequence #status predicted #label SIG\ !$46-358 #product hydrogenase small chain #status experimental !8#label MAT\ !$62,65,160,194 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$232,235,260,266 #binding_site 4Fe-4S cluster (His, Cys, Cys, Cys) !8(covalent) (type N3) #status predicted\ !$275,294,297 #binding_site 3Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 358 #molecular-weight 39259 #checksum 7376 SEQUENCE /// ENTRY A43255 #type complete TITLE hydrogenase (EC 1.18.99.1) membrane-bound subunit - Alcaligenes eutrophus ORGANISM #formal_name Alcaligenes eutrophus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-May-2000 ACCESSIONS A43255 REFERENCE A43255 !$#authors Kortluke, C.; Horstmann, K.; Schwartz, E.; Rohde, M.; !1Binsack, R.; Friedrich, B. !$#journal J. Bacteriol. (1992) 174:6277-6289 !$#title A gene complex coding for the membrane-bound hydrogenase of !1Alcaligenes eutrophus H16. !$#cross-references MUID:93015670; PMID:1383192 !$#accession A43255 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-360 ##label KOR !'##cross-references GB:M96433; NID:g141932; PIDN:AAA16461.1; !1PID:g141933 !'##experimental_source H16, megaplasmid pHG1 !'##note sequence extracted from NCBI backbone (NCBIP:115450) CLASSIFICATION #superfamily hydrogenase (NiFe) small chain KEYWORDS 4Fe-4S; membrane bound; metalloprotein; oxidoreductase FEATURE !$60,63,158,192 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$230,233,258,264 #binding_site 4Fe-4S cluster (His, Cys, Cys, Cys) !8(covalent) (type N3) #status predicted SUMMARY #length 360 #molecular-weight 39472 #checksum 6317 SEQUENCE /// ENTRY JH0775 #type complete TITLE hydrogenase (EC 1.18.99.1) small chain precursor - Alcaligenes hydrogenophilus ORGANISM #formal_name Alcaligenes hydrogenophilus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 20-Apr-2000 ACCESSIONS JH0775 REFERENCE JH0775 !$#authors Yagi, K.; Seto, T.; Terakado, M.; Umeda, F.; Doi, T.; !1Imanishi, T.; Miura, Y. !$#journal Chem. Pharm. Bull. (1992) 40:3292-3296 !$#title Nucleotide sequences of membrane-bound hydrogenase gene in !1Alcaligenes hydrogenophilus. !$#cross-references MUID:93193199; PMID:1294332 !$#accession JH0775 !'##molecule_type DNA !'##residues 1-363 ##label YAG !'##cross-references GB:S56898; NID:g299291; PIDN:AAB25779.1; !1PID:g299292 GENETICS !$#gene hupS COMPLEX heterodimer; large and small chain FUNCTION !$#pathway hydrogen metabolism !$#note contains iron-sulfur and nickel CLASSIFICATION #superfamily hydrogenase (NiFe) small chain KEYWORDS 3Fe-4S; 4Fe-4S; heterodimer; hydrogen metabolism; !1iron-sulfur protein; membrane bound; metalloprotein; nickel; !1oxidoreductase FEATURE !$1-43 #domain signal sequence #status predicted #label SIG\ !$44-360 #product hydrogenase small chain #status predicted !8#label MAT\ !$60,63,158,192 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$230,233,258,264 #binding_site 4Fe-4S cluster (His, Cys, Cys, Cys) !8(covalent) (type N3) #status predicted\ !$273,292,295 #binding_site 3Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 363 #molecular-weight 39695 #checksum 1937 SEQUENCE /// ENTRY S09250 #type complete TITLE hydrogenase (EC 1.18.99.1) (uptake) small chain precursor - Rhodocyclus gelatinosus ORGANISM #formal_name Rhodocyclus gelatinosus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 20-Apr-2000 ACCESSIONS S09250 REFERENCE S09250 !$#authors Uffen, R.L.; Colbeau, A.; Richaud, P.; Vignais, P.M. !$#journal Mol. Gen. Genet. (1990) 221:49-58 !$#title Cloning and sequencing the genes encoding uptake-hydrogenase !1subunits of Rhodocyclus gelatinosus. !$#cross-references MUID:90220520; PMID:2325631 !$#accession S09250 !'##molecule_type DNA !'##residues 1-360 ##label UFF !'##cross-references EMBL:X52522; NID:g46165; PIDN:CAA36754.1; !1PID:g46166 GENETICS !$#gene hupS COMPLEX heterodimer; large and small chain FUNCTION !$#pathway hydrogen metabolism !$#note contains iron-sulfur and nickel; insensitive to inhibition !1by CO CLASSIFICATION #superfamily hydrogenase (NiFe) small chain KEYWORDS 4Fe-4S; heterodimer; hydrogen metabolism; iron-sulfur !1protein; membrane bound; metalloprotein; nickel; !1oxidoreductase FEATURE !$1-42 #domain signal sequence #status predicted #label SIG\ !$43-357 #product hydrogenase (uptake) small chain #status !8predicted #label MAT\ !$59,62,156,190 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$228,231,256,262 #binding_site 4Fe-4S cluster (His, Cys, Cys, Cys) !8(covalent) (type N3) #status predicted SUMMARY #length 360 #molecular-weight 39388 #checksum 1404 SEQUENCE /// ENTRY HQDVSB #type complete TITLE cytochrome-c3 hydrogenase (EC 1.12.2.1) (NiFeSe) small chain precursor - Desulfovibrio baculatus ALTERNATE_NAMES hydrogenlyase; NiFeSe hydrogenase ORGANISM #formal_name Desulfovibrio baculatus DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 20-Apr-2000 ACCESSIONS A28380; G27480; I27480 REFERENCE A28380 !$#authors Menon, N.K.; Peck Jr., H.D.; Le Gall, J.; Przybyla, A.E. !$#journal J. Bacteriol. (1987) 169:5401-5407 !$#title Cloning and sequencing of the genes encoding the large and !1small subunits of the periplasmic (NiFeSe) hydrogenase of !1Desulfovibrio baculatus. !$#cross-references MUID:88058744; PMID:3316183 !$#accession A28380 !'##molecule_type DNA !'##residues 1-315 ##label MEN !'##cross-references GB:M18271; NID:g145101; PIDN:AAA23376.1; !1PID:g145103; GB:M22139 REFERENCE A27480 !$#authors Prickril, B.C.; He, S.H.; Li, C.; Menon, N.; Choi, E.S.; !1Przybyla, A.E.; DerVartanian, D.V.; Peck Jr., H.D.; Fauque, !1G.; LeGall, J.; Teixeira, M.; Moura, I.; Moura, J.J.G.; !1Patil, D.; Huynh, B.H. !$#journal Biochem. Biophys. Res. Commun. (1987) 149:369-377 !$#title Identification of three classes of hydrogenase in the genus, !1Desulfovibrio. !$#cross-references MUID:88106446; PMID:3322275 !$#accession G27480 !'##molecule_type protein !'##residues 33-34,'Q',36-47,'E',49-61,'C',63-64 ##label PRI !'##experimental_source strain Norway 4 !$#accession I27480 !'##molecule_type protein !'##residues 33-49,'X',51-67 ##label PR2 !'##experimental_source strain DSM 1743 COMMENT Hydrogenases catalyze reactions involving the production or !1consumption of molecular hydrogen coupled with the oxidation !1or reduction of an electron carrier. Three distinctive !1types, the Fe, NiFe, and NiFeSe hydrogenases, are found in !1the periplasm of sulfate-reducing bacteria. COMMENT The active NiFeSe hydrogenase is a dimer of large and small !1chains, having two [4Fe-4S] clusters, one redox-active Ni !1center, and one selenocysteine in the large chain. CLASSIFICATION #superfamily hydrogenase (NiFe) small chain KEYWORDS 3Fe-4S; 4Fe-4S; heterodimer; hydrogen metabolism; !1iron-sulfur protein; metalloprotein; oxidoreductase; !1periplasmic space FEATURE !$1-32 #domain signal sequence #status predicted #label SIG\ !$33-315 #product hydrogenase (NiFeSe) small chain #status !8predicted #label MAT\ !$50,53,158,196 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$240,243,263,269 #binding_site 4Fe-4S cluster (His, Cys, Cys, Cys) !8(covalent) (type N3) #status predicted\ !$278,296,299 #binding_site 3Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 315 #molecular-weight 34221 #checksum 7175 SEQUENCE /// ENTRY S33852 #type complete TITLE hydrogenase (EC 1.18.99.1) (NiFe) hydA - Wolinella succinogenes ORGANISM #formal_name Wolinella succinogenes DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-May-2000 ACCESSIONS S33852; S22404; S33063 REFERENCE S33852 !$#authors Dross, F.; Geisler, V.; Lenger, R.; Theis, F.; Krafft, T.; !1Fahrenholz, F.; Kojro, E.; Duchene, A.; Tripier, D.; !1Juvenal, K.; Kroeger, A. !$#journal Eur. J. Biochem. (1993) 214:949-950 !$#title Correction. The quinone-reactive Ni/Fe-hydrogenase of !1Wolinella succinogenes. !$#cross-references MUID:93307313; PMID:8319698 !$#accession S33852 !'##molecule_type DNA !'##residues 1-386 ##label DRO !'##cross-references EMBL:X65189; NID:g296081; PIDN:CAA46302.1; !1PID:g296082 !'##note this is a revision to the sequence from reference S22404 REFERENCE S22404 !$#authors Dross, F.; Geisler, V.; Lenger, R.; Theis, F.; Krafft, T.; !1Fahrenholz, F.; Kojro, E.; Duchene, A.; Tripier, D.; !1Juvenal, K.; Kroeger, A. !$#journal Eur. J. Biochem. (1992) 206:93-102 !$#title The quinone-reactive Ni/Fe-hydrogenase of Wolinella !1succinogenes. !$#cross-references MUID:92267032; PMID:1587288 !$#accession S22404 !'##molecule_type DNA !'##residues 33-86,'VVA',90-91,'PKNRWSGLTVS',105-106,'F',109-215,'LDVS', !1221-227,'KL',230-234,'LD',238-367 ##label DRW !'##cross-references EMBL:X65189 !'##note this sequence has been revised in reference S33852 GENETICS !$#gene hydA CLASSIFICATION #superfamily hydrogenase (NiFe) small chain KEYWORDS 4Fe-4S; metalloprotein; oxidoreductase FEATURE !$85,88,185,218 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$256,259,284,290 #binding_site 4Fe-4S cluster (His, Cys, Cys, Cys) !8(covalent) (type N3) #status predicted SUMMARY #length 386 #molecular-weight 42062 #checksum 1785 SEQUENCE /// ENTRY HQDVSG #type complete TITLE cytochrome-c3 hydrogenase (EC 1.12.2.1) (NiFe) small chain precursor [validated] - Desulfovibrio gigas ALTERNATE_NAMES hydrogenlyase ORGANISM #formal_name Desulfovibrio gigas DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 15-Sep-2000 ACCESSIONS A32315; A27492; B60485; C27480 REFERENCE A32315 !$#authors Voordouw, G.; Menon, N.K.; LeGall, J.; Choi, E.S.; Peck Jr., !1H.D.; Przybyla, A.E. !$#journal J. Bacteriol. (1989) 171:2894-2899 !$#title Analysis and comparison of nucleotide sequences encoding the !1genes for [NiFe] and [NiFeSe] hydrogenases from !1Desulfovibrio gigas and Desulfovibrio baculatus. !$#cross-references MUID:89213989; PMID:2651421 !$#contents corrections !$#accession A32315 !'##molecule_type DNA !'##residues 1-314 ##label VOO REFERENCE A27492 !$#authors Li, C.; Peck Jr., H.D.; LeGall, J.; Przybyla, A.E. !$#journal DNA (1987) 6:539-551 !$#title Cloning, characterization, and sequencing of the genes !1encoding the large and small subunits of the periplasmic !1[NiFe]hydrogenase of Desulfovibrio gigas. !$#cross-references MUID:88111028; PMID:3322743 !$#accession A27492 !'##status significant sequence differences !'##molecule_type DNA !'##cross-references EMBL:M18083 !'##note this sequence has been extensively revised in A32315 REFERENCE A60485 !$#authors Niviere, V.; Forget, N.; Bovier-Lapierre, G.; Bonicel, J.; !1Hatchikian, C. !$#journal Biochimie (1988) 70:267-271 !$#title Isolation, amino acid analysis and N-terminal sequence !1determination of the two subunits of the nickel-containing !1hydrogenase of Desulfovibrio gigas. !$#cross-references MUID:88281536; PMID:3134950 !$#accession B60485 !'##molecule_type protein !'##residues 51-73,'V',75 ##label NIV REFERENCE A27480 !$#authors Prickril, B.C.; He, S.H.; Li, C.; Menon, N.; Choi, E.S.; !1Przybyla, A.E.; DerVartanian, D.V.; Peck Jr., H.D.; Fauque, !1G.; LeGall, J.; Teixeira, M.; Moura, I.; Moura, J.J.G.; !1Patil, D.; Huynh, B.H. !$#journal Biochem. Biophys. Res. Commun. (1987) 149:369-377 !$#title Identification of three classes of hydrogenase in the genus, !1Desulfovibrio. !$#cross-references MUID:88106446; PMID:3322275 !$#accession C27480 !'##molecule_type protein !'##residues 'SEMQ',55-72,'LV',75-84 ##label PRI REFERENCE A65633 !$#authors Volbeda, A.; Frey, M.; Fontecilla-Camps, J.C. !$#submission submitted to the Brookhaven Protein Data Bank, March 1996 !$#cross-references PDB:1FRV !$#contents annotation; X-ray crystallography, 2.85 angstroms, residues !153-314 REFERENCE A57765 !$#authors Volbeda, A.; Charon, M.H.; Piras, C.; Hatchikian, E.C.; !1Frey, M.; Fontecilla-Camps, J.C. !$#journal Nature (1995) 373:580-587 !$#title Crystal structure of the nickel-iron hydrogenase from !1Desulfovibrio gigas. !$#cross-references MUID:95157629; PMID:7854413 !$#contents annotation; X-ray crystallography, 2.85 angstroms COMMENT The complex contains two [4Fe-4S] clusters, one [3Fe-4S] !1cluster, and one redox-active Ni center. COMMENT Three distinct types of hydrogeases, the Fe, NiFe, and !1NiFeSe, are found in the periplasm of sulfate-reducing !1bacteria. COMPLEX heterodimer of large (see PIR:HQDVSL) and small chains FUNCTION !$#description catalyzes reactions involving the production or consumption !1of molecular hydrogen coupled with the oxidation or !1reduction of an electron carrier CLASSIFICATION #superfamily hydrogenase (NiFe) small chain KEYWORDS 3Fe-4S; 4Fe-4S; heterodimer; hydrogen metabolism; !1iron-sulfur protein; metalloprotein; oxidoreductase; !1periplasmic space FEATURE !$1-50 #domain signal sequence #status predicted #label SIG\ !$51-314 #product hydrogenase (NiFe) small chain #status !8experimental #label MAT\ !$67,70,162,198 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8experimental\ !$235,238,263,269 #binding_site 4Fe-4S cluster (His, Cys, Cys, Cys) !8(covalent) (type N3) #status experimental\ !$278,296,299 #binding_site 3Fe-4S cluster (Cys) (covalent) #status !8experimental SUMMARY #length 314 #molecular-weight 33983 #checksum 3372 SEQUENCE /// ENTRY A45865 #type complete TITLE cytochrome-c3 hydrogenase (EC 1.12.2.1) (NiFe) small chain - Desulfovibrio vulgaris (strain Miyazaki) ORGANISM #formal_name Desulfovibrio vulgaris DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-May-2000 ACCESSIONS A45865 REFERENCE A45865 !$#authors Deckers, H.M.; Wilson, F.R.; Voordouw, G. !$#journal J. Gen. Microbiol. (1990) 136:2021-2028 !$#title Cloning and sequencing of a [NiFe] hydrogenase operon from !1Desulfovibrio vulgaris Miyazaki F. !$#cross-references MUID:91100954; PMID:2269874 !$#accession A45865 !'##status preliminary !'##molecule_type DNA !'##residues 1-317 ##label DEC !'##cross-references GB:M58339; GB:M33174; NID:g145092; PIDN:AAA23369.1; !1PID:g145093 CLASSIFICATION #superfamily hydrogenase (NiFe) small chain KEYWORDS 4Fe-4S; metalloprotein; oxidoreductase FEATURE !$67,70,164,200 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$238,241,266,272 #binding_site 4Fe-4S cluster (His, Cys, Cys, Cys) !8(covalent) (type N3) #status predicted SUMMARY #length 317 #molecular-weight 34113 #checksum 31 SEQUENCE /// ENTRY HQDVSV #type complete TITLE hydrogenase (EC 1.18.99.1) (Fe) small chain precursor - Desulfovibrio vulgaris subsp. oxamicus ALTERNATE_NAMES Fe hydrogenase beta chain precursor ORGANISM #formal_name Desulfovibrio vulgaris DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 11-Jun-1999 ACCESSIONS B32886 REFERENCE A32886 !$#authors Voordouw, G.; Strang, J.D.; Wilson, F.R. !$#journal J. Bacteriol. (1989) 171:3881-3889 !$#title Organization of the genes encoding [Fe] hydrogenase in !1Desulfovibrio vulgaris subsp. oxamicus Monticello. !$#cross-references MUID:89291738; PMID:2661538 !$#accession B32886 !'##molecule_type DNA !'##residues 1-124 ##label VOO !'##cross-references GB:M27212; NID:g145098; PIDN:AAA23374.1; !1PID:g145100 COMMENT Hydrogenases catalyze reactions involving the production or !1consumption of molecular hydrogen coupled with the oxidation !1or reduction of an electron carrier. Three distinctive !1types, the Fe, NiFe, and NiFeSe hydrogenases, are found in !1the periplasm of sulfate-reducing bacteria. COMMENT The active Fe hydrogenase is a dimer of large (alpha) and !1small (beta) chains, binding three [4Fe-4S] iron-sulfur !1clusters. It may be involved in hydrogen uptake for the !1reduction of sulfate to hydrogen sulfide in an electron !1transport chain. Cytochrome c3 is likely to be the !1physiological electron carrier for the enzyme. GENETICS !$#gene hydB CLASSIFICATION #superfamily hydrogenase (Fe) small chain KEYWORDS hydrogen metabolism; iron-sulfur protein; oxidoreductase; !1periplasmic space FEATURE !$1-34 #domain signal sequence #status predicted #label SIG\ !$35-124 #product hydrogenase (Fe) small chain #status !8predicted #label MAT SUMMARY #length 124 #molecular-weight 13962 #checksum 3107 SEQUENCE /// ENTRY HQDVFS #type complete TITLE hydrogenase (EC 1.18.99.1) (Fe) small chain precursor - Desulfovibrio vulgaris (strain Hildenborough) ALTERNATE_NAMES Fe hydrogenase beta chain ORGANISM #formal_name Desulfovibrio vulgaris DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jun-2000 ACCESSIONS B24551; A27480 REFERENCE A24551 !$#authors Voordouw, G.; Brenner, S. !$#journal Eur. J. Biochem. (1985) 148:515-520 !$#title Nucleotide sequence of the gene encoding the hydrogenase !1from Desulfovibrio vulgaris (Hildenborough). !$#cross-references MUID:85203856; PMID:3888621 !$#accession B24551 !'##molecule_type DNA !'##residues 1-123 ##label VOO !'##cross-references GB:X02416; NID:g40829; PIDN:CAA26267.1; PID:g40831 REFERENCE A27480 !$#authors Prickril, B.C.; He, S.H.; Li, C.; Menon, N.; Choi, E.S.; !1Przybyla, A.E.; DerVartanian, D.V.; Peck Jr., H.D.; Fauque, !1G.; LeGall, J.; Teixeira, M.; Moura, I.; Moura, J.J.G.; !1Patil, D.; Huynh, B.H. !$#journal Biochem. Biophys. Res. Commun. (1987) 149:369-377 !$#title Identification of three classes of hydrogenase in the genus, !1Desulfovibrio. !$#cross-references MUID:88106446; PMID:3322275 !$#accession A27480 !'##status preliminary !'##molecule_type protein !'##residues 35-69 ##label PRI COMMENT Three distinctive types of hydrogenases, the Fe, NiFe, and !1NiFeSe, are found in the periplasm of sulfate-reducing !1bacteria. COMMENT This hydrogenase complex contains three [4Fe-4S] iron-sulfur !1clusters. GENETICS !$#gene hydB COMPLEX heterodimer of large (alpha, see PIR:HQDVFL) and small !1(beta) chains FUNCTION !$#description catalyze reactions involving the production or consumption !1of molecular hydrogen coupled with the oxidation or !1reduction of an electron carrier !$#note may be involved in hydrogen uptake for the reduction of !1sulfate to hydrogen sulfide; cytochrome c3 is probably the !1physiological electron carrier CLASSIFICATION #superfamily hydrogenase (Fe) small chain KEYWORDS hydrogen metabolism; iron-sulfur protein; oxidoreductase; !1periplasmic space FEATURE !$1-34 #domain signal sequence #status predicted #label SIG\ !$35-123 #product hydrogenase (Fe) small chain #status !8predicted #label MAT SUMMARY #length 123 #molecular-weight 13624 #checksum 3478 SEQUENCE /// ENTRY B43331 #type complete TITLE sulfur oxygenase/reductase (EC 1.97.-.-) - Desulfurolobus ambivalens ORGANISM #formal_name Desulfurolobus ambivalens DATE 10-Jun-1993 #sequence_revision 10-Nov-1995 #text_change 11-Jun-1999 ACCESSIONS B43331; S24832 REFERENCE A43331 !$#authors Kletzin, A. !$#journal J. Bacteriol. (1992) 174:5854-5859 !$#title Molecular characterization of the sor gene, which encodes !1the sulfur oxygenase/reductase of the thermoacidophilic !1Archaeum Desulfurolobus ambivalens. !$#cross-references MUID:92394888; PMID:1522063 !$#accession B43331 !'##molecule_type DNA !'##residues 1-309 ##label KLE !'##cross-references EMBL:X56616; NID:g40788; PIDN:CAA39952.1; !1PID:g40790 !'##note sequence extracted from NCBI backbone (NCBIN:112992, !1NCBIP:112994) GENETICS !$#gene sor COMPLEX oligomer of about 16 identical chains FUNCTION !$#description catalyzes the simultaneous production of sulfite, !1thiosulfate and hydrogen sulfide from of sulfur in the !1presence of oxygen !$#pathway sulfur oxidation CLASSIFICATION #superfamily sulfur oxygenase/reductase KEYWORDS iron-sulfur protein; oxidoreductase SUMMARY #length 309 #molecular-weight 35318 #checksum 4592 SEQUENCE /// ENTRY DAAL2E #type complete TITLE catechol 2,3-dioxygenase (EC 1.13.11.2) II - Alcaligenes eutrophus ALTERNATE_NAMES metapyrocatechase II ORGANISM #formal_name Alcaligenes eutrophus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 11-Jun-1999 ACCESSIONS S14691 REFERENCE S14691 !$#authors Kabisch, M.; Fortnagel, P. !$#journal Nucleic Acids Res. (1990) 18:5543 !$#title Nucleotide sequence of the metapyrocatechase II (catechol 2, !13-oxygenase II) gene mpcII from Alcaligenes eutrophus JMP !1222. !$#cross-references MUID:91016840; PMID:2216726 !$#accession S14691 !'##molecule_type DNA !'##residues 1-320 ##label KAB !'##cross-references EMBL:X52415; NID:g38779; PIDN:CAA36666.1; !1PID:g38780 GENETICS !$#gene mpcII CLASSIFICATION #superfamily catechol 2,3-dioxygenase II KEYWORDS oxidoreductase SUMMARY #length 320 #molecular-weight 35387 #checksum 6824 SEQUENCE /// ENTRY DAPSAA #type complete TITLE protocatechuate 3,4-dioxygenase (EC 1.13.11.3) alpha chain [validated] - Pseudomonas putida ORGANISM #formal_name Pseudomonas putida #note strain ATCC 23975 was formerly classified as Pseudomonas aeruginosa DATE 31-Jan-1980 #sequence_revision 14-Feb-1997 #text_change 20-Jan-2003 ACCESSIONS B36930; A00505 REFERENCE A36930 !$#authors Frazee, R.W.; Livingston, D.M.; LaPorte, D.C.; Lipscomb, !1J.D. !$#journal J. Bacteriol. (1993) 175:6194-6202 !$#title Cloning, sequencing, and expression of the Pseudomonas !1putida protocatechuate 3,4-dioxygenase genes. !$#cross-references MUID:94012480; PMID:8407791 !$#accession B36930 !'##molecule_type DNA !'##residues 1-201 ##label FRA !'##cross-references GB:L14836; NID:g294343; PIDN:AAB41025.1; !1PID:g294345 !'##experimental_source ATCC 23975 REFERENCE A00505 !$#authors Kohlmiller, N.A.; Howard, J.B. !$#journal J. Biol. Chem. (1979) 254:7309-7315 !$#title The primary structure of the alpha subunit of !1protocatechuate 3,4-dioxygenase. II. Isolation and sequence !1of overlap peptides and complete sequence. !$#cross-references MUID:79216432; PMID:465136 !$#accession A00505 !'##molecule_type protein !'##residues 2-59,'D',61-76,'D',78-201 ##label KOH !'##experimental_source ATCC 23975 !'##note this is the second of two papers giving the experimental !1details REFERENCE A52887 !$#authors Ohlendorf, D.H.; Orville, A.M.; Lipscomb, J.D. !$#submission submitted to the Brookhaven Protein Data Bank, June 1994 !$#cross-references PDB:2PCD !$#contents annotation; X-ray crystallography, 2.15 angstroms, residues !12-201 REFERENCE A58475 !$#authors Ohlendorf, D.H.; Orville, A.M.; Lipscomb, J.D. !$#journal J. Mol. Biol. (1994) 244:586-608 !$#title Structure of protocatechuate 3,4-dioxygenase from !1Pseudomonas aeruginosa at 2.15 angstroms resolution. !$#cross-references MUID:95082024; PMID:7990141 !$#contents annotation; X-ray crystallography, 2.15 angstroms REFERENCE A50309 !$#authors Ohlendorf, D.H.; Weber, P.C. !$#submission submitted to the Brookhaven Protein Data Bank, September !11990 !$#cross-references PDB:1PCD !$#contents annotation; X-ray crystallography, 2.8 angstroms, residues !12-24,'G',25-59,'D',61-76,'D',78-135,'G',136-173,175-201 REFERENCE A58474 !$#authors Ohlendorf, D.H.; Lipscomb, J.D.; Weber, P.C. !$#journal Nature (1988) 336:403-405 !$#title Structure and assembly of protocatechuate 3,4-dioxygenase. !$#cross-references MUID:89057125; PMID:3194022 !$#contents annotation; X-ray crystallography, 2.8 angstroms GENETICS !$#gene pcaG COMPLEX dodecamer of heterodimers of alpha and beta chains FUNCTION !$#description catalyzes the oxidative cleavage of 3,4-dihydroxybenzoate to !1(E,Z)-1,3-butadiene-1,2,4-tricarboxylic acid by dioxygen !$#note this is the second step in the conversion of !14-hydroxybenzoate to succinate and acetyl-CoA CLASSIFICATION #superfamily protocatechuate 3,4-dioxygenase beta chain KEYWORDS aromatic hydrocarbon catabolism; dodecamer; heterodimer; !1oxidoreductase FEATURE !$2-201 #product protocatechuate 3,4-dioxygenase alpha chain !8#status experimental #label MAT\ !$134 #binding_site substrate (Arg) #status predicted SUMMARY #length 201 #molecular-weight 22387 #checksum 486 SEQUENCE /// ENTRY D35119 #type complete TITLE protocatechuate 3,4-dioxygenase (EC 1.13.11.3) alpha chain - Acinetobacter calcoaceticus ORGANISM #formal_name Acinetobacter calcoaceticus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 20-Jan-2003 ACCESSIONS D35119 REFERENCE A35119 !$#authors Hartnett, C.; Neidle, E.L.; Ngai, K.L.; Ornston, L.N. !$#journal J. Bacteriol. (1990) 172:956-966 !$#title DNA sequences of genes encoding Acinetobacter calcoaceticus !1protocatechuate 3,4-dioxygenase: evidence indicating !1shuffling of genes and of DNA sequences within genes during !1their evolutionary divergence. !$#cross-references MUID:90130333; PMID:2298704 !$#accession D35119 !'##status preliminary !'##molecule_type DNA !'##residues 1-209 ##label HAR !'##cross-references GB:M33798; NID:g141771 CLASSIFICATION #superfamily protocatechuate 3,4-dioxygenase beta chain KEYWORDS aromatic hydrocarbon catabolism; heterodimer; oxidoreductase FEATURE !$142 #binding_site substrate (Arg) #status predicted SUMMARY #length 209 #molecular-weight 23456 #checksum 1942 SEQUENCE /// ENTRY DAPSBA #type complete TITLE protocatechuate 3,4-dioxygenase (EC 1.13.11.3) beta chain [validated] - Pseudomonas putida ORGANISM #formal_name Pseudomonas putida #note strain ATCC 23975 was formerly classified as Pseudomonas aeruginosa DATE 31-Jan-1980 #sequence_revision 14-Feb-1997 #text_change 20-Jan-2003 ACCESSIONS A36930; A00506 REFERENCE A36930 !$#authors Frazee, R.W.; Livingston, D.M.; LaPorte, D.C.; Lipscomb, !1J.D. !$#journal J. Bacteriol. (1993) 175:6194-6202 !$#title Cloning, sequencing, and expression of the Pseudomonas !1putida protocatechuate 3,4-dioxygenase genes. !$#cross-references MUID:94012480; PMID:8407791 !$#accession A36930 !'##molecule_type DNA !'##residues 1-239 ##label FRA !'##cross-references GB:L14836; NID:g294343; PIDN:AAB41024.1; !1PID:g294344 !'##experimental_source ATCC 23975 !'##note authors translated the codon AAA for residue 26 as Leu, and TAC !1for residue 89 as Thr REFERENCE A00506 !$#authors Iwaki, M.; Kagamiyama, H.; Nozaki, M. !$#journal J. Biochem. (1979) 86:1159-1162 !$#title The complete amino acid sequence of the beta-subunit of !1protocatechuate 3,4-dioxygenase from Pseudomonas aeruginosa. !$#cross-references MUID:80049609; PMID:115853 !$#accession A00506 !'##molecule_type protein !'##residues 2-61,'D',63-69,'D',71,73-217,'N',219-239 ##label IWA !'##experimental_source ATCC 23975 REFERENCE A52887 !$#authors Ohlendorf, D.H.; Orville, A.M.; Lipscomb, J.D. !$#submission submitted to the Brookhaven Protein Data Bank, June 1994 !$#cross-references PDB:2PCD !$#contents annotation; X-ray crystallography, 2.15 angstroms, residues !12-68;72-237 REFERENCE A58475 !$#authors Ohlendorf, D.H.; Orville, A.M.; Lipscomb, J.D. !$#journal J. Mol. Biol. (1994) 244:586-608 !$#title Structure of protocatechuate 3,4-dioxygenase from !1Pseudomonas aeruginosa at 2.15 angstroms resolution. !$#cross-references MUID:95082024; PMID:7990141 !$#contents annotation; X-ray crystallography, 2.15 angstroms REFERENCE A50309 !$#authors Ohlendorf, D.H.; Weber, P.C. !$#submission submitted to the Brookhaven Protein Data Bank, September !11990 !$#cross-references PDB:1PCD !$#contents annotation; X-ray crystallography, 2.8 angstroms, residues !12-217,'G',218-239 REFERENCE A58474 !$#authors Ohlendorf, D.H.; Lipscomb, J.D.; Weber, P.C. !$#journal Nature (1988) 336:403-405 !$#title Structure and assembly of protocatechuate 3,4-dioxygenase. !$#cross-references MUID:89057125; PMID:3194022 !$#contents annotation; X-ray crystallography, 2.8 angstroms GENETICS !$#gene pcaH COMPLEX dodecamer of heterodimers of alpha and beta chains FUNCTION !$#description catalyzes the oxidative cleavage of 3,4-dihydroxybenzoate to !1(E,Z)-1,3-butadiene-1,2,4-tricarboxylic acid by dioxygen !$#note this is the second step in the conversion of !14-hydroxybenzoate to succinate and acetyl-CoA CLASSIFICATION #superfamily protocatechuate 3,4-dioxygenase beta chain KEYWORDS aromatic hydrocarbon catabolism; dodecamer; heterodimer; !1iron; metalloprotein; oxidoreductase FEATURE !$2-239 #product protocatechuate 3,4-dioxygenase beta chain !8#status experimental #label MAT\ !$109,148,161,163 #binding_site iron (Tyr, Tyr, His, His) #status !8experimental SUMMARY #length 239 #molecular-weight 26793 #checksum 774 SEQUENCE /// ENTRY C35119 #type complete TITLE protocatechuate 3,4-dioxygenase (EC 1.13.11.3) beta chain - Acinetobacter calcoaceticus ORGANISM #formal_name Acinetobacter calcoaceticus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 20-Jan-2003 ACCESSIONS C35119 REFERENCE A35119 !$#authors Hartnett, C.; Neidle, E.L.; Ngai, K.L.; Ornston, L.N. !$#journal J. Bacteriol. (1990) 172:956-966 !$#title DNA sequences of genes encoding Acinetobacter calcoaceticus !1protocatechuate 3,4-dioxygenase: evidence indicating !1shuffling of genes and of DNA sequences within genes during !1their evolutionary divergence. !$#cross-references MUID:90130333; PMID:2298704 !$#accession C35119 !'##status preliminary !'##molecule_type DNA !'##residues 1-237 ##label HAR !'##cross-references GB:M33798; NID:g141771; PID:g141773 CLASSIFICATION #superfamily protocatechuate 3,4-dioxygenase beta chain KEYWORDS aromatic hydrocarbon catabolism; heterodimer; iron; !1metalloprotein; oxidoreductase FEATURE !$109,148,161,163 #binding_site iron (Tyr, Tyr, His, His) #status !8predicted SUMMARY #length 237 #molecular-weight 27134 #checksum 7745 SEQUENCE /// ENTRY A27058 #type complete TITLE chlorocatechol 1,2-dioxygenase (EC 1.13.11.-) - Pseudomonas putida plasmid pAC27 ALTERNATE_NAMES chlorocatechol-specific pyrocatechase; pyrocatechase II ORGANISM #formal_name Pseudomonas putida DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 20-Jan-2003 ACCESSIONS A27058; S06449 REFERENCE A94163 !$#authors Frantz, B.; Chakrabarty, A.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:4460-4464 !$#title Organization and nucleotide sequence determination of a gene !1cluster involved in 3-chlorocatechol degradation. !$#cross-references MUID:87260828; PMID:3299368 !$#accession A27058 !'##molecule_type DNA !'##residues 1-260 ##label FRA !'##cross-references EMBL:M16964; NID:g141915; PIDN:AAA98281.1; !1PID:g141916 REFERENCE S06449 !$#authors Ghosal, D.; You, I.S. !$#journal Mol. Gen. Genet. (1988) 211:113-120 !$#title Nucleotide homology and organization of chlorocatechol !1oxidation genes of plasmids pJP4 and pAC27. !$#cross-references MUID:88142559; PMID:2830460 !$#accession S06449 !'##molecule_type DNA !'##residues 1-186,'P',188-260 ##label GHO !'##cross-references EMBL:M36279; NID:g141979; PIDN:AAA98294.1; !1PID:g141980 !'##experimental_source strain AC867 GENETICS !$#gene clcA !$#genome plasmid CLASSIFICATION #superfamily protocatechuate 3,4-dioxygenase beta chain KEYWORDS oxidoreductase SUMMARY #length 260 #molecular-weight 28988 #checksum 726 SEQUENCE /// ENTRY A33487 #type complete TITLE protocatechuate 3,4-dioxygenase (EC 1.13.11.3) alpha chain - Pseudomonas cepacia ORGANISM #formal_name Pseudomonas cepacia DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 20-Jan-2003 ACCESSIONS A33487 REFERENCE A33487 !$#authors Zylstra, G.J.; Olsen, R.H.; Ballou, D.P. !$#journal J. Bacteriol. (1989) 171:5915-5921 !$#title Genetic organization and sequence of the Pseudomonas cepacia !1genes for the alpha and beta subunits of protocatechuate 3, !14-dioxygenase. !$#cross-references MUID:90036674; PMID:2808303 !$#accession A33487 !'##status preliminary !'##molecule_type DNA !'##residues 1-197 ##label ZYL !'##cross-references GB:M30791; NID:g151429; PIDN:AAA25925.1; !1PID:g151431 CLASSIFICATION #superfamily protocatechuate 3,4-dioxygenase beta chain KEYWORDS oxidoreductase SUMMARY #length 197 #molecular-weight 21394 #checksum 2096 SEQUENCE /// ENTRY B33487 #type complete TITLE protocatechuate 3,4-dioxygenase (EC 1.13.11.3) beta chain - Pseudomonas cepacia ORGANISM #formal_name Pseudomonas cepacia DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 20-Jan-2003 ACCESSIONS B33487 REFERENCE A33487 !$#authors Zylstra, G.J.; Olsen, R.H.; Ballou, D.P. !$#journal J. Bacteriol. (1989) 171:5915-5921 !$#title Genetic organization and sequence of the Pseudomonas cepacia !1genes for the alpha and beta subunits of protocatechuate 3, !14-dioxygenase. !$#cross-references MUID:90036674; PMID:2808303 !$#accession B33487 !'##status preliminary !'##molecule_type DNA !'##residues 1-235 ##label ZYL !'##cross-references GB:M30791; NID:g151429; PIDN:AAA25924.1; !1PID:g151430 CLASSIFICATION #superfamily protocatechuate 3,4-dioxygenase beta chain KEYWORDS aromatic hydrocarbon catabolism; heterodimer; iron; !1metalloprotein; oxidoreductase FEATURE !$107,146,159,161 #binding_site iron (Tyr, Tyr, His, His) #status !8predicted SUMMARY #length 235 #molecular-weight 26550 #checksum 7294 SEQUENCE /// ENTRY DASYL1 #type complete TITLE lipoxygenase (EC 1.13.11.12) 2 - soybean ALTERNATE_NAMES carotene oxidase 2; lipoxidase 2 ORGANISM #formal_name Glycine max #common_name soybean DATE 31-Mar-1989 #sequence_revision 30-Jun-1991 #text_change 19-Jan-2001 ACCESSIONS A28161; A30831; A37160; S13536 REFERENCE A28161 !$#authors Shibata, D.; Steczko, J.; Dixon, J.E.; Andrews, P.C.; !1Hermodson, M.; Axelrod, B. !$#journal J. Biol. Chem. (1988) 263:6816-6821 !$#title Primary structure of soybean lipoxygenase L-2. !$#cross-references MUID:88198254; PMID:2834391 !$#accession A28161 !'##molecule_type mRNA !'##residues 1-865 ##label SHI !'##cross-references GB:J03211; NID:g170013; PIDN:AAA33987.1; !1PID:g170014 !'##note there are no disulfide bonds REFERENCE A30831 !$#authors Start, W.G.; Ma, Y.; Polacco, J.C.; Hildebrand, D.F.; !1Freyer, G.A.; Altschuler, M. !$#journal Plant Mol. Biol. (1986) 7:11-23 !$#title Two soybean seed lipoxygenase nulls accumulate reduced !1levels of lipoxygenase transcripts. !$#accession A30831 !'##molecule_type mRNA !'##residues 232-262,'NL',265-312,'Y',314-362,'E',364-399,'P',401-427, !1'H',429-485,'G',487-501,'G',503-533,'L',535-690 ##label STA !'##cross-references GB:M16876 !'##experimental_source clone pLX-65 !'##note due to a frameshift error, residues in the region 691-865 do !1not correspond to the sequence shown !'##note this sequence has been revised in reference A37160 REFERENCE A37160 !$#authors Start, W.G.; Ma, Y.; Polacco, J.C.; Hildebrand, D.F.; !1Freyer, G.A.; Altschuler, M. !$#citation unpublished results, cited by Yenofsky, R.L., Fine, M., and !1Liu, C., in Mol. Gen. Genet. 211, 215-222, 1988 !$#accession A37160 !'##molecule_type mRNA !'##residues 232-262,'NL',265-312,'Y',314-399,'PK',402-427,'H',429-485, !1'G',487-501,'G',503-533,'L',535-722,'K',724-732,'Q',734-747, !1'S',749-753,'V',755-852,'E',853-865 ##label ST2 !'##note this is a revision to the sequence from reference A30831 REFERENCE S13381 !$#authors Shibata, D.; Kato, T.; Tanaka, K. !$#journal Plant Mol. Biol. (1991) 16:353-359 !$#title Nucleotide sequences of a soybean lipoxygenase gene and the !1short intergenic region between an upstream lipoxygenase !1gene. !$#cross-references MUID:91370880; PMID:1909908 !$#accession S13536 !'##status preliminary !'##molecule_type DNA !'##residues 859-865 ##label SH2 !'##cross-references EMBL:X56139; NID:g18745; PIDN:CAA39605.1; !1PID:g829267 COMMENT In soybean, four isozymes are found with distinct !1electrophoretic properties. The enzyme may be involved in !1aging and in pest resistance. FUNCTION !$#description catalyzes the oxidation of unsaturated fatty acids with a 1, !14-cis,cis pentadiene structure to the corresponding !1hydroperoxy acids CLASSIFICATION #superfamily lipoxygenase KEYWORDS fatty acid oxidation; iron; metalloprotein; oxidoreductase FEATURE !$527,532,718,722,865 #binding_site iron (His, His, His, Asn, Ile) #status !8predicted SUMMARY #length 865 #molecular-weight 97145 #checksum 4699 SEQUENCE /// ENTRY S07075 #type complete TITLE lipoxygenase (EC 1.13.11.12) 2 [similarity] - garden pea ORGANISM #formal_name Pisum sativum #common_name garden pea DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS S07075 REFERENCE S07075 !$#authors Ealing, P.M.; Casey, R. !$#journal Biochem. J. (1989) 264:929-932 !$#title The cDNA cloning of a pea (Pisum sativum) seed lipoxygenase. !1Sequence comparisons of the two major pea seed lipoxygenase !1isoforms. !$#cross-references MUID:90147555; PMID:2515855 !$#accession S07075 !'##molecule_type mRNA !'##residues 1-864 ##label EAL !'##cross-references EMBL:X17061; NID:g20801; PIDN:CAA34906.1; !1PID:g20802 CLASSIFICATION #superfamily lipoxygenase KEYWORDS oxidoreductase SUMMARY #length 864 #molecular-weight 97133 #checksum 144 SEQUENCE /// ENTRY DASYL2 #type complete TITLE lipoxygenase (EC 1.13.11.12) 1 [validated] - soybean ALTERNATE_NAMES carotene oxidase 1; lipoxidase 1 ORGANISM #formal_name Glycine max #common_name soybean DATE 31-Mar-1989 #sequence_revision 07-Feb-1997 #text_change 15-Sep-2000 ACCESSIONS S25064; A28435; B30831 REFERENCE S25064 !$#authors Masayoshi, M.; Chikafusa, F. !$#submission submitted to the EMBL Data Library, June 1992 !$#description The cDNA sequence of soybean lipoxygenase 1. !$#accession S25064 !'##molecule_type mRNA !'##residues 1-839 ##label MAS !'##cross-references EMBL:X67304; NID:g18674; PIDN:CAA47717.1; !1PID:g18675 REFERENCE A28435 !$#authors Shibata, D.; Steczko, J.; Dixon, J.E.; Hermodson, M.; !1Yazdanparast, R.; Axelrod, B. !$#journal J. Biol. Chem. (1987) 262:10080-10085 !$#title Primary structure of soybean lipoxygenase-1. !$#cross-references MUID:87280024; PMID:3112136 !$#accession A28435 !'##molecule_type mRNA !'##residues 1-478,'ATS',483-839 ##label SHI !'##cross-references GB:J02795; NID:g295117; PIDN:AAA33986.1; !1PID:g295118 REFERENCE A30831 !$#authors Start, W.G.; Ma, Y.; Polacco, J.C.; Hildebrand, D.F.; !1Freyer, G.A.; Altschuler, M. !$#journal Plant Mol. Biol. (1986) 7:11-23 !$#title Two soybean seed lipoxygenase nulls accumulate reduced !1levels of lipoxygenase transcripts. !$#accession B30831 !'##molecule_type mRNA !'##residues 'RN',428-557,'AL',561-571,'EL',575-640,'P',642-662 ##label !1STA !'##cross-references GB:M16921; NID:g170017 !'##experimental_source clone pAL-134 !'##note due to a frameshift error, residues following residue 662 do !1not correspond to the sequence shown REFERENCE A67236 !$#authors Amzel, L.M.; Boyington, J.C. !$#submission submitted to the Brookhaven Protein Data Bank, July 1993 !$#cross-references PDB:2SBL !$#contents annotation; X-ray crystallography, 2.6 angstroms, residues !17-21;32-68;74-117;112-453;461-839 REFERENCE A57547 !$#authors Boyington, J.C.; Gaffney, B.J.; Amzel, L.M. !$#journal Science (1993) 260:1482-1486 !$#title The three-dimensional structure of an arachidonic acid !115-lipoxygenase. !$#cross-references MUID:93276267; PMID:8502991 !$#contents annotation; X-ray crystallography, 2.6 angstroms !$#note the carboxyl group of the carboxyl-terminal Ile is one of !1the binding groups for iron COMMENT In soybean, four isozymes are found with distinct !1electrophoretic properties. This enzyme may be involved in !1aging and in pest resistance. FUNCTION !$#description catalyzes the oxidation of unsaturated fatty acids with a 1, !14-cis,cis pentadiene structure to corresponding hydroperoxy !1acids CLASSIFICATION #superfamily lipoxygenase KEYWORDS fatty acid oxidation; iron; metalloprotein; oxidoreductase FEATURE !$499,504,690,694,839 #binding_site iron (His, His, His, Asn, Ile) #status !8experimental SUMMARY #length 839 #molecular-weight 94369 #checksum 6391 SEQUENCE /// ENTRY S01142 #type complete TITLE lipoxygenase (EC 1.13.11.12) 3 [similarity] - garden pea ORGANISM #formal_name Pisum sativum #common_name garden pea DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS S01142 REFERENCE S01142 !$#authors Ealing, P.M.; Casey, R. !$#journal Biochem. J. (1988) 253:915-918 !$#title The complete amino acid sequence of a pea (Pisum sativum) !1seed lipoxygenase predicted from a near full-length cDNA. !$#cross-references MUID:89025643; PMID:3140791 !$#accession S01142 !'##molecule_type mRNA !'##residues 1-861 ##label EAL !'##cross-references EMBL:X07807; NID:g20799; PIDN:CAA30666.1; !1PID:g20800 CLASSIFICATION #superfamily lipoxygenase KEYWORDS oxidoreductase SUMMARY #length 861 #molecular-weight 97628 #checksum 1228 SEQUENCE /// ENTRY JQ2267 #type complete TITLE lipoxygenase (EC 1.13.11.12) Lox1 - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JQ2267 REFERENCE JQ2267 !$#authors Melan, M.A.; Dong, X.; Endara, M.E.; Davis, K.R.; Ausubel, !1F.M.; Peterman, T.K. !$#journal Plant Physiol. (1993) 101:441-450 !$#title An Arabidopsis thaliana lipoxygenase gene can be induced by !1pathogens, abscisic acid, and methyl jasmonate. !$#cross-references MUID:94105302; PMID:7506426 !$#accession JQ2267 !'##molecule_type mRNA !'##residues 1-859 ##label MEL !'##cross-references GB:L04637; NID:g289202; PIDN:AAA32827.1; !1PID:g289203 COMMENT This enzyme catalyzes the hydroperoxidation of !1polyunsaturated fatty acids containing a cis,cis-1, !14-pentadiene-conjugated double-bond system. CLASSIFICATION #superfamily lipoxygenase KEYWORDS fatty acid oxidation; oxidoreductase SUMMARY #length 859 #molecular-weight 98044 #checksum 3952 SEQUENCE /// ENTRY S23454 #type complete TITLE lipoxygenase (EC 1.13.11.12) L-2 - rice ORGANISM #formal_name Oryza sativa #common_name rice DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S23454; S24576 REFERENCE S23454 !$#authors Ohta, H.; Shirano, Y.; Tanaka, K.; Morita, Y.; Shibata, D. !$#journal Eur. J. Biochem. (1992) 206:331-336 !$#title cDNA cloning of rice lipoxygenase L-2 and characterization !1using an active enzyme expressed from the cDNA in !1Escherichia coli. !$#cross-references MUID:92283256; PMID:1597177 !$#accession S23454 !'##molecule_type mRNA !'##residues 1-865 ##label OHT !'##cross-references EMBL:X64396; NID:g20266; PIDN:CAA45738.1; !1PID:g20267 !$#accession S24576 !'##molecule_type protein !'##residues !119-24;27-39;355-369;506-520;549-561;622-626;672-677;743-748; !1806-817 ##label OHT1 CLASSIFICATION #superfamily lipoxygenase KEYWORDS oxidoreductase SUMMARY #length 865 #molecular-weight 96657 #checksum 1939 SEQUENCE /// ENTRY DAHUAL #type complete TITLE arachidonate 5-lipoxygenase (EC 1.13.11.34) [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1989 #sequence_revision 03-May-1996 #text_change 23-Mar-2001 ACCESSIONS A28117; A37017; A28397; A32104; A38410 REFERENCE A28117 !$#authors Dixon, R.A.F.; Jones, R.E.; Diehl, R.E.; Bennett, C.D.; !1Kargman, S.; Rouzer, C.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:416-420 !$#title Cloning of the cDNA for human 5-lipoxygenase. !$#cross-references MUID:88124852; PMID:3422434 !$#accession A28117 !'##molecule_type mRNA !'##residues 1-674 ##label DIX !'##cross-references GB:J03600; NID:g187192; PIDN:AAA36183.1; !1PID:g187193 REFERENCE A37017 !$#authors Matsumoto, T.; Funk, C.D.; Radmark, O.; Hoeoeg, J.O.; !1Joernvall, H.; Samuelsson, B. !$#journal Adv. Prostaglandin Thromboxane Leukot. Res. (1989) !119:466-469 !$#title Molecular cloning and amino acid sequence of human !15-lipoxygenase. !$#cross-references MUID:89320027; PMID:2526519 !$#accession A37017 !'##molecule_type mRNA !'##residues 1-674 ##label MATS REFERENCE A28397 !$#authors Matsumoto, T.; Funk, C.D.; Raadmark, O.; Hoeoeg, J.O.; !1Joernvall, H.; Samuelsson, B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:26-30 !$#title Molecular cloning and amino acid sequence of human !15-lipoxygenase. !$#cross-references MUID:88124804; PMID:2829172 !$#accession A28397 !'##molecule_type mRNA !'##residues 1-535,'PVGVPDRGDLHRLRPARRGQLRPVRLVLLDPQCAPNHASPATDCQ', !1581-674 ##label RF1 !'##note parts of the sequence, including the amino end, were confirmed !1by protein sequencing !'##note this sequence report appears to contain a frameshift error REFERENCE A32104 !$#authors Funk, C.D.; Hoshiko, S.; Matsumoto, T.; Radmark, O.; !1Samuelsson, B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:2587-2591 !$#title Characterization of the human 5-lipoxygenase gene. !$#cross-references MUID:89202374; PMID:2565035 !$#accession A32104 !'##molecule_type DNA !'##residues 1-50 ##label FUN !'##cross-references GB:J04520; NID:g187168; PIDN:AAA59522.1; !1PID:g187169 REFERENCE A38410 !$#authors Hoshiko, S.; Radmark, O.; Samuelsson, B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:9073-9077 !$#title Characterization of the human 5-lipoxygenase gene promoter. !$#cross-references MUID:91067649; PMID:2251250 !$#accession A38410 !'##molecule_type DNA !'##residues 1-11 ##label HOS !'##cross-references GB:M38191 COMMENT This calcium- and ATP-requiring enzyme catalyzes the first !1two steps in the biosynthesis of leukotriene derivatives !1from arachidonic acid. GENETICS !$#gene GDB:ALOX5 !'##cross-references GDB:132453; OMIM:152390 !$#map_position 10q11.2-10q11.2 CLASSIFICATION #superfamily arachidonate 5-lipoxygenase KEYWORDS iron; leukotriene biosynthesis; metalloprotein; !1oxidoreductase FEATURE !$2-674 #product arachidonate 5-lipoxygenase #status !8experimental #label MAT\ !$368,373,551,555,674 #binding_site iron (His, His, His, Asn, Ile) #status !8predicted SUMMARY #length 674 #molecular-weight 77983 #checksum 3525 SEQUENCE /// ENTRY A30882 #type complete TITLE arachidonate 5-lipoxygenase (EC 1.13.11.34) - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A30882 REFERENCE A30882 !$#authors Balcarek, J.M.; Theisen, T.W.; Cook, M.N.; Varrichio, A.; !1Hwang, S.M.; Strohsacker, M.W.; Crooke, S.T. !$#journal J. Biol. Chem. (1988) 263:13937-13941 !$#title Isolation and characterization of a cDNA clone encoding rat !15-lipoxygenase. !$#cross-references MUID:88330933; PMID:3417684 !$#accession A30882 !'##molecule_type mRNA !'##residues 1-670 ##label BAL !'##cross-references GB:J03960; NID:g205228; PIDN:AAA41538.1; !1PID:g205229 CLASSIFICATION #superfamily arachidonate 5-lipoxygenase KEYWORDS oxidoreductase SUMMARY #length 670 #molecular-weight 77867 #checksum 8682 SEQUENCE /// ENTRY A38283 #type complete TITLE arachidonate 12-lipoxygenase (EC 1.13.11.31) - human ALTERNATE_NAMES platelet-type 12-lipoxygenase ORGANISM #formal_name Homo sapiens #common_name man DATE 31-May-1991 #sequence_revision 03-May-1996 #text_change 21-Jul-2000 ACCESSIONS A38283; A36246; A35953; I51906; I64836; A33091 REFERENCE A38283 !$#authors Izumi, T.; Hoshiko, S.; Radmark, O.; Samuelsson, B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:7477-7481 !$#title Cloning of the cDNA for human 12-lipoxygenase. !$#cross-references MUID:91017529; PMID:2217179 !$#accession A38283 !'##molecule_type mRNA !'##residues 1-663 ##label IZU !'##cross-references GB:M38192; GB:M38792; GB:M58704; NID:g187170; !1PIDN:AAA59523.1; PID:g187171 !'##experimental_source platelet mRNA !'##note some sequence heretogeneity was found REFERENCE A36246 !$#authors Yoshimoto, T.; Yamamoto, Y.; Arakawa, T.; Suzuki, H.; !1Yamamoto, S.; Yokoyama, C.; Tanabe, T.; Toh, H. !$#journal Biochem. Biophys. Res. Commun. (1990) 172:1230-1235 !$#title Molecular cloning and expression of human arachidonate !112-lipoxygenase. !$#cross-references MUID:91058562; PMID:2244907 !$#accession A36246 !'##molecule_type mRNA !'##residues 1-188,'PCLH',193-260,'Q',262-321,'S',323-344,'C',346-663 !1##label YOS !'##cross-references GB:M62982; NID:g177106; PIDN:AAA51533.1; !1PID:g177107 REFERENCE A35953 !$#authors Funk, C.D.; Furci, L.; FitzGerald, G.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:5638-5642 !$#title Molecular cloning, primary structure, and expression of the !1human platelet/erythroleukemia cell 12-lipoxygenase. !$#cross-references MUID:90332636; PMID:2377602 !$#accession A35953 !'##molecule_type mRNA !'##residues 1-260,'Q',262-321,'S',323-388,'P',390-663 ##label FUN !'##cross-references GB:M35418; NID:g189773; PIDN:AAA60056.1; !1PID:g189774 REFERENCE I51906 !$#authors Hussain, H.; Shornick, L.P.; Shannon, V.R.; Wilson, J.D.; !1Funk, C.D.; Pentland, A.P.; Holtzman, M.J. !$#journal Am. J. Physiol. (1994) 266:C243-C253 !$#title Epidermis contains platelet-type 12-lipoxygenase that is !1overexpressed in germinal layer keratinocytes in psoriasis. !$#cross-references MUID:94136572; PMID:8304420 !$#accession I51906 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 340-427 ##label RES !'##cross-references GB:S68587; NID:g545223; PIDN:AAD14020.1; !1PID:g4261720 !'##experimental_source skin, epidermal cells !$#accession I64836 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 340-396,'V',398-427 ##label RE2 !'##cross-references GB:S68588; NID:g545222; PIDN:AAD14021.1; !1PID:g4261721 GENETICS !$#gene GDB:ALOX12 !'##cross-references GDB:127547; OMIM:152391 !$#map_position 17p13.1-17p13.1 FUNCTION !$#description catalyzes the oxidation of arachidonic acid to (5Z,8Z,10E, !114Z)-(12S)-12-hydroperoxyeicosa-5,8,10,14-tetraenoic acid by !1dioxygen !$#pathway leukotriene biosynthesis CLASSIFICATION #superfamily arachidonate 5-lipoxygenase KEYWORDS fatty acid oxidation; iron; leukotriene biosynthesis; !1metalloprotein; oxidoreductase FEATURE !$360,365,540,544,663 #binding_site iron (His, His, His, Asn, Ile) #status !8predicted SUMMARY #length 663 #molecular-weight 75721 #checksum 8233 SEQUENCE /// ENTRY A54075 #type complete TITLE arachidonate 12-lipoxygenase (EC 1.13.11.31), platelet [validated] - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS A54075 REFERENCE A54075 !$#authors Chen, X.S.; Kurre, U.; Jenkins, N.A.; Copeland, N.G.; Funk, !1C.D. !$#journal J. Biol. Chem. (1994) 269:13979-13987 !$#title cDNA cloning, expression, mutagenesis of C-terminal !1isoleucine, genomic structure, and chromosomal localizations !1of murine 12-lipoxygenases. !$#cross-references MUID:94245713; PMID:8188678 !$#accession A54075 !'##molecule_type DNA; mRNA !'##residues 1-663 ##label CHE !'##cross-references GB:U04334; NID:g467220; PIDN:AAA20659.1; !1PID:g467221 !'##experimental_source strain C57BL/6, blood platelets !'##note removal or substitution of Ile-663 abolished enzyme activity COMMENT A second arachidonate 12-lipoxygenase from mouse leukocytes !1is shown in (PIR:B54075). GENETICS !$#map_position 11 CLASSIFICATION #superfamily arachidonate 5-lipoxygenase KEYWORDS oxidoreductase SUMMARY #length 663 #molecular-weight 75345 #checksum 2553 SEQUENCE /// ENTRY A31349 #type complete TITLE arachidonate 15-lipoxygenase (EC 1.13.11.33) - human ALTERNATE_NAMES arachidonate omega-6 lipoxygenase ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1990 #sequence_revision 07-Feb-1997 #text_change 11-Jun-1999 ACCESSIONS A31349; A28192; S19625; S19577; A61164; B61164 REFERENCE A31349 !$#authors Sigal, E.; Craik, C.S.; Highland, E.; Grunberger, D.; !1Costello, L.L.; Dixon, R.A.F.; Nadel, J.A. !$#journal Biochem. Biophys. Res. Commun. (1988) 157:457-464 !$#title Molecular cloning and primary structure of human !115-lipoxygenase. !$#cross-references MUID:89076270; PMID:3202857 !$#accession A31349 !'##molecule_type mRNA !'##residues 1-662 ##label SIG !'##cross-references GB:M23892; NID:g187190; PIDN:AAA36182.1; !1PID:g307135 !'##experimental_source reticulocyte REFERENCE A28192 !$#authors Sigal, E.; Grunberger, D.; Craik, C.S.; Caughey, G.H.; !1Nadel, J.A. !$#journal J. Biol. Chem. (1988) 263:5328-5332 !$#title Arachidonate 15-lipoxygenase (omega-6 lipoxygenase) from !1human leukocytes. Purification and structural homology to !1other mammalian lipoxygenases. !$#cross-references MUID:88186828; PMID:3356688 !$#accession A28192 !'##molecule_type protein !'##residues 3-16 ##label SI2 !'##experimental_source leukocyte REFERENCE S19577 !$#authors Izumi, T.; Radmark, O.; Joernvall, H.; Samuelsson, B. !$#journal Eur. J. Biochem. (1991) 202:1231-1238 !$#title Purification of two forms of arachidonate 15-lipoxygenase !1from human leukocytes. !$#cross-references MUID:92111501; PMID:1662607 !$#accession S19625 !'##molecule_type protein !'##residues 'X',3-4,'X',6,'X',8-22;38-45;157-162,'XX',165-168;627-631 !1##label IZU !$#accession S19577 !'##molecule_type protein !'##residues 'X',3-25,27-31 ##label IZ1 !'##note there appear to be distinct chromatographic forms, at least one !1each from reticulocyte and eosinophil, and two from !1leukocyte, arising from a post-translational modification of !1a common precursor REFERENCE A61164 !$#authors Izumi, T.; Radmark, O.; Samuelsson, B. !$#journal Adv. Prostaglandin Thromboxane Leukotriene Res. (1990) !121:101-104 !$#title Purification of 15-lipoxygenase from human leukocytes, !1evidence for the presence of isozymes. !$#accession A61164 !'##molecule_type protein !'##residues 'X',3-4,'X',6,'X',8-12,'X',14-19,'T',21-22 ##label IZ2 !'##experimental_source leukocyte !$#accession B61164 !'##molecule_type protein !'##residues 'X',3-25,27-31 ##label IZ3 !'##experimental_source leukocyte GENETICS !$#gene GDB:ALOX15 !'##cross-references GDB:132454 !$#map_position 17pter-17qter FUNCTION !$#description catalyzes the oxidation of arachidonic acid to (5Z,8Z,11Z, !113E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoic acid by !1dioxygen !$#pathway leukotriene biosynthesis CLASSIFICATION #superfamily arachidonate 5-lipoxygenase KEYWORDS fatty acid oxidation; iron; leukotriene biosynthesis; !1metalloprotein; oxidoreductase FEATURE !$360,365,540,544,662 #binding_site iron (His, His, His, His, Ile) #status !8predicted SUMMARY #length 662 #molecular-weight 74804 #checksum 2368 SEQUENCE /// ENTRY JQ0018 #type complete TITLE arachidonate 15-lipoxygenase (EC 1.13.11.33), erythroid-specific - rabbit ALTERNATE_NAMES carotene oxidase; lipoxidase CONTAINS lipoxygenase peptides ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS JQ0018; A61060; A27327; A61568; JC1513 REFERENCE JQ0018 !$#authors Fleming, J.; Thiele, B.J.; Chester, J.; O'Prey, J.; !1Janetzki, S.; Aitken, A.; Anton, I.A.; Rapoport, S.M.; !1Harrison, P.R. !$#journal Gene (1989) 79:181-188 !$#title The complete sequence of the rabbit erythroid cell-specific !115-lipoxygenase mRNA: comparison of the predicted amino acid !1sequence of the erythrocyte lipoxygenase with other !1lipoxygenases. !$#cross-references MUID:89378774; PMID:2777088 !$#accession JQ0018 !'##molecule_type mRNA !'##residues 1-663 ##label FLE !'##cross-references GB:M27214; NID:g2642134; PIDN:AAB86978.1; !1PID:g164907 REFERENCE A61060 !$#authors Thiele, B.J.; Fleming, J.; Chester, J.; O'Prey, J.; Prehn, !1S.; Janetzki, S.; Rapoport, S.M.; Harrison, P.R. !$#journal Biomed. Biochim. Acta (1990) 49:s17-s24 !$#title Structure of the mRNA and of the gene coding for the rabbit !1erythroid 15-lipoxygenase. !$#cross-references MUID:90351403; PMID:2386503 !$#accession A61060 !'##status not compared with conceptual translation !'##molecule_type mRNA; DNA !'##residues 2-605,'F',607-663 ##label THI !'##note nucleotide sequence is given only for intron/exon boundaries REFERENCE A27327 !$#authors Thiele, B.J.; Fleming, J.; Kasturi, K.; O'Prey, J.; Black, !1E.; Chester, J.; Rapoport, S.M.; Harrison, P.R. !$#journal Gene (1987) 57:111-119 !$#title Cloning of a rabbit erythroid-cell-specific lipoxygenase !1mRNA. !$#cross-references MUID:88112854; PMID:3123326 !$#accession A27327 !'##molecule_type mRNA !'##residues 1-31 ##label TH2 !'##cross-references GB:M33291 REFERENCE A61568 !$#authors Thiele, B.J.; Black, E.; Fleming, J.; Nack, B.; Rapoport, !1S.M.; Harrison, P.R. !$#journal Biomed. Biochim. Acta (1987) 46:S120-S123 !$#title Cloning of reticulocyte lipoxygenase mRNA. !$#cross-references MUID:87241419; PMID:3109402 !$#accession A61568 !'##molecule_type mRNA !'##residues 1-40,'SHEH',540-582,'S' ##label TH3 !'##note this clone was reevaluated in reference JQ0018 and is thought !1to represent a cloning artifact REFERENCE JC1513 !$#authors O'Prey, J.; Chester, J.; Thiele, B.J.; Janetzki, S.; Prehn, !1S.; Fleming, J.; Harrison, P.R. !$#journal Gene (1989) 84:493-499 !$#title The promoter structure and complete sequence of the gene !1encoding the rabbit erythroid cell-specific 15-lipoxygenase. !$#cross-references MUID:90128296; PMID:2612916 !$#accession JC1513 !'##molecule_type DNA !'##residues 1-112,'T',114-189,'N',191-193,'I',195-663 ##label OPR !'##cross-references GB:M33291; NID:g164731; PIDN:AAA75014.1; !1PID:g164732 COMMENT Rabbit reticulocyte lipoxygenase plays a role in the !1degradation of mitochondria during reticulocyte maturation. COMMENT This enzyme catalyzes the dioxygenation of polyenoic fatty !1acids containing at least one 1,4-cis,cis-pentadiene system. GENETICS !$#gene 15-lox !$#introns 45/3; 114/1; 141/2; 182/2; 217/1; 270/3; 318/3; 388/3; 417/ !13; 474/2; 515/1; 548/3; 604/3 CLASSIFICATION #superfamily arachidonate 5-lipoxygenase KEYWORDS erythrocyte; iron; oxidoreductase SUMMARY #length 663 #molecular-weight 75308 #checksum 820 SEQUENCE /// ENTRY A35087 #type complete TITLE arachidonate 12-lipoxygenase (EC 1.13.11.31) - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A35087 REFERENCE A35087 !$#authors Yoshimoto, T.; Suzuki, H.; Yamamoto, S.; Takai, T.; !1Yokoyama, C.; Tanabe, T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:2142-2146 !$#title Cloning and sequence analysis of the cDNA for arachidonate !112-lipoxygenase of porcine leukocytes. !$#cross-references MUID:90192763; PMID:2315307 !$#accession A35087 !'##status preliminary !'##molecule_type mRNA !'##residues 1-663 ##label YOS !'##cross-references GB:M31417 CLASSIFICATION #superfamily arachidonate 5-lipoxygenase KEYWORDS oxidoreductase SUMMARY #length 663 #molecular-weight 74974 #checksum 4092 SEQUENCE /// ENTRY B54075 #type complete TITLE arachidonate 12-lipoxygenase (EC 1.13.11.31), leukocyte [validated] - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS B54075; I49439 REFERENCE A54075 !$#authors Chen, X.S.; Kurre, U.; Jenkins, N.A.; Copeland, N.G.; Funk, !1C.D. !$#journal J. Biol. Chem. (1994) 269:13979-13987 !$#title cDNA cloning, expression, mutagenesis of C-terminal !1isoleucine, genomic structure, and chromosomal localizations !1of murine 12-lipoxygenases. !$#cross-references MUID:94245713; PMID:8188678 !$#accession B54075 !'##molecule_type DNA; mRNA !'##residues 1-663 ##label CHE !'##cross-references GB:U04331; NID:g467216; PIDN:AAA20658.1; !1PID:g467217 !'##experimental_source strains C57BL/6 and ICR, spleen leukocytes !'##note removal or substitution of Ile-663 abolished enzyme activity REFERENCE I49439 !$#authors Freire-Moar, J.; Alavi-Nassab, A.; Ng, M.; Mulkins, M.; !1Sigal, E. !$#journal Biochim. Biophys. Acta (1995) 1254:112-116 !$#title Cloning and characterization of a murine macrophage !1lipoxygenase. !$#cross-references MUID:95110857; PMID:7811740 !$#accession I49439 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-36,'N',38-118,'Q',120-396,'N',398-663 ##label RES !'##cross-references GB:L34570; NID:g509607; PIDN:AAA64930.1; !1PID:g763530 COMMENT A second arachidonate 12-lipoxygenase from mouse platelets !1is shown in (PIR:A54075). GENETICS !$#map_position 11 CLASSIFICATION #superfamily arachidonate 5-lipoxygenase KEYWORDS oxidoreductase SUMMARY #length 663 #molecular-weight 75444 #checksum 7421 SEQUENCE /// ENTRY S30051 #type complete TITLE arachidonate 12-lipoxygenase (EC 1.13.11.31) - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S30051 REFERENCE S30051 !$#authors Watanabe, T.; Medina, J.F.; Haeggstroem, J.Z.; Radmark, O.; !1Samuelsson, B. !$#journal Eur. J. Biochem. (1993) 212:605-612 !$#title Molecular cloning of a 12-lipoxygenase cDNA from rat brain. !$#cross-references MUID:93185682; PMID:8444196 !$#accession S30051 !'##molecule_type mRNA !'##residues 1-663 ##label WAT !'##cross-references EMBL:L06040; NID:g205212; PIDN:AAA41532.1; !1PID:g205213 CLASSIFICATION #superfamily arachidonate 5-lipoxygenase KEYWORDS oxidoreductase SUMMARY #length 663 #molecular-weight 75391 #checksum 6102 SEQUENCE /// ENTRY DAPSPC #type complete TITLE biphenyl-2,3-diol 1,2-dioxygenase (EC 1.13.11.39) - Pseudomonas sp. (strain KKS102) ALTERNATE_NAMES 2,3-dihydroxybiphenyl dioxygenase ORGANISM #formal_name Pseudomonas sp. DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jun-2000 ACCESSIONS A32312; PC2281; JU0085 REFERENCE A32312 !$#authors Kimbara, K.; Hashimoto, T.; Fukuda, M.; Koana, T.; Takagi, !1M.; Oishi, M.; Yano, K. !$#journal J. Bacteriol. (1989) 171:2740-2747 !$#title Cloning and sequencing of two tandem genes involved in !1degradation of 2,3-dihydroxybiphenyl to benzoic acid in the !1polychlorinated biphenyl-degrading soil bacterium !1Pseudomonas sp. strain KKS102. !$#cross-references MUID:89213965; PMID:2540155 !$#accession A32312 !'##molecule_type DNA !'##residues 1-293 ##label KIM !'##cross-references GB:M26433; NID:g151098; PIDN:AAA25750.1; !1PID:g151099 !'##experimental_source strain KKS102 REFERENCE JC2438 !$#authors Fukuda, M.; Yasukochi, Y.; Kikuchi, Y.; Nagata, Y.; Kimbara, !1K.; Horiuchi, H.; Takagi, M.; Yano, K. !$#journal Biochem. Biophys. Res. Commun. (1994) 202:850-856 !$#title Identification of the bphA and bphB genes of Pseudomonas sp. !1strain KKS102 involved in degradation of biphenyl and !1polychlorinated biphenyls. !$#cross-references MUID:94324977; PMID:8048958 !$#accession PC2281 !'##molecule_type DNA !'##residues 1-16 ##label FUK !'##cross-references DDBJ:D17319; NID:g391831; PIDN:BAA04141.1; !1PID:g391837 GENETICS !$#gene bphC FUNCTION !$#description catalyzes the third step in the major degradative pathway !1for biphenyl and polychlorinated biphenyls (PCBs), cleavage !1of a 2,3-dihydroxybiphenyl derivative at the 1 and 2 !1positions to give a derivative of !12-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate. CLASSIFICATION #superfamily biphenyl-2,3-diol 1,2-dioxygenase KEYWORDS aromatic hydrocarbon catabolism; iron; oxidoreductase; PCB !1biodegradation SUMMARY #length 293 #molecular-weight 32244 #checksum 7776 SEQUENCE /// ENTRY JN0815 #type complete TITLE biphenyl-2,3-diol 1,2-dioxygenase (EC 1.13.11.39) - Pseudomonas sp. (strain LB400) ALTERNATE_NAMES 2,3-dihydroxybiphenyl dioxygenase ORGANISM #formal_name Pseudomonas sp. DATE 10-Mar-1994 #sequence_revision 06-Jan-1995 #text_change 11-Jun-1999 ACCESSIONS JN0815; A45212 REFERENCE PN0632 !$#authors Hofer, B.; Eltis, L.D.; Dowling, D.N.; Timmis, K.N. !$#journal Gene (1993) 130:47-55 !$#title Genetic analysis of a Pseudomonas locus encoding a pathway !1for biphenyl/polychlorinated biphenyl degradation. !$#cross-references MUID:93345822; PMID:8344527 !$#accession JN0815 !'##molecule_type DNA !'##residues 1-298 ##label HOF !'##cross-references GB:X66122; NID:g397882; PIDN:CAA46910.1; !1PID:g397884 !'##experimental_source strain LB400 REFERENCE A45212 !$#authors Eltis, L.D.; Hofmann, B.; Hecht, H.J.; Lunsdorf, H.; Timmis, !1K.N. !$#journal J. Biol. Chem. (1993) 268:2727-2732 !$#title Purification and crystallization of 2,3-dihydroxybiphenyl 1, !12-dioxygenase. !$#cross-references MUID:93155087; PMID:8428946 !$#accession A45212 !'##molecule_type protein !'##residues 2-32 ##label ELT !'##experimental_source expression plasmid pLEBD4 in parent strain LB400 !'##note sequence extracted from NCBI backbone (NCBIP:124194) COMMENT This enzyme catalyzes the third step in the major !1degradative pathway for biphenyl and polychlorinated !1biphenyls (PCBs): cleavage of a 2,3-dihydroxybiphenyl !1derivative at the 1 and 2 positions to give a derivative of !12-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate. COMMENT 3,4-dihydroxybiphenyl was not a substrate. Catechol, !13-methylcatechol, and 4-methylcatechol were inefficient !1substrates. GENETICS !$#gene bphC CLASSIFICATION #superfamily biphenyl-2,3-diol 1,2-dioxygenase KEYWORDS aromatic hydrocarbon catabolism; homooctamer; iron; !1oxidoreductase; PCB biodegradation SUMMARY #length 298 #molecular-weight 32471 #checksum 4005 SEQUENCE /// ENTRY G42409 #type complete TITLE biphenyl-2,3-diol 1,2-dioxygenase (EC 1.13.11.39) - Pseudomonas pseudoalcaligenes ALTERNATE_NAMES 2,3-dihydroxybiphenyl dioxygenase ORGANISM #formal_name Pseudomonas pseudoalcaligenes DATE 03-Feb-1994 #sequence_revision 06-Jan-1995 #text_change 10-Feb-1995 ACCESSIONS G42409 REFERENCE A42409 !$#authors Taira, K.; Hirose, J.; Hayashida, S.; Furukawa, K. !$#journal J. Biol. Chem. (1992) 267:4844-4853 !$#title Analysis of bph operon from the polychlorinated !1biphenyl-degrading strain of Pseudomonas pseudoalcaligenes !1KF707. !$#cross-references MUID:92165849; PMID:1537863 !$#accession G42409 !'##molecule_type DNA !'##residues 1-298 ##label TAI !'##cross-references GB:S75161 !'##experimental_source strain KF707 !'##note sequence extracted from NCBI backbone (NCBIN:84014, !1NCBIP:84023) COMMENT This enzyme catalyzes the third step in the major !1degradative pathway for biphenyl and polychlorinated !1biphenyls (PCBs): cleavage of a 2,3-dihydroxybiphenyl !1derivative at the 1 and 2 positions to give a derivative of !12-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate. GENETICS !$#gene bphC CLASSIFICATION #superfamily biphenyl-2,3-diol 1,2-dioxygenase KEYWORDS aromatic hydrocarbon catabolism; iron; oxidoreductase; PCB !1biodegradation SUMMARY #length 298 #molecular-weight 32499 #checksum 4299 SEQUENCE /// ENTRY B35124 #type complete TITLE biphenyl-2,3-diol 1,2-dioxygenase (EC 1.13.11.39) - Pseudomonas putida ALTERNATE_NAMES 2,3-dihydroxybiphenyl dioxygenase ORGANISM #formal_name Pseudomonas putida DATE 03-Aug-1990 #sequence_revision 06-Jan-1995 #text_change 11-Jun-1999 ACCESSIONS B35124 REFERENCE A35124 !$#authors Hayase, N.; Taira, K.; Furukawa, K. !$#journal J. Bacteriol. (1990) 172:1160-1164 !$#title Pseudomonas putida KF715 bphABCD operon encoding biphenyl !1and polychlorinated biphenyl degradation: cloning, analysis, !1and expression in soil bacteria. !$#cross-references MUID:90130279; PMID:2105297 !$#accession B35124 !'##molecule_type DNA !'##residues 1-292 ##label HAY !'##cross-references GB:M33813; NID:g151105; PIDN:AAA25756.1; !1PID:g151107 !'##experimental_source strain KF715 COMMENT This enzyme catalyzes the third step in the major !1degradative pathway for biphenyl and polychlorinated !1biphenyls (PCBs): cleavage of a 2,3-dihydroxybiphenyl !1derivative at the 1 and 2 positions to give a derivative of !12-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate. GENETICS !$#gene bphC CLASSIFICATION #superfamily biphenyl-2,3-diol 1,2-dioxygenase KEYWORDS aromatic hydrocarbon catabolism; iron; oxidoreductase; PCB !1biodegradation SUMMARY #length 292 #molecular-weight 31947 #checksum 164 SEQUENCE /// ENTRY F36516 #type complete TITLE 3-methylcatechol 2,3-dioxygenase (EC 1.13.11.-) - Pseudomonas putida ORGANISM #formal_name Pseudomonas putida DATE 15-Feb-1991 #sequence_revision 06-Jan-1995 #text_change 11-Jun-1999 ACCESSIONS F36516 REFERENCE A36516 !$#authors Zylstra, G.J.; Gibson, D.T. !$#journal J. Biol. Chem. (1989) 264:14940-14946 !$#title Toluene degradation by Pseudomonas putida F1. Nucleotide !1sequence of the todC1C2BADE genes and their expression in !1Escherichia coli. !$#cross-references MUID:89359301; PMID:2670929 !$#accession F36516 !'##molecule_type DNA !'##residues 1-291 ##label ZYL !'##cross-references GB:J04996; NID:g151600; PIDN:AAA26010.1; !1PID:g151606 !'##experimental_source strain F1 COMMENT This enzyme catalyzes the third step in the major !1degradative pathway for toluene: cleavage of 1, !12-dihydroxytoluene at the 2 and 3 positions to give !12-hydroxy-6-oxo-6-2,4-heptadienoate. GENETICS !$#gene todE CLASSIFICATION #superfamily biphenyl-2,3-diol 1,2-dioxygenase KEYWORDS aromatic hydrocarbon catabolism; iron; oxidoreductase SUMMARY #length 291 #molecular-weight 32209 #checksum 9612 SEQUENCE /// ENTRY B53419 #type complete TITLE biphenyl-2,3-diol 1,2-dioxygenase (EC 1.13.11.39) I - Rhodococcus globerulus ALTERNATE_NAMES 2,3-dihydroxybiphenyl dioxygenase I ORGANISM #formal_name Rhodococcus globerulus DATE 25-May-1994 #sequence_revision 06-Jan-1995 #text_change 11-Jun-1999 ACCESSIONS B53419 REFERENCE A53419 !$#authors Asturias, J.A.; Eltis, L.D.; Prucha, M.; Timmis, K.N. !$#journal J. Biol. Chem. (1994) 269:7807-7815 !$#title Analysis of three 2,3-dihydroxybiphenyl 1,2-dioxygenases !1found in Rhodococcus globerulus P6. Identification of a new !1family of extradiol dioxygenases. !$#cross-references MUID:94171820; PMID:8126007 !$#accession B53419 !'##molecule_type DNA !'##residues 1-291 ##label AST !'##cross-references GB:X75633; NID:g473115; PIDN:CAA53297.1; !1PID:g473117 !'##experimental_source strain P6 COMMENT This enzyme catalyzes the third step in the major !1degradative pathway for biphenyl and polychlorinated !1biphenyls (PCBs): cleavage of a 2,3-dihydroxybiphenyl !1derivative at the 1 and 2 positions to give a derivative of !12-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate. COMMENT This is one of the three biphenyl-2,3-diol 1,2-dioxygenases !1found in R. globerulus P6; it is the only one that exhibits !1homology with the corresponding proteins of analogous !1degradative pathways in gram-negative bacteria. The other !1two, biphenyl-2,3-diol 1,2-dioxygenases II and III, although !1homologous, belong to another class of biphenyl-2,3-diol 1, !12-dioxygenases. GENETICS !$#gene bphC1 CLASSIFICATION #superfamily biphenyl-2,3-diol 1,2-dioxygenase KEYWORDS aromatic hydrocarbon catabolism; iron; oxidoreductase; PCB !1biodegradation SUMMARY #length 291 #molecular-weight 32081 #checksum 1071 SEQUENCE /// ENTRY C53419 #type complete TITLE biphenyl-2,3-diol 1,2-dioxygenase (EC 1.13.11.39) II - Rhodococcus globerulus ALTERNATE_NAMES 2,3-dihydroxybiphenyl dioxygenase II ORGANISM #formal_name Rhodococcus globerulus DATE 25-May-1994 #sequence_revision 06-Jan-1995 #text_change 11-Jun-1999 ACCESSIONS C53419 REFERENCE A53419 !$#authors Asturias, J.A.; Eltis, L.D.; Prucha, M.; Timmis, K.N. !$#journal J. Biol. Chem. (1994) 269:7807-7815 !$#title Analysis of three 2,3-dihydroxybiphenyl 1,2-dioxygenases !1found in Rhodococcus globerulus P6. Identification of a new !1family of extradiol dioxygenases. !$#cross-references MUID:94171820; PMID:8126007 !$#accession C53419 !'##molecule_type DNA !'##residues 1-190 ##label AST !'##cross-references GB:X75634; NID:g473118; PIDN:CAA53298.1; !1PID:g473119 !'##experimental_source strain P6 COMMENT This enzyme catalyzes the third step in the major !1degradative pathway for biphenyl and polychlorinated !1biphenyls (PCBs): cleavage of a 2,3-dihydroxybiphenyl !1derivative at the 1 and 2 positions to give a derivative of !12-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate. COMMENT This is one of the three biphenyl-2,3-diol 1,2-dioxygenases !1found in R. globerulus P6. It is homologous to biphenyl-2, !13-diol 1,2-dioxygenase III but differs from the other !1biphenyl-2,3-diol 1,2-dioxygenase dioxygenases. COMMENT The active enzyme is a hexamer of identical chains !1containing one tightly bound iron per chain. GENETICS !$#gene bphC2 CLASSIFICATION #superfamily R. globerulus biphenyl-2,3-diol 1,2-dioxygenase !1II KEYWORDS aromatic hydrocarbon catabolism; homohexamer; iron; !1oxidoreductase; PCB biodegradation SUMMARY #length 190 #molecular-weight 20844 #checksum 4024 SEQUENCE /// ENTRY D53419 #type complete TITLE biphenyl-2,3-diol 1,2-dioxygenase (EC 1.13.11.39) III - Rhodococcus globerulus ALTERNATE_NAMES 2,3-dihydroxybiphenyl dioxygenase III ORGANISM #formal_name Rhodococcus globerulus DATE 25-May-1994 #sequence_revision 06-Jan-1995 #text_change 11-Jun-1999 ACCESSIONS D53419 REFERENCE A53419 !$#authors Asturias, J.A.; Eltis, L.D.; Prucha, M.; Timmis, K.N. !$#journal J. Biol. Chem. (1994) 269:7807-7815 !$#title Analysis of three 2,3-dihydroxybiphenyl 1,2-dioxygenases !1found in Rhodococcus globerulus P6. Identification of a new !1family of extradiol dioxygenases. !$#cross-references MUID:94171820; PMID:8126007 !$#accession D53419 !'##molecule_type DNA !'##residues 1-190 ##label AST !'##cross-references GB:X75635; NID:g473120; PIDN:CAA53299.1; !1PID:g473121 !'##experimental_source strain P6 COMMENT This enzyme catalyzes the third step in the major !1degradative pathway for biphenyl and polychlorinated !1biphenyls (PCBs): cleavage of a 2,3-dihydroxybiphenyl !1derivative at the 1 and 2 positions to give a derivative of !12-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate. COMMENT This is one of the three biphenyl-2,3-diol 1,2-dioxygenases !1found in R. globerulus P6. It is homologous to biphenyl-2, !13-diol 1,2-dioxygenase II but differs from the other !1biphenyl-2,3-diol 1,2-dioxygenase dioxygenases. COMMENT The active enzyme may be a hexamer of identical chains !1containing one tightly bound iron per chain. GENETICS !$#gene bphC3 CLASSIFICATION #superfamily R. globerulus biphenyl-2,3-diol 1,2-dioxygenase !1II KEYWORDS aromatic hydrocarbon catabolism; homohexamer; iron; !1oxidoreductase; PCB biodegradation SUMMARY #length 190 #molecular-weight 21191 #checksum 4827 SEQUENCE /// ENTRY DAAGWT #type complete TITLE tryptophan 2-monooxygenase (EC 1.13.12.3) TA - Agrobacterium tumefaciens plasmid pTiTm4 ORGANISM #formal_name Agrobacterium tumefaciens DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 09-Jun-2000 ACCESSIONS S15002; S15450 REFERENCE S15001 !$#authors Bonnard, G.; Vincent, F.; Otten, L. !$#journal Plant Mol. Biol. (1991) 16:733-738 !$#title Sequence of Agrobacterium tumefaciens biotype III auxin !1genes. !$#cross-references MUID:91329707; PMID:1868204 !$#accession S15002 !'##molecule_type DNA !'##residues 1-755 ##label BO2 !'##cross-references EMBL:X56185; NID:g39133; PIDN:CAA39646.1; !1PID:g39134 !'##experimental_source strain Tm4; strain octopine GENETICS !$#gene iaaM !$#genome plasmid pTiTm4 FUNCTION !$#pathway tryptophan metabolism; auxin biosynthesis !$#note catalyzes the first step in the biosynthesis of auxins from !1tryptophan CLASSIFICATION #superfamily Agrobacterium plasmid tryptophan !12-monooxygenase KEYWORDS monooxygenase; oxidoreductase SUMMARY #length 755 #molecular-weight 83972 #checksum 8243 SEQUENCE /// ENTRY QQAG4T #type complete TITLE tryptophan 2-monooxygenase (EC 1.13.12.3) - Agrobacterium tumefaciens plasmids pTiAch5, pTi15955, and pTiA6NC ORGANISM #formal_name Agrobacterium tumefaciens DATE 13-Aug-1986 #sequence_revision 13-Aug-1986 #text_change 09-Jun-2000 ACCESSIONS A04497; S28687; A20966 REFERENCE A91001 !$#authors Gielen, J.; De Beuckeleer, M.; Seurinck, J.; Deboeck, F.; De !1Greve, H.; Lemmers, M.; Van Montagu, M.; Schell, J. !$#journal EMBO J. (1984) 3:835-846 !$#title The complete nucleotide sequence of the TL-DNA of the !1Agrobacterium tumefaciens plasmid pTiAch5. !$#cross-references MUID:84207942; PMID:6327292 !$#accession A04497 !'##molecule_type DNA !'##residues 1-755 ##label GIE !'##genetics G1 REFERENCE S28683 !$#authors Barker, R.F.; Idler, K.B.; Thompson, D.V.; Kemp, J.D. !$#journal Plant Mol. Biol. (1983) 2:335-350 !$#title Nucleotide sequence of the T-DNA region from the !1Agrobacterium tumefaciens octopine Ti plasmid pTi15955. !$#accession S28687 !'##status translation not shown !'##molecule_type DNA !'##residues 1-362,'H',364-596,'S',598-717,'IQ',720,'A',722-755 ##label !1BAR !'##cross-references EMBL:X00493; NID:g39062; PIDN:CAA25167.1; !1PID:g39067 !'##experimental_source strain octopine !'##genetics G2 REFERENCE A20966 !$#authors Klee, H.; Montoya, A.; Horodyski, F.; Lichtenstein, C.; !1Garfinkel, D.; Fuller, S.; Flores, C.; Peschon, J.; Nester, !1E.; Gordon, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:1728-1732 !$#title Nucleotide sequence of the tms genes of the pTiA6NC octopine !1Ti plasmid: two gene products involved in plant !1tumorigenesis. !$#cross-references MUID:84170374; PMID:6584906 !$#accession A20966 !'##molecule_type DNA !'##residues 1-717,'IQ',720,'A',722-755 ##label KLE !'##cross-references GB:K02554; NID:g154747; PIDN:AAA92550.1; !1PID:g154750 !'##experimental_source strain octopine !'##genetics G3 GENETICS G1 !$#genome plasmid !$#note plasmid pTiAch5 GENETICS G2 !$#genome plasmid !$#note plasmid pTi15955 GENETICS G3 !$#gene tms1 !$#genome plasmid !$#note plasmid pTiA6NC FUNCTION !$#pathway tryptophan metabolism; auxin biosynthesis !$#note catalyzes the first step in the biosynthesis of auxins from !1tryptophan CLASSIFICATION #superfamily Agrobacterium plasmid tryptophan !12-monooxygenase KEYWORDS monooxygenase; oxidoreductase SUMMARY #length 755 #molecular-weight 83946 #checksum 540 SEQUENCE /// ENTRY S30105 #type complete TITLE tryptophan 2-monooxygenase (EC 1.13.12.3) - Agrobacterium vitis plasmid pTiS4 ORGANISM #formal_name Agrobacterium vitis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS S30105 REFERENCE S30104 !$#authors Canaday, J.; Gerard, J.C.; Crouzet, P.; Otten, L. !$#journal Mol. Gen. Genet. (1992) 235:292-303 !$#title Organization and functional analysis of three T-DNAs from !1the vitopine Ti plasmid pTiS4. !$#cross-references MUID:93101133; PMID:1465104 !$#accession S30105 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-723 ##label CAN !'##cross-references EMBL:M91609; NID:g149127; PIDN:AAA98149.1; !1PID:g149129 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1992 GENETICS !$#gene iaaM !$#genome plasmid CLASSIFICATION #superfamily Agrobacterium plasmid tryptophan !12-monooxygenase KEYWORDS monooxygenase; oxidoreductase SUMMARY #length 723 #molecular-weight 80802 #checksum 5997 SEQUENCE /// ENTRY A25493 #type complete TITLE tryptophan 2-monooxygenase (EC 1.13.12.3) - Pseudomonas syringae pv. savastanoi ORGANISM #formal_name Pseudomonas syringae pv. savastanoi DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS A25493 REFERENCE A94062 !$#authors Yamada, T.; Palm, C.J.; Brooks, B.; Kosuge, T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:6522-6526 !$#title Nucleotide sequences of the Pseudomonas savastanoi !1indoleacetic acid genes show homology with Agrobacterium !1tumefaciens T-DNA. !$#accession A25493 !'##molecule_type DNA !'##residues 1-557 ##label YAM GENETICS !$#gene iaaM CLASSIFICATION #superfamily Pseudomonas tryptophan 2-monooxygenase KEYWORDS monooxygenase; oxidoreductase SUMMARY #length 557 #molecular-weight 61861 #checksum 1040 SEQUENCE /// ENTRY A53376 #type complete TITLE tryptophan 2-monooxygenase (EC 1.13.12.3) - Pseudomonas syringae pv. syringae ORGANISM #formal_name Pseudomonas syringae pv. syringae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS A53376 REFERENCE A53376 !$#authors Mazzola, M.; White, F.F. !$#journal J. Bacteriol. (1994) 176:1374-1382 !$#title A mutation in the indole-3-acetic acid biosynthesis pathway !1of Pseudomonas syringae pv. syringae affects growth in !1Phaseolus vulgaris and syringomycin production. !$#cross-references MUID:94156842; PMID:8113177 !$#accession A53376 !'##status preliminary !'##molecule_type DNA !'##residues 1-556 ##label MAZ !'##cross-references GB:U04358; NID:g472559; PIDN:AAA17678.1; !1PID:g472560 GENETICS !$#gene iaaM CLASSIFICATION #superfamily Pseudomonas tryptophan 2-monooxygenase KEYWORDS monooxygenase; oxidoreductase SUMMARY #length 556 #molecular-weight 61691 #checksum 8749 SEQUENCE /// ENTRY DAHUA1 #type complete TITLE procollagen-proline dioxygenase (EC 1.14.11.2) alpha chain precursor, splice form 1 - human ALTERNATE_NAMES procollagen-proline,2-oxoglutarate 4-dioxygenase alpha chain; proline hydroxylase; proline,2-oxoglutarate 4-dioxygenase; prolyl 4-hydroxylase; protocollagen hydroxylase ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-May-2000 ACCESSIONS A33919; I37174 REFERENCE A33919 !$#authors Helaakoski, T.; Vuori, K.; Myllylae, R.; Kivirikko, K.I.; !1Pihlajaniemi, T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:4392-4396 !$#title Molecular cloning of the alpha-subunit of human prolyl !14-hydroxylase: the complete cDNA-derived amino acid sequence !1and evidence for alternative splicing of RNA transcripts. !$#cross-references MUID:89282778; PMID:2543975 !$#accession A33919 !'##molecule_type mRNA !'##residues 1-534 ##label HEL !'##cross-references GB:M24486 !'##note this sequence follows the authors' translation for residues !1119-122 REFERENCE A57298 !$#authors Lamberg, A.; Pihlajaniemi, T.; Kivirikko, K.I. !$#journal J. Biol. Chem. (1995) 270:9926-9931 !$#title Site-directed mutagenesis of the alpha subunit of human !1prolyl 4-hydroxylase. Identification of three histidine !1residues critical for catalytic activity. !$#cross-references MUID:95247786; PMID:7730375 !$#contents annotation; iron binding site !$#note Cys-503 and 528 are predicted to form interchain disulfide !1bonds with either alpha or beta chains REFERENCE I37173 !$#authors Helaakoski, T.; Veijola, J.; Vuori, K.; Rehn, M.; Chow, !1L.T.; Taillon-Miller, P.; Kivirikko, K.I.; Pihlajaniemi, T. !$#journal J. Biol. Chem. (1994) 269:27847-27854 !$#title Structure and expression of the human gene for the !1alpha-subunit of prolyl 4-hydroxylase. !$#cross-references MUID:95050550; PMID:7961714 !$#accession I37174 !'##molecule_type DNA !'##residues 1-534 ##label RES !'##cross-references EMBL:U14620; NID:g602673; PIDN:AAA59069.1; !1PID:g602676 COMMENT The carboxyl-terminal four residues may function as an !1endoplasmic reticulum retention signal. The beta chain has !1the classic Lys-Asp-Glu-Leu retention signal and may help to !1retain the alpha chain. GENETICS !$#gene GDB:P4HA !'##cross-references GDB:120257; OMIM:176710 !$#map_position 10q21.3-10q23.1 !$#introns 26/1; 58/2; 109/1; 155/1; 235/1; 300/3; 359/3; 383/2; 416/3; !1434/3; 456/3; 479/3; 512/1 COMPLEX heterotetramer of two alpha chains and two beta chains (see !1PIR:ISHUSS) FUNCTION !$#description 4-hydroxylates proline residues in the G-X-P-G motif of !1collagen and collagen-like molecules !$#pathway collagen synthesis CLASSIFICATION #superfamily procollagen-proline,2-oxoglutarate !14-dioxygenase alpha chain KEYWORDS alternative splicing; ascorbic acid; endoplasmic reticulum; !1glycoprotein; heterotetramer; iron; metalloprotein; !1oxidoreductase FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-534 #product procollagen-proline dioxygenase alpha chain, !8splice form 1 #status predicted #label MAT\ !$531-534 #region endoplasmic reticulum retention signal !8#status atypical\ !$113,259 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$429,500,518 #binding_site iron (His) #status predicted\ !$503,528 #disulfide_bonds interchain #status predicted SUMMARY #length 534 #molecular-weight 60967 #checksum 9237 SEQUENCE /// ENTRY DAHUA2 #type complete TITLE procollagen-proline dioxygenase (EC 1.14.11.2) alpha chain precursor, splice form 2 - human ALTERNATE_NAMES procollagen-proline,2-oxoglutarate 4-dioxygenase alpha chain; proline hydroxylase; proline,2-oxoglutarate 4-dioxygenase; prolyl 4-hydroxylase; protocollagen hydroxylase ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-May-2000 ACCESSIONS I37173; B33919 REFERENCE I37173 !$#authors Helaakoski, T.; Veijola, J.; Vuori, K.; Rehn, M.; Chow, !1L.T.; Taillon-Miller, P.; Kivirikko, K.I.; Pihlajaniemi, T. !$#journal J. Biol. Chem. (1994) 269:27847-27854 !$#title Structure and expression of the human gene for the !1alpha-subunit of prolyl 4-hydroxylase. !$#cross-references MUID:95050550; PMID:7961714 !$#accession I37173 !'##molecule_type DNA !'##residues 1-534 ##label RES !'##cross-references EMBL:U14620; NID:g602673; PIDN:AAA59068.1; !1PID:g602675 REFERENCE A33919 !$#authors Helaakoski, T.; Vuori, K.; Myllylae, R.; Kivirikko, K.I.; !1Pihlajaniemi, T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:4392-4396 !$#title Molecular cloning of the alpha-subunit of human prolyl !14-hydroxylase: the complete cDNA-derived amino acid sequence !1and evidence for alternative splicing of RNA transcripts. !$#cross-references MUID:89282778; PMID:2543975 !$#accession B33919 !'##molecule_type mRNA !'##residues 1-534 ##label HEL !'##cross-references GB:M24487 !'##note this sequence follows the authors' translation for residues !1119-122 REFERENCE A57298 !$#authors Lamberg, A.; Pihlajaniemi, T.; Kivirikko, K.I. !$#journal J. Biol. Chem. (1995) 270:9926-9931 !$#title Site-directed mutagenesis of the alpha subunit of human !1prolyl 4-hydroxylase. Identification of three histidine !1residues critical for catalytic activity. !$#cross-references MUID:95247786; PMID:7730375 !$#contents annotation; iron binding site !$#note Cys-503 and 528 are predicted to form interchain disulfide !1bonds with either alpha or beta chains COMMENT The carboxyl-terminal four residues may function as an !1endoplasmic reticulum retention signal. The beta chain has !1the classic Lys-Asp-Glu-Leu retention signal and may help to !1retain the alpha chain. GENETICS !$#gene GDB:P4HA !'##cross-references GDB:120257; OMIM:176710 !$#map_position 10q21.3-10q23.1 !$#introns 26/1; 58/2; 109/1; 155/1; 235/1; 300/3; 359/3; 383/2; 416/3; !1434/3; 456/3; 479/3; 512/1 COMPLEX heterotetramer of two alpha chains and two beta chains (see !1PIR:ISHUSS) FUNCTION !$#description 4-hydroxylates proline residues in the G-X-P-G motif of !1collagen and collagen-like molecules !$#pathway collagen synthesis CLASSIFICATION #superfamily procollagen-proline,2-oxoglutarate !14-dioxygenase alpha chain KEYWORDS alternative splicing; ascorbic acid; endoplasmic reticulum; !1glycoprotein; heterotetramer; iron; metalloprotein; !1oxidoreductase FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-534 #product procollagen-proline dioxygenase alpha chain, !8form 2 #status predicted #label MAT\ !$531-534 #region endoplasmic reticulum retention signal !8#status atypical\ !$113,259 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$429,500,518 #binding_site iron (His) #status predicted\ !$503,528 #disulfide_bonds interchain #status predicted SUMMARY #length 534 #molecular-weight 61049 #checksum 8756 SEQUENCE /// ENTRY DACHA #type complete TITLE procollagen-proline dioxygenase (EC 1.14.11.2) alpha chain - chicken ALTERNATE_NAMES procollagen-proline,2-oxoglutarate 4-dioxygenase alpha chain; proline hydroxylase; proline,2-oxoglutarate 4-dioxygenase; prolyl 4-hydroxylase; protocollagen hydroxylase ORGANISM #formal_name Gallus gallus #common_name chicken DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-May-2000 ACCESSIONS A33832; B33832 REFERENCE A33832 !$#authors Bassuk, J.A.; Kao, W.W.Y.; Herzer, P.; Kedersha, N.L.; !1Seyer, J.; DeMartino, J.A.; Daugherty, B.L.; Mark III, G.E.; !1Berg, R.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:7382-7386 !$#title Prolyl 4-hydroxylase: molecular cloning and the primary !1structure of the alpha-subunit from chicken embryo. !$#cross-references MUID:90017483; PMID:2552442 !$#accession A33832 !'##molecule_type mRNA !'##residues 43-516 ##label BAS !'##cross-references GB:M26217 !$#accession B33832 !'##molecule_type protein !'##residues 1-42;210-220;229-246;439-450 ##label BAS2 COMMENT This protein is a heterotetramer of two alpha chains and two !1beta chains; the beta chain is protein disulfide-isomerase. COMMENT The carboxyl-terminal four residues may function as an !1endoplasmic reticulum retention signal. The beta chain has !1the classic Lys-Asp-Glu-Leu retention signal and may help to !1retain the alpha chain. CLASSIFICATION #superfamily procollagen-proline,2-oxoglutarate !14-dioxygenase alpha chain KEYWORDS ascorbic acid; endoplasmic reticulum; glycoprotein; !1heterotetramer; oxidoreductase FEATURE !$513-516 #region endoplasmic reticulum retention signal !8#status atypical\ !$97,243 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 516 #molecular-weight 59440 #checksum 3353 SEQUENCE /// ENTRY A38206 #type complete TITLE procollagen-lysine 5-dioxygenase (EC 1.14.11.4) 1 precursor - human ALTERNATE_NAMES lysyl hydroxylase; procollagen-lysine, 2-oxoglutarate 5-dioxygenase ORGANISM #formal_name Homo sapiens #common_name man DATE 24-Nov-1999 #sequence_revision 24-Nov-1999 #text_change 19-May-2000 ACCESSIONS A38206 REFERENCE A38206 !$#authors Hautala, T.; Byers, M.G.; Eddy, R.L.; Shows, T.B.; !1Kivirikko, K.I.; Myllylae, R. !$#journal Genomics (1992) 13:62-69 !$#title Cloning of human lysyl hydroxylase: complete cDNA-derived !1amino acid sequence and assignment of the gene (PLOD) to !1chromosome 1p36.3->p36.2. !$#cross-references MUID:92250066; PMID:1577494 !$#accession A38206 !'##molecule_type mRNA !'##residues 1-727 ##label HAU !'##cross-references GB:L06419; NID:g190073; PIDN:AAA60116.1; !1PID:g190074 !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing GENETICS !$#gene GDB:PLOD; LLH !'##cross-references GDB:127821; OMIM:153454; OMIM:225400 !$#map_position 1p36.3-1p36.2 !$#note defects in this gene can cause type VI Ehlers-Danlos !1syndrome FUNCTION !$#description catalyzes the 5-hydroxylation of certain collagen lysine !1residues by oxygen and 2-oxoglutarate to form succinate and !1carbon dioxide !$#note iron and ascorbic acid are cofactors CLASSIFICATION #superfamily human procollagen-lysine 5-dioxygenase KEYWORDS ascorbic acid; Ehlers-Danlos syndrome; glycoprotein; !1homodimer; oxidoreductase FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-727 #product procollagen-lysine 5-dioxygenase #status !8predicted #label MAT\ !$163,197,538,686 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 727 #molecular-weight 83580 #checksum 2247 SEQUENCE /// ENTRY A40005 #type complete TITLE hyoscyamine (6S)-dioxygenase (EC 1.14.11.11) - henbane ORGANISM #formal_name Hyoscyamus niger #common_name henbane DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-May-2000 ACCESSIONS A40005 REFERENCE A40005 !$#authors Matsuda, J.; Okabe, S.; Hashimoto, T.; Yamada, Y. !$#journal J. Biol. Chem. (1991) 266:9460-9464 !$#title Molecular cloning of hyoscyamine 6beta-hydroxylase, a !12-oxoglutarate-dependent dioxygenase, from cultured roots of !1Hyoscyamus niger. !$#cross-references MUID:91236712; PMID:2033047 !$#accession A40005 !'##status preliminary !'##molecule_type mRNA !'##residues 1-344 ##label MAT !'##cross-references GB:M62719; NID:g168267; PIDN:AAA33387.1; !1PID:g168268 CLASSIFICATION #superfamily 1-aminocyclopropane-1-carboxylate oxidase KEYWORDS ascorbic acid; iron; metalloprotein; oxidoreductase FEATURE !$66,217,274 #binding_site iron (His) #status predicted SUMMARY #length 344 #molecular-weight 39000 #checksum 442 SEQUENCE /// ENTRY T01935 #type complete TITLE naringenin 3-dioxygenase (EC 1.14.11.9) - common tobacco ALTERNATE_NAMES flavanone 3-hydroxylase ORGANISM #formal_name Nicotiana tabacum #common_name common tobacco DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-May-2000 ACCESSIONS T01935 REFERENCE Z14463 !$#authors Kim, G.; Kim, Y. !$#journal Plant Physiol. (1998) 116:1605 !$#title Flavanone 3-hydroxylase (Accession No. AF036093) cloning and !1sequencing from Nicotiana tabacum (PGR98-070). !$#accession T01935 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-621 ##label KIM !'##cross-references EMBL:AF036093; NID:g2828005; PIDN:AAC15414.1; !1PID:g2828006 !'##experimental_source tissue-type petal CLASSIFICATION #superfamily tobacco naringenin 3-dioxygenase KEYWORDS ascorbic acid; oxidoreductase SUMMARY #length 621 #molecular-weight 70367 #checksum 4389 SEQUENCE /// ENTRY BABOH #type complete TITLE peptide-aspartate beta-dioxygenase (EC 1.14.11.16) - bovine ALTERNATE_NAMES aspartyl (asparaginyl) beta-hydroxylase ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Dec-1993 #sequence_revision 10-Feb-1995 #text_change 11-Jun-1999 ACCESSIONS A42969; A39470; B39470; C39470; S27948 REFERENCE A42969 !$#authors Jia, S.; VanDusen, W.J.; Diehl, R.E.; Kohl, N.E.; Dixon, !1R.A.; Elliston, K.O.; Stern, A.M.; Friedman, P.A. !$#journal J. Biol. Chem. (1992) 267:14322-14327 !$#title cDNA cloning and expression of bovine aspartyl (asparaginyl) !1beta-hydroxylase. !$#cross-references MUID:92332546; PMID:1378441 !$#accession A42969 !'##molecule_type mRNA !'##residues 1-754 ##label JIA !'##cross-references EMBL:M91213; NID:g162693; PIDN:AAA03563.1; !1PID:g162694 !'##experimental_source brain !'##note sequence extracted from NCBI backbone (NCBIP:108534) REFERENCE A39470 !$#authors Wang, Q.; VanDusen, W.J.; Petroski, C.J.; Garsky, V.M.; !1Stern, A.M.; Friedman, P.A. !$#journal J. Biol. Chem. (1991) 266:14004-14010 !$#title Bovine liver aspartyl beta-hydroxylase. Purification and !1characterization. !$#cross-references MUID:91310689; PMID:1856229 !$#accession A39470 !'##molecule_type protein !'##residues 289-328 ##label WAN !$#accession B39470 !'##molecule_type protein !'##residues 615,'X',617-630,'XX',633-634,'X',636,'XX',639-641 ##label !1WA2 !$#accession C39470 !'##molecule_type protein !'##residues 311-347,'X',349,'X',351-373,'X',375-379,'X',381-382 ##label !1WA3 COMMENT This enzyme uses ferrous iron as a cofactor, and while !1beta-hydroxylating the peptidyl-aspartate substrate converts !1alpha-ketoglutarate to succinate and releases carbon !1dioxide. COMMENT Aspartic acid and asparagine residues in the EGF homology !1domain of certain plasma proteins serve as the !1peptidyl-aspartate substrate. CLASSIFICATION #superfamily peptide-aspartate beta-dioxygenase; !1tetratricopeptide repeat homology KEYWORDS glycoprotein; oxidoreductase; transmembrane protein FEATURE !$2-56 #domain intracellular #status predicted #label INC\ !$57-78 #domain transmembrane #status predicted #label TRM\ !$289-754 #product peptide-aspartate beta-dioxygenase, 56K form !8#status predicted #label 56K\ !$311-754 #product peptide-aspartate beta-dioxygenase, 52K form !8#status predicted #label 52K\ !$337-370 #domain tetratricopeptide repeat homology #label TT1\ !$371-404 #domain tetratricopeptide repeat homology #label TT2\ !$13,96,466,702 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 754 #molecular-weight 84998 #checksum 9667 SEQUENCE /// ENTRY A36516 #type complete TITLE toluene dioxygenase (EC 1.14.12.11) terminal oxygenase component large chain - Pseudomonas putida ORGANISM #formal_name Pseudomonas putida DATE 15-Feb-1991 #sequence_revision 06-Jan-1995 #text_change 18-Jun-1999 ACCESSIONS A36516 REFERENCE A36516 !$#authors Zylstra, G.J.; Gibson, D.T. !$#journal J. Biol. Chem. (1989) 264:14940-14946 !$#title Toluene degradation by Pseudomonas putida F1. Nucleotide !1sequence of the todC1C2BADE genes and their expression in !1Escherichia coli. !$#cross-references MUID:89359301; PMID:2670929 !$#accession A36516 !'##molecule_type DNA !'##residues 1-450 ##label ZYL !'##cross-references GB:J04996; NID:g151600; PIDN:AAA26005.1; !1PID:g151601 !'##experimental_source strain F1 GENETICS !$#gene todC1 CLASSIFICATION #superfamily toluene dioxygenase terminal oxygenase !1component large chain; Rieske [2Fe-2S] homology KEYWORDS 2Fe-2S; aromatic hydrocarbon catabolism; metalloprotein; !1oxidoreductase; Rieske iron-sulfur protein FEATURE !$86-134 #domain Rieske [2Fe-2S] homology #label RSK\ !$96,98,116,119 #binding_site 2Fe-2S cluster (Cys, His, Cys, His) !8(covalent) #status predicted SUMMARY #length 450 #molecular-weight 50944 #checksum 1371 SEQUENCE /// ENTRY A29830 #type complete TITLE benzene 1,2-dioxygenase (EC 1.14.12.3) terminal oxygenase component large chain - Pseudomonas putida ALTERNATE_NAMES 50K benzene oxidation protein; benzene 1,2-dioxygenase (EC 1.14.12.3) terminal oxygenase component alph chain ORGANISM #formal_name Pseudomonas putida DATE 30-Jun-1989 #sequence_revision 06-Jan-1995 #text_change 18-Jun-1999 ACCESSIONS A29830 REFERENCE A91848 !$#authors Irie, S.; Doi, S.; Yorifuji, T.; Takagi, M.; Yano, K. !$#journal J. Bacteriol. (1987) 169:5174-5179 !$#title Nucleotide sequencing and characterization of the genes !1encoding benzene oxidation enzymes of Pseudomonas putida. !$#cross-references MUID:88032840; PMID:3667527 !$#accession A29830 !'##molecule_type DNA !'##residues 1-448 ##label IRI !'##cross-references GB:M17904; NID:g151068; PIDN:AAA25735.1; !1PID:g151069 !'##experimental_source strain 136R-3 CLASSIFICATION #superfamily toluene dioxygenase terminal oxygenase !1component large chain; Rieske [2Fe-2S] homology KEYWORDS 2Fe-2S; aromatic hydrocarbon catabolism; metalloprotein; !1oxidoreductase; Rieske iron-sulfur protein FEATURE !$86-134 #domain Rieske [2Fe-2S] homology #label RSK\ !$96,98,116,119 #binding_site 2Fe-2S cluster (Cys, His, Cys, His) !8(covalent) #status predicted SUMMARY #length 448 #molecular-weight 50208 #checksum 4582 SEQUENCE /// ENTRY JN0812 #type complete TITLE benzene 1,2-dioxygenase (EC 1.14.12.3) terminal oxygenase component large chain - Pseudomonas putida (strain ML2) plasmid pHMT112 ORGANISM #formal_name Pseudomonas putida DATE 19-May-1994 #sequence_revision 06-Jan-1995 #text_change 21-Jul-2000 ACCESSIONS JN0812 REFERENCE JN0810 !$#authors Tan, H.M.; Tang, H.Y.; Joannou, C.L.; Abdel-Wahab, N.H.; !1Mason, J.R. !$#journal Gene (1993) 130:33-39 !$#title The Pseudomonas putida ML2 plasmid-encoded genes for benzene !1dioxygenase are unusual in codon usage and low in G+C !1content. !$#cross-references MUID:93345820; PMID:8344526 !$#accession JN0812 !'##molecule_type DNA !'##residues 1-450 ##label TAN !'##cross-references GB:L04642; GB:L04643; NID:g6552505; !1PIDN:AAA17758.1; PID:g309855 !'##experimental_source strain ML2 COMMENT This enzyme is involved in catalyzing the oxidation of !1benzene to cis-1,2-dihydroxy-cyclohexa-3,5-diene. COMMENT The reduced enzyme catalyzes the oxidation of benzene to !1cis-benzene dihydrodiol. GENETICS !$#gene bedC1 !$#genome plasmid CLASSIFICATION #superfamily toluene dioxygenase terminal oxygenase !1component large chain; Rieske [2Fe-2S] homology KEYWORDS 2Fe-2S; aromatic hydrocarbon catabolism; metalloprotein; !1oxidoreductase; Rieske iron-sulfur protein FEATURE !$86-134 #domain Rieske [2Fe-2S] homology #label RSK\ !$96,98,116,119 #binding_site 2Fe-2S cluster (Cys, His, Cys, His) !8(covalent) #status predicted SUMMARY #length 450 #molecular-weight 51108 #checksum 8180 SEQUENCE /// ENTRY B41858 #type complete TITLE biphenyl dioxygenase (EC 1.14.12.-) terminal oxygenase component large chain - Pseudomonas sp. ORGANISM #formal_name Pseudomonas sp. DATE 04-Mar-1993 #sequence_revision 06-Jan-1995 #text_change 05-May-2000 ACCESSIONS B41858 REFERENCE A41858 !$#authors Erickson, B.D.; Mondello, F.J. !$#journal J. Bacteriol. (1992) 174:2903-2912 !$#title Nucleotide sequencing and transcriptional mapping of the !1genes encoding biphenyl dioxygenase, a multicomponent !1polychlorinated-biphenyl-degrading enzyme in Pseudomonas !1strain LB400. !$#cross-references MUID:92234948; PMID:1569021 !$#accession B41858 !'##molecule_type DNA !'##residues 1-459 ##label ERI !'##cross-references GB:M86348; NID:g349602; PIDN:AAB63425.1; !1PID:g151084 !'##experimental_source strain LB400 !'##note sequence extracted from NCBI backbone (NCBIN:97256, !1NCBIP:97259) GENETICS !$#gene bphA1; bphA CLASSIFICATION #superfamily toluene dioxygenase terminal oxygenase !1component large chain; Rieske [2Fe-2S] homology KEYWORDS 2Fe-2S; aromatic hydrocarbon catabolism; metalloprotein; !1oxidoreductase; PCB biodegradation; Rieske iron-sulfur !1protein FEATURE !$90-138 #domain Rieske [2Fe-2S] homology #label RSK\ !$100,102,120,123 #binding_site 2Fe-2S cluster (Cys, His, Cys, His) !8(covalent) #status predicted SUMMARY #length 459 #molecular-weight 51513 #checksum 4694 SEQUENCE /// ENTRY A42409 #type complete TITLE biphenyl dioxygenase (EC 1.14.-.-) terminal oxygenase component large chain - Pseudomonas pseudoalcaligenes ORGANISM #formal_name Pseudomonas pseudoalcaligenes DATE 04-Mar-1993 #sequence_revision 06-Jan-1995 #text_change 18-Jun-1999 ACCESSIONS A42409 REFERENCE A42409 !$#authors Taira, K.; Hirose, J.; Hayashida, S.; Furukawa, K. !$#journal J. Biol. Chem. (1992) 267:4844-4853 !$#title Analysis of bph operon from the polychlorinated !1biphenyl-degrading strain of Pseudomonas pseudoalcaligenes !1KF707. !$#cross-references MUID:92165849; PMID:1537863 !$#accession A42409 !'##molecule_type DNA !'##residues 1-458 ##label TAI !'##cross-references GB:M83673; NID:g151090; PIDN:AAA25743.1; !1PID:g151091 !'##experimental_source strain KF707 !'##note sequence extracted from NCBI backbone (NCBIN:84014, !1NCBIP:84016) GENETICS !$#gene bphA1; bphA CLASSIFICATION #superfamily toluene dioxygenase terminal oxygenase !1component large chain; Rieske [2Fe-2S] homology KEYWORDS 2Fe-2S; aromatic hydrocarbon catabolism; metalloprotein; !1oxidoreductase; PCB biodegradation; Rieske iron-sulfur !1protein FEATURE !$90-138 #domain Rieske [2Fe-2S] homology #label RSK\ !$100,102,120,123 #binding_site 2Fe-2S cluster (Cys, His, Cys, His) !8(covalent) #status predicted SUMMARY #length 458 #molecular-weight 51437 #checksum 4187 SEQUENCE /// ENTRY JC4993 #type complete TITLE biphenyl dioxygenase (EC 1.14.-.-) terminal oxygenase component large chain - Comamonas testosteroni ALTERNATE_NAMES iron-sulphur protein alpha chain ORGANISM #formal_name Comamonas testosteroni DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JC4993 REFERENCE JC4993 !$#authors Sylvestre, M.; Sirois, M.; Hurtubise, Y.; Bergeron, J.; !1Ahmad, D.; Shareck, F.; Barriault, D.; Guillemette, I.; !1Juteau, J.M. !$#journal Gene (1996) 174:195-202 !$#title Sequencing of Comamonas testosteroni strain B-356-biphenyl/ !1chlorobiphenyl dioxygenase genes: Evolutionary relationships !1among Gram-negative bacterial biphenyl dioxygenases. !$#cross-references MUID:97045812; PMID:8890734 !$#accession JC4993 !'##molecule_type DNA !'##residues 1-457 ##label SYL !'##cross-references GB:U47637; NID:g1245151; PIDN:AAC44526.1; !1PID:g1245152 !'##experimental_source strain B-356 GENETICS !$#gene bphA CLASSIFICATION #superfamily toluene dioxygenase terminal oxygenase !1component large chain; Rieske [2Fe-2S] homology KEYWORDS 2Fe-2S; aromatic hydrocarbon catabolism; metalloprotein; !1oxidoreductase; PCB biodegradation; Rieske iron-sulfur !1protein FEATURE !$90-138 #domain Rieske [2Fe-2S] homology #label RSK\ !$100,102,120,123 #binding_site 2Fe-2S cluster (Cys, His, Cys, His) !8(covalent) #status predicted SUMMARY #length 457 #molecular-weight 51691 #checksum 5277 SEQUENCE /// ENTRY B29830 #type complete TITLE toluene dioxygenase (EC 1.14.12.11) terminal oxygenase component small chain - Pseudomonas putida ALTERNATE_NAMES 22K benzene oxidation protein; benzene 1,2-dioxygenase (EC 1.14.12.3) terminal oxygenase component beta chain ORGANISM #formal_name Pseudomonas putida DATE 30-Jun-1989 #sequence_revision 06-Jan-1995 #text_change 11-Jun-1999 ACCESSIONS B29830; B36516 REFERENCE A91848 !$#authors Irie, S.; Doi, S.; Yorifuji, T.; Takagi, M.; Yano, K. !$#journal J. Bacteriol. (1987) 169:5174-5179 !$#title Nucleotide sequencing and characterization of the genes !1encoding benzene oxidation enzymes of Pseudomonas putida. !$#cross-references MUID:88032840; PMID:3667527 !$#accession B29830 !'##molecule_type DNA !'##residues 1-187 ##label IRI !'##cross-references GB:M17904; NID:g151068; PIDN:AAA25736.1; !1PID:g151070 !'##experimental_source strain 136R-3 REFERENCE A36516 !$#authors Zylstra, G.J.; Gibson, D.T. !$#journal J. Biol. Chem. (1989) 264:14940-14946 !$#title Toluene degradation by Pseudomonas putida F1. Nucleotide !1sequence of the todC1C2BADE genes and their expression in !1Escherichia coli. !$#cross-references MUID:89359301; PMID:2670929 !$#accession B36516 !'##molecule_type DNA !'##residues 1-187 ##label ZYL !'##cross-references GB:J04996; NID:g151600; PIDN:AAA26006.1; !1PID:g151602 !'##experimental_source strain F1 GENETICS !$#gene todC2 CLASSIFICATION #superfamily toluene dioxygenase terminal oxygenase !1component small chain KEYWORDS aromatic hydrocarbon catabolism; oxidoreductase SUMMARY #length 187 #molecular-weight 22013 #checksum 8229 SEQUENCE /// ENTRY JN0813 #type complete TITLE benzene 1,2-dioxygenase (EC 1.14.12.3) terminal oxygenase component small chain - Pseudomonas putida (strain ML2) plasmid pHMT112 ORGANISM #formal_name Pseudomonas putida DATE 19-May-1994 #sequence_revision 06-Jan-1995 #text_change 21-Jul-2000 ACCESSIONS JN0813 REFERENCE JN0810 !$#authors Tan, H.M.; Tang, H.Y.; Joannou, C.L.; Abdel-Wahab, N.H.; !1Mason, J.R. !$#journal Gene (1993) 130:33-39 !$#title The Pseudomonas putida ML2 plasmid-encoded genes for benzene !1dioxygenase are unusual in codon usage and low in G+C !1content. !$#cross-references MUID:93345820; PMID:8344526 !$#accession JN0813 !'##molecule_type DNA !'##residues 1-187 ##label TAN !'##cross-references GB:L04642; GB:L04643; NID:g6552505; !1PIDN:AAA17759.1; PID:g309856 !'##experimental_source strain ML2 GENETICS !$#gene bedC2 !$#genome plasmid CLASSIFICATION #superfamily toluene dioxygenase terminal oxygenase !1component small chain KEYWORDS aromatic hydrocarbon catabolism; oxidoreductase SUMMARY #length 187 #molecular-weight 22253 #checksum 7528 SEQUENCE /// ENTRY C41858 #type complete TITLE biphenyl dioxygenase (EC 1.14.12.-) terminal oxygenase component small chain - Pseudomonas sp. ORGANISM #formal_name Pseudomonas sp. DATE 04-Mar-1993 #sequence_revision 06-Jan-1995 #text_change 05-May-2000 ACCESSIONS C41858 REFERENCE A41858 !$#authors Erickson, B.D.; Mondello, F.J. !$#journal J. Bacteriol. (1992) 174:2903-2912 !$#title Nucleotide sequencing and transcriptional mapping of the !1genes encoding biphenyl dioxygenase, a multicomponent !1polychlorinated-biphenyl-degrading enzyme in Pseudomonas !1strain LB400. !$#cross-references MUID:92234948; PMID:1569021 !$#accession C41858 !'##molecule_type DNA !'##residues 1-188 ##label ERI !'##cross-references GB:M86348; NID:g349602; PIDN:AAB63426.1; !1PID:g151085 !'##experimental_source strain LB400 !'##note sequence extracted from NCBI backbone (NCBIN:97256, !1NCBIP:97261) GENETICS !$#gene bphA2; bphE CLASSIFICATION #superfamily toluene dioxygenase terminal oxygenase !1component small chain KEYWORDS aromatic hydrocarbon catabolism; oxidoreductase; PCB !1biodegradation SUMMARY #length 188 #molecular-weight 22085 #checksum 8442 SEQUENCE /// ENTRY B42409 #type complete TITLE biphenyl dioxygenase (EC 1.14.-.-) terminal oxygenase component small chain - Pseudomonas pseudoalcaligenes ORGANISM #formal_name Pseudomonas pseudoalcaligenes DATE 04-Mar-1993 #sequence_revision 06-Jan-1995 #text_change 11-Jun-1999 ACCESSIONS B42409 REFERENCE A42409 !$#authors Taira, K.; Hirose, J.; Hayashida, S.; Furukawa, K. !$#journal J. Biol. Chem. (1992) 267:4844-4853 !$#title Analysis of bph operon from the polychlorinated !1biphenyl-degrading strain of Pseudomonas pseudoalcaligenes !1KF707. !$#cross-references MUID:92165849; PMID:1537863 !$#accession B42409 !'##molecule_type DNA !'##residues 1-213 ##label TAI !'##cross-references GB:M83673; NID:g151090; PIDN:AAA25744.1; !1PID:g151092 !'##experimental_source KF707 !'##note sequence extracted from NCBI backbone (NCBIN:84014, !1NCBIP:84017) GENETICS !$#gene bphA2; bphE CLASSIFICATION #superfamily toluene dioxygenase terminal oxygenase !1component small chain KEYWORDS aromatic hydrocarbon catabolism; oxidoreductase; PCB !1biodegradation SUMMARY #length 213 #molecular-weight 24979 #checksum 7401 SEQUENCE /// ENTRY JC4994 #type complete TITLE biphenyl dioxygenase (EC 1.14.-.-) terminal oxygenase component small chain - Comamonas testosteroni ALTERNATE_NAMES iron-sulphur protein beta chain ORGANISM #formal_name Comamonas testosteroni DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JC4994 REFERENCE JC4993 !$#authors Sylvestre, M.; Sirois, M.; Hurtubise, Y.; Bergeron, J.; !1Ahmad, D.; Shareck, F.; Barriault, D.; Guillemette, I.; !1Juteau, J.M. !$#journal Gene (1996) 174:195-202 !$#title Sequencing of Comamonas testosteroni strain B-356-biphenyl/ !1chlorobiphenyl dioxygenase genes: Evolutionary relationships !1among Gram-negative bacterial biphenyl dioxygenases. !$#cross-references MUID:97045812; PMID:8890734 !$#accession JC4994 !'##molecule_type DNA !'##residues 1-186 ##label SYL !'##cross-references GB:U47637; NID:g1245151; PIDN:AAC44527.1; !1PID:g1245153 !'##experimental_source strain B-356 GENETICS !$#gene bphE CLASSIFICATION #superfamily toluene dioxygenase terminal oxygenase !1component small chain KEYWORDS aromatic hydrocarbon catabolism; oxidoreductase; PCB !1biodegradation SUMMARY #length 186 #molecular-weight 21556 #checksum 6587 SEQUENCE /// ENTRY B65031 #type complete TITLE biphenyl dioxygenase (EC 1.14.-.-) terminal oxygenase component alpha chain - Escherichia coli (strain K-12) ALTERNATE_NAMES digoxigenin alpha chain ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS B65031; S49293 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65031 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-172 ##label BLAT !'##cross-references GB:AE000340; GB:U00096; NID:g1788883; !1PIDN:AAC75592.1; PID:g1788889; UWGP:b2539 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S49292 !$#authors Turlin, E.; Gasser, F.; Biville, F. !$#submission submitted to the EMBL Data Library, September 1994 !$#description Cloning and sequencing of an E. coli gene homologous to !1dioxygenase of Gram negative bacteria. !$#accession S49293 !'##molecule_type DNA !'##residues 1-10,'Y',12-48,'D' ##label TUR !'##cross-references EMBL:Z37966; NID:g550595; PIDN:CAA86019.1; !1PID:g550597 !'##experimental_source strain K12 CLASSIFICATION #superfamily toluene dioxygenase terminal oxygenase !1component small chain KEYWORDS aromatic hydrocarbon catabolism; oxidoreductase; PCB !1biodegradation SUMMARY #length 172 #molecular-weight 20579 #checksum 926 SEQUENCE /// ENTRY C36516 #type complete TITLE toluene dioxygenase (EC 1.14.12.11) Rieske iron-sulfur component - Pseudomonas putida ALTERNATE_NAMES 10K benzene oxidation protein; benzene 1,2-dioxygenase ferredoxin component ORGANISM #formal_name Pseudomonas putida DATE 15-Feb-1991 #sequence_revision 06-Jan-1995 #text_change 18-Jun-1999 ACCESSIONS C36516; C29830 REFERENCE A36516 !$#authors Zylstra, G.J.; Gibson, D.T. !$#journal J. Biol. Chem. (1989) 264:14940-14946 !$#title Toluene degradation by Pseudomonas putida F1. Nucleotide !1sequence of the todC1C2BADE genes and their expression in !1Escherichia coli. !$#cross-references MUID:89359301; PMID:2670929 !$#accession C36516 !'##molecule_type DNA !'##residues 1-107 ##label ZYL !'##cross-references GB:J04996; NID:g151600; PIDN:AAA26007.1; !1PID:g151603 !'##experimental_source strain F1 REFERENCE A91848 !$#authors Irie, S.; Doi, S.; Yorifuji, T.; Takagi, M.; Yano, K. !$#journal J. Bacteriol. (1987) 169:5174-5179 !$#title Nucleotide sequencing and characterization of the genes !1encoding benzene oxidation enzymes of Pseudomonas putida. !$#cross-references MUID:88032840; PMID:3667527 !$#accession C29830 !'##molecule_type DNA !'##residues 17-107 ##label IRI !'##cross-references GB:M17904; NID:g151068; PIDN:AAA25737.1; !1PID:g151071 !'##experimental_source strain 136R-3 GENETICS !$#gene todB CLASSIFICATION #superfamily toluene dioxygenase Rieske iron-sulfur !1component; Rieske [2Fe-2S] homology KEYWORDS 2Fe-2S; aromatic hydrocarbon catabolism; metalloprotein; !1oxidoreductase; Rieske iron-sulfur protein FEATURE !$33-81 #domain Rieske [2Fe-2S] homology #label RSK\ !$43,45,62,65 #binding_site 2Fe-2S cluster (Cys, His, Cys, His) !8(covalent) #status predicted SUMMARY #length 107 #molecular-weight 11890 #checksum 9532 SEQUENCE /// ENTRY JN0811 #type complete TITLE benzene 1,2-dioxygenase (EC 1.14.12.3) Rieske iron-sulfur component - Pseudomonas putida plasmid pHMT112 ORGANISM #formal_name Pseudomonas putida DATE 19-May-1994 #sequence_revision 06-Jan-1995 #text_change 21-Jul-2000 ACCESSIONS JN0811; S00559 REFERENCE JN0810 !$#authors Tan, H.M.; Tang, H.Y.; Joannou, C.L.; Abdel-Wahab, N.H.; !1Mason, J.R. !$#journal Gene (1993) 130:33-39 !$#title The Pseudomonas putida ML2 plasmid-encoded genes for benzene !1dioxygenase are unusual in codon usage and low in G+C !1content. !$#cross-references MUID:93345820; PMID:8344526 !$#accession JN0811 !'##molecule_type DNA !'##residues 1-107 ##label TAN !'##cross-references GB:L04642; GB:L04643; NID:g6552505; !1PIDN:AAA17760.1; PID:g309857 !'##experimental_source strain ML2 REFERENCE S00559 !$#authors Morrice, N.; Geary, P.; Cammack, R.; Harris, A.; Beg, F.; !1Aitken, A. !$#journal FEBS Lett. (1988) 231:336-340 !$#title Primary structure of protein B from Pseudomonas putida, !1member of a new class of 2Fe-2S ferredoxins. !$#cross-references MUID:88196420; PMID:3360142 !$#accession S00559 !'##molecule_type protein !'##residues 2-107 ##label MOR COMMENT This enzyme component reduces the terminal oxygenase in the !1oxidation of benzene to cis-1,2-dihydroxy-cyclohexa-3, !15-diene. GENETICS !$#gene bedB !$#genome plasmid CLASSIFICATION #superfamily toluene dioxygenase Rieske iron-sulfur !1component; Rieske [2Fe-2S] homology KEYWORDS 2Fe-2S; aromatic hydrocarbon catabolism; metalloprotein; !1oxidoreductase; Rieske iron-sulfur protein FEATURE !$33-81 #domain Rieske [2Fe-2S] homology #label RSK\ !$43,45,62,65 #binding_site 2Fe-2S cluster (Cys, His, Cys, His) !8(covalent) #status predicted SUMMARY #length 107 #molecular-weight 11940 #checksum 9936 SEQUENCE /// ENTRY D42409 #type complete TITLE biphenyl dioxygenase (EC 1.14.12.-) Rieske iron-sulfur component - Pseudomonas pseudoalcaligenes ORGANISM #formal_name Pseudomonas pseudoalcaligenes DATE 04-Mar-1993 #sequence_revision 06-Jan-1995 #text_change 18-Jun-1999 ACCESSIONS D42409 REFERENCE A42409 !$#authors Taira, K.; Hirose, J.; Hayashida, S.; Furukawa, K. !$#journal J. Biol. Chem. (1992) 267:4844-4853 !$#title Analysis of bph operon from the polychlorinated !1biphenyl-degrading strain of Pseudomonas pseudoalcaligenes !1KF707. !$#cross-references MUID:92165849; PMID:1537863 !$#accession D42409 !'##molecule_type DNA !'##residues 1-109 ##label TAI !'##cross-references GB:M83673; NID:g151090; PIDN:AAA25746.1; !1PID:g151094 !'##experimental_source KF707 !'##note sequence extracted from NCBI backbone (NCBIN:84014, !1NCBIP:84019) COMMENT This enzyme component reduces the terminal oxygenase in the !1oxidation of benzene to cis-1,2-dihydroxy-cyclohexa-3, !15-diene. GENETICS !$#gene bphA3; bphF CLASSIFICATION #superfamily toluene dioxygenase Rieske iron-sulfur !1component; Rieske [2Fe-2S] homology KEYWORDS 2Fe-2S; aromatic hydrocarbon catabolism; metalloprotein; !1oxidoreductase; PCB biodegradation; Rieske iron-sulfur !1protein FEATURE !$33-82 #domain Rieske [2Fe-2S] homology #label RSK\ !$43,45,63,66 #binding_site 2Fe-2S cluster (Cys, His, Cys, His) !8(covalent) #status predicted SUMMARY #length 109 #molecular-weight 11954 #checksum 7669 SEQUENCE /// ENTRY E41858 #type complete TITLE biphenyl dioxygenase (EC 1.14.12.-) Rieske iron-sulfur component - Pseudomonas sp. ORGANISM #formal_name Pseudomonas sp. DATE 04-Mar-1993 #sequence_revision 06-Jan-1995 #text_change 18-Jun-1999 ACCESSIONS E41858 REFERENCE A41858 !$#authors Erickson, B.D.; Mondello, F.J. !$#journal J. Bacteriol. (1992) 174:2903-2912 !$#title Nucleotide sequencing and transcriptional mapping of the !1genes encoding biphenyl dioxygenase, a multicomponent !1polychlorinated-biphenyl-degrading enzyme in Pseudomonas !1strain LB400. !$#cross-references MUID:92234948; PMID:1569021 !$#accession E41858 !'##molecule_type DNA !'##residues 1-109 ##label ERI !'##experimental_source strain LB400 !'##note sequence extracted from NCBI backbone (NCBIN:97256, !1NCBIP:97264) COMMENT This enzyme component reduces the terminal oxygenase in the !1oxidation of benzene to cis-1,2-dihydroxy-cyclohexa-3, !15-diene. GENETICS !$#gene bphA3; bphF CLASSIFICATION #superfamily toluene dioxygenase Rieske iron-sulfur !1component; Rieske [2Fe-2S] homology KEYWORDS 2Fe-2S; aromatic hydrocarbon catabolism; metalloprotein; !1oxidoreductase; PCB biodegradation; Rieske iron-sulfur !1protein FEATURE !$33-82 #domain Rieske [2Fe-2S] homology #label RSK\ !$43,45,63,66 #binding_site 2Fe-2S cluster (Cys, His, Cys, His) !8(covalent) #status predicted SUMMARY #length 109 #molecular-weight 11981 #checksum 7312 SEQUENCE /// ENTRY JC4995 #type complete TITLE biphenyl dioxygenase (EC 1.14.12.-) Rieske iron-sulfur component - Comamonas testosteroni ORGANISM #formal_name Comamonas testosteroni DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JC4995 REFERENCE JC4993 !$#authors Sylvestre, M.; Sirois, M.; Hurtubise, Y.; Bergeron, J.; !1Ahmad, D.; Shareck, F.; Barriault, D.; Guillemette, I.; !1Juteau, J.M. !$#journal Gene (1996) 174:195-202 !$#title Sequencing of Comamonas testosteroni strain B-356-biphenyl/ !1chlorobiphenyl dioxygenase genes: Evolutionary relationships !1among Gram-negative bacterial biphenyl dioxygenases. !$#cross-references MUID:97045812; PMID:8890734 !$#accession JC4995 !'##molecule_type DNA !'##residues 1-109 ##label SYL !'##cross-references GB:U47637; NID:g1245151; PIDN:AAC44529.1; !1PID:g1245155 !'##experimental_source strain B-356 GENETICS !$#gene bphF FUNCTION !$#description reduces the terminal oxygenase in the oxidation of benzene !1to cis-1,2-dihydroxy-cyclohexa-3,5-diene CLASSIFICATION #superfamily toluene dioxygenase Rieske iron-sulfur !1component; Rieske [2Fe-2S] homology KEYWORDS 2Fe-2S; aromatic hydrocarbon catabolism; metalloprotein; !1oxidoreductase; PCB biodegradation; Rieske iron-sulfur !1protein FEATURE !$33-82 #domain Rieske [2Fe-2S] homology #label RSK\ !$43,45,63,66 #binding_site 2Fe-2S cluster (Cys, His, Cys, His) !8(covalent) #status predicted SUMMARY #length 109 #molecular-weight 11909 #checksum 6091 SEQUENCE /// ENTRY D36516 #type complete TITLE toluene dioxygenase (EC 1.14.12.11) ferredoxin reductase component - Pseudomonas putida ALTERNATE_NAMES 43K benzene oxidation protein CONTAINS benzene 1,2-dioxygenase (EC 1.14.12.3) ferredoxin reductase component ORGANISM #formal_name Pseudomonas putida DATE 15-Feb-1991 #sequence_revision 06-Jan-1995 #text_change 11-Jun-1999 ACCESSIONS D36516; D29830 REFERENCE A36516 !$#authors Zylstra, G.J.; Gibson, D.T. !$#journal J. Biol. Chem. (1989) 264:14940-14946 !$#title Toluene degradation by Pseudomonas putida F1. Nucleotide !1sequence of the todC1C2BADE genes and their expression in !1Escherichia coli. !$#cross-references MUID:89359301; PMID:2670929 !$#accession D36516 !'##molecule_type DNA !'##residues 1-410 ##label ZYL !'##cross-references GB:J04996; NID:g151600; PIDN:AAA26008.1; !1PID:g151604 !'##experimental_source strain F1 REFERENCE A91848 !$#authors Irie, S.; Doi, S.; Yorifuji, T.; Takagi, M.; Yano, K. !$#journal J. Bacteriol. (1987) 169:5174-5179 !$#title Nucleotide sequencing and characterization of the genes !1encoding benzene oxidation enzymes of Pseudomonas putida. !$#cross-references MUID:88032840; PMID:3667527 !$#accession D29830 !'##molecule_type DNA !'##residues 1-269,'YSPSEMWPVGAA',283-410 ##label IRI !'##cross-references GB:M17904; NID:g151068; PIDN:AAA25738.1; !1PID:g151072 !'##experimental_source strain 136R-3 GENETICS !$#gene todA CLASSIFICATION #superfamily toluene dioxygenase ferredoxin reductase !1component KEYWORDS aromatic hydrocarbon catabolism; FAD; NAD; oxidoreductase FEATURE !$2-410 #product toluene dioxygenase ferredoxin reductase !8component #status predicted #label MAT\ !$9-25 #region FAD/NAD-binding motif\ !$150-166 #region FAD/NAD-binding motif\ !$265-278 #region FAD/NAD-binding motif SUMMARY #length 410 #molecular-weight 42942 #checksum 295 SEQUENCE /// ENTRY JN0810 #type complete TITLE benzene 1,2-dioxygenase (EC 1.14.12.3) ferredoxin reductase component - Pseudomonas putida plasmid pHMT112 ORGANISM #formal_name Pseudomonas putida DATE 19-May-1994 #sequence_revision 06-Jan-1995 #text_change 21-Jul-2000 ACCESSIONS JN0810 REFERENCE JN0810 !$#authors Tan, H.M.; Tang, H.Y.; Joannou, C.L.; Abdel-Wahab, N.H.; !1Mason, J.R. !$#journal Gene (1993) 130:33-39 !$#title The Pseudomonas putida ML2 plasmid-encoded genes for benzene !1dioxygenase are unusual in codon usage and low in G+C !1content. !$#cross-references MUID:93345820; PMID:8344526 !$#accession JN0810 !'##molecule_type DNA !'##residues 1-410 ##label TAN !'##cross-references GB:L04642; GB:L04643; NID:g6552505; !1PIDN:AAA17761.1; PID:g309858 !'##experimental_source strain ML2 COMMENT This enzyme is involved in catalyzing the oxidation of !1benzene to cis-1,2-dihydroxy-cyclohexa-3,5-diene. COMMENT This compound accepts electrons from NADH and transfers them !1to the ferredoxin component. GENETICS !$#gene bedA !$#genome plasmid CLASSIFICATION #superfamily toluene dioxygenase ferredoxin reductase !1component KEYWORDS aromatic hydrocarbon catabolism; FAD; NAD; oxidoreductase FEATURE !$2-410 #product benzene 1,2-dioxygenase ferredoxin reductase !8component #status predicted #label MAT\ !$9-25 #region FAD/NAD-binding motif\ !$150-166 #region FAD/NAD-binding motif\ !$265-278 #region FAD/NAD-binding motif SUMMARY #length 410 #molecular-weight 43586 #checksum 3512 SEQUENCE /// ENTRY E42409 #type complete TITLE biphenyl dioxygenase (EC 1.14.-.-) ferredoxin reductase component - Pseudomonas pseudoalcaligenes ORGANISM #formal_name Pseudomonas pseudoalcaligenes DATE 04-Mar-1993 #sequence_revision 06-Jan-1995 #text_change 11-Jun-1999 ACCESSIONS E42409 REFERENCE A42409 !$#authors Taira, K.; Hirose, J.; Hayashida, S.; Furukawa, K. !$#journal J. Biol. Chem. (1992) 267:4844-4853 !$#title Analysis of bph operon from the polychlorinated !1biphenyl-degrading strain of Pseudomonas pseudoalcaligenes !1KF707. !$#cross-references MUID:92165849; PMID:1537863 !$#accession E42409 !'##molecule_type DNA !'##residues 1-408 ##label TAI !'##cross-references GB:M83673; NID:g151090; PIDN:AAA25747.1; !1PID:g151095 !'##experimental_source strain KF707 !'##note sequence extracted from NCBI backbone (NCBIN:84014, !1NCBIP:84021) GENETICS !$#gene bphA4; bphG CLASSIFICATION #superfamily toluene dioxygenase ferredoxin reductase !1component KEYWORDS aromatic hydrocarbon catabolism; FAD; NAD; oxidoreductase; !1PCB biodegradation FEATURE !$2-408 #product biphenyl dioxygenase ferredoxin reductase !8component #status predicted #label MAT\ !$9-25 #region FAD/NAD-binding motif\ !$150-166 #region FAD/NAD-binding motif\ !$265-278 #region FAD/NAD-binding motif SUMMARY #length 408 #molecular-weight 42953 #checksum 9556 SEQUENCE /// ENTRY F41858 #type complete TITLE biphenyl dioxygenase (EC 1.14.-.-) ferredoxin reductase component - Pseudomonas sp. ORGANISM #formal_name Pseudomonas sp. DATE 04-Mar-1993 #sequence_revision 06-Jan-1995 #text_change 10-Feb-1995 ACCESSIONS F41858 REFERENCE A41858 !$#authors Erickson, B.D.; Mondello, F.J. !$#journal J. Bacteriol. (1992) 174:2903-2912 !$#title Nucleotide sequencing and transcriptional mapping of the !1genes encoding biphenyl dioxygenase, a multicomponent !1polychlorinated-biphenyl-degrading enzyme in Pseudomonas !1strain LB400. !$#cross-references MUID:92234948; PMID:1569021 !$#accession F41858 !'##molecule_type DNA !'##residues 1-408 ##label ERI !'##experimental_source strain LB400 !'##note sequence extracted from NCBI backbone (NCBIN:97256, !1NCBIP:97265) GENETICS !$#gene bphA4; bphG CLASSIFICATION #superfamily toluene dioxygenase ferredoxin reductase !1component KEYWORDS aromatic hydrocarbon catabolism; FAD; NAD; oxidoreductase; !1PCB biodegradation FEATURE !$2-408 #product biphenyl dioxygenase ferredoxin reductase !8component #status predicted #label MAT\ !$9-25 #region FAD/NAD-binding motif\ !$150-166 #region FAD/NAD-binding motif\ !$265-278 #region FAD/NAD-binding motif SUMMARY #length 408 #molecular-weight 42970 #checksum 9012 SEQUENCE /// ENTRY JC4996 #type complete TITLE biphenyl dioxygenase (EC 1.14.-.-) ferredoxin reductase component - Comamonas testosteroni ORGANISM #formal_name Comamonas testosteroni DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JC4996 REFERENCE JC4993 !$#authors Sylvestre, M.; Sirois, M.; Hurtubise, Y.; Bergeron, J.; !1Ahmad, D.; Shareck, F.; Barriault, D.; Guillemette, I.; !1Juteau, J.M. !$#journal Gene (1996) 174:195-202 !$#title Sequencing of Comamonas testosteroni strain B-356-biphenyl/ !1chlorobiphenyl dioxygenase genes: Evolutionary relationships !1among Gram-negative bacterial biphenyl dioxygenases. !$#cross-references MUID:97045812; PMID:8890734 !$#accession JC4996 !'##molecule_type DNA !'##residues 1-406 ##label SYL !'##cross-references GB:U47638; NID:g1245157; PIDN:AAC44531.1; !1PID:g1245158 !'##experimental_source strain B-356 GENETICS !$#gene bphG CLASSIFICATION #superfamily toluene dioxygenase ferredoxin reductase !1component KEYWORDS aromatic hydrocarbon catabolism; FAD; NAD; oxidoreductase; !1PCB biodegradation FEATURE !$14-30 #region FAD/NAD-binding motif\ !$152-168 #region FAD/NAD-binding motif\ !$263-276 #region FAD/NAD-binding motif SUMMARY #length 406 #molecular-weight 43338 #checksum 1288 SEQUENCE /// ENTRY C65075 #type complete TITLE probable 2-octaprenyl-6-methoxyphenol 4-monoxygenase (EC 1.14.13.-) ubiH - Escherichia coli (strain K-12) ALTERNATE_NAMES visB protein ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS C65075; C47020; JQ0844 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65075 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-392 ##label BLAT !'##cross-references GB:AE000374; GB:U00096; NID:g1789270; !1PIDN:AAC75945.1; PID:g1789274; UWGP:b2907 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A47020 !$#authors Nakahigashi, K.; Miyamoto, K.; Nishimura, K.; Inokuchi, H. !$#journal J. Bacteriol. (1992) 174:7352-7359 !$#title Isolation and characterization of a light-sensitive mutant !1of Escherichia coli K-12 with a mutation in a gene that is !1required for the biosynthesis of ubiquinone. !$#cross-references MUID:93054351; PMID:1339425 !$#accession C47020 !'##status preliminary !'##molecule_type DNA !'##residues 1-381,'V',383-392 ##label NAK !'##cross-references GB:D90281; NID:g216625; PIDN:BAA14326.1; !1PID:g216628 !'##experimental_source strain K12 CA274 !'##note sequence extracted from NCBI backbone (NCBIN:118090, !1NCBIP:118093) COMMENT This protein is responsible for ubiquinone biosynthesis, and !1is sensitive to visible light. GENETICS !$#gene ubiH; ubiH(visB) !$#map_position 63 min CLASSIFICATION #superfamily ubiH protein KEYWORDS oxidoreductase SUMMARY #length 392 #molecular-weight 42288 #checksum 7887 SEQUENCE /// ENTRY D64801 #type complete TITLE probable monooxygenase (EC 1.14.13.-) yleB - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS D64801 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64801 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-391 ##label BLAT !'##cross-references GB:AE000170; GB:U00096; NID:g1786875; !1PIDN:AAC73763.1; PID:g1786883; UWGP:b0662 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yleB CLASSIFICATION #superfamily ubiH protein KEYWORDS oxidoreductase SUMMARY #length 391 #molecular-weight 42953 #checksum 7919 SEQUENCE /// ENTRY B65075 #type complete TITLE probable monooxygenase (EC 1.14.13.-) visC - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS B65075; D47020; JQ0845 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65075 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-400 ##label BLAT !'##cross-references GB:AE000374; GB:U00096; NID:g1789270; !1PIDN:AAC75944.1; PID:g1789273; UWGP:b2906 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A47020 !$#authors Nakahigashi, K.; Miyamoto, K.; Nishimura, K.; Inokuchi, H. !$#journal J. Bacteriol. (1992) 174:7352-7359 !$#title Isolation and characterization of a light-sensitive mutant !1of Escherichia coli K-12 with a mutation in a gene that is !1required for the biosynthesis of ubiquinone. !$#cross-references MUID:93054351; PMID:1339425 !$#accession D47020 !'##molecule_type DNA !'##residues 1-25,'A',27-382,'A',384-400 ##label NAK !'##cross-references GB:D90281; NID:g216625; PIDN:BAA14327.1; !1PID:g216629 !'##experimental_source strain K12 CA274 !'##note sequence extracted from NCBI backbone (NCBIN:118090, !1NCBIP:118094) COMMENT This protein is sensitive to visible light. GENETICS !$#gene visC !$#map_position 63 min CLASSIFICATION #superfamily ubiH protein KEYWORDS oxidoreductase SUMMARY #length 400 #molecular-weight 44244 #checksum 8493 SEQUENCE /// ENTRY S74699 #type complete TITLE probable 2-octaprenyl-6-methoxyphenol 4-monoxygenase (EC 1.14.13.-) ubiH - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein slr1300 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S74699 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74699 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-414 ##label KAN !'##cross-references EMBL:D90901; GB:AB001339; NID:g1651897; !1PIDN:BAA16850.1; PID:g1651924 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene ubiH CLASSIFICATION #superfamily ubiH protein KEYWORDS oxidoreductase SUMMARY #length 414 #molecular-weight 45623 #checksum 785 SEQUENCE /// ENTRY WHPSBF #type complete TITLE 4-hydroxybenzoate 3-monooxygenase (EC 1.14.13.2) - Pseudomonas fluorescens (tentative sequence) ALTERNATE_NAMES p-hydroxybenzoate hydroxylase ORGANISM #formal_name Pseudomonas fluorescens DATE 30-Apr-1981 #sequence_revision 05-Apr-1983 #text_change 31-Mar-2000 ACCESSIONS A90643; A91101; A91102; S27003; A00507 REFERENCE A90643 !$#authors Weijer, W.J.; Hofsteenge, J.; Vereijken, J.M.; Jekel, P.A.; !1Beintema, J.J. !$#journal Biochim. Biophys. Acta (1982) 704:385-388 !$#title Primary structure of p-hydroxybenzoate hydroxylase from !1Pseudomonas fluorescens. !$#cross-references MUID:82257502; PMID:6809053 !$#accession A90643 !'##molecule_type protein !'##residues 1-394 ##label WEI REFERENCE A91101 !$#authors Hofsteenge, J.; Vereijken, J.M.; Weijer, W.J.; Beintema, !1J.J.; Wierenga, R.K.; Drenth, J. !$#journal Eur. J. Biochem. (1980) 113:141-150 !$#title Primary and tertiary structure studies of p-hydroxybenzoate !1hydroxylase from Pseudomonas fluorescens. !$#cross-references MUID:81114230; PMID:6780352 !$#accession A91101 !'##molecule_type protein !'##residues 111-138;270-280 ##label HOF REFERENCE A91102 !$#authors Vereijken, J.M.; Hofsteenge, J.; Bak, H.J.; Beintema, J.J. !$#journal Eur. J. Biochem. (1980) 113:151-157 !$#title The amino-acid sequence of the three smallest CNBr peptides !1from p-hydroxybenzoate hydroxylase from Pseudomonas !1fluorescens. !$#cross-references MUID:81114232; PMID:6780353 !$#accession A91102 !'##molecule_type protein !'##residues 1-52;53-65;66-110 ##label VER REFERENCE S27003 !$#authors van Berkel, W.; Westphal, A.; Eschrich, K.; Eppink, M.; de !1Kok, A. !$#journal Eur. J. Biochem. (1992) 210:411-419 !$#title Substitution of Arg214 at the substrate-binding site of !1p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens. !$#cross-references MUID:93092974; PMID:1459126 !$#accession S27003 !'##status preliminary !'##molecule_type DNA !'##residues 1-343,'W',345-394 ##label VAN !'##cross-references EMBL:X68438; NID:g49144; PIDN:CAA48483.1; !1PID:g49145 REFERENCE A91132 !$#authors Hofsteenge, J.; Weijer, W.J.; Jekel, P.A.; Beintema, J.J. !$#journal Eur. J. Biochem. (1983) 133:91-108 !$#title p-Hydroxybenzoate hydroxylase from Pseudomonas fluorescens. !11. Completion of the elucidation of the primary structure. !$#cross-references MUID:83209654; PMID:6406229 !$#contents annotation; sequences of CNBr peptides; tertiary structure REFERENCE A91129 !$#authors Weijer, W.J.; Hofsteenge, J.; Beintema, J.J.; Wierenga, !1R.K.; Drenth, J. !$#journal Eur. J. Biochem. (1983) 133:109-118 !$#title p-Hydroxybenzoate hydroxylase from Pseudomonas fluorescens. !12. Fitting of the amino-acid sequence to the tertiary !1structure. !$#cross-references MUID:83209623; PMID:6406227 !$#contents annotation; sequences of CNBr peptides; structure of active !1site REFERENCE A92857 !$#authors Wierenga, R.K.; de Jong, R.J.; Kalk, K.H.; Hol, W.G.J.; !1Drenth, J. !$#journal J. Mol. Biol. (1979) 131:55-73 !$#title Crystal structure of rho-hydroxybenzoate hydroxylase. !$#cross-references MUID:80029705; PMID:40036 !$#contents annotation; X-ray crystallography, 2.5 angstroms !$#note the structure of the flavin adenine dinucleotide binding !1site is described COMMENT This FAD monooxygenase catalyzes the conversion of !1p-hyroxybenzoate to protocatechuate, which is further !1degraded to succinate and actyl-CoA. The active enzyme is a !1dimer of identical chains. CLASSIFICATION #superfamily 4-hydroxybenzoate 3-monooxygenase KEYWORDS FAD; homodimer; monooxygenase; oxidoreductase FEATURE !$4-32 #region beta-alpha-beta FAD nucleotide-binding fold SUMMARY #length 394 #molecular-weight 44298 #checksum 1980 SEQUENCE /// ENTRY JU0142 #type complete TITLE 4-hydroxybenzoate 3-monooxygenase (EC 1.14.13.2) - Acinetobacter calcoaceticus ALTERNATE_NAMES p-hydroxybenzoate hydroxylase ORGANISM #formal_name Acinetobacter calcoaceticus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JU0142 REFERENCE JU0142 !$#authors DiMarco, A.A.; Averhoff, B.A.; Kim, E.E.; Ornston, L.N. !$#journal Gene (1993) 125:25-33 !$#title Evolutionary divergence of pobA, the structural gene !1encoding p-hydroxybenzoate hydroxylase in an Acinetobacter !1calcoaceticus strain well-suited for genetic analysis. !$#cross-references MUID:93194074; PMID:8449410 !$#accession JU0142 !'##molecule_type DNA !'##residues 1-404 ##label DIM !'##experimental_source strain ADP1 COMMENT This flavin-containing monooxygenase catalyzes the !1conversion of p-hydroxybenzoate to protocatechuate. GENETICS !$#gene pobA CLASSIFICATION #superfamily 4-hydroxybenzoate 3-monooxygenase KEYWORDS FAD; homodimer; oxidoreductase FEATURE !$7-35 #region beta-alpha-beta FAD nucleotide-binding fold\ !$278-307 #domain FAD binding #status predicted #label FAD SUMMARY #length 404 #molecular-weight 45271 #checksum 7980 SEQUENCE /// ENTRY A47489 #type complete TITLE 4-hydroxybenzoate 3-monooxygenase (EC 1.14.13.2) [similarity] - Pseudomonas fluorescens (ATCC 13525) ORGANISM #formal_name Pseudomonas fluorescens DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 05-May-2000 ACCESSIONS A47489 REFERENCE A47489 !$#authors Shuman, B.; Dix, T.A. !$#journal J. Biol. Chem. (1993) 268:17057-17062 !$#title Cloning, nucleotide sequence, and expression of a !1p-hydroxybenzoate hydroxylase isozyme gene from Pseudomonas !1fluorescens. !$#cross-references MUID:93352481; PMID:8349594 !$#accession A47489 !'##molecule_type DNA !'##residues 1-397 ##label SHU !'##cross-references GB:L13747; NID:g294364; PIDN:AAA25834.1; !1PID:g294365 !'##note authors translated the codon TGG for residue 347 as Tyr CLASSIFICATION #superfamily 4-hydroxybenzoate 3-monooxygenase KEYWORDS FAD; homodimer; oxidoreductase FEATURE !$7-35 #region beta-alpha-beta FAD nucleotide-binding fold SUMMARY #length 397 #molecular-weight 44140 #checksum 2034 SEQUENCE /// ENTRY WHPSBA #type complete TITLE 4-hydroxybenzoate 3-monooxygenase (EC 1.14.13.2) - Pseudomonas aeruginosa ALTERNATE_NAMES p-hydroxybenzoate hydroxylase; pobA protein ORGANISM #formal_name Pseudomonas aeruginosa DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 06-Oct-2000 ACCESSIONS JT0384; S41383; E83613 REFERENCE JT0384 !$#authors Entsch, B.; Nan, Y.; Weaich, K.; Scott, K.F. !$#journal Gene (1988) 71:279-291 !$#title Sequence and organization of pobA, the gene coding for !1p-hydroxybenzoate hydroxylase, an inducible enzyme from !1Pseudomonas aeruginosa. !$#cross-references MUID:89138003; PMID:2465205 !$#accession JT0384 !'##molecule_type DNA !'##residues 1-394 ##label ENT !'##cross-references GB:M23173; NID:g151505; PIDN:AAA88455.1; !1PID:g151506 REFERENCE S41380 !$#authors Entsch, B.; Squire, L.; Wicks, R.E. !$#submission submitted to the EMBL Data Library, December 1993 !$#description Gene for the regulation of PARA-hydroxybenzoate hydroxylase !1in Pseudomonas aeruginosa. !$#accession S41383 !'##status preliminary !'##molecule_type DNA !'##residues 1-54 ##label EN2 !'##cross-references EMBL:X76994; NID:g444024; PIDN:CAA54302.1; !1PID:g444028 REFERENCE A82950 !$#authors Stover, C.K.; Pham, X.Q.; Erwin, A.L.; Mizoguchi, S.D.; !1Warrener, P.; Hickey, M.J.; Brinkman, F.S.L.; Hufnagle, !1W.O.; Kowalik, D.J.; Lagrou, M.; Garber, R.L.; Goltry, L.; !1Tolentino, E.; Westbrook-Wadman, S.; Yuan, Y.; Brody, L.L.; !1Coulter, S.N.; Folger, K.R.; Kas, A.; Larbig, K.; Lim, R.M.; !1Smith, K.A.; Spencer, D.H.; Wong, G.K.S.; Wu, Z.; Paulsen, !1I.T.; Reizer, J.; Saier, M.H.; Hancock, R.E.W.; Lory, S.; !1Olson, M.V. !$#journal Nature (2000) 406:959-964 !$#title Complete genome sequence of Pseudomonas aeruginosa PA01, an !1opportunistic pathogen. !$#cross-references MUID:20437337; PMID:10984043 !$#accession E83613 !'##status preliminary !'##molecule_type DNA !'##residues 1-394 ##label STO !'##cross-references GB:AE004463; GB:AE004091; NID:g9946086; !1PIDN:AAG03636.1; GSPDB:GN00131; PASP:PA0247 !'##experimental_source strain PAO1 COMMENT This FAD monooxygenase catalyzes the conversion of !1p-hydroxybenzoate to protocatechuate, which is further !1degraded to succinate and acetyl-CoA. GENETICS !$#gene pobA; PA0247 CLASSIFICATION #superfamily 4-hydroxybenzoate 3-monooxygenase KEYWORDS FAD; homodimer; monooxygenase; oxidoreductase FEATURE !$4-32 #region beta-alpha-beta FAD nucleotide-binding fold SUMMARY #length 394 #molecular-weight 44323 #checksum 2297 SEQUENCE /// ENTRY B55349 #type complete TITLE 4-hydroxyphenylacetate 3-monooxygenase (EC 1.14.13.3) large chain - Escherichia coli (ATCC 11105) ALTERNATE_NAMES 4-hydroxyphenylacetate 3-hydroxylase large chain ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B55349; S41919 REFERENCE A55349 !$#authors Prieto, M.A.; Garcia, J.L. !$#journal J. Biol. Chem. (1994) 269:22823-22829 !$#title Molecular characterization of 4-hydroxyphenylacetate !13-hydroxylase of Escherichia coli. A two-protein component !1enzyme. !$#cross-references MUID:94357932; PMID:8077235 !$#accession B55349 !'##status preliminary !'##molecule_type DNA !'##residues 1-520 ##label PRI !'##cross-references GB:Z29081; NID:g452839; PIDN:CAA82321.1; !1PID:g452841 GENETICS !$#gene hpaB CLASSIFICATION #superfamily Escherichia coli 4-hydroxyphenylacetate !13-monooxygenase large chain KEYWORDS FAD; NAD; oxidoreductase SUMMARY #length 520 #molecular-weight 58847 #checksum 5194 SEQUENCE /// ENTRY E69291 #type complete TITLE 4-hydroxyphenylacetate 3-monooxygenase (EC 1.14.13.3) hpaA-1 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS E69291 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession E69291 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-500 ##label KLE !'##cross-references GB:AE001081; GB:AE000782; NID:g2689404; !1PIDN:AAB90900.1; PID:g2650300; TIGR:AF0333 CLASSIFICATION #superfamily Escherichia coli 4-hydroxyphenylacetate !13-monooxygenase large chain KEYWORDS FAD; NAD; oxidoreductase SUMMARY #length 500 #molecular-weight 55897 #checksum 2069 SEQUENCE /// ENTRY C69378 #type complete TITLE 4-hydroxyphenylacetate 3-monooxygenase (EC 1.14.13.3) hpaA-3 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C69378 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession C69378 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-480 ##label KLE !'##cross-references GB:AE001032; GB:AE000782; NID:g2689355; !1PIDN:AAB90216.1; PID:g2649567; TIGR:AF1027 CLASSIFICATION #superfamily Escherichia coli 4-hydroxyphenylacetate !13-monooxygenase large chain KEYWORDS FAD; NAD; oxidoreductase SUMMARY #length 480 #molecular-weight 53498 #checksum 8841 SEQUENCE /// ENTRY E69360 #type complete TITLE 4-hydroxyphenylacetate 3-monooxygenase (EC 1.14.13.3) hpaA-2 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS E69360 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession E69360 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-461 ##label KLE !'##cross-references GB:AE001043; GB:AE000782; NID:g2689366; !1PIDN:AAB90358.1; PID:g2649720; TIGR:AF0885 CLASSIFICATION #superfamily Escherichia coli 4-hydroxyphenylacetate !13-monooxygenase large chain KEYWORDS FAD; NAD; oxidoreductase SUMMARY #length 461 #molecular-weight 51217 #checksum 8528 SEQUENCE /// ENTRY A40876 #type complete TITLE dimethylaniline monooxygenase (N-oxide-forming) (EC 1.14.13.8), hepatic 1 - human ALTERNATE_NAMES dimethylaniline oxidase; flavin-containing monooxygenase ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 11-Jun-1999 ACCESSIONS A40876 REFERENCE A40876 !$#authors Dolphin, C.; Shephard, E.A.; Povey, S.; Palmer, C.N.A.; !1Ziegler, D.M.; Ayesh, R.; Smith, R.L.; Phillips, I.R. !$#journal J. Biol. Chem. (1991) 266:12379-12385 !$#title Cloning, primary sequence, and chromosomal mapping of a !1human flavin-containing monooxygenase (FMO1). !$#cross-references MUID:91286259; PMID:1712018 !$#accession A40876 !'##molecule_type mRNA !'##residues 1-532 ##label DOL !'##cross-references GB:M64082; NID:g182670; PIDN:AAA52457.1; !1PID:g182671 COMMENT This enzyme is involved in the metabolism of many drugs, !1pesticides, and other foreign compounds, including !1xenobiotics, by catalyzing the NADPH-dependent oxidation of !1various substrates. GENETICS !$#gene GDB:FMO1 !'##cross-references GDB:126689; OMIM:136130 !$#map_position 1q23-1q25 CLASSIFICATION #superfamily dimethylaniline monooxygenase (N-oxide-forming) KEYWORDS FAD; flavoprotein; microsome; monooxygenase; NADP; !1oxidoreductase FEATURE !$4-32 #region beta-alpha-beta FAD nucleotide-binding fold\ !$186-214 #region beta-alpha-beta NADP nucleotide-binding fold SUMMARY #length 532 #molecular-weight 60310 #checksum 1426 SEQUENCE /// ENTRY A33768 #type complete TITLE dimethylaniline monooxygenase (N-oxide-forming) (EC 1.14.13.8), hepatic - pig ALTERNATE_NAMES dimethylaniline oxidase; flavin-containing monooxygenase ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 03-Dec-1999 ACCESSIONS A33768; B33768; A35420 REFERENCE A33768 !$#authors Gasser, R.; Tynes, R.E.; Lawton, M.P.; Korsmeyer, K.K.; !1Ziegler, D.M.; Philpot, R.M. !$#journal Biochemistry (1990) 29:119-124 !$#title The flavin-containing monooxygenase expressed in pig liver: !1primary sequence, distribution, and evidence for a single !1gene. !$#cross-references MUID:90212556; PMID:2322534 !$#accession A33768 !'##molecule_type mRNA !'##residues 1-532 ##label GAS1 !'##cross-references GB:M32031; NID:g164454; PIDN:AAA31033.1; !1PID:g164455 !$#accession B33768 !'##molecule_type protein !'##residues 309-318 ##label GAS2 REFERENCE A35420 !$#authors Guan, S.; Falick, A.M.; Cashman, J.R. !$#journal Biochem. Biophys. Res. Commun. (1990) 170:937-943 !$#title N-terminus determination: FAD and NADP binding domain !1mapping of hog liver flavin-containing monooxygenase by !1tandem mass spectrometry. !$#cross-references MUID:90343821; PMID:2383273 !$#accession A35420 !'##molecule_type protein !'##residues 2-14;185-202 ##label GUA COMMENT This enzyme is involved in the metabolism of many drugs, !1pesticides, and other foreign compounds, including !1xenobiotics, by catalyzing the NADPH-dependent oxidation of !1various substrates. CLASSIFICATION #superfamily dimethylaniline monooxygenase (N-oxide-forming) KEYWORDS acetylated amino end; FAD; flavoprotein; liver; microsome; !1monooxygenase; NADP; oxidoreductase FEATURE !$4-32 #region beta-alpha-beta FAD nucleotide-binding fold\ !$186-214 #region beta-alpha-beta NADP nucleotide-binding fold\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental SUMMARY #length 532 #molecular-weight 59952 #checksum 3488 SEQUENCE /// ENTRY A35182 #type complete TITLE dimethylaniline monooxygenase (N-oxide-forming) (EC 1.14.13.8), hepatic 3 - rabbit ALTERNATE_NAMES dimethylaniline oxidase; flavin-containing monooxygenase ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 11-Jun-1999 ACCESSIONS A35182 REFERENCE A35182 !$#authors Lawton, M.P.; Gasser, R.; Tynes, R.E.; Hodgson, E.; Philpot, !1R.M. !$#journal J. Biol. Chem. (1990) 265:5855-5861 !$#title The flavin-containing monooxygenase enzymes expressed in !1rabbit liver and lung are products of related but distinctly !1different genes. !$#cross-references MUID:90202836; PMID:2318837 !$#accession A35182 !'##molecule_type mRNA !'##residues 1-535 ##label LAW !'##cross-references GB:M32030; NID:g165097; PIDN:AAA31278.1; !1PID:g165098 COMMENT This enzyme is involved in the metabolism of many drugs, !1pesticides, and other foreign compounds, including !1xenobiotics, by catalyzing the NADPH-dependent oxidation of !1various substrates. CLASSIFICATION #superfamily dimethylaniline monooxygenase (N-oxide-forming) KEYWORDS FAD; flavoprotein; microsome; monooxygenase; NADP; !1oxidoreductase FEATURE !$4-32 #region beta-alpha-beta FAD nucleotide-binding fold\ !$186-214 #region beta-alpha-beta NADP nucleotide-binding fold SUMMARY #length 535 #molecular-weight 60182 #checksum 884 SEQUENCE /// ENTRY A35427 #type complete TITLE dimethylaniline monooxygenase (N-oxide-forming) (EC 1.14.13.8), hepatic 1 - rabbit ALTERNATE_NAMES dimethylaniline oxidase; flavin-containing monooxygenase ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 13-Mar-1997 ACCESSIONS A35427; A32914; S18381 REFERENCE A35427 !$#authors Ozols, J. !$#journal J. Biol. Chem. (1990) 265:10289-10299 !$#title Covalent structure of liver microsomal flavin-containing !1monooxygenase form 1. !$#cross-references MUID:90285148; PMID:2355001 !$#accession A35427 !'##molecule_type protein !'##residues 1-536 ##label OZO1 REFERENCE A32914 !$#authors Ozols, J. !$#journal Biochem. Biophys. Res. Commun. (1989) 163:49-55 !$#title Liver microsomes contain two distinct NADPH-monooxygenases !1with NH-2-terminal segments homologous to the flavin !1containing NADPH monooxygenase of Pseudomonas fluorescens. !$#cross-references MUID:89374273; PMID:2505769 !$#accession A32914 !'##molecule_type protein !'##residues 3-32 ##label OZO2 COMMENT This enzyme is involved in the metabolism of many drugs, !1pesticides, and other foreign compounds, including !1xenobiotics, by catalyzing the NADPH-dependent oxidation of !1various substrates. CLASSIFICATION #superfamily dimethylaniline monooxygenase (N-oxide-forming) KEYWORDS acetylated amino end; FAD; flavoprotein; microsome; !1monooxygenase; NADP; oxidoreductase FEATURE !$3-31 #region beta-alpha-beta FAD nucleotide-binding fold\ !$185-213 #region beta-alpha-beta NADP nucleotide-binding fold\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental SUMMARY #length 536 #molecular-weight 60237 #checksum 1984 SEQUENCE /// ENTRY A38228 #type complete TITLE dimethylaniline monooxygenase (N-oxide-forming) (EC 1.14.13.8), hepatic 2 - human ALTERNATE_NAMES dimethylaniline oxidase; flavin-containing monooxygenase ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 11-Jun-1999 ACCESSIONS A38228 REFERENCE A38228 !$#authors Lomri, N.; Gu, Q.; Cashman, J.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:1685-1689 !$#title Molecular cloning of the flavin-containing monooxygenase !1(form II) cDNA from adult human liver. !$#cross-references MUID:92179247; PMID:1542660 !$#accession A38228 !'##molecule_type mRNA !'##residues 1-533 ##label LOM !'##cross-references GB:M83772; NID:g188630; PIDN:AAA86284.1; !1PID:g188631 !'##experimental_source adult liver !'##note sequence extracted from NCBI backbone (NCBIN:86904, !1NCBIP:86905) COMMENT This enzyme is involved in the metabolism of many drugs, !1pesticides, and other foreign compounds, including !1xenobiotics, by catalyzing the NADPH-dependent oxidation of !1various substrates. GENETICS !$#gene GDB:FMO2 !'##cross-references GDB:335399 !$#map_position 1q-1q CLASSIFICATION #superfamily dimethylaniline monooxygenase (N-oxide-forming) KEYWORDS FAD; flavoprotein; microsome; monooxygenase; NADP; !1oxidoreductase FEATURE !$4-32 #region beta-alpha-beta FAD nucleotide-binding fold\ !$186-214 #region beta-alpha-beta NADP nucleotide-binding fold SUMMARY #length 533 #molecular-weight 59719 #checksum 420 SEQUENCE /// ENTRY S18380 #type complete TITLE dimethylaniline monooxygenase (N-oxide-forming) (EC 1.14.13.8), hepatic 2 - rabbit ALTERNATE_NAMES dimethylaniline oxidase; flavin-containing monooxygenase ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 13-Mar-1997 ACCESSIONS S18380; B32914 REFERENCE S18380 !$#authors Ozols, J. !$#journal Arch. Biochem. Biophys. (1991) 290:103-115 !$#title Multiple forms of liver microsomal flavin-containing !1monooxygenases: complete covalent structure of form 2. !$#cross-references MUID:91378577; PMID:1898080 !$#accession S18380 !'##molecule_type protein !'##residues 1-533 ##label OZO1 REFERENCE A32914 !$#authors Ozols, J. !$#journal Biochem. Biophys. Res. Commun. (1989) 163:49-55 !$#title Liver microsomes contain two distinct NADPH-monooxygenases !1with NH-2-terminal segments homologous to the flavin !1containing NADPH monooxygenase of Pseudomonas fluorescens. !$#cross-references MUID:89374273; PMID:2505769 !$#accession B32914 !'##molecule_type protein !'##residues 1-32 ##label OZO2 COMMENT This enzyme is involved in the metabolism of many drugs, !1pesticides, and other foreign compounds, including !1xenobiotics, by catalyzing the NADPH-dependent oxidation of !1various substrates. CLASSIFICATION #superfamily dimethylaniline monooxygenase (N-oxide-forming) KEYWORDS FAD; flavoprotein; microsome; monooxygenase; NADP; !1oxidoreductase FEATURE !$3-31 #region beta-alpha-beta FAD nucleotide-binding fold\ !$185-213 #region beta-alpha-beta NADP nucleotide-binding fold SUMMARY #length 533 #molecular-weight 60096 #checksum 1027 SEQUENCE /// ENTRY B35182 #type complete TITLE dimethylaniline monooxygenase (N-oxide-forming) (EC 1.14.13.8), pulmonary - rabbit ALTERNATE_NAMES dimethylaniline oxidase; flavin-containing monooxygenase ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 13-Mar-1997 ACCESSIONS B35182 REFERENCE A35182 !$#authors Lawton, M.P.; Gasser, R.; Tynes, R.E.; Hodgson, E.; Philpot, !1R.M. !$#journal J. Biol. Chem. (1990) 265:5855-5861 !$#title The flavin-containing monooxygenase enzymes expressed in !1rabbit liver and lung are products of related but distinctly !1different genes. !$#cross-references MUID:90202836; PMID:2318837 !$#accession B35182 !'##molecule_type mRNA !'##residues 1-535 ##label LAW !'##cross-references GB:M32030 COMMENT This enzyme is involved in the metabolism of many drugs, !1pesticides, and other foreign compounds, including !1xenobiotics, by catalyzing the NADPH-dependent oxidation of !1various substrates. CLASSIFICATION #superfamily dimethylaniline monooxygenase (N-oxide-forming) KEYWORDS FAD; flavoprotein; microsome; monooxygenase; NADP; !1oxidoreductase FEATURE !$4-32 #region beta-alpha-beta FAD nucleotide-binding fold\ !$186-214 #region beta-alpha-beta NADP nucleotide-binding fold SUMMARY #length 535 #molecular-weight 61144 #checksum 4204 SEQUENCE /// ENTRY A47501 #type complete TITLE nitric-oxide synthase (EC 1.14.13.39), endothelial - human ORGANISM #formal_name Homo sapiens #common_name man DATE 02-Jun-1995 #sequence_revision 21-Jul-1995 #text_change 03-Mar-2000 ACCESSIONS A47501; S24052; A38948; A49813; A42867; S45691; I37361 REFERENCE A47501 !$#authors Marsden, P.A.; Heng, H.H.Q.; Scherer, S.W.; Stewart, R.J.; !1Hall, A.V.; Shi, X.M.; Tsui, L.C.; Schappert, K.T. !$#journal J. Biol. Chem. (1993) 268:17478-17488 !$#title Structure and chromosomal localization of the human !1constitutive endothelial nitric oxide synthase gene. !$#cross-references MUID:93352539; PMID:7688726 !$#accession A47501 !'##molecule_type DNA !'##residues 1-1203 ##label MAR1 !'##cross-references GB:L10709; NID:g348235; PIDN:AAA36365.1; !1PID:g348237; GB:L10693; NID:g348219; GB:L10694; NID:g348220; !1GB:L10695; NID:g348221; GB:L10696; NID:g348222; GB:L10697; !1NID:g348223; GB:L10698; NID:g348224; GB:L10699; NID:g348225; !1GB:L10700; NID:g348226; GB:L10701; NID:g348227; GB:L10702; !1NID:g348228; GB:L10703; NID:g348229; GB:L10704; NID:g348230; !1GB:L10705; NID:g348231; GB:L10706; NID:g348232; GB:L10707; !1NID:g348233; GB:L10708; NID:g348234 REFERENCE S24052 !$#authors Marsden, P.A.; Schappert, K.T.; Chen, H.S.; Flowers, M.; !1Sundell, C.L.; Wilcox, J.N.; Lamas, S.; Michel, T. !$#journal FEBS Lett. (1992) 307:287-293 !$#title Molecular cloning and characterization of human endothelial !1nitric oxide synthase. !$#cross-references MUID:92354731; PMID:1379542 !$#accession S24052 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-1203 ##label MAR2 !'##cross-references GB:M95296; NID:g189259; PIDN:AAA36372.1; !1PID:g189260 REFERENCE A38948 !$#authors Janssens, S.P.; Shimouchi, A.; Quertermous, T.; Bloch, D.B.; !1Bloch, K.D. !$#submission submitted to GenBank, September 1992 !$#accession A38948 !'##molecule_type mRNA !'##residues 1-1203 ##label JAN1 !'##cross-references GB:M93718; NID:g189211; PIDN:AAA36364.1; !1PID:g189212 !'##note the sequence in GenBank entry HUMNIOXSYN, release 111.0, has !1been corrected to correspond with the sequence for A38948 !1but is not annotated to reflect the correction REFERENCE A49813 !$#authors Janssens, S.P.; Simouchi, A.; Quertermous, T.; Bloch, D.B.; !1Bloch, K.D. !$#journal J. Biol. Chem. (1992) 267:22694b !$#cross-references MUID:93054573; PMID:1385404 !$#contents erratum !$#accession A49813 !'##molecule_type mRNA !'##residues 1191-1203 ##label JAN2 !'##cross-references PIDN:AAB23920.1; PID:g258793 !'##note sequence extracted from NCBI backbone (NCBIP:117314) REFERENCE A42867 !$#authors Janssens, S.P.; Shimouchi, A.; Quertermous, T.; Bloch, D.B.; !1Bloch, K.D. !$#journal J. Biol. Chem. (1992) 267:14519-14522 !$#title Cloning and expression of a cDNA encoding human !1endothelium-derived relaxing factor/nitric oxide synthase. !$#cross-references MUID:92340475; PMID:1378832 !$#accession A42867 !'##molecule_type mRNA !'##residues 1-82,'S',84-179,'F',181-566,'W',568-647,'Q',649-854,'V', !1856-1008,'G',1010-1103,'V',1105-1190, !1'GVRASRLRHQQPLRAAWLSLPVPGERLPDS', !1'GPPDQDQPRSSPLEVVPSHICPEAARIQHY', !1'SSRKEQNASFPSLGLLPRAWVRLNLEGPSQ','QRYPRAYCHPLPVS' ##label !1JAN3 !'##cross-references GB:M93718; NID:g189211 !'##note this sequence has been revised in reference A49813 REFERENCE S45691 !$#authors Garvey, E.P.; Tuttle, J.V.; Covington, K.; Merrill, B.M.; !1Wood, E.R.; Baylis, S.A.; Charles, I.G. !$#journal Arch. Biochem. Biophys. (1994) 311:235-241 !$#title Purification and characterization of the constitutive nitric !1oxide synthase from human placenta. !$#cross-references MUID:94263196; PMID:7515611 !$#accession S45691 !'##molecule_type protein !'##residues 'XX',169-175;531-536,'X',538-540;835,'X',837-843,'X', !1845;876-877,'X',879-881;886-898;1001-1005;1068-1077,'X',1079 !1##label GAR !'##experimental_source placenta REFERENCE I37361 !$#authors Nadaud, S.; Bonnardeaux, A.; Lathrop, M.; Soubrier, F. !$#journal Biochem. Biophys. Res. Commun. (1994) 198:1027-1033 !$#title Gene structure, polymorphism and mapping of the human !1endothelial nitric oxide synthase gene. !$#cross-references MUID:94161710; PMID:7509596 !$#accession I37361 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-297,'D',299-566,'W',568-1193,'E',1195-1203 ##label NAD !'##cross-references EMBL:X76303; NID:g461307; PIDN:CAA53950.1; !1PID:g825652 GENETICS !$#gene GDB:NOS3 !'##cross-references GDB:209976; OMIM:163729 !$#map_position 7q36-7q36 !$#introns 53/2; 90/3; 140/2; 194/3; 225/2; 272/3; 319/2; 377/3; 411/3; !1476/3; 501/2; 549/3; 584/3; 607/2; 646/2; 704/3; 749/1; 775/ !12; 838/1; 895/3; 966/1; 995/2; 1036/1; 1085/3; 1150/3 FUNCTION !$#description catalyzes the oxidation of an L-arginine guanidino nitrogen !1and of NADPH by dioxygen to produce nitric oxide, citrulline !1and NADP+ CLASSIFICATION #superfamily nitric-oxide synthase; flavodoxin homology; !1NADPH-ferrihemoprotein reductase homology KEYWORDS blocked amino end; calmodulin binding; chromoprotein; FAD; !1flavoprotein; FMN; heme; iron; lipoprotein; metalloprotein; !1myristylation; NADP; oxidoreductase FEATURE !$491-509 #region calmodulin binding #status predicted\ !$520-1159 #domain NADPH-ferrihemoprotein reductase homology !8#label FEH\ !$522-703 #domain flavodoxin homology #label FLX\ !$648-680 #region FMN binding #status predicted\ !$791-804 #region FAD-pyrophosphate binding #status predicted\ !$935-946 #region FAD-isoalloxazine binding #status predicted\ !$1010-1028 #region NADP-ribose binding #status predicted\ !$1108-1124 #region NADP-adenine binding #status predicted\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #modified_site aspartic acid (Asn) #status predicted\ !$184 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 1203 #molecular-weight 133288 #checksum 9542 SEQUENCE /// ENTRY A38943 #type complete TITLE nitric-oxide synthase (EC 1.14.13.39), endothelial - bovine ALTERNATE_NAMES ECNOS; nitric-oxide synthase type III ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 02-Jun-1995 #sequence_revision 02-Jun-1995 #text_change 03-Mar-2000 ACCESSIONS A38943; A46033; I45945; A42841; I45946; A38944 REFERENCE A38943 !$#authors Lamas, S.; Marsden, P.A.; Li, G.K.; Tempst, P.; Michel, T. !$#submission submitted to GenBank, July 1992 !$#accession A38943 !'##molecule_type mRNA !'##residues 1-1205 ##label LAM1 !'##cross-references GB:M89952; NID:g162976; PIDN:AAA30494.1; !1PID:g162977 !'##experimental_source aortic endothelial cells REFERENCE A46033 !$#authors Lamas, S.; Marsden, P.A.; Li, G.K.; Tempst, P.; Michel, T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:6348-6352 !$#title Endothelial nitric oxide synthase: molecular cloning and !1characterization of a distinct constitutive enzyme isoform. !$#cross-references MUID:92335295; PMID:1378626 !$#accession A46033 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-860,'I',862-1205 ##label LAM2 !'##cross-references GB:M89952; NID:g162976 !'##experimental_source endothelial !'##note sequence extracted from NCBI backbone (NCBIP:108720) REFERENCE I45945 !$#authors Nishida, K.; Harrison, D.G.; Navas, J.P.; Fisher, A.A.; !1Dockery, S.P.; Nerem, R.M.; Alexander, R.W.; Murphy, T.J. !$#journal J. Clin. Invest. (1992) 90:2092-2096 !$#title Molecular Cloning and Characterization of the constitutive !1bovine aortic Endothelial cell Nitric Oxide synthase. !$#cross-references MUID:93055452; PMID:1385480 !$#accession I45945 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-1205 ##label NIS !'##cross-references GB:M99057; NID:g163421; PIDN:AAA30667.1; !1PID:g163422 REFERENCE A42841 !$#authors Sessa, W.C.; Harrison, J.K.; Barber, C.M.; Zeng, D.; !1Durieux, M.E.; D'Angelo, D.D.; Lynch, K.R.; Peach, M.J. !$#journal J. Biol. Chem. (1992) 267:15274-15276 !$#title Molecular cloning and expression of a cDNA encoding !1endothelial cell nitric oxide synthase. !$#cross-references MUID:92348367; PMID:1379225 !$#accession A42841 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-51,'N',53-99,'R',101-147,'M',149-164,'I',166-317,'GA', !1320,'HTGVVRGP',329-359,'N',361-407,'Y',409-422,'W',424-431, !1'M',433-454,'Y',456-458,'P',460-462,'W',464-504,'Y',506-511, !1'N',513-515,'K',517-692,'G',694-740,'A',742-753,'N',755-799, !1'N',801-803,'SA',806-856,'V',858-906,'LV',909-955,'N', !1957-973,'M',975-988,'P',990,'Y',992-1041,'H',1043-1157,'N', !11159-1205 ##label SE2 !'##experimental_source aortic endothelial cells !'##note sequence extracted from NCBI backbone (NCBIP:109564); contains !1a number of typographical errors !$#accession I45946 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-99,'R',101-164,'I',166-317,'GA',320,'HTGVVRGP',329-454, !1'Y',456-458,'P',460-740,'A',742-803,'SA',806-856,'V', !1858-906,'LV',909-1041,'H',1043-1205 ##label SE3 !'##cross-references GB:M95674; NID:g163426; PIDN:AAA30669.1; !1PID:g163427 !'##experimental_source aortic endothelial cells !'##note submitted to GenBank, August 1992 !'##note GenBank entry BOVNOS, release 103.0, has a typographical error !1in the reference citation FUNCTION !$#description catalyzes the oxidation of an L-arginine guanidino nitrogen !1and of NADPH by dioxygen to produce nitric oxide, citrulline !1and NADP+ CLASSIFICATION #superfamily nitric-oxide synthase; flavodoxin homology; !1NADPH-ferrihemoprotein reductase homology KEYWORDS blocked amino end; calmodulin binding; chromoprotein; FAD; !1flavoprotein; FMN; heme; iron; lipoprotein; metalloprotein; !1myristylation; NADP; oxidoreductase FEATURE !$493-512 #region calmodulin binding #status predicted\ !$522-1161 #domain NADPH-ferrihemoprotein reductase homology !8#label FEH\ !$524-705 #domain flavodoxin homology #label FLX\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #modified_site aspartic acid (Asn) #status predicted\ !$186 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 1205 #molecular-weight 133286 #checksum 242 SEQUENCE /// ENTRY A43271 #type complete TITLE nitric-oxide synthase (EC 1.14.13.39), calmodulin-independent - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS A43271; A42166; JN0458; A46186 REFERENCE A43271 !$#authors Xie, Q.; Cho, H.J.; Calaycay, J.; Mumford, R.A.; Swiderek, !1K.M.; Lee, T.D.; Ding, A.; Troso, T.; Nathan, C. !$#journal Science (1992) 256:225-228 !$#title Cloning and characterization of inducible nitric oxide !1synthase from mouse macrophages. !$#cross-references MUID:92229444; PMID:1373522 !$#accession A43271 !'##status preliminary !'##molecule_type mRNA !'##residues 1-1144 ##label XIE !'##cross-references GB:M87039; NID:g198406; PIDN:AAA39315.1; !1PID:g198407 REFERENCE A42166 !$#authors Lyons, C.R.; Orloff, G.J.; Cunningham, J.M. !$#journal J. Biol. Chem. (1992) 267:6370-6374 !$#title Molecular cloning and functional expression of an inducible !1nitric oxide synthase from a murine macrophage cell line. !$#cross-references MUID:92210618; PMID:1372907 !$#accession A42166 !'##status preliminary !'##molecule_type mRNA !'##residues 1-1144 ##label LYO !'##cross-references GB:M84373; NID:g200095; PIDN:AAA39834.1; !1PID:g200096 REFERENCE JN0457 !$#authors Wood, E.R.; Berger Jr., H.; Sherman, P.A.; Lapetina, E.G. !$#journal Biochem. Biophys. Res. Commun. (1993) 191:767-774 !$#title Hepatocytes and macrophages express an identical cytokine !1inducible nitric oxide synthase gene. !$#cross-references MUID:93221515; PMID:7682072 !$#accession JN0458 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-278,'F',280-682,'H',684-937,939-1144 ##label WOO !'##experimental_source liver REFERENCE A46186 !$#authors Lowenstein, C.J.; Glatt, C.S.; Bredt, D.S.; Snyder, S.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:6711-6715 !$#title Cloned and expressed macrophage nitric oxide synthase !1contrasts with the brain enzyme. !$#cross-references MUID:92357701; PMID:1379716 !$#accession A46186 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-190,'V',192-765,'P',767-843,'G',845-1144 ##label LOW !'##cross-references GB:M92649; NID:g200109 !'##experimental_source BALB/c, RAW 264.7 cells, macrophage !'##note sequence extracted from NCBI backbone (NCBIP:113541) GENETICS !$#gene NOS FUNCTION !$#description catalyzes the oxidation of an L-arginine guanidino nitrogen !1and of NADPH by dioxygen to produce nitric oxide, citrulline !1and NADP+ CLASSIFICATION #superfamily nitric-oxide synthase; flavodoxin homology; !1NADPH-ferrihemoprotein reductase homology KEYWORDS calmodulin binding; chromoprotein; FAD; flavoprotein; FMN; !1heme; iron; metalloprotein; NADP; oxidoreductase FEATURE !$533-1121 #domain NADPH-ferrihemoprotein reductase homology !8#label FEH\ !$535-671 #domain flavodoxin homology #label FLX\ !$194 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 1144 #molecular-weight 130574 #checksum 8294 SEQUENCE /// ENTRY S47647 #type complete TITLE nitric-oxide synthase (EC 1.14.13.39) - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 16-Jun-2000 ACCESSIONS S47647; JC1472 REFERENCE S47647 !$#authors Geng, Y.; Almqvist, M.; Hansson, G.K. !$#journal Biochim. Biophys. Acta (1994) 1218:421-424 !$#title cDNA cloning and expression of inducible nitric oxide !1synthase from rat vascular smooth muscle cells. !$#cross-references MUID:94325351; PMID:7519448 !$#accession S47647 !'##molecule_type mRNA !'##residues 1-1147 ##label GEN !'##cross-references EMBL:X76881; NID:g439283; PIDN:CAA54208.1; !1PID:g439284 REFERENCE JC1472 !$#authors Nunokawa, Y.; Ishida, N.; Tanaka, S. !$#journal Biochem. Biophys. Res. Commun. (1993) 191:89-94 !$#title Cloning of inducible nitric oxide synthase in rat vascular !1smooth muscle cells. !$#cross-references MUID:93191721; PMID:7680561 !$#accession JC1472 !'##molecule_type DNA !'##residues 1-71,'Y',73-347,'PV',350-678,'VP',681-720,'L',722-739,'L', !1741-843,'G',845-1083,'M',1085-1147 ##label NUN !'##cross-references DDBJ:D14051; NID:g286260; PIDN:BAA03138.1; !1PID:g286261 !'##experimental_source vascular smooth muscle CLASSIFICATION #superfamily nitric-oxide synthase; flavodoxin homology; !1NADPH-ferrihemoprotein reductase homology KEYWORDS calmodulin binding; chromoprotein; FAD; flavoprotein; FMN; !1heme; iron; metalloprotein; NADP; oxidoreductase FEATURE !$536-1124 #domain NADPH-ferrihemoprotein reductase homology !8#label FEH\ !$538-674 #domain flavodoxin homology #label FLX\ !$197 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 1147 #molecular-weight 130660 #checksum 5127 SEQUENCE /// ENTRY I56575 #type complete TITLE nitric-oxide synthase (EC 1.14.13.39) [similarity] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 05-May-2000 ACCESSIONS I56575 REFERENCE I56575 !$#authors Galea, E.; Reis, D.J.; Feinstein, D.L. !$#journal J. Neurosci. Res. (1994) 37:406-414 !$#title Cloning and expression of inducible nitric oxide synthase !1from rat astrocytes. !$#cross-references MUID:94231594; PMID:7513765 !$#accession I56575 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-1147 ##label RES !'##cross-references EMBL:U03699; NID:g430718; PIDN:AAC13747.1; !1PID:g430719 CLASSIFICATION #superfamily nitric-oxide synthase; flavodoxin homology; !1NADPH-ferrihemoprotein reductase homology KEYWORDS calmodulin binding; chromoprotein; FAD; flavoprotein; FMN; !1heme; iron; metalloprotein; NADP; oxidoreductase FEATURE !$536-1124 #domain NADPH-ferrihemoprotein reductase homology !8#label FEH\ !$538-674 #domain flavodoxin homology #label FLX\ !$197 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 1147 #molecular-weight 130641 #checksum 4419 SEQUENCE /// ENTRY S38253 #type complete TITLE nitric-oxide synthase (EC 1.14.13.39) - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 16-Jun-2000 ACCESSIONS S38253; JN0457 REFERENCE S38253 !$#authors Adachi, H.; Iida, S.; Oguchi, S.; Ohshima, H.; Suzuki, H.; !1Nagasaki, K.; Kawasaki, H.; Sugimura, T.; Esumi, H. !$#journal Eur. J. Biochem. (1993) 217:37-43 !$#title Molecular cloning of a cDNA encoding an inducible !1calmodulin-dependent nitric-oxide synthase from rat liver !1and its expression in COS 1 cells. !$#cross-references MUID:94039059; PMID:7693462 !$#accession S38253 !'##molecule_type mRNA !'##residues 1-1147 ##label ADA !'##cross-references GB:D12520; NID:g391858; PIDN:BAA02090.1; !1PID:g391859 !'##experimental_source liver REFERENCE JN0457 !$#authors Wood, E.R.; Berger Jr., H.; Sherman, P.A.; Lapetina, E.G. !$#journal Biochem. Biophys. Res. Commun. (1993) 191:767-774 !$#title Hepatocytes and macrophages express an identical cytokine !1inducible nitric oxide synthase gene. !$#cross-references MUID:93221515; PMID:7682072 !$#accession JN0457 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-41,'SS',44-103,105-190,'Q',192-213,'R',215-247,'T', !1249-263,'I',265-373,'IE',376-394,'R',396-409,'D',410-582, !1'P',584-612,'HG',615-735,'L',737-755,'S',757-761,'H', !1763-819,821,'S',823-894,'S',896-1000,'LG',1003-1015,'RR', !11018-1026,'EQ',1029-1147 ##label WOO !'##cross-references PIDN:AAB26037.1 !'##experimental_source liver GENETICS !$#gene NOS FUNCTION !$#description catalyzes the oxidation of an L-arginine guanidino nitrogen !1and of NADPH by dioxygen to produce nitric oxide, citrulline !1and NADP+ CLASSIFICATION #superfamily nitric-oxide synthase; flavodoxin homology; !1NADPH-ferrihemoprotein reductase homology KEYWORDS calmodulin binding; chromoprotein; FAD; flavoprotein; FMN; !1heme; iron; metalloprotein; NADP; oxidoreductase FEATURE !$536-1124 #domain NADPH-ferrihemoprotein reductase homology !8#label FEH\ !$538-674 #domain flavodoxin homology #label FLX\ !$197 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 1147 #molecular-weight 130584 #checksum 4402 SEQUENCE /// ENTRY I53165 #type complete TITLE nitric-oxide synthase (EC 1.14.13.39) [similarity] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 05-May-2000 ACCESSIONS I53165 REFERENCE I53165 !$#authors Karlsen, A.E.; Andersen, H.U.; Vissing, H.; Larsen, P.M.; !1Fey, S.J.; Cuartero, B.G.; Madsen, O.D.; Petersen, J.S.; !1Mortensen, S.B.; Mandrup-Poulsen, T.; Boel, E.; Nerup, J. !$#journal Diabetes (1995) 44:753-758 !$#title Cloning and expression of cytokine-inducible nitric oxide !1synthase cDNA from rat islets of Langerhans. !$#cross-references MUID:95309542; PMID:7540573 !$#accession I53165 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-1147 ##label RES !'##cross-references EMBL:U26686; NID:g886072; PIDN:AAA85861.1; !1PID:g886073 GENETICS !$#gene NOS2 CLASSIFICATION #superfamily nitric-oxide synthase; flavodoxin homology; !1NADPH-ferrihemoprotein reductase homology KEYWORDS calmodulin binding; chromoprotein; FAD; flavoprotein; FMN; !1heme; iron; metalloprotein; NADP; oxidoreductase FEATURE !$536-1124 #domain NADPH-ferrihemoprotein reductase homology !8#label FEH\ !$538-674 #domain flavodoxin homology #label FLX\ !$197 #binding_site heme iron (Cys) (axial ligand) #status !8predicted SUMMARY #length 1147 #molecular-weight 130705 #checksum 5905 SEQUENCE /// ENTRY S00574 #type complete TITLE alkanal monooxygenase (FMN-linked) (EC 1.14.14.3) alpha chain - Vibrio fischeri ALTERNATE_NAMES luciferase alpha chain ORGANISM #formal_name Vibrio fischeri DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS S00574 REFERENCE S00574 !$#authors Foran, D.R.; Brown, W.M. !$#journal Nucleic Acids Res. (1988) 16:777 !$#title Nucleotide sequence of the LuxA and LuxB genes of the !1bioluminescent marine bacterium Vibrio fischeri. !$#cross-references MUID:88124280; PMID:3340562 !$#accession S00574 !'##status translation not shown !'##molecule_type DNA !'##residues 1-354 ##label FOR !'##cross-references EMBL:X06758; NID:g48432; PIDN:CAA29931.1; !1PID:g48433 GENETICS !$#gene LuxA CLASSIFICATION #superfamily alkanal monooxygenase (FMN-linked) KEYWORDS flavoprotein; FMN; luminescence; monooxygenase; !1oxidoreductase SUMMARY #length 354 #molecular-weight 40342 #checksum 6285 SEQUENCE /// ENTRY JH0387 #type complete TITLE alkanal monooxygenase (FMN-linked) (EC 1.14.14.3) alpha chain [validated] - Photobacterium phosphoreum ALTERNATE_NAMES bacterial luciferase alpha chain ORGANISM #formal_name Photobacterium phosphoreum DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS JH0387 REFERENCE JH0387 !$#authors Ferri, S.R.; Soly, R.R.; Szittner, R.B.; Meighen, E.A. !$#journal Biochem. Biophys. Res. Commun. (1991) 176:541-548 !$#title Structure and properties of luciferase from Photobacterium !1phosphoreum. !$#cross-references MUID:91207448; PMID:2018544 !$#accession JH0387 !'##molecule_type DNA !'##residues 1-346 ##label FER !'##cross-references GB:M65067; NID:g150694; PIDN:AAA70297.1; !1PID:g150695 COMMENT Luciferase catalyzes the oxidation of long chain aldehydes !1and FMNH2 to produce the corresponding fatty acid. GENETICS !$#gene luxA CLASSIFICATION #superfamily alkanal monooxygenase (FMN-linked) KEYWORDS flavoprotein; FMN; luminescence; monooxygenase; !1oxidoreductase SUMMARY #length 346 #molecular-weight 39364 #checksum 5717 SEQUENCE /// ENTRY S17953 #type complete TITLE alkanal monooxygenase (FMN-linked) (EC 1.14.14.3) alpha chain [validated] - Photobacterium leiognathi ALTERNATE_NAMES luciferase alpha chain ORGANISM #formal_name Photobacterium leiognathi DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS S17953 REFERENCE S17836 !$#authors Lee, C.Y.; Szittner, R.B.; Meighen, E.A. !$#journal Eur. J. Biochem. (1991) 201:161-167 !$#title The lux genes of the luminous bacterial symbiont, !1Photobacterium leiognathi, of the ponyfish. Nucleotide !1sequence, difference in gene organization, and high !1expression in mutant Escherichia coli. !$#cross-references MUID:92007870; PMID:1915359 !$#accession S17953 !'##molecule_type DNA !'##residues 1-354 ##label LEE !'##cross-references EMBL:M63594; NID:g150687; PIDN:AAA25618.1; !1PID:g150690 GENETICS !$#gene luxA CLASSIFICATION #superfamily alkanal monooxygenase (FMN-linked) KEYWORDS flavoprotein; FMN; luminescence; monooxygenase; !1oxidoreductase SUMMARY #length 354 #molecular-weight 40402 #checksum 1453 SEQUENCE /// ENTRY A22613 #type complete TITLE alkanal monooxygenase (FMN-linked) (EC 1.14.14.3) alpha chain - Vibrio harveyi ALTERNATE_NAMES bacterial luciferase alpha chain ORGANISM #formal_name Vibrio harveyi DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS A22613; S18546 REFERENCE A92523 !$#authors Cohn, D.H.; Mileham, A.J.; Simon, M.I.; Nealson, K.H.; !1Rausch, S.K.; Bonam, D.; Baldwin, T.O. !$#journal J. Biol. Chem. (1985) 260:6139-6146 !$#title Nucleotide sequence of the luxA gene of Vibrio harveyi and !1the complete amino acid sequence of the alpha subunit of !1bacterial luciferase. !$#cross-references MUID:85207595; PMID:3997817 !$#accession A22613 !'##molecule_type DNA !'##residues 1-355 ##label COH !'##cross-references GB:M10961; GB:M13494; NID:g155174; PIDN:AAA88685.1; !1PID:g155175 REFERENCE S18546 !$#authors Escher, A.; O'Kane, D.J.; Szalay, A.A. !$#journal Mol. Gen. Genet. (1991) 230:385-393 !$#title The beta subunit polypeptide of Vibrio harveyi luciferase !1determines light emission at 42 C. !$#cross-references MUID:92114868; PMID:1685011 !$#accession S18546 !'##status preliminary; translation not shown !'##molecule_type DNA !'##residues 1-67,'K',69-203,'HV',206-237,'K',239-320,'N',322-355 !1##label ESC !'##cross-references EMBL:X58791; NID:g48446; PIDN:CAA41597.1; !1PID:g48447 GENETICS !$#gene luxA CLASSIFICATION #superfamily alkanal monooxygenase (FMN-linked) KEYWORDS flavoprotein; FMN; luminescence; monooxygenase; !1oxidoreductase SUMMARY #length 355 #molecular-weight 40153 #checksum 5418 SEQUENCE /// ENTRY D42951 #type complete TITLE alkanal monooxygenase (FMN-linked) (EC 1.14.14.3) beta chain [similarity] - Xenorhabdus luminescens ALTERNATE_NAMES luciferase beta chain ORGANISM #formal_name Xenorhabdus luminescens DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS D42951; D38448 REFERENCE A42951 !$#authors Meighen, E.A.; Szittner, R.B. !$#journal J. Bacteriol. (1992) 174:5371-5381 !$#title Multiple repetitive elements and organization of the lux !1operons of luminescent terrestrial bacteria. !$#cross-references MUID:92355513; PMID:1644764 !$#accession D42951 !'##molecule_type DNA !'##residues 1-324 ##label MEI !'##cross-references GB:M90092; NID:g155411; PIDN:AAD05358.1; !1PID:g155415 !'##experimental_source strain Hw !'##note sequence extracted from NCBI backbone (NCBIN:110516, !1NCBIP:110523) REFERENCE A38448 !$#authors Xi, L.; Cho, K.W.; Tu, S.C. !$#journal J. Bacteriol. (1991) 173:1399-1405 !$#title Cloning and nucleotide sequences of lux genes and !1characterization of luciferase of Xenorhabdus luminescens !1from a human wound. !$#cross-references MUID:91139581; PMID:1995589 !$#accession D38448 !'##status preliminary !'##molecule_type DNA !'##residues 1-114,'P',116-157,'M',159-291,'T',293-324 ##label XIA !'##cross-references GB:M62917; GB:M38525; NID:g155427; PIDN:AAA63566.1; !1PID:g155431 CLASSIFICATION #superfamily alkanal monooxygenase (FMN-linked) KEYWORDS flavoprotein; FMN; luminescence; monooxygenase; !1oxidoreductase SUMMARY #length 324 #molecular-weight 37093 #checksum 1780 SEQUENCE /// ENTRY S00575 #type complete TITLE alkanal monooxygenase (FMN-linked) (EC 1.14.14.3) beta chain [similarity] - Vibrio fischeri ALTERNATE_NAMES luciferase beta chain ORGANISM #formal_name Vibrio fischeri DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS S00575 REFERENCE S00574 !$#authors Foran, D.R.; Brown, W.M. !$#journal Nucleic Acids Res. (1988) 16:777 !$#title Nucleotide sequence of the LuxA and LuxB genes of the !1bioluminescent marine bacterium Vibrio fischeri. !$#cross-references MUID:88124280; PMID:3340562 !$#accession S00575 !'##status translation not shown !'##molecule_type DNA !'##residues 1-326 ##label FOR !'##cross-references EMBL:X06758; NID:g48432; PIDN:CAA29932.1; !1PID:g48434 GENETICS !$#gene LuxB CLASSIFICATION #superfamily alkanal monooxygenase (FMN-linked) KEYWORDS flavoprotein; FMN; luminescence; monooxygenase; !1oxidoreductase SUMMARY #length 326 #molecular-weight 37357 #checksum 2151 SEQUENCE /// ENTRY S17954 #type complete TITLE alkanal monooxygenase (FMN-linked) (EC 1.14.14.3) beta chain [validated] - Photobacterium leiognathi ALTERNATE_NAMES luciferase beta chain ORGANISM #formal_name Photobacterium leiognathi DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS S17954 REFERENCE S17836 !$#authors Lee, C.Y.; Szittner, R.B.; Meighen, E.A. !$#journal Eur. J. Biochem. (1991) 201:161-167 !$#title The lux genes of the luminous bacterial symbiont, !1Photobacterium leiognathi, of the ponyfish. Nucleotide !1sequence, difference in gene organization, and high !1expression in mutant Escherichia coli. !$#cross-references MUID:92007870; PMID:1915359 !$#accession S17954 !'##molecule_type DNA !'##residues 1-326 ##label LEE !'##cross-references EMBL:M63594; NID:g150687; PIDN:AAA25619.1; !1PID:g150691 GENETICS !$#gene luxE CLASSIFICATION #superfamily alkanal monooxygenase (FMN-linked) KEYWORDS flavoprotein; FMN; luminescence; monooxygenase; !1oxidoreductase SUMMARY #length 326 #molecular-weight 37701 #checksum 7053 SEQUENCE /// ENTRY JH0388 #type complete TITLE alkanal monooxygenase (FMN-linked) (EC 1.14.14.3) beta chain [validated] - Photobacterium phosphoreum ALTERNATE_NAMES bacterial luciferase beta chain ORGANISM #formal_name Photobacterium phosphoreum DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 21-Jul-2000 ACCESSIONS JH0388; B31572 REFERENCE JH0387 !$#authors Ferri, S.R.; Soly, R.R.; Szittner, R.B.; Meighen, E.A. !$#journal Biochem. Biophys. Res. Commun. (1991) 176:541-548 !$#title Structure and properties of luciferase from Photobacterium !1phosphoreum. !$#cross-references MUID:91207448; PMID:2018544 !$#accession JH0388 !'##molecule_type DNA !'##residues 1-318 ##label FER !'##cross-references GB:M65067; NID:g150694; PIDN:AAA70298.1; !1PID:g150696 REFERENCE A90145 !$#authors Soly, R.R.; Mancini, J.A.; Ferri, S.R.; Boylan, M.; Meighen, !1E.A. !$#journal Biochem. Biophys. Res. Commun. (1988) 155:351-358 !$#title A new lux gene in bioluminescent bacteria codes for a !1protein homologous to the bacterial luciferase subunits. !$#cross-references MUID:88326325; PMID:3415691 !$#accession B31572 !'##molecule_type DNA !'##residues 301-307,'V',308-318 ##label SOL !'##cross-references GB:M22128; NID:g150698; PIDN:AAA25622.1; !1PID:g150699 COMMENT Luciferase catalyzes the oxidation of long chain aldehydes !1and FMNH2 to produce the corresponding fatty acid. GENETICS !$#gene luxB CLASSIFICATION #superfamily alkanal monooxygenase (FMN-linked) KEYWORDS flavoprotein; FMN; luminescence; monooxygenase; !1oxidoreductase SUMMARY #length 318 #molecular-weight 36397 #checksum 4105 SEQUENCE /// ENTRY A31266 #type complete TITLE alkane 1-monooxygenase (EC 1.14.15.3) - Pseudomonas oleovorans plasmid OCT ALTERNATE_NAMES alkane 1-hydroxylase ORGANISM #formal_name Pseudomonas oleovorans DATE 26-Apr-1989 #sequence_revision 26-May-1995 #text_change 11-Jun-1999 ACCESSIONS A32849; S27990; A31266 REFERENCE A32849 !$#authors Kok, M.; Oldenhuis, R.; van der Linden, M.P.G.; Raatjes, P.; !1Kingma, J.; van Lelyveld, P.H.; Witholt, B. !$#journal J. Biol. Chem. (1989) 264:5435-5441 !$#title The Pseudomonas oleovorans alkane hydroxylase gene. Sequence !1and expression. !$#cross-references MUID:89174581; PMID:2647718 !$#accession A32849 !'##molecule_type DNA !'##residues 1-401 ##label KOK !'##cross-references GB:X65936; GB:J04618; NID:g49078; PIDN:CAA46733.1; !1PID:g49079; GB:J04619 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by peptide sequencing REFERENCE A40196 !$#authors van Beilen, J.B.; Penninga, D.; Witholt, B. !$#journal J. Biol. Chem. (1992) 267:9194-9201 !$#title Topology of the membrane-bound alkane hydroxylase of !1Pseudomonas oleovorans. !$#cross-references MUID:92250518; PMID:1315749 !$#contents annotation REFERENCE S27990 !$#authors van Beilen, J.B.; Eggink, G.; Enequist, H.; Bos, R.; !1Witholt, B. !$#journal Mol. Microbiol. (1992) 6:3121-3136 !$#title DNA sequence determination and functional characterization !1of the OCT-plasmid-encoded alkJKL genes of Pseudomonas !1oleovorans. !$#cross-references MUID:93086421; PMID:1453953 !$#accession S27990 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-401 ##label BEI !'##cross-references EMBL:X65936; NID:g49078; PIDN:CAA46733.1; !1PID:g49079 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1992 GENETICS !$#gene alkB !$#genome plasmid OCT CLASSIFICATION #superfamily alkane 1-monooxygenase KEYWORDS inner membrane; oxidoreductase; transmembrane protein FEATURE !$1-401 #product alkane 1-monooxygenase #status predicted !8#label MAT\ !$20-39 #domain transmembrane #status predicted #label TM1\ !$40-42 #domain periplasmic #status predicted #label PR1\ !$43-62 #domain transmembrane #status predicted #label TM2\ !$89-109 #domain transmembrane #status predicted #label TM3\ !$110-112 #domain periplasmic #status predicted #label PR2\ !$113-134 #domain transmembrane #status predicted #label TM4\ !$228-246 #domain transmembrane #status predicted #label TM5\ !$247-249 #domain periplasmic #status predicted #label PR3\ !$250-271 #domain transmembrane #status predicted #label TM6 SUMMARY #length 401 #molecular-weight 45806 #checksum 159 SEQUENCE /// ENTRY WHHUF #type complete TITLE phenylalanine 4-monooxygenase (EC 1.14.16.1) - human ALTERNATE_NAMES phenylalanine 4-hydroxylase ORGANISM #formal_name Homo sapiens #common_name man DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 21-Jul-2000 ACCESSIONS A00508; S02687; I52416; I54346; S74142; I54257 REFERENCE A00508 !$#authors Kwok, S.C.M.; Ledley, F.D.; DiLella, A.G.; Robson, K.J.H.; !1Woo, S.L.C. !$#journal Biochemistry (1985) 24:556-561 !$#title Nucleotide sequence of a full-length complementary DNA clone !1and amino acid sequence of human phenylalanine hydroxylase. !$#cross-references MUID:85199778; PMID:2986678 !$#accession A00508 !'##molecule_type mRNA !'##residues 1-452 ##label KWO !'##cross-references GB:K03020; NID:g189936; PIDN:AAA60082.1; !1PID:g189937 REFERENCE S02687 !$#authors Cotton, R.G.H.; McAdam, W.; Jennings, I.; Morgan, F.J. !$#journal Biochem. J. (1988) 255:193-196 !$#title A monoclonal antibody to aromatic amino acid hydroxylases. !1Identification of the epitope. !$#cross-references MUID:89061656; PMID:2461704 !$#accession S02687 !'##molecule_type protein !'##residues 131-144 ##label COT REFERENCE I52416 !$#authors Konecki, D.S.; Wang, Y.; Trefz, F.K.; Lichter-Konecki, U.; !1Woo, S.L. !$#journal Biochemistry (1992) 31:8363-8368 !$#title Structural characterization of the 5' regions of the human !1phenylalanine hydroxylase gene. !$#cross-references MUID:92399453; PMID:1326329 !$#accession I52416 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-20 ##label KON !'##cross-references GB:S44225; NID:g255493 REFERENCE I54346 !$#authors Abadie, V.; Jaruzelska, J.; Lyonnet, S.; Millasseau, P.; !1Berthelon, M.; Rey, F.; Munnich, A.; Rey, J. !$#journal Hum. Mol. Genet. (1993) 2:31-34 !$#title Illegitimate transcription of the phenylalanine hydroxylase !1gene in lymphocytes for identification of mutations in !1phenylketonuria. !$#cross-references MUID:93258345; PMID:8098245 !$#accession I54346 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 381-389,'G',391-405 ##label ABA !'##cross-references GB:S61296; NID:g300410; PIDN:AAD13926.1; !1PID:g4261626 !'##experimental_source lymphocytes, mutant form REFERENCE S74142 !$#authors Kowlessur, D.; Citron, B.A.; Kaufman, S. !$#journal Arch. Biochem. Biophys. (1996) 333:85-95 !$#title Recombinant human phenylalanine hydroxylase: novel !1regulatory and structural properties. !$#cross-references MUID:96400381; PMID:8806757 !$#accession S74142 !'##molecule_type protein !'##residues 2-21 ##label KOW REFERENCE I54257 !$#authors Eigel, A.; Dworniczak, B.; Kalaydjieva, L.; Horst, J. !$#journal Hum. Genet. (1991) 87:739-741 !$#title A frameshift mutation in exon 2 of the phenylalanine !1hydroxylase gene linked to RFLP haplotype 1. !$#cross-references MUID:92039642; PMID:1682235 !$#accession I54257 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 53-54,'LRRMM' ##label EIG !'##cross-references GB:S62592; NID:g238240; PIDN:AAB20205.1; !1PID:g238241 !'##note mutant sequence found in patients with phenylketonuria GENETICS !$#gene GDB:PAH !'##cross-references GDB:119470; OMIM:261600 !$#map_position 12q24.1-12q24.1 !$#note a defect in this gene can cause phenylketonuria COMPLEX homodimer FUNCTION !$#description catalyzes the 4'-hydroxylation of phenylalanine to tyrosine !1by tetrahydrobiopterin and oxygen !$#pathway tyrosine biosynthesis; phenylalanine catabolism CLASSIFICATION #superfamily phenylalanine 4-monooxygenase KEYWORDS biopterin; homodimer; iron; metalloprotein; monooxygenase; !1oxidoreductase; phenylalanine catabolism; phenylketonuria; !1phosphoprotein; tyrosine biosynthesis FEATURE !$16 #binding_site phosphate (Ser) (covalent) (by !8calmodulin-dependent kinase) #status predicted\ !$23 #binding_site phosphate (Ser) (covalent) (by !8cAMP-dependent kinase) #status predicted\ !$285,290,330 #binding_site iron (His, His, Glu) #status predicted SUMMARY #length 452 #molecular-weight 51862 #checksum 2416 SEQUENCE /// ENTRY WHRTF #type complete TITLE phenylalanine 4-monooxygenase (EC 1.14.16.1) - rat ALTERNATE_NAMES phenylalanine 4-hydroxylase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 04-Dec-1986 #sequence_revision 19-Oct-1995 #text_change 03-Mar-2000 ACCESSIONS A25321; A00509; A14970 REFERENCE A25321 !$#authors Dahl, H.H.M.; Mercer, J.F.B. !$#journal J. Biol. Chem. (1986) 261:4148-4153 !$#title Isolation and sequence of a cDNA clone which contains the !1complete coding region of rat phenylalanine hydroxylase. !$#cross-references MUID:86140234; PMID:2869038 !$#accession A25321 !'##molecule_type mRNA !'##residues 1-453 ##label DAH !'##cross-references GB:M12337; NID:g206120; PIDN:AAA41843.1; !1PID:g206121 REFERENCE A00509 !$#authors Robson, K.J.H.; Beattie, W.; James, R.J.; Cotton, R.C.H.; !1Morgan, F.J.; Woo, S.L.C. !$#journal Biochemistry (1984) 23:5671-5675 !$#title Sequence comparison of rat liver phenylalanine hydroxylase !1and its cDNA clones. !$#cross-references MUID:85122617; PMID:6098294 !$#accession A00509 !'##molecule_type mRNA !'##residues 208-453 ##label ROB !'##cross-references GB:K02599; NID:g205961; PIDN:AAA41794.1; !1PID:g205962 REFERENCE A14970 !$#authors Wretborn, M.; Humble, E.; Ragnarsson, U.; Engstrom, L. !$#journal Biochem. Biophys. Res. Commun. (1980) 93:403-408 !$#title Amino acid sequence at the phosphorylated site of rat liver !1phenylalanine hydroxylase and phosphorylation of a !1corresponding synthetic peptide. !$#cross-references MUID:80220293; PMID:7387651 !$#accession A14970 !'##molecule_type protein !'##residues 12-16,'B',18-19,'ZZ' ##label WRE COMPLEX homodimer FUNCTION !$#description catalyzes the 4'-hydroxylation of phenylalanine to tyrosine !1by tetrahydrobiopterin and oxygen !$#pathway tyrosine biosynthesis; phenylalanine catabolism CLASSIFICATION #superfamily phenylalanine 4-monooxygenase KEYWORDS biopterin; homodimer; iron; metalloprotein; monooxygenase; !1oxidoreductase; phenylalanine catabolism; phenylketonuria; !1phosphoprotein; tyrosine biosynthesis FEATURE !$16 #binding_site phosphate (Ser) (covalent) (by !8calmodulin-dependent kinase) #status predicted\ !$23 #binding_site phosphate (Ser) (covalent) (by !8cAMP-dependent kinase) #status predicted\ !$285,290,330 #binding_site iron (His, His, Glu) #status predicted SUMMARY #length 453 #molecular-weight 51821 #checksum 8192 SEQUENCE /// ENTRY WHRTW #type complete TITLE tryptophan 5-monooxygenase (EC 1.14.16.4) - rat ALTERNATE_NAMES tryptophan 5-hydroxylase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 03-Mar-2000 ACCESSIONS JL0034; A60034; A24367 REFERENCE JL0034 !$#authors Darmon, M.C.; Guibert, B.; Leviel, V.; Ehret, M.; Maitre, !1M.; Mallet, J. !$#journal J. Neurochem. (1988) 51:312-316 !$#title Sequence of two mRNAs encoding active rat tryptophan !1hydroxylase. !$#cross-references MUID:88244702; PMID:3379411 !$#accession JL0034 !'##molecule_type mRNA !'##residues 1-444 ##label DAR !'##cross-references GB:X53501; NID:g57760; PIDN:CAA37579.1; PID:g57761 !'##experimental_source pineal gland REFERENCE A60034 !$#authors Kim, K.S.; Wessel, T.C.; Stone, D.M.; Carver, C.H.; Joh, !1T.H.; Park, D.H. !$#journal Brain Res. Mol. Brain Res. (1991) 9:277-283 !$#title Molecular cloning and characterization of cDNA encoding !1tryptophan hydroxylase from rat central serotonergic !1neurons. !$#cross-references MUID:91245924; PMID:1645430 !$#accession A60034 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-444 ##label KIM !'##experimental_source dorsal raphe nucleus REFERENCE A24367 !$#authors Darmon, M.C.; Grima, B.; Cash, C.D.; Maitre, M.; Mallet, J. !$#journal FEBS Lett. (1986) 206:43-46 !$#title Isolation of a rat pineal gland cDNA clone homologous to !1tyrosine and phenylalanine hydroxylases. !$#cross-references MUID:87005247; PMID:2875901 !$#accession A24367 !'##molecule_type mRNA !'##residues 167-261 ##label DA2 !'##cross-references GB:M28000; NID:g207432; PIDN:AAA42262.1; !1PID:g207433 COMMENT This enzyme has different physical properties in pineal !1gland and in dorsal raphe nucleus but identical mRNA !1sequences. FUNCTION !$#description catalyzes the oxidation of tryptophan to !15'-hydroxytryptophan by tetrahydrobiopterin and oxygen !$#pathway melatonin biosynthesis; serotonin biosynthesis; tryptophan !1catabolism CLASSIFICATION #superfamily phenylalanine 4-monooxygenase KEYWORDS biopterin; iron; melatonin biosynthesis; metalloprotein; !1monooxygenase; oxidoreductase; phosphoprotein; serotonin !1biosynthesis; tryptophan catabolism FEATURE !$58 #binding_site phosphate (Ser) (covalent) (by !8cAMP-dependent kinase) #status predicted\ !$260,443 #binding_site phosphate (Ser) (covalent) (by !8calmodulin-dependent kinase) #status predicted\ !$272,277,317 #binding_site iron (His, His, Glu) #status predicted SUMMARY #length 444 #molecular-weight 51068 #checksum 1654 SEQUENCE /// ENTRY A42271 #type complete TITLE tryptophan 5-monooxygenase (EC 1.14.16.4) - fruit fly (Drosophila sp.) ALTERNATE_NAMES tryptophan hydroxylase ORGANISM #formal_name Drosophila sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 31-Mar-2000 ACCESSIONS A42271 REFERENCE A42271 !$#authors Neckameyer, W.S.; White, K. !$#journal J. Biol. Chem. (1992) 267:4199-4206 !$#title A single locus encodes both phenylalanine hydroxylase and !1tryptophan hydroxylase activities in Drosophila. !$#cross-references MUID:92156168; PMID:1371286 !$#accession A42271 !'##molecule_type mRNA !'##residues 1-453 ##label NEC !'##note sequence extracted from NCBI backbone (NCBIN:82902, !1NCBIP:82903) GENETICS !$#gene FlyBase:Tph !'##cross-references FlyBase:FBgn0005770 CLASSIFICATION #superfamily phenylalanine 4-monooxygenase KEYWORDS biopterin; iron; metalloprotein; monooxygenase; !1oxidoreductase; phosphoprotein FEATURE !$284,289,329 #binding_site iron (His, His, Glu) #status predicted SUMMARY #length 453 #molecular-weight 51682 #checksum 9022 SEQUENCE /// ENTRY S10489 #type complete TITLE tryptophan 5-monooxygenase (EC 1.14.16.4) - human ALTERNATE_NAMES tryptophan 5-hydroxylase ORGANISM #formal_name Homo sapiens #common_name man DATE 04-Sep-1998 #sequence_revision 04-Sep-1998 #text_change 03-Mar-2000 ACCESSIONS S10489; S51559 REFERENCE S10489 !$#authors Boularand, S.; Darmon, M.C.; Ganem, Y.; Launay, J.M.; !1Mallet, J. !$#journal Nucleic Acids Res. (1990) 18:4257 !$#title Complete coding sequence of human tryptophan hydroxylase. !$#cross-references MUID:90332431; PMID:2377472 !$#accession S10489 !'##molecule_type mRNA !'##residues 1-444 ##label BOU !'##cross-references EMBL:X52836; NID:g37954; PIDN:CAA37018.1; !1PID:g37955 REFERENCE S51199 !$#authors Tipper, J.P.; Citron, B.A.; Ribeiro, P.; Kaufman, S. !$#journal Arch. Biochem. Biophys. (1994) 315:445-453 !$#title Cloning and expression of rabbit and human brain tryptophan !1hydroxylase cDNA in Escherichia coli. !$#cross-references MUID:95077422; PMID:7986090 !$#accession S51559 !'##status preliminary !'##molecule_type mRNA !'##residues 1-18,'T',20-67,'T',69-89,'TP',92-96,'M',98-99,'E',101-103, !1'S',105-150,'S',152-153,'S',155-156,'Y',158-178,'R',180-206, !1'Q',208-216,'I',218-343,'V',345-413,'A',415-418,'N',420-424, !1'R',426-435,'G',437-444 ##label TIP !'##cross-references GB:L29306; NID:g531192; PIDN:AAA67050.1; !1PID:g531193 GENETICS !$#gene GDB:TPH; TPRH !'##cross-references GDB:120732; OMIM:191060 !$#map_position 11p15.1-11p14.3 FUNCTION !$#description catalyzes the oxidation of tryptophan to !15'-hydroxytryptophan by tetrahydrobiopterin and oxygen !$#pathway melatonin biosynthesis; serotonin biosynthesis; tryptophan !1catabolism CLASSIFICATION #superfamily phenylalanine 4-monooxygenase KEYWORDS biopterin; iron; melatonin biosynthesis; metalloprotein; !1monooxygenase; oxidoreductase; phosphoprotein; serotonin !1biosynthesis; tryptophan catabolism FEATURE !$58 #binding_site phosphate (Ser) (covalent) (by !8cAMP-dependent kinase) #status predicted\ !$260,443 #binding_site phosphate (Ser) (covalent) (by !8calmodulin-dependent kinase) #status predicted\ !$272,277,317 #binding_site iron (His, His, Glu) #status predicted SUMMARY #length 444 #molecular-weight 50985 #checksum 8037 SEQUENCE /// ENTRY WHHUY4 #type complete TITLE tyrosine 3-monooxygenase (EC 1.14.16.2), splice form 4 - human ALTERNATE_NAMES tyrosine 3-hydroxylase CONTAINS tyrosine 3-monooxygenase, splice form 1; tyrosine 3-monooxygenase, splice form 2; tyrosine 3-monooxygenase, splice form 3 ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 16-Jun-2000 ACCESSIONS A30002; A26825; A60201; JE0012; JE0013; JE0014; A27791; !1B27791; C27791; PN0575; PN0582; PN0588; I52396; I38340; !1I55282; I70056 REFERENCE A94509 !$#authors Nagatsu, T. !$#submission submitted to GenBank, December 1987 !$#accession A30002 !'##molecule_type mRNA !'##residues 1-528 ##label NAG1 !'##cross-references GB:M17589; NID:g339680; PIDN:AAA61179.1; !1PID:g339681 REFERENCE A90136 !$#authors Kaneda, N.; Kobayashi, K.; Ichinose, H.; Kishi, F.; !1Nakazawa, A.; Kurosawa, Y.; Fujita, K.; Nagatsu, T. !$#journal Biochem. Biophys. Res. Commun. (1987) 146:971-975 !$#title Isolation of a novel cDNA clone for human tyrosine !1hydroxylase: alternative RNA splicing produces four kinds of !1mRNA from a single gene. !$#cross-references MUID:87298614; PMID:2887169 !$#accession A26825 !'##molecule_type mRNA !'##residues 1-94 ##label NAG2 !'##cross-references GB:M17589; NID:g339680; PIDN:AAA61179.1; !1PID:g339681 REFERENCE A60201 !$#authors Le Bourdelles, B.; Boularand, S.; Boni, C.; Horellou, P.; !1Dumas, S.; Grima, B.; Mallet, J. !$#journal J. Neurochem. (1988) 50:988-991 !$#title Analysis of the 5' region of the human tyrosine hydroxylase !1gene: combinatorial patterns of exon splicing generate !1multiple regulated tyrosine hydroxylase isoforms. !$#cross-references MUID:88117543; PMID:2892893 !$#accession A60201 !'##molecule_type mRNA !'##residues 1-65 ##label LEB !'##cross-references GB:M24790; NID:g556223; PIDN:AAA61174.1; !1PID:g556224 REFERENCE JE0012 !$#authors Kobayashi, K.; Kaneda, N.; Ichinose, H.; Kishi, F.; !1Nakazawa, A.; Kurosawa, Y.; Fujita, K.; Nagatsu, T. !$#journal J. Biochem. (1988) 103:907-912 !$#title Structure of the human tyrosine hydroxylase gene: !1alternative splicing from a single gene accounts for !1generation of four mRNA types. !$#cross-references MUID:89008200; PMID:2902075 !$#accession JE0012 !'##molecule_type DNA !'##residues 1-30,62-135 ##label KOB1 !'##cross-references GB:D00269; NID:g220099; PIDN:BAA25094.1; !1PID:g2951764 !'##experimental_source splice form 1 !'##note this splice form is produced by an alternative donor site !1within exon 1 !$#accession JE0013 !'##molecule_type DNA !'##residues 1-34,62-135 ##label KOB2 !'##cross-references GB:D00269; NID:g220099; PIDN:BAA25097.1; !1PID:g2951767 !'##experimental_source splice form 2 !$#accession JE0014 !'##molecule_type DNA !'##residues 1-30,35-135 ##label KOB3 !'##cross-references GB:D00269; NID:g220099; PIDN:BAA25095.1; !1PID:g2951765 !'##experimental_source splice form 3 !'##note this splice form is produced by an alternative donor site !1within exon 1 REFERENCE A93393 !$#authors Grima, B.; Lamouroux, A.; Boni, C.; Julien, J.F.; !1Javoy-Agid, F.; Mallet, J. !$#journal Nature (1987) 326:707-711 !$#title A single human gene encoding multiple tyrosine hydroxylases !1with different predicted functional characteristics. !$#cross-references MUID:87173064; PMID:2882428 !$#accession A27791 !'##molecule_type mRNA !'##residues 1-30,62-528 ##label GRI1 !'##cross-references GB:X05290; NID:g32501; PIDN:CAA28908.1; PID:g32502 !'##experimental_source splice form 1 !'##note this splice form is produced by an alternative donor site !1within exon 1 !$#accession B27791 !'##molecule_type mRNA !'##residues 1-34,62-528 ##label GRI2 !'##cross-references GB:X05290; NID:g32501 !'##experimental_source splice form 2 !$#accession C27791 !'##molecule_type mRNA !'##residues 30,35-528 ##label GRI3 !'##cross-references GB:X05290; NID:g32501 !'##experimental_source splice form 3 !'##note this isozyme is produced by use of an alternative donor site !1within exon 1 REFERENCE PN0575 !$#authors Ichinose, H.; Ohye, T.; Fujita, K.; Yoshida, M.; Ueda, S.; !1Nagatsu, T. !$#journal Biochem. Biophys. Res. Commun. (1993) 195:158-165 !$#title Increased heterogeneity of tyrosine hydroxylase in humans. !$#cross-references MUID:93371398; PMID:7689834 !$#accession PN0575 !'##status translation not shown !'##molecule_type DNA !'##residues 19-30 ##label ICH1 !$#accession PN0582 !'##status translation not shown !'##molecule_type DNA !'##residues 35-61 ##label ICH2 !$#accession PN0588 !'##status translation not shown !'##molecule_type DNA !'##residues 62-106 ##label ICH3 REFERENCE I52396 !$#authors O'Malley, K.L.; Anhalt, M.J.; Martin, B.M.; Kelsoe, J.R.; !1Winfield, S.L.; Ginns, E.I. !$#journal Biochemistry (1987) 26:2910-2914 !$#title Isolation and characterization of the human tyrosine !1hydroxylase gene: identification of 5' alternative splice !1sites responsible for multiple mRNAs. !$#cross-references MUID:88107612; PMID:2892528 !$#accession I52396 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-61 ##label OMA !'##cross-references GB:M18116; NID:g339633; PIDN:AAA77649.1; !1PID:g1004335 REFERENCE I38340 !$#authors Kobayashi, K.; Kaneda, N.; Ichinose, H.; Kishi, F.; !1Nakazawa, A.; Kurosawa, Y.; Fujita, K.; Nagatsu, T. !$#journal Nucleic Acids Res. (1987) 15:6733 !$#title Isolation of a full-length cDNA clone encoding human !1tyrosine hydroxylase type 3. !$#cross-references MUID:87316931; PMID:2888085 !$#accession I38340 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-30,35-528 ##label KOB4 !'##cross-references EMBL:Y00414; NID:g37126; PIDN:CAA68472.1; !1PID:g37127 REFERENCE I55282 !$#authors Ginns, E.I.; Rehavi, M.; Martin, B.M.; Weller, M.; O'Malley, !1K.L.; LaMarca, M.E.; McAllister, C.G.; Paul, S.M. !$#journal J. Biol. Chem. (1988) 263:7406-7410 !$#title Expression of human tyrosine hydroxylase cDNA in !1invertebrate cells using a baculovirus vector. !$#cross-references MUID:88213428; PMID:2896667 !$#accession I55282 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-30,62-64 ##label GIN1 !'##cross-references GB:M20911; NID:g339636; PIDN:AAA61167.1; !1PID:g339637 !$#accession I70056 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-34,62-64 ##label GIN2 !'##cross-references GB:M20912; NID:g339642; PIDN:AAA61168.1; !1PID:g339643 COMMENT The expression of the four distinct proteins produced by !1alternate splicing varies in different parts of the nervous !1system. GENETICS !$#gene GDB:TH !'##cross-references GDB:119612; OMIM:191290 !$#map_position 11p15.5-11p15.5 !$#introns 34/3; 61/3; 135/3 !$#note the list of introns is incomplete FUNCTION !$#description catalyzes the 3'-hydroxylation of tyrosine to 3', !14'-dihydroxyphenylalanine by tetrahydrobiopterin and oxygen !$#pathway catecholamine biosynthesis !$#note this is the rate-limiting step in catecholamine biosynthesis CLASSIFICATION #superfamily phenylalanine 4-monooxygenase KEYWORDS alternative splicing; biopterin; catecholamine biosynthesis; !1iron; metalloprotein; monooxygenase; oxidoreductase; !1phosphoprotein FEATURE !$1-528 #product tyrosine 3-monooxygenase, splice form 4 !8#status predicted #label MAT4\ !$1-34,62-528 #product tyrosine 3-monooxygenase, splice form 2 !8#status predicted #label MAT2\ !$1-30,35-528 #product tyrosine 3-monooxygenase, splice form 3 !8#status predicted #label MAT3\ !$1-30,62-528 #product tyrosine 3-monooxygenase, splice form 1 !8#status predicted #label MAT1\ !$8 #binding_site phosphate (Thr) (covalent) (by !8unidentified kinase) #status predicted\ !$19 #binding_site phosphate (Ser) (covalent) (by !8calmodulin-dependent kinase) #status predicted\ !$71,183 #binding_site phosphate (Ser) (covalent) (by !8cAMP-dependent kinase) #status predicted\ !$361,366,406 #binding_site iron (His, His, Glu) #status predicted SUMMARY #length 528 #molecular-weight 58523 #checksum 9742 SEQUENCE /// ENTRY WHRTY #type complete TITLE tyrosine 3-monooxygenase (EC 1.14.16.2) - rat ALTERNATE_NAMES tyrosine 3-hydroxylase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 03-Mar-2000 ACCESSIONS A00510; A44714; S03026; I58264 REFERENCE A00510 !$#authors Grima, B.; Lamouroux, A.; Blanot, F.; Faucon Biguet, N.; !1Mallet, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:617-621 !$#title Complete coding sequence of rat tyrosine hydroxylase mRNA. !$#cross-references MUID:85113249; PMID:2857492 !$#accession A00510 !'##molecule_type mRNA !'##residues 1-498 ##label GRI !'##cross-references GB:M10244; NID:g207408; PIDN:AAA42257.1; !1PID:g207409 REFERENCE A44714 !$#authors Campbell, D.G.; Hardie, D.G.; Vulliet, P.R. !$#journal J. Biol. Chem. (1986) 261:10489-10492 !$#title Identification of four phosphorylation sites in the !1N-terminal region of tyrosine hydroxylase. !$#cross-references MUID:86278113; PMID:2874140 !$#accession A44714 !'##status preliminary !'##molecule_type protein !'##residues 2-12;16-24;38-47;151-157 ##label CAM REFERENCE S03026 !$#authors Bonnefoy, E.; Ferrara, P.; Rohrer, H.; Gros, F.; Thibault, !1J. !$#journal Eur. J. Biochem. (1988) 174:685-690 !$#title Role of the N-terminus of rat pheochromocytoma tyrosine !1hydroxylase in the regulation of the enzyme's activity. !$#cross-references MUID:88271342; PMID:2899026 !$#accession S03026 !'##molecule_type protein !'##residues 2-26 ##label BON REFERENCE I58264 !$#authors Harrington, C.A.; Lewis, E.J.; Krzemien, D.; Chikaraishi, !1D.M. !$#journal Nucleic Acids Res. (1987) 15:2363-2384 !$#title Identification and cell type specificity of the tyrosine !1hydroxylase gene promoter. !$#cross-references MUID:87174758; PMID:2882469 !$#accession I58264 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-30 ##label RES !'##cross-references EMBL:X04914; NID:g57355; PIDN:CAA28584.1; !1PID:g57356 FUNCTION !$#description catalyzes the 3'-hydroxylation of tyrosine to 3', !14'-dihydroxyphenylalanine by tetrahydrobiopterin and oxygen !$#pathway catecholamine biosynthesis !$#note this is the rate-limiting step in catecholamine biosynthesis CLASSIFICATION #superfamily phenylalanine 4-monooxygenase KEYWORDS biopterin; catecholamine biosynthesis; iron; metalloprotein; !1monooxygenase; oxidoreductase; phosphoprotein FEATURE !$8 #binding_site phosphate (Ser) (covalent) (by !8unidentified kinase) #status experimental\ !$19 #binding_site phosphate (Ser) (covalent) (by !8calmodulin-dependent kinase) #status experimental\ !$40,153 #binding_site phosphate (Ser) (covalent) (by !8cAMP-dependent kinase) #status experimental\ !$331,336,376 #binding_site iron (His, His, Glu) #status predicted SUMMARY #length 498 #molecular-weight 55965 #checksum 41 SEQUENCE /// ENTRY A55369 #type complete TITLE tyrosine 3-monooxygenase (EC 1.14.16.2), major splice form - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES tyrosine 3-hydroxylase, type I; tyrosine 3-hydroxylase, type II CONTAINS tyrosine 3-monooxygenase, minor splice form ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A55369; B55369; JN0010 REFERENCE A55369 !$#authors Birman, S.; Morgan, B.; Anzivino, M.; Hirsh, J. !$#journal J. Biol. Chem. (1994) 269:26559-26567 !$#title A novel and major isoform of tyrosine hydroxylase in !1Drosophila is generated by alternative RNA processing. !$#cross-references MUID:95014502; PMID:7929381 !$#accession A55369 !'##status preliminary !'##molecule_type DNA !'##residues 1-579 ##label BIR1 !'##cross-references GB:U14395; NID:g595799; PIDN:AAA62876.1; !1PID:g595800 !'##note authors translated the codon CGC for residue 219 as Ser, and !1TCC for residue 220 as Arg !$#accession B55369 !'##status preliminary !'##molecule_type DNA !'##residues 1-61,133-579 ##label BIR2 !'##cross-references GB:U14395; NID:g595799; PIDN:AAA62877.1; !1PID:g595801 !'##note authors translated the codon CGC for residue 219 as Ser, and !1TCC for residue 220 as Arg REFERENCE JN0010 !$#authors Neckameyer, W.S.; Quinn, W.G. !$#journal Neuron (1989) 2:1167-1175 !$#title Isolation and characterization of the gene for drosophila !1tyrosine hydroxylase. !$#cross-references MUID:90166583; PMID:2483109 !$#accession JN0010 !'##molecule_type mRNA !'##residues 1-61,133-579 ##label NEC !'##cross-references GB:X76209; NID:g433469; PIDN:CAA53802.1; !1PID:g433470 GENETICS !$#gene FlyBase:ple !'##cross-references FlyBase:FBgn0005626 !$#map_position 3L 65B !$#introns 23/3; 61/1; 101/1; 132/1; 405/2; 447/3 CLASSIFICATION #superfamily phenylalanine 4-monooxygenase KEYWORDS alternative splicing; biopterin; iron; metalloprotein; !1oxidoreductase FEATURE !$409,414,454 #binding_site iron (His, His, Glu) #status predicted SUMMARY #length 579 #molecular-weight 65995 #checksum 5798 SEQUENCE /// ENTRY E69997 #type complete TITLE nitrilotriacetate monooxygenase (EC 1.14.13.-) component A homolog ytnJ - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS E69997 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69997 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-442 ##label KUN !'##cross-references GB:Z99118; GB:Z99119; GB:AL009126; NID:g2635411; !1PIDN:CAB14909.1; PID:g2635415; NID:g2635200; PID:g2635396 !'##experimental_source strain 168 GENETICS !$#gene ytnJ CLASSIFICATION #superfamily nitrilotriacetate monooxygenase KEYWORDS oxidoreductase SUMMARY #length 442 #molecular-weight 49411 #checksum 4996 SEQUENCE /// ENTRY E70075 #type complete TITLE nitrilotriacetate monooxygenase (EC 1.14.13.-) component A homolog yxeK - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS E70075 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E70075 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-441 ##label KUN !'##cross-references GB:Z99124; GB:AL009126; NID:g2636442; !1PIDN:CAB15988.1; PID:g2636498 !'##experimental_source strain 168 GENETICS !$#gene yxeK CLASSIFICATION #superfamily nitrilotriacetate monooxygenase KEYWORDS oxidoreductase SUMMARY #length 441 #molecular-weight 49339 #checksum 8696 SEQUENCE /// ENTRY I40750 #type complete TITLE nitrilotriacetate monooxygenase (EC 1.14.13.-) component A - Chelatobacter heintzii ALTERNATE_NAMES NTA monooxygenase component A ORGANISM #formal_name Chelatobacter heintzii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS I40750 REFERENCE I40749 !$#authors Uetz, T.; Schneider, R.; Snozzi, M.; Egli, T. !$#journal J. Bacteriol. (1992) 174:1179-1188 !$#title Purification and characterization of a two-component !1monooxygenase that hydroxylates nitrilotriacetate from !1'Chelatobacter' strain ATCC 29600. !$#cross-references MUID:92138609; PMID:1735711 !$#accession I40750 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-453 ##label RES !'##cross-references EMBL:U39411; NID:g1066333; PID:g1066335 GENETICS !$#gene ntaA CLASSIFICATION #superfamily nitrilotriacetate monooxygenase KEYWORDS oxidoreductase SUMMARY #length 453 #molecular-weight 50525 #checksum 1523 SEQUENCE /// ENTRY URXLA1 #type complete TITLE peptidylglycine monooxygenase (EC 1.14.17.3) I precursor - African clawed frog ALTERNATE_NAMES C-terminal alpha-amidating enzyme AE-I; peptidyl alpha-amidating enzyme I; peptidylglycine 2-hydroxylase I ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 23-Jul-1999 ACCESSIONS A29726; S54374 REFERENCE A29726 !$#authors Mizuno, K.; Ohsuye, K.; Wada, Y.; Fuchimura, K.; Tanaka, S.; !1Matsuo, H. !$#journal Biochem. Biophys. Res. Commun. (1987) 148:546-552 !$#title Cloning and sequence of cDNA encoding a peptide C-terminal !1alpha-amidating enzyme from Xenopus laevis. !$#cross-references MUID:88076923; PMID:3689360 !$#accession A29726 !'##molecule_type mRNA !'##residues 1-400 ##label MIZ !'##cross-references GB:M33461 !'##experimental_source skin !$#accession S54374 !'##molecule_type protein !'##residues 38-51;82-96;146-153;174-178;189-193;237-250;256-288;359-381 !1##label MIW !'##experimental_source skin FUNCTION !$#description catalyzes oxidation of peptidylglycine to the corresponding !1peptidyl(2-hydroxyglycine) in the presence of ascorbate; the !1product is unstable and dismutates to glyoxylate and the !1corresponding desglycine peptide alpha-amide !$#note C-terminal alpha-amide structure is essential for the !1biological activity of many peptide hormones CLASSIFICATION #superfamily peptidylglycine monooxygenase I; !1peptidylglycine monooxygenase I homology KEYWORDS copper; monooxygenase; oxidoreductase FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-37 #domain propeptide #status predicted #label PRO\ !$38-381 #product peptidylglycine monooxygenase I #status !8experimental #label MAT\ !$131-342 #domain peptidylglycine monooxygenase I homology !8#label PGM\ !$382-400 #domain carboxyl-terminal propeptide #status !8predicted #label CTP SUMMARY #length 400 #molecular-weight 44456 #checksum 8024 SEQUENCE /// ENTRY URHUAP #type complete TITLE peptidylglycine monooxygenase (EC 1.14.17.3) / peptidylamidoglycolate lyase (EC 4.3.2.5) precursor - human ALTERNATE_NAMES C-terminal alpha-amidating enzyme; peptidyl alpha-amidating enzyme; peptidylglycine 2-hydroxylase CONTAINS peptidyl-alpha hydroxyglycine alpha-amidating lyase; peptidylglycine alpha-amidating monoxygenase PAM15; peptidylglycine alpha-hydroxylating monoxygenase ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 11-Jun-1999 ACCESSIONS A35477; JC2418 REFERENCE A35477 !$#authors Glauder, J.; Ragg, H.; Rauch, J.; Engels, J.W. !$#journal Biochem. Biophys. Res. Commun. (1990) 169:551-558 !$#title Human peptidylglycine alpha-amidating monooxygenase: cDNA, !1cloning and functional expression of a truncated form in cos !1cells. !$#cross-references MUID:90290494; PMID:2357221 !$#accession A35477 !'##molecule_type mRNA !'##residues 1-974 ##label GLA !'##cross-references GB:M37721; NID:g189594; PIDN:AAA36414.1; !1PID:g189595 REFERENCE JC2418 !$#authors Tateishi, K.; Arakawa, F.; Misumi, Y.; Treston, A.M.; Vos, !1M.; Matsuoka, Y. !$#journal Biochem. Biophys. Res. Commun. (1994) 205:282-290 !$#title Isolation and functional expression of human pancreatic !1peptidylglycine alpha-amidating monooxygenase. !$#cross-references MUID:95091738; PMID:7999037 !$#accession JC2418 !'##molecule_type mRNA !'##residues 1-573,'G',575-828,830-896,898-974 ##label TAT GENETICS !$#gene GDB:PAM !'##cross-references GDB:128628; OMIM:170270 !$#map_position 5q15-5q21 CLASSIFICATION #superfamily peptidylglycine monooxygenase II; !1peptidylglycine monooxygenase I homology KEYWORDS alternative splicing; amidine-lyase; carbon-nitrogen lyase; !1copper; glycoprotein; monooxygenase; multifunctional enzyme; !1oxidoreductase; transmembrane protein FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-30 #domain propeptide #status predicted #label PRO\ !$31-974 #product peptidylglycine monooxygenase #status !8predicted #label PAM\ !$130-341 #domain peptidylglycine monooxygenase I homology !8#label PGM\ !$864-887 #domain transmembrane #status predicted #label TMM\ !$762 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 974 #molecular-weight 108474 #checksum 5244 SEQUENCE /// ENTRY URBOAP #type complete TITLE peptidylglycine monooxygenase (EC 1.14.17.3) / peptidylamidoglycolate lyase (EC 4.3.2.5) precursor - bovine ALTERNATE_NAMES C-terminal alpha-amidating enzyme; peptidyl alpha-amidating enzyme; peptidylglycine 2-hydroxylase CONTAINS peptidylamidoglycolate lyase (EC 4.3.2.5); peptidylglycine monooxygenase (EC 1.14.17.3) ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 11-Jun-1999 ACCESSIONS A40063; B40063; A39571 REFERENCE A40063 !$#authors Eipper, B.A.; Park, L.P.; Dickerson, I.M.; Keutmann, H.T.; !1Thiele, E.A.; Rodriguez, H.; Schofield, P.R.; Mains, R.E. !$#journal Mol. Endocrinol. (1987) 1:777-790 !$#title Structure of the precursor to an enzyme mediating !1COOH-terminal amidation in peptide biosynthesis. !$#cross-references MUID:91042563; PMID:3153462 !$#accession A40063 !'##molecule_type mRNA !'##residues 1-972 ##label EIP !'##cross-references GB:M18683; NID:g163481; PIDN:AAA30683.1; !1PID:g163482 !$#accession B40063 !'##molecule_type protein !'##residues 31-45;37-53;64-76;84-97;202-228;230-258;319-339 ##label EI2 !'##experimental_source pituitary REFERENCE A39571 !$#authors Katopodis, A.G.; Ping, D.; Smith, C.E.; May, S.W. !$#journal Biochemistry (1991) 30:6189-6194 !$#title Functional and structural characterization of !1peptidylamidoglycolate lyase, the enzyme catalyzing the !1second step in peptide amidation. !$#cross-references MUID:91283459; PMID:2059626 !$#accession A39571 !'##molecule_type protein !'##residues 478-499;544-575;611-630;665-695 ##label KAT CLASSIFICATION #superfamily peptidylglycine monooxygenase II; !1peptidylglycine monooxygenase I homology KEYWORDS amidine-lyase; carbon-nitrogen lyase; copper; glycoprotein; !1monooxygenase; multifunctional enzyme; oxidoreductase; !1transmembrane protein FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-30 #domain propeptide #status predicted #label PRO\ !$31-477 #product peptidylglycine monooxygenase 1 #status !8predicted #label PAM\ !$130-341 #domain peptidylglycine monooxygenase I homology !8#label PGM\ !$478-972 #product peptidylamidoglycolate lyase #status !8predicted #label PGL\ !$859-888 #domain transmembrane #status predicted #label TMN\ !$762 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 972 #molecular-weight 108176 #checksum 5240 SEQUENCE /// ENTRY URRTAP #type complete TITLE peptidylglycine monooxygenase (EC 1.14.17.3) precursor - rat ALTERNATE_NAMES C-terminal alpha-amidating enzyme; peptidyl alpha-amidating enzyme; peptidylglycine 2-hydroxylase CONTAINS peptidylamidoglycolate lyase (EC 4.3.2.5) (peptidyl-alpha-hydroxyglycine alpha-amidating lyase, PAL) ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 11-Jun-1999 ACCESSIONS A32193; B32193; S11333; S09582; B46679; A46679; S11334; !1S11335; S11336; S11337 REFERENCE A32193 !$#authors Stoffers, D.A.; Green, C.B.R.; Eipper, B.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:735-739 !$#title Alternative mRNA splicing generates multiple forms of !1peptidyl-glycine alpha-amidating monooxygenase in rat !1atrium. !$#cross-references MUID:89099006; PMID:2911604 !$#accession A32193 !'##molecule_type mRNA !'##residues 1-976 ##label STO !'##cross-references GB:M25732; NID:g206022; PIDN:AAA41803.1; !1PID:g206023 !$#accession B32193 !'##molecule_type mRNA !'##residues 1-392,498-976 ##label ST2 !'##cross-references GB:M25719; NID:g206024; PIDN:AAA41804.1; !1PID:g206025 !'##experimental_source atrium REFERENCE S11333 !$#authors Kato, I.; Yonekura, H.; Yamamoto, H.; Okamoto, H. !$#journal FEBS Lett. (1990) 269:319-323 !$#title Isolation and functional expression of pituitary !1peptidylglycine alpha-amidating enzyme mRNA. A variant !1lacking the transmembrane domain. !$#cross-references MUID:90382572; PMID:2401356 !$#accession S11333 !'##molecule_type mRNA !'##residues 1-958,'S',960-976 ##label KAT !'##cross-references GB:X59688; GB:X55770; NID:g56842 !'##experimental_source pituitary REFERENCE S09582 !$#authors Bertelsen, A.H.; Beaudry, G.A.; Galella, E.A.; Jones, B.N.; !1Ray, M.L.; Mehta, N.M. !$#journal Arch. Biochem. Biophys. (1990) 279:87-96 !$#title Cloning and characterization of two alternatively spliced !1rat alpha-amidating enzyme cDNAs from rat medullary thyroid !1carcinoma. !$#cross-references MUID:90247899; PMID:2337358 !$#accession S09582 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-393,499-831,833-886,918-958,'S',960-976 ##label BER !'##cross-references GB:U52650; GB:L01679; NID:g2934921; GB:U52653; !1GB:L01682; NID:g2934924; GB:U52664; GB:L01693; NID:g2934935 REFERENCE A46679 !$#authors Husten, E.J.; Tausk, F.A.; Keutmann, H.T.; Eipper, B.A. !$#journal J. Biol. Chem. (1993) 268:9709-9717 !$#title Use of endoproteases to identify catalytic domains, linker !1regions, and functional interactions in soluble !1peptidylglycine alpha-amidating monooxygenase. !$#cross-references MUID:93252847; PMID:8486658 !$#accession B46679 !'##molecule_type protein !'##residues 26-55 ##label HUS !'##experimental_source rat clone expressed in human embryonic kidney !1cell line hEK-293 !'##note sequence extracted from NCBI backbone (NCBIP:133913) !$#accession A46679 !'##molecule_type protein !'##residues 376-392,498-504 ##label HU2 !'##experimental_source rat clone expressed in embryonic kidney cell !1line hEK-293 !'##note sequence extracted from NCBI backbone (NCBIP:133914) CLASSIFICATION #superfamily peptidylglycine monooxygenase II; !1peptidylglycine monooxygenase I homology KEYWORDS alternative splicing; amidine-lyase; carbon-nitrogen lyase; !1copper; glycoprotein; monooxygenase; multifunctional enzyme; !1oxidoreductase; phosphoprotein; transmembrane protein FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-35 #domain propeptide #status predicted #label PRO\ !$36-976 #product peptidylglycine monooxygenase 1 #status !8experimental #label PAM1\ !$36-900,918-976 #product peptidylglycine monooxygenase 4 #status !8experimental #label PAM4\ !$36-831,900-976 #product peptidylglycine monooxygenase 3 #status !8experimental #label PAM3\ !$36-392,498-899, !$918-976 #product peptidylglycine monooxygenase 5 #status !8experimental #label PAM5\ !$36-392,498-976 #product peptidylglycine monooxygenase 2 #status !8experimental #label PAM2\ !$135-346 #domain peptidylglycine monooxygenase I homology !8#label PGM\ !$863-891 #domain transmembrane #status predicted #label TMN\ !$47-186,81-126, !$114-131,227-334, !$293-315 #disulfide_bonds #status experimental\ !$79,313,318 #active_site Tyr, Glu, Tyr #status predicted\ !$107,108,172 #binding_site copper 1 (His) #status predicted\ !$242,244,314 #binding_site copper 2 (His, His, Met) #status !8predicted\ !$765 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 976 #molecular-weight 108674 #checksum 7129 SEQUENCE /// ENTRY URXLA2 #type complete TITLE peptidylglycine monooxygenase (EC 1.14.17.3) II precursor - African clawed frog ALTERNATE_NAMES C-terminal alpha-amidating enzyme II (AE-II); peptidyl alpha-amidating enzyme II; peptidylglycine 2-hydroxylase II ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 13-Jun-1997 ACCESSIONS A27715 REFERENCE A27715 !$#authors Ohsuye, K.; Kitano, K.; Wada, Y.; Fuchimura, K.; Tanaka, S.; !1Mizuno, K.; Matsuo, H. !$#journal Biochem. Biophys. Res. Commun. (1988) 150:1275-1281 !$#title Cloning of cDNA encoding a new peptide C-terminal !1alpha-amidating enzyme having a putative membrane-spanning !1domain from Xenopus laevis skin. !$#cross-references MUID:88134244; PMID:2829895 !$#accession A27715 !'##molecule_type mRNA !'##residues 1-875 ##label OHS !'##cross-references GB:M20191 !'##experimental_source skin COMMENT This copper protein is one of two enzymes that catalyze the !1oxidation of peptidylglycine to the corresponding peptidyl !1(2-hydroxyglycine) in the presence of ascorbate; the product !1is unstable and dismutates to glyoxylate and the !1corresponding desglycine peptide alpha-amide. The presence !1of such a C-terminal alpha-amide structure is essential for !1the biological activity of many peptide hormones. The other !1enzyme is peptidyl alpha-amidating enzyme I. CLASSIFICATION #superfamily peptidylglycine monooxygenase II; !1peptidylglycine monooxygenase I homology KEYWORDS copper; glycoprotein; monooxygenase; oxidoreductase; !1transmembrane protein FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$24-39 #domain propeptide #status predicted #label PRO\ !$40-385 #product peptidylglycine monooxygenase II #status !8predicted #label MAT\ !$133-344 #domain peptidylglycine monooxygenase I homology !8#label PGM\ !$764-787 #domain transmembrane #status predicted #label TMN\ !$465,662,743 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 875 #molecular-weight 97084 #checksum 94 SEQUENCE /// ENTRY YRNC #type complete TITLE monophenol monooxygenase (EC 1.14.18.1) precursor - Neurospora crassa ALTERNATE_NAMES tyrosinase ORGANISM #formal_name Neurospora crassa DATE 28-Feb-1980 #sequence_revision 10-Oct-1997 #text_change 11-Jun-1999 ACCESSIONS A34460; A92374; A92375; B92375; A00511 REFERENCE A34460 !$#authors Kupper, U.; Niedermann, D.M.; Travaglini, G.; Lerch, K. !$#journal J. Biol. Chem. (1989) 264:17250-17258 !$#title Isolation and characterization of the tyrosinase gene from !1Neurospora crassa. !$#cross-references MUID:90008884; PMID:2529259 !$#accession A34460 !'##molecule_type DNA !'##residues 1-621 ##label KUP !'##cross-references GB:M33271; NID:g168919; PIDN:AAA33618.1; !1PID:g168920; GB:J05052 !'##note the larger precursor form was demonstrated by Western transfer !1from crude cellular extracts and by in vitro translation REFERENCE A92374 !$#authors Lerch, K. !$#journal J. Biol. Chem. (1982) 257:6414-6419 !$#title Primary structure of tyrosinase from Neurospora crassa. II. !1Complete amino acid sequence and chemical structure of a !1tripeptide containing an unusual thioether. !$#cross-references MUID:82190018; PMID:6210696 !$#accession A92374 !'##molecule_type protein !'##residues 2-201,'N',203-234,'D',236-408 ##label LER !'##experimental_source strain TL REFERENCE A92375 !$#authors Ruegg, C.; Ammer, D.; Lerch, K. !$#journal J. Biol. Chem. (1982) 257:6420-6426 !$#title Comparison of amino acid sequence and thermostability of !1tyrosinase from three wild type strains of Neurospora !1crassa. !$#cross-references MUID:82190019; PMID:6210697 !$#accession A92375 !'##molecule_type protein !'##residues 2-234,'D',236-408 ##label RUE !'##experimental_source strain TS !$#accession B92375 !'##molecule_type protein !'##residues 2-29,'E',31-129,'T',131-234,'D',236-345,'QN',348-370,'T', !1372-408 ##label RU2 !'##experimental_source strain Sing COMMENT This enzyme is a copper-containing oxidase that functions in !1the formation of pigments such as melanins and other !1polyphenolic compounds. GENETICS !$#gene 20/1; 308/2 CLASSIFICATION #superfamily Neurospora monophenol monooxygenase KEYWORDS acetylated amino end; oxidoreductase FEATURE !$2-408 #product monophenol monooxygenase #status !8experimental #label MAT\ !$409-621 #domain carboxyl-terminal propeptide #status !8predicted #label CPRO\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental\ !$95-97 #cross-link cysteinylhistidine (Cys-His) #status !8experimental\ !$189,194,290,307 #binding_site copper (His) #status predicted SUMMARY #length 621 #molecular-weight 68691 #checksum 1274 SEQUENCE /// ENTRY YRHUB6 #type complete TITLE tyrosinase-related protein 1 precursor - human ALTERNATE_NAMES brown locus protein homolog; CAS2 protein; melanoma antigen gp75; monophenol monooxygenase homolog; protein TRP-1 ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1989 #sequence_revision 17-May-1996 #text_change 11-Jun-1999 ACCESSIONS S09999; JN0077; A60930; S22565; S16036 REFERENCE S09999 !$#authors Cohen, T.; Muller, R.M.; Tomita, Y.; Shibahara, S. !$#journal Nucleic Acids Res. (1990) 18:2807-2808 !$#title Nucleotide sequence of the cDNA encoding human !1tyrosinase-related protein. !$#cross-references MUID:90251459; PMID:2111010 !$#accession S09999 !'##molecule_type mRNA !'##residues 1-525,'RI' ##label COH !'##cross-references EMBL:X51420; NID:g37512; PIDN:CAA35785.1; !1PID:g37513 REFERENCE JN0077 !$#authors Chintamaneni, C.D.; Ramsay, M.; Colman, M.A.; Fox, M.F.; !1Pickard, R.T.; Kwon, B.S. !$#journal Biochem. Biophys. Res. Commun. (1991) 178:227-235 !$#title Mapping the human CAS2 gene, the homologue of the mouse !1brown (b) locus, to human chromosome 9p22-pter. !$#cross-references MUID:91298952; PMID:1906272 !$#accession JN0077 !'##molecule_type mRNA !'##residues 25-525,'RI' ##label CHI REFERENCE A60930 !$#authors Vijayasaradhi, S.; Bouchard, B.; Houghton, A.N. !$#journal J. Exp. Med. (1990) 171:1375-1380 !$#title The melanoma antigen gp75 is the human homologue of the !1mouse b (brown) locus gene product. !$#cross-references MUID:90217958; PMID:2324688 !$#accession A60930 !'##molecule_type protein !'##residues 271-284;357-373;452-465 ##label VIJ REFERENCE S22565 !$#authors Urquhart, A. !$#journal Nucleic Acids Res. (1991) 19:5803 !$#title Human tyrosinase-like protein (TYRL) carboxy terminus: !1closer homology with the mouse protein than previously !1reported. !$#cross-references MUID:92051358; PMID:1945866 !$#contents correction to S09999 !$#accession S22565 !'##molecule_type DNA !'##residues 521-537 ##label URQ2 !'##cross-references EMBL:X60955; NID:g37516; PIDN:CAA43288.1; !1PID:g37517 REFERENCE S16036 !$#authors Urquhart, A.J. !$#submission submitted to the EMBL Data Library, July 1991 !$#accession S16036 !'##molecule_type DNA !'##residues 481-537 ##label URQ1 !'##cross-references EMBL:X60955; NID:g37516; PIDN:CAA43288.1; !1PID:g37517 GENETICS !$#gene GDB:TYRP1; CAS2; TYRP !'##cross-references GDB:126337; OMIM:115501 !$#map_position 9p23-9p23 CLASSIFICATION #superfamily monophenol monooxygenase KEYWORDS copper; glycoprotein; transmembrane protein FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-537 #product tyrosinase-related protein 1 #status !8predicted #label MAT\ !$478-501 #domain transmembrane #status predicted #label TRA\ !$96,104,181,304,350, !$385 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$192,215,224,227 #binding_site copper (His) #status predicted\ !$377,381,404,434 #binding_site copper (His) #status predicted SUMMARY #length 537 #molecular-weight 60724 #checksum 509 SEQUENCE /// ENTRY YRMSB6 #type complete TITLE tyrosinase-related protein precursor - mouse ALTERNATE_NAMES brown (b) locus protein; monophenol monooxygenase homolog ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 11-Jun-1999 ACCESSIONS A24933 REFERENCE A24933 !$#authors Shibahara, S.; Tomita, Y.; Sakakura, T.; Nager, C.; !1Chaudhuri, B.; Muller, R. !$#journal Nucleic Acids Res. (1986) 14:2413-2427 !$#title Cloning and expression of cDNA encoding mouse tyrosinase. !$#cross-references MUID:86176740; PMID:3008090 !$#accession A24933 !'##molecule_type mRNA !'##residues 1-537 ##label SHI !'##cross-references GB:X03687; NID:g55067; PIDN:CAA27323.1; PID:g55068 !'##experimental_source strain B16 !'##note the authors have studied the function of this protein further !1since publication of this paper and have shown it to lack !1tyrosinase activity; see entry JN0077 for the homologous !1protein in man COMMENT This protein corresponds to the brown (b) locus that !1determines the type of melanin produced. Mutation leads to a !1brown or hypopigmented coat rather than to an absence of !1pigment. CLASSIFICATION #superfamily monophenol monooxygenase KEYWORDS copper; glycoprotein; transmembrane protein FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-537 #product tyrosinase-related protein #status predicted !8#label MAT\ !$478-501 #domain transmembrane #status predicted #label TRA\ !$104,181,304,350, !$385,533 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$192,215,224,227 #binding_site copper (His) #status predicted\ !$377,381,404,434 #binding_site copper (His) #status predicted SUMMARY #length 537 #molecular-weight 60761 #checksum 1892 SEQUENCE /// ENTRY S19243 #type complete TITLE tyrosinase-related protein TRP-2 [similarity] - mouse ALTERNATE_NAMES DOPAchrome tautomerase ORGANISM #formal_name Mus musculus #common_name house mouse DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS S19243; S55476 REFERENCE S19243 !$#authors Jackson, I.J.; Chambers, D.M.; Tsukamoto, K.; Copeland, !1N.G.; Gilbert, D.J.; Jenkins, N.A.; Hearing, V. !$#journal EMBO J. (1992) 11:527-535 !$#title A second tyrosinase-related protein, TRP-2, maps to and is !1mutated at the mouse slaty locus. !$#cross-references MUID:92164640; PMID:1537334 !$#accession S19243 !'##molecule_type mRNA !'##residues 1-517 ##label JAC !'##cross-references EMBL:X63349; NID:g55065; PIDN:CAA44951.1; !1PID:g55066 REFERENCE S55476 !$#authors Budd, P.S. !$#submission submitted to the EMBL Data Library, March 1995 !$#accession S55476 !'##molecule_type DNA !'##residues 1-98 ##label BUD !'##cross-references EMBL:X85126; NID:g854334; PIDN:CAA59440.1; !1PID:g854335 CLASSIFICATION #superfamily monophenol monooxygenase KEYWORDS transmembrane protein SUMMARY #length 517 #molecular-weight 58569 #checksum 6717 SEQUENCE /// ENTRY YRHU1 #type complete TITLE monophenol monooxygenase (EC 1.14.18.1) precursor [validated] - human ALTERNATE_NAMES cresolase; monophenol oxidase; phenolase; tyrosinase ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1990 #sequence_revision 31-Mar-1993 #text_change 08-Dec-2000 ACCESSIONS A38444; S07760; A33393; A38718; JL0098; A40957; S04760; !1A60149; B60149; S53560; A60464; S53559 REFERENCE A38444 !$#authors Giebel, L.B.; Strunk, K.M.; Spritz, R.A. !$#journal Genomics (1991) 9:435-445 !$#title Organization and nucleotide sequences of the human !1tyrosinase gene and a truncated tyrosinase-related segment. !$#cross-references MUID:91236163; PMID:1903356 !$#accession A38444 !'##molecule_type DNA !'##residues 1-529 ##label GIE !'##cross-references GB:M63239; GB:M60296; NID:g340033; PIDN:AAA61242.1; !1PID:g340035 REFERENCE S07760 !$#authors Kikuchi, H.; Miura, H.; Yamamoto, H.; Takeuchi, T.; Dei, T.; !1Watanabe, M. !$#journal Biochim. Biophys. Acta (1989) 1009:283-286 !$#title Characteristic sequences in the upstream region of the human !1tyrosinase gene. !$#cross-references MUID:90089403; PMID:2480811 !$#accession S07760 !'##molecule_type DNA !'##residues 1-273 ##label KIK !'##cross-references EMBL:X16073; NID:g37506; PIDN:CAA34205.1; !1PID:g37507 REFERENCE A33393 !$#authors Takeda, A.; Tomita, Y.; Okinaga, S.; Tagami, H.; Shibahara, !1S. !$#journal Biochem. Biophys. Res. Commun. (1989) 162:984-990 !$#title Functional analysis of the cDNA encoding human tyrosinase !1precursor. !$#cross-references MUID:89351001; PMID:2504160 !$#accession A33393 !'##molecule_type DNA !'##residues 1-32 ##label TAK !'##cross-references GB:M27160 REFERENCE A38718 !$#authors Giebel, L.B.; Tripathi, R.K.; Strunk, K.M.; Hanifin, J.M.; !1Jackson, C.E.; King, R.A.; Spritz, R.A. !$#journal Am. J. Hum. Genet. (1991) 48:1159-1167 !$#title Tyrosinase gene mutations associated with type IB ("yellow") !1oculocutaneous albinism. !$#cross-references MUID:91241133; PMID:1903591 !$#accession A38718 !'##molecule_type DNA !'##residues 274-280;401-411;500-509 ##label GI2 REFERENCE JL0098 !$#authors Bouchard, B.; Fuller, B.B.; Vijayasaradhi, S.; Houghton, !1A.N. !$#journal J. Exp. Med. (1989) 169:2029-2042 !$#title Induction of pigmentation in mouse fibroblasts by expression !1of human tyrosinase cDNA. !$#cross-references MUID:89279151; PMID:2499655 !$#accession JL0098 !'##molecule_type mRNA !'##residues 'GR',1-178,'I',180-191,'Y',193-529 ##label BOU !'##cross-references EMBL:Y00819; NID:g37508; PIDN:CAA68756.1; !1PID:g37509 REFERENCE A40957 !$#authors Chintamaneni, C.D.; Halaban, R.; Kobayashi, Y.; Witkop Jr., !1C.J.; Kwon, B.S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:5272-5276 !$#title A single base insertion in the putative transmembrane domain !1of the tyrosinase gene as a cause for tyrosinase-negative !1oculocutaneous albinism. !$#cross-references MUID:91271371; PMID:1711223 !$#accession A40957 !'##molecule_type mRNA !'##residues 1-165,'I',167-489,'CPAGRACELAVSSQEKAAS' ##label CHI !'##cross-references GB:M74314 !'##experimental_source albino melanocytes !'##note mutant protein isolated from patient with tyrosinase-negative !1oculocutaneous albinism REFERENCE A94185 !$#authors Kwon, B.S.; Haq, A.K.; Pomerantz, S.H.; Halaban, R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:7473-7477 !$#title Isolation and sequence of a cDNA clone for human tyrosinase !1that maps at the mouse c-albino locus. !$#cross-references MUID:88041128; PMID:2823263 !$#accession S04760 !'##molecule_type mRNA !'##residues 'L',2-41,'TGV',46-191,'Y',193-307,'T',309-372,'HVPGT', !1379-401,'Q',403-494,'P',496-519,'GLPQ',524, !1'VSEPFIKGLGNRVGPKSPDLTLTQSNVQVPENICWYFL' ##label KWO !'##cross-references GB:J03581; NID:g340027; PIDN:AAA61241.1; !1PID:g340028 !'##experimental_source normal melanocytes !'##note the sequence differs from that shown in several regions due to !1reading frameshifts, at a number of single residues, and in !1having a carboxyl-terminal extension of 33 residues REFERENCE A60149 !$#authors Wittbjer, A.; Odh, G.; Rosengren, A.M.; Rosengren, E.; !1Rorsman, H. !$#journal Acta Derm. Venereol. (1990) 70:291-294 !$#title Isolation of soluble tyrosinase from human melanoma cells. !$#cross-references MUID:91021767; PMID:1977251 !$#accession A60149 !'##molecule_type protein !'##residues 19-23,'X',25-28 ##label WIT !'##note the sequence was determined from a soluble form of the enzyme !1from melanoma cells !$#accession B60149 !'##molecule_type protein !'##residues 19-23,'X',25-34,'XX',37-38 ##label WIT2 !'##note the sequence was determined from a membrane-bound form of the !1enzyme from melanoma cells REFERENCE S53560 !$#authors Giebel, L.B.; Strunk, K.M.; Spritz, R.A. !$#submission submitted to the EMBL Data Library, July 1991 !$#description Organization and nucleotide sequences of the human !1tyrosinase gene and a truncated tyrosine-related segment. !$#accession S53560 !'##molecule_type DNA !'##residues 396-455 ##label GI3 !'##cross-references EMBL:M63238 REFERENCE A60464 !$#authors Wittbjer, A.; Dahlbaeck, B.; Odh, G.; Rosengren, A.M.; !1Rosengren, E.; Rorsman, H. !$#journal Acta Derm. Venereol. (1989) 69:125-131 !$#title Isolation of human tyrosinase from cultured melanoma cells. !$#cross-references MUID:89163645; PMID:2564229 !$#accession A60464 !'##molecule_type protein !'##residues 'L',2-13;19-23,'X',25-34,'XX',37-38 ##label WI2 REFERENCE S53559 !$#authors Guo, Z.; Guilfoyle, R.A.; Thiel, A.J.; Wang, R.; Smith, L.M. !$#journal Nucleic Acids Res. (1994) 22:5456-5465 !$#title Direct fluorescence analysis of genetic polymorphisms by !1hybridization with oligonucleotide arrays on glass supports. !$#cross-references MUID:95116340; PMID:7816638 !$#contents annotation COMMENT This cell-specific oxidase is a glycoprotein containing two !1Cu per enzyme; it catalyzes the oxidation of tyrosine to !1dihydroxyphenylalanine (dopa) and of dopa to dopaquinone, !1the first two reactions in the formation of pigments such as !1melanins and other polyphenolic compounds in melanocytes. GENETICS !$#gene GDB:TYR !'##cross-references GDB:120476; OMIM:203100 !$#map_position 11q21-11q21 !$#introns 273/3; 346/1; 395/2; 456/1 CLASSIFICATION #superfamily monophenol monooxygenase KEYWORDS albinism; copper; glycoprotein; melanin biosynthesis; !1monooxygenase; oxidoreductase; transmembrane protein FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-529 #product monophenol monooxygenase #status !8experimental #label MAT\ !$474-500 #domain transmembrane #status predicted #label TMM\ !$86,111,161,230,337, !$371 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$180,202,211 #binding_site copper (His) #status predicted\ !$363,367,390,420 #binding_site copper (His) #status predicted SUMMARY #length 529 #molecular-weight 60393 #checksum 3879 SEQUENCE /// ENTRY YRMSCS #type complete TITLE monophenol monooxygenase (EC 1.14.18.1) precursor [validated] - mouse ALTERNATE_NAMES cresolase; monophenol oxidase; phenolase; tyrosinase ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 20-Apr-2000 ACCESSIONS A27711; A60778; A32429; B32429; S01170; S02278; S15753; !1I49736 REFERENCE A27711 !$#authors Kwon, B.S.; Wakulchik, M.; Haq, A.K.; Halaban, R.; Kestler, !1D. !$#journal Biochem. Biophys. Res. Commun. (1988) 153:1301-1309 !$#title Sequence analysis of mouse tyrosinase cDNA and the effect of !1melanotropin on its gene expression. !$#cross-references MUID:88268910; PMID:3134020 !$#accession A27711 !'##molecule_type mRNA !'##residues 1-533 ##label KWO !'##cross-references GB:M20234; NID:g202247; PIDN:AAA40516.1; !1PID:g202248 !'##experimental_source Cloudman S-91 melanoma cells REFERENCE A60778 !$#authors Kwon, B.S.; Haq, A.K.; Wakulchik, M.; Kestler, D.; Barton, !1D.E.; Francke, U.; Lamoreux, M.L.; Whitney III, J.B.; !1Halaban, R. !$#journal J. Invest. Dermatol. (1989) 93:589-594 !$#title Isolation, chromosomal mapping, and expression of the mouse !1tyrosinase gene. !$#cross-references MUID:90010220; PMID:2507645 !$#accession A60778 !'##status translation not shown !'##molecule_type DNA !'##residues 1-273 ##label KW2 !'##experimental_source BALB/c REFERENCE A32429 !$#authors Terao, M.; Tabe, L.; Garattini, E.; Sartori, D.; Studer, M.; !1Mintz, B. !$#journal Biochem. Biophys. Res. Commun. (1989) 159:848-853 !$#title Isolation and characterization of variant cDNAs encoding !1mouse tyrosinase. !$#cross-references MUID:89193679; PMID:2494997 !$#accession A32429 !'##molecule_type mRNA !'##residues 1-102,'C',104-345,'G',347-533 ##label TER !'##cross-references GB:M24560; NID:g202249; PIDN:AAA40517.1; !1PID:g202250 !$#accession B32429 !'##molecule_type mRNA !'##residues 1-77;155-345,'G',347-533 ##label TE2 !'##cross-references GB:M24560 !'##experimental_source B16 melanoma cells REFERENCE S01170 !$#authors Mueller, G.; Ruppert, S.; Schmid, E.; Schuetz, G. !$#journal EMBO J. (1988) 7:2723-2730 !$#title Functional analysis of alternatively spliced tyrosinase gene !1transcripts. !$#cross-references MUID:89030636; PMID:3141148 !$#accession S01170 !'##molecule_type mRNA !'##residues 1-102,'C',104-263,'I',265-345,'G',347-533 ##label MUE !'##cross-references GB:X12782; NID:g55061; PIDN:CAA31273.1; PID:g55062 REFERENCE S02278 !$#authors Yamamoto, H.; Takeuchi, S.; Kudo, T.; Makino, K.; Nakata, !1A.; Shinoda, T.; Takeuchi, T. !$#journal Jpn. J. Genet. (1987) 62:271-274 !$#title Cloning and sequencing of mouse tyrosinase cDNA. !$#accession S02278 !'##molecule_type mRNA !'##residues 1-102,'C',104-263,'I',265-345,'G',347-448 ##label YAM !'##cross-references EMBL:X12782 !'##note part of this sequence was confirmed by protein sequencing REFERENCE S15753 !$#authors Shibahara, S.; Okinaga, S.; Tomita, Y.; Takeda, A.; !1Yamamoto, H.; Sato, M.; Takeuchi, T. !$#journal Eur. J. Biochem. (1990) 189:455-461 !$#title A point mutation in the tyrosinase gene of BALB/c albino !1mouse causing the cysteine -> serine substitution at !1position 85. !$#cross-references MUID:90249393; PMID:2110899 !$#accession S15753 !'##status translation not shown !'##molecule_type DNA !'##residues 1-13 ##label SHI !'##cross-references EMBL:X51743; NID:g55057; PIDN:CAA36033.1; !1PID:g55058 !'##experimental_source strain BALB/c REFERENCE I49736 !$#authors Kwon, B.S.; Halaban, R.; Chintamaneni, C. !$#journal Biochem. Biophys. Res. Commun. (1989) 161:252-260 !$#title Molecular basis of mouse Himalayan mutation. !$#cross-references MUID:89273644; PMID:2567165 !$#accession I49736 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-39,'I',41-102,'C',104-196,'Q',198-345,'G',347-419,'R', !1421-533 ##label RES !'##cross-references GB:M26729; NID:g193845; PIDN:AAA37806.1; !1PID:g309296 COMMENT This cell-specific oxidase is a glycoprotein containing two !1Cu per enzyme; it catalyzes the oxidation of tyrosine to !1dihydroxyphenylalanine (dopa) and of dopa to dopaquinone, !1the first two reactions in the formation of pigments such as !1melanins and other polyphenolic compounds in melanoma cells. GENETICS !$#gene Tyr1 !$#map_position 7 CLASSIFICATION #superfamily monophenol monooxygenase KEYWORDS albinism; alternative splicing; copper; glycoprotein; !1melanin biosynthesis; monooxygenase; oxidoreductase; !1transmembrane protein FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-533 #product monophenol monooxygenase #status predicted !8#label MAT\ !$474-497 #domain transmembrane #status predicted #label TMM\ !$86,111,161,230,337, !$371 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 533 #molecular-weight 60632 #checksum 8356 SEQUENCE /// ENTRY YRHUR2 #type complete TITLE dopachrome isomerase (EC 5.3.3.12) precursor - human ALTERNATE_NAMES dopachrome conversion factor; dopachrome oxidoreductase; dopachrome tautomerase; tyrosinase-related protein 2 ORGANISM #formal_name Homo sapiens #common_name man DATE 13-Jan-1995 #sequence_revision 17-May-1996 #text_change 03-Jun-2002 ACCESSIONS S43510; S41089; I53786 REFERENCE S43510 !$#authors Yokoyama, K.; Suzuki, H.; Yasumoto, K.; Tomita, Y.; !1Shibahara, S. !$#journal Biochim. Biophys. Acta (1994) 1217:317-321 !$#title Molecular cloning and functional analysis of a cDNA coding !1for human DOPAchrome tautomerase/tyrosinase-related !1protein-2. !$#cross-references MUID:94198295; PMID:8148378 !$#accession S43510 !'##molecule_type mRNA !'##residues 1-519 ##label YOK !'##cross-references EMBL:D17547; NID:g484259; PIDN:BAA04484.1; !1PID:g914938 REFERENCE S41089 !$#authors Bouchard, B.; del Marmol, V.; Jackson, I.J.; Cherif, D.; !1Dubertret, L. !$#journal Eur. J. Biochem. (1994) 219:127-134 !$#title Molecular characterization of a human !1tyrosinase-related-protein-2 cDNA. Patterns of expression in !1melanocytic cells. !$#cross-references MUID:94139684; PMID:8306979 !$#accession S41089 !'##molecule_type mRNA !'##residues 1-519 ##label BOU !'##cross-references GB:S69231; NID:g545618; PIDN:AAC60627.1; !1PID:g545619 REFERENCE A44749 !$#authors Pawelek, J.M. !$#journal Biochem. Biophys. Res. Commun. (1990) 166:1328-1333 !$#title Dopachrome conversion factor as an isomerase. !$#cross-references MUID:90165938; PMID:2106316 !$#contents annotation; reaction description REFERENCE I53786 !$#authors Cassady, J.L.; Sturm, R.A. !$#journal Gene (1994) 143:295-298 !$#title Sequence of the human dopachrome tautomerase-encoding TRP-2 !1cDNA. !$#cross-references MUID:94266170; PMID:8206391 !$#accession I53786 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-519 ##label RES !'##cross-references GB:L18967; NID:g399581; PIDN:AAA20870.1; !1PID:g399582 !'##experimental_source melanoma cell line A2058 GENETICS !$#gene GDB:DCT; TYRP2 !'##cross-references GDB:231628; OMIM:191275 !$#map_position 13q32-13q32 FUNCTION !$#description catalyzes the isomerization between 2-carboxy-1,2,3, !15-tetrahydroindolinium (dopachrome tautomer) and 5, !16-dihydroxyindole-2-carboxylic acid !$#pathway melanin biosynthesis CLASSIFICATION #superfamily monophenol monooxygenase KEYWORDS copper; glycoprotein; intramolecular oxidoreductase; !1isomerase; melanin biosynthesis; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-519 #product dopachrome Delta-isomerase #status predicted !8#label MAT\ !$475-493 #domain transmembrane #status predicted #label TRM\ !$170,237,300,342,377 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$189,211,220,223 #binding_site copper (His) #status predicted\ !$369,373,396,426 #binding_site copper (His) #status predicted SUMMARY #length 519 #molecular-weight 59145 #checksum 989 SEQUENCE /// ENTRY OHRTD #type complete TITLE heme oxygenase (decyclizing) (EC 1.14.99.3) - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 11-Jun-1999 ACCESSIONS A92645; A94075; A23563; A29323 REFERENCE A92645 !$#authors Mueller, R.M.; Taguchi, H.; Shibahara, S. !$#journal J. Biol. Chem. (1987) 262:6795-6802 !$#title Nucleotide sequence and organization of the rat heme !1oxygenase gene. !$#cross-references MUID:87194929; PMID:3032976 !$#accession A92645 !'##molecule_type DNA !'##residues 1-289 ##label MUE !'##cross-references GB:J02722; GB:M12129; NID:g204647; PIDN:AAA41346.1; !1PID:g204648 REFERENCE A94075 !$#authors Shibahara, S.; Muller, R.; Taguchi, H.; Yoshida, T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:7865-7869 !$#title Cloning and expression of cDNA for rat heme oxygenase. !$#cross-references MUID:86068004; PMID:3865203 !$#accession A94075 !'##molecule_type mRNA !'##residues 1-289 ##label SHI !'##cross-references GB:J02722; GB:M12129; NID:g204647; PIDN:AAA41346.1; !1PID:g204648 COMMENT This enzyme catalyzes the oxidative degradation of heme to !1biliverdin, which is subsequently converted to bilirubin. In !1the rat, the activity of heme oxygenase is highest in the !1spleen. It is inducible by heme, metal ions, endotoxin, !1bromobenzene, and other substances. GENETICS !$#introns 8/2; 48/3; 212/3; 246/1 CLASSIFICATION #superfamily heme oxygenase (decyclizing) KEYWORDS heme catabolism; oxidoreductase SUMMARY #length 289 #molecular-weight 33005 #checksum 1252 SEQUENCE /// ENTRY S00325 #type complete TITLE heme oxygenase (decyclizing) (EC 1.14.99.3) 1 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 24-Sep-1999 ACCESSIONS S00325; I37551; I59158 REFERENCE S00325 !$#authors Yoshida, T.; Biro, P.; Cohen, T.; Mueller, R.M.; Shibahara, !1S. !$#journal Eur. J. Biochem. (1988) 171:457-461 !$#title Human heme oxygenase cDNA and induction of its mRNA by !1hemin. !$#cross-references MUID:88151939; PMID:3345742 !$#accession S00325 !'##molecule_type mRNA !'##residues 1-288 ##label YOS !'##cross-references EMBL:X06985; NID:g35172; PIDN:CAA30045.1; !1PID:g35173 REFERENCE I37551 !$#authors Shibahara, S.; Sato, M.; Muller, R.M.; Yoshida, T. !$#journal Eur. J. Biochem. (1989) 179:557-563 !$#title Structural organization of the human heme oxygenase gene and !1the function of its promoter. !$#cross-references MUID:89153089; PMID:2537723 !$#accession I37551 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-7 ##label SHI !'##cross-references EMBL:X14782; NID:g32362; PIDN:CAA32886.1; !1PID:g579973 REFERENCE I59158 !$#authors Keyse, S.M.; Tyrrell, R.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:99-103 !$#title Heme oxygenase is the major 32-kDa stress protein induced in !1human skin fibroblasts by UVA radiation, hydrogen peroxide, !1and sodium arsenite. !$#cross-references MUID:89098939; PMID:2911585 !$#accession I59158 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-103 ##label KEY !'##cross-references GB:M23041; NID:g557551; PIDN:AAA50403.1; !1PID:g557552 GENETICS !$#gene GDB:HMOX1; HMOX; HO !'##cross-references GDB:135036; OMIM:141250 !$#map_position 22q12-22q12 CLASSIFICATION #superfamily heme oxygenase (decyclizing) KEYWORDS oxidoreductase SUMMARY #length 288 #molecular-weight 32818 #checksum 2485 SEQUENCE /// ENTRY A35199 #type complete TITLE heme oxygenase (decyclizing) (EC 1.14.99.3) 2 [similarity] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS A35199; A29922 REFERENCE A35199 !$#authors Rotenberg, M.O.; Maines, M.D. !$#journal J. Biol. Chem. (1990) 265:7501-7506 !$#title Isolation, characterization, and expression in Escherichia !1coli of a cDNA encoding rat heme oxygenase-2. !$#cross-references MUID:90237051; PMID:2185251 !$#accession A35199 !'##molecule_type mRNA !'##residues 1-315 ##label ROT !'##cross-references GB:J05405; NID:g204626; PIDN:AAA41340.1; !1PID:g204627 REFERENCE A29922 !$#authors Cruse, I.; Maines, M.D. !$#journal J. Biol. Chem. (1988) 263:3348-3353 !$#title Evidence suggesting that the two forms of heme oxygenase are !1products of different genes. !$#cross-references MUID:88139412; PMID:3343248 !$#accession A29922 !'##molecule_type mRNA !'##residues 'EFRNK',147-229,'TEF' ##label CRU !'##cross-references GB:M18918; NID:g204649; PIDN:AAA41347.1; !1PID:g554443 CLASSIFICATION #superfamily heme oxygenase (decyclizing) KEYWORDS oxidoreductase SUMMARY #length 315 #molecular-weight 35762 #checksum 8535 SEQUENCE /// ENTRY A24699 #type complete TITLE stearoyl-CoA 9-desaturase (EC 1.14.19.1) [similarity] - rat ALTERNATE_NAMES acyl-CoA desaturase; Delta9 fatty acid desaturase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS A24699; JX0150; I58133 REFERENCE A24699 !$#authors Thiede, M.A.; Ozols, J.; Strittmatter, P. !$#journal J. Biol. Chem. (1986) 261:13230-13235 !$#title Construction and sequence of cDNA for rat liver stearyl !1coenzyme a desaturase. !$#cross-references MUID:87008535; PMID:2428815 !$#accession A24699 !'##molecule_type mRNA !'##residues 1-358 ##label THI !'##cross-references GB:J02585; NID:g206859; PIDN:AAA42116.1; !1PID:g206860 REFERENCE JX0150 !$#authors Mihara, K. !$#journal J. Biochem. (1990) 108:1022-1029 !$#title Structure and regulation of rat liver microsomal !1stearoyl-CoA desaturase gene. !$#cross-references MUID:91210202; PMID:1982442 !$#accession JX0150 !'##molecule_type DNA !'##residues 1-290,'A',292-358 ##label MIH REFERENCE I58133 !$#authors Baba, H.; Fuss, B.; Watson, J.B.; Zane, L.T.; Macklin, W.B. !$#journal Neurochem. Res. (1994) 19:1091-1099 !$#title Identification of novel mRNAs expressed in oligodendrocytes. !$#cross-references MUID:95098214; PMID:7800118 !$#accession I58133 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-4,'I',6-10,'G',12-13,'SA',16-20,'A',22-25,'GQ',28-30,'G', !132-33,'FE',36,'N',38,'HHWGA',44,'V',46-48,'IKD',52,'LY', !155-60 ##label RES !'##cross-references GB:S75730; NID:g861452; PIDN:AAB32826.1; !1PID:g861453 CLASSIFICATION #superfamily mammalian stearoyl-CoA desaturase; stearoyl-CoA !1desaturase homology KEYWORDS oxidoreductase; unsaturated fatty acid biosynthesis FEATURE !$113-307 #domain stearoyl-CoA desaturase homology #label SDH SUMMARY #length 358 #molecular-weight 41482 #checksum 7100 SEQUENCE /// ENTRY A36507 #type complete TITLE stearoyl-CoA 9-desaturase (EC 1.14.19.1) 2 [similarity] - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 03-Jun-2002 ACCESSIONS A36507 REFERENCE A36507 !$#authors Kaestner, K.H.; Ntambi, J.M.; Kelly Jr., T.J.; Lane, M.D. !$#journal J. Biol. Chem. (1989) 264:14755-14761 !$#title Differentiation-induced gene expression in 3T3-L1 !1preadipocytes. A second differentially expressed gene !1encoding stearoyl-CoA desaturase. !$#cross-references MUID:89359271; PMID:2570068 !$#accession A36507 !'##molecule_type mRNA !'##residues 1-358 ##label KAE !'##cross-references GB:M26270; NID:g200933; PIDN:AAA40094.1; !1PID:g200934 CLASSIFICATION #superfamily mammalian stearoyl-CoA desaturase; stearoyl-CoA !1desaturase homology KEYWORDS oxidoreductase FEATURE !$113-307 #domain stearoyl-CoA desaturase homology #label SDH SUMMARY #length 358 #molecular-weight 41073 #checksum 7288 SEQUENCE /// ENTRY S57643 #type complete TITLE stearoyl-CoA 9-desaturase (EC 1.14.19.1) - Synechococcus sp. ALTERNATE_NAMES Delta9 fatty acid desaturase ORGANISM #formal_name Synechococcus sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S57643 REFERENCE S57643 !$#authors Nishizawa, O.; Toguri, T. !$#submission submitted to the EMBL Data Library, January 1994 !$#description Fatty acid desatarase gene from Anacytis nidulans. !$#accession S57643 !'##molecule_type DNA !'##residues 1-278 ##label NIS !'##cross-references EMBL:X77367; NID:g886832; PIDN:CAA54556.1; !1PID:g886833 !'##note the source is designated as Anacystis nidulans CLASSIFICATION #superfamily mammalian stearoyl-CoA desaturase; stearoyl-CoA !1desaturase homology KEYWORDS oxidoreductase; unsaturated fatty acid biosynthesis FEATURE !$54-243 #domain stearoyl-CoA desaturase homology #label SDH SUMMARY #length 278 #molecular-weight 32236 #checksum 2170 SEQUENCE /// ENTRY S75765 #type complete TITLE stearoyl-CoA 9-desaturase (EC 1.14.19.1) 1 - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES acyl-CoA desaturase 1; Delta9 fatty acid desaturase; protein sll0541 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S75765 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75765 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-318 ##label KAN !'##cross-references EMBL:D64003; GB:AB001339; NID:g1001200; !1PIDN:BAA10500.1; PID:g1001256 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene des9 CLASSIFICATION #superfamily mammalian stearoyl-CoA desaturase; stearoyl-CoA !1desaturase homology KEYWORDS oxidoreductase; unsaturated fatty acid biosynthesis FEATURE !$95-278 #domain stearoyl-CoA desaturase homology #label SDH SUMMARY #length 318 #molecular-weight 37203 #checksum 5229 SEQUENCE /// ENTRY S61359 #type complete TITLE stearoyl-CoA 9-desaturase (EC 1.14.19.1) - Rosa hybrida ALTERNATE_NAMES Delta9 fatty acid desaturase ORGANISM #formal_name Rosa hybrida DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S61359 REFERENCE S61359 !$#authors Fukuchi-Mizutani, M.; Savin, K.; Cornish, E.; Tanaka, Y.; !1Ashikari, T.; Kusumi, T.; Murata, N. !$#journal Plant Mol. Biol. (1995) 29:627-635 !$#title Senescence-induced expression of a homologue of Delta-9 !1desaturase in rose petals. !$#cross-references MUID:96128006; PMID:8541490 !$#accession S61359 !'##molecule_type mRNA !'##residues 1-297 ##label FUK !'##cross-references DDBJ:D49383; NID:g2580424; PIDN:BAA23134.1; !1PID:g2580425; DDBJ:D49384; NID:g2580426; PID:g2580427; !1DDBJ:D49385; NID:g2580428; PID:g2580429 !'##experimental_source strain Kardinal, clones RP4, RP44, and RP46 CLASSIFICATION #superfamily mammalian stearoyl-CoA desaturase; stearoyl-CoA !1desaturase homology KEYWORDS oxidoreductase; unsaturated fatty acid biosynthesis FEATURE !$60-247 #domain stearoyl-CoA desaturase homology #label SDH SUMMARY #length 297 #molecular-weight 34729 #checksum 6497 SEQUENCE /// ENTRY JC6180 #type complete TITLE stearoyl-CoA 9-desaturase (EC 1.14.19.1) - yeast (Pichia angusta) ALTERNATE_NAMES Delta9 fatty acid desaturase ORGANISM #formal_name Pichia angusta DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS JC6180 REFERENCE JC6180 !$#authors Anamnart, S.; Tomita, T.; Fukui, F.; Fujimori, K.; !1Harashima, S.; Yamada, Y.; Oshima, Y. !$#journal Gene (1997) 184:299-306 !$#title The P-OLE1 gene of Pichia angusta encodes a delta 9-fatty !1acid desaturase and complements the ole1 mutation of !1Saccharomyces cerevisiae. !$#cross-references MUID:97183677; PMID:9031643 !$#accession JC6180 !'##molecule_type DNA !'##residues 1-451 ##label ANA !'##cross-references DDBJ:D83185; NID:g1871453; PIDN:BAA11837.1; !1PID:g1871454 COMMENT This enzyme is a major determinant of cellular membrane and !1storage lipid composition, and it is important in cell !1growth. GENETICS !$#gene P-ole1 CLASSIFICATION #superfamily yeast stearoyl-CoA desaturase; cytochrome b5 !1core homology; stearoyl-CoA desaturase homology KEYWORDS heme; iron; metalloprotein; oxidoreductase; unsaturated !1fatty acid biosynthesis FEATURE !$95-285 #domain stearoyl-CoA desaturase homology #label SDH\ !$349-426 #domain cytochrome b5 core homology #label CB5\ !$384,410 #binding_site heme iron (His) (axial ligands) #status !8predicted SUMMARY #length 451 #molecular-weight 51941 #checksum 6244 SEQUENCE /// ENTRY S64059 #type complete TITLE stearoyl-CoA 9-desaturase (EC 1.14.19.1) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES Delta9 fatty acid desaturase; protein G3472; protein YGL055w ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S64059; A23675 REFERENCE S64044 !$#authors Feuermann, M.; Potier, S.; Souciet, J.L. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64059 !'##molecule_type DNA !'##residues 1-510 ##label FEU !'##cross-references EMBL:Z72577; NID:g1322551; PIDN:CAA96757.1; !1PID:g1322552; GSPDB:GN00007; MIPS:YGL055w !'##experimental_source strain S288C REFERENCE A23675 !$#authors Stukey, J.E.; McDonough, V.M.; Martin, C.E. !$#journal J. Biol. Chem. (1990) 265:20144-20149 !$#title The OLE1 gene of Saccharomyces cerevisiae encodes the delta9 !1fatty acid desaturase and can be functionally replaced by !1the rat stearoyl-CoA desaturase gene. !$#cross-references MUID:91056050; PMID:1978720 !$#accession A23675 !'##molecule_type DNA !'##residues 1-303,'M',305-510 ##label STU !'##cross-references GB:J05676; NID:g172063; PIDN:AAA34826.1; !1PID:g172064 GENETICS !$#gene SGD:OLE1; MDM2; MIPS:YGL055w !'##cross-references SGD:S0003023; MIPS:YGL055w !$#map_position 7L CLASSIFICATION #superfamily yeast stearoyl-CoA desaturase; cytochrome b5 !1core homology; stearoyl-CoA desaturase homology KEYWORDS endoplasmic reticulum; heme; iron; metalloprotein; !1oxidoreductase; transmembrane protein; unsaturated fatty !1acid biosynthesis FEATURE !$116-132 #domain transmembrane #status predicted #label TM1\ !$141-157 #domain transmembrane #status predicted #label TM2\ !$155-345 #domain stearoyl-CoA desaturase homology #label SDH\ !$257-273 #domain transmembrane #status predicted #label TM3\ !$409-486 #domain cytochrome b5 core homology #label CB5\ !$444,470 #binding_site heme iron (His) (axial ligands) #status !8predicted SUMMARY #length 510 #molecular-weight 58403 #checksum 1467 SEQUENCE /// ENTRY S71634 #type complete TITLE stearoyl-CoA 9-desaturase (EC 1.14.19.1) - Cryptococcus curvatus ALTERNATE_NAMES Delta9 fatty acid desaturase ORGANISM #formal_name Cryptococcus curvatus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S71634 REFERENCE S71634 !$#authors Meesters, P.A.E.P.; Eggink, G. !$#journal Yeast (1996) 12:723-730 !$#title Isolation and characterization of a Delta-9 fatty acid !1desaturase gene from the oleaginous yeast Cryptococcus !1curvatus CBS 570. !$#cross-references MUID:96408765; PMID:8813759 !$#accession S71634 !'##molecule_type DNA !'##residues 1-493 ##label MEE !'##cross-references EMBL:Y10422; NID:g1783356; PIDN:CAA71449.1; !1PID:g1783357 !'##experimental_source strain CBS570 GENETICS !$#gene Ole1 CLASSIFICATION #superfamily yeast stearoyl-CoA desaturase; cytochrome b5 !1core homology; stearoyl-CoA desaturase homology KEYWORDS heme; iron; metalloprotein; oxidoreductase; unsaturated !1fatty acid biosynthesis FEATURE !$119-308 #domain stearoyl-CoA desaturase homology #label SDH\ !$372-448 #domain cytochrome b5 core homology #label CB5\ !$406,432 #binding_site heme iron (His) (axial ligands) #status !8predicted SUMMARY #length 493 #molecular-weight 54717 #checksum 4560 SEQUENCE /// ENTRY OHCSAD #type complete TITLE acyl-[acyl-carrier-protein] desaturase (EC 1.14.19.2) precursor - castor bean ALTERNATE_NAMES stearoyl-[acyl-carrier-protein] desaturase ORGANISM #formal_name Ricinus communis #common_name castor bean DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 03-Jun-2002 ACCESSIONS S16463; A39170 REFERENCE S16463 !$#authors Knutzon, D.S.; Scherer, D.E.; Schreckengost, W.E. !$#journal Plant Physiol. (1991) 96:344-345 !$#title Nucleotide sequence of a complementary DNA clone encoding !1stearoyl-acyl carrier protein desaturase from castor bean, !1Ricinus communis. !$#accession S16463 !'##molecule_type mRNA !'##residues 1-396 ##label KNU !'##cross-references EMBL:X56508; NID:g21092; PIDN:CAA39859.1; !1PID:g21093 REFERENCE A39170 !$#authors Shanklin, J.; Somerville, C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:2510-2514 !$#title Stearoyl-acyl-carrier-protein desaturase from higher plants !1is structurally unrelated to the animal and fungal homologs. !$#cross-references MUID:91172837; PMID:2006187 !$#accession A39170 !'##status preliminary !'##molecule_type mRNA !'##residues 1-396 ##label SHA !'##cross-references GB:M59858 !'##note parts of this sequence were confirmed by peptide sequencing CLASSIFICATION #superfamily acyl-[acyl-carrier-protein] desaturase KEYWORDS chloroplast; fatty acid biosynthesis; oxidoreductase FEATURE !$1-33 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$34-396 #product acyl-[acyl-carrier-protein] desaturase !8#status predicted #label MAT SUMMARY #length 396 #molecular-weight 45370 #checksum 590 SEQUENCE /// ENTRY OHSPAD #type complete TITLE acyl-[acyl-carrier-protein] desaturase (EC 1.14.19.2) precursor - spinach ALTERNATE_NAMES stearoyl-[acyl-carrier-protein] desaturase ORGANISM #formal_name Spinacia oleracea #common_name spinach DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 03-Jun-2002 ACCESSIONS S22480; S18183 REFERENCE S22480 !$#authors Nishida, I.; Beppu, T.; Matsuo, T.; Murata, N. !$#journal Plant Mol. Biol. (1992) 19:711-713 !$#title Nucleotide sequence of a cDNA clone encoding a precursor to !1stearoyl-(acyl-carrier-protein) desaturase from spinach, !1Spinacia oleracea. !$#cross-references MUID:92329733; PMID:1627785 !$#accession S22480 !'##molecule_type mRNA !'##residues 1-399 ##label NIS !'##cross-references EMBL:X62898; NID:g21229; PIDN:CAA44687.1; !1PID:g21230 CLASSIFICATION #superfamily acyl-[acyl-carrier-protein] desaturase KEYWORDS chloroplast; fatty acid biosynthesis; oxidoreductase FEATURE !$1-35 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$36-399 #product acyl-[acyl-carrier-protein] desaturase !8#status predicted #label MAT SUMMARY #length 399 #molecular-weight 45663 #checksum 2965 SEQUENCE /// ENTRY A39173 #type complete TITLE acyl-[acyl-carrier-protein] desaturase (EC 1.14.19.2) precursor - safflower ORGANISM #formal_name Carthamus tinctorius #common_name safflower DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS A39173 REFERENCE A39173 !$#authors Thompson, G.A.; Scherer, D.E.; Foxall-Van Aken, S.; Kenny, !1J.W.; Young, H.L.; Shintani, D.K.; Kridl, J.C.; Knauf, V.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:2578-2582 !$#title Primary structures of the precursor and mature forms of !1stearoyl-acyl carrier protein desaturase from safflower !1embryos and requirement of ferredoxin for enzyme activity. !$#cross-references MUID:91172850; PMID:2006194 !$#accession A39173 !'##status preliminary !'##molecule_type mRNA !'##residues 1-396 ##label THO !'##cross-references GB:M61109; NID:g167196; PIDN:AAA33021.1; !1PID:g167197 CLASSIFICATION #superfamily acyl-[acyl-carrier-protein] desaturase KEYWORDS chloroplast; oxidoreductase SUMMARY #length 396 #molecular-weight 45054 #checksum 1581 SEQUENCE /// ENTRY JQ2336 #type complete TITLE omega-3 fatty acid desaturase (EC 1.14.99.-) CFD [similarity] - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 21-Jul-2000 ACCESSIONS JQ2336; A49503 REFERENCE JQ2335 !$#authors Yadav, N.S.; Wierzbicki, A.; Aegerter, M.; Caster, C.S.; !1Perez-Grau, L.; Kinney, A.J.; Hitz, W.D.; Booth Jr., J.R.; !1Schweiger, B.; Stecca, K.L.; Allen, S.M.; Blackwell, M.; !1Reiter, R.S.; Carlson, T.J.; Russell, S.H.; Feldmann, K.A.; !1Pierce, J.; Browse, J. !$#journal Plant Physiol. (1993) 103:467-476 !$#title Cloning of higher plant omega-3 fatty acid desaturases. !$#cross-references MUID:94302147; PMID:8029334 !$#accession JQ2336 !'##molecule_type mRNA !'##residues 1-446 ##label YAD !'##cross-references GB:D26019; NID:g809491; PIDN:BAA05040.1; !1PID:g468434 REFERENCE A49503 !$#authors Iba, K.; Gibson, S.; Nishiuchi, T.; Fuse, T.; Nishimura, M.; !1Arondel, V.; Hugly, S.; Somerville, C. !$#journal J. Biol. Chem. (1993) 268:24099-24105 !$#title A gene encoding a chloroplast omega-3 fatty acid desaturase !1complements alterations in fatty acid desaturation and !1chloroplast copy number of the fad7 mutant of Arabidopsis !1thaliana. !$#cross-references MUID:94043239; PMID:8226956 !$#accession A49503 !'##molecule_type DNA !'##residues 1-446 ##label IBA !'##cross-references GB:D14007; NID:g461160; PIDN:BAA03106.1; !1PID:g541653 COMMENT The omega-6 and omega-3 fatty acid desaturases introduce the !1second and the third double bonds, respectively, in the !1biosynthesis of 18:2 and 18:3 fatty acids, which are !1important constituents of plant membranes. CLASSIFICATION #superfamily omega-3 fatty acid desaturase KEYWORDS oxidoreductase SUMMARY #length 446 #molecular-weight 51174 #checksum 4653 SEQUENCE /// ENTRY JQ2339 #type complete TITLE omega-3 fatty acid desaturase (EC 1.14.99.-) GMD [similarity] - soybean ORGANISM #formal_name Glycine max #common_name soybean DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS JQ2339 REFERENCE JQ2335 !$#authors Yadav, N.S.; Wierzbicki, A.; Aegerter, M.; Caster, C.S.; !1Perez-Grau, L.; Kinney, A.J.; Hitz, W.D.; Booth Jr., J.R.; !1Schweiger, B.; Stecca, K.L.; Allen, S.M.; Blackwell, M.; !1Reiter, R.S.; Carlson, T.J.; Russell, S.H.; Feldmann, K.A.; !1Pierce, J.; Browse, J. !$#journal Plant Physiol. (1993) 103:467-476 !$#title Cloning of higher plant omega-3 fatty acid desaturases. !$#cross-references MUID:94302147; PMID:8029334 !$#contents cDNA:GMD !$#accession JQ2339 !'##molecule_type mRNA !'##residues 1-453 ##label YAD !'##cross-references GB:L22965; NID:g408791; PIDN:AAA61776.1; !1PID:g408792 COMMENT This enzyme introduces the third double bond in the !1biosynthesis of 18:2 and 18:3 fatty acids which are !1important constituents of plant membranes. CLASSIFICATION #superfamily omega-3 fatty acid desaturase KEYWORDS chloroplast; oxidoreductase SUMMARY #length 453 #molecular-weight 51362 #checksum 7549 SEQUENCE /// ENTRY JQ2335 #type complete TITLE omega-3 fatty acid desaturase (EC 1.14.99.-) CF3 [similarity] - Arabidopsis thaliana ALTERNATE_NAMES protein F23F1.10 ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 02-Feb-2001 ACCESSIONS JQ2335; T02487; A84703 REFERENCE JQ2335 !$#authors Yadav, N.S.; Wierzbicki, A.; Aegerter, M.; Caster, C.S.; !1Perez-Grau, L.; Kinney, A.J.; Hitz, W.D.; Booth Jr., J.R.; !1Schweiger, B.; Stecca, K.L.; Allen, S.M.; Blackwell, M.; !1Reiter, R.S.; Carlson, T.J.; Russell, S.H.; Feldmann, K.A.; !1Pierce, J.; Browse, J. !$#journal Plant Physiol. (1993) 103:467-476 !$#title Cloning of higher plant omega-3 fatty acid desaturases. !$#cross-references MUID:94302147; PMID:8029334 !$#accession JQ2335 !'##molecule_type mRNA !'##residues 1-386 ##label YAD !'##cross-references GB:D17579; NID:g1030693; PIDN:BAA04505.1; !1PID:g471091 REFERENCE Z14675 !$#authors Rounsley, S.D.; Lin, X.; Ketchum, K.A.; Crosby, M.L.; !1Brandon, R.C.; Sykes, S.M.; Kaul, S.; Mason, T.M.; !1Kerlavage, A.R.; Adams, M.D.; Somerville, C.R.; Venter, J.C. !$#submission submitted to the EMBL Data Library, August 1998 !$#description Arabidopsis thaliana chromosome II BAC F23F1 genomic !1sequence. !$#accession T02487 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-386 ##label ROU !'##cross-references EMBL:AC004680; NID:g3420043; PIDN:AAC31854.1; !1PID:g3420053 !'##experimental_source cultivar Columbia REFERENCE A84420 !$#authors Lin, X.; Kaul, S.; Rounsley, S.D.; Shea, T.P.; Benito, M.I.; !1Town, C.D.; Fujii, C.Y.; Mason, T.M.; Bowman, C.L.; !1Barnstead, M.E.; Feldblyum, T.V.; Buell, C.R.; Ketchum, !1K.A.; Lee, J.J.; Ronning, C.M.; Koo, H.; Moffat, K.S.; !1Cronin, L.A.; Shen, M.; VanAken, S.E.; Umayam, L.; Tallon, !1L.J.; Gill, J.E.; Adams, M.D.; Carrera, A.J.; Creasy, T.H.; !1Goodman, H.M.; Somerville, C.R.; Copenhaver, G.P.; Preuss, !1D.; Nierman, W.C.; White, O.; Eisen, J.A.; Salzberg, S.L.; !1Fraser, C.M.; Venter, J.C. !$#journal Nature (1999) 402:761-768 !$#title Sequence and analysis of chromosome 2 of the plant !1Arabidopsis thaliana. !$#cross-references MUID:20083487; PMID:10617197 !$#accession A84703 !'##status preliminary !'##molecule_type DNA !'##residues 1-386 ##label STO !'##cross-references GB:AE002093; NID:g3420053; PIDN:AAC31854.1; !1GSPDB:GN00139 COMMENT The omega-6 and omega-3 fatty acid desaturases introduce the !1second and the third double bonds, respectively, in the !1biosynthesis of 18:2 and 18:3 fatty acids, which are !1important constituents of plant membranes. GENETICS !$#gene At2g29980; F23F1.10 !$#map_position 2 !$#introns 103/2; 133/2; 155/3; 186/3; 248/3; 275/3; 321/3 CLASSIFICATION #superfamily omega-3 fatty acid desaturase KEYWORDS oxidoreductase SUMMARY #length 386 #molecular-weight 44076 #checksum 8044 SEQUENCE /// ENTRY A44227 #type complete TITLE omega-3 fatty acid desaturase (EC 1.14.99.-) [similarity] - rape ALTERNATE_NAMES omega-3 linoleate desaturase ORGANISM #formal_name Brassica napus #common_name rape DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS A44227 REFERENCE A44227 !$#authors Arondel, V.; Lemieux, B.; Hwang, I.; Gibson, S.; Goodman, !1H.M.; Somerville, C.R. !$#journal Science (1992) 258:1353-1355 !$#title Map-based cloning of a gene controlling omega-3 fatty acid !1desaturation in Arabidopsis. !$#cross-references MUID:93088059; PMID:1455229 !$#accession A44227 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-383 ##label ARO !'##cross-references GB:L01418; NID:g167147; PIDN:AAA32994.1; !1PID:g167148 !'##experimental_source developing seed !'##note sequence extracted from NCBI backbone (NCBIP:119842) CLASSIFICATION #superfamily omega-3 fatty acid desaturase KEYWORDS oxidoreductase SUMMARY #length 383 #molecular-weight 43936 #checksum 2897 SEQUENCE /// ENTRY JQ2337 #type complete TITLE omega-3 fatty acid desaturase (EC 1.14.99.-) BN3 [similarity] - rape ORGANISM #formal_name Brassica napus #common_name rape DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS JQ2337 REFERENCE JQ2335 !$#authors Yadav, N.S.; Wierzbicki, A.; Aegerter, M.; Caster, C.S.; !1Perez-Grau, L.; Kinney, A.J.; Hitz, W.D.; Booth Jr., J.R.; !1Schweiger, B.; Stecca, K.L.; Allen, S.M.; Blackwell, M.; !1Reiter, R.S.; Carlson, T.J.; Russell, S.H.; Feldmann, K.A.; !1Pierce, J.; Browse, J. !$#journal Plant Physiol. (1993) 103:467-476 !$#title Cloning of higher plant omega-3 fatty acid desaturases. !$#cross-references MUID:94302147; PMID:8029334 !$#contents cDNA:BN3 !$#accession JQ2337 !'##molecule_type mRNA !'##residues 1-377 ##label YAD !'##cross-references GB:L22962; NID:g408491; PIDN:AAA61775.1; !1PID:g408492 COMMENT This enzyme introduces the third double bond in the !1biosynthesis of 18:2 and 18:3 fatty acids which are !1important constituents of plant membranes. CLASSIFICATION #superfamily omega-3 fatty acid desaturase KEYWORDS oxidoreductase SUMMARY #length 377 #molecular-weight 43258 #checksum 3294 SEQUENCE /// ENTRY DSHUCZ #type complete TITLE superoxide dismutase (EC 1.15.1.1) (Cu-Zn) [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Aug-1980 #sequence_revision 19-Feb-1984 #text_change 21-Jul-2000 ACCESSIONS A22703; PC2217; A23046; A93969; JX0055; A91282; A90440; !1I54382; I68676; I68677; JC5686; A00512 REFERENCE A22703 !$#authors Levanon, D.; Lieman-Hurwitz, J.; Dafni, N.; Wigderson, M.; !1Sherman, L.; Bernstein, Y.; Laver-Rudich, Z.; Danciger, E.; !1Stein, O.; Groner, Y. !$#journal EMBO J. (1985) 4:77-84 !$#title Architecture and anatomy of the chromosomal locus in human !1chromosome 21 encoding the Cu/Zn superoxide dismutase. !$#cross-references MUID:85257452; PMID:3160582 !$#accession A22703 !'##molecule_type DNA !'##residues 2-154 ##label LEV !'##cross-references EMBL:X01780; NID:g36534; PIDN:CAA25915.1; !1PID:g36535; EMBL:X01781; NID:g36523; EMBL:X01782; !1NID:g36525; EMBL:X01783; NID:g36527; EMBL:X01784; !1NID:g36529; PID:g1237407 !'##note the authors did not translate the codon for residue 1 REFERENCE PC2217 !$#authors Kim, H.T.; Kim, Y.H.; Nam, J.W.; Lee, H.J.; Rho, H.M.; Jung, !1G. !$#journal Biochem. Biophys. Res. Commun. (1994) 201:1526-1533 !$#title Study of 5'-flanking region of human Cu/Zn superoxide !1dismutase. !$#cross-references MUID:94296434; PMID:8024598 !$#accession PC2217 !'##molecule_type DNA !'##residues 1-24 ##label KIM !'##cross-references EMBL:Z29336; NID:g531099 REFERENCE A23046 !$#authors Hallewell, R.A.; Masiarz, F.R.; Najarian, R.C.; Puma, J.P.; !1Quiroga, M.R.; Randolph, A.; Sanchez-Pescador, R.; !1Scandella, C.J.; Smith, B.; Steimer, K.S.; Mullenbach, G.T. !$#journal Nucleic Acids Res. (1985) 13:2017-2034 !$#title Human Cu/Zn superoxide dismutase cDNA: isolation of clones !1synthesising high levels of active or inactive enzyme from !1an expression library. !$#cross-references MUID:85215596; PMID:3889846 !$#accession A23046 !'##molecule_type mRNA !'##residues 1-154 ##label HAL !'##cross-references EMBL:X02317; NID:g36541; PIDN:CAA26182.1; !1PID:g36542 REFERENCE A93969 !$#authors Sherman, L.; Dafni, N.; Lieman-Hurwitz, J.; Groner, Y. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:5465-5469 !$#title Nucleotide sequence and expression of human chromosome !121-encoded superoxide dismutase mRNA. !$#cross-references MUID:83299994; PMID:6577438 !$#accession A93969 !'##molecule_type mRNA !'##residues 2-154 ##label SHE !'##cross-references GB:K00065; NID:g36541; PIDN:CAA26182.1; PID:g36542 !'##note the authors did not translate the codon for residue 1 REFERENCE JX0055 !$#authors Kajihara, J.; Enomoto, M.; Nishijima, K.; Yabuuchi, M.; !1Katoh, K. !$#journal J. Biochem. (1988) 104:851-854 !$#title Comparison of properties between human recombinant and !1placental copper-zinc SOD. !$#cross-references MUID:89174523; PMID:2853161 !$#accession JX0055 !'##molecule_type protein !'##residues 2-154 ##label KAJ !'##experimental_source placenta REFERENCE A91282 !$#authors Barra, D.; Martini, F.; Bannister, J.V.; Schinina, M.E.; !1Rotilio, G.; Bannister, W.H.; Bossa, F. !$#journal FEBS Lett. (1980) 120:53-56 !$#title The complete amino acid sequence of human Cu/Zn superoxide !1dismutase. !$#cross-references MUID:81067132; PMID:7002610 !$#accession A91282 !'##molecule_type protein !'##residues 2-11,'N',13-92,'N',94-154 ##label BAR !'##experimental_source erythrocytes REFERENCE A90440 !$#authors Jabusch, J.R.; Farb, D.L.; Kerschensteiner, D.A.; Deutsch, !1H.F. !$#journal Biochemistry (1980) 19:2310-2316 !$#title Some sulfhydryl properties and primary structure of human !1erythrocyte superoxide dismutase. !$#cross-references MUID:80221052; PMID:6770891 !$#accession A90440 !'##molecule_type protein !'##residues 2-17,'S',19-26,'N',28-49,'Q',51-52,'ND',55-98,'V',100-154 !1##label JAB REFERENCE I54382 !$#authors Enayat, Z.E.; Orrell, R.W.; Claus, A.; Ludolph, A.; Bachus, !1R.; Brockmueller, J.; Ray-Chaudhuri, K.; Radunovic, A.; !1Shaw, C.; Wilkinson, J.; King, A.; Swash, M.; Leigh, P.N.; !1de Belleroche, J.; Powell, J. !$#journal Hum. Mol. Genet. (1995) 4:1239-1240 !$#title Two novel mutations in the gene for copper zinc superoxide !1dismutase in UK families with amyotrophic lateral sclerosis. !$#cross-references MUID:96133303; PMID:8528216 !$#accession I54382 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 'SMKKQIH',127-154 ##label ENA1 !'##cross-references GB:L44746; NID:g928824; PIDN:AAC41773.1; !1PID:g928825 !'##note mutated exon 5 from patient with familial amyotrophic lateral !1sclerosis !$#accession I68676 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 25-48,'Q',50-56 ##label ENA2 !'##cross-references GB:L46374; NID:g939772; PIDN:AAB59626.1; !1PID:g939773 !'##note mutant sequence from patient with familial amyotrophic lateral !1sclerosis !$#accession I68677 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 120-125,'H',127-154 ##label ENA3 !'##cross-references GB:L46375; NID:g939774; PIDN:AAB59627.1; !1PID:g939775 !'##note mutant sequence from patient with familial amyotrophic lateral !1sclerosis REFERENCE JC5686 !$#authors Yamazaki, Y.; Takao, T.; Murata, H.; Kawaharada, Y.; !1Sugiyama, T.; Shimonishi, Y. !$#journal Res. Commun. Biochem. Cell Mol. Biol. (1997) 1:205-217 !$#title The use of capillary liquid chromatography/electrospray mass !1spectrometry to identify a specific cysteine residue !1susceptible to S-thiolation in recombinant human Cu,Zn !1superoxide dismutase. !$#accession JC5686 !'##molecule_type protein !'##residues 2-154 ##label YAM !'##note intermolecular disulfide bonds form under non-physiological !1conditions REFERENCE A44737 !$#authors Rosen, D.R.; Siddique, T.; Patterson, D.; Figlewicz, D.A.; !1Sapp, P.; Hentati, A.; Donaldson, D.; Goto, J.; O'Regan, !1J.P.; Deng, H.X.; Rahmani, Z.; Krizus, A.; McKenna-Yasek, !1D.; Cayabyab, A.; Gaston, S.M.; Berger, R.; Tanzi, R.E.; !1Halperin, J.J.; Herzfeldt, B.; Van den Bergh, R.; Hung, !1W.Y.; Bird, T.; Deng, G.; Mulder, D.W.; Smyth, C.; Laing, !1N.G.; Soriano, E.; Pericak-Vance, M.A.; Haines, J.; Rouleau, !1G.A.; Gusella, J.S.; Horvitz, H.R.; Brown Jr., R.H. !$#journal Nature (1993) 362:59-62 !$#title Mutations in Cu/Zn superoxide dismutase gene are associated !1with familial amyotrophic lateral sclerosis. !$#cross-references MUID:93188958; PMID:8446170 !$#contents annotation; mutant sequences reported REFERENCE A52244 !$#authors Parge, H.E.; Tainer, J.A. !$#submission submitted to the Brookhaven Protein Data Bank, July 1993 !$#cross-references PDB:1SPD !$#contents annotation; X-ray crystallography, 2.4 angstroms, residues !12-154 !$#note erythrocyte recombinant form expressed in yeast REFERENCE A44540 !$#authors Parge, H.E.; Hallewell, R.A.; Tainer, J.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:6109-6113 !$#title Atomic structures of wild-type and thermostable mutant !1recombinant human Cu,Zn superoxide dismutase. !$#cross-references MUID:92335247; PMID:1463506 !$#contents annotation; X-ray crystallography, 2.5 angstroms GENETICS !$#gene GDB:SOD1; ALS; ALS1 !'##cross-references GDB:119596; OMIM:147450 !$#map_position 21q22.1-21q22.1 !$#introns 24/3; 56/3; 80/3; 119/3 !$#note a defect in this enzyme is the cause of adult familial !1amyotrophic lateral sclerosis, Lou Gehrig's disease COMPLEX homodimer FUNCTION !$#description catalyzes the dismutation of 2 molecules of peroxide radical !1to dioxygen and hydrogen peroxide CLASSIFICATION #superfamily superoxide dismutase (Cu-Zn) KEYWORDS acetylated amino end; copper; homodimer; Lou Gehrig's !1disease; metalloprotein; oxidoreductase; zinc FEATURE !$2-154 #product superoxide dismutase (Cu-Zn) #status !8experimental #label MAT\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental\ !$47,49,64,121 #binding_site copper (His) #status experimental\ !$58-147 #disulfide_bonds #status experimental\ !$64,72,81,84 #binding_site zinc (His, His, His, Asp) #status !8experimental\ !$144 #active_site Arg #status experimental SUMMARY #length 154 #molecular-weight 15936 #checksum 8033 SEQUENCE /// ENTRY DSBOCZ #type complete TITLE superoxide dismutase (EC 1.15.1.1) (Cu-Zn) [validated] - bovine ALTERNATE_NAMES thymus hypocholesterolemic factor ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 24-Apr-1984 #sequence_revision 27-Feb-1997 #text_change 16-Jun-2000 ACCESSIONS I45883; S13674; A92163; A56902; A00513 REFERENCE I45883 !$#authors Hallewell, R.A.; Imlay, K.C.; Lee, P.; Fong, N.M.; Gallegos, !1C.; Getzoff, E.D.; Tainer, J.A.; Cabelli, D.E.; !1Tekamp-Olson, P.; Mullenbach, G.T.; Cousens, L.S. !$#journal Biochem. Biophys. Res. Commun. (1991) 181:474-480 !$#title Thermostabilization of recombinant human and bovine CuZu !1superoxide dismutases by replacement of free cysteines. !$#cross-references MUID:92068236; PMID:1958215 !$#accession I45883 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-152 ##label HAL !'##cross-references GB:M81129; NID:g162960; PIDN:AAA73164.1; !1PID:g162961 REFERENCE S13674 !$#authors Gibbs, L.S.; Shaffer, J.B. !$#journal Nucleic Acids Res. (1990) 18:7171 !$#title Nucleotide sequence of bovine copper/zinc superoxide !1dismutase cDNA generated by the polymerase chain reaction. !$#cross-references MUID:91088332; PMID:2263495 !$#accession S13674 !'##molecule_type mRNA !'##residues 2-152 ##label GIB !'##cross-references EMBL:X54799 !'##experimental_source lung REFERENCE A92163 !$#authors Steinman, H.M.; Naik, V.R.; Abernethy, J.L.; Hill, R.L. !$#journal J. Biol. Chem. (1974) 249:7326-7338 !$#title Bovine erythrocyte superoxide dismutase. Complete amino acid !1sequence. !$#cross-references MUID:75060425; PMID:4279916 !$#accession A92163 !'##molecule_type protein !'##residues 2-152 ##label STE REFERENCE A92164 !$#authors Abernethy, J.L.; Steinman, H.M.; Hill, R.L. !$#journal J. Biol. Chem. (1974) 249:7339-7347 !$#title Bovine erythrocyte superoxide dismutase. Subunit structure !1and sequence location of the intrasubunit disulfide bond. !$#cross-references MUID:75060426; PMID:4436313 !$#contents annotation; disulfide bond !$#note the molecule is a dimer of identical chains REFERENCE A93796 !$#authors Richardson, J.S.; Thomas, K.A.; Rubin, B.H.; Richardson, !1D.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1975) 72:1349-1353 !$#title Crystal structure of bovine Cu,Zn superoxide dismutase at 3 !1angstrom resolution: chain tracing and metal ligands. !$#cross-references MUID:75158289; PMID:1055410 !$#contents annotation; X-ray crystallography, 3.0 angstroms REFERENCE A50536 !$#authors Tainer, J.A.; Getzoff, E.D.; Richardson, J.S.; Richardson, !1D.C. !$#submission submitted to the Brookhaven Protein Data Bank, March 1980 !$#cross-references PDB:2SOD !$#contents annotation; X-ray crystallography, 2.0 angstroms, residues !11-151 REFERENCE A90436 !$#authors Malinowski, D.P.; Friedovich, I. !$#journal Biochemistry (1979) 18:5909-5917 !$#title Chemical modification of arginine at the active site of the !1bovine erythrocyte superoxide dismutase. !$#cross-references MUID:80088307; PMID:518876 !$#contents annotation; active site !$#note chemical modification of Arg-142 inactivates the enzyme REFERENCE A56902 !$#authors Mondola, P.; Santillo, M.; Belfiore, A.; Camardella, L.; !1Santangelo, F. !$#journal Comp. Biochem. Physiol. B (1993) 104:193-199 !$#title The thymus hypocholesterolemic factor (TphF): a bovine !1thymic superoxide dismutase active on HMG-CoA reductase. !$#cross-references MUID:93193420; PMID:8448990 !$#accession A56902 !'##molecule_type protein !'##residues 5-38;70-130;136-152 ##label MON !'##note sequence modified after extraction from NCBI backbone FUNCTION !$#description catalyzes the dismutation of 2 molecules of peroxide radical !1to dioxygen and hydrogen peroxide CLASSIFICATION #superfamily superoxide dismutase (Cu-Zn) KEYWORDS acetylated amino end; copper; homodimer; metalloprotein; !1oxidoreductase; zinc FEATURE !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental\ !$45,47,62,119 #binding_site copper (His) #status experimental\ !$56-145 #disulfide_bonds #status experimental\ !$62,70,79,82 #binding_site zinc (His, His, His, Asp) #status !8experimental\ !$142 #active_site Arg #status experimental SUMMARY #length 152 #molecular-weight 15682 #checksum 5279 SEQUENCE /// ENTRY DSPGCZ #type complete TITLE superoxide dismutase (EC 1.15.1.1) (Cu-Zn) [validated] - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 20-Apr-2000 ACCESSIONS A00514 REFERENCE A00514 !$#authors Schinina, M.E.; Barra, D.; Simmaco, M.; Bossa, F.; Rotilio, !1G. !$#journal FEBS Lett. (1985) 186:267-270 !$#title Primary structure of porcine Cu,Zn superoxide dismutase. !$#cross-references MUID:85231234; PMID:3891411 !$#accession A00514 !'##molecule_type protein !'##residues 1-152 ##label SCH FUNCTION !$#description catalyzes the dismutation of 2 molecules of peroxide radical !1to dioxygen and hydrogen peroxide CLASSIFICATION #superfamily superoxide dismutase (Cu-Zn) KEYWORDS acetylated amino end; copper; metalloprotein; !1oxidoreductase; zinc FEATURE !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$45,47,62,119 #binding_site copper (His) #status predicted\ !$56-145 #disulfide_bonds #status predicted\ !$62,70,79,82 #binding_site zinc (His, His, His, Asp) #status !8predicted\ !$142 #active_site Arg #status predicted SUMMARY #length 152 #molecular-weight 15761 #checksum 4791 SEQUENCE /// ENTRY DSHOCZ #type complete TITLE superoxide dismutase (EC 1.15.1.1) (Cu-Zn) 1 [validated] - horse ORGANISM #formal_name Equus caballus #common_name domestic horse DATE 02-Apr-1982 #sequence_revision 09-Aug-1997 #text_change 20-Apr-2000 ACCESSIONS JC5215; A00515 REFERENCE JC5215 !$#authors de la Rua-Domenech, R.; Wiedmann, M.; Mohammed, H.O.; !1Cummings, J.F.; Divers, T.J.; Batt, C.A. !$#journal Gene (1996) 178:83-88 !$#title Equine motor neuron disease is not linked to Cu/Zn !1superoxide dismutase mutations: Sequence analysis of the !1equine Cu/Zn superoxide dismutase cDNA. !$#cross-references MUID:97080551; PMID:8921896 !$#accession JC5215 !'##status preliminary !'##molecule_type mRNA !'##residues 1-154 ##label DEA !'##cross-references GB:U38956; NID:g1228115; PIDN:AAC48682.1; !1PID:g1228116 !'##experimental_source leukocyte REFERENCE A00515 !$#authors Lerch, K.; Ammer, D. !$#journal J. Biol. Chem. (1981) 256:11545-11551 !$#title Amino acid sequence of copper-zinc superoxide dismutase from !1horse liver. !$#cross-references MUID:82052979; PMID:7298616 !$#accession A00515 !'##molecule_type protein !'##residues 2-154 ##label LER GENETICS !$#gene sod1 FUNCTION !$#description catalyzes the dismutation of 2 molecules of peroxide radical !1to dioxygen and hydrogen peroxide CLASSIFICATION #superfamily superoxide dismutase (Cu-Zn) KEYWORDS acetylated amino end; copper; metalloprotein; !1oxidoreductase; zinc FEATURE !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental\ !$47,49,64,121 #binding_site copper (His) #status predicted\ !$58-147 #disulfide_bonds #status predicted\ !$64,72,81,84 #binding_site zinc (His, His, His, Asp) #status !8predicted\ !$144 #active_site Arg #status predicted SUMMARY #length 154 #molecular-weight 16071 #checksum 8351 SEQUENCE /// ENTRY S09568 #type complete TITLE superoxide dismutase (EC 1.15.1.1) (Cu-Zn) B - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 13-Jan-1995 #sequence_revision 11-Apr-1997 #text_change 11-Jun-1999 ACCESSIONS S09568; S05022; S59617 REFERENCE S09568 !$#authors Carri, M.T.; Battistoni, A.; Mariottini, P.; Rotilio, G. !$#journal Nucleic Acids Res. (1990) 18:1641 !$#title Xenopus laevis Cu,Zn superoxide dismutase B cDNA sequence. !$#cross-references MUID:90221905; PMID:2326205 !$#accession S09568 !'##molecule_type mRNA !'##residues 1-151 ##label CAR !'##cross-references EMBL:X51518; NID:g65258; PIDN:CAA35890.1; !1PID:g65259 REFERENCE S05021 !$#authors Schinina, M.E.; Barra, D.; Bossa, F.; Calabrese, L.; !1Montesano, L.; Carri, M.T.; Mariottini, P.; Amaldi, F.; !1Rotilio, G. !$#journal Arch. Biochem. Biophys. (1989) 272:507-515 !$#title Primary structure from amino acid and cDNA sequences of two !1Cu,Zn superoxide dismutase variants from Xenopus laevis. !$#cross-references MUID:89321563; PMID:2751312 !$#accession S05022 !'##molecule_type protein !'##residues 2-60,'P',62-151 ##label SCH !'##note residues 78-151 were also determined by cDNA sequencing !$#accession S59617 !'##status preliminary !'##molecule_type mRNA !'##residues 78-151 ##label SC2 FUNCTION !$#description catalyzes the dismutation of 2 molecules of peroxide radical !1to dioxygen and hydrogen peroxide CLASSIFICATION #superfamily superoxide dismutase (Cu-Zn) KEYWORDS copper; metalloprotein; oxidoreductase; zinc FEATURE !$45,47,62,118 #binding_site copper (His) #status predicted\ !$56-144 #disulfide_bonds #status predicted\ !$62,70,79,82 #binding_site zinc (His, His, His, Asp) #status !8predicted\ !$141 #active_site Arg #status predicted SUMMARY #length 151 #molecular-weight 15418 #checksum 1061 SEQUENCE /// ENTRY DSWFCZ #type complete TITLE superoxide dismutase (EC 1.15.1.1) (Cu-Zn) - swordfish ORGANISM #formal_name Xiphias gladius #common_name swordfish DATE 13-Aug-1986 #sequence_revision 13-Aug-1986 #text_change 05-Mar-1999 ACCESSIONS A00516 REFERENCE A00516 !$#authors Rocha, H.A.; Bannister, W.H.; Bannister, J.V. !$#journal Eur. J. Biochem. (1984) 145:477-484 !$#title The amino-acid sequence of copper/zinc superoxide dismutase !1from swordfish liver. !$#cross-references MUID:85076642; PMID:6510412 !$#accession A00516 !'##molecule_type protein !'##residues 1-151 ##label ROC FUNCTION !$#description catalyzes the dismutation of 2 molecules of peroxide radical !1to dioxygen and hydrogen peroxide CLASSIFICATION #superfamily superoxide dismutase (Cu-Zn) KEYWORDS copper; metalloprotein; oxidoreductase; zinc FEATURE !$46,48,63,119 #binding_site copper (His) #status predicted\ !$57-145 #disulfide_bonds #status predicted\ !$63,71,80,83 #binding_site zinc (His, His, His, Asp) #status !8predicted\ !$142 #active_site Arg #status predicted SUMMARY #length 151 #molecular-weight 15517 #checksum 9781 SEQUENCE /// ENTRY DSFFCZ #type complete TITLE superoxide dismutase (EC 1.15.1.1) (Cu-Zn) [validated] - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 28-Aug-1985 #sequence_revision 31-Mar-1989 #text_change 20-Apr-2000 ACCESSIONS S02725; S06326; S09184; A27861; PS0082; S08648; A00517 REFERENCE S02725 !$#authors Kwiatowski, J.; Patel, M.; Ayala, F.J. !$#journal Nucleic Acids Res. (1989) 17:1264 !$#title Drosophila melanogaster Cu, Zn superoxide dismutase gene !1sequence. !$#cross-references MUID:89160267; PMID:2493630 !$#accession S02725 !'##molecule_type DNA !'##residues 1-153 ##label KWI !'##cross-references EMBL:X13780; NID:g8644; PIDN:CAA32028.1; PID:g8645 REFERENCE S06326 !$#authors Seto, N.O.L.; Hayashi, S.; Tener, G.M. !$#journal Nucleic Acids Res. (1987) 15:10601 !$#title The sequence of the Cu-Zn superoxide dismutase gene of !1Drosophila. !$#cross-references MUID:88096604; PMID:3122185 !$#accession S06326 !'##molecule_type DNA !'##residues 1-153 ##label SET !'##cross-references GB:Z19591; NID:g7792; PIDN:CAA79639.1; PID:g7793 REFERENCE S09184 !$#authors Lee, Y.M.; Friedman, D.J.; Ayala, F.J. !$#journal Arch. Biochem. Biophys. (1985) 241:577-589 !$#title Complete amino acid sequence of copper-zinc superoxide !1dismutase from Drosophila melanogaster. !$#cross-references MUID:85305751; PMID:3929689 !$#accession S09184 !'##molecule_type protein !'##residues 2-152 ##label LEE REFERENCE A27861 !$#authors Seto, N.O.L.; Hayashi, S.; Tener, G.M. !$#journal Nucleic Acids Res. (1987) 15:5483 !$#title Drosophila Cu-Zn superoxide dismutase cDNA sequence. !$#cross-references MUID:87260017; PMID:3110743 !$#accession A27861 !'##molecule_type mRNA !'##residues 1-153 ##label SE2 !'##cross-references GB:Y00367; NID:g8642; PIDN:CAA68443.1; PID:g8643 REFERENCE PS0082 !$#authors Kirkland, K.C.; Phillips, J.P. !$#journal Gene (1987) 61:415-419 !$#title Isolation and chromosomal localization of genomic DNA !1sequences coding for cytoplasmic superoxide dismutase from !1Drosophila melanogaster. !$#cross-references MUID:88185843; PMID:3128462 !$#accession PS0082 !'##molecule_type DNA !'##residues 91-96,'K',98-122 ##label KIR !'##cross-references GB:M18823; NID:g158472; PIDN:AAA28905.1; !1PID:g552135 !'##experimental_source strain canton-S !'##note the sequence difference is thought to be due to different !1strains REFERENCE S08648 !$#authors Phillips, J.P. !$#submission submitted to the EMBL Data Library, December 1989 !$#accession S08648 !'##molecule_type DNA !'##residues 1-96,'K',98-153 ##label PHI !'##cross-references EMBL:X17332; NID:g8646; PIDN:CAA35210.1; PID:g8647 GENETICS !$#gene cSOD !'##cross-references FlyBase:FBgn0003462 !$#map_position 3L 68A8-9 !$#introns 22/3 FUNCTION !$#description catalyzes the dismutation of 2 molecules of peroxide radical !1to dioxygen and hydrogen peroxide CLASSIFICATION #superfamily superoxide dismutase (Cu-Zn) KEYWORDS copper; homodimer; metalloprotein; oxidoreductase; zinc FEATURE !$2-152 #product superoxide dismutase (Cu-Zn) #status !8experimental #label MAT\ !$45,47,62,119 #binding_site copper (His) #status predicted\ !$56-145 #disulfide_bonds #status predicted\ !$62,70,79,82 #binding_site zinc (His, His, His, Asp) #status !8predicted\ !$142 #active_site Arg #status predicted SUMMARY #length 153 #molecular-weight 15699 #checksum 4726 SEQUENCE /// ENTRY DSNVAC #type complete TITLE superoxide dismutase (EC 1.15.1.1) (Cu-Zn) - Autographa californica nuclear polyhedrosis virus ORGANISM #formal_name Autographa californica nuclear polyhedrosis virus, AcMNPV DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 20-Apr-2000 ACCESSIONS A40564; G72853 REFERENCE A40564 !$#authors Tomalski, M.D.; Eldridge, R.; Miller, L.K. !$#journal Virology (1991) 184:149-161 !$#title A baculovirus homolog of a Cu/Zn superoxide dismutase gene. !$#cross-references MUID:91335744; PMID:1871962 !$#accession A40564 !'##molecule_type DNA !'##residues 1-151 ##label TOM !'##cross-references GB:M68862; NID:g332485; PIDN:AAA46746.1; !1PID:g332486 !'##experimental_source strain L1 REFERENCE A72850 !$#authors Ayres, M.D.; Howard, S.C.; Kuzio, J.; Lopez-Ferber, M.; !1Possee, R.D. !$#journal Virology (1994) 202:586-605 !$#title The complete DNA sequence of Autographa californica nuclear !1polyhedrosis virus. !$#cross-references MUID:94303173; PMID:8030224 !$#accession G72853 !'##status preliminary !'##molecule_type DNA !'##residues 1-151 ##label AYR !'##cross-references GB:L22858; NID:g510708; PIDN:AAA66661.1; !1PID:g559100 GENETICS !$#gene Ac-sod FUNCTION !$#description catalyzes the dismutation of 2 molecules of peroxide radical !1to dioxygen and hydrogen peroxide CLASSIFICATION #superfamily superoxide dismutase (Cu-Zn) KEYWORDS copper; metalloprotein; oxidoreductase; zinc FEATURE !$43,45,60,118 #binding_site copper (His) #status predicted\ !$54-144 #disulfide_bonds #status predicted\ !$60,68,77,80 #binding_site zinc (His, His, His, Asp) #status !8predicted\ !$141 #active_site Arg #status predicted SUMMARY #length 151 #molecular-weight 16182 #checksum 4639 SEQUENCE /// ENTRY DSBYC #type complete TITLE superoxide dismutase (EC 1.15.1.1) (Cu-Zn) [validated] - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein J1968; protein YJR104c ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Jan-1980 #sequence_revision 30-Sep-1992 #text_change 21-Jul-2000 ACCESSIONS A36171; A00518; A92281; S57125; A40093 REFERENCE A36171 !$#authors Bermingham-McDonogh, O.; Gralla, E.B.; Valentine, J.S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:4789-4793 !$#title The copper, zinc-superoxide dismutase gene of Saccharomyces !1cerevisiae: cloning, sequencing, and biological activity. !$#cross-references MUID:88263032; PMID:3290902 !$#accession A36171 !'##molecule_type DNA !'##residues 1-154 ##label BER !'##cross-references EMBL:J03279; NID:g171341; PIDN:AAA34543.1; !1PID:g171342 REFERENCE A90760 !$#authors Johansen, J.T.; Overballe-Petersen, C.; Martin, B.; !1Hasemann, V.; Svendsen, I. !$#journal Carlsberg Res. Commun. (1979) 44:201-217 !$#title The complete amino acid sequence of copper, zinc superoxide !1dismutase from Saccharomyces cerevisiae. !$#accession A00518 !'##molecule_type protein !'##residues 2-154 ##label JOH REFERENCE A92281 !$#authors Steinman, H.M. !$#journal J. Biol. Chem. (1980) 255:6758-6765 !$#title The amino acid sequence of copper-zinc superoxide dismutase !1from Saccharomyces cerevisiae. !$#cross-references MUID:80227835; PMID:6993479 !$#accession A92281 !'##molecule_type protein !'##residues 2-55,'D',57-92,'D',94-154 ##label STE REFERENCE S57111 !$#authors Ramezani Rad, M.; Kirchrath, L.; Hollenberg, C.P. !$#submission submitted to the Protein Sequence Database, September 1995 !$#accession S57125 !'##molecule_type DNA !'##residues 1-154 ##label RAM !'##cross-references EMBL:Z49604; NID:g1015811; PIDN:CAA89634.1; !1PID:g1015812; GSPDB:GN00010; MIPS:YJR104c REFERENCE A40093 !$#authors Horiuchi, S. !$#submission submitted to the Protein Sequence Database, March 1992 !$#accession A40093 !'##molecule_type protein !'##residues 2-7,'KL',10-42,'L',44-55,'D',57-88,'L',90-91,'AD',94-100, !1'Q',102,'K',104-107,'F',109,'VN',112-151,'I' ##label HOR GENETICS !$#gene SGD:SOD1; MIPS:YJR104c !'##cross-references SGD:S0003865; MIPS:YJR104c !$#map_position 10R FUNCTION !$#description catalyzes the dismutation of 2 molecules of peroxide radical !1to dioxygen and hydrogen peroxide CLASSIFICATION #superfamily superoxide dismutase (Cu-Zn) KEYWORDS copper; metalloprotein; oxidoreductase; zinc FEATURE !$2-154 #product superoxide dismutase (Cu-Zn) #status !8experimental #label MAT\ !$47,49,64,121 #binding_site copper (His) #status predicted\ !$58-147 #disulfide_bonds #status experimental\ !$64,72,81,84 #binding_site zinc (His, His, His, Asp) #status !8predicted\ !$144 #active_site Arg #status predicted SUMMARY #length 154 #molecular-weight 15855 #checksum 1414 SEQUENCE /// ENTRY DSSPCZ #type complete TITLE superoxide dismutase (EC 1.15.1.1) (Cu-Zn) precursor, chloroplast [validated] - spinach ORGANISM #formal_name Spinacia oleracea #common_name spinach DATE 30-Sep-1988 #sequence_revision 03-Feb-1994 #text_change 20-Apr-2000 ACCESSIONS JQ0940; JS0011 REFERENCE JQ0940 !$#authors Sakamoto, A.; Ohsuga, H.; Wakaura, M.; Mitsukawa, N.; !1Hibino, T.; Masumura, T.; Sasaki, Y.; Tanaka, K. !$#submission submitted to JIPID, June 1991 !$#accession JQ0940 !'##molecule_type mRNA !'##residues 1-222 ##label SAK !'##experimental_source cv. King of Denmark REFERENCE A92001 !$#authors Kitagawa, Y.; Tsunasawa, S.; Tanaka, N.; Katsube, Y.; !1Sakiyama, F.; Asada, K. !$#journal J. Biochem. (1986) 99:1289-1298 !$#title Amino acid sequence of copper,zinc-superoxide dismutase from !1spinach leaves. !$#cross-references MUID:86223926; PMID:3519601 !$#accession JS0011 !'##molecule_type protein !'##residues 69-222 ##label KIT REFERENCE A49492 !$#authors Kitagawa, Y.; Tanaka, N.; Hata, Y.; Kusunoki, M.; Lee, G.; !1Katsube, Y.; Asada, K.; Aibara, S.; Morita, Y. !$#journal J. Biochem. (1991) 109:477-485 !$#title Three-dimensional structure of Cu,Zn-superoxide dismutase !1from spinach at 2.0 angstrom resolution. !$#cross-references MUID:91349191; PMID:1880134 !$#contents annotation; X-ray crystallography, 2.0 angstroms, residues !169-222 REFERENCE A51980 !$#authors Kitagawa, Y.; Katsube, Y. !$#submission submitted to the Brookhaven Protein Data Bank, April 1993 !$#cross-references PDB:1SRD !$#contents annotation; X-ray crystallography, 2.0 angstroms, residues !169-222 FUNCTION !$#description catalyzes the dismutation of 2 molecules of peroxide radical !1to dioxygen and hydrogen peroxide CLASSIFICATION #superfamily superoxide dismutase (Cu-Zn) KEYWORDS chloroplast; copper; homodimer; metalloprotein; !1oxidoreductase; zinc FEATURE !$1-68 #domain transit peptide (chloroplast) #status !8predicted #label TRP\ !$69-222 #product superoxide dismutase (Cu-Zn) #status !8experimental #label MAT\ !$114,116,131,188 #binding_site copper (His) #status experimental\ !$125-214 #disulfide_bonds #status experimental\ !$131,139,148,151 #binding_site zinc (His, His, His, Asp) #status !8experimental\ !$211 #active_site Arg #status predicted SUMMARY #length 222 #molecular-weight 22567 #checksum 1283 SEQUENCE /// ENTRY DSSPCY #type complete TITLE superoxide dismutase (EC 1.15.1.1) (Cu-Zn) I, cytosolic [validated] - spinach ORGANISM #formal_name Spinacia oleracea #common_name spinach DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 20-Apr-2000 ACCESSIONS S12595; S29148; C61531 REFERENCE S12595 !$#authors Sakamoto, A.; Ohsuga, H.; Wakaura, M.; Mitsukawa, N.; !1Hibino, T.; Masumura, T.; Sasaki, Y.; Tanaka, K. !$#journal Nucleic Acids Res. (1990) 18:4923 !$#title Nucleotide sequence of cDNA for the cytosolic Cu/ !1Zn-superoxide dismutase from spinach (Spinacia oleracea L.). !$#cross-references MUID:90370486; PMID:2395656 !$#accession S12595 !'##molecule_type mRNA !'##residues 1-152 ##label SAK !'##cross-references EMBL:X53872; NID:g21339; PIDN:CAA37866.1; !1PID:g21340 REFERENCE S29146 !$#authors Kanematsu, S.; Asada, K. !$#journal Plant Cell Physiol. (1990) 31:99-112 !$#title Characteristic amino acid sequences of chloroplast and !1cytosol isozymes of CuZn-superoxide dismutase in spinach, !1rice and horsetail. !$#accession S29148 !'##molecule_type protein !'##residues 2-51,'X',53,'X',55,'X',57;150-152 ##label KAN REFERENCE A61531 !$#authors Kanematsu, S.; Asada, K. !$#journal Free Radic. Res. Commun. (1991) 12:383-390 !$#title Chloroplast and cytosol isozymes of CuZn-superoxide !1dismutase: their characteristic amino acid sequences. !$#accession C61531 !'##molecule_type protein !'##residues 2-51,'X',53,'X',55,'X',57;'LQ',60 ##label KA2 FUNCTION !$#description catalyzes the dismutation of 2 molecules of peroxide radical !1to dioxygen and hydrogen peroxide CLASSIFICATION #superfamily superoxide dismutase (Cu-Zn) KEYWORDS copper; cytosol; metalloprotein; oxidoreductase; zinc FEATURE !$2-152 #product superoxide dismutase (Cu-Zn), cytosolic !8#status experimental #label MAT\ !$45,47,62,119 #binding_site copper (His) #status predicted\ !$56-145 #disulfide_bonds #status predicted\ !$62,70,79,82 #binding_site zinc (His, His, His, Asp) #status !8predicted\ !$142 #active_site Arg #status predicted SUMMARY #length 152 #molecular-weight 15223 #checksum 6155 SEQUENCE /// ENTRY DSMUZ #type complete TITLE superoxide dismutase (EC 1.15.1.1) (Cu-Zn) - Arabidopsis thaliana ALTERNATE_NAMES protein F22O13.34 ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 11-Jun-1999 ACCESSIONS S19117; T00739; PT0086; S16032 REFERENCE S19117 !$#authors Hindges, R.; Slusarenko, A. !$#journal Plant Mol. Biol. (1992) 18:123-125 !$#title cDNA and derived amino acid sequence of a cytosolic Cu,Zn !1superoxide dismutase from Arabidopsis thaliana (L.) Heyhn. !$#cross-references MUID:92119218; PMID:1731963 !$#accession S19117 !'##molecule_type mRNA !'##residues 1-152 ##label HIN !'##cross-references EMBL:X60935; NID:g16249; PIDN:CAA43270.1; !1PID:g16250 REFERENCE Z14200 !$#authors Shinn, P.; Buehler, E.; Dewar, K.; Feng, J.; Kim, C.; Li, !1Y.; Sun, H.; Conway, A.; Conway, A.; Kurtz, D.; Oji, O.; !1Shen, Y.K.; Toriumi, M.; Vysotskaia, V.; Yu, G.; Davis, !1R.W.; Federspiel, N.A.; Theologis, A.; Ecker, J.R. !$#submission submitted to the EMBL Data Library, April 1998 !$#description Genomic sequence for Arabidopsis thaliana BAC F22O13. !$#accession T00739 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 'MLCRTICFFLDLYLFVYVLVYVYVFTDHKGQVT',1-152 ##label SHI !'##cross-references EMBL:AC003981; NID:g3063438; PIDN:AAC14060.1; !1PID:g3063472 REFERENCE PN0173 !$#authors Tsugita, A.; Kamo, M.; Kawakami, M.; Ohki, Y. !$#submission submitted to JIPID, December 1995 !$#description Two dimensional electrophoresis of plant proteins and !1standardization of the gel patterns. !$#accession PT0086 !'##molecule_type protein !'##residues 'ATX',3,'A',5-8,'KGTSK',14,'E' ##label TSU !'##experimental_source leaf GENETICS !$#map_position I !$#introns 26/1; 60/1; 92/1; 102/3; 128/1; 146/1 FUNCTION !$#description catalyzes the dismutation of 2 molecules of peroxide radical !1to dioxygen and hydrogen peroxide CLASSIFICATION #superfamily superoxide dismutase (Cu-Zn) KEYWORDS copper; metalloprotein; oxidoreductase; zinc FEATURE !$45,47,62,119 #binding_site copper (His) #status predicted\ !$56-145 #disulfide_bonds #status predicted\ !$62,70,79,82 #binding_site zinc (His, His, His, Asp) #status !8predicted\ !$142 #active_site Arg #status predicted SUMMARY #length 152 #molecular-weight 15098 #checksum 5233 SEQUENCE /// ENTRY DSRPZC #type complete TITLE superoxide dismutase (EC 1.15.1.1) (Cu-Zn) - cabbage ORGANISM #formal_name Brassica oleracea var. capitata #common_name cabbage DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 05-Mar-1999 ACCESSIONS A25569 REFERENCE A25569 !$#authors Steffens, G.J.; Michelson, A.M.; Oetting, F.; Puget, K.; !1Strassburger, W.; Flohe, L. !$#journal Biol. Chem. Hoppe-Seyler (1986) 367:1007-1016 !$#title Primary structure of Cu-Zn superoxide dismutase of Brassica !1oleracea proves homology with corresponding enzymes of !1animals, fungi and prokaryotes. !$#cross-references MUID:87076036; PMID:3790249 !$#accession A25569 !'##molecule_type protein !'##residues 1-151 ##label STE COMPLEX homodimer FUNCTION !$#description catalyzes the dismutation of 2 molecules of peroxide radical !1to dioxygen and hydrogen peroxide CLASSIFICATION #superfamily superoxide dismutase (Cu-Zn) KEYWORDS copper; metalloprotein; oxidoreductase; zinc FEATURE !$44,46,61,118 #binding_site copper (His) #status predicted\ !$55-144 #disulfide_bonds #status predicted\ !$61,69,78,81 #binding_site zinc (His, His, His, Asp) #status !8predicted\ !$141 #active_site Arg #status predicted SUMMARY #length 151 #molecular-weight 15040 #checksum 2262 SEQUENCE /// ENTRY DSPMCZ #type complete TITLE superoxide dismutase (EC 1.15.1.1) (Cu-Zn) precursor, chloroplast - garden pea ALTERNATE_NAMES superoxide dismutase (Cu-Zn) II ORGANISM #formal_name Pisum sativum #common_name garden pea DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 11-Jun-1999 ACCESSIONS A30204; S12313 REFERENCE A30204 !$#authors Scioli, J.R.; Zilinskas, B.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:7661-7665 !$#title Cloning and characterization of a cDNA encoding the !1chloroplastic copper/zinc-superoxide dismutase from pea. !$#cross-references MUID:89017257; PMID:2845417 !$#accession A30204 !'##molecule_type mRNA !'##residues 1-202 ##label SCI !'##cross-references GB:J04087; NID:g169159; PIDN:AAA33688.1; !1PID:g169160 !'##note the authors translated the codon TCT for residue 55 as Ala and !1CAG for residue 151 as Glu REFERENCE S12313 !$#authors Isin, S.H.; Burke, J.J.; Allen, R.D. !$#journal Plant Mol. Biol. (1990) 15:789-791 !$#title Sequence divergence of pea Cu/Zn superoxide dismutase II !1cDNAs. !$#cross-references MUID:91346717; PMID:2102887 !$#accession S12313 !'##molecule_type mRNA !'##residues 1-54,'A',56-202 ##label ISI !'##cross-references EMBL:X56435; NID:g20899; PIDN:CAA39819.1; !1PID:g20900 GENETICS !$#gene SOD9 FUNCTION !$#description catalyzes the dismutation of 2 molecules of peroxide radical !1to dioxygen and hydrogen peroxide CLASSIFICATION #superfamily superoxide dismutase (Cu-Zn) KEYWORDS chloroplast; copper; metalloprotein; oxidoreductase; zinc FEATURE !$1-48 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$49-202 #product superoxide dismutase (Cu-Zn) #status !8predicted #label MAT\ !$94,96,111,168 #binding_site copper (His) #status predicted\ !$105-194 #disulfide_bonds #status predicted\ !$111,119,128,131 #binding_site zinc (His, His, His, Asp) #status !8predicted\ !$191 #active_site Arg #status predicted SUMMARY #length 202 #molecular-weight 20626 #checksum 8275 SEQUENCE /// ENTRY DSVZCR #type complete TITLE superoxide dismutase (Cu-Zn) related protein SalF8R - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jun-2000 ACCESSIONS F40897; JQ1783 REFERENCE A40897 !$#authors Blasco, R.; Cole, N.B.; Moss, B. !$#journal J. Virol. (1991) 65:4598-4608 !$#title Sequence analysis, expression, and deletion of a vaccinia !1virus gene encoding a homolog of profilin, a eukaryotic !1actin-binding protein. !$#cross-references MUID:91332999; PMID:1870190 !$#accession F40897 !'##molecule_type DNA !'##residues 1-125 ##label BLA !'##cross-references GB:M72474; NID:g335761; PIDN:AAA48312.1; !1PID:g335767 REFERENCE JQ1767 !$#authors Smith, G.L.; Chan, Y.S.; Howard, S.T. !$#journal J. Gen. Virol. (1991) 72:1349-1376 !$#title Nucleotide sequence of 42kbp of vaccinia virus strain WR !1from near the right inverted terminal repeat. !$#cross-references MUID:91259063; PMID:2045793 !$#accession JQ1783 !'##molecule_type DNA !'##residues 1-125 ##label SMI !'##cross-references DDBJ:D11079; NID:g222717; PIDN:BAA01819.1; !1PID:g222734 COMMENT This protein does not have the characteristic metal binding !1sites necessary for enzyme activity. CLASSIFICATION #superfamily superoxide dismutase (Cu-Zn) KEYWORDS metalloprotein FEATURE !$52-102 #disulfide_bonds #status predicted SUMMARY #length 125 #molecular-weight 13663 #checksum 7152 SEQUENCE /// ENTRY DSFOCL #type complete TITLE superoxide dismutase (EC 1.15.1.1) (Cu-Zn) precursor - Photobacterium leiognathi ORGANISM #formal_name Photobacterium leiognathi DATE 03-Aug-1984 #sequence_revision 12-Apr-1996 #text_change 11-Jun-1999 ACCESSIONS A26689; A00519 REFERENCE A26689 !$#authors Steinman, H.M. !$#journal J. Biol. Chem. (1987) 262:1882-1887 !$#title Bacteriocuprein superoxide dismutase of Photobacterium !1leiognathi. Isolation and sequence of the gene and evidence !1for a precursor form. !$#cross-references MUID:87109348; PMID:3805055 !$#accession A26689 !'##molecule_type DNA !'##residues 1-173 ##label STE !'##cross-references GB:J02658; NID:g150710; PIDN:AAA25632.1; !1PID:g150711 REFERENCE A00519 !$#authors Steffens, G.J.; Bannister, J.V.; Bannister, W.H.; Flohe, L.; !1Gunzler, W.A.; Kim, S.M.A.; Otting, F. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1983) 364:675-690 !$#title The primary structure of Cu-Zn superoxide dismutase from !1Photobacterium leiognathi: evidence for a separate evolution !1of Cu-Zn superoxide dismutase in bacteria. !$#cross-references MUID:83289129; PMID:6884993 !$#accession A00519 !'##molecule_type protein !'##residues 23-173 ##label ST2 FUNCTION !$#description catalyzes the dismutation of 2 molecules of peroxide radical !1to dioxygen and hydrogen peroxide CLASSIFICATION #superfamily superoxide dismutase (Cu-Zn) KEYWORDS copper; metalloprotein; oxidoreductase; zinc FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-173 #product superoxide dismutase (Cu-Zn) #status !8predicted #label MAT\ !$67,69,92,147 #binding_site copper (His) #status predicted\ !$74-169 #disulfide_bonds #status predicted\ !$92,101,110,113 #binding_site zinc (His, His, His, Asp) #status !8predicted\ !$166 #active_site Arg #status predicted SUMMARY #length 173 #molecular-weight 18109 #checksum 2213 SEQUENCE /// ENTRY A41654 #type complete TITLE superoxide dismutase (EC 1.15.1.1) (Cu-Zn) precursor - Haemophilus influenzae ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A41654 REFERENCE A41654 !$#authors Kroll, J.S.; Langford, P.R.; Loynds, B.M. !$#journal J. Bacteriol. (1991) 173:7449-7457 !$#title Copper-zinc superoxide dismutase of Haemophilus influenzae !1and Haemophilus parainfluenzae. !$#cross-references MUID:92041655; PMID:1938942 !$#accession A41654 !'##status preliminary !'##molecule_type DNA !'##residues 1-187 ##label KRO !'##cross-references GB:M84012; NID:g148881; PIDN:AAA24953.1; !1PID:g148882 GENETICS !$#gene sodC FUNCTION !$#description catalyzes the dismutation of 2 molecules of peroxide radical !1to dioxygen and hydrogen peroxide CLASSIFICATION #superfamily superoxide dismutase (Cu-Zn) KEYWORDS copper; metalloprotein; oxidoreductase; zinc FEATURE !$1-35 #domain signal sequence #status predicted #label SIG\ !$36-187 #product superoxide dismutase (Cu-Zn) #status !8predicted #label MAT\ !$87-183 #disulfide_bonds #status predicted\ !$105,114,123,126 #binding_site zinc (His, His, His, Asp) #status !8predicted\ !$180 #active_site Arg #status predicted SUMMARY #length 187 #molecular-weight 19536 #checksum 584 SEQUENCE /// ENTRY B41654 #type complete TITLE superoxide dismutase (EC 1.15.1.1) (Cu-Zn) precursor - Haemophilus parainfluenzae ORGANISM #formal_name Haemophilus parainfluenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B41654 REFERENCE A41654 !$#authors Kroll, J.S.; Langford, P.R.; Loynds, B.M. !$#journal J. Bacteriol. (1991) 173:7449-7457 !$#title Copper-zinc superoxide dismutase of Haemophilus influenzae !1and Haemophilus parainfluenzae. !$#cross-references MUID:92041655; PMID:1938942 !$#accession B41654 !'##status preliminary !'##molecule_type DNA !'##residues 1-187 ##label KRO !'##cross-references GB:M84013; NID:g148883; PIDN:AAA24954.1; !1PID:g148884 FUNCTION !$#description catalyzes the dismutation of 2 molecules of peroxide radical !1to dioxygen and hydrogen peroxide CLASSIFICATION #superfamily superoxide dismutase (Cu-Zn) KEYWORDS copper; metalloprotein; oxidoreductase; zinc FEATURE !$1-35 #domain signal sequence #status predicted #label SIG\ !$36-187 #product superoxide dismutase (Cu-Zn) #status !8predicted #label MAT\ !$80,82,105,161 #binding_site copper (His) #status predicted\ !$87-183 #disulfide_bonds #status predicted\ !$180 #active_site Arg #status predicted SUMMARY #length 187 #molecular-weight 19510 #checksum 1153 SEQUENCE /// ENTRY A33893 #type complete TITLE superoxide dismutase (EC 1.15.1.1) (Cu-Zn) - Brucella abortus ORGANISM #formal_name Brucella abortus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A33893 REFERENCE A33893 !$#authors Beck, B.L.; Tabatabai, L.B.; Mayfield, J.E. !$#journal Biochemistry (1990) 29:372-376 !$#title A protein isolated from Brucella abortus is a Cu-Zn !1superoxide dismutase. !$#cross-references MUID:90148961; PMID:2105741 !$#accession A33893 !'##molecule_type protein !'##residues 1-154 ##label BEC FUNCTION !$#description catalyzes the dismutation of 2 molecules of peroxide radical !1to dioxygen and hydrogen peroxide CLASSIFICATION #superfamily superoxide dismutase (Cu-Zn) KEYWORDS copper; metalloprotein; oxidoreductase; zinc FEATURE !$48,50,73,128 #binding_site copper (His) #status predicted\ !$55-150 #disulfide_bonds #status predicted\ !$147 #active_site Arg #status predicted SUMMARY #length 154 #molecular-weight 16072 #checksum 155 SEQUENCE /// ENTRY DSHUEC #type complete TITLE superoxide dismutase (EC 1.15.1.1) (Cu-Zn) precursor, extracellular - human ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 20-Apr-2000 ACCESSIONS A28301; A54656; I55405 REFERENCE A28301 !$#authors Hjalmarsson, K.; Marklund, S.L.; Engstroem, A.; Edlund, T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:6340-6344 !$#title Isolation and sequence of complementary DNA encoding human !1extracellular superoxide dismutase. !$#cross-references MUID:87317647; PMID:3476950 !$#accession A28301 !'##molecule_type mRNA !'##residues 1-240 ##label HJA !'##cross-references GB:J02947; NID:g338283; PIDN:AAA66000.1; !1PID:g338284 REFERENCE A54656 !$#authors Folz, R.J.; Crapo, J.D. !$#journal Genomics (1994) 22:162-171 !$#title Extracellular superoxide dismutase (SOD3): tissue-specific !1expression, genomic characterization, and computer-asisted !1sequence analysis of the human EC SOD gene. !$#cross-references MUID:95048365; PMID:7959763 !$#accession A54656 !'##molecule_type DNA !'##residues 1-39 ##label FOL !'##cross-references GB:U10116 REFERENCE I55405 !$#authors Sandstrom, J.; Nilsson, P.; Karlsson, K.; Marklund, S.L. !$#journal J. Biol. Chem. (1994) 269:19163-19166 !$#title 10-fold increase in human plasma extracellular superoxide !1dismutase content caused by a mutation in heparin-binding !1domain. !$#cross-references MUID:94308185; PMID:8034674 !$#accession I55405 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 195-230,'G',232-240 ##label RES !'##cross-references GB:S71544; NID:g565135; PIDN:AAB31336.1; !1PID:g565136 !'##note mutant sequence GENETICS !$#gene GDB:SOD3 !'##cross-references GDB:125291; OMIM:185490 !$#map_position 4p16.3-4q21 !$#introns #status absent !$#note the two introns occur before the initiator codon COMPLEX homotetramer FUNCTION !$#description catalyzes the dismutation of 2 molecules of peroxide radical !1to dioxygen and hydrogen peroxide CLASSIFICATION #superfamily superoxide dismutase (Cu-Zn) KEYWORDS copper; glycoprotein; metalloprotein; oxidoreductase; zinc FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-240 #product superoxide dismutase (Cu-Zn), extracellular !8#status predicted #label MAT\ !$107 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$114,116,131,181 #binding_site copper (His) #status predicted\ !$125-208 #disulfide_bonds #status predicted\ !$131,139,142,145 #binding_site zinc (His, His, His, Asp) #status !8predicted\ !$204 #active_site Arg #status predicted SUMMARY #length 240 #molecular-weight 25881 #checksum 4183 SEQUENCE /// ENTRY DSHUN #type complete TITLE superoxide dismutase (EC 1.15.1.1) (Mn) precursor [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 04-Dec-1986 #sequence_revision 06-Feb-1995 #text_change 20-Apr-2000 ACCESSIONS S13162; S02272; S11756; S00356; S02230; S00663; A92447; !1I38033; A00520; A27297 REFERENCE S13162 !$#authors Church, S.L. !$#journal Biochim. Biophys. Acta (1990) 1087:250-252 !$#title Manganese superoxide dismutase: nucleotide and deduced amino !1acid sequence of a cDNA encoding a new human transcript. !$#cross-references MUID:91027939; PMID:1699607 !$#accession S13162 !'##molecule_type mRNA !'##residues 1-222 ##label CHU !'##note cross-reference GB:M34665 cited in paper is not correct REFERENCE S02272 !$#authors Wispe, J.R.; Clark, J.C.; Burhans, M.S.; Kropp, K.E.; !1Korfhagen, T.R.; Whitsett, J.A. !$#journal Biochim. Biophys. Acta (1989) 994:30-36 !$#title Synthesis and processing of the precursor for human !1mangano-superoxide dismutase. !$#cross-references MUID:89076921; PMID:2462451 !$#accession S02272 !'##molecule_type mRNA !'##residues 1-81,'T',83-222 ##label WIS !'##cross-references EMBL:X14322; NID:g34706; PIDN:CAA32502.1; !1PID:g34707 REFERENCE S11756 !$#authors StClair, D.K. !$#submission submitted to the EMBL Data Library, April 1989 !$#description Nucleotide sequence of a human tumor MnSOD cDNA. !$#accession S11756 !'##molecule_type mRNA !'##residues 1-64,'N',66-222 ##label EMB !'##cross-references EMBL:X15132; NID:g34794; PIDN:CAA33228.1; !1PID:g34795 REFERENCE S00356 !$#authors Ho, Y.S.; Crapo, J.D. !$#journal FEBS Lett. (1988) 229:256-260 !$#title Isolation and characterization of complementary DNAs !1encoding human manganese-containing superoxide dismutase. !$#cross-references MUID:88152250; PMID:2831093 !$#accession S00356 !'##molecule_type mRNA !'##residues 1-81,'T',83-222 ##label HO1 !'##cross-references EMBL:Y00985; NID:g36536; PIDN:CAA68791.1; !1PID:g36537 REFERENCE S02230 !$#authors Heckl, K. !$#journal Nucleic Acids Res. (1988) 16:6224 !$#title Isolation of cDNAs encoding human manganese superoxide !1dismutase. !$#cross-references MUID:88289364; PMID:3399391 !$#accession S02230 !'##molecule_type mRNA !'##residues 1-13,'P',15,'V',17-122,'L',124-222 ##label HEC !'##cross-references EMBL:X07834; NID:g36517; PIDN:CAA30687.1; !1PID:g36518 !'##note the authors translated the codon CTG for residue 123 as Arg REFERENCE S00663 !$#authors Beck, Y.; Oren, R.; Amit, B.; Levanon, A.; Gorecki, M.; !1Hartman, J.R. !$#journal Nucleic Acids Res. (1987) 15:9076 !$#title Human Mn superoxide dismutase cDNA sequence. !$#cross-references MUID:88067716; PMID:3684581 !$#accession S00663 !'##molecule_type mRNA !'##residues 1-154,'Q',156-222 ##label BEC !'##cross-references EMBL:Y00472; NID:g34710; PIDN:CAA68533.1; !1PID:g34711 REFERENCE A92447 !$#authors Barra, D.; Schinina, M.E.; Simmaco, M.; Bannister, J.V.; !1Bannister, W.H.; Rotilio, G.; Bossa, F. !$#journal J. Biol. Chem. (1984) 259:12595-12601 !$#title The primary structure of human liver manganese superoxide !1dismutase. !$#cross-references MUID:85030346; PMID:6386798 !$#accession A92447 !'##molecule_type protein !'##residues 25-65,'Q',67-111,'Q',113-132,'Q',134-147,150-154,'Q', !1156-222 ##label BAR REFERENCE I38033 !$#authors St Clair, D.K.; Holland, J.C. !$#journal Cancer Res. (1991) 51:939-943 !$#title Complementary DNA encoding human colon cancer manganese !1superoxide dismutase and the expression of its gene in human !1cells. !$#cross-references MUID:91105727; PMID:1988135 !$#accession I38033 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-64,'N',66-222 ##label RES !'##cross-references EMBL:X59445; NID:g34708; PIDN:CAA42066.1; !1PID:g34709 REFERENCE A43483 !$#authors Borgstahl, G.E.O.; Parge, H.E.; Hickey, M.J.; Beyer Jr., !1W.F.; Hallewell, R.A.; Tainer, J.A. !$#journal Cell (1992) 71:107-118 !$#title The structure of human mitochondrial manganese superoxide !1dismutase reveals a novel tetrameric interface of two !14-helix bundles. !$#cross-references MUID:93008233; PMID:1394426 !$#contents annotation; X-ray crystallography, 2.2 angstroms REFERENCE A51016 !$#authors Borgstahl, G.E.O.; Parge, H.E.; Tainer, J.A. !$#submission submitted to the Brookhaven Protein Data Bank, August 1992 !$#cross-references PDB:1ABM !$#contents annotation; X-ray crystallography, 2.2 angstroms, residues !125-222 !$#note kidney recombinant form expressed in Escherichia coli REFERENCE A51304 !$#authors Sussman, J.; Wagner, U.G.; Pattridge, K.A.; Ludwig, M.L. !$#submission submitted to the Brookhaven Protein Data Bank, November 1992 !$#cross-references PDB:1MSD !$#contents annotation; X-ray crystallography, 3.2 angstroms, residues !125-222 GENETICS !$#gene GDB:SOD2 !'##cross-references GDB:119597; OMIM:147460 !$#map_position 6q25.2-6q25.2 FUNCTION !$#description catalyzes the dismutation of 2 molecules of peroxide radical !1to dioxygen and hydrogen peroxide CLASSIFICATION #superfamily superoxide dismutase (Mn) KEYWORDS manganese; metalloprotein; mitochondrion; oxidoreductase FEATURE !$1-24 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$25-222 #product superoxide dismutase (Mn) #status !8experimental #label MAT\ !$50,98,183,187 #binding_site manganese (His, His, Asp, His) #status !8experimental SUMMARY #length 222 #molecular-weight 24722 #checksum 5500 SEQUENCE /// ENTRY DSRTN #type complete TITLE superoxide dismutase (EC 1.15.1.1) (Mn) precursor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 11-Jun-1999 ACCESSIONS S21661; S06310 REFERENCE S21661 !$#authors Ho, Y.S.; Howard, A.J.; Crapo, J.D. !$#submission submitted to the EMBL Data Library, October 1990 !$#accession S21661 !'##molecule_type DNA !'##residues 1-222 ##label HOY1 !'##cross-references EMBL:X56600; NID:g57272; PIDN:CAA39937.1; !1PID:g57273 REFERENCE S06310 !$#authors Ho, Y.S.; Crapo, J.D. !$#journal Nucleic Acids Res. (1987) 15:10070 !$#title Nucleotide sequences of cDNAs coding for rat !1manganese-containing superoxide dismutase. !$#cross-references MUID:88096516; PMID:3697077 !$#accession S06310 !'##molecule_type mRNA !'##residues 1-166,'H',168-222 ##label HOY2 !'##cross-references EMBL:Y00497; NID:g56690; PIDN:CAA68549.1; !1PID:g56691 !'##note 167-Gln was also found GENETICS !$#gene SOD2 !$#introns 8/2; 76/1; 115/1; 175/1 FUNCTION !$#description catalyzes the dismutation of 2 molecules of peroxide radical !1to dioxygen and hydrogen peroxide CLASSIFICATION #superfamily superoxide dismutase (Mn) KEYWORDS manganese; metalloprotein; mitochondrion; oxidoreductase FEATURE !$1-24 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$25-222 #product superoxide dismutase (Mn) #status predicted !8#label MAT\ !$50,98,183,187 #binding_site manganese (His, His, Asp, His) #status !8predicted SUMMARY #length 222 #molecular-weight 24674 #checksum 8675 SEQUENCE /// ENTRY DSPMN #type complete TITLE superoxide dismutase (EC 1.15.1.1) (Mn) precursor - garden pea ORGANISM #formal_name Pisum sativum #common_name garden pea DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 11-Jun-1999 ACCESSIONS S18343; S15560 REFERENCE S18343 !$#authors Wong-Vega, L.; Burke, J.J.; Allen, R.D. !$#journal Plant Mol. Biol. (1991) 17:1271-1274 !$#title Isolation and sequence analysis of a cDNA that encodes pea !1manganese superoxide dismutase. !$#cross-references MUID:92032795; PMID:1932701 !$#accession S18343 !'##molecule_type mRNA !'##residues 1-240 ##label WON !'##cross-references EMBL:X60170; NID:g20901; PIDN:CAA42737.1; !1PID:g20902 FUNCTION !$#description catalyzes the dismutation of 2 molecules of peroxide radical !1to dioxygen and hydrogen peroxide CLASSIFICATION #superfamily superoxide dismutase (Mn) KEYWORDS manganese; metalloprotein; mitochondrion; oxidoreductase FEATURE !$1-36 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$37-240 #product superoxide dismutase (Mn) #status predicted !8#label MAT\ !$64,112,201,205 #binding_site manganese (His, His, Asp, His) #status !8predicted SUMMARY #length 240 #molecular-weight 26637 #checksum 9854 SEQUENCE /// ENTRY DSBYN #type complete TITLE superoxide dismutase (EC 1.15.1.1) (Mn) precursor [validated] - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YHR008c ORGANISM #formal_name Saccharomyces cerevisiae DATE 19-Feb-1984 #sequence_revision 17-Mar-1987 #text_change 23-Mar-2001 ACCESSIONS A00521; S46785; A90766 REFERENCE A91141 !$#authors Marres, C.A.M.; Van Loon, A.P.G.M.; Oudshoorn, P.; Van !1Steeg, H.; Grivell, L.A.; Slater, E.C. !$#journal Eur. J. Biochem. (1985) 147:153-161 !$#title Nucleotide sequence analysis of the nuclear gene coding for !1manganese superoxide dismutase of yeast mitochondria, a gene !1previously assumed to code for the Rieske iron-sulphur !1protein. !$#cross-references MUID:85127011; PMID:3882422 !$#accession A00521 !'##molecule_type DNA !'##residues 1-233 ##label MAR !'##cross-references EMBL:X02156; NID:g4513; PIDN:CAA26092.1; PID:g4514 REFERENCE S46774 !$#authors Du, Z. !$#submission submitted to the EMBL Data Library, June 1994 !$#description The sequence of S. cerevisiae cosmid L2825. !$#accession S46785 !'##molecule_type DNA !'##residues 1-233 ##label DUZ !'##cross-references EMBL:U10400; NID:g500701; PIDN:AAB68939.1; !1PID:g500704; GSPDB:GN00008; MIPS:YHR008c REFERENCE A90766 !$#authors Ditlow, C.; Johansen, J.T.; Martin, B.M.; Svendsen, I. !$#journal Carlsberg Res. Commun. (1982) 47:81-91 !$#title The complete amino acid sequence of manganese-superoxide !1dismutase from Saccharomyces cerevisae. !$#accession A90766 !'##molecule_type protein !'##residues 27-229 ##label DIT GENETICS !$#gene SGD:SOD2; MIPS:YHR008c !'##cross-references SGD:S0001050; MIPS:YHR008c !$#map_position 8R !$#genome nuclear COMPLEX homotetramer FUNCTION !$#description catalyzes the dismutation of 2 molecules of peroxide radical !1to dioxygen and hydrogen peroxide CLASSIFICATION #superfamily superoxide dismutase (Mn) KEYWORDS homotetramer; manganese; metalloprotein; mitochondrial !1matrix; mitochondrion; oxidoreductase FEATURE !$1-26 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$27-229 #product superoxide dismutase (Mn) #status !8experimental #label MAT\ !$52,107,194,198 #binding_site manganese (His, His, Asp, His) #status !8predicted SUMMARY #length 233 #molecular-weight 25774 #checksum 3160 SEQUENCE /// ENTRY DSECN #type complete TITLE superoxide dismutase (EC 1.15.1.1) (Mn) sodA [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-May-1979 #sequence_revision 27-Jan-1995 #text_change 01-Mar-2002 ACCESSIONS A24141; A00522; S26146; S40852; C42436; G65196 REFERENCE A24141 !$#authors Takeda, Y.; Avila, H. !$#journal Nucleic Acids Res. (1986) 14:4577-4589 !$#title Structure and gene expression of the E. coli Mn-superoxide !1dismutase gene. !$#cross-references MUID:86232592; PMID:3520487 !$#accession A24141 !'##molecule_type DNA !'##residues 1-206 ##label TAK !'##cross-references GB:X03951; NID:g42972; PIDN:CAA27580.1; PID:g42973 !'##experimental_source strain K12 K802 REFERENCE A00522 !$#authors Steinman, H.M. !$#journal J. Biol. Chem. (1978) 253:8708-8720 !$#title The amino acid sequence of mangano superoxide dismutase from !1Escherichia coli B. !$#cross-references MUID:79067747; PMID:363708 !$#accession A00522 !'##molecule_type protein !'##residues 2-80,'HN',83-164,'L',166-206 ##label STE REFERENCE S26145 !$#authors Garcia-Martin, C.; Baldoma, L.; Badia, J.; Aguilar, J. !$#journal J. Gen. Microbiol. (1992) 138:1109-1116 !$#title Nucleotide sequence of the rhaR-sodA interval specifying !1rhaT in Escherichia coli. !$#cross-references MUID:92407483; PMID:1339463 !$#accession S26146 !'##molecule_type DNA !'##residues 1-96 ##label GAR !'##cross-references EMBL:X60699; NID:g42726; PIDN:CAA43108.1; !1PID:g42727 REFERENCE S40802 !$#authors Plunkett III, G.; Burland, V.; Daniels, D.L.; Blattner, F.R. !$#journal Nucleic Acids Res. (1993) 21:3391-3398 !$#title Analysis of the Escherichia coli genome. III. DNA sequence !1of the region from 87.2 to 89.2 minutes. !$#cross-references MUID:93347969; PMID:8346018 !$#accession S40852 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-206 ##label PLU !'##cross-references EMBL:L19201; NID:g304961; PIDN:AAB03041.1; !1PID:g305012 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1993 REFERENCE A42436 !$#authors Tate, C.G.; Muiry, J.A.; Henderson, P.J. !$#journal J. Biol. Chem. (1992) 267:6923-6932 !$#title Mapping, cloning, expression, and sequencing of the rhaT !1gene, which encodes a novel L-rhamnose-H+ transport protein !1in Salmonella typhimurium and Escherichia coli. !$#cross-references MUID:92202251; PMID:1551902 !$#accession C42436 !'##status preliminary !'##molecule_type DNA !'##residues 1-63 ##label TAT !'##note sequence extracted from NCBI backbone (NCBIN:91675, !1NCBIP:91681) REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65196 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-206 ##label BLAT !'##cross-references GB:AE000465; GB:U00096; NID:g2367326; !1PIDN:AAC76890.1; PID:g1790342; UWGP:b3908 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene sodA; Mn-SOD !$#map_position 87.5 min COMPLEX homodimer FUNCTION !$#description catalyzes the dismutation of 2 molecules of peroxide radical !1to dioxygen and hydrogen peroxide CLASSIFICATION #superfamily superoxide dismutase (Mn) KEYWORDS homodimer; manganese; metalloprotein; oxidoreductase FEATURE !$2-206 #product superoxide dismutase (Mn) #status !8experimental #label MAT\ !$27,82,168,172 #binding_site manganese (His, His, Asp, His) #status !8predicted SUMMARY #length 206 #molecular-weight 23097 #checksum 9028 SEQUENCE /// ENTRY DSBSNF #type complete TITLE superoxide dismutase (EC 1.15.1.1) (Mn) - Bacillus stearothermophilus ORGANISM #formal_name Bacillus stearothermophilus DATE 31-Oct-1980 #sequence_revision 27-Jan-1995 #text_change 23-Mar-2001 ACCESSIONS A35134; A90441; A91103; A91414; S27522; A00523 REFERENCE A35134 !$#authors Bowler, C.; Van Kaer, L.; Van Camp, W.; Van Montagu, M.; !1Inze, D.; Dhaese, P. !$#journal J. Bacteriol. (1990) 172:1539-1546 !$#title Characterization of the Bacillus stearothermophilus !1manganese superoxide dismutase gene and its ability to !1complement copper/zinc superoxide dismutase deficiency in !1Saccharomyces cerevisiae. !$#cross-references MUID:90170872; PMID:2407726 !$#accession A35134 !'##molecule_type DNA !'##residues 1-204 ##label BOW !'##cross-references GB:M26646; NID:g143202; PIDN:AAA22600.1; !1PID:g143203 !'##experimental_source strain ATCC 12980 REFERENCE A90441 !$#authors Brock, C.J.; Walker, J.E. !$#journal Biochemistry (1980) 19:2873-2882 !$#title Superoxide dismutase from Bacillus stearothermophilus. !1Complete amino acid sequence of a manganese enzyme. !$#cross-references MUID:80242540; PMID:7397109 !$#accession A90441 !'##molecule_type protein !'##residues 2-204 ##label BRO REFERENCE A91103 !$#authors Auffret, A.D.; Blake, T.J.; Williams, D.H. !$#journal Eur. J. Biochem. (1981) 113:333-338 !$#title Mass spectrometric sequence studies of a superoxide !1dismutase from Bacillus stearothermophilus. !$#cross-references MUID:81138217; PMID:7202415 !$#contents mass spectrometric analysis !$#accession A91103 !'##molecule_type protein !'##residues 2-121,'G',123-204 ##label AUF REFERENCE A91414 !$#authors Bridgen, J.; Harris, J.I.; Northrop, F. !$#journal FEBS Lett. (1975) 49:392-395 !$#title Evolutionary relationships in superoxide dismutase. !$#cross-references MUID:75075578; PMID:1089067 !$#accession A91414 !'##molecule_type protein !'##residues 2-54,'ZZ',57,'P',59,'B',61 ##label BRI REFERENCE S27522 !$#authors Brehm, J.K.; Chambers, S.P.; Bown, K.J.; Atkinson, T.; !1Minton, N.P. !$#submission submitted to the EMBL Data Library, December 1991 !$#description Molecular cloning and nucleotide sequence determination of !1the Bacillus stearothermophilus superoxide dismutase gene !1and its overexpression in Escherichia coli. !$#accession S27522 !'##status preliminary !'##molecule_type DNA !'##residues 1-204 ##label BRE !'##cross-references EMBL:M81188; NID:g143551; PIDN:AAA22765.1; !1PID:g143552 FUNCTION !$#description catalyzes the dismutation of 2 molecules of peroxide radical !1to dioxygen and hydrogen peroxide CLASSIFICATION #superfamily superoxide dismutase (Mn) KEYWORDS homodimer; manganese; metalloprotein; oxidoreductase FEATURE !$2-204 #product superoxide dismutase (Mn) #status predicted !8#label MAT\ !$27,79,164,168 #binding_site manganese (His, His, Asp, His) #status !8predicted SUMMARY #length 204 #molecular-weight 22861 #checksum 7425 SEQUENCE /// ENTRY DSHSNH #type complete TITLE superoxide dismutase (EC 1.15.1.1) (Mn) - Halobacterium salinarum ORGANISM #formal_name Halobacterium salinarum DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 21-Jul-2000 ACCESSIONS C32580; JT0401; A30483 REFERENCE A32580 !$#authors Takao, M.; Kobayashi, T.; Oikawa, A.; Yasui, A. !$#journal J. Bacteriol. (1989) 171:6323-6329 !$#title Tandem arrangement of photolyase and superoxide dismutase !1genes in Halobacterium halobium. !$#cross-references MUID:90036726; PMID:2681164 !$#accession C32580 !'##molecule_type DNA !'##residues 1-200 ##label TAK !'##cross-references GB:M24544; NID:g148791; PIDN:AAA72750.1; !1PID:g148794 !'##note the source is designated as Halobacterium halobium REFERENCE JT0401 !$#authors Salin, M.L.; Duke, M.V.; Oesterhelt, D.; Ma, D.P. !$#journal Gene (1988) 70:153-159 !$#title Cloning and determination of the nucleotide sequence of the !1Mn-containing superoxide dismutase gene from Halobacterium !1halobium. !$#cross-references MUID:89196907; PMID:3240866 !$#accession JT0401 !'##molecule_type DNA !'##residues 1-87,'AASRPGRSPTASRRTSAPTRTGGLNSRWRPARP',121-173,'T', !1175-200 ##label SAL !'##cross-references GB:M22408; NID:g148813; PIDN:AAA72704.1; !1PID:g148814 !'##note the source is designated as Halobacterium halobium !'##note the authors translated the codon ACG for residue 174 as Ser !'##note the sequence for residues 88-120 has been corrected in !1reference A30483 REFERENCE A30483 !$#authors Salin, M.L.; Duke, M.V.; Oesterhelt, D.; Ma, D.P. !$#journal Gene (1990) 87:153 !$#contents erratum !$#accession A30483 !'##molecule_type DNA !'##residues 88-120 ##label SA2 FUNCTION !$#description catalyzes the dismutation of 2 molecules of peroxide radical !1to dioxygen and hydrogen peroxide CLASSIFICATION #superfamily superoxide dismutase (Mn) KEYWORDS manganese; metalloprotein; oxidoreductase FEATURE !$28,76,158,162 #binding_site manganese (His, His, Asp, His) #status !8predicted SUMMARY #length 200 #molecular-weight 22208 #checksum 6264 SEQUENCE /// ENTRY A34319 #type complete TITLE superoxide dismutase (EC 1.15.1.1) (Mn) [validated] - Halobacterium salinarum ORGANISM #formal_name Halobacterium salinarum DATE 18-Feb-2000 #sequence_revision 18-Feb-2000 #text_change 21-Jul-2000 ACCESSIONS A34319; A26932; S11601 REFERENCE A34319 !$#authors May, B.P.; Dennis, P.P. !$#journal J. Biol. Chem. (1989) 264:12253-12258 !$#title Evolution and regulation of the gene encoding superoxide !1dismutase from the archaebacterium Halobacterium cutirubrum. !$#cross-references MUID:89308646; PMID:2745441 !$#accession A34319 !'##molecule_type DNA !'##residues 1-200 ##label MAY !'##cross-references GB:J04956; NID:g148815; PIDN:AAA72217.1; !1PID:g148816 !'##note the source is designated as Halobacterium cutirubrum REFERENCE A26932 !$#authors May, B.P.; Dennis, P.P. !$#journal J. Bacteriol. (1987) 169:1417-1422 !$#title Superoxide dismutase from the extremely halophilic !1archaebacterium Halobacterium cutirubrum. !$#cross-references MUID:87165744; PMID:3104309 !$#accession A26932 !'##molecule_type protein !'##residues 'T',3-35,'X',37-47,'XX',50,'XN',53-55,'X',57 ##label MA2 !'##note the source is designated as Halobacterium cutirubrum REFERENCE S11601 !$#authors May, B.P.; Tam, P.; Dennis, P.P. !$#journal Can. J. Microbiol. (1989) 35:171-175 !$#title The expression of the superoxide dismutase gene in !1Halobacterium cutirubrum and Halobacterium volcanii. !$#cross-references MUID:89248676; PMID:2720491 !$#accession S11601 !'##status preliminary !'##molecule_type DNA !'##residues 2-200 ##label MA3 !'##note the source is designated as Halobacterium cutirubrum FUNCTION !$#description EC 1.15.1.1 [validated, MUID:87165744]; catalyzes the !1dismutation of 2 molecules of peroxide radical to dioxygen !1and hydrogen peroxide !$#note shows anomalously high resistance to azide inhibition and !1sensitivity to inactivation by hydrogen peroxide CLASSIFICATION #superfamily superoxide dismutase (Mn) KEYWORDS manganese; metalloprotein; oxidoreductase FEATURE !$2-200 #product superoxide dismutase (Mn) #status predicted !8#label MAT\ !$28,76,158,162 #binding_site manganese (His, His, Asp, His) #status !8predicted SUMMARY #length 200 #molecular-weight 22385 #checksum 5669 SEQUENCE /// ENTRY DSECF #type complete TITLE superoxide dismutase (EC 1.15.1.1) (Fe) sodB [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 15-Dec-1988 #sequence_revision 27-Jan-1995 #text_change 01-Mar-2002 ACCESSIONS A29940; S00091; B64923 REFERENCE A29940 !$#authors Carlioz, A.; Ludwig, M.L.; Stallings, W.C.; Fee, J.A.; !1Steinman, H.M.; Touati, D. !$#journal J. Biol. Chem. (1988) 263:1555-1562 !$#title Iron superoxide dismutase. Nucleotide sequence of the gene !1from Escherichia coli K12 and correlations with crystal !1structures. !$#cross-references MUID:88087302; PMID:2447093 !$#contents X-ray crystallography, 3.1 angstroms !$#accession A29940 !'##molecule_type DNA !'##residues 1-193 ##label CAR !'##cross-references GB:J03511; NID:g147841; PIDN:AAA24637.1; !1PID:g147842 !'##experimental_source strain K12 REFERENCE S00091 !$#authors Schinina, M.E.; Maffey, L.; Barra, D.; Bossa, F.; Puget, K.; !1Michelson, A.M. !$#journal FEBS Lett. (1987) 221:87-90 !$#title The primary structure of iron superoxide dismutase from !1Escherichia coli. !$#cross-references MUID:87304820; PMID:3305077 !$#accession S00091 !'##molecule_type protein !'##residues 2-193 ##label SCH REFERENCE A52604 !$#authors Lah, M.S.; Dixon, M.; Pattridge, K.A.; Stallings, W.C.; Fee, !1J.A.; Ludwig, M.L. !$#submission submitted to the Brookhaven Protein Data Bank, July 1994 !$#cross-references PDB:1ISA !$#contents annotation; X-ray crystallography, 1.80 angstroms, residues !12-193, ferrous state REFERENCE A52605 !$#authors Lah, M.S.; Dixon, M.; Pattridge, K.A.; Stallings, W.C.; Fee, !1J.A.; Ludwig, M.L. !$#submission submitted to the Brookhaven Protein Data Bank, July 1994 !$#cross-references PDB:1ISB !$#contents annotation; X-ray crystallography, 1.85 angstroms, residues !12-193, ferric state REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64923 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-193 ##label BLAT !'##cross-references GB:AE000261; GB:U00096; NID:g1787945; !1PIDN:AAC74728.1; PID:g1787946; UWGP:b1656 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene sodB; Fe-SOD !$#map_position 36 min FUNCTION !$#description catalyzes the dismutation of 2 molecules of peroxide radical !1to dioxygen and hydrogen peroxide CLASSIFICATION #superfamily superoxide dismutase (Mn) KEYWORDS iron; metalloprotein; oxidoreductase FEATURE !$2-193 #product superoxide dismutase (Fe) #status !8experimental #label MAT\ !$27,74,157,161 #binding_site iron (His, His, Asp, His) #status !8experimental SUMMARY #length 193 #molecular-weight 21266 #checksum 2645 SEQUENCE /// ENTRY RDPSHA #type complete TITLE mercury(II) reductase (EC 1.16.1.1) - Pseudomonas aeruginosa transposon Tn501 ALTERNATE_NAMES Hg(II) reductase; merA protein; mercuric reductase ORGANISM #formal_name Pseudomonas aeruginosa DATE 18-Apr-1984 #sequence_revision 18-Apr-1984 #text_change 21-Jul-2000 ACCESSIONS A00406 REFERENCE A90473 !$#authors Brown, N.L.; Ford, S.J.; Pridmore, R.D.; Fritzinger, D.C. !$#journal Biochemistry (1983) 22:4089-4095 !$#title Nucleotide sequence of a gene from the Pseudomonas !1transposon Tn501 encoding mercuric reductase. !$#cross-references MUID:84000429; PMID:6311258 !$#accession A00406 !'##molecule_type DNA !'##residues 1-561 ##label BRO !'##cross-references GB:Z00027; GB:K00031; NID:g43714; PIDN:CAA77323.1; !1PID:g43718 REFERENCE A90472 !$#authors Fox, B.S.; Walsh, C.T. !$#journal Biochemistry (1983) 22:4082-4088 !$#title Mercuric reductase: homology to glutathione reductase and !1lipoamide dehydrogenase. Iodoacetamide alkylation and !1sequence of the active site peptide. !$#cross-references MUID:84000428; PMID:6412751 !$#contents annotation; active site COMMENT Bacterial resistance to mercuric ions is determined by this !1detoxification enzyme, which is encoded in plasmids and !1transposons. GENETICS !$#gene merA FUNCTION !$#description catalyzes the reduction of mercury (+2) to mercury (0) using !1NADPH CLASSIFICATION #superfamily mercury(II) reductase; dihydrolipoamide !1dehydrogenase homology; heavy-metal-associated homology KEYWORDS FAD; flavoprotein; metal binding; NADP; oxidoreductase; !1redox-active disulfide FEATURE !$6-35 #domain heavy-metal-associated homology #label HMA\ !$100-128 #region beta-alpha-beta FAD nucleotide-binding fold\ !$102-542 #domain dihydrolipoamide dehydrogenase homology !8#label DLD\ !$272-300 #region beta-alpha-beta NADP nucleotide-binding fold\ !$136-141 #disulfide_bonds redox-active #status experimental\ !$558,559 #binding_site mercury (Cys) #status predicted SUMMARY #length 561 #molecular-weight 58727 #checksum 8934 SEQUENCE /// ENTRY D33858 #type fragment TITLE mercury(II) reductase (EC 1.16.1.1) - Escherichia coli plasmid pDU1358 (fragment) ALTERNATE_NAMES Hg(II) reductase; merA protein; mercuric reductase ORGANISM #formal_name Escherichia coli DATE 04-Sep-1998 #sequence_revision 04-Sep-1998 #text_change 15-Jan-1999 ACCESSIONS D33858 REFERENCE A33858 !$#authors Nucifora, G.; Chu, L.; Silver, S.; Misra, T.K. !$#journal J. Bacteriol. (1989) 171:4241-4247 !$#title Mercury operon regulation by the merR gene of the !1organomercurial resistance system of plasmid pDU1358. !$#cross-references MUID:89327136; PMID:2666393 !$#accession D33858 !'##status preliminary !'##molecule_type DNA !'##residues 1-343 ##label NUC !'##cross-references GB:M24940 COMMENT Bacterial resistance to mercuric ions is determined by this !1detoxification enzyme, which is encoded in plasmids and !1transposons. GENETICS !$#genome plasmid FUNCTION !$#description catalyzes the reduction of mercury (+2) to mercury (0) using !1NADPH CLASSIFICATION #superfamily mercury(II) reductase; dihydrolipoamide !1dehydrogenase homology; heavy-metal-associated homology KEYWORDS FAD; flavoprotein; metal binding; NADP; oxidoreductase; !1redox-active disulfide FEATURE !$6-35 #domain heavy-metal-associated homology #label HMA\ !$100-128 #region beta-alpha-beta FAD nucleotide-binding fold\ !$102-343 #domain dihydrolipoamide dehydrogenase homology !8(fragment) #label DLD\ !$272-300 #region beta-alpha-beta NADP nucleotide-binding fold\ !$11,14 #binding_site mercury (Cys) #status predicted\ !$136-141 #disulfide_bonds redox-active #status experimental SUMMARY #length 343 #checksum 4840 SEQUENCE /// ENTRY RDEBHA #type complete TITLE mercury(II) reductase (EC 1.16.1.1) - Shigella flexneri plasmid R100 ALTERNATE_NAMES Hg(II) reductase; merA protein; mercuric reductase ORGANISM #formal_name Shigella flexneri DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 18-Sep-1998 ACCESSIONS A22799 REFERENCE A22799 !$#authors Misra, T.K.; Brown, N.L.; Haberstroh, L.; Schmidt, A.; !1Goddette, D.; Silver, S. !$#journal Gene (1985) 34:253-262 !$#title Mercuric reductase structural genes from plasmid R100 and !1transposon Tn501: functional domains of the enzyme. !$#cross-references MUID:85232071; PMID:2989109 !$#accession A22799 !'##molecule_type DNA !'##residues 1-564 ##label MIS !'##cross-references GB:J01730; NID:g151742 COMMENT Bacterial resistance to mercuric ions is determined by this !1detoxification enzyme, which is encoded in plasmids and !1transposons. GENETICS !$#gene merA !$#genome plasmid COMPLEX homodimer FUNCTION !$#description catalyzes the reduction of mercury (+2) to mercury (0) using !1NADPH. CLASSIFICATION #superfamily mercury(II) reductase; dihydrolipoamide !1dehydrogenase homology; heavy-metal-associated homology KEYWORDS FAD; flavoprotein; homodimer; metal binding; NADP; !1oxidoreductase; redox-active disulfide FEATURE !$6-35 #domain heavy-metal-associated homology #label HMA\ !$99-127 #region beta-alpha-beta FAD nucleotide-binding fold\ !$101-545 #domain dihydrolipoamide dehydrogenase homology !8#label DLD\ !$271-299 #region beta-alpha-beta NADP nucleotide-binding fold\ !$135-140 #disulfide_bonds redox-active #status experimental\ !$561,562 #binding_site mercury (Cys) #status predicted SUMMARY #length 564 #molecular-weight 58974 #checksum 3548 SEQUENCE /// ENTRY S77979 #type complete TITLE mercury(II) reductase (EC 1.16.1.1) - plasmid NR1 ALTERNATE_NAMES Hg(II) reductase; merA protein; mercuric reductase ORGANISM #formal_name plasmid NR1 DATE 04-Sep-1998 #sequence_revision 04-Sep-1998 #text_change 11-Jun-1999 ACCESSIONS S77979; S09526 REFERENCE S77979 !$#authors Summers, A.O. !$#submission submitted to the EMBL Data Library, July 1986 !$#accession S77979 !'##molecule_type DNA !'##residues 1-564 ##label SUM !'##cross-references EMBL:K03089; NID:g150389; PIDN:AAB59078.1; !1PID:g150396 REFERENCE S07447 !$#authors Barrineau, P.; Gilbert, P.; Jackson, W.J.; Jones, C.S.; !1Summers, A.O.; Wisdom, S. !$#journal J. Mol. Appl. Genet. (1984) 2:601-619 !$#title The DNA sequence of the mercury resistance operon of the !1IncFII plasmid NR1. !$#cross-references MUID:85159407; PMID:6530603 !$#accession S09526 !'##molecule_type DNA !'##residues 1-69,'P',71-564 ##label BAR !'##cross-references EMBL:K03089 COMMENT Bacterial resistance to mercuric ions is determined by this !1detoxification enzyme, which is encoded in plasmids and !1transposons. GENETICS !$#gene merA !$#genome plasmid FUNCTION !$#description catalyzes the reduction of mercury (+2) to mercury (0) using !1NADPH CLASSIFICATION #superfamily mercury(II) reductase; dihydrolipoamide !1dehydrogenase homology; heavy-metal-associated homology KEYWORDS FAD; flavoprotein; metal binding; NADP; oxidoreductase; !1redox-active disulfide FEATURE !$6-35 #domain heavy-metal-associated homology #label HMA\ !$99-127 #region beta-alpha-beta FAD nucleotide-binding fold\ !$101-545 #domain dihydrolipoamide dehydrogenase homology !8#label DLD\ !$271-299 #region beta-alpha-beta NADP nucleotide-binding fold\ !$135-140 #disulfide_bonds redox-active #status experimental\ !$561,562 #binding_site mercury (Cys) #status predicted SUMMARY #length 564 #molecular-weight 58879 #checksum 1774 SEQUENCE /// ENTRY S70146 #type complete TITLE mercury(II) reductase (EC 1.16.1.1) - Xanthomonas sp. ALTERNATE_NAMES Hg(II) reductase; merA protein; mercuric reductase ORGANISM #formal_name Xanthomonas sp. DATE 04-Sep-1998 #sequence_revision 04-Sep-1998 #text_change 11-Jun-1999 ACCESSIONS S70146 REFERENCE S70140 !$#authors Kholodii, G.Y.; Mindlin, S.Z.; Bass, I.A.; Yurieva, O.V.; !1Minakhina, S.V.; Nikiforov, V.G. !$#journal Mol. Microbiol. (1995) 17:1189-1200 !$#title Four genes, two ends, and a res region are involved in !1transposition of Tn5053: a paradigm for a novel family of !1transposons carrying either a mer operon or an integron. !$#cross-references MUID:96130850; PMID:8594337 !$#accession S70146 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-548 ##label KHO !'##cross-references EMBL:L40585; NID:g710572; PIDN:AAA98326.1; !1PID:g710579 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1May 1995 COMMENT Bacterial resistance to mercuric ions is determined by this !1detoxification enzyme, which is encoded in plasmids and !1transposons. GENETICS !$#gene merA FUNCTION !$#description catalyzes the reduction of mercury (+2) to mercury (0) using !1NADPH CLASSIFICATION #superfamily mercury(II) reductase; dihydrolipoamide !1dehydrogenase homology; heavy-metal-associated homology KEYWORDS FAD; flavoprotein; metal binding; NADP; oxidoreductase; !1redox-active disulfide FEATURE !$6-35 #domain heavy-metal-associated homology #label HMA\ !$87-115 #region beta-alpha-beta FAD nucleotide-binding fold\ !$89-529 #domain dihydrolipoamide dehydrogenase homology !8#label DLD\ !$259-287 #region beta-alpha-beta NADP nucleotide-binding fold\ !$123-128 #disulfide_bonds redox-active #status experimental\ !$545,546 #binding_site mercury (Cys) #status predicted SUMMARY #length 548 #molecular-weight 57483 #checksum 8354 SEQUENCE /// ENTRY JQ0153 #type complete TITLE mercury(II) reductase (EC 1.16.1.1) - Thiobacillus ferrooxidans ALTERNATE_NAMES Hg(II) reductase; merA protein; mercuric reductase ORGANISM #formal_name Thiobacillus ferrooxidans DATE 04-Sep-1998 #sequence_revision 04-Sep-1998 #text_change 16-Jun-2000 ACCESSIONS JQ0153 REFERENCE JQ0153 !$#authors Inoue, C.; Sugawara, K.; Shiratori, T.; Kusano, T.; !1Kitagawa, Y. !$#journal Gene (1989) 84:47-54 !$#title Nucleotide sequence of the Thiobacillus ferrooxidans !1chromosomal gene encoding mercuric reductase. !$#cross-references MUID:90108716; PMID:2691338 !$#accession JQ0153 !'##molecule_type DNA !'##residues 1-545 ##label INO !'##cross-references GB:D90110; GB:M32353; NID:g217155; PIDN:BAA14139.1; !1PID:g217158 !'##experimental_source strain E-15 COMMENT Bacterial resistance to mercuric ions is determined by this !1detoxification enzyme, which is encoded in plasmids and !1transposons. GENETICS !$#gene merA FUNCTION !$#description catalyzes the reduction of mercury (+2) to mercury (0) using !1NADPH CLASSIFICATION #superfamily mercury(II) reductase; dihydrolipoamide !1dehydrogenase homology; heavy-metal-associated homology KEYWORDS FAD; flavoprotein; metal binding; NADP; oxidoreductase; !1redox-active disulfide FEATURE !$11-40 #domain heavy-metal-associated homology #label HMA\ !$86-114 #region beta-alpha-beta FAD nucleotide-binding fold\ !$88-526 #domain dihydrolipoamide dehydrogenase homology !8#label DLD\ !$258-286 #region beta-alpha-beta NADP nucleotide-binding fold\ !$122-127 #disulfide_bonds redox-active #status experimental\ !$542,543 #binding_site mercury (Cys) #status predicted SUMMARY #length 545 #molecular-weight 57242 #checksum 4311 SEQUENCE /// ENTRY S18586 #type complete TITLE inactive mercury(II) reductase homolog [similarity] - Thiobacillus ferrooxidans ALTERNATE_NAMES merA protein homolog ORGANISM #formal_name Thiobacillus ferrooxidans DATE 04-Sep-1998 #sequence_revision 04-Sep-1998 #text_change 17-Nov-2000 ACCESSIONS S18586 REFERENCE S18584 !$#authors Inoue, C.; Sugawara, K.; Kusano, T. !$#journal Mol. Microbiol. (1991) 5:2707-2718 !$#title The merR regulatory gene in Thiobacillus ferrooxidans is !1spaced apart from the mer structural genes. !$#cross-references MUID:92140035; PMID:1779760 !$#accession S18586 !'##molecule_type DNA !'##residues 1-473 ##label INO !'##cross-references EMBL:X57326; NID:g48150; PIDN:CAA40599.1; !1PID:g48153 COMMENT Bacterial resistance to mercuric ions is determined by this !1detoxification enzyme, which is encoded in plasmids and !1transposons. FUNCTION !$#description catalyzes the reduction of mercury (+2) to mercury (0) using !1NADPH CLASSIFICATION #superfamily mercury(II) reductase; dihydrolipoamide !1dehydrogenase homology; heavy-metal-associated homology KEYWORDS FAD; flavoprotein; metal binding; NADP; redox-active !1disulfide FEATURE !$9-38 #domain heavy-metal-associated homology #label HMA\ !$88-116 #region beta-alpha-beta FAD nucleotide-binding fold\ !$90-473 #domain dihydrolipoamide dehydrogenase homology !8#status atypical #label DLD\ !$260-288 #region beta-alpha-beta NADP nucleotide-binding fold\ !$14,17 #binding_site mercury (Cys) #status predicted\ !$124-129 #disulfide_bonds redox-active #status experimental SUMMARY #length 473 #molecular-weight 50582 #checksum 1584 SEQUENCE /// ENTRY S18588 #type complete TITLE hypothetical mercury(II) reductase truncated homolog [similarity] - Thiobacillus ferrooxidans ALTERNATE_NAMES Hg(II) reductase; merA protein; mercuric reductase ORGANISM #formal_name Thiobacillus ferrooxidans DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 17-Nov-2000 ACCESSIONS S18588 REFERENCE S18584 !$#authors Inoue, C.; Sugawara, K.; Kusano, T. !$#journal Mol. Microbiol. (1991) 5:2707-2718 !$#title The merR regulatory gene in Thiobacillus ferrooxidans is !1spaced apart from the mer structural genes. !$#cross-references MUID:92140035; PMID:1779760 !$#accession S18588 !'##molecule_type DNA !'##residues 1-228 ##label INO !'##cross-references EMBL:X57326; NID:g48150; PIDN:CAA40601.1; !1PID:g48155 !'##experimental_source strain E-15 CLASSIFICATION #superfamily mercury(II) reductase; dihydrolipoamide !1dehydrogenase homology; heavy-metal-associated homology KEYWORDS FAD; flavoprotein; metal binding; redox-active disulfide FEATURE !$9-38 #domain heavy-metal-associated homology #label HMA\ !$90-228 #domain dihydrolipoamide dehydrogenase homology !8#status atypical #label DLD\ !$124-129 #disulfide_bonds redox-active #status predicted SUMMARY #length 228 #molecular-weight 24166 #checksum 6785 SEQUENCE /// ENTRY E32227 #type complete TITLE mercury(II) reductase (EC 1.16.1.1) [validated] - Bacillus sp. (strain RC607) ALTERNATE_NAMES Hg(II) reductase; merA protein; mercuric reductase; mercury resistance protein ORGANISM #formal_name Bacillus sp. #variety strain RC607 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Nov-2000 ACCESSIONS E32227 REFERENCE A32227 !$#authors Wang, Y.; Moore, M.; Levinson, H.S.; Silver, S.; Walsh, C.; !1Mahler, I. !$#journal J. Bacteriol. (1989) 171:83-92 !$#title Nucleotide sequence of a chromosomal mercury resistance !1determinant from a Bacillus sp. with broad-spectrum mercury !1resistance. !$#cross-references MUID:89123092; PMID:2536669 !$#accession E32227 !'##status preliminary !'##molecule_type DNA !'##residues 1-631 ##label WAN !'##cross-references GB:M22708; NID:g143188; PIDN:AAA83977.1; !1PID:g143191 !'##experimental_source strain RC607 GENETICS !$#gene merA FUNCTION !$#description EC 1.16.1.1 [validated, MUID:95080381] CLASSIFICATION #superfamily Bacillus mercury(II) reductase; !1dihydrolipoamide dehydrogenase homology; !1heavy-metal-associated homology KEYWORDS metal binding; oxidoreductase; redox-active disulfide FEATURE !$8-36 #domain heavy-metal-associated homology #label HMA1\ !$87-115 #domain heavy-metal-associated homology #label HMA2\ !$173-612 #domain dihydrolipoamide dehydrogenase homology !8#label DLD\ !$13,16 #binding_site mercury (Cys) #status predicted\ !$92,95 #binding_site mercury (Cys) #status predicted\ !$207,628 #binding_site mercury (Cys) #status experimental\ !$207-212 #disulfide_bonds redox-active #status predicted\ !$264,605 #binding_site mercury (Tyr) #status experimental SUMMARY #length 631 #molecular-weight 68072 #checksum 8453 SEQUENCE /// ENTRY KUHU #type complete TITLE ferroxidase (EC 1.16.3.1) precursor [validated] - human ALTERNATE_NAMES ceruloplasmin CONTAINS ferroxidase long form (CP-1); ferroxidase short form (CP-2) ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Aug-1980 #sequence_revision 12-May-1995 #text_change 08-Dec-2000 ACCESSIONS A25443; A24165; A35450; A00524; I59067 REFERENCE A25443 !$#authors Koschinsky, M.L.; Funk, W.D.; van Oost, B.A.; MacGillivray, !1R.T.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:5086-5090 !$#title Complete cDNA sequence of human preceruloplasmin. !$#cross-references MUID:86259737; PMID:2873574 !$#accession A25443 !'##molecule_type mRNA !'##residues 1-1060,1065-1069 ##label KOS !'##cross-references GB:M13699; NID:g180255; PIDN:AAA51976.1; !1PID:g180256 !'##note this is the short or CP-2 alternatively spliced form REFERENCE A24165 !$#authors Mercer, J.F.B.; Grimes, A. !$#journal FEBS Lett. (1986) 203:185-190 !$#title Isolation of a human ceruloplasmin cDNA clone that includes !1the N-terminal leader sequence. !$#cross-references MUID:86275241; PMID:3755405 !$#accession A24165 !'##molecule_type mRNA !'##residues 1-40;549-599;784-829;919-952 ##label MER REFERENCE A35450 !$#authors Yang, F.; Friedrichs, W.E.; Cupples, R.L.; Bonifacio, M.J.; !1Sanford, J.A.; Horton, W.A.; Bowman, B.H. !$#journal J. Biol. Chem. (1990) 265:10780-10785 !$#title Human ceruloplasmin. Tissue-specific expression of !1transcripts produced by alternative splicing. !$#cross-references MUID:90285218; PMID:2355023 !$#accession A35450 !'##molecule_type DNA !'##residues 1007-1064 ##label YAN !'##cross-references GB:J05506 !'##note this is the long or CP-1 alternatively spliced form REFERENCE A00524 !$#authors Takahashi, N.; Ortel, T.L.; Putnam, F.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:390-394 !$#title Single-chain structure of human ceruloplsmin: the complete !1amino acid sequence of the whole molecule. !$#cross-references MUID:84119493; PMID:6582496 !$#accession A00524 !'##molecule_type protein !'##residues 20-1060,1065-1069 ##label TAK !'##note 79-Gly and 449-Gly were also found REFERENCE I59067 !$#authors Yang, F.; Naylor, S.L.; Lum, J.B.; Cutshaw, S.; McCombs, !1J.L.; Naberhaus, K.H.; McGill, J.R.; Adrian, G.S.; Moore, !1C.M.; Barnett, D.R.; Bowman, B.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:3257-3261 !$#title Characterization, mapping, and expression of the human !1ceruloplasmin gene. !$#cross-references MUID:86205876; PMID:3486416 !$#accession I59067 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 218-1069 ##label RES !'##cross-references GB:M13536; NID:g180248; PIDN:AAA51975.1; !1PID:g180249 COMMENT Ferroxidase is a blue, plasma alpha2-glycoprotein binding !16-7 copper ions per molecule. COMMENT In Wilson's disease the plasma levels of ferroxidase are !1diminished or undetectable. COMMENT The three fragment chains are produced spontaneously during !1purification and may be present in vivo. GENETICS !$#gene GDB:CP !'##cross-references GDB:119069; OMIM:117700 !$#map_position 3q23-3q25 !$#introns 1006/3; 1061/1 !$#note the list of introns is incomplete FUNCTION !$#description catalyzes the oxidation of free iron(II) to iron(III) !1coupled with the reduction of dioxygen to water !$#note iron(III), but not iron(II), is the form bound and !1transported by transferrin !$#note other possible functions are amine oxidase activity, copper !1transport and homeostasis, and superoxide dismutase activity CLASSIFICATION #superfamily ferroxidase; ferroxidase repeat homology KEYWORDS acute phase; alternative splicing; copper; duplication; !1glycoprotein; oxidoreductase; plasma FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-1069 #product ferroxidase, long form #status predicted !8#label MATL\ !$20-1060 #product ferroxidase, short form #status experimental !8#label MATS\ !$20-499 #product ferroxidase 67K chain #status experimental !8#label K67\ !$23-357 #domain ferroxidase repeat homology #label FO1\ !$373-718 #domain ferroxidase repeat homology #label FO2\ !$501-905 #product ferroxidase 50K chain #status experimental !8#label K50\ !$733-1059 #domain ferroxidase repeat homology #label FO3\ !$907-1065 #product ferroxidase 19K chain #status experimental !8#label K19\ !$138,397,762 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$174-200,276-357, !$534-560,637-718, !$874-900 #disulfide_bonds #status predicted\ !$227,588,926 #binding_site carbohydrate (Asn) (covalent) #status !8absent\ !$295,338,343 #binding_site copper (His, Cys, His) (type 1) #status !8predicted\ !$358 #binding_site carbohydrate (Asn) (covalent) (partial) !8#status experimental\ !$656,699,704,709 #binding_site copper (His, Cys, His, Met) (type 1) !8#status predicted\ !$994,1040,1045,1050 #binding_site copper (His, Cys, His, Met) (type 1) !8#status predicted SUMMARY #length 1069 #molecular-weight 122651 #checksum 4175 SEQUENCE /// ENTRY A35210 #type complete TITLE ferroxidase (EC 1.16.3.1) precursor - rat ALTERNATE_NAMES ceruloplasmin ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A35210; A41753; A29564; S21692 REFERENCE A35210 !$#authors Fleming, R.E.; Gitlin, J.D. !$#journal J. Biol. Chem. (1990) 265:7701-7707 !$#title Primary structure of rat ceruloplasmin and analysis of !1tissue-specific gene expression during development. !$#cross-references MUID:90237081; PMID:2332446 !$#accession A35210 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-1059 ##label FLE !'##cross-references GB:J05424 REFERENCE A41753 !$#authors Fleming, R.E.; Gitlin, J.D. !$#journal J. Biol. Chem. (1992) 267:479-486 !$#title Structural and functional analysis of the 5'-flanking region !1of the rat ceruloplasmin gene. !$#cross-references MUID:92112697; PMID:1730611 !$#accession A41753 !'##molecule_type DNA !'##residues 1-48 ##label FL2 !'##note the authors translated the codon GAA for residue 40 as Gly, GAA !1for residue 41 as Gly, and GAA for residue 43 as Gly REFERENCE A29564 !$#authors Aldred, A.R.; Grimes, A.; Schreiber, G.; Mercer, J.F.B. !$#journal J. Biol. Chem. (1987) 262:2875-2878 !$#title Rat ceruloplasmin. Molecular cloning and gene expression in !1liver, choroid plexus, yolk sac, placenta, and testis. !$#cross-references MUID:87137545; PMID:3818625 !$#accession A29564 !'##molecule_type mRNA !'##residues 'NSG',215-216,'Y',218,'FAT',222,'F',224-226,'E',228,'LL', !1231,'D',233-235,'RM',238,'TTA',242-243,'N',245-270,'A', !1272-295,824-829,832,'L',834-867,'V',869-883,'Y',885-890,'R', !1892 ##label ALD !'##experimental_source liver !'##note the authors translated the codon GCG for residue 60 as Gly and !1GTG for residue 127 as Cys REFERENCE S21692 !$#authors Ryan, T.P.; Grover, T.A.; Aust, S.D. !$#journal Arch. Biochem. Biophys. (1992) 293:1-8 !$#title Rat ceruloplasmin: resistance to proteolysis and kinetic !1comparison with human ceruloplasmin. !$#cross-references MUID:92117681; PMID:1531003 !$#accession S21692 !'##molecule_type protein !'##residues 20-29,'Q';902-910 ##label RYA CLASSIFICATION #superfamily ferroxidase; ferroxidase repeat homology KEYWORDS copper; glycoprotein; oxidoreductase; plasma FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-1059 #product ferroxidase #status predicted #label MAT\ !$23-356 #domain ferroxidase repeat homology #label FO1\ !$372-712 #domain ferroxidase repeat homology #label FO2\ !$727-1053 #domain ferroxidase repeat homology #label FO3 SUMMARY #length 1059 #molecular-weight 120664 #checksum 318 SEQUENCE /// ENTRY EZHU #type complete TITLE coagulation factor VIII precursor [validated] - human ALTERNATE_NAMES antihemophilic factor A; coagulation factor VIIIc; procoagulant component ORGANISM #formal_name Homo sapiens #common_name man DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 08-Dec-2000 ACCESSIONS I54318; A00525; I58059; A23584; A26174; A42348; A43986; !1S63527; S66445; B42348; C42348; D42348; E42348; F42348; !1G42348; H42348; I42348 REFERENCE I54318 !$#authors Gitschier, J.; Wood, W.I. !$#journal Hum. Mol. Genet. (1992) 1:199-200 !$#title Sequence of the exon-containing regions of the human factor !1VIII gene. !$#cross-references MUID:93265012; PMID:1303178 !$#accession I54318 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-1921,'S',1923-2351 ##label RES !'##cross-references GB:M88648; NID:g182381; PIDN:AAA52420.1; !1PID:g182383 REFERENCE A00525 !$#authors Wood, W.I.; Capon, D.J.; Simonsen, C.C.; Eaton, D.L.; !1Gitschier, J.; Keyt, B.; Seeburg, P.H.; Smith, D.H.; !1Hollingshead, P.; Wion, K.L.; Delwart, E.; Tuddenham, !1E.G.D.; Vehar, G.A.; Lawn, R.M. !$#journal Nature (1984) 312:330-337 !$#title Expression of active human factor VIII from recombinant DNA !1clones. !$#cross-references MUID:85061548; PMID:6438526 !$#accession A00525 !'##molecule_type mRNA !'##residues 1-2351 ##label WOO !'##cross-references EMBL:X01165; EMBL:X01166; EMBL:X01179 REFERENCE I58059 !$#authors Toole, J.J.; Knopf, J.L.; Wozney, J.M.; Sultzman, L.A.; !1Buecker, J.L.; Pittman, D.D.; Kaufman, R.J.; Brown, E.; !1Shoemaker, C.; Orr, E.C.; Amphlett, G.W.; Foster, W.B.; Coe, !1M.L.; Knutson, G.J.; Fass, D.N.; Hewick, R.M. !$#journal Nature (1984) 312:342-347 !$#title Molecular cloning of a cDNA encoding human antihaemophilic !1factor. !$#cross-references MUID:85061550; PMID:6438528 !$#accession I58059 !'##status nucleic acid sequence not shown; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-74,'V',76-1259,'E',1261-2351 ##label RE2 !'##cross-references GB:K01740; NID:g182802; PIDN:AAA52484.1; !1PID:g182803 REFERENCE A23584 !$#authors Truett, M.A.; Blacher, R.; Burke, R.L.; Caput, D.; Chu, C.; !1Dina, D.; Hartog, K.; Kuo, C.H.; Masiarz, F.R.; !1Merryweather, J.P.; Najarian, R.; Pachl, C.; Potter, S.J.; !1Puma, J.; Quiroga, M.; Rall, L.B.; Randolph, A.; Urdea, !1M.S.; Valenzuela, P.; Dahl, H.H.; Favalaro, J.; Hansen, J.; !1Nordfang, O.; Ezban, M. !$#journal DNA (1985) 4:333-349 !$#title Characterization of the polypeptide composition of human !1factor VIII:C and the nucleotide sequence and expression of !1the human kidney cDNA. !$#cross-references MUID:86081164; PMID:3935400 !$#accession A23584 !'##molecule_type mRNA !'##residues 1-2351 ##label TRU !'##cross-references GB:M14113; NID:g182817; PIDN:AAA52485.1; !1PID:g182818 REFERENCE A26174 !$#authors Eaton, D.; Rodriguez, H.; Vehar, G.A. !$#journal Biochemistry (1986) 25:505-512 !$#title Proteolytic processing of human factor VIII. Correlation of !1specific cleavages by thrombin, factor Xa, and activated !1protein C with activation and inactivation of factor VIII !1coagulant activity. !$#cross-references MUID:86159740; PMID:3082357 !$#accession A26174 !'##molecule_type protein !'##residues 20-36;392-399,'X',401-402;1668-1678;1709-1722,'D', !11723-1725;1741-1755 ##label EAT REFERENCE A42348 !$#authors Pittman, D.D.; Wang, J.H.; Kaufman, R.J. !$#journal Biochemistry (1992) 31:3315-3325 !$#title Identification and functional importance of tyrosine sulfate !1residues within recombinant factor VIII. !$#cross-references MUID:92207952; PMID:1554716 !$#accession A42348 !'##molecule_type protein !'##residues 20-36;356-371;392-408;582-594;1668-1669,'X', !11671;1672-1692;1693-1708;1709-1721,'E' ##label PIT !'##experimental_source recombinant material from Chinese hamster ovary !1cells !'##note sequence extracted from NCBI backbone and corrected to !1correspond with the published sequence REFERENCE A43986 !$#authors Fay, P.J.; Smudzin, T.M. !$#journal J. Biol. Chem. (1989) 264:14005-14010 !$#title Intersubunit fluorescence energy transfer in human factor !1VIII. !$#cross-references MUID:89340500; PMID:2503509 !$#accession A43986 !'##molecule_type protein !'##residues 'X',517-523;1853-1860,'X',1862-1864,'X',1866 ##label FAY REFERENCE A56109 !$#authors Leyte, A.; van Schijndel, H.B.; Niehrs, C.; Huttner, W.B.; !1Verbeet, M.P.; Mertens, K.; van Mourik, J.A. !$#journal J. Biol. Chem. (1991) 266:740-746 !$#title Sulfation of Tyr(1680) of human blood coagulation factor !1VIII is essential for the interaction of factor VIII with !1von Willebrand factor. !$#cross-references MUID:91093266; PMID:1898735 !$#contents annotation; sulfation REFERENCE A56196 !$#authors Gitschier, J.; Wood, W.I.; Goralka, T.M.; Wion, K.L.; Chen, !1E.Y.; Eaton, D.H.; Vehar, G.A.; Capon, D.J.; Lawn, R.M. !$#journal Nature (1984) 312:326-330 !$#title Characterization of the human factor VIII gene. !$#cross-references MUID:85061547; PMID:6438525 !$#contents annotation; introns REFERENCE A56216 !$#authors McMullen, B.A.; Fujikawa, K.; Davie, E.W.; Hedner, U.; !1Ezban, M. !$#journal Protein Sci. (1995) 4:740-746 !$#title Locations of disulfide bonds and free cysteines in the heavy !1and light chains of recombinant human factor VIII !1(antihemophilic factor A). !$#cross-references MUID:95338127; PMID:7613471 !$#contents annotation; disulfide bonds !$#note 329-Cys, 711-Cys, and 2019-Cys were shown to have free !1sulfhydryls REFERENCE S63527 !$#authors Kjalke, M.; Heding, A.; Talbo, G.; Persson, E.; Thomsen, J.; !1Ezban, M. !$#journal Eur. J. Biochem. (1995) 234:773-779 !$#title Amino acid residues 721-729 are required for full factor !1VIII activity. !$#cross-references MUID:96163459; PMID:8575434 !$#accession S63527 !'##molecule_type protein !'##residues 733-752;753-759 ##label KJA REFERENCE S66445 !$#authors Lind, P.; Larsson, K.; Spira, J.; Sydow-Baeckman, M.; !1Almstedt, A.; Gray, E.; Sandberg, H. !$#journal Eur. J. Biochem. (1995) 232:19-27 !$#title Novel forms of B-domain-deleted recombinant factor VIII !1molecules. Construction and biochemical characterization. !$#cross-references MUID:96048024; PMID:7556150 !$#accession S66445 !'##status preliminary !'##molecule_type protein !'##residues 1668-1685 ##label LIN COMMENT Factor VIII is activated by factor Xa and thrombin, but !1prolonged exposure produces additional cleavages that !1inactivate factor VIIIa. GENETICS !$#gene GDB:F8C !'##cross-references GDB:119124; OMIM:306700 !$#map_position Xq28-Xq28 !$#introns 48/2; 89/1; 130/1; 201/1; 224/1; 263/1; 337/1; 424/2; 481/3; !1513/1; 584/3; 635/1; 705/1; 1740/2; 1791/3; 1862/3; 1939/1; !12000/1; 2039/1; 2063/1; 2091/3; 2143/3; 2192/1; 2241/3; !12300/3 FUNCTION !$#description acts as a cofactor, with calcium and phospholipid, for the !1factor IXa proteolytic activation of factor X !$#pathway blood coagulation CLASSIFICATION #superfamily coagulation factor VIII; discoidin I !1amino-terminal homology; ferroxidase repeat homology KEYWORDS acute phase; blood coagulation; duplication; glycoprotein; !1hemophilia A; plasma; sulfoprotein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-2351 #product coagulation factor VIII #status experimental !8#label MAT\ !$20-740 #product coagulation factor VIIIa heavy chain #status !8experimental #label ACH\ !$20-356 #domain A1 #label DA1\ !$23-348 #domain ferroxidase repeat homology #label FO1\ !$392-759 #domain A2 #label DA2\ !$402-730 #domain ferroxidase repeat homology #label FO2\ !$760-1667 #domain B #label DB0\ !$1668-2351 #product coagulation factor VIIIa light chain #status !8experimental #label ACL\ !$1709-2038 #domain A3 #label DA3\ !$1716-2038 #domain ferroxidase repeat homology #label FO3\ !$2039-2191 #domain C1 #label DC1\ !$2039-2188 #domain discoidin I amino-terminal homology #label !8DN1\ !$2192-2351 #domain C2 #label DC2\ !$2192-2345 #domain discoidin I amino-terminal homology #label !8DN2\ !$60,258,601,776,803, !$847,919,962,982, !$1020,1024,1074, !$1085,1204,1274, !$1278,1301,1319, !$1403,1431,1461, !$1531,1704,1829,2137 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$172-198,267-348, !$547-573,649-730, !$1851-1877, !$1918-1922,2040-2188 #disulfide_bonds #status experimental\ !$355-356 #cleavage_site Arg-Met (coagulation factor Xa, !8protein C) #status predicted\ !$365,737,738,742, !$1683,1699 #binding_site sulfate (Tyr) (covalent) #status !8experimental\ !$391-392 #cleavage_site Arg-Ser (coagulation factor Xa, !8thrombin) #status experimental\ !$414,426 #binding_site sulfate (Tyr) (covalent) #status !8predicted\ !$759-760 #cleavage_site Arg-Ser (coagulation factor Xa, !8thrombin) #status experimental\ !$1667-1668 #cleavage_site Arg-Glu (unidentified proteinase) !8#status experimental\ !$1708-1709 #cleavage_site Arg-Ser (coagulation factor Xa, !8thrombin) #status experimental\ !$1740-1741 #cleavage_site Arg-Ala (coagulation factor Xa) !8#status experimental\ !$2193-2345 #disulfide_bonds #status predicted SUMMARY #length 2351 #molecular-weight 267007 #checksum 1863 SEQUENCE /// ENTRY KFHU5 #type complete TITLE coagulation factor V precursor [validated] - human ALTERNATE_NAMES coagulation labile factor; proaccelerin ORGANISM #formal_name Homo sapiens #common_name man DATE 19-May-1989 #sequence_revision 02-Jun-1995 #text_change 08-Dec-2000 ACCESSIONS A56172; A42344; A28028; A27498; A25897 REFERENCE A42344 !$#authors Cripe, L.D.; Moore, K.D.; Kane, W.H. !$#journal Biochemistry (1992) 31:3777-3785 !$#title Structure of the gene for human coagulation factor V. !$#cross-references MUID:92232668; PMID:1567832 !$#accession A56172 !'##molecule_type DNA !'##residues 1-2224 ##label CRI !'##cross-references GB:J05368 !$#accession A42344 !'##molecule_type DNA !'##residues !148-58;79-89;120-130;191-201;239-249;313-323;368-378;428-437; !1461-471;533-542;583-593;654-664;1598-1607;1653-1662; !11732-1741;1802-1812;1862-1872;1901-1911;1925-1935;1960-1969; !12012-2021;2060-2070;2111-2120;2172-2181 ##label CR2 REFERENCE A28028 !$#authors Jenny, R.J.; Pittman, D.D.; Toole, J.J.; Kriz, R.W.; Aldape, !1R.A.; Hewick, R.M.; Kaufman, R.J.; Mann, K.G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:4846-4850 !$#title Complete cDNA and derived amino acid sequence of human !1factor V. !$#cross-references MUID:87260886; PMID:3110773 !$#accession A28028 !'##molecule_type mRNA !'##residues 1-857,'R',859-864,'R',866-924,'E',926-1763,'I',1765-2212, !1'T',2214-2224 ##label JEN !'##cross-references GB:M16967 !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing REFERENCE A27498 !$#authors Kane, W.H.; Ichinose, A.; Hagen, F.S.; Davie, E.W. !$#journal Biochemistry (1987) 26:6508-6514 !$#title Cloning of cDNAs coding for the heavy chain region and !1connecting region of human factor V, a blood coagulation !1factor with four types of internal repeats. !$#cross-references MUID:88107560; PMID:2827731 !$#accession A27498 !'##molecule_type mRNA !'##residues 1-1284,'I',1286-1600 ##label KAN !'##cross-references GB:M17785 !'##note parts of this sequence were determined by protein sequencing REFERENCE A25897 !$#authors Kane, W.H.; Davie, E.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:6800-6804 !$#title Cloning of a cDNA coding for human factor V, a blood !1coagulation factor homologous to factor VIII and !1ceruloplasmin. !$#cross-references MUID:86313665; PMID:3092220 !$#accession A25897 !'##molecule_type mRNA !'##residues 1188-1215,1315-2224 ##label KA2 !'##cross-references GB:M14335 !'##note parts of this sequence were determined by protein sequencing REFERENCE A56139 !$#authors Keller, F.G.; Ortel, T.L.; Quinn-Allen, M.A.; Kane, W.H. !$#journal Biochemistry (1995) 34:4118-4124 !$#title Thrombin-catalyzed activation of recombinant human factor V. !$#cross-references MUID:95210278; PMID:7696276 !$#contents annotation; thrombin cleavage sites COMMENT Factor V is activated by thrombin and partially by !1coagulation factor Xa. GENETICS !$#gene GDB:F5 !'##cross-references GDB:119896; OMIM:227400 !$#map_position 1q23-1q23 !$#introns 53/2; 84/1; 125/1; 196/1; 244/1; 318/1; 373/2; 432/3; 466/1; !1537/3; 588/1; 659/1; 1599/2; 1657/3; 1736/3; 1807/1; 1867/1; !11906/1; 1930/1; 1964/3; 2016/3; 2065/1; 2115/3; 2176/3 FUNCTION !$#description acts as a cofactor, with calcium and phospholipid, for the !1factor Xa proteolytic activation of prothrombin to thrombin !$#pathway blood coagulation CLASSIFICATION #superfamily coagulation factor V; discoidin I !1amino-terminal homology; ferroxidase repeat homology KEYWORDS blood coagulation; duplication; glycoprotein; phospholipid !1binding; plasma; sulfoprotein; tandem repeat FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-2224 #product coagulation factor V #status predicted !8#label MAT\ !$29-737 #product coagulation factor Va heavy chain #status !8experimental #label VAH\ !$29-345 #domain A1 #label DA1\ !$33-329 #domain ferroxidase repeat homology #label FO1\ !$346-691 #domain A2 #label DA2\ !$351-684 #domain ferroxidase repeat homology #label FO2\ !$692-1573 #domain B #label DOB\ !$1183-1461 #region 9-residue repeats (Q-X-T/N-L-S-P-D-L-S)\ !$1574-2224 #product coagulation factor Va light chain #status !8experimental #label VAL\ !$1574-1905 #domain A3 #label DA3\ !$1581-1905 #domain ferroxidase repeat homology #label FO3\ !$1667-1765 #region phospholipid binding #status predicted\ !$1906-2064 #domain C1 #label DC1\ !$1906-2061 #domain discoidin I amino-terminal homology #label !8DN1\ !$2065-2224 #domain C2 #label DC2\ !$2065-2221 #domain discoidin I amino-terminal homology #label !8DN2\ !$51,55,239,297,460, !$468,554,741,752, !$760,776,782,821, !$938,977,1074,1083, !$1103,1106,1479, !$1499,1559,1703, !$2010,2209 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$167-193,248-329, !$500-526,603-684, !$1725-1751, !$1907-2061,2066-2221 #disulfide_bonds #status predicted\ !$334-335 #cleavage_site Arg-Asn (protein C) #status predicted\ !$363,693,1546 #binding_site sulfate (Tyr) (covalent) #status !8predicted\ !$376-377 #cleavage_site Arg-Ser (coagulation factor Xa) !8#status predicted\ !$382,1338 #binding_site carbohydrate (Asn) (covalent) #status !8absent\ !$534-535 #cleavage_site Arg-Gly (protein C) #status predicted\ !$737-738 #cleavage_site Arg-Ser (coagulation factor Xa, !8thrombin) #status experimental\ !$1046-1047 #cleavage_site Arg-Thr (coagulation factor Xa, !8thrombin) #status experimental\ !$1573-1574 #cleavage_site Arg-Ser (thrombin) #status !8experimental SUMMARY #length 2224 #molecular-weight 251683 #checksum 1308 SEQUENCE /// ENTRY KFBO5 #type complete TITLE coagulation factor V precursor - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 04-Mar-1993 #sequence_revision 28-Apr-1995 #text_change 11-Jun-1999 ACCESSIONS A42580; A36497 REFERENCE A42580 !$#authors Guinto, E.R.; Esmon, C.T.; Mann, K.G.; MacGillivray, R.T. !$#journal J. Biol. Chem. (1992) 267:2971-2978 !$#title The complete cDNA sequence of bovine coagulation factor V. !$#cross-references MUID:92147638; PMID:1737753 !$#accession A42580 !'##molecule_type mRNA !'##residues 1-2211 ##label GUI !'##cross-references GB:M81440; NID:g163037; PIDN:AAA30512.1; !1PID:g163038 !'##note sequence extracted from NCBI backbone (NCBIN:80774, !1NCBIP:80776) REFERENCE A36497 !$#authors Kalafatis, M.; Jenny, R.J.; Mann, K.G. !$#journal J. Biol. Chem. (1990) 265:21580-21589 !$#title Identification and characterization of a !1phospholipid-binding site of bovine factor Va. !$#cross-references MUID:91072354; PMID:2254316 !$#accession A36497 !'##molecule_type protein !'##residues 1566-1570,'X',1572-1581,'X',1583-1584;1673-1676,'X', !11678-1679,'X',1681,'X',1683-1689,'XX',1692-1693,'X', !11695-1696 ##label KAL REFERENCE A55979 !$#authors Xue, J.; Kalafatis, M.; Silveira, J.R.; Kung, C.; Mann, K.G. !$#journal Biochemistry (1994) 33:13109-13116 !$#title Determination of the disulfide bridges in factor Va heavy !1chain. !$#cross-references MUID:95034740; PMID:7947716 !$#contents annotation !$#note 566-Cys and 617-Cys were shown to have free sulfhydryls COMMENT Factor V is activated by thrombin and partially by !1coagulation factor Xa. FUNCTION !$#description acts as a cofactor, with calcium and phospholipid, for the !1factor Xa proteolytic activation of prothrombin to thrombin !$#pathway blood coagulation CLASSIFICATION #superfamily coagulation factor V; discoidin I !1amino-terminal homology; ferroxidase repeat homology KEYWORDS blood coagulation; duplication; glycoprotein; phospholipid !1binding; plasma; sulfoprotein; tandem repeat FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-2211 #product coagulation factor V #status predicted !8#label MAT\ !$29-741 #product coagulation factor Va heavy chain #status !8predicted #label VAH\ !$29-345 #domain A1 #label DA1\ !$33-329 #domain ferroxidase repeat homology #label FO1\ !$346-695 #domain A2 #label DA2\ !$351-688 #domain ferroxidase repeat homology #label FO2\ !$696-1564 #domain B #label DOB\ !$1175-1437 #region 9-residue repeats (Q-X-T/N-L-S-P-D-L-S)\ !$1565-2211 #product coagulation factor Va light chain #status !8predicted #label VAL\ !$1565-1892 #domain A3 #label DA3\ !$1572-1892 #domain ferroxidase repeat homology #label FO3\ !$1654-1752 #region phospholipid binding #status predicted\ !$1893-2051 #domain C1 #label DC1\ !$1893-2048 #domain discoidin I amino-terminal homology #label !8DN1\ !$2052-2211 #domain C2 #label DC2\ !$2052-2208 #domain discoidin I amino-terminal homology #label !8DN2\ !$167-193,248-329, !$499-525 #disulfide_bonds #status experimental\ !$225,239,297,382, !$460,553,587,745, !$756,774,780,902, !$952,964,1044,1053, !$1062,1071,1078, !$1094,1451,1490, !$1550,1690,1839, !$1997,2196 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$334-335 #cleavage_site Arg-Asn (protein C) #status predicted\ !$363,697,1537 #binding_site sulfate (Tyr) (covalent) #status !8predicted\ !$376-377 #cleavage_site Arg-Ser (coagulation factor Xa) !8#status predicted\ !$533-534 #cleavage_site Arg-Gly (protein C) #status predicted\ !$607-688,1712-1738, !$1894-2048,2053-2208 #disulfide_bonds #status predicted\ !$741-742 #cleavage_site Arg-Ser (coagulation factor Xa, !8thrombin) #status predicted\ !$1034-1035 #cleavage_site Arg-Ser (coagulation factor Xa, !8thrombin) #status predicted\ !$1564-1565 #cleavage_site Arg-Ser (thrombin) #status !8experimental SUMMARY #length 2211 #molecular-weight 248981 #checksum 7102 SEQUENCE /// ENTRY WMBE18 #type complete TITLE ribonucleoside-diphosphate reductase (EC 1.17.4.1) small chain - human herpesvirus 3 ALTERNATE_NAMES ribonucleotide reductase small chain ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 11-Jun-1999 ACCESSIONS I27342 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession I27342 !'##molecule_type DNA !'##residues 1-306 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27901.1; !1PID:g60007 GENETICS !$#gene 18 FUNCTION !$#description catalyzes the reduction of ribonucleoside diphosphate to !1deoxyribonucleoside diphosphate CLASSIFICATION #superfamily herpesvirus ribonucleoside-diphosphate !1reductase small chain KEYWORDS deoxyribonucleotide biosynthesis; early protein; iron; !1metalloprotein; oxidoreductase FEATURE !$66,96,99,159,193, !$196 #binding_site 2Fe-O cluster (Asp, Glu, His, Glu, Glu, !8His) #status predicted\ !$103 #active_site Tyr (stable tyrosyl radical) #status !8predicted SUMMARY #length 306 #molecular-weight 35397 #checksum 3090 SEQUENCE /// ENTRY WMBES7 #type complete TITLE ribonucleoside-diphosphate reductase (EC 1.17.4.1) small chain - human herpesvirus 1 (strain 17) ALTERNATE_NAMES ribonucleotide reductase small chain ORGANISM #formal_name human herpesvirus 1 DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jun-2000 ACCESSIONS D30088 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession D30088 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-340 ##label MCG !'##cross-references GB:X14112; NID:g1944536; PIDN:CAA32303.1; !1PID:g59540; GB:D00317 GENETICS !$#gene UL40 FUNCTION !$#description catalyzes the reduction of ribonucleoside diphosphate to !1deoxyribonucleoside diphosphate CLASSIFICATION #superfamily herpesvirus ribonucleoside-diphosphate !1reductase small chain KEYWORDS deoxyribonucleotide biosynthesis; early protein; iron; !1metalloprotein; oxidoreductase FEATURE !$94,124,127,187,221, !$224 #binding_site 2Fe-O cluster (Asp, Glu, His, Glu, Glu, !8His) #status predicted\ !$131 #active_site Tyr (stable tyrosyl radical) #status !8predicted SUMMARY #length 340 #molecular-weight 38019 #checksum 3687 SEQUENCE /// ENTRY WMBEB2 #type complete TITLE ribonucleoside-diphosphate reductase (EC 1.17.4.1) small chain - human herpesvirus 2 (strain 333) ALTERNATE_NAMES ribonucleotide reductase small chain ORGANISM #formal_name human herpesvirus 2 DATE 20-Sep-1984 #sequence_revision 20-Sep-1984 #text_change 11-Jun-1999 ACCESSIONS A00529 REFERENCE A00529 !$#authors Galloway, D.A.; Swain, M.A. !$#journal J. Virol. (1984) 49:724-730 !$#title Organization of the left-hand end of the herpes simplex !1virus type 2 BglII N fragment. !$#cross-references MUID:84138764; PMID:6321759 !$#accession A00529 !'##molecule_type DNA !'##residues 1-337 ##label GAL !'##cross-references GB:M12700; GB:K02023; GB:K02911; NID:g330198; !1PIDN:AAA45807.1; PID:g330200 FUNCTION !$#description catalyzes the reduction of ribonucleoside diphosphate to !1deoxyribonucleoside diphosphate CLASSIFICATION #superfamily herpesvirus ribonucleoside-diphosphate !1reductase small chain KEYWORDS deoxyribonucleotide biosynthesis; early protein; iron; !1metalloprotein; oxidoreductase FEATURE !$91,121,124,184,218, !$221 #binding_site 2Fe-O cluster (Asp, Glu, His, Glu, Glu, !8His) #status predicted\ !$128 #active_site Tyr (stable tyrosyl radical) #status !8predicted SUMMARY #length 337 #molecular-weight 37625 #checksum 4088 SEQUENCE /// ENTRY WMBE32 #type complete TITLE ribonucleoside-diphosphate reductase (EC 1.17.4.1) small chain - human herpesvirus 2 ALTERNATE_NAMES ribonucleotide reductase small chain ORGANISM #formal_name human herpesvirus 2 DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 11-Jun-1999 ACCESSIONS A00528 REFERENCE A90974 !$#authors McLauchlan, J.; Clements, J.B. !$#journal EMBO J. (1983) 2:1953-1961 !$#title DNA sequence homology between two co-linear loci on the HSV !1genome which have different transforming abilities. !$#cross-references MUID:84057718; PMID:6315408 !$#accession A00528 !'##molecule_type DNA !'##residues 1-337 ##label MCL !'##cross-references GB:X00048; NID:g59911; PIDN:CAA24930.1; PID:g59912 FUNCTION !$#description catalyzes the reduction of ribonucleoside diphosphate to !1deoxyribonucleoside diphosphate CLASSIFICATION #superfamily herpesvirus ribonucleoside-diphosphate !1reductase small chain KEYWORDS deoxyribonucleotide biosynthesis; early protein; iron; !1metalloprotein; oxidoreductase FEATURE !$91,121,124,184,218, !$221 #binding_site 2Fe-O cluster (Asp, Glu, His, Glu, Glu, !8His) #status predicted\ !$128 #active_site Tyr (stable tyrosyl radical) #status !8predicted SUMMARY #length 337 #molecular-weight 37669 #checksum 4093 SEQUENCE /// ENTRY WMBEB4 #type complete TITLE ribonucleoside-diphosphate reductase (EC 1.17.4.1) small chain - bovine herpesvirus 1 (strain 34) ALTERNATE_NAMES ribonucleotide reductase small chain ORGANISM #formal_name bovine herpesvirus 1 DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 11-Jun-1999 ACCESSIONS A43367 REFERENCE A43367 !$#authors Simard, C.; Bastien, N.; Trudel, M. !$#journal Virology (1992) 190:689-701 !$#title Sequencing and 5'- and 3'-end transcript mapping of the gene !1encoding the small subunit of ribonucleotide reductase from !1bovine herpesvirus type-1. !$#cross-references MUID:92391086; PMID:1325701 !$#accession A43367 !'##molecule_type DNA !'##residues 1-314 ##label SIM !'##cross-references GB:M84470; NID:g330771; PIDN:AAA46063.1; !1PID:g330772 FUNCTION !$#description catalyzes the reduction of ribonucleoside diphosphate to !1deoxyribonucleoside diphosphate CLASSIFICATION #superfamily herpesvirus ribonucleoside-diphosphate !1reductase small chain KEYWORDS deoxyribonucleotide biosynthesis; early protein; iron; !1metalloprotein; oxidoreductase FEATURE !$73,103,106,166,200, !$203 #binding_site 2Fe-O cluster (Asp, Glu, His, Glu, Glu, !8His) #status predicted\ !$110 #active_site Tyr (stable tyrosyl radical) #status !8predicted SUMMARY #length 314 #molecular-weight 35251 #checksum 9071 SEQUENCE /// ENTRY WMBEA1 #type complete TITLE ribonucleoside-diphosphate reductase (EC 1.17.4.1) small chain - equine herpesvirus 1 (strain Ab4p) ALTERNATE_NAMES ribonucleotide reductase small chain ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 11-Jun-1999 ACCESSIONS C36797 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession C36797 !'##molecule_type DNA !'##residues 1-321 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02455.1; !1PID:g330812 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 20 FUNCTION !$#description catalyzes the reduction of ribonucleoside diphosphate to !1deoxyribonucleoside diphosphate !$#pathway DNA replication CLASSIFICATION #superfamily herpesvirus ribonucleoside-diphosphate !1reductase small chain KEYWORDS deoxyribonucleotide biosynthesis; early protein; iron; !1metalloprotein; oxidoreductase FEATURE !$78,108,111,171,205, !$208 #binding_site 2Fe-O cluster (Asp, Glu, His, Glu, Glu, !8His) #status predicted\ !$115 #active_site Tyr (stable tyrosyl radical) #status !8predicted SUMMARY #length 321 #molecular-weight 36017 #checksum 5528 SEQUENCE /// ENTRY S06735 #type complete TITLE ribonucleoside-diphosphate reductase (EC 1.17.4.1) chain M2 - mouse ALTERNATE_NAMES ribonucleotide reductase M2 subunit ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-May-2000 ACCESSIONS S06735; A24835 REFERENCE S06735 !$#authors Thelander, M.; Thelander, L. !$#journal EMBO J. (1989) 8:2475-2479 !$#title Molecular cloning and expression of the functional gene !1encoding the M2 subunit of mouse ribonucleotide reductase: a !1new dominant marker gene. !$#cross-references MUID:90060004; PMID:2684652 !$#accession S06735 !'##status translation not shown !'##molecule_type DNA !'##residues 1-390 ##label THE !'##cross-references EMBL:X15666; NID:g50719; PIDN:CAA33707.1; !1PID:g50720 REFERENCE A24835 !$#authors Thelander, L.; Berg, P. !$#journal Mol. Cell. Biol. (1986) 6:3433-3442 !$#title Isolation and characterization of expressible cDNA clones !1encoding the M1 and M2 subunits of mouse ribonucleotide !1reductase. !$#cross-references MUID:87089677; PMID:3025593 !$#accession A24835 !'##status preliminary !'##molecule_type mRNA !'##residues 1-390 ##label THE2 !'##cross-references GB:M14223; NID:g200767; PIDN:AAA40062.1; !1PID:g200768 !'##note the authors translated the codon GGG for residue 315 as Glu GENETICS !$#map_position 12 !$#introns 33/3; 58/3; 107/3; 146/3; 191/2; 223/1; 267/3; 302/3; 340/3 CLASSIFICATION #superfamily herpesvirus ribonucleoside-diphosphate !1reductase small chain KEYWORDS iron; oxidoreductase FEATURE !$139,170,173,233, !$267,270 #binding_site 2Fe-O cluster (Asp, Glu, His, Glu, Glu, !8His) #status predicted\ !$177 #active_site Tyr (stable tyrosyl radical) #status !8predicted SUMMARY #length 390 #molecular-weight 45095 #checksum 7141 SEQUENCE /// ENTRY A26916 #type complete TITLE ribonucleoside-diphosphate reductase (EC 1.17.4.1) small chain - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein J1271; protein YJL026w; ribonucleotide reductase small chain ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A26916; S07605; S56798 REFERENCE A26916 !$#authors Elledge, S.J.; Davis, R.W. !$#journal Mol. Cell. Biol. (1987) 7:2783-2793 !$#title Identification and isolation of the gene encoding the small !1subunit of ribonucleotide reductase from Saccharomyces !1cerevisiae: DNA damage-inducible gene required for mitotic !1viability. !$#cross-references MUID:88038817; PMID:3313004 !$#accession A26916 !'##molecule_type DNA !'##residues 1-399 ##label ELL !'##cross-references EMBL:M17221 !'##note the authors translated the codon GAA for residue 101 as Lys, !1GCT for residue 102 as Arg, TCT for residue 103 as Ala, TTC !1for residue 104 as Glu, TGG for residue 105 as Ala, ACC for !1residue 106 as Ser, GCT for residue 107 as Phe, and GAA for !1residue 108 as Trp !'##note the sequence shown follows the authors' translation REFERENCE S07605 !$#authors Hurd, H.K.; Roberts, C.W.; Roberts, J.W. !$#journal Mol. Cell. Biol. (1987) 7:3673-3677 !$#title Identification of the gene for the yeast ribonucleotide !1reductase small subunit and its inducibility by methyl !1methanesulfonate. !$#cross-references MUID:88065506; PMID:3316984 !$#accession S07605 !'##molecule_type DNA !'##residues 1-399 ##label HUR !'##cross-references EMBL:M17789; NID:g172449; PIDN:AAA34988.1; !1PID:g172450 REFERENCE S56793 !$#authors Pohl, T.M.; Aljinovic, G. !$#submission submitted to the Protein Sequence Database, September 1995 !$#accession S56798 !'##molecule_type DNA !'##residues 1-399 ##label TOV !'##cross-references EMBL:Z49301; NID:g1008141; PIDN:CAA89317.1; !1PID:g1008142; GSPDB:GN00010; MIPS:YJL026w GENETICS !$#gene SGD:RNR2; MIPS:YJL026w !'##cross-references SGD:S0003563; MIPS:YJL026w !$#map_position 10L FUNCTION !$#description oxidoreductase; pyrimidine deoxynucleotide metabolism CLASSIFICATION #superfamily herpesvirus ribonucleoside-diphosphate !1reductase small chain KEYWORDS iron; oxidoreductase; pyrimidine deoxynucleotide metabolism FEATURE !$145,176,179,239, !$273,276 #binding_site 2Fe-O cluster (Asp, Glu, His, Glu, Glu, !8His) #status predicted\ !$183 #active_site Tyr (stable tyrosyl radical) #status !8predicted SUMMARY #length 399 #molecular-weight 46147 #checksum 4118 SEQUENCE /// ENTRY WMBE12 #type complete TITLE ribonucleoside-diphosphate reductase (EC 1.17.4.1) small chain - human herpesvirus 4 (strain B95-8) ALTERNATE_NAMES ribonucleotide reductase small chain ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 11-Jun-1999 ACCESSIONS A00530; S32997 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession A00530 !'##molecule_type DNA !'##residues 1-302 ##label BAN !'##cross-references EMBL:V01555; NID:g59074; PIDN:CAA24843.1; !1PID:g1334857 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region FUNCTION !$#description catalyzes the reduction of ribonucleoside diphosphate to !1deoxyribonucleoside diphosphate CLASSIFICATION #superfamily herpesvirus ribonucleoside-diphosphate !1reductase small chain KEYWORDS deoxyribonucleotide biosynthesis; early protein; iron; !1metalloprotein; oxidoreductase FEATURE !$61,91,94,154,188, !$191 #binding_site 2Fe-O cluster (Glu, Glu, His, Glu, Glu, !8His) #status predicted\ !$98 #active_site Tyr (stable tyrosyl radical) #status !8predicted SUMMARY #length 302 #molecular-weight 34358 #checksum 7419 SEQUENCE /// ENTRY WMBEP5 #type complete TITLE ribonucleoside-diphosphate reductase (EC 1.17.4.1) small chain - saimiriine herpesvirus 1 (strain 11) ALTERNATE_NAMES ribonucleotide reductase small chain ORGANISM #formal_name saimiriine herpesvirus 1 #note host Saimiri sciureus (common squirrel monkey) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 11-Jun-1999 ACCESSIONS D36812 REFERENCE A36806 !$#authors Albrecht, J. !$#submission submitted to the EMBL Data Library, January 1992 !$#description Primary structure of the herpesvirus saimiri genome. !$#accession D36812 !'##molecule_type DNA !'##residues 1-305 ##label ALB !'##cross-references GB:X64346; NID:g60320; PIDN:CAA45683.1; PID:g60381 REFERENCE A37309 !$#authors Albrecht, J.C.; Nicholas, J.; Biller, D.; Cameron, K.R.; !1Biesinger, B.; Newman, C.; Wittmann, S.; Craxton, M.A.; !1Coleman, H.; Fleckenstein, B.; Honess, R.W. !$#journal J. Virol. (1992) 66:5047-5058 !$#title Primary structure of the herpesvirus saimiri genome. !$#cross-references MUID:92333688; PMID:1321287 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 60 FUNCTION !$#description catalyzes the reduction of ribonucleoside diphosphate to !1deoxyribonucleoside diphosphate !$#pathway DNA replication CLASSIFICATION #superfamily herpesvirus ribonucleoside-diphosphate !1reductase small chain KEYWORDS deoxyribonucleotide biosynthesis; early protein; iron; !1metalloprotein; oxidoreductase FEATURE !$64,94,97,157,191, !$194 #binding_site 2Fe-O cluster (Glu, Glu, His, Glu, Glu, !8His) #status predicted\ !$101 #active_site Tyr (stable tyrosyl radical) #status !8predicted SUMMARY #length 305 #molecular-weight 35167 #checksum 4357 SEQUENCE /// ENTRY RDVZVV #type complete TITLE ribonucleoside-diphosphate reductase (EC 1.17.4.1) small chain - vaccinia virus ALTERNATE_NAMES F4L protein ORGANISM #formal_name vaccinia virus DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 11-Jun-1999 ACCESSIONS A29892; I42506; F36213 REFERENCE A29892 !$#authors Slabaugh, M.; Roseman, N.; Davis, R.; Mathews, C. !$#journal J. Virol. (1988) 62:519-527 !$#title Vaccinia virus-encoded ribonucleotide reductase: sequence !1conservation of the gene for the small subunit and its !1amplification in hydroxyurea-resistant mutants. !$#cross-references MUID:88091062; PMID:2826813 !$#accession A29892 !'##molecule_type DNA !'##residues 1-319 ##label SLA !'##cross-references GB:M19117; NID:g335808; PIDN:AAA88680.1; !1PID:g335809 !'##experimental_source strain WR REFERENCE A42501 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:517-563 !$#title Appendix to "The complete DNA sequence of vaccinia virus". !$#accession I42506 !'##molecule_type DNA !'##residues 1-212,'Y',214-319 ##label GOE !'##cross-references GB:M35027; NID:g335317; PIDN:AAA48018.1; !1PID:g335366 !'##experimental_source strain Copenhagen REFERENCE A42531 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:247-266 !$#title The complete DNA sequence of vaccinia virus. !$#cross-references MUID:91021027; PMID:2219722 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given REFERENCE A36213 !$#authors Roseman, N.A.; Slabaugh, M.B. !$#journal Virology (1990) 178:410-418 !$#title The vaccinia virus HindIII F fragment: nucleotide sequence !1of the left 6.2 kb. !$#cross-references MUID:91020979; PMID:2219701 !$#accession F36213 !'##status preliminary !'##molecule_type DNA !'##residues 1-319 ##label ROS !'##cross-references EMBL:M34368; NID:g335618; PIDN:AAA48244.1; !1PID:g335624 !'##experimental_source strain WR FUNCTION !$#description catalyzes the reduction of ribonucleoside diphosphate to !1deoxyribonucleoside diphosphate CLASSIFICATION #superfamily herpesvirus ribonucleoside-diphosphate !1reductase small chain KEYWORDS DNA replication; iron; metalloprotein; oxidoreductase FEATURE !$70,101,104,163,197, !$200 #binding_site 2Fe-O cluster (Asp, Glu, His, Glu, Glu, !8His) #status predicted\ !$108 #active_site Tyr (stable tyrosyl radical) #status !8predicted SUMMARY #length 319 #molecular-weight 36973 #checksum 8198 SEQUENCE /// ENTRY RDSS2R #type fragment TITLE ribonucleoside-diphosphate reductase (EC 1.17.4.1) small chain - Atlantic surf clam (fragment) ALTERNATE_NAMES ribonucleotide reductase small chain ORGANISM #formal_name Spisula solidissima #common_name Atlantic surf clam DATE 28-Dec-1987 #sequence_revision 30-Sep-1988 #text_change 06-Nov-1998 ACCESSIONS A22259 REFERENCE A22259 !$#authors Standart, N.M.; Bray, S.J.; George, E.L.; Hunt, T.; !1Ruderman, J.V. !$#journal J. Cell Biol. (1985) 100:1968-1976 !$#title The small subunit of ribonucleotide-diphosphate reductase is !1encoded by one of the most abundant translationally !1regulated maternal RNAs in clam and sea urchin eggs. !$#cross-references MUID:85207963; PMID:2987274 !$#accession A22259 !'##molecule_type DNA !'##residues 1-299 ##label STA COMMENT The synthesis of this polypeptide chain is triggered by !1fertilization of the egg; it provides the precursors needed !1for DNA synthesis. FUNCTION !$#description catalyzes the reduction of ribonucleoside diphosphate to !1deoxyribonucleoside diphosphate CLASSIFICATION #superfamily herpesvirus ribonucleoside-diphosphate !1reductase small chain KEYWORDS deoxyribonucleotide biosynthesis; iron; metalloprotein; !1oxidoreductase FEATURE !$45,76,79,139,173, !$176 #binding_site 2Fe-O cluster (Asp, Glu, His, Glu, Glu, !8His) #status predicted\ !$83 #active_site Tyr (stable tyrosyl radical) #status !8predicted SUMMARY #length 299 #checksum 8841 SEQUENCE /// ENTRY RDVZAS #type complete TITLE ribonucleoside-diphosphate reductase (EC 1.17.4.1) small chain - African swine fever virus (strain Malawi LIL20/1) ALTERNATE_NAMES ribonucleotide reductase small chain ORGANISM #formal_name African swine fever virus, ASFV DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 06-Nov-1998 ACCESSIONS B40568 REFERENCE A40568 !$#authors Boursnell, M.; Shaw, K.; Yanez, R.J.; Vinuela, E.; Dixon, L. !$#journal Virology (1991) 184:411-416 !$#title The sequences of the ribonucleotide reductase genes from !1African swine fever virus show considerable homology with !1those of the orthopoxvirus, vaccinia virus. !$#cross-references MUID:91335775; PMID:1871976 !$#accession B40568 !'##molecule_type DNA !'##residues 1-327 ##label BOU !'##cross-references GB:M64728 FUNCTION !$#description catalyzes the reduction of ribonucleoside diphosphate to !1deoxyribonucleoside diphosphate CLASSIFICATION #superfamily herpesvirus ribonucleoside-diphosphate !1reductase small chain KEYWORDS deoxyribonucleotide biosynthesis; early protein; iron; !1metalloprotein; oxidoreductase FEATURE !$70,101,104,164,198, !$201 #binding_site 2Fe-O cluster (Asp, Glu, His, Glu, Glu, !8His) #status predicted\ !$108 #active_site Tyr (stable tyrosyl radical) #status !8predicted SUMMARY #length 327 #molecular-weight 38966 #checksum 4725 SEQUENCE /// ENTRY RDEC2R #type complete TITLE ribonucleoside-diphosphate reductase (EC 1.17.4.1) 1 beta chain [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES ribonucleotide reductase B2 protein ORGANISM #formal_name Escherichia coli DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 01-Mar-2002 ACCESSIONS A00527; A64994; A24542 REFERENCE A00526 !$#authors Carlson, J.; Fuchs, J.A.; Messing, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:4294-4297 !$#title Primary structure of the Escherichia coli ribonucleoside !1diphosphate reductase operon. !$#cross-references MUID:84272624; PMID:6087316 !$#accession A00527 !'##molecule_type DNA !'##residues 1-376 ##label CAR !'##cross-references GB:K02672; NID:g146964; PIDN:AAA24224.1; !1PID:g146967 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64994 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-376 ##label BLAT !'##cross-references GB:AE000313; GB:U00096; NID:g2367132; !1PIDN:AAC75295.1; PID:g1788567; UWGP:b2235 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A24542 !$#authors Salowe, S.P.; Stubbe, J. !$#journal J. Bacteriol. (1986) 165:363-366 !$#cross-references MUID:86111594; PMID:3511029 !$#accession A24542 !'##molecule_type protein !'##residues 2-21 ##label SAL REFERENCE A51874 !$#authors Eklund, H.; Nordlund, P. !$#submission submitted to the Brookhaven Protein Data Bank, July 1992 !$#cross-references PDB:1MRR !$#contents annotation; X-ray crystallography, 2.5 angstroms, with !1manganese, residues 2-7,'A',9-24,'Q',26-326,'N',328-341 REFERENCE A44539 !$#authors Nordlund, P.; Sjoeberg, B.M.; Eklund, H. !$#journal Nature (1990) 345:593-598 !$#title Three-dimensional structure of the free radical protein of !1ribonucleotide reductase. !$#cross-references MUID:90272001; PMID:2190093 !$#contents annotation; X-ray crystallography GENETICS !$#gene nrdB !$#map_position 49 COMPLEX heterotetramer of two alpha chains (the R1 or B1 homodimer, !1see PIR:RDEC1R) and two beta chains (the R2 or B2 homodimer) FUNCTION !$#description catalyzes the reduction of ribonucleoside diphosphates by !1reduced thioredoxin to the corresponding deoxyribonucleoside !1diphosphates and water !$#pathway deoxyribonucleotide biosynthesis CLASSIFICATION #superfamily herpesvirus ribonucleoside-diphosphate !1reductase small chain KEYWORDS deoxyribonucleotide biosynthesis; heterotetramer; iron; !1metalloprotein; oxidoreductase FEATURE !$2-376 #product ribonucleoside-diphosphate reductase beta !8chain #status experimental #label MAT\ !$85,116,119,205,239, !$242 #binding_site 2Fe-O cluster (Asp, Glu, His, Glu, Glu, !8His) #status experimental\ !$123 #active_site Tyr (stable tyrosyl radical) #status !8experimental SUMMARY #length 376 #molecular-weight 43517 #checksum 3391 SEQUENCE /// ENTRY C64135 #type complete TITLE ribonucleoside-diphosphate reductase (EC 1.17.4.1) beta chain - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C64135 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession C64135 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-376 ##label TIGR !'##cross-references GB:U32839; GB:L42023; NID:g1574508; !1PIDN:AAC23306.1; PID:g1574510; TIGR:HI1660 CLASSIFICATION #superfamily herpesvirus ribonucleoside-diphosphate !1reductase small chain KEYWORDS DNA replication; iron; metalloprotein; oxidoreductase FEATURE !$85,116,119,205,239, !$242 #binding_site 2Fe-O cluster (Asp, Glu, His, Glu, Glu, !8His) #status predicted SUMMARY #length 376 #molecular-weight 43326 #checksum 1985 SEQUENCE /// ENTRY RDBP24 #type complete TITLE ribonucleoside-diphosphate reductase (EC 1.17.4.1) - phage T4 ALTERNATE_NAMES ribonucleotide reductase B2 chain; ribonucleotide reductase small chain ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 06-Nov-1998 ACCESSIONS S07190; JF0023 REFERENCE S07190 !$#authors Sjoeberg, B.M.; Hahne, S.; Mathews, C.Z.; Mathews, C.K.; !1Rand, K.N.; Gait, M.J. !$#journal EMBO J. (1986) 5:2031-2036 !$#title The bacteriophage T4 gene for the small subunit of !1ribonucleotide reductase contains an intron. !$#cross-references MUID:87004574; PMID:3530746 !$#accession S07190 !'##molecule_type DNA !'##residues 1-379 ##label SJO !'##cross-references EMBL:X04140 GENETICS !$#gene nrdB !$#map_position 136.1-137.8 FUNCTION !$#description catalyzes the reduction of ribonucleoside diphosphate to !1deoxyribonucleoside diphosphate !$#pathway DNA replication CLASSIFICATION #superfamily herpesvirus ribonucleoside-diphosphate !1reductase small chain KEYWORDS deoxyribonucleotide biosynthesis; early protein; iron; !1metalloprotein; oxidoreductase FEATURE !$84,115,118,212,238, !$241 #binding_site 2Fe-O cluster (Asp, Glu, His, Glu, Glu, !8His) #status predicted\ !$122 #active_site Tyr (stable tyrosyl radical) #status !8experimental SUMMARY #length 379 #molecular-weight 44212 #checksum 1617 SEQUENCE /// ENTRY WMBEV3 #type complete TITLE ribonucleoside-diphosphate reductase (EC 1.17.4.1) large chain - human cytomegalovirus (strain AD169) ALTERNATE_NAMES ribonucleotide reductase large chain; UL45 protein ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 #note host Homo sapiens (man) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 21-Aug-1998 ACCESSIONS S09808 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09808 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-915 ##label CHE !'##cross-references EMBL:X17403 !'##note possible protein-coding frames are given !'##note the DNA sequence was submitted to EMBL, December 1989, in !1computer-readable form !'##note this reading frame extends between two stop codons and does not !1begin with a start codon CLASSIFICATION #superfamily herpesvirus ribonucleoside-diphosphate !1reductase large chain KEYWORDS deoxyribonucleotide biosynthesis; early protein; !1oxidoreductase; redox-active disulfide SUMMARY #length 915 #molecular-weight 102836 #checksum 2222 SEQUENCE /// ENTRY WMBY3L #type complete TITLE ribonucleoside-diphosphate reductase (EC 1.17.4.1) 3 large chain - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YIL066c; ribonucleotide reductase regulatory chain 3 ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1991 #sequence_revision 19-Jul-1996 #text_change 21-Jul-2000 ACCESSIONS S48413; S12066; B35845; A35930 REFERENCE S48407 !$#authors Smith, V. !$#submission submitted to the EMBL Data Library, September 1994 !$#accession S48413 !'##molecule_type DNA !'##residues 1-885 ##label SMI !'##cross-references EMBL:Z38060; NID:g557796; PIDN:CAA86157.1; !1PID:g557803; GSPDB:GN00009; MIPS:YIL066c REFERENCE A35930 !$#authors Yagle, K.; McEntee, K. !$#journal Mol. Cell. Biol. (1990) 10:5553-5557 !$#title The DNA damage-inducible gene DIN1 of Saccharomyces !1cerevisiae encodes a regulatory subunit of ribonucleotide !1reductase and is identical to RNR3. !$#cross-references MUID:90377250; PMID:2204819 !$#accession S12066 !'##molecule_type DNA !'##residues 17-142,'TRY',147-227,'L',229-262,'VLS',267-302,'TRVVTRD', !1315,'V',317,'S',319,'FS',320,'SHGMQISSTKF',329-773,'P' !1##label YAG !'##cross-references EMBL:M58012; NID:g171398; PIDN:AAA34569.1; !1PID:g171399 REFERENCE A35845 !$#authors Elledge, S.J.; Davis, R.W. !$#journal Genes Dev. (1990) 4:740-751 !$#title Two genes differentially regulated in the cell cycle and by !1DNA-damaging agents encode alternative regulatory subunits !1of ribonucleotide reductase. !$#cross-references MUID:90337312; PMID:2199320 !$#accession B35845 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type DNA !'##residues 17-36,'VL',39-52,'F',54-73,'I',75-84,'H',86-98,'T', !1100-117;'TGR',668-691,'L',693-702,'SR',705-725,'Q',727 !1##label ELL GENETICS !$#gene SGD:RNR3; DIN1; MIPS:YIL066c !'##cross-references SGD:S0001328; MIPS:YIL066c !$#map_position 9L CLASSIFICATION #superfamily herpesvirus ribonucleoside-diphosphate !1reductase large chain KEYWORDS deoxyribonucleotide biosynthesis; heterotetramer; !1oxidoreductase; redox-active disulfide FEATURE !$234-459,880-883 #disulfide_bonds redox-active #status predicted\ !$442,446 #active_site Asn, Glu #status predicted\ !$444 #active_site Cys (cysteine thiyl radical !8intermediate) #status predicted SUMMARY #length 885 #molecular-weight 99208 #checksum 3743 SEQUENCE /// ENTRY WZVZH4 #type complete TITLE ribonucleoside-diphosphate reductase (EC 1.17.4.1) large chain - vaccinia virus (strain WR) ALTERNATE_NAMES I4 protein; ribonucleotide reductase large chain ORGANISM #formal_name vaccinia virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 11-Jun-1999 ACCESSIONS A28611; D29889 REFERENCE A28611 !$#authors Tengelsen, L.A.; Slabaugh, M.B.; Bibler, J.K.; Hruby, D.E. !$#journal Virology (1988) 164:121-131 !$#title Nucleotide sequence and molecular genetic analysis of the !1large subunit of ribonucleotide reductase encoded by !1vaccinia virus. !$#cross-references MUID:88206055; PMID:3284177 !$#accession A28611 !'##molecule_type DNA !'##residues 1-771 ##label TEN REFERENCE A29889 !$#authors Schmitt, J.F.C.; Stunnenberg, H.G. !$#journal J. Virol. (1988) 62:1889-1897 !$#title Sequence and transcriptional analysis of the vaccinia virus !1HindIII I fragment. !$#cross-references MUID:88215015; PMID:2835495 !$#accession D29889 !'##molecule_type DNA !'##residues 1-466,'D',468-525,'L',527-600,'M',602,'TAST',607-771 !1##label SCH !'##cross-references GB:J03399; NID:g335662; PIDN:AAB59806.1; !1PID:g335666 GENETICS !$#gene I4 CLASSIFICATION #superfamily herpesvirus ribonucleoside-diphosphate !1reductase large chain KEYWORDS deoxyribonucleotide biosynthesis; early protein; !1oxidoreductase; redox-active disulfide FEATURE !$218-444,761-766 #disulfide_bonds redox-active #status predicted\ !$427,431 #active_site Asn, Glu #status predicted\ !$429 #active_site Cys (cysteine thiyl radical !8intermediate) #status predicted SUMMARY #length 771 #molecular-weight 87858 #checksum 2505 SEQUENCE /// ENTRY A24050 #type complete TITLE ribonucleoside-diphosphate reductase (EC 1.17.4.1) chain M1 - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A24050 REFERENCE A24050 !$#authors Caras, I.W.; Levinson, B.B.; Fabry, M.; Williams, S.R.; !1Martin Jr., D.W. !$#journal J. Biol. Chem. (1985) 260:7015-7022 !$#cross-references MUID:85207721; PMID:2581962 !$#accession A24050 !'##molecule_type mRNA !'##residues 1-792 ##label CAR CLASSIFICATION #superfamily herpesvirus ribonucleoside-diphosphate !1reductase large chain KEYWORDS DNA replication; oxidoreductase SUMMARY #length 792 #molecular-weight 90209 #checksum 7206 SEQUENCE /// ENTRY S28302 #type complete TITLE ribonucleoside-diphosphate reductase (EC 1.17.4.1) large chain - Caenorhabditis elegans ALTERNATE_NAMES protein T23G5.1 ORGANISM #formal_name Caenorhabditis elegans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S28302 REFERENCE S28296 !$#authors Berks, M. !$#submission submitted to the EMBL Data Library, December 1992 !$#accession S28302 !'##molecule_type DNA !'##residues 1-788 ##label BER !'##cross-references EMBL:Z19158; NID:g6880; PID:g1163132 GENETICS !$#introns 42/3; 135/3; 379/2; 596/2 CLASSIFICATION #superfamily herpesvirus ribonucleoside-diphosphate !1reductase large chain KEYWORDS DNA replication; oxidoreductase SUMMARY #length 788 #molecular-weight 88969 #checksum 2123 SEQUENCE /// ENTRY WMVZ9J #type complete TITLE ribonucleoside-diphosphate reductase (EC 1.17.4.1) large chain - vaccinia virus (strain Copenhagen and Ankara) ALTERNATE_NAMES I4L protein ORGANISM #formal_name vaccinia virus #note host Homo sapiens (man) DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 18-Feb-2000 ACCESSIONS I42510; T37341 REFERENCE A42501 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:517-563 !$#title Appendix to "The complete DNA sequence of vaccinia virus". !$#accession I42510 !'##molecule_type DNA !'##residues 1-771 ##label GOE !'##cross-references GB:M35027; NID:g335317; PIDN:AAA48059.1; !1PID:g335407 !'##experimental_source strain Copenhagen REFERENCE A42531 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:247-266 !$#title The complete DNA sequence of vaccinia virus. !$#cross-references MUID:91021027; PMID:2219722 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given REFERENCE Z20877 !$#authors Antoine, G.; Scheiflinger, F.; Falkner, F.G.; Dorner, F. !$#submission submitted to the EMBL Data Library, March 1997 !$#description The complete genomic sequence of the Modified Vaccinia !1Ankara (MVA) strain. !$#accession T37341 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-771 ##label ANT !'##cross-references EMBL:U94848; PIDN:AAB96436.1 !'##experimental_source strain Ankara GENETICS !$#note MVA065L CLASSIFICATION #superfamily herpesvirus ribonucleoside-diphosphate !1reductase large chain KEYWORDS deoxyribonucleotide biosynthesis; early protein; !1oxidoreductase; redox-active disulfide FEATURE !$218-444,761-766 #disulfide_bonds redox-active #status predicted\ !$427,431 #active_site Asn, Glu #status predicted\ !$429 #active_site Cys (cysteine thiyl radical !8intermediate) #status predicted SUMMARY #length 771 #molecular-weight 87753 #checksum 2837 SEQUENCE /// ENTRY WMBEB1 #type complete TITLE ribonucleoside-diphosphate reductase (EC 1.17.4.1) large chain - human herpesvirus 1 ALTERNATE_NAMES ribonucleotide reductase large chain ORGANISM #formal_name human herpesvirus 1 DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jun-2000 ACCESSIONS A26536; C30088 REFERENCE A26536 !$#authors Nikas, I.; McLauchlan, J.; Davison, A.J.; Taylor, W.R.; !1Clements, J.B. !$#journal Proteins (1986) 1:376-384 !$#title Structural features of ribonucleotide reductase. !$#cross-references MUID:88217882; PMID:2835765 !$#accession A26536 !'##molecule_type DNA !'##residues 1-1137 ##label NIK !'##cross-references GB:M18410 !'##experimental_source clone pYN1 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession C30088 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-69,'N',71-1137 ##label MCG !'##cross-references GB:X14112; NID:g1944536; PIDN:CAA32314.1; !1PID:g59539 !'##experimental_source strain 17 GENETICS !$#gene UL39 COMPLEX heterodimer of large (136K) and small (38K) chain CLASSIFICATION #superfamily herpesvirus ribonucleoside-diphosphate !1reductase large chain KEYWORDS deoxyribonucleotide biosynthesis; early protein; !1oxidoreductase; redox-active disulfide FEATURE !$582-818,1132-1135 #disulfide_bonds redox-active #status predicted\ !$791,795 #active_site Asn, Glu #status predicted\ !$793 #active_site Cys (cysteine thiyl radical !8intermediate) #status predicted SUMMARY #length 1137 #molecular-weight 124022 #checksum 8288 SEQUENCE /// ENTRY WMVZAL #type complete TITLE ribonucleoside-diphosphate reductase (EC 1.17.4.1) large chain - African swine fever virus (strain Malawi LIL20/1) ALTERNATE_NAMES ribonucleotide reductase large chain ORGANISM #formal_name African swine fever virus, ASFV DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 11-Jun-1999 ACCESSIONS A40568 REFERENCE A40568 !$#authors Boursnell, M.; Shaw, K.; Yanez, R.J.; Vinuela, E.; Dixon, L. !$#journal Virology (1991) 184:411-416 !$#title The sequences of the ribonucleotide reductase genes from !1African swine fever virus show considerable homology with !1those of the orthopoxvirus, vaccinia virus. !$#cross-references MUID:91335775; PMID:1871976 !$#accession A40568 !'##molecule_type DNA !'##residues 1-779 ##label BOU !'##cross-references GB:M64728; NID:g210649; PIDN:AAA42732.1; !1PID:g554615 CLASSIFICATION #superfamily herpesvirus ribonucleoside-diphosphate !1reductase large chain KEYWORDS deoxyribonucleotide biosynthesis; early protein; !1oxidoreductase; redox-active disulfide FEATURE !$194-440,774-777 #disulfide_bonds redox-active #status predicted\ !$420,424 #active_site Asn, Glu #status predicted\ !$422 #active_site Cys (cysteine thiyl radical !8intermediate) #status predicted SUMMARY #length 779 #molecular-weight 87387 #checksum 9195 SEQUENCE /// ENTRY QQBE11 #type complete TITLE ribonucleoside-diphosphate reductase (EC 1.17.4.1) large chain - human herpesvirus 4 (strain B95-8) ALTERNATE_NAMES ribonucleotide reductase large chain ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 11-Jun-1999 ACCESSIONS A03753; A22907; S32996 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession A03753 !'##molecule_type DNA !'##residues 1-826 ##label BAN !'##cross-references EMBL:V01555; NID:g59074; PIDN:CAA24842.1; !1PID:g1334856 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region REFERENCE A22907 !$#authors Gibson, T.; Stockwell, P.; Ginsburg, M.; Barrell, B. !$#journal Nucleic Acids Res. (1984) 12:5087-5099 !$#title Homology between two EBV early genes and HSV ribonucleotide !1reductase and 38K genes. !$#cross-references MUID:84247360; PMID:6330697 !$#contents annotation CLASSIFICATION #superfamily herpesvirus ribonucleoside-diphosphate !1reductase large chain KEYWORDS deoxyribonucleotide biosynthesis; early protein; !1oxidoreductase; redox-active disulfide FEATURE !$187-403,822-825 #disulfide_bonds redox-active #status predicted\ !$387,391 #active_site Asn, Glu #status predicted\ !$389 #active_site Cys (cysteine thiyl radical !8intermediate) #status predicted SUMMARY #length 826 #molecular-weight 93030 #checksum 821 SEQUENCE /// ENTRY WMBE19 #type complete TITLE ribonucleoside-diphosphate reductase (EC 1.17.4.1) large chain - human herpesvirus 3 ALTERNATE_NAMES ribonucleotide reductase large chain ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 11-Jun-1999 ACCESSIONS A27343 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession A27343 !'##molecule_type DNA !'##residues 1-775 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27902.1; !1PID:g60008 GENETICS !$#gene 19 CLASSIFICATION #superfamily herpesvirus ribonucleoside-diphosphate !1reductase large chain KEYWORDS deoxyribonucleotide biosynthesis; early protein; !1oxidoreductase; redox-active disulfide FEATURE !$216-444,770-773 #disulfide_bonds redox-active #status predicted\ !$427,431 #active_site Asn, Glu #status predicted\ !$429 #active_site Cys (cysteine thiyl radical !8intermediate) #status predicted SUMMARY #length 775 #molecular-weight 86827 #checksum 2100 SEQUENCE /// ENTRY WMBEA2 #type complete TITLE ribonucleoside-diphosphate reductase (EC 1.17.4.1) large chain - equine herpesvirus 1 (strain Ab4p) ALTERNATE_NAMES ribonucleotide reductase large chain ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 11-Jun-1999 ACCESSIONS D36797 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession D36797 !'##molecule_type DNA !'##residues 1-790 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02456.1; !1PID:g330813 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 21 CLASSIFICATION #superfamily herpesvirus ribonucleoside-diphosphate !1reductase large chain KEYWORDS deoxyribonucleotide biosynthesis; early protein; !1oxidoreductase; redox-active disulfide FEATURE !$224-453,785-788 #disulfide_bonds redox-active #status predicted\ !$436,440 #active_site Asn, Glu #status predicted\ !$438 #active_site Cys (cysteine thiyl radical !8intermediate) #status predicted SUMMARY #length 790 #molecular-weight 88398 #checksum 6377 SEQUENCE /// ENTRY WMBEP6 #type complete TITLE ribonucleoside-diphosphate reductase (EC 1.17.4.1) large chain - saimiriine herpesvirus 1 (strain 11) ALTERNATE_NAMES ribonucleotide reductase large chain ORGANISM #formal_name saimiriine herpesvirus 1 #note host Saimiri sciureus (common squirrel monkey) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 11-Jun-1999 ACCESSIONS E36812 REFERENCE A36806 !$#authors Albrecht, J. !$#submission submitted to the EMBL Data Library, January 1992 !$#description Primary structure of the herpesvirus saimiri genome. !$#accession E36812 !'##molecule_type DNA !'##residues 1-767 ##label ALB !'##cross-references GB:X64346; NID:g60320; PIDN:CAA45684.1; PID:g60382 REFERENCE A37309 !$#authors Albrecht, J.C.; Nicholas, J.; Biller, D.; Cameron, K.R.; !1Biesinger, B.; Newman, C.; Wittmann, S.; Craxton, M.A.; !1Coleman, H.; Fleckenstein, B.; Honess, R.W. !$#journal J. Virol. (1992) 66:5047-5058 !$#title Primary structure of the herpesvirus saimiri genome. !$#cross-references MUID:92333688; PMID:1321287 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 61 CLASSIFICATION #superfamily herpesvirus ribonucleoside-diphosphate !1reductase large chain KEYWORDS deoxyribonucleotide biosynthesis; early protein; !1oxidoreductase; redox-active disulfide FEATURE !$192-408,763-766 #disulfide_bonds redox-active #status predicted\ !$392,396 #active_site Asn, Glu #status predicted\ !$394 #active_site Cys (cysteine thiyl radical !8intermediate) #status predicted SUMMARY #length 767 #molecular-weight 87216 #checksum 7415 SEQUENCE /// ENTRY RDEC1R #type complete TITLE ribonucleoside-diphosphate reductase (EC 1.17.4.1) 1 alpha chain [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES ribonucleotide reductase B1 protein; ribonucleotide reductase R1 protein ORGANISM #formal_name Escherichia coli DATE 17-May-1985 #sequence_revision 21-Nov-1997 #text_change 01-Mar-2002 ACCESSIONS H64993; S00926; A60900; A00526; S01259 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64993 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-761 ##label BLAT !'##cross-references GB:AE000313; GB:U00096; NID:g2367132; !1PIDN:AAC75294.1; PID:g2367133; UWGP:b2234 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S00926 !$#authors Nilsson, O.; Aberg, A.; Lundqvist, T.; Sjoeberg, B.M. !$#journal Nucleic Acids Res. (1988) 16:4174 !$#title Nucleotide sequence of the gene coding for the large subunit !1of ribonucleotide reductase of Escherichia coli. Correction. !$#cross-references MUID:88234023; PMID:3287341 !$#accession S00926 !'##molecule_type DNA !'##residues 1-525,'ND',528-761 ##label NIL !'##cross-references EMBL:X06999; NID:g42137; PIDN:CAA30056.1; !1PID:g42138 REFERENCE A60900 !$#authors Sjoeberg, B.M.; Eriksson, S.; Joernvall, H.; Carlquist, M.; !1Eklund, H. !$#journal Eur. J. Biochem. (1985) 150:423-427 !$#title Protein B1 of ribonucleotide reductase. Direct analytical !1data and comparisons with data indirectly deduced from the !1nucleotide sequence of the Escherichia coli nrdA gene. !$#cross-references MUID:85257670; PMID:3894026 !$#accession A60900 !'##molecule_type protein !'##residues 1-12,'X';'X',143,'X',145-149,'X',151,'X',153-157;213-215, !1'X',217-219,'X',221-226,'X',228-229;247-251;509,'XX', !1512-522,'X',524-526 ##label SJO REFERENCE A00526 !$#authors Carlson, J.; Fuchs, J.A.; Messing, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:4294-4297 !$#title Primary structure of the Escherichia coli ribonucleoside !1diphosphate reductase operon. !$#cross-references MUID:84272624; PMID:6087316 !$#contents annotation !$#note this sequence has been extensively revised REFERENCE A68658 !$#authors Eriksson, M.; Eklund, H. !$#submission submitted to the Brookhaven Protein Data Bank, July 1997 !$#cross-references PDB:2R1R !$#contents annotation; X-ray crystallography, 3.0 angstroms, residues !15-737 REFERENCE A68696 !$#authors Eriksson, M.; Eklund, H. !$#submission submitted to the Brookhaven Protein Data Bank, July 1997 !$#cross-references PDB:3R1R !$#contents annotation; X-ray crystallography, 3.0 angstroms, residues !15-737 REFERENCE A58858 !$#authors Uhlin, U.; Eklund, H. !$#journal Nature (1994) 370:533-539 !$#title Structure of ribonucleotide reductase protein R1. !$#cross-references MUID:94329174; PMID:8052308 !$#contents annotation; X-ray crystallography, 3.0 angstroms COMMENT Heterogeneity in processing the amino end is observed. Both !11-Met and 2-Asn can be removed, and a 25 residue !1amino-terminal peptide may be removed under some metabolic !1conditions. GENETICS !$#gene nrdA !$#map_position 49 COMPLEX heterotetramer of two alpha chains (the R1 or B1 homodimer) !1and two beta chains (the R2 or B2 homodimer, see PIR:RDEC2R) FUNCTION !$#description catalyzes the reduction of ribonucleoside diphosphates by !1reduced thioredoxin to the corresponding deoxyribonucleoside !1diphosphates and water !$#pathway deoxyribonucleotide biosynthesis CLASSIFICATION #superfamily herpesvirus ribonucleoside-diphosphate !1reductase large chain KEYWORDS deoxyribonucleotide biosynthesis; heterotetramer; !1oxidoreductase; redox-active disulfide FEATURE !$1-761 #product ribonucleoside-diphosphate reductase alpha !8chain #status experimental #label ALF\ !$26-761 #product ribonucleoside-diphosphate reductase alpha' !8chain #status predicted #label ALP\ !$225-462 #disulfide_bonds redox-active #status experimental\ !$437,441 #active_site Asn, Glu #status predicted\ !$439 #active_site Cys (cysteine thiyl radical !8intermediate) #status predicted\ !$754-759 #disulfide_bonds redox-active #status predicted SUMMARY #length 761 #molecular-weight 85774 #checksum 3226 SEQUENCE /// ENTRY H64604 #type complete TITLE ribonucleoside-diphosphate reductase (EC 1.17.4.1) 1 alpha chain [similarity] - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS H64604 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession H64604 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-788 ##label TOM !'##cross-references GB:AE000581; GB:AE000511; NID:g2313802; !1PIDN:AAD14884.1; PID:g2313806; TIGR:HP0680 GENETICS !$#start_codon TTG CLASSIFICATION #superfamily herpesvirus ribonucleoside-diphosphate !1reductase large chain KEYWORDS deoxyribonucleotide biosynthesis; oxidoreductase; !1redox-active disulfide FEATURE !$216-497,784-787 #disulfide_bonds redox-active #status predicted\ !$424,428 #active_site Asn, Glu #status predicted\ !$426 #active_site Cys (cysteine thiyl radical !8intermediate) #status predicted SUMMARY #length 788 #molecular-weight 90159 #checksum 8940 SEQUENCE /// ENTRY F71908 #type complete TITLE ribonucleoside-diphosphate reductase 1 alpha chain [similarity] - Helicobacter pylori (strain J99) ORGANISM #formal_name Helicobacter pylori #variety strain J99 DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS F71908 REFERENCE A71800 !$#authors Alm, R.A.; Ling, L.S.L.; Moir, D.T.; King, B.L.; Brown, !1E.D.; Doig, P.C.; Smith, D.R.; Noonan, B.; Guild, B.C.; !1deJonge, B.L.; Carmel, G.; Tummino, P.J.; Caruso, A.; !1Uria-Nickelsen, M.; Mills, D.M.; Ives, C.; Gibson, R.; !1Merberg, D.; Mills, S.D.; Jiang, Q.; Taylor, D.E.; Vovis, !1G.F.; Trust, T.J. !$#journal Nature (1999) 397:176-180 !$#title Genomic sequence comparison of two unrelated isolates of the !1human gastric pathogen Helicobacter pylori. !$#cross-references MUID:99120557; PMID:9923682 !$#accession F71908 !'##molecule_type DNA !'##residues 1-788 ##label ARN !'##cross-references GB:AE001494; GB:AE001439; NID:g4155170; !1PIDN:AAD06201.1; PID:g4155174 !'##experimental_source strain J99 GENETICS !$#gene nrdA CLASSIFICATION #superfamily herpesvirus ribonucleoside-diphosphate !1reductase large chain SUMMARY #length 788 #molecular-weight 90231 #checksum 7501 SEQUENCE /// ENTRY D70309 #type complete TITLE ribonucleoside-diphosphate reductase (EC 1.17.4.1) alpha chain [similarity] - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS D70309 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession D70309 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-801 ##label AQF !'##cross-references GB:AE000673; NID:g2982834; PIDN:AAC06460.1; !1PID:g2982838; GB:AE000657 !'##experimental_source strain VF5 GENETICS !$#gene nrdA CLASSIFICATION #superfamily herpesvirus ribonucleoside-diphosphate !1reductase large chain KEYWORDS deoxyribonucleotide biosynthesis; oxidoreductase; !1redox-active disulfide FEATURE !$235-521,796-799 #disulfide_bonds redox-active #status predicted\ !$483,487 #active_site Asn, Glu #status predicted\ !$485 #active_site Cys (cysteine thiyl radical !8intermediate) #status predicted SUMMARY #length 801 #molecular-weight 92913 #checksum 5449 SEQUENCE /// ENTRY B71255 #type complete TITLE ribonucleoside-diphosphate reductase (EC 1.17.4.1) alpha chain [similarity] - syphilis spirochete ORGANISM #formal_name Treponema pallidum subsp. pallidum #common_name syphilis spirochete DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 05-May-2000 ACCESSIONS B71255 REFERENCE A71250 !$#authors Fraser, C.M.; Norris, S.J.; Weinstock, G.M.; White, O.; !1Sutton, G.G.; Dodson, R.; Gwinn, M.; Hickey, E.K.; Clayton, !1R.; Ketchum, K.A.; Sodergren, E.; Hardham, J.M.; McLeod, !1M.P.; Salzberg, S.; Peterson, J.; Khalak, H.; Richardson, !1D.; Howell, J.K.; Chidambaram, M.; Utterback, T.; McDonald, !1L.; Artiach, P.; Bowman, C.; Cotton, M.D.; Fujii, C.; !1Garland, S.; Hatch, B.; Horst, K.; Roberts, K.; Watthey, L.; !1Weidman, J.; Smith, H.O.; Venter, J.C. !$#journal Science (1998) 281:375-388 !$#title Complete genome sequence of Treponema pallidum, the syphilis !1spirochete. !$#cross-references MUID:98332770; PMID:9665876 !$#accession B71255 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-845 ##label COL !'##cross-references GB:AE001268; GB:AE000520; NID:g3323326; !1PIDN:AAC65956.1; PID:g3323332 !'##experimental_source strain Nichols GENETICS !$#gene TP1008 CLASSIFICATION #superfamily herpesvirus ribonucleoside-diphosphate !1reductase large chain KEYWORDS oxidoreductase SUMMARY #length 845 #molecular-weight 95986 #checksum 5175 SEQUENCE /// ENTRY S75875 #type complete TITLE ribonucleoside-diphosphate reductase (EC 1.17.4.1) alpha chain [similarity] - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein slr1164; ribonucleotide reductase alpha chain ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 16-Jun-2000 ACCESSIONS S75875 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75875 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-767 ##label KAN !'##cross-references EMBL:D90913; GB:AB001339; NID:g1653348; !1PIDN:BAA18334.1; PID:g1653420 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene nrdA CLASSIFICATION #superfamily herpesvirus ribonucleoside-diphosphate !1reductase large chain KEYWORDS oxidoreductase SUMMARY #length 767 #molecular-weight 85636 #checksum 1371 SEQUENCE /// ENTRY Z6BPT9 #type complete TITLE ribonucleoside-triphosphate reductase, oxygen-sensitive (EC 1.17.4.-) - phage T4 ALTERNATE_NAMES gene 55.11 protein ORGANISM #formal_name phage T4 DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 11-Jun-1999 ACCESSIONS E29284 REFERENCE A30291 !$#authors Tomaschewski, J.; Rueger, W. !$#journal Nucleic Acids Res. (1987) 15:3632-3633 !$#title Nucleotide sequence and primary structures of gene products !1coded for by the T4 genome between map positions 48.266 kb !1and 39.166 kb. !$#cross-references MUID:87203398; PMID:3575111 !$#accession E29284 !'##molecule_type DNA !'##residues 1-397 ##label TOM !'##cross-references GB:Y00122; NID:g15346; PIDN:CAA68310.1; PID:g15352 COMMENT This enzyme must be activated by the anaerobic !1ribonucleotide reductase activase (see PIR:Z8BPT9) to !1generate the glycyl free radical active site. Oxygen !1destroys this active site and causes peptide cleavage. GENETICS !$#gene 55.11 FUNCTION !$#description catalyzes the reduction by reduced thioredoxin of a !1ribonucleoside triphosphate to a 2'-deoxyribonucleoside !1triphosphate and water !$#pathway deoxyribonucleotide biosynthesis !$#note this enzyme is different both from !1ribonucleoside-triphosphate reductase (EC 1.17.4.2), which !1uses a cobalamine cofactor, and from !1ribonucleoside-diphosphate reductase (EC 1.17.4.1), which !1binds iron and has a tyrosyl radical CLASSIFICATION #superfamily phage T4 oxygen-sensitive !1ribonucleoside-triphosphate reductase; oxygen-sensitive !1ribonucleoside-triphosphate reductase carboxyl-terminal !1homology; rubredoxin homology KEYWORDS deoxyribonucleotide biosynthesis; iron; metalloprotein; !1oxidoreductase FEATURE !$1-397 #domain oxygen-sensitive ribonucleoside-triphosphate !8reductase carboxyl-terminal homology #label ARRC\ !$332-362 #domain rubredoxin homology #status atypical #label !8RUB\ !$335,338,353,356 #binding_site iron (Cys) #status predicted\ !$372 #active_site Gly (stable glycyl radical) #status !8predicted SUMMARY #length 397 #molecular-weight 44793 #checksum 3503 SEQUENCE /// ENTRY A47331 #type complete TITLE ribonucleoside-triphosphate reductase, oxygen-sensitive (EC 1.17.4.-) - Escherichia coli (strain K-12) ALTERNATE_NAMES anaerobic ribonucleotide reductase ORGANISM #formal_name Escherichia coli DATE 21-Sep-1993 #sequence_revision 19-Jan-1996 #text_change 01-Mar-2002 ACCESSIONS A47331; S56464; A65236 REFERENCE A47331 !$#authors Sun, X.; Harder, J.; Krook, M.; Jornvall, H.; Sjoberg, B.M.; !1Reichard, P. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:577-581 !$#title A possible glycine radical in anaerobic ribonucleotide !1reductase from Escherichia coli: nucleotide sequence of the !1cloned nrdD gene. !$#cross-references MUID:93133831; PMID:8421692 !$#accession A47331 !'##molecule_type DNA; protein !'##residues 1-256,'R',258-419,'P',421-712 ##label SUN !'##cross-references GB:L06097; NID:g146968; PIDN:AAA24226.1; !1PID:g146970 !'##note sequence extracted from NCBI backbone (NCBIN:122818, !1NCBIP:122819) !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56464 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-712 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97135.1; !1PID:g537080 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65236 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-712 ##label BLAT !'##cross-references GB:AE000495; GB:U00096; NID:g2367361; !1PIDN:AAC77195.1; PID:g1790686; UWGP:b4238 !'##experimental_source strain K-12, substrain MG1655 COMMENT This enzyme must be activated by the anaerobic !1ribonucleotide reductase activase (see PIR:A55692) to !1generate the glycyl free radical active site. Oxygen !1destroys this active site and causes peptide cleavage. GENETICS !$#gene nrdD !$#map_position 96 min COMPLEX homodimer FUNCTION !$#description catalyzes the reduction by reduced thioredoxin of a !1ribonucleoside triphosphate to a 2'-deoxyribonucleoside !1triphosphate and water !$#pathway deoxyribonucleotide biosynthesis !$#note this enzyme is different both from !1ribonucleoside-triphosphate reductase (EC 1.17.4.2), which !1uses a cobalamine cofactor, and from !1ribonucleoside-diphosphate reductase (EC 1.17.4.1), which !1binds iron and has a tyrosyl radical CLASSIFICATION #superfamily Escherichia coli oxygen-sensitive !1ribonucleoside-triphosphate reductase; oxygen-sensitive !1ribonucleoside-triphosphate reductase carboxyl-terminal !1homology; oxygen-sensitive ribonucleoside-triphosphate !1reductase middle homology; rubredoxin homology KEYWORDS deoxyribonucleotide biosynthesis; homodimer; iron; !1metalloprotein; oxidoreductase FEATURE !$96-279 #domain oxygen-sensitive ribonucleoside-triphosphate !8reductase middle homology #label ARRM\ !$305-706 #domain oxygen-sensitive ribonucleoside-triphosphate !8reductase carboxyl-terminal homology #label ARRC\ !$641-671 #domain rubredoxin homology #status atypical #label !8RUB\ !$644,647,662,665 #binding_site iron (Cys) #status predicted\ !$681 #active_site Gly (stable glycyl radical) #status !8predicted SUMMARY #length 712 #molecular-weight 80022 #checksum 6582 SEQUENCE /// ENTRY A64047 #type complete TITLE ribonucleoside-triphosphate reductase, oxygen-sensitive (EC 1.17.4.-) - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 18-Aug-1995 #sequence_revision 19-Jan-1996 #text_change 11-Jun-1999 ACCESSIONS A64047 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession A64047 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-707 ##label TIGR !'##cross-references GB:U32693; GB:L42023; NID:g1573021; !1PIDN:AAC21751.1; PID:g1573024; TIGR:HI0075 COMMENT This enzyme must be activated by the anaerobic !1ribonucleotide reductase activase (see PIR:E64168) to !1generate the glycyl free radical active site. Oxygen !1destroys this active site and causes peptide cleavage. FUNCTION !$#description catalyzes the reduction by reduced thioredoxin of a !1ribonucleoside triphosphate to a 2'-deoxyribonucleoside !1triphosphate and water !$#pathway deoxyribonucleotide biosynthesis !$#note this enzyme is different both from !1ribonucleoside-triphosphate reductase (EC 1.17.4.2), which !1uses a cobalamine cofactor, and from !1ribonucleoside-diphosphate reductase (EC 1.17.4.1), which !1binds iron and has a tyrosyl radical CLASSIFICATION #superfamily Escherichia coli oxygen-sensitive !1ribonucleoside-triphosphate reductase; oxygen-sensitive !1ribonucleoside-triphosphate reductase carboxyl-terminal !1homology; oxygen-sensitive ribonucleoside-triphosphate !1reductase middle homology; rubredoxin homology KEYWORDS deoxyribonucleotide biosynthesis; iron; metalloprotein; !1oxidoreductase FEATURE !$99-282 #domain oxygen-sensitive ribonucleoside-triphosphate !8reductase middle homology #label ARRM\ !$308-707 #domain oxygen-sensitive ribonucleoside-triphosphate !8reductase carboxyl-terminal homology #label ARRC\ !$642-672 #domain rubredoxin homology #status atypical #label !8RUB\ !$645,648,663,666 #binding_site iron (Cys) #status predicted\ !$682 #active_site Gly (stable glycyl radical) #status !8predicted SUMMARY #length 707 #molecular-weight 80233 #checksum 1932 SEQUENCE /// ENTRY RDDVBX #type complete TITLE rubredoxin-NAD+ reductase (EC 1.18.1.1) rbo - Desulfovibrio vulgaris (strain Hildenborough) ALTERNATE_NAMES desulfoferrodoxin 2; desulforedoxin ORGANISM #formal_name Desulfovibrio vulgaris DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 03-Jun-2002 ACCESSIONS A33962; B36498 REFERENCE A33962 !$#authors Brumlik, M.J.; Voordouw, G. !$#journal J. Bacteriol. (1989) 171:4996-5004 !$#title Analysis of the transcriptional unit encoding the genes for !1rubredoxin (rub) and a putative rubredoxin oxidoreductase !1(rbo) in Desulfovibrio vulgaris Hildenborough. !$#cross-references MUID:89359139; PMID:2549009 !$#accession A33962 !'##molecule_type DNA !'##residues 1-126 ##label BRU !'##cross-references GB:M28848; NID:g342028; PIDN:AAA64797.1; !1PID:g758676 !'##experimental_source strain Hildenborough REFERENCE A36498 !$#authors Moura, I.; Tavares, P.; Moura, J.J.G.; Ravi, N.; Huynh, !1B.H.; Liu, M.Y.; LeGall, J. !$#journal J. Biol. Chem. (1990) 265:21596-21602 !$#title Purification and characterization of desulfoferrodoxin. A !1novel protein from Desulfovibrio desulfuricans (ATCC 27774) !1and from Desulfovibrio vulgaris (strain Hildenborough) that !1contains a distorted rubredoxin center and a mononuclear !1ferrous center. !$#cross-references MUID:91072356; PMID:2174880 !$#accession B36498 !'##molecule_type protein !'##residues 'M',3-9,'X',11-12,'X',14-28,'XX',31,'X',33-34,'XX',37,'X', !139-40,'X',42-45 ##label MOU !'##experimental_source strain Hildenborough !'##note report lack of rubredoxin-NAD+ reductase activity REFERENCE A30644 !$#authors Verhagen, M.F.J.M.; Voorhorst, W.G.B.; Kolkman, J.A.; !1Wolbert, R.B.G.; Hagen, W.R. !$#journal FEBS Lett. (1993) 336:13-18 !$#title On the two iron centers of desulfoferrodoxin. !$#cross-references MUID:94085568; PMID:8262195 !$#contents annotation !$#note report presence of rubredoxin-NAD+ reductase activity COMMENT This is probably an enzyme that serves to reduce rubredoxin, !1but there is disagreement about whether nicotinamide !1dinucleotides can serve as reducing agents. COMMENT There is a second ferrous iron-binding site that is not well !1characterized but probably consists of nitrogen and oxygen !1ligands. GENETICS !$#gene rbo CLASSIFICATION #superfamily rubredoxin-NAD+ reductase rbo; desulforedoxin !1homology KEYWORDS iron; metalloprotein; oxidoreductase FEATURE !$1-37 #domain desulforedoxin homology #label DSX\ !$2-126 #product rubredoxin-NAD+ reductase #status !8experimental #label MAT\ !$10,13,29,30 #binding_site iron (Cys) #status predicted SUMMARY #length 126 #molecular-weight 13983 #checksum 1270 SEQUENCE /// ENTRY RDSGXX #type complete TITLE ferredoxin-NADP reductase (EC 1.18.1.2) - Spirulina sp. ALTERNATE_NAMES ferredoxin oxidoreductase ORGANISM #formal_name Spirulina sp. DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 03-Jun-2002 ACCESSIONS A00531; A61303 REFERENCE A00531 !$#authors Yao, Y.; Tamura, T.; Wada, K.; Matsubara, H.; Kodo, K. !$#journal J. Biochem. (1984) 95:1513-1516 !$#title Spirulina ferredoxin-NADP+ reductase. The complete amino !1acid sequence. !$#cross-references MUID:84264466; PMID:6430889 !$#accession A00531 !'##molecule_type protein !'##residues 1-294 ##label YAO REFERENCE A61303 !$#authors Wada, K.; Tamura, T.; Matsubara, H.; Kodo, K. !$#journal J. Biochem. (1983) 94:387-393 !$#title Spirulina ferredoxin-NADP+ reductase. Further !1characterization with an improved preparation. !$#cross-references MUID:84032337; PMID:6415047 !$#accession A61303 !'##molecule_type protein !'##residues 1-10;289-291,'Q',293-294 ##label WAD REFERENCE A00530 !$#authors Yao, Y.; Tamura, T.; Wada, K.; Matsubara, H.; Kodo, K. !$#journal J. Biochem. (1984) 96:935 !$#contents annotation COMMENT This FAD-containing enzyme forms a one-to-one complex with !1ferredoxin and NADP and catalyzes the electron transfer from !1reduced ferredoxin to NADP. FUNCTION !$#description catalyzes the reversible reduction of NADP+ by reduced !1ferredoxin or reduced flavodoxin !$#pathway photosynthesis !$#note reversible reaction CLASSIFICATION #superfamily ferredoxin-NADP+ reductase; cytochrome-b5 !1reductase homology KEYWORDS electron transfer; FAD; flavoprotein; NADP; oxidoreductase; !1photosynthesis FEATURE !$1-141 #domain FAD binding #label FAD\ !$23-279 #domain cytochrome-b5 reductase homology #label CBR\ !$142-294 #domain NADP binding #label NADP SUMMARY #length 294 #molecular-weight 33349 #checksum 9121 SEQUENCE /// ENTRY S33479 #type complete TITLE ferredoxin-NADP reductase (EC 1.18.1.2) precursor [validated] - Anabaena sp. (PCC 7119) ALTERNATE_NAMES ferredoxin oxidoreductase ORGANISM #formal_name Anabaena sp. #variety PCC 7119 DATE 02-Dec-1993 #sequence_revision 10-May-1996 #text_change 03-Jun-2002 ACCESSIONS S35150; S13103; A27581; S33479 REFERENCE S35150 !$#authors Fillat, M.F.; Flores, E.; Gomez-Moreno, C. !$#journal Plant Mol. Biol. (1993) 22:725-729 !$#title Homology of the N-terminal domain of the petH gene product !1from Anabaena sp. PCC 7119 to the CpcD phycobilisome linker !1polypeptide. !$#cross-references MUID:93344523; PMID:8343609 !$#accession S35150 !'##molecule_type DNA !'##residues 1-440 ##label FIL1 !'##cross-references EMBL:X72394; NID:g4239683; PIDN:CAA51088.1; !1PID:g311533 !'##experimental_source PCC 7119 REFERENCE S13103 !$#authors Fillat, M.F.; Bakker, H.A.C.; Weisbeek, P.J. !$#journal Nucleic Acids Res. (1990) 18:7161 !$#title Sequence of the ferredoxin-NADP(+)-reductase gene from !1Anabaena PCC 7119. !$#cross-references MUID:91088322; PMID:2124680 !$#accession S13103 !'##molecule_type DNA !'##residues 137-440 ##label FIL2 !'##cross-references EMBL:X54039; NID:g39250; PIDN:CAA37973.1; !1PID:g39251 !'##experimental_source PCC 7119; ATCC 29151 REFERENCE A27581 !$#authors Sancho, J.; Peleato, M.L.; Gomez-Moreno, C.; Edmondson, D.E. !$#journal Arch. Biochem. Biophys. (1988) 260:200-207 !$#title Purification and properties of ferredoxin-NADP !1oxidoreductase from the nitrogen-fixing cyanobacteria !1Anabaena variabilis. !$#cross-references MUID:88132819; PMID:3124746 !$#accession A27581 !'##molecule_type protein !'##residues 152-161,'X',163-170,'X',172-174,'XX',177-179,'L',181-183 !1##label SAN !'##experimental_source strain 1403.46 REFERENCE A66455 !$#authors Serre, L.; Frey, M.; Vellieux, F.M.D. !$#submission submitted to the Brookhaven Protein Data Bank, July 1996 !$#cross-references PDB:1QUE !$#contents annotation; X-ray crystallography, 1.80 angstroms, residues !1138-382,'Q',384-440 REFERENCE A58632 !$#authors Serre, L.; Vellieux, F.M.D.; Medina, M.; Gomez-Moreno, C.; !1Fontecilla-Camps, J.C.; Frey, M. !$#journal J. Mol. Biol. (1996) 263:20-39 !$#title X-ray structure of the ferredoxin:NADP+ reductase from the !1cyanobacterium Anabaena PCC 7119 at 1.8 Angstroms !1resolution, and crystallographic studies of NADP+ binding at !12.25 Angstroms resolution. !$#cross-references MUID:97045988; PMID:8890910 !$#contents annotation; X-ray crystallography, 1.80 angstroms GENETICS !$#gene petH FUNCTION !$#description catalyzes the reversible reduction of NADP+ by reduced !1ferredoxin or reduced flavodoxin !$#pathway photosynthesis !$#note FAD cofactor CLASSIFICATION #superfamily ferredoxin-NADP+ reductase; cytochrome-b5 !1reductase homology KEYWORDS electron transfer; FAD; flavoprotein; NADP; oxidoreductase; !1photosynthesis FEATURE !$1-134 #domain signal sequence #status predicted #label SIG\ !$135-440 #product ferredoxin-NADP+ reductase #status predicted !8#label MAT\ !$139-283 #domain FAD binding #status predicted #label FAD\ !$165-425 #domain cytochrome-b5 reductase homology #label CBR\ !$284-440 #domain NADP binding #status predicted #label NADP SUMMARY #length 440 #molecular-weight 48865 #checksum 2938 SEQUENCE /// ENTRY B42194 #type complete TITLE ferredoxin-NADP reductase (EC 1.18.1.2) - Synechococcus sp. (PCC 7002) ORGANISM #formal_name Synechococcus sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS B42194 REFERENCE A42194 !$#authors Schluchter, W.M.; Bryant, D.A. !$#journal Biochemistry (1992) 31:3092-3102 !$#title Molecular characterization of ferredoxin-NADP+ !1oxidoreductase in cyanobacteria: cloning and sequence of the !1petH gene of Synechococcus sp. PCC 7002 and studies on the !1gene product. !$#cross-references MUID:92207922; PMID:1554697 !$#accession B42194 !'##status preliminary !'##molecule_type DNA !'##residues 1-402 ##label SCH !'##experimental_source PCC 7002 !'##note this sequence is inconsistent with the nucleotide translation !'##note sequence extracted from NCBI backbone (NCBIP:91789) GENETICS !$#gene petH CLASSIFICATION #superfamily ferredoxin-NADP+ reductase; cytochrome-b5 !1reductase homology KEYWORDS FAD; flavoprotein; NADP; oxidoreductase FEATURE !$130-387 #domain cytochrome-b5 reductase homology #label CBR SUMMARY #length 402 #molecular-weight 44953 #checksum 9666 SEQUENCE /// ENTRY RDSPXX #type complete TITLE ferredoxin-NADP reductase (EC 1.18.1.2) precursor, leaf [validated] - spinach ALTERNATE_NAMES ferredoxin oxidoreductase ORGANISM #formal_name Spinacia oleracea #common_name spinach DATE 28-May-1986 #sequence_revision 30-Sep-1993 #text_change 03-Jun-2002 ACCESSIONS S00438; A00532; S30285; S09584; S14225; S25698 REFERENCE S00438 !$#authors Jansen, T.; Reilaender, H.; Steppuhn, J.; Herrmann, R.G. !$#journal Curr. Genet. (1988) 13:517-522 !$#title Analysis of cDNA clones encoding the entire !1precursor-polypeptide for ferredoxin:NADP+ oxidoreductase !1from spinach. !$#cross-references MUID:88295233; PMID:2969782 !$#accession S00438 !'##molecule_type mRNA !'##residues 1-369 ##label JAN !'##cross-references EMBL:X07981; NID:g21246; PIDN:CAA30791.1; !1PID:g21247 !'##note 324-Val was also found REFERENCE A00532 !$#authors Karplus, P.A.; Walsh, K.A.; Herriott, J.R. !$#journal Biochemistry (1984) 23:6576-6583 !$#title Amino acid sequence of spinach ferredoxin:NADP(+) !1oxidoreductase. !$#cross-references MUID:85150075; PMID:6529571 !$#accession A00532 !'##molecule_type protein !'##residues 56-323,'V',325-369 ##label KAR REFERENCE S30285 !$#authors Oelmueller, R.; Bolle, C.; Tyagi, A.K.; Niekrawietz, N.; !1Breit, S. !$#journal Mol. Gen. Genet. (1993) 237:261-272 !$#title Characterization of the promoter from the single-copy gene !1encoding ferredoxin-NADP(+)-oxidoreductase from spinach. !$#cross-references MUID:93204903; PMID:8455561 !$#accession S30285 !'##molecule_type DNA !'##residues 1-120 ##label OEL !'##cross-references EMBL:X64351; NID:g21249; PIDN:CAA45703.1; !1PID:g21250 !'##experimental_source strain var. Monatol; seedling REFERENCE S09584 !$#authors Shin, M.; Tsujita, M.; Tomizawa, H.; Sakihama, N.; Kamei, !1K.; Oshino, R. !$#journal Arch. Biochem. Biophys. (1990) 279:97-103 !$#title Proteolytic degradation of ferredoxin-NADP reductase during !1purification from spinach. !$#cross-references MUID:90247900; PMID:2186705 !$#accession S09584 !'##molecule_type protein !'##residues 57-62;67-78 ##label SHI REFERENCE A50129 !$#authors Karplus, P.A.; Daniels, M.J.; Herriott, J.R. !$#submission submitted to the Brookhaven Protein Data Bank, June 1990 !$#cross-references PDB:1FNR !$#contents annotation; X-ray structure at 2.2 Angstrom resolution GENETICS !$#genome nuclear !$#introns 36/3 FUNCTION !$#description catalyzes the reversible reduction of NADP+ by reduced !1ferredoxin or reduced flavodoxin !$#pathway photosynthesis !$#note reversible reaction; FAD cofactor CLASSIFICATION #superfamily ferredoxin-NADP+ reductase; cytochrome-b5 !1reductase homology KEYWORDS chloroplast; electron transfer; FAD; flavoprotein; leaf; !1NADP; oxidoreductase; photosynthesis FEATURE !$1-55 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$56-369 #product ferredoxin-NADP+ reductase #status !8experimental #label MAT\ !$74-216 #domain FAD binding #status predicted #label FAD\ !$100-354 #domain cytochrome-b5 reductase homology #label CBR\ !$217-369 #domain NADP binding #status predicted #label NADP SUMMARY #length 369 #molecular-weight 41188 #checksum 3789 SEQUENCE /// ENTRY A44974 #type complete TITLE ferredoxin-NADP reductase (EC 1.18.1.2) precursor - common ice plant ORGANISM #formal_name Mesembryanthemum crystallinum #common_name common ice plant DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS A44974 REFERENCE A44974 !$#authors Michalowski, C.B.; Schmitt, J.M.; Bohnert, H.J. !$#journal Plant Physiol. (1989) 89:817-822 !$#title Expression during salt stress and nucleotide sequence of !1cDNA for ferredoxin-NADP(+) reductase from Mesembryanthemum !1crystallinum. !$#accession A44974 !'##status preliminary !'##molecule_type mRNA !'##residues 1-365 ##label MIC !'##cross-references GB:M25528; GB:X13884; NID:g167255; PIDN:AAA33029.1; !1PID:g167256 CLASSIFICATION #superfamily ferredoxin-NADP+ reductase; cytochrome-b5 !1reductase homology KEYWORDS electron transfer; FAD; flavoprotein; NADP; oxidoreductase FEATURE !$96-350 #domain cytochrome-b5 reductase homology #label CBR SUMMARY #length 365 #molecular-weight 41063 #checksum 8422 SEQUENCE /// ENTRY S04030 #type complete TITLE ferredoxin-NADP reductase (EC 1.18.1.2) precursor - garden pea ORGANISM #formal_name Pisum sativum #common_name garden pea DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S04030 REFERENCE S04030 !$#authors Newman, B.J.; Gray, J.C. !$#journal Plant Mol. Biol. (1988) 10:511-520 !$#title Characterisation of a full-length cDNA clone for pea !1ferredoxin-NADP(+) reductase. !$#accession S04030 !'##molecule_type mRNA !'##residues 1-360 ##label NEW !'##cross-references EMBL:X12446; NID:g20721; PIDN:CAA30978.1; !1PID:g20722 !'##experimental_source cultivar Little Marvel !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing !'##note 59-Glu was also found GENETICS !$#gene fnr !$#genome nuclear COMPLEX monomer FUNCTION !$#description catalyzes electron transfer from reduced ferredoxin to NADP !$#pathway photosynthesis !$#note FAD cofactor CLASSIFICATION #superfamily ferredoxin-NADP+ reductase; cytochrome-b5 !1reductase homology KEYWORDS chloroplast; electron transfer; FAD; flavoprotein; NADP; !1oxidoreductase; photosynthesis FEATURE !$1-52 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$53-360 #product ferredoxin-NADP+ reductase #status !8experimental #label MAT\ !$69-207 #domain FAD binding #status predicted #label FAD\ !$91-345 #domain cytochrome-b5 reductase homology #label CBR\ !$208-360 #domain NADP binding #status predicted #label NADP SUMMARY #length 360 #molecular-weight 40194 #checksum 879 SEQUENCE /// ENTRY A56664 #type complete TITLE ferredoxin-NADP reductase (EC 1.18.1.2) precursor - Cyanophora paradoxa ORGANISM #formal_name Cyanophora paradoxa DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S33545; S38805; A56664; S30032 REFERENCE S33545 !$#authors Jakowitsch, J.; Bayer, M.G.; Maier, T.L.; Luettke, A.; !1Gebhart, U.B.; Brandtner, M.; Hamilton, B.; !1Neumann-Spallart, C.; Michalowski, C.B.; Bohnert, H.J.; !1Schenk, H.E.A.; Loeffelhardt, W. !$#journal Plant Mol. Biol. (1993) 21:1023-1033 !$#title Sequence analysis of pre-ferredoxin-NADP(+)-reductase cDNA !1from Cyanophora paradoxa specifying a precursor for a !1nucleus-encoded cyanelle polypeptide. !$#cross-references MUID:93257619; PMID:8490125 !$#accession S33545 !'##molecule_type mRNA !'##residues 1-363 ##label JAK !'##cross-references EMBL:X66372; NID:g18099; PIDN:CAA47015.1; !1PID:g18100 !'##experimental_source strain LB555 UTEX !$#accession S38805 !'##molecule_type protein !'##residues 66-90 ##label JA2 !'##experimental_source strain LB555 UTEX REFERENCE A56664 !$#authors Gebhart, U.B.; Maier, T.L.; Stevanovic, S.; Bayer, M.G.; !1Schenk, H.E. !$#journal Protein Expr. Purif. (1992) 3:228-235 !$#title Ferredoxin:NADP oxidoreductase of Cyanophora paradoxa: !1purification, partial characterization, and N-terminal amino !1acid sequence. !$#cross-references MUID:93005754; PMID:1392619 !$#accession A56664 !'##molecule_type protein !'##residues 67-90 ##label GEB !'##note a shorter form lacking the first four residues from the amino !1end was also found !'##note sequence extracted from NCBI backbone (NCBIP:119664) GENETICS !$#gene petH !$#genome nuclear COMPLEX monomer FUNCTION !$#description catalyzes electron transfer from reduced ferredoxin to NADP !$#pathway photosynthesis !$#note FAD cofactor CLASSIFICATION #superfamily ferredoxin-NADP+ reductase; cytochrome-b5 !1reductase homology KEYWORDS cyanelle; electron transfer; FAD; flavoprotein; NADP; !1oxidoreductase; photosynthesis FEATURE !$1-65 #domain transit peptide (cyanelle) #status predicted !8#label TNP\ !$66-363 #product ferredoxin-NADP+ reductase #status !8experimental #label MAT\ !$70-210 #domain FAD binding #status predicted #label FAD\ !$94-348 #domain cytochrome-b5 reductase homology #label CBR\ !$211-363 #domain NADP binding #status predicted #label NADP SUMMARY #length 363 #molecular-weight 40491 #checksum 9037 SEQUENCE /// ENTRY T03758 #type complete TITLE probable ferredoxin-NADP reductase (EC 1.18.1.2) precursor, root - rice ORGANISM #formal_name Oryza sativa #common_name rice DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS T03758; JS0728 REFERENCE Z15056 !$#authors Aoki, H.; Ida, S. !$#journal Biochim. Biophys. Acta (1994) 1183:553-556 !$#title Nucleotide sequence of a rice root ferredoxin-NADP+ !1reductase cDNA and its induction by nitrate. !$#cross-references MUID:94114560; PMID:8286405 !$#accession T03758 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-378 ##label AOK1 !'##cross-references EMBL:D17410; NID:g397841; PIDN:BAA04232.1; !1PID:g435647 !'##experimental_source subsp. japonica, cv. Kinmaze REFERENCE JS0728 !$#authors Aoki, H.; Ida, S. !$#submission submitted to JIPID, August 1992 !$#accession JS0728 !'##status translation not shown !'##molecule_type mRNA !'##residues 62-378 ##label AOK2 !'##cross-references DDBJ:D12815; NID:g218162; PIDN:BAA02248.1; !1PID:g218163 !'##experimental_source subsp. japonica, strain Kinmaze; root FUNCTION !$#description catalyzes the reversible reduction of NADP+ by reduced !1ferredoxin or reduced flavodoxin !$#note probably involved in the nitrate assimilation CLASSIFICATION #superfamily ferredoxin-NADP+ reductase; cytochrome-b5 !1reductase homology KEYWORDS electron transfer; FAD; flavoprotein; NADP; oxidoreductase; !1root FEATURE !$1-62 #domain transit peptide (plastid) #status predicted !8#label TNP\ !$63-378 #product ferredoxin-NADP+ reductase #status predicted !8#label MAT\ !$103-363 #domain cytochrome-b5 reductase homology #label CBR SUMMARY #length 378 #molecular-weight 41878 #checksum 9999 SEQUENCE /// ENTRY A40487 #type complete TITLE ferredoxin-NADP reductase (EC 1.18.1.2), long form, precursor - human ALTERNATE_NAMES adrenodoxin reductase ORGANISM #formal_name Homo sapiens #common_name man DATE 24-Jan-1992 #sequence_revision 18-Oct-1996 #text_change 03-Jun-2002 ACCESSIONS A40487; B40487; A36482 REFERENCE A40487 !$#authors Solish, S.B.; Picado-Leonard, J.; Morel, Y.; Kuhn, R.W.; !1Mohandas, T.K.; Hanukoglu, I.; Miller, W.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:7104-7108 !$#title Human adrenodoxin reductase: two mRNAs encoded by a single !1gene on chromosome 17cen->q25 are expressed in steroidogenic !1tissues. !$#cross-references MUID:89017146; PMID:2845396 !$#accession A40487 !'##molecule_type mRNA !'##residues 1-497 ##label SOL !'##cross-references GB:J03826; NID:g178212; PIDN:AAB59498.1; !1PID:g178214 !$#accession B40487 !'##molecule_type mRNA !'##residues 66-122,'R',124-203,210-497 ##label SO2 !'##cross-references GB:J03826 REFERENCE A36482 !$#authors Lin, D.; Shi, Y.; Miller, W.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:8516-8520 !$#title Cloning and sequence of the human adrenodoxin reductase !1gene. !$#cross-references MUID:91046028; PMID:2236061 !$#accession A36482 !'##molecule_type DNA !'##residues 1-122,'R',124-497 ##label LIN !'##cross-references GB:M38255; GB:M58509; GB:M38256; NID:g178206; !1PIDN:AAA51668.1; PID:g178208 COMMENT Ferredoxin-NADP+ reductase is localized in the matrix of !1adrenal cortex mitochondria and functions as a component of !1the mitochondrial steroid-hydroxylating enzyme system, which !1includes ferredoxin-NADP+ reductase, adrenodoxin and two !1forms of cytochrome P-450. GENETICS !$#gene GDB:FDXR; ADXR !'##cross-references GDB:119659; OMIM:103270 !$#map_position 17q24-17q25 FUNCTION !$#description catalyzes the reversible reduction of NADP+ by reduced !1ferredoxin or reduced flavodoxin CLASSIFICATION #superfamily human ferredoxin-NADP+ reductase KEYWORDS alternative splicing; electron transfer; flavoprotein; !1mitochondrion; monomer; NADP; oxidoreductase FEATURE !$1-32 #domain transit peptide (mitochondrion) #status !8predicted #label SIG\ !$33-497 #product ferredoxin-NADP+ reductase, long form !8#status predicted #label MAT\ !$33-203,210-497 #product ferredoxin-NADP+ reductase, short form !8#status predicted #label MA2\ !$40-69 #region beta-alpha-beta FAD nucleotide-binding fold\ !$179-189 #region NADP binding #status predicted\ !$280 #binding_site substrate (Lys) #status predicted SUMMARY #length 497 #molecular-weight 54450 #checksum 7386 SEQUENCE /// ENTRY JT0751 #type complete TITLE ferredoxin-NADP reductase (EC 1.18.1.2), long form precursor - bovine ALTERNATE_NAMES adrenodoxin reductase ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 14-Jul-1994 #sequence_revision 18-Oct-1996 #text_change 03-Jun-2002 ACCESSIONS JT0751; JT0079; JS0390; S03558; PS0003; A29604; S52100 REFERENCE JT0751 !$#authors Takata, Y.; Sagara, Y.; Kono, A.; Sekimizu, K.; Horiuchi, T. !$#journal Biol. Pharm. Bull. (1993) 16:1200-1206 !$#title Gene structure of bovine adrenodoxin reductase. !$#cross-references MUID:94177140; PMID:8130767 !$#accession JT0751 !'##molecule_type DNA !'##residues 1-498 ##label TAK !'##cross-references GB:D83475; NID:g1199916; PIDN:BAA11921.1; !1PID:g4521308 !'##experimental_source adrenal cortex !'##note the authors translated the codon GTC for residue 205 as Gly REFERENCE JT0079 !$#authors Sagara, Y.; Takata, Y.; Miyata, T.; Hara, T.; Horiuchi, T. !$#journal J. Biochem. (1987) 102:1333-1336 !$#title Cloning and sequence analysis of adrenodoxin reductase cDNA !1from bovine adrenal cortex. !$#cross-references MUID:88198050; PMID:3448086 !$#accession JT0079 !'##molecule_type mRNA !'##residues 1-204,211-498 ##label SAG !'##cross-references GB:D00211; NID:g217433; PIDN:BAA00150.1; !1PID:g217434 !'##note the deduced sequence is partially confirmed by amino acid !1sequencing of 15 isolated peptides REFERENCE JS0390 !$#authors Sagara, Y. !$#submission submitted to DDBJ, September 1989 !$#contents revision, insertion of residues 205-210 !$#accession JS0390 !'##molecule_type mRNA !'##residues 56-498 ##label SA2 REFERENCE S03558 !$#authors Hanukoglu, I.; Gutfinger, T. !$#journal Eur. J. Biochem. (1989) 180:479-484 !$#title cDNA sequence of adrenodoxin reductase. Identification of !1NADP-binding sites in oxidoreductases. !$#cross-references MUID:89170752; PMID:2924777 !$#accession S03558 !'##molecule_type mRNA !'##residues 155-204,211-498 ##label HAN !'##cross-references EMBL:X13736; NID:g65; PIDN:CAA32002.1; PID:g833776 !'##note 405-Ser was also found REFERENCE PS0003 !$#authors Hamamoto, I.; Kurokohchi, K.; Tanaka, S.; Ichikawa, Y. !$#journal Biochim. Biophys. Acta (1988) 953:207-213 !$#title Adrenoferredoxin-binding peptide of NADPH-adrenoferredoxin !1reductase. !$#cross-references MUID:88184054; PMID:3355838 !$#accession PS0003 !'##molecule_type protein !'##residues 33-41,'S',43-62;260-283,'TM';496-498 ##label HAM !'##note a cyanogen bromide peptide binds to adrenoferredoxin REFERENCE A29604 !$#authors Nonaka, Y.; Murakami, H.; Yabusaki, Y.; Kuramitsu, S.; !1Kagamiyama, H.; Yamano, T.; Okamoto, M. !$#journal Biochem. Biophys. Res. Commun. (1987) 145:1239-1247 !$#title Molecular cloning and sequence analysis of full-length cDNA !1for mRNA of adrenodoxin oxidoreductase from bovine adrenal !1cortex. !$#cross-references MUID:87270696; PMID:3038094 !$#accession A29604 !'##molecule_type mRNA !'##residues 1-76,'R',78-80,'VWLALTTPRSRMLL',95-123,'RVYRLT',129-204, !1211-273,'R',275-322,'RL',325-328,'ARRSAWQSPE',340-346, !1'HPGSAHWGCGGP',359-498 ##label NON !'##cross-references GB:M17029; NID:g162628; PIDN:AAA30362.1; !1PID:g162629 !'##experimental_source adrenal cortex REFERENCE S52100 !$#authors Warburton, R.J.; Seybert, D.W. !$#journal Biochim. Biophys. Acta (1995) 1246:39-46 !$#title Structural and functional characterization of bovine !1adrenodoxin reductase by limited proteolysis. !$#cross-references MUID:95110846; PMID:7811729 !$#accession S52100 !'##status preliminary !'##molecule_type protein !'##residues 'X',34-41,'X',43-48,'X',50-51;304-306,'X',308-309,'X', !1311-326 ##label WAR COMMENT Ferredoxin-NADP+ reductase is localized in the matrix of !1adrenal cortex mitochondria and functions as a component of !1the mitochondrial steroid-hydroxylating enzyme system, which !1includes ferredoxin-NADP+ reductase, adrenodoxin and two !1forms of cytochrome P-450. GENETICS !$#introns 27/1; 59/3; 91/3; 132/3; 170/3; 204/3; 246/3; 275/1; 341/3; !1399/1; 456/1 FUNCTION !$#description catalyzes the reversible reduction of NADP+ by reduced !1ferredoxin or reduced flavodoxin CLASSIFICATION #superfamily human ferredoxin-NADP+ reductase KEYWORDS alternative splicing; flavoprotein; mitochondrion; monomer; !1NADP; oxidoreductase FEATURE !$1-32 #domain transit peptide (mitochondrion) #status !8predicted #label SIG\ !$33-498 #product ferredoxin-NADP+ reductase, long form !8#status predicted #label MAT\ !$33-204,211-498 #product ferredoxin-NADP+ reductase, short form !8#status experimental #label MA2\ !$40-70 #region beta-alpha-beta FAD nucleotide-binding fold\ !$180-190 #region NADP binding #status predicted\ !$281 #binding_site substrate (Lys) #status experimental SUMMARY #length 498 #molecular-weight 55008 #checksum 7201 SEQUENCE /// ENTRY S60028 #type complete TITLE ferredoxin-NADP reductase (EC 1.18.1.2) precursor - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S60028; I49671 REFERENCE I49671 !$#authors Itoh, S.; Iemura, O.; Yamada, E.; Yoshimura, T.; Tsujikawa, !1K.; Kohama, Y.; Mimura, T. !$#journal Biochim. Biophys. Acta (1995) 1264:159-162 !$#title cDNA cloning of mouse ferredoxin reductase from kidney. !$#cross-references MUID:96085117; PMID:7495857 !$#accession S60028 !'##molecule_type mRNA !'##residues 1-494 ##label ITO !'##cross-references EMBL:D49920; NID:g1088468; PIDN:BAA08659.1; !1PID:g1088469 GENETICS !$#genome nuclear CLASSIFICATION #superfamily human ferredoxin-NADP+ reductase KEYWORDS FAD; mitochondrion; NADP; oxidoreductase FEATURE !$1-34 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$35-494 #product ferredoxin-NADP+ reductase #status predicted !8#label MAT SUMMARY #length 494 #molecular-weight 54202 #checksum 5424 SEQUENCE /// ENTRY NICLFP #type complete TITLE nitrogenase (EC 1.18.6.1) iron protein - Clostridium pasteurianum ALTERNATE_NAMES nitrogenase component II; nitrogenase reductase ORGANISM #formal_name Clostridium pasteurianum DATE 31-May-1979 #sequence_revision 29-Jul-1981 #text_change 19-Jan-2001 ACCESSIONS A00533; S02217; I40815 REFERENCE A00533 !$#authors Tanaka, M.; Haniu, M.; Yasunobu, K.T.; Mortenson, L.E. !$#journal J. Biol. Chem. (1977) 252:7093-7100 !$#title The amino acid sequence of Clostridium pasteurianum iron !1protein, a component of nitrogenase. III. The NH-2-terminal !1and COOH-terminal sequences, tryptic peptides of large !1cyanogen bromide peptides, and the complete sequence. !$#cross-references MUID:78005513; PMID:561783 !$#accession A00533 !'##molecule_type protein !'##residues 1-273 ##label TAN !'##note this is the final paper in a series characterizing the complete !1sequence REFERENCE S01723 !$#authors Wang, S.Z.; Chen, J.S.; Johnson, J.L. !$#journal Nucleic Acids Res. (1988) 16:439-454 !$#title The presence of five nifH-like sequences in Clostridium !1pasteurianum: sequence divergence and transcription !1properties. !$#cross-references MUID:88124247; PMID:2829127 !$#accession S02217 !'##molecule_type DNA !'##residues 1-273 ##label WAN !'##cross-references EMBL:X07472; NID:g40588; PIDN:CAA30359.1; !1PID:g40589 REFERENCE I40814 !$#authors Chen, K.C. !$#journal J. Bacteriol. (1986) 166:162-172 !$#title Structural features of multiple nifH-like sequences and very !1biased codon usage in nitrogenase genes of Clostridium !1pasteurianum. !$#cross-references MUID:86168010; PMID:3457003 !$#accession I40815 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-273 ##label RES !'##cross-references GB:M21537; NID:g144870; PIDN:AAA83530.1; !1PID:g144872 GENETICS !$#gene nifH COMPLEX homodimer FUNCTION !$#description the enzyme complex catalyzes the reduction of dinitrogen to !12 molecules of ammonia with the hydrolysis of 16 molecules !1of ATP to ADP and phosphate and the oxidation of ferredoxin. !$#pathway nitrogen fixation CLASSIFICATION #superfamily nitrogenase iron protein KEYWORDS 4Fe-4S; ATP; iron-sulfur protein; metalloprotein; nitrogen !1fixation; nucleotide binding; oxidoreductase; P-loop FEATURE !$8-15 #region nucleotide-binding motif A (P-loop)\ !$14 #binding_site ATP (Lys) #status predicted\ !$38,42 #active_site Asp #status predicted\ !$94,129 #binding_site 4Fe-4S cluster (Cys) (covalent) (shared !8with dimeric partner) #status predicted SUMMARY #length 273 #molecular-weight 29662 #checksum 9753 SEQUENCE /// ENTRY JQ2155 #type complete TITLE nitrogenase (EC 1.18.6.1) iron protein - Plectonema boryanum ORGANISM #formal_name Plectonema boryanum DATE 03-Feb-1994 #sequence_revision 03-Feb-1994 #text_change 19-Jan-2001 ACCESSIONS JQ2155; S36674 REFERENCE JQ2154 !$#authors Fujita, Y.; Takahashi, Y.; Shonai, F.; Ogura, Y.; Matsubara, !1H. !$#journal Plant Cell Physiol. (1991) 32:1093-1106 !$#title Cloning, nucleotide sequences and differential expression of !1the nifH and nifH-like (frxC) genes from the filamentous !1nitrogen-fixing cyanobacterium Plectonema boryanum. !$#accession JQ2155 !'##molecule_type DNA !'##residues 1-296 ##label FUJ !'##cross-references DDBJ:D00666; NID:g216823; PIDN:BAA00568.1; !1PID:g216824 !'##experimental_source strain IAM-M101 GENETICS !$#gene nifH CLASSIFICATION #superfamily nitrogenase iron protein KEYWORDS 4Fe-4S; ATP; iron-sulfur protein; metalloprotein; nitrogen !1fixation; nucleotide binding; oxidoreductase; P-loop FEATURE !$13-20 #region nucleotide-binding motif A (P-loop)\ !$19 #binding_site ATP (Lys) #status predicted\ !$43,47 #active_site Asp #status predicted\ !$101,135 #binding_site 4Fe-4S cluster (Cys) (covalent) (shared !8with dimeric partner) #status predicted SUMMARY #length 296 #molecular-weight 32333 #checksum 5026 SEQUENCE /// ENTRY NIAIF #type complete TITLE nitrogenase (EC 1.18.6.1) iron protein nifH [similarity] - Anabaena sp. ALTERNATE_NAMES nitrogenase component II; nitrogenase reductase ORGANISM #formal_name Anabaena sp. DATE 29-Jul-1981 #sequence_revision 29-Jul-1981 #text_change 19-Jan-2001 ACCESSIONS A00534; I39612 REFERENCE A00534 !$#authors Mevarech, M.; Rice, D.; Haselkorn, R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1980) 77:6476-6480 !$#title Nucleotide sequence of a cyanobacterial nifH gene coding for !1nitrogenase reductase. !$#accession A00534 !'##molecule_type DNA !'##residues 1-299 ##label MEV !'##experimental_source strain PCC 7120 REFERENCE I39612 !$#authors Ben-Porath, J.; Zehr, J.P. !$#journal Appl. Environ. Microbiol. (1994) 60:880-887 !$#title Detection and characterization of cyanobacterial nifH genes. !$#cross-references MUID:94213463; PMID:8161180 !$#accession I39612 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 48-51,'T',53-67,'K',69-76,'E',78,'I',80-87,'Q',89-119,'T', !1121-155 ##label RES !'##cross-references GB:L15553; NID:g289136; PIDN:AAA19027.1; !1PID:g289137 GENETICS !$#gene nifH COMPLEX homodimer CLASSIFICATION #superfamily nitrogenase iron protein KEYWORDS 4Fe-4S; ATP; homodimer; iron-sulfur protein; metalloprotein; !1nitrogen fixation; nucleotide binding; oxidoreductase; !1P-loop FEATURE !$13-20 #region nucleotide-binding motif A (P-loop)\ !$19 #binding_site ATP (Lys) #status predicted\ !$43,47 #active_site Asp #status predicted\ !$101,135 #binding_site 4Fe-4S cluster (Cys) (covalent) (shared !8with dimeric partner) #status predicted SUMMARY #length 299 #molecular-weight 32814 #checksum 7877 SEQUENCE /// ENTRY NIKBFP #type complete TITLE nitrogenase (EC 1.18.6.1) iron protein - Klebsiella pneumoniae ALTERNATE_NAMES nitrogenase component II; nitrogenase reductase ORGANISM #formal_name Klebsiella pneumoniae DATE 29-Jul-1981 #sequence_revision 09-Aug-1997 #text_change 19-Jan-2001 ACCESSIONS A92834; A92314; A93849; S39152; A00535 REFERENCE A92834 !$#authors Scott, K.F.; Rolfe, B.G.; Shine, J. !$#journal J. Mol. Appl. Genet. (1981) 1:71-81 !$#title Biological nitrogen fixation: primary structure of the !1Klebsiella pneumoniae nifH and nifD genes. !$#cross-references MUID:82267647; PMID:6809876 !$#accession A92834 !'##molecule_type DNA !'##residues 2-293 ##label SCO !'##cross-references GB:V00631; GB:J01741; NID:g43874; PIDN:CAA23903.1; !1PID:g43875 !'##experimental_source strain UNF841 REFERENCE A92314 !$#authors Sundaresan, V.; Ausubel, F.M. !$#journal J. Biol. Chem. (1981) 256:2808-2812 !$#title Nucleotide sequence of the gene coding for the nitrogenase !1iron protein from Klebsiella pneumoniae. !$#cross-references MUID:81142258; PMID:6259144 !$#contents plasmid pSB1 !$#accession A92314 !'##molecule_type DNA !'##residues 2-293 ##label SUN REFERENCE A93849 !$#authors Hausinger, R.P.; Howard, J.B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1980) 77:3826-3830 !$#title Comparison of the iron proteins from the nitrogen fixation !1complexes of Azotobacter vinelandii, Clostridium !1pasteurianum, and Klebsiella pneumoniae. !$#cross-references MUID:81054664; PMID:7001444 !$#accession A93849 !'##molecule_type protein !'##residues 2-26 ##label HAU REFERENCE S35903 !$#authors Charlton, W.; Cannon, W.; Buck, M. !$#journal Mol. Microbiol. (1993) 7:1007-1021 !$#title The Klebsiella pneumoniae nifJ promoter: analysis of !1promoter elements regulating activation by the NifA !1promoter. !$#cross-references MUID:93247479; PMID:8483412 !$#accession S39152 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-17,'Y' ##label CHA !'##cross-references EMBL:X13109 !'##note the authors translated the codon ACC for residue 2 as Ile GENETICS !$#gene nifH FUNCTION !$#description the enzyme complex catalyzes the reduction of dinitrogen to !12 molecules of ammonia with the hydrolysis of 16 molecules !1of ATP to ADP and phosphate and the oxidation of ferredoxin. !$#pathway nitrogen fixation CLASSIFICATION #superfamily nitrogenase iron protein KEYWORDS 4Fe-4S; ATP; iron-sulfur protein; metalloprotein; nitrogen !1fixation; nucleotide binding; oxidoreductase; P-loop FEATURE !$10-17 #region nucleotide-binding motif A (P-loop)\ !$16 #binding_site ATP (Lys) #status predicted\ !$40,44 #active_site Asp #status predicted\ !$98,133 #binding_site 4Fe-4S cluster (Cys) (covalent) (shared !8with dimeric partner) #status predicted SUMMARY #length 293 #molecular-weight 31902 #checksum 3973 SEQUENCE /// ENTRY NIAVF #type complete TITLE nitrogenase (EC 1.18.6.1) 1 iron protein [validated] - Azotobacter vinelandii ALTERNATE_NAMES nitrogenase component II; nitrogenase reductase ORGANISM #formal_name Azotobacter vinelandii DATE 15-Oct-1982 #sequence_revision 28-Dec-1987 #text_change 19-Jan-2001 ACCESSIONS A94666; S02323; A92364; A42427; A00536; A23969 REFERENCE A94666 !$#authors Brigle, K.E.; Newton, W.E.; Dean, D.R. !$#journal Gene (1985) 37:37-44 !$#title Complete nucleotide sequence of the Azotobacter vinelandii !1nitrogenase structural gene cluster. !$#cross-references MUID:86031364; PMID:3863780 !$#accession A94666 !'##molecule_type DNA !'##residues 1-290 ##label BRI !'##cross-references GB:M11579; NID:g142329; PIDN:AAA22142.1; !1PID:g142330 REFERENCE S02323 !$#authors Hiratsuka, K.; Roy, K.L. !$#journal Nucleic Acids Res. (1988) 16:1207 !$#title Sequence of a 1.4 kb Eco RI fragment of Azotobacter !1vinelandii nif DNA. !$#cross-references MUID:88144000; PMID:3344210 !$#accession S02323 !'##molecule_type DNA !'##residues 271-290 ##label HIR !'##cross-references EMBL:X06886; NID:g39263; PIDN:CAA30003.1; !1PID:g39264 REFERENCE A92364 !$#authors Hausinger, R.P.; Howard, J.B. !$#journal J. Biol. Chem. (1982) 257:2483-2490 !$#title The amino acid sequence of the nitrogenase iron protein from !1Azotobacter vinelandii. !$#cross-references MUID:82142349; PMID:6801032 !$#accession A92364 !'##molecule_type protein !'##residues 1-290 ##label HAU REFERENCE A42427 !$#authors Seefeldt, L.C.; Morgan, T.V.; Dean, D.R.; Mortenson, L.E. !$#journal J. Biol. Chem. (1992) 267:6680-6688 !$#title Mapping the site(s) of MgATP and MgADP interaction with the !1nitrogenase of Azotobacter vinelandii. Lysine 15 of the iron !1protein plays a major role in MgATP interaction. !$#cross-references MUID:92202214; PMID:1313018 !$#accession A42427 !'##molecule_type protein !'##residues 2-21 ##label SEE !'##note sequence extracted from NCBI backbone (NCBIP:89942) !'##note amino-terminal sequences of both wild-type and mutant forms !1were determined !'##note by site-directed mutagenesis Lys-16 probably interacts with the !1gamma-phosphate of ATP REFERENCE A51313 !$#authors Komiya, H.; Georgiadis, M.M.; Chakrabarti, P.; Woo, D.; !1Kornuc, J.J.; Rees, D.C. !$#submission submitted to the Brookhaven Protein Data Bank, September !11992 !$#cross-references PDB:1NIP !$#contents annotation; X-ray crystallography, 2.9 angstroms, residues !12-284 REFERENCE A43282 !$#authors Georgiadis, M.M.; Komiya, H.; Chakrabarti, P.; Woo, D.; !1Kornuc, J.J.; Rees, D.C. !$#journal Science (1992) 257:1653-1659 !$#title Crystallographic structure of the nitrogenase iron protein !1from Azotobacter vinelandii. !$#cross-references MUID:92410322; PMID:1529353 !$#contents annotation; X-ray crystallography, 2.9 angstroms GENETICS !$#gene nifH COMPLEX homodimer FUNCTION !$#description the enzyme complex catalyzes the reduction of dinitrogen to !12 molecules of ammonia with the hydrolysis of 16 molecules !1of ATP to ADP and phosphate and the oxidation of ferredoxin. !$#pathway nitrogen fixation CLASSIFICATION #superfamily nitrogenase iron protein KEYWORDS 4Fe-4S; ATP; homodimer; iron-sulfur protein; metalloprotein; !1nitrogen fixation; nucleotide binding; oxidoreductase; !1P-loop; phosphoprotein FEATURE !$2-290 #product nitrogenase iron protein #status !8experimental #label MAT\ !$10-17 #region nucleotide-binding motif A (P-loop)\ !$16 #binding_site ATP (Lys) #status experimental\ !$40,44 #active_site Asp #status predicted\ !$98,133 #binding_site 4Fe-4S cluster (Cys) (covalent) (shared !8with dimeric partner) #status experimental\ !$101 #modified_site ADP-ribosylarginine (Arg) (by !8NAD+-nitrogenase ADP-D-ribosyltransferase) #status !8predicted SUMMARY #length 290 #molecular-weight 31516 #checksum 3821 SEQUENCE /// ENTRY JN0516 #type complete TITLE nitrogenase (EC 1.18.6.1) 1 iron protein - Azotobacter chroococcum ALTERNATE_NAMES nitrogenase component II; nitrogenase reductase ORGANISM #formal_name Azotobacter chroococcum DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 19-Jan-2001 ACCESSIONS JN0516 REFERENCE JN0516 !$#authors Jones, R.; Woodley, P.; Birkmann-Zinoni, A.; Robson, R.L. !$#journal Gene (1993) 123:145-146 !$#title The nifH gene encoding the Fe protein Component of the !1molybdenum nitrogenase from Azotobacter chroococcum. !$#cross-references MUID:93138425; PMID:8423000 !$#accession JN0516 !'##molecule_type DNA !'##residues 1-291 ##label JON !'##cross-references GB:M73020 GENETICS !$#gene nifH COMPLEX homodimer FUNCTION !$#description the enzyme complex catalyzes the reduction of dinitrogen to !12 molecules of ammonia with the hydrolysis of 16 molecules !1of ATP to ADP and phosphate and the oxidation of ferredoxin. !$#pathway nitrogen fixation CLASSIFICATION #superfamily nitrogenase iron protein KEYWORDS 4Fe-4S; ATP; homodimer; iron-sulfur protein; metalloprotein; !1nitrogen fixation; nucleotide binding; oxidoreductase; !1P-loop FEATURE !$10-17 #region nucleotide-binding motif A (P-loop)\ !$16 #binding_site ATP (Lys) #status predicted\ !$40,44 #active_site Asp #status predicted\ !$98,133 #binding_site 4Fe-4S cluster (Cys) (covalent) (shared !8with dimeric partner) #status predicted SUMMARY #length 291 #molecular-weight 31521 #checksum 3806 SEQUENCE /// ENTRY JW0039 #type complete TITLE nitrogenase (EC 1.18.6.1) iron protein - Rhodospirillum rubrum ALTERNATE_NAMES dinitrogenase reductase ORGANISM #formal_name Rhodospirillum rubrum DATE 21-Nov-1993 #sequence_revision 26-May-1995 #text_change 19-Jan-2001 ACCESSIONS JW0039; A61610 REFERENCE JW0039 !$#authors Lehman, L.J.; Fitzmaurice, W.P.; Roberts, G.P. !$#journal Gene (1990) 95:143-147 !$#title The cloning and functional characterization of the nifH gene !1of Rhodospirillum rubrum. !$#cross-references MUID:91071597; PMID:1979299 !$#accession JW0039 !'##molecule_type DNA !'##residues 1-295 ##label LEH !'##cross-references GB:M33774; NID:g152609; PIDN:AAA26463.1; !1PID:g152610 REFERENCE A61610 !$#authors Pope, M.R.; Murrell, S.A.; Ludden, P.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:3173-3177 !$#title Covalent modification of the iron protein of nitrogenase !1from Rhodospirillum rubrum by adenosine !1diphosphoribosylation of a specific arginine residue. !$#cross-references MUID:85216464; PMID:3923473 !$#accession A61610 !'##molecule_type protein !'##residues 101-106 ##label POP COMMENT This protein is regulated by reversible ADP-ribosylation on !1a specific Arg residue and is inactive when ADP-ribosylated. GENETICS !$#gene nifH CLASSIFICATION #superfamily nitrogenase iron protein KEYWORDS 4Fe-4S; ATP; homodimer; iron-sulfur protein; metalloprotein; !1nitrogen fixation; nucleotide binding; oxidoreductase; !1P-loop; phosphoprotein FEATURE !$11-18 #region nucleotide-binding motif A (P-loop)\ !$17 #binding_site ATP (Lys) #status predicted\ !$41,45 #active_site Asp #status predicted\ !$99,133 #binding_site 4Fe-4S cluster (Cys) (covalent) (shared !8with dimeric partner) #status predicted\ !$102 #modified_site ADP-ribosylarginine (Arg) (by !8NAD+-nitrogenase ADP-D-ribosyltransferase) #status !8experimental SUMMARY #length 295 #molecular-weight 31642 #checksum 4142 SEQUENCE /// ENTRY NIZRFM #type complete TITLE nitrogenase (EC 1.18.6.1) iron protein - Rhizobium meliloti ALTERNATE_NAMES nitrogenase component II; nitrogenase reductase ORGANISM #formal_name Rhizobium meliloti DATE 02-Apr-1982 #sequence_revision 02-Apr-1982 #text_change 19-Jan-2001 ACCESSIONS A00537 REFERENCE A00537 !$#authors Torok, I.; Kondorosi, A. !$#journal Nucleic Acids Res. (1981) 9:5711-5723 !$#title Nucleotide sequence of the R. meliloti nitrogenase reductase !1(nifH) gene. !$#cross-references MUID:82081854; PMID:6273806 !$#accession A00537 !'##molecule_type DNA !'##residues 1-297 ##label TOR COMMENT Rhizobium meliloti was isolated from sweet clover (Melilotus !1sp.). GENETICS !$#gene nifH CLASSIFICATION #superfamily nitrogenase iron protein KEYWORDS 4Fe-4S; ATP; iron-sulfur protein; metalloprotein; nitrogen !1fixation; nucleotide binding; oxidoreductase; P-loop FEATURE !$11-18 #region nucleotide-binding motif A (P-loop)\ !$17 #binding_site ATP (Lys) #status predicted\ !$41,45 #active_site Asp #status predicted\ !$99,133 #binding_site 4Fe-4S cluster (Cys) (covalent) (shared !8with dimeric partner) #status predicted SUMMARY #length 297 #molecular-weight 32023 #checksum 5316 SEQUENCE /// ENTRY NIZRFT #type complete TITLE nitrogenase (EC 1.18.6.1) iron protein - Rhizobium leguminosarum bv. trifolii ALTERNATE_NAMES nitrogenase component II; nitrogenase reductase ORGANISM #formal_name Rhizobium leguminosarum bv. trifolii DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 19-Jan-2001 ACCESSIONS A00538 REFERENCE A90942 !$#authors Scott, K.F.; Rolfe, B.G.; Shine, J. !$#journal DNA (1983) 2:149-155 !$#title Biological nitrogen fixation: primary structure of the !1Rhizobium trifolii iron protein gene. !$#cross-references MUID:83261209; PMID:6307623 !$#accession A00538 !'##molecule_type DNA !'##residues 1-297 ##label SCO !'##experimental_source strain SU329 GENETICS !$#gene nifH CLASSIFICATION #superfamily nitrogenase iron protein KEYWORDS 4Fe-4S; ATP; iron-sulfur protein; metalloprotein; nitrogen !1fixation; nucleotide binding; oxidoreductase; P-loop FEATURE !$11-18 #region nucleotide-binding motif A (P-loop)\ !$17 #binding_site ATP (Lys) #status predicted\ !$41,45 #active_site Asp #status predicted\ !$99,133 #binding_site 4Fe-4S cluster (Cys) (covalent) (shared !8with dimeric partner) #status predicted SUMMARY #length 297 #molecular-weight 31902 #checksum 7013 SEQUENCE /// ENTRY NIZRF #type complete TITLE nitrogenase (EC 1.18.6.1) iron protein - Rhizobium leguminosarum bv. phaseoli ALTERNATE_NAMES nitrogenase component II; nitrogenase reductase ORGANISM #formal_name Rhizobium leguminosarum bv. phaseoli DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 19-Jan-2001 ACCESSIONS A00539 REFERENCE A00539 !$#authors Quinto, C.; de la Vega, H.; Flores, M.; Leemans, J.; !1Cevallos, M.A.; Pardo, M.A.; Azpiroz, R.; de Lourdes Girard, !1M.; Calva, E.; Palacios, R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:1170-1174 !$#title Nitrogenase reductase: a functional multigene family in !1Rhizobium phaseoli. !$#accession A00539 !'##molecule_type DNA !'##residues 1-297 ##label QUI !'##experimental_source strain CFN-42 GENETICS !$#gene nifH CLASSIFICATION #superfamily nitrogenase iron protein KEYWORDS 4Fe-4S; ATP; iron-sulfur protein; metalloprotein; nitrogen !1fixation; nucleotide binding; oxidoreductase; P-loop FEATURE !$11-18 #region nucleotide-binding motif A (P-loop)\ !$17 #binding_site ATP (Lys) #status predicted\ !$41,45 #active_site Asp #status predicted\ !$99,133 #binding_site 4Fe-4S cluster (Cys) (covalent) (shared !8with dimeric partner) #status predicted SUMMARY #length 297 #molecular-weight 31966 #checksum 4987 SEQUENCE /// ENTRY JS0238 #type complete TITLE nitrogenase (EC 1.18.6.1) iron protein [similarity] - Rhizobium sp. plasmid pNGR234a ORGANISM #formal_name Rhizobium sp. DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 19-Jan-2001 ACCESSIONS JS0238; T10828 REFERENCE A91604 !$#authors Badenoch-Jones, J.; Holton, T.A.; Morrison, C.M.; Scott, !1K.F.; Shine, J. !$#journal Gene (1989) 77:141-153 !$#title Structural and functional analysis of nitrogenase genes from !1the broad-host-range Rhizobium strain ANU240. !$#cross-references MUID:89306671; PMID:2744485 !$#accession JS0238 !'##molecule_type DNA !'##residues 1-296 ##label BAD !'##cross-references GB:M26961; NID:g152327; PIDN:AAA26329.1; !1PID:g152331 !'##experimental_source strain ANU240 REFERENCE Z14734 !$#authors Freiberg, C.; Fellay, R.; Bairoch, A.; Broughton, W.J.; !1Rosenthal, A.; Perret, X. !$#journal Nature (1997) 387:394-401 !$#title Molecular basis of symbiosis between Rhizobium and legumes. !$#cross-references MUID:97305956; PMID:9163424 !$#accession T10828 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-261,'T',263-296 ##label FRE !'##cross-references EMBL:AE000105; EMBL:U00090; NID:g2182706; !1PIDN:AAB91923.1; PID:g2182707 !'##experimental_source strain NGR234 COMMENT This protein is one of the three structural components of !1nitrogenase. GENETICS !$#gene nifH !$#genome plasmid pNGR234a CLASSIFICATION #superfamily nitrogenase iron protein KEYWORDS 4Fe-4S; ATP; iron-sulfur protein; metalloprotein; nitrogen !1fixation; nucleotide binding; oxidoreductase; P-loop FEATURE !$11-18 #region nucleotide-binding motif A (P-loop)\ !$17 #binding_site ATP (Lys) #status predicted\ !$41,45 #active_site Asp #status predicted\ !$99,133 #binding_site 4Fe-4S cluster (Cys) (covalent) (shared !8with dimeric partner) #status predicted SUMMARY #length 296 #molecular-weight 31760 #checksum 4668 SEQUENCE /// ENTRY NIZRFX #type complete TITLE nitrogenase (EC 1.18.6.1) iron protein - Rhizobium sp. ALTERNATE_NAMES nitrogenase component II; nitrogenase reductase ORGANISM #formal_name Rhizobium sp. DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 19-Jan-2001 ACCESSIONS A00540 REFERENCE A00540 !$#authors Scott, K.F.; Rolfe, B.G.; Shine, J. !$#journal DNA (1983) 2:141-148 !$#title Nitrogenase structural genes are unlinked in the nonlegume !1symbiont Parasponia rhizobium. !$#cross-references MUID:83261208; PMID:6307622 !$#accession A00540 !'##molecule_type DNA !'##residues 1-294 ##label SCO !'##cross-references GB:K00487; NID:g169749; PIDN:AAA33884.1; !1PID:g169750 !'##experimental_source strain ANU289 GENETICS !$#gene nifH CLASSIFICATION #superfamily nitrogenase iron protein KEYWORDS 4Fe-4S; ATP; iron-sulfur protein; metalloprotein; nitrogen !1fixation; nucleotide binding; oxidoreductase; P-loop FEATURE !$11-18 #region nucleotide-binding motif A (P-loop)\ !$17 #binding_site ATP (Lys) #status predicted\ !$41,45 #active_site Asp #status predicted\ !$99,133 #binding_site 4Fe-4S cluster (Cys) (covalent) (shared !8with dimeric partner) #status predicted SUMMARY #length 294 #molecular-weight 31637 #checksum 6240 SEQUENCE /// ENTRY NIZJFE #type complete TITLE nitrogenase (EC 1.18.6.1) iron protein - Bradyrhizobium japonicum ALTERNATE_NAMES dinitrogenase reductase; nitrogenase component II ORGANISM #formal_name Bradyrhizobium japonicum DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 19-Jan-2001 ACCESSIONS S14044; S07446 REFERENCE S14044 !$#authors Fuhrmann, M.; Hennecke, H. !$#journal J. Bacteriol. (1984) 158:1005-1011 !$#title Rhizobium japonicum nitrogenase Fe protein gene (nifH). !$#cross-references MUID:84212258; PMID:6327620 !$#accession S14044 !'##molecule_type DNA !'##residues 1-294 ##label FUH !'##cross-references EMBL:K01620; NID:g152315; PIDN:AAA26322.1; !1PID:g152316 !'##note the source is designated as Rhizobium japonicum REFERENCE S07446 !$#authors Adams, T.H.; Chelm, B.K. !$#journal J. Mol. Appl. Genet. (1984) 2:392-405 !$#title The nifH and nifDK promoter regions from Rhizobium japonicum !1share structural homologies with each other and with !1nitrogen-regulated promoters from other organisms. !$#cross-references MUID:84241516; PMID:6588133 !$#accession S07446 !'##molecule_type DNA !'##residues 1-82,'R',84-94 ##label ADA !'##cross-references EMBL:K01620 !'##note the authors translated the codon ACT for residue 20 as Ser !'##note the source is designated as Rhizobium japonicum GENETICS !$#gene nifH CLASSIFICATION #superfamily nitrogenase iron protein KEYWORDS 4Fe-4S; ATP; homodimer; iron-sulfur protein; metalloprotein; !1nitrogen fixation; nucleotide binding; oxidoreductase; !1P-loop FEATURE !$11-18 #region nucleotide-binding motif A (P-loop)\ !$17 #binding_site ATP (Lys) #status predicted\ !$41,45 #active_site Asp #status predicted\ !$99,133 #binding_site 4Fe-4S cluster (Cys) (covalent) (shared !8with dimeric partner) #status predicted SUMMARY #length 294 #molecular-weight 31561 #checksum 4249 SEQUENCE /// ENTRY NIMXVO #type complete TITLE nitrogenase (EC 1.18.6.1) iron protein - Methanococcus voltae ALTERNATE_NAMES nitrogenase component II; nitrogenase reductase ORGANISM #formal_name Methanococcus voltae DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 19-Jan-2001 ACCESSIONS S07313 REFERENCE S07313 !$#authors Souillard, N.; Sibold, L. !$#journal Mol. Gen. Genet. (1986) 203:21-28 !$#title Primary structure and expression of a gene homologous to !1nifH (nitrogenase Fe protein) from the archaebacterium !1Methanococcus voltae. !$#accession S07313 !'##molecule_type DNA !'##residues 1-278 ##label SOU !'##cross-references EMBL:X03777; NID:g44732; PIDN:CAA27407.1; !1PID:g44733 !'##note the authors translated the codon CAA for residue 114 as Gln CLASSIFICATION #superfamily nitrogenase iron protein KEYWORDS 4Fe-4S; ATP; iron-sulfur protein; metalloprotein; nitrogen !1fixation; nucleotide binding; oxidoreductase; P-loop FEATURE !$8-15 #region nucleotide-binding motif A (P-loop)\ !$14 #binding_site ATP (Lys) #status predicted\ !$38,42 #active_site Asp #status predicted\ !$94,130 #binding_site 4Fe-4S cluster (Cys) (covalent) (shared !8with dimeric partner) #status predicted SUMMARY #length 278 #molecular-weight 30396 #checksum 489 SEQUENCE /// ENTRY NILVC #type complete TITLE frxC protein - liverwort (Marchantia polymorpha) chloroplast ALTERNATE_NAMES nitrogenase (EC 1.18.6.1) iron protein homolog ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 19-Jan-2001 ACCESSIONS A00541; S01517 REFERENCE A00150 !$#authors Ohyama, K. !$#submission submitted to the EMBL Data Library, October 1986 !$#accession A00541 !'##molecule_type DNA !'##residues 1-289 ##label OHY REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features REFERENCE S01512 !$#authors Kohchi, T.; Shirai, H.; Fukuzawa, H.; Sano, T.; Komano, T.; !1Umesono, K.; Inokuchi, H.; Ozeki, H.; Ohyama, K. !$#journal J. Mol. Biol. (1988) 203:353-372 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. IV. Inverted repeat and small single !1copy regions. !$#cross-references MUID:89068688; PMID:3199437 !$#accession S01517 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-289 ##label KOH !'##cross-references GB:X04465; GB:Y00686; NID:g11640; PIDN:CAA28144.1; !1PID:g11733 GENETICS !$#gene frxC !$#genome chloroplast CLASSIFICATION #superfamily nitrogenase iron protein KEYWORDS 4Fe-4S; ATP; chloroplast; iron-sulfur protein; !1metalloprotein; nucleotide binding; oxidoreductase; P-loop FEATURE !$7-14 #region nucleotide-binding motif A (P-loop)\ !$13 #binding_site ATP (Lys) #status predicted\ !$37,41 #active_site Asp #status predicted\ !$95,129 #binding_site 4Fe-4S cluster (Cys) (covalent) (shared !8with dimeric partner) #status predicted SUMMARY #length 289 #molecular-weight 31945 #checksum 7317 SEQUENCE /// ENTRY JQ2154 #type complete TITLE frxC protein - Plectonema boryanum ALTERNATE_NAMES nitrogenase (EC 1.18.6.1) iron protein homolog ORGANISM #formal_name Plectonema boryanum DATE 03-Feb-1994 #sequence_revision 03-Feb-1994 #text_change 19-Jan-2001 ACCESSIONS JQ2154; S36671 REFERENCE JQ2154 !$#authors Fujita, Y.; Takahashi, Y.; Shonai, F.; Ogura, Y.; Matsubara, !1H. !$#journal Plant Cell Physiol. (1991) 32:1093-1106 !$#title Cloning, nucleotide sequences and differential expression of !1the nifH and nifH-like (frxC) genes from the filamentous !1nitrogen-fixing cyanobacterium Plectonema boryanum. !$#accession JQ2154 !'##molecule_type DNA !'##residues 1-286 ##label FUJ !'##cross-references DDBJ:D00665; NID:g216814; PIDN:BAA00565.1; !1PID:g441179 !'##experimental_source strain IAM-M101 GENETICS !$#gene frxC !$#start_codon GTG CLASSIFICATION #superfamily nitrogenase iron protein KEYWORDS 4Fe-4S; ATP; iron-sulfur protein; metalloprotein; nucleotide !1binding; oxidoreductase; P-loop FEATURE !$7-14 #region nucleotide-binding motif A (P-loop)\ !$13 #binding_site ATP (Lys) #status predicted\ !$37,41 #active_site Asp #status predicted\ !$95,129 #binding_site 4Fe-4S cluster (Cys) (covalent) (shared !8with dimeric partner) #status predicted SUMMARY #length 286 #molecular-weight 31219 #checksum 2121 SEQUENCE /// ENTRY A23874 #type complete TITLE nitrogenase (EC 1.18.6.1) molybdenum-iron protein alpha chain - Rhizobium sp. ALTERNATE_NAMES dinitrogenase alpha chain; nitrogenase component I alpha chain ORGANISM #formal_name Rhizobium sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS A23874 REFERENCE A93542 !$#authors Weinman, J.J.; Fellows, F.F.; Gresshoff, P.M.; Shine, J.; !1Scott, K.F. !$#journal Nucleic Acids Res. (1984) 12:8329-8344 !$#title Structural analysis of the genes encoding the !1molybdenum-iron protein of nitrogenase in the Parasponia !1rhizobium strain ANU289. !$#cross-references MUID:85062817; PMID:6095197 !$#accession A23874 !'##molecule_type DNA !'##residues 1-500 ##label WEI !'##experimental_source strain ANU289 GENETICS !$#gene nifD CLASSIFICATION #superfamily dinitrogenase alpha chain; nitrogenase !1vanadium-iron protein alpha chain homology KEYWORDS ATP; iron-sulfur protein; metalloprotein; molybdenum; !1nitrogen fixation; oxidoreductase FEATURE !$19-491 #domain nitrogenase vanadium-iron protein alpha chain !8homology #label VIA\ !$283 #binding_site homocitryl Mo-7Fe-8S cluster (Cys) !8(covalent) #status predicted\ !$451 #binding_site homocitryl Mo-7Fe-8S cluster molybdenum !8(His) (ligand) #status predicted SUMMARY #length 500 #molecular-weight 56142 #checksum 8693 SEQUENCE /// ENTRY NIAIMA #type complete TITLE nitrogenase (EC 1.18.6.1) molybdenum-iron protein alpha chain - Anabaena sp. ALTERNATE_NAMES dinitrogenase alpha chain; nitrogenase, component I alpha chain ORGANISM #formal_name Anabaena sp. DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 19-Jan-2001 ACCESSIONS A00542; S28191; I39611 REFERENCE A00542 !$#authors Lammers, P.J.; Haselkorn, R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:4723-4727 !$#title Sequence of the nifD gene coding for the alpha subunit of !1dinitrogenase from the cyanobacterium Anabaena. !$#accession A00542 !'##molecule_type DNA !'##residues 1-480 ##label LAM !'##cross-references GB:J01537; NID:g38639 !'##experimental_source PCC 7120 !'##note this ORF is not annotated in GenBank entry A7NIFX, release !1103.0 REFERENCE S28189 !$#authors Murphy, S.T.; Jackman, D.M.; Mulligan, M.E. !$#journal Biochim. Biophys. Acta (1993) 1171:337-340 !$#title Cloning and nucleotide sequence of the gene for !1dinitrogenase reductase (nifH) from the heterocyst-forming !1cyanobacterium Anabaena sp. L31. !$#cross-references MUID:93144353; PMID:8424961 !$#accession S28191 !'##molecule_type DNA !'##residues 1-10,'Q',12-23 ##label MUR !'##cross-references GB:L04499; NID:g142055; PIDN:AAA22015.1; !1PID:g142058 !'##experimental_source strain L31 COMMENT The key enzymatic reactions in nitrogen fixation are !1catalyzed by the nitrogenase complex, which has two !1components: the molybdenum-iron protein (also called !1component I or dinitrogenase) and the iron protein (also !1called component II or nitrogenase reductase). GENETICS !$#gene nifD COMPLEX heterotetramer of two alpha and two beta chains FUNCTION !$#description the enzyme complex catalyzes the reduction of dinitrogen to !12 molecules of ammonia with the hydrolysis of 16 molecules !1of ATP to ADP and phosphate and the oxidation of ferredoxin !$#pathway nitrogen fixation CLASSIFICATION #superfamily dinitrogenase alpha chain; nitrogenase !1vanadium-iron protein alpha chain homology KEYWORDS 4Fe-4S; ATP; heterotetramer; iron-sulfur protein; !1metalloprotein; molybdenum; nitrogen fixation; !1oxidoreductase FEATURE !$16-477 #domain nitrogenase vanadium-iron protein alpha chain !8homology #label VIA\ !$64,90,156 #binding_site 4Fe-4S cluster 1 (Cys) (covalent) !8#status predicted\ !$90 #binding_site 4Fe-4S cluster 2 (Cys) (covalent) !8#status predicted\ !$282 #binding_site homocitryl Mo-7Fe-8S cluster (Cys) !8(covalent) #status predicted\ !$449 #binding_site homocitryl Mo-7Fe-8S cluster molybdenum !8(His) (ligand) #status predicted SUMMARY #length 480 #molecular-weight 54262 #checksum 12 SEQUENCE /// ENTRY B29042 #type complete TITLE nitrogenase (EC 1.18.6.1) molybdenum-iron protein alpha chain - Rhodobacter capsulatus ALTERNATE_NAMES dinitrogenase alpha chain; nitrogenase component I alpha chain ORGANISM #formal_name Rhodobacter capsulatus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS B29042 REFERENCE A91562 !$#authors Schumann, J.P.; Waitches, G.M.; Scolnik, P.A. !$#journal Gene (1986) 48:81-92 !$#title A DNA fragment hybridizing to a nif probe in Rhodobacter !1capsulatus is homologous to a 16S rRNA gene. !$#cross-references MUID:87163519; PMID:3557130 !$#accession B29042 !'##molecule_type DNA !'##residues 1-499 ##label SCH !'##cross-references GB:M15270; NID:g151971; PIDN:AAA26141.1; !1PID:g151973 GENETICS !$#gene nifD CLASSIFICATION #superfamily dinitrogenase alpha chain; nitrogenase !1vanadium-iron protein alpha chain homology KEYWORDS ATP; iron-sulfur protein; metalloprotein; molybdenum; !1nitrogen fixation; oxidoreductase FEATURE !$19-496 #domain nitrogenase vanadium-iron protein alpha chain !8homology #label VIA\ !$290 #binding_site homocitryl Mo-7Fe-8S cluster (Cys) !8(covalent) #status predicted\ !$454 #binding_site homocitryl Mo-7Fe-8S cluster molybdenum !8(His) (ligand) #status predicted SUMMARY #length 499 #molecular-weight 56104 #checksum 3014 SEQUENCE /// ENTRY S26191 #type complete TITLE nitrogenase (EC 1.18.6.1) molybdenum-iron protein alpha chain - Frankia sp. ALTERNATE_NAMES dinitrogenase reductase ORGANISM #formal_name Frankia sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S26191 REFERENCE S26190 !$#authors Normand, P. !$#submission submitted to the EMBL Data Library, November 1990 !$#accession S26191 !'##molecule_type DNA !'##residues 1-473 ##label NOR !'##cross-references EMBL:X57006; NID:g296359; PIDN:CAA40327.1; !1PID:g43427 GENETICS !$#gene nifD CLASSIFICATION #superfamily dinitrogenase alpha chain; nitrogenase !1vanadium-iron protein alpha chain homology KEYWORDS ATP; iron-sulfur protein; metalloprotein; molybdenum; !1nitrogen fixation; oxidoreductase FEATURE !$15-469 #domain nitrogenase vanadium-iron protein alpha chain !8homology #label VIA\ !$274 #binding_site homocitryl Mo-7Fe-8S cluster (Cys) !8(covalent) #status predicted SUMMARY #length 473 #molecular-weight 52093 #checksum 8195 SEQUENCE /// ENTRY JQ2156 #type complete TITLE nitrogenase (EC 1.18.6.1) molybdenum-iron protein alpha chain - Plectonema boryanum ALTERNATE_NAMES dinitrogenase alpha chain; nifD protein; nitrogenase component I alpha chain ORGANISM #formal_name Plectonema boryanum DATE 03-Feb-1994 #sequence_revision 03-Feb-1994 #text_change 19-Jan-2001 ACCESSIONS JQ2156; S36675 REFERENCE JQ2154 !$#authors Fujita, Y.; Takahashi, Y.; Shonai, F.; Ogura, Y.; Matsubara, !1H. !$#journal Plant Cell Physiol. (1991) 32:1093-1106 !$#title Cloning, nucleotide sequences and differential expression of !1the nifH and nifH-like (frxC) genes from the filamentous !1nitrogen-fixing cyanobacterium Plectonema boryanum. !$#accession JQ2156 !'##molecule_type DNA !'##residues 1-494 ##label FUJ !'##cross-references DDBJ:D00666; NID:g216823; PIDN:BAA00569.1; !1PID:g216825 !'##experimental_source strain IAM-M101 GENETICS !$#gene nifD CLASSIFICATION #superfamily dinitrogenase alpha chain; nitrogenase !1vanadium-iron protein alpha chain homology KEYWORDS 4Fe-4S; ATP; iron; iron-sulfur protein; metalloprotein; !1molybdenum; nitrogen fixation; oxidoreductase FEATURE !$22-480 #domain nitrogenase vanadium-iron protein alpha chain !8homology #label VIA\ !$70,96,162 #binding_site 4Fe-4S cluster 1 (Cys) (covalent) !8#status predicted\ !$96 #binding_site 4Fe-4S cluster 2 (Cys) (covalent) !8#status predicted\ !$288 #binding_site homocitryl Mo-7Fe-8S cluster (Cys) !8(covalent) #status predicted\ !$455 #binding_site homocitryl Mo-7Fe-8S cluster molybdenum !8(His) (ligand) #status predicted SUMMARY #length 494 #molecular-weight 55423 #checksum 7347 SEQUENCE /// ENTRY NIBCAT #type complete TITLE nitrogenase (EC 1.18.6.1) molybdenum-iron protein alpha chain - Thiobacillus ferrooxidans ALTERNATE_NAMES dinitrogenase alpha chain; nitrogenase, component I alpha chain ORGANISM #formal_name Thiobacillus ferrooxidans DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 19-Jan-2001 ACCESSIONS A91597; A91841; B26931; JT0340 REFERENCE A91597 !$#authors Rawlings, D.E. !$#journal Gene (1988) 69:337-343 !$#title Sequence and structural analysis of the alpha- and !1beta-dinitrogenase subunits of Thiobacillus ferrooxidans. !$#cross-references MUID:89172078; PMID:3234769 !$#accession A91597 !'##molecule_type DNA !'##residues 1-489 ##label RAW !'##cross-references GB:M15238; GB:M22482; NID:g154637; PIDN:AAA27375.1; !1PID:g154639 !'##experimental_source ATCC 33020 REFERENCE A91841 !$#authors Pretorius, I.M.; Rawlings, D.E.; O'Neill, E.G.; Jones, W.A.; !1Kirby, R.; Woods, D.R. !$#journal J. Bacteriol. (1987) 169:367-370 !$#title Nucleotide sequence of the gene encoding the nitrogenase !1iron protein of Thiobacillus ferrooxidans. !$#cross-references MUID:87083392; PMID:3539923 !$#accession A91841 !'##molecule_type DNA !'##residues 1-54,'C',56-128,'E',130-175,'F',177-222 ##label PRE GENETICS !$#gene nifD CLASSIFICATION #superfamily dinitrogenase alpha chain; nitrogenase !1vanadium-iron protein alpha chain homology KEYWORDS 4Fe-4S; ATP; iron; iron-sulfur protein; metalloprotein; !1molybdenum; nitrogen fixation; oxidoreductase FEATURE !$23-489 #domain nitrogenase vanadium-iron protein alpha chain !8homology #label VIA\ !$71,97,163 #binding_site 4Fe-4S cluster 1 (Cys) (covalent) !8#status predicted\ !$97 #binding_site 4Fe-4S cluster 2 (Cys) (covalent) !8#status predicted\ !$284 #binding_site homocitryl Mo-7Fe-8S cluster (Cys) !8(covalent) #status predicted\ !$451 #binding_site homocitryl Mo-7Fe-8S cluster molybdenum !8(His) (ligand) #status predicted SUMMARY #length 489 #molecular-weight 55056 #checksum 2613 SEQUENCE /// ENTRY NIZRAT #type fragment TITLE nitrogenase (EC 1.18.6.1) molybdenum-iron protein alpha chain - Rhizobium leguminosarum bv. trifolii (fragment) ALTERNATE_NAMES dinitrogenase alpha chain; nitrogenase, component I alpha chain ORGANISM #formal_name Rhizobium leguminosarum bv. trifolii DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 19-Jan-2001 ACCESSIONS A00543 REFERENCE A90942 !$#authors Scott, K.F.; Rolfe, B.G.; Shine, J. !$#journal DNA (1983) 2:149-155 !$#title Biological nitrogen fixation: primary structure of the !1Rhizobium trifolii iron protein gene. !$#cross-references MUID:83261209; PMID:6307623 !$#accession A00543 !'##molecule_type DNA !'##residues 1-141 ##label SCO !'##experimental_source strain SU329 COMMENT The key enzymatic reactions in nitrogen fixation are !1catalyzed by the nitrogenase complex, which has two !1components: the iron protein (also called component II or !1nitrogenase reductase) and the molybdenum-iron protein, !1which is a tetramer of two alpha and two beta chains that !1binds 30-32 Fe, 2 Mo, and inorganic sulfur. GENETICS !$#gene nifD CLASSIFICATION #superfamily dinitrogenase alpha chain; nitrogenase !1vanadium-iron protein alpha chain homology KEYWORDS 4Fe-4S; ATP; iron; iron-sulfur protein; metalloprotein; !1molybdenum; nitrogen fixation; oxidoreductase FEATURE !$17-141 #domain nitrogenase vanadium-iron protein alpha chain !8homology (fragment) #label VIA\ !$72,98 #binding_site 4Fe-4S cluster 1 (Cys) (covalent) !8#status predicted\ !$98 #binding_site 4Fe-4S cluster 2 (Cys) (covalent) !8#status predicted SUMMARY #length 141 #checksum 2009 SEQUENCE /// ENTRY NIKBMA #type complete TITLE nitrogenase (EC 1.18.6.1) molybdenum-iron protein alpha chain - Klebsiella pneumoniae ALTERNATE_NAMES dinitrogenase alpha chain; nitrogenase component I alpha chain ORGANISM #formal_name Klebsiella pneumoniae DATE 29-Jul-1981 #sequence_revision 01-May-1998 #text_change 19-Jan-2001 ACCESSIONS S01729; S02504; S03823; A00544; A32520; S02051; B32511 REFERENCE S01729 !$#authors Steinbauer, J.; Wenzel, W.; Hess, D. !$#journal Nucleic Acids Res. (1988) 16:7199 !$#title Nucleotide and deduced amino acid sequences of the !1Klebsiella pneumoniae nifK gene coding for the beta-subunit !1of nitrogenase MoFe protein. !$#cross-references MUID:88303358; PMID:3043382 !$#accession S01729 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-483 ##label STE !'##cross-references EMBL:X07748; NID:g43844; PIDN:CAA30571.1; !1PID:g43845 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1May 1988 REFERENCE S01836 !$#authors Arnold, W.; Rump, A.; Klipp, W.; Priefer, U.B.; Puehler, A. !$#journal J. Mol. Biol. (1988) 203:715-738 !$#title Nucleotide sequence of a 24,206-base-pair DNA fragment !1carrying the entire nitrogen fixation gene cluster of !1Klebsiella pneumoniae. !$#cross-references MUID:89094839; PMID:3062178 !$#accession S02504 !'##molecule_type DNA !'##residues 1-354,'I',356-483 ##label ARN !'##cross-references EMBL:X13303; NID:g43820; PIDN:CAA31667.1; !1PID:g43823 REFERENCE S03823 !$#authors Holland, D.; Zilberstein, A.; Zamir, A.; Sussman, J.L. !$#journal Biochem. J. (1987) 247:277-285 !$#title A quantitative approach to sequence comparisons of !1nitrogenase MoFe protein alpha- and beta-subunits including !1the newly sequenced nifK gene from Klebsiella pneumoniae. !$#cross-references MUID:88106348; PMID:3322261 !$#accession S03823 !'##molecule_type DNA !'##residues 452-483 ##label HOL !'##cross-references EMBL:X06243; NID:g43848; PIDN:CAA29587.1; !1PID:g809705 !'##note the authors translated the codon TAC for residue 453 as Leu REFERENCE A92834 !$#authors Scott, K.F.; Rolfe, B.G.; Shine, J. !$#journal J. Mol. Appl. Genet. (1981) 1:71-81 !$#title Biological nitrogen fixation: primary structure of the !1Klebsiella pneumoniae nifH and nifD genes. !$#cross-references MUID:82267647; PMID:6809876 !$#accession A00544 !'##molecule_type DNA !'##residues 1-207 ##label SCO !'##cross-references GB:J01741; NID:g43874; PIDN:CAA23904.1; PID:g43876 !'##experimental_source strain UNF841 REFERENCE A32520 !$#authors Ioannidis, I.; Buck, M. !$#journal Biochem. J. (1987) 247:287-291 !$#title Nucleotide sequence of the Klebsiella pneumoniae nifD gene !1and predicted amino acid sequence of the alpha-subunit of !1nitrogenase MoFe protein. !$#cross-references MUID:88106349; PMID:3322262 !$#accession A32520 !'##molecule_type DNA !'##residues 1-15,'Q',17-483 ##label IOA !'##cross-references GB:Y00316; NID:g43846 REFERENCE S02051 !$#authors Ligon, J.M.; Nakas, J.P. !$#journal Nucleic Acids Res. (1988) 16:11843 !$#title Nucleotide sequence of nifK and partial sequence of nifD !1from Frankia species strain FaC1. !$#cross-references MUID:89098356; PMID:3211766 !$#accession S02051 !'##status translation not shown !'##molecule_type DNA !'##residues 207-260,'GDGD',265-287,'D',289-340,'NIA',344-348, !1'LRCCSIWRLP',362-468,'T',470-483 ##label LIG !'##cross-references EMBL:X12649; NID:g43415; PIDN:CAA31179.1; !1PID:g809697 REFERENCE S10137 !$#authors Ligon, J.M.; Nakas, J.P. !$#journal Nucleic Acids Res. (1990) 18:1097 !$#contents annotation; correction of species identification COMMENT The key enzymatic reactions in nitrogen fixation are !1catalyzed by the nitrogenase complex, which has two !1components: the molybdenum-iron protein (also called !1component I or dinitrogenase) and the iron protein (also !1called component II or nitrogenase reductase). GENETICS !$#gene nifD COMPLEX heterotetramer of two alpha and two beta chains FUNCTION !$#description the enzyme complex catalyzes the reduction of dinitrogen to !12 molecules of ammonia with the hydrolysis of 16 molecules !1of ATP to ADP and phosphate and the oxidation of ferredoxin !$#pathway nitrogen fixation CLASSIFICATION #superfamily dinitrogenase alpha chain; nitrogenase !1vanadium-iron protein alpha chain homology KEYWORDS 4Fe-4S; ATP; heterotetramer; iron-sulfur protein; !1metalloprotein; molybdenum; nitrogen fixation; !1oxidoreductase FEATURE !$13-483 #domain nitrogenase vanadium-iron protein alpha chain !8homology #label VIA\ !$63,89,155 #binding_site 4Fe-4S cluster 1 (Cys) (covalent) !8#status predicted\ !$89 #binding_site 4Fe-4S cluster 2 (Cys) (covalent) !8#status predicted\ !$275 #binding_site homocitryl Mo-7Fe-8S cluster (Cys) !8(covalent) #status predicted\ !$442 #binding_site homocitryl Mo-7Fe-8S cluster molybdenum !8(His) (ligand) #status predicted SUMMARY #length 483 #molecular-weight 54157 #checksum 3054 SEQUENCE /// ENTRY NICLMA #type complete TITLE nitrogenase (EC 1.18.6.1) molybdenum-iron protein alpha chain [validated] - Clostridium pasteurianum ALTERNATE_NAMES dinitrogenase alpha chain; nitrogenase component I alpha chain ORGANISM #formal_name Clostridium pasteurianum DATE 01-Sep-1981 #sequence_revision 31-Dec-1991 #text_change 19-Jan-2001 ACCESSIONS S07389; I40816; A00545 REFERENCE S07389 !$#authors Wang, S.Z.; Chen, J.S.; Johnson, J.L. !$#journal Nucleic Acids Res. (1987) 15:3935 !$#title Nucleotide and deduced amino acid sequences of nifD encoding !1the alpha-subunit of nitrogenase MoFe protein of Clostridium !1pasteurianum. !$#cross-references MUID:87231095; PMID:3473447 !$#accession S07389 !'##molecule_type DNA !'##residues 1-534 ##label WAN !'##cross-references EMBL:Y00155; NID:g40583; PIDN:CAA68349.1; !1PID:g580995 REFERENCE I40814 !$#authors Chen, K.C. !$#journal J. Bacteriol. (1986) 166:162-172 !$#title Structural features of multiple nifH-like sequences and very !1biased codon usage in nitrogenase genes of Clostridium !1pasteurianum. !$#cross-references MUID:86168010; PMID:3457003 !$#accession I40816 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-167 ##label CHE !'##cross-references GB:M21537; NID:g144870; PIDN:AAA83531.1; !1PID:g551775 REFERENCE A00545 !$#authors Hase, T.; Nakano, T.; Matsubara, H.; Zumft, W.G. !$#journal J. Biochem. (1981) 90:295-298 !$#title Correspondence of the larger subunit of the MoFe-protein in !1clostridial nitrogenase to the nif D gene products of other !1N-2-fixing organisms. !$#cross-references MUID:82030699; PMID:7026551 !$#accession A00545 !'##molecule_type protein !'##residues 2-41,'K',43-94,'D',96-180 ##label HAS REFERENCE A51301 !$#authors Kim, J.; Woo, D.; Rees, D.C. !$#submission submitted to the Brookhaven Protein Data Bank, March 1993 !$#cross-references PDB:1MIO !$#contents annotation; X-ray crystallography, 3.0 angstroms, residues !12-425,'A',427-526 COMMENT The key enzymatic reactions in nitrogen fixation are !1catalyzed by the nitrogenase complex, which has two !1components: the molybdenum-iron protein (also called !1component I or dinitrogenase) and the iron protein (also !1called component II or nitrogenase reductase). COMMENT Each alpha/beta dimer covalently binds one !1molybdenum-iron-sulfur cluster and two 4Fe-4S clusters. GENETICS !$#gene nifD !$#start_codon GTG COMPLEX heterotetramer of two alpha and two beta chains FUNCTION !$#description the enzyme complex catalyzes the reduction of dinitrogen to !12 molecules of ammonia with the hydrolysis of 16 molecules !1of ATP to ADP and phosphate and the oxidation of ferredoxin. !$#pathway nitrogen fixation CLASSIFICATION #superfamily dinitrogenase alpha chain; nitrogenase !1vanadium-iron protein alpha chain homology KEYWORDS 4Fe-4S; ATP; heterotetramer; iron-sulfur protein; !1metalloprotein; molybdenum; nitrogen fixation; !1oxidoreductase FEATURE !$2-534 #product nitrogenase molybdenum-iron protein alpha !8chain #status experimental #label MAT\ !$5-522 #domain nitrogenase vanadium-iron protein alpha chain !8homology #label VIA\ !$53,79,145 #binding_site 4Fe-4S cluster 1 (Cys) (covalent) !8#status experimental\ !$79 #binding_site 4Fe-4S cluster 2 (Cys) (covalent) !8#status experimental\ !$262 #binding_site homocitryl Mo-7Fe-8S cluster (Cys) !8(covalent) #status experimental\ !$482 #binding_site homocitryl Mo-7Fe-8S cluster molybdenum !8(His) (ligand) #status experimental SUMMARY #length 534 #molecular-weight 59125 #checksum 2428 SEQUENCE /// ENTRY NIAVMA #type complete TITLE nitrogenase (EC 1.18.6.1) 1 molybdenum-iron protein alpha chain [validated] - Azotobacter vinelandii ALTERNATE_NAMES dinitrogenase alpha chain; nitrogenase, component I alpha chain ORGANISM #formal_name Azotobacter vinelandii DATE 28-Dec-1987 #sequence_revision 07-Apr-1994 #text_change 19-Jan-2001 ACCESSIONS A43049; S02324; B23969; B13724 REFERENCE A43049 !$#authors Dean, D.R. !$#submission submitted to GenBank, September 1988 !$#accession A43049 !'##molecule_type DNA !'##residues 1-492 ##label JAC !'##cross-references GB:M20568; NID:g758356; PIDN:AAA64710.1; !1PID:g758358 !'##experimental_source strain OP REFERENCE S02323 !$#authors Hiratsuka, K.; Roy, K.L. !$#journal Nucleic Acids Res. (1988) 16:1207 !$#title Sequence of a 1.4 kb Eco RI fragment of Azotobacter !1vinelandii nif DNA. !$#cross-references MUID:88144000; PMID:3344210 !$#accession S02324 !'##molecule_type DNA !'##residues 1-409 ##label HIR !'##cross-references EMBL:X06886; NID:g39263; PIDN:CAA30004.1; !1PID:g39265 !'##experimental_source strain UW REFERENCE A94666 !$#authors Brigle, K.E.; Newton, W.E.; Dean, D.R. !$#journal Gene (1985) 37:37-44 !$#title Complete nucleotide sequence of the Azotobacter vinelandii !1nitrogenase structural gene cluster. !$#cross-references MUID:86031364; PMID:3863780 !$#accession B23969 !'##molecule_type DNA !'##residues 1-2,'R',4-211,'A',213-257,'Y',259-260,'Q',262-406,'M', !1408-439,'Q',441-492 ##label BRI !'##cross-references GB:M11579; NID:g142329; PIDN:AAA22143.1; !1PID:g142331 !'##experimental_source strain UW REFERENCE A92227 !$#authors Lundell, D.J.; Howard, J.B. !$#journal J. Biol. Chem. (1978) 253:3422-3426 !$#title Isolation and partial characterization of two different !1subunits from the molybdenum-iron protein of Azotobacter !1vinelandii nitrogenase. !$#cross-references MUID:78171480; PMID:649581 !$#accession B13724 !'##molecule_type protein !'##residues 2-20;'IFEAF' ##label LUN !'##experimental_source strain OP, ATCC 13705 !'##note the authors refer to this as the beta chain REFERENCE A32055 !$#authors Jacobson, M.R.; Brigle, K.E.; Bennett, L.T.; Setterquist, !1R.A.; Wilson, M.S.; Cash, V.L.; Beynon, J.; Newton, W.E.; !1Dean, D.R. !$#journal J. Bacteriol. (1989) 171:1017-1027 !$#title Physical and genetic map of the major nif gene cluster from !1Azotobacter vinelandii. !$#cross-references MUID:89123097; PMID:2644218 !$#contents annotation; genetics REFERENCE A67331 !$#authors Peters, J.W.; Stowell, M.H.B.; Soltis, S.M.; Day, M.W.; Kim, !1J.; Rees, D.C. !$#submission submitted to the Brookhaven Protein Data Bank, December 1996 !$#cross-references PDB:3MIN !$#contents annotation; X-ray crystallography, 2.03 angstroms, residues !15-35;45-480 REFERENCE A49884 !$#authors Kim, J.; Rees, D.C. !$#journal Science (1992) 257:1677-1682 !$#title Structural models for the metal centers in the nitrogenase !1molybdenum-iron protein. !$#cross-references MUID:92410323; PMID:1529354 !$#contents annotation; X-ray crystallography, 2.7 angstroms; cofactor !1structure REFERENCE A49883 !$#authors Kim, J.; Rees, D.C. !$#journal Nature (1992) 360:553-560 !$#title Crystallographic structure and functional implications of !1the nitrogenase molybdenum-iron protein from Azotobacter !1vinelandii. !$#contents annotation; X-ray crystallography, 2.7 angstroms; cofactor !1structure COMMENT The key enzymatic reactions in nitrogen fixation are !1catalyzed by the nitrogenase complex, which has two !1components: the molybdenum-iron protein (also called !1component I or dinitrogenase) and the iron protein (also !1called component II or nitrogenase reductase). COMMENT Each alpha/beta dimer covalently binds one !1molybdenum-iron-sulfur cluster and two 4Fe-4S clusters. GENETICS !$#gene nifD COMPLEX heterotetramer of two alpha and two beta chains FUNCTION !$#description the enzyme complex catalyzes the reduction of dinitrogen to !12 molecules of ammonia with the hydrolysis of 16 molecules !1of ATP to ADP and phosphate and the oxidation of ferredoxin. !$#pathway nitrogen fixation CLASSIFICATION #superfamily dinitrogenase alpha chain; nitrogenase !1vanadium-iron protein alpha chain homology KEYWORDS 4Fe-4S; ATP; heterotetramer; iron-sulfur protein; !1metalloprotein; molybdenum; nitrogen fixation; !1oxidoreductase FEATURE !$12-482 #domain nitrogenase vanadium-iron protein alpha chain !8homology #label VIA\ !$62,88,154 #binding_site 4Fe-4S cluster 1 (Cys) (covalent) !8#status experimental\ !$88 #binding_site 4Fe-4S cluster 2 (Cys) (covalent) !8#status experimental\ !$275 #binding_site homocitryl Mo-7Fe-8S cluster (Cys) !8(covalent) #status experimental\ !$442 #binding_site homocitryl Mo-7Fe-8S cluster molybdenum !8(His) (ligand) #status experimental SUMMARY #length 492 #molecular-weight 55289 #checksum 5865 SEQUENCE /// ENTRY NIZJAM #type complete TITLE nitrogenase (EC 1.18.6.1) molybdenum-iron protein alpha chain - Bradyrhizobium japonicum ALTERNATE_NAMES dinitrogenase alpha chain; nitrogenase component I alpha chain ORGANISM #formal_name Bradyrhizobium japonicum DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 19-Jan-2001 ACCESSIONS S07301; S09564 REFERENCE S07301 !$#authors Kaluza, K.; Hennecke, H. !$#journal Mol. Gen. Genet. (1984) 196:35-42 !$#title Fine structure analysis of the nifDK operon encoding the !1alpha and beta subunits of dinitrogenase from Rhizobium !1japonicum. !$#accession S07301 !'##molecule_type DNA !'##residues 1-515 ##label KAL !'##cross-references EMBL:X01045; NID:g46172; PIDN:CAA25523.1; !1PID:g46173 !'##note the source is designated as Rhizobium japonicum REFERENCE S07446 !$#authors Adams, T.H.; Chelm, B.K. !$#journal J. Mol. Appl. Genet. (1984) 2:392-405 !$#title The nifH and nifDK promoter regions from Rhizobium japonicum !1share structural homologies with each other and with !1nitrogen-regulated promoters from other organisms. !$#cross-references MUID:84241516; PMID:6588133 !$#accession S09564 !'##molecule_type DNA !'##residues 1-23,'P',25-35,'R',37-57,'R',59-100,'G',102-116 ##label ADA !'##cross-references GB:K01621; NID:g152283; PIDN:AAA26310.1; !1PID:g551966 !'##note the authors translated the codon CGG for residue 36 as Ala and !1TGC for residue 93 as Lys !'##note the source is designated as Rhizobium japonicum GENETICS !$#gene nifD CLASSIFICATION #superfamily dinitrogenase alpha chain; nitrogenase !1vanadium-iron protein alpha chain homology KEYWORDS 4Fe-4S; ATP; heterotetramer; iron; iron-sulfur protein; !1metalloprotein; molybdenum; nitrogen fixation; !1oxidoreductase FEATURE !$19-491 #domain nitrogenase vanadium-iron protein alpha chain !8homology #label VIA\ !$67,93,159 #binding_site 4Fe-4S cluster 1 (Cys) (covalent) !8#status predicted\ !$93 #binding_site 4Fe-4S cluster 2 (Cys) (covalent) !8#status predicted\ !$283 #binding_site homocitryl Mo-7Fe-8S cluster (Cys) !8(covalent) #status predicted\ !$451 #binding_site homocitryl Mo-7Fe-8S cluster molybdenum !8(His) (ligand) #status predicted SUMMARY #length 515 #molecular-weight 57991 #checksum 597 SEQUENCE /// ENTRY NIZJME #type complete TITLE nitrogenase molybdenum-cofactor synthesis protein nifE - Bradyrhizobium japonicum ORGANISM #formal_name Bradyrhizobium japonicum DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 11-Jun-1999 ACCESSIONS S12263; S16637 REFERENCE S12263 !$#authors Aguilar, O.M.; Taormino, J.; Thoeny, B.; Ramseier, T.; !1Hennecke, H.; Szalay, A.A. !$#journal Mol. Gen. Genet. (1990) 224:413-420 !$#title The nifEN genes participating in FeMo cofactor biosynthesis !1and genes encoding dinitrogenase are part of the same operon !1in Bradyrhizobium species. !$#cross-references MUID:91094779; PMID:2266945 !$#accession S12263 !'##molecule_type DNA !'##residues 1-547 ##label AGU1 !'##cross-references EMBL:X56894 REFERENCE S16637 !$#authors Agiular, O.M. !$#submission submitted to the EMBL Data Library, August 1991 !$#accession S16637 !'##molecule_type DNA !'##residues 1-57,'N',59-547 ##label AGU2 !'##cross-references EMBL:X56894; NID:g39541; PIDN:CAA40213.1; !1PID:g39542 GENETICS !$#gene nifE CLASSIFICATION #superfamily dinitrogenase alpha chain; nitrogenase !1vanadium-iron protein alpha chain homology KEYWORDS 4Fe-4S; iron; iron-sulfur protein; metalloprotein; !1molybdenum; nitrogen fixation FEATURE !$1-452 #domain nitrogenase vanadium-iron protein alpha chain !8homology #label VIA\ !$45,70,131 #binding_site 4Fe-4S cluster 1 (Cys) (covalent) !8#status predicted\ !$70 #binding_site 4Fe-4S cluster 2 (Cys) (covalent) !8#status predicted\ !$248 #binding_site homocitryl Mo-7Fe-8S cluster (Cys) !8(covalent) #status predicted SUMMARY #length 547 #molecular-weight 59522 #checksum 8053 SEQUENCE /// ENTRY A36936 #type complete TITLE nitrogenase (EC 1.18.6.1) vanadium-iron protein alpha/delta chain - Anabaena variabilis (ATCC 29413) ORGANISM #formal_name Anabaena variabilis #variety strain FD DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS A36936 REFERENCE A36936 !$#authors Thiel, T. !$#journal J. Bacteriol. (1993) 175:6276-6286 !$#title Characterization of genes for an alternative nitrogenase in !1the cyanobacterium Anabaena variabilis. !$#cross-references MUID:94012490; PMID:8407800 !$#accession A36936 !'##molecule_type DNA !'##residues 1-587 ##label THI !'##cross-references GB:L20472; NID:g304058; PIDN:AAC36815.1; !1PID:g304059 !'##note in the author's translation, residues 1-5 are followed by !1residues 33-52, 13-32, 6-12, and 53-587 COMMENT It is not known whether this protein contains the !1molybdenum, vanadium, or iron-only form of the cofactor. GENETICS !$#gene vnfDG !$#note this gene appears to be the result of a fusion of the vnfD !1and vnfG genes found separately in other closely related !1organisms FUNCTION !$#description the enzyme complex catalyzes the reduction of dinitrogen to !12 molecules of ammonia with the hydrolysis of 16 molecules !1of ATP to ADP and phosphate and the oxidation of ferredoxin !$#pathway nitrogen fixation CLASSIFICATION #superfamily dinitrogenase alpha/delta chain; nitrogenase !1vanadium-iron protein alpha chain homology; nitrogenase !1vanadium-iron protein delta chain homology KEYWORDS 4Fe-4S; ATP; iron-sulfur protein; metalloprotein; !1molybdenum; nitrogen fixation; oxidoreductase FEATURE !$1-462 #domain nitrogenase vanadium-iron protein alpha chain !8homology #label VIA\ !$477-587 #domain nitrogenase vanadium-iron protein delta chain !8homology #label VID\ !$49,75,138 #binding_site 4Fe-4S cluster 1 (Cys) (covalent) !8#status predicted\ !$75 #binding_site 4Fe-4S cluster 2 (Cys) (covalent) !8#status predicted\ !$257 #binding_site homocitryl Mo-7Fe-8S cluster (Cys) !8(covalent) #status predicted\ !$423 #binding_site homocitryl Mo-7Fe-8S cluster molybdenum !8(His) (ligand) #status predicted SUMMARY #length 587 #molecular-weight 66195 #checksum 8307 SEQUENCE /// ENTRY S04114 #type complete TITLE nitrogenase (EC 1.18.6.1) vanadium-iron protein delta chain - Azotobacter chroococcum ORGANISM #formal_name Azotobacter chroococcum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S04114; S10433; S14696 REFERENCE S04113 !$#authors Robson, R.L.; Woodley, P.R.; Pau, R.N.; Eady, R.R. !$#journal EMBO J. (1989) 8:1217-1224 !$#title Structural genes for the vanadium nitrogenase from !1Azotobacter chroococcum. !$#cross-references MUID:89305526; PMID:2743980 !$#accession S04114 !'##molecule_type DNA !'##residues 1-113 ##label ROB !'##cross-references EMBL:X15077; NID:g38762; PIDN:CAA33174.1; !1PID:g38764 !'##note the sequence from Fig. 5 is inconsistent with that from Fig. 2 !1in lacking 13-Thr !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing !'##note the authors translated the codon CAA for residue 101 as Thr and !1AGC for residue 102 as Arg REFERENCE S10429 !$#authors Fallik, E.; Robson, R.L. !$#submission submitted to the EMBL Data Library, February 1990 !$#description Complete sequence of the region encoding the structural !1genes for the vanadium nitrogenase of Azotobacter !1chroococcum. !$#accession S10433 !'##molecule_type DNA !'##residues 1-113 ##label FAL !'##cross-references EMBL:X51756; NID:g38755; PIDN:CAA36059.1; !1PID:g38760 GENETICS !$#gene vnfG CLASSIFICATION #superfamily dinitrogenase delta chain; nitrogenase !1vanadium-iron protein delta chain homology KEYWORDS ATP; metalloprotein; nitrogen fixation; oxidoreductase; !1vanadium FEATURE !$2-113 #product nitrogenase vanadium-iron protein delta !8chain #status experimental #label MAT\ !$3-113 #domain nitrogenase vanadium-iron protein delta chain !8homology #label VID SUMMARY #length 113 #molecular-weight 13364 #checksum 9816 SEQUENCE /// ENTRY D35405 #type complete TITLE nitrogenase (EC 1.18.6.1) 2 vanadium-iron protein delta chain - Azotobacter vinelandii ORGANISM #formal_name Azotobacter vinelandii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS D35405 REFERENCE A35405 !$#authors Joerger, R.D.; Loveless, T.M.; Pau, R.N.; Mitchenall, L.A.; !1Simon, B.H.; Bishop, P.E. !$#journal J. Bacteriol. (1990) 172:3400-3408 !$#title Nucleotide sequences and mutational analysis of the !1structural genes for nitrogenase 2 of Azotobacter !1vinelandii. !$#cross-references MUID:90264339; PMID:2345152 !$#accession D35405 !'##status preliminary !'##molecule_type DNA !'##residues 1-113 ##label JOE !'##cross-references GB:M32371; NID:g142401; PIDN:AAA22173.1; !1PID:g142405 CLASSIFICATION #superfamily dinitrogenase delta chain; nitrogenase !1vanadium-iron protein delta chain homology KEYWORDS ATP; metalloprotein; nitrogen fixation; oxidoreductase; !1vanadium FEATURE !$3-113 #domain nitrogenase vanadium-iron protein delta chain !8homology #label VID SUMMARY #length 113 #molecular-weight 13372 #checksum 760 SEQUENCE /// ENTRY S34611 #type complete TITLE nitrogenase (EC 1.18.6.1) delta chain anfG homolog - Clostridium pasteurianum ORGANISM #formal_name Clostridium pasteurianum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S34611 REFERENCE S34610 !$#authors Zinoni, F.; Robson, R.M.; Robson, R.L. !$#journal Biochim. Biophys. Acta (1993) 1174:83-86 !$#title Organization of potential alternative nitrogenase genes from !1Clostridium pasteurianum. !$#cross-references MUID:93326641; PMID:8334167 !$#accession S34611 !'##status preliminary !'##molecule_type DNA !'##residues 1-116 ##label ZIN !'##cross-references GB:L09762; NID:g385204; PIDN:AAC36971.1; !1PID:g385206 COMMENT This protein is presumed not to contain molybdenum. CLASSIFICATION #superfamily dinitrogenase delta chain; nitrogenase !1vanadium-iron protein delta chain homology KEYWORDS ATP; metalloprotein; nitrogen fixation; oxidoreductase FEATURE !$6-116 #domain nitrogenase vanadium-iron protein delta chain !8homology #label VID SUMMARY #length 116 #molecular-weight 13713 #checksum 2953 SEQUENCE /// ENTRY C32057 #type complete TITLE nitrogenase (EC 1.18.6.1) 3 delta chain - Azotobacter vinelandii ORGANISM #formal_name Azotobacter vinelandii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS C32057; S34059 REFERENCE A32057 !$#authors Joerger, R.D.; Jacobson, M.R.; Premakumar, R.; Wolfinger, !1E.D.; Bishop, P.E. !$#journal J. Bacteriol. (1989) 171:1075-1086 !$#title Nucleotide sequence and mutational analysis of the !1structural genes (anfHDGK) for the second alternative !1nitrogenase from Azotobacter vinelandii. !$#cross-references MUID:89123105; PMID:2644222 !$#accession C32057 !'##molecule_type DNA !'##residues 1-132 ##label JOE !'##cross-references GB:M23528; NID:g142378; PIDN:AAA82510.1; !1PID:g142381 REFERENCE S34058 !$#authors Pau, R.N.; Eldridge, M.E.; Lowe, D.J.; Mitchenall, L.A.; !1Eady, R.R. !$#journal Biochem. J. (1993) 293:101-107 !$#title Molybdenum-independent nitrogenases of Azotobacter !1vinelandii: a functional species of alternative !1nitrogenase-3 isolated from a molybdenum-tolerant strain !1contains an iron-molybdenum cofactor. !$#cross-references MUID:93319493; PMID:8392330 !$#accession S34059 !'##molecule_type protein !'##residues 2-4,'X',6-8 ##label PAU COMMENT Nitrogenase 3 may be able to use either the molybenum !1cofactor, or an uncharacterized cofactor containing iron but !1not molybenum or vanadium. GENETICS !$#gene anfG FUNCTION !$#description the enzyme complex catalyzes the reduction of dinitrogen to !12 molecules of ammonia with the hydrolysis of 16 molecules !1of ATP to ADP and phosphate and the oxidation of ferredoxin !$#pathway nitrogen fixation CLASSIFICATION #superfamily dinitrogenase delta chain; nitrogenase !1vanadium-iron protein delta chain homology KEYWORDS ATP; metalloprotein; nitrogen fixation; oxidoreductase FEATURE !$22-132 #domain nitrogenase vanadium-iron protein delta chain !8homology #label VID SUMMARY #length 132 #molecular-weight 15343 #checksum 4843 SEQUENCE /// ENTRY S34946 #type complete TITLE nitrogenase (EC 1.18.6.1) delta chain anfG - Rhodobacter capsulatus ORGANISM #formal_name Rhodobacter capsulatus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S34946 REFERENCE S34944 !$#authors Schueddekopf, K.; Hennecke, S.; Liese, U.; Kutsche, M.; !1Klipp, W. !$#journal Mol. Microbiol. (1993) 8:673-684 !$#title Characterization of anf genes specific for the alternative !1nitrogenase and identification of nif genes required for !1both nitrogenases in Rhodobacter capsulatus. !$#cross-references MUID:93323746; PMID:8332060 !$#accession S34946 !'##status preliminary; nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-115 ##label SCH !'##cross-references EMBL:X70033; NID:g312236; PIDN:CAA49626.1; !1PID:g312239 GENETICS !$#gene anfG CLASSIFICATION #superfamily dinitrogenase delta chain; nitrogenase !1vanadium-iron protein delta chain homology KEYWORDS ATP; metalloprotein; nitrogen fixation; oxidoreductase FEATURE !$5-115 #domain nitrogenase vanadium-iron protein delta chain !8homology #label VID SUMMARY #length 115 #molecular-weight 13396 #checksum 215 SEQUENCE /// ENTRY NIAVMB #type complete TITLE nitrogenase (EC 1.18.6.1) 1 molybdenum-iron protein beta chain [validated] - Azotobacter vinelandii ALTERNATE_NAMES dinitrogenase beta chain; nitrogenase, component I beta chain ORGANISM #formal_name Azotobacter vinelandii DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 19-Jan-2001 ACCESSIONS B43049; C23969; A13724 REFERENCE A43049 !$#authors Dean, D.R. !$#submission submitted to GenBank, September 1988 !$#accession B43049 !'##molecule_type DNA !'##residues 1-523 ##label JAC !'##cross-references GB:M20568; NID:g758356; PIDN:AAA64711.1; !1PID:g142346 !'##experimental_source strain OP REFERENCE A94666 !$#authors Brigle, K.E.; Newton, W.E.; Dean, D.R. !$#journal Gene (1985) 37:37-44 !$#title Complete nucleotide sequence of the Azotobacter vinelandii !1nitrogenase structural gene cluster. !$#cross-references MUID:86031364; PMID:3863780 !$#accession C23969 !'##molecule_type DNA !'##residues 1-523 ##label BRI !'##cross-references GB:M11579; NID:g142329; PIDN:AAA22144.1; !1PID:g142332 !'##experimental_source strain UW REFERENCE A92227 !$#authors Lundell, D.J.; Howard, J.B. !$#journal J. Biol. Chem. (1978) 253:3422-3426 !$#title Isolation and partial characterization of two different !1subunits from the molybdenum-iron protein of Azotobacter !1vinelandii nitrogenase. !$#cross-references MUID:78171480; PMID:649581 !$#accession A13724 !'##molecule_type protein !'##residues 2-20;521,'RV' ##label LUN !'##experimental_source strain OP, ATCC 13705 !'##note the authors refer to this as the alpha chain REFERENCE A67331 !$#authors Peters, J.W.; Stowell, M.H.B.; Soltis, S.M.; Day, M.W.; Kim, !1J.; Rees, D.C. !$#submission submitted to the Brookhaven Protein Data Bank, December 1996 !$#cross-references PDB:3MIN !$#contents annotation; X-ray crystallography, 2.03 angstroms, residues !12-523 REFERENCE A49884 !$#authors Kim, J.; Rees, D.C. !$#journal Science (1992) 257:1677-1682 !$#title Structural models for the metal centers in the nitrogenase !1molybdenum-iron protein. !$#cross-references MUID:92410323; PMID:1529354 !$#contents annotation; X-ray crystallography, 2.7 angstroms; cofactor !1structure REFERENCE A49883 !$#authors Kim, J.; Rees, D.C. !$#journal Nature (1992) 360:553-560 !$#title Crystallographic structure and functional implications of !1the nitrogenase molybdenum-iron protein from Azotobacter !1vinelandii. !$#contents annotation; X-ray crystallography, 2.7 angstroms; cofactor !1structure REFERENCE A32055 !$#authors Jacobson, M.R.; Brigle, K.E.; Bennett, L.T.; Setterquist, !1R.A.; Wilson, M.S.; Cash, V.L.; Beynon, J.; Newton, W.E.; !1Dean, D.R. !$#journal J. Bacteriol. (1989) 171:1017-1027 !$#title Physical and genetic map of the major nif gene cluster from !1Azotobacter vinelandii. !$#cross-references MUID:89123097; PMID:2644218 !$#contents annotation; genetics COMMENT The key enzymatic reactions in nitrogen fixation are !1catalyzed by the nitrogenase complex, which has two !1components: the molybdenum-iron protein (also called !1component I or dinitrogenase) and the iron protein (also !1called component II or nitrogenase reductase). COMMENT Each alpha/beta dimer covalently binds one !1molybdenum-iron-sulfur cluster and two 4Fe-4S clusters. GENETICS !$#gene nifK COMPLEX heterotetramer of two alpha and two beta chains FUNCTION !$#description the enzyme complex catalyzes the reduction of dinitrogen to !12 molecules of ammonia with the hydrolysis of 16 molecules !1of ATP to ADP and phosphate and the oxidation of ferredoxin. !$#pathway nitrogen fixation CLASSIFICATION #superfamily dinitrogenase beta chain KEYWORDS 4Fe-4S; ATP; heterotetramer; iron-sulfur protein; !1metalloprotein; nitrogen fixation; oxidoreductase FEATURE !$2-523 #product nitrogenase molybdenum-iron protein beta !8chain #status experimental #label PRO\ !$70,95,153 #binding_site 4Fe-4S cluster 2 (Cys) (covalent) !8#status experimental\ !$95 #binding_site 4Fe-4S cluster 1 (Cys) (covalent) !8#status experimental\ !$188 #binding_site 4Fe-4S cluster 2 iron (Ser) (ligand) !8#status experimental SUMMARY #length 523 #molecular-weight 59460 #checksum 6069 SEQUENCE /// ENTRY S02505 #type complete TITLE nitrogenase (EC 1.18.6.1) molybdenum-iron protein beta chain - Klebsiella pneumoniae ALTERNATE_NAMES nitrogenase component I beta chain ORGANISM #formal_name Klebsiella pneumoniae DATE 07-Jun-1990 #sequence_revision 10-May-1996 #text_change 19-Jan-2001 ACCESSIONS S02505; S01735; S03824; S02052; A32511 REFERENCE S01836 !$#authors Arnold, W.; Rump, A.; Klipp, W.; Priefer, U.B.; Puehler, A. !$#journal J. Mol. Biol. (1988) 203:715-738 !$#title Nucleotide sequence of a 24,206-base-pair DNA fragment !1carrying the entire nitrogen fixation gene cluster of !1Klebsiella pneumoniae. !$#cross-references MUID:89094839; PMID:3062178 !$#accession S02505 !'##molecule_type DNA !'##residues 1-520 ##label ARN !'##cross-references EMBL:X13303; NID:g43820; PIDN:CAA31668.1; !1PID:g43824 REFERENCE S01729 !$#authors Steinbauer, J.; Wenzel, W.; Hess, D. !$#journal Nucleic Acids Res. (1988) 16:7199 !$#title Nucleotide and deduced amino acid sequences of the !1Klebsiella pneumoniae nifK gene coding for the beta-subunit !1of nitrogenase MoFe protein. !$#cross-references MUID:88303358; PMID:3043382 !$#accession S01735 !'##molecule_type DNA !'##residues 1-56,'Q',58-416,'K',418-520 ##label STE !'##cross-references EMBL:X07749; NID:g43866; PIDN:CAA30573.1; !1PID:g43867 REFERENCE S03823 !$#authors Holland, D.; Zilberstein, A.; Zamir, A.; Sussman, J.L. !$#journal Biochem. J. (1987) 247:277-285 !$#title A quantitative approach to sequence comparisons of !1nitrogenase MoFe protein alpha- and beta-subunits including !1the newly sequenced nifK gene from Klebsiella pneumoniae. !$#cross-references MUID:88106348; PMID:3322261 !$#accession S03824 !'##molecule_type DNA !'##residues 1-56,'Q',58-286,'AAP',291-350,'IV',353-356,358-394, !1'GQQTLD',401-410,'R',412-421,'R',423-434,'SAGL',439-481,'S', !1483-496,'V',498-507,'PA',510-520 ##label HOL !'##cross-references EMBL:X06243; NID:g43848; PIDN:CAA29588.1; !1PID:g43850 REFERENCE S02051 !$#authors Ligon, J.M.; Nakas, J.P. !$#journal Nucleic Acids Res. (1988) 16:11843 !$#title Nucleotide sequence of nifK and partial sequence of nifD !1from Frankia species strain FaC1. !$#cross-references MUID:89098356; PMID:3211766 !$#accession S02052 !'##status translation not shown !'##molecule_type DNA !'##residues 1-23,'V',25-32,'R',34-56,'H',59-69,'HA',72-98,'G',100-162, !1'R',164-179,'W',181-221,'KL',222-224,'P',226-232,'TG', !1233-264,'Q',266-411,'NRARYS',418-450,'V',452-509,'A',511-520 !1##label LIG !'##cross-references EMBL:X12649; NID:g43415; PIDN:CAA31180.1; !1PID:g43416 REFERENCE S10137 !$#authors Ligon, J.M.; Nakas, J.P. !$#journal Nucleic Acids Res. (1990) 18:1097 !$#contents annotation; correction of species identification GENETICS !$#gene nifK CLASSIFICATION #superfamily dinitrogenase beta chain KEYWORDS 4Fe-4S; ATP; heterotetramer; iron-sulfur protein; !1metalloprotein; molybdenum; nitrogen fixation; !1oxidoreductase FEATURE !$2-520 #product nitrogenase molybdenum-iron protein beta !8chain #status predicted #label MAT\ !$69,94,152 #binding_site 4Fe-4S cluster 2 (Cys) (covalent) !8#status predicted\ !$94 #binding_site 4Fe-4S cluster 1 (Cys) (covalent) !8#status predicted\ !$187 #binding_site 4Fe-4S cluster 2 iron (Ser) (ligand) !8#status predicted SUMMARY #length 520 #molecular-weight 58407 #checksum 9961 SEQUENCE /// ENTRY NIBCBT #type complete TITLE nitrogenase (EC 1.18.6.1) molybdenum-iron protein beta chain - Thiobacillus ferrooxidans ALTERNATE_NAMES dinitrogenase beta chain; nitrogenase, component I beta chain ORGANISM #formal_name Thiobacillus ferrooxidans DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 19-Jan-2001 ACCESSIONS JT0341 REFERENCE A91597 !$#authors Rawlings, D.E. !$#journal Gene (1988) 69:337-343 !$#title Sequence and structural analysis of the alpha- and !1beta-dinitrogenase subunits of Thiobacillus ferrooxidans. !$#cross-references MUID:89172078; PMID:3234769 !$#accession JT0341 !'##molecule_type DNA !'##residues 1-518 ##label RAW !'##cross-references GB:M15238; GB:M22482; NID:g154637; PIDN:AAA27376.1; !1PID:g154640 !'##experimental_source ATCC 33020 COMMENT The key enzymatic reactions in nitrogen fixation are !1catalyzed by the nitrogenase complex, which has two !1components: the iron protein (also called component II or !1nitrogenase reductase) and the molybdenum-iron protein, !1which is a tetramer of two alpha and two beta chains that !1binds 30-32 Fe, 2 Mo, and inorganic sulfur. COMMENT The active form is a tetramer of two alpha and two beta !1chains, as a dimer of alpha/beta dimers. COMMENT Each alpha/beta dimer covalently binds one !1molybdenum-iron-sulfur cluster and two 4Fe-4S clusters. GENETICS !$#gene nifK CLASSIFICATION #superfamily dinitrogenase beta chain KEYWORDS 4Fe-4S; ATP; heterotetramer; iron-sulfur protein; !1metalloprotein; molybdenum; nitrogen fixation; !1oxidoreductase FEATURE !$70,94,152 #binding_site 4Fe-4S cluster 2 (Cys) (covalent) !8#status predicted\ !$94 #binding_site 4Fe-4S cluster 1 (Cys) (covalent) !8#status predicted\ !$187 #binding_site 4Fe-4S cluster 2 iron (Ser) (ligand) !8#status predicted SUMMARY #length 518 #molecular-weight 57892 #checksum 8429 SEQUENCE /// ENTRY B23874 #type complete TITLE nitrogenase (EC 1.18.6.1) molybdenum-iron protein beta chain - Rhizobium sp. ALTERNATE_NAMES dinitrogenase beta chain; nitrogenase component I beta chain ORGANISM #formal_name Rhizobium sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS B23874 REFERENCE A93542 !$#authors Weinman, J.J.; Fellows, F.F.; Gresshoff, P.M.; Shine, J.; !1Scott, K.F. !$#journal Nucleic Acids Res. (1984) 12:8329-8344 !$#title Structural analysis of the genes encoding the !1molybdenum-iron protein of nitrogenase in the Parasponia !1rhizobium strain ANU289. !$#cross-references MUID:85062817; PMID:6095197 !$#accession B23874 !'##molecule_type DNA !'##residues 1-513 ##label WEI !'##experimental_source strain ANU289 GENETICS !$#gene nifK CLASSIFICATION #superfamily dinitrogenase beta chain KEYWORDS ATP; iron-sulfur protein; molybdenum; nitrogen fixation; !1oxidoreductase SUMMARY #length 513 #molecular-weight 56538 #checksum 6501 SEQUENCE /// ENTRY NIAIMB #type complete TITLE nitrogenase (EC 1.18.6.1) molybdenum-iron protein beta chain - Anabaena sp. ALTERNATE_NAMES dinitrogenase beta chain; nitrogenase, component I beta chain ORGANISM #formal_name Anabaena sp. #note strain PCC 7120 DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 19-Jan-2001 ACCESSIONS A00546 REFERENCE A00546 !$#authors Mazur, B.J.; Chui, C.F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:6782-6786 !$#title Sequence of the gene coding for the beta-subunit of !1dinitrogenase from the blue-green alga Anabaena. !$#accession A00546 !'##molecule_type DNA !'##residues 1-512 ##label MAZ !'##cross-references GB:J01539; NID:g142063 !'##note this ORF is not annotated in GenBank entry ANANIFK, release !1103.0 COMMENT The key enzymatic reactions in nitrogen fixation are !1catalyzed by the nitrogenase complex, which has two !1components: the iron protein (also called component II or !1nitrogenase reductase) and the molybdenum-iron protein, !1which is a tetramer of two alpha and two beta chains that !1binds 30-32 Fe, 2 Mo, and inorganic sulfur. COMMENT Anabaena is a blue-green alga. COMMENT The active form is a tetramer of two alpha and two beta !1chains, as a dimer of alpha/beta dimers. COMMENT Each alpha/beta dimer covalently binds one !1molybdenum-iron-sulfur cluster and two 4Fe-4S clusters. GENETICS !$#gene nifK CLASSIFICATION #superfamily dinitrogenase beta chain KEYWORDS 4Fe-4S; ATP; heterotetramer; iron-sulfur protein; !1metalloprotein; molybdenum; nitrogen fixation; !1oxidoreductase FEATURE !$70,95,153 #binding_site 4Fe-4S cluster 2 (Cys) (covalent) !8#status predicted\ !$95 #binding_site 4Fe-4S cluster 1 (Cys) (covalent) !8#status predicted\ !$188 #binding_site 4Fe-4S cluster 2 iron (Ser) (ligand) !8#status predicted SUMMARY #length 512 #molecular-weight 57575 #checksum 6092 SEQUENCE /// ENTRY NICLMB #type complete TITLE nitrogenase (EC 1.18.6.1) molybdenum-iron protein beta chain [validated] - Clostridium pasteurianum ALTERNATE_NAMES dinitrogenase beta chain; nitrogenase, component I beta chain ORGANISM #formal_name Clostridium pasteurianum DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 19-Jan-2001 ACCESSIONS A29992 REFERENCE A29992 !$#authors Wang, S.Z.; Chen, J.S.; Johnson, J.L. !$#journal Biochemistry (1988) 27:2800-2810 !$#title Distinct structural features of the alpha and beta subunits !1of nitrogenase molybdenum-iron protein of Clostridium !1pasteurianum: an analysis of amino acid sequences. !$#cross-references MUID:88294019; PMID:2840948 !$#accession A29992 !'##molecule_type DNA !'##residues 1-458 ##label WAN !'##cross-references GB:M20380; NID:g144874 !'##experimental_source strain W5 !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing REFERENCE A51301 !$#authors Kim, J.; Woo, D.; Rees, D.C. !$#submission submitted to the Brookhaven Protein Data Bank, March 1993 !$#cross-references PDB:1MIO !$#contents annotation; X-ray crystallography, 3.0 angstroms, residues !12-458 COMMENT The key enzymatic reactions in nitrogen fixation are !1catalyzed by the nitrogenase complex, which has two !1components: the molybdenum-iron protein (also called !1component I or dinitrogenase) and the iron protein (also !1called component II or nitrogenase reductase). COMMENT Each alpha/beta dimer covalently binds one !1molybdenum-iron-sulfur cluster and two 4Fe-4S clusters. GENETICS !$#gene nifK COMPLEX heterotetramer of two alpha and two beta chains FUNCTION !$#description the enzyme complex catalyzes the reduction of dinitrogen to !12 molecules of ammonia with the hydrolysis of 16 molecules !1of ATP to ADP and phosphate and the oxidation of ferredoxin. !$#pathway nitrogen fixation CLASSIFICATION #superfamily dinitrogenase beta chain KEYWORDS 4Fe-4S; ATP; heterotetramer; iron-sulfur protein; !1metalloprotein; nitrogen fixation; oxidoreductase FEATURE !$2-458 #product nitrogenase molybdenum-iron protein beta !8chain #status experimental #label MAT\ !$23,48,106 #binding_site 4Fe-4S cluster 2 (Cys) (covalent) !8#status experimental\ !$48 #binding_site 4Fe-4S cluster 1 (Cys) (covalent) !8#status experimental\ !$141 #binding_site 4Fe-4S cluster 2 iron (Ser) (ligand) !8#status experimental SUMMARY #length 458 #molecular-weight 50119 #checksum 1218 SEQUENCE /// ENTRY NIZJMN #type complete TITLE nitrogenase (EC 1.18.6.1) molybdenum-iron protein nifN - Bradyrhizobium japonicum ORGANISM #formal_name Bradyrhizobium japonicum DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 19-Jan-2001 ACCESSIONS S12264 REFERENCE S12263 !$#authors Aguilar, O.M.; Taormino, J.; Thoeny, B.; Ramseier, T.; !1Hennecke, H.; Szalay, A.A. !$#journal Mol. Gen. Genet. (1990) 224:413-420 !$#title The nifEN genes participating in FeMo cofactor biosynthesis !1and genes encoding dinitrogenase are part of the same operon !1in Bradyrhizobium species. !$#cross-references MUID:91094779; PMID:2266945 !$#accession S12264 !'##molecule_type DNA !'##residues 1-469 ##label AGU !'##cross-references EMBL:X56894; NID:g39541; PIDN:CAA40214.1; !1PID:g39543 !'##note the sequence from Fig. 2 is inconsistent with that from Fig. 3 !1in having 303-Leu and 304-Ala and having an additional Ile !1and Arg after 354-Arg GENETICS !$#gene nifN CLASSIFICATION #superfamily dinitrogenase beta chain KEYWORDS 4Fe-4S; ATP; iron; iron-sulfur protein; metalloprotein; !1molybdenum; nitrogen fixation; oxidoreductase FEATURE !$44 #binding_site 4Fe-4S cluster 1 (Cys) (covalent) !8#status predicted SUMMARY #length 469 #molecular-weight 51231 #checksum 8152 SEQUENCE /// ENTRY A55692 #type complete TITLE anaerobic ribonucleotide reductase activase (EC 1.97.1.-) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 15-Jan-1999 #sequence_revision 15-Jan-1999 #text_change 01-Mar-2002 ACCESSIONS A55692; S56463; H65235 REFERENCE A55692 !$#authors Sun, X.; Eliasson, R.; Pontis, E.; Andersson, J.; Buist, G.; !1Sjoeberg, B.M.; Reichard, P. !$#journal J. Biol. Chem. (1995) 270:2443-2446 !$#title Generation of the glycyl radical of the anaerobic !1Escherichia coli ribonucleotide reductase requires a !1specific activating enzyme. !$#cross-references MUID:95155298; PMID:7852304 !$#accession A55692 !'##molecule_type DNA !'##residues 1-154 ##label SUN !'##cross-references GB:Z46865; NID:g607075; PIDN:CAA86937.1; !1PID:g619866 !'##note confirmed enzymatic activity and presence of iron, probably !1cysteine-ligated REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56463 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-154 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97134.1; !1PID:g537079 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65235 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-154 ##label BLAT !'##cross-references GB:AE000495; GB:U00096; NID:g2367361; !1PIDN:AAC77194.1; PID:g1790685; UWGP:b4237 !'##experimental_source strain K-12, substrain MG1655 COMMENT This enzyme specifically activates anaerobic ribonucleotide !1reductase (see PIR:A47331) to generate the glycyl free !1radical active site of that enzyme. GENETICS !$#gene nrdG !$#map_position 96 min CLASSIFICATION #superfamily anaerobic ribonucleotide reductase activase KEYWORDS iron; metalloprotein; oxidoreductase FEATURE !$26,30,33 #binding_site iron (Cys) #status predicted SUMMARY #length 154 #molecular-weight 17446 #checksum 6912 SEQUENCE /// ENTRY E64168 #type complete TITLE anaerobic ribonucleotide reductase activase (EC 1.97.1.-) - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 15-Jan-1999 #sequence_revision 15-Jan-1999 #text_change 11-Jun-1999 ACCESSIONS E64168 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession E64168 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-155 ##label TIGR !'##cross-references GB:U32795; GB:L42023; NID:g1574708; !1PIDN:AAC22810.1; PID:g1574712; TIGR:HI1155 COMMENT This enzyme specifically activates anaerobic ribonucleotide !1reductase (see PIR:A64047) to generate the glycyl free !1radical active site of that enzyme. CLASSIFICATION #superfamily anaerobic ribonucleotide reductase activase KEYWORDS iron; metalloprotein; oxidoreductase FEATURE !$26,30,33 #binding_site iron (Cys) #status predicted SUMMARY #length 155 #molecular-weight 17856 #checksum 7902 SEQUENCE /// ENTRY D69136 #type complete TITLE anaerobic ribonucleotide reductase activase (EC 1.97.1.-) - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 15-Jan-1999 #sequence_revision 15-Jan-1999 #text_change 11-Jun-1999 ACCESSIONS D69136 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession D69136 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-237 ##label MTH !'##cross-references GB:AE000814; GB:AE000666; NID:g2621334; !1PIDN:AAB84793.1; PID:g2621339 !'##experimental_source strain Delta H GENETICS !$#gene MTH287 !$#start_codon GTG CLASSIFICATION #superfamily anaerobic ribonucleotide reductase activase KEYWORDS iron; metalloprotein; oxidoreductase FEATURE !$64,68,71 #binding_site iron (Cys) #status predicted SUMMARY #length 237 #molecular-weight 26438 #checksum 2456 SEQUENCE /// ENTRY Z8BPT9 #type complete TITLE anaerobic ribonucleotide reductase activase (EC 1.97.1.-) - phage T4 ALTERNATE_NAMES gene 55.9 protein ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 11-Jun-1999 ACCESSIONS G29284 REFERENCE A30291 !$#authors Tomaschewski, J.; Rueger, W. !$#journal Nucleic Acids Res. (1987) 15:3632-3633 !$#title Nucleotide sequence and primary structures of gene products !1coded for by the T4 genome between map positions 48.266 kb !1and 39.166 kb. !$#cross-references MUID:87203398; PMID:3575111 !$#accession G29284 !'##molecule_type DNA !'##residues 1-156 ##label TOM !'##cross-references GB:Y00122; NID:g15346; PIDN:CAA68312.1; PID:g15354 GENETICS !$#gene 55.9 CLASSIFICATION #superfamily anaerobic ribonucleotide reductase activase KEYWORDS iron; metalloprotein; oxidoreductase FEATURE !$26,30,33 #binding_site iron (Cys) #status predicted SUMMARY #length 156 #molecular-weight 18247 #checksum 3765 SEQUENCE /// ENTRY S01789 #type complete TITLE formate acetyltransferase activating enzyme (EC 1.97.1.4), lyase 1-specific - Escherichia coli (strain K-12) ALTERNATE_NAMES formate C-acetyltransferase 1-activating enzyme; pyruvate formate-lyase I activase ORGANISM #formal_name Escherichia coli #variety strain K-12 DATE 06-Nov-1998 #sequence_revision 06-Nov-1998 #text_change 01-Mar-2002 ACCESSIONS S01789; E64829 REFERENCE S01788 !$#authors Roedel, W.; Plaga, W.; Frank, R.; Knappe, J. !$#journal Eur. J. Biochem. (1988) 177:153-158 !$#title Primary structures of Escherichia coli pyruvate !1formate-lyase and pyruvate-formate-lyase-activating enzyme !1deduced from the DNA nucleotide sequences. !$#cross-references MUID:89030680; PMID:3053170 !$#accession S01789 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-246 ##label ROE !'##cross-references EMBL:X08035; NID:g42369; PIDN:CAA30829.1; !1PID:g42371 !'##experimental_source strain K-12 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64829 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-246 ##label BLAT !'##cross-references GB:AE000192; GB:U00096; NID:g1787125; !1PIDN:AAC73988.1; PID:g1787130; UWGP:b0902 !'##experimental_source strain K-12, substrain MG1655 COMMENT This enzyme specifically activates formate !1C-acetyltransferase 1 (pyruvate formate-lyase I, see !1PIR:S01788) to generate the glycyl free radical active site !1of that enzyme. GENETICS !$#gene pflA; act !$#map_position 20.5 FUNCTION !$#description catalyzes the reaction of S-adenosyl-L-methionine and !1dihydroflavodoxin to produce 5'-deoxyadenosinyl radical, !1L-methionine, and flavodoxin; subsequently !15'-deoxyadenosinyl radical reacts with inactive [pyruvate !1formate-lyase]-glycine to form active [pyruvate !1formate-lyase]-glycyl radical and 5'-deoxyadenosine !$#pathway anaerobic glucose metabolism CLASSIFICATION #superfamily pyruvate formate-lyase activating enzyme, lyase !11-specific KEYWORDS iron; metalloprotein; oxidoreductase FEATURE !$2-246 #product pyruvate formate-lyase activating enzyme !8#status experimental #label MAT\ !$30,34,37 #binding_site iron (Cys) #status predicted SUMMARY #length 246 #molecular-weight 28204 #checksum 7214 SEQUENCE /// ENTRY E64052 #type complete TITLE formate acetyltransferase activating enzyme (EC 1.97.1.4), lyase 1-specific - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES formate C-acetyltransferase 1-activating enzyme; pyruvate formate-lyase I activase ORGANISM #formal_name Haemophilus influenzae DATE 15-Jan-1999 #sequence_revision 15-Jan-1999 #text_change 24-Aug-2001 ACCESSIONS E64052 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession E64052 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-246 ##label TIGR !'##cross-references GB:U32703; GB:L42023; NID:g1573133; !1PIDN:AAC21848.1; PID:g1573135; TIGR:HI0179 GENETICS !$#gene pflA; act FUNCTION !$#description catalyzes the reaction of S-adenosyl-L-methionine and !1dihydroflavodoxin to produce 5'-deoxyadenosinyl radical, !1L-methionine, and flavodoxin; subsequently !15'-deoxyadenosinyl radical reacts with inactive [pyruvate !1formate-lyase]-glycine to form active [pyruvate !1formate-lyase]-glycyl radical and 5'-deoxyadenosine CLASSIFICATION #superfamily pyruvate formate-lyase activating enzyme, lyase !11-specific KEYWORDS iron; metalloprotein; oxidoreductase FEATURE !$2-246 #product pyruvate formate-lyase activating enzyme !8#status experimental #label MAT\ !$30,34,37 #binding_site iron (Cys) #status predicted SUMMARY #length 246 #molecular-weight 28235 #checksum 8382 SEQUENCE /// ENTRY JC6011 #type complete TITLE formate acetyltransferase activating enzyme (EC 1.97.1.4), lyase 1-specific - Clostridium pasteurianum ALTERNATE_NAMES Act protein; formate C-acetyltransferase 1-activating enzyme; pyruvate formate-lyase I activase ORGANISM #formal_name Clostridium pasteurianum DATE 15-Jan-1999 #sequence_revision 15-Jan-1999 #text_change 24-Aug-2001 ACCESSIONS JC6011 REFERENCE JC6010 !$#authors Weidner, G.; Sawers, G. !$#journal J. Bacteriol. (1996) 178:2440-2444 !$#title Molecular characterization of the genes encoding pyruvate !1formate-lyase and its activating enzyme of Clostridium !1pasteurianum. !$#cross-references MUID:96218720; PMID:8636053 !$#accession JC6011 !'##molecule_type DNA !'##residues 1-238 ##label WEI !'##cross-references EMBL:X93463; NID:g1072360; PIDN:CAA63749.1; !1PID:g1072362 GENETICS !$#gene act FUNCTION !$#description catalyzes the reaction of S-adenosyl-L-methionine and !1dihydroflavodoxin to produce 5'-deoxyadenosinyl radical, !1L-methionine, and flavodoxin; subsequently !15'-deoxyadenosinyl radical reacts with inactive [pyruvate !1formate-lyase]-glycine to form active [pyruvate !1formate-lyase]-glycyl radical and 5'-deoxyadenosine CLASSIFICATION #superfamily pyruvate formate-lyase activating enzyme, lyase !11-specific KEYWORDS iron; metalloprotein; oxidoreductase FEATURE !$29,33,36 #binding_site iron (Cys) #status predicted SUMMARY #length 238 #molecular-weight 27147 #checksum 4044 SEQUENCE /// ENTRY B64453 #type complete TITLE probable formate acetyltransferase activating enzyme (EC 1.97.1.4) - Methanococcus jannaschii ALTERNATE_NAMES formate C-acetyltransferase activating enzyme; pyruvate formate-lyase activase ORGANISM #formal_name Methanococcus jannaschii DATE 15-Jan-1999 #sequence_revision 15-Jan-1999 #text_change 24-Aug-2001 ACCESSIONS B64453 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession B64453 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-240 ##label BUL !'##cross-references GB:U67563; GB:L77117; NID:g2826379; !1PIDN:AAB99230.1; PID:g1591858; TIGR:MJ1227 GENETICS !$#map_position FOR1170387-1171109 !$#start_codon GTG CLASSIFICATION #superfamily Methanococcus probable pyruvate formate-lyase !1activating enzyme KEYWORDS iron; metalloprotein; oxidoreductase FEATURE !$29,33,36 #binding_site iron (Cys) #status predicted SUMMARY #length 240 #molecular-weight 27682 #checksum 2445 SEQUENCE /// ENTRY F69078 #type complete TITLE probable formate acetyltransferase activating enzyme (EC 1.97.1.4) - Methanobacterium thermoautotrophicum (strain Delta H) ALTERNATE_NAMES formate C-acetyltransferase activating enzyme; pyruvate formate-lyase activase ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 15-Jan-1999 #sequence_revision 15-Jan-1999 #text_change 24-Aug-2001 ACCESSIONS F69078 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession F69078 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-233 ##label MTH !'##cross-references GB:AE000918; GB:AE000666; NID:g2622699; !1PIDN:AAB86059.1; PID:g2622709 !'##experimental_source strain Delta H GENETICS !$#gene MTH1586 !$#start_codon GTG CLASSIFICATION #superfamily Methanococcus probable pyruvate formate-lyase !1activating enzyme KEYWORDS iron; metalloprotein; oxidoreductase FEATURE !$29,33,36 #binding_site iron (Cys) #status predicted SUMMARY #length 233 #molecular-weight 26012 #checksum 3053 SEQUENCE /// ENTRY H64819 #type complete TITLE formate acetyltransferase activating enzyme (EC 1.97.1.4) 3 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS H64819 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64819 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-308 ##label BLAT !'##cross-references GB:AE000184; GB:U00096; NID:g1787036; !1PIDN:AAC73911.1; PID:g1787045; UWGP:b0824 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ybiY FUNCTION !$#description activation of pyruvate formate-lyase under anaerobic !1conditions by generation of an organic free radical !$#pathway anaerobic glucose metabolism !$#note iron dependent CLASSIFICATION #superfamily probable pyruvate formate-lyase 2 activating !1enzyme; ferredoxin 2[4Fe-4S] homology KEYWORDS iron; metalloprotein; oxidoreductase FEATURE !$34,38,41 #binding_site iron (Cys) #status predicted SUMMARY #length 308 #molecular-weight 34139 #checksum 2004 SEQUENCE /// ENTRY C65202 #type complete TITLE probable formate acetyltransferase activating enzyme (EC 1.97.1.4), lyase 2-specific - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS C65202 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65202 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-292 ##label BLAT !'##cross-references GB:AE000469; GB:U00096; NID:g1790385; !1PIDN:AAC76934.1; PID:g1790389; UWGP:b3952 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene pflC CLASSIFICATION #superfamily probable pyruvate formate-lyase 2 activating !1enzyme; ferredoxin 2[4Fe-4S] homology KEYWORDS oxidoreductase SUMMARY #length 292 #molecular-weight 32429 #checksum 4984 SEQUENCE /// ENTRY A69431 #type complete TITLE formate acetyltransferase activating enzyme (EC 1.97.1.4) pflC homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 24-Aug-2001 ACCESSIONS A69431 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession A69431 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-302 ##label KLE !'##cross-references GB:AE001003; GB:AE000782; NID:g2689326; !1PIDN:AAB89799.1; PID:g2649121; TIGR:AF1450 CLASSIFICATION #superfamily probable pyruvate formate-lyase 2 activating !1enzyme; ferredoxin 2[4Fe-4S] homology KEYWORDS oxidoreductase SUMMARY #length 302 #molecular-weight 34114 #checksum 8182 SEQUENCE /// ENTRY D69144 #type complete TITLE formate acetyltransferase activating enzyme (EC 1.97.1.4) - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 24-Aug-2001 ACCESSIONS D69144 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession D69144 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-288 ##label MTH !'##cross-references GB:AE000819; GB:AE000666; NID:g2621396; !1PIDN:AAB84851.1; PID:g2621402 !'##experimental_source strain Delta H GENETICS !$#gene MTH345 !$#start_codon GTG CLASSIFICATION #superfamily probable pyruvate formate-lyase 2 activating !1enzyme; ferredoxin 2[4Fe-4S] homology KEYWORDS oxidoreductase SUMMARY #length 288 #molecular-weight 32296 #checksum 2379 SEQUENCE /// ENTRY S56603 #type complete TITLE probable formate acetyltransferase activating enzyme (EC 1.97.1.4) - Escherichia coli (strain K-12) ALTERNATE_NAMES hypothetical protein f287 ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS S56603; B65253 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56603 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-287 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97275.1; !1PID:g537219 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65253 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-287 ##label BLAT !'##cross-references GB:AE000508; GB:U00096; NID:g2367382; !1PIDN:AAC77332.1; PID:g1790839; UWGP:b4379 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yjjW CLASSIFICATION #superfamily probable pyruvate formate-lyase 2 activating !1enzyme; ferredoxin 2[4Fe-4S] homology KEYWORDS iron; metalloprotein; oxidoreductase FEATURE !$40-93 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$31,35,38 #binding_site iron (Cys) #status predicted SUMMARY #length 287 #molecular-weight 31490 #checksum 5827 SEQUENCE /// ENTRY B64154 #type complete TITLE probable radical-forming protein HI0520 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 15-Jan-1999 #sequence_revision 15-Jan-1999 #text_change 11-Jun-1999 ACCESSIONS B64154 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession B64154 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-262 ##label TIGR !'##cross-references GB:U32734; GB:L42023; NID:g1573498; !1PIDN:AAC22178.1; PID:g1573503; TIGR:HI0520 !'##note best homolog was a hypothetical protein from Escherichia coli CLASSIFICATION #superfamily probable radical-forming protein HI0520 KEYWORDS iron; metalloprotein FEATURE !$34,38,41 #binding_site iron (Cys) #status predicted SUMMARY #length 262 #molecular-weight 29496 #checksum 9147 SEQUENCE /// ENTRY E64302 #type complete TITLE probable radical-forming protein MJ0021 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 15-Jan-1999 #sequence_revision 15-Jan-1999 #text_change 03-Mar-2000 ACCESSIONS E64302 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession E64302 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-375 ##label BUL !'##cross-references GB:U67461; GB:L77117; NID:g1590827; !1PIDN:AAB98003.1; PID:g1498780; TIGR:MJ0021 GENETICS !$#gene MJ0021 !$#map_position FOR22762-23889 CLASSIFICATION #superfamily probable radical-forming protein MJ0021 KEYWORDS iron; metalloprotein FEATURE !$38,42,45 #binding_site iron (Cys) #status predicted SUMMARY #length 375 #molecular-weight 43446 #checksum 4797 SEQUENCE /// ENTRY F71058 #type complete TITLE probable radical-forming protein PH1164 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 15-Jan-1999 #sequence_revision 15-Jan-1999 #text_change 16-Jun-2000 ACCESSIONS F71058 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession F71058 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-371 ##label KAW !'##cross-references GB:AP000005; NID:g3236132; PIDN:BAA30264.1; !1PID:g3257581 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1164 CLASSIFICATION #superfamily probable radical-forming protein MJ0021 KEYWORDS iron; metalloprotein FEATURE !$46,50,53 #binding_site iron (Cys) #status predicted SUMMARY #length 371 #molecular-weight 43006 #checksum 5661 SEQUENCE /// ENTRY S75404 #type complete TITLE probable radical-forming protein c04038 - Sulfolobus solfataricus ORGANISM #formal_name Sulfolobus solfataricus DATE 15-Jan-1999 #sequence_revision 15-Jan-1999 #text_change 16-Jun-2000 ACCESSIONS S75404 REFERENCE S73076 !$#authors Sensen, C.W.; Klenk, H.P.; Singh, R.K.; Allard, G.; Chan, !1C.C.Y.; Liu, Q.Y.; Penny, S.L.; Young, F.; Schenk, M.E.; !1Gaasterland, T.; Doolittle, W.F.; Ragan, M.A.; Charlebois, !1R.L. !$#journal Mol. Microbiol. (1996) 22:175-191 !$#title Organizational characteristics and information content of an !1archaeal genome: 156 kb of sequence from Sulfolobus !1solfataricus P2. !$#cross-references MUID:97055432; PMID:8899719 !$#accession S75404 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-350 ##label SEN !'##cross-references EMBL:Y08257; NID:g1707772; PIDN:CAA69567.1; !1PID:g1707810 !'##experimental_source strain P2 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1September 1996 GENETICS !$#gene c04038 !$#start_codon TTG CLASSIFICATION #superfamily probable radical-forming protein MJ0021 KEYWORDS iron; metalloprotein FEATURE !$37,41,44 #binding_site iron (Cys) #status predicted SUMMARY #length 350 #molecular-weight 39888 #checksum 3814 SEQUENCE /// ENTRY H69401 #type complete TITLE probable radical-forming protein AF1217 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 15-Jan-1999 #sequence_revision 15-Jan-1999 #text_change 03-Mar-2000 ACCESSIONS H69401 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession H69401 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-341 ##label KLE !'##cross-references GB:AE001020; GB:AE000782; NID:g2689343; !1PIDN:AAB90028.1; PID:g2649366; TIGR:AF1217 GENETICS !$#gene AF1217 CLASSIFICATION #superfamily probable radical-forming protein MJ0021 KEYWORDS iron; metalloprotein FEATURE !$44,48,51 #binding_site iron (Cys) #status predicted SUMMARY #length 341 #molecular-weight 39547 #checksum 6223 SEQUENCE /// ENTRY S69049 #type complete TITLE iron-sulfur cofactor synthesis protein nifU homolog YPL135w [similarity] - yeast (Saccharomyces cerevisiae) ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S69049 REFERENCE S69040 !$#authors Hall, J.; DePaulo, T.; Ahmed, A.; Bussey, H.; Fortin, N.; !1Friesen, J.D.; Storms, R.K.; Vo, D.H.; Wang, Y.; Winnett, E. !$#submission submitted to the EMBL Data Library, December 1995 !$#description The sequence of Saccharomyces cerevisiae chromosome XVI left !1arm. !$#accession S69049 !'##molecule_type DNA !'##residues 1-165 ##label HAL !'##cross-references EMBL:U43703; NID:g1244769; PIDN:AAB68224.1; !1PID:g1244779; GSPDB:GN00016; MIPS:YPL135w GENETICS !$#gene SGD:ISU1; MIPS:YPL135w !'##cross-references SGD:S0006056 !$#map_position 16L CLASSIFICATION #superfamily Yeast nitrogen fixation protein; nitrogen !1fixation protein homology KEYWORDS metalloprotein FEATURE !$68-121 #domain nitrogen fixation protein homology #label !8NFH\ !$69,96 #binding_site iron-sulfur clusters (Cys) (covalent) !8#status predicted SUMMARY #length 165 #molecular-weight 17895 #checksum 5557 SEQUENCE /// ENTRY E70019 #type complete TITLE iron-sulfur cofactor synthesis protein nifU homolog yurV [similarity] - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 08-Dec-2000 ACCESSIONS E70019 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E70019 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-147 ##label KUN !'##cross-references GB:Z99120; GB:AL009126; NID:g2635613; !1PIDN:CAB15257.1; PID:g2635764 !'##experimental_source strain 168 GENETICS !$#gene yurV CLASSIFICATION #superfamily Yeast nitrogen fixation protein; nitrogen !1fixation protein homology KEYWORDS metalloprotein FEATURE !$40-91 #domain nitrogen fixation protein homology #label !8NFH\ !$41,66 #binding_site iron-sulfur clusters (Cys) (covalent) !8#status predicted SUMMARY #length 147 #molecular-weight 16166 #checksum 376 SEQUENCE /// ENTRY S72754 #type complete TITLE iron-sulfur cofactor synthesis protein nifU homolog nifU7 [similarity] - Mycobacterium leprae ALTERNATE_NAMES protein B1496_C1_157; protein MLCL536.24c ORGANISM #formal_name Mycobacterium leprae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 23-Mar-2001 ACCESSIONS S72754; T11010 REFERENCE S72695 !$#authors Smith, D.R.; Robison, K. !$#submission submitted to the EMBL Data Library, November 1993 !$#description Mycobacterium leprae cosmid B1496. !$#accession S72754 !'##molecule_type DNA !'##residues 1-165 ##label SMI !'##cross-references EMBL:U00013; NID:g466868; PIDN:AAA17120.1; !1PID:g466875 REFERENCE Z16918 !$#authors Parkhill, J.; Barrell, B.G.; Rajandream, M.A. !$#submission submitted to the EMBL Data Library, September 1997 !$#accession T11010 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-165 ##label PAR !'##cross-references EMBL:Z99125; PIDN:CAB16167.1 GENETICS !$#gene MLCL536.24c CLASSIFICATION #superfamily Yeast nitrogen fixation protein; nitrogen !1fixation protein homology KEYWORDS metalloprotein FEATURE !$39-92 #domain nitrogen fixation protein homology #label !8NFH\ !$40,67 #binding_site iron-sulfur clusters (Cys) (covalent) !8#status predicted SUMMARY #length 165 #molecular-weight 17909 #checksum 117 SEQUENCE /// ENTRY S02506 #type complete TITLE nitrogen fixation protein nifU homolog - Klebsiella pneumoniae ORGANISM #formal_name Klebsiella pneumoniae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 23-Mar-2001 ACCESSIONS S02506; S01707; S34846; S37295 REFERENCE S01836 !$#authors Arnold, W.; Rump, A.; Klipp, W.; Priefer, U.B.; Puehler, A. !$#journal J. Mol. Biol. (1988) 203:715-738 !$#title Nucleotide sequence of a 24,206-base-pair DNA fragment !1carrying the entire nitrogen fixation gene cluster of !1Klebsiella pneumoniae. !$#cross-references MUID:89094839; PMID:3062178 !$#accession S02506 !'##molecule_type DNA !'##residues 1-274 ##label ARN !'##cross-references EMBL:X13303; NID:g43820; PIDN:CAA31674.1; !1PID:g43830 REFERENCE S01702 !$#authors Beynon, J.; Cannon, M.; Buchanan-Wollaston, V.; Ally, A.; !1Setterquist, R.; Dean, D.; Cannon, F. !$#journal Nucleic Acids Res. (1988) 16:9860 !$#title The nucleotide sequence of the nifT, nifY, nifX and nifW !1genes of K. pneumoniae. !$#cross-references MUID:89041575; PMID:3054814 !$#accession S01707 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-274 ##label BEY !'##cross-references EMBL:X12600; NID:g43877; PIDN:CAA31117.1; !1PID:g43879 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1988 REFERENCE S29756 !$#authors Beynon, J.; Ally, A.; Cannon, M.; Cannon, F.; Jacobson, M.; !1Cash, V.; Dean, D. !$#journal J. Bacteriol. (1987) 169:4024-4029 !$#title Comparative organization of nitrogen fixation-specific genes !1from Azotobacter vinelandii and Klebsiella pneumoniae: DNA !1sequence of the nifUSV genes. !$#cross-references MUID:87307977; PMID:3040672 !$#accession S34846 !'##status preliminary !'##molecule_type DNA !'##residues 1-274 ##label BE2 !'##cross-references EMBL:M17350 REFERENCE S34843 !$#authors Beynon, J.; Ally, A.; Cannon, M.; Cannon, F.; Jacobson, M.; !1Cash, V.; Dean, D. !$#submission submitted to the EMBL Data Library, October 1987 !$#description Comparative organization of nitrogen fixation-specific genes !1from Azotobacter vinelandii and Klebsiella pneumoniae: DNA !1sequence of the nifUSV genes. !$#accession S37295 !'##status preliminary !'##molecule_type DNA !'##residues 1-4,'C',6-274 ##label BEW !'##cross-references EMBL:M17350; NID:g149342; PIDN:AAA25155.1; !1PID:g149343 GENETICS !$#gene nifU CLASSIFICATION #superfamily Helicobacter nitrogen fixation protein; !1nitrogen fixation protein homology FEATURE !$34-87 #domain nitrogen fixation protein homology #label NFH SUMMARY #length 274 #molecular-weight 29495 #checksum 7497 SEQUENCE /// ENTRY S29756 #type complete TITLE nitrogen fixation protein nifU homolog - Azotobacter vinelandii ORGANISM #formal_name Azotobacter vinelandii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S29756; S34843 REFERENCE S29756 !$#authors Beynon, J.; Ally, A.; Cannon, M.; Cannon, F.; Jacobson, M.; !1Cash, V.; Dean, D. !$#journal J. Bacteriol. (1987) 169:4024-4029 !$#title Comparative organization of nitrogen fixation-specific genes !1from Azotobacter vinelandii and Klebsiella pneumoniae: DNA !1sequence of the nifUSV genes. !$#cross-references MUID:87307977; PMID:3040672 !$#accession S29756 !'##molecule_type DNA !'##residues 1-312 ##label BEY1 !'##cross-references EMBL:M17349 REFERENCE S34843 !$#authors Beynon, J.; Ally, A.; Cannon, M.; Cannon, F.; Jacobson, M.; !1Cash, V.; Dean, D. !$#submission submitted to the EMBL Data Library, October 1987 !$#description Comparative organization of nitrogen fixation-specific genes !1from Azotobacter vinelandii and Klebsiella pneumoniae: DNA !1sequence of the nifUSV genes. !$#accession S34843 !'##molecule_type DNA !'##residues 1-91,'M',93-184,'Q',186-312 ##label BEY2 !'##cross-references EMBL:M17349; NID:g142395; PIDN:AAA22167.1; !1PID:g142396 GENETICS !$#gene nifU CLASSIFICATION #superfamily Helicobacter nitrogen fixation protein; !1nitrogen fixation protein homology KEYWORDS nitrogen fixation FEATURE !$34-87 #domain nitrogen fixation protein homology #label NFH SUMMARY #length 312 #molecular-weight 33272 #checksum 7106 SEQUENCE /// ENTRY A43706 #type complete TITLE nitrogen fixation protein nifU homolog - Azotobacter chroococcum ORGANISM #formal_name Azotobacter chroococcum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A43706 REFERENCE A43706 !$#authors Evans, D.J.; Jones, R.; Woodley, P.R.; Wilborn, J.R.; !1Robson, R.L. !$#journal J. Bacteriol. (1991) 173:5457-5469 !$#title Nucleotide sequence and genetic analysis of the Azotobacter !1chroococcum nifUSVWZM gene cluster, including a new gene !1(nifP) which encodes a serine acetyltransferase. !$#cross-references MUID:91358323; PMID:1885524 !$#accession A43706 !'##status preliminary !'##molecule_type DNA !'##residues 1-309 ##label EVA !'##cross-references EMBL:M60090; NID:g142386; PIDN:AAA22159.1; !1PID:g142387 CLASSIFICATION #superfamily Helicobacter nitrogen fixation protein; !1nitrogen fixation protein homology FEATURE !$34-87 #domain nitrogen fixation protein homology #label NFH SUMMARY #length 309 #molecular-weight 33933 #checksum 363 SEQUENCE /// ENTRY D34443 #type complete TITLE nitrogen fixation protein nifU - Anabaena sp. ORGANISM #formal_name Anabaena sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS D34443 REFERENCE A34443 !$#authors Mulligan, M.E.; Haselkorn, R. !$#journal J. Biol. Chem. (1989) 264:19200-19207 !$#title Nitrogen fixation (nif) genes of the cyanobacterium Anabaena !1species strain PCC 7120. The nifB-fdxN-nifS-nifU operon. !$#cross-references MUID:90037054; PMID:2553733 !$#accession D34443 !'##status preliminary !'##molecule_type DNA !'##residues 1-300 ##label MUL !'##cross-references GB:J05111; NID:g142034; PIDN:AAA22007.1; !1PID:g142038; GB:J01538; GB:J05152; GB:M21840; GB:X05593; !1GB:X05595 CLASSIFICATION #superfamily Helicobacter nitrogen fixation protein; !1nitrogen fixation protein homology FEATURE !$40-93 #domain nitrogen fixation protein homology #label NFH SUMMARY #length 300 #molecular-weight 32132 #checksum 3491 SEQUENCE /// ENTRY E64547 #type complete TITLE nitrogen fixation protein nifU homolog - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS E64547 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession E64547 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-326 ##label TOM !'##cross-references GB:AE000542; GB:AE000511; NID:g2313310; !1PIDN:AAD07289.1; PID:g2313312; TIGR:HP0221 CLASSIFICATION #superfamily Helicobacter nitrogen fixation protein; !1nitrogen fixation protein homology FEATURE !$53-106 #domain nitrogen fixation protein homology #label NFH SUMMARY #length 326 #molecular-weight 36349 #checksum 2027 SEQUENCE /// ENTRY A46621 #type complete TITLE corrinoid/iron-sulfur protein large chain - Clostridium thermaceticum ALTERNATE_NAMES C/Fe-SP large chain AcsC ORGANISM #formal_name Clostridium thermaceticum DATE 21-Sep-1993 #sequence_revision 04-Oct-1996 #text_change 18-Sep-1998 ACCESSIONS A46621 REFERENCE A46621 !$#authors Lu, W.P.; Schiau, I.; Cunningham, J.R.; Ragsdale, S.W. !$#journal J. Biol. Chem. (1993) 268:5605-5614 !$#title Sequence and expression of the gene encoding the corrinoid/ !1iron-sulfur protein from Clostridium thermoaceticum and !1reconstitution of the recombinant protein to full activity. !$#cross-references MUID:93194857; PMID:8449924 !$#accession A46621 !'##molecule_type DNA; protein !'##residues 1-446 ##label LU1 !'##note sequence extracted from NCBI backbone (NCBIN:127877, !1NCBIP:127878) GENETICS !$#gene acsC CLASSIFICATION #superfamily corrinoid/iron-sulfur protein large chain KEYWORDS 4Fe-4S; carbon dioxide fixation; electron transfer; !1heterodimer; iron-sulfur protein; metalloprotein FEATURE !$2-446 #product corrinoid/iron-sulfur protein large chain !8#status experimental #label MAT\ !$17,20,25,42 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 446 #molecular-weight 48153 #checksum 3949 SEQUENCE /// ENTRY H64313 #type complete TITLE corrinoid/iron-sulfur protein large chain - Methanococcus jannaschii ALTERNATE_NAMES C/Fe-SP large chain ORGANISM #formal_name Methanococcus jannaschii DATE 13-Sep-1996 #sequence_revision 04-Oct-1996 #text_change 11-Jun-1999 ACCESSIONS H64313 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession H64313 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-488 ##label BUL !'##cross-references GB:U67468; GB:L77117; NID:g1590882; !1PIDN:AAB98093.1; PID:g1590888; TIGR:MJ0112 GENETICS !$#map_position REV110157-108691 CLASSIFICATION #superfamily corrinoid/iron-sulfur protein large chain KEYWORDS 4Fe-4S; carbon dioxide fixation; electron transfer; !1heterodimer; iron-sulfur protein; metalloprotein FEATURE !$19,22,27,44 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 488 #molecular-weight 55026 #checksum 1631 SEQUENCE /// ENTRY B46621 #type complete TITLE corrinoid/iron-sulfur protein small chain - Clostridium thermaceticum ALTERNATE_NAMES C/Fe-SP small chain AcsD ORGANISM #formal_name Clostridium thermaceticum DATE 21-Sep-1993 #sequence_revision 04-Oct-1996 #text_change 04-Oct-1996 ACCESSIONS B46621 REFERENCE A46621 !$#authors Lu, W.P.; Schiau, I.; Cunningham, J.R.; Ragsdale, S.W. !$#journal J. Biol. Chem. (1993) 268:5605-5614 !$#title Sequence and expression of the gene encoding the corrinoid/ !1iron-sulfur protein from Clostridium thermoaceticum and !1reconstitution of the recombinant protein to full activity. !$#cross-references MUID:93194857; PMID:8449924 !$#accession B46621 !'##molecule_type DNA !'##residues 1-323 ##label LU1 !'##note sequence extracted from NCBI backbone (NCBIN:127879, !1NCBIP:127880) !'##note parts of this sequence, including the amino end of the mature !1protein; were confirmed by peptide sequencing GENETICS !$#gene acsD CLASSIFICATION #superfamily corrinoid/iron-sulfur protein small chain KEYWORDS carbon dioxide fixation; cobalt; heterodimer; iron-sulfur !1protein FEATURE !$2-323 #product corrinoid/iron-sulfur protein small chain !8#status experimental #label MAT SUMMARY #length 323 #molecular-weight 35070 #checksum 8262 SEQUENCE /// ENTRY A64314 #type complete TITLE corrinoid/iron-sulfur protein small chain - Methanococcus jannaschii ALTERNATE_NAMES C/Fe-SP small chain ORGANISM #formal_name Methanococcus jannaschii DATE 13-Sep-1996 #sequence_revision 04-Oct-1996 #text_change 11-Jun-1999 ACCESSIONS A64314 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession A64314 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-405 ##label BUL !'##cross-references GB:U67468; GB:L77117; NID:g1590882; !1PIDN:AAB98094.1; PID:g1590889; TIGR:MJ0113 GENETICS !$#map_position REV111545-110328 CLASSIFICATION #superfamily corrinoid/iron-sulfur protein small chain KEYWORDS carbon dioxide fixation; heterodimer SUMMARY #length 405 #molecular-weight 45343 #checksum 8614 SEQUENCE /// ENTRY B65036 #type complete TITLE probable glycyl radical protein yfiD - Escherichia coli (strain K-12) ALTERNATE_NAMES hypothetical 14.3kD protein srmB-ung intergenic region ORGANISM #formal_name Escherichia coli DATE 06-Nov-1998 #sequence_revision 06-Nov-1998 #text_change 01-Mar-2002 ACCESSIONS B65036 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65036 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-127 ##label BLAT !'##cross-references GB:AE000344; GB:U00096; NID:g1788927; !1PIDN:AAC75632.1; PID:g1788933; UWGP:b2579 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yfiD CLASSIFICATION #superfamily probable glycyl radical protein yfiD; glycyl !1radical homology FEATURE !$68-127 #domain glycyl radical homology #label GFR\ !$102 #active_site Gly (stable glycyl radical) #status !8predicted SUMMARY #length 127 #molecular-weight 14284 #checksum 147 SEQUENCE /// ENTRY S22666 #type complete TITLE probable glycyl radical protein - Serratia liquefaciens ALTERNATE_NAMES hypothetical protein phlA 5'-region ORGANISM #formal_name Serratia liquefaciens DATE 06-Nov-1998 #sequence_revision 06-Nov-1998 #text_change 11-Jun-1999 ACCESSIONS S22666; A31390; S32922 REFERENCE S22666 !$#authors Givskov, M.; Molin, S. !$#journal Mol. Microbiol. (1992) 6:1363-1374 !$#title Expression of extracellular phospholipase from Serratia !1liquefaciens is growth-phase-dependent, catabolite-repressed !1and regulated by anaerobiosis. !$#cross-references MUID:92349964; PMID:1640837 !$#accession S22666 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-127 ##label GIV1 !'##cross-references GB:X66505; GB:S42593; NID:g395373; PIDN:CAA47136.1; !1PID:g395374 REFERENCE S32922 !$#authors Givskov, M.; Molin, S. !$#journal Mol. Microbiol. (1993) 8:229-242 !$#title Secretion of Serratia liquefaciens phospholipase from !1Escherichia coli. !$#cross-references MUID:93302499; PMID:8316077 !$#contents annotation; expression in Escherichia coli REFERENCE A31390 !$#authors Givskov, M.; Olsen, L.; Molin, S. !$#journal J. Bacteriol. (1988) 170:5855-5862 !$#title Cloning and expression in Escherichia coli of the gene for !1extracellular phospholipase A1 from Serratia liquefaciens. !$#cross-references MUID:89053916; PMID:3056919 !$#accession A31390 !'##molecule_type DNA !'##residues 21-28,'VVRM','RQ',36-127 ##label GIV2 !'##cross-references GB:M23640; NID:g152820 !'##note this ORF is not annotated in GenBank entry SMAEXPH, release !1106.0 CLASSIFICATION #superfamily probable glycyl radical protein yfiD; glycyl !1radical homology FEATURE !$68-127 #domain glycyl radical homology #label GFR\ !$102 #active_site Gly (stable glycyl radical) #status !8predicted SUMMARY #length 127 #molecular-weight 14375 #checksum 1325 SEQUENCE /// ENTRY C64140 #type complete TITLE probable glycyl radical protein HI0017 - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES hypothetical protein HI0017 ORGANISM #formal_name Haemophilus influenzae DATE 06-Nov-1998 #sequence_revision 06-Nov-1998 #text_change 11-Jun-1999 ACCESSIONS C64140 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession C64140 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-127 ##label TIGR !'##cross-references GB:U32687; GB:L42023; NID:g1572955; !1PIDN:AAC21695.1; PID:g1572961; TIGR:HI0017 CLASSIFICATION #superfamily probable glycyl radical protein yfiD; glycyl !1radical homology FEATURE !$68-127 #domain glycyl radical homology #label GFR\ !$102 #active_site Gly (stable glycyl radical) #status !8predicted SUMMARY #length 127 #molecular-weight 14291 #checksum 85 SEQUENCE /// ENTRY S01788 #type complete TITLE formate C-acetyltransferase (EC 2.3.1.54) 1 - Escherichia coli (strain K-12) ALTERNATE_NAMES pyruvate formate-lyase I ORGANISM #formal_name Escherichia coli DATE 06-Nov-1998 #sequence_revision 06-Nov-1998 #text_change 01-Mar-2002 ACCESSIONS S01788; B32305; F64829 REFERENCE S01788 !$#authors Roedel, W.; Plaga, W.; Frank, R.; Knappe, J. !$#journal Eur. J. Biochem. (1988) 177:153-158 !$#title Primary structures of Escherichia coli pyruvate !1formate-lyase and pyruvate-formate-lyase-activating enzyme !1deduced from the DNA nucleotide sequences. !$#cross-references MUID:89030680; PMID:3053170 !$#accession S01788 !'##molecule_type DNA; protein !'##residues 1-760 ##label ROE !'##cross-references EMBL:X08035; NID:g42369; PIDN:CAA30828.1; !1PID:g42370 !'##experimental_source strain K-12 !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing REFERENCE A32305 !$#authors Sawers, G.; Boeck, A. !$#journal J. Bacteriol. (1989) 171:2485-2498 !$#title Novel transcriptional control of the pyruvate formate-lyase !1gene: upstream regulatory sequences and multiple promoters !1regulate anaerobic expression. !$#cross-references MUID:89213931; PMID:2651404 !$#accession B32305 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-13 ##label SAW !'##cross-references GB:M26413; NID:g147153; PIDN:AAA20391.1; !1PID:g147155 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64829 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-760 ##label BLAT !'##cross-references GB:AE000192; GB:U00096; NID:g1787125; !1PIDN:AAC73989.1; PID:g1787131; UWGP:b0903 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A46565 !$#authors Wagner, A.F.V.; Frey, M.; Neugebauer, F.A.; Schaefer, W.; !1Knappe, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:996-1000 !$#title The free radical in pyruvate formate-lyase is located on !1glycine-734. !$#cross-references MUID:92141244; PMID:1310545 !$#contents annotation; active site COMMENT This enzyme must be activated by the lyase 1-specific !1pyruvate formate-lyase activating enzyme (see PIR:S01789) to !1generate the glycyl free radical active site. Oxygen !1destroys this active site and causes peptide cleavage. GENETICS !$#gene pflB; pfl !$#map_position 20.5 COMPLEX homodimer FUNCTION !$#description catalyzes the reversible conversion of acetyl-CoA and !1formate into pyruvate and CoA !$#pathway anaerobic glucose metabolism CLASSIFICATION #superfamily formate C-acetyltransferase 1; glycyl radical !1homology KEYWORDS acyltransferase; coenzyme A; homodimer; thiolester bond FEATURE !$2-760 #product formate C-acetyltransferase 1 #status !8experimental #label MAT\ !$701-760 #domain glycyl radical homology #label GFR\ !$419 #active_site Cys (cysteine thiyl radical !8intermediate) #status predicted\ !$420 #active_site Cys (S-acetylcysteine intermediate) !8#status experimental\ !$735 #active_site Gly (stable glycyl radical) #status !8experimental SUMMARY #length 760 #molecular-weight 85357 #checksum 8486 SEQUENCE /// ENTRY F64052 #type complete TITLE formate C-acetyltransferase (EC 2.3.1.54) - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-May-2000 ACCESSIONS F64052 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession F64052 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-772 ##label TIGR !'##cross-references GB:U32703; GB:L42023; NID:g1573133; !1PIDN:AAC21849.1; PID:g1573136; TIGR:HI0180 COMMENT This enzyme must be activated by the lyase-specific pyruvate !1formate-lyase activating enzyme (see PIR:E64052) to generate !1the glycyl free radical active site. Oxygen destroys this !1active site and causes peptide cleavage. FUNCTION !$#description catalyzes the reversible conversion of acetyl-CoA and !1formate into pyruvate and CoA !$#pathway anaerobic glucose metabolism CLASSIFICATION #superfamily formate C-acetyltransferase 1; glycyl radical !1homology KEYWORDS acyltransferase; coenzyme A; thiolester bond FEATURE !$713-772 #domain glycyl radical homology #label GFR\ !$421 #active_site Cys (cysteine thiyl radical !8intermediate) #status predicted\ !$422 #active_site Cys (S-acetylcysteine intermediate) !8#status predicted\ !$747 #active_site Gly (stable glycyl radical) #status !8predicted SUMMARY #length 772 #molecular-weight 86531 #checksum 4680 SEQUENCE /// ENTRY G65100 #type complete TITLE formate C-acetyltransferase (EC 2.3.1.54) 3 [similarity] - Escherichia coli (strain K-12) ALTERNATE_NAMES keto-acid formate lyase CONTAINS keto-acid formate acetyltransferase (EC 2.3.1.-) ORGANISM #formal_name Escherichia coli DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 01-Mar-2002 ACCESSIONS G65100 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65100 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-746 ##label BLAT !'##cross-references GB:AE000393; GB:U00096; NID:g1789499; !1PIDN:AAC76149.1; PID:g1789502; UWGP:b3114 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yhaS; tdcE FUNCTION PFL !$#description catalyzes the reversible conversion of acetyl-CoA and !1formate into pyruvate and CoA !$#pathway anaerobic glucose metabolism FUNCTION KFL !$#description catalyzes the reversible conversion of propanoyl-CoA and !1formate into 2-oxobutanoate and CoA !$#pathway threonine catabolism CLASSIFICATION #superfamily formate C-acetyltransferase 1; glycyl radical !1homology KEYWORDS acyltransferase; coenzyme A; thiolester bond; threonine !1catabolism FEATURE !$705-746 #domain glycyl radical homology #status atypical !8#label GFR\ !$423 #active_site Cys (cysteine thiyl radical !8intermediate) #status predicted\ !$424 #active_site Cys (S-acetylcysteine intermediate) !8#status predicted\ !$739 #active_site Gly (stable glycyl radical) #status !8predicted SUMMARY #length 746 #molecular-weight 83730 #checksum 4816 SEQUENCE /// ENTRY JC6010 #type complete TITLE formate C-acetyltransferase (EC 2.3.1.54) - Clostridium pasteurianum ALTERNATE_NAMES Pf1 protein; pyruvate formate-lyase ORGANISM #formal_name Clostridium pasteurianum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-May-2000 ACCESSIONS JC6010; PC6004 REFERENCE JC6010 !$#authors Weidner, G.; Sawers, G. !$#journal J. Bacteriol. (1996) 178:2440-2444 !$#title Molecular characterization of the genes encoding pyruvate !1formate-lyase and its activating enzyme of Clostridium !1pasteurianum. !$#cross-references MUID:96218720; PMID:8636053 !$#accession JC6010 !'##molecule_type DNA !'##residues 1-740 ##label WEI1 !'##cross-references EMBL:X93463; NID:g1072360; PIDN:CAA63748.1; !1PID:g1072361 !$#accession PC6004 !'##molecule_type protein !'##residues 1-740 ##label WEI2 COMMENT This enzyme must be activated by the lyase-specific pyruvate !1formate-lyase-activating enzyme (see PIR:JC6011) to generate !1the glycyl free radical active site. Oxygen destroys this !1active site and causes peptide cleavage. GENETICS !$#gene pfl !$#start_codon TTG COMPLEX homodimer FUNCTION !$#description catalyzes the reversible conversion of acetyl-CoA and !1formate into pyruvate and CoA !$#pathway anaerobic glucose metabolism CLASSIFICATION #superfamily formate C-acetyltransferase 1; glycyl radical !1homology KEYWORDS acyltransferase; coenzyme A; homodimer; lyase; thiolester !1bond FEATURE !$681-740 #domain glycyl radical homology #label GFR\ !$405 #active_site Cys (cysteine thiyl radical !8intermediate) #status predicted\ !$406 #active_site Cys (S-acetylcysteine intermediate) !8#status predicted\ !$715 #active_site Gly (stable glycyl radical) #status !8predicted SUMMARY #length 740 #molecular-weight 83216 #checksum 5473 SEQUENCE /// ENTRY B65202 #type complete TITLE formate C-acetyltransferase (EC 2.3.1.54) 2 - Escherichia coli (strain K-12) ALTERNATE_NAMES pyruvate formate-lyase II ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS B65202 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65202 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-765 ##label BLAT !'##cross-references GB:AE000469; GB:U00096; NID:g1790385; !1PIDN:AAC76933.1; PID:g1790388; UWGP:b3951 !'##experimental_source strain K-12, substrain MG1655 COMMENT This enzyme must be activated by the lyase 2-specific !1pyruvate formate-lyase activating enzyme (see PIR:C65202) to !1generate the glycyl free radical active site. Oxygen !1destroys this active site and causes peptide cleavage. GENETICS !$#gene pflD !$#map_position 89.3 FUNCTION !$#description catalyzes the reversible conversion of acetyl-CoA and !1formate into pyruvate and CoA !$#pathway anaerobic glucose metabolism CLASSIFICATION #superfamily formate C-acetyltransferase 2; glycyl radical !1homology KEYWORDS acyltransferase; coenzyme A; thiolester bond FEATURE !$2-765 #product formate C-acetyltransferase #status !8predicted #label MAT\ !$708-765 #domain glycyl radical homology #label GFR\ !$419 #active_site Cys (S-acetylcysteine intermediate) !8#status predicted\ !$741 #active_site Gly (stable glycyl radical) #status !8predicted SUMMARY #length 765 #molecular-weight 85959 #checksum 8442 SEQUENCE /// ENTRY H69430 #type complete TITLE probable formate C-acetyltransferase (EC 2.3.1.54) - Archaeoglobus fulgidus ALTERNATE_NAMES pyruvate formate-lyase 2 (pflD) homolog ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-May-2000 ACCESSIONS H69430 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession H69430 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-776 ##label KLE !'##cross-references GB:AE001003; GB:AE000782; NID:g2689326; !1PIDN:AAB89800.1; PID:g2649123; TIGR:AF1449 CLASSIFICATION #superfamily formate C-acetyltransferase 2; glycyl radical !1homology KEYWORDS acyltransferase; coenzyme A; thiolester bond FEATURE !$718-776 #domain glycyl radical homology #label GFR\ !$426 #active_site Cys (S-acetylcysteine intermediate) !8#status predicted\ !$752 #active_site Gly (stable glycyl radical) #status !8predicted SUMMARY #length 776 #molecular-weight 87166 #checksum 8699 SEQUENCE /// ENTRY G64819 #type complete TITLE probable formate C-acetyltransferase (EC 2.3.1.54) - Escherichia coli (strain K-12) ALTERNATE_NAMES pyruvate formate-lyase 3 ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS G64819 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64819 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-810 ##label BLAT !'##cross-references GB:AE000184; GB:U00096; NID:g1787036; !1PIDN:AAC73910.1; PID:g1787044; UWGP:b0823 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ybiW CLASSIFICATION #superfamily formate C-acetyltransferase 2; glycyl radical !1homology KEYWORDS acyltransferase; coenzyme A; thiolester bond FEATURE !$752-810 #domain glycyl radical homology #label GFR\ !$441 #active_site Cys (S-acetylcysteine intermediate) !8#status predicted\ !$786 #active_site Gly (stable glycyl radical) #status !8predicted SUMMARY #length 810 #molecular-weight 90125 #checksum 5710 SEQUENCE /// ENTRY XYECMH #type complete TITLE 5-methyltetrahydrofolate-homocysteine S-methyltransferase (EC 2.1.1.13) - Escherichia coli (strain K-12) ALTERNATE_NAMES methionine synthase; tetrahydropteroylglutamate methyltransferase ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 05-Dec-1997 #text_change 03-Jun-2002 ACCESSIONS B65209; JH0096; A32644; B54337; A54337; S06691 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65209 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1227 ##label BLAT !'##cross-references GB:AE000475; GB:U00096; NID:g1790448; !1PIDN:AAC76989.1; PID:g1790450; UWGP:b4019 !'##experimental_source strain K-12, substrain MG1655 REFERENCE JH0096 !$#authors Old, I.G.; Margarita, D.; Glass, R.E.; Saint-Girons, I. !$#journal Gene (1990) 87:15-21 !$#title Nucleotide sequence of the metH gene of Escherichia coli !1K-12 and comparison with that of Salmonella typhimurium LT2. !$#cross-references MUID:90236292; PMID:2185137 !$#accession JH0096 !'##molecule_type DNA !'##residues 1-112,'R',114-640,'T',642-1078,'HD',1081-1194,'TSARSG' !1##label OLD !'##cross-references GB:X16584; NID:g42031; PIDN:CAA34601.1; PID:g581135 !'##experimental_source strain K12 !'##note see reference A54337 for redefinition of the carboxyl end REFERENCE A32644 !$#authors Banerjee, R.V.; Johnston, N.L.; Sobeski, J.K.; Datta, P.; !1Matthews, R.G. !$#journal J. Biol. Chem. (1989) 264:13888-13895 !$#title Cloning and sequence analysis of the Escherichia coli metH !1gene encoding cobalamin-dependent methionine synthase and !1isolation of a tryptic fragment containing the !1cobalamin-binding domain. !$#cross-references MUID:89340482; PMID:2668277 !$#accession A32644 !'##molecule_type DNA !'##residues 1-112,'R',114-174,'E',176-759,'E',761-1036,'A',1038-1112, !1'AMRRTRTSATKS' ##label BAN !'##cross-references GB:J04975 !'##note this sequence contains an apparent frame shift after position !11112 !'##note see reference A54337 for redefinition of the carboxyl end REFERENCE A55243 !$#authors Drennan, C.L.; Huang, S.; Drummond, J.T.; Matthews, R.G.; !1Ludwig, M.L. !$#journal Science (1994) 266:1669-1674 !$#title How a protein binds B-12: a 3.0 angstrom X-ray structure of !1B-12-binding domains of methionine synthase. !$#cross-references MUID:95084154; PMID:7992050 !$#contents annotation; X-ray crystallography, 3.0 angstroms REFERENCE A54337 !$#authors Drummond, J.T.; Loo, R.R.O.; Matthews, R.G. !$#journal Biochemistry (1993) 32:9282-9289 !$#title Electrospray mass spectrometric analysis of the domains of a !1large enzyme: observation of the occupied cobalamin-binding !1domain and redefinition of the carboxyl terminus of !1methionine synthase. !$#cross-references MUID:93378978; PMID:8369296 !$#accession B54337 !'##molecule_type protein; DNA !'##residues 1165-1227 ##label DR2 !'##note this region was sequenced completely by Edman degradation; a !1portion was confirmed by DNA sequencing !$#accession A54337 !'##molecule_type protein !'##residues 901-1227 ##label DRU !'##note this sequence, including identification of the correct residues !1at positions 1037, 1079, and 1080, was deduced by a !1combination of electrospray mass spectrometry (in the !1context of previously reported DNA sequences) and some !1protein sequencing COMMENT This enzyme may be a regulatory protein for its own !1synthesis. GENETICS !$#gene metH !$#map_position 91 min !$#start_codon GTG FUNCTION !$#description catalyzes methylation of homocysteine by !1methyltetrahydrofolate to form methionine !$#note the inactivated form of this enzyme is reactivated with !1S-adenosyl-L-methionine and either reduced flavodoxin or !1FADH CLASSIFICATION #superfamily cobalamin-dependent methionine synthase; !1cobalamin-binding homology KEYWORDS cobalt; methionine biosynthesis; methyltransferase; monomer FEATURE !$649-896 #domain cobalamin binding #status experimental #label !8B12\ !$745-836 #domain cobalamin-binding homology #label VBB\ !$900-1227 #domain S-adenosylmethionine binding #status !8experimental #label SADM\ !$759 #binding_site methylcobalamin cobalt (His) (axial !8ligand) #status experimental SUMMARY #length 1227 #molecular-weight 135996 #checksum 2026 SEQUENCE /// ENTRY A42863 #type complete TITLE 5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase (EC 2.1.1.14) - Escherichia coli (strain K-12) ALTERNATE_NAMES cobalamin-independent methionine synthase; tetrahydropteroylglutamate methyltransferase ORGANISM #formal_name Escherichia coli DATE 17-Feb-1994 #sequence_revision 10-Oct-1997 #text_change 03-Jun-2002 ACCESSIONS F65187; A42863; S30719; I79560 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65187 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-753 ##label BLAT !'##cross-references GB:AE000458; GB:U00096; NID:g2367299; !1PIDN:AAC76832.1; PID:g2367304; UWGP:b3829 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A42863 !$#authors Gonzalez, J.C.; Banerjee, R.V.; Huang, S.; Sumner, J.S.; !1Matthews, R.G. !$#journal Biochemistry (1992) 31:6045-6056 !$#title Comparison of cobalamin-independent and cobalamin-dependent !1methionine synthases from Escherichia coli: two solutions to !1the same chemical problem. !$#cross-references MUID:92329421; PMID:1339288 !$#accession A42863 !'##molecule_type DNA !'##residues 1-362,'V',364-753 ##label GON !'##cross-references GB:M87625; NID:g304870; PIDN:AAA23544.1; !1PID:g145474 !'##experimental_source strain DH5alphaF' !'##note sequence extracted from NCBI backbone (NCBIP:109176) REFERENCE S30660 !$#authors Daniels, D.L.; Plunkett III, G.; Burland, V.; Blattner, F.R. !$#journal Science (1992) 257:771-778 !$#title Analysis of the Escherichia coli genome: DNA sequence of the !1region from 84.5 to 86.5 minutes. !$#cross-references MUID:92358234; PMID:1379743 !$#accession S30719 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-580,'CVMKWPIWKPLELASSRLTNRR',603-604,'Q',606-658,'R', !1660-753 ##label DAN !'##cross-references EMBL:M87049 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1992 !'##note this sequence has been corrected in reference A64720 REFERENCE I59156 !$#authors Maxon, M.E.; Redfield, B.; Cai, X. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:85-89 !$#title Regulation of methionine synthesis in Escherichia coli: !1Effect of the MetR protein on the expression of the metE and !1metR genes. !$#cross-references MUID:89098936; PMID:2643109 !$#accession I79560 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-22 ##label RES !'##cross-references GB:J04155; NID:g146825; PIDN:AAA24160.1; !1PID:g146827 GENETICS !$#gene metE CLASSIFICATION #superfamily cobalamin-independent methionine synthase KEYWORDS methionine biosynthesis; methylated amino acid; !1methyltransferase FEATURE !$726 #active_site Cys (methylcysteine intermediate) !8#status experimental SUMMARY #length 753 #molecular-weight 84673 #checksum 6435 SEQUENCE /// ENTRY B64137 #type complete TITLE 5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase (EC 2.1.1.14) - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES cobalamin-independent methionine synthase; tetrahydropteroylglutamate methyltransferase ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS B64137 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession B64137 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-756 ##label TIGR !'##cross-references GB:U32843; GB:L42023; NID:g1574554; !1PIDN:AAC23348.1; PID:g1574556; TIGR:HI1702 CLASSIFICATION #superfamily cobalamin-independent methionine synthase KEYWORDS methionine biosynthesis; methylated amino acid; !1methyltransferase FEATURE !$727 #active_site Cys (methylcysteine intermediate) !8#status predicted SUMMARY #length 756 #molecular-weight 85238 #checksum 3795 SEQUENCE /// ENTRY S57636 #type complete TITLE 5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase (EC 2.1.1.14) - Madagascar periwinkle ALTERNATE_NAMES cobalamin-independent methionine synthase; tetrahydropteroylglutamate methyltransferase ORGANISM #formal_name Catharanthus roseus #common_name Madagascar periwinkle DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S57636; S65957 REFERENCE S57636 !$#authors Eichel, J.; Gonzalez, J.C.; Hotze, M.; Matthews, R.G.; !1Schroeder, J. !$#submission submitted to the EMBL Data Library, December 1994 !$#description Cloning and expression of vitamin B12 independent !1L-methionine synthase from the higher plant Catharanthus !1roseus. !$#accession S57636 !'##molecule_type mRNA !'##residues 1-765 ##label EIC !'##cross-references EMBL:X83499; NID:g886470; PIDN:CAA58474.1; !1PID:g886471 REFERENCE S65957 !$#authors Eichel, J.; Gonzalez, J.C.; Hotze, M.; Matthews, R.G.; !1Schroeder, J. !$#journal Eur. J. Biochem. (1995) 230:1053-1058 !$#title Vitamin-B(12)-independent methionine synthase from a higher !1plant (Catharanthus roseus). Molecular characterization, !1regulation, heterologous expression, and enzyme properties. !$#cross-references MUID:95324563; PMID:7601135 !$#accession S65957 !'##status preliminary; nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-765 ##label EI2 !'##cross-references EMBL:X83499; NID:g886470; PIDN:CAA58474.1; !1PID:g886471 GENETICS !$#gene metE CLASSIFICATION #superfamily cobalamin-independent methionine synthase KEYWORDS methionine biosynthesis; methylated amino acid; !1methyltransferase FEATURE !$733 #active_site Cys (methylcysteine intermediate) !8#status predicted SUMMARY #length 765 #molecular-weight 84856 #checksum 7284 SEQUENCE /// ENTRY S50594 #type complete TITLE 5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase (EC 2.1.1.14) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES cobalamin-independent methionine synthase; protein YER091c; tetrahydropteroylglutamate methyltransferase ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S50594; S51518; S59355; S25436; S55758 REFERENCE S50436 !$#authors Dietrich, F.S. !$#submission submitted to the EMBL Data Library, December 1994 !$#description The sequence of S. cerevisiae cosmids 9747, 8198, 9781, and !1lambda clones 3612 and 6052. !$#accession S50594 !'##molecule_type DNA !'##residues 1-767 ##label DIE !'##cross-references EMBL:U18839; NID:g603313; PIDN:AAB64646.1; !1PID:g603329; GSPDB:GN00005; MIPS:YER091c REFERENCE S51518 !$#authors McClurg, J.C. !$#submission submitted to the EMBL Data Library, September 1994 !$#accession S51518 !'##molecule_type DNA !'##residues 1-406,'R',408-767 ##label MCC !'##cross-references EMBL:U15099; NID:g791186; PIDN:AAA65711.1; !1PID:g609350 REFERENCE S59352 !$#authors Korch, C.; Mountain, H.A.; Wenzlau, J.M. !$#submission submitted to the EMBL Data Library, July 1995 !$#description Structure and regulation of MET6, the vitamin !1B12-independent methionine synthase gene of Saccharomyces !1cerevisiae. !$#accession S59355 !'##molecule_type DNA !'##residues 1-767 ##label KOR !'##cross-references EMBL:U32508; NID:g976437; PIDN:AAB60301.1; !1PID:g976441 REFERENCE S25436 !$#authors Ohtake, Y. !$#submission submitted to the EMBL Data Library, March 1988 !$#accession S25436 !'##molecule_type DNA !'##residues 1-71,'FVFVVQCHS',81-486 ##label OHT !'##cross-references EMBL:X07238; NID:g3657; PIDN:CAA30227.1; PID:g3658 REFERENCE S55757 !$#authors Boucherie, H.; Dujardin, G.; Kermorgant, M.; Monribot, C.; !1Slonimski, P.; Perrot, M. !$#journal Yeast (1995) 11:601-613 !$#title Two-dimensional protein map of Saccharomyces cerevisiae: !1construction of a gene-protein index. !$#cross-references MUID:96093904; PMID:7483834 !$#accession S55758 !'##molecule_type protein !'##residues 2-3,'T',5-14 ##label BOU GENETICS !$#gene SGD:MET6; MIPS:YER091c !'##cross-references SGD:S0000893; MIPS:YER091c !$#map_position 5R CLASSIFICATION #superfamily cobalamin-independent methionine synthase KEYWORDS methionine biosynthesis; methylated amino acid; !1methyltransferase FEATURE !$737 #active_site Cys (methylcysteine intermediate) !8#status predicted SUMMARY #length 767 #molecular-weight 85859 #checksum 2117 SEQUENCE /// ENTRY A28443 #type complete TITLE phosphatidylethanolamine N-methyltransferase (EC 2.1.1.17) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein G6673; protein YGR157w ORGANISM #formal_name Saccharomyces cerevisiae DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 21-Jul-2000 ACCESSIONS A28443; S60447; S64466 REFERENCE A92616 !$#authors Kodaki, T.; Yamashita, S. !$#journal J. Biol. Chem. (1987) 262:15428-15435 !$#title Yeast phosphatidylethanolamine methylation pathway. Cloning !1and characterization of two distinct methyltransferase !1genes. !$#cross-references MUID:88058872; PMID:2445736 !$#accession A28443 !'##molecule_type DNA !'##residues 1-869 ##label KOD !'##cross-references EMBL:M16987; NID:g172113; PIDN:AAA34850.1; !1PID:g172114 REFERENCE S60435 !$#authors Skala, J.; Nawrocki, A.; Goffeau, A. !$#journal Yeast (1995) 11:1421-1427 !$#title The sequence of a 27 kb segment on the right arm of !1chromosome VII from Saccharomyces cerevisiae reveals MOL1, !1NAT2, RPL30B, RSR1, CYS4, PEM1/CHO2, NSR1 genes and ten new !1open reading frames. !$#cross-references MUID:96158062; PMID:8585325 !$#accession S60447 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-869 ##label SKA !'##cross-references EMBL:X85807; NID:g1045249; PIDN:CAA59814.1; !1PID:g1045262 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1March 1995 REFERENCE S64428 !$#authors Van Dyck, L.; Skala, J.; de Wergifosse, P.; Purnelle, B.; !1Talla, E.; Nawrocki, A.; Del Bino, S.; Goffeau, A. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64466 !'##molecule_type DNA !'##residues 1-869 ##label VAN !'##cross-references EMBL:Z72942; NID:g1323266; PID:g1323267; !1GSPDB:GN00007; MIPS:YGR157w !'##experimental_source strain S288C GENETICS !$#gene SGD:CHO2; PEM1; MIPS:YGR157w !'##cross-references SGD:S0003389; MIPS:YGR157w !$#map_position 7R CLASSIFICATION #superfamily Saccharomyces cerevisiae !1phosphatidylethanolamine N-methyltransferase KEYWORDS methyltransferase; S-adenosylmethionine; transmembrane !1protein FEATURE !$60-76 #domain transmembrane #status predicted #label TM1\ !$188-204 #domain transmembrane #status predicted #label TM2\ !$221-237 #domain transmembrane #status predicted #label TM3\ !$391-407 #domain transmembrane #status predicted #label TM4\ !$528-544 #domain transmembrane #status predicted #label TM6\ !$549-565 #domain transmembrane #status predicted #label TM5 SUMMARY #length 869 #molecular-weight 101203 #checksum 5267 SEQUENCE /// ENTRY A28171 #type complete TITLE phenylethanolamine N-methyltransferase (EC 2.1.1.28) - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-May-2000 ACCESSIONS A28171; S10894; A28210 REFERENCE A28171 !$#authors Kaneda, N.; Ichinose, H.; Kobayashi, K.; Oka, K.; Kishi, F.; !1Nakazawa, A.; Kurosawa, Y.; Fujita, K.; Nagatsu, T. !$#journal J. Biol. Chem. (1988) 263:7672-7677 !$#title Molecular cloning of cDNA and chromosomal assignment of the !1gene for human phenylethanolamine N-methyltransferase, the !1enzyme for epinephrine biosynthesis. !$#cross-references MUID:88227966; PMID:3372503 !$#accession A28171 !'##molecule_type mRNA !'##residues 1-282 ##label KAN !'##cross-references GB:J03727; NID:g190141; PIDN:AAA60130.1; !1PID:g190142 REFERENCE S10894 !$#authors Sasaoka, T.; Kaneda, N.; Kurosawa, Y.; Fujita, K.; Nagatsu, !1T. !$#journal Neurochem. Int. (1989) 15:555-565 !$#title Structure of human phenylethanolamine N-methyltransferase !1gene: existence of two types of mRNA with different !1transcription initiation sites. !$#accession S10894 !'##status preliminary !'##molecule_type DNA !'##residues 1-282 ##label SAS !'##cross-references EMBL:X52730; NID:g35560; PIDN:CAA36944.1; !1PID:g296668 REFERENCE A28210 !$#authors Baetge, E.E.; Behringer, R.R.; Messing, A.; Brinster, R.L.; !1Palmiter, R.D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:3648-3652 !$#title Transgenic mice express the human phenylethanolamine !1N-methyltransferase gene in adrenal medulla and retina. !$#cross-references MUID:88217959; PMID:2835776 !$#accession A28210 !'##molecule_type mRNA !'##residues 1-168,'AQ',171-282 ##label BAE !'##cross-references GB:J03280; NID:g190143; PIDN:AAA60131.1; !1PID:g387032 GENETICS !$#gene GDB:PNMT; PENT !'##cross-references GDB:120271; OMIM:171190 !$#map_position 17pter-17qter !$#introns 68/1; 137/2 CLASSIFICATION #superfamily phenylethanolamine N-methyltransferase KEYWORDS methyltransferase; S-adenosylmethionine SUMMARY #length 282 #molecular-weight 30855 #checksum 6043 SEQUENCE /// ENTRY S38567 #type complete TITLE phenylethanolamine N-methyltransferase (EC 2.1.1.28) - rat ALTERNATE_NAMES noradrenaline N-methyltransferase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-May-2000 ACCESSIONS S38567; A60060; S03614; I56509 REFERENCE S38567 !$#authors Suh, Y.H.; Kim, S.S.; Choi, W.; Hong, I.A.; Chong, Y.H. !$#submission submitted to the EMBL Data Library, September 1993 !$#description Structure and tissue specific expression of the rat !1phenylethanolamine N-methyl transferase gene. !$#accession S38567 !'##molecule_type DNA !'##residues 1-285 ##label SUH !'##cross-references EMBL:X75333; NID:g414186; PIDN:CAA53082.1; !1PID:g414187 REFERENCE A60060 !$#authors Weisberg, E.P.; Baruchin, A.; Stachowiak, M.K.; Stricker, !1E.M.; Zigmond, M.J.; Kaplan, B.B. !$#journal Brain Res. Mol. Brain Res. (1989) 6:159-166 !$#title Isolation of a rat adrenal cDNA clone encoding !1phenylethanolamine N-methyltransferase and cold-induced !1alterations in adrenal PNMT mRNA and protein. !$#cross-references MUID:90135920; PMID:2575695 !$#accession A60060 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 'LA',18-210,'H',212-213,'L',215-285 ##label WEI REFERENCE S03614 !$#authors Mezey, E. !$#journal Nucleic Acids Res. (1989) 17:2125 !$#title Cloning of the rat adrenal medullary !1phenylethanolamine-N-methyltransferase. !$#cross-references MUID:89183620; PMID:2928117 !$#accession S03614 !'##molecule_type mRNA !'##residues 26-51,'H',53-203,'A',205-210,'H',212-213,'L',215-285 !1##label MEZ !'##cross-references EMBL:X14211; NID:g56943; PIDN:CAA32428.1; !1PID:g56944 REFERENCE I56509 !$#authors Suh, Y.H.; Chun, Y.S.; Lee, I.S.; Kim, S.S.; Choi, W.; !1Chong, Y.H.; Hong, L.; Kim, S.H.; Park, C.W.; Kim, C.G. !$#journal J. Neurochem. (1994) 63:1603-1608 !$#title Complete nucleotide sequence and tissue-specific expression !1of the rat phenylethanolamine N-methyltransferase gene. !$#cross-references MUID:95016700; PMID:7931317 !$#accession I56509 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-285 ##label RES !'##cross-references EMBL:X75333; NID:g414186; PIDN:CAA53082.1; !1PID:g414187 COMMENT This enzyme converts noradrenaline into adrenaline. COMMENT Increased expression of this protein occurs in the adrenal !1medulla of cold-stressed animals. GENETICS !$#introns 69/1; 138/2 CLASSIFICATION #superfamily phenylethanolamine N-methyltransferase KEYWORDS adrenal gland; methyltransferase; S-adenosylmethionine SUMMARY #length 285 #molecular-weight 31670 #checksum 9085 SEQUENCE /// ENTRY A24313 #type complete TITLE phenylethanolamine N-methyltransferase (EC 2.1.1.28) - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-May-2000 ACCESSIONS A24313 REFERENCE A24313 !$#authors Baetge, E.E.; Suh, Y.H.; Joh, T.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:5454-5458 !$#title Complete nucleotide and deduced amino acid sequence of !1bovine phenylethanolamine N-methyltransferase: partial amino !1acid homology with rat tyrosine hydroxylase. !$#cross-references MUID:86287277; PMID:2874553 !$#accession A24313 !'##molecule_type mRNA !'##residues 1-284 ##label BAE !'##cross-references GB:M14318; NID:g163553; PIDN:AAA30715.1; !1PID:g163554 CLASSIFICATION #superfamily phenylethanolamine N-methyltransferase KEYWORDS methyltransferase; S-adenosylmethionine SUMMARY #length 284 #molecular-weight 31147 #checksum 694 SEQUENCE /// ENTRY S42627 #type complete TITLE glycine N-methyltransferase (EC 2.1.1.20) - human ALTERNATE_NAMES folate-binding protein ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 31-Dec-2000 ACCESSIONS S42627; S44383 REFERENCE S42627 !$#authors Ogawa, H.; Gomi, T.; Fujioka, M. !$#journal Comp. Biochem. Physiol. B (1993) 106:601-611 !$#title Mammalian glycine N-methyltransferases. Comparative kinetic !1and structural properties of the enzymes from human, rat, !1rabbit and pig livers. !$#cross-references MUID:94109127; PMID:8281755 !$#accession S42627 !'##status preliminary !'##molecule_type mRNA !'##residues 1-295 ##label OGA !'##cross-references EMBL:X62250; NID:g433939 REFERENCE S44383 !$#authors Ogawa, H. !$#submission submitted to the EMBL Data Library, September 1991 !$#accession S44383 !'##molecule_type mRNA !'##residues 1-118,120-174,'S',176-255,'S','PSS',261-295 ##label OG2 !'##cross-references EMBL:X62250; NID:g433939; PIDN:CAA44164.1; !1PID:g1335203 !'##note the translated sequence in GenBank entry HSLGMETF, release !1114.0, (PIDN:AA44164.1) differs from the published sequence !1in beginning translation at Trp-31 CLASSIFICATION #superfamily glycine N-methyltransferase KEYWORDS acetylated amino end; folate; methyltransferase; !1S-adenosylmethionine FEATURE !$2-295 #product glycine N-methyltransferase #status !8predicted #label MAT\ !$2 #modified_site acetylated amino end (Val) (in mature !8form) #status predicted SUMMARY #length 295 #molecular-weight 32756 #checksum 5213 SEQUENCE /// ENTRY S00112 #type complete TITLE glycine N-methyltransferase (EC 2.1.1.20) - rat ALTERNATE_NAMES folate-binding protein ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 15-Oct-1999 ACCESSIONS S00112; A53205 REFERENCE S00112 !$#authors Ogawa, H.; Konishi, K.; Takata, Y.; Nakashima, H.; Fujioka, !1M. !$#journal Eur. J. Biochem. (1987) 168:141-151 !$#title Rat glycine methyltransferase. Complete amino acid sequence !1deduced from a cDNA clone and characterization of the !1genomic DNA. !$#cross-references MUID:88029410; PMID:2822402 !$#accession S00112 !'##molecule_type DNA !'##residues 1-293 ##label OGA !'##cross-references EMBL:X07833; NID:g56296; PIDN:CAA30686.1; !1PID:g56297 REFERENCE A53205 !$#authors Raha, A.; Wagner, C.; MacDonald, R.G.; Bresnick, E. !$#journal J. Biol. Chem. (1994) 269:5750-5756 !$#title Rat liver cytosolic 4 S polycyclic aromatic !1hydrocarbon-binding protein is glycine N-methyltransferase. !$#cross-references MUID:94164924; PMID:8119914 !$#accession A53205 !'##status preliminary !'##molecule_type protein !'##residues 10-25;167-189;202-228 ##label RAH GENETICS !$#introns 69/2; 112/1; 149/1; 196/3; 237/2 FUNCTION !$#description catalyzes the reversible conversion of !1S-adenosyl-L-methionine and glycine to !1S-adenosyl-L-homocysteine and sarcosine CLASSIFICATION #superfamily glycine N-methyltransferase KEYWORDS acetylated amino end; folate; methyltransferase; !1S-adenosylmethionine FEATURE !$2-293 #product glycine N-methyltransferase #status !8predicted #label MAT\ !$2 #modified_site acetylated amino end (Val) (in mature !8form) #status experimental SUMMARY #length 293 #molecular-weight 32549 #checksum 5109 SEQUENCE /// ENTRY XYECG1 #type complete TITLE tRNA (guanine-N1-)-methyltransferase (EC 2.1.1.31) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 01-Mar-2002 ACCESSIONS A30380; B65039; Q00359 REFERENCE A30380 !$#authors Bystroem, A.S.; Hjalmarsson, K.J.; Wikstroem, P.M.; Bjoerk, !1G.R. !$#journal EMBO J. (1983) 2:899-905 !$#title The nucleotide sequence of an Escherichia coli operon !1containing genes for the tRNA(m1G)methyltransferase, the !1ribosomal proteins S16 and L19 and a 21-K polypeptide. !$#cross-references MUID:84057772; PMID:6357787 !$#accession A30380 !'##molecule_type DNA !'##residues 1-255 ##label BYS !'##cross-references EMBL:X01818; NID:g43141; PIDN:CAA25959.1; !1PID:g43144 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65039 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-255 ##label BLAT !'##cross-references GB:AE000346; GB:U00096; NID:g2367141; !1PIDN:AAC75656.1; PID:g1788959; UWGP:b2607 !'##experimental_source strain K-12, substrain MG1655 COMMENT This protein is one of several nucleases operating together !1with the tRNA-modifying enzymes before the formation of the !1mature tRNA. GENETICS !$#gene trmD !$#map_position 57 min CLASSIFICATION #superfamily tRNA (guanine-N1) methyltransferase KEYWORDS methyltransferase; S-adenosylmethionine; tRNA biosynthesis SUMMARY #length 255 #molecular-weight 28422 #checksum 1640 SEQUENCE /// ENTRY SYLBT #type complete TITLE thymidylate synthase (EC 2.1.1.45) - Lactobacillus casei ORGANISM #formal_name Lactobacillus casei DATE 30-Nov-1980 #sequence_revision 30-Nov-1980 #text_change 07-May-1999 ACCESSIONS A29817; A00548 REFERENCE A29817 !$#authors Pinter, K.; Davisson, V.J.; Santi, D.V. !$#journal DNA (1988) 7:235-241 !$#title Cloning, sequencing, and expression of the Lactobacillus !1casei thymidylate synthase gene. !$#cross-references MUID:88283342; PMID:2840247 !$#accession A29817 !'##molecule_type DNA !'##residues 1-316 ##label PIN !'##cross-references GB:M19653 REFERENCE A00548 !$#authors Maley, G.F.; Bellisario, R.L.; Guarino, D.U.; Maley, F. !$#journal J. Biol. Chem. (1979) 254:1301-1304 !$#title The primary structure of Lactobacillus casei thymidylate !1synthetase. III. The use of 2- !1(2-nitrophenylsulfenyl)-3-methyl-3-bromoindolenine and !1limited tryptic peptides to establish the complete amino !1acid sequence of the enzyme. !$#cross-references MUID:79109713; PMID:105005 !$#accession A00548 !'##molecule_type protein !'##residues 1-316 ##label MAL !'##note this is the final paper of a series CLASSIFICATION #superfamily thymidylate synthase; thymidylate synthase !1homology KEYWORDS deoxyribonucleotide biosynthesis; homodimer; !1methyltransferase FEATURE !$3-316 #domain thymidylate synthase homology #label TDS\ !$198 #active_site Cys #status experimental SUMMARY #length 316 #molecular-weight 36579 #checksum 7059 SEQUENCE /// ENTRY YXSAT3 #type complete TITLE thymidylate synthase (EC 2.1.1.45) - Staphylococcus aureus plasmid pSK1 transposon Tn4003 ORGANISM #formal_name Staphylococcus aureus DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 11-Jun-1999 ACCESSIONS S04163; S14178 REFERENCE S04162 !$#authors Rouch, D.A.; Messerotti, L.J.; Loo, L.S.L.; Jackson, C.A.; !1Skurray, R.A. !$#journal Mol. Microbiol. (1989) 3:161-175 !$#title Trimethoprim resistance transposon Tn4003 from !1Staphylococcus aureus encodes genes for a dihydrofolate !1reductase and thymidylate synthetase flanked by three copies !1of IS257. !$#cross-references MUID:89343620; PMID:2548057 !$#accession S04163 !'##molecule_type DNA !'##residues 1-318 ##label ROU !'##cross-references EMBL:X13290; NID:g46747; PIDN:CAA31648.1; !1PID:g46749 REFERENCE S10715 !$#authors Burdeska, A.; Ott, M.; Bannwarth, W.; Then, R.L. !$#journal FEBS Lett. (1990) 266:159-162 !$#title Identical genes for trimethoprim-resistant dihydrofolate !1reductase from Staphylococcus aureus in Australia and !1Central Europe. !$#cross-references MUID:90306343; PMID:2365064 !$#accession S14178 !'##status preliminary; translation not shown !'##molecule_type DNA !'##residues 253-318 ##label BUR !'##cross-references EMBL:Y07536; NID:g46551; PIDN:CAA68823.1; !1PID:g46552 GENETICS !$#gene thyA !$#genome plasmid CLASSIFICATION #superfamily thymidylate synthase; thymidylate synthase !1homology KEYWORDS deoxyribonucleotide biosynthesis; methyltransferase FEATURE !$6-318 #domain thymidylate synthase homology #label TDS\ !$201 #active_site Cys #status predicted SUMMARY #length 318 #molecular-weight 37178 #checksum 2798 SEQUENCE /// ENTRY SYECT #type complete TITLE thymidylate synthase (EC 2.1.1.45) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 01-Mar-2002 ACCESSIONS A00549; B24137; D65065 REFERENCE A00549 !$#authors Belfort, M.; Maley, G.; Pedersen-Lane, J.; Maley, F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:4914-4918 !$#title Primary structure of the Escherichia coli thyA gene and its !1thymidylate synthase product. !$#cross-references MUID:83273723; PMID:6308660 !$#accession A00549 !'##molecule_type DNA !'##residues 1-264 ##label BEL !'##cross-references GB:J01710; NID:g147986; PIDN:AAA24675.1; !1PID:g147987 !'##experimental_source strain JM103 !'##note most of the sequence was confirmed by protein sequencing REFERENCE A93625 !$#authors Finch, P.W.; Wilson, R.E.; Brown, K.; Hickson, I.D.; !1Tomkinson, A.E.; Emmerson, P.T. !$#journal Nucleic Acids Res. (1986) 14:4437-4451 !$#title Complete nucleotide sequence of the Escherichia coli recC !1gene and of the thyA-recC intergenic region. !$#cross-references MUID:86232583; PMID:3520484 !$#accession B24137 !'##molecule_type DNA !'##residues 63-264 ##label FIN !'##cross-references GB:X03966; NID:g42684; PIDN:CAA27600.1; PID:g42685 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65065 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-264 ##label BLAT !'##cross-references GB:AE000366; GB:U00096; NID:g1789185; !1PIDN:AAC75866.1; PID:g1789191; UWGP:b2827 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene thyA !$#map_position 61 min CLASSIFICATION #superfamily thymidylate synthase; thymidylate synthase !1homology KEYWORDS deoxyribonucleotide biosynthesis; methyltransferase FEATURE !$1-264 #domain thymidylate synthase homology #label TDS\ !$146 #active_site Cys #status predicted SUMMARY #length 264 #molecular-weight 30479 #checksum 5393 SEQUENCE /// ENTRY SYBSTB #type complete TITLE thymidylate synthase (EC 2.1.1.45) B - Bacillus subtilis (strain 168) ORGANISM #formal_name Bacillus subtilis #variety strain 168 DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jun-2000 ACCESSIONS JT0290; E69723 REFERENCE A91594 !$#authors Iwakura, M.; Kawata, M.; Tsuda, K.; Tanaka, T. !$#journal Gene (1988) 64:9-20 !$#title Nucleotide sequence of the thymidylate synthase B and !1dihydrofolate reductase genes contained in one Bacillus !1subtilis operon. !$#cross-references MUID:88284366; PMID:2840350 !$#accession JT0290 !'##molecule_type DNA !'##residues 1-264 ##label IWA !'##cross-references GB:M20012 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69723 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-143,'P',145-264 ##label KUN !'##cross-references GB:Z99115; GB:AL009126; NID:g2634478; !1PIDN:CAB14100.1; PID:g2634602 COMMENT In contrast to the major form of this enzyme, thymidylate !1synthase A (see PIR:I40494), thymidylate synthase B in this !1strain is heat-sensitive. For a heat-stable thymidylate !1synthase B see PIR:S35239. GENETICS !$#gene thyB !$#map_position 200 (degrees) !$#note the thyB gene is 5' to the dfrA gene and overlaps it by one !1nucleotide FUNCTION !$#description catalyzes the methylation of dUMP to dTMP by 5, !110-methylentetrahydrofolate !$#pathway deoxyribonucleotide biosynthesis CLASSIFICATION #superfamily thymidylate synthase; thymidylate synthase !1homology KEYWORDS deoxyribonucleotide biosynthesis; methyltransferase FEATURE !$1-264 #domain thymidylate synthase homology #label TDS\ !$146 #active_site Cys #status predicted SUMMARY #length 264 #molecular-weight 30512 #checksum 4938 SEQUENCE /// ENTRY S35239 #type complete TITLE thymidylate synthase (EC 2.1.1.45) B - Bacillus subtilis (strain ATCC 6633) ORGANISM #formal_name Bacillus subtilis DATE 03-Feb-1994 #sequence_revision 02-Jul-1998 #text_change 11-Jun-1999 ACCESSIONS S35239 REFERENCE S35239 !$#authors Montorsi, M.; Lorenzetti, R. !$#journal Mol. Gen. Genet. (1993) 239:1-5 !$#title Heat-stable and heat-labile thymidylate synthases B of !1Bacillus subtilis: comparison of the nucleotide and amino !1acid sequences. !$#cross-references MUID:93287974; PMID:8510640 !$#accession S35239 !'##molecule_type DNA !'##residues 1-264 ##label MON !'##cross-references EMBL:X69661; NID:g311939; PIDN:CAA49350.1; !1PID:g311940 COMMENT In this strain, unlike strain 168 (see PIR:SYBSTB), !1thymidylate synthase B is heat-stable. GENETICS !$#gene thyB FUNCTION !$#description catalyzes the methylation of dUMP to dTMP by 5, !110-methylentetrahydrofolate !$#pathway deoxyribonucleotide biosynthesis CLASSIFICATION #superfamily thymidylate synthase; thymidylate synthase !1homology KEYWORDS deoxyribonucleotide biosynthesis; methyltransferase FEATURE !$1-264 #domain thymidylate synthase homology #label TDS\ !$146 #active_site Cys #status predicted SUMMARY #length 264 #molecular-weight 30518 #checksum 5301 SEQUENCE /// ENTRY YXHUT #type complete TITLE thymidylate synthase (EC 2.1.1.45) - human ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jun-2000 ACCESSIONS A23047; I55318; JU0120; A22393; A33842 REFERENCE A23047 !$#authors Takeishi, K.; Kaneda, S.; Ayusawa, D.; Shimizu, K.; Gotoh, !1O.; Seno, T. !$#journal Nucleic Acids Res. (1985) 13:2035-2043 !$#title Nucleotide sequence of a functional cDNA for human !1thymidylate synthase. !$#cross-references MUID:85215597; PMID:2987839 !$#accession A23047 !'##molecule_type mRNA !'##residues 1-313 ##label TAK !'##cross-references EMBL:X02308; NID:g37478; PIDN:CAA26178.1; !1PID:g37479 REFERENCE I55318 !$#authors Kaneda, S.; Nalbantoglu, J.; Takeishi, K.; Shimizu, K.; !1Gotoh, O.; Seno, T.; Ayusawa, D. !$#journal J. Biol. Chem. (1990) 265:20277-20284 !$#title Structural and Functional Analysis of the Human Thymidylate !1Synthase Gene. !$#cross-references MUID:91056070; PMID:2243092 !$#accession I55318 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-313 ##label RES !'##cross-references GB:D00596; NID:g220135; PIDN:BAA00472.1; !1PID:g220136 REFERENCE JU0120 !$#authors Takeishi, K.; Kaneda, S.; Ayusawa, D.; Shimizu, K.; Gotoh, !1O.; Seno, T. !$#journal J. Biochem. (1989) 106:575-583 !$#title Human thymidylate synthase gene: isolation of phage clones !1which cover a functionally active gene and structural !1analysis of the region upstream from the translation !1initiation codon. !$#cross-references MUID:90110051; PMID:2532645 !$#accession JU0120 !'##status translation not shown !'##molecule_type DNA !'##residues 1-68 ##label TA2 !'##cross-references GB:D00517; NID:g220133; PIDN:BAA00404.1; !1PID:g2160415 REFERENCE A22393 !$#authors Shimizu, K.; Ayusawa, D.; Takeishi, K.; Seno, T. !$#journal J. Biochem. (1985) 97:845-850 !$#title Purification and NH2-terminal amino acid sequence of human !1thymidylate synthase in an overproducing transformant of !1mouse FM3A cells. !$#cross-references MUID:85261174; PMID:3839505 !$#accession A22393 !'##molecule_type protein !'##residues 2-25 ##label SHI REFERENCE A33842 !$#authors Davisson, V.J.; Sirawaraporn, W.; Santi, D.V. !$#journal J. Biol. Chem. (1989) 264:9145-9148 !$#title Expression of human thymidylate synthase in Escherichia !1coli. !$#cross-references MUID:89255401; PMID:2656695 !$#accession A33842 !'##molecule_type protein !'##residues 2-10 ##label DAV GENETICS !$#gene GDB:TYMS !'##cross-references GDB:120465; OMIM:188350 !$#map_position 18p11.32-18p11.32 !$#introns 69/1; 93/3; 152/1; 186/1; 244/3; 268/3 CLASSIFICATION #superfamily thymidylate synthase; thymidylate synthase !1homology KEYWORDS deoxyribonucleotide biosynthesis; methyltransferase FEATURE !$30-313 #domain thymidylate synthase homology #label TDS\ !$199 #active_site Cys #status predicted SUMMARY #length 313 #molecular-weight 35716 #checksum 2798 SEQUENCE /// ENTRY YXMST #type complete TITLE thymidylate synthase (EC 2.1.1.45) - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 11-Jun-1999 ACCESSIONS A26323; A24157; I48858 REFERENCE A26323 !$#authors Deng, T.; Li, D.; Jenh, C.H.; Johnson, L.F. !$#journal J. Biol. Chem. (1986) 261:16000-16005 !$#title Structure of the gene for mouse thymidylate synthase. !1Locations of introns and multiple transcriptional start !1sites. !$#cross-references MUID:87057259; PMID:3782103 !$#accession A26323 !'##molecule_type DNA !'##residues 1-307 ##label DEN !'##cross-references GB:M13352; NID:g202048; PIDN:AAA40444.1; !1PID:g202050 REFERENCE A24157 !$#authors Perryman, S.M.; Rossana, C.; Deng, T.; Vanin, E.F.; Johnson, !1L.F. !$#journal Mol. Biol. Evol. (1986) 3:313-321 !$#title Sequence of a cDNA for mouse thymidylate synthase reveals !1striking similarity with the prokaryotic enzyme. !$#cross-references MUID:88174353; PMID:3444407 !$#accession A24157 !'##molecule_type mRNA !'##residues 1-307 ##label PER !'##cross-references GB:M13019; NID:g202029; PIDN:AAA40439.1; !1PID:g202030 REFERENCE I48858 !$#authors Deng, T.L.; Li, Y.; Johnson, L.F. !$#journal Nucleic Acids Res. (1989) 17:645-658 !$#title Thymidylate synthase gene expression is stimulated by some !1(but not all) introns. !$#cross-references MUID:89128436; PMID:2915925 !$#accession I48858 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 236-265 ##label RES !'##cross-references EMBL:X14489; NID:g54931; PIDN:CAA32651.1; !1PID:g899339 GENETICS !$#introns 63/1; 87/3; 146/1; 180/1; 238/3; 262/3 CLASSIFICATION #superfamily thymidylate synthase; thymidylate synthase !1homology KEYWORDS deoxyribonucleotide biosynthesis; methyltransferase FEATURE !$24-307 #domain thymidylate synthase homology #label TDS\ !$193 #active_site Cys #status predicted SUMMARY #length 307 #molecular-weight 34958 #checksum 8352 SEQUENCE /// ENTRY SYBE13 #type complete TITLE thymidylate synthase (EC 2.1.1.45) - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 11-Jun-1999 ACCESSIONS D27342 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession D27342 !'##molecule_type DNA !'##residues 1-301 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27896.1; !1PID:g60002 GENETICS !$#gene 13 CLASSIFICATION #superfamily thymidylate synthase; thymidylate synthase !1homology KEYWORDS deoxyribonucleotide biosynthesis; methyltransferase FEATURE !$18-301 #domain thymidylate synthase homology #label TDS\ !$183 #active_site Cys #status predicted SUMMARY #length 301 #molecular-weight 34533 #checksum 3923 SEQUENCE /// ENTRY SYBEHS #type complete TITLE thymidylate synthase (EC 2.1.1.45) - saimiriine herpesvirus 1 ORGANISM #formal_name saimiriine herpesvirus 1 DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 11-Jun-1999 ACCESSIONS A26269 REFERENCE A26269 !$#authors Honess, R.W.; Bodemer, W.; Cameron, K.R.; Niller, H.H.; !1Fleckenstein, B.; Randall, R.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:3604-3608 !$#title The A+T-rich genome of Herpesvirus saimiri contains a highly !1conserved gene for thymidylate synthase. !$#cross-references MUID:86233282; PMID:3012520 !$#accession A26269 !'##molecule_type DNA !'##residues 1-294 ##label HON !'##cross-references GB:M13190; NID:g331074; PIDN:AAA46175.1; !1PID:g331075 CLASSIFICATION #superfamily thymidylate synthase; thymidylate synthase !1homology KEYWORDS deoxyribonucleotide biosynthesis; methyltransferase FEATURE !$11-294 #domain thymidylate synthase homology #label TDS\ !$176 #active_site Cys #status predicted SUMMARY #length 294 #molecular-weight 33497 #checksum 2708 SEQUENCE /// ENTRY SYBEAT #type complete TITLE thymidylate synthase (EC 2.1.1.45) - ateline herpesvirus 2 (strain 810) ORGANISM #formal_name ateline herpesvirus 2 #note host Ateles spp. (spider monkeys) DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 11-Jun-1999 ACCESSIONS A28879 REFERENCE A28879 !$#authors Richter, J.; Puchtler, I.; Fleckenstein, B. !$#journal J. Virol. (1988) 62:3530-3535 !$#title Thymidylate synthase gene of herpesvirus ateles. !$#cross-references MUID:88300915; PMID:3404583 !$#accession A28879 !'##molecule_type DNA !'##residues 1-290 ##label RIC !'##cross-references GB:M22036; NID:g331063; PIDN:AAA46170.1; !1PID:g331064 CLASSIFICATION #superfamily thymidylate synthase; thymidylate synthase !1homology KEYWORDS deoxyribonucleotide biosynthesis; methyltransferase FEATURE !$7-290 #domain thymidylate synthase homology #label TDS\ !$172 #active_site Cys #status predicted SUMMARY #length 290 #molecular-weight 32911 #checksum 2642 SEQUENCE /// ENTRY YXBYT #type complete TITLE thymidylate synthase (EC 2.1.1.45) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein O2950; protein YOR074c ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1993 #sequence_revision 13-Mar-1997 #text_change 16-Jun-2000 ACCESSIONS S66957; A29546 REFERENCE S66929 !$#authors Bohn, C.; Bolotin-Fukuhara, M.; Daignan-Fornier, B.; Dang, !1D.V.; Valens, M. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S66957 !'##molecule_type DNA !'##residues 1-259 ##label BOH !'##cross-references EMBL:Z74982; NID:g1420228; PIDN:CAA99267.1; !1PID:g1420229; GSPDB:GN00015; MIPS:YOR074c !'##experimental_source strain S288C REFERENCE A29546 !$#authors Taylor, G.R.; Lagosky, P.A.; Storms, R.K.; Haynes, R.H. !$#journal J. Biol. Chem. (1987) 262:5298-5307 !$#title Molecular characterization of the cell cycle-regulated !1thymidylate synthase gene of Saccharomyces cerevisiae. !$#cross-references MUID:87165970; PMID:3031048 !$#accession A29546 !'##molecule_type DNA !'##residues 1-33,'GTLSLFAPPQLRFSLRDDTFPLLTTKKVFTRGIILELLWFLAGDT',34-259 !1##label TAY !'##cross-references GB:J02706; NID:g172989; PIDN:AAA60940.1; !1PID:g172990 GENETICS !$#gene SGD:CDC21; TMP1; MIPS:YOR074c !'##cross-references SGD:S0005600; MIPS:YOR074c !$#map_position 15R !$#introns 34/1 CLASSIFICATION #superfamily thymidylate synthase; thymidylate synthase !1homology KEYWORDS deoxyribonucleotide biosynthesis; homodimer; !1methyltransferase; nucleus; pyrimidine deoxynucleotide !1metabolism FEATURE !$10-259 #domain thymidylate synthase homology #label TDS\ !$132 #active_site Cys #status predicted SUMMARY #length 259 #molecular-weight 29955 #checksum 590 SEQUENCE /// ENTRY YXUNTP #type complete TITLE thymidylate synthase (EC 2.1.1.45) - Pneumocystis carinii ORGANISM #formal_name Pneumocystis carinii DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 11-Jun-1999 ACCESSIONS A33720 REFERENCE A33720 !$#authors Edman, U.; Edman, J.C.; Lundgren, B.; Santi, D.V. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:6503-6507 !$#title Isolation and expression of the Pneumocystis carinii !1thymidylate synthase gene. !$#cross-references MUID:89367277; PMID:2671992 !$#accession A33720 !'##molecule_type DNA !'##residues 1-297 ##label EDM !'##cross-references GB:M25415; NID:g169429; PIDN:AAA33802.1; !1PID:g169430 CLASSIFICATION #superfamily thymidylate synthase; thymidylate synthase !1homology KEYWORDS deoxyribonucleotide biosynthesis; methyltransferase FEATURE !$6-297 #domain thymidylate synthase homology #label TDS\ !$173 #active_site Cys #status predicted SUMMARY #length 297 #molecular-weight 34362 #checksum 6599 SEQUENCE /// ENTRY YXCKTA #type complete TITLE thymidylate synthase (EC 2.1.1.45) - yeast (Candida albicans) ORGANISM #formal_name Candida albicans DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 11-Jun-1999 ACCESSIONS A32805 REFERENCE A32805 !$#authors Singer, S.C.; Richards, C.A.; Ferone, R.; Benedict, D.; Ray, !1P. !$#journal J. Bacteriol. (1989) 171:1372-1378 !$#title Cloning, purification, and properties of Candida albicans !1thymidylate synthase. !$#cross-references MUID:89155436; PMID:2646281 !$#accession A32805 !'##molecule_type DNA !'##residues 1-315 ##label SIN !'##cross-references GB:J04230; NID:g170935; PIDN:AAA34374.1; !1PID:g170936 CLASSIFICATION #superfamily thymidylate synthase; thymidylate synthase !1homology KEYWORDS deoxyribonucleotide biosynthesis; methyltransferase FEATURE !$9-315 #domain thymidylate synthase homology #label TDS\ !$176 #active_site Cys #status predicted SUMMARY #length 315 #molecular-weight 36022 #checksum 2514 SEQUENCE /// ENTRY SYBPT4 #type complete TITLE thymidylate synthase (EC 2.1.1.45) - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 01-Dec-2000 ACCESSIONS A00550; T10129 REFERENCE A00550 !$#authors Chu, F.K.; Maley, G.F.; Maley, F.; Belfort, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:3049-3053 !$#title Intervening sequence in the thymidylate synthase gene of !1bacteriophage T4. !$#cross-references MUID:84221902; PMID:6328492 !$#accession A00550 !'##molecule_type DNA !'##residues 1-286 ##label CHU !'##cross-references GB:K01804 REFERENCE Z16963 !$#authors Chu, F. !$#submission submitted to the EMBL Data Library, April 1998 !$#accession T10129 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-31,'T',33-286 ##label CH2 !'##cross-references EMBL:M12742; NID:g3033366; PID:g3033367 !'##experimental_source strain alc4 COMMENT This enzyme is also expressed by the thyA gene of E. coli; !1the phage and host synthases exhibit striking !1dissimilarities in both structure and function. GENETICS !$#gene td CLASSIFICATION #superfamily thymidylate synthase; thymidylate synthase !1homology KEYWORDS deoxyribonucleotide biosynthesis; methyltransferase FEATURE !$1-286 #domain thymidylate synthase homology #label TDS\ !$156 #active_site Cys #status experimental SUMMARY #length 286 #molecular-weight 33073 #checksum 1264 SEQUENCE /// ENTRY I40494 #type complete TITLE thymidylate synthase (EC 2.1.1.45) A - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 12-Aug-1996 #sequence_revision 02-Jul-1998 #text_change 16-Jun-2000 ACCESSIONS I40494; S51710; D69723 REFERENCE I40494 !$#authors Tam, N.H.; Borriss, R. !$#journal Microbiology (1995) 141:291-297 !$#title The thyA gene from Bacillus subtilis exhibits similarity !1with the phage phi 3T thymidylate synthase gene. !$#cross-references MUID:95219082; PMID:7704257 !$#accession I40494 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-279 ##label TAM1 !'##cross-references EMBL:X78560; NID:g607047; PIDN:CAA55307.1; !1PID:g607048 REFERENCE S51710 !$#authors Wolf, M.; Geczi, A.; Simon, O.; Borriss, R. !$#submission submitted to the EMBL Data Library, June 1994 !$#description Cloning and structural characterization of the thyA gene !1from Bacillus subtilis. !$#accession S51710 !'##molecule_type DNA !'##residues 1-279 ##label TAM2 !'##cross-references EMBL:X78560; NID:g607047; PIDN:CAA55307.1; !1PID:g607048 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D69723 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-279 ##label KUN !'##cross-references GB:Z99113; GB:AL009126; NID:g2634090; !1PIDN:CAB13652.1; PID:g2634152 !'##experimental_source strain 168 GENETICS !$#gene thyA FUNCTION !$#description catalyzes the methylation of dUMP to dTMP by 5, !110-methylentetrahydrofolate !$#pathway deoxyribonucleotide biosynthesis CLASSIFICATION #superfamily thymidylate synthase; thymidylate synthase !1homology KEYWORDS deoxyribonucleotide biosynthesis; methyltransferase FEATURE !$5-279 #domain thymidylate synthase homology #label TDS\ !$161 #active_site Cys #status predicted SUMMARY #length 279 #molecular-weight 32807 #checksum 7128 SEQUENCE /// ENTRY SYBP3T #type complete TITLE thymidylate synthase (EC 2.1.1.45) - phage phi-3T ORGANISM #formal_name phage phi-3T #note host Bacillus subtilis DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 11-Jun-1999 ACCESSIONS A22800; A60443 REFERENCE A22800 !$#authors Kenny, E.; Atkinson, T.; Hartley, B.S. !$#journal Gene (1985) 34:335-342 !$#title Nucleotide sequence of the thymidylate synthetase gene !1(thyP3) from the Bacillus subtilis phage phi-3T. !$#cross-references MUID:85232079; PMID:3924741 !$#accession A22800 !'##molecule_type DNA !'##residues 1-279 ##label KEN !'##cross-references GB:M10122; NID:g215472; PIDN:AAA32353.1; !1PID:g215473 REFERENCE A60443 !$#authors Maley, G.F.; Maley, F. !$#journal Adv. Enzyme Regul. (1989) 29:181-187 !$#title An anomaly in the active site region of thymidylate !1synthase. !$#cross-references MUID:90224695; PMID:2699152 !$#accession A60443 !'##status preliminary !'##molecule_type protein !'##residues 1-30;157-160,'X',162-172 ##label MAL GENETICS !$#gene thyP3 CLASSIFICATION #superfamily thymidylate synthase; thymidylate synthase !1homology KEYWORDS deoxyribonucleotide biosynthesis; methyltransferase FEATURE !$5-279 #domain thymidylate synthase homology #label TDS\ !$161 #active_site Cys #status predicted SUMMARY #length 279 #molecular-weight 32785 #checksum 8590 SEQUENCE /// ENTRY A43797 #type complete TITLE thymidylate synthase (EC 2.1.1.45) - Lactococcus lactis subsp. lactis ORGANISM #formal_name Lactococcus lactis subsp. lactis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A43797 REFERENCE A43797 !$#authors Ross, P.; O'Gara, F.; Condon, S. !$#journal Appl. Environ. Microbiol. (1990) 56:2156-2163 !$#title Cloning and characterization of the thymidylate synthase !1gene from Lactococcus lactis subsp. lactis. !$#cross-references MUID:90358505; PMID:2117882 !$#accession A43797 !'##molecule_type DNA !'##residues 1-279 ##label ROS !'##cross-references GB:M33770; NID:g149512; PIDN:AAA25221.1; !1PID:g149513 GENETICS !$#gene thyA CLASSIFICATION #superfamily thymidylate synthase; thymidylate synthase !1homology KEYWORDS DNA biosynthesis; methyltransferase FEATURE !$5-279 #domain thymidylate synthase homology #label TDS SUMMARY #length 279 #molecular-weight 32577 #checksum 5380 SEQUENCE /// ENTRY SZBPSP #type complete TITLE deoxyuridylate hydroxymethyltransferase (EC 2.1.2.-) - phage SPO1 ALTERNATE_NAMES deoxyuridylate hydroxymethylase ORGANISM #formal_name phage SPO1 #note host Bacillus subtilis DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 15-Jan-1999 ACCESSIONS A42992; S21505 REFERENCE A42992 !$#authors Wilhelm, K.; Rueger, W. !$#journal Virology (1992) 189:640-646 !$#title Deoxyuridylate-hydroxymethylase of bacteriophage SPO1. !$#cross-references MUID:92351562; PMID:1641983 !$#accession A42992 !'##molecule_type DNA !'##residues 1-383 ##label WIL !'##cross-references GB:S41270 GENETICS !$#gene 29 CLASSIFICATION #superfamily thymidylate synthase; thymidylate synthase !1homology KEYWORDS transferase FEATURE !$10-304 #domain thymidylate synthase homology #label TDS\ !$162 #active_site Cys #status predicted SUMMARY #length 383 #molecular-weight 44600 #checksum 4398 SEQUENCE /// ENTRY SZBPT2 #type complete TITLE deoxycytidylate 5-hydroxymethyltransferase (EC 2.1.2.8) - phage T2 ALTERNATE_NAMES deoxycytidylate hydroxymethylase ORGANISM #formal_name phage T2 #note host Escherichia coli DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 11-Jun-1999 ACCESSIONS A34273; S35622 REFERENCE JF0071 !$#authors Lamm, N.; Wang, Y.; Mathews, C.K.; Rueger, W. !$#journal Eur. J. Biochem. (1988) 172:553-563 !$#title Deoxycytidylate hydroxymethylase gene of bacteriophage T4: !1nucleotide sequence determination and over-expression of the !1gene. !$#cross-references MUID:88166734; PMID:3350013 !$#accession A34273 !'##molecule_type DNA !'##residues 1-246 ##label LAM REFERENCE S35622 !$#authors Winkler, M.; Rueger, W. !$#journal Nucleic Acids Res. (1993) 21:1500 !$#title Cloning and sequencing of the genes of !1beta-glucosyl-HMC-alpha-glucosyl-transferase of !1bacteriophages T2 and T6. !$#cross-references MUID:93219141; PMID:8464751 !$#accession S35622 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 218-246 ##label WIN !'##cross-references EMBL:X68724; NID:g296435; PIDN:CAA48663.1; !1PID:g296436 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1992 GENETICS !$#gene 42 !$#map_position 25.6-26.2 CLASSIFICATION #superfamily thymidylate synthase; thymidylate synthase !1homology KEYWORDS DNA metabolism; transferase FEATURE !$6-246 #domain thymidylate synthase homology #label TDS\ !$148 #active_site Cys (covalent substrate-binding) #status !8predicted SUMMARY #length 246 #molecular-weight 28583 #checksum 9243 SEQUENCE /// ENTRY SZBPT4 #type complete TITLE deoxycytidylate 5-hydroxymethyltransferase (EC 2.1.2.8) - phage T4 ALTERNATE_NAMES deoxycytidylate hydroxymethylase; gp 42 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 11-Jun-1999 ACCESSIONS JS0786; JF0071; A27746 REFERENCE JS0544 !$#authors Lamm, N.; Tomaschewski, J.; Rueger, W. !$#journal Nucleic Acids Res. (1987) 15:3920 !$#title Nucleotide sequence of the deoxycytidylate hydroxymethylase !1gene of bacteriophage T4 (g42) and the homology of its gene !1product with thymidylate synthase of E. coli. !$#cross-references MUID:87231080; PMID:3295783 !$#accession JS0786 !'##molecule_type DNA !'##residues 1-246 ##label LAM !'##cross-references GB:Y00148; NID:g15311; PIDN:CAA68342.1; PID:g15312 REFERENCE JF0071 !$#authors Lamm, N.; Wang, Y.; Mathews, C.K.; Rueger, W. !$#journal Eur. J. Biochem. (1988) 172:553-563 !$#title Deoxycytidylate hydroxymethylase gene of bacteriophage T4: !1nucleotide sequence determination and over-expression of the !1gene. !$#cross-references MUID:88166734; PMID:3350013 !$#accession JF0071 !'##molecule_type DNA !'##residues 1-246 ##label LA2 !'##cross-references GB:M37159; GB:M28192; NID:g215839; PIDN:AAA21709.1; !1PID:g215843 REFERENCE A27746 !$#authors Thylen, C. !$#journal J. Bacteriol. (1988) 170:1994-1998 !$#title Expression and DNA sequence of the cloned bacteriophage T4 !1dCMP hydroxymethylase gene. !$#cross-references MUID:88169543; PMID:2832395 !$#accession A27746 !'##molecule_type DNA !'##residues 1-163,'L',165-246 ##label THY GENETICS !$#gene 42 !$#map_position 25.483-26.221 FUNCTION !$#description This enzyme catalyzes the hydroxymethylation of dCMP with 5, !110-methylenetetrahydrofolate. CLASSIFICATION #superfamily thymidylate synthase; thymidylate synthase !1homology KEYWORDS DNA metabolism; transferase FEATURE !$6-246 #domain thymidylate synthase homology #label TDS\ !$96,123,124,168,218 #binding_site substrate (Tyr, Arg, Arg, Arg, Tyr) !8#status predicted\ !$148 #active_site Cys (covalent substrate-binding) #status !8predicted SUMMARY #length 246 #molecular-weight 28489 #checksum 9272 SEQUENCE /// ENTRY SZBPT6 #type complete TITLE deoxycytidylate 5-hydroxymethyltransferase (EC 2.1.2.8) - phage T6 ALTERNATE_NAMES deoxycytidylate hydroxymethylase ORGANISM #formal_name phage T6 #note host Escherichia coli DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 11-Jun-1999 ACCESSIONS B34273; S35625 REFERENCE JF0071 !$#authors Lamm, N.; Wang, Y.; Mathews, C.K.; Rueger, W. !$#journal Eur. J. Biochem. (1988) 172:553-563 !$#title Deoxycytidylate hydroxymethylase gene of bacteriophage T4: !1nucleotide sequence determination and over-expression of the !1gene. !$#cross-references MUID:88166734; PMID:3350013 !$#accession B34273 !'##molecule_type DNA !'##residues 1-246 ##label LAM REFERENCE S35622 !$#authors Winkler, M.; Rueger, W. !$#journal Nucleic Acids Res. (1993) 21:1500 !$#title Cloning and sequencing of the genes of !1beta-glucosyl-HMC-alpha-glucosyl-transferase of !1bacteriophages T2 and T6. !$#cross-references MUID:93219141; PMID:8464751 !$#accession S35625 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 200-229,'N',231-246 ##label WIN !'##cross-references EMBL:X68725; NID:g296439; PIDN:CAA48666.1; !1PID:g836596 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1992 GENETICS !$#gene 42 !$#map_position 25.6-26.2 CLASSIFICATION #superfamily thymidylate synthase; thymidylate synthase !1homology KEYWORDS DNA metabolism; transferase FEATURE !$6-246 #domain thymidylate synthase homology #label TDS\ !$148 #active_site Cys (covalent substrate-binding) #status !8predicted SUMMARY #length 246 #molecular-weight 28621 #checksum 9111 SEQUENCE /// ENTRY S46047 #type complete TITLE probable 3-methyl-2-oxobutanoate hydroxymethyltransferase (EC 2.1.2.11) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein YBR1238; hypothetical protein YBR176w ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-May-2000 ACCESSIONS S46047 REFERENCE S46013 !$#authors Entian, K.D.; Koetter, P.; Rose, M.; Becker, J.; Grey, M.; !1Li, Z.; Niegemann, E.; Schenk-Groeninger, R.; Servos, J.; !1Wehner, E.; Wolter, R.; Brendel, M.; Bauer, J.; Braun, H.; !1Dern, K.; Duesterhus, S.; Gruenbein, R.; Hedges, D.; Kiesau, !1P.; Korol, S.; Krems, B.; Proft, M.; Siegers, K.; Baur, A.; !1Boles, E.; Miosga, T.; Schaaff-Gerstenschlaeger, I.; !1Zimmermann, F.K. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S46047 !'##molecule_type DNA !'##residues 1-312 ##label ENT !'##cross-references EMBL:Z36045; NID:g536524; PIDN:CAA85137.1; !1PID:g536525; GSPDB:GN00002; MIPS:YBR176w !'##experimental_source strain S288C GENETICS !$#gene SGD:ECM31; MIPS:YBR176w !'##cross-references SGD:S0000380; MIPS:YBR176w !$#map_position 2R CLASSIFICATION #superfamily 3-methyl-2-oxobutanoate !1hydroxymethyltransferase KEYWORDS coenzyme A biosynthesis; transferase SUMMARY #length 312 #molecular-weight 34465 #checksum 3560 SEQUENCE /// ENTRY RDLNTS #type complete TITLE dihydrofolate reductase (EC 1.5.1.3) / thymidylate synthase (EC 2.1.1.45) - Leishmania major CONTAINS dihydrofolate reductase (EC 1.5.1.3); thymidylate synthase (EC 2.1.1.45) ORGANISM #formal_name Leishmania major DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 11-Jun-1999 ACCESSIONS A23403; A24311; A24734; S08691; S14709 REFERENCE A23403 !$#authors Beverley, S.M.; Ellenberger, T.E.; Cordingley, J.S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:2584-2588 !$#title Primary structure of the gene encoding the bifunctional !1dihydrofolate reductase-thymidylate synthase of Leishmania !1major. !$#cross-references MUID:86205996; PMID:3458220 !$#accession A23403 !'##molecule_type DNA !'##residues 1-520 ##label BEV !'##cross-references EMBL:M12734; NID:g159309; PIDN:AAA29232.1; !1PID:g159310 REFERENCE A24311 !$#authors Grumont, R.; Washtien, W.L.; Caput, D.; Santi, D.V. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:5387-5391 !$#title Bifunctional thymidylate synthase-dihydrofolate reductase !1from Leishmania tropica: sequence homology with the !1corresponding monofunctional proteins. !$#cross-references MUID:86287263; PMID:3461439 !$#accession A24311 !'##molecule_type DNA !'##residues 1-48,'S',50-71,'EEAQR',77-124,'RML',128-306,'T',308-396, !1'V',398-520 ##label GRU !'##cross-references GB:M14330 REFERENCE A24734 !$#authors Garvey, E.P.; Santi, D.V. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:7188-7192 !$#title Limited proteolysis of the bifunctional thymidylate !1synthase-dihydrofolate reductase from Leishmania tropica. !$#cross-references MUID:86042631; PMID:3903747 !$#accession A24734 !'##molecule_type protein !'##residues 334-345,'G',347,349-352,354-358,360-361 ##label GAR CLASSIFICATION #superfamily bifunctional dihydrofolate !1reductase-thymidylate synthase; thymidylate synthase !1homology; type I dihydrofolate reductase homology KEYWORDS deoxyribonucleotide biosynthesis; methyltransferase; !1multifunctional enzyme; NADP; oxidoreductase FEATURE !$26-166 #domain type I dihydrofolate reductase homology !8#label DFR\ !$234-520 #domain thymidylate synthase homology #label TDS\ !$400 #active_site Cys #status predicted SUMMARY #length 520 #molecular-weight 58688 #checksum 2419 SEQUENCE /// ENTRY RDLNTZ #type complete TITLE dihydrofolate reductase (EC 1.5.1.3) / thymidylate synthase (EC 2.1.1.45) - Leishmania mexicana amazonensis CONTAINS dihydrofolate reductase (EC 1.5.1.3); thymidylate synthase (EC 2.1.1.45) ORGANISM #formal_name Leishmania mexicana amazonensis DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 11-Jun-1999 ACCESSIONS S15756; S08660 REFERENCE S15756 !$#authors Nelson, K.; Alonso, G.; Langer, P.J.; Beverley, S.M. !$#journal Nucleic Acids Res. (1990) 18:2819 !$#title Sequence of the dihydrofolate reductase-thymidylate synthase !1(DHFR-TS) gene of Leishmania amazonensis. !$#cross-references MUID:90251468; PMID:2339068 !$#accession S15756 !'##status translation not shown !'##molecule_type DNA !'##residues 1-520 ##label NEL !'##cross-references EMBL:X51735; NID:g9470; PIDN:CAA36020.1; PID:g9471 CLASSIFICATION #superfamily bifunctional dihydrofolate !1reductase-thymidylate synthase; thymidylate synthase !1homology; type I dihydrofolate reductase homology KEYWORDS deoxyribonucleotide biosynthesis; methyltransferase; !1multifunctional enzyme; NADP; oxidoreductase; pyrimethamine !1resistance FEATURE !$26-166 #domain type I dihydrofolate reductase homology !8#label DFR\ !$234-520 #domain thymidylate synthase homology #label TDS\ !$400 #active_site Cys #status predicted SUMMARY #length 520 #molecular-weight 58609 #checksum 1849 SEQUENCE /// ENTRY RDZQK1 #type complete TITLE dihydrofolate reductase (EC 1.5.1.3) / thymidylate synthase (EC 2.1.1.45) - malaria parasite (Plasmodium falciparum) ORGANISM #formal_name Plasmodium falciparum DATE 31-Mar-1990 #sequence_revision 31-Mar-1993 #text_change 09-Jun-2000 ACCESSIONS A39975; A31262; B31262; G31262; C31262; E31262; F31262; !1JS0208; D31262 REFERENCE A39975 !$#authors Bzik, D.J.; Li, W.; Horii, T.; Inselburg, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:8360-8364 !$#title Molecular cloning and sequence analysis of the Plasmodium !1falciparum dihydrofolate reductase-thymidylate synthase !1gene. !$#cross-references MUID:88068594; PMID:2825189 !$#accession A39975 !'##molecule_type DNA !'##residues 1-608 ##label BZI !'##cross-references GB:J03028; NID:g160261; PIDN:AAA29585.1; !1PID:g160262 REFERENCE A94216 !$#authors Cowman, A.F.; Morry, M.J.; Biggs, B.A.; Cross, G.A.M.; !1Foote, S.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:9109-9113 !$#title Amino acid changes linked to pyrimethamine resistance in the !1dihydrofolate reductase-thymidylate synthase gene of !1Plasmodium falciparum. !$#cross-references MUID:89057885; PMID:3057499 !$#accession A31262 !'##molecule_type DNA !'##residues 1-608 ##label COW1 !'##cross-references GB:J03772; NID:g340507; PIDN:AAB59212.1; !1PID:g623444 !$#accession B31262 !'##molecule_type DNA !'##residues 1-50,'I',52-608 ##label COW2 !'##cross-references GB:J03772 !'##note these two sequences are from two different clones, HB3 and 7G8 !$#accession G31262 !'##molecule_type DNA !'##residues 1-15,'V',17-107,'T',109-608 ##label COW !$#accession C31262 !'##molecule_type DNA !'##residues 1-107,'S',109-258 ##label CO2 !$#accession E31262 !'##molecule_type DNA !'##residues 1-58,'R',60-258 ##label CO3 !$#accession F31262 !'##molecule_type DNA !'##residues 1-58,'R',60-163,'L',165-258 ##label CO4 REFERENCE JS0208 !$#authors Snewin, V.A.; England, S.M.; Sims, P.F.G.; Hyde, J.E. !$#journal Gene (1989) 76:41-52 !$#title Characterisation of the dihydrofolate reductase-thymidylate !1synthetase gene from human malaria parasites highly !1resistant to pyrimethamine. !$#cross-references MUID:89306658; PMID:2663650 !$#accession JS0208 !'##molecule_type DNA !'##residues 1-58,'R',60-608 ##label SNE !'##cross-references GB:M22159; NID:g160259; PIDN:AAA29580.1; !1PID:g160260 !'##experimental_source strain K1 !'##note the authors suggest that translation may begin at Met-2 !'##note this sequence is from a pyrimethamine-resistant strain; the !1sequence from the pyrimethamine-sensitive strain FCR3 !1differs from that shown in having 59-Cys and 108-Thr COMMENT Dihydrofolate reductase catalyzes the production of !1methylenetetrahydrofolate; thymidylate synthase catalyzes !1the conversion of dUMP to dTMP using !1methylenetetrahydrofolate. GENETICS !$#map_position 4 CLASSIFICATION #superfamily bifunctional dihydrofolate !1reductase-thymidylate synthase; thymidylate synthase !1homology; type I dihydrofolate reductase homology KEYWORDS deoxyribonucleotide biosynthesis; methyltransferase; !1multifunctional enzyme; NADP; oxidoreductase; pyrimethamine !1resistance FEATURE !$27-163 #domain type I dihydrofolate reductase homology !8#label DFR\ !$325-608 #domain thymidylate synthase homology #label TDS\ !$490 #active_site Cys #status predicted SUMMARY #length 608 #molecular-weight 71764 #checksum 4203 SEQUENCE /// ENTRY RDZQTB #type complete TITLE dihydrofolate reductase (EC 1.5.1.3) / thymidylate synthase (EC 2.1.1.45) - Plasmodium chabaudi ORGANISM #formal_name Plasmodium chabaudi DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 11-Jun-1999 ACCESSIONS A33484 REFERENCE A33484 !$#authors Cowman, A.F.; Lew, A.M. !$#journal Mol. Cell. Biol. (1989) 9:5182-5188 !$#title Antifolate drug selection results in duplication and !1rearrangement of chromosome 7 in Plasmodium chabaudi. !$#cross-references MUID:90097935; PMID:2601715 !$#accession A33484 !'##molecule_type DNA !'##residues 1-583 ##label COW !'##cross-references GB:M30834; NID:g160265; PIDN:AAA29587.1; !1PID:g160266 CLASSIFICATION #superfamily bifunctional dihydrofolate !1reductase-thymidylate synthase; thymidylate synthase !1homology; type I dihydrofolate reductase homology KEYWORDS deoxyribonucleotide biosynthesis; methyltransferase; !1multifunctional enzyme; NADP; oxidoreductase; pyrimethamine !1resistance FEATURE !$24-164 #domain type I dihydrofolate reductase homology !8#label DFR\ !$300-583 #domain thymidylate synthase homology #label TDS\ !$465 #active_site Cys #status predicted SUMMARY #length 583 #molecular-weight 68050 #checksum 7911 SEQUENCE /// ENTRY S06725 #type complete TITLE probable hydro-lyase (EC 4.2.1.-) eryC1 - Saccharopolyspora erythraea ALTERNATE_NAMES erythromycin resistance protein 1 ORGANISM #formal_name Saccharopolyspora erythraea DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 31-Mar-2000 ACCESSIONS S06725; A25855 REFERENCE S06725 !$#authors Dhillon, N.; Hale, R.S.; Cortes, J.; Leadlay, P.F. !$#journal Mol. Microbiol. (1989) 3:1405-1414 !$#title Molecular characterization of a gene from Saccharopolyspora !1erythraea (Streptomyces erythraeus) which is involved in !1erythromycin biosynthesis. !$#cross-references MUID:90136068; PMID:2575703 !$#accession S06725 !'##molecule_type DNA !'##residues 1-365 ##label DHI !'##cross-references EMBL:X15541; NID:g46973; PIDN:CAA33548.1; !1PID:g46974 REFERENCE A91545 !$#authors Bibb, M.J.; Janssen, G.R.; Ward, J.M. !$#journal Gene (1986) 41:E357-E368 !$#title Cloning and analysis of the promoter region of the !1erythromycin-resistance gene (ermE) of Streptomyces !1erythraeus. !$#accession A25855 !'##molecule_type DNA !'##residues 1-32 ##label BIB GENETICS !$#gene eryC1; ermE FUNCTION !$#description induced by erythromycin, this protein is confers resistance !1to the macrolide-lincosamide-streptogramin B group of !1antibiotics CLASSIFICATION #superfamily erythromycin resistance protein KEYWORDS antibiotic resistance; carbon-oxygen lyase; hydro-lyase; !1phosphoprotein; pyridoxal phosphate FEATURE !$185 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 365 #molecular-weight 39235 #checksum 2355 SEQUENCE /// ENTRY S49052 #type complete TITLE probable hydro-lyase (EC 4.2.1.-) tylB - Streptomyces fradiae (strain T59235) ORGANISM #formal_name Streptomyces fradiae #variety strain T59235 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S49052 REFERENCE S49051 !$#authors Merson-Davies, L.A.; Cundliffe, E. !$#journal Mol. Microbiol. (1994) 13:349-355 !$#title Analysis of five tylosin biosynthetic genes from the tyIIBA !1region of the Streptomyces fradiae genome. !$#cross-references MUID:95075319; PMID:7984112 !$#accession S49052 !'##status preliminary !'##molecule_type DNA !'##residues 1-388 ##label MER !'##cross-references EMBL:U08223; NID:g6849140; PIDN:AAA21342.1; !1PID:g473598 !'##note the translation of residues 381-388 and the corresponding !1nucleotide sequence are not shown GENETICS !$#gene tylB !$#start_codon GTG CLASSIFICATION #superfamily erythromycin resistance protein KEYWORDS antibiotic resistance; carbon-oxygen lyase; hydro-lyase; !1phosphoprotein; pyridoxal phosphate FEATURE !$200 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 388 #molecular-weight 41273 #checksum 9724 SEQUENCE /// ENTRY I39599 #type complete TITLE 3-amino-5-hydroxybenzoic acid synthase (EC 4.2.1.-) - Amycolatopsis mediterranei ORGANISM #formal_name Amycolatopsis mediterranei DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 31-Mar-2000 ACCESSIONS I39599 REFERENCE I39599 !$#authors Kim, C.G.; Kirschning, A.; Bergon, P.; Ahn, Y.; Wang, J.J.; !1Shibuya, M.; Floss, H.G. !$#journal J. Am. Chem. Soc. (1992) 114:4941-4943 !$#title Formation of 3-amino-5-hydroxy-benzoic acid, the precursor !1of mC7N units in ansamycin antibiotics, by a new variant of !1the shikimate pathway. !$#accession I39599 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-388 ##label RES !'##cross-references EMBL:U33061; NID:g974606; PIDN:AAA75105.1; !1PID:g974607 GENETICS !$#gene rifD CLASSIFICATION #superfamily erythromycin resistance protein KEYWORDS carbon-oxygen lyase; hydro-lyase; phosphoprotein; pyridoxal !1phosphate FEATURE !$188 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status experimental SUMMARY #length 388 #molecular-weight 42123 #checksum 4402 SEQUENCE /// ENTRY I39657 #type complete TITLE 3-amino-5-hydroxybenzoic acid synthase (EC 4.2.1.-) - Actinosynnema pretiosum subsp. auranticum ORGANISM #formal_name Actinosynnema pretiosum subsp. auranticum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 31-Mar-2000 ACCESSIONS I39657 REFERENCE I39599 !$#authors Kim, C.G.; Kirschning, A.; Bergon, P.; Ahn, Y.; Wang, J.J.; !1Shibuya, M.; Floss, H.G. !$#journal J. Am. Chem. Soc. (1992) 114:4941-4943 !$#title Formation of 3-amino-5-hydroxy-benzoic acid, the precursor !1of mC7N units in ansamycin antibiotics, by a new variant of !1the shikimate pathway. !$#accession I39657 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-388 ##label RES !'##cross-references EMBL:U33059; NID:g974608; PIDN:AAC13997.1; !1PID:g974609 GENETICS !$#gene amtD CLASSIFICATION #superfamily erythromycin resistance protein KEYWORDS carbon-oxygen lyase; hydro-lyase; phosphoprotein; pyridoxal !1phosphate FEATURE !$190 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 388 #molecular-weight 41983 #checksum 2811 SEQUENCE /// ENTRY C53308 #type complete TITLE probable hydro-lyase (EC 4.2.1.-) mosB - Rhizobium meliloti (strain L5-30) ORGANISM #formal_name Rhizobium meliloti DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 31-Mar-2000 ACCESSIONS C53308 REFERENCE A53308 !$#authors Murphy, P.J.; Trenz, S.P.; Grzemski, W.; De Bruijn, F.J.; !1Schell, J. !$#journal J. Bacteriol. (1993) 175:5193-5204 !$#title The Rhizobium meliloti rhizopine mos locus is a mosaic !1structure facilitating its symbiotic regulation. !$#cross-references MUID:93352426; PMID:8349559 !$#accession C53308 !'##status preliminary !'##molecule_type DNA !'##residues 1-507 ##label MUR !'##cross-references GB:L17071; NID:g310301; PIDN:AAA26302.1; !1PID:g310304 GENETICS !$#gene mosB CLASSIFICATION #superfamily erythromycin resistance protein KEYWORDS antibiotic resistance; carbon-oxygen lyase; hydro-lyase; !1phosphoprotein; pyridoxal phosphate FEATURE !$282 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 507 #molecular-weight 55886 #checksum 4233 SEQUENCE /// ENTRY S70674 #type complete TITLE probable hydro-lyase (EC 4.2.1.-) bplC protein - Bordetella pertussis ORGANISM #formal_name Bordetella pertussis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 31-Mar-2000 ACCESSIONS S70674 REFERENCE S70669 !$#authors Allen, A.; Maskell, D. !$#journal Mol. Microbiol. (1996) 19:37-52 !$#title The identification, cloning and mutagenesis of a genetic !1locus required for lipopolysaccharide biosynthesis in !1Bordetella pertussis. !$#cross-references MUID:96419162; PMID:8821935 !$#accession S70674 !'##status preliminary; nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-366 ##label ALL !'##cross-references EMBL:X90711; NID:g992967; PIDN:CAA62247.1; !1PID:g992973 GENETICS !$#gene bplC CLASSIFICATION #superfamily erythromycin resistance protein KEYWORDS antibiotic resistance; carbon-oxygen lyase; hydro-lyase; !1phosphoprotein; pyridoxal phosphate FEATURE !$184 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 366 #molecular-weight 39505 #checksum 1371 SEQUENCE /// ENTRY S70677 #type complete TITLE probable hydro-lyase (EC 4.2.1.-) bplF protein - Bordetella pertussis ORGANISM #formal_name Bordetella pertussis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 31-Mar-2000 ACCESSIONS S70677 REFERENCE S70669 !$#authors Allen, A.; Maskell, D. !$#journal Mol. Microbiol. (1996) 19:37-52 !$#title The identification, cloning and mutagenesis of a genetic !1locus required for lipopolysaccharide biosynthesis in !1Bordetella pertussis. !$#cross-references MUID:96419162; PMID:8821935 !$#accession S70677 !'##status preliminary; nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-395 ##label ALL !'##cross-references EMBL:X90711; NID:g992967; PIDN:CAA62250.1; !1PID:g992976 GENETICS !$#gene bplF CLASSIFICATION #superfamily erythromycin resistance protein KEYWORDS antibiotic resistance; carbon-oxygen lyase; hydro-lyase; !1phosphoprotein; pyridoxal phosphate FEATURE !$185 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 395 #molecular-weight 43546 #checksum 7955 SEQUENCE /// ENTRY B65183 #type complete TITLE probable hydro-lyase (EC 4.2.1.-) - Escherichia coli (strain K-12) ALTERNATE_NAMES hypothetical 41.9K protein rffE-rffT intergenetic region ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS B65183; S30685 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65183 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-376 ##label BLAT !'##cross-references GB:AE000455; GB:U00096; NID:g2367282; !1PIDN:AAC76796.1; PID:g2367285; UWGP:b3791 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S30660 !$#authors Daniels, D.L.; Plunkett III, G.; Burland, V.; Blattner, F.R. !$#journal Science (1992) 257:771-778 !$#title Analysis of the Escherichia coli genome: DNA sequence of the !1region from 84.5 to 86.5 minutes. !$#cross-references MUID:92358234; PMID:1379743 !$#accession S30685 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-268,'RLWRKPGVSSCRRFPMAACRTRICSTLNCGY' ##label DAN !'##cross-references EMBL:M87049; NID:g836656; PIDN:AAA67591.1; !1PID:g148194 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1992 !'##note this sequence is corrected in reference A64720 GENETICS !$#gene yifI CLASSIFICATION #superfamily erythromycin resistance protein KEYWORDS antibiotic resistance; carbon-oxygen lyase; hydro-lyase; !1phosphoprotein; pyridoxal phosphate FEATURE !$181 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 376 #molecular-weight 41901 #checksum 4290 SEQUENCE /// ENTRY C64996 #type complete TITLE probable hydro-lyase (EC 4.2.1.-) b2253 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS C64996 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64996 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-390 ##label BLAT !'##cross-references GB:AE000315; GB:U00096; NID:g1788582; !1PIDN:AAC75313.1; PID:g1788587; UWGP:b2253 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily erythromycin resistance protein KEYWORDS antibiotic resistance; carbon-oxygen lyase; hydro-lyase; !1phosphoprotein; pyridoxal phosphate FEATURE !$193 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 390 #molecular-weight 42890 #checksum 4083 SEQUENCE /// ENTRY S28471 #type complete TITLE probable hydro-lyase (EC 4.2.1.-) perosamine synthetase - Vibrio cholerae ORGANISM #formal_name Vibrio cholerae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 31-Mar-2000 ACCESSIONS S28471 REFERENCE S28467 !$#authors Manning, P.A. !$#submission submitted to the EMBL Data Library, May 1991 !$#accession S28471 !'##molecule_type DNA !'##residues 1-367 ##label MAN !'##cross-references EMBL:X59554; NID:g48381; PIDN:CAA42137.1; !1PID:g48386 !'##experimental_source strain 017 GENETICS !$#gene rfbE CLASSIFICATION #superfamily erythromycin resistance protein KEYWORDS antibiotic resistance; carbon-oxygen lyase; hydro-lyase; !1phosphoprotein; pyridoxal phosphate FEATURE !$181 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 367 #molecular-weight 41010 #checksum 1955 SEQUENCE /// ENTRY I39836 #type complete TITLE probable hydro-lyase (EC 4.2.1.-) degT - Bacillus stearothermophilus ORGANISM #formal_name Bacillus stearothermophilus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 31-Mar-2000 ACCESSIONS I39836 REFERENCE I39836 !$#authors Takagi, T.; Takada, H.; Imanaka, T. !$#journal J. Bacteriol. (1990) 172:411-418 !$#title Nucleotide sequence and cloning in Bacillus subtilis of the !1Bacillus stearothermophilus pleiotropic regulatory gene, !1degT. !$#cross-references MUID:90094248; PMID:2104607 !$#accession I39836 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-372 ##label RES !'##cross-references GB:M29002; NID:g142839; PIDN:AAA22387.1; !1PID:g142840 GENETICS !$#gene degT CLASSIFICATION #superfamily erythromycin resistance protein KEYWORDS antibiotic resistance; carbon-oxygen lyase; hydro-lyase; !1phosphoprotein; pyridoxal phosphate FEATURE !$186 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 372 #molecular-weight 41246 #checksum 1799 SEQUENCE /// ENTRY S76874 #type complete TITLE probable hydro-lyase (EC 4.2.1.-) - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S76874 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76874 !'##status preliminary !'##molecule_type DNA !'##residues 1-385 ##label KAN !'##cross-references EMBL:D90917; GB:AB001339; NID:g1653836; !1PIDN:BAA18786.1; PID:g1653876 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily erythromycin resistance protein KEYWORDS antibiotic resistance; carbon-oxygen lyase; hydro-lyase; !1phosphoprotein; pyridoxal phosphate FEATURE !$205 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 385 #molecular-weight 41596 #checksum 1436 SEQUENCE /// ENTRY S74758 #type complete TITLE probable hydro-lyase (EC 4.2.1.-) slr1615 - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein slr1615 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S74758 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74758 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-378 ##label KAN !'##cross-references EMBL:D90901; GB:AB001339; NID:g1651897; !1PIDN:BAA16909.1; PID:g1651983 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene rfbE CLASSIFICATION #superfamily erythromycin resistance protein KEYWORDS antibiotic resistance; carbon-oxygen lyase; hydro-lyase; !1phosphoprotein; pyridoxal phosphate FEATURE !$185 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 378 #molecular-weight 41944 #checksum 5354 SEQUENCE /// ENTRY S75490 #type complete TITLE probable hydro-lyase (EC 4.2.1.-) slr2114 - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES spore coat polysaccharide biosynthesis protein spsC homolog ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S75490 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75490 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-345 ##label KAN !'##cross-references EMBL:D90911; GB:AB001339; NID:g1653083; !1PIDN:BAA18051.1; PID:g1653135 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene spsC CLASSIFICATION #superfamily erythromycin resistance protein KEYWORDS antibiotic resistance; carbon-oxygen lyase; hydro-lyase; !1phosphoprotein; pyridoxal phosphate FEATURE !$162 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 345 #molecular-weight 38405 #checksum 5451 SEQUENCE /// ENTRY S39720 #type complete TITLE probable hydro-lyase (EC 4.2.1.-) spsC - Bacillus subtilis ALTERNATE_NAMES protein ipa-65d; spore coat polysaccharide synthesis protein spsC ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S39720; A69717 REFERENCE S39655 !$#authors Glaser, P.; Kunst, F.; Arnaud, M.; Coudart, M.P.; Gonzales, !1W.; Hullo, M.F.; Ionescu, M.; Lubochinsky, B.; Marcelino, !1L.; Moszer, I.; Presecan, E.; Santana, M.; Schneider, E.; !1Schweizer, J.; Vertes, A.; Rapoport, G.; Danchin, A. !$#journal Mol. Microbiol. (1993) 10:371-384 !$#title Bacillus subtilis genome project: cloning and sequencing of !1the 97 kb region from 325 degrees to 333 degrees. !$#cross-references MUID:95020537; PMID:7934828 !$#accession S39720 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-389 ##label GLA !'##cross-references EMBL:X73124; NID:g413923; PIDN:CAA51621.1; !1PID:g413989 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1993 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69717 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-389 ##label KUN !'##cross-references GB:Z99123; GB:AL009126; NID:g2636240; !1PIDN:CAB15815.1; PID:g2636324 !'##experimental_source strain 168 GENETICS !$#gene spsC CLASSIFICATION #superfamily erythromycin resistance protein KEYWORDS antibiotic resistance; carbon-oxygen lyase; hydro-lyase; !1phosphoprotein; pyridoxal phosphate FEATURE !$187 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 389 #molecular-weight 43190 #checksum 7818 SEQUENCE /// ENTRY A64433 #type complete TITLE probable hydro-lyase (EC 4.2.1.-) spsC homolog - Methanococcus jannaschii ALTERNATE_NAMES spore coat polysaccharide biosynthesis protein C homolog ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A64433 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession A64433 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-386 ##label BUL !'##cross-references GB:U67549; GB:L77117; NID:g2826363; !1PIDN:AAB99069.1; PID:g1591718; TIGR:MJ1066 GENETICS !$#map_position REV1008090-1006930 CLASSIFICATION #superfamily erythromycin resistance protein KEYWORDS antibiotic resistance; carbon-oxygen lyase; hydro-lyase; !1phosphoprotein; pyridoxal phosphate FEATURE !$185 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 386 #molecular-weight 44501 #checksum 7218 SEQUENCE /// ENTRY S44965 #type complete TITLE probable hydro-lyase (EC 4.2.1.-) lmbS - Streptomyces lincolnensis ORGANISM #formal_name Streptomyces lincolnensis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 31-Mar-2000 ACCESSIONS S44965; S69805 REFERENCE S44946 !$#authors Peschke, U.; Schmidt, H.; Zhang, H.Z.; Piepersberg, W. !$#submission submitted to the EMBL Data Library, May 1994 !$#description Organization of the complete gene cluster for linocomycin !1production in an overproducing strain of Streptomyces !1lincolnenesis 78-11. !$#accession S44965 !'##molecule_type DNA !'##residues 1-382 ##label PES !'##cross-references EMBL:X79146; NID:g499194; PIDN:CAA55764.1; !1PID:g581695 REFERENCE S69805 !$#authors Peschke, U.; Schmidt, H.; Zhang, H.Z.; Piepersberg, W. !$#journal Mol. Microbiol. (1995) 16:1137-1156 !$#title Molecular characterization of the lincomycin-production gene !1cluster of Streptomyces lincolnensis 78-11. !$#cross-references MUID:96020646; PMID:8577249 !$#accession S69805 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type DNA !'##residues 1-3,'WT',6-28,'G',29-47,'RR',50-51,'G',53-60,'R',62,'G', !164-65,'R',67,'N',69-76,'S',78-79,'QVP',83-84,'PRPPAWSTP',94, !1'G',96-97,'CSRTSV',104,'STSP',109-125,'RARCT',131, !1'RPHGRHWN',139-141,'F',143-151,'PRTPRTP',159-196,'T', !1198-217,'V',218-220,232-242,'GRRP',247,'P',249-281, !1'RGHRHQP',290-361,'H',362-379 ##label PEW GENETICS !$#gene lmbS !$#start_codon GTG CLASSIFICATION #superfamily erythromycin resistance protein KEYWORDS antibiotic resistance; carbon-oxygen lyase; hydro-lyase; !1phosphoprotein; pyridoxal phosphate FEATURE !$183 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 382 #molecular-weight 41013 #checksum 6740 SEQUENCE /// ENTRY B43306 #type complete TITLE probable hydro-lyase (EC 4.2.1.-) dnrJ - Streptomyces peucetius ORGANISM #formal_name Streptomyces peucetius DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 31-Mar-2000 ACCESSIONS B43306 REFERENCE A43306 !$#authors Stutzman-Engwall, K.J.; Otten, S.L.; Hutchinson, C.R. !$#journal J. Bacteriol. (1992) 174:144-154 !$#title Regulation of secondary metabolism in Streptomyces spp. and !1overproduction of daunorubicin in Streptomyces peucetius. !$#cross-references MUID:92104954; PMID:1729206 !$#accession B43306 !'##status preliminary !'##molecule_type DNA !'##residues 1-370 ##label STU !'##experimental_source ATCC 29050 !'##note sequence extracted from NCBI backbone (NCBIN:75271, !1NCBIP:75273) CLASSIFICATION #superfamily erythromycin resistance protein KEYWORDS antibiotic resistance; carbon-oxygen lyase; hydro-lyase; !1phosphoprotein; pyridoxal phosphate FEATURE !$186 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 370 #molecular-weight 40967 #checksum 7865 SEQUENCE /// ENTRY I39482 #type complete TITLE MSL leader peptide 2 - Streptococcus agalactiae ORGANISM #formal_name Streptococcus agalactiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS I39482 REFERENCE I39478 !$#authors Brantl, S.; Kummer, C.; Behnke, D. !$#journal Gene (1994) 142:155-156 !$#title Complete nucleotide sequence of plasmid pGB3631, a !1derivative of the Streptococcus agalactiae plasmid pIP501. !$#cross-references MUID:94237483; PMID:7514148 !$#accession I39482 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-43 ##label RES !'##cross-references EMBL:X72021; NID:g511074; PIDN:CAA50903.1; !1PID:g511079 CLASSIFICATION #superfamily MSL leader peptide SUMMARY #length 43 #molecular-weight 4865 #checksum 2605 SEQUENCE /// ENTRY C25028 #type complete TITLE hypothetical erythromycin resistance protein 3 - Enterococcus faecalis ALTERNATE_NAMES macrolide-lincosamide-streptogramin B-resistance protein ORGANISM #formal_name Enterococcus faecalis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C25028 REFERENCE A91808 !$#authors Shaw, J.H.; Clewell, D.B. !$#journal J. Bacteriol. (1985) 164:782-796 !$#title Complete nucleotide sequence of !1macrolide-lincosamide-streptogramin B-resistance transposon !1Tn917 in Streptococccus faecalis. !$#cross-references MUID:86033641; PMID:2997130 !$#accession C25028 !'##molecule_type DNA !'##residues 1-43 ##label SHA CLASSIFICATION #superfamily MSL leader peptide SUMMARY #length 43 #molecular-weight 4806 #checksum 2731 SEQUENCE /// ENTRY S49317 #type complete TITLE MSL leader peptide 3 - Enterococcus hirae ALTERNATE_NAMES probable erythromycin resistance protein 3 ORGANISM #formal_name Enterococcus hirae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S49317 REFERENCE S49315 !$#authors Raze, D.; Coyette, J.; Ghuysen, J.M. !$#submission submitted to the EMBL Data Library, September 1994 !$#accession S49317 !'##molecule_type DNA !'##residues 1-43 ##label RAZ !'##cross-references EMBL:X81655; NID:g551433; PIDN:CAA57315.1; !1PID:g551436 !'##experimental_source strain S185 CLASSIFICATION #superfamily MSL leader peptide SUMMARY #length 43 #molecular-weight 4806 #checksum 2731 SEQUENCE /// ENTRY I40879 #type complete TITLE hypothetical protein 3 ermBP 5'-region - Clostridium perfringens ORGANISM #formal_name Clostridium perfringens DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS I40879 REFERENCE I40877 !$#authors Berryman, D.I.; Rood, J.I. !$#journal Antimicrob. Agents Chemother. (1995) 39:1830-1834 !$#title The closely related ermB/AM genes from Clostridium !1perfringens, Enterococcus faecalis (pAM*1), and !1Streptococcus agalactiae (pIP501), are flanked by variants !1of a directly repeated sequence. !$#cross-references MUID:96100758; PMID:7486927 !$#accession I40879 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-43 ##label BER !'##cross-references EMBL:U18931; NID:g841200; PIDN:AAC43481.1; !1PID:g841203 CLASSIFICATION #superfamily MSL leader peptide SUMMARY #length 43 #molecular-weight 4806 #checksum 2731 SEQUENCE /// ENTRY JS0635 #type complete TITLE rRNA (adenine-N6-)-methyltransferase (EC 2.1.1.48) - Streptomyces lividans ORGANISM #formal_name Streptomyces lividans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-May-2000 ACCESSIONS JS0635 REFERENCE JS0635 !$#authors Jenkins, G.; Cundliffe, E. !$#journal Gene (1991) 108:55-62 !$#title Cloning and characterization of two genes from Streptomyces !1lividans that confer inducible resistance to lincomycin and !1macrolide antibiotics. !$#cross-references MUID:92104506; PMID:1761231 !$#accession JS0635 !'##molecule_type DNA !'##residues 1-260 ##label JEN !'##cross-references GB:M74717; NID:g153345; PIDN:AAA26779.1; !1PID:g153346 !'##experimental_source strain TK21 COMMENT This enzyme confers resistance to lincomycin. COMMENT This enzyme catalyzes the monomethylation of a specific !1adenosine within 23S rRNA. GENETICS !$#gene lrm CLASSIFICATION #superfamily rRNA (adenine-N6-)-methyltransferase KEYWORDS methyltransferase; S-adenosylmethionine SUMMARY #length 260 #molecular-weight 28837 #checksum 6858 SEQUENCE /// ENTRY XYSMRE #type complete TITLE rRNA (adenine-N6-)-methyltransferase (EC 2.1.1.48) - Saccharopolyspora erythraea ALTERNATE_NAMES erythromycin resistance protein ORGANISM #formal_name Saccharopolyspora erythraea DATE 28-Dec-1987 #sequence_revision 30-Sep-1988 #text_change 05-May-2000 ACCESSIONS A91534; A91537; B25855; S09077; A24518; A24524 REFERENCE A91534 !$#authors Uchiyama, H.; Weisblum, B. !$#journal Gene (1985) 38:103-110 !$#title N-Methyl transferase of Streptomyces erythraeus that confers !1resistance to the macrolide-lincosamide-streptogramin B !1antibiotics: amino acid sequence and its homology to cognate !1R-factor enzymes from pathogenic bacilli and cocci. !$#cross-references MUID:86056966; PMID:3934045 !$#accession A91534 !'##molecule_type DNA !'##residues 1-370 ##label UCH REFERENCE A91537 !$#authors Bibb, M.J.; Janssen, G.R.; Ward, J.M. !$#journal Gene (1985) 38:215-226 !$#title Cloning and analysis of the promoter region of the !1erythromycin resistance gene (ermE) of Streptomyces !1erythraeus. !$#cross-references MUID:86056979; PMID:2998943 !$#accession A91537 !'##molecule_type DNA !'##residues 1-70,'V',72-133 ##label BIB REFERENCE A91545 !$#authors Bibb, M.J.; Janssen, G.R.; Ward, J.M. !$#journal Gene (1986) 41:E357-E368 !$#title Cloning and analysis of the promoter region of the !1erythromycin-resistance gene (ermE) of Streptomyces !1erythraeus. !$#note this is an amemded version of the authors previous !1publication (ref. A91537) !$#accession B25855 !'##molecule_type DNA !'##residues 1-70,'V',72-133 ##label BI2 !'##note the authors translated the initiation codon GTG for residue 1 !1as Val REFERENCE S09077 !$#authors Dhillon, N.; Leadlay, P.F. !$#journal FEBS Lett. (1990) 262:189-193 !$#title A repeated decapeptide motif in the C-terminal domain of the !1ribosomal RNA methyltransferase from the erythromycin !1producer Saccharopolyspora erythraea. !$#cross-references MUID:90242924; PMID:2335200 !$#accession S09077 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 155-192,'RRLFKPVPKVD',193-245,'L',247-370 ##label DHI !'##cross-references EMBL:X51891 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1February 1990 GENETICS !$#gene ermE !$#start_codon GTG FUNCTION !$#description induced by erythromycin and confers resistance to the !1macrolide-lincosamide-streptogramin B group of antibiotics CLASSIFICATION #superfamily rRNA (adenine-N6-)-methyltransferase KEYWORDS antibiotic resistance; erythromycin resistance; !1methyltransferase; S-adenosylmethionine SUMMARY #length 370 #molecular-weight 41698 #checksum 6501 SEQUENCE /// ENTRY YESA9E #type complete TITLE rRNA (adenine-N6-)-methyltransferase (EC 2.1.1.48) - Staphylococcus aureus plasmids ALTERNATE_NAMES erythromycin resistance protein ORGANISM #formal_name Staphylococcus aureus DATE 30-Apr-1981 #sequence_revision 01-Sep-1981 #text_change 05-May-2000 ACCESSIONS A93717; A93866; D46568; A03506 REFERENCE A93717 !$#authors Gryczan, T.J.; Grandi, G.; Hahn, J.; Grandi, R.; Dubnau, D. !$#journal Nucleic Acids Res. (1980) 8:6081-6097 !$#title Conformational alteration of mRNA structure and the !1posttranscriptional regulation of erythro-mycin-induced drug !1resistance. !$#cross-references MUID:81124320; PMID:6162157 !$#accession A93717 !'##molecule_type DNA !'##residues 1-244 ##label GRY !'##cross-references GB:V01278; GB:J01755; GB:J01756; GB:J01757; !1GB:J01758; GB:V01279; GB:V01280; NID:g46555; !1PIDN:CAA24591.1; PID:g46558 !'##experimental_source plasmid pE194 REFERENCE A93866 !$#authors Horinouchi, S.; Weisblum, B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1980) 77:7079-7083 !$#title Posttranscriptional modification of mRNA conformation: !1mechanism that regulates erythromycin-induced resistance. !$#cross-references MUID:81175093; PMID:6938954 !$#accession A93866 !'##molecule_type DNA !'##residues 1-244 ##label HOR !'##cross-references GB:V01278; GB:J01755; GB:J01756; GB:J01757; !1GB:J01758; GB:V01279; GB:V01280; NID:g46555; !1PIDN:CAA24591.1; PID:g46558 !'##experimental_source plasmid pE194 REFERENCE A46568 !$#authors Catchpole, I.; Thomas, C.; Davies, A.; Dyke, K.G.H. !$#journal J. Gen. Microbiol. (1988) 134:697-709 !$#title The nucleotide sequence of Staphylococcus aureus plasmid !1pT48 conferring inducible !1macrolide-lincosamide-streptogramin B resistance and !1comparison with similar plasmids expressing constitutive !1resistance. !$#cross-references MUID:89036120; PMID:3141573 !$#accession D46568 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-48 ##label CAT !'##experimental_source plasmid plasmid pT48 GENETICS !$#genome plasmid FUNCTION !$#description this protein is inducible by erythromycin and confers !1resistance to the macrolide-lincosamide-streptogramin B !1group of antibiotics; it is thought to be an rRNA methylase CLASSIFICATION #superfamily rRNA (adenine-N6-)-methyltransferase KEYWORDS antibiotic resistance; erythromycin resistance; !1methyltransferase; S-adenosylmethionine SUMMARY #length 244 #molecular-weight 28861 #checksum 5744 SEQUENCE /// ENTRY XYECRO #type complete TITLE rRNA (adenine-N6,N6-)-dimethyltransferase (EC 2.1.1.-) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 01-Mar-2002 ACCESSIONS A24527; S40572; S03721; C64726 REFERENCE A24527 !$#authors van Buul, C.P.J.J.; van Knippenberg, P.H. !$#journal Gene (1985) 38:65-72 !$#title Nucleotide sequence of the ksgA gene of Escherichia coli: !1comparison of methyltransferases effecting dimethylation of !1adenosine in ribosomal RNA. !$#cross-references MUID:86056993; PMID:3905517 !$#accession A24527 !'##molecule_type DNA !'##residues 1-273 ##label VAN !'##cross-references GB:M11054; NID:g146570; PIDN:AAA24049.1; !1PID:g146571 REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40572 !'##molecule_type DNA !'##residues 1-273 ##label YUR !'##cross-references EMBL:D10483; NID:g216434; PIDN:BAA01327.1; !1PID:g216476 REFERENCE S00843 !$#authors van Gemen, B.; Koets, H.J.; Plooy, C.A.M.; Bodlaender, J.; !1van Knippenberg, P.H. !$#journal Biochimie (1987) 69:841-848 !$#title Characterization of the ksgA gene of Escherichia coli !1determining kasugamycin sensitivity. !$#cross-references MUID:88107880; PMID:3122846 !$#accession S03721 !'##status preliminary !'##molecule_type DNA !'##residues 1-66 ##label VA2 !'##cross-references EMBL:X06536 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64726 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-273 ##label BLAT !'##cross-references GB:AE000115; GB:U00096; NID:g1786230; !1PIDN:AAC73162.1; PID:g1786236; UWGP:b0051 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ksgA !$#map_position 1 min FUNCTION !$#description catalyzes specifically the dimethylation of two adjacent !1adenosine residues near the 3' end of 16S RNA in the 30S !1particle; inactivation of the enzyme leads to kasugamycin !1resistance CLASSIFICATION #superfamily rRNA (adenine-N6-)-methyltransferase KEYWORDS antibiotic resistance; methyltransferase SUMMARY #length 273 #molecular-weight 30420 #checksum 4995 SEQUENCE /// ENTRY I64076 #type complete TITLE rRNA (adenine-N6,N6-)-dimethyltransferase (EC 2.1.1.-) - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS I64076 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession I64076 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-287 ##label TIGR !'##cross-references GB:U32736; GB:L42023; NID:g1573519; !1PIDN:AAC22207.1; PID:g1573534; TIGR:HI0549 CLASSIFICATION #superfamily rRNA (adenine-N6-)-methyltransferase KEYWORDS antibiotic resistance; methyltransferase SUMMARY #length 287 #molecular-weight 32525 #checksum 6395 SEQUENCE /// ENTRY B64251 #type complete TITLE probable methyltransferase (EC 2.1.1.-) ksgA homolog - Mycoplasma genitalium ALTERNATE_NAMES kasgamycin resistance protein ksgA homolog ORGANISM #formal_name Mycoplasma genitalium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B64251 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession B64251 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-259 ##label TIGR !'##cross-references GB:U39733; GB:L43967; NID:g3845054; !1PIDN:AAC72483.1; PID:g3845058; TIGR:MG463 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 !$#start_codon GTG CLASSIFICATION #superfamily rRNA (adenine-N6-)-methyltransferase KEYWORDS antibiotic resistance; methyltransferase SUMMARY #length 259 #molecular-weight 29954 #checksum 1811 SEQUENCE /// ENTRY S73489 #type complete TITLE probable S-adenosylmethionine-6-N',N'-adenosyl(rRNA) dimethyltransferase (EC 2.1.1.-) ksgA - Mycoplasma pneumoniae (ATCC 28342) ALTERNATE_NAMES hypothetical protein K05_orf263V ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 07-Dec-1999 ACCESSIONS S73489 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73489 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-263 ##label HIM !'##cross-references EMBL:AE000017; GB:U00089; NID:g1673812; !1PIDN:AAB95811.1; PID:g1673824 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#gene ksgA !$#genetic_code SGC3 !$#start_codon GTG CLASSIFICATION #superfamily rRNA (adenine-N6-)-methyltransferase KEYWORDS antibiotic resistance; methyltransferase SUMMARY #length 263 #molecular-weight 29794 #checksum 5873 SEQUENCE /// ENTRY D64428 #type complete TITLE probable (adenine-N6,N6-)-dimethyltransferase (EC 2.1.1.-) - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D64428 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession D64428 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-275 ##label BUL !'##cross-references GB:U67545; GB:L77117; NID:g1591680; !1PIDN:AAB99033.1; PID:g1591684; TIGR:MJ1029 GENETICS !$#map_position FOR961664-962491 CLASSIFICATION #superfamily rRNA (adenine-N6-)-methyltransferase KEYWORDS antibiotic resistance; methyltransferase SUMMARY #length 275 #molecular-weight 31771 #checksum 738 SEQUENCE /// ENTRY S66071 #type complete TITLE probable (adenine-N6,N6-)-dimethyltransferase (EC 2.1.1.-) ksgA - Bacillus subtilis ALTERNATE_NAMES high level kasgamycin resistance protein ksgA ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S66071; A69649 REFERENCE S65967 !$#authors Ogasawara, N.; Nakai, S.; Yoshikawa, H. !$#journal DNA Res. (1994) 1:1-14 !$#title Systematic sequencing of the 180 kilobase region of the !1Bacillus subtilis chromosome containing the replication !1origin. !$#cross-references MUID:96051385; PMID:7584024 !$#accession S66071 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-292 ##label OGA !'##cross-references EMBL:D26185; NID:g467326; PIDN:BAA05277.1; !1PID:g467431 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1993 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69649 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-292 ##label KUN !'##cross-references GB:Z99104; GB:AL009126; NID:g2632267; !1PIDN:CAB11818.1; PID:g2632309 !'##experimental_source strain 168 GENETICS !$#gene ksgA CLASSIFICATION #superfamily rRNA (adenine-N6-)-methyltransferase KEYWORDS antibiotic resistance; methyltransferase SUMMARY #length 292 #molecular-weight 32721 #checksum 217 SEQUENCE /// ENTRY S42117 #type complete TITLE kasugamycin dimethyltransferase (EC 2.1.1.-) - Mycoplasma capricolum ORGANISM #formal_name Mycoplasma capricolum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S42117 REFERENCE S42116 !$#authors Miyata, M.; Sano, K.I.; Okada, R.; Fukumura, T. !$#journal Nucleic Acids Res. (1993) 21:4816-4823 !$#title Mapping of replication initiation site in Mycoplasma !1capricolum genome by two-dimensional gel-electrophoretic !1analysis. !$#cross-references MUID:94051609; PMID:8233831 !$#accession S42117 !'##status preliminary; nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-204 ##label MIY !'##cross-references EMBL:D14983; NID:g416232; PIDN:BAA03626.1; !1PID:g416234 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily rRNA (adenine-N6-)-methyltransferase KEYWORDS antibiotic resistance; methyltransferase SUMMARY #length 204 #molecular-weight 24179 #checksum 3499 SEQUENCE /// ENTRY S74516 #type complete TITLE (adenine-N6,N6-)-dimethyltransferase (EC 2.1.1.-) ksgA - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES hypothetical protein sll0708 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S74516 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74516 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-284 ##label KAN !'##cross-references EMBL:D90899; GB:AB001339; NID:g1651650; !1PIDN:BAA16668.1; PID:g1651740 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene ksgA CLASSIFICATION #superfamily rRNA (adenine-N6-)-methyltransferase KEYWORDS antibiotic resistance; methyltransferase SUMMARY #length 284 #molecular-weight 31648 #checksum 5535 SEQUENCE /// ENTRY S47985 #type complete TITLE rRNA (adenine-N6,N6-)-dimethyltransferase (EC 2.1.1.-) DIM1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein P0367; protein YPL266w ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S47985; S65299; S65320 REFERENCE S47985 !$#authors Lafontaine, D.; Delcour, J.; Glasser, A.L.; Desgres, J.; !1Vandenhaute, J. !$#journal J. Mol. Biol. (1994) 241:492-497 !$#title The DIM1 gene responsible for the conserved m(6)(2)Am(6)(2)A !1dimethylation in the 3'-terminal loop of 18 S rRNA is !1essential in yeast. !$#cross-references MUID:94343533; PMID:8064863 !$#accession S47985 !'##molecule_type DNA !'##residues 1-318 ##label LAF !'##cross-references EMBL:L26480; NID:g601875; PIDN:AAA57357.1; !1PID:g601876 REFERENCE S65292 !$#authors Duesterhoeft, A.; Floeth, M.; Fritz, M.; Hilbert, H.; !1Moestl, D. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S65299 !'##molecule_type DNA !'##residues 1-318 ##label DUE !'##cross-references EMBL:Z73622; NID:g1370548; PIDN:CAA98001.1; !1PID:g1370549; GSPDB:GN00016; MIPS:YPL266w !'##experimental_source strain S288C (AB972) REFERENCE S64967 !$#authors Delius, H.; Hebling, U. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S65320 !'##molecule_type DNA !'##residues 1-318 ##label DEL !'##cross-references EMBL:Z73622; NID:g1370548; PIDN:CAA98001.1; !1PID:g1370549; GSPDB:GN00016; MIPS:YPL266w !'##experimental_source strain S288C (AB972) GENETICS !$#gene SGD:DIM1; MIPS:YPL266w !'##cross-references SGD:S0006187; MIPS:YPL266w !$#map_position 16L CLASSIFICATION #superfamily rRNA (adenine-N6-)-methyltransferase KEYWORDS methyltransferase SUMMARY #length 318 #molecular-weight 35951 #checksum 6010 SEQUENCE /// ENTRY A47697 #type complete TITLE probable methyltransferase (EC 2.1.1.-) - Bacillus anthracis ORGANISM #formal_name Bacillus anthracis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A47697 REFERENCE A47697 !$#authors Kim, H.S.; Choi, E.C.; Kim, B.K. !$#journal J. Gen. Microbiol. (1993) 139:601-607 !$#title A macrolide-lincosamide-streptogramin B resistance !1determinant from Bacillus anthracis 590: cloning and !1expression of ermJ. !$#cross-references MUID:93232776; PMID:8473865 !$#accession A47697 !'##status preliminary !'##molecule_type DNA !'##residues 1-287 ##label KIM !'##cross-references GB:L08389; NID:g143196 !'##experimental_source 590 !'##note sequence inconsistent with the nucleotide translation !'##note sequence extracted from NCBI backbone (NCBIN:129973, !1NCBIP:129975) CLASSIFICATION #superfamily rRNA (adenine-N6-)-methyltransferase KEYWORDS antibiotic resistance; methyltransferase SUMMARY #length 287 #molecular-weight 32825 #checksum 8769 SEQUENCE /// ENTRY I39885 #type complete TITLE rRNA methylase ermD [similarity] - Bacillus licheniformis ALTERNATE_NAMES macrolide-lincosamide-streptogramin B resistance protein ORGANISM #formal_name Bacillus licheniformis DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS I39885; B42473 REFERENCE I39884 !$#authors Gryczan, T.; Israeli-Reches, M.; Del Bue, M.; Dubnau, D.A. !$#journal Mol. Gen. Genet. (1984) 194:349-356 !$#title DNA sequence and regulation of ermD, a !1macrolide-lincosamide-streptogramin B resistance element !1from Bacillus licheniformis. !$#cross-references MUID:84245158; PMID:6429477 !$#accession I39885 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-287 ##label RES !'##cross-references GB:M29832; NID:g143199; PIDN:AAA22599.1; !1PID:g143201 REFERENCE A42473 !$#authors Kwak, J.H.; Choi, E.C.; Weisblum, B. !$#journal J. Bacteriol. (1991) 173:4725-4735 !$#title Transcriptional attenuation control of ermK, a !1macrolide-lincosamide-streptogramin B resistance determinant !1from Bacillus licheniformis. !$#cross-references MUID:91310580; PMID:1713206 !$#accession B42473 !'##molecule_type DNA !'##residues 1-17,'Y',19-60,'M',62-79,'A',81-89,'P',91-209,'L',211-220, !1'QA',223,'F',225-287 ##label KWA !'##cross-references GB:M77505; NID:g143194; PIDN:AAA22595.1; !1PID:g143195 GENETICS !$#gene ermD; ermK CLASSIFICATION #superfamily rRNA (adenine-N6-)-methyltransferase SUMMARY #length 287 #molecular-weight 32797 #checksum 8367 SEQUENCE /// ENTRY S55397 #type complete TITLE probable methyltransferase (EC 2.1.1.-) [similarity] - Bacteroides fragilis plasmid CONTAINS macrolide/lincosamide/streptogramin B resistance protein ORGANISM #formal_name Bacteroides fragilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 18-Jul-2001 ACCESSIONS A25157; S34413; S55397 REFERENCE A25157 !$#authors Rasmussen, J.L.; Odelson, D.A.; Macrina, F.L. !$#journal J. Bacteriol. (1986) 168:523-533 !$#title Complete nucleotide sequence and transcription of ermF, a !1macrolide-lincosamide-streptogramin B resistance determinant !1from Bacteroides fragilis. !$#cross-references MUID:87056929; PMID:3023281 !$#accession A25157 !'##molecule_type DNA !'##residues 1-266 ##label RAS !'##cross-references GB:M14730; NID:g150540; PIDN:AAA98217.1; !1PID:g150541 !'##experimental_source plasmid pBF4 REFERENCE S34413 !$#authors Halula, M.C.; Manning, S.; Macrina, F.L. !$#journal Nucleic Acids Res. (1991) 19:3453 !$#title Nucleotide sequence of ermFU, a !1macrolide-lincosamide-streptogramin (MLS) resistance gene !1encoding an RNA methylase from the conjugal element of !1Bacteroides fragilis V503. !$#cross-references MUID:91288232; PMID:1905805 !$#accession S34413 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-7,'L',9-119,'N',121,'E',123-132,'F',134-192,'I',194-202, !1'C',204-226,'T',228-266 ##label HAL !'##cross-references EMBL:M62487; NID:g143942; PIDN:AAA63165.1; !1PID:g143943 !'##experimental_source strain V503, isolate VPI 12256 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1991 REFERENCE S55397 !$#authors Haggoud, A.; Trinh, S.; Mohieddine, M.; Reysset, G. !$#submission submitted to the EMBL Data Library, May 1995 !$#description Genetic analysis of the minimal replicon of plasmid pIP417 !1and comparison with other encoding 5-nitroimidazole !1resistance plasmids from Bacteroides. !$#accession S55397 !'##molecule_type DNA !'##residues 1-266 ##label HAG !'##cross-references EMBL:X87253; NID:g853781; PIDN:CAA60706.1; !1PID:g853782 !'##experimental_source plasmid pIP417 GENETICS !$#gene ermF !$#genome plasmid CLASSIFICATION #superfamily rRNA (adenine-N6-)-methyltransferase KEYWORDS antibiotic resistance; methyltransferase SUMMARY #length 266 #molecular-weight 30356 #checksum 2834 SEQUENCE /// ENTRY G64698 #type complete TITLE 16S rRNA (adenosine-N6,N6-)-dimethyltransferase (EC 2.1.1.-) - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS G64698 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession G64698 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-271 ##label TOM !'##cross-references GB:AE000643; GB:AE000511; NID:g2314598; !1PIDN:AAD08470.1; PID:g2314603; TIGR:HP1431 CLASSIFICATION #superfamily rRNA (adenine-N6-)-methyltransferase KEYWORDS antibiotic resistance; methyltransferase SUMMARY #length 271 #molecular-weight 30644 #checksum 5524 SEQUENCE /// ENTRY A47682 #type complete TITLE 3-demethylubiquinone-9 3-O-methyltransferase (EC 2.1.1.64) - Escherichia coli (strain K-12) ALTERNATE_NAMES 2-octaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinone methyltransferase; ubiG protein ORGANISM #formal_name Escherichia coli DATE 28-May-1999 #sequence_revision 28-May-1999 #text_change 01-Mar-2002 ACCESSIONS A47682; S03757; F64993 REFERENCE A47682 !$#authors Wu, G.; Williams, H.D.; Zamanian, M.; Gibson, F.; Poole, !1R.K. !$#journal J. Gen. Microbiol. (1992) 138:2101-2112 !$#title Isolation and characterization of Escherichia coli mutants !1affected in aerobic respiration: the cloning and nucleotide !1sequence of ubiG. Identification of an !1S-adenosylmethionine-binding motif in protein, RNA, and !1small-molecule methyltransferases. !$#cross-references MUID:93123968; PMID:1479344 !$#accession A47682 !'##molecule_type DNA !'##residues 1-240 ##label WU1 !'##cross-references GB:M87509; NID:g148103; PIDN:AAA24714.1; !1PID:g148104 !'##note sequence extracted from NCBI backbone (NCBIN:121831, !1NCBIP:121832) REFERENCE S03757 !$#authors Hussain, K.; Elliott, E.J.; Salmond, G.P.C. !$#journal Mol. Microbiol. (1987) 1:259-273 !$#title The ParD(-) mutant of Escherichia coli also carries a gyrA !1(am) mutation. The complete sequence of gyrA. !$#cross-references MUID:88201664; PMID:2834621 !$#accession S03757 !'##molecule_type DNA !'##residues 1-240 ##label HUS !'##cross-references EMBL:Y00544; NID:g41637; PIDN:CAA68610.1; !1PID:g41638 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64993 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-240 ##label BLAT !'##cross-references GB:AE000313; GB:U00096; NID:g2367132; !1PIDN:AAC75292.1; PID:g1788564; UWGP:b2232 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ubiG CLASSIFICATION #superfamily 3-demethylubiquinone-9 3-O-methyltransferase; !1bioC homology KEYWORDS methyltransferase; S-adenosylmethionine; ubiquinone !1biosynthesis FEATURE !$57-159 #domain bioC homology #label BIOC SUMMARY #length 240 #molecular-weight 26555 #checksum 8417 SEQUENCE /// ENTRY S32628 #type fragment TITLE 3-demethylubiquinone-9 3-O-methyltransferase (EC 2.1.1.64) - Salmonella typhimurium (fragment) ALTERNATE_NAMES 2-octaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinone methyltransferase; ubiG protein ORGANISM #formal_name Salmonella typhimurium DATE 28-May-1999 #sequence_revision 28-May-1999 #text_change 05-May-2000 ACCESSIONS S32628 REFERENCE S32628 !$#authors Jordan, A. !$#submission submitted to the EMBL Data Library, March 1993 !$#accession S32628 !'##molecule_type DNA !'##residues 1-209 ##label JOR !'##cross-references EMBL:X72948; NID:g510348; PIDN:CAA51451.1; !1PID:g295895 CLASSIFICATION #superfamily 3-demethylubiquinone-9 3-O-methyltransferase; !1bioC homology KEYWORDS methyltransferase; S-adenosylmethionine; ubiquinone !1biosynthesis FEATURE !$24-126 #domain bioC homology #label BIOC SUMMARY #length 209 #checksum 1954 SEQUENCE /// ENTRY G71667 #type complete TITLE probable 3-demethylubiquinone-9 3-O-methyltransferase (EC 2.1.1.64) RP622 - Rickettsia prowazekii ALTERNATE_NAMES 2-octaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinone methyltransferase; ubiG protein ORGANISM #formal_name Rickettsia prowazekii DATE 28-May-1999 #sequence_revision 28-May-1999 #text_change 03-Nov-2000 ACCESSIONS G71667 REFERENCE A71630 !$#authors Andersson, S.G.E.; Zomorodipour, A.; Andersson, J.O.; !1Sicheritz-Ponten, T.; Alsmark, U.C.M.; Podowski, R.M.; !1Naeslund, A.K.; Eriksson, A.S.; Winkler, H.H.; Kurland, C.G. !$#journal Nature (1998) 396:133-140 !$#title The genome sequence of Rickettsia prowazekii and the origin !1of mitochondria. !$#cross-references MUID:99039499; PMID:9823893 !$#accession G71667 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-252 ##label AND !'##cross-references GB:AJ235272; GB:AJ235269; NID:g3861033; !1PIDN:CAA15065.1; PID:g3861165; GSPDB:GN00081 !'##experimental_source strain Madrid E GENETICS !$#gene ubiG; RP622 CLASSIFICATION #superfamily 3-demethylubiquinone-9 3-O-methyltransferase; !1bioC homology KEYWORDS methyltransferase; S-adenosylmethionine; ubiquinone !1biosynthesis FEATURE !$53-153 #domain bioC homology #label BIOC SUMMARY #length 252 #molecular-weight 28772 #checksum 4375 SEQUENCE /// ENTRY I53714 #type complete TITLE 3,4-dihydroxy-5-hexaprenylbenzoate methyltransferase (EC 2.1.1.-) - rat ALTERNATE_NAMES DHHB methyltransferase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 28-May-1999 #sequence_revision 28-May-1999 #text_change 11-Jun-1999 ACCESSIONS I53714 REFERENCE I53714 !$#authors Marbois, B.N.; Hsu, A.; Pillai, R.; Colicelli, J.; Clarke, !1C.F. !$#journal Gene (1994) 138:213-217 !$#title Cloning of a rat cDNA encoding dihydroxypolyprenylbenzoate !1methyltransferase by functional complementation of a !1Saccharomyces cerevisiae mutant deficient in ubiquinone !1biosynthesis. !$#cross-references MUID:94171040; PMID:8125303 !$#accession I53714 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-286 ##label RES !'##cross-references GB:L20427; NID:g457371; PIDN:AAC37643.1; !1PID:g457372 CLASSIFICATION #superfamily 3-demethylubiquinone-9 3-O-methyltransferase; !1bioC homology KEYWORDS methyltransferase; ubiquinone biosynthesis FEATURE !$88-193 #domain bioC homology #label BIOC SUMMARY #length 286 #molecular-weight 32076 #checksum 2784 SEQUENCE /// ENTRY A41171 #type complete TITLE 3,4-dihydroxy-5-hexaprenylbenzoate methyltransferase (EC 2.1.1.-) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES DHHB methyltransferase; protein HRF316; protein O0915; protein YOL096c ORGANISM #formal_name Saccharomyces cerevisiae DATE 28-May-1999 #sequence_revision 28-May-1999 #text_change 21-Jul-2000 ACCESSIONS A41171; S51902; S59178; S66792; S66790 REFERENCE A41171 !$#authors Clarke, C.F.; Williams, W.; Teruya, J.H. !$#journal J. Biol. Chem. (1991) 266:16636-16644 !$#title Ubiquinone biosynthesis in Saccharomyces cerevisiae. !1Isolation and sequence of COQ3, the 3, !14-dihydroxy-5-hexaprenylbenzoate methyltransferase gene. !$#cross-references MUID:91358456; PMID:1885593 !$#accession A41171 !'##molecule_type DNA !'##residues 1-316 ##label CLA !'##cross-references GB:M73270; NID:g171391; PIDN:AAB63972.1; !1PID:g171392 REFERENCE S51848 !$#authors Vandenbol, M.; Durand, P.; Portetelle, D.; Hilger, F. !$#submission submitted to the EMBL Data Library, January 1995 !$#description Sequence analysis of a 44kb DNA fragment of yeast chromosome !1XV including the Ty1-H3 retrotransposon, the suf1(+) !1frameshift suppressor gene for tRNA-Gly, the yeast transfer !1RNA-Thr-1a and a Delta. !$#accession S51902 !'##molecule_type DNA !'##residues 1-316 ##label VAN !'##cross-references EMBL:Z48149; NID:g663234; PIDN:CAA88165.1; !1PID:g663257 REFERENCE S59156 !$#authors Vandenbol, M.; Durand, P.; Portetelle, D.; Hilger, F. !$#journal Yeast (1995) 11:1069-1075 !$#title Sequence analysis of a 44 kb DNA fragment of yeast !1chromosome XV including the Ty1-H3 retrotransposon, the suf1 !1(+) frameshift suppressor gene for tRNA-Gly, the yeast !1transfer RNA-Thr-1a and a delta element. !$#cross-references MUID:96076631; PMID:7502582 !$#accession S59178 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-316 ##label VAW !'##cross-references EMBL:Z48149; NID:g663234; PIDN:CAA88165.1; !1PID:g663257 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1995 REFERENCE S66791 !$#authors Durand, P.; Hilger, F.; Portetelle, D.; Vandenbol, M. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S66792 !'##molecule_type DNA !'##residues 1-316 ##label DUR !'##cross-references EMBL:Z74838; NID:g1419945; PIDN:CAA99109.1; !1PID:g1419946; GSPDB:GN00015; MIPS:YOL096c !'##experimental_source strain S288C REFERENCE S66775 !$#authors Zumstein, E.; Pearson, B.M.; Kalogeropoulos, A.; Schweizer, !1M. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S66790 !'##molecule_type DNA !'##residues 1-8 ##label ZUM !'##cross-references EMBL:Z74838; GSPDB:GN00015; MIPS:YOL096c !'##experimental_source strain S288C GENETICS !$#gene SGD:COQ3; MIPS:YOL096c !'##cross-references SGD:S0005456; MIPS:YOL096c !$#map_position 15L CLASSIFICATION #superfamily 3-demethylubiquinone-9 3-O-methyltransferase; !1bioC homology KEYWORDS methyltransferase; mitochondrion; ubiquinone biosynthesis FEATURE !$127-231 #domain bioC homology #label BIOC SUMMARY #length 316 #molecular-weight 36779 #checksum 6466 SEQUENCE /// ENTRY XYECP4 #type complete TITLE site-specific DNA-methyltransferase (adenine-specific) (EC 2.1.1.72) EcoRI - Escherichia coli plasmids ORGANISM #formal_name Escherichia coli DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 05-May-2000 ACCESSIONS A92308; A00551 REFERENCE A92308 !$#authors Newman, A.K.; Rubin, R.A.; Kim, S.H.; Modrich, P. !$#journal J. Biol. Chem. (1981) 256:2131-2139 !$#title DNA sequences of structural genes for Eco RI DNA restriction !1and modification enzymes. !$#cross-references MUID:81117318; PMID:6257701 !$#accession A92308 !'##molecule_type DNA !'##residues 1-325 ##label NEW !'##cross-references GB:J01675; NID:g152446; PIDN:AAA26372.1; !1PID:g152448 !'##experimental_source strain C600, plasmid pMB4 REFERENCE A92309 !$#authors Rubin, R.A.; Modrich, P.; Vanaman, T.C. !$#journal J. Biol. Chem. (1981) 256:2140-2142 !$#title Partial NH-2- and COOH-terminal sequence analyses of ECO RI !1DNA restriction and modification enzymes. !$#cross-references MUID:81117319; PMID:6257702 !$#contents annotation !$#note the amino and carboxyl ends of the sequence were confirmed !1by amino acid analysis REFERENCE A92310 !$#authors Greene, P.J.; Gupta, M.; Boyer, H.W.; Brown, W.E.; !1Rosenberg, J.M. !$#journal J. Biol. Chem. (1981) 256:2143-2153 !$#title Sequence analysis of the DNA encoding the Eco RI !1endonuclease and methylase. !$#cross-references MUID:81117320; PMID:6257703 !$#accession A00551 !'##molecule_type DNA !'##residues 1-325 ##label GRE !'##cross-references GB:J01675; NID:g152446; PIDN:AAA26372.1; !1PID:g152448 !'##experimental_source plasmid pMB1 GENETICS !$#genome plasmid CLASSIFICATION #superfamily site-specific methyltransferase EcoRI KEYWORDS methyltransferase; restriction modification system; !1S-adenosylmethionine SUMMARY #length 325 #molecular-weight 37913 #checksum 6436 SEQUENCE /// ENTRY XYPS7A #type complete TITLE site-specific DNA-methyltransferase (adenine-specific) (EC 2.1.1.72) PaeR7I - Pseudomonas aeruginosa plasmid pMG7 ALTERNATE_NAMES modification methylase PaeR7I ORGANISM #formal_name Pseudomonas aeruginosa DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 05-May-2000 ACCESSIONS S07366 REFERENCE S07366 !$#authors Theriault, G.; Roy, P.H.; Howard, K.A.; Benner, J.S.; !1Brooks, J.E.; Waters, A.F.; Gingeras, T.R. !$#journal Nucleic Acids Res. (1985) 13:8441-8461 !$#title Nucleotide sequence of the PaeR7 restriction/modification !1system and partial characterization of its protein products. !$#cross-references MUID:86093653; PMID:3001639 !$#accession S07366 !'##molecule_type DNA !'##residues 1-531 ##label THE !'##cross-references EMBL:X03274; NID:g45385; PIDN:CAA27025.1; !1PID:g581435 GENETICS !$#gene paeR7IM !$#genome plasmid !$#start_codon GTG CLASSIFICATION #superfamily site-specific methyltransferase !1(adenine-specific) PaeR7I KEYWORDS methyltransferase; S-adenosylmethionine SUMMARY #length 531 #molecular-weight 59282 #checksum 390 SEQUENCE /// ENTRY XYNHAL #type complete TITLE site-specific DNA-methyltransferase (adenine-specific) (EC 2.1.1.72) NlaIII - Neisseria lactamica ORGANISM #formal_name Neisseria lactamica DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 11-Jun-1999 ACCESSIONS S12036 REFERENCE S12036 !$#authors Labbe, D.; Hoeltke, H.J.; Lau, P.C.K. !$#journal Mol. Gen. Genet. (1990) 224:101-110 !$#title Cloning and characterization of two tandemly arranged DNA !1methyltransferase genes of Neisseria lactamica: an !1adenine-specific M.NlaIII and a cytosine-type methylase. !$#cross-references MUID:91117164; PMID:2277628 !$#accession S12036 !'##molecule_type DNA !'##residues 1-334 ##label LAB !'##cross-references EMBL:X54485; NID:g45002; PIDN:CAA38356.1; !1PID:g45003 GENETICS !$#gene M.NlaIII CLASSIFICATION #superfamily site-specific methyltransferase !1(adenine-specific) NlaIII KEYWORDS methyltransferase; restriction modification system; !1S-adenosylmethionine SUMMARY #length 334 #molecular-weight 38382 #checksum 4098 SEQUENCE /// ENTRY S01615 #type complete TITLE site-specific DNA-methyltransferase (adenine-specific) (EC 2.1.1.72) CviBIII - Chlorella virus CV-NC1A ORGANISM #formal_name Chlorella virus CV-NC1A DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S01615 REFERENCE S01615 !$#authors Narva, K.E.; Wendell, D.L.; Skrdla, M.P.; van Etten, J.L. !$#journal Nucleic Acids Res. (1987) 15:9807-9823 !$#title Molecular cloning and characterization of the gene encoding !1the DNA methyltransferase, M.CviBIII, from Chlorella virus !1NC-1A. !$#cross-references MUID:88096540; PMID:3320956 !$#accession S01615 !'##molecule_type DNA !'##residues 1-377 ##label NAR !'##cross-references EMBL:X06618; NID:g60638; PIDN:CAA29835.1; !1PID:g60639 GENETICS !$#gene cviBIIIM CLASSIFICATION #superfamily site-specific DNA-methyltransferase !1(adenine-specific) CviBIII KEYWORDS methyltransferase; restriction modification system; !1S-adenosylmethionine SUMMARY #length 377 #molecular-weight 42895 #checksum 9973 SEQUENCE /// ENTRY XYSONA #type complete TITLE site-specific DNA-methyltransferase (adenine-specific) (EC 2.1.1.72) DnpII - Streptococcus pneumoniae ALTERNATE_NAMES modification methylase DnpII; restriction-modification system DnpII ORGANISM #formal_name Streptococcus pneumoniae DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 05-May-2000 ACCESSIONS A00556; E24372 REFERENCE A00556 !$#authors Mannarelli, B.M.; Balganesh, T.S.; Greenberg, B.; !1Springhorn, S.S.; Lacks, S.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:4468-4472 !$#title Nucleotide sequence of the Dpn II DNA methylase gene of !1Streptococcus pneumoniae and its relationship to the dam !1gene of Escherichia coli. !$#cross-references MUID:85242705; PMID:2989823 !$#accession A00556 !'##molecule_type DNA !'##residues 1-284 ##label MAN !'##cross-references GB:M11226; NID:g153612; PIDN:AAA26872.1; !1PID:g153613 REFERENCE A24372 !$#authors Lacks, S.A.; Mannarelli, B.M.; Springhorn, S.S.; Greenberg, !1B. !$#journal Cell (1986) 46:993-1000 !$#title Genetic basis of the complementary Dpnl and Dpnll !1restriction systems of S. pneumoniae: an intercellular !1cassette mechanism. !$#cross-references MUID:87002480; PMID:3019562 !$#accession E24372 !'##status preliminary !'##molecule_type DNA !'##residues 1-284 ##label LAC !'##cross-references GB:M14339; NID:g153608; PIDN:AAA88580.1; !1PID:g153609 GENETICS !$#gene DnpM FUNCTION !$#description this site-specific methylase recognizes the double-stranded !1tetranucleotide 5'-GATC and methylates adenine on both !1strands; it protects the DNA from cleavage by DpnII !1restriction enzyme CLASSIFICATION #superfamily site-specific methyltransferase !1(adenine-specific) EcoRV KEYWORDS methyltransferase; S-adenosylmethionine SUMMARY #length 284 #molecular-weight 32907 #checksum 8231 SEQUENCE /// ENTRY XYECR5 #type complete TITLE site-specific DNA-methyltransferase (adenine-specific) (EC 2.1.1.72) EcoRV - Escherichia coli ALTERNATE_NAMES modification methylase EcoRV; restriction-modification system EcoRV ORGANISM #formal_name Escherichia coli DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 05-May-2000 ACCESSIONS A00557; I57396 REFERENCE A93516 !$#authors Bougueleret, L.; Schwarzstein, M.; Tsugita, A.; Zabeau, M. !$#journal Nucleic Acids Res. (1984) 12:3659-3676 !$#title Characterization of the genes coding for the Eco RV !1restriction and modification system of Escherichia coli. !$#cross-references MUID:84221388; PMID:6328432 !$#accession A00557 !'##molecule_type DNA !'##residues 1-298 ##label BOU !'##cross-references GB:X00530; GB:K02335; NID:g41324; PIDN:CAA25209.1; !1PID:g41326 !'##note the authors translated the codon TGC for residue 22 as Trp REFERENCE I57396 !$#authors Kraev, A.S.; Kravets, A.N.; Chernov, B.K.; Skryabin, K.G.; !1Baev, A.A. !$#journal Mol. Biol. (1985) 19:236-242 !$#title The EcoRV restriction-modification system: Genes, enzymes, !1synthetic substrates. !$#accession I57396 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-45 ##label RES !'##cross-references GB:M19941; NID:g147784; PIDN:AAA24614.1; !1PID:g551835 COMMENT This site-specific methylase recognizes the double-stranded !1hexanucleotide 5'-GATATC and causes specific modification !1(methylation) on both strands; it protects the DNA from !1cleavage by EcoRV restriction enzyme. CLASSIFICATION #superfamily site-specific methyltransferase !1(adenine-specific) EcoRV KEYWORDS methyltransferase; S-adenosylmethionine SUMMARY #length 298 #molecular-weight 34638 #checksum 7905 SEQUENCE /// ENTRY XYECDA #type complete TITLE site-specific DNA-methyltransferase (adenine-specific) (EC 2.1.1.72) dam - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 01-Mar-2002 ACCESSIONS A00555; S31744; S04387; S55289; F65133 REFERENCE A00555 !$#authors Brooks, J.E.; Blumenthal, R.M.; Gingeras, T.R. !$#journal Nucleic Acids Res. (1983) 11:837-851 !$#title The isolation and characterization of the Escherichia coli !1DNA adenine methylase (dam) gene. !$#cross-references MUID:83168905; PMID:6300769 !$#accession A00555 !'##molecule_type DNA !'##residues 1-278 ##label BRO !'##cross-references GB:V00272; NID:g41229; PIDN:CAA23530.1; PID:g41230 REFERENCE S31739 !$#authors Lyngstadaas, A.; Boye, E. !$#submission submitted to the EMBL Data Library, January 1993 !$#description dam operon. !$#accession S31744 !'##molecule_type DNA !'##residues 1-278 ##label LYN !'##cross-references EMBL:Z19601; NID:g41221; PIDN:CAA79668.1; !1PID:g41227 REFERENCE A93129 !$#authors Jonczyk, P.; Hines, R.; Smith, D.W. !$#journal Mol. Gen. Genet. (1989) 217:85-96 !$#title The Escherichia coli dam gene is expressed as a distal gene !1of a new operon. !$#cross-references MUID:89364696; PMID:2549371 !$#accession S04387 !'##status preliminary !'##molecule_type DNA !'##residues 1-18 ##label JON !'##cross-references EMBL:X15162; NID:g43273; PIDN:CAA33254.1; !1PID:g43275 !'##note the authors translated the codon TAT for residue 15 as Thr REFERENCE S55287 !$#authors Lyngstadaas, A.; Lobner-Olesen, A.; Boye, E. !$#journal Mol. Gen. Genet. (1995) 247:546-554 !$#title Characterization of three genes in the dam-containing operon !1of Escherichia coli. !$#cross-references MUID:95327050; PMID:7603433 !$#accession S55289 !'##status preliminary !'##molecule_type DNA !'##residues 232-278 ##label LY2 !'##cross-references EMBL:Z19601 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65133 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-278 ##label BLAT !'##cross-references GB:AE000414; GB:U00096; NID:g1789783; !1PIDN:AAC76412.1; PID:g1789789; UWGP:b3387 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene dam !$#map_position 74.3 min FUNCTION !$#description methylates DNA within the sequence GATC and protects the DNA !1from cleavage by the restriction endonuclease MboI; although !1it shares sequence specificity with a number of type II !1restriction endonucleases and methylases, it is thought to !1act in postreplication mismatch repair rather than as part !1of a restriction modification system; it may also play a !1role in DNA replication CLASSIFICATION #superfamily site-specific methyltransferase !1(adenine-specific) EcoRV KEYWORDS methyltransferase; S-adenosylmethionine SUMMARY #length 278 #molecular-weight 32099 #checksum 9733 SEQUENCE /// ENTRY JQ0851 #type complete TITLE site-specific DNA-methyltransferase (adenine-specific) (EC 2.1.1.72) dam, msDNA specific - Escherichia coli retron Ec67 ALTERNATE_NAMES dam methylase homolog ORGANISM #formal_name Escherichia coli retron Ec67 DATE 12-Feb-1993 #sequence_revision 15-Oct-1996 #text_change 05-May-2000 ACCESSIONS JQ0851 REFERENCE JQ0851 !$#authors Hsu, M.Y.; Inouye, M.; Inouye, S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:9454-9458 !$#title Retron for the 67-base multicopy single-stranded DNA from !1Escherichia coli: a potential transposable element encoding !1both reverse transcriptase and Dam methylase functions. !$#cross-references MUID:91067724; PMID:1701261 !$#accession JQ0851 !'##molecule_type DNA !'##residues 1-285 ##label HSU !'##cross-references GB:M55249; NID:g145143; PIDN:AAA23396.1; !1PID:g145150 !'##experimental_source strain Cl-1 GENETICS !$#gene dam !$#note insertion site is equivalent to 19 min of E. coli K12 !1genetic map FUNCTION !$#description catalyzes the methylation of DNA within the sequence GATC !1and protects the DNA from cleavage by the restriction !1endonuclease MboI; it may play a regulatory role in the !1functions of the retron CLASSIFICATION #superfamily site-specific methyltransferase !1(adenine-specific) EcoRV KEYWORDS methyltransferase; S-adenosylmethionine SUMMARY #length 285 #molecular-weight 32254 #checksum 2529 SEQUENCE /// ENTRY XYBPT4 #type complete TITLE site-specific DNA-methyltransferase (adenine-specific) (EC 2.1.1.72) - phage T4 ALTERNATE_NAMES dam protein; DNA adenine methylase; gp dam CONTAINS dam protein, long form; dam protein, short form ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 05-May-2000 ACCESSIONS A00554; S09361 REFERENCE A90996 !$#authors Macdonald, P.M.; Mosig, G. !$#journal EMBO J. (1984) 3:2863-2871 !$#title Regulation of a new bacteriophage T4 gene, 69, that spans an !1origin of DNA replication. !$#cross-references MUID:85126881; PMID:6098451 !$#accession A00554 !'##molecule_type DNA !'##residues 1-259 ##label MAC !'##cross-references GB:X01416; NID:g15329; PIDN:CAA25660.1; PID:g15330 REFERENCE S09361 !$#authors Miner, Z.; Schlagman, S.L.; Hattman, S. !$#journal Nucleic Acids Res. (1989) 17:8149-8157 !$#title Single amino acid changes that alter the DNA sequence !1specificity of the DNA-[N6-adenine] methyltransferase (Dam) !1of bacteriophage T4. !$#cross-references MUID:90045940; PMID:2510127 !$#accession S09361 !'##molecule_type DNA !'##residues 1-259 ##label MIN !'##cross-references EMBL:X17641 COMMENT The gene is under control of the T4 regA protein, a !1translational repressor. GENETICS !$#gene dam FUNCTION !$#description The enzyme produces the methylated base, N6-methyladenine. !$#note The enzyme has a wider range of recognition sequence than !1the host enzyme which recognizes only the palindromic !1sequence CLASSIFICATION #superfamily site-specific methyltransferase !1(adenine-specific) EcoRV KEYWORDS alternative initiators; DNA biosynthesis; DNA replication; !1methyltransferase; S-adenosylmethionine FEATURE !$1-259 #product dam protein, long form #status predicted !8#label MAT\ !$58-259 #product dam protein, short form #status predicted !8#label MA2 SUMMARY #length 259 #molecular-weight 30417 #checksum 1201 SEQUENCE /// ENTRY XYBPT2 #type complete TITLE site-specific DNA-methyltransferase (adenine-specific) (EC 2.1.1.72) - phage T2 ORGANISM #formal_name phage T2 DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 05-May-2000 ACCESSIONS A30195 REFERENCE A30195 !$#authors Miner, Z.; Hattman, S. !$#journal J. Bacteriol. (1988) 170:5177-5184 !$#title Molecular cloning, sequencing, and mapping of the !1bacteriophage T2 dam gene. !$#cross-references MUID:89033901; PMID:3053648 !$#accession A30195 !'##molecule_type DNA !'##residues 1-259 ##label MIN !'##cross-references GB:M22342; NID:g215792; PIDN:AAA32477.1; !1PID:g215793 GENETICS !$#gene dam CLASSIFICATION #superfamily site-specific methyltransferase !1(adenine-specific) EcoRV KEYWORDS methyltransferase; S-adenosylmethionine SUMMARY #length 259 #molecular-weight 30439 #checksum 239 SEQUENCE /// ENTRY JH0768 #type complete TITLE site-specific DNA-methyltransferase (adenine-specific) (EC 2.1.1.72) CviBI - Chlorella virus CV-NC1A ALTERNATE_NAMES modification methylase CviBI ORGANISM #formal_name Chlorella virus CV-NC1A DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 05-May-2000 ACCESSIONS JH0768; S27903 REFERENCE JH0768 !$#authors Kan, T.N.J.; Li, L.; Chandrasegaran, S. !$#journal Gene (1992) 121:1-7 !$#title Cloning, sequencing, overproduction, and purification of M !1CviBI (GANTC) methyltransferase from Chlorella virus NC-1A. !$#cross-references MUID:93051343; PMID:1427082 !$#accession JH0768 !'##molecule_type DNA !'##residues 1-260 ##label KAN !'##cross-references GB:M96366; NID:g323325; PIDN:AAA88829.1; !1PID:g323326 GENETICS !$#gene cvibIM CLASSIFICATION #superfamily site-specific methyltransferase !1(adenine-specific) EcoRV KEYWORDS methyltransferase; S-adenosylmethionine SUMMARY #length 260 #molecular-weight 30704 #checksum 6290 SEQUENCE /// ENTRY XYHIH2 #type complete TITLE site-specific DNA-methyltransferase (adenine-specific) (EC 2.1.1.72) HhaII - Haemophilus haemolyticus ORGANISM #formal_name Haemophilus haemolyticus DATE 20-Sep-1984 #sequence_revision 31-Jul-1998 #text_change 05-May-2000 ACCESSIONS JS0103; PS0316; A00552 REFERENCE JS0103 !$#authors Chandrasegaran, S.; Wu, L.P.; Valda, E.; Smith, H.O. !$#journal Gene (1988) 74:15-21 !$#title Overproduction and purification of the M.HhaII !1methyltransferase from Haemophilus haemolyticus. !$#cross-references MUID:89252850; PMID:3248721 !$#accession JS0103 !'##molecule_type DNA !'##residues 1-228 ##label CHA !'##cross-references GB:M24624; NID:g148897; PIDN:AAA24963.1; !1PID:g148898 !$#accession PS0316 !'##molecule_type protein !'##residues 1-51 ##label CH2 REFERENCE A91503 !$#authors Schoner, B.; Kelly, S.; Smith, H.O. !$#journal Gene (1983) 24:227-236 !$#title The nucleotide sequence of the HhaII restriction and !1modification genes from Haemophilus haemolyticus. !$#cross-references MUID:84059084; PMID:6315538 !$#accession A00552 !'##molecule_type DNA !'##residues 47-192,'WIQHLE',199,'ILCLNAVNKQIEILLVAI' ##label SCH !'##cross-references GB:K00508; NID:g148974 COMMENT The HhaII methylase recognizes the double-stranded !1pentanucleotide GANTC, causes specific modification !1(methylation) on both strands, and protects the DNA from !1cleavage by HhaII endonuclease. COMMENT H. haemolyticus is a minute, gram-negative, rod-shaped !1parasitic bacterium found in mucus membrane of the upper !1respiratory tract of man. GENETICS !$#gene hhaIIM CLASSIFICATION #superfamily site-specific DNA-methyltransferase !1(adenine-specific) HhaII KEYWORDS methyltransferase; S-adenosylmethionine SUMMARY #length 228 #molecular-weight 26432 #checksum 3523 SEQUENCE /// ENTRY C69952 #type complete TITLE probable ribosomal protein L11 methyltransferase (EC 2.1.1.-) yqeT - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS C69952 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69952 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-311 ##label KUN !'##cross-references GB:Z99117; GB:AL009126; NID:g2634966; !1PIDN:CAB14487.1; PID:g2634991 !'##experimental_source strain 168 GENETICS !$#gene yqeT CLASSIFICATION #superfamily ribosomal protein L11 methyltransferase; bioC !1homology KEYWORDS methyltransferase FEATURE !$176-274 #domain bioC homology #label BIOC SUMMARY #length 311 #molecular-weight 34594 #checksum 3492 SEQUENCE /// ENTRY S41759 #type complete TITLE ribosomal protein L11 methyltransferase (EC 2.1.1.-) - Clostridium acetobutylicum ORGANISM #formal_name Clostridium acetobutylicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S41759 REFERENCE S41758 !$#authors Behrens, S.; Narberhaus, F.; Bahl, H. !$#journal FEMS Microbiol. Lett. (1993) 114:53-60 !$#title Cloning, nucleotide sequence and structural analysis of the !1Clostridium acetobutylicum dnaJ gene. !$#cross-references MUID:94123950; PMID:7507453 !$#accession S41759 !'##status preliminary !'##molecule_type DNA !'##residues 1-300 ##label BEH !'##cross-references EMBL:X69050 GENETICS !$#gene prmA CLASSIFICATION #superfamily ribosomal protein L11 methyltransferase; bioC !1homology KEYWORDS methyltransferase FEATURE !$177-274 #domain bioC homology #label BIOC SUMMARY #length 300 #molecular-weight 33778 #checksum 2056 SEQUENCE /// ENTRY S75015 #type complete TITLE ribosomal protein L11 methyltransferase (EC 2.1.1.-) - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES hypothetical protein sll1909 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S75015 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75015 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-300 ##label KAN !'##cross-references EMBL:D90910; GB:AB001339; NID:g1652956; !1PIDN:BAA17877.1; PID:g1652960 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene prmA CLASSIFICATION #superfamily ribosomal protein L11 methyltransferase; bioC !1homology KEYWORDS methyltransferase FEATURE !$157-259 #domain bioC homology #label BIOC SUMMARY #length 300 #molecular-weight 33698 #checksum 5874 SEQUENCE /// ENTRY I64105 #type complete TITLE ribosomal protein L11 methyltransferase (EC 2.1.1.-) - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS I64105 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession I64105 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-296 ##label TIGR !'##cross-references GB:U32778; GB:L42023; NID:g1573997; !1PIDN:AAC22638.1; PID:g1574006; TIGR:HI0978 GENETICS !$#gene prmA CLASSIFICATION #superfamily ribosomal protein L11 methyltransferase; bioC !1homology KEYWORDS methyltransferase FEATURE !$160-257 #domain bioC homology #label BIOC SUMMARY #length 296 #molecular-weight 32764 #checksum 1710 SEQUENCE /// ENTRY D64653 #type complete TITLE ribosomal protein L11 methyltransferase (EC 2.1.1.-) - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS D64653 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession D64653 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-333 ##label TOM !'##cross-references GB:AE000614; GB:AE000511; NID:g2314216; !1PIDN:AAD08114.1; PID:g2314218; TIGR:HP1068 GENETICS !$#gene prmA !$#start_codon GTG CLASSIFICATION #superfamily ribosomal protein L11 methyltransferase; bioC !1homology KEYWORDS methyltransferase FEATURE !$195-292 #domain bioC homology #label BIOC SUMMARY #length 333 #molecular-weight 38160 #checksum 7204 SEQUENCE /// ENTRY S28681 #type complete TITLE site-specific DNA-methyltransferase (adenine-specific) (EC 2.1.1.72) HpaI - Haemophilus parainfluenzae ALTERNATE_NAMES HpaI methyltransferase ORGANISM #formal_name Haemophilus parainfluenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S28681 REFERENCE S28680 !$#authors Ito, H.; Shimato, H.; Sadaoka, A.; Kotani, H.; Kimizuka, F.; !1Kato, I. !$#journal Nucleic Acids Res. (1992) 20:705-709 !$#title Cloning and expression of the HpaI restriction-modification !1genes. !$#cross-references MUID:92178963; PMID:1542567 !$#accession S28681 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-314 ##label ITO !'##cross-references EMBL:D10668; NID:g216713; PIDN:BAA01519.1; !1PID:g216715 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1March 1992 CLASSIFICATION #superfamily site-specific DNA-methyltransferase !1(adenine-specific) HpaI KEYWORDS methyltransferase; restriction modification system; !1S-adenosylmethionine SUMMARY #length 314 #molecular-weight 37392 #checksum 7412 SEQUENCE /// ENTRY H64688 #type complete TITLE site-specific DNA methyltransferase (EC 2.1.1.-) HP1352 - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS H64688 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession H64688 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-359 ##label TOM !'##cross-references GB:AE000636; GB:AE000511; NID:g2314517; !1PIDN:AAD08395.1; PID:g2314521; TIGR:HP1352 CLASSIFICATION #superfamily site-specific DNA-methyltransferase !1(adenine-specific) HpaI KEYWORDS methyltransferase; restriction modification system SUMMARY #length 359 #molecular-weight 41887 #checksum 5412 SEQUENCE /// ENTRY JT0391 #type complete TITLE site-specific DNA methyltransferase (EC 2.1.1.-) HinfI - Haemophilus influenzae ALTERNATE_NAMES modification methylase HinfI ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JT0391 REFERENCE JT0390 !$#authors Chandrasegaran, S.; Lunnen, K.D.; Smith, H.O.; Wilson, G.G. !$#journal Gene (1988) 70:387-392 !$#title Cloning and sequencing the HinfI restriction and !1modification genes. !$#cross-references MUID:89108022; PMID:3063606 !$#accession JT0391 !'##molecule_type DNA !'##residues 1-359 ##label CHA !'##cross-references GB:M22862; NID:g148944; PIDN:AAA24986.1; !1PID:g148945 CLASSIFICATION #superfamily site-specific DNA-methyltransferase !1(adenine-specific) HpaI KEYWORDS methyltransferase; restriction modification system SUMMARY #length 359 #molecular-weight 41805 #checksum 8654 SEQUENCE /// ENTRY S43876 #type complete TITLE site-specific DNA methyltransferase (EC 2.1.1.-) - Caulobacter crescentus ORGANISM #formal_name Caulobacter crescentus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S43876 REFERENCE S43876 !$#authors Zweiger, G.; Marczynski, G.; Shapiro, L. !$#journal J. Mol. Biol. (1994) 235:472-485 !$#title A Caulobacter DNA methyltransferase that functions only in !1the predivisional cell. !$#cross-references MUID:94118303; PMID:8289276 !$#accession S43876 !'##status preliminary !'##molecule_type DNA !'##residues 1-358 ##label ZWE !'##cross-references EMBL:U01032; NID:g393011; PIDN:AAA18913.1; !1PID:g393012 CLASSIFICATION #superfamily site-specific DNA-methyltransferase !1(adenine-specific) HpaI KEYWORDS methyltransferase; restriction modification system SUMMARY #length 358 #molecular-weight 39617 #checksum 1535 SEQUENCE /// ENTRY S35647 #type complete TITLE site-specific DNA methyltransferase (EC 2.1.1.-) mboC - Moraxella bovis ORGANISM #formal_name Moraxella bovis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S35647 REFERENCE S35646 !$#authors Ueno, T.; Ito, H.; Kimizuka, F.; Kotani, H.; Nakajima, K. !$#journal Nucleic Acids Res. (1993) 21:2309-2313 !$#title Gene structure and expression of the MboI restriction - !1modification system. !$#cross-references MUID:93281373; PMID:8506128 !$#accession S35647 !'##status preliminary !'##molecule_type DNA !'##residues 1-273 ##label UEN !'##cross-references GB:D13968; NID:g303627; PIDN:BAA03073.1; !1PID:g303630 CLASSIFICATION #superfamily site-specific DNA-methyltransferase !1(adenine-specific) HpaI KEYWORDS methyltransferase; restriction modification system SUMMARY #length 273 #molecular-weight 31923 #checksum 3532 SEQUENCE /// ENTRY F64073 #type complete TITLE site-specific DNA-methyltransferase (adenine-specific) (EC 2.1.1.72) HincII - Haemophilus influenzae (strains Rd KW20 and Rc) ALTERNATE_NAMES HincII methyltransferase ORGANISM #formal_name Haemophilus influenzae DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 05-May-2000 ACCESSIONS F64073; S10322 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession F64073 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-518 ##label TIGR !'##cross-references GB:U32733; GB:L42023; NID:g1573493; !1PIDN:AAC22171.1; PID:g1573494; TIGR:HI0513 !'##experimental_source strain Rd KW20 REFERENCE S10322 !$#authors Ito, H.; Sadaoka, A.; Kotani, H.; Hiraoka, N.; Nakamura, T. !$#journal Nucleic Acids Res. (1990) 18:3903-3911 !$#title Cloning, nucleotide sequence, and expression of the HincII !1restriction-modification system. !$#cross-references MUID:90326512; PMID:2374714 !$#accession S10322 !'##molecule_type DNA !'##residues 1-261,'Q',263-269,'S',271,288-328,'L',330-333,'N',335-370, !1'EV',373-464,'T',466-518 ##label ITO !'##cross-references EMBL:X52124; NID:g43573; PIDN:CAA36369.1; !1PID:g43574 !'##experimental_source strain Rc CLASSIFICATION #superfamily site-specific DNA-methyltransferase !1(adenine-specific) HincII KEYWORDS methyltransferase; restriction modification system; !1S-adenosylmethionine SUMMARY #length 518 #molecular-weight 60409 #checksum 8479 SEQUENCE /// ENTRY JU0470 #type complete TITLE site-specific DNA-methyltransferase (adenine-specific) (EC 2.1.1.72) type II - Acinetobacter calcoaceticus ALTERNATE_NAMES type II restriction enzyme, M chain ORGANISM #formal_name Acinetobacter calcoaceticus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-May-2000 ACCESSIONS JU0470 REFERENCE JU0469 !$#authors Kawakami, B.; Christophe, H.; Nagatomo, M.; Oka, M. !$#journal Agric. Biol. Chem. (1991) 55:1553-1559 !$#title Cloning and nucleotide sequences of the AccI !1restriction-modification genes in Acinetobacter !1calcoaceticus. !$#cross-references MUID:91345839; PMID:1368703 !$#accession JU0470 !'##molecule_type DNA !'##residues 1-540 ##label KAW GENETICS !$#gene M-ACCI CLASSIFICATION #superfamily site-specific DNA-methyltransferase !1(adenine-specific) HincII KEYWORDS methyltransferase; restriction modification system; !1S-adenosylmethionine FEATURE !$123-146 #region characteristic of N6-adenine methylase SUMMARY #length 540 #molecular-weight 63019 #checksum 2695 SEQUENCE /// ENTRY F64633 #type complete TITLE site-specific DNA-methyltransferase (EC 2.1.1.-) HP0910 - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 18-Aug-2000 ACCESSIONS F64633 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession F64633 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-379 ##label TOM !'##cross-references GB:AE000600; GB:AE000511; NID:g2314042; !1PIDN:AAD07955.1; PID:g2314045; TIGR:HP0910 GENETICS !$#start_codon TTG CLASSIFICATION #superfamily site-specific DNA-methyltransferase HP0910 KEYWORDS methyltransferase; restriction modification system SUMMARY #length 379 #molecular-weight 44081 #checksum 7528 SEQUENCE /// ENTRY CTBPSR #type complete TITLE site-specific DNA-methyltransferase (cytosine-specific) (EC 2.1.1.73) - phage SPR ALTERNATE_NAMES cytosine-specific DNA methylase; cytosine-specific DNA methyltransferase; DNA (cytosine-5)-methyltransferase; DNA cytosine methylase ORGANISM #formal_name phage SPR #note host Bacillus subtilis DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 24-Sep-1999 ACCESSIONS A91516; A93548; S02599; A00558 REFERENCE A91516 !$#authors Buhk, H.J.; Behrens, B.; Tailor, R.; Wilke, K.; Prada, J.J.; !1Gunthert, U.; Noyer-Weidner, M.; Jentsch, S.; Trautner, T.A. !$#journal Gene (1984) 29:51-61 !$#title Restriction and modification in Bacillus subtilis: !1nucleotide sequence, functional organization and product of !1the DNA methyltransferase gene of bacteriophage SPR. !$#cross-references MUID:85028440; PMID:6092231 !$#accession A91516 !'##molecule_type DNA !'##residues 1-439 ##label BUH REFERENCE A93548 !$#authors Posfai, G.; Baldauf, F.; Erdei, S.; Posfai, J.; Venetianer, !1P.; Kiss, A. !$#journal Nucleic Acids Res. (1984) 12:9039-9049 !$#title Structure of the gene coding for the sequence-specific !1DNA-methyltransferase of the Bacillus subtilis phage SPR. !$#cross-references MUID:85087917; PMID:6096817 !$#accession A93548 !'##molecule_type DNA !'##residues 1-412,'A',414-433,'V',435-439 ##label POS !'##cross-references GB:X01670; NID:g14873; PIDN:CAA25829.1; PID:g579089 REFERENCE S02598 !$#authors Wilke, K.; Rauhut, E.; Noyer-Weidner, M.; Lauster, R.; !1Pawlek, B.; Behrens, B.; Trautner, T.A. !$#journal EMBO J. (1988) 7:2601-2609 !$#title Sequential order of target-recognizing domains in !1multispecific DNA-methyltransferases. !$#cross-references MUID:89052677; PMID:3142766 !$#accession S02599 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-296,330-412,'A',414-433,'V',435-439 ##label WIL COMMENT This enzyme methylates the 5' cytosine in the sequence GGCC !1and both cytosines in the sequence CCGG. GENETICS !$#start_codon TTG CLASSIFICATION #superfamily site-specific methyltransferase !1(cytosine-specific) EcoRII KEYWORDS methyltransferase; S-adenosylmethionine SUMMARY #length 439 #molecular-weight 49881 #checksum 3788 SEQUENCE /// ENTRY CTBPRH #type complete TITLE site-specific DNA-methyltransferase (cytosine-specific) (EC 2.1.1.73) - phage rho-11s ALTERNATE_NAMES DNA cytosine methylase; DNA methyltransferase ORGANISM #formal_name phage rho-11s #note host Bacillus subtilis DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 24-Oct-1997 ACCESSIONS A28137 REFERENCE A91063 !$#authors Behrens, B.; Noyer-Weidner, M.; Pawlek, B.; Lauster, R.; !1Balganesh, T.S.; Trautner, T.A. !$#journal EMBO J. (1987) 6:1137-1142 !$#title Organization of multispecific DNA methyltransferases encoded !1by temperate Bacillus subtilis phages. !$#cross-references MUID:87246516; PMID:3109889 !$#accession A28137 !'##molecule_type DNA !'##residues 1-475,'E',477-503 ##label BEH !'##cross-references EMBL:X05242 REFERENCE A94502 !$#authors Trautner, T.A. !$#submission submitted to the EMBL Data Library, September 1987 !$#contents annotation: revision of residue 476 COMMENT This enzyme methylates cytosine within the sequences GGCC !1and GAGCTC. CLASSIFICATION #superfamily site-specific methyltransferase !1(cytosine-specific) EcoRII KEYWORDS methyltransferase; S-adenosylmethionine SUMMARY #length 503 #molecular-weight 57129 #checksum 8732 SEQUENCE /// ENTRY CTBPPT #type complete TITLE site-specific DNA-methyltransferase (cytosine-specific) (EC 2.1.1.73) - phage phi-3T ALTERNATE_NAMES cytosine-specific DNA methylase; cytosine-specific DNA methyltransferase; DNA (cytosine-5)-methyltransferase; DNA cytosine methylase ORGANISM #formal_name phage phi-3T #note host Bacillus subtilis DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 11-Jun-1999 ACCESSIONS A24465; S02598 REFERENCE A24465 !$#authors Tran-Betcke, A.; Behrens, B.; Noyer-Weidner, M.; Trautner, !1T.A. !$#journal Gene (1986) 42:89-96 !$#title DNA methyltransferase genes of Bacillus subtilis phages: !1comparison of their nucleotide sequences. !$#cross-references MUID:86248684; PMID:3087819 !$#accession A24465 !'##molecule_type DNA !'##residues 1-443 ##label TRA !'##cross-references GB:M13488; NID:g215470; PIDN:AAA32352.1; !1PID:g215471 REFERENCE S02598 !$#authors Wilke, K.; Rauhut, E.; Noyer-Weidner, M.; Lauster, R.; !1Pawlek, B.; Behrens, B.; Trautner, T.A. !$#journal EMBO J. (1988) 7:2601-2609 !$#title Sequential order of target-recognizing domains in !1multispecific DNA-methyltransferases. !$#cross-references MUID:89052677; PMID:3142766 !$#accession S02598 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-39,'V',41-91;125-195,'L',197-443 ##label WIL GENETICS !$#start_codon TTG CLASSIFICATION #superfamily site-specific methyltransferase !1(cytosine-specific) EcoRII KEYWORDS methyltransferase; S-adenosylmethionine SUMMARY #length 443 #molecular-weight 50509 #checksum 6305 SEQUENCE /// ENTRY CTYMCS #type complete TITLE site-specific DNA-methyltransferase (cytosine-specific) (EC 2.1.1.73) SssI - Spiroplasma sp. (strain MQ1) ALTERNATE_NAMES CpG DNA methylase SssI; DNA methyltransferase SssI ORGANISM #formal_name Spiroplasma sp. DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 07-Dec-1999 ACCESSIONS S10345 REFERENCE S10345 !$#authors Renbaum, P.; Abrahamove, D.; Fainsod, A.; Wilson, G.; !1Rottem, S.; Razin, A. !$#journal Nucleic Acids Res. (1990) 18:1145-1152 !$#title Cloning, characterization, and expression in Escherichia !1coli of the gene coding for the CpG DNA methylase from !1Spiroplasma sp. strain MQ1 (M.SssI). !$#cross-references MUID:90206772; PMID:2181400 !$#accession S10345 !'##molecule_type DNA !'##residues 1-386 ##label REN !'##cross-references EMBL:X17195; NID:g47552; PIDN:CAA35058.1; !1PID:g47553 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily site-specific methyltransferase !1(cytosine-specific) EcoRII KEYWORDS DNA binding; methyltransferase; restriction modification !1system; S-adenosylmethionine FEATURE !$141 #active_site Cys #status predicted SUMMARY #length 386 #molecular-weight 44312 #checksum 1695 SEQUENCE /// ENTRY XYHIH1 #type complete TITLE site-specific DNA-methyltransferase (cytosine-specific) (EC 2.1.1.73) HhaI - Haemophilus haemolyticus ALTERNATE_NAMES modification methylase HhaI; restriction-modification system HhaI ORGANISM #formal_name Haemophilus haemolyticus DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 11-Jun-1999 ACCESSIONS A26260 REFERENCE A26260 !$#authors Caserta, M.; Zacharias, W.; Nwankwo, D.; Wilson, G.G.; !1Wells, R.D. !$#journal J. Biol. Chem. (1987) 262:4770-4777 !$#title Cloning, sequencing, in vivo promoter mapping, and !1expression in Escherichia coli of the gene for the HhaI !1methyltransferase. !$#cross-references MUID:87165890; PMID:3549710 !$#accession A26260 !'##molecule_type DNA !'##residues 1-327 ##label CAS !'##cross-references GB:J02677; NID:g148948; PIDN:AAA24989.1; !1PID:g148949 COMMENT This site-specific methylase recognizes the tetranucleotide !1GCGC, causes specific modification (methylation) on both !1strands, and protects the DNA from cleavage by HhaI !1endonuclease. COMMENT H. haemolyticus is a gram-negative, rod-shaped parasitic !1bacterium found in mucus membrane of the upper respiratory !1tract of man. CLASSIFICATION #superfamily site-specific methyltransferase !1(cytosine-specific) EcoRII KEYWORDS methyltransferase; restriction modification system; !1S-adenosylmethionine SUMMARY #length 327 #molecular-weight 36996 #checksum 8789 SEQUENCE /// ENTRY CTNHP2 #type complete TITLE site-specific DNA-methyltransferase (cytosine-specific) (EC 2.1.1.73) NgoPII - Neisseria gonorrhoeae ALTERNATE_NAMES M.NgoPII methyltransferase; modification methylase NgoPII ORGANISM #formal_name Neisseria gonorrhoeae DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 11-Jun-1999 ACCESSIONS S00920; S04420 REFERENCE S00920 !$#authors Sullivan, K.M.; Saunders, J.R. !$#journal Nucleic Acids Res. (1988) 16:4369-4387 !$#title Sequence analysis of the NgoPII methyltransferase gene from !1Neisseria gonorrhoeae P9: homologies with other enzymes !1recognizing the sequence 5'-GGCC-3'. !$#cross-references MUID:88247748; PMID:2837733 !$#accession S00920 !'##molecule_type DNA !'##residues 1-341 ##label SUL !'##cross-references EMBL:X06965; NID:g44872; PIDN:CAA30038.1; !1PID:g44873 CLASSIFICATION #superfamily site-specific methyltransferase !1(cytosine-specific) EcoRII KEYWORDS methyltransferase; restriction modification system; !1S-adenosylmethionine FEATURE !$84 #active_site Cys #status predicted SUMMARY #length 341 #molecular-weight 38443 #checksum 3244 SEQUENCE /// ENTRY JS0102 #type complete TITLE site-specific DNA-methyltransferase (cytosine-specific) (EC 2.1.1.73) HaeIII - Haemophilus aegyptius ALTERNATE_NAMES HaeIII modification methylase ORGANISM #formal_name Haemophilus aegyptius DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-May-2000 ACCESSIONS JS0102 REFERENCE JS0102 !$#authors Slatko, B.E.; Croft, R.; Moran, L.S.; Wilson, G.G. !$#journal Gene (1988) 74:45-50 !$#title Cloning and analysis of the HaeIII and HaeII !1methyltransferase genes. !$#cross-references MUID:89252890; PMID:3248732 !$#accession JS0102 !'##molecule_type DNA !'##residues 1-330 ##label SLA !'##cross-references GB:M24625; NID:g148914; PIDN:AAA24970.1; !1PID:g148915 !'##experimental_source ATCC 11116 COMMENT This methyltransferase produces 5-methylcytosine (m5C). It !1specifically catalyzes modification of DNA sequence !15'-GGCC-3' to 5'-GGm5CC-3'. GENETICS !$#gene haeIIIM CLASSIFICATION #superfamily site-specific methyltransferase !1(cytosine-specific) EcoRII KEYWORDS methyltransferase; S-adenosylmethionine SUMMARY #length 330 #molecular-weight 37686 #checksum 8262 SEQUENCE /// ENTRY B42941 #type complete TITLE site-specific DNA-methyltransferase (cytosine-specific) (EC 2.1.1.73) MthTI - Methanobacterium thermoformicicum plasmid ALTERNATE_NAMES modification methylase MthTI; restriction-modification system MthTI ORGANISM #formal_name Methanobacterium thermoformicicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-May-2000 ACCESSIONS B42941; S30310; S26445 REFERENCE A42941 !$#authors Nolling, J.; de Vos, W.M. !$#journal J. Bacteriol. (1992) 174:5719-5726 !$#title Characterization of the archaeal, plasmid-encoded type II !1restriction-modification system MthTI from Methanobacterium !1thermoformicicum THF: homology to the bacterial NgoPII !1system from Neisseria gonorrhoeae. !$#cross-references MUID:92380950; PMID:1512204 !$#accession B42941 !'##status preliminary !'##molecule_type DNA !'##residues 1-330 ##label NOL !'##cross-references GB:M97222; NID:g149741; PIDN:AAA73370.1; !1PID:g149743 !'##experimental_source THF, DSM 3848, pFV1 !'##note sequence extracted from NCBI backbone (NCBIN:112825, !1NCBIP:112830) REFERENCE S30302 !$#authors Noelling, J.; van Eeden, F.J.M.; Eggen, R.I.L.; de Vos, W.M. !$#journal Nucleic Acids Res. (1992) 20:6501-6507 !$#title Modular organization of related Archaeal plasmids encoding !1different restriction-modification systems in !1Methanobacterium thermoformicicum. !$#cross-references MUID:93126090; PMID:1336177 !$#accession S30310 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-330 ##label NOE !'##cross-references EMBL:X68366; NID:g44632; PIDN:CAA48436.1; !1PID:g44641 GENETICS !$#gene TIM !$#genome plasmid CLASSIFICATION #superfamily site-specific methyltransferase !1(cytosine-specific) EcoRII KEYWORDS methyltransferase; S-adenosylmethionine SUMMARY #length 330 #molecular-weight 37360 #checksum 7945 SEQUENCE /// ENTRY XYNHCL #type complete TITLE site-specific DNA-methyltransferase (cytosine-specific) (EC 2.1.1.73) NlaX - Neisseria lactamica ORGANISM #formal_name Neisseria lactamica DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 11-Jun-1999 ACCESSIONS S12037 REFERENCE S12036 !$#authors Labbe, D.; Hoeltke, H.J.; Lau, P.C.K. !$#journal Mol. Gen. Genet. (1990) 224:101-110 !$#title Cloning and characterization of two tandemly arranged DNA !1methyltransferase genes of Neisseria lactamica: an !1adenine-specific M.NlaIII and a cytosine-type methylase. !$#cross-references MUID:91117164; PMID:2277628 !$#accession S12037 !'##molecule_type DNA !'##residues 1-313 ##label LAB !'##cross-references EMBL:X54485; NID:g45002; PIDN:CAA38357.1; !1PID:g45004 CLASSIFICATION #superfamily site-specific methyltransferase !1(cytosine-specific) EcoRII KEYWORDS methyltransferase; S-adenosylmethionine FEATURE !$74 #active_site Cys #status predicted SUMMARY #length 313 #molecular-weight 34842 #checksum 4960 SEQUENCE /// ENTRY XYBSR1 #type complete TITLE site-specific DNA-methyltransferase (cytosine-specific) (EC 2.1.1.73) BsuRI - Bacillus subtilis (strain R) ALTERNATE_NAMES modification methylase BsuRI; restriction-modification system BsuRI ORGANISM #formal_name Bacillus subtilis DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 11-Jun-1999 ACCESSIONS B23488 REFERENCE A93587 !$#authors Kiss, A.; Posfai, G.; Keller, C.C.; Venetianer, P.; Roberts, !1R.J. !$#journal Nucleic Acids Res. (1985) 13:6403-6421 !$#title Nucleotide sequence of the BsuRI restriction-modification !1system. !$#cross-references MUID:86041846; PMID:2997708 !$#accession B23488 !'##molecule_type DNA !'##residues 1-436 ##label KIS !'##cross-references GB:X02988; NID:g40245; PIDN:CAA26731.1; PID:g40247 COMMENT This enzyme in this strain is not found in strain 168. CLASSIFICATION #superfamily site-specific methyltransferase !1(cytosine-specific) EcoRII KEYWORDS methyltransferase; restriction modification system; !1S-adenosylmethionine SUMMARY #length 436 #molecular-weight 49634 #checksum 8824 SEQUENCE /// ENTRY S07792 #type complete TITLE site-specific DNA-methyltransferase (cytosine-specific) (EC 2.1.1.73) BspR - Bacillus sphaericus ORGANISM #formal_name Bacillus sphaericus DATE 18-Feb-1994 #sequence_revision 02-Jul-1998 #text_change 05-May-2000 ACCESSIONS S07792; S48066; A53896 REFERENCE S07792 !$#authors Posfai, G.; Kiss, A.; Erdei, S.; Posfai, J.; Venetianer, P. !$#journal J. Mol. Biol. (1983) 170:597-610 !$#title Structure of the Bacillus sphaericus R modification !1methylase gene. !$#cross-references MUID:84036221; PMID:6313947 !$#accession S07792 !'##molecule_type DNA !'##residues 1-321,'L',323-424 ##label POS !'##cross-references EMBL:X15758; NID:g39985; PIDN:CAA33764.1; !1PID:g39986 !'##note this sequence is revised in S48066 REFERENCE S48066 !$#authors Szilak, L.; Finta, C.; Patthy, A.; Venetianer, P.; Kiss, A. !$#journal Nucleic Acids Res. (1994) 22:2876-2881 !$#title Self-methylation of BspRI DNA-methyltransferase. !$#cross-references MUID:94344739; PMID:8065896 !$#accession S48066 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-424 ##label SZI1 !$#accession A53896 !'##molecule_type protein !'##residues 150-153,'X',155-156,'X',158;181-186 ##label SZI2 !'##note cysteines 156 and 181 were labeled after prolonged exposure to !1radioactive S-adenosylmethionine; cysteine 181 is not !1conserved FUNCTION !$#description catalyzes the methylation of cytosine in a specific DNA !1sequence by S-adenosylmethionine to form 5-methylcytosine !$#note this enzyme acts on cytosine in the third position of a GGCC !1sequence CLASSIFICATION #superfamily site-specific methyltransferase !1(cytosine-specific) EcoRII KEYWORDS autophosphorylation; methylated amino acid; !1methyltransferase; S-adenosylmethionine FEATURE !$156 #active_site Cys (methylcysteine intermediate) !8#status experimental SUMMARY #length 424 #molecular-weight 48241 #checksum 7307 SEQUENCE /// ENTRY CTBSFI #type complete TITLE site-specific DNA-methyltransferase (cytosine-specific) (EC 2.1.1.73) BsuFI - Bacillus subtilis (strain ISF18) ORGANISM #formal_name Bacillus subtilis DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 11-Jun-1999 ACCESSIONS S09247 REFERENCE S09247 !$#authors Walter, J.; Noyer-Weidner, M.; Trautner, T.A. !$#journal EMBO J. (1990) 9:1007-1013 !$#title The amino acid sequence of the CCGG recognizing DNA !1methyltransferase M.BsuFI: implications for the analysis of !1sequence recognition by cytosine DNA methyltransferases. !$#cross-references MUID:90214606; PMID:2108858 !$#accession S09247 !'##molecule_type DNA !'##residues 1-409 ##label WAL !'##cross-references EMBL:X51515; NID:g39983; PIDN:CAA35888.1; !1PID:g39984 COMMENT This enzyme in this strain is not found in strain 168. CLASSIFICATION #superfamily site-specific methyltransferase !1(cytosine-specific) EcoRII KEYWORDS methyltransferase; restriction modification system; !1S-adenosylmethionine FEATURE !$170 #active_site Cys #status predicted SUMMARY #length 409 #molecular-weight 46911 #checksum 3194 SEQUENCE /// ENTRY CTKEMM #type complete TITLE site-specific DNA-methyltransferase (cytosine-specific) (EC 2.1.1.73) MspI - Moraxella sp. ALTERNATE_NAMES cytosine methylase MspI ORGANISM #formal_name Moraxella sp. DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 11-Jun-1999 ACCESSIONS S04188 REFERENCE S04187 !$#authors Lin, P.M.; Lee, C.H.; Roberts, R.J. !$#journal Nucleic Acids Res. (1989) 17:3001-3011 !$#title Cloning and characterization of the genes encoding the MspI !1restriction modification system. !$#cross-references MUID:89263712; PMID:2471145 !$#accession S04188 !'##molecule_type DNA !'##residues 1-418 ##label LIN !'##cross-references EMBL:X14191; NID:g44538; PIDN:CAA32393.1; !1PID:g44539 !'##note part of this sequence was confirmed by protein sequencing CLASSIFICATION #superfamily site-specific methyltransferase !1(cytosine-specific) EcoRII KEYWORDS methyltransferase; restriction modification system; !1S-adenosylmethionine FEATURE !$174 #active_site Cys #status predicted SUMMARY #length 418 #molecular-weight 47656 #checksum 6471 SEQUENCE /// ENTRY XYECR2 #type complete TITLE site-specific DNA-methyltransferase (cytosine-specific) (EC 2.1.1.73) EcoRII - Escherichia coli (strain HB101) ALTERNATE_NAMES C-5 cytosine-specific DNA methylase; modification methylase EcoRII ORGANISM #formal_name Escherichia coli #variety strain HB101 DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 11-Jun-1999 ACCESSIONS A25871 REFERENCE A25871 !$#authors Som, S.; Bhagwat, A.S.; Friedman, S. !$#journal Nucleic Acids Res. (1987) 15:313-332 !$#title Nucleotide sequence and expression of the gene encoding the !1EcoRII modification enzyme. !$#cross-references MUID:87146340; PMID:3029675 !$#accession A25871 !'##molecule_type DNA !'##residues 1-477 ##label SOM !'##cross-references GB:X05050; NID:g41316; PIDN:CAA28725.1; PID:g41317 !'##experimental_source strain HB101 FUNCTION !$#description catalyzes methylation of the internal cytosine residue in !1the CCWGG pentanucleotide and protects the DNA from cleavage !1by its own restriction enzyme CLASSIFICATION #superfamily site-specific methyltransferase !1(cytosine-specific) EcoRII KEYWORDS methyltransferase; restriction modification system; !1S-adenosylmethionine SUMMARY #length 477 #molecular-weight 54556 #checksum 7022 SEQUENCE /// ENTRY CTBSBA #type complete TITLE site-specific DNA-methyltransferase (cytosine-specific) (EC 2.1.1.73) BanI - Bacillus aneurinolyticus ORGANISM #formal_name Bacillus aneurinolyticus DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jun-2000 ACCESSIONS JS0489; A38796 REFERENCE JS0489 !$#authors Maekawa, Y.; Yasukawa, H.; Kawakami, B. !$#journal J. Biochem. (1990) 107:645-649 !$#title Cloning and nucleotide sequences of the BanI !1restriction-modification genes in Bacillus aneurinolyticus. !$#cross-references MUID:90292998; PMID:2358438 !$#accession JS0489 !'##molecule_type DNA !'##residues 1-428 ##label MAE !'##cross-references GB:D00704; NID:g216240; PIDN:BAA00613.1; !1PID:g216242 !'##experimental_source strain IAM1077 !$#accession A38796 !'##molecule_type protein !'##residues 1-15 ##label MAE2 CLASSIFICATION #superfamily site-specific methyltransferase !1(cytosine-specific) EcoRII KEYWORDS methyltransferase; restriction modification system; !1S-adenosylmethionine FEATURE !$1-428 #product site-specific methyltransferase !8(cytosine-specific) BanI #status experimental #label !8MAT\ !$76 #active_site Cys #status predicted SUMMARY #length 428 #molecular-weight 48618 #checksum 1235 SEQUENCE /// ENTRY A46355 #type complete TITLE site-specific DNA-methyltransferase (cytosine-specific) (EC 2.1.1.73) - Chlorella virus IL-3A ALTERNATE_NAMES cytosine-specific DNA methylase; cytosine-specific DNA methyltransferase; DNA cytosine methylase ORGANISM #formal_name Chlorella virus IL-3A DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 11-Jun-1999 ACCESSIONS A46355 REFERENCE A46355 !$#authors Shields, S.L.; Burbank, D.E.; Grabherr, R.; van Etten, J.L. !$#journal Virology (1990) 176:16-24 !$#title Cloning and sequencing the cytosine methyltransferase gene !1M.CviJI from Chlorella virus IL-3A. !$#cross-references MUID:90232725; PMID:2158687 !$#accession A46355 !'##molecule_type DNA !'##residues 1-367 ##label SHI !'##cross-references GB:M27265; NID:g323314; PIDN:AAA88826.1; !1PID:g323315 CLASSIFICATION #superfamily site-specific methyltransferase !1(cytosine-specific) EcoRII KEYWORDS methyltransferase; restriction modification system; !1S-adenosylmethionine FEATURE !$73 #active_site Cys #status predicted SUMMARY #length 367 #molecular-weight 41860 #checksum 4725 SEQUENCE /// ENTRY C64580 #type complete TITLE site-specific DNA-methyltransferase (cytosine-specific) (EC 2.1.1.73) HP0483 - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-May-2000 ACCESSIONS C64580 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession C64580 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-328 ##label TOM !'##cross-references GB:AE000511; TIGR:HP0483 CLASSIFICATION #superfamily DNA methyltransferase (cytosine-specific) KEYWORDS methyltransferase; S-adenosylmethionine SUMMARY #length 328 #molecular-weight 37197 #checksum 8513 SEQUENCE /// ENTRY C64526 #type complete TITLE site-specific DNA-methyltransferase (cytosine-specific) (EC 2.1.1.73) HP0051 - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-May-2000 ACCESSIONS C64526 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession C64526 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-355 ##label TOM !'##cross-references GB:AE000526; GB:AE000511; NID:g2313116; !1PIDN:AAD07117.1; PID:g2313124; TIGR:HP0051 CLASSIFICATION #superfamily DNA methyltransferase (cytosine-specific) KEYWORDS methyltransferase; S-adenosylmethionine SUMMARY #length 355 #molecular-weight 39791 #checksum 7846 SEQUENCE /// ENTRY S70707 #type complete TITLE site-specific DNA-methyltransferase (cytosine-specific) (EC 2.1.1.73) HphI - Haemophilus parahaemolyticus (ATCC 49700) ORGANISM #formal_name Haemophilus parahaemolyticus #variety ATCC 49700 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-May-2000 ACCESSIONS S70707; S53120 REFERENCE S70707 !$#authors Lubys, A.; Lubiene, J.; Kulakauskas, S.; Stankevicius, K.; !1Timinskas, A.; Janulaitis, A. !$#journal Nucleic Acids Res. (1996) 24:2760-2766 !$#title Cloning and analysis of the genes encoding the type IIS !1restriction-modification system HphI from Haemophilus !1parahaemolyticus. !$#cross-references MUID:96313243; PMID:8759008 !$#accession S70707 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-372 ##label LUB !'##cross-references EMBL:X85374; NID:g732728; PIDN:CAA59690.1; !1PID:g732729 !'##experimental_source ATCC 49700 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1March 1995 GENETICS !$#gene hphIM(C) CLASSIFICATION #superfamily DNA methyltransferase (cytosine-specific) KEYWORDS methyltransferase; restriction modification system; !1S-adenosylmethionine SUMMARY #length 372 #molecular-weight 42248 #checksum 9449 SEQUENCE /// ENTRY XYOFS #type complete TITLE site-specific DNA-methyltransferase (adenine-specific) (EC 2.1.1.72) PstI - Providencia stuartii ALTERNATE_NAMES modification methylase PstI; restriction-modification system PstI ORGANISM #formal_name Providencia stuartii DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 05-May-2000 ACCESSIONS A00553 REFERENCE A92485 !$#authors Walder, R.Y.; Walder, J.A.; Donelson, J.E. !$#journal J. Biol. Chem. (1984) 259:8015-8026 !$#title The organization and complete nucleotide sequence of the !1PstI restriction-modification system. !$#cross-references MUID:84239756; PMID:6330092 !$#accession A00553 !'##molecule_type DNA !'##residues 1-507 ##label WAL !'##cross-references GB:K02081; NID:g150922; PIDN:AAA25672.1; !1PID:g455323 !'##experimental_source strain 164 !'##note the authors translated the codon CAA for residue 456 as Glu COMMENT Providencia, a genus of enterobacteriacean rods, is !1sometimes included in the genus Proteus. FUNCTION MET !$#description This site-specific methylase recognizes the double-stranded !1hexanucleotide 5'-CTGCAG and causes specific modification !1(methylation) on both strands; it protects the DNA from !1cleavage by PstI endonuclease (see PIR:NDOFS). CLASSIFICATION #superfamily site-specific DNA-methyltransferase !1(adenine-specific) PstI KEYWORDS methyltransferase; S-adenosylmethionine SUMMARY #length 507 #molecular-weight 56877 #checksum 2377 SEQUENCE /// ENTRY S35515 #type complete TITLE site-specific DNA-methyltransferase (adenine-specific) (EC 2.1.1.72) - Bacillus subtilis (strain ISB8) ALTERNATE_NAMES modification methyltransferase BsuBI; site-specific DNA-methyltransferase BsuBI ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-May-2000 ACCESSIONS S35515; S36924 REFERENCE S35515 !$#authors Xu, G.L.; Kapfer, W.; Walter, J.; Trautner, T.A. !$#journal Nucleic Acids Res. (1992) 20:6517-6523 !$#title BsuBI-an isospecific restriction and modification system of !1PstI: characterization of the BsuBI genes and enzymes. !$#cross-references MUID:93126092; PMID:1480472 !$#accession S35515 !'##molecule_type DNA !'##residues 1-501 ##label XUG !'##cross-references EMBL:L01541 !'##experimental_source strain ISB8 !'##note part of this sequence was confirmed by protein sequencing REFERENCE S36924 !$#authors Birkenbihl, R.P.; Subramani, S. !$#submission submitted to the EMBL Data Library, September 1992 !$#accession S36924 !'##molecule_type DNA !'##residues 1-495,'N',497-501 ##label BIR !'##cross-references EMBL:L01541; NID:g143053; PIDN:AAA18169.1; !1PID:g143054 COMMENT This site-specific methylase recognizes the double-stranded !1hexanucleotide 5'-CTGCAG and causes specific modification !1(methylation) on both strands; it protects the DNA from !1cleavage by the BsuBI (or PstI) endonuclease (see !1PIR:S35516). CLASSIFICATION #superfamily site-specific DNA-methyltransferase !1(adenine-specific) PstI KEYWORDS methyltransferase; restriction modification system; !1S-adenosylmethionine SUMMARY #length 501 #molecular-weight 57170 #checksum 5975 SEQUENCE /// ENTRY XUECAD #type complete TITLE methylated-DNA-[protein]-cysteine S-methyltransferase (EC 2.1.1.63) [similarity] - Escherichia coli (strain K-12) ALTERNATE_NAMES O(6)-alkylguanine-DNA alkyltransferase; O (6)-methylguanine-DNA alkyltransferase; O-methylguanine-DNA methyltransferase ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 21-Nov-1997 #text_change 05-Jan-2003 ACCESSIONS B64883; A27276 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64883 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-171 ##label BLAT !'##cross-references GB:AE000231; GB:U00096; NID:g1787588; !1PIDN:AAC74417.1; PID:g1787596; UWGP:b1335 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A27276 !$#authors Potter, P.M.; Wilkinson, M.C.; Fitton, J.; Carr, F.J.; !1Brennand, J.; Cooper, D.P.; Margison, G.P. !$#journal Nucleic Acids Res. (1987) 15:9177-9193 !$#title Characterisation and nucleotide sequence of ogt, the O !1(6)-alkylguanine-DNA-alkyltransferase gene of E. coli. !$#cross-references MUID:88067749; PMID:2825131 !$#accession A27276 !'##molecule_type DNA !'##residues 1-36,'A',38-67,'D',69-171 ##label POT !'##cross-references GB:Y00495; NID:g42157; PIDN:CAA68548.1; PID:g42158 GENETICS !$#gene ogt FUNCTION !$#description DNA-repair enzyme; catalyzes transfer of the alkyl group !1from O(6)-alkylguanine in DNA to a cysteine residue in the !1enzyme itself and causes irreversible autoinactivation of !1the enzyme CLASSIFICATION #superfamily methylated-DNA-protein-cysteine !1S-methyltransferase; methylated-DNA-protein-cysteine !1S-methyltransferase homology KEYWORDS DNA repair; methylated amino acid; methyltransferase FEATURE !$86-166 #domain methylated-DNA-protein-cysteine !8S-methyltransferase homology #label MGT\ !$139 #binding_site methyl (Cys) (covalent) #status !8predicted SUMMARY #length 171 #molecular-weight 19179 #checksum 1277 SEQUENCE /// ENTRY XUBSMB #type complete TITLE methylated-DNA-[protein]-cysteine S-methyltransferase (EC 2.1.1.63) [similarity] - Bacillus subtilis ALTERNATE_NAMES O(6)-alkylguanine-DNA alkyltransferase; O (6)-methylguanine-DNA alkyltransferase; O-methylguanine-DNA methyltransferase ORGANISM #formal_name Bacillus subtilis DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 05-Jan-2003 ACCESSIONS S11564; G69582 REFERENCE S11483 !$#authors Morohoshi, F.; Hayashi, K.; Munakata, N. !$#journal Nucleic Acids Res. (1990) 18:5473-5480 !$#title Bacillus subtilis ada operon encodes two DNA !1alkyltransferases. !$#cross-references MUID:91016831; PMID:2120677 !$#accession S11564 !'##molecule_type DNA !'##residues 1-179 ##label MOR !'##cross-references EMBL:X53399; NID:g39786; PIDN:CAA37476.1; !1PID:g39788 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69582 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-179 ##label KUN !'##cross-references GB:Z99104; GB:Z99105; GB:AL009126; NID:g2632457; !1PIDN:CAB11975.1; PID:g2632467; NID:g2632267; PID:g2632449 !'##experimental_source strain 168 GENETICS !$#gene adaB CLASSIFICATION #superfamily methylated-DNA-protein-cysteine !1S-methyltransferase; methylated-DNA-protein-cysteine !1S-methyltransferase homology KEYWORDS DNA repair; methylated amino acid; methyltransferase FEATURE !$88-168 #domain methylated-DNA-protein-cysteine !8S-methyltransferase homology #label MGT\ !$141 #binding_site methyl (Cys) (covalent) #status !8predicted SUMMARY #length 179 #molecular-weight 20124 #checksum 1085 SEQUENCE /// ENTRY XUBSM1 #type complete TITLE methylated-DNA-[protein]-cysteine S-methyltransferase (EC 2.1.1.63) [similarity] - Bacillus subtilis ALTERNATE_NAMES O(6)-alkylguanine-DNA alkyltransferase; O (6)-methylguanine-DNA alkyltransferase; O-methylguanine-DNA methyltransferase ORGANISM #formal_name Bacillus subtilis DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 05-Jan-2003 ACCESSIONS S04877; A60649; C69613 REFERENCE S04877 !$#authors Morohoshi, F.; Hayashi, K.; Munakata, N. !$#journal Nucleic Acids Res. (1989) 17:6531-6543 !$#title Bacillus subtilis gene coding for constitutive O !1(6)-methylguanine-DNA alkyltransferase. !$#cross-references MUID:89385980; PMID:2506524 !$#accession S04877 !'##molecule_type DNA !'##residues 1-165 ##label MOR !'##cross-references EMBL:X15659; NID:g39875; PIDN:CAA33694.1; !1PID:g39876 REFERENCE A60649 !$#authors Kodama, K.; Nakabeppu, Y.; Sekiguchi, M. !$#journal Mutat. Res. (1989) 218:153-163 !$#title Cloning and expression of the Bacillus subtilis !1methyltransferase gene in Escherichia coli ada- cells. !$#cross-references MUID:89364938; PMID:2505068 !$#accession A60649 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-165 ##label KOD REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69613 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-165 ##label KUN !'##cross-references GB:Z99111; GB:AL009126; NID:g2633699; !1PIDN:CAB13227.1; PID:g2633725 !'##experimental_source strain 168 GENETICS !$#gene dat; dat1 CLASSIFICATION #superfamily methylated-DNA-protein-cysteine !1S-methyltransferase; methylated-DNA-protein-cysteine !1S-methyltransferase homology KEYWORDS DNA repair; methylated amino acid; methyltransferase FEATURE !$77-158 #domain methylated-DNA-protein-cysteine !8S-methyltransferase homology #label MGT\ !$130 #binding_site methyl (Cys) (covalent) #status !8predicted SUMMARY #length 165 #molecular-weight 18752 #checksum 1737 SEQUENCE /// ENTRY XUBYMC #type complete TITLE methylated-DNA-[protein]-cysteine S-methyltransferase (EC 2.1.1.63) [similarity] - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES DNA repair methyltransferase; O(4)-methylthymine-DNA alkyltransferase; O(6)-alkylguanine-DNA alkyltransferase; O (6)-methylguanine-DNA alkyltransferase; O (6)-methylguanine-DNA methyltransferase; protein D1204; protein YDL200c ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1993 #sequence_revision 10-Nov-1995 #text_change 05-Jan-2003 ACCESSIONS S29370; S16713; S58777; S67759; S67755; S72060 REFERENCE S29370 !$#authors Xiao, W.; Samson, L. !$#journal Nucleic Acids Res. (1992) 20:3599-3606 !$#title The Saccharomyces cerevisiae MGT1 DNA repair !1methyltransferase gene: its promoter and entire coding !1sequence, regulation and in vivo biological functions. !$#cross-references MUID:92350658; PMID:1641326 !$#accession S29370 !'##molecule_type DNA !'##residues 1-206 ##label XIA !'##cross-references EMBL:M94227; NID:g171948; PIDN:AAA34780.1; !1PID:g171949 !'##experimental_source strain DBY747 REFERENCE S16713 !$#authors Xiao, W.; Derfler, B.; Chen, J.; Samson, L. !$#journal EMBO J. (1991) 10:2179-2186 !$#title Primary sequence and biological functions of a Saccharomyces !1cerevisiae O(6)-methylguanine/O(4)-methylthymine DNA repair !1methyltransferase gene. !$#cross-references MUID:91293093; PMID:2065659 !$#accession S16713 !'##molecule_type DNA !'##residues 13-206 ##label XI2 !'##cross-references EMBL:X60368 !'##experimental_source strain DBY747 REFERENCE S58777 !$#authors Verhasselt, P.; Voet, M.; Volckaert, G. !$#submission submitted to the EMBL Data Library, December 1994 !$#accession S58777 !'##molecule_type DNA !'##residues 19-152 ##label VER !'##cross-references EMBL:X83276 REFERENCE S67756 !$#authors Schmidt, E.R.; Bahr, A.; Kraemer, C.; Hankeln, T.; !1Moeller-Rieker, S. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67759 !'##molecule_type DNA !'##residues 1-206 ##label SCH !'##cross-references EMBL:Z74248; NID:g1431329; PIDN:CAA98778.1; !1PID:g1431330; GSPDB:GN00004; MIPS:YDL200c !'##experimental_source strain S288C REFERENCE S67735 !$#authors Volckaert, G.; Verhasselt, P.; Voet, M. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67755 !'##molecule_type DNA !'##residues 1-152 ##label VOL !'##cross-references EMBL:Z74248; GSPDB:GN00004; MIPS:YDL200c !'##experimental_source strain S288C REFERENCE S72060 !$#authors Verhasselt, P.; Voet, M.; Mathys, J.; Volckaert, G. !$#journal Yeast (1996) 12:1065-1070 !$#title The sequence of 23 kb surrounding the SNF3 locus on the left !1arm of yeast chromosome IV reveals the location of five !1known genes and characterizes at least six new open reading !1frames including putative genes for ribosomal protein L35 !1and a sugar transport protein. !$#cross-references MUID:97051595; PMID:8896272 !$#accession S72060 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 19-152 ##label VEW !'##cross-references EMBL:X83276 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1994 GENETICS !$#gene SGD:MGT1; MIPS:YDL200c !'##cross-references MIPS:YDL200c; SGD:S0002359 !$#map_position 4L FUNCTION !$#description DNA repair; methyltransferase; removes methyl groups from O !1(6)-methylguanine; removes methyl groups from O !1(4)-methylthymine CLASSIFICATION #superfamily methylated-DNA-protein-cysteine !1S-methyltransferase; methylated-DNA-protein-cysteine !1S-methyltransferase homology KEYWORDS DNA repair; methylated amino acid; methyltransferase FEATURE !$116-196 #domain methylated-DNA-protein-cysteine !8S-methyltransferase homology #label MGT\ !$169 #binding_site methyl (Cys) (covalent) #status !8predicted SUMMARY #length 206 #molecular-weight 23579 #checksum 3886 SEQUENCE /// ENTRY XUHUMC #type complete TITLE methylated-DNA-[protein]-cysteine S-methyltransferase (EC 2.1.1.63) [similarity] - human ALTERNATE_NAMES O(6)-alkylguanine-DNA alkyltransferase; O (6)-methylguanine-DNA alkyltransferase; O-methylguanine-DNA methyltransferase ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 05-Jan-2003 ACCESSIONS A34889; S10642; A35310; A35799; A39095; S12646 REFERENCE A34889 !$#authors Tano, K.; Shiota, S.; Collier, J.; Foote, R.S.; Mitra, S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:686-690 !$#title Isolation and structural characterization of a cDNA clone !1encoding the human DNA repair protein for O(6)-alkylguanine. !$#cross-references MUID:90138892; PMID:2405387 !$#accession A34889 !'##molecule_type mRNA !'##residues 1-207 ##label TAN !'##cross-references GB:M29971; NID:g187588; PIDN:AAA59596.1; !1PID:g307199 REFERENCE S10642 !$#authors Hayakawa, H.; Koike, G.; Sekiguchi, M. !$#journal J. Mol. Biol. (1990) 213:739-747 !$#title Expression and cloning of complementary DNA for a human !1enzyme that repairs O(6)-methylguanine in DNA. !$#cross-references MUID:90294292; PMID:2359121 !$#accession S10642 !'##molecule_type mRNA !'##residues 1-207 ##label HAY !'##cross-references GB:X54228; NID:g34558; PIDN:CAA38137.1; PID:g34559 REFERENCE A35310 !$#authors Rydberg, B.; Spurr, N.; Karran, P. !$#journal J. Biol. Chem. (1990) 265:9563-9569 !$#title cDNA cloning and chromosomal assignment of the human O !1(6)-methylguanine-DNA methyltransferase. cDNA expression in !1Escherichia coli and gene expression in human cells. !$#cross-references MUID:90264461; PMID:2188979 !$#accession A35310 !'##molecule_type mRNA !'##residues 1-126,'T',128-207 ##label RYD !'##cross-references GB:M31767; NID:g181615; PIDN:AAA52317.1; !1PID:g181616 REFERENCE A35799 !$#authors Koike, G.; Maki, H.; Takeya, H.; Hayakawa, H.; Sekiguchi, M. !$#journal J. Biol. Chem. (1990) 265:14754-14762 !$#title Purification, structure, and biochemical properties of human !1O(6)-methylguanine-DNA methyltransferase. !$#cross-references MUID:90368638; PMID:2394694 !$#accession A35799 !'##molecule_type protein !'##residues 9-23,'X',25-28,'X',30-61,'X',63-66;108-124,'X',126-134,'X', !1136-144;166-207 ##label KOI REFERENCE A39095 !$#authors von Wronski, M.A.; Shiota, S.; Tano, K.; Mitra, S.; Bigner, !1D.D.; Brent, T.P. !$#journal J. Biol. Chem. (1991) 266:1064-1070 !$#title Structural and immunological comparison of indigenous human !1O(6)-methylguanine-DNA methyltransferase with that encoded !1by a cloned cDNA. !$#cross-references MUID:91093213; PMID:1985934 !$#accession A39095 !'##molecule_type protein !'##residues !18-23;25-28;31-32;37-57;59;61;63-64;66-81;130-144;146-149; !1151-155 ##label VON REFERENCE S12646 !$#authors Major, G.N.; Gardner, E.J.; Carne, A.F.; Lawley, P.D. !$#journal Nucleic Acids Res. (1990) 18:1351-1359 !$#title Purification to homogeneity and partial amino acid sequence !1of a fragment which includes the methyl acceptor site of the !1human DNA repair protein for O(6)-methylguanine. !$#cross-references MUID:90221855; PMID:2109306 !$#accession S12646 !'##molecule_type protein !'##residues 'VD',133-139,'X',141,'A',143-145 ##label MAJ GENETICS !$#gene GDB:MGMT !'##cross-references GDB:125264; OMIM:156569 !$#map_position 10q26-10q26 FUNCTION !$#description this unusual DNA repair protein transfers a methyl group of !16-O-methylguanine in damaged DNA to its own methyl-accepting !1Cys residue in a suicide reaction that blocks further !1activity CLASSIFICATION #superfamily methylated-DNA-protein-cysteine !1S-methyltransferase; methylated-DNA-protein-cysteine !1S-methyltransferase homology KEYWORDS DNA repair; methylated amino acid; methyltransferase FEATURE !$91-172 #domain methylated-DNA-protein-cysteine !8S-methyltransferase homology #label MGT\ !$145 #binding_site methyl (Cys) (covalent) #status !8experimental SUMMARY #length 207 #molecular-weight 21646 #checksum 5937 SEQUENCE /// ENTRY XURTMC #type complete TITLE methylated-DNA-[protein]-cysteine S-methyltransferase (EC 2.1.1.63) [similarity] - rat ALTERNATE_NAMES O(6)-alkylguanine-DNA alkyltransferase; O (6)-methylguanine-DNA alkyltransferase; O-methylguanine-DNA methyltransferase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 05-Jan-2003 ACCESSIONS JN0071; A61217; S33698; S40636 REFERENCE JN0071 !$#authors Rahden-Staron, I.; Laval, F. !$#journal Biochem. Biophys. Res. Commun. (1991) 177:597-602 !$#title cDNA cloning of the rat !1O6-methylguanine-DNA-methyltransferase. !$#cross-references MUID:91264819; PMID:2049083 !$#accession JN0071 !'##molecule_type mRNA !'##residues 1-209 ##label RAH !'##cross-references GB:M76704; NID:g206684; PIDN:AAA42052.1; !1PID:g206685 REFERENCE A61217 !$#authors Potter, P.M.; Rafferty, J.A.; Cawkwell, L.; Wilkinson, M.C.; !1Cooper, D.P.; O'Connor, P.J.; Margison, G.P. !$#journal Carcinogenesis (1991) 12:727-733 !$#title Isolation and cDNA cloning of a rat O !1(6)-alkylguanine-DNA-alkyltransferase gene, molecular !1analysis of expression in rat liver. !$#cross-references MUID:91191734; PMID:2013136 !$#accession A61217 !'##molecule_type mRNA !'##residues 1-209 ##label POT1 REFERENCE S33698 !$#authors Potter, P.M.; Harris, L.C.; Remack, J.S.; Edwards, C.C.; !1Brent, T.P. !$#journal Cancer Res. (1993) 53:1731-1734 !$#title Ribozyme-mediated modulation of human O(6)-methylguanine-DNA !1methyltransferase expression. !$#cross-references MUID:93223177; PMID:8467487 !$#accession S33698 !'##status preliminary !'##molecule_type mRNA !'##residues 1-209 ##label POT2 !'##cross-references EMBL:X54862; NID:g311908; PIDN:CAA38648.1; !1PID:g311909 REFERENCE S40636 !$#authors Sakumi, K.; Shiraishi, A.; Hayakawa, H.; Sekiguchi, M. !$#journal Nucleic Acids Res. (1991) 19:5597-5601 !$#title Cloning and expression of cDNA for rat O !1(6)-methylguanine-DNA methyltransferase. !$#cross-references MUID:92051302; PMID:1945835 !$#accession S40636 !'##status preliminary !'##molecule_type mRNA !'##residues 1-209 ##label SAK !'##cross-references GB:S61804; NID:g238092; PIDN:AAB20187.1; !1PID:g238093 CLASSIFICATION #superfamily methylated-DNA-protein-cysteine !1S-methyltransferase; methylated-DNA-protein-cysteine !1S-methyltransferase homology KEYWORDS DNA repair; methylated amino acid; methyltransferase FEATURE !$95-177 #domain methylated-DNA-protein-cysteine !8S-methyltransferase homology #label MGT\ !$149 #binding_site methyl (Cys) (covalent) #status !8predicted SUMMARY #length 209 #molecular-weight 22244 #checksum 3668 SEQUENCE /// ENTRY XUHYMC #type complete TITLE methylated-DNA-[protein]-cysteine S-methyltransferase (EC 2.1.1.63) [similarity] - black-bellied hamster ALTERNATE_NAMES O(6)-alkylguanine-DNA alkyltransferase; O (6)-methylguanine-DNA alkyltransferase; O-methylguanine-DNA methyltransferase ORGANISM #formal_name Cricetus cricetus #common_name black-bellied hamster DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 05-Jan-2003 ACCESSIONS S22650 REFERENCE S22650 !$#authors Rafferty, J.A.; Elder, R.H.; Watson, A.J.; Cawkwell, L.; !1Potter, P.M.; Margison, G.P. !$#journal Nucleic Acids Res. (1992) 20:1891-1895 !$#title Isolation and partial characterisation of a Chinese hamster !1O(6)-alkylguanine-DNA alkyltransferase cDNA. !$#cross-references MUID:92253409; PMID:1579490 !$#accession S22650 !'##molecule_type mRNA !'##residues 1-209 ##label RAF !'##cross-references EMBL:X65081; NID:g49424; PIDN:CAA46209.1; !1PID:g49425 CLASSIFICATION #superfamily methylated-DNA-protein-cysteine !1S-methyltransferase; methylated-DNA-protein-cysteine !1S-methyltransferase homology KEYWORDS DNA repair; methylated amino acid; methyltransferase FEATURE !$95-177 #domain methylated-DNA-protein-cysteine !8S-methyltransferase homology #label MGT\ !$149 #binding_site methyl (Cys) (covalent) #status !8predicted SUMMARY #length 209 #molecular-weight 22333 #checksum 3229 SEQUENCE /// ENTRY XUBSMM #type complete TITLE methylphosphotriester-DNA alkyltransferase (EC 2.1.1.-) / adaAB operon transcription activator adaA - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jun-2000 ACCESSIONS S11483; F69582 REFERENCE S11483 !$#authors Morohoshi, F.; Hayashi, K.; Munakata, N. !$#journal Nucleic Acids Res. (1990) 18:5473-5480 !$#title Bacillus subtilis ada operon encodes two DNA !1alkyltransferases. !$#cross-references MUID:91016831; PMID:2120677 !$#accession S11483 !'##molecule_type DNA !'##residues 1-211 ##label MOR !'##cross-references EMBL:X53399; NID:g39786; PIDN:CAA37475.1; !1PID:g39787 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69582 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-211 ##label KUN !'##cross-references GB:Z99104; GB:Z99105; GB:AL009126; NID:g2632457; !1PIDN:CAB11974.1; PID:g2632466; NID:g2632267; PID:g2632448 !'##experimental_source strain 168 GENETICS !$#gene adaA CLASSIFICATION #superfamily methylphosphotriester-DNA methyltransferase; !1methylphosphotriester-DNA methyltransferase homology KEYWORDS DNA binding; DNA repair; methyltransferase; transcription !1regulation FEATURE !$23-207 #domain methylphosphotriester-DNA methyltransferase !8homology #label MPT SUMMARY #length 211 #molecular-weight 24299 #checksum 8255 SEQUENCE /// ENTRY XYECO2 #type complete TITLE methylated-DNA-[protein]-cysteine S-methyltransferase (EC 2.1.1.63) - Escherichia coli (strain K-12) CONTAINS methylated-DNA-protein-cysteine S-methyltransferase (EC 2.1.1.63) ada; methylphosphotriester-DNA methyltransferase ORGANISM #formal_name Escherichia coli DATE 28-Dec-1987 #sequence_revision 05-Dec-1997 #text_change 03-Jun-2002 ACCESSIONS C64991; A22630; A22667; I41114; I41115 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64991 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-354 ##label BLAT !'##cross-references GB:AE000310; GB:U00096; NID:g2367131; !1PIDN:AAC75273.1; PID:g1788542; UWGP:b2213 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A22630 !$#authors Nakabeppu, Y.; Kondo, H.; Kawabata, S.; Iwanaga, S.; !1Sekiguchi, M. !$#journal J. Biol. Chem. (1985) 260:7281-7288 !$#title Purification and structure of the intact Ada regulatory !1protein of Escherichia coli K12, O(6)-methylguanine-DNA !1methyltransferase. !$#cross-references MUID:85207761; PMID:2987251 !$#accession A22630 !'##molecule_type DNA !'##residues 1-133,'R',135-354 ##label NAK !'##cross-references GB:M10211; NID:g145188; PIDN:AAA23412.1; !1PID:g145189 !'##experimental_source strain K12 REFERENCE A22667 !$#authors Demple, B.; Sedgwick, B.; Robins, P.; Totty, N.; Waterfield, !1M.D.; Lindahl, T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:2688-2692 !$#title Active site and complete sequence of the suicidal !1methyltransferase that counters alkylation mutagenesis. !$#cross-references MUID:85190562; PMID:3887409 !$#accession A22667 !'##molecule_type DNA !'##residues 1-74,'D',76-78,'PR',81-317,'V',319-329,'S',331-354 ##label !1DEM !'##cross-references GB:M10315; NID:g145190; PIDN:AAA23413.1; !1PID:g145191 !'##experimental_source strain B/r REFERENCE I41114 !$#authors Nakabeppu, Y.; Sekiguchi, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:6297-6301 !$#title Regulatory mechanisms for induction of synthesis of repair !1enzymes in response to alkylating agents: Ada protein acts !1as a transcriptional regulator. !$#cross-references MUID:86313568; PMID:3529081 !$#accession I41114 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-27 ##label RES !'##cross-references GB:M13828; NID:g145196; PIDN:AAA23417.1; !1PID:g145197 REFERENCE I41115 !$#authors Teo, I.; Sedgwick, B.; Kilpatrick, M.W.; McCarthy, T.V.; !1Lindahl, T. !$#journal Cell (1986) 45:315-324 !$#title The intracellular signal for induction of resistance to !1alkylating agents in e. coli. !$#cross-references MUID:86189944; PMID:3009022 !$#accession I41115 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-29 ##label RE2 !'##cross-references GB:M13155; NID:g145198; PIDN:AAA23418.1; !1PID:g145199 COMMENT This enzyme has an inducible DNA repair system that protects !1against methylating and alkylating agents by transferring !1the alkyl group from O(6)-alkylguanine in DNA to a cysteine !1residue located within the enzyme itself. GENETICS !$#gene ada !$#map_position 48 min CLASSIFICATION #superfamily adaptive response regulatory protein; !1methylated-DNA-protein-cysteine S-methyltransferase !1homology; methylphosphotriester-DNA methyltransferase !1homology KEYWORDS DNA binding; DNA repair; methylated amino acid; !1methyltransferase; transcription regulation FEATURE !$7-191 #domain methylphosphotriester-DNA methyltransferase !8homology #label MPT\ !$268-348 #domain methylated-DNA-protein-cysteine !8S-methyltransferase homology #label MGT\ !$321 #binding_site methyl (Cys) (covalent) #status !8predicted SUMMARY #length 354 #molecular-weight 39323 #checksum 7668 SEQUENCE /// ENTRY XYEBOT #type complete TITLE methylated-DNA-[protein]-cysteine S-methyltransferase (EC 2.1.1.63) - Salmonella typhimurium CONTAINS methylated-DNA-protein-cysteine S-methyltransferase (EC 2.1.1.63) ada; methylphosphotriester-DNA methyltransferase ORGANISM #formal_name Salmonella typhimurium DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 03-Jun-2002 ACCESSIONS A39433 REFERENCE A39433 !$#authors Hakura, A.; Morimoto, K.; Sofuni, T.; Nohmi, T. !$#journal J. Bacteriol. (1991) 173:3663-3672 !$#title Cloning and characterization of the Salmonella typhimurium !1ada gene, which encodes O(6)-methylguanine-DNA !1methyltransferase. !$#cross-references MUID:91267928; PMID:1904855 !$#accession A39433 !'##molecule_type DNA !'##residues 1-352 ##label HAK !'##cross-references GB:D90221; NID:g217046; PIDN:BAA14252.1; !1PID:g217047 COMMENT This enzyme is part of an inducible DNA repair system that !1protects against methylating and alkylating agents by !1transferring the alkyl group from O(6)-alkylguanine in DNA !1to a cysteine residue located within the enzyme itself. GENETICS !$#gene ada CLASSIFICATION #superfamily adaptive response regulatory protein; !1methylated-DNA-protein-cysteine S-methyltransferase !1homology; methylphosphotriester-DNA methyltransferase !1homology KEYWORDS DNA binding; DNA repair; methylated amino acid; !1methyltransferase; transcription regulation FEATURE !$6-190 #domain methylphosphotriester-DNA methyltransferase !8homology #label MPT\ !$267-347 #domain methylated-DNA-protein-cysteine !8S-methyltransferase homology #label MGT\ !$320 #binding_site methyl (Cys) (covalent) #status !8predicted SUMMARY #length 352 #molecular-weight 39217 #checksum 4195 SEQUENCE /// ENTRY XYECCR #type complete TITLE protein-glutamate O-methyltransferase (EC 2.1.1.80) - Escherichia coli (strain K-12) ALTERNATE_NAMES methyl-accepting chemotaxis protein O-methyltransferase; protein methylase II; protein-glutamate methyltransferase ORGANISM #formal_name Escherichia coli DATE 28-Dec-1987 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS D64951; C25195 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64951 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-286 ##label BLAT !'##cross-references GB:AE000282; GB:U00096; NID:g1788189; !1PIDN:AAC74954.1; PID:g1788193; UWGP:b1884 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A91811 !$#authors Mutoh, N.; Simon, M.I. !$#journal J. Bacteriol. (1986) 165:161-166 !$#title Nucleotide sequence corresponding to five chemotaxis genes !1in Escherichia coli. !$#cross-references MUID:86085665; PMID:3510184 !$#accession C25195 !'##molecule_type DNA !'##residues 1-112,'G',114-286 ##label MUT !'##cross-references GB:M13463; NID:g145517; PIDN:AAA23568.1; !1PID:g145523 COMMENT This enzyme catalyzes the transfer of methyl groups from !1S-adenosylmethionine to the membrane-bound methyl-accepting !1chemotaxis proteins (MCP) to form gamma-glutamyl methyl !1ester residues in MCP. The MCP methylation state of the cell !1is crucial for sensory responses and adaptations. GENETICS !$#gene cheR !$#map_position 42 min CLASSIFICATION #superfamily protein-glutamate O-methyltransferase; !1protein-glutamate O-methyltransferase homology KEYWORDS chemotaxis; methyltransferase; S-adenosylmethionine FEATURE !$20-273 #domain protein-glutamate O-methyltransferase !8homology #label PGM SUMMARY #length 286 #molecular-weight 32849 #checksum 626 SEQUENCE /// ENTRY XYEBGM #type complete TITLE protein-glutamate O-methyltransferase (EC 2.1.1.80) - Salmonella typhimurium ALTERNATE_NAMES methyl-accepting chemotaxis protein O-methyltransferase; protein methylase II; protein-glutamate methyltransferase ORGANISM #formal_name Salmonella typhimurium DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 05-May-2000 ACCESSIONS A29303 REFERENCE A29303 !$#authors Simms, S.A.; Stock, A.M.; Stock, J.B. !$#journal J. Biol. Chem. (1987) 262:8537-8543 !$#title Purification and characterization of the !1S-adenosylmethionine: glutamyl methyltransferase that !1modifies membrane chemoreceptor proteins in bacteria. !$#cross-references MUID:87250466; PMID:3298235 !$#accession A29303 !'##molecule_type DNA !'##residues 1-288 ##label SIM !'##cross-references GB:J02757; NID:g153902; PIDN:AAA27035.1; !1PID:g153903 COMMENT This enzyme catalyzes the transfer of methyl groups from !1S-adenosylmethionine to the membrane-bound methyl-accepting !1chemotaxis proteins (MCP) to form gamma-glutamyl methyl !1ester residues in MCP. The MCP methylation state of the cell !1is crucial for sensory responses and adaptations. GENETICS !$#gene cheR !$#map_position 40 min CLASSIFICATION #superfamily protein-glutamate O-methyltransferase; !1protein-glutamate O-methyltransferase homology KEYWORDS chemotaxis; methyltransferase; S-adenosylmethionine; sensory !1transduction FEATURE !$20-273 #domain protein-glutamate O-methyltransferase !8homology #label PGM SUMMARY #length 288 #molecular-weight 32923 #checksum 815 SEQUENCE /// ENTRY XYYZFG #type complete TITLE frzG protein - Myxococcus xanthus ORGANISM #formal_name Myxococcus xanthus DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 11-Jun-1999 ACCESSIONS B36707 REFERENCE A36707 !$#authors McCleary, W.R.; McBride, M.J.; Zusman, D.R. !$#journal J. Bacteriol. (1990) 172:4877-4887 !$#title Developmental sensory transduction in Myxococcus xanthus !1involves methylation and demethylation of FrzCD. !$#cross-references MUID:90368538; PMID:2168368 !$#accession B36707 !'##molecule_type DNA !'##residues 1-593 ##label MCC !'##cross-references GB:M35200; NID:g150092; PIDN:AAA25398.1; !1PID:g150094 COMMENT This is one of the proteins required for the normal !1aggregation of M. xanthus cells during fruiting body !1formation. It is also a component of a sensory transduction !1pathway that controls the frequency at which cells reverse !1their gliding direction. GENETICS !$#gene frzG !$#start_codon GTG CLASSIFICATION #superfamily frzG protein; protein-glutamate !1O-methyltransferase homology; tetratricopeptide repeat !1homology KEYWORDS chemotaxis; sensory transduction FEATURE !$2-260 #domain protein-glutamate O-methyltransferase !8homology #label PGM\ !$423-456 #domain tetratricopeptide repeat homology #label TT1\ !$457-490 #domain tetratricopeptide repeat homology #label TT2\ !$491-524 #domain tetratricopeptide repeat homology #label TT3\ !$525-558 #domain tetratricopeptide repeat homology #label TT4 SUMMARY #length 593 #molecular-weight 64668 #checksum 8608 SEQUENCE /// ENTRY XYECS #type complete TITLE glycine hydroxymethyltransferase (EC 2.1.2.1) - Escherichia coli (strain K-12) ALTERNATE_NAMES serine methylase ORGANISM #formal_name Escherichia coli DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 01-Mar-2002 ACCESSIONS A00559; F65032 REFERENCE A00559 !$#authors Plamann, M.D.; Stauffer, L.T.; Urbanowski, M.L.; Stauffer, !1G.V. !$#journal Nucleic Acids Res. (1983) 11:2065-2075 !$#title Complete nucleotide sequence of the Escherichia coli glyA !1gene. !$#cross-references MUID:83168944; PMID:6300791 !$#accession A00559 !'##molecule_type DNA !'##residues 1-417 ##label PLA !'##cross-references GB:V00283; NID:g41602; PIDN:CAA23547.1; PID:g41603 !'##experimental_source strain K12 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65032 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-417 ##label BLAT !'##cross-references GB:AE000341; GB:U00096; NID:g1788899; !1PIDN:AAC75604.1; PID:g1788902; UWGP:b2551 !'##experimental_source strain K-12, substrain MG1655 COMMENT This enzyme catalyzes the conversion of serine to glycine !1and 5,10-methylenetetrahydrofolate. GENETICS !$#gene glyA !$#map_position 55 min CLASSIFICATION #superfamily glycine hydroxymethyltransferase KEYWORDS phosphoprotein; pyridoxal phosphate; transferase FEATURE !$229 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 417 #molecular-weight 45316 #checksum 4104 SEQUENCE /// ENTRY B48427 #type complete TITLE glycine hydroxymethyltransferase (EC 2.1.2.1) - Salmonella typhimurium ALTERNATE_NAMES serine hydroxymethyltransferase ORGANISM #formal_name Salmonella typhimurium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B48427; A22083; S05947 REFERENCE A48427 !$#authors Steiert, J.G.; Urbanowski, M.L.; Stauffer, L.T.; Plamann, !1M.D.; Stauffer, G.V. !$#journal DNA Seq. (1990) 1:107-113 !$#title Nucleotide sequence of the Salmonella typhimurium glyA gene. !$#cross-references MUID:92190538; PMID:2134182 !$#accession B48427 !'##status preliminary !'##molecule_type DNA !'##residues 1-417 ##label ST2 !'##cross-references EMBL:X15816; NID:g47697; PIDN:CAA33808.1; !1PID:g47698 !'##note sequence extracted from NCBI backbone (NCBIN:89484, !1NCBIP:89491) REFERENCE A22083 !$#authors Urbanowski, M.L.; Plamann, M.D.; Stauffer, L.T.; Stauffer, !1G.V. !$#journal Gene (1984) 27:47-54 !$#title Cloning and characterization of the gene for Salmonella !1typhimurium serine hydroxymethyltransferase. !$#cross-references MUID:84183610; PMID:6325301 !$#accession A22083 !'##molecule_type DNA !'##residues 179-192,'Y',194-215 ##label URB !'##cross-references GB:K01616; NID:g154095; PIDN:AAA27135.1; !1PID:g154096 GENETICS !$#gene glyA CLASSIFICATION #superfamily glycine hydroxymethyltransferase KEYWORDS phosphoprotein; pyridoxal phosphate; transferase FEATURE !$229 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 417 #molecular-weight 45414 #checksum 5154 SEQUENCE /// ENTRY JQ1016 #type complete TITLE glycine hydroxymethyltransferase (EC 2.1.2.1) - Campylobacter jejuni ALTERNATE_NAMES serine aldolase; serine hydroxymethylase; serine methylase; threonine aldolase ORGANISM #formal_name Campylobacter jejuni DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 20-Apr-2001 ACCESSIONS JQ1016; S16468 REFERENCE JQ1016 !$#authors Chan, V.L.; Bingham, H.L. !$#journal Gene (1991) 101:51-58 !$#title Complete sequence of the Campylobacter jejuni glyA gene !1encoding serine hydroxymethyltransferase. !$#cross-references MUID:91285434; PMID:2060796 !$#accession JQ1016 !'##molecule_type DNA !'##residues 1-414 ##label CHA1 !'##cross-references EMBL:X53816; NID:g40533; PIDN:CAA37812.1; !1PID:g40534 COMMENT In the presence of tetrahydrofolate, this enzyme catalyzes !1the reversible cleavage of Ser to Gly and the formation of !15,10-methylenetetrahydrofolate. GENETICS !$#gene glyA CLASSIFICATION #superfamily glycine hydroxymethyltransferase KEYWORDS phosphoprotein; pyridoxal phosphate; transferase FEATURE !$224 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 414 #molecular-weight 45751 #checksum 215 SEQUENCE /// ENTRY S34379 #type complete TITLE glycine hydroxymethyltransferase (EC 2.1.2.1) - Actinobacillus actinomycetemcomitans ORGANISM #formal_name Actinobacillus actinomycetemcomitans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S34379 REFERENCE S34379 !$#authors Brogan, J.M.; Demuth, D.R. !$#submission submitted to the EMBL Data Library, July 1993 !$#description Nucleotide sequence of the Actinobacillus !1actinomycetemcomitans glyA gene. !$#accession S34379 !'##molecule_type DNA !'##residues 1-420 ##label BRO !'##cross-references EMBL:Z23269; NID:g313831; PIDN:CAA80807.1; !1PID:g313832 GENETICS !$#gene glyA CLASSIFICATION #superfamily glycine hydroxymethyltransferase KEYWORDS phosphoprotein; pyridoxal phosphate; transferase FEATURE !$228 #active_site His #status predicted\ !$229 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 420 #molecular-weight 45790 #checksum 9481 SEQUENCE /// ENTRY D64100 #type complete TITLE glycine hydroxymethyltransferase (EC 2.1.2.1) - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES serine methylase ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS D64100 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession D64100 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-421 ##label TIGR !'##cross-references GB:U32771; GB:L42023; NID:g1573907; !1PIDN:AAC22549.1; PID:g1573908; TIGR:HI0889 CLASSIFICATION #superfamily glycine hydroxymethyltransferase KEYWORDS phosphoprotein; pyridoxal phosphate; transferase FEATURE !$229 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 421 #molecular-weight 45904 #checksum 1062 SEQUENCE /// ENTRY I40483 #type complete TITLE glycine hydroxymethyltransferase (EC 2.1.2.1) glyA - Bacillus subtilis ALTERNATE_NAMES serine hydroxymethyltransferase ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS I40483; H69635; S49363 REFERENCE I40473 !$#authors Martinussen, J.; Glaser, P.; Andersen, P.S.; Saxild, H.H. !$#journal J. Bacteriol. (1995) 177:271-274 !$#title Two genes encoding uracil phosphoribosyltransferase are !1present in Bacillus subtilis. !$#cross-references MUID:95095982; PMID:7798145 !$#accession I40483 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-415 ##label RES !'##cross-references EMBL:Z38002; NID:g556877; PIDN:CAA86110.1; !1PID:g556886 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69635 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-415 ##label KUN !'##cross-references GB:Z99122; GB:AL009126; NID:g2636029; !1PIDN:CAB15707.1; PID:g2636215 !'##experimental_source strain 168 GENETICS !$#gene glyA; glyC CLASSIFICATION #superfamily glycine hydroxymethyltransferase KEYWORDS phosphoprotein; pyridoxal phosphate; transferase FEATURE !$226 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 415 #molecular-weight 45489 #checksum 2474 SEQUENCE /// ENTRY S15203 #type complete TITLE glycine hydroxymethyltransferase (EC 2.1.2.1) [validated] - Bradyrhizobium japonicum ORGANISM #formal_name Bradyrhizobium japonicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 17-Mar-2000 ACCESSIONS S15203 REFERENCE S15203 !$#authors Rossbach, S.; Hennecke, H. !$#journal Mol. Microbiol. (1991) 5:39-47 !$#title Identification of glyA as a symbiotically essential gene in !1Bradyrhizobium japonicum. !$#cross-references MUID:91194557; PMID:2014004 !$#accession S15203 !'##molecule_type DNA !'##residues 1-432 ##label ROS !'##cross-references EMBL:X54638; NID:g39530; PIDN:CAA38450.1; !1PID:g39531 GENETICS !$#gene glyA FUNCTION !$#description EC 2.1.2.1 [validated, MUID:91194557] !$#note B. japonicum may have an additional pathway for glycine !1biosynthesis CLASSIFICATION #superfamily glycine hydroxymethyltransferase KEYWORDS phosphoprotein; pyridoxal phosphate; transferase FEATURE !$239 #active_site His #status predicted\ !$240 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 432 #molecular-weight 45991 #checksum 2221 SEQUENCE /// ENTRY XYRBSC #type complete TITLE glycine hydroxymethyltransferase (EC 2.1.2.1), cytosolic - rabbit ALTERNATE_NAMES serine hydroxymethylase; serine hydroxymethyltransferase; serine methylase; threonine aldolase ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 30-Sep-1988 #sequence_revision 01-Mar-1996 #text_change 11-Jun-1999 ACCESSIONS S24342; PC4073; A29140; A35555; B35555; A15070 REFERENCE S24342 !$#authors Byrne, P.C.; Sanders, P.G.; Snell, K. !$#journal Biochem. J. (1992) 286:117-123 !$#title Nucleotide sequence and expression of a cDNA encoding rabbit !1liver cytosolic serine hydroxymethyltransferase. !$#cross-references MUID:92392263; PMID:1381582 !$#accession S24342 !'##molecule_type mRNA !'##residues 1-484 ##label BYR !'##cross-references EMBL:Z11846; NID:g1536; PIDN:CAA77870.1; PID:g1537 REFERENCE PC4073 !$#authors Byrne, P.C.; Sanders, P.G.; Snell, K. !$#journal Biochem. Biophys. Res. Commun. (1995) 214:496-502 !$#title Translational control of mammalian serine !1hydroxymethyltransferase expression. !$#cross-references MUID:95408277; PMID:7677757 !$#accession PC4073 !'##molecule_type mRNA !'##residues 1-98 ##label BY2 !'##cross-references EMBL:Z11846 !'##experimental_source liver REFERENCE A29140 !$#authors Martini, F.; Angelaccio, S.; Pascarella, S.; Barra, D.; !1Bossa, F.; Schirch, V. !$#journal J. Biol. Chem. (1987) 262:5499-5509 !$#title The primary structure of rabbit liver cytosolic serine !1hydroxymethyltransferase. !$#cross-references MUID:87194733; PMID:3553178 !$#accession A29140 !'##molecule_type protein !'##residues 2-484 ##label MAR !'##experimental_source liver REFERENCE A35555 !$#authors Artigues, A.; Birkett, A.; Schirch, V. !$#journal J. Biol. Chem. (1990) 265:4853-4858 !$#title Evidence for the in vivo deamidation and isomerization of an !1asparaginyl residue in cytosolic serine !1hydroxymethyltransferase. !$#cross-references MUID:90202954; PMID:2318867 !$#accession A35555 !'##molecule_type protein !'##residues 2-15 ##label ART !$#accession B35555 !'##molecule_type protein !'##residues 2-5,'D',7-15 ##label AR2 !'##note this form represents the product of nonenzymatic deamidation; !16-isoAsp was also found REFERENCE A15070 !$#authors Schirch, L.; Slagel, S.; Barra, D.; Martini, F.; Bossa, F. !$#journal J. Biol. Chem. (1980) 255:2986-2989 !$#title Evidence for a sulfhydryl group at the active site of serine !1transhydroxymethylase. !$#cross-references MUID:80137560; PMID:7358720 !$#accession A15070 !'##molecule_type protein !'##residues 194-205 ##label SCH COMMENT The active enzyme, a tetramer of identical chains, catalyzes !1the conversion of serine and tetrahydrofolate to glycine and !15,10-methylenetetrahydrofolate. Both products are involved !1in de novo purine and pyrimidine nucleotide synthesis. CLASSIFICATION #superfamily glycine hydroxymethyltransferase KEYWORDS acetylated amino end; homotetramer; phosphoprotein; !1pyridoxal phosphate; transferase FEATURE !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental\ !$204 #active_site Cys #status experimental\ !$256 #active_site His #status predicted\ !$257 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status experimental SUMMARY #length 484 #molecular-weight 52975 #checksum 6175 SEQUENCE /// ENTRY A46746 #type complete TITLE glycine hydroxymethyltransferase (EC 2.1.2.1), cytosolic - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A46746 REFERENCE A46746 !$#authors Garrow, T.A.; Brenner, A.A.; Whitehead, V.M.; Chen, X.N.; !1Duncan, R.G.; Korenberg, J.R.; Shane, B. !$#journal J. Biol. Chem. (1993) 268:11910-11916 !$#title Cloning of human cDNAs encoding mitochondrial and cytosolic !1serine hydroxymethyltransferases and chromosomal !1localization. !$#cross-references MUID:93280158; PMID:8505317 !$#accession A46746 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-483 ##label GAR !'##cross-references GB:L11931; NID:g307421; PIDN:AAA63257.1; !1PID:g307422 GENETICS !$#gene GDB:SHMT1 !'##cross-references GDB:141855; OMIM:182144 !$#map_position 17p11.2-17p11.2 CLASSIFICATION #superfamily glycine hydroxymethyltransferase KEYWORDS cytosol; phosphoprotein; pyridoxal phosphate; transferase FEATURE !$257 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 483 #molecular-weight 53082 #checksum 6909 SEQUENCE /// ENTRY A42906 #type complete TITLE glycine hydroxymethyltransferase (EC 2.1.2.1) - garden pea ORGANISM #formal_name Pisum sativum #common_name garden pea DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A42906 REFERENCE A42906 !$#authors Turner, S.R.; Ireland, R.; Morgan, C.; Rawsthorne, S. !$#journal J. Biol. Chem. (1992) 267:13528-13534 !$#title Identification and localization of multiple forms of serine !1hydroxymethyltransferase in pea (Pisum sativum) and !1characterization of a cDNA encoding a mitochondrial isoform. !$#cross-references MUID:92317078; PMID:1618853 !$#accession A42906 !'##status preliminary !'##molecule_type mRNA !'##residues 1-518 ##label TUR !'##cross-references GB:M87649; GB:M87650; NID:g169157; PIDN:AAA33687.1; !1PID:g169158 !'##experimental_source cv. Birte !'##note sequence extracted from NCBI backbone (NCBIN:107785, !1NCBIP:107786) CLASSIFICATION #superfamily glycine hydroxymethyltransferase KEYWORDS phosphoprotein; pyridoxal phosphate; transferase FEATURE !$287 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 518 #molecular-weight 57292 #checksum 9273 SEQUENCE /// ENTRY S40218 #type complete TITLE glycine hydroxymethyltransferase (EC 2.1.2.1) - potato ORGANISM #formal_name Solanum tuberosum #common_name potato DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 23-Mar-2001 ACCESSIONS S40218 REFERENCE S40212 !$#authors Kopriva, S.; Bauwe, H. !$#submission submitted to the EMBL Data Library, September 1993 !$#description cDNA cloning and sequencing of two isoforms of serine !1hydroxymethyltransferase in Flaveria pringlei. !$#accession S40218 !'##molecule_type mRNA !'##residues 1-518 ##label KOP !'##cross-references EMBL:Z25863; NID:g438246; PIDN:CAA81082.1; !1PID:g438247 CLASSIFICATION #superfamily glycine hydroxymethyltransferase KEYWORDS phosphoprotein; pyridoxal phosphate; transferase FEATURE !$286 #active_site His #status predicted\ !$287 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 518 #molecular-weight 57146 #checksum 4823 SEQUENCE /// ENTRY A42241 #type complete TITLE glycine hydroxymethyltransferase (EC 2.1.2.1), cytosolic - Neurospora crassa ALTERNATE_NAMES serine hydroxymethyltransferase ORGANISM #formal_name Neurospora crassa DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A42241 REFERENCE A42241 !$#authors McClung, C.R.; Davis, C.R.; Page, K.M.; Denome, S.A. !$#journal Mol. Cell. Biol. (1992) 12:1412-1421 !$#title Characterization of the formate (for) locus, which encodes !1the cytosolic serine hydroxymethyltransferase of Neurospora !1crassa. !$#cross-references MUID:92195285; PMID:1532227 !$#accession A42241 !'##status preliminary !'##molecule_type DNA !'##residues 1-479 ##label MCC !'##cross-references GB:M81918 CLASSIFICATION #superfamily glycine hydroxymethyltransferase KEYWORDS cytosol; phosphoprotein; pyridoxal phosphate; transferase FEATURE !$249 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 479 #molecular-weight 52821 #checksum 5679 SEQUENCE /// ENTRY XYECGF #type complete TITLE phosphoribosylglycinamide formyltransferase (EC 2.1.2.2) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 01-Mar-2002 ACCESSIONS A28486; C65026 REFERENCE A28486 !$#authors Smith, J.M.; Daum III, H.A. !$#journal J. Biol. Chem. (1987) 262:10565-10569 !$#title Identification and nucleotide sequence of a gene encoding !15'- phosphoribosylglycinamide transformylase in Escherichia !1coli K12. !$#cross-references MUID:87280114; PMID:3301838 !$#accession A28486 !'##molecule_type DNA !'##residues 1-212 ##label SMI !'##cross-references EMBL:M13747; NID:g147424; PIDN:AAA83899.1; !1PID:g147426 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65026 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-212 ##label BLAT !'##cross-references GB:AE000336; GB:U00096; NID:g1788839; !1PIDN:AAC75553.1; PID:g1788846; UWGP:b2500 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene purN !$#map_position 54 min CLASSIFICATION #superfamily phosphoribosylglycinamide formyltransferase; !1phosphoribosylglycinamide formyltransferase homology KEYWORDS purine nucleotide biosynthesis; transferase FEATURE !$3-194 #domain phosphoribosylglycinamide formyltransferase !8homology #label PRGF SUMMARY #length 212 #molecular-weight 23238 #checksum 8380 SEQUENCE /// ENTRY XYBSGF #type complete TITLE phosphoribosylglycinamide formyltransferase (EC 2.1.2.2) - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jun-2000 ACCESSIONS I29326; B69685 REFERENCE A29326 !$#authors Ebbole, D.J.; Zalkin, H. !$#journal J. Biol. Chem. (1987) 262:8274-8287 !$#title Cloning and characterization of a 12-gene cluster from !1Bacillus subtilis encoding nine enzymes for de novo purine !1nucleotide synthesis. !$#cross-references MUID:87250425; PMID:3036807 !$#accession I29326 !'##molecule_type DNA !'##residues 1-195 ##label EBB !'##cross-references EMBL:J02732; NID:g143363; PIDN:AAA22682.1; !1PID:g143372 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69685 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-195 ##label KUN !'##cross-references GB:Z99107; GB:AL009126; NID:g2632866; !1PIDN:CAB12471.1; PID:g2632965 !'##experimental_source strain 168 GENETICS !$#gene purN !$#map_position 18 min CLASSIFICATION #superfamily phosphoribosylglycinamide formyltransferase; !1phosphoribosylglycinamide formyltransferase homology KEYWORDS purine nucleotide biosynthesis; transferase FEATURE !$4-194 #domain phosphoribosylglycinamide formyltransferase !8homology #label PRGF SUMMARY #length 195 #molecular-weight 21776 #checksum 3229 SEQUENCE /// ENTRY S37105 #type complete TITLE phosphoribosylglycinamide formyltransferase (EC 2.1.2.2) - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 06-Jan-1994 #sequence_revision 28-Oct-1994 #text_change 11-Jun-1999 ACCESSIONS S37105 REFERENCE S37104 !$#authors Schnorr, K.M. !$#submission submitted to the EMBL Data Library, August 1993 !$#accession S37105 !'##molecule_type mRNA !'##residues 1-226 ##label SCH !'##cross-references EMBL:X74767; NID:g398611; PIDN:CAA52779.1; !1PID:g398612 GENETICS !$#gene PUR3 CLASSIFICATION #superfamily phosphoribosylglycinamide formyltransferase; !1phosphoribosylglycinamide formyltransferase homology KEYWORDS purine nucleotide biosynthesis; transferase FEATURE !$34-226 #domain phosphoribosylglycinamide formyltransferase !8homology #label PRGF SUMMARY #length 226 #molecular-weight 24601 #checksum 3103 SEQUENCE /// ENTRY DTBSPH #type complete TITLE purH bifunctional enzyme - Bacillus subtilis CONTAINS IMP cyclohydrolase (EC 3.5.4.10); phosphoribosylaminoimidazolecarboxamide formyltransferase (EC 2.1.2.3) ORGANISM #formal_name Bacillus subtilis DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jun-2000 ACCESSIONS A29183; F69684 REFERENCE A29326 !$#authors Ebbole, D.J.; Zalkin, H. !$#journal J. Biol. Chem. (1987) 262:8274-8287 !$#title Cloning and characterization of a 12-gene cluster from !1Bacillus subtilis encoding nine enzymes for de novo purine !1nucleotide synthesis. !$#cross-references MUID:87250425; PMID:3036807 !$#accession A29183 !'##molecule_type DNA !'##residues 1-512 ##label EBB !'##cross-references EMBL:J02732; NID:g143363; PIDN:AAA22683.1; !1PID:g143373 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69684 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-512 ##label KUN !'##cross-references GB:Z99107; GB:AL009126; NID:g2632866; !1PIDN:CAB12472.1; PID:g2632966 !'##experimental_source strain 168 GENETICS !$#gene purH; purJ !$#map_position 18 min CLASSIFICATION #superfamily purH bifunctional enzyme KEYWORDS hydrolase; multifunctional enzyme; purine nucleotide !1biosynthesis; transferase SUMMARY #length 512 #molecular-weight 55739 #checksum 7910 SEQUENCE /// ENTRY DTECPH #type complete TITLE purH bifunctional enzyme - Escherichia coli (strain K-12) CONTAINS IMP cyclohydrolase (EC 3.5.4.10); phosphoribosylaminoimidazolecarboxamide formyltransferase (EC 2.1.2.3) ORGANISM #formal_name Escherichia coli DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 01-Mar-2002 ACCESSIONS B34193; S09571; A65208 REFERENCE A92739 !$#authors Aiba, A.; Mizobuchi, K. !$#journal J. Biol. Chem. (1989) 264:21239-21246 !$#title Nucleotide sequence analysis of genes purH and purD involved !1in the de novo purine nucleotide biosynthesis of Escherichia !1coli. !$#cross-references MUID:90078227; PMID:2687276 !$#accession B34193 !'##molecule_type DNA !'##residues 1-529 ##label AIB !'##cross-references EMBL:J05126; NID:g147419; PIDN:AAA24454.1; !1PID:g147420 REFERENCE S09571 !$#authors Flannigan, K.A.; Hennigan, S.H.; Vogelbacker, H.H.; Gots, !1J.S.; Smith, J.M. !$#journal Mol. Microbiol. (1990) 4:381-392 !$#title Purine biosynthesis in Escherichia coli K12: structure and !1DNA sequence studies of the purHD locus. !$#cross-references MUID:90286915; PMID:2192230 !$#accession S09571 !'##molecule_type DNA !'##residues 1-529 ##label FLA !'##cross-references EMBL:X51950; NID:g42594; PIDN:CAA36212.1; !1PID:g42595 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65208 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-529 ##label BLAT !'##cross-references GB:AE000473; GB:U00096; NID:g2367336; !1PIDN:AAC76980.1; PID:g1790439; UWGP:b4006 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene purH; purJ !$#map_position 90 min CLASSIFICATION #superfamily purH bifunctional enzyme KEYWORDS hydrolase; multifunctional enzyme; purine nucleotide !1biosynthesis; transferase SUMMARY #length 529 #molecular-weight 57329 #checksum 265 SEQUENCE /// ENTRY DTEBPH #type fragment TITLE purH bifunctional enzyme - Salmonella typhimurium (fragment) CONTAINS IMP cyclohydrolase (EC 3.5.4.10); phosphoribosylaminoimidazolecarboxamide formyltransferase (EC 2.1.2.3) ORGANISM #formal_name Salmonella typhimurium DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 11-Jun-1999 ACCESSIONS S18488 REFERENCE S18488 !$#authors Chopra, A.K.; Peterson, J.W.; Prasad, R. !$#journal Biochim. Biophys. Acta (1991) 1090:351-354 !$#title Nucleotide sequence analysis of purH and purD genes from !1Salmonella typhimurium. !$#cross-references MUID:92062738; PMID:1954258 !$#accession S18488 !'##molecule_type DNA !'##residues 1-508 ##label CHO !'##cross-references EMBL:M66160; NID:g154286; PIDN:AAA27197.1; !1PID:g154287 GENETICS !$#gene purH; purJ !$#map_position 90 min CLASSIFICATION #superfamily purH bifunctional enzyme KEYWORDS hydrolase; multifunctional enzyme; purine nucleotide !1biosynthesis; transferase SUMMARY #length 508 #checksum 7350 SEQUENCE /// ENTRY DTCHPH #type complete TITLE purH bifunctional enzyme - chicken CONTAINS IMP cyclohydrolase (EC 3.5.4.10); phosphoribosylaminoimidazolecarboxamide formyltransferase (EC 2.1.2.3) ORGANISM #formal_name Gallus gallus #common_name chicken DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 11-Jun-1999 ACCESSIONS JQ1281 REFERENCE JQ1281 !$#authors Ni, L.; Guan, K.; Zalkin, H.; Dixon, J.E. !$#journal Gene (1991) 106:197-205 !$#title De novo purine nucleotide biosynthesis: cloning, sequencing !1and expression of a chicken PurH cDNA encoding !15-aminoimidazole-4-carboxamide-ribonucleotide !1transformylase-IMP cyclohydrolase. !$#cross-references MUID:92039077; PMID:1937050 !$#accession JQ1281 !'##molecule_type mRNA !'##residues 1-593 ##label NIL !'##cross-references GB:S64492; NID:g238785; PIDN:AAB20309.1; !1PID:g238786 !'##experimental_source liver COMMENT This protein catalyzes two steps in the de novo synthesis of !1purine nucleotide. GENETICS !$#gene purH CLASSIFICATION #superfamily purH bifunctional enzyme KEYWORDS hydrolase; purine nucleotide biosynthesis; transferase SUMMARY #length 593 #molecular-weight 64414 #checksum 8258 SEQUENCE /// ENTRY DTECR #type complete TITLE aspartate carbamoyltransferase (EC 2.1.3.2) regulatory chain - Escherichia coli (strain K-12) ALTERNATE_NAMES aspartate transcarbamylase; carbamylaspartotranskinase ORGANISM #formal_name Escherichia coli DATE 24-Apr-1984 #sequence_revision 03-Aug-1984 #text_change 01-Mar-2002 ACCESSIONS A93985; A00560; S56470; I56404; G65236 REFERENCE A93985 !$#authors Schachman, H.K.; Pauza, C.D.; Navre, M.; Karels, M.J.; Wu, !1L.; Yang, Y.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:115-119 !$#title Location of amino acid alterations in mutants of aspartate !1transcarbamoylase: structural aspects of interallelic !1complementation. !$#cross-references MUID:84119419; PMID:6364131 !$#accession A93985 !'##molecule_type DNA !'##residues 1-153 ##label SCH !'##cross-references GB:K01472; NID:g147463; PIDN:AAA24477.1; !1PID:g147465 REFERENCE A93154 !$#authors Weber, K. !$#journal Nature (1968) 218:1116-1119 !$#title New structural model of Escherichia coli aspartate !1transcarbamylase and the amino-acid sequence of the !1regulatory polypeptide chain. !$#cross-references MUID:68284659; PMID:4872216 !$#accession A00560 !'##molecule_type protein !'##residues 1-3,'ND',6-9,'AE',12-18,'N',20-23,'E',25-38,'QD',41-86, !1'ND',89-102,'NID',106-110,'D',112-128,130-153 ##label WEB REFERENCE A93823 !$#authors Monaco, H.L.; Crawford, J.L.; Lipscomb, W.N. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1978) 75:5276-5280 !$#title Three-dimensional structures of aspartate !1carbamoyltransferase from Escherichia coli and of its !1complex with cytidine triphosphate. !$#cross-references MUID:79074799; PMID:364472 !$#contents annotation; X-ray crystallography, 2.8 angstroms REFERENCE A93993 !$#authors Ke, H.; Honzatko, R.B.; Lipscomb, W.N. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:4037-4040 !$#title Structure of unligated aspartate carbamoyltransferase of !1Escherichia coli at 2.6-angstroms resolution. !$#cross-references MUID:84248054; PMID:6377306 !$#contents annotation; X-ray crystallography, 2.6 angstroms; quaternary !1structure REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56470 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-153 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97141.1; !1PID:g537086 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE I56404 !$#authors Cunin, R.; Jacobs, A.; Charlier, D.; Crabeel, M.; Herve, G.; !1Glansdorff, N.; Pierard, A. !$#journal J. Mol. Biol. (1985) 186:707-713 !$#title Structure-function relationship in allosteric aspartate !1carbamoyltransferase from Escherichia coli: I. Primary !1structure of a pyrI gene encoding a modified regulatory !1subunit. !$#cross-references MUID:86143826; PMID:3912513 !$#accession I56404 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 128-153 ##label RES !'##cross-references GB:M28578; NID:g147480; PIDN:AAA24487.1; !1PID:g147481 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65236 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-153 ##label BLAT !'##cross-references GB:AE000495; GB:U00096; NID:g2367361; !1PIDN:AAC77201.1; PID:g1790692; UWGP:b4244 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene pyrI !$#map_position 97 min COMPLEX heterododecamer of two trimers of catalytic chains and three !1dimers of regulatory chains (homodimer, homohexamer, and !1homotrimer) FUNCTION !$#description catalyzes the transcarbamylation of carbanoyl phophate and !1aspartate, the rate-limiting step in the biosynthesis of !1pyrimidines !$#pathway pyrimidine nucleotide biosynthesis CLASSIFICATION #superfamily aspartate carbamoyltransferase regulatory chain KEYWORDS acyltransferase; heterododecamer; homodimer; homohexamer; !1homotrimer; pyrimidine nucleotide biosynthesis; zinc FEATURE !$109,114,138,141 #binding_site zinc (Cys) #status experimental SUMMARY #length 153 #molecular-weight 17120 #checksum 1672 SEQUENCE /// ENTRY DTEBCT #type complete TITLE aspartate carbamoyltransferase (EC 2.1.3.2) regulatory chain - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 11-Jun-1999 ACCESSIONS S00050 REFERENCE S00028 !$#authors Michaels, G.; Kelln, R.A.; Nargang, F.E. !$#journal Eur. J. Biochem. (1987) 166:55-61 !$#title Cloning, nucleotide sequence and expression of the pyrBI !1operon of Salmonella typhimurium LT2. !$#cross-references MUID:87246692; PMID:3036524 !$#accession S00050 !'##molecule_type DNA !'##residues 1-153 ##label MIC !'##cross-references GB:X05641; NID:g47861; PIDN:CAA29130.1; PID:g47864 COMMENT The active enzyme contains two trimers of catalytic chains !1and three dimers of regulatory chains; it catalyzes the !1rate-limiting step in the biosynthesis of pyrimidines. GENETICS !$#gene pyrI CLASSIFICATION #superfamily aspartate carbamoyltransferase regulatory chain KEYWORDS heterododecamer; homodimer; homohexamer; pyrimidine !1nucleotide biosynthesis; transferase; zinc FEATURE !$109,114,138,141 #binding_site zinc (Cys) #status predicted SUMMARY #length 153 #molecular-weight 17087 #checksum 2672 SEQUENCE /// ENTRY DTSECM #type complete TITLE aspartate carbamoyltransferase (EC 2.1.3.2) regulatory chain - Serratia marcescens ALTERNATE_NAMES aspartate transcarbamylase regulatory chain; carbamylaspartotranskinase ORGANISM #formal_name Serratia marcescens DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 11-Jun-1999 ACCESSIONS C34396 REFERENCE A34396 !$#authors Beck, D.; Kedzie, K.M.; Wild, J.R. !$#journal J. Biol. Chem. (1989) 264:16629-16637 !$#title Comparison of the aspartate transcarbamoylases from Serratia !1marcescens and Escherichia coli. !$#cross-references MUID:89380286; PMID:2674139 !$#accession C34396 !'##molecule_type DNA !'##residues 1-154 ##label BEC !'##cross-references GB:J05033; NID:g398074; PIDN:AAA26565.1; !1PID:g398076 COMMENT The active enzyme contains two trimers of catalytic chains !1and three dimers of regulatory chains; it catalyzes the !1rate-limiting step in the biosynthesis of pyrimidines. GENETICS !$#gene pyrI CLASSIFICATION #superfamily aspartate carbamoyltransferase regulatory chain KEYWORDS heterododecamer; homodimer; homohexamer; pyrimidine !1nucleotide biosynthesis; transferase; zinc FEATURE !$109,114,138,141 #binding_site zinc (Cys) #status predicted SUMMARY #length 154 #molecular-weight 17306 #checksum 3392 SEQUENCE /// ENTRY DTECC #type complete TITLE aspartate carbamoyltransferase (EC 2.1.3.2) catalytic chain - Escherichia coli (strain K-12) ALTERNATE_NAMES aspartate transcarbamylase catalytic chain; aspartyl carbamoyltransferase catalytic chain; carbamylaspartotranskinase catalytic chain ORGANISM #formal_name Escherichia coli DATE 30-Nov-1980 #sequence_revision 10-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS H65236; A00561; A21121; B36599; A21120; S56471 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65236 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-311 ##label BLAT !'##cross-references GB:AE000495; GB:U00096; NID:g2367361; !1PIDN:AAC77202.1; PID:g2367364; UWGP:b4245 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A93985 !$#authors Schachman, H.K.; Pauza, C.D.; Navre, M.; Karels, M.J.; Wu, !1L.; Yang, Y.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:115-119 !$#title Location of amino acid alterations in mutants of aspartate !1transcarbamoylase: structural aspects of interallelic !1complementation. !$#cross-references MUID:84119419; PMID:6364131 !$#accession A00561 !'##molecule_type DNA !'##residues 1-149,'E',151-311 ##label SCH !'##cross-references GB:K01472; NID:g147463; PIDN:AAA24476.1; !1PID:g147464 REFERENCE A21121 !$#authors Hoover, T.A.; Roof, W.D.; Foltermann, K.F.; O'Donovan, G.A.; !1Bencini, D.A.; Wild, J.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:2462-2466 !$#title Nucleotide sequence of the structural gene (pyrB) that !1encodes the catalytic polypeptide of aspartate !1transcarbamoylase of Escherichia coli. !$#cross-references MUID:83195078; PMID:6302686 !$#accession A21121 !'##molecule_type DNA !'##residues 1-60,'Q',62-165,'T',167-220,'V',222-311 ##label HOO !'##cross-references GB:V00323 REFERENCE A36599 !$#authors Donahue, J.P.; Turnbough Jr., C.L. !$#journal J. Biol. Chem. (1990) 265:19091-19099 !$#title Characterization of transcriptional initiation from !1promoters P-1 and P-2 of the pyrBI operon of Escherichia !1coli K12. !$#cross-references MUID:91035438; PMID:1699940 !$#accession B36599 !'##molecule_type DNA !'##residues 1-18 ##label DON !'##cross-references GB:M60508; NID:g147469; PIDN:AAA24481.1; !1PID:g147471 REFERENCE A21120 !$#authors Konigsberg, W.H.; Henderson, L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:2467-2471 !$#title Amino acid sequence of the catalytic subunit of aspartate !1transcarbamoylase from Escherichia coli. !$#cross-references MUID:83195079; PMID:6341995 !$#accession A21120 !'##molecule_type protein !'##residues 2-60,'Q',62-86,'Q',88-90,'N',92-129,'N',131-220,'V', !1222-256,'D',258-259,'M',261,'A',263-311 ##label KON REFERENCE A93993 !$#authors Ke, H.; Honzatko, R.B.; Lipscomb, W.N. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:4037-4040 !$#title Structure of unligated aspartate carbamoyltransferase of !1Escherichia coli at 2.6-angstroms resolution. !$#cross-references MUID:84248054; PMID:6377306 !$#contents annotation; X-ray crystallography, 2.6 angstroms; quaternary !1structure REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56471 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-195,'R',197-311 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97142.1; !1PID:g537087 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 COMMENT The active enzyme contains two trimers of catalytic chains !1and three dimers of regulatory chains; it catalyzes the !1rate-limiting step in the biosynthesis of pyrimidines. GENETICS !$#gene pyrB !$#map_position 97 min CLASSIFICATION #superfamily ornithine carbamoyltransferase; aspartate/ !1ornithine carbamoyltransferase homology KEYWORDS heterododecamer; homohexamer; homotrimer; pyrimidine !1nucleotide biosynthesis; transferase FEATURE !$8-305 #domain aspartate/ornithine carbamoyltransferase !8homology #label ACT SUMMARY #length 311 #molecular-weight 34427 #checksum 4302 SEQUENCE /// ENTRY OWEBAC #type complete TITLE aspartate carbamoyltransferase (EC 2.1.3.2) catalytic chain - Salmonella typhimurium ALTERNATE_NAMES aspartate transcarbamylase catalytic chain; carbamylaspartotranskinase ORGANISM #formal_name Salmonella typhimurium DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 11-Jun-1999 ACCESSIONS S00049 REFERENCE S00028 !$#authors Michaels, G.; Kelln, R.A.; Nargang, F.E. !$#journal Eur. J. Biochem. (1987) 166:55-61 !$#title Cloning, nucleotide sequence and expression of the pyrBI !1operon of Salmonella typhimurium LT2. !$#cross-references MUID:87246692; PMID:3036524 !$#accession S00049 !'##molecule_type DNA !'##residues 1-311 ##label MIC !'##cross-references GB:X05641; NID:g47861; PIDN:CAA29129.1; PID:g47863 COMMENT The active enzyme contains two trimers of catalytic chains !1and three dimers of regulatory chains; it catalyzes the !1rate-limiting step in the biosynthesis of pyrimidines. GENETICS !$#gene pyrB !$#map_position 98 min CLASSIFICATION #superfamily ornithine carbamoyltransferase; aspartate/ !1ornithine carbamoyltransferase homology KEYWORDS heterododecamer; homohexamer; homotrimer; pyrimidine !1nucleotide biosynthesis; transferase FEATURE !$8-305 #domain aspartate/ornithine carbamoyltransferase !8homology #label ACT SUMMARY #length 311 #molecular-weight 34438 #checksum 4073 SEQUENCE /// ENTRY OWSEAC #type complete TITLE aspartate carbamoyltransferase (EC 2.1.3.2) catalytic chain - Serratia marcescens ALTERNATE_NAMES aspartate transcarbamylase catalytic chain; carbamylaspartotranskinase ORGANISM #formal_name Serratia marcescens DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 11-Jun-1999 ACCESSIONS B34396 REFERENCE A34396 !$#authors Beck, D.; Kedzie, K.M.; Wild, J.R. !$#journal J. Biol. Chem. (1989) 264:16629-16637 !$#title Comparison of the aspartate transcarbamoylases from Serratia !1marcescens and Escherichia coli. !$#cross-references MUID:89380286; PMID:2674139 !$#accession B34396 !'##molecule_type DNA !'##residues 1-306 ##label BEC !'##cross-references GB:J05033; NID:g398074; PIDN:AAA26564.1; !1PID:g398075 COMMENT The active enzyme contains two trimers of catalytic chains !1and three dimers of regulatory chains; it catalyzes the !1rate-limiting step in the biosynthesis of pyrimidines. GENETICS !$#gene pyrB CLASSIFICATION #superfamily ornithine carbamoyltransferase; aspartate/ !1ornithine carbamoyltransferase homology KEYWORDS heterododecamer; homohexamer; homotrimer; pyrimidine !1nucleotide biosynthesis; transferase FEATURE !$8-300 #domain aspartate/ornithine carbamoyltransferase !8homology #label ACT SUMMARY #length 306 #molecular-weight 33371 #checksum 6543 SEQUENCE /// ENTRY OWBSAC #type complete TITLE aspartate carbamoyltransferase (EC 2.1.3.2) catalytic chain [validated] - Bacillus subtilis ALTERNATE_NAMES aspartate transcarbamoylase ORGANISM #formal_name Bacillus subtilis DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 15-Sep-2000 ACCESSIONS A25015; C39845; B69686 REFERENCE A25015 !$#authors Lerner, C.G.; Switzer, R.L. !$#journal J. Biol. Chem. (1986) 261:11156-11165 !$#title Cloning and structure of the Bacillus subtilis aspartate !1transcarbamylase gene (pyrB). !$#cross-references MUID:86278215; PMID:3015959 !$#accession A25015 !'##molecule_type DNA !'##residues 1-304 ##label LER !'##cross-references GB:M13128; NID:g143383; PIDN:AAA22685.1; !1PID:g143384 REFERENCE A39845 !$#authors Quinn, C.L.; Stephenson, B.T.; Switzer, R.L. !$#journal J. Biol. Chem. (1991) 266:9113-9127 !$#title Functional organization and nucleotide sequence of the !1Bacillus subtilis pyrimidine biosynthetic operon. !$#cross-references MUID:91225016; PMID:1709162 !$#accession C39845 !'##molecule_type DNA !'##residues 1-304 ##label QUI !'##cross-references GB:M59757; NID:g4887706; PIDN:AAA21267.1; !1PID:g143387 REFERENCE A52046 !$#authors Stevens, R.C.; Reinisch, K.M.; Lipscomb, W.N. !$#submission submitted to the Brookhaven Protein Data Bank, July 1992 !$#cross-references PDB:2AT2 !$#contents annotation; X-ray crystallography, 3.0 angstroms, residues !11-295 REFERENCE A41114 !$#authors Stevens, R.C.; Reinisch, K.M.; Lipscomb, W.N. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:6087-6091 !$#title Molecular structure of Bacillus subtilis aspartate !1transcarbamoylase at 3.0 angstrom resolution. !$#cross-references MUID:91296766; PMID:1906175 !$#contents annotation; X-ray crystallography, 3.0 angstroms REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69686 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-304 ##label KUN !'##cross-references GB:Z99112; GB:AL009126; NID:g2633902; !1PIDN:CAB13423.1; PID:g2633922 !'##experimental_source strain 168 GENETICS !$#gene pyrB !$#map_position 37 min COMPLEX heterododecamer consisting of two trimers of catalytic !1chains and three dimers of regulatory chains FUNCTION !$#description catalyzes the reaction of carbamoyl phosphate with aspartic !1acid to form carbamoyl aspartate and phosphoric acid !$#pathway pyrimidine nucleotide biosynthesis !$#note this is the rate-limiting step in this pathway CLASSIFICATION #superfamily ornithine carbamoyltransferase; aspartate/ !1ornithine carbamoyltransferase homology KEYWORDS heterododecamer; homohexamer; homotrimer; pyrimidine !1nucleotide biosynthesis; transferase FEATURE !$2-289 #domain aspartate/ornithine carbamoyltransferase !8homology #label ACT SUMMARY #length 304 #molecular-weight 34170 #checksum 9007 SEQUENCE /// ENTRY OWHU #type complete TITLE ornithine carbamoyltransferase (EC 2.1.3.3) precursor - human ALTERNATE_NAMES citrulline phosphorylase; ornithine transcarbamylase ORGANISM #formal_name Homo sapiens #common_name man DATE 28-Feb-1986 #sequence_revision 31-Mar-1993 #text_change 16-Jun-2000 ACCESSIONS A41444; B41444; A00562; I38078; JC4672; I59039; I54377 REFERENCE A41444 !$#authors Hata, A.; Tsuzuki, T.; Shimada, K.; Takiguchi, M.; Mori, M.; !1Matsuda, I. !$#journal J. Biochem. (1988) 103:302-308 !$#title Structure of the human ornithine transcarbamylase gene. !$#cross-references MUID:88227905; PMID:2836378 !$#accession A41444 !'##molecule_type DNA !'##residues 1-354 ##label HAT !'##cross-references GB:D00230; NID:g219957; PIDN:BAA00161.1; !1PID:g219959 !$#accession B41444 !'##molecule_type mRNA !'##residues 1-354 ##label HA2 !'##cross-references GB:D00230; NID:g219957; PIDN:BAA00161.1; !1PID:g219959 REFERENCE A00562 !$#authors Horwich, A.L.; Fenton, W.A.; Williams, K.R.; Kalousek, F.; !1Kraus, J.P.; Doolittle, R.F.; Konigsberg, W.; Rosenberg, !1L.E. !$#journal Science (1984) 224:1068-1074 !$#title Structure and expression of a complementary DNA for the !1nuclear coded precursor of human mitochondrial ornithine !1transcarbamylase. !$#cross-references MUID:84196410; PMID:6372096 !$#accession A00562 !'##molecule_type mRNA !'##residues 1-100,'F',102-110,'P',112-192,'CF',195-269,'R',271-354 !1##label HOR !'##cross-references GB:D00230 REFERENCE I38078 !$#authors Hata, A.; Tsuzuki, T.; Shimada, K.; Takiguchi, M.; Mori, M.; !1Matsuda, I. !$#journal J. Biochem. (1986) 100:717-725 !$#title Isolation and characterization of the human ornithine !1transcarbamylase gene: structure of the 5'-end region. !$#cross-references MUID:87057134; PMID:3782067 !$#accession I38078 !'##status translation not shown !'##molecule_type DNA !'##residues 1-26 ##label RES !'##cross-references EMBL:X04443; NID:g35162; PIDN:CAA28039.1; !1PID:g35163 REFERENCE JC4672 !$#authors Wheeler, V.C.; Prodromou, C.P.; Pearl, L.H.; Williamson, R.; !1Coutelle, C. !$#journal Gene (1996) 169:251-255 !$#title Synthesis of a modified gene encoding human ornithine !1transcarbamylase for expression in mammalian mitochondrial !1and universal translation systems: A novel approach towards !1correction of a genetic defect. !$#cross-references MUID:96194812; PMID:8647457 !$#accession JC4672 !'##molecule_type DNA !'##residues 'M',33-100,'F',102-110,'P',112-192,'CF',195-269,'R',271-354 !1##label WHE !'##note this report represents a synthetic gene designed for expression !1in (rather than transport to) mitochondria; the gene product !1when expressed in Escherichia coli was not functional REFERENCE I59039 !$#authors Horwich, A.L.; Kalousek, F.; Rosenberg, L.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:4930-4933 !$#title Arginine in the leader peptide is required for both import !1and proteolytic cleavage of a mitochondrial precursor. !$#cross-references MUID:85270440; PMID:3895227 !$#accession I59039 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-36 ##label RE2 !'##cross-references GB:M11235; NID:g189408; PIDN:AAA59976.1; !1PID:g189409 REFERENCE I54377 !$#authors Gilbert-Dussardier, B.; Rabier, D.; Strautnieks, S.; Segues, !1B.; Bonnefont, J.P.; Munnich, A. !$#journal Hum. Mol. Genet. (1994) 3:831-832 !$#title A novel arginine (245) to glutamine change in exon 8 of the !1ornithine carbamoyl transferase gene in two unrelated !1children presenting with late onset deficiency and showing !1the same enzymatic pattern. !$#cross-references MUID:94362689; PMID:8081373 !$#accession I54377 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 269-276,'Q',278-289 ##label RE3 !'##cross-references GB:S73640; NID:g688001; PIDN:AAB31859.1; !1PID:g688002 !'##note this sequence represents a disease defect in ornithine !1carbamoyltransferase COMMENT The active enzyme is a dimer of identical chains with one !1tightly bound zinc atom per chain; it catalyzes the !1reversible cyclization of carbamyl aspartate to !1dihydroorotate, one step in the synthesis of UMP. COMMENT The active enzyme catalyzes the condensation of carbamoyl !1phosphate and ornithine into citrulline, a step in the !1arginine biosynthesis pathway. GENETICS !$#gene GDB:OTC !'##cross-references GDB:119468; OMIM:311250 !$#map_position Xp21.1-Xp21.1 CLASSIFICATION #superfamily ornithine carbamoyltransferase; aspartate/ !1ornithine carbamoyltransferase homology KEYWORDS arginine biosynthesis; homotrimer; mitochondrion; !1transferase; urea cycle FEATURE !$1-32 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$33-354 #product ornithine carbamoyltransferase #status !8predicted #label MAT\ !$40-342 #domain aspartate/ornithine carbamoyltransferase !8homology #label ACT SUMMARY #length 354 #molecular-weight 39901 #checksum 1397 SEQUENCE /// ENTRY OWRT #type complete TITLE ornithine carbamoyltransferase (EC 2.1.3.3) precursor - rat ALTERNATE_NAMES citrulline phosphorylase; ornithine transcarbamylase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 11-Jun-1999 ACCESSIONS A00563; A28042; A23090; S02466; I52976; I67609; I53457 REFERENCE A00563 !$#authors Takiguchi, M.; Miura, S.; Mori, M.; Tatibana, M.; Nagata, !1S.; Kaziro, Y. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:7412-7416 !$#title Molecular cloning and nucleotide sequence of cDNA for rat !1ornithine carbamoyltransferase precursor. !$#cross-references MUID:85063800; PMID:6095294 !$#accession A00563 !'##molecule_type mRNA !'##residues 1-354 ##label TAK1 !'##cross-references GB:K03040; NID:g205873; PIDN:AAA41768.1; !1PID:g205874 REFERENCE A28042 !$#authors Takiguchi, M.; Murakami, T.; Miura, S.; Mori, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:6136-6140 !$#title Structure of the rat ornithine carbamoyltransferase gene, a !1large, X chromosome-linked gene with an atypical promoter. !$#cross-references MUID:87317609; PMID:3476935 !$#accession A28042 !'##molecule_type DNA !'##residues 1-354 ##label TAK2 !'##cross-references GB:M16933; GB:J02957; NID:g205884; PIDN:AAA41769.1; !1PID:g205886 REFERENCE A23090 !$#authors Kraus, J.P.; Hodges, P.E.; Williamson, C.L.; Horwich, A.L.; !1Kalousek, F.; Williams, K.R.; Rosenberg, L.E. !$#journal Nucleic Acids Res. (1985) 13:943-952 !$#title A cDNA clone for the precursor of rat mitochondrial !1ornithine transcarbamylase: comparison of rat and human !1leader sequences and conservation of catalytic sites. !$#cross-references MUID:85215524; PMID:3839075 !$#accession A23090 !'##molecule_type mRNA !'##residues 1-38,'P',40-240,'S',242-354 ##label KRA !'##cross-references GB:X01976 REFERENCE S02466 !$#authors Aoki, Y.; Sunaga, H.; Suzuki, K.T. !$#journal Biochem. J. (1988) 250:735-742 !$#title A cadmium-binding protein in rat liver identified as !1ornithine carbamoyltransferase. !$#cross-references MUID:88268748; PMID:3390141 !$#accession S02466 !'##molecule_type protein !'##residues 33-56;293-302;307-317;322-329 ##label AOK REFERENCE I52976 !$#authors McIntyre, P.; Graf, L.; Mercer, J.F.B.; Wake, S.A.; Hudson, !1P.J.; Hoogenraad, N. !$#journal DNA (1985) 4:147-156 !$#title The primary structure of the imported mitochondrial protein, !1ornithine transcarbamylase from rat liver: mRNA levels !1during ontogeny. !$#cross-references MUID:85203360; PMID:3838931 !$#accession I52976 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-354 ##label RES !'##cross-references GB:M11266; NID:g205871; PIDN:AAA41767.1; !1PID:g205872 REFERENCE I53457 !$#authors McIntyre, P.; Graf, L.; Mercer, J.; Peterson, G.; Hudson, !1P.J.; Hoogenraad, N. !$#journal FEBS Lett. (1984) 177:41-46 !$#title A highly basic N-terminal extension of the mitochondrial !1matrix enzyme ornithine transcarbamylase from rat liver. !$#cross-references MUID:85051832; PMID:6548714 !$#accession I67609 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-102 ##label RE2 !'##cross-references EMBL:X01178; NID:g56802; PIDN:CAA25618.1; !1PID:g56803 !$#accession I53457 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-43,'N',45-99,'R',101-102 ##label RE3 !'##cross-references GB:K03041; NID:g205889; PIDN:AAA41771.1; !1PID:g205890 GENETICS !$#introns 26/2; 72/3; 100/1; 129/2; 180/3; 221/3; 239/3; 289/3; 335/3 CLASSIFICATION #superfamily ornithine carbamoyltransferase; aspartate/ !1ornithine carbamoyltransferase homology KEYWORDS arginine biosynthesis; homotrimer; mitochondrion; !1transferase; urea cycle FEATURE !$1-32 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$33-354 #product ornithine carbamoyltransferase #status !8predicted #label MAT\ !$40-342 #domain aspartate/ornithine carbamoyltransferase !8homology #label ACT SUMMARY #length 354 #molecular-weight 39886 #checksum 5233 SEQUENCE /// ENTRY OWMS #type complete TITLE ornithine carbamoyltransferase (EC 2.1.3.3) precursor - mouse ALTERNATE_NAMES citrulline phosphorylase; ornithine transcarbamylase ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Mar-1993 #sequence_revision 13-Mar-1997 #text_change 11-Jun-1999 ACCESSIONS A43609; S03407; I55252 REFERENCE A43609 !$#authors Veres, G.; Gibbs, R.A.; Scherer, S.E.; Caskey, C.T. !$#journal Science (1987) 237:415-417 !$#title The molecular basis of the sparse fur mouse mutation. !$#cross-references MUID:87263407; PMID:3603027 !$#accession A43609 !'##status preliminary !'##molecule_type mRNA !'##residues 1-354 ##label VER !'##cross-references GB:M17030; NID:g200162; PIDN:AAA39865.1; !1PID:g200163 REFERENCE S03407 !$#authors Scherer, S.E.; Veres, G.; Caskey, C.T. !$#journal Nucleic Acids Res. (1988) 16:1593-1601 !$#title The genetic structure of mouse ornithine transcarbamylase. !$#cross-references MUID:88157717; PMID:2831503 !$#accession S03407 !'##status translation not shown !'##molecule_type DNA !'##residues 1-194,'R',196-335 ##label SCH !'##cross-references EMBL:X07092 REFERENCE I55252 !$#authors Veres, G.; Craigen, W.J.; Caskey, C.T. !$#journal J. Biol. Chem. (1986) 261:7588-7591 !$#title The 5' flanking region of the ornithine transcarbamylase !1gene contains DNA sequences regulating tissue-specific !1expression. !$#cross-references MUID:86224037; PMID:3011788 !$#accession I55252 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-19,'LLWFDIF' ##label RES !'##cross-references GB:M12716; NID:g200160; PIDN:AAA39864.1; !1PID:g554248 !'##note the end of this sequence is near the boundary of the cloned !1region and may be artifactual GENETICS !$#gene OTC !$#map_position X !$#introns 26/2; 72/3; 100/1; 129/2; 180/3; 221/3; 239/3; 289/3 CLASSIFICATION #superfamily ornithine carbamoyltransferase; aspartate/ !1ornithine carbamoyltransferase homology KEYWORDS mitochondrion; transferase; urea cycle FEATURE !$1-32 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$33-335 #product ornithine carbamoyltransferase #status !8predicted #label MAT\ !$40-342 #domain aspartate/ornithine carbamoyltransferase !8homology #label ACT SUMMARY #length 354 #molecular-weight 39765 #checksum 5198 SEQUENCE /// ENTRY OWBY #type complete TITLE ornithine carbamoyltransferase (EC 2.1.3.3) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES citrulline phosphorylase; ornithine transcarbamylase; protein J0924; protein YJL088w ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1991 #sequence_revision 08-Sep-1995 #text_change 12-Nov-1999 ACCESSIONS S56020; S00058; S14175; S56865 REFERENCE S56016 !$#authors Miosga, T.; Schaaff-Gerstenschlaeger, I.; Chalwatzis, N.; !1Baur, A.; Boles, E.; Fournier, C.; Schmitt, S.; Velten, C.; !1Wilhelm, N.; Zimmermann, F.K. !$#journal Yeast (1995) 11:681-689 !$#title Sequence analysis of a 33.1 kb fragment from the left arm of !1Saccharomyces cerevisiae chromosome X, including putative !1proteins with leucine zippers, a fungal Zn(II)(2)-Cys(6) !1binuclear cluster domain and a putative alpha-2-SCB-alpha-2 !1binding site. !$#cross-references MUID:96093911; PMID:7483841 !$#accession S56020 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-440 ##label MIO !'##cross-references EMBL:X83502; NID:g929861; PIDN:CAA58480.1; !1PID:g929866 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1994 REFERENCE S00058 !$#authors Huygen, R.; Crabeel, M.; Glansdorff, N. !$#journal Eur. J. Biochem. (1987) 166:371-377 !$#title Nucleotide sequence of the ARG3 gene of the yeast !1Saccharomyces cerevisiae encoding ornithine !1carbamoyltransferase. Comparison with other !1carbamoyltransferases. !$#cross-references MUID:87275920; PMID:3038540 !$#accession S00058 !'##molecule_type DNA !'##residues 103-440 ##label HUY !'##cross-references EMBL:M28301; NID:g171076; PIDN:AAA34433.1; !1PID:g171077 !'##note the sequence from Fig. 3 is inconsistent with that from Fig. 2 !1in having an additional Ala after 223-Ala REFERENCE S14175 !$#authors Crabeel, M.; Huygen, R.; Verschueren, K.; Messenguy, F.; !1Tinel, K.; Cunin, R.; Glansdorff, N. !$#journal Mol. Cell. Biol. (1985) 5:3139-3148 !$#title General amino acid control and specific arginine repression !1in Saccharomyces cerevisiae: physical study of the !1bifunctional regulatory region of the ARG3 gene. !$#cross-references MUID:86310783; PMID:3915770 !$#accession S14175 !'##molecule_type DNA !'##residues 103-128 ##label CRA !'##cross-references EMBL:M11946 REFERENCE S56855 !$#authors Miosga, T.; Schaaff-Gerstenschlaeger, I.; Baur, A.; Boles, !1E.; Chalwatzis, N.; Fournier, C.; Schmitt, S.; Velten, C.; !1Wilhelm, N.; Witzel, A.; Zimmermann, F.K. !$#submission submitted to the Protein Sequence Database, September 1995 !$#accession S56865 !'##molecule_type DNA !'##residues 1-440 ##label MIW !'##cross-references EMBL:Z49363; NID:g1008255; PIDN:CAA89381.1; !1PID:g1008256; GSPDB:GN00010; MIPS:YJL088w GENETICS !$#gene SGD:ARG3; MIPS:YJL088w !'##cross-references SGD:S0003624; MIPS:YJL088w !$#map_position 10L COMPLEX homotrimer FUNCTION !$#description transferase !$#pathway arginine biosynthesis CLASSIFICATION #superfamily ornithine carbamoyltransferase; aspartate/ !1ornithine carbamoyltransferase homology KEYWORDS arginine biosynthesis; homotrimer; transferase FEATURE !$114-430 #domain aspartate/ornithine carbamoyltransferase !8homology #label ACT SUMMARY #length 440 #molecular-weight 49624 #checksum 6044 SEQUENCE /// ENTRY OWASN #type complete TITLE ornithine carbamoyltransferase (EC 2.1.3.3) precursor - Emericella nidulans ALTERNATE_NAMES citrulline phosphorylase; ornithine transcarbamylase ORGANISM #formal_name Emericella nidulans, Aspergillus nidulans DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 07-Jul-1995 ACCESSIONS S07317 REFERENCE S07317 !$#authors Upshall, A.; Gilbert, T.; Saari, G.; O'Hara, P.J.; !1Weglenski, P.; Berse, B.; Miller, K.; Timberlake, W.E. !$#journal Mol. Gen. Genet. (1986) 204:349-354 !$#title Molecular analysis of the argB gene of Aspergillus nidulans. !$#cross-references MUID:87014107; PMID:3020372 !$#accession S07317 !'##molecule_type DNA !'##residues 1-397 ##label UPS !'##cross-references EMBL:M29819 GENETICS !$#gene argB CLASSIFICATION #superfamily ornithine carbamoyltransferase; aspartate/ !1ornithine carbamoyltransferase homology KEYWORDS arginine biosynthesis; homotrimer; mitochondrion; !1transferase FEATURE !$1-24 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$25-359 #product ornithine carbamoyltransferase #status !8predicted #label MAT\ !$72-390 #domain aspartate/ornithine carbamoyltransferase !8homology #label ACT SUMMARY #length 397 #molecular-weight 43441 #checksum 1992 SEQUENCE /// ENTRY OWASG #type complete TITLE ornithine carbamoyltransferase (EC 2.1.3.3) precursor - Aspergillus niger ALTERNATE_NAMES citrulline phosphorylase; ornithine transcarbamylase ORGANISM #formal_name Aspergillus niger DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 11-Jun-1999 ACCESSIONS A27362 REFERENCE A27362 !$#authors Buxton, F.P.; Gwynne, D.I.; Garven, S.; Sibley, S.; Davies, !1R.W. !$#journal Gene (1987) 60:255-266 !$#title Cloning and molecular analysis of the ornithine carbamoyl !1transferase gene of Aspergillus niger. !$#cross-references MUID:88167829; PMID:3443301 !$#accession A27362 !'##molecule_type mRNA !'##residues 1-370 ##label BUX !'##cross-references GB:M19158; NID:g166491; PIDN:AAA32688.1; !1PID:g166492 GENETICS !$#gene argB CLASSIFICATION #superfamily ornithine carbamoyltransferase; aspartate/ !1ornithine carbamoyltransferase homology KEYWORDS arginine biosynthesis; homotrimer; mitochondrion; !1transferase FEATURE !$1-38 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$39-370 #product ornithine carbamoyltransferase #status !8predicted #label MAT\ !$44-363 #domain aspartate/ornithine carbamoyltransferase !8homology #label ACT SUMMARY #length 370 #molecular-weight 39924 #checksum 2634 SEQUENCE /// ENTRY OWCKPT #type complete TITLE ornithine carbamoyltransferase (EC 2.1.3.3) precursor - yeast (Pachysolen tannophilus) ALTERNATE_NAMES citrulline phosphorylase; ornithine transcarbamylase ORGANISM #formal_name Pachysolen tannophilus DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 11-Jun-1999 ACCESSIONS S08643; S09292 REFERENCE S08643 !$#authors Skrzypek, M.; Borsuk, P.; Maleszka, R. !$#journal Yeast (1990) 6:141-148 !$#title Cloning and sequencing of the ornithine carbamoyltransferase !1gene from Pachysolen tannophilus. !$#cross-references MUID:90224363; PMID:2327179 !$#accession S08643 !'##molecule_type DNA !'##residues 1-347 ##label SKR !'##cross-references EMBL:X15412; NID:g3266; PIDN:CAA33458.1; PID:g3267 CLASSIFICATION #superfamily ornithine carbamoyltransferase; aspartate/ !1ornithine carbamoyltransferase homology KEYWORDS arginine biosynthesis; homotrimer; mitochondrion; !1transferase FEATURE !$1-25 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$26-347 #product ornithine carbamoyltransferase #status !8predicted #label MAT\ !$33-340 #domain aspartate/ornithine carbamoyltransferase !8homology #label ACT SUMMARY #length 347 #molecular-weight 38313 #checksum 1311 SEQUENCE /// ENTRY OWZP #type complete TITLE ornithine carbamoyltransferase (EC 2.1.3.3) - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES citrulline phosphorylase; ornithine transcarbamylase ORGANISM #formal_name Schizosaccharomyces pombe DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 10-Dec-1999 ACCESSIONS S22390; T38869; S22175 REFERENCE S22389 !$#authors van Huffel, C.; Dubois, E.; Messenguy, F. !$#journal Eur. J. Biochem. (1992) 205:33-43 !$#title Cloning and sequencing of arg3 and arg11 genes of !1Schizosaccharomyces pombe on a 10-kb DNA fragment. !1Heterologous expression and mitochondrial targeting of their !1translation products. !$#cross-references MUID:92209520; PMID:1313366 !$#accession S22390 !'##molecule_type DNA !'##residues 1-327 ##label VAN !'##cross-references EMBL:X63577; NID:g4907; PIDN:CAA45133.1; PID:g4908 REFERENCE Z21732 !$#authors Connor, R.; Churcher, C.M.; Barrell, B.G.; Rajandream, M.A.; !1Walsh, S.V. !$#submission submitted to the EMBL Data Library, February 1996 !$#accession T38869 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-327 ##label CON !'##cross-references EMBL:Z69727; PIDN:CAA93560.1; GSPDB:GN00066; !1SPDB:SPAC4G9.10 !'##experimental_source strain 972h-; cosmid c4G9 GENETICS !$#gene arg3 !$#map_position 1L CLASSIFICATION #superfamily ornithine carbamoyltransferase; aspartate/ !1ornithine carbamoyltransferase homology KEYWORDS arginine biosynthesis; mitochondrion; transferase FEATURE !$8-315 #domain aspartate/ornithine carbamoyltransferase !8homology #label ACT SUMMARY #length 327 #molecular-weight 36119 #checksum 9240 SEQUENCE /// ENTRY OWECI #type complete TITLE ornithine carbamoyltransferase (EC 2.1.3.3) chain I - Escherichia coli (strain K-12) ALTERNATE_NAMES citrulline phosphorylase chain I; ornithine transcarbamylase chain I ORGANISM #formal_name Escherichia coli DATE 17-Mar-1987 #sequence_revision 30-Jun-1990 #text_change 01-Mar-2002 ACCESSIONS A31314; A00564; S56479; A65238 REFERENCE A31314 !$#authors Kuo, L.C.; Miller, A.W.; Lee, S.; Kozuma, C. !$#journal Biochemistry (1988) 27:8823-8832 !$#title Site-directed mutagenesis of Escherichia coli ornithine !1transcarbamoylase: role of arginine-57 in substrate binding !1and catalysis. !$#cross-references MUID:89207485; PMID:3072022 !$#accession A31314 !'##molecule_type DNA !'##residues 2-334 ##label KUO !'##cross-references GB:J02842; NID:g145343; PIDN:AAA23483.1; !1PID:g145344 !'##experimental_source strain K12 REFERENCE A00564 !$#authors Bencini, D.A.; Houghton, J.E.; Hoover, T.A.; Foltermann, !1K.F.; Wild, J.R.; O'Donovan, G.A. !$#journal Nucleic Acids Res. (1983) 11:8509-8518 !$#title The DNA sequence of argI from Escherichia coli. !$#cross-references MUID:84169495; PMID:6369246 !$#accession A00564 !'##molecule_type DNA !'##residues 1-118,'Q',120,'R',122-138,'IEYK',143-241,'Q',243-251,'A', !1253-314,'G',316-334 ##label BEN !'##cross-references GB:X00210; NID:g40961; PIDN:CAA25037.1; PID:g40962 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56479 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-334 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97150.1; !1PID:g537095 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65238 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-334 ##label BLAT !'##cross-references GB:AE000496; GB:U00096; NID:g2367366; !1PIDN:AAC77211.1; PID:g1790703; UWGP:b4254 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene argI !$#map_position 97 min COMPLEX trimer of identical or nonidentical chains, which are coded !1by two duplicated genes (argI and argF) at different loci CLASSIFICATION #superfamily ornithine carbamoyltransferase; aspartate/ !1ornithine carbamoyltransferase homology KEYWORDS arginine biosynthesis; heterotrimer; homotrimer; transferase FEATURE !$2-334 #product ornithine carbamoyltransferase chain I !8#status predicted #label MAT\ !$7-310 #domain aspartate/ornithine carbamoyltransferase !8homology #label ACT SUMMARY #length 334 #molecular-weight 36907 #checksum 5069 SEQUENCE /// ENTRY OWECF #type complete TITLE ornithine carbamoyltransferase (EC 2.1.3.3) chain F - Escherichia coli (strain K-12) ALTERNATE_NAMES citrulline phosphorylase F; ornithine carbamoyltransferase argF; ornithine transcarbamylase F; OTCase chain F ORGANISM #formal_name Escherichia coli DATE 31-Mar-1993 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS A64753; S07355; A21897 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64753 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-334 ##label BLAT !'##cross-references GB:AE000135; GB:U00096; NID:g1786465; !1PIDN:AAC73376.1; PID:g1786469; UWGP:b0273 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S07355 !$#authors van Vliet, F.; Cunin, R.; Jacobs, A.; Piette, J.; Gigot, D.; !1Lauwereys, M.; Pierard, A.; Glansdorff, N. !$#journal Nucleic Acids Res. (1984) 12:6277-6289 !$#title Evolutionary divergence of genes for ornithine and aspartate !1carbamoyl-transferases - complete sequence and mode of !1regulation of the Escherichia coli argF gene; comparison of !1argF with argI and pyrB. !$#cross-references MUID:84297228; PMID:6382166 !$#accession S07355 !'##molecule_type DNA !'##residues 1-120,'P',122-334 ##label VAN !'##cross-references EMBL:X00759; NID:g40959; PIDN:CAA25329.1; !1PID:g40960 !'##note the authors translated the codon CCG for residue 121 as Ala and !1GCG for residue 220 as Val REFERENCE A91800 !$#authors Falmagne, P.; Portetelle, D.; Stalon, V. !$#journal J. Bacteriol. (1985) 161:714-719 !$#cross-references MUID:85104799; PMID:3968036 !$#accession A21897 !'##molecule_type protein !'##residues 2-41 ##label FAL GENETICS !$#gene argF !$#map_position 7 min COMPLEX homotrimer FUNCTION !$#description catalyzes the conversion of ornithine and carbamoylphosphate !1to citrulline !$#pathway amino acid metabolism; arginine biosynthesis !$#note evolutionary related to aspartate carbamoyltransferase (EC !12.1.3.2) CLASSIFICATION #superfamily ornithine carbamoyltransferase; aspartate/ !1ornithine carbamoyltransferase homology KEYWORDS arginine biosynthesis; homotrimer; transferase FEATURE !$2-334 #product ornithine carbamoyltransferase chain F !8#status experimental #label MAT\ !$7-310 #domain aspartate/ornithine carbamoyltransferase !8homology #label ACT SUMMARY #length 334 #molecular-weight 36827 #checksum 3119 SEQUENCE /// ENTRY OWNHG #type complete TITLE ornithine carbamoyltransferase (EC 2.1.3.3) - Neisseria gonorrhoeae ALTERNATE_NAMES citrulline phosphorylase; ornithine transcarbamylase ORGANISM #formal_name Neisseria gonorrhoeae DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 11-Jun-1999 ACCESSIONS JQ0775 REFERENCE JQ0775 !$#authors Martin, P.R.; Cooperider, J.W.; Mulks, M.H. !$#journal Gene (1990) 94:139-140 !$#title Sequence of the argF gene encoding ornithine !1transcarbamoylase from Neisseria gonorrhoeae. !$#cross-references MUID:91033057; PMID:2121620 !$#accession JQ0775 !'##molecule_type DNA !'##residues 1-331 ##label MAR !'##cross-references GB:M34930; NID:g150240; PIDN:AAA25446.1; !1PID:g150241 GENETICS !$#gene argF CLASSIFICATION #superfamily ornithine carbamoyltransferase; aspartate/ !1ornithine carbamoyltransferase homology KEYWORDS arginine biosynthesis; transferase FEATURE !$6-307 #domain aspartate/ornithine carbamoyltransferase !8homology #label ACT SUMMARY #length 331 #molecular-weight 36732 #checksum 1687 SEQUENCE /// ENTRY OWPSCA #type complete TITLE ornithine carbamoyltransferase (EC 2.1.3.3), catabolic - Pseudomonas aeruginosa ALTERNATE_NAMES catabolic citrulline phosphorylase; catabolic ornithine transcarbamylase ORGANISM #formal_name Pseudomonas aeruginosa #variety strain PAO DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 31-Dec-2000 ACCESSIONS S00032; C82999 REFERENCE S00032 !$#authors Baur, H.; Stalon, V.; Falmagne, P.; Luethi, E.; Haas, D. !$#journal Eur. J. Biochem. (1987) 166:111-117 !$#title Primary and quaternary structure of the catabolic ornithine !1carbamoyltransferase from Pseudomonas aeruginosa: extensive !1sequence homology with the anabolic ornithine !1carbamoyltransferases of Escherichia coli. !$#cross-references MUID:87246664; PMID:3109911 !$#accession S00032 !'##molecule_type DNA !'##residues 1-336 ##label BAU !'##cross-references EMBL:X05637; NID:g45287; PIDN:CAA29124.1; !1PID:g45288 !'##experimental_source strain PAO !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE A82950 !$#authors Stover, C.K.; Pham, X.Q.; Erwin, A.L.; Mizoguchi, S.D.; !1Warrener, P.; Hickey, M.J.; Brinkman, F.S.L.; Hufnagle, !1W.O.; Kowalik, D.J.; Lagrou, M.; Garber, R.L.; Goltry, L.; !1Tolentino, E.; Westbrook-Wadman, S.; Yuan, Y.; Brody, L.L.; !1Coulter, S.N.; Folger, K.R.; Kas, A.; Larbig, K.; Lim, R.M.; !1Smith, K.A.; Spencer, D.H.; Wong, G.K.S.; Wu, Z.; Paulsen, !1I.T.; Reizer, J.; Saier, M.H.; Hancock, R.E.W.; Lory, S.; !1Olson, M.V. !$#journal Nature (2000) 406:959-964 !$#title Complete genome sequence of Pseudomonas aeruginosa PA01, an !1opportunistic pathogen. !$#cross-references MUID:20437337; PMID:10984043 !$#accession C82999 !'##status preliminary !'##molecule_type DNA !'##residues 1-336 ##label STO !'##cross-references GB:AE004930; GB:AE004091; NID:g9951472; !1PIDN:AAG08557.1; GSPDB:GN00131; PASP:PA5172 !'##experimental_source strain PAO1 GENETICS !$#gene arcB; PA5172 FUNCTION !$#description catalyzes the conversion of ornithine and carbamoyl !1phosphate to citrulline !$#pathway amino acid metabolism; arginine biosynthesis !$#note evolutionary related to aspartate carbamoyltransferase (EC !12.1.3.2) CLASSIFICATION #superfamily ornithine carbamoyltransferase; aspartate/ !1ornithine carbamoyltransferase homology KEYWORDS arginine catabolism; homotrimer; transferase FEATURE !$2-336 #product ornithine carbamoyltransferase #status !8experimental #label MAT\ !$8-311 #domain aspartate/ornithine carbamoyltransferase !8homology #label ACT SUMMARY #length 336 #molecular-weight 38108 #checksum 4314 SEQUENCE /// ENTRY OWBS #type complete TITLE ornithine carbamoyltransferase (EC 2.1.3.3) - Bacillus subtilis ALTERNATE_NAMES citrulline phosphorylase; ornithine transcarbamylase ORGANISM #formal_name Bacillus subtilis DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jun-2000 ACCESSIONS S11000; A38768; I40378; A69589; S38434 REFERENCE S10999 !$#authors Mountain, A.; Smith, M.C.M.; Baumberg, S. !$#journal Nucleic Acids Res. (1990) 18:4594 !$#title Nucleotide sequence of the Bacillus subtilis argF gene !1encoding ornithine carbamoyltransferase. !$#cross-references MUID:90356402; PMID:2117745 !$#accession S11000 !'##molecule_type DNA !'##residues 1-319 ##label MOU !'##cross-references EMBL:X53360; NID:g39809; PIDN:CAA37444.1; !1PID:g39811 !$#accession A38768 !'##molecule_type protein !'##residues 1,'X',3-14,'XX',17-20,'X',22-30,'XX',33,'X',35-39 ##label !1MOU2 REFERENCE I40372 !$#authors O'Reilly, M.; Devine, K.M. !$#journal Microbiology (1994) 140:1023-1025 !$#title Sequence and analysis of the citrulline biosynthetic operon !1argC-F from Bacillus subtilis. !$#cross-references MUID:94297722; PMID:8025667 !$#accession I40378 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-319 ##label RES !'##cross-references EMBL:Z26919; NID:g408113; PIDN:CAA81542.1; !1PID:g408120 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69589 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-319 ##label KUN !'##cross-references GB:Z99109; GB:Z99110; GB:AL009126; NID:g2633472; !1PIDN:CAB12982.1; PID:g2633479; NID:g2633260; PID:g2633462 !'##experimental_source strain 168 GENETICS !$#gene argF !$#map_position 100 (degrees) CLASSIFICATION #superfamily ornithine carbamoyltransferase; aspartate/ !1ornithine carbamoyltransferase homology KEYWORDS arginine biosynthesis; transferase FEATURE !$1-319 #product ornithine carbamoyltransferase #status !8experimental #label MAT\ !$12-310 #domain aspartate/ornithine carbamoyltransferase !8homology #label ACT SUMMARY #length 319 #molecular-weight 34663 #checksum 4381 SEQUENCE /// ENTRY OWPSAA #type complete TITLE ornithine carbamoyltransferase (EC 2.1.3.3), anabolic - Pseudomonas aeruginosa ALTERNATE_NAMES anabolic citrulline phosphorylase; anabolic ornithine transcarbamylase ORGANISM #formal_name Pseudomonas aeruginosa DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 11-Jun-1999 ACCESSIONS A32013 REFERENCE A32013 !$#authors Itoh, Y.; Soldati, L.; Stalon, V.; Falmagne, P.; Terawaki, !1Y.; Leisinger, T.; Haas, D. !$#journal J. Bacteriol. (1988) 170:2725-2734 !$#title Anabolic ornithine carbamoyltransferase of Pseudomonas !1aeruginosa: nucleotide sequence and transcriptional control !1of the argF structural gene. !$#cross-references MUID:88227856; PMID:3131308 !$#accession A32013 !'##molecule_type DNA !'##residues 1-305 ##label ITO !'##cross-references GB:M19939; NID:g151038; PIDN:AAA25720.1; !1PID:g151039 !'##note the authors translated the codon GAG for residues 170 and 171 !1as Ala and ATG for residues 172 and 236 as Leu CLASSIFICATION #superfamily ornithine carbamoyltransferase; aspartate/ !1ornithine carbamoyltransferase homology KEYWORDS arginine biosynthesis; homotrimer; transferase FEATURE !$4-299 #domain aspartate/ornithine carbamoyltransferase !8homology #label ACT SUMMARY #length 305 #molecular-weight 34076 #checksum 9936 SEQUENCE /// ENTRY OWPSY #type complete TITLE ornithine carbamoyltransferase (EC 2.1.3.3) - Pseudomonas syringae pv. phaseolicola ALTERNATE_NAMES citrulline phosphorylase; ornithine transcarbamylase ORGANISM #formal_name Pseudomonas syringae pv. phaseolicola DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jun-2000 ACCESSIONS S11943; A43327 REFERENCE S11943 !$#authors Mosqueda, G.; van den Broeck, G.; Saucedo, O.; Bailey, A.M.; !1Alvarez-Morales, A.; Herrera-Estrella, L. !$#journal Mol. Gen. Genet. (1990) 222:461-466 !$#title Isolation and characterization of the gene from Pseudomonas !1syringae pv. phaseolicola encoding the !1phaseolotoxin-insensitive ornithine carbamoyltransferase. !$#cross-references MUID:91109740; PMID:2274044 !$#accession S11943 !'##molecule_type DNA !'##residues 1-327 ##label MOS !'##cross-references GB:D86356; NID:g2077925; PIDN:BAA19878.1; !1PID:g2077926 REFERENCE A43327 !$#authors Hatziloukas, E.; Panopoulos, N.J. !$#journal J. Bacteriol. (1992) 174:5895-5909 !$#title Origin, structure, and regulation of argK, encoding the !1phaseolotoxin-resistant ornithine carbamoyltransferase in !1Pseudomonas syringae pv. phaseolicola, and functional !1expression of argK in transgenic tobacco. !$#cross-references MUID:92394893; PMID:1522066 !$#accession A43327 !'##molecule_type DNA !'##residues 1-327 ##label HAT !'##cross-references GB:D86356; NID:g2077925; PIDN:BAA19878.1; !1PID:g2077926 !'##experimental_source NPS3121, pv. phaseolicola !'##note sequence extracted from NCBI backbone (NCBIP:115416) GENETICS !$#gene argK CLASSIFICATION #superfamily ornithine carbamoyltransferase; aspartate/ !1ornithine carbamoyltransferase homology KEYWORDS arginine biosynthesis; transferase FEATURE !$9-303 #domain aspartate/ornithine carbamoyltransferase !8homology #label ACT SUMMARY #length 327 #molecular-weight 36562 #checksum 8558 SEQUENCE /// ENTRY XJSMIG #type complete TITLE scyllo-inosamine-4-phosphate amidinotransferase (EC 2.1.4.2) II - Streptomyces griseus ORGANISM #formal_name Streptomyces griseus DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 03-Jun-2002 ACCESSIONS S18620; S19781 REFERENCE S18617 !$#authors Pissowotzki, K.; Mansouri, K.; Piepersberg, W. !$#journal Mol. Gen. Genet. (1991) 231:113-123 !$#title Genetics of streptomycin production in Streptomyces griseus: !1molecular structure and putative function of genes !1strELMB2N. !$#cross-references MUID:92092953; PMID:1661369 !$#accession S18620 !'##molecule_type DNA !'##residues 1-349 ##label PIS !'##cross-references EMBL:X62567; NID:g49009; PIDN:CAA44441.1; !1PID:g49011 !'##note the sequence from Fig. 5 is inconsistent with that from Fig. 2 !1in having 98-Gly, 154-Leu, 163-Asp, 253-Arg, 254-Ser, !1255-Arg, 256-Leu, 305-Met and 306-Leu !'##note the authors translated the codon GGC for residue 115 as Asp and !1GAC for residue 116 as Gly GENETICS !$#gene str2B CLASSIFICATION #superfamily inosamine-phosphate amidinotransferase KEYWORDS amidinotransferase; streptomycin biosynthesis SUMMARY #length 349 #molecular-weight 38218 #checksum 2630 SEQUENCE /// ENTRY XJECTK #type complete TITLE transketolase (EC 2.2.1.1) A - Escherichia coli (strain K-12) ALTERNATE_NAMES glycolaldehydetransferase A ORGANISM #formal_name Escherichia coli DATE 31-Mar-1993 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS F65078; S25495; S43433 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65078 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-663 ##label BLAT !'##cross-references GB:AE000376; GB:U00096; NID:g2367176; !1PIDN:AAC75972.1; PID:g2367177; UWGP:b2935 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S25495 !$#authors Sprenger, G.A. !$#submission submitted to the EMBL Data Library, August 1992 !$#accession S25495 !'##molecule_type DNA !'##residues 1-102,'S',104,'V',106,'PL',108-631,'IE',634-663 ##label SPR !'##cross-references EMBL:X68025 REFERENCE S43433 !$#authors Sprenger, G.A. !$#journal Biochim. Biophys. Acta (1993) 1216:307-310 !$#title Nucleotide sequence of the Escherichia coli K-12 !1transketolase (tkt) gene. !$#cross-references MUID:94060107; PMID:8241274 !$#accession S43433 !'##molecule_type DNA !'##residues 1-102,'S',104,'V',106,'PL',108-663 ##label SP2 !'##cross-references EMBL:X68025; NID:g312666; PIDN:CAA48166.1; !1PID:g312667 !'##experimental_source strain K-12 GENETICS !$#gene tktA; tkt !$#map_position 62 min COMPLEX homodimer FUNCTION !$#description catalyzes the formation of D-ribose 5-phosphate and !1D-xylulose 5-phosphate from sedoheptulose 7-phosphate and !1D-glyceraldehyde 3-phosphate using cofactor thiamine !1pyrophosphate CLASSIFICATION #superfamily transketolase; thiamin pyrophosphate-binding !1domain homology KEYWORDS Calvin cycle; homodimer; magnesium; pentose phosphate !1pathway; thiamin pyrophosphate; transferase FEATURE !$144-194 #domain thiamin pyrophosphate-binding domain homology !8#label TPB SUMMARY #length 663 #molecular-weight 72201 #checksum 320 SEQUENCE /// ENTRY A48660 #type complete TITLE transketolase (EC 2.2.1.1) B - Escherichia coli (strain K-12) ALTERNATE_NAMES glycolaldehydetransferase B; transketolase (EC 2.2.1.1) 2 ORGANISM #formal_name Escherichia coli DATE 16-Feb-1994 #sequence_revision 04-Oct-1996 #text_change 01-Mar-2002 ACCESSIONS A48660; H65021 REFERENCE A48660 !$#authors Iida, A.; Teshiba, S.; Mizobuchi, K. !$#journal J. Bacteriol. (1993) 175:5375-5383 !$#title Identification and characterization of the tktB gene !1encoding a second transketolase in Escherichia coli K-12. !$#cross-references MUID:93374831; PMID:8396116 !$#accession A48660 !'##status preliminary !'##molecule_type DNA !'##residues 1-667 ##label IID !'##cross-references GB:D12473; NID:g440349; PIDN:BAA02039.1; !1PID:g460975 !'##experimental_source strain K-12 !'##note sequence extracted from NCBI backbone (NCBIN:137560, !1NCBIP:137561) REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65021 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-667 ##label BLAT !'##cross-references GB:AE000333; GB:U00096; NID:g1788805; !1PIDN:AAC75518.1; PID:g1788808; UWGP:b2465 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene tktB !$#map_position 53 min COMPLEX homodimer FUNCTION !$#description catalyzes the formation of D-ribose 5-phosphate and !1D-xylulose 5-phosphate from sedoheptulose 7-phosphate and !1D-glyceraldehyde 3-phosphate using cofactor thiamine !1pyrophosphate CLASSIFICATION #superfamily transketolase; thiamin pyrophosphate-binding !1domain homology KEYWORDS Calvin cycle; homodimer; magnesium; pentose phosphate !1pathway; thiamin pyrophosphate; transferase FEATURE !$143-193 #domain thiamin pyrophosphate-binding domain homology !8#label TPB SUMMARY #length 667 #molecular-weight 73042 #checksum 3014 SEQUENCE /// ENTRY XJRFTK #type complete TITLE transketolase (EC 2.2.1.1) - Rhodobacter sphaeroides ALTERNATE_NAMES glycolaldehydetransferase ORGANISM #formal_name Rhodobacter sphaeroides DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 15-Oct-1999 ACCESSIONS B41080 REFERENCE A41080 !$#authors Chen, J.H.; Gibson, J.L.; McCue, L.A.; Tabita, F.R. !$#journal J. Biol. Chem. (1991) 266:20447-20452 !$#title Identification, expression, and deduced primary structure of !1transketolase and other enzymes encoded within the form II !1CO-2 fixation operon of Rhodobacter sphaeroides. !$#cross-references MUID:92041881; PMID:1939098 !$#accession B41080 !'##molecule_type DNA !'##residues 1-657 ##label CHE !'##cross-references GB:M68914; NID:g151988; PIDN:AAA26155.1; !1PID:g151990 !'##note the authors translated the codon GGC for residue 173 as Ala COMMENT The active enzyme catalyzes the transfer of a keto group to !1an aldehyde acceptor; it has a broad substrate specificity, !1requires thiamin pyrophosphate as a cofactor and magnesium !1ion for optimal activity. CLASSIFICATION #superfamily transketolase; thiamin pyrophosphate-binding !1domain homology KEYWORDS Calvin cycle; homodimer; magnesium; pentose phosphate !1pathway; thiamin pyrophosphate; transferase FEATURE !$147-197 #domain thiamin pyrophosphate-binding domain homology !8#label TPB SUMMARY #length 657 #molecular-weight 69337 #checksum 452 SEQUENCE /// ENTRY XJSOKP #type complete TITLE transketolase (EC 2.2.1.1) homolog - Streptococcus pneumoniae ALTERNATE_NAMES recP protein ORGANISM #formal_name Streptococcus pneumoniae DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 15-Oct-1999 ACCESSIONS A43018 REFERENCE A43018 !$#authors Radnis, B.A.; Rhee, D.K.; Morrison, D.A. !$#journal J. Bacteriol. (1990) 172:3669-3674 !$#title Genetic transformation in Streptococcus pneumoniae: !1Nucleotide sequence and predicted amino acid sequence of !1recP. !$#cross-references MUID:90299784; PMID:2361942 !$#accession A43018 !'##molecule_type DNA !'##residues 1-656 ##label RAD !'##cross-references GB:M31296; NID:g153791; PIDN:AAA26967.1; !1PID:g153792 !'##experimental_source strain CP1200 GENETICS !$#gene recP CLASSIFICATION #superfamily transketolase; thiamin pyrophosphate-binding !1domain homology KEYWORDS Calvin cycle; homodimer; magnesium; pentose phosphate !1pathway; thiamin pyrophosphate; transferase FEATURE !$141-195 #domain thiamin pyrophosphate-binding domain homology !8#label TPB SUMMARY #length 656 #molecular-weight 71662 #checksum 6274 SEQUENCE /// ENTRY XJBYTK #type complete TITLE transketolase (EC 2.2.1.1) TKL1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES glycolaldehydetransferase; protein YP9499.29c; protein YPR074c ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1993 #sequence_revision 25-Apr-1997 #text_change 21-Jul-2000 ACCESSIONS A49510; S54095; S69062; A42084; S21067; S74183; S37409 REFERENCE A49510 !$#authors Sundstroem, M.; Lindqvist, Y.; Schneider, G.; Hellman, U.; !1Ronne, H. !$#journal J. Biol. Chem. (1993) 268:24346-24352 !$#title Yeast TKL1 gene encodes a transketolase that is required for !1efficient glycolysis and biosynthesis of aromatic amino !1acids. !$#cross-references MUID:94043273; PMID:8226984 !$#accession A49510 !'##status preliminary !'##molecule_type DNA !'##residues 1-680 ##label SUN !'##cross-references EMBL:X73224; NID:g404200; PIDN:CAA51693.1; !1PID:g404201 REFERENCE S54059 !$#authors Badcock, K.; Churcher, C.M. !$#submission submitted to the EMBL Data Library, May 1995 !$#accession S54095 !'##molecule_type DNA !'##residues 1-680 ##label BAD !'##cross-references EMBL:Z49219; NID:g805025; PIDN:CAA89191.1; !1PID:g805054; GSPDB:GN00016; MIPS:YPR074c !'##experimental_source strain AB972 REFERENCE S69057 !$#authors Couch, J. !$#submission submitted to the EMBL Data Library, March 1996 !$#description The sequence of S. cerevisiae cosmid 9513. !$#accession S69062 !'##molecule_type DNA !'##residues 1-680 ##label COU !'##cross-references EMBL:U51033; NID:g1230676; PIDN:AAB68125.1; !1PID:g1230682; GSPDB:GN00016; MIPS:YPR074c REFERENCE A42084 !$#authors Fletcher, T.S.; Kwee, I.L.; Nakada, T.; Largman, C.; Martin, !1B.M. !$#journal Biochemistry (1992) 31:1892-1896 !$#title DNA sequence of the yeast transketolase gene. !$#cross-references MUID:92144611; PMID:1737042 !$#accession A42084 !'##molecule_type DNA !'##residues 1-36,'RS',39-44,'GESNAHEPNQPKTGSTEIDLSCLTVTRSLCCIY',78-135, !1'DMPLTTSRA',144-231,'R',233,'R',235-242,'FDQNDHNHWLRFLRS', !1258-383,'VLPIL',384-395,'S',397-527,'PDKTCHNWKVAL',539-638, !1'PVRHQKSSSSSVSPQKVILKELKRPLHSIRVTS' ##label FLE !'##cross-references GB:M63302 REFERENCE S21067 !$#authors Nixon, P.F.; Duggleby, R.G. !$#journal Protein Seq. Data Anal. (1991) 4:325-326 !$#title The N-terminal amino acid sequence of yeast transketolase. !$#cross-references MUID:92253546; PMID:1812485 !$#accession S21067 !'##molecule_type protein !'##residues 2-36 ##label NIX REFERENCE S74183 !$#authors Kovina, M.; Viryasov, M.; Baratova, L.; Kochetov, G. !$#journal FEBS Lett. (1996) 392:293-294 !$#title Localization of reactive tyrosine residues of baker's yeast !1transketolase. !$#cross-references MUID:96371030; PMID:8774865 !$#accession S74183 !'##molecule_type protein !'##residues 181-187;209-213;368-373;104-105 ##label KOV COMMENT The active enzyme catalyzes the transfer of a keto group to !1an aldehyde acceptor; it has a broad substrate specificity, !1requires thiamine pyrophosphate as a cofactor and magnesium !1ion for optimal activity. GENETICS !$#gene SGD:TKL1; MIPS:YPR074c !'##cross-references SGD:S0006278; MIPS:YPR074c !$#map_position 16R COMPLEX homodimer FUNCTION !$#description transferase !$#pathway pentose phosphate pathway CLASSIFICATION #superfamily transketolase; thiamin pyrophosphate-binding !1domain homology KEYWORDS homodimer; magnesium; pentose phosphate pathway; thiamin !1pyrophosphate; transferase FEATURE !$2-680 #product transketolase #status experimental #label !8MAT\ !$146-196 #domain thiamin pyrophosphate-binding domain homology !8#label TPB SUMMARY #length 680 #molecular-weight 73805 #checksum 3800 SEQUENCE /// ENTRY XJHQFK #type complete TITLE formaldehyde transketolase (EC 2.2.1.3) - yeast (Pichia angusta) ALTERNATE_NAMES dihydroxyacetone synthase; glycerone synthase ORGANISM #formal_name Pichia angusta DATE 31-Mar-1993 #sequence_revision 30-Sep-1993 #text_change 20-Apr-2000 ACCESSIONS A23009; S30110 REFERENCE A23009 !$#authors Janowicz, Z.A.; Eckart, M.R.; Drewke, C.; Roggenkamp, R.O.; !1Hollenberg, C.P. !$#journal Nucleic Acids Res. (1985) 13:3043-3062 !$#title Cloning and characterization of the DAS gene encoding the !1major methanol assimilatory enzyme from the methylotrophic !1yeast Hansenula polymorpha. !$#cross-references MUID:85215670; PMID:2987872 !$#accession A23009 !'##molecule_type DNA !'##residues 1-693,'RLPGPEGKA' ##label JAN !'##cross-references GB:X02424 !'##experimental_source ATCC 34438 !'##note this sequence has been revised in reference S30110 REFERENCE S30110 !$#authors Hansen, H.; Didion, T.; Thiemann, A.; Veenhuis, M.; !1Roggenkamp, R. !$#journal Mol. Gen. Genet. (1992) 235:269-278 !$#title Targeting sequences of the two major peroxisomal proteins in !1the methylotrophic yeast Hansenula polymorpha. !$#cross-references MUID:93101130; PMID:1465101 !$#accession S30110 !'##molecule_type DNA !'##residues 667-710 ##label HAN !'##cross-references EMBL:X02424 !'##note this is a revision to the sequence from reference A23009 COMMENT This is the major methanol assimilatory enzyme from this !1methylotrophic organism. GENETICS !$#gene DAS CLASSIFICATION #superfamily transketolase; thiamin pyrophosphate-binding !1domain homology KEYWORDS peroxisome; thiamin pyrophosphate; transferase FEATURE !$158-208 #domain thiamin pyrophosphate-binding domain homology !8#status atypical #label TPB\ !$708-710 #region peroxisome/glyoxysome location signal #status !8atypical SUMMARY #length 710 #molecular-weight 78842 #checksum 6780 SEQUENCE /// ENTRY XXECPL #type complete TITLE ribosomal-protein-serine N-acetyltransferase (EC 2.3.1.-) rimL - Escherichia coli (strain K-12) ALTERNATE_NAMES peptide N-acetyltransferase rimL ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 01-Mar-2002 ACCESSIONS S04776; F64894 REFERENCE S04776 !$#authors Tanaka, S.; Matsushita, Y.; Yoshikawa, A.; Isono, K. !$#journal Mol. Gen. Genet. (1989) 217:289-293 !$#title Cloning and molecular characterization of the gene rimL !1which encodes an enzyme acetylating ribosomal protein L12 of !1Escherichia coli K12. !$#cross-references MUID:89364711; PMID:2671655 !$#accession S04776 !'##molecule_type DNA !'##residues 1-179 ##label TAN !'##cross-references GB:X15860; NID:g42748; PIDN:CAA33869.1; PID:g42749 !'##experimental_source strain K-12, substrain KL14 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64894 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-179 ##label BLAT !'##cross-references GB:AE000240; GB:U00096; NID:g1787695; !1PIDN:AAC74509.1; PID:g1787697; UWGP:b1427 !'##experimental_source strain K-12, substrain MG1655 COMMENT For ribosomal protein L7/L12, see PIR:R5EC7. GENETICS !$#gene rimL !$#map_position 33 min FUNCTION !$#description catalyzes the acetylation by acetyl-CoA of the !1amino-terminal serine of ribosomal protein L12 (converting !1it to ribosomal protein L7) CLASSIFICATION #superfamily Escherichia coli ribosomal-protein-serine !1N-acetyltransferase rimL KEYWORDS acetyl-CoA; acyltransferase FEATURE !$98 #active_site Tyr #status predicted SUMMARY #length 179 #molecular-weight 20680 #checksum 440 SEQUENCE /// ENTRY F69768 #type complete TITLE ribosomal-protein-serine N-acetyltransferase (EC 2.3.1.-) rimL homolog ydaF - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 24-Sep-1999 #sequence_revision 24-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS F69768 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69768 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-183 ##label KUN !'##cross-references GB:Z99106; GB:AL009126; NID:g2632653; !1PIDN:CAB12228.1; PID:g2632721 !'##experimental_source strain 168 GENETICS !$#gene ydaF CLASSIFICATION #superfamily Escherichia coli ribosomal-protein-serine !1N-acetyltransferase rimL KEYWORDS acetyl-CoA; acyltransferase FEATURE !$98 #active_site Tyr #status predicted SUMMARY #length 183 #molecular-weight 21025 #checksum 7458 SEQUENCE /// ENTRY XXFOGA #type complete TITLE phosphatidylcholine-sterol O-acyltransferase (EC 2.3.1.43) precursor - Aeromonas hydrophila ALTERNATE_NAMES lecithin-cholesterol acyltransferase; phospholipid-cholesterol acyltransferase ORGANISM #formal_name Aeromonas hydrophila DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 03-Jun-2002 ACCESSIONS A36035; JS0320 REFERENCE A36035 !$#authors Hilton, S.; McCubbin, W.D.; Kay, C.M.; Buckley, J.T. !$#journal Biochemistry (1990) 29:9072-9078 !$#title Purification and spectral study of a microbial fatty !1acyltransferase: activation by limited proteolysis. !$#cross-references MUID:91104814; PMID:2271578 !$#accession A36035 !'##molecule_type DNA !'##residues 1-335 ##label HIL !'##cross-references GB:M59478 REFERENCE JS0320 !$#authors Thornton, J.; Howard, S.P.; Buckley, J.T. !$#journal Biochim. Biophys. Acta (1988) 959:153-159 !$#title Molecular cloning of a phospholipid-cholesterol !1acyltransferase from Aeromonas hydrophila. Sequence !1homologies with lecithin-cholesterol acyltransferase and !1other lipases. !$#cross-references MUID:88163749; PMID:3280033 !$#accession JS0320 !'##molecule_type DNA !'##residues 1-299 ##label THO !'##cross-references GB:X07279 COMMENT This enzyme catalyzes fatty acid transfer between !1phosphatidylcholine and cholesterol. In the absence of acyl !1acceptors, this protein also acts as a phospholipase and !1hydrolyzes other hydrophobic substrates such as cholesteryl !1ester under some conditions. CLASSIFICATION #superfamily phosphatidylcholine-sterol O-acyltransferase KEYWORDS acyltransferase; carboxylic ester hydrolase FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-335 #product phosphatidylcholine-sterol O-acyltransferase !8#status predicted #label MAT SUMMARY #length 335 #molecular-weight 37121 #checksum 6927 SEQUENCE /// ENTRY A53888 #type complete TITLE thermolabile hemolysin (EC 3.1.1.-) precursor - Vibrio parahaemolyticus ALTERNATE_NAMES lecithin-dependent hemolysin ORGANISM #formal_name Vibrio parahaemolyticus DATE 07-Oct-1994 #sequence_revision 07-Oct-1994 #text_change 11-Jun-1999 ACCESSIONS A53888; A49827; B49827; A39996; B39996 REFERENCE A53888 !$#authors Taniguchi, H.; Hirano, H.; Kubomura, S.; Higashi, K.; !1Mizuguchi, Y. !$#journal Microb. Pathog. (1986) 1:425-432 !$#title Comparison of the nucleotide sequences of the genes for the !1thermostable direct hemolysin and the thermolabile hemolysin !1from Vibrio parahaemolyticus. !$#cross-references MUID:89237825; PMID:3508495 !$#accession A53888 !'##molecule_type DNA !'##residues 1-418 ##label TAN !'##cross-references GB:M36437; NID:g155177; PIDN:AAA27526.1; !1PID:g155178 REFERENCE A49827 !$#authors Shinoda, S.; Matsuoka, H.; Tsuchie, T.; Miyoshi, S.; !1Yamamoto, S.; Taniguchi, H.; Mizuguchi, Y. !$#journal J. Gen. Microbiol. (1991) 137:2705-2711 !$#title Purification and characterization of a lecithin-dependent !1haemolysin from Escherichia coli transformed by a Vibrio !1parahaemolyticus gene. !$#cross-references MUID:92166705; PMID:1791426 !$#accession A49827 !'##molecule_type protein !'##residues 'T',21-32 ##label SHI !'##experimental_source E. coli strain C600 transformed with plasmid !1pHL591 !'##note submitted to the Protein Sequence Database, October 1991 !$#accession B49827 !'##molecule_type protein !'##residues 33-41,'X',43-45,'X',47 ##label SH2 !'##experimental_source C600, plasmid pHL591 !'##note submitted to the Protein Sequence Database, October 1991 COMMENT This hemolysin hydrolyzes phosphatidylcholine to !1lysophosphatidylcholine (which is hemolytic) and then !1further to glycerophosphorylcholine. CLASSIFICATION #superfamily phosphatidylcholine-sterol O-acyltransferase KEYWORDS carboxylic ester hydrolase; hemolysis FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-418 #product thermolabile hemolysin, long form #status !8experimental #label MATL\ !$33-418 #product thermolabile hemolysin, short form #status !8experimental #label MATS SUMMARY #length 418 #molecular-weight 47377 #checksum 4112 SEQUENCE /// ENTRY XYBYT1 #type complete TITLE protein N-acetyltransferase (EC 2.3.1.-) chain NAT1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein D2720; protein N-acetyltransferase chain AAT1; protein YDL040c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jun-2000 ACCESSIONS S05783; A34321; S15065; S05745; S17241; S67573 REFERENCE A34321 !$#authors Lee, F.J.S.; Lin, L.W.; Smith, J.A. !$#journal J. Biol. Chem. (1989) 264:12339-12343 !$#title Molecular cloning and sequencing of a cDNA encoding N !1(alpha)-acetyltransferase from Saccharomyces cerevisiae. !$#cross-references MUID:89308659; PMID:2663856 !$#accession S05783 !'##molecule_type mRNA !'##residues 1-854 ##label LEE !'##cross-references EMBL:M23166; NID:g172027; PIDN:AAA88728.1; !1PID:g172028 !'##note the authors translated the codon GTA for residue 226 as Tyr !$#accession A34321 !'##molecule_type protein !'##residues !161-101;130-142;151-159;301-307;313-327;331-354;471-479; !1587-596;598-606;614-622;668-683;685-705 ##label LEE2 REFERENCE S15065 !$#authors Grunstein, M. !$#submission submitted to the EMBL Data Library, April 1989 !$#accession S15065 !'##molecule_type DNA !'##residues 1-854 ##label GRU !'##cross-references EMBL:X15135; NID:g4027; PIDN:CAA33233.1; PID:g4028 REFERENCE S05745 !$#authors Mullen, J.R.; Kayne, P.S.; Moerschell, R.P.; Tsunasawa, S.; !1Gribskov, M.; Colavito-Shepanski, M.; Grunstein, M.; !1Sherman, F.; Sternglanz, R. !$#journal EMBO J. (1989) 8:2067-2075 !$#title Identification and characterization of genes and mutants for !1an N-terminal acetyltransferase from yeast. !$#cross-references MUID:90005412; PMID:2551674 !$#accession S05745 !'##molecule_type DNA !'##residues 1-496,'LV',500-854 ##label MUL !'##cross-references EMBL:X15135 REFERENCE S05891 !$#authors Shore, D.; Squire, M.; Nasmyth, K.A. !$#journal EMBO J. (1984) 3:2817-2823 !$#title Characterization of two genes required for the !1position-effect control of yeast mating-type genes. !$#cross-references MUID:85126876; PMID:6098447 !$#accession S17241 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 613-853 ##label SHO !'##cross-references EMBL:X01419 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1984 REFERENCE S67560 !$#authors Paulin, L.; Saren, A.M.; Laamanen, P. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67573 !'##molecule_type DNA !'##residues 1-854 ##label PAU !'##cross-references EMBL:Z74088; NID:g1431024; PIDN:CAA98599.1; !1PID:g1431025; GSPDB:GN00004; MIPS:YDL040c !'##experimental_source strain S288C GENETICS !$#gene SGD:NAT1; AAA1; AAT1; MIPS:YDL040c !'##cross-references SGD:S0002198; MIPS:YDL040c !$#map_position 4L CLASSIFICATION #superfamily protein N-acetyltransferase chain NAT1 KEYWORDS acetyl-CoA; acetylated amino end; acyltransferase; blocked !1amino end FEATURE !$2-854 #product protein N-acetyltransferase chain NAT1 !8#status predicted #label MAT\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status predicted SUMMARY #length 854 #molecular-weight 98904 #checksum 2422 SEQUENCE /// ENTRY XYECAA #type complete TITLE amino-acid N-acetyltransferase (EC 2.3.1.1) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 01-Mar-2002 ACCESSIONS A30372; C65064; Q00382 REFERENCE A30372 !$#authors Brown, K.; Finch, P.W.; Hickson, I.D.; Emmerson, P.T. !$#journal Nucleic Acids Res. (1987) 15:10586 !$#title Complete nucleotide sequence of the Escherichia coli argA !1gene. !$#cross-references MUID:88096590; PMID:3320971 !$#accession A30372 !'##molecule_type DNA !'##residues 1-443 ##label BRO !'##cross-references EMBL:Y00492; NID:g40952; PIDN:CAA68547.1; !1PID:g581038 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65064 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-443 ##label BLAT !'##cross-references GB:AE000365; GB:U00096; NID:g2367163; !1PIDN:AAC75857.1; PID:g1789181; UWGP:b2818 !'##experimental_source strain K-12, substrain MG1655 COMMENT This enzyme catalyzes the first reaction, the transfer of !1the acetyl group from acetyl-CoA to glutamate, in the !1arginine biosynthesis pathway. GENETICS !$#gene argA !$#map_position 61 min !$#start_codon GTG CLASSIFICATION #superfamily amino-acid acetyltransferase KEYWORDS acyltransferase; arginine biosynthesis; coenzyme A SUMMARY #length 443 #molecular-weight 49195 #checksum 9937 SEQUENCE /// ENTRY JQ0377 #type complete TITLE 4''-O-acyltransferase (EC 2.3.1.-) acyB1 - Streptomyces sp. ALTERNATE_NAMES 4''-mycarosyl isovaleryl-CoA transferase ORGANISM #formal_name Streptomyces sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS JQ0377; JC2031 REFERENCE JQ0377 !$#authors Epp, J.K.; Huber, M.L.B.; Turner, J.R.; Goodson, T.; !1Schoner, B.E. !$#journal Gene (1989) 85:293-301 !$#title Production of a hybrid macrolide antibiotic in Streptomyces !1ambofaciens and Streptomyces lividans by introduction of a !1cloned carbomycin biosynthetic gene from Streptomyces !1thermotolerans. !$#cross-references MUID:90185202; PMID:2628170 !$#accession JQ0377 !'##molecule_type DNA !'##residues 1-388 ##label EPP !'##cross-references GB:D31821; NID:g506870; PIDN:BAA06607.1; !1PID:g506872 !'##note the source is designated as Streptomyces thermotolerans REFERENCE JC2031 !$#authors Arisawa, A.; Kawamura, N.; Tsunekawa, H.; Okamura, K.; Tone, !1H.; Okamoto, R. !$#journal Biosci. Biotechnol. Biochem. (1993) 57:2020-2025 !$#title Cloning and nucleotide sequences of two genes involved in !1the 4''-O-acylation of macrolide antibiotics from !1Streptomyces thermotolerans. !$#cross-references MUID:94122440; PMID:7764361 !$#accession JC2031 !'##molecule_type DNA !'##residues 1-388 ##label ARI !'##note the source is designated as Streptomyces thermotolerans GENETICS !$#gene acyB1; carE FUNCTION !$#description involved in converting exogenously added tylosin to !14''-O-acyltylosins; catalyzes the reaction of two !1antibiotics, spiramycin and carbomycin into a hybrid !1antibiotic, isovaleryl-spiramycin CLASSIFICATION #superfamily 4''-O-acyltransferase KEYWORDS acyltransferase SUMMARY #length 388 #molecular-weight 43560 #checksum 7183 SEQUENCE /// ENTRY S56237 #type complete TITLE glucosamine-phosphate N-acetyltransferase (EC 2.3.1.4) [validated] - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES phosphoglucosamine acetylase; phosphoglucosamine transacetylase; protein R003; protein YFL017c ORGANISM #formal_name Saccharomyces cerevisiae DATE 18-Feb-2000 #sequence_revision 18-Feb-2000 #text_change 19-Apr-2002 ACCESSIONS S56237; S48321; S62296 REFERENCE S56186 !$#authors Murakami, Y.; Naitou, M.; Hagiwara, H.; Shibata, T.; Ozawa, !1M.; Sasanuma, S.I.; Sasanuma, M.; Tsuchiya, Y.; Soeda, E.; !1Yokoyama, K.; Yamazaki, M.; Tashiro, H.; Eki, T. !$#submission submitted to the EMBL Data Library, May 1995 !$#description Analysis of the nucleotide sequence of chromosome VI from !1Saccaromyces cerevisiae. !$#accession S56237 !'##molecule_type DNA !'##residues 1-159 ##label MUR !'##cross-references EMBL:D50617; NID:g836685; PIDN:BAA09221.1; !1PID:g836737; GSPDB:GN00006; MIPS:YFL017c REFERENCE S48310 !$#authors Churcher, C. !$#submission submitted to the EMBL Data Library, September 1994 !$#accession S48321 !'##molecule_type DNA !'##residues 1-111,'ASS' ##label CHU !'##cross-references EMBL:Z46255; NID:g559925; PIDN:CAA86352.1; !1PID:g559937; GSPDB:GN00006; MIPS:YFL017c REFERENCE S62230 !$#authors Murakami, Y. !$#submission submitted to the EMBL Data Library, December 1994 !$#accession S62296 !'##molecule_type DNA !'##residues 1-159 ##label MUW !'##cross-references EMBL:D44596; NID:g1100783; PIDN:BAA08000.1; !1PID:g1100787 GENETICS !$#gene SGD:GNA1; GNA1; MIPS:YFL017c !'##cross-references MIPS:YFL017c; SGD:S0001877 !$#map_position 6L FUNCTION !$#description EC 2.3.1.4 [validated, MUID:99085039]; glucosamine-phosphate !1N-acetyltransferase !$#note phosphoglucosamine acetyltransferase activity has been shown !1in vitro, by incubation with Agm1 !1(phospho-N-acetylglucosamine mutase) and Uap1 !1(UDP-N-acetylglucosamine pyrophosphorylase); !1UDP-N-acetylglucosamine is produced from glucosamine !16-phosphate, indicating that 142-Phe and 143-Tyr are !1essential for catalysis CLASSIFICATION #superfamily Saccharomyces glucosamine-phosphate !1N-acetyltransferase KEYWORDS acyltransferase; coenzyme A SUMMARY #length 159 #molecular-weight 18135 #checksum 9274 SEQUENCE /// ENTRY XYRBPR #type complete TITLE arylamine N-acetyltransferase (EC 2.3.1.5), polymorphic - rabbit ALTERNATE_NAMES arylamine acetylase ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 05-May-2000 ACCESSIONS A39870; B39870; S11559; S04138; A60882; A33181 REFERENCE A39870 !$#authors Sasaki, Y.; Ohsako, S.; Deguchi, T. !$#journal J. Biol. Chem. (1991) 266:13243-13250 !$#title Molecular and genetic analyses of arylamine !1N-acetyltransferase polymorphism of rabbit liver. !$#cross-references MUID:91302353; PMID:2071601 !$#accession A39870 !'##molecule_type DNA !'##residues 1-290 ##label SA1 !'##cross-references GB:M90378 !$#accession B39870 !'##molecule_type mRNA !'##residues 1-290 ##label SA2 !'##cross-references GB:M90380 REFERENCE S11559 !$#authors Blum, M.; Heim, M.; Meyer, U.A. !$#journal Nucleic Acids Res. (1990) 18:5295 !$#title Nucleotide sequence of rabbit NAT2 encoding polymorphic !1liver arylamine N-acetyltransferase (NAT). !$#cross-references MUID:90384846; PMID:2402461 !$#accession S11559 !'##molecule_type DNA !'##residues 1-290 ##label BL2 !'##cross-references EMBL:X53767; NID:g1647; PIDN:CAA37786.1; PID:g1648 REFERENCE S04138 !$#authors Blum, M.; Grant, D.M.; Demierre, A.; Meyer, U.A. !$#journal Nucleic Acids Res. (1989) 17:3589 !$#title Nucleotide sequence of a full-length cDNA for arylamine !1N-acetyltransferase from rabbit liver. !$#cross-references MUID:89263801; PMID:2726493 !$#accession S04138 !'##molecule_type mRNA !'##residues 1-290 ##label BLU !'##cross-references EMBL:X14673; NID:g1437; PIDN:CAA32803.1; PID:g1438 REFERENCE A60882 !$#authors Andres, H.H.; Vogel, R.S.; Tarr, G.E.; Johnson, L.; Weber, !1W.W. !$#journal Mol. Pharmacol. (1987) 31:446-456 !$#title Purification, physicochemical, and kinetic properties of !1liver acetyl-CoA:arylamine N-acetyltransferase from rapid !1acetylator rabbits. !$#cross-references MUID:87201456; PMID:3574290 !$#accession A60882 !'##molecule_type protein !'##residues 10-13;19-33;118-125,'K';128-151;154-158,'C',160-162,'D', !1164-165;167-178;189-213,'D',215;222,'K',224-232,'W', !1234-238;243-277;'VASISLPTSG';'LAIEAGFR' ##label AND !'##note the last two fragments attributed to this enzyme by the authors !1appear instead to be fragments of trypsin and of another !1enzyme COMMENT The polymorphic locus for this enzyme is deleted in slow !1acetylator rabbits but present in intermediate and rapid !1acetylator rabbits. A monomorphic locus for this enzyme is !1present in all rabbits. Polymorphism of the homologous !1enzyme in humans affects the rate of N-acetylation of amine- !1and hydrazine-containing drugs. COMMENT This protein contains no amino sugars and no cofactors. The !1amino end is blocked, even after treatment with !1pyroglutamate aminopeptidase. GENETICS !$#introns #status absent CLASSIFICATION #superfamily arylamine acetyltransferase KEYWORDS acyltransferase; blocked amino end; coenzyme A SUMMARY #length 290 #molecular-weight 33649 #checksum 7978 SEQUENCE /// ENTRY A28168 #type complete TITLE arylamine N-acetyltransferase (EC 2.3.1.5) - chicken ALTERNATE_NAMES arylamine acetylase ORGANISM #formal_name Gallus gallus #common_name chicken DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 05-May-2000 ACCESSIONS A28168; A28167 REFERENCE A28168 !$#authors Ohsako, S.; Ohtomi, M.; Sakamoto, Y.; Uyemura, K.; Deguchi, !1T. !$#journal J. Biol. Chem. (1988) 263:7534-7538 !$#title Arylamine N-acetyltransferase from chicken liver. II. !1Cloning of cDNA and expression in Chinese hamster ovary !1cells. !$#cross-references MUID:88227946; PMID:2897360 !$#accession A28168 !'##molecule_type mRNA !'##residues 1-287 ##label OHS !'##cross-references GB:J03737; NID:g211136; PIDN:AAA48590.1; !1PID:g211137 REFERENCE A28167 !$#authors Deguchi, T.; Sakamoto, Y.; Sasaki, Y.; Uyemura, K. !$#journal J. Biol. Chem. (1988) 263:7528-7533 !$#title Arylamine N-acetyltransferase from chicken liver. Monoclonal !1antibodies, immunoaffinity purification, and amino acid !1sequences. !$#cross-references MUID:88227945; PMID:2897359 !$#accession A28167 !'##molecule_type protein !'##residues 116-131;143-164;272-279 ##label DEG CLASSIFICATION #superfamily arylamine acetyltransferase KEYWORDS acyltransferase; coenzyme A SUMMARY #length 287 #molecular-weight 32915 #checksum 262 SEQUENCE /// ENTRY XYRBM #type complete TITLE arylamine N-acetyltransferase (EC 2.3.1.5), monomorphic - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 05-May-2000 ACCESSIONS C39870; S11220 REFERENCE A39870 !$#authors Sasaki, Y.; Ohsako, S.; Deguchi, T. !$#journal J. Biol. Chem. (1991) 266:13243-13250 !$#title Molecular and genetic analyses of arylamine !1N-acetyltransferase polymorphism of rabbit liver. !$#cross-references MUID:91302353; PMID:2071601 !$#accession C39870 !'##molecule_type DNA !'##residues 1-290 ##label SAS !'##cross-references GB:M90377 !'##note only a list of differences from sequence A39870 is shown REFERENCE S11220 !$#authors Blum, M.; Heim, M.; Meyer, U.A. !$#journal Nucleic Acids Res. (1990) 18:5287 !$#title Nucleotide sequence of rabbit NAT1 encoding monomorphic !1arylamine N-acetyltransferase. !$#cross-references MUID:90384838; PMID:2402454 !$#accession S11220 !'##molecule_type DNA !'##residues 1-284,'N',286-290 ##label BLU !'##cross-references EMBL:X53765; NID:g1644; PIDN:CAA37785.1; PID:g1645 GENETICS !$#introns #status absent CLASSIFICATION #superfamily arylamine acetyltransferase KEYWORDS acyltransferase; coenzyme A SUMMARY #length 290 #molecular-weight 33803 #checksum 6680 SEQUENCE /// ENTRY XYCHY3 #type complete TITLE arylamine N-acetyltransferase (EC 2.3.1.5) (clone p-NAT-3) - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 05-May-2000 ACCESSIONS S06652 REFERENCE S06652 !$#authors Ohtomi, M.; Sasaki, M.; Deguchi, T. !$#journal Eur. J. Biochem. (1989) 185:253-261 !$#title Two arylamine N-acetyltransferases from chicken pineal gland !1as identified by cDNA cloning. !$#cross-references MUID:90060108; PMID:2583181 !$#accession S06652 !'##molecule_type mRNA !'##residues 1-290 ##label OHT !'##cross-references GB:X17480; EMBL:X16020; NID:g62963; !1PIDN:CAA35515.1; PID:g62964 CLASSIFICATION #superfamily arylamine acetyltransferase KEYWORDS acyltransferase; coenzyme A SUMMARY #length 290 #molecular-weight 33663 #checksum 1592 SEQUENCE /// ENTRY XYCHY0 #type complete TITLE arylamine N-acetyltransferase (EC 2.3.1.5) (clone p-NAT-10) - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 05-May-2000 ACCESSIONS S06653 REFERENCE S06652 !$#authors Ohtomi, M.; Sasaki, M.; Deguchi, T. !$#journal Eur. J. Biochem. (1989) 185:253-261 !$#title Two arylamine N-acetyltransferases from chicken pineal gland !1as identified by cDNA cloning. !$#cross-references MUID:90060108; PMID:2583181 !$#accession S06653 !'##molecule_type mRNA !'##residues 1-290 ##label OHT !'##cross-references EMBL:X16021; NID:g62961; PIDN:CAA34153.1; !1PID:g62962 CLASSIFICATION #superfamily arylamine acetyltransferase KEYWORDS acyltransferase; coenzyme A SUMMARY #length 290 #molecular-weight 33925 #checksum 5679 SEQUENCE /// ENTRY C64897 #type complete TITLE probable phosphinothricin N-acetyltransferase (EC 2.3.1.-) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS C64897 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64897 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-172 ##label BLAT !'##cross-references GB:AE000241; GB:U00096; NID:g1787706; !1PIDN:AAC74530.1; PID:g1787719; UWGP:b1448 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily phosphinothricin N-acetyltransferase KEYWORDS acyltransferase SUMMARY #length 172 #molecular-weight 19248 #checksum 5615 SEQUENCE /// ENTRY S75140 #type complete TITLE probable phosphinothricin N-acetyltransferase (EC 2.3.1.-) sll1647 - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S75140 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75140 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-172 ##label KAN !'##cross-references EMBL:D90903; GB:AB001339; NID:g1652127; !1PIDN:BAA17054.1; PID:g1652130 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily phosphinothricin N-acetyltransferase KEYWORDS acyltransferase SUMMARY #length 172 #molecular-weight 19576 #checksum 8118 SEQUENCE /// ENTRY B70064 #type complete TITLE probable phosphinothricin N-acetyltransferase (EC 2.3.1.-) ywnH - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS B70064 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B70064 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-163 ##label KUN !'##cross-references GB:Z99122; GB:AL009126; NID:g2636029; !1PIDN:CAB15673.1; PID:g2636181 !'##experimental_source strain 168 GENETICS !$#gene ywnH CLASSIFICATION #superfamily phosphinothricin N-acetyltransferase KEYWORDS acyltransferase SUMMARY #length 163 #molecular-weight 18364 #checksum 3293 SEQUENCE /// ENTRY JH0246 #type complete TITLE phosphinothricin N-acetyltransferase (EC 2.3.1.-) - Streptomyces coelicolor ORGANISM #formal_name Streptomyces coelicolor DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Dec-1999 ACCESSIONS JH0246; T42030; A35404 REFERENCE JH0246 !$#authors Bedford, D.J.; Lewis, C.G.; Buttner, M.J. !$#journal Gene (1991) 104:39-45 !$#title Characterization of a gene conferring bialaphos resistance !1in Streptomyces coelicolor A3(2). !$#cross-references MUID:92009194; PMID:1916276 !$#accession JH0246 !'##molecule_type DNA !'##residues 1-171 ##label BED !'##cross-references GB:M62753; NID:g153178; PIDN:AAA26705.1; !1PID:g153179 !'##experimental_source strain A3[2] !$#accession T42030 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-171 ##label BE2 !'##cross-references EMBL:M62753; PIDN:AAA26705.1 REFERENCE A35404 !$#authors Buttner, M.J.; Chater, K.F.; Bibb, M.J. !$#journal J. Bacteriol. (1990) 172:3367-3378 !$#title Cloning, disruption, and transcriptional analysis of three !1RNA polymerase sigma factor genes of Streptomyces coelicolor !1A3(2). !$#cross-references MUID:90264336; PMID:2160942 !$#accession A35404 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-99 ##label BUT !'##cross-references GB:M37919; NID:g153312; PIDN:AAA26766.1; !1PID:g153313 COMMENT This enzyme inactivates phosphinothricin by transfer of !1acetyl groups from acetyl CoA. COMMENT The km for phosphinothricin of this enzyme is 1mM, a !1concentration nearly 20-fold higher than the km of the S. !1hygroscopicus. GENETICS !$#gene bar CLASSIFICATION #superfamily phosphinothricin N-acetyltransferase KEYWORDS acyltransferase SUMMARY #length 171 #molecular-weight 19205 #checksum 1624 SEQUENCE /// ENTRY S49184 #type complete TITLE phosphinothricin N-acetyltransferase (EC 2.3.1.-) - Streptomyces griseus ORGANISM #formal_name Streptomyces griseus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S49184 REFERENCE S49183 !$#authors Marcos, A.T.; Diez, B.; Gutierrez, S.; Fernandez, F.J.; !1Oguiza, J.A.; Martin, J.F. !$#submission submitted to the EMBL Data Library, June 1994 !$#description Three genes hrdB, hrdD and hrdT of Streptomyces griseus IMRU !13570, encoding sigma factor-like proteins, are !1differentially expressed under specific nutritional !1conditions. !$#accession S49184 !'##status preliminary !'##molecule_type DNA !'##residues 1-194 ##label MAR !'##cross-references EMBL:X79980; NID:g510451; PIDN:CAA56304.1; !1PID:g510453 CLASSIFICATION #superfamily phosphinothricin N-acetyltransferase KEYWORDS acyltransferase SUMMARY #length 194 #molecular-weight 21112 #checksum 2316 SEQUENCE /// ENTRY JT0409 #type complete TITLE phosphinothricin N-acetyltransferase (EC 2.3.1.-) - Streptomyces viridochromogenes ORGANISM #formal_name Streptomyces viridochromogenes DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JT0409; S20685 REFERENCE JT0409 !$#authors Wohlleben, W.; Arnold, W.; Broer, I.; Hillemann, D.; !1Strauch, E.; Puehler, A. !$#journal Gene (1988) 70:25-37 !$#title Nucleotide sequence of the phosphinothricin !1N-acetyltransferase gene from Streptomyces viridochromogenes !1Tue494 and its expression in Nicotiana tabacum. !$#cross-references MUID:89196914; PMID:3240868 !$#accession JT0409 !'##molecule_type DNA !'##residues 1-183 ##label WOH !'##cross-references GB:M22827; NID:g295177; PIDN:AAA72709.1; !1PID:g295179 !'##experimental_source strain Tue 494 !'##note it is uncertain whether Met-1 (GTG) or Met-18 is the initiator REFERENCE S20683 !$#authors Alijah, R.; Hillemann, D.; Nussbaumer, B.; Pelzer, S.; !1Wohlleben, W. !$#submission submitted to the EMBL Data Library, March 1992 !$#description Gene disruption and gene replacement analysis of a 4 kb !1BamHI fragment which caries PTT biosynthetic genes. !$#accession S20685 !'##status preliminary !'##molecule_type DNA !'##residues 1-183 ##label ALI !'##cross-references EMBL:X65195; NID:g47997; PIDN:CAA46314.1; !1PID:g581786 GENETICS !$#gene pat !$#start_codon GTG CLASSIFICATION #superfamily phosphinothricin N-acetyltransferase KEYWORDS acyltransferase SUMMARY #length 183 #molecular-weight 20618 #checksum 8644 SEQUENCE /// ENTRY S08615 #type complete TITLE phosphinothricin N-acetyltransferase (EC 2.3.1.-) - Streptomyces hygroscopicus ORGANISM #formal_name Streptomyces hygroscopicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S08615 REFERENCE S08615 !$#authors White, J.; Chang, S.Y.P.; Bibb, M.J.; Bibb, M.J. !$#journal Nucleic Acids Res. (1990) 18:1062 !$#title A cassette containing the bar gene of Streptomyces !1hygroscopicus: a selectable marker for plant transformation. !$#cross-references MUID:90192137; PMID:2315036 !$#accession S08615 !'##molecule_type DNA !'##residues 1-183 ##label WHI !'##cross-references EMBL:X17220; NID:g47128; PIDN:CAA35093.1; !1PID:g47129 GENETICS !$#gene bar CLASSIFICATION #superfamily phosphinothricin N-acetyltransferase KEYWORDS acyltransferase SUMMARY #length 183 #molecular-weight 20637 #checksum 9405 SEQUENCE /// ENTRY A69962 #type complete TITLE phosphate butyryltransferase (EC 2.3.1.19) yqiS - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A69962 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69962 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-299 ##label KUN !'##cross-references GB:Z99116; GB:AL009126; NID:g2634723; !1PIDN:CAB14340.1; PID:g2634843 !'##experimental_source strain 168 GENETICS !$#gene yqiS CLASSIFICATION #superfamily phosphate acetyltransferase KEYWORDS acyltransferase; coenzyme A SUMMARY #length 299 #molecular-weight 31772 #checksum 158 SEQUENCE /// ENTRY JN0794 #type complete TITLE phosphate butyryltransferase (EC 2.3.1.19) - Clostridium acetobutylicum (strain NCIMB 8052) ALTERNATE_NAMES phosphotransbutyrylase ORGANISM #formal_name Clostridium acetobutylicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-May-2000 ACCESSIONS JN0794 REFERENCE PN0619 !$#authors Oultram, J.D.; Burr, I.D.; Elmore, M.J.; Minton, N.P. !$#journal Gene (1993) 131:107-112 !$#title Cloning and sequence analysis of the genes encoding !1phosphotransbutyrylase and butyrate kinase from Clostridium !1acetobutylicum NCIMB 8052. !$#cross-references MUID:93380658; PMID:8396545 !$#accession JN0794 !'##molecule_type DNA !'##residues 1-302 ##label OUL !'##cross-references GB:L04468; NID:g144890; PIDN:AAA52080.1; !1PID:g144892 COMMENT This enzyme is involved in butyrate generation and catalyzes !1the conversion of butyryl-CoA through butyryl phosphate to !1butyrate. GENETICS !$#gene ptb CLASSIFICATION #superfamily phosphate acetyltransferase KEYWORDS acyltransferase; coenzyme A SUMMARY #length 302 #molecular-weight 32441 #checksum 2696 SEQUENCE /// ENTRY A49338 #type complete TITLE phosphate acetyltransferase (EC 2.3.1.8) - Methanosarcina thermophila ORGANISM #formal_name Methanosarcina thermophila DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-May-2000 ACCESSIONS A49338 REFERENCE A49338 !$#authors Latimer, M.T.; Ferry, J.G. !$#journal J. Bacteriol. (1993) 175:6822-6829 !$#title Cloning, sequence analysis, and hyperexpression of the genes !1encoding phosphotransacetylase and acetate kinase from !1Methanosarcina thermophila. !$#cross-references MUID:94042843; PMID:8226623 !$#accession A49338 !'##status preliminary !'##molecule_type DNA !'##residues 1-333 ##label LAT !'##cross-references GB:L23147; NID:g349832; PIDN:AAA72041.1; !1PID:g349833 GENETICS !$#start_codon TTG CLASSIFICATION #superfamily phosphate acetyltransferase KEYWORDS acyltransferase; coenzyme A SUMMARY #length 333 #molecular-weight 35219 #checksum 4541 SEQUENCE /// ENTRY A65021 #type complete TITLE ethanolamine utilization protein EutI - Escherichia coli (strain K-12) CONTAINS probable phosphate acyltransferase (EC 2.3.1.-) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS A65021 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65021 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-338 ##label BLAT !'##cross-references GB:AE000332; GB:U00096; NID:g1788789; !1PIDN:AAC75511.1; PID:g1788800; UWGP:b2458 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene eutI CLASSIFICATION #superfamily phosphate acetyltransferase KEYWORDS acyltransferase SUMMARY #length 338 #molecular-weight 36066 #checksum 3945 SEQUENCE /// ENTRY XXRTAC #type complete TITLE acetyl-CoA C-acetyltransferase (EC 2.3.1.9) precursor, mitochondrial - rat ALTERNATE_NAMES acetoacetyl-CoA thiolase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jun-2000 ACCESSIONS JU0072 REFERENCE JU0072 !$#authors Fukao, T.; Kamijo, K.; Osumi, T.; Fujiki, Y.; Yamaguchi, S.; !1Orii, T.; Hashimoto, T. !$#journal J. Biochem. (1989) 106:197-204 !$#title Molecular cloning and nucleotide sequence of cDNA encoding !1the entire precursor of rat mitochondrial acetoacetyl-CoA !1thiolase. !$#cross-references MUID:90036762; PMID:2478525 !$#accession JU0072 !'##molecule_type mRNA !'##residues 1-424 ##label FUK !'##cross-references GB:D13921; GB:D00511; NID:g220654; PIDN:BAA03016.1; !1PID:g220655 !'##note the amino-terminal 20 residues of the mature protein were !1sequenced COMMENT The enzyme plays a major role in ketone body metabolism and !1catalyzes the reversible reaction, acetoacetyl-CoA + CoA = 2 !1acetyl-CoA. COMMENT This enzyme is a tetramer of identical chains. CLASSIFICATION #superfamily acetyl-CoA acetyltransferase KEYWORDS acyltransferase; coenzyme A; homotetramer; ketone body !1metabolism; mitochondrion FEATURE !$1-30 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$31-424 #product acetoacetyl-CoA thiolase #status predicted !8#label ACO\ !$123 #active_site Cys #status predicted SUMMARY #length 424 #molecular-weight 44695 #checksum 2830 SEQUENCE /// ENTRY JH0255 #type complete TITLE acetyl-CoA C-acetyltransferase (EC 2.3.1.9) 1 precursor, mitochondrial - human ALTERNATE_NAMES acetoacetyl-coenzyme A thiolase ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS JH0255; A37233; I55572 REFERENCE JH0255 !$#authors Kano, M.; Fukao, T.; Yamaguchi, S.; Orii, T.; Osumi, T.; !1Hashimoto, T. !$#journal Gene (1991) 109:285-290 !$#title Structure and expression of the human mitochondrial !1acetoacetyl-CoA thiolase-encoding gene. !$#cross-references MUID:92112057; PMID:1684944 !$#accession JH0255 !'##molecule_type mRNA !'##residues 1-427 ##label KAN !'##cross-references DDBJ:D90476; DDBJ:D90477; DDBJ:D90478; DDBJ:D90479 !'##note the authors translated the codon GGT for residue 92 as Glu and !1ACT for residue 185 as Tyr REFERENCE A37233 !$#authors Fukao, T.; Yamaguchi, S.; Kano, M.; Orii, T.; Fujiki, Y.; !1Osumi, T.; Hashimoto, T. !$#journal J. Clin. Invest. (1990) 86:2086-2092 !$#title Molecular cloning and sequence of the complementary DNA !1encoding human mitochondrial acetoacetyl-coenzyme a thiolase !1and study of the variant enzymes in cultured fibroblasts !1from patients with 3-ketothiolase deficiency. !$#cross-references MUID:91072688; PMID:1979337 !$#accession A37233 !'##molecule_type mRNA !'##residues 1-339,'V',341-345,'D',347-411,'I',413-427 ##label FUK1 !'##cross-references GB:D90228; NID:g219917; PIDN:BAA14278.1; !1PID:g219918; GB:M61117 REFERENCE I55572 !$#authors Fukao, T.; Yamaguchi, S.; Orii, T.; Schutgens, R.B.; Osumi, !1T.; Hashimoto, T. !$#journal J. Clin. Invest. (1992) 89:474-479 !$#title Identification of three mutant alleles of the gene for !1mitochondrial acetoacetyl-coenzyme A thiolase. A complete !1analysis of two generations of a family with 3-ketothiolase !1deficiency. !$#cross-references MUID:92147861; PMID:1346617 !$#accession I55572 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 182,'R',184-185 ##label FUK2 !'##cross-references GB:S81263; NID:g245354; PIDN:AAB21419.1; !1PID:g245355 !'##note mutant sequence from a patient with acetoacetyl-CoA thiolase !1deficiency GENETICS !$#gene GDB:ACAT1; ACAT !'##cross-references GDB:126861; OMIM:203750 !$#map_position 11q22.3-11q23.1 !$#introns 24/3; 40/3; 80/1; 112/1; 145/3; 193/3; 244/1; 276/1; 314/1; !1335/3; 388/2 FUNCTION !$#description catalyzes the reversible cleavage of acetoacetyl-coenzyme A !1by coenzyme A to form two molecules of acetyl-coenzyme A !$#pathway fatty acid beta-oxidation CLASSIFICATION #superfamily acetyl-CoA acetyltransferase KEYWORDS acyltransferase; coenzyme A; fatty acid beta-oxidation; !1mitochondrion FEATURE !$1-33 #domain transit peptide (mitochondrion) #status !8predicted #label SIG\ !$34-421 #product acetyl-CoA acetyltransferase #status !8predicted #label ACE SUMMARY #length 427 #molecular-weight 45264 #checksum 3280 SEQUENCE /// ENTRY XXGZAC #type complete TITLE acetyl-CoA C-acetyltransferase (EC 2.3.1.9) - Zoogloea ramigera ALTERNATE_NAMES acetoacetyl-CoA thiolase; biosynthetic thiolase; thiolase II ORGANISM #formal_name Zoogloea ramigera DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 05-May-2000 ACCESSIONS A26121 REFERENCE A26121 !$#authors Peoples, O.P.; Masamune, S.; Walsh, C.T.; Sinskey, A.J. !$#journal J. Biol. Chem. (1987) 262:97-102 !$#title Biosynthetic thiolase from Zoogloea ramigera. III. Isolation !1and characterization of the structural gene. !$#cross-references MUID:87083504; PMID:2878929 !$#accession A26121 !'##molecule_type DNA !'##residues 1-391 ##label PEO !'##cross-references EMBL:J02631; NID:g155617; PIDN:AAA27706.1; !1PID:g155618 !'##experimental_source strain I-16-M, ATCC 19623 COMMENT The active enzyme, a tetramer of identical chains, catalyzes !1the reversible reaction: acetoacetyl-CoA + CoA = 2 !1acetyl-CoA; it plays a major role in ketone body metabolism, !1steroid biosynthesis, and poly-beta-hydroxybutyrate !1biosynthesis. GENETICS !$#gene phbA CLASSIFICATION #superfamily acetyl-CoA acetyltransferase KEYWORDS acyltransferase; coenzyme A; homotetramer; ketone body !1metabolism; poly-beta-hydroxybutyrate biosynthesis; steroid !1biosynthesis FEATURE !$2-391 #product acetyl-CoA acetyltransferase #status !8predicted #label MAT\ !$89 #active_site Cys #status predicted SUMMARY #length 391 #molecular-weight 40416 #checksum 4976 SEQUENCE /// ENTRY XXALAE #type complete TITLE acetyl-CoA C-acetyltransferase (EC 2.3.1.9) [validated] - Alcaligenes eutrophus ALTERNATE_NAMES acetoacetyl-CoA thiolase; beta-ketothiolase; biosynthetic thiolase; thiolase II ORGANISM #formal_name Alcaligenes eutrophus DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 18-Aug-2000 ACCESSIONS A34340 REFERENCE A34340 !$#authors Peoples, O.P.; Sinskey, A.J. !$#journal J. Biol. Chem. (1989) 264:15293-15297 !$#title Poly-beta-hydroxybutyrate biosynthesis in Alcaligenes !1eutrophus H16. Characterization of the genes encoding !1beta-ketothiolase and acetoacetyl-CoA reductase. !$#cross-references MUID:89359356; PMID:2670935 !$#accession A34340 !'##molecule_type DNA !'##residues 1-393 ##label PEO !'##cross-references GB:J04987; NID:g141953; PIDN:AAA21972.1; !1PID:g141954 !'##experimental_source strain H16 GENETICS !$#gene phbA COMPLEX homotetramer FUNCTION !$#description EC 2.3.1.16 [validated, MUID:89359356]; catalyzes the !1condensation of two acetyl-CoA molecules to form !1acetoacetyl-CoA !$#note it plays a major role in ketone body metabolism, steroid !1biosynthesis, and poly-beta-hydroxybutyrate biosynthesis CLASSIFICATION #superfamily acetyl-CoA acetyltransferase KEYWORDS acyltransferase; coenzyme A; ketone body metabolism; !1poly-beta-hydroxybutyrate biosynthesis; steroid biosynthesis FEATURE !$88 #active_site Cys #status predicted SUMMARY #length 393 #molecular-weight 40549 #checksum 4685 SEQUENCE /// ENTRY S75020 #type complete TITLE acetyl-CoA C-acetyltransferase (EC 2.3.1.9) slr1993 - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S75020 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75020 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-409 ##label KAN !'##cross-references EMBL:D90910; GB:AB001339; NID:g1652956; !1PIDN:BAA17882.1; PID:g1652965 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene thl CLASSIFICATION #superfamily acetyl-CoA acetyltransferase KEYWORDS acyltransferase; coenzyme A SUMMARY #length 409 #molecular-weight 43281 #checksum 3980 SEQUENCE /// ENTRY XXBYAC #type complete TITLE acetyl-CoA C-acetyltransferase (EC 2.3.1.9), cytosolic [similarity] - yeast (Saccharomyces cerevisiae) (strain uvarum 0230) ALTERNATE_NAMES acetoacetyl-CoA thiolase; biosynthetic thiolase; protein YPL028w; thiolase II ORGANISM #formal_name Saccharomyces cerevisiae #variety strain uvarum 0230 DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 19-Apr-2002 ACCESSIONS S01099 REFERENCE S01099 !$#authors Dequin, S.; Gloeckler, R.; Herbert, C.J.; Boutelet, F. !$#journal Curr. Genet. (1988) 13:471-478 !$#title Cloning, sequencing and analysis of the yeast S. uvarum !1ERG10 gene encoding acetoacetyl CoA thiolase. !$#cross-references MUID:88295227; PMID:2900076 !$#accession S01099 !'##molecule_type DNA !'##residues 1-398 ##label DEQ !'##cross-references EMBL:X07976; NID:g5156; PIDN:CAA30788.1; PID:g5157 !'##experimental_source strain uvarum 0230 !'##note the source is designated as Saccharomyces uvarum GENETICS !$#gene ERG10 !'##cross-references SGD:S0005949 !$#map_position 16L COMPLEX homotetramer FUNCTION !$#description catalyzes the reversible reaction of acetoacetyl-CoA and CoA !1to produce 2 molecules of acetyl-CoA !$#note plays a major role in ketone body metabolism, steroid !1biosynthesis, and poly-beta-hydroxybutyrate biosynthesis CLASSIFICATION #superfamily acetyl-CoA acetyltransferase KEYWORDS acyltransferase; coenzyme A; homotetramer; ketone body !1metabolism; poly-beta-hydroxybutyrate biosynthesis; steroid !1biosynthesis FEATURE !$91 #active_site Cys #status predicted SUMMARY #length 398 #molecular-weight 41658 #checksum 3785 SEQUENCE /// ENTRY XUHUAB #type complete TITLE acetyl-CoA C-acyltransferase (EC 2.3.1.16) precursor, peroxisomal - human ALTERNATE_NAMES 3-ketoacyl-CoA thiolase; beta-ketothiolase; thiolase I ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 05-May-2000 ACCESSIONS S17515; S04092; S01912 REFERENCE S17515 !$#authors Bout, A.; Franse, M.M.; Collins, J.; Blonden, L.; Tager, !1J.M.; Benne, R. !$#journal Biochim. Biophys. Acta (1991) 1090:43-51 !$#title Characterization of the gene encoding human peroxisomal !13-oxoacyl-CoA thiolase (ACAA). No large DNA rearrangement in !1a thiolase-deficient patient. !$#cross-references MUID:91355229; PMID:1679347 !$#accession S17515 !'##molecule_type DNA !'##residues 1-424 ##label BO1 !'##cross-references EMBL:X62041; EMBL:X65140; NID:g28253; !1PIDN:CAA46270.1; PID:g825617; EMBL:X65141; EMBL:X65142; !1EMBL:X65143; EMBL:X65144; EMBL:X65145; EMBL:X65146; !1EMBL:X65147; EMBL:X65148 REFERENCE S04092 !$#authors Fairbairn, L.J.; Tanner, M.J.A. !$#journal Nucleic Acids Res. (1989) 17:3588 !$#title Complete cDNA sequence of human foetal liver peroxisomal !13-oxoacyl-CoA thiolase. !$#cross-references MUID:89263800; PMID:2726492 !$#accession S04092 !'##molecule_type mRNA !'##residues 1-424 ##label FAI !'##cross-references EMBL:X14813; NID:g23875; PIDN:CAA32918.1; !1PID:g23876 REFERENCE S01912 !$#authors Bout, A.; Teunissen, Y.; Hashimoto, T.; Benne, R.; Tager, !1J.M. !$#journal Nucleic Acids Res. (1988) 16:10369 !$#title Nucleotide sequence of human peroxisomal 3-oxoacyl-CoA !1thiolase. !$#cross-references MUID:89057483; PMID:3194209 !$#accession S01912 !'##molecule_type mRNA !'##residues 1-284,'SPA',288-424 ##label BO2 !'##cross-references EMBL:X12966 !'##note this sequence has been corrected in reference S17515 COMMENT Two structurally distinct isozymes, A and B, have been found !1in rat liver, but evidence suggests there is only one human !1gene the sequence of which is closer to that of isozyme B. GENETICS !$#gene GDB:ACAA !'##cross-references GDB:119643; OMIM:261510 !$#map_position 3p23-3p22 !$#introns 57/3; 89/1; 108/3; 135/1; 149/2; 182/2; 209/2; 273/1; 333/1; !1351/3; 400/2 !$#note a defect in this gene may cause pseudo-Zellweger syndrome COMPLEX the functional peroxisomal enzyme is a homodimer FUNCTION !$#description catalyzes the transfer of the acyl group from acyl-CoA to !1acetyl-CoA to form 3-oxoacyl-CoA, the last step of fatty !1acid beta-oxidation !$#pathway fatty acid beta-oxidation !$#note has broad specificity for CoASH-initiated thiolysis of !1beta-ketoacyl-CoAs with chain lengths of 4 to 16 carbons CLASSIFICATION #superfamily acetyl-CoA acetyltransferase KEYWORDS acyltransferase; coenzyme A; fatty acid beta-oxidation; !1peroxisome FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-424 #product acetyl-CoA acyltransferase #status predicted !8#label MAT\ !$123 #active_site Cys #status predicted SUMMARY #length 424 #molecular-weight 44292 #checksum 8098 SEQUENCE /// ENTRY XURTAB #type complete TITLE acetyl-CoA C-acyltransferase (EC 2.3.1.16) precursor, peroxisomal - rat ALTERNATE_NAMES 3-ketoacyl-CoA thiolase; beta-ketothiolase; degradative thiolase; thiolase I ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 01-Dec-2000 ACCESSIONS B35725; A29327; B29452 REFERENCE A35725 !$#authors Hijikata, M.; Wen, J.K.; Osumi, T.; Hashimoto, T. !$#journal J. Biol. Chem. (1990) 265:4600-4606 !$#title Rat peroxisomal 3-ketoacyl-CoA thiolase gene. Occurrence of !1two closely related but differentially regulated genes. !$#cross-references MUID:90170971; PMID:2307679 !$#accession B35725 !'##molecule_type DNA !'##residues 1-424 ##label HIJ1 !'##cross-references GB:J05269 REFERENCE A29327 !$#authors Hijikata, M.; Ishii, N.; Kagamiyama, H.; Osumi, T.; !1Hashimoto, T. !$#journal J. Biol. Chem. (1987) 262:8151-8158 !$#title Structural analysis of cDNA for rat peroxisomal !13-ketoacyl-CoA thiolase. !$#cross-references MUID:87250407; PMID:3036803 !$#accession A29327 !'##molecule_type mRNA !'##residues 1-43,'Q',45-424 ##label HIJ2 !'##cross-references GB:J02749 REFERENCE A29452 !$#authors Arakawa, H.; Takiguchi, M.; Amaya, Y.; Nagata, S.; Hayashi, !1H.; Mori, M. !$#journal EMBO J. (1987) 6:1361-1366 !$#title cDNA-derived amino acid sequence of rat mitochondrial !13-oxoacyl-CoA thiolase with no transient presequence: !1structural relationship with peroxisomal isozyme. !$#cross-references MUID:87275831; PMID:3038520 !$#accession B29452 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-47,'NR',50-424 ##label ARA !'##note this sequence is reported in the paper as a personal !1communication from Osumi, Hashimoto, and others of Shinshu !1University COMMENT Acetyl-CoA acyltransferase catalyzes the transfer of the !1acyl group from acyl-CoA to acetyl-CoA to form !13-oxoacyl-CoA, the last step of fatty acid beta-oxidation. !1It has broad specificity for CoASH-initiated thiolysis of !1beta-ketoacyl-CoAs with chain lengths of 4 to 16 carbons. !1The functional peroxisomal enzyme is a dimer of identical !1chains. Two structurally distinct isozymes (A and B) have !1been found in rat liver. GENETICS !$#introns 57/3; 89/1; 108/2; 135/1; 149/2; 182/2; 209/2; 273/1; 333/1; !1351/3; 400/2 CLASSIFICATION #superfamily acetyl-CoA acetyltransferase KEYWORDS acyltransferase; coenzyme A; fatty acid beta-oxidation; !1peroxisome FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-424 #product acetyl-CoA acyltransferase #status predicted !8#label MAT\ !$123 #active_site Cys #status predicted SUMMARY #length 424 #molecular-weight 43820 #checksum 8812 SEQUENCE /// ENTRY XURTAA #type complete TITLE acetyl-CoA C-acyltransferase (EC 2.3.1.16) A precursor, peroxisomal - rat ALTERNATE_NAMES 3-ketoacyl-CoA thiolase; beta-ketothiolase; degradative thiolase; thiolase I ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 01-Dec-2000 ACCESSIONS A35725; JT0551; JS0399 REFERENCE A35725 !$#authors Hijikata, M.; Wen, J.K.; Osumi, T.; Hashimoto, T. !$#journal J. Biol. Chem. (1990) 265:4600-4606 !$#title Rat peroxisomal 3-ketoacyl-CoA thiolase gene. Occurrence of !1two closely related but differentially regulated genes. !$#cross-references MUID:90170971; PMID:2307679 !$#accession A35725 !'##molecule_type DNA !'##residues 1-434 ##label HIJ !'##cross-references GB:D90058; GB:J05269; NID:g220847; PIDN:BAA14106.1; !1PID:g220849 REFERENCE JT0551 !$#authors Bodnar, A.G.; Rachubinski, R.A. !$#journal Gene (1990) 91:193-199 !$#title Cloning and sequence determination of cDNA encoding a second !1rat liver peroxisomal 3-ketoacyl-CoA thiolase. !$#cross-references MUID:91007275; PMID:2210380 !$#accession JT0551 !'##molecule_type mRNA !'##residues 1-408,'T',410-434 ##label BOD !'##cross-references GB:M32801; NID:g205048; PIDN:AAA41471.1; !1PID:g205049 !'##experimental_source liver COMMENT Acetyl-CoA acyltransferase catalyzes the transfer of the !1acyl group from acyl-CoA to acetyl-CoA to form !13-oxoacyl-CoA, the last step of fatty acid beta-oxidation. !1It has broad specificity for CoASH-initiated thiolysis of !1beta-ketoacyl-CoAs with chain lengths of 4 to 16 carbons. !1The functional peroxisomal enzyme is a dimer of identical !1chains. Two structurally distinct isozymes (A and B) have !1been found in rat liver. GENETICS !$#gene THL2 !$#introns 67/3; 99/1; 118/2; 145/1; 159/2; 192/2; 219/2; 283/1; 343/1; !1361/3; 410/2 CLASSIFICATION #superfamily acetyl-CoA acetyltransferase KEYWORDS acyltransferase; coenzyme A; fatty acid beta-oxidation; !1peroxisome FEATURE !$1-36 #domain signal sequence #status predicted #label SIG\ !$37-434 #product acetyl-CoA acyltransferase #status predicted !8#label MAT\ !$130-138 #region substrate binding\ !$133 #active_site Cys #status predicted SUMMARY #length 434 #molecular-weight 44839 #checksum 1778 SEQUENCE /// ENTRY S22784 #type complete TITLE acetyl-CoA C-acyltransferase (EC 2.3.1.16), peroxisomal - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES 3-oxoacyl-CoA thiolase; protein YIL160c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-May-2000 ACCESSIONS S22784; S28652; S48374 REFERENCE S22784 !$#authors Einerhand, A.W.C.; Voorn-Brouwer, T.M.; Erdmann, R.; Kunau, !1W.H.; Tabak, H.F. !$#journal Eur. J. Biochem. (1991) 200:113-122 !$#title Regulation of transcription of the gene coding for !1peroxisomal 3-oxoacyl-CoA thiolase of Saccharomyces !1cerevisiae. !$#cross-references MUID:91348028; PMID:1715273 !$#accession S22784 !'##status translation not shown !'##molecule_type DNA !'##residues 1-417 ##label EIN !'##cross-references EMBL:X53946; NID:g3701; PIDN:CAA37893.1; PID:g3702 REFERENCE S28652 !$#authors Igual, J.C.; Matallana, E.; Gonzalez-Bosch, C.; Franco, L.; !1Perez-Ortin, J.E. !$#journal Yeast (1991) 7:379-389 !$#title A new glucose-repressible gene identified from the analysis !1of chromatin structure in deletion mutants of yeast SUC2 !1locus. !$#cross-references MUID:91335894; PMID:1872029 !$#accession S28652 !'##molecule_type DNA !'##residues 1-417 ##label IGU !'##cross-references EMBL:X53395; NID:g4196; PIDN:CAA37472.1; PID:g4197 REFERENCE S48373 !$#authors Churcher, C. !$#submission submitted to the EMBL Data Library, September 1994 !$#accession S48374 !'##molecule_type DNA !'##residues 1-417 ##label CHU !'##cross-references GB:Z47047; EMBL:Z38059; NID:g603997; PID:g763186; !1GSPDB:GN00009; MIPS:YIL160c GENETICS !$#gene SGD:POT1; FOX3; MIPS:YIL160c !'##cross-references SGD:S0001422; MIPS:YIL160c !$#map_position 9L CLASSIFICATION #superfamily acetyl-CoA acetyltransferase KEYWORDS acyltransferase; coenzyme A; peroxisome; transmembrane !1protein FEATURE !$399-415 #domain transmembrane #status predicted #label TMM SUMMARY #length 417 #molecular-weight 44730 #checksum 2323 SEQUENCE /// ENTRY JS0624 #type complete TITLE fatty-acid beta-oxidation multienzyme complex beta chain - Pseudomonas fragi ALTERNATE_NAMES acetyl-CoA C-acyltransferase homolog CONTAINS acetyl-CoA C-acyltransferase (EC 2.3.1.16) ORGANISM #formal_name Pseudomonas fragi DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS JS0624; PS0268 REFERENCE JX0199 !$#authors Sato, S.; Hayashi, M.; Imamura, S.; Ozeki, Y.; Kawaguchi, A. !$#journal J. Biochem. (1992) 111:8-15 !$#title Primary structures of the genes, faoA and faoB, from !1Pseudomonas fragi B-0771 which encode the two subunits of !1the HDT multienzyme complex involved in fatty acid !1beta-oxidation. !$#cross-references MUID:92299657; PMID:1607366 !$#accession JS0624 !'##molecule_type DNA !'##residues 1-391 ##label SAT !'##cross-references GB:D10390; GB:D90447; NID:g391838; PIDN:BAA01228.1; !1PID:g391840 !'##experimental_source strain B-0771 !$#accession PS0268 !'##molecule_type protein !'##residues 20-41;161-182;207-229;262-294;298-320;336-350,'X',352-353 !1##label SAT1 GENETICS !$#gene faoB COMPLEX heterotetramer of 2 alpha and 2 beta chains FUNCTION !$#description catalyzes the cleavage of a 3-ketoacyl-coenzyme A by !1coenzyme A to acetyl-coenzyme A and a 3-ketoacyl-coenzyme A !1that is 2 carbons shorter !$#pathway fatty acid beta-oxidation CLASSIFICATION #superfamily acetyl-CoA acetyltransferase KEYWORDS acyltransferase; coenzyme A; fatty acid beta-oxidation; !1heterotetramer FEATURE !$2-391 #product fatty-acid beta-oxidation multienzyme !8complex beta chain #status predicted #label MAT SUMMARY #length 391 #molecular-weight 41606 #checksum 8600 SEQUENCE /// ENTRY XURT #type complete TITLE acetyl-CoA C-acyltransferase (EC 2.3.1.16), mitochondrial - rat ALTERNATE_NAMES 3-ketoacyl-CoA thiolase; beta-ketothiolase; degradative thiolase; thiolase I ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 05-May-2000 ACCESSIONS A29452 REFERENCE A29452 !$#authors Arakawa, H.; Takiguchi, M.; Amaya, Y.; Nagata, S.; Hayashi, !1H.; Mori, M. !$#journal EMBO J. (1987) 6:1361-1366 !$#title cDNA-derived amino acid sequence of rat mitochondrial !13-oxoacyl-CoA thiolase with no transient presequence: !1structural relationship with peroxisomal isozyme. !$#cross-references MUID:87275831; PMID:3038520 !$#accession A29452 !'##molecule_type mRNA !'##residues 1-397 ##label ARA !'##cross-references EMBL:X05341; NID:g55543; PIDN:CAA28952.1; !1PID:g55544 COMMENT Acetyl-CoA acyltransferase catalyzes the transfer of the !1acyl group from acyl-CoA to acetyl-CoA to form !13-oxoacyl-CoA, the last step of fatty acid beta-oxidation. !1It has broad specificity for CoASH-initiated thiolysis of !1beta-ketoacyl-CoAs with chain lengths of 4 to 16 carbons. !1The functional mitochondrial enzyme is a tetramer of !1identical chains. CLASSIFICATION #superfamily acetyl-CoA acetyltransferase KEYWORDS acyltransferase; coenzyme A; fatty acid beta-oxidation; !1mitochondrion FEATURE !$92 #active_site Cys #status predicted SUMMARY #length 397 #molecular-weight 41871 #checksum 7137 SEQUENCE /// ENTRY XUEC #type complete TITLE acetyl-CoA C-acyltransferase (EC 2.3.1.16) - Escherichia coli (strain K-12) ALTERNATE_NAMES 3-ketoacyl-CoA thiolase; beta-ketothiolase; degradative thiolase; fatty acid beta oxidation multienzyme complex small (beta) chain; thiolase I ORGANISM #formal_name Escherichia coli DATE 30-Jun-1991 #sequence_revision 10-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS F65189; JV0109; JQ0655; A35436; S30736; A40816 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65189 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-387 ##label BLAT !'##cross-references GB:AE000460; GB:U00096; NID:g2367315; !1PIDN:AAC76848.1; PID:g2367316; UWGP:b3845 !'##experimental_source strain K-12, substrain MG1655 REFERENCE JV0108 !$#authors Dirusso, C.C. !$#journal J. Bacteriol. (1990) 172:6459-6468 !$#title Primary sequence of the Escherichia coli fadBA operon, !1encoding the fatty acid-oxidizing multienzyme complex, !1indicates a high degree of homology to eucaryotic enzymes. !$#cross-references MUID:91035260; PMID:1699931 !$#accession JV0109 !'##molecule_type DNA !'##residues 1-36,'S',38-387 ##label DIR !'##cross-references GB:M59368; GB:M36149; NID:g145899; PIDN:AAA23751.1; !1PID:g145901 REFERENCE JQ0654 !$#authors Nakahigashi, K.; Inokuchi, H. !$#journal Nucleic Acids Res. (1990) 18:4937 !$#title Nucleotide sequence of the fadA and fadB genes from !1Escherichia coli. !$#cross-references MUID:90370500; PMID:2204034 !$#accession JQ0655 !'##molecule_type DNA !'##residues 1-118,'G',120-387 ##label NAK !'##cross-references EMBL:X52837; NID:g41370; PIDN:CAB40810.1; !1PID:g4584723 REFERENCE A35436 !$#authors Yang, S.Y.; Yang, X.Y.H.; Healy-Louie, G.; Schulz, H.; !1Elzinga, M. !$#journal J. Biol. Chem. (1990) 265:10424-10429 !$#title Nucleotide sequence of the fadA gene. Primary structure of !13-ketoacyl-coenzyme A thiolase from Escherichia coli and the !1structural organization of the fadAB operon. !$#cross-references MUID:90285166; PMID:2191949 !$#accession A35436 !'##molecule_type DNA !'##residues 1-36,'S',38-370,'DG',373,'VS',375-387 ##label YAN !'##cross-references EMBL:J05498 REFERENCE S30660 !$#authors Daniels, D.L.; Plunkett III, G.; Burland, V.; Blattner, F.R. !$#journal Science (1992) 257:771-778 !$#title Analysis of the Escherichia coli genome: DNA sequence of the !1region from 84.5 to 86.5 minutes. !$#cross-references MUID:92358234; PMID:1379743 !$#accession S30736 !'##molecule_type DNA !'##residues 1-48,'X',50-81,'X',83-170,'XX',173-339,'X',341-387 ##label !1DAN !'##cross-references EMBL:M87049 REFERENCE A40816 !$#authors Yang, S.Y.; Yang, X.Y.H.; Healy-Louie, G.; Schulz, H.; !1Elzinga, M. !$#journal J. Biol. Chem. (1991) 266:16255 !$#cross-references MUID:91340783; PMID:1678742 !$#contents erratum !$#accession A40816 !'##status preliminary !'##molecule_type DNA !'##residues 368-377 ##label YA2 GENETICS !$#gene fadA !$#map_position 87 min FUNCTION !$#description catalyzes the transfer of the acyl group from acyl-CoA to !1acetyl-CoA to form 3-oxoacyl-CoA, the last step of fatty !1acid beta-oxidation !$#pathway fatty acid beta-oxidation !$#note the E. coli enzyme is the beta chain of the fatty acid !1complex CLASSIFICATION #superfamily acetyl-CoA acetyltransferase KEYWORDS acyltransferase; coenzyme A; fatty acid beta-oxidation FEATURE !$91 #active_site Cys #status predicted SUMMARY #length 387 #molecular-weight 40890 #checksum 7496 SEQUENCE /// ENTRY S52478 #type complete TITLE carnitine O-acetyltransferase (EC 2.3.1.7) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YM8054.01; protein YML042w ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-May-2000 ACCESSIONS S52478; A44423; B44423; S28519 REFERENCE S52478 !$#authors Connor, R.; Churcher, C. !$#submission submitted to the EMBL Data Library, February 1995 !$#accession S52478 !'##molecule_type DNA !'##residues 1-670 ##label CON !'##cross-references EMBL:Z48430; NID:g683664; PIDN:CAA88327.1; !1PID:g683665; GSPDB:GN00013; MIPS:YML042w REFERENCE A44423 !$#authors Kispal, G.; Sumegi, B.; Dietmeier, K.; Bock, I.; Gajdos, G.; !1Tomcsanyi, T.; Sandor, A. !$#journal J. Biol. Chem. (1993) 268:1824-1829 !$#title Cloning and sequencing of a cDNA encoding Saccharomyces !1cerevisiae carnitine acetyltransferase. Use of the cDNA in !1gene disruption studies. !$#cross-references MUID:93131929; PMID:8420957 !$#accession A44423 !'##molecule_type DNA !'##residues 1-262,'H',264-307,'M',309-670 ##label KIS1 !'##cross-references EMBL:Z14021; NID:g3461; PIDN:CAA78399.1; PID:g3462 !$#accession B44423 !'##molecule_type mRNA !'##residues 7-262,'H',264-307,'M',309-670 ##label KIS2 !'##note sequence extracted from NCBI backbone (NCBIP:122841) GENETICS !$#gene SGD:CAT2; YCAT; CAT; MIPS:YML042w !'##cross-references SGD:S0004506; MIPS:YML042w !$#map_position 13L CLASSIFICATION #superfamily carnitine O-acetyltransferase KEYWORDS acyltransferase; coenzyme A SUMMARY #length 670 #molecular-weight 77241 #checksum 8903 SEQUENCE /// ENTRY A39018 #type complete TITLE carnitine O-palmitoyltransferase (EC 2.3.1.21) II, precursor [validated] - human ALTERNATE_NAMES carnitine palmitoyltransferase II, liver; carnitine palmitoyltransferase II, mitochondrial ORGANISM #formal_name Homo sapiens #common_name man DATE 24-Nov-1999 #sequence_revision 24-Nov-1999 #text_change 08-Dec-2000 ACCESSIONS A39018; A41614; B41614; S12951; I37260 REFERENCE A39018 !$#authors Finocchiaro, G.; Taroni, F.; Rocchi, M.; Martin, A.L.; !1Colombo, I.; Tarelli, G.T.; DiDonato, S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:661-665 !$#title cDNA cloning, sequence analysis, and chromosomal !1localization of the gene for human carnitine !1palmitoyltransferase. !$#cross-references MUID:91110588; PMID:1988962 !$#accession A39018 !'##molecule_type mRNA !'##residues 1-282,'G',284-374,'E',376-658 ##label FIN1 !'##cross-references GB:M58581; NID:g180988 !'##note this sequence is revised in reference A41614 REFERENCE A41614 !$#authors Finocchiaro, G.; Taroni, F.; Rocchi, M.; Martin, A.L.; !1Colombo, I.; Tarelli, G.T.; DiDonato, S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:10981 !$#cross-references MUID:92073411; PMID:1961767 !$#contents erratum !$#accession A41614 !'##molecule_type mRNA !'##residues 282-316;352-386 ##label FIN2 !'##cross-references GB:M58581; NID:g180988 !$#accession B41614 !'##status nucleic acid sequence not shown; translation not shown; !1translated from GB/EMBL/DDBJ; not compared with conceptual !1translation !'##molecule_type mRNA !'##residues 1-658 ##label FIN3 !'##cross-references GB:M58581; NID:g180988; PIDN:AAB59462.1; !1PID:g180989 !'##experimental_source clone pL60; tissue fetal liver REFERENCE S12951 !$#authors Finocchiaro, G.; Colombo, I.; DiDonato, S. !$#journal FEBS Lett. (1990) 274:163-166 !$#title Purification, characterization and partial amino acid !1sequences of carnitine palmitoyl-transferase from human !1liver. !$#cross-references MUID:91071422; PMID:2174799 !$#accession S12951 !'##molecule_type protein !'##residues 26-34,'X',36,'X',38-41;108-137,'X', !1139;194-219;249-273;297-306;462-469,'X',471-473,'XX', !1476;567-610 ##label FIN4 REFERENCE I37260 !$#authors Montermini, L.; Wang, H.; Verderio, E.; Taroni, F.; !1DiDonato, S.; Finocchiaro, G. !$#journal Biochim. Biophys. Acta (1994) 1219:237-240 !$#title Identification of 5' regulatory regions of the human !1carnitine palmitoyltransferase II gene. !$#cross-references MUID:94368866; PMID:8086471 !$#accession I37260 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-6 ##label MON !'##cross-references EMBL:X78707; NID:g507073; PIDN:CAA55360.1; !1PID:g579811 !'##note in GenBank entry HSCPT1, release 112.0, this sequence is !1misidentified as carnitine palmitoyltransferase 1 COMMENT This enzyme works at the mitochondrial inner membrane with !1carnitine O-palmitoyltransferase I (see PIR:I59351) at the !1outer membrane and carnitine-acylcarnitine translocase to !1move fatty acids into the mitochondrion. GENETICS !$#gene GDB:CPT2; CPT1; CPTASE !'##cross-references GDB:127272; OMIM:255110; OMIM:600649; OMIM:600650 !$#map_position 1p32-1p32 FUNCTION !$#description catalyzes the reversible transfer of palmitoyl, and other !1long chain fatty acids, from carnitine to coenzyme A !$#pathway fatty acid beta-oxidation CLASSIFICATION #superfamily carnitine O-acetyltransferase KEYWORDS acyltransferase; coenzyme A; fatty acid beta-oxidation; !1mitochondrial inner membrane; mitochondrion FEATURE !$1-25 #domain transit peptide (mitochondrion) #status !8predicted #label TRP\ !$26-658 #product carnitine O-palmitoyltransferase II #status !8experimental #label MAT SUMMARY #length 658 #molecular-weight 73776 #checksum 5125 SEQUENCE /// ENTRY S31083 #type complete TITLE glycerol-3-phosphate O-acyltransferase (EC 2.3.1.15) precursor - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S31083; S31084 REFERENCE S31083 !$#authors Nishida, I.; Tasaka, Y.; Shiraishi, H.; Murata, N. !$#journal Plant Mol. Biol. (1993) 21:267-277 !$#title The gene and the RNA for the precursor to the !1plastid-located glycerol-3-phosphate acyltransferase of !1Arabidopsis thaliana. !$#cross-references MUID:93144702; PMID:7678766 !$#accession S31083 !'##molecule_type DNA !'##residues 1-459 ##label NIS !'##cross-references EMBL:D00672; NID:g217844; PIDN:BAA00575.1; !1PID:g217845 !$#accession S31084 !'##molecule_type mRNA !'##residues 1-459 ##label NI2 !'##cross-references EMBL:D00673; NID:g217846; PIDN:BAA00576.1; !1PID:g217847 GENETICS !$#gene ATS1 !$#introns 106/1; 138/3; 167/3; 200/2; 219/3; 253/3; 274/2; 311/2; 337/ !13; 377/3; 415/3 CLASSIFICATION #superfamily glycerol-3-phosphate O-acyltransferase KEYWORDS acyltransferase; chloroplast; coenzyme A FEATURE !$1-90 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$91-459 #product glycerol-3-phosphate O-acyltransferase !8#status predicted #label MAT SUMMARY #length 459 #molecular-weight 50432 #checksum 1756 SEQUENCE /// ENTRY XXHU #type fragment TITLE dihydrolipoamide S-acetyltransferase (EC 2.3.1.12) precursor, liver splice form [validated] - human (fragment) ALTERNATE_NAMES pyruvate dehydrogenase component E2 ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 01-Sep-2000 ACCESSIONS S01783; S25665; S38724 REFERENCE S01783 !$#authors Thekkumkara, T.J.; Ho, L.; Wexler, I.D.; Pons, G.; Liu, !1T.C.; Patel, M.S. !$#journal FEBS Lett. (1988) 240:45-48 !$#title Nucleotide sequence of a cDNA for the dihydrolipoamide !1acetyltransferase component of human pyruvate dehydrogenase !1complex. !$#cross-references MUID:89052894; PMID:3191998 !$#accession S01783 !'##molecule_type mRNA !'##residues 1-615 ##label THE !'##cross-references EMBL:Y00978; NID:g35359; PIDN:CAA68787.1; !1PID:g35360 !'##experimental_source liver REFERENCE S25665 !$#authors Moehario, L.H.; Smooker, P.M.; Devenish, R.J.; Mackay, I.R.; !1Gershwin, M.E.; Marzuki, S. !$#journal Biochem. Int. (1990) 20:417-422 !$#title Nucleotide sequence of a cDNA encoding the lipoate acetyl !1transferase (E2) of human heart pyruvate dehydrogenase !1complex differs from that of human placenta. !$#cross-references MUID:90197673; PMID:2317220 !$#accession S25665 !'##molecule_type mRNA !'##residues 'P',306-524 ##label MOE1 !'##cross-references EMBL:X13822; NID:g30523 !'##experimental_source heart REFERENCE S38724 !$#authors Moehario, L.H. !$#submission submitted to the EMBL Data Library, December 1988 !$#accession S38724 !'##molecule_type mRNA !'##residues 'P',306-450,'R',452-524 ##label MOE2 !'##cross-references EMBL:X13822; NID:g30523; PIDN:CAA32052.1; !1PID:g30524 !'##experimental_source heart COMMENT For alternative splice forms, see PIR:A40497 and PIR:S52490. GENETICS !$#gene GDB:DLAT; DLTA !'##cross-references GDB:118785 !$#map_position 11q23.1-11q23.1 !$#genome nuclear COMPLEX component E2 of pyruvate dehydrogenase complex FUNCTION !$#description catalyzes conversion of acetyl-CoA and dihydrolipoamide to !1S-acetyldihydrolipoamide and CoA !$#pathway pyruvate metabolism !$#note lipoyl cofactor; E2 component of multienzyme pyruvate !1dehydrogenase complex; major autoantigene of primary biliary !1cirrhosis CLASSIFICATION #superfamily dihydrolipoamide acetyltransferase; lipoyl/ !1biotin-binding homology KEYWORDS acetyl-CoA; acyltransferase; alternative splicing; cardiac !1muscle; coenzyme A; duplication; heart; lipoamide; !1mitochondrion FEATURE !$1-54 #domain transit peptide (mitochondrion) (fragment) !8#status predicted #label TNP\ !$55-615 #product dihydrolipoamide acetyltransferase #status !8predicted #label MAT\ !$61-135 #domain lipoyl/biotin-binding homology #label LPB1\ !$188-262 #domain lipoyl/biotin-binding homology #label LPB2\ !$309-366 #domain component E3 binding #status predicted #label !8E3B\ !$385-615 #domain catalytic #status predicted #label CAT\ !$100 #binding_site lipoamide (Lys) (covalent) #status !8predicted\ !$227 #binding_site lipoamide (Lys) (covalent) #status !8predicted\ !$588,592 #active_site His, Asp #status predicted SUMMARY #length 615 #checksum 3492 SEQUENCE /// ENTRY XUBOLA #type complete TITLE dihydrolipoamide S-(2-methylpropanoyl)transferase (EC 2.3.1.-) precursor - bovine ALTERNATE_NAMES branched-chain alpha-keto acid dehydrogenase complex, E2 component precursor; lipoamide acyltransferase ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Mar-1989 #sequence_revision 12-May-1995 #text_change 11-Jun-1999 ACCESSIONS A30801; B28707; B28655; A30784 REFERENCE A30784 !$#authors Griffin, T.A.; Lau, K.S.; Chuang, D.T. !$#journal J. Biol. Chem. (1988) 263:14008-14014 !$#title Characterization and conservation of the inner E-2 core !1domain structure of branched-chain alpha-keto acid !1dehydrogenase complex from bovine liver. Construction of a !1cDNA encoding the entire transacylase (E-2b) precursor. !$#cross-references MUID:89008232; PMID:3049570 !$#accession A30801 !'##molecule_type mRNA !'##residues 1-482 ##label GRI !'##cross-references GB:M21572; NID:g163242; PIDN:AAA30597.1; !1PID:g163243 !'##note the authors translated the codon TTC for residue 32 as Leu !'##note the sequence shown follows the authors translation at residue !132 REFERENCE A90529 !$#authors Lau, K.S.; Griffin, T.A.; Hu, C.W.C.; Chuang, D.T. !$#journal Biochemistry (1988) 27:1972-1981 !$#title Conservation of primary structure in the lipoyl-bearing and !1dihydrolipoyl dehydrogenase binding domains of mammalian !1branched-chain alpha-keto acid dehydrogenase complex: !1molecular cloning of human and bovine transacylase (E2) !1cDNAs. !$#cross-references MUID:88241022; PMID:2837277 !$#accession B28707 !'##molecule_type mRNA !'##residues 1-172,'G',174-227 ##label LAU !'##cross-references GB:M19475 REFERENCE A28655 !$#authors Hummel, K.B.; Litwer, S.; Bradford, A.P.; Aitken, A.; !1Danner, D.J.; Yeaman, S.J. !$#journal J. Biol. Chem. (1988) 263:6165-6168 !$#title Nucleotide sequence of a cDNA for branched chain !1acyltransferase with analysis of the deduced protein !1structure. !$#cross-references MUID:88198156; PMID:3245861 !$#accession B28655 !'##molecule_type protein !'##residues 100-109 ##label HUM COMMENT This enzyme is one of three components of the branched-chain !1alpha-keto dehydrogenase complex that catalyzes the !1oxidative decarboxylation of alpha-keto acids to acyl-CoA !1and carbon dioxide. The other two components are !1branched-chain alpha-keto acid decarboxylase (E1) and !1dihydrolipoyl dehydrogenase (E3). COMMENT The catalytic function of this enzyme is to accept, and to !1transfer to coenzyme A, acyl groups that are generated by !1the branched-chain alpha-keto acid decarboxylase component. !1It forms a 24-polypeptide structural core with octahedral !1symmetry. CLASSIFICATION #superfamily dihydrolipoamide acetyltransferase; lipoyl/ !1biotin-binding homology KEYWORDS acyltransferase; lipoamide; mitochondrion FEATURE !$1-61 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$62-482 #product lipoamide acyltransferase #status predicted !8#label MAT\ !$66-139 #domain lipoyl/biotin-binding homology #label LPB\ !$105 #binding_site lipoamide (Lys) (covalent) #status !8experimental\ !$452,456 #active_site His, Asp #status predicted SUMMARY #length 482 #molecular-weight 53409 #checksum 5387 SEQUENCE /// ENTRY XXPS2M #type complete TITLE dihydrolipoamide S-(2-methylpropanoyl)transferase (EC 2.3.1.-) - Pseudomonas putida ALTERNATE_NAMES 3-methyl-2-oxobutanoate dehydrogenase (lipoamide) complex chain E2; branched chain oxoacid dehydrogenase complex transacylase component ORGANISM #formal_name Pseudomonas putida DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 24-Sep-1999 ACCESSIONS S01322; S03010 REFERENCE S01322 !$#authors Burns, G.; Brown, T.; Hatter, K.; Sokatch, J.R. !$#journal Eur. J. Biochem. (1988) 176:165-169 !$#title Comparison of the amino acid sequences of the transacylase !1components of branched chain oxoacid dehydrogenase of !1Pseudomonas putida, and the pyruvate and 2-oxoglutarate !1dehydrogenases of Escherichia coli. !$#cross-references MUID:88329056; PMID:3046941 !$#accession S01322 !'##molecule_type DNA !'##residues 1-423 ##label BUR !'##cross-references GB:M57613; EMBL:X13004; NID:g790512; !1PIDN:AAA65617.1; PID:g790517 GENETICS !$#gene bkdB CLASSIFICATION #superfamily dihydrolipoamide acetyltransferase; lipoyl/ !1biotin-binding homology KEYWORDS acetyl-CoA; acyltransferase; lipoamide FEATURE !$2-423 #product 2-oxoisovalerate dehydrogenase (acylating) !8chain E2b #status predicted #label MAT\ !$5-78 #domain lipoyl/biotin-binding homology #label LPB\ !$112-165 #domain component E3 binding #status predicted #label !8E3B\ !$166-423 #domain catalytic #status predicted #label CAT\ !$44 #binding_site lipoamide (Lys) (covalent) #status !8predicted\ !$395,399 #active_site His, Asp #status predicted SUMMARY #length 423 #molecular-weight 45128 #checksum 2282 SEQUENCE /// ENTRY XUBYSD #type complete TITLE dihydrolipoamide S-succinyltransferase (EC 2.3.1.61) precursor - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES alpha-ketoglutarate dehydrogenase complex chain KE2; dihydrolipoyl transsuccinylase; protein YD8358.05c; protein YDR148c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1991 #sequence_revision 12-Apr-1996 #text_change 05-May-2000 ACCESSIONS S57975; A35654; S78755; S11195 REFERENCE S57971 !$#authors Murphy, L.; Richards, C.; Harris, D. !$#submission submitted to the EMBL Data Library, July 1995 !$#accession S57975 !'##molecule_type DNA !'##residues 1-463 ##label MUR !'##cross-references EMBL:Z50046; NID:g899393; PIDN:CAA90371.1; !1PID:g899398; GSPDB:GN00004; MIPS:YDR148c !'##experimental_source strain AB972 REFERENCE A35654 !$#authors Repetto, B.; Tzagoloff, A. !$#journal Mol. Cell. Biol. (1990) 10:4221-4232 !$#title Structure and regulation of KGD2, the structural gene for !1yeast dihydrolipoyl transsuccinylase. !$#cross-references MUID:90318388; PMID:2115121 !$#accession A35654 !'##molecule_type DNA !'##residues 1-169,'HRKVSPQGKTQVRKRLQR',188,'KLLQR',194,'KPLQR',200, !1'KLQNQ',206,'RT',209-440,'EKLLS',446-459,'CCYGDLKFAAHTNLIS' !1##label REP !'##cross-references EMBL:M34531; NID:g171782; PIDN:AAA34720.1; !1PID:g171783 REFERENCE S78754 !$#authors Ruecknagel, K.P.; Rospert, S. !$#submission submitted to the Protein Sequence Database, March 1999 !$#accession S78755 !'##molecule_type protein !'##residues 72-83 ##label RUE GENETICS !$#gene SGD:KGD2; MIPS:YDR148c !'##cross-references SGD:S0002555; MIPS:YDR148c !$#map_position 4R !$#genome nuclear CLASSIFICATION #superfamily dihydrolipoamide acetyltransferase; lipoyl/ !1biotin-binding homology KEYWORDS acetyl-CoA; acyltransferase; coenzyme A; lipoamide; !1mitochondrion; tricarboxylic acid cycle FEATURE !$1-71 #domain transit peptide (mitochondrion) #status !8experimental #label TNP\ !$72-463 #product dihydrolipoamide S-succinyltransferase !8#status experimental #label MAT\ !$75-148 #domain lipoyl/biotin-binding homology #label LPB\ !$114 #binding_site lipoamide (Lys) (covalent) #status !8predicted\ !$435,439 #active_site His, Asp #status predicted SUMMARY #length 463 #molecular-weight 50430 #checksum 8721 SEQUENCE /// ENTRY XUECSD #type complete TITLE dihydrolipoamide S-succinyltransferase (EC 2.3.1.61) [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES 2-oxoglutarate dehydrogenase complex E2 component ORGANISM #formal_name Escherichia coli DATE 31-Mar-1989 #sequence_revision 24-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS F64808; A30259 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64808 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-405 ##label BLAT !'##cross-references GB:AE000175; GB:U00096; NID:g1786934; !1PIDN:AAC73821.1; PID:g1786946; UWGP:b0727 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A30259 !$#authors Spencer, M.E.; Darlison, M.G.; Stephens, P.E.; Duckenfield, !1I.K.; Guest, J.R. !$#journal Eur. J. Biochem. (1984) 141:361-374 !$#title Nucleotide sequence of the sucB gene encoding the !1dihydrolipoamide succinyltransferase of Escherichia coli K12 !1and homology with the corresponding acetyltransferase. !$#cross-references MUID:84236169; PMID:6376124 !$#accession A30259 !'##molecule_type DNA !'##residues 1-100,'AA',104-405 ##label SPE !'##cross-references GB:X00664; NID:g43021; PIDN:CAA25284.1; PID:g43022 REFERENCE A51636 !$#authors Clore, G.M.; Robien, M.A.; Gronenborn, A.M. !$#submission submitted to the Brookhaven Protein Data Bank, February 1992 !$#cross-references PDB:1BBL !$#contents annotation; conformation by (1)H-NMR, residues 114-150 REFERENCE A58629 !$#authors Robien, M.A.; Clore, G.M.; Omichinski, J.G.; Perham, R.N.; !1Appella, E.; Sakaguchi, K.; Gronenborn, A.M. !$#journal Biochemistry (1992) 31:3463-3471 !$#title Three-dimensional solution structure of the E3-binding !1domain of the dihydrolipoamide succinyltransferase core from !1the 2-oxoglutarate dehydrogenase multienzyme complex of !1Escherichia coli. !$#cross-references MUID:92207970; PMID:1554728 !$#contents annotation; conformation by (1)H-NMR GENETICS !$#gene sucB !$#map_position 17 min COMPLEX octamer of homotrimers; the central core may associate !1randomly with approximately 12 E1 and 12 E3 component chains FUNCTION !$#description accepts transfer of 2-oxoglutarate to its covalently bound !1lipoamide forming S-succinyl-dihydrolipoamide, then !1catalyzes the reaction of S-succinyl-dihydrolipoamide and !1coenzyme A to form succinyl-CoA and dihydrolipoamide !$#note the 2-oxoglutarate dehydrogenase complex, including !12-oxoglutarate dehydrogenase (E1), dihydrolipoamide !1succinyltransferase (E2) and lipoamide dehydrogenase (E3), !1catalyzes the oxidative decarboxylation of 2-oxoglutarate to !1succinyl-CoA and carbon dioxide CLASSIFICATION #superfamily dihydrolipoamide acetyltransferase; lipoyl/ !1biotin-binding homology KEYWORDS acyltransferase; coenzyme A; homotrimer; lipoamide; !1tricarboxylic acid cycle FEATURE !$5-78 #domain lipoyl/biotin-binding homology #label LPB\ !$44 #binding_site lipoamide (Lys) (covalent) #status !8predicted\ !$376,380 #active_site His, Asp #status predicted SUMMARY #length 405 #molecular-weight 44011 #checksum 9315 SEQUENCE /// ENTRY XXECDP #type complete TITLE dihydrolipoamide S-acetyltransferase (EC 2.3.1.12) aceF [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES dihydrolipoyl transacetylase component; lipoate acetyltransferase CONTAINS pyruvate dehydrogenase (lipoamide) (EC 1.2.4.1) chain E2 ORGANISM #formal_name Escherichia coli DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 03-Jun-2002 ACCESSIONS A30278; S45194; S13174; A16026; C64734; S17951 REFERENCE A30278 !$#authors Stephens, P.E.; Darlison, M.G.; Lewis, H.M.; Guest, J.R. !$#journal Eur. J. Biochem. (1983) 133:481-489 !$#title The pyruvate dehydrogenase complex of Escherichia coli K12. !1Nucleotide sequence encoding the dihydrolipoamide !1acetyltransferase component. !$#cross-references MUID:83234434; PMID:6345153 !$#accession A30278 !'##molecule_type DNA !'##residues 1-630 ##label STE !'##cross-references EMBL:V01498; NID:g431915; PIDN:CAA24741.1; !1PID:g434011 REFERENCE S45181 !$#authors Fujita, N. !$#submission submitted to the EMBL Data Library, January 1994 !$#accession S45194 !'##molecule_type DNA !'##residues 1-630 ##label FUJ !'##cross-references EMBL:D26562; NID:g473770; PIDN:BAA05573.1; !1PID:g473784 !'##experimental_source strain K-12 substrain W3110 REFERENCE S13174 !$#authors Ali, S.T.; Guest, J.R. !$#journal Biochem. J. (1990) 271:139-145 !$#title Isolation and characterization of lipoylated and !1unlipoylated domains of the E2p subunit of the pyruvate !1dehydrogenase complex of Escherichia coli. !$#cross-references MUID:91024917; PMID:2121129 !$#accession S13174 !'##molecule_type protein !'##residues 2-47;252-290 ##label ALI !'##experimental_source strain K-12 REFERENCE A16026 !$#authors Hale, G.; Perham, R.N. !$#journal Biochem. J. (1980) 187:905-908 !$#title Amino acid sequence around lipoic acid residues in the !1pyruvate dehydrogenase multienzyme complex of Escherichia !1coli. !$#cross-references MUID:84256520; PMID:6821375 !$#accession A16026 !'##molecule_type protein !'##residues 35-47 ##label HAL REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64734 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-630 ##label BLAT !'##cross-references GB:AE000120; GB:U00096; NID:g1786298; !1PIDN:AAC73226.1; PID:g1786305; UWGP:b0115 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S17857 !$#authors Schulze, E.; Westphal, A.H.; Obmolova, G.; Mattevi, A.; Hol, !1W.G.J.; de Kok, A. !$#journal Eur. J. Biochem. (1991) 201:561-568 !$#title The catalytic domain of the dihydrolipoyl transacetylase !1component of the pyruvate dehydrogenase complex from !1Azotobacter vinelandii and Escherichia coli. Expression, !1purification, properties and preliminary X-ray analysis. !$#cross-references MUID:92037610; PMID:1935951 !$#accession S17951 !'##molecule_type protein !'##residues 372-381 ##label SCH GENETICS !$#gene aceF !$#map_position 3 min COMPLEX this is the E2 component of the pyruvate dehydrogenase !1complex in E. coli; it contains covalently bound lipoyl !1cofactors; in E. coli, this protein contains 24 identical !1polypeptide chains forming the structural core of the !1complex to which the pyruvate dehydrogenase (E1 component) !1and lipoamide dehydrogenase (E3 component) are independently !1bound FUNCTION !$#description participates in the generation of acetyl groups from !1hydroxyethyl-thiamine pyrophosphate-E1 and their transfer to !1coenzyme A CLASSIFICATION #superfamily Escherichia coli dihydrolipoamide !1S-acetyltransferase; lipoyl/biotin-binding homology KEYWORDS acyltransferase; coenzyme A; duplication; lipoamide; !1oxidoreductase FEATURE !$2-630 #product dihydrolipoamide S-acetyltransferase #status !8experimental #label MAT\ !$4-75 #domain lipoyl/biotin-binding homology #label LPB1\ !$107-178 #domain lipoyl/biotin-binding homology #label LPB2\ !$208-279 #domain lipoyl/biotin-binding homology #label LPB3\ !$41,144,245 #binding_site lipoamide (Lys) (covalent) #status !8experimental\ !$603,607 #active_site His, Asp #status predicted SUMMARY #length 630 #molecular-weight 66095 #checksum 3567 SEQUENCE /// ENTRY XXAV #type complete TITLE dihydrolipoamide S-acetyltransferase (EC 2.3.1.12) [validated] - Azotobacter vinelandii ALTERNATE_NAMES dihydrolipoyltransacetylase; lipoate acetyltransferase; thioltransacetylase A CONTAINS pyruvate dehydrogenase (lipoamide) (EC 1.2.4.1) chain E2 ORGANISM #formal_name Azotobacter vinelandii DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 03-Jun-2002 ACCESSIONS S01017; S02291; S17857 REFERENCE S01017 !$#authors Hanemaaijer, R.; Janssen, A.; de Kok, A.; Veeger, C. !$#journal Eur. J. Biochem. (1988) 174:593-599 !$#title The dihydrolipoyltransacetylase component of the pyruvate !1dehydrogenase complex from Azotobacter vinelandii. Molecular !1cloning and sequence analysis. !$#cross-references MUID:88271330; PMID:3292237 !$#accession S01017 !'##molecule_type DNA !'##residues 1-638 ##label HAN1 !'##cross-references EMBL:X12455 REFERENCE S02291 !$#authors Hanemaaijer, R.; de Kok, A.; Jolles, J.; Veeger, C. !$#journal Eur. J. Biochem. (1987) 169:245-252 !$#title The domain structure of the dihydrolipoyl transacetylase !1component of the pyruvate dehydrogenase complex from !1Azotobacter vinelandii. !$#cross-references MUID:88082750; PMID:3691494 !$#accession S02291 !'##molecule_type protein !'##residues 2-13,'D',15-16;381-416,'M' ##label HAN2 !'##note 381-Arg was also found REFERENCE S17857 !$#authors Schulze, E.; Westphal, A.H.; Obmolova, G.; Mattevi, A.; Hol, !1W.G.J.; de Kok, A. !$#journal Eur. J. Biochem. (1991) 201:561-568 !$#title The catalytic domain of the dihydrolipoyl transacetylase !1component of the pyruvate dehydrogenase complex from !1Azotobacter vinelandii and Escherichia coli. Expression, !1purification, properties and preliminary X-ray analysis. !$#cross-references MUID:92037610; PMID:1935951 !$#accession S17857 !'##molecule_type protein !'##residues 384-394 ##label SCH REFERENCE A65901 !$#authors Berg, A.; Vervoort, J.; De Kok, A. !$#submission submitted to the Brookhaven Protein Data Bank, September !11996 !$#cross-references PDB:1IYU !$#contents annotation; conformation by (1)H-, and (15)N-NMR, residues !12-79,'R' REFERENCE A65902 !$#authors Berg, A.; Vervoort, J.; De Kok, A. !$#submission submitted to the Brookhaven Protein Data Bank, September !11996 !$#cross-references PDB:1IYV !$#contents annotation; conformation by (1)H-, and (15)N-NMR, residues !12-79,'R' REFERENCE S63511 !$#authors Berg, A.; Smits, O.; de Kok, A.; Vervoort, J. !$#journal Eur. J. Biochem. (1995) 234:148-159 !$#title Sequential (1)H and (15)N nuclear magnetic resonance !1assignments and secondary structure of the lipoyl domain of !1the 2-oxoglutarate dehydrogenase complex from Azotobacter !1vinelandii. Evidence for high structural similarity with the !1lipoyl domain of the pyruvate dehydrogenase complex. !$#cross-references MUID:96096733; PMID:8529634 !$#contents annotation; conformation by (1)H-, and (15)N-NMR REFERENCE S43251 !$#authors Berg, A.; de Kok, A.; Vervoort, J. !$#journal Eur. J. Biochem. (1994) 221:87-100 !$#title Sequential (1)H and (15)N nuclear magnetic resonance !1assignments and secondary structure of the N-terminal lipoyl !1domain of the dihydrolipoyl transacetylase component of the !1pyruvate dehydrogenase complex from Azotobacter vinelandii. !$#cross-references MUID:94222112; PMID:8068086 !$#contents annotation; conformation by (1)H-, and (15)N-NMR GENETICS !$#start_codon GTG CLASSIFICATION #superfamily Escherichia coli dihydrolipoamide !1S-acetyltransferase; lipoyl/biotin-binding homology KEYWORDS acetyl-CoA; acyltransferase; coenzyme A; duplication; !1lipoamide; oxidoreductase FEATURE !$2-638 #product dihydrolipoamide acetyltransferase #status !8experimental #label MAT\ !$4-74 #domain lipoyl/biotin-binding homology #label LPB1\ !$119-191 #domain lipoyl/biotin-binding homology #label LPB2\ !$224-296 #domain lipoyl/biotin-binding homology #label LPB3\ !$333-376 #domain component E3 binding #status predicted #label !8E3B\ !$382-638 #domain catalytic #status predicted #label CAT\ !$40 #binding_site lipoamide (Lys) (covalent) #status !8experimental\ !$157,262 #binding_site lipoamide (Lys) (covalent) #status !8predicted SUMMARY #length 638 #molecular-weight 65044 #checksum 6377 SEQUENCE /// ENTRY T44892 #type complete TITLE probable dihydrolipoamide S-succinyltransferase (EC 2.3.1.61) sucB [similarity] - Mycobacterium leprae ORGANISM #formal_name Mycobacterium leprae DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 08-Sep-2000 ACCESSIONS T44892 REFERENCE Z22864 !$#authors Parkhill, J.; Barrell, B.G.; Rajandream, M.A. !$#submission submitted to the EMBL Data Library, August 1997 !$#accession T44892 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-530 ##label PAR !'##cross-references EMBL:Z98741; PIDN:CAB11382.1 !'##experimental_source cosmid B22 GENETICS !$#gene sucB CLASSIFICATION #superfamily Mycobacterium probable dihydrolipoamide !1succinyltransferase; lipoyl/biotin-binding homology KEYWORDS acyltransferase; coenzyme A FEATURE !$4-77 #domain lipoyl/biotin-binding homology #label LPB1\ !$120-193 #domain lipoyl/biotin-binding homology #label LPB2\ !$43,159 #binding_site lipoamide (Lys) (covalent) #status !8predicted\ !$43 #binding_site lipoamide (Lys) (covalent) #status !8predicted\ !$159 #binding_site lipoamide (Lys) (covalent) #status !8predicted SUMMARY #length 530 #molecular-weight 55472 #checksum 4882 SEQUENCE /// ENTRY A75570 #type complete TITLE 2-oxo acid dehydrogenase, E2 component - Deinococcus radiodurans (strain R1) ORGANISM #formal_name Deinococcus radiodurans DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 01-Sep-2000 ACCESSIONS A75570 REFERENCE A75250 !$#authors White, O.; Eisen, J.A.; Heidelberg, J.F.; Hickey, E.K.; !1Peterson, J.D.; Dodson, R.J.; Haft, D.H.; Gwinn, M.L.; !1Nelson, W.C.; Richardson, D.L.; Moffat, K.S.; Qin, H.; !1Jiang, L.; Pamphile, W.; Crosby, M.; Shen, M.; Vamathevan, !1J.J.; Lam, P.; McDonald, L.; Utterback, T.; Zalewski, C.; !1Makarova, K.S.; Aravind, L.; Daly, M.J.; Minton, K.W.; !1Fleischmann, R.D.; Ketchum, K.A.; Nelson, K.E.; Salzberg, !1S.; Smith, H.O.; Venter, J.C.; Fraser, C.M. !$#journal Science (1999) 286:1571-1577 !$#title Genome sequence of the radioresistant bacterium Deinococcus !1radiodurans R1. !$#cross-references MUID:20036896; PMID:10567266 !$#accession A75570 !'##molecule_type DNA !'##residues 1-525 ##label WHI !'##cross-references GB:AE001866; GB:AE000513; NID:g6457680; !1PIDN:AAF09623.1; PID:g6457690; TIGR:DR0032; GSPDB:GN00077 !'##experimental_source strain R1 GENETICS !$#gene DR0032 !$#map_position 1 CLASSIFICATION #superfamily Mycobacterium probable dihydrolipoamide !1succinyltransferase; lipoyl/biotin-binding homology FEATURE !$42 #binding_site lipoamide (Lys) (covalent) #status !8predicted SUMMARY #length 525 #molecular-weight 55589 #checksum 9763 SEQUENCE /// ENTRY H70786 #type complete TITLE probable dihydrolipoamide acetyltransferase component [similarity] - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 01-Sep-2000 ACCESSIONS H70786 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession H70786 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-553 ##label COL !'##cross-references GB:Z70283; GB:AL123456; NID:g3261561; !1PIDN:CAA94256.1; PID:g1237068 !'##experimental_source strain H37Rv GENETICS !$#gene sucB CLASSIFICATION #superfamily Mycobacterium probable dihydrolipoamide !1succinyltransferase; lipoyl/biotin-binding homology FEATURE !$4-77 #domain lipoyl/biotin-binding homology #label LPB1\ !$43 #binding_site lipoamide (Lys) (covalent) #status !8predicted\ !$162 #binding_site lipoamide (Lys) (covalent) #status !8predicted SUMMARY #length 553 #molecular-weight 57087 #checksum 4512 SEQUENCE /// ENTRY T35297 #type complete TITLE probable dihydrolipoamide S-succinyltransferase (EC 2.3.1.61) SC5F7.20 [similarity] - Streptomyces coelicolor ORGANISM #formal_name Streptomyces coelicolor DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 08-Sep-2000 ACCESSIONS T35297 REFERENCE Z21574 !$#authors Seeger, K.; Harris, D.; Bentley, S.D.; Parkhill, J.; !1Barrell, B.G.; Rajandream, M.A. !$#submission submitted to the EMBL Data Library, July 1999 !$#accession T35297 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-590 ##label SEE !'##cross-references EMBL:AL096872; PIDN:CAB51265.1; GSPDB:GN00070; !1SCOEDB:SC5F7.20 !'##experimental_source strain A3(2) GENETICS !$#gene sucB; SCOEDB:SC5F7.20 CLASSIFICATION #superfamily Mycobacterium probable dihydrolipoamide !1succinyltransferase; lipoyl/biotin-binding homology KEYWORDS acyltransferase; coenzyme A FEATURE !$4-77 #domain lipoyl/biotin-binding homology #label LPB1\ !$131-204 #domain lipoyl/biotin-binding homology #label LPB2\ !$43,170 #binding_site lipoamide (Lys) (covalent) #status !8predicted\ !$43 #binding_site lipoamide (Lys) (covalent) #status !8predicted\ !$170 #binding_site lipoamide (Lys) (covalent) #status !8predicted SUMMARY #length 590 #molecular-weight 59035 #checksum 3909 SEQUENCE /// ENTRY D42462 #type complete TITLE dihydrolipoamide S-acetyltransferase (EC 2.3.1.12) - Alcaligenes eutrophus (strain H16) ORGANISM #formal_name Alcaligenes eutrophus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Sep-2000 ACCESSIONS D42462 REFERENCE A42462 !$#authors Priefert, H.; Hein, S.; Krueger, N.; Zeh, K.; Schmidt, B.; !1Steinbuechel, A. !$#journal J. Bacteriol. (1991) 173:4056-4071 !$#title Identification and molecular characterization of the !1Alcaligenes eutrophus H16 aco operon genes involved in !1acetoin catabolism. !$#cross-references MUID:91286190; PMID:2061286 !$#accession D42462 !'##status preliminary !'##molecule_type DNA !'##residues 1-374 ##label PRI !'##cross-references GB:M66060 CLASSIFICATION #superfamily dihydrolipoamide S-acetyltransferase; lipoyl/ !1biotin-binding homology KEYWORDS acyltransferase; coenzyme A FEATURE !$11-84 #domain lipoyl/biotin-binding homology #label LPB\ !$50 #binding_site lipoamide (Lys) (covalent) #status !8predicted SUMMARY #length 374 #molecular-weight 39135 #checksum 2067 SEQUENCE /// ENTRY H69004 #type complete TITLE 2-oxoglutarate-ferredoxin oxidoreductase (EC 1.2.7.-) alpha chain - Methanobacterium thermoautotrophicum (strain Delta H) ALTERNATE_NAMES 2-oxoacid:ferredoxin oxidoreductase (CoA-acetylating) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS H69004 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession H69004 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-378 ##label MTH !'##cross-references GB:AE000875; GB:AE000666; NID:g2622123; !1PIDN:AAB85529.1; PID:g2622136 !'##experimental_source strain Delta H GENETICS !$#gene MTH1033 CLASSIFICATION #superfamily Helicobacter pylori 2-oxoacid ferredoxin !1oxidoreductase; 2-oxoacid ferredoxin oxidoreductase homology KEYWORDS oxidoreductase FEATURE !$8-189 #domain 2-oxoacid ferredoxin oxidoreductase homology !8#label FEO SUMMARY #length 378 #molecular-weight 41636 #checksum 7939 SEQUENCE /// ENTRY E64593 #type complete TITLE 2-oxoacid-ferredoxin oxidoreductase (EC 1.2.7.-) alpha chain - Helicobacter pylori (strain 26695) ALTERNATE_NAMES 2-oxoacid:ferredoxin oxidoreductase (CoA-acetylating) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS E64593 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession E64593 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-375 ##label TOM !'##cross-references GB:AE000572; GB:AE000511; NID:g2313703; !1PIDN:AAD07654.1; PID:g2313707; TIGR:HP0589 CLASSIFICATION #superfamily Helicobacter pylori 2-oxoacid ferredoxin !1oxidoreductase; 2-oxoacid ferredoxin oxidoreductase homology KEYWORDS oxidoreductase FEATURE !$5-186 #domain 2-oxoacid ferredoxin oxidoreductase homology !8#label FEO SUMMARY #length 375 #molecular-weight 41509 #checksum 2325 SEQUENCE /// ENTRY A69194 #type complete TITLE 2-oxoacid-ferredoxin oxidoreductase (EC 1.2.7.-) alpha chain - Methanobacterium thermoautotrophicum (strain Delta H) ALTERNATE_NAMES 2-oxoacid:ferredoxin oxidoreductase (CoA-acetylating); 2-oxoisovalerate oxidoreductase beta chain [misidentification] ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 04-Feb-2000 ACCESSIONS A69194 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession A69194 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-348 ##label MTH !'##cross-references GB:AE000849; GB:AE000666; NID:g2621780; !1PIDN:AAB85209.1; PID:g2621790 !'##experimental_source strain Delta H GENETICS !$#gene MTH704 CLASSIFICATION #superfamily Helicobacter pylori 2-oxoacid ferredoxin !1oxidoreductase; 2-oxoacid ferredoxin oxidoreductase homology KEYWORDS oxidoreductase FEATURE !$1-183 #domain 2-oxoacid ferredoxin oxidoreductase homology !8#label FEO SUMMARY #length 348 #molecular-weight 38196 #checksum 2091 SEQUENCE /// ENTRY JC4919 #type complete TITLE 2-oxoacid-ferredoxin oxidoreductase (EC 1.2.7.-) alpha chain [validated] - Sulfolobus sp. (strain 7) ALTERNATE_NAMES 2-oxoacid:ferredoxin oxidoreductase (CoA-acetylating) ORGANISM #formal_name Sulfolobus sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS JC4919; PC4195 REFERENCE JC4919 !$#authors Zhang, Q.; Iwasaki, T.; Wakagi, T.; Oshima, T. !$#journal J. Biochem. (1996) 120:587-599 !$#title 2-Oxoacid:Ferredoxin oxidoreductase from the !1thermoacidophilic archaeon, Sulfolobus sp. strain 7. !$#cross-references MUID:97058305; PMID:8902625 !$#accession JC4919 !'##status preliminary !'##molecule_type DNA !'##residues 1-632 ##label ZHA1 !'##cross-references DDBJ:D64024; NID:g1565182; PIDN:BAA10898.1; !1PID:g1565183 !'##experimental_source strain 7 !$#accession PC4195 !'##status preliminary !'##molecule_type protein !'##residues 1-12 ##label ZHA2 COMPLEX heterodimer of alpha and beta chains FUNCTION !$#description catalyzes decarboxylation of pyruvate and 2-oxoglutarate CLASSIFICATION #superfamily Halobacterium halobium 2-oxoacid ferredoxin !1oxidoreductase; 2-oxoacid ferredoxin oxidoreductase homology KEYWORDS oxidoreductase FEATURE !$6-39 #region gamma-domain #status predicted\ !$210-270 #region alpha-domain #status predicted\ !$243-423 #domain 2-oxoacid ferredoxin oxidoreductase homology !8#label FEO SUMMARY #length 632 #molecular-weight 70758 #checksum 6229 SEQUENCE /// ENTRY S22396 #type complete TITLE pyruvate synthase (EC 1.2.7.1) alpha chain [validated] - Halobacterium salinarum ALTERNATE_NAMES pyruvate:ferredoxin 2-oxidoreductase (CoA-acetylating) ORGANISM #formal_name Halobacterium salinarum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-May-2000 ACCESSIONS S22396 REFERENCE S22396 !$#authors Plaga, W.; Lottspeich, F.; Oesterhelt, D. !$#journal Eur. J. Biochem. (1992) 205:391-397 !$#title Improved purification, crystallization and primary structure !1of pyruvate: ferredoxin oxidoreductase from Halobacterium !1halobium. !$#cross-references MUID:92209529; PMID:1555599 !$#accession S22396 !'##status preliminary !'##molecule_type DNA !'##residues 1-628 ##label PLA !'##cross-references EMBL:X64521; NID:g43497; PIDN:CAA45825.1; !1PID:g43498 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing !'##note the source was designated as Halobacterium halobium COMPLEX heterotetramer; 2 alpha chains (PIR:S22396), 2 beta chains !1(PIR:S22397) [validated, MUID:92209529] FUNCTION !$#description EC 1.2.7.1 [validated, MUID:92209529] CLASSIFICATION #superfamily Halobacterium halobium 2-oxoacid ferredoxin !1oxidoreductase; 2-oxoacid ferredoxin oxidoreductase homology KEYWORDS coenzyme A; oxidoreductase FEATURE !$2-628 #product pyruvate synthase alpha chain #status !8experimental #label MAT\ !$234-404 #domain 2-oxoacid ferredoxin oxidoreductase homology !8#label FEO SUMMARY #length 628 #molecular-weight 68052 #checksum 606 SEQUENCE /// ENTRY G69170 #type complete TITLE 2-oxoacid-ferredoxin oxidoreductase (EC 1.2.7.-) alpha chain - Methanobacterium thermoautotrophicum (strain Delta H) ALTERNATE_NAMES 2-oxoacid:ferredoxin oxidoreductase (CoA-acetylating) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS G69170 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession G69170 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-512 ##label MTH !'##cross-references GB:AE000836; GB:AE000666; NID:g2621601; !1PIDN:AAB85042.1; PID:g2621610 !'##experimental_source strain Delta H GENETICS !$#gene MTH536 CLASSIFICATION #superfamily Halobacterium halobium 2-oxoacid ferredoxin !1oxidoreductase; 2-oxoacid ferredoxin oxidoreductase homology KEYWORDS oxidoreductase FEATURE !$150-332 #domain 2-oxoacid ferredoxin oxidoreductase homology !8#label FEO SUMMARY #length 512 #molecular-weight 56279 #checksum 8622 SEQUENCE /// ENTRY XUECAG #type complete TITLE glycerol-3-phosphate O-acyltransferase (EC 2.3.1.15) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 01-Mar-2002 ACCESSIONS A00565; C42956; H65211 REFERENCE A92393 !$#authors Lightner, V.A.; Bell, R.M.; Modrich, P. !$#journal J. Biol. Chem. (1983) 258:10856-10861 !$#title The DNA sequences encoding plsB and dgk loci of Escherichia !1coli. !$#cross-references MUID:83291031; PMID:6309817 !$#accession A00565 !'##molecule_type DNA !'##residues 1-827 ##label LIG !'##note this sequence was partially confirmed by protein sequencing REFERENCE A42956 !$#authors Nichols, B.P.; Green, J.M. !$#journal J. Bacteriol. (1992) 174:5309-5316 !$#title Cloning and sequencing of Escherichia coli ubiC and !1purification of chorismate lyase. !$#cross-references MUID:92355505; PMID:1644758 !$#accession C42956 !'##status preliminary !'##molecule_type DNA !'##residues 805-827 ##label NIC !'##note sequence extracted from NCBI backbone (NCBIN:110475, !1NCBIP:110483) REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65211 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-827 ##label BLAT !'##cross-references GB:AE000477; GB:U00096; NID:g2367338; !1PIDN:AAC77011.1; PID:g1790474; UWGP:b4041 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene plsB !$#map_position 92 min FUNCTION !$#description this membrane-bound enzyme catalyzes the first step in de !1novo phospholipid biosynthesis, the condensation of !1glycerol-3-phosphate and fatty acid thioesters to yield !1lysophosphatidic acid; it may also function in the !1regulation of membrane biogenesis !$#pathway phospholipid biosynthesis CLASSIFICATION #superfamily glycerol-3-phosphate acyltransferase KEYWORDS acyltransferase; coenzyme A; membrane protein; phospholipid !1biosynthesis SUMMARY #length 827 #molecular-weight 93695 #checksum 732 SEQUENCE /// ENTRY XXECTG #type complete TITLE galactoside O-acetyltransferase (EC 2.3.1.18) [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES acetyl-CoA:beta-D-galactoside 6-acetyltransferase; thiogalactoside acetyltransferase; thiogalactoside transacetylase ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 01-Mar-2002 ACCESSIONS A94061; A90678; F64761; A23558; A25176 REFERENCE A94061 !$#authors Hediger, M.A.; Johnson, D.F.; Nierlich, D.P.; Zabin, I. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:6414-6418 !$#title DNA sequence of the lactose operon: the lacA gene and the !1transcriptional termination region. !$#cross-references MUID:86016712; PMID:3901000 !$#accession A94061 !'##molecule_type DNA !'##residues 1-203 ##label HED !'##cross-references GB:X51872; NID:g41891; PIDN:CAA36162.1; PID:g581122 REFERENCE A90678 !$#authors Fowler, A.V.; Hediger, M.A.; Musso, R.E.; Zabin, I. !$#journal Biochimie (1985) 67:101-108 !$#title The amino acid sequence of thiogalactoside transacetylase of !1Escherichia coli. !$#cross-references MUID:85200082; PMID:3922433 !$#accession A90678 !'##molecule_type protein !'##residues 1-203 ##label FOW REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64761 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-203 ##label BLAT !'##cross-references GB:AE000141; GB:U00096; NID:g1786532; !1PIDN:AAC73445.1; PID:g1786537; UWGP:b0342 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene lacA !$#map_position 8 min !$#start_codon TTG !$#note part of lac operon COMPLEX homodimer [validated, MUID:85200082] FUNCTION !$#description EC 2.3.1.18 [validated, MUID:85200082]; catalyzes the !1transfer of acetyl groups from acetyl-CoA to galactoside CLASSIFICATION #superfamily galactoside acetyltransferase KEYWORDS acyltransferase; coenzyme A; tandem repeat FEATURE !$1-203 #product galactoside O-acetyltransferase (partial) !8#status experimental #label MAT1\ !$2-203 #product galactoside O-acetyltransferase (partial) !8#status experimental #label MAT2\ !$58-63 #region 6-residue repeats ([IV]-G-X-N-[VS][IVLWY])\ !$98-103 #region 6-residue repeats ([IV]-G-X-N-[VS][IVLWY])\ !$134-139 #region 6-residue repeats ([IV]-G-X-N-[VS][IVLWY])\ !$140-145 #region 6-residue repeats ([IV]-G-X-N-[VS][IVLWY])\ !$152-157 #region 6-residue repeats ([IV]-G-X-N-[VS][IVLWY])\ !$158-163 #region 6-residue repeats ([IV]-G-X-N-[VS][IVLWY]) SUMMARY #length 203 #molecular-weight 22799 #checksum 2514 SEQUENCE /// ENTRY S50709 #type complete TITLE probable O-acetyltransferase (EC 2.3.1.-) YJL218w - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein HRA196; hypothetical protein J0224 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S50709; S57008; S45154 REFERENCE S50701 !$#authors Vandenbol, M.; Durand, P.; Bolle, P.A.; Dion, C.; !1Portetelle, D.; Hilger, F. !$#journal Yeast (1994) 10:1657-1662 !$#title Sequence analysis of a 40.2 kb DNA fragment located near the !1left telomere of yeast chromosome X. !$#cross-references MUID:95242842; PMID:7725802 !$#accession S50709 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-196 ##label VAN !'##cross-references EMBL:Z34098; NID:g496934; PIDN:CAA83992.1; !1PID:g496943 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1994 REFERENCE S56835 !$#authors Vandenbol, M.; Durand, P.; Portetelle, D.; Hilger, F. !$#submission submitted to the Protein Sequence Database, September 1995 !$#accession S57008 !'##molecule_type DNA !'##residues 1-196 ##label VAW !'##cross-references EMBL:Z49493; NID:g1015607; PIDN:CAA89515.1; !1PID:g1015608; GSPDB:GN00010; MIPS:YJL218w GENETICS !$#gene MIPS:YJL218w !'##cross-references SGD:S0003754 !$#map_position 10L CLASSIFICATION #superfamily galactoside acetyltransferase KEYWORDS acyltransferase SUMMARY #length 196 #molecular-weight 21479 #checksum 3141 SEQUENCE /// ENTRY A48026 #type complete TITLE sterol O-acyltransferase (EC 2.3.1.26) - human ALTERNATE_NAMES ACAT; acyl-coenzyme A cholesterol acyltransferase ORGANISM #formal_name Homo sapiens #common_name man DATE 28-May-1999 #sequence_revision 28-May-1999 #text_change 05-May-2000 ACCESSIONS A59038; A48026 REFERENCE A59038 !$#authors Chang, C.C.Y.; Chang, T.Y. !$#submission submitted to GenBank, May 1999 !$#description Molecular cloning and functional expression of human !1acyl-coenzyme A:cholesterol acyltransferase cDNA in mutant !1Chinese hamster ovary cells. !$#contents correction !$#accession A59038 !'##molecule_type mRNA !'##residues 1-550 ##label CHA2 !'##cross-references GB:L21934; NID:g4878021; PIDN:AAC37532.2; !1PID:g4878022 REFERENCE A48026 !$#authors Chang, C.C.Y.; Huh, H.Y.; Cadigan, K.M.; Chang, T.Y. !$#journal J. Biol. Chem. (1993) 268:20747-20755 !$#title Molecular cloning and functional expression of human !1acyl-coenzyme A:cholesterol acyltransferase cDNA in mutant !1Chinese hamster ovary cells. !$#cross-references MUID:94012607; PMID:8407899 !$#accession A48026 !'##molecule_type mRNA !'##residues 1-206,'R',208-550 ##label CHA1 !'##cross-references GB:L21934 GENETICS !$#gene GDB:SOAT; STAT; ACAT !'##cross-references GDB:251696; OMIM:102642 !$#map_position 1q25-1q25 FUNCTION !$#description catalyzes the esterification of cholesterol by acyl-CoA !$#pathway cholesterol metabolism !$#note helps maintain cellular cholesterol homeostasis; plays a !1role in the development of atherosclerosis; enzyme activity !1is stimulated by cholesterol and oxygenated sterols CLASSIFICATION #superfamily sterol O-acyltransferase KEYWORDS acyltransferase; cholesterol metabolism; coenzyme A; !1endoplasmic reticulum; glycoprotein; macrophage; !1transmembrane protein FEATURE !$409,491 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 550 #molecular-weight 64762 #checksum 627 SEQUENCE /// ENTRY I49454 #type complete TITLE sterol O-acyltransferase (EC 2.3.1.26) - mouse ALTERNATE_NAMES acyl-coenzyme A cholesterol acyltransferase ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 02-Jun-2000 ACCESSIONS I49454; JC4617 REFERENCE I49454 !$#authors Uelmen, P.J.; Oka, K.; Sullivan, M.C.; Chang, T. !$#journal J. Biol. Chem. (1995) 270:26192-26201 !$#title Molecular cloning of mouse ACACT. !$#cross-references MUID:96064687; PMID:7592824 !$#accession I49454 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-540 ##label RES !'##cross-references GB:L42293; NID:g1066809; PIDN:AAC42075.1; !1PID:g1066810 REFERENCE JC4617 !$#authors Green, S.; Steinberg, D.; Quehenberger, O. !$#journal Biochem. Biophys. Res. Commun. (1996) 218:924-929 !$#title Cloning and expression in Xenopus oocytes of a mouse !1homologue of the human acylcoenzyme A: Cholesterol !1acyltransferase and its potential role in metabolism of !1oxidized LDL. !$#cross-references MUID:96158986; PMID:8579615 !$#accession JC4617 !'##molecule_type mRNA !'##residues 1-194,'R',196-540 ##label GRE !'##cross-references GB:S81092; NID:g1478335; PIDN:AAB36050.1; !1PID:g1478336 !'##experimental_source peritoneal macrophages COMMENT This enzyme helps maintain cellular cholesterol homeostasis !1by catalyzing esterification of cholesterol; it plays a role !1in the development of atherosclerosis. This activity is !1activated by cholesterol and oxygenated sterols. GENETICS !$#gene ACACT !$#map_position 1 CLASSIFICATION #superfamily sterol O-acyltransferase KEYWORDS acyltransferase; cholesterol; coenzyme A; endoplasmic !1reticulum; transmembrane protein SUMMARY #length 540 #molecular-weight 63739 #checksum 2257 SEQUENCE /// ENTRY XXECC1 #type complete TITLE chloramphenicol O-acetyltransferase (EC 2.3.1.28) - Escherichia coli plasmids ORGANISM #formal_name Escherichia coli DATE 30-Nov-1980 #sequence_revision 24-Sep-1981 #text_change 05-May-2000 ACCESSIONS A93220; A93219; A91275; A00566 REFERENCE A93220 !$#authors Shaw, W.V.; Packman, L.C.; Burleigh, B.D.; Dell, A.; Morris, !1H.R.; Hartley, B.S. !$#journal Nature (1979) 282:870-872 !$#title Primary structure of a chloramphenicol acetyltransferse !1specified by R plasmids. !$#cross-references MUID:80078151; PMID:390404 !$#contents plasmid JR66b !$#accession A93220 !'##molecule_type protein !'##residues 1-219 ##label SHA !'##note the chloramphenicol binding site may include regions near !1residues 31 and 192-196. Lys-136 may be involved in the !1formation of salt bridges between the chains REFERENCE A93219 !$#authors Alton, N.K.; Vapnek, D. !$#journal Nature (1979) 282:864-869 !$#title Nucleotide sequence analysis of the chloramphenicol !1resistance transposon Tn9. !$#cross-references MUID:80078150; PMID:390403 !$#contents transposable genetic element Tn9 !$#accession A93219 !'##molecule_type DNA !'##residues 1-219 ##label ALT !'##cross-references GB:V00622; GB:J01841; NID:g43766; PIDN:CAA23899.1; !1PID:g43767 !'##note residues 77-219 correspond to a probable fusidic acid !1resistance protein REFERENCE A91275 !$#authors Marcoli, R.; Iida, S.; Bickle, T.A. !$#journal FEBS Lett. (1980) 110:11-14 !$#title The DNA sequence of an IS1-flanked transposon coding for !1resistance to chloramphenicol and fusidic acid. !$#cross-references MUID:80113302; PMID:7353655 !$#contents transposon Tncam204, derived from the R plasmid NR1 [=R100] !$#accession A91275 !'##molecule_type DNA !'##residues 1-219 ##label MAR !'##cross-references GB:V00623; GB:J01842; NID:g43768; PIDN:CAA23900.1; !1PID:g43769 COMMENT This enzyme, a type I variant mediated by an R plasmid in E. !1coli, exists as a tetramer of identical chains. GENETICS !$#genome plasmid CLASSIFICATION #superfamily chloramphenicol acetyltransferase KEYWORDS acetyl-CoA; acyltransferase; antibiotic resistance; coenzyme !1A; homotrimer SUMMARY #length 219 #molecular-weight 25663 #checksum 7746 SEQUENCE /// ENTRY JQ0972 #type complete TITLE chloramphenicol O-acetyltransferase (EC 2.3.1.28) - Acinetobacter baumannii ORGANISM #formal_name Acinetobacter baumannii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-May-2000 ACCESSIONS JQ0972 REFERENCE JQ0972 !$#authors Elisha, B.G.; Steyn, L.M. !$#journal Plasmid (1991) 25:96-104 !$#title Identification of an acinetobacter baumannii gene region !1with sequence and organizational similarity to Tn2670. !$#cross-references MUID:91312959; PMID:1650008 !$#accession JQ0972 !'##molecule_type DNA !'##residues 1-219 ##label ELI !'##cross-references GB:M37690; NID:g141788; PIDN:AAA62571.1; !1PID:g141789 !'##experimental_source strain SAK GENETICS !$#gene cat CLASSIFICATION #superfamily chloramphenicol acetyltransferase KEYWORDS acyltransferase; antibiotic resistance; coenzyme A; !1homotrimer SUMMARY #length 219 #molecular-weight 25663 #checksum 7746 SEQUENCE /// ENTRY A24651 #type complete TITLE chloramphenicol O-acetyltransferase (EC 2.3.1.28) - Proteus mirabilis (strain PM13) ORGANISM #formal_name Proteus mirabilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-May-2000 ACCESSIONS A24651 REFERENCE A24651 !$#authors Charles, I.G.; Keyte, J.W.; Shaw, W.V. !$#journal J. Bacteriol. (1985) 164:123-129 !$#title Nucleotide sequence analysis of the cat gene of Proteus !1mirabilis: comparison with the type I (Tn9) cat gene. !$#cross-references MUID:86008040; PMID:3900035 !$#accession A24651 !'##molecule_type DNA !'##residues 1-217 ##label CHA !'##cross-references GB:M11587; NID:g150882; PIDN:AAA25655.1; !1PID:g150883 GENETICS !$#gene cat CLASSIFICATION #superfamily chloramphenicol acetyltransferase KEYWORDS acyltransferase; antibiotic resistance; coenzyme A; !1homotrimer SUMMARY #length 217 #molecular-weight 25313 #checksum 2262 SEQUENCE /// ENTRY XXECC3 #type complete TITLE chloramphenicol O-acetyltransferase (EC 2.3.1.28) III - Escherichia coli ORGANISM #formal_name Escherichia coli DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 05-May-2000 ACCESSIONS A00567 REFERENCE A00567 !$#authors Packman, L.C.; Kaye, N.M.C.; Fitton, J.E. !$#citation unpublished results, cited by Shaw, W.V., CRC Crit. Rev. !1Biochem. 14, 1-46, 1983 !$#accession A00567 !'##molecule_type protein !'##residues 1-203 ##label PAC CLASSIFICATION #superfamily chloramphenicol acetyltransferase KEYWORDS acyltransferase; antibiotic resistance; coenzyme A SUMMARY #length 203 #molecular-weight 23824 #checksum 9862 SEQUENCE /// ENTRY XXEBCF #type complete TITLE chloramphenicol O-acetyltransferase (EC 2.3.1.28) III - Shigella flexneri plasmid R387 ORGANISM #formal_name Shigella flexneri DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 05-May-2000 ACCESSIONS S00602 REFERENCE S00602 !$#authors Murray, I.A.; Hawkins, A.R.; Keyte, J.W.; Shaw, W.V. !$#journal Biochem. J. (1988) 252:173-179 !$#title Nucleotide sequence analysis and overexpression of the gene !1encoding a type III chloramphenicol acetyltransferase. !$#cross-references MUID:88339790; PMID:3048245 !$#accession S00602 !'##molecule_type DNA !'##residues 1-213 ##label MUR !'##cross-references EMBL:X07848; NID:g47024; PIDN:CAA30695.1; !1PID:g47025 GENETICS !$#gene catIII !$#genome plasmid CLASSIFICATION #superfamily chloramphenicol acetyltransferase KEYWORDS acetyl-CoA; acyltransferase; antibiotic resistance; coenzyme !1A; homotrimer FEATURE !$1-213 #product chloramphenicol acetyltransferase III !8#status experimental #label MAT\ !$189 #active_site His #status experimental SUMMARY #length 213 #molecular-weight 24993 #checksum 8499 SEQUENCE /// ENTRY XXSACC #type complete TITLE chloramphenicol O-acetyltransferase (EC 2.3.1.28) - Staphylococcus aureus plasmids ORGANISM #formal_name Staphylococcus aureus DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 05-May-2000 ACCESSIONS A00568; S09567 REFERENCE A91791 !$#authors Horinouchi, S.; Weisblum, B. !$#journal J. Bacteriol. (1982) 150:815-825 !$#title Nucleotide sequence and functional map of pC194, a plasmid !1that specifies inducible chloramphenicol resistance. !$#cross-references MUID:82167188; PMID:6950931 !$#accession A00568 !'##molecule_type DNA !'##residues 1-216 ##label HOR !'##cross-references GB:V01277; GB:J01754; NID:g46531; PIDN:CAA24586.1; !1PID:g46534 !'##experimental_source plasmid pC194 REFERENCE S09565 !$#authors Minton, N.P.; Swinfield, T.J.; Brehm, J.K.; Oultram, J.D. !$#journal Nucleic Acids Res. (1990) 18:1651 !$#title The Gram-positive cloning vector pBD64 arose by a 1844 bp !1deletion of pC194 derived DNA. !$#cross-references MUID:90221915; PMID:2326208 !$#accession S09567 !'##status preliminary !'##molecule_type DNA !'##residues 1-216 ##label MIN !'##cross-references EMBL:X51450; NID:g57998; PID:g58001 !'##experimental_source plasmid pCB64 GENETICS !$#genome plasmid CLASSIFICATION #superfamily chloramphenicol acetyltransferase KEYWORDS acetyl-CoA; acyltransferase; antibiotic resistance; coenzyme !1A SUMMARY #length 216 #molecular-weight 25039 #checksum 155 SEQUENCE /// ENTRY S04711 #type complete TITLE chloramphenicol O-acetyltransferase (EC 2.3.1.28) - Clostridium difficile ORGANISM #formal_name Clostridium difficile DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-May-2000 ACCESSIONS S04711 REFERENCE S04711 !$#authors Wren, B.W.; Mullany, P.; Clayton, C.; Tabaqchali, S. !$#journal Nucleic Acids Res. (1989) 17:4877 !$#title Nucleotide sequence of a chloramphenicol acetyl transferase !1gene from Clostridium difficile. !$#cross-references MUID:89315228; PMID:2748343 !$#accession S04711 !'##molecule_type DNA !'##residues 1-212 ##label WRE !'##cross-references EMBL:X15100; NID:g40432; PIDN:CAA33203.1; !1PID:g40433 GENETICS !$#gene catD CLASSIFICATION #superfamily chloramphenicol acetyltransferase KEYWORDS acyltransferase; antibiotic resistance; coenzyme A SUMMARY #length 212 #molecular-weight 24835 #checksum 4194 SEQUENCE /// ENTRY XXSAC2 #type complete TITLE chloramphenicol O-acetyltransferase (EC 2.3.1.28) [validated] - Staphylococcus aureus plasmid ORGANISM #formal_name Staphylococcus aureus DATE 03-Aug-1984 #sequence_revision 28-Aug-1985 #text_change 05-May-2000 ACCESSIONS A00569; S40420; A24362; A44849 REFERENCE A00569 !$#authors Shaw, W.V.; Brenner, D.G.; LeGrice, S.F.J.; Skinner, S.E.; !1Hawkins, A.R. !$#journal FEBS Lett. (1985) 179:101-106 !$#title Chloramphenicol acetyltransferase gene of staphylococcal !1plasmid pC221. Nucleotide sequence analysis and expression !1studies. !$#cross-references MUID:85076982; PMID:3855295 !$#accession A00569 !'##molecule_type DNA !'##residues 1-215 ##label SHA !'##cross-references GB:X02166; NID:g46545; PIDN:CAA26105.1; PID:g46548 !'##experimental_source plasmid pC221 REFERENCE S40418 !$#authors Projan, S.J.; Kornblum, J.; Moghazeh, S.L.; Edelman, I.; !1Gennaro, M.L.; Novick, R.P. !$#journal Mol. Gen. Genet. (1985) 199:452-464 !$#title Comparative sequence and functional analysis of pT181 and !1pC221, cognate plasmid replicons from Staphylococcus aureus. !$#cross-references MUID:85295465; PMID:2993795 !$#accession S40420 !'##status preliminary !'##molecule_type DNA !'##residues 1-215 ##label PRO !'##cross-references EMBL:X02529; NID:g46630; PIDN:CAA26367.1; !1PID:g46632 !'##experimental_source plasmid pC221 !'##note this enzyme is an effector of chloramphenicol resistance in !1bacteria REFERENCE A24362 !$#authors Bruckner, R.; Matzura, H. !$#journal EMBO J. (1985) 4:2295-2300 !$#title Regulation of the inducible chloramphenicol !1acetyltransferase gene of the Staphylococcus aureus plasmid !1pUB112. !$#cross-references MUID:86081739; PMID:3865770 !$#accession A24362 !'##molecule_type DNA !'##residues 1-119,'F',121-160,'S',162-200,'I',202-208,'N',210-215 !1##label BRU !'##cross-references GB:X02872; NID:g46536; PIDN:CAA26631.1; PID:g46537 !'##experimental_source plasmid pUB112 REFERENCE A44849 !$#authors Cardoso, M.; Schwarz, S. !$#journal J. Gen. Microbiol. (1992) 138:275-281 !$#title Characterization of the chloramphenicol acetyltransferase !1variants encoded by the plasmids pSCS6 and pSCS7 from !1Staphylococcus aureus. !$#cross-references MUID:92226689; PMID:1564439 !$#accession A44849 !'##molecule_type DNA !'##residues 1-41,'S',43-138,'L',140-200,'I',202-208,'K',210-215 ##label !1CAR !'##experimental_source chloramphenicol resistance plasmid pSCS6 !'##note sequence extracted from NCBI backbone (NCBIP:94699) GENETICS !$#genome plasmid COMPLEX homotrimer FUNCTION !$#description catalyzes the acetyl-CoA-dependent acetylation of the !1antibiotic chloramphenicol CLASSIFICATION #superfamily chloramphenicol acetyltransferase KEYWORDS acetyl-CoA; acyltransferase; antibiotic resistance; coenzyme !1A; homotrimer SUMMARY #length 215 #molecular-weight 25745 #checksum 5270 SEQUENCE /// ENTRY XXBSCP #type complete TITLE chloramphenicol O-acetyltransferase (EC 2.3.1.28) - Bacillus pumilus ORGANISM #formal_name Bacillus pumilus DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 05-May-2000 ACCESSIONS A00570; A25026 REFERENCE A00570 !$#authors Harwood, C.R.; Williams, D.M.; Lovett, P.S. !$#journal Gene (1983) 24:163-169 !$#title Nucleotide sequence of a Bacillus pumilus gene specifying !1chloramphenicol acetyltransferase. !$#cross-references MUID:84059077; PMID:6315534 !$#accession A00570 !'##molecule_type DNA !'##residues 1-220 ##label HAR !'##cross-references GB:K00544; GB:M10591; NID:g142634; PIDN:AAA22289.1; !1PID:g551695 !'##experimental_source NCIB 8600 REFERENCE A25026 !$#authors Ambulos Jr., N.P.; Mongkolsuk, S.; Kaufman, J.D.; Lovett, !1P.S. !$#journal J. Bacteriol. (1985) 164:696-703 !$#title Chloramphenicol-induced translation of cat-86 mRNA requires !1two cis-acting regulatory regions. !$#cross-references MUID:86033629; PMID:2414270 !$#accession A25026 !'##molecule_type DNA !'##residues 1-220 ##label AMB !'##cross-references GB:K00544; GB:M10591; NID:g142634; PIDN:AAA22289.1; !1PID:g551695 GENETICS !$#start_codon TTG CLASSIFICATION #superfamily chloramphenicol acetyltransferase KEYWORDS acetyl-CoA; acyltransferase; antibiotic resistance; coenzyme !1A SUMMARY #length 220 #molecular-weight 26018 #checksum 3848 SEQUENCE /// ENTRY B53402 #type complete TITLE serine O-acetyltransferase (EC 2.3.1.30) cysE [validated] - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS B53402; S66122; G69611 REFERENCE A53402 !$#authors Gagnon, Y.; Breton, R.; Putzer, H.; Pelchat, M.; !1Grunberg-Manago, M.; Lapointe, J. !$#journal J. Biol. Chem. (1994) 269:7473-7482 !$#title Clustering and co-transcription of the Bacillus subtilis !1genes encoding the aminoacyl-tRNA synthetases specific for !1glutamate and for cysteine and the first enzyme for cysteine !1biosynthesis. !$#cross-references MUID:94171772; PMID:7510287 !$#accession B53402 !'##status preliminary !'##molecule_type DNA !'##residues 1-217 ##label GAG !'##cross-references GB:L14580; NID:g289278; PIDN:AAA21797.1; !1PID:g289283 REFERENCE S65967 !$#authors Ogasawara, N.; Nakai, S.; Yoshikawa, H. !$#journal DNA Res. (1994) 1:1-14 !$#title Systematic sequencing of the 180 kilobase region of the !1Bacillus subtilis chromosome containing the replication !1origin. !$#cross-references MUID:96051385; PMID:7584024 !$#accession S66122 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-217 ##label OGA !'##cross-references EMBL:D26185; NID:g467326; PIDN:BAA05327.1; !1PID:g467481 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1993 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69611 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-217 ##label KUN !'##cross-references GB:Z99104; GB:AL009126; NID:g2632267; !1PIDN:CAB11869.1; PID:g2632360 !'##experimental_source strain 168 GENETICS !$#gene cysE; cysA !$#start_codon GTG FUNCTION !$#description EC 2.3.1.30 [validated, MUID:94171772] !$#note rate-limiting step in cysteine biosynthesis CLASSIFICATION #superfamily Bacillus serine acetyltransferase; serine !1acetyltransferase homology KEYWORDS acyltransferase; coenzyme A FEATURE !$9-169 #domain serine acetyltransferase homology #label SAT SUMMARY #length 217 #molecular-weight 24143 #checksum 9360 SEQUENCE /// ENTRY E53402 #type complete TITLE serine O-acetyltransferase (EC 2.3.1.30) cysE [similarity] - Bacillus stearothermophilus ORGANISM #formal_name Bacillus stearothermophilus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-May-2000 ACCESSIONS E53402 REFERENCE A53402 !$#authors Gagnon, Y.; Breton, R.; Putzer, H.; Pelchat, M.; !1Grunberg-Manago, M.; Lapointe, J. !$#journal J. Biol. Chem. (1994) 269:7473-7482 !$#title Clustering and co-transcription of the Bacillus subtilis !1genes encoding the aminoacyl-tRNA synthetases specific for !1glutamate and for cysteine and the first enzyme for cysteine !1biosynthesis. !$#cross-references MUID:94171772; PMID:7510287 !$#accession E53402 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-225 ##label GAG GENETICS !$#gene cysE FUNCTION !$#pathway cysteine biosynthesis !$#note rate-limiting step CLASSIFICATION #superfamily Bacillus serine acetyltransferase; serine !1acetyltransferase homology KEYWORDS acyltransferase; coenzyme A FEATURE !$9-169 #domain serine acetyltransferase homology #label SAT SUMMARY #length 225 #molecular-weight 25046 #checksum 1164 SEQUENCE /// ENTRY B64671 #type complete TITLE serine O-acetyltransferase (EC 2.3.1.30) - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-May-2000 ACCESSIONS B64671 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession B64671 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-171 ##label TOM !'##cross-references GB:AE000626; GB:AE000511; NID:g2314360; !1PIDN:AAD08254.1; PID:g2314370; TIGR:HP1210 CLASSIFICATION #superfamily Bacillus serine acetyltransferase; serine !1acetyltransferase homology KEYWORDS acyltransferase; coenzyme A FEATURE !$7-167 #domain serine acetyltransferase homology #label SAT SUMMARY #length 171 #molecular-weight 18342 #checksum 5098 SEQUENCE /// ENTRY S75606 #type complete TITLE serine O-acetyltransferase (EC 2.3.1.30) cysE - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein slr1348 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S75606; S72547 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75606 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-249 ##label KAN !'##cross-references EMBL:D90912; GB:AB001339; NID:g1653228; !1PIDN:BAA18167.1; PID:g1653252 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 REFERENCE S72547 !$#authors Sakamoto, T.; Murata, N. !$#journal Plant Mol. Biol. (1995) 29:187 !$#title Sequence announcement. !$#accession S72547 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-79,'S',81-249 ##label SAK !'##cross-references EMBL:D13777; NID:g1100769; PIDN:BAA02919.1; !1PID:g1100770 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1992 GENETICS !$#gene cysE !$#start_codon GTG CLASSIFICATION #superfamily Bacillus serine acetyltransferase; serine !1acetyltransferase homology KEYWORDS acyltransferase; coenzyme A FEATURE !$8-168 #domain serine acetyltransferase homology #label SAT SUMMARY #length 249 #molecular-weight 27336 #checksum 4241 SEQUENCE /// ENTRY D43706 #type complete TITLE serine O-acetyltransferase (EC 2.3.1.30) nifP - Azotobacter chroococcum ORGANISM #formal_name Azotobacter chroococcum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-May-2000 ACCESSIONS D43706 REFERENCE A43706 !$#authors Evans, D.J.; Jones, R.; Woodley, P.R.; Wilborn, J.R.; !1Robson, R.L. !$#journal J. Bacteriol. (1991) 173:5457-5469 !$#title Nucleotide sequence and genetic analysis of the Azotobacter !1chroococcum nifUSVWZM gene cluster, including a new gene !1(nifP) which encodes a serine acetyltransferase. !$#cross-references MUID:91358323; PMID:1885524 !$#accession D43706 !'##status preliminary !'##molecule_type DNA !'##residues 1-269 ##label EVA !'##cross-references EMBL:M60090; NID:g142386; PIDN:AAA22162.1; !1PID:g142390 CLASSIFICATION #superfamily Bacillus serine acetyltransferase; serine !1acetyltransferase homology KEYWORDS acyltransferase; coenzyme A FEATURE !$10-169 #domain serine acetyltransferase homology #label SAT SUMMARY #length 269 #molecular-weight 28578 #checksum 6787 SEQUENCE /// ENTRY XYECSA #type complete TITLE serine O-acetyltransferase (EC 2.3.1.30) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 01-Mar-2002 ACCESSIONS A27896; A34563; S47828; A65161 REFERENCE A27896 !$#authors Denk, D.; Bock, A. !$#journal J. Gen. Microbiol. (1987) 133:515-525 !$#title L-Cysteine biosynthesis in Escherichia coli: nucleotide !1sequence and expression of the serine acetyltransferase !1(cysE) gene from the wild-type and a cysteine-excreting !1mutant. !$#cross-references MUID:88009872; PMID:3309158 !$#accession A27896 !'##molecule_type DNA !'##residues 1-273 ##label DEN !'##cross-references GB:M15745; NID:g145675; PIDN:AAA23648.1; !1PID:g145676 REFERENCE A34563 !$#authors Tei, H.; Murata, K.; Kimura, A. !$#journal Biochem. Biophys. Res. Commun. (1990) 167:948-955 !$#title Structure and expression of CYSX, the second gene in the !1Escherichia coli K-12 CYSE locus. !$#cross-references MUID:90211342; PMID:2108679 !$#accession A34563 !'##molecule_type DNA !'##residues 1-273 ##label TEI !'##cross-references GB:M34333; NID:g145693; PIDN:AAA23659.1; !1PID:g145694 REFERENCE S47666 !$#authors Plunkett, G. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S47828 !'##molecule_type DNA !'##residues 1-273 ##label PLU !'##cross-references EMBL:U00039; NID:g466582; PIDN:AAB18584.1; !1PID:g466745 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65161 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-273 ##label BLAT !'##cross-references GB:AE000438; GB:U00096; NID:g2367251; !1PIDN:AAC76631.1; PID:g1790035; UWGP:b3607 !'##experimental_source strain K-12, substrain MG1655 COMMENT This enzyme catalyzes the conversion of L-serine to O-acetyl !1serine (by acetyl CoA), which is in turn converted to !1L-cysteine. It is sensitive to feedback inhibition by !1L-cysteine. GENETICS !$#gene cysE !$#map_position 81 min CLASSIFICATION #superfamily serine acetyltransferase; serine !1acetyltransferase homology KEYWORDS aminoacyltransferase; coenzyme A; cysteine biosynthesis FEATURE !$84-244 #domain serine acetyltransferase homology #label SAT SUMMARY #length 273 #molecular-weight 29316 #checksum 6276 SEQUENCE /// ENTRY JC1293 #type complete TITLE serine O-acetyltransferase (EC 2.3.1.30) - Buchnera aphidicola ORGANISM #formal_name Buchnera aphidicola DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 05-May-2000 ACCESSIONS JC1293 REFERENCE JC1291 !$#authors Lai, C.Y.; Baumann, P. !$#journal Gene (1992) 119:113-118 !$#title Sequence analysis of a DNA fragment from Buchnera aphidicola !1(an endosymbiont of aphids) containing genes homologous to !1dnaG, rpoD, cysE, and secB. !$#cross-references MUID:93012960; PMID:1398077 !$#accession JC1293 !'##molecule_type DNA !'##residues 1-261 ##label LAI !'##cross-references GB:M90644; NID:g144135; PIDN:AAA73232.1; !1PID:g144137 GENETICS !$#gene cysE CLASSIFICATION #superfamily serine acetyltransferase; serine !1acetyltransferase homology KEYWORDS acyltransferase; coenzyme A; cysteine biosynthesis FEATURE !$84-245 #domain serine acetyltransferase homology #label SAT SUMMARY #length 261 #molecular-weight 28914 #checksum 5940 SEQUENCE /// ENTRY XYIMHA #type complete TITLE homoserine O-acetyltransferase (EC 2.3.1.31) - fungus (Ascobolus immersus) ORGANISM #formal_name Ascobolus immersus DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 05-May-2000 ACCESSIONS JT0271 REFERENCE JT0271 !$#authors Goyon, C.; Faugeron, G.; Rossignol, J.L. !$#journal Gene (1988) 63:297-308 !$#title Molecular cloning and characterization of the met2 gene from !1Ascobolus immersus. !$#cross-references MUID:88255875; PMID:2838393 !$#accession JT0271 !'##molecule_type DNA !'##residues 1-518 ##label GOY !'##cross-references GB:M26662; NID:g166479; PIDN:AAA32681.1; !1PID:g166480 GENETICS !$#gene met2 !$#introns 17/1 CLASSIFICATION #superfamily homoserine acetyltransferase KEYWORDS acyltransferase; coenzyme A; methionine biosynthesis SUMMARY #length 518 #molecular-weight 57717 #checksum 3888 SEQUENCE /// ENTRY B41864 #type complete TITLE acetyl-CoA-deacetylcephalosporin C acetyltransferase (EC 2.3.1.-) precursor - fungus (Acremonium chrysogenum) CONTAINS acetyl-CoA-deacetylcephalosporin C O-acetyltransferase chain I; acetyl-CoA-deacetylcephalosporin C O-acetyltransferase chain II ORGANISM #formal_name Acremonium chrysogenum DATE 03-Feb-1994 #sequence_revision 03-Feb-1994 #text_change 10-Dec-1999 ACCESSIONS B41864; S28917; JC1105; JQ1394; PQ0268; S25139 REFERENCE A41864 !$#authors Gutierrez, S.; Velasco, J.; Fernandez, F.J.; Martin, J.F. !$#journal J. Bacteriol. (1992) 174:3056-3064 !$#title The cefG gene of Cephalosporium acremonium is linked to the !1cefEF gene and encodes a deacetylcephalosporin C !1acetyltransferase closely related to homoserine !1O-acetyltransferase. !$#cross-references MUID:92234966; PMID:1569032 !$#accession B41864 !'##molecule_type DNA !'##residues 1-444 ##label GUT !'##cross-references GB:M91649; NID:g166449; PIDN:AAA32673.1; !1PID:g166450 !'##experimental_source strain C10 !'##note sequence extracted from NCBI backbone (NCBIN:97567, !1NCBIP:97581) REFERENCE S28917 !$#authors Mathison, L.; Soliday, C.; Stepan, T.; Aldrich, T.; !1Rambosek, J. !$#journal Curr. Genet. (1993) 23:33-41 !$#title Cloning, characterization, and use in strain improvement of !1the Cephalosporium acremonium gene cefG encoding acetyl !1transferase. !$#cross-references MUID:93153828; PMID:8428381 !$#accession S28917 !'##molecule_type DNA !'##residues 1-444 ##label MATH !'##cross-references EMBL:X65583 !'##note the authors predicted Met-46 to be the initiator REFERENCE JC1105 !$#authors Matsuda, A.; Sugiura, H.; Matsuyama, K.; Matsumoto, H.; !1Ichikawa, S.; Komatsu, K. !$#journal Biochem. Biophys. Res. Commun. (1992) 186:40-46 !$#title Cloning and disruption of the cefG gene encoding acetyl !1coenzyme A: deacetylcephalosporin C O-acetyltransferase from !1Acremonium chrysogenum. !$#cross-references MUID:92337627; PMID:1632779 !$#accession JC1105 !'##molecule_type DNA !'##residues 1-444 ##label MA2 !'##experimental_source strain IS-5 !'##note the authors predicted Met-60 to be the initiator REFERENCE JQ1394 !$#authors Matsuda, A.; Sugiura, H.; Matsuyama, K.; Matsumoto, H.; !1Ichikawa, S.; Komatsu, K. !$#journal Biochem. Biophys. Res. Commun. (1992) 182:995-1001 !$#title Molecular cloning of acetyl coenzyme A: !1deacetylcephalosporin C O-acetyltransferase cDNA from !1Acremonium chrysogenum: sequence and expression of catalytic !1activity in yeast. !$#cross-references MUID:92171978; PMID:1540196 !$#accession JQ1394 !'##molecule_type mRNA !'##residues 'NS',51-444 ##label MAT !$#accession PQ0268 !'##molecule_type protein !'##residues 72,'X',74-91;319-345 ##label MA3 !'##note the authors predicted Met-60 to be the initiator COMMENT This enzyme catalyzes the conversion of !1deacetylcephalosporin C to cephalosporin C, the terminal !1reaction in the biosynthesis of cephalosporin C. GENETICS !$#gene cefG !$#introns 187/2; 303/1 CLASSIFICATION #superfamily homoserine acetyltransferase KEYWORDS acyltransferase FEATURE !$72-318 #product acetyl-CoA-deacetylcephalosporin C !8O-acetyltransferase chain I #status experimental !8#label ACI\ !$319-444 #product acetyl-CoA-deacetylcephalosporin C !8O-acetyltransferase chain II #status experimental !8#label AII SUMMARY #length 444 #molecular-weight 49160 #checksum 1317 SEQUENCE /// ENTRY S63251 #type complete TITLE homoserine O-acetyltransferase (EC 2.3.1.31) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein N0615; protein YNL277w ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S63251; A27163 REFERENCE S63245 !$#authors Messenguy, F.; Dubois, E.; Vierendeels, F.; Scherens, B.; !1Pierard, A.; Glansdorff, N. !$#submission submitted to the Protein Sequence Database, April 1996 !$#accession S63251 !'##molecule_type DNA !'##residues 1-486 ##label MES !'##cross-references EMBL:Z71553; NID:g1302343; PIDN:CAA96188.1; !1PID:g1302344; GSPDB:GN00014; MIPS:YNL277w !'##experimental_source strain S288C REFERENCE A27163 !$#authors Langin, T.; Faugeron, G.; Goyon, C.; Nicolas, A.; Rossignol, !1J.L. !$#journal Gene (1986) 49:283-293 !$#title The MET2 gene of Saccharomyces cerevisiae: molecular cloning !1and nucleotide sequence. !$#cross-references MUID:87192018; PMID:3552887 !$#accession A27163 !'##molecule_type DNA !'##residues 1-428,'ATMPSYWSLS' ##label LAN !'##cross-references EMBL:M15675; NID:g171937; PIDN:AAA34775.1; !1PID:g171938 GENETICS !$#gene SGD:MET2; MIPS:YNL277w !'##cross-references SGD:S0005221; MIPS:YNL277w !$#map_position 14L CLASSIFICATION #superfamily homoserine acetyltransferase KEYWORDS acyltransferase; coenzyme A; transmembrane protein FEATURE !$145-161 #domain transmembrane #status predicted #label TMM SUMMARY #length 486 #molecular-weight 53659 #checksum 716 SEQUENCE /// ENTRY SYHUAL #type complete TITLE 5-aminolevulinate synthase (EC 2.3.1.37) precursor, nonspecific, mitochondrial - human ALTERNATE_NAMES 5-aminolevulinate synthase 1; delta-aminolevulinate synthase, housekeeping ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1990 #sequence_revision 23-Aug-1996 #text_change 05-May-2000 ACCESSIONS S13682; A27834 REFERENCE S13682 !$#authors Bishop, D.F. !$#journal Nucleic Acids Res. (1990) 18:7187-7188 !$#title Two different genes encode delta-aminolevulinate synthase in !1humans: nucleotide sequences of cDNAs for the housekeeping !1and erythroid genes. !$#cross-references MUID:91088347; PMID:2263504 !$#accession S13682 !'##molecule_type mRNA !'##residues 1-640 ##label BIS !'##cross-references EMBL:X56351; NID:g28582; PIDN:CAA39794.1; !1PID:g28583 REFERENCE A27834 !$#authors Bawden, M.J.; Borthwick, I.A.; Healy, H.M.; Morris, C.P.; !1May, B.K.; Elliott, W.H. !$#journal Nucleic Acids Res. (1987) 15:8563 !$#title Sequence of human 5-aminolevulinate synthase cDNA. !$#cross-references MUID:88040476; PMID:3671094 !$#accession A27834 !'##molecule_type mRNA !'##residues 1-42,'QPSRIVHCSSTLPQDQ',60-68,'Q',70-78, !1'LMDPSRVQMAHSFRLDSVWT',96-97,'A',99-115,'IREAAVSSAKPVLSFRR', !1133-140,'K',142-143,'G',145-169,'V',171-186,'H',188-197,'H', !1199-206,'S',208-210,'ND',213-315,'H',317-323,'V',325-337, !1'D',339-386,'V',388-391,'L',393-415,'W',417-457,'R',459-460, !1'M',462-499,'V',501-638,'K',640 ##label BAW !'##cross-references GB:Y00451; NID:g36648; PIDN:CAA68506.1; PID:g599830 GENETICS !$#gene GDB:ALAS1; ALASH !'##cross-references GDB:120543; OMIM:125290 !$#map_position 3p21.1-3p12 COMPLEX homodimer FUNCTION !$#description catalyzes the formation of 5-aminolevulinic acid from !1succinyl CoA and glycine !$#pathway porphyrin biosynthesis CLASSIFICATION #superfamily 5-aminolevulinate synthase; glycine !1C-acetyltransferase homology KEYWORDS acyltransferase; coenzyme A; homodimer; mitochondrial !1matrix; mitochondrion; phosphoprotein; porphyrin !1biosynthesis; pyridoxal phosphate FEATURE !$1-56 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$57-640 #product 5-aminolevulinate synthase 1 #status !8predicted #label MAT\ !$248-588 #domain glycine C-acetyltransferase homology #label !8GCA\ !$445 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 640 #molecular-weight 70580 #checksum 580 SEQUENCE /// ENTRY SYRTAL #type complete TITLE 5-aminolevulinate synthase (EC 2.3.1.37) precursor, nonspecific, mitochondrial - rat ALTERNATE_NAMES delta-aminolevulinate synthase, nonspecific ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 05-May-2000 ACCESSIONS A28191; A31904 REFERENCE A28191 !$#authors Srivastava, G.; Borthwick, I.A.; Maguire, D.J.; Elferink, !1C.J.; Bawden, M.J.; Mercer, J.F.B.; May, B.K. !$#journal J. Biol. Chem. (1988) 263:5202-5209 !$#title Regulation of 5-aminolevulinate synthase mRNA in different !1rat tissues. !$#cross-references MUID:88186809; PMID:3356687 !$#accession A28191 !'##molecule_type mRNA !'##residues 1-642 ##label SRI !'##cross-references GB:J03190; NID:g203067; PIDN:AAA40790.1; !1PID:g203068 REFERENCE A31904 !$#authors Yamamoto, M.; Kure, S.; Engel, J.D.; Hiraga, K. !$#journal J. Biol. Chem. (1988) 263:15973-15979 !$#title Structure, turnover, and heme-mediated suppression of the !1level of mRNA encoding rat liver delta-aminolevulinate !1synthase. !$#cross-references MUID:89034050; PMID:3182776 !$#accession A31904 !'##molecule_type mRNA !'##residues 1-117,'SQTGSSVFRKASLELQEDV',137-143,'K',145-194,'S', !1196-243,'KK',246-250,'C',252-376,'L',378-586,'F',588-642 !1##label YAM !'##cross-references GB:J04044; NID:g202859; PIDN:AAA40724.1; !1PID:g202860 COMMENT The mature functional enzyme is a dimer of identical chains !1containing pyridoxal phosphate; it catalyzes the formation !1of 5-aminolevulinic acid from succinyl CoA and glycine, the !1first and rate-limiting step in porphyrin biosynthesis. CLASSIFICATION #superfamily 5-aminolevulinate synthase; glycine !1C-acetyltransferase homology KEYWORDS acyltransferase; coenzyme A; mitochondrial matrix; !1mitochondrion; phosphoprotein; porphyrin biosynthesis; !1pyridoxal phosphate FEATURE !$1-56 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$57-642 #product 5-aminolevulinate synthase #status predicted !8#label MAT\ !$250-590 #domain glycine C-acetyltransferase homology #label !8GCA\ !$447 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 642 #molecular-weight 71128 #checksum 5277 SEQUENCE /// ENTRY SYMSAL #type fragment TITLE 5-aminolevulinate synthase (EC 2.3.1.37) precursor, erythroid-specific, mitochondrial - mouse (fragment) ALTERNATE_NAMES delta-aminolevulinate synthase, nonspecific ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 05-May-2000 ACCESSIONS A29040 REFERENCE A29040 !$#authors Schoenhaut, D.S.; Curtis, P.J. !$#journal Gene (1986) 48:55-63 !$#title Nucleotide sequence of mouse 5-aminolevulinic acid synthase !1cDNA and expression of its gene in hepatic and erythroid !1tissues. !$#cross-references MUID:87163516; PMID:3557128 !$#accession A29040 !'##molecule_type mRNA !'##residues 1-586 ##label SCH !'##cross-references GB:M15268; NID:g191857; PIDN:AAA37207.1; !1PID:g387096 REFERENCE A48183 !$#authors Ferreira, G.C.; Neame, P.J.; Dailey, H.A. !$#journal Protein Sci. (1993) 2:1959-1965 !$#title Heme biosynthesis in mammalian systems: evidence of a Schiff !1base linkage between the pyridoxal 5'-phosphate cofactor and !1a lysine residue in 5-aminolevulinate synthase. !$#cross-references MUID:94093402; PMID:8268805 !$#contents annotation; cofactor binding site COMMENT The transit peptide is removed from the nuclear-encoded !1precursor during transport into the mitochondrial matrix. !1The mature functional enzyme is a dimer of identical chains !1containing pyridoxal phosphate; it catalyzes the formation !1of 5-aminolevulinic acid from succinyl CoA and glycine, the !1first and rate-limiting step in porphyrin biosynthesis. CLASSIFICATION #superfamily 5-aminolevulinate synthase; glycine !1C-acetyltransferase homology KEYWORDS acyltransferase; coenzyme A; mitochondrial matrix; !1mitochondrion; phosphoprotein; porphyrin biosynthesis; !1pyridoxal phosphate FEATURE !$1-8 #domain transit peptide (mitochondrion) (fragment) !8#status predicted #label TRM\ !$9-586 #product 5-aminolevulinate synthase #status predicted !8#label MAT\ !$193-533 #domain glycine C-acetyltransferase homology #label !8GCA\ !$390 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status experimental SUMMARY #length 586 #checksum 3428 SEQUENCE /// ENTRY SYHUAE #type complete TITLE 5-aminolevulinate synthase (EC 2.3.1.37) precursor, erythroid-specific, mitochondrial - human ALTERNATE_NAMES 5-aminolevulinate synthase 2; erythroid delta-aminolevulinate synthase ORGANISM #formal_name Homo sapiens #common_name man DATE 21-Nov-1993 #sequence_revision 06-Sep-1996 #text_change 05-May-2000 ACCESSIONS S16347; S13683 REFERENCE S16347 !$#authors Cox, T.C.; Bawden, M.J.; Martin, A.; May, B.K. !$#journal EMBO J. (1991) 10:1891-1902 !$#title Human erythroid 5-aminolevulinate synthase: promoter !1analysis and identification of an iron-responsive element in !1the mRNA. !$#cross-references MUID:91266919; PMID:2050125 !$#accession S16347 !'##status preliminary !'##molecule_type mRNA !'##residues 1-587 ##label COX !'##cross-references EMBL:X60364; NID:g28587; PIDN:CAA42916.1; !1PID:g28588 !'##note the sequence from Fig. 4 is inconsistent with that from Fig. 2 !1in having 147-Leu REFERENCE S13682 !$#authors Bishop, D.F. !$#journal Nucleic Acids Res. (1990) 18:7187-7188 !$#title Two different genes encode delta-aminolevulinate synthase in !1humans: nucleotide sequences of cDNAs for the housekeeping !1and erythroid genes. !$#cross-references MUID:91088347; PMID:2263504 !$#accession S13683 !'##molecule_type mRNA !'##residues 6-181,'F',183-587 ##label BIS !'##cross-references EMBL:X56352; NID:g28585; PIDN:CAA39795.1; !1PID:g28586 GENETICS !$#gene GDB:ALAS2; ASB; ALASE !'##cross-references GDB:119666; OMIM:301300 !$#map_position Xp11.21-Xp11.21 !$#note defects in this gene may result in sideroblastic/hypochromic !1anemia COMPLEX homodimer FUNCTION !$#description catalyzes the formation of 5-aminolevulinic acid from !1succinyl CoA and glycine !$#pathway porphyrin biosynthesis CLASSIFICATION #superfamily 5-aminolevulinate synthase; glycine !1C-acetyltransferase homology KEYWORDS acyltransferase; coenzyme A; homodimer; mitochondrial !1matrix; mitochondrion; phosphoprotein; porphyrin !1biosynthesis; pyridoxal phosphate FEATURE !$1-49 #domain transit peptide (mitochondrion) #status !8predicted #label TRP\ !$50-587 #product 5-aminolevulinate synthase 2 #status !8predicted #label MAT\ !$194-534 #domain glycine C-acetyltransferase homology #label !8GCA\ !$391 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 587 #molecular-weight 64633 #checksum 8788 SEQUENCE /// ENTRY SYCHAL #type complete TITLE 5-aminolevulinate synthase (EC 2.3.1.37) precursor, nonspecific, mitochondrial - chicken ALTERNATE_NAMES delta-aminolevulinate synthase, nonspecific ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 05-May-2000 ACCESSIONS A23538; A23111; B31452 REFERENCE A23538 !$#authors Maguire, D.J.; Day, A.R.; Borthwick, I.A.; Srivastava, G.; !1Wigley, P.L.; May, B.K.; Elliott, W.H. !$#journal Nucleic Acids Res. (1986) 14:1379-1391 !$#title Nucleotide sequence of the chicken 5-aminolevulinate !1synthase gene. !$#cross-references MUID:86148479; PMID:3005973 !$#accession A23538 !'##molecule_type DNA !'##residues 1-635 ##label MAG !'##cross-references GB:X03517; NID:g63040; PIDN:CAA27223.1; PID:g763098 !'##experimental_source embryo liver REFERENCE A23111 !$#authors Borthwick, I.A.; Srivastava, G.; Day, A.R.; Pirola, B.A.; !1Snoswell, M.A.; May, B.K.; Elliott, W.H. !$#journal Eur. J. Biochem. (1985) 150:481-484 !$#title Complete nucleotide sequence of hepatic 5-aminolaevulinate !1synthase precursor. !$#cross-references MUID:85257679; PMID:3839458 !$#accession A23111 !'##molecule_type mRNA !'##residues 1-52,'A',54-635 ##label BOR !'##cross-references GB:X02827; GB:M24366; NID:g63607; PIDN:CAA26595.1; !1PID:g63608 !'##experimental_source embryo liver REFERENCE A31452 !$#authors Riddle, R.D.; Yamamoto, M.; Engel, J.D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:792-796 !$#title Expression of delta-aminolevulinate synthase in avian cells: !1separate genes encode erythroid-specific and nonspecific !1isozymes. !$#cross-references MUID:89128863; PMID:2915978 !$#accession B31452 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-52,'A',54-635 ##label RID !'##experimental_source liver COMMENT The mature functional enzyme is a dimer of identical chains !1containing pyridoxal phosphate; it catalyzes the formation !1of 5-aminolevulinic acid from succinyl CoA and glycine, the !1first and rate-limiting step in porphyrin biosynthesis. GENETICS !$#gene ALASN !$#introns 67/1; 136/1; 188/1; 262/2; 324/1; 384/1; 439/1; 528/3; 583/1 CLASSIFICATION #superfamily 5-aminolevulinate synthase; glycine !1C-acetyltransferase homology KEYWORDS acyltransferase; coenzyme A; liver; mitochondrial matrix; !1mitochondrion; phosphoprotein; porphyrin biosynthesis; !1pyridoxal phosphate FEATURE !$1-56 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$57-635 #product 5-aminolevulinate synthase, nonspecific !8#status predicted #label MAT\ !$243-583 #domain glycine C-acetyltransferase homology #label !8GCA\ !$440 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 635 #molecular-weight 69948 #checksum 8280 SEQUENCE /// ENTRY SYCHLE #type complete TITLE 5-aminolevulinate synthase (EC 2.3.1.37) precursor, erythroid-specific, mitochondrial - chicken ALTERNATE_NAMES delta-aminolevulinate synthase, erythroid-specific ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 05-May-2000 ACCESSIONS A31452 REFERENCE A31452 !$#authors Riddle, R.D.; Yamamoto, M.; Engel, J.D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:792-796 !$#title Expression of delta-aminolevulinate synthase in avian cells: !1separate genes encode erythroid-specific and nonspecific !1isozymes. !$#cross-references MUID:89128863; PMID:2915978 !$#accession A31452 !'##molecule_type mRNA !'##residues 1-513 ##label RID COMMENT The transit peptide is removed from the nuclear-encoded !1precursor during transport into the mitochondrial matrix. !1The mature functional enzyme is a pyridoxal phosphate !1protein and a dimer of identical chains; it catalyzes the !1formation of 5-aminolevulinic acid from succinyl CoA and !1glycine, the first and rate-limiting step in porphyrin !1biosynthesis. GENETICS !$#gene ALASE CLASSIFICATION #superfamily 5-aminolevulinate synthase; glycine !1C-acetyltransferase homology KEYWORDS acyltransferase; coenzyme A; mitochondrial matrix; !1mitochondrion; phosphoprotein; porphyrin biosynthesis; !1pyridoxal phosphate FEATURE !$1-18 #domain transit peptide (mitochondrion) #status !8predicted #label TRM\ !$19-513 #product 5-aminolevulinate synthase, !8erythroid-specific #status predicted #label MAT\ !$126-464 #domain glycine C-acetyltransferase homology #label !8GCA\ !$323 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 513 #molecular-weight 54825 #checksum 8169 SEQUENCE /// ENTRY SYBYAL #type complete TITLE 5-aminolevulinate synthase (EC 2.3.1.37) precursor, mitochondrial - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES delta-aminolevulinate synthase; protein YD9934.16; protein YDR232w ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 21-Jul-2000 ACCESSIONS A24870; A24837; S59438 REFERENCE A24870 !$#authors Urban-Grimal, D.; Volland, C.; Garnier, T.; Dehoux, P.; !1Labbe-Bois, R. !$#journal Eur. J. Biochem. (1986) 156:511-519 !$#title The nucleotide sequence of the HEM1 gene and evidence for a !1precursor form of the mitochondrial 5-aminolevulinate !1synthase in Saccharomyces cerevisiae. !$#cross-references MUID:86192482; PMID:3516694 !$#accession A24870 !'##molecule_type mRNA !'##residues 1-548 ##label URB !'##cross-references EMBL:M26329; NID:g171661; PIDN:AAA34668.1; !1PID:g171662 REFERENCE A24837 !$#authors Keng, T.; Alani, E.; Guarente, L. !$#journal Mol. Cell. Biol. (1986) 6:355-364 !$#title The nine amino-terminal residues of delta-aminolevulinate !1synthase direct beta-galactosidase into the mitochondrial !1matrix. !$#cross-references MUID:87064318; PMID:3023841 !$#accession A24837 !'##molecule_type DNA !'##residues 1-75 ##label KEN REFERENCE S59423 !$#authors Murphy, L.; Harris, D. !$#submission submitted to the EMBL Data Library, March 1995 !$#accession S59438 !'##molecule_type DNA !'##residues 1-548 ##label MUR !'##cross-references EMBL:Z48612; NID:g728671; PIDN:CAA88511.1; !1PID:g728687; GSPDB:GN00004; MIPS:YDR232w !'##experimental_source strain AB972 COMMENT This protein catalyzes the formation of 5-aminolevulinic !1acid from succinyl CoA and glycine, the first and !1rate-limiting step in porphyrin biosynthesis. GENETICS !$#gene SGD:HEM1; MIPS:YDR232w !'##cross-references SGD:S0002640; MIPS:YDR232w !$#map_position 4R !$#genome nuclear CLASSIFICATION #superfamily 5-aminolevulinate synthase; glycine !1C-acetyltransferase homology KEYWORDS acyltransferase; coenzyme A; homodimer; mitochondrion; !1phosphoprotein; porphyrin biosynthesis; pyridoxal phosphate FEATURE !$118-478 #domain glycine C-acetyltransferase homology #label !8GCA\ !$337 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 548 #molecular-weight 59362 #checksum 7792 SEQUENCE /// ENTRY SYZJAL #type complete TITLE 5-aminolevulinate synthase (EC 2.3.1.37) - Bradyrhizobium japonicum ALTERNATE_NAMES delta-aminolevulinate synthase ORGANISM #formal_name Bradyrhizobium japonicum DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 05-May-2000 ACCESSIONS A27478 REFERENCE A27478 !$#authors McClung, C.R.; Somerville, J.E.; Guerinot, M.L.; Chelm, B.K. !$#journal Gene (1987) 54:133-139 !$#title Structure of the Bradyrhizobium japonicum gene hemA encoding !15-aminolevulinic acid synthase. !$#cross-references MUID:87277426; PMID:3609750 !$#accession A27478 !'##molecule_type DNA !'##residues 1-409 ##label MCC !'##cross-references GB:M16751; NID:g152096; PIDN:AAA26216.1; !1PID:g152097 COMMENT This pyridoxal phosphate enzyme catalyzes the formation of !15-aminolevulinic acid from succinyl CoA and glycine, the !1first and rate-limiting step in porphyrin biosynthesis. GENETICS !$#gene hemA CLASSIFICATION #superfamily 5-aminolevulinate synthase; glycine !1C-acetyltransferase homology KEYWORDS acyltransferase; coenzyme A; phosphoprotein; porphyrin !1biosynthesis; pyridoxal phosphate FEATURE !$50-388 #domain glycine C-acetyltransferase homology #label !8GCA\ !$247 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 409 #molecular-weight 44602 #checksum 3018 SEQUENCE /// ENTRY A49845 #type complete TITLE 5-aminolevulinate synthase (EC 2.3.1.37) HemT - Rhodobacter sphaeroides ORGANISM #formal_name Rhodobacter sphaeroides DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 05-May-2000 ACCESSIONS A49845 REFERENCE A49845 !$#authors Neidle, E.L.; Kaplan, S. !$#journal J. Bacteriol. (1993) 175:2292-2303 !$#title Expression of the Rhodobacter sphaeroides hemA and hemT !1genes, encoding two 5-aminolevulinic acid synthase isozymes. !$#cross-references MUID:93224451; PMID:8468290 !$#contents 2.4.1 !$#accession A49845 !'##molecule_type DNA !'##residues 1-407 ##label NEI !'##cross-references GB:L07489; NID:g151938; PIDN:AAA26124.1; !1PID:g151939 !'##note sequence extracted from NCBI backbone (NCBIN:129176, !1NCBIP:129177) CLASSIFICATION #superfamily 5-aminolevulinate synthase; glycine !1C-acetyltransferase homology KEYWORDS acyltransferase; coenzyme A; phosphoprotein; pyridoxal !1phosphate FEATURE !$51-389 #domain glycine C-acetyltransferase homology #label !8GCA\ !$248 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 407 #molecular-weight 44332 #checksum 6701 SEQUENCE /// ENTRY S10528 #type complete TITLE 5-aminolevulinate synthase (EC 2.3.1.37) - Rhodobacter capsulatus ORGANISM #formal_name Rhodobacter capsulatus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S10528; S16149; S16880 REFERENCE S10528 !$#authors Hornberger, U.; Liebetanz, R.; Tichy, H.V.; Drews, G. !$#journal Mol. Gen. Genet. (1990) 221:371-378 !$#title Cloning and sequencing of the hemA gene of Rhodobacter !1capsulatus and isolation of a delta-aminolevulinic !1acid-dependent mutant strain. !$#cross-references MUID:90340288; PMID:2381418 !$#accession S10528 !'##molecule_type DNA !'##residues 1-401 ##label HOR !'##cross-references EMBL:X53309; NID:g46028; PIDN:CAA37393.1; !1PID:g46029 REFERENCE S16149 !$#authors Wright, M.S.; Eckert, J.J.; Biel, S.W.; Biel, A.J. !$#journal FEMS Microbiol. Lett. (1991) 78:339-342 !$#title Use of a lacZ fusion to study transcriptional regulation of !1the Rhodobacter capsulatus hemA gene. !$#accession S16149 !'##molecule_type DNA !'##residues 1-401 ##label WRI !'##cross-references EMBL:X53864; NID:g974201; PIDN:CAA37857.1; !1PID:g974202 REFERENCE S16880 !$#authors Eckert, J.J. !$#submission submitted to the EMBL Data Library, July 1990 !$#accession S16880 !'##molecule_type DNA !'##residues 1-30,'A',32-127,'V',129-285,'LARRPRSR',294 ##label ECK !'##cross-references EMBL:X53864 CLASSIFICATION #superfamily 5-aminolevulinate synthase; glycine !1C-acetyltransferase homology KEYWORDS acyltransferase; coenzyme A; phosphoprotein; pyridoxal !1phosphate FEATURE !$51-391 #domain glycine C-acetyltransferase homology #label !8GCA\ !$248 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 401 #molecular-weight 43575 #checksum 1242 SEQUENCE /// ENTRY SYECKP #type complete TITLE 8-amino-7-oxononanoate synthase (EC 2.3.1.47) bioF [similarity] - Escherichia coli (strain K-12) ALTERNATE_NAMES 7-KAP synthetase; 7-keto-8-amino pelargonic acid synthetase ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 01-Mar-2002 ACCESSIONS D32025; H64813 REFERENCE A32025 !$#authors Otsuka, A.J.; Buoncristiani, M.R.; Howard, P.K.; Flamm, J.; !1Johnson, C.; Yamamoto, R.; Uchida, K.; Cook, C.; Ruppert, !1J.; Matsuzaki, J. !$#journal J. Biol. Chem. (1988) 263:19577-19585 !$#title The Escherichia coli biotin biosynthetic enzyme sequences !1predicted from the nucleotide sequence of the bio operon. !$#cross-references MUID:89066784; PMID:3058702 !$#accession D32025 !'##molecule_type DNA !'##residues 1-384 ##label OTS !'##cross-references GB:J04423; NID:g145422; PIDN:AAA23516.1; !1PID:g145426 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64813 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-384 ##label BLAT !'##cross-references GB:AE000180; GB:U00096; NID:g1786988; !1PIDN:AAC73863.1; PID:g1786993; UWGP:b0776 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene bioF !$#map_position 17 min CLASSIFICATION #superfamily 5-aminolevulinate synthase; glycine !1C-acetyltransferase homology KEYWORDS acyltransferase; biotin biosynthesis; coenzyme A; !1phosphoprotein; pyridoxal phosphate FEATURE !$44-378 #domain glycine C-acetyltransferase homology #label !8GCA\ !$236 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 384 #molecular-weight 41594 #checksum 733 SEQUENCE /// ENTRY XUECGA #type complete TITLE glycine C-acetyltransferase (EC 2.3.1.29) - Escherichia coli (strain K-12) ALTERNATE_NAMES 2-amino-3-ketobutyrate CoA ligase ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS C65162; S00913; S47838; A29474; S07529 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65162 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-398 ##label BLAT !'##cross-references GB:AE000439; GB:U00096; NID:g1790036; !1PIDN:AAC76641.1; PID:g1790046; UWGP:b3617 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S00913 !$#authors Aronson, B.D.; Ravnikar, P.D.; Somerville, R.L. !$#journal Nucleic Acids Res. (1988) 16:3586 !$#title Nucleotide sequence of the 2-amino-3-ketobutyrate coenzyme A !1ligase (kbl) gene of E. coli. !$#cross-references MUID:88233955; PMID:3287333 !$#accession S00913 !'##molecule_type DNA !'##residues 1-42,'Q',44-170,'R',172-182,'L',184-398 ##label ARO !'##cross-references GB:X06690; NID:g41862; PIDN:CAA29883.1; PID:g41863 REFERENCE S47666 !$#authors Plunkett, G. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S47838 !'##molecule_type DNA !'##residues 1-398 ##label PLU !'##cross-references EMBL:U00039; NID:g466582; PIDN:AAB18594.1; !1PID:g466755 REFERENCE A29474 !$#authors Mukherjee, J.J.; Dekker, E.E. !$#journal J. Biol. Chem. (1987) 262:14441-14447 !$#title Purification, properties, and N-terminal amino acid sequence !1of homogeneous Escherichia coli 2-amino-3-ketobutyrate CoA !1ligase, a pyridoxal phosphate-dependent enzyme. !$#cross-references MUID:88032988; PMID:3117785 !$#accession A29474 !'##molecule_type DNA !'##residues 1-21 ##label MUK REFERENCE S07529 !$#authors Mukherjee, J.J.; Dekker, E.E. !$#journal Biochim. Biophys. Acta (1990) 1037:24-29 !$#title 2-Amino-3-ketobutyrate CoA ligase of Escherichia coli: !1stoichiometry of pyridoxal phosphate binding and location of !1the pyridoxyllysine peptide in the primary structure of the !1enzyme. !$#cross-references MUID:90105507; PMID:2104756 !$#accession S07529 !'##molecule_type protein !'##residues 235-257 ##label MU2 GENETICS !$#gene kbl !$#map_position 81 min CLASSIFICATION #superfamily 5-aminolevulinate synthase; glycine !1C-acetyltransferase homology KEYWORDS acyltransferase; coenzyme A; phosphoprotein; pyridoxal !1phosphate FEATURE !$47-385 #domain glycine C-acetyltransferase homology #label !8GCA\ !$244 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status experimental SUMMARY #length 398 #molecular-weight 43117 #checksum 1293 SEQUENCE /// ENTRY JQ0512 #type complete TITLE 8-amino-7-oxononanoate synthase (EC 2.3.1.47) - Bacillus sphaericus ALTERNATE_NAMES 7-KAP synthetase 7-keto-8-amino pelargonic acid synthetase ORGANISM #formal_name Bacillus sphaericus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-May-2000 ACCESSIONS JQ0512; S21284 REFERENCE JQ0506 !$#authors Gloeckler, R.; Ohsawa, I.; Speck, D.; Ledoux, C.; Bernard, !1S.; Zinsius, M.; Villeval, D.; Kisou, T.; Kamogawa, K.; !1Lemoine, Y. !$#journal Gene (1990) 87:63-70 !$#title Cloning and characterization of the Bacillus sphaericus !1genes controlling the bioconversion of pimelate into !1dethiobiotin. !$#cross-references MUID:90236299; PMID:2110099 !$#accession JQ0512 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-389 ##label GLO !'##cross-references GB:M29291; NID:g142592; PIDN:AAA22271.1; !1PID:g142595 !'##experimental_source strain IFO3525 REFERENCE S21284 !$#authors Ploux, O.; Marquet, A. !$#journal Biochem. J. (1992) 283:327-331 !$#title The 8-amino-7-oxopelargonate synthase from Bacillus !1sphaericus. Purification and preliminary characterization of !1the cloned enzyme overproduced in Escherichia coli. !$#cross-references MUID:92246854; PMID:1575677 !$#accession S21284 !'##status preliminary !'##molecule_type protein !'##residues 1-14 ##label PLO GENETICS !$#gene bioF FUNCTION !$#description catalyzes the condensation of pimelyl-CoA and L-alanine to !1form 8-amino-7-oxononanoate synthase CLASSIFICATION #superfamily 5-aminolevulinate synthase; glycine !1C-acetyltransferase homology KEYWORDS acyltransferase; biotin biosynthesis; coenzyme A; !1phosphoprotein; pyridoxal phosphate FEATURE !$42-377 #domain glycine C-acetyltransferase homology #label !8GCA\ !$237 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 389 #molecular-weight 42530 #checksum 437 SEQUENCE /// ENTRY BVECHA #type complete TITLE glutamyl-tRNA reductase (EC 1.2.1.-) - Escherichia coli (strain K-12) ALTERNATE_NAMES hemA protein ORGANISM #formal_name Escherichia coli #variety strain K-12 DATE 30-Jun-1990 #sequence_revision 10-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS A45918; G64867; I83568; JQ0089; PC1179; S04414 REFERENCE A45918 !$#authors Verkamp, E.; Chelm, B.K. !$#journal J. Bacteriol. (1989) 171:4728-4735 !$#title Isolation, nucleotide sequence, and preliminary !1characterization of the Escherichia coli K-12 hemA gene. !$#cross-references MUID:89359103; PMID:2548996 !$#accession A45918 !'##molecule_type DNA !'##residues 1-418 ##label VER !'##cross-references GB:M25323; NID:g146331; PIDN:AAA23954.1; !1PID:g146333 !'##experimental_source strain K-12 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64867 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-418 ##label BLAT !'##cross-references GB:AE000219; GB:U00096; NID:g1787453; !1PIDN:AAC74294.1; PID:g1787461; UWGP:b1210 !'##experimental_source strain K-12, substrain MG1655 REFERENCE I60364 !$#authors Strohmaier, H.; Remler, P.; Renner, W.; Hogenauer, G. !$#journal J. Bacteriol. (1995) 177:4488-4500 !$#title Expression of genes kdsA and kdsB involved in !13-deoxy-D-manno-octulosonic acid metabolism and biosynthesis !1of enterobacterial lipopolysaccharide is growth phase !1regulated primarily at the transcriptional level in !1Escherichia coli K-12. !$#cross-references MUID:95362678; PMID:7543480 !$#accession I83568 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-242,'R',244-418 ##label STR !'##cross-references EMBL:U18555; NID:g968925; PIDN:AAC43436.1; !1PID:g968929 !'##experimental_source strain K-12 REFERENCE JQ0089 !$#authors Li, J.M.; Russell, C.S.; Cosloy, S.D. !$#journal Gene (1989) 82:209-217 !$#title Cloning and structure of the hemA gene of Escherichia coli !1K-12. !$#cross-references MUID:90060810; PMID:2684779 !$#accession JQ0089 !'##molecule_type DNA !'##residues 1-242,'R',244-418 ##label LIJ !'##cross-references GB:M30785; NID:g146329; PIDN:AAA23953.1; !1PID:g146330 !'##experimental_source strain K-12 !'##note misidentified as delta-aminolevulinate synthase (EC 2.3.1.37) !1in GenBank REFERENCE JC1381 !$#authors Ikemi, M.; Murakami, K.; Hashimoto, M.; Murooka, Y. !$#journal Gene (1992) 121:127-132 !$#title Cloning and characterization of genes involved in the !1biosynthesis of delta-aminolevulinic acid in Escherichia !1coli. !$#cross-references MUID:93051347; PMID:1427085 !$#accession PC1179 !'##molecule_type DNA !'##residues 1-48 ##label IKE !'##cross-references DDBJ:D10264; NID:g216522; PID:g2160233 REFERENCE S04414 !$#authors Drolet, M.; Peloquin, L.; Echelard, Y.; Cousineau, L.; !1Sasarman, A. !$#journal Mol. Gen. Genet. (1989) 216:347-352 !$#title Isolation and nucleotide sequence of the hemA gene of !1Escherichia coli K12. !$#cross-references MUID:89313673; PMID:2664455 !$#accession S04414 !'##molecule_type DNA !'##residues 1-150,'PFALKQISVPALCLSLLP',169-171,'V',173-239,'M',241-332, !1'N',334-364,'R',366-418 ##label DRO !'##cross-references GB:X17434; NID:g41659; PIDN:CAA35476.1; PID:g41660 GENETICS !$#gene hemA !$#map_position 27 min FUNCTION !$#description catalyzes reduction of glutamyl-tRNA(Glu) by NADPH to !1glutamic acid 1-semialdehyde and tRNA(Glu) !$#pathway aminolevulinate biosynthesis; porphyrin biosynthesis CLASSIFICATION #superfamily glutamyl-tRNA reductase KEYWORDS aminolevulinate biosynthesis; NADP; oxidoreductase; !1porphyrin biosynthesis SUMMARY #length 418 #molecular-weight 46306 #checksum 2394 SEQUENCE /// ENTRY BVEBHA #type complete TITLE glutamyl-tRNA reductase (EC 1.2.1.-) - Salmonella typhimurium ALTERNATE_NAMES hemA protein ORGANISM #formal_name Salmonella typhimurium DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 10-Oct-1997 ACCESSIONS A32661 REFERENCE A32661 !$#authors Elliott, T. !$#journal J. Bacteriol. (1989) 171:3948-3960 !$#title Cloning, genetic characterization, and nucleotide sequence !1of the hemA-prfA operon of Salmonella typhimurium. !$#cross-references MUID:89291746; PMID:2544564 !$#accession A32661 !'##molecule_type DNA !'##residues 1-418 ##label ELL GENETICS !$#gene hemA !$#map_position 34 min FUNCTION !$#description catalyzes the reduction of glutamyl-tRNA(GLU) by NADPH to !1glutamic acid 1-semialdehyde and tRNA(GLU) !$#pathway aminolevulinate biosynthesis; porphyrin biosynthesis CLASSIFICATION #superfamily glutamyl-tRNA reductase KEYWORDS aminolevulinate biosynthesis; NADP; oxidoreductase; !1porphyrin biosynthesis SUMMARY #length 418 #molecular-weight 46105 #checksum 2126 SEQUENCE /// ENTRY S77180 #type complete TITLE glutamyl-tRNA reductase (EC 1.2.1.-) - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES hemA protein; protein slr1808; transfer RNA-Gln reductase ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 25-Apr-1997 #sequence_revision 25-Apr-1997 #text_change 16-Jun-2000 ACCESSIONS S77180; A38087; S37660 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S77180 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-463 ##label KAN !'##cross-references EMBL:D90908; GB:AB001339; NID:g1652725; !1PIDN:BAA17738.1; PID:g1652819 !'##note protein slr1808 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 REFERENCE A38087 !$#authors Verkamp, E.; Jahn, M.; Jahn, D.; Kumar, A.M.; Soell, D. !$#journal J. Biol. Chem. (1992) 267:8275-8280 !$#title Glutamyl-tRNA reductase from Escherichia coli and !1Synechocystis 6803. Gene structure and expression. !$#cross-references MUID:92235044; PMID:1569081 !$#accession A38087 !'##molecule_type DNA !'##residues 37-463 ##label VER !'##cross-references GB:M84218; NID:g154469; PIDN:AAA27289.1; !1PID:g154470 REFERENCE S37660 !$#authors Grimm, B. !$#journal Hereditas (1992) 117:195-197 !$#title Identification of a hemA gene from Synechocystis by !1complementation of an E. coli hemA mutant. !$#cross-references MUID:93093989; PMID:1459859 !$#accession S37660 !'##status preliminary !'##molecule_type DNA !'##residues 37-463 ##label GRI !'##cross-references EMBL:X65963; NID:g288421; PIDN:CAA46779.1; !1PID:g288422 GENETICS !$#gene hemA !$#start_codon GTG FUNCTION !$#description catalyzes the reduction of glutamyl-tRNA(Glu) by NADPH to !1glutamic acid 1-semialdehyde and tRNA(Glu) !$#pathway aminolevulinate biosynthesis; porphyrin biosynthesis CLASSIFICATION #superfamily glutamyl-tRNA reductase KEYWORDS aminolevulinate biosynthesis; NADP; oxidoreductase; !1porphyrin biosynthesis SUMMARY #length 463 #molecular-weight 51469 #checksum 8544 SEQUENCE /// ENTRY A35252 #type complete TITLE glutamyl-tRNA reductase (EC 1.2.1.-) hemA - Bacillus subtilis ALTERNATE_NAMES hemA protein ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A35252; C69639 REFERENCE A35252 !$#authors Petricek, M.; Rutberg, L.; Schroeder, I.; Hederstedt, L. !$#journal J. Bacteriol. (1990) 172:2250-2258 !$#title Cloning and characterization of the hemA region of the !1Bacillus subtilis chromosome. !$#cross-references MUID:90236876; PMID:2110138 !$#accession A35252 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-455 ##label PET !'##cross-references GB:M57676; GB:M32130; NID:g143034; PIDN:AAA22510.1; !1PID:g143035 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69639 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-455 ##label KUN !'##cross-references GB:Z99118; GB:AL009126; NID:g2635200; !1PIDN:CAB14777.1; PID:g2635282 !'##experimental_source strain 168 GENETICS !$#gene hemA CLASSIFICATION #superfamily glutamyl-tRNA reductase KEYWORDS aminolevulinate biosynthesis; NADP; oxidoreductase; !1porphyrin biosynthesis SUMMARY #length 455 #molecular-weight 50843 #checksum 7749 SEQUENCE /// ENTRY S51136 #type complete TITLE glutamyl-tRNA reductase (EC 1.2.1.-) - Methanobacterium thermoautotrophicum (strain Marburg) ALTERNATE_NAMES hemA protein ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S51136 REFERENCE S51136 !$#authors Hungerer, C.; Weiss, D.; Thauer, R.K.; Jahn, D. !$#submission submitted to the EMBL Data Library, January 1995 !$#description Cloning and characterization of the Methanobacterium !1thermoautotrophicum hemA gene encoding glutamyl-tRNA !1reductase. !$#accession S51136 !'##status preliminary !'##molecule_type DNA !'##residues 1-398 ##label HUN !'##cross-references EMBL:X83691; NID:g624029; PIDN:CAA58664.1; !1PID:g809718 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily glutamyl-tRNA reductase KEYWORDS aminolevulinate biosynthesis; NADP; oxidoreductase; !1porphyrin biosynthesis SUMMARY #length 398 #molecular-weight 44536 #checksum 2550 SEQUENCE /// ENTRY A48359 #type complete TITLE glutamyl-tRNA reductase (EC 1.2.1.-) HemA - Chlorobium vibrioforme ORGANISM #formal_name Chlorobium vibrioforme DATE 19-Nov-1993 #sequence_revision 18-Nov-1994 #text_change 10-Oct-1997 ACCESSIONS A48359; S27546 REFERENCE A48359 !$#authors Majumdar, D.; Avissar, Y.J.; Wyche, J.H.; Beale, S.I. !$#journal Arch. Microbiol. (1991) 156:281-289 !$#title Structure and expression of the Chlorobium vibrioforme hemA !1gene. !$#cross-references MUID:92171712; PMID:1793335 !$#accession A48359 !'##molecule_type DNA !'##residues 1-415 ##label MAJ !'##cross-references EMBL:M59194; NID:g144474; PID:g144475 !'##note submitted to the EMBL Data Library, July 1991 !'##note sequence extracted from NCBI backbone (NCBIN:86184, !1NCBIP:86186) FUNCTION !$#description catalyzes the reduction of glutamyl-tRNA(GLU) by NADPH to !1glutamic acid 1-semialdehyde and tRNA(GLU) !$#pathway aminolevulinate biosynthesis; porphyrin biosynthesis CLASSIFICATION #superfamily glutamyl-tRNA reductase KEYWORDS aminolevulinate biosynthesis; NADP; oxidoreductase; !1porphyrin biosynthesis SUMMARY #length 415 #molecular-weight 46226 #checksum 532 SEQUENCE /// ENTRY B41856 #type complete TITLE [acyl-carrier-protein] S-malonyltransferase (EC 2.3.1.39) fabD [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 04-Mar-1993 #sequence_revision 13-Jan-1995 #text_change 01-Mar-2002 ACCESSIONS B41856; A42147; S20443; A64853 REFERENCE A41856 !$#authors Verwoert, I.I.; Verbree, E.C.; van der Linden, K.H.; !1Nijkamp, H.J.; Stuitje, A.R. !$#journal J. Bacteriol. (1992) 174:2851-2857 !$#title Cloning, nucleotide sequence, and expression of the !1Escherichia coli fabD gene, encoding malonyl coenzyme A-acyl !1carrier protein transacylase. !$#cross-references MUID:92234941; PMID:1314802 !$#accession B41856 !'##molecule_type DNA !'##residues 1-309 ##label VER !'##cross-references GB:M87040; NID:g145885; PIDN:AAA23742.1; !1PID:g145887 !'##note sequence extracted from NCBI backbone (NCBIN:97135, !1NCBIP:97148) REFERENCE A42147 !$#authors Rawlings, M.; Cronan Jr., J.E. !$#journal J. Biol. Chem. (1992) 267:5751-5754 !$#title The gene encoding Escherichia coli acyl carrier protein lies !1within a cluster of fatty acid biosynthetic genes. !$#cross-references MUID:92210530; PMID:1556094 !$#accession A42147 !'##molecule_type DNA !'##residues 289-309 ##label RAW !'##cross-references GB:M84991; NID:g145879; PIDN:AAA23738.1; !1PID:g145880 REFERENCE S20443 !$#authors Magnuson, K.; Oh, W.; Larson, T.J.; Cronan Jr., J.E. !$#journal FEBS Lett. (1992) 299:262-266 !$#title Cloning and nucleotide sequence of the fabD gene encoding !1malonyl coenzyme A-acyl carrier protein transacylase of !1Escherichia coli. !$#cross-references MUID:92183950; PMID:1339356 !$#accession S20443 !'##molecule_type DNA !'##residues 1-309 ##label MAG !'##cross-references EMBL:Z11565; NID:g41363; PIDN:CAA77658.1; !1PID:g41364 !'##experimental_source strain K-12 !'##note amino end of the mature protein confirmed by protein sequencing REFERENCE A55383 !$#authors Ruch, F.E.; Vagelos, P.R. !$#journal J. Biol. Chem. (1973) 248:8095-8106 !$#title Characterization of a malonyl-enzyme intermediate and !1identification of the malonyl binding site in malonyl !1coenzyme A-acyl carrier protein transacylase of Escherichia !1coli. !$#cross-references MUID:74030718; PMID:4584823 !$#contents annotation; active site REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64853 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-309 ##label BLAT !'##cross-references GB:AE000210; GB:U00096; NID:g1787332; !1PIDN:AAC74176.1; PID:g1787334; UWGP:b1092 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene fabD; tfpA !$#map_position 24 min FUNCTION !$#description catalyzes the reaction of malonyl-CoA with acyl carrier !1protein to form malonyl-acyl carrier protein and coenzyme A !$#pathway fatty acid biosynthesis CLASSIFICATION #superfamily [acyl-carrier-protein] S-malonyltransferase; !1[acyl-carrier-protein] S-malonyltransferase homology KEYWORDS acyltransferase; coenzyme A; fatty acid biosynthesis FEATURE !$2-309 #product [acyl-carrier-protein] S-malonyltransferase !8#status experimental #label MAT\ !$5-289 #domain [acyl-carrier-protein] S-malonyltransferase !8homology #label AMT\ !$92 #active_site Ser (covalent substrate-binding) #status !8experimental\ !$201 #active_site His #status predicted SUMMARY #length 309 #molecular-weight 32417 #checksum 6198 SEQUENCE /// ENTRY SYECA1 #type complete TITLE 3-oxoacyl-[acyl-carrier-protein] synthase (EC 2.3.1.41) I - Escherichia coli (strain K-12) ALTERNATE_NAMES acetoacetyl-ACP synthase I; beta-ketoacyl-ACP synthase I ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 01-Mar-2002 ACCESSIONS A31284; A65005 REFERENCE A31284 !$#authors Kauppinen, S.; Siggaard-Andersen, M.; von Wettstein-Knowles, !1P. !$#journal Carlsberg Res. Commun. (1988) 53:357-370 !$#title Beta-ketoacyl-ACP synthase I of Escherichia coli: nucleotide !1sequence of the fabB gene and identification of the !1cerulenin binding residue. !$#cross-references MUID:89351280; PMID:3076376 !$#accession A31284 !'##molecule_type DNA !'##residues 1-406 ##label KAU !'##cross-references GB:M24427; NID:g3776599; PIDN:AAC67304.1; !1PID:g145884 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65005 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-406 ##label BLAT !'##cross-references GB:AE000321; GB:U00096; NID:g1788659; !1PIDN:AAC75383.1; PID:g1788663; UWGP:b2323 !'##experimental_source strain K-12, substrain MG1655 COMMENT This is one of three enzymes that catalyze the condensation !1of a two-carbon unit to a growing fatty acid chain; it is !1specific for elongation from C-10 to unsaturated C-16 and !1C-18 fatty acids. GENETICS !$#gene fabB !$#map_position 50 min CLASSIFICATION #superfamily 3-oxoacyl-[acyl-carrier-protein] synthase I; !13-oxoacyl-[acyl-carrier-protein] synthase I homology KEYWORDS acyltransferase; fatty acid biosynthesis FEATURE !$22-401 #domain 3-oxoacyl-[acyl-carrier-protein] synthase I !8homology #label OAS SUMMARY #length 406 #molecular-weight 42613 #checksum 5295 SEQUENCE /// ENTRY A39356 #type complete TITLE 3-oxoacyl-[acyl-carrier-protein] synthase (EC 2.3.1.41) I beta chain precursor, chloroplast - barley ALTERNATE_NAMES beta-ketoacyl-[acyl carrier protein] synthase I ORGANISM #formal_name Hordeum vulgare #common_name barley DATE 06-Mar-1992 #sequence_revision 13-Jan-1995 #text_change 11-Jun-1999 ACCESSIONS A39356; A45129 REFERENCE A39356 !$#authors Siggaard-Andersen, M.; Kauppinen, S.; von Wettstein-Knowles, !1P. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:4114-4118 !$#title Primary structure of a cerulenin-binding beta-ketoacyl-[acyl !1carrier protein] synthase from barley chloroplasts. !$#cross-references MUID:91239517; PMID:2034657 !$#accession A39356 !'##molecule_type mRNA !'##residues 1-462 ##label SIG !'##cross-references GB:M60410; NID:g167064; PIDN:AAA32968.1; !1PID:g167065 !'##experimental_source cv. Bonus, leaf !'##note parts of this sequence, including the amino end of the mature !1protein, were confirmed by protein sequencing REFERENCE A45129 !$#authors Kauppinen, S. !$#journal J. Biol. Chem. (1992) 267:23999-24006 !$#title Structure and expression of the Kas12 gene encoding a !1beta-ketoacyl-acyl carrier protein synthase I isozyme from !1barley. !$#cross-references MUID:93054767; PMID:1429736 !$#accession A45129 !'##molecule_type DNA !'##residues 1-395,397-414,'T',415-462 ##label KAU !'##experimental_source cv. Bonus !'##note sequence inconsistent with the nucleotide translation; !1translation agrees with sequence in reference A39356 !'##note sequence extracted from NCBI backbone (NCBIP:118934) GENETICS !$#gene Kas12 !$#map_position 2 !$#introns 144/3; 288/3; 346/3; 384/3; 418/3; 441/1 COMPLEX homodimer or heterodimer with alpha chain CLASSIFICATION #superfamily 3-oxoacyl-[acyl-carrier-protein] synthase I; !13-oxoacyl-[acyl-carrier-protein] synthase I homology KEYWORDS acyltransferase; chloroplast; fatty acid biosynthesis; !1heterodimer; homodimer FEATURE !$1-36 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$36-462 #product 3-oxoacyl-[acyl-carrier-protein] synthase I !8beta chain #status experimental #label MAT\ !$68-457 #domain 3-oxoacyl-[acyl-carrier-protein] synthase I !8homology #label OAS\ !$213 #active_site Cys #status experimental SUMMARY #length 462 #molecular-weight 49015 #checksum 9221 SEQUENCE /// ENTRY S47076 #type complete TITLE 3-oxoacyl-[acyl-carrier-protein] synthase (EC 2.3.1.41) precursor [similarity] - barley ORGANISM #formal_name Hordeum vulgare #common_name barley DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 23-Mar-2001 ACCESSIONS S47076 REFERENCE S47075 !$#authors Wissenbach, M. !$#submission submitted to the EMBL Data Library, June 1994 !$#description New members of the barley beta-ketoacyl-ACP synthase (KAS) !1gene family. !$#accession S47076 !'##molecule_type mRNA !'##residues 1-489 ##label WIS !'##cross-references EMBL:Z34269; NID:g498741; PIDN:CAA84023.1; !1PID:g498742 CLASSIFICATION #superfamily 3-oxoacyl-[acyl-carrier-protein] synthase I; !13-oxoacyl-[acyl-carrier-protein] synthase I homology KEYWORDS acyltransferase FEATURE !$99-486 #domain 3-oxoacyl-[acyl-carrier-protein] synthase I !8homology #label OAS SUMMARY #length 489 #molecular-weight 52376 #checksum 7027 SEQUENCE /// ENTRY S47074 #type complete TITLE 3-oxoacyl-[acyl-carrier-protein] synthase (EC 2.3.1.41) precursor [similarity] - barley ORGANISM #formal_name Hordeum vulgare #common_name barley DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 05-May-2000 ACCESSIONS S47074; S47075; S47092 REFERENCE S47074 !$#authors Wissenbach, M. !$#submission submitted to the EMBL Data Library, June 1994 !$#description New members of the barley Kas gene family encoding !1beta-ketoacyl-acyl carrier protein (ACP) synthases (KASes). !$#accession S47074 !'##molecule_type mRNA !'##residues 1-495 ##label WIS !'##cross-references EMBL:Z34268; NID:g498739; PIDN:CAA84022.1; !1PID:g498740 !$#accession S47075 !'##molecule_type mRNA !'##residues 1-416 ##label WI2 !'##cross-references EMBL:Z34266 !$#accession S47092 !'##molecule_type mRNA !'##residues 103-495 ##label WI3 !'##cross-references EMBL:Z34267 CLASSIFICATION #superfamily 3-oxoacyl-[acyl-carrier-protein] synthase I; !13-oxoacyl-[acyl-carrier-protein] synthase I homology KEYWORDS acyltransferase FEATURE !$104-491 #domain 3-oxoacyl-[acyl-carrier-protein] synthase I !8homology #label OAS SUMMARY #length 495 #molecular-weight 53126 #checksum 4274 SEQUENCE /// ENTRY B24706 #type complete TITLE nodulation protein nodE - Rhizobium meliloti plasmid ALTERNATE_NAMES hsnB protein ORGANISM #formal_name Rhizobium meliloti DATE 30-Jun-1988 #sequence_revision 13-Jan-1995 #text_change 11-Jun-1999 ACCESSIONS B24706; S07674; B24193 REFERENCE A93638 !$#authors Debelle, F.; Sharma, S.B. !$#journal Nucleic Acids Res. (1986) 14:7453-7472 !$#title Nucleotide sequence of Rhizobium meliloti RCR2011 genes !1involved in host specificity of nodulation. !$#cross-references MUID:87016382; PMID:3020515 !$#accession B24706 !'##molecule_type DNA !'##residues 1-402 ##label DEB !'##cross-references EMBL:X04379; NID:g46305; PIDN:CAA27961.1; !1PID:g46307 !'##experimental_source strain RCR2011 symbiotic plasmid REFERENCE S06395 !$#authors Fisher, R.F.; Swanson, J.A.; Mulligan, J.T.; Long, S.R. !$#journal Genetics (1987) 117:191-201 !$#title Extended region of nodulation genes in Rhizobium meliloti !11021. II. Nucleotide sequence, transcription start sites and !1protein products. !$#accession S07674 !'##molecule_type DNA !'##residues 1-402 ##label FIS !'##cross-references EMBL:Y00604; NID:g46301; PIDN:CAA68648.1; !1PID:g46303 !'##experimental_source strain 1021 REFERENCE A94655 !$#authors Horvath, B.; Kondorosi, E.; John, M.; Schmidt, J.; Toeroek, !1I.; Gyoergypal, Z.; Barabas, I.; Wieneke, U.; Schell, J.; !1Kondorosi, A. !$#journal Cell (1986) 46:335-343 !$#title Organization, structure and symbiotic function of Rhizobium !1meliloti nodulation genes determining host specificity for !1alfalfa. !$#cross-references MUID:86272081; PMID:3731273 !$#accession B24193 !'##molecule_type DNA !'##residues 1-26,'SARR',31-36,'V',38-52,'I',54-118,'PS',121,'ST', !1124-125,127-402 ##label HOR !'##cross-references GB:M14052; NID:g152239; PIDN:AAA26289.1; !1PID:g152241 !'##experimental_source strain AK631 (a variant of strain 41) !'##note authors translated the codon GCC for residue 216 as Asn COMMENT This is one of several proteins that control host !1specificity of root hair infection and nodulation. GENETICS !$#gene nodE; hsnB !$#genome plasmid CLASSIFICATION #superfamily 3-oxoacyl-[acyl-carrier-protein] synthase I; !13-oxoacyl-[acyl-carrier-protein] synthase I homology KEYWORDS host range; membrane protein; nodulation FEATURE !$2-402 #product nodulation protein nodE #status predicted !8#label MAT\ !$23-399 #domain 3-oxoacyl-[acyl-carrier-protein] synthase I !8homology #label OAS SUMMARY #length 402 #molecular-weight 41826 #checksum 5806 SEQUENCE /// ENTRY B25095 #type complete TITLE nodulation protein nodE - Rhizobium leguminosarum bv. viciae plasmid RL1JI ORGANISM #formal_name Rhizobium leguminosarum bv. viciae DATE 05-Oct-1988 #sequence_revision 13-Jan-1995 #text_change 11-Jun-1999 ACCESSIONS B25095; S02059 REFERENCE A25095 !$#authors Shearman, C.A.; Rossen, L.; Johnston, A.W.B.; Downie, J.A. !$#journal EMBO J. (1986) 5:647-652 !$#title The Rhizobium leguminosarum nodulation gene nodF encodes a !1polypeptide similar to acyl-carrier protein and is regulated !1by nodD plus a factor in pea root exudate. !$#accession B25095 !'##molecule_type DNA !'##residues 1-26,'NARRP',32-403 ##label SHE !'##cross-references EMBL:Y00548 !'##experimental_source symbiotic plasmid RL1JI REFERENCE S06020 !$#authors Spaink, H.P.; Weinman, J.; Djordjevic, M.A.; Wijffelman, !1C.A.; Okker, R.J.H.; Lugtenberg, B.J.J. !$#journal EMBO J. (1989) 8:2811-2818 !$#title Genetic analysis and cellular localization of the Rhizobium !1host specificity-determining NodE protein. !$#cross-references MUID:90059862; PMID:2684629 !$#contents annotation; revision to residues 27-31 !$#note extent of resequencing by these authors was not indicated REFERENCE S02059 !$#authors Downie, J.A. !$#submission submitted to the EMBL Data Library, April 1988 !$#accession S02059 !'##molecule_type DNA !'##residues 1-26,'NARRP',32-57,'HN',60-403 ##label DOW !'##cross-references EMBL:Y00548; NID:g46212; PIDN:CAA68624.1; !1PID:g46219 !'##experimental_source strain 248 bv. viciae symbiotic plasmid RL1JI COMMENT This is one of several proteins that control host !1specificity of root hair infection and nodulation. GENETICS !$#gene nodE !$#genome plasmid CLASSIFICATION #superfamily 3-oxoacyl-[acyl-carrier-protein] synthase I; !13-oxoacyl-[acyl-carrier-protein] synthase I homology KEYWORDS host range; membrane protein; nodulation FEATURE !$23-399 #domain 3-oxoacyl-[acyl-carrier-protein] synthase I !8homology #label OAS SUMMARY #length 403 #molecular-weight 42110 #checksum 3758 SEQUENCE /// ENTRY S06021 #type complete TITLE nodulation protein nodE - Rhizobium leguminosarum bv. trifolii plasmid ORGANISM #formal_name Rhizobium leguminosarum bv. trifolii DATE 07-Sep-1990 #sequence_revision 13-Jan-1995 #text_change 11-Jun-1999 ACCESSIONS S06021; E23766 REFERENCE S06020 !$#authors Spaink, H.P.; Weinman, J.; Djordjevic, M.A.; Wijffelman, !1C.A.; Okker, R.J.H.; Lugtenberg, B.J.J. !$#journal EMBO J. (1989) 8:2811-2818 !$#title Genetic analysis and cellular localization of the Rhizobium !1host specificity-determining NodE protein. !$#cross-references MUID:90059862; PMID:2684629 !$#accession S06021 !'##molecule_type DNA !'##residues 1-401 ##label SPA !'##cross-references GB:X16620; NID:g46458; PIDN:CAA34617.1; PID:g46460 !'##experimental_source strain ANU843 symbiotic plasmid REFERENCE A93614 !$#authors Schofield, P.R.; Watson, J.M. !$#journal Nucleic Acids Res. (1986) 14:2891-2903 !$#title DNA sequence of Rhizobium trifolii nodulation genes reveals !1a reiterated and potentially regulatory sequence preceding !1nodABC and nodFE. !$#cross-references MUID:86176774; PMID:3008100 !$#accession E23766 !'##molecule_type DNA !'##residues 1-42 ##label SCH !'##cross-references GB:X03721; NID:g46461; PIDN:CAA27356.1; PID:g46467 !'##experimental_source strain ANU843 symbiotic plasmid COMMENT This is one of several proteins that control host !1specificity of root hair infection and nodulation. GENETICS !$#gene nodE !$#genome plasmid CLASSIFICATION #superfamily 3-oxoacyl-[acyl-carrier-protein] synthase I; !13-oxoacyl-[acyl-carrier-protein] synthase I homology KEYWORDS host range; membrane protein; nodulation FEATURE !$23-398 #domain 3-oxoacyl-[acyl-carrier-protein] synthase I !8homology #label OAS SUMMARY #length 401 #molecular-weight 42000 #checksum 3426 SEQUENCE /// ENTRY S25076 #type complete TITLE 3-oxoacyl-[acyl-carrier-protein] synthase (EC 2.3.1.41) chain 1 - Streptomyces cinnamonensis ALTERNATE_NAMES monensin-producing polyketide synthase chain 1 ORGANISM #formal_name Streptomyces cinnamonensis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S25076; S18167 REFERENCE S25076 !$#authors Arrowsmith, T.J.; Malpartida, F.; Sherman, D.H.; Birch, A.; !1Hopwood, D.A.; Robinson, J.A. !$#journal Mol. Gen. Genet. (1992) 234:254-264 !$#title Characterisation of actI-homologous DNA encoding polyketide !1synthase genes from the monensin producer Streptomyces !1cinnamonensis. !$#cross-references MUID:92374994; PMID:1508151 !$#accession S25076 !'##molecule_type DNA !'##residues 1-420 ##label ARR !'##cross-references EMBL:Z11511; NID:g46799; PIDN:CAA77596.1; !1PID:g46800 CLASSIFICATION #superfamily 3-oxoacyl-[acyl-carrier-protein] synthase I; !13-oxoacyl-[acyl-carrier-protein] synthase I homology KEYWORDS acyltransferase FEATURE !$24-412 #domain 3-oxoacyl-[acyl-carrier-protein] synthase I !8homology #label OAS SUMMARY #length 420 #molecular-weight 44453 #checksum 4298 SEQUENCE /// ENTRY S05973 #type complete TITLE tetracenomycin C polyketide beta-ketoacyl synthase (EC 2.3.1.-) chain 1 - Streptomyces glaucescens ALTERNATE_NAMES 3-oxoacyl-[acyl-carrier-protein] synthase homolog 1; tetracenomycin polyketide synthase-condensing enzyme ORGANISM #formal_name Streptomyces glaucescens DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S05973; S27693 REFERENCE S05972 !$#authors Bibb, M.J.; Biro, S.; Motamedi, H.; Collins, J.F.; !1Hutchinson, C.R. !$#journal EMBO J. (1989) 8:2727-2736 !$#title Analysis of the nucleotide sequence of the Streptomyces !1glaucescens tcmI genes provides key information about the !1enzymology of polyketide antibiotic biosynthesis. !$#cross-references MUID:90060035; PMID:2684656 !$#accession S05973 !'##molecule_type DNA !'##residues 1-426 ##label BIB !'##cross-references EMBL:X15312; NID:g47112; PIDN:CAA33369.1; !1PID:g47114 !'##experimental_source strain GLA.0., ETH22794 REFERENCE S27686 !$#authors Guilfoile, P.G.; Hutchinson, C.R. !$#submission submitted to the EMBL Data Library, February 1992 !$#description Evidence that tetracenomycin C resistance in Streptomyces !1glaucescens is similar in mechanism and regulation to !1eubacterial tetracycline resistance. !$#accession S27693 !'##molecule_type DNA !'##residues 1-426 ##label GUI !'##cross-references EMBL:M80674; NID:g153488; PIDN:AAA67515.1; !1PID:g153496 GENETICS !$#gene tcmIa CLASSIFICATION #superfamily 3-oxoacyl-[acyl-carrier-protein] synthase I; !13-oxoacyl-[acyl-carrier-protein] synthase I homology KEYWORDS acyltransferase FEATURE !$27-418 #domain 3-oxoacyl-[acyl-carrier-protein] synthase I !8homology #label OAS SUMMARY #length 426 #molecular-weight 45077 #checksum 1915 SEQUENCE /// ENTRY S05393 #type complete TITLE granaticin polyketide beta-ketoacyl synthase (EC 2.3.1.-) chain 1 [similarity] - Streptomyces violaceoruber ALTERNATE_NAMES 3-oxoacyl-[acyl-carrier-protein] synthase homolog 1; polyketide synthase keto-acyl synthase ORGANISM #formal_name Streptomyces violaceoruber DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 11-May-2000 ACCESSIONS S05393; T46537 REFERENCE S05393 !$#authors Sherman, D.H.; Malpartida, F.; Bibb, M.J.; Kieser, H.M.; !1Bibb, M.J.; Hopwood, D.A. !$#journal EMBO J. (1989) 8:2717-2725 !$#title Structure and deduced function of the granaticin-producing !1polyketide synthase gene cluster of Streptomyces !1violaceoruber Tue22. !$#cross-references MUID:90060034; PMID:2583128 !$#accession S05393 !'##molecule_type DNA !'##residues 1-421 ##label SHE !'##cross-references EMBL:X16144; NID:g47976; PIDN:CAA34264.1; !1PID:g581781 REFERENCE Z23045 !$#authors Ichinose, K.; Bedford, D.J.; Tornus, D.; Bechthold, A.; !1Bibb, M.J.; Revill, W.P.; Floss, H.G.; Hopwood, D.A. !$#journal Chem. Biol. (1998) 5:647-659 !$#title The granaticin biosynthetic gene cluster of Streptomyces !1violaceoruber Tu22: sequence analysis and expression in a !1heterologous host. !$#cross-references MUID:99051446; PMID:9831526 !$#accession T46537 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-421 ##label ICH !'##cross-references EMBL:AJ011500; PIDN:CAA09653.1 !'##experimental_source strain Tu22 GENETICS !$#gene graI !$#start_codon GTG !$#note gra-orf1 CLASSIFICATION #superfamily 3-oxoacyl-[acyl-carrier-protein] synthase I; !13-oxoacyl-[acyl-carrier-protein] synthase I homology KEYWORDS acyltransferase FEATURE !$23-414 #domain 3-oxoacyl-[acyl-carrier-protein] synthase I !8homology #label OAS SUMMARY #length 421 #molecular-weight 44392 #checksum 3211 SEQUENCE /// ENTRY JC1210 #type complete TITLE polyketide beta-ketoacyl synthase (EC 2.3.1.-) chain 1 - Streptomyces cyaneus ALTERNATE_NAMES beta-ketoacyl synthase; curA protein ORGANISM #formal_name Streptomyces cyaneus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JC1210; C33073 REFERENCE JC1210 !$#authors Bergh, S.; Uhlen, M. !$#journal Gene (1992) 117:131-136 !$#title Analysis of a polyketide synthesis-encoding gene cluster of !1Streptomyces curacoi. !$#cross-references MUID:92354925; PMID:1644304 !$#accession JC1210 !'##molecule_type DNA !'##residues 1-422 ##label BER !'##cross-references GB:X62518; NID:g46888; PIDN:CAA44380.1; PID:g581629 !'##note the source is designated as Streptomyces curacoi GENETICS !$#gene curA !$#start_codon GTG CLASSIFICATION #superfamily 3-oxoacyl-[acyl-carrier-protein] synthase I; !13-oxoacyl-[acyl-carrier-protein] synthase I homology KEYWORDS acyltransferase FEATURE !$23-414 #domain 3-oxoacyl-[acyl-carrier-protein] synthase I !8homology #label OAS SUMMARY #length 422 #molecular-weight 44726 #checksum 6552 SEQUENCE /// ENTRY JN0825 #type complete TITLE polyketide beta-ketoacyl synthase (EC 2.3.1.-) - Streptomyces halstedii ALTERNATE_NAMES polyketide synthesis condensing enzyme ORGANISM #formal_name Streptomyces halstedii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JN0825 REFERENCE PN0639 !$#authors Blanco, G.; Brian, P.; Pereda, A.; Mendez, C.; Salas, J.A.; !1Chater, K.F. !$#journal Gene (1993) 130:107-116 !$#title Hybridization and DNA sequence analyses suggest an early !1evolutionary divergence of related biosynthetic gene sets !1encoding polyketide antibiotics and spore pigments in !1Streptomyces spp. !$#cross-references MUID:93345807; PMID:8344517 !$#accession JN0825 !'##molecule_type DNA !'##residues 1-422 ##label BLA !'##cross-references GB:L05390; NID:g153319; PIDN:AAA02833.1; !1PID:g153323 GENETICS !$#gene sch CLASSIFICATION #superfamily 3-oxoacyl-[acyl-carrier-protein] synthase I; !13-oxoacyl-[acyl-carrier-protein] synthase I homology KEYWORDS acyltransferase FEATURE !$23-414 #domain 3-oxoacyl-[acyl-carrier-protein] synthase I !8homology #label OAS SUMMARY #length 422 #molecular-weight 44986 #checksum 7121 SEQUENCE /// ENTRY S25077 #type complete TITLE monensin polyketide beta-ketoacyl synthase (EC 2.3.1.-) chain 2 - Streptomyces cinnamonensis ORGANISM #formal_name Streptomyces cinnamonensis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S25077; S18168 REFERENCE S25076 !$#authors Arrowsmith, T.J.; Malpartida, F.; Sherman, D.H.; Birch, A.; !1Hopwood, D.A.; Robinson, J.A. !$#journal Mol. Gen. Genet. (1992) 234:254-264 !$#title Characterisation of actI-homologous DNA encoding polyketide !1synthase genes from the monensin producer Streptomyces !1cinnamonensis. !$#cross-references MUID:92374994; PMID:1508151 !$#accession S25077 !'##molecule_type DNA !'##residues 1-402 ##label ARR !'##cross-references EMBL:Z11511; NID:g46799; PIDN:CAA77597.1; !1PID:g46801 CLASSIFICATION #superfamily 3-oxoacyl-[acyl-carrier-protein] synthase I; !13-oxoacyl-[acyl-carrier-protein] synthase I homology KEYWORDS acyltransferase FEATURE !$22-398 #domain 3-oxoacyl-[acyl-carrier-protein] synthase I !8homology #label OAS SUMMARY #length 402 #molecular-weight 41270 #checksum 1904 SEQUENCE /// ENTRY S05974 #type complete TITLE tetracenomycin C polyketide beta-ketoacyl synthase (EC 2.3.1.-) chain 2 - Streptomyces glaucescens ALTERNATE_NAMES 3-oxoacyl-[acyl-carrier-protein] synthase homolog 2 ORGANISM #formal_name Streptomyces glaucescens DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S05974 REFERENCE S05972 !$#authors Bibb, M.J.; Biro, S.; Motamedi, H.; Collins, J.F.; !1Hutchinson, C.R. !$#journal EMBO J. (1989) 8:2727-2736 !$#title Analysis of the nucleotide sequence of the Streptomyces !1glaucescens tcmI genes provides key information about the !1enzymology of polyketide antibiotic biosynthesis. !$#cross-references MUID:90060035; PMID:2684656 !$#accession S05974 !'##molecule_type DNA !'##residues 1-405 ##label BIB !'##cross-references EMBL:X15312 GENETICS !$#gene tcmId CLASSIFICATION #superfamily 3-oxoacyl-[acyl-carrier-protein] synthase I; !13-oxoacyl-[acyl-carrier-protein] synthase I homology KEYWORDS acyltransferase FEATURE !$25-401 #domain 3-oxoacyl-[acyl-carrier-protein] synthase I !8homology #label OAS SUMMARY #length 405 #molecular-weight 42312 #checksum 8488 SEQUENCE /// ENTRY S05394 #type complete TITLE granaticin polyketide beta-ketoacyl synthase (EC 2.3.1.-) chain 2 [similarity] - Streptomyces violaceoruber ALTERNATE_NAMES 3-oxoacyl-[acyl-carrier-protein] synthase homolog 2; polyketide synthase chain length factor ORGANISM #formal_name Streptomyces violaceoruber DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 11-May-2000 ACCESSIONS S05394; T46538 REFERENCE S05393 !$#authors Sherman, D.H.; Malpartida, F.; Bibb, M.J.; Kieser, H.M.; !1Bibb, M.J.; Hopwood, D.A. !$#journal EMBO J. (1989) 8:2717-2725 !$#title Structure and deduced function of the granaticin-producing !1polyketide synthase gene cluster of Streptomyces !1violaceoruber Tue22. !$#cross-references MUID:90060034; PMID:2583128 !$#accession S05394 !'##molecule_type DNA !'##residues 1-415 ##label SHE !'##cross-references EMBL:X16144; NID:g47976; PIDN:CAA34265.1; !1PID:g581782 REFERENCE Z23045 !$#authors Ichinose, K.; Bedford, D.J.; Tornus, D.; Bechthold, A.; !1Bibb, M.J.; Revill, W.P.; Floss, H.G.; Hopwood, D.A. !$#journal Chem. Biol. (1998) 5:647-659 !$#title The granaticin biosynthetic gene cluster of Streptomyces !1violaceoruber Tu22: sequence analysis and expression in a !1heterologous host. !$#cross-references MUID:99051446; PMID:9831526 !$#accession T46538 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-415 ##label ICH !'##cross-references EMBL:AJ011500; PIDN:CAA09654.1 !'##experimental_source strain Tu22 GENETICS !$#gene graI !$#start_codon GTG !$#note gra-orf2 CLASSIFICATION #superfamily 3-oxoacyl-[acyl-carrier-protein] synthase I; !13-oxoacyl-[acyl-carrier-protein] synthase I homology KEYWORDS acyltransferase FEATURE !$27-404 #domain 3-oxoacyl-[acyl-carrier-protein] synthase I !8homology #label OAS SUMMARY #length 415 #molecular-weight 43401 #checksum 6296 SEQUENCE /// ENTRY JC1211 #type complete TITLE beta-ketoacyl synthase (EC 2.3.1.-) curB - Streptomyces cyaneus ORGANISM #formal_name Streptomyces cyaneus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JC1211; S17334 REFERENCE JC1210 !$#authors Bergh, S.; Uhlen, M. !$#journal Gene (1992) 117:131-136 !$#title Analysis of a polyketide synthesis-encoding gene cluster of !1Streptomyces curacoi. !$#cross-references MUID:92354925; PMID:1644304 !$#accession JC1211 !'##molecule_type DNA !'##residues 1-419 ##label BER !'##cross-references GB:X62518; NID:g46888; PIDN:CAA44381.1; PID:g46892 !'##note the source is designated as Streptomyces curacoi GENETICS !$#gene curB CLASSIFICATION #superfamily 3-oxoacyl-[acyl-carrier-protein] synthase I; !13-oxoacyl-[acyl-carrier-protein] synthase I homology KEYWORDS acyltransferase FEATURE !$31-411 #domain 3-oxoacyl-[acyl-carrier-protein] synthase I !8homology #label OAS SUMMARY #length 419 #molecular-weight 42974 #checksum 9740 SEQUENCE /// ENTRY S11975 #type complete TITLE probable beta-ketoacyl synthase (EC 2.3.1.-) - Streptomyces coelicolor ALTERNATE_NAMES hypothetical protein 4 ORGANISM #formal_name Streptomyces coelicolor DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 12-Nov-1999 ACCESSIONS S11975; T35612 REFERENCE S11972 !$#authors Davis, N.K.; Chater, K.F. !$#journal Mol. Microbiol. (1990) 4:1679-1691 !$#title Spore colour in Streptomyces coelicolor A3(2) involves the !1developmentally regulated synthesis of a compound !1biosynthetically related to polyketide antibiotics. !$#cross-references MUID:91171868; PMID:2077356 !$#accession S11975 !'##status preliminary !'##molecule_type DNA !'##residues 1-424 ##label DAV !'##cross-references EMBL:X55942; NID:g46919; PIDN:CAA39409.1; !1PID:g46923 REFERENCE Z21584 !$#authors Seeger, K.J.; Harris, D.; James, K.D.; Parkhill, J.; !1Barrell, B.G.; Rajandream, M.A. !$#submission submitted to the EMBL Data Library, June 1999 !$#accession T35612 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-424 ##label SEE !'##cross-references EMBL:AL079356; PIDN:CAB45607.1; GSPDB:GN00070; !1SCOEDB:SC6G9.16 !'##experimental_source strain A3(2) GENETICS !$#gene SCOEDB:SC6G9.16 CLASSIFICATION #superfamily 3-oxoacyl-[acyl-carrier-protein] synthase I; !13-oxoacyl-[acyl-carrier-protein] synthase I homology KEYWORDS acyltransferase FEATURE !$34-414 #domain 3-oxoacyl-[acyl-carrier-protein] synthase I !8homology #label OAS SUMMARY #length 424 #molecular-weight 43557 #checksum 6208 SEQUENCE /// ENTRY JN0826 #type complete TITLE probable beta-ketoacyl synthase (EC 2.3.1.-) - Streptomyces halstedii ORGANISM #formal_name Streptomyces halstedii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JN0826 REFERENCE PN0639 !$#authors Blanco, G.; Brian, P.; Pereda, A.; Mendez, C.; Salas, J.A.; !1Chater, K.F. !$#journal Gene (1993) 130:107-116 !$#title Hybridization and DNA sequence analyses suggest an early !1evolutionary divergence of related biosynthetic gene sets !1encoding polyketide antibiotics and spore pigments in !1Streptomyces spp. !$#cross-references MUID:93345807; PMID:8344517 !$#accession JN0826 !'##molecule_type DNA !'##residues 1-414 ##label BLA !'##cross-references GB:L05390; NID:g153319; PIDN:AAA02834.1; !1PID:g153324 COMMENT This protein is similar to ketosynthase but locks active !1site motif. GENETICS !$#gene sch CLASSIFICATION #superfamily 3-oxoacyl-[acyl-carrier-protein] synthase I; !13-oxoacyl-[acyl-carrier-protein] synthase I homology KEYWORDS acyltransferase FEATURE !$25-405 #domain 3-oxoacyl-[acyl-carrier-protein] synthase I !8homology #label OAS SUMMARY #length 414 #molecular-weight 42776 #checksum 5011 SEQUENCE /// ENTRY S36204 #type complete TITLE probable beta-ketoacyl synthase (EC 2.3.1.-) CEM1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YER061c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS S36204; S50564 REFERENCE S36204 !$#authors Harington, A.; Herbert, C.J.; Tung, B.; Getz, G.S.; !1Slonimski, P.P. !$#journal Mol. Microbiol. (1993) 9:545-555 !$#title Identification of a new nuclear gene (CEM1) encoding a !1protein homologous to a beta-keto-acyl synthase which is !1essential for mitochondrial respiration in Saccharomyces !1cerevisiae. !$#cross-references MUID:94018649; PMID:8412701 !$#accession S36204 !'##molecule_type DNA !'##residues 1-442 ##label HAR !'##cross-references EMBL:X73488; NID:g403310; PIDN:CAB58180.1; !1PID:g6066682 REFERENCE S50557 !$#authors Dietrich, F.S. !$#submission submitted to the EMBL Data Library, December 1994 !$#description The sequence of S. cerevisiae lambda clones 6592, 4678, !14742, and 3612. !$#accession S50564 !'##molecule_type DNA !'##residues 1-442 ##label DIE !'##cross-references EMBL:U18813; NID:g1381127; PIDN:AAB64597.1; !1PID:g603297; GSPDB:GN00005; MIPS:YER061c GENETICS !$#gene SGD:CEM1; MIPS:YER061c !'##cross-references SGD:S0000863; MIPS:YER061c !$#map_position 5R CLASSIFICATION #superfamily 3-oxoacyl-[acyl-carrier-protein] synthase I; !13-oxoacyl-[acyl-carrier-protein] synthase I homology KEYWORDS acyltransferase; mitochondrion FEATURE !$23-436 #domain 3-oxoacyl-[acyl-carrier-protein] synthase I !8homology #label OAS SUMMARY #length 442 #molecular-weight 47555 #checksum 9938 SEQUENCE /// ENTRY A42431 #type complete TITLE 3-oxoacyl-[acyl-carrier-protein] synthase (EC 2.3.1.41) III - Escherichia coli (strain K-12) ALTERNATE_NAMES beta-ketoacyl-acyl carrier protein synthase III ORGANISM #formal_name Escherichia coli DATE 04-Mar-1993 #sequence_revision 13-Jan-1995 #text_change 01-Mar-2002 ACCESSIONS A42431; A41856; S30131; H64852 REFERENCE A42431 !$#authors Tsay, J.T.; Oh, W.; Larson, T.J.; Jackowski, S.; Rock, C.O. !$#journal J. Biol. Chem. (1992) 267:6807-6814 !$#title Isolation and characterization of the beta-ketoacyl-acyl !1carrier protein synthase III gene (fabH) from Escherichia !1coli K-12. !$#cross-references MUID:92202232; PMID:1551888 !$#accession A42431 !'##molecule_type DNA !'##residues 1-317 ##label TSA !'##cross-references GB:M77744; NID:g145897; PIDN:AAA23749.1; !1PID:g145898 !'##experimental_source strain K-12 !'##note sequence extracted from NCBI backbone (NCBIN:90061, !1NCBIP:90064) !'##note amino-terminal 30 residues confirmed by protein sequencing REFERENCE A41856 !$#authors Verwoert, I.I.; Verbree, E.C.; van der Linden, K.H.; !1Nijkamp, H.J.; Stuitje, A.R. !$#journal J. Bacteriol. (1992) 174:2851-2857 !$#title Cloning, nucleotide sequence, and expression of the !1Escherichia coli fabD gene, encoding malonyl coenzyme A-acyl !1carrier protein transacylase. !$#cross-references MUID:92234941; PMID:1314802 !$#accession A41856 !'##molecule_type DNA !'##residues 147-317 ##label VER !'##cross-references GB:M87040; NID:g145885; PIDN:AAA23741.1; !1PID:g145886 !'##note sequence extracted from NCBI backbone (NCBIN:97135, !1NCBIP:97142) REFERENCE S20443 !$#authors Magnuson, K.; Oh, W.; Larson, T.J.; Cronan Jr., J.E. !$#journal FEBS Lett. (1992) 299:262-266 !$#title Cloning and nucleotide sequence of the fabD gene encoding !1malonyl coenzyme A-acyl carrier protein transacylase of !1Escherichia coli. !$#cross-references MUID:92183950; PMID:1339356 !$#accession S30131 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 201-317 ##label MAG !'##cross-references EMBL:Z11565; NID:g41363; PIDN:CAA77659.1; !1PID:g41365 !'##experimental_source strain K-12 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1992 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64852 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-317 ##label BLAT !'##cross-references GB:AE000210; GB:U00096; NID:g1787332; !1PIDN:AAC74175.1; PID:g1787333; UWGP:b1091 !'##experimental_source strain K-12, substrain MG1655 COMMENT This enzyme also has [acyl-carrier-protein] !1S-acetyltransferase activity. GENETICS !$#gene fabH !$#map_position 24.5 min FUNCTION !$#description catalyzes the initial condensing reaction in fatty acid !1biosynthesis, using acetyl-CoA as the acyl receptor !$#pathway fatty acid biosynthesis CLASSIFICATION #superfamily 3-oxoacyl-[acyl-carrier-protein] synthase III KEYWORDS acyltransferase; fatty acid biosynthesis; monomer FEATURE !$112 #active_site Cys #status predicted SUMMARY #length 317 #molecular-weight 33515 #checksum 9485 SEQUENCE /// ENTRY JQ2386 #type complete TITLE 3-oxoacyl-[acyl-carrier-protein] synthase (EC 2.3.1.41) III precursor, chloroplast - spinach ORGANISM #formal_name Spinacia oleracea #common_name spinach DATE 28-Aug-1985 #sequence_revision 13-Jan-1995 #text_change 11-Jun-1999 ACCESSIONS JQ2386; PQ0861; S33474 REFERENCE JQ2386 !$#authors Tai, H.; Jaworski, J.G. !$#journal Plant Physiol. (1993) 103:1361-1367 !$#title 3-Ketoacyl-acyl carrier protein synthase III from spinach !1(Spinacia oleracea) is not similar to other condensing !1enzymes of fatty acid synthase. !$#cross-references MUID:94120009; PMID:8290632 !$#accession JQ2386 !'##molecule_type mRNA !'##residues 1-405 ##label TAI !'##cross-references EMBL:Z22771; NID:g311685; PIDN:CAA80452.1; !1PID:g311686 !$#accession PQ0861 !'##molecule_type protein !'##residues !174-81;84-104;118-127;130-151;214-220;261-279;286-294; !1306-314;320-336;351-367 ##label TA2 !'##experimental_source leaf and root COMMENT This enzyme catalyzes the initial condensing reaction in !1fatty acid biosynthesis, using acetyl-CoA as the acyl !1receptor. CLASSIFICATION #superfamily 3-oxoacyl-[acyl-carrier-protein] synthase III KEYWORDS acyltransferase; chloroplast; fatty acid biosynthesis FEATURE !$181 #active_site Cys #status predicted SUMMARY #length 405 #molecular-weight 42534 #checksum 3639 SEQUENCE /// ENTRY XXHUN #type complete TITLE phosphatidylcholine-sterol O-acyltransferase (EC 2.3.1.43) precursor [validated] - human ALTERNATE_NAMES lecithin-cholesterol acyltransferase precursor; phospholipid-cholesterol acyltransferase precursor ORGANISM #formal_name Homo sapiens #common_name man DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 03-Jun-2002 ACCESSIONS A00571; A25575; A29661; JQ0036; A29133; I52260; A28511 REFERENCE A00571 !$#authors McLean, J.; Fielding, C.; Drayna, D.; Dieplinger, H.; Baer, !1B.; Kohr, W.; Henzel, W.; Lawn, R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:2335-2339 !$#title Cloning and expression of human lecithin-cholesterol !1acyltransferase cDNA. !$#cross-references MUID:86205950; PMID:3458198 !$#accession A00571 !'##molecule_type mRNA !'##residues 1-440 ##label MCL1 !'##cross-references GB:M12625; NID:g187022; PIDN:AAA59498.1; !1PID:g307117 REFERENCE A25575 !$#authors McLean, J.; Wion, K.; Drayna, D.; Fielding, C.; Lawn, R. !$#journal Nucleic Acids Res. (1986) 14:9397-9406 !$#title Human lecithin-cholesterol acyltransferase gene: complete !1gene sequence and sites of expression. !$#cross-references MUID:87091568; PMID:3797244 !$#accession A25575 !'##molecule_type DNA !'##residues 1-440 ##label MCL2 !'##cross-references GB:X04981; NID:g34286; PIDN:CAA28651.1; PID:g34287 REFERENCE A29661 !$#authors Rogne, S.; Skretting, G.; Larsen, F.; Myklebost, O.; Mevag, !1B.; Carlson, L.A.; Holmquist, L.; Gjone, E.; Prydz, H. !$#journal Biochem. Biophys. Res. Commun. (1987) 148:161-169 !$#title The isolation and characterisation of a cDNA clone for human !1lecithin:cholesterol acyl transferase and its use to analyse !1the genes in patients with LCAT deficiency and fish eye !1disease. !$#cross-references MUID:88049652; PMID:2823801 !$#accession A29661 !'##molecule_type mRNA !'##residues 13-440 ##label ROG !'##cross-references GB:M17959; NID:g187026; PIDN:AAA59500.1; !1PID:g386858 REFERENCE A90666 !$#authors Tata, F.; Chaves, M.E.; Markham, A.F.; Scrace, G.D.; !1Waterfield, M.D.; McIntyre, N.; Williamson, R.; Humphries, !1S.E. !$#journal Biochim. Biophys. Acta (1987) 910:142-148 !$#title The isolation and characterisation of cDNA and genomic !1clones for human lecithin:cholesterol acyltransferase. !$#cross-references MUID:88050946; PMID:2823898 !$#accession JQ0036 !'##molecule_type mRNA !'##residues 17-256,'H',258-440 ##label TAT !'##cross-references GB:X06537; NID:g34284; GB:M26268; NID:g187024; !1PIDN:AAA59499.1; PID:g187025 !'##note the authors translated the codon CAT for residue 241 as Ile and !1CAG for residues 251, 304, 368, 373, and 384 as Leu REFERENCE A29133 !$#authors Yang, C.; Manoogian, D.; Pao, Q.; Lee, F.; Knapp, R.D.; !1Gotto Jr., A.M.; Pownall, H.J. !$#journal J. Biol. Chem. (1987) 262:3086-3091 !$#title Lecithin: cholesterol acyltransferase. Functional regions !1and a structural model of the enzyme. !$#cross-references MUID:87137578; PMID:2880847 !$#accession A29133 !'##molecule_type protein !'##residues 25-284,'Q',286-333,'Q',335-440 ##label YAN REFERENCE I52260 !$#authors Bujo, H.; Kusunoki, J.; Ogasawara, M.; Yamamoto, T.; Ohta, !1Y.; Shimada, T.; Saito, Y.; Yoshida, S. !$#journal Biochem. Biophys. Res. Commun. (1991) 181:933-940 !$#title Molecular defect in familial lecithin:cholesterol !1acyltransferase (LCAT) deficiency: a single nucleotide !1insertion in LCAT gene causes a complete deficient type of !1the disease. !$#cross-references MUID:92109783; PMID:1662503 !$#accession I52260 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 25-34,'AHHAQG' ##label BUJ !'##cross-references GB:S74079; NID:g241428; PIDN:AAB20750.1; !1PID:g241429 !'##note defective frame shift mutant sequence REFERENCE A57914 !$#authors Schindler, P.A.; Settineri, C.A.; Collet, X.; Fielding, !1C.J.; Burlingame, A.L. !$#journal Protein Sci. (1995) 4:791-803 !$#title Site-specific detection and structural characterization of !1the glycosylation of human plasma proteins !1lecithin:cholesterol acyltransferase and apolipoprotein D !1using HPLC/electrospray mass spectrometry and sequential !1glycosidase digestion. !$#cross-references MUID:95338133; PMID:7613477 !$#contents annotation; peptide sequences; N- and O-glycosylation COMMENT Apolipoprotein A-I (see PIR:LPHUA1) is a potent activator of !1this enzyme. GENETICS !$#gene GDB:LCAT !'##cross-references GDB:119359; OMIM:245900 !$#map_position 16q22.1-16q22.1 FUNCTION !$#description catalyzes the transfer of sn-2 fatty acyl groups from !1phosphatidylcholine (lecithin) to sterol to form sterol !1fatty esters and 1-acylglycerphosphocholine !$#note palmitoyl, oleoyl, and linoleoyl residues can be !1transferred; a number of sterols, including cholesterol, can !1act as acceptor CLASSIFICATION #superfamily phosphatidylcholine-sterol acyltransferase KEYWORDS acyltransferase; cholesterol; glycoprotein; lipid !1metabolism; lipoprotein FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-440 #product phosphatidylcholine-sterol acyltransferase !8#status experimental #label MAT\ !$202-207 #region interfacial lipid recognition (GXSXG) motif\ !$44,108,296,408 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$431 #binding_site carbohydrate (Thr) (covalent) #status !8experimental\ !$433 #binding_site carbohydrate (Ser) (covalent) #status !8experimental SUMMARY #length 440 #molecular-weight 49578 #checksum 8696 SEQUENCE /// ENTRY XXRTN #type complete TITLE phosphatidylcholine-sterol O-acyltransferase (EC 2.3.1.43) precursor - rat ALTERNATE_NAMES lecithin-cholesterol acyltransferase precursor; phospholipid-cholesterol acyltransferase precursor ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 03-Jun-2002 ACCESSIONS S11214; S11302 REFERENCE S11214 !$#authors Meroni, G.; Malgaretti, N.; Magnaghi, P.; Taramelli, R. !$#journal Nucleic Acids Res. (1990) 18:5308 !$#title Nucleotide sequence of the cDNA for lecithin-cholesterol !1acyl transferase (LCAT) from the rat. !$#cross-references MUID:90384859; PMID:2402469 !$#accession S11214 !'##molecule_type mRNA !'##residues 1-440 ##label MER !'##cross-references EMBL:X54096 REFERENCE S11302 !$#authors Taramelli, R. !$#submission submitted to the EMBL Data Library, July 1990 !$#accession S11302 !'##molecule_type mRNA !'##residues 1-389,'G',391-440 ##label TAR !'##cross-references EMBL:X54096; NID:g56563; PIDN:CAA38030.1; !1PID:g56564 COMMENT The active enzyme catalyzes the transfer of acyl groups from !1lecithin to sterol to form sterol esters. Palmitoyl, oleoyl, !1and linoleoyl residues can be transferred; a number of !1sterols, including cholesterol, can act as acceptor. !1Apolipoprotein A-I is a potent activator for this enzyme. GENETICS !$#gene LCAT CLASSIFICATION #superfamily phosphatidylcholine-sterol acyltransferase KEYWORDS acyltransferase; glycoprotein; lipid metabolism; lipoprotein FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-438 #product phosphatidylcholine-sterol acyltransferase !8#status predicted #label MAT\ !$44,108,296,408 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 440 #molecular-weight 49741 #checksum 6639 SEQUENCE /// ENTRY XXMSN #type complete TITLE phosphatidylcholine-sterol O-acyltransferase (EC 2.3.1.43) precursor - mouse ALTERNATE_NAMES lecithin-cholesterol acyltransferase precursor; phospholipid-cholesterol acyltransferase precursor ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 03-Jun-2002 ACCESSIONS A34158; S21370 REFERENCE A34158 !$#authors Warden, C.H.; Langner, C.A.; Gordon, J.I.; Taylor, B.A.; !1McLean, J.W.; Lusis, A.J. !$#journal J. Biol. Chem. (1989) 264:21573-21581 !$#title Tissue-specific expression, developmental regulation, and !1chromosomal mapping of the lecithin:cholesterol !1acyltransferase gene. Evidence for expression in brain and !1testes as well as liver. !$#cross-references MUID:90094326; PMID:2600083 !$#accession A34158 !'##molecule_type mRNA !'##residues 1-438 ##label WAR !'##cross-references GB:J05154; NID:g198759; PIDN:AAA39419.1; !1PID:g293697 !'##note the authors translated the codon ATG for residue 411 as Leu REFERENCE S21370 !$#authors Meroni, G.; Malgaretti, N.; Magnaghi, P.; Taramelli, R. !$#submission submitted to the EMBL Data Library, July 1990 !$#description Promoter and 5' flanking sequences of the mouse LCAT gene. !$#accession S21370 !'##molecule_type DNA !'##residues 1-14 ##label MER !'##cross-references EMBL:X54095; NID:g52873; PIDN:CAA38029.1; !1PID:g52874 COMMENT The active enzyme catalyzes the transfer of acyl groups from !1lecithin to sterol to form sterol esters. Palmitoyl, oleoyl, !1and linoleoyl residues can be transferred; a number of !1sterols, including cholesterol, can act as acceptor. !1Apolipoprotein A-I is a potent activator for this enzyme. CLASSIFICATION #superfamily phosphatidylcholine-sterol acyltransferase KEYWORDS acyltransferase; glycoprotein; lipid metabolism; lipoprotein FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-438 #product phosphatidylcholine-sterol acyltransferase !8#status predicted #label MAT\ !$44,108,296,408 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 438 #molecular-weight 49765 #checksum 1794 SEQUENCE /// ENTRY XYECM #type complete TITLE homoserine O-succinyltransferase (EC 2.3.1.46) - Escherichia coli (strain K-12) ALTERNATE_NAMES homoserine O-transsuccinylase ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS D65208; A93686; A91798; S05690; A05053; JV0023 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65208 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-309 ##label BLAT !'##cross-references GB:AE000474; GB:U00096; NID:g1790440; !1PIDN:AAC76983.1; PID:g1790443; UWGP:b4013 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A93686 !$#authors Duclos, B.; Cortay, J.C.; Bleicher, F.; Ron, E.Z.; Richaud, !1C.; Saint Girons, I.; Cozzone, A.J. !$#journal Nucleic Acids Res. (1989) 17:2856 !$#title Nucleotide sequence of the metA gene encoding homoserine !1trans-succinylase in Escherichia coli. !$#cross-references MUID:89240044; PMID:2654885 !$#accession A93686 !'##molecule_type DNA !'##residues 1-66,'V',68-309 ##label DUC !'##cross-references GB:X14501; NID:g41997; PIDN:CAA32654.1; PID:g41998 REFERENCE A91798 !$#authors Michaeli, S.; Mevarech, M.; Ron, E.Z. !$#journal J. Bacteriol. (1984) 160:1158-1162 !$#title Regulatory region of the metA gene of Escherichia coli K-12. !$#cross-references MUID:85054633; PMID:6094503 !$#accession A91798 !'##molecule_type DNA !'##residues 1-66,'V',68-69 ##label MIC !'##cross-references GB:M10210; NID:g146820; PIDN:AAA24157.1; !1PID:g146821 REFERENCE S01438 !$#authors Byrne, C.; Stokes, H.W.; Ward, K.A. !$#journal Nucleic Acids Res. (1988) 16:9342 !$#title Nucleotide sequence of the aceB gene encoding malate !1synthase A in Escherichia coli. !$#cross-references MUID:89016638; PMID:3050899 !$#accession S05690 !'##status preliminary !'##molecule_type DNA !'##residues 207-309 ##label BYR !'##cross-references EMBL:X12431 COMMENT This enzyme catalyzes the first step in methionine !1biosynthesis, the formation of O-succinyl-L-homoserine from !1succinyl-CoA and homoserine. GENETICS !$#gene metA !$#map_position 91 CLASSIFICATION #superfamily homoserine succinyltransferase KEYWORDS acyltransferase; coenzyme A; methionine biosynthesis SUMMARY #length 309 #molecular-weight 35727 #checksum 1870 SEQUENCE /// ENTRY SYSKCD #type complete TITLE naringenin-chalcone synthase (EC 2.3.1.74) - garden snapdragon ALTERNATE_NAMES chalcone synthase ORGANISM #formal_name Antirrhinum majus #common_name garden snapdragon DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 05-May-2000 ACCESSIONS S07312; A33217 REFERENCE S07312 !$#authors Sommer, H.; Saedler, H. !$#journal Mol. Gen. Genet. (1986) 202:429-434 !$#title Structure of the chalcone synthase gene of Antirrhinum !1majus. !$#accession S07312 !'##molecule_type DNA !'##residues 1-390 ##label SOM !'##cross-references EMBL:X03710; NID:g16015; PIDN:CAA27338.1; !1PID:g16016 !$#accession A33217 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-390 ##label SOM2 GENETICS !$#gene chs !$#introns 60/1; 162/3 CLASSIFICATION #superfamily chalcone synthase KEYWORDS acyltransferase; coenzyme A; flavonoid biosynthesis SUMMARY #length 390 #molecular-weight 42636 #checksum 3815 SEQUENCE /// ENTRY SYMUCN #type complete TITLE naringenin-chalcone synthase (EC 2.3.1.74) - Arabidopsis thaliana ALTERNATE_NAMES chalcone synthase ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 05-May-2000 ACCESSIONS A27721 REFERENCE A27721 !$#authors Feinbaum, R.L.; Ausubel, F.M. !$#journal Mol. Cell. Biol. (1988) 8:1985-1992 !$#title Transcriptional regulation of the Arabidopsis thaliana !1chalcone synthase gene. !$#cross-references MUID:88261274; PMID:3386631 !$#accession A27721 !'##molecule_type DNA !'##residues 1-395 ##label FEI !'##cross-references GB:M20308; NID:g166669; PIDN:AAA32771.1; !1PID:g166670 COMMENT This enzyme plays a central role in the biosynthesis of all !1classes of flavonoids in plants. GENETICS !$#introns 65/1 CLASSIFICATION #superfamily chalcone synthase KEYWORDS acyltransferase; coenzyme A; flavonoid biosynthesis SUMMARY #length 395 #molecular-weight 43115 #checksum 1754 SEQUENCE /// ENTRY SYISC1 #type complete TITLE naringenin-chalcone synthase (EC 2.3.1.74) 1 - white mustard ORGANISM #formal_name Sinapis alba #common_name white mustard DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 05-May-2000 ACCESSIONS S14716; S06876; S06778 REFERENCE S14716 !$#authors Batschauer, A.; Ehmann, B.; Schaefer, E. !$#journal Plant Mol. Biol. (1991) 16:175-185 !$#title Cloning and characterization of a chalcone synthase gene !1from mustard and its light-dependent expression. !$#cross-references MUID:91370861; PMID:1893096 !$#accession S14716 !'##molecule_type DNA !'##residues 1-395 ##label BAT !'##cross-references EMBL:X16437; NID:g21164; PIDN:CAA34460.1; !1PID:g295835 REFERENCE S06876 !$#authors Ehmann, B.; Schaefer, E. !$#journal Plant Mol. Biol. (1988) 11:869-870 !$#title Nucleotide sequences encoding two different chalcone !1synthases expressed in cotyledons of SAN 9789 treated !1mustard (Sinapis alba L.). !$#accession S06876 !'##molecule_type mRNA !'##residues 124-290,'R',292-395 ##label EHM !'##cross-references EMBL:X14315; NID:g21161; PIDN:CAA32496.1; !1PID:g829290 GENETICS !$#introns 65/1 CLASSIFICATION #superfamily chalcone synthase KEYWORDS acyltransferase; coenzyme A; flavonoid biosynthesis SUMMARY #length 395 #molecular-weight 42993 #checksum 912 SEQUENCE /// ENTRY SYISC3 #type complete TITLE naringenin-chalcone synthase (EC 2.3.1.74) 3 - white mustard ALTERNATE_NAMES chalcone synthase ORGANISM #formal_name Sinapis alba #common_name white mustard DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 05-May-2000 ACCESSIONS S06877 REFERENCE S06876 !$#authors Ehmann, B.; Schaefer, E. !$#journal Plant Mol. Biol. (1988) 11:869-870 !$#title Nucleotide sequences encoding two different chalcone !1synthases expressed in cotyledons of SAN 9789 treated !1mustard (Sinapis alba L.). !$#accession S06877 !'##molecule_type mRNA !'##residues 1-395 ##label EHM !'##cross-references GB:X14314; NID:g21162; PIDN:CAA32495.1; PID:g21163 COMMENT This enzyme plays a central role in the biosynthesis of all !1classes of flavonoids in plants. CLASSIFICATION #superfamily chalcone synthase KEYWORDS acyltransferase; coenzyme A; flavonoid biosynthesis SUMMARY #length 395 #molecular-weight 43064 #checksum 887 SEQUENCE /// ENTRY SYJCCS #type complete TITLE naringenin-chalcone synthase (EC 2.3.1.74) - common stock ORGANISM #formal_name Matthiola incana #common_name common stock DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 05-May-2000 ACCESSIONS S11876 REFERENCE S11876 !$#authors Epping, B.; Kittel, M.; Ruhnau, B.; Hemleben, V. !$#journal Plant Mol. Biol. (1990) 14:1061-1063 !$#title Isolation and sequence analysis of a chalcone synthase cDNA !1of Matthiola incana R. Br. (Brassicaceae). !$#cross-references MUID:91346693; PMID:2102873 !$#accession S11876 !'##molecule_type mRNA !'##residues 1-394 ##label EPP !'##cross-references EMBL:X17577; NID:g19556; PIDN:CAA35600.1; !1PID:g19557 CLASSIFICATION #superfamily chalcone synthase KEYWORDS acyltransferase; coenzyme A; flavonoid biosynthesis SUMMARY #length 394 #molecular-weight 42968 #checksum 6500 SEQUENCE /// ENTRY SYPJCJ #type complete TITLE naringenin-chalcone synthase (EC 2.3.1.74) J - garden petunia ALTERNATE_NAMES chalcone synthase ORGANISM #formal_name Petunia x hybrida #common_name garden petunia DATE 30-Sep-1991 #sequence_revision 17-Mar-2000 #text_change 05-May-2000 ACCESSIONS D72821; JS0309 REFERENCE JS0308 !$#authors Koes, R.E.; Spelt, C.E.; van den Elzen, P.J.M.; Mol, J.N.M. !$#journal Gene (1989) 81:245-257 !$#title Cloning and molecular characterization of the chalcone !1synthase multigene family of Petunia hybrida. !$#cross-references MUID:90034197; PMID:2806915 !$#accession D72821 !'##molecule_type DNA !'##residues 1-389 ##label KOE !'##cross-references EMBL:X14597; NID:g20535; PIDN:CAA32737.1; !1PID:g20536 !'##experimental_source strain Violet 30, leaf !$#accession JS0309 !'##molecule_type DNA !'##residues 1-50,'D',52-74,'V',76-228,'I',230-297,'L',299-389 ##label !1KO2 !'##note the sequence is revised in GenBank entry PHCHSJ release 114, !1(PIDN:CAA32737.1) COMMENT This enzyme plays a central role in the biosynthesis of all !1classes of flavonoids in plants. GENETICS !$#gene chsJ !$#map_position V !$#note chsJ is expressed in various floral tissues and UV !1illuminated seedlings CLASSIFICATION #superfamily chalcone synthase KEYWORDS acyltransferase; coenzyme A; flavonoid biosynthesis SUMMARY #length 389 #molecular-weight 42558 #checksum 466 SEQUENCE /// ENTRY SYPJCN #type complete TITLE naringenin-chalcone synthase (EC 2.3.1.74) R - garden petunia ALTERNATE_NAMES chalcone synthase ORGANISM #formal_name Petunia x hybrida #common_name garden petunia DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 05-May-2000 ACCESSIONS A23643 REFERENCE A23643 !$#authors Koes, R.E.; Spelt, C.E.; Reif, H.J.; van den Elzen, P.J.M.; !1Veltkamp, E.; Mol, J.N.M. !$#journal Nucleic Acids Res. (1986) 14:5229-5239 !$#title Floral tissue of Petunia hybrida (V30) expresses only one !1member of the chalcone synthase multigene family. !$#cross-references MUID:86286540; PMID:3016642 !$#accession A23643 !'##molecule_type mRNA !'##residues 1-389 ##label KOE !'##cross-references GB:X04080; NID:g20541; PIDN:CAA27718.1; PID:g20542 !'##experimental_source strain Violet 30, flowers COMMENT This enzyme plays a central role in the biosynthesis of all !1classes of flavonoids in plants. GENETICS !$#gene chsR !$#note expressed in floral tissue CLASSIFICATION #superfamily chalcone synthase KEYWORDS acyltransferase; coenzyme A; flavonoid biosynthesis SUMMARY #length 389 #molecular-weight 42525 #checksum 7905 SEQUENCE /// ENTRY SYPJCA #type complete TITLE naringenin-chalcone synthase (EC 2.3.1.74) A - garden petunia ALTERNATE_NAMES chalcone synthase ORGANISM #formal_name Petunia x hybrida #common_name garden petunia DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 05-May-2000 ACCESSIONS JS0308 REFERENCE JS0308 !$#authors Koes, R.E.; Spelt, C.E.; van den Elzen, P.J.M.; Mol, J.N.M. !$#journal Gene (1989) 81:245-257 !$#title Cloning and molecular characterization of the chalcone !1synthase multigene family of Petunia hybrida. !$#cross-references MUID:90034197; PMID:2806915 !$#accession JS0308 !'##molecule_type DNA !'##residues 1-389 ##label KOE !'##cross-references GB:X14591; NID:g20524; PIDN:CAA32731.1; PID:g20525 !'##experimental_source strain Violet 30, leaf COMMENT This enzyme plays a central role in the biosynthesis of all !1classes of flavonoids in plants. GENETICS !$#gene chsA !$#map_position V !$#note chsA is the major expressed member of the genefamily in !1various floral tissues and in seedlings treated with UV !1light. It is relatively low expressed in tissue culture !1material CLASSIFICATION #superfamily chalcone synthase KEYWORDS acyltransferase; coenzyme A; flavonoid biosynthesis SUMMARY #length 389 #molecular-weight 42573 #checksum 7681 SEQUENCE /// ENTRY SYFJCP #type complete TITLE naringenin-chalcone synthase (EC 2.3.1.74) I - kudzu vine ALTERNATE_NAMES chalcone synthase I ORGANISM #formal_name Pueraria lobata #common_name kudzu vine DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 05-May-2000 ACCESSIONS JQ0911; JC4539 REFERENCE JQ0911 !$#authors Nakajima, O.; Akiyama, T.; Hakamatsuka, T.; Shibuya, M.; !1Noguchi, H.; Ebizuka, Y.; Sankawa, U. !$#submission submitted to JIPID, May 1991 !$#accession JQ0911 !'##molecule_type DNA !'##residues 1-389 ##label NAK REFERENCE JC4539 !$#authors Nakajima, O.; Shibuya, M.; Hakamatsuka, T.; Noguchi, H.; !1Ebizuka, Y.; Sankawa, U. !$#journal Biol. Pharm. Bull. (1996) 19:71-76 !$#title cDNA and genomic DNA clonings of chalcone synthase from !1Pueraria lobata. !$#cross-references MUID:96418130; PMID:8820915 !$#accession JC4539 !'##molecule_type mRNA !'##residues 1-389 ##label NA2 COMMENT This enzyme plays a central role in the biosynthesis of all !1classes of flavonoids in plants. COMMENT This enzyme catalyzes the formation of chalcone from !1p-coumaroyl and malonyl CoAs, and is the key !1pathway-specific enzyme in flavonoid biosynthesis. This !1enzyme is regarded as the metabolic regulatory point in !1isoflavonoidphytoalexin biosynthesis. GENETICS !$#gene chs CLASSIFICATION #superfamily chalcone synthase KEYWORDS acyltransferase; coenzyme A; flavonoid biosynthesis SUMMARY #length 389 #molecular-weight 42832 #checksum 9268 SEQUENCE /// ENTRY SYSYCN #type complete TITLE naringenin-chalcone synthase (EC 2.3.1.74) 2 - soybean ORGANISM #formal_name Glycine max #common_name soybean DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 05-May-2000 ACCESSIONS S16338; S10475 REFERENCE S16338 !$#authors Akada, S.; Kung, S.D.; Dube, S.K. !$#journal Nucleic Acids Res. (1990) 18:3398 !$#title Nucleotide sequence of one member of soybean chalcone !1synthase multi-gene family. !$#cross-references MUID:90287722; PMID:2356130 !$#accession S16338 !'##molecule_type DNA !'##residues 1-388 ##label AKA !'##cross-references EMBL:X52097; NID:g18751; PIDN:CAA36317.1; !1PID:g295803 GENETICS !$#gene chs !$#introns 60/1 CLASSIFICATION #superfamily chalcone synthase KEYWORDS acyltransferase; coenzyme A; flavonoid biosynthesis SUMMARY #length 388 #molecular-weight 42504 #checksum 6629 SEQUENCE /// ENTRY SYSYC1 #type complete TITLE naringenin-chalcone synthase (EC 2.3.1.74) 1 - soybean ORGANISM #formal_name Glycine max #common_name soybean DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 05-May-2000 ACCESSIONS S15006 REFERENCE S15006 !$#authors Akada, S.; Kung, S.D.; Dube, S.K. !$#journal Plant Mol. Biol. (1991) 16:751-752 !$#title The nucleotide sequence of gene 1 of the soybean chalcone !1synthase multigene family. !$#cross-references MUID:91329712; PMID:1868209 !$#accession S15006 !'##molecule_type DNA !'##residues 1-388 ##label AKA !'##cross-references EMBL:X54644; NID:g18561; PIDN:CAA38456.1; !1PID:g18562 GENETICS !$#introns 60/1 CLASSIFICATION #superfamily chalcone synthase KEYWORDS acyltransferase; coenzyme A; flavonoid biosynthesis SUMMARY #length 388 #molecular-weight 42516 #checksum 6626 SEQUENCE /// ENTRY SYSYC3 #type complete TITLE naringenin-chalcone synthase (EC 2.3.1.74) 3 - soybean ORGANISM #formal_name Glycine max #common_name soybean DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 05-May-2000 ACCESSIONS S11486 REFERENCE S11486 !$#authors Akada, S.; Kung, S.D.; Dube, S.K. !$#journal Nucleic Acids Res. (1990) 18:5899 !$#title The nucleotide sequence of gene 3 of the soybean chalcone !1synthase multigene family. !$#cross-references MUID:91016949; PMID:2216793 !$#accession S11486 !'##molecule_type DNA !'##residues 1-388 ##label AKA !'##cross-references EMBL:X53958; NID:g18588; PIDN:CAA37909.1; !1PID:g18589 GENETICS !$#introns 60/1 CLASSIFICATION #superfamily chalcone synthase KEYWORDS acyltransferase; coenzyme A; flavonoid biosynthesis SUMMARY #length 388 #molecular-weight 42389 #checksum 6783 SEQUENCE /// ENTRY SYZMCC #type complete TITLE naringenin-chalcone synthase (EC 2.3.1.74) c2 - maize ORGANISM #formal_name Zea mays #common_name maize DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 05-May-2000 ACCESSIONS S16598 REFERENCE S16598 !$#authors Franken, P.; Niesbach-Kloesgen, U.; Weydemann, U.; !1Marechal-Drouard, L.; Saedler, H.; Wienand, U. !$#journal EMBO J. (1991) 10:2605-2612 !$#title The duplicated chalcone synthase genes C2 and Whp (white !1pollen) of Zea mays are independently regulated; evidence !1for translational control of Whp expression by the !1anthocyanin intensifying gene in. !$#cross-references MUID:91330885; PMID:1714383 !$#accession S16598 !'##molecule_type DNA !'##residues 1-400 ##label FRA !'##cross-references EMBL:X60205; NID:g22217; PIDN:CAA42764.1; !1PID:g22218 GENETICS !$#gene c2 !$#map_position 4L !$#introns 64/1 CLASSIFICATION #superfamily chalcone synthase KEYWORDS acyltransferase; coenzyme A; flavonoid biosynthesis SUMMARY #length 400 #molecular-weight 43195 #checksum 462 SEQUENCE /// ENTRY SYZMW1 #type complete TITLE naringenin-chalcone synthase (EC 2.3.1.74) whp1 - maize ORGANISM #formal_name Zea mays #common_name maize DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 05-May-2000 ACCESSIONS S16599 REFERENCE S16598 !$#authors Franken, P.; Niesbach-Kloesgen, U.; Weydemann, U.; !1Marechal-Drouard, L.; Saedler, H.; Wienand, U. !$#journal EMBO J. (1991) 10:2605-2612 !$#title The duplicated chalcone synthase genes C2 and Whp (white !1pollen) of Zea mays are independently regulated; evidence !1for translational control of Whp expression by the !1anthocyanin intensifying gene in. !$#cross-references MUID:91330885; PMID:1714383 !$#accession S16599 !'##molecule_type DNA !'##residues 1-400 ##label FRA !'##cross-references EMBL:X60204; NID:g22511; PIDN:CAA42763.1; !1PID:g22512 GENETICS !$#gene whp1 !$#map_position 2L !$#introns 64/1 CLASSIFICATION #superfamily chalcone synthase KEYWORDS acyltransferase; coenzyme A; flavonoid biosynthesis SUMMARY #length 400 #molecular-weight 43172 #checksum 8339 SEQUENCE /// ENTRY SYPJCD #type complete TITLE naringenin-chalcone synthase (EC 2.3.1.74) D - garden petunia ALTERNATE_NAMES chalcone synthase ORGANISM #formal_name Petunia x hybrida #common_name garden petunia DATE 30-Sep-1991 #sequence_revision 17-Mar-2000 #text_change 21-Jul-2000 ACCESSIONS A72821; JS0312 REFERENCE JS0308 !$#authors Koes, R.E.; Spelt, C.E.; van den Elzen, P.J.M.; Mol, J.N.M. !$#journal Gene (1989) 81:245-257 !$#title Cloning and molecular characterization of the chalcone !1synthase multigene family of Petunia hybrida. !$#cross-references MUID:90034197; PMID:2806915 !$#accession A72821 !'##molecule_type DNA !'##residues 1-419 ##label KOE !'##cross-references GB:X14593; NID:g20528; PIDN:CAA32733.1; PID:g20529 !'##experimental_source strain Violet 30, leaf !$#accession JS0312 !'##molecule_type DNA !'##residues 1-117,'D',119,'H',121-313,'DI',316-419 ##label KO2 !'##note the sequence was revised in GenBank entry PHCHSD, release 114, !1(PIDN:CAA32733.1) COMMENT This enzyme plays a central role in the biosynthesis of all !1classes of flavonoids in plants. GENETICS !$#gene chsD !$#map_position V CLASSIFICATION #superfamily chalcone synthase KEYWORDS acyltransferase; coenzyme A; flavonoid biosynthesis SUMMARY #length 419 #molecular-weight 45979 #checksum 2327 SEQUENCE /// ENTRY SYPJCF #type complete TITLE naringenin-chalcone synthase (EC 2.3.1.74) F - garden petunia ALTERNATE_NAMES chalcone synthase ORGANISM #formal_name Petunia x hybrida #common_name garden petunia DATE 30-Sep-1991 #sequence_revision 17-Mar-2000 #text_change 05-May-2000 ACCESSIONS B72821; JS0313 REFERENCE JS0308 !$#authors Koes, R.E.; Spelt, C.E.; van den Elzen, P.J.M.; Mol, J.N.M. !$#journal Gene (1989) 81:245-257 !$#title Cloning and molecular characterization of the chalcone !1synthase multigene family of Petunia hybrida. !$#cross-references MUID:90034197; PMID:2806915 !$#accession B72821 !'##molecule_type DNA !'##residues 1-389 ##label KOE !'##cross-references GB:X14594; NID:g20530; PIDN:CAA32734.1; PID:g20531 !'##experimental_source strain Violet 30, leaf !$#accession JS0313 !'##molecule_type DNA !'##residues 1-2,'T',4-33,'S',35-389 ##label KO2 !'##note the sequence was revised in GenBank entry PHCHSD, release 114, !1(PIDN:CAA32734.1) COMMENT This enzyme plays a central role in the biosynthesis of all !1classes of flavonoids in plants. GENETICS !$#gene chsF !$#map_position V !$#note chsF does not appear to be pseudogene, expression of this !1gene could however not be detected in various floral tissues !1nor in seedlings after illumination with UV light CLASSIFICATION #superfamily chalcone synthase KEYWORDS acyltransferase; coenzyme A; flavonoid biosynthesis SUMMARY #length 389 #molecular-weight 42934 #checksum 1272 SEQUENCE /// ENTRY SYPJCG #type complete TITLE naringenin-chalcone synthase (EC 2.3.1.74) G - garden petunia ALTERNATE_NAMES chalcone synthase ORGANISM #formal_name Petunia x hybrida #common_name garden petunia DATE 30-Sep-1991 #sequence_revision 17-Mar-2000 #text_change 05-May-2000 ACCESSIONS C72821; JS0310 REFERENCE JS0308 !$#authors Koes, R.E.; Spelt, C.E.; van den Elzen, P.J.M.; Mol, J.N.M. !$#journal Gene (1989) 81:245-257 !$#title Cloning and molecular characterization of the chalcone !1synthase multigene family of Petunia hybrida. !$#cross-references MUID:90034197; PMID:2806915 !$#accession C72821 !'##molecule_type DNA !'##residues 1-393 ##label KOE !'##cross-references GB:X14595; NID:g20532; PIDN:CAA32735.1; PID:g20533 !'##experimental_source strain Violet 30, leaf !$#accession JS0310 !'##molecule_type DNA !'##residues 1-111,'E',113-150,'L',152-393 ##label KO2 !'##note the sequence is revised in GenBank entry PHCHSG, release 114, !1(PIDN:CAA32735.1) COMMENT This enzyme plays a central role in the biosynthesis of all !1classes of flavonoids in plants. GENETICS !$#gene chsG !$#map_position II !$#note chsG is expressed in seedlings after illumination with UV !1light, no expression detectable in flowers, it is not known !1for sure wether chsG encodes a chalcone synthase or a very !1closely related condensing enzyme CLASSIFICATION #superfamily chalcone synthase KEYWORDS acyltransferase; coenzyme A; flavonoid biosynthesis SUMMARY #length 393 #molecular-weight 42827 #checksum 827 SEQUENCE /// ENTRY SYPJCB #type complete TITLE naringenin-chalcone synthase (EC 2.3.1.74) B - garden petunia ALTERNATE_NAMES chalcone synthase ORGANISM #formal_name Petunia x hybrida #common_name garden petunia DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 05-May-2000 ACCESSIONS JS0311 REFERENCE JS0308 !$#authors Koes, R.E.; Spelt, C.E.; van den Elzen, P.J.M.; Mol, J.N.M. !$#journal Gene (1989) 81:245-257 !$#title Cloning and molecular characterization of the chalcone !1synthase multigene family of Petunia hybrida. !$#cross-references MUID:90034197; PMID:2806915 !$#accession JS0311 !'##molecule_type DNA !'##residues 1-392 ##label KOE !'##cross-references GB:X14592; NID:g20526; PIDN:CAA32732.1; PID:g20527 !'##experimental_source strain Violet 30, leaf COMMENT This enzyme plays a central role in the biosynthesis of all !1classes of flavonoids in plants. GENETICS !$#gene chsB !$#map_position V !$#note chsB is expressed at low level in seedlings after !1illumination with UV light. No expression in flowers or !1tissue culture CLASSIFICATION #superfamily chalcone synthase KEYWORDS acyltransferase; coenzyme A; flavonoid biosynthesis SUMMARY #length 392 #molecular-weight 42956 #checksum 8913 SEQUENCE /// ENTRY SYNPHS #type fragment TITLE trihydroxystilbene synthase (EC 2.3.1.95) - peanut (fragment) ALTERNATE_NAMES resveratrol synthase ORGANISM #formal_name Arachis hypogaea #common_name peanut DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 05-May-2000 ACCESSIONS S09062 REFERENCE S00334 !$#authors Schroeder, G.; Brown, J.W.S.; Schroeder, J. !$#journal Eur. J. Biochem. (1988) 172:161-169 !$#title Molecular analysis of resveratrol synthase. cDNA, genomic !1clones and relationship with chalcone synthase. !$#cross-references MUID:88151982; PMID:2450022 !$#accession S09062 !'##molecule_type mRNA !'##residues 1-313 ##label SCH !'##experimental_source clone pGSC2 COMMENT This enzyme, a dimer of identical chains, catalyzes the !1formation of resveratrol from coumaroyl-CoA and malonyl-CoA; !1it is involved in the synthesis of stilbene-type !1phytoalexins. CLASSIFICATION #superfamily chalcone synthase KEYWORDS acyltransferase; coenzyme A; phytoalexin biosynthesis SUMMARY #length 313 #checksum 7686 SEQUENCE /// ENTRY A48897 #type complete TITLE aminoglycoside N6'-acetyltransferase (EC 2.3.1.-) Ic - Serratia marcescens ALTERNATE_NAMES AAC(6')-Ic; aminoglycoside resistance protein ORGANISM #formal_name Serratia marcescens DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A48897 REFERENCE A48897 !$#authors Shaw, K.J.; Rather, P.N.; Sabatelli, F.J.; Mann, P.; !1Munayyer, H.; Mierzwa, R.; Petrikkos, G.L.; Hare, R.S.; !1Miller, G.H.; Bennett, P.; Downey, P. !$#journal Antimicrob. Agents Chemother. (1992) 36:1447-1455 !$#title Characterization of the chromosomal aac(6')-Ic gene from !1Serratia marcescens. !$#cross-references MUID:92378239; PMID:1354954 !$#accession A48897 !'##status preliminary !'##molecule_type DNA !'##residues 1-146 ##label SHA !'##cross-references GB:M94066; NID:g152813; PIDN:AAA26549.1; !1PID:g152814 !'##note sequence extracted from NCBI backbone (NCBIN:111788, !1NCBIP:111789) CLASSIFICATION #superfamily 6'-N-acetyltransferase KEYWORDS acyltransferase SUMMARY #length 146 #molecular-weight 16281 #checksum 6996 SEQUENCE /// ENTRY A57788 #type complete TITLE enoyl-[acyl-carrier-protein] reductase (NADPH2, B-specific) (EC 1.3.1.10) (version 1) - human CONTAINS 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase (EC 4.2.1.61); 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100); 3-oxoacyl-[acyl-carrier-protein] synthase (EC 2.3.1.41); enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific) (EC 1.3.1.10); oleoyl-[acyl-carrier-protein] hydrolase (EC 3.1.2.14); [acyl-carrier-protein] S-acetyltransferase (EC 2.3.1.38); [acyl-carrier-protein] S-malonyltransferase (EC 2.3.1.39) ORGANISM #formal_name Homo sapiens #common_name man DATE 23-Feb-1996 #sequence_revision 10-Jul-1998 #text_change 03-Jun-2002 ACCESSIONS A57788; B57788 REFERENCE A57788 !$#authors Jayakumar, A.; Tai, M.H.; Huang, W.Y.; al-Feel, W.; Hsu, M.; !1Abu-Elheiga, L.; Chirala, S.S.; Wakil, S.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1995) 92:8695-8699 !$#title Human fatty acid synthase: properties and molecular cloning. !$#cross-references MUID:96004605; PMID:7567999 !$#accession A57788 !'##status preliminary !'##molecule_type mRNA !'##residues 1-2504 ##label JAY1 !'##cross-references EMBL:U26644; NID:g1049052; PIDN:AAC50259.1; !1PID:g1049053 !$#accession B57788 !'##status preliminary !'##molecule_type mRNA !'##residues 1-1297,'TPTQDASSLSSLSYQQVA',1316-2504 ##label JAY2 GENETICS !$#gene GDB:FASN !'##cross-references GDB:342064; OMIM:600212 !$#map_position 17q25-17q25 CLASSIFICATION #superfamily rat fatty-acid synthase; !13-oxoacyl-[acyl-carrier-protein] synthase I homology; acyl !1carrier protein homology; long-chain alcohol dehydrogenase !1homology; oleoyl-[acyl-carrier-protein] hydrolase homology; !1short-chain alcohol dehydrogenase homology; !1[acyl-carrier-protein] S-malonyltransferase homology KEYWORDS acyltransferase; carbon-oxygen lyase; carrier protein; !1coenzyme A; fatty acid biosynthesis; hydro-lyase; mammary !1gland; NADP; oxidoreductase; phosphopantetheine; !1phosphoprotein; thiolester hydrolase FEATURE !$22-403 #domain 3-oxoacyl-[acyl-carrier-protein] synthase I !8homology #label OAS\ !$492-773 #domain [acyl-carrier-protein] S-malonyltransferase !8homology #label AMT\ !$1315-1333 #region catalytic (of !83-hydroxypalmitoyl-[acyl-carrier-protein] !8dehydratase) #status predicted\ !$1545-1849 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$1664-1694 #region beta-alpha-beta NADP nucleotide-binding fold\ !$1879-2061 #domain short-chain alcohol dehydrogenase homology !8#label SADH\ !$2116-2186 #domain acyl carrier protein homology #label ACP\ !$2212-2504 #domain oleoyl-[acyl-carrier-protein] hydrolase !8#status predicted #label ENZ7\ !$2228-2480 #domain oleoyl-[acyl-carrier-protein] hydrolase !8homology #label ACPH\ !$161 #active_site Cys (of 3-oxoacyl-[acyl-carrier-protein] !8synthase) #status predicted\ !$580 #active_site Ser (covalent substrate-binding) (of !8[acyl-carrier-protein] S-malonyltransferase) #status !8predicted\ !$1696,1699 #active_site Ser, Lys (of !8enoyl-[acyl-carrier-protein] reductase) #status !8predicted\ !$1921 #active_site Lys (of 3-oxoacyl-[acyl-carrier-protein] !8reductase) #status predicted\ !$2151 #binding_site phosphopantetheine (Ser) (covalent) !8#status predicted\ !$2302 #active_site Ser (of oleoyl-[acyl-carrier-protein] !8hydrolase) #status predicted SUMMARY #length 2504 #molecular-weight 273100 #checksum 9338 SEQUENCE /// ENTRY XYRTFA #type complete TITLE enoyl-[acyl-carrier-protein] reductase (NADPH2, B-specific) (EC 1.3.1.10) - rat CONTAINS 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase (EC 4.2.1.61); 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100); 3-oxoacyl-[acyl-carrier-protein] synthase (EC 2.3.1.41); enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific) (EC 1.3.1.10); oleoyl-[acyl-carrier-protein] hydrolase (EC 3.1.2.14); [acyl-carrier-protein] S-acetyltransferase (EC 2.3.1.38); [acyl-carrier-protein] S-malonyltransferase (EC 2.3.1.39) ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Jun-2002 ACCESSIONS A30313; A30443; A38188; S30447; S30446; S03429; S00021; !1A30444; A29933; A60919 REFERENCE A30313 !$#authors Amy, C.M.; Witkowski, A.; Naggert, J.; Williams, B.; !1Randhawa, Z.; Smith, S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:3114-3118 !$#title Molecular cloning and sequencing of cDNAs encoding the !1entire rat fatty acid synthase. !$#cross-references MUID:89240686; PMID:2717611 !$#accession A30313 !'##molecule_type mRNA !'##residues 1-2505 ##label AMY !'##cross-references GB:M76767; GB:X14175; NID:g204094; PIDN:AAA57219.1; !1PID:g204095 !$#accession A30443 !'##molecule_type protein !'##residues 2-10,'X',12-13;33-34,'XX',37-42;76-85;133-139;141-145,'X', !1147-150;202-213;330-338;432-436;454-463;466-467,'X', !1469-475;500-504;571-580;621-626,'X', !1628-630;688-698;786-798;1035-1042;1146-1152;1236-1245; !11261-1280;1282-1291,'X',1293-1297;1328-1339;'X', !11341-1354;1440-1449;1497-1506;1572-1581;1593-1600;1777-1786; !11838-1847;1859-1868;1968-1974,'X',1976-1983;2036,'X',2038, !1'X',2040-2045;2068-2077;2087-2096;2154-2162;2186-2193,'X', !12195 ##label AM2 REFERENCE A38188 !$#authors Amy, C.M.; Williams-Ahlf, B.; Naggert, J.; Smith, S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:1105-1108 !$#title Intron-exon organization of the gene for the multifunctional !1animal fatty acid synthase. !$#cross-references MUID:92141210; PMID:1736293 !$#accession A38188 !'##molecule_type DNA !'##residues 1-183,'T',185-2295,'Y',2297-2505 ##label AM3 !'##cross-references GB:M84761; NID:g204098; PIDN:AAA41145.1; !1PID:g204099 !'##note only intron/exon boundaries are shown REFERENCE S30446 !$#authors Beck, K.F.; Schreglmann, R.; Stathopulos, I.; Klein, H.; !1Hoch, J.; Schweizer, M. !$#journal DNA Seq. (1992) 2:359-386 !$#title The fatty acid synthase (FAS) gene and its promoter in !1Rattus norvegicus. !$#cross-references MUID:93075999; PMID:1339331 !$#accession S30447 !'##molecule_type DNA !'##residues 1-821 ##label BEC !'##cross-references EMBL:X56694; NID:g57883; PID:g57884 !$#accession S30446 !'##molecule_type mRNA !'##residues 1-2105,'A',2107-2295,'Y',2297-2505 ##label BE2 !'##cross-references EMBL:X62888; NID:g57889; PIDN:CAA44679.1; !1PID:g57890 REFERENCE S03429 !$#authors Schweizer, M.; Takabayashi, K.; Laux, T.; Beck, K.F.; !1Schreglmann, R. !$#journal Nucleic Acids Res. (1989) 17:567-586 !$#title Rat mammary gland fatty acid synthase: localization of the !1constituent domains and two functional polyadenylation/ !1termination signals in the cDNA. !$#cross-references MUID:89128431; PMID:2915923 !$#accession S03429 !'##molecule_type mRNA !'##residues 75-870,'P',872-2105,'A',2107-2295,'Y',2297-2505 ##label SCH !'##cross-references EMBL:X13415; NID:g56132; PIDN:CAA31780.1; !1PID:g56133 !'##note 410-Arg was also found REFERENCE S00021 !$#authors Witkowski, A.; Naggert, J.; Mikkelsen, J.; Smith, S. !$#journal Eur. J. Biochem. (1987) 165:601-606 !$#title Molecular cloning and sequencing of a cDNA encoding the acyl !1carrier protein and its flanking domains in the mammalian !1fatty acid synthetase. !$#cross-references MUID:87246646; PMID:3109907 !$#accession S00021 !'##molecule_type mRNA !'##residues 1921-1966,'IL',1969-2324 ##label WIT !'##cross-references EMBL:X13527 !$#accession A30444 !'##molecule_type protein !'##residues 2258-2278 ##label WI2 REFERENCE A29933 !$#authors Naggert, J.; Witkowski, A.; Mikkelsen, J.; Smith, S. !$#journal J. Biol. Chem. (1988) 263:1146-1150 !$#title Molecular cloning and sequencing of a cDNA encoding the !1thioesterase domain of the rat fatty acid synthetase. !$#cross-references MUID:88087240; PMID:2891707 !$#accession A29933 !'##molecule_type mRNA !'##residues 'P',2086-2105,'A',2107-2505 ##label NAG REFERENCE A60919 !$#authors Clarke, S.D.; Armstrong, M.K.; Jump, D.B. !$#journal J. Nutr. (1990) 120:218-224 !$#title Nutritional control of rat liver fatty acid synthase and S14 !1mRNA abundance. !$#cross-references MUID:90188542; PMID:2313386 !$#accession A60919 !'##molecule_type mRNA !'##residues 2377-2413 ##label CLA GENETICS !$#introns 43/1; 94/1; 152/1; 219/1; 260/1; 298/3; 343/3; 498/1; 560/3; !1624/1; 655/3; 700/3; 768/3; 807/2; 865/1; 929/1; 956/1; !11016/1; 1076/1; 1144/1; 1239/3; 1368/3; 1423/3; 1463/2; !11515/1; 1584/1; 1634/2; 1694/1; 1734/1; 1775/1; 1849/3; !11917/1; 1967/3; 1998/2; 2049/1; 2131/1; 2194/1; 2270/1; !12343/3; 2376/3; 2460/3 CLASSIFICATION #superfamily rat fatty-acid synthase; !13-oxoacyl-[acyl-carrier-protein] synthase I homology; acyl !1carrier protein homology; long-chain alcohol dehydrogenase !1homology; oleoyl-[acyl-carrier-protein] hydrolase homology; !1short-chain alcohol dehydrogenase homology; !1[acyl-carrier-protein] S-malonyltransferase homology KEYWORDS acyltransferase; carbon-oxygen lyase; carrier protein; !1coenzyme A; fatty acid biosynthesis; homodimer; hydro-lyase; !1mammary gland; NADP; oxidoreductase; phosphopantetheine; !1phosphoprotein; thiolester hydrolase FEATURE !$22-404 #domain 3-oxoacyl-[acyl-carrier-protein] synthase I !8homology #label OAS\ !$493-775 #domain [acyl-carrier-protein] S-malonyltransferase !8homology #label AMT\ !$1312-1330 #region catalytic (of !83-hydroxypalmitoyl-[acyl-carrier-protein] !8dehydratase) #status predicted\ !$1543-1840 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$1663-1693 #region beta-alpha-beta NADP nucleotide-binding fold\ !$1879-2061 #domain short-chain alcohol dehydrogenase homology !8#label SADH\ !$2116-2186 #domain acyl carrier protein homology #label ACP\ !$2211-2505 #domain oleoyl-[acyl-carrier-protein] hydrolase !8#status predicted #label ENZ7\ !$2227-2480 #domain oleoyl-[acyl-carrier-protein] hydrolase !8homology #label ACPH\ !$161 #active_site Cys (of 3-oxoacyl-[acyl-carrier-protein] !8synthase) #status predicted\ !$581 #active_site Ser (covalent substrate-binding) (of !8[acyl-carrier-protein] S-malonyltransferase) #status !8predicted\ !$1695,1698 #active_site Ser, Lys (of !8enoyl-[acyl-carrier-protein] reductase) #status !8predicted\ !$1921 #active_site Lys (of 3-oxoacyl-[acyl-carrier-protein] !8reductase) #status predicted\ !$2151 #binding_site phosphopantetheine (Ser) (covalent) !8#status predicted\ !$2302 #active_site Ser (of oleoyl-[acyl-carrier-protein] !8hydrolase) #status predicted SUMMARY #length 2505 #molecular-weight 272649 #checksum 81 SEQUENCE /// ENTRY XYCHFA #type complete TITLE enoyl-[acyl-carrier-protein] reductase (NADPH2, B-specific) (EC 1.3.1.10) - chicken CONTAINS 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase (EC 4.2.1.61); 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100); 3-oxoacyl-[acyl-carrier-protein] synthase (EC 2.3.1.41); enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific) (EC 1.3.1.10); oleoyl-[acyl-carrier-protein] hydrolase (EC 3.1.2.14); [acyl-carrier-protein] S-acetyltransferase (EC 2.3.1.38); [acyl-carrier-protein] S-malonyltransferase (EC 2.3.1.39) ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Sep-1991 #sequence_revision 12-Apr-1996 #text_change 03-Jun-2002 ACCESSIONS S57248; S51519; A30620; A29967; A33918; A30445; A31236; !1B31236; A30297; A31184; A31185; A30446; S03856; A32015; !1S57249 REFERENCE S57248 !$#authors Huang, W.Y.; Chirala, S.S.; Wakil, S.J. !$#submission submitted to the EMBL Data Library, January 1989 !$#description Amino-terminal blocking group and sequence of the animal !1fatty acid synthase. !$#accession S57248 !'##molecule_type mRNA !'##residues 1-2512 ##label HUA1 !'##cross-references EMBL:J04485; NID:g460908; PIDN:AAB46389.1; !1PID:g460907 REFERENCE S51519 !$#authors Huang, W.Y.; Chirala, S.S.; Wakil, S.J. !$#journal Arch. Biochem. Biophys. (1994) 314:45-49 !$#title Amino-terminal blocking group and sequence of the animal !1fatty acid synthase. !$#cross-references MUID:95031085; PMID:7944406 !$#accession S51519 !'##molecule_type mRNA !'##residues 1-182 ##label HUA2 !'##cross-references EMBL:J04485; NID:g460908 !$#accession A30620 !'##molecule_type protein !'##residues 1-12 ##label HUA3 !'##note determination of acetylated amino end REFERENCE A29967 !$#authors Chang, S.I.; Hammes, G.G. !$#journal Biochemistry (1988) 27:4753-4760 !$#title Amino acid sequences of substrate-binding sites in chicken !1liver fatty acid synthase. !$#cross-references MUID:89000676; PMID:3167014 !$#accession A29967 !'##molecule_type protein !'##residues 144-166;575-583;2141-2165 ##label CHA1 REFERENCE A33918 !$#authors Holzer, K.P.; Liu, W.; Hammes, G.G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:4387-4391 !$#title Molecular cloning and sequencing of chicken liver fatty acid !1synthase cDNA. !$#cross-references MUID:89282777; PMID:2734291 !$#accession A33918 !'##molecule_type mRNA !'##residues 75-77,'PV',80-116,'A',118-675,'S',677-1169,'N',1171-1178, !1'T',1180-1191,'H',1193-1198,'L',1200-1286,'ND',1289-1372, !1'E',1374-1533,'Y',1535-1577,'R',1579-1732,'E',1734-1745,'N', !11747-1775 ##label HOL !$#accession A30445 !'##molecule_type protein !'##residues 107-113;1086-1091 ##label HOL1 REFERENCE A31236 !$#authors Yuan, Z.; Liu, W.; Hammes, G.G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:6328-6331 !$#title Molecular cloning and sequencing of DNA complementary to !1chicken liver fatty acid synthase mRNA. !$#cross-references MUID:88320436; PMID:2842766 !$#accession A31236 !'##molecule_type mRNA !'##residues 1752-2350,'CFSFSLFQ',2351-2512 ##label YUA1 !$#accession B31236 !'##molecule_type mRNA !'##residues 1752-2512 ##label YUA2 !'##cross-references GB:J03860; GB:M22987; NID:g211766 !'##note neither the complete nucleic acid sequence nor the complete !1translation are shown REFERENCE A30297 !$#authors Chirala, S.S.; Kasturi, R.; Pazirandeh, M.; Stolow, D.T.; !1Huang, W.Y.; Wakil, S.J. !$#journal J. Biol. Chem. (1989) 264:3750-3757 !$#title A novel cDNA extension procedure. Isolation of chicken fatty !1acid synthase cDNA clones. !$#cross-references MUID:89139426; PMID:2917973 !$#accession A30297 !'##molecule_type mRNA !'##residues 1568-2512 ##label CHI !'##cross-references EMBL:J04485; NID:g460908 !'##note neither the complete nucleic acid sequence nor the complete !1translation are shown REFERENCE A31184 !$#authors Yang, C.Y.; Huang, W.Y.; Chirala, S.; Wakil, S.J. !$#journal Biochemistry (1988) 27:7773-7777 !$#title Complete amino acid sequence of the thioesterase domain of !1chicken liver fatty acid synthase. !$#cross-references MUID:89088151; PMID:3207709 !$#accession A31184 !'##molecule_type protein !'##residues 2209-2508 ##label YAN REFERENCE A31185 !$#authors Kasturi, R.; Chirala, S.; Pazirandeh, M.; Wakil, S.J. !$#journal Biochemistry (1988) 27:7778-7785 !$#title Characterization of a genomic and cDNA clone coding for the !1thioesterase domain and 3' noncoding region of the chicken !1liver fatty acid synthase gene. !$#cross-references MUID:89088152; PMID:3207710 !$#accession A31185 !'##molecule_type DNA !'##residues 2202-2512 ##label KAS1 !'##cross-references EMBL:J02839; NID:g211768; PIDN:AAA82106.1; !1PID:g211769 !$#accession A30446 !'##molecule_type mRNA !'##residues 2202-2512 ##label KAS2 !'##cross-references EMBL:J02839; NID:g211768 !'##note the translated sequence in GenBank entry CHKFASA, release !1113.0, PIDN:AAA82106.1, PID:g211769, differs from the !1published sequence in lacking residues 2202-2350 preceeding !1intron "n-2" as shown in Fig. 5 REFERENCE S03856 !$#authors Huang, W.Y.; Stoops, J.K.; Wakil, S.J. !$#journal Arch. Biochem. Biophys. (1989) 270:92-98 !$#title Complete amino acid sequence of chicken liver acyl carrier !1protein derived from the fatty acid synthase. !$#cross-references MUID:89192401; PMID:2648999 !$#accession S03856 !'##molecule_type protein !'##residues 2121-2209 ##label HUA4 REFERENCE A32015 !$#authors Chang, S.I.; Hammes, G.G. !$#journal Biochemistry (1989) 28:3781-3788 !$#title Amino acid sequences of pyridoxal 5'-phosphate binding sites !1and fluorescence resonance energy transfer in chicken liver !1fatty acid synthase. !$#cross-references MUID:89323081; PMID:2751995 !$#accession A32015 !'##molecule_type protein !'##residues 667-675;1699-1709 ##label CHA2 !'##note the binding of pyridoxal 5'-phosphate to Lys-1708 competitively !1inhibits the binding of NADPH FUNCTION HPD !$#description as 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase (EC !14.2.1.61) catalyzes the dehydration !1(3R)-3-hydroxyacyl-[acyl-carrier-protein] to (E)-2, !13-dehydroacyl-[acyl-carrier-protein] !$#pathway fatty acid biosynthesis !$#note this activity is specific for C12 to C16 acyl compounds FUNCTION OAR !$#description as 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100) !1catalyzes the reversible reaction of !13-oxoacyl-[acyl-carrier-protein] with NADPH and a proton to !1produce (3R)-3-hydroxyacyl-[acyl-carrier-protein] and NADP+ !$#pathway fatty acid biosynthesis FUNCTION OAS !$#description as 3-oxoacyl-[acyl-carrier-protein] synthase (EC 2.3.1.41) !1catalyzes the irreversible reaction of !1malonyl-[acyl-carrier-protein] with !1acyl-[acyl-carrier-protein] to produce !13-oxoacyl-[acyl-carrier-protein], acyl-carrier-protein and !1carbon dioxide !$#pathway fatty acid biosynthesis FUNCTION EAR !$#description as enoyl-[acyl-carrier-protein] reductase (NADPH, !1B-specific) (EC 1.3.1.10) catalyzes the reaction of (E)-2, !13-dehydroacyl-[acyl-carrier-protein] with NADPH and a proton !1to produce acyl-[acyl-carrier-protein] and NADP+ !$#pathway fatty acid biosynthesis FUNCTION HYD !$#description as oleoyl-[acyl-carrier-protein] hydrolase (EC 3.1.2.14) !1catalyzes the hydrolysis of oleoyl-[acyl-carrier-protein] to !1oleoate and acyl-carrier-protein !$#pathway fatty acid biosynthesis FUNCTION SAT !$#description as [acyl-carrier-protein] S-acetyltransferase (EC 2.3.1.38) !1catalyzes the reversible reaction of acetyl-CoA with !1acyl-carrier-protein to produce !1acetyl-[acyl-carrier-protein] and coenzyme A !$#pathway fatty acid biosynthesis FUNCTION SMT !$#description as [acyl-carrier-protein] S-malonyltransferase (EC 2.3.1.39) !1catalyzes the reversible reaction of malonyl-CoA with !1acyl-carrier-protein to produce !1malonyl-[acyl-carrier-protein] and coenzyme A !$#pathway fatty acid biosynthesis CLASSIFICATION #superfamily rat fatty-acid synthase; !13-oxoacyl-[acyl-carrier-protein] synthase I homology; acyl !1carrier protein homology; long-chain alcohol dehydrogenase !1homology; oleoyl-[acyl-carrier-protein] hydrolase homology; !1short-chain alcohol dehydrogenase homology; !1[acyl-carrier-protein] S-malonyltransferase homology KEYWORDS acetylated amino end; acyltransferase; alternative splicing; !1carbon-oxygen lyase; carrier protein; coenzyme A; fatty acid !1biosynthesis; homodimer; hydro-lyase; multifunctional !1enzyme; NADP; oxidoreductase; phosphopantetheine; !1phosphoprotein; thiolester hydrolase FEATURE !$1-2512 #product fatty-acid synthase, splice form 1 #status !8predicted #label MAT1\ !$1-2350,'CFSFSLFQ', !$2351-2512 #product fatty-acid synthase, splice form 2 #status !8predicted #label MAT2\ !$22-404 #domain 3-oxoacyl-[acyl-carrier-protein] synthase I !8homology #label OASH\ !$492-774 #domain [acyl-carrier-protein] S-malonyltransferase !8homology #label AMT\ !$1322-1340 #region catalytic (of !83-hydroxypalmitoyl-[acyl-carrier-protein] !8dehydratase) #status predicted\ !$1554-1858 #domain long-chain alcohol dehydrogenase homology !8#label LADH\ !$1675-1704 #region beta-alpha-beta NADP nucleotide-binding fold\ !$1888-2070 #domain short-chain alcohol dehydrogenase homology !8#label SADH\ !$2123-2193 #domain acyl carrier protein homology #label ACP\ !$2234-2487 #domain oleoyl-[acyl-carrier-protein] hydrolase !8homology #label ACPH\ !$1 #modified_site acetylated amino end (Met) #status !8experimental\ !$161 #active_site Cys #link OAS #status predicted\ !$580 #active_site Ser #link SAT, SMT #status predicted\ !$1705,1708 #active_site Ser, Lys #link EAR #status predicted\ !$1930 #active_site Lys #link OAR #status predicted\ !$2158 #binding_site phosphopantetheine (Ser) (covalent) !8#status predicted\ !$2309 #active_site Ser #link HYD #status predicted SUMMARY #length 2512 #molecular-weight 274779 #checksum 6791 SEQUENCE /// ENTRY S01787 #type complete TITLE fatty-acid synthase (EC 2.3.1.85) - Penicillium griseofulvum ALTERNATE_NAMES fatty acid synthetase ORGANISM #formal_name Penicillium griseofulvum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-May-2000 ACCESSIONS S01787 REFERENCE S01787 !$#authors Wiesner, P.; Beck, J.; Beck, K.F.; Ripka, S.; Mueller, G.; !1Luecke, S.; Schweizer, E. !$#journal Eur. J. Biochem. (1988) 177:69-79 !$#title Isolation and sequence analysis of the fatty acid synthetase !1FAS2 gene from Penicillium patulum. !$#cross-references MUID:89030697; PMID:3053172 !$#accession S01787 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-1857 ##label WIE !'##cross-references GB:M37461; NID:g169179; PIDN:AAA33695.1; !1PID:g169180 !'##note the source is designated as Penicillium patulum GENETICS !$#gene fas2 CLASSIFICATION #superfamily yeast fatty-acid synthase KEYWORDS acyltransferase; coenzyme A SUMMARY #length 1857 #molecular-weight 204464 #checksum 4992 SEQUENCE /// ENTRY JC4086 #type complete TITLE fatty-acid synthase (EC 2.3.1.85) alpha chain - yeast (Candida albicans) ORGANISM #formal_name Candida albicans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-May-2000 ACCESSIONS JC4086 REFERENCE JC4086 !$#authors Southard, S.B.; Cihlar, R.L. !$#journal Gene (1995) 156:133-138 !$#title Analysis and expression of the Candida albicans FAS2 gene. !$#cross-references MUID:95255657; PMID:7737507 !$#accession JC4086 !'##molecule_type DNA !'##residues 1-1885 ##label SOU !'##cross-references GB:L29063; NID:g456442; PIDN:AAA34345.1; !1PID:g456443 GENETICS !$#gene fas2 !$#map_position 3 CLASSIFICATION #superfamily yeast fatty-acid synthase KEYWORDS acyltransferase; coenzyme A; fatty acid biosynthesis; !1phosphopantetheine; phosphoprotein FEATURE !$1299-1304 #region cerulenin binding #status predicted\ !$181 #binding_site phosphopantetheine (Ser) (covalent) !8#status predicted SUMMARY #length 1885 #molecular-weight 207588 #checksum 7273 SEQUENCE /// ENTRY XNECSD #type complete TITLE 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase (EC 2.3.1.117) - Escherichia coli (strain K-12) ALTERNATE_NAMES succinyldiaminopimelate aminotransferase; succinyldiaminopimelate transferase; tetrahydrodipicolinate N-succinyltransferase ORGANISM #formal_name Escherichia coli DATE 13-Aug-1986 #sequence_revision 17-Oct-1997 #text_change 03-Jun-2002 ACCESSIONS F64740; A00601; S45231; S36255; S31963 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64740 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-274 ##label BLAT !'##cross-references GB:AE000126; GB:U00096; NID:g1786358; !1PIDN:AAC73277.1; PID:g1786362; UWGP:b0166 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A00601 !$#authors Richaud, C.; Richaud, F.; Martin, C.; Haziza, C.; Patte, !1J.C. !$#journal J. Biol. Chem. (1984) 259:14824-14828 !$#title Regulation of expression and nucleotide sequence of the !1Escherichia coli dapD gene. !$#cross-references MUID:85054973; PMID:6094577 !$#accession A00601 !'##molecule_type DNA !'##residues 1-30,'D',32-162,'R',164-176,'M',178-189,'L',191-274 ##label !1RIC !'##cross-references GB:K02970; NID:g145711; PIDN:AAA23667.1; !1PID:g145712 REFERENCE S45181 !$#authors Fujita, N. !$#submission submitted to the EMBL Data Library, January 1994 !$#accession S45231 !'##molecule_type DNA !'##residues 1-274 ##label FUJ !'##cross-references EMBL:D26562; NID:g473770; PIDN:BAA05610.1; !1PID:g473821 !'##experimental_source strain K-12, substrain W3110 REFERENCE S36254 !$#authors van Heeswijk, W.C.; Rabenberg, M.; Westerhoff, H.V.; Kahn, !1D. !$#journal Mol. Microbiol. (1993) 9:443-457 !$#title The genes of the glutamine synthetase adenylylation cascade !1are not regulated by nitrogen in Escherichia coli. !$#cross-references MUID:94018640; PMID:8412694 !$#accession S36255 !'##molecule_type DNA !'##residues 1-14 ##label VAN !'##cross-references EMBL:Z21842 GENETICS !$#gene dapD !$#map_position 4 min CLASSIFICATION #superfamily 2,3,4,5-tetrahydropyridine-2-carboxylate !1N-succinyltransferase KEYWORDS acyltransferase; coenzyme A; diaminopimelate biosynthesis; !1lysine biosynthesis; pyridoxal phosphate SUMMARY #length 274 #molecular-weight 29892 #checksum 8068 SEQUENCE /// ENTRY S18857 #type complete TITLE 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase (EC 2.3.1.117) - Actinobacillus pleuropneumoniae ALTERNATE_NAMES tetrahydrodipicolinate N-succinyltransferase ORGANISM #formal_name Actinobacillus pleuropneumoniae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S18857 REFERENCE S18857 !$#authors Denich, K.; O'Hanley, P.; Lalonde, G. !$#submission submitted to the EMBL Data Library, November 1991 !$#description Cloning and sequence analysis of the DAPD gene from !1Actinobacillus pleuropneumonia. !$#accession S18857 !'##status preliminary !'##molecule_type DNA !'##residues 1-274 ##label DEN !'##cross-references EMBL:X63201; NID:g38946; PIDN:CAA44883.1; !1PID:g38947 CLASSIFICATION #superfamily 2,3,4,5-tetrahydropyridine-2-carboxylate !1N-succinyltransferase KEYWORDS acyltransferase; aminotransferase; coenzyme A; !1diaminopimelate biosynthesis; lysine biosynthesis; pyridoxal !1phosphate SUMMARY #length 274 #molecular-weight 29761 #checksum 6782 SEQUENCE /// ENTRY H64133 #type complete TITLE 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase (EC 2.3.1.117) - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS H64133 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession H64133 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-303 ##label TIGR !'##cross-references GB:U32836; GB:L42023; NID:g1574473; !1PIDN:AAC23279.1; PID:g1574480; TIGR:HI1634 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily 2,3,4,5-tetrahydropyridine-2-carboxylate !1N-succinyltransferase KEYWORDS acyltransferase; coenzyme A; diaminopimelate biosynthesis; !1lysine biosynthesis; pyridoxal phosphate SUMMARY #length 303 #molecular-weight 32817 #checksum 4377 SEQUENCE /// ENTRY XUECDP #type complete TITLE acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase (EC 2.3.1.129) - Escherichia coli (strain K-12) ALTERNATE_NAMES lpxA protein ORGANISM #formal_name Escherichia coli DATE 31-Dec-1988 #sequence_revision 21-Nov-1997 #text_change 03-Jun-2002 ACCESSIONS E64742; C33171; A28389 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64742 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-262 ##label BLAT !'##cross-references GB:AE000127; GB:U00096; NID:g1786370; !1PIDN:AAC73292.1; PID:g1786378; UWGP:b0181 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A33171 !$#authors Coleman, J.; Raetz, C.R.H. !$#journal J. Bacteriol. (1988) 170:1268-1274 !$#title First committed step of lipid A biosynthesis in Escherichia !1coli: sequence of the lpxA gene. !$#cross-references MUID:88139188; PMID:3277952 !$#accession C33171 !'##molecule_type DNA !'##residues 1-63,'SV',66-124,'D',126-262 ##label COL !'##cross-references GB:M19334; NID:g450760; PIDN:AAC36918.1; !1PID:g146661 REFERENCE A91854 !$#authors Crowell, D.N.; Reznikoff, W.S.; Raetz, C.R.H. !$#journal J. Bacteriol. (1987) 169:5727-5734 !$#title Nucleotide sequence of the Escherichia coli gene for lipid A !1disaccharide synthase. !$#cross-references MUID:88058790; PMID:2824445 !$#accession A28389 !'##molecule_type DNA !'##residues 148-262 ##label CRO COMMENT This protein is involved in the biosynthesis of lipid A, a !1phosphorylated glycolipid that anchors the !1lipopolysaccharide to the outer membrane of the E. coli !1cell. It catalyzes the transfer of a beta-hydroxymyristoyl !1moiety from beta-hydroxymyristoyl acylcarrier protein to !1UDP-N-acetylglucosamine. GENETICS !$#gene lpxA !$#map_position 4 min !$#start_codon GTG FUNCTION !$#pathway lipid A biosynthesis CLASSIFICATION #superfamily UDP-N-acetylglucosamine acyltransferase KEYWORDS acyltransferase; lipid A biosynthesis SUMMARY #length 262 #molecular-weight 28080 #checksum 7011 SEQUENCE /// ENTRY EKECEX #type complete TITLE gamma-glutamyltransferase (EC 2.3.2.2) precursor - Escherichia coli (strain K-12) ALTERNATE_NAMES GGT protein; glutamyl transpeptidase CONTAINS gamma-glutamyltransferase large chain; gamma-glutamyltransferase small chain ORGANISM #formal_name Escherichia coli DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 01-Mar-2002 ACCESSIONS JV0028; S47666; B65141; PC4349 REFERENCE JV0028 !$#authors Suzuki, H.; Kumagai, H.; Echigo, T.; Tochikura, T. !$#journal J. Bacteriol. (1989) 171:5169-5172 !$#title DNA sequence of the Escherichia coli K-12 !1gamma-glutamyltranspeptidase gene, ggt. !$#cross-references MUID:89359163; PMID:2570061 !$#accession JV0028 !'##molecule_type DNA !'##residues 1-580 ##label SUZ !'##cross-references EMBL:M28722; NID:g146132; PIDN:AAA23869.1; !1PID:g146133 REFERENCE S47666 !$#authors Plunkett, G. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S47666 !'##status preliminary !'##molecule_type DNA !'##residues 1-361 ##label PLU !'##cross-references EMBL:U00039 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65141 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-580 ##label BLAT !'##cross-references GB:AE000421; GB:U00096; NID:g1789854; !1PIDN:AAC76472.1; PID:g1789856; UWGP:b3447 !'##experimental_source strain K-12, substrain MG1655 REFERENCE PC4349 !$#authors Hashimoto, W.; Suzuki, H.; Yamamoto, K.; Kumagai, H. !$#journal Biosci. Biotechnol. Biochem. (1997) 61:34-39 !$#title Analysis of low temperature inducible mechanism of !1gamma-glutamyltranspeptidase of Escherichia coli K-12. !$#cross-references MUID:97179798; PMID:9028034 !$#accession PC4349 !'##molecule_type DNA !'##residues 1-38 ##label HAS !'##experimental_source K-12 strain MG1655 COMMENT This enzyme catalyzes the transfer of the gamma-glutamyl !1residue from gamma-glutamyl compounds such as glutathione to !1amino acids and peptides. It also catalyzes the hydrolysis !1of gamma-glutamyl compounds; however, its physiological role !1remains unclear. The active enzyme is a dimer of large and !1small chains. GENETICS !$#gene ggt !$#map_position 76 min CLASSIFICATION #superfamily gamma-glutamyltransferase KEYWORDS aminoacyltransferase FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-390 #product gamma-glutamyltransferase large chain !8#status predicted #label CH1\ !$391-580 #product gamma-glutamyltransferase small chain !8#status predicted #label CH2 SUMMARY #length 580 #molecular-weight 61767 #checksum 183 SEQUENCE /// ENTRY EKHUEX #type complete TITLE gamma-glutamyltransferase (EC 2.3.2.2) type 1 precursor [validated] - human ALTERNATE_NAMES glutamyl transpeptidase CONTAINS gamma-glutamyltransferase heavy chain; gamma-glutamyltransferase light chain ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1990 #sequence_revision 01-Dec-1995 #text_change 08-Dec-2000 ACCESSIONS A31253; JS0067; A60439; A48987; A47739; B35074; PS0312; !1PS0313; C45946; S43366; S45638; S45639 REFERENCE A31253 !$#authors Meyts, E.R.D.; Heisterkamp, N.; Groffen, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:8840-8844 !$#title Cloning and nucleotide sequence of human gamma-glutamyl !1transpeptidase. !$#cross-references MUID:89057834; PMID:2904146 !$#accession A31253 !'##molecule_type mRNA !'##residues 1-569 ##label MEY !'##cross-references GB:J04131; NID:g183137; PIDN:AAA52547.1; !1PID:g183138 REFERENCE JS0067 !$#authors Goodspeed, D.C.; Dunn, T.J.; Miller, C.D.; Pitot, H.C. !$#journal Gene (1989) 76:1-9 !$#title Human gamma-glutamyl transpeptidase cDNA: comparison of !1hepatoma and kidney mRNA in the human and rat. !$#cross-references MUID:89306644; PMID:2568315 !$#accession JS0067 !'##molecule_type mRNA !'##residues 1-569 ##label GOO !'##cross-references GB:M24903; NID:g183128; PIDN:AAA52546.1; !1PID:g183129 !'##experimental_source hepatoma REFERENCE A60439 !$#authors Pitot, H.C.; Goodspeed, D.; Dunn, T.; Hendrich, S.; !1Maronpot, R.R.; Moran, S. !$#journal Toxicol. Appl. Pharmacol. (1989) 97:23-34 !$#title Regulation of the expression of some genes for enzymes of !1glutathione metabolism in hepatotoxicity and !1hepatocarcinogenesis. !$#cross-references MUID:89130553; PMID:2563599 !$#accession A60439 !'##molecule_type mRNA !'##residues 1-569 ##label PIT REFERENCE A48987 !$#authors Courtay, C.; Oster, T.; Michelet, F.; Visvikis, A.; !1Diederich, M.; Wellman, M.; Siest, G. !$#journal Biochem. Pharmacol. (1992) 43:2527-2533 !$#title Gamma-glutamyltransferase: nucleotide sequence of the human !1pancreatic cDNA. Evidence for a ubiquitous !1gamma-glutamyltransferase polypeptide in human tissues. !$#cross-references MUID:92337688; PMID:1378736 !$#accession A48987 !'##molecule_type mRNA !'##residues 1-569 ##label COU !'##cross-references EMBL:X60069; NID:g416525; PIDN:CAA42674.1; !1PID:g416526; EMBL:S40064 !'##experimental_source pancreas !'##note sequence extracted from NCBI backbone (NCBIN:108649, !1NCBIP:108650) REFERENCE A47739 !$#authors Wetmore, L.A.; Gerard, C.; Drazen, J.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:7461-7465 !$#title Human lung expresses unique gamma-glutamyl transpeptidase !1transcripts. !$#cross-references MUID:93361468; PMID:7689219 !$#accession A47739 !'##molecule_type mRNA !'##residues 345-569 ##label WET !'##cross-references GB:L20490; NID:g306748; PIDN:AAA02884.1; !1PID:g306749 !'##note this fragment was designated lung gamma-glutamyltransferase !1light chain I REFERENCE A35074 !$#authors Pawlak, A.; Cohen, E.H.; Octave, J.N.; Schweickhardt, R.; !1Wu, S.J.; Bulle, F.; Chikhi, N.; Baik, J.H.; Siegrist, S.; !1Guellaeen, G. !$#journal J. Biol. Chem. (1990) 265:3256-3262 !$#title An alternatively processed mRNA specific for gamma-glutamyl !1transpeptidase in human tissues. !$#cross-references MUID:90153977; PMID:1968061 !$#accession B35074 !'##molecule_type mRNA !'##residues 345-569 ##label PAW !'##cross-references GB:J05235 !'##note this sequence represents the second open reading frame from an !1alternatively spliced mRNA and includes the light chain !1domain; see A35074 for alternative form of heavy chain from !1the same gene REFERENCE JS0210 !$#authors Sakamuro, D.; Yamazoe, M.; Matsuda, Y.; Kangawa, K.; !1Taniguchi, N.; Matsuo, H.; Yoshikawa, H.; Ogasawara, N. !$#journal Gene (1988) 73:1-9 !$#title The primary structure of human gamma-glutamyl !1transpeptidase. !$#cross-references MUID:89211939; PMID:2907498 !$#accession PS0312 !'##molecule_type mRNA !'##residues 'V',2-569 ##label SAK !'##cross-references GB:M24087; NID:g306766; PIDN:AAA35899.1; !1PID:g306767 !$#accession PS0313 !'##molecule_type protein !'##residues 30-49,'X',51-58;381-408 ##label SA2 !'##experimental_source fetal liver !'##note this fragment was designated gamma-glutamyltransferase !1precursor small chain REFERENCE A45946 !$#authors Tate, S.S.; Khadse, V.; Wellner, D. !$#journal Arch. Biochem. Biophys. (1988) 262:397-408 !$#title Renal gamma-glutamyl transpeptidases: structural and !1immunological studies. !$#cross-references MUID:88208399; PMID:2896486 !$#accession C45946 !'##molecule_type protein !'##residues 'KS',32-46,'K',48;381-398,'X',400-403 ##label TAT REFERENCE S43366 !$#authors Courtay, C.; Heisterkamp, N.; Siest, G.; Groffen, J. !$#journal Biochem. J. (1994) 297:503-508 !$#title Expression of multiple gamma-glutamyltransferase genes in !1man. !$#cross-references MUID:94153322; PMID:7906515 !$#accession S43366 !'##status preliminary !'##molecule_type DNA !'##residues 414-493 ##label CO2 REFERENCE S45638 !$#authors Thioudellet, C.; Oster, T.; Wellman, M.; Siest, G. !$#journal Eur. J. Biochem. (1994) 222:1009-1016 !$#title Molecular and functional characterization of recombinant !1human gamma-glutamyltransferase. Coupling of its activity to !1glutathione levels in V79 cells. !$#cross-references MUID:94298802; PMID:7913033 !$#accession S45638 !'##status preliminary !'##molecule_type protein !'##residues 30-40 ##label THI !$#accession S45639 !'##status preliminary !'##molecule_type protein !'##residues 381-390 ##label TH2 GENETICS !$#gene GDB:GGT1; GGT !'##cross-references GDB:120623; OMIM:231950 !$#map_position 22q11.2-22q12.1 FUNCTION !$#description catalyzes the hydrolysis of glutathione and transfer of the !1gamma-glutamyl residue CLASSIFICATION #superfamily gamma-glutamyltransferase KEYWORDS aminoacyltransferase; glycoprotein FEATURE !$1-29 #domain signal sequence #status predicted #label SIG\ !$30-380 #product gamma-glutamyl transpeptidase heavy chain !8#status experimental #label GTH\ !$381-569 #product gamma-glutamyl transpeptidase light chain !8#status experimental #label GTL\ !$95,120,230,266,297, !$344,511 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 569 #molecular-weight 61382 #checksum 4133 SEQUENCE /// ENTRY S05532 #type complete TITLE gamma-glutamyltransferase (EC 2.3.2.2) - pig ALTERNATE_NAMES gamma-glutamyl transpeptidase ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S05532 REFERENCE S05532 !$#authors Papandrikopoulou, A.; Frey, A.; Gassen, H.G. !$#journal Eur. J. Biochem. (1989) 183:693-698 !$#title Cloning and expression of gamma-glutamyl transpeptidase from !1isolated porcine brain capillaries. !$#cross-references MUID:89377838; PMID:2476308 !$#accession S05532 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-568 ##label PAP !'##cross-references GB:Z46922; NID:g600818; PIDN:CAA87031.1; !1PID:g600819 CLASSIFICATION #superfamily gamma-glutamyltransferase KEYWORDS aminoacyltransferase; glycoprotein; heterodimer; membrane !1protein FEATURE !$1-379 #product gamma-glutamyltransferase heavy chain !8#status predicted #label HCH\ !$380-568 #product gamma-glutamyltransferase light chain !8#status predicted #label LCH SUMMARY #length 568 #molecular-weight 61315 #checksum 3041 SEQUENCE /// ENTRY A05225 #type complete TITLE gamma-glutamyltransferase (EC 2.3.2.2) precursor - rat ALTERNATE_NAMES gamma-glutamyl transpeptidase CONTAINS gamma-glutamyltransferase large chain; gamma-glutamyltransferase small chain ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jun-2000 ACCESSIONS A05225; JS0210; A23539; PS0318; A25154; A37376; A39179; !1S08540; I55400 REFERENCE A05225 !$#authors Matsuda, Y.; Tsuji, A.; Katunuma, N. !$#journal J. Biochem. (1983) 93:1427-1433 !$#title Studies on the structure of gamma-glutamyltranspeptidase !1III. Evidence that the amino terminus of the heavy subunit !1is the membrane binding segment. !$#cross-references MUID:83290784; PMID:6136502 !$#accession A05225 !'##molecule_type protein !'##residues 1-21 ##label MAT REFERENCE JS0210 !$#authors Sakamuro, D.; Yamazoe, M.; Matsuda, Y.; Kangawa, K.; !1Taniguchi, N.; Matsuo, H.; Yoshikawa, H.; Ogasawara, N. !$#journal Gene (1988) 73:1-9 !$#title The primary structure of human gamma-glutamyl !1transpeptidase. !$#cross-references MUID:89211939; PMID:2907498 !$#accession JS0210 !'##molecule_type mRNA !'##residues 64-136 ##label SAK REFERENCE A23539 !$#authors Coloma, J.; Pitot, H.C. !$#journal Nucleic Acids Res. (1986) 14:1393-1403 !$#title Characterization and sequence of a cDNA clone of !1gamma-glutamyltranspeptidase. !$#cross-references MUID:86148480; PMID:2869471 !$#accession A23539 !'##molecule_type mRNA !'##residues 4-65, !1'GPSQACCVWGSLMPTVWASGAASSSPSTTAPHEKLKLSMPVKWLPGWPIPACSIILRTL !1KKEAFQWQFL',135-568 ##label CO0 !'##cross-references GB:X03518; NID:g56209; PIDN:CAA27224.1; !1PID:g1334277 !$#accession PS0318 !'##molecule_type protein !'##residues 380-389 ##label CO2 !'##experimental_source kidney !'##note the large difference in the sequence was caused by a frame !1shift error REFERENCE A25154 !$#authors Laperche, Y.; Bulle, F.; Aissani, T.; Chobert, M.N.; !1Aggerbeck, M.; Hanoune, J.; Guellaen, G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:937-941 !$#title Molecular cloning and nucleotide sequence of rat kidney !1gamma-glutamyl transpeptidase cDNA. !$#cross-references MUID:86149255; PMID:2869484 !$#accession A25154 !'##molecule_type mRNA !'##residues 1-69,'ACCVW',75-80,'VWAS',85,'AASSSPSTTAPHE',99, !1'LKLSMPVKWL',110,'SWPIPACSIILRTLKKEAFQWQFL',135-396,'S', !1398-415,'F',417-443,'L',445-568 ##label LAP !'##experimental_source kidney !'##note the authors translated the codon CAG for residue 241 as Glu REFERENCE A37376 !$#authors Griffiths, S.A.; Manson, M.M. !$#journal Cancer Lett. (1989) 46:69-74 !$#title Rat liver gamma glutamyl transpeptidase mRNA differs in the !15' untranslated sequence from the corresponding kidney mRNA. !$#cross-references MUID:89288004; PMID:2567622 !$#accession A37376 !'##status preliminary !'##molecule_type mRNA !'##residues 1-369,'P',371-396,'S',398-415,'F',417-568 ##label GRI !'##cross-references GB:X15443; NID:g57805; PIDN:CAA33483.1; PID:g57806 REFERENCE A39179 !$#authors Kurauchi, O.; Lahuna, O.; Darbouy, M.; Aggerbeck, M.; !1Chobert, M.N.; Laperche, Y. !$#journal Biochemistry (1991) 30:1618-1623 !$#title Organization of the 5' end of the rat gamma-glutamyl !1transpeptidase gene: structure of a promoter active in the !1kidney. !$#cross-references MUID:91129234; PMID:1671556 !$#accession A39179 !'##molecule_type DNA !'##residues 1-8 ##label KUR !'##cross-references GB:J05310 REFERENCE S08540 !$#authors Griffiths, S.A.; Manson, M.M. !$#submission submitted to the EMBL Data Library, May 1989 !$#accession S08540 !'##molecule_type mRNA !'##residues 1-369,'P',371-396,'S',398-415,'F',417-568 ##label GR2 !'##cross-references EMBL:X15443; NID:g57805; PIDN:CAA33483.1; !1PID:g57806 !'##experimental_source hepatic REFERENCE I55400 !$#authors Brouillet, X.; Darbouy, M.; Okamoto, X.; Chobert, M.N.; !1Lahuna, O.; Garlatti, X.; Goodspeed, D.C.; Laperche, Y. !$#journal J. Biol. Chem. (1994) 269:14878-14884 !$#title Functional characterization of the rat gamma-glutamyl !1transpeptidase promoter that is expressed and regulated in !1the liver and hepatoma cells. !$#cross-references MUID:94253037; PMID:7910821 !$#accession I55400 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-18 ##label RES !'##cross-references GB:L29167; NID:g508571; PIDN:AAA41218.1; !1PID:g508572 GENETICS !$#gene GGT CLASSIFICATION #superfamily gamma-glutamyltransferase KEYWORDS aminoacyltransferase; transmembrane protein FEATURE !$1-379 #product gamma-glutamyltransferase large chain !8#status predicted #label GGL\ !$380-568 #product gamma-glutamyltransferase small chain !8#status predicted #label GGS SUMMARY #length 568 #molecular-weight 61579 #checksum 1953 SEQUENCE /// ENTRY B28392 #type complete TITLE penicillin amidase (EC 3.5.1.11) I precursor - Pseudomonas sp. ALTERNATE_NAMES cephalosporin acylase I ORGANISM #formal_name Pseudomonas sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B28392 REFERENCE A91857 !$#authors Matsuda, A.; Toma, K.; Komatsu, K.I. !$#journal J. Bacteriol. (1987) 169:5821-5826 !$#title Nucleotide sequences of the genes for two distinct !1cephalosporin acylases from a Pseudomonas strain. !$#cross-references MUID:88058804; PMID:3680178 !$#accession B28392 !'##molecule_type DNA !'##residues 1-558 ##label MAT !'##cross-references GB:M18279; NID:g150966; PIDN:AAA88424.1; !1PID:g150967 !'##experimental_source strain SE83 GENETICS !$#gene acyI CLASSIFICATION #superfamily gamma-glutamyltransferase KEYWORDS antibiotic resistance; hydrolase SUMMARY #length 558 #molecular-weight 58094 #checksum 4303 SEQUENCE /// ENTRY S64019 #type complete TITLE arginyltransferase (EC 2.3.2.8) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein G3710; protein YGL017w ORGANISM #formal_name Saccharomyces cerevisiae DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 21-Jul-2000 ACCESSIONS S64019; S31566; A35198 REFERENCE S64003 !$#authors Hebling, U.; Hofmann, B.; Delius, H. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64019 !'##molecule_type DNA !'##residues 1-503 ##label HEB !'##cross-references EMBL:Z72539; NID:g1322478; PIDN:CAA96717.1; !1PID:g1322479; GSPDB:GN00007; MIPS:YGL017w !'##experimental_source strain S288C REFERENCE S15040 !$#authors Chen, W.; Balzi, E.; Capieaux, E.; Choder, M.; Goffeau, A. !$#journal Yeast (1991) 7:287-299 !$#title The DNA sequencing of the 17 kb HindIII fragment spanning !1the LEU1 and ATE1 loci on chromosome VII from Saccharomyces !1cerevisiae reveals the PDR6 gene, a new member of the !1genetic network controlling pleiotropic drug resistance. !$#cross-references MUID:91353083; PMID:1882553 !$#accession S31566 !'##status translation not shown !'##molecule_type DNA !'##residues 1-121,'S',123-503 ##label CHE !'##cross-references GB:S58126; NID:g234321; PIDN:AAD13904.1; !1PID:g4261604 REFERENCE A35198 !$#authors Balzi, E.; Choder, M.; Chen, W.; Varshavsky, A.; Goffeau, A. !$#journal J. Biol. Chem. (1990) 265:7464-7471 !$#title Cloning and functional analysis of the arginyl-tRNA-protein !1transferase gene ATE1 of Saccharomyces cerevisiae. !$#cross-references MUID:90237046; PMID:2185248 !$#accession A35198 !'##molecule_type DNA !'##residues 1-121,'S',123-401,'I',403-503 ##label BAL !'##cross-references EMBL:J05404; NID:g171096; PIDN:AAA34439.1; !1PID:g171097 GENETICS !$#gene SGD:ATE1; MIPS:YGL017w !'##cross-references SGD:S0002985; MIPS:YGL017w !$#map_position 7L CLASSIFICATION #superfamily Saccharomyces cerevisiae arginyltransferase KEYWORDS aminoacyltransferase SUMMARY #length 503 #molecular-weight 57930 #checksum 1773 SEQUENCE /// ENTRY A39045 #type complete TITLE protein-glutamine gamma-glutamyltransferase (EC 2.3.2.13) 2, splice form 1 - human ALTERNATE_NAMES transglutaminase 2 ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-May-2000 ACCESSIONS A39045 REFERENCE A39045 !$#authors Gentile, V.; Saydak, M.; Chiocca, E.A.; Akande, O.; !1Birckbichler, P.J.; Lee, K.N.; Stein, J.P.; Davies, P.J.A. !$#journal J. Biol. Chem. (1991) 266:478-483 !$#title Isolation and characterization of cDNA clones to mouse !1macrophage and human endothelial cell tissue !1transglutaminases. !$#cross-references MUID:91093168; PMID:1670766 !$#accession A39045 !'##molecule_type mRNA !'##residues 1-687 ##label GEN !'##cross-references GB:M55153; NID:g339520; PIDN:AAA63261.1; !1PID:g339521 !'##note the authors translated the codon CAG for residue 51 as Glu GENETICS !$#gene GDB:TGM2 !'##cross-references GDB:128013; OMIM:190196 !$#map_position 20q11.2-20q12 CLASSIFICATION #superfamily protein-glutamine gamma-glutamyltransferase KEYWORDS alternative splicing; aminoacyltransferase FEATURE !$277 #active_site Cys #status predicted SUMMARY #length 687 #molecular-weight 77257 #checksum 5084 SEQUENCE /// ENTRY B39045 #type complete TITLE protein-glutamine gamma-glutamyltransferase (EC 2.3.2.13) - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 22-Oct-1999 ACCESSIONS B39045 REFERENCE A39045 !$#authors Gentile, V.; Saydak, M.; Chiocca, E.A.; Akande, O.; !1Birckbichler, P.J.; Lee, K.N.; Stein, J.P.; Davies, P.J.A. !$#journal J. Biol. Chem. (1991) 266:478-483 !$#title Isolation and characterization of cDNA clones to mouse !1macrophage and human endothelial cell tissue !1transglutaminases. !$#cross-references MUID:91093168; PMID:1670766 !$#accession B39045 !'##status preliminary !'##molecule_type mRNA !'##residues 1-687 ##label GEN !'##cross-references GB:M55154 !'##note the authors translated the codon CTG for residue 32 as Val, GTG !1for residue 33 as Leu, CAG for residue 51 as Glu, CAA for !1residue 186 as Glu, GAC for residue 226 as Ala, GAC for !1residue 408 as Glu, GAA for residue 409 as Asp, ATC for !1residue 421 as Val, GAC for residue 435 as Glu, TAC for !1residue 537 as Phe, GAC for residue 558 as Gly, GTG for !1residue 584 as Leu, AAC for residue 600 as Lys, and ATC for !1residue 621 as Thr CLASSIFICATION #superfamily protein-glutamine gamma-glutamyltransferase KEYWORDS aminoacyltransferase FEATURE !$277 #active_site Cys #status predicted SUMMARY #length 687 #molecular-weight 77482 #checksum 8858 SEQUENCE /// ENTRY A29996 #type complete TITLE protein-glutamine gamma-glutamyltransferase (EC 2.3.2.13) - guinea pig ORGANISM #formal_name Cavia porcellus #common_name guinea pig DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 22-Oct-1999 ACCESSIONS A29996 REFERENCE A29996 !$#authors Ikura, K.; Nasu, T.; Yokota, H.; Tsuchiya, Y.; Sasaki, R.; !1Chiba, H. !$#journal Biochemistry (1988) 27:2898-2905 !$#title Amino acid sequence of guinea pig liver transglutaminase !1from its cDNA sequence. !$#cross-references MUID:88294033; PMID:2900023 !$#accession A29996 !'##molecule_type mRNA !'##residues 1-691 ##label IKU !'##experimental_source liver CLASSIFICATION #superfamily protein-glutamine gamma-glutamyltransferase KEYWORDS aminoacyltransferase FEATURE !$277 #active_site Cys #status predicted SUMMARY #length 691 #molecular-weight 76752 #checksum 8505 SEQUENCE /// ENTRY A47203 #type complete TITLE protein-glutamine gamma-glutamyltransferase (EC 2.3.2.13) - chicken ALTERNATE_NAMES transglutaminase ORGANISM #formal_name Gallus gallus #common_name chicken DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 29-Oct-1999 ACCESSIONS A47203 REFERENCE A47203 !$#authors Weraarchakul-Boonmark, N.; Jeong, J.M.; Murthy, S.N.; Engel, !1J.D.; Lorand, L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:9804-9808 !$#title Cloning and expression of chicken erythrocyte !1transglutaminase. !$#cross-references MUID:93028551; PMID:1357669 !$#accession A47203 !'##status preliminary !'##molecule_type mRNA !'##residues 1-698 ##label WER !'##cross-references GB:L02270; NID:g212793; PIDN:AAA49104.1; !1PID:g212794 !'##experimental_source erythrocyte !'##note sequence extracted from NCBI backbone (NCBIN:115845, !1NCBIP:115846) CLASSIFICATION #superfamily protein-glutamine gamma-glutamyltransferase KEYWORDS aminoacyltransferase; blocked amino end; lipoprotein; !1myristylation FEATURE !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$287 #active_site Cys #status predicted SUMMARY #length 698 #molecular-weight 78739 #checksum 3463 SEQUENCE /// ENTRY EKHUX #type complete TITLE protein-glutamine gamma-glutamyltransferase (EC 2.3.2.13), plasma [validated] - human ALTERNATE_NAMES activated fibrin-stabilizing factor; coagulation factor XIIIa; factor XIII chain a; fibrinoligase; plasma transglutaminase a chain; protein-glutamine gamma-glutamyltransferase chain a ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Nov-1980 #sequence_revision 31-Dec-1992 #text_change 05-May-2000 ACCESSIONS A35583; A25051; A25515; A25514; A00572 REFERENCE A35583 !$#authors Ichinose, A.; Davie, E.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:5829-5833 !$#title Characterization of the gene for the a subunit of human !1factor XIII (plasma transglutaminase), a blood coagulation !1factor. !$#cross-references MUID:88320337; PMID:2901091 !$#accession A35583 !'##molecule_type DNA !'##residues 1-564,'L',566-732 ##label ICH !'##cross-references GB:M22001; GB:J03834; NID:g182307; PIDN:AAA52415.1; !1PID:g182309 REFERENCE A25051 !$#authors Ichinose, A.; Hendrickson, L.E.; Fujikawa, K.; Davie, E.W. !$#journal Biochemistry (1986) 25:6900-6906 !$#title Amino acid sequence of the a subunit of human factor XIII. !$#cross-references MUID:87100950; PMID:3026437 !$#accession A25051 !'##molecule_type mRNA !'##residues 'REEVPEAHRASPREGTSGGERLQDLVKSK',1-650,'I',652-732 ##label !1IC2 !'##cross-references GB:M14539; NID:g182836; PIDN:AAA52489.1; !1PID:g182837 !'##note parts of this sequence were determined by protein sequencing REFERENCE A25515 !$#authors Grundmann, U.; Amann, E.; Zettlmeissl, G.; Kuepper, H.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:8024-8028 !$#title Characterization of cDNA coding for human factor XIIIa. !$#cross-references MUID:87041394; PMID:2877457 !$#accession A25515 !'##molecule_type mRNA !'##residues 1-88,'L',90-732 ##label GRU !'##cross-references GB:M14354; NID:g182834; PIDN:AAA52488.1; !1PID:g182835 !'##experimental_source placenta REFERENCE A25514 !$#authors Takahashi, N.; Takahashi, Y.; Putnam, F.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:8019-8023 !$#title Primary structure of blood coagulation factor XIIIa !1(fibrinoligase, transglutaminase) from human placenta. !$#cross-references MUID:87041393; PMID:2877456 !$#accession A25514 !'##molecule_type protein !'##residues 2-651,'E',653-731 ##label TAK REFERENCE A00572 !$#authors Takagi, T.; Doolittle, R.F. !$#journal Biochemistry (1974) 13:750-756 !$#title Amino acid sequence studies on factor XIII and the peptide !1released during its activation by thrombin. !$#cross-references MUID:74086956; PMID:4811064 !$#accession A00572 !'##molecule_type protein !'##residues 2-35,37-40,'B',42,'ZZ' ##label TA2 COMMENT Differences in the reported sequences from several !1references may represent polymorphism. A consensus sequence !1is shown. COMMENT This protein is activated by thrombin and calcium ion to !1form intermolecular gamma-glutamyl to epsilon-lysine !1cross-links between fibrin molecules as the last step in !1blood coagulation. COMMENT This polypeptide forms a homodimer in placenta, platelets, !1and megakaryocytes but forms a tetramer with two copies of a !1noncatalytic b chain in plasma. The activated form !1dissociates from the b chains. This protein is not !1glycosylated in placenta and is lightly glycosylated, if at !1all, in plasma. COMMENT It is uncertain whether Met-1 is the initiator or whether !1translation is initiated 5' to the sequenced region. The !1known sequence of the 5'-untranslated region contains no !1in-frame stop codon but does not code for a typical leader !1sequence and does contain a ribosome binding site. GENETICS !$#gene GDB:F13A1; F13A !'##cross-references GDB:120614; OMIM:134570 !$#map_position 6p25.1-6p24.3 !$#introns 44/1; 107/1; 191/1; 230/3; 266/3; 325/1; 371/2; 406/1; 435/ !13; 487/1; 583/1; 636/3; 682/2 CLASSIFICATION #superfamily protein-glutamine gamma-glutamyltransferase KEYWORDS acetylated amino end; aminoacyltransferase; calcium; !1coagulation; glycoprotein; heterotetramer; homodimer; !1plasma; zymogen FEATURE !$2-732 #product protein-glutamine gamma-glutamyltransferase, !8plasma #status experimental #label MAT\ !$2-38 #domain activation peptide #status experimental !8#label ACT\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental\ !$18,614,687 #binding_site carbohydrate (Asn) (covalent) #status !8absent\ !$38-39 #cleavage_site Arg-Gly (thrombin) #status predicted\ !$315 #active_site Cys #status experimental SUMMARY #length 732 #molecular-weight 83267 #checksum 987 SEQUENCE /// ENTRY TGHUM1 #type complete TITLE protein-glutamine gamma-glutamyltransferase (EC 2.3.2.13) 1, epidermal [validated] - human ALTERNATE_NAMES epidermal transglutaminase; keratinocyte transglutaminase; transglutaminase 1; transglutaminase I; transglutaminase K ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1993 #sequence_revision 17-Feb-1995 #text_change 16-Jun-2000 ACCESSIONS A43401; A42317; A42493; A38423; JT0570; A39048; A45298; !1A61374; I37944 REFERENCE A43401 !$#authors Yamanishi, K.; Inazawa, J.; Liew, F.M.; Nonomura, K.; !1Ariyama, T.; Yasuno, H.; Abe, T.; Doi, H.; Hirano, J.; !1Fukushima, S. !$#journal J. Biol. Chem. (1992) 267:17858-17863 !$#title Structure of the gene for human transglutaminase 1. !$#cross-references MUID:92388143; PMID:1381356 !$#accession A43401 !'##molecule_type DNA !'##residues 1-817 ##label YA2 !'##cross-references GB:D10339 !'##experimental_source skin !'##note sequence extracted from NCBI backbone (NCBIN:112775, !1NCBIP:112776) REFERENCE A42317 !$#authors Phillips, M.A.; Stewart, B.E.; Rice, R.H. !$#journal J. Biol. Chem. (1992) 267:2282-2286 !$#title Genomic structure of keratinocyte transglutaminase. !1Recruitment of new exon for modified function. !$#cross-references MUID:92129301; PMID:1346394 !$#accession A42317 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type DNA !'##residues 1-817 ##label PH2 !'##cross-references GB:M98447; NID:g186734; PIDN:AAA96667.1; !1PID:g1256959 !'##experimental_source placenta !'##note sequence extracted from NCBI backbone (NCBIP:78239) and !1corrected to correspond with the published sequence REFERENCE A42493 !$#authors Kim, I.G.; McBride, O.W.; Wang, M.; Kim, S.Y.; Idler, W.W.; !1Steinert, P.M. !$#journal J. Biol. Chem. (1992) 267:7710-7717 !$#title Structure and organization of the human transglutaminase 1 !1gene. !$#cross-references MUID:92218433; PMID:1348508 !$#accession A42493 !'##molecule_type DNA !'##residues 2-31,'R',33-550,'E',552-553,'A',555-668,'I',670-817 ##label !1KIM !'##cross-references GB:M86360 !'##experimental_source placenta !'##note this sequence is inconsistent with the nucleotide translation; !1the authors' translation is shown !'##note sequence extracted from NCBI backbone (NCBIN:94167, !1NCBIP:94168) REFERENCE A38423 !$#authors Phillips, M.A.; Stewart, B.E.; Qin, Q.; Chakravarty, R.; !1Floyd, E.E.; Jetten, A.M.; Rice, R.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:9333-9337 !$#title Primary structure of keratinocyte transglutaminase. !$#cross-references MUID:91067700; PMID:1979171 !$#accession A38423 !'##molecule_type mRNA !'##residues 1-817 ##label PHI !'##cross-references GB:M55183; NID:g186789; PIDN:AAA59474.1; !1PID:g186790 !'##experimental_source skin REFERENCE JT0570 !$#authors Yamanishi, K.; Liew, F.M.; Konishi, K.; Yasuno, H.; Doi, H.; !1Hirano, J.; Fukushima, S. !$#journal Biochem. Biophys. Res. Commun. (1991) 175:906-913 !$#title Molecular cloning of human epidermal transglutaminase cDNA !1from keratinocytes in culture. !$#cross-references MUID:91222201; PMID:1673840 !$#accession JT0570 !'##molecule_type mRNA !'##residues 1-817 ##label YAM !'##cross-references GB:D90287; NID:g219631; PIDN:BAA14329.1; !1PID:g219632 !'##experimental_source skin REFERENCE A39048 !$#authors Kim, H.C.; Idler, W.W.; Kim, I.G.; Han, J.H.; Chung, S.I.; !1Steinert, P.M. !$#journal J. Biol. Chem. (1991) 266:536-539 !$#title The complete amino acid sequence of the human !1transglutaminase K enzyme deduced from the nucleic acid !1sequences of cDNA clones. !$#cross-references MUID:91093179; PMID:1670769 !$#accession A39048 !'##molecule_type mRNA !'##residues 2,'GHVPMWAVGVAT',17-553,'A',555-668,'I',670-817 ##label KI2 !'##cross-references GB:M62925; NID:g339603; PIDN:AAA61166.1; !1PID:g339604 !'##note the authors translated the codon CAC for residue 2 as Pro !'##note the cited Genbank accession number, J05712, is not in release !1101.0 REFERENCE A45298 !$#authors Polakowska, R.R.; Eickbush, T.; Falciano, V.; Razvi, F.; !1Goldsmith, L.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:4476-4480 !$#title Organization and evolution of the human epidermal !1keratinocyte transglutaminase I gene. !$#cross-references MUID:92262462; PMID:1350092 !$#accession A45298 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 310-509 ##label POL !'##cross-references GB:M83230 !'##note sequence extracted from NCBI backbone (NCBIP:102101) REFERENCE A61374 !$#authors Polakowska, R.; Herting, E.; Goldsmith, L.A. !$#journal J. Invest. Dermatol. (1991) 96:285-288 !$#title Isolation of cDNA for human epidermal type I !1transglutaminase. !$#cross-references MUID:91123765; PMID:1704039 !$#accession A61374 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 6-551 ##label PO2 REFERENCE I37944 !$#authors Schroeder, W.T.; Thacher, S.M.; Stewart-Galetka, S.; !1Annarella, M.; Chema, D.; Siciliano, M.J.; Davies, P.J.; !1Tang, H.Y.; Sowa, B.A.; Duvic, M. !$#journal J. Invest. Dermatol. (1992) 99:27-34 !$#title Type I keratinocyte transglutaminase: expression in human !1skin and psoriasis. !$#cross-references MUID:92300061; PMID:1351505 !$#accession I37944 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 375-817 ##label RES !'##cross-references EMBL:X57974; NID:g510524; PIDN:CAA41040.1; !1PID:g510525 GENETICS !$#gene GDB:TGM1; KTG !'##cross-references GDB:125299; OMIM:190195; OMIM:242300 !$#map_position 14q11.2-14q11.2 !$#introns 107/1; 170/1; 253/1; 292/3; 328/3; 387/1; 433/2; 468/1; 497/ !13; 549/1; 643/1; 696/3; 742/2 CLASSIFICATION #superfamily protein-glutamine gamma-glutamyltransferase KEYWORDS aminoacyltransferase; lipoprotein; thiolester bond FEATURE !$315-317 #region cell attachment (R-G-D) motif\ !$47,48,50,51,53 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$377 #active_site Cys #status predicted SUMMARY #length 817 #molecular-weight 89786 #checksum 7607 SEQUENCE /// ENTRY A27335 #type complete TITLE glycogen phosphorylase (EC 2.4.1.1), muscle - human ALTERNATE_NAMES muscle phosphorylase a; muscle phosphorylase b ORGANISM #formal_name Homo sapiens #common_name man DATE 14-May-1999 #sequence_revision 14-May-1999 #text_change 11-Jun-1999 ACCESSIONS A27335; I55545; B23093 REFERENCE A27335 !$#authors Burke, J.; Hwang, P.; Anderson, L.; Lebo, R.; Gorin, F.; !1Fletterick, R. !$#journal Proteins (1987) 2:177-187 !$#title Intron/exon structure of the human gene for the muscle !1isozyme of glycogen phosphorylase. !$#cross-references MUID:88190078; PMID:3447177 !$#accession A27335 !'##molecule_type DNA !'##residues 1-842 ##label BUR !'##cross-references GB:M32598; NID:g190782; PIDN:AAA60231.1; !1PID:g190784 !'##note the authors translated the codon TGG for residue 791 as Leu REFERENCE I55545 !$#authors Gautron, S.; Daegelen, D.; Mennecier, F.; Dubocq, D.; !1Dreyfus, J. !$#journal J. Clin. Invest. (1987) 79:275-281 !$#title Molecular mechanisms of McArdle's disease (muscle glycogen !1phosphorylase deficiency): RNA and DNA analysis. !$#cross-references MUID:87083949; PMID:3466902 !$#accession I55545 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 455-676 ##label GAU !'##cross-references GB:M16013; NID:g187594; PIDN:AAA36216.1; !1PID:g187595 REFERENCE A91152 !$#authors Hwang, P.K.; See, Y.P.; Vincentini, A.M.; Powers, M.A.; !1Fletterick, R.J.; Crerar, M.M. !$#journal Eur. J. Biochem. (1985) 152:267-274 !$#title Comparative sequence analysis of rat, rabbit, and human !1muscle glycogen phosphorylase cDNAs. !$#cross-references MUID:86030264; PMID:3840433 !$#accession B23093 !'##molecule_type mRNA !'##residues 676-741,'L',743-790,'L',792-842 ##label HWA !'##cross-references GB:X03031; NID:g35457 COMMENT The unphosphorylated phosphorylase b is less enzymatically !1active but more allosterically sensitive than the !1phosphorylated phosphorylase a. Phosphorylase b is !1phosphorylated to phosphorylase a by phosphorylase kinase. GENETICS !$#gene GDB:PYGM !'##cross-references GDB:120329; OMIM:232600 !$#map_position 11q13.1-11q13.1 !$#introns 81/3; 115/3; 142/1; 176/3; 221/1; 258/1; 285/3; 333/3; 364/ !13; 413/3; 468/2; 506/3; 540/3; 590/1; 609/3; 657/1; 726/2; !1771/2; 793/3 !$#note defects in this gene can result in McArdle syndrome and !1glycogen storage disease type V COMPLEX homodimer, as phosphorylase b; homotetramer, as !1phosphorylase a FUNCTION !$#description catalyzes the phosphorolysis of terminal alpha-1,4-D-glucose !1units from glycogen by phosphate to form alpha-D-glucose !11-phosphate !$#pathway glycogen metabolism CLASSIFICATION #superfamily phosphorylase KEYWORDS acetylated amino end; allosteric regulation; glycogen !1metabolism; glycosyltransferase; hexosyltransferase; !1homodimer; homotetramer; muscle; phosphoprotein; pyridoxal !1phosphate FEATURE !$2-842 #product glycogen phosphorylase, muscle #status !8predicted #label MAT\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status predicted\ !$15 #binding_site phosphate (Ser) (covalent) (by !8phosphorylase kinase) (in phosphorylase a) #status !8experimental\ !$76,156 #binding_site AMP, allosteric (Tyr) #status !8predicted\ !$681 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 842 #molecular-weight 97164 #checksum 5256 SEQUENCE /// ENTRY PHRBG #type complete TITLE glycogen phosphorylase (EC 2.4.1.1), muscle - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 30-Nov-1980 #sequence_revision 11-Apr-1997 #text_change 16-Jun-2000 ACCESSIONS A24302; A90421; A90422; A90423; A92232; A23093; A00573 REFERENCE A24302 !$#authors Nakano, K.; Hwang, P.K.; Fletterick, R.J. !$#journal FEBS Lett. (1986) 204:283-287 !$#title Complete cDNA sequence for rabbit muscle glycogen !1phosphorylase. !$#cross-references MUID:86275269; PMID:3015680 !$#accession A24302 !'##molecule_type mRNA !'##residues 1-843 ##label NAK REFERENCE A90421 !$#authors Koide, A.; Titani, K.; Ericsson, L.H.; Kumar, S.; Neurath, !1H.; Walsh, K.A. !$#journal Biochemistry (1978) 17:5657-5672 !$#title Sequence of the amino-terminal 349 residues of rabbit muscle !1glycogen phosphorylase including the sites of covalent and !1allosteric control. !$#cross-references MUID:79082846; PMID:728424 !$#accession A90421 !'##molecule_type protein !'##residues 2-30,'D',32,'D',34-42,'N',44-55,'H',57,'L',59-88,'Q', !190-112,'D',114-308,310-351 ##label KOI !'##experimental_source skeletal muscle !'##note the identifications of Asn-236, Asn-237, Cys-319, and Asp-321 !1are based on indirect evidence !'##note Ser-15 is phosphorylated by phosphorylase kinase in the !1conversion of phosphorylase b to a !'##note Tyr-156 can be labeled by an AMP analog and may therefore be !1involved in the allosteric control of enzyme activity !'##note Cys-109 and Cys-143 are involved in the association of subunits REFERENCE A90422 !$#authors Hermann, J.; Titani, K.; Ericsson, L.H.; Wade, R.D.; !1Neurath, H.; Walsh, K.A. !$#journal Biochemistry (1978) 17:5672-5679 !$#title Amino acid sequence of two cyanogen bromide fragments of !1glycogen phosphorylase. !$#cross-references MUID:79082847; PMID:728425 !$#accession A90422 !'##molecule_type protein !'##residues 352-429;443-605 ##label HER !'##experimental_source skeletal muscle REFERENCE A90423 !$#authors Titani, K.; Koide, A.; Ericsson, L.H.; Kumar, S.; Hermann, !1J.; Wade, R.D.; Walsh, K.A.; Neurath, H.; Fischer, E.H. !$#journal Biochemistry (1978) 17:5680-5693 !$#title Sequence of the carboxyl-terminal 492 residues of rabbit !1muscle glycogen phosphorylase including the pyridoxal !15'-phosphate binding site. !$#cross-references MUID:79082848; PMID:728426 !$#accession A90423 !'##molecule_type protein !'##residues 352-843 ##label TIT !'##experimental_source skeletal muscle REFERENCE A90424 !$#authors Sprang, S.; Fletterick, R.J. !$#journal Biochemistry (1978) 17:5693-5694 !$#title Appendix I: Crystallographic analysis of phosphorylase a at !12.5 A resolution, a comment on the chemical sequence. !$#cross-references MUID:79082849; PMID:728427 !$#contents annotation; phosphorylase a, X-ray crystallography, 2.5 !1angstroms !$#note the proposed order of the CNBr peptides is confirmed REFERENCE A90425 !$#authors Jenkins, J.A.; Johnson, L.N.; Wilson, K.S. !$#journal Biochemistry (1978) 17:5694-5695 !$#title Appendix II: Assignment of the amino acid sequence to the !1crystal structure of glycogen phosphorylase b. !$#cross-references MUID:79082850; PMID:728428 !$#contents annotation; phosphorylase b, X-ray crystallography, 3.0 !1angstroms REFERENCE A92232 !$#authors Lee, Y.M.; Benisek, W.F. !$#journal J. Biol. Chem. (1978) 253:5460-5463 !$#title Inactivation of phosphorylase b by potassium ferrate. !1Identification of a tyrosine residue involved in the binding !1of adenosine 5'-monophosphate. !$#cross-references MUID:78218229; PMID:670209 !$#accession A92232 !'##molecule_type protein !'##residues 71-81 ##label LEE !'##note when Tyr-76 is involved with ferrate it does not bind 5'-AMP !1and vice versa; this suggests that Tyr-76 is present in the !15'-AMP binding site and may be involved in AMP binding REFERENCE A91152 !$#authors Hwang, P.K.; See, Y.P.; Vincentini, A.M.; Powers, M.A.; !1Fletterick, R.J.; Crerar, M.M. !$#journal Eur. J. Biochem. (1985) 152:267-274 !$#title Comparative sequence analysis of rat, rabbit, and human !1muscle glycogen phosphorylase cDNAs. !$#cross-references MUID:86030264; PMID:3840433 !$#accession A23093 !'##molecule_type mRNA !'##residues 575-577,'FF',580-712,'C',714-843 ##label HWA !'##cross-references GB:X03030; GB:V00889; GB:V00890; GB:V00891; !1NID:g1665; PIDN:CAA26833.1; PID:g1364243 COMMENT The unphosphorylated phosphorylase b is less enzymatically !1active but more allosterically sensitive than the !1phosphorylated phosphorylase a. Phosphorylase b is !1phosphorylated to phosphorylase a by phosphorylase kinase. COMMENT The activity of phosphorylase is controlled both by !1allosteric means (through the noncovalent binding of !1metabolites) and by covalent modification. Thus AMP !1allosterically activates, whereas ATP, ADP, and !1glucose-6-phosphate allosterically inhibit, phosphorylase b. !1The phosphorylation of Ser-15 in each chain will also !1convert phosphorylase b to phosphorylase a. COMPLEX homodimer, as phosphorylase b; homotetramer, as !1phosphorylase a FUNCTION !$#description catalyzes the phosphorolysis of terminal alpha-1,4-D-glucose !1units from glycogen by phosphate to form alpha-D-glucose !11-phosphate !$#pathway glycogen metabolism CLASSIFICATION #superfamily phosphorylase KEYWORDS acetylated amino end; allosteric regulation; glycogen !1metabolism; glycosyltransferase; hexosyltransferase; !1homotetramer; phosphoprotein; pyridoxal phosphate FEATURE !$2-843 #product glycogen phosphorylase, muscle #status !8experimental #label MAT\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental\ !$15 #binding_site phosphate (Ser) (covalent) (by !8phosphorylase kinase) (in phosphorylase a) #status !8experimental\ !$76,156 #binding_site AMP, allosteric (Tyr) #status !8predicted\ !$681 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status experimental SUMMARY #length 843 #molecular-weight 97289 #checksum 1008 SEQUENCE /// ENTRY A25518 #type complete TITLE glycogen phosphorylase (EC 2.4.1.1), hepatic - human ALTERNATE_NAMES glycogen phosphorylase IV ORGANISM #formal_name Homo sapiens #common_name man DATE 14-May-1999 #sequence_revision 14-May-1999 #text_change 11-Jun-1999 ACCESSIONS A25518; I56524 REFERENCE A25518 !$#authors Newgard, C.B.; Nakano, K.; Hwang, P.K.; Fletterick, R.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:8132-8136 !$#title Sequence analysis of the cDNA encoding human liver glycogen !1phosphorylase reveals tissue-specific codon usage. !$#cross-references MUID:87041414; PMID:2877458 !$#accession A25518 !'##molecule_type mRNA !'##residues 1-847 ##label NEW !'##cross-references GB:M14636; NID:g183352; PIDN:AAA52577.1; !1PID:g183353 REFERENCE I56524 !$#authors Gorin, F.A.; Mullinax, R.L.; Ignacio, P.C.; Neve, R.L.; !1Kurnit, D.M. !$#journal J. Neurogenet. (1987) 4:293-308 !$#title McArdle's and Hers' diseases: Glycogen phosphorylase !1transcriptional expression in human tissues. !$#cross-references MUID:88155137; PMID:3509980 !$#accession I56524 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 482-714,'R',716-847 ##label RES !'##cross-references GB:M36807; NID:g183350; PIDN:AAA35906.1; !1PID:g183351 COMMENT The unphosphorylated phosphorylase b is less enzymatically !1active but more allosterically sensitive than the !1phosphorylated phosphorylase a. Phosphorylase b is !1phosphorylated to phosphorylase a by phosphorylase kinase. GENETICS !$#gene GDB:PYGL !'##cross-references GDB:120328; OMIM:232700 !$#map_position 14q21-14q21 !$#note defects in this gene can result in Hers disease and glycogen !1storage disease type VI COMPLEX homodimer, as phosphorylase b; homotetramer, as !1phosphorylase a FUNCTION !$#description catalyzes the phosphorolysis of terminal alpha-1,4-D-glucose !1units from glycogen by phosphate to form alpha-D-glucose !11-phosphate !$#pathway glycogen metabolism CLASSIFICATION #superfamily phosphorylase KEYWORDS allosteric regulation; glycogen metabolism; !1glycosyltransferase; hexosyltransferase; homodimer; !1homotetramer; liver; phosphoprotein; pyridoxal phosphate FEATURE !$2-847 #product glycogen phosphorylase, hepatic #status !8predicted #label MAT\ !$15 #binding_site phosphate (Ser) (covalent) (by !8phosphorylase kinase) (in phosphorylase a) #status !8predicted\ !$76,156 #binding_site AMP, allosteric (Tyr) #status !8predicted\ !$681 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 847 #molecular-weight 97222 #checksum 6607 SEQUENCE /// ENTRY A40138 #type complete TITLE glycogen phosphorylase (EC 2.4.1.1), brain - human ORGANISM #formal_name Homo sapiens #common_name man DATE 14-May-1999 #sequence_revision 14-May-1999 #text_change 11-Jun-1999 ACCESSIONS A40138; A29949 REFERENCE A40138 !$#authors Gelinas, R.P.; Froman, B.E.; McElroy, F.; Tait, R.C.; Gorin, !1F.A. !$#journal Brain Res. Mol. Brain Res. (1989) 6:177-185 !$#title Human brain glycogen phosphorylase: characterization of !1fetal cDNA and genomic sequences. !$#cross-references MUID:90135922; PMID:2615594 !$#accession A40138 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-843 ##label GEL !'##cross-references GB:U47025; NID:g1172225; PIDN:AAB60395.1; !1PID:g1172226 !'##experimental_source fetal brain REFERENCE A29949 !$#authors Newgard, C.B.; Littman, D.R.; van Genderen, C.; Smith, M.; !1Fletterick, R.J. !$#journal J. Biol. Chem. (1988) 263:3850-3857 !$#title Human brain glycogen phosphorylase. Cloning, sequence !1analysis, chromosomal mapping, tissue expression, and !1comparison with the human liver and muscle isozymes. !$#cross-references MUID:88153685; PMID:3346228 !$#accession A29949 !'##molecule_type mRNA !'##residues 1-247,'R',249-301,'G',303-834, !1'LQHLPHPEWESGGATCWAPPELCTHLAMY' ##label NEW !'##cross-references GB:J03544; NID:g187596; PIDN:AAA59597.1; !1PID:g307200 !'##experimental_source astrocytoma cell line COMMENT The unphosphorylated phosphorylase b is less enzymatically !1active but more allosterically sensitive than the !1phosphorylated phosphorylase a. Phosphorylase b is !1phosphorylated to phosphorylase a by phosphorylase kinase. GENETICS !$#gene GDB:PYGB !'##cross-references GDB:120326; OMIM:138550 !$#map_position 20p11.2-20p11.1 COMPLEX homodimer, as phosphorylase b; homotetramer, as !1phosphorylase a FUNCTION !$#description catalyzes the phosphorolysis of terminal alpha-1,4-D-glucose !1units from glycogen by phosphate to form alpha-D-glucose !11-phosphate !$#pathway glycogen metabolism CLASSIFICATION #superfamily phosphorylase KEYWORDS allosteric regulation; brain; glycogen metabolism; !1glycosyltransferase; hexosyltransferase; homodimer; !1homotetramer; phosphoprotein; pyridoxal phosphate FEATURE !$2-843 #product glycogen phosphorylase, brain #status !8predicted #label MAT\ !$15 #binding_site phosphate (Ser) (covalent) (by !8phosphorylase kinase) (in phosphorylase a) #status !8predicted\ !$76,156 #binding_site AMP, allosteric (Tyr) #status !8predicted\ !$681 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 843 #molecular-weight 96682 #checksum 9177 SEQUENCE /// ENTRY PHPOAG #type complete TITLE starch phosphorylase (EC 2.4.1.1) precursor - potato ALTERNATE_NAMES alpha-glucan phosphorylase ORGANISM #formal_name Solanum tuberosum #common_name potato DATE 04-Dec-1986 #sequence_revision 30-Sep-1990 #text_change 21-Jul-2000 ACCESSIONS JU0130; A00574; PQ0139; S15531; S12033 REFERENCE A91915 !$#authors Nakano, K.; Mori, H.; Fukui, T. !$#journal J. Biochem. (1989) 106:691-695 !$#title Molecular cloning of cDNA encoding potato amyloplast !1alpha-glucan phosphorylase and the structure of its transit !1peptide. !$#cross-references MUID:90110071; PMID:2481677 !$#accession JU0130 !'##molecule_type mRNA !'##residues 1-966 ##label NA1 !'##cross-references GB:D00520; NID:g3702676; PIDN:BAA00407.1; !1PID:g217999 REFERENCE A92591 !$#authors Nakano, K.; Fukui, T. !$#journal J. Biol. Chem. (1986) 261:8230-8236 !$#title The complete amino acid sequence of potato alpha-glucan !1phosphorylase. !$#cross-references MUID:86250715; PMID:3722153 !$#accession A00574 !'##molecule_type protein !'##residues 51-966 ##label NAK REFERENCE PQ0139 !$#authors Brisson, N.; Giroux, H.; Zollinger, M.; Camirand, A.; !1Simard, C. !$#journal Plant Cell (1989) 1:559-566 !$#title Maturation and subcellular compartmentation of potato starch !1phosphorylase. !$#cross-references MUID:92404721; PMID:2535551 !$#accession PQ0139 !'##molecule_type mRNA !'##residues 1-130 ##label BRI !'##experimental_source tuber, cv. Kennebec REFERENCE S15531 !$#authors Brisson, N. !$#submission submitted to the EMBL Data Library, April 1990 !$#accession S15531 !'##molecule_type mRNA !'##residues 1-158,'D',160-966 ##label BR2 !'##cross-references EMBL:X52385; NID:g21578; PIDN:CAA36612.1; !1PID:g21579 REFERENCE S12033 !$#authors Camirand, A.; St-Pierre, B.; Marineau, C.; Brisson, N. !$#journal Mol. Gen. Genet. (1990) 224:33-39 !$#title Occurrence of a copia-like transposable element in one of !1the introns of the potato starch phosphorylase gene. !$#cross-references MUID:91117174; PMID:1703627 !$#accession S12033 !'##molecule_type mRNA !'##residues 416-595 ##label CAM !'##cross-references EMBL:X52385 COMMENT Phosphorylase, an important allosteric enzyme in !1carbohydrate metabolism, catalyzes the formation of glucose !11-phosphate from polyglucose. Enzymes from different sources !1differ in their regulatory mechanisms and in their natural !1substrates. However, all known phosphorylases share !1catalytic and structural properties; the binding site for !1pyridoxal 5'-phosphate is highly conserved. CLASSIFICATION #superfamily phosphorylase KEYWORDS allosteric regulation; carbohydrate metabolism; !1glycosyltransferase; hexosyltransferase; phosphoprotein; !1pyridoxal phosphate FEATURE !$1-50 #domain transit peptide (amyloplast) #status !8predicted #label TNP\ !$51-966 #product phosphorylase #status experimental #label !8MAT\ !$812 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 966 #molecular-weight 109505 #checksum 4821 SEQUENCE /// ENTRY A40995 #type complete TITLE starch phosphorylase (EC 2.4.1.1) H [similarity] - potato ORGANISM #formal_name Solanum tuberosum #common_name potato DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS A40995 REFERENCE A40995 !$#authors Mori, H.; Tanizawa, K.; Fukui, T. !$#journal J. Biol. Chem. (1991) 266:18446-18453 !$#title Potato tuber type H phosphorylase isozyme. Molecular !1cloning, nucleotide sequence, and expression of a !1full-length cDNA in Escherichia coli. !$#cross-references MUID:92011592; PMID:1917968 !$#accession A40995 !'##molecule_type mRNA !'##residues 1-838 ##label MOR !'##cross-references GB:M69038; NID:g169472; PIDN:AAA33809.1; !1PID:g169473 CLASSIFICATION #superfamily phosphorylase KEYWORDS glycosyltransferase; hexosyltransferase; phosphoprotein; !1pyridoxal phosphate FEATURE !$684 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 838 #molecular-weight 95111 #checksum 9760 SEQUENCE /// ENTRY PHECGG #type complete TITLE phosphorylase (EC 2.4.1.1) glgP - Escherichia coli (strain K-12) ALTERNATE_NAMES alpha-glucan phosphorylase ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 31-Oct-1997 #text_change 02-Aug-2002 ACCESSIONS G65138; A30880; JT0418; S02178; JT0476 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65138 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-815 ##label BLAT !'##cross-references GB:AE000419; GB:U00096; NID:g2367227; !1PIDN:AAC76453.1; PID:g2367228; UWGP:b3428 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A30880 !$#authors Yu, F.; Jen, Y.; Takeuchi, E.; Inouye, M.; Nakayama, H.; !1Tagaya, M.; Fukui, T. !$#journal J. Biol. Chem. (1988) 263:13706-13711 !$#title Alpha-glucan phosphorylase from Escherichia coli. Cloning of !1the gene, and purification and characterization of the !1protein. !$#cross-references MUID:88330897; PMID:3047129 !$#accession A30880 !'##molecule_type DNA !'##residues 1-181,188-279,'DV',282-449,'L',451-728,'T',730-815 ##label !1YUF !'##cross-references GB:J03966; NID:g146145; PIDN:AAA23874.1; !1PID:g146146 REFERENCE JT0418 !$#authors Romeo, T.; Kumar, A.; Preiss, J. !$#journal Gene (1988) 70:363-376 !$#title Analysis of the Escherichia coli glycogen gene cluster !1suggests that catabolic enzymes are encoded among the !1biosynthetic genes. !$#cross-references MUID:89108020; PMID:2975249 !$#accession JT0418 !'##molecule_type DNA !'##residues 1-59,'P',61-93,'TH',96-247,'DR',250-279,'G',281-323,'S', !1325-376,'S',378-383 ##label ROM REFERENCE S02178 !$#authors Choi, Y.L.; Kawamukai, M.; Utsumi, R.; Sakai, H.; Komano, T. !$#journal FEBS Lett. (1989) 243:193-198 !$#title Molecular cloning and sequencing of the glycogen !1phosphorylase gene from Escherichia coli. !$#cross-references MUID:89137514; PMID:2645169 !$#accession S02178 !'##molecule_type DNA !'##residues 26-174,'S',176-190,'V',192-486,'GT',489-519,'NV',522-815 !1##label CHO !'##cross-references GB:X16931; NID:g41558; PIDN:CAA34807.1; PID:g41559 GENETICS !$#gene glgP; glgY !$#map_position 75 min FUNCTION !$#description catalyzes the phosphorolysis of terminal alpha-1,4-D-glucose !1units from maltodextrin by phosphate to form alpha-D-glucose !11-phosphate !$#note specific for glycogen degradation with low activity; may be !1involved in the degradation of endogenous glycogen during !1long stationary conditions CLASSIFICATION #superfamily phosphorylase KEYWORDS allosteric regulation; carbohydrate metabolism; !1glycosyltransferase; hexosyltransferase; phosphoprotein; !1pyridoxal phosphate FEATURE !$662 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 815 #molecular-weight 93172 #checksum 7991 SEQUENCE /// ENTRY S20595 #type complete TITLE glycogen phosphorylase (EC 2.4.1.1) 1 - slime mold (Dictyostelium discoideum) ORGANISM #formal_name Dictyostelium discoideum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S20595 REFERENCE S20595 !$#authors Rogers, P.V.; Luo, S.; Sucic, J.F.; Rutherford, C.L. !$#journal Biochim. Biophys. Acta (1992) 1129:262-272 !$#title Characterization and cloning of glycogen phosphorylase 1 !1from Dictyostelium discoideum. !$#cross-references MUID:92162744; PMID:1536877 !$#accession S20595 !'##status preliminary !'##molecule_type DNA !'##residues 1-853 ##label ROG !'##cross-references EMBL:X62142 GENETICS !$#introns 40/1 CLASSIFICATION #superfamily phosphorylase KEYWORDS glycosyltransferase; hexosyltransferase; phosphoprotein; !1pyridoxal phosphate FEATURE !$697 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 853 #molecular-weight 98331 #checksum 3739 SEQUENCE /// ENTRY PHECGM #type complete TITLE phosphorylase (EC 2.4.1.1) malP - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 28-May-1986 #sequence_revision 17-Oct-1997 #text_change 02-Aug-2002 ACCESSIONS D65137; S00596; A93357; A93122; S03773; I64878; A00575 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65137 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-797 ##label BLAT !'##cross-references GB:AE000417; GB:U00096; NID:g2367220; !1PIDN:AAC76442.1; PID:g2367221; UWGP:b3417 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S00596 !$#authors Palm, D.; Goerl, R.; Weidinger, G.; Zeier, R.; Fischer, B.; !1Schinzel, R. !$#journal Z. Naturforsch. C (1987) 42:394-400 !$#title E. coli maltodextrin phosphorylase: primary structure and !1deletion mapping of the C-terminal site. !$#cross-references MUID:87265999; PMID:3037809 !$#accession S00596 !'##molecule_type DNA !'##residues 1-293,'E',295-487,'V',489,'L',491-497,'DL',500-501,'V', !1503-521,'D',523-547,'R',549-681,'K',683-700,'D',702-797 !1##label PAL !'##cross-references EMBL:X06791 !'##note the authors translated the codon GAC for residue 492 as Gln REFERENCE A93357 !$#authors Palm, D.; Goerl, R.; Burger, K.J. !$#journal Nature (1985) 313:500-502 !$#title Evolution of catalytic and regulatory sites in !1phosphorylases. !$#cross-references MUID:85111169; PMID:3155826 !$#accession A93357 !'##molecule_type DNA !'##residues 1-293,'E',295-487,'V',489,'L',491-498,'L',500-501,'V', !1503-521,'D',523-547,'R',549-681,'K',683-687,'D' ##label PA2 !'##note the authors translated the codon CAG for residue 498 as Asp, !1CAG for residue 505 as His, and GAA for residue 558 as Gln REFERENCE A93122 !$#authors Debarbouille, M.; Cossart, P.; Raibaud, O. !$#journal Mol. Gen. Genet. (1982) 185:88-92 !$#title A DNA sequence containing the control sites for gene malT !1and for the malPQ operon. !$#cross-references MUID:82219203; PMID:6283313 !$#accession A93122 !'##molecule_type DNA !'##residues 1-54 ##label DEB !'##cross-references GB:V00304; NID:g41967; PIDN:CAA23584.1; PID:g581130 REFERENCE S03773 !$#authors Pugsley, A.P.; Dubreuil, C. !$#journal Mol. Microbiol. (1988) 2:473-479 !$#title Molecular characterization of malQ, the structural gene for !1the Escherichia coli enzyme amylomaltase. !$#cross-references MUID:89013888; PMID:2845225 !$#accession S03773 !'##molecule_type DNA !'##residues 635-700,'D',702-797 ##label PUG !'##cross-references EMBL:M32793; NID:g146713; PIDN:AAA24105.1; !1PID:g146714 !'##note the authors translated the codon GAG for residue 750 as Phe REFERENCE I51943 !$#authors Raibaud, O.; Debarbouille, M.; Cossart, P. !$#journal Ann. Inst. Pasteur Microbiol. (1982) 133:59-63 !$#title Clonage de la region malA de Escherichia coli K12: Sequence !1des nucleotides des regions regulatrices et des promoteurs, !1identification et purification de la proteine activatrice !1MalT. !$#accession I64878 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-54 ##label RES !'##cross-references GB:M24342; NID:g146718; PIDN:AAA24108.1; !1PID:g551818 COMMENT Phosphorylase, an important allosteric enzyme in !1carbohydrate metabolism, catalyzes the formation of !1glucose-1-phosphate from polyglucose. Enzymes from different !1sources differ in their regulatory mechanisms and their !1natural substrates. However, all known phosphorylases share !1catalytic and structural properties; the binding site for !1pyridoxal 5'-phosphate is highly conserved. GENETICS !$#gene malP !$#map_position 75 min CLASSIFICATION #superfamily phosphorylase KEYWORDS allosteric regulation; carbohydrate metabolism; !1glycosyltransferase; hexosyltransferase; phosphoprotein; !1pyridoxal phosphate FEATURE !$2-797 #product maltodextrin phosphorylase #status predicted !8#label MAT\ !$646 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 797 #molecular-weight 90464 #checksum 2594 SEQUENCE /// ENTRY YUZMS #type complete TITLE sucrose synthase (EC 2.4.1.13) - maize ORGANISM #formal_name Zea mays #common_name maize DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 11-Jun-1999 ACCESSIONS S07184; S19085 REFERENCE S07184 !$#authors Werr, W.; Frommer, W.B.; Maas, C.; Starlinger, P. !$#journal EMBO J. (1985) 4:1373-1380 !$#title Structure of the sucrose synthase gene on chromosome 9 of !1Zea mays L. !$#accession S07184 !'##molecule_type DNA !'##residues 1-802 ##label WER !'##cross-references EMBL:X02382; NID:g22487; PIDN:CAA26229.1; !1PID:g22488 !$#accession S19085 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-802 ##label WER2 !'##cross-references EMBL:X02400; NID:g22485; PIDN:CAA26247.1; !1PID:g22486 GENETICS !$#gene sh !$#map_position 9 !$#introns 32/2; 72/3; 123/2; 187/3; 227/2; 299/3; 331/3; 389/3; 428/3; !1484/2; 559/2; 665/3; 747/2; 793/3 CLASSIFICATION #superfamily sucrose synthase; sucrose/sucrose-phosphate !1synthase homology KEYWORDS glycosyltransferase; hexosyltransferase FEATURE !$276-750 #domain sucrose/sucrose-phosphate synthase homology !8#label SSPS SUMMARY #length 802 #molecular-weight 91731 #checksum 6146 SEQUENCE /// ENTRY YUPOS #type complete TITLE sucrose synthase (EC 2.4.1.13) - potato ORGANISM #formal_name Solanum tuberosum #common_name potato DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 11-Jun-1999 ACCESSIONS A29615 REFERENCE A29615 !$#authors Salanoubat, M.; Belliard, G. !$#journal Gene (1987) 60:47-56 !$#title Molecular cloning and sequencing of sucrose synthase cDNA !1from potato (Solanum tuberosum L.): preliminary !1characterization of sucrose synthase mRNA distribution. !$#cross-references MUID:88152501; PMID:2964386 !$#accession A29615 !'##molecule_type mRNA !'##residues 1-805 ##label SAL !'##cross-references GB:M18745; NID:g169571; PIDN:AAA33841.1; !1PID:g169572 !'##experimental_source var. Sirtema 2n=4x CLASSIFICATION #superfamily sucrose synthase; sucrose/sucrose-phosphate !1synthase homology KEYWORDS glycosyltransferase; hexosyltransferase FEATURE !$279-753 #domain sucrose/sucrose-phosphate synthase homology !8#label SSPS SUMMARY #length 805 #molecular-weight 92415 #checksum 9301 SEQUENCE /// ENTRY YUMU #type complete TITLE sucrose synthase (EC 2.4.1.13) - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 11-Jun-1999 ACCESSIONS S19125 REFERENCE S19125 !$#authors Chopra, S.; Del-favero, J.; Dolferus, R.; Jacobs, M. !$#journal Plant Mol. Biol. (1992) 18:131-134 !$#title Sucrose synthase of Arabidopsis: genomic cloning and !1sequence characterization. !$#cross-references MUID:92119221; PMID:1531031 !$#accession S19125 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-804 ##label CHO !'##cross-references EMBL:X60987; NID:g16525; PIDN:CAA43303.1; !1PID:g16526 GENETICS !$#introns 31/2; 72/3; 123/2; 187/3; 227/2; 299/3; 331/3; 389/3; 428/3; !1484/2; 559/2; 666/3; 747/2; 793/3 CLASSIFICATION #superfamily sucrose synthase; sucrose/sucrose-phosphate !1synthase homology KEYWORDS glycosyltransferase; hexosyltransferase FEATURE !$276-750 #domain sucrose/sucrose-phosphate synthase homology !8#label SSPS SUMMARY #length 804 #molecular-weight 91989 #checksum 177 SEQUENCE /// ENTRY JQ1329 #type complete TITLE sucrose-phosphate synthase (EC 2.4.1.14) - maize ORGANISM #formal_name Zea mays #common_name maize DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JQ1329; PQ0260 REFERENCE JQ1329 !$#authors Worrell, A.C.; Bruneau, J.M.; Summerfelt, K.; Boersig, M.; !1Voelker, T.A. !$#journal Plant Cell (1991) 3:1121-1130 !$#title Expression of a maize sucrose phosphate synthase in tomato !1alters leaf carbohydrate partitioning. !$#cross-references MUID:92338837; PMID:1840396 !$#accession JQ1329 !'##molecule_type mRNA !'##residues 1-1068 ##label WOR !'##cross-references GB:M97550; NID:g168625; PIDN:AAA33513.1; !1PID:g168626 !$#accession PQ0260 !'##molecule_type protein !'##residues 71-74;206-212;471-481;872-892 ##label WOR1 COMMENT This enzyme transfers the glucosyl group from UDPglucose to !1fructose-6-phosphate. COMMENT This enzyme is involved in the regulation of carbon !1partitioning in the leaves of plants. FUNCTION !$#description catalyzes the formation of sucrose-6-phosphate from !1UDPglucose and D-fructose 6-phosphate !$#pathway sucrose biosynthesis CLASSIFICATION #superfamily sucrose-phosphate synthase; sucrose/ !1sucrose-phosphate synthase homology KEYWORDS glycosyltransferase; hexosyltransferase; sucrose !1biosynthesis FEATURE !$178-666 #domain sucrose/sucrose-phosphate synthase homology !8#label SSPS SUMMARY #length 1068 #molecular-weight 118574 #checksum 5016 SEQUENCE /// ENTRY NQECA #type complete TITLE 1,4-alpha-glucan branching enzyme (EC 2.4.1.18) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 01-Mar-2002 ACCESSIONS A25498; C65139 REFERENCE A25498 !$#authors Baecker, P.A.; Greenberg, E.; Preiss, J. !$#journal J. Biol. Chem. (1986) 261:8738-8743 !$#title Biosynthesis of bacterial glycogen. Primary structure of !1Escherichia coli 1,4-alpha-D-glucan:1,4-alpha-D-glucan !16-alpha-D-(1,4-alpha-D-glucano)-transferase as deduced from !1the nucleotide sequence of the glgB gene. !$#cross-references MUID:86250792; PMID:3013861 !$#accession A25498 !'##molecule_type DNA !'##residues 1-728 ##label BAE !'##cross-references GB:M13751; NID:g146141; PIDN:AAA23872.1; !1PID:g146142 !'##note the authors translated the codon AAA for residue 546 as Gly REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65139 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-728 ##label BLAT !'##cross-references GB:AE000419; GB:U00096; NID:g2367227; !1PIDN:AAC76457.1; PID:g1789839; UWGP:b3432 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene glgB !$#map_position 75 min FUNCTION !$#description catalyzes the transglycosylation of a terminal segment of a !11,4-alpha-D-glucan chain to an unbranched chain, thereby !1converting amylose to amylopectin or creating branches in !1glycogen !$#pathway bacterial glycogen biosynthesis CLASSIFICATION #superfamily 1,4-alpha-glucan branching enzyme KEYWORDS glycogen/starch biosynthesis; glycosyltransferase; !1hexosyltransferase; monomer SUMMARY #length 728 #molecular-weight 84336 #checksum 1536 SEQUENCE /// ENTRY I64118 #type complete TITLE 1,4-alpha-glucan branching enzyme (EC 2.4.1.18) - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS I64118 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession I64118 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-730 ##label TIGR !'##cross-references GB:U32815; GB:L42023; NID:g1574818; !1PIDN:AAC23004.1; PID:g1574820; TIGR:HI1357 CLASSIFICATION #superfamily 1,4-alpha-glucan branching enzyme KEYWORDS glycogen/starch biosynthesis; glycosyltransferase; !1hexosyltransferase SUMMARY #length 730 #molecular-weight 83820 #checksum 9710 SEQUENCE /// ENTRY B41328 #type complete TITLE 1,4-alpha-glucan branching enzyme (EC 2.4.1.18) - Butyrivibrio fibrisolvens ORGANISM #formal_name Butyrivibrio fibrisolvens DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B41328 REFERENCE A41328 !$#authors Rumbak, E.; Rawlings, D.E.; Lindsey, G.G.; Woods, D.R. !$#journal J. Bacteriol. (1991) 173:6732-6741 !$#title Characterization of the Butyrivibrio fibrisolvens glgB gene, !1which encodes a glycogen-branching enzyme with !1starch-clearing activity. !$#cross-references MUID:92041554; PMID:1938880 !$#accession B41328 !'##status preliminary !'##molecule_type DNA !'##residues 1-639 ##label RUM !'##cross-references GB:M64980; NID:g144156; PIDN:AAA23007.1; !1PID:g144158 FUNCTION !$#description catalyzes the transglycosylation of a terminal segment of a !11,4-alpha-D-glucan chain to an unbranched chain, thereby !1converting amylose to amylopectin or creating branches in !1glycogen !$#pathway glycogen/starch biosynthesis !$#note final step in biosynthesis of glycogen or amylopectin CLASSIFICATION #superfamily 1,4-alpha-glucan branching enzyme KEYWORDS glycogen/starch biosynthesis; glycosyltransferase; !1hexosyltransferase SUMMARY #length 639 #molecular-weight 73875 #checksum 3560 SEQUENCE /// ENTRY S40048 #type complete TITLE 1,4-alpha-glucan branching enzyme (EC 2.4.1.18) glgB - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S40048; F69632; S36624 REFERENCE S40048 !$#authors Kiel, J.A.K.W.; Boels, J.M.; Beldman, G.; Venema, G. !$#journal Mol. Microbiol. (1994) 11:203-218 !$#title Glycogen in Bacillus subtilis: molecular characterization of !1an operon encoding enzymes involved in glycogen biosynthesis !1and degradation. !$#cross-references MUID:94195107; PMID:8145641 !$#accession S40048 !'##status preliminary !'##molecule_type DNA !'##residues 1-627 ##label KIE !'##cross-references EMBL:Z25795; NID:g397487; PIDN:CAA81040.1; !1PID:g397488 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69632 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-627 ##label KUN !'##cross-references GB:Z99119; GB:AL009126; NID:g2635411; !1PIDN:CAB15076.1; PID:g2635582 !'##experimental_source strain 168 GENETICS !$#gene glgB FUNCTION !$#description catalyzes the transglycosylation of a terminal segment of a !11,4-alpha-D-glucan chain to an unbranched chain, thereby !1converting amylose to amylopectin or creating branches in !1glycogen !$#pathway glycogen/starch biosynthesis !$#note final step in biosynthesis of glycogen or amylopectin CLASSIFICATION #superfamily 1,4-alpha-glucan branching enzyme KEYWORDS glycogen/starch biosynthesis; glycosyltransferase; !1hexosyltransferase SUMMARY #length 627 #molecular-weight 73665 #checksum 4240 SEQUENCE /// ENTRY S34218 #type complete TITLE 1,4-alpha-glucan branching enzyme (EC 2.4.1.18) II - Streptomyces coelicolor ALTERNATE_NAMES glycogen branching enzyme ORGANISM #formal_name Streptomyces coelicolor DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Dec-1999 ACCESSIONS S70078; S34218; T42039 REFERENCE S70078 !$#authors Bruton, C.J.; Plaskitt, K.A.; Chater, K.F. !$#journal Mol. Microbiol. (1995) 18:89-99 !$#title Tissue-specific glycogen branching isoenzymes in a !1multicellular prokaryote, Streptomyces coelicolor A3(2). !$#cross-references MUID:96154943; PMID:8596463 !$#accession S70078 !'##molecule_type DNA !'##residues 1-741 ##label BR2 !'##cross-references EMBL:X73903; NID:g394742; PIDN:CAA52109.1; !1PID:g581619 !'##experimental_source strain A3(2) !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1993 !'##note only a part of the nucleic acid sequence is shown !'##note only a part of the translation is shown GENETICS !$#gene glgBII !$#start_codon GTG FUNCTION !$#description catalyzes the transglycosylation of a terminal segment of a !11,4-alpha-D-glucan chain to an unbranched chain, thereby !1converting amylose to amylopectin or creating branches in !1glycogen !$#pathway glycogen/starch biosynthesis !$#note final step in biosynthesis of glycogen or amylopectin CLASSIFICATION #superfamily 1,4-alpha-glucan branching enzyme KEYWORDS glycogen/starch biosynthesis; glycosyltransferase; !1hexosyltransferase SUMMARY #length 741 #molecular-weight 82784 #checksum 2561 SEQUENCE /// ENTRY S50448 #type complete TITLE 1,4-alpha-glucan branching enzyme (EC 2.4.1.18) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES glycogen branching enzyme; protein YEL011w ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-Nov-1999 ACCESSIONS S50448; A42752 REFERENCE S50428 !$#authors Dietrich, F.S. !$#submission submitted to the EMBL Data Library, December 1994 !$#description Saccharomyces cerevisiae chromosome V cosmids 9871, 8199, !19867, 9495 and lambda clones 6693 and 5898. !$#accession S50448 !'##molecule_type DNA !'##residues 1-704 ##label DIE !'##cross-references EMBL:U18530; NID:g602367; PIDN:AAB64488.1; !1PID:g602378; GSPDB:GN00005; MIPS:YEL011w REFERENCE A42752 !$#authors Thon, V.J.; Vigneron-Lesens, C.; Marianne-Pepin, T.; !1Montreuil, J.; Decq, A.; Rachez, C.; Ball, S.G.; Cannon, !1J.F. !$#journal J. Biol. Chem. (1992) 267:15224-15228 !$#title Coordinate regulation of glycogen metabolism in the yeast !1Saccharomyces cerevisiae. Induction of glycogen branching !1enzyme. !$#cross-references MUID:92340578; PMID:1634552 !$#accession A42752 !'##molecule_type DNA !'##residues 1-563,'T',565-704 ##label THO !'##cross-references EMBL:M76739; NID:g171568; PIDN:AAA34632.1; !1PID:g171569; EMBL:S40655 !'##note sequence extracted from NCBI backbone (NCBIN:109485, !1NCBIP:109486) GENETICS !$#gene SGD:GLC3; MIPS:YEL011w !'##cross-references SGD:S0000737; MIPS:YEL011w !$#map_position 5L FUNCTION !$#description catalyzes the transglycosylation of a terminal segment of a !11,4-alpha-D-glucan chain to an unbranched chain, thereby !1converting amylose to amylopectin or creating branches in !1glycogen !$#pathway glycogen/starch biosynthesis !$#note final step in biosynthesis of glycogen or amylopectin CLASSIFICATION #superfamily 1,4-alpha-glucan branching enzyme KEYWORDS glycogen/starch biosynthesis; glycosyltransferase; !1hexosyltransferase SUMMARY #length 704 #molecular-weight 81115 #checksum 6525 SEQUENCE /// ENTRY S34730 #type complete TITLE 1,4-alpha-glucan branching enzyme (EC 2.4.1.18) precursor, amyloplast - potato ALTERNATE_NAMES starch branching enzyme ORGANISM #formal_name Solanum tuberosum #common_name potato DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 07-Dec-1999 ACCESSIONS S34730; S38733; S38732; S18594 REFERENCE S34730 !$#authors Poulsen, P. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Starch-branching enzyme cDNA from Solanum tuberosum. !$#accession S34730 !'##molecule_type mRNA !'##residues 1-861 ##label POU !'##cross-references EMBL:X69805; NID:g396080; PIDN:CAA49463.1; !1PID:g396081 REFERENCE S38732 !$#authors Khoshnoodi, J.; Ek, B.; Rask, L.; Larsson, H. !$#journal FEBS Lett. (1993) 332:132-138 !$#title Characterization of the 97 and 103 kDa forms of starch !1branching enzyme from potato tubers. !$#cross-references MUID:94009663; PMID:8405428 !$#accession S38733 !'##status preliminary !'##molecule_type protein !'##residues 76-95;236-244,'X', !1246-255;311-329;393-402;515-520;523-529;545-558;'F',636-638, !1'X',640-650 ##label KHO !$#accession S38732 !'##status preliminary !'##molecule_type mRNA !'##residues 318-492,'S',494-538,'K',540-550 ##label KHW REFERENCE S18594 !$#authors Kossmann, J.; Visser, R.G.F.; Mueller-Roeber, B.; !1Willmitzer, L.; Sonnewald, U. !$#journal Mol. Gen. Genet. (1991) 230:39-44 !$#title Cloning and expression analysis of a potato cDNA that !1encodes branching enzyme: evidence for co-expression of !1starch biosynthetic genes. !$#cross-references MUID:92079917; PMID:1745241 !$#accession S18594 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 279-527 ##label KOS GENETICS !$#gene SBE !$#genome nuclear FUNCTION !$#description catalyzes the transglycosylation of a terminal segment of a !11,4-alpha-D-glucan chain to an unbranched chain, thereby !1converting amylose to amylopectin or creating branches in !1glycogen !$#pathway glycogen/starch biosynthesis !$#note final step in biosynthesis of glycogen or amylopectin CLASSIFICATION #superfamily 1,4-alpha-glucan branching enzyme KEYWORDS amyloplast; glycogen/starch biosynthesis; !1glycosyltransferase; hexosyltransferase FEATURE !$1-75 #domain transit peptide (amyloplast) #status !8predicted #label TNP\ !$76-861 #product 1,4-alpha-glucan branching enzyme #status !8experimental #label MAT SUMMARY #length 861 #molecular-weight 99083 #checksum 5621 SEQUENCE /// ENTRY JX0243 #type complete TITLE 1,4-alpha-glucan branching enzyme (EC 2.4.1.18) I precursor - rice ALTERNATE_NAMES amylopectine branching enzyme; Q-enzyme; starch branching enzyme ORGANISM #formal_name Oryza sativa #common_name rice DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 16-Jun-2000 ACCESSIONS JX0243; PS0457; S34037; S30251 REFERENCE JX0243 !$#authors Mizuno, K.; Kimura, K.; Arai, Y.; Kawasaki, T.; Shimada, H.; !1Baba, T. !$#journal J. Biochem. (1992) 112:643-651 !$#title Starch branching enzymes from immature rice seeds. !$#cross-references MUID:93123194; PMID:1478924 !$#accession JX0243 !'##molecule_type mRNA !'##residues 1-820 ##label MIZ !'##cross-references DDBJ:D11082; NID:g218150; PIDN:BAA01855.1; !1PID:g218151 !$#accession PS0457 !'##molecule_type protein !'##residues 65-67,'X',69-81 ##label MI2 REFERENCE S34037 !$#authors Shimada, H.; Kawasaki, T. !$#submission submitted to the EMBL Data Library, March 1992 !$#accession S34037 !'##molecule_type DNA !'##residues 1-714,'LAMMWITSRL',725,'RECQEYQKQISTTALTHS',744,'SFPR',749, !1'VPVW',754-820 ##label SHI !'##cross-references GB:D10838; NID:g287403; PIDN:BAA01616.1; !1PID:g287404 REFERENCE S30251 !$#authors Kawasaki, T.; Mizuno, K.; Baba, T.; Shimada, H. !$#journal Mol. Gen. Genet. (1993) 237:10-16 !$#title Molecular analysis of the gene encoding a rice starch !1branching enzyme. !$#cross-references MUID:93204882; PMID:8455548 !$#accession S30251 !'##molecule_type DNA !'##residues 1-109 ##label KAW !'##cross-references GB:D10838 GENETICS !$#gene sbe1 !$#introns 28/3; 49/3; 119/1; 142/2; 232/2; 534/3; 573/3; 594/3; 630/3; !1664/3; 687/2; 714/2; 753/2 FUNCTION !$#description catalyzes the transglycosylation of a terminal segment of a !11,4-alpha-D-glucan chain to an unbranched chain, thereby !1converting amylose to amylopectin or creating branches in !1glycogen !$#pathway glycogen/starch biosynthesis !$#note final step in biosynthesis of glycogen or amylopectin CLASSIFICATION #superfamily 1,4-alpha-glucan branching enzyme KEYWORDS amyloplast; glycogen/starch biosynthesis; !1glycosyltransferase; hexosyltransferase FEATURE !$1-64 #domain transit peptide (amyloplast) #status !8predicted #label TMM\ !$65-820 #product 1,4-alpha-glucan branching enzyme I, form 1 !8#status experimental #label MAT\ !$67-820 #product 1,4-alpha-glucan branching enzyme I, form 2 !8#status experimental #label MA2 SUMMARY #length 820 #molecular-weight 93236 #checksum 6721 SEQUENCE /// ENTRY JQ0550 #type complete TITLE 1,4-alpha-glucan branching enzyme (EC 2.4.1.18) - Synechococcus sp. (strain PCC 7942) ORGANISM #formal_name Synechococcus sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JQ0550 REFERENCE JQ0550 !$#authors Kiel, J.A.K.W.; Boels, J.M.; Beldman, G.; Venema, G. !$#journal Gene (1990) 89:77-84 !$#title Nucleotide sequence of the Synechococcus sp. PCC7942 !1branching enzyme gene (glgB): expression in Bacillus !1subtilis. !$#cross-references MUID:90323609; PMID:2142668 !$#accession JQ0550 !'##status preliminary !'##molecule_type DNA !'##residues 1-774 ##label KIE !'##cross-references GB:M31544; NID:g142134; PIDN:AAB39038.1; !1PID:g142135 GENETICS !$#gene glgB FUNCTION !$#description catalyzes the transglycosylation of a terminal segment of a !11,4-alpha-D-glucan chain to an unbranched chain, thereby !1converting amylose to amylopectin or creating branches in !1glycogen !$#pathway glycogen/starch biosynthesis !$#note final step in biosynthesis of glycogen or amylopectin CLASSIFICATION #superfamily 1,4-alpha-glucan branching enzyme KEYWORDS glycogen/starch biosynthesis; glycosyltransferase; !1hexosyltransferase SUMMARY #length 774 #molecular-weight 89194 #checksum 8943 SEQUENCE /// ENTRY YUPOY #type complete TITLE starch synthase (EC 2.4.1.21) precursor - potato ALTERNATE_NAMES starch synthase ORGANISM #formal_name Solanum tuberosum #common_name potato DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 02-Aug-2002 ACCESSIONS S16555; S24392; S26060; S26061 REFERENCE S16555 !$#authors van der Leij, F.R.; Visser, R.G.F.; Ponstein, A.S.; !1Jacobsen, E.; Feenstra, W.J. !$#journal Mol. Gen. Genet. (1991) 228:240-248 !$#title Sequence of the structural gene for granule-bound starch !1synthase of potato (Solanum tuberosum L.) and evidence for a !1single point deletion in the amf allele. !$#cross-references MUID:91360072; PMID:1886609 !$#accession S16555 !'##molecule_type DNA !'##residues 1-607 ##label LEI !'##cross-references EMBL:X58453; NID:g21470; PIDN:CAA41359.1; !1PID:g21471 !'##note the authors translated the codon AAC for residue 453 as Gly and !1GCT for residue 455 as Val !$#accession S24392 !'##molecule_type protein !'##residues 78-92,'X',94-98,'XXX',102,'XX',105-107 ##label LE2 REFERENCE S26060 !$#authors Rohde, W.; Becker, D.; Kull, B.; Salamini, F. !$#journal J. Genet. Breed. (1990) 44:311-315 !$#title Structural and functional analysis of two waxy gene !1promoters from potato. !$#accession S26060 !'##molecule_type DNA !'##residues 1-43 ##label ROH1 !'##cross-references EMBL:X52416; NID:g21613; PIDN:CAA36667.1; !1PID:g21614 !'##experimental_source cv. Granola, clone G1 !$#accession S26061 !'##molecule_type DNA !'##residues 1-43 ##label ROH2 !'##cross-references EMBL:X52417; NID:g21615; PIDN:CAA36668.1; !1PID:g21616 !'##experimental_source cv. Granola, clone G28 GENETICS !$#gene waxy !$#genome nuclear !$#introns 111/3; 138/3; 171/3; 201/3; 223/1; 256/3; 293/2; 374/3; 433/ !13; 497/3; 526/3; 569/3 FUNCTION !$#description catalyzes the alpha-1,4-glucosylation of starch by !1ADPglucose producing elongated starch and ADP !$#pathway starch biosynthesis CLASSIFICATION #superfamily starch synthase KEYWORDS amyloplast; glycogen/starch biosynthesis; !1glycosyltransferase; hexosyltransferase FEATURE !$1-77 #domain transit peptide (amyloplast) #status !8predicted #label TNP\ !$78-607 #product ADPglucose-starch glucosyltransferase !8#status experimental #label MAT SUMMARY #length 607 #molecular-weight 66575 #checksum 1902 SEQUENCE /// ENTRY YUBHY #type complete TITLE glycogen(starch) synthase (EC 2.4.1.11) precursor - barley ALTERNATE_NAMES starch synthase ORGANISM #formal_name Hordeum vulgare #common_name barley DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 02-Aug-2002 ACCESSIONS S01727; S01728 REFERENCE S01727 !$#authors Rohde, W.; Becker, D.; Salamini, F. !$#journal Nucleic Acids Res. (1988) 16:7185-7186 !$#title Structural analysis of the waxy locus from Hordeum vulgare. !$#cross-references MUID:88303345; PMID:2970062 !$#accession S01727 !'##molecule_type DNA !'##residues 1-603 ##label ROH !'##cross-references EMBL:X07931; NID:g19126; PIDN:CAA30755.1; !1PID:g295809 !$#accession S01728 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-603 ##label ROH2 !'##cross-references EMBL:X07932; NID:g19128; PIDN:CAA30756.1; !1PID:g19129 GENETICS !$#gene waxy !$#introns 106/3; 133/3; 166/3; 218/1; 251/3; 369/3; 429/3; 493/3; 522/ !13; 565/3 FUNCTION !$#description catalyzes the alpha-1,4-glucosylation of starch by !1UDPglucose producing elongated starch and UDP !$#pathway starch biosynthesis CLASSIFICATION #superfamily starch synthase KEYWORDS amyloplast; glycogen/starch biosynthesis; !1glycosyltransferase; hexosyltransferase FEATURE !$1-72 #domain transit peptide (amyloplast) #status !8predicted #label TNP\ !$73-603 #product UDPglucose-starch glucosyltransferase !8#status predicted #label MAT SUMMARY #length 603 #molecular-weight 66211 #checksum 6457 SEQUENCE /// ENTRY YUWTY #type complete TITLE glycogen(starch) synthase (EC 2.4.1.11) precursor - wheat ALTERNATE_NAMES starch synthase ORGANISM #formal_name Triticum aestivum #common_name common wheat DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 02-Aug-2002 ACCESSIONS S16261; S33636 REFERENCE S16261 !$#authors Clark, J.R.; Robertson, M.; Ainsworth, C.C. !$#journal Plant Mol. Biol. (1991) 16:1099-1101 !$#title Nucleotide sequence of a wheat (Triticum aestivum L.) cDNA !1clone encoding the waxy protein. !$#cross-references MUID:91322506; PMID:1863765 !$#accession S16261 !'##molecule_type mRNA !'##residues 1-615 ##label CLA !'##cross-references EMBL:X57233; NID:g21901; PIDN:CAA40509.1; !1PID:g21902 REFERENCE S33636 !$#authors Ainsworth, C.; Clark, J.; Balsdon, J. !$#journal Plant Mol. Biol. (1993) 22:67-82 !$#title Expression, organisation and structure of the genes encoding !1the waxy protein (granule-bound starch synthase) in wheat. !$#cross-references MUID:93271462; PMID:8499619 !$#accession S33636 !'##molecule_type protein !'##residues 71-75,'X',77-78 ##label AIN GENETICS !$#gene waxy FUNCTION !$#description catalyzes the alpha-1,4-glucosylation of starch by !1UDPglucose producing elongated starch and UDP !$#pathway starch biosynthesis CLASSIFICATION #superfamily starch synthase KEYWORDS amyloplast; glycogen/starch biosynthesis; !1glycosyltransferase; hexosyltransferase FEATURE !$1-70 #domain transit peptide (amyloplast) #status !8predicted #label TNP\ !$71-615 #product UDPglucose-starch glucosyltransferase !8#status experimental #label MAT SUMMARY #length 615 #molecular-weight 67751 #checksum 2249 SEQUENCE /// ENTRY S07314 #type complete TITLE glycogen(starch) synthase (EC 2.4.1.11) precursor - maize ALTERNATE_NAMES starch synthase; UDP-glucose starch glycosyltransferase, starch granule-bound ORGANISM #formal_name Zea mays #common_name maize DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 02-Aug-2002 ACCESSIONS S07314 REFERENCE S07314 !$#authors Kloesgen, R.B.; Gierl, A.; Schwarz-Sommer, Z.; Saedler, H. !$#journal Mol. Gen. Genet. (1986) 203:237-244 !$#title Molecular analysis of the waxy locus of Zea mays. !$#accession S07314 !'##molecule_type DNA !'##residues 1-605 ##label KLO !'##cross-references EMBL:X03935; NID:g22509; PIDN:CAA27574.1; !1PID:g1644339 !'##experimental_source line C !'##note translation of the nucleotide sequence is not complete !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing GENETICS !$#gene waxy !$#introns 107/3; 134/3; 167/3; 197/3; 219/1; 252/3; 289/2; 370/3; 431/ !13; 495/3; 524/3; 567/3 FUNCTION !$#description catalyzes the alpha-1,4-glucosylation of starch by !1UDPglucose producing elongated starch and UDP CLASSIFICATION #superfamily starch synthase KEYWORDS amyloplast; chloroplast; glycogen/starch biosynthesis; !1glycosyltransferase; hexosyltransferase FEATURE !$1-72 #domain transit peptide (amyloplast) #status !8predicted #label TNP\ !$73-605 #product glycogen (starch) synthase #status !8experimental #label MAT SUMMARY #length 605 #molecular-weight 65966 #checksum 8954 SEQUENCE /// ENTRY SYECGL #type complete TITLE starch synthase (EC 2.4.1.21) - Escherichia coli (strain K-12) ALTERNATE_NAMES bacterial-glycogen synthase; glycogen synthase ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 17-Oct-1997 #text_change 02-Aug-2002 ACCESSIONS H65138; A26327 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65138 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-477 ##label BLAT !'##cross-references GB:AE000419; GB:U00096; NID:g2367227; !1PIDN:AAC76454.1; PID:g1789836; UWGP:b3429 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A26327 !$#authors Kumar, A.; Larsen, C.E.; Preiss, J. !$#journal J. Biol. Chem. (1986) 261:16256-16259 !$#title Biosynthesis of bacterial glycogen. Primary structure of !1Escherichia coli ADP-glucose:alpha-1,4-glucan, !14-glucosyltransferase as deduced from the nucleotide !1sequence of the glgA gene. !$#cross-references MUID:87057301; PMID:3097003 !$#accession A26327 !'##molecule_type mRNA !'##residues 1-62,'S',64-101,'VH',104-244,'P',246-279,'S',281-285,'S', !1287-308,'S',310-313,'S',315-316,'SS',319-386,'S',388-418, !1'N',420-421,'I',423-433,'T',435-443,'C',445,'P',447-460,'G', !1462-475,'S',477 ##label KUM !'##cross-references GB:J02616; NID:g146138; PIDN:AAA23870.1; !1PID:g146139 COMMENT In bacteria, this enzyme catalyzes the synthesis of an !1alpha-1,4-glucan chain from a preexisting primer using !1ADP-glucose as the glycosyl donor. GENETICS !$#gene glgA !$#map_position 75 min FUNCTION !$#description catalyzes the alpha-1,4-glucosylation of bacterial glycogen !1by ADPglucose producing elongated bacterial glycogen and ADP !$#pathway bacterial glycogen biosynthesis CLASSIFICATION #superfamily starch synthase KEYWORDS glycogen/starch biosynthesis; glycosyltransferase; !1hexosyltransferase SUMMARY #length 477 #molecular-weight 52822 #checksum 3433 SEQUENCE /// ENTRY JC4695 #type complete TITLE glycogenin glucosyltransferase (EC 2.4.1.186) - human ALTERNATE_NAMES glycogenin CONTAINS glycogen(starch) synthase, glycogenin subunit ORGANISM #formal_name Homo sapiens #common_name man DATE 21-May-1999 #sequence_revision 21-May-1999 #text_change 11-Jun-1999 ACCESSIONS JC4695; G01948; S45141 REFERENCE JC4695 !$#authors Barbetti, F.; Rocchi, M.; Bossolasco, M.; Cordera, R.; !1Sbraccia, P.; Finelli, P.; Consalez, G.G. !$#journal Biochem. Biophys. Res. Commun. (1996) 220:72-77 !$#title The human skeletal muscle glycogenin gene: cDNA, tissue !1expression, and chromosomal localization. !$#cross-references MUID:96176958; PMID:8602861 !$#accession JC4695 !'##molecule_type mRNA !'##residues 1-333 ##label BAR !'##cross-references GB:U44131; NID:g1174166; PIDN:AAB00114.1; !1PID:g1174167 !'##experimental_source skeletal muscle REFERENCE G08914 !$#authors Rodriguez, I.R. !$#submission submitted to the EMBL Data Library, July 1995 !$#accession G01948 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-333 ##label ROD !'##cross-references EMBL:U31525; NID:g976399; PIDN:AAB09752.1; !1PID:g976400 REFERENCE S45140 !$#authors Leffers, H.; Wiemann, S.; Ansorge, W. !$#submission submitted to the EMBL Data Library, June 1994 !$#description Cloning and sequencing of a cDNA encoding human glycogenin. !$#accession S45141 !'##molecule_type mRNA !'##residues 1-203,'KMSQEPYHICPLGRSQLWHSRLYPRKNGR', !1'NDGNRARLIIWEQIPLTTSRGNLTLTSSR','NTAFFCEHIHFTSLVSDT' ##label !1LEF !'##cross-references EMBL:X79537; NID:g496894; PIDN:CAA56073.1; !1PID:g496895 GENETICS !$#gene GDB:GYG !'##cross-references GDB:1326953 !$#map_position 3q24-3q25.1 FUNCTION !$#description catalyzes the alpha-glucosylation of itself on a specific !1tyrosine residue by UDPglucose to produce glucosyl-glcogenin !1and UDP; catalyzes the subsequent alpha-1,4-glucosylation of !1glucosyl-glycogenin by UDPglucose to produce glycogen and !1UDP !$#pathway glycogen/starch biosynthesis !$#note required to initiate the synthesis of glycogen CLASSIFICATION #superfamily glycogenin KEYWORDS acetylated amino end; glycogen/starch biosynthesis; !1glycoprotein; glycosyltransferase; hexosyltransferase FEATURE !$2 #modified_site acetylated amino end (Thr) (in mature !8form) #status predicted\ !$195 #binding_site carbohydrate (Tyr) (covalent) #status !8predicted SUMMARY #length 333 #molecular-weight 37478 #checksum 6069 SEQUENCE /// ENTRY A45094 #type complete TITLE glycogenin glucosyltransferase (EC 2.4.1.186) - rabbit ALTERNATE_NAMES glycogen synthase 38K chain; glycogenin ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 21-May-1999 #sequence_revision 21-May-1999 #text_change 11-Jun-1999 ACCESSIONS A45094; S06482; S02470 REFERENCE A45094 !$#authors Viskupic, E.; Cao, Y.; Zhang, W.; Cheng, C.; DePaoli-Roach, !1A.A.; Roach, P.J. !$#journal J. Biol. Chem. (1992) 267:25759-25763 !$#title Rabbit skeletal muscle glycogenin. Molecular cloning and !1production of fully functional protein in Escherichia coli. !$#cross-references MUID:93100288; PMID:1281472 !$#accession A45094 !'##molecule_type mRNA !'##residues 1-332 ##label VIS !'##cross-references GB:L01791; NID:g165512; PIDN:AAA31404.1; !1PID:g165513 !'##experimental_source skeletal muscle !'##note sequence is inconsistent with the nucleotide translation !'##note sequence extracted from NCBI backbone (NCBIP:120846) REFERENCE S06482 !$#authors Campbell, D.G.; Cohen, P. !$#journal Eur. J. Biochem. (1989) 185:119-125 !$#title The amino acid sequence of rabbit skeletal muscle !1glycogenin. !$#cross-references MUID:90032666; PMID:2806254 !$#accession S06482 !'##molecule_type protein !'##residues 1-87,'S',89-96,'L',98-332 ##label CAM REFERENCE S02470 !$#authors Pitcher, J.; Smythe, C.; Campbell, D.G.; Cohen, P. !$#journal Eur. J. Biochem. (1987) 169:497-502 !$#title Identification of the 38-kDa subunit of rabbit skeletal !1muscle glycogen synthase as glycogenin. !$#cross-references MUID:88082782; PMID:3121316 !$#accession S02470 !'##molecule_type protein !'##residues 9-19;38-44,'M';90-94;204-207,'F',209-210,'KH',213-219 !1##label PIT FUNCTION !$#description catalyzes the alpha-glucosylation of itself on a specific !1tyrosine residue by UDPglucose to produce glucosyl-glcogenin !1and UDP; catalyzes the subsequent alpha-1,4-glucosylation of !1glucosyl-glycogenin by UDPglucose to produce glycogen and !1UDP !$#pathway glycogen/starch biosynthesis !$#note required to initiate the synthesis of glycogen CLASSIFICATION #superfamily glycogenin KEYWORDS acetylated amino end; glycogen/starch biosynthesis; !1glycoprotein; glycosyltransferase; hexosyltransferase FEATURE !$1 #modified_site acetylated amino end (Thr) #status !8experimental\ !$194 #binding_site carbohydrate (Tyr) (covalent) #status !8experimental SUMMARY #length 332 #molecular-weight 37266 #checksum 1782 SEQUENCE /// ENTRY S45879 #type complete TITLE chitin synthase (EC 2.4.1.16) 3 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YBR023c; protein YBR0305 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-Nov-1999 ACCESSIONS S45879; S46554; S22776; A39639; S17247 REFERENCE S45875 !$#authors Grivell, L.A.; de Haan, M.; Maat, M.J.; Smits, P.H.M. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S45879 !'##molecule_type DNA !'##residues 1-1165 ##label GRI !'##cross-references EMBL:Z35892; NID:g536229; PIDN:CAA84965.1; !1PID:g536230; GSPDB:GN00002; MIPS:YBR023c !'##experimental_source strain S288C REFERENCE S46551 !$#authors Smits, P.H.M.; de Haan, M.; Maat, C.; Grivell, L.A. !$#journal Yeast (1994) 10(Suppl.A):S75-S80 !$#title The complete sequence of a 33 kb fragment on the right arm !1of chromosome II from Saccharomyces cerevisiae reveals 16 !1open reading frames, including ten new open reading frames, !1five previously identified genes and a homologue of the SCO1 !1gene. !$#cross-references MUID:94378725; PMID:8091864 !$#accession S46554 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1165 ##label SMI !'##cross-references EMBL:X76078; NID:g498748; PIDN:CAA53680.1; !1PID:g498752 !'##experimental_source strain S288C !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1993 REFERENCE S22776 !$#authors Bulawa, C.E. !$#journal Mol. Cell. Biol. (1992) 12:1764-1776 !$#title CSD2, CSD3, and CSD4, genes required for chitin synthesis in !1Saccharomyces cerevisiae: the CSD2 gene product is related !1to chitin synthases and to developmentally regulated !1proteins in Rhizobium species and Xenopus laevis. !$#cross-references MUID:92195323; PMID:1532231 !$#accession S22776 !'##molecule_type DNA !'##residues 1-1162,'L',1164-1165 ##label BUL !'##cross-references EMBL:M73697; NID:g172103; PIDN:AAA34844.1; !1PID:g172104 REFERENCE A39639 !$#authors Valdivieso, M.H.; Mol, P.C.; Shaw, J.A.; Cabib, E.; Duran, !1A. !$#journal J. Cell Biol. (1991) 114:101-109 !$#title CAL1, a gene required for activity of chitin synthase 3 in !1Saccharomyces cerevisiae. !$#cross-references MUID:91268144; PMID:2050737 !$#accession A39639 !'##molecule_type DNA !'##residues 67-1165 ##label VAL !'##cross-references GB:X57300; NID:g3359; PIDN:CAA40559.1; PID:g3360 GENETICS !$#gene SGD:CHS3; CAL1; CSD2; MIPS:YBR023c !'##cross-references MIPS:YBR023c; SGD:S0000227 !$#map_position 2R FUNCTION !$#description catalyzes the alpha-1,4-glycosylation of chitin by !1UDP-N-acetyl-D-glucosamine producing elongated chitin and !1UDP CLASSIFICATION #superfamily chitin synthase chs4 KEYWORDS chitin biosynthesis; glycosyltransferase; !1hexosyltransferase; transmembrane protein FEATURE !$203-219 #domain transmembrane #status predicted #label TM1\ !$457-473 #domain transmembrane #status predicted #label TM2\ !$1018-1034 #domain transmembrane #status predicted #label TM3\ !$1035-1054 #domain transmembrane #status predicted #label TM4\ !$1060-1076 #domain transmembrane #status predicted #label TM5\ !$1084-1100 #domain transmembrane #status predicted #label TM6 SUMMARY #length 1165 #molecular-weight 131600 #checksum 128 SEQUENCE /// ENTRY A70004 #type complete TITLE probable hexosyltransferase (EC 2.4.1.-) ytxN - Bacillus subtilis ALTERNATE_NAMES lipopolysaccharide N-acetylglucosaminyltransferase ytxN ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A70004 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A70004 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-377 ##label KUN !'##cross-references GB:Z99119; GB:AL009126; NID:g2635411; !1PIDN:CAB15069.1; PID:g2635575 !'##experimental_source strain 168 GENETICS !$#gene ytxN CLASSIFICATION #superfamily probable hexosyltransferase ytxN KEYWORDS glycosyltransferase; hexosyltransferase SUMMARY #length 377 #molecular-weight 42912 #checksum 8522 SEQUENCE /// ENTRY A69989 #type complete TITLE probable hexosyltransferase (EC 2.4.1.-) ytcC - Bacillus subtilis ALTERNATE_NAMES lipopolysaccharide N-acetylglucosaminyltransferase ytcC ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A69989 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69989 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-407 ##label KUN !'##cross-references GB:Z99119; GB:AL009126; NID:g2635411; !1PIDN:CAB15066.1; PID:g2635572 !'##experimental_source strain 168 GENETICS !$#gene ytcC CLASSIFICATION #superfamily probable hexosyltransferase ytxN KEYWORDS glycosyltransferase; hexosyltransferase SUMMARY #length 407 #molecular-weight 46160 #checksum 1898 SEQUENCE /// ENTRY F64500 #type complete TITLE probable hexosyltransferase (EC 2.4.1.-) MJ1607 - Methanococcus jannaschii ALTERNATE_NAMES probable lipopolysaccharide N-acetylglucosaminyltransferase rfbU ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F64500 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession F64500 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-390 ##label BUL !'##cross-references GB:U67601; GB:L77117; NID:g2826439; !1PIDN:AAB99629.1; PID:g1500505; TIGR:MJ1607 GENETICS !$#map_position FOR1581714-1582886 CLASSIFICATION #superfamily probable hexosyltransferase ytxN KEYWORDS glycosyltransferase; hexosyltransferase SUMMARY #length 390 #molecular-weight 44446 #checksum 8641 SEQUENCE /// ENTRY S77553 #type complete TITLE probable hexosyltransferase (EC 2.4.1.-) sll1971 [similarity] - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 16-Jun-2000 ACCESSIONS S77553 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S77553 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-404 ##label KAN !'##cross-references EMBL:D90905; GB:AB001339; NID:g1652360; !1PIDN:BAA17400.1; PID:g1652478 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily probable hexosyltransferase ytxN KEYWORDS glycosyltransferase; hexosyltransferase SUMMARY #length 404 #molecular-weight 46174 #checksum 5588 SEQUENCE /// ENTRY C70859 #type complete TITLE probable hexosyltransferase (EC 2.4.1.-) Rv3032 [similarity] - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 16-Jun-2000 ACCESSIONS C70859 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession C70859 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-414 ##label COL !'##cross-references GB:AL021287; GB:AL123456; NID:g3261508; !1PIDN:CAA16117.1; PID:g2791630 !'##experimental_source strain H37Rv GENETICS !$#gene Rv3032 CLASSIFICATION #superfamily probable hexosyltransferase ytxN KEYWORDS glycosyltransferase; hexosyltransferase SUMMARY #length 414 #molecular-weight 44805 #checksum 644 SEQUENCE /// ENTRY T34839 #type complete TITLE probable hexosyltransferase (EC 2.4.1.-) SC2G5.06 [similarity] - Streptomyces coelicolor ALTERNATE_NAMES probable transferase ORGANISM #formal_name Streptomyces coelicolor DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS T34839 REFERENCE Z21559 !$#authors Oliver, K.; Harris, D.; Bentley, S.D.; Parkhill, J.; !1Barrell, B.G.; Rajandream, M.A. !$#submission submitted to the EMBL Data Library, February 1999 !$#accession T34839 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-406 ##label OLI !'##cross-references EMBL:AL035478; PIDN:CAB36593.1; GSPDB:GN00070; !1SCOEDB:SC2G5.06 !'##experimental_source strain A3(2) GENETICS !$#gene SCOEDB:SC2G5.06 CLASSIFICATION #superfamily probable hexosyltransferase ytxN KEYWORDS glycosyltransferase; hexosyltransferase SUMMARY #length 406 #molecular-weight 43630 #checksum 791 SEQUENCE /// ENTRY S72892 #type complete TITLE probable hexosyltransferase (EC 2.4.1.-) B2168_C2_201 [similarity] - Mycobacterium leprae ORGANISM #formal_name Mycobacterium leprae DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 23-Mar-2001 ACCESSIONS S72892 REFERENCE S72586 !$#authors Smith, D.R.; Robison, K. !$#submission submitted to the EMBL Data Library, November 1993 !$#description Mycobacterium leprae cosmid B2168. !$#accession S72892 !'##molecule_type DNA !'##residues 1-409 ##label SMI !'##cross-references EMBL:U00018; NID:g467037; PIDN:AAA17228.1; !1PID:g467044 CLASSIFICATION #superfamily probable hexosyltransferase ytxN KEYWORDS glycosyltransferase; hexosyltransferase SUMMARY #length 409 #molecular-weight 43517 #checksum 5726 SEQUENCE /// ENTRY A70744 #type complete TITLE probable hexosyltransferase (EC 2.4.1.-) Rv0486 [similarity] - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 16-Jun-2000 ACCESSIONS A70744 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession A70744 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-480 ##label COL !'##cross-references GB:Z77162; GB:AL123456; NID:g3261606; !1PIDN:CAB00947.1; PID:g1449284 !'##experimental_source strain H37Rv GENETICS !$#gene Rv0486 CLASSIFICATION #superfamily probable hexosyltransferase ytxN KEYWORDS glycosyltransferase; hexosyltransferase SUMMARY #length 480 #molecular-weight 50541 #checksum 3018 SEQUENCE /// ENTRY D70351 #type complete TITLE probable hexosyltransferase (EC 2.4.1.-) aq_572 [similarity] - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS D70351 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession D70351 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-366 ##label AQF !'##cross-references GB:AE000696; NID:g2983196; PIDN:AAC06809.1; !1PID:g2983210; GB:AE000657 !'##experimental_source strain VF5 GENETICS !$#gene aq_572 CLASSIFICATION #superfamily probable hexosyltransferase ytxN KEYWORDS glycosyltransferase; hexosyltransferase SUMMARY #length 366 #molecular-weight 41541 #checksum 7585 SEQUENCE /// ENTRY A75033 #type complete TITLE probable hexosyltransferase (EC 2.4.1.-) PAB0827 [similarity] - Pyrococcus abyssi (strain Orsay) ALTERNATE_NAMES galactosyltransferase; LPS biosynthesis rfbU related protein ORGANISM #formal_name Pyrococcus abyssi DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 16-Jun-2000 ACCESSIONS A75033 REFERENCE A75001 !$#authors anonymous, Genoscope !$#submission submitted to the EMBL Data Library, July 1999 !$#description Pyrococcus abyssi genome sequence: insights into archaeal !1chromosome structure and evolution. !$#accession A75033 !'##molecule_type DNA !'##residues 1-371 ##label KAW !'##cross-references GB:AJ248287; GB:AL096836; NID:g5458657; !1PIDN:CAB50158.1; PID:g5458671 !'##experimental_source strain Orsay GENETICS !$#gene PAB0827 CLASSIFICATION #superfamily probable hexosyltransferase ytxN KEYWORDS glycosyltransferase; hexosyltransferase SUMMARY #length 371 #molecular-weight 40748 #checksum 8709 SEQUENCE /// ENTRY D72511 #type complete TITLE probable hexosyltransferase (EC 2.4.1.-) APE2066 [similarity] - Aeropyrum pernix (strain K1) ALTERNATE_NAMES probable N-acetylglucosaminyl-phosphatidylinositol biosynthetic protein ORGANISM #formal_name Aeropyrum pernix DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 16-Jun-2000 ACCESSIONS D72511 REFERENCE A72450 !$#authors Kawarabayasi, Y.; Hino, Y.; Horikawa, H.; Yamazaki, S.; !1Haikawa, Y.; Jin-no, K.; Takahashi, M.; Sekine, M.; Baba, !1S.; Ankai, A.; Kosugi, H.; Hosoyama, A.; Fukui, S.; Nagai, !1Y.; Nishijima, K.; Nakazawa, H.; Takamiya, M.; Masuda, S.; !1Funahashi, T.; Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, !1N.; Oguchi, A.; Aoki, K.; Kubota, K.; Nakamura, Y.; Nomura, !1N.; Sako, Y.; Kikuchi, H. !$#journal DNA Res. (1999) 6:83-101 !$#title Complete genome sequence of an aerobic hyper-thermophilic !1Crenarchaeon, Aeropyrum pernix K1. !$#cross-references MUID:99310339; PMID:10382966 !$#accession D72511 !'##molecule_type DNA !'##residues 1-392 ##label KAW !'##cross-references DDBJ:AP000063; NID:g5105654; PIDN:BAA81076.1; !1PID:g5105764 !'##experimental_source strain K1 GENETICS !$#gene APE2066 CLASSIFICATION #superfamily probable hexosyltransferase ytxN KEYWORDS glycosyltransferase; hexosyltransferase SUMMARY #length 392 #molecular-weight 43397 #checksum 5919 SEQUENCE /// ENTRY A75059 #type complete TITLE probable hexosyltransferase (EC 2.4.1.-) PAB0973 [similarity] - Pyrococcus abyssi (strain Orsay) ALTERNATE_NAMES LPS biosynthesis rfbU related protein ORGANISM #formal_name Pyrococcus abyssi DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 16-Jun-2000 ACCESSIONS A75059 REFERENCE A75001 !$#authors anonymous, Genoscope !$#submission submitted to the EMBL Data Library, July 1999 !$#description Pyrococcus abyssi genome sequence: insights into archaeal !1chromosome structure and evolution. !$#accession A75059 !'##molecule_type DNA !'##residues 1-390 ##label KAW !'##cross-references GB:AJ248287; GB:AL096836; NID:g5458657; !1PIDN:CAB50366.1; PID:g5458879 !'##experimental_source strain Orsay GENETICS !$#gene PAB0973 CLASSIFICATION #superfamily probable hexosyltransferase ytxN KEYWORDS glycosyltransferase; hexosyltransferase SUMMARY #length 390 #molecular-weight 44025 #checksum 4142 SEQUENCE /// ENTRY A70571 #type complete TITLE probable hexosyltransferase (EC 2.4.1.-) Rv2610c [similarity] - Mycobacterium tuberculosis (strain H37RV) ALTERNATE_NAMES probable glycosyltransferase ORGANISM #formal_name Mycobacterium tuberculosis DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 16-Jun-2000 ACCESSIONS A70571 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession A70571 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-378 ##label COL !'##cross-references GB:Z95387; GB:AL123456; NID:g3261763; !1PIDN:CAB08632.1; PID:g2104303 !'##experimental_source strain H37Rv GENETICS !$#gene Rv2610c CLASSIFICATION #superfamily probable hexosyltransferase ytxN KEYWORDS glycosyltransferase; hexosyltransferase SUMMARY #length 378 #molecular-weight 40445 #checksum 1867 SEQUENCE /// ENTRY C72590 #type complete TITLE probable hexosyltransferase (EC 2.4.1.-) APE1191 [similarity] - Aeropyrum pernix (strain K1) ALTERNATE_NAMES probable capM protein ORGANISM #formal_name Aeropyrum pernix DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 16-Jun-2000 ACCESSIONS C72590 REFERENCE A72450 !$#authors Kawarabayasi, Y.; Hino, Y.; Horikawa, H.; Yamazaki, S.; !1Haikawa, Y.; Jin-no, K.; Takahashi, M.; Sekine, M.; Baba, !1S.; Ankai, A.; Kosugi, H.; Hosoyama, A.; Fukui, S.; Nagai, !1Y.; Nishijima, K.; Nakazawa, H.; Takamiya, M.; Masuda, S.; !1Funahashi, T.; Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, !1N.; Oguchi, A.; Aoki, K.; Kubota, K.; Nakamura, Y.; Nomura, !1N.; Sako, Y.; Kikuchi, H. !$#journal DNA Res. (1999) 6:83-101 !$#title Complete genome sequence of an aerobic hyper-thermophilic !1Crenarchaeon, Aeropyrum pernix K1. !$#cross-references MUID:99310339; PMID:10382966 !$#accession C72590 !'##molecule_type DNA !'##residues 1-363 ##label KAW !'##cross-references DDBJ:AP000061; NID:g5104821; PIDN:BAA80177.1; !1PID:g5104863 !'##experimental_source strain K1 GENETICS !$#gene APE1191 CLASSIFICATION #superfamily probable hexosyltransferase ytxN KEYWORDS glycosyltransferase; hexosyltransferase SUMMARY #length 363 #molecular-weight 41409 #checksum 2568 SEQUENCE /// ENTRY F69142 #type complete TITLE probable hexosyltransferase (EC 2.4.1.-) MTH332 [similarity] - Methanobacterium thermoautotrophicum (strain Delta H) ALTERNATE_NAMES LPS biosynthesis rfbU related protein ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS F69142 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession F69142 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-400 ##label MTH !'##cross-references GB:AE000818; GB:AE000666; NID:g2621384; !1PIDN:AAB84838.1; PID:g2621388 !'##experimental_source strain Delta H GENETICS !$#gene MTH332 CLASSIFICATION #superfamily probable hexosyltransferase ytxN KEYWORDS glycosyltransferase; hexosyltransferase SUMMARY #length 400 #molecular-weight 46160 #checksum 9654 SEQUENCE /// ENTRY F69254 #type complete TITLE probable hexosyltransferase (EC 2.4.1.-) AF0038 [similarity] - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS F69254 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession F69254 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-361 ##label KLE !'##cross-references GB:AE001104; GB:AE000782; NID:g2689427; !1PIDN:AAB91191.1; PID:g2650614; TIGR:AF0038 CLASSIFICATION #superfamily probable hexosyltransferase ytxN KEYWORDS glycosyltransferase; hexosyltransferase SUMMARY #length 361 #molecular-weight 41271 #checksum 4611 SEQUENCE /// ENTRY G69290 #type complete TITLE probable hexosyltransferase (EC 2.4.1.-) AF0327 [similarity] - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS G69290 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession G69290 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-357 ##label KLE !'##cross-references GB:AE001082; GB:AE000782; NID:g2689405; !1PIDN:AAB90909.1; PID:g2650310; TIGR:AF0327 CLASSIFICATION #superfamily probable hexosyltransferase ytxN KEYWORDS glycosyltransferase; hexosyltransferase SUMMARY #length 357 #molecular-weight 40406 #checksum 2503 SEQUENCE /// ENTRY G75058 #type complete TITLE probable hexosyltransferase (EC 2.4.1.-) PAB1410 [similarity] - Pyrococcus abyssi (strain Orsay) ALTERNATE_NAMES LPS biosynthesis rfbU related protein ORGANISM #formal_name Pyrococcus abyssi DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 16-Jun-2000 ACCESSIONS G75058 REFERENCE A75001 !$#authors anonymous, Genoscope !$#submission submitted to the EMBL Data Library, July 1999 !$#description Pyrococcus abyssi genome sequence: insights into archaeal !1chromosome structure and evolution. !$#accession G75058 !'##molecule_type DNA !'##residues 1-368 ##label KAW !'##cross-references GB:AJ248287; GB:AL096836; NID:g5458657; !1PIDN:CAB50364.1; PID:g5458877 !'##experimental_source strain Orsay GENETICS !$#gene PAB1410 CLASSIFICATION #superfamily probable hexosyltransferase ytxN KEYWORDS glycosyltransferase; hexosyltransferase SUMMARY #length 368 #molecular-weight 42429 #checksum 7457 SEQUENCE /// ENTRY C69098 #type complete TITLE probable hexosyltransferase (EC 2.4.1.-) MTH173 - Methanobacterium thermoautotrophicum (strain Delta H) ALTERNATE_NAMES lipopolysaccharide N-acetylglucosaminyltransferase rfbU ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jan-2000 ACCESSIONS C69098 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession C69098 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-382 ##label MTH !'##cross-references GB:AE000805; GB:AE000666; NID:g2621213; !1PIDN:AAB84679.1; PID:g2621216 !'##experimental_source strain Delta H GENETICS !$#gene MTH173 !$#start_codon GTG CLASSIFICATION #superfamily probable hexosyltransferase ytxN KEYWORDS glycosyltransferase; hexosyltransferase SUMMARY #length 382 #molecular-weight 42635 #checksum 7496 SEQUENCE /// ENTRY H64446 #type complete TITLE probable hexosyltransferase (EC 2.4.1.-) MJ1178 [similarity] - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 21-Jul-2000 ACCESSIONS H64446 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession H64446 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-351 ##label BUL !'##cross-references GB:U67559; GB:L77117; NID:g1591798; !1PIDN:AAB99181.1; PID:g1591805; TIGR:MJ1178 GENETICS !$#map_position REV1117459-1116404 !$#start_codon GTG CLASSIFICATION #superfamily probable hexosyltransferase ytxN KEYWORDS glycosyltransferase; hexosyltransferase SUMMARY #length 351 #molecular-weight 39863 #checksum 6338 SEQUENCE /// ENTRY G70961 #type complete TITLE probable hexosyltransferase (EC 2.4.1.-) Rv0225 [similarity] - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 16-Jun-2000 ACCESSIONS G70961 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession G70961 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-384 ##label COL !'##cross-references GB:Z92669; GB:AL123456; NID:g3242271; !1PIDN:CAB06992.1; PID:g1871598 !'##experimental_source strain H37Rv GENETICS !$#gene Rv0225 CLASSIFICATION #superfamily probable hexosyltransferase ytxN KEYWORDS glycosyltransferase; hexosyltransferase SUMMARY #length 384 #molecular-weight 42054 #checksum 3565 SEQUENCE /// ENTRY A45049 #type complete TITLE 4-alpha-glucanotransferase (EC 2.4.1.25) - potato ALTERNATE_NAMES amylomaltase; D-enzyme; disproportionating enzyme ORGANISM #formal_name Solanum tuberosum #common_name potato DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A45049 REFERENCE A45049 !$#authors Takaha, T.; Yanase, M.; Okada, S.; Smith, S.M. !$#journal J. Biol. Chem. (1993) 268:1391-1396 !$#title Disproportionating enzyme (4-alpha-glucanotransferase; EC !12.4.1.25) of potato. Purification, molecular cloning, and !1potential role in starch metabolism. !$#cross-references MUID:93123262; PMID:7678257 !$#accession A45049 !'##status preliminary !'##molecule_type mRNA !'##residues 1-576 ##label TAK !'##cross-references GB:X68664; GB:S52648; NID:g296691; PIDN:CAA48630.1; !1PID:g296692 !'##experimental_source cv. May Queen, tubers !'##note sequence extracted from NCBI backbone (NCBIN:122077, !1NCBIP:122078) CLASSIFICATION #superfamily 4-alpha-glucanotransferase KEYWORDS chloroplast; glycosyltransferase; hexosyltransferase SUMMARY #length 576 #molecular-weight 64950 #checksum 1489 SEQUENCE /// ENTRY C65137 #type complete TITLE 4-alpha-glucanotransferase (EC 2.4.1.25) - Escherichia coli (strain K-12) ALTERNATE_NAMES amylomaltase ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS C65137; S03774 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65137 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-694 ##label BLAT !'##cross-references GB:AE000417; GB:U00096; NID:g2367220; !1PIDN:AAC76441.1; PID:g1789821; UWGP:b3416 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S03773 !$#authors Pugsley, A.P.; Dubreuil, C. !$#journal Mol. Microbiol. (1988) 2:473-479 !$#title Molecular characterization of malQ, the structural gene for !1the Escherichia coli enzyme amylomaltase. !$#cross-references MUID:89013888; PMID:2845225 !$#accession S03774 !'##molecule_type DNA !'##residues 1-21,'P',23-198,'TA',201-379,'GT',382-461,'R',463-694 !1##label PUG !'##cross-references EMBL:M32793; NID:g146713; PIDN:AAA24106.1; !1PID:g146715 !'##note the authors translated the codon CCC for residue 22 as Ala, GAG !1for residue 71 as Phe, CGC for residue 462 as Gly, and GAG !1for residue 527 as Phe GENETICS !$#gene malQ !$#map_position 75 min CLASSIFICATION #superfamily 4-alpha-glucanotransferase KEYWORDS glycosyltransferase; hexosyltransferase SUMMARY #length 694 #molecular-weight 78503 #checksum 5428 SEQUENCE /// ENTRY XUBPB4 #type complete TITLE DNA beta-glucosyltransferase (EC 2.4.1.27) - phage T4 ALTERNATE_NAMES gp beta-gt ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 11-Jun-1999 ACCESSIONS A00576; B00576 REFERENCE A00576 !$#authors Tomaschewski, J.; Gram, H.; Crabb, J.W.; Ruger, W. !$#journal Nucleic Acids Res. (1985) 13:7551-7568 !$#title T4-induced alpha- and beta-glucosyltransferase: cloning of !1the genes and a comparison of their products based on !1sequencing data. !$#cross-references MUID:86067181; PMID:2999696 !$#accession A00576 !'##molecule_type DNA !'##residues 1-351 ##label TOM !'##cross-references GB:K03111; NID:g215824; PIDN:CAA26908.1; !1PID:g215825; EMBL:X03139; NID:g15250; PID:g15252 !$#accession B00576 !'##molecule_type protein !'##residues 1-30 ##label TO2 COMMENT The enzyme catalyzes the transfer of the sugar from UDPG to !1the hydroxymethyl group of 5-HMC. COMMENT Active form of the enzyme is dimer. GENETICS !$#gene beta-gt !$#map_position 24.076-25.129 CLASSIFICATION #superfamily phage T4 DNA beta-glucosyltransferase KEYWORDS dimer; glycosyltransferase; hexosyltransferase SUMMARY #length 351 #molecular-weight 40666 #checksum 9386 SEQUENCE /// ENTRY XUBPA4 #type complete TITLE DNA alpha-glucosyltransferase (EC 2.4.1.26) - phage T4 ALTERNATE_NAMES laminaribiose phosphorylase [misidentification] ORGANISM #formal_name phage T4 DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 04-Feb-2000 ACCESSIONS A00577; T10157 REFERENCE A91016 !$#authors Gram, H.; Ruger, W. !$#journal EMBO J. (1985) 4:257-264 !$#title Genes 55, alpha-gt, 47 and 46 of bacteriophage T4: the !1genomic organization as deduced by sequence analysis. !$#cross-references MUID:85257446; PMID:4018026 !$#accession A00577 !'##molecule_type DNA !'##residues 1-400 ##label GRA !'##cross-references GB:X01804; NID:g15229; PIDN:CAA25940.1; PID:g15236 GENETICS !$#gene alpha-gt CLASSIFICATION #superfamily DNA alpha-glucosyltransferase KEYWORDS glycosyltransferase; hexosyltransferase SUMMARY #length 400 #molecular-weight 46704 #checksum 5040 SEQUENCE /// ENTRY JC5432 #type complete TITLE glycoprotein 6-alpha-L-fucosyltransferase (EC 2.4.1.68) precursor - human ALTERNATE_NAMES alpha 1-6 FucT; GDP-L-fucose:N-acetyl-beta-D-glucosaminyl:6-alpha-L-fucosylt ransferase; GDPfucose-glycoprotein fucosyltransferase ORGANISM #formal_name Homo sapiens #common_name man DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 16-Jun-2000 ACCESSIONS JC5432; PC4322 REFERENCE JC5432 !$#authors Yanagidani, S.; Uozumi, N.; Ihara, Y.; Miyoshi, E.; !1Yamaguchi, N.; Taniguchi, N. !$#journal J. Biochem. (1997) 121:626-632 !$#title Purification and cDNA cloning of !1GDP-L-Fuc:N-acetyl-beta-D-glucosaminide:alpha 1-6 !1fucosyltransferase (alpha 1-6 FucT) from human gastric !1cancer MKN45 cells. !$#cross-references MUID:97279058; PMID:9133635 !$#accession JC5432 !'##molecule_type mRNA !'##residues 1-575 ##label YAN1 !'##cross-references DDBJ:D89289; NID:g2055306; PIDN:BAA19764.1; !1PID:g2055307 !$#accession PC4322 !'##molecule_type protein !'##residues 68-87;352-376;419-432 ##label YAN2 COMMENT This enzyme catalyzes the transfer of fucose from !1GDP-fucopyranoside to asparagine-linked type complex !1glycopeptides. GENETICS !$#gene GDB:FUT8 !'##cross-references GDB:9786294; OMIM:602589 !$#map_position 14q23-14q23 CLASSIFICATION #superfamily human glycoprotein 6-alpha-L-fucosyltransferase KEYWORDS glycosyltransferase; hexosyltransferase FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-575 #product glycoprotein 6-alpha-L-fucosyltransferase !8#status predicted #label MAT SUMMARY #length 575 #molecular-weight 66515 #checksum 7773 SEQUENCE /// ENTRY XUBHFG #type complete TITLE flavonol 3-O-glucosyltransferase (EC 2.4.1.91) - barley ORGANISM #formal_name Hordeum vulgare #common_name barley DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 12-Nov-1999 ACCESSIONS S14919; S08105 REFERENCE S14919 !$#authors Wise, R.P.; Rohde, W.; Salamini, F. !$#journal Plant Mol. Biol. (1990) 14:277-279 !$#title Nucleotide sequence of the Bronze-1 homologous gene from !1Hordeum vulgare. !$#cross-references MUID:91329682; PMID:2151660 !$#accession S14919 !'##molecule_type DNA !'##residues 1-455 ##label WIS !'##cross-references EMBL:X15694; NID:g18939; PIDN:CAA33729.1; !1PID:g295807 GENETICS !$#map_position 1 !$#introns 162/1 CLASSIFICATION #superfamily flavonol O3-glucosyltransferase KEYWORDS flavonoid biosynthesis; glycosyltransferase; !1hexosyltransferase SUMMARY #length 455 #molecular-weight 47079 #checksum 7403 SEQUENCE /// ENTRY S08325 #type complete TITLE flavonol 3-O-glucosyltransferase (EC 2.4.1.91) (allele BzMcC2) - maize ALTERNATE_NAMES UDPglucose flavonoid glucosyl-transferase ORGANISM #formal_name Zea mays #common_name maize DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S08325 REFERENCE S08324 !$#authors Furtek, D.; Schiefelbein, J.W.; Johnston, F.; Nelson Jr., !1O.E. !$#journal Plant Mol. Biol. (1988) 11:473-481 !$#title Sequence comparisons of three wild-type Bronze-1 alleles !1from Zea mays. !$#accession S08325 !'##status translation not shown !'##molecule_type DNA !'##residues 1-471 ##label FUR !'##cross-references EMBL:X13501; NID:g22361; PIDN:CAA31856.1; !1PID:g295854 GENETICS !$#gene Bz1 !$#introns 175/1 CLASSIFICATION #superfamily flavonol O3-glucosyltransferase KEYWORDS glycosyltransferase; hexosyltransferase SUMMARY #length 471 #molecular-weight 48621 #checksum 7439 SEQUENCE /// ENTRY A44128 #type complete TITLE (N-acetylneuraminyl)-galactosylglucosylceramide N-acetylgalactosaminyltransferase (EC 2.4.1.92) - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A44128 REFERENCE A44128 !$#authors Nagata, Y.; Yamashiro, S.; Yodoi, J.; Lloyd, K.O.; Shiku, !1H.; Furukawa, K. !$#journal J. Biol. Chem. (1992) 267:12082-12089 !$#title Expression cloning of beta 1,4 !1N-acetylgalactosaminyltransferase cDNAs that determine the !1expression of GM2 and GD2 gangliosides. !$#cross-references MUID:92291088; PMID:1601877 !$#accession A44128 !'##status preliminary !'##molecule_type mRNA !'##residues 1-561 ##label NAG !'##experimental_source NK-like cell line YT !'##note sequence extracted from NCBI backbone (NCBIN:106611, !1NCBIP:106612) CLASSIFICATION #superfamily N-acetylgalactosaminyltransferase KEYWORDS glycosyltransferase; hexosyltransferase; transmembrane !1protein SUMMARY #length 561 #molecular-weight 61002 #checksum 7172 SEQUENCE /// ENTRY XUHUMB #type complete TITLE alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase (EC 2.4.1.101) - human ALTERNATE_NAMES N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase I ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Jun-2002 ACCESSIONS JH0397; A39271 REFERENCE JH0397 !$#authors Hull, E.; Sarkar, M.; Spruijt, M.P.N.; Hoeppener, J.W.M.; !1Dunn, R.; Schachter, H. !$#journal Biochem. Biophys. Res. Commun. (1991) 176:608-615 !$#title Organization and localization to chromosome 5 of the human !1UDP-N-acetylglucosamine: alpha-3-D-mannoside beta-1, !12-N-acetylglucosaminyltransferase I gene. !$#cross-references MUID:91222222; PMID:1827260 !$#accession JH0397 !'##molecule_type DNA !'##residues 1-445 ##label HUL !'##cross-references GB:M61829; NID:g340075; PIDN:AAA75523.1; !1PID:g340076 REFERENCE A39271 !$#authors Kumar, R.; Yang, J.; Larsen, R.D.; Stanley, P. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:9948-9952 !$#title Cloning and expression of N-acetylglucosaminyltransferase I, !1the medial Golgi transferase that initiates complex N-linked !1carbohydrate formation. !$#cross-references MUID:91088628; PMID:1702225 !$#accession A39271 !'##molecule_type mRNA !'##residues 1-434,'L',436-445 ##label KUM !'##cross-references GB:M55621; NID:g183236; PIDN:AAA52563.1; !1PID:g183237 GENETICS !$#gene GDB:MGAT1 !'##cross-references GDB:128225; OMIM:160995 !$#map_position 5q33.2-5qter CLASSIFICATION #superfamily alpha-1,3-mannosyl-glycoprotein beta-1, !12-N-acetylglucosaminyltransferase KEYWORDS glycosyltransferase; Golgi apparatus; hexosyltransferase; !1transmembrane protein FEATURE !$7-29 #domain transmembrane #status predicted #label TMM SUMMARY #length 445 #molecular-weight 50862 #checksum 6010 SEQUENCE /// ENTRY A42500 #type complete TITLE alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase (EC 2.4.1.101) - mouse ALTERNATE_NAMES GlcNAc-TI; N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase I ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS A42500; I54228 REFERENCE A42500 !$#authors Pownall, S.; Kozak, C.A.; Schappert, K.; Sarkar, M.; Hull, !1E.; Schachter, H.; Marth, J.D. !$#journal Genomics (1992) 12:699-704 !$#title Molecular cloning and characterization of the mouse !1UDP-N-acetylglucosamine:alpha-3-D-mannoside beta-1, !12-N-acetylglucosaminyltransferase I gene. !$#cross-references MUID:92241867; PMID:1533386 !$#accession A42500 !'##molecule_type DNA !'##residues 1-447 ##label POW !'##cross-references GB:M73491; NID:g193526; PIDN:AAA37698.1; !1PID:g193527 !'##note sequence extracted from NCBI backbone (NCBIN:98361, !1NCBIP:98366) REFERENCE I54228 !$#authors Kumar, R.; Yang, J.; Eddy, R.L. !$#journal Glycobiology (1992) 2:383-393 !$#title Cloning and expression of the murine gene and chromosomal !1location of the human gene encoding !1N-acetylglucosaminyltransferase I. !$#cross-references MUID:93043841; PMID:1421759 !$#accession I54228 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-447 ##label RES !'##cross-references GB:L07037; NID:g202145; PIDN:AAA40478.1; !1PID:g202146 CLASSIFICATION #superfamily alpha-1,3-mannosyl-glycoprotein beta-1, !12-N-acetylglucosaminyltransferase KEYWORDS glycosyltransferase; Golgi apparatus; hexosyltransferase; !1membrane protein SUMMARY #length 447 #molecular-weight 51690 #checksum 9126 SEQUENCE /// ENTRY A38561 #type complete TITLE alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase (EC 2.4.1.101) - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS A38561 REFERENCE A38561 !$#authors Sarkar, M.; Hull, E.; Nishikawa, Y.; Simpson, R.J.; Moritz, !1R.L.; Dunn, R.; Schachter, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:234-238 !$#title Molecular cloning and expression of cDNA encoding the enzyme !1that controls conversion of high-mannose to hybrid and !1complex N-glycans: !1UDP-N-acetylglucosamine:alpha-3-D-mannoside beta-1, !12-N-acetylglucosaminyltransferase I. !$#cross-references MUID:91095435; PMID:1824724 !$#accession A38561 !'##status preliminary !'##molecule_type mRNA !'##residues 1-447 ##label SAR !'##cross-references GB:M57301; NID:g165781; PIDN:AAA31493.1; !1PID:g165782 CLASSIFICATION #superfamily alpha-1,3-mannosyl-glycoprotein beta-1, !12-N-acetylglucosaminyltransferase KEYWORDS glycosyltransferase; hexosyltransferase; transmembrane !1protein SUMMARY #length 447 #molecular-weight 51540 #checksum 7458 SEQUENCE /// ENTRY XUNVAC #type complete TITLE ecdysteroid UDPglucosyltransferase (EC 2.4.1.-) - Autographa californica nuclear polyhedrosis virus ORGANISM #formal_name Autographa californica nuclear polyhedrosis virus, AcMNPV DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 24-Nov-1999 ACCESSIONS A34114; G72851 REFERENCE A34114 !$#authors O'Reilly, D.R.; Miller, L.K. !$#journal J. Virol. (1990) 64:1321-1328 !$#title Regulation of expression of a baculovirus ecdysteroid !1UDPglucosyltransferase gene. !$#cross-references MUID:90156533; PMID:2106039 !$#accession A34114 !'##molecule_type DNA !'##residues 1-506 ##label ORE !'##cross-references EMBL:M22619; NID:g332422; PIDN:AAA69845.1; !1PID:g332423 !'##experimental_source strain L1 REFERENCE A72850 !$#authors Ayres, M.D.; Howard, S.C.; Kuzio, J.; Lopez-Ferber, M.; !1Possee, R.D. !$#journal Virology (1994) 202:586-605 !$#title The complete DNA sequence of Autographa californica nuclear !1polyhedrosis virus. !$#cross-references MUID:94303173; PMID:8030224 !$#accession G72851 !'##status preliminary !'##molecule_type DNA !'##residues 1-506 ##label AYR !'##cross-references GB:L22858; NID:g510708; PIDN:AAA66645.1; !1PID:g559084 COMMENT This enzyme catalyzes the transfer of glucose from !1UDPglucose to ecdysteroid insect molting hormones. GENETICS !$#gene Ac-egt CLASSIFICATION #superfamily ecdysteroid UDPglucosyltransferase KEYWORDS glycosyltransferase; hexosyltransferase SUMMARY #length 506 #molecular-weight 57033 #checksum 6817 SEQUENCE /// ENTRY PHHUPN #type complete TITLE purine-nucleoside phosphorylase (EC 2.4.2.1) [validated] - human ALTERNATE_NAMES inosine phosphorylase; PNP; purine-nucleotide orthophosphate ribosyltransferase ORGANISM #formal_name Homo sapiens #common_name man DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 15-Sep-2000 ACCESSIONS A00578; I55256 REFERENCE A00578 !$#authors Williams, S.R.; Goddard, J.M.; Martin Jr., D.W. !$#journal Nucleic Acids Res. (1984) 12:5779-5787 !$#title Human purine nucleoside phosphorylase cDNA sequence and !1genomic clone characterization. !$#cross-references MUID:84272252; PMID:6087295 !$#accession A00578 !'##molecule_type mRNA !'##residues 1-289 ##label WIL !'##cross-references GB:K02574; GB:X00737; NID:g35564; PIDN:CAA25320.1; !1PID:g35565 REFERENCE I55256 !$#authors Williams, S.R.; Gekeler, V.; McIvor, R.S.; Martin, D.W. !$#journal J. Biol. Chem. (1987) 262:2332-2338 !$#title A human purine nucleoside phosphorylase deficiency caused by !1a single base change. !$#cross-references MUID:87137463; PMID:3029074 !$#accession I55256 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-88,'K',90-289 ##label RES !'##cross-references GB:M13953; NID:g190150; PIDN:AAA36460.1; !1PID:g387033 !'##note this mutant form is associated with nucleoside phosphorylase !1deficiency !'##note details in the paper make it clear that for the mutated codon !1for residue 89, the sequence in GenBank is incorrect; the !1codon was determined to be AAA (Lys), as compared to GAA !1(Glu) in the wild type and AGA (Arg) as shown in GenBank !1release 92 REFERENCE A50872 !$#authors Ealick, S.E.; Rule, S.A.; Carter, D.C.; Greenhough, T.J.; !1Babu, Y.S.; Cook, W.J.; Habash, J.; Helliwell, J.R.; !1Stoeckler, J.D.; Parks Jr., R.E.; Chen, S.F.; Bugg, C.E. !$#submission submitted to the Brookhaven Protein Data Bank, November 1991 !$#cross-references PDB:1ULA !$#contents annotation; X-ray crystallography, 2.75 angstroms, residues !11-289 REFERENCE A50873 !$#authors Ealick, S.E.; Rule, S.A.; Carter, D.C.; Greenhough, T.J.; !1Babu, Y.S.; Cook, W.J.; Habash, J.; Helliwell, J.R.; !1Stoeckler, J.D.; Parks Jr., R.E.; Chen, S.F.; Bugg, C.E. !$#submission submitted to the Brookhaven Protein Data Bank, November 1991 !$#cross-references PDB:1ULB !$#contents annotation; X-ray crystallography, 2.75 angstroms, residues !11-289 REFERENCE A35024 !$#authors Ealick, S.E.; Rule, S.A.; Carter, D.C.; Greenhough, T.J.; !1Babu, Y.S.; Cook, W.J.; Habash, J.; Helliwell, J.R.; !1Stoeckler, J.D.; Parks Jr., R.E.; Chen, S.; Bugg, C.E. !$#journal J. Biol. Chem. (1990) 265:1812-1820 !$#title Three-dimensional structure of human erythrocytic purine !1nucleoside phosphorylase at 3.2 angstrom resolution. !$#cross-references MUID:90110256; PMID:2104852 !$#contents annotation; X-ray crystallography, 3.2 angstroms GENETICS !$#gene GDB:NP !'##cross-references GDB:120239; OMIM:164050 !$#map_position 14q11.2-14q11.2 !$#introns 4/2; 61/1; 95/3; 154/2; 218/1 !$#note a defect in this gene may result in severe T-cell !1immunodeficiency COMPLEX homotrimer FUNCTION !$#description catalyzes the reversible phosphorolysis of the guanine and !1hypoxanthine nucleosides and 2'-deoxyribonucleosides to !1their respective bases and pentose-alpha-1-phosphate !$#pathway nucleotide salvage pathway CLASSIFICATION #superfamily purine-nucleoside phosphorylase KEYWORDS glycosyltransferase; homotrimer; immunodeficiency; !1pentosyltransferase; salvage pathway FEATURE !$33,88,116,201,243, !$244 #binding_site substrate (Ser, Tyr, Ala, Glu, Asn, !8Lys) #status experimental\ !$33,84,86,220 #binding_site substrate phosphate (Ser, Arg, His, !8Ser) #status experimental SUMMARY #length 289 #molecular-weight 32148 #checksum 1390 SEQUENCE /// ENTRY I57010 #type complete TITLE purine-nucleoside phosphorylase (EC 2.4.2.1) - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS I57010; I76671; S26825; JC1115 REFERENCE I57010 !$#authors Jenuth, J.P.; Mangat, R.K.; Snyder, F.F. !$#journal Mamm. Genome (1993) 4:598-603 !$#title cDNA sequence of four purine nucleoside phosphorylase (Np) !1alleles in the mouse. !$#cross-references MUID:94093208; PMID:7903568 !$#accession I57010 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-289 ##label RES !'##cross-references GB:L11290; NID:g388918; PIDN:AAC37634.1; !1PID:g388919 !$#accession I76671 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-257,'K',259-289 ##label RE2 !'##cross-references GB:L11291; NID:g388920; PIDN:AAC37635.1; !1PID:g388921 REFERENCE S26825 !$#authors Jenuth, J.P.; Snyder, F.F. !$#journal Nucleic Acids Res. (1991) 19:1708 !$#title Nucleotide sequence of murine purine nucleoside !1phosphorylase cDNA. !$#cross-references MUID:91227171; PMID:1902950 !$#accession S26825 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type mRNA !'##residues 1-175,'S',177-289 ##label JEN !'##cross-references EMBL:X56548; NID:g976084; PIDN:CAA39888.1; !1PID:g53750 !'##experimental_source strain C57BL/6 !'##note 176-Thr was found in other strains REFERENCE JC1115 !$#authors Nelson, D.M.; Foresman, M.D.; Ronnei, B.J.; McIvor, R.S. !$#journal Gene (1992) 113:215-221 !$#title Isolation and expression of a murine purine nucleoside !1phosphorylase-encoding cDNA and sequence similarity with the !1human message. !$#cross-references MUID:92241671; PMID:1374046 !$#accession JC1115 !'##molecule_type mRNA !'##residues 1-289 ##label NEL !'##cross-references GB:M84563; NID:g200097; PIDN:AAA39835.1; !1PID:g200098 COMMENT This enzyme catalyzes the phosphorolytic cleavage of guanine !1and hypoxanthine ribonucleoside and 2' deoxyribonucleosides !1to their respective bases and pentose-1-phosphate. GENETICS !$#gene Np CLASSIFICATION #superfamily purine-nucleoside phosphorylase KEYWORDS glycosyltransferase; pentosyltransferase; polymorphism; !1salvage pathway SUMMARY #length 289 #molecular-weight 32277 #checksum 299 SEQUENCE /// ENTRY S48560 #type complete TITLE purine-nucleoside phosphorylase (EC 2.4.2.1) YLR209c - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein L8167.19 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S48560 REFERENCE S48545 !$#authors Pauley, A. !$#submission submitted to the EMBL Data Library, September 1994 !$#description The sequence of S. cerevisiae cosmid 8167. !$#accession S48560 !'##molecule_type DNA !'##residues 1-311 ##label PAU !'##cross-references EMBL:U14913; NID:g544497; PIDN:AAB67440.1; !1PID:g544515; GSPDB:GN00012; MIPS:YLR209c GENETICS !$#gene SGD:PNP1; MIPS:YLR209c !'##cross-references SGD:S0004199 !$#map_position 12R CLASSIFICATION #superfamily purine-nucleoside phosphorylase KEYWORDS glycosyltransferase; pentosyltransferase SUMMARY #length 311 #molecular-weight 33755 #checksum 6524 SEQUENCE /// ENTRY S03904 #type complete TITLE platelet-derived endothelial cell growth factor precursor [validated] - human CONTAINS thymidine phosphorylase (EC 2.4.2.4) ORGANISM #formal_name Homo sapiens #common_name man DATE 23-Oct-1998 #sequence_revision 23-Oct-1998 #text_change 23-Dec-2002 ACCESSIONS S03904; JX0275; A60966 REFERENCE S03904 !$#authors Ishikawa, F.; Miyazono, K.; Hellman, U.; Drexler, H.; !1Wernstedt, C.; Hagiwara, K.; Usuki, K.; Takaku, F.; Risau, !1W.; Heldin, C.H. !$#journal Nature (1989) 338:557-562 !$#title Identification of angiogenic activity and the cloning and !1expression of platelet-derived endothelial cell growth !1factor. !$#cross-references MUID:89181955; PMID:2467210 !$#accession S03904 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-482 ##label ISH !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing !'##note 471-Ser was also found REFERENCE JX0275 !$#authors Sumizawa, T.; Furukawa, T.; Haraguchi, M.; Yoshimura, A.; !1Takeyasu, A.; Ishizawa, M.; Yamada, Y.; Akiyama, S. !$#journal J. Biochem. (1993) 114:9-14 !$#title Thymidine phosphorylase activity associated with !1platelet-derived endothelial cell growth factor. !$#cross-references MUID:94012588; PMID:8407883 !$#accession JX0275 !'##molecule_type mRNA !'##residues 125-244 ##label SUM !'##experimental_source placenta REFERENCE A60966 !$#authors Usuki, K.; Norberg, L.; Larsson, E.; Miyazono, K.; Hellman, !1U.; Wernstedt, C.; Rubin, K.; Heldin, C.H. !$#journal Cell Regul. (1990) 1:577-596 !$#title Localization of platelet-derived endothelial cell growth !1factor in human placenta and purification of an !1alternatively processed form. !$#cross-references MUID:91175877; PMID:2078568 !$#accession A60966 !'##molecule_type protein !'##residues 6-14 ##label USU GENETICS !$#gene GDB:ECGF1 !'##cross-references GDB:127754; OMIM:131222 !$#map_position 22q13-22q13 CLASSIFICATION #superfamily thymidine phosphorylase/pyrimidine-nucleoside !1phosphorylase KEYWORDS angiogenesis; glycosyltransferase; growth factor; mitogen; !1pentosyltransferase FEATURE !$6-482 #product platelet-derived endothelial cell growth !8factor, placental form #status experimental #label !8MAT1\ !$11-482 #product platelet-derived endothelial cell growth !8factor, platelet form #status experimental #label !8MAT2\ !$63 #binding_site carbohydrate (Asn) (covalent) #status !8absent SUMMARY #length 482 #molecular-weight 49981 #checksum 4701 SEQUENCE /// ENTRY S56606 #type complete TITLE thymidine phosphorylase (EC 2.4.2.4) deoA [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 23-Oct-1998 #sequence_revision 23-Oct-1998 #text_change 23-Dec-2002 ACCESSIONS S56606; E65253; A37131; A22909 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56606 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-440 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97278.1; !1PID:g537222 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65253 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-440 ##label BLAT !'##cross-references GB:AE000508; GB:U00096; NID:g2367382; !1PIDN:AAC77335.1; PID:g1790842; UWGP:b4382 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A37131 !$#authors Walter, M.R.; Cook, W.J.; Cole, L.B.; Short, S.A.; Koszalka, !1G.W.; Krenitsky, T.A.; Ealick, S.E. !$#journal J. Biol. Chem. (1990) 265:14016-14022 !$#title Three-dimensional structure of thymidine phosphorylase from !1Escherichia coli at 2.8 angstrom resolution. !$#cross-references MUID:90338026; PMID:2199449 !$#contents sequence; X-ray crystallography, 2.8 angstroms !$#accession A37131 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type mRNA !'##residues 'L',2-136,'F',137-440 ##label WAL REFERENCE A50379 !$#authors Walter, M.R.; Cook, W.J.; Cole, L.B.; Short, S.A.; Koszalka, !1G.W.; Krenitsky, T.A.; Ealick, S.E. !$#submission submitted to the Brookhaven Protein Data Bank, June 1990 !$#cross-references PDB:1TPT !$#contents annotation; X-ray crystallography, 2.8 angstroms, residues !1'L',2-440 REFERENCE A93525 !$#authors Valentin-Hansen, P.; Hammer, K.; Larsen, J.E.L.; Svendsen, !1I. !$#journal Nucleic Acids Res. (1984) 12:5211-5224 !$#title The internal regulated promoter of the deo operon of !1Escherichia coli K-12. !$#cross-references MUID:84272212; PMID:6087276 !$#accession A22909 !'##molecule_type DNA !'##residues 377-440 ##label VAL !'##cross-references GB:X00742; NID:g41249; PIDN:CAA25324.1; PID:g41250 GENETICS !$#gene deoA !$#map_position 100 min !$#start_codon TTG FUNCTION !$#description catalyzes the reversible reaction of thymine and !12-deoxy-D-ribose 1-phosphate to form thymidine and phosphate CLASSIFICATION #superfamily thymidine phosphorylase/pyrimidine-nucleoside !1phosphorylase KEYWORDS glycosyltransferase; pentosyltransferase FEATURE !$84,85,86,95,113,123 #binding_site substrate phosphate (Lys, His, Ser, !8Ser, Ser, Thr) #status predicted\ !$171,186,190 #binding_site substrate (Arg, Ser, Lys) #status !8experimental SUMMARY #length 440 #molecular-weight 47207 #checksum 9161 SEQUENCE /// ENTRY S49457 #type complete TITLE pyrimidine-nucleoside phosphorylase (EC 2.4.2.2) pdp - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 23-Oct-1998 #sequence_revision 23-Oct-1998 #text_change 23-Dec-2002 ACCESSIONS S78770; D69674; S49457 REFERENCE A71573 !$#authors Saxild, H.H.; Andersen, L.N.; Hammer, K. !$#journal J. Bacteriol. (1996) 178:424-434 !$#title Dra-nupC-pdp operon of Bacillus subtilis: nucleotide !1sequence, induction by deoxyribonucleosides, and !1transcriptional regulation by the deoR-encoded DeoR !1repressor protein. !$#cross-references MUID:96134975; PMID:8550462 !$#accession S78770 !'##status preliminary !'##molecule_type DNA !'##residues 1-434 ##label SAX2 !'##cross-references EMBL:X82174; NID:g558554; PIDN:CAA57664.1; !1PID:g558559 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D69674 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-434 ##label KUN !'##cross-references GB:Z99124; GB:AL009126; NID:g2636442; !1PIDN:CAB15976.1; PID:g2636486 !'##experimental_source strain 168 GENETICS !$#gene pdp FUNCTION !$#description catalyzes the reversible phosphorolysis of uridine and !1thymidine. CLASSIFICATION #superfamily thymidine phosphorylase/pyrimidine-nucleoside !1phosphorylase KEYWORDS glycosyltransferase; pentosyltransferase SUMMARY #length 434 #molecular-weight 46532 #checksum 6555 SEQUENCE /// ENTRY JT0875 #type complete TITLE pyrimidine-nucleoside phosphorylase (EC 2.4.2.2) - Bacillus stearothermophilus ORGANISM #formal_name Bacillus stearothermophilus DATE 23-Oct-1998 #sequence_revision 23-Oct-1998 #text_change 23-Dec-2002 ACCESSIONS JT0875; JC4992; PC4206 REFERENCE JT0875 !$#authors Okuyama, K.; Hamamoto, T.; Noguchi, T.; Nidorikawa, Y. !$#journal Biosci. Biotechnol. Biochem. (1996) 60:1055-1059 !$#title Molecluar cloning and expression of purine nucleoside !1phosphorylase I gene from Bacillus stearothermophilus TH6-2. !$#accession JT0875 !'##molecule_type DNA !'##residues 1-433 ##label OKU REFERENCE JC4992 !$#authors Okuyama, K.; Hamamoto, T.; Noguchi, T.; Midorikawa, Y. !$#journal Biosci. Biotechnol. Biochem. (1996) 60:1655-1659 !$#title Molecular cloning and expression of the pyrimidine !1nucleoside phosphorylase gene from Bacillus !1stearothermophilus TH 6-2. !$#cross-references MUID:97141320; PMID:8987664 !$#accession JC4992 !'##molecule_type DNA !'##residues 1-433 ##label OK3 !'##cross-references GB:D87961; NID:g1620899; PIDN:BAA13512.1; !1PID:g1620901 !'##experimental_source strain TH6-2 !$#accession PC4206 !'##molecule_type protein !'##residues 1-12 ##label OK2 GENETICS !$#gene pyn COMPLEX homodimer FUNCTION !$#description catalyzes the reversible phosphorolysis of uridine and !1thymidine. CLASSIFICATION #superfamily thymidine phosphorylase/pyrimidine-nucleoside !1phosphorylase KEYWORDS glycosyltransferase; pentosyltransferase SUMMARY #length 433 #molecular-weight 46332 #checksum 7422 SEQUENCE /// ENTRY F64205 #type complete TITLE thymidine phosphorylase (EC 2.4.2.4) - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 23-Oct-1998 #sequence_revision 23-Oct-1998 #text_change 23-Dec-2002 ACCESSIONS F64205 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession F64205 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-421 ##label TIGR !'##cross-references GB:U39684; GB:L43967; NID:g3844650; !1PIDN:AAC71267.1; PID:g1045724; TIGR:MG051 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily thymidine phosphorylase/pyrimidine-nucleoside !1phosphorylase KEYWORDS glycosyltransferase; pentosyltransferase SUMMARY #length 421 #molecular-weight 46355 #checksum 1771 SEQUENCE /// ENTRY S73416 #type complete TITLE thymidine phosphorylase (EC 2.4.2.4) deoA - Mycoplasma pneumoniae (strain ATCC 29342) ALTERNATE_NAMES hypothetical protein D09_orf421 ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 23-Oct-1998 #sequence_revision 23-Oct-1998 #text_change 23-Dec-2002 ACCESSIONS S73416 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73416 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-421 ##label HIM !'##cross-references EMBL:AE000011; GB:U00089; NID:g1673740; !1PIDN:AAB95738.1; PID:g1673745 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#gene deoA !$#genetic_code SGC3 CLASSIFICATION #superfamily thymidine phosphorylase/pyrimidine-nucleoside !1phosphorylase KEYWORDS glycosyltransferase; pentosyltransferase SUMMARY #length 421 #molecular-weight 46628 #checksum 6605 SEQUENCE /// ENTRY C53312 #type complete TITLE thymidine phosphorylase (EC 2.4.2.4) - Mycoplasma pirum (strain BER) ORGANISM #formal_name Mycoplasma pirum DATE 23-Oct-1998 #sequence_revision 23-Oct-1998 #text_change 23-Dec-2002 ACCESSIONS C53312 REFERENCE A53312 !$#authors Tham, T.N.; Ferris, S.; Kovacic, R.; Montagnier, L.; !1Blanchard, A. !$#journal J. Bacteriol. (1993) 175:5281-5285 !$#title Identification of Mycoplasma pirum genes involved in the !1salvage pathways for nucleosides. !$#cross-references MUID:93352438; PMID:8349569 !$#accession C53312 !'##status preliminary !'##molecule_type DNA !'##residues 1-419 ##label THA !'##cross-references GB:L13289; NID:g401781; PIDN:AAA25432.1; !1PID:g401784 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily thymidine phosphorylase/pyrimidine-nucleoside !1phosphorylase KEYWORDS glycosyltransferase; pentosyltransferase SUMMARY #length 419 #molecular-weight 47278 #checksum 8363 SEQUENCE /// ENTRY D69417 #type complete TITLE probable thymidine phosphorylase (EC 2.4.2.4) 1 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 23-Oct-1998 #sequence_revision 23-Oct-1998 #text_change 23-Dec-2002 ACCESSIONS D69417 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession D69417 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-504 ##label KLE !'##cross-references GB:AE001011; GB:AE000782; NID:g2689334; !1PIDN:AAB89903.1; PID:g2649233; TIGR:AF1341 CLASSIFICATION #superfamily thymidine phosphorylase/pyrimidine-nucleoside !1phosphorylase KEYWORDS glycosyltransferase; pentosyltransferase SUMMARY #length 504 #molecular-weight 54098 #checksum 4654 SEQUENCE /// ENTRY E69417 #type complete TITLE probable thymidine phosphorylase (EC 2.4.2.4) 2 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 23-Oct-1998 #sequence_revision 23-Oct-1998 #text_change 23-Dec-2002 ACCESSIONS E69417 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession E69417 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-505 ##label KLE !'##cross-references GB:AE001011; GB:AE000782; NID:g2689334; !1PIDN:AAB89902.1; PID:g2649232; TIGR:AF1342 CLASSIFICATION #superfamily thymidine phosphorylase/pyrimidine-nucleoside !1phosphorylase KEYWORDS glycosyltransferase; pentosyltransferase SUMMARY #length 505 #molecular-weight 54692 #checksum 1174 SEQUENCE /// ENTRY C64383 #type complete TITLE thymidine phosphorylase (EC 2.4.2.4) - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 23-Oct-1998 #sequence_revision 23-Oct-1998 #text_change 23-Dec-2002 ACCESSIONS C64383 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession C64383 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-503 ##label BUL !'##cross-references GB:U67514; GB:L77117; NID:g2826304; !1PIDN:AAB98662.1; PID:g1591381; TIGR:MJ0667 GENETICS !$#map_position FOR592705-594216 CLASSIFICATION #superfamily thymidine phosphorylase/pyrimidine-nucleoside !1phosphorylase KEYWORDS glycosyltransferase; pentosyltransferase SUMMARY #length 503 #molecular-weight 54721 #checksum 2582 SEQUENCE /// ENTRY RTHUA #type complete TITLE adenine phosphoribosyltransferase (EC 2.4.2.7) [validated] - human ALTERNATE_NAMES AMP pyrophosphorylase; transphosphoribosidase ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1988 #sequence_revision 07-Jul-1995 #text_change 08-Dec-2000 ACCESSIONS S06232; A28021; A26156; A36539; I38613 REFERENCE S06232 !$#authors Hidaka, Y.; Tarle, S.A.; O'Toole, T.E.; Kelley, W.N.; !1Palella, T.D. !$#journal Nucleic Acids Res. (1987) 15:9086 !$#title Nucleotide sequence of the human APRT gene. !$#cross-references MUID:88067724; PMID:3684585 !$#accession S06232 !'##status translation not shown !'##molecule_type DNA !'##residues 1-180 ##label HID !'##cross-references EMBL:Y00486; NID:g28818; PIDN:CAA68543.1; !1PID:g28819 REFERENCE A28021 !$#authors Broderick, T.P.; Schaff, D.A.; Bertino, A.M.; Dush, M.K.; !1Tischfield, J.A.; Stambrook, P.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:3349-3353 !$#title Comparative anatomy of the human APRT gene and enzyme: !1nucleotide sequence divergence and conservation of a !1nonrandom CpG dinucleotide arrangement. !$#cross-references MUID:87204134; PMID:3554238 !$#accession A28021 !'##molecule_type DNA !'##residues 1-180 ##label BRO !'##cross-references EMBL:M16446; NID:g178866; PIDN:AAA51769.1; !1PID:g178867 REFERENCE A26156 !$#authors Wilson, J.M.; O'Toole, T.E.; Argos, P.; Shewach, D.S.; !1Daddona, P.E.; Kelley, W.N. !$#journal J. Biol. Chem. (1986) 261:13677-13683 !$#title Human adenine phosphoribosyltransferase. Complete amino acid !1sequence of the erythrocyte enzyme. !$#cross-references MUID:87008604; PMID:3531209 !$#accession A26156 !'##molecule_type protein !'##residues 2-180 ##label WIL REFERENCE A36539 !$#authors Mimori, A.; Hidaka, Y.; Wu, V.C.; Tarle, S.A.; Kamatani, N.; !1Kelley, W.N.; Pallela, T.D. !$#journal Am. J. Hum. Genet. (1991) 48:103-107 !$#title A mutant allele common to the type I adenine !1phosphoribosyltransferase deficiency in Japanese subjects. !$#cross-references MUID:91090095; PMID:1985452 !$#accession A36539 !'##status preliminary !'##molecule_type DNA !'##residues 97-100 ##label MIM REFERENCE I38613 !$#authors Chen, J.; Sahota, A.; Stambrook, P.J.; Tischfield, J.A. !$#journal Mutat. Res. (1991) 249:169-176 !$#title Polymerase chain reaction amplification and sequence !1analysis of the human mutant phosphoribosyltransferse genes: !1The nature and frequency of errors caused by Taq DNA !1polymerase. !$#cross-references MUID:91295958; PMID:2067530 !$#accession I38613 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-27,'C',53-54 ##label CHE !'##cross-references EMBL:U09817; NID:g498573; PIDN:AAB84304.1; !1PID:g498574 GENETICS !$#gene GDB:APRT !'##cross-references GDB:119003; OMIM:102600 !$#map_position 16q24.2-16qter !$#introns 27/2; 63/1; 107/3; 134/1 COMPLEX homodimer FUNCTION !$#description catalyzes the phosphoribosylation of adenine by !15-phospho-alpha-D-ribose 1-diphosphate to form AMP and !1pyrophosphate !$#pathway purine salvage CLASSIFICATION #superfamily adenine phosphoribosyltransferase KEYWORDS glycosyltransferase; homodimer; pentosyltransferase; salvage !1pathway FEATURE !$2-180 #product adenine phosphoribosyltransferase #status !8experimental #label MAT SUMMARY #length 180 #molecular-weight 19608 #checksum 8510 SEQUENCE /// ENTRY A29596 #type complete TITLE adenine phosphoribosyltransferase (EC 2.4.2.7) - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES AMP pyrophosphorylase; transphosphoribosidase ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A29596 REFERENCE A29596 !$#authors Johnson, D.H.; Edstroem, J.E.; Burnett, J.B.; Friedman, T.B. !$#journal Gene (1987) 59:77-86 !$#title Cloning of a Drosophila melanogaster adenine !1phosphoribosyltransferase structural gene and deduced amino !1acid sequence of the enzyme. !$#cross-references MUID:88137948; PMID:3125085 !$#accession A29596 !'##molecule_type mRNA !'##residues 1-183 ##label JOH !'##cross-references GB:M18432; NID:g156954; PIDN:AAA28377.1; !1PID:g156955 GENETICS !$#gene Aprt !'##cross-references FlyBase:FBgn0000109 CLASSIFICATION #superfamily adenine phosphoribosyltransferase KEYWORDS glycosyltransferase; pentosyltransferase; salvage pathway SUMMARY #length 183 #molecular-weight 19876 #checksum 2996 SEQUENCE /// ENTRY RTMSA #type complete TITLE adenine phosphoribosyltransferase (EC 2.4.2.7) - mouse ALTERNATE_NAMES AMP pyrophosphorylase; gene APRT protein; transphosphoribosidase ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 11-Jun-1999 ACCESSIONS A22670; I49509 REFERENCE A22670 !$#authors Dush, M.K.; Sikela, J.M.; Khan, S.A.; Tischfield, J.A.; !1Stambrook, P.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:2731-2735 !$#title Nucleotide sequence and organization of the mouse adenine !1phosphoribosyltransferase gene: presence of a coding region !1common to animal and bacterial phosphoribosyltransferases !1that has a variable intron/exon arrangement. !$#cross-references MUID:85190571; PMID:3921964 !$#accession A22670 !'##molecule_type DNA !'##residues 1-180 ##label DUS !'##cross-references GB:M11310; NID:g192009; PIDN:AAA37255.1; !1PID:g387103 REFERENCE I49509 !$#authors Turker, M.S.; Cooper, G.E.; Bishop, P.L. !$#journal J. Mol. Evol. (1993) 36:31-40 !$#title Region-specific rates of molecular evolution: A fourfold !1reduction in the rate of accumulation of silent mutations in !1transcribed versus nontranscribed regions of homologous DNA !1fragments derived from two closely related mouse species. !$#cross-references MUID:93164265; PMID:8433377 !$#accession I49509 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 63-107,'VR',108-133 ##label RES !'##cross-references GB:M86439; NID:g192011; PIDN:AAA37256.1; !1PID:g553869 COMMENT The active enzyme is a dimer of identical chains. GENETICS !$#gene MGI:Aprt !'##cross-references MGI:88061 !$#introns 27/2; 63/1; 107/3; 134/1 CLASSIFICATION #superfamily adenine phosphoribosyltransferase KEYWORDS glycosyltransferase; pentosyltransferase; salvage pathway SUMMARY #length 180 #molecular-weight 19736 #checksum 749 SEQUENCE /// ENTRY RTECA #type complete TITLE adenine phosphoribosyltransferase (EC 2.4.2.7) - Escherichia coli (strain K-12) ALTERNATE_NAMES AMP pyrophosphorylase; transphosphoribosidase ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 01-Mar-2002 ACCESSIONS A25635; B25549; D64777 REFERENCE A91548 !$#authors Hershey, H.V.; Taylor, M.W. !$#journal Gene (1986) 43:287-293 !$#title Nucleotide sequence and deduced amino acid sequence of !1Escherichia coli adenine phosphoribosyltransferase and !1comparison with other analogous enzymes. !$#cross-references MUID:86301884; PMID:3527873 !$#accession A25635 !'##molecule_type DNA !'##residues 1-183 ##label HER !'##cross-references GB:M14040; GB:M25902; NID:g145293; PIDN:AAA23455.1; !1PID:g145294 REFERENCE A25549 !$#authors Flower, A.M.; McHenry, C.S. !$#journal Nucleic Acids Res. (1986) 14:8091-8101 !$#title The adjacent dnaZ and dnaX genes of Escherichia coli are !1contained within one continuous open reading frame. !$#cross-references MUID:87040775; PMID:3534795 !$#accession B25549 !'##molecule_type DNA !'##residues 40-183 ##label FLO !'##cross-references GB:X04487; NID:g43319; PIDN:CAA28173.1; PID:g809695 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64777 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-183 ##label BLAT !'##cross-references GB:AE000153; GB:U00096; NID:g1786671; !1PIDN:AAC73571.1; PID:g1786675; UWGP:b0469 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene apt !$#map_position 11 min FUNCTION !$#pathway purine salvage CLASSIFICATION #superfamily adenine phosphoribosyltransferase KEYWORDS glycosyltransferase; homodimer; pentosyltransferase; salvage !1pathway SUMMARY #length 183 #molecular-weight 19859 #checksum 199 SEQUENCE /// ENTRY S20867 #type complete TITLE adenine phosphoribosyltransferase (EC 2.4.2.7) 1 [similarity] - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS S20867 REFERENCE S20867 !$#authors Moffatt, B.A.; McWhinnie, E.A.; Burkhart, W.E.; Pasternak, !1J.J.; Rothstein, S.J. !$#journal Plant Mol. Biol. (1992) 18:653-662 !$#title A complete cDNA for adenine phosphoribosyltransferase from !1Arabidopsis thaliana. !$#cross-references MUID:92216042; PMID:1558943 !$#accession S20867 !'##molecule_type mRNA !'##residues 1-183 ##label MOF !'##cross-references EMBL:X58640; NID:g16163; PIDN:CAA41497.1; !1PID:g16164 !'##experimental_source strain cv.columbia !'##note the authors translated the codon CTC for residue 138 as Ser !'##note part of this sequence was confirmed by protein sequencing GENETICS !$#gene apt; apt1 FUNCTION !$#pathway purine salvage CLASSIFICATION #superfamily adenine phosphoribosyltransferase KEYWORDS glycosyltransferase; pentosyltransferase; salvage pathway SUMMARY #length 183 #molecular-weight 19739 #checksum 7882 SEQUENCE /// ENTRY S71272 #type complete TITLE adenine phosphoribosyltransferase (EC 2.4.2.7) 2 [similarity] - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 16-Jun-2000 ACCESSIONS S71272 REFERENCE S71272 !$#authors Schnorr, K.M.; Laloue, M.; Hirel, B. !$#submission submitted to the EMBL Data Library, March 1996 !$#description Isolation of cDNAs encoding two purine biosynthetic enzymes !1of soybean and expression of the corresponding transcripts !1in roots and root nodules. !$#accession S71272 !'##molecule_type mRNA !'##residues 1-192 ##label SCH !'##cross-references EMBL:X96866; NID:g1402893; PIDN:CAA65609.1; !1PID:g1321681 !'##experimental_source strain cv. columbia; isolate A19 GENETICS !$#gene apt2 !$#map_position 1 FUNCTION !$#pathway purine salvage CLASSIFICATION #superfamily adenine phosphoribosyltransferase KEYWORDS glycosyltransferase; pentosyltransferase; salvage pathway SUMMARY #length 192 #molecular-weight 21008 #checksum 461 SEQUENCE /// ENTRY RTHUG #type complete TITLE hypoxanthine phosphoribosyltransferase (EC 2.4.2.8) [validated] - human ALTERNATE_NAMES hypoxanthine-guanine phosphoribosyltransferase ORGANISM #formal_name Homo sapiens #common_name man DATE 17-Dec-1982 #sequence_revision 08-Feb-1996 #text_change 17-Mar-2000 ACCESSIONS A32728; A93963; A92344; A93983; A92469; I54249; I54263; !1I51843; I64798; I64796; I64797; I57607; A00579 REFERENCE A32728 !$#authors Edwards, A.; Voss, H.; Rice, P.; Civitello, A.; Stegemann, !1J.; Schwager, C.; Zimmermann, J.; Erfle, H.; Caskey, C.T.; !1Ansorge, W. !$#journal Genomics (1990) 6:593-608 !$#title Automated DNA sequencing of the human HPRT locus. !$#cross-references MUID:90256168; PMID:2341149 !$#accession A32728 !'##molecule_type DNA !'##residues 1-218 ##label EDW !'##cross-references GB:M26434; NID:g184369; PIDN:AAA36012.1; !1PID:g184370; GB:J00205; GB:M27558; GB:M27559; GB:M27560; !1GB:M27561; GB:M29753; GB:M29754; GB:M29755; GB:M29756; !1GB:M29757 REFERENCE A93963 !$#authors Jolly, D.J.; Okayama, H.; Berg, P.; Esty, A.C.; Filpula, D.; !1Bohlen, P.; Johnson, G.G.; Shively, J.E.; Hunkapillar, T.; !1Friedmann, T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:477-481 !$#title Isolation and characterization of a full-length expressible !1cDNA for human hypoxanthine phosphoribosyltransferase. !$#cross-references MUID:83169681; PMID:6300847 !$#accession A93963 !'##molecule_type mRNA !'##residues 2-218 ##label JOL !'##cross-references GB:M31642; GB:J00205; GB:V00530; NID:g184349; !1PIDN:AAA52690.1; PID:g306885 !'##note initiator Met not shown REFERENCE A92344 !$#authors Wilson, J.M.; Tarr, G.E.; Mahoney, W.C.; Kelley, W.N. !$#journal J. Biol. Chem. (1982) 257:10978-10985 !$#title Human hypoxanthine-guanine phosphoribosyltransferase. !1Complete amino acid sequence of the erythrocyte enzyme. !$#cross-references MUID:82265815; PMID:7107641 !$#accession A92344 !'##molecule_type protein !'##residues 2-218 ##label WIL !'##note 107-Asp was also found, presumably as a result of deamidation !1after translation rather than a genetic variation REFERENCE A93983 !$#authors Wilson, J.M.; Tarr, G.E.; Kelley, W.N. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:870-873 !$#title Human hypoxanthine (guanine) phosphoribosyltransferase: an !1amino acid substitution in a mutant form of the enzyme !1isolated from a patient with gout. !$#cross-references MUID:83144031; PMID:6572373 !$#accession A93983 !'##molecule_type protein !'##residues 2-109,'L',111-218 ##label WI2 !'##experimental_source variant London !'##note this form was isolated from a patient with severe gout REFERENCE A92469 !$#authors Wilson, J.M.; Kelley, W.N. !$#journal J. Biol. Chem. (1984) 259:27-30 !$#title Human hypoxanthine-guanine phosphoribosyltransferase. !1Structural alteration in a dysfunctional enzyme variant !1(HPRT-Munich) isolated from a patient with gout. !$#cross-references MUID:84161915; PMID:6706936 !$#accession A92469 !'##molecule_type protein !'##residues 2-103,'R',105-218 ##label WI3 !'##experimental_source variant Munich !'##note this substitution is in the probable hypoxanthine-binding site !1and results in abnormal enzyme function REFERENCE I54249 !$#authors Snyder, F.F.; Chudley, A.E.; MacLeod, P.M.; Carter, R.J.; !1Fung, E.; Lowe, J.K. !$#journal Hum. Genet. (1984) 67:18-22 !$#title Partial deficiency of hypoxanthine-guanine !1phosphoribosyltransferase with reduced affinity for !1PP-ribose-P in four related males with gout. !$#cross-references MUID:84263016; PMID:6204922 !$#accession I54249 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-193,'E',195-218 ##label SNY !'##cross-references GB:L29382; NID:g459816; PIDN:AAB59392.1; !1PID:g459817 REFERENCE I54263 !$#authors Lightfoot, T.; Joshi, R.; Nuki, G.; Snyder, F.F. !$#journal Hum. Genet. (1992) 88:695-696 !$#title The point mutation of hypoxanthine-guanine !1phosphoribosyltransferase (HPRTEdinburgh) and detection by !1allele-specific polymerase chain reaction. !$#cross-references MUID:92201839; PMID:1551676 !$#accession I54263 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-51,'G',53-218 ##label LIG !'##cross-references GB:L29383; NID:g459814; PIDN:AAB59391.1; !1PID:g459815 REFERENCE I51843 !$#authors Yamada, Y.; Goto, H.; Ogasawara, N. !$#journal Adv. Exp. Med. Biol. (1991) 309B:121-124 !$#title Identification of two independent Japanese mutant HPRT genes !1using the PCR technique. !$#cross-references MUID:92142870; PMID:1840476 !$#accession I51843 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 183-187,'A',189-193 ##label YAM1 !'##cross-references GB:S79313; NID:g244377; PIDN:AAB21289.1; !1PID:g244378 !'##note point mutation from a patient with Lesh-Nyhan syndrome !$#accession I64798 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 103-107,'VL' ##label YAM2 !'##cross-references GB:S79320; NID:g244383; PIDN:AAB21292.1; !1PID:g244384 !'##note frameshift mutation from a patient with Lesh-Nyhan syndrome !$#accession I64796 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 103-106,'TSQQGT' ##label YAM3 !'##cross-references GB:S79316; NID:g244379; PIDN:AAB21290.1; !1PID:g244380 !$#accession I64797 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 103-106,'STGDIK' ##label YAM4 !'##cross-references GB:S79318; NID:g244381; PIDN:AAB21291.1; !1PID:g244382 REFERENCE I57607 !$#authors Patel, P.I.; Framson, P.E.; Caskey, C.T.; Chinault, A.C. !$#journal Mol. Cell. Biol. (1986) 6:393-403 !$#title Fine structure of the human hypoxanthine !1phosphoribosyltransferase gene. !$#cross-references MUID:87064322; PMID:3023844 !$#accession I57607 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-9 ##label PAT !'##cross-references GB:M12452; NID:g184351; PIDN:AAA52691.1; !1PID:g184352 GENETICS !$#gene GDB:HPRT1; HPRT !'##cross-references GDB:119317; OMIM:308000 !$#map_position Xq26.1-Xq26.1 !$#note mutations in this gene can cause Lesch-Nyhan syndrome in !1which there is no enzyme activity, and hyperuricemia with an !1early onset of gout, in which there is partial enzyme !1activity FUNCTION !$#description catalyzes the formation of guanine monophosphate (GMP) or !1inosine monophosphate (IMP) and pyrophosphate from !15-phospho-alpha-D-ribose 1-diphosphate, and guanine or !1hypoxanthine CLASSIFICATION #superfamily hypoxanthine phosphoribosyltransferase KEYWORDS acetylated amino end; glycosyltransferase; !1pentosyltransferase; salvage pathway FEATURE !$2-218 #product hypoxanthine phosphoribosyltransferase !8#status experimental #label MAT\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental SUMMARY #length 218 #molecular-weight 24579 #checksum 6530 SEQUENCE /// ENTRY RTMSG #type complete TITLE hypoxanthine phosphoribosyltransferase (EC 2.4.2.8) - mouse ALTERNATE_NAMES hypoxanthine-guanine phosphoribosyltransferase ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1989 #sequence_revision 09-Aug-1997 #text_change 11-Jun-1999 ACCESSIONS I49756; A26218; A00579 REFERENCE I49756 !$#authors Melton, D.W.; Konecki, D.S.; Brennand, J.; Caskey, C.T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:2147-2151 !$#title Structure, expression,and mutation of the hypoxanthine !1phosphoribosyltransferase gene. !$#cross-references MUID:84193967; PMID:6326107 !$#accession I49756 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-218 ##label RES !'##cross-references GB:K01515; NID:g193994; PIDN:AAA96271.1; !1PID:g387206 REFERENCE A93446 !$#authors Konecki, D.S.; Brennand, J.; Fuscoe, J.C.; Caskey, C.T.; !1Chinault, A.C. !$#journal Nucleic Acids Res. (1982) 10:6763-6775 !$#title Hypoxanthine-guanine phosphoribosyltransferase genes of !1mouse and Chinese hamster: construction and sequence !1analysis of cDNA recombinants. !$#cross-references MUID:83090437; PMID:6294614 !$#accession A26218 !'##molecule_type mRNA !'##residues 2-200,'N',202-218 ##label KON !'##cross-references GB:J00423; NID:g193984; PIDN:AAA96232.1; !1PID:g309315 !'##note initiator Met not shown !'##note this variant protein has enzymatic activity and its sequence is !1expected to be very similar to the wild type; the gene was !1cloned from a mutant cell line derived in turn from another !1mutant line having no enzymatic activity GENETICS !$#introns 9/3; 45/2; 106/3; 128/3; 134/3; 162/2; 178/1; 203/3 CLASSIFICATION #superfamily hypoxanthine phosphoribosyltransferase KEYWORDS glycosyltransferase; pentosyltransferase; salvage pathway SUMMARY #length 218 #molecular-weight 24570 #checksum 6540 SEQUENCE /// ENTRY RTHYG #type complete TITLE hypoxanthine phosphoribosyltransferase (EC 2.4.2.8) - Chinese hamster ALTERNATE_NAMES hypoxanthine-guanine phosphoribosyltransferase ORGANISM #formal_name Cricetulus griseus #common_name Chinese hamster DATE 31-Dec-1989 #sequence_revision 12-Apr-1996 #text_change 01-Dec-2000 ACCESSIONS S14402; A26219; I58003; A00579 REFERENCE S14402 !$#authors Rossiter, B.J.F.; Fuscoe, J.C.; Muzny, D.M.; Fox, M.; !1Caskey, C.T. !$#journal Genomics (1991) 9:247-256 !$#title The Chinese hamster HPRT gene: restriction map, sequence !1analysis, and multiplex PCR deletion screen. !$#cross-references MUID:91169526; PMID:2004774 !$#accession S14402 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-218 ##label ROS !'##cross-references EMBL:X53073; NID:g49505; PIDN:CAA37247.1; !1PID:g817936 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1May 1990 REFERENCE A93446 !$#authors Konecki, D.S.; Brennand, J.; Fuscoe, J.C.; Caskey, C.T.; !1Chinault, A.C. !$#journal Nucleic Acids Res. (1982) 10:6763-6775 !$#title Hypoxanthine-guanine phosphoribosyltransferase genes of !1mouse and Chinese hamster: construction and sequence !1analysis of cDNA recombinants. !$#cross-references MUID:83090437; PMID:6294614 !$#accession A26219 !'##molecule_type mRNA !'##residues 2-218 ##label KON !'##cross-references GB:J00060; NID:g191112; PIDN:AAA36990.1; !1PID:g304515 !'##note initiator Met not shown !'##note this variant protein has enzymatic activity and its sequence is !1expected to be very similar to the wild type; the gene was !1cloned from a mutant cell line derived in turn from another !1mutant line having no enzymatic activity REFERENCE I58003 !$#authors Fuscoe, J.C.; Zimmerman, L.J.; Fekete, A.; Setzer, R.W.; !1Rossiter, B.J. !$#journal Mutat. Res. (1992) 269:171-183 !$#title Analysis of X-ray-induced HPRT mutations in CHO cells: !1insertion and deletions. !$#cross-references MUID:93024555; PMID:1383700 !$#accession I58003 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 32-44 ##label RES !'##cross-references GB:S46270; NID:g257049 GENETICS !$#gene hprt !$#introns 9/3; 45/2; 106/3; 128/3; 134/3; 162/2; 178/1; 203/3 CLASSIFICATION #superfamily hypoxanthine phosphoribosyltransferase KEYWORDS glycosyltransferase; pentosyltransferase; salvage pathway SUMMARY #length 218 #molecular-weight 24643 #checksum 6761 SEQUENCE /// ENTRY S76559 #type complete TITLE probable uracil phosphoribosyltransferase (EC 2.4.2.9) - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S76559 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76559 !'##status preliminary !'##molecule_type DNA !'##residues 1-178 ##label KAN !'##cross-references EMBL:D64002; GB:AB001339; NID:g1001612; !1PIDN:BAA10405.1; PID:g1001670 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily hypoxanthine phosphoribosyltransferase KEYWORDS DNA binding; glycosyltransferase; pentosyltransferase; !1transcription regulation SUMMARY #length 178 #molecular-weight 19946 #checksum 2759 SEQUENCE /// ENTRY B57986 #type complete TITLE uracil phosphoribosyltransferase (EC 2.4.2.9) pyrR - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 20-Apr-2000 #text_change 16-Jun-2000 ACCESSIONS A69687; A59228; A39845; B57986 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69687 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-181 ##label KUN !'##cross-references GB:Z99112; GB:AL009126; NID:g2633902; !1PIDN:CAB13421.1; PID:g2633920 !'##experimental_source strain 168 REFERENCE A38984 !$#authors Turner, R.J.; Lu, Y.; Switzer, R.L. !$#journal J. Bacteriol. (1994) 176:3708-3722 !$#title Regulation of the Bacillus subtilis pyrimidine biosynthetic !1(pyr) gene cluster by an autogenous transcriptional !1attenuation mechanism. !$#cross-references MUID:94266724; PMID:8206849 !$#accession A59228 !'##molecule_type DNA !'##residues 1-181 ##label TUR !'##cross-references GB:M59757; NID:g4887706; PIDN:AAA21265.2; !1PID:g4887707 !'##note this sequence has been revised from that in ref A39845 REFERENCE A39845 !$#authors Quinn, C.L.; Stephenson, B.T.; Switzer, R.L. !$#journal J. Biol. Chem. (1991) 266:9113-9127 !$#title Functional organization and nucleotide sequence of the !1Bacillus subtilis pyrimidine biosynthetic operon. !$#cross-references MUID:91225016; PMID:1709162 !$#accession A39845 !'##molecule_type DNA !'##residues 1-33,'S',35-52,'P',54-181 ##label QUI !'##cross-references GB:M59757; NID:g387576 !'##note this sequence has been revised in reference A38984 GENETICS !$#gene pyrR CLASSIFICATION #superfamily hypoxanthine phosphoribosyltransferase KEYWORDS DNA binding; glycosyltransferase; pentosyltransferase; !1transcription regulation SUMMARY #length 181 #molecular-weight 20263 #checksum 3512 SEQUENCE /// ENTRY S38892 #type complete TITLE uracil phosphoribosyltransferase (EC 2.4.2.9) pyrR - Bacillus caldolyticus ORGANISM #formal_name Bacillus caldolyticus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S38892 REFERENCE S38892 !$#authors Ghim, S.Y.; Neuhard, J. !$#submission submitted to the EMBL Data Library, November 1993 !$#description The pyrimidine biosynthesis operon of the thermophile !1Bacillus caldolyticus includes genes for uracil !1phosphoribosyltransferase and uracil permease. !$#accession S38892 !'##status preliminary !'##molecule_type DNA !'##residues 1-179 ##label GHI !'##cross-references EMBL:X76083; NID:g431229; PIDN:CAA53696.1; !1PID:g431230 GENETICS !$#gene pyrR CLASSIFICATION #superfamily hypoxanthine phosphoribosyltransferase KEYWORDS DNA binding; glycosyltransferase; pentosyltransferase; !1transcription regulation SUMMARY #length 179 #molecular-weight 19938 #checksum 2417 SEQUENCE /// ENTRY G64069 #type complete TITLE uracil phosphoribosyltransferase (EC 2.4.2.9) pyrR - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS G64069 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession G64069 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-179 ##label TIGR !'##cross-references GB:U32728; GB:L42023; NID:g1573425; !1PIDN:AAC22117.1; PID:g1573433; TIGR:HI0459 GENETICS !$#gene purR CLASSIFICATION #superfamily hypoxanthine phosphoribosyltransferase KEYWORDS DNA binding; glycosyltransferase; pentosyltransferase; !1transcription regulation SUMMARY #length 179 #molecular-weight 20527 #checksum 3203 SEQUENCE /// ENTRY A65026 #type complete TITLE uracil phosphoribosyltransferase (EC 2.4.2.9) upp - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS A65026; S23412 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65026 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-217 ##label BLAT !'##cross-references GB:AE000336; GB:U00096; NID:g1788839; !1PIDN:AAC75551.1; PID:g1788844; UWGP:b2498 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S23412 !$#authors Andersen, P.S.; Smith, J.M.; Mygind, B. !$#journal Eur. J. Biochem. (1992) 204:51-56 !$#title Characterization of the upp gene encoding uracil !1phosphoribosyltransferase of Escherichia coli K12. !$#cross-references MUID:92155236; PMID:1371255 !$#accession S23412 !'##molecule_type DNA !'##residues 10-217 ##label AND !'##cross-references EMBL:X57104; NID:g43271; PIDN:CAA40388.1; !1PID:g43272 GENETICS !$#gene upp CLASSIFICATION #superfamily uracil phosphoribosyltransferase upp KEYWORDS glycosyltransferase; pentosyltransferase SUMMARY #length 217 #molecular-weight 23559 #checksum 7787 SEQUENCE /// ENTRY E64111 #type complete TITLE uracil phosphoribosyltransferase (EC 2.4.2.9) upp-type - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS E64111 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession E64111 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-208 ##label TIGR !'##cross-references GB:U32802; GB:L42023; NID:g1574151; !1PIDN:AAC22881.1; PID:g1574158; TIGR:HI1228 CLASSIFICATION #superfamily uracil phosphoribosyltransferase upp KEYWORDS glycosyltransferase; pentosyltransferase SUMMARY #length 208 #molecular-weight 22664 #checksum 8231 SEQUENCE /// ENTRY I40484 #type complete TITLE uracil phosphoribosyltransferase (EC 2.4.2.9) upp - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS I40484; A69729; S49364 REFERENCE I40473 !$#authors Martinussen, J.; Glaser, P.; Andersen, P.S.; Saxild, H.H. !$#journal J. Bacteriol. (1995) 177:271-274 !$#title Two genes encoding uracil phosphoribosyltransferase are !1present in Bacillus subtilis. !$#cross-references MUID:95095982; PMID:7798145 !$#accession I40484 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-209 ##label RES !'##cross-references EMBL:Z38002; NID:g556877; PIDN:CAA86111.1; !1PID:g556887 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69729 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-209 ##label KUN !'##cross-references GB:Z99122; GB:AL009126; NID:g2636029; !1PIDN:CAB15706.1; PID:g2636214 !'##experimental_source strain 168 GENETICS !$#gene upp CLASSIFICATION #superfamily uracil phosphoribosyltransferase upp KEYWORDS glycosyltransferase; pentosyltransferase SUMMARY #length 209 #molecular-weight 23037 #checksum 9909 SEQUENCE /// ENTRY S74616 #type complete TITLE uracil phosphoribosyltransferase (EC 2.4.2.9) upp - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES hypothetical protein sll1035 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S74616 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74616 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-216 ##label KAN !'##cross-references EMBL:D90900; GB:AB001339; NID:g1651768; !1PIDN:BAA16768.1; PID:g1651841 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene upp CLASSIFICATION #superfamily uracil phosphoribosyltransferase upp KEYWORDS glycosyltransferase; pentosyltransferase SUMMARY #length 216 #molecular-weight 23637 #checksum 5743 SEQUENCE /// ENTRY C64203 #type complete TITLE uracil phosphoribosyltransferase (EC 2.4.2.9) upp-type - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 07-Dec-1999 ACCESSIONS C64203 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession C64203 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-206 ##label TIGR !'##cross-references GB:U39681; GB:L43967; NID:g1045694; PID:g1045700; !1TIGR:MG030 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 !$#start_codon GTG CLASSIFICATION #superfamily uracil phosphoribosyltransferase upp KEYWORDS glycosyltransferase; pentosyltransferase SUMMARY #length 206 #molecular-weight 22973 #checksum 7583 SEQUENCE /// ENTRY S73447 #type complete TITLE uracil phosphoribosyltransferase (EC 2.4.2.9) upp - Mycoplasma pneumoniae (strain ATCC 29342) ALTERNATE_NAMES hypothetical protein B01_orf178 ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Dec-1999 ACCESSIONS S73447 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73447 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-178 ##label HIM !'##cross-references EMBL:AE000015; GB:U00089; NID:g1673779; !1PIDN:AAB95769.1; PID:g1673780 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#gene upp !$#genetic_code SGC3 CLASSIFICATION #superfamily uracil phosphoribosyltransferase upp KEYWORDS glycosyltransferase; pentosyltransferase SUMMARY #length 178 #molecular-weight 19484 #checksum 6819 SEQUENCE /// ENTRY F70485 #type complete TITLE uracil phosphoribosyltransferase (EC 2.4.2.9) upp-type - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS F70485 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession F70485 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-208 ##label AQF !'##cross-references GB:AE000776; NID:g2984355; PIDN:AAC07880.1; !1PID:g2984361; GB:AE000657 !'##experimental_source strain VF5 GENETICS !$#gene uraP CLASSIFICATION #superfamily uracil phosphoribosyltransferase upp KEYWORDS glycosyltransferase; pentosyltransferase SUMMARY #length 208 #molecular-weight 23532 #checksum 9534 SEQUENCE /// ENTRY C69015 #type complete TITLE probable uracil phosphoribosyltransferase (EC 2.4.2.9) upp-type - Methanobacterium thermoautotrophicum (strain Delta H) ALTERNATE_NAMES hypothetical protein MTH1114 ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C69015 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession C69015 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-215 ##label MTH !'##cross-references GB:AE000881; GB:AE000666; NID:g2622206; !1PIDN:AAB85603.1; PID:g2622216 !'##experimental_source strain Delta H GENETICS !$#gene MTH1114 !$#start_codon GTG CLASSIFICATION #superfamily uracil phosphoribosyltransferase upp KEYWORDS glycosyltransferase; pentosyltransferase SUMMARY #length 215 #molecular-weight 23827 #checksum 544 SEQUENCE /// ENTRY JH0147 #type complete TITLE uracil phosphoribosyltransferase (EC 2.4.2.9) FUR1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YHR128w ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 23-Mar-2001 ACCESSIONS JH0147; S48972; S48293; S19643 REFERENCE JH0147 !$#authors Kern, L.; de Montigny, J.; Jund, R.; Lacroute, F. !$#journal Gene (1990) 88:149-157 !$#title The FUR1 gene of Saccharomyces cerevisiae: cloning, !1structure and expression of wild-type and mutant alleles. !$#cross-references MUID:90269602; PMID:2189783 !$#accession JH0147 !'##molecule_type DNA !'##residues 1-251 ##label KER !'##cross-references GB:M36485; NID:g171528; PIDN:AAA34611.1; !1PID:g171529 REFERENCE S48967 !$#authors Fulton, L. !$#submission submitted to the EMBL Data Library, June 1994 !$#description The sequence of S. cerevisiae cosmid 9315. !$#accession S48972 !'##molecule_type DNA !'##residues 1-251 ##label FUL !'##cross-references EMBL:U10398; NID:g551328; PIDN:AAB68405.1; !1PID:g500672; GSPDB:GN00008; MIPS:YHR128w REFERENCE S48292 !$#authors Clark, S.W.; Meyer, D.I. !$#journal J. Cell Biol. (1994) 127:129-138 !$#title ACT3: A putative centractin homologue in S. cerevisiae is !1required for proper orientation of the mitotic spindle. !$#cross-references MUID:95014703; PMID:7929558 !$#accession S48293 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-251 ##label CLA !'##cross-references EMBL:X79811; NID:g557669; PIDN:CAA56207.1; !1PID:g557671 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1994 COMMENT This enzyme catalyzes the conversion of uracil into uridine !15'-monophosphate and pyrophosphate in the pyrimidine salvage !1pathway. GENETICS !$#gene SGD:FUR1; MIPS:YHR128w !'##cross-references SGD:S0001170; MIPS:YHR128w !$#map_position 8R CLASSIFICATION #superfamily uracil phosphoribosyltransferase upp KEYWORDS glycosyltransferase; pentosyltransferase; salvage pathway SUMMARY #length 251 #molecular-weight 28748 #checksum 6454 SEQUENCE /// ENTRY XJEC #type complete TITLE orotate phosphoribosyltransferase (EC 2.4.2.10) pyrE [similarity] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 19-Feb-1984 #sequence_revision 23-Jan-1998 #text_change 01-Mar-2002 ACCESSIONS D65165; A00580 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65165 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-213 ##label BLAT !'##cross-references GB:AE000441; GB:U00096; NID:g1790063; !1PIDN:AAC76666.1; PID:g1790073; UWGP:b3642 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A05110 !$#authors Poulsen, P.; Jensen, K.F.; Valentin-Hansen, P.; Carlsson, !1P.; Lundberg, L.G. !$#journal Eur. J. Biochem. (1983) 135:223-229 !$#title Nucleotide sequence of the Escherichia coli pyrE gene and of !1the DNA in front of the protein-coding region. !$#cross-references MUID:83287414; PMID:6349999 !$#accession A00580 !'##molecule_type DNA !'##residues 1-35,'T',37-132,134-149,'L',151-193,'RL',196-213 ##label !1POU !'##note the authors translated the codons for residues 36, 150, 194, !1and 195 as Asn, Val, Lys, and Pro, respectively GENETICS !$#gene pyrE !$#map_position 82 min FUNCTION !$#description catalyzes the formation of orotidine 5'-phosphate and !1pyrophosphate from orotate and 5'-phospho-alpha-D-ribose !11-diphosphate !$#pathway pyrimidine nucleotide biosynthesis CLASSIFICATION #superfamily orotate phosphoribosyltransferase; orotate !1phosphoribosyltransferase homology KEYWORDS glycosyltransferase; pentosyltransferase; pyrimidine !1nucleotide biosynthesis FEATURE !$1-192 #domain orotate phosphoribosyltransferase homology !8#label OPT\ !$2-213 #product orotate phosphoribosyltransferase #status !8predicted #label MAT SUMMARY #length 213 #molecular-weight 23567 #checksum 7164 SEQUENCE /// ENTRY XJBY5 #type complete TITLE orotate phosphoribosyltransferase (EC 2.4.2.10) URA5 [validated] - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YM8339.13; protein YML106w ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1993 #sequence_revision 01-Sep-1995 #text_change 31-Mar-2000 ACCESSIONS S53966; JV0010; S51917; S07618 REFERENCE S53954 !$#authors Skelton, J.; Churcher, C.M. !$#submission submitted to the EMBL Data Library, May 1995 !$#accession S53966 !'##molecule_type DNA !'##residues 1-226 ##label SKE !'##cross-references EMBL:Z49210; NID:g798881; PIDN:CAA89112.1; !1PID:g798894; GSPDB:GN00013; MIPS:YML106w REFERENCE JV0010 !$#authors de Montigny, J.; Belarbi, A.; Hubert, J.C.; Lacroute, F. !$#journal Mol. Gen. Genet. (1989) 215:455-462 !$#title Structure and expression of the URA5 gene of Saccharomyces !1cerevisiae. !$#cross-references MUID:89218955; PMID:2651891 !$#accession JV0010 !'##molecule_type DNA !'##residues 1-149,'S',151-226 ##label DEM !'##cross-references EMBL:X14795; NID:g4766; PIDN:CAA32901.1; PID:g4767 REFERENCE S51916 !$#authors Stirling, C.J. !$#submission submitted to the EMBL Data Library, February 1995 !$#accession S51917 !'##molecule_type DNA !'##residues 13-226 ##label STI !'##cross-references EMBL:X65783; NID:g671637; PIDN:CAA46665.1; !1PID:g671639 GENETICS !$#gene SGD:URA5; MIPS:YML106w !'##cross-references SGD:S0004574; MIPS:YML106w !$#map_position 13L CLASSIFICATION #superfamily orotate phosphoribosyltransferase; orotate !1phosphoribosyltransferase homology KEYWORDS glycosyltransferase; pentosyltransferase; pyrimidine !1nucleotide biosynthesis FEATURE !$1-204 #domain orotate phosphoribosyltransferase homology !8#label OPT\ !$133-138 #region phosphoribosylpyrophosphate binding #status !8predicted SUMMARY #length 226 #molecular-weight 24664 #checksum 883 SEQUENCE /// ENTRY XJBY10 #type complete TITLE orotate phosphoribosyltransferase (EC 2.4.2.10) URA10 [validated] - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YM8156.13c; protein YMR271c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1993 #sequence_revision 17-Nov-1995 #text_change 31-Mar-2000 ACCESSIONS S48223; S54483; S22854; S21537; S43623 REFERENCE S48223 !$#authors Hohmann, S.; van Dijck, P.; Luyten, K.; Thevelein, J.M. !$#journal Curr. Genet. (1994) 26:295-301 !$#title The byp1-3 allele of the Saccharomyces cerevisiae GGS1/TPS1 !1gene and its multi-copy suppressor tRNA(GLN) (CAG): Ggs1/ !1Tps1 protein levels restraining growth on fermentable sugars !1and trehalose accumulation. !$#cross-references MUID:95188265; PMID:7882422 !$#accession S48223 !'##molecule_type DNA !'##residues 1-227 ##label HOH !'##cross-references EMBL:X66375; NID:g4758; PIDN:CAA47016.1; PID:g4759 REFERENCE S54014 !$#authors Lye, G.; Churcher, C.M. !$#submission submitted to the EMBL Data Library, May 1995 !$#accession S54483 !'##molecule_type DNA !'##residues 1-227 ##label LYE !'##cross-references EMBL:Z49260; NID:g809081; PIDN:CAA89254.1; !1PID:g809094; GSPDB:GN00013; MIPS:YMR271c !'##experimental_source strain AB972 REFERENCE S22854 !$#authors de Montigny, J.; Kern, L.; Hubert, J.C.; Lacroute, F. !$#journal Curr. Genet. (1990) 17:105-111 !$#title Cloning and sequencing of URA10, a second gene encoding !1orotate phosphoribosyl transferase in Saccharomyces !1cerevisiae. !$#cross-references MUID:90213539; PMID:2182197 !$#accession S22854 !'##molecule_type DNA !'##residues 1-142,'R',144-157,'L',159-227 ##label DEM !'##cross-references EMBL:X52194; NID:g4756; PIDN:CAA36440.1; PID:g4757 !'##note the authors translated the codon AAC for residue 55 as Leu and !1CTA for residue 158 as Val REFERENCE S21537 !$#authors Hohman, S. !$#submission submitted to the EMBL Data Library, May 1992 !$#accession S21537 !'##molecule_type DNA !'##residues 1-227 ##label HOF !'##cross-references EMBL:X66375; NID:g4758; PIDN:CAA47016.1; PID:g4759 REFERENCE S43623 !$#authors Mockovciakova, D.; Janitorova, V.; Zigova, M.; Kaclikova, !1E.; Zagulski, M.; Subik, J. !$#journal Curr. Genet. (1993) 24:377-381 !$#title The ogd1 and kgd1 mutants lacking 2-oxoglutarate !1dehydrogenase activity in yeast are allelic and can be !1differentiated by the cloned amber suppressor. !$#cross-references MUID:94130313; PMID:8299151 !$#accession S43623 !'##status translation not shown !'##molecule_type DNA !'##residues 82-142,'R',144-199,'N',201-223,'PMV',225,'EL' ##label MOC !'##cross-references EMBL:X75376; NID:g469105; PIDN:CAA53149.1; !1PID:g940864 GENETICS !$#gene SGD:URA10; MIPS:YMR271c !'##cross-references SGD:S0004884; MIPS:YMR271c !$#map_position 13R CLASSIFICATION #superfamily orotate phosphoribosyltransferase; orotate !1phosphoribosyltransferase homology KEYWORDS glycosyltransferase; pentosyltransferase; pyrimidine !1nucleotide biosynthesis FEATURE !$5-207 #domain orotate phosphoribosyltransferase homology !8#label OPT\ !$132-142 #region phosphoribosylpyrophosphate binding #status !8predicted SUMMARY #length 227 #molecular-weight 24810 #checksum 7524 SEQUENCE /// ENTRY A29459 #type complete TITLE orotate phosphoribosyltransferase (EC 2.4.2.10) - Podospora anserina ALTERNATE_NAMES orotidine-5'-phosphate pyrophosphorylase; orotidylic acid phosphorylase ORGANISM #formal_name Podospora anserina DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A29459 REFERENCE A29459 !$#authors Turcq, B.; Begueret, J. !$#journal Gene (1987) 53:201-209 !$#title The ura5 gene of the filamentous fungus Podospora anserina: !1nucleotide sequence and expression in transformed strains. !$#cross-references MUID:87277410; PMID:3609748 !$#accession A29459 !'##molecule_type DNA !'##residues 1-231 ##label TUR CLASSIFICATION #superfamily orotate phosphoribosyltransferase; orotate !1phosphoribosyltransferase homology KEYWORDS glycosyltransferase; pentosyltransferase; pyrimidine !1nucleotide biosynthesis FEATURE !$1-209 #domain orotate phosphoribosyltransferase homology !8#label OPT SUMMARY #length 231 #molecular-weight 25353 #checksum 7513 SEQUENCE /// ENTRY JS0175 #type complete TITLE orotate phosphoribosyltransferase (EC 2.4.2.10) - Sordaria macrospora ALTERNATE_NAMES orotidine-5'-phosphate pyrophosphorylase; orotidylic acid phosphorylase ORGANISM #formal_name Sordaria macrospora DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JS0175 REFERENCE JS0175 !$#authors Le Chevanton, L.; Leblon, G. !$#journal Gene (1989) 77:39-49 !$#title The ura5 gene of the ascomycete Sordaria macrospora: !1molecular cloning, characterization and expression in !1Escherichia coli. !$#cross-references MUID:89306679; PMID:2663654 !$#accession JS0175 !'##molecule_type DNA !'##residues 1-232 ##label LEC !'##cross-references GB:M26957; NID:g341555; PIDN:AAA33929.1; !1PID:g530193 !'##experimental_source strain FGSC4818, ATCC60255 !'##note this sequence shows high homology with that from Podospora !1anserina GENETICS !$#gene ura5 CLASSIFICATION #superfamily orotate phosphoribosyltransferase; orotate !1phosphoribosyltransferase homology KEYWORDS glycosyltransferase; pentosyltransferase; pyrimidine !1nucleotide biosynthesis FEATURE !$3-210 #domain orotate phosphoribosyltransferase homology !8#label OPT\ !$132-135 #region phosphoribosylpyrophosphate binding #status !8predicted SUMMARY #length 232 #molecular-weight 24944 #checksum 5095 SEQUENCE /// ENTRY S30118 #type complete TITLE orotate phosphoribosyltransferase (EC 2.4.2.10) - anthracnose fungus (Colletotrichum graminicola) ORGANISM #formal_name Glomerella graminicola, Colletotrichum graminicola DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S30118 REFERENCE S30118 !$#authors Rasmussen, J.B.; Panaccione, D.G.; Fang, G.C.; Hanau, R.M. !$#journal Mol. Gen. Genet. (1992) 235:74-80 !$#title The PYR1 gene of the plant pathogenic fungus Colletotrichum !1graminicola: selection by intraspecific complementation and !1sequence analysis. !$#cross-references MUID:93062810; PMID:1435732 !$#accession S30118 !'##molecule_type DNA !'##residues 1-233 ##label RAS !'##cross-references EMBL:S47907; NID:g259366; PIDN:AAB24061.1; !1PID:g259367 GENETICS !$#gene PYR1 CLASSIFICATION #superfamily orotate phosphoribosyltransferase; orotate !1phosphoribosyltransferase homology KEYWORDS glycosyltransferase; pentosyltransferase; pyrimidine !1nucleotide biosynthesis FEATURE !$2-211 #domain orotate phosphoribosyltransferase homology !8#label OPT SUMMARY #length 233 #molecular-weight 25231 #checksum 5380 SEQUENCE /// ENTRY S13091 #type complete TITLE orotate phosphoribosyltransferase (EC 2.4.2.10) - fungus (Trichoderma reesei) ORGANISM #formal_name Trichoderma reesei DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S13091 REFERENCE S13090 !$#authors Berges, T.; Perrot, M.; Barreau, C. !$#journal Nucleic Acids Res. (1990) 18:7183 !$#title Nucleotide sequences of the Trichoderma reesei ura3 !1(OMPdecase) and ura5 (OPRTase) genes. !$#cross-references MUID:91088344; PMID:2263502 !$#accession S13091 !'##status preliminary !'##molecule_type DNA !'##residues 1-236 ##label BER !'##cross-references EMBL:X55879; NID:g5187; PIDN:CAA39364.1; PID:g5188 CLASSIFICATION #superfamily orotate phosphoribosyltransferase; orotate !1phosphoribosyltransferase homology KEYWORDS glycosyltransferase; pentosyltransferase FEATURE !$4-214 #domain orotate phosphoribosyltransferase homology !8#label OPT SUMMARY #length 236 #molecular-weight 25742 #checksum 8935 SEQUENCE /// ENTRY A60993 #type complete TITLE orotate phosphoribosyltransferase (EC 2.4.2.10) pyrE [validated] - Lactobacillus plantarum ORGANISM #formal_name Lactobacillus plantarum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 31-Mar-2000 ACCESSIONS A60993 REFERENCE A60993 !$#authors Bouia, A.; Bringel, F.; Frey, L.; Belarbi, A.; Guyonvarch, !1A.; Kammerer, B.; Hubert, J.C. !$#journal FEMS Microbiol. Lett. (1990) 69:233-238 !$#title Cloning and structure of the pyrE gene of Lactobacillus !1plantarum CCM 1904. !$#accession A60993 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-212 ##label BOU GENETICS !$#gene pyrE CLASSIFICATION #superfamily orotate phosphoribosyltransferase; orotate !1phosphoribosyltransferase homology KEYWORDS glycosyltransferase; pentosyltransferase; pyrimidine !1nucleotide biosynthesis FEATURE !$1-197 #domain orotate phosphoribosyltransferase homology !8#label OPT SUMMARY #length 212 #molecular-weight 22705 #checksum 8745 SEQUENCE /// ENTRY F69686 #type complete TITLE orotate phosphoribosyltransferase (EC 2.4.2.10) pyrE [similarity] - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 05-Dec-1997 #sequence_revision 02-Jul-1998 #text_change 16-Jun-2000 ACCESSIONS F69686; A30492 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69686 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-216 ##label KUN !'##cross-references GB:Z99112; GB:AL009126; NID:g2633902; !1PIDN:CAB13430.1; PID:g2633929 !'##experimental_source strain 168 REFERENCE A39845 !$#authors Quinn, C.L.; Stephenson, B.T.; Switzer, R.L. !$#journal J. Biol. Chem. (1991) 266:9113-9127 !$#title Functional organization and nucleotide sequence of the !1Bacillus subtilis pyrimidine biosynthetic operon. !$#cross-references MUID:91225016; PMID:1709162 !$#accession A30492 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 'M',8-216 ##label QUI !'##cross-references GB:M59757; NID:g387576 !'##note these authors used TTG as a start codon GENETICS !$#gene pyrE FUNCTION !$#description catalyzes the formation of orotidine 5'-phosphate and !1pyrophosphate from orotate and 5-phospho-alpha-D-ribose !11-diphosphate !$#pathway pyrimidine nucleotide biosynthesis CLASSIFICATION #superfamily orotate phosphoribosyltransferase; orotate !1phosphoribosyltransferase homology KEYWORDS glycosyltransferase; pentosyltransferase; pyrimidine !1nucleotide biosynthesis FEATURE !$7-200 #domain orotate phosphoribosyltransferase homology !8#label OPT SUMMARY #length 216 #molecular-weight 23522 #checksum 9788 SEQUENCE /// ENTRY I40173 #type complete TITLE orotate phosphoribosyltransferase (EC 2.4.2.10) pyrE [similarity] - Bacillus caldolyticus ORGANISM #formal_name Bacillus caldolyticus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 31-Mar-2000 ACCESSIONS I40173; S34325 REFERENCE I40166 !$#authors Ghim, S.Y.; Neuhard, J. !$#journal J. Bacteriol. (1994) 176:3698-3707 !$#title The pyrimidine biosynthesis operon of the thermophile !1Bacillus caldolyticus includes genes for uracil !1phosphoribosyltransferase and uracil permease. !$#cross-references MUID:94266723; PMID:8206848 !$#accession I40173 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-206 ##label RES !'##cross-references EMBL:X73308; NID:g312439; PIDN:CAA51743.1; !1PID:g312447 REFERENCE S34318 !$#authors Ghim, S.Y.; Nielsen, P.; Neuhard, J. !$#submission submitted to the EMBL Data Library, June 1993 !$#description Molecular characterization of pyrimidine biosynthesis genes !1from the thermophile Bacillus caldolyticus. !$#accession S34325 !'##molecule_type DNA !'##residues 1-206 ##label GHI !'##cross-references EMBL:X73308; NID:g312439; PIDN:CAA51743.1; !1PID:g312447 GENETICS !$#gene pyrE CLASSIFICATION #superfamily orotate phosphoribosyltransferase; orotate !1phosphoribosyltransferase homology KEYWORDS glycosyltransferase; pentosyltransferase FEATURE !$1-193 #domain orotate phosphoribosyltransferase homology !8#label OPT SUMMARY #length 206 #molecular-weight 22401 #checksum 1651 SEQUENCE /// ENTRY A30148 #type complete TITLE UMP synthase - human ALTERNATE_NAMES protein DKFZp564G1272.1; uridine monophosphate synthase CONTAINS orotate phosphoribosyltransferase (EC 2.4.2.10); orotidine-5'-phosphate decarboxylase (EC 4.1.1.23) ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 31-Mar-2000 ACCESSIONS A30148; A60258; I58020; T12484 REFERENCE A30148 !$#authors Suttle, D.P.; Bugg, B.Y.; Winkler, J.K.; Kanalas, J.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:1754-1758 !$#title Molecular cloning and nucleotide sequence for the complete !1coding region of human UMP synthase. !$#cross-references MUID:88158071; PMID:3279416 !$#accession A30148 !'##molecule_type mRNA !'##residues 1-480 ##label SUT !'##cross-references GB:J03626; NID:g340167; PIDN:AAA61255.1; !1PID:g340168 REFERENCE A60258 !$#authors Suchi, M.; Harada, N.; Tsuboi, T.; Asai, K.; Okajima, K.; !1Wada, Y.; Takagi, Y. !$#journal Adv. Exp. Med. Biol. (1989) 253A:511-518 !$#title Molecular cloning of human UMP synthase. !$#cross-references MUID:90164247; PMID:2624233 !$#accession A60258 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-480 ##label SUC1 REFERENCE I58020 !$#authors Suchi, M. !$#journal Nagoya Med. J. (1988) 32:207-220 !$#title Molecular genetic studies on hereditary orotic aciduria: I. !1Purification of human orotidine 5'-monophosphate !1decarboxylase and cloning of its cDNA. !$#accession I58020 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 'G',14-376,'Q',378-480 ##label SUC2 !'##cross-references GB:M36661; NID:g340169; PIDN:AAA61256.1; !1PID:g340170 REFERENCE Z17526 !$#authors Blum, H.; Bauersachs, S.; Mewes, H.W.; Gassenhuber, J.; !1Wiemann, S. !$#submission submitted to the Protein Sequence Database, June 1999 !$#accession T12484 !'##molecule_type mRNA !'##residues 179-429 ##label BLU !'##cross-references EMBL:AL080099; NID:g5262522; PIDN:CAB45710.1; !1PID:g5262523 !'##experimental_source fetal brain; clone DKFZp564G1272 GENETICS !$#gene GDB:UMPS; DKFZp564G1272.1 !'##cross-references GDB:120482; OMIM:258900 !$#map_position 3q13-3q13 FUNCTION OPTD !$#description catalyzes conversion of orotidine 5'-phosphate and !1diphosphate to orotate and 5-phospho-alpha-D-ribose !11-diphosphate !$#pathway pyrimidine metabolism !$#note catalyzes the last two steps in de novo synthesis of UMP FUNCTION OPTU !$#description catalyzes the reversible conversion of orotidine !15'-phosphate to UMP and CO2 !$#pathway pyrimidine metabolism CLASSIFICATION #superfamily UMP synthase; orotate phosphoribosyltransferase !1homology; orotidine-5'-phosphate decarboxylase homology KEYWORDS carbon-carbon lyase; carboxy-lyase; glycosyltransferase; !1hexosyltransferase; pentosyltransferase; pyrimidine !1nucleotide biosynthesis FEATURE !$1-196 #domain orotate phosphoribosyltransferase homology !8#label OPT\ !$225-479 #domain orotidine-5'-phosphate decarboxylase homology !8#label OPD SUMMARY #length 480 #molecular-weight 52221 #checksum 4913 SEQUENCE /// ENTRY JN0558 #type complete TITLE UMP synthase - bovine ALTERNATE_NAMES uridine monophosphate synthase CONTAINS orotate phosphoribosyltransferase (EC 2.4.2.10); orotidine-5'-phosphate decarboxylase (EC 4.1.1.23) ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 31-Mar-2000 ACCESSIONS JN0558; S24266 REFERENCE JN0558 !$#authors Schoeber, S.; Simon, D.; Schwenger, B. !$#journal Gene (1993) 124:307-308 !$#title Sequence of the cDNA encoding bovine uridine monophosphate !1synthase. !$#cross-references MUID:93185942; PMID:8444356 !$#accession JN0558 !'##molecule_type mRNA !'##residues 1-480 ##label SCH !'##cross-references EMBL:X65125; NID:g831; PIDN:CAA46253.1; PID:g832 !'##experimental_source liver REFERENCE S24266 !$#authors Schoeber, S. !$#submission submitted to the EMBL Data Library, March 1992 !$#accession S24266 !'##status preliminary !'##molecule_type mRNA !'##residues 1-36,'S',38-480 ##label SC2 !'##cross-references EMBL:X65125 !'##experimental_source liver GENETICS !$#gene UMPS FUNCTION OPTD !$#description catalyzes conversion of orotidine 5'-phosphate and !1diphosphate to orotate and 5-phospho-alpha-D-ribose !11-diphosphate !$#pathway pyrimidine metabolism FUNCTION OPU !$#description catalyzes the reversible conversion of orotidine !15'-phosphate to UMP and CO2 !$#pathway pyrimidine metabolism CLASSIFICATION #superfamily UMP synthase; orotate phosphoribosyltransferase !1homology; orotidine-5'-phosphate decarboxylase homology KEYWORDS carbon-carbon lyase; carboxy-lyase; glycosyltransferase; !1hexosyltransferase; pentosyltransferase; pyrimidine !1nucleotide biosynthesis FEATURE !$1-196 #domain orotate phosphoribosyltransferase homology !8#label OPT\ !$225-479 #domain orotidine-5'-phosphate decarboxylase homology !8#label OPD SUMMARY #length 480 #molecular-weight 52229 #checksum 4145 SEQUENCE /// ENTRY JU0141 #type complete TITLE UMP synthase - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES uridine monophosphate synthase CONTAINS orotate phosphoribosyltransferase (EC 2.4.2.10); orotidine-5'-phosphate decarboxylase (EC 4.1.1.23) ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JU0141; S11907 REFERENCE JU0141 !$#authors Eisenberg, M.; Kirkpatrick, R.; Rawls, J. !$#journal Gene (1993) 124:263-267 !$#title Structure of the rudimentary-like gene and UMP synthase in !1Drosophila melanogaster. !$#cross-references MUID:93185933; PMID:8444350 !$#accession JU0141 !'##molecule_type DNA !'##residues 1-493 ##label EIS !'##cross-references GB:L00968 REFERENCE S11907 !$#authors Eisenberg, M.; Gathy, K.; Vincent, T.; Rawls, J. !$#journal Mol. Gen. Genet. (1990) 222:1-8 !$#title Molecular cloning of the UMP synthase gene rudimentary-like !1from Drosophila melanogaster. !$#cross-references MUID:91042409; PMID:2122228 !$#accession S11907 !'##molecule_type mRNA !'##residues 1-78 ##label EIW !'##cross-references GB:X54230; NID:g468803; PIDN:CAA38138.1; !1PID:g468804 COMMENT In higher eucaryotes this protein contains two distinct !1enzymatic domains, orotidylate decarboxylase and orotate !1phosphoribosyltransferase. GENETICS !$#gene FlyBase:r-l !'##cross-references FlyBase:FBgn0003257 !$#introns 51/3; 224/1 FUNCTION OPTD !$#description catalyzes conversion of orotidine 5'-phosphate and !1diphosphate to orotate and 5-phospho-alpha-D-ribose !11-diphosphate !$#pathway pyrimidine metabolism FUNCTION OPTU !$#description catalyzes the reversible conversion of orotidine !15'-phosphate to UMP and CO2 !$#pathway pyrimidine metabolism CLASSIFICATION #superfamily UMP synthase; orotate phosphoribosyltransferase !1homology; orotidine-5'-phosphate decarboxylase homology KEYWORDS carbon-carbon lyase; carboxy-lyase; glycosyltransferase; !1pentosyltransferase; pyrimidine nucleotide biosynthesis FEATURE !$1-197 #domain orotate phosphoribosyltransferase homology !8#label OPT\ !$232-492 #domain orotidine-5'-phosphate decarboxylase homology !8#label OPD SUMMARY #length 493 #molecular-weight 53479 #checksum 9868 SEQUENCE /// ENTRY S03826 #type complete TITLE UMP synthase - slime mold (Dictyostelium discoideum) ALTERNATE_NAMES uridine monophosphate synthase CONTAINS orotate phosphoribosyltransferase (EC 2.4.2.10); orotidine-5'-phosphate decarboxylase (EC 4.1.1.23) ORGANISM #formal_name Dictyostelium discoideum #variety strain AX3 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S03826 REFERENCE S03826 !$#authors Jacquet, M.; Guilbaud, R.; Garreau, H. !$#journal Mol. Gen. Genet. (1988) 211:441-445 !$#title Sequence analysis of the DdPYR5-6 gene coding for UMP !1synthase in Dictyostelium discoideum and comparison with !1orotate phosphoribosyl transferases and OMP decarboxylases. !$#cross-references MUID:88216255; PMID:2835631 !$#accession S03826 !'##molecule_type DNA !'##residues 1-478 ##label JAC !'##cross-references EMBL:X07560; NID:g7332; PIDN:CAA30443.1; PID:g7333 !'##experimental_source strain AX3 GENETICS !$#gene PYR5-6 FUNCTION !$#description catalyzes the conversion of orotidine 5'-phosphate and !1diphosphate to orotate and 5-phospho-alpha-D-ribose !11-diphosphate !$#pathway pyrimidine metabolism FUNCTION OPTD !$#description catalyzes the reversible conversion of orotidine !15'-phosphate to UMP and CO2 !$#pathway pyrimidine metabolism CLASSIFICATION #superfamily UMP synthase; orotate phosphoribosyltransferase !1homology; orotidine-5'-phosphate decarboxylase homology KEYWORDS carbon-carbon lyase; carboxy-lyase; glycosyltransferase; !1pentosyltransferase; pyrimidine nucleotide biosynthesis FEATURE !$1-194 #domain orotate phosphoribosyltransferase homology !8#label OPT\ !$225-478 #domain orotidine-5'-phosphate decarboxylase homology !8#label OPD SUMMARY #length 478 #molecular-weight 52536 #checksum 2622 SEQUENCE /// ENTRY JQ0756 #type complete TITLE nicotinate phosphoribosyltransferase (EC 2.4.2.11) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS JQ0756; B64833 REFERENCE JQ0756 !$#authors Wubbolts, M.G.; Terpstra, P.; van Beilen, J.B.; Kingma, J.; !1Meesters, H.A.R.; Witholt, B. !$#journal J. Biol. Chem. (1990) 265:17665-17672 !$#title Variation of cofactor levels in Escherichia coli; sequence !1analysis and expression of the pncB gene encoding nicitinic !1acid phosphoribosyltransferase. !$#cross-references MUID:91009224; PMID:2211655 !$#accession JQ0756 !'##status preliminary !'##molecule_type DNA !'##residues 1-400 ##label WUB !'##cross-references GB:J05568; NID:g147306; PIDN:AAA24400.1; !1PID:g147307 !'##experimental_source strain GEC70 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64833 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-400 ##label BLAT !'##cross-references GB:AE000195; GB:U00096; NID:g1787156; !1PIDN:AAC74017.1; PID:g1787162; UWGP:b0931 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene pncB FUNCTION !$#pathway nicotinate and nicotinamide metabolism CLASSIFICATION #superfamily nicotinate phosphoribosyltransferase KEYWORDS glycosyltransferase; pentosyltransferase SUMMARY #length 400 #molecular-weight 45897 #checksum 6749 SEQUENCE /// ENTRY A39130 #type complete TITLE nicotinate phosphoribosyltransferase (EC 2.4.2.11) - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A39130 REFERENCE A39130 !$#authors Vinitsky, A.; Teng, H.; Grubmeyer, C.T. !$#journal J. Bacteriol. (1991) 173:536-540 !$#title Cloning and nucleic acid sequence of the Salmonella !1typhimurium pncB gene and structure of nicotinate !1phosphoribosyltransferase. !$#cross-references MUID:91100340; PMID:1987148 !$#accession A39130 !'##status preliminary !'##molecule_type DNA !'##residues 1-400 ##label VIN !'##cross-references GB:M55986; NID:g154268; PIDN:AAA27190.1; !1PID:g154269 GENETICS !$#gene pncB FUNCTION !$#pathway nicotinate and nicotinamide metabolism CLASSIFICATION #superfamily nicotinate phosphoribosyltransferase KEYWORDS glycosyltransferase; pentosyltransferase SUMMARY #length 400 #molecular-weight 45661 #checksum 6638 SEQUENCE /// ENTRY XQEC #type complete TITLE amidophosphoribosyltransferase (EC 2.4.2.14) [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 18-Aug-1982 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS F65003; A92366; A92367; S01389; I51823; A00581 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65003 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-505 ##label BLAT !'##cross-references GB:AE000320; GB:U00096; NID:g1788647; !1PIDN:AAC75372.1; PID:g1788651; UWGP:b2312 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A92366 !$#authors Tso, J.Y.; Zalkin, H.; van Cleemput, M.; Yanofsky, C.; !1Smith, J.M. !$#journal J. Biol. Chem. (1982) 257:3525-3531 !$#title Nucleotide sequence of Escherichia coli purF and deduced !1amino acid sequence of glutamine phosphoribosylpyrophosphate !1amidotransferase. !$#cross-references MUID:82142516; PMID:6277938 !$#accession A92366 !'##molecule_type DNA !'##residues 1-44,'SL',47-49,'A',51-212,228,'SIRWALISCVTSRRAR',231-276, !1'A',278-282,'V',284-493,'S',495-505 ##label TS1 !'##cross-references GB:J01666; GB:M10318; NID:g147414; PIDN:AAA24452.1; !1PID:g147416 REFERENCE A92367 !$#authors Tso, J.Y.; Hermodson, M.A.; Zalkin, H. !$#journal J. Biol. Chem. (1982) 257:3532-3536 !$#title Glutamine phosphoribosylpyrophosphate amidotransferase from !1cloned Escherichia coli purF. NH-2-terminal amino acid !1sequence, identification of the glutamine site, and trace !1metal analysis. !$#cross-references MUID:82142517; PMID:7037784 !$#accession A92367 !'##molecule_type protein !'##residues 2-24 ##label TS2 REFERENCE S01389 !$#authors Sampei, G.I.; Mizobuchi, K. !$#journal Nucleic Acids Res. (1988) 16:8717 !$#title Nucleotide sequence of the Escherichia coli purF gene !1encoding amidophosphoribosyltransferase for de novo purine !1nucleotide synthesis. !$#cross-references MUID:88335626; PMID:3047685 !$#accession S01389 !'##molecule_type DNA !'##residues 1-385,'R',387-505 ##label SAM !'##cross-references GB:X12423; NID:g42592; PIDN:CAA30971.1; PID:g42593 REFERENCE I51823 !$#authors Zalkin, H. !$#journal Adv. Enzyme Regul. (1983) 21:225-237 !$#title Structure, function, and regulation of amidophosphoribosyl- !1transferase from prokaryotes. !$#cross-references MUID:86073632; PMID:6443594 !$#accession I51823 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-44,'SL',47-49,'A',51-212,228,'SIRWALISCVTSRRAR',231-276, !1'A',278-282,'V',284-336,'I',338-493,'S',495-505 ##label RES !'##cross-references GB:M26893; NID:g147417; PIDN:AAA24453.1; !1PID:g147418 GENETICS !$#gene purF !$#map_position 49 min FUNCTION !$#description catalyzes the formation of phosphoribosylamine and glutamate !1from 5-phosphoribosyl-1-diphosphate and glutamine !1[validated, MUID:82142517] !$#pathway purine nucleotide biosynthesis CLASSIFICATION #superfamily amidophosphoribosyltransferase KEYWORDS glycosyltransferase; pentosyltransferase; purine nucleotide !1biosynthesis FEATURE !$2-505 #product amidophosphoribosyltransferase #status !8predicted #label MAT\ !$2 #active_site Cys #status predicted SUMMARY #length 505 #molecular-weight 56487 #checksum 462 SEQUENCE /// ENTRY XQBS #type complete TITLE amidophosphoribosyltransferase (EC 2.4.2.14) purF precursor [validated] - Bacillus subtilis ALTERNATE_NAMES phosphoribosylpyrophosphate amidotransferase ORGANISM #formal_name Bacillus subtilis DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jun-2000 ACCESSIONS A00582; E69684 REFERENCE A00582 !$#authors Makaroff, C.A.; Zalkin, H.; Switzer, R.L.; Vollmer, S.J. !$#journal J. Biol. Chem. (1983) 258:10586-10593 !$#title Cloning of the Bacillus subtilis glutamine !1phosphoribosylpyrophosphate amidotransferase gene in !1Escherichia coli. Nucleotide sequence determination and !1properties of the plasmid-encoded enzyme. !$#cross-references MUID:83290989; PMID:6411717 !$#accession A00582 !'##molecule_type DNA !'##residues 1-476 ##label MAK !'##cross-references GB:J02732; GB:K00047; NID:g143363; PIDN:AAA22680.1; !1PID:g143370 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69684 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-476 ##label KUN !'##cross-references GB:Z99107; GB:AL009126; NID:g2632866; !1PIDN:CAB12469.1; PID:g2632963 !'##experimental_source strain 168 REFERENCE A52352 !$#authors Smith, J.L. !$#submission submitted to the Brookhaven Protein Data Bank, April 1994 !$#cross-references PDB:1GPH !$#contents annotation; X-ray crystallography, 3.0 angstroms, residues !112-412,'D',414-476 REFERENCE A58681 !$#authors Smith, J.L.; Zaluzec, E.J.; Wery, J.P.; Niu, L.; Switzer, !1R.L.; Zalkin, H.; Satow, Y. !$#journal Science (1994) 264:1427-1433 !$#title Structure of the allosteric regulatory enzyme of purine !1biosynthesis. !$#cross-references MUID:94255765; PMID:8197456 !$#contents annotation; X-ray crystallography, 3.0 angstroms COMMENT Although an intact 4Fe-4S cluster is required for enzyme !1activity, the cluster is not catalytic and may serve an !1oxygen sensory role. GENETICS !$#gene purF COMPLEX homodimer; also forms homotetramers FUNCTION !$#description catalyzes the formation of phosphoribosylamine and glutamate !1from 5-phosphoribosyl-1-pyrophosphate and glutamine !$#pathway purine nucleotide biosynthesis CLASSIFICATION #superfamily amidophosphoribosyltransferase KEYWORDS 4Fe-4S; glycosyltransferase; homodimer; iron-sulfur protein; !1metalloprotein; pentosyltransferase; purine nucleotide !1biosynthesis FEATURE !$1-11 #domain propeptide #status predicted #label PRO\ !$12-476 #product amidophosphoribosyltransferase #status !8predicted #label MAT\ !$12-241 #domain amino-terminal #label ATD\ !$242-476 #domain carboxyl-terminal #label CTD\ !$12 #active_site Cys #status predicted\ !$247,393,448,451 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8experimental SUMMARY #length 476 #molecular-weight 51619 #checksum 7328 SEQUENCE /// ENTRY XRBY #type complete TITLE ATP phosphoribosyltransferase (EC 2.4.2.17) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YER055c ORGANISM #formal_name Saccharomyces cerevisiae DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 10-May-2001 ACCESSIONS A00583; S50558 REFERENCE A00583 !$#authors Hinnebusch, A.G.; Fink, G.R. !$#journal J. Biol. Chem. (1983) 258:5238-5247 !$#title Repeated DNA sequences upstream from HIS1 also occur at !1several other co-regulated genes in Saccharomyces !1cerevisiae. !$#cross-references MUID:83161150; PMID:6300123 !$#accession A00583 !'##molecule_type DNA !'##residues 1-297 ##label HIN !'##cross-references EMBL:V01306; NID:g3772; PIDN:CAA24613.1; PID:g3773 REFERENCE S50427 !$#authors Dietrich, F.S. !$#submission submitted to the EMBL Data Library, December 1994 !$#description The sequence of S. cerevisiae lambda clones 6592, 4678, !14742, and 3612. !$#accession S50558 !'##molecule_type DNA !'##residues 1-297 ##label DIE !'##cross-references EMBL:U18813; NID:g1381127; PIDN:AAB64591.1; !1PID:g603291; GSPDB:GN00005; MIPS:YER055c GENETICS !$#gene SGD:HIS1; MIPS:YER055c !'##cross-references SGD:S0000857; MIPS:YER055c !$#map_position 5R CLASSIFICATION #superfamily ATP phosphoribosyltransferase; ATP !1phosphoribosyltransferase homology KEYWORDS glycosyltransferase; pentosyltransferase FEATURE !$61-183 #domain ATP phosphoribosyltransferase homology #label !8HSG SUMMARY #length 297 #molecular-weight 32266 #checksum 6814 SEQUENCE /// ENTRY XREBT #type complete TITLE ATP phosphoribosyltransferase (EC 2.4.2.17) [validated] - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 30-Nov-1980 #sequence_revision 30-Nov-1980 #text_change 26-May-2000 ACCESSIONS JS0156; A00584; A33864 REFERENCE JS0131 !$#authors Carlomagno, M.S.; Chiariotti, L.; Alifano, P.; Nappo, A.G.; !1Bruni, C.B. !$#journal J. Mol. Biol. (1988) 203:585-606 !$#title Structure and function of the Salmonella typhimurium and !1Escherichia coli K-12 histidine operons. !$#cross-references MUID:89094829; PMID:3062174 !$#accession JS0156 !'##molecule_type DNA !'##residues 1-299 ##label CAR !'##cross-references GB:X13464; NID:g47719; PIDN:CAA31822.1; PID:g47721 REFERENCE A00584 !$#authors Piszkiewicz, D.; Tilley, B.E.; Rand-Meir, T.; Parsons, S.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1979) 76:1589-1592 !$#title Amino acid sequence of ATP phosphoribosyltransferse of !1Salmonella typhimurium. !$#cross-references MUID:79201645; PMID:377278 !$#accession A00584 !'##molecule_type protein !'##residues 1-299 ##label PIS REFERENCE A33864 !$#authors Ciampi, M.S.; Alifano, P.; Nappo, A.G.; Bruni, C.B.; !1Carlomagno, M.S. !$#journal J. Bacteriol. (1989) 171:4472-4478 !$#title Features of the Rho-dependent transcription termination !1polar element within the hisG cistron of Salmonella !1typhimurium. !$#cross-references MUID:89327167; PMID:2666402 !$#accession A33864 !'##molecule_type DNA !'##residues 1-66 ##label CIA !'##cross-references GB:M28367 GENETICS !$#gene hisG !$#map_position 42 min COMPLEX homohexamer FUNCTION !$#description EC 2.4.2.17 [validated, MUID:78066719]; catalyzes the first !1step of the histidine biosynthetic pathway; it is subject to !1feedback inhibition and plays an important role in the !1regulation of histidine metabolism !$#pathway histidine biosynthesis !$#note first step of histidine biosynthesis CLASSIFICATION #superfamily ATP phosphoribosyltransferase; ATP !1phosphoribosyltransferase homology KEYWORDS glycosyltransferase; histidine biosynthesis; homohexamer; !1pentosyltransferase SUMMARY #length 299 #molecular-weight 33211 #checksum 2182 SEQUENCE /// ENTRY D64070 #type complete TITLE ATP phosphoribosyltransferase (EC 2.4.2.17) - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 17-Mar-2000 ACCESSIONS D64070 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession D64070 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-303 ##label TIGR !'##cross-references GB:U32729; GB:L42023; NID:g1573439; !1PIDN:AAC22127.1; PID:g1573446; TIGR:HI0468 !'##note named as homolog to a protein from Escherichia coli CLASSIFICATION #superfamily ATP phosphoribosyltransferase; ATP !1phosphoribosyltransferase homology KEYWORDS glycosyltransferase; histidine biosynthesis; !1pentosyltransferase SUMMARY #length 303 #molecular-weight 33821 #checksum 1755 SEQUENCE /// ENTRY XREC #type complete TITLE ATP phosphoribosyltransferase (EC 2.4.2.17) - Escherichia coli (strain K-12) ALTERNATE_NAMES phosphoribosyl-ATP pyrophosphohydrolase ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 21-Nov-1997 #text_change 01-Mar-2002 ACCESSIONS B64967; JS0131; S19176; I56436 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64967 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-299 ##label BLAT !'##cross-references GB:AE000293; GB:U00096; NID:g2367127; !1PIDN:AAC75080.1; PID:g1788330; UWGP:b2019 !'##experimental_source strain K-12, substrain MG1655 REFERENCE JS0131 !$#authors Carlomagno, M.S.; Chiariotti, L.; Alifano, P.; Nappo, A.G.; !1Bruni, C.B. !$#journal J. Mol. Biol. (1988) 203:585-606 !$#title Structure and function of the Salmonella typhimurium and !1Escherichia coli K-12 histidine operons. !$#cross-references MUID:89094829; PMID:3062174 !$#accession JS0131 !'##molecule_type DNA !'##residues 1-48,'GV',51-262,'A',264-299 ##label CAR !'##cross-references GB:X13462; NID:g41706; PIDN:CAA31811.1; PID:g41708 !'##experimental_source strain K12 REFERENCE S19176 !$#authors Jovanovic, G. !$#submission submitted to the EMBL Data Library, January 1992 !$#accession S19176 !'##molecule_type DNA !'##residues 1-43,'K',45-299 ##label JOV !'##cross-references EMBL:X63697 REFERENCE I56436 !$#authors Jovanovic, G.; Kostic, T.; Jankovic, M.; Savic, D.J. !$#journal J. Mol. Biol. (1994) 239:433-435 !$#title Nucleotide sequence of the Escherichia coli K-12 histidine !1operon revisited. !$#cross-references MUID:94260549; PMID:8201624 !$#accession I56436 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-299 ##label RES !'##cross-references EMBL:U02070; NID:g509816; PIDN:AAA19742.1; !1PID:g509817 GENETICS !$#gene hisG !$#map_position 44 min COMPLEX homohexamer FUNCTION !$#description catalyzes the synthesis of 5-phospho-D-ribose 1-diphosphate !1from 1-(5-phospho-D-ribosyl)-ATP and pyrophosphate !$#pathway histidine biosynthesis !$#note subjects to feedback inhibition and plays an important role !1in the regulation of histidine metabolism CLASSIFICATION #superfamily ATP phosphoribosyltransferase; ATP !1phosphoribosyltransferase homology KEYWORDS glycosyltransferase; histidine biosynthesis; homohexamer; !1pentosyltransferase FEATURE !$57-182 #domain ATP phosphoribosyltransferase homology #label !8HSG SUMMARY #length 299 #molecular-weight 33366 #checksum 2053 SEQUENCE /// ENTRY NPKEDC #type complete TITLE anthranilate phosphoribosyltransferase (EC 2.4.2.18) - Acinetobacter calcoaceticus ORGANISM #formal_name Acinetobacter calcoaceticus DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 11-Jun-1999 ACCESSIONS A00585 REFERENCE A93052 !$#authors Kaplan, J.B.; Goncharoff, P.; Seibold, A.M.; Nichols, B.P. !$#journal Mol. Biol. Evol. (1984) 1:456-472 !$#title Nucleotide sequence of the Acinetobacter calcoaceticus !1trpGDC gene cluster. !$#cross-references MUID:88174326; PMID:6599977 !$#accession A00585 !'##molecule_type DNA !'##residues 1-349 ##label KAP !'##cross-references GB:M36636; NID:g141799; PIDN:AAA21904.1; !1PID:g141801 COMMENT This enzyme catalyzes the formation of anthranilate by !1transferring the phosphoribosyl group from !1phosphoribosylanthranilate to pyrophosphate. In E. coli and !1certain other bacteria, it is the carboxyl-terminal !1two-thirds of component II of anthranilate synthase (EC !14.1.3.27). GENETICS !$#gene trpD CLASSIFICATION #superfamily anthranilate phosphoribosyltransferase; trpD !1homology KEYWORDS glycosyltransferase; pentosyltransferase; tryptophan !1biosynthesis FEATURE !$6-339 #domain trpD homology #label TRD SUMMARY #length 349 #molecular-weight 37556 #checksum 6969 SEQUENCE /// ENTRY C40362 #type complete TITLE anthranilate phosphoribosyltransferase (EC 2.4.2.18) trpD - Methanobacterium thermoautotrophicum (strain Marburg) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C40362 REFERENCE A40362 !$#authors Meile, L.; Stettler, R.; Banholzer, R.; Kotik, M.; !1Leisinger, T. !$#journal J. Bacteriol. (1991) 173:5017-5023 !$#title Tryptophan gene cluster of Methanobacterium !1thermoautotrophicum Marburg: molecular cloning and !1nucleotide sequence of a putative trpEGCFBAD operon. !$#cross-references MUID:91317718; PMID:1860817 !$#accession C40362 !'##status preliminary !'##molecule_type DNA !'##residues 1-350 ##label MEI !'##cross-references GB:M65060; NID:g149744; PIDN:AAA73034.1; !1PID:g149751 CLASSIFICATION #superfamily anthranilate phosphoribosyltransferase; trpD !1homology KEYWORDS glycosyltransferase; pentosyltransferase; tryptophan !1biosynthesis FEATURE !$6-346 #domain trpD homology #label TRD SUMMARY #length 350 #molecular-weight 37296 #checksum 3813 SEQUENCE /// ENTRY S35126 #type complete TITLE anthranilate phosphoribosyltransferase (EC 2.4.2.18) - Lactococcus lactis subsp. lactis ORGANISM #formal_name Lactococcus lactis subsp. lactis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S35126 REFERENCE S35123 !$#authors Bardowski, J.; Ehrlich, S.D.; Chopin, A. !$#journal J. Bacteriol. (1992) 174:6563-6570 !$#title Tryptophan biosynthesis genes in Lactococcus lactis subsp. !1lactis. !$#cross-references MUID:93015708; PMID:1400208 !$#accession S35126 !'##molecule_type DNA !'##residues 1-335 ##label BAR !'##cross-references EMBL:M87483; NID:g149514; PIDN:AAA25225.1; !1PID:g149518 GENETICS !$#gene trpD CLASSIFICATION #superfamily anthranilate phosphoribosyltransferase; trpD !1homology KEYWORDS glycosyltransferase; pentosyltransferase; tryptophan !1biosynthesis FEATURE !$4-332 #domain trpD homology #label TRD SUMMARY #length 335 #molecular-weight 35845 #checksum 7738 SEQUENCE /// ENTRY D24723 #type complete TITLE anthranilate phosphoribosyltransferase (EC 2.4.2.18) trpD - Corynebacterium glutamicum ORGANISM #formal_name Corynebacterium glutamicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS D24723 REFERENCE A93606 !$#authors Matsui, K.; Sano, K.; Ohtsubo, E. !$#journal Nucleic Acids Res. (1986) 14:10113-10114 !$#title Complete nucleotide and deduced amino acid sequences of the !1Brevibacterium lactofermentum tryptophan operon. !$#cross-references MUID:87117512; PMID:3808947 !$#accession D24723 !'##molecule_type DNA !'##residues 1-348 ##label MAT !'##cross-references GB:X04960; NID:g39591; PIDN:CAA28625.1; PID:g39595 !'##note the source is designated as Brevibacterium lactofermentum GENETICS !$#gene trpD CLASSIFICATION #superfamily anthranilate phosphoribosyltransferase; trpD !1homology KEYWORDS glycosyltransferase; pentosyltransferase; tryptophan !1biosynthesis FEATURE !$9-338 #domain trpD homology #label TRD SUMMARY #length 348 #molecular-weight 36649 #checksum 3886 SEQUENCE /// ENTRY NPBS #type complete TITLE anthranilate phosphoribosyltransferase (EC 2.4.2.18) - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 13-Aug-1986 #sequence_revision 13-Aug-1986 #text_change 21-Jul-2000 ACCESSIONS A00586; B22794; B69726 REFERENCE A91509 !$#authors Band, L.; Shimotsu, H.; Henner, D.J. !$#journal Gene (1984) 27:55-65 !$#title Nucleotide sequence of the Bacillus subtilis trpE and trpD !1genes. !$#cross-references MUID:84183611; PMID:6425119 !$#accession A00586 !'##molecule_type DNA !'##residues 1-337 ##label BAN !'##cross-references GB:K01391; NID:g143767; PIDN:AAA22866.1; !1PID:g143769 REFERENCE A91520 !$#authors Henner, D.J.; Band, L.; Shimotsu, H. !$#journal Gene (1985) 34:169-177 !$#title Nucleotide sequence of the Bacillus subtilis tryptophan !1operon. !$#cross-references MUID:85232062; PMID:3924737 !$#accession B22794 !'##molecule_type DNA !'##residues 1-337 ##label HEN !'##cross-references GB:K01391; NID:g143767; PIDN:AAA22866.1; !1PID:g143769 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69726 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-337 ##label KUN !'##cross-references GB:Z99115; GB:AL009126; NID:g2634478; !1PIDN:CAB14183.1; PID:g2634685 !'##experimental_source strain 168 GENETICS !$#gene trpD !$#map_position 205 CLASSIFICATION #superfamily anthranilate phosphoribosyltransferase; trpD !1homology KEYWORDS glycosyltransferase; pentosyltransferase; tryptophan !1biosynthesis FEATURE !$4-331 #domain trpD homology #label TRD SUMMARY #length 337 #molecular-weight 35898 #checksum 8483 SEQUENCE /// ENTRY JH0099 #type complete TITLE anthranilate phosphoribosyltransferase (EC 2.4.2.18) - Bacillus pumilus ORGANISM #formal_name Bacillus pumilus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JH0099 REFERENCE JH0098 !$#authors Rivas, M.V.; Jarvis, E.D.; Rudner, R. !$#journal Gene (1990) 87:71-78 !$#title The structure of the trpE, trpD and 5' trpC genes of !1Bacillus pumilus. !$#cross-references MUID:90236301; PMID:2110100 !$#accession JH0099 !'##molecule_type DNA !'##residues 1-340 ##label RIV !'##cross-references GB:M36468; NID:g1374669; PIDN:AAB02273.1; !1PID:g1374670 GENETICS !$#gene trpD CLASSIFICATION #superfamily anthranilate phosphoribosyltransferase; trpD !1homology KEYWORDS glycosyltransferase; pentosyltransferase; tryptophan !1biosynthesis FEATURE !$4-332 #domain trpD homology #label TRD SUMMARY #length 340 #molecular-weight 36789 #checksum 7261 SEQUENCE /// ENTRY NPBY #type complete TITLE anthranilate phosphoribosyltransferase (EC 2.4.2.18) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES phosphoribosyl-anthranilate pycophosphorylase; protein D9476.4; protein YDR354w ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 23-Mar-2001 ACCESSIONS S05865; S34287; B49455; S61151 REFERENCE S05865 !$#authors Furter, R.; Paravicini, G.; Aebi, M.; Braus, G.; Prantl, F.; !1Niederberger, P.; Huetter, R. !$#journal Nucleic Acids Res. (1986) 14:6357-6373 !$#title The TRP4 gene of Saccharomyces cerevisiae: isolation and !1structural analysis. !$#cross-references MUID:86312904; PMID:2428012 !$#accession S05865 !'##molecule_type DNA !'##residues 1-380 ##label FUR !'##cross-references EMBL:X04273; NID:g4671; PIDN:CAA27822.1; PID:g4672 REFERENCE S34287 !$#authors Kilmartin, J.V.; Dyos, S.L.; Kershaw, D.; Finch, J.T. !$#submission submitted to the EMBL Data Library, June 1993 !$#description A spacer element in the Saccharomyces cerevisiae spindle !1pole body whose transcript is cell cycle-regulated. !$#accession S34287 !'##molecule_type DNA !'##residues 202-380 ##label KIL !'##cross-references EMBL:X73297; NID:g312173; PIDN:CAA51732.1; !1PID:g312174 REFERENCE A49455 !$#authors Kilmartin, J.V.; Dyos, S.L.; Kershaw, D.; Finch, J.T. !$#journal J. Cell Biol. (1993) 123:1175-1184 !$#title A spacer protein in the Saccharomyces cerevisiae spindle !1pole body whose transcript is cell cycle-regulated. !$#cross-references MUID:94064779; PMID:7503995 !$#accession B49455 !'##molecule_type DNA !'##residues 355-380 ##label KI2 !'##cross-references EMBL:X73297 REFERENCE S61148 !$#authors Du, Z. !$#submission submitted to the EMBL Data Library, June 1995 !$#description The sequence of S. cerevisiae cosmid 9476. !$#accession S61151 !'##molecule_type DNA !'##residues 1-380 ##label DUZ !'##cross-references EMBL:U28372; NID:g849170; PIDN:AAB64790.1; !1PID:g849174; GSPDB:GN00004; MIPS:YDR354w GENETICS !$#gene SGD:TRP4; MIPS:YDR354w !'##cross-references SGD:S0002762; MIPS:YDR354w !$#map_position 4R CLASSIFICATION #superfamily anthranilate phosphoribosyltransferase; trpD !1homology KEYWORDS glycosyltransferase; pentosyltransferase; tryptophan !1biosynthesis FEATURE !$10-376 #domain trpD homology #label TRD SUMMARY #length 380 #molecular-weight 41374 #checksum 5746 SEQUENCE /// ENTRY E64121 #type complete TITLE anthranilate phosphoribosyltransferase (EC 2.4.2.18) HI1389 - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES trpD protein homolog ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS E64121 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession E64121 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-333 ##label TIGR !'##cross-references GB:U32819; GB:L42023; NID:g1574218; !1PIDN:AAC23035.1; PID:g1574223; TIGR:HI1389 CLASSIFICATION #superfamily anthranilate phosphoribosyltransferase; trpD !1homology KEYWORDS glycosyltransferase; pentosyltransferase; tryptophan !1biosynthesis FEATURE !$6-333 #domain trpD homology #label TRD SUMMARY #length 333 #molecular-weight 35625 #checksum 4849 SEQUENCE /// ENTRY A49897 #type complete TITLE anthranilate phosphoribosyltransferase (EC 2.4.2.18) - Buchnera aphidicola ORGANISM #formal_name Buchnera aphidicola DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A49897; S36426 REFERENCE A49897 !$#authors Munson, M.A.; Baumann, P. !$#journal J. Bacteriol. (1993) 175:6426-6432 !$#title Molecular cloning and nucleotide sequence of a putative !1trpDC(F)BA operon in Buchnera aphidicola (endosymbiont of !1the aphid Schizaphis graminum). !$#cross-references MUID:94012512; PMID:8407819 !$#accession A49897 !'##status preliminary !'##molecule_type DNA !'##residues 1-335 ##label MUN !'##cross-references EMBL:Z19055; NID:g396655; PIDN:CAA79498.1; !1PID:g396656 GENETICS !$#gene trpD CLASSIFICATION #superfamily anthranilate phosphoribosyltransferase; trpD !1homology KEYWORDS glycosyltransferase; pentosyltransferase; tryptophan !1biosynthesis FEATURE !$4-331 #domain trpD homology #label TRD SUMMARY #length 335 #molecular-weight 38090 #checksum 3883 SEQUENCE /// ENTRY H64679 #type complete TITLE anthranilate phosphoribosyltransferase (EC 2.4.2.18) - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS H64679 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession H64679 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-335 ##label TOM !'##cross-references GB:AE000511; TIGR:HP1280 CLASSIFICATION #superfamily anthranilate phosphoribosyltransferase; trpD !1homology KEYWORDS glycosyltransferase; pentosyltransferase; tryptophan !1biosynthesis FEATURE !$4-332 #domain trpD homology #label TRD SUMMARY #length 335 #molecular-weight 36709 #checksum 7601 SEQUENCE /// ENTRY JS0340 #type complete TITLE anthranilate phosphoribosyltransferase (EC 2.4.2.18) - Lactobacillus casei ALTERNATE_NAMES trpD protein ORGANISM #formal_name Lactobacillus casei DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S42343; JS0340 REFERENCE S42342 !$#authors Natori, Y.; Kano, Y.; Imamoto, F. !$#journal J. Biochem. (1990) 107:248-255 !$#title Nucleotide sequences and genomic constitution of five !1tryptophan genes of Lactobacillus casei. !$#cross-references MUID:90299861; PMID:2113923 !$#accession S42343 !'##status preliminary !'##molecule_type DNA !'##residues 1-341 ##label NAT !'##cross-references EMBL:D00496; NID:g216754; PIDN:BAA00383.1; !1PID:g216756 !'##experimental_source isolate RNL7 GENETICS !$#gene trpD CLASSIFICATION #superfamily anthranilate phosphoribosyltransferase; trpD !1homology KEYWORDS glycosyltransferase; pentosyltransferase; tryptophan !1biosynthesis FEATURE !$5-332 #domain trpD homology #label TRD SUMMARY #length 341 #molecular-weight 36490 #checksum 4300 SEQUENCE /// ENTRY RTECGX #type complete TITLE xanthine phosphoribosyltransferase (EC 2.4.2.22) - Escherichia coli (strain K-12) ALTERNATE_NAMES xanthine-guanine phosphoribosyltransferase ORGANISM #formal_name Escherichia coli DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 01-Mar-2002 ACCESSIONS A00587; I41070; I41254; I41253; G64748; I41255 REFERENCE A00587 !$#authors Pratt, D.; Subramani, S. !$#journal Nucleic Acids Res. (1983) 11:8817-8823 !$#title Nucleotide sequence of the Escherichia coli xanthine-guanine !1phosphoribosyl transferase gene. !$#cross-references MUID:84169518; PMID:6324103 !$#accession A00587 !'##molecule_type DNA !'##residues 1-152 ##label PRA !'##cross-references GB:X00221; GB:K01784; NID:g41606; PIDN:CAA25040.1; !1PID:g41607 REFERENCE I41070 !$#authors Richardson, K.K.; Fostel, J.; Skopek, T.R. !$#journal Nucleic Acids Res. (1983) 11:8809-8816 !$#title Nucleotide sequence of the xanthine guanine phosphoribosyl !1transferase gene of E. coli. !$#cross-references MUID:84169517; PMID:6324102 !$#accession I41070 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-152 ##label RES !'##cross-references EMBL:X00222; NID:g41608; PIDN:CAA25041.1; !1PID:g41609 REFERENCE I41254 !$#authors Jagadeeswaran, P.; Ashman, C.R.; Roberts, S.; Langenberg, J. !$#journal Gene (1984) 31:309-313 !$#title Nucleotide sequence and analysis of deletion mutants of the !1Escherichia coli gpt gene in plasmid pSV-2 gpt. !$#cross-references MUID:85128454; PMID:6396164 !$#accession I41254 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-152 ##label RE2 !'##cross-references GB:M12907; NID:g146261; PIDN:AAA23932.1; !1PID:g146262 REFERENCE I41253 !$#authors Mulligan, R.C.; Berg, P. !$#journal Mol. Cell. Biol. (1981) 1:449-459 !$#title Factors governing the expression of a bacterial gene in !1mammalian cells. !$#cross-references MUID:88094360; PMID:6100966 !$#accession I41253 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-49 ##label RE3 !'##cross-references GB:M10382; NID:g146259; PIDN:AAA23931.1; !1PID:g146260 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64748 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-152 ##label BLAT !'##cross-references GB:AE000132; GB:U00096; NID:g2367098; !1PIDN:AAC73342.1; PID:g1786433; UWGP:b0238 !'##experimental_source strain K-12, substrain MG1655 REFERENCE I41255 !$#authors Richardson, K.K.; Richardson, F.C.; Crosby, R.M.; Swenberg, !1J.A.; Skopek, T.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:344-348 !$#title DNA base changes and alkylation following in vivo exposure !1of Escherichia coli to N-methyl-N-nitrosourea or !1N-ethyl-N-nitrosourea. !$#cross-references MUID:87092406; PMID:3540961 !$#accession I41255 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-121,'G',123-152 ##label RE4 !'##cross-references GB:M15035; NID:g146263; PIDN:AAA23933.1; !1PID:g146264 GENETICS !$#gene gpt !$#map_position 6 min COMPLEX homotrimer FUNCTION !$#description catalyzes conversion of xanthine or guanine to XMP or GMP !1using phosphoribosylpyrophosphate CLASSIFICATION #superfamily xanthine phosphoribosyltransferase KEYWORDS glycosyltransferase; pentosyltransferase SUMMARY #length 152 #molecular-weight 16970 #checksum 7005 SEQUENCE /// ENTRY A29725 #type complete TITLE NAD ADP-ribosyltransferase (EC 2.4.2.30), nuclear - human ALTERNATE_NAMES poly (ADP-ribose) polymerase; poly (ADP-ribose) synthetase; poly(ADP) polymerase ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS A29725; A28498; A39976; A26901; I38096; B33321; A33321; !1A35635; A61559; S14010 REFERENCE A29725 !$#authors Uchida, K.; Morita, T.; Sato, T.; Ogura, T.; Yamashita, R.; !1Noguchi, S.; Suzuki, H.; Nyunoya, H.; Miwa, M.; Sugimura, T. !$#journal Biochem. Biophys. Res. Commun. (1987) 148:617-622 !$#title Nucleotide sequence of a full-length cDNA for human !1fibroblast poly(ADP-ribose) polymerase. !$#cross-references MUID:88076933; PMID:3120710 !$#accession A29725 !'##molecule_type mRNA !'##residues 1-69,'Q',71-1014 ##label UCH !'##cross-references GB:M18112; NID:g190166; PIDN:AAA60137.1; !1PID:g190167 REFERENCE A28498 !$#authors Kurosaki, T.; Ushiro, H.; Mitsuuchi, Y.; Suzuki, S.; !1Matsuda, M.; Matsuda, Y.; Katunuma, N.; Kangawa, K.; Matsuo, !1H.; Hirose, T.; Inayama, S.; Shizuta, Y. !$#journal J. Biol. Chem. (1987) 262:15990-15997 !$#title Primary structure of human poly (ADP-ribose) synthetase as !1deduced from cDNA sequence. !$#cross-references MUID:88058958; PMID:2824474 !$#accession A28498 !'##molecule_type mRNA !'##residues 1-16,'E',18-211,'K',213-236,'R',238-366,'H',369-1014 !1##label KUR !'##cross-references GB:J03473 REFERENCE A39976 !$#authors Cherney, B.W.; McBride, O.W.; Chen, D.; Alkhatib, H.; !1Bhatia, K.; Hensley, P.; Smulson, M.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:8370-8374 !$#title cDNA sequence, protein structure, and chromosomal location !1of the human gene for poly(ADP-ribose) polymerase. !$#cross-references MUID:88068596; PMID:2891139 !$#accession A39976 !'##molecule_type mRNA !'##residues 1-49,'D',51-612,'Q',614-907,'Y',909-939,'R',941-979,'I', !1981-1014 ##label CHE !'##cross-references GB:J03030 !'##note the authors translated the codon ATA for residue 980 as Asn REFERENCE A26901 !$#authors Suzuki, H.; Uchida, K.; Shima, H.; Sato, T.; Okamoto, T.; !1Kimura, T.; Miwa, M. !$#journal Biochem. Biophys. Res. Commun. (1987) 146:403-409 !$#title Molecular cloning of cDNA for human poly(ADP-ribose) !1polymerase and expression of its gene during HL-60 cell !1differentiation. !$#cross-references MUID:87298455; PMID:3113420 !$#accession A26901 !'##molecule_type mRNA !'##residues 441-610,'N',612-880;921-1014 ##label SUZ !'##note the sequence figure has an omission of forty residues REFERENCE I38096 !$#authors Ogura, T.; Nyunoya, H.; Takahashi-Masutani, M.; Miwa, M.; !1Sugimura, T.; Esumi, H. !$#journal Biochem. Biophys. Res. Commun. (1990) 167:701-710 !$#title Characterization of a putative promoter region of the human !1poly(ADP-ribose) polymerase gene: structural similarity to !1that of the DNA polymerase beta gene. !$#cross-references MUID:90211250; PMID:2108670 !$#accession I38096 !'##status translation not shown !'##molecule_type DNA !'##residues 1-40 ##label RES !'##cross-references EMBL:X16674; NID:g510112; PIDN:CAA34663.1; !1PID:g1017423 REFERENCE A33321 !$#authors Auer, B.; Nagl, U.; Herzog, H.; Schneider, R.; Schweiger, M. !$#journal DNA (1989) 8:575-580 !$#title Human nuclear NAD(+) ADP-ribosyltransferase(polymerizing): !1organization of the gene. !$#cross-references MUID:90091744; PMID:2513174 !$#accession B33321 !'##molecule_type DNA !'##residues !138-43;93-98;132-137;204-209;237-242;276-281;335-340;384-389; !1431-436;512-517;535-540;580-585;645-650;688-693;716-721; !1757-762;800-805;833-838;884-889;927-932;947-952;986-991 !1##label AUE !'##cross-references GB:M29544; GB:M22953 !'##note the authors translated the codon GTG for residue 54 as Glu !'##note these fragments represent intron-exon boundaries !$#accession A33321 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type DNA !'##residues 16-66;96;121-159,'D',161-167 ##label AU2 !'##note these fragments represent a zinc finger-containing DNA-binding !1region REFERENCE A35635 !$#authors Gradwohl, G.; Menissier de Murcia, J.; Molinete, M.; !1Simonin, F.; Koken, M.; Hoeijmakers, J.H.J.; de Murcia, G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:2990-2994 !$#title The second zinc-finger domain of poly(ADP-ribose) polymerase !1determines specificity for single-stranded breaks in DNA. !$#cross-references MUID:90222155; PMID:2109322 !$#accession A35635 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 12-26,'T',28-66;116-166 ##label GRA REFERENCE A61559 !$#authors Schneider, R.; Auer, B.; Kuehne, C.; Herzog, H.; Klocker, !1H.; Burtscher, H.J.; Hirsch-Kauffmann, M.; Wintersberger, !1U.; Schweiger, M. !$#journal Eur. J. Cell Biol. (1987) 44:302-307 !$#title Isolation of a cDNA clone for human NAD (+): protein !1ADP-ribosyltransferase. !$#cross-references MUID:88082900; PMID:3121332 !$#accession A61559 !'##molecule_type mRNA !'##residues 381-420;682-710 ##label SCH REFERENCE S14010 !$#authors Yokoyama, Y.; Kawamoto, T.; Mitsuuchi, Y.; Kurosaki, T.; !1Toda, K.; Ushiro, H.; Terashima, M.; Sumimoto, H.; !1Kuribayashi, I.; Yamamoto, Y.; Maeda, T.; Ikeda, H.; Sagara, !1Y.; Shizuta, Y. !$#journal Eur. J. Biochem. (1990) 194:521-526 !$#title Human poly(ADP-ribose) polymerase gene. Cloning of the !1promoter region. !$#cross-references MUID:91099327; PMID:2125269 !$#accession S14010 !'##status preliminary !'##molecule_type DNA !'##residues 1-95 ##label YOK !'##cross-references EMBL:X56140; NID:g35286; PIDN:CAA39606.1; !1PID:g825702 COMMENT This protein can ADP-ribosylate itself as well as other !1proteins. GENETICS !$#gene GDB:ADPRT; PPOL !'##cross-references GDB:119508; OMIM:173870 !$#map_position 1q41-1q42 CLASSIFICATION #superfamily NAD+ ADP-ribosyltransferase KEYWORDS DNA binding; DNA repair; glycosyltransferase; NAD; nucleus; !1pentosyltransferase; zinc finger SUMMARY #length 1014 #molecular-weight 113083 #checksum 7353 SEQUENCE /// ENTRY S04200 #type complete TITLE NAD ADP-ribosyltransferase (EC 2.4.2.30) - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S04200 REFERENCE S04200 !$#authors Huppi, K.; Bhatia, K.; Siwarski, D.; Klinman, D.; Cherney, !1B.; Smulson, M. !$#journal Nucleic Acids Res. (1989) 17:3387-3401 !$#title Sequence and organization of the mouse poly (ADP-ribose) !1polymerase gene. !$#cross-references MUID:89263780; PMID:2498841 !$#accession S04200 !'##molecule_type DNA !'##residues 1-1013 ##label HUP !'##cross-references EMBL:X14206; NID:g49893; PIDN:CAA32421.1; !1PID:g49894 GENETICS !$#map_position 1 CLASSIFICATION #superfamily NAD+ ADP-ribosyltransferase KEYWORDS DNA binding; glycosyltransferase; NAD; nucleus; !1pentosyltransferase; zinc finger SUMMARY #length 1013 #molecular-weight 113099 #checksum 5611 SEQUENCE /// ENTRY JS0428 #type complete TITLE NAD ADP-ribosyltransferase (EC 2.4.2.30) - bovine ALTERNATE_NAMES ADP-ribosyltransferase (polymerizing); poly(adenosine diphosphate ribose) polymerase; poly(ADP-ribose) polymerase ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS JS0428; S00328; A30458 REFERENCE JS0428 !$#authors Saito, I. !$#submission submitted to JIPID, February 1990 !$#accession JS0428 !'##molecule_type mRNA !'##residues 1-1016 ##label SAI !'##experimental_source thymus REFERENCE S00328 !$#authors Taniguchi, T.; Yamauchi, K.; Yamamoto, T.; Toyoshima, K.; !1Harada, N.; Tanaka, H.; Takahashi, S.; Yamamoto, H.; !1Fujimoto, S. !$#journal Eur. J. Biochem. (1988) 171:571-575 !$#title Depression in gene expression for poly(ADP-ribose) !1synthetase during the interferon-gamma-induced activation !1process of murine macrophage tumor cells. !$#cross-references MUID:88151954; PMID:2450019 !$#accession S00328 !'##molecule_type mRNA !'##residues 648-714;838-904 ##label TAN !'##cross-references EMBL:X06986 !$#accession A30458 !'##molecule_type protein !'##residues 658-685;689-696;893-901 ##label TA2 CLASSIFICATION #superfamily NAD+ ADP-ribosyltransferase KEYWORDS DNA binding; glycosyltransferase; NAD; nucleotide binding; !1nucleus; P-loop; pentosyltransferase; zinc finger FEATURE !$21-51 #region zinc finger\ !$128-165 #region zinc finger\ !$200-220 #region helix-turn-helix motif\ !$224-231 #region nuclear location signal\ !$250-270 #region helix-turn-helix motif\ !$494-501 #region nucleotide-binding motif A (P-loop)\ !$890-903 #region nucleotide binding #status predicted SUMMARY #length 1016 #molecular-weight 113486 #checksum 8204 SEQUENCE /// ENTRY JH0581 #type complete TITLE NAD ADP-ribosyltransferase (EC 2.4.2.30) - chicken ALTERNATE_NAMES poly(ADP-ribose) synthase ORGANISM #formal_name Gallus gallus #common_name chicken DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS JH0581 REFERENCE JH0581 !$#authors Ittel, M.E.; Garnier, J.M.; Jeltsch, J.M.; Niedergang, C.P. !$#journal Gene (1991) 102:157-164 !$#title Chicken poly(ADP-ribose) synthetase: complete deduced amino !1acid sequence and comparison with mammalian enzyme !1sequences. !$#cross-references MUID:91340148; PMID:1840535 !$#accession JH0581 !'##molecule_type mRNA !'##residues 1-1011 ##label ITT !'##cross-references EMBL:X52690; NID:g63742; PIDN:CAA36917.1; !1PID:g63743 COMMENT This protein is a chromatin-bound enzyme. COMMENT This enzyme catalyzes DNA-dependent post-translational !1modifications of various nuclear proteins. CLASSIFICATION #superfamily NAD+ ADP-ribosyltransferase KEYWORDS DNA binding; glycosyltransferase; NAD; nucleus; !1pentosyltransferase; zinc finger SUMMARY #length 1011 #molecular-weight 113605 #checksum 5006 SEQUENCE /// ENTRY A47474 #type complete TITLE NAD ADP-ribosyltransferase (EC 2.4.2.30) - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS A47474 REFERENCE A47474 !$#authors Uchida, K.; Hanai, S.; Ishikawa, K.; Ozawa, Y.; Uchida, M.; !1Sugimura, T.; Miwa, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:3481-3485 !$#title Cloning of cDNA encoding Drosophila poly(ADP-ribose) !1polymerase: leucine zipper in the auto-modification domain. !$#cross-references MUID:93234521; PMID:8475096 !$#accession A47474 !'##status preliminary !'##molecule_type mRNA !'##residues 1-994 ##label UCH !'##cross-references GB:D13806; GB:D13807; GB:D13808; NID:g303545; !1PIDN:BAA02964.1; PID:g303546 !'##note sequence extracted from NCBI backbone (NCBIN:129703, !1NCBIP:129704) GENETICS !$#gene FlyBase:Parp !'##cross-references FlyBase:FBgn0010247 CLASSIFICATION #superfamily NAD+ ADP-ribosyltransferase KEYWORDS DNA binding; glycosyltransferase; NAD; nucleus; !1pentosyltransferase SUMMARY #length 994 #molecular-weight 113791 #checksum 5917 SEQUENCE /// ENTRY S42208 #type complete TITLE NAD ADP-ribosyltransferase (EC 2.4.2.30) - flesh fly (Sarcophaga peregrina) ALTERNATE_NAMES poly(ADP-ribose) polymerase ORGANISM #formal_name Sarcophaga peregrina DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S42208; S71496 REFERENCE S42208 !$#authors Masutani, M.; Nozaki, T.; Hitomi, Y.; Ikejima, M.; Nagasaki, !1K.; de Prati, A.C.; Kurata, S.; Natori, S.; Sugimura, T.; !1Esumi, H. !$#journal Eur. J. Biochem. (1994) 220:607-614 !$#title Cloning and functional expression of poly(ADP-ribose) !1polymerase cDNA from Sarcophaga peregrina. !$#cross-references MUID:94170813; PMID:8125121 !$#accession S42208 !'##molecule_type mRNA !'##residues 1-996 ##label MAS !'##cross-references EMBL:D16482; NID:g473742; PIDN:BAA03943.1; !1PID:g538248 !$#accession S71496 !'##molecule_type protein !'##residues 170-188;721-736;813-819;879-885 ##label MAX CLASSIFICATION #superfamily NAD+ ADP-ribosyltransferase KEYWORDS DNA binding; glycosyltransferase; NAD; pentosyltransferase; !1zinc finger FEATURE !$1-369 #domain DNA binding #status predicted #label DNA\ !$370-507 #domain auto-modification #status predicted #label !8AMO\ !$508-996 #domain NAD binding #status predicted #label NAD SUMMARY #length 996 #molecular-weight 113018 #checksum 1061 SEQUENCE /// ENTRY DOCGPO #type complete TITLE NAD-diphthamide ADP-ribosyltransferase (EC 2.4.2.36) precursor - corynephage omega CONTAINS diphtheria toxin fragment A; diphtheria toxin fragment B ORGANISM #formal_name corynephage omega DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 03-Jun-2002 ACCESSIONS A00728; A60137; A31356; A33131; A35880 REFERENCE A00728 !$#authors Ratti, G.; Rappuoli, R.; Giannini, G. !$#journal Nucleic Acids Res. (1983) 11:6589-6595 !$#title The complete nucleotide sequence of the gene coding for !1diphtheria toxin in the corynephage omega (tox+) genome. !$#cross-references MUID:84041471; PMID:6314249 !$#accession A00728 !'##molecule_type DNA !'##residues 1-560 ##label RAT !'##cross-references GB:M19546; EMBL:V01536; NID:g166116; !1PIDN:AAA32181.1; PID:g166117 REFERENCE A60137 !$#authors Falmagne, P.; Capiau, C.; Lambotte, P.; Zanen, J.; Cabiaux, !1V.; Ruysschaert, J.M. !$#journal Biochim. Biophys. Acta (1985) 827:45-50 !$#title The complete amino acid sequence of diphtheria toxin !1fragment B. Correlation with its lipid-binding properties. !$#cross-references MUID:85097828; PMID:3967029 !$#accession A60137 !'##molecule_type protein !'##residues 219-325,'V',327-413,'N',415-560 ##label FAL REFERENCE A31356 !$#authors Cieplak, W.; Hasemann, C.; Eidels, L. !$#journal Biochem. Biophys. Res. Commun. (1988) 157:747-754 !$#title Specific cleavage of diphtheria toxin by human urokinase. !$#cross-references MUID:89076312; PMID:3144277 !$#accession A31356 !'##molecule_type protein !'##residues 219-225,'X',227,'M',229-230 ##label CIE REFERENCE A33131 !$#authors Palmiter, R.D.; Behringer, R.R.; Quaife, C.J.; Maxwell, F.; !1Maxwell, I.H.; Brinster, R.L. !$#journal Cell (1987) 50:435-443 !$#title Cell lineage ablation in transgenic mice by cell-specific !1expression of a toxin gene. !$#cross-references MUID:87273505; PMID:3649277 !$#contents annotation !$#note the authors demonstrate a technique of ablating select !1lineages of cells by transgenic expression of a construct !1containing fragment A under control of an enhancer and !1promoter specific for that cell lineage !$#note the sequence shown for this construct has been revised COMMENT Diphtheria toxin, produced by a bacteriophage infecting !1Corynebacterium diphtheriae, catalyzes the covalent !1attachment of ADP-ribose from NAD to the diphthamide residue !1of eukaryotic translation elongation factor 2, blocking !1protein synthesis. One molecule is sufficient to cause cell !1death. COMMENT Fragment B binds to the receptor protein and is responsible !1for the movement of fragment A across the cell membrane. !1After a trypsin-like cleavage and reduction, intracellular !1fragment A becomes catalytically active. GENETICS !$#start_codon GTG CLASSIFICATION #superfamily diphtheria toxin KEYWORDS glycosyltransferase; NAD; pentosyltransferase; toxin FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-560 #product diphtheria toxin #status experimental #label !8MAT\ !$26-218 #product NAD+-diphthamide ADP-ribosyltransferase !8(diphtheria toxin fragment A) #status experimental !8#label FRA\ !$26-218 #domain catalytic #status experimental #label CAT\ !$219-560 #product diphtheria toxin fragment B #status !8experimental #label FRB\ !$230-403 #domain membrane insertion #status predicted #label !8MIN\ !$411-560 #domain receptor binding #status predicted #label !8RBD\ !$46,90 #binding_site NAD (His, Tyr) #status predicted\ !$173 #active_site Glu #status predicted\ !$211-226,486-496 #disulfide_bonds #status predicted SUMMARY #length 560 #molecular-weight 60814 #checksum 485 SEQUENCE /// ENTRY DOCGA #type complete TITLE NAD-diphthamide ADP-ribosyltransferase (EC 2.4.2.36) precursor - corynephage beta CONTAINS diphtheria toxin fragment A; diphtheria toxin fragment B ORGANISM #formal_name corynephage beta DATE 24-Apr-1984 #sequence_revision 10-Feb-1995 #text_change 03-Jun-2002 ACCESSIONS A05128; A00729; A00730 REFERENCE A05128 !$#authors Greenfield, L.; Bjorn, M.J.; Horn, G.; Fong, D.; Buck, G.A.; !1Collier, R.J.; Kaplan, D.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:6853-6857 !$#title Nucleotide sequence of the structural gene for diphtheria !1toxin carried by corynebacteriophage beta. !$#cross-references MUID:84070728; PMID:6316330 !$#accession A05128 !'##molecule_type DNA !'##residues 1-560 ##label GRE !'##cross-references GB:K01722; NID:g166118; PIDN:AAA32182.1; !1PID:g166119 REFERENCE A92256 !$#authors DeLange, R.J.; Williams, L.C.; Drazin, R.E.; Collier, R.J. !$#journal J. Biol. Chem. (1979) 254:5838-5842 !$#title The amino acid sequence of fragment A, an enzymically active !1fragment of diphtheria toxin. III. The chymotryptic !1peptides, the peptides derived by cleavage at tryptophan !1residues, and the complete sequence of the protein. !$#cross-references MUID:79194138; PMID:221484 !$#accession A00729 !'##molecule_type protein !'##residues 26-170,'VES',174-218 ##label DEL !'##note this is the final paper in a series of three !'##note this protein is found in three forms, terminating with residue !1215-Arg, 217-Arg, or 218-Arg; all three forms have !1approximately equal enzymatic activity REFERENCE A00730 !$#authors Kaczorek, M.; Delpeyroux, F.; Chenciner, N.; Streeck, R.E.; !1Murphy, J.R.; Boquet, P.; Tiollais, P. !$#journal Science (1983) 221:855-858 !$#title Nucleotide sequence and expression of the diphtheria tox228 !1gene in Escherichia coli. !$#cross-references MUID:83275723; PMID:6348945 !$#accession A00730 !'##molecule_type DNA !'##residues 1-103,'D',105-186,'K',188-221,'G',223-402,'S',404-455,'S', !1457-560 ##label KAC !'##cross-references GB:K01723 !'##note a nontoxic diphtheria toxin homolog, produced by corynephage !1beta after N-methyl-N'-nitro-N-nitrosoguanidine mutagenesis !'##note either of the first two mutations completely abolishes !1ADP-ribosylating activity of fragment A; the last two may !1reduce receptor binding REFERENCE A90616 !$#authors Michel, A.; Dirkx, J. !$#journal Biochim. Biophys. Acta (1977) 491:286-295 !$#title Occurrence of tryptophan in the enzymically active site of !1diphtheria toxin fragment A. !$#cross-references MUID:77134904; PMID:849463 !$#contents annotation; active site !$#note modification of Trp-153 inactivates the enzyme; this residue !1may be concerned with catalysis or with substrate binding REFERENCE A44679 !$#authors Choe, S.; Bennett, M.J.; Fujii, G.; Curmi, P.M.G.; !1Kantardjieff, K.A.; Collier, R.J.; Eisenberg, D. !$#journal Nature (1992) 357:216-222 !$#title The crystal structure of diphtheria toxin. !$#cross-references MUID:92269934; PMID:1589020 !$#contents annotation; X-ray crystallography, 2.0 angstroms COMMENT Diphtheria toxin, produced by a bacteriophage infecting !1Corynebacterium diphtheriae, catalyzes the covalent !1attachment of ADP-ribose from NAD to the diphthamide residue !1of eukaryotic translation elongation factor 2, blocking !1protein synthesis. One molecule is sufficient to cause cell !1death. COMMENT Fragment B binds to the receptor protein and is responsible !1for the movement of fragment A across the cell membrane. !1After a trypsin-like cleavage and reduction, intracellular !1fragment A becomes catalytically active. GENETICS !$#start_codon GTG CLASSIFICATION #superfamily diphtheria toxin KEYWORDS glycosyltransferase; NAD; pentosyltransferase; toxin FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-560 #product diphtheria toxin #status predicted #label !8MAT\ !$26-218 #product NAD+-diphthamide ADP-ribosyltransferase !8(diphtheria toxin fragment A) #status experimental !8#label FRA\ !$26-218 #domain catalytic #status experimental #label CAT\ !$219-560 #product diphtheria toxin fragment B #status !8predicted #label FRB\ !$230-403 #domain membrane insertion #status predicted #label !8MIN\ !$411-560 #domain receptor binding #status predicted #label !8RBD\ !$46,90 #binding_site NAD (His, Tyr) #status predicted\ !$173 #active_site Glu #status predicted\ !$211-226,486-496 #disulfide_bonds #status experimental SUMMARY #length 560 #molecular-weight 60814 #checksum 485 SEQUENCE /// ENTRY SXBPT4 #type complete TITLE NAD+-protein ADP-ribosyltransferase (EC 2.4.2.-) precursor - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 07-Jun-1996 ACCESSIONS JU0096 REFERENCE JU0096 !$#authors Hilse, D.; Koch, T.; Rueger, W. !$#journal Nucleic Acids Res. (1989) 17:6731 !$#title Nucleotide sequence of the alt gene of bacteriophage T4. !$#cross-references MUID:89386005; PMID:2506526 !$#accession JU0096 !'##status translation not shown !'##molecule_type DNA !'##residues 1-685 ##label HIL COMMENT This enzyme catalyzes the ADP-ribosylation of one of the two !1alpha-subunits of the bacterial RNA polymerase. GENETICS !$#gene alt CLASSIFICATION #superfamily phage T4 NAD-protein ADP-ribosyltransferase KEYWORDS glycosyltransferase; pentosyltransferase FEATURE !$7-685 #product NAD-protein ADP-ribosyltransferase #status !8predicted #label MAT SUMMARY #length 685 #molecular-weight 76784 #checksum 9835 SEQUENCE /// ENTRY S31714 #type complete TITLE NAD+-protein ADP-ribosyltransferase (EC 2.4.2.-) precursor - phage T6 ORGANISM #formal_name phage T6 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 23-Mar-2001 ACCESSIONS S31714 REFERENCE S31630 !$#authors Koch, T.; Rueger, W. !$#submission submitted to the EMBL Data Library, December 1992 !$#description The ADP-ribosyltransferase of bacteriophages T2, T4 and T6: !1Sequencing of the genes and comparision of their products. !$#accession S31714 !'##status preliminary !'##molecule_type DNA !'##residues 1-698 ##label KOC !'##cross-references EMBL:X69894; NID:g15422; PIDN:CAA49518.1; !1PID:g15423 CLASSIFICATION #superfamily phage T4 NAD-protein ADP-ribosyltransferase KEYWORDS glycosyltransferase; NAD; pentosyltransferase SUMMARY #length 698 #molecular-weight 77947 #checksum 3528 SEQUENCE /// ENTRY S31630 #type complete TITLE NAD+-protein ADP-ribosyltransferase (EC 2.4.2.-) precursor - phage T2 ORGANISM #formal_name phage T2 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-May-2001 ACCESSIONS S31630 REFERENCE S31630 !$#authors Koch, T.; Rueger, W. !$#submission submitted to the EMBL Data Library, December 1992 !$#description The ADP-ribosyltransferase of bacteriophages T2, T4 and T6: !1Sequencing of the genes and comparision of their products. !$#accession S31630 !'##status preliminary !'##molecule_type DNA !'##residues 1-698 ##label KOC !'##cross-references EMBL:X69893; NID:g15187; PIDN:CAA49517.1; !1PID:g15188 CLASSIFICATION #superfamily phage T4 NAD-protein ADP-ribosyltransferase KEYWORDS glycosyltransferase; NAD; pentosyltransferase SUMMARY #length 698 #molecular-weight 77996 #checksum 2927 SEQUENCE /// ENTRY C69651 #type complete TITLE prolipoprotein diacylglyceryl transferase (EC 2.4.99.-) lgt - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS C69651 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69651 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-269 ##label KUN !'##cross-references GB:Z99121; GB:AL009126; NID:g2635827; !1PIDN:CAB15504.1; PID:g2636012 !'##experimental_source strain 168 GENETICS !$#gene lgt CLASSIFICATION #superfamily prolipoprotein diacylglyceryl transferase KEYWORDS glycosyltransferase SUMMARY #length 269 #molecular-weight 30619 #checksum 6759 SEQUENCE /// ENTRY S74710 #type complete TITLE prolipoprotein diacylglyceryl transferase (EC 2.4.99.-) - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein sll1187 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S74710 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74710 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-283 ##label KAN !'##cross-references EMBL:D90901; GB:AB001339; NID:g1651897; !1PIDN:BAA16861.1; PID:g1651935 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene lgt CLASSIFICATION #superfamily prolipoprotein diacylglyceryl transferase KEYWORDS glycosyltransferase SUMMARY #length 283 #molecular-weight 32107 #checksum 2147 SEQUENCE /// ENTRY C64639 #type complete TITLE prolipoprotein diacylglyceryl transferase (EC 2.4.99.-) - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C64639 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession C64639 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-284 ##label TOM !'##cross-references GB:AE000604; GB:AE000511; NID:g2314086; !1PIDN:AAD07998.1; PID:g2314092; TIGR:HP0955 CLASSIFICATION #superfamily prolipoprotein diacylglyceryl transferase KEYWORDS glycosyltransferase SUMMARY #length 284 #molecular-weight 32643 #checksum 9904 SEQUENCE /// ENTRY E64209 #type complete TITLE prolipoprotein diacylglyceryl transferase homolog - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 07-Dec-1999 ACCESSIONS E64209 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession E64209 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-382 ##label TIGR !'##cross-references GB:U39688; GB:L43967; NID:g1045753; PID:g1045763; !1TIGR:MG086 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily Mycoplasma prolipoprotein diacylglyceryl !1transferase homolog SUMMARY #length 382 #molecular-weight 44431 #checksum 8286 SEQUENCE /// ENTRY S73933 #type complete TITLE prolipoprotein diacylglyceryl transferase lgt - Mycoplasma pneumoniae (strain ATCC 29342) ALTERNATE_NAMES hypothetical protein G07_orf389b ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 10-Dec-1999 ACCESSIONS S73933 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73933 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-389 ##label HIM !'##cross-references EMBL:AE000058; GB:U00089; NID:g1674291; !1PIDN:AAB96255.1; PID:g1674309 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#gene lgt !$#genetic_code SGC3 CLASSIFICATION #superfamily Mycoplasma prolipoprotein diacylglyceryl !1transferase homolog SUMMARY #length 389 #molecular-weight 44596 #checksum 904 SEQUENCE /// ENTRY XQECHH #type complete TITLE imidazole glycerol phosphate synthase (EC 2.4.2.-) chain hisH - Escherichia coli (strain K-12) ALTERNATE_NAMES amidotransferase ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 01-Mar-2002 ACCESSIONS JS0132; F64967 REFERENCE JS0131 !$#authors Carlomagno, M.S.; Chiariotti, L.; Alifano, P.; Nappo, A.G.; !1Bruni, C.B. !$#journal J. Mol. Biol. (1988) 203:585-606 !$#title Structure and function of the Salmonella typhimurium and !1Escherichia coli K-12 histidine operons. !$#cross-references MUID:89094829; PMID:3062174 !$#accession JS0132 !'##molecule_type DNA !'##residues 1-196 ##label CAR !'##cross-references GB:X13462; NID:g41706; PIDN:CAA31815.1; PID:g41712 !'##experimental_source strain K12 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64967 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-196 ##label BLAT !'##cross-references GB:AE000293; GB:U00096; NID:g2367127; !1PIDN:AAC75084.1; PID:g1788334; UWGP:b2023 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene hisH !$#map_position 44 min FUNCTION !$#description protein catalyzes an amidotransferase reaction that !1generates imidazole-glycerol phosphate !$#pathway histidine biosynthesis !$#note hisH and hisF gene products form a dimer that constitutes !1imidazole glycerol phosphate synthase (IPG) FUNCTION atr !$#description protein catalyzes an amidotransferase reaction that !1generates 5-aminoimidazol-4-carboxamide ribonucleotide !$#pathway purine biosynthesis CLASSIFICATION #superfamily amidotransferase hisH; trpG homology KEYWORDS glycosyltransferase; histidine biosynthesis; !1pentosyltransferase FEATURE !$3-194 #domain trpG homology #label TRG SUMMARY #length 196 #molecular-weight 21653 #checksum 9783 SEQUENCE /// ENTRY XQEBHT #type complete TITLE amidotransferase hisH (EC 2.4.2.-) - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 21-Jan-2000 ACCESSIONS JS0160 REFERENCE JS0131 !$#authors Carlomagno, M.S.; Chiariotti, L.; Alifano, P.; Nappo, A.G.; !1Bruni, C.B. !$#journal J. Mol. Biol. (1988) 203:585-606 !$#title Structure and function of the Salmonella typhimurium and !1Escherichia coli K-12 histidine operons. !$#cross-references MUID:89094829; PMID:3062174 !$#accession JS0160 !'##molecule_type DNA !'##residues 1-194 ##label CAR !'##cross-references GB:X13464; NID:g47719; PIDN:CAA31826.1; PID:g47725 COMMENT This protein is involved in the histidine biosynthetic !1pathway and catalyzes an amidotransferase reaction that !1generates imidazole-glycerol phosphate and !15-aminoimidazol-4-carboxamide ribonucleotide, which is used !1for purine synthesis. GENETICS !$#gene hisH !$#map_position 42 min CLASSIFICATION #superfamily amidotransferase hisH; trpG homology KEYWORDS glycosyltransferase; histidine biosynthesis; !1pentosyltransferase FEATURE !$3-192 #domain trpG homology #label TRG SUMMARY #length 194 #molecular-weight 21522 #checksum 5424 SEQUENCE /// ENTRY G64070 #type complete TITLE imidazoleglycerol-phosphate synthase (EC 2.4.2.-) hisH - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS G64070 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession G64070 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-199 ##label TIGR !'##cross-references GB:U32730; GB:L42023; NID:g3212191; !1PIDN:AAC22131.1; PID:g1573451; TIGR:HI0472 !'##note named as homolog to a protein from Escherichia coli CLASSIFICATION #superfamily amidotransferase hisH; trpG homology KEYWORDS glycosyltransferase; histidine biosynthesis; !1pentosyltransferase FEATURE !$4-194 #domain trpG homology #label TRG SUMMARY #length 199 #molecular-weight 22048 #checksum 8157 SEQUENCE /// ENTRY PE0007 #type complete TITLE imidazoleglycerol-phosphate synthase (EC 2.4.2.-) - Azospirillum brasilense ORGANISM #formal_name Azospirillum brasilense DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S16799; PE0007; S04400 REFERENCE S16798 !$#authors Fani, R. !$#submission submitted to the EMBL Data Library, August 1991 !$#accession S16799 !'##molecule_type DNA !'##residues 1-192 ##label FAN !'##cross-references EMBL:X61207; NID:g38669; PIDN:CAA43516.1; !1PID:g38671 REFERENCE JE0045 !$#authors Fani, R.; Bazzicalupo, M.; Damiani, G.; Bianchi, A.; !1Schipani, C.; Sgaramella, V.; Polsinelli, M. !$#journal Mol. Gen. Genet. (1989) 216:224-229 !$#title Cloning of histidine genes of Azospirillum brasilense: !1organization of the ABFH gene cluster and nucleotide !1sequence of the hisB gene. !$#cross-references MUID:89313660; PMID:2664449 !$#accession PE0007 !'##molecule_type DNA !'##residues 1-70 ##label FA2 !'##cross-references GB:X17435; NID:g38666; PIDN:CAA35479.1; PID:g38668 GENETICS !$#gene hisH CLASSIFICATION #superfamily amidotransferase hisH; trpG homology KEYWORDS glycosyltransferase; hexosyltransferase; histidine !1biosynthesis; pentosyltransferase SUMMARY #length 192 #molecular-weight 20826 #checksum 1888 SEQUENCE /// ENTRY A35726 #type complete TITLE farnesyl-pyrophosphate synthetase - human ALTERNATE_NAMES prenyltransferase and farnesyl-diphosphate synthase CONTAINS dimethylallyltranstransferase (EC 2.5.1.1); geranyltranstransferase (EC 2.5.1.10) ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 11-Jun-1999 ACCESSIONS A35726; A33415 REFERENCE A35726 !$#authors Wilkin, D.J.; Kutsunai, S.Y.; Edwards, P.A. !$#journal J. Biol. Chem. (1990) 265:4607-4614 !$#title Isolation and sequence of the human farnesyl pyrophosphate !1synthetase cDNA. Coordinate regulation of the mRNAs for !1farnesyl pyrophosphate synthetase, !13-hydroxy-3-methylglutaryl coenzyme A reductase, and !13-hydroxy-3-methylglutaryl coenzyme A synthase by phorbol !1ester. !$#cross-references MUID:90170972; PMID:1968462 !$#accession A35726 !'##molecule_type mRNA !'##residues 1-353 ##label WIL !'##cross-references GB:J05262; NID:g182398; PIDN:AAA52423.1; !1PID:g182399 REFERENCE A33415 !$#authors Sheares, B.T.; White, S.S.; Molowa, D.T.; Chan, K.; Ding, !1V.D.H.; Kroon, P.A.; Bostedor, R.G.; Karkas, J.D. !$#journal Biochemistry (1989) 28:8129-8135 !$#title Cloning, analysis, and bacterial expression of human !1farnesyl pyrophosphate synthetase and its regulation in Hep !1G2 cells. !$#cross-references MUID:90105318; PMID:2690933 !$#accession A33415 !'##molecule_type mRNA !'##residues 8-115,'I',117-353 ##label SHE !'##cross-references GB:M29863; NID:g182404; PIDN:AAA35820.1; !1PID:g182405 GENETICS !$#gene GDB:FDPS !'##cross-references GDB:128629; OMIM:134629 !$#map_position 4q21-4q25 FUNCTION !$#description catalyzes the condensation of isopentenyl diphosphate with !1dimethylallyl diphosphate forming geranyl diphosphate and !1pyrophosphate; catalyzes the condensation of isopentenyl !1diphosphate with geranyl diphosphate forming farnesyl !1diphosphate and pyrophosphate !$#pathway steroidogenesis; lipoprotein synthesis CLASSIFICATION #superfamily farnesyl-pyrophosphate synthetase KEYWORDS cholesterol biosynthesis; homodimer; transferase SUMMARY #length 353 #molecular-weight 40520 #checksum 7314 SEQUENCE /// ENTRY B34713 #type complete TITLE farnesyl-pyrophosphate synthetase, hepatic - rat ALTERNATE_NAMES 39K cholesterol-repressible enzyme; CR39 protein; prenyltransferase and farnesyl-diphosphate synthase CONTAINS dimethylallyltranstransferase (EC 2.5.1.1); geranyltranstransferase (EC 2.5.1.10) ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 21-May-1995 ACCESSIONS B34713; A27772 REFERENCE A34713 !$#authors Teruya, J.H.; Kutsunai, S.Y.; Spear, D.H.; Edwards, P.A.; !1Clarke, C.F. !$#journal Mol. Cell. Biol. (1990) 10:2315-2326 !$#title Testis-specific transcription initiation sites of rat !1farnesyl pyrophosphate synthetase mRNA. !$#cross-references MUID:90220617; PMID:2325654 !$#accession B34713 !'##molecule_type mRNA !'##residues 1-353 ##label TER !'##cross-references GB:M34477 REFERENCE A27772 !$#authors Clarke, C.F.; Tanaka, R.D.; Svenson, K.; Wamsley, M.; !1Fogelman, A.M.; Edwards, P.A. !$#journal Mol. Cell. Biol. (1987) 7:3138-3146 !$#title Molecular cloning and sequence of a cholesterol-repressible !1enzyme related to prenyltransferase in the isoprene !1biosynthetic pathway. !$#cross-references MUID:88038866; PMID:3670308 !$#accession A27772 !'##molecule_type mRNA !'##residues 1-344 ##label CLA !'##cross-references GB:M34477 !'##note this sequence has since been revised FUNCTION !$#description catalyzes the condensation of isopentenyl diphosphate with !1dimethylallyl diphosphate forming geranyl diphosphate and !1pyrophosphate; catalyzes the condensation of isopentenyl !1diphosphate with geranyl diphosphate forming farnesyl !1diphosphate and pyrophosphate !$#pathway steroidogenesis; lipoprotein synthesis CLASSIFICATION #superfamily farnesyl-pyrophosphate synthetase KEYWORDS cholesterol biosynthesis; homodimer; transferase SUMMARY #length 353 #molecular-weight 40829 #checksum 2006 SEQUENCE /// ENTRY A34713 #type complete TITLE farnesyl-pyrophosphate synthetase, testis - rat ALTERNATE_NAMES 39K cholesterol-repressible enzyme; CR39 protein; prenyltransferase and farnesyl-diphosphate synthase CONTAINS dimethylallyltranstransferase (EC 2.5.1.1); geranyltranstransferase (EC 2.5.1.10) ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 11-Jun-1999 ACCESSIONS A34713 REFERENCE A34713 !$#authors Teruya, J.H.; Kutsunai, S.Y.; Spear, D.H.; Edwards, P.A.; !1Clarke, C.F. !$#journal Mol. Cell. Biol. (1990) 10:2315-2326 !$#title Testis-specific transcription initiation sites of rat !1farnesyl pyrophosphate synthetase mRNA. !$#cross-references MUID:90220617; PMID:2325654 !$#accession A34713 !'##molecule_type mRNA !'##residues 1-353 ##label TER !'##cross-references GB:M34477; NID:g204091; PIDN:AAA41143.1; !1PID:g204092 FUNCTION !$#description catalyzes the condensation of isopentenyl diphosphate with !1dimethylallyl diphosphate forming geranyl diphosphate and !1pyrophosphate; catalyzes the condensation of isopentenyl !1diphosphate with geranyl diphosphate forming farnesyl !1diphosphate and pyrophosphate !$#pathway steroidogenesis; lipoprotein synthesis CLASSIFICATION #superfamily farnesyl-pyrophosphate synthetase KEYWORDS cholesterol biosynthesis; homodimer; testis; transferase SUMMARY #length 353 #molecular-weight 40803 #checksum 1105 SEQUENCE /// ENTRY A34441 #type complete TITLE farnesyl-pyrophosphate synthetase - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES prenyltransferase and farnesyl-diphosphate synthase; protein J0525; protein YJL167w CONTAINS dimethylallyltranstransferase (EC 2.5.1.1); geranyltranstransferase (EC 2.5.1.10) ORGANISM #formal_name Saccharomyces cerevisiae DATE 03-Feb-1994 #sequence_revision 03-Feb-1994 #text_change 21-Jul-2000 ACCESSIONS A34441; S05861; S56950 REFERENCE A34441 !$#authors Anderson, M.S.; Yarger, J.G.; Burck, C.L.; Poulter, C.D. !$#journal J. Biol. Chem. (1989) 264:19176-19184 !$#title Farnesyl diphosphate synthetase. Molecular cloning, !1sequence, and expression of an essential gene from !1Saccharomyces cerevisiae. !$#cross-references MUID:90037051; PMID:2681213 !$#accession A34441 !'##molecule_type DNA !'##residues 1-352 ##label AND !'##cross-references GB:J05091; NID:g171516; PIDN:AAA34606.1; !1PID:g171517 REFERENCE S05860 !$#authors Maarse, A.C.; Grivell, L.A. !$#journal Eur. J. Biochem. (1987) 165:419-425 !$#title Nucleotide sequence of the gene encoding the 11-kDa subunit !1of the ubiquinol--cytochrome-c oxidoreductase in !1Saccharomyces cerevisiae. !$#cross-references MUID:87246620; PMID:3036507 !$#accession S05861 !'##molecule_type DNA !'##residues 131-352 ##label MAA !'##cross-references EMBL:X05550; NID:g312353; PIDN:CAA29064.1; !1PID:g4725 REFERENCE S56937 !$#authors Obermaier, B.; Piravandi, E.; Rinke, M.; Domdey, H. !$#submission submitted to the Protein Sequence Database, September 1995 !$#accession S56950 !'##molecule_type DNA !'##residues 1-352 ##label OBE !'##cross-references EMBL:Z49442; NID:g1008357; PIDN:CAA89462.1; !1PID:g1008358; GSPDB:GN00010; MIPS:YJL167w GENETICS !$#gene SGD:ERG20; FPP1; MIPS:YJL167w !'##cross-references SGD:S0003703; MIPS:YJL167w !$#map_position 10L FUNCTION !$#description catalyzes condensation of isopentenyl diphosphate with !1dimethylallyl diphosphate forming geranyl diphosphate and !1pyrophosphate; catalyzes condensation of isopentenyl !1diphosphate with geranyl diphosphate forming farnesyl !1diphosphate and pyrophosphate; transferase !$#pathway cholesterol biosynthesis; isoprenoid biosynthesis !$#note first reaction specified by dimethylallyltranstransferase !1(EC 2.5.1.1); second reaction specified by !1geranyltranstransferase (EC 2.5.1.10) CLASSIFICATION #superfamily farnesyl-pyrophosphate synthetase KEYWORDS cholesterol biosynthesis; cytosol; dimer; isoprenoid !1biosynthesis; multifunctional enzyme; transferase FEATURE !$100-104 #region DDXXD motif\ !$240-244 #region DDXXD motif SUMMARY #length 352 #molecular-weight 40483 #checksum 3096 SEQUENCE /// ENTRY T40301 #type complete TITLE farnesyl pyrophosphate synthetase [similarity] - fission yeast (Schizosaccharomyces pombe) ORGANISM #formal_name Schizosaccharomyces pombe DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS T40301 REFERENCE Z21919 !$#authors Lyne, M.; Wood, V.; Rajandream, M.A.; Barrell, B.G.; !1Hilbert, H.; Moestl, D.; Duesterhoeft, A. !$#submission submitted to the EMBL Data Library, May 1998 !$#accession T40301 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-351 ##label LYN !'##cross-references EMBL:AL023589; PIDN:CAA19054.1; GSPDB:GN00067; !1SPDB:SPBC36.06c !'##experimental_source strain 972h(-); cosmid c36 GENETICS !$#gene SPDB:SPBC36.06c !$#map_position 2 !$#introns 45/3; 91/3; 158/3 CLASSIFICATION #superfamily farnesyl-pyrophosphate synthetase SUMMARY #length 351 #molecular-weight 40946 #checksum 4031 SEQUENCE /// ENTRY S27363 #type complete TITLE methionine adenosyltransferase (EC 2.5.1.6) 1 - human ALTERNATE_NAMES hepatic methionine adenosyltransferase; S-adenosylmethionine synthetase 1 ORGANISM #formal_name Homo sapiens #common_name man DATE 22-Nov-1993 #sequence_revision 10-Nov-1995 #text_change 16-Jun-2000 ACCESSIONS S27363; S35056; S30561 REFERENCE S27363 !$#authors Horikawa, S.; Tsukada, K. !$#journal Biochem. Int. (1991) 25:81-90 !$#title Molecular cloning and nucleotide sequence of cDNA encoding !1the human liver S-adenosylmethionine synthetase. !$#cross-references MUID:92126072; PMID:1772450 !$#accession S27363 !'##molecule_type mRNA !'##residues 1-395 ##label HOR !'##cross-references GB:D49357; EMBL:D11332; NID:g676878; !1PIDN:BAA08355.1; PID:g220066 REFERENCE S35056 !$#authors Alvarez, L.; Corrales, F.; Martin-Duce, A.; Mato, J.M. !$#journal Biochem. J. (1993) 293:481-486 !$#title Characterization of a full-length cDNA encoding human liver !1S-adenosylmethionine synthetase: tissue-specific gene !1expression and mRNA levels in hepatopathies. !$#cross-references MUID:93343881; PMID:8393662 !$#accession S35056 !'##molecule_type mRNA !'##residues 1-271,'GG',274-395 ##label ALV !'##cross-references EMBL:X69078; NID:g36328; PIDN:CAA48822.1; !1PID:g36329 GENETICS !$#gene GDB:MAT1A; MAT; SAMS; MATA1; SAMS1 !'##cross-references GDB:129077; OMIM:250850 !$#map_position 10q22-10q22 !$#note defects in this gene may result in hypermethioninemia FUNCTION !$#description catalyzes the formation of S-adenosyl methionine with !1phosphate and pyrophosphate from methionine, ATP and one !1molecule of water !$#pathway one-carbon metabolism CLASSIFICATION #superfamily methionine adenosyltransferase KEYWORDS ATP; liver; magnesium; metalloprotein; one-carbon !1metabolism; P-loop; S-adenosylmethionine; transferase FEATURE !$279-286 #region nucleotide-binding motif A (P-loop) #status !8atypical\ !$31 #binding_site magnesium 2 (Asp) #status predicted\ !$285,289 #active_site Lys #status predicted\ !$291 #binding_site magnesium 1 (Asp) #status predicted SUMMARY #length 395 #molecular-weight 43676 #checksum 501 SEQUENCE /// ENTRY S27257 #type complete TITLE methionine adenosyltransferase (EC 2.5.1.6) 2 alpha chain - human ALTERNATE_NAMES renal methionine adenosyltransferase (MAT); S-adenosylmethionine synthetase 2 (SAMS2) ORGANISM #formal_name Homo sapiens #common_name man DATE 22-Nov-1993 #sequence_revision 10-Nov-1995 #text_change 11-Jun-1999 ACCESSIONS S27257 REFERENCE S27257 !$#authors Horikawa, S.; Tsukada, K. !$#journal FEBS Lett. (1992) 312:37-41 !$#title Molecular cloning and developmental expression of a human !1kidney S-adenosylmethionine synthetase. !$#cross-references MUID:93050159; PMID:1426236 !$#accession S27257 !'##status preliminary !'##molecule_type mRNA !'##residues 1-395 ##label HOR !'##cross-references EMBL:X68836; GB:S47859; NID:g36326; !1PIDN:CAA48726.1; PID:g36327 GENETICS !$#gene GDB:MAT2A; SAMS2; MATA2 !'##cross-references GDB:136213; OMIM:601468 !$#map_position 2p11.2-2p11.2 !$#introns 15/2; 256/3 COMPLEX heterodimer of catalytic alpha and regulatory beta chains FUNCTION !$#description catalyzes the formation of S-adenosyl methionine with !1phosphate and pyrophosphate from methionine, ATP and one !1molecule of water !$#pathway one-carbon metabolism CLASSIFICATION #superfamily methionine adenosyltransferase KEYWORDS ATP; heterodimer; kidney; magnesium; metalloprotein; !1one-carbon metabolism; P-loop; S-adenosylmethionine; !1transferase FEATURE !$279-286 #region nucleotide-binding motif A (P-loop) #status !8atypical\ !$31 #binding_site magnesium 2 (Asp) #status predicted\ !$285,289 #active_site Lys #status predicted\ !$291 #binding_site magnesium 1 (Asp) #status predicted SUMMARY #length 395 #molecular-weight 43660 #checksum 9205 SEQUENCE /// ENTRY SYECSM #type complete TITLE methionine adenosyltransferase (EC 2.5.1.6) [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES S-adenosylmethionine synthetase ORGANISM #formal_name Escherichia coli DATE 17-Mar-1987 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS E65079; A00590 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65079 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-384 ##label BLAT !'##cross-references GB:AE000377; GB:U00096; NID:g2367178; !1PIDN:AAC75979.1; PID:g1789311; UWGP:b2942 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A00590 !$#authors Markham, G.D.; DeParasis, J.; Gatmaitan, J. !$#journal J. Biol. Chem. (1984) 259:14505-14507 !$#title The sequence of metK, the structural gene for !1S-adenosylmethionine synthetase in Escherichia coli. !$#cross-references MUID:85054924; PMID:6094561 !$#accession A00590 !'##molecule_type DNA !'##residues 1-49,'IGFSWRRNHHQRP',62-122,'DVSATQLMKPTC',134-158,'R','V', !1162-171,'S',173-251,'T',253-304,'L',306-336,338,'I',340-384 !1##label MAR !'##cross-references GB:K02129; NID:g146838; PIDN:AAA24164.1; !1PID:g146839 REFERENCE A65643 !$#authors Fu, Z.; Markham, G.D.; Takusagawa, F. !$#submission submitted to the Brookhaven Protein Data Bank, February 1996 !$#cross-references PDB:1FUG !$#contents annotation; X-ray crystallography, 3.2 angstroms, residues !12-384 REFERENCE A66184 !$#authors Takusagawa, F.; Kamitori, S.; Markham, G.D. !$#submission submitted to the Brookhaven Protein Data Bank, January 1996 !$#cross-references PDB:1MXA !$#contents annotation; X-ray crystallography, 2.8 angstroms, residues !12-384 REFERENCE A66950 !$#authors Takusagawa, F.; Kamitori, S.; Misaki, S.; Markham, G.D. !$#submission submitted to the Brookhaven Protein Data Bank, October 1995 !$#cross-references PDB:1XRA !$#contents annotation; X-ray crystallography, 3.0 angstroms, residues !12-384 REFERENCE A58829 !$#authors Takusagawa, F.; Kamitori, S.; Markham, G.D. !$#journal Biochemistry (1996) 35:2586-2596 !$#title Structure and function of S-adenosylmethionine synthetase: !1crystal structures of S-adenosylmethionine synthetase with !1ADP, BrADP, and PP-i at 2.8 Angstroms resolution. !$#cross-references MUID:96180683; PMID:8611562 !$#contents annotation; X-ray crystallography, 2.8 angstroms GENETICS !$#gene metK !$#map_position 64 min COMPLEX homotetramer FUNCTION !$#description catalyzes the formation of S-adenosyl methionine with !1phosphate and pyrophosphate from methionine, ATP and one !1molecule of water !$#pathway one-carbon metabolism CLASSIFICATION #superfamily methionine adenosyltransferase KEYWORDS ATP; homotetramer; magnesium; metalloprotein; one-carbon !1metabolism; P-loop; S-adenosylmethionine; transferase FEATURE !$2-384 #product methionine adenosyltransferase #status !8experimental #label MAT\ !$260-267 #region nucleotide-binding motif A (P-loop) #status !8atypical\ !$17 #binding_site magnesium 2 (Asp) #status predicted\ !$266,270 #active_site Lys #status predicted\ !$272 #binding_site magnesium 1 (Asp) #status predicted SUMMARY #length 384 #molecular-weight 41951 #checksum 867 SEQUENCE /// ENTRY A35711 #type complete TITLE riboflavin synthase (EC 2.5.1.9) alpha chain - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 28-Sep-1990 #sequence_revision 06-Feb-1995 #text_change 16-Jun-2000 ACCESSIONS S45544; A35711; C69692 REFERENCE S45533 !$#authors Sorokin, A.; Zumstein, E.; Azevedo, V.; Ehrlich, S.D.; !1Serror, P. !$#submission submitted to the EMBL Data Library, November 1993 !$#accession S45544 !'##molecule_type DNA !'##residues 1-215 ##label SOR !'##cross-references EMBL:L09228; NID:g410114; PIDN:AAA67482.1; !1PID:g410126 REFERENCE A35711 !$#authors Schott, K.; Kellermann, J.; Lottspeich, F.; Bacher, A. !$#journal J. Biol. Chem. (1990) 265:4204-4209 !$#title Riboflavin synthases of Bacillus subtilis. Purification and !1amino acid sequence of the alpha subunit. !$#cross-references MUID:90170913; PMID:2106516 !$#accession A35711 !'##molecule_type protein !'##residues 1-202 ##label SCH REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69692 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-215 ##label KUN !'##cross-references GB:Z99116; GB:AL009126; NID:g2634723; !1PIDN:CAB14259.1; PID:g2634762 !'##experimental_source strain 168 COMMENT The light enzyme is a homotrimer of this alpha chain. The !1heavy enzyme is a homotrimer of the alpha chain enclosed in !1an icosahedral structure of sixty beta chains. GENETICS !$#gene ribB CLASSIFICATION #superfamily riboflavin synthase alpha chain KEYWORDS duplication; homotrimer; riboflavin biosynthesis; !1transferase FEATURE !$1-96 #domain riboflavin synthase alpha chain repeat #label !8RSA1\ !$97-195 #domain riboflavin synthase alpha chain repeat #label !8RSA2 SUMMARY #length 215 #molecular-weight 23481 #checksum 565 SEQUENCE /// ENTRY SYECOG #type complete TITLE dihydropteroate synthase (EC 2.5.1.15) - Enterobacteriaceae plasmid pDGO100 and others ALTERNATE_NAMES sulfonamide resistance protein ORGANISM #formal_name Enterobacteriaceae DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jun-2000 ACCESSIONS A60174; S04811; C41857; C49790; S21847; S04691; I83521; !1S07657; S08080 REFERENCE A60174 !$#authors Hall, R.M.; Stokes, H.W. !$#journal Plasmid (1990) 23:76-79 !$#title The structure of a partial duplication in the integron of !1plasmid pDGO100. !$#cross-references MUID:90272804; PMID:2349283 !$#accession A60174 !'##molecule_type DNA !'##residues 1-279 ##label HA2 !'##cross-references EMBL:X15369; NID:g42556; PIDN:CAA33427.1; !1PID:g42557 !'##genetics CH1 !'##note sequence encoded by plasmid pDGO100; this plasmid contains two !1copies of the sulI gene REFERENCE S04809 !$#authors Sundstroem, L.; Radstroem, P.; Swedberg, G.; Skoeld, O. !$#journal Mol. Gen. Genet. (1988) 213:191-201 !$#title Site-specific recombination promotes linkage between !1trimethoprim- and sulfonamide resistance genes. Sequence !1characterization of dhfrV and sulI and a recombination !1active locus of Tn21. !$#cross-references MUID:89039710; PMID:3054482 !$#accession S04811 !'##molecule_type DNA !'##residues 1-279 ##label SUN1 !'##cross-references EMBL:X12869; NID:g45795; PIDN:CAA31360.1; !1PID:g45797 !'##genetics CH2 !'##note sequence encoded by plasmid R388 REFERENCE A41857 !$#authors Parent, R.; Roy, P.H. !$#journal J. Bacteriol. (1992) 174:2891-2897 !$#title The chloramphenicol acetyltransferase gene of Tn2424: a new !1breed of cat. !$#cross-references MUID:92234946; PMID:1314803 !$#accession C41857 !'##molecule_type DNA !'##residues 1-279 ##label PAR1 !'##cross-references GB:AF047479; GB:M80188; NID:g3088616; !1PIDN:AAC14739.1; PID:g3088629 !'##genetics CH3 !'##note sequence extracted from NCBI backbone (NCBIN:97182, !1NCBIP:97195) !'##note sequence encoded by transposon Tn2424 from IncFII plasmid NR79 REFERENCE A49790 !$#authors Parsons, Y.; Hall, R.M.; Stokes, H.W. !$#journal Antimicrob. Agents Chemother. (1991) 35:2436-2439 !$#title A new trimethoprim resistance gene, dhfrX, in the In7 !1integron of plasmid pDGO100. !$#cross-references MUID:92206862; PMID:1804022 !$#accession C49790 !'##status preliminary !'##molecule_type DNA !'##residues 1-120 ##label PAR2 !'##cross-references GB:M69220 !'##experimental_source plasmid pDGO100 !'##genetics CH1 REFERENCE S21844 !$#authors Sundstroem, L.; Swedberg, G.; Skold, O. !$#submission submitted to the EMBL Data Library, March 1991 !$#description Characterization of the transposon Tn5086, and its !1site-specifically inserted gene dhfrVII, which encodes a new !1type of trimethoprim-resistant dihydrofolate reductase. !$#accession S21847 !'##status preliminary !'##molecule_type DNA !'##residues 1-120 ##label SUN2 !'##cross-references EMBL:X58425; NID:g43090; PIDN:CAA41328.1; !1PID:g43094 !'##experimental_source transposon Tn5086, plasmid pLM027 !'##genetics CH4 REFERENCE S04691 !$#authors Guerineau, F.; Mullineaux, P. !$#journal Nucleic Acids Res. (1989) 17:4370 !$#title Nucleotide sequence of the sulfonamide resistance gene from !1plasmid R46. !$#cross-references MUID:89296482; PMID:2662140 !$#accession S04691 !'##status translation not shown !'##molecule_type DNA !'##residues 1-258,'I',260-279 ##label GUE !'##cross-references EMBL:X15024; NID:g42646; PIDN:CAA33123.1; !1PID:g42647 !'##experimental_source plasmid R46 !'##genetics CH5 REFERENCE I60356 !$#authors Radstrom, P.; Skold, O.; Swedberg, G.; Flensburg, J.; Roy, !1P.H.; Sundstrom, L. !$#journal J. Bacteriol. (1994) 176:3257-3268 !$#title Transposon Tn5090 of plasmid R751, which carries an !1integron, is related to Tn7, Mu, and the retroelements. !$#cross-references MUID:94252994; PMID:8195081 !$#accession I83521 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-120 ##label RES !'##cross-references EMBL:X58425; NID:g43090; PIDN:CAA41328.1; !1PID:g43094 !'##experimental_source plasmid pLM027 !'##genetics CH4 REFERENCE S07654 !$#authors Stokes, H.W.; Hall, R.M. !$#journal Mol. Microbiol. (1989) 3:1669-1683 !$#title A novel family of potentially mobile DNA elements encoding !1site-specific gene-integration functions: integrons. !$#cross-references MUID:90158115; PMID:2560119 !$#accession S07657 !'##molecule_type DNA !'##residues 1-279 ##label STO !'##cross-references EMBL:X15370; NID:g47843; PIDN:CAA33429.1 !'##experimental_source plasmid R46 !'##genetics CH5 GENETICS CH1 !$#gene dhfrX !$#genome plasmid pDGO100 GENETICS CH2 !$#gene sulI !$#genome plasmid R388 GENETICS CH3 !$#gene sulI; dhfrX !$#genome plasmid NR79 GENETICS CH4 !$#gene sulI !$#genome plasmid pLM027 GENETICS CH5 !$#gene sulI !$#map_position 46.9-48.8 !$#genome plasmid R46 CLASSIFICATION #superfamily dihydropteroate synthase; dihydropteroate !1synthase homology KEYWORDS antibiotic resistance; folate biosynthesis; transferase FEATURE !$4-248 #domain dihydropteroate synthase homology #label DPH SUMMARY #length 279 #molecular-weight 30126 #checksum 1602 SEQUENCE /// ENTRY C42646 #type complete TITLE dihydropteroate synthase (EC 2.5.1.15) Sul1 - Pseudomonas aeruginosa ALTERNATE_NAMES sulfonamide resistance protein ORGANISM #formal_name Pseudomonas aeruginosa DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Sep-2000 ACCESSIONS C42646 REFERENCE A42646 !$#authors Bissonnette, L.; Roy, P.H. !$#journal J. Bacteriol. (1992) 174:1248-1257 !$#title Characterization of In0 of Pseudomonas aeruginosa plasmid !1pVS1, an ancestor of integrons of multiresistance plasmids !1and transposons of gram-negative bacteria. !$#cross-references MUID:92138617; PMID:1310501 !$#accession C42646 !'##status preliminary !'##molecule_type DNA !'##residues 1-279 ##label BIS !'##cross-references GB:M73819; NID:g151299; PIDN:AAA25859.1; !1PID:g151302 !'##experimental_source plasmid pVS1 !'##note sequence extracted from NCBI backbone (NCBIN:79394, !1NCBIP:79401) CLASSIFICATION #superfamily dihydropteroate synthase; dihydropteroate !1synthase homology KEYWORDS antibiotic resistance; folate biosynthesis; transferase FEATURE !$4-248 #domain dihydropteroate synthase homology #label DHS SUMMARY #length 279 #molecular-weight 30126 #checksum 1602 SEQUENCE /// ENTRY A34950 #type complete TITLE dihydropteroate synthase (EC 2.5.1.15) II, sulfonamide resistant - Escherichia coli plasmid RSF1010 ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Sep-2000 ACCESSIONS A34950 REFERENCE A34950 !$#authors Radstroem, P.; Swedberg, G. !$#journal Antimicrob. Agents Chemother. (1988) 32:1684-1692 !$#title RSF1010 and a conjugative plasmid contain sulII, one of two !1known genes for plasmid-borne sulfonamide resistance !1dihydropteroate synthase. !$#cross-references MUID:89301592; PMID:3075438 !$#accession A34950 !'##molecule_type DNA !'##residues 1-271 ##label RAD !'##cross-references GB:M36657; NID:g148735; PIDN:AAA24936.1; !1PID:g148736 GENETICS !$#gene sulII !$#genome plasmid CLASSIFICATION #superfamily dihydropteroate synthase; dihydropteroate !1synthase homology KEYWORDS antibiotic resistance; folate biosynthesis; transferase FEATURE !$7-249 #domain dihydropteroate synthase homology #label DHS SUMMARY #length 271 #molecular-weight 28469 #checksum 2904 SEQUENCE /// ENTRY A56649 #type complete TITLE dihydropteroate synthase (EC 2.5.1.15) - Pasteurella haemolytica plasmid pYFC1 ORGANISM #formal_name Pasteurella haemolytica DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Sep-2000 ACCESSIONS A56649 REFERENCE A56649 !$#authors Chang, Y.F.; Ma, D.P.; Bai, H.Q.; Young, R.; Struck, D.K.; !1Shin, S.J.; Lein, D.H. !$#journal DNA Seq. (1992) 3:89-97 !$#title Characterization of plasmids with antimicrobial resistant !1genes in Pasteurella haemolytica A1. !$#cross-references MUID:93091250; PMID:1333838 !$#accession A56649 !'##status preliminary !'##molecule_type DNA !'##residues 1-283 ##label CHA !'##cross-references GB:M83717; NID:g150499; PIDN:AAA68897.1; !1PID:g150500 !'##experimental_source A1 strain, R plasmid pYFC1 !'##note sequence extracted from NCBI backbone (NCBIN:120094, !1NCBIP:120095) GENETICS !$#gene sulII !$#genome plasmid CLASSIFICATION #superfamily dihydropteroate synthase; dihydropteroate !1synthase homology KEYWORDS antibiotic resistance; folate biosynthesis; transferase FEATURE !$7-249 #domain dihydropteroate synthase homology #label DHS SUMMARY #length 283 #molecular-weight 29807 #checksum 9312 SEQUENCE /// ENTRY A43326 #type complete TITLE dihydropteroate synthase (EC 2.5.1.15) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Mar-1994 #sequence_revision 05-Jan-1996 #text_change 01-Mar-2002 ACCESSIONS A43326; B41380; I41216; I41046; S29705; C65108; I41214; !1S29704 REFERENCE A43326 !$#authors Dallas, W.S.; Gowen, J.E.; Ray, P.H.; Cox, M.J.; Dev, I.K. !$#journal J. Bacteriol. (1992) 174:5961-5970 !$#title Cloning, sequencing, and enhanced expression of the !1dihydropteroate synthase gene of Escherichia coli MC4100. !$#cross-references MUID:92394900; PMID:1522070 !$#accession A43326 !'##molecule_type DNA !'##residues 1-282 ##label DAL !'##cross-references GB:L06494; NID:g146014; PIDN:AAA23804.1; !1PID:g146015 !'##experimental_source strain MC4100 !'##note sequence extracted from NCBI backbone (NCBIN:113043, !1NCBIP:113044) REFERENCE A41380 !$#authors Talarico, T.L.; Dev, I.K.; Dallas, W.S.; Ferone, R.; Ray, !1P.H. !$#journal J. Bacteriol. (1991) 173:7029-7032 !$#title Purification and partial characterization of 7, !18-dihydro-6-hydroxymethylpterin-pyrophosphokinase and 7, !18-dihydropteroate synthase from Escherichia coli MC4100. !$#cross-references MUID:92041593; PMID:1657875 !$#accession B41380 !'##status preliminary !'##molecule_type protein !'##residues 1-5,'E',7-28 ##label TAL REFERENCE I41215 !$#authors Dallas, W.S.; Dev, I.K.; Ray, P.H. !$#journal J. Bacteriol. (1993) 175:7743-7744 !$#title The dihydropteroate synthase gene, folP, is near the leucine !1tRNA gene, leuU, on the Escherichia coli chromosome. !$#cross-references MUID:94064577; PMID:8244950 !$#accession I41216 !'##status preliminary !'##molecule_type DNA !'##residues 1-282 ##label RES !'##cross-references GB:L12968; NID:g290442; PIDN:AAA16123.1; !1PID:g290444 REFERENCE I41046 !$#authors Swedberg, G.; Fermer, C.; Skold, O. !$#journal Adv. Exp. Med. Biol. (1993) 338:555-558 !$#title Point mutations in the dihydropteroate synthase gene causing !1sulfonamide resistance. !$#cross-references MUID:94136300; PMID:8304179 !$#accession I41046 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-282 ##label RE2 !'##cross-references EMBL:X68776; NID:g41272; PIDN:CAA48676.1; !1PID:g41273 !'##experimental_source strain c-167 REFERENCE S29704 !$#authors Swedberg, G.; Radstrom, P.; Soderstrom, J.; Fermer, C. !$#submission submitted to the EMBL Data Library, September 1992 !$#accession S29705 !'##molecule_type DNA !'##residues 1-27,'I',29-282 ##label SWE2 !'##cross-references EMBL:X68777; NID:g41274; PIDN:CAA48677.1; !1PID:g41275 !'##note strain c-167ts20 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65108 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 'MLRGFFLSIHTRDNI',1-282 ##label BLAT !'##cross-references GB:AE000398; GB:U00096; NID:g1789562; !1PIDN:AAC76209.1; PID:g1789567; UWGP:b3177 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene folP; dhpS CLASSIFICATION #superfamily dihydropteroate synthase; dihydropteroate !1synthase homology KEYWORDS antibiotic resistance; folate biosynthesis; transferase FEATURE !$17-257 #domain dihydropteroate synthase homology #label DHS SUMMARY #length 282 #molecular-weight 30615 #checksum 2457 SEQUENCE /// ENTRY E64117 #type complete TITLE dihydropteroate synthase (EC 2.5.1.15) - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Sep-2000 ACCESSIONS E64117; A64125 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession E64117 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-275 ##label TIG1 !'##cross-references GB:U32813; GB:L42023; NID:g1574796; !1PIDN:AAC22983.1; PID:g1574797; TIGR:HI1336 !'##note named as homolog to a protein from Escherichia coli !$#accession A64125 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-275 ##label TIG2 !'##cross-references GB:U32824; GB:L42023; NID:g1574298; !1PIDN:AAC23111.1; PID:g1574304; TIGR:HI1464 GENETICS !$#note two copies of this gene are found in the Haemophilus !1influenzae chromosome CLASSIFICATION #superfamily dihydropteroate synthase; dihydropteroate !1synthase homology KEYWORDS antibiotic resistance; folate biosynthesis; transferase FEATURE !$17-257 #domain dihydropteroate synthase homology #label DHS SUMMARY #length 275 #molecular-weight 30330 #checksum 8026 SEQUENCE /// ENTRY A57423 #type complete TITLE dihydropteroate synthase (EC 2.5.1.15) - Neisseria meningitidis ORGANISM #formal_name Neisseria meningitidis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Sep-2000 ACCESSIONS A57423; S25609; S65834; S55373 REFERENCE A57423 !$#authors Fermer, C.; Kristiansen, B.E.; Skold, O.; Swedberg, G. !$#journal J. Bacteriol. (1995) 177:4669-4675 !$#title Sulfonamide resistance in Neisseria meningitidis as defined !1by site-directed mutagenesis could have its origin in other !1species. !$#cross-references MUID:95370144; PMID:7642493 !$#accession A57423 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-283 ##label RES !'##cross-references EMBL:X87405; NID:g854350; PIDN:CAA60855.1; !1PID:g854351 !'##experimental_source strain 3976 REFERENCE S25607 !$#authors Radstrom, P.; Fermer, C.; Kristiansen, B.E.; Jenkins, A.; !1Skold, O.; Swedberg, G. !$#submission submitted to the EMBL Data Library, August 1992 !$#description Transformational exchanges in the dihydropteroate synthase !1gene of Neisseria meningitidis, a novel mechanism for the !1acquisition of sulfonamide resistance. !$#accession S25609 !'##molecule_type DNA !'##residues 146-283 ##label RAD !'##cross-references EMBL:X68064; NID:g45025; PIDN:CAA48201.1; !1PID:g45026 !'##experimental_source strain BT227 REFERENCE S65832 !$#authors Radstroem, P.; Fermer, C.; Kristiansen, B.E.; Jenkins, A.; !1Skoeld, O.; Swedberg, G. !$#journal J. Bacteriol. (1992) 174:6386-6393 !$#title Transformational exchanges in the dihydropteroate synthase !1gene of Neisseria meningitidis: a novel mechanism for !1acquisition of sulfonamide resistance. !$#cross-references MUID:93015687; PMID:1400191 !$#accession S65834 !'##status preliminary !'##molecule_type DNA !'##residues 146-283 ##label RA2 !'##cross-references EMBL:X68064; NID:g45025; PIDN:CAA48201.1; !1PID:g45026 GENETICS !$#gene dhps CLASSIFICATION #superfamily dihydropteroate synthase; dihydropteroate !1synthase homology KEYWORDS antibiotic resistance; folate biosynthesis; transferase FEATURE !$20-264 #domain dihydropteroate synthase homology #label DHS SUMMARY #length 283 #molecular-weight 29956 #checksum 4365 SEQUENCE /// ENTRY G69719 #type complete TITLE dihydropteroate synthase (EC 2.5.1.15) - Bacillus subtilis ALTERNATE_NAMES dihydropteroate pyrophosphorylase ORGANISM #formal_name Bacillus subtilis DATE 05-Dec-1997 #sequence_revision 02-Jul-1998 #text_change 16-Jun-2000 ACCESSIONS G69719; S66107; D37854 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69719 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-285 ##label KUN !'##cross-references GB:Z99104; GB:AL009126; NID:g2632267; !1PIDN:CAB11853.1; PID:g2632344 !'##experimental_source strain 168 REFERENCE S65967 !$#authors Ogasawara, N.; Nakai, S.; Yoshikawa, H. !$#journal DNA Res. (1994) 1:1-14 !$#title Systematic sequencing of the 180 kilobase region of the !1Bacillus subtilis chromosome containing the replication !1origin. !$#cross-references MUID:96051385; PMID:7584024 !$#accession S66107 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-285 ##label OGA !'##cross-references EMBL:D26185; NID:g467326; PIDN:BAA05312.1; !1PID:g467466 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1993 REFERENCE A37854 !$#authors Slock, J.; Stahly, D.P.; Han, C.Y.; Six, E.W.; Crawford, !1I.P. !$#journal J. Bacteriol. (1990) 172:7211-7226 !$#title An apparent Bacillus subtilis folic acid biosynthetic operon !1containing pab, an amphibolic trpG gene, a third gene !1required for synthesis of para-aminobenzoic acid, and the !1dihydropteroate synthase gene. !$#cross-references MUID:91072277; PMID:2123867 !$#accession D37854 !'##molecule_type DNA !'##residues 1-194,'P',196-285 ##label SLO !'##cross-references GB:M34053; NID:g143406; PIDN:AAA22697.1; !1PID:g143410 GENETICS !$#gene sul FUNCTION !$#description catalyzes the formation of dihydropteroate and pyrophosphate !1from 4-aminobenzoate and !12-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine !1diphosphate !$#pathway folate biosynthesis CLASSIFICATION #superfamily dihydropteroate synthase; dihydropteroate !1synthase homology KEYWORDS antibiotic resistance; folate biosynthesis; transferase FEATURE !$27-261 #domain dihydropteroate synthase homology #label DHS SUMMARY #length 285 #molecular-weight 31001 #checksum 5216 SEQUENCE /// ENTRY A43661 #type complete TITLE dihydropteroate synthase (EC 2.5.1.15) - Streptococcus pneumoniae ORGANISM #formal_name Streptococcus pneumoniae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Sep-2000 ACCESSIONS A43661 REFERENCE A43661 !$#authors Lopez, P.; Espinosa, M.; Greenberg, B.; Lacks, S.A. !$#journal J. Bacteriol. (1987) 169:4320-4326 !$#title Sulfonamide resistance in Streptococcus pneumoniae: DNA !1sequence of the gene encoding dihydropteroate synthase and !1characterization of the enzyme. !$#cross-references MUID:87308021; PMID:3114239 !$#accession A43661 !'##status preliminary !'##molecule_type DNA !'##residues 1-316 ##label LOP !'##cross-references GB:U16156; GB:M17362; NID:g2276393; !1PIDN:AAB63944.1; PID:g564017 CLASSIFICATION #superfamily dihydropteroate synthase; dihydropteroate !1synthase homology KEYWORDS antibiotic resistance; folate biosynthesis; transferase FEATURE !$12-286 #domain dihydropteroate synthase homology #label DHS SUMMARY #length 316 #molecular-weight 34660 #checksum 4202 SEQUENCE /// ENTRY A71494 #type complete TITLE 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase (EC 2.7.6.3) - Chlamydia trachomatis (serotype D, strain UW3/Cx) CONTAINS 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase (EC 2.7.6.3); dihydropteroate synthase (EC 2.5.1.15) ORGANISM #formal_name Chlamydia trachomatis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS A71494 REFERENCE A71570 !$#authors Stephens, R.S.; Kalman, S.; Lammel, C.J.; Fan, J.; Marathe, !1R.; Aravind, L.; Mitchell, W.P.; Olinger, L.; Tatusov, R.L.; !1Zhao, Q.; Koonin, E.V.; Davis, R.W. !$#journal Science (1998) 282:754-759 !$#title Genome sequence of an obligate intracellular pathogen of !1humans: Chlamydia trachomatis. !$#cross-references MUID:99000809; PMID:9784136 !$#accession A71494 !'##status preliminary !'##molecule_type DNA !'##residues 1-450 ##label ARN !'##cross-references GB:AE001331; GB:AE001273; NID:g3329046; !1PIDN:AAC68216.1; PID:g3329058 !'##experimental_source serotype D, strain UW-3/Cx GENETICS !$#gene folP CLASSIFICATION #superfamily Chlamydia bifunctional folic acid synthesis !1protein; 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine !1pyrophosphokinase homology; dihydropteroate synthase !1homology KEYWORDS diphosphotransferase; folate biosynthesis FEATURE !$9-147 #domain !82-amino-4-hydroxy-6-hydroxymethyldihydropteridine !8pyrophosphokinase homology #label AHP\ !$182-431 #domain dihydropteroate synthase homology #label DHS SUMMARY #length 450 #molecular-weight 50312 #checksum 3784 SEQUENCE /// ENTRY G72039 #type complete TITLE 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase (EC 2.7.6.3) - Chlamydophila pneumoniae (strsain CWL029 and AR39) CONTAINS 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase (EC 2.7.6.3); dihydropteroate synthase (EC 2.5.1.15) ORGANISM #formal_name Chlamydophila pneumoniae, Chlamydia pneumoniae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS G72039; C81502 REFERENCE A72000 !$#authors Kalman, S.; Mitchell, W.; Marathe, R.; Lammel, C.; Fan, J.; !1Olinger, L.; Grimwood, J.; Davis, R.W.; Stephens, R.S. !$#journal Nature Genet. (1999) 21:385-389 !$#title Comparative genomes of Clamydia pneumoniae and C. !1trachomatis. !$#cross-references MUID:99206606; PMID:10192388 !$#accession G72039 !'##molecule_type DNA !'##residues 1-450 ##label ARN !'##cross-references GB:AE001657; GB:AE001363; NID:g4377057; !1PIDN:AAD18896.1; PID:g4377065 !'##experimental_source strain CWL029 REFERENCE A81500 !$#authors Read, T.D.; Brunham, R.C.; Shen, C.; Gill, S.R.; Heidelberg, !1J.F.; White, O.; Hickey, E.K.; Peterson, J.; Utterback, T.; !1Berry, K.; Bass, S.; Linher, K.; Weidman, J.; Khouri, H.; !1Craven, B.; Bowman, C.; Dodson, R.; Gwinn, M.; Nelson, W.; !1DeBoy, R.; Kolonay, J.; McClarty, G.; Salzberg, S.L.; Eisen, !1J.; Fraser, C.M. !$#journal Nucleic Acids Res. (2000) 28:1397-1406 !$#title Genome sequences of Chlamydia trachomatis MoPn and Chlamydia !1pneumoniae AR39. !$#cross-references MUID:20150255; PMID:10684935 !$#accession C81502 !'##molecule_type DNA !'##residues 1-450 ##label REA !'##cross-references GB:AE002267; GB:AE002161; NID:g7190018; !1PIDN:AAF38881.1; PID:g7190026; GSPDB:GN00122; TIGR:CP1114 !'##experimental_source strain AR39, HL cells GENETICS !$#gene folP; CP1114 CLASSIFICATION #superfamily Chlamydia bifunctional folic acid synthesis !1protein; 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine !1pyrophosphokinase homology; dihydropteroate synthase !1homology KEYWORDS diphosphotransferase; folate biosynthesis FEATURE !$9-148 #domain !82-amino-4-hydroxy-6-hydroxymethyldihydropteridine !8pyrophosphokinase homology #label AHP\ !$183-430 #domain dihydropteroate synthase homology #label DHS SUMMARY #length 450 #molecular-weight 49815 #checksum 9667 SEQUENCE /// ENTRY T06595 #type complete TITLE 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase (EC 2.7.6.3) - garden pea CONTAINS 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase (EC 2.7.6.3); dihydropteroate synthase (EC 2.5.1.15) ORGANISM #formal_name Pisum sativum #common_name garden pea DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS T06595 REFERENCE Z15785 !$#authors Rebeille, F.; Macherel, D.; Mouillon, J.M.; Garin, J.; !1Douce, R. !$#journal EMBO J. (1997) 16:947-957 !$#title Folate biosynthesis in higher plants: purification and !1molecular cloning of a bifunctional 6-hydroxymethyl-7, !18-dihydropterin pyrophosphokinase/7, 8-dihydropteroate !1synthase localized in mitochondria. !$#cross-references MUID:97224122; PMID:9118956 !$#accession T06595 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-515 ##label REB !'##cross-references EMBL:Y08611; NID:g1934971; PIDN:CAA69903.1; !1PID:g1934972 !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing FUNCTION HPPK !$#description EC 2.7.6.3 [validated, MUID:97224122] !$#pathway folate biosynthesis FUNCTION DHFS !$#description EC 2.5.1.15 [validated, MUID:97224122] !$#pathway folate biosynthesis !$#note cofactor Mg(2+) CLASSIFICATION #superfamily Chlamydia bifunctional folic acid synthesis !1protein; 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine !1pyrophosphokinase homology; dihydropteroate synthase !1homology KEYWORDS diphosphotransferase; folate biosynthesis; mitochondrion FEATURE !$1-28 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$29-515 #product bifunctional folic acid synthesis protein !8#status experimental #label MAT\ !$48-179 #domain !82-amino-4-hydroxy-6-hydroxymethyldihydropteridine !8pyrophosphokinase homology #label AHP\ !$232-488 #domain dihydropteroate synthase homology #label DHS SUMMARY #length 515 #molecular-weight 56454 #checksum 7943 SEQUENCE /// ENTRY C71844 #type complete TITLE dihydropteroate synthase (EC 2.5.1.15) [similarity] - Helicobacter pylori (strain J99) ORGANISM #formal_name Helicobacter pylori #variety strain J99 DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 01-Sep-2000 ACCESSIONS C71844 REFERENCE A71800 !$#authors Alm, R.A.; Ling, L.S.L.; Moir, D.T.; King, B.L.; Brown, !1E.D.; Doig, P.C.; Smith, D.R.; Noonan, B.; Guild, B.C.; !1deJonge, B.L.; Carmel, G.; Tummino, P.J.; Caruso, A.; !1Uria-Nickelsen, M.; Mills, D.M.; Ives, C.; Gibson, R.; !1Merberg, D.; Mills, S.D.; Jiang, Q.; Taylor, D.E.; Vovis, !1G.F.; Trust, T.J. !$#journal Nature (1999) 397:176-180 !$#title Genomic sequence comparison of two unrelated isolates of the !1human gastric pathogen Helicobacter pylori. !$#cross-references MUID:99120557; PMID:9923682 !$#accession C71844 !'##molecule_type DNA !'##residues 1-380 ##label ARN !'##cross-references GB:AE001542; GB:AE001439; NID:g4155739; !1PIDN:AAD06726.1; PID:g4155747 !'##experimental_source strain J99 GENETICS !$#gene folP CLASSIFICATION #superfamily Helicobacter pylori dihydropteroate synthase; !1dihydropteroate synthase homology KEYWORDS folate biosynthesis; transferase FEATURE !$121-361 #domain dihydropteroate synthase homology #label DHS SUMMARY #length 380 #molecular-weight 43285 #checksum 3865 SEQUENCE /// ENTRY H64673 #type complete TITLE dihydropteroate synthase (EC 2.5.1.15) [similarity] - Helicobacter pylori (strain 26695) ALTERNATE_NAMES dihydropteroate pyrophosphorylase ORGANISM #formal_name Helicobacter pylori DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 01-Sep-2000 ACCESSIONS H64673 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession H64673 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-380 ##label TOM !'##cross-references GB:AE000628; GB:AE000511; NID:g2314386; !1PIDN:AAD08276.1; PID:g2314394; TIGR:HP1232 CLASSIFICATION #superfamily Helicobacter pylori dihydropteroate synthase; !1dihydropteroate synthase homology KEYWORDS folate biosynthesis; transferase FEATURE !$121-361 #domain dihydropteroate synthase homology #label DHS SUMMARY #length 380 #molecular-weight 43275 #checksum 4410 SEQUENCE /// ENTRY F70427 #type complete TITLE dihydropteroate synthase (EC 2.5.1.15) - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Sep-2000 ACCESSIONS F70427 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession F70427 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-399 ##label AQF !'##cross-references GB:AE000741; NID:g2983841; PIDN:AAC07396.1; !1PID:g2983842; GB:AE000657 !'##experimental_source strain VF5 GENETICS !$#gene folP CLASSIFICATION #superfamily Helicobacter pylori dihydropteroate synthase; !1dihydropteroate synthase homology KEYWORDS folate biosynthesis; transferase FEATURE !$128-378 #domain dihydropteroate synthase homology #label DHS SUMMARY #length 399 #molecular-weight 45383 #checksum 9820 SEQUENCE /// ENTRY SYECSD #type complete TITLE spermidine synthase (EC 2.5.1.16) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 01-Mar-2002 ACCESSIONS A29778; S45198; B33863; A64735 REFERENCE A29778 !$#authors Tabor, C.W.; Tabor, H. !$#journal J. Biol. Chem. (1987) 262:16037-16040 !$#title The speEspeD operon of Escherichia coli. Formation and !1processing of a proenzyme form of S-adenosylmethionine !1decarboxylase. !$#cross-references MUID:88058963; PMID:3316212 !$#accession A29778 !'##molecule_type DNA !'##residues 1-288 ##label TAB !'##cross-references GB:D26562; NID:g473770; PIDN:BAA05577.1; !1PID:g473788 REFERENCE S45181 !$#authors Fujita, N. !$#submission submitted to the EMBL Data Library, January 1994 !$#accession S45198 !'##molecule_type DNA !'##residues 1-288 ##label FUJ !'##cross-references EMBL:D26562; NID:g473770; PIDN:BAA05577.1; !1PID:g473788 !'##experimental_source strain K-12 substrain W3110 REFERENCE A33863 !$#authors Xie, Q.W.; Tabor, C.W.; Tabor, H. !$#journal J. Bacteriol. (1989) 171:4457-4465 !$#title Spermidine biosynthesis in Escherichia coli: promoter and !1termination regions of the speED operon. !$#cross-references MUID:89327165; PMID:2666401 !$#accession B33863 !'##status preliminary !'##molecule_type DNA !'##residues 1-18 ##label XIE !'##cross-references GB:J02804; GB:J04247 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64735 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-288 ##label BLAT !'##cross-references GB:AE000121; GB:U00096; NID:g1786306; !1PIDN:AAC73232.1; PID:g1786312; UWGP:b0121 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene speE !$#map_position 3 min FUNCTION !$#description catalyzes the formation of spermidine from decarboxylated !1S-adenosylmethionine (or S-adenosylmethioninamine) and !1putrescine !$#pathway polyamine biosynthesis CLASSIFICATION #superfamily spermidine synthase KEYWORDS polyamine biosynthesis; transferase SUMMARY #length 288 #molecular-weight 32321 #checksum 6772 SEQUENCE /// ENTRY XURT8C #type complete TITLE glutathione transferase (EC 2.5.1.18) 8, cytosolic - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1991 #sequence_revision 17-Apr-1998 #text_change 21-Jul-2000 ACCESSIONS S23433; S24505; S05250 REFERENCE S23433 !$#authors Stenberg, G.; Ridderstroem, M.; Engstroem, A.; Pemble, S.E.; !1Mannervik, B. !$#journal Biochem. J. (1992) 284:313-319 !$#title Cloning and heterologous expression of cDNA encoding class !1Alpha rat glutathione transferase 8-8, an enzyme with high !1catalytic activity towards genotoxic alpha, beta-unsaturated !1carbonyl compounds. !$#cross-references MUID:92287032; PMID:1599415 !$#accession S23433 !'##molecule_type mRNA !'##residues 1-222 ##label STE !'##cross-references EMBL:X62660; NID:g57578; PIDN:CAB46530.1; !1PID:g5420030 !'##experimental_source hepatoma; strain Wistar !$#accession S24505 !'##molecule_type protein !'##residues 1-14 ##label STE2 !'##experimental_source hepatoma REFERENCE S05250 !$#authors Alin, P.; Jensson, H.; Cederlund, E.; Joernvall, H.; !1Mannervik, B. !$#journal Biochem. J. (1989) 261:531-539 !$#title Cytosolic glutathione transferases from rat liver. Primary !1structure of class alpha glutathione transferase 8-8 and !1characterization of low-abundance class Mu glutathione !1transferases. !$#cross-references MUID:89374154; PMID:2775231 !$#accession S05250 !'##molecule_type protein !'##residues 1-17,'V',19-47,'D',49-222 ##label ALI !'##experimental_source liver COMMENT Glutathione transferases are multifunctional dimers of !1identical or similar Ya chains that catalyze the !1nucleophilic addition of glutathione to various compounds; !1they also exhibit selenium-independent glutathione !1peroxidase activity toward organic hydroperoxides. In !1addition to its enzymatic activity, the homodimer of Ya !1chains, called ligandin, binds various organic anions, !1xenobiotics, and azocarcinogen dyes. It is a cytosolic !1protein found in many mammalian tissues. FUNCTION !$#description catalyzes the conjugation of glutathione to electrophilic !1xenobiotics; involved in the reduction of organic !1hydroperoxides, the isomerization of prostaglandins and the !1binding of non-substrate hydrophobic ligands CLASSIFICATION #superfamily glutathione transferase KEYWORDS acetylated amino end; dimer; transferase FEATURE !$1-222 #product glutathione transferase 8 #status !8experimental #label MAT\ !$1 #modified_site acetylated amino end (Met) #status !8experimental SUMMARY #length 222 #molecular-weight 25510 #checksum 6928 SEQUENCE /// ENTRY XURTG #type complete TITLE glutathione transferase (EC 2.5.1.18) class alpha chain Ya1 - rat ALTERNATE_NAMES glutathione S-alkyltransferase; glutathione S-aryltransferase; glutathione S-transferase; glutathione transferase 1; ligandin ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 18-Aug-1982 #sequence_revision 28-May-1986 #text_change 07-May-1999 ACCESSIONS A92479; A92370; S64679; A00591 REFERENCE A92479 !$#authors Lai, H.C.J.; Li, N.; Weiss, M.J.; Reddy, C.C.; Tu, C.P.D. !$#journal J. Biol. Chem. (1984) 259:5536-5542 !$#title The nucleotide sequence of a rat liver glutathione !1S-transferase subunit cDNA clone. !$#cross-references MUID:84185691; PMID:6201485 !$#accession A92479 !'##molecule_type mRNA !'##residues 1-222 ##label LAI !'##experimental_source clone pGTR261, liver REFERENCE A92370 !$#authors Kalinyak, J.E.; Taylor, J.M. !$#journal J. Biol. Chem. (1982) 257:523-530 !$#title Rat glutathione S-transferase. Cloning of double-stranded !1cDNA and induction of its mRNA. !$#cross-references MUID:82075944; PMID:6273441 !$#accession A92370 !'##molecule_type mRNA !'##residues 46-197 ##label KAL REFERENCE S64679 !$#authors Yeh, H.I.; Lee, J.Y.; Tsai, S.P.; Hsieh, C.H.; Tam, M.F. !$#journal Biochem. J. (1996) 314:1017-1025 !$#title Rat kidney glutathione S-transferase 1 subunits have !1C-terminal truncations. !$#cross-references MUID:96177880; PMID:8615753 !$#accession S64679 !'##molecule_type protein !'##residues 32-207,'V',209-222 ##label YEH !'##experimental_source kidney, liver COMMENT Glutathione transferases are multifunctional dimers of !1identical or similar Ya chains that catalyze the !1nucleophilic addition of glutathione to various compounds; !1they also exhibit selenium-independent glutathione !1peroxidase activity toward organic hydroperoxides. COMMENT In addition to its enzymatic activity, the homodimer of Ya !1chains, called ligandin, binds various organic anions, !1xenobiotics, and azocarcinogen dyes. It is a cytosolic !1protein found in many mammalian tissues. CLASSIFICATION #superfamily glutathione transferase KEYWORDS acetylated amino end; dimer; kidney; liver; transferase FEATURE !$2-222 #product glutathione transferase 1, 25.5K (liver, !8kidney) #status experimental #label GT1\ !$2-221 #product glutathione transferase 1, 25.3K (liver, !8kidney) #status experimental #label GT2\ !$2-218 #product glutathione transferase 1, 24.9K (kidney) !8#status experimental #label GT3\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status predicted SUMMARY #length 222 #molecular-weight 25639 #checksum 4268 SEQUENCE /// ENTRY A27848 #type complete TITLE glutathione transferase (EC 2.5.1.18) class alpha chain Ya1 [similarity] - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 31-Dec-2000 ACCESSIONS A27848; S15851; C28946 REFERENCE A27848 !$#authors Daniel, V.; Sharon, R.; Tichauer, Y.; Sarid, S. !$#journal DNA (1987) 6:317-324 !$#title Mouse glutathione S-transferase Ya subunit: gene structure !1and sequence. !$#cross-references MUID:88003969; PMID:3652905 !$#accession A27848 !'##molecule_type DNA !'##residues 1-223 ##label DAN !'##cross-references GB:M19250; NID:g193693; GB:M19251; NID:g193694; !1GB:M19252; NID:g193695; GB:M19253; NID:g193696; GB:M19254; !1NID:g193697; GB:M19255; NID:g193698; GB:M19256; NID:g193699; !1GB:X06723; GB:M17336; PIDN:AAA37750.1; PID:g387179 REFERENCE S15851 !$#authors McLellan, L.I.; Kerr, L.A.; Cronshaw, A.D.; Hayes, J.D. !$#journal Biochem. J. (1991) 276:461-469 !$#title Regulation of mouse glutathione S-transferases by !1chemoprotectors. Molecular evidence for the existence of !1three distinct Alpha-class glutathione S-transferase !1subunits, Ya(1), Ya(2) and Ya(3), in mouse liver. !$#cross-references MUID:91264802; PMID:2049074 !$#accession S15851 !'##molecule_type protein !'##residues 16-36;51-59;63-165;208-223 ##label MCL REFERENCE A92668 !$#authors Pearson, W.R.; Reinhart, J.; Sisk, S.C.; Anderson, K.S.; !1Adler, P.N. !$#journal J. Biol. Chem. (1988) 263:13324-13332 !$#title Tissue-specific induction of murine glutathione transferase !1mRNAs by butylated hydroxyanisole. !$#cross-references MUID:88330838; PMID:3417659 !$#accession C28946 !'##molecule_type mRNA !'##residues 1-65,'V',67-95,'T',97-157,'V',159-162,'L',164-169,'L', !1171-207,'L',209-213,'E',215-218,'V',220-221,'F' ##label PEA !'##cross-references GB:J03958; NID:g193691; PIDN:AAA37749.1; !1PID:g309279 GENETICS !$#gene Ya1; MGI:Gsta1 !'##cross-references MGI:1095417 !$#map_position 9:43.0 CLASSIFICATION #superfamily glutathione transferase KEYWORDS dimer; transferase SUMMARY #length 223 #molecular-weight 25608 #checksum 9216 SEQUENCE /// ENTRY B41031 #type complete TITLE glutathione transferase (EC 2.5.1.18) alpha-II, hepatic [similarity] - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS B41031 REFERENCE A41031 !$#authors Gardlik, S.; Gasser, R.; Philpot, R.M.; Serabjit-Singh, C.J. !$#journal J. Biol. Chem. (1991) 266:19681-19687 !$#title The major alpha-class glutathione S-transferases of rabbit !1lung and liver. Primary sequences, expression, and !1regulation. !$#cross-references MUID:92011771; PMID:1918075 !$#accession B41031 !'##molecule_type mRNA !'##residues 1-221 ##label GAR !'##cross-references GB:M74529; NID:g349539; PIDN:AAA31260.1; !1PID:g349540 CLASSIFICATION #superfamily glutathione transferase KEYWORDS liver; transferase SUMMARY #length 221 #molecular-weight 25449 #checksum 1916 SEQUENCE /// ENTRY A41031 #type complete TITLE glutathione transferase (EC 2.5.1.18) alpha-I, pulmonary [similarity] - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS A41031 REFERENCE A41031 !$#authors Gardlik, S.; Gasser, R.; Philpot, R.M.; Serabjit-Singh, C.J. !$#journal J. Biol. Chem. (1991) 266:19681-19687 !$#title The major alpha-class glutathione S-transferases of rabbit !1lung and liver. Primary sequences, expression, and !1regulation. !$#cross-references MUID:92011771; PMID:1918075 !$#accession A41031 !'##molecule_type mRNA !'##residues 1-223 ##label GAR !'##cross-references GB:M74528; NID:g349537; PIDN:AAA31259.1; !1PID:g349538 CLASSIFICATION #superfamily glutathione transferase KEYWORDS dimer; transferase SUMMARY #length 223 #molecular-weight 25691 #checksum 624 SEQUENCE /// ENTRY A26753 #type complete TITLE glutathione transferase (EC 2.5.1.18) Yc1 [similarity] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS A26753; A26754; B54858; S09585 REFERENCE A26753 !$#authors Telakowski-Hopkins, C.A.; Rodkey, J.A.; Bennett, C.D.; Lu, !1A.Y.H.; Pickett, C.B. !$#journal J. Biol. Chem. (1985) 260:5820-5825 !$#title Rat liver glutathione S-transferases. Construction of a cDNA !1clone complementary to a Yc mRNA and prediction of the !1complete amino acid sequence of a Yc subunit. !$#cross-references MUID:85182743; PMID:2985614 !$#accession A26753 !'##molecule_type mRNA !'##residues 1-221 ##label TEL !'##cross-references GB:K01932; GB:M10960; NID:g204516; PIDN:AAA41294.1; !1PID:g204517 REFERENCE A26754 !$#authors Tu, C.P.D.; Lai, H.C.J.; Li, N.; Weiss, M.J.; Reddy, C.C. !$#journal J. Biol. Chem. (1984) 259:9434-9439 !$#title The Yc and Ya subunits of rat liver glutathione !1S-transferases are the products of separate genes. !$#cross-references MUID:84264589; PMID:6204982 !$#accession A26754 !'##molecule_type mRNA !'##residues 75-221 ##label TUC REFERENCE A54858 !$#authors Hayes, J.D.; Nguyen, T.; Judah, D.J.; Petersson, D.G.; Neal, !1G.E. !$#journal J. Biol. Chem. (1994) 269:20707-20717 !$#title Cloning of cDNAs from fetal rat liver encoding glutathione !1S-transferase Yc polypeptides. The Yc-2 subunit is expressed !1in adult rat liver resistant to the hepatocarcinogen !1aflatoxin B-1. !$#cross-references MUID:94327654; PMID:8051171 !$#accession B54858 !'##molecule_type mRNA !'##residues 1-221 ##label HAY !'##cross-references GB:X78848; NID:g576437; PIDN:CAA55405.1; !1PID:g576438 REFERENCE S09585 !$#authors Huskey, S.E.W.; Wang, R.W.; Linemeyer, D.L.; Pickett, C.B.; !1Lu, A.Y.H. !$#journal Arch. Biochem. Biophys. (1990) 279:116-121 !$#title Expression in Escherichia coli of rat liver cytosolic !1glutathione S-transferase Yc cDNA. !$#cross-references MUID:90247876; PMID:2186703 !$#accession S09585 !'##molecule_type protein !'##residues 1-31 ##label HUS CLASSIFICATION #superfamily glutathione transferase KEYWORDS dimer; transferase SUMMARY #length 221 #molecular-weight 25319 #checksum 6179 SEQUENCE /// ENTRY A37378 #type complete TITLE glutathione transferase (EC 2.5.1.18) pi [validated] - human ALTERNATE_NAMES glutathione S-alkyltransferase; glutathione S-aryltransferase; glutathione S-transferase-pi (GST-pi); glutathione transferase 3; S-(hydroxyalkyl)-glutathione lyase ORGANISM #formal_name Homo sapiens #common_name man DATE 17-Apr-1993 #sequence_revision 17-Apr-1993 #text_change 15-Sep-2000 ACCESSIONS JS0153; S01672; S00899; S03015; A37378; A60445; A60775; !1JT0770; JT0769; G01934; S09316; A22457; A37520; A60976; !1A60826; S27189; S23937; C28810; A61370; S35051; D28810; !1L24735 REFERENCE JS0153 !$#authors Morrow, C.S.; Cowan, K.H.; Goldsmith, M.E. !$#journal Gene (1989) 75:3-11 !$#title Structure of the human genomic glutathione S-transferase-pi !1gene. !$#cross-references MUID:89252918; PMID:2542132 !$#accession JS0153 !'##molecule_type DNA !'##residues 1-210 ##label MOR !'##cross-references GB:M24485; NID:g341173; PIDN:AAA56823.1; !1PID:g598158 REFERENCE S01672 !$#authors Cowell, I.G.; Dixon, K.H.; Pemble, S.E.; Ketterer, B.; !1Taylor, J.B. !$#journal Biochem. J. (1988) 255:79-83 !$#title The structure of the human glutathione S-transferase pi !1gene. !$#cross-references MUID:89061690; PMID:3196325 !$#accession S01672 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-184,'R',186-210 ##label COW1 !'##cross-references EMBL:X08094 !'##note the authors translated codon CGT for residue 71 as Leu, and !1codon AGG for residue 185 as Ser REFERENCE S00899 !$#authors Kano, T.; Sakai, M.; Muramatsu, M. !$#journal Cancer Res. (1987) 47:5626-5630 !$#title Structure and expression of a human class pi glutathione !1S-transferase messenger RNA. !$#cross-references MUID:88026724; PMID:3664469 !$#accession S00899 !'##molecule_type mRNA !'##residues 1-210 ##label KAN !'##cross-references EMBL:X06547; NID:g31945; PIDN:CAA29794.1; !1PID:g31946 REFERENCE S03015 !$#authors Cowell, I.G. !$#submission submitted to the EMBL Data Library, July 1988 !$#accession S03015 !'##molecule_type DNA !'##residues 1-92,'M',94-95,'AWRTSAANTSPSSTPTM',113-185,'P',187-210 !1##label COW2 !'##cross-references EMBL:X08094 REFERENCE A37378 !$#authors Moscow, J.A.; Fairchild, C.R.; Madden, M.J.; Ransom, D.T.; !1Wieand, H.S.; O'Brien, E.E.; Poplack, D.G.; Cossman, J.; !1Myers, C.E.; Cowan, K.H. !$#journal Cancer Res. (1989) 49:1422-1428 !$#title Expression of anionic glutathione-S-transferase and !1P-glycoprotein genes in human tissues and tumors. !$#cross-references MUID:89168166; PMID:2466554 !$#accession A37378 !'##molecule_type mRNA !'##residues 1-210 ##label MOS !'##cross-references GB:X15480; NID:g31947; PIDN:CAA33508.1; PID:g31948 REFERENCE A60445 !$#authors Board, P.G.; Webb, G.C.; Coggan, M. !$#journal Ann. Hum. Genet. (1989) 53:205-213 !$#title Isolation of a cDNA clone and localization of the human !1glutathione S-transferase 3 genes to chromosome bands 11q13 !1and 12q13-14. !$#cross-references MUID:90087645; PMID:2596826 !$#accession A60445 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 35-104,'V',106-113,'V',115-210 ##label BOA !'##experimental_source lung REFERENCE A60775 !$#authors Konohana, A.; Konohana, I.; Schroeder, W.T.; O'Brien, W.R.; !1Amagai, M.; Greer, J.; Shimizu, N.; Gammon, W.R.; Siciliano, !1M.J.; Duvic, M. !$#journal J. Invest. Dermatol. (1990) 95:119-126 !$#title Placental glutathione-S-transferase-pi mRNA is abundantly !1expressed in human skin. !$#cross-references MUID:90338790; PMID:2380573 !$#accession A60775 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 23-210 ##label KON !'##experimental_source placenta !'##note the mRNA was also detected in skin REFERENCE JT0769 !$#authors Mera, N.; Ohmori, S.; Nakasa, H.; Kitada, M. !$#submission submitted to JIPID, May 1994 !$#description Nucleotide sequence of pi class glutathione S-transferase in !1human fetal liver. !$#accession JT0770 !'##molecule_type mRNA !'##residues 1-210 ##label MER1 !'##experimental_source fetal liver; clone pFGP-2 !$#accession JT0769 !'##molecule_type mRNA !'##residues 1-104,'V',106-210 ##label MER2 !'##experimental_source fetal liver; clone pFGP-1 REFERENCE H00710 !$#authors Ali-Osman, F.; Akande, O. !$#submission submitted to the EMBL Data Library, July 1995 !$#accession G01934 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 'LRHL',2-104,'V',106-107,'V',109-210 ##label ALI2 !'##cross-references EMBL:U30897; NID:g1401046; PID:g1401047 REFERENCE S09316 !$#authors Ahmad, H.; Wilson, D.E.; Fritz, R.R.; Singh, S.V.; Medh, !1R.D.; Nagle, G.T.; Awasthi, Y.C.; Kurosky, A. !$#journal Arch. Biochem. Biophys. (1990) 278:398-408 !$#title Primary and secondary structural analyses of glutathione !1S-transferase pi from human placenta. !$#cross-references MUID:90225809; PMID:2327795 !$#accession S09316 !'##molecule_type protein !'##residues 2-210 ##label AH3 !'##note 104-Val was also found REFERENCE A91336 !$#authors Alin, P.; Mannervik, B.; Jornvall, H. !$#journal FEBS Lett. (1985) 182:319-322 !$#title Structural evidence for three different types of glutathione !1transferase in human tissues. !$#cross-references MUID:85154554; PMID:3979555 !$#accession A22457 !'##molecule_type protein !'##residues 2-24 ##label ALI1 REFERENCE A24735 !$#authors Mannervik, B.; Alin, P.; Guthenberg, C.; Jensson, H.; Tahir, !1M.K.; Warholm, M.; Jornvall, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:7202-7206 !$#title Identification of three classes of cytosolic glutathione !1transferase common to several mammalian species: correlation !1between structural data and enzymatic properties. !$#cross-references MUID:86042634; PMID:3864155 !$#accession A37520 !'##molecule_type protein !'##residues 2-24 ##label MAN REFERENCE A60976 !$#authors Ahmad, H.; Medh, R.D.; Singh, S.V.; Caccuri, A.M.; Ansari, !1G.A.S.; Awasthi, Y.C. !$#journal Enzyme (1989) 42:129-135 !$#title Anionic glutathione S-transferases of human erythrocytes, !1placenta, and lung: evidence for structural differences. !$#cross-references MUID:90126718; PMID:2612452 !$#accession A60976 !'##molecule_type protein !'##residues 'X',2-14,'X',16-19,'X',21-22 ##label AHM !'##experimental_source erythrocytes REFERENCE A60826 !$#authors Caccuri, A.M.; Di Ilio, C.; Compagnone, D.; Barra, D.; !1Federici, G. !$#journal Biochem. Med. Metab. Biol. (1988) 40:123-132 !$#title Acidic glutathione transferase from human heart. !1Characterization and N-terminal sequence determination. !$#cross-references MUID:89050639; PMID:3190921 !$#accession A60826 !'##molecule_type protein !'##residues 2-14,'X',16-46,'ASM' ##label CAC !'##experimental_source heart REFERENCE S27188 !$#authors Singhal, S.S.; Saxena, M.; Awasthi, S.; Ahmad, H.; Sharma, !1R.; Awasthi, Y.C. !$#journal Biochim. Biophys. Acta (1992) 1171:19-26 !$#title Gender related differences in the expression and !1characteristics of glutathione S-transferases of human !1colon. !$#cross-references MUID:93042004; PMID:1420361 !$#accession S27189 !'##status preliminary !'##molecule_type protein !'##residues 2-13 ##label SIN REFERENCE S23937 !$#authors Lo Bello, M.; Petruzzelli, R.; Reale, L.; Ricci, G.; Barra, !1D.; Federici, G. !$#journal Biochim. Biophys. Acta (1992) 1121:167-172 !$#title Chemical modification of human placental glutathione !1transferase by pyridoxal 5'-phosphate. !$#cross-references MUID:92287946; PMID:1599939 !$#accession S23937 !'##status preliminary !'##molecule_type protein !'##residues 122-131,'Y',133-141 ##label LOA REFERENCE A90081 !$#authors Singh, S.V.; Ahmad, H.; Kurosky, A.; Awasthi, Y.C. !$#journal Arch. Biochem. Biophys. (1988) 264:13-22 !$#title Purification and characterization of unique glutathione !1S-transferases from human muscle. !$#cross-references MUID:88280250; PMID:3395118 !$#accession C28810 !'##molecule_type protein !'##residues 2-14 ##label SI2 REFERENCE A61370 !$#authors Blacker, K.L.; Olson, E.; Vessey, D.A.; Boyer, T.D. !$#journal J. Invest. Dermatol. (1991) 97:442-446 !$#title Characterization of glutathione S-transferase in cultured !1human keratinocytes. !$#cross-references MUID:91341211; PMID:1875044 !$#accession A61370 !'##molecule_type protein !'##residues 2-12,'X',14,'X',16-17 ##label BLA !'##experimental_source keratinocytes REFERENCE S35051 !$#authors Xia, C.; Meyer, D.J.; Chen, H.; Reinemer, P.; Huber, R.; !1Ketterer, B. !$#journal Biochem. J. (1993) 293:357-362 !$#title Chemical modification of GSH transferase P1-1 confirms the !1presence of Arg-13, Lys-44 and one carboxylate group in the !1GSH-binding domain of the active site. !$#cross-references MUID:93343862; PMID:8343115 !$#accession S35051 !'##molecule_type protein !'##residues 31-50 ##label XIA REFERENCE A51752 !$#authors Reinemer, P.; Dirr, H.W.; Ladenstein, R.; Lo Bello, M.; !1Federici, G.; Huber, R.; Parker, M.W. !$#submission submitted to the Brookhaven Protein Data Bank, May 1992 !$#cross-references PDB:1GSS !$#contents annotation; X-ray crystallography, 2.8 angstroms, residues !12-210 REFERENCE A38951 !$#authors Reinemer, P.; Dirr, H.W.; Ladenstein, R.; Huber, R.; !1LoBello, M.; Federici, G.; Parker, M.W. !$#journal J. Mol. Biol. (1992) 227:214-226 !$#title Three-dimensional structure of class pi glutathione !1S-transferase from human placenta in complex with !1S-hexylglutathione at 2.8 angstroms resolution. !$#cross-references MUID:92395662; PMID:1522586 !$#contents annotation; X-ray crystallography, 2.8 angstroms GENETICS !$#gene GDB:GSTP1 !'##cross-references GDB:120024; OMIM:138370 !$#map_position 11q13-11q13 !$#introns 1/1; 13/1; 48/3; 78/1; 112/3; 148/3 COMPLEX homodimer; heterodimer of alpha, mu, or pi chains FUNCTION !$#description catalyzes the conjugation of compounds with electrophilic !1groups by reduced glutathione !$#pathway detoxification !$#note involved in the detoxification of several electrophilic, !1hydrophobic xenobiotics CLASSIFICATION #superfamily glutathione transferase KEYWORDS detoxification; glutathione; heterodimer; homodimer; !1transferase FEATURE !$2-210 #product glutathione transferase #status predicted !8#label MAT\ !$8 #active_site Tyr #status predicted\ !$14,45 #binding_site substrate (Arg, Lys) #status !8experimental\ !$99 #binding_site substrate (Asp) (shared with dimeric !8partner) #status experimental SUMMARY #length 210 #molecular-weight 23356 #checksum 7474 SEQUENCE /// ENTRY XURTGP #type complete TITLE glutathione transferase (EC 2.5.1.18) 7 - rat ALTERNATE_NAMES glutathione S-alkyltransferase; glutathione S-aryltransferase; glutathione S-transferase P; glutathione transferase, placental ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 11-Jun-1999 ACCESSIONS A26546; A23780; A60785; D37520; M24735 REFERENCE A26546 !$#authors Okuda, A.; Sakai, M.; Muramatsu, M. !$#journal J. Biol. Chem. (1987) 262:3858-3863 !$#title The structure of the rat glutathione S-transferase P gene !1and related pseudogenes. !$#cross-references MUID:87137695; PMID:3029128 !$#accession A26546 !'##molecule_type DNA !'##residues 1-210 ##label OKU !'##cross-references GB:L29427; GB:J02690; GB:N00039; NID:g459938; !1PIDN:AAB59718.1; PID:g459939 REFERENCE A23780 !$#authors Suguoka, Y.; Kano, T.; Okuda, A.; Sakai, M.; Kitagawa, T.; !1Muramatsu, M. !$#journal Nucleic Acids Res. (1985) 13:6049-6057 !$#title Cloning and the nucleotide sequence of rat glutathione !1S-transferase P cDNA. !$#cross-references MUID:86016072; PMID:2995915 !$#accession A23780 !'##molecule_type mRNA !'##residues 1-210 ##label SUG !'##cross-references GB:X02904; NID:g56335; PIDN:CAA26664.1; PID:g56336 REFERENCE A60785 !$#authors Rushmore, T.H.; Harris, L.; Nagai, M.; Sharma, R.N.; Hayes, !1M.A.; Cameron, R.G.; Murray, R.K.; Farber, E. !$#journal Cancer Res. (1988) 48:2805-2812 !$#title Purification and characterization of P-52 (glutathione !1S-transferase-P or 7-7) from normal liver and putative !1preneoplastic liver nodules. !$#cross-references MUID:88194343; PMID:3359441 !$#accession A60785 !'##molecule_type protein !'##residues 2-14,'Y',16-27 ##label RUS !'##note the source was a mixture of monomers of closely related !1isoforms REFERENCE A24735 !$#authors Mannervik, B.; Alin, P.; Guthenberg, C.; Jensson, H.; Tahir, !1M.K.; Warholm, M.; Jornvall, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:7202-7206 !$#title Identification of three classes of cytosolic glutathione !1transferase common to several mammalian species: correlation !1between structural data and enzymatic properties. !$#cross-references MUID:86042634; PMID:3864155 !$#accession D37520 !'##molecule_type protein !'##residues 2-11 ##label MAN COMMENT This glutathione transferase isozyme polypeptide chain is !1distinct from the liver enzyme Ya and Yc chains. GENETICS !$#introns 1/1; 13/1; 48/3; 78/1; 112/3; 148/3 CLASSIFICATION #superfamily glutathione transferase KEYWORDS dimer; transferase SUMMARY #length 210 #molecular-weight 23439 #checksum 8598 SEQUENCE /// ENTRY A55140 #type complete TITLE glutathione transferase (EC 2.5.1.18) piA [similarity] - mouse ALTERNATE_NAMES glutathione S-transferase piA ORGANISM #formal_name Mus musculus #common_name house mouse DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS A55140; S43380 REFERENCE A55140 !$#authors Xu, X.; Stambrook, P.J. !$#journal J. Biol. Chem. (1994) 269:30268-30273 !$#title Two murine GSTpi genes are arranged in tandem and are !1differentially expressed. !$#cross-references MUID:95074023; PMID:7982937 !$#accession A55140 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-209 ##label XUA !'##cross-references GB:U15654; NID:g577418; PIDN:AAA64836.1; !1PID:g577419 REFERENCE S43379 !$#authors Bammler, T.K.; Smith, C.A.D.; Wolf, C.R. !$#journal Biochem. J. (1994) 298:385-390 !$#title Isolation and characterization of two mouse Pi-class !1glutathione S-transferase genes. !$#cross-references MUID:94183166; PMID:8135745 !$#accession S43380 !'##molecule_type DNA !'##residues 1-209 ##label BAM !'##cross-references GB:X76143; NID:g429045 !'##experimental_source strain Balb/C, adult liver !'##note this ORF is not trnaslated in GenBank entry MMGSTP1, release !1114 GENETICS !$#gene GSTpiA !$#map_position 1 CLASSIFICATION #superfamily glutathione transferase KEYWORDS transferase SUMMARY #length 209 #molecular-weight 23406 #checksum 3830 SEQUENCE /// ENTRY B55140 #type complete TITLE glutathione transferase (EC 2.5.1.18) class piB [validated] - mouse ALTERNATE_NAMES glutathione S-transferase class pi; glutathione S-transferase Yf ORGANISM #formal_name Mus musculus #common_name house mouse DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS S12709; B55140; S43379; S15420; S24426; S32549; S30374; !1S35605; S71488 REFERENCE S12709 !$#authors Hatayama, I.; Satoh, K.; Sato, K. !$#journal Nucleic Acids Res. (1990) 18:4606 !$#title A cDNA sequence coding a class pi glutathione S-transferase !1of mouse. !$#cross-references MUID:90356413; PMID:2388840 !$#accession S12709 !'##molecule_type mRNA !'##residues 1-210 ##label HAT !'##cross-references EMBL:X53451; NID:g51124; PIDN:CAA37529.1; !1PID:g51125 !'##experimental_source strain BALB/c REFERENCE A55140 !$#authors Xu, X.; Stambrook, P.J. !$#journal J. Biol. Chem. (1994) 269:30268-30273 !$#title Two murine GSTpi genes are arranged in tandem and are !1differentially expressed. !$#cross-references MUID:95074023; PMID:7982937 !$#accession B55140 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 2-210 ##label XUA !'##cross-references GB:U15654; NID:g577418; PIDN:AAA64837.1; !1PID:g577420 !'##experimental_source strain 129SvJ; liver REFERENCE S43379 !$#authors Bammler, T.K.; Smith, C.A.D.; Wolf, C.R. !$#journal Biochem. J. (1994) 298:385-390 !$#title Isolation and characterization of two mouse Pi-class !1glutathione S-transferase genes. !$#cross-references MUID:94183166; PMID:8135745 !$#accession S43379 !'##molecule_type DNA !'##residues 2-210 ##label BAM !'##cross-references GB:X76144; NID:g429046 !'##experimental_source strain Balb/C, adult liver !'##note this ORF is not trnaslated in GenBank entry MMGSTP2, release !1114 REFERENCE S15420 !$#authors Phillips, M.F.; Mantle, T.J. !$#journal Biochem. J. (1991) 275:703-709 !$#title The initial-rate kinetics of mouse glutathione S-transferase !1YfYf. Evidence for an allosteric site for ethacrynic acid. !$#cross-references MUID:91248105; PMID:2039447 !$#accession S15420 !'##molecule_type protein !'##residues 2-26 ##label PHI REFERENCE S24426 !$#authors Singhal, S.S.; Saxena, M.; Ahmad, H.; Awasthi, Y.C. !$#journal Biochim. Biophys. Acta (1992) 1117:105 !$#title Corrigendum. Glutathione S-transferase of mouse liver: !1sex-related differences in the expression of various !1isozymes. !$#cross-references MUID:92329477; PMID:1627586 !$#accession S24426 !'##molecule_type protein !'##residues 2-21 ##label SIN REFERENCE S32548 !$#authors Singhal, S.S.; Saxena, M.; Ahmad, H.; Awasthi, Y.C. !$#journal Biochim. Biophys. Acta (1992) 1116:137-146 !$#title Glutathione S-transferases of mouse liver: sex-related !1differences in the expression of various isozymes. !$#cross-references MUID:92256466; PMID:1581342 !$#accession S32549 !'##molecule_type protein !'##residues 2-11 ##label SI2 !'##experimental_source isoform pI 8.7, female; liver REFERENCE S30369 !$#authors Awasthi, S.; Singhal, S.S.; Srivastava, S.K.; Awasthi, Y.C. !$#journal Arch. Biochem. Biophys. (1993) 301:143-150 !$#title Purification and characterization of glutathione !1S-transferase of murine ovary and testis. !$#cross-references MUID:93183007; PMID:8442656 !$#accession S30374 !'##molecule_type protein !'##residues 2-11 ##label AWA !'##experimental_source isoform pI 8.9 REFERENCE S35605 !$#authors Phillips, M.F.; Mantle, T.J. !$#journal Biochem. J. (1993) 294:57-62 !$#title Inactivation of mouse liver glutathione S-transferase YfYf !1(Pi class) by ethacrynic acid and 5,5'-dithiobis- !1(2-nitrobenzoic acid). !$#cross-references MUID:93371382; PMID:8363586 !$#accession S35605 !'##molecule_type protein !'##residues 17-36 ##label PH2 !'##experimental_source liver REFERENCE S16933 !$#authors Hayes, J.D.; Kerr, L.A.; Peacock, S.D.; Cronshaw, A.D.; !1McLellan, L.I. !$#journal Biochem. J. (1991) 277:501-512 !$#title Hepatic glutathione S-transferases in mice fed on a diet !1containing the anticarcinogenic antioxidant butylated !1hydroxyanisole. Isolation of mouse glutathione S-transferase !1heterodimers by gradient elution of the !1glutathione-Sepharose affinity matrix. !$#cross-references MUID:91315425; PMID:1859377 !$#accession S71488 !'##molecule_type protein !'##residues 2-14,'X',16-27 ##label HAY !'##experimental_source liver COMMENT At least five species-independent classes of cytosolic !1glutathion transferases have been described: alpha, mu, pi, !1sigma and theta. Additionally a microsomal trimeric form and !1a theta-class mitochondrial form are known. GENETICS !$#gene GSTpiB !$#map_position 1 COMPLEX dimer FUNCTION !$#description catalyzes the nucleophilic conjugation of intracellular !1glutathione to a wide variety of electrophilic cytotoxic and !1genotoxic molecules from endogenous origin !$#pathway detoxification; xenobiotics metabolism !$#note increased hydrophilicity of GSH-conjugates facilitates their !1further metabolism and elimination; used as anti-cancer !1drug; inhibited by S-hexylglutathion; protects tissues !1against various types of damage CLASSIFICATION #superfamily glutathione transferase KEYWORDS dimer; transferase FEATURE !$2-210 #product glutathione transferase class pi #status !8experimental #label MAT\ !$8 #active_site Tyr #status predicted\ !$14,45 #binding_site substrate (Arg, Lys) #status predicted\ !$99 #binding_site substrate (Asp) (shared with dimeric !8partner) #status predicted SUMMARY #length 210 #molecular-weight 23609 #checksum 8609 SEQUENCE /// ENTRY XURTG4 #type complete TITLE glutathione transferase (EC 2.5.1.18) 4 - rat ALTERNATE_NAMES glutathione S-transferase Yb2 chain (anionic) ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1988 #sequence_revision 31-Dec-1989 #text_change 11-Jun-1999 ACCESSIONS A29231; A25386; B26187; A26307; G24735; A61004; S33238 REFERENCE A29231 !$#authors Lai, H.C.J.; Qian, B.; Grove, G.; Tu, C.P.D. !$#journal J. Biol. Chem. (1988) 263:11389-11395 !$#title Gene expression of rat glutathione S-transferases. Evidence !1for gene conversion in the evolution of the Y-b multigene !1family. !$#cross-references MUID:88298790; PMID:3403534 !$#accession A29231 !'##molecule_type mRNA; DNA !'##residues 1-218 ##label LAI !'##cross-references GB:J03914; NID:g204527; PIDN:AAA41296.1; !1PID:g204528 REFERENCE A91167 !$#authors Alin, P.; Mannervik, B.; Jornvall, H. !$#journal Eur. J. Biochem. (1986) 156:343-350 !$#title Cytosolic rat liver glutathione transferase 4-4. Primary !1structure of the protein reveals extensive differences !1between homologous glutathione transferases of classes alpha !1and mu. !$#cross-references MUID:86192461; PMID:3699019 !$#accession A25386 !'##molecule_type protein !'##residues 2-146,'S',148-218 ##label ALI REFERENCE A26187 !$#authors Lai, H.C.J.; Tu, C.P.D. !$#journal J. Biol. Chem. (1986) 261:13793-13799 !$#title Rat glutathione S-transferases supergene family. !1Characterization of an anionic Yb subunit cDNA clone. !$#cross-references MUID:87008619; PMID:3020050 !$#accession B26187 !'##molecule_type mRNA; DNA !'##residues 1-218 ##label LA2 REFERENCE A26307 !$#authors Ding, G.J.F.; Ding, V.D.H.; Rodkey, J.A.; Bennett, C.D.; Lu, !1A.Y.H.; Pickett, C.B. !$#journal J. Biol. Chem. (1986) 261:7952-7957 !$#title Rat liver glutathione S-transferases. DNA sequence analysis !1of a Yb2 cDNA clone and regulation of the Yb1 and Yb2 mRNAs !1by phenobarbital. !$#cross-references MUID:86224097; PMID:3011803 !$#accession A26307 !'##molecule_type mRNA; protein !'##residues 2-218 ##label DIN !'##cross-references GB:M13590 REFERENCE A24735 !$#authors Mannervik, B.; Alin, P.; Guthenberg, C.; Jensson, H.; Tahir, !1M.K.; Warholm, M.; Jornvall, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:7202-7206 !$#title Identification of three classes of cytosolic glutathione !1transferase common to several mammalian species: correlation !1between structural data and enzymatic properties. !$#cross-references MUID:86042634; PMID:3864155 !$#accession G24735 !'##molecule_type protein !'##residues 2-26 ##label MAN REFERENCE A61004 !$#authors Chang, L.H.; Hsieh, J.C.; Chen, W.L.; Tam, M.F. !$#journal Electrophoresis (1990) 11:589-593 !$#title Identification of rat liver glutathione S-transferase Yb !1subunits by partial N-terminal sequencing after !1electro-blotting of proteins onto a polyvinylidene !1difluoride membrane from an analytical isoelectric focusing !1gel. !$#cross-references MUID:91031411; PMID:2226415 !$#accession A61004 !'##molecule_type protein !'##residues 2-28 ##label CHA REFERENCE S33237 !$#authors Ben-Arie, N.; Khen, M.; Lancet, D. !$#journal Biochem. J. (1993) 292:379-384 !$#title Glutathione S-transferases in rat olfactory epithelium: !1purification, molecular properties and odorant !1biotransformation. !$#cross-references MUID:93277499; PMID:8503873 !$#accession S33238 !'##molecule_type protein !'##residues 2-22 ##label BEN !'##note 4-Ile, 8-Arg, 9-Asn, 10-Val, 14-Thr, and 20-Leu were also found COMMENT The active cytosolic glutathione transferases are dimers; at !1least six combinations of the four chain types can occur, !11-1, 1-2, 2-2, 3-3, 3-4, and 4-4. GENETICS !$#gene Yb2 !$#introns 12/3; 38/1; 59/3; 87/1; 120/3; 152/3; 189/3 CLASSIFICATION #superfamily glutathione transferase KEYWORDS dimer; transferase SUMMARY #length 218 #molecular-weight 25702 #checksum 2285 SEQUENCE /// ENTRY XUFF11 #type complete TITLE glutathione transferase (EC 2.5.1.18) D1 - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 21-Jul-2000 ACCESSIONS A34798; G46681 REFERENCE A34798 !$#authors Toung, Y.P.S.; Hsieh, T.; Tu, C.P.D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:31-35 !$#title Drosophila glutathione S-transferase 1-1 shares a region of !1sequence homology with the maize glutathione S-transferase !1III. !$#cross-references MUID:90115864; PMID:2296588 !$#accession A34798 !'##molecule_type DNA !'##residues 1-209 ##label TOU1 !'##cross-references GB:X14233; NID:g8033; PIDN:CAA32449.1; PID:g8034 REFERENCE A46681 !$#authors Toung, Y.P.; Hsieh, T.S.; Tu, C.P. !$#journal J. Biol. Chem. (1993) 268:9737-9746 !$#title The glutathione S-transferase D genes. A divergently !1organized, intronless gene family in Drosophila !1melanogaster. !$#cross-references MUID:93252851; PMID:7683659 !$#accession G46681 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 2-209 ##label TOU2 !'##note sequence extracted from NCBI backbone (NCBIP:133944) GENETICS !$#gene FlyBase:GstD1 !'##cross-references FlyBase:FBgn0001149 COMPLEX homodimer CLASSIFICATION #superfamily glutathione transferase KEYWORDS homodimer; transferase FEATURE !$6 #active_site Tyr #status predicted SUMMARY #length 209 #molecular-weight 23866 #checksum 5317 SEQUENCE /// ENTRY A42045 #type complete TITLE glutathione transferase (EC 2.5.1.18) class I - house fly ORGANISM #formal_name Musca domestica #common_name house fly DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A42045; S16293 REFERENCE A42045 !$#authors Fournier, D.; Bride, J.M.; Poirie, M.; Berge, J.B.; Plapp !1Jr., F.W. !$#journal J. Biol. Chem. (1992) 267:1840-1845 !$#title Insect glutathione S-transferases. Biochemical !1characteristics of the major forms from houseflies !1susceptible and resistant to insecticides. !$#cross-references MUID:92112911; PMID:1730722 !$#accession A42045 !'##molecule_type mRNA !'##residues 1-208 ##label FOU !'##cross-references GB:M83249; NID:g159467; PIDN:AAA29294.1; !1PID:g159468 !'##note sequence extracted from NCBI backbone (NCBIN:76017, !1NCBIP:76018) REFERENCE S16293 !$#authors Wang, J.; McCommas, S.; Syvanen, M. !$#journal Mol. Gen. Genet. (1991) 227:260-266 !$#title Molecular cloning of a glutathione S-transferase !1overproduced in an insecticide-resistant strain of the !1housefly (Musca domestica). !$#cross-references MUID:91287705; PMID:2062307 !$#accession S16293 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-208 ##label WAN !'##cross-references GB:M83249; NID:g159467; PIDN:AAA29294.1; !1PID:g159468 CLASSIFICATION #superfamily glutathione transferase KEYWORDS transferase SUMMARY #length 208 #molecular-weight 23651 #checksum 84 SEQUENCE /// ENTRY S43851 #type complete TITLE glutathione transferase (EC 2.5.1.18) - greenbottle fly (Lucilia cuprina) ORGANISM #formal_name Lucilia cuprina DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S43851 REFERENCE S43851 !$#authors Board, P.; Russell, R.J.; Marano, R.J.; Oakeshott, J.G. !$#journal Biochem. J. (1994) 299:425-430 !$#title Purification, molecular cloning and heterologous expression !1of a glutathione S-transferase from the Australian sheep !1blowfly (Lucilia cuprina). !$#cross-references MUID:94226605; PMID:8172603 !$#accession S43851 !'##status preliminary !'##molecule_type mRNA !'##residues 1-208 ##label BOA !'##cross-references EMBL:L23126; NID:g409145; PIDN:AAA29287.1; !1PID:g409146 CLASSIFICATION #superfamily glutathione transferase KEYWORDS transferase SUMMARY #length 208 #molecular-weight 23715 #checksum 9520 SEQUENCE /// ENTRY XUZM1 #type complete TITLE glutathione transferase (EC 2.5.1.18) I - maize ORGANISM #formal_name Zea mays #common_name maize DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 11-Jun-1999 ACCESSIONS S03726; S00716; S03727 REFERENCE S03726 !$#authors Shah, D.M.; Hironaka, C.M.; Wiegand, R.C.; Harding, E.I.; !1Krivi, G.G.; Tiemeier, D.C. !$#journal Plant Mol. Biol. (1986) 6:203-211 !$#title Structural analysis of a maize gene coding for !1glutathione-S-transferase involved in herbicide !1detoxification. !$#accession S03726 !'##molecule_type DNA !'##residues 1-213 ##label SHA !'##cross-references GB:M16902 REFERENCE S00716 !$#authors Grove, G.; Zarlengo, R.P.; Timmerman, K.P.; Li, N.Q.; Tam, !1M.F.; Tu, C.P.D. !$#journal Nucleic Acids Res. (1988) 16:425-438 !$#title Characterization and heterospecific expression of cDNA !1clones of genes in the maize GSH S-transferase multigene !1family. !$#cross-references MUID:88124246; PMID:3277162 !$#accession S00716 !'##molecule_type mRNA !'##residues 1-14,'L',16-115,'Q',116-213 ##label GRO !'##cross-references GB:X06754; NID:g22314; PIDN:CAA29928.1; PID:g22315 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing GENETICS !$#gene GST-I CLASSIFICATION #superfamily glutathione transferase KEYWORDS dimer; transferase FEATURE !$2-213 #product glutathione transferase #status experimental !8#label MAT SUMMARY #length 213 #molecular-weight 23679 #checksum 5416 SEQUENCE /// ENTRY XUZM31 #type complete TITLE glutathione transferase (EC 2.5.1.18) III (version 1) - maize ORGANISM #formal_name Zea mays #common_name maize DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 11-Jun-1999 ACCESSIONS A24703 REFERENCE A24703 !$#authors Moore, R.E.; Davies, M.S.; O'Connell, K.M.; Harding, E.I.; !1Wiegand, R.C.; Tiemeier, D.C. !$#journal Nucleic Acids Res. (1986) 14:7227-7235 !$#title Cloning and expression of a cDNA encoding a maize !1glutathione-S-transferase in E. coli. !$#cross-references MUID:87016368; PMID:3532034 !$#accession A24703 !'##molecule_type mRNA !'##residues 1-220 ##label MOO !'##cross-references GB:X04375; NID:g22318; PIDN:CAA27957.1; PID:g22319; !1GB:X04455; NID:g22279; PID:g22280 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing GENETICS !$#gene GST-III CLASSIFICATION #superfamily glutathione transferase KEYWORDS dimer; transferase FEATURE !$2-220 #product glutathione transferase #status predicted !8#label MAT SUMMARY #length 220 #molecular-weight 23806 #checksum 5071 SEQUENCE /// ENTRY XUZM32 #type complete TITLE glutathione transferase (EC 2.5.1.18) III (version 2) - maize ORGANISM #formal_name Zea mays #common_name maize DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 11-Jun-1999 ACCESSIONS S00717 REFERENCE S00716 !$#authors Grove, G.; Zarlengo, R.P.; Timmerman, K.P.; Li, N.Q.; Tam, !1M.F.; Tu, C.P.D. !$#journal Nucleic Acids Res. (1988) 16:425-438 !$#title Characterization and heterospecific expression of cDNA !1clones of genes in the maize GSH S-transferase multigene !1family. !$#cross-references MUID:88124246; PMID:3277162 !$#accession S00717 !'##molecule_type mRNA !'##residues 1-222 ##label GRO !'##cross-references EMBL:X06755; NID:g22316; PIDN:CAA29929.1; !1PID:g22317 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing GENETICS !$#gene GST-III CLASSIFICATION #superfamily glutathione transferase KEYWORDS dimer; transferase FEATURE !$2-222 #product glutathione transferase #status experimental !8#label MAT SUMMARY #length 222 #molecular-weight 23849 #checksum 1662 SEQUENCE /// ENTRY A60635 #type complete TITLE glutathione transferase (EC 2.5.1.18), fosfomycin-modifying - Escherichia coli plasmid pSU961 transposon Tn2921 ALTERNATE_NAMES fosfomycin resistance protein ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A60635; A60631 REFERENCE A60635 !$#authors Navas, J.; Leon, J.; Arroyo, M.; Garcia Lobo, J.M. !$#journal Antimicrob. Agents Chemother. (1990) 34:2016-2018 !$#title Nucleotide sequence and intracellular location of the !1product of the fosfomycin resistance gene from transposon !1Tn2921. !$#cross-references MUID:91151067; PMID:1963292 !$#note plasmid pSU961 !$#accession A60635 !'##molecule_type DNA !'##residues 1-141 ##label NAV !'##cross-references GB:M85195; GB:M31685; NID:g154988; PIDN:AAA98399.1; !1PID:g154989 REFERENCE A60631 !$#authors Arca, P.; Hardisson, C.; Suarez, J.E. !$#journal Antimicrob. Agents Chemother. (1990) 34:844-848 !$#title Purification of a glutathione S-transferase that mediates !1fosfomycin resistance in bacteria. !$#cross-references MUID:90297618; PMID:2193621 !$#note plasmid pUC18 !$#accession A60631 !'##molecule_type protein !'##residues 1-9 ##label ARC COMMENT This enzyme inactivates the antibiotic phosphomycin by !1opening the epoxide ring and creating an adduct with !1glutathione. GENETICS !$#genome plasmid CLASSIFICATION #superfamily fosfomycin resistance protein KEYWORDS antibiotic resistance; homodimer; transferase SUMMARY #length 141 #molecular-weight 15959 #checksum 9837 SEQUENCE /// ENTRY E69890 #type complete TITLE glutathione transferase (EC 2.5.1.18) yndN, fosfomycin-modifying - Bacillus subtilis ALTERNATE_NAMES fosfomycin resistance protein ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS E69890 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69890 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-144 ##label KUN !'##cross-references GB:Z99113; GB:AL009126; NID:g2634090; !1PIDN:CAB13668.1; PID:g2634168 !'##experimental_source strain 168 GENETICS !$#gene yndN CLASSIFICATION #superfamily fosfomycin resistance protein KEYWORDS antibiotic resistance; transferase SUMMARY #length 144 #molecular-weight 17172 #checksum 4511 SEQUENCE /// ENTRY B48175 #type complete TITLE glutathione transferase (EC 2.5.1.18), fosfomycin-modifying - Staphylococcus epidermidis ALTERNATE_NAMES fosfomycin resistance protein B ORGANISM #formal_name Staphylococcus epidermidis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B48175 REFERENCE A48175 !$#authors Zilhao, R.; Courvalin, P. !$#journal FEMS Microbiol. Lett. (1990) 68:267-272 !$#title Nucleotide sequence of the fosB gene conferring fosfomycin !1resistance in Staphylococcus epidermidis. !$#accession B48175 !'##status preliminary !'##molecule_type DNA !'##residues 1-139 ##label ZIL !'##cross-references GB:X54227; NID:g46980; PIDN:CAA38136.1; PID:g46982 CLASSIFICATION #superfamily fosfomycin resistance protein KEYWORDS antibiotic resistance; transferase SUMMARY #length 139 #molecular-weight 16363 #checksum 3738 SEQUENCE /// ENTRY XUMUVS #type complete TITLE 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) precursor - Arabidopsis thaliana ALTERNATE_NAMES 5-enolpyruvylshikimate-3-phosphate synthase ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 12-Apr-1996 ACCESSIONS S01061 REFERENCE S01061 !$#authors Klee, H.J.; Muskopf, Y.M.; Gasser, C.S. !$#journal Mol. Gen. Genet. (1987) 210:437-442 !$#title Cloning of an Arabidopsis thaliana gene encoding !15-enolpyruvylshikimate-3-phosphate synthase: sequence !1analysis and manipulation to obtain glyphosate-tolerant !1plants. !$#cross-references MUID:88121718; PMID:3481024 !$#accession S01061 !'##molecule_type DNA !'##residues 1-520 ##label KLE !'##cross-references EMBL:X06613 !'##note the authors translated the codon AGT for residue 195 as Arg COMMENT This enzyme catalyzes the synthesis of O(5)- !1(1-carboxyvinyl)-3-phosphoshikimate from phosphoenolpyruvate !1and 3-phosphoshikimate; this reaction is the sixth step in !1the shikimate pathway, which leads to chorismate and thus to !1aromatic amino acids and related aromatic compounds. GENETICS !$#introns 113/3; 195/2; 246/3; 318/2; 357/3; 428/1; 448/3 CLASSIFICATION #superfamily 3-phosphoshikimate 1-carboxyvinyltransferase; !13-phosphoshikimate 1-carboxyvinyltransferase homology KEYWORDS aromatic amino acid biosynthesis; chloroplast; transferase FEATURE !$1-76 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$77-520 #product 3-phosphoshikimate 1-carboxyvinyltransferase !8#status predicted #label MAT\ !$91-512 #domain 3-phosphoshikimate 1-carboxyvinyltransferase !8homology #label PSK SUMMARY #length 520 #molecular-weight 55723 #checksum 4425 SEQUENCE /// ENTRY XUTOVS #type complete TITLE 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) precursor - tomato ALTERNATE_NAMES 5-enolpyruvylshikimate-3-phosphate synthase; EPSP synthase ORGANISM #formal_name Lycopersicon esculentum #common_name tomato DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 12-Apr-1996 ACCESSIONS B28198 REFERENCE A92711 !$#authors Gasser, C.S.; Winter, J.A.; Hironaka, C.M.; Shah, D.M. !$#journal J. Biol. Chem. (1988) 263:4280-4287 !$#title Structure, expression, and evolution of the !15-enolpyruvylshikimate-3-phosphate synthase genes of petunia !1and tomato. !$#cross-references MUID:88153749; PMID:3346248 !$#accession B28198 !'##molecule_type mRNA !'##residues 1-520 ##label GAS COMMENT This enzyme catalyzes the synthesis of O(5)- !1(1-carboxyvinyl)-3-phosphoshikimate from phosphoenolpyruvate !1and 3-phosphoshikimate; this reaction is the sixth step in !1the shikimate pathway, which leads to chorismate and thus to !1aromatic amino acids and related aromatic compounds. CLASSIFICATION #superfamily 3-phosphoshikimate 1-carboxyvinyltransferase; !13-phosphoshikimate 1-carboxyvinyltransferase homology KEYWORDS aromatic amino acid biosynthesis; chloroplast; transferase FEATURE !$1-76 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$77-520 #product 3-phosphoshikimate 1-carboxyvinyltransferase !8#status predicted #label MAT\ !$91-512 #domain 3-phosphoshikimate 1-carboxyvinyltransferase !8homology #label PSK SUMMARY #length 520 #molecular-weight 55655 #checksum 2525 SEQUENCE /// ENTRY XUPJVS #type complete TITLE 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) precursor - garden petunia ALTERNATE_NAMES 5-enolpyruvylshikimate-3-phosphate synthase; EPSP synthase ORGANISM #formal_name Petunia x hybrida #common_name garden petunia DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 28-May-1999 ACCESSIONS A28198 REFERENCE A92711 !$#authors Gasser, C.S.; Winter, J.A.; Hironaka, C.M.; Shah, D.M. !$#journal J. Biol. Chem. (1988) 263:4280-4287 !$#title Structure, expression, and evolution of the !15-enolpyruvylshikimate-3-phosphate synthase genes of petunia !1and tomato. !$#cross-references MUID:88153749; PMID:3346248 !$#accession A28198 !'##molecule_type mRNA !'##residues 1-516 ##label GAS !'##cross-references GB:M21084; GB:J03227; NID:g169190; PIDN:AAA33699.1; !1PID:g169191 COMMENT This enzyme catalyzes the synthesis of O(5)- !1(1-carboxyvinyl)-3-phosphoshikimate from phosphoenolpyruvate !1and 3-phosphoshikimate; this reaction is the sixth step in !1the shikimate pathway, which leads to chorismate and thus to !1aromatic amino acids and related aromatic compounds. CLASSIFICATION #superfamily 3-phosphoshikimate 1-carboxyvinyltransferase; !13-phosphoshikimate 1-carboxyvinyltransferase homology KEYWORDS aromatic amino acid biosynthesis; chloroplast; transferase FEATURE !$1-72 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$73-516 #product 3-phosphoshikimate 1-carboxyvinyltransferase !8#status predicted #label MAT\ !$87-508 #domain 3-phosphoshikimate 1-carboxyvinyltransferase !8homology #label PSK SUMMARY #length 516 #molecular-weight 55537 #checksum 4175 SEQUENCE /// ENTRY XUECVS #type complete TITLE 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) - Escherichia coli (strain K-12) ALTERNATE_NAMES 5-enolpyruvylshikimate-3-phosphate synthase; EPSP synthase ORGANISM #formal_name Escherichia coli DATE 31-Mar-1990 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS C64830; A30370; S13902; Q00166 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64830 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-427 ##label BLAT !'##cross-references GB:AE000193; GB:U00096; NID:g1787134; !1PIDN:AAC73994.1; PID:g1787137; UWGP:b0908 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A30370 !$#authors Duncan, K.; Lewendon, A.; Coggins, J.R. !$#journal FEBS Lett. (1984) 170:59-63 !$#title The complete amino acid sequence of Escherichia coli !15-enolpyruvylshikimate 3-phosphate synthase. !$#accession A30370 !'##molecule_type DNA !'##residues 1-22,'T',24-329,'R',331-427 ##label DUN !'##cross-references EMBL:X00557; NID:g40965; PIDN:CAA25223.1; !1PID:g40966 REFERENCE S13902 !$#authors Huynh, Q.K. !$#journal Arch. Biochem. Biophys. (1991) 284:407-412 !$#title 5-enolpyruvylshikimate-3-phosphate synthase from Escherichia !1coli - the substrate analogue bromopyruvate inactivates the !1enzyme by modifying cys-408 and lys-411. !$#cross-references MUID:91112841; PMID:1899181 !$#accession S13902 !'##molecule_type protein !'##residues 409-410,'X',412-422 ##label HUY GENETICS !$#gene aroA !$#map_position 20 min FUNCTION !$#description catalyzes the synthesis of O(5)- !1(1-carboxyvinyl)-3-phosphoshikimate from phosphoenolpyruvate !1and 3-phosphoshikimate !$#pathway shikimate pathway !$#note leads to chorismate and to aromatic amino acids and related !1aromatic compounds CLASSIFICATION #superfamily 3-phosphoshikimate 1-carboxyvinyltransferase; !13-phosphoshikimate 1-carboxyvinyltransferase homology KEYWORDS aromatic amino acid biosynthesis; monomer; transferase FEATURE !$14-418 #domain 3-phosphoshikimate 1-carboxyvinyltransferase !8homology #label PSK SUMMARY #length 427 #molecular-weight 46095 #checksum 5776 SEQUENCE /// ENTRY XUEBVS #type complete TITLE 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) - Salmonella typhimurium ALTERNATE_NAMES 5-enolpyruvylshikimate-3-phosphate synthase; EPSP synthase ORGANISM #formal_name Salmonella typhimurium DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 11-Jun-1999 ACCESSIONS A22566 REFERENCE A22566 !$#authors Stalker, D.M.; Hiatt, W.R.; Comai, L. !$#journal J. Biol. Chem. (1985) 260:4724-4728 !$#title A single amino acid substitution in the enzyme !15-enolpyruvylshikimate-3-phosphate synthase confers !1resistance to the herbicide glyphosate. !$#cross-references MUID:85182581; PMID:2985565 !$#accession A22566 !'##molecule_type DNA !'##residues 1-427 ##label STA !'##cross-references GB:M10947; NID:g153875; PIDN:AAA27028.1; !1PID:g153876 !'##note the authors translated the codon CCT for residue 35 as Ala COMMENT The enzyme catalyzes the synthesis of O(5)- !1(1-carboxyvinyl)-3-phosphoshikimate from phosphoenolpyruvate !1and 3-phosphoshikimate; this reaction is the sixth step in !1the shikimate pathway, which leads to chorismate and thus to !1aromatic amino acids and related aromatic compounds. GENETICS !$#gene aroA !$#map_position 19 min CLASSIFICATION #superfamily 3-phosphoshikimate 1-carboxyvinyltransferase; !13-phosphoshikimate 1-carboxyvinyltransferase homology KEYWORDS aromatic amino acid biosynthesis; transferase FEATURE !$14-418 #domain 3-phosphoshikimate 1-carboxyvinyltransferase !8homology #label PSK SUMMARY #length 427 #molecular-weight 46157 #checksum 4952 SEQUENCE /// ENTRY XUEBY #type complete TITLE 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) [validated] - Yersinia enterocolitica ALTERNATE_NAMES 5-enolpyruvylshikimate 3-phosphate synthase; ESPS synthase ORGANISM #formal_name Yersinia enterocolitica DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 21-Jul-2000 ACCESSIONS JQ0131 REFERENCE JQ0130 !$#authors O'Gaora, P.; Maskell, D.; Coleman, D.; Cafferkey, M.; !1Dougan, G. !$#journal Gene (1989) 84:23-30 !$#title Cloning and characterisation of the serC and aroA genes of !1Yersinia enterocolitica, and construction of an aroA mutant. !$#cross-references MUID:90108713; PMID:2691337 !$#accession JQ0131 !'##molecule_type DNA !'##residues 1-427 ##label OGA !'##cross-references GB:M32213; NID:g155521; PIDN:AAA27666.1; !1PID:g155523 !'##experimental_source strain 8081 COMMENT This organism causes a variety of diseases in humans ranging !1from mild gastroenteritis to septicemia. GENETICS !$#gene aroA FUNCTION !$#description EC 2.5.1.19 [validated, MUID:90108713] CLASSIFICATION #superfamily 3-phosphoshikimate 1-carboxyvinyltransferase; !13-phosphoshikimate 1-carboxyvinyltransferase homology KEYWORDS aromatic amino acid biosynthesis; transferase FEATURE !$15-418 #domain 3-phosphoshikimate 1-carboxyvinyltransferase !8homology #label PSK SUMMARY #length 427 #molecular-weight 46303 #checksum 3069 SEQUENCE /// ENTRY XUBRVS #type complete TITLE 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) - Bordetella pertussis ALTERNATE_NAMES 5-enolpyruvylshikimate-3-phosphate synthase; EPSP synthase ORGANISM #formal_name Bordetella pertussis DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 11-Jun-1999 ACCESSIONS A32007 REFERENCE A32007 !$#authors Maskell, D.J.; Morrissey, P.; Dougan, G. !$#journal J. Bacteriol. (1988) 170:2467-2471 !$#title Cloning and nucleotide sequence of the aroA gene of !1Bordetella pertussis. !$#cross-references MUID:88227818; PMID:2897356 !$#accession A32007 !'##molecule_type DNA !'##residues 1-442 ##label DUN !'##cross-references EMBL:M20023; NID:g144036; PIDN:AAA22968.1; !1PID:g144037 COMMENT This enzyme catalyzes the synthesis of O(5)- !1(1-carboxyvinyl)-3-phosphoshikimate from phosphoenolpyruvate !1and 3-phosphoshikimate; this reaction is the sixth step in !1the shikimate pathway, which leads to chorismate and thus to !1aromatic amino acids and related aromatic compounds. GENETICS !$#gene aroA CLASSIFICATION #superfamily 3-phosphoshikimate 1-carboxyvinyltransferase; !13-phosphoshikimate 1-carboxyvinyltransferase homology KEYWORDS aromatic amino acid biosynthesis; transferase FEATURE !$17-432 #domain 3-phosphoshikimate 1-carboxyvinyltransferase !8homology #label PSK SUMMARY #length 442 #molecular-weight 46688 #checksum 1828 SEQUENCE /// ENTRY S46682 #type complete TITLE farnesyl-diphosphate farnesyltransferase (EC 2.5.1.21) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES farnesyltransferase; presqualene-di-diphosphosphate synthase; protein H9998.9; protein YHR190w; squalene synthetase ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 23-Mar-2001 ACCESSIONS S46682; A41113; S19048 REFERENCE S46674 !$#authors Macri, C. !$#submission submitted to the EMBL Data Library, February 1994 !$#description The sequence of S. cerevisiae cosmid 9998. !$#accession S46682 !'##molecule_type DNA !'##residues 1-444 ##label MAC !'##cross-references EMBL:U00030; NID:g458927; PIDN:AAB68360.1; !1PID:g458934; GSPDB:GN00008; MIPS:YHR190w REFERENCE A41113 !$#authors Jennings, S.M.; Tsay, Y.H.; Fisch, T.M.; Robinson, G.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:6038-6042 !$#title Molecular cloning and characterization of the yeast gene for !1squalene synthetase. !$#cross-references MUID:91296756; PMID:2068081 !$#accession A41113 !'##molecule_type DNA !'##residues 1-285,'S',287-444 ##label JEN !'##cross-references GB:M63979; NID:g171480; PIDN:AAA34597.1; !1PID:g171481 REFERENCE S19048 !$#authors Fegueur, M.; Richard, L.; Charles, A.D.; Karst, F. !$#journal Curr. Genet. (1991) 20:365-372 !$#title Isolation and primary structure of the ERG9 gene of !1Saccharomyces cerevisiae encoding squalene synthetase. !$#cross-references MUID:92224278; PMID:1807826 !$#accession S19048 !'##molecule_type DNA !'##residues 1-47,'F',49-319,'D',321-329,'C',331-428,'S',430-444 ##label !1FEG !'##cross-references EMBL:X59959; NID:g3685; PIDN:CAA42583.1; PID:g3686 GENETICS !$#gene SGD:ERG9; MIPS:YHR190w !'##cross-references SGD:S0001233; MIPS:YHR190w !$#map_position 8R CLASSIFICATION #superfamily farnesyl-diphosphate farnesyltransferase KEYWORDS isoprenoid biosynthesis; transferase; transmembrane protein FEATURE !$177-197 #domain transmembrane #status predicted #label TM1\ !$265-285 #domain transmembrane #status predicted #label TM2\ !$291-311 #domain transmembrane #status predicted #label TM3\ !$421-441 #domain transmembrane #status predicted #label TM4 SUMMARY #length 444 #molecular-weight 51719 #checksum 1856 SEQUENCE /// ENTRY JJAG3Z #type complete TITLE trans-zeatin secretion protein - Agrobacterium tumefaciens plasmid pTiT37 CONTAINS dimethylallylpyrophosphate-AMP transferase (EC 2.-.-.-) ORGANISM #formal_name Agrobacterium tumefaciens DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 11-Jun-1999 ACCESSIONS A23000; A05219 REFERENCE A93564 !$#authors Akiyoshi, D.E.; Regier, D.A.; Jen, G.; Gordon, M.P. !$#journal Nucleic Acids Res. (1985) 13:2773-2788 !$#title Cloning and nucleotide sequence of the tzs gene from !1Agrobacterium tumefaciens strain T37. !$#cross-references MUID:85215648; PMID:2987868 !$#accession A23000 !'##molecule_type DNA !'##residues 1-243 ##label AKI !'##cross-references GB:X02423; NID:g39183; PIDN:CAA26275.1; PID:g39184 !'##experimental_source strain T37 COMMENT This protein is reponsible for the secretion of trans-zeatin !1into bacterial culture medium. It also has DMA transferase !1(dimethylallylpyrophosphate-AMP transferase) activity, which !1catalyzes the addition of the dimethylallyl side chain to !1AMP during the initial step in biosynthesis of cytokinins. GENETICS !$#gene tzs !$#genome plasmid CLASSIFICATION #superfamily dimethylallylpyrophosphate-AMP transferase KEYWORDS cytokinin biosynthesis; transferase SUMMARY #length 243 #molecular-weight 27576 #checksum 8968 SEQUENCE /// ENTRY S06738 #type complete TITLE probable adenylate isopentenyltransferase (EC 2.5.1.27) - Agrobacterium rhizogenes plasmid pRiA4 ALTERNATE_NAMES trans-zeatin secretion protein ORGANISM #formal_name Agrobacterium rhizogenes DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S06738 REFERENCE S06738 !$#authors Regier, D.A.; Akiyoshi, D.E.; Gordon, M.P. !$#journal Nucleic Acids Res. (1989) 17:8885 !$#title Nucleotide sequence of the tzs gene from Agrobacterium !1rhizogenes strain A4. !$#cross-references MUID:90067879; PMID:2685753 !$#accession S06738 !'##molecule_type DNA !'##residues 1-243 ##label REG !'##cross-references EMBL:X16380; NID:g38989; PIDN:CAA34417.1; !1PID:g38990 GENETICS !$#gene tzs !$#genome plasmid CLASSIFICATION #superfamily dimethylallylpyrophosphate-AMP transferase KEYWORDS isoprenoid biosynthesis; transferase; transmembrane protein SUMMARY #length 243 #molecular-weight 27727 #checksum 704 SEQUENCE /// ENTRY S06739 #type complete TITLE probable adenylate isopentenyltransferase (EC 2.5.1.27) - Pseudomonas solanacearum ALTERNATE_NAMES trans-zeatin secretion protein ORGANISM #formal_name Pseudomonas solanacearum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S06739 REFERENCE S06739 !$#authors Akiyoshi, D.E.; Regier, D.A.; Gordon, M.P. !$#journal Nucleic Acids Res. (1989) 17:8886 !$#title Nucleotide sequence of the tzs gene from Pseudomonas !1solanacearum strain K60. !$#cross-references MUID:90067880; PMID:2587241 !$#accession S06739 !'##molecule_type DNA !'##residues 1-238 ##label AKI !'##cross-references EMBL:X16381; NID:g45894; PIDN:CAA34418.1; !1PID:g45895 GENETICS !$#gene tzs CLASSIFICATION #superfamily dimethylallylpyrophosphate-AMP transferase KEYWORDS isoprenoid biosynthesis; transferase; transmembrane protein SUMMARY #length 238 #molecular-weight 26440 #checksum 3513 SEQUENCE /// ENTRY A24937 #type complete TITLE probable adenylate isopentenyltransferase (EC 2.5.1.27) ptz - Pseudomonas syringae pv. savastanoi plasmid pck1 ORGANISM #formal_name Pseudomonas syringae pv. savastanoi DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 24-Sep-1999 ACCESSIONS A24937 REFERENCE A24937 !$#authors Powell, G.K.; Morris, R.O. !$#journal Nucleic Acids Res. (1986) 14:2555-2565 !$#title Nucleotide sequence and expression of a Pseudomonas !1savastanoi cytokinin biosynthetic gene: homology with !1Agrobacterium tumefaciens tmr and tzs loci. !$#cross-references MUID:86176749; PMID:3515320 !$#accession A24937 !'##molecule_type DNA !'##residues 1-234 ##label POW !'##cross-references GB:X03679; NID:g45878; PIDN:CAA27315.1; PID:g45879 !'##note the authors translated the codon GAA for residue 211 as Gly !'##note the source is designated as Pseudomonas savastanoi GENETICS !$#gene ptz !$#genome plasmid CLASSIFICATION #superfamily dimethylallylpyrophosphate-AMP transferase KEYWORDS isoprenoid biosynthesis; transferase; transmembrane protein SUMMARY #length 234 #molecular-weight 26810 #checksum 2650 SEQUENCE /// ENTRY JJAGBT #type complete TITLE adenylate isopentenyltransferase (EC 2.5.1.27) - Agrobacterium tumefaciens plasmid pTiBo542 ALTERNATE_NAMES cytokinin synthase; isopentenyl transferase ORGANISM #formal_name Agrobacterium tumefaciens DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 11-Jun-1999 ACCESSIONS S04421 REFERENCE S04421 !$#authors Strabala, T.J.; Bednarek, S.Y.; Bertoni, G.; Amasino, R.M. !$#journal Mol. Gen. Genet. (1989) 216:388-394 !$#title Isolation and characterization of an ipt gene from the Ti !1plasmid Bo542. !$#cross-references MUID:89313678; PMID:2747621 !$#accession S04421 !'##molecule_type DNA !'##residues 1-239 ##label STR !'##cross-references EMBL:X14410; NID:g38689; PIDN:CAA32582.1; !1PID:g38690 GENETICS !$#gene ipt !$#genome plasmid CLASSIFICATION #superfamily dimethylallylpyrophosphate-AMP transferase KEYWORDS cytokinin biosynthesis; transferase SUMMARY #length 239 #molecular-weight 26873 #checksum 7799 SEQUENCE /// ENTRY JJAG3T #type complete TITLE dimethylallylpyrophosphate-AMP transferase (EC 2.-.-.-) - Agrobacterium tumefaciens plasmid pTiT37 ALTERNATE_NAMES DMA transferase ORGANISM #formal_name Agrobacterium tumefaciens DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 11-Jun-1999 ACCESSIONS A00588 REFERENCE A00588 !$#authors Goldberg, S.B.; Flick, J.S.; Rogers, S.G. !$#journal Nucleic Acids Res. (1984) 12:4665-4677 !$#title Nucleotide sequence of the tmr locus of Agrobacterium !1tumefaciens pTi T37 T-DNA. !$#cross-references MUID:84247329; PMID:6330678 !$#accession A00588 !'##molecule_type DNA !'##residues 1-240 ##label GOL !'##cross-references GB:X00639; NID:g944822; PIDN:CAA25268.1; !1PID:g944823 COMMENT The gene that codes for this protein is located in the left !1part of the T-DNA in octopine tumor cells. The protein, !1which catalyzes the addition of the dimethylallyl side chain !1to AMP during the initial step in biosynthesis of !1cytokinins, mediates the growth of Ti plasmid-transformed !1plant cells in the absence of cytokinin, a phytohormone. GENETICS !$#gene tmr !$#genome plasmid CLASSIFICATION #superfamily dimethylallylpyrophosphate-AMP transferase KEYWORDS cytokinin biosynthesis; transferase SUMMARY #length 240 #molecular-weight 27025 #checksum 8077 SEQUENCE /// ENTRY JJAGTT #type complete TITLE adenylate isopentenyltransferase (EC 2.5.1.27) - Agrobacterium tumefaciens plasmid pTiTm-4 ALTERNATE_NAMES cytokinin synthase; isopentenyl transferase ORGANISM #formal_name Agrobacterium tumefaciens DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 11-Jun-1999 ACCESSIONS JE0028; S04422 REFERENCE JE0028 !$#authors Bonnard, G.; Tinland, B.; Paulus, F.; Szegedi, E.; Otten, L. !$#journal Mol. Gen. Genet. (1989) 216:428-438 !$#title Nucleotide sequence, evolutionary origin and biological role !1of a rearranged cytokinin gene isolated from a wide host !1range biotype III Agrobacterium strain. !$#cross-references MUID:89313683; PMID:2546041 !$#accession JE0028 !'##molecule_type DNA !'##residues 1-240 ##label BON !'##cross-references EMBL:X56185; NID:g39133; PIDN:CAA39647.1; !1PID:g39135 GENETICS !$#gene ipt !$#genome plasmid CLASSIFICATION #superfamily dimethylallylpyrophosphate-AMP transferase KEYWORDS cytokinin biosynthesis; transferase SUMMARY #length 240 #molecular-weight 26814 #checksum 6989 SEQUENCE /// ENTRY JJAG5T #type complete TITLE tmr protein - Agrobacterium tumefaciens plasmid pTiAch5 ORGANISM #formal_name Agrobacterium tumefaciens DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 11-Jun-1999 ACCESSIONS A00589; S28690 REFERENCE A00589 !$#authors Heidekamp, F.; Dirkse, W.G.; Hille, J.; van Ormondt, H. !$#journal Nucleic Acids Res. (1983) 11:6211-6223 !$#title Nucleotide sequence of the Agrobacterium tumefaciens !1octopine Ti plasmid-encoded tmr gene. !$#cross-references MUID:84015366; PMID:6312414 !$#accession A00589 !'##molecule_type DNA !'##residues 1-240 ##label HEI !'##cross-references GB:X00010; NID:g39172; PIDN:CAA24911.1; PID:g39173 !'##experimental_source plasmid pTiAch5 REFERENCE S28683 !$#authors Barker, R.F.; Idler, K.B.; Thompson, D.V.; Kemp, J.D. !$#journal Plant Mol. Biol. (1983) 2:335-350 !$#title Nucleotide sequence of the T-DNA region from the !1Agrobacterium tumefaciens octopine Ti plasmid pTi15955. !$#accession S28690 !'##status translation not shown !'##molecule_type DNA !'##residues 1-240 ##label BAR !'##cross-references EMBL:X00493; NID:g39062; PIDN:CAA25170.1; !1PID:g39070 !'##experimental_source plasmid pTi15955 COMMENT The gene that codes for this protein is located in the left !1part of the T-DNA in octopine tumor cells. The protein, !1which may be an enzyme involved in the biosynthesis of !1cytokinins in these cells, mediates the growth of Ti !1plasmid-transformed plant cells in the absence of cytokinin, !1a phytohormone. GENETICS !$#gene tmr !$#genome plasmid CLASSIFICATION #superfamily dimethylallylpyrophosphate-AMP transferase KEYWORDS cytokinin biosynthesis SUMMARY #length 240 #molecular-weight 27004 #checksum 8222 SEQUENCE /// ENTRY XUBYTP #type complete TITLE trans-pentaprenyltranstransferase (EC 2.5.1.33) precursor - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hexaprenyl pyrophosphate synthetase; protein YBR003w; protein YBR0109 ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 01-Feb-2002 ACCESSIONS A36625; S44562; S45854; S45855; S11194; S37324 REFERENCE A36625 !$#authors Ashby, M.N.; Edwards, P.A. !$#journal J. Biol. Chem. (1990) 265:13157-13164 !$#title Elucidation of the deficiency in two yeast coenzyme Q !1mutants. Characterization of the structural gene encoding !1hexaprenyl pyrophosphate synthetase. !$#cross-references MUID:90330660; PMID:2198286 !$#accession A36625 !'##molecule_type DNA !'##residues 1-473 ##label ASH !'##cross-references EMBL:J05547; NID:g171703; PIDN:AAA34686.1; !1PID:g171704 REFERENCE S44556 !$#authors Wolfe, K.H.; Lohan, A.J.E. !$#journal Yeast (1994) 10(Suppl.A):S41-S46 !$#title Sequence around the centromere of Saccharomyces cerevisiae !1chromosome II: similarity of CEN2 to CEN4. !$#cross-references MUID:94378721; PMID:8091860 !$#accession S44562 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-285 ##label WOL !'##cross-references EMBL:Z26494; NID:g403311; PIDN:CAA81272.1; !1PID:g403318 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1September 1993 REFERENCE S45730 !$#authors Lohan, A.J.E.; Wolfe, K.H. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S45854 !'##molecule_type DNA !'##residues 1-285 ##label LOH !'##cross-references EMBL:Z35872; GSPDB:GN00002; MIPS:YBR003w REFERENCE S45816 !$#authors Domdey, H.; Gassenhuber, H.; Obermaier, B.; Piravandi, E. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S45855 !'##molecule_type DNA !'##residues 260-473 ##label DOM !'##cross-references EMBL:Z35872; GSPDB:GN00002; MIPS:YBR003w GENETICS !$#gene SGD:COQ1; MIPS:YBR003w !'##cross-references SGD:S0000207; MIPS:YBR003w !$#map_position 2R CLASSIFICATION #superfamily trans-pentaprenyltranstransferase KEYWORDS ubiquinone biosynthesis; isoprenoid biosynthesis; !1mitochondrion; transferase SUMMARY #length 473 #molecular-weight 52559 #checksum 2512 SEQUENCE /// ENTRY JC4338 #type complete TITLE tryptophan dimethylallyltransferase (EC 2.5.1.34) - ergot fungus ALTERNATE_NAMES dimethylallyl diphosphate:L-tryptophan dimethylallyltransferase; dimethylallyltryptophan synthase ORGANISM #formal_name Claviceps purpurea #common_name ergot fungus DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Dec-1999 ACCESSIONS JC4338 REFERENCE JC4338 !$#authors Tsai, H.F.; Wang, H.; Gebler, J.C.; Poulter, C.D.; Schardl, !1C.L. !$#journal Biochem. Biophys. Res. Commun. (1995) 216:119-125 !$#title The Claviceps purpurea gene encoding dimethylallyltryptophan !1synthase,the committed step for ergot alkaloid biosynthesis. !$#cross-references MUID:96067540; PMID:7488077 !$#accession JC4338 !'##molecule_type mRNA !'##residues 1-455 ##label TSA !'##cross-references GB:L39640; NID:g1005417; PID:g1005418 !'##experimental_source ATCC 26245 GENETICS !$#gene dmaW !$#introns 396/2; 437/1 FUNCTION !$#description catalyzes the synthesis of 4'-(gamma, !1gamma-dimethylallyl)-tryptophan from tryptophan and !1dimethylallyl diphosphate !$#pathway ergot alkaloid biosynthesis CLASSIFICATION #superfamily ergot fungus tryptophan !1dimethylallyltransferase KEYWORDS alkaloid biosynthesis; transferase FEATURE !$113-117 #region prenyl diphosphate binding #status predicted SUMMARY #length 455 #molecular-weight 51857 #checksum 9709 SEQUENCE /// ENTRY A55145 #type complete TITLE thiamine-phosphate diphosphorylase (EC 2.5.1.3) / hydroxyethylthiazole kinase (EC 2.7.1.50) THI6 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein P1785; protein YPL214c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS A55145; S65233 REFERENCE A55145 !$#authors Nosaka, K.; Nishimura, H.; Kawasaki, Y.; Tsujihara, T.; !1Iwashima, A. !$#journal J. Biol. Chem. (1994) 269:30510-30516 !$#title Isolation and characterization of the THI6 gene encoding a !1bifunctional thiamin-phosphate pyrophosphorylase/ !1hydroxyethylthiazole kinase from Saccharomyces cerevisiae. !$#cross-references MUID:95074059; PMID:7982968 !$#accession A55145 !'##molecule_type DNA !'##residues 1-540 ##label NOS !'##cross-references GB:D31908; NID:g633124; PIDN:BAA06703.1; !1PID:g633125 REFERENCE S65202 !$#authors Rieger, M.; Mueller-Auer, S.; Schaefer, M. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S65233 !'##molecule_type DNA !'##residues 1-540 ##label RIE !'##cross-references EMBL:Z73570; NID:g1370443; PIDN:CAA97929.1; !1PID:g1370444; GSPDB:GN00016; MIPS:YPL214c !'##experimental_source strain S288C (AB972) GENETICS !$#gene SGD:THI6; MIPS:YPL214c !'##cross-references SGD:S0006135; MIPS:YPL214c !$#map_position 16 CLASSIFICATION #superfamily yeast thi4 protein; hydroxyethylthiazole kinase !1homology; thiamin-phosphate pyrophosphorylase homology KEYWORDS homooctamer; multifunctional enzyme; phosphotransferase FEATURE !$22-148 #domain thiamin-phosphate pyrophosphorylase homology !8#label THPP\ !$255-448 #domain hydroxyethylthiazole kinase homology #label !8HTK SUMMARY #length 540 #molecular-weight 58058 #checksum 6842 SEQUENCE /// ENTRY S44183 #type complete TITLE thiamine-phosphate diphosphorylase (EC 2.5.1.3) / hydroxyethylthiazole kinase (EC 2.7.1.50) thi4 - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES thi4 protein ORGANISM #formal_name Schizosaccharomyces pombe DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S44183; T38318 REFERENCE S44183 !$#authors Zurlinden, A. !$#submission submitted to the EMBL Data Library, April 1994 !$#accession S44183 !'##status preliminary !'##molecule_type DNA !'##residues 1-518 ##label ZUR !'##cross-references EMBL:X78824; NID:g473356; PIDN:CAA55402.1; !1PID:g473357 REFERENCE Z21733 !$#authors Brown, D.; Churcher, C.M.; Barrell, B.G.; Rajandream, M.A.; !1Wood, V. !$#submission submitted to the EMBL Data Library, September 1997 !$#accession T38318 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-518 ##label BRO !'##cross-references EMBL:Z98977; PIDN:CAB11664.1; GSPDB:GN00066; !1SPDB:SPAC23H4.10c !'##experimental_source strain 972h-; cosmid c23H4 GENETICS !$#gene SPAC23H4.10c !$#map_position 1 CLASSIFICATION #superfamily yeast thi4 protein; hydroxyethylthiazole kinase !1homology; thiamin-phosphate pyrophosphorylase homology KEYWORDS multifunctional enzyme; phosphotransferase FEATURE !$19-142 #domain thiamin-phosphate pyrophosphorylase homology !8#label THPP\ !$246-435 #domain hydroxyethylthiazole kinase homology #label !8HTK SUMMARY #length 518 #molecular-weight 55565 #checksum 6673 SEQUENCE /// ENTRY S35118 #type complete TITLE thiamine-phosphate diphosphorylase (EC 2.5.1.3) thiE - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S35118; D65206 REFERENCE S35117 !$#authors Vander Horn, P.B.; Backstrom, A.D.; Stewart, V.; Begley, !1T.P. !$#journal J. Bacteriol. (1993) 175:982-992 !$#title Structural genes for thiamine biosynthetic enzymes !1(thiCEFGH) in Escherichia coli K-12. !$#cross-references MUID:93163063; PMID:8432721 !$#accession S35118 !'##status preliminary !'##molecule_type DNA !'##residues 1-211 ##label VAN !'##cross-references EMBL:M88701; NID:g1469146; PIDN:AAB95617.1; !1PID:g414233 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65206 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-211 ##label BLAT !'##cross-references GB:AE000473; GB:U00096; NID:g2367336; !1PIDN:AAC76967.1; PID:g1790426; UWGP:b3993 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene thiE CLASSIFICATION #superfamily thiE protein; thiamin-phosphate !1pyrophosphorylase homology KEYWORDS transferase FEATURE !$16-139 #domain thiamin-phosphate pyrophosphorylase homology !8#label THPP SUMMARY #length 211 #molecular-weight 23015 #checksum 4850 SEQUENCE /// ENTRY S39681 #type complete TITLE thiamine-phosphate diphosphorylase (EC 2.5.1.3) thiC - Bacillus subtilis ALTERNATE_NAMES protein ipa-26d ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S39681; E69722 REFERENCE S39655 !$#authors Glaser, P.; Kunst, F.; Arnaud, M.; Coudart, M.P.; Gonzales, !1W.; Hullo, M.F.; Ionescu, M.; Lubochinsky, B.; Marcelino, !1L.; Moszer, I.; Presecan, E.; Santana, M.; Schneider, E.; !1Schweizer, J.; Vertes, A.; Rapoport, G.; Danchin, A. !$#journal Mol. Microbiol. (1993) 10:371-384 !$#title Bacillus subtilis genome project: cloning and sequencing of !1the 97 kb region from 325 degrees to 333 degrees. !$#cross-references MUID:95020537; PMID:7934828 !$#accession S39681 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-222 ##label GLA !'##cross-references EMBL:X73124; NID:g413923; PIDN:CAA51582.1; !1PID:g413950 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1993 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69722 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-222 ##label KUN !'##cross-references GB:Z99123; GB:AL009126; NID:g2636240; !1PIDN:CAB15855.1; PID:g2636364 !'##experimental_source strain 168 GENETICS !$#gene thiC CLASSIFICATION #superfamily thiE protein; thiamin-phosphate !1pyrophosphorylase homology KEYWORDS transferase FEATURE !$23-148 #domain thiamin-phosphate pyrophosphorylase homology !8#label THPP SUMMARY #length 222 #molecular-weight 23681 #checksum 2024 SEQUENCE /// ENTRY S74943 #type complete TITLE thiamine-phosphate diphosphorylase (EC 2.5.1.3) - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein sll0635 CONTAINS thiamin-phosphate pyrophosphorylase (EC 2.5.1.3) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S74943 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74943 !'##status preliminary !'##molecule_type DNA !'##residues 1-343 ##label KAN !'##cross-references EMBL:D90902; GB:AB001339; NID:g1652027; !1PIDN:BAA16983.1; PID:g1652058 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 FUNCTION !$#pathway thiamin biosynthesis CLASSIFICATION #superfamily thiamin biosynthetic bifunctional protein; !1thiamin-phosphate pyrophosphorylase homology KEYWORDS thiamin biosynthesis; transferase FEATURE !$150-273 #domain thiamin-phosphate pyrophosphorylase homology !8#label THPP SUMMARY #length 343 #molecular-weight 37883 #checksum 1364 SEQUENCE /// ENTRY G64977 #type complete TITLE hydroxyethylthiazole kinase (EC 2.7.1.50) - Escherichia coli (strain K-12) ALTERNATE_NAMES hypothetical protein b2104 ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS G64977 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64977 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-262 ##label BLAT !'##cross-references GB:AE000299; GB:U00096; NID:g1788413; !1PIDN:AAC75165.1; PID:g1788421; UWGP:b2104 !'##experimental_source strain K-12, substrain MG1655 FUNCTION !$#description catalyzes the phosphorylation by ATP of 4-methyl-5- !1(2-hydroxyethyl)-thiazole to 4-methyl-5- !1(2-phosphono-oxyethyl)-thiazole !$#pathway thiamin biosynthesis CLASSIFICATION #superfamily hydroxyethylthiazole kinase; !1hydroxyethylthiazole kinase homology KEYWORDS phosphotransferase; thiamin biosynthesis FEATURE !$15-203 #domain hydroxyethylthiazole kinase homology #label !8HTK SUMMARY #length 262 #molecular-weight 27339 #checksum 2475 SEQUENCE /// ENTRY H64151 #type complete TITLE hydroxyethylthiazole kinase (EC 2.7.1.50) - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES hypothetical protein HI0415 ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS H64151 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession H64151 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-265 ##label TIGR !'##cross-references GB:U32725; GB:L42023; NID:g1573387; !1PIDN:AAC22073.1; PID:g1573389; TIGR:HI0415 !'##note best homolog was a hypothetical protein from Bacillus subtilis FUNCTION !$#description catalyzes the phosphorylation by ATP of 4-methyl-5- !1(2-hydroxyethyl)-thiazole to 4-methyl-5- !1(2-phosphono-oxyethyl)-thiazole !$#pathway thiamin biosynthesis CLASSIFICATION #superfamily hydroxyethylthiazole kinase; !1hydroxyethylthiazole kinase homology KEYWORDS phosphotransferase; thiamin biosynthesis FEATURE !$8-197 #domain hydroxyethylthiazole kinase homology #label !8HTK SUMMARY #length 265 #molecular-weight 27733 #checksum 2808 SEQUENCE /// ENTRY S39680 #type complete TITLE hydroxyethylthiazole kinase (EC 2.7.1.50) thiK - Bacillus subtilis ALTERNATE_NAMES protein ipa-25d ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S39680; G69722 REFERENCE S39655 !$#authors Glaser, P.; Kunst, F.; Arnaud, M.; Coudart, M.P.; Gonzales, !1W.; Hullo, M.F.; Ionescu, M.; Lubochinsky, B.; Marcelino, !1L.; Moszer, I.; Presecan, E.; Santana, M.; Schneider, E.; !1Schweizer, J.; Vertes, A.; Rapoport, G.; Danchin, A. !$#journal Mol. Microbiol. (1993) 10:371-384 !$#title Bacillus subtilis genome project: cloning and sequencing of !1the 97 kb region from 325 degrees to 333 degrees. !$#cross-references MUID:95020537; PMID:7934828 !$#accession S39680 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-272 ##label GLA !'##cross-references EMBL:X73124; NID:g413923; PIDN:CAA51581.1; !1PID:g413949 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1993 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69722 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-272 ##label KUN !'##cross-references GB:Z99123; GB:AL009126; NID:g2636240; !1PIDN:CAB15856.1; PID:g2636365 !'##experimental_source strain 168 GENETICS !$#gene thiK FUNCTION !$#description catalyzes the phosphorylation by ATP of 4-methyl-5- !1(2-hydroxyethyl)-thiazole to 4-methyl-5- !1(2-phosphono-oxyethyl)-thiazole !$#pathway thiamin biosynthesis CLASSIFICATION #superfamily hydroxyethylthiazole kinase; !1hydroxyethylthiazole kinase homology KEYWORDS phosphotransferase; thiamin biosynthesis; transmembrane !1protein FEATURE !$10-200 #domain hydroxyethylthiazole kinase homology #label !8HTK SUMMARY #length 272 #molecular-weight 28213 #checksum 2877 SEQUENCE /// ENTRY E64625 #type complete TITLE hydroxyethylthiazole kinase (EC 2.7.1.50) - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS E64625 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession E64625 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-273 ##label TOM !'##cross-references GB:AE000595; GB:AE000511; NID:g2313969; !1PIDN:AAD07891.1; PID:g2313976; TIGR:HP0845 FUNCTION !$#description catalyzes the phosphorylation by ATP of 4-methyl-5- !1(2-hydroxyethyl)-thiazole to 4-methyl-5- !1(2-phosphono-oxyethyl)-thiazole !$#pathway thiamin biosynthesis CLASSIFICATION #superfamily hydroxyethylthiazole kinase; !1hydroxyethylthiazole kinase homology KEYWORDS phosphotransferase; thiamin biosynthesis FEATURE !$16-203 #domain hydroxyethylthiazole kinase homology #label !8HTK SUMMARY #length 273 #molecular-weight 29229 #checksum 2154 SEQUENCE /// ENTRY BVBYA1 #type complete TITLE 3-dehydroquinate synthase (EC 4.2.3.4) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YD9302.02; protein YDR127w CONTAINS 3-dehydroquinate dehydratase (EC 4.2.1.10); 3-dehydroquinate synthase (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19); shikimate 5-dehydrogenase (EC 1.1.1.25); shikimate kinase (EC 2.7.1.71) ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 19-Jul-2002 ACCESSIONS A32519; S51854; S42150; S42151 REFERENCE A32519 !$#authors Duncan, K.; Edwards, R.M.; Coggins, J.R. !$#journal Biochem. J. (1987) 246:375-386 !$#title The pentafunctional AROM enzyme of Saccharomyces cerevisiae !1is a mosaic of monofunctional domains. !$#cross-references MUID:88076802; PMID:2825635 !$#accession A32519 !'##molecule_type DNA !'##residues 1-1588 ##label DUN !'##cross-references EMBL:X06077; NID:g3380; PIDN:CAA29458.1; PID:g3381 REFERENCE S51853 !$#authors Oliver, K.; Harris, D. !$#submission submitted to the EMBL Data Library, February 1995 !$#accession S51854 !'##molecule_type DNA !'##residues 1-1588 ##label OLI !'##cross-references EMBL:Z48179; NID:g665657; PIDN:CAA88208.1; !1PID:g665659; GSPDB:GN00004; MIPS:YDR127w REFERENCE S42150 !$#authors Duncan, K.; Edwards, R.M.; Coggins, J.R. !$#journal FEBS Lett. (1988) 241:83-88 !$#title The Saccharomyces cerevisiae ARO1 gene. An example of the !1co-ordinate regulation of five enzymes on a single !1biosynthetic pathway. !$#cross-references MUID:89065111; PMID:2848727 !$#accession S42150 !'##molecule_type DNA !'##residues 1-44;1557-1588 ##label DUW !'##cross-references EMBL:X13802; EMBL:X13803 GENETICS !$#gene SGD:ARO1; MIPS:YDR127w !'##cross-references SGD:S0002534; MIPS:YDR127w !$#map_position 4R CLASSIFICATION #superfamily aro1 protein; 3-dehydroquinate dehydratase !1homology; 3-dehydroquinate synthase homology; !13-phosphoshikimate 1-carboxyvinyltransferase homology; !1shikimate dehydrogenase homology; shikimate kinase homology KEYWORDS aromatic amino acid biosynthesis; ATP; carbon-oxygen lyase; !1hydro-lyase; multifunctional enzyme; NADP; oxidoreductase; !1phosphorus-oxygen lyase; phosphotransferase FEATURE !$7-380 #domain 3-dehydroquinate synthase homology #label !8DQS\ !$417-863 #domain 3-phosphoshikimate 1-carboxyvinyltransferase !8homology #label PSK\ !$887-1008 #domain shikimate kinase homology #label SKI\ !$1078-1291 #domain 3-dehydroquinate dehydratase homology #label !8DQD\ !$1362-1572 #domain shikimate dehydrogenase homology #label SKD SUMMARY #length 1588 #molecular-weight 174754 #checksum 6266 SEQUENCE /// ENTRY BVASA1 #type complete TITLE 3-dehydroquinate synthase (EC 4.2.3.4) - Emericella nidulans ALTERNATE_NAMES biosynthetic dehydroquinase CONTAINS 3-dehydroquinate dehydratase (EC 4.2.1.10); 3-dehydroquinate synthase (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19); shikimate 5-dehydrogenase (EC 1.1.1.25); shikimate kinase (EC 2.7.1.71) ORGANISM #formal_name Emericella nidulans, Aspergillus nidulans DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 19-Jul-2002 ACCESSIONS A24962; A24042 REFERENCE A24962 !$#authors Charles, I.G.; Keyte, J.W.; Brammar, W.J.; Smith, M.; !1Hawkins, A.R. !$#journal Nucleic Acids Res. (1986) 14:2201-2213 !$#title The isolation and nucleotide sequence of the complex AROM !1locus of Aspergillus nidulans. !$#cross-references MUID:86176723; PMID:3515316 !$#accession A24962 !'##molecule_type DNA !'##residues 1-1603 ##label DUN REFERENCE A24042 !$#authors Charles, I.G.; Keyte, J.W.; Brammar, W.J.; Hawkins, A.R. !$#journal Nucleic Acids Res. (1985) 13:8119-8128 !$#title Nucleotide sequence encoding the biosynthetic dehydroquinase !1function of the penta-functional AROM locus of Aspergillus !1nidulans. !$#cross-references MUID:86067221; PMID:3906567 !$#accession A24042 !'##molecule_type DNA !'##residues 844-1048,'G',1050-1093,'N',1095-1458,'T',1460-1474 ##label !1CHA GENETICS !$#gene aroM CLASSIFICATION #superfamily aro1 protein; 3-dehydroquinate dehydratase !1homology; 3-dehydroquinate synthase homology; !13-phosphoshikimate 1-carboxyvinyltransferase homology; !1shikimate dehydrogenase homology; shikimate kinase homology KEYWORDS aromatic amino acid biosynthesis; ATP; carbon-oxygen lyase; !1hydro-lyase; multifunctional enzyme; NADP; oxidoreductase; !1phosphorus-oxygen lyase; phosphotransferase FEATURE !$7-372 #domain 3-dehydroquinate synthase homology #label !8DQS\ !$407-835 #domain 3-phosphoshikimate 1-carboxyvinyltransferase !8homology #label PSK\ !$863-982 #domain shikimate kinase homology #label SKI\ !$1054-1275 #domain 3-dehydroquinate dehydratase homology #label !8DQD\ !$1344-1567 #domain shikimate dehydrogenase homology #label SKD SUMMARY #length 1603 #molecular-weight 175079 #checksum 7102 SEQUENCE /// ENTRY XNPGDC #type complete TITLE aspartate transaminase (EC 2.6.1.1), cytosolic - pig ALTERNATE_NAMES aspartate aminotransferase, cytosolic; glutamic-oxaloacetic transaminase ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 24-Apr-1984 #sequence_revision 02-Dec-1994 #text_change 11-Jun-1999 ACCESSIONS A30138; A91388; A90287; A00592 REFERENCE A30138 !$#authors Nagashima, F.; Tanase, S.; Fukumoto, Y.; Joh, T.; Nomiyama, !1H.; Tsuzuki, T.; Shimada, K.; Kuramitsu, S.; Kagamiyama, H.; !1Morino, Y. !$#journal Biochemistry (1989) 28:1153-1160 !$#title cDNA cloning and expression of pig cytosolic aspartate !1aminotransferase in Escherichia coli: amino-terminal !1heterogeneity of expressed products and lack of its !1correlation with enzyme function. !$#cross-references MUID:89229121; PMID:2653435 !$#accession A30138 !'##molecule_type mRNA !'##residues 1-413 ##label NAG !'##cross-references GB:M24088; NID:g577493; PIDN:AAA53531.1; !1PID:g577494 !'##experimental_source heart muscle REFERENCE A91388 !$#authors Ovchinnikov, Y.A.; Egorov, T.A.; Aldanova, N.A.; Feigina, !1M.Y.; Lipkin, V.M.; Abdulaev, N.G.; Grishin, E.V.; Kiselev, !1A.P.; Modyanov, N.N.; Braunstein, A.E.; Polyanovsky, O.L.; !1Nosikov, V.V. !$#journal FEBS Lett. (1973) 29:31-34 !$#title The complete amino acid sequence of cytoplasmic aspartate !1aminotransferase from pig heart. !$#accession A91388 !'##molecule_type protein !'##residues 2-144,'D',146-413 ##label OVC !'##experimental_source heart muscle REFERENCE A91776 !$#authors Ovchinnikov, Y.A.; Egorov, T.A.; Aldanova, N.A.; Feigina, !1M.Y.; Lipkin, V.M.; Abdulaev, N.G.; Grishin, E.V.; Kiselev, !1A.P.; Modyanov, N.N.; Braunstein, A.E.; Polyanovsky, O.L.; !1Nosikov, V.V. !$#journal Izv. Akad. Nauk SSSR Ser. Khim. (1974) 1974:1189-1196 !$#title Complete primary structure of cytoplasmic aspartate !1aminotransferase from the pig heart muscle. !$#contents annotation !$#note this paper summarizes the determination of the complete !1sequence and lists references in which the experimental !1details are given REFERENCE A90287 !$#authors Doonan, S.; Doonan, H.J.; Hanford, R.; Vernon, C.A.; Walker, !1J.M.; Airoldi, L.P.S.; Bossa, F.; Barra, D.; Carloni, M.; !1Fasella, P.; Riva, F. !$#journal Biochem. J. (1975) 149:497-506 !$#title The primary structure of aspartate aminotransferase from pig !1heart muscle. Digestion with a proteinase having specificity !1from lysine residues. !$#cross-references MUID:76087776; PMID:1239277 !$#accession A90287 !'##molecule_type protein !'##residues 2-63,'N',65-288,'Q',290-376,'Q',378-413 ##label DOO !'##experimental_source heart muscle !'##note 128-Glx, 158-Ala, 284-Asp, and 348-Trp, as well as a deletion !1of residues 405-407, were also found in some of the !1molecules REFERENCE A91381 !$#authors Polyanovsky, O.L.; Demidkina, T.V.; Egorov, C.A. !$#journal FEBS Lett. (1972) 23:262-264 !$#title The position of an essential tyrosine residue in the !1polypeptide chain of aspartate transaminase. !$#cross-references MUID:73044407; PMID:4634443 !$#contents annotation !$#note in the presence of substrates, Tyr-41 reacts with !1tetranitromethane with concomitant inactivation of the !1enzyme REFERENCE A90558 !$#authors Morino, Y.; Watanabe, T. !$#journal Biochemistry (1969) 8:3412-3417 !$#title Primary structure of pyridoxal phosphate binding site in the !1mitochondrial and extramitochondrial aspartate !1aminotransferases from pig heart muscle. Chymotryptic !1peptides. !$#cross-references MUID:69285398; PMID:5809231 !$#contents annotation; active site COMMENT The molecule is a dimer of identical chains. CLASSIFICATION #superfamily aspartate aminotransferase KEYWORDS aminotransferase; homodimer; phosphoprotein; pyridoxal !1phosphate FEATURE !$2-413 #product aspartate transaminase, cytosolic #status !8experimental #label MAT\ !$259 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status experimental SUMMARY #length 413 #molecular-weight 46474 #checksum 5603 SEQUENCE /// ENTRY XNCHDC #type complete TITLE aspartate transaminase (EC 2.6.1.1), cytosolic - chicken ALTERNATE_NAMES aspartate aminotransferase, cytosolic ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Nov-1980 #sequence_revision 02-Dec-1994 #text_change 11-Jun-1999 ACCESSIONS S05583; S11347; A00593; JN0243 REFERENCE S05583 !$#authors Mattes, U.; Jaussi, R.; Ziak, M.; Juretic, N.; Lindenmann, !1J.M.; Christen, P. !$#journal Biochimie (1989) 71:411-416 !$#title Structure of cDNA of cytosolic aspartate aminotransferase of !1chicken and its expression in E. coli. !$#cross-references MUID:89335814; PMID:2503046 !$#accession S05583 !'##molecule_type DNA !'##residues 1-412 ##label MAT !'##cross-references EMBL:X15636; NID:g63065; PIDN:CAA33646.1; !1PID:g63066 REFERENCE S11346 !$#authors Juretic, N.; Mattes, U.; Ziak, M.; Christen, P.; Jaussi, R. !$#journal Eur. J. Biochem. (1990) 192:119-126 !$#title Structure of the genes of two homologous intracellularly !1heterotopic isoenzymes. Cytosolic and mitochondrial !1aspartate aminotransferase of chicken. !$#cross-references MUID:90382432; PMID:2401287 !$#accession S11347 !'##status preliminary !'##molecule_type DNA !'##residues 1-412 ##label JUR REFERENCE A91272 !$#authors Shlyapnikov, S.V.; Myasnikov, A.N.; Severin, E.S.; Myagkova, !1M.A.; Torchinsky, Y.M.; Braunstein, A.E. !$#journal FEBS Lett. (1979) 106:385-388 !$#title Primary structure of cytoplasmic aspartate aminotransferase !1from chicken heart and its homology with pig heart !1isoenzymes. !$#cross-references MUID:80047259; PMID:499525 !$#accession A00593 !'##molecule_type protein !'##residues 2-62,'N',64-120,122-174,'S',176-231,'N',233,'E',235-412 !1##label SHL REFERENCE JN0243 !$#authors Shlyapnikov, S.V.; Myasnikov, A.N.; Severin, E.S.; Myagkova, !1M.A.; Demidkina, T.V.; Torchinsky, Y.M.; Braunstein, A.E. !$#journal Bioorg. Khim. (1980) 6:876-884 !$#title Primary structure of cytoplasmic aspartate aminotransferase !1from chicken heart IV, Structure of cyanogen bromide !1peptides and the complete amino acid sequence of the !1protein. !$#accession JN0243 !'##molecule_type protein !'##residues 2-62,'N',64-120,122-139,'S',141-174,'S',176-231,'N',233, !1'E',235-412 ##label SH2 !'##experimental_source heart !'##note article in Russian with English abstract REFERENCE A93221 !$#authors Borisov, V.V.; Borisova, S.N.; Sosfenov, N.I.; Vainshtein, !1B.K. !$#journal Nature (1980) 284:189-190 !$#title Electron density map of chicken heart cytosol aspartate !1transaminase at 3.5 angstrom resolution. !$#cross-references MUID:80143195; PMID:7360247 !$#contents annotation; X-ray crystallography, 3.5 angstroms CLASSIFICATION #superfamily aspartate aminotransferase KEYWORDS acetylated amino end; aminotransferase; phosphoprotein; !1pyridoxal phosphate FEATURE !$2-412 #product aspartate transaminase, cytosolic #status !8experimental #label MA1\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental\ !$258 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status experimental SUMMARY #length 412 #molecular-weight 45935 #checksum 2595 SEQUENCE /// ENTRY XNHUDM #type complete TITLE aspartate transaminase (EC 2.6.1.1) precursor, mitochondrial [validated] - human ALTERNATE_NAMES aspartate aminotransferase, mitochondrial; transaminase A ORGANISM #formal_name Homo sapiens #common_name man DATE 28-Feb-1986 #sequence_revision 11-Nov-1994 #text_change 08-Dec-2000 ACCESSIONS A31873; A00594 REFERENCE A31873 !$#authors Pol, S.; Bousquet-Lemercier, B.; Pave-Preux, M.; Pawlak, A.; !1Nalpas, B.; Berthelot, P.; Hanoune, J.; Barouki, R. !$#journal Biochem. Biophys. Res. Commun. (1988) 157:1309-1315 !$#title Nucleotide sequence and tissue distribution of the human !1mitochondrial aspartate aminotransferase mRNA. !$#cross-references MUID:89087454; PMID:3207426 !$#accession A31873 !'##molecule_type mRNA !'##residues 1-430 ##label POL !'##cross-references GB:M22632; NID:g179103; PIDN:AAA35568.1; !1PID:g179104 REFERENCE A00594 !$#authors Martini, F.; Angelaccio, S.; Barra, D.; Pascarella, S.; !1Maras, B.; Doonan, S.; Bossa, F. !$#journal Biochim. Biophys. Acta (1985) 832:46-51 !$#title The primary structure of mitochondrial aspartate !1aminotransferase from human heart. !$#cross-references MUID:86026367; PMID:4052435 !$#accession A00594 !'##molecule_type protein !'##residues 30-109,'EA',112-254,'N',256-304,'Q',306-430 ##label MAR !'##note Val-346 was also found COMMENT The active enzyme is a dimer of identical chains. COMMENT Both isozymes of aspartate aminotransferase are nuclear !1encoded and synthesized in the cytoplasm; this isozyme is !1translocated into the mitochondrion, where a segment is !1cleaved to form the mature enzyme. GENETICS !$#gene GDB:GOT2 !'##cross-references GDB:120009; OMIM:138150 !$#map_position 16q21-16q21 CLASSIFICATION #superfamily aspartate aminotransferase KEYWORDS aminotransferase; homodimer; mitochondrion; phosphoprotein; !1pyridoxal phosphate FEATURE !$1-29 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$30-430 #product aspartate aminotransferase #status !8experimental #label MAT\ !$279 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 430 #molecular-weight 47475 #checksum 2748 SEQUENCE /// ENTRY XNPGDM #type complete TITLE aspartate transaminase (EC 2.6.1.1) precursor, mitochondrial - pig ALTERNATE_NAMES aspartate aminotransferase, mitochondrial ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 31-May-1979 #sequence_revision 02-Dec-1994 #text_change 11-Jun-1999 ACCESSIONS A25165; A92278; A91093; A00595 REFERENCE A25165 !$#authors Joh, T.; Nomiyama, H.; Maeda, S.; Shimada, K.; Morino, Y. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:6065-6069 !$#title Cloning and sequence analysis of a cDNA encoding porcine !1mitochondrial aspartate aminotransferase precursor. !$#cross-references MUID:85298297; PMID:3862118 !$#accession A25165 !'##molecule_type mRNA !'##residues 1-430 ##label JOH !'##cross-references GB:M11732; NID:g164375; PIDN:AAA30999.1; !1PID:g164376 REFERENCE A92278 !$#authors Kagamiyama, H.; Sakakibara, R.; Tanase, S.; Morino, Y.; !1Wada, H. !$#journal J. Biol. Chem. (1980) 255:6153-6159 !$#title Complete amino acid sequence of mitochondrial aspartate !1aminotransferase from pig heart muscle. Peptide ordering !1procedures and the complete sequence. !$#cross-references MUID:80227735; PMID:7391012 !$#accession A92278 !'##molecule_type protein !'##residues 30-70,'D',72-430 ##label KAG !'##experimental_source heart muscle !'##note no disulfide bonds are present REFERENCE A91093 !$#authors Barra, D.; Bossa, F.; Doonan, S.; Fahmy, H.M.A.; Hughes, !1G.J.; Martini, F.; Petruzzelli, R.; Wittmann-Liebold, B. !$#journal Eur. J. Biochem. (1980) 108:405-414 !$#title The cytosolic and mitochondrial aspartate aminotransferases !1from pig heart. A comparison of their primary structures, !1predicted secondary structures and some physical properties. !$#cross-references MUID:81003863; PMID:7408859 !$#accession A91093 !'##molecule_type protein !'##residues 30-304,'Q',306-430 ##label BAR !'##experimental_source heart muscle REFERENCE A91775 !$#authors Barra, D.; Savi, M.R.; Petruzzelli, R.; Bossa, F.; Doonan, !1S. !$#journal Ital. J. Biochem. (1979) 28:478-490 !$#title The primary structure of mitochondrial aspartate !1aminotransferase from pig heart: peptide obtained by !1cleavage with pepsin and with Staphylococcus aureus !1protease. !$#cross-references MUID:81093308; PMID:121997 !$#contents annotation; experimental details !$#note this is the final paper in a series COMMENT The molecule is a dimer of identical chains. CLASSIFICATION #superfamily aspartate aminotransferase KEYWORDS aminotransferase; homodimer; mitochondrion; phosphoprotein; !1pyridoxal phosphate FEATURE !$1-29 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$30-430 #product aspartate aminotransferase, mitochondrial !8#status experimental #label MAT\ !$279 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status experimental SUMMARY #length 430 #molecular-weight 47436 #checksum 5373 SEQUENCE /// ENTRY XNRTDM #type complete TITLE aspartate transaminase (EC 2.6.1.1) precursor, mitochondrial - rat ALTERNATE_NAMES aspartate aminotransferase; glutamic oxaloacetic transaminase; transaminase A ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1981 #sequence_revision 30-Jun-1993 #text_change 01-Dec-2000 ACCESSIONS A28005; A90224; A91964; A60389; I52214; A00596 REFERENCE A28005 !$#authors Mattingly Jr., J.R.; Rodriguez-Berrocal, F.J.; Gordon, J.; !1Iriarte, A.; Martinez-Carrion, M. !$#journal Biochem. Biophys. Res. Commun. (1987) 149:859-865 !$#title Molecular cloning and in vivo expression of a precursor to !1rat mitochondrial aspartate aminotransferase. !$#cross-references MUID:88106546; PMID:3322287 !$#accession A28005 !'##molecule_type mRNA !'##residues 1-430 ##label MATT !'##cross-references GB:M18467; NID:g203009; PIDN:AAB54275.1; !1PID:g203010 REFERENCE A90224 !$#authors Huynh, Q.K.; Sakakibara, R.; Watanabe, T.; Wada, H. !$#journal Biochem. Biophys. Res. Commun. (1980) 97:474-479 !$#title Primary structure of mitochondrial glutamic oxaloacetic !1transaminase from rat liver: comparison with that of the pig !1heart isozyme. !$#cross-references MUID:81133608; PMID:7470110 !$#accession A90224 !'##molecule_type protein !'##residues 30-39,'G',41-161,'G',163-166,'E',168,'A',170-176,'E', !1178-231,'Y',233-235,'N',237-254,'N',256-337,'QG',340-351, !1'G',353-385,'I',387-399,'I',401-430 ##label HUY REFERENCE A91964 !$#authors Huynh, Q.K.; Sakakibara, R.; Watanabe, T.; Wada, H. !$#journal J. Biochem. (1981) 90:863-875 !$#title The complete amino acid sequence of mitochondrial glutamic !1oxaloacetic transaminase from rat liver. !$#cross-references MUID:82075716; PMID:7309704 !$#accession A91964 !'##molecule_type protein !'##residues 30-39,'G',41-161,'G',163-166,'E',168,'A',170-176,'E', !1178-231,'Y',233-235,'N',237-254,'N',256-337,'QG',340-351, !1'G',353-385,'I',387-399,'I',401-430 ##label HUY2 REFERENCE A60389 !$#authors Stump, D.D.; Zhou, S.L.; Potter, B.J.; Berk, P.D. !$#journal Protein Expr. Purif. (1990) 1:49-53 !$#title Purification of rat liver mitochondrial aspartate !1aminotransferase and separation of its isoforms utilizing !1high-performance liquid chromatography. !$#cross-references MUID:93044515; PMID:2152184 !$#accession A60389 !'##molecule_type protein !'##residues 'X',31-32,'X',34-47 ##label STU REFERENCE I52214 !$#authors Horio, Y.; Sakakibara, R.; Tanaka, T.; Taketoshi, M.; Obaru, !1K.; Shimada, K.; Morino, Y.; Wada, H. !$#journal Biochem. Biophys. Res. Commun. (1986) 134:803-811 !$#title Molecular cloning of rat mitochondrial glutamic oxaloacetic !1transaminase mRNA and regulation of its expression in !1regenerating liver. !$#cross-references MUID:86130567; PMID:3004464 !$#accession I52214 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 279-329 ##label RES !'##cross-references GB:M12709; NID:g204450; PIDN:AAA41267.1; !1PID:g204451 CLASSIFICATION #superfamily aspartate aminotransferase KEYWORDS aminotransferase; mitochondrion; phosphoprotein; pyridoxal !1phosphate FEATURE !$1-29 #domain transit peptide (mitochondrion) #status !8predicted #label TSP\ !$30-430 #product aspartate aminotransferase, mitochondrial !8#status experimental #label MAT\ !$279 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status experimental SUMMARY #length 430 #molecular-weight 47314 #checksum 4523 SEQUENCE /// ENTRY XNCHDM #type complete TITLE aspartate transaminase (EC 2.6.1.1) precursor, mitochondrial - chicken ALTERNATE_NAMES mitochondrial aspartate aminotransferase ORGANISM #formal_name Gallus gallus #common_name chicken DATE 25-Feb-1985 #sequence_revision 02-Dec-1994 #text_change 11-Jun-1999 ACCESSIONS A24554; A00597; S29260; S11346 REFERENCE A24554 !$#authors Jaussi, R.; Cotton, B.; Juretic, N.; Christen, P.; !1Schumperli, D. !$#journal J. Biol. Chem. (1985) 260:16060-16063 !$#title The primary structure of the precursor of chicken !1mitochondrial aspartate aminotransferase. Cloning and !1sequence analysis of cDNA. !$#cross-references MUID:86059504; PMID:3840803 !$#accession A24554 !'##molecule_type mRNA !'##residues 1-423 ##label JAU !'##cross-references GB:M12105; NID:g211208; PIDN:AAA48603.1; !1PID:g211209 REFERENCE A00597 !$#authors Graf-Hausner, U.; Wilson, K.J.; Christen, P. !$#journal J. Biol. Chem. (1983) 258:8813-8826 !$#title The covalent structure of mitochondrial aspartate !1aminotransferase from chicken. Identification of segments of !1the polypeptide chain invariant specifically in the !1mitochondrial isoenzyme. !$#cross-references MUID:83238520; PMID:6345546 !$#accession A00597 !'##molecule_type protein !'##residues 23-66,'P',68-167,'E',169-215,'E',217-423 ##label GRA REFERENCE S29260 !$#authors Schmid, D.; Jaussi, R.; Christen, P. !$#journal Eur. J. Biochem. (1992) 208:699-704 !$#title Precursor of mitochondrial aspartate aminotransferase !1synthesized in Escherichia coli is complexed with heat-shock !1protein DnaK. !$#cross-references MUID:93011098; PMID:1396676 !$#accession S29260 !'##molecule_type protein !'##residues 2-25 ##label SCH REFERENCE S11346 !$#authors Juretic, N.; Mattes, U.; Ziak, M.; Christen, P.; Jaussi, R. !$#journal Eur. J. Biochem. (1990) 192:119-126 !$#title Structure of the genes of two homologous intracellularly !1heterotopic isoenzymes. Cytosolic and mitochondrial !1aspartate aminotransferase of chicken. !$#cross-references MUID:90382432; PMID:2401287 !$#accession S11346 !'##molecule_type DNA !'##residues 24-196,'SI',199,'L',201-423 ##label JUR CLASSIFICATION #superfamily aspartate aminotransferase KEYWORDS aminotransferase; homodimer; mitochondrion; phosphoprotein; !1pyridoxal phosphate FEATURE !$1-22 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$23-423 #product aspartate transaminase, mitochondrial !8#status experimental #label MAT\ !$272 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status experimental SUMMARY #length 423 #molecular-weight 47241 #checksum 9118 SEQUENCE /// ENTRY XNECD #type complete TITLE aspartate transaminase (EC 2.6.1.1) aspC [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES aspartate aminotransferase; transaminase A ORGANISM #formal_name Escherichia coli DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 01-Mar-2002 ACCESSIONS A00598; A38045; A29306; G64832 REFERENCE A00598 !$#authors Kuramitsu, S.; Okuno, S.; Ogawa, T.; Ogawa, H.; Kagamiyama, !1H. !$#journal J. Biochem. (1985) 97:1259-1262 !$#title Aspartate aminotransferase of Escherichia coli: nucleotide !1sequence of the aspC gene. !$#cross-references MUID:85289110; PMID:3897210 !$#accession A00598 !'##molecule_type DNA !'##residues 1-396 ##label KUR !'##cross-references GB:X05904; NID:g41012; PIDN:CAA29333.1; PID:g41013 REFERENCE A38045 !$#authors Kondo, K.; Wakabayashi, S.; Yagi, T.; Kagamiyama, H. !$#journal Biochem. Biophys. Res. Commun. (1984) 122:62-67 !$#title The complete amino acid sequence of aspartate !1aminotransferase from Escherichia coli: sequence comparison !1with pig isoenzymes. !$#cross-references MUID:84256832; PMID:6378205 !$#accession A38045 !'##molecule_type protein !'##residues 1-396 ##label KON1 REFERENCE A29306 !$#authors Kondo, K.; Wakabayashi, S.; Kagamiyama, H. !$#journal J. Biol. Chem. (1987) 262:8648-8659 !$#title Structural studies on aspartate aminotransferase from !1Escherichia coli. Covalent structure. !$#cross-references MUID:87250482; PMID:3298240 !$#accession A29306 !'##molecule_type protein !'##residues 1-396 ##label KON2 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64832 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-396 ##label BLAT !'##cross-references GB:AE000195; GB:U00096; NID:g1787156; !1PIDN:AAC74014.1; PID:g1787159; UWGP:b0928 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene aspC !$#map_position 21 min COMPLEX homodimer FUNCTION !$#description catalyzes the reversible transfer of the amino group from !1L-aspartate to 2-oxoglutarate to form oxaloacetate and !1L-glutamate !$#pathway aspartate catabolism !$#note in eukaryotes, there are two isozymes: one is located in the !1mitochondrial matrix, the second is cytoplasmic; in !1prokaryotes, only one form is found CLASSIFICATION #superfamily aspartate aminotransferase KEYWORDS aminotransferase; homodimer; phosphoprotein; pyridoxal !1phosphate FEATURE !$246 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status experimental\ !$374 #binding_site substrate (Arg) #status predicted SUMMARY #length 396 #molecular-weight 43573 #checksum 9894 SEQUENCE /// ENTRY XNYLB #type fragment TITLE aspartate transaminase (EC 2.6.1.1) precursor - narrow-leaved blue lupine (fragment) ALTERNATE_NAMES aspartate aminotransferase ORGANISM #formal_name Lupinus angustifolius #common_name narrow-leaved blue lupine DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 11-Jun-1999 ACCESSIONS S22465; S16741 REFERENCE S22465 !$#authors Reynolds, P.H.S.; Smith, L.A.; Dickson, J.M.J.J.; Jones, !1W.T.; Jones, S.D.; Rodber, K.A.; Carne, A.; Liddane, C.P. !$#journal Plant Mol. Biol. (1992) 19:465-472 !$#title Molecular cloning of a cDNA encoding aspartate !1aminotransferase-P(2) from lupin root nodules. !$#cross-references MUID:92322978; PMID:1623192 !$#accession S22465 !'##molecule_type mRNA !'##residues 1-454 ##label REY !'##cross-references EMBL:X59761; NID:g19138; PIDN:CAA42430.1; !1PID:g19139 CLASSIFICATION #superfamily aspartate aminotransferase KEYWORDS aminotransferase; chloroplast; phosphoprotein; pyridoxal !1phosphate FEATURE !$1-49 #domain transit peptide (chloroplast) (fragment) !8#status predicted #label TNP\ !$50-454 #product aspartate aminotransferase, #status !8predicted #label MAT\ !$299 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 454 #checksum 9286 SEQUENCE /// ENTRY XNECY #type complete TITLE aromatic-amino-acid transaminase (EC 2.6.1.57) tyrB [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES tyrosine aminotransferase CONTAINS tyrosine transaminase (EC 2.6.1.5) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 01-Mar-2002 ACCESSIONS A30379; I52211; I54888; E65213; Q00614 REFERENCE A30379 !$#authors Fotheringham, I.G.; Dacey, S.A.; Taylor, P.P.; Smith, T.J.; !1Hunter, M.G.; Finlay, M.E.; Primrose, S.B.; Parker, D.M.; !1Edwards, R.M. !$#journal Biochem. J. (1986) 234:593-604 !$#title The cloning and sequence analysis of the aspC and tyrB genes !1from Escherichia coli K12. Comparison of the primary !1structures of the aspartate aminotransferase and aromatic !1aminotransferase of E. coli with those of the pig aspartate !1aminotransferase isoenzymes. !$#cross-references MUID:86242111; PMID:3521591 !$#accession A30379 !'##molecule_type DNA !'##residues 1-397 ##label FOT !'##cross-references EMBL:X03629 REFERENCE I52211 !$#authors Kuramitsu, S.; Inoue, K.; Ogawa, T.; Ogawa, H.; Kagamiyama, !1H. !$#journal Biochem. Biophys. Res. Commun. (1985) 133:134-139 !$#title Aromatic amino acid aminotransferase of Escherichia coli !1nucleotide sequence of the tyrB gene. !$#cross-references MUID:86076977; PMID:3907634 !$#accession I52211 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-397 ##label RES !'##cross-references GB:M12047; NID:g148084; PIDN:AAA24703.1; !1PID:g148085 REFERENCE I54888 !$#authors Yang, J.; Pittard, J. !$#journal J. Bacteriol. (1987) 169:4710-4715 !$#title Molecular analysis of the regulatory region of the !1Escherichia coli K-12 tyrB gene. !$#cross-references MUID:88007418; PMID:3308851 !$#accession I54888 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-39 ##label RE2 !'##cross-references GB:M17809; NID:g148086; PIDN:AAA24704.1; !1PID:g551844 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65213 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-397 ##label BLAT !'##cross-references GB:AE000478; GB:U00096; NID:g2367339; !1PIDN:AAC77024.1; PID:g1790488; UWGP:b4054 !'##experimental_source strain K-12, substrain MG1655 COMMENT This pyridoxal phosphate enzyme catalyzes the transamination !1reaction of tyrosine and alpha-ketoglutarate to form !1glutamate. GENETICS !$#gene tyrB !$#map_position 92 min !$#start_codon GTG CLASSIFICATION #superfamily aspartate aminotransferase KEYWORDS aminotransferase; phosphoprotein; pyridoxal phosphate FEATURE !$247 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 397 #molecular-weight 43537 #checksum 5403 SEQUENCE /// ENTRY XNRTY #type complete TITLE tyrosine transaminase (EC 2.6.1.5) - rat ALTERNATE_NAMES tyrosine aminotransferase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 11-Jun-1999 ACCESSIONS A23310; A31804; JN0343; A48430; S18308; S17849 REFERENCE A23310 !$#authors Grange, T.; Guenet, C.; Dietrich, J.B.; Chasserot, S.; !1Fromont, M.; Befort, N.; Jami, J.; Beck, G.; Pictet, R. !$#journal J. Mol. Biol. (1985) 184:347-350 !$#title Complete complementary DNA of rat tyrosine aminotransferase !1messenger RNA. Deduction of the primary structure of the !1enzyme. !$#cross-references MUID:85293103; PMID:2863382 !$#accession A23310 !'##molecule_type mRNA !'##residues 1-454 ##label GRA !'##cross-references EMBL:X02741; NID:g57327; PIDN:CAA26519.1; !1PID:g57328 !'##note part of this sequence was confirmed by protein sequencing REFERENCE A31804 !$#authors Hargrove, J.L.; Scoble, H.A.; Mathews, W.R.; Baumstark, !1B.R.; Biemann, K. !$#journal J. Biol. Chem. (1989) 264:45-53 !$#title The structure of tyrosine aminotransferase. Evidence for !1domains involved in catalysis and enzyme turnover. !$#cross-references MUID:89079691; PMID:2562840 !$#accession A31804 !'##molecule_type mRNA !'##residues 226-284,'G',286-358,'DL',361-444,'D',446-454 ##label HAR !'##cross-references GB:M18340 !'##note the authors translated the codon GGG for residue 285 as Pro !'##note part of this sequence was confirmed by protein sequencing REFERENCE JN0343 !$#authors Zelenin, S.M.; Popova, V.S.; Morozov, I.V.; Tishkav, V.I.; !1Egorov, A.M.; Mertvetsov, N.P. !$#journal Bioorg. Khim. (1991) 17:994-996 !$#title Nucleotide sequence of an EcoRI-fragment of the rat tyrosine !1aminotransferase gene determined on the automated sequencer !1"Applied Biosystems" model 370A. !$#cross-references MUID:92172066; PMID:1686548 !$#accession JN0343 !'##molecule_type DNA !'##residues 385-454 ##label ZEL !'##experimental_source liver REFERENCE A48430 !$#authors Morozov, I.V.; Mishin, V.P.; Zelenin, S.M.; Popova, V.S.; !1Mertvetsov, N.P. !$#journal DNA Seq. (1990) 1:151-155 !$#title Nucleotide sequence of rat liver tyrosine aminotransferase !1gene fragment. !$#cross-references MUID:92190544; PMID:1983704 !$#accession A48430 !'##status preliminary !'##molecule_type DNA !'##residues 190-284,'L',286-386 ##label MOR !'##cross-references GB:X15690; NID:g57845; PIDN:CAA33725.1; !1PID:g1334238 !'##experimental_source liver !'##note sequence extracted from NCBI backbone (NCBIN:89708, !1NCBIP:89709) REFERENCE S18308 !$#authors Lorber, B.; Dietrich, J.B.; Kern, D. !$#journal FEBS Lett. (1991) 291:345-349 !$#title Isolation and characterization of active N-terminal !1truncated apo- and holoenzyme of mammalian liver tyrosine !1aminotransferase. !$#cross-references MUID:92038067; PMID:1682164 !$#accession S18308 !'##molecule_type protein !'##residues 38-52;58-81 ##label LOR !'##experimental_source liver REFERENCE S17849 !$#authors Dietrich, J.B.; Lorber, B.; Kern, D. !$#journal Eur. J. Biochem. (1991) 201:399-407 !$#title Expression of mammalian tyrosine aminotransferase in !1Saccharomyces cerevisiae and Escherichia coli. Purification !1to homogeneity and characterization of the enzyme !1overproduced in the bacteria. !$#cross-references MUID:92037592; PMID:1682148 !$#accession S17849 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1,'V',3-10 ##label DIE !'##experimental_source liver GENETICS !$#introns 408/3 CLASSIFICATION #superfamily mammalian tyrosine aminotransferase KEYWORDS acetylated amino end; aminotransferase; homodimer; !1phosphoprotein; pyridoxal phosphate FEATURE !$383-394 #region PEST sequence\ !$1 #modified_site acetylated amino end (Met) #status !8experimental\ !$280 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status experimental SUMMARY #length 454 #molecular-weight 50635 #checksum 7044 SEQUENCE /// ENTRY XNECHC #type complete TITLE histidinol-phosphate transaminase (EC 2.6.1.9) [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES histidinol-phosphate aminotransferase; imidazolylacetolphosphate aminotransferase ORGANISM #formal_name Escherichia coli DATE 31-Mar-1989 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS D64967; I73527; A30270 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64967 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-356 ##label BLAT !'##cross-references GB:AE000293; GB:U00096; NID:g2367127; !1PIDN:AAC75082.1; PID:g1788332; UWGP:b2021 !'##experimental_source strain K-12, substrain MG1655 REFERENCE I56436 !$#authors Jovanovic, G.; Kostic, T.; Jankovic, M.; Savic, D.J. !$#journal J. Mol. Biol. (1994) 239:433-435 !$#title Nucleotide sequence of the Escherichia coli K-12 histidine !1operon revisited. !$#cross-references MUID:94260549; PMID:8201624 !$#accession I73527 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-356 ##label RES !'##cross-references EMBL:U02071; NID:g509818; PIDN:AAA19743.1; !1PID:g509819 REFERENCE A30270 !$#authors Grisolia, V.; Carlomagno, M.S.; Nappo, A.G.; Bruni, C.B. !$#journal J. Bacteriol. (1985) 164:1317-1323 !$#title Cloning, structure, and expression of the Escherichia coli !1K-12 hisC gene. !$#cross-references MUID:86059230; PMID:2999081 !$#accession A30270 !'##molecule_type DNA !'##residues 1-129,'P',131-148,'A',150-356 ##label GRI !'##cross-references EMBL:X03416; NID:g41694; PIDN:CAA27150.1; !1PID:g41695 GENETICS !$#gene hisC !$#map_position 44 min FUNCTION !$#description EC 2.6.1.9 [validated, MUID:86059230]; catalyzes the !1conversion of imidazolylacetolphosphate to L-histidinol !1phosphate !$#pathway histidine biosynthesis !$#note eighth step CLASSIFICATION #superfamily histidinol-phosphate aminotransferase KEYWORDS aminotransferase; histidine biosynthesis SUMMARY #length 356 #molecular-weight 39360 #checksum 4146 SEQUENCE /// ENTRY XNEBHC #type complete TITLE histidinol-phosphate transaminase (EC 2.6.1.9) - Salmonella typhimurium ALTERNATE_NAMES histidinol-phosphate aminotransferase ORGANISM #formal_name Salmonella typhimurium DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 28-May-1999 ACCESSIONS JS0158 REFERENCE JS0131 !$#authors Carlomagno, M.S.; Chiariotti, L.; Alifano, P.; Nappo, A.G.; !1Bruni, C.B. !$#journal J. Mol. Biol. (1988) 203:585-606 !$#title Structure and function of the Salmonella typhimurium and !1Escherichia coli K-12 histidine operons. !$#cross-references MUID:89094829; PMID:3062174 !$#accession JS0158 !'##molecule_type DNA !'##residues 1-359 ##label CAR !'##cross-references GB:X13464; NID:g47719; PIDN:CAA31824.1; PID:g47723 COMMENT This enzyme catalyzes the conversion of !1imidazolylacetolphosphate to L-histidinol phosphate, the !1eighth step in histidine biosynthesis. GENETICS !$#gene hisC !$#map_position 42 min CLASSIFICATION #superfamily histidinol-phosphate aminotransferase KEYWORDS aminotransferase; histidine biosynthesis SUMMARY #length 359 #molecular-weight 39729 #checksum 1849 SEQUENCE /// ENTRY E64070 #type complete TITLE histidinol-phosphate transaminase (EC 2.6.1.9) - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS E64070 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession E64070 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-367 ##label TIGR !'##cross-references GB:U32730; GB:L42023; NID:g3212191; !1PIDN:AAC22129.1; PID:g1573449; TIGR:HI0470 !'##note named as homolog to a protein from Escherichia coli CLASSIFICATION #superfamily histidinol-phosphate aminotransferase KEYWORDS aminotransferase; histidine biosynthesis SUMMARY #length 367 #molecular-weight 40794 #checksum 1545 SEQUENCE /// ENTRY A48329 #type complete TITLE histidinol-phosphate transaminase (EC 2.6.1.9) - yeast (Candida maltosa) ORGANISM #formal_name Candida maltosa DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A48329 REFERENCE A48329 !$#authors Hikiji, T.; Ohkuma, M.; Takagi, M.; Yano, K. !$#journal Curr. Genet. (1989) 16:261-266 !$#title An improved host-vector system for Candida maltosa using a !1gene isolated from its genome that complements the his5 !1mutation of Saccharomyces cerevisiae. !$#cross-references MUID:90182717; PMID:2697466 !$#accession A48329 !'##status preliminary !'##molecule_type DNA !'##residues 1-389 ##label HIK !'##cross-references GB:X17310; NID:g2604; PIDN:CAA35189.1; PID:g3805888 CLASSIFICATION #superfamily histidinol-phosphate aminotransferase KEYWORDS aminotransferase SUMMARY #length 389 #molecular-weight 43392 #checksum 7009 SEQUENCE /// ENTRY S48456 #type complete TITLE histidinol-phosphate transaminase (EC 2.6.1.9) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YIL116w ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 12-Nov-1999 ACCESSIONS S48456; S05902 REFERENCE S48455 !$#authors Bowman, S.; Churcher, C. !$#submission submitted to the EMBL Data Library, September 1994 !$#accession S48456 !'##molecule_type DNA !'##residues 1-385 ##label BOW !'##cross-references GB:Z47047; EMBL:Z38125; NID:g603997; PID:g763230; !1GSPDB:GN00009; MIPS:YIL116w REFERENCE S05902 !$#authors Nishiwaki, K.; Hayashi, N.; Irie, S.; Chung, D.H.; !1Harashima, S.; Oshima, Y. !$#journal Mol. Gen. Genet. (1987) 208:159-167 !$#title Structure of the yeast HIS5 gene responsive to general !1control of amino acid biosynthesis. !$#cross-references MUID:87286400; PMID:3302607 !$#accession S05902 !'##molecule_type DNA !'##residues 1-109,'RE',113-124,'S',126-141,'I',143-293,'L',295-385 !1##label NIS !'##cross-references EMBL:X05650; NID:g3786; PIDN:CAA29139.1; PID:g3788 GENETICS !$#gene SGD:HIS5; MIPS:YIL116w !'##cross-references SGD:S0001378; MIPS:YIL116w !$#map_position 9L CLASSIFICATION #superfamily histidinol-phosphate aminotransferase KEYWORDS aminotransferase; histidine biosynthesis SUMMARY #length 385 #molecular-weight 42646 #checksum 8838 SEQUENCE /// ENTRY S41584 #type complete TITLE histidinol-phosphate transaminase (EC 2.6.1.9) his3 - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES imidazoleglycerol-phosphate dehydratase ORGANISM #formal_name Schizosaccharomyces pombe DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 18-Feb-2000 ACCESSIONS S41584; T43329 REFERENCE S41584 !$#authors Burke, J.D.; Gould, K.L. !$#journal Mol. Gen. Genet. (1994) 242:169-176 !$#title Molecular cloning and characterization of the !1Schizosaccharomyces pombe his3 gene for use as a selectable !1marker. !$#cross-references MUID:94211206; PMID:8159167 !$#accession S41584 !'##status preliminary !'##molecule_type DNA !'##residues 1-384 ##label BUR !'##cross-references GB:L19523; NID:g431763; PIDN:AAA67316.1; !1PID:g431764 !$#accession T43329 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-384 ##label BU2 !'##cross-references EMBL:L19524; PIDN:AAA86664.1 !'##experimental_source strain 972 GENETICS !$#gene his3 !$#introns 23/2; 27/2; 231/2 FUNCTION !$#pathway histidine biosynthesis CLASSIFICATION #superfamily histidinol-phosphate aminotransferase KEYWORDS aminotransferase; histidine biosynthesis SUMMARY #length 384 #molecular-weight 42733 #checksum 3410 SEQUENCE /// ENTRY JQ0637 #type complete TITLE histidinol-phosphate transaminase (EC 2.6.1.9) - Streptomyces coelicolor ALTERNATE_NAMES histidinol-phosphate aminotransferase; imidazolylacetolphosphate aminotransferase ORGANISM #formal_name Streptomyces coelicolor DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 12-Nov-1999 ACCESSIONS JQ0637; T35082 REFERENCE JQ0637 !$#authors Limauro, D.; Avitabile, A.; Cappellano, C.; Puglia, A.M.; !1Bruni, C.B. !$#journal Gene (1990) 90:31-41 !$#title Cloning and characterization of the histidine biosynthetic !1gene cluster of Streptomyces coelicolor A3(2). !$#cross-references MUID:90337345; PMID:2199329 !$#accession JQ0637 !'##molecule_type DNA !'##residues 1-369 ##label LIM !'##cross-references GB:M31628; NID:g153295; PIDN:AAA26756.1; !1PID:g153297 !'##experimental_source strain A3[2] REFERENCE Z21567 !$#authors Seeger, K.J.; Harris, D.; Bentley, S.D.; Parkhill, J.; !1Barrell, B.G.; Rajandream, M.A. !$#submission submitted to the EMBL Data Library, July 1999 !$#accession T35082 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-369 ##label SEE !'##cross-references EMBL:AL096884; PIDN:CAB51445.1; GSPDB:GN00070; !1SCOEDB:hisC !'##experimental_source strain A3(2) COMMENT This enzyme catalyzes the conversion of !1imidazolylacetophosphate to L-histidinolphosphate. GENETICS !$#gene hisC !$#start_codon GTG CLASSIFICATION #superfamily histidinol-phosphate aminotransferase KEYWORDS aminotransferase; histidine biosynthesis SUMMARY #length 369 #molecular-weight 40387 #checksum 8538 SEQUENCE /// ENTRY XNHUO #type complete TITLE ornithine-oxo-acid transaminase (EC 2.6.1.13) precursor [validated] - human ALTERNATE_NAMES ornithine aminotransferase; ornithine-oxo-acid aminotransferase ORGANISM #formal_name Homo sapiens #common_name man DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 03-Jun-2002 ACCESSIONS A30806; I53424; S05662; A34979; A00599; A25792; I77348; !1I57460 REFERENCE A92670 !$#authors Mitchell, G.A.; Looney, J.E.; Brody, L.C.; Steel, G.; !1Suchanek, M.; Engelhardt, J.F.; Willard, H.F.; Valle, D. !$#journal J. Biol. Chem. (1988) 263:14288-14295 !$#title Human ornithine-delta-aminotransferase. cDNA cloning and !1analysis of the structural gene. !$#cross-references MUID:89008274; PMID:3170546 !$#accession A30806 !'##molecule_type DNA !'##residues 1-439 ##label MIT !'##cross-references EMBL:M23204; NID:g189347; PIDN:AAA36386.1; !1PID:g189348 REFERENCE I53424 !$#authors Zintz, C.B.; Inana, G. !$#journal Exp. Eye Res. (1990) 50:759-770 !$#title Analysis of the human ornithine aminotransferase gene !1family. !$#cross-references MUID:90323157; PMID:2373169 !$#accession I53424 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-439 ##label ZIN !'##cross-references GB:M29927; NID:g189340; PIDN:AAA59957.1; !1PID:g386987 REFERENCE S05662 !$#authors Kobayashi, T.; Nishii, M.; Takagi, Y.; Titani, K.; !1Matsuzawa, T. !$#journal FEBS Lett. (1989) 255:300-304 !$#title Molecular cloning and nucleotide sequence analysis of mRNA !1for human kidney ornithine aminotransferase. An examination !1of ornithine aminotransferase isozymes between liver and !1kidney. !$#cross-references MUID:90005995; PMID:2507357 !$#accession S05662 !'##molecule_type mRNA !'##residues 1-439 ##label KOB !'##cross-references EMBL:Y07511; NID:g34137; PIDN:CAA68809.1; !1PID:g34138 !$#accession A34979 !'##molecule_type protein !'##residues 36-40 ##label KOB2 REFERENCE A00599 !$#authors Inana, G.; Totsuka, S.; Redmond, M.; Dougherty, T.; Nagle, !1J.; Shiono, T.; Ohura, T.; Kominami, E.; Katunuma, N. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:1203-1207 !$#title Molecular cloning of human ornithine aminotransferase mRNA. !$#cross-references MUID:86149273; PMID:3456579 !$#accession A00599 !'##molecule_type mRNA !'##residues 1-439 ##label INA !'##cross-references GB:M12267; NID:g189328; PIDN:AAA59956.1; !1PID:g189329 REFERENCE A25792 !$#authors Ramesh, V.; Shaffer, M.M.; Allaire, J.M.; Shih, V.E.; !1Gusella, J.F. !$#journal DNA (1986) 5:493-501 !$#title Investigation of gyrate atrophy using a cDNA clone for human !1ornithine aminotransferase. !$#cross-references MUID:87132922; PMID:3816496 !$#accession A25792 !'##molecule_type mRNA !'##residues 1-439 ##label RAM1 !'##cross-references GB:M14963; NID:g189350; PIDN:AAA59959.1; !1PID:g189351 REFERENCE A56001 !$#authors Simmaco, M.; John, R.A.; Barra, D.; Bossa, F. !$#journal FEBS Lett. (1986) 199:39-42 !$#title The primary structure of ornithine aminotransferase. !1Identification of active-site sequence and site of !1post-translational proteolysis. !$#cross-references MUID:86164995; PMID:3754226 !$#contents annotation REFERENCE I57460 !$#authors Ramesh, V.; Gusella, J.F.; Shih, V.E. !$#journal Mol. Biol. Med. (1991) 8:81-93 !$#title Molecular pathology of gyrate atrophy of the choroid and !1retina due to ornithine aminotransferase deficiency. !$#cross-references MUID:92048471; PMID:1682785 !$#accession I77348 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 50-53,'K',55-58 ##label RAM2 !'##cross-references GB:S66421; NID:g238718; PIDN:AAB20297.1; !1PID:g238719 !$#accession I57460 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 328-331,'M',333-336 ##label RAM3 !'##cross-references GB:S66418; NID:g238720; PIDN:AAB20298.1; !1PID:g238721 GENETICS !$#gene GDB:OAT !'##cross-references GDB:120246; OMIM:258870 !$#map_position 10q26-10q26 !$#introns 67/1; 142/1; 174/1; 216/3; 257/3; 300/3; 338/3; 387/1 !$#note defects in this gene result in ornithinemia and the eye !1disease gyrate atrophy FUNCTION !$#description catalyzes the reversible transamination of L-ornithine and !12-oxoglutarate to form L-glutamate 5-semialdehyde and !1L-glutamate !$#pathway arginine catabolism !$#note other 2-oxoacids may serve as substrates with L-ornithine CLASSIFICATION #superfamily ornithine-oxo-acid aminotransferase KEYWORDS aminotransferase; arginine catabolism; mitochondrial matrix; !1mitochondrion; phosphoprotein; pyridoxal phosphate FEATURE !$1-25 #domain transit peptide (mitochondrion) #status !8predicted #label TNP1\ !$26-439 #product ornithine aminotransferase, hepatic form !8#status experimental #label MAT1\ !$36-439 #product ornithine-oxo-acid aminotransferase, renal !8form #status experimental #label MAT2\ !$292 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status experimental SUMMARY #length 439 #molecular-weight 48534 #checksum 3547 SEQUENCE /// ENTRY XNMSO #type complete TITLE ornithine-oxo-acid transaminase (EC 2.6.1.13) precursor - mouse ALTERNATE_NAMES ornithine aminotransferase; ornithine-oxo-acid aminotransferase ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 03-Jun-2002 ACCESSIONS S19937 REFERENCE S19937 !$#authors Manenti, G.; Gariboldi, M.; Pierotti, M.A.; Della Porta, G.; !1Dragani, T.A. !$#submission submitted to the EMBL Data Library, March 1992 !$#description Elevated ornithine amino transferase expression in !1transplanted murine hepatocellular tumors. !$#accession S19937 !'##molecule_type mRNA !'##residues 1-439 ##label MAN !'##cross-references EMBL:X64837; NID:g53458; PIDN:CAA46049.1; !1PID:g53459 GENETICS !$#gene Oat !$#map_position Y CLASSIFICATION #superfamily ornithine-oxo-acid aminotransferase KEYWORDS aminotransferase; arginine catabolism; mitochondrion; !1phosphoprotein; pyridoxal phosphate FEATURE !$1-35 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$36-439 #product ornithine-oxo-acid aminotransferase #status !8predicted #label MAT\ !$292 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 439 #molecular-weight 48354 #checksum 1490 SEQUENCE /// ENTRY XNRTO #type complete TITLE ornithine-oxo-acid transaminase (EC 2.6.1.13) precursor - rat ALTERNATE_NAMES ornithine aminotransferase; ornithine-oxo-acid aminotransferase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 03-Jun-2002 ACCESSIONS A00600; B30806; JX0121; JQ1351; S28952; S28953 REFERENCE A00600 !$#authors Mueckler, M.M.; Pitot, H.C. !$#journal J. Biol. Chem. (1985) 260:12993-12997 !$#title Sequence of the precursor to rat ornithine aminotransferase !1deduced from a cDNA clone. !$#cross-references MUID:86033730; PMID:3840476 !$#accession A00600 !'##molecule_type mRNA !'##residues 1-439 ##label MUE !'##cross-references GB:M11842; NID:g205869; PIDN:AAA41766.1; !1PID:g205870 REFERENCE A92670 !$#authors Mitchell, G.A.; Looney, J.E.; Brody, L.C.; Steel, G.; !1Suchanek, M.; Engelhardt, J.F.; Willard, H.F.; Valle, D. !$#journal J. Biol. Chem. (1988) 263:14288-14295 !$#title Human ornithine-delta-aminotransferase. cDNA cloning and !1analysis of the structural gene. !$#cross-references MUID:89008274; PMID:3170546 !$#accession B30806 !'##molecule_type mRNA !'##residues 1-439 ##label MIT !'##cross-references EMBL:M23204 REFERENCE JX0121 !$#authors Oyama, R.; Suzuki, M.; Matsuzawa, T.; Titani, K. !$#journal J. Biochem. (1990) 108:133-138 !$#title Complete amino acid sequence of rat kidney ornithine !1aminotransferase: identity with liver ornithine !1aminotransferase. !$#cross-references MUID:91035318; PMID:2229004 !$#accession JX0121 !'##molecule_type protein !'##residues 36-439 ##label OYA !'##experimental_source kidney REFERENCE JQ1351 !$#authors Shull, J.D.; Pennington, K.L.; George, S.M.; Kilibarda, K.A. !$#journal Gene (1991) 104:203-209 !$#title The ornithine aminotransferase-encoding gene family of rat: !1cloning, characterization, and evolutionary relationships !1between a single expressed gene and three pseudogenes. !$#cross-references MUID:92009214; PMID:1916291 !$#accession JQ1351 !'##status translation not shown !'##molecule_type DNA !'##residues 1-439 ##label SHU REFERENCE S28952 !$#authors Shull, J.D.; Pennington, K.L.; Pitot, H.C.; Boryca, V.S.; !1Schulte, B.L. !$#journal Biochim. Biophys. Acta (1992) 1132:214-218 !$#title Isolation and characterization of the rat gene encoding !1ornithine aminotransferase. !$#cross-references MUID:93003328; PMID:1390894 !$#accession S28952 !'##status translation not shown !'##molecule_type DNA !'##residues 1-97 ##label SH2 !'##cross-references EMBL:M93295 !$#accession S28953 !'##status translation not shown !'##molecule_type DNA !'##residues 217-439 ##label SH3 !'##cross-references EMBL:M93301; NID:g206703; PIDN:AAA42061.1; !1PID:g206706 COMMENT Ornithine amino transferase is a mitochondrial matrix enzyme !1that catalyzes the interconvertion of L-ornithine and !1L-delta 1-pyrroline-5-carboxylic acid. GENETICS !$#introns 67/1; 257/3; 300/3; 338/3; 387/1 CLASSIFICATION #superfamily ornithine-oxo-acid aminotransferase KEYWORDS aminotransferase; arginine catabolism; mitochondrial matrix; !1mitochondrion; phosphoprotein; pyridoxal phosphate FEATURE !$1-35 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$36-439 #product ornithine-oxo-acid aminotransferase #status !8experimental #label MAT\ !$292 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 439 #molecular-weight 48332 #checksum 1373 SEQUENCE /// ENTRY A48515 #type complete TITLE ornithine-oxo-acid transaminase (EC 2.6.1.13) - moth bean ALTERNATE_NAMES ornithine delta-aminotransferase ORGANISM #formal_name Vigna aconitifolia #common_name moth bean DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS A48515 REFERENCE A48515 !$#authors Delauney, A.J.; Hu, C.A.A.; Kishor, P.B.K.; Verma, D.P.S. !$#journal J. Biol. Chem. (1993) 268:18673-18678 !$#title Cloning of ornithine delta-aminotransferase cDNA from Vigna !1aconitifolia by trans-complementation in Escherichia coli !1and regulation of proline biosynthesis. !$#cross-references MUID:93366777; PMID:8103048 !$#accession A48515 !'##status preliminary !'##molecule_type mRNA !'##residues 1-426 ##label DEL !'##cross-references GB:L08400; NID:g170639; PIDN:AAA02916.1; !1PID:g170640 CLASSIFICATION #superfamily ornithine-oxo-acid aminotransferase KEYWORDS aminotransferase; phosphoprotein; pyridoxal phosphate FEATURE !$291 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 426 #molecular-weight 48139 #checksum 1570 SEQUENCE /// ENTRY XNBYO #type complete TITLE ornithine-oxo-acid transaminase (EC 2.6.1.13) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES ornithine aminotransferase; ornithine-oxo-acid aminotransferase; protein L9753.2; protein YLR438w ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1991 #sequence_revision 23-Feb-1996 #text_change 03-Jun-2002 ACCESSIONS S59406; S00181; S05827 REFERENCE S59401 !$#authors Du, Z. !$#submission submitted to the EMBL Data Library, February 1995 !$#description The sequence of S. cerevisiae cosmid 9753. !$#accession S59406 !'##molecule_type DNA !'##residues 1-424 ##label DUZ !'##cross-references EMBL:U21094; NID:g665967; PIDN:AAB67514.1; !1PID:g665969; GSPDB:GN00012; MIPS:YLR438w !'##experimental_source strain S288C (AB972) REFERENCE S00181 !$#authors Degols, G. !$#journal Eur. J. Biochem. (1987) 169:193-200 !$#title Functional analysis of the regulatory region adjacent to the !1cargB gene of Saccharomyces cerevisiae: nucleotide sequence, !1gene fusion experiments and cis-dominant regulatory mutation !1analysis. !$#cross-references MUID:88055042; PMID:2824201 !$#accession S00181 !'##molecule_type DNA !'##residues 1-6,8-37,'L',39-98,'S',100-211,'R',213-384,'Q',386-424 !1##label DEG !'##cross-references EMBL:X06790; NID:g3459; PIDN:CAA29947.1; PID:g3460 REFERENCE S05827 !$#authors Degols, G.; Jauniaux, J.C.; Wiame, J.M. !$#journal Eur. J. Biochem. (1987) 165:289-296 !$#title Molecular characterization of !1transposable-element-associated mutations that lead to !1constitutive L-ornithine aminotransferase expression in !1Saccharomyces cerevisiae. !$#cross-references MUID:87246605; PMID:3036506 !$#accession S05827 !'##molecule_type DNA !'##residues 1-6,8-37,'L',39-55 ##label DE2 !'##cross-references EMBL:X05571; NID:g3453; PIDN:CAA29081.1; PID:g3454 !'##note in the authors' translation residues 38-40 are duplicated and, !1consequently, residues 41-49 are displaced three codons to !1the right and residues 50-52 are lacking GENETICS !$#gene SGD:CAR2; CARGB; MIPS:YLR438w !'##cross-references SGD:S0004430; MIPS:YLR438w !$#map_position 12R CLASSIFICATION #superfamily ornithine-oxo-acid aminotransferase KEYWORDS aminotransferase; arginine catabolism; phosphoprotein; !1pyridoxal phosphate FEATURE !$272 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 424 #molecular-weight 46086 #checksum 6297 SEQUENCE /// ENTRY XNECDP #type complete TITLE adenosylmethionine-8-amino-7-oxononanoate transaminase (EC 2.6.1.62) bioA [similarity] - Escherichia coli (strain K-12) ALTERNATE_NAMES 7,8-diaminononanoate aminotransferase; adenosylmethionine-8-amino-7-oxononanoate aminotransferase; DAPA aminotransferase ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 17-Oct-1997 #text_change 03-Jun-2002 ACCESSIONS F64813; A32025 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64813 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-429 ##label BLAT !'##cross-references GB:AE000180; GB:U00096; NID:g1786988; !1PIDN:AAC73861.1; PID:g1786991; UWGP:b0774 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A32025 !$#authors Otsuka, A.J.; Buoncristiani, M.R.; Howard, P.K.; Flamm, J.; !1Johnson, C.; Yamamoto, R.; Uchida, K.; Cook, C.; Ruppert, !1J.; Matsuzaki, J. !$#journal J. Biol. Chem. (1988) 263:19577-19585 !$#title The Escherichia coli biotin biosynthetic enzyme sequences !1predicted from the nucleotide sequence of the bio operon. !$#cross-references MUID:89066784; PMID:3058702 !$#accession A32025 !'##molecule_type DNA !'##residues 1-98,'SGRNA',103-429 ##label OTS !'##cross-references GB:J04423; NID:g145422; PIDN:AAA23514.1; !1PID:g457106 GENETICS !$#gene bioA !$#map_position 17 min COMPLEX homodimer CLASSIFICATION #superfamily ornithine-oxo-acid aminotransferase KEYWORDS aminotransferase; biotin biosynthesis; homodimer; !1phosphoprotein; pyridoxal phosphate FEATURE !$274 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 429 #molecular-weight 47335 #checksum 8381 SEQUENCE /// ENTRY JC5005 #type complete TITLE adenosylmethionine-8-amino-7-oxononanoate transaminase (EC 2.6.1.62) - Erwinia herbicola ALTERNATE_NAMES 7,8-diaminononanoate aminotransferase; adenosylmethionine-8-amino-7-oxononanoate aminotransferase; DAPA aminotransferase ORGANISM #formal_name Erwinia herbicola DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS JC5005 REFERENCE JC5005 !$#authors Wu, C.H.; Chen, H.Y.; Shiuan, D. !$#journal Gene (1996) 174:251-258 !$#title Isolation and characterization of the Erwinia herbicola bio !1operon and the sequences of the bioA and bioB genes. !$#cross-references MUID:97045821; PMID:8890743 !$#accession JC5005 !'##molecule_type DNA !'##residues 1-429 ##label WUA !'##cross-references GB:U38519; NID:g1228109; PIDN:AAC44533.1; !1PID:g1228110 !'##note the authors translated the codon ACC for residue 249 as Ile and !1AGC for residue 297 as Ser GENETICS !$#gene bioA COMPLEX homodimer containing pyridoxal phosphate. CLASSIFICATION #superfamily ornithine-oxo-acid aminotransferase KEYWORDS aminotransferase; biotin biosynthesis; phosphoprotein; !1pyridoxal phosphate FEATURE !$274 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 429 #molecular-weight 46945 #checksum 6204 SEQUENCE /// ENTRY XNBYGM #type complete TITLE glutamine-fructose-6-phosphate transaminase (isomerizing) (EC 2.6.1.16) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES glutamine-fructose-6-phosphate aminotransferase (isomerizing); protein YKL104c; protein YKL457 ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1991 #sequence_revision 02-May-1994 #text_change 19-Jul-2002 ACCESSIONS S37931; S39100; A33704; S05736 REFERENCE S37920 !$#authors Cheret, G.; Fukuhara, H.; Bolotin-Fukuhara, M.; !1Daignan-Fornier, B.; Pallier, C.; Puzos, V.; Valens, M. !$#submission submitted to the Protein Sequence Database, March 1994 !$#accession S37931 !'##molecule_type DNA !'##residues 1-717 ##label CHR !'##cross-references EMBL:Z28104; NID:g486174; PIDN:CAA81944.1; !1PID:g486175; GSPDB:GN00011; MIPS:YKL104c !'##experimental_source strain S288C REFERENCE S39094 !$#authors Cheret, G.; Pallier, C.; Valens, M.; Daignan-Fornier, B.; !1Fukuhara, H.; Bolotin-Fukuhara, M.; Sor, F. !$#journal Yeast (1993) 9:1259-1265 !$#title The DNA sequence analysis of the HAP4-LAP4 region on !1chromosome XI of Saccharomyces cerevisiae suggests the !1presence of a second aspartate aminotransferase gene in !1yeast. !$#cross-references MUID:94152173; PMID:8109175 !$#accession S39100 !'##status translation not shown !'##molecule_type DNA !'##residues 1-717 ##label CHE !'##cross-references EMBL:X71133; NID:g431205; PIDN:CAA50453.1; !1PID:g431212 !'##experimental_source strain S288C REFERENCE A33704 !$#authors Watzele, G.; Tanner, W. !$#journal J. Biol. Chem. (1989) 264:8753-8758 !$#title Cloning of the glutamine: fructose-6-phosphate !1amidotransferase gene from yeast. Pheromonal regulation of !1its transcription. !$#cross-references MUID:89255339; PMID:2656689 !$#accession A33704 !'##molecule_type DNA !'##residues 1-452,'HC',455-532,534-717 ##label WAT !'##cross-references EMBL:J04719; NID:g171595; PIDN:AAA34643.1; !1PID:g171596 GENETICS !$#gene SGD:GFA1; MIPS:YKL104c !'##cross-references SGD:S0001587; MIPS:YKL104c !$#map_position 11L FUNCTION !$#description catalyzes the formation of D-glucosamine-6-phosphate from !1the amido group of L-glutamine and fructose-6-phosphate !$#pathway glucosamine biosynthesis !$#note glucosamine-6-phosphate is used in the biosynthesis of amino !1sugars of asparagine-linked oligosaccharide chains in !1glycoproteins and, in some organisms, in the biosynthesis of !1chitin CLASSIFICATION #superfamily glutamine-fructose-6-phosphate aminotransferase !1(isomerizing) KEYWORDS aminotransferase; intramolecular oxidoreductase; isomerase FEATURE !$2-717 #product glutamine-fructose-6-phosphate transaminase !8(isomerizing) #status predicted #label MAT\ !$2 #active_site Cys #status predicted SUMMARY #length 717 #molecular-weight 80046 #checksum 2096 SEQUENCE /// ENTRY XNECGM #type complete TITLE glutamine-fructose-6-phosphate transaminase (isomerizing) (EC 2.6.1.16) - Escherichia coli (strain K-12) ALTERNATE_NAMES glucosamine-6-phosphate synthase; glucosaminephosphate isomerase (glutamine-forming); glutamine-fructose-6-phosphate aminotransferase (isomerizing); hexosephosphate aminotransferase ORGANISM #formal_name Escherichia coli DATE 31-Mar-1990 #sequence_revision 17-Oct-1997 #text_change 19-Jul-2002 ACCESSIONS B65176; A30389; I41219; S17839; Q90513 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65176 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-609 ##label BLAT !'##cross-references GB:AE000450; GB:U00096; NID:g1790166; !1PIDN:AAC76752.1; PID:g1790167; UWGP:b3729 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A30389 !$#authors Walker, J.E.; Gay, N.J.; Saraste, M.; Eberle, A.N. !$#journal Biochem. J. (1984) 224:799-815 !$#title DNA sequence around the Escherichia coli unc operon. !1Completion of the sequence of a 17 kilobase segment !1containing asnA, oriC, unc, glmS and phoS. !$#cross-references MUID:85121806; PMID:6395859 !$#accession A30389 !'##molecule_type DNA !'##residues 1-418,'NV',421-609 ##label WAL !'##cross-references GB:X01631; NID:g43256; PIDN:CAA25785.1; PID:g43268 REFERENCE I41219 !$#authors McKown, R.L.; Orle, K.A.; Chen, T.; Craig, N.L. !$#journal J. Bacteriol. (1988) 170:352-358 !$#title Sequence requirements of Escherichia coli attTn7, a specific !1site of transposon Tn7 insertion. !$#cross-references MUID:88086894; PMID:2826397 !$#accession I41219 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 597-609 ##label RES !'##cross-references GB:M18980; NID:g146074; PIDN:AAA23836.1; !1PID:g146075 REFERENCE S17839 !$#authors Golinelli-Pimpaneau, B.; Badet, B. !$#journal Eur. J. Biochem. (1991) 201:175-182 !$#title Possible involvement of Lys603 from Escherichia coli !1glucosamine-6-phosphate synthase in the binding of its !1substrate fructose 6-phosphate. !$#cross-references MUID:92007872; PMID:1915361 !$#accession S17839 !'##molecule_type protein !'##residues 49-50,'X',52-53;218;219,220-223,'X', !1225-231;489-493;504-508;'K';'K';601-609 ##label GOL GENETICS !$#gene glmS !$#map_position 4 min FUNCTION !$#description catalyzes the formation of D-glucosamine-6-phosphate from !1the amido group of L-glutamine and fructose-6-phosphate !$#pathway glucosamine biosynthesis !$#note glucosamine-6-phosphate is used in the biosynthesis of amino !1sugars of asparagine-linked oligosaccharide chains in !1glycoproteins and, in some organisms, in the biosynthesis of !1chitin CLASSIFICATION #superfamily glutamine-fructose-6-phosphate aminotransferase !1(isomerizing) KEYWORDS aminotransferase; intramolecular oxidoreductase; isomerase FEATURE !$2-609 #product glutamine-fructose-6-phosphate transaminase !8(isomerizing) #status predicted #label MAT\ !$2 #active_site Cys #status predicted SUMMARY #length 609 #molecular-weight 66894 #checksum 9756 SEQUENCE /// ENTRY S01040 #type complete TITLE glutamine-fructose-6-phosphate transaminase (isomerizing) (EC 2.6.1.16) - Rhizobium leguminosarum bv. viciae plasmid pRL1JI ALTERNATE_NAMES nodulation protein nodM ORGANISM #formal_name Rhizobium leguminosarum bv. viciae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jul-2002 ACCESSIONS S01040 REFERENCE S01039 !$#authors Surin, B.P.; Downie, J.A. !$#journal Mol. Microbiol. (1988) 2:173-183 !$#title Characterization of the Rhizobium leguminosarum genes nodLMN !1involved in efficient host-specific nodulation. !$#cross-references MUID:88246045; PMID:3132583 !$#accession S01040 !'##molecule_type DNA !'##residues 1-608 ##label SUR !'##cross-references EMBL:Y00548; NID:g46212; PIDN:CAA68626.1; !1PID:g46221 GENETICS !$#gene nodM !$#genome plasmid pRL1JI CLASSIFICATION #superfamily glutamine-fructose-6-phosphate aminotransferase !1(isomerizing) KEYWORDS aminotransferase; intramolecular oxidoreductase; isomerase; !1nodulation FEATURE !$2-608 #product glutamine-fructose-6-phosphate transaminase !8(isomerizing) #status predicted #label MAT\ !$2 #active_site Cys #status predicted SUMMARY #length 608 #molecular-weight 65794 #checksum 2437 SEQUENCE /// ENTRY JQ0197 #type complete TITLE 4-aminobutyrate transaminase (EC 2.6.1.19) - Emericella nidulans ALTERNATE_NAMES 4-aminobutyrate aminotransferase ORGANISM #formal_name Emericella nidulans, Aspergillus nidulans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 24-Sep-1999 ACCESSIONS JQ0197; S04395 REFERENCE JQ0197 !$#authors Richardson, I.B.; Hurley, S.K.; Hynes, M.J. !$#journal Mol. Gen. Genet. (1989) 217:118-125 !$#title Cloning and molecular characterisation of the amdR !1controlled gatA gene of Aspergillus nidulans. !$#cross-references MUID:89364674; PMID:2505051 !$#accession JQ0197 !'##molecule_type DNA !'##residues 1-498 ##label RIC !'##cross-references GB:X15647; NID:g2345; PIDN:CAA33674.1; PID:g2346 GENETICS !$#gene gatA !$#introns 84/2; 96/2; 484/1 CLASSIFICATION #superfamily 4-aminobutyrate transaminase KEYWORDS aminotransferase; phosphoprotein; pyridoxal phosphate FEATURE !$356 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 498 #molecular-weight 55489 #checksum 7021 SEQUENCE /// ENTRY JQ0507 #type complete TITLE adenosylmethionine-8-amino-7-oxononanoate transaminase (EC 2.6.1.62) - Bacillus sphaericus ALTERNATE_NAMES 7,8-diaminononanoate aminotransferase DAPA aminotransferase; adenosylmethionine-8-amino-7-oxononanoate aminotransferase ORGANISM #formal_name Bacillus sphaericus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS JQ0507 REFERENCE JQ0506 !$#authors Gloeckler, R.; Ohsawa, I.; Speck, D.; Ledoux, C.; Bernard, !1S.; Zinsius, M.; Villeval, D.; Kisou, T.; Kamogawa, K.; !1Lemoine, Y. !$#journal Gene (1990) 87:63-70 !$#title Cloning and characterization of the Bacillus sphaericus !1genes controlling the bioconversion of pimelate into !1dethiobiotin. !$#cross-references MUID:90236299; PMID:2110099 !$#accession JQ0507 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-455 ##label GLO !'##cross-references GB:M29292; NID:g142587; PIDN:AAB02325.1; !1PID:g142589 !'##experimental_source strain IFO3525 COMMENT The enzyme catalyzes the condensation of !18-amino-7-oxononanoate and S-adenosyl-L-methionine to form !17,8-diaminononanoate. GENETICS !$#gene bioA !$#start_codon GTG CLASSIFICATION #superfamily beta-alanine-pyruvate transaminase KEYWORDS aminotransferase; biotin biosynthesis; phosphoprotein; !1pyridoxal phosphate FEATURE !$285 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 455 #molecular-weight 51774 #checksum 7135 SEQUENCE /// ENTRY C69594 #type complete TITLE adenosylmethionine-8-amino-7-oxononanoate transaminase (EC 2.6.1.62) bioA - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS C69594 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69594 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-448 ##label KUN !'##cross-references GB:Z99119; GB:AL009126; NID:g2635411; !1PIDN:CAB15001.1; PID:g2635507 !'##experimental_source strain 168 GENETICS !$#gene bioA CLASSIFICATION #superfamily beta-alanine-pyruvate transaminase KEYWORDS aminotransferase; biotin biosynthesis; phosphoprotein; !1pyridoxal phosphate FEATURE !$280 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 448 #molecular-weight 50111 #checksum 7162 SEQUENCE /// ENTRY B69835 #type complete TITLE adenosylmethionine-8-amino-7-oxononanoate homolog yhxA - Bacillus subtilis ALTERNATE_NAMES probable transaminase (EC 2.6.1.-) ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS B69835; A47700 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69835 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-450 ##label KUN !'##cross-references GB:Z99108; GB:Z99109; GB:AL009126; NID:g2633260; !1PIDN:CAB12765.1; PID:g2633261; NID:g2633055; PID:g2633249 !'##experimental_source strain 168 REFERENCE A47700 !$#authors Beijer, L.; Nilsson, R.P.; Holmberg, C.; Rutberg, L. !$#journal J. Gen. Microbiol. (1993) 139:349-359 !$#title The glpP and glpF genes of the glycerol regulon in Bacillus !1subtilis. !$#cross-references MUID:93171878; PMID:8436953 !$#accession A47700 !'##status preliminary !'##molecule_type DNA !'##residues 352-450 ##label BEI !'##note sequence extracted from NCBI backbone (NCBIN:125668, !1NCBIP:125670) GENETICS !$#gene yhxA CLASSIFICATION #superfamily beta-alanine-pyruvate transaminase KEYWORDS aminotransferase; phosphoprotein; pyridoxal phosphate FEATURE !$283 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 450 #molecular-weight 49871 #checksum 1316 SEQUENCE /// ENTRY F69904 #type complete TITLE adenosylmethionine-8-amino-7-oxononanoate homolog yodT - Bacillus subtilis ALTERNATE_NAMES probable transaminase (EC 2.6.1.-) ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS F69904 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69904 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-444 ##label KUN !'##cross-references GB:Z99114; GB:AL009126; NID:g2634230; !1PIDN:CAB13865.1; PID:g2634366 !'##experimental_source strain 168 GENETICS !$#gene yodT CLASSIFICATION #superfamily beta-alanine-pyruvate transaminase KEYWORDS aminotransferase; phosphoprotein; pyridoxal phosphate FEATURE !$268 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 444 #molecular-weight 48413 #checksum 7591 SEQUENCE /// ENTRY A42800 #type complete TITLE beta-alanine-pyruvate transaminase (EC 2.6.1.18) - Pseudomonas putida ALTERNATE_NAMES omega-amino acid-pyruvate aminotransferase ORGANISM #formal_name Pseudomonas putida DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS A42800 REFERENCE A42800 !$#authors Yonaha, K.; Nishie, M.; Aibara, S. !$#journal J. Biol. Chem. (1992) 267:12506-12510 !$#title The primary structure of omega-amino acid:pyruvate !1aminotransferase. !$#cross-references MUID:92316928; PMID:1618757 !$#accession A42800 !'##status preliminary !'##molecule_type protein !'##residues 1-449 ##label YON CLASSIFICATION #superfamily beta-alanine-pyruvate transaminase KEYWORDS aminotransferase; phosphoprotein; pyridoxal phosphate FEATURE !$288 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 449 #molecular-weight 48600 #checksum 8923 SEQUENCE /// ENTRY XNECV #type complete TITLE branched-chain-amino-acid transaminase (EC 2.6.1.42) [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES branched-chain-amino-acid aminotransferase; transaminase B ORGANISM #formal_name Escherichia coli DATE 30-Nov-1980 #sequence_revision 10-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS E65180; C26570; A91996; A93693; S30668; A57546; A00602 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65180 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-309 ##label BLAT !'##cross-references GB:AE000453; GB:U00096; NID:g2367276; !1PIDN:AAC77490.1; PID:g1790205; UWGP:b3770 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A26570 !$#authors Lawther, R.P.; Wek, R.C.; Lopes, J.M.; Pereira, R.; Taillon, !1B.E.; Hatfield, G.W. !$#journal Nucleic Acids Res. (1987) 15:2137-2155 !$#title The complete nucleotide sequence of the ilvGMEDA operon of !1Escherichia coli K-12. !$#cross-references MUID:87174741; PMID:3550695 !$#accession C26570 !'##molecule_type DNA !'##residues 1-150,'A',152-309 ##label LA1 !'##cross-references GB:X04890; NID:g288528; PIDN:CAA28575.1; !1PID:g288531 REFERENCE A91996 !$#authors Kuramitsu, S.; Ogawa, T.; Ogawa, H.; Kagamiyama, H. !$#journal J. Biochem. (1985) 97:993-999 !$#title Branched-chain amino acid aminotransferase of Escherichia !1coli: nucleotide sequence of ilvE gene and the deduced amino !1acid sequence. !$#cross-references MUID:85289113; PMID:3897211 !$#accession A91996 !'##molecule_type DNA !'##residues 1-150,'A',152-309 ##label KUR !'##cross-references GB:X02413; NID:g41787; PIDN:CAA26262.1; PID:g41789 !'##experimental_source strain K12 REFERENCE A93693 !$#authors Lawther, R.P.; Nichols, B.; Zurawski, G.; Hatfield, G.W. !$#journal Nucleic Acids Res. (1979) 7:2289-2301 !$#title The nucleotide sequence preceding and including the !1beginning of the ilvE gene of the ilvGEDA operon of !1Escherichia coli K12. !$#cross-references MUID:80101081; PMID:392469 !$#accession A93693 !'##molecule_type DNA !'##residues 1-57,'V',59-61,'R',63-81 ##label LA2 !'##experimental_source strain K12 REFERENCE S30660 !$#authors Daniels, D.L.; Plunkett III, G.; Burland, V.; Blattner, F.R. !$#journal Science (1992) 257:771-778 !$#title Analysis of the Escherichia coli genome: DNA sequence of the !1region from 84.5 to 86.5 minutes. !$#cross-references MUID:92358234; PMID:1379743 !$#accession S30668 !'##molecule_type DNA !'##residues 1-309 ##label DAN !'##cross-references EMBL:M87049; NID:g836656; PIDN:AAA67573.1; !1PID:g148177 REFERENCE A57546 !$#authors Inoue, K.; Kuramitsu, S.; Aki, K.; Watanabe, Y.; Takagi, T.; !1Nishigai, M.; Ikai, A.; Kagamiyama, H. !$#journal J. Biochem. (1988) 104:777-784 !$#title Branched-chain amino acid aminotransferase of Escherichia !1coli: overproduction and properties. !$#cross-references MUID:89174510; PMID:3069843 !$#accession A57546 !'##molecule_type protein !'##residues 2-31;150,'A',152-165;308-309 ##label INO !'##note identification of N6-pyridoxal phosphate lysine GENETICS !$#gene ilvE !$#map_position 85 min FUNCTION !$#description EC 2.6.1.42 [validated, MUID:85289113]; catalyzes the !1reversible transamination of alpha-amino groups from !1leucine, valine, or isoleucine to 2-oxoglutarate !$#pathway branched-chain amino acid biosynthesis CLASSIFICATION #superfamily branched-chain-amino-acid aminotransferase KEYWORDS aminotransferase; branched-chain amino acid biosynthesis; !1phosphoprotein; pyridoxal phosphate FEATURE !$2-309 #product branched-chain-amino-acid aminotransferase !8#status experimental #label MAT\ !$160 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status experimental SUMMARY #length 309 #molecular-weight 34179 #checksum 3545 SEQUENCE /// ENTRY A34082 #type complete TITLE branched-chain-amino-acid transaminase (EC 2.6.1.42) - Salmonella typhimurium ALTERNATE_NAMES branched-chain-amino-acid aminotransferase; transaminase B ORGANISM #formal_name Salmonella typhimurium DATE 30-Apr-1999 #sequence_revision 30-Apr-1999 #text_change 30-Apr-1999 ACCESSIONS A34082; A05077 REFERENCE A34082 !$#authors Feild, M.J.; Nguyen, D.C.; Armstrong, F.B. !$#journal Biochemistry (1989) 28:5306-5310 !$#title Amino acid sequence of Salmonella typhimurium branched-chain !1amino acid aminotransferase. !$#cross-references MUID:89352621; PMID:2669973 !$#accession A34082 !'##status preliminary !'##molecule_type protein !'##residues 1-308 ##label FEI REFERENCE A05077 !$#authors Randall, R.R.; Wallis, M.H.; Young, G.J.; Armstrong, F.B. !$#journal Fed. Proc. (1979) 38:325A !$#title N-terminal sequence of branched-chain amino acid !1aminotransferase. !$#accession A05077 !'##molecule_type protein !'##residues 1-5 ##label RAN FUNCTION !$#description catalyzes the reversible transamination of alpha-amino !1groups from leucine, valine, or isoleucine to 2-oxoglutarate !$#pathway branched-chain amino acid biosynthesis CLASSIFICATION #superfamily branched-chain-amino-acid aminotransferase KEYWORDS aminotransferase; branched-chain amino acid biosynthesis; !1phosphoprotein; pyridoxal phosphate FEATURE !$159 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 308 #molecular-weight 33849 #checksum 2148 SEQUENCE /// ENTRY XNHUSP #type complete TITLE serine-pyruvate transaminase (EC 2.6.1.51), peroxisomal [validated] - human ALTERNATE_NAMES alanine-glyoxylate aminotransferase; serine-pyruvate aminotransferase, peroxisomal CONTAINS alanine-glyoxylate transaminase (EC 2.6.1.44) ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 19-Jul-2002 ACCESSIONS I39419; S10557; A38764; S14002; A36681; PS0392 REFERENCE I39419 !$#authors Purdue, P.E.; Lumb, M.J.; Fox, M.; Griffo, G.; Hamon-Benais, !1C.; Povey, S.; Danpure, C.J. !$#journal Genomics (1991) 10:34-42 !$#title Characterization and chromosomal mapping of a genomic clone !1encoding human alanine:glyoxylate aminotransferase. !$#cross-references MUID:91257848; PMID:2045108 !$#accession I39419 !'##status translation not shown !'##molecule_type DNA !'##residues 1-392 ##label RES !'##cross-references GB:M61763; NID:g178271; PIDN:AAA51680.1; !1PID:g178273 REFERENCE S10557 !$#authors Takada, Y.; Kaneko, N.; Esumi, H.; Purdue, P.E.; Danpure, !1C.J. !$#journal Biochem. J. (1990) 268:517-520 !$#title Human peroxisomal L-alanine: glyoxylate aminotransferase. !1Evolutionary loss of a mitochondrial targeting signal by !1point mutation of the initiation codon. !$#cross-references MUID:90303236; PMID:2363689 !$#accession S10557 !'##molecule_type mRNA !'##residues 1-392 ##label TAK1 !'##cross-references EMBL:X53414; NID:g28560; PIDN:CAA37493.1; !1PID:g28561 !$#accession A38764 !'##molecule_type protein !'##residues 52-61;318-330 ##label TAK2 REFERENCE S14002 !$#authors Nishiyama, K.; Berstein, G.; Oda, T.; Ichiyama, A. !$#journal Eur. J. Biochem. (1990) 194:9-18 !$#title Cloning and nucleotide sequence of cDNA encoding human liver !1serine-pyruvate aminotransferase. !$#cross-references MUID:91071216; PMID:2253628 !$#accession S14002 !'##molecule_type mRNA !'##residues 1-392 ##label NIS !'##cross-references EMBL:X56092; NID:g36581; PIDN:CAA39572.1; !1PID:g36582 REFERENCE A36681 !$#authors Purdue, P.E.; Takada, Y.; Danpure, C.J. !$#journal J. Cell Biol. (1990) 111:2341-2351 !$#title Identification of mutations associated with !1peroxisome-to-mitochondrion mistargeting of alanine/ !1glyoxylate aminotransferase in primary hyperoxaluria type 1. !$#cross-references MUID:91115929; PMID:1703535 !$#accession A36681 !'##molecule_type mRNA !'##residues 1-314,'T',316-392 ##label PUR !'##cross-references GB:X53414 REFERENCE PX0075 !$#authors Matsui Lee, I.S.; Takio, K.; Kido, R.; Titani, K. !$#journal J. Biochem. (1994) 116:12-17 !$#title Purification and amino- and carboxyl-terminal amino acid !1sequences of alanine-glyoxylate transaminase 1 from human !1liver. !$#cross-references MUID:95096006; PMID:7798168 !$#accession PS0392 !'##molecule_type protein !'##residues 2-38;349-392 ##label MTK !'##experimental_source liver GENETICS !$#gene GDB:AGXT; SPAT !'##cross-references GDB:127113; OMIM:259900 !$#map_position 2q37.3-2q37.3 !$#introns 55/3; 120/1; 141/3; 175/2; 199/1; 227/2; 259/2; 282/3; 314/ !13; 357/3 !$#note defects in this gene can result in oxalosis I, hyperoxaluria !1I and glycolicaciduria FUNCTION !$#description catalyzes the transamination of L-serine and pyruvate to !13-hydroxpyruvate and L-alanine; catalyzes the transamination !1of L-alanine and glyoxylate to pyruvate and glycine CLASSIFICATION #superfamily serine-pyruvate aminotransferase KEYWORDS acetylated amino end; aminotransferase; glycoprotein; !1homodimer; peroxisome; phosphoprotein; pyridoxal phosphate FEATURE !$2-392 #product serine-pyruvate transaminase, peroxisomal !8#status experimental #label MAT\ !$390-392 #region peroxisome/glyoxysome location signal #status !8atypical\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental\ !$209 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted\ !$367 #binding_site carbohydrate (Asn) (covalent) #status !8absent SUMMARY #length 392 #molecular-weight 43010 #checksum 1797 SEQUENCE /// ENTRY XNRTSP #type complete TITLE serine-pyruvate transaminase (EC 2.6.1.51) precursor, mitochondrial - rat ALTERNATE_NAMES serine-pyruvate aminotransferase, mitochondrial ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Jun-2002 ACCESSIONS S00164; A38753; A35200; B35200 REFERENCE S00164 !$#authors Oda, T.; Miyajima, H.; Suzuki, Y.; Ichiyama, A. !$#journal Eur. J. Biochem. (1987) 168:537-542 !$#title Nucleotide sequence of the cDNA encoding the precursor for !1mitochondrial serine:pyruvate aminotransferase of rat liver. !$#cross-references MUID:88029472; PMID:2822418 !$#accession S00164 !'##molecule_type mRNA !'##residues 1-414 ##label ODA !'##cross-references EMBL:X06357; NID:g207032; PIDN:AAA42168.1; !1PID:g207033 !$#accession A38753 !'##molecule_type protein !'##residues 25-36,'X',38-39,'XX',42-44 ##label ODA2 REFERENCE A35200 !$#authors Oda, T.; Funai, T.; Ichiyama, A. !$#journal J. Biol. Chem. (1990) 265:7513-7519 !$#title Generation from a single gene of two mRNAs that encode the !1mitochondrial and peroxisomal serine:pyruvate !1aminotransferase of rat liver. !$#cross-references MUID:90237053; PMID:2332438 !$#accession A35200 !'##status preliminary !'##molecule_type mRNA !'##residues 1-30 ##label OD2 !'##cross-references GB:M35270; GB:X06357 !$#accession B35200 !'##status preliminary !'##molecule_type mRNA !'##residues 23-30 ##label OD3 !'##cross-references GB:M35270; GB:X06357 !'##experimental_source peroxisomal CLASSIFICATION #superfamily serine-pyruvate aminotransferase KEYWORDS aminotransferase; mitochondrion; peroxisome; phosphoprotein; !1pyridoxal phosphate FEATURE !$1-24 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$25-414 #product serine-pyruvate aminotransferase #status !8experimental #label MAT\ !$231 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 414 #molecular-weight 45834 #checksum 2419 SEQUENCE /// ENTRY HQYCSS #type complete TITLE soluble hydrogenase (EC 1.12.-.-) small chain - Synechococcus sp. (strain PCC 6716) ORGANISM #formal_name Synechococcus sp. DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 11-Jun-1999 ACCESSIONS S06919 REFERENCE S06919 !$#authors van der Oost, J.; van Walraven, H.S.; Bogerd, J.; Smit, !1A.B.; Ewart, G.D.; Smith, G.D. !$#journal Nucleic Acids Res. (1989) 17:10098 !$#title Nucleotide sequence of the gene proposed to encode the small !1subunit of the soluble hydrogenase of the thermophilic !1unicellular cyanobacterium Synechococcus PCC 6716. !$#cross-references MUID:90098775; PMID:2513553 !$#accession S06919 !'##molecule_type DNA !'##residues 1-384 ##label VAN !'##cross-references EMBL:X16658; NID:g48053; PIDN:CAA34644.1; !1PID:g48054 COMMENT Synechococcus appears to have two hydrogenase activities: a !1membrane-bound "hydrogen uptake" enzyme that couples !1molecular hydrogen to photosynthetic and respiratory !1electron transport; and a soluble "reversible" hydrogenase !1of unknown function. This protein is the hydrogen-binding !1component of the soluble enzyme, which is a dimer of !1nonidentical chains; it also possesses tritium exchange !1activity independent of the other component (i.e., the large !1chain). CLASSIFICATION #superfamily serine-pyruvate aminotransferase KEYWORDS oxidoreductase SUMMARY #length 384 #molecular-weight 40876 #checksum 7128 SEQUENCE /// ENTRY XNEBPY #type complete TITLE phosphoserine transaminase (EC 2.6.1.52) - Yersinia enterocolitica ALTERNATE_NAMES phosphoserine aminotransferase ORGANISM #formal_name Yersinia enterocolitica DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 11-Jun-1999 ACCESSIONS JQ0130 REFERENCE JQ0130 !$#authors O'Gaora, P.; Maskell, D.; Coleman, D.; Cafferkey, M.; !1Dougan, G. !$#journal Gene (1989) 84:23-30 !$#title Cloning and characterisation of the serC and aroA genes of !1Yersinia enterocolitica, and construction of an aroA mutant. !$#cross-references MUID:90108713; PMID:2691337 !$#accession JQ0130 !'##molecule_type DNA !'##residues 1-361 ##label OGA !'##cross-references GB:M32213; NID:g155521; PIDN:AAA27665.1; !1PID:g155522 !'##experimental_source strain 8081 COMMENT This organism causes a variety of diseases in humans ranging !1from mild gastroenteritis to septicemia. GENETICS !$#gene serC FUNCTION !$#description catalyzes the transfer of the amino group from glutamic acid !1to phosphonooxypyruvate, with the formation of !12-oxoglutarate and phosphoserine !$#pathway serine biosynthesis CLASSIFICATION #superfamily phosphoserine aminotransferase KEYWORDS aminotransferase; phosphoprotein; pyridoxal phosphate; !1serine biosynthesis FEATURE !$197 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 361 #molecular-weight 40162 #checksum 3872 SEQUENCE /// ENTRY S10512 #type complete TITLE phosphoserine transaminase (EC 2.6.1.52) - Salmonella gallinarum ORGANISM #formal_name Salmonella gallinarum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S10512 REFERENCE S10512 !$#authors Griffin, H.G. !$#journal Nucleic Acids Res. (1990) 18:4260 !$#title Nucleotide sequence of the Salmonella serC gene. !$#cross-references MUID:90332434; PMID:2198540 !$#accession S10512 !'##molecule_type DNA !'##residues 1-362 ##label GRI !'##cross-references EMBL:X53381; NID:g47093; PIDN:CAA37461.1; !1PID:g47094 !'##experimental_source strain 9 GENETICS !$#gene serC FUNCTION !$#pathway serine biosynthesis CLASSIFICATION #superfamily phosphoserine aminotransferase KEYWORDS aminotransferase; phosphoprotein; pyridoxal phosphate; !1serine biosynthesis FEATURE !$198 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 362 #molecular-weight 39855 #checksum 1116 SEQUENCE /// ENTRY B64830 #type complete TITLE phosphoserine transaminase (EC 2.6.1.52) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS B64830; S28806; S09360 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64830 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-362 ##label BLAT !'##cross-references GB:AE000193; GB:U00096; NID:g1787134; !1PIDN:AAC73993.1; PID:g1787136; UWGP:b0907 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S28806 !$#authors Duncan, K.; Coggins, J.R. !$#journal Biochem. J. (1986) 234:49-57 !$#title The serC-aroA operon of Escherichia coli. A mixed function !1operon encoding enzymes from two different amino acid !1biosynthetic pathways. !$#cross-references MUID:86215119; PMID:3518706 !$#accession S28806 !'##molecule_type DNA !'##residues 1-292,'R',294-362 ##label DUN !'##cross-references EMBL:M25608 !'##experimental_source strain K-12 GENETICS !$#gene serC; pdxF FUNCTION !$#pathway serine biosynthesis CLASSIFICATION #superfamily phosphoserine aminotransferase KEYWORDS aminotransferase; phosphoprotein; pyridoxal phosphate; !1serine biosynthesis FEATURE !$198 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 362 #molecular-weight 39783 #checksum 210 SEQUENCE /// ENTRY E64187 #type complete TITLE phosphoserine transaminase (EC 2.6.1.52) - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS E64187 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession E64187 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-362 ##label TIGR !'##cross-references GB:U32796; GB:L42023; NID:g1574086; !1PIDN:AAC22822.1; PID:g1574094; TIGR:HI1167 GENETICS !$#gene serC FUNCTION !$#pathway serine biosynthesis CLASSIFICATION #superfamily phosphoserine aminotransferase KEYWORDS aminotransferase; phosphoprotein; pyridoxal phosphate; !1serine biosynthesis FEATURE !$196 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 362 #molecular-weight 40313 #checksum 9667 SEQUENCE /// ENTRY A26998 #type complete TITLE probable phosphoserine transaminase (EC 2.6.1.52), progesterone-induced, endometrial - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A26998 REFERENCE A26998 !$#authors Misrahi, M.; Atger, M.; Milgrom, E. !$#journal Biochemistry (1987) 26:3975-3982 !$#title A novel progesterone-induced messenger RNA in rabbit and !1human endometria. Cloning and sequence analysis of the !1complementary DNA. !$#cross-references MUID:88000617; PMID:3651428 !$#accession A26998 !'##molecule_type mRNA !'##residues 1-370 ##label MIS !'##cross-references GB:M17099; NID:g165008; PIDN:AAA31245.1; !1PID:g165009 CLASSIFICATION #superfamily phosphoserine aminotransferase KEYWORDS aminotransferase; phosphoprotein; pyridoxal phosphate FEATURE !$200 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 370 #molecular-weight 40621 #checksum 3409 SEQUENCE /// ENTRY JT0482 #type complete TITLE glucokinase (EC 2.7.1.2) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YCL040w; protein YCL312 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS JT0482; S19369; S25350 REFERENCE JT0482 !$#authors Albig, W.; Entian, K.D. !$#journal Gene (1988) 73:141-152 !$#title Structure of yeast glucokinase, a strongly diverged specific !1aldo-hexose-phosphorylating isoenzyme. !$#cross-references MUID:89211944; PMID:3072253 !$#accession JT0482 !'##molecule_type DNA !'##residues 1-500 ##label ALB !'##cross-references GB:M24077; NID:g341102; PIDN:AAA53536.1; !1PID:g577521 REFERENCE S19367 !$#authors Dubois, E.; Pierard, A.; Gigot, D.; Glansdorff, N.; !1Messenguy, F.; Scherens, B. !$#submission submitted to the Protein Sequence Database, March 1992 !$#accession S19369 !'##molecule_type DNA !'##residues 1-500 ##label DUB !'##cross-references EMBL:X59720; NID:g1907116; PIDN:CAA42376.1; !1PID:g5323; GSPDB:GN00003; MIPS:YCL040w REFERENCE S25347 !$#authors Scherens, B.; Messenguy, F.; Gigot, D.; Dubois, E. !$#journal Yeast (1992) 8:577-586 !$#title The complete sequence of a 9,543 bp segment on the left arm !1of chromosome III reveals five open reading frames including !1glucokinase and the protein disulfide isomerase. !$#cross-references MUID:92397595; PMID:1523890 !$#accession S25350 !'##molecule_type DNA !'##residues 1-500 ##label SCH !'##cross-references EMBL:X59720; NID:g1907116; PIDN:CAA42376.1; !1PID:g5323 GENETICS !$#gene SGD:GLK1; MIPS:YCL040w !'##cross-references SGD:S0000545; MIPS:YCL040w !$#map_position 3L CLASSIFICATION #superfamily hexokinase; hexokinase homology KEYWORDS ATP; glycolysis; phosphotransferase FEATURE !$27-499 #domain hexokinase homology #label HXK\ !$487-493 #region ATP binding #status predicted SUMMARY #length 500 #molecular-weight 55377 #checksum 761 SEQUENCE /// ENTRY KIBYHB #type complete TITLE hexokinase (EC 2.7.1.1) B - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES HEX1 protein; hexokinase II; hexokinase PII; protein G0556; protein NRB486; protein YGL253w; SCI2 protein ORGANISM #formal_name Saccharomyces cerevisiae DATE 28-Dec-1987 #sequence_revision 12-Apr-1996 #text_change 16-Jun-2000 ACCESSIONS S61608; B23523; S22430; A23958; S05731; S33656; S64279; !1A53632; S28555 REFERENCE S61598 !$#authors Coissac, E.; Maillier, E.; Robineau, S.; Netter, P. !$#submission submitted to the EMBL Data Library, December 1995 !$#accession S61608 !'##molecule_type DNA !'##residues 1-486 ##label COI !'##cross-references EMBL:X94357; NID:g1150575; PIDN:CAA64134.1; !1PID:g1150586 REFERENCE A93649 !$#authors Stachelek, C.; Stachelek, J.; Swan, J.; Botstein, D.; !1Konigsberg, W. !$#journal Nucleic Acids Res. (1986) 14:945-963 !$#title Identification, cloning and sequence determination of the !1genes specifying hexokinase A and B from yeast. !$#cross-references MUID:86120382; PMID:3003701 !$#accession B23523 !'##molecule_type DNA !'##residues 1-28,'I',30-60,'V',62-196,'S',198-486 ##label STA !'##cross-references EMBL:X03483; NID:g3792; PIDN:CAA27203.1; PID:g3793 !'##note the authors translated the codon GTT for residue 61 as Gly !$#accession S22430 !'##molecule_type protein !'##residues 2-7;'I', !130-46;78-111;114-119;166-173;177-194;228-236;250-281; !1283-300;330-335;395-406;408-423;431-436;453-464;475-486 !1##label STA2 REFERENCE A23958 !$#authors Frohlich, K.; Entian, K.; Mecke, D. !$#journal Gene (1985) 36:105-111 !$#title The primary structure of the yeast hexokinase PII gene !1(HXK2) which is responsible for glucose repression. !$#cross-references MUID:86056943; PMID:3905511 !$#accession A23958 !'##molecule_type DNA !'##residues 1-32,'N',34-60,'V',62-420,'ST',423-443,'PH',446-452,'V', !1454-461,'P',463-486 ##label FRO !'##cross-references EMBL:M11181 !'##note the authors translated the codon GTT for residue 61 as Gly REFERENCE S05731 !$#authors Schmidt, J.J.; Colowick, S.P. !$#journal Arch. Biochem. Biophys. (1973) 158:471-477 !$#title Identification of a peptide sequence involved in association !1of subunits of yeast hexokinases. !$#cross-references MUID:74114889; PMID:4592981 !$#accession S05731 !'##molecule_type protein !'##residues 2-12 ##label SCH REFERENCE S33654 !$#authors Breitwieser, W.; Price, C.; Schuster, T. !$#journal Yeast (1993) 9:551-556 !$#title Identification of a gene encoding a novel zinc finger !1protein in Saccharomyces cerevisiae. !$#cross-references MUID:93311123; PMID:8322518 !$#accession S33656 !'##molecule_type DNA !'##residues 1-247 ##label BRE !'##cross-references EMBL:X67787; NID:g3707; PIDN:CAA48003.1; PID:g3710 REFERENCE S64271 !$#authors Coissac, E.; Maillier, E.; Netter, P. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64279 !'##molecule_type DNA !'##residues 1-486 ##label COW !'##cross-references EMBL:Z72775; NID:g1322930; PIDN:CAA96973.1; !1PID:g1322931; GSPDB:GN00007; MIPS:YGL253w !'##experimental_source strain S288C REFERENCE A53632 !$#authors Kriegel, T.M.; Rush, J.; Vojtek, A.B.; Clifton, D.; !1Fraenkel, D.G. !$#journal Biochemistry (1994) 33:148-152 !$#title In vivo phosphorylation site of hexokinase 2 in !1Saccharomyces cerevisiae. !$#cross-references MUID:94114477; PMID:8286332 !$#accession A53632 !'##status preliminary !'##molecule_type protein !'##residues 13-21 ##label KRI GENETICS !$#gene SGD:HXK2; HEX1; SCI2; HKB; MIPS:YGL253w !'##cross-references SGD:S0003222; MIPS:YGL253w !$#map_position 7L CLASSIFICATION #superfamily hexokinase; hexokinase homology KEYWORDS allosteric regulation; ATP; glycolysis; phosphoprotein; !1phosphotransferase FEATURE !$2-486 #product hexokinase B #status experimental #label !8MAT\ !$36-470 #domain hexokinase homology #label HXK\ !$15 #binding_site phosphate (Ser) (covalent) #status !8experimental SUMMARY #length 486 #molecular-weight 53942 #checksum 1782 SEQUENCE /// ENTRY KIBYHA #type complete TITLE hexokinase (EC 2.7.1.1) A - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hexokinase I; hexokinase PI; protein F003; protein YFR053c ORGANISM #formal_name Saccharomyces cerevisiae DATE 28-Dec-1987 #sequence_revision 19-Oct-1995 #text_change 16-Jun-2000 ACCESSIONS S56308; A24531; A23523; S05731; S62264; S63800; A28178; !1A11133 REFERENCE S56186 !$#authors Murakami, Y.; Naitou, M.; Hagiwara, H.; Shibata, T.; Ozawa, !1M.; Sasanuma, S.I.; Sasanuma, M.; Tsuchiya, Y.; Soeda, E.; !1Yokoyama, K.; Yamazaki, M.; Tashiro, H.; Eki, T. !$#submission submitted to the EMBL Data Library, May 1995 !$#description Analysis of the nucleotide sequence of chromosome VI from !1Saccaromyces cerevisiae. !$#accession S56308 !'##molecule_type DNA !'##residues 1-485 ##label MUR !'##cross-references EMBL:D50617; NID:g836685; PIDN:BAA09292.1; !1PID:g836808; GSPDB:GN00006; MIPS:YFR053c REFERENCE A24531 !$#authors Kopetzki, E.; Entian, K.D.; Mecke, D. !$#journal Gene (1985) 39:95-102 !$#title Complete nucleotide sequence of the hexokinase PI gene !1(HXK1) of Saccharomyces cerevisiae. !$#cross-references MUID:86083199; PMID:3908224 !$#accession A24531 !'##molecule_type DNA !'##residues 1-355,'VF',358-485 ##label KOP !'##cross-references EMBL:M11184 !'##note the authors translated the codon ACT for residue 388 as Ile; !1the sequence shown follows the authors' translation REFERENCE A93649 !$#authors Stachelek, C.; Stachelek, J.; Swan, J.; Botstein, D.; !1Konigsberg, W. !$#journal Nucleic Acids Res. (1986) 14:945-963 !$#title Identification, cloning and sequence determination of the !1genes specifying hexokinase A and B from yeast. !$#cross-references MUID:86120382; PMID:3003701 !$#accession A23523 !'##molecule_type DNA !'##residues 1-60,'V',62-102,'R',104-193,'K',195-243,'C',245-363,'M', !1365-443,'EN',445-478,'VS',481-485 ##label STA !'##cross-references EMBL:X03482; NID:g3790; PIDN:CAA27202.1; PID:g3791 !'##note the authors translated the codon GTT for residue 61 as Gly, CGT !1for residue 103 as His, ATG for residue 364 as Ile, and ACG !1for residue 452 as Arg REFERENCE S05731 !$#authors Schmidt, J.J.; Colowick, S.P. !$#journal Arch. Biochem. Biophys. (1973) 158:471-477 !$#title Identification of a peptide sequence involved in association !1of subunits of yeast hexokinases. !$#cross-references MUID:74114889; PMID:4592981 !$#accession S05731 !'##molecule_type protein !'##residues 2-12 ##label SCH REFERENCE S62230 !$#authors Murakami, Y. !$#submission submitted to the EMBL Data Library, December 1994 !$#accession S62264 !'##molecule_type DNA !'##residues 1-485 ##label MUW !'##cross-references EMBL:D44597; NID:g871938; PIDN:BAA08019.1; !1PID:g871952 REFERENCE S63787 !$#authors Eki, T.; Naitou, M.; Hagiwara, H.; Ozawa, M.; Sasanuma, !1S.I.; Sasanuma, M.; Tsuchiya, Y.; Shibata, T.; Hanaoka, F.; !1Murakami, Y. !$#journal Yeast (1996) 12:149-167 !$#title Analysis of a 36.2 kb DNA sequence including the right !1telomere of chromosome VI from Saccharomyces cerevisiae. !$#cross-references MUID:96287652; PMID:8686379 !$#accession S63800 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-485 ##label EKI !'##cross-references EMBL:D44597; NID:g871938; PIDN:BAA08019.1; !1PID:g871952 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1995 REFERENCE A28178 !$#authors Tamura, J.K.; LaDine, J.R.; Cross, R.L. !$#journal J. Biol. Chem. (1988) 263:7907-7912 !$#title The adenine nucleotide binding site on yeast hexokinase PII. !1Affinity labeling of Lys-111 by pyridoxal !15'-diphospho-5'-adenosine. !$#cross-references MUID:88227998; PMID:3131329 !$#accession A28178 !'##molecule_type protein !'##residues 104-112 ##label TAM GENETICS !$#gene SGD:HXK1; MIPS:YFR053c !'##cross-references SGD:S0001949; MIPS:YFR053c !$#map_position 6R CLASSIFICATION #superfamily hexokinase; hexokinase homology KEYWORDS allosteric regulation; ATP; glycolysis; phosphotransferase FEATURE !$2-485 #product hexokinase A #status experimental #label !8MAT\ !$36-469 #domain hexokinase homology #label HXK SUMMARY #length 485 #molecular-weight 53738 #checksum 7867 SEQUENCE /// ENTRY A31869 #type complete TITLE hexokinase (EC 2.7.1.1) I [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 08-Dec-2000 ACCESSIONS A31869; A39047; B39047; S23966 REFERENCE A31869 !$#authors Nishi, S.; Seino, S.; Bell, G.I. !$#journal Biochem. Biophys. Res. Commun. (1988) 157:937-943 !$#title Human hexokinase: sequences of amino- and carboxyl-terminal !1halves are homologous. !$#cross-references MUID:89087485; PMID:3207429 !$#accession A31869 !'##molecule_type mRNA !'##residues 1-917 ##label NIS !'##cross-references GB:M75126; NID:g184020; PIDN:AAA52646.1; !1PID:g184021 REFERENCE A39047 !$#authors Magnani, M.; Serafini, G.; Bianchi, M.; Casabianca, A.; !1Stocchi, V. !$#journal J. Biol. Chem. (1991) 266:502-505 !$#title Human hexokinase type I microheterogeneity is due to !1different amino-terminal sequences. !$#cross-references MUID:91093173; PMID:1985912 !$#accession A39047 !'##molecule_type protein !'##residues 11-60,'Y',62-120 ##label MAG !$#accession B39047 !'##molecule_type protein !'##residues 103-120 ##label MA2 REFERENCE S23966 !$#authors Magnani, M.; Bianchi, M.; Casabianca, A.; Stocchi, V.; !1Daniele, A.; Altruda, F.; Ferrone, M.; Silengo, L. !$#journal Biochem. J. (1992) 285:193-199 !$#title A recombinant human 'mini'-hexokinase is catalytically !1active and regulated by hexose 6-phosphates. !$#cross-references MUID:92344570; PMID:1637300 !$#accession S23966 !'##status preliminary !'##molecule_type mRNA !'##residues 287-917 ##label MA3 !'##cross-references EMBL:X66957; NID:g311377; PIDN:CAA47379.1; !1PID:g34670 GENETICS !$#gene GDB:HK1 !'##cross-references GDB:120044; OMIM:142600 !$#map_position 10q22-10q22 CLASSIFICATION #superfamily human hexokinase I; hexokinase homology KEYWORDS ATP; duplication; glycolysis; phosphotransferase FEATURE !$11-917 #product hexokinase, high molecular weight #status !8experimental #label MAT\ !$31-459 #domain hexokinase homology #label HXK1\ !$103-917 #product hexokinase, low molecular weight #status !8experimental #label MAL\ !$479-907 #domain hexokinase homology #label HXK2 SUMMARY #length 917 #molecular-weight 102502 #checksum 9221 SEQUENCE /// ENTRY A35244 #type complete TITLE hexokinase (EC 2.7.1.1), tumor - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A35244 REFERENCE A35244 !$#authors Arora, K.K.; Fanciulli, M.; Pedersen, P.L. !$#journal J. Biol. Chem. (1990) 265:6481-6488 !$#title Glucose phosphorylation in tumor cells. Cloning, sequencing, !1and overexpression in active form of a full-length cDNA !1encoding a mitochondrial bindable form of hexokinase. !$#cross-references MUID:90202933; PMID:2318862 !$#accession A35244 !'##status preliminary !'##molecule_type mRNA !'##residues 1-918 ##label ARO !'##cross-references GB:J05277 CLASSIFICATION #superfamily human hexokinase I; hexokinase homology KEYWORDS ATP; glycolysis; phosphotransferase FEATURE !$31-459 #domain hexokinase homology #label HXK1\ !$479-907 #domain hexokinase homology #label HXK2 SUMMARY #length 918 #molecular-weight 102272 #checksum 1367 SEQUENCE /// ENTRY S15885 #type complete TITLE hexokinase (EC 2.7.1.1) II precursor [similarity] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 16-Jun-2000 ACCESSIONS S15885; S23672; S52114 REFERENCE S15885 !$#authors Thelen, A.P.; Wilson, J.E. !$#journal Arch. Biochem. Biophys. (1991) 286:645-651 !$#title Complete amino acid sequence of the Type II isozyme of rat !1hexokinase, deduced from the cloned cDNA: comparison with a !1hexokinase from Novikoff ascites tumor. !$#cross-references MUID:91378366; PMID:1897984 !$#accession S15885 !'##molecule_type mRNA !'##residues 1-917 ##label ARC !'##cross-references EMBL:M68971; NID:g204612; PIDN:AAA41333.1; !1PID:g204613 !$#accession S23672 !'##molecule_type protein !'##residues 11-18 ##label THE1 REFERENCE S52114 !$#authors Ichihara, J.; Shinohara, Y.; Kogure, K.; Terada, H. !$#journal Biochim. Biophys. Acta (1995) 1260:365-368 !$#title Nucleotide sequence of the 5'-flanking region of the rat !1type II hexokinase gene. !$#cross-references MUID:95178563; PMID:7873617 !$#accession S52114 !'##molecule_type DNA !'##residues 1-21 ##label ICH !'##cross-references GB:D26393; NID:g893403; PIDN:BAA05409.1; !1PID:g1526568 CLASSIFICATION #superfamily human hexokinase I; hexokinase homology KEYWORDS ATP; duplication; glycolysis; monomer; phosphotransferase FEATURE !$31-459 #domain hexokinase homology #label HXK1\ !$479-907 #domain hexokinase homology #label HXK2 SUMMARY #length 917 #molecular-weight 102543 #checksum 1670 SEQUENCE /// ENTRY S13913 #type complete TITLE hexokinase (EC 2.7.1.1) III [similarity] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 05-May-2000 ACCESSIONS S13913 REFERENCE S13913 !$#authors Schwab, D.A.; Wilson, J.E. !$#journal Arch. Biochem. Biophys. (1991) 285:365-370 !$#title Complete amino acid sequence of the type III isozyme of rat !1hexokinase, deduced from the cloned cDNA. !$#cross-references MUID:91378267; PMID:1897938 !$#accession S13913 !'##molecule_type mRNA !'##residues 1-924 ##label SCH !'##cross-references GB:U73859; GB:S55552; NID:g1658067; !1PIDN:AAB18253.1; PID:g1658068 CLASSIFICATION #superfamily human hexokinase I; hexokinase homology KEYWORDS ATP; duplication; glycolysis; monomer; phosphotransferase FEATURE !$42-472 #domain hexokinase homology #label HXK1\ !$492-914 #domain hexokinase homology #label HXK2 SUMMARY #length 924 #molecular-weight 100253 #checksum 7546 SEQUENCE /// ENTRY E70014 #type complete TITLE rhamnulokinase (EC 2.7.1.5) yulC - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS E70014 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E70014 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-485 ##label KUN !'##cross-references GB:Z99119; GB:Z99120; GB:AL009126; NID:g2635613; !1PIDN:CAB15109.1; PID:g2635616; NID:g2635411; PID:g2635604 !'##experimental_source strain 168 GENETICS !$#gene yulC CLASSIFICATION #superfamily rhamnulokinase KEYWORDS phosphotransferase SUMMARY #length 485 #molecular-weight 54735 #checksum 3457 SEQUENCE /// ENTRY JQ1289 #type complete TITLE rhamnulokinase (EC 2.7.1.5) - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JQ1289; S21853 REFERENCE JQ1288 !$#authors Nishitani, J.; Wilcox, G. !$#journal Gene (1991) 105:37-42 !$#title Cloning and characterization of the L-rhamnose regulon in !1Salmonella typhimurium LT2. !$#cross-references MUID:92039016; PMID:1657713 !$#accession JQ1289 !'##molecule_type DNA !'##residues 1-489 ##label NIS !'##cross-references EMBL:X57299; NID:g47905; PIDN:CAA40557.1; !1PID:g47907 !'##experimental_source strain AZ056 COMMENT This protein is necessary for the metabolism of L-rhamnose. GENETICS !$#gene rhaB CLASSIFICATION #superfamily rhamnulokinase KEYWORDS phosphotransferase SUMMARY #length 489 #molecular-weight 54578 #checksum 8015 SEQUENCE /// ENTRY E64081 #type complete TITLE probable rhamnulokinase (EC 2.7.1.5) - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES fucokinase ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS E64081 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession E64081 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-470 ##label TIGR !'##cross-references GB:U32743; GB:L42023; NID:g1573597; !1PIDN:AAC22272.1; PID:g1573606; TIGR:HI0613 CLASSIFICATION #superfamily rhamnulokinase KEYWORDS phosphotransferase SUMMARY #length 470 #molecular-weight 51949 #checksum 8849 SEQUENCE /// ENTRY KIBYGG #type complete TITLE galactokinase (EC 2.7.1.6) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YBR020w; protein YBR0302 ORGANISM #formal_name Saccharomyces cerevisiae DATE 17-Mar-1987 #sequence_revision 09-Sep-1994 #text_change 05-Nov-1999 ACCESSIONS S45876; S46665; A00603; S23294; B13446; S46551 REFERENCE S45875 !$#authors Grivell, L.A.; de Haan, M.; Maat, M.J.; Smits, P.H.M. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S45876 !'##molecule_type DNA !'##residues 1-528 ##label GRI !'##cross-references EMBL:Z35889; NID:g536223; PIDN:CAA84962.1; !1PID:g536224; GSPDB:GN00002; MIPS:YBR020w !'##experimental_source strain S288C REFERENCE S46665 !$#authors Smits, P.H.M. !$#submission submitted to the EMBL Data Library, November 1993 !$#accession S46665 !'##molecule_type DNA !'##residues 1-528 ##label SM2 !'##cross-references EMBL:X76078; NID:g498748; PIDN:CAA53677.1; !1PID:g498749 !'##experimental_source strain S288C REFERENCE A91795 !$#authors Citron, B.A.; Donelson, J.E. !$#journal J. Bacteriol. (1984) 158:269-278 !$#title Sequence of the Saccharomyces GAL region and its !1transcription in vivo. !$#cross-references MUID:84185433; PMID:6715281 !$#accession A00603 !'##molecule_type DNA !'##residues 1-161,'I',163-205,'DIMLVLTMAVWIRLPLFAVRKIMLYTLSSNAVE', !1240-296,'P',298-427,'V',429-483,'N',484-528 ##label CIT !'##cross-references EMBL:K01609; NID:g171562; PIDN:AAA34631.1; !1PID:g171567 !'##note the source is designated as Saccharomyces carlsbergensis REFERENCE S23294 !$#authors Johnston, M.; Davis, R.W. !$#journal Mol. Cell. Biol. (1984) 4:1440-1448 !$#title Sequences that regulate the divergent GAL1-GAL10 promoter in !1Saccharomyces cerevisiae. !$#cross-references MUID:85036279; PMID:6092912 !$#accession S23294 !'##status translation not shown !'##molecule_type DNA !'##residues 1-29 ##label JOH !'##cross-references EMBL:K02115; NID:g171546; PIDN:AAA34621.1; !1PID:g171548 REFERENCE A94664 !$#authors Schlesinger, D.H.; Schell, M.A.; Wilson, D.B. !$#journal FEBS Lett. (1977) 83:45-47 !$#title The NH-2-terminal sequences of galactokinase from !1Escherichia coli and Saccharomyces cerevisiae. !$#cross-references MUID:78043686; PMID:200486 !$#accession B13446 !'##molecule_type protein !'##residues 2-5,'R',7,'R',9-12 ##label SCH !'##note residue 8 has also been sequenced as Glu REFERENCE S46551 !$#authors Smits, P.H.M.; de Haan, M.; Maat, C.; Grivell, L.A. !$#journal Yeast (1994) 10(Suppl.A):S75-S80 !$#title The complete sequence of a 33 kb fragment on the right arm !1of chromosome II from Saccharomyces cerevisiae reveals 16 !1open reading frames, including ten new open reading frames, !1five previously identified genes and a homologue of the SCO1 !1gene. !$#cross-references MUID:94378725; PMID:8091864 !$#accession S46551 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-45 ##label SMI !'##cross-references EMBL:X76078 !'##experimental_source strain S288C GENETICS !$#gene SGD:GAL1; MIPS:YBR020w !'##cross-references SGD:S0000224; MIPS:YBR020w !$#map_position 2R CLASSIFICATION #superfamily galactokinase KEYWORDS ATP; galactose metabolism; phosphotransferase; transmembrane !1protein FEATURE !$2-528 #product galactokinase #status experimental #label !8MAT\ !$68-84 #domain transmembrane #status predicted #label TM1\ !$166-189 #domain transmembrane #status predicted #label TM2\ !$281-297 #domain transmembrane #status predicted #label TM3 SUMMARY #length 528 #molecular-weight 57944 #checksum 943 SEQUENCE /// ENTRY S50990 #type complete TITLE galactokinase (EC 2.7.1.6) GAL3 [similarity] - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein D3205; protein PZA520; protein YDR009w ORGANISM #formal_name Saccharomyces cerevisiae DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 21-Jul-2000 ACCESSIONS S50990; S63416; S67822; A31197; S72107 REFERENCE S50976 !$#authors Murphy, L.; Richards, C.; Gentles, S.; Harris, D. !$#submission submitted to the EMBL Data Library, January 1995 !$#accession S50990 !'##molecule_type DNA !'##residues 1-520 ##label MUR !'##cross-references EMBL:Z48008; NID:g642799; PIDN:CAA88069.1; !1PID:g642814 REFERENCE S63416 !$#authors Eide, L.G.; Sander, C.; Prydz, H. !$#submission submitted to the EMBL Data Library, February 1996 !$#description Sequencing and analysis of a 35.4 kb region on the left arm !1of chromosome IV for Saccharomyces cerevisiae reveal 23 open !1reading frames. !$#accession S63416 !'##molecule_type DNA !'##residues 1-520 ##label EID !'##cross-references EMBL:X95966; NID:g1216215; PIDN:CAA65201.1; !1PID:g1216216 REFERENCE S67822 !$#authors Prydz, H.; Eide, L.G. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67822 !'##molecule_type DNA !'##residues 1-520 ##label PRY !'##cross-references EMBL:Z74305; NID:g1431425; PIDN:CAA98829.1; !1PID:g1431426; GSPDB:GN00004; MIPS:YDR009w !'##experimental_source strain S288C REFERENCE A31197 !$#authors Bajwa, W.; Torchia, T.E.; Hopper, J.E. !$#journal Mol. Cell. Biol. (1988) 8:3439-3447 !$#title Yeast regulatory gene GAL3: carbon regulation; UAS-Gal !1elements in common with GAL1, GAL2, GAL7, GAL10, GAL80, and !1MEL1; encoded protein strikingly similar to yeast and !1Escherichia coli galactokinases. !$#cross-references MUID:89096937; PMID:3062381 !$#accession A31197 !'##molecule_type DNA !'##residues 1-36,'NLILSLGLL',46-169,'GR',172-191, !1'ASQRLRSTMLESIMVVWIKQ',212-226,'MA',229,'T',231,'WPH',235, !1'QVSSIE',242-250,'ILCTR',256-257,'NRTLLHISLSCSL',268, !1'TLLYISTF',277,'REPCGPDTLG',288,'TISQGQ',295-302,'EIYGCLL', !1312,'PDTKTK',319,'NH',322,'ME',324,'SELVLNVYSRCYNWY', !1339-406,'I',408,410,'RTR',414,'LYR',418,'WPTNE' ##label BAJ !'##cross-references EMBL:M21615; NID:g171555; PIDN:AAA34625.1; !1PID:g171556 !'##note the differences throughout the sequence are due to frameshift !1errors REFERENCE S72107 !$#authors Eide, L.G.; Sander, C.; Prydz, H. !$#journal Yeast (1996) 12:1085-1090 !$#title Sequencing and analysis of a 35.4 kb region on the left arm !1of chromosome IV from Saccharomyces cerevisiae reveal 23 !1open reading frames. !$#cross-references MUID:97051598; PMID:8896275 !$#accession S72107 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-520 ##label EIW !'##cross-references EMBL:X95966; NID:g1216215; PIDN:CAA65201.1; !1PID:g1216216 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1February 1996 GENETICS !$#gene SGD:GAL3; MIPS:YDR009w !'##cross-references MIPS:YDR009w; SGD:S0002416 !$#map_position 4R FUNCTION !$#description functions as sensor and transducer of galactose signal in !1the induction pathway of GAL4 protein-activated genes CLASSIFICATION #superfamily galactokinase KEYWORDS ATP; galactose metabolism; phosphotransferase SUMMARY #length 520 #molecular-weight 58129 #checksum 2931 SEQUENCE /// ENTRY A41684 #type complete TITLE galactokinase (EC 2.7.1.6) - yeast (Kluyveromyces marxianus var. lactis) ORGANISM #formal_name Kluyveromyces marxianus var. lactis, Candida sphaerica DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A41684; S01409 REFERENCE A41684 !$#authors Meyer, J.; Walker-Jonah, A.; Hollenberg, C.P. !$#journal Mol. Cell. Biol. (1991) 11:5454-5461 !$#title Galactokinase encoded by GAL1 is a bifunctional protein !1required for induction of the GAL genes in Kluyveromyces !1lactis and is able to suppress the gal3 phenotype in !1Saccharomyces cerevisiae. !$#cross-references MUID:92017824; PMID:1922058 !$#accession A41684 !'##molecule_type DNA !'##residues 1-503 ##label MEY !'##cross-references GB:M74111; NID:g173272; PIDN:AAA35255.1; !1PID:g173273 !'##note the source is designated as Kluyveromyces lactis REFERENCE S01407 !$#authors Webster, T.D.; Dickson, R.C. !$#journal Nucleic Acids Res. (1988) 16:8192-8194 !$#title Nucleotide sequence of the galactose gene cluster of !1Kluyveromyces lactis. !$#cross-references MUID:88335573; PMID:3419917 !$#accession S01409 !'##molecule_type DNA !'##residues 1-56,'H',58,60-62,'S',64-124,'V',126-169,'T',171-178, !1'SQSSRMN' ##label WEB !'##cross-references EMBL:X07039; NID:g2817; PIDN:CAA30089.1; PID:g2818 !'##note the authors translated the codon TGG for residue 113 as Val GENETICS !$#gene GAL1 CLASSIFICATION #superfamily galactokinase KEYWORDS ATP; galactose metabolism; phosphotransferase SUMMARY #length 503 #molecular-weight 55805 #checksum 9224 SEQUENCE /// ENTRY KIECGG #type complete TITLE galactokinase (EC 2.7.1.6) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 01-Mar-2002 ACCESSIONS B23044; A13446; S53653; E64811 REFERENCE A93558 !$#authors Debouck, C.; Riccio, A.; Schumperli, D.; McKenney, K.; !1Jeffers, J.; Hughes, C.; Rosenberg, M.; Heusterspreute, M.; !1Brunel, F.; Davison, J. !$#journal Nucleic Acids Res. (1985) 13:1841-1853 !$#title Structure of the galactokinase gene of Escherichia coli, the !1last (?) gene of the gal operon. !$#cross-references MUID:85215584; PMID:3158881 !$#accession B23044 !'##molecule_type DNA !'##residues 1-382 ##label DEB !'##cross-references GB:X02306; NID:g41530; PIDN:CAA26172.1; PID:g41532 REFERENCE A94664 !$#authors Schlesinger, D.H.; Schell, M.A.; Wilson, D.B. !$#journal FEBS Lett. (1977) 83:45-47 !$#title The NH-2-terminal sequences of galactokinase from !1Escherichia coli and Saccharomyces cerevisiae. !$#cross-references MUID:78043686; PMID:200486 !$#accession A13446 !'##molecule_type protein !'##residues 2-20 ##label SCH REFERENCE S53653 !$#authors Bouffard, G.G.; Rudd, K.E.; Adhya, S.L. !$#journal J. Mol. Biol. (1994) 244:269-278 !$#title Dependence of lactose metabolism upon mutarotase encoded in !1the gal operon in Escherichia coli. !$#cross-references MUID:95055764; PMID:7966338 !$#accession S53653 !'##status preliminary !'##molecule_type DNA !'##residues 371-382 ##label BOU !'##cross-references GB:U13636; NID:g1620033; PIDN:AAB17019.1; !1PID:g1620034 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64811 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-382 ##label BLAT !'##cross-references GB:AE000178; GB:U00096; NID:g1786967; !1PIDN:AAC73844.1; PID:g1786972; UWGP:b0757 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene galK; galA !$#map_position 17 min FUNCTION !$#description catalyzes transfer of phosphate from ATP to galactose !$#pathway galactose catabolism !$#note first step CLASSIFICATION #superfamily galactokinase KEYWORDS ATP; galactose metabolism; phosphotransferase SUMMARY #length 382 #molecular-weight 41442 #checksum 3270 SEQUENCE /// ENTRY C37760 #type complete TITLE galactokinase (EC 2.7.1.6) - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C37760 REFERENCE A37760 !$#authors Houng, H.S.H.; Kopecko, D.J.; Baron, L.S. !$#journal J. Bacteriol. (1990) 172:4392-4398 !$#title Molecular cloning and physical and functional !1characterization of the Salmonella typhimurium and !1Salmonella typhi galactose utilization operons. !$#cross-references MUID:90330544; PMID:2198256 !$#accession C37760 !'##status preliminary !'##molecule_type DNA !'##residues 1-380 ##label HOU !'##cross-references GB:M33681; NID:g154046; PIDN:AAA27113.1; !1PID:g154049 CLASSIFICATION #superfamily galactokinase KEYWORDS ATP; phosphotransferase SUMMARY #length 380 #molecular-weight 41144 #checksum 8301 SEQUENCE /// ENTRY KISMG #type complete TITLE galactokinase (EC 2.7.1.6) - Streptomyces sp. ORGANISM #formal_name Streptomyces sp. DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 28-May-1999 ACCESSIONS C28669 REFERENCE A28669 !$#authors Adams, C.W.; Fornwald, J.A.; Schmidt, F.J.; Rosenberg, M.; !1Brawner, M.E. !$#journal J. Bacteriol. (1988) 170:203-212 !$#title Gene organization and structure of the Streptomyces lividans !1gal operon. !$#cross-references MUID:88086869; PMID:3335481 !$#accession C28669 !'##molecule_type DNA !'##residues 1-395 ##label ADA !'##cross-references GB:M18953; NID:g153259; PIDN:AAA26748.1; !1PID:g153262 !'##note the source is designated as Streptomyces lividans GENETICS !$#gene galK CLASSIFICATION #superfamily galactokinase KEYWORDS ATP; galactose metabolism; phosphotransferase SUMMARY #length 395 #molecular-weight 40948 #checksum 5698 SEQUENCE /// ENTRY S39690 #type complete TITLE galactokinase (EC 2.7.1.6) galK - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S39690; E69628 REFERENCE S39655 !$#authors Glaser, P.; Kunst, F.; Arnaud, M.; Coudart, M.P.; Gonzales, !1W.; Hullo, M.F.; Ionescu, M.; Lubochinsky, B.; Marcelino, !1L.; Moszer, I.; Presecan, E.; Santana, M.; Schneider, E.; !1Schweizer, J.; Vertes, A.; Rapoport, G.; Danchin, A. !$#journal Mol. Microbiol. (1993) 10:371-384 !$#title Bacillus subtilis genome project: cloning and sequencing of !1the 97 kb region from 325 degrees to 333 degrees. !$#cross-references MUID:95020537; PMID:7934828 !$#accession S39690 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-390 ##label GLA !'##cross-references EMBL:X73124; NID:g413923; PIDN:CAA51591.1; !1PID:g413959 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1993 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69628 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-390 ##label KUN !'##cross-references GB:Z99123; GB:AL009126; NID:g2636240; !1PIDN:CAB15846.1; PID:g2636355 !'##experimental_source strain 168 GENETICS !$#gene galK CLASSIFICATION #superfamily galactokinase galK KEYWORDS ATP; phosphotransferase SUMMARY #length 390 #molecular-weight 43521 #checksum 4673 SEQUENCE /// ENTRY A41894 #type complete TITLE fructokinase (EC 2.7.1.4) - Zymomonas mobilis ORGANISM #formal_name Zymomonas mobilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A41894; S27750 REFERENCE A41894 !$#authors Zembrzuski, B.; Chilco, P.; Liu, X.L.; Liu, J.; Conway, T.; !1Scopes, R. !$#journal J. Bacteriol. (1992) 174:3455-3460 !$#title Cloning, sequencing, and expression of the Zymomonas mobilis !1fructokinase gene and structural comparison of the enzyme !1with other hexose kinases. !$#cross-references MUID:92276320; PMID:1317376 !$#accession A41894 !'##status preliminary !'##molecule_type DNA !'##residues 1-301 ##label ZEM !'##cross-references EMBL:M97296; NID:g155582; PIDN:AAA27687.1; !1PID:g155583 !'##experimental_source ZM6, ATCC 29191 !'##note sequence extracted from NCBI backbone (NCBIP:104596) CLASSIFICATION #superfamily fructokinase; glucose kinase homology KEYWORDS ATP; phosphotransferase FEATURE !$62-199 #domain glucose kinase homology #label GKH SUMMARY #length 301 #molecular-weight 32609 #checksum 389 SEQUENCE /// ENTRY KIBSFF #type complete TITLE 6-phosphofructokinase (EC 2.7.1.11) - Bacillus stearothermophilus ALTERNATE_NAMES phosphofructokinase 1; phosphohexokinase ORGANISM #formal_name Bacillus stearothermophilus DATE 30-Sep-1980 #sequence_revision 14-Jul-1994 #text_change 24-Sep-1999 ACCESSIONS A27474; A00605; S29784 REFERENCE A27474 !$#authors French, B.A.; Chang, S.H. !$#journal Gene (1987) 54:65-71 !$#title Nucleotide sequence of the phosphofructokinase gene from !1Bacillus stearothermophilus and comparison with the !1homologous Escherichia coli gene. !$#cross-references MUID:87277434; PMID:2956156 !$#accession A27474 !'##molecule_type DNA !'##residues 1-319 ##label FRE !'##cross-references GB:M15643; NID:g143311; PIDN:AAA22656.1; !1PID:g143312 REFERENCE A91097 !$#authors Kolb, E.; Hudson, P.J.; Harris, J.I. !$#journal Eur. J. Biochem. (1980) 108:587-597 !$#title Phosphofructokinase: complete amino-acid sequence of the !1enzyme from Bacillus stearothermophilus. !$#cross-references MUID:81003881; PMID:6447595 !$#accession A00605 !'##molecule_type protein !'##residues 1-11,'N',13-35,39-42,'V',44-81,'E',83-94,'Q',96-224,'L', !1226-263,'SA',266-319 ##label KOL !'##note this enzyme is regulated by ADP and phosphoenolpyruvate, in !1contrast to the eukaryote enzyme, which is regulated by AMP, !1ATP, and citrate REFERENCE A93208 !$#authors Evans, P.R.; Hudson, P.J. !$#journal Nature (1979) 279:500-504 !$#title Structure and control of phosphofructokinase from Bacillus !1stearothermophilus. !$#cross-references MUID:79199719; PMID:156307 !$#contents annotation; X-ray crystallography, 2.4 angstroms !$#note each chain of the active enzyme consists of two domains; !1domain 1 consists approximately of residues 1-131 and !1251-301, and domain 2 consists approximately of residues !1132-250 and 302-316 !$#note the 6-phosphate group of fructose 6-phosphate (F6P) is bound !1by His-246 from one chain and Arg-159 and Arg-240 from an !1adjacent chain; the 1-hydroxyl group of F6P is apparently !1hydrogen-bonded to Asp-124; the sugar ring is bound by !1Arg-249, Met-166, Glu-219, and Asp-124. ATP is bound to !1domain 1 and to Arg-168 of domain 2. Asp-100 may be involved !1in binding Mg++ !$#note the main interaction with ADP appears to be with the !1beta-phosphate group, which is bound by Arg-151 from one !1chain and Arg-21 and Arg-25 from an adjacent chain; the !1ribose is bound by His-212 and Thr-155; the phosphate group !1of phosphoenolpyruvate appears to bind in the same place as !1the beta-phosphate group of ADP REFERENCE S29783 !$#authors Sakai, H.; Ohta, T. !$#journal Eur. J. Biochem. (1993) 211:851-859 !$#title Molecular cloning and nucleotide sequence of the gene for !1pyruvate kinase of Bacillus stearothermophilus and the !1production of the enzyme in Escherichia coli. Evidence that !1the genes for phosphofructokinase and pyruvate kinase !1constitute an operon. !$#cross-references MUID:93170322; PMID:8436141 !$#accession S29784 !'##molecule_type DNA !'##residues 300-319 ##label SAK !'##cross-references EMBL:D13095 GENETICS !$#gene Bs-pfk !$#start_codon GTG CLASSIFICATION #superfamily 6-phosphofructokinase; 6-phosphofructokinase 1 !1homology KEYWORDS allosteric regulation; ATP; glycolysis; homotetramer; !1phosphotransferase FEATURE !$4-278 #domain 6-phosphofructokinase 1 homology #label 6PF1 SUMMARY #length 319 #molecular-weight 34119 #checksum 9500 SEQUENCE /// ENTRY KIECFA #type complete TITLE 6-phosphofructokinase (EC 2.7.1.11) 1 - Escherichia coli (strain K-12) ALTERNATE_NAMES phosphofructokinase 1, isozyme 1; phosphohexokinase, isozyme 1 ORGANISM #formal_name Escherichia coli DATE 31-Dec-1988 #sequence_revision 10-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS G65197; A25206; S40859 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65197 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-320 ##label BLAT !'##cross-references GB:AE000466; GB:U00096; NID:g2367328; !1PIDN:AAC76898.1; PID:g1790350; UWGP:b3916 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A91144 !$#authors Hellinga, H.W.; Evans, P.R. !$#journal Eur. J. Biochem. (1985) 149:363-373 !$#title Nucleotide sequence and high-level expression of the major !1Escherichia coli phosphofructokinase. !$#cross-references MUID:85203917; PMID:3158524 !$#accession A25206 !'##molecule_type DNA !'##residues 1-73,'C',75-102,'DG',105-162,'P',164-316,'E',318,'M',320 !1##label HEL !'##cross-references GB:X02519; NID:g42365; PIDN:CAA26356.1; PID:g42366 !'##note this sequence has since been corrected REFERENCE A94501 !$#authors Evans, P.R. !$#submission submitted to the EMBL Data Library, October 1986 !$#contents annotation; corrections REFERENCE S40802 !$#authors Plunkett III, G.; Burland, V.; Daniels, D.L.; Blattner, F.R. !$#journal Nucleic Acids Res. (1993) 21:3391-3398 !$#title Analysis of the Escherichia coli genome. III. DNA sequence !1of the region from 87.2 to 89.2 minutes. !$#cross-references MUID:93347969; PMID:8346018 !$#accession S40859 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-320 ##label PLU !'##cross-references EMBL:L19201; NID:g304961; PIDN:AAB03048.1; !1PID:g305019 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1993 COMMENT The active enzyme catalyzes the key control step of !1glycolysis, the phosphorylation of fructose-6-phosphate by !1ATP to form fructose-1,6-bisphosphate. It is an allosteric !1enzyme activated by ADP and inhibited by !1phosphoenolpyruvate. COMMENT In E. coli this enzyme is responsible for 90% of the !1phosphofructokinase activity; the minor enzyme, !16-phosphofructokinase isozyme 2, is responsible for the !1remaining activity. The two enzymes are different !1kinetically; there is also no immunological !1cross-reactivity. GENETICS !$#gene pfkA !$#map_position 88 min CLASSIFICATION #superfamily 6-phosphofructokinase; 6-phosphofructokinase 1 !1homology KEYWORDS allosteric regulation; ATP; glycolysis; homotetramer; !1phosphotransferase FEATURE !$5-279 #domain 6-phosphofructokinase 1 homology #label 6PF1 SUMMARY #length 320 #molecular-weight 34842 #checksum 4067 SEQUENCE /// ENTRY JN0614 #type complete TITLE 6-phosphofructokinase (EC 2.7.1.11) - Lactococcus lactis subsp. lactis (strain LM0230) ALTERNATE_NAMES phosphofructokinase 1; phosphohexokinase ORGANISM #formal_name Lactococcus lactis subsp. lactis DATE 03-Feb-1994 #sequence_revision 03-May-1996 #text_change 03-Aug-2001 ACCESSIONS A40620; JN0614; E86791 REFERENCE A40620 !$#authors Llanos, R.M.; Harris, C.J.; Hillier, A.J.; Davidson, B.E. !$#journal J. Bacteriol. (1993) 175:2541-2551 !$#title Identification of a novel operon in Lactococcus lactis !1encoding three enzymes for lactic acid synthesis: !1phosphofructokinase, pyruvate kinase, and lactate !1dehydrogenase. !$#cross-references MUID:93239679; PMID:8478320 !$#accession A40620 !'##molecule_type DNA !'##residues 1-340 ##label LLA !'##cross-references GB:L07920; NID:g308856; PIDN:AAA99894.1; !1PID:g308857 !'##experimental_source strain LM0230 (a plasmid-free derivative of !1strain C2) !'##note sequence extracted from NCBI backbone (NCBIN:130458, !1NCBIP:130459) REFERENCE JN0614 !$#authors Xiao, Q.; Moore, C.H. !$#journal Biochem. Biophys. Res. Commun. (1993) 194:65-71 !$#title The primary structure of phosphofructokinase from !1Lactococcus lactis. !$#cross-references MUID:93326179; PMID:8333872 !$#accession JN0614 !'##molecule_type protein !'##residues 1-189,'S',191-193,'L',195-218,'IV',221-339 ##label XIA !'##experimental_source Lactococcus lactis C10 REFERENCE A86625 !$#authors Bolotin, A.; Wincker, P.; Mauger, S.; Jaillon, O.; Malarme, !1K.; Weissenbach, J.; Ehrlich, S.D.; Sorokin, A. !$#journal Genome Res. (2001) 11:731-753 !$#title The complete genome sequence of the lactic acid bacterium !1Lactococcus lactis ssp. lactis IL1403. !$#cross-references MUID:21235186; PMID:11337471 !$#accession E86791 !'##status preliminary !'##molecule_type DNA !'##residues 1-340 ##label STO !'##cross-references GB:AE005176; PID:g12724314; PIDN:AAK05431.1; !1GSPDB:GN00146 !'##experimental_source strain IL1403 GENETICS !$#gene pfk CLASSIFICATION #superfamily 6-phosphofructokinase; 6-phosphofructokinase 1 !1homology KEYWORDS ATP; glycolysis; phosphotransferase FEATURE !$4-279 #domain 6-phosphofructokinase 1 homology #label 6PF1 SUMMARY #length 340 #molecular-weight 35805 #checksum 2517 SEQUENCE /// ENTRY JQ1028 #type complete TITLE 6-phosphofructokinase (EC 2.7.1.11) 1 - Thermus aquaticus ALTERNATE_NAMES phosphofructokinase 1; phosphohexokinase ORGANISM #formal_name Thermus aquaticus DATE 10-Mar-1994 #sequence_revision 14-Jul-1994 #text_change 11-Jun-1999 ACCESSIONS JQ1028 REFERENCE JQ1028 !$#authors Xu, J.; Seki, M.; Denda, K.; Yoshida, M. !$#journal Biochem. Biophys. Res. Commun. (1991) 176:1313-1318 !$#title Molecular cloning of phosphofructokinase 1 gene from a !1thermophilic bacterium, Thermus thermophilus. !$#cross-references MUID:91248220; PMID:1828151 !$#accession JQ1028 !'##molecule_type DNA !'##residues 1-322 ##label XUA !'##cross-references GB:M71213; NID:g155116; PIDN:AAA27501.1; !1PID:g155117 GENETICS !$#gene pfk1 CLASSIFICATION #superfamily 6-phosphofructokinase; 6-phosphofructokinase 1 !1homology KEYWORDS allosteric regulation; ATP; glycolysis; phosphotransferase FEATURE !$4-281 #domain 6-phosphofructokinase 1 homology #label 6PF1 SUMMARY #length 322 #molecular-weight 33606 #checksum 5025 SEQUENCE /// ENTRY S77078 #type complete TITLE 6-phosphofructokinase (EC 2.7.1.11) pfkA-1 - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein sll0745 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S77078 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S77078 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-384 ##label KAN !'##cross-references EMBL:D64005; GB:AB001339; NID:g1001779; !1PIDN:BAA10770.1; PID:g1006614 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene pfkA-1 CLASSIFICATION #superfamily 6-phosphofructokinase; 6-phosphofructokinase 1 !1homology KEYWORDS glycolysis; phosphotransferase FEATURE !$6-326 #domain 6-phosphofructokinase 1 homology #label 6PF SUMMARY #length 384 #molecular-weight 41759 #checksum 2572 SEQUENCE /// ENTRY S74694 #type complete TITLE 6-phosphofructokinase (EC 2.7.1.11) pfkA-2 - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein sll1196 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S74694 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74694 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-361 ##label KAN !'##cross-references EMBL:D90901; GB:AB001339; NID:g1651897; !1PIDN:BAA16845.1; PID:g1651919 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene pfkA-2 CLASSIFICATION #superfamily 6-phosphofructokinase; 6-phosphofructokinase 1 !1homology KEYWORDS glycolysis; phosphotransferase FEATURE !$7-313 #domain 6-phosphofructokinase 1 homology #label 6PF SUMMARY #length 361 #molecular-weight 38588 #checksum 2462 SEQUENCE /// ENTRY E35270 #type complete TITLE 6-phosphofructokinase (EC 2.7.1.11) - Spiroplasma citri ALTERNATE_NAMES phosphofructokinase 1; phosphohexokinase ORGANISM #formal_name Spiroplasma citri DATE 17-Aug-1990 #sequence_revision 14-Jul-1994 #text_change 07-Dec-1999 ACCESSIONS E35270 REFERENCE A35270 !$#authors Chevalier, C.; Saillard, C.; Bove, J.M. !$#journal J. Bacteriol. (1990) 172:2693-2703 !$#title Organization and nucleotide sequences of the Spiroplasma !1citri genes for ribosomal protein S2, elongation factor Ts, !1spiralin, phosphofructokinase, pyruvate kinase, and an !1unidentified protein. !$#cross-references MUID:90236934; PMID:2139649 !$#accession E35270 !'##molecule_type DNA !'##residues 1-327 ##label CHE !'##cross-references GB:M31161; NID:g152884; PID:g152889 !'##note the authors translated the codon GCT for residue 195 as Ile GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily 6-phosphofructokinase; 6-phosphofructokinase 1 !1homology KEYWORDS ATP; phosphotransferase FEATURE !$5-280 #domain 6-phosphofructokinase 1 homology #label 6PF1 SUMMARY #length 327 #molecular-weight 35197 #checksum 6190 SEQUENCE /// ENTRY G64223 #type complete TITLE 6-phosphofructokinase (EC 2.7.1.11) - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 07-Dec-1999 ACCESSIONS G64223 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession G64223 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-323 ##label TIGR !'##cross-references GB:U39698; GB:L43967; NID:g1045891; PID:g1045901; !1TIGR:MG215 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily 6-phosphofructokinase; 6-phosphofructokinase 1 !1homology KEYWORDS glycolysis; phosphotransferase FEATURE !$4-282 #domain 6-phosphofructokinase 1 homology #label 6PF1 SUMMARY #length 323 #molecular-weight 35641 #checksum 8460 SEQUENCE /// ENTRY KIHUFM #type complete TITLE 6-phosphofructokinase (EC 2.7.1.11), muscle - human ALTERNATE_NAMES ATP:D-fructose-6-phosphate 1-phosphotransferase; phosphofructokinase 1; phosphohexokinase ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1990 #sequence_revision 13-Jan-1995 #text_change 11-Jun-1999 ACCESSIONS A91605; S00158; PH0223; A35290; I54035; A91380; JS0205 REFERENCE A91605 !$#authors Sharma, P.M.; Reddy, G.R.; Vora, S.; Babior, B.M.; !1McLachlan, A. !$#journal Gene (1989) 77:177-183 !$#title Cloning and expression of a human muscle phosphofructokinase !1cDNA. !$#cross-references MUID:89306675; PMID:2526045 !$#accession A91605 !'##molecule_type mRNA !'##residues 1-780 ##label SHA !'##cross-references GB:M26066; NID:g189854; PIDN:AAA60068.1; !1PID:g189855 REFERENCE S00158 !$#authors Nakajima, H.; Noguchi, T.; Yamasaki, T.; Kono, N.; Tanaka, !1T.; Tarui, S. !$#journal FEBS Lett. (1987) 223:113-116 !$#title Cloning of human muscle phosphofructokinase cDNA. !$#cross-references MUID:88030023; PMID:2822475 !$#accession S00158 !'##molecule_type mRNA !'##residues 1-780 ##label NA2 !'##cross-references EMBL:Y00698; NID:g32342; PIDN:CAA68692.1; !1PID:g32343 REFERENCE PH0223 !$#authors Yamasaki, T.; Nakajima, H.; Kono, N.; Hotta, K.; Yamada, K.; !1Imai, E.; Kuwajima, M.; Noguchi, T.; Tanaka, T.; Tarui, S. !$#journal Gene (1991) 104:277-282 !$#title Structure of the entire human muscle !1phosphofructokinase-encoding gene: a two-promoter system. !$#cross-references MUID:92009225; PMID:1833270 !$#accession PH0223 !'##status translation not shown !'##molecule_type DNA !'##residues 1-780 ##label YAM !'##cross-references GB:M59720; GB:M59721; GB:M59723; GB:M59724 !'##note nucleotide sequence is not complete REFERENCE A35290 !$#authors Sharma, P.M.; Reddy, G.R.; Babior, B.M.; McLachlan, A. !$#journal J. Biol. Chem. (1990) 265:9006-9010 !$#title Alternative splicing of the transcript encoding the human !1muscle isoenzyme of phosphofructokinase. !$#cross-references MUID:90264379; PMID:2140567 !$#accession A35290 !'##molecule_type mRNA !'##residues 272-281,313-322;672-681 ##label SH2 !'##cross-references GB:J05533; NID:g189856; PIDN:AAA79220.1; !1PID:g189857 !'##experimental_source fibroblast cell line IMR-90 !'##note this alternative splice form, lacking residues 282-312, is !1expressed at some level in all cells examined and at high !1levels in cell lines and skeletal muscle tissue !'##note the cited Genbank accession number, J05525, is not in release !1101.0 REFERENCE I54035 !$#authors Valdez, B.C.; Chen, Z.; Sosa, M.G.; Younathan, E.S.; Chang, !1S.H. !$#journal Gene (1989) 76:167-169 !$#title Human 6-phosphofructo-1-kinase gene has an additional intron !1upstream of start codon. !$#cross-references MUID:89306652; PMID:2526044 !$#accession I54035 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-28 ##label RES !'##cross-references GB:M24925; NID:g341282; PIDN:AAA36436.1; !1PID:g553609 GENETICS !$#gene GDB:PFKM !'##cross-references GDB:120277; OMIM:232800 !$#map_position 1cen-1q32 !$#introns 29/1; 53/3; 79/3; 143/1; 198/2; 213/2; 249/3; 281/3; 312/3; !1354/3; 376/2; 397/3; 447/3; 471/2; 500/3; 551/3; 606/3; 627/ !12; 664/3; 698/1; 733/2 !$#note defects in this gene can cause glycogenosis type VII CLASSIFICATION #superfamily human 6-phosphofructokinase; !16-phosphofructokinase 1 homology KEYWORDS alternative splicing; ATP; duplication; glycolysis; !1homotetramer; muscle; phosphotransferase FEATURE !$1-281,313-780 #product 6-phosphofructokinase, short form #status !8predicted #label ALT\ !$18-327 #domain 6-phosphofructokinase 1 homology #label 6PF1\ !$403-689 #domain 6-phosphofructokinase 1 homology #label 6PF2 SUMMARY #length 780 #molecular-weight 85182 #checksum 1235 SEQUENCE /// ENTRY KIRBF #type complete TITLE 6-phosphofructokinase (EC 2.7.1.11), muscle - rabbit ALTERNATE_NAMES phosphofructo-1-kinase; phosphofructokinase 1; phosphohexokinase ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 28-May-1986 #sequence_revision 14-Jul-1994 #text_change 11-Jun-1999 ACCESSIONS A26550; A00604; S03878 REFERENCE A26550 !$#authors Lee, C.P.; Kao, M.C.; French, B.A.; Putney, S.D.; Chang, !1S.H. !$#journal J. Biol. Chem. (1987) 262:4195-4199 !$#title The rabbit muscle phosphofructokinase gene. Implications for !1protein structure, function, and tissue specificity. !$#cross-references MUID:87166033; PMID:2951385 !$#accession A26550 !'##molecule_type DNA !'##residues 1-780 ##label LEE !'##cross-references GB:M14477; GB:J02702; NID:g165626; PIDN:AAA31441.1; !1PID:g165628 REFERENCE A00604 !$#authors Poorman, R.A.; Randolph, A.; Kemp, R.G.; Heinrikson, R.L. !$#journal Nature (1984) 309:467-469 !$#title Evolution of phosphofructokinase-gene duplication and !1creation of new effector sites. !$#cross-references MUID:84219739; PMID:6233492 !$#accession A00604 !'##molecule_type protein !'##residues 2-268,'S',270-442,'L',444-479,509-558,'I',560-565,567-780 !1##label POO REFERENCE S03878 !$#authors Valaitis, A.P.; Foe, L.G.; Kwiatkowska, D.; Latshaw, S.P.; !1Kemp, R.G. !$#journal Biochim. Biophys. Acta (1989) 995:187-194 !$#title The sites of phosphorylation of rabbit brain !1phosphofructo-1-kinase by cyclic AMP-dependent protein !1kinase. !$#cross-references MUID:89194250; PMID:2539199 !$#accession S03878 !'##status preliminary !'##molecule_type protein !'##residues 768-780 ##label VAL COMMENT The active enzyme catalyzes the key control step of !1glycolysis, the phosphorylation of fructose-6-phosphate by !1ATP to form fructose-1,6-bisphosphate in the presence of !1magnesium ion. It is an allosteric enzyme activated by ADP, !1AMP, or fructose bisphosphate and inhibited by ATP or !1citrate. GENETICS !$#introns 29/1; 53/3; 79/3; 143/1; 198/2; 213/2; 249/3; 281/3; 312/3; !1354/3; 376/2; 397/2; 447/3; 500/3; 551/3; 606/3; 627/2; 664/ !13; 698/1; 733/2 CLASSIFICATION #superfamily human 6-phosphofructokinase; !16-phosphofructokinase 1 homology KEYWORDS acetylated amino end; allosteric regulation; ATP; !1duplication; glycolysis; homotetramer; phosphoprotein; !1phosphotransferase FEATURE !$2-780 #product 6-phosphofructokinase #status experimental !8#label MAT\ !$18-327 #domain 6-phosphofructokinase 1 homology #label 6PF1\ !$403-689 #domain 6-phosphofructokinase 1 homology #label 6PF2\ !$2 #modified_site acetylated amino end (Thr) (in mature !8form) #status experimental\ !$775 #binding_site phosphate (Ser) (covalent) (by !8cAMP-dependent kinase) #status experimental SUMMARY #length 780 #molecular-weight 85203 #checksum 2678 SEQUENCE /// ENTRY A33639 #type complete TITLE 6-phosphofructokinase (EC 2.7.1.11), hepatic - human ALTERNATE_NAMES ATP:D-fructose-6-phosphate 1-phosphotransferase ORGANISM #formal_name Homo sapiens #common_name man DATE 09-Mar-1990 #sequence_revision 14-Jul-1994 #text_change 02-Sep-1997 ACCESSIONS A33639 REFERENCE A33639 !$#authors Levanon, D.; Danciger, E.; Dafni, N.; Bernstein, Y.; Elson, !1A.; Moens, W.; Brandeis, M.; Groner, Y. !$#journal DNA (1989) 8:733-743 !$#title The primary structure of human liver type !1phosphofructokinase and its comparison with other types of !1PFK. !$#cross-references MUID:90126227; PMID:2533063 !$#accession A33639 !'##molecule_type mRNA !'##residues 1-780 ##label LEV !'##cross-references GB:X15573 GENETICS !$#gene GDB:PFKL !'##cross-references GDB:120276; OMIM:171860 !$#map_position 21q22.3-21q22.3 CLASSIFICATION #superfamily human 6-phosphofructokinase; !16-phosphofructokinase 1 homology KEYWORDS ATP; phosphotransferase FEATURE !$18-327 #domain 6-phosphofructokinase 1 homology #label 6PF1\ !$402-688 #domain 6-phosphofructokinase 1 homology #label 6PF2 SUMMARY #length 780 #molecular-weight 85128 #checksum 5117 SEQUENCE /// ENTRY A31070 #type complete TITLE 6-phosphofructokinase (EC 2.7.1.11), hepatic - mouse ALTERNATE_NAMES ATP:D-fructose-6-phosphate 1-phosphotransferase ORGANISM #formal_name Mus musculus #common_name house mouse DATE 19-Jan-1989 #sequence_revision 14-Jul-1994 #text_change 11-Jun-1999 ACCESSIONS A31070 REFERENCE A31070 !$#authors Gehnrich, S.C.; Gekakis, N.; Sul, H.S. !$#journal J. Biol. Chem. (1988) 263:11755-11759 !$#title Liver (B-type) phosphofructokinase mRNA. Cloning, structure, !1and expression. !$#cross-references MUID:88298847; PMID:2969893 !$#accession A31070 !'##molecule_type mRNA !'##residues 1-780 ##label GEH !'##cross-references GB:J03928; NID:g200297; PIDN:AAA20076.1; !1PID:g515965 CLASSIFICATION #superfamily human 6-phosphofructokinase; !16-phosphofructokinase 1 homology KEYWORDS ATP; phosphotransferase FEATURE !$18-327 #domain 6-phosphofructokinase 1 homology #label 6PF1\ !$402-688 #domain 6-phosphofructokinase 1 homology #label 6PF2 SUMMARY #length 780 #molecular-weight 85300 #checksum 2140 SEQUENCE /// ENTRY A45617 #type complete TITLE 6-phosphofructokinase (EC 2.7.1.11) - nematode (Haemonchus contortus) ALTERNATE_NAMES phosphofructokinase 1; phosphohexokinase ORGANISM #formal_name Haemonchus contortus DATE 03-Feb-1994 #sequence_revision 14-Jul-1994 #text_change 11-Jun-1999 ACCESSIONS A45617 REFERENCE A45617 !$#authors Klein, R.D.; Olson, E.R.; Favreau, M.A.; Winterrowd, C.A.; !1Hatzenbuhler, N.T.; Shea, M.H.; Nulf, S.C.; Geary, T.G. !$#journal Mol. Biochem. Parasitol. (1991) 48:17-26 !$#title Cloning of a cDNA encoding phosphofructokinase from !1Haemonchus contortus. !$#cross-references MUID:92140452; PMID:1838137 !$#accession A45617 !'##molecule_type mRNA !'##residues 1-789 ##label KLE !'##cross-references GB:M59805; NID:g159184; PIDN:AAA29181.1; !1PID:g159185 !'##experimental_source strain DF1020 !'##note this sequence is inconsistent with the nucleotide translation !'##note sequence extracted from NCBI backbone (NCBIN:79638, !1NCBIP:79639) CLASSIFICATION #superfamily human 6-phosphofructokinase; !16-phosphofructokinase 1 homology KEYWORDS ATP; glycolysis; phosphoprotein; phosphotransferase FEATURE !$34-342 #domain 6-phosphofructokinase 1 homology #label 6PF1\ !$421-708 #domain 6-phosphofructokinase 1 homology #label 6PF2 SUMMARY #length 789 #molecular-weight 87184 #checksum 6380 SEQUENCE /// ENTRY JQ0016 #type complete TITLE 6-phosphofructokinase (EC 2.7.1.11) alpha chain - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES phosphofructokinase 1; phosphohexokinase; protein 194; protein G8599; protein YGR240c ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1990 #sequence_revision 14-Jul-1994 #text_change 23-Mar-2001 ACCESSIONS JQ0016; S38963; S57708; S64566; S64564; S63924 REFERENCE A91608 !$#authors Heinisch, J.; Ritzel, R.G.; von Borstel, R.C.; Aguilera, A.; !1Rodicio, R.; Zimmermann, F.K. !$#journal Gene (1989) 78:309-321 !$#title The phosphofructokinase genes of yeast evolved from two !1duplication events. !$#cross-references MUID:89378757; PMID:2528496 !$#accession JQ0016 !'##molecule_type DNA !'##residues 1-987 ##label HEI !'##cross-references EMBL:M26943; NID:g172137; PIDN:AAA34859.1; !1PID:g172138 REFERENCE S38963 !$#authors Kopperschlaeger, G.; Baer, J.; Stellwagen, E. !$#journal Eur. J. Biochem. (1993) 217:527-533 !$#title Limited proteolysis of yeast phosphofructokinase. Sequence !1locations of cleavage sites created by the actions of !1different proteinases. !$#cross-references MUID:94039086; PMID:8223596 !$#accession S38963 !'##molecule_type protein !'##residues 1-6;90-97;197-205;914-921 ##label KOP REFERENCE S57680 !$#authors van der Aart, Q.J.M.; Kleine, K.; Steensma, H.Y. !$#submission submitted to the EMBL Data Library, June 1995 !$#description Sequence analysis of the 43 KB !1CRM1-YLM9-PET54-SMI1-PHO81-YHB4-PFK1 region from the right !1arm of Saccharomyces cerevisiae chromosome VII. !$#accession S57708 !'##molecule_type DNA !'##residues 794-987 ##label VAN !'##cross-references EMBL:X87941; NID:g886908; PIDN:CAA61193.1; !1PID:g886937 !'##experimental_source strain S288C REFERENCE S64565 !$#authors Guerreiro, P.; Barreiros, T.; Azevedo, D.; !1Rodrigues-Pousada, C. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64566 !'##molecule_type DNA !'##residues 1-987 ##label GUE !'##cross-references EMBL:Z73025; NID:g1323434; PIDN:CAA97268.1; !1PID:g1323435; GSPDB:GN00007; MIPS:YGR240c !'##experimental_source strain S288C REFERENCE S64541 !$#authors van der Aart, Q.J.M.; Steensma, H.Y. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64564 !'##molecule_type DNA !'##residues 794-987 ##label VAW !'##cross-references EMBL:Z73025; GSPDB:GN00007; MIPS:YGR240c !'##experimental_source strain S288C REFERENCE S63896 !$#authors van der Aart, Q.J.M.; Kleine, K.; Steensma, H.Y. !$#journal Yeast (1996) 12:385-390 !$#title Sequence analysis of the 43 kb !1CRM1-YLM9-PET54-DIE2-SMI1-PHO81-YHB4-PFK1 region from the !1right arm of Saccharomyces cerevisiae chromosome VII. !$#cross-references MUID:96267763; PMID:8701610 !$#accession S63924 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 794-987 ##label VAF !'##cross-references EMBL:X87941; NID:g886908; PIDN:CAA61193.1; !1PID:g886937 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1995 COMMENT Phosphofructokinase is composed of four alpha chains and !1four beta chains. GENETICS !$#gene SGD:PFK1; MIPS:YGR240c !'##cross-references SGD:S0003472; MIPS:YGR240c !$#map_position 7R CLASSIFICATION #superfamily human 6-phosphofructokinase; !16-phosphofructokinase 1 homology KEYWORDS ATP; glycolysis; phosphotransferase FEATURE !$208-517 #domain 6-phosphofructokinase 1 homology #label 6PF1\ !$596-888 #domain 6-phosphofructokinase 1 homology #label 6PF2\ !$225,229 #binding_site AMP, allosteric (Arg) #status !8predicted\ !$309,310 #binding_site ATP (Asp, Gly) #status predicted\ !$356 #active_site Asp #status predicted\ !$398,455,482,488, !$491,729 #binding_site fructose-6-phosphate (Met, Glu, Lys, !8His, Arg, Gly) #status predicted\ !$751 #binding_site citrate, allosteric (Lys) #status !8predicted SUMMARY #length 987 #molecular-weight 107969 #checksum 4812 SEQUENCE /// ENTRY JQ0017 #type complete TITLE 6-phosphofructokinase (EC 2.7.1.11) beta chain - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES phosphofructokinase 1; phosphohexokinase; protein YM8325.06c; protein YMR205c ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1990 #sequence_revision 01-Mar-1996 #text_change 12-Nov-1999 ACCESSIONS S59446; JQ0017; S38964 REFERENCE S59441 !$#authors Odell, C.; Bowman, S. !$#submission submitted to the EMBL Data Library, March 1995 !$#accession S59446 !'##molecule_type DNA !'##residues 1-959 ##label ODE !'##cross-references EMBL:Z48755; NID:g736296; PIDN:CAA88646.1; !1PID:g736302; GSPDB:GN00013; MIPS:YMR205c !'##experimental_source strain AB972 REFERENCE A91608 !$#authors Heinisch, J.; Ritzel, R.G.; von Borstel, R.C.; Aguilera, A.; !1Rodicio, R.; Zimmermann, F.K. !$#journal Gene (1989) 78:309-321 !$#title The phosphofructokinase genes of yeast evolved from two !1duplication events. !$#cross-references MUID:89378757; PMID:2528496 !$#accession JQ0017 !'##molecule_type DNA !'##residues 1-136,'G',138-879,'E',881-959 ##label HEI !'##cross-references EMBL:M26943 REFERENCE S38963 !$#authors Kopperschlaeger, G.; Baer, J.; Stellwagen, E. !$#journal Eur. J. Biochem. (1993) 217:527-533 !$#title Limited proteolysis of yeast phosphofructokinase. Sequence !1locations of cleavage sites created by the actions of !1different proteinases. !$#cross-references MUID:94039086; PMID:8223596 !$#accession S38964 !'##molecule_type protein !'##residues 2-12;181-185;192-197 ##label KOP GENETICS !$#gene SGD:PFK2; MIPS:YMR205c !'##cross-references SGD:S0004818; MIPS:YMR205c !$#map_position 13R COMPLEX heterooctamer; composed of four alpha chains and four beta !1chains CLASSIFICATION #superfamily human 6-phosphofructokinase; !16-phosphofructokinase 1 homology KEYWORDS ATP; glycolysis; heterooctamer; phosphotransferase FEATURE !$199-510 #domain 6-phosphofructokinase 1 homology #label 6PF1\ !$589-882 #domain 6-phosphofructokinase 1 homology #label 6PF2\ !$216,220 #binding_site AMP, allosteric (Arg) #status !8predicted\ !$301,302 #binding_site ATP (Asp, Gly) #status predicted\ !$348 #active_site Asp #status predicted\ !$390,447,475,481, !$484,723 #binding_site fructose-6-phosphate (Met, Glu, Arg, !8His, Arg, Gly) #status predicted\ !$745 #binding_site citrate, allosteric (Lys) #status !8predicted SUMMARY #length 959 #molecular-weight 104617 #checksum 5696 SEQUENCE /// ENTRY A41169 #type complete TITLE diphosphate-fructose-6-phosphate 1-phosphotransferase (EC 2.7.1.90) - Propionibacterium freudenreichii ALTERNATE_NAMES 6-phosphofructokinase (pyrophosphate) ORGANISM #formal_name Propionibacterium freudenreichii DATE 17-Jul-1992 #sequence_revision 14-Jul-1994 #text_change 03-Jun-2002 ACCESSIONS A41169 REFERENCE A41169 !$#authors Ladror, U.S.; Gollapudi, L.; Tripathi, R.L.; Latshaw, S.P.; !1Kemp, R.G. !$#journal J. Biol. Chem. (1991) 266:16550-16555 !$#title Cloning, sequencing, and expression of !1pyrophosphate-dependent phosphofructokinase from !1Propionibacterium freudenreichii. !$#cross-references MUID:91358443; PMID:1653240 !$#accession A41169 !'##molecule_type DNA !'##residues 1-404 ##label LAD !'##cross-references GB:M67447; NID:g150930; PIDN:AAA25675.1; !1PID:g150931 COMMENT This is an example of a nonallosteric, !1pyrophosphate-dependent phosphfructokinase. CLASSIFICATION #superfamily pyrophosphate-fructose-6-phosphate !11-phosphotransferase; 6-phosphofructokinase 1 homology KEYWORDS phosphotransferase FEATURE !$5-322 #domain 6-phosphofructokinase 1 homology #label 6PF1 SUMMARY #length 404 #molecular-weight 43245 #checksum 3940 SEQUENCE /// ENTRY A71366 #type complete TITLE diphosphate-fructose-6-phosphate 1-phosphotransferase (EC 2.7.1.90) - syphilis spirochete ALTERNATE_NAMES 6-phosphofructokinase (pyrophosphate) ORGANISM #formal_name Treponema pallidum subsp. pallidum #common_name syphilis spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS A71366 REFERENCE A71250 !$#authors Fraser, C.M.; Norris, S.J.; Weinstock, G.M.; White, O.; !1Sutton, G.G.; Dodson, R.; Gwinn, M.; Hickey, E.K.; Clayton, !1R.; Ketchum, K.A.; Sodergren, E.; Hardham, J.M.; McLeod, !1M.P.; Salzberg, S.; Peterson, J.; Khalak, H.; Richardson, !1D.; Howell, J.K.; Chidambaram, M.; Utterback, T.; McDonald, !1L.; Artiach, P.; Bowman, C.; Cotton, M.D.; Fujii, C.; !1Garland, S.; Hatch, B.; Horst, K.; Roberts, K.; Watthey, L.; !1Weidman, J.; Smith, H.O.; Venter, J.C. !$#journal Science (1998) 281:375-388 !$#title Complete genome sequence of Treponema pallidum, the syphilis !1spirochete. !$#cross-references MUID:98332770; PMID:9665876 !$#accession A71366 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-461 ##label COL !'##cross-references GB:AE001195; GB:AE000520; NID:g3322366; !1PIDN:AAC26556.1; PID:g3322371 !'##experimental_source strain Nichols GENETICS !$#gene TP0108 CLASSIFICATION #superfamily pyrophosphate-fructose-6-phosphate !11-phosphotransferase; 6-phosphofructokinase 1 homology KEYWORDS phosphotransferase FEATURE !$83-409 #domain 6-phosphofructokinase 1 homology #label 6PF SUMMARY #length 461 #molecular-weight 50161 #checksum 6072 SEQUENCE /// ENTRY F70190 #type complete TITLE probable diphosphate-fructose-6-phosphate 1-phosphotransferase (EC 2.7.1.90) - Lyme disease spirochete ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS F70190 REFERENCE A70100 !$#authors Fraser, C.M.; Casjens, S.; Huang, W.M.; Sutton, G.G.; !1Clayton, R.; Lathigra, R.; White, O.; Ketchum, K.A.; Dodson, !1R.; Hickey, E.K.; Gwinn, M.; Dougherty, B.; Tomb, J.F.; !1Fleischmann, R.D.; Richardson, D.; Peterson, J.; Kerlavage, !1A.R.; Quackenbush, J.; Salzberg, S.; Hanson, M.; Vugt, R.V.; !1Palmer, N.; Adams, M.D.; Gocayne, J.; Weidman, J.; !1Utterback, T.; Watthey, L.; McDonald, L.; Artiach, P.; !1Bowman, C.; Garland, S.; Fujii, C.; Cotton, M.D.; Horst, K.; !1Roberts, K.; Hatch, B.; Smith, H.O.; Venter, J.C. !$#journal Nature (1997) 390:580-586 !$#title Genomic sequence of a Lyme disease spirochaete, Borrelia !1burgdorferi. !$#cross-references MUID:98065943; PMID:9403685 !$#accession F70190 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-448 ##label KLE !'##cross-references GB:AE001172; GB:AE000783; NID:g2688654; !1PIDN:AAC67070.1; PID:g2688657; TIGR:BB0727 !'##experimental_source strain B31 CLASSIFICATION #superfamily pyrophosphate-fructose-6-phosphate !11-phosphotransferase; 6-phosphofructokinase 1 homology KEYWORDS phosphotransferase FEATURE !$82-398 #domain 6-phosphofructokinase 1 homology #label 6PF SUMMARY #length 448 #molecular-weight 49887 #checksum 7482 SEQUENCE /// ENTRY S49458 #type complete TITLE diphosphate-fructose-6-phosphate 1-phosphotransferase (EC 2.7.1.90) [validated] - Entamoeba histolytica ALTERNATE_NAMES 6-phosphofructokinase (pyrophosphate) ORGANISM #formal_name Entamoeba histolytica DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 03-Jun-2002 ACCESSIONS S49458; S68243; S52082 REFERENCE S49458 !$#authors Bruchhaus, I. !$#submission submitted to the EMBL Data Library, October 1994 !$#accession S49458 !'##molecule_type mRNA !'##residues 1-436 ##label BRW !'##cross-references EMBL:X82173; NID:g558573; PIDN:CAA57659.1; !1PID:g558574 REFERENCE S68243 !$#authors Bruchhaus, I.; Jacobs, T.; Denart, M.; Tannich, E. !$#journal Biochem. J. (1996) 316:57-63 !$#title Pyrophosphate-dependent phosphofructokinase of Entamoeba !1histolytica: molecular cloning, recombinant expression and !1inhibition by pyrophosphate analogues. !$#cross-references MUID:96235172; PMID:8645233 !$#accession S68243 !'##molecule_type mRNA !'##residues 1-429,'T',431-436 ##label BRU !'##cross-references EMBL:X82173; NID:g558573 !'##note the authors present evidence of the enzymes activity !'##note the sequence is revised in GenBank entry EHPPIPFK, release 114, !1(PIDN:CAA57659.1) REFERENCE S52082 !$#authors Huang, M.; Albach, R.A.; Chang, K.P.; Tripathi, R.L.; Kemp, !1R.G. !$#journal Biochim. Biophys. Acta (1995) 1260:215-217 !$#title Cloning and sequencing a putative pyrophosphate-dependent !1phosphofructokinase gene from Entamoeba histolytica. !$#cross-references MUID:95143279; PMID:7841199 !$#accession S52082 !'##status preliminary !'##molecule_type DNA !'##residues 46-108,'R',110-416,'NELI',435,'MDHYIL' ##label HUA !'##cross-references EMBL:U12513; NID:g529008; PIDN:AAA92671.1; !1PID:g529009 GENETICS !$#gene Eh/PPi-PFK CLASSIFICATION #superfamily pyrophosphate-fructose-6-phosphate !11-phosphotransferase; 6-phosphofructokinase 1 homology KEYWORDS phosphotransferase SUMMARY #length 436 #molecular-weight 47570 #checksum 1316 SEQUENCE /// ENTRY KIECFB #type complete TITLE 6-phosphofructokinase (EC 2.7.1.11) isozyme 2 - Escherichia coli (strain K-12) ALTERNATE_NAMES phosphofructokinase 1 isozyme 2; phosphohexokinase isozyme 2 ORGANISM #formal_name Escherichia coli DATE 28-Dec-1987 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS C64931; A24950; I56378; A05220 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64931 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-309 ##label BLAT !'##cross-references GB:AE000267; GB:U00096; NID:g1788011; !1PIDN:AAC74793.1; PID:g1788017; UWGP:b1723 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A91513 !$#authors Daldal, F. !$#journal Gene (1984) 28:337-342 !$#title Nucleotide sequence of gene pfkB encoding the minor !1phosphofructokinase of Escherichia coli K-12. !$#cross-references MUID:84262485; PMID:6235149 !$#accession A24950 !'##molecule_type DNA !'##residues 1-25,'ENCAVPHRCSN',37-40,42-154,'LRKNK',160,'SAASSTVL',169, !1'QG',172-244,'AL',247-256,'RL',259-309 ##label DAL !'##cross-references GB:K02500; NID:g147151; PIDN:AAA24321.1; !1PID:g147152 !'##experimental_source strain K12 REFERENCE I56378 !$#authors Daldal, F. !$#journal J. Mol. Biol. (1983) 168:285-305 !$#title Molecular cloning of the gene for phosphofructokinase-2 of !1Escherichia coli and the nature of a mutation, pfkB1, !1causing a high level of the enzyme. !$#cross-references MUID:83294514; PMID:6310120 !$#accession I56378 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-25,'ENCAVPHRCSN',37-38 ##label RES !'##cross-references GB:K00128; NID:g147149; PIDN:AAA24320.1; !1PID:g147150 COMMENT This enzyme is not to be confused with !16-phosphofructo-2-kinase (EC 2.7.1.105), which is also !1called phosphofructokinase 2. GENETICS !$#gene pfkB !$#map_position 38 min COMPLEX homotetramer FUNCTION !$#description catalyzes phosphorylation of fructose 6-phosphate to !1fructose 1,6-bisphosphate !$#pathway glycolysis CLASSIFICATION #superfamily 6-phosphofructokinase 2 KEYWORDS glycolysis; phosphotransferase SUMMARY #length 309 #molecular-weight 32456 #checksum 8691 SEQUENCE /// ENTRY A39407 #type complete TITLE 1-phosphofructokinase (EC 2.7.1.56) - Rhodobacter capsulatus ORGANISM #formal_name Rhodobacter capsulatus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A39407; A37852 REFERENCE A39407 !$#authors Wu, L.F.; Reizer, A.; Reizer, J.; Cai, B.; Tomich, J.M.; !1Saier Jr., M.H. !$#journal J. Bacteriol. (1991) 173:3117-3127 !$#title Nucleotide sequence of the Rhodobacter capsulatus fruK gene, !1which encodes fructose-1-phosphate kinase: evidence for a !1kinase superfamily including both phosphofructokinases of !1Escherichia coli. !$#cross-references MUID:91216983; PMID:1850730 !$#accession A39407 !'##status preliminary !'##molecule_type DNA !'##residues 1-316 ##label WUA !'##cross-references GB:M62785; NID:g151929; PIDN:AAA26120.1; !1PID:g151931; GB:M68879; GB:X53150; NID:g46018; PID:g46020 REFERENCE A37852 !$#authors Wu, L.F.; Saier Jr., M.H. !$#journal J. Bacteriol. (1990) 172:7167-7178 !$#title Nucleotide sequence of the fruA gene, encoding the fructose !1permease of the Rhodobacter capsulatus phosphotransferase !1system, and analyses of the deduced protein sequence. !$#cross-references MUID:91072273; PMID:2254279 !$#accession A37852 !'##status preliminary !'##molecule_type DNA !'##residues 288-316 ##label WU2 !'##cross-references GB:M62785; GB:M68879; GB:M53150 CLASSIFICATION #superfamily 6-phosphofructokinase 2 KEYWORDS phosphotransferase SUMMARY #length 316 #molecular-weight 31232 #checksum 4530 SEQUENCE /// ENTRY KIECRB #type complete TITLE ribokinase (EC 2.7.1.15) [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 01-Mar-2002 ACCESSIONS A26305; A65179 REFERENCE A26305 !$#authors Hope, J.N.; Bell, A.W.; Hermodson, M.A.; Groarke, J.M. !$#journal J. Biol. Chem. (1986) 261:7663-7668 !$#title Ribokinase from Escherichia coli K12. Nucleotide sequence !1and overexpression of the rbsK gene and purification of !1ribokinase. !$#cross-references MUID:86224052; PMID:3011794 !$#accession A26305 !'##molecule_type DNA !'##residues 1-309 ##label HOP !'##cross-references GB:M13169; GB:M13517; NID:g147511; PIDN:AAA51476.1; !1PID:g147516 !'##experimental_source strain K12 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65179 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-309 ##label BLAT !'##cross-references GB:AE000452; GB:U00096; NID:g1790188; !1PIDN:AAC76775.1; PID:g1790193; UWGP:b3752 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene rbsK !$#map_position 84 min COMPLEX homodimer (in solution); [validated, MUID:98046763] FUNCTION !$#description EC 2.7.1.15 [validated, MUID:86224052]; catalyzes the !1phosphorylation of ribose to ribose 5-phosphate using ATP, !1the first step in ribose metabolism CLASSIFICATION #superfamily ribokinase KEYWORDS ATP; phosphotransferase; ribose metabolism SUMMARY #length 309 #molecular-weight 32290 #checksum 8722 SEQUENCE /// ENTRY KIBYRB #type complete TITLE ribokinase (EC 2.7.1.15) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YCR036w; protein YCR523 ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jun-2000 ACCESSIONS S12918; S19448 REFERENCE S12916 !$#authors Thierry, A.; Fairhead, C.; Dujon, B. !$#journal Yeast (1990) 6:521-534 !$#title The complete sequence of the 8.2 kb segment left of MAT on !1chromosome III reveals five ORFs, including a gene for a !1yeast ribokinase. !$#cross-references MUID:91181345; PMID:1964349 !$#accession S12918 !'##molecule_type DNA !'##residues 1-333 ##label THI !'##cross-references EMBL:X56909; NID:g4489; PIDN:CAA40228.1; PID:g4492 REFERENCE S19445 !$#authors Herbert, C.J.; Jia, Y.; Slonimski, P.P. !$#submission submitted to the Protein Sequence Database, March 1992 !$#accession S19448 !'##molecule_type DNA !'##residues 1-333 ##label DUJ !'##cross-references EMBL:X59720; NID:g1907116; PIDN:CAA42303.1; !1PID:g1907178; GSPDB:GN00003; MIPS:YCR036w GENETICS !$#gene SGD:RBK1; MIPS:YCR036w !'##cross-references SGD:S0000632; MIPS:YCR036w !$#map_position 3R CLASSIFICATION #superfamily ribokinase KEYWORDS phosphotransferase SUMMARY #length 333 #molecular-weight 36984 #checksum 5645 SEQUENCE /// ENTRY S18523 #type complete TITLE fructokinase (EC 2.7.1.4) - Klebsiella pneumoniae ORGANISM #formal_name Klebsiella pneumoniae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S18523; S16037 REFERENCE S18523 !$#authors Aulkemeyer, P.; Ebner, R.; Heilenmann, G.; Jahreis, K.; !1Schmid, K.; Wrieden, S.; Lengeler, J.W. !$#journal Mol. Microbiol. (1991) 5:2913-2922 !$#title Molecular analysis of two fructokinases involved in sucrose !1metabolism of enteric bacteria. !$#cross-references MUID:92236409; PMID:1809835 !$#accession S18523 !'##molecule_type DNA !'##residues 1-307 ##label AUL !'##cross-references EMBL:X61004; NID:g43929; PIDN:CAA43322.1; !1PID:g43930 GENETICS !$#gene scrK CLASSIFICATION #superfamily ribokinase KEYWORDS phosphotransferase SUMMARY #length 307 #molecular-weight 32343 #checksum 8194 SEQUENCE /// ENTRY S18524 #type complete TITLE fructokinase (EC 2.7.1.4) - Salmonella typhimurium plasmid pUR400 ORGANISM #formal_name Salmonella typhimurium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S18524; S16044 REFERENCE S18523 !$#authors Aulkemeyer, P.; Ebner, R.; Heilenmann, G.; Jahreis, K.; !1Schmid, K.; Wrieden, S.; Lengeler, J.W. !$#journal Mol. Microbiol. (1991) 5:2913-2922 !$#title Molecular analysis of two fructokinases involved in sucrose !1metabolism of enteric bacteria. !$#cross-references MUID:92236409; PMID:1809835 !$#accession S18524 !'##molecule_type DNA !'##residues 1-307 ##label AUL !'##cross-references EMBL:X61005; NID:g47927; PIDN:CAA43323.1; !1PID:g47928 GENETICS !$#gene scrK !$#genome plasmid CLASSIFICATION #superfamily ribokinase KEYWORDS phosphotransferase SUMMARY #length 307 #molecular-weight 32916 #checksum 3362 SEQUENCE /// ENTRY JQ0782 #type complete TITLE fructokinase (EC 2.7.1.4) - Vibrio alginolyticus ORGANISM #formal_name Vibrio alginolyticus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JQ0782 REFERENCE JQ0781 !$#authors Blatch, G.L.; Scholle, R.R.; Woods, D.R. !$#journal Gene (1990) 95:17-23 !$#title Nucleotide sequence and analysis of the Vibrio alginolyticus !1sucrose uptake-encoding region. !$#cross-references MUID:91071601; PMID:2174811 !$#accession JQ0782 !'##molecule_type DNA !'##residues 1-307 ##label BLA !'##cross-references GB:M76768; GB:M30194; NID:g155261; PIDN:AAA27556.1; !1PID:g155263 CLASSIFICATION #superfamily ribokinase KEYWORDS phosphotransferase SUMMARY #length 307 #molecular-weight 33045 #checksum 2381 SEQUENCE /// ENTRY S52161 #type complete TITLE probable fructokinase (EC 2.7.1.4) - Escherichia coli ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S52161 REFERENCE S52160 !$#authors Bockmann, J. !$#submission submitted to the EMBL Data Library, September 1994 !$#accession S52161 !'##status preliminary !'##molecule_type DNA !'##residues 1-305 ##label BOC !'##cross-references EMBL:X81461; NID:g608705; PIDN:CAA57218.1; !1PID:g608707 CLASSIFICATION #superfamily ribokinase KEYWORDS phosphotransferase SUMMARY #length 305 #molecular-weight 33081 #checksum 8768 SEQUENCE /// ENTRY S40827 #type complete TITLE probable sugar kinase (EC 2.7.1.-) - Escherichia coli (strain K-12) ALTERNATE_NAMES hypothetical 31.9K protein (glnA-fdhE intergenic region); hypothetical protein o300 ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS S40827; F65193 REFERENCE S40802 !$#authors Plunkett III, G.; Burland, V.; Daniels, D.L.; Blattner, F.R. !$#journal Nucleic Acids Res. (1993) 21:3391-3398 !$#title Analysis of the Escherichia coli genome. III. DNA sequence !1of the region from 87.2 to 89.2 minutes. !$#cross-references MUID:93347969; PMID:8346018 !$#accession S40827 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-300 ##label PLU !'##cross-references EMBL:L19201; NID:g304961; PIDN:AAB03016.1; !1PID:g304987 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1993 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65193 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-300 ##label BLAT !'##cross-references GB:AE000464; GB:U00096; NID:g2367324; !1PIDN:AAD13445.1; PID:g1790316; UWGP:b3883 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yihV CLASSIFICATION #superfamily ribokinase KEYWORDS phosphotransferase SUMMARY #length 300 #molecular-weight 31960 #checksum 6216 SEQUENCE /// ENTRY D64937 #type complete TITLE probable sugar kinase (EC 2.7.1.-) - Escherichia coli (strain K-12) ALTERNATE_NAMES hypothetical protein b1772 ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS D64937 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64937 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-322 ##label BLAT !'##cross-references GB:AE000272; GB:U00096; NID:g1788067; !1PIDN:AAC74842.1; PID:g1788071; UWGP:b1772 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily ribokinase KEYWORDS phosphotransferase SUMMARY #length 322 #molecular-weight 34951 #checksum 8671 SEQUENCE /// ENTRY D69690 #type complete TITLE ribokinase (EC 2.7.1.15) - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS D69690; I40463; S42711 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D69690 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-293 ##label KUN !'##cross-references GB:Z99122; GB:AL009126; NID:g2636029; !1PIDN:CAB15609.1; PID:g2636117 !'##experimental_source strain 168 REFERENCE I40462 !$#authors Woodson, K.; Devine, K.M. !$#journal Microbiology (1994) 140:1829-1838 !$#title Analysis of a ribose transport operon from Bacillus !1subtilis. !$#cross-references MUID:95005437; PMID:7921236 !$#accession I40463 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-283,'DKK' ##label RES !'##cross-references EMBL:Z25798; NID:g397493; PIDN:CAA81049.1; !1PID:g397495 COMMENT This enzyme catalyzes the phosphorylation of ribose to !1ribose 5-phosphate, the first step in ribose metabolism. GENETICS !$#gene rbsK CLASSIFICATION #superfamily ribokinase KEYWORDS phosphotransferase; ribose metabolism SUMMARY #length 293 #molecular-weight 31138 #checksum 6263 SEQUENCE /// ENTRY S39997 #type complete TITLE fructokinase (EC 2.7.1.4) - potato ORGANISM #formal_name Solanum tuberosum #common_name potato DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S39997 REFERENCE S39997 !$#authors Smith, S. !$#submission submitted to the EMBL Data Library, May 1992 !$#accession S39997 !'##molecule_type mRNA !'##residues 1-319 ##label SMI !'##cross-references EMBL:Z12823; NID:g297014; PIDN:CAA78283.1; !1PID:g297015 CLASSIFICATION #superfamily ribokinase KEYWORDS phosphotransferase SUMMARY #length 319 #molecular-weight 33764 #checksum 2064 SEQUENCE /// ENTRY KIECRU #type complete TITLE ribulokinase (EC 2.7.1.16) - Escherichia coli (strain K-12) ALTERNATE_NAMES L-ribulokinase ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS G64727; B29022; S40579; I41134 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64727 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-566 ##label BLAT !'##cross-references GB:AE000116; GB:U00096; NID:g1786240; !1PIDN:AAC73174.1; PID:g1786249; UWGP:b0063 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A91559 !$#authors Lee, N.; Gielow, W.; Martin, R.; Hamilton, E.; Fowler, A. !$#journal Gene (1986) 47:231-244 !$#title The organization of the araBAD operon of Escherichia coli. !$#cross-references MUID:87163495; PMID:3549454 !$#accession B29022 !'##molecule_type DNA !'##residues 1-22,'S',24-126,'RS',129-349,'S',351-364,'A',366-402,'S', !1404-524,'R',526-566 ##label LEE !'##cross-references GB:D10483; GB:J01597; GB:J01683; GB:J01706; !1GB:K01298; GB:K01990; GB:M10420; GB:M10611; GB:M12544; !1GB:V00259; GB:X04711; GB:X54847; GB:X54945; GB:X55034; !1GB:X56742; NID:g216434; PIDN:BAA01334.1; PID:g216483 REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40579 !'##molecule_type DNA !'##residues 1-22,'S',24-126,'RS',129-349,'S',351-364,'A',366-402,'S', !1404-524,'R',526-566 ##label YUR !'##cross-references EMBL:D10483; NID:g216434; PIDN:BAA01334.1; !1PID:g216483 REFERENCE I41134 !$#authors Lee, N.; Carbon, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1977) 74:49-53 !$#title Nucleotide sequence of the 5' end of araBAD operon messenger !1RNA in Escherichia coli B/r. !$#cross-references MUID:77102763; PMID:189315 !$#accession I41134 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-14 ##label RES !'##cross-references GB:K01304; NID:g145312; PIDN:AAA23465.1; !1PID:g145313 COMMENT This enzyme catalyzes the phosphorylation of L-ribulose to !1L-ribulose-5-phosphate. GENETICS !$#gene araB !$#map_position 1 min CLASSIFICATION #superfamily ribulokinase KEYWORDS arabinose metabolism; phosphotransferase SUMMARY #length 566 #molecular-weight 61089 #checksum 7534 SEQUENCE /// ENTRY A24984 #type complete TITLE ribulokinase (EC 2.7.1.16) - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A24984 REFERENCE A24984 !$#authors Lin, H.C.; Lei, S.P.; Wilcox, G. !$#journal Gene (1985) 34:111-122 !$#title The araBAD operon of Salmonella typhimurium LT2. I. !1Nucleotide sequence of araB and primary structure of its !1product, ribulokinase. !$#cross-references MUID:85232044; PMID:2989100 !$#accession A24984 !'##molecule_type DNA !'##residues 1-569 ##label LIN !'##cross-references GB:M11047; GB:M11045; GB:M11046; NID:g153866; !1PIDN:AAA27023.1; PID:g153867 !'##experimental_source strain LT2 GENETICS !$#gene araB FUNCTION !$#description catalyzes phosphorylation of L-ribulose to !1L-ribulose-5-phosphate CLASSIFICATION #superfamily ribulokinase KEYWORDS arabinose metabolism; phosphotransferase; protein kinase SUMMARY #length 569 #molecular-weight 61751 #checksum 1890 SEQUENCE /// ENTRY KIECXY #type complete TITLE xylulokinase (EC 2.7.1.17) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 01-Mar-2002 ACCESSIONS A30266; S47785; F65155 REFERENCE A90043 !$#authors Lawlis, V.B.; Dennis, M.S.; Chen, E.Y.; Smith, D.H.; Henner, !1D.J. !$#journal Appl. Environ. Microbiol. (1984) 47:15-21 !$#title Cloning and sequencing of the xylose isomerase and xylulose !1kinase genes of Escherichia coli. !$#cross-references MUID:84126725; PMID:6320721 !$#accession A30266 !'##molecule_type DNA !'##residues 1-484 ##label LAW !'##cross-references GB:K01996; NID:g148278; PIDN:AAA24769.1; !1PID:g148280 REFERENCE S47666 !$#authors Plunkett, G. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S47785 !'##molecule_type DNA !'##residues 1-484 ##label PLU !'##cross-references EMBL:U00039; NID:g466582; PIDN:AAB18541.1; !1PID:g466702 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65155 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-484 ##label BLAT !'##cross-references GB:AE000433; GB:U00096; NID:g1789977; !1PIDN:AAC76588.1; PID:g1789987; UWGP:b3564 !'##experimental_source strain K-12, substrain MG1655 COMMENT This enzyme catalyzes the phosphorylation of xylulose to !1xylulose-5-phosphate with ATP converting to ADP. GENETICS !$#gene xylB !$#map_position 80 min CLASSIFICATION #superfamily xylulokinase KEYWORDS phosphotransferase SUMMARY #length 484 #molecular-weight 52618 #checksum 5675 SEQUENCE /// ENTRY KIECFK #type complete TITLE fucokinase (EC 2.7.1.52) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 01-Mar-2002 ACCESSIONS JS0186; G65062 REFERENCE S04702 !$#authors Lu, Z.; Lin, E.C.C. !$#journal Nucleic Acids Res. (1989) 17:4883-4884 !$#title The nucleotide sequence of Escherichia coli genes for !1L-fucose dissimilation. !$#cross-references MUID:89315234; PMID:2664711 !$#accession JS0186 !'##molecule_type DNA !'##residues 1-482 ##label LUZ !'##cross-references GB:X15025; NID:g41501; PIDN:CAA33128.1; PID:g41506 !'##note it is uncertain whether Met-1 or Met-11 is the initiator REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65062 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-482 ##label BLAT !'##cross-references GB:AE000364; GB:U00096; NID:g2367162; !1PIDN:AAC75845.1; PID:g1789168; UWGP:b2803 !'##experimental_source strain K-12, substrain MG1655 COMMENT This protein is a kinase involved in an inducible catabolic !1pathway for L-fucose. GENETICS !$#gene fucK !$#map_position 60 min CLASSIFICATION #superfamily xylulokinase KEYWORDS L-fucose catabolism; L-fucose utilization; !1phosphotransferase SUMMARY #length 482 #molecular-weight 53235 #checksum 2252 SEQUENCE /// ENTRY KIECGL #type complete TITLE glycerol kinase (EC 2.7.1.30) [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 01-Mar-2002 ACCESSIONS A27339; S40869; B42157; S04595; A65199; S72651 REFERENCE A27339 !$#authors Pettigrew, D.W.; Ma, D.P.; Conrad, C.A.; Johnson, J.R. !$#journal J. Biol. Chem. (1988) 263:135-139 !$#title Escherichia coli glycerol kinase. Cloning and sequencing of !1the glpK gene and the primary structure of the enzyme. !$#cross-references MUID:88087079; PMID:2826434 !$#accession A27339 !'##molecule_type DNA !'##residues 1-502 ##label PET !'##cross-references GB:M18393; NID:g146219; PIDN:AAA23913.1; !1PID:g146220 REFERENCE S40802 !$#authors Plunkett III, G.; Burland, V.; Daniels, D.L.; Blattner, F.R. !$#journal Nucleic Acids Res. (1993) 21:3391-3398 !$#title Analysis of the Escherichia coli genome. III. DNA sequence !1of the region from 87.2 to 89.2 minutes. !$#cross-references MUID:93347969; PMID:8346018 !$#accession S40869 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-502 ##label PLU !'##cross-references EMBL:L19201; NID:g304961; PIDN:AAB03058.1; !1PID:g305029 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1993 REFERENCE A42157 !$#authors Weissenborn, D.L.; Wittekindt, N.; Larson, T.J. !$#journal J. Biol. Chem. (1992) 267:6122-6131 !$#title Structure and regulation of the glpFK operon encoding !1glycerol diffusion facilitator and glycerol kinase of !1Escherichia coli K-12. !$#cross-references MUID:92210584; PMID:1372899 !$#accession B42157 !'##molecule_type DNA !'##residues 1-144 ##label WEI !'##cross-references GB:M55990 REFERENCE S04594 !$#authors Muramatsu, S.; Mizuno, T. !$#journal Nucleic Acids Res. (1989) 17:4378 !$#title Nucleotide sequence of the region encompassing the glpKF !1operon and its upstream region containing a bent DNA !1sequence of Escherichia coli. !$#cross-references MUID:89296490; PMID:2544860 !$#accession S04595 !'##molecule_type DNA !'##residues 1-31 ##label MUR !'##cross-references EMBL:X15054; NID:g41577; PIDN:CAA33154.1; !1PID:g41579 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65199 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-502 ##label BLAT !'##cross-references GB:AE000467; GB:U00096; NID:g1790356; !1PIDN:AAC76908.1; PID:g1790361; UWGP:b3926 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S72651 !$#authors Gonzalez-Gil, G.; Bringmann, P.; Kahmann, R. !$#journal Mol. Microbiol. (1996) 22:21-29 !$#title FIS is a regulator of metabolism in Escherichia coli. !$#cross-references MUID:97055418; PMID:8899705 !$#accession S72651 !'##molecule_type protein !'##residues 2-14 ##label GON GENETICS !$#gene glpK !$#map_position 88 min FUNCTION !$#description EC 2.7.1.30 [validated, MUID:88087079]; catalyzes the !1ATP-dependent phosphorylation of glycerol to form glycerol !13-phosphate; this reaction is the rate-limiting step !$#pathway glycerol utilization !$#note requires magnesium CLASSIFICATION #superfamily xylulokinase KEYWORDS glycerol metabolism; phosphotransferase FEATURE !$2-502 #product glycerol kinase #status experimental #label !8MAT SUMMARY #length 502 #molecular-weight 56230 #checksum 8914 SEQUENCE /// ENTRY S18562 #type complete TITLE xylulokinase (EC 2.7.1.17) - Lactobacillus pentosus ORGANISM #formal_name Lactobacillus pentosus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S18562 REFERENCE S18560 !$#authors Lokman, B.C.; van Santen, P.; Verdoes, J.C.; Kruese, J.; !1Leer, R.J.; Posno, M.; Pouwels, P.H. !$#journal Mol. Gen. Genet. (1991) 230:161-169 !$#title Organization and characterization of three genes involved in !1D-xylose catabolism in Lactobacillus pentosus. !$#cross-references MUID:92079891; PMID:1660563 !$#accession S18562 !'##status preliminary !'##molecule_type DNA !'##residues 1-501 ##label LOK !'##cross-references EMBL:M57384; NID:g149604; PIDN:AAA25259.1; !1PID:g149607 GENETICS !$#gene xylB CLASSIFICATION #superfamily xylulokinase KEYWORDS phosphotransferase SUMMARY #length 501 #molecular-weight 54793 #checksum 1139 SEQUENCE /// ENTRY S47801 #type complete TITLE L-xylulokinase (EC 2.7.1.53) - Escherichia coli (strain K-12) ALTERNATE_NAMES cryptic l-xylulose kinase; hypothetical protein o498 ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS S47801; F65157 REFERENCE S47666 !$#authors Plunkett, G. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S47801 !'##status preliminary !'##molecule_type DNA !'##residues 1-498 ##label PLU !'##cross-references EMBL:U00039; NID:g466582; PIDN:AAB18557.1; !1PID:g466718 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65157 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-498 ##label BLAT !'##cross-references GB:AE000435; GB:U00096; NID:g2367244; !1PIDN:AAC76604.1; PID:g1790005; UWGP:b3580 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene lyxK CLASSIFICATION #superfamily xylulokinase KEYWORDS phosphotransferase SUMMARY #length 498 #molecular-weight 55154 #checksum 632 SEQUENCE /// ENTRY S75895 #type complete TITLE probable L-xylulokinase (EC 2.7.1.53) - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S75895 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75895 !'##status preliminary !'##molecule_type DNA !'##residues 1-495 ##label KAN !'##cross-references EMBL:D90913; GB:AB001339; NID:g1653348; !1PIDN:BAA18354.1; PID:g1653440 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily xylulokinase KEYWORDS phosphotransferase SUMMARY #length 495 #molecular-weight 54351 #checksum 4379 SEQUENCE /// ENTRY B26190 #type complete TITLE gluconokinase (EC 2.7.1.12) gntK - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS B26190; C69636 REFERENCE A92561 !$#authors Fujita, Y.; Fujita, T.; Miwa, Y.; Nihashi, J.; Aratani, Y. !$#journal J. Biol. Chem. (1986) 261:13744-13753 !$#title Organization and transcription of the gluconate operon, gnt, !1of Bacillus subtilis. !$#cross-references MUID:87008613; PMID:3020045 !$#accession B26190 !'##molecule_type DNA !'##residues 1-513 ##label FUJ !'##cross-references GB:AB005554; GB:D45242; GB:D31629; NID:g2280496; !1PIDN:BAA21578.1; PID:g563932 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69636 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-513 ##label KUN !'##cross-references GB:Z99124; GB:AL009126; NID:g2636442; !1PIDN:CAB16043.1; PID:g2636553 !'##experimental_source strain 168 GENETICS !$#gene gntK CLASSIFICATION #superfamily xylulokinase KEYWORDS phosphotransferase SUMMARY #length 513 #molecular-weight 57169 #checksum 7526 SEQUENCE /// ENTRY S36175 #type complete TITLE glycerol kinase (EC 2.7.1.30) - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS I37427; S36175; S46937; I37416; S37661 REFERENCE I37427 !$#authors Walker, A.P.; Muscatelli, F.; Monaco, A.P. !$#journal Hum. Mol. Genet. (1993) 2:107-114 !$#title Isolation of the human Xp21 glycerol kinase gene by !1positional cloning. !$#cross-references MUID:93271953; PMID:8499898 !$#accession I37427 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 130-524 ##label WAL !'##cross-references EMBL:X69886; NID:g288561; PIDN:CAA49512.1; !1PID:g871290 REFERENCE S36175 !$#authors Guo, W.; Worley, K.; Adams, V.; Mason, J.; !1Sylvester-Jackson, D.; Zhang, Y.H.; Towbin, J.A.; Fogt, !1D.D.; Madu, S.; Wheeler, D.A.; McCabe, E.R.B. !$#journal Nature Genet. (1993) 4:367-372 !$#title Genomic scanning for expressed sequences in Xp21 identifies !1the glycerol kinase gene. !$#cross-references MUID:94004964; PMID:8401584 !$#accession S36175 !'##status preliminary !'##molecule_type mRNA !'##residues 1-524 ##label GUO !'##cross-references GB:L13943; NID:g348166; PIDN:AAA52576.1; !1PID:g348167 REFERENCE S46937 !$#authors Sargent, C.A.; Young, C.; Ferguson-Smith, M.A.; Affara, N.A. !$#submission submitted to the EMBL Data Library, April 1992 !$#description The glycerol kinase gene family: structure of the Xp gene !1and related intronless retroposons. !$#accession S46937 !'##status preliminary !'##molecule_type mRNA !'##residues 1-30,'R',32-80,'G',82-98,'A',100-231,'H',233-449,'L', !1451-469,'D',471-520,'G',522,'D',524, !1'SVFCSLPLGFFIVSSMAMLIGARYISGIP' ##label SAR REFERENCE I37415 !$#authors Sargent, C.A.; Young, C.; Marsh, S.; Ferguson-Smith, M.A.; !1Affara, N.A. !$#journal Hum. Mol. Genet. (1994) 3:1317-1324 !$#title The glycerol kinase gene family: structure of the Xp gene, !1and related intronless retroposons. !$#cross-references MUID:95078834; PMID:7987308 !$#accession I37416 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-30,'R',32-80,'G',82-98,'A',100-231,'H',233-449,'L', !1451-469,'D',471-520,'G',522,'D',524, !1'SVFCSLPLGFFIVSSMAMLIGARYISGIP' ##label RE2 !'##cross-references EMBL:X78711; NID:g515028; PIDN:CAA55364.1; !1PID:g515029 REFERENCE S37661 !$#authors Sargent, C.A.; Affara, N.A.; Bentley, E.; Pelmear, A.; !1Bailey, D.M.D.; Davey, P.; Dow, D.; Leversha, M.; Aplin, H.; !1Besley, G.T.N.; Ferguson-Smith, M.A. !$#journal Hum. Mol. Genet. (1993) 2:97-106 !$#title Cloning of the X-linked glycerol kinase deficiency gene and !1its identification by sequence comparison to the Bacillus !1subtilis homologue. !$#cross-references MUID:93271973; PMID:8499912 !$#accession S37661 !'##status preliminary !'##molecule_type mRNA !'##residues 77-200,'MQVGLCFSTC',211-244,'ISHSVK',245-458, !1'RLWRQGLQKESAYGVSNPRICLPSRWSGLN','LRLMRRKVKFVILHGRKL' !1##label SA2 !'##cross-references EMBL:X68285; NID:g38413; PIDN:CAA48346.1; !1PID:g38414 GENETICS !$#gene GDB:GK !'##cross-references GDB:119271; OMIM:307030 !$#map_position Xp21.3-Xp21.2 CLASSIFICATION #superfamily xylulokinase KEYWORDS phosphotransferase SUMMARY #length 524 #molecular-weight 57489 #checksum 484 SEQUENCE /// ENTRY B64204 #type complete TITLE glycerol kinase (EC 2.7.1.30) - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 07-Dec-1999 ACCESSIONS B64204 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession B64204 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-508 ##label TIGR !'##cross-references GB:U39682; GB:L43967; NID:g1045702; PID:g1045709; !1TIGR:MG038 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily xylulokinase KEYWORDS phosphotransferase SUMMARY #length 508 #molecular-weight 56901 #checksum 8227 SEQUENCE /// ENTRY KIQXPR #type complete TITLE phosphoribulokinase (EC 2.7.1.19) - Xanthobacter flavus ORGANISM #formal_name Xanthobacter flavus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 11-Jun-1999 ACCESSIONS B45867; S13577 REFERENCE A45867 !$#authors Meijer, W.G.; Enequist, H.G.; Terpstra, P.; Dijkhuizen, L. !$#journal J. Gen. Microbiol. (1990) 136:2225-2230 !$#title Nucleotide sequences of the genes encoding !1fructosebisphosphatase and phosphoribulokinase from !1Xanthobacter flavus H4-14. !$#cross-references MUID:91178501; PMID:1964170 !$#accession B45867 !'##molecule_type DNA !'##residues 1-291 ##label ME2 !'##cross-references EMBL:X17252; NID:g48543; PIDN:CAA35119.1; !1PID:g48548 REFERENCE S13573 !$#authors Meijer, W.G.; Arnberg, A.C.; Enequist, H.G.; Terpstra, P.; !1Lidstrom, M.E.; Dijkhuizen, L. !$#journal Mol. Gen. Genet. (1991) 225:320-330 !$#title Identification and organization of carbon dioxide fixation !1genes in Xanthobacter flavus H4-14. !$#cross-references MUID:91172133; PMID:1900916 !$#accession S13577 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-291 ##label ME1 !'##cross-references EMBL:X17252; NID:g48543; PIDN:CAA35119.1; !1PID:g48548 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1989 GENETICS !$#gene cfxP CLASSIFICATION #superfamily phosphoribulokinase KEYWORDS ATP; Calvin cycle; phosphotransferase SUMMARY #length 291 #molecular-weight 33409 #checksum 1368 SEQUENCE /// ENTRY KIRFAS #type complete TITLE phosphoribulokinase (EC 2.7.1.19) A - Rhodobacter sphaeroides ALTERNATE_NAMES phosphopentokinase ORGANISM #formal_name Rhodobacter sphaeroides DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 11-Jun-1999 ACCESSIONS C40767; A26973 REFERENCE A40767 !$#authors Gibson, J.L.; Falcone, D.L.; Tabita, F.R. !$#journal J. Biol. Chem. (1991) 266:14646-14653 !$#title Nucleotide sequence, transcriptional analysis, and !1expression of genes encoded within the form I CO-2 fixation !1operon of Rhodobacter sphaeroides. !$#cross-references MUID:91317831; PMID:1907281 !$#accession C40767 !'##molecule_type DNA !'##residues 1-290 ##label GIB !'##cross-references GB:M64624; NID:g151920; PIDN:AAA26113.1; !1PID:g151922 REFERENCE A26973 !$#authors Hallenbeck, P.L.; Kaplan, S. !$#journal J. Bacteriol. (1987) 169:3669-3678 !$#title Cloning of the gene for phosphoribulokinase activity from !1Rhodobacter sphaeroides and its expression in Escherichia !1coli. !$#cross-references MUID:87279918; PMID:3038847 !$#accession A26973 !'##molecule_type DNA !'##residues 1-28 ##label HAL !'##cross-references GB:M28006; NID:g151986; PIDN:AAA26153.1; !1PID:g151987 COMMENT This protein is encoded within the form I !1ribulose-bisphosphate carboxylase operon, which predominates !1when carbon dioxide is limiting. GENETICS !$#gene prkA CLASSIFICATION #superfamily phosphoribulokinase KEYWORDS ATP; Calvin cycle; phosphotransferase SUMMARY #length 290 #molecular-weight 32664 #checksum 9656 SEQUENCE /// ENTRY B35819 #type complete TITLE phosphoribulokinase (EC 2.7.1.19) B [similarity] - Rhodobacter sphaeroides ORGANISM #formal_name Rhodobacter sphaeroides DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 05-May-2000 ACCESSIONS B35819; A41080 REFERENCE A35819 !$#authors Gibson, J.L.; Chen, J.H.; Tower, P.A.; Tabita, F.R. !$#journal Biochemistry (1990) 29:8085-8093 !$#title The form II fructose 1,6-bisphosphatase and !1phosphoribulokinase genes form part of a large operon in !1Rhodobacter sphaeroides: primary structure and insertional !1mutagenesis analysis. !$#cross-references MUID:91084479; PMID:2175647 !$#accession B35819 !'##molecule_type DNA !'##residues 1-292 ##label GIB !'##cross-references GB:J02922; NID:g151908; PIDN:AAA26106.1; !1PID:g294656 !'##note the authors translated the codon ACG for residue 24 as Phe, TTC !1for residue 25 as Glu, and CAC for residue 193 as Gly REFERENCE A41080 !$#authors Chen, J.H.; Gibson, J.L.; McCue, L.A.; Tabita, F.R. !$#journal J. Biol. Chem. (1991) 266:20447-20452 !$#title Identification, expression, and deduced primary structure of !1transketolase and other enzymes encoded within the form II !1CO-2 fixation operon of Rhodobacter sphaeroides. !$#cross-references MUID:92041881; PMID:1939098 !$#accession A41080 !'##molecule_type DNA !'##residues 259-292 ##label CHE !'##cross-references GB:M68914; NID:g151988; PIDN:AAA26154.1; !1PID:g387872 CLASSIFICATION #superfamily phosphoribulokinase KEYWORDS ATP; phosphotransferase SUMMARY #length 292 #molecular-weight 33176 #checksum 1607 SEQUENCE /// ENTRY JQ0399 #type complete TITLE phosphoribulokinase (EC 2.7.1.19) [similarity] - Alcaligenes eutrophus ORGANISM #formal_name Alcaligenes eutrophus DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 05-May-2000 ACCESSIONS JQ0399 REFERENCE JQ0399 !$#authors Kossmann, J.; Klintworth, R.; Bowien, B. !$#journal Gene (1989) 85:247-252 !$#title Sequence analysis of the chromosomal and plasmid genes !1encoding phosphoribulokinase from Alcaligenes eutrophus. !$#cross-references MUID:90152372; PMID:2559876 !$#accession JQ0399 !'##molecule_type DNA !'##residues 1-292 ##label KOS !'##cross-references GB:M33563; NID:g141908; PIDN:AAA21959.1; !1PID:g141910 !'##experimental_source strain H16 COMMENT This enzyme catalyzes the formation of ribulose-1, !15-bisphosphate. GENETICS !$#gene cfxP CLASSIFICATION #superfamily phosphoribulokinase KEYWORDS ATP; phosphotransferase SUMMARY #length 292 #molecular-weight 33316 #checksum 4343 SEQUENCE /// ENTRY JQ0400 #type complete TITLE phosphoribulokinase (EC 2.7.1.19) [similarity] - Alcaligenes eutrophus plasmid pHG1 ORGANISM #formal_name Alcaligenes eutrophus DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 05-May-2000 ACCESSIONS JQ0400 REFERENCE JQ0399 !$#authors Kossmann, J.; Klintworth, R.; Bowien, B. !$#journal Gene (1989) 85:247-252 !$#title Sequence analysis of the chromosomal and plasmid genes !1encoding phosphoribulokinase from Alcaligenes eutrophus. !$#cross-references MUID:90152372; PMID:2559876 !$#accession JQ0400 !'##molecule_type DNA !'##residues 1-292 ##label KOS !'##cross-references GB:M33562; NID:g141905; PIDN:AAA21957.1; !1PID:g141907 !'##experimental_source strain H16 COMMENT This enzyme catalyzes the formation of ribulose-1, !15-bisphosphate. GENETICS !$#gene cfxP !$#genome plasmid CLASSIFICATION #superfamily phosphoribulokinase KEYWORDS ATP; phosphotransferase SUMMARY #length 292 #molecular-weight 33161 #checksum 5050 SEQUENCE /// ENTRY KIHUT #type complete TITLE thymidine kinase (EC 2.7.1.21), cytosolic - human ORGANISM #formal_name Homo sapiens #common_name man DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 19-Jan-2001 ACCESSIONS A27318; A00606; I57602 REFERENCE A27318 !$#authors Flemington, E.; Bradshaw Jr., H.D.; Traina-Dorge, V.; !1Slagel, V.; Deininger, P.L. !$#journal Gene (1987) 52:267-277 !$#title Sequence, structure and promoter characterization of the !1human thymidine kinase gene. !$#cross-references MUID:87277399; PMID:3301530 !$#accession A27318 !'##molecule_type DNA !'##residues 1-234 ##label FLE !'##cross-references GB:M15205; GB:M15206; NID:g339718; PIDN:AAA61191.1; !1PID:g339719 !'##note the authors translated the codon TGC for residue 109 as Lys REFERENCE A00606 !$#authors Bradshaw Jr., H.D.; Deininger, P.L. !$#journal Mol. Cell. Biol. (1984) 4:2316-2320 !$#title Human thymidine kinase gene: molecular cloning and !1nucleotide sequence of a cDNA expressible in mammalian !1cells. !$#cross-references MUID:85085935; PMID:6549046 !$#accession A00606 !'##molecule_type mRNA !'##residues 1-234 ##label BRA !'##cross-references GB:K02581; NID:g339708; PIDN:AAA61187.1; !1PID:g339709 REFERENCE I57602 !$#authors Kreidberg, J.A.; Kelly, T.J. !$#journal Mol. Cell. Biol. (1986) 6:2903-2909 !$#title Genetic analysis of the human thymidine kinase gene !1promoter. !$#cross-references MUID:87064597; PMID:3785218 !$#accession I57602 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-22 ##label RES !'##cross-references GB:M13643; NID:g339712; PIDN:AAA61189.1; !1PID:g339713 COMMENT Two forms of thymidine kinase, which catalyzes the !1phosphorylation of thymidine to thymidine 5'-monophosphate, !1have been identified in animal cells, one in mitochondria !1and the other in cytosol. Activity of this cytosolic enzyme !1is high in proliferating cells and it peaks during the S !1phase of the cell cycle; it is very low in resting cells. GENETICS !$#gene GDB:TK1 !'##cross-references GDB:120439; OMIM:188300 !$#map_position 17q23.2-17q25.3 !$#introns 22/3; 33/2; 70/2; 101/3; 131/3; 171/3 CLASSIFICATION #superfamily thymidine kinase KEYWORDS ATP; DNA biosynthesis; nucleotide binding; P-loop; !1phosphotransferase FEATURE !$26-33 #region nucleotide-binding motif A (P-loop)\ !$93-98 #region nucleotide-binding motif B SUMMARY #length 234 #molecular-weight 25501 #checksum 8110 SEQUENCE /// ENTRY KIMST #type complete TITLE thymidine kinase (EC 2.7.1.21), cytosolic - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 04-Dec-1986 #sequence_revision 30-Sep-1993 #text_change 19-Jan-2001 ACCESSIONS JC1252; A00607; S22599; I58005 REFERENCE JC1252 !$#authors Gudas, J.M.; Fridovich-Keil, J.L.; Datta, M.W.; Bryan, J.; !1Pardee, A.B. !$#journal Gene (1992) 118:205-216 !$#title Characterization of the murine thymidine kinase-encoding !1gene and analysis of transcription start point !1heterogeneity. !$#cross-references MUID:92380505; PMID:1511894 !$#accession JC1252 !'##molecule_type DNA !'##residues 1-233 ##label GUD !'##cross-references GB:M68489; NID:g202078; PIDN:AAA40454.1; !1PID:g202079 REFERENCE A00607 !$#authors Lin, P.F.; Lieberman, H.B.; Yeh, D.B.; Xu, T.; Zhao, S.Y.; !1Ruddle, F.H. !$#journal Mol. Cell. Biol. (1985) 5:3149-3156 !$#title Molecular cloning and structural analysis of murine !1thymidine kinase genomic and cDNA sequences. !$#cross-references MUID:86310784; PMID:3018504 !$#accession A00607 !'##molecule_type mRNA !'##residues 1-87,'L',89-233 ##label LIN !'##cross-references GB:M11945; NID:g202072; PIDN:AAA40451.1; !1PID:g202073 REFERENCE S22599 !$#authors Rotheneder, H.; Grabner, M.; Wintersberger, E. !$#journal Nucleic Acids Res. (1991) 19:6805-6809 !$#title Presence of regulatory sequences within intron 2 of the !1mouse thymidine kinase gene. !$#cross-references MUID:92107666; PMID:1762910 !$#accession S22599 !'##status translation not shown !'##molecule_type DNA !'##residues 1-32 ##label ROT !'##cross-references EMBL:X60980; NID:g54809; PIDN:CAA43296.1; !1PID:g54810 REFERENCE I58005 !$#authors Liechty, M.C.; Rauchfuss, H.S.; Lugo, M.H.; Hozier, J.C. !$#journal Mutat. Res. (1993) 286:299-307 !$#title Sequence analysis of tka(-)-1 and tkb(+)-1 alleles in L5178Y !1tk+/- mouse-lymphoma cells and spontaneous tk-/- mutants. !$#cross-references MUID:93211435; PMID:7681542 !$#accession I58005 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-87,'S',89-233 ##label RES !'##cross-references GB:S57244; NID:g298945; PIDN:AAB26001.1; !1PID:g298946 COMMENT Two forms of thymidine kinase, which catalyzes the !1phosphorylation of thymidine to thymidine 5'-monophosphate, !1have been identified in animal cells, one in mitochondria !1and the other in cytosol. Activity of this cytosolic enzyme !1is high in proliferating cells and it peaks during the S !1phase of the cell cycle; it is very low in resting cells. GENETICS !$#gene TK1 !$#introns 22/3; 33/2; 70/2; 101/3; 131/3; 171/3 CLASSIFICATION #superfamily thymidine kinase KEYWORDS ATP; DNA biosynthesis; nucleotide binding; P-loop; !1phosphotransferase FEATURE !$26-33 #region nucleotide-binding motif A (P-loop)\ !$93-98 #region nucleotide-binding motif B SUMMARY #length 233 #molecular-weight 25760 #checksum 2532 SEQUENCE /// ENTRY A25243 #type complete TITLE thymidine kinase (EC 2.7.1.21) - Chinese hamster ORGANISM #formal_name Cricetulus griseus #common_name Chinese hamster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS A25243 REFERENCE A25243 !$#authors Lewis, J.A. !$#journal Mol. Cell. Biol. (1986) 6:1998-2010 !$#title Structure and expression of the chinese hamster thymidine !1kinase gene. !$#cross-references MUID:87064490; PMID:3453109 !$#accession A25243 !'##molecule_type mRNA !'##residues 1-234 ##label LEW !'##cross-references GB:L00369; GB:M13622; NID:g336728; PIDN:AAA37022.1; !1PID:g457429 CLASSIFICATION #superfamily thymidine kinase KEYWORDS ATP; DNA biosynthesis; nucleotide binding; P-loop; !1phosphotransferase FEATURE !$26-33 #region nucleotide-binding motif A (P-loop) SUMMARY #length 234 #molecular-weight 25621 #checksum 988 SEQUENCE /// ENTRY KICHT #type complete TITLE thymidine kinase (EC 2.7.1.21), cytosolic - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 19-Jan-2001 ACCESSIONS A00608; I50430 REFERENCE A00608 !$#authors Kwoh, T.J.; Engler, J.A. !$#journal Nucleic Acids Res. (1984) 12:3959-3971 !$#title The nucleotide sequence of the chicken thymidine kinase gene !1and the relationship of its predicted polypeptide to that of !1the vaccinia virus thymidine kinase. !$#cross-references MUID:84221409; PMID:6328447 !$#accession A00608 !'##molecule_type DNA !'##residues 1-224 ##label KWO REFERENCE I50430 !$#authors Merrill, G.F.; Harland, R.M.; Groudine, M.; McKnight, S.L. !$#journal Mol. Cell. Biol. (1984) 4:1769-1776 !$#title Genetic and physical analysis of the chicken tk gene. !$#cross-references MUID:85036328; PMID:6092937 !$#accession I50430 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-224 ##label MER !'##cross-references GB:K02611; NID:g212775; PIDN:AAA49096.1; !1PID:g212776 GENETICS !$#gene TK1 !$#introns 22/3; 33/2; 71/2; 102/3; 132/3; 172/3 CLASSIFICATION #superfamily thymidine kinase KEYWORDS ATP; DNA biosynthesis; nucleotide binding; P-loop; !1phosphotransferase FEATURE !$26-33 #region nucleotide-binding motif A (P-loop)\ !$94-99 #region nucleotide-binding motif B SUMMARY #length 224 #molecular-weight 24872 #checksum 5002 SEQUENCE /// ENTRY KIVZ #type complete TITLE thymidine kinase (EC 2.7.1.21) - vaccinia virus (strains WR and Copenhagen) ALTERNATE_NAMES J2R protein ORGANISM #formal_name vaccinia virus #note host Homo sapiens (man) DATE 20-Sep-1984 #sequence_revision 20-Sep-1984 #text_change 19-Jan-2001 ACCESSIONS A00609; A21143; G23092; E42513 REFERENCE A00609 !$#authors Weir, J.P.; Moss, B. !$#journal J. Virol. (1983) 46:530-537 !$#title Nucleotide sequence of the vaccinia virus thymidine kinase !1gene and the nature of spontaneous frameshift mutations. !$#cross-references MUID:83189354; PMID:6842679 !$#accession A00609 !'##molecule_type DNA !'##residues 1-177 ##label WEI !'##cross-references EMBL:X01978; NID:g61387; PIDN:CAA26016.1; !1PID:g61395 !'##experimental_source strain WR REFERENCE A21143 !$#authors Hruby, D.E.; Maki, R.A.; Miller, D.B.; Ball, L.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:3411-3415 !$#title Fine structure analysis and nucleotide sequence of the !1vaccinia virus thymidine kinase gene. !$#cross-references MUID:83221605; PMID:6304709 !$#accession A21143 !'##molecule_type DNA !'##residues 1-177 ##label HRU !'##cross-references GB:X01978; EMBL:J02424; NID:g61387; !1PIDN:CAA26016.1; PID:g61395 !'##experimental_source strain WR !'##note the authors translated the codon ATT for residue 6 as Ala REFERENCE A23092 !$#authors Plucienniczak, A.; Schroeder, E.; Zettlmeissl, G.; Streeck, !1R.E. !$#journal Nucleic Acids Res. (1985) 13:985-998 !$#title Nucleotide sequence of a cluster of early and late genes in !1a conserved segment of the vaccinia virus genome. !$#cross-references MUID:85215527; PMID:2987815 !$#accession G23092 !'##molecule_type DNA !'##residues 1-177 ##label PLU !'##cross-references GB:X01978; EMBL:V01537; NID:g61387; !1PIDN:CAA26016.1; PID:g61395 !'##experimental_source strain WR REFERENCE A42501 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:517-563 !$#title Appendix to "The complete DNA sequence of vaccinia virus". !$#accession E42513 !'##molecule_type DNA !'##residues 1-177 ##label GOE !'##cross-references GB:M35027; NID:g335317; PIDN:AAA48082.1; !1PID:g335430 !'##experimental_source strain Copenhagen REFERENCE A42531 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:247-266 !$#title The complete DNA sequence of vaccinia virus. !$#cross-references MUID:91021027; PMID:2219722 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given CLASSIFICATION #superfamily thymidine kinase KEYWORDS ATP; DNA biosynthesis; early protein; nucleotide binding; !1P-loop; phosphotransferase FEATURE !$11-18 #region nucleotide-binding motif A (P-loop)\ !$78-83 #region nucleotide-binding motif B SUMMARY #length 177 #molecular-weight 20100 #checksum 7996 SEQUENCE /// ENTRY KIVZMV #type complete TITLE thymidine kinase (EC 2.7.1.21) - monkeypox virus ORGANISM #formal_name monkeypox virus #note host (monkey) DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 19-Jan-2001 ACCESSIONS A00610 REFERENCE A94333 !$#authors Esposito, J.J.; Knight, J.C. !$#journal Virology (1984) 135:561-567 !$#title Nucleotide sequence of the thymidine kinase gene region of !1monkeypox and variola viruses. !$#cross-references MUID:84251718; PMID:6330986 !$#accession A00610 !'##molecule_type DNA !'##residues 1-177 ##label ESP !'##cross-references GB:K02025; NID:g332175; PIDN:AAA80529.1; !1PID:g332176 GENETICS !$#gene tk CLASSIFICATION #superfamily thymidine kinase KEYWORDS ATP; DNA biosynthesis; nucleotide binding; P-loop; !1phosphotransferase FEATURE !$11-18 #region nucleotide-binding motif A (P-loop)\ !$78-83 #region nucleotide-binding motif B SUMMARY #length 177 #molecular-weight 20040 #checksum 8872 SEQUENCE /// ENTRY KIVZVV #type complete TITLE thymidine kinase (EC 2.7.1.21) - variola virus ALTERNATE_NAMES L2R protein ORGANISM #formal_name variola virus #note host Homo sapiens (man) DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 23-Mar-2001 ACCESSIONS A00611; D36845; S33093 REFERENCE A94333 !$#authors Esposito, J.J.; Knight, J.C. !$#journal Virology (1984) 135:561-567 !$#title Nucleotide sequence of the thymidine kinase gene region of !1monkeypox and variola viruses. !$#cross-references MUID:84251718; PMID:6330986 !$#accession A00611 !'##molecule_type DNA !'##residues 1-177 ##label ESP !'##cross-references GB:K02031; NID:g335842; PIDN:AAA80461.1; !1PID:g335843 REFERENCE A36859 !$#authors Blinov, V.M. !$#submission submitted to GenBank, November 1992 !$#accession D36845 !'##status preliminary !'##molecule_type DNA !'##residues 1-89,'I',91-162,'I',164-177 ##label BLI !'##cross-references GB:X69198; NID:g456758; PIDN:CAA49020.1; !1PID:g297259 !'##experimental_source strain India-1967, ssp. major, isolate Ind3 REFERENCE S33069 !$#authors Shchelkunov, S.N.; Blinov, V.M.; Totmenin, A.V.; !1Marennikova, S.S.; Kolykhalov, A.A.; Frolov, I.V.; !1Chizhikov, V.E.; Gytorov, V.V.; Gashikov, P.V.; Belanov, !1E.F.; Belavin, P.A.; Resenchuk, S.M.; Andzhaparidze, O.G.; !1Sandakhchiev, L.S. !$#journal Virus Res. (1993) 27:25-35 !$#title Nucleotide sequence analysis of variola virus HindIII M, L, !1I genome fragments. !$#cross-references MUID:93190624; PMID:8383392 !$#accession S33093 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-89,'I',91-162,'I',164-177 ##label SHC !'##cross-references EMBL:X67119; NID:g62330; PIDN:CAA47578.1; !1PID:g62355 !'##experimental_source strain India-1967, isolate Ind3 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1992 GENETICS !$#gene tk CLASSIFICATION #superfamily thymidine kinase KEYWORDS ATP; DNA biosynthesis; nucleotide binding; P-loop; !1phosphotransferase FEATURE !$11-18 #region nucleotide-binding motif A (P-loop)\ !$78-83 #region nucleotide-binding motif B SUMMARY #length 177 #molecular-weight 20042 #checksum 8902 SEQUENCE /// ENTRY KIVZSF #type complete TITLE thymidine kinase (EC 2.7.1.21) - rabbit fibroma virus ORGANISM #formal_name rabbit fibroma virus, Shope fibroma virus DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 19-Jan-2001 ACCESSIONS A26102 REFERENCE A26102 !$#authors Upton, C.; McFadden, G. !$#journal J. Virol. (1986) 60:920-927 !$#title Identification and nucleotide sequence of the thymidine !1kinase gene of Shope fibroma virus. !$#cross-references MUID:87061216; PMID:3023681 !$#accession A26102 !'##molecule_type DNA !'##residues 1-176 ##label UPT !'##cross-references GB:M14493; NID:g333615; PIDN:AAA47227.1; !1PID:g333616 !'##experimental_source strain Kasza GENETICS !$#gene tk CLASSIFICATION #superfamily thymidine kinase KEYWORDS ATP; DNA biosynthesis; nucleotide binding; P-loop; !1phosphotransferase FEATURE !$11-18 #region nucleotide-binding motif A (P-loop)\ !$78-83 #region nucleotide-binding motif B SUMMARY #length 176 #molecular-weight 19749 #checksum 6961 SEQUENCE /// ENTRY KIVZM1 #type complete TITLE thymidine kinase (EC 2.7.1.21) - myxoma virus ALTERNATE_NAMES MF8 protein ORGANISM #formal_name myxoma virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 19-Jan-2001 ACCESSIONS JQ1421 REFERENCE JQ1421 !$#authors Jackson, R.J.; Bults, H.G. !$#journal J. Gen. Virol. (1992) 73:323-328 !$#title The myxoma virus thymidine kinase gene: sequence and !1transcriptional mapping. !$#cross-references MUID:92166739; PMID:1538190 !$#accession JQ1421 !'##molecule_type DNA !'##residues 1-178 ##label JAC !'##cross-references GB:X52655; NID:g987956; PIDN:CAA36880.1; PID:g60616 CLASSIFICATION #superfamily thymidine kinase KEYWORDS ATP; nucleotide binding; P-loop; phosphotransferase FEATURE !$13-20 #region nucleotide-binding motif A (P-loop)\ !$80-85 #region nucleotide-binding motif B SUMMARY #length 178 #molecular-weight 19931 #checksum 8424 SEQUENCE /// ENTRY KIVZCP #type complete TITLE thymidine kinase (EC 2.7.1.21) - sheep pox virus (isolate Kenya sheep-1, KS-1) ORGANISM #formal_name sheep pox virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 19-Jan-2001 ACCESSIONS B31813 REFERENCE A31813 !$#authors Gershon, P.D.; Black, D.N. !$#journal J. Gen. Virol. (1989) 70:525-533 !$#title The nucleotide sequence around the capripoxvirus thymidine !1kinase gene reveals a gene shared specifically with !1leporipoxvirus. !$#cross-references MUID:89279233; PMID:2732700 !$#accession B31813 !'##molecule_type DNA !'##residues 1-177 ##label GER !'##cross-references GB:D00423; NID:g221120; PIDN:BAA00324.1; !1PID:g221123 GENETICS !$#gene tk CLASSIFICATION #superfamily thymidine kinase KEYWORDS ATP; DNA biosynthesis; early protein; nucleotide binding; !1P-loop; phosphotransferase FEATURE !$11-18 #region nucleotide-binding motif A (P-loop)\ !$78-83 #region nucleotide-binding motif B SUMMARY #length 177 #molecular-weight 20447 #checksum 7339 SEQUENCE /// ENTRY KIVZSW #type complete TITLE thymidine kinase (EC 2.7.1.21) - swinepox virus ORGANISM #formal_name swinepox virus DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 19-Jan-2001 ACCESSIONS B37949 REFERENCE A37949 !$#authors Schnitzlein, W.M.; Tripathy, D.N. !$#journal Virology (1991) 181:727-732 !$#title Identification and nucleotide sequence of the thymidine !1kinase gene of swinepox virus. !$#cross-references MUID:91196265; PMID:1840707 !$#accession B37949 !'##molecule_type DNA !'##residues 1-177 ##label SCH !'##cross-references EMBL:M59931; NID:g335128; PIDN:AAA47891.1; !1PID:g335130 CLASSIFICATION #superfamily thymidine kinase KEYWORDS ATP; DNA biosynthesis; early protein; nucleotide binding; !1P-loop; phosphotransferase FEATURE !$11-18 #region nucleotide-binding motif A (P-loop)\ !$79-84 #region nucleotide-binding motif B SUMMARY #length 177 #molecular-weight 20053 #checksum 6542 SEQUENCE /// ENTRY KIVZSK #type complete TITLE thymidine kinase (EC 2.7.1.21) - swinepox virus (strain Kasza) ORGANISM #formal_name swinepox virus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 19-Jan-2001 ACCESSIONS A40475 REFERENCE A40475 !$#authors Feller, J.A.; Massung, R.F.; Turner, P.C.; Gibbs, E.P.J.; !1Bockamp, E.O.; Beloso, A.; Talavera, A.; Vinuela, E.; Moyer, !1R.W. !$#journal Virology (1991) 183:578-585 !$#title Isolation and molecular characterization of the swinepox !1virus thymidine kinase gene. !$#cross-references MUID:91306440; PMID:1853562 !$#accession A40475 !'##molecule_type DNA !'##residues 1-181 ##label FEL !'##cross-references GB:M64000; NID:g335133; PIDN:AAA47894.1; !1PID:g335134 CLASSIFICATION #superfamily thymidine kinase KEYWORDS ATP; DNA replication; early protein; nucleotide binding; !1P-loop; phosphotransferase FEATURE !$15-22 #region nucleotide-binding motif A (P-loop)\ !$83-88 #region nucleotide-binding motif B SUMMARY #length 181 #molecular-weight 20574 #checksum 9306 SEQUENCE /// ENTRY KIVZAM #type complete TITLE thymidine kinase (EC 2.7.1.21) - Amsacta moorei poxvirus ORGANISM #formal_name Amsacta moorei poxvirus #note host Amsacta moorei (Indian red army worm) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 19-Jan-2001 ACCESSIONS B40818; JQ1924 REFERENCE A40818 !$#authors Gruidl, M.E.; Hall, R.L.; Moyer, R.W. !$#journal Virology (1992) 186:507-516 !$#title Mapping and molecular characterization of a functional !1thymidine kinase from Amsacta moorei entomopoxvirus. !$#cross-references MUID:92124724; PMID:1733099 !$#accession B40818 !'##molecule_type DNA !'##residues 1-182 ##label GRU !'##cross-references GB:M80924; NID:g209638; PIDN:AAA42386.1; !1PID:g455125 REFERENCE JQ1922 !$#authors Lytvyn, V.; Fortin, Y.; Banville, M.; Arif, B.; Richardson, !1C. !$#journal J. Gen. Virol. (1992) 73:3235-3240 !$#title Comparison of the thymidine kinase genes from three !1entomopoxviruses. !$#cross-references MUID:93107860; PMID:1469363 !$#accession JQ1924 !'##molecule_type DNA !'##residues 1-182 ##label LYT !'##cross-references GB:D10679; NID:g221015; PIDN:BAA01525.1; !1PID:g221016 GENETICS !$#gene TK CLASSIFICATION #superfamily thymidine kinase KEYWORDS ATP; nucleotide binding; P-loop; phosphotransferase FEATURE !$8-15 #region nucleotide-binding motif A (P-loop) SUMMARY #length 182 #molecular-weight 21240 #checksum 7713 SEQUENCE /// ENTRY JQ1922 #type complete TITLE thymidine kinase (EC 2.7.1.21) - Choristoneura biennis poxvirus ORGANISM #formal_name Choristoneura biennis poxvirus #note host Choristoneura biennis (two-year cycle spruce budworm) DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 19-Jan-2001 ACCESSIONS JQ1922 REFERENCE JQ1922 !$#authors Lytvyn, V.; Fortin, Y.; Banville, M.; Arif, B.; Richardson, !1C. !$#journal J. Gen. Virol. (1992) 73:3235-3240 !$#title Comparison of the thymidine kinase genes from three !1entomopoxviruses. !$#cross-references MUID:93107860; PMID:1469363 !$#accession JQ1922 !'##molecule_type DNA !'##residues 1-186 ##label LYT !'##cross-references GB:D10680; NID:g221126; PIDN:BAA01526.1; !1PID:g221127 GENETICS !$#gene TK CLASSIFICATION #superfamily thymidine kinase KEYWORDS ATP; nucleotide binding; P-loop; phosphotransferase FEATURE !$8-15 #region nucleotide-binding motif A (P-loop) SUMMARY #length 186 #molecular-weight 21426 #checksum 8237 SEQUENCE /// ENTRY JQ1923 #type complete TITLE thymidine kinase (EC 2.7.1.21) - Choristoneura fumiferana poxvirus ORGANISM #formal_name Choristoneura fumiferana poxvirus #note host Choristoneura fumiferana (eastern spruce budworm) DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 19-Jan-2001 ACCESSIONS JQ1923 REFERENCE JQ1922 !$#authors Lytvyn, V.; Fortin, Y.; Banville, M.; Arif, B.; Richardson, !1C. !$#journal J. Gen. Virol. (1992) 73:3235-3240 !$#title Comparison of the thymidine kinase genes from three !1entomopoxviruses. !$#cross-references MUID:93107860; PMID:1469363 !$#accession JQ1923 !'##molecule_type DNA !'##residues 1-185 ##label LYT !'##cross-references GB:D10681; NID:g221129; PIDN:BAA01527.1; !1PID:g221130 GENETICS !$#gene TK CLASSIFICATION #superfamily thymidine kinase KEYWORDS ATP; nucleotide binding; P-loop; phosphotransferase FEATURE !$8-15 #region nucleotide-binding motif A (P-loop) SUMMARY #length 185 #molecular-weight 21298 #checksum 7404 SEQUENCE /// ENTRY KIVZFP #type complete TITLE thymidine kinase (EC 2.7.1.21) - fowlpox virus ORGANISM #formal_name fowlpox virus DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 19-Jan-2001 ACCESSIONS A27532; JS0229; C48563; S10909 REFERENCE A27532 !$#authors Boyle, D.B.; Coupar, B.E.H.; Gibbs, A.J.; Seigman, L.J.; !1Both, G.W. !$#journal Virology (1987) 156:355-365 !$#title Fowlpox virus thymidine kinase: nucleotide sequence and !1relationships to other thymidine kinases. !$#cross-references MUID:87122176; PMID:3027984 !$#accession A27532 !'##molecule_type DNA !'##residues 1-183 ##label BOY !'##cross-references GB:M16617; NID:g325380; PIDN:AAA43822.1; !1PID:g325381 REFERENCE JS0220 !$#authors Binns, M.M.; Tomley, F.M.; Campbell, J.; Boursnell, M.E.G. !$#journal J. Gen. Virol. (1988) 69:1275-1283 !$#title Comparison of a conserved region in fowlpox virus and !1vaccinia virus genomes and the translocation of the fowlpox !1virus thymidine kinase gene. !$#cross-references MUID:88258470; PMID:2838574 !$#accession JS0229 !'##molecule_type DNA !'##residues 1-183 ##label BI1 !'##cross-references GB:D00321; NID:g221411; PIDN:BAA00233.1; !1PID:g221413 !'##experimental_source strain HP444 REFERENCE A48563 !$#authors Binns, M.M.; Boursnell, M.E.; Skinner, M.A. !$#journal Virus Res. (1992) 24:161-172 !$#title Gene translocations in poxviruses: the fowlpox virus !1thymidine kinase gene is flanked by 15 bp direct repeats and !1occupies the locus which in vaccinia virus is occupied by !1the ribonucleotide reductase large subunit gene. !$#cross-references MUID:92410746; PMID:1326827 !$#accession C48563 !'##molecule_type DNA !'##residues 1-183 ##label BI2 !'##cross-references GB:X12700; NID:g59344 !'##experimental_source strain HP444 !'##note sequence extracted from NCBI backbone (NCBIN:113549, !1NCBIP:113552) !'##note this ORF is not annotated in GenBank entry FVTKGENE, release !1106 REFERENCE S10909 !$#authors Beisel, C.E.; Nazerian, K. !$#submission submitted to the EMBL Data Library, April 1990 !$#description Nucleotide sequence of the thymidine kinase gene of a !1vaccine strain of a fowlpox virus. !$#accession S10909 !'##molecule_type DNA !'##residues 1-183 ##label EMB !'##cross-references EMBL:X52860; NID:g61233; PIDN:CAA37041.1; !1PID:g61234 CLASSIFICATION #superfamily thymidine kinase KEYWORDS ATP; DNA biosynthesis; early protein; nucleotide binding; !1P-loop; phosphotransferase FEATURE !$11-18 #region nucleotide-binding motif A (P-loop) SUMMARY #length 183 #molecular-weight 20380 #checksum 868 SEQUENCE /// ENTRY KIXFAS #type complete TITLE thymidine kinase (EC 2.7.1.21) - African swine fever virus ORGANISM #formal_name African swine fever virus, ASFV DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 19-Jan-2001 ACCESSIONS A37079; A37922 REFERENCE A37079 !$#authors Blasco, R.; Lopez-Otin, C.; Munoz, M.; Bockamp, E.O.; !1Simon-Mateo, C.; Vinuela, E. !$#journal Virology (1990) 178:301-304 !$#title Sequence and evolutionary relationships of African swine !1fever virus thymidine kinase. !$#cross-references MUID:90357780; PMID:2389555 !$#accession A37079 !'##molecule_type DNA !'##residues 1-196 ##label BLA !'##cross-references EMBL:M31715; NID:g210655; PIDN:AAA42736.1; !1PID:g210656 REFERENCE A37922 !$#authors Hernandez, A.M.M.; Tabares, E. !$#journal J. Virol. (1991) 65:1046-1052 !$#title Expression and characterization of the thymidine kinase gene !1of African swine fever virus. !$#cross-references MUID:91101261; PMID:1987368 !$#accession A37922 !'##molecule_type DNA !'##residues 1-196 ##label HER !'##cross-references EMBL:M63119; NID:g210657; PIDN:AAA42737.1; !1PID:g210658 CLASSIFICATION #superfamily thymidine kinase KEYWORDS ATP; DNA biosynthesis; nucleotide binding; P-loop; !1phosphotransferase FEATURE !$17-24 #region nucleotide-binding motif A (P-loop) SUMMARY #length 196 #molecular-weight 22420 #checksum 9553 SEQUENCE /// ENTRY KIBET #type complete TITLE thymidine kinase (EC 2.7.1.21) - human herpesvirus 1 ORGANISM #formal_name human herpesvirus 1 DATE 31-Mar-1981 #sequence_revision 29-Jul-1981 #text_change 19-Jan-2001 ACCESSIONS A93715; A00612 REFERENCE A93715 !$#authors McKnight, S.L. !$#journal Nucleic Acids Res. (1980) 8:5949-5964 !$#title The nucleotide sequence and transcript map of the Herpes !1simplex thymidine kinase gene. !$#cross-references MUID:81124310; PMID:6258156 !$#accession A93715 !'##molecule_type DNA !'##residues 1-376 ##label MCK !'##cross-references GB:J02224 CLASSIFICATION #superfamily herpesvirus thymidine kinase; herpesvirus !1thymidine kinase homology KEYWORDS ATP; DNA biosynthesis; nucleotide binding; P-loop; !1phosphotransferase FEATURE !$49-331 #domain herpesvirus thymidine kinase homology #label !8HTK\ !$56-63 #region nucleotide-binding motif A (P-loop)\ !$158-162 #region nucleotide-binding motif B\ !$62 #binding_site ATP (Lys) #status predicted SUMMARY #length 376 #molecular-weight 40898 #checksum 8695 SEQUENCE /// ENTRY KIBETC #type complete TITLE thymidine kinase (EC 2.7.1.21) - human herpesvirus 1 (strain CL101) ORGANISM #formal_name human herpesvirus 1 DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 19-Jan-2001 ACCESSIONS A93870; A00612 REFERENCE A93870 !$#authors Wagner, M.J.; Sharp, J.A.; Summers, W.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:1441-1445 !$#title Nucleotide sequence of the thymidine kinase gene of Herpes !1simplex virus type 1. !$#cross-references MUID:81199468; PMID:6262799 !$#accession A93870 !'##molecule_type DNA !'##residues 1-376 ##label WAG !'##cross-references GB:V00467; NID:g59828; PIDN:CAA23741.1; PID:g59829 CLASSIFICATION #superfamily herpesvirus thymidine kinase; herpesvirus !1thymidine kinase homology KEYWORDS ATP; DNA biosynthesis; nucleotide binding; P-loop; !1phosphotransferase FEATURE !$49-331 #domain herpesvirus thymidine kinase homology #label !8HTK\ !$56-63 #region nucleotide-binding motif A (P-loop)\ !$158-162 #region nucleotide-binding motif B\ !$62 #binding_site ATP (Lys) #status predicted SUMMARY #length 376 #molecular-weight 40912 #checksum 8972 SEQUENCE /// ENTRY KIBEHF #type complete TITLE thymidine kinase (EC 2.7.1.21) - human herpesvirus 1 (strain HFEM) ORGANISM #formal_name human herpesvirus 1 DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 19-Jan-2001 ACCESSIONS A24187 REFERENCE A94342 !$#authors Gompels, U.; Minson, A. !$#journal Virology (1986) 153:230-247 !$#title The properties and sequence of glycoprotein H of herpes !1simplex virus type 1. !$#cross-references MUID:86291165; PMID:3016991 !$#accession A24187 !'##molecule_type DNA !'##residues 1-376 ##label GOM !'##cross-references GB:M14884; NID:g330213; PIDN:AAA45814.1; !1PID:g330215 CLASSIFICATION #superfamily herpesvirus thymidine kinase; herpesvirus !1thymidine kinase homology KEYWORDS ATP; DNA biosynthesis; nucleotide binding; P-loop; !1phosphotransferase FEATURE !$49-331 #domain herpesvirus thymidine kinase homology #label !8HTK\ !$56-63 #region nucleotide-binding motif A (P-loop)\ !$158-162 #region nucleotide-binding motif B\ !$62 #binding_site ATP (Lys) #status predicted SUMMARY #length 376 #molecular-weight 40858 #checksum 8545 SEQUENCE /// ENTRY KIBE16 #type complete TITLE thymidine kinase (EC 2.7.1.21) - human herpesvirus 1 (strain SC16) ORGANISM #formal_name human herpesvirus 1 DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 19-Jan-2001 ACCESSIONS A27240 REFERENCE A27240 !$#authors Darby, G.; Larder, B.A.; Inglis, M.M. !$#journal J. Gen. Virol. (1986) 67:753-758 !$#title Evidence that the 'active centre' of the herpes simplex !1virus thymidine kinase involves an interaction between three !1distinct regions of the polypeptide. !$#cross-references MUID:86170422; PMID:3007662 !$#accession A27240 !'##molecule_type DNA !'##residues 1-376 ##label DAR !'##cross-references GB:X03764; NID:g59889; PIDN:CAA27395.1; PID:g59890 CLASSIFICATION #superfamily herpesvirus thymidine kinase; herpesvirus !1thymidine kinase homology KEYWORDS ATP; DNA biosynthesis; nucleotide binding; P-loop; !1phosphotransferase FEATURE !$49-331 #domain herpesvirus thymidine kinase homology #label !8HTK\ !$56-63 #region nucleotide-binding motif A (P-loop)\ !$158-162 #region nucleotide-binding motif B\ !$62 #binding_site ATP (Lys) #status predicted SUMMARY #length 376 #molecular-weight 40876 #checksum 8601 SEQUENCE /// ENTRY KIBE17 #type complete TITLE thymidine kinase (EC 2.7.1.21) - human herpesvirus 1 (strain 17) ORGANISM #formal_name human herpesvirus 1 DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 19-Jan-2001 ACCESSIONS E30084 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession E30084 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-376 ##label MCG !'##cross-references GB:X14112; NID:g1944536; PIDN:CAA32315.1; !1PID:g59524 CLASSIFICATION #superfamily herpesvirus thymidine kinase; herpesvirus !1thymidine kinase homology KEYWORDS ATP; DNA biosynthesis; nucleotide binding; P-loop; !1phosphotransferase FEATURE !$49-331 #domain herpesvirus thymidine kinase homology #label !8HTK\ !$56-63 #region nucleotide-binding motif A (P-loop)\ !$158-162 #region nucleotide-binding motif B\ !$62 #binding_site ATP (Lys) #status predicted SUMMARY #length 376 #molecular-weight 40921 #checksum 7885 SEQUENCE /// ENTRY KIBEKS #type complete TITLE thymidine kinase (EC 2.7.1.21) - human herpesvirus 1 (strain KOS) ORGANISM #formal_name human herpesvirus 1 #note host Homo sapiens (man) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 19-Jan-2001 ACCESSIONS A31291 REFERENCE A31291 !$#authors Irmiere, A.F.; Manos, M.M.; Jacobson, J.G.; Gibbs, J.S.; !1Coen, D.M. !$#journal Virology (1989) 168:210-220 !$#title Effect of an amber mutation in the herpes simplex virus !1thymidine kinase gene on polypeptide synthesis and !1stability. !$#cross-references MUID:89130932; PMID:2536979 !$#accession A31291 !'##molecule_type DNA !'##residues 1-376 ##label IRM !'##cross-references GB:J04327 COMMENT The sequence from the mutant KG111 differs from that shown !1in having 175-Thr. CLASSIFICATION #superfamily herpesvirus thymidine kinase; herpesvirus !1thymidine kinase homology KEYWORDS ATP; DNA biosynthesis; nucleotide binding; P-loop; !1phosphotransferase FEATURE !$49-331 #domain herpesvirus thymidine kinase homology #label !8HTK\ !$56-63 #region nucleotide-binding motif A (P-loop)\ !$158-162 #region nucleotide-binding motif B\ !$62 #binding_site ATP (Lys) #status predicted SUMMARY #length 376 #molecular-weight 40927 #checksum 8280 SEQUENCE /// ENTRY KIBET3 #type complete TITLE thymidine kinase (EC 2.7.1.21) - human herpesvirus 2 (strain 333) ORGANISM #formal_name human herpesvirus 2 #note host Homo sapiens (man) DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 19-Jan-2001 ACCESSIONS A90648; A92992; T01963; A00613 REFERENCE A90648 !$#authors Kit, S.; Kit, M.; Qavi, H.; Trkula, D.; Otsuka, H. !$#journal Biochim. Biophys. Acta (1983) 741:158-170 !$#title Nucleotide sequence of the herpes simplex virus type 2 (HSV- !12) thymidine kinase gene and predicted amino acid sequence !1of thymidine kinase polypeptide and its comparison with the !1HSV-1 thymidine kinase gene. !$#cross-references MUID:84080453; PMID:6317035 !$#accession A90648 !'##molecule_type DNA !'##residues 1-375 ##label KIT !'##cross-references GB:X01712; NID:g59898; PIDN:CAA25858.1; PID:g59899 REFERENCE A92992 !$#authors Swain, M.A.; Galloway, D.A. !$#journal J. Virol. (1983) 46:1045-1050 !$#title Nucleotide sequence of the herpes simplex virus type 2 !1thymidine kinase gene. !$#cross-references MUID:83216300; PMID:6304336 !$#accession A92992 !'##molecule_type DNA !'##residues 1-375 ##label SWA !'##cross-references GB:V00466 REFERENCE Z14474 !$#authors Palu, G.; Gerna, G.; Bevilacqua, F.; Marcello, A. !$#journal Virus Res. (1992) 25:133-144 !$#title A point mutation in the thymidine kinase gene is responsible !1for acyclovir-resistance in herpes simplex virus type 2 !1sequential isolates. !$#cross-references MUID:93033713; PMID:1329374 !$#accession T01963 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-75,'H',77-139,'F',141-173,'RPRGTSWEA' ##label PAL !'##cross-references EMBL:S46714; NID:g257970 !'##note the difference at the carboxyl end is due to a genomic mutation CLASSIFICATION #superfamily herpesvirus thymidine kinase; herpesvirus !1thymidine kinase homology KEYWORDS ATP; DNA biosynthesis; nucleotide binding; P-loop; !1phosphotransferase FEATURE !$49-331 #domain herpesvirus thymidine kinase homology #label !8HTK\ !$56-63 #region nucleotide-binding motif A (P-loop)\ !$159-163 #region nucleotide-binding motif B\ !$62 #binding_site ATP (Lys) #status predicted SUMMARY #length 375 #molecular-weight 40370 #checksum 7367 SEQUENCE /// ENTRY KIBEBR #type complete TITLE thymidine kinase (EC 2.7.1.21) - bovine herpesvirus 1 (strain 6660) ORGANISM #formal_name bovine herpesvirus 1 DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 19-Jan-2001 ACCESSIONS A31330 REFERENCE A31330 !$#authors Mittal, S.K.; Field, H.J. !$#journal J. Gen. Virol. (1989) 70:901-918 !$#title Analysis of the bovine herpesvirus type 1 thymidine kinase !1(TK) gene from wild-type virus and TK-deficient mutants. !$#cross-references MUID:89279273; PMID:2543766 !$#accession A31330 !'##molecule_type DNA !'##residues 1-357 ##label MIT !'##cross-references EMBL:D00438; NID:g221806; PIDN:BAA00339.1; !1PID:g221807 CLASSIFICATION #superfamily herpesvirus thymidine kinase; herpesvirus !1thymidine kinase homology KEYWORDS ATP; DNA biosynthesis; nucleotide binding; P-loop; !1phosphotransferase FEATURE !$10-306 #domain herpesvirus thymidine kinase homology #label !8HTK\ !$17-24 #region nucleotide-binding motif A (P-loop)\ !$128-132 #region nucleotide-binding motif B\ !$23 #binding_site ATP (Lys) #status predicted SUMMARY #length 357 #molecular-weight 36759 #checksum 7271 SEQUENCE /// ENTRY KIBEBT #type complete TITLE thymidine kinase (EC 2.7.1.21) - bovine herpesvirus 1 (strain Q3932) ORGANISM #formal_name bovine herpesvirus 1 DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 19-Jan-2001 ACCESSIONS A36254 REFERENCE A36254 !$#authors Smith, G.A.; Young, P.L.; Mattick, J.S. !$#journal J. Gen. Virol. (1990) 71:2417-2424 !$#title The location and nucleotide sequence of the thymidine kinase !1gene of bovine herpesvirus type 1.2. !$#cross-references MUID:91037975; PMID:2172455 !$#accession A36254 !'##molecule_type DNA !'##residues 1-359 ##label SMI CLASSIFICATION #superfamily herpesvirus thymidine kinase; herpesvirus !1thymidine kinase homology KEYWORDS ATP; DNA biosynthesis; nucleotide binding; P-loop; !1phosphotransferase FEATURE !$10-308 #domain herpesvirus thymidine kinase homology #label !8HTK\ !$17-24 #region nucleotide-binding motif A (P-loop)\ !$129-133 #region nucleotide-binding motif B\ !$23 #binding_site ATP (Lys) #status predicted SUMMARY #length 359 #molecular-weight 36902 #checksum 5566 SEQUENCE /// ENTRY A45663 #type complete TITLE thymidine kinase (EC 2.7.1.21) - bovine herpesvirus 5 (strain N569) ORGANISM #formal_name bovine herpesvirus 5 DATE 24-Feb-1994 #sequence_revision 24-Feb-1994 #text_change 19-Jan-2001 ACCESSIONS A45663 REFERENCE A45663 !$#authors Smith, G.A.; Young, P.L.; Mattick, J.S. !$#journal Arch. Virol. (1991) 119:199-210 !$#title Nucleotide and amino acid sequence analysis of the thymidine !1kinase gene of a bovine encephalitis herpesvirus. !$#cross-references MUID:91345479; PMID:1678935 !$#accession A45663 !'##molecule_type DNA !'##residues 1-350 ##label SMI !'##cross-references GB:S56149; NID:g234022; PIDN:AAB19542.1; !1PID:g234023 !'##note sequence extracted from NCBI backbone (NCBIN:56149, !1NCBIP:56150) CLASSIFICATION #superfamily herpesvirus thymidine kinase; herpesvirus !1thymidine kinase homology KEYWORDS ATP; DNA biosynthesis; nucleotide binding; P-loop; !1phosphotransferase FEATURE !$8-298 #domain herpesvirus thymidine kinase homology #label !8HTK\ !$15-22 #region nucleotide-binding motif A (P-loop)\ !$120-124 #region nucleotide-binding motif B\ !$21 #binding_site ATP (Lys) #status predicted SUMMARY #length 350 #molecular-weight 36262 #checksum 6332 SEQUENCE /// ENTRY KIBEB2 #type complete TITLE thymidine kinase (EC 2.7.1.21) - bovine herpesvirus 2 ORGANISM #formal_name bovine herpesvirus 2 #note host Bos primigenius taurus (cattle) DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 19-Jan-2001 ACCESSIONS JT0532 REFERENCE JT0532 !$#authors Sheppard, M.; May, J.T. !$#journal J. Gen. Virol. (1989) 70:3067-3071 !$#title Location and characterization of the bovine herpesvirus type !12 thymidine kinase gene. !$#cross-references MUID:90063553; PMID:2555436 !$#accession JT0532 !'##molecule_type DNA !'##residues 1-306 ##label SHE !'##cross-references EMBL:D00537; NID:g221804; PIDN:BAA00425.1; !1PID:g221805 CLASSIFICATION #superfamily herpesvirus thymidine kinase; herpesvirus !1thymidine kinase homology KEYWORDS ATP; DNA biosynthesis; nucleotide binding; P-loop; !1phosphotransferase FEATURE !$4-278 #domain herpesvirus thymidine kinase homology #label !8HTK\ !$11-18 #region nucleotide-binding motif A (P-loop)\ !$111-115 #region nucleotide-binding motif B\ !$17 #binding_site ATP (Lys) #status predicted SUMMARY #length 306 #molecular-weight 32929 #checksum 8076 SEQUENCE /// ENTRY KIBEFH #type complete TITLE thymidine kinase (EC 2.7.1.21) - feline herpesvirus 1 (strain UC-D) ORGANISM #formal_name feline herpesvirus 1 #note host Felis silvestris catus (domestic cat) DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 19-Jan-2001 ACCESSIONS A32388 REFERENCE A32388 !$#authors Nunberg, J.H.; Wright, D.K.; Cole, G.E.; Petrovskis, E.A.; !1Post, L.E.; Compton, T.; Gilbert, J.H. !$#journal J. Virol. (1989) 63:3240-3249 !$#title Identification of the thymidine kinase gene of feline !1herpesvirus: use of degenerate oligonucleotides in the !1polymerase chain reaction to isolate herpesvirus gene !1homologs. !$#cross-references MUID:89311610; PMID:2746729 !$#accession A32388 !'##molecule_type DNA !'##residues 1-343 ##label NUN !'##cross-references GB:M26660; NID:g331066; PIDN:AAA46172.1; !1PID:g331068 CLASSIFICATION #superfamily herpesvirus thymidine kinase; herpesvirus !1thymidine kinase homology KEYWORDS ATP; DNA biosynthesis; nucleotide binding; P-loop; !1phosphotransferase FEATURE !$20-306 #domain herpesvirus thymidine kinase homology #label !8HTK\ !$27-34 #region nucleotide-binding motif A (P-loop)\ !$128-134 #region nucleotide-binding motif B\ !$33 #binding_site ATP (Lys) #status predicted SUMMARY #length 343 #molecular-weight 38922 #checksum 8061 SEQUENCE /// ENTRY KIBEE4 #type complete TITLE thymidine kinase (EC 2.7.1.21) - equine herpesvirus 4 (strain 1942) ORGANISM #formal_name equine herpesvirus 4 DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 19-Jan-2001 ACCESSIONS A36657 REFERENCE A36657 !$#authors Nicolson, L.; Cullinane, A.A.; Onions, D.E. !$#journal J. Gen. Virol. (1990) 71:1801-1805 !$#title The nucleotide sequence of the equine herpesvirus 4 !1thymidine kinase gene. !$#cross-references MUID:90362067; PMID:2391500 !$#accession A36657 !'##molecule_type DNA !'##residues 1-352 ##label NIC !'##cross-references GB:D14486; GB:D00684; NID:g221820; PIDN:BAA03378.1; !1PID:g221822 CLASSIFICATION #superfamily herpesvirus thymidine kinase; herpesvirus !1thymidine kinase homology KEYWORDS ATP; DNA biosynthesis; nucleotide binding; P-loop; !1phosphotransferase FEATURE !$25-310 #domain herpesvirus thymidine kinase homology #label !8HTK\ !$32-39 #region nucleotide-binding motif A (P-loop)\ !$132-138 #region nucleotide-binding motif B\ !$38 #binding_site ATP (Lys) #status predicted SUMMARY #length 352 #molecular-weight 38784 #checksum 1451 SEQUENCE /// ENTRY KIBED2 #type complete TITLE thymidine kinase (EC 2.7.1.21) - equine herpesvirus 1 ORGANISM #formal_name equine herpesvirus 1 DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 19-Jan-2001 ACCESSIONS S01995; D36799; S25498; A56627 REFERENCE S01993 !$#authors Robertson, G.R.; Whalley, J.M. !$#journal Nucleic Acids Res. (1988) 16:11303-11317 !$#title Evolution of the herpes thymidine kinase: identification and !1comparison of the equine herpesvirus 1 thymidine kinase gene !1reveals similarity to a cell-encoded thymidylate kinase. !$#cross-references MUID:89083562; PMID:2849761 !$#accession S01995 !'##molecule_type DNA !'##residues 1-352 ##label ROB !'##cross-references EMBL:X13209; NID:g59229; PIDN:CAA31599.1; !1PID:g59232 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession D36799 !'##molecule_type DNA !'##residues 1-352 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02474.1; !1PID:g330831 !'##experimental_source strain Ab4p REFERENCE S25496 !$#authors Corrochano, L.M.; Madueno, F.; Field, H.J.; de la Fuente, R. !$#submission submitted to the EMBL Data Library, August 1992 !$#description DNA sequence analysis of thymidine kinase defective mutants !1of equine herpesvirus-1 (EHV-1). !$#accession S25498 !'##molecule_type DNA !'##residues 1-352 ##label COR !'##cross-references EMBL:X67961; NID:g59213; PIDN:CAA48144.1; !1PID:g59214 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given REFERENCE A56627 !$#authors Robertson, G.R.; Scott, N.A.; Miller, J.M.; Sabine, M.; !1Zheng, M.; Bell, C.W.; Whalley, J.M. !$#journal DNA Seq. (1991) 1:241-249 !$#title Sequence characteristics of a gene in equine herpesvirus 1 !1homologous to glycoprotein H of herpes simplex virus. !$#cross-references MUID:92216126; PMID:1666854 !$#accession A56627 !'##status preliminary !'##molecule_type DNA !'##residues 337-352 ##label RO2 !'##cross-references GB:S93400; NID:g59229 !'##experimental_source strain HVS 25A !'##note sequence extracted from NCBI backbone (NCBIN:93400, !1NCBIP:93440) FUNCTION !$#description catalyzes the reversible phosphorylation of thymidine by ATP !1to produce thymidine 5'-phosphate and ADP CLASSIFICATION #superfamily herpesvirus thymidine kinase; herpesvirus !1thymidine kinase homology KEYWORDS ATP; DNA biosynthesis; nucleotide binding; P-loop; !1phosphotransferase FEATURE !$25-310 #domain herpesvirus thymidine kinase homology #label !8HTK\ !$32-39 #region nucleotide-binding motif A (P-loop)\ !$134-138 #region nucleotide-binding motif B\ !$38 #binding_site ATP (Lys) #status predicted SUMMARY #length 352 #molecular-weight 38750 #checksum 1481 SEQUENCE /// ENTRY KIBETM #type complete TITLE thymidine kinase (EC 2.7.1.21) - saimiriine herpesvirus 1 ORGANISM #formal_name saimiriine herpesvirus 1 #note host (marmoset) DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 19-Jan-2001 ACCESSIONS A00614 REFERENCE A00614 !$#authors Otsuka, H.; Kit, S. !$#journal Virology (1984) 135:316-330 !$#title Nucleotide sequence of the marmoset herpesvirus thymidine !1kinase gene and predicted amino acid sequence of thymidine !1kinase polypeptide. !$#cross-references MUID:84251697; PMID:6330976 !$#accession A00614 !'##molecule_type DNA !'##residues 1-376 ##label OTS !'##cross-references GB:K02122 CLASSIFICATION #superfamily herpesvirus thymidine kinase; herpesvirus !1thymidine kinase homology KEYWORDS ATP; DNA biosynthesis; nucleotide binding; P-loop; !1phosphotransferase FEATURE !$10-316 #domain herpesvirus thymidine kinase homology #label !8HTK\ !$17-24 #region nucleotide-binding motif A (P-loop)\ !$126-130 #region nucleotide-binding motif B\ !$23 #binding_site ATP (Lys) #status predicted SUMMARY #length 376 #molecular-weight 41334 #checksum 3488 SEQUENCE /// ENTRY KIBETH #type complete TITLE thymidine kinase (EC 2.7.1.21) - turkey herpesvirus ORGANISM #formal_name turkey herpesvirus DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 19-Jan-2001 ACCESSIONS A33346 REFERENCE A33346 !$#authors Martin, S.L.; Aparisio, D.I.; Bandyopadhyay, P.K. !$#journal J. Virol. (1989) 63:2847-2852 !$#title Genetic and biochemical characterization of the thymidine !1kinase gene from herpesvirus of turkeys. !$#cross-references MUID:89259069; PMID:2724415 !$#accession A33346 !'##molecule_type DNA !'##residues 1-310 ##label MAR !'##cross-references GB:M26659; NID:g330940; PIDN:AAA46109.1; !1PID:g330941 CLASSIFICATION #superfamily herpesvirus thymidine kinase; herpesvirus !1thymidine kinase homology KEYWORDS ATP; DNA biosynthesis; nucleotide binding; P-loop; !1phosphotransferase FEATURE !$10-301 #domain herpesvirus thymidine kinase homology #label !8HTK\ !$17-24 #region nucleotide-binding motif A (P-loop)\ !$117-121 #region nucleotide-binding motif B\ !$23 #binding_site ATP (Lys) #status predicted SUMMARY #length 310 #molecular-weight 35512 #checksum 7680 SEQUENCE /// ENTRY KIBEFC #type complete TITLE thymidine kinase (EC 2.7.1.21) - turkey herpesvirus (strain Fc-126) ORGANISM #formal_name turkey herpesvirus DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 19-Jan-2001 ACCESSIONS A33375 REFERENCE A33375 !$#authors Scott, S.D.; Ross, N.L.J.; Binns, M.M. !$#journal J. Gen. Virol. (1989) 70:3055-3065 !$#title Nucleotide and predicted amino acid sequences of the Marek's !1disease virus and turkey herpesvirus thymidine kinase genes; !1comparison with thymidine kinase genes of other !1herpesviruses. !$#cross-references MUID:90063552; PMID:2555435 !$#accession A33375 !'##molecule_type DNA !'##residues 1-350 ##label SCO !'##cross-references EMBL:D00561 CLASSIFICATION #superfamily herpesvirus thymidine kinase; herpesvirus !1thymidine kinase homology KEYWORDS ATP; DNA biosynthesis; nucleotide binding; P-loop; !1phosphotransferase FEATURE !$10-301 #domain herpesvirus thymidine kinase homology #label !8HTK\ !$17-24 #region nucleotide-binding motif A (P-loop)\ !$117-121 #region nucleotide-binding motif B\ !$23 #binding_site ATP (Lys) #status predicted SUMMARY #length 350 #molecular-weight 39968 #checksum 1250 SEQUENCE /// ENTRY KIBEMV #type complete TITLE thymidine kinase (EC 2.7.1.21) - Marek's disease virus (strain RB1B) ORGANISM #formal_name Marek's disease virus DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 19-Jan-2001 ACCESSIONS B33375 REFERENCE A33375 !$#authors Scott, S.D.; Ross, N.L.J.; Binns, M.M. !$#journal J. Gen. Virol. (1989) 70:3055-3065 !$#title Nucleotide and predicted amino acid sequences of the Marek's !1disease virus and turkey herpesvirus thymidine kinase genes; !1comparison with thymidine kinase genes of other !1herpesviruses. !$#cross-references MUID:90063552; PMID:2555435 !$#accession B33375 !'##molecule_type DNA !'##residues 1-353 ##label SCO !'##cross-references EMBL:D00561 CLASSIFICATION #superfamily herpesvirus thymidine kinase; herpesvirus !1thymidine kinase homology KEYWORDS ATP; DNA biosynthesis; nucleotide binding; P-loop; !1phosphotransferase FEATURE !$19-310 #domain herpesvirus thymidine kinase homology #label !8HTK\ !$26-33 #region nucleotide-binding motif A (P-loop)\ !$126-130 #region nucleotide-binding motif B\ !$32 #binding_site ATP (Lys) #status predicted SUMMARY #length 353 #molecular-weight 40508 #checksum 2391 SEQUENCE /// ENTRY KIBE36 #type complete TITLE thymidine kinase (EC 2.7.1.21) - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 19-Jan-2001 ACCESSIONS A27341; A45715 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession A27341 !'##molecule_type DNA !'##residues 1-341 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27919.1; !1PID:g60025 REFERENCE A45715 !$#authors Talarico, C.L.; Phelps, W.C.; Biron, K.K. !$#journal J. Virol. (1993) 67:1024-1033 !$#title Analysis of the thymidine kinase genes from !1acyclovir-resistant mutants of varicella-zoster virus !1isolated from patients with AIDS. !$#cross-references MUID:93124537; PMID:8380452 !$#contents annotation; analysis of acyclovir-resistant strain mutations CLASSIFICATION #superfamily herpesvirus thymidine kinase; herpesvirus !1thymidine kinase homology KEYWORDS ATP; DNA biosynthesis; nucleotide binding; P-loop; !1phosphotransferase FEATURE !$12-300 #domain herpesvirus thymidine kinase homology #label !8HTK\ !$19-26 #region nucleotide-binding motif A (P-loop)\ !$125-129 #region nucleotide-binding motif B\ !$25 #binding_site ATP (Lys) #status predicted SUMMARY #length 341 #molecular-weight 37816 #checksum 3054 SEQUENCE /// ENTRY KIBEEL #type complete TITLE thymidine kinase (EC 2.7.1.21) - human herpesvirus 3 (strains Ellen, Oka, ppIIa, and 5-1-1) ALTERNATE_NAMES pyrimidine deoxyribonucleoside kinase ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 19-Jan-2001 ACCESSIONS A28930; A46450 REFERENCE A92798 !$#authors Sawyer, M.H.; Inchauspe, G.; Biron, K.K.; Waters, D.J.; !1Straus, S.E.; Ostrove, J.M. !$#journal J. Gen. Virol. (1988) 69:2585-2593 !$#title Molecular analysis of the pyrimidine deoxyribonucleoside !1kinase gene of wild-type and acyclovir-resistant strains of !1varicella-zoster virus. !$#cross-references MUID:89010695; PMID:2844967 !$#accession A28930 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-341 ##label SAW !'##experimental_source strains Ellen, Oka, ppIIa, 5-1-1 REFERENCE A46450 !$#authors Mori, H.; Shiraki, K.; Kato, T.; Hayakawa, Y.; Yamanishi, !1K.; Takahashi, M. !$#journal Intervirology (1988) 29:301-310 !$#title Molecular analysis of the thymidine kinase gene of thymidine !1kinase-deficient mutants of varicella-zoster virus. !$#cross-references MUID:89154977; PMID:2852653 !$#accession A46450 !'##status preliminary !'##molecule_type DNA !'##residues 1-341 ##label MOR !'##cross-references GB:M36160; NID:g330326; PIDN:AAA45865.1; !1PID:g330327 !'##experimental_source strain Oka CLASSIFICATION #superfamily herpesvirus thymidine kinase; herpesvirus !1thymidine kinase homology KEYWORDS ATP; DNA biosynthesis; nucleotide binding; P-loop; !1phosphotransferase FEATURE !$12-300 #domain herpesvirus thymidine kinase homology #label !8HTK\ !$19-26 #region nucleotide-binding motif A (P-loop)\ !$125-129 #region nucleotide-binding motif B\ !$25 #binding_site ATP (Lys) #status predicted SUMMARY #length 341 #molecular-weight 37843 #checksum 3033 SEQUENCE /// ENTRY KIBE73 #type complete TITLE thymidine kinase (EC 2.7.1.21) - human herpesvirus 3 (strain 7-1-3) ALTERNATE_NAMES pyrimidine deoxyribonucleoside kinase ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 19-Jan-2001 ACCESSIONS B28930 REFERENCE A92798 !$#authors Sawyer, M.H.; Inchauspe, G.; Biron, K.K.; Waters, D.J.; !1Straus, S.E.; Ostrove, J.M. !$#journal J. Gen. Virol. (1988) 69:2585-2593 !$#title Molecular analysis of the pyrimidine deoxyribonucleoside !1kinase gene of wild-type and acyclovir-resistant strains of !1varicella-zoster virus. !$#cross-references MUID:89010695; PMID:2844967 !$#accession B28930 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-341 ##label SAW CLASSIFICATION #superfamily herpesvirus thymidine kinase; herpesvirus !1thymidine kinase homology KEYWORDS ATP; DNA biosynthesis; nucleotide binding; P-loop; !1phosphotransferase FEATURE !$12-300 #domain herpesvirus thymidine kinase homology #label !8HTK\ !$19-26 #region nucleotide-binding motif A (P-loop)\ !$125-129 #region nucleotide-binding motif B\ !$25 #binding_site ATP (Lys) #status predicted SUMMARY #length 341 #molecular-weight 37815 #checksum 3017 SEQUENCE /// ENTRY KIBE40 #type complete TITLE thymidine kinase (EC 2.7.1.21) - human herpesvirus 3 (strain 40a2) ALTERNATE_NAMES pyrimidine deoxyribonucleoside kinase ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 19-Jan-2001 ACCESSIONS C28930 REFERENCE A92798 !$#authors Sawyer, M.H.; Inchauspe, G.; Biron, K.K.; Waters, D.J.; !1Straus, S.E.; Ostrove, J.M. !$#journal J. Gen. Virol. (1988) 69:2585-2593 !$#title Molecular analysis of the pyrimidine deoxyribonucleoside !1kinase gene of wild-type and acyclovir-resistant strains of !1varicella-zoster virus. !$#cross-references MUID:89010695; PMID:2844967 !$#accession C28930 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-341 ##label SAW CLASSIFICATION #superfamily herpesvirus thymidine kinase; herpesvirus !1thymidine kinase homology KEYWORDS ATP; DNA biosynthesis; nucleotide binding; P-loop; !1phosphotransferase FEATURE !$12-300 #domain herpesvirus thymidine kinase homology #label !8HTK\ !$19-26 #region nucleotide-binding motif A (P-loop)\ !$125-129 #region nucleotide-binding motif B\ !$25 #binding_site ATP (Lys) #status predicted SUMMARY #length 341 #molecular-weight 37827 #checksum 3193 SEQUENCE /// ENTRY KIBEGK #type complete TITLE thymidine kinase (EC 2.7.1.21) - human herpesvirus 3 (strain GK) ALTERNATE_NAMES pyrimidine deoxyribonucleoside kinase ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 19-Jan-2001 ACCESSIONS E28930 REFERENCE A92798 !$#authors Sawyer, M.H.; Inchauspe, G.; Biron, K.K.; Waters, D.J.; !1Straus, S.E.; Ostrove, J.M. !$#journal J. Gen. Virol. (1988) 69:2585-2593 !$#title Molecular analysis of the pyrimidine deoxyribonucleoside !1kinase gene of wild-type and acyclovir-resistant strains of !1varicella-zoster virus. !$#cross-references MUID:89010695; PMID:2844967 !$#accession E28930 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-341 ##label SAW CLASSIFICATION #superfamily herpesvirus thymidine kinase; herpesvirus !1thymidine kinase homology KEYWORDS ATP; DNA biosynthesis; nucleotide binding; P-loop; !1phosphotransferase FEATURE !$12-300 #domain herpesvirus thymidine kinase homology #label !8HTK\ !$19-26 #region nucleotide-binding motif A (P-loop)\ !$125-129 #region nucleotide-binding motif B\ !$25 #binding_site ATP (Lys) #status predicted SUMMARY #length 341 #molecular-weight 37871 #checksum 3747 SEQUENCE /// ENTRY D43675 #type complete TITLE thymidine kinase (EC 2.7.1.21) - infectious laryngotracheitis virus (strain Thorne) ORGANISM #formal_name infectious laryngotracheitis virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 19-Jan-2001 ACCESSIONS D43675 REFERENCE A43675 !$#authors Griffin, A.M.; Boursnell, M.E.G. !$#journal J. Gen. Virol. (1990) 71:841-850 !$#title Analysis of the nucleotide sequence of DNA from the region !1of the thymidine kinase gene of infectious laryngotracheitis !1virus; potential evolutionary relationships between the !1herpesvirus subfamilies. !$#cross-references MUID:90218031; PMID:2157797 !$#accession D43675 !'##molecule_type DNA !'##residues 1-364 ##label GRI !'##cross-references GB:D00565; NID:g221899; PIDN:BAA00442.1; !1PID:g221903 CLASSIFICATION #superfamily herpesvirus thymidine kinase; herpesvirus !1thymidine kinase homology KEYWORDS ATP; DNA biosynthesis; nucleotide binding; P-loop; !1phosphotransferase FEATURE !$30-321 #domain herpesvirus thymidine kinase homology #label !8HTK\ !$36-43 #region nucleotide-binding motif A (P-loop)\ !$143-147 #region nucleotide-binding motif B\ !$42 #binding_site ATP (Lys) #status predicted SUMMARY #length 364 #molecular-weight 40214 #checksum 8025 SEQUENCE /// ENTRY KIBEHS #type complete TITLE thymidine kinase (EC 2.7.1.21) - saimiriine herpesvirus 1 (strain 11[Onc]) ORGANISM #formal_name saimiriine herpesvirus 1 #note host Saimiri sciureus (common squirrel monkey) DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 19-Jan-2001 ACCESSIONS A33374 REFERENCE A33374 !$#authors Honess, R.W.; Craxton, M.A.; Williams, L.; Gompels, U.A. !$#journal J. Gen. Virol. (1989) 70:3003-3013 !$#title A comparative analysis of the sequence of the thymidine !1kinase gene of a gammaherpesvirus, herpesvirus saimiri. !$#cross-references MUID:90063548; PMID:2555434 !$#accession A33374 !'##molecule_type DNA !'##residues 1-527 ##label HON !'##cross-references EMBL:D00543; NID:g221853; PIDN:BAA00432.1; !1PID:g221856 CLASSIFICATION #superfamily saimiriine herpesvirus 1 thymidine kinase; !1herpesvirus thymidine kinase homology KEYWORDS ATP; DNA biosynthesis; nucleotide binding; P-loop; !1phosphotransferase FEATURE !$209-492 #domain herpesvirus thymidine kinase homology #label !8HTK\ !$216-223 #region nucleotide-binding motif A (P-loop)\ !$311-315 #region nucleotide-binding motif B\ !$222 #binding_site ATP (Lys) #status predicted SUMMARY #length 527 #molecular-weight 59806 #checksum 4764 SEQUENCE /// ENTRY T42934 #type complete TITLE thymidine kinase (EC 2.7.1.21) [similarity] - ateline herpesvirus 3 (strain 73) ORGANISM #formal_name ateline herpesvirus 3 #variety strain 73 DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 05-May-2000 ACCESSIONS T42934 REFERENCE Z22274 !$#authors Albrecht, J.C.; Fleckenstein, B. !$#submission submitted to the EMBL Data Library, August 1998 !$#description Primary structure of the herpesvirus ateles genome. !$#accession T42934 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-527 ##label ALB !'##cross-references EMBL:AF083424; PIDN:AAC95545.1 !'##experimental_source strain 73 GENETICS !$#note orf 20 CLASSIFICATION #superfamily saimiriine herpesvirus 1 thymidine kinase; !1herpesvirus thymidine kinase homology KEYWORDS phosphotransferase SUMMARY #length 527 #molecular-weight 59674 #checksum 6817 SEQUENCE /// ENTRY KIBEIC #type complete TITLE thymidine kinase (EC 2.7.1.21) - ictalurid herpesvirus 1 ORGANISM #formal_name ictalurid herpesvirus 1 #note host Ictalurus punctatus (channel catfish) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 11-Jun-1999 ACCESSIONS JQ1336 REFERENCE JQ1336 !$#authors Harrison, P.T.; Thompson, R.; Davison, A.J. !$#journal J. Gen. Virol. (1991) 72:2583-2586 !$#title Evolution of herpesvirus thymidine kinases from cellular !1deoxycytidine kinase. !$#cross-references MUID:92013982; PMID:1919533 !$#accession JQ1336 !'##molecule_type DNA !'##residues 1-228 ##label HAR !'##cross-references GB:M75136; NID:g331209; PIDN:AAA88108.1; !1PID:g331215 CLASSIFICATION #superfamily ictalurid herpesvirus thymidine kinase KEYWORDS ATP; DNA biosynthesis; phosphotransferase SUMMARY #length 228 #molecular-weight 25642 #checksum 9346 SEQUENCE /// ENTRY B65056 #type complete TITLE adenylyl-sulfate kinase (EC 2.7.1.25) precursor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS B65056; JN0328; PS0431; A44200 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65056 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-201 ##label BLAT !'##cross-references GB:AE000358; GB:U00096; NID:g2367156; !1PIDN:AAC75792.1; PID:g1789107; UWGP:b2750 !'##experimental_source strain K-12, substrain MG1655 REFERENCE JN0326 !$#authors Leyh, T.S.; Vogt, T.F.; Suo, Y. !$#journal J. Biol. Chem. (1992) 267:10405-10410 !$#title The DNA sequence of the sulfate activation locus from !1Escherichia coli K-12. !$#cross-references MUID:92268080; PMID:1316900 !$#accession JN0328 !'##molecule_type DNA !'##residues 1-133,'Q',135-201 ##label LEY !'##cross-references GB:M74586; NID:g145670; PIDN:AAA23647.1; !1PID:g145674 !'##experimental_source strain K12 !$#accession PS0431 !'##molecule_type protein !'##residues 'AL',5-9 ##label LEY1 REFERENCE A44200 !$#authors Satishchandran, C.; Hickman, Y.N.; Markham, G.D. !$#journal Biochemistry (1992) 31:11684-11688 !$#title Characterization of the phosphorylated enzyme intermediate !1formed in the adenosine 5'-phosphosulfate kinase reaction. !$#cross-references MUID:93075778; PMID:1332767 !$#accession A44200 !'##molecule_type DNA !'##residues 1-201 ##label SAT !'##note sequence extracted from NCBI backbone (NCBIN:119393, !1NCBIP:119394) GENETICS !$#gene cysC !$#map_position 59 min CLASSIFICATION #superfamily adenylylsulfate kinase; adenylylsulfate kinase !1homology KEYWORDS ATP; P-loop; phosphotransferase; purine nucleotide binding FEATURE !$2-201 #product adenylylsulfate kinase #status experimental !8#label MAT\ !$28-188 #domain adenylylsulfate kinase homology #label ASK\ !$35-42 #domain DNA binding #status predicted #label DNB\ !$35-42 #region nucleotide-binding motif A (P-loop) SUMMARY #length 201 #molecular-weight 22321 #checksum 388 SEQUENCE /// ENTRY S18729 #type complete TITLE adenylyl-sulfate kinase (EC 2.7.1.25) - Pseudomonas aeruginosa ORGANISM #formal_name Pseudomonas aeruginosa DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S18729 REFERENCE S18729 !$#authors Vliegenthart, J.S.; Ketelaar-van Gaalen, P.A.G.; van de !1Klundert, J.A.M. !$#journal Antimicrob. Agents Chemother. (1991) 35:892-897 !$#title Nucleotide sequence of the aacC3 gene, a gentamicin !1resistance determinant encoding aminoglycoside- !1(3)-N-acetyltransferase III expressed in Pseudomonas !1aeruginosa but not in Escherichia coli. !$#cross-references MUID:91307267; PMID:1649572 !$#accession S18729 !'##status preliminary !'##molecule_type DNA !'##residues 1-214 ##label VLI !'##cross-references EMBL:X55652; NID:g45264; PIDN:CAA39183.1; !1PID:g45265 CLASSIFICATION #superfamily adenylylsulfate kinase; adenylylsulfate kinase !1homology KEYWORDS ATP; P-loop; phosphotransferase; purine nucleotide binding FEATURE !$6-165 #domain adenylylsulfate kinase homology #label ASK\ !$13-20 #region nucleotide-binding motif A (P-loop) SUMMARY #length 214 #molecular-weight 23922 #checksum 2008 SEQUENCE /// ENTRY S74917 #type complete TITLE adenylyl-sulfate kinase (EC 2.7.1.25) - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein slr0676 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S74917 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74917 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-177 ##label KAN !'##cross-references EMBL:D90902; GB:AB001339; NID:g1652027; !1PIDN:BAA16957.1; PID:g1652032 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene cysC CLASSIFICATION #superfamily adenylylsulfate kinase; adenylylsulfate kinase !1homology KEYWORDS ATP; P-loop; phosphotransferase; purine nucleotide binding FEATURE !$5-164 #domain adenylylsulfate kinase homology #label ASK\ !$12-19 #region nucleotide-binding motif A (P-loop) SUMMARY #length 177 #molecular-weight 19674 #checksum 8796 SEQUENCE /// ENTRY S47640 #type complete TITLE adenylyl-sulfate kinase (EC 2.7.1.25) precursor - Arabidopsis thaliana ALTERNATE_NAMES APS kinase; protein F26C24.11 ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S47640; T02601; A84521; S38587 REFERENCE S47640 !$#authors Arz, H.E.; Gisselmann, G.; Schiffmann, S.; Schwenn, J.D. !$#journal Biochim. Biophys. Acta (1994) 1218:447-452 !$#title A cDNA for adenylyl sulphate (APS)-kinase from Arabidopsis !1thaliana. !$#cross-references MUID:94325358; PMID:8049272 !$#accession S47640 !'##molecule_type mRNA !'##residues 1-276 ##label ARZ !'##cross-references EMBL:X75782; NID:g414736; PIDN:CAA53426.1; !1PID:g414737 !'##note it is uncertain whether Met-1, Met-14 or Met-26 is the !1initiator REFERENCE Z14680 !$#authors Rounsley, S.D.; Kaul, S.; Lin, X.; Ketchum, K.A.; Crosby, !1M.L.; Brandon, R.C.; Sykes, S.M.; Mason, T.M.; Kerlavage, !1A.R.; Adams, M.D.; Somerville, C.R.; Venter, J.C. !$#submission submitted to the EMBL Data Library, June 1998 !$#description Arabidopsis thaliana chromosome II BAC F26C24 genomic !1sequence. !$#accession T02601 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-276 ##label ROU !'##cross-references EMBL:AC004705; NID:g3252804; PIDN:AAC24182.1; !1PID:g3252812 !'##experimental_source cultivar Columbia REFERENCE A84420 !$#authors Lin, X.; Kaul, S.; Rounsley, S.D.; Shea, T.P.; Benito, M.I.; !1Town, C.D.; Fujii, C.Y.; Mason, T.M.; Bowman, C.L.; !1Barnstead, M.E.; Feldblyum, T.V.; Buell, C.R.; Ketchum, !1K.A.; Lee, J.J.; Ronning, C.M.; Koo, H.; Moffat, K.S.; !1Cronin, L.A.; Shen, M.; VanAken, S.E.; Umayam, L.; Tallon, !1L.J.; Gill, J.E.; Adams, M.D.; Carrera, A.J.; Creasy, T.H.; !1Goodman, H.M.; Somerville, C.R.; Copenhaver, G.P.; Preuss, !1D.; Nierman, W.C.; White, O.; Eisen, J.A.; Salzberg, S.L.; !1Fraser, C.M.; Venter, J.C. !$#journal Nature (1999) 402:761-768 !$#title Sequence and analysis of chromosome 2 of the plant !1Arabidopsis thaliana. !$#cross-references MUID:20083487; PMID:10617197 !$#accession A84521 !'##status preliminary !'##molecule_type DNA !'##residues 1-276 ##label STO !'##cross-references GB:AE002093; NID:g3252812; PIDN:AAC24182.1; !1GSPDB:GN00139 GENETICS !$#gene At2g14750; F26C24.11 !$#map_position 2 !$#genome nuclear !$#introns 66/1; 113/1; 163/1; 202/3; 231/1; 246/3 CLASSIFICATION #superfamily adenylylsulfate kinase; adenylylsulfate kinase !1homology KEYWORDS ATP; P-loop; phosphotransferase; purine nucleotide binding FEATURE !$1-37 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$38-276 #product adenylylsulfate kinase #status predicted !8#label MAT\ !$101-262 #domain adenylylsulfate kinase homology #label ASK\ !$108-115 #region nucleotide-binding motif A (P-loop) SUMMARY #length 276 #molecular-weight 29787 #checksum 2486 SEQUENCE /// ENTRY S17244 #type complete TITLE adenylyl-sulfate kinase (EC 2.7.1.25) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES adenosine-5-phosphosulfate kinase; protein YKL001c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S17244; S25323; S37811 REFERENCE S17244 !$#authors Korch, C.; Mountain, H.A.; Bystroem, A.S. !$#journal Mol. Gen. Genet. (1991) 229:96-108 !$#title Cloning, nucleotide sequence, and regulation of MET14, the !1gene encoding the APS kinase of Saccharomyces cerevisiae. !$#cross-references MUID:91375456; PMID:1654509 !$#accession S17244 !'##molecule_type DNA !'##residues 1-202 ##label KOR !'##cross-references GB:S55315; NID:g235814; PIDN:AAB19854.1; !1PID:g235815 REFERENCE S25322 !$#authors Duesterhoeft, A.; Philippsen, P. !$#journal Yeast (1992) 8:749-759 !$#title DNA sequencing and analysis of a 24.7 kb segment !1encompassing centromere CEN11 of Saccharomyces cerevisiae !1reveals nine previously unknown open reading frames. !$#cross-references MUID:93070612; PMID:1441752 !$#accession S25323 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-202 ##label DUE !'##cross-references EMBL:X65124; NID:g3517; PIDN:CAA46252.1; PID:g3529 !'##experimental_source strain S288C REFERENCE S37811 !$#authors Duesterhoeft, A.; Moestl, D.; Poehlmann, R.; Philippsen, P. !$#submission submitted to the Protein Sequence Database, March 1994 !$#accession S37811 !'##molecule_type DNA !'##residues 1-202 ##label DU2 !'##cross-references EMBL:Z28001; NID:g485972; PIDN:CAA81833.1; !1PID:g485973; GSPDB:GN00011; MIPS:YKL001c !'##experimental_source strain S288C GENETICS !$#gene SGD:MET14; MIPS:YKL001c !'##cross-references SGD:S0001484; MIPS:YKL001c !$#map_position 11L CLASSIFICATION #superfamily adenylylsulfate kinase; adenylylsulfate kinase !1homology KEYWORDS ATP; P-loop; phosphotransferase; purine nucleotide binding FEATURE !$24-187 #domain adenylylsulfate kinase homology #label ASK\ !$31-38 #region nucleotide-binding motif A (P-loop)\ !$37 #binding_site ATP (Lys) #status predicted SUMMARY #length 202 #molecular-weight 23060 #checksum 2954 SEQUENCE /// ENTRY BVECRS #type complete TITLE pantothenate kinase (EC 2.7.1.33) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 08-Feb-1996 #text_change 01-Mar-2002 ACCESSIONS A45727; JV0016; E65204 REFERENCE A45727 !$#authors Song, W.J.; Jackowski, S. !$#journal J. Bacteriol. (1992) 174:6411-6417 !$#title Cloning, sequencing, and expression of the pantothenate !1kinase (coaA) gene of Escherichia coli. !$#cross-references MUID:93015690; PMID:1328157 !$#accession A45727 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-316 ##label SON !'##cross-references GB:M90071; NID:g145559; PIDN:AAA23590.1; !1PID:g145560 REFERENCE A91599 !$#authors Flamm, J.A.; Friesen, J.D.; Otsuka, A.J. !$#journal Gene (1988) 74:555-558 !$#title The nucleotide sequence of the Escherichia coli rts gene. !$#cross-references MUID:89232747; PMID:3073109 !$#accession JV0016 !'##molecule_type DNA !'##residues 'MTRHGKYRFADRAMTARNML',1-316 ##label FLA !'##cross-references GB:M36321; NID:g1000852; PIDN:AAA76838.1; !1PID:g147780 !'##note the authors had assign the initiation codon incorrectly REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65204 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-316 ##label BLAT !'##cross-references GB:AE000471; GB:U00096; NID:g1790404; !1PIDN:AAC76952.1; PID:g1790409; UWGP:b3974 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene coaA; rts !$#map_position 90 min !$#start_codon GTG FUNCTION !$#description catalyzes the transfer of phosphate from ATP to pantothenate !1forming 4'-phosphopantothenate, the rate-controlling step in !1CoA biosynthesis; its activity is subject to feedback !1inhibition; plays a crucial role in regulating the !1inracellular CoA concentration; it is also an essential !1temperature-sensitive allele in E. coli. !$#pathway coenzyme A biosynthesis CLASSIFICATION #superfamily pantothenate kinase KEYWORDS coenzyme A biosynthesis; phosphotransferase SUMMARY #length 316 #molecular-weight 36359 #checksum 1731 SEQUENCE /// ENTRY A42919 #type complete TITLE mevalonate kinase (EC 2.7.1.36) - human ALTERNATE_NAMES MK ORGANISM #formal_name Homo sapiens #common_name man DATE 04-Mar-1993 #sequence_revision 18-Mar-1997 #text_change 11-Jun-1999 ACCESSIONS A42919; A58527 REFERENCE A42919 !$#authors Schafer, B.L.; Bishop, R.W.; Kratunis, V.J.; Kalinowski, !1S.S.; Mosley, S.T.; Gibson, K.M.; Tanaka, R.D. !$#journal J. Biol. Chem. (1992) 267:13229-13238 !$#title Molecular cloning of human mevalonate kinase and !1identification of a missense mutation in the genetic disease !1mevalonic aciduria. !$#cross-references MUID:92317034; PMID:1377680 !$#accession A42919 !'##molecule_type mRNA !'##residues 1-396 ##label SCH !'##cross-references GB:M88468; NID:g307197; PIDN:AAB59362.1; !1PID:g187561 !'##note sequence extracted from NCBI backbone (NCBIN:107743, !1NCBIP:107744) REFERENCE S42226 !$#authors Graef, E.; Caselmann, W.H.; Wells, J.; Koshy, R. !$#journal Oncogene (1994) 9:81-87 !$#title Insertional activation of mevalonate kinase by hepatitis B !1virus DNA in a human hepatoma cell line. !$#cross-references MUID:94134441; PMID:8302606 !$#accession A58527 !'##molecule_type mRNA !'##residues 1-396 ##label GRA !'##cross-references EMBL:X75311; NID:g450345; PIDN:CAA53060.1; !1PID:g450347 GENETICS !$#gene GDB:MVK !'##cross-references GDB:134189; OMIM:251170 !$#map_position 12pter-12qter !$#note defects in this gene can cause mevalonic aciduria FUNCTION !$#description catalyzes the reversible phosphorylation of (R)-mevalonic !1acid by ATP to produce (R)-5-phosphomevalonic acid and ADP !$#pathway isoprenoid biosynthesis !$#note this enzyme can also utilize GTP, CTP, and UTP CLASSIFICATION #superfamily mevalonate kinase KEYWORDS ATP; isoprenoid biosynthesis; phosphotransferase FEATURE !$335-357 #region ATP binding #status predicted\ !$357 #binding_site ATP (Lys) #status predicted SUMMARY #length 396 #molecular-weight 42450 #checksum 3552 SEQUENCE /// ENTRY A35629 #type complete TITLE mevalonate kinase (EC 2.7.1.36) [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 28-Sep-1990 #sequence_revision 18-Mar-1997 #text_change 21-Jul-2000 ACCESSIONS A35629 REFERENCE A35629 !$#authors Tanaka, R.D.; Lee, L.Y.; Schafer, B.L.; Kratunis, V.J.; !1Mohler, W.A.; Robinson, G.W.; Mosley, S.T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:2872-2876 !$#title Molecular cloning of mevalonate kinase and regulation of its !1mRNA levels in rat liver. !$#cross-references MUID:90222132; PMID:2158094 !$#accession A35629 !'##molecule_type mRNA !'##residues 1-395 ##label TAN !'##cross-references GB:M29472; NID:g205377; PIDN:AAA41588.1; !1PID:g205378 FUNCTION !$#description EC 2.7.1.36 [validated, MUID:90222132]; mevalonate kinase; !1catalyzes the reversible phosphorylation of (R)-mevalonic !1acid by ATP to produce (R)-5-phosphomevalonic acid and ADP !$#pathway isoprenoid biosynthesis !$#note this enzyme can also utilize GTP, CTP, and UTP !$#note may function as a regulatory site in the cholesterol !1biosynthetic pathway !$#note a mutation in the gene coding for this enzyme is thought to !1cause the genetic disease mevalonic aciduria CLASSIFICATION #superfamily mevalonate kinase KEYWORDS ATP; isoprenoid biosynthesis; phosphotransferase FEATURE !$330-339 #region ATP binding #status predicted\ !$357 #binding_site ATP (Lys) #status predicted SUMMARY #length 395 #molecular-weight 41987 #checksum 9871 SEQUENCE /// ENTRY S42088 #type complete TITLE mevalonate kinase (EC 2.7.1.36) - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S42088 REFERENCE S42088 !$#authors Riou, C.; Tourte, Y.; Lacroute, F.; Karst, F. !$#submission submitted to the EMBL Data Library, February 1994 !$#description Isolation and characterization of a cDNA encoding !1Arabidopsis thaliana mevalonate kinase by genetic !1complementation in yeast. !$#accession S42088 !'##molecule_type mRNA !'##residues 1-378 ##label RIO !'##cross-references EMBL:X77793; NID:g456613; PIDN:CAA54820.1; !1PID:g456614 FUNCTION !$#description catalyzes the reversible phosphorylation of (R)-mevalonic !1acid by ATP to produce (R)-5-phosphomevalonic acid and ADP !$#pathway isoprenoid biosynthesis !$#note this enzyme can also utilize GTP, CTP, and UTP CLASSIFICATION #superfamily mevalonate kinase KEYWORDS ATP; isoprenoid biosynthesis; phosphotransferase FEATURE !$330-339 #region ATP binding #status predicted\ !$352 #binding_site ATP (Lys) #status predicted SUMMARY #length 378 #molecular-weight 40643 #checksum 6171 SEQUENCE /// ENTRY S62440 #type complete TITLE mevalonate kinase (EC 2.7.1.36) - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES hypothetical protein SPAC13G6.11c ORGANISM #formal_name Schizosaccharomyces pombe DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Dec-1999 ACCESSIONS S62440; T37646 REFERENCE S62430 !$#authors Odell, C.; Bowman, S. !$#submission submitted to the EMBL Data Library, October 1995 !$#accession S62440 !'##status preliminary !'##molecule_type DNA !'##residues 1-404 ##label ODE !'##cross-references EMBL:Z54308; NID:g1008985; PIDN:CAA91104.1; !1PID:g1008996 REFERENCE Z21734 !$#authors Odell, C.; Bowman, S.; Barrell, B.G.; Rajandream, M.A.; !1Walsh, S.V.; Wood, V. !$#submission submitted to the EMBL Data Library, October 1995 !$#accession T37646 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-404 ##label OD2 !'##cross-references EMBL:Z54308; PIDN:CAA91104.1; GSPDB:GN00066; !1SPDB:SPAC13G6.11c !'##experimental_source strain 972h-; cosmid c13G6 GENETICS !$#gene SPDB:SPAC13G6.11c !$#map_position 1L !$#introns 25/3 CLASSIFICATION #superfamily mevalonate kinase KEYWORDS ATP; isoprenoid biosynthesis; phosphotransferase SUMMARY #length 404 #molecular-weight 43406 #checksum 2567 SEQUENCE /// ENTRY BVBYR1 #type complete TITLE mevalonate kinase (EC 2.7.1.36) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YM8261.02; protein YMR208w ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 21-Jul-2000 ACCESSIONS S05875; S13531; S55090 REFERENCE S05875 !$#authors Kearsey, S.E.; Edwards, J. !$#journal Mol. Gen. Genet. (1987) 210:509-517 !$#title Mutations that increase the mitotic stability of !1minichromosomes in yeast: characterization of RAR1. !$#cross-references MUID:88121728; PMID:3323847 !$#accession S05875 !'##molecule_type DNA !'##residues 1-443 ##label KEA !'##cross-references EMBL:X06114; NID:g4286; PIDN:CAA29487.1; PID:g4287 REFERENCE S13531 !$#authors Oulmouden, A.; Karst, F. !$#journal Curr. Genet. (1991) 19:9-14 !$#title Nucleotide sequence of the ERG12 gene of Saccharomyces !1cerevisiae encoding mevalonate kinase. !$#cross-references MUID:91243209; PMID:1645230 !$#accession S13531 !'##molecule_type DNA !'##residues 1-443 ##label OUL !'##cross-references EMBL:X55875; NID:g3683; PIDN:CAA39359.1; PID:g3684 REFERENCE S55089 !$#authors Dedman, K.; Brown, D.; Bowman, S. !$#submission submitted to the EMBL Data Library, June 1995 !$#accession S55090 !'##molecule_type DNA !'##residues 1-443 ##label DED !'##cross-references EMBL:Z49809; NID:g854459; PIDN:CAA89923.1; !1PID:g854460; GSPDB:GN00013; MIPS:YMR208w !'##experimental_source strain AB972 GENETICS !$#gene SGD:ERG12; RAR1; MIPS:YMR208w !'##cross-references SGD:S0004821; MIPS:YMR208w !$#map_position 13R FUNCTION !$#description catalyzes the reversible phosphorylation of (R)-mevalonic !1acid by ATP to produce (R)-5-phosphomevalonic acid and ADP !$#pathway isoprenoid biosynthesis !$#note this enzyme can also utilize GTP, CTP, and UTP CLASSIFICATION #superfamily mevalonate kinase KEYWORDS ATP; isoprenoid biosynthesis; phosphotransferase FEATURE !$348-357 #region ATP binding #status predicted\ !$375 #binding_site ATP (Lys) #status predicted SUMMARY #length 443 #molecular-weight 48459 #checksum 9228 SEQUENCE /// ENTRY KIBPO7 #type complete TITLE protein kinase (EC 2.7.1.37) - phage T7 ORGANISM #formal_name phage T7 DATE 01-Sep-1981 #sequence_revision 01-Sep-1981 #text_change 11-Jun-1999 ACCESSIONS D94615; E92866; S42288; A00616 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession D94615 !'##molecule_type DNA !'##residues 1-359 ##label DU1 REFERENCE A92866 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1981) 148:303-330 !$#title Nucleotide sequence from the genetic left end of !1bacteriophage T7 DNA to the beginning of gene 4. !$#cross-references MUID:82078034; PMID:7310871 !$#accession E92866 !'##molecule_type DNA !'##residues 1-359 ##label DU2 !'##cross-references GB:V01127; NID:g15498; PIDN:CAA24332.1; PID:g15504 REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42288 !'##molecule_type DNA !'##residues 1-359 ##label DUN !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24389.1; !1PID:g15568 COMMENT Protein kinase, which is expressed in the early stage of !1lytic development, interferes with transcription by the host !1RNA polymerase by phosphorylating the beta prime and beta !1subunits of the polymerase. GENETICS !$#gene 0.7 !$#map_position 5.05-7.74 CLASSIFICATION #superfamily phage T7 protein kinase KEYWORDS phosphotransferase SUMMARY #length 359 #molecular-weight 41123 #checksum 2873 SEQUENCE /// ENTRY OKHU1R #type complete TITLE protein kinase (EC 2.7.1.37), cAMP-dependent, type I-alpha regulatory chain - human ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS A34627; A28003 REFERENCE A34627 !$#authors Sandberg, M.; Skaalhegg, B.; Jahnsen, T. !$#journal Biochem. Biophys. Res. Commun. (1990) 167:323-330 !$#title The two mRNA forms for the type I-alpha regulatory subunit !1of cAMP-dependent protein kinase from human testis are due !1to the use of different polyadenylation site signals. !$#cross-references MUID:90179769; PMID:2310396 !$#accession A34627 !'##molecule_type mRNA !'##residues 1-381 ##label SAN !'##cross-references GB:M33336; NID:g1526989; PIDN:AAB50921.1; !1PID:g179895 REFERENCE A28003 !$#authors Sandberg, M.; Tasken, K.; Oeyen, O.; Hansson, V.; Jahnsen, !1T. !$#journal Biochem. Biophys. Res. Commun. (1987) 149:939-945 !$#title Molecular cloning, cDNA structure and deduced amino acid !1sequence for a type I regulatory subunit of cAMP-dependent !1protein kinase from human testis. !$#cross-references MUID:88106558; PMID:3426618 !$#accession A28003 !'##molecule_type mRNA !'##residues 1-381 ##label SA2 !'##cross-references GB:M18468; NID:g1526988; PIDN:AAB50922.1; !1PID:g179922 COMMENT The inactive form of the enzyme is composed of two !1regulatory chains and two catalytic chains. Activation by !1cAMP produces two active catalytic monomers and a regulatory !1dimer that binds four cAMP molecules. COMMENT Four types of regulatory chains are found: I-alpha, I-beta, !1II-alpha, and II-beta. Their expression varies among tissues !1and is in some cases constitutive and in others inducible. COMMENT Type I regulatory chains contain a high-affinity binding !1site for MgATP. COMMENT The pseudophosphorylation site binds to the !1substrate-binding region of the catalytic chain but is not !1phosphorylated. The physiological significance of !1phosphorylations by other kinases is unclear. GENETICS !$#gene GDB:PRKAR1A !'##cross-references GDB:120313; OMIM:188830 !$#map_position 17q23-17q24 CLASSIFICATION #superfamily cAMP-dependent protein kinase regulatory chain; !1cAMP receptor protein cyclic nucleotide-binding domain !1homology KEYWORDS ATP binding; cAMP binding; duplication; heterotetramer; !1homodimer; phosphoprotein; phosphotransferase FEATURE !$1-136 #domain protein interaction #label DIM\ !$96-100 #region pseudophosphorylation motif\ !$137-254 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP1\ !$255-381 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP2\ !$18 #disulfide_bonds interchain (to 39) #status !8predicted\ !$39 #disulfide_bonds interchain (to 18) #status !8predicted\ !$202,211 #binding_site cAMP (Glu, Arg) #status predicted\ !$326,335 #binding_site cAMP (Glu, Arg) #status predicted SUMMARY #length 381 #molecular-weight 42981 #checksum 5115 SEQUENCE /// ENTRY OKRT1R #type complete TITLE protein kinase (EC 2.7.1.37), cAMP-dependent, type I-alpha regulatory chain - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS A26910 REFERENCE A26910 !$#authors Kuno, T.; Ono, Y.; Hirai, M.; Hashimoto, S.; Shuntoh, H.; !1Tanaka, C. !$#journal Biochem. Biophys. Res. Commun. (1987) 146:878-883 !$#title Molecular cloning and cDNA structure of the regulatory !1subunit of type I cAMP-dependent protein kinase from rat !1brain. !$#cross-references MUID:87298524; PMID:3619906 !$#accession A26910 !'##molecule_type mRNA !'##residues 1-381 ##label KUN !'##cross-references GB:M17086; NID:g206672; PIDN:AAB54276.1; !1PID:g206673 COMMENT The inactive form of the enzyme is composed of two !1regulatory chains and two catalytic chains. Activation by !1cAMP produces two active catalytic monomers and a regulatory !1dimer that binds four cAMP molecules. COMMENT Four types of regulatory chains are found: I-alpha, I-beta, !1II-alpha, and II-beta. Their expression varies among tissues !1and is in some cases constitutive and in others inducible. COMMENT Type I regulatory chains contain a high-affinity binding !1site for MgATP. COMMENT The pseudophosphorylation site binds to the !1substrate-binding region of the catalytic chain but is not !1phosphorylated. The physiological significance of !1phosphorylations by other kinases is unclear. CLASSIFICATION #superfamily cAMP-dependent protein kinase regulatory chain; !1cAMP receptor protein cyclic nucleotide-binding domain !1homology KEYWORDS acetylated amino end; ATP binding; cAMP binding; !1duplication; heterotetramer; homodimer; phosphoprotein; !1phosphotransferase FEATURE !$2-381 #product protein kinase, cAMP-dependent, type I-alpha !8regulatory chain #status predicted #label MAT\ !$2-136 #domain protein interaction #label DIM\ !$96-100 #region pseudophosphorylation motif\ !$137-254 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP1\ !$255-381 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP2\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status predicted\ !$18 #disulfide_bonds interchain (to 39) #status !8predicted\ !$39 #disulfide_bonds interchain (to 18) #status !8predicted\ !$202,211 #binding_site cAMP (Glu, Arg) #status predicted\ !$326,335 #binding_site cAMP (Glu, Arg) #status predicted SUMMARY #length 381 #molecular-weight 43095 #checksum 5095 SEQUENCE /// ENTRY OKPG1R #type complete TITLE protein kinase (EC 2.7.1.37), cAMP-dependent, type I-alpha regulatory chain - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS S00083; S28552; A15647; A60477 REFERENCE S00083 !$#authors Nowak, I.; Seipel, K.; Schwarz, M.; Jans, D.A.; Hemmings, !1B.A. !$#journal Eur. J. Biochem. (1987) 167:27-33 !$#title Isolation of a cDNA and characterization of the 5'flanking !1region of the gene encoding the type I regulatory subunit of !1the cAMP-dependent protein kinase. !$#cross-references MUID:87304236; PMID:3040400 !$#accession S00083 !'##molecule_type mRNA !'##residues 1-380 ##label NOW1 !'##cross-references EMBL:X05942; NID:g2049; PIDN:CAA29375.1; PID:g2050 !$#accession S28552 !'##molecule_type DNA !'##residues 1-58 ##label NOW2 !'##cross-references EMBL:X06158; NID:g2047; PIDN:CAA29515.1; PID:g2048 REFERENCE A15647 !$#authors Potter, R.L.; Taylor, S.S. !$#journal J. Biol. Chem. (1980) 255:9706-9712 !$#title The structural domains of cAMP-dependent protein kinase I. !$#cross-references MUID:81046771; PMID:7430094 !$#accession A15647 !'##molecule_type protein !'##residues 'K',96-101 ##label POT !'##note 95-Arg was also found REFERENCE A60477 !$#authors Bubis, J.; Vedvick, T.S.; Taylor, S.S. !$#journal J. Biol. Chem. (1987) 262:14961-14966 !$#title Antiparallel alignment of the two protomers of the !1regulatory subunit dimer of cAMP-dependent protein kinase I. !$#cross-references MUID:88033069; PMID:3667618 !$#contents interchain disulfide bonds !$#accession A60477 !'##molecule_type protein !'##residues 13-23;32-50;346-349;358-364,'V',366-367 ##label BUB COMMENT The inactive form of the enzyme is composed of two !1regulatory chains and two catalytic chains. Activation by !1cAMP produces two active catalytic monomers and a regulatory !1dimer that binds four cAMP molecules. COMMENT Four types of regulatory chains are found: I-alpha, I-beta, !1II-alpha, and II-beta. Their expression varies among tissues !1and is in some cases constitutive and in others inducible. COMMENT Type I regulatory chains contain a high-affinity binding !1site for MgATP. COMMENT The pseudophosphorylation site binds to the !1substrate-binding region of the catalytic chain but is not !1phosphorylated. The physiological significance of !1phosphorylations by other kinases is unclear. GENETICS !$#introns 58/3 CLASSIFICATION #superfamily cAMP-dependent protein kinase regulatory chain; !1cAMP receptor protein cyclic nucleotide-binding domain !1homology KEYWORDS acetylated amino end; ATP binding; cAMP binding; !1duplication; heterotetramer; homodimer; phosphoprotein; !1phosphotransferase FEATURE !$2-380 #product protein kinase, cAMP-dependent, type I-alpha !8regulatory chain #status predicted #label MAT\ !$2-135 #domain protein interaction #label DIM\ !$95-99 #region pseudophosphorylation motif\ !$136-253 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP1\ !$254-380 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP2\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status predicted\ !$17 #disulfide_bonds interchain (to 38) #status !8experimental\ !$38 #disulfide_bonds interchain (to 17) #status !8experimental\ !$201,210 #binding_site cAMP (Glu, Arg) #status predicted\ !$325,334 #binding_site cAMP (Glu, Arg) #status predicted SUMMARY #length 380 #molecular-weight 42921 #checksum 344 SEQUENCE /// ENTRY OKBO1R #type complete TITLE protein kinase (EC 2.7.1.37), cAMP-dependent, type I-alpha regulatory chain - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 16-Jul-1999 ACCESSIONS A00617; B60477 REFERENCE A00617 !$#authors Titani, K.; Sasagawa, T.; Ericsson, L.H.; Kumar, S.; Smith, !1S.B.; Krebs, E.G.; Walsh, K.A. !$#journal Biochemistry (1984) 23:4193-4199 !$#title Amino acid sequence of the regulatory subunit of bovine type !1I adenosine cyclic 3'.5'-phosphate dependent protein kinase. !$#cross-references MUID:85023305; PMID:6487597 !$#accession A00617 !'##molecule_type protein !'##residues 1-379 ##label TIT REFERENCE A60477 !$#authors Bubis, J.; Vedvick, T.S.; Taylor, S.S. !$#journal J. Biol. Chem. (1987) 262:14961-14966 !$#title Antiparallel alignment of the two protomers of the !1regulatory subunit dimer of cAMP-dependent protein kinase I. !$#cross-references MUID:88033069; PMID:3667618 !$#contents interchain disulfide bonds !$#accession B60477 !'##molecule_type protein !'##residues 12-29;31-49;345-347;356-366 ##label BUB COMMENT The inactive form of the enzyme is composed of two !1regulatory chains and two catalytic chains. Activation by !1cAMP produces two active catalytic monomers and a regulatory !1dimer that binds four cAMP molecules. COMMENT Four types of regulatory chains are found: I-alpha, I-beta, !1II-alpha, and II-beta. Their expression varies among tissues !1and is in some cases constitutive and in others inducible. COMMENT Type I regulatory chains contain a high-affinity binding !1site for MgATP. COMMENT The pseudophosphorylation site binds to the !1substrate-binding region of the catalytic chain but is not !1phosphorylated. The physiological significance of !1phosphorylations by other kinases is unclear. CLASSIFICATION #superfamily cAMP-dependent protein kinase regulatory chain; !1cAMP receptor protein cyclic nucleotide-binding domain !1homology KEYWORDS acetylated amino end; ATP binding; cAMP binding; !1duplication; heterotetramer; homodimer; phosphoprotein; !1phosphotransferase FEATURE !$1-134 #domain protein interaction #label DIM\ !$94-98 #region pseudophosphorylation motif\ !$135-252 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP1\ !$253-379 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP2\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$16 #disulfide_bonds interchain (to 37) #status !8experimental\ !$37 #disulfide_bonds interchain (to 16) #status !8experimental\ !$200,209 #binding_site cAMP (Glu, Arg) #status predicted\ !$324,333 #binding_site cAMP (Glu, Arg) #status predicted SUMMARY #length 379 #molecular-weight 42761 #checksum 7140 SEQUENCE /// ENTRY OKHUR1 #type complete TITLE protein kinase (EC 2.7.1.37), cAMP-dependent, type I-beta regulatory chain - human ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS JH0392 REFERENCE JH0392 !$#authors Solberg, R.; Tasken, K.; Keiserud, A.; Jahnsen, T. !$#journal Biochem. Biophys. Res. Commun. (1991) 176:166-172 !$#title Molecular cloning, cDNA structure and tissue-specific !1expression of the human regulatory subunit RI beta of !1cAMP-dependent protein kinases. !$#cross-references MUID:91207387; PMID:1708242 !$#accession JH0392 !'##molecule_type mRNA !'##residues 1-379 ##label SOL !'##cross-references GB:M65066 COMMENT The inactive form of the enzyme is composed of two !1regulatory chains and two catalytic chains. Activation by !1cAMP produces two active catalytic monomers and a regulatory !1dimer that binds four cAMP molecules. COMMENT Four types of regulatory chains are found: I-alpha, I-beta, !1II-alpha, and II-beta. Their expression varies among tissues !1and is in some cases constitutive and in others inducible. COMMENT Type I regulatory chains contain a high-affinity binding !1site for MgATP. COMMENT Although type I regulatory chains are thought not to be !1autophosphorylated, this chain has a potential !1autophosphorylation site at residue 99. The physiological !1significance of phosphorylations by other kinases is !1unclear. GENETICS !$#gene GDB:PRKAR1B !'##cross-references GDB:127455; OMIM:176911 !$#map_position 7pter-7p22 CLASSIFICATION #superfamily cAMP-dependent protein kinase regulatory chain; !1cAMP receptor protein cyclic nucleotide-binding domain !1homology KEYWORDS acetylated amino end; ATP binding; cAMP binding; !1duplication; heterotetramer; homodimer; phosphoprotein; !1phosphotransferase FEATURE !$1-379 #product protein kinase, cAMP-dependent, type I-beta !8regulatory chain #status predicted #label MAT\ !$1-134 #domain protein interaction #label DIM\ !$135-252 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP1\ !$253-379 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP2\ !$1 #modified_site acetylated amino end (Ala) #status !8predicted\ !$17 #disulfide_bonds interchain (to 38) #status !8predicted\ !$38 #disulfide_bonds interchain (to 17) #status !8predicted\ !$200,209 #binding_site cAMP (Glu, Arg) #status predicted\ !$324,333 #binding_site cAMP (Glu, Arg) #status predicted SUMMARY #length 379 #molecular-weight 43083 #checksum 9842 SEQUENCE /// ENTRY OKMSR1 #type complete TITLE protein kinase (EC 2.7.1.37), cAMP-dependent, type I-beta regulatory chain - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS A30205 REFERENCE A30205 !$#authors Clegg, C.H.; Cadd, G.G.; McKnight, G.S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:3703-3707 !$#title Genetic characterization of a brain-specific form of the !1type I regulatory subunit of cAMP-dependent protein kinase. !$#cross-references MUID:88234494; PMID:3375237 !$#accession A30205 !'##molecule_type mRNA !'##residues 1-381 ##label CLE !'##cross-references GB:M20473; NID:g200364; PIDN:AAA39935.1; !1PID:g200365 COMMENT The inactive form of the enzyme is composed of two !1regulatory chains and two catalytic chains. Activation by !1cAMP produces two active catalytic monomers and a regulatory !1dimer that binds four cAMP molecules. COMMENT Four types of regulatory chains are found: I-alpha, I-beta, !1II-alpha, and II-beta. Their expression varies among tissues !1and is in some cases constitutive and in others inducible. COMMENT Type I regulatory chains contain a high-affinity binding !1site for MgATP. COMMENT The pseudophosphorylation site binds to the !1substrate-binding region of the catalytic chain but is not !1phosphorylated. The physiological significance of !1phosphorylations by other kinases is unclear. CLASSIFICATION #superfamily cAMP-dependent protein kinase regulatory chain; !1cAMP receptor protein cyclic nucleotide-binding domain !1homology KEYWORDS acetylated amino end; ATP binding; cAMP binding; !1duplication; heterotetramer; homodimer; phosphoprotein; !1phosphotransferase FEATURE !$2-381 #product protein kinase, cAMP-dependent, type I-beta !8regulatory chain #status predicted #label MAT\ !$2-136 #domain protein interaction #label DIM\ !$96-100 #region pseudophosphorylation motif\ !$137-254 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP1\ !$255-381 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP2\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status predicted\ !$18 #disulfide_bonds interchain (to 39) #status !8predicted\ !$39 #disulfide_bonds interchain (to 18) #status !8predicted\ !$202,211 #binding_site cAMP (Glu, Arg) #status predicted\ !$326,335 #binding_site cAMP (Glu, Arg) #status predicted SUMMARY #length 381 #molecular-weight 43224 #checksum 6372 SEQUENCE /// ENTRY A60669 #type complete TITLE protein kinase (EC 2.7.1.37), cAMP-dependent, type I-beta regulatory chain - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 28-Apr-1993 #sequence_revision 27-Jun-1994 #text_change 16-Jul-1999 ACCESSIONS A60669 REFERENCE A60669 !$#authors Massa, J.S.; Fellows, R.E.; Maurer, R.A. !$#journal Mol. Reprod. Dev. (1990) 26:129-133 !$#title Rat RIbeta isoform of type I regulatory subunit of cyclic !1adenosine monophosphate-dependent protein kinase: cDNA !1sequence analysis, mRNA tissue specificity, and rat/mouse !1difference in expression in testis. !$#cross-references MUID:90321570; PMID:2372396 !$#accession A60669 !'##molecule_type mRNA !'##residues 1-381 ##label MAS COMMENT The inactive form of the enzyme is composed of two !1regulatory chains and two catalytic chains. Activation by !1cAMP produces two active catalytic monomers and a regulatory !1dimer that binds four cAMP molecules. COMMENT Four types of regulatory chains are found: I-alpha, I-beta, !1II-alpha, and II-beta. Their expression varies among tissues !1and is in some cases constitutive and in others inducible. COMMENT Type I regulatory chains contain a high-affinity binding !1site for Mg-ATP. COMMENT The pseudophosphorylation site binds to the !1substrate-binding region of the catalytic chain but is not !1phosphorylated. The physiological significance of !1phosphorylations by other kinases is unclear. CLASSIFICATION #superfamily cAMP-dependent protein kinase regulatory chain; !1cAMP receptor protein cyclic nucleotide-binding domain !1homology KEYWORDS acetylated amino end; ATP binding; cAMP binding; !1duplication; heterotetramer; homodimer; phosphotransferase FEATURE !$2-381 #product protein kinase, cAMP-dependent, type I-beta !8regulatory chain #status predicted #label MAT\ !$2-136 #domain protein interaction #label DIM\ !$96-100 #region pseudophosphorylation motif\ !$137-254 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP1\ !$255-381 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP2\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status predicted\ !$18 #disulfide_bonds interchain (to 39) #status !8predicted\ !$39 #disulfide_bonds interchain (to 18) #status !8predicted\ !$202,211 #binding_site cAMP (Glu, Arg) #status predicted\ !$326,335 #binding_site cAMP (Glu, Arg) #status predicted SUMMARY #length 381 #molecular-weight 43282 #checksum 6234 SEQUENCE /// ENTRY OKGAR1 #type complete TITLE protein kinase (EC 2.7.1.37), cAMP-dependent, type I regulatory chain - California sea hare ORGANISM #formal_name Aplysia californica #common_name California sea hare DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS JH0590 REFERENCE JH0590 !$#authors Bergold, P.J.; Beushausen, S.A.; Sacktor, T.C.; Cheley, S.; !1Bayley, H.; Schwartz, J.H. !$#journal Neuron (1992) 8:387-397 !$#title A regulatory subunit of the cAMP-dependent protein kinase !1down-regulated in aplysia sensory neurons during long-term !1sensitization. !$#cross-references MUID:92153429; PMID:1310865 !$#accession JH0590 !'##molecule_type mRNA !'##residues 1-378 ##label BER !'##cross-references EMBL:X62382; NID:g5587; PIDN:CAA44246.1; PID:g5588 !'##note this protein is identified as the N4 isoform COMMENT The inactive form of the enzyme is composed of two !1regulatory chains and two catalytic chains. Activation by !1cAMP produces two active catalytic monomers and a regulatory !1dimer that binds four cAMP molecules. COMMENT Type I regulatory chains contain a high-affinity binding !1site for MgATP. COMMENT The pseudophosphorylation site binds to the !1substrate-binding region of the catalytic chain but is not !1phosphorylated. The physiological significance of !1phosphorylations by other kinases is unclear. CLASSIFICATION #superfamily cAMP-dependent protein kinase regulatory chain; !1cAMP receptor protein cyclic nucleotide-binding domain !1homology KEYWORDS acetylated amino end; ATP binding; cAMP binding; !1duplication; heterotetramer; homodimer; phosphoprotein; !1phosphotransferase FEATURE !$2-378 #product protein kinase, cAMP-dependent, type I-beta !8regulatory chain #status predicted #label MAT\ !$2-133 #domain protein interaction #label DIM\ !$93-97 #region pseudophosphorylation motif\ !$134-251 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP1\ !$252-378 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP2\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status predicted\ !$199,208 #binding_site cAMP (Glu, Arg) #status predicted\ !$323,332 #binding_site cAMP (Glu, Arg) #status predicted SUMMARY #length 378 #molecular-weight 42737 #checksum 2977 SEQUENCE /// ENTRY OKFF1R #type complete TITLE protein kinase (EC 2.7.1.37), cAMP-dependent, type I regulatory chain - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 21-Jul-2000 ACCESSIONS A31751; G31751; H31751 REFERENCE A31751 !$#authors Kalderon, D.; Rubin, G.M. !$#journal Genes Dev. (1988) 2:1539-1556 !$#title Isolation and characterization of Drosophila cAMP-dependent !1protein kinase genes. !$#cross-references MUID:89107990; PMID:3215511 !$#accession A31751 !'##molecule_type DNA !'##residues 1-377 ##label KAL !'##cross-references EMBL:X16970; NID:g7871; PIDN:CAA34841.1; !1PID:g1209411 !$#accession G31751 !'##molecule_type DNA !'##residues 'M',59-377 ##label KA2 !'##cross-references EMBL:X16963; NID:g7859; PIDN:CAA34837.1; !1PID:g1209410 !$#accession H31751 !'##molecule_type DNA !'##residues 81-377 ##label KA3 !'##cross-references EMBL:X16966; NID:g7818; PIDN:CAA34838.1; !1PID:g4377449 !'##note several alternatively spliced mRNA species were detected; the !1full-length messenger is expressed and translated at all !1developmental stages; the shorter mRNAs are detected in !1adults but it is not clear if they are translated COMMENT The inactive form of the enzyme is composed of two !1regulatory chains and two catalytic chains. Activation by !1cAMP produces two active catalytic monomers and a regulatory !1dimer that binds four cAMP molecules. COMMENT Type I regulatory chains contain a high-affinity binding !1site for MgATP. COMMENT The pseudophosphorylation site binds to the !1substrate-binding region of the catalytic chain but is not !1phosphorylated. The physiological significance of !1phosphorylations by other kinases is unclear. GENETICS !$#gene FlyBase:Pka-R1 !'##cross-references FlyBase:FBgn0000275 !$#map_position 77F !$#introns 58/3; 178/3; 303/3; 350/2 CLASSIFICATION #superfamily cAMP-dependent protein kinase regulatory chain; !1cAMP receptor protein cyclic nucleotide-binding domain !1homology KEYWORDS alternative splicing; ATP binding; cAMP binding; !1duplication; heterotetramer; homodimer; phosphoprotein; !1phosphotransferase FEATURE !$1-377 #product protein kinase, cAMP-dependent, type I !8regulatory chain form 1 #status predicted #label MAT\ !$1-131 #domain protein interaction #label DIM\ !$1,59-377 #product protein kinase, cAMP-dependent, type I !8regulatory chain form 2 #status predicted #label MA2\ !$81-377 #product protein kinase, cAMP-dependent, type I !8regulatory chain form 3 #status predicted #label MA3\ !$91-95 #region pseudophosphorylation motif\ !$132-249 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP1\ !$250-377 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP2\ !$17 #disulfide_bonds interchain (to 38) #status !8predicted\ !$38 #disulfide_bonds interchain (to 17) #status !8predicted\ !$197,206 #binding_site cAMP (Glu, Arg) #status predicted\ !$322,331 #binding_site cAMP (Glu, Arg) #status predicted SUMMARY #length 377 #molecular-weight 42367 #checksum 3324 SEQUENCE /// ENTRY OKKW1R #type complete TITLE protein kinase (EC 2.7.1.37), cAMP-dependent, type I regulatory chain - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS A35076 REFERENCE A35076 !$#authors Lu, X.; Gross, R.E.; Bagchi, S.; Rubin, C.S. !$#journal J. Biol. Chem. (1990) 265:3293-3303 !$#title Cloning, structure, and expression of the gene for a novel !1regulatory subunit of cAMP-dependent protein kinase in !1Caenorhabditis elegans. !$#cross-references MUID:90153982; PMID:2303451 !$#accession A35076 !'##molecule_type mRNA; DNA !'##residues 1-376 ##label LUX !'##cross-references GB:J05220; NID:g156236; PIDN:AAA27980.1; !1PID:g156237 COMMENT The inactive form of the enzyme is composed of two !1regulatory chains and two catalytic chains. Activation by !1cAMP produces two active catalytic monomers and a regulatory !1dimer that binds four cAMP molecules. COMMENT The pseudophosphorylation site binds to the !1substrate-binding region of the catalytic chain but is not !1phosphorylated. The physiological significance of !1phosphorylations by other kinases is unclear. GENETICS !$#gene kin-A !$#map_position II !$#introns 41/1; 68/3; 137/3; 175/3; 213/3; 251/3; 320/1 CLASSIFICATION #superfamily cAMP-dependent protein kinase regulatory chain; !1cAMP receptor protein cyclic nucleotide-binding domain !1homology KEYWORDS ATP binding; cAMP binding; duplication; heterotetramer; !1homodimer; phosphoprotein; phosphotransferase FEATURE !$1-131 #domain protein interaction #label DIM\ !$92-96 #region pseudophosphorylation motif\ !$132-249 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP1\ !$250-376 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP2\ !$23 #disulfide_bonds interchain (to 44) #status !8predicted\ !$44 #disulfide_bonds interchain (to 23) #status !8predicted\ !$197,206 #binding_site cAMP (Glu, Arg) #status predicted\ !$321,330 #binding_site cAMP (Glu, Arg) #status predicted SUMMARY #length 376 #molecular-weight 42649 #checksum 6750 SEQUENCE /// ENTRY OKHU2R #type complete TITLE protein kinase (EC 2.7.1.37), cAMP-dependent, type II-alpha regulatory chain - human ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 04-Feb-2000 ACCESSIONS S03885 REFERENCE S03885 !$#authors Oeyen, O.; Myklebust, F.; Scott, J.D.; Hansson, V.; Jahnsen, !1T. !$#journal FEBS Lett. (1989) 246:57-64 !$#title Human testis cDNA for the regulatory subunit RII-alpha of !1cAMP-dependent protein kinase encodes an alternate !1amino-terminal region. !$#cross-references MUID:89211413; PMID:2540040 !$#accession S03885 !'##molecule_type mRNA !'##residues 1-404 ##label OYE !'##cross-references EMBL:X14968; NID:g29647; PIDN:CAA33094.1; !1PID:g29648 COMMENT The inactive form of the enzyme is composed of two !1regulatory chains and two catalytic chains. Activation by !1cAMP produces two active catalytic monomers and a regulatory !1dimer that binds four cAMP molecules. COMMENT Four types of regulatory chains are found: I-alpha, I-beta, !1II-alpha, and II-beta. Their expression varies among tissues !1and is in some cases constitutive and in others inducible. COMMENT Type II regulatory chains are phosphorylated by the !1activated catalytic chain. The physiological significance of !1phosphorylations by other kinases is unclear. COMMENT Type II regulatory chains mediate membrane association by !1binding to anchoring proteins, including the MAP2 kinase. !1The amino-terminal 50 residues are essential for this !1binding and for dimerization. GENETICS !$#gene GDB:PRKAR2A !'##cross-references GDB:120314; OMIM:176910 !$#map_position 7pter-7p22 CLASSIFICATION #superfamily cAMP-dependent protein kinase regulatory chain; !1cAMP receptor protein cyclic nucleotide-binding domain !1homology KEYWORDS acetylated amino end; autophosphorylation; cAMP binding; !1duplication; heterotetramer; homodimer; phosphoprotein; !1phosphotransferase FEATURE !$2-404 #product protein kinase, cAMP-dependent, type !8II-alpha regulatory chain #status predicted #label !8MAT\ !$2-138 #domain protein interaction #label DIM\ !$139-260 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP1\ !$261-393 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP2\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status predicted\ !$99 #binding_site phosphate (Ser) (covalent) (by !8autophosphorylation) #status predicted\ !$208,217 #binding_site cAMP (Glu, Arg) #status predicted\ !$338,347 #binding_site cAMP (Glu, Arg) #status predicted SUMMARY #length 404 #molecular-weight 45518 #checksum 9820 SEQUENCE /// ENTRY OKBO2R #type complete TITLE protein kinase (EC 2.7.1.37), cAMP-dependent, type II-alpha regulatory chain - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 15-Oct-1982 #sequence_revision 15-Oct-1982 #text_change 04-Feb-2000 ACCESSIONS A00618; S17058 REFERENCE A00618 !$#authors Takio, K.; Smith, S.B.; Krebs, E.G.; Walsh, K.A.; Titani, K. !$#journal Biochemistry (1984) 23:4200-4206 !$#title Amino acid sequence of the regulatory subunit of bovine type !1II adenosine cyclic 3',5'-phosphate dependent protein !1kinase. !$#cross-references MUID:85023306; PMID:6386045 !$#accession A00618 !'##molecule_type protein !'##residues 1-400 ##label TAK REFERENCE S17058 !$#authors Braun, R.K.; Vulliet, P.R.; Carbonaro-Hall, D.A.; Hall, F.L. !$#journal Arch. Biochem. Biophys. (1991) 289:187-191 !$#title Phosphorylation of RII subunit and attenuation of !1cAMP-dependent protein kinase activity by proline-directed !1protein kinase. !$#cross-references MUID:91378531; PMID:1654846 !$#accession S17058 !'##molecule_type protein !'##residues 155-166 ##label BRA COMMENT The inactive form of the enzyme is composed of two !1regulatory chains and two catalytic chains. Activation by !1cAMP produces two active catalytic monomers and a regulatory !1dimer that binds four cAMP molecules. COMMENT Four types of regulatory chains are found: I-alpha, I-beta, !1II-alpha, and II-beta. Their expression varies among tissues !1and is in some cases constitutive and in others inducible. COMMENT Type II regulatory chains are phosphorylated by the !1activated catalytic chain. The physiological significance of !1phosphorylations by other kinases is unclear. COMMENT Type II regulatory chains mediate membrane association by !1binding to anchoring proteins, including the MAP2 kinase. !1The amino-terminal 50 residues are essential for this !1binding and for dimerization. CLASSIFICATION #superfamily cAMP-dependent protein kinase regulatory chain; !1cAMP receptor protein cyclic nucleotide-binding domain !1homology KEYWORDS acetylated amino end; autophosphorylation; cAMP binding; !1duplication; heterotetramer; homodimer; phosphoprotein; !1phosphotransferase FEATURE !$1-134 #domain protein interaction #label DIM\ !$135-256 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP1\ !$257-389 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP2\ !$1 #modified_site acetylated amino end (Ser) #status !8experimental\ !$48,211 #binding_site phosphate (Thr) (covalent) (by !8proline-directed kinase) #status predicted\ !$95 #binding_site phosphate (Ser) (covalent) (by !8autophosphorylation) #status experimental\ !$204,213 #binding_site cAMP (Glu, Arg) #status predicted\ !$334,343 #binding_site cAMP (Glu, Arg) #status predicted SUMMARY #length 400 #molecular-weight 44962 #checksum 8889 SEQUENCE /// ENTRY OKMS2R #type complete TITLE protein kinase (EC 2.7.1.37), cAMP-dependent, type II-alpha regulatory chain - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 04-Feb-2000 ACCESSIONS B28325 REFERENCE A94172 !$#authors Scott, J.D.; Glaccum, M.B.; Zoller, M.J.; Uhler, M.D.; !1Helfman, D.M.; McKnight, G.S.; Krebs, E.G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:5192-5196 !$#title The molecular cloning of a type II regulatory subunit of the !1cAMP-dependent protein kinase from rat skeletal muscle and !1mouse brain. !$#cross-references MUID:87260955; PMID:3037538 !$#accession B28325 !'##molecule_type mRNA !'##residues 1-401 ##label SCO !'##cross-references GB:J02935; NID:g200356; PIDN:AAA39932.1; !1PID:g387511 COMMENT The inactive form of the enzyme is composed of two !1regulatory chains and two catalytic chains. Activation by !1cAMP produces two active catalytic monomers and a regulatory !1dimer that binds four cAMP molecules. COMMENT Four types of regulatory chains are found: I-alpha, I-beta, !1II-alpha, and II-beta. Their expression varies among tissues !1and is in some cases constitutive and in others inducible. COMMENT Type II regulatory chains are phosphorylated by the !1activated catalytic chain. The physiological significance of !1phosphorylations by other kinases is unclear. COMMENT Type II regulatory chains mediate membrane association by !1binding to anchoring proteins, including the MAP2 kinase. !1The amino-terminal 50 residues are essential for this !1binding and for dimerization. CLASSIFICATION #superfamily cAMP-dependent protein kinase regulatory chain; !1cAMP receptor protein cyclic nucleotide-binding domain !1homology KEYWORDS acetylated amino end; autophosphorylation; cAMP binding; !1duplication; heterotetramer; homodimer; phosphoprotein; !1phosphotransferase FEATURE !$2-401 #product protein kinase, cAMP-dependent, type !8II-alpha regulatory chain #status predicted #label !8MAT\ !$2-135 #domain protein interaction #label DIM\ !$136-257 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP1\ !$258-390 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP2\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status predicted\ !$96 #binding_site phosphate (Ser) (covalent) (by !8autophosphorylation) #status predicted\ !$205,214 #binding_site cAMP (Glu, Arg) #status predicted\ !$335,344 #binding_site cAMP (Glu, Arg) #status predicted SUMMARY #length 401 #molecular-weight 45389 #checksum 6954 SEQUENCE /// ENTRY OKRT2R #type fragment TITLE protein kinase (EC 2.7.1.37), cAMP-dependent, type II-alpha regulatory chain - rat (fragment) ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 04-Feb-2000 ACCESSIONS A28325 REFERENCE A94172 !$#authors Scott, J.D.; Glaccum, M.B.; Zoller, M.J.; Uhler, M.D.; !1Helfman, D.M.; McKnight, G.S.; Krebs, E.G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:5192-5196 !$#title The molecular cloning of a type II regulatory subunit of the !1cAMP-dependent protein kinase from rat skeletal muscle and !1mouse brain. !$#cross-references MUID:87260955; PMID:3037538 !$#accession A28325 !'##molecule_type mRNA !'##residues 1-370 ##label SCO !'##cross-references GB:J02934; NID:g206149; PIDN:AAA41856.1; !1PID:g206150 COMMENT The inactive form of the enzyme is composed of two !1regulatory chains and two catalytic chains. Activation by !1cAMP produces two active catalytic monomers and a regulatory !1dimer that binds four cAMP molecules. COMMENT Four types of regulatory chains are found: I-alpha, I-beta, !1II-alpha, and II-beta. Their expression varies among tissues !1and is in some cases constitutive and in others inducible. COMMENT Type II regulatory chains are phosphorylated by the !1activated catalytic chain. The physiological significance of !1phosphorylations by other kinases is unclear. COMMENT Type II regulatory chains mediate membrane association by !1binding to anchoring proteins, including the MAP2 kinase. !1The amino-terminal 50 residues are essential for this !1binding and for dimerization. CLASSIFICATION #superfamily cAMP-dependent protein kinase regulatory chain; !1cAMP receptor protein cyclic nucleotide-binding domain !1homology KEYWORDS autophosphorylation; cAMP binding; duplication; !1heterotetramer; homodimer; phosphoprotein; !1phosphotransferase FEATURE !$105-226 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP1\ !$227-359 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP2\ !$66 #binding_site phosphate (Ser) (covalent) (by !8autophosphorylation) #status predicted\ !$174,183 #binding_site cAMP (Glu, Arg) #status predicted\ !$304,313 #binding_site cAMP (Glu, Arg) #status predicted SUMMARY #length 370 #checksum 3511 SEQUENCE /// ENTRY OKHUR2 #type complete TITLE protein kinase (EC 2.7.1.37), cAMP-dependent, type II-beta regulatory chain - human ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 04-Feb-2000 ACCESSIONS A40915 REFERENCE A40915 !$#authors Levy, F.O.; Oeyen, O.; Sandberg, M.; Tasken, K.; Eskild, W.; !1Hansson, V.; Jahnsen, T. !$#journal Mol. Endocrinol. (1988) 2:1364-1373 !$#title Molecular cloning, complementary deoxyribonucleic acid !1structure and predicted full-length amino acid sequence of !1the hormone-inducible regulatory subunit of 3'-5'-cyclic !1adenosine monophosphate-dependent protein kinase from human !1testis. !$#cross-references MUID:89112218; PMID:2851102 !$#accession A40915 !'##molecule_type mRNA !'##residues 1-418 ##label LEV !'##cross-references GB:M31158; NID:g189980; PIDN:AAA60099.1; !1PID:g189981 COMMENT The inactive form of the enzyme is composed of two !1regulatory chains and two catalytic chains. Activation by !1cAMP produces two active catalytic monomers and a regulatory !1dimer that binds four cAMP molecules. COMMENT Four types of regulatory chains are found: I-alpha, I-beta, !1II-alpha, and II-beta. Their expression varies among tissues !1and is in some cases constitutive and in others inducible. COMMENT Type II regulatory chains are phosphorylated by the !1activated catalytic chain. The physiological significance of !1phosphorylations by other kinases is unclear. COMMENT Type II regulatory chains mediate membrane association by !1binding to anchoring proteins, including the MAP2 kinase. !1The amino-terminal 50 residues are essential for this !1binding and for dimerization. GENETICS !$#gene GDB:PRKAR2B !'##cross-references GDB:127902; OMIM:176912 !$#map_position 7q22-7q22 CLASSIFICATION #superfamily cAMP-dependent protein kinase regulatory chain; !1cAMP receptor protein cyclic nucleotide-binding domain !1homology KEYWORDS acetylated amino end; autophosphorylation; cAMP binding; !1duplication; heterotetramer; homodimer; phosphoprotein; !1phosphotransferase FEATURE !$2-418 #product protein kinase, cAMP-dependent, type II-beta !8regulatory chain #status predicted #label MAT\ !$2-153 #domain protein interaction #label DIM\ !$154-275 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP1\ !$276-407 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP2\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status predicted\ !$114 #binding_site phosphate (Ser) (covalent) (by !8autophosphorylation) #status predicted\ !$223,232 #binding_site cAMP (Glu, Arg) #status predicted\ !$352,361 #binding_site cAMP (Glu, Arg) #status predicted SUMMARY #length 418 #molecular-weight 46346 #checksum 4346 SEQUENCE /// ENTRY OKRTR2 #type complete TITLE protein kinase (EC 2.7.1.37), cAMP-dependent, type II-beta regulatory chain - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 04-Feb-2000 ACCESSIONS A28893; A25201 REFERENCE A28893 !$#authors Sandberg, M.; Levy, F.O.; Oeyen, O.; Hansson, V.; Jahnsen, !1T. !$#journal Biochem. Biophys. Res. Commun. (1988) 154:705-711 !$#title Molecular cloning, cDNA structure and deduced amino acid !1sequence for the hormone-induced regulatory subunit !1(RII-beta) of cAMP-dependent protein kinase from rat ovarian !1granulosa cells. !$#cross-references MUID:88293504; PMID:3401231 !$#accession A28893 !'##molecule_type mRNA !'##residues 1-415 ##label SAN !'##cross-references GB:M12492; GB:M21194; NID:g206670; PIDN:AAA42047.1; !1PID:g206671 REFERENCE A25201 !$#authors Jahnsen, T.; Hedin, L.; Kidd, V.J.; Beattie, W.G.; Lohmann, !1S.M.; Walter, U.; Durica, J.; Schulz, T.Z.; Schiltz, E.; !1Browner, M.; Lawrence, C.B.; Goldman, D.; Ratoosh, S.L.; !1Richards, J.S. !$#journal J. Biol. Chem. (1986) 261:12352-12361 !$#title Molecular cloning, cDNA structure, and regulation of the !1regulatory subunit of type II cAMP-dependent protein kinase !1from rat ovarian granulosa cells. !$#cross-references MUID:86304397; PMID:2427518 !$#accession A25201 !'##molecule_type mRNA !'##residues 15-49,'SAMRAGPG',58,'TR',62,'QPR',66,'R',68-415 ##label JAH !'##cross-references GB:M12492 !'##note this sequence has been revised in reference A28893 COMMENT The inactive form of the enzyme is composed of two !1regulatory chains and two catalytic chains. Activation by !1cAMP produces two active catalytic monomers and a regulatory !1dimer that binds four cAMP molecules. COMMENT Four types of regulatory chains are found: I-alpha, I-beta, !1II-alpha, and II-beta. Their expression varies among tissues !1and is in some cases constitutive and in others inducible. COMMENT Type II regulatory chains are phosphorylated by the !1activated catalytic chain. The physiological significance of !1phosphorylations by other kinases is unclear. COMMENT Type II regulatory chains mediate membrane association by !1binding to anchoring proteins, including the MAP2 kinase. !1The amino-terminal 50 residues are essential for this !1binding and for dimerization. CLASSIFICATION #superfamily cAMP-dependent protein kinase regulatory chain; !1cAMP receptor protein cyclic nucleotide-binding domain !1homology KEYWORDS acetylated amino end; autophosphorylation; cAMP binding; !1duplication; heterotetramer; homodimer; phosphoprotein; !1phosphotransferase FEATURE !$1-415 #product protein kinase, cAMP-dependent, type II-beta !8regulatory chain #status predicted #label MAT\ !$1-150 #domain protein interaction #label DIM\ !$151-272 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP1\ !$273-404 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP2\ !$1 #modified_site acetylated amino end (Ser) #status !8predicted\ !$111 #binding_site phosphate (Ser) (covalent) (by !8autophosphorylation) #status predicted\ !$220,229 #binding_site cAMP (Glu, Arg) #status predicted\ !$349,358 #binding_site cAMP (Glu, Arg) #status predicted SUMMARY #length 415 #molecular-weight 45991 #checksum 353 SEQUENCE /// ENTRY OKBOR2 #type complete TITLE protein kinase (EC 2.7.1.37), cAMP-dependent, type II-beta regulatory chain - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 04-Feb-2000 ACCESSIONS A36528 REFERENCE A36528 !$#authors Luo, Z.; Shafit-Zagardo, B.; Erlichman, J. !$#journal J. Biol. Chem. (1990) 265:21804-21810 !$#title Identification of the MAP2- and P75-binding domain in the !1regulatory subunit (RIIbeta) of type II cAMP-dependent !1protein kinase. Cloning and expression of the cDNA for !1bovine brain RIIbeta. !$#cross-references MUID:91072385; PMID:2254332 !$#accession A36528 !'##molecule_type mRNA !'##residues 1-418 ##label LUO !'##cross-references GB:J05692; NID:g163669; PIDN:AAA30755.1; !1PID:g163670 COMMENT The inactive form of the enzyme is composed of two !1regulatory chains and two catalytic chains. Activation by !1cAMP produces two active catalytic monomers and a regulatory !1dimer that binds four cAMP molecules. COMMENT Four types of regulatory chains are found: I-alpha, I-beta, !1II-alpha, and II-beta. Their expression varies among tissues !1and is in some cases constitutive and in others inducible. COMMENT Type II regulatory chains are phosphorylated by the !1activated catalytic chain. The physiological significance of !1phosphorylations by other kinases is unclear. COMMENT Type II regulatory chains mediate membrane association by !1binding to anchoring proteins, including the MAP2 kinase. !1The amino-terminal 50 residues are essential for this !1binding and for dimerization. CLASSIFICATION #superfamily cAMP-dependent protein kinase regulatory chain; !1cAMP receptor protein cyclic nucleotide-binding domain !1homology KEYWORDS acetylated amino end; autophosphorylation; cAMP binding; !1duplication; heterotetramer; homodimer; phosphoprotein; !1phosphotransferase FEATURE !$2-418 #product protein kinase, cAMP-dependent, type II-beta !8regulatory chain #status predicted #label MAT\ !$2-153 #domain protein interaction #label DIM\ !$154-275 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP1\ !$276-407 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP2\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status predicted\ !$114 #binding_site phosphate (Ser) (covalent) (by !8autophosphorylation) #status predicted\ !$223,232 #binding_site cAMP (Glu, Arg) #status predicted\ !$352,361 #binding_site cAMP (Glu, Arg) #status predicted SUMMARY #length 418 #molecular-weight 46336 #checksum 3566 SEQUENCE /// ENTRY OKBYRC #type complete TITLE protein kinase (EC 2.7.1.37), cAMP-dependent, regulatory chain - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES cyclic AMP-dependent protein kinase regulatory chain; protein YI9905.15c; protein YIL033c ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 21-Jul-2000 ACCESSIONS A25868; A27202; A26911; S49945 REFERENCE A25868 !$#authors Kunisawa, R.; Davis, T.N.; Urdea, M.S.; Thorner, J. !$#journal Nucleic Acids Res. (1987) 15:368-369 !$#title Complete nucleotide sequence of the gene encoding the !1regulatory subunit of 3',5'-cyclic AMP-dependent protein !1kinase from the yeast Saccharomyces cerevisiae. !$#cross-references MUID:87146350; PMID:3547325 !$#accession A25868 !'##molecule_type DNA !'##residues 1-416 ##label KUN !'##cross-references GB:X05051 REFERENCE A27202 !$#authors Toda, T.; Cameron, S.; Sass, P.; Zoller, M.; Scott, J.D.; !1McMullen, B.; Hurwitz, M.; Krebs, E.G.; Wigler, M. !$#journal Mol. Cell. Biol. (1987) 7:1371-1377 !$#title Cloning and characterization of BCY1, a locus encoding a !1regulatory subunit of the cyclic AMP-dependent protein !1kinase in Saccharomyces cerevisiae. !$#cross-references MUID:87257825; PMID:3037314 !$#accession A27202 !'##molecule_type DNA !'##residues 1-416 ##label TOD !'##cross-references EMBL:M15756; NID:g171158; PIDN:AAA34468.1; !1PID:g171159 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE A93094 !$#authors Cannon, J.F.; Tatchell, K. !$#journal Mol. Cell. Biol. (1987) 7:2653-2663 !$#title Characterization of Saccharomyces cerevisiae genes encoding !1subunits of cyclic AMP-dependent protein kinase. !$#cross-references MUID:88038803; PMID:2823100 !$#accession A26911 !'##molecule_type DNA !'##residues 1-416 ##label CAN !'##cross-references GB:M17223; NID:g172688; PIDN:AAA66934.1; !1PID:g172689 REFERENCE S49931 !$#authors Odell, C.; Bowman, S. !$#submission submitted to the EMBL Data Library, December 1994 !$#accession S49945 !'##molecule_type DNA !'##residues 1-416 ##label ODE !'##cross-references GB:Z47047; EMBL:Z46861; NID:g603997; PID:g763313; !1GSPDB:GN00009; MIPS:YIL033c GENETICS !$#gene SGD:SRA1; REG1; BCY1; MIPS:YIL033c !'##cross-references SGD:S0001295; MIPS:YIL033c !$#map_position 9L CLASSIFICATION #superfamily cAMP-dependent protein kinase regulatory chain; !1cAMP receptor protein cyclic nucleotide-binding domain !1homology KEYWORDS autophosphorylation; cAMP binding; duplication; !1phosphoprotein; phosphotransferase FEATURE !$2-416 #product protein kinase, cAMP-dependent, regulatory !8chain #status experimental #label MAT\ !$2-183 #domain protein interaction #label DIM\ !$184-301 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP1\ !$302-416 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP2\ !$145 #binding_site phosphate (Ser) (covalent) (by !8autophosphorylation) #status experimental\ !$249,258 #binding_site cAMP (Glu, Arg) #status predicted\ !$368,377 #binding_site cAMP (Glu, Arg) #status predicted SUMMARY #length 416 #molecular-weight 47219 #checksum 4482 SEQUENCE /// ENTRY A43435 #type complete TITLE protein kinase (EC 2.7.1.37), cAMP-dependent, type II regulatory chain - fungus (Blastocladiella emersonii) ORGANISM #formal_name Blastocladiella emersonii DATE 04-Mar-1993 #sequence_revision 28-Jul-1995 #text_change 04-Feb-2000 ACCESSIONS A43435; B43435 REFERENCE A43435 !$#authors Marques, M.V.; Gomes, S.L. !$#journal J. Biol. Chem. (1992) 267:17201-17207 !$#title Cloning and structural analysis of the gene for the !1regulatory subunit of cAMP-dependent protein kinase in !1Blastocladiella emersonii. !$#cross-references MUID:92381035; PMID:1512258 !$#accession A43435 !'##molecule_type mRNA !'##residues 1-403 ##label MAR !'##cross-references GB:M81714; NID:g167191; PIDN:AAA33016.1; !1PID:g167192 !'##note sequence extracted from NCBI backbone (NCBIN:111926, !1NCBIP:111927) !$#accession B43435 !'##molecule_type DNA !'##residues 1-371,'T',373-403 ##label MA2 !'##cross-references GB:M81713; NID:g167189; PIDN:AAA33015.1; !1PID:g167190 COMMENT Type II regulatory chains are phosphorylated by the !1activated catalytic chain. The physiological significance of !1phosphorylations by other kinases is unclear. COMMENT Type II regulatory chains mediate membrane association by !1binding to anchoring proteins, including the MAP2 kinase. !1The amino-terminal 50 residues are essential for this !1binding and for dimerization. GENETICS !$#introns 52/1 COMPLEX The inactive form of the enzyme is composed of two !1regulatory chains and two catalytic chains. Activation by !1cAMP produces two active catalytic monomers and a regulatory !1dimer that binds four cAMP molecules. CLASSIFICATION #superfamily cAMP-dependent protein kinase regulatory chain; !1cAMP receptor protein cyclic nucleotide-binding domain !1homology KEYWORDS autophosphorylation; cAMP binding; duplication; !1heterotetramer; homodimer; phosphoprotein; !1phosphotransferase FEATURE !$2-403 #product protein kinase, cAMP-dependent, type II !8regulatory chain #status predicted #label MAT\ !$2-155 #domain protein interaction #label DIM\ !$156-278 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP1\ !$279-403 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP2\ !$117 #binding_site phosphate (Ser) (covalent) (by !8autophosphorylation) #status predicted\ !$226,235 #binding_site cAMP (Glu, Arg) #status predicted\ !$349,358 #binding_site cAMP (Glu, Arg) #status predicted SUMMARY #length 403 #molecular-weight 44467 #checksum 2703 SEQUENCE /// ENTRY OKDDRC #type complete TITLE protein kinase (EC 2.7.1.37), cAMP-dependent, regulatory chain - slime mold (Dictyostelium discoideum) ORGANISM #formal_name Dictyostelium discoideum DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS A29076 REFERENCE A29076 !$#authors Mutzel, R.; Lacombe, M.L.; Simon, M.N.; de Gunzburg, J.; !1Veron, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:6-10 !$#title Cloning and cDNA sequence of the regulatory subunit of !1cAMP-dependent protein kinase from Dictyostelium discoideum. !$#cross-references MUID:87092396; PMID:3467359 !$#accession A29076 !'##molecule_type mRNA !'##residues 1-327 ##label MUT !'##cross-references GB:M15081; NID:g167848; PIDN:AAA33236.1; !1PID:g167849 COMMENT The inactive form of the enzyme is a dimer of a regulatory !1chain and a catalytic chain, which dissociates upon !1activation by cAMP. COMMENT This regulatory chain binds only one molecule of cAMP with !1high affinity; the second potential binding site may bind !1cAMP with low affinity. COMMENT The pseudophosphorylation site binds to the !1substrate-binding region of the catalytic chain but is not !1phosphorylated. The physiological significance of !1phosphorylations by other kinases is unclear. CLASSIFICATION #superfamily cAMP-dependent protein kinase regulatory chain; !1cAMP receptor protein cyclic nucleotide-binding domain !1homology KEYWORDS cAMP binding; duplication; heterodimer; phosphoprotein; !1phosphotransferase FEATURE !$1-65 #domain protein interaction #label DIM\ !$27-31 #region pseudophosphorylation motif\ !$66-188 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP1\ !$189-317 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP2\ !$136,145 #binding_site cAMP (Glu, Arg) #status predicted\ !$262,271 #binding_site cAMP (Glu, Arg) #status predicted SUMMARY #length 327 #molecular-weight 36835 #checksum 2133 SEQUENCE /// ENTRY JC4602 #type complete TITLE protein kinase (EC 2.7.1.37) A - Bacillus subtilis ALTERNATE_NAMES PrKA protein; serine protein kinase prkA; serine/threonine protein kinase A ORGANISM #formal_name Bacillus subtilis DATE 10-Apr-1996 #sequence_revision 02-Jul-1996 #text_change 16-Jun-2000 ACCESSIONS JC4602; B69682; S45045 REFERENCE JC4602 !$#authors Fischer, C.; Geourjon, C.; Bourson, C.; Deutscher, J. !$#journal Gene (1996) 168:55-60 !$#title Cloning and characterization of the Bacillus subtilis prkA !1gene encoding a novel serine protein kinase. !$#cross-references MUID:96186955; PMID:8626065 !$#accession JC4602 !'##molecule_type DNA !'##residues 1-631 ##label FIS !'##cross-references EMBL:X79388; NID:g872031; PIDN:CAA55933.1; !1PID:g494961 !'##experimental_source strain 168 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69682 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-631 ##label KUN !'##cross-references GB:Z99108; GB:AL009126; NID:g2633055; !1PIDN:CAB12725.1; PID:g2633220 !'##experimental_source strain 168 COMMENT This enzyme phosphorylates a 60-kDa protein at a serine !1residue. GENETICS !$#gene prkA !$#map_position 169 degrees CLASSIFICATION #superfamily Bacillus protein kinase A KEYWORDS nucleotide binding; P-loop; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$102-109 #region nucleotide-binding motif A (P-loop)\ !$134 #active_site Lys #status predicted SUMMARY #length 631 #molecular-weight 72887 #checksum 3767 SEQUENCE /// ENTRY KIHUCA #type complete TITLE protein kinase C (EC 2.7.1.-) alpha - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 11-Jun-1999 ACCESSIONS S09496 REFERENCE S09496 !$#authors Finkenzeller, G.; Marme, D.; Hug, H. !$#journal Nucleic Acids Res. (1990) 18:2183 !$#title Sequence of human protein kinase C alpha. !$#cross-references MUID:90245676; PMID:2336401 !$#accession S09496 !'##molecule_type mRNA !'##residues 1-672 ##label FIN !'##cross-references EMBL:X52479; NID:g35482; PIDN:CAA36718.1; !1PID:g35483 COMMENT This is a calcium-activated, phospholipid-dependent, serine- !1and threonine-specific enzyme. It is activated by !1diacylglycerol produced in the cell membrane during !1signal-induced turnover of inositol phospholipids. This !1protein is a receptor for tumor-promoting phorbol esters, !1which can substitute for diacylglycerol in activating the !1enzyme. COMMENT Binding to acidic phospholipids (phosphatidylserine) in the !1cell membrane may occur at multiple sites, including near !1the pseudosubstrate-binding region and within the C2 domain. COMMENT The zinc-stabilized regions bind diacylglycerol and phorbol !1esters. GENETICS !$#gene GDB:PRKCA !'##cross-references GDB:128015; OMIM:176960 !$#map_position 17q22-17q23.2 CLASSIFICATION #superfamily protein kinase C alpha; protein kinase C C2 !1region homology; protein kinase C zinc-binding repeat !1homology; protein kinase homology KEYWORDS ATP; autophosphorylation; calcium binding; duplication; !1phorbol ester binding; phospholipid binding; phosphoprotein; !1phosphotransferase; serine/threonine-specific protein !1kinase; zinc FEATURE !$19-29 #region phospholipid binding #status experimental\ !$22-27 #region pseudophosphorylation motif\ !$37-86 #domain protein kinase C zinc-binding repeat homology !8#label KZ1\ !$102-151 #domain protein kinase C zinc-binding repeat homology !8#label KZ2\ !$152-264 #domain protein kinase C C2 region homology #label !8KC2\ !$337-597 #domain protein kinase homology #label KIN\ !$345-353 #region protein kinase ATP-binding motif\ !$37,67,70,86 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$50,53,75,78 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$102,132,135,151 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$115,118,140,143 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$368 #active_site Lys #status predicted\ !$631,638 #binding_site phosphate (Thr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 672 #molecular-weight 76763 #checksum 5347 SEQUENCE /// ENTRY KIRTC #type complete TITLE protein kinase C (EC 2.7.1.-) alpha - rat ALTERNATE_NAMES protein kinase C type III ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 11-Jun-1999 ACCESSIONS S02248; S02620 REFERENCE S02129 !$#authors Ono, Y.; Fujii, T.; Igarashi, K.; Kikkawa, U.; Ogita, K.; !1Nishizuka, Y. !$#journal Nucleic Acids Res. (1988) 16:5199-5200 !$#title Nucleotide sequences of cDNAs for alpha and gamma subspecies !1of rat brain protein kinase C. !$#cross-references MUID:88262515; PMID:3387228 !$#accession S02248 !'##molecule_type mRNA !'##residues 1-672 ##label ONO !'##cross-references EMBL:X07286; NID:g56913; PIDN:CAA30266.1; !1PID:g56914 COMMENT This is a calcium-activated, phospholipid-dependent, serine- !1and threonine-specific enzyme. It is activated by !1diacylglycerol produced in the cell membrane during !1signal-induced turnover of inositol phospholipids. This !1protein is a receptor for tumor-promoting phorbol esters, !1which can substitute for diacylglycerol in activating the !1enzyme. COMMENT Binding to acidic phospholipids (phosphatidylserine) in the !1cell membrane may occur at multiple sites, including near !1the pseudosubstrate-binding region and within the C2 domain. COMMENT The zinc-stabilized regions bind diacylglycerol and phorbol !1esters. CLASSIFICATION #superfamily protein kinase C alpha; protein kinase C C2 !1region homology; protein kinase C zinc-binding repeat !1homology; protein kinase homology KEYWORDS ATP; autophosphorylation; calcium binding; duplication; !1phorbol ester binding; phospholipid binding; phosphoprotein; !1phosphotransferase; serine/threonine-specific protein !1kinase; zinc FEATURE !$19-29 #region phospholipid binding #status experimental\ !$22-27 #region pseudophosphorylation motif\ !$37-86 #domain protein kinase C zinc-binding repeat homology !8#label KZ1\ !$102-151 #domain protein kinase C zinc-binding repeat homology !8#label KZ2\ !$152-264 #domain protein kinase C C2 region homology #label !8KC2\ !$337-597 #domain protein kinase homology #label KIN\ !$345-353 #region protein kinase ATP-binding motif\ !$368 #active_site Lys #status predicted\ !$631,638 #binding_site phosphate (Thr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 672 #molecular-weight 76791 #checksum 6571 SEQUENCE /// ENTRY KIMSCA #type complete TITLE protein kinase C (EC 2.7.1.-) alpha - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 11-Jun-1999 ACCESSIONS S07104; JS0078 REFERENCE S07104 !$#authors Megidish, T.; Mazurek, N. !$#journal Nature (1989) 342:807-811 !$#title A mutant protein kinase C that can transform fibroblasts. !$#cross-references MUID:90098082; PMID:2601739 !$#accession S07104 !'##molecule_type mRNA !'##residues 1-672 ##label MEG !'##cross-references GB:X52685; GB:X51603; NID:g49938; PIDN:CAA36908.1; !1PID:g49939 !'##experimental_source strain Balb/c REFERENCE JS0078 !$#authors Rose-John, S.; Dietrich, A.; Marks, F. !$#journal Gene (1988) 74:465-471 !$#title Molecular cloning of mouse protein kinase C (PKC) cDNA from !1Swiss 3T3 fibroblasts. !$#cross-references MUID:89232737; PMID:2469625 !$#accession JS0078 !'##molecule_type mRNA !'##residues 1-146,'D',148-217,'N',219-276,'AH',279-312,'V',314-466,'N', !1468-471,'N',473-575,'Q',577-672 ##label ROS !'##cross-references GB:M25811 !'##note the authors translated the codon AAC for residue 141 as Lys; !1the sequence shown follows the authors' translation COMMENT This is a calcium-activated, phospholipid-dependent, serine- !1and threonine-specific enzyme. It is activated by !1diacylglycerol produced in the cell membrane during !1signal-induced turnover of inositol phospholipids. This !1protein is a receptor for tumor-promoting phorbol esters, !1which can substitute for diacylglycerol in activating the !1enzyme. COMMENT Binding to acidic phospholipids (phosphatidylserine) in the !1cell membrane may occur at multiple sites, including near !1the pseudosubstrate-binding region and within the C2 domain. COMMENT The zinc-stabilized regions bind diacylglycerol and phorbol !1esters. CLASSIFICATION #superfamily protein kinase C alpha; protein kinase C C2 !1region homology; protein kinase C zinc-binding repeat !1homology; protein kinase homology KEYWORDS ATP; autophosphorylation; calcium binding; duplication; !1phorbol ester binding; phospholipid binding; phosphoprotein; !1phosphotransferase; serine/threonine-specific protein !1kinase; zinc FEATURE !$19-29 #region phospholipid binding #status experimental\ !$22-27 #region pseudophosphorylation motif\ !$37-86 #domain protein kinase C zinc-binding repeat homology !8#label KZ1\ !$102-151 #domain protein kinase C zinc-binding repeat homology !8#label KZ2\ !$152-264 #domain protein kinase C C2 region homology #label !8KC2\ !$337-597 #domain protein kinase homology #label KIN\ !$345-353 #region protein kinase ATP-binding motif\ !$37,67,70,86 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$50,53,75,78 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$102,132,135,151 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$115,118,140,143 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$368 #active_site Lys #status predicted\ !$631,638 #binding_site phosphate (Thr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 672 #molecular-weight 76824 #checksum 6445 SEQUENCE /// ENTRY KIRBC #type complete TITLE protein kinase C (EC 2.7.1.-) alpha - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 11-Jun-1999 ACCESSIONS C26037 REFERENCE A26037 !$#authors Ohno, S.; Kawasaki, H.; Imajoh, S.; Suzuki, K.; Inagaki, M.; !1Yokokura, H.; Sakoh, T.; Hidaka, H. !$#journal Nature (1987) 325:161-166 !$#title Tissue-specific expression of three distinct types of rabbit !1protein kinase C. !$#cross-references MUID:87115883; PMID:3808073 !$#accession C26037 !'##molecule_type mRNA !'##residues 1-672 ##label OHN !'##cross-references EMBL:X04796; NID:g1672; PIDN:CAA28483.1; PID:g1673 COMMENT This is a calcium-activated, phospholipid-dependent, serine- !1and threonine-specific enzyme. It is activated by !1diacylglycerol produced in the cell membrane during !1signal-induced turnover of inositol phospholipids. This !1protein is a receptor for tumor-promoting phorbol esters, !1which can substitute for diacylglycerol in activating the !1enzyme. COMMENT Binding to acidic phospholipids (phosphatidylserine) in the !1cell membrane may occur at multiple sites, including near !1the pseudosubstrate-binding region and within the C2 domain. COMMENT The zinc-stabilized regions bind diacylglycerol and phorbol !1esters. CLASSIFICATION #superfamily protein kinase C alpha; protein kinase C C2 !1region homology; protein kinase C zinc-binding repeat !1homology; protein kinase homology KEYWORDS ATP; autophosphorylation; calcium binding; duplication; !1phorbol ester binding; phospholipid binding; phosphoprotein; !1phosphotransferase; serine/threonine-specific protein !1kinase; zinc FEATURE !$19-29 #region phospholipid binding #status experimental\ !$22-27 #region pseudophosphorylation motif\ !$37-86 #domain protein kinase C zinc-binding repeat homology !8#label KZ1\ !$102-151 #domain protein kinase C zinc-binding repeat homology !8#label KZ2\ !$152-264 #domain protein kinase C C2 region homology #label !8KC2\ !$337-597 #domain protein kinase homology #label KIN\ !$345-353 #region protein kinase ATP-binding motif\ !$37,67,70,86 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$50,53,75,78 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$102,132,135,151 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$115,118,140,143 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$368 #active_site Lys #status predicted\ !$631,638 #binding_site phosphate (Thr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 672 #molecular-weight 76781 #checksum 7409 SEQUENCE /// ENTRY KIBOC #type complete TITLE protein kinase C (EC 2.7.1.-) alpha - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 11-Jun-1999 ACCESSIONS A00621 REFERENCE A00621 !$#authors Parker, P.J.; Coussens, L.; Totty, N.; Rhee, L.; Young, S.; !1Chen, E.; Stabel, S.; Waterfield, M.D.; Ullrich, A. !$#journal Science (1986) 233:853-859 !$#title The complete primary structure of protein kinase C - the !1major phorbol ester receptor. !$#cross-references MUID:86289425; PMID:3755547 !$#accession A00621 !'##molecule_type mRNA !'##residues 1-672 ##label PAR !'##cross-references GB:M13973; NID:g163529; PIDN:AAA30706.1; !1PID:g163530 !'##experimental_source brain COMMENT This is a calcium-activated, phospholipid-dependent, serine- !1and threonine-specific enzyme. It is activated by !1diacylglycerol produced in the cell membrane during !1signal-induced turnover of inositol phospholipids. This !1protein is a receptor for tumor-promoting phorbol esters, !1which can substitute for diacylglycerol in activating the !1enzyme. COMMENT Binding to acidic phospholipids (phosphatidylserine) in the !1cell membrane may occur at multiple sites, including near !1the pseudosubstrate-binding region and within the C2 domain. COMMENT The zinc-stabilized regions bind diacylglycerol and phorbol !1esters. CLASSIFICATION #superfamily protein kinase C alpha; protein kinase C C2 !1region homology; protein kinase C zinc-binding repeat !1homology; protein kinase homology KEYWORDS ATP; autophosphorylation; calcium binding; duplication; !1phorbol ester binding; phospholipid binding; phosphoprotein; !1phosphotransferase; serine/threonine-specific protein !1kinase; zinc FEATURE !$19-29 #region phospholipid binding #status experimental\ !$22-27 #region pseudophosphorylation motif\ !$37-86 #domain protein kinase C zinc-binding repeat homology !8#label KZ1\ !$102-151 #domain protein kinase C zinc-binding repeat homology !8#label KZ2\ !$152-264 #domain protein kinase C C2 region homology #label !8KC2\ !$337-597 #domain protein kinase homology #label KIN\ !$345-353 #region protein kinase ATP-binding motif\ !$37,67,70,86 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$50,53,75,78 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$102,132,135,151 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$115,118,140,143 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$368 #active_site Lys #status predicted\ !$631,638 #binding_site phosphate (Thr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 672 #molecular-weight 76837 #checksum 6340 SEQUENCE /// ENTRY KIHUC1 #type complete TITLE protein kinase C (EC 2.7.1.-) beta-I - human ALTERNATE_NAMES protein kinase C beta, splice form 1 ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 21-Jul-2000 ACCESSIONS S00159; I38118; B29583; I55365; I38117 REFERENCE S00159 !$#authors Kubo, K.; Ohno, S.; Suzuki, K. !$#journal FEBS Lett. (1987) 223:138-142 !$#title Primary structures of human protein kinase C beta-I and !1beta-II differ only in their C-terminal sequences. !$#cross-references MUID:88030028; PMID:3666134 !$#accession S00159 !'##molecule_type mRNA !'##residues 1-671 ##label KUB1 !'##cross-references EMBL:X06318; GB:M27545; NID:g35488; !1PIDN:CAA29634.1; PID:g35489 !'##note the authors translated the codon AGC for residue 352 as Phe, !1TTT for residue 353 as Ser, CTC for residue 647 as Phe, and !1TTC for residue 648 as Leu REFERENCE I38118 !$#authors Kubo, K.; Ohno, S.; Suzuki, K. !$#journal Nucleic Acids Res. (1987) 15:7179-7180 !$#title Nucleotide sequence of the 3' portion of a human gene for !1protein kinase C beta I/beta II. !$#cross-references MUID:88015556; PMID:3658678 !$#accession I38118 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 622-671 ##label KUB2 !'##cross-references EMBL:X05972; NID:g35486; PIDN:CAA29396.1; !1PID:g763117 REFERENCE A90959 !$#authors Coussens, L.; Rhee, L.; Parker, P.J.; Ullrich, A. !$#journal DNA (1987) 6:389-394 !$#title Alternative splicing increases the diversity of the human !1protein kinase C family. !$#cross-references MUID:88054462; PMID:3677994 !$#accession B29583 !'##molecule_type DNA; mRNA !'##residues 612-666,'Y',668-671 ##label COU !'##cross-references GB:M18255; GB:M18181; NID:g189974; PIDN:AAA60097.1; !1PID:g189977 !'##note the authors translated the codon TAT for residue 667 as Phe; !1this sequence is identified by the authors Figure 2 and in !1GenBank entry HUMPKC3 release 106 as beta splice form 2 REFERENCE I55365 !$#authors Obeid, L.M.; Blobe, G.C.; Karolak, L.A.; Hannun, Y.A. !$#journal J. Biol. Chem. (1992) 267:20804-20810 !$#title Cloning and characterization of the major promoter of the !1human protein kinase C beta gene. Regulation by phorbol !1esters. !$#cross-references MUID:93015985; PMID:1400396 !$#accession I55365 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-57 ##label OBE !'##cross-references GB:S47311; NID:g257870; PIDN:AAD13852.1; !1PID:g4261552 REFERENCE I38117 !$#authors Mahajna, J.; King, P.; Parker, P.; Haley, J. !$#journal DNA Cell Biol. (1995) 14:213-222 !$#title Autoregulation of cloned human protein kinase C beta and !1gamma gene promoters in U937 cells. !$#cross-references MUID:95186059; PMID:7880442 !$#accession I38117 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-68,'G' ##label MAH !'##cross-references EMBL:X62532; NID:g619880; PIDN:CAA44393.1; !1PID:g633224 COMMENT This serine/threonine-specific protein kinase is !1calcium-activated and phospholipid-dependent. It is !1activated by diacylglycerol produced in the cell membrane !1during signal-induced turnover of inositol phospholipids. !1This protein acts as a receptor for the tumor-promoting !1phorbol esters that substitute for diacylglycerol in !1activating the enzyme. COMMENT Binding to acidic phospholipids (phosphatidylserine) in the !1cell membrane may occur at multiple sites, including near !1the pseudosubstrate-binding region and within the C2 domain. COMMENT The zinc-stabilized regions bind diacylglycerol and phorbol !1esters. COMMENT For the alternate splice form protein kinase C beta II see !1PIR:KIHUC2. GENETICS !$#gene GDB:PRKCB1; PKCB; PRKCB; PRKCB2 !'##cross-references GDB:128016; OMIM:176970 !$#map_position 16p11.2-16p11.2 !$#introns 58/2; 621/3 !$#note the list of introns is incomplete FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP CLASSIFICATION #superfamily protein kinase C alpha; protein kinase C C2 !1region homology; protein kinase C zinc-binding repeat !1homology; protein kinase homology KEYWORDS alternative splicing; ATP; autophosphorylation; calcium !1binding; duplication; phorbol ester binding; phospholipid !1binding; phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase; zinc FEATURE !$19-29 #region phospholipid binding #status experimental\ !$22-27 #region pseudophosphorylation motif\ !$37-86 #domain protein kinase C zinc-binding repeat homology !8#label KZ1\ !$102-151 #domain protein kinase C zinc-binding repeat homology !8#label KZ2\ !$152-264 #domain protein kinase C C2 region homology #label !8KC2\ !$340-600 #domain protein kinase homology #label KIN\ !$348-356 #region protein kinase ATP-binding motif\ !$11 #binding_site phosphate (Ser) (covalent) (by casein !8kinase II) #status predicted\ !$16 #binding_site phosphate (Ser) (covalent) (by !8autophosphorylation) #status predicted\ !$17,314,324,635,642 #binding_site phosphate (Thr) (covalent) (by !8autophosphorylation) #status predicted\ !$37,67,70,86 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$50,53,75,78 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$102,132,135,151 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$115,118,140,143 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$371 #active_site Lys #status predicted SUMMARY #length 671 #molecular-weight 76868 #checksum 2161 SEQUENCE /// ENTRY KIRTC1 #type complete TITLE protein kinase C (EC 2.7.1.-) beta-I - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 11-Jun-1999 ACCESSIONS A00622; A28423; A05107; I53460; A26408 REFERENCE A00622 !$#authors Ono, Y.; Kurokawa, T.; Fujii, T.; Kawahara, K.; Igarashi, !1K.; Kikkawa, U.; Ogita, K.; Nishizuka, Y. !$#journal FEBS Lett. (1986) 206:347-352 !$#title Two types of complementary DNAs of rat brain protein kinase !1C. Heterogeneity determined by alternative splicing. !$#cross-references MUID:87005287; PMID:2428667 !$#accession A00622 !'##molecule_type mRNA !'##residues 1-671 ##label ONO !'##cross-references EMBL:X04439; NID:g56958; PIDN:CAA28035.1; !1PID:g56959 REFERENCE A28423 !$#authors Housey, G.M.; Johnson, M.D.; Hsiao, W.L.W.; O'Brian, C.A.; !1Murphy, J.P.; Kirschmeier, P.; Weinstein, I.B. !$#journal Cell (1988) 52:343-354 !$#title Overproduction of protein kinase C causes disordered growth !1control in rat fibroblasts. !$#cross-references MUID:88151039; PMID:3345563 !$#accession A28423 !'##molecule_type mRNA !'##residues 1-24,'P',26-293,'E',295-418,'V',420-671 ##label HOU !'##cross-references GB:M19007; NID:g206174; PIDN:AAA41868.1; !1PID:g206175 REFERENCE A90883 !$#authors Knopf, J.L.; Lee, M.H.; Sultzman, L.A.; Kriz, R.W.; Loomis, !1C.R.; Hewick, R.M.; Bell, R.M. !$#journal Cell (1986) 46:491-502 !$#title Cloning and expression of multiple protein kinase C cDNAs. !$#cross-references MUID:86272097; PMID:3755379 !$#accession A05107 !'##molecule_type mRNA !'##residues 80-337;370-671 ##label KNO !'##cross-references GB:K03485; GB:K03486 !'##note the authors translated the codon AUG for residue 650 as Arg. !1Codons for residues 628 and 640 are missing from the !1nucleotide sequence shown in Fig. 4 REFERENCE A38239 !$#authors Hubbard, S.R.; Bishop, W.R.; Kirschmeier, P.; George, S.J.; !1Cramer, S.P.; Hendrickson, W.A. !$#journal Science (1991) 254:1776-1779 !$#title Identification and characterization of zinc binding sites in !1protein kinase C. !$#cross-references MUID:92108419; PMID:1763327 !$#contents annotation; zinc binding REFERENCE I53460 !$#authors Ono, Y.; Kurokawa, T.; Kawahara, K.; Nishimura, O.; !1Marumoto, R.; Igarashi, K.; Sugino, Y.; Kikkawa, U.; Ogita, !1K.; Nishizuka, Y. !$#journal FEBS Lett. (1986) 203:111-115 !$#title Cloning of rat brain protein kinase C complementary DNA. !$#cross-references MUID:86275229; PMID:3755404 !$#accession I53460 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 448-671 ##label RES !'##cross-references EMBL:X04139; NID:g56919; PIDN:CAA27756.1; !1PID:g56920 COMMENT This is a calcium-activated, phospholipid-dependent, serine- !1and threonine-specific enzyme. It is activated by !1diacylglycerol produced in the cell membrane during !1signal-induced turnover of inositol phospholipids. This !1protein is a receptor for tumor-promoting phorbol esters, !1which can substitute for diacylglycerol in activating the !1enzyme. COMMENT The two forms of protein kinase C beta (I and II) are !1encoded by the same gene and differ from each other only at !1their carboxyl ends. COMMENT Binding to acidic phospholipids (phosphatidylserine) in the !1cell membrane may occur at multiple sites, including near !1the pseudosubstrate-binding region and within the C2 domain. COMMENT The zinc-stabilized regions bind diacylglycerol and phorbol !1esters. CLASSIFICATION #superfamily protein kinase C alpha; protein kinase C C2 !1region homology; protein kinase C zinc-binding repeat !1homology; protein kinase homology KEYWORDS alternative splicing; ATP; autophosphorylation; calcium !1binding; duplication; phorbol ester binding; phospholipid !1binding; phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase; zinc FEATURE !$19-29 #region phospholipid binding #status experimental\ !$22-27 #region pseudophosphorylation motif\ !$37-86 #domain protein kinase C zinc-binding repeat homology !8#label KZ1\ !$102-151 #domain protein kinase C zinc-binding repeat homology !8#label KZ2\ !$152-264 #domain protein kinase C C2 region homology #label !8KC2\ !$340-600 #domain protein kinase homology #label KIN\ !$348-356 #region protein kinase ATP-binding motif\ !$11 #binding_site phosphate (Ser) (covalent) (by casein !8kinase II) #status predicted\ !$16 #binding_site phosphate (Ser) (covalent) (by !8autophosphorylation) #status predicted\ !$17,314,324,635,642 #binding_site phosphate (Thr) (covalent) (by !8autophosphorylation) #status predicted\ !$37,67,70,86 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$50,53,75,78 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$102,132,135,151 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$115,118,140,143 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$371 #active_site Lys #status predicted SUMMARY #length 671 #molecular-weight 76782 #checksum 9470 SEQUENCE /// ENTRY KIRBC1 #type complete TITLE protein kinase C (EC 2.7.1.-) beta-I - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 11-Jun-1999 ACCESSIONS B26037 REFERENCE A26037 !$#authors Ohno, S.; Kawasaki, H.; Imajoh, S.; Suzuki, K.; Inagaki, M.; !1Yokokura, H.; Sakoh, T.; Hidaka, H. !$#journal Nature (1987) 325:161-166 !$#title Tissue-specific expression of three distinct types of rabbit !1protein kinase C. !$#cross-references MUID:87115883; PMID:3808073 !$#accession B26037 !'##molecule_type mRNA !'##residues 1-671 ##label OHN !'##cross-references EMBL:X04795; NID:g1670; PIDN:CAA28482.1; PID:g1671 COMMENT This is a calcium-activated, phospholipid-dependent, serine- !1and threonine-specific enzyme. It is activated by !1diacylglycerol produced in the cell membrane during !1signal-induced turnover of inositol phospholipids. This !1protein is a receptor for tumor-promoting phorbol esters, !1which can substitute for diacylglycerol in activating the !1enzyme. COMMENT The two forms of protein kinase C beta (I and II) are !1encoded by the same gene and differ from each other only at !1their carboxyl ends. COMMENT Binding to acidic phospholipids (phosphatidylserine) in the !1cell membrane may occur at multiple sites, including near !1the pseudosubstrate-binding region and within the C2 domain. COMMENT The zinc-stabilized regions bind diacylglycerol and phorbol !1esters. CLASSIFICATION #superfamily protein kinase C alpha; protein kinase C C2 !1region homology; protein kinase C zinc-binding repeat !1homology; protein kinase homology KEYWORDS alternative splicing; ATP; autophosphorylation; calcium !1binding; duplication; phorbol ester binding; phospholipid !1binding; phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase; zinc FEATURE !$19-29 #region phospholipid binding #status experimental\ !$22-27 #region pseudophosphorylation motif\ !$37-86 #domain protein kinase C zinc-binding repeat homology !8#label KZ1\ !$102-151 #domain protein kinase C zinc-binding repeat homology !8#label KZ2\ !$152-264 #domain protein kinase C C2 region homology #label !8KC2\ !$340-600 #domain protein kinase homology #label KIN\ !$348-356 #region protein kinase ATP-binding motif\ !$11 #binding_site phosphate (Ser) (covalent) (by casein !8kinase II) #status predicted\ !$16 #binding_site phosphate (Ser) (covalent) (by !8autophosphorylation) #status predicted\ !$17,314,324,635,642 #binding_site phosphate (Thr) (covalent) (by !8autophosphorylation) #status predicted\ !$37,67,70,86 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$50,53,75,78 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$102,132,135,151 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$115,118,140,143 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$371 #active_site Lys #status predicted SUMMARY #length 671 #molecular-weight 76827 #checksum 924 SEQUENCE /// ENTRY KIHUC2 #type complete TITLE protein kinase C (EC 2.7.1.-) beta-II - human ALTERNATE_NAMES protein kinase C beta, splice form 2 ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jun-2000 ACCESSIONS B24664; A29583; S01626; I38119; A42159 REFERENCE A94291 !$#authors Coussens, L.; Parker, P.J.; Rhee, L.; Yang-Feng, T.L.; Chen, !1E.; Waterfield, M.D.; Francke, U.; Ullrich, A. !$#journal Science (1986) 233:859-866 !$#title Multiple, distinct forms of bovine and human protein kinase !1C suggest diversity in cellular signaling pathways. !$#cross-references MUID:86289426; PMID:3755548 !$#accession B24664 !'##molecule_type mRNA !'##residues 1-673 ##label COU1 !'##cross-references GB:M13975; NID:g189968; PIDN:AAA60095.1; !1PID:g189969 REFERENCE A90959 !$#authors Coussens, L.; Rhee, L.; Parker, P.J.; Ullrich, A. !$#journal DNA (1987) 6:389-394 !$#title Alternative splicing increases the diversity of the human !1protein kinase C family. !$#cross-references MUID:88054462; PMID:3677994 !$#accession A29583 !'##molecule_type DNA !'##residues 622-673 ##label COU2 !'##cross-references GB:M18254; NID:g189973; PIDN:AAA60096.1; !1PID:g189976 !'##note this sequence is identified by the authors Figure 2 and in !1GenBank entry HUMPKC2 release 106 as beta splice form 1 REFERENCE S00159 !$#authors Kubo, K.; Ohno, S.; Suzuki, K. !$#journal FEBS Lett. (1987) 223:138-142 !$#title Primary structures of human protein kinase C beta-I and !1beta-II differ only in their C-terminal sequences. !$#cross-references MUID:88030028; PMID:3666134 !$#accession S01626 !'##status preliminary !'##molecule_type mRNA !'##residues 1-673 ##label KUB1 !'##cross-references EMBL:X07109; GB:M27546; NID:g35492; !1PIDN:CAA30130.1; PID:g35493 REFERENCE I38118 !$#authors Kubo, K.; Ohno, S.; Suzuki, K. !$#journal Nucleic Acids Res. (1987) 15:7179-7180 !$#title Nucleotide sequence of the 3' portion of a human gene for !1protein kinase C beta I/beta II. !$#cross-references MUID:88015556; PMID:3658678 !$#accession I38119 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 622-673 ##label KUB2 !'##cross-references EMBL:X05971; NID:g35490; PIDN:CAA29395.1; !1PID:g763118 REFERENCE A42159 !$#authors Niino, Y.S.; Ohno, S.; Suzuki, K. !$#journal J. Biol. Chem. (1992) 267:6158-6163 !$#title Positive and negative regulation of the transcription of the !1human protein kinase C beta gene. !$#cross-references MUID:92210589; PMID:1556124 !$#accession A42159 !'##molecule_type DNA !'##residues 1-58 ##label NII !'##cross-references GB:D10022; NID:g220001; PIDN:BAA00912.1; !1PID:g220002 COMMENT This serine/threonine-specific protein kinase is !1calcium-activated and phospholipid-dependent. It is !1activated by diacylglycerol produced in the cell membrane !1during signal-induced turnover of inositol phospholipids. !1This protein acts as a receptor for the tumor-promoting !1phorbol esters that substitute for diacylglycerol in !1activating the enzyme. COMMENT Binding to acidic phospholipids (phosphatidylserine) in the !1cell membrane may occur at multiple sites, including near !1the pseudosubstrate-binding region and within the C2 domain. COMMENT The zinc-stabilized regions bind diacylglycerol and phorbol !1esters. COMMENT For the alternate splice form protein kinase C beta I see !1PIR:KIHUC1. GENETICS !$#gene GDB:PRKCB1; PRKCB2; PKCB; PRKCB !'##cross-references GDB:128016; OMIM:176970 !$#map_position 16p11.2-16p11.2 !$#introns 58/2; 621/3 !$#note the list of introns is incomplete FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP CLASSIFICATION #superfamily protein kinase C alpha; protein kinase C C2 !1region homology; protein kinase C zinc-binding repeat !1homology; protein kinase homology KEYWORDS alternative splicing; ATP; autophosphorylation; calcium !1binding; duplication; phorbol ester binding; phospholipid !1binding; phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase; zinc FEATURE !$19-29 #region phospholipid binding #status experimental\ !$22-27 #region pseudophosphorylation motif\ !$37-86 #domain protein kinase C zinc-binding repeat homology !8#label KZ1\ !$102-151 #domain protein kinase C zinc-binding repeat homology !8#label KZ2\ !$152-264 #domain protein kinase C C2 region homology #label !8KC2\ !$340-600 #domain protein kinase homology #label KIN\ !$348-356 #region protein kinase ATP-binding motif\ !$11 #binding_site phosphate (Ser) (covalent) (by casein !8kinase II) #status predicted\ !$16 #binding_site phosphate (Ser) (covalent) (by !8autophosphorylation) #status predicted\ !$17,314,324,634,641 #binding_site phosphate (Thr) (covalent) (by !8autophosphorylation) #status predicted\ !$37,67,70,86 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$50,53,75,78 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$102,132,135,151 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$115,118,140,143 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$371 #active_site Lys #status predicted SUMMARY #length 673 #molecular-weight 77012 #checksum 7476 SEQUENCE /// ENTRY KIRTC2 #type complete TITLE protein kinase C (EC 2.7.1.-) beta-II - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 11-Jun-1999 ACCESSIONS A00623; A05106; A38237; A38238; A43612 REFERENCE A00622 !$#authors Ono, Y.; Kurokawa, T.; Fujii, T.; Kawahara, K.; Igarashi, !1K.; Kikkawa, U.; Ogita, K.; Nishizuka, Y. !$#journal FEBS Lett. (1986) 206:347-352 !$#title Two types of complementary DNAs of rat brain protein kinase !1C. Heterogeneity determined by alternative splicing. !$#cross-references MUID:87005287; PMID:2428667 !$#accession A00623 !'##molecule_type mRNA !'##residues 1-673 ##label ONO !'##cross-references EMBL:X04440; NID:g56960; PIDN:CAA28036.1; !1PID:g56961 REFERENCE A90883 !$#authors Knopf, J.L.; Lee, M.H.; Sultzman, L.A.; Kriz, R.W.; Loomis, !1C.R.; Hewick, R.M.; Bell, R.M. !$#journal Cell (1986) 46:491-502 !$#title Cloning and expression of multiple protein kinase C cDNAs. !$#cross-references MUID:86272097; PMID:3755379 !$#accession A05106 !'##molecule_type mRNA !'##residues 1-125,'V',127-137,'S',139-140,'R',142-148,'G',150-163,'V', !1165-169,'GG',172-173,'V',175-418,'V',420-673 ##label KNO !'##cross-references GB:M13706; NID:g206188; PIDN:AAA41875.1; !1PID:g206189 REFERENCE A38237 !$#authors Flint, A.J.; Paladini, R.D.; Koshland Jr., D.E. !$#journal Science (1990) 249:408-411 !$#title Autophosphorylation of protein kinase C at three separated !1regions of its primary sequence. !$#cross-references MUID:90333259; PMID:2377895 !$#contents autophosphorylation sites !$#accession A38237 !'##molecule_type protein !'##residues 3-19;310-327;632-649 ##label FLI REFERENCE A38238 !$#authors Tominaga, M.; Kitagawa, Y.; Tanaka, S.; Kishimoto, A. !$#journal J. Biochem. (1991) 110:655-660 !$#title Phosphorylation of type II (beta) protein kinase C by casein !1kinase II. !$#cross-references MUID:92138675; PMID:1778990 !$#contents casein kinase II phosphorylation site !$#accession A38238 !'##molecule_type protein !'##residues 3-12 ##label TOM REFERENCE A43612 !$#authors Ono, Y.; Kikkawa, U.; Ogita, K.; Fujii, T.; Kurokawa, T.; !1Asaoka, Y.; Sekiguchi, K.; Ase, K.; Igarashi, K.; Nishizuka, !1Y. !$#journal Science (1987) 236:1116-1120 !$#title Expression and properties of two types of protein kinase C: !1alternative splicing from a single gene. !$#cross-references MUID:87206239; PMID:3576226 !$#accession A43612 !'##molecule_type DNA !'##residues 622-673 ##label ON2 !'##cross-references GB:M16829; NID:g206176; PIDN:AAA41869.1; !1PID:g206177 COMMENT This is a calcium-activated, phospholipid-dependent, serine- !1and threonine-specific enzyme. It is activated by !1diacylglycerol produced in the cell membrane during !1signal-induced turnover of inositol phospholipids. This !1protein is a receptor for tumor-promoting phorbol esters, !1which can substitute for diacylglycerol in activating the !1enzyme. COMMENT The two forms of protein kinase C beta (I and II) are !1encoded by the same gene and differ from each other only at !1their carboxyl ends. COMMENT Binding to acidic phospholipids (phosphatidylserine) in the !1cell membrane may occur at multiple sites, including near !1the pseudosubstrate-binding region and within the C2 domain. COMMENT The zinc-stabilized regions bind diacylglycerol and phorbol !1esters. CLASSIFICATION #superfamily protein kinase C alpha; protein kinase C C2 !1region homology; protein kinase C zinc-binding repeat !1homology; protein kinase homology KEYWORDS alternative splicing; ATP; autophosphorylation; calcium !1binding; duplication; phorbol ester binding; phospholipid !1binding; phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase; zinc FEATURE !$19-29 #region phospholipid binding #status experimental\ !$22-27 #region pseudophosphorylation motif\ !$37-86 #domain protein kinase C zinc-binding repeat homology !8#label KZ1\ !$102-151 #domain protein kinase C zinc-binding repeat homology !8#label KZ2\ !$152-264 #domain protein kinase C C2 region homology #label !8KC2\ !$340-600 #domain protein kinase homology #label KIN\ !$348-356 #region protein kinase ATP-binding motif\ !$11 #binding_site phosphate (Ser) (covalent) (by casein !8kinase II) (partial) #status experimental\ !$16 #binding_site phosphate (Ser) (covalent) (by !8autophosphorylation) (partial) #status experimental\ !$17,314,324,634,641 #binding_site phosphate (Thr) (covalent) (by !8autophosphorylation) (partial) #status experimental\ !$37,67,70,86 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$50,53,75,78 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$102,132,135,151 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$115,118,140,143 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$371 #active_site Lys #status predicted SUMMARY #length 673 #molecular-weight 76926 #checksum 4785 SEQUENCE /// ENTRY KIRBC2 #type complete TITLE protein kinase C (EC 2.7.1.-) beta-II - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 11-Jun-1999 ACCESSIONS A26037 REFERENCE A26037 !$#authors Ohno, S.; Kawasaki, H.; Imajoh, S.; Suzuki, K.; Inagaki, M.; !1Yokokura, H.; Sakoh, T.; Hidaka, H. !$#journal Nature (1987) 325:161-166 !$#title Tissue-specific expression of three distinct types of rabbit !1protein kinase C. !$#cross-references MUID:87115883; PMID:3808073 !$#accession A26037 !'##molecule_type mRNA !'##residues 1-673 ##label OHN !'##cross-references EMBL:X04793; NID:g1668; PIDN:CAA28480.1; PID:g1669 COMMENT This is a calcium-activated, phospholipid-dependent, serine- !1and threonine-specific enzyme. It is activated by !1diacylglycerol produced in the cell membrane during !1signal-induced turnover of inositol phospholipids. This !1protein is a receptor for tumor-promoting phorbol esters, !1which can substitute for diacylglycerol in activating the !1enzyme. COMMENT The two forms of protein kinase C beta (I and II) are !1encoded by the same gene and differ from each other only at !1their carboxyl ends. COMMENT Binding to acidic phospholipids (phosphatidylserine) in the !1cell membrane may occur at multiple sites, including near !1the pseudosubstrate-binding region and within the C2 domain. COMMENT The zinc-stabilized regions bind diacylglycerol and phorbol !1esters. CLASSIFICATION #superfamily protein kinase C alpha; protein kinase C C2 !1region homology; protein kinase C zinc-binding repeat !1homology; protein kinase homology KEYWORDS alternative splicing; ATP; autophosphorylation; calcium !1binding; duplication; phorbol ester binding; phospholipid !1binding; phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase; zinc FEATURE !$19-29 #region phospholipid binding #status experimental\ !$22-27 #region pseudophosphorylation motif\ !$37-86 #domain protein kinase C zinc-binding repeat homology !8#label KZ1\ !$102-151 #domain protein kinase C zinc-binding repeat homology !8#label KZ2\ !$152-264 #domain protein kinase C C2 region homology #label !8KC2\ !$340-600 #domain protein kinase homology #label KIN\ !$348-356 #region protein kinase ATP-binding motif\ !$11 #binding_site phosphate (Ser) (covalent) (by casein !8kinase II) #status predicted\ !$16 #binding_site phosphate (Ser) (covalent) (by !8autophosphorylation) #status predicted\ !$17,314,324,634,641 #binding_site phosphate (Thr) (covalent) (by !8autophosphorylation) #status predicted\ !$37,67,70,86 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$50,53,75,78 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$102,132,135,151 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$115,118,140,143 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$371 #active_site Lys #status predicted SUMMARY #length 673 #molecular-weight 76971 #checksum 6239 SEQUENCE /// ENTRY KIBOC2 #type complete TITLE protein kinase C (EC 2.7.1.-) beta-II - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 11-Jun-1999 ACCESSIONS A24664 REFERENCE A94291 !$#authors Coussens, L.; Parker, P.J.; Rhee, L.; Yang-Feng, T.L.; Chen, !1E.; Waterfield, M.D.; Francke, U.; Ullrich, A. !$#journal Science (1986) 233:859-866 !$#title Multiple, distinct forms of bovine and human protein kinase !1C suggest diversity in cellular signaling pathways. !$#cross-references MUID:86289426; PMID:3755548 !$#accession A24664 !'##molecule_type mRNA !'##residues 1-673 ##label COU !'##cross-references GB:M13974; NID:g163523; PIDN:AAA30703.1; !1PID:g163524 COMMENT This is a calcium-activated, phospholipid-dependent, serine- !1and threonine-specific enzyme. It is activated by !1diacylglycerol produced in the cell membrane during !1signal-induced turnover of inositol phospholipids. This !1protein is a receptor for tumor-promoting phorbol esters, !1which can substitute for diacylglycerol in activating the !1enzyme. COMMENT The two forms of protein kinase C beta (I and II) are !1encoded by the same gene and differ from each other only at !1their carboxyl ends. COMMENT Binding to acidic phospholipids (phosphatidylserine) in the !1cell membrane may occur at multiple sites, including near !1the pseudosubstrate-binding region and within the C2 domain. COMMENT The zinc-stabilized regions bind diacylglycerol and phorbol !1esters. CLASSIFICATION #superfamily protein kinase C alpha; protein kinase C C2 !1region homology; protein kinase C zinc-binding repeat !1homology; protein kinase homology KEYWORDS alternative splicing; ATP; autophosphorylation; calcium !1binding; duplication; phorbol ester binding; phospholipid !1binding; phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase; zinc FEATURE !$19-29 #region phospholipid binding #status experimental\ !$22-27 #region pseudophosphorylation motif\ !$37-86 #domain protein kinase C zinc-binding repeat homology !8#label KZ1\ !$102-151 #domain protein kinase C zinc-binding repeat homology !8#label KZ2\ !$152-264 #domain protein kinase C C2 region homology #label !8KC2\ !$340-600 #domain protein kinase homology #label KIN\ !$348-356 #region protein kinase ATP-binding motif\ !$11 #binding_site phosphate (Ser) (covalent) (by casein !8kinase II) #status predicted\ !$16 #binding_site phosphate (Ser) (covalent) (by !8autophosphorylation) #status predicted\ !$17,324,634,641 #binding_site phosphate (Thr) (covalent) (by !8autophosphorylation) #status predicted\ !$371 #active_site Lys #status predicted SUMMARY #length 673 #molecular-weight 76915 #checksum 6145 SEQUENCE /// ENTRY KIRTGC #type complete TITLE protein kinase C (EC 2.7.1.-) gamma - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 11-Jun-1999 ACCESSIONS A05105; S02129; I55317 REFERENCE A90883 !$#authors Knopf, J.L.; Lee, M.H.; Sultzman, L.A.; Kriz, R.W.; Loomis, !1C.R.; Hewick, R.M.; Bell, R.M. !$#journal Cell (1986) 46:491-502 !$#title Cloning and expression of multiple protein kinase C cDNAs. !$#cross-references MUID:86272097; PMID:3755379 !$#accession A05105 !'##molecule_type mRNA !'##residues 1-697 ##label KNO !'##cross-references GB:M13707; NID:g206186; PIDN:AAA41874.1; !1PID:g206187 !'##note the authors translated the codon UUU for residue 432 as Glu REFERENCE S02129 !$#authors Ono, Y.; Fujii, T.; Igarashi, K.; Kikkawa, U.; Ogita, K.; !1Nishizuka, Y. !$#journal Nucleic Acids Res. (1988) 16:5199-5200 !$#title Nucleotide sequences of cDNAs for alpha and gamma subspecies !1of rat brain protein kinase C. !$#cross-references MUID:88262515; PMID:3387228 !$#accession S02129 !'##molecule_type mRNA !'##residues 1-697 ##label ONO !'##cross-references EMBL:X07287; NID:g56917; PIDN:CAA30267.1; !1PID:g56918 REFERENCE I55317 !$#authors Chen, K. !$#journal J. Biol. Chem. (1990) 265:19961-19965 !$#title Characterization of the 5'-flanking region of the rat !1protein kinase C gamma gene. !$#cross-references MUID:91060619; PMID:2246272 !$#accession I55317 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-56 ##label RES !'##cross-references GB:M55417; NID:g206184; PIDN:AAA41873.1; !1PID:g554487 COMMENT This is a calcium-activated, phospholipid-dependent, serine- !1and threonine-specific enzyme. It is activated by !1diacylglycerol produced in the cell membrane during !1signal-induced turnover of inositol phospholipids. This !1protein is a receptor for tumor-promoting phorbol esters, !1which can substitute for diacylglycerol in activating the !1enzyme. COMMENT Binding to acidic phospholipids (phosphatidylserine) in the !1cell membrane may occur at multiple sites, including near !1the pseudosubstrate-binding region and within the C2 domain. COMMENT The zinc-stabilized regions bind diacylglycerol and phorbol !1esters. GENETICS !$#gene PRKC-gamma CLASSIFICATION #superfamily protein kinase C alpha; protein kinase C C2 !1region homology; protein kinase C zinc-binding repeat !1homology; protein kinase homology KEYWORDS ATP; autophosphorylation; calcium binding; duplication; !1phorbol ester binding; phospholipid binding; phosphoprotein; !1phosphotransferase; serine/threonine-specific protein !1kinase; zinc FEATURE !$18-28 #region phospholipid binding #status predicted\ !$21-26 #region pseudophosphorylation motif\ !$36-85 #domain protein kinase C zinc-binding repeat homology !8#label KZ1\ !$101-150 #domain protein kinase C zinc-binding repeat homology !8#label KZ2\ !$151-264 #domain protein kinase C C2 region homology #label !8KC2\ !$349-614 #domain protein kinase homology #label KIN\ !$357-365 #region protein kinase ATP-binding motif\ !$36,66,69,85 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$49,52,74,77 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$101,131,134,150 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$114,117,139,142 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$380 #active_site Lys #status predicted\ !$648,655 #binding_site phosphate (Thr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 697 #molecular-weight 78357 #checksum 6853 SEQUENCE /// ENTRY KIRBGC #type complete TITLE protein kinase C (EC 2.7.1.-) gamma - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 11-Jun-1999 ACCESSIONS A28708 REFERENCE A28708 !$#authors Ohno, S.; Kawasaki, H.; Konno, Y.; Inagaki, M.; Hidaka, H.; !1Suzuki, K. !$#journal Biochemistry (1988) 27:2083-2087 !$#title A fourth type of rabbit protein kinase C. !$#cross-references MUID:88241036; PMID:2837282 !$#accession A28708 !'##molecule_type mRNA !'##residues 1-697 ##label OHN !'##cross-references GB:M19338; NID:g165651; PIDN:AAA31449.1; !1PID:g165652 COMMENT This is a calcium-activated, phospholipid-dependent, serine- !1and threonine-specific enzyme. It is activated by !1diacylglycerol produced in the cell membrane during !1signal-induced turnover of inositol phospholipids. This !1protein is a receptor for tumor-promoting phorbol esters, !1which can substitute for diacylglycerol in activating the !1enzyme. COMMENT Binding to acidic phospholipids (phosphatidylserine) in the !1cell membrane may occur at multiple sites, including near !1the pseudosubstrate-binding region and within the C2 domain. COMMENT The zinc-stabilized regions bind diacylglycerol and phorbol !1esters. CLASSIFICATION #superfamily protein kinase C alpha; protein kinase C C2 !1region homology; protein kinase C zinc-binding repeat !1homology; protein kinase homology KEYWORDS ATP; autophosphorylation; calcium binding; duplication; !1phorbol ester binding; phospholipid binding; phosphoprotein; !1phosphotransferase; serine/threonine-specific protein !1kinase; zinc FEATURE !$18-28 #region phospholipid binding #status predicted\ !$21-26 #region pseudophosphorylation motif\ !$36-85 #domain protein kinase C zinc-binding repeat homology !8#label KZ1\ !$101-150 #domain protein kinase C zinc-binding repeat homology !8#label KZ2\ !$151-264 #domain protein kinase C C2 region homology #label !8KC2\ !$349-614 #domain protein kinase homology #label KIN\ !$357-365 #region protein kinase ATP-binding motif\ !$36,66,69,85 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$49,52,74,77 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$101,131,134,150 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$114,117,139,142 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$380 #active_site Lys #status predicted\ !$648,655 #binding_site phosphate (Thr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 697 #molecular-weight 78371 #checksum 7549 SEQUENCE /// ENTRY KIBOGC #type fragment TITLE protein kinase C (EC 2.7.1.-) gamma - bovine (fragment) ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 11-Jun-1999 ACCESSIONS C24664 REFERENCE A94291 !$#authors Coussens, L.; Parker, P.J.; Rhee, L.; Yang-Feng, T.L.; Chen, !1E.; Waterfield, M.D.; Francke, U.; Ullrich, A. !$#journal Science (1986) 233:859-866 !$#title Multiple, distinct forms of bovine and human protein kinase !1C suggest diversity in cellular signaling pathways. !$#cross-references MUID:86289426; PMID:3755548 !$#accession C24664 !'##molecule_type mRNA !'##residues 1-682 ##label OHN !'##cross-references GB:M13976; NID:g163525; PIDN:AAA30704.1; !1PID:g163526 COMMENT This is a calcium-activated, phospholipid-dependent, serine- !1and threonine-specific enzyme. It is activated by !1diacylglycerol produced in the cell membrane during !1signal-induced turnover of inositol phospholipids. This !1protein is a receptor for tumor-promoting phorbol esters, !1which can substitute for diacylglycerol in activating the !1enzyme. COMMENT Binding to acidic phospholipids (phosphatidylserine) in the !1cell membrane may occur at multiple sites, including near !1the pseudosubstrate-binding region and within the C2 domain. COMMENT The zinc-stabilized regions bind diacylglycerol and phorbol !1esters. CLASSIFICATION #superfamily protein kinase C alpha; protein kinase C C2 !1region homology; protein kinase C zinc-binding repeat !1homology; protein kinase homology KEYWORDS ATP; autophosphorylation; calcium binding; duplication; !1phorbol ester binding; phospholipid binding; phosphoprotein; !1phosphotransferase; serine/threonine-specific protein !1kinase; zinc FEATURE !$3-13 #region phospholipid binding #status predicted\ !$6-11 #region pseudophosphorylation motif\ !$21-70 #domain protein kinase C zinc-binding repeat homology !8#label KZ1\ !$86-135 #domain protein kinase C zinc-binding repeat homology !8#label KZ2\ !$136-249 #domain protein kinase C C2 region homology #label !8KC2\ !$334-599 #domain protein kinase homology #label KIN\ !$342-350 #region protein kinase ATP-binding motif\ !$21,51,54,70 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$34,37,59,62 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$86,116,119,135 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$99,102,124,127 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$365 #active_site Lys #status predicted\ !$633,640 #binding_site phosphate (Thr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 682 #checksum 302 SEQUENCE /// ENTRY S35704 #type complete TITLE protein kinase C (EC 2.7.1.-) delta - human ORGANISM #formal_name Homo sapiens #common_name man DATE 06-Jan-1995 #sequence_revision 06-Jan-1995 #text_change 11-Jun-1999 ACCESSIONS S35704; S35705; S65016 REFERENCE S35704 !$#authors Aris, J.P.; Basta, P.V.; Holmes, W.D.; Ballas, L.M.; Moomaw, !1C.; Rankl, N.B.; Blobel, G.; Loomis, C.R.; Burns, D.J. !$#journal Biochim. Biophys. Acta (1993) 1174:171-181 !$#title Molecular and biochemical characterization of a recombinant !1human PKC-delta family member. !$#cross-references MUID:93363635; PMID:8357834 !$#accession S35704 !'##status preliminary !'##molecule_type mRNA !'##residues 1-676 ##label ARI !'##cross-references EMBL:L07861; NID:g189984; PIDN:AAA03175.1; !1PID:g189985 !$#accession S35705 !'##status preliminary !'##molecule_type mRNA !'##residues 1-374,'S',376-592,'M',594-676 ##label AR2 !'##cross-references EMBL:L07860; NID:g189679; PIDN:AAA03176.1; !1PID:g189680 REFERENCE S51020 !$#authors Palmer, R.H.; Ridden, J.; Parker, P.J. !$#journal FEBS Lett. (1994) 356:5-8 !$#title Identification of multiple, novel, protein kinase C-related !1gene products. !$#cross-references MUID:95080426; PMID:7988719 !$#accession S65016 !'##status preliminary; nucleic acid sequence not shown; not compared !1with conceptual translation !'##molecule_type mRNA !'##residues 432-493,'V',495-532,'A' ##label PAL GENETICS !$#gene GDB:PRKCD; Hs.458 !'##cross-references GDB:128038; OMIM:176977 !$#map_position 3pter-3qter FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP !$#note activity is calcium-independent, phospholipid-dependent, and !1activated by diacylglycerol and by tumor-promoting phorbol !1esters CLASSIFICATION #superfamily protein kinase C delta; protein kinase C !1zinc-binding repeat homology; protein kinase homology KEYWORDS ATP; duplication; phorbol ester binding; phospholipid !1binding; phosphotransferase; serine/threonine-specific !1protein kinase; zinc FEATURE !$144-149 #region pseudophosphorylation motif\ !$159-208 #domain protein kinase C zinc-binding repeat homology !8#label KZ1\ !$231-280 #domain protein kinase C zinc-binding repeat homology !8#label KZ2\ !$347-603 #domain protein kinase homology #label KIN\ !$355-363 #region protein kinase ATP-binding motif\ !$159,189,192,208 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$172,175,197,200 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$231,261,264,280 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$244,247,269,272 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$378,397,473,475 #active_site Lys, Glu, Asp, Lys #status predicted SUMMARY #length 676 #molecular-weight 77504 #checksum 5757 SEQUENCE /// ENTRY KIRTCD #type complete TITLE protein kinase C (EC 2.7.1.-) delta [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Aug-2000 ACCESSIONS A28163; S17832; S00215 REFERENCE A92717 !$#authors Ono, Y.; Fujii, T.; Ogita, K.; Kikkawa, U.; Igarashi, K.; !1Nishizuka, Y. !$#journal J. Biol. Chem. (1988) 263:6927-6932 !$#title The structure, expression, and properties of additional !1members of the protein kinase C family. !$#cross-references MUID:88198270; PMID:2834397 !$#accession A28163 !'##molecule_type DNA !'##residues 1-673 ##label ONO !'##cross-references GB:M18330; NID:g206180; PIDN:AAA41871.1; !1PID:g206181 REFERENCE S17832 !$#authors Olivier, A.R.; Parker, P.J. !$#journal Eur. J. Biochem. (1991) 200:805-810 !$#title Expression and characterization of protein kinase C-delta. !$#cross-references MUID:92007860; PMID:1915352 !$#accession S17832 !'##molecule_type protein !'##residues 142-146,'S',148-153 ##label OLI COMMENT This is a calcium-independent, phospholipid-dependent, !1serine- and threonine-specific enzyme. It is activated by !1diacylglycerol produced in the cell membrane during !1signal-induced turnover of inositol phospholipids. This !1protein is a receptor for tumor-promoting phorbol esters, !1which can substitute for diacylglycerol in activating the !1enzyme. CLASSIFICATION #superfamily protein kinase C delta; protein kinase C !1zinc-binding repeat homology; protein kinase homology KEYWORDS ATP; duplication; phorbol ester binding; phospholipid !1binding; phosphotransferase; serine/threonine-specific !1protein kinase; zinc FEATURE !$144-149 #region pseudophosphorylation motif\ !$159-208 #domain protein kinase C zinc-binding repeat homology !8#label KZ1\ !$231-280 #domain protein kinase C zinc-binding repeat homology !8#label KZ2\ !$345-601 #domain protein kinase homology #label KIN\ !$353-361 #region protein kinase ATP-binding motif\ !$159,189,192,208 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$172,175,197,200 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$231,261,264,280 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$244,247,269,272 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$376 #active_site Lys #status predicted SUMMARY #length 673 #molecular-weight 77520 #checksum 7710 SEQUENCE /// ENTRY KIMSCD #type complete TITLE protein kinase C (EC 2.7.1.-) delta - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 11-Jun-1999 ACCESSIONS A40281; S19709 REFERENCE A40281 !$#authors Mischak, H.; Bodenteich, A.; Kolch, W.; Goodnight, J.; !1Hofer, F.; Mushinski, J.F. !$#journal Biochemistry (1991) 30:7925-7931 !$#title Mouse protein kinase C-delta, the major isoform expressed in !1mouse hemopoietic cells: sequence of the cDNA, expression !1patterns, and characterization of the protein. !$#cross-references MUID:91329364; PMID:1868068 !$#accession A40281 !'##molecule_type mRNA !'##residues 1-674 ##label MIS !'##cross-references GB:M69042; NID:g200380; PIDN:AAA73056.1; !1PID:g200381 REFERENCE S19709 !$#authors Mizuno, K.; Kubo, K.; Saido, T.C.; Akita, Y.; Osada, S.; !1Kuroki, T.; Ohno, S.; Suzuki, K. !$#journal Eur. J. Biochem. (1991) 202:931-940 !$#title Structure and properties of a ubiquitously expressed protein !1kinase C, nPKCdelta. !$#cross-references MUID:92111544; PMID:1765103 !$#accession S19709 !'##status preliminary !'##molecule_type mRNA !'##residues 1-318,'E',320-329,'G',331-336,'E',338-500,'G',502,'A', !1504-512,'I',514-674 ##label MIZ !'##cross-references EMBL:X60304; NID:g53436; PIDN:CAA42845.1; !1PID:g53437 COMMENT This is a calcium-independent, phospholipid-dependent, !1serine- and threonine-specific enzyme. It is activated by !1diacylglycerol produced in the cell membrane during !1signal-induced turnover of inositol phospholipids. This !1protein is a receptor for tumor-promoting phorbol esters, !1which can substitute for diacylglycerol in activating the !1enzyme. CLASSIFICATION #superfamily protein kinase C delta; protein kinase C !1zinc-binding repeat homology; protein kinase homology KEYWORDS ATP; duplication; phorbol ester binding; phospholipid !1binding; phosphotransferase; serine/threonine-specific !1protein kinase; zinc FEATURE !$144-149 #region pseudophosphorylation motif\ !$159-208 #domain protein kinase C zinc-binding repeat homology !8#label KZ1\ !$231-280 #domain protein kinase C zinc-binding repeat homology !8#label KZ2\ !$345-601 #domain protein kinase homology #label KIN\ !$353-361 #region protein kinase ATP-binding motif\ !$159,189,192,208 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$172,175,197,200 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$231,261,264,280 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$244,247,269,272 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$376 #active_site Lys #status predicted SUMMARY #length 674 #molecular-weight 77690 #checksum 2911 SEQUENCE /// ENTRY A45416 #type complete TITLE protein kinase C (EC 2.7.1.-) theta - human ORGANISM #formal_name Homo sapiens #common_name man DATE 21-Sep-1993 #sequence_revision 18-Nov-1994 #text_change 11-Jun-1999 ACCESSIONS A45416; A47160 REFERENCE A45416 !$#authors Baier, G.; Telford, D.; Giampa, L.; Coggeshall, K.M.; !1Baier-Bitterlich, G.; Isakov, N.; Altman, A. !$#journal J. Biol. Chem. (1993) 268:4997-5004 !$#title Molecular cloning and characterization of PKC theta, a novel !1member of the protein kinase C (PKC) gene family expressed !1predominantly in hematopoietic cells. !$#cross-references MUID:93186810; PMID:8444877 !$#accession A45416 !'##molecule_type mRNA !'##residues 1-706 ##label BAI !'##cross-references GB:L07032; NID:g189990; PIDN:AAA60101.1; !1PID:g558100 !'##experimental_source peripheral blood !'##note sequence extracted from NCBI backbone (NCBIN:126797, !1NCBIP:126798) REFERENCE A47160 !$#authors Chang, J.D.; Xu, Y.; Raychowdhury, M.K.; Ware, J.A. !$#journal J. Biol. Chem. (1993) 268:14208-14214 !$#title Molecular cloning and expression of a cDNA encoding a novel !1isoenzyme of protein kinase C (nPKC). A new member of the !1nPKC family expressed in skeletal muscle, megakaryoblastic !1cells, and platelets. !$#cross-references MUID:93300813; PMID:7686153 !$#accession A47160 !'##molecule_type mRNA !'##residues 1-329,'L',331-649,'T',651-700,'WSG' ##label CHA !'##cross-references GB:L01087; NID:g558098 GENETICS !$#gene GDB:PRKCQ; Hs.22071 !'##cross-references GDB:136263; OMIM:600448 !$#map_position 10p15-10p15 FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP !$#note activity is calcium-independent, phospholipid-dependent, and !1activated by diacylglycerol and by tumor-promoting phorbol !1esters; highest levels of expression are in hematopoietic !1tissues and skeletal muscle CLASSIFICATION #superfamily protein kinase C delta; protein kinase C !1zinc-binding repeat homology; protein kinase homology KEYWORDS ATP; autophosphorylation; duplication; phorbol ester !1binding; phospholipid binding; phosphotransferase; serine/ !1threonine-specific protein kinase; zinc FEATURE !$145-150 #region pseudophosphorylation motif\ !$160-209 #domain protein kinase C zinc-binding repeat homology !8#label KZ1\ !$232-281 #domain protein kinase C zinc-binding repeat homology !8#label KZ2\ !$378-634 #domain protein kinase homology #label KIN\ !$386-394 #region protein kinase ATP-binding motif\ !$160,190,193,209 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$173,176,198,201 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$232,262,265,281 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$245,248,270,273 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$409,428,504,506 #active_site Lys, Glu, Asp, Lys #status predicted SUMMARY #length 706 #molecular-weight 81864 #checksum 9002 SEQUENCE /// ENTRY A44500 #type complete TITLE protein kinase C (EC 2.7.1.-) theta - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Jun-1993 #sequence_revision 18-Nov-1994 #text_change 16-Jun-2000 ACCESSIONS A44500 REFERENCE A44500 !$#authors Osada, S.; Mizuno, K.; Saido, T.C.; Suzuki, K.; Kuroki, T.; !1Ohno, S. !$#journal Mol. Cell. Biol. (1992) 12:3930-3938 !$#title A new member of the protein kinase C family, nPKC theta, !1predominantly expressed in skeletal muscle. !$#cross-references MUID:92375061; PMID:1508194 !$#accession A44500 !'##molecule_type mRNA !'##residues 1-707 ##label OSA !'##cross-references GB:D11091; NID:g220573; PIDN:BAA01864.1; !1PID:g220574 !'##experimental_source brain !'##note sequence extracted from NCBI backbone (NCBIN:111692, !1NCBIP:111693) FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP !$#note activity is calcium-independent, phospholipid-dependent, and !1activated by diacylglycerol and by tumor-promoting phorbol !1esters; highest levels of expression are in hematopoietic !1tissues and skeletal muscle CLASSIFICATION #superfamily protein kinase C delta; protein kinase C !1zinc-binding repeat homology; protein kinase homology KEYWORDS ATP; autophosphorylation; duplication; phorbol ester !1binding; phospholipid binding; phosphotransferase; serine/ !1threonine-specific protein kinase; zinc FEATURE !$145-150 #region pseudophosphorylation motif\ !$160-209 #domain protein kinase C zinc-binding repeat homology !8#label KZ1\ !$232-281 #domain protein kinase C zinc-binding repeat homology !8#label KZ2\ !$378-634 #domain protein kinase homology #label KIN\ !$386-394 #region protein kinase ATP-binding motif\ !$160,190,193,209 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$173,176,198,201 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$232,262,265,281 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$245,248,270,273 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$409,428,504,506 #active_site Lys, Glu, Asp, Lys #status predicted SUMMARY #length 707 #molecular-weight 81572 #checksum 5415 SEQUENCE /// ENTRY S60117 #type complete TITLE protein kinase C (EC 2.7.1.-) TPA-1A - Caenorhabditis elegans CONTAINS protein kinase C TPA-1B ORGANISM #formal_name Caenorhabditis elegans DATE 19-Mar-1997 #sequence_revision 25-Apr-1997 #text_change 16-Jun-2000 ACCESSIONS S60117; T33398 REFERENCE S60117 !$#authors Sano, T.; Tabuse, Y.; Nishiwaki, K.; Miwa, J. !$#journal J. Mol. Biol. (1995) 251:477-485 !$#title The tpa-1 gene of Caenorhabditis elegans encodes two !1proteins similar to Ca(2+)-independent protein kinase Cs: !1evidence by complete genomic and complementary DNA sequences !1of the tpa-1 gene. !$#cross-references MUID:95387388; PMID:7658466 !$#accession S60117 !'##molecule_type DNA !'##residues 1-704 ##label SAN !'##cross-references EMBL:D49525; NID:g1217583; PIDN:BAA08470.1; !1PID:g1217584 REFERENCE Z21337 !$#authors Rohlfing, T. !$#submission submitted to the EMBL Data Library, July 1998 !$#description The sequence of C. elegans cosmid B0545. !$#accession T33398 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-704 ##label ROH !'##cross-references EMBL:AF078781; PIDN:AAC26916.1; GSPDB:GN00022; !1CESP:B0545.1a !'##experimental_source strain Bristol N2; clone B0545 GENETICS !$#gene tpa-1a; CESP:B0545.1a !$#map_position IV; 4 !$#introns 9/2; 45/1; 93/3; 128/1; 153/1; 226/3; 270/1; 446/3; 498/2; !1655/3 FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP !$#note activity is calcium-independent, phospholipid-dependent, and !1activated by diacylglycerol and by tumor-promoting phorbol !1esters CLASSIFICATION #superfamily protein kinase C delta; protein kinase C !1zinc-binding repeat homology; protein kinase homology KEYWORDS alternative splicing; ATP; duplication; phorbol ester !1binding; phospholipid binding; phosphotransferase; serine/ !1threonine-specific protein kinase; zinc FEATURE !$138-704 #product protein kinase C TPA-1B #status predicted !8#label MAT2\ !$151-156 #region pseudophosphorylation motif\ !$166-215 #domain protein kinase C zinc-binding repeat homology !8#label KZ1\ !$238-287 #domain protein kinase C zinc-binding repeat homology !8#label KZ2\ !$373-634 #domain protein kinase homology #label KIN\ !$381-389 #region protein kinase ATP-binding motif\ !$166,196,199,215 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$179,182,204,207 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$238,268,271,287 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$251,254,276,279 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$404,423,499,501 #active_site Lys, Glu, Asp, Lys #status predicted SUMMARY #length 704 #molecular-weight 80298 #checksum 7955 SEQUENCE /// ENTRY S28942 #type complete TITLE protein kinase C (EC 2.7.1.-) epsilon - human ORGANISM #formal_name Homo sapiens #common_name man DATE 13-Jan-1995 #sequence_revision 13-Jan-1995 #text_change 11-Jun-1999 ACCESSIONS S28942 REFERENCE S28942 !$#authors Basta, P.; Strickland, M.B.; Holmes, W.; Loomis, C.R.; !1Ballas, L.M.; Burns, D.J. !$#journal Biochim. Biophys. Acta (1992) 1132:154-160 !$#title Sequence and expression of human protein kinase C-epsilon. !$#cross-references MUID:93003318; PMID:1382605 !$#accession S28942 !'##status preliminary !'##molecule_type mRNA !'##residues 1-737 ##label BAS !'##cross-references EMBL:X65293; NID:g35494; PIDN:CAA46388.1; !1PID:g35495 COMMENT This is a calcium-independent, phospholipid-dependent, !1serine- and threonine-specific enzyme. It is activated by !1diacylglycerol produced in the cell membrane during !1signal-induced turnover of inositol phospholipids. This !1protein is a receptor for tumor-promoting phorbol esters, !1which can substitute for diacylglycerol in activating the !1enzyme. GENETICS !$#gene GDB:PRKCE !'##cross-references GDB:128039; OMIM:176975 !$#map_position 3pter-3qter FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP !$#note activity is calcium-independent, phospholipid-dependent, and !1activated by diacylglycerol and by tumor-promoting phorbol !1esters; expressed mainly in brain CLASSIFICATION #superfamily protein kinase C delta; protein kinase C !1zinc-binding repeat homology; protein kinase homology KEYWORDS ATP; duplication; phorbol ester binding; phospholipid !1binding; phosphotransferase; serine/threonine-specific !1protein kinase; zinc FEATURE !$156-161 #region pseudophosphorylation motif\ !$170-220 #domain protein kinase C zinc-binding repeat homology !8#label KZ1\ !$243-292 #domain protein kinase C zinc-binding repeat homology !8#label KZ2\ !$406-668 #domain protein kinase homology #label KIN\ !$414-422 #region protein kinase ATP-binding motif\ !$170,201,204,220 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$183,186,209,212 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$243,273,276,292 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$256,259,281,284 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$437,456,532,534 #active_site Lys, Glu, Asp, Lys #status predicted SUMMARY #length 737 #molecular-weight 83673 #checksum 9192 SEQUENCE /// ENTRY KIRBCE #type complete TITLE protein kinase C (EC 2.7.1.-) epsilon - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 21-Nov-1997 ACCESSIONS A29880 REFERENCE A29880 !$#authors Ohno, S.; Akita, Y.; Konno, Y.; Imajoh, S.; Suzuki, K. !$#journal Cell (1988) 53:731-741 !$#title A novel phorbol ester receptor/protein kinase, nPKC, !1distantly related to the protein kinase C family. !$#cross-references MUID:88223367; PMID:3370672 !$#accession A29880 !'##molecule_type mRNA !'##residues 1-736 ##label OHN !'##cross-references GB:M20014 FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP !$#note activity is calcium-independent, phospholipid-dependent, and !1activated by diacylglycerol and by tumor-promoting phorbol !1esters; expressed mainly in brain CLASSIFICATION #superfamily protein kinase C delta; protein kinase C !1zinc-binding repeat homology; protein kinase homology KEYWORDS ATP; autophosphorylation; duplication; phorbol ester !1binding; phospholipid binding; phosphoprotein; !1phosphotransferase; serine/threonine-specific protein !1kinase; zinc FEATURE !$156-161 #region pseudophosphorylation motif\ !$170-220 #domain protein kinase C zinc-binding repeat homology !8#label KZ1\ !$243-292 #domain protein kinase C zinc-binding repeat homology !8#label KZ2\ !$405-667 #domain protein kinase homology #label KIN\ !$413-421 #region protein kinase ATP-binding motif\ !$170,201,204,220 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$183,186,209,212 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$243,273,276,292 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$256,259,281,284 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$436,455,531,533 #active_site Lys, Glu, Asp, Lys #status predicted\ !$702,709 #binding_site phosphate (Thr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 736 #molecular-weight 83519 #checksum 5224 SEQUENCE /// ENTRY KIRTCE #type complete TITLE protein kinase C (EC 2.7.1.-) epsilon - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 11-Jun-1999 ACCESSIONS B28163; B26408; S00216 REFERENCE A92717 !$#authors Ono, Y.; Fujii, T.; Ogita, K.; Kikkawa, U.; Igarashi, K.; !1Nishizuka, Y. !$#journal J. Biol. Chem. (1988) 263:6927-6932 !$#title The structure, expression, and properties of additional !1members of the protein kinase C family. !$#cross-references MUID:88198270; PMID:2834397 !$#accession B28163 !'##molecule_type DNA !'##residues 1-737 ##label ONO !'##cross-references GB:M18331; NID:g206182; PIDN:AAA41872.1; !1PID:g206183 REFERENCE A94145 !$#authors Housey, G.M.; O'Brian, C.A.; Johnson, M.D.; Kirschmeier, P.; !1Weinstein, I.B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:1065-1069 !$#title Isolation of cDNA clones encoding protein kinase C: evidence !1for a protein kinase C-related gene family. !$#cross-references MUID:87147193; PMID:3469647 !$#accession B26408 !'##molecule_type mRNA !'##residues 397-447,'GQRGLHDDREEDFGSGAET',467,'LSNPTLLLLPDQGPPLLRQ', !1487-545,'C',547-636 ##label HOU !'##cross-references GB:M15523; NID:g206192; PIDN:AAA41877.1; !1PID:g206193 COMMENT Protein kinase C epsilon and epsilon' appear to be encoded !1by the same gene and differ from each other only at their !1amino ends. FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP !$#note activity is calcium-independent, phospholipid-dependent, and !1activated by diacylglycerol and by tumor-promoting phorbol !1esters; expressed mainly in brain CLASSIFICATION #superfamily protein kinase C delta; protein kinase C !1zinc-binding repeat homology; protein kinase homology KEYWORDS alternative splicing; ATP; autophosphorylation; duplication; !1phorbol ester binding; phospholipid binding; phosphoprotein; !1phosphotransferase; serine/threonine-specific protein !1kinase; zinc FEATURE !$156-161 #region pseudophosphorylation motif\ !$170-220 #domain protein kinase C zinc-binding repeat homology !8#label KZ1\ !$243-292 #domain protein kinase C zinc-binding repeat homology !8#label KZ2\ !$406-668 #domain protein kinase homology #label KIN\ !$414-422 #region protein kinase ATP-binding motif\ !$170,201,204,220 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$183,186,209,212 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$243,273,276,292 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$256,259,281,284 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$437,456,532,534 #active_site Lys, Glu, Asp, Lys #status predicted\ !$703,710 #binding_site phosphate (Thr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 737 #molecular-weight 83478 #checksum 8125 SEQUENCE /// ENTRY KIMSCE #type complete TITLE protein kinase C (EC 2.7.1.-) epsilon - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 21-Nov-1997 ACCESSIONS S02270 REFERENCE S02270 !$#authors Schaap, D.; Parker, P.J.; Bristol, A.; Kriz, R.; Knopf, J. !$#journal FEBS Lett. (1989) 243:351-357 !$#title Unique substrate specificity and regulatory properties of !1PKC-epsilon: a rationale for diversity. !$#cross-references MUID:89137541; PMID:2917656 !$#accession S02270 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type mRNA !'##residues 1-737 ##label SCH FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP !$#note activity is calcium-independent, phospholipid-dependent, and !1activated by diacylglycerol and by tumor-promoting phorbol !1esters; expressed mainly in brain CLASSIFICATION #superfamily protein kinase C delta; protein kinase C !1zinc-binding repeat homology; protein kinase homology KEYWORDS ATP; autophosphorylation; duplication; phorbol ester !1binding; phospholipid binding; phosphoprotein; !1phosphotransferase; serine/threonine-specific protein !1kinase; zinc FEATURE !$156-161 #region pseudophosphorylation motif\ !$170-220 #domain protein kinase C zinc-binding repeat homology !8#label KZ1\ !$243-292 #domain protein kinase C zinc-binding repeat homology !8#label KZ2\ !$406-668 #domain protein kinase homology #label KIN\ !$414-422 #region protein kinase ATP-binding motif\ !$170,201,204,220 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$183,186,209,212 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$243,273,276,292 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$256,259,281,284 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$437,456,532,534 #active_site Lys, Glu, Asp, Lys #status predicted\ !$703,710 #binding_site phosphate (Thr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 737 #molecular-weight 83560 #checksum 6835 SEQUENCE /// ENTRY A39666 #type complete TITLE protein kinase C (EC 2.7.1.-) eta - human ALTERNATE_NAMES protein kinase C PKC-L ORGANISM #formal_name Homo sapiens #common_name man DATE 08-Nov-1991 #sequence_revision 11-Apr-1997 #text_change 21-Jul-2000 ACCESSIONS A39666; A42131; S65018 REFERENCE A39666 !$#authors Bacher, N.; Zisman, Y.; Berent, E.; Livneh, E. !$#journal Mol. Cell. Biol. (1991) 11:126-133 !$#title Isolation and characterization of PKC-L, a new member of the !1protein kinase C-related gene family specifically expressed !1in lung, skin, and heart. !$#cross-references MUID:91094824; PMID:1986216 !$#accession A39666 !'##molecule_type mRNA !'##residues 1-276,'YVNECAY','SMSSERG',292-296,'MRWN',301,'PRP','GRD', !1309-682 ##label BA2 !'##cross-references GB:M55284; NID:g189988; PIDN:AAA60100.1; !1PID:g189989 !'##note the cross-reference is to the corrected sequence REFERENCE A42131 !$#authors Bacher, N.; Zisman, Y.; Berent, E.; Livneh, E. !$#journal Mol. Cell. Biol. (1992) 12:1404 !$#title Isolation and characterization of PKC-L, a new member of the !1protein kinase C-related gene family specifically expressed !1in lung, skin, and heart. !$#cross-references MUID:92186874; PMID:1545821 !$#contents erratum !$#accession A42131 !'##molecule_type mRNA !'##residues 277-308 ##label BA3 !'##cross-references GB:M55284 !'##note this report is a revision to reference A39666 REFERENCE S51020 !$#authors Palmer, R.H.; Ridden, J.; Parker, P.J. !$#journal FEBS Lett. (1994) 356:5-8 !$#title Identification of multiple, novel, protein kinase C-related !1gene products. !$#cross-references MUID:95080426; PMID:7988719 !$#accession S65018 !'##status preliminary !'##molecule_type mRNA !'##residues 437-470,'E',472-538 ##label PAL !'##cross-references EMBL:S74620; NID:g786485; PIDN:AAB32724.1; !1PID:g786486 GENETICS !$#gene GDB:PRKCH; PKC-L; PRKCL !'##cross-references GDB:129009 !$#map_position 19q13.4-19q13.4 FUNCTION !$#description catalyzes protein phosphorylation at Ser or Thr residues !$#note activity is calcium-independent, phospholipid-dependent, and !1activated by diacylglycerol and by tumor-promoting phorbol !1esters; expressed in lung, skin, and heart CLASSIFICATION #superfamily protein kinase C delta; protein kinase C !1zinc-binding repeat homology; protein kinase homology KEYWORDS ATP; autophosphorylation; duplication; phorbol ester !1binding; phospholipid binding; phosphotransferase; serine/ !1threonine-specific protein kinase; zinc FEATURE !$157-162 #region pseudophosphorylation motif\ !$171-221 #domain protein kinase C zinc-binding repeat homology !8#label KZ1\ !$245-294 #domain protein kinase C zinc-binding repeat homology !8#label KZ2\ !$352-613 #domain protein kinase homology #label KIN\ !$360-368 #region protein kinase ATP-binding motif\ !$171,202,205,221 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$184,187,210,213 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$245,275,278,294 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$258,261,283,286 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$383,402,478,480 #active_site Lys, Glu, Asp, Lys #status predicted SUMMARY #length 682 #molecular-weight 77563 #checksum 5637 SEQUENCE /// ENTRY A23690 #type complete TITLE protein kinase (EC 2.7.1.37) eta - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 04-Oct-1991 #sequence_revision 04-Oct-1991 #text_change 16-Jun-2000 ACCESSIONS A23690 REFERENCE A23690 !$#authors Osada, S.; Mizuno, K.; Saido, T.C.; Akita, Y.; Suzuki, K.; !1Kuroki, T.; Ohno, S. !$#journal J. Biol. Chem. (1990) 265:22434-22440 !$#title A phorbol ester receptor/protein kinase, nPKC-eta, a new !1member of the protein kinase C family predominantly !1expressed in lung and skin. !$#cross-references MUID:91093089; PMID:2266135 !$#accession A23690 !'##molecule_type mRNA !'##residues 1-683 ##label OSA !'##cross-references GB:D90242; GB:J05703; NID:g220526; PIDN:BAA14288.1; !1PID:g220527 FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP !$#note activity is calcium-independent, phospholipid-dependent, and !1activated by diacylglycerol and by tumor-promoting phorbol !1esters; expressed mainly in lung and skin CLASSIFICATION #superfamily protein kinase C delta; protein kinase C !1zinc-binding repeat homology; protein kinase homology KEYWORDS ATP; autophosphorylation; duplication; phorbol ester !1binding; phospholipid binding; phosphotransferase; serine/ !1threonine-specific protein kinase; zinc FEATURE !$158-163 #region pseudophosphorylation motif\ !$172-222 #domain protein kinase C zinc-binding repeat homology !8#label KZ1\ !$246-295 #domain protein kinase C zinc-binding repeat homology !8#label KZ2\ !$353-614 #domain protein kinase homology #label KIN\ !$361-369 #region protein kinase ATP-binding motif\ !$172,203,206,222 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$185,188,211,214 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$246,276,279,295 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$259,262,284,287 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$384,403,479,481 #active_site Lys, Glu, Asp, Lys #status predicted SUMMARY #length 683 #molecular-weight 77973 #checksum 8355 SEQUENCE /// ENTRY S29478 #type complete TITLE protein kinase C (EC 2.7.1.-) eta - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 13-Jan-1995 #sequence_revision 13-Jan-1995 #text_change 11-Jun-1999 ACCESSIONS I60246; S29478 REFERENCE I60246 !$#authors Dekker, L.V.; Parker, P.J.; McIntyre, P. !$#journal FEBS Lett. (1992) 312:195-199 !$#title Biochemical properties of rat protein kinase C-eta expressed !1in COS cells. !$#cross-references MUID:93050193; PMID:1426252 !$#accession I60246 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-683 ##label RES !'##cross-references EMBL:X68400; NID:g56915; PIDN:CAA48466.1; !1PID:g56916 FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP !$#note activity is calcium-independent, phospholipid-dependent, and !1activated by diacylglycerol and by tumor-promoting phorbol !1esters CLASSIFICATION #superfamily protein kinase C delta; protein kinase C !1zinc-binding repeat homology; protein kinase homology KEYWORDS ATP; autophosphorylation; duplication; phorbol ester !1binding; phospholipid binding; phosphotransferase; serine/ !1threonine-specific protein kinase; zinc FEATURE !$158-163 #region pseudophosphorylation motif\ !$172-222 #domain protein kinase C zinc-binding repeat homology !8#label KZ1\ !$246-295 #domain protein kinase C zinc-binding repeat homology !8#label KZ2\ !$353-614 #domain protein kinase homology #label KIN\ !$361-369 #region protein kinase ATP-binding motif\ !$172,203,206,222 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$185,188,211,214 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$246,276,279,295 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$259,262,284,287 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$384,403,479,481 #active_site Lys, Glu, Asp, Lys #status predicted SUMMARY #length 683 #molecular-weight 77946 #checksum 9956 SEQUENCE /// ENTRY B32392 #type complete TITLE protein kinase C (EC 2.7.1.-) epsilon-related - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES protein kinase C 98F ORGANISM #formal_name Drosophila melanogaster DATE 22-Nov-1989 #sequence_revision 22-Nov-1989 #text_change 11-Jun-1999 ACCESSIONS B32392 REFERENCE A32392 !$#authors Schaeffer, E.; Smith, D.; Mardon, G.; Quinn, W.; Zuker, C. !$#journal Cell (1989) 57:403-412 !$#title Isolation and characterization of two new Drosophila protein !1kinase C genes, including one specifically expressed in !1photoreceptor cells. !$#cross-references MUID:89249302; PMID:2720775 !$#accession B32392 !'##molecule_type mRNA !'##residues 1-634 ##label SCH !'##cross-references GB:J04848; NID:g158128; PIDN:AAA28818.1; !1PID:g158129 GENETICS !$#gene FlyBase:Pkc98E !'##cross-references FlyBase:FBgn0003093 FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP !$#note activity is calcium-independent, phospholipid-dependent, and !1activated by diacylglycerol and by tumor-promoting phorbol !1esters CLASSIFICATION #superfamily protein kinase C delta; protein kinase C !1zinc-binding repeat homology; protein kinase homology KEYWORDS ATP; duplication; phorbol ester binding; phospholipid !1binding; phosphotransferase; serine/threonine-specific !1protein kinase; zinc FEATURE !$58-63 #region pseudophosphorylation motif\ !$72-121 #domain protein kinase C zinc-binding repeat homology !8#label KZ1\ !$147-196 #domain protein kinase C zinc-binding repeat homology !8#label KZ2\ !$301-560 #domain protein kinase homology #label KIN\ !$309-317 #region protein kinase ATP-binding motif\ !$72,102,105,121 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$85,88,110,113 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$147,177,180,196 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$160,163,185,188 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$332,351,427,429 #active_site Lys, Glu, Asp, Lys #status predicted SUMMARY #length 634 #molecular-weight 71156 #checksum 5190 SEQUENCE /// ENTRY A53530 #type complete TITLE protein kinase C (EC 2.7.1.-) epsilon-related - Caenorhabditis elegans ALTERNATE_NAMES protein kinase C PKC1B, neuronal ORGANISM #formal_name Caenorhabditis elegans DATE 06-Jan-1995 #sequence_revision 06-Jan-1995 #text_change 11-Jun-1999 ACCESSIONS A53530 REFERENCE A53530 !$#authors Land, M.; Islas-Trejo, A.; Freedman, J.H.; Rubin, C.S. !$#journal J. Biol. Chem. (1994) 269:9234-9244 !$#title Structure and expression of a novel, neuronal protein kinase !1C (PKC1B) from Caenorhabditis elegans. PKC1B is expressed !1selectively in neurons that receive, transmit, and process !1environmental signals. !$#cross-references MUID:94179345; PMID:8132661 !$#accession A53530 !'##molecule_type mRNA !'##residues 1-707 ##label LAN !'##cross-references GB:U00181; NID:g484065; PIDN:AAA18259.1; !1PID:g392435 GENETICS !$#gene kin-13 !$#map_position V !$#note located near myo-3, col-1, and CPROT/2 genes FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP !$#note activity is calcium-independent, phospholipid-dependent, and !1activated by diacylglycerol and by tumor-promoting phorbol !1esters CLASSIFICATION #superfamily protein kinase C delta; protein kinase C !1zinc-binding repeat homology; protein kinase homology KEYWORDS ATP; duplication; phorbol ester binding; phospholipid !1binding; phosphotransferase; serine/threonine-specific !1protein kinase; zinc FEATURE !$157-162 #region pseudophosphorylation motif\ !$171-220 #domain protein kinase C zinc-binding repeat homology !8#label KZ1\ !$249-298 #domain protein kinase C zinc-binding repeat homology !8#label KZ2\ !$376-638 #domain protein kinase homology #label KIN\ !$384-392 #region protein kinase ATP-binding motif\ !$171,201,204,220 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$184,187,209,212 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$249,279,282,298 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$262,265,287,290 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$407,426,502,504 #active_site Lys, Glu, Asp, Lys #status predicted SUMMARY #length 707 #molecular-weight 80121 #checksum 9414 SEQUENCE /// ENTRY A53215 #type complete TITLE protein kinase C (EC 2.7.1.-) mu precursor - human ALTERNATE_NAMES protein kinase D ORGANISM #formal_name Homo sapiens #common_name man DATE 19-Oct-1995 #sequence_revision 19-Oct-1995 #text_change 11-Jun-1999 ACCESSIONS A53215; S40279 REFERENCE A53215 !$#authors Johannes, F.J.; Prestle, J.; Eis, S.; Oberhagemann, P.; !1Pfizenmaier, K. !$#journal J. Biol. Chem. (1994) 269:6140-6148 !$#title PKCmu is a novel, atypical member of the protein kinase C !1family. !$#cross-references MUID:94164979; PMID:8119958 !$#accession A53215 !'##molecule_type mRNA !'##residues 1-912 ##label JOH !'##cross-references EMBL:X75756; NID:g438372; PIDN:CAA53384.1; !1PID:g438373 GENETICS !$#gene GDB:PRKCM; Hs.2891; PKCM !'##cross-references GDB:330794 !$#map_position 21pter-21qter FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP !$#note expressed at low levels in a variety of tissues; !1phosphorylates a 30K protein at serine residues; in contrast !1to the closely related mouse enzyme, this protein appears !1not to bind phorbol esters CLASSIFICATION #superfamily protein kinase C mu; protein kinase C !1zinc-binding repeat homology; protein kinase homology KEYWORDS ATP; autophosphorylation; duplication; phospholipid binding; !1phosphotransferase; serine/threonine-specific protein !1kinase; zinc FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-912 #product protein kinase mu #status predicted #label !8MAT\ !$147-196 #domain protein kinase C zinc-binding repeat homology !8#label KZ1\ !$271-320 #domain protein kinase C zinc-binding repeat homology !8#label KZ2\ !$581-839 #domain protein kinase homology #label KIN\ !$589-597 #region protein kinase ATP-binding motif\ !$612,630,706,708 #active_site Lys, Glu, Asp, Lys #status predicted SUMMARY #length 912 #molecular-weight 101888 #checksum 8566 SEQUENCE /// ENTRY I48719 #type complete TITLE protein kinase C (EC 2.7.1.-) mu precursor - mouse ALTERNATE_NAMES protein kinase D ORGANISM #formal_name Mus musculus #common_name house mouse DATE 02-Jul-1996 #sequence_revision 02-Jul-1996 #text_change 11-Jun-1999 ACCESSIONS I48719 REFERENCE I48719 !$#authors Valverde, A.M.; Sinnett-Smith, J.; Van Lint, J.; Rozengurt, !1E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1994) 91:8572-8576 !$#title Molecular cloning and characterization of protein kinase D: !1a target for diacylglycerol and phorbol esters with a !1distinctive catalytic domain. !$#cross-references MUID:94359973; PMID:8078925 !$#accession I48719 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-918 ##label RES !'##cross-references EMBL:Z34524; NID:g520877; PIDN:CAA84283.1; !1PID:g520878 FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP !$#note expressed at low levels in a variety of tissues; !1phosphorylates the peptide syntide 2, a substrate for !1calmodulin-dependent protein kinases, only at the serine !1residue; in contrast to the closely related human enzyme, !1this protein is reported to bind phorbol esters CLASSIFICATION #superfamily protein kinase C mu; protein kinase C !1zinc-binding repeat homology; protein kinase homology KEYWORDS ATP; autophosphorylation; duplication; phorbol ester !1binding; phospholipid binding; phosphotransferase; serine/ !1threonine-specific protein kinase; zinc FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-918 #product protein kinase mu #status predicted #label !8MAT\ !$145-194 #domain protein kinase C zinc-binding repeat homology !8#label KZ1\ !$277-326 #domain protein kinase C zinc-binding repeat homology !8#label KZ2\ !$587-845 #domain protein kinase homology #label KIN\ !$595-603 #region protein kinase ATP-binding motif\ !$618,636,712,714 #active_site Lys, Glu, Asp, Lys #status predicted SUMMARY #length 918 #molecular-weight 102067 #checksum 6546 SEQUENCE /// ENTRY S47220 #type complete TITLE protein kinase C (EC 2.7.1.-) PKC1 - yeast (Candida albicans) ORGANISM #formal_name Candida albicans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S47220; S71641 REFERENCE S47220 !$#authors Paravicini, G.; Mendoza, A.; Autoussou, B.; Cooper, M.; !1Losberger, C.; Paytou, M. !$#submission submitted to the EMBL Data Library, August 1994 !$#description The Candida albicans PKC1 gene encodes a protein kinase C !1(PKC) homolog necessary for osmotic stability but not !1dimorphism. !$#accession S47220 !'##molecule_type DNA !'##residues 1-1097 ##label PAR !'##cross-references EMBL:X81142; NID:g535094; PIDN:CAA57048.1; !1PID:g832908 !'##experimental_source strain 10261 REFERENCE S71641 !$#authors Paravicini, G.; Mendoza, A.; Antonsson, B.; Cooper, M.; !1Losberger, C.; Payton, M.A. !$#journal Yeast (1996) 12:741-756 !$#title The Candida albicans PKC1 gene encodes a protein kinase C !1homolog necessary for cellular integrity but not dimorphism. !$#cross-references MUID:96408767; PMID:8813761 !$#accession S71641 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 396-531;764-1097 ##label PAW !'##cross-references EMBL:X81142 GENETICS !$#gene PKC1 CLASSIFICATION #superfamily yeast protein kinase C; protein kinase C !1zinc-binding repeat homology; protein kinase homology KEYWORDS ATP; duplication; phospholipid binding; phosphotransferase; !1serine/threonine-specific protein kinase; zinc FEATURE !$416-462 #domain protein kinase C zinc-binding repeat homology !8#label KZ1\ !$481-530 #domain protein kinase C zinc-binding repeat homology !8#label KZ2\ !$768-1029 #domain protein kinase homology #label KIN\ !$776-784 #region protein kinase ATP-binding motif\ !$799,895 #active_site Lys, Asp #status predicted SUMMARY #length 1097 #molecular-weight 125390 #checksum 1392 SEQUENCE /// ENTRY S45390 #type complete TITLE protein kinase C (EC 2.7.1.-) PKC1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YBL0807; protein YBL105c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-Nov-1999 ACCESSIONS S45390; S45848; S12305; S59187 REFERENCE S45387 !$#authors Obermaier, B.; Gassenhuber, J.; Piravandi, E.; Domdey, H. !$#submission submitted to the EMBL Data Library, May 1994 !$#description Sequence analysis of a 78,6 kb segment of the left end of !1Saccaromyces cerevisiae chromosome II. !$#accession S45390 !'##molecule_type DNA !'##residues 1-1151 ##label OBE !'##cross-references EMBL:X79489; NID:g496661; PIDN:CAA55990.1; !1PID:g496664 !'##experimental_source strain S288C REFERENCE S45816 !$#authors Domdey, H.; Gassenhuber, H.; Obermaier, B.; Piravandi, E. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S45848 !'##molecule_type DNA !'##residues 1-1151 ##label DOM !'##cross-references EMBL:Z35866; NID:g536177; PIDN:CAA84932.1; !1PID:g536178; GSPDB:GN00002; MIPS:YBL105c REFERENCE S12305 !$#authors Levin, D.E.; Fields, F.O.; Kunisawa, R.; Bishop, J.M.; !1Thorner, J. !$#journal Cell (1990) 62:213-224 !$#title A candidate protein kinase C gene, PKC1, is required for the !1S. cerevisiae cell cycle. !$#cross-references MUID:90322419; PMID:2196995 !$#accession S12305 !'##molecule_type DNA !'##residues 1-80,'C',82-243,'S',245-605,'E',607-622,'P',624-788,'A', !1790-1151 ##label LEV !'##cross-references EMBL:M32491; NID:g172176; PIDN:AAA34878.1; !1PID:g172177 !'##experimental_source strain EG123 REFERENCE S59184 !$#authors Obermaier, B.; Gassenhuber, J.; Piravandi, E.; Domdey, H. !$#journal Yeast (1995) 11:1103-1112 !$#title Sequence analysis of a 78.6 kb segment of the left end of !1Saccharomyces cerevisiae chromosome II. !$#cross-references MUID:96076635; PMID:7502586 !$#accession S59187 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1151 ##label OBW !'##cross-references EMBL:X79489; NID:g496661; PIDN:CAA55990.1; !1PID:g496664 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1May 1994 GENETICS !$#gene SGD:PKC1; MIPS:YBL105c !'##cross-references SGD:S0000201; MIPS:YBL105c !$#map_position 2L FUNCTION !$#description phosphotransferase; serine/threonine-specific protein kinase !$#note cells depleted of PKC1 product arrest cell division at a !1point subsequent to DNA replication, but prior to mitosis CLASSIFICATION #superfamily yeast protein kinase C; protein kinase C !1zinc-binding repeat homology; protein kinase homology KEYWORDS ATP; cell cycle control; phosphotransferase; serine/ !1threonine-specific protein kinase; zinc FEATURE !$415-461 #domain protein kinase C zinc-binding repeat homology !8#label KZ1\ !$482-531 #domain protein kinase C zinc-binding repeat homology !8#label KZ2\ !$822-1083 #domain protein kinase homology #label KIN\ !$830-838 #region protein kinase ATP-binding motif\ !$853,949 #active_site Lys, Asp #status predicted SUMMARY #length 1151 #molecular-weight 131518 #checksum 7224 SEQUENCE /// ENTRY S61917 #type complete TITLE protein kinase C (EC 2.7.1.-) PKCA - Aspergillus niger ORGANISM #formal_name Aspergillus niger DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S61917 REFERENCE S61917 !$#authors Morawetz, R.; Lendenfeld, T.; Mischak, H.; Muehlbauer, M.; !1Gruber, F.; Goodnight, J.; de Graaff, L.H.; Visser, J.; !1Mushinski, J.F.; Kubicek, C.P. !$#journal Mol. Gen. Genet. (1996) 250:17-28 !$#title Cloning and characterisation of genes (pkc1 and pkcA) !1encoding protein kinase C homologues from Trichoderma reesei !1and Aspergillus niger. !$#cross-references MUID:96158841; PMID:8569684 !$#accession S61917 !'##status preliminary; nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-1096 ##label MOR !'##cross-references EMBL:U10549; NID:g507899; PIDN:AAA97433.1; !1PID:g507900 GENETICS !$#gene pkcA !$#introns 145/1; 234/1; 428/1; 560/1; 698/1; 874/2; 941/3; 1077/1 CLASSIFICATION #superfamily yeast protein kinase C; protein kinase C !1zinc-binding repeat homology; protein kinase homology KEYWORDS ATP; duplication; phospholipid binding; phosphotransferase; !1serine/threonine-specific protein kinase; zinc FEATURE !$460-507 #domain protein kinase C zinc-binding repeat homology !8#label KZ1\ !$528-577 #domain protein kinase C zinc-binding repeat homology !8#label KZ2\ !$769-1030 #domain protein kinase homology #label KIN\ !$777-785 #region protein kinase ATP-binding motif SUMMARY #length 1096 #molecular-weight 122234 #checksum 9998 SEQUENCE /// ENTRY S61918 #type complete TITLE protein kinase C (EC 2.7.1.-) PKC1 - fungus (Trichoderma reesei) ORGANISM #formal_name Trichoderma reesei DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S61918 REFERENCE S61917 !$#authors Morawetz, R.; Lendenfeld, T.; Mischak, H.; Muehlbauer, M.; !1Gruber, F.; Goodnight, J.; de Graaff, L.H.; Visser, J.; !1Mushinski, J.F.; Kubicek, C.P. !$#journal Mol. Gen. Genet. (1996) 250:17-28 !$#title Cloning and characterisation of genes (pkc1 and pkcA) !1encoding protein kinase C homologues from Trichoderma reesei !1and Aspergillus niger. !$#cross-references MUID:96158841; PMID:8569684 !$#accession S61918 !'##status preliminary; nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-1139 ##label MOR !'##cross-references EMBL:U10016; NID:g501074; PIDN:AAA97432.1; !1PID:g501075 GENETICS !$#gene pkc1 !$#introns 139/1; 228/1; 555/1; 917/2; 984/3; 1120/1 CLASSIFICATION #superfamily yeast protein kinase C; protein kinase C !1zinc-binding repeat homology; protein kinase homology KEYWORDS ATP; duplication; phospholipid binding; phosphotransferase; !1serine/threonine-specific protein kinase; zinc FEATURE !$455-502 #domain protein kinase C zinc-binding repeat homology !8#label KZ1\ !$523-572 #domain protein kinase C zinc-binding repeat homology !8#label KZ2\ !$812-1073 #domain protein kinase homology #label KIN\ !$820-828 #region protein kinase ATP-binding motif SUMMARY #length 1139 #molecular-weight 126054 #checksum 3417 SEQUENCE /// ENTRY A46079 #type complete TITLE protein kinase C (EC 2.7.1.-) pck2 - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES pombe C-kinase 2 ORGANISM #formal_name Schizosaccharomyces pombe DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A46079; S35363; S39843; T39384 REFERENCE A46079 !$#authors Mazzei, G.J.; Schmid, E.M.; Knowles, J.K.; Payton, M.A.; !1Maundrell, K.G. !$#journal J. Biol. Chem. (1993) 268:7401-7406 !$#title A Ca(2+)-independent protein kinase C from fission yeast. !$#cross-references MUID:93216684; PMID:8463273 !$#accession A46079 !'##status preliminary !'##molecule_type DNA !'##residues 1-1016 ##label MAZ !'##cross-references GB:L07637; NID:g173426; PIDN:AAA35323.1; !1PID:g173427 !'##note sequence extracted from NCBI backbone (NCBIN:129017, !1NCBIP:129018) REFERENCE S35362 !$#authors Toda, T.; Shimanuki, M.; Yanagida, M. !$#journal EMBO J. (1993) 12:1987-1995 !$#title Two novel protein kinase C-related genes of fission yeast !1are essential for cell viability and implicated in cell !1shape control. !$#cross-references MUID:93259141; PMID:8491190 !$#accession S35363 !'##molecule_type DNA !'##residues 1-1016 ##label TOD !'##cross-references EMBL:D14338 REFERENCE S39843 !$#authors Toda, T.; Shimanuki, M.; Yanagida, M. !$#submission submitted to the EMBL Data Library, February 1993 !$#accession S39843 !'##molecule_type DNA !'##residues 1-151,'V',153-1016 ##label TO2 !'##cross-references EMBL:D14338; NID:g303940; PIDN:BAA03268.1; !1PID:g303941 REFERENCE Z21850 !$#authors Lyne, M.; Rajandream, M.A.; Barrell, B.G.; Xiang, Z.; Aves, !1S. !$#submission submitted to the EMBL Data Library, January 1999 !$#accession T39384 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-1016 ##label LYN !'##cross-references EMBL:AL035085; PIDN:CAA22678.1; GSPDB:GN00067; !1SPDB:SPBC12D12.04c !'##experimental_source strain 972h-; cosmid c12D12 GENETICS !$#gene pck2 !$#map_position 2 CLASSIFICATION #superfamily yeast protein kinase C; protein kinase C !1zinc-binding repeat homology; protein kinase homology KEYWORDS ATP; duplication; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$406-453 #domain protein kinase C zinc-binding repeat homology !8#label KZ1\ !$474-523 #domain protein kinase C zinc-binding repeat homology !8#label KZ2\ !$681-942 #domain protein kinase homology #label KIN\ !$689-697 #region protein kinase ATP-binding motif SUMMARY #length 1016 #molecular-weight 116004 #checksum 9827 SEQUENCE /// ENTRY S35362 #type complete TITLE protein kinase C (EC 2.7.1.-) pck1 - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES pombe C-kinase 1 ORGANISM #formal_name Schizosaccharomyces pombe DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 06-Oct-2000 ACCESSIONS S35362; T37866; T38203 REFERENCE S35362 !$#authors Toda, T.; Shimanuki, M.; Yanagida, M. !$#journal EMBO J. (1993) 12:1987-1995 !$#title Two novel protein kinase C-related genes of fission yeast !1are essential for cell viability and implicated in cell !1shape control. !$#cross-references MUID:93259141; PMID:8491190 !$#accession S35362 !'##molecule_type DNA !'##residues 1-988 ##label TOD !'##cross-references EMBL:D14337; NID:g303938; PIDN:BAA03267.1; !1PID:g303939 REFERENCE Z21750 !$#authors Devlin, K.; Churcher, C.M.; Barrell, B.G.; Rajandream, M.A.; !1Walsh, S.V. !$#submission submitted to the EMBL Data Library, February 1996 !$#accession T37866 !'##molecule_type DNA !'##residues 93-988 ##label DEV !'##cross-references EMBL:Z69795; PIDN:CAA93697.1; GSPDB:GN00066; !1SPDB:SPAC17G8.14c REFERENCE Z21778 !$#authors Grishchuk, K.; McIntosh, J.R.; Devlin, K.; Churcher, C.; !1Barrell, B.G.; Rajandream, M.A.; Walsh, S.V. !$#submission submitted to the EMBL Data Library, February 1996 !$#accession T38203 !'##molecule_type DNA !'##residues 1-26,'AMVASTKNP',36-137 ##label GRI !'##cross-references EMBL:Z69730; PIDN:CAA93602.1; GSPDB:GN00066; !1SPDB:SPAC22H10.01c !'##experimental_source strain 972h-; cosmid c22H10 GENETICS !$#gene pck1 !$#map_position 1L !$#introns 767/2; 834/3; 897/3; 959/1 CLASSIFICATION #superfamily yeast protein kinase C; protein kinase C !1zinc-binding repeat homology; protein kinase homology KEYWORDS ATP; duplication; phospholipid binding; phosphotransferase; !1serine/threonine-specific protein kinase; zinc FEATURE !$414-461 #domain protein kinase C zinc-binding repeat homology !8#label KZ1\ !$481-530 #domain protein kinase C zinc-binding repeat homology !8#label KZ2\ !$662-923 #domain protein kinase homology #label KIN\ !$670-678 #region protein kinase ATP-binding motif SUMMARY #length 988 #molecular-weight 111804 #checksum 723 SEQUENCE /// ENTRY A30314 #type complete TITLE protein kinase C (EC 2.7.1.-) zeta - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A30314; C28163; S00217 REFERENCE A30314 !$#authors Ono, Y.; Fujii, T.; Ogita, K.; Kikkawa, U.; Igarashi, K.; !1Nishizuka, Y. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:3099-3103 !$#title Protein kinase C zeta-subspecies from rat brain: its !1structure, expression, and properties. !$#cross-references MUID:89240683; PMID:2470089 !$#accession A30314 !'##status preliminary !'##molecule_type mRNA !'##residues 1-592 ##label ONO !'##cross-references GB:J04532; NID:g206353; PIDN:AAA41934.1; !1PID:g206354 REFERENCE A92717 !$#authors Ono, Y.; Fujii, T.; Ogita, K.; Kikkawa, U.; Igarashi, K.; !1Nishizuka, Y. !$#journal J. Biol. Chem. (1988) 263:6927-6932 !$#title The structure, expression, and properties of additional !1members of the protein kinase C family. !$#cross-references MUID:88198270; PMID:2834397 !$#accession C28163 !'##molecule_type DNA !'##residues 101,'FRAEEAAEKAE',113-592 ##label ON3 !'##cross-references GB:M18332; NID:g206194; PIDN:AAA41878.1; !1PID:g206195; GB:J03204 REFERENCE S00215 !$#authors Ono, Y.; Fujii, T.; Ogita, K.; Kikkawa, U.; Igarashi, K.; !1Nishizuka, Y. !$#journal FEBS Lett. (1987) 226:125-128 !$#title Identification of three additional members of rat protein !1kinase C family: delta-, epsilon- and zeta-subspecies. !$#cross-references MUID:88083621; PMID:3691811 !$#accession S00217 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 101,'FRAEEAAEKAE',113-180 ##label ON2 CLASSIFICATION #superfamily protein kinase C zeta; protein kinase C !1zinc-binding repeat homology; protein kinase homology KEYWORDS ATP; phorbol ester binding; phosphotransferase; serine/ !1threonine-specific protein kinase; zinc FEATURE !$131-180 #domain protein kinase C zinc-binding repeat homology !8#label KZ1\ !$250-518 #domain protein kinase homology #label KIN\ !$258-266 #region protein kinase ATP-binding motif\ !$281 #active_site Lys #status predicted SUMMARY #length 592 #molecular-weight 67733 #checksum 2914 SEQUENCE /// ENTRY JC1480 #type complete TITLE protein kinase C (EC 2.7.1.-) zeta - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 05-May-2000 ACCESSIONS JC1480 REFERENCE JC1480 !$#authors Goodnight, J.; Kazanietz, M.G.; Blumberg, P.M.; Mushinski, !1J.F.; Mischak, H. !$#journal Gene (1992) 122:305-311 !$#title The cDNA sequence, expression pattern and protein !1characteristics of mouse protein kinase C-zeta. !$#cross-references MUID:93138400; PMID:1487145 !$#accession JC1480 !'##molecule_type mRNA !'##residues 1-592 ##label GOO !'##cross-references GB:M94632; NID:g200498; PIDN:AAA39983.1; !1PID:g200499 !'##experimental_source brain CLASSIFICATION #superfamily protein kinase C zeta; protein kinase C !1zinc-binding repeat homology; protein kinase homology KEYWORDS ATP; phorbol ester binding; phosphotransferase; serine/ !1threonine-specific protein kinase; zinc FEATURE !$131-180 #domain protein kinase C zinc-binding repeat homology !8#label KZ1\ !$250-518 #domain protein kinase homology #label KIN\ !$258-266 #region protein kinase ATP-binding motif\ !$281 #active_site Lys #status predicted SUMMARY #length 592 #molecular-weight 67624 #checksum 3018 SEQUENCE /// ENTRY TVHUF6 #type complete TITLE protein kinase raf-1 (EC 2.7.1.-) - human ALTERNATE_NAMES kinase-related transforming protein raf-1; raf-1 proto-oncogene protein-serine/threonine kinase CONTAINS protein kinase (EC 2.7.1.37) ORGANISM #formal_name Homo sapiens #common_name man DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 11-Jun-1999 ACCESSIONS A00637; I57580 REFERENCE A00637 !$#authors Bonner, T.I.; Oppermann, H.; Seeburg, P.; Kerby, S.B.; !1Gunnell, M.A.; Young, A.C.; Rapp, U.R. !$#journal Nucleic Acids Res. (1986) 14:1009-1015 !$#title The complete coding sequence of the human raf oncogene and !1the corresponding structure of the c-raf-1 gene. !$#cross-references MUID:86120351; PMID:3003687 !$#accession A00637 !'##molecule_type mRNA !'##residues 1-648 ##label BON1 !'##cross-references GB:X03484; NID:g35841; PIDN:CAA27204.1; PID:g35842 REFERENCE I57580 !$#authors Bonner, T.I.; Kerby, S.B.; Sutrave, P.; Gunnell, M.A.; Mark, !1G.; Rapp, U.R. !$#journal Mol. Cell. Biol. (1985) 5:1400-1407 !$#title Structure and biological activity of human homologs of the !1raf/mil oncogene. !$#cross-references MUID:85295973; PMID:2993863 !$#accession I57580 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 228-239,'L',241-541,'I',543-648 ##label BON2 !'##cross-references GB:L00212; NID:g190837; PIDN:AAA60247.1; !1PID:g496091 REFERENCE A43089 !$#authors Morrison, D.K.; Heidecker, G.; Rapp, U.R.; Copeland, T.D. !$#journal J. Biol. Chem. (1993) 268:17309-17316 !$#title Identification of the major phosphorylation sites of the !1Raf-1 kinase. !$#cross-references MUID:93352516; PMID:8349614 !$#contents annotation; phosphorylation sites !$#note expression is ubiquitous in mammalian tissues that have been !1studied COMMENT After phosphorylation and activation by protein kinase C and !1other kinases, this kinase is responsible for activating MAP !1kinase kinase (see PIR:A45100 and PIR:A46723). GENETICS !$#gene GDB:RAF1 !'##cross-references GDB:119546; OMIM:164760 !$#map_position 3p25-3p25 !$#introns 278/3; 288/1; 330/3; 370/1; 398/2; 457/2; 473/1; 512/3; 556/ !13; 601/3 !$#note the list of introns is incomplete FUNCTION !$#description catalyzes the formation of specific !1peptidyl-threonine-phosphate and peptidyl-serine-phosphate !1residues in MAP kinase kinase using ATP !$#pathway MAP kinase cascade CLASSIFICATION #superfamily protein kinase A-raf; protein kinase C !1zinc-binding repeat homology; protein kinase homology KEYWORDS ATP; autophosphorylation; phosphoprotein; !1phosphotransferase; proto-oncogene; serine/ !1threonine-specific protein kinase; signal transduction; !1transforming protein; zinc FEATURE !$139-184 #domain protein kinase C zinc-binding repeat homology !8#label KZN\ !$347-613 #domain protein kinase homology #label KIN\ !$355-363 #region protein kinase ATP-binding motif\ !$43,621 #binding_site phosphate (Ser) (covalent) #status !8experimental\ !$139,165,168,184 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$152,155,173,176 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$259 #binding_site phosphate (Ser) (covalent) (by protein !8kinase C) #status experimental\ !$268 #binding_site phosphate (Thr) (covalent) (by !8autophosphorylation) #status experimental\ !$375 #active_site Lys #status predicted\ !$499 #binding_site phosphate (Ser) (covalent) (by protein !8kinase C) #status predicted SUMMARY #length 648 #molecular-weight 73051 #checksum 680 SEQUENCE /// ENTRY TVRTRF #type complete TITLE protein kinase raf-1 (EC 2.7.1.-) - rat ALTERNATE_NAMES kinase-related transforming protein raf-1; raf-1 proto-oncogene protein-serine/threonine kinase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 11-Jun-1999 ACCESSIONS A26126 REFERENCE A26126 !$#authors Ishikawa, F.; Takaku, F.; Nagao, M.; Sugimura, T. !$#journal Mol. Cell. Biol. (1987) 7:1226-1232 !$#title Rat c-raf oncogene activation by a rearrangement that !1produces a fused protein. !$#cross-references MUID:87172791; PMID:3550433 !$#accession A26126 !'##molecule_type mRNA !'##residues 1-648 ##label ISH !'##cross-references GB:M15427; NID:g206544; PIDN:AAA42001.1; !1PID:g206545 GENETICS !$#gene raf FUNCTION !$#description signal transduction between cell membrane and nucleus; after !1phosphorylation and activation by protein kinase C, !1phosphorylates and activates MAP kinase kinase !$#pathway MAP kinase cascade !$#note expression is ubiquitous in mammalian tissues that have been !1studied CLASSIFICATION #superfamily protein kinase A-raf; protein kinase C !1zinc-binding repeat homology; protein kinase homology KEYWORDS ATP; autophosphorylation; phosphoprotein; !1phosphotransferase; proto-oncogene; serine/ !1threonine-specific protein kinase; signal transduction; !1transforming protein; zinc FEATURE !$139-184 #domain protein kinase C zinc-binding repeat homology !8#label KZN\ !$347-613 #domain protein kinase homology #label KIN\ !$355-363 #region protein kinase ATP-binding motif\ !$43,621 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$139,165,168,184 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$152,155,173,176 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$259 #binding_site phosphate (Ser) (covalent) (by protein !8kinase C) #status predicted\ !$268 #binding_site phosphate (Thr) (covalent) (by !8autophosphorylation) #status predicted\ !$375 #active_site Lys #status predicted\ !$499 #binding_site phosphate (Ser) (covalent) (by protein !8kinase C) #status predicted\ !$499 #binding_site phosphate (Ser) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 648 #molecular-weight 72928 #checksum 9976 SEQUENCE /// ENTRY S00644 #type complete TITLE protein kinase raf-1 (EC 2.7.1.-) - chicken ALTERNATE_NAMES kinase-related transforming protein raf-1; mht/raf; protein kinase c-mil; raf-1 proto-oncogene protein-serine/threonine kinase ORGANISM #formal_name Gallus gallus #common_name chicken DATE 18-Oct-1989 #sequence_revision 23-Aug-1996 #text_change 11-Jun-1999 ACCESSIONS S00644; I50380; I50381 REFERENCE S00644 !$#authors Koenen, M.; Sippel, A.E.; Trachmann, C.; Bister, K. !$#journal Oncogene (1988) 2:179-185 !$#title Primary structure of the chicken c-mil protein: !1identification of domains shared with or absent from the !1retroviral v-mil protein. !$#cross-references MUID:88217299; PMID:3285296 !$#accession S00644 !'##molecule_type mRNA !'##residues 1-647 ##label KOE !'##cross-references EMBL:X07017; NID:g63232; PIDN:CAA30069.1; !1PID:g63233 REFERENCE I50380 !$#authors Flordellis, C.S.; Kan, N.C.; Lautenberger, J.A.; Samuel, !1K.P.; Garon, C.F.; Papas, T.S. !$#journal Virology (1985) 141:267-274 !$#title Analysis of the cellular proto-oncogene mht/raf: !1Relationship to the 5' sequences of v-mht in avian carcinoma !1virus MH2 and v-raf in murine sarcoma virus 3611. !$#cross-references MUID:86098644; PMID:3002017 !$#accession I50380 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 230-330 ##label FLO !'##cross-references GB:K03048; NID:g212306; PIDN:AAA48951.1; !1PID:g212308 REFERENCE I50381 !$#authors Jansen, H.W.; Bister, K. !$#journal Virology (1985) 143:359-367 !$#title Nucleotide sequence analysis of the chicken gene c-mil, the !1progenitor of the retroviral oncogene v-mil. !$#cross-references MUID:86045899; PMID:2998016 !$#accession I50381 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 228-548,'F',550-647 ##label JAN !'##cross-references GB:K03269; NID:g212319; PIDN:AAA48952.1; !1PID:g212321 GENETICS !$#introns 278/3; 288/1; 330/3; 370/1; 398/2; 457/2; 473/1; 512/3; 556/ !13; 601/3 !$#note the list of introns may be incomplete FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP; signal transduction !1between cell membrane and nucleus !$#pathway MAP kinase cascade !$#note after phosphorylation and activation by protein kinase C, !1phosphorylates and activates MAP kinase kinase; expression !1is ubiquitous in mammalian tissues that have been studied CLASSIFICATION #superfamily protein kinase A-raf; protein kinase C !1zinc-binding repeat homology; protein kinase homology KEYWORDS ATP; autophosphorylation; phosphoprotein; !1phosphotransferase; proto-oncogene; serine/ !1threonine-specific protein kinase; signal transduction; !1transforming protein; zinc FEATURE !$139-184 #domain protein kinase C zinc-binding repeat homology !8#label KZN\ !$347-613 #domain protein kinase homology #label KIN\ !$355-363 #region protein kinase ATP-binding motif\ !$43,621 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$139,165,168,184 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$152,155,173,176 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$259 #binding_site phosphate (Ser) (covalent) (by protein !8kinase C) #status predicted\ !$268 #binding_site phosphate (Thr) (covalent) (by !8autophosphorylation) #status predicted\ !$375,393,468,470 #active_site Lys, Glu, Asp, Lys #status predicted\ !$499 #binding_site phosphate (Ser) (covalent) (by protein !8kinase C) #status predicted SUMMARY #length 647 #molecular-weight 73124 #checksum 549 SEQUENCE /// ENTRY TVXLRF #type complete TITLE protein kinase raf-1 (EC 2.7.1.-) - African clawed frog ALTERNATE_NAMES kinase-related transforming protein raf-1; raf-1 proto-oncogene protein-serine/threonine kinase ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 11-Jun-1999 ACCESSIONS S01930; I51254 REFERENCE S01930 !$#authors le Guellec, R.; le Guellec, K.; Paris, J.; Philippe, M. !$#journal Nucleic Acids Res. (1988) 16:10357 !$#title Nucleotide sequence of Xenopus C-raf coding region. !$#cross-references MUID:89057471; PMID:3194203 !$#accession S01930 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-638 ##label LEG !'##cross-references EMBL:X12948; NID:g65027; PIDN:CAA31407.1; !1PID:g65028 REFERENCE I51254 !$#authors Le Guellec, R.; Couturier, A.; Le Guellec, K.; Paris, J.; Le !1Fur, N.; Philippe, M. !$#journal Biol. Cell (1991) 72:39-45 !$#title Xenopus c-raf proto-oncogene: cloning and expression during !1oogenesis and early development. !$#cross-references MUID:92096753; PMID:1721855 !$#accession I51254 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-308,'R',310-638 ##label LEX !'##cross-references GB:S74063; NID:g241259; PIDN:AAB20707.1; !1PID:g241260 GENETICS !$#gene raf FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP; signal transduction !1between cell membrane and nucleus !$#pathway MAP kinase cascade !$#note after phosphorylation and activation by protein kinase C, !1phosphorylates and activates MAP kinase kinase; expression !1is ubiquitous in mammalian tissues that have been studied CLASSIFICATION #superfamily protein kinase A-raf; protein kinase C !1zinc-binding repeat homology; protein kinase homology KEYWORDS ATP; autophosphorylation; phosphoprotein; !1phosphotransferase; proto-oncogene; serine/ !1threonine-specific protein kinase; signal transduction; !1transforming protein; zinc FEATURE !$138-183 #domain protein kinase C zinc-binding repeat homology !8#label KZN\ !$338-604 #domain protein kinase homology #label KIN\ !$346-354 #region protein kinase ATP-binding motif\ !$43 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$138,164,167,183 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$151,154,172,175 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$257 #binding_site phosphate (Ser) (covalent) (by protein !8kinase C) #status predicted\ !$266 #binding_site phosphate (Thr) (covalent) (by !8autophosphorylation) #status predicted\ !$366,384,459,461 #active_site Lys, Glu, Asp, Lys #status predicted\ !$490 #binding_site phosphate (Ser) (covalent) (by protein !8kinase C) #status predicted SUMMARY #length 638 #molecular-weight 71959 #checksum 2746 SEQUENCE /// ENTRY TVHUAF #type complete TITLE protein kinase A-raf-1 (EC 2.7.1.-) - human ALTERNATE_NAMES A-raf-1 proto-oncogene protein-serine/threonine kinase; kinase-related transforming protein A-raf-1; pks proto-oncogene protein-serine/threonine kinase ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1988 #sequence_revision 14-Jul-1994 #text_change 16-Jun-2000 ACCESSIONS A53026; A26439; A23541 REFERENCE A53026 !$#authors Lee, J.E.; Beck, T.W.; Brennscheidt, U.; DeGennaro, L.J.; !1Rapp, U.R. !$#journal Genomics (1994) 20:43-55 !$#title The complete sequence and promoter activity of the human !1A-raf-1 gene (ARAF1). !$#cross-references MUID:94292185; PMID:8020955 !$#accession A53026 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-606 ##label LEE !'##cross-references GB:L24038; NID:g508473; PIDN:AAA65219.1; !1PID:g780127 REFERENCE A26439 !$#authors Beck, T.W.; Huleihel, M.; Gunnell, M.; Bonner, T.I.; Rapp, !1U.R. !$#journal Nucleic Acids Res. (1987) 15:595-609 !$#title The complete coding sequence of the human A-raf-1 oncogene !1and transforming activity of a human A-raf carrying !1retrovirus. !$#cross-references MUID:87146380; PMID:3029685 !$#accession A26439 !'##molecule_type mRNA !'##residues 1-297,'X',299-606 ##label BEC !'##cross-references EMBL:X04790; NID:g28820; PIDN:CAA28476.1; !1PID:g1340152 REFERENCE A23541 !$#authors Mark, G.E.; Seeley, T.W.; Shows, T.B.; Mountz, J.D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:6312-6316 !$#title pks, a raf-related sequence in humans. !$#cross-references MUID:86313571; PMID:3529082 !$#accession A23541 !'##molecule_type mRNA !'##residues 292-367,'P',369-377,'V',379-468,'P',470-477,'T',479-589 !1##label MAR !'##cross-references GB:M13829; NID:g189999; PIDN:AAB08754.1; !1PID:g387023 GENETICS !$#gene GDB:ARAF1 !'##cross-references GDB:119004; OMIM:311010 !$#map_position Xp11.3-Xp11.23 !$#introns 32/3; 67/2; 101/3; 153/2; 186/2; 230/3; 240/1; 288/3; 356/2; !1415/2; 431/1; 470/3; 514/3; 559/3 FUNCTION !$#description signal transduction between cell membrane and nucleus; after !1phosphorylation and activation by protein kinase C, !1phosphorylates and activates MAP kinase kinase !$#pathway MAP kinase cascade !$#note in mouse, expressed in urogenital tissues and, at lower !1levels, in other tissues CLASSIFICATION #superfamily protein kinase A-raf; protein kinase C !1zinc-binding repeat homology; protein kinase homology KEYWORDS ATP; autophosphorylation; phosphoprotein; !1phosphotransferase; proto-oncogene; serine/ !1threonine-specific protein kinase; signal transduction; !1transforming protein; zinc FEATURE !$99-144 #domain protein kinase C zinc-binding repeat homology !8#label KZN\ !$308-574 #domain protein kinase homology #label KIN\ !$316-324 #region protein kinase ATP-binding motif\ !$99,125,128,144 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$112,115,133,136 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$214 #binding_site phosphate (Ser) (covalent) (by protein !8kinase C) #status predicted\ !$223 #binding_site phosphate (Thr) (covalent) (by !8autophosphorylation) #status predicted\ !$336 #active_site Lys #status predicted\ !$582 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 606 #molecular-weight 67585 #checksum 1480 SEQUENCE /// ENTRY S00726 #type complete TITLE protein kinase A-raf-1 (EC 2.7.1.-) - rat ALTERNATE_NAMES A-raf-1 proto-oncogene protein-serine/threonine kinase; kinase-related transforming protein A-raf-1; pks proto-oncogene protein-serine/threonine kinase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1989 #sequence_revision 23-Aug-1996 #text_change 11-Jun-1999 ACCESSIONS S00726 REFERENCE S00726 !$#authors Ishikawa, F.; Takaku, F.; Nagao, M.; Sugimura, T. !$#journal Oncogene Res. (1987) 1:243-253 !$#title The complete primary structure of the rat A-raf cDNA coding !1region: conservation of the putative regulatory regions !1present in rat c-raf. !$#cross-references MUID:88217324; PMID:3449797 !$#accession S00726 !'##molecule_type mRNA !'##residues 1-604 ##label ISH !'##cross-references EMBL:X06942; NID:g55756; PIDN:CAA30023.1; !1PID:g55757 FUNCTION !$#description signal transduction between cell membrane and nucleus; after !1phosphorylation and activation by protein kinase C, !1phosphorylates and activates MAP kinase kinase !$#pathway MAP kinase cascade !$#note in mouse, expressed in urogenital tissues and, at lower !1levels, in other tissues CLASSIFICATION #superfamily protein kinase A-raf; protein kinase C !1zinc-binding repeat homology; protein kinase homology KEYWORDS ATP; autophosphorylation; phosphoprotein; !1phosphotransferase; proto-oncogene; serine/ !1threonine-specific protein kinase; signal transduction; !1transforming protein; zinc FEATURE !$99-144 #domain protein kinase C zinc-binding repeat homology !8#label KZN\ !$306-572 #domain protein kinase homology #label KIN\ !$314-322 #region protein kinase ATP-binding motif\ !$99,125,128,144 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$112,115,133,136 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$214 #binding_site phosphate (Ser) (covalent) (by protein !8kinase C) #status predicted\ !$223 #binding_site phosphate (Thr) (covalent) (by !8autophosphorylation) #status predicted\ !$334 #active_site Lys #status predicted\ !$580 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 604 #molecular-weight 67551 #checksum 7605 SEQUENCE /// ENTRY TVMSRF #type fragment TITLE protein kinase A-raf-1 (EC 2.7.1.-) - mouse (fragment) ALTERNATE_NAMES A-raf-1 proto-oncogene protein-serine/threonine kinase; kinase-related transforming protein A-raf-1; pks proto-oncogene protein-serine/threonine kinase ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 11-Jun-1999 ACCESSIONS A25382 REFERENCE A25382 !$#authors Huleihel, M.; Goldsborough, M.; Cleveland, J.; Gunnell, M.; !1Bonner, T.; Rapp, U.R. !$#journal Mol. Cell. Biol. (1986) 6:2655-2662 !$#title Characterization of murine A-raf, a new oncogene related to !1the v-raf oncogene. !$#cross-references MUID:87064566; PMID:3491291 !$#accession A25382 !'##molecule_type mRNA !'##residues 1-437 ##label HUL !'##cross-references GB:M13071; NID:g192016; PIDN:AAA37258.1; !1PID:g387104 GENETICS !$#gene A-raf FUNCTION !$#description signal transduction between cell membrane and nucleus; after !1phosphorylation and activation by protein kinase C, !1phosphorylates and activates MAP kinase kinase !$#pathway MAP kinase cascade !$#note in mouse, expressed in urogenital tissues and, at lower !1levels, in other tissues CLASSIFICATION #superfamily protein kinase A-raf; protein kinase C !1zinc-binding repeat homology; protein kinase homology KEYWORDS ATP; autophosphorylation; phosphoprotein; !1phosphotransferase; proto-oncogene; serine/ !1threonine-specific protein kinase; signal transduction; !1transforming protein; zinc FEATURE !$139-405 #domain protein kinase homology #label KIN\ !$147-155 #region protein kinase ATP-binding motif\ !$47 #binding_site phosphate (Ser) (covalent) (by protein !8kinase C) #status predicted\ !$56 #binding_site phosphate (Thr) (covalent) (by !8autophosphorylation) #status predicted\ !$167 #active_site Lys #status predicted\ !$413 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 437 #checksum 8034 SEQUENCE /// ENTRY TVHUBF #type complete TITLE protein kinase B-raf (EC 2.7.1.-) - human ALTERNATE_NAMES kinase-related transforming protein B-raf; P94 ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1989 #sequence_revision 10-May-1996 #text_change 11-Jun-1999 ACCESSIONS A57977; A45006; S13798; A31850; I37211 REFERENCE A57977 !$#authors Stephens, R.M.; Sithanandam, G.; Copeland, T.; Kaplan, D.R.; !1Rapp, U.R.; Morrison, D.K. !$#citation unpublished results, 1992, cited by GenBank !$#description 95kDa b-Raf serine/threonine kinase: idendification of the !1protein and its major autophosphorylation site. !$#accession A57977 !'##molecule_type mRNA !'##residues 1-765 ##label STE !'##cross-references GB:M95712; NID:g179532; PIDN:AAA35609.1; !1PID:g179533; GB:M95720; EMBL:X54072 !'##note sequence is a composite of those reported in references A45006 !1and S13798 REFERENCE A45006 !$#authors Stephens, R.M.; Sithanandam, G.; Copeland, T.D.; Kaplan, !1D.R.; Rapp, U.R.; Morrison, D.K. !$#journal Mol. Cell. Biol. (1992) 12:3733-3742 !$#title 95-kilodalton B-Raf serine/threonine kinase: identification !1of the protein and its major autophosphorylation site. !$#cross-references MUID:92375040; PMID:1508179 !$#accession A45006 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type mRNA; protein !'##residues 1-115 ##label ST2 !'##note sequence extracted from NCBI backbone (NCBIP:111729) !'##note the major in vitro autophophorylation site, Thr-372, is not a !1major phosphorylation site in NGF-stimulated cells; Ser-366 !1was a minor autophosphorylated residue in some experiments REFERENCE S13798 !$#authors Sithanandam, G.; Kolch, W.; Duh, F.M.; Rapp, U.R. !$#journal Oncogene (1990) 5:1775-1780 !$#title Complete coding sequence of a human B-raf cDNA and detection !1of B-raf protein kinase with isozyme specific antibodies. !$#cross-references MUID:91133728; PMID:2284096 !$#accession S13798 !'##status preliminary !'##molecule_type mRNA !'##residues 116-765 ##label SIT !'##cross-references EMBL:X54072; NID:g179532 REFERENCE A31850 !$#authors Ikawa, S.; Fukui, M.; Ueyama, Y.; Tamaoki, N.; Yamamoto, T.; !1Toyoshima, K. !$#journal Mol. Cell. Biol. (1988) 8:2651-2654 !$#title B-raf, a new member of the raf family, is activated by DNA !1rearrangement. !$#cross-references MUID:88302178; PMID:3043188 !$#accession A31850 !'##molecule_type mRNA !'##residues 438-765 ##label IKA !'##cross-references GB:M21001; NID:g179534 REFERENCE I37211 !$#authors Eychene, A.; Barnier, J.V.; Apiou, F.; Dutrillaux, B.; !1Calothy, G. !$#journal Oncogene (1992) 7:1657-1660 !$#title Chromosomal assignment of two human B-raf(Rmil) !1proto-oncogene loci: B-raf-1 encoding the p94Braf/Rmil and !1B-raf-2, a processed pseudogene. !$#cross-references MUID:92334878; PMID:1630826 !$#accession I37211 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-30,'AGA',33-199 ##label EYC !'##cross-references EMBL:X65187; NID:g29485; PIDN:CAA46301.1; !1PID:g29486 GENETICS !$#gene GDB:BRAF !'##cross-references GDB:127513; OMIM:164757 !$#map_position 7q34-7q34 FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP; signal transduction !1activated by nerve growth factor or epidermal growth factor !$#pathway MAP kinase cascade !$#note believed to phosphorylate MAP kinase kinase; found in !1hippocampal neurons and dendritic spines and in high levels !1in fetal brain and cerebrum CLASSIFICATION #superfamily protein kinase A-raf; protein kinase C !1zinc-binding repeat homology; protein kinase homology KEYWORDS ATP; autophosphorylation; phosphoprotein; !1phosphotransferase; proto-oncogene; serine/ !1threonine-specific protein kinase; signal transduction; !1transforming protein; zinc FEATURE !$234-279 #domain protein kinase C zinc-binding repeat homology !8#label KZ2\ !$454-720 #domain protein kinase homology #label KIN\ !$462-470 #region protein kinase ATP-binding motif\ !$234,260,263,279 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$247,250,268,271 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$364,606 #binding_site phosphate (Ser) (covalent) (by protein !8kinase C) #status predicted\ !$372 #binding_site phosphate (Thr) (covalent) (by !8autophosphorylation) #status predicted\ !$482,500,575,577 #active_site Lys, Glu, Asp, Lys #status predicted\ !$728 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 765 #molecular-weight 84490 #checksum 8655 SEQUENCE /// ENTRY TVMSBF #type fragment TITLE protein kinase B-raf (EC 2.7.1.-) - mouse (fragment) ALTERNATE_NAMES kinase-related transforming protein B-raf; P94 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Mar-1993 #sequence_revision 09-Aug-1996 #text_change 23-Feb-1997 ACCESSIONS A40951 REFERENCE A40951 !$#authors Miki, T.; Fleming, T.P.; Crescenzi, M.; Molloy, C.J.; Blam, !1S.B.; Reynolds, S.H.; Aaronson, S.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:5167-5171 !$#title Development of a highly efficient expression cDNA cloning !1system: application to oncogene isolation. !$#cross-references MUID:91271351; PMID:2052597 !$#accession A40951 !'##molecule_type mRNA !'##residues 1-328 ##label MIK !'##cross-references GB:M64429 !'##note the reported sequence is the product of recombination of TIF1 !1and B-raf genes; the B-raf portion is given here GENETICS !$#gene B-raf FUNCTION !$#description member of signal transduction pathway(s) activated by nerve !1growth factor or epidermal growth factor; believed to !1phosphorylate MAP kinase kinase !$#pathway MAP kinase cascade !$#note found in hippocampal neurons and dendritic spines and in !1high levels in fetal brain and cerebrum CLASSIFICATION #superfamily protein kinase A-raf; protein kinase C !1zinc-binding repeat homology; protein kinase homology KEYWORDS ATP; autophosphorylation; phosphoprotein; !1phosphotransferase; proto-oncogene; serine/ !1threonine-specific protein kinase; signal transduction; !1transforming protein; zinc FEATURE !$17-283 #domain protein kinase homology #label KIN\ !$25-33 #region protein kinase ATP-binding motif\ !$45 #active_site Lys #status predicted\ !$169 #binding_site phosphate (Ser) (covalent) (by protein !8kinase C) #status predicted SUMMARY #length 328 #checksum 5247 SEQUENCE /// ENTRY JN0612 #type complete TITLE protein kinase B-raf (EC 2.7.1.-), long form - chicken ALTERNATE_NAMES kinase-related transforming protein B-raf; protein kinase Rmil; transforming protein c-Rmil CONTAINS protein kinase B-raf, short form ORGANISM #formal_name Gallus gallus #common_name chicken DATE 24-Feb-1994 #sequence_revision 23-Aug-1996 #text_change 11-Jun-1999 ACCESSIONS JN0612; S31792 REFERENCE JN0612 !$#authors Calogeraki, I.; Barnier, J.V.; Eychene, A.; Felder, M.P.; !1Calothy, G.; Marx, M. !$#journal Biochem. Biophys. Res. Commun. (1993) 193:1324-1331 !$#title Genomic organization and nucleotide sequence of the coding !1region of the chicken c-Rmil(B-raf-1) proto-oncogene. !$#cross-references MUID:93312327; PMID:8323553 !$#accession JN0612 !'##molecule_type DNA !'##residues 1-806 ##label CAL !'##cross-references EMBL:X67052; NID:g63339; PIDN:CAA47436.1; !1PID:g63340 GENETICS !$#gene c-Rmil !$#introns 46/3; 80/3; 168/3; 203/2; 237/3; 287/2; 327/2; 380/2; 393/1; !1433/1; 478/3; 518/1; 546/2; 605/2; 621/1; 660/3; 704/3; 749/ !13 FUNCTION !$#description member of signal transduction pathway(s) activated by nerve !1growth factor or epidermal growth factor; believed to !1phosphorylate MAP kinase kinase !$#pathway MAP kinase cascade CLASSIFICATION #superfamily protein kinase A-raf; protein kinase C !1zinc-binding repeat homology; protein kinase homology KEYWORDS alternative splicing; ATP; autophosphorylation; !1phosphoprotein; phosphotransferase; proto-oncogene; serine/ !1threonine-specific protein kinase; signal transduction; !1transforming protein; zinc FEATURE !$1-806 #product protein kinase B-raf, long form #status !8predicted #label MAT\ !$1-392,433-806 #product protein kinase B-raf, short form #status !8predicted #label SHF\ !$235-280 #domain protein kinase C zinc-binding repeat homology !8#label KZ2\ !$495-761 #domain protein kinase homology #label KIN\ !$503-511 #region protein kinase ATP-binding motif\ !$235,261,264,280 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$248,251,269,272 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$365,647 #binding_site phosphate (Ser) (covalent) (by protein !8kinase C) #status predicted\ !$373 #binding_site phosphate (Thr) (covalent) (by !8autophosphorylation) #status predicted\ !$523 #active_site Lys #status predicted\ !$769 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 806 #molecular-weight 89365 #checksum 8599 SEQUENCE /// ENTRY I51153 #type complete TITLE protein kinase B-raf (EC 2.7.1.-), long splice form - quail ALTERNATE_NAMES kinase-related transforming protein B-raf; protein kinase Rmil; transforming protein c-Rmil CONTAINS protein kinase B-raf, short splice form ORGANISM #formal_name Coturnix coturnix #common_name quail DATE 13-Sep-1996 #sequence_revision 13-Sep-1996 #text_change 11-Jun-1999 ACCESSIONS I51153; I51152 REFERENCE I51152 !$#authors Eychene, A.; Barnier, J. !$#journal Oncogene (1992) 7:1315-1323 !$#title Quail neuroretina c-Rmil(B-raf) protooncogene cDNAs encode !1two proteins of 93.5 and 95 KD resulting from alternative !1splicing. !$#cross-references MUID:92319540; PMID:1620546 !$#accession I51153 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-807 ##label EYC !'##cross-references GB:M80846; NID:g213600; PIDN:AAA49493.1; !1PID:g213601 !$#accession I51152 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-392,433-807 ##label EY2 !'##cross-references GB:M80845; NID:g213598; PIDN:AAA49492.1; !1PID:g213599 GENETICS !$#gene c-Rmil FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP; signal transduction !1activated by nerve growth factor or epidermal growth factor !$#pathway MAP kinase cascade !$#note believed to phosphorylate MAP kinase kinase; found in !1hippocampal neurons and dendritic spines and in high levels !1in fetal brain and cerebrum CLASSIFICATION #superfamily protein kinase A-raf; protein kinase C !1zinc-binding repeat homology; protein kinase homology KEYWORDS alternative splicing; ATP; autophosphorylation; !1phosphoprotein; phosphotransferase; proto-oncogene; serine/ !1threonine-specific protein kinase; signal transduction; !1transforming protein; zinc FEATURE !$1-392,433-807 #product protein kinase B-raf, short splice form !8#status predicted #label MAT2\ !$235-280 #domain protein kinase C zinc-binding repeat homology !8#label KZ2\ !$495-761 #domain protein kinase homology #label KIN\ !$503-511 #region protein kinase ATP-binding motif\ !$235,261,264,280 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$248,251,269,272 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$365,647 #binding_site phosphate (Ser) (covalent) (by protein !8kinase C) #status predicted\ !$373 #binding_site phosphate (Thr) (covalent) (by !8autophosphorylation) #status predicted\ !$523,541,616,618 #active_site Lys, Glu, Asp, Lys #status predicted\ !$769 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 807 #molecular-weight 89521 #checksum 9013 SEQUENCE /// ENTRY TVFFDF #type complete TITLE protein kinase Draf-1 (EC 2.7.1.-) - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES Draf-1 proto-oncogene protein-serine/threonine kinase; kinase-related transforming protein Draf-1; pole-hole protein ORGANISM #formal_name Drosophila melanogaster DATE 31-Mar-1991 #sequence_revision 23-Feb-1996 #text_change 23-Feb-1997 ACCESSIONS S00393; S60191; A27808; S33602 REFERENCE S00393 !$#authors Nishida, Y.; Hata, M.; Ayaki, T.; Ryo, H.; Yamagata, M.; !1Shimizu, K.; Nishizuka, Y. !$#journal EMBO J. (1988) 7:775-781 !$#title Proliferation of both somatic and germ cells is affected in !1the Drosophila mutants of raf proto-oncogene. !$#cross-references MUID:88283647; PMID:3135183 !$#accession S00393 !'##molecule_type DNA !'##residues 1-781 ##label NIS !'##cross-references EMBL:X07181 !'##note the assignment of the start codon has been revised in reference !1S33602 !$#accession S60191 !'##molecule_type mRNA !'##residues 148-781 ##label NIS2 REFERENCE A27808 !$#authors Mark, G.E.; MacIntyre, R.J.; Digan, M.E.; Ambrosio, L.; !1Perrimon, N. !$#journal Mol. Cell. Biol. (1987) 7:2134-2140 !$#title Drosophila melanogaster homologs of the raf oncogene. !$#cross-references MUID:87257926; PMID:3037346 !$#accession A27808 !'##molecule_type mRNA !'##residues 'LQ',465-519,'R',521,'A',523-570,'R',572-699,'PQAL', !1704-713,'PT',716-753 ##label MAR REFERENCE S33602 !$#authors Sprenger, F.; Trosclair, M.M.; Morrison, D.K. !$#journal Mol. Cell. Biol. (1993) 13:1163-1172 !$#title Biochemical analysis of torso and D-raf during Drosophila !1embryogenesis: implications for terminal signal !1transduction. !$#cross-references MUID:93140754; PMID:8423783 !$#contents annotation !$#note this is a revision of the assignment of the start codon in !1reference S00393 !$#note the authors call the N-terminal extended version of the !1protein Draf-3 !$#note the cited sequence in S33602 shows Pro for residue 342 GENETICS !$#gene Draf-1 !'##cross-references FlyBase:FBgn0003079 !$#map_position X 2F !$#introns 417/3; 464/3; 589/2 CLASSIFICATION #superfamily protein kinase A-raf; protein kinase C !1zinc-binding repeat homology; protein kinase homology KEYWORDS ATP; phosphotransferase; proto-oncogene; serine/ !1threonine-specific protein kinase; transforming protein FEATURE !$265-310 #domain protein kinase C zinc-binding repeat homology !8#label KZ2\ !$469-735 #domain protein kinase homology #label KIN\ !$477-485 #region protein kinase ATP-binding motif\ !$497 #active_site Lys #status predicted SUMMARY #length 781 #molecular-weight 88768 #checksum 9872 SEQUENCE /// ENTRY S33261 #type complete TITLE protein kinase lin-45 (EC 2.7.1.-) - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 22-Nov-1993 #sequence_revision 01-Sep-1995 #text_change 11-Jun-1999 ACCESSIONS S33261 REFERENCE S33261 !$#authors Han, M.; Golden, A.; Han, Y.; Sternberg, P.W. !$#journal Nature (1993) 363:133-140 !$#title C. elegans lin-45 raf gene participates in let-60 !1ras-stimulated vulval differentiation. !$#cross-references MUID:93247635; PMID:8483497 !$#accession S33261 !'##status preliminary !'##molecule_type mRNA !'##residues 1-813 ##label HAN !'##cross-references EMBL:L15347; NID:g289715; PIDN:AAA28142.1; !1PID:g289716 GENETICS !$#gene lin-45 !$#map_position IV !$#note between unc-44 and deb-1 FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP; signal transduction !$#pathway vulval differentiation CLASSIFICATION #superfamily protein kinase A-raf; protein kinase C !1zinc-binding repeat homology; protein kinase homology KEYWORDS ATP; phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase; signal transduction; zinc FEATURE !$171-217 #domain protein kinase C zinc-binding repeat homology !8#label KZ2\ !$479-748 #domain protein kinase homology #label KIN\ !$487-495 #region protein kinase ATP-binding motif\ !$171,198,201,217 #binding_site zinc (His, Cys, Cys, Cys) #status !8predicted\ !$184,187,206,209 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted\ !$312 #binding_site phosphate (Ser) (covalent) (by protein !8kinase C) #status predicted\ !$507,525,602,604 #active_site Lys, Glu, Asp, Lys #status predicted\ !$756 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 813 #molecular-weight 90491 #checksum 6400 SEQUENCE /// ENTRY S68178 #type complete TITLE mixed-lineage protein kinase 2 (EC 2.7.1.-) - human ORGANISM #formal_name Homo sapiens #common_name man DATE 28-Oct-1996 #sequence_revision 13-Mar-1997 #text_change 11-Jun-1999 ACCESSIONS S68178; I38044; S32468 REFERENCE S68178 !$#authors Dorow, D.S.; Devereux, L.; Tu, G.F.; Price, G.; Nicholl, !1J.K.; Sutherland, G.R.; Simpson, R.J. !$#journal Eur. J. Biochem. (1995) 234:492-500 !$#title Complete nucleotide sequence, expression, and chromosomal !1localisation of human mixed-lineage kinase 2. !$#cross-references MUID:96128179; PMID:8536694 !$#accession S68178 !'##molecule_type mRNA !'##residues 1-954 ##label DOR !'##cross-references EMBL:X90846; NID:g971419; PIDN:CAA62351.1; !1PID:g971420 REFERENCE I38044 !$#authors Katoh, M.; Hirai, M.; Sugimura, T.; Terada, M. !$#journal Oncogene (1995) 10:1447-1451 !$#title Cloning and characterization of MST, a novel (putative) !1serine/threonine kinase with SH3 domain. !$#cross-references MUID:95249256; PMID:7731697 !$#accession I38044 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-461,'A','V',465-470,'S',472-806,'R',808-817,'A',819-954 !1##label RES !'##cross-references EMBL:Z48615; NID:g758592; PIDN:CAA88531.1; !1PID:g758593 REFERENCE S32467 !$#authors Dorow, D.S.; Devereux, L.; Dietzsch, E.; de Kretser, T. !$#journal Eur. J. Biochem. (1993) 213:701-710 !$#title Identification of a new family of human epithelial protein !1kinases containing two leucine/isoleucine-zipper domains. !$#cross-references MUID:93238756; PMID:8477742 !$#accession S32468 !'##molecule_type mRNA !'##residues 244-464,'AQAAGRRQPHQPALWL' ##label DO2 GENETICS !$#gene GDB:MLK2; GDB:MST !'##cross-references GDB:362654; GDB:624810; OMIM:600137 !$#map_position 19q13.1-19q13.2 CLASSIFICATION #superfamily mixed-lineage protein kinase 2; protein kinase !1homology; SH3 homology KEYWORDS ATP; leucine zipper; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$23-76 #domain SH3 homology #label SH3\ !$96-364 #domain protein kinase homology #label KIN\ !$104-112 #region protein kinase ATP-binding motif\ !$384-405 #region leucine zipper motif\ !$419-440 #region leucine zipper motif\ !$449-463 #region basic\ !$125,145,222,224 #active_site Lys, Glu, Asp, Lys #status predicted SUMMARY #length 954 #molecular-weight 103622 #checksum 7280 SEQUENCE /// ENTRY A53800 #type complete TITLE mixed-lineage protein kinase (EC 2.7.1.-) 3 - human ALTERNATE_NAMES protein kinase PTK1; protein kinase SPRK ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A53800; I58395 REFERENCE A53800 !$#authors Gallo, K.A.; Mark, M.R.; Scadden, D.T.; Wang, Z.; Gu, Q.; !1Godowski, P.J. !$#journal J. Biol. Chem. (1994) 269:15092-15100 !$#title Identification and characterization of SPRK, a novel !1src-homology 3 domain-containing proline-rich kinase with !1serine/threonine kinase activity. !$#cross-references MUID:94253068; PMID:8195146 !$#accession A53800 !'##status preliminary !'##molecule_type mRNA !'##residues 1-847 ##label GAL !'##cross-references GB:U07747; NID:g464027; PIDN:AAA19647.1; !1PID:g464028 REFERENCE I58395 !$#authors Ing, Y.L.; Leung, I.W.; Heng, H.H.; Tsui, L.C.; Lassam, N.J. !$#journal Oncogene (1994) 9:1745-1750 !$#title MLK-3: identification of a widely-expressed protein kinase !1bearing an SH3 domain and a leucine zipper-basic region !1domain. !$#cross-references MUID:94239754; PMID:8183572 !$#accession I58395 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-847 ##label RES !'##cross-references GB:L32976; NID:g488295; PIDN:AAA59859.1; !1PID:g488296 GENETICS !$#gene GDB:MLK3; PTK1; SPRK !'##cross-references GDB:134755; OMIM:600050 !$#map_position 11q13.1-11q13.3 CLASSIFICATION #superfamily mixed-lineage protein kinase 3; protein kinase !1homology; SH3 homology KEYWORDS ATP; leucine zipper; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$48-100 #domain SH3 homology #label SH32\ !$115-383 #domain protein kinase homology #label KIN\ !$123-131 #region protein kinase ATP-binding motif\ !$403-424 #region leucine zipper motif\ !$438-459 #region leucine zipper motif\ !$468-482 #region basic SUMMARY #length 847 #molecular-weight 92687 #checksum 4129 SEQUENCE /// ENTRY TVRTRR #type complete TITLE protein kinase (EC 2.7.1.37) raf - rat ALTERNATE_NAMES kinase-related transforming protein raf; raf proto-oncogene protein-serine/threonine kinase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 11-Jun-1999 ACCESSIONS B26126 REFERENCE A26126 !$#authors Ishikawa, F.; Takaku, F.; Nagao, M.; Sugimura, T. !$#journal Mol. Cell. Biol. (1987) 7:1226-1232 !$#title Rat c-raf oncogene activation by a rearrangement that !1produces a fused protein. !$#cross-references MUID:87172791; PMID:3550433 !$#accession B26126 !'##molecule_type mRNA !'##residues 1-602 ##label ISH !'##cross-references GB:M15428; NID:g206546; PIDN:AAA42002.1; !1PID:g206547 GENETICS !$#gene raf CLASSIFICATION #superfamily rat protein kinase raf; protein kinase homology KEYWORDS ATP; autophosphorylation; phosphoprotein; !1phosphotransferase; serine/threonine-specific protein !1kinase; transforming protein FEATURE !$301-567 #domain protein kinase homology #label KIN\ !$309-317 #region protein kinase ATP-binding motif\ !$329 #active_site Lys #status predicted\ !$453 #binding_site phosphate (Ser) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 602 #molecular-weight 69209 #checksum 6726 SEQUENCE /// ENTRY OKBOG #type complete TITLE protein kinase (EC 2.7.1.37), cGMP-dependent, type I-alpha - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 17-May-1985 #sequence_revision 17-Feb-1995 #text_change 20-Apr-2000 ACCESSIONS A00619; A37547; A37548; S05034 REFERENCE A00619 !$#authors Takio, K.; Wade, R.D.; Smith, S.B.; Krebs, E.G.; Walsh, !1K.A.; Titani, K. !$#journal Biochemistry (1984) 23:4207-4218 !$#title Guanosine cyclic 3',5'-phosphate dependent protein kinase, a !1chimeric protein homologous with two separate protein !1families. !$#cross-references MUID:85023307; PMID:6091741 !$#accession A00619 !'##molecule_type protein !'##residues 2-18;90-375;408-671 ##label TAK REFERENCE A37547 !$#authors Takio, K.; Smith, S.B.; Walsh, K.A.; Krebs, E.G.; Titani, K. !$#journal J. Biol. Chem. (1983) 258:5531-5536 !$#title Amino acid sequence around a "hinge" region and its !1"autophosphorylation" site in bovine Lung cGMP-dependent !1protein kinase. !$#cross-references MUID:83213511; PMID:6304091 !$#accession A37547 !'##molecule_type protein !'##residues 14-105 ##label TAK2 REFERENCE A37548 !$#authors Hashimoto, E.; Takio, K.; Krebs, E.G. !$#journal J. Biol. Chem. (1982) 257:727-733 !$#title Amino acid sequence at the ATP-binding site of !1cGMP-dependent protein kinase. !$#cross-references MUID:82098123; PMID:6274862 !$#contents ATP-binding site !$#accession A37548 !'##molecule_type protein !'##residues 374-410 ##label HAS REFERENCE S05034 !$#authors Wernet, W.; Flockerzi, V.; Hofmann, F. !$#journal FEBS Lett. (1989) 251:191-196 !$#title The cDNA of the two isoforms of bovine cGMP-dependent !1protein kinase. !$#cross-references MUID:89325663; PMID:2546820 !$#accession S05034 !'##molecule_type mRNA !'##residues 1-671 ##label WER !'##cross-references EMBL:X16086; NID:g211; PIDN:CAA34214.1; PID:g212 CLASSIFICATION #superfamily cGMP-dependent protein kinase; cAMP receptor !1protein cyclic nucleotide-binding domain homology; protein !1kinase homology KEYWORDS acetylated amino end; ATP; autophosphorylation; cGMP !1binding; homodimer; phosphoprotein; phosphotransferase; !1serine/threonine-specific protein kinase FEATURE !$2-671 #product protein kinase, cGMP-dependent, type I-alpha !8#status experimental #label MAT\ !$2-102 #domain dimerization #label DIM\ !$103-220 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP1\ !$221-344 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP2\ !$358-619 #domain protein kinase homology #label KIN\ !$366-374 #region protein kinase ATP-binding motif\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental\ !$43 #disulfide_bonds interchain #status experimental\ !$59 #binding_site phosphate (Thr) (covalent) (by !8autophosphorylation) #status experimental\ !$390 #active_site Lys #status experimental SUMMARY #length 671 #molecular-weight 76418 #checksum 8829 SEQUENCE /// ENTRY S05702 #type complete TITLE protein kinase (EC 2.7.1.37), cGMP-dependent, type I-beta - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1991 #sequence_revision 24-Feb-1995 #text_change 20-Apr-2000 ACCESSIONS S05702 REFERENCE S05702 !$#authors Sandberg, M.; Natarajan, V.; Ronander, I.; Kalderon, D.; !1Walter, U.; Lohmann, S.M.; Jahnsen, T. !$#journal FEBS Lett. (1989) 255:321-329 !$#title Molecular cloning and predicted full-length amino acid !1sequence of the type I-beta isozyme of cGMP-dependent !1protein kinase from human placenta. !$#cross-references MUID:90005998; PMID:2792381 !$#accession S05702 !'##molecule_type mRNA !'##residues 1-686 ##label SAN !'##cross-references EMBL:Y07512; NID:g31708; PIDN:CAA68810.1; !1PID:g31709 GENETICS !$#gene GDB:PRKG1B; cGKI; PGK; PRKGR1B !'##cross-references GDB:127918; OMIM:176894 !$#map_position 10q11.2-10q11.2 CLASSIFICATION #superfamily cGMP-dependent protein kinase; cAMP receptor !1protein cyclic nucleotide-binding domain homology; protein !1kinase homology KEYWORDS acetylated amino end; alternative splicing; ATP; !1autophosphorylation; cGMP binding; homodimer; !1phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$2-686 #product protein kinase, cGMP-dependent, type I-beta !8#status predicted #label MAT\ !$2-117 #domain dimeric association #status predicted #label !8DIM\ !$118-235 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP1\ !$236-359 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP2\ !$373-634 #domain protein kinase homology #label KIN\ !$381-389 #region protein kinase ATP-binding motif\ !$2 #modified_site acetylated amino end (Gly) (in mature !8form) #status predicted\ !$80 #binding_site phosphate (Ser) (covalent) (by !8autophosphorylation) #status predicted\ !$405 #active_site Lys #status experimental SUMMARY #length 686 #molecular-weight 77803 #checksum 5375 SEQUENCE /// ENTRY A46590 #type complete TITLE protein kinase (EC 2.7.1.37), cGMP-dependent, type II - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 03-May-1994 #sequence_revision 24-Feb-1995 #text_change 20-Apr-2000 ACCESSIONS A46590 REFERENCE A46590 !$#authors Uhler, M.D. !$#journal J. Biol. Chem. (1993) 268:13586-13591 !$#title Cloning and expression of a novel cyclic GMP-dependent !1protein kinase from mouse brain. !$#cross-references MUID:93293885; PMID:8514791 !$#accession A46590 !'##molecule_type mRNA !'##residues 1-762 ##label UHL !'##cross-references GB:L12460; NID:g309167; PIDN:AAA02572.1; !1PID:g309168 CLASSIFICATION #superfamily cGMP-dependent protein kinase; cAMP receptor !1protein cyclic nucleotide-binding domain homology; protein !1kinase homology KEYWORDS ATP; cGMP binding; phosphoprotein; phosphotransferase; !1serine/threonine-specific protein kinase FEATURE !$168-285 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP1\ !$286-408 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP2\ !$451-711 #domain protein kinase homology #label KIN\ !$459-467 #region protein kinase ATP-binding motif\ !$482 #active_site Lys #status experimental SUMMARY #length 762 #molecular-weight 87084 #checksum 3292 SEQUENCE /// ENTRY A34106 #type complete TITLE protein kinase (EC 2.7.1.37), cGMP-dependent 1 - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 05-May-2000 ACCESSIONS A34106; B28269 REFERENCE A34106 !$#authors Kalderon, D.; Rubin, G.M. !$#journal J. Biol. Chem. (1989) 264:10738-10748 !$#title cGMP-dependent protein kinase genes in Drosophila. !$#cross-references MUID:89278147; PMID:2732245 !$#accession A34106 !'##molecule_type DNA; mRNA !'##residues 1-768 ##label KAL !'##cross-references GB:M27113; GB:M27114; NID:g157200; PIDN:AAA28453.1; !1PID:g157202; GB:J04816 REFERENCE A92684 !$#authors Foster, J.L.; Higgins, G.C.; Jackson, F.R. !$#journal J. Biol. Chem. (1988) 263:1676-1681 !$#title Cloning, sequence, and expression of the Drosophila !1cAMP-dependent protein kinase catalytic subunit gene. !$#cross-references MUID:88115281; PMID:2828348 !$#accession B28269 !'##molecule_type DNA !'##residues 172-433,'R',435-437,'Q',439-644 ##label FOS GENETICS !$#gene FlyBase:Pkg21D !'##cross-references FlyBase:FBgn0000442 CLASSIFICATION #superfamily cGMP-dependent protein kinase; cAMP receptor !1protein cyclic nucleotide-binding domain homology; protein !1kinase homology KEYWORDS ATP; cGMP binding; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$185-303 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP1\ !$304-429 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP2\ !$455-717 #domain protein kinase homology #label KIN\ !$463-471 #region protein kinase ATP-binding motif SUMMARY #length 768 #molecular-weight 86758 #checksum 7284 SEQUENCE /// ENTRY C36856 #type complete TITLE kinase-related transforming protein (EC 2.7.1.-) B12R - variola virus ALTERNATE_NAMES B13R protein (COP) ORGANISM #formal_name variola virus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 23-Mar-2001 ACCESSIONS C36856; S46870 REFERENCE A36859 !$#authors Blinov, V.M. !$#submission submitted to GenBank, November 1992 !$#accession C36856 !'##status preliminary !'##molecule_type DNA !'##residues 1-134 ##label BLI !'##cross-references GB:X69198; NID:g456758; PIDN:CAA49121.1; !1PID:g457071 !'##experimental_source strain India-1967, ssp. major, isolate Ind3 REFERENCE S46868 !$#authors Kolykhalov, A.A.; Blinov, V.M.; Gytorov, V.V.; Pozdnyakov, !1S.G.; Chizhikov, V.E.; Frolov, I.V.; Totmenin, A.V.; !1Shchelkunov, S.N.; Sandakhchiev, L.S. !$#submission submitted to the EMBL Data Library, April 1992 !$#description Nucleotide sequence analysis of the region of Variola virus !1XhoI F O H P Q genome fragment. !$#accession S46870 !'##status preliminary !'##molecule_type DNA !'##residues 1-134 ##label KOL !'##cross-references EMBL:X67117; NID:g516428; PIDN:CAA47522.1; !1PID:g516431 !'##experimental_source strain India-1967, isolate Ind3 CLASSIFICATION #superfamily variola virus B12R protein; protein kinase !1homology KEYWORDS ATP; phosphotransferase; serine/threonine-specific protein !1kinase; transforming protein FEATURE !$1-68 #domain protein kinase homology #status atypical !8#label KIN SUMMARY #length 134 #molecular-weight 16301 #checksum 1754 SEQUENCE /// ENTRY A39357 #type complete TITLE connexin-crossreactive protein - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A39357 REFERENCE A39357 !$#authors Meiners, S.; Xu, A.; Schindler, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:4119-4122 !$#title Gap junction protein homologue from Arabidopsis thaliana: !1evidence for connexins in plants. !$#cross-references MUID:91239518; PMID:1851993 !$#accession A39357 !'##status preliminary !'##molecule_type mRNA !'##residues 1-280 ##label MEI !'##cross-references GB:M63234 CLASSIFICATION #superfamily Arabidopsis thaliana connexin-crossreactive !1protein; protein kinase homology KEYWORDS transmembrane protein FEATURE !$1-148 #domain protein kinase homology #status atypical !8#label KIN SUMMARY #length 280 #molecular-weight 32482 #checksum 5825 SEQUENCE /// ENTRY S39151 #type complete TITLE cyclin-supressing protein kinase csk1 (EC 2.7.1.-) - fission yeast (Schizosaccharomyces pombe) ORGANISM #formal_name Schizosaccharomyces pombe DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Dec-1999 ACCESSIONS S39151; T38047 REFERENCE S35380 !$#authors Molz, L.; Beach, D. !$#journal EMBO J. (1993) 12:1723-1732 !$#title Characterization of the fission yeast mcs2 cyclin and its !1associated protein kinase activity. !$#cross-references MUID:93223713; PMID:8467814 !$#accession S39151 !'##molecule_type DNA !'##residues 1-306 ##label MOL !'##cross-references GB:S59896; NID:g299548; PIDN:AAB26194.1; !1PID:g299549 REFERENCE Z21765 !$#authors Lye, G.; Churcher, C.M.; Barrell, B.G.; Rajandream, M.A.; !1Walsh, S.V. !$#submission submitted to the EMBL Data Library, February 1995 !$#accession T38047 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-306 ##label LYE !'##cross-references EMBL:Z69239; PIDN:CAA93215.1; GSPDB:GN00066; !1SPDB:SPAC1D4.06c !'##experimental_source strain 972h-; cosmid c1D4 GENETICS !$#gene csk1; SPAC1D4.06c !$#map_position 1 !$#introns 168/3; 240/3 CLASSIFICATION #superfamily fission yeast cyclin kinase csk1; protein !1kinase homology KEYWORDS phosphotransferase; serine/threonine-specific protein kinase FEATURE !$9-268 #domain protein kinase homology #label KIN SUMMARY #length 306 #molecular-weight 34672 #checksum 3826 SEQUENCE /// ENTRY JW0097 #type complete TITLE bicoid-related homeobox protein Pitx2 - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 15-Oct-1999 ACCESSIONS JW0097 REFERENCE JW0097 !$#authors St.Amand, T.R.; Ra, J.; Zhang, Y.; Hu, Y.; Baber, S.I.; Qiu, !1M.S.; Chen, Y.P. !$#journal Biochem. Biophys. Res. Commun. (1998) 247:100-105 !$#title Cloning and expression pattern of chicken Pitx2: A new !1component in the SHH signaling pathway controlling embryonic !1heart looping. !$#cross-references MUID:98300291; PMID:9636662 !$#accession JW0097 !'##molecule_type mRNA !'##residues 1-333 ##label STA !'##cross-references GB:AF076640; NID:g3335642; PIDN:AAC27322.1; !1PID:g3335643 COMMENT This protein is a new component in the Sonic hedgehog !1signaling pathway and plays a role in determining left-right !1asymmetry and in vasculogenesis during avian embryogenesis. GENETICS !$#gene cPitx2 CLASSIFICATION #superfamily chicken bicoid-related homeobox protein Pitx2; !1homeobox homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$102-158 #domain homeobox homology #label HOX SUMMARY #length 333 #molecular-weight 36557 #checksum 987 SEQUENCE /// ENTRY OKHU2C #type complete TITLE protein kinase (EC 2.7.1.37), cAMP-dependent, alpha catalytic chain - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 11-Jun-1999 ACCESSIONS S01404 REFERENCE S01404 !$#authors Maldonado, F.; Hanks, S.K. !$#journal Nucleic Acids Res. (1988) 16:8189-8190 !$#title A cDNA clone encoding human cAMP-dependent protein kinase !1catalytic subunit C-alpha. !$#cross-references MUID:88335571; PMID:2843813 !$#accession S01404 !'##molecule_type mRNA !'##residues 1-351 ##label MAL !'##cross-references EMBL:X07767; GB:M36872; NID:g35478; !1PIDN:CAA30597.1; PID:g35479 COMMENT The inactive enzyme contains two regulatory chains and two !1catalytic chains. Activation by cAMP produces two active !1catalytic monomers and a regulatory dimer that binds four !1cAMP molecules. Two types found in mammalian tissue are !1distinguished by having either type I or type II regulatory !1chains. COMMENT Both alpha and beta catalytic chains are found in many !1tissues, with the alpha form being the more abundant. GENETICS !$#gene GDB:PRKACA !'##cross-references GDB:120717; OMIM:601639 !$#map_position 19p13.1-19p13.1 FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; blocked amino end; cAMP binding; heterotetramer; !1lipoprotein; magnesium; myristylation; phosphoprotein; !1phosphotransferase; serine/threonine-specific protein kinase FEATURE !$2-351 #product protein kinase, cAMP-dependent, alpha !8catalytic chain #status predicted #label MAT\ !$42-298 #domain protein kinase homology #label KIN\ !$50-58 #region protein kinase ATP-binding motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #modified_site aspartic acid (Asn) #status predicted\ !$11,339 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$55,56,122,128,171, !$184 #binding_site Mg-ATP (Phe, Gly, Glu, Glu, Glu, Thr) !8#status predicted\ !$73,92,167,169 #active_site Lys, Glu, Asp, Lys #status predicted\ !$172,185 #binding_site magnesium (Asn, Asp) #status predicted\ !$198 #binding_site phosphate (Thr) (covalent) #status !8predicted SUMMARY #length 351 #molecular-weight 40589 #checksum 6114 SEQUENCE /// ENTRY OKBO2C #type complete TITLE protein kinase (EC 2.7.1.37), cAMP-dependent, alpha catalytic chain - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Apr-1981 #sequence_revision 19-May-1995 #text_change 11-Jun-1999 ACCESSIONS S27159; A00620; A38010; S24961 REFERENCE S27159 !$#authors Wiemann, S.; Kinzel, V.; Pyerin, W. !$#journal Biochim. Biophys. Acta (1992) 1171:93-96 !$#title Cloning of the Calpha catalytic subunit of the bovine !1cAMP-dependent protein kinase. !$#cross-references MUID:93042013; PMID:1420367 !$#accession S27159 !'##molecule_type mRNA !'##residues 1-351 ##label WIE !'##cross-references EMBL:X67154; NID:g632; PIDN:CAA47627.1; PID:g633 REFERENCE A00620 !$#authors Shoji, S.; Ericsson, L.H.; Walsh, K.A.; Fischer, E.H.; !1Titani, K. !$#journal Biochemistry (1983) 22:3702-3709 !$#title Amino acid sequence of the catalytic subunit of bovine type !1II adenosine cyclic 3',5'-phosphate dependent protein !1kinase. !$#cross-references MUID:84000375; PMID:6311252 !$#accession A00620 !'##molecule_type protein !'##residues 2-286,'D',288-351 ##label SHO REFERENCE A38010 !$#authors Bramson, H.N.; Thomas, N.; Matsueda, R.; Nelson, N.C.; !1Taylor, S.S.; Kaiser, E.T. !$#journal J. Biol. Chem. (1982) 257:10575-10581 !$#title Modification of the catalytic subunit of bovine heart !1cAMP-dependent protein kinase with affinity labels related !1to peptide substrates. !$#cross-references MUID:82265755; PMID:6286662 !$#accession A38010 !'##molecule_type protein !'##residues 196-201,'N',203,'Q',205,'S',207-214 ##label BRA !'##note Cys-200 is close to or at the peptide substrate binding site COMMENT The inactive enzyme contains two regulatory chains and two !1catalytic chains. Activation by cAMP produces two active !1catalytic monomers and a regulatory dimer that binds four !1cAMP molecules. Two types found in mammalian tissue are !1distinguished by having either type I or type II regulatory !1chains. COMMENT Both alpha and beta catalytic chains are found in many !1tissues, with the alpha form being the more abundant. FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; blocked amino end; cAMP binding; lipoprotein; !1magnesium; myristylation; phosphoprotein; !1phosphotransferase; serine/threonine-specific protein kinase FEATURE !$42-298 #domain protein kinase homology #label KIN\ !$50-58 #region protein kinase ATP-binding motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status experimental\ !$3 #modified_site aspartic acid (Asn) #status !8experimental\ !$11 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$55,56,122,128,171, !$184 #binding_site Mg-ATP (Phe, Gly, Glu, Glu, Glu, Thr) !8#status predicted\ !$73,92,167,169 #active_site Lys, Glu, Asp, Lys #status predicted\ !$172,185 #binding_site magnesium (Asn, Asp) #status predicted\ !$198 #binding_site phosphate (Thr) (covalent) #status !8experimental\ !$339 #binding_site phosphate (Ser) (covalent) #status !8experimental SUMMARY #length 351 #molecular-weight 40619 #checksum 5963 SEQUENCE /// ENTRY OKRT2C #type complete TITLE protein kinase (EC 2.7.1.37), cAMP-dependent, alpha catalytic chain - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 11-Jun-1999 ACCESSIONS S16240 REFERENCE S16240 !$#authors Wiemann, S.; Voss, H.; Kinzel, V.; Pyerin, W. !$#journal Biochim. Biophys. Acta (1991) 1089:254-256 !$#title Rat C-alpha catalytic subunit of the cAMP-dependent protein !1kinase: cDNA sequence and evidence that it is the only !1isoform expressed in myoblasts. !$#cross-references MUID:91274359; PMID:1711374 !$#accession S16240 !'##molecule_type mRNA !'##residues 1-351 ##label WIE !'##cross-references EMBL:X57986; NID:g56911; PIDN:CAA41052.1; !1PID:g56912 COMMENT The inactive enzyme contains two regulatory chains and two !1catalytic chains. Activation by cAMP produces two active !1catalytic monomers and a regulatory dimer that binds four !1cAMP molecules. Two types found in mammalian tissue are !1distinguished by having either type I or type II regulatory !1chains. COMMENT Both alpha and beta catalytic chains are found in many !1tissues, with the alpha form being the more abundant. FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; blocked amino end; cAMP binding; heterotetramer; !1lipoprotein; magnesium; myristylation; phosphoprotein; !1phosphotransferase; serine/threonine-specific protein kinase FEATURE !$2-351 #product protein kinase, cAMP-dependent, alpha !8catalytic chain #status predicted #label MAT\ !$42-298 #domain protein kinase homology #label KIN\ !$50-58 #region protein kinase ATP-binding motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status experimental\ !$3 #modified_site aspartic acid (Asn) #status !8experimental\ !$11,339 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$55,56,122,128,171, !$184 #binding_site Mg-ATP (Phe, Gly, Glu, Glu, Glu, Thr) !8#status predicted\ !$73,92,167,169 #active_site Lys, Glu, Asp, Lys #status predicted\ !$172,185 #binding_site magnesium (Asn, Asp) #status predicted\ !$198 #binding_site phosphate (Thr) (covalent) #status !8predicted SUMMARY #length 351 #molecular-weight 40619 #checksum 6175 SEQUENCE /// ENTRY OKMSCA #type complete TITLE protein kinase (EC 2.7.1.37), cAMP-dependent, alpha catalytic chain - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 11-Jun-1999 ACCESSIONS A28619; A25125 REFERENCE A28619 !$#authors Chrivia, J.C.; Uhler, M.D.; McKnight, G.S. !$#journal J. Biol. Chem. (1988) 263:5739-5744 !$#title Characterization of genomic clones coding for the C-alpha !1and C-beta subunits of mouse cAMP-dependent protein kinase. !$#cross-references MUID:88186891; PMID:2833513 !$#accession A28619 !'##molecule_type DNA !'##residues 1-351 ##label CHR !'##cross-references GB:M19960; DDBJ:J03192; DDBJ:J03194; NID:g200377; !1PIDN:AAA39937.1; PID:g387513 REFERENCE A25125 !$#authors Uhler, M.D.; Carmichael, D.F.; Lee, D.C.; Chrivia, J.C.; !1Krebs, E.G.; McKnight, G.S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:1300-1304 !$#title Isolation of cDNA clones coding for the catalytic subunit of !1mouse cAMP-dependent protein kinase. !$#cross-references MUID:86149293; PMID:3456589 !$#accession A25125 !'##molecule_type mRNA !'##residues 1-32,'D',34-286,'D',288-351 ##label UHL !'##cross-references GB:M12303; NID:g200366; PIDN:AAA39936.1; !1PID:g200367 REFERENCE A47226 !$#authors Zheng, J.; Knighton, D.R.; Ten Eyck, L.F.; Karlsson, R.; !1Xuong, N.; Taylor, S.S.; Sowadski, J.M. !$#journal Biochemistry (1993) 32:2154-2161 !$#title Crystal structure of the catalytic subunit of cAMP-dependent !1protein kinase complexed with MgATP and peptide inhibitor. !$#cross-references MUID:93183878; PMID:8443157 !$#contents annotation; X-ray crystallography, 2.7 angstroms COMMENT The inactive enzyme contains two regulatory chains and two !1catalytic chains. Activation by cAMP produces two active !1catalytic monomers and a regulatory dimer that binds four !1cAMP molecules. Two types found in mammalian tissue are !1distinguished by having either type I or type II regulatory !1chains. COMMENT Both alpha and beta catalytic chains are found in many !1tissues, with the alpha form being the more abundant. GENETICS !$#introns 16/1; 36/3; 79/3; 112/3; 140/2; 182/3; 214/3; 255/3; 310/3 FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; blocked amino end; cAMP binding; heterotetramer; !1lipoprotein; magnesium; myristylation; phosphoprotein; !1phosphotransferase; serine/threonine-specific protein kinase FEATURE !$2-351 #product protein kinase, cAMP-dependent, alpha !8catalytic chain #status predicted #label MAT\ !$42-298 #domain protein kinase homology #label KIN\ !$50-58 #region protein kinase ATP-binding motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #modified_site aspartic acid (Asn) #status predicted\ !$11,339 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$55,56,122,128,171, !$184 #binding_site Mg-ATP (Phe, Gly, Glu, Glu, Glu, Thr) !8#status predicted\ !$73,92,167,169 #active_site Lys, Glu, Asp, Lys #status predicted\ !$172,185 #binding_site magnesium (Asn, Asp) #status predicted\ !$198 #binding_site phosphate (Thr) (covalent) #status !8predicted SUMMARY #length 351 #molecular-weight 40570 #checksum 6925 SEQUENCE /// ENTRY OKHYCA #type complete TITLE protein kinase (EC 2.7.1.37), cAMP-dependent, alpha catalytic chain - Chinese hamster ORGANISM #formal_name Cricetulus griseus #common_name Chinese hamster DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 11-Jun-1999 ACCESSIONS B40384 REFERENCE A40384 !$#authors Howard, P.; Day, K.H.; Kim, K.E.; Richardson, J.; Thomas, !1J.; Abraham, I.; Fleischmann, R.D.; Gottesman, M.M.; Maurer, !1R.A. !$#journal J. Biol. Chem. (1991) 266:10189-10195 !$#title Decreased catalytic subunit mRNA levels and altered !1catalytic subunit mRNA structure in a cAMP-resistant Chinese !1hamster ovary cell line. !$#cross-references MUID:91244783; PMID:1645343 !$#accession B40384 !'##molecule_type mRNA !'##residues 1-351 ##label HOW !'##cross-references GB:M63311; NID:g191174; PIDN:AAA37010.1; !1PID:g191175 COMMENT The inactive enzyme contains two regulatory chains and two !1catalytic chains. Activation by cAMP produces two active !1catalytic monomers and a regulatory dimer that binds four !1cAMP molecules. Two types found in mammalian tissue are !1distinguished by having either type I or type II regulatory !1chains. COMMENT Both alpha and beta catalytic chains are found in many !1tissues, with the alpha form being the more abundant. FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; blocked amino end; cAMP binding; heterotetramer; !1lipoprotein; magnesium; myristylation; phosphoprotein; !1phosphotransferase; serine/threonine-specific protein kinase FEATURE !$2-351 #product protein kinase, cAMP-dependent, alpha !8catalytic chain #status predicted #label MAT\ !$42-298 #domain protein kinase homology #label KIN\ !$50-58 #region protein kinase ATP-binding motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #modified_site aspartic acid (Asn) #status predicted\ !$11,339 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$55,56,122,128,171, !$184 #binding_site Mg-ATP (Phe, Gly, Glu, Glu, Glu, Thr) !8#status predicted\ !$73,92,167,169 #active_site Lys, Glu, Asp, Lys #status predicted\ !$172,185 #binding_site magnesium (Asn, Asp) #status predicted\ !$198 #binding_site phosphate (Thr) (covalent) #status !8predicted SUMMARY #length 351 #molecular-weight 40619 #checksum 6705 SEQUENCE /// ENTRY OKHUCB #type complete TITLE protein kinase (EC 2.7.1.37), cAMP-dependent, beta catalytic chain - human ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 11-Jun-1999 ACCESSIONS A34724 REFERENCE A34724 !$#authors Beebe, S.J.; Oyen, O.; Sandberg, M.; Froysa, A.; Hansson, !1V.; Jahnsen, T. !$#journal Mol. Endocrinol. (1990) 4:465-475 !$#title Molecular cloning of a tissue-specific protein kinase (C !1gamma) from human testis--representing a third isoform for !1the catalytic subunit of cAMP-dependent protein kinase. !$#cross-references MUID:90258940; PMID:2342480 !$#accession A34724 !'##molecule_type mRNA !'##residues 1-351 ##label BEE !'##cross-references GB:M34181; NID:g189982; PIDN:AAA60170.1; !1PID:g189983 COMMENT The inactive enzyme contains two regulatory chains and two !1catalytic chains. Activation by cAMP produces two active !1catalytic monomers and a regulatory dimer that binds four !1cAMP molecules. Two types found in mammalian tissue are !1distinguished by having either type I or type II regulatory !1chains. COMMENT Both alpha and beta catalytic chains are found in many !1tissues, with the alpha form being the more abundant. The !1highest concentrations of the beta form are found in brain. GENETICS !$#gene GDB:PRKACB !'##cross-references GDB:120718; OMIM:176892 !$#map_position 1p36.1-1p36.1 FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; blocked amino end; cAMP binding; heterotetramer; !1lipoprotein; magnesium; myristylation; phosphoprotein; !1phosphotransferase; serine/threonine-specific protein kinase FEATURE !$2-351 #product protein kinase, cAMP-dependent, beta !8catalytic chain #status predicted #label MAT\ !$42-298 #domain protein kinase homology #label KIN\ !$50-58 #region protein kinase ATP-binding motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #modified_site aspartic acid (Asn) #status predicted\ !$11,339 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$55,56,122,128,171, !$184 #binding_site Mg-ATP (Phe, Gly, Glu, Glu, Glu, Thr) !8#status predicted\ !$73,92,167,169 #active_site Lys, Glu, Asp, Lys #status predicted\ !$172,185 #binding_site magnesium (Asn, Asp) #status predicted\ !$198 #binding_site phosphate (Thr) (covalent) #status !8predicted SUMMARY #length 351 #molecular-weight 40622 #checksum 7229 SEQUENCE /// ENTRY OKBOB1 #type complete TITLE protein kinase (EC 2.7.1.37), cAMP-dependent, beta-1 catalytic chain - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 11-Jun-1999 ACCESSIONS A25334 REFERENCE A25334 !$#authors Showers, M.O.; Maurer, R.A. !$#journal J. Biol. Chem. (1986) 261:16288-16291 !$#title A cloned bovine cDNA encodes an alternate form of the !1catalytic subunit of cAMP-dependent protein kinase. !$#cross-references MUID:87057309; PMID:3023347 !$#accession A25334 !'##molecule_type mRNA !'##residues 1-351 ##label SHO !'##cross-references GB:J02647; NID:g163531; PIDN:AAA30707.1; !1PID:g163532 !'##note the authors translated the codon GAG for residue 42 as Gly COMMENT The inactive enzyme contains two regulatory chains and two !1catalytic chains. Activation by cAMP produces two active !1catalytic monomers and a regulatory dimer that binds four !1cAMP molecules. Two types found in mammalian tissue are !1distinguished by having either type I or type II regulatory !1chains. COMMENT Both alpha and beta catalytic chains are found in many !1tissues, with the alpha form being the more abundant. The !1highest concentrations of the beta form are found in brain. FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS alternative splicing; ATP; blocked amino end; cAMP binding; !1heterotetramer; lipoprotein; magnesium; myristylation; !1phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$2-351 #product protein kinase, cAMP-dependent, beta-1 !8catalytic chain #status predicted #label MAT\ !$42-298 #domain protein kinase homology #label KIN\ !$50-58 #region protein kinase ATP-binding motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #modified_site aspartic acid (Asn) #status predicted\ !$11,339 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$55,56,122,128,171, !$184 #binding_site Mg-ATP (Phe, Gly, Glu, Glu, Glu, Thr) !8#status predicted\ !$73,92,167,169 #active_site Lys, Glu, Asp, Lys #status predicted\ !$172,185 #binding_site magnesium (Asn, Asp) #status predicted\ !$198 #binding_site phosphate (Thr) (covalent) #status !8predicted SUMMARY #length 351 #molecular-weight 40593 #checksum 6518 SEQUENCE /// ENTRY OKRTCB #type complete TITLE protein kinase (EC 2.7.1.37), cAMP-dependent, beta catalytic chain - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jun-2000 ACCESSIONS JQ1139; S23134 REFERENCE JQ1139 !$#authors Shuntoh, H.; Sakamoto, N.; Saitoh, M.; Katayama, S.; !1Matsuyama, S.; Tanaka, C. !$#submission submitted to JIPID, August 1991 !$#accession JQ1139 !'##molecule_type mRNA !'##residues 1-351 ##label SHU REFERENCE S23134 !$#authors Shuntoh, H.; Sakamoto, N.; Matsuyama, S.; Saitoh, M.; !1Tanaka, C. !$#journal Biochim. Biophys. Acta (1992) 1131:175-180 !$#title Molecular structure of the Cbeta catalytic subunit of rat !1cAMP-dependent protein kinase and differential expression of !1Calpha and Cbeta isoforms in rat tissues and cultured cells. !$#cross-references MUID:92305056; PMID:1610898 !$#accession S23134 !'##status preliminary !'##molecule_type mRNA !'##residues 1-351 ##label SHU2 !'##cross-references EMBL:D10770; NID:g220703; PIDN:BAA01601.1; !1PID:g220704; EMBL:D01144 COMMENT The inactive enzyme contains two regulatory chains and two !1catalytic chains. Activation by cAMP produces two active !1catalytic monomers and a regulatory dimer that binds four !1cAMP molecules. Two types found in mammalian tissue are !1distinguished by having either type I or type II regulatory !1chains. COMMENT Both alpha and beta catalytic chains are found in many !1tissues, with the alpha form being the more abundant. The !1highest concentrations of the beta form are found in brain. CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; blocked amino end; cAMP binding; heterotetramer; !1lipoprotein; magnesium; myristylation; phosphoprotein; !1phosphotransferase; serine/threonine-specific protein kinase FEATURE !$2-351 #product protein kinase, cAMP-dependent, beta !8catalytic chain #status predicted #label MAT\ !$42-298 #domain protein kinase homology #label KIN\ !$50-58 #region protein kinase ATP-binding motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #modified_site aspartic acid (Asn) #status predicted\ !$55,56,122,128,171, !$184 #binding_site Mg-ATP (Phe, Gly, Glu, Glu, Glu, Thr) !8#status predicted\ !$73,92,167,169 #active_site Lys, Glu, Asp, Lys #status predicted\ !$172,185 #binding_site magnesium (Asn, Asp) #status predicted\ !$198 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$339 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 351 #molecular-weight 40708 #checksum 8058 SEQUENCE /// ENTRY OKMSCB #type complete TITLE protein kinase (EC 2.7.1.37), cAMP-dependent, beta catalytic chain - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 11-Jun-1999 ACCESSIONS A24596; B28619; S37708 REFERENCE A24596 !$#authors Uhler, M.D.; Chrivia, J.C.; McKnight, G.S. !$#journal J. Biol. Chem. (1986) 261:15360-15363 !$#title Evidence for a second isoform of the catalytic subunit of !1cAMP-dependent protein kinase. !$#cross-references MUID:87057152; PMID:3023318 !$#accession A24596 !'##molecule_type mRNA !'##residues 1-351 ##label UHL !'##cross-references GB:J02626; NID:g200386; PIDN:AAA39941.1; !1PID:g200387 REFERENCE A28619 !$#authors Chrivia, J.C.; Uhler, M.D.; McKnight, G.S. !$#journal J. Biol. Chem. (1988) 263:5739-5744 !$#title Characterization of genomic clones coding for the C-alpha !1and C-beta subunits of mouse cAMP-dependent protein kinase. !$#cross-references MUID:88186891; PMID:2833513 !$#accession B28619 !'##molecule_type DNA !'##residues 1-15 ##label CHR !'##cross-references GB:M21096; GB:J03192; GB:J03194; NID:g200382; !1PIDN:AAA39938.1; PID:g554257 REFERENCE S37707 !$#authors Kato, K. !$#journal J. Neurosci. (1991) 2:704-711 !$#title A collection of cDNA clones with specific expression !1patterns in mouse brain. !$#accession S37708 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type mRNA !'##residues 281-351 ##label KAT !'##cross-references EMBL:X61434; NID:g50282; PIDN:CAA43676.1; !1PID:g50283 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1991 COMMENT The inactive enzyme contains two regulatory chains and two !1catalytic chains. Activation by cAMP produces two active !1catalytic monomers and a regulatory dimer that binds four !1cAMP molecules. Two types found in mammalian tissue are !1distinguished by having either type I or type II regulatory !1chains. COMMENT Both alpha and beta catalytic chains are found in many !1tissues, with the alpha form being the more abundant. The !1highest concentrations of the beta form are found in brain. GENETICS !$#introns 16/1 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; blocked amino end; cAMP binding; heterotetramer; !1lipoprotein; magnesium; myristylation; phosphoprotein; !1phosphotransferase; serine/threonine-specific protein kinase FEATURE !$2-351 #product protein kinase, cAMP-dependent, beta !8catalytic chain #status predicted #label MAT\ !$42-298 #domain protein kinase homology #label KIN\ !$50-58 #region protein kinase ATP-binding motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #modified_site aspartic acid (Asn) #status predicted\ !$55,56,122,128,171, !$184 #binding_site Mg-ATP (Phe, Gly, Glu, Glu, Glu, Thr) !8#status predicted\ !$73,92,167,169 #active_site Lys, Glu, Asp, Lys #status predicted\ !$172,185 #binding_site magnesium (Asn, Asp) #status predicted\ !$198 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$339 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 351 #molecular-weight 40708 #checksum 8058 SEQUENCE /// ENTRY OKHYCB #type complete TITLE protein kinase (EC 2.7.1.37), cAMP-dependent, beta catalytic chain - Chinese hamster ORGANISM #formal_name Cricetulus griseus #common_name Chinese hamster DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 11-Jun-1999 ACCESSIONS A40384 REFERENCE A40384 !$#authors Howard, P.; Day, K.H.; Kim, K.E.; Richardson, J.; Thomas, !1J.; Abraham, I.; Fleischmann, R.D.; Gottesman, M.M.; Maurer, !1R.A. !$#journal J. Biol. Chem. (1991) 266:10189-10195 !$#title Decreased catalytic subunit mRNA levels and altered !1catalytic subunit mRNA structure in a cAMP-resistant Chinese !1hamster ovary cell line. !$#cross-references MUID:91244783; PMID:1645343 !$#accession A40384 !'##molecule_type mRNA !'##residues 1-351 ##label HOW !'##cross-references GB:M63312; NID:g191176; PIDN:AAA37011.1; !1PID:g191177 COMMENT The inactive enzyme contains two regulatory chains and two !1catalytic chains. Activation by cAMP produces two active !1catalytic monomers and a regulatory dimer that binds four !1cAMP molecules. Two types found in mammalian tissue are !1distinguished by having either type I or type II regulatory !1chains. COMMENT Both alpha and beta catalytic chains are found in many !1tissues, with the alpha form being the more abundant. The !1highest concentrations of the beta form are found in brain. CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; blocked amino end; cAMP binding; heterotetramer; !1lipoprotein; magnesium; myristylation; phosphoprotein; !1phosphotransferase; serine/threonine-specific protein kinase FEATURE !$2-351 #product protein kinase, cAMP-dependent, beta !8catalytic chain #status predicted #label MAT\ !$42-298 #domain protein kinase homology #label KIN\ !$50-58 #region protein kinase ATP-binding motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #modified_site aspartic acid (Asn) #status predicted\ !$55,56,122,128,171, !$184 #binding_site Mg-ATP (Phe, Gly, Glu, Glu, Glu, Thr) !8#status predicted\ !$73,92,167,169 #active_site Lys, Glu, Asp, Lys #status predicted\ !$172,185 #binding_site magnesium (Asn, Asp) #status predicted\ !$198 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$339 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 351 #molecular-weight 40708 #checksum 8058 SEQUENCE /// ENTRY OKBOB2 #type complete TITLE protein kinase (EC 2.7.1.37), cAMP-dependent, beta-2 catalytic chain - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 11-Jun-1999 ACCESSIONS A23716 REFERENCE A23716 !$#authors Wiemann, S.; Kinzel, V.; Pyerin, W. !$#journal J. Biol. Chem. (1991) 266:5140-5146 !$#title Isoform Cbeta2, an unusual form of the bovine catalytic !1subunit of cAMP-dependent protein kinase. !$#cross-references MUID:91161607; PMID:2002051 !$#accession A23716 !'##molecule_type mRNA !'##residues 1-397 ##label WIE !'##cross-references GB:M60482; NID:g162786; PIDN:AAA30424.1; !1PID:g162787 COMMENT The inactive enzyme contains two regulatory chains and two !1catalytic chains. Activation by cAMP produces two active !1catalytic monomers and a regulatory dimer that binds four !1cAMP molecules. Two types found in mammalian tissue are !1distinguished by having either type I or type II regulatory !1chains. COMMENT Both alpha and beta catalytic chains are found in many !1tissues, with the alpha form being the more abundant. The !1highest concentrations of the beta forms are found in brain. CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS alternative splicing; ATP; cAMP binding; heterotetramer; !1magnesium; phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$2-397 #product protein kinase, cAMP-dependent, beta-2 !8catalytic chain #status predicted #label MAT\ !$88-344 #domain protein kinase homology #label KIN\ !$96-104 #region protein kinase ATP-binding motif\ !$101,102,168,174, !$217,230 #binding_site Mg-ATP (Phe, Gly, Glu, Glu, Glu, Thr) !8#status predicted\ !$119,138,213,215 #active_site Lys, Glu, Asp, Lys #status predicted\ !$218,231 #binding_site magnesium (Asn, Asp) #status predicted\ !$244 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$385 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 397 #molecular-weight 46107 #checksum 9126 SEQUENCE /// ENTRY OKHUCG #type complete TITLE protein kinase (EC 2.7.1.37), cAMP-dependent, gamma catalytic chain - human ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 11-Jun-1999 ACCESSIONS B34724 REFERENCE A34724 !$#authors Beebe, S.J.; Oyen, O.; Sandberg, M.; Froysa, A.; Hansson, !1V.; Jahnsen, T. !$#journal Mol. Endocrinol. (1990) 4:465-475 !$#title Molecular cloning of a tissue-specific protein kinase (C !1gamma) from human testis--representing a third isoform for !1the catalytic subunit of cAMP-dependent protein kinase. !$#cross-references MUID:90258940; PMID:2342480 !$#accession B34724 !'##molecule_type mRNA !'##residues 1-360 ##label BEE !'##cross-references GB:M34182; NID:g189986; PIDN:AAC41690.1; !1PID:g189987 !'##note it is uncertain whether Met-1 or Met-10 is the initiator COMMENT The inactive enzyme contains two regulatory chains and two !1catalytic chains. Activation by cAMP produces two active !1catalytic monomers and a regulatory dimer that binds four !1cAMP molecules. Two types found in mammalian tissue are !1distinguished by having either type I or type II regulatory !1chains. COMMENT The gamma catalytic chain has been detected only in testis. GENETICS !$#gene GDB:PRKACG !'##cross-references GDB:120719; OMIM:176893 !$#map_position 9q13-9q13 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; autophosphorylation; blocked amino end; cAMP binding; !1heterotetramer; lipoprotein; magnesium; myristylation; !1phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$11-360 #product protein kinase, cAMP-dependent, gamma !8catalytic chain #status predicted #label MAT\ !$51-307 #domain protein kinase homology #label KIN\ !$59-67 #region protein kinase ATP-binding motif\ !$11 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$12 #modified_site aspartic acid (Asn) #status predicted\ !$64,65,131,137,180, !$193 #binding_site Mg-ATP (Phe, Gly, Glu, Glu, Glu, Thr) !8#status predicted\ !$82,101,176,178 #active_site Lys, Glu, Asp, Lys #status predicted\ !$181,194 #binding_site magnesium (Asn, Asp) #status predicted\ !$207 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$348 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 360 #molecular-weight 41168 #checksum 8990 SEQUENCE /// ENTRY OKKWC1 #type complete TITLE protein kinase (EC 2.7.1.37), cAMP-dependent, catalytic chain 1 - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 05-Dec-1997 ACCESSIONS A35755 REFERENCE A35755 !$#authors Gross, R.E.; Bagchi, S.; Lu, X.; Rubin, C.S. !$#journal J. Biol. Chem. (1990) 265:6896-6907 !$#title Cloning, characterization, and expression of the gene for !1the catalytic subunit of cAMP-dependent protein kinase in !1Caenorhabditis elegans. Identification of highly conserved !1and unique isoforms generated by alternative splicing. !$#cross-references MUID:90216721; PMID:2324104 !$#accession A35755 !'##molecule_type mRNA !'##residues 1-359 ##label GRO !'##cross-references GB:J05289 GENETICS !$#introns 24/1; 44/3; 87/3; 121/1; 190/3; 318/3 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS alternative splicing; ATP; cAMP binding; heterotetramer; !1magnesium; phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$2-359 #product protein kinase, cAMP-dependent, catalytic !8chain 1 #status predicted #label MAT\ !$50-306 #domain protein kinase homology #label KIN\ !$58-66 #region protein kinase ATP-binding motif\ !$63,64,130,136,179, !$192 #binding_site Mg-ATP (Phe, Gly, Glu, Glu, Glu, Thr) !8#status predicted\ !$81,100,175,177 #active_site Lys, Glu, Asp, Lys #status predicted\ !$180,193 #binding_site magnesium (Asn, Asp) #status predicted\ !$206 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$347 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 359 #molecular-weight 41327 #checksum 702 SEQUENCE /// ENTRY OKKWC2 #type complete TITLE protein kinase (EC 2.7.1.37), cAMP-dependent, catalytic chain 2 - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 21-Jul-2000 ACCESSIONS B35755; T37313 REFERENCE A35755 !$#authors Gross, R.E.; Bagchi, S.; Lu, X.; Rubin, C.S. !$#journal J. Biol. Chem. (1990) 265:6896-6907 !$#title Cloning, characterization, and expression of the gene for !1the catalytic subunit of cAMP-dependent protein kinase in !1Caenorhabditis elegans. Identification of highly conserved !1and unique isoforms generated by alternative splicing. !$#cross-references MUID:90216721; PMID:2324104 !$#accession B35755 !'##molecule_type mRNA !'##residues 1-375 ##label GRO !'##cross-references GB:J05289 !$#accession T37313 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-375 ##label GR2 !'##cross-references EMBL:M37119; NID:g156230; PIDN:AAA51610.1; !1PID:g156233 GENETICS !$#introns 24/1; 44/3; 87/3; 121/1; 190/3; 318/3 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS alternative splicing; ATP; cAMP binding; heterotetramer; !1magnesium; phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$2-375 #product protein kinase, cAMP-dependent, catalytic !8chain 1 #status predicted #label MAT\ !$50-306 #domain protein kinase homology #label KIN\ !$58-66 #region protein kinase ATP-binding motif\ !$63,64,130,136,179, !$192 #binding_site Mg-ATP (Phe, Gly, Glu, Glu, Glu, Thr) !8#status predicted\ !$81,100,175,177 #active_site Lys, Glu, Asp, Lys #status predicted\ !$180,193 #binding_site magnesium (Asn, Asp) #status predicted\ !$206 #binding_site phosphate (Thr) (covalent) #status !8predicted SUMMARY #length 375 #molecular-weight 43158 #checksum 5784 SEQUENCE /// ENTRY JC6094 #type complete TITLE MAPK-activated protein kinase (EC 2.7.1.-) 3 - human ALTERNATE_NAMES mitogen-activated protein kinase-activated protein kinase 3pK ORGANISM #formal_name Homo sapiens #common_name man DATE 18-Feb-2000 #sequence_revision 18-Feb-2000 #text_change 18-Feb-2000 ACCESSIONS JC6094 REFERENCE JC6094 !$#authors Sithanandam, G.; Latif, F.; Duh, F.M.; Bernal, R.; Smola, !1U.; Li, H.; Kuzmin, I.; Wixler, V.; Geil, L.; Shrestha, S.; !1Lloyd, P.A.; Bader, S.; Sekido, Y.; Tartof, K.D.; Kashuba, !1V.I.; Zabarovsky, E.R.; Dean, M.; Klein, G.; Lerman, M.I.; !1Minna, J.D.; Rapp, U.R.; Allikmets, R. !$#journal Mol. Cell. Biol. (1996) 16:868-876 !$#title 3pK, a new mitogen-activated protein kinase-activated !1protein kinase located in the small cell lung cancer tumor !1suppressor gene region. !$#cross-references MUID:96182089; PMID:8622688 !$#accession JC6094 !'##molecule_type mRNA !'##residues 1-382 ##label SIT !'##cross-references GB:U09578; NID:g1209017; PIDN:AAD09136.1; !1PID:g1209018 !'##experimental_source heart GENETICS !$#gene GDB:MAPKAP; 3pK !'##cross-references GDB:6175915 !$#map_position 3p21.3 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$12-16 #region proline-rich\ !$41-304 #domain protein kinase homology #label KIN\ !$50-58 #region protein kinase ATP-binding motif\ !$364-368 #region nuclear location signal\ !$313 #binding_site phosphate (Thr) (covalent) (by MAP !8kinase) #status predicted SUMMARY #length 382 #molecular-weight 42987 #checksum 8259 SEQUENCE /// ENTRY OKBYC1 #type complete TITLE protein kinase (EC 2.7.1.37), cAMP-dependent, catalytic chain 1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES cdc25-suppressing protein kinase PK-25; protein J0541; protein YJL164c ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Dec-1993 #sequence_revision 31-May-1996 #text_change 21-Jul-2000 ACCESSIONS JC1034; A27070; A29554; S56947; C26911 REFERENCE JC1034 !$#authors Chen, C.Z.; Yang, Y.; Xia, Q.C.; Li, B.L. !$#journal Acta Biochim. Biophys. Sin. (1994) 26:197-205 !$#title Cloning and expression of the TPKA gene, coding for the !1catalytic subunit of cAMP-dependent protein kinase from S. !1cerevisiae. !$#accession JC1034 !'##molecule_type DNA !'##residues 1-399 ##label CHE REFERENCE A90896 !$#authors Toda, T.; Cameron, S.; Sass, P.; Zoller, M.; Wigler, M. !$#journal Cell (1987) 50:277-287 !$#title Three different genes in S. cerevisiae encode the catalytic !1subunits of the cAMP-dependent protein kinase. !$#cross-references MUID:87244343; PMID:3036373 !$#accession A27070 !'##molecule_type DNA !'##residues 3-287,'N',289-399 ##label TOD !'##cross-references EMBL:M17072; NID:g173008; PIDN:AAA35164.1; !1PID:g173009 REFERENCE A29554 !$#authors Lisziewicz, J.; Godany, A.; Foerster, H.H.; Kuentzel, H. !$#journal J. Biol. Chem. (1987) 262:2549-2553 !$#title Isolation and nucleotide sequence of a Saccharomyces !1cerevisiae protein kinase gene suppressing the cell cycle !1start mutation cdc25. !$#cross-references MUID:87137496; PMID:3546292 !$#accession A29554 !'##molecule_type DNA !'##residues 3-287,'N',289-399 ##label LIS !'##cross-references EMBL:J02665; NID:g172174; PIDN:AAA34877.1; !1PID:g172175 REFERENCE S56937 !$#authors Obermaier, B.; Piravandi, E.; Rinke, M.; Domdey, H. !$#submission submitted to the Protein Sequence Database, September 1995 !$#accession S56947 !'##molecule_type DNA !'##residues 3-80,'V',82,'SIVYKN',89-287,'N',289-399 ##label OBE !'##cross-references EMBL:Z49439; NID:g1008351; PIDN:CAA89459.1; !1PID:g1008352; GSPDB:GN00010; MIPS:YJL164c REFERENCE A93094 !$#authors Cannon, J.F.; Tatchell, K. !$#journal Mol. Cell. Biol. (1987) 7:2653-2663 !$#title Characterization of Saccharomyces cerevisiae genes encoding !1subunits of cyclic AMP-dependent protein kinase. !$#cross-references MUID:88038803; PMID:2823100 !$#accession C26911 !'##molecule_type DNA !'##residues 'MCERINFL',2-80,'V',82,'SIVYKN',89-165,'ILKV',170,'R', !1174-181,'KD',184-189,'QIF',193-287,'N',289-399 ##label CAN !'##cross-references EMBL:M17224; NID:g172690; PIDN:AAA35088.1; !1PID:g172691 GENETICS !$#gene SGD:SRA3; TPK1; MIPS:YJL164c !'##cross-references SGD:S0003700; MIPS:YJL164c !$#map_position 10L COMPLEX heterotetramer FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; cAMP binding; heterotetramer; magnesium; !1phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$87-343 #domain protein kinase homology #label KIN\ !$95-103 #region protein kinase ATP-binding motif\ !$100,101,167,173, !$216,229 #binding_site Mg-ATP (Phe, Gly, Asp, Glu, Glu, Thr) !8#status predicted\ !$118,137,212,214 #active_site Lys, Glu, Asp, Lys #status predicted\ !$217,230 #binding_site magnesium (Asn, Asp) #status predicted\ !$243 #binding_site phosphate (Thr) (covalent) #status !8predicted SUMMARY #length 399 #molecular-weight 46265 #checksum 4307 SEQUENCE /// ENTRY OKBYC2 #type complete TITLE protein kinase (EC 2.7.1.37), cAMP-dependent, catalytic chain 2 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein kinase YKR; protein P1855; protein YPL203w ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Dec-1993 #sequence_revision 26-Jul-1996 #text_change 19-Apr-2002 ACCESSIONS S65222; B27070; S00125 REFERENCE S65202 !$#authors Rieger, M.; Mueller-Auer, S.; Schaefer, M. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S65222 !'##molecule_type DNA !'##residues 1-380 ##label RIE !'##cross-references EMBL:Z73559; NID:g1370421; PIDN:CAA97917.1; !1PID:g1370422; GSPDB:GN00016; MIPS:YPL203w !'##experimental_source strain S288C (AB972) REFERENCE A90896 !$#authors Toda, T.; Cameron, S.; Sass, P.; Zoller, M.; Wigler, M. !$#journal Cell (1987) 50:277-287 !$#title Three different genes in S. cerevisiae encode the catalytic !1subunits of the cAMP-dependent protein kinase. !$#cross-references MUID:87244343; PMID:3036373 !$#accession B27070 !'##molecule_type DNA !'##residues 1-288,'Q',290-380 ##label TOD !'##cross-references EMBL:M17073; NID:g173010; PIDN:AAA35165.1; !1PID:g173011 REFERENCE S00125 !$#authors Ohno, S.; Aoshima, M.; Matsumoto, S.; Yahara, I.; Suzuki, K. !$#journal FEBS Lett. (1987) 222:279-285 !$#title A yeast gene coding for a putative protein kinase homologous !1to cdc25 suppressing protein kinase. !$#cross-references MUID:88005168; PMID:3308514 !$#accession S00125 !'##molecule_type DNA !'##residues 1-213,'LRQRGTN',221-259,'V',261-380 ##label OHN !'##cross-references EMBL:Y00694; NID:g4624; PIDN:CAA68689.1; PID:g4625 GENETICS !$#gene SGD:TPK2; TPK2; YKR1; PKA2; MIPS:YPL203w !'##cross-references SGD:S0006124 !$#map_position 16L CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; cAMP binding; heterotetramer; magnesium; !1phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$2-380 #product protein kinase, cAMP-dependent, catalytic !8chain 2 #status predicted #label MAT\ !$68-324 #domain protein kinase homology #label KIN\ !$76-84 #region protein kinase ATP-binding motif\ !$81,82,148,154,197, !$210 #binding_site Mg-ATP (Phe, Gly, Asp, Glu, Glu, Thr) !8#status predicted\ !$99,118,193,195 #active_site Lys, Glu, Asp, Lys #status predicted\ !$198,211 #binding_site magnesium (Asn, Asp) #status predicted\ !$224 #binding_site phosphate (Thr) (covalent) #status !8predicted SUMMARY #length 380 #molecular-weight 44219 #checksum 4916 SEQUENCE /// ENTRY OKBYC3 #type complete TITLE protein kinase (EC 2.7.1.37), cAMP-dependent, catalytic chain 3 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YKL166c; protein YKL630 ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Dec-1993 #sequence_revision 02-May-1994 #text_change 12-Nov-1999 ACCESSIONS S37996; S44595; C27070; S38415 REFERENCE S37976 !$#authors Vandenbol, M.; Bolle, P.A.; Dion, C.; Portetelle, D.; !1Hilger, F. !$#submission submitted to the Protein Sequence Database, March 1994 !$#accession S37996 !'##molecule_type DNA !'##residues 1-398 ##label VAN !'##cross-references EMBL:Z28166; NID:g486290; PIDN:CAA82008.1; !1PID:g486291; GSPDB:GN00011; MIPS:YKL166c !'##experimental_source S288C REFERENCE S44583 !$#authors Vandenbol, M.; Bolle, P.A.; Dion, C.; Portetelle, D.; !1Hilger, F. !$#journal Yeast (1994) 10:25-33 !$#title Sequencing and analysis of a 20.5 kb DNA segment located on !1the left arm of yeast chromosome XI. !$#accession S44595 !'##status translation not shown !'##molecule_type DNA !'##residues 1-398 ##label VA2 !'##cross-references EMBL:Z26878; NID:g407503; PIDN:CAA81521.1; !1PID:g407516 !'##experimental_source S288C REFERENCE A90896 !$#authors Toda, T.; Cameron, S.; Sass, P.; Zoller, M.; Wigler, M. !$#journal Cell (1987) 50:277-287 !$#title Three different genes in S. cerevisiae encode the catalytic !1subunits of the cAMP-dependent protein kinase. !$#cross-references MUID:87244343; PMID:3036373 !$#accession C27070 !'##molecule_type DNA !'##residues 1-3,'E',5-207,'T',209-398 ##label TOD !'##cross-references EMBL:M17074; NID:g173012; PIDN:AAA35166.1; !1PID:g173013 GENETICS !$#gene SGD:TPK3; MIPS:YKL166c !'##cross-references SGD:S0001649; MIPS:YKL166c !$#map_position 11L CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; cAMP binding; heterotetramer; magnesium; !1phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$2-398 #product protein kinase, cAMP-dependent, catalytic !8chain 3 #status predicted #label MAT\ !$86-342 #domain protein kinase homology #label KIN\ !$94-102 #region protein kinase ATP-binding motif\ !$99,100,166,172,215, !$228 #binding_site Mg-ATP (Phe, Gly, Asp, Glu, Glu, Thr) !8#status predicted\ !$117,136,211,213 #active_site Lys, Glu, Asp, Lys #status predicted\ !$216,229 #binding_site magnesium (Asn, Asp) #status predicted\ !$242 #binding_site phosphate (Thr) (covalent) #status !8predicted SUMMARY #length 398 #molecular-weight 45977 #checksum 2781 SEQUENCE /// ENTRY OKGASA #type complete TITLE protein kinase (EC 2.7.1.37) sak - California sea hare ALTERNATE_NAMES spermatozoon-associated kinase ORGANISM #formal_name Aplysia californica #common_name California sea hare DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 11-Jun-1999 ACCESSIONS A36371; B36371 REFERENCE A36371 !$#authors Beushausen, S.; Bayley, H. !$#journal Mol. Cell. Biol. (1990) 10:6775-6780 !$#title A relative of the catalytic subunit of cyclic AMP-dependent !1protein kinase in Aplysia spermatozoa. !$#cross-references MUID:91061788; PMID:1701024 !$#accession A36371 !'##molecule_type DNA !'##residues 1-351 ##label BEU !'##cross-references GB:M59380; GB:M38049; NID:g155721; PIDN:AAA27745.1; !1PID:g155722 !$#accession B36371 !'##molecule_type DNA !'##residues 86-126 ##label BE2 COMMENT This protein is found in the ovotestis, particularly in !1spermatogenic cells. It may play a role in fertilization. GENETICS !$#introns 85/3 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; magnesium; phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$2-351 #product protein kinase sak #status predicted #label !8MAT\ !$40-298 #domain protein kinase homology #label KIN\ !$48-56 #region protein kinase ATP-binding motif\ !$53,54,122,128,171, !$184 #binding_site Mg-ATP (Phe, Gly, Glu, Glu, Glu, Thr) !8#status predicted\ !$73,92,167,169 #active_site Lys, Glu, Asp, Lys #status predicted\ !$172,185 #binding_site magnesium (Asn, Asp) #status predicted\ !$198 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$339 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 351 #molecular-weight 40994 #checksum 6287 SEQUENCE /// ENTRY A45100 #type complete TITLE mitogen-activated protein kinase kinase (EC 2.7.1.-) 1, splice form A [validated] - human ALTERNATE_NAMES extracellular signal-regulated kinase activator kinase 1 (ERK kinase 1); MAP kinase kinase 1 (MAPKK1); MEK1 CONTAINS MAP kinase kinase 1, splice form B; protein kinase (EC 2.7.1.37); protein-tyrosine kinase (EC 2.7.1.112) ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Jun-1993 #sequence_revision 18-Nov-1994 #text_change 08-Dec-2000 ACCESSIONS A45100; B45100; B46723; JC2504 REFERENCE A45100 !$#authors Seger, R.; Seger, D.; Lozeman, F.J.; Ahn, N.G.; Graves, !1L.M.; Campbell, J.S.; Ericsson, L.; Harrylock, M.; Jensen, !1A.M.; Krebs, E.G. !$#journal J. Biol. Chem. (1992) 267:25628-25631 !$#title Human T-cell mitogen-activated protein kinase kinases are !1related to yeast signal transduction kinases. !$#cross-references MUID:93100262; PMID:1281467 !$#accession A45100 !'##molecule_type mRNA; protein !'##residues 1-393 ##label SEG1 !'##cross-references GB:L05624; NID:g188568; PIDN:AAA36318.1; !1PID:g188569 !'##experimental_source T-cells !'##note sequence extracted from NCBI backbone (NCBIN:120827, !1NCBIP:120828) !$#accession B45100 !'##molecule_type mRNA; protein !'##residues 1-146,173-393 ##label SEG2 !'##cross-references GB:L05624; NID:g188568 !'##experimental_source T-cells !'##note sequence extracted from NCBI backbone (NCBIN:120837, !1NCBIP:120838) REFERENCE A46723 !$#authors Zheng, C.F.; Guan, K.L. !$#journal J. Biol. Chem. (1993) 268:11435-11439 !$#title Cloning and characterization of two distinct human !1extracellular signal-regulated kinase activator kinases, !1MEK1 and MEK2. !$#cross-references MUID:93266604; PMID:8388392 !$#accession B46723 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-295,'G',296-393 ##label ZHE !'##cross-references GB:L11284; NID:g307183 !'##note sequence extracted from NCBI backbone (NCBIP:132852) REFERENCE JC2504 !$#authors Mansour, S.J.; Resing, K.A.; Candi, J.M.; Hermann, A.S.; !1Gloor, J.W.; Herskind, K.R.; Wartmann, M.; Davis, R.J.; Ahn, !1N.G. !$#journal J. Biochem. (1994) 116:304-314 !$#title Mitogen-activated protein (MAP) kinase phosphorylation of !1MAP kinase kinase: Determination of phosphorylation sites by !1mass spectrometry and site-directed mutagenesis. !$#cross-references MUID:95122457; PMID:7822248 !$#accession JC2504 !'##molecule_type protein !'##residues 5-96;98-349;354-393 ##label MAN !'##note phosphorylation sites determined in vitro COMMENT This enzyme is activated by protein kinase raf-1 (see !1PIR:A00637). It in turn is responsible for activating MAP !1kinase (see PIR:A48082 and PIR:JQ1400). See also PIR:A46723. GENETICS !$#gene GDB:PRKMK1; MEK1; MAPKK1 !'##cross-references GDB:136418; OMIM:176872 COMPLEX monomer FUNCTION !$#description catalyzes the formation of specific !1peptidyl-threonine-phosphate and peptidyl-tyrosine-phosphate !1residues in MAP kinase using ATP !$#pathway MAP kinase cascade CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS alternative splicing; ATP; monomer; phosphoprotein; !1phosphotransferase; serine/threonine/tyrosine-specific !1protein kinase; signal transduction FEATURE !$1-393 #product MAP kinase kinase 1, splice form A #status !8experimental #label MATA\ !$1-146,173-393 #product MAP kinase kinase 1, splice form B #status !8predicted #label MATB\ !$66-361 #domain protein kinase homology #label KIN\ !$74-82 #region protein kinase ATP-binding motif\ !$97,114,190,192 #active_site Lys, Glu, Asp, Lys #status predicted\ !$218,222 #binding_site phosphate (Ser) (covalent) (by raf-1 !8kinase) #status predicted\ !$292,386 #binding_site phosphate (Thr) (covalent) (by raf-1 !8kinase) #status experimental SUMMARY #length 393 #molecular-weight 43439 #checksum 9929 SEQUENCE /// ENTRY S42068 #type complete TITLE mitogen-activated protein kinase kinase (EC 2.7.1.-) 1, splice form A - rabbit ALTERNATE_NAMES ERK kinase 1; extracellular signal-regulated kinase activator kinase 1; MAP kinase kinase 1; MAPKK1; MEK1 CONTAINS mitogen-activated protein kinase kinase 1B ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 06-Jan-1995 #sequence_revision 06-Jan-1995 #text_change 11-Jun-1999 ACCESSIONS S42068 REFERENCE S42068 !$#authors Ashworth, A. !$#submission submitted to the EMBL Data Library, February 1994 !$#description cDNA sequence of rabbit MAP kinase kinase 1. !$#accession S42068 !'##status preliminary !'##molecule_type mRNA !'##residues 1-393 ##label ASH !'##cross-references EMBL:Z30163; NID:g456201; PIDN:CAA82912.1; !1PID:g456202 COMPLEX monomer FUNCTION !$#description catalyzes the formation of specific !1peptidyl-threonine-phosphate and peptidyl-tyrosine-phosphate !1residues in mitogen-activated protein kinase using ATP !$#pathway growth factor-stimulated cascade in which Raf-1, MAPKK, and !1MAPK are sequentially activated CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS alternative splicing; ATP; phosphoprotein; !1phosphotransferase; serine/threonine/tyrosine-specific !1protein kinase FEATURE !$1-146,173-393 #product mitogen-activated protein kinase kinase 1, !8splice form B #status predicted #label F1B\ !$66-361 #domain protein kinase homology #label KIN\ !$74-82 #region protein kinase ATP-binding motif\ !$97,114,190,192 #active_site Lys, Glu, Asp, Lys #status predicted\ !$292,386 #binding_site phosphate (Thr) (covalent) (by MAP !8kinase) #status predicted SUMMARY #length 393 #molecular-weight 43453 #checksum 9671 SEQUENCE /// ENTRY JN0840 #type complete TITLE mitogen-activated protein kinase kinase (EC 2.7.1.-) 1, splice form A - rat ALTERNATE_NAMES ERK kinase 1; extracellular signal-regulated kinase activator kinase 1; MAP kinase kinase 1; MAPKK1; MEK1 CONTAINS mitogen-activated protein kinase kinase 1B ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 03-Feb-1994 #sequence_revision 03-Feb-1994 #text_change 16-Jun-2000 ACCESSIONS JN0840; PN0645; A47177; S29863; S32411 REFERENCE JN0840 !$#authors Doering, F.; Drewes, G.; Berling, B.; Mandelkow, E.M. !$#journal Gene (1993) 131:303-304 !$#title Cloning and sequencing of a cDNA encoding rat brain !1mitogen-activated protein (MAP) kinase activator. !$#cross-references MUID:94010327; PMID:8406028 !$#accession JN0840 !'##molecule_type mRNA !'##residues 1-393 ##label DOE !'##cross-references GB:X62313; NID:g407860; PIDN:CAA44192.1; !1PID:g407861 !$#accession PN0645 !'##molecule_type protein !'##residues 3-14;50-57;71-84;176-183 ##label DO2 REFERENCE A47177 !$#authors Wu, J.; Harrison, J.K.; Vincent, L.A.; Haystead, C.; !1Haystead, T.A.; Michel, H.; Hunt, D.F.; Lynch, K.R.; !1Sturgill, T.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:173-177 !$#title Molecular structure of a protein-tyrosine/threonine kinase !1activating p42 mitogen-activated protein (MAP) kinase: MAP !1kinase kinase. !$#cross-references MUID:93126336; PMID:8380494 !$#accession A47177 !'##molecule_type mRNA !'##residues 1-393 ##label WU1 !'##cross-references GB:Z16415; NID:g56628; PIDN:CAA78905.1; PID:g56629; !1GB:L04485; NID:g205309; PID:g205310 !'##experimental_source kidney !'##note sequence extracted from NCBI backbone (NCBIN:121997, !1NCBIP:121998) REFERENCE S29863 !$#authors Wu, J. !$#submission submitted to the EMBL Data Library, October 1992 !$#accession S29863 !'##status preliminary !'##molecule_type mRNA !'##residues 1-393 ##label WUJ !'##cross-references EMBL:Z16415; NID:g56628; PIDN:CAA78905.1; !1PID:g56629 REFERENCE S32411 !$#authors Otsu, M.; Terada, Y.; Okayama, H. !$#journal FEBS Lett. (1993) 320:246-250 !$#title Isolation of two members of the rat MAP kinase kinase gene !1family. !$#cross-references MUID:93215844; PMID:8462694 !$#accession S32411 !'##status preliminary !'##molecule_type mRNA !'##residues 1-393 ##label OTS !'##cross-references EMBL:D14591; NID:g286228; PIDN:BAA03441.1; !1PID:g303803 COMPLEX monomer FUNCTION !$#description catalyzes the formation of specific !1peptidyl-threonine-phosphate and peptidyl-tyrosine-phosphate !1residues in mitogen-activated protein kinase using ATP !$#pathway growth factor-stimulated cascade in which Raf-1, MAPKK, and !1MAPK are sequentially activated CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS alternative splicing; ATP; phosphoprotein; !1phosphotransferase; serine/threonine/tyrosine-specific !1protein kinase FEATURE !$1-146,173-393 #product mitogen-activated protein kinase kinase 1, !8splice form B #status predicted #label F1B\ !$66-361 #domain protein kinase homology #label KIN\ !$74-82 #region protein kinase ATP-binding motif\ !$97,114,190,192 #active_site Lys, Glu, Asp, Lys #status predicted\ !$292,386 #binding_site phosphate (Thr) (covalent) (by MAP !8kinase) #status predicted SUMMARY #length 393 #molecular-weight 43465 #checksum 9820 SEQUENCE /// ENTRY I59571 #type complete TITLE mitogen-activated protein kinase kinase (EC 2.7.1.-) 1, splice form A - mouse ALTERNATE_NAMES ERK kinase 1; extracellular signal-regulated kinase activator kinase 1; MAP kinase kinase 1; MAPKK1; MEK1 CONTAINS mitogen-activated protein kinase kinase 1B ORGANISM #formal_name Mus musculus #common_name house mouse DATE 02-Aug-1996 #sequence_revision 02-Aug-1996 #text_change 11-Jun-1999 ACCESSIONS I59571; A46267; B46267; C46267; D46267; E46267 REFERENCE I59571 !$#authors Crews, C.M.; Alessandrini, A.A.; Erikson, R.L. !$#journal Science (1992) 258:478-480 !$#title The primary structure of MEK, a protein kinase that !1phosphorylates and activates the ERK gene product. !$#cross-references MUID:93030761; PMID:1411546 !$#accession I59571 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-393 ##label RES !'##cross-references GB:L02526; NID:g199123; PIDN:AAA39523.1; !1PID:g199124 REFERENCE A46267 !$#authors Crews, C.M.; Erikson, R.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:8205-8209 !$#title Purification of a murine protein-tyrosine/threonine kinase !1that phosphorylates and activates the Erk-1 gene product: !1relationship to the fission yeast byr1 gene product. !$#cross-references MUID:92390415; PMID:1381507 !$#accession A46267 !'##molecule_type protein !'##residues 4-20;71-84;114-136;206-227;228-234;363-373,'Q',375,'X', !1377-379,'X',381-384 ##label CRE !'##note sequence modified after extraction from NCBI backbone !'##note sequence extracted from NCBI backbone (NCBIP:112867) COMPLEX monomer FUNCTION !$#description catalyzes the formation of specific !1peptidyl-threonine-phosphate and peptidyl-tyrosine-phosphate !1residues in mitogen-activated protein kinase using ATP !$#pathway growth factor-stimulated cascade in which Raf-1, MAPKK, and !1MAPK are sequentially activated CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS alternative splicing; ATP; phosphoprotein; !1phosphotransferase; serine/threonine/tyrosine-specific !1protein kinase FEATURE !$1-146,173-393 #product mitogen-activated protein kinase kinase 1, !8splice form B #status predicted #label F1B\ !$66-361 #domain protein kinase homology #label KIN\ !$74-82 #region protein kinase ATP-binding motif\ !$97,114,190,192 #active_site Lys, Glu, Asp, Lys #status predicted\ !$292,386 #binding_site phosphate (Thr) (covalent) (by MAP !8kinase) #status predicted SUMMARY #length 393 #molecular-weight 43474 #checksum 9370 SEQUENCE /// ENTRY S46361 #type complete TITLE mitogen-activated protein kinase kinase (EC 2.7.1.-) 1, splice form A - Chinese hamster ALTERNATE_NAMES ERK kinase 1; extracellular signal-regulated kinase activator kinase 1; MAP kinase kinase 1; MAPKK1; MEK1 CONTAINS mitogen-activated protein kinase kinase 1B ORGANISM #formal_name Cricetulus griseus #common_name Chinese hamster DATE 19-Mar-1997 #sequence_revision 19-Mar-1997 #text_change 11-Jun-1999 ACCESSIONS S46361 REFERENCE S46361 !$#authors Pages, G.; Brunet, A.; L'Allemain, G.; Pouyssegur, J. !$#journal EMBO J. (1994) 13:3003-3010 !$#title Constitutive mutant and putative regulatory serine !1phosphorylation site of mammalian MAP kinase kinase (MEK1). !$#cross-references MUID:94313981; PMID:8039496 !$#accession S46361 !'##status preliminary !'##molecule_type mRNA !'##residues 1-393 ##label PAG !'##cross-references GB:S70933; NID:g547336; PIDN:AAB31379.1; !1PID:g547337 COMPLEX monomer FUNCTION !$#description catalyzes the formation of specific !1peptidyl-threonine-phosphate and peptidyl-tyrosine-phosphate !1residues in mitogen-activated protein kinase using ATP !$#pathway growth factor-stimulated cascade in which Raf-1, MAPKK, and !1MAPK are sequentially activated CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS alternative splicing; ATP; phosphoprotein; !1phosphotransferase; serine/threonine/tyrosine-specific !1protein kinase FEATURE !$1-146,173-393 #product mitogen-activated protein kinase kinase 1, !8splice form B #status predicted #label F1B\ !$66-361 #domain protein kinase homology #label KIN\ !$74-82 #region protein kinase ATP-binding motif\ !$97,114,190,192 #active_site Lys, Glu, Asp, Lys #status predicted\ !$292,386 #binding_site phosphate (Thr) (covalent) (by MAP !8kinase) #status experimental SUMMARY #length 393 #molecular-weight 43479 #checksum 67 SEQUENCE /// ENTRY S36186 #type complete TITLE mitogen-activated protein kinase kinase (EC 2.7.1.-) 1 - African clawed frog ALTERNATE_NAMES ERK kinase 1; extracellular signal-regulated kinase activator kinase 1; MAP kinase kinase 1; MAPKK1; MEK1 ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jun-2000 ACCESSIONS S36186; S37632; S23389 REFERENCE S36186 !$#authors Kosako, H.; Nishida, E.; Gotoh, Y. !$#journal EMBO J. (1993) 12:787-794 !$#title cDNA cloning of MAP kinase kinase reveals kinase cascade !1pathways in yeasts to vertebrates. !$#cross-references MUID:93178455; PMID:8440264 !$#accession S36186 !'##molecule_type mRNA !'##residues 1-395 ##label KOS !'##cross-references EMBL:D13700; NID:g222964; PIDN:BAA02860.1; !1PID:g222965 !$#accession S37632 !'##molecule_type protein !'##residues !12-20;37-47;49-57;71-84;169-177;186-214;282-287;317-324; !1327-341;356-363 ##label KO2 REFERENCE S23389 !$#authors Kosako, H.; Gotoh, Y.; Matsuda, S.; Ishikawa, M.; Nishida, !1E. !$#journal EMBO J. (1992) 11:2903-2908 !$#title Xenopus MAP kinase activator is a serine/threonine/tyrosine !1kinase activated by threonine phosphorylation. !$#cross-references MUID:92347324; PMID:1322292 !$#accession S23389 !'##molecule_type protein !'##residues 186-203,'X',205-206,'X',208-214 ##label KO3 COMPLEX monomer FUNCTION !$#description catalyzes the formation of specific !1peptidyl-threonine-phosphate and peptidyl-tyrosine-phosphate !1residues in mitogen-activated protein kinase using ATP !$#pathway growth factor-stimulated cascade in which Raf-1, MAPKK, and !1MAPK are sequentially activated CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphoprotein; phosphotransferase; serine/threonine/ !1tyrosine-specific protein kinase FEATURE !$2-395 #product mitogen-activated protein kinase kinase !8#status experimental #label MAT\ !$66-363 #domain protein kinase homology #label KIN\ !$74-82 #region protein kinase ATP-binding motif\ !$97,114,190,192 #active_site Lys, Glu, Asp, Lys #status predicted\ !$388 #binding_site phosphate (Thr) (covalent) (by MAP !8kinase) #status predicted SUMMARY #length 395 #molecular-weight 43742 #checksum 9370 SEQUENCE /// ENTRY A46723 #type complete TITLE MAP kinase kinase 2 (EC 2.7.1.-) - human ALTERNATE_NAMES extracellular signal-regulated kinase activator kinase 2 (ERK kinase 2); MEK2; mitogen-activated protein kinase kinase 2 (MAPKK2) CONTAINS protein kinase (EC 2.7.1.37); protein-tyrosine kinase (EC 2.7.1.112) ORGANISM #formal_name Homo sapiens #common_name man DATE 03-Mar-1994 #sequence_revision 18-Nov-1994 #text_change 04-Sep-1998 ACCESSIONS A46723 REFERENCE A46723 !$#authors Zheng, C.F.; Guan, K.L. !$#journal J. Biol. Chem. (1993) 268:11435-11439 !$#title Cloning and characterization of two distinct human !1extracellular signal-regulated kinase activator kinases, !1MEK1 and MEK2. !$#cross-references MUID:93266604; PMID:8388392 !$#accession A46723 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type mRNA !'##residues 1-400 ##label ZHE !'##cross-references GB:L11285; NID:g307184 !'##note sequence extracted from NCBI backbone (NCBIP:132853); this ORF !1is not annotated in GenBank entry HUMMEK2NF, release 106.0 COMMENT This enzyme is activated by protein kinase raf-1 (see !1PIR:A00637). It in turn is responsible for activating MAP !1kinase (see PIR:A48082 and PIR:JQ1400). See also PIR:A45100. GENETICS !$#gene GDB:PRKMK2; MEK2 !'##cross-references GDB:202924; OMIM:601263 COMPLEX monomer FUNCTION !$#description catalyzes the formation of specific !1peptidyl-threonine-phosphate and peptidyl-tyrosine-phosphate !1residues in MAP kinase using ATP !$#pathway MAP kinase cascade CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; monomer; phosphoprotein; phosphotransferase; serine/ !1threonine/tyrosine-specific protein kinase; signal !1transduction FEATURE !$70-369 #domain protein kinase homology #label KIN\ !$78-86 #region protein kinase ATP-binding motif\ !$101,118,194,196 #active_site Lys, Glu, Asp, Lys #status predicted\ !$222,226 #binding_site phosphate (Ser) (covalent) (by raf-1 !8kinase) #status predicted\ !$394 #binding_site phosphate (Thr) (covalent) (by raf-1 !8kinase) #status predicted SUMMARY #length 400 #molecular-weight 44424 #checksum 6048 SEQUENCE /// ENTRY A48081 #type complete TITLE mitogen-activated protein kinase kinase (EC 2.7.1.-) 2 - rat ALTERNATE_NAMES ERK kinase 2; extracellular signal-regulated kinase activator kinase 2; MAP kinase kinase 2; MAPKK2 protein; MEK2 protein ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 26-May-1994 #sequence_revision 26-May-1994 #text_change 16-Jun-2000 ACCESSIONS A48081; S38376; S38301; S32412 REFERENCE A48081 !$#authors Wu, J.; Harrison, J.K.; Dent, P.; Lynch, K.R.; Weber, M.J.; !1Sturgill, T.W. !$#journal Mol. Cell. Biol. (1993) 13:4539-4548 !$#title Identification and characterization of a new mammalian !1mitogen-activated protein kinase kinase, MKK2. !$#cross-references MUID:93330248; PMID:8393135 !$#accession A48081 !'##status preliminary !'##molecule_type mRNA !'##residues 1-400 ##label WUA !'##cross-references GB:L14936; NID:g349544; PIDN:AAA41620.1; !1PID:g349545 REFERENCE S38376 !$#authors Otsu, M. !$#submission submitted to the EMBL Data Library, March 1993 !$#description CORRIGENDUM: Isolation of two members of rat MAP kinase !1kinase gene family. !$#accession S38376 !'##molecule_type mRNA !'##residues 1-400 ##label OTS !'##cross-references EMBL:D14592; NID:g286229; PIDN:BAA03442.1; !1PID:g303804 REFERENCE S38301 !$#authors Otsu, M.; Terada, Y.; Okayama, H. !$#journal FEBS Lett. (1993) 331:307 !$#title Corrigendum. Isolation of two members of the rat MAP kinase !1kinase gene family. !$#cross-references MUID:93387489; PMID:8397117 !$#accession S38301 !'##molecule_type mRNA !'##residues 360-366 ##label OTW !'##cross-references EMBL:D14592 REFERENCE S32411 !$#authors Otsu, M.; Terada, Y.; Okayama, H. !$#journal FEBS Lett. (1993) 320:246-250 !$#title Isolation of two members of the rat MAP kinase kinase gene !1family. !$#cross-references MUID:93215844; PMID:8462694 !$#accession S32412 !'##status preliminary !'##molecule_type mRNA !'##residues 1-238,'I',240-359,'KC',362,'IK',365,'P',367-400 ##label OT2 GENETICS !$#gene MEK2 COMPLEX monomer FUNCTION !$#description catalyzes the formation of specific !1peptidyl-threonine-phosphate and peptidyl-tyrosine-phosphate !1residues in mitogen-activated protein kinase using ATP !$#pathway growth factor-stimulated cascade in which Raf-1, MAPKK, and !1MAPK are sequentially activated CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphoprotein; phosphotransferase; serine/threonine/ !1tyrosine-specific protein kinase FEATURE !$70-369 #domain protein kinase homology #label KIN\ !$78-86 #region protein kinase ATP-binding motif\ !$101,118,194,196 #active_site Lys, Glu, Asp, Lys #status predicted\ !$394 #binding_site phosphate (Thr) (covalent) (by MAP !8kinase) #status predicted SUMMARY #length 400 #molecular-weight 44281 #checksum 6322 SEQUENCE /// ENTRY I52829 #type complete TITLE mitogen-activated protein kinase kinase (EC 2.7.1.-) 2 - mouse ALTERNATE_NAMES ERK kinase 2; extracellular signal-regulated kinase activator kinase 2; MAP kinase kinase 2; MAPKK2; MEK2 ORGANISM #formal_name Mus sp. #common_name mouse DATE 02-Aug-1996 #sequence_revision 02-Aug-1996 #text_change 11-Jun-1999 ACCESSIONS I52829 REFERENCE I52829 !$#authors Brott, B.K.; Alessandrini, A.; Largaespada, D.A.; Copeland, !1N.G.; Jenkins, N.A.; Crews, C.M.; Erikson, R.L. !$#journal Cell Growth Differ. (1993) 4:921-929 !$#title MEK2 is a kinase related to MEK1 and is differentially !1expressed in murine tissues. !$#cross-references MUID:94128609; PMID:8297798 !$#accession I52829 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-401 ##label RES !'##cross-references GB:S68267; NID:g545202; PIDN:AAC60678.1; !1PID:g545203 GENETICS !$#gene mek2 COMPLEX monomer FUNCTION !$#description catalyzes the formation of specific !1peptidyl-threonine-phosphate and peptidyl-tyrosine-phosphate !1residues in mitogen-activated protein kinase using ATP !$#pathway growth factor-stimulated cascade in which Raf-1, MAPKK, and !1MAPK are sequentially activated CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphoprotein; phosphotransferase; serine/threonine/ !1tyrosine-specific protein kinase FEATURE !$70-370 #domain protein kinase homology #label KIN\ !$78-86 #region protein kinase ATP-binding motif\ !$101,118,194,196 #active_site Lys, Glu, Asp, Lys #status predicted\ !$395 #binding_site phosphate (Thr) (covalent) (by MAP !8kinase) #status predicted SUMMARY #length 401 #molecular-weight 44436 #checksum 7473 SEQUENCE /// ENTRY S41054 #type complete TITLE mitogen-activated protein kinase kinase (EC 2.7.1.-) 2 - common carp ALTERNATE_NAMES ERK kinase 2; extracellular signal-regulated kinase activator kinase 2; MAP kinase kinase 2; MAPKK2; MEK2 ORGANISM #formal_name Cyprinus carpio #common_name common carp DATE 13-Jan-1995 #sequence_revision 13-Jan-1995 #text_change 11-Jun-1999 ACCESSIONS S41054 REFERENCE S41054 !$#authors Huang, C.J.; Lee, M.S.; Chang, G.D.; Huang, F.L.; Lo, T.B. !$#journal Biochim. Biophys. Acta (1994) 1220:223-225 !$#title Molecular cloning and sequencing of a carp cDNA encoding !1mitogen-activated protein kinase kinase. !$#cross-references MUID:94146120; PMID:8312367 !$#accession S41054 !'##status preliminary !'##molecule_type mRNA !'##residues 1-397 ##label HUA !'##cross-references EMBL:L23935; NID:g397677; PIDN:AAA19788.1; !1PID:g397678 COMPLEX monomer FUNCTION !$#description catalyzes the formation of specific !1peptidyl-threonine-phosphate and peptidyl-tyrosine-phosphate !1residues in mitogen-activated protein kinase using ATP !$#pathway growth factor-stimulated cascade in which Raf-1, MAPKK, and !1MAPK are sequentially activated CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphoprotein; phosphotransferase; serine/threonine/ !1tyrosine-specific protein kinase FEATURE !$67-366 #domain protein kinase homology #label KIN\ !$75-83 #region protein kinase ATP-binding motif\ !$98,115,191,193 #active_site Lys, Glu, Asp, Lys #status predicted\ !$391 #binding_site phosphate (Thr) (covalent) (by MAP !8kinase) #status predicted SUMMARY #length 397 #molecular-weight 44147 #checksum 5303 SEQUENCE /// ENTRY A56466 #type complete TITLE mitogen-activated protein kinase kinase (EC 2.7.1.-) 2 - Caenorhabditis elegans ALTERNATE_NAMES ERK kinase 2; extracellular signal-regulated kinase activator kinase 2; MAP kinase kinase 2; MAPKK2; MEK2 ORGANISM #formal_name Caenorhabditis elegans DATE 09-Mar-1996 #sequence_revision 09-Mar-1996 #text_change 11-Jun-1999 ACCESSIONS A56466 REFERENCE A56466 !$#authors Wu, Y.; Han, M.; Guan, K.L. !$#journal Genes Dev. (1995) 9:742-755 !$#title MEK-2, a Caenorhabditis elegans MAP kinase kinase, functions !1in Ras-mediated vulval induction and other developmental !1events. !$#cross-references MUID:95247035; PMID:7729690 !$#accession A56466 !'##status preliminary !'##molecule_type mRNA !'##residues 1-387 ##label RES !'##cross-references EMBL:U21107; NID:g773352; PIDN:AAA85118.1; !1PID:g773353 GENETICS !$#gene MEK-2 COMPLEX monomer FUNCTION !$#description catalyzes the formation of specific !1peptidyl-threonine-phosphate and peptidyl-tyrosine-phosphate !1residues in mitogen-activated protein kinase using ATP !$#pathway growth factor-stimulated cascade in which Raf-1, MAPKK, and !1MAPK are sequentially activated CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphoprotein; phosphotransferase; serine/threonine/ !1tyrosine-specific protein kinase FEATURE !$71-360 #domain protein kinase homology #label KIN\ !$79-87 #region protein kinase ATP-binding motif\ !$102,119,195,197 #active_site Lys, Glu, Asp, Lys #status predicted SUMMARY #length 387 #molecular-weight 42794 #checksum 5642 SEQUENCE /// ENTRY OKBYR1 #type complete TITLE protein kinase byr1 (EC 2.7.1.-) - fission yeast (Schizosaccharomyces pombe) ORGANISM #formal_name Schizosaccharomyces pombe DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 10-Dec-1999 ACCESSIONS S00473; T38054 REFERENCE S00473 !$#authors Nadin-Davis, S.A.; Nasim, A. !$#journal EMBO J. (1988) 7:985-993 !$#title A gene which encodes a predicted protein kinase can restore !1some functions of the ras gene in fission yeast. !$#cross-references MUID:88296442; PMID:3042386 !$#accession S00473 !'##molecule_type DNA !'##residues 1-340 ##label NAD !'##cross-references EMBL:X07445; NID:g4918; PIDN:CAA30326.1; PID:g4919 REFERENCE Z21765 !$#authors Lye, G.; Churcher, C.M.; Barrell, B.G.; Rajandream, M.A.; !1Walsh, S.V. !$#submission submitted to the EMBL Data Library, February 1995 !$#accession T38054 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-340 ##label LYE !'##cross-references EMBL:Z69239; PIDN:CAA93222.1; GSPDB:GN00066; !1SPDB:SPAC1D4.13 !'##experimental_source strain 972h-; cosmid c1D4 COMMENT Inactivation of this gene does not interfere with mitotic !1growth but prevents conjugation and sporulation. GENETICS !$#gene byr1 !$#map_position 1 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; cell cycle control; phosphoprotein; phosphotransferase; !1serine/threonine-specific protein kinase; sporulation FEATURE !$64-320 #domain protein kinase homology #label KIN\ !$72-80 #region protein kinase ATP-binding motif\ !$93 #active_site Lys #status predicted SUMMARY #length 340 #molecular-weight 38189 #checksum 9801 SEQUENCE /// ENTRY KIHUCT #type complete TITLE phosphorylase kinase (EC 2.7.1.38) catalytic chain, testis - human ALTERNATE_NAMES gamma 2 phosphorylase kinase, testis ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 11-Jun-1999 ACCESSIONS A40069; A26368 REFERENCE A40069 !$#authors Hanks, S.K. !$#journal Mol. Endocrinol. (1989) 3:110-116 !$#title Messenger ribonucleic acid encoding an apparent isoform of !1phosphorylase kinase catalytic subunit is abundant in the !1adult testis. !$#cross-references MUID:89127266; PMID:2915644 !$#accession A40069 !'##molecule_type mRNA !'##residues 1-406 ##label HAN !'##cross-references GB:M31606; NID:g189940; PIDN:AAA36442.1; !1PID:g189941 !'##experimental_source HeLa cDNA library, clone PSK-C3 !'##note corrects and extends sequence A26368 REFERENCE A94156 !$#authors Hanks, S.K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:388-392 !$#title Homology probing: identification of cDNA clones encoding !1members of the protein-serine kinase family. !$#cross-references MUID:87092414; PMID:2948189 !$#accession A26368 !'##molecule_type mRNA !'##residues 129-145,'P',147-175,'S',177-178,'D',180-211,'LVD',215-220, !1'E',222-273 ##label HA2 !'##cross-references GB:M14503; NID:g190657; PIDN:AAA36518.1; !1PID:g190658 !'##experimental_source HeLa cDNA library, clone PSK-C3 COMMENT The mRNA for this isoform was present in testis but absent !1from skeletal muscle, liver, and ovary. GENETICS !$#gene GDB:PHKG2 !'##cross-references GDB:140316; OMIM:172471 !$#map_position 16p11.2-16p11.2 FUNCTION !$#description catalyzes the ATP-dependent phosphorylation of phosphorylase !1b CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphotransferase; serine/threonine-specific protein !1kinase; testis FEATURE !$2-406 #product phosphorylase kinase catalytic chain #status !8predicted #label MAT\ !$22-291 #domain protein kinase homology #label KIN\ !$30-38 #region protein kinase ATP-binding motif\ !$53 #active_site Lys #status predicted SUMMARY #length 406 #molecular-weight 46442 #checksum 214 SEQUENCE /// ENTRY A42034 #type complete TITLE phosphorylase kinase (EC 2.7.1.38) catalytic chain, gamma T - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 05-May-2000 ACCESSIONS A42034 REFERENCE A42034 !$#authors Calalb, M.B.; Fox, D.T.; Hanks, S.K. !$#journal J. Biol. Chem. (1992) 267:1455-1463 !$#title Molecular cloning and enzymatic analysis of the rat homolog !1of "PhK-gamma T," an isoform of phosphorylase kinase !1catalytic subunit. !$#cross-references MUID:92112855; PMID:1370475 !$#accession A42034 !'##molecule_type DNA !'##residues 1-406 ##label CAL !'##cross-references GB:M73808; NID:g206163; PIDN:AAA41863.1; !1PID:g206164 !'##note sequence extracted from NCBI backbone (NCBIN:75819, !1NCBIP:75820) CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; multimer; phosphotransferase; serine/threonine-specific !1protein kinase FEATURE !$22-291 #domain protein kinase homology #label KIN\ !$30-38 #region protein kinase ATP-binding motif\ !$53 #active_site Lys #status predicted SUMMARY #length 406 #molecular-weight 46677 #checksum 9978 SEQUENCE /// ENTRY KIRBFG #type complete TITLE phosphorylase kinase (EC 2.7.1.38) catalytic chain, skeletal muscle - rabbit ALTERNATE_NAMES phosphorylase kinase gamma chain ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 17-May-1985 #sequence_revision 30-Jun-1991 #text_change 11-Jun-1999 ACCESSIONS S00075; A00624 REFERENCE S00075 !$#authors da Cruz e Silva, E.F.; Cohen, P.T.W. !$#journal FEBS Lett. (1987) 220:36-42 !$#title Isolation and sequence analysis of a cDNA clone encoding the !1entire catalytic subunit of phosphorylase kinase. !$#cross-references MUID:87276568; PMID:3609320 !$#accession S00075 !'##molecule_type mRNA !'##residues 1-387 ##label DAC !'##cross-references EMBL:Y00684; NID:g1659; PIDN:CAA68682.1; PID:g1660 REFERENCE A00624 !$#authors Reimann, E.M.; Titani, K.; Ericsson, L.H.; Wade, R.D.; !1Fischer, E.H.; Walsh, K.A. !$#journal Biochemistry (1984) 23:4185-4192 !$#title Homology of the gamma subunit of phosphorylase b kinase with !1cAMP-dependent protein kinase. !$#cross-references MUID:85023304; PMID:6541504 !$#accession A00624 !'##molecule_type protein !'##residues 2-387 ##label REI COMMENT This protein is a polymer of 16 chains, four each of alpha, !1beta, gamma, and delta. Alpha and beta are regulatory !1chains, gamma is the catalytic chain, and delta is !1calmodulin. CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; multimer; phosphotransferase; serine/threonine-specific !1protein kinase FEATURE !$2-387 #product phosphorylase kinase catalytic chain #status !8experimental #label MAT\ !$18-288 #domain protein kinase homology #label KIN\ !$26-34 #region protein kinase ATP-binding motif\ !$49 #active_site Lys #status predicted SUMMARY #length 387 #molecular-weight 44802 #checksum 6355 SEQUENCE /// ENTRY A29872 #type complete TITLE phosphorylase kinase (EC 2.7.1.38) catalytic chain, skeletal muscle - mouse ALTERNATE_NAMES phosphorylase kinase (EC 2.7.1.38) gamma chain ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-May-2000 ACCESSIONS A29872; A29315; A46124 REFERENCE A29872 !$#authors Chamberlain, J.S.; VanTuinen, P.; Reeves, A.A.; Philip, !1B.A.; Caskey, C.T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:2886-2890 !$#title Isolation of cDNA clones for the catalytic gamma-subunit of !1mouse muscle phosphorylase kinase: expression of mRNA in !1normal and mutant Phk mice. !$#cross-references MUID:87204232; PMID:3472241 !$#accession A29872 !'##molecule_type mRNA !'##residues 1-388 ##label CHA !'##cross-references GB:M16216; NID:g200340; PIDN:AAA39926.1; !1PID:g200341 !'##experimental_source strain C57BL/10, muscle REFERENCE A29315 !$#authors Bender, P.K.; Emerson Jr., C.P. !$#journal J. Biol. Chem. (1987) 262:8799-8805 !$#title Skeletal muscle phosphorylase kinase catalytic subunit mRNAs !1are expressed in heart tissue but not in liver. !$#cross-references MUID:87250504; PMID:3597394 !$#accession A29315 !'##molecule_type mRNA !'##residues 1-312,'L',314-388 ##label BEN !'##cross-references GB:J03293; GB:J02731; NID:g200338; PIDN:AAA39925.1; !1PID:g200339 !'##experimental_source strain ICR Swiss White, muscle REFERENCE A46124 !$#authors Maichele, A.J.; Farwell, N.J.; Chamberlain, J.S. !$#journal Genomics (1993) 16:139-149 !$#title A B2 repeat insertion generates alternate structures of the !1mouse muscle gamma-phosphorylase kinase gene. !$#cross-references MUID:93252370; PMID:8486349 !$#accession A46124 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-312,'L',314-388 ##label RES !'##cross-references GB:S60494; NID:g300120 !'##experimental_source strain Balb/C, muscle !'##note this translation is not annotated in GenBank entry S60491S4, !1release 114 GENETICS !$#introns 28/2; 88/1; 106/2; 128/2; 183/1; 213/2; 264/3; 306/3 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS alternative splicing; ATP; muscle; phosphotransferase; !1serine/threonine-specific protein kinase; skeletal muscle FEATURE !$18-288 #domain protein kinase homology #label KIN\ !$26-34 #region protein kinase ATP-binding motif\ !$49 #active_site Lys #status predicted SUMMARY #length 388 #molecular-weight 44945 #checksum 8067 SEQUENCE /// ENTRY S00731 #type complete TITLE phosphorylase kinase (EC 2.7.1.38) catalytic chain [similarity] - rat ALTERNATE_NAMES phosphorylase kinase (EC 2.7.1.38) gamma chain ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 05-May-2000 ACCESSIONS S00731; A45044 REFERENCE S00731 !$#authors Cawley, K.C.; Ramachandran, C.; Gorin, F.A.; Walsh, D.A. !$#journal Nucleic Acids Res. (1988) 16:2355-2356 !$#title Nucleotide sequence of cDNA encoding the catalytic subunit !1of phosphorylase kinase from rat soleus muscle. !$#cross-references MUID:88189845; PMID:3357797 !$#accession S00731 !'##molecule_type mRNA !'##residues 1-388 ##label CAW !'##cross-references EMBL:X07320; NID:g56926; PIDN:CAA30280.1; !1PID:g56927 REFERENCE A45044 !$#authors Cawley, K.C.; Akita, C.G.; Angelos, K.L.; Walsh, D.A. !$#journal J. Biol. Chem. (1993) 268:1194-1200 !$#title Characterization of the gene for rat phosphorylase kinase !1catalytic subunit. !$#cross-references MUID:93123233; PMID:8419323 !$#accession A45044 !'##molecule_type DNA !'##residues 2-388 ##label CA2 !'##cross-references GB:M98826 !'##experimental_source Wistar !'##note this sequence is inconsistent with the nucleotide translation !'##note sequence extracted from NCBI backbone (NCBIP:121962) CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphotransferase; serine/threonine-specific protein !1kinase FEATURE !$18-288 #domain protein kinase homology #label KIN\ !$26-34 #region protein kinase ATP-binding motif\ !$49 #active_site Lys #status predicted SUMMARY #length 388 #molecular-weight 45014 #checksum 8269 SEQUENCE /// ENTRY TVBY2A #type complete TITLE casein kinase II (EC 2.7.1.-) alpha' chain - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein O2810; protein YOR061w ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jun-2000 ACCESSIONS S11192; C26688; S66944; A35651 REFERENCE A35651 !$#authors Padmanabha, R.; Chen-Wu, J.L.P.; Hanna, D.E.; Glover, C.V.C. !$#journal Mol. Cell. Biol. (1990) 10:4089-4099 !$#title Isolation, sequencing, and disruption of the yeast CKA2 !1gene: casein kinase II is essential for viability in !1Saccharomyces cerevisiae. !$#cross-references MUID:90318373; PMID:2196445 !$#accession S11192 !'##molecule_type DNA !'##residues 1-339 ##label PAD !'##cross-references EMBL:M33759; NID:g171232; PIDN:AAA34500.1; !1PID:g171233 !'##note the authors translated the codon TTT for residue 295 as Leu and !1ATA for residue 296 as Leu REFERENCE A92624 !$#authors Padmanabha, R.; Glover, C.V.C. !$#journal J. Biol. Chem. (1987) 262:1829-1835 !$#title Casein kinase II of yeast contains two distinct !1alpha-polypeptides and an unusually large beta-subunit. !$#cross-references MUID:87109340; PMID:3468112 !$#accession C26688 !'##molecule_type protein !'##residues 2-25,'XX',28-31,'X',33,'X',35-36,'X',38 ##label PAW REFERENCE S66929 !$#authors Bohn, C.; Bolotin-Fukuhara, M.; Daignan-Fornier, B.; Dang, !1D.V.; Valens, M. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S66944 !'##molecule_type DNA !'##residues 1-339 ##label BOH !'##cross-references EMBL:Z74969; NID:g1420202; PIDN:CAA99254.1; !1PID:g1420203; GSPDB:GN00015; MIPS:YOR061w !'##experimental_source strain S288C GENETICS !$#gene SGD:CKA2; MIPS:YOR061w !'##cross-references SGD:S0005587; MIPS:YOR061w !$#map_position 15R CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; heterotetramer; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$2-339 #product casein kinase II alpha' chain #status !8experimental #label MAT\ !$48-309 #domain protein kinase homology #label KIN\ !$56-64 #region protein kinase ATP-binding motif\ !$79 #active_site Lys #status predicted SUMMARY #length 339 #molecular-weight 39403 #checksum 9472 SEQUENCE /// ENTRY S53324 #type complete TITLE glycogen synthase kinase 3 beta (EC 2.7.1.-) - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S53324 REFERENCE S53324 !$#authors Stambolic, V.; Woodgett, J.R. !$#journal Biochem. J. (1994) 303:701-704 !$#title Mitogen inactivation of glycogen synthase kinase-3-beta in !1intact cells via serine 9 phosphorylation. !$#cross-references MUID:95071278; PMID:7980435 !$#accession S53324 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type mRNA !'##residues 1-420 ##label STA !'##cross-references EMBL:L33801; NID:g529236; PIDN:AAA66475.1; !1PID:g529237 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 COMMENT This enzyme is inhibited by phosphorylation of serine 9 by !1p70 S6 kinase (see PIR:A41687) or p90 S6 kinase RSK1 (see !1PIR:I51901). GENETICS !$#gene GDB:GSK3B !'##cross-references GDB:6108057 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphoprotein; phosphotransferase FEATURE !$54-315 #domain protein kinase homology #label KIN\ !$62-70 #region protein kinase ATP-binding motif\ !$9 #binding_site phosphate (Ser) (covalent) (by !8ribosomal protein S6 kinase) #status experimental\ !$85 #active_site Lys #status predicted SUMMARY #length 420 #molecular-weight 46768 #checksum 8031 SEQUENCE /// ENTRY TVRTKA #type complete TITLE protein kinase (EC 2.7.1.37) GSK-3-alpha - rat ALTERNATE_NAMES factor A; glycogen synthase kinase 3 alpha ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 11-Jun-1999 ACCESSIONS S14707 REFERENCE S14707 !$#authors Woodgett, J.R. !$#journal EMBO J. (1990) 9:2431-2438 !$#title Molecular cloning and expression of glycogen synthase !1kinase-3/Factor A. !$#cross-references MUID:90316097; PMID:2164470 !$#accession S14707 !'##molecule_type mRNA !'##residues 1-483 ##label WOO !'##cross-references EMBL:X53427; NID:g56331; PIDN:CAA37518.1; !1PID:g56332 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$117-378 #domain protein kinase homology #label KIN\ !$125-133 #region protein kinase ATP-binding motif\ !$148 #active_site Lys #status predicted SUMMARY #length 483 #molecular-weight 51026 #checksum 3491 SEQUENCE /// ENTRY TVRTKB #type complete TITLE tau-protein kinase (EC 2.7.1.135) I - rat ALTERNATE_NAMES factor A; glycogen synthase kinase 3 beta; protein kinase GSK-3-beta; tau-protein kinase I ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 11-Jun-1999 ACCESSIONS S14708; S33741; S36729 REFERENCE S14707 !$#authors Woodgett, J.R. !$#journal EMBO J. (1990) 9:2431-2438 !$#title Molecular cloning and expression of glycogen synthase !1kinase-3/Factor A. !$#cross-references MUID:90316097; PMID:2164470 !$#accession S14708 !'##molecule_type mRNA !'##residues 1-420 ##label WOO !'##cross-references EMBL:X53428; NID:g56333; PIDN:CAA37519.1; !1PID:g56334 !'##note the author translated the codon ATG for residue 240 as Val REFERENCE S33741 !$#authors Ishiguro, K.; Shiratsuchi, A.; Sato, S.; Omori, A.; Arioka, !1M.; Kobayashi, S.; Uchida, T.; Imahori, K. !$#journal FEBS Lett. (1993) 325:167-172 !$#title Glycogen synthase kinase 3-beta is identical to tau protein !1kinase I generating several epitopes of paired helical !1filaments. !$#cross-references MUID:93307488; PMID:7686508 !$#accession S33741 !'##molecule_type mRNA !'##residues 1-239,'V',241-420 ##label ISH !'##cross-references EMBL:X73653; NID:g402651; PIDN:CAA52020.1; !1PID:g402652 !$#accession S36729 !'##molecule_type protein !'##residues 37-58;61-74;151-158;293-316;318-325;327-332;351-368;370-375 !1##label ISH2 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$54-315 #domain protein kinase homology #label KIN\ !$62-70 #region protein kinase ATP-binding motif\ !$85 #active_site Lys #status predicted SUMMARY #length 420 #molecular-weight 46742 #checksum 6775 SEQUENCE /// ENTRY S37643 #type complete TITLE protein kinase MSK-2 (EC 2.7.1.-) [similarity] - alfalfa ORGANISM #formal_name Medicago sativa #common_name alfalfa DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 05-May-2000 ACCESSIONS S37643 REFERENCE S37642 !$#authors Pay, A.; Jonak, C.; Boegre, L.; Meskiene, I.; Mairinger, T.; !1Szalay, A.; Heberle-Bors, E.; Hirt, H. !$#journal Plant J. (1993) 3:847-856 !$#title The MsK family of alfalfa protein kinase genes encodes !1homologues of shaggy/glycogen synthase kinase-3 and shows !1differential expression patterns in plant organs and !1development. !$#cross-references MUID:94004996; PMID:8401615 !$#accession S37643 !'##molecule_type mRNA !'##residues 1-411 ##label PAY !'##cross-references EMBL:X68410; NID:g313145; PIDN:CAA48473.1; !1PID:g313146 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphotransferase FEATURE !$72-333 #domain protein kinase homology #label KIN\ !$80-88 #region protein kinase ATP-binding motif\ !$103 #active_site Lys #status predicted SUMMARY #length 411 #molecular-weight 46062 #checksum 744 SEQUENCE /// ENTRY S37642 #type complete TITLE protein kinase MSK-3 (EC 2.7.1.-) [similarity] - alfalfa ORGANISM #formal_name Medicago sativa #common_name alfalfa DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 05-May-2000 ACCESSIONS S37642 REFERENCE S37642 !$#authors Pay, A.; Jonak, C.; Boegre, L.; Meskiene, I.; Mairinger, T.; !1Szalay, A.; Heberle-Bors, E.; Hirt, H. !$#journal Plant J. (1993) 3:847-856 !$#title The MsK family of alfalfa protein kinase genes encodes !1homologues of shaggy/glycogen synthase kinase-3 and shows !1differential expression patterns in plant organs and !1development. !$#cross-references MUID:94004996; PMID:8401615 !$#accession S37642 !'##molecule_type mRNA !'##residues 1-412 ##label PAY !'##cross-references EMBL:X68409; NID:g313147; PIDN:CAA48472.1; !1PID:g313148 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphotransferase FEATURE !$73-334 #domain protein kinase homology #label KIN\ !$81-89 #region protein kinase ATP-binding motif\ !$104 #active_site Lys #status predicted SUMMARY #length 412 #molecular-weight 46403 #checksum 1503 SEQUENCE /// ENTRY S37644 #type complete TITLE protein kinase MSK-1 (EC 2.7.1.-) [similarity] - alfalfa ORGANISM #formal_name Medicago sativa #common_name alfalfa DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 05-May-2000 ACCESSIONS S37644 REFERENCE S37642 !$#authors Pay, A.; Jonak, C.; Boegre, L.; Meskiene, I.; Mairinger, T.; !1Szalay, A.; Heberle-Bors, E.; Hirt, H. !$#journal Plant J. (1993) 3:847-856 !$#title The MsK family of alfalfa protein kinase genes encodes !1homologues of shaggy/glycogen synthase kinase-3 and shows !1differential expression patterns in plant organs and !1development. !$#cross-references MUID:94004996; PMID:8401615 !$#accession S37644 !'##molecule_type mRNA !'##residues 1-411 ##label PAY !'##cross-references EMBL:X68411; NID:g313143; PIDN:CAA48474.1; !1PID:g313144 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphotransferase FEATURE !$73-334 #domain protein kinase homology #label KIN\ !$81-89 #region protein kinase ATP-binding motif\ !$104 #active_site Lys #status predicted SUMMARY #length 411 #molecular-weight 46774 #checksum 1097 SEQUENCE /// ENTRY S41597 #type complete TITLE protein kinase ASK-gamma (EC 2.7.1.-) [similarity] - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 05-May-2000 ACCESSIONS S41597 REFERENCE S41596 !$#authors Bianchi, M.W.; Guivarc'h, D.; Thomas, M.; Woodgett, J.R.; !1Kreis, M. !$#journal Mol. Gen. Genet. (1994) 242:337-345 !$#title Arabidopsis homologs of the shaggy and GSK-3 protein !1kinases: molecular cloning and functional expression in !1Escherichia coli. !$#cross-references MUID:94150468; PMID:7509023 !$#accession S41597 !'##molecule_type mRNA !'##residues 1-409 ##label BIA !'##cross-references EMBL:X75431; NID:g456508; PIDN:CAA53180.1; !1PID:g456509 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphotransferase FEATURE !$71-332 #domain protein kinase homology #label KIN\ !$79-87 #region protein kinase ATP-binding motif\ !$102 #active_site Lys #status predicted SUMMARY #length 409 #molecular-weight 46587 #checksum 9828 SEQUENCE /// ENTRY S41596 #type complete TITLE protein kinase ASK-alpha (EC 2.7.1.-) [similarity] - Arabidopsis thaliana ALTERNATE_NAMES shaggy-related protein kinase ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 16-Jun-2000 ACCESSIONS S41596; S26627 REFERENCE S41596 !$#authors Bianchi, M.W.; Guivarc'h, D.; Thomas, M.; Woodgett, J.R.; !1Kreis, M. !$#journal Mol. Gen. Genet. (1994) 242:337-345 !$#title Arabidopsis homologs of the shaggy and GSK-3 protein !1kinases: molecular cloning and functional expression in !1Escherichia coli. !$#cross-references MUID:94150468; PMID:7509023 !$#accession S41596 !'##molecule_type mRNA !'##residues 1-405 ##label BIA1 !'##cross-references EMBL:X75432; NID:g460831; PIDN:CAA53181.1; !1PID:g460832 REFERENCE S26627 !$#authors Bianchi, M.; Guivarc'h, D.; Kreis, M. !$#submission submitted to the EMBL Data Library, September 1992 !$#description Arabidopsis genes encoding homologs of the shaggy/GSK-3 !1protein kinase. !$#accession S26627 !'##molecule_type DNA !'##residues 1-405 ##label BIA2 !'##cross-references EMBL:X68525; NID:g1769888; PIDN:CAA48538.1; !1PID:g1769889 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphotransferase FEATURE !$67-328 #domain protein kinase homology #label KIN\ !$75-83 #region protein kinase ATP-binding motif\ !$98 #active_site Lys #status predicted SUMMARY #length 405 #molecular-weight 46024 #checksum 8604 SEQUENCE /// ENTRY T02254 #type complete TITLE shaggy protein kinase (EC 2.7.1.-) 111 [similarity] - common tobacco ORGANISM #formal_name Nicotiana tabacum #common_name common tobacco DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 21-Jul-2000 ACCESSIONS T02254 REFERENCE Z14641 !$#authors Tichtinsky, G.; Tavares, R.; Takvorian, A.; Schwebel-Dugue, !1N.; Twell, D.; Kreis, M. !$#journal Biochim. Biophys. Acta (1998) 1442:261-273 !$#title An evolutionary conserved group of plant GSK-3/shaggy like !1protein kinase genes preferentially expressed in developing !1pollen. !$#cross-references MUID:99023747; PMID:9804971 !$#accession T02254 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-469 ##label TIC !'##cross-references EMBL:AJ002314; NID:g2598600; PIDN:CAA05328.1; !1PID:g2598601 !'##experimental_source cultivar Samsun NN; cell-type pollen GENETICS !$#gene NSK 111 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphotransferase; protein kinase FEATURE !$138-399 #domain protein kinase homology #label KIN SUMMARY #length 469 #molecular-weight 53584 #checksum 7368 SEQUENCE /// ENTRY T02256 #type complete TITLE shaggy protein kinase (EC 2.7.1.-) 59 [similarity] - common tobacco ORGANISM #formal_name Nicotiana tabacum #common_name common tobacco DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 21-Jul-2000 ACCESSIONS T02256 REFERENCE Z14641 !$#authors Tichtinsky, G.; Tavares, R.; Takvorian, A.; Schwebel-Dugue, !1N.; Twell, D.; Kreis, M. !$#journal Biochim. Biophys. Acta (1998) 1442:261-273 !$#title An evolutionary conserved group of plant GSK-3/shaggy like !1protein kinase genes preferentially expressed in developing !1pollen. !$#cross-references MUID:99023747; PMID:9804971 !$#accession T02256 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-469 ##label TIC !'##cross-references EMBL:AJ002315; NID:g2598602; PIDN:CAA05329.1; !1PID:g2598603 !'##experimental_source cultivar Samsun NN; cell-type pollen GENETICS !$#gene NSK 59 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphotransferase; protein kinase FEATURE !$138-399 #domain protein kinase homology #label KIN SUMMARY #length 469 #molecular-weight 53363 #checksum 7643 SEQUENCE /// ENTRY T02297 #type complete TITLE shaggy protein kinase (EC 2.7.1.-) 91 [similarity] - common tobacco ORGANISM #formal_name Nicotiana tabacum #common_name common tobacco DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 21-Jul-2000 ACCESSIONS T02297 REFERENCE Z14641 !$#authors Tichtinsky, G.; Tavares, R.; Takvorian, A.; Schwebel-Dugue, !1N.; Twell, D.; Kreis, M. !$#journal Biochim. Biophys. Acta (1998) 1442:261-273 !$#title An evolutionary conserved group of plant GSK-3/shaggy like !1protein kinase genes preferentially expressed in developing !1pollen. !$#cross-references MUID:99023747; PMID:9804971 !$#accession T02297 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-471 ##label TIC !'##cross-references EMBL:AJ224163; NID:g3236114; PIDN:CAA11860.1; !1PID:g3236115 !'##experimental_source cultivar Samsun NN; tissue-type pollen GENETICS !$#gene NSK 91 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphotransferase; protein kinase FEATURE !$140-401 #domain protein kinase homology #label KIN SUMMARY #length 471 #molecular-weight 53499 #checksum 9507 SEQUENCE /// ENTRY T01236 #type complete TITLE serine/threonine-specific protein kinase (EC 2.7.1.-) F6N23.11 [similarity] - Arabidopsis thaliana ALTERNATE_NAMES protein F6N23.11; shaggy-related protein kinase tetha ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 05-May-2000 ACCESSIONS T01236 REFERENCE Z14281 !$#authors Geisel, C. !$#submission submitted to the EMBL Data Library, April 1998 !$#description The sequence of A. thaliana F6N23. !$#accession T01236 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-472 ##label GEI !'##cross-references EMBL:AF058919; NID:g3047100; PIDN:AAC13616.1; !1PID:g30105; GSPDB:GN00063; ATSP:F6N23.11 GENETICS !$#gene ATSP:F6N23.11 !$#map_position 5 !$#introns 21/3; 103/3; 134/3; 154/3; 245/3; 270/3; 289/3; 336/3; 353/ !13; 385/3; 413/3; 448/1 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphotransferase; protein kinase FEATURE !$136-397 #domain protein kinase homology #label KIN\ !$144-152 #region protein kinase ATP-binding motif\ !$167 #active_site Lys #status predicted SUMMARY #length 472 #molecular-weight 53161 #checksum 8858 SEQUENCE /// ENTRY T48250 #type complete TITLE serine/threonine-specific protein kinase NAK (EC 2.7.1.-) - Arabidopsis thaliana ALTERNATE_NAMES novel Arabidopsis protein kinase; protein T1E22.50 ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 05-May-2000 ACCESSIONS T48250; S38326 REFERENCE Z24489 !$#authors Bevan, M.; Hilbert, H.; Braun, M.; Holzer, E.; Brandt, A.; !1Duesterhoeft, A.; Bancroft, I.; Mewes, H.W.; Rudd, S.; !1Lemcke, K.; Mayer, K.F.X. !$#submission submitted to the Protein Sequence Database, March 2000 !$#accession T48250 !'##molecule_type DNA !'##residues 1-389 ##label BEV !'##cross-references EMBL:AL162874; PIDN:CAB85534.1 !'##experimental_source cultivar Columbia; BAC clone T1E22 REFERENCE S38326 !$#authors Moran, T.V.; Walker, J.C. !$#journal Biochim. Biophys. Acta (1993) 1216:9-14 !$#title Molecular cloning of two novel protein kinase genes from !1Arabidopsis thaliana. !$#cross-references MUID:94032493; PMID:8218420 !$#accession S38326 !'##molecule_type mRNA !'##residues 1-286,'V',288-389 ##label MOR !'##cross-references EMBL:L07248; NID:g166808; PIDN:AAA18853.1; !1PID:g166809 GENETICS !$#map_position 5 !$#introns 18/1; 120/3; 166/1; 213/3; 255/1 !$#note T1E22.50 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphotransferase; serine/threonine-specific protein !1kinase FEATURE !$66-357 #domain protein kinase homology #label KIN\ !$74-82 #region protein kinase ATP-binding motif SUMMARY #length 389 #molecular-weight 43533 #checksum 4738 SEQUENCE /// ENTRY S28615 #type complete TITLE serine/threonine/tyrosine-specific protein kinase APK1 (EC 2.7.1.-) [validated] - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 16-Jun-2000 ACCESSIONS S28615 REFERENCE S28615 !$#authors Hirayama, T.; Oka, A. !$#journal Plant Mol. Biol. (1992) 20:653-662 !$#title Novel protein kinase of Arabidopsis thaliana (APK1) that !1phosphorylates tyrosine, serine and threonine. !$#cross-references MUID:93081726; PMID:1450380 !$#accession S28615 !'##molecule_type mRNA !'##residues 1-410 ##label HIR !'##cross-references EMBL:D12522; NID:g217828; PIDN:BAA02092.1; !1PID:g217829 !'##experimental_source Columbia ecotype !'##note tyrosine phosphorylation occured only on limited substrates GENETICS !$#gene APK1 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphotransferase; serine/threonine/tyrosine-specific !1protein kinase FEATURE !$66-357 #domain protein kinase homology #label KIN\ !$74-82 #region protein kinase ATP-binding motif SUMMARY #length 410 #molecular-weight 45519 #checksum 2890 SEQUENCE /// ENTRY S24913 #type complete TITLE protein kinase (EC 2.7.1.37) cdc2 [similarity] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 05-May-2000 ACCESSIONS S24913 REFERENCE S20658 !$#authors Kanaoka, Y.; Nojima, H.; Okayama, H. !$#submission submitted to the EMBL Data Library, July 1991 !$#description Nucleotide sequences of cDNAs encoding rat cdc2 + and cyclin !12. !$#accession S24913 !'##molecule_type mRNA !'##residues 1-297 ##label KAN !'##cross-references EMBL:X60767; NID:g57533; PIDN:CAA43177.1; !1PID:g57534 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$2-256 #domain protein kinase homology #label KIN\ !$10-18 #region protein kinase ATP-binding motif\ !$33,51,128,130 #active_site Lys, Glu, Asp, Lys #status predicted SUMMARY #length 297 #molecular-weight 34134 #checksum 9329 SEQUENCE /// ENTRY A36074 #type complete TITLE protein kinase (EC 2.7.1.37) cdc2 [validated] - mouse ALTERNATE_NAMES cell division control protein cdc2; CTD kinase; p34 protein kinase ORGANISM #formal_name Mus musculus #common_name house mouse DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 05-May-2000 ACCESSIONS A36074; S05049; I48288 REFERENCE A36074 !$#authors Th'ng, J.P.H.; Wright, P.S.; Hamaguchi, J.; Lee, M.G.; !1Norbury, C.J.; Nurse, P.; Bradbury, E.M. !$#journal Cell (1990) 63:313-324 !$#title The FT210 cell line is a mouse G2 phase mutant with a !1temperature-sensitive CDC2 gene product. !$#cross-references MUID:91004239; PMID:2208288 !$#accession A36074 !'##molecule_type mRNA !'##residues 1-297 ##label THA !'##cross-references GB:M38724 REFERENCE S05049 !$#authors Cisek, L.J.; Corden, J.L. !$#journal Nature (1989) 339:679-684 !$#title Phosphorylation of RNA polymerase by the murine homologue of !1the cell-cycle control protein cdc2. !$#cross-references MUID:89295557; PMID:2662013 !$#accession S05049 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-103,'T',105-112,'M',114-211,'Q',213-244,'N',246-259,'C', !1261-262,'F',264-297 ##label CIS !'##note part of this sequence was confirmed by protein sequencing REFERENCE I48288 !$#authors Spurr, N.K.; Gough, A.C.; Lee, M.G. !$#journal DNA Seq. (1990) 1:49-54 !$#title Cloning of the mouse homologue of the yeast cell cycle !1control gene cdc2. !$#cross-references MUID:92119319; PMID:2132958 !$#accession I48288 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-164,'L',166-211,'Q',213-272,'T',274-297 ##label RES !'##cross-references EMBL:X16461; NID:g50359; PIDN:CAA34481.1; !1PID:g50360 COMMENT The carboxyl-terminal domain of the large chain of !1DNA-dependent RNA polymerase II is the major substrate for !1the CTD protein kinase, which does not appear to be !1identical to the M-phase specific kinase. GENETICS !$#gene CDC2 COMPLEX In various organisms, cdc2 has been identified as a !1component of the M-phase specific histone H1 kinase !1(maturation-promoting factor, growth-associated H1 kinase) !1and CTD kinase. CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; cell cycle control; phosphoprotein; phosphotransferase; !1serine/threonine-specific protein kinase FEATURE !$2-256 #domain protein kinase homology #label KIN\ !$10-18 #region protein kinase ATP-binding motif\ !$33,51,128,130 #active_site Lys, Glu, Asp, Lys #status predicted SUMMARY #length 297 #molecular-weight 34092 #checksum 8355 SEQUENCE /// ENTRY S06011 #type complete TITLE protein kinase (EC 2.7.1.37) cdc2 - chicken ALTERNATE_NAMES cell division control protein cdc2 ORGANISM #formal_name Gallus gallus #common_name chicken DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S06011 REFERENCE S06011 !$#authors Krek, W.; Nigg, E.A. !$#journal EMBO J. (1989) 8:3071-3078 !$#title Structure and developmental expression of the chicken CDC2 !1kinase. !$#cross-references MUID:90059893; PMID:2684635 !$#accession S06011 !'##molecule_type mRNA !'##residues 1-303 ##label KRE !'##cross-references EMBL:X16881; NID:g63172; PIDN:CAA34764.1; !1PID:g63173 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$2-256 #domain protein kinase homology #label KIN\ !$10-18 #region protein kinase ATP-binding motif\ !$33,51,128,130 #active_site Lys, Glu, Asp, Lys #status predicted SUMMARY #length 303 #molecular-weight 34688 #checksum 7342 SEQUENCE /// ENTRY A44349 #type complete TITLE protein kinase (EC 2.7.1.37) cdc2-A [similarity] - African clawed frog ALTERNATE_NAMES maturation-promoting factor p34cdc2 chain A ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 05-May-2000 ACCESSIONS A44349 REFERENCE A44349 !$#authors Pickham, K.M.; Meyer, A.N.; Li, J.; Donoghue, D.J. !$#journal Mol. Cell. Biol. (1992) 12:3192-3203 !$#title Requirement of mos(Xe) protein kinase for meiotic maturation !1of Xenopus oocytes induced by a cdc2 mutant lacking !1regulatory phosphorylation sites. !$#cross-references MUID:92318937; PMID:1377775 !$#accession A44349 !'##molecule_type mRNA !'##residues 1-302 ##label PIC !'##cross-references GB:M60680; NID:g214022; PIDN:AAA63561.1; !1PID:g214023 !'##experimental_source oocytes !'##note sequence extracted from NCBI backbone (NCBIN:107682, !1NCBIP:107683) CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$2-256 #domain protein kinase homology #label KIN\ !$10-18 #region protein kinase ATP-binding motif\ !$33,51,128,130 #active_site Lys, Glu, Asp, Lys #status predicted SUMMARY #length 302 #molecular-weight 34506 #checksum 3971 SEQUENCE /// ENTRY I50474 #type complete TITLE protein kinase (EC 2.7.1.37) cdc2 [similarity] - goldfish ORGANISM #formal_name Carassius auratus #common_name goldfish DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 05-May-2000 ACCESSIONS I50474 REFERENCE I50474 !$#authors Kajiura, H.; Yamashita, M.; Katsu, Y.; Nagahama, Y. !$#journal Dev. Growth Differ. (1993) 35:647-654 !$#title Isolation and characterization of goldfish cdc2, a catalytic !1component of maturation-promoting factor. !$#accession I50474 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-302 ##label KAJ !'##cross-references GB:D17758; NID:g471097; PIDN:BAA04605.1; !1PID:g471098 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphotransferase FEATURE !$2-256 #domain protein kinase homology #label KIN\ !$10-18 #region protein kinase ATP-binding motif\ !$33,51,128,130 #active_site Lys, Glu, Asp, Lys #status predicted SUMMARY #length 302 #molecular-weight 34499 #checksum 7972 SEQUENCE /// ENTRY S12009 #type complete TITLE protein kinase cdc2 (EC 2.7.1.-) [similarity] - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 05-May-2000 ACCESSIONS S12009; S12006 REFERENCE S12008 !$#authors Jimenez, J.; Alphey, L.; Nurse, P.; Glover, D.M. !$#journal EMBO J. (1990) 9:3565-3571 !$#title Complementation of fission yeast cdc2(ts) and cdc25(ts) !1mutants identifies two cell cycle genes from Drosophila: a !1cdc2 homologue and string. !$#cross-references MUID:91006056; PMID:2120044 !$#accession S12009 !'##status preliminary !'##molecule_type mRNA !'##residues 1-297 ##label JIM !'##cross-references GB:X57496; NID:g7704; PIDN:CAA40733.1; PID:g7705 REFERENCE S12006 !$#authors Lehner, C.F.; O'Farrell, P.H. !$#journal EMBO J. (1990) 9:3573-3581 !$#title Drosophila cdc2 homologs: a functional homolog is !1coexpressed with a cognate variant. !$#cross-references MUID:91006057; PMID:2120045 !$#accession S12006 !'##status preliminary !'##molecule_type mRNA !'##residues 1-297 ##label LEH !'##cross-references EMBL:X57485; NID:g7710; PIDN:CAA40723.1; PID:g7711 !'##experimental_source strain Oregon R GENETICS !$#gene FlyBase:cdc2 !'##cross-references FlyBase:FBgn0004106 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$2-256 #domain protein kinase homology #label KIN\ !$10-18 #region protein kinase ATP-binding motif\ !$33,51,128,130 #active_site Lys, Glu, Asp, Lys #status predicted SUMMARY #length 297 #molecular-weight 34439 #checksum 8371 SEQUENCE /// ENTRY S41003 #type complete TITLE protein kinase (EC 2.7.1.37) cdc2 homolog - Caenorhabditis elegans ALTERNATE_NAMES hypothetical protein T05G5.3; p34; protein kinase NCC-1 ORGANISM #formal_name Caenorhabditis elegans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S41003; S26572; S52565 REFERENCE S41001 !$#authors Thomas, K. !$#submission submitted to the EMBL Data Library, October 1993 !$#accession S41003 !'##molecule_type DNA !'##residues 1-332 ##label THO !'##cross-references EMBL:Z27079; NID:g414641; PID:g414644 REFERENCE S26572 !$#authors Ferraz, C.; Thierry-Mieg, D.; le Peuch, C.J. !$#submission submitted to the EMBL Data Library, September 1992 !$#description Complete nucleotide sequence of a cDNA coding for a !1p34-cdc2-like protein from Caenorhabiditis elegans. !$#accession S26572 !'##molecule_type mRNA !'##residues 1-332 ##label FER !'##cross-references EMBL:X68384; NID:g6659; PIDN:CAA48455.1; PID:g6660 REFERENCE S52565 !$#authors Mori, H.; Palmer, R.E.; Sternberg, P.W. !$#journal Mol. Gen. Genet. (1994) 245:781-786 !$#title The identification of a Caenorhabditis elegans homolog of !1p34(cdc2) kinase. !$#cross-references MUID:95131956; PMID:7830726 !$#accession S52565 !'##status preliminary !'##molecule_type mRNA !'##residues 1-175,'P',177-332 ##label MOR !'##cross-references GB:S75262; NID:g807196; PIDN:AAC60520.1; !1PID:g807197 !'##note the sequence from Fig. 2 is inconsistent with that from Fig. 1 !1in having 135-Leu GENETICS !$#introns 60/3; 129/3; 181/3; 290/3 COMPLEX In various organisms, cdc2 has been identified as a !1component of the M-phase specific histone H1 kinase !1(maturation-promoting factor, growth-associated H1 kinase) !1and CTD kinase. CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; cell cycle control; phosphoprotein; phosphotransferase; !1serine/threonine-specific protein kinase FEATURE !$20-274 #domain protein kinase homology #label KIN\ !$28-36 #region protein kinase ATP-binding motif\ !$51,69,146,148 #active_site Lys, Glu, Asp, Lys #status predicted SUMMARY #length 332 #molecular-weight 38295 #checksum 9588 SEQUENCE /// ENTRY A44878 #type complete TITLE protein kinase (EC 2.7.1.37) cdk2 [validated] - goldfish ORGANISM #formal_name Carassius auratus #common_name goldfish DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 05-May-2000 ACCESSIONS A44878 REFERENCE A44878 !$#authors Hirai, T.; Yamashita, M.; Yoshikuni, M.; Tokumoto, T.; !1Kajiura, H.; Sakai, N.; Nagahama, Y. !$#journal Dev. Biol. (1992) 152:113-120 !$#title Isolation and characterization of goldfish cdk2, a cognate !1variant of the cell cycle regulator cdc2. !$#cross-references MUID:92331802; PMID:1339336 !$#accession A44878 !'##status preliminary !'##molecule_type mRNA !'##residues 1-298 ##label HIR !'##cross-references GB:S40289; NID:g251619; PIDN:AAB22550.1; !1PID:g251620 !'##experimental_source oocyte !'##note sequence extracted from NCBI backbone (NCBIN:108782, !1NCBIP:108783) GENETICS !$#gene cdk2 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; cell cycle control; mitosis; phosphoprotein; !1phosphotransferase; serine/threonine-specific protein kinase FEATURE !$2-255 #domain protein kinase homology #label KIN\ !$10-18 #region protein kinase ATP-binding motif\ !$33,51,127,129 #active_site Lys, Glu, Asp, Lys #status predicted SUMMARY #length 298 #molecular-weight 33998 #checksum 692 SEQUENCE /// ENTRY I78840 #type complete TITLE protein kinase (EC 2.7.1.37) cdk2, beta splice form - rat ALTERNATE_NAMES cyclin dependent kinase 2 (cdk2) CONTAINS protein kinase cdk2, alpha splice form ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 06-Oct-2000 ACCESSIONS I78840; I58348 REFERENCE I58348 !$#authors Kotani, S.; Endo, T.; Kitagawa, M.; Higashi, H.; Onaya, T. !$#journal Oncogene (1995) 10:663-669 !$#title A variant form of cyclin-dependent kinase 2 (Cdk2) in a !1malignantly transformed rat thyroid (FRTL-Tc) cell line. !$#cross-references MUID:95166553; PMID:7862443 !$#accession I78840 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-346 ##label RES !'##cross-references GB:D28754; NID:g710026; PIDN:BAA05948.1; !1PID:g710027 !$#accession I58348 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-196,245-346 ##label RE2 !'##cross-references GB:D28753; NID:g710024; PIDN:BAA05947.1; !1PID:g710025 !'##note in Genbank entry RATCDK2B, release 113.0, the source is !1designated as Rattus rattus, cell line FRTL-5 (strain !1Fischer) COMPLEX In various organisms, cdc2 has been identified as a !1component of the M-phase specific histone H1 kinase !1(maturation-promoting factor, growth-associated H1 kinase) !1and CTD kinase. CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS alternative splicing; ATP; cell cycle control; !1phosphotransferase; serine/threonine-specific protein kinase FEATURE !$1-346 #product protein kinase cdk2, beta splice form !8#status predicted #label MATB\ !$1-196,245-346 #product protein kinase cdk2, alpha splice form !8#status predicted #label MATA\ !$2-303 #domain protein kinase homology #status atypical !8#label KIN\ !$10-18 #region protein kinase ATP-binding motif\ !$33,51,127,129 #active_site Lys, Glu, Asp, Lys #status predicted SUMMARY #length 346 #molecular-weight 39034 #checksum 174 SEQUENCE /// ENTRY I48157 #type complete TITLE protein kinase (EC 2.7.1.37) cdk2L - golden hamster CONTAINS protein kinase cdk2 ORGANISM #formal_name Mesocricetus auratus #common_name golden hamster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS I48157; I48156 REFERENCE I48156 !$#authors Noguchi, E.; Sekiguchi, T.; Yamashita, K.; Nishimoto, T. !$#journal Biochem. Biophys. Res. Commun. (1993) 197:1524-1529 !$#title Molecular cloning and identification of two types of hamster !1cyclin-dependent kinases: cdk2 and cdk2L. !$#cross-references MUID:94107363; PMID:8280171 !$#accession I48157 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-346 ##label RES !'##cross-references GB:D17351; NID:g464160; PIDN:BAA04166.1; !1PID:g666952 !$#accession I48156 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-196,245-346 ##label RE2 !'##cross-references GB:D17350; NID:g464159; PIDN:BAA04165.1; !1PID:g666951 COMPLEX In various organisms, cdc2 has been identified as a !1component of the M-phase specific histone H1 kinase !1(maturation-promoting factor, growth-associated H1 kinase) !1and CTD kinase. CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; cell cycle control; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$1-196,245-346 #product protein kinase cdc2 #status predicted #label !8MAT2\ !$2-303 #domain protein kinase homology #status atypical !8#label KIN\ !$10-18 #region protein kinase ATP-binding motif\ !$33,51,127,129 #active_site Lys, Glu, Asp, Lys #status predicted SUMMARY #length 346 #molecular-weight 38986 #checksum 588 SEQUENCE /// ENTRY S12007 #type complete TITLE protein kinase (EC 2.7.1.37) cdc2 homolog C - fruit fly (Drosophila sp.) ORGANISM #formal_name Drosophila sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S12007 REFERENCE S12006 !$#authors Lehner, C.F.; O'Farrell, P.H. !$#journal EMBO J. (1990) 9:3573-3581 !$#title Drosophila cdc2 homologs: a functional homolog is !1coexpressed with a cognate variant. !$#cross-references MUID:91006057; PMID:2120045 !$#accession S12007 !'##status preliminary !'##molecule_type mRNA !'##residues 1-314 ##label LEH !'##cross-references EMBL:X57486; NID:g7708; PIDN:CAA40724.1; PID:g7709 GENETICS !$#gene FlyBase:cdc2c !'##cross-references FlyBase:FBgn0004107 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$6-258 #domain protein kinase homology #label KIN\ !$14-22 #region protein kinase ATP-binding motif\ !$37,55,130,132 #active_site Lys, Glu, Asp, Lys #status predicted SUMMARY #length 314 #molecular-weight 35888 #checksum 5274 SEQUENCE /// ENTRY JQ2243 #type complete TITLE protein kinase (EC 2.7.1.37) cdc2 homolog - moth bean ORGANISM #formal_name Vigna aconitifolia #common_name moth bean DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JQ2243 REFERENCE JQ2243 !$#authors Hong, Z.; Miao, G.H.; Verma, D.P.S. !$#journal Plant Physiol. (1993) 101:1399-1400 !$#title p34cdc2 Protein kinase homolog from mothbean (Vigna !1aconitifolia). !$#cross-references MUID:94143490; PMID:8310070 !$#accession JQ2243 !'##molecule_type mRNA !'##residues 1-294 ##label HON !'##cross-references GB:M99497; NID:g170641; PIDN:AAA34241.1; !1PID:g170642 !'##experimental_source root nodule CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; cell cycle control; phosphotransferase FEATURE !$2-256 #domain protein kinase homology #label KIN\ !$10-18 #region protein kinase ATP-binding motif\ !$42-57 #region PSTAIR motif\ !$33,51,127,129 #active_site Lys, Glu, Asp, Lys #status predicted SUMMARY #length 294 #molecular-weight 33983 #checksum 3162 SEQUENCE /// ENTRY S57928 #type complete TITLE protein kinase (EC 2.7.1.37) cdc2 homolog - cowpea ORGANISM #formal_name Vigna unguiculata #common_name cowpea DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S57928 REFERENCE S57928 !$#authors Krause, A.; El Kovaissi, R.; Broughton, W.J. !$#submission submitted to the EMBL Data Library, July 1995 !$#accession S57928 !'##status preliminary !'##molecule_type mRNA !'##residues 1-294 ##label KRA !'##cross-references EMBL:X89400; NID:g908911; PIDN:CAA61581.1; !1PID:g1235610 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphotransferase FEATURE !$2-256 #domain protein kinase homology #label KIN\ !$10-18 #region protein kinase ATP-binding motif\ !$33,51,127,129 #active_site Lys, Glu, Asp, Lys #status predicted SUMMARY #length 294 #molecular-weight 34023 #checksum 3588 SEQUENCE /// ENTRY S42049 #type complete TITLE protein kinase (EC 2.7.1.37) cdc2 - Norway spruce ORGANISM #formal_name Picea abies #common_name Norway spruce DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S42049; S52987; S52986 REFERENCE S42049 !$#authors Kvarnheden, A.; Tandre, K.; Engstrm, P. !$#submission submitted to the EMBL Data Library, January 1994 !$#description A cdc2 homologue and closely related processed !1retropseudogenes from Norway spruce. !$#accession S42049 !'##molecule_type mRNA !'##residues 1-294 ##label KVA !'##cross-references EMBL:X77680; NID:g454979; PIDN:CAA54746.1; !1PID:g454980 REFERENCE S52986 !$#authors Kvarnheden, A.; Tandre, K.; Engstroem, P. !$#journal Plant Mol. Biol. (1995) 27:391-403 !$#title A cdc2 homologue and closely related processed !1retropseudogenes from Norway spruce. !$#cross-references MUID:95195165; PMID:7888627 !$#accession S52987 !'##status preliminary !'##molecule_type DNA !'##residues 132-236 ##label KV2 !'##cross-references EMBL:X77681; NID:g467786; PIDN:CAA54747.1; !1PID:g758205 !$#accession S52986 !'##status preliminary !'##molecule_type mRNA !'##residues 1-294 ##label KV3 !'##cross-references EMBL:X77680; NID:g454979; PIDN:CAA54746.1; !1PID:g454980 GENETICS !$#gene cdc2 !$#introns 163/3; 218/2 !$#note the list of introns may be incomplete CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; cell cycle control; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$2-256 #domain protein kinase homology #label KIN\ !$10-18 #region protein kinase ATP-binding motif\ !$33,51,127,129 #active_site Lys, Glu, Asp, Lys #status predicted SUMMARY #length 294 #molecular-weight 33704 #checksum 1091 SEQUENCE /// ENTRY S31332 #type complete TITLE protein kinase (EC 2.7.1.37) cdc2-B - alfalfa ORGANISM #formal_name Medicago sativa #common_name alfalfa DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S31332 REFERENCE S31332 !$#authors Hirt, H.; Pay, A.; Begre, L.; Meskiene, I.; Heberle-Bors, E. !$#submission submitted to the EMBL Data Library, January 1993 !$#description CDC2B, a cognate CDC2 gene from Alfalfa, complements the G1/ !1S but not the G2/M transition of budding yeast CDC28 !1mutants. !$#accession S31332 !'##status preliminary !'##molecule_type mRNA !'##residues 1-294 ##label HIR !'##cross-references EMBL:X70707; NID:g19582; PIDN:CAA50038.1; !1PID:g19583 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$2-256 #domain protein kinase homology #label KIN\ !$10-18 #region protein kinase ATP-binding motif\ !$33,51,127,129 #active_site Lys, Glu, Asp, Lys #status predicted SUMMARY #length 294 #molecular-weight 33886 #checksum 810 SEQUENCE /// ENTRY A40444 #type complete TITLE protein kinase (EC 2.7.1.37) cdc2 homolog A - maize ORGANISM #formal_name Zea mays #common_name maize DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A40444 REFERENCE A40444 !$#authors Colasanti, J.; Tyers, M.; Sundaresan, V. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:3377-3381 !$#title Isolation and characterization of cDNA clones encoding a !1functional p34(cdc2) homologue from Zea mays. !$#cross-references MUID:91195354; PMID:2014258 !$#accession A40444 !'##status preliminary !'##molecule_type mRNA !'##residues 1-294 ##label COL !'##cross-references GB:M60526 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphotransferase FEATURE !$2-256 #domain protein kinase homology #label KIN\ !$10-18 #region protein kinase ATP-binding motif\ !$33,51,127,129 #active_site Lys, Glu, Asp, Lys #status predicted SUMMARY #length 294 #molecular-weight 33834 #checksum 2393 SEQUENCE /// ENTRY TVBY8 #type complete TITLE protein kinase (EC 2.7.1.37) cdc28 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES cell division control protein CDC28; protein YBR1211; protein YBR160w ORGANISM #formal_name Saccharomyces cerevisiae DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 21-Jul-2000 ACCESSIONS A00657; S46031; S47309; S55841; A25085 REFERENCE A00657 !$#authors Lorincz, A.T.; Reed, S.I. !$#journal Nature (1984) 307:183-185 !$#title Primary structure homology between the product of yeast cell !1division control gene CDC28 and vertebrate oncogenes. !$#cross-references MUID:84093623; PMID:6361575 !$#accession A00657 !'##molecule_type DNA !'##residues 1-298 ##label LOR !'##cross-references EMBL:X00257; NID:g3485; PIDN:CAA25065.1; PID:g3486 REFERENCE S46013 !$#authors Entian, K.D.; Koetter, P.; Rose, M.; Becker, J.; Grey, M.; !1Li, Z.; Niegemann, E.; Schenk-Groeninger, R.; Servos, J.; !1Wehner, E.; Wolter, R.; Brendel, M.; Bauer, J.; Braun, H.; !1Dern, K.; Duesterhus, S.; Gruenbein, R.; Hedges, D.; Kiesau, !1P.; Korol, S.; Krems, B.; Proft, M.; Siegers, K.; Baur, A.; !1Boles, E.; Miosga, T.; Schaaff-Gerstenschlaeger, I.; !1Zimmermann, F.K. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S46031 !'##molecule_type DNA !'##residues 1-298 ##label ENT !'##cross-references EMBL:Z36029; NID:g536493; PIDN:CAA85119.1; !1PID:g536494; GSPDB:GN00002; MIPS:YBR160w REFERENCE S47309 !$#authors Baur, S.; Becker, J.; Li, Z.; Niegemann, E.; Wehner, E.; !1Wolter, R.; Brendel, M. !$#submission submitted to the EMBL Data Library, September 1994 !$#description Sequence analysis of a 5.6 kb fragment of chromosome II from !1Saccharomyces cerevisiae reveals two new open reading frames !1next to CDC28. !$#accession S47309 !'##molecule_type DNA !'##residues 1-298 ##label BAU !'##cross-references EMBL:X80224; NID:g535468; PIDN:CAA56509.1; !1PID:g535469 REFERENCE S55841 !$#authors Baur, S.; Becker, J.; Li, Z.; Niegemann, E.; Wehner, E.; !1Wolter, R.; Brendel, M. !$#journal Yeast (1995) 11:455-458 !$#title Sequence analysis of a 5.6 kb fragment of chromosome II from !1Saccharomyces cerevisiae reveals two new open reading frames !1next to CDC28. !$#cross-references MUID:95321017; PMID:7597849 !$#accession S55841 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-298 ##label BAW !'##cross-references EMBL:X80224; NID:g535468; PIDN:CAA56509.1; !1PID:g535469 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1September 1994 GENETICS !$#gene SGD:CDC28; MIPS:YBR160w !'##cross-references SGD:S0000364; MIPS:YBR160w !$#map_position 2R CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; cell cycle control; phosphoprotein; phosphotransferase; !1serine/threonine-specific protein kinase FEATURE !$6-264 #domain protein kinase homology #label KIN\ !$14-22 #region protein kinase ATP-binding motif\ !$40,58,136,138 #active_site Lys, Glu, Asp, Lys #status predicted SUMMARY #length 298 #molecular-weight 34061 #checksum 3359 SEQUENCE /// ENTRY JC4827 #type complete TITLE protein kinase (EC 2.7.1.37) cdc28 - yeast (Candida albicans) ALTERNATE_NAMES cyclin-dependent kinase CDK1 ORGANISM #formal_name Candida albicans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JC4827; S51611; S47030 REFERENCE JC4827 !$#authors Damagnez, V.; Cottarel, G. !$#journal Gene (1996) 172:137-141 !$#title Candida albicans CDK1 and CYB1: cDNA homologues of the cdc2/ !1CDC28 and cdc13/CLB1/CLB2 cell cycle control genes. !$#cross-references MUID:96257268; PMID:8654974 !$#accession JC4827 !'##molecule_type mRNA !'##residues 1-317 ##label DAM !'##cross-references GB:U40405; NID:g1103925; PIDN:AAC49450.1; !1PID:g1103926 REFERENCE S51611 !$#authors Sherlock, G.; Bahman, A.M.; Mahal, A.; Shieh, J.C.; !1Ferreira, M.; Rosamond, J. !$#journal Mol. Gen. Genet. (1994) 245:716-723 !$#title Molecular cloning and analysis of CDC28 and cyclin !1homologues from the human fungal pathogen Candida albicans. !$#cross-references MUID:95131949; PMID:7830719 !$#accession S51611 !'##molecule_type DNA !'##residues 1-317 ##label SHE !'##cross-references EMBL:X80034; NID:g520627; PIDN:CAA56338.1; !1PID:g520628 GENETICS !$#gene cdk1 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; cell cycle control; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$5-262 #domain protein kinase homology #label KIN\ !$13-21 #region protein kinase ATP-binding motif\ !$37,55,133,135 #active_site Lys, Glu, Asp, Lys #status predicted SUMMARY #length 317 #molecular-weight 36647 #checksum 7651 SEQUENCE /// ENTRY S36437 #type complete TITLE protein kinase (EC 2.7.1.37) cdc2 homolog - Ajellomyces capsulata ORGANISM #formal_name Ajellomyces capsulata, Histoplasma capsulatum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S36437 REFERENCE S36437 !$#authors di Lallo, G.; Gargano, S.; Maresca, B. !$#submission submitted to the EMBL Data Library, July 1993 !$#description Histoplasma capsulatum cdc2 gene is transcriptionally !1regulated during the morphologic transition. !$#accession S36437 !'##status preliminary !'##molecule_type DNA !'##residues 1-324 ##label DIL !'##cross-references EMBL:X74361; NID:g396692; PIDN:CAA52405.1; !1PID:g396693 GENETICS !$#introns 13/1; 183/3; 238/2 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphotransferase FEATURE !$2-276 #domain protein kinase homology #label KIN\ !$10-18 #region protein kinase ATP-binding motif\ !$34,52,148,150 #active_site Lys, Glu, Asp, Lys #status predicted SUMMARY #length 324 #molecular-weight 36823 #checksum 5126 SEQUENCE /// ENTRY TVZP2 #type complete TITLE protein kinase (EC 2.7.1.37) cdc2 - fission yeast (Schizosaccharomyces pombe) ORGANISM #formal_name Schizosaccharomyces pombe DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 11-Jun-1999 ACCESSIONS A23359; A05227 REFERENCE A05227 !$#authors Hindley, J.; Phear, G.A. !$#journal Gene (1984) 31:129-134 !$#title Sequence of the cell division gene CDC2 from !1Schizosaccharomyces pombe; patterns of splicing and homology !1to protein kinases. !$#cross-references MUID:85128427; PMID:6526270 !$#accession A23359 !'##molecule_type DNA !'##residues 1-297 ##label HIN !'##cross-references GB:M12912; NID:g173358; PIDN:AAA35293.1; !1PID:g173359 COMMENT This is one of the regulatory proteins that are involved in !1the control of cell division; it functions at the early !1stage of the G1 phase and also in the G2 phase of the cell !1cycle. GENETICS !$#gene cdc2 !$#introns 13/1; 69/2; 169/3; 271/3 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; cell cycle control; mitosis; phosphoprotein; !1phosphotransferase; serine/threonine-specific protein kinase FEATURE !$2-262 #domain protein kinase homology #label KIN\ !$10-18 #region protein kinase ATP-binding motif\ !$33,51,134,136 #active_site Lys, Glu, Asp, Lys #status predicted SUMMARY #length 297 #molecular-weight 34358 #checksum 3278 SEQUENCE /// ENTRY S42566 #type complete TITLE protein kinase (EC 2.7.1.37) cdc2 homolog - malaria parasite (Plasmodium falciparum) ORGANISM #formal_name Plasmodium falciparum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS S42566; S22008 REFERENCE S42566 !$#authors Ross-MacDonald, P.B.; Graeser, R.; Kappes, B.; Franklin, R.; !1Williamson, D.H. !$#journal Eur. J. Biochem. (1994) 220:693-701 !$#title Isolation and expression of a gene specifying a cdc2-like !1protein kinase from the human malaria parasite Plasmodium !1falciparum. !$#cross-references MUID:94192659; PMID:8143724 !$#accession S42566 !'##status preliminary !'##molecule_type DNA !'##residues 1-288 ##label ROS !'##cross-references EMBL:X61921; NID:g9933; PIDN:CAA43923.1; PID:g9934 GENETICS !$#introns 47/1; 95/1; 148/2; 249/3 COMPLEX In various organisms, cdc2 has been identified as a !1component of the M-phase specific histone H1 kinase !1(maturation-promoting factor, growth-associated H1 kinase) !1and CTD kinase. CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; cell cycle control; phosphoprotein; phosphotransferase; !1serine/threonine-specific protein kinase FEATURE !$2-253 #domain protein kinase homology #label KIN\ !$10-18 #region protein kinase ATP-binding motif\ !$32,50,125,127 #active_site Lys, Glu, Asp, Lys #status predicted SUMMARY #length 288 #molecular-weight 32996 #checksum 9262 SEQUENCE /// ENTRY A46365 #type complete TITLE protein kinase (EC 2.7.1.37) cdc2-related nclk [similarity] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 16-Jun-2000 #sequence_revision 16-Jun-2000 #text_change 16-Jun-2000 ACCESSIONS A46365 REFERENCE A46365 !$#authors Hellmich, M.R.; Pant, H.C.; Wada, E.; Battey, J.F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:10867-10871 !$#title Neuronal cdc2-like kinase: a cdc2-related protein kinase !1with predominantly neuronal expression. !$#cross-references MUID:93066344; PMID:1279696 !$#accession A46365 !'##molecule_type mRNA !'##residues 1-292 ##label HEL !'##cross-references GB:L02121; NID:g203389; PIDN:AAA40902.1; !1PID:g203390 !'##experimental_source brain !'##note sequence extracted from NCBI backbone (NCBIN:118707, !1NCBIP:118708) CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$2-255 #domain protein kinase homology #label KIN\ !$10-18 #region protein kinase ATP-binding motif\ !$33,51,126,128 #active_site Lys, Glu, Asp, Lys #status predicted SUMMARY #length 292 #molecular-weight 33254 #checksum 9911 SEQUENCE /// ENTRY I49592 #type complete TITLE protein kinase (EC 2.7.1.37) crk6 [similarity] - mouse ALTERNATE_NAMES CDK5; cyclin-dependent kinase 5 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 16-Jun-2000 #sequence_revision 16-Jun-2000 #text_change 16-Jun-2000 ACCESSIONS I49592; PN0487 REFERENCE I49592 !$#authors Ino, H.; Ishizuka, T.; Chiba, T.; Tatibana, M. !$#journal Brain Res. (1994) 661:196-206 !$#title Expression of CDK5 (PSSALRE kinase), a neural cdc2-related !1protein kinase, in the mature and developing mouse central !1and peripheral nervous systems. !$#cross-references MUID:95135945; PMID:7834371 !$#accession I49592 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-292 ##label RES !'##cross-references GB:D29678; NID:g577635; PIDN:BAA06148.1; !1PID:g577636 REFERENCE PN0479 !$#authors Ershler, M.A.; Nagorskaya, T.V.; Visser, J.W.M.; Belyavsky, !1A.V. !$#journal Gene (1993) 124:305-306 !$#title Novel CDC2-related protein kinases produced in murine !1hematopoietic stem cells. !$#cross-references MUID:93185941; PMID:8444355 !$#accession PN0487 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 124-168,'A',170,'E' ##label ERS !'##cross-references EMBL:X64604; NID:g50558 !'##experimental_source strain CBA; bone marrow GENETICS !$#gene MGI:Cdk5 !'##cross-references MGI:101765 !$#map_position 5:12.0 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; cell cycle control; phosphotransferase FEATURE !$2-255 #domain protein kinase homology #label KIN\ !$10-18 #region protein kinase ATP-binding motif\ !$33,51,126,128 #active_site Lys, Glu, Asp, Lys #status predicted SUMMARY #length 292 #molecular-weight 33288 #checksum 9617 SEQUENCE /// ENTRY A45091 #type complete TITLE protein kinase (EC 2.7.1.37) cdc2-related nclk - bovine ALTERNATE_NAMES cdc2-related protein kinase PSSALRE homolog; tau protein kinase II large chain ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A45091; S39453; S39454 REFERENCE A45091 !$#authors Lew, J.; Winkfein, R.J.; Paudel, H.K.; Wang, J.H. !$#journal J. Biol. Chem. (1992) 267:25922-25926 !$#title Brain proline-directed protein kinase is a neurofilament !1kinase which displays high sequence homology to p34cdc2. !$#cross-references MUID:93100310; PMID:1464604 !$#accession A45091 !'##molecule_type mRNA !'##residues 1-292 ##label LEW !'##cross-references GB:L04798 !'##experimental_source brain !'##note sequence extracted from NCBI backbone (NCBIN:120848, !1NCBIP:120849) REFERENCE S39453 !$#authors Kobayashi, S.; Ishiguro, K.; Omori, A.; Takamatsu, M.; !1Arioka, M.; Imahori, K.; Uchida, T. !$#journal FEBS Lett. (1993) 335:171-175 !$#title A cdc2-related kinase PSSALRE/cdk5 is homologous with the 30 !1kDa subunit of tau protein kinase II, a proline-directed !1protein kinase associated with microtubule. !$#cross-references MUID:94074679; PMID:8253190 !$#accession S39453 !'##molecule_type mRNA !'##residues 1-292 ##label KOB !'##cross-references GB:X82440; NID:g572618; PIDN:CAA57821.1; !1PID:g572619 !$#accession S39454 !'##molecule_type protein !'##residues 9-40;232-247;280-287 ##label KO2 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphotransferase FEATURE !$2-255 #domain protein kinase homology #label KIN\ !$10-18 #region protein kinase ATP-binding motif\ !$33,51,126,128 #active_site Lys, Glu, Asp, Lys #status predicted SUMMARY #length 292 #molecular-weight 33288 #checksum 9617 SEQUENCE /// ENTRY S53538 #type complete TITLE protein kinase (EC 2.7.1.37) cdc2 homolog - Paramecium tetraurelia ORGANISM #formal_name Paramecium tetraurelia DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 07-Dec-1999 ACCESSIONS S53538 REFERENCE S53538 !$#authors Tang, L.; Pelech, S.L.; Berger, J.D. !$#journal Biochim. Biophys. Acta (1995) 1265:161-167 !$#title Isolation of the cell cycle control gene cdc2 from !1Paramecium tetraurelia. !$#cross-references MUID:95210349; PMID:7696344 !$#accession S53538 !'##status preliminary !'##molecule_type DNA !'##residues 1-308 ##label TAN !'##note the sequence from Fig. 3 is inconsistent with that from Fig. 1 !1in having 70-Arg, and 271-Ile GENETICS !$#genetic_code SGC5 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphotransferase FEATURE !$7-262 #domain protein kinase homology #label KIN\ !$15-23 #region protein kinase ATP-binding motif\ !$38,56,133,135 #active_site Lys, Glu, Asp, Lys #status predicted SUMMARY #length 308 #molecular-weight 35362 #checksum 8359 SEQUENCE /// ENTRY OKBY85 #type complete TITLE protein kinase PHO85 (EC 2.7.1.-) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein P7102.18c-a; protein YPL031c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1991 #sequence_revision 26-Jul-1996 #text_change 03-Dec-1999 ACCESSIONS S62043; S05853; JC1063; PC4036 REFERENCE S62026 !$#authors Dietrich, F.S.; Allen, E.; Araujo, R.; Aparicio, A.; !1Carpenter, J.; Cherry, J.M.; Chung, E.; Davis, K.; Duncan, !1M.; Hunicke-Smith, S.; Hyman, R.; Kalman, S.; Komp, C.; !1Kurdi, O.; Lashkari, D.; Lew, H.; Lin, A.; Lin, D.; Marathe, !1R.; Mirtipati, S.; Namath, A.; Oefner, P.; Petel, F.X.; !1Roberts, D.; Schramm, S.; Schroeder, M.; Botstein, D.; !1Davis, R.W. !$#submission submitted to the EMBL Data Library, December 1995 !$#accession S62043 !'##molecule_type DNA !'##residues 1-302 ##label DIE !'##cross-references EMBL:U44030; NID:g1171408; PID:g1171426; !1GSPDB:GN00016; MIPS:YPL031c REFERENCE S05853 !$#authors Uesono, Y.; Tanaka, K.; Toh-e, A. !$#journal Nucleic Acids Res. (1987) 15:10299-10309 !$#title Negative regulators of the PHO system in Saccharomyces !1cerevisiae: isolation and structural characterization of !1PHO85. !$#cross-references MUID:88096568; PMID:3320965 !$#accession S05853 !'##molecule_type DNA !'##residues 1-95,'A',97-302 ##label UES !'##cross-references EMBL:Y00867; NID:g4169; PIDN:CAA68774.1; PID:g4170 !'##experimental_source strain DC5 REFERENCE JC1063 !$#authors Zhong, H.L.; Li, B.L.; Ao, S.Z. !$#journal Acta Biochim. Biophys. Sin. (1992) 24:523-529 !$#title Cloning and high expression of yeast PHO85 gene in !1Escherichia coli. !$#accession JC1063 !'##molecule_type DNA !'##residues 1-83,'N',86-95,'A',97-302 ##label ZHO !$#accession PC4036 !'##molecule_type protein !'##residues 1-15 ##label ZH2 GENETICS !$#gene SGD:PHO85; MIPS:YPL031c !'##cross-references SGD:S0005952; MIPS:YPL031c !$#map_position 16L CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphotransferase; serine/threonine-specific protein !1kinase FEATURE !$2-258 #domain protein kinase homology #label KIN\ !$10-18 #region protein kinase ATP-binding motif\ !$33,50,130,132 #active_site Lys, Glu, Asp, Lys #status predicted SUMMARY #length 302 #molecular-weight 34700 #checksum 4888 SEQUENCE /// ENTRY S42101 #type complete TITLE protein kinase (EC 2.7.1.37) cdc2 homolog - Trypanosoma congolense ORGANISM #formal_name Trypanosoma congolense DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S42101 REFERENCE S42101 !$#authors Ricard, B.; Mottram, J.C.; Muthiani, A.; Omolo, E.; Pandit, !1P.; Gobright, E.; Murphy, N.B. !$#submission submitted to the EMBL Data Library, February 1994 !$#description Isolation and characterisation of a cdc2-like gene and its !1protein product from African trypanosomes. !$#accession S42101 !'##status preliminary !'##molecule_type DNA !'##residues 1-301 ##label RIC !'##cross-references EMBL:Z30312; NID:g457420; PIDN:CAA82956.1; !1PID:g457421 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphotransferase FEATURE !$3-257 #domain protein kinase homology #label KIN\ !$11-19 #region protein kinase ATP-binding motif\ !$34,52,127,129 #active_site Lys, Glu, Asp, Lys #status predicted SUMMARY #length 301 #molecular-weight 34467 #checksum 1814 SEQUENCE /// ENTRY S19209 #type complete TITLE protein kinase (EC 2.7.1.37) cdc2-like [similarity] - Trypanosoma brucei ORGANISM #formal_name Trypanosoma brucei DATE 16-Jun-2000 #sequence_revision 16-Jun-2000 #text_change 16-Jun-2000 ACCESSIONS S19209 REFERENCE S19209 !$#authors Ricard, B.; Mottram, J.C.; Muthiani, A.; Omolo, E.; Pandit, !1P.; Gobright, E.; Murphy, N.B. !$#submission submitted to the EMBL Data Library, January 1992 !$#description Isolation and characterisation of a cdc2-like gene and its !1protein product from african trypanosomes. !$#accession S19209 !'##molecule_type DNA !'##residues 1-301 ##label RIC !'##cross-references EMBL:X64314; NID:g10457; PIDN:CAA45595.1; !1PID:g10458 !'##experimental_source strain IsTat GENETICS !$#gene crk1 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$3-257 #domain protein kinase homology #label KIN\ !$11-19 #region protein kinase ATP-binding motif\ !$34,52,127,129 #active_site Lys, Glu, Asp, Lys #status predicted SUMMARY #length 301 #molecular-weight 34350 #checksum 1231 SEQUENCE /// ENTRY A48041 #type complete TITLE protein kinase (EC 2.7.1.37) cdc2-related CRK1 - Leishmania mexicana ORGANISM #formal_name Leishmania mexicana DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A48041; S31366 REFERENCE A48041 !$#authors Mottram, J.C.; Kinnaird, J.H.; Shiels, B.R.; Tait, A.; !1Barry, J.D. !$#journal J. Biol. Chem. (1993) 268:21044-21052 !$#title A novel CDC2-related protein kinase from Leishmania !1mexicana, LmmCRK1, is post-translationally regulated during !1the life cycle. !$#cross-references MUID:94012652; PMID:8407941 !$#accession A48041 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-301 ##label MOT !'##cross-references EMBL:X60385; NID:g9539; PIDN:CAA42936.1; PID:g9540 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphotransferase FEATURE !$3-257 #domain protein kinase homology #label KIN\ !$11-19 #region protein kinase ATP-binding motif\ !$34,52,127,129 #active_site Lys, Glu, Asp, Lys #status predicted SUMMARY #length 301 #molecular-weight 34473 #checksum 2123 SEQUENCE /// ENTRY S36607 #type complete TITLE protein kinase (EC 2.7.1.37) crk2 [similarity] - Trypanosoma brucei ORGANISM #formal_name Trypanosoma brucei DATE 16-Jun-2000 #sequence_revision 16-Jun-2000 #text_change 16-Jun-2000 ACCESSIONS S36607 REFERENCE S36607 !$#authors Smith, G.; Mottram, J. !$#submission submitted to the EMBL Data Library, August 1993 !$#description A family of CDC2-related kinases in Trypanosoma brucei. !$#accession S36607 !'##molecule_type DNA !'##residues 1-345 ##label SMI !'##cross-references EMBL:X74598; NID:g397161; PIDN:CAA52676.1; !1PID:g397162 !'##experimental_source strain IsTat GENETICS !$#gene crk2 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphotransferase FEATURE !$44-297 #domain protein kinase homology #label KIN\ !$52-60 #region protein kinase ATP-binding motif\ !$75,93,168,170 #active_site Lys, Glu, Asp, Lys #status predicted SUMMARY #length 345 #molecular-weight 39238 #checksum 6168 SEQUENCE /// ENTRY JN0631 #type complete TITLE protein kinase (EC 2.7.1.37) cdc2 homolog - Entamoeba histolytica ORGANISM #formal_name Entamoeba histolytica DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JN0631 REFERENCE JN0631 !$#authors Lohia, A.; Samuelson, J. !$#journal Gene (1993) 127:203-207 !$#title Cloning of the Eh cdc2 gene from Entamoeba histolytica !1encoding a protein kinase p34-cdc2 homologue. !$#cross-references MUID:93273232; PMID:8500762 !$#accession JN0631 !'##molecule_type DNA !'##residues 1-291 ##label LOH !'##cross-references GB:L03810; NID:g158923; PIDN:AAA51480.1; !1PID:g158924 GENETICS !$#gene cdc2 !$#introns 65/2 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$2-253 #domain protein kinase homology #label KIN\ !$10-18 #region protein kinase ATP-binding motif\ !$33,51,125,127 #active_site Lys, Glu, Asp, Lys #status predicted SUMMARY #length 291 #molecular-weight 33845 #checksum 881 SEQUENCE /// ENTRY A44293 #type complete TITLE protein kinase (EC 2.7.1.37) crk3 - mouse ALTERNATE_NAMES G1 cyclin, D type, catalytic subunit p34 PSK-J3/cdk4; tyrosine kinase Mpk-4 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A44293; PN0484; S30500; S19945 REFERENCE A44293 !$#authors Matsushime, H.; Ewen, M.E.; Strom, D.K.; Kato, J.Y.; Hanks, !1S.K.; Roussel, M.F.; Sherr, C.J. !$#journal Cell (1992) 71:323-334 !$#title Identification and properties of an atypical catalytic !1subunit (p34PSK-J3/cdk4) for mammalian D type G1 cyclins. !$#cross-references MUID:93046632; PMID:1423597 !$#accession A44293 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-303 ##label MAT !'##experimental_source BAC1.2F5A macrophage !'##note sequence extracted from NCBI backbone (NCBIP:116695) REFERENCE PN0479 !$#authors Ershler, M.A.; Nagorskaya, T.V.; Visser, J.W.M.; Belyavsky, !1A.V. !$#journal Gene (1993) 124:305-306 !$#title Novel CDC2-related protein kinases produced in murine !1hematopoietic stem cells. !$#cross-references MUID:93185941; PMID:8444355 !$#accession PN0484 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 138-184 ##label ERS !'##cross-references EMBL:X65069 REFERENCE S30496 !$#authors Gilardi-Hebenstreit, P.; Nieto, M.A.; Frain, M.; Mattei, !1M.G.; Chestier, A.; Wilkinson, D.G.; Charnay, P. !$#journal Oncogene (1992) 7:2499-2506 !$#title An Eph-related receptor protein tyrosine kinase gene !1segmentally expressed in the developing mouse hindbrain. !$#cross-references MUID:93096484; PMID:1281307 !$#accession S30500 !'##status preliminary !'##molecule_type mRNA !'##residues 142-188 ##label GIL !'##cross-references EMBL:X57238; NID:g53193; PIDN:CAA40514.1; !1PID:g53194 REFERENCE S19941 !$#authors Ershler, M.A.; Nagorskaya, T.V.; Visser, J.W.M.; Belyavsky, !1A.V. !$#submission submitted to the EMBL Data Library, March 1992 !$#description Novel cdc-related kinases expressed in early hematopoietic !1cells. !$#accession S19945 !'##molecule_type mRNA !'##residues 144-178 ##label ER2 !'##cross-references EMBL:X65069; NID:g50555; PIDN:CAA46202.1; !1PID:g50556 GENETICS !$#gene crk3 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; cell cycle control; phosphoprotein; phosphotransferase; !1serine/threonine-specific protein kinase FEATURE !$4-264 #domain protein kinase homology #label KIN\ !$12-20 #region protein kinase ATP-binding motif\ !$35,56,140,142 #active_site Lys, Glu, Asp, Lys #status predicted SUMMARY #length 303 #molecular-weight 33751 #checksum 3483 SEQUENCE /// ENTRY JN0460 #type complete TITLE protein kinase (EC 2.7.1.37) cdk4 - rat ALTERNATE_NAMES cyclin-dependent kinase 4 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JN0460 REFERENCE JN0460 !$#authors Cho, F.S.; Phillips, K.S.; Khan, S.A.; Weaver, T.E. !$#journal Biochem. Biophys. Res. Commun. (1993) 191:860-865 !$#title Cloning of the rat cyclin-dependent kinase 4 cDNA: !1Implication in proliferation-dependent expression in rat !1tissues. !$#cross-references MUID:93221528; PMID:8466525 !$#accession JN0460 !'##molecule_type mRNA !'##residues 1-303 ##label CHO !'##experimental_source fetal lung GENETICS !$#gene cdk4 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$4-264 #domain protein kinase homology #label KIN\ !$12-20 #region protein kinase ATP-binding motif\ !$17 #binding_site phosphate (Tyr) (covalent) #status !8predicted\ !$35,56,140,142 #active_site Lys, Glu, Asp, Lys #status predicted\ !$172 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$285 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 303 #molecular-weight 33799 #checksum 4403 SEQUENCE /// ENTRY S57926 #type complete TITLE protein kinase (EC 2.7.1.37) cdk4 - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S57926 REFERENCE S57922 !$#authors Cockerill, M.J.; Hunt, T. !$#submission submitted to the EMBL Data Library, July 1995 !$#description D-type cyclins in Xenopus laevis. !$#accession S57926 !'##status preliminary !'##molecule_type mRNA !'##residues 1-319 ##label COC !'##cross-references EMBL:X89477; NID:g897816; PIDN:CAA61666.1; !1PID:g897817 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphotransferase FEATURE !$7-279 #domain protein kinase homology #label KIN\ !$15-23 #region protein kinase ATP-binding motif\ !$38,56,140,142 #active_site Lys, Glu, Asp, Lys #status predicted SUMMARY #length 319 #molecular-weight 35684 #checksum 4868 SEQUENCE /// ENTRY TVHUP1 #type complete TITLE protein kinase (EC 2.7.1.37) pim-1 - human ALTERNATE_NAMES kinase-related transforming protein pim-1; pim-1 proto-oncogene protein-serine/threonine kinase ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1989 #sequence_revision 07-Oct-1994 #text_change 11-Jun-1999 ACCESSIONS JU0327; A46554; A27476; I58412 REFERENCE JU0327 !$#authors Reeves, R.; Spies, G.A.; Kiefer, M.; Barr, P.J.; Power, M. !$#journal Gene (1990) 90:303-307 !$#title Primary structure of the putative human oncogene, pim-1. !$#cross-references MUID:90382681; PMID:2205533 !$#accession JU0327 !'##molecule_type DNA !'##residues 1-313 ##label REE !'##cross-references GB:M27903; NID:g189958; PIDN:AAA60090.1; !1PID:g387022 REFERENCE A46554 !$#authors Meeker, T.C.; Nagarajan, L.; ar-Rushdi, A.; Croce, C.M. !$#journal J. Cell. Biochem. (1987) 35:105-112 !$#title Cloning and characterization of the human PIM-1 gene: a !1putative oncogene related to the protein kinases. !$#cross-references MUID:88115604; PMID:3429489 !$#accession A46554 !'##molecule_type mRNA !'##residues 1-313 ##label MEE !'##cross-references GB:M24779; NID:g1066790; PIDN:AAA81553.1; !1PID:g1066791 REFERENCE A27476 !$#authors Zakut-Houri, R.; Hazum, S.; Givol, D.; Telerman, A. !$#journal Gene (1987) 54:105-111 !$#title The cDNA sequence and gene analysis of the human pim !1oncogene. !$#cross-references MUID:87277423; PMID:3475233 !$#accession A27476 !'##molecule_type mRNA !'##residues 1-14,'RA',17-313 ##label ZAK !'##cross-references GB:M16750; NID:g189956; PIDN:AAA60089.1; !1PID:g189957 REFERENCE I58412 !$#authors Domen, J.; Von Lindern, M.; Hermans, A.; Breuer, M.; !1Grosveld, G.; Berns, A.A. !$#journal Oncogene Res. (1987) 1:103-112 !$#title Comparison of the human and mouse PIM-1 cDNAs: Nucleotide !1sequence and immunological identification of the in vitro !1synthesized PIM-1 protein. !$#cross-references MUID:88217305; PMID:3329709 !$#accession I58412 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-313 ##label DOM !'##cross-references GB:M54915; NID:g189961; PIDN:AAA36447.1; !1PID:g189962 COMMENT Pim-1 autophosphorylates at unknown sites. GENETICS !$#gene GDB:PIM1 !'##cross-references GDB:119495; OMIM:164960 !$#map_position 6p21.2-6p21.2 !$#introns 28/2; 63/3; 80/3; 203/1; 262/1 FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; autophosphorylation; phosphoprotein; !1phosphotransferase; proto-oncogene; serine/ !1threonine-specific protein kinase; transforming protein FEATURE !$36-290 #domain protein kinase homology #label KIN\ !$44-52 #region protein kinase ATP-binding motif\ !$67 #active_site Lys #status predicted SUMMARY #length 313 #molecular-weight 35685 #checksum 2798 SEQUENCE /// ENTRY S26298 #type complete TITLE protein kinase (EC 2.7.1.37) pim-1 - rat ALTERNATE_NAMES kinase-related transforming protein pim-1; pim-1 proto-oncogene protein-serine/threonine kinase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 25-Feb-1994 #sequence_revision 21-Jan-1997 #text_change 11-Jun-1999 ACCESSIONS S26298 REFERENCE S26298 !$#authors Wingett, D.; Reeves, R.; Magnuson, N.S. !$#journal Nucleic Acids Res. (1992) 20:3183-3189 !$#title Characterization of the testes-specific pim-1 transcript in !1rat. !$#cross-references MUID:92319652; PMID:1620615 !$#accession S26298 !'##molecule_type mRNA !'##residues 1-313 ##label WIN !'##cross-references EMBL:X63675; NID:g56902; PIDN:CAA45214.1; !1PID:g56903 !'##experimental_source testis !'##note testis-specific transcript is shorter and more stable than the !1somatic transcript because of an alternative polyadenylation !1site COMMENT Pim-1 autophosphorylates at unknown sites. FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP !$#note in testis may be involved in signal transduction events of !1normal germ cell maturation CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; autophosphorylation; phosphoprotein; !1phosphotransferase; proto-oncogene; serine/ !1threonine-specific protein kinase; transforming protein FEATURE !$36-290 #domain protein kinase homology #label KIN\ !$44-52 #region protein kinase ATP-binding motif\ !$67 #active_site Lys #status predicted SUMMARY #length 313 #molecular-weight 35630 #checksum 4225 SEQUENCE /// ENTRY TVMSP1 #type complete TITLE protein kinase (EC 2.7.1.37) pim-1 - mouse ALTERNATE_NAMES kinase-related transforming protein pim-1; pim-1 proto-oncogene protein-serine/threonine kinase ORGANISM #formal_name Mus musculus #common_name house mouse DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 11-Jun-1999 ACCESSIONS A24169 REFERENCE A24169 !$#authors Selten, G.; Cuypers, H.T.; Boelens, W.; Robanus-Maandag, E.; !1Verbeek, J.; Domen, J.; van Beveren, C.; Berns, A. !$#journal Cell (1986) 46:603-611 !$#title The primary structure of the putative oncogene pim-1 shows !1extensive homology with protein kinases. !$#cross-references MUID:86272109; PMID:3015420 !$#accession A24169 !'##molecule_type DNA !'##residues 1-313 ##label SEL !'##cross-references GB:M13945; GB:M13946; NID:g200352; PIDN:AAA39930.1; !1PID:g387510 COMMENT Pim-1 autophosphorylates at unknown sites. GENETICS !$#gene pim-1 !$#introns 28/1; 63/3; 80/3; 203/1; 262/1 FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; autophosphorylation; phosphotransferase; !1proto-oncogene; serine/threonine-specific protein kinase; !1transforming protein FEATURE !$36-290 #domain protein kinase homology #label KIN\ !$44-52 #region protein kinase ATP-binding motif\ !$67 #active_site Lys #status predicted SUMMARY #length 313 #molecular-weight 35536 #checksum 2811 SEQUENCE /// ENTRY S55333 #type complete TITLE protein kinase pim-2 (EC 2.7.1.-) - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Oct-1995 #sequence_revision 21-Jan-1997 #text_change 15-Oct-1999 ACCESSIONS S55333; A43093; B43093 REFERENCE S55333 !$#authors van der Lugt, N.M.T.; Domen, J.; Verhoeven, E.; Linders, K.; !1van der Gulden, H.; Allen, J.; Berns, A. !$#journal EMBO J. (1995) 14:2536-2544 !$#title Proviral tagging in E-mu-myc transgenic mice lacking the !1Pim-1 proto-oncogene leads to compensatory activation of !1Pim-2. !$#cross-references MUID:95300786; PMID:7781606 !$#accession S55333 !'##molecule_type mRNA !'##residues 1-370 ##label VAN !'##cross-references GB:L41495; NID:g765065; PIDN:AAA98922.1; !1PID:g765066 !'##note 40K form !$#accession A43093 !'##molecule_type mRNA !'##residues 'M',27-370 ##label VA2 !'##cross-references GB:L41495; NID:g765065; PIDN:AAA98923.1; !1PID:g765067 !'##note 37K form !$#accession B43093 !'##molecule_type mRNA !'##residues 'M',61-370 ##label VA3 !'##cross-references GB:L41495; NID:g765065; PIDN:AAA98924.1; !1PID:g765068 !'##note 34K form COMMENT Pim-2 autophosphorylates at unknown sites. GENETICS !$#gene Pim-2 !$#map_position X !$#start_codon CTG !$#note locus between A-raf and Act-7, near Kv4.1 FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS alternative initiators; ATP; autophosphorylation; !1phosphoprotein; phosphotransferase; proto-oncogene; serine/ !1threonine-specific protein kinase; transforming protein FEATURE !$89-345 #domain protein kinase homology #label KIN\ !$97-105 #region protein kinase ATP-binding motif\ !$120 #active_site Lys #status predicted SUMMARY #length 370 #molecular-weight 40059 #checksum 5844 SEQUENCE /// ENTRY B43674 #type complete TITLE protein kinase (EC 2.7.1.37) - human herpesvirus 2 ALTERNATE_NAMES kinase-related transforming protein; proto-oncogene protein-serine/threonine kinase; US3 protein ORGANISM #formal_name human herpesvirus 2 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B43674 REFERENCE A43674 !$#authors McGeoch, D.J.; Moss, H.W.M.; McNab, D.; Frame, M.C. !$#journal J. Gen. Virol. (1987) 68:19-38 !$#title DNA sequence and genetic content of the HindIII l region in !1the short unique component of the herpes simplex virus type !12 genome: identification of the gene encoding glycoprotein !1G, and evolutionary comparisons. !$#cross-references MUID:87111457; PMID:3027242 !$#accession B43674 !'##molecule_type DNA !'##residues 1-481 ##label MCG !'##cross-references EMBL:X04798; NID:g59900; PIDN:CAA28489.1; !1PID:g59903 !'##experimental_source strain HG52 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphotransferase; serine/threonine-specific protein !1kinase; transforming protein FEATURE !$189-455 #domain protein kinase homology #label KIN\ !$197-205 #region protein kinase ATP-binding motif\ !$220 #active_site Lys #status predicted SUMMARY #length 481 #molecular-weight 52677 #checksum 6291 SEQUENCE /// ENTRY TVMVM #type complete TITLE protein kinase (EC 2.7.1.37) MOS - Moloney murine sarcoma virus ALTERNATE_NAMES kinase-related transforming protein MOS; MOS proto-oncogene protein-serine/threonine kinase ORGANISM #formal_name Moloney murine sarcoma virus DATE 22-May-1981 #sequence_revision 17-Dec-1982 #text_change 11-Jun-1999 ACCESSIONS A00647; A92987 REFERENCE A00645 !$#authors Van Beveren, C.; van Straaten, F.; Galleshaw, J.A.; Verma, !1I.M. !$#journal Cell (1981) 27:97-108 !$#title Nucleotide sequence of the genome of a murine sarcoma virus. !$#cross-references MUID:82115347; PMID:6173134 !$#accession A00647 !'##molecule_type DNA !'##residues 1-255,'V',257-374 ##label VAN !'##cross-references GB:V01185; GB:J02263; NID:g61647; PIDN:CAA24508.1; !1PID:g61649 !'##experimental_source clone 124 REFERENCE A94610 !$#authors Van Beveren, C.; van Straaten, F.; Galleshaw, J.A.; Verma, !1I.M. !$#submission submitted to the Atlas, October 1982 !$#contents annotation; revision to residue 256 !$#note antisera raised against the carboxyl-terminal peptide !1inferred from this sequence cause immunoprecipitation of the !1protein; antisera against the sequence predicted by Reddy !1and his coworkers do not cause immunoprecipitation REFERENCE A92987 !$#authors Donoghue, D.J. !$#journal J. Virol. (1982) 42:538-546 !$#title Demonstration of biological activity and nucleotide sequence !1of an in vitro synthesized clone of the Moloney murine !1sarcoma virus mos gene. !$#cross-references MUID:82217036; PMID:7045395 !$#accession A92987 !'##molecule_type DNA !'##residues 1-374 ##label DON !'##cross-references GB:J02265 !'##experimental_source clone 124 REFERENCE A94261 !$#authors Reddy, E.P.; Smith, M.J.; Aaronson, S.A. !$#journal Science (1981) 214:445-450 !$#title Complete nucleotide sequence and organization of the Moloney !1murine sarcoma virus genome. !$#cross-references MUID:82039559; PMID:6170110 !$#contents annotation !$#note this sequence, translated from the genomic RNA sequence, has !1409 residues and differs from that shown due to a frameshift GENETICS !$#gene mos CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; oncogene; phosphotransferase; serine/threonine-specific !1protein kinase FEATURE !$92-373 #domain protein kinase homology #label KIN\ !$100-108 #region protein kinase ATP-binding motif\ !$121 #active_site Lys #status predicted SUMMARY #length 374 #molecular-weight 40977 #checksum 3872 SEQUENCE /// ENTRY TVMVMU #type complete TITLE protein kinase (EC 2.7.1.37) MOS - Moloney murine sarcoma virus (strain MuSVts110) ALTERNATE_NAMES kinase-related transforming protein MOS; MOS proto-oncogene protein-serine/threonine kinase ORGANISM #formal_name Moloney murine sarcoma virus DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 26-Feb-1999 ACCESSIONS B42745 REFERENCE A42745 !$#authors Huai, L.; Chiocca, S.M.; Gilbreth, M.A.; Ainsworth, J.R.; !1Bishop, L.A.; Murphy Jr., E.C. !$#journal J. Virol. (1992) 66:5329-5337 !$#title Moloney murine sarcoma virus MuSVts110 DNA: cloning, !1nucleotide sequence, and gene expression. !$#cross-references MUID:92365121; PMID:1501276 !$#accession B42745 !'##molecule_type DNA !'##residues 1-354 ##label HUA !'##cross-references GB:M96854 COMMENT This protein is probably translated as a gag-mos !1polyprotein. GENETICS !$#gene mos CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; oncogene; phosphotransferase; serine/threonine-specific !1protein kinase FEATURE !$72-353 #domain protein kinase homology #label KIN\ !$80-88 #region protein kinase ATP-binding motif\ !$101 #active_site Lys #status predicted SUMMARY #length 354 #molecular-weight 38850 #checksum 5637 SEQUENCE /// ENTRY TVMVHT #type complete TITLE protein kinase (EC 2.7.1.37) MOS - Moloney murine sarcoma virus (strain HT-1) ALTERNATE_NAMES kinase-related transforming protein MOS; MOS proto-oncogene protein-serine/threonine kinase ORGANISM #formal_name Moloney murine sarcoma virus DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 11-Jun-1999 ACCESSIONS A25318 REFERENCE A25318 !$#authors Seth, A.; Vande Woude, G.F. !$#journal J. Virol. (1985) 56:144-152 !$#title Nucleotide sequence and biochemical activities of the !1Moloney murine sarcoma virus strain HT-1 mos gene. !$#cross-references MUID:85293214; PMID:2993645 !$#accession A25318 !'##molecule_type DNA !'##residues 1-374 ##label SET !'##cross-references GB:M11909; NID:g331962; PIDN:AAA46496.1; !1PID:g331963 GENETICS !$#gene mos CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; oncogene; phosphotransferase; serine/threonine-specific !1protein kinase; transforming protein FEATURE !$92-373 #domain protein kinase homology #label KIN\ !$100-108 #region protein kinase ATP-binding motif\ !$121 #active_site Lys #status predicted SUMMARY #length 374 #molecular-weight 41094 #checksum 4100 SEQUENCE /// ENTRY TVMV1M #type complete TITLE protein kinase (EC 2.7.1.37) MOS - Moloney murine sarcoma virus (strain m1) ALTERNATE_NAMES kinase-related transforming protein MOS; MOS proto-oncogene protein-serine/threonine kinase ORGANISM #formal_name Moloney murine sarcoma virus DATE 18-Apr-1984 #sequence_revision 18-Apr-1984 #text_change 11-Jun-1999 ACCESSIONS A00646 REFERENCE A00646 !$#authors Brow, M.A.D.; Sen, A.; Sutcliffe, J.G. !$#journal J. Virol. (1984) 49:579-582 !$#title Nucleotide sequence of the transforming gene of m1 murine !1sarcoma virus. !$#cross-references MUID:84115084; PMID:6319757 !$#accession A00646 !'##molecule_type DNA !'##residues 1-376 ##label BRO !'##cross-references GB:K02728; NID:g331964; PIDN:AAA46497.1; !1PID:g331965 GENETICS !$#gene mos CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; oncogene; phosphotransferase; serine/threonine-specific !1protein kinase FEATURE !$92-373 #domain protein kinase homology #label KIN\ !$100-108 #region protein kinase ATP-binding motif\ !$121 #active_site Lys #status predicted SUMMARY #length 376 #molecular-weight 41330 #checksum 8391 SEQUENCE /// ENTRY TVMVM9 #type complete TITLE protein kinase (EC 2.7.1.37) MOS (clone ts159) - myeloproliferative sarcoma virus ALTERNATE_NAMES kinase-related transforming protein MOS; MOS proto-oncogene protein-serine/threonine kinase ORGANISM #formal_name myeloproliferative sarcoma virus DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 11-Jun-1999 ACCESSIONS A26592 REFERENCE A26592 !$#authors Friel, J.; Stocking, C.; Stacey, A.; Ostertag, W. !$#journal J. Virol. (1987) 61:889-897 !$#title A temperature-sensitive mutant of the myeloproliferative !1sarcoma virus, altered by a point mutation in the mos !1oncogene, has been modified as a selectable retroviral !1vector. !$#cross-references MUID:87113002; PMID:3027415 !$#accession A26592 !'##molecule_type DNA !'##residues 1-342 ##label FRI !'##cross-references GB:M15424; NID:g332210; PIDN:AAA46581.1; !1PID:g332211 GENETICS !$#gene mos CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; oncogene; phosphotransferase; serine/threonine-specific !1protein kinase; transforming protein FEATURE !$61-341 #domain protein kinase homology #label KIN\ !$69-77 #region protein kinase ATP-binding motif\ !$90 #active_site Lys #status predicted SUMMARY #length 342 #molecular-weight 37970 #checksum 8888 SEQUENCE /// ENTRY TVMSM #type complete TITLE protein kinase (EC 2.7.1.37) MOS - mouse ALTERNATE_NAMES kinase-related transforming protein MOS; MOS proto-oncogene protein-serine/threonine kinase ORGANISM #formal_name Mus musculus #common_name house mouse DATE 17-Dec-1982 #sequence_revision 18-Apr-1984 #text_change 20-Aug-1994 ACCESSIONS A00645; A38015 REFERENCE A00645 !$#authors Van Beveren, C.; van Straaten, F.; Galleshaw, J.A.; Verma, !1I.M. !$#journal Cell (1981) 27:97-108 !$#title Nucleotide sequence of the genome of a murine sarcoma virus. !$#cross-references MUID:82115347; PMID:6173134 !$#accession A00645 !'##molecule_type DNA !'##residues 1-390 ##label VAN REFERENCE A38015 !$#authors Rechavi, G.; Givol, D.; Canaani, E. !$#journal Nature (1982) 300:607-611 !$#title Activation of a cellular oncogene by DNA rearrangement: !1possible involvement of an IS-like element. !$#cross-references MUID:83062922; PMID:6292737 !$#accession A38015 !'##molecule_type DNA !'##residues 1-97 ##label REC GENETICS !$#gene mos CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphotransferase; proto-oncogene; serine/ !1threonine-specific protein kinase FEATURE !$108-389 #domain protein kinase homology #label KIN\ !$116-124 #region protein kinase ATP-binding motif\ !$137 #active_site Lys #status predicted SUMMARY #length 390 #molecular-weight 42890 #checksum 3920 SEQUENCE /// ENTRY TVRTM #type complete TITLE protein kinase (EC 2.7.1.37) MOS - rat ALTERNATE_NAMES kinase-related transforming protein MOS; MOS proto-oncogene protein-serine/threonine kinase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 18-Apr-1984 #sequence_revision 18-Apr-1984 #text_change 11-Jun-1999 ACCESSIONS A00648; I60596 REFERENCE A00648 !$#authors Van der Hoorn, F.A.; Firzlaff, J. !$#journal Nucleic Acids Res. (1984) 12:2147-2156 !$#title Complete c-mos (rat) nucleotide sequence: presence of !1conserved domains in c-mos proteins. !$#cross-references MUID:84144095; PMID:6322135 !$#accession A00648 !'##molecule_type DNA !'##residues 1-339 ##label VAN !'##note the authors translated the codon TAC for residue 279 as His and !1GAG for 295 as Ala REFERENCE I60596 !$#authors Leibovitch, S.A.; Lenormand, J.L.; Leibovitch, M.P.; !1Guiller, M.; Mallard, L.; Harel, J. !$#journal Oncogene (1990) 5:1149-1157 !$#title Rat myogenic c-mos cDNA: cloning sequence analysis and !1regulation during muscle development. !$#cross-references MUID:90363547; PMID:1697408 !$#accession I60596 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-46,'V',48-101,'A',103-294,'A',296-339 ##label RES !'##cross-references EMBL:X52952; NID:g55965; PIDN:CAA37128.1; !1PID:g55966 GENETICS !$#gene mos CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphotransferase; proto-oncogene; serine/ !1threonine-specific protein kinase FEATURE !$59-338 #domain protein kinase homology #label KIN\ !$67-75 #region protein kinase ATP-binding motif\ !$88 #active_site Lys #status predicted SUMMARY #length 339 #molecular-weight 37679 #checksum 6230 SEQUENCE /// ENTRY TVHUMS #type complete TITLE protein kinase (EC 2.7.1.37) MOS - human ALTERNATE_NAMES kinase-related transforming protein MOS; MOS proto-oncogene protein-serine/threonine kinase ORGANISM #formal_name Homo sapiens #common_name man DATE 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 11-Jun-1999 ACCESSIONS A00649 REFERENCE A00649 !$#authors Watson, R.; Oskarsson, M.; Vande Woude, G.F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:4078-4082 !$#title Human DNA sequence homologous to the transforming gene (mos) !1of Moloney murine sarcoma virus. !$#cross-references MUID:82275068; PMID:6287464 !$#accession A00649 !'##molecule_type DNA !'##residues 1-346 ##label WAT !'##cross-references GB:J00119; NID:g180640; PIDN:AAA52029.1; !1PID:g180641 !'##experimental_source placenta GENETICS !$#gene GDB:MOS !'##cross-references GDB:119396; OMIM:190060 !$#map_position 8q11-8q11 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphotransferase; proto-oncogene; serine/ !1threonine-specific protein kinase; transforming protein FEATURE !$58-345 #domain protein kinase homology #label KIN\ !$66-74 #region protein kinase ATP-binding motif\ !$87 #active_site Lys #status predicted SUMMARY #length 346 #molecular-weight 37819 #checksum 6719 SEQUENCE /// ENTRY TVMKMS #type complete TITLE protein kinase (EC 2.7.1.37) MOS - green monkey ALTERNATE_NAMES kinase-related transforming protein MOS; MOS proto-oncogene protein-serine/threonine kinase ORGANISM #formal_name Cercopithecus aethiops #common_name green monkey, grivet DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 20-Aug-1994 ACCESSIONS A28264 REFERENCE A28264 !$#authors Paules, R.S.; Propst, F.; Dunn, K.J.; Blair, D.G.; Kaul, K.; !1Palmer, A.E.; Vande Woude, G.F. !$#journal Oncogene (1988) 3:59-68 !$#title Primate c-mos proto-oncogene structure and expression: !1transcription initiation both upstream and within the gene !1in a tissue-specific manner. !$#accession A28264 !'##molecule_type DNA !'##residues 1-346 ##label PAU GENETICS !$#gene mos CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphotransferase; proto-oncogene; serine/ !1threonine-specific protein kinase; transforming protein FEATURE !$58-345 #domain protein kinase homology #label KIN\ !$66-74 #region protein kinase ATP-binding motif\ !$87 #active_site Lys #status predicted SUMMARY #length 346 #molecular-weight 37740 #checksum 7576 SEQUENCE /// ENTRY TVCHMS #type complete TITLE protein kinase (EC 2.7.1.37) MOS - chicken ALTERNATE_NAMES kinase-related transforming protein MOS; MOS proto-oncogene protein-serine/threonine kinase ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 11-Jun-1999 ACCESSIONS A28130 REFERENCE A28130 !$#authors Schmidt, M.; Oskarsson, M.K.; Dunn, J.K.; Blair, D.G.; !1Hughes, S.; Propst, F.; Vande Woude, G.F. !$#journal Mol. Cell. Biol. (1988) 8:923-929 !$#title Chicken homolog of the mos proto-oncogene. !$#cross-references MUID:88174737; PMID:2832744 !$#accession A28130 !'##molecule_type DNA !'##residues 1-349 ##label SCH !'##cross-references GB:M19412; NID:g212343; PIDN:AAA48959.1; !1PID:g212344 GENETICS !$#gene mos CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphotransferase; proto-oncogene; serine/ !1threonine-specific protein kinase; transforming protein FEATURE !$62-349 #domain protein kinase homology #label KIN\ !$70-78 #region protein kinase ATP-binding motif\ !$91 #active_site Lys #status predicted SUMMARY #length 349 #molecular-weight 38263 #checksum 7286 SEQUENCE /// ENTRY TVXLMS #type complete TITLE protein kinase (EC 2.7.1.37) MOS - African clawed frog ALTERNATE_NAMES 39K phosphoprotein; kinase-related transforming protein MOS; MOS proto-oncogene protein-serine/threonine kinase; PP39-MOS ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 30-Sep-1990 #sequence_revision 30-Sep-1992 #text_change 11-Jun-1999 ACCESSIONS S06433; A33547 REFERENCE S06433 !$#authors Sagata, N.; Oskarsson, M.; Copeland, T.; Brumbaugh, J.; !1vande Woude, G.F. !$#journal Nature (1988) 335:519-525 !$#title Function of c-mos proto-oncogene product in meiotic !1maturation in Xenopus oocytes. !$#cross-references MUID:88334744; PMID:2971141 !$#accession S06433 !'##molecule_type mRNA !'##residues 1-359 ##label SAG !'##cross-references EMBL:X13311; NID:g64957; PIDN:CAA31689.1; !1PID:g64958 !'##note the authors translated the codon CGG for residue 103 as Lys REFERENCE A33547 !$#authors Freeman, R.S.; Pickham, K.M.; Kanki, J.P.; Lee, B.A.; Pena, !1S.V.; Donoghue, D.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:5805-5809 !$#title Xenopus homolog of the mos protooncogene transforms !1mammalian fibroblasts and induces maturation of Xenopus !1oocytes. !$#cross-references MUID:89345555; PMID:2527365 !$#accession A33547 !'##molecule_type mRNA !'##residues 1-45,'P',47-359 ##label FRE !'##cross-references EMBL:M25366; NID:g214039; PIDN:AAA49677.1; !1PID:g214040 GENETICS !$#gene mos CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; meiosis; phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase; transforming protein FEATURE !$61-338 #domain protein kinase homology #label KIN\ !$69-77 #region protein kinase ATP-binding motif\ !$90 #active_site Lys #status predicted SUMMARY #length 359 #molecular-weight 39221 #checksum 5399 SEQUENCE /// ENTRY TVMVF6 #type complete TITLE protein kinase (EC 2.7.1.37) raf - murine sarcoma virus 3611 ALTERNATE_NAMES kinase-related transforming protein raf; raf proto-oncogene protein-serine/threonine kinase ORGANISM #formal_name murine sarcoma virus 3611 #note host Mus musculus (mouse) DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 23-Feb-1997 ACCESSIONS A00638; A38020 REFERENCE A00638 !$#authors Kan, N.C.; Flordellis, C.S.; Mark, G.E.; Duesberg, P.H.; !1Papas, T.S. !$#journal Science (1984) 223:813-816 !$#title A common onc gene sequence transduced by avian carcinoma !1virus MH2 and by murine sarcoma virus 3611. !$#cross-references MUID:84121298; PMID:6320371 !$#accession A00638 !'##molecule_type DNA !'##residues 1-323 ##label KAN !'##experimental_source ATCC 45010 REFERENCE A38020 !$#authors Mark, G.E.; Rapp, U.R. !$#journal Science (1984) 224:285-289 !$#title Primary structure of v-raf: relatedness to the src family of !1oncogenes. !$#cross-references MUID:84172180; PMID:6324342 !$#accession A38020 !'##molecule_type DNA !'##residues 1-323 ##label MAR COMMENT This protein is translated as a gag-raf polyprotein. GENETICS !$#gene raf CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; oncogene; phosphotransferase; serine/threonine-specific !1protein kinase; transforming protein FEATURE !$22-288 #domain protein kinase homology #label KIN\ !$30-38 #region protein kinase ATP-binding motif\ !$50 #active_site Lys #status predicted SUMMARY #length 323 #molecular-weight 36883 #checksum 1664 SEQUENCE /// ENTRY TVFVMM #type complete TITLE protein kinase (EC 2.7.1.37) mil - avian myelocytomatosis virus MH2 ALTERNATE_NAMES kinase-related transforming protein mil (mht); mil proto-oncogene protein-serine/threonine kinase ORGANISM #formal_name avian myelocytomatosis virus MH2 #note host Gallus gallus (chicken) DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 23-Feb-1997 ACCESSIONS A00639; B00638; A21137 REFERENCE A00639 !$#authors Sutrave, P.; Bonner, T.I.; Rapp, U.R.; Jansen, H.W.; !1Patschinsky, T.; Bister, K. !$#journal Nature (1984) 309:85-88 !$#title Nucleotide sequence of avian retroviral oncogene v-mil: !1homologue of murine retroviral oncogene v-raf. !$#cross-references MUID:84191511; PMID:6325930 !$#accession A00639 !'##molecule_type DNA !'##residues 1-380 ##label SUT !'##cross-references GB:K02082 !'##note the authors translated the codon CAG for residue 58 as Gly REFERENCE A00638 !$#authors Kan, N.C.; Flordellis, C.S.; Mark, G.E.; Duesberg, P.H.; !1Papas, T.S. !$#journal Science (1984) 223:813-816 !$#title A common onc gene sequence transduced by avian carcinoma !1virus MH2 and by murine sarcoma virus 3611. !$#cross-references MUID:84121298; PMID:6320371 !$#accession B00638 !'##molecule_type DNA !'##residues 1-210,'E',212-380 ##label KAN !'##cross-references GB:K02084 REFERENCE A21137 !$#authors Kan, N.C.; Flordellis, C.S.; Mark, G.E.; Duesberg, P.H.; !1Papas, T.S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:3000-3004 !$#title Nucleotide sequence of avian carcinoma virus MH2: two !1potential onc genes, one related to avian virus MC29 and the !1other related to murine sarcoma virus 3611. !$#cross-references MUID:84221892; PMID:6328485 !$#accession A21137 !'##molecule_type DNA !'##residues 1-210,'E',212-230,'E',232-380 ##label KA2 !'##cross-references GB:K02082 COMMENT This protein is translated as a gag-mht or gag-mil !1polyprotein. GENETICS !$#gene mht; mil CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; oncogene; phosphotransferase; polyprotein; serine/ !1threonine-specific protein kinase; transforming protein FEATURE !$80-346 #domain protein kinase homology #label KIN\ !$88-96 #region protein kinase ATP-binding motif\ !$108 #active_site Lys #status predicted SUMMARY #length 380 #molecular-weight 42853 #checksum 2221 SEQUENCE /// ENTRY TVFVMR #type complete TITLE protein kinase (EC 2.7.1.37) R-mil - Rous-associated virus (type 1) ALTERNATE_NAMES kinase-related transforming protein R-mil; R-mil proto-oncogene protein-serine/threonine kinase ORGANISM #formal_name Rous-associated virus #note host Gallus gallus (chicken) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 11-Jun-1999 ACCESSIONS A40341 REFERENCE A40341 !$#authors Felder, M.P.; Eychene, A.; Barnier, J.V.; Calogeraki, I.; !1Calothy, G.; Marx, M. !$#journal J. Virol. (1991) 65:3633-3640 !$#title Common mechanism of retrovirus activation and transduction !1of c-mil and c-Rmil in chicken neuroretina cells infected !1with Rous-associated virus type 1. !$#cross-references MUID:91251215; PMID:1645786 !$#accession A40341 !'##molecule_type DNA !'##residues 1-450 ##label FEL !'##cross-references GB:M62407; NID:g210080; PIDN:AAA42549.1; !1PID:g210081 COMMENT This protein is translated as a mil-env polyprotein. GENETICS !$#gene R-mil CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; oncogene; phosphotransferase; serine/threonine-specific !1protein kinase; transforming protein FEATURE !$81-347 #domain protein kinase homology #label KIN\ !$89-97 #region protein kinase ATP-binding motif\ !$109 #active_site Lys #status predicted SUMMARY #length 450 #molecular-weight 50313 #checksum 7337 SEQUENCE /// ENTRY A40811 #type complete TITLE myosin-light-chain kinase (EC 2.7.1.117) A - slime mold (Dictyostelium discoideum) ALTERNATE_NAMES MLCK-A ORGANISM #formal_name Dictyostelium discoideum DATE 10-Apr-1992 #sequence_revision 21-Jan-1997 #text_change 11-Jun-1999 ACCESSIONS A40811; A37125 REFERENCE A40811 !$#authors Tan, J.L.; Spudich, J.A. !$#journal J. Biol. Chem. (1991) 266:16044-16049 !$#title Characterization and bacterial expression of the !1Dictyostelium myosin light chain kinase cDNA. Identification !1of an autoinhibitory domain. !$#cross-references MUID:91340753; PMID:1651931 !$#accession A40811 !'##molecule_type mRNA !'##residues 1-301 ##label TAN !'##cross-references GB:M64176; NID:g1498249; PIDN:AAB06337.1; !1PID:g1498250 REFERENCE A37125 !$#authors Tan, J.L.; Spudich, J.A. !$#journal J. Biol. Chem. (1990) 265:13818-13824 !$#title Dictyostelium myosin light chain kinase. Purification and !1characterization. !$#cross-references MUID:90337997; PMID:2380188 !$#accession A37125 !'##molecule_type protein !'##residues 9-12,'I',14-19;163-167,'S',169-179;192-198 ##label TA2 GENETICS !$#gene mlkA FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate, using ATP, in myosin !1regulatory light chain, activating myosin ATPase and !1contractile activity, and in itself !$#pathway cytokinesis; fruiting body formation !$#note not activated by Ca2+/calmodulin in contrast with MLCK from !1higher eukaryotes CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; autophosphorylation; cell division; phosphoprotein; !1phosphotransferase; serine/threonine-specific protein kinase FEATURE !$6-265 #domain protein kinase homology #label KIN\ !$14-22 #region protein kinase ATP-binding motif\ !$267-295 #domain inhibitory #status predicted #label INH\ !$37 #active_site Lys #status predicted\ !$296 #binding_site phosphate (Thr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 301 #molecular-weight 34309 #checksum 8980 SEQUENCE /// ENTRY TVBE17 #type complete TITLE protein kinase (EC 2.7.1.37) - human herpesvirus 1 ALTERNATE_NAMES kinase-related transforming protein; proto-oncogene protein-serine/threonine kinase ORGANISM #formal_name human herpesvirus 1 #note host Homo sapiens (man) DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 11-Jun-1999 ACCESSIONS A00656 REFERENCE A00656 !$#authors McGeoch, D.J.; Dolan, A.; Donald, S.; Rixon, F.J. !$#journal J. Mol. Biol. (1985) 181:1-13 !$#title Sequence determination and genetic content of the short !1unique region in the genome of herpes simplex virus type 1. !$#cross-references MUID:85160822; PMID:2984429 !$#accession A00656 !'##molecule_type DNA !'##residues 1-481 ##label MCG !'##cross-references GB:X02138; NID:g59865; PIDN:CAA26057.1; PID:g59869 !'##experimental_source strain 17 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphotransferase; serine/threonine-specific protein !1kinase; transforming protein FEATURE !$189-455 #domain protein kinase homology #label KIN\ !$197-205 #region protein kinase ATP-binding motif\ !$220 #active_site Lys #status predicted SUMMARY #length 481 #molecular-weight 52834 #checksum 463 SEQUENCE /// ENTRY TVBE66 #type complete TITLE protein kinase (EC 2.7.1.37) - human herpesvirus 3 ALTERNATE_NAMES kinase-related transforming protein; proto-oncogene protein-serine/threonine kinase ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 11-Jun-1999 ACCESSIONS E27345 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession E27345 !'##molecule_type DNA !'##residues 1-393 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27949.1; !1PID:g60055 GENETICS !$#gene 66 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphotransferase; serine/threonine-specific protein !1kinase; transforming protein FEATURE !$91-355 #domain protein kinase homology #label KIN\ !$122 #active_site Lys #status predicted SUMMARY #length 393 #molecular-weight 43679 #checksum 6375 SEQUENCE /// ENTRY B46113 #type complete TITLE protein kinase (EC 2.7.1.37) - cercopithecine herpesvirus 9 (strain DHV) ALTERNATE_NAMES kinase-related transforming protein; proto-oncogene protein-serine/threonine kinase ORGANISM #formal_name cercopithecine herpesvirus 9 DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 11-Jun-1999 ACCESSIONS B46113 REFERENCE A46113 !$#authors Fletcher III, T.M.; Gray, W.L. !$#journal Virology (1993) 193:762-773 !$#title DNA sequence and genetic organization of the unique short !1(Us) region of the simian varicella virus genome. !$#cross-references MUID:93212509; PMID:8384754 !$#accession B46113 !'##molecule_type DNA !'##residues 1-345 ##label FLE !'##cross-references GB:L07067; NID:g310715; PIDN:AAA47887.1; !1PID:g310717 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphotransferase; serine/threonine-specific protein !1kinase; transforming protein FEATURE !$47-310 #domain protein kinase homology #label KIN\ !$78 #active_site Lys #status predicted SUMMARY #length 345 #molecular-weight 38954 #checksum 9556 SEQUENCE /// ENTRY TVBEPS #type complete TITLE protein kinase (EC 2.7.1.37) - suid herpesvirus 1 (strain Ka) ALTERNATE_NAMES kinase-related transforming protein; proto-oncogene protein-serine/threonine kinase ORGANISM #formal_name suid herpesvirus 1 DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jun-2000 ACCESSIONS A36655 REFERENCE A36655 !$#authors Zhang, G.; Stevens, R.; Leader, D.P. !$#journal J. Gen. Virol. (1990) 71:1757-1765 !$#title The protein kinase encoded in the short unique region of !1pseudorabies virus: description of the gene and !1identification of its product in virions and in infected !1cells. !$#cross-references MUID:90362062; PMID:2167929 !$#accession A36655 !'##molecule_type DNA !'##residues 1-334 ##label ZHA !'##cross-references GB:D00676; EMBL:D00545; NID:g222595; !1PIDN:BAA00581.1; PID:g2160376 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphotransferase; serine/threonine-specific protein !1kinase; transforming protein FEATURE !$51-309 #domain protein kinase homology #label KIN\ !$59-67 #region protein kinase ATP-binding motif\ !$82 #active_site Lys #status predicted SUMMARY #length 334 #molecular-weight 36879 #checksum 8540 SEQUENCE /// ENTRY TVBEPN #type complete TITLE protein kinase (EC 2.7.1.37) - suid herpesvirus 1 (strain NIA-3) ALTERNATE_NAMES kinase-related transforming protein; proto-oncogene protein-serine/threonine kinase ORGANISM #formal_name suid herpesvirus 1 DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 20-Aug-1994 ACCESSIONS A36654 REFERENCE A36654 !$#authors van Zijl, M.; van der Gulden, H.; de Wind, N.; Gielkens, A.; !1Berns, A. !$#journal J. Gen. Virol. (1990) 71:1747-1755 !$#title Identification of two genes in the unique short region of !1pseudorabies virus; comparison with herpes simplex virus and !1varicella-zoster virus. !$#cross-references MUID:90362061; PMID:2167928 !$#accession A36654 !'##molecule_type DNA !'##residues 1-390 ##label VAN CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphotransferase; serine/threonine-specific protein !1kinase; transforming protein FEATURE !$107-365 #domain protein kinase homology #label KIN\ !$115-123 #region protein kinase ATP-binding motif\ !$138 #active_site Lys #status predicted SUMMARY #length 390 #molecular-weight 43029 #checksum 483 SEQUENCE /// ENTRY TVBEG1 #type complete TITLE protein kinase (EC 2.7.1.37) - equine herpesvirus 1 (strain Ab4p) ALTERNATE_NAMES kinase-related transforming protein; proto-oncogene protein-serine/threonine kinase ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 11-Jun-1999 ACCESSIONS F36802 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession F36802 !'##molecule_type DNA !'##residues 1-382 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02504.1; !1PID:g330860 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 69 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphotransferase; serine/threonine-specific protein !1kinase; transforming protein FEATURE !$91-356 #domain protein kinase homology #label KIN\ !$99-107 #region protein kinase ATP-binding motif\ !$122 #active_site Lys #status predicted SUMMARY #length 382 #molecular-weight 42543 #checksum 9217 SEQUENCE /// ENTRY TVBEKA #type complete TITLE protein kinase (EC 2.7.1.37) - equine herpesvirus 1 (strain Kentucky A) ALTERNATE_NAMES kinase-related transforming protein; proto-oncogene protein-serine/threonine kinase ORGANISM #formal_name equine herpesvirus 1 DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 11-Jun-1999 ACCESSIONS A42538 REFERENCE A42538 !$#authors Colle III, C.F.; Flowers, C.C.; O'Callaghan, D.J. !$#journal Virology (1992) 188:545-557 !$#title Open reading frames encoding a protein kinase, homolog of !1glycoprotein gX of pseudorabies virus, and a novel !1glycoprotein map within the unique short segment of equine !1herpesvirus type 1. !$#cross-references MUID:92263758; PMID:1316673 !$#accession A42538 !'##molecule_type DNA !'##residues 1-382 ##label COL !'##cross-references GB:M87497; NID:g330878; PIDN:AAA46070.1; !1PID:g330880 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphotransferase; serine/threonine-specific protein !1kinase; transforming protein FEATURE !$91-356 #domain protein kinase homology #label KIN\ !$99-107 #region protein kinase ATP-binding motif\ !$122 #active_site Lys #status predicted SUMMARY #length 382 #molecular-weight 42503 #checksum 8602 SEQUENCE /// ENTRY C48338 #type complete TITLE protein kinase (EC 2.7.1.37) - equine herpesvirus 4 (strain 405/76) ALTERNATE_NAMES kinase-related transforming protein ORGANISM #formal_name equine herpesvirus 4 #note host Equus caballus (domestic horse) DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 11-Jun-1999 ACCESSIONS C48338 REFERENCE A48338 !$#authors Nagesha, H.S.; Crabb, B.S.; Studdert, M.J. !$#journal Arch. Virol. (1993) 128:143-154 !$#title Analysis of the nucleotide sequence of five genes at the !1left end of the unique short region of the equine !1herpesvirus 4 genome. !$#cross-references MUID:93119267; PMID:8380320 !$#accession C48338 !'##molecule_type DNA !'##residues 1-328 ##label NAG !'##cross-references GB:M89634; NID:g330929; PIDN:AAA46102.1; !1PID:g330932 !'##note sequence extracted from NCBI backbone (NCBIN:121741, !1NCBIP:121744) GENETICS !$#gene 69 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphotransferase; serine/threonine-specific protein !1kinase; transforming protein FEATURE !$37-302 #domain protein kinase homology #label KIN\ !$45-53 #region protein kinase ATP-binding motif\ !$68 #active_site Lys #status predicted SUMMARY #length 328 #molecular-weight 37064 #checksum 3740 SEQUENCE /// ENTRY F48552 #type complete TITLE protein kinase (EC 2.7.1.37) - infectious laryngotracheitis virus ALTERNATE_NAMES kinase-related transforming protein ORGANISM #formal_name infectious laryngotracheitis virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 11-Jun-1999 ACCESSIONS F48552 REFERENCE A48552 !$#authors Sakaguchi, M.; Urakawa, T.; Hirayama, Y.; Miki, N.; !1Yamamoto, M.; Hirai, K. !$#journal Virus Genes (1992) 6:365-378 !$#title Sequence determination and genetic content of an 8.9-kb !1restriction fragment in the short unique region and the !1internal inverted repeat of Marek's disease virus type 1 !1DNA. !$#cross-references MUID:93118245; PMID:1282282 !$#accession F48552 !'##molecule_type DNA !'##residues 1-402 ##label SAK !'##cross-references GB:M80595; NID:g291557; PIDN:AAB59895.1; !1PID:g291564 !'##note sequence extracted from NCBI backbone (NCBIN:121622, !1NCBIP:121630) !'##note the source is designated as Marek's disease virus type 1 by the !1authors, and as Gallid herpesvirus 1 in GenBank entry !1HSMUSORFS, release 109.0 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphotransferase; protein kinase; transforming !1protein FEATURE !$100-363 #domain protein kinase homology #label KIN\ !$133 #active_site Lys #status predicted SUMMARY #length 402 #molecular-weight 44715 #checksum 3577 SEQUENCE /// ENTRY TVVZVW #type complete TITLE protein kinase (EC 2.7.1.37) B1R - vaccinia virus (strain WR) ALTERNATE_NAMES B1R protein ORGANISM #formal_name vaccinia virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jun-2000 ACCESSIONS A34152; B33610; JQ1795 REFERENCE A34152 !$#authors Traktman, P.; Anderson, M.K.; Rempel, R.E. !$#journal J. Biol. Chem. (1989) 264:21458-21461 !$#title Vaccinia virus encodes an essential gene with strong !1homology to protein kinases. !$#cross-references MUID:90094307; PMID:2600076 !$#accession A34152 !'##molecule_type DNA !'##residues 1-300 ##label TRA !'##cross-references EMBL:J05178; NID:g335305; PIDN:AAA47963.1; !1PID:g335306 REFERENCE A33610 !$#authors Howard, S.T.; Smith, G.L. !$#journal J. Gen. Virol. (1989) 70:3187-3201 !$#title Two early vaccinia virus genes encode polypeptides related !1to protein kinases. !$#cross-references MUID:90111697; PMID:2607336 !$#accession B33610 !'##molecule_type DNA !'##residues 1-300 ##label HOW !'##cross-references EMBL:D00628; NID:g222700; PIDN:BAA00519.1; !1PID:g222701 REFERENCE JQ1767 !$#authors Smith, G.L.; Chan, Y.S.; Howard, S.T. !$#journal J. Gen. Virol. (1991) 72:1349-1376 !$#title Nucleotide sequence of 42kbp of vaccinia virus strain WR !1from near the right inverted terminal repeat. !$#cross-references MUID:91259063; PMID:2045793 !$#accession JQ1795 !'##molecule_type DNA !'##residues 1-300 ##label SMI !'##cross-references DDBJ:D11079; NID:g222717; PIDN:BAA01831.1; !1PID:g222746; DDBJ:D00628; NID:g222700; PID:g222701 COMMENT This protein is expressed early during infection and is !1essential for viral replication. GENETICS !$#gene B1R FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP !$#note ribosomal proteins Sa and S2 are substrates CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphotransferase; serine/threonine-specific protein !1kinase FEATURE !$14-300 #domain protein kinase homology #label KIN\ !$22-30 #region protein kinase ATP-binding motif\ !$41 #active_site Lys #status predicted SUMMARY #length 300 #molecular-weight 34273 #checksum 4231 SEQUENCE /// ENTRY TVVZ9Z #type complete TITLE protein kinase (EC 2.7.1.37) B1R - vaccinia virus (strain Copenhagen) ALTERNATE_NAMES B1R protein ORGANISM #formal_name vaccinia virus #note host Homo sapiens (man) DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 11-Jun-1999 ACCESSIONS I42525 REFERENCE A42501 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:517-563 !$#title Appendix to "The complete DNA sequence of vaccinia virus". !$#accession I42525 !'##molecule_type DNA !'##residues 1-300 ##label GOE !'##cross-references GB:M35027; NID:g335317; PIDN:AAA48194.1; !1PID:g335542 REFERENCE A42531 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:247-266 !$#title The complete DNA sequence of vaccinia virus. !$#cross-references MUID:91021027; PMID:2219722 !$#contents annotation; possible protein-coding frames COMMENT This protein is expressed early during infection and is !1essential for viral replication. GENETICS !$#gene B1R FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP !$#note ribosomal proteins Sa and S2 are substrates CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphotransferase; serine/threonine-specific protein !1kinase FEATURE !$14-300 #domain protein kinase homology #label KIN\ !$22-30 #region protein kinase ATP-binding motif\ !$41 #active_site Lys #status predicted SUMMARY #length 300 #molecular-weight 34301 #checksum 5260 SEQUENCE /// ENTRY A36855 #type complete TITLE protein kinase (EC 2.7.1.37) B1R - variola virus (strain India-1967) ALTERNATE_NAMES B1R protein ORGANISM #formal_name variola virus DATE 30-Sep-1993 #sequence_revision 21-Jan-1997 #text_change 23-Mar-2001 ACCESSIONS A36855 REFERENCE A36859 !$#authors Blinov, V.M. !$#submission submitted to GenBank, November 1992 !$#accession A36855 !'##molecule_type DNA !'##residues 1-300 ##label BLI !'##cross-references GB:X69198; NID:g456758; PIDN:CAA49110.1; !1PID:g457060 GENETICS !$#gene B1R FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP !$#note essential for viral replication; expressed early during !1infection !$#note ribosomal proteins Sa and S2 are substrates CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphotransferase; serine/threonine-specific protein !1kinase FEATURE !$14-300 #domain protein kinase homology #label KIN\ !$22-30 #region protein kinase ATP-binding motif\ !$41 #active_site Lys #status predicted SUMMARY #length 300 #molecular-weight 34259 #checksum 6279 SEQUENCE /// ENTRY TVVZBW #type complete TITLE kinase-related transforming protein (EC 2.7.1.-) B12R - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jun-2000 ACCESSIONS A33610; JQ1806 REFERENCE A33610 !$#authors Howard, S.T.; Smith, G.L. !$#journal J. Gen. Virol. (1989) 70:3187-3201 !$#title Two early vaccinia virus genes encode polypeptides related !1to protein kinases. !$#cross-references MUID:90111697; PMID:2607336 !$#accession A33610 !'##molecule_type DNA !'##residues 1-283 ##label HOW !'##cross-references EMBL:D00629; NID:g222692; PIDN:BAA00520.1; !1PID:g222693 REFERENCE JQ1767 !$#authors Smith, G.L.; Chan, Y.S.; Howard, S.T. !$#journal J. Gen. Virol. (1991) 72:1349-1376 !$#title Nucleotide sequence of 42kbp of vaccinia virus strain WR !1from near the right inverted terminal repeat. !$#cross-references MUID:91259063; PMID:2045793 !$#accession JQ1806 !'##molecule_type DNA !'##residues 1-283 ##label SMI !'##cross-references DDBJ:D11079; NID:g222717; PIDN:BAA01842.1; !1PID:g222757 CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphotransferase; serine/threonine-specific protein !1kinase; transforming protein FEATURE !$14-283 #domain protein kinase homology #label KIN\ !$17-25 #region protein kinase ATP-binding motif\ !$45 #active_site Lys #status predicted SUMMARY #length 283 #molecular-weight 33310 #checksum 6521 SEQUENCE /// ENTRY TVVZB2 #type complete TITLE kinase-related transforming protein (EC 2.7.1.-) B12R - vaccinia virus (strain Copenhagen) ORGANISM #formal_name vaccinia virus #note host Homo sapiens (man) DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 11-Jun-1999 ACCESSIONS B42527 REFERENCE A42501 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:517-563 !$#title Appendix to "The complete DNA sequence of vaccinia virus". !$#accession B42527 !'##molecule_type DNA !'##residues 1-283 ##label GOE !'##cross-references GB:M35027; NID:g335317; PIDN:AAA48209.1; !1PID:g335557 !'##experimental_source strain Copenhagen REFERENCE A42531 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:247-266 !$#title The complete DNA sequence of vaccinia virus. !$#cross-references MUID:91021027; PMID:2219722 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphotransferase; serine/threonine-specific protein !1kinase; transforming protein FEATURE !$14-283 #domain protein kinase homology #label KIN\ !$17-25 #region protein kinase ATP-binding motif\ !$45 #active_site Lys #status predicted SUMMARY #length 283 #molecular-weight 33366 #checksum 6890 SEQUENCE /// ENTRY TVFVUR #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) ros - avian sarcoma virus UR2 ORGANISM #formal_name avian sarcoma virus UR2 #note host Gallus gallus (chicken) DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 23-Feb-1997 ACCESSIONS A00635 REFERENCE A00635 !$#authors Neckameyer, W.S.; Wang, L.H. !$#journal J. Virol. (1985) 53:879-884 !$#title Nucleotide sequence of avian sarcoma virus UR2 and !1comparison of its transforming gene with other members of !1the tyrosine protein kinase oncogene family. !$#cross-references MUID:85135034; PMID:2983097 !$#accession A00635 !'##molecule_type genomic RNA !'##residues 1-402 ##label NEC COMMENT This protein is synthesized as a gag-ros polyprotein. GENETICS !$#gene ros CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; autophosphorylation; oncogene; phosphoprotein; !1phosphotransferase; transforming protein; tyrosine-specific !1protein kinase FEATURE !$96-376 #domain protein kinase homology #label KIN\ !$104-112 #region protein kinase ATP-binding motif\ !$133 #active_site Lys #status predicted SUMMARY #length 402 #molecular-weight 45073 #checksum 9994 SEQUENCE /// ENTRY B43362 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) ryk - avian retrovirus RPL30 ORGANISM #formal_name avian retrovirus RPL30 DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 23-Feb-1997 ACCESSIONS B43362 REFERENCE A43362 !$#authors Jia, R.; Mayer, B.J.; Hanafusa, T.; Hanafusa, H. !$#journal J. Virol. (1992) 66:5975-5987 !$#title A novel oncogene, v-ryk, encoding a truncated receptor !1tyrosine kinase is transduced into the RPL30 virus without !1loss of viral sequences. !$#cross-references MUID:92407992; PMID:1527848 !$#accession B43362 !'##molecule_type genomic RNA !'##residues 1-442 ##label JIA !'##cross-references GB:M92847 !'##note this protein is synthesized as a env-ryk polyprotein GENETICS !$#gene ryk CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; autophosphorylation; oncogene; phosphoprotein; !1phosphotransferase; transforming protein; tyrosine-specific !1protein kinase FEATURE !$43-319 #domain protein kinase homology #label KIN\ !$51-59 #region protein kinase ATP-binding motif\ !$77 #active_site Lys #status predicted SUMMARY #length 442 #molecular-weight 49108 #checksum 8368 SEQUENCE /// ENTRY A48082 #type complete TITLE MAP kinase 3 (EC 2.7.1.-) - human ALTERNATE_NAMES extracellular signal-regulated kinase 1 (ERK1); mitogen-activated protein kinase 3 (MAPK3); p44; protein kinase ERK1 CONTAINS protein kinase (EC 2.7.1.37) ORGANISM #formal_name Homo sapiens #common_name man DATE 04-Sep-1998 #sequence_revision 04-Sep-1998 #text_change 16-Jun-2000 ACCESSIONS A48082; PQ0270; S23428; S15519; S21579 REFERENCE A48082 !$#authors Charest, D.L.; Mordret, G.; Harder, K.W.; Jirik, F.; Pelech, !1S.L. !$#journal Mol. Cell. Biol. (1993) 13:4679-4690 !$#title Molecular cloning, expression, and characterization of the !1human mitogen-activated protein kinase p44(erk1). !$#cross-references MUID:93330262; PMID:7687743 !$#accession A48082 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-379 ##label CHA !'##cross-references EMBL:X60188; NID:g31220; PIDN:CAA42744.1; !1PID:g31221 !'##experimental_source hepatoma cell line HEP G2 !'##note authors translated the codon AGC for residue 174 as Ile REFERENCE JQ1400 !$#authors Owaki, H.; Makar, R.; Boulton, T.G.; Cobb, M.H.; Geppert, !1T.D. !$#journal Biochem. Biophys. Res. Commun. (1992) 182:1416-1422 !$#title Extracellular signal-regulated kinases in T cells: !1characterization of human ERK1 and ERK2 cDNAs. !$#cross-references MUID:92171961; PMID:1540184 !$#accession PQ0270 !'##molecule_type mRNA !'##residues 14-173,'I',175-379 ##label OWA !'##cross-references GB:M84490; NID:g186695; PIDN:AAA36142.1; !1PID:g186696 !'##experimental_source cell line CEM REFERENCE S23426 !$#authors Gonzalez, F.A.; Raden, D.L.; Rigby, M.R.; Davis, R.J. !$#journal FEBS Lett. (1992) 304:170-178 !$#title Heterogeneous expression of four MAP kinase isoforms in !1human tissues. !$#cross-references MUID:92316223; PMID:1319925 !$#accession S23428 !'##molecule_type mRNA !'##residues 25-173,'I',175-379 ##label GON !'##cross-references EMBL:Z11696; NID:g23882; PIDN:CAA77754.1; !1PID:g1335009 COMMENT This enzyme is activated by MAP kinase kinase (see PIR:45100 !1and PIR:A46723). It in turn is responsible for !1phosphorylating a number of regulatory proteins. See also !1PIR:JQ1400. GENETICS !$#gene GDB:PRKM3; ERK1 !'##cross-references GDB:135679; OMIM:601795 !$#map_position 16pter-16qter COMPLEX monomer FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP !$#pathway MAP kinase cascade CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; monomer; phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase; signal transduction FEATURE !$40-330 #domain protein kinase homology #label KIN\ !$48-56 #region protein kinase ATP-binding motif\ !$202 #binding_site phosphate (Thr) (covalent) (by MAP !8kinase kinase) #status predicted\ !$204 #binding_site phosphate (Tyr) (covalent) (by MAP !8kinase kinase) #status predicted SUMMARY #length 379 #molecular-weight 43109 #checksum 1952 SEQUENCE /// ENTRY JQ1400 #type complete TITLE MAP kinase 1 (EC 2.7.1.-) - human ALTERNATE_NAMES ERK; extracellular signal-regulated kinase 2 (ERK2); mitogen-activated protein kinase 1 (MAPK1); p40; p41; protein kinase ERK2 CONTAINS protein kinase (EC 2.7.1.37) ORGANISM #formal_name Homo sapiens #common_name man DATE 04-Sep-1998 #sequence_revision 04-Sep-1998 #text_change 11-Jun-1999 ACCESSIONS JQ1400; S23426; S23427; S21577; S21578 REFERENCE JQ1400 !$#authors Owaki, H.; Makar, R.; Boulton, T.G.; Cobb, M.H.; Geppert, !1T.D. !$#journal Biochem. Biophys. Res. Commun. (1992) 182:1416-1422 !$#title Extracellular signal-regulated kinases in T cells: !1characterization of human ERK1 and ERK2 cDNAs. !$#cross-references MUID:92171961; PMID:1540184 !$#accession JQ1400 !'##molecule_type mRNA !'##residues 1-360 ##label OWA !'##cross-references GB:M84489; NID:g182190; PIDN:AAA58459.1; !1PID:g182191 !'##experimental_source cell line Jurkat REFERENCE S23426 !$#authors Gonzalez, F.A.; Raden, D.L.; Rigby, M.R.; Davis, R.J. !$#journal FEBS Lett. (1992) 304:170-178 !$#title Heterogeneous expression of four MAP kinase isoforms in !1human tissues. !$#cross-references MUID:92316223; PMID:1319925 !$#accession S23426 !'##molecule_type mRNA !'##residues 13-360 ##label GON1 !'##cross-references EMBL:Z11695; NID:g23878; PIDN:CAA77753.1; !1PID:g23879 !$#accession S23427 !'##molecule_type mRNA !'##residues 1-90,'Q',92-360 ##label GON2 !'##cross-references EMBL:Z11694; NID:g23880; PIDN:CAA77752.1; !1PID:g23881 COMMENT This enzyme is activated by MAP kinase kinase (see PIR:45100 !1and PIR:A46723). It in turn is responsible for !1phosphorylating a number of regulatory proteins. See also !1PIR:A48082. GENETICS !$#gene GDB:PRKM1; ERK; MAPK1; ERK2 !'##cross-references GDB:135677; OMIM:176948 !$#map_position 22q11.2-22q11.2 COMPLEX monomer FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP !$#pathway MAP kinase cascade CLASSIFICATION #superfamily kinase-related transforming protein; protein !1kinase homology KEYWORDS ATP; phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase; signal transduction FEATURE !$23-313 #domain protein kinase homology #label KIN\ !$31-39 #region protein kinase ATP-binding motif\ !$185 #binding_site phosphate (Thr) (covalent) (by MAP !8kinase kinase) #status predicted\ !$187 #binding_site phosphate (Tyr) (covalent) (by MAP !8kinase kinase) #status predicted SUMMARY #length 360 #molecular-weight 41389 #checksum 6760 SEQUENCE /// ENTRY S71887 #type complete TITLE serine/threonine-specific kinase (EC 2.7.1.-), pk9.7 gastrula-specific - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S71887 REFERENCE S71887 !$#authors Snape, A.M.; Smith, J.C. !$#journal EMBO J. (1996) 15:4556-4565 !$#title Regulation of embryonic cell division by a Xenopus !1gastrula-specific protein kinase. !$#cross-references MUID:97042347; PMID:8887547 !$#accession S71887 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-358 ##label SNA !'##cross-references EMBL:X99406; NID:g1480369; PIDN:CAA67783.1; !1PID:g1480370 GENETICS !$#gene pk9.7 FUNCTION !$#description involved in regulation of cell division CLASSIFICATION #superfamily African clawed frog serine/threonine-specific !1kinase, gastrula-specific; protein kinase homology KEYWORDS phosphotransferase FEATURE !$9-274 #domain protein kinase homology #label KIN SUMMARY #length 358 #molecular-weight 40857 #checksum 9194 SEQUENCE /// ENTRY A57247 #type complete TITLE threonine/tyrosine-specific protein kinase (EC 2.7.1.-) Myt1 - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A57247 REFERENCE A57247 !$#authors Mueller, P.R.; Coleman, T.R.; Kumagai, A.; Dunphy, W.G. !$#journal Science (1995) 270:86-90 !$#title Myt1: a membrane-associated inhibitory kinase that !1phosphorylates Cdc2 on both threonine-14 and tyrosine-15. !$#cross-references MUID:96008579; PMID:7569953 !$#accession A57247 !'##status preliminary !'##molecule_type mRNA !'##residues 1-548 ##label MUE !'##cross-references GB:U28931; NID:g1019112; PIDN:AAC59716.1; !1PID:g1019113 CLASSIFICATION #superfamily African clawed frog threonine/tyrosine-specific !1protein kinase Myt1; protein kinase homology KEYWORDS cell cycle control; phosphotransferase; transmembrane !1protein FEATURE !$101-353 #domain protein kinase homology #label KIN SUMMARY #length 548 #molecular-weight 61785 #checksum 8689 SEQUENCE /// ENTRY G71532 #type complete TITLE probable threonine/tyrosine-specific protein kinase (EC 2.7.1.-) - Chlamydia trachomatis (serotype D, strain UW3/Cx) ORGANISM #formal_name Chlamydia trachomatis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS G71532 REFERENCE A71570 !$#authors Stephens, R.S.; Kalman, S.; Lammel, C.J.; Fan, J.; Marathe, !1R.; Aravind, L.; Mitchell, W.P.; Olinger, L.; Tatusov, R.L.; !1Zhao, Q.; Koonin, E.V.; Davis, R.W. !$#journal Science (1998) 282:754-759 !$#title Genome sequence of an obligate intracellular pathogen of !1humans: Chlamydia trachomatis. !$#cross-references MUID:99000809; PMID:9784136 !$#accession G71532 !'##status preliminary !'##molecule_type DNA !'##residues 1-934 ##label ARN !'##cross-references GB:AE001302; GB:AE001273; NID:g3328708; !1PIDN:AAC67894.1; PID:g3328716 !'##experimental_source serotype D, strain UW-3/Cx GENETICS !$#gene pknD CLASSIFICATION #superfamily Chlamydia trachomatis probable threonine/ !1tyrosine-specific protein kinase; protein kinase homology KEYWORDS phosphotransferase FEATURE !$2-293 #domain protein kinase homology #label KIN SUMMARY #length 934 #molecular-weight 107665 #checksum 4900 SEQUENCE /// ENTRY B70747 #type complete TITLE probable serine/threonine-specific protein kinase (EC 2.7.1.-) 3 - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS B70747 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession B70747 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-585 ##label COL !'##cross-references GB:Z74697; GB:AL123456; NID:g3261602; !1PIDN:CAA98986.1; PID:g3261603 !'##experimental_source strain H37Rv GENETICS !$#gene pknI CLASSIFICATION #superfamily Mycobacterium tuberculosis probable serine/ !1threonine-specific protein kinase 3; protein kinase homology KEYWORDS phosphotransferase FEATURE !$11-252 #domain protein kinase homology #label KIN SUMMARY #length 585 #molecular-weight 61804 #checksum 832 SEQUENCE /// ENTRY C70986 #type complete TITLE probable serine/threonine protein kinase (EC 2.7.1.-) - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS C70986 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession C70986 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-476 ##label COL !'##cross-references GB:Z95890; GB:AL123456; NID:g3242245; !1PIDN:CAB09332.1; PID:g2131011 !'##experimental_source strain H37Rv GENETICS !$#gene pknF CLASSIFICATION #superfamily Mycobacterium tuberculosis probable serine/ !1threonine protein kinase; protein kinase homology KEYWORDS phosphotransferase FEATURE !$11-279 #domain protein kinase homology #label KIN SUMMARY #length 476 #molecular-weight 50668 #checksum 5866 SEQUENCE /// ENTRY B70936 #type complete TITLE probable serine/threonine-specific protein kinase (EC 2.7.1.-) 2 - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS B70936 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession B70936 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-399 ##label COL !'##cross-references GB:AL021957; GB:AL123456; NID:g3242293; !1PIDN:CAA17480.1; PID:g2911096 !'##experimental_source strain H37Rv GENETICS !$#gene pknL CLASSIFICATION #superfamily Mycobacterium tuberculosis probable serine/ !1threonine-specific protein kinase 2; protein kinase homology KEYWORDS phosphotransferase FEATURE !$17-270 #domain protein kinase homology #label KIN SUMMARY #length 399 #molecular-weight 42833 #checksum 6006 SEQUENCE /// ENTRY S70965 #type complete TITLE serine/threonine-specific protein kinase (EC 2.7.1.-) pkn6 - Myxococcus xanthus ALTERNATE_NAMES serine/threonine protein kinase homolog ORGANISM #formal_name Myxococcus xanthus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S70965 REFERENCE S70964 !$#authors Zhang, W.; Inouye, M.; Inouye, S. !$#journal Mol. Microbiol. (1996) 20:435-447 !$#title Reciprocal regulation of the differentiation of Myxococcus !1xanthus by Pkn5 and Pkn6, eukaryotic-like Ser/Thr protein !1kinases. !$#cross-references MUID:96310380; PMID:8733241 !$#accession S70965 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-710 ##label ZHA !'##cross-references EMBL:U40656; NID:g1113924; PIDN:AAB40050.1; !1PID:g1113926 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1995 GENETICS !$#gene pkn6 CLASSIFICATION #superfamily Myxococcus xanthus serine/threonine-specific !1protein kinase pkn6; protein kinase homology KEYWORDS phosphotransferase FEATURE !$5-277 #domain protein kinase homology #label KIN SUMMARY #length 710 #molecular-weight 74621 #checksum 8075 SEQUENCE /// ENTRY A70652 #type complete TITLE probable serine/threonine-specific protein kinase (EC 2.7.1.-) 1 - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A70652 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession A70652 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-1110 ##label COL !'##cross-references GB:Z83866; GB:AL123456; NID:g3261691; !1PIDN:CAB06268.1; PID:g3261694 !'##experimental_source strain H37Rv GENETICS !$#gene pknK CLASSIFICATION #superfamily Mycobacterium tuberculosis probable serine/ !1threonine-specific protein kinase 1; protein kinase homology KEYWORDS phosphotransferase FEATURE !$25-284 #domain protein kinase homology #label KIN SUMMARY #length 1110 #molecular-weight 119417 #checksum 8043 SEQUENCE /// ENTRY A46373 #type complete TITLE probable serine/threonine-specific protein kinase (EC 2.7.1.-) PRO25 - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 10-Sep-1999 #sequence_revision 19-Jul-2002 #text_change 19-Jul-2002 ACCESSIONS H86345; A46373 REFERENCE A86141 !$#authors Theologis, A.; Ecker, J.R.; Palm, C.J.; Federspiel, N.A.; !1Kaul, S.; White, O.; Alonso, J.; Altaf, H.; Araujo, R.; !1Bowman, C.L.; Brooks, S.Y.; Buehler, E.; Chan, A.; Chao, Q.; !1Chen, H.; Cheuk, R.F.; Chin, C.W.; Chung, M.K.; Conn, L.; !1Conway, A.B.; Conway, A.R.; Creasy, T.H.; Dewar, K.; Dunn, !1P.; Etgu, P.; Feldblyum, T.V.; Feng, J.; Fong, B.; Fujii, !1C.Y.; Gill, J.E.; Goldsmith, A.D.; Haas, B.; Hansen, N.F.; !1Hughes, B.; Huizar, L.; Hunter, J.L.; Jenkins, J.; !1Johnson-Hopson, C.; Khan, S.; Khaykin, E.; Kim, C.J.; Koo, !1H.L.; Kremenetskaia, I.; Kurtz, D.B.; Kwan, A.; Lam, B.; !1Langin-Hooper, S.; Lee, A.; Lee, J.M.; Lenz, C.A.; Li, J.H.; !1Li, Y.; Lin, X.; Liu, S.X.; Liu, Z.A.; Luros, J.S.; Maiti, !1R.; Marziali, A.; Militscher, J.; Miranda, M.; Nguyen, M.; !1Nierman, W.C.; Osborne, B.I.; Pai, G.; Peterson, J.; Pham, !1P.K.; Rizzo, M.; Rooney, T.; Rowley, D.; Sakano, H.; !1Salzberg, S.L.; Schwartz, J.R.; Shinn, P.; Southwick, A.M.; !1Sun, H.; Tallon, L.J.; Tambunga, G.; Toriumi, M.J.; Town, !1C.D.; Utterback, T.; van Aken, S.; Vaysberg, M.; Vysotskaia, !1V.S.; Walker, M.; Wu, D.; Yu, G.; Fraser, C.M.; Venter, !1J.C.; Davis, R.W. !$#journal Nature (2000) 408:816-820 !$#title Sequence and analysis of chromosome 1 of the plant !1Arabidopsis. !$#cross-references MUID:21016719; PMID:11130712 !$#accession H86345 !'##status preliminary !'##molecule_type DNA !'##residues 1-733 ##label STO !'##cross-references GB:AE005172; NID:g8920634; PIDN:AAF81356.1; !1GSPDB:GN00141 REFERENCE A46373 !$#authors Kohorn, B.D.; Lane, S.; Smith, T.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:10989-10992 !$#title An Arabidopsis serine/threonine kinase homologue with an !1epidermal growth factor repeat selected in yeast for its !1specificity for a thylakoid membrane protein. !$#cross-references MUID:93066369; PMID:1438303 !$#accession A46373 !'##status preliminary !'##molecule_type mRNA !'##residues 138-211,'C',213-243,'I',245-279,'CQD',281-384,387-455,'P', !1457-660,'T','N',664,'RG',667-733 ##label KOH !'##cross-references GB:L04999; NID:g166812; PIDN:AAA32844.1; !1PID:g166813 !'##note sequence extracted from NCBI backbone (NCBIN:118788, !1NCBIP:118790) GENETICS !$#map_position 1 CLASSIFICATION #superfamily Arabidopsis probable serine/threonine-specific !1protein kinase PRO25; protein kinase homology KEYWORDS phosphotransferase FEATURE !$405-684 #domain protein kinase homology #label KIN SUMMARY #length 733 #molecular-weight 81027 #checksum 1126 SEQUENCE /// ENTRY G71612 #type complete TITLE novel serine/threonine-specific protein kinase (EC 2.7.1.-) PFB0520w - malaria parasite (Plasmodium falciparum) ORGANISM #formal_name Plasmodium falciparum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS G71612 REFERENCE A71600 !$#authors Gardner, M.J.; Tettelin, H.; Carucci, D.J.; Cummings, L.M.; !1Aravind, L.; Koonin, E.V.; Shallom, S.; Mason, T.; Yu, K.; !1Fujii, C.; Pederson, J.; Shen, K.; Jing, J.; Aston, C.; Lai, !1Z.; Schwartz, D.C.; Pertea, M.; Salzberg, S.; Zhou, L.; !1Sutton, G.G.; Clayton, R.; White, O.; Smith, H.O.; Fraser, !1C.M.; Adams, M.D.; Venter, J.C.; Hoffman, S.L. !$#journal Science (1998) 282:1126-1132 !$#title Chromosome 2 sequence of the human malaria parasite !1Plasmodium falciparum. !$#cross-references MUID:99021743; PMID:9804551 !$#accession G71612 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-1233 ##label GAR !'##cross-references GB:AE001400; GB:AE001362; NID:g3845204; !1PIDN:AAC71893.1; PID:g3845206; TIGR:PFB0520w !'##experimental_source clone 3D7 GENETICS !$#gene PFB0520w CLASSIFICATION #superfamily malaria parasite serine/threonine-specific !1protein kinase PFB0520w; protein kinase homology KEYWORDS phosphotransferase FEATURE !$949-1221 #domain protein kinase homology #label KIN SUMMARY #length 1233 #molecular-weight 148226 #checksum 9579 SEQUENCE /// ENTRY H71621 #type complete TITLE serine/threonine-specific protein kinase (EC 2.7.1.-) PFB0150c - malaria parasite (Plasmodium falciparum) ORGANISM #formal_name Plasmodium falciparum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS H71621 REFERENCE A71600 !$#authors Gardner, M.J.; Tettelin, H.; Carucci, D.J.; Cummings, L.M.; !1Aravind, L.; Koonin, E.V.; Shallom, S.; Mason, T.; Yu, K.; !1Fujii, C.; Pederson, J.; Shen, K.; Jing, J.; Aston, C.; Lai, !1Z.; Schwartz, D.C.; Pertea, M.; Salzberg, S.; Zhou, L.; !1Sutton, G.G.; Clayton, R.; White, O.; Smith, H.O.; Fraser, !1C.M.; Adams, M.D.; Venter, J.C.; Hoffman, S.L. !$#journal Science (1998) 282:1126-1132 !$#title Chromosome 2 sequence of the human malaria parasite !1Plasmodium falciparum. !$#cross-references MUID:99021743; PMID:9804551 !$#accession H71621 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-2485 ##label GAR !'##cross-references GB:AE001376; GB:AE001362; NID:g3845108; !1PIDN:AAC71820.1; PID:g3845109; TIGR:PFB0150c !'##experimental_source clone 3D7 GENETICS !$#gene PFB0150c CLASSIFICATION #superfamily malaria parasite serine/threonine-specific !1protein kinase PFB0150c; protein kinase homology KEYWORDS phosphotransferase FEATURE !$2087-2352 #domain protein kinase homology #label KIN SUMMARY #length 2485 #molecular-weight 293766 #checksum 4248 SEQUENCE /// ENTRY I78885 #type complete TITLE serine/threonine-specific protein kinase (EC 2.7.1.-) STK2 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 29-Sep-1999 ACCESSIONS I78885 REFERENCE I58396 !$#authors Levedakou, E.N.; He, M.; Baptist, E.W.; Craven, R.J.; Cance, !1W.G.; Welcsh, P.L.; Simmons, A.; Naylor, S.L.; Leach, R.J.; !1Lewis, T.B.; Liu, E.T. !$#journal Oncogene (1994) 9:1977-1988 !$#title Two novel human serine/threonine kinases with homologies to !1the cell cycle regulating Xenopus MO15, and NIMA kinases: !1cloning and characterization of their expression pattern. !$#cross-references MUID:94268838; PMID:8208544 !$#accession I78885 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-841 ##label RES !'##cross-references GB:L20321; NID:g348244; PIDN:AAA36658.1; !1PID:g348245 GENETICS !$#gene GDB:STK2 !'##cross-references GDB:374125 !$#map_position 3p21.1-3p21.1 CLASSIFICATION #superfamily human serine/threonine-specific protein kinase !1STK2; protein kinase homology KEYWORDS phosphotransferase FEATURE !$4-261 #domain protein kinase homology #label KIN SUMMARY #length 841 #molecular-weight 94570 #checksum 2187 SEQUENCE /// ENTRY H70351 #type complete TITLE probable serine/threonine-specific protein kinase (EC 2.7.1.-) stpK - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS H70351 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession H70351 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-271 ##label AQF !'##cross-references GB:AE000696; NID:g2983196; PIDN:AAC06804.1; !1PID:g2983205; GB:AE000657 !'##experimental_source strain VF5 GENETICS !$#gene stpK CLASSIFICATION #superfamily Aquifex aeolicus serine/threonine-specific !1protein kinase; protein kinase homology KEYWORDS phosphotransferase FEATURE !$12-266 #domain protein kinase homology #label KIN SUMMARY #length 271 #molecular-weight 31532 #checksum 7192 SEQUENCE /// ENTRY JW0051 #type complete TITLE serine/threonine-specific protein kinase (EC 2.7.1.-) ULK1 - mouse ALTERNATE_NAMES protein kinase UNC-51-like ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JW0051 REFERENCE JW0051 !$#authors Yan, J.; Kuroyanagi, H.; Kuroiwa, A.; Matsuda, Y.; !1Tokumitsu, H.; Tomoda, T.; Shirasawa, T.; Muramatsu, M. !$#journal Biochem. Biophys. Res. Commun. (1998) 246:222-227 !$#title Identification of mouse ULK1, a novel protein kinase !1structurally related to C. elegans UNC-51. !$#cross-references MUID:98262945; PMID:9600096 !$#accession JW0051 !'##molecule_type mRNA !'##residues 1-1051 ##label YAN !'##cross-references GB:AF053756; NID:g3136153; PIDN:AAC40118.1; !1PID:g3136154 GENETICS !$#map_position 12q16.3 CLASSIFICATION #superfamily mouse protein kinase ULK1; protein kinase !1homology KEYWORDS phosphotransferase FEATURE !$14-278 #domain protein kinase homology #label KIN SUMMARY #length 1051 #molecular-weight 112462 #checksum 7291 SEQUENCE /// ENTRY I49101 #type complete TITLE conserved helix-loop-helix ubiquitous kinase (EC 2.7.1.-) CHUK - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS I49101 REFERENCE I49101 !$#authors Mock, B.A.; Connelly, M.A.; McBride, O.W.; Kozak, C.A.; !1Marcu, K.B. !$#journal Genomics (1995) 27:348-351 !$#title CHUK, a conserved helix-loop-helix ubiquitous kinase, maps !1to human chromosome 10 and mouse chromosome 19. !$#cross-references MUID:96044444; PMID:7558004 !$#accession I49101 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-745 ##label RES !'##cross-references EMBL:U12473; NID:g1079492; PIDN:AAC52589.1; !1PID:g1079493 GENETICS !$#gene CHUK CLASSIFICATION #superfamily mouse conserved helix-loop-helix ubiquitous !1kinase; protein kinase homology KEYWORDS ATP; phosphotransferase FEATURE !$13-283 #domain protein kinase homology #label KIN SUMMARY #length 745 #molecular-weight 84728 #checksum 1197 SEQUENCE /// ENTRY JQ1150 #type complete TITLE protein kinase (EC 2.7.1.37) cAMP-dependent, catalytic chain - slime mold (Dictyostelium discoideum) ORGANISM #formal_name Dictyostelium discoideum DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 24-Apr-1998 ACCESSIONS JQ1150 REFERENCE JQ1150 !$#authors Buerki, E.; Anjard, C.; Scholder, J.C.; Reymond, C.D. !$#journal Gene (1991) 102:57-65 !$#title Isolation of two genes encoding putative protein kinases !1regulated during Dictyostelium discoideum development. !$#cross-references MUID:91323730; PMID:1864510 !$#accession JQ1150 !'##molecule_type DNA !'##residues 1-648 ##label BUE !'##cross-references GB:M38703 GENETICS !$#gene PK2 !$#introns 578/3 COMPLEX heterodimer with regulatory chain; active catalytic chain is !1released when cAMP binds to the regulatory chain FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP !$#note important for cell type differentiation and fruiting body !1morphogenesis CLASSIFICATION #superfamily Dictyostelium cAMP-dependent protein kinase !1catalytic chain; protein kinase homology KEYWORDS ATP; magnesium; phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$126-223 #region glutamine-rich\ !$297-312 #region glutamine-rich\ !$334-590 #domain protein kinase homology #label KIN\ !$342-350 #region protein kinase ATP-binding motif\ !$365,384,459,461 #active_site Lys, Glu, Asp, Lys #status predicted\ !$464,468 #binding_site magnesium (Asn, Asp) #status predicted SUMMARY #length 648 #molecular-weight 74458 #checksum 2120 SEQUENCE /// ENTRY TVFVMI #type complete TITLE gag-Rmil-env polyprotein - avian retrovirus IC10 CONTAINS env polyprotein; gag polyprotein; protein kinase (EC 2.7.1.37) Rmil ORGANISM #formal_name avian retrovirus IC10 #note host Gallus gallus (chicken) DATE 31-Mar-1991 #sequence_revision 16-Aug-1996 #text_change 11-Jun-1999 ACCESSIONS A43095; A36753; S01645; B36753; S03832 REFERENCE A43095 !$#authors Dezelee, P. !$#submission submitted to GenBank, December 1988 !$#accession A43095 !'##molecule_type DNA !'##residues 1-1079 ##label DEZ !'##cross-references GB:X13744; NID:g61592; PIDN:CAA32008.1; PID:g61593 REFERENCE S01645 !$#authors Marx, M.; Eychene, A.; Laugier, D.; Bechade, C.; Crisanti, !1P.; Dezelee, P.; Pessac, B.; Calothy, G. !$#journal EMBO J. (1988) 7:3369-3373 !$#title A novel oncogene related to c-mil is transduced in chicken !1neuroretina cells induced to proliferate by infection with !1an avian lymphomatosis virus. !$#cross-references MUID:89091077; PMID:2850163 !$#accession A36753 !'##molecule_type DNA !'##residues 513-645 ##label MAR !$#accession S01645 !'##molecule_type DNA !'##residues 646-1012 ##label MA2 !$#accession B36753 !'##molecule_type DNA !'##residues 1013-1079 ##label MA3 REFERENCE S03832 !$#authors Eychene, A.; Marx, M.; Dezelee, P.; Calothy, G. !$#journal Nucleic Acids Res. (1989) 17:1250 !$#title Complete nucleotide sequence of IC10, a retrovirus !1containing the Rmil oncogene transduced in chicken !1neuroretina cells infected with avian retrovirus RAV-1. !$#cross-references MUID:89160254; PMID:2537952 !$#accession S03832 !'##status translation not shown !'##molecule_type DNA !'##residues 1-1079 ##label EYC !'##cross-references EMBL:X13744; NID:g61592; PIDN:CAA32008.1; !1PID:g61593 COMMENT This virus arose by recombination between host Rmil and !1viral sequences during passaging of Rous-associated virus !1type 1 in cultured chicken embryonic neuroretina cells. GENETICS !$#gene gag-Rmil-env CLASSIFICATION #superfamily avian retrovirus IC10 gag-Rmil-env polyprotein; !1protein kinase homology KEYWORDS ATP; coat protein; oncogene; phosphotransferase; !1polyprotein; serine/threonine-specific protein kinase; !1transforming protein FEATURE !$1-645 #region viral gag gene-derived\ !$646-1012 #region host Rmil gene-derived\ !$710-976 #domain protein kinase homology #label KIN\ !$718-726 #region protein kinase ATP-binding motif\ !$1013-1079 #region viral env gene-derived\ !$738 #active_site Lys #status predicted SUMMARY #length 1079 #molecular-weight 117079 #checksum 5871 SEQUENCE /// ENTRY A41365 #type complete TITLE rhodopsin kinase (EC 2.7.1.125) - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A41365 REFERENCE A41365 !$#authors Lorenz, W.; Inglese, J.; Palczewski, K.; Onorato, J.J.; !1Caron, M.G.; Lefkowitz, R.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:8715-8719 !$#title The receptor kinase family: primary structure of rhodopsin !1kinase reveals similarities to the beta-adrenergic receptor !1kinase. !$#cross-references MUID:92020922; PMID:1656454 !$#accession A41365 !'##status preliminary !'##molecule_type mRNA !'##residues 1-561 ##label LOR !'##cross-references GB:M73836; NID:g163658; PIDN:AAA30752.1; !1PID:g163659 CLASSIFICATION #superfamily rhodopsin kinase; protein kinase homology KEYWORDS ATP; autophosphorylation; lipoprotein; methylated carboxyl !1end; phosphoprotein; phosphotransferase; prenylated !1cysteine; serine/threonine-specific protein kinase FEATURE !$185-452 #domain protein kinase homology #label KIN\ !$193-201 #region protein kinase ATP-binding motif\ !$558 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted\ !$558 #binding_site farnesyl (Cys) (covalent) #status !8predicted SUMMARY #length 561 #molecular-weight 62933 #checksum 5806 SEQUENCE /// ENTRY A54372 #type complete TITLE G protein-coupled receptor kinase (EC 2.7.1.-) 5 - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A54372 REFERENCE A54372 !$#authors Premont, R.T.; Koch, W.J.; Inglese, J.; Lefkowitz, R.J. !$#journal J. Biol. Chem. (1994) 269:6832-6841 !$#title Identification, purification, and characterization of GRK5, !1a member of the family of G protein-coupled receptor !1kinases. !$#cross-references MUID:94165084; PMID:8120045 !$#accession A54372 !'##status preliminary !'##molecule_type mRNA !'##residues 1-590 ##label PRE !'##cross-references GB:U01206; NID:g437105; PIDN:AAA17561.1; !1PID:g437106 CLASSIFICATION #superfamily rhodopsin kinase; protein kinase homology KEYWORDS ATP; phosphotransferase; serine/threonine-specific protein !1kinase FEATURE !$184-448 #domain protein kinase homology #label KIN\ !$192-200 #region protein kinase ATP-binding motif SUMMARY #length 590 #molecular-weight 67888 #checksum 2720 SEQUENCE /// ENTRY B41615 #type complete TITLE G protein-coupled receptor kinase (EC 2.7.1.-) 2 - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B41615 REFERENCE A41615 !$#authors Cassill, J.A.; Whitney, M.; Joazeiro, C.A.P.; Becker, A.; !1Zuker, C.S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:11067-11070 !$#title Isolation of Drosophila genes encoding G protein-coupled !1receptor kinases. !$#cross-references MUID:92107891; PMID:1662381 !$#accession B41615 !'##status preliminary !'##molecule_type mRNA !'##residues 1-427 ##label CAS !'##cross-references GB:M80494; NID:g157555; PIDN:AAA28589.1; !1PID:g157556 GENETICS !$#gene FlyBase:Gprk2 !'##cross-references FlyBase:FBgn0004834 CLASSIFICATION #superfamily rhodopsin kinase; protein kinase homology KEYWORDS ATP; phosphotransferase; serine/threonine-specific protein !1kinase FEATURE !$20-287 #domain protein kinase homology #label KIN\ !$28-36 #region protein kinase ATP-binding motif SUMMARY #length 427 #molecular-weight 48971 #checksum 5999 SEQUENCE /// ENTRY A53791 #type complete TITLE beta-adrenergic-receptor kinase (EC 2.7.1.126) 1 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 25-Oct-1994 #sequence_revision 18-Nov-1994 #text_change 11-Jun-1999 ACCESSIONS A53791; A42433; S15781 REFERENCE A53791 !$#authors Penn, R.B.; Benovic, J.L. !$#journal J. Biol. Chem. (1994) 269:14924-14930 !$#title Structure of the human gene encoding the beta-adrenergic !1receptor kinase. !$#cross-references MUID:94253044; PMID:8195124 !$#accession A53791 !'##molecule_type DNA !'##residues 1-689 ##label PEN !'##experimental_source lymphocyte !'##note sequence extracted from NCBI backbone (NCBIN:147950, !1NCBIN:147952, NCBIN:147955, NCBIN:147958, NCBIN:147960, !1NCBIN:147962, NCBIN:147964, NCBIN:147966, NCBIN:147968, !1NCBIN:147970, NCBIN:147972, NCBIN:147974, NCBIP:147975) REFERENCE A42433 !$#authors Chuang, T.T.; Sallese, M.; Ambrosini, G.; Parruti, G.; De !1Blasi, A. !$#journal J. Biol. Chem. (1992) 267:6886-6892 !$#title High expression of beta-adrenergic receptor kinase in human !1peripheral blood leukocytes. Isoproterenol and platelet !1activating factor can induce kinase translocation. !$#cross-references MUID:92202245; PMID:1339451 !$#accession A42433 !'##molecule_type mRNA !'##residues 1-210,'A',212-421,'R',423-689 ##label CHU !'##cross-references GB:M80776; NID:g179334; PIDN:AAA58391.1; !1PID:g179335 !'##experimental_source peripheral blood leukocytes !'##note sequence extracted from NCBI backbone (NCBIN:91610, !1NCBIP:91612) REFERENCE S15781 !$#authors Benovic, J.L.; Stone, W.C.; Huebner, K.; Croce, C.; Caron, !1M.G.; Lefkowitz, R.J. !$#journal FEBS Lett. (1991) 283:122-126 !$#title cDNA cloning and chromosomal localization of the human !1beta-adrenergic receptor kinase. !$#cross-references MUID:91243858; PMID:2037065 !$#accession S15781 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-464,'R',466-689 ##label LEF !'##cross-references GB:X61157; NID:g288307; PIDN:CAA43470.1; !1PID:g288308 !'##experimental_source retina GENETICS !$#gene GDB:ADRBK1 !'##cross-references GDB:128604; OMIM:109635 !$#map_position 11q13-11q13 FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP !$#pathway desensitization of beta-adrenergic receptor !$#note phosphorylation inactivates the agonist-occupied receptor CLASSIFICATION #superfamily beta-adrenergic-receptor kinase; pleckstrin !1repeat homology; protein kinase homology KEYWORDS ATP; magnesium; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$189-453 #domain protein kinase homology #label KIN\ !$197-205 #region protein kinase ATP-binding motif\ !$557-650 #domain pleckstrin repeat homology #label PLK\ !$220,239,317,319 #active_site Lys, Glu, Asp, Lys #status predicted\ !$322,326 #binding_site magnesium (Asn, Asp) #status predicted SUMMARY #length 689 #molecular-weight 79639 #checksum 3170 SEQUENCE /// ENTRY A40088 #type complete TITLE beta-adrenergic-receptor kinase (EC 2.7.1.126) 1 - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 20-Mar-1992 #sequence_revision 20-Mar-1992 #text_change 11-Jun-1999 ACCESSIONS A40088 REFERENCE A40088 !$#authors Benovic, J.L.; DeBlasi, A.; Stone, W.C.; Caron, M.G.; !1Lefkowitz, R.J. !$#journal Science (1989) 246:235-246 !$#title Beta-adrenergic receptor kinase: primary structure !1delineates a multigene family. !$#cross-references MUID:90019526; PMID:2552582 !$#accession A40088 !'##molecule_type mRNA !'##residues 1-689 ##label BEN !'##cross-references GB:M34019; NID:g162683; PIDN:AAA30384.1; !1PID:g162684 !'##experimental_source brain FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP !$#pathway desensitization of beta-adrenergic receptor !$#note phosphorylation inactivates the agonist-occupied receptor CLASSIFICATION #superfamily beta-adrenergic-receptor kinase; pleckstrin !1repeat homology; protein kinase homology KEYWORDS ATP; magnesium; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$189-453 #domain protein kinase homology #label KIN\ !$197-205 #region protein kinase ATP-binding motif\ !$557-650 #domain pleckstrin repeat homology #label PLK\ !$220,239,317,319 #active_site Lys, Glu, Asp, Lys #status predicted\ !$322,326 #binding_site magnesium (Asn, Asp) #status predicted SUMMARY #length 689 #molecular-weight 79646 #checksum 2454 SEQUENCE /// ENTRY I56531 #type complete TITLE beta-adrenergic-receptor kinase (EC 2.7.1.126) 1 - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 26-Jul-1996 #sequence_revision 26-Jul-1996 #text_change 11-Jun-1999 ACCESSIONS I56531; I58185 REFERENCE I56531 !$#authors Arriza, J.L.; Dawson, T.M.; Simerly, R.B.; Martin, L.J.; !1Caron, M.G.; Snyder, S.H.; Lefkowitz, R.J. !$#journal J. Neurosci. (1992) 12:4045-4055 !$#title The G protein-receptor kinases beta-ARK1 and beta-ARK2 are !1widely distributed at synapses in rat brain. !$#cross-references MUID:93019546; PMID:1403099 !$#accession I56531 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-689 ##label RES !'##cross-references GB:M87854; NID:g203097; PIDN:AAA40802.1; !1PID:g203098 REFERENCE I58185 !$#authors Owada, Y.; Watanabe, M.; Kondo, H. !$#journal Neurosci. Lett. (1992) 144:9-13 !$#title Localization of mRNA for beta-adrenergic receptor kinase in !1the brain of adult rats. !$#cross-references MUID:93064196; PMID:1436718 !$#accession I58185 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-23,'RR',26-45,'N',47-71,'C',73-89,'K',91-248,'V',250-269, !1'S',271-295,'Y',297-446,'V',448-593,'G',595-689 ##label RE2 !'##cross-references GB:S48813; NID:g260171; PIDN:AAB24228.1; !1PID:g260172 !'##experimental_source rat brain (species and strain unspecified) GENETICS !$#gene beta-ARK1 FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP !$#pathway desensitization of beta-adrenergic receptor !$#note phosphorylation inactivates the agonist-occupied receptor CLASSIFICATION #superfamily beta-adrenergic-receptor kinase; pleckstrin !1repeat homology; protein kinase homology KEYWORDS ATP; magnesium; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$189-453 #domain protein kinase homology #label KIN\ !$197-205 #region protein kinase ATP-binding motif\ !$557-650 #domain pleckstrin repeat homology #label PLK\ !$220,239,317,319 #active_site Lys, Glu, Asp, Lys #status predicted\ !$322,326 #binding_site magnesium (Asn, Asp) #status predicted SUMMARY #length 689 #molecular-weight 79784 #checksum 2150 SEQUENCE /// ENTRY JC1469 #type complete TITLE beta-adrenergic-receptor kinase (EC 2.7.1.126) 2 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 11-Jun-1999 ACCESSIONS JC1469 REFERENCE JC1469 !$#authors Parruti, G.; Ambrosini, G.; Sallese, M.; De Blasi, A. !$#journal Biochem. Biophys. Res. Commun. (1993) 190:475-481 !$#title Molecular cloning, functional expression and mRNA analysis !1of human beta-adrenergic receptor kinase 2. !$#cross-references MUID:93151831; PMID:8427589 !$#accession JC1469 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-688 ##label PAR !'##cross-references GB:X69117; NID:g312394; PIDN:CAA48870.1; !1PID:g312395 !'##experimental_source pituitary COMMENT This enzyme plays a role in the regulation of !1receptor-mediated immune functions. GENETICS !$#gene GDB:ADRBK2 !'##cross-references GDB:131716; OMIM:109636 !$#map_position 22q11-22q11 FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP !$#pathway desensitization of beta-adrenergic receptor !$#note phosphorylation inactivates the agonist-occupied receptor CLASSIFICATION #superfamily beta-adrenergic-receptor kinase; pleckstrin !1repeat homology; protein kinase homology KEYWORDS ATP; magnesium; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$189-453 #domain protein kinase homology #label KIN\ !$197-205 #region protein kinase ATP-binding motif\ !$557-650 #domain pleckstrin repeat homology #label PLK\ !$220,239,317,319 #active_site Lys, Glu, Asp, Lys #status predicted\ !$322,326 #binding_site magnesium (Asn, Asp) #status predicted SUMMARY #length 688 #molecular-weight 79601 #checksum 6536 SEQUENCE /// ENTRY A39336 #type complete TITLE beta-adrenergic-receptor kinase (EC 2.7.1.126) 2 - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 03-Apr-1992 #sequence_revision 03-Apr-1992 #text_change 11-Jun-1999 ACCESSIONS A39336 REFERENCE A39336 !$#authors Benovic, J.L.; Onorato, J.J.; Arriza, J.L.; Stone, W.C.; !1Lohse, M.; Jenkins, N.A.; Gilbert, D.J.; Copeland, N.G.; !1Caron, M.G.; Lefkowitz, R.J. !$#journal J. Biol. Chem. (1991) 266:14939-14946 !$#title Cloning, expression, and chromosomal localization of !1beta-adrenergic receptor kinase 2. A new member of the !1receptor kinase family. !$#cross-references MUID:91332005; PMID:1869533 !$#accession A39336 !'##molecule_type mRNA !'##residues 1-688 ##label BEN !'##cross-references GB:M73216; NID:g162734; PIDN:AAA30406.1; !1PID:g162735 FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP !$#pathway desensitization of beta-adrenergic receptor !$#note phosphorylation inactivates the agonist-occupied receptor CLASSIFICATION #superfamily beta-adrenergic-receptor kinase; pleckstrin !1repeat homology; protein kinase homology KEYWORDS ATP; magnesium; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$189-453 #domain protein kinase homology #label KIN\ !$197-205 #region protein kinase ATP-binding motif\ !$557-650 #domain pleckstrin repeat homology #label PLK\ !$220,239,317,319 #active_site Lys, Glu, Asp, Lys #status predicted\ !$322,326 #binding_site magnesium (Asn, Asp) #status predicted SUMMARY #length 688 #molecular-weight 79803 #checksum 9052 SEQUENCE /// ENTRY I73628 #type complete TITLE beta-adrenergic-receptor kinase (EC 2.7.1.126) 2 - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 02-Aug-1996 #sequence_revision 02-Aug-1996 #text_change 11-Jun-1999 ACCESSIONS I73628 REFERENCE I56531 !$#authors Arriza, J.L.; Dawson, T.M.; Simerly, R.B.; Martin, L.J.; !1Caron, M.G.; Snyder, S.H.; Lefkowitz, R.J. !$#journal J. Neurosci. (1992) 12:4045-4055 !$#title The G protein-receptor kinases beta-ARK1 and beta-ARK2 are !1widely distributed at synapses in rat brain. !$#cross-references MUID:93019546; PMID:1403099 !$#accession I73628 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-688 ##label RES !'##cross-references GB:M87855; NID:g203099; PIDN:AAA40803.1; !1PID:g203100 GENETICS !$#gene beta-ARK2 FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP !$#pathway desensitization of beta-adrenergic receptor !$#note phosphorylation inactivates the agonist-occupied receptor CLASSIFICATION #superfamily beta-adrenergic-receptor kinase; pleckstrin !1repeat homology; protein kinase homology KEYWORDS ATP; magnesium; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$189-453 #domain protein kinase homology #label KIN\ !$197-205 #region protein kinase ATP-binding motif\ !$557-650 #domain pleckstrin repeat homology #label PLK\ !$220,239,317,319 #active_site Lys, Glu, Asp, Lys #status predicted\ !$322,326 #binding_site magnesium (Asn, Asp) #status predicted SUMMARY #length 688 #molecular-weight 79887 #checksum 6273 SEQUENCE /// ENTRY A41615 #type complete TITLE beta-adrenergic-receptor kinase (EC 2.7.1.126) 1 - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 28-Aug-1992 #sequence_revision 28-Aug-1992 #text_change 05-Dec-1997 ACCESSIONS A41615 REFERENCE A41615 !$#authors Cassill, J.A.; Whitney, M.; Joazeiro, C.A.P.; Becker, A.; !1Zuker, C.S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:11067-11070 !$#title Isolation of Drosophila genes encoding G protein-coupled !1receptor kinases. !$#cross-references MUID:92107891; PMID:1662381 !$#accession A41615 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-700 ##label CAS !'##cross-references GB:M80493 GENETICS !$#gene FlyBase:Gprk1 !'##cross-references FlyBase:FBgn0004833 FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP !$#pathway desensitization of beta-adrenergic receptor !$#note phosphorylation inactivates the agonist-occupied receptor CLASSIFICATION #superfamily beta-adrenergic-receptor kinase; pleckstrin !1repeat homology; protein kinase homology KEYWORDS ATP; magnesium; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$189-454 #domain protein kinase homology #label KIN\ !$197-205 #region protein kinase ATP-binding motif\ !$556-655 #domain pleckstrin repeat homology #label PLK\ !$220,239,318,320 #active_site Lys, Glu, Asp, Lys #status predicted\ !$323,327 #binding_site magnesium (Asn, Asp) #status predicted SUMMARY #length 700 #molecular-weight 80585 #checksum 1214 SEQUENCE /// ENTRY A54600 #type complete TITLE 1-phosphatidylinositol 3-kinase (EC 2.7.1.137) 110K chain beta isoform - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A54600 REFERENCE A54600 !$#authors Hu, P.; Mondino, A.; Skolnik, E.Y.; Schlessinger, J. !$#journal Mol. Cell. Biol. (1993) 13:7677-7688 !$#title Cloning of a novel, ubiquitously expressed human !1phosphatidylinositol 3-kinase and identification of its !1binding site on p85. !$#cross-references MUID:94067128; PMID:8246984 !$#accession A54600 !'##status preliminary !'##molecule_type mRNA !'##residues 1-1070 ##label HU1 !'##cross-references GB:S67334; NID:g455759; PIDN:AAB29081.1; !1PID:g455760 !'##note sequence extracted from NCBI backbone (NCBIN:140879, !1NCBIP:140880) GENETICS !$#gene GDB:PIK3CB; PIK3C1 !'##cross-references GDB:136233 CLASSIFICATION #superfamily phosphatidylinositol 3-kinase KEYWORDS phosphotransferase SUMMARY #length 1070 #molecular-weight 122761 #checksum 7198 SEQUENCE /// ENTRY A57134 #type complete TITLE 1-phosphatidylinositol 3-kinase (EC 2.7.1.137) gamma isoform - human ALTERNATE_NAMES p110-gamma protein ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A57134 REFERENCE A57134 !$#authors Stoyanov, B.; Volinia, S.; Hanck, T.; Rubio, I.; !1Loubtchenkov, M.; Malek, D.; Stoyanova, S.; Vanhaesebroeck, !1B.; Dhand, R.; Nuernberg, B.; Gierschik, P.; Seedorf, K.; !1Hsuan, J.J.; Waterfield, M.D.; Wetzker, R. !$#journal Science (1995) 269:690-693 !$#title Cloning and characterization of a G protein-activated human !1phosphoinositide-3 kinase. !$#cross-references MUID:95350661; PMID:7624799 !$#accession A57134 !'##status preliminary !'##molecule_type mRNA !'##residues 1-1050 ##label STO !'##cross-references GB:X83368 GENETICS !$#gene GDB:PIK3CG !'##cross-references GDB:370920 !$#map_position 3q26.3-3q26.3 CLASSIFICATION #superfamily phosphatidylinositol 3-kinase KEYWORDS phosphotransferase SUMMARY #length 1050 #molecular-weight 120444 #checksum 5420 SEQUENCE /// ENTRY A43322 #type complete TITLE 1-phosphatidylinositol 3-kinase (EC 2.7.1.137) 110K chain - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A43322 REFERENCE A43322 !$#authors Hiles, I.D.; Otsu, M.; Volinia, S.; Fry, M.J.; Gout, I.; !1Dhand, R.; Panayotou, G.; Ruiz-Larrea, F.; Thompson, A.; !1Totty, N.F.; Hsuan, J.J.; Courtneidge, S.A.; Parker, P.J.; !1Waterfield, M.D. !$#journal Cell (1992) 70:419-429 !$#title Phosphatidylinositol 3-kinase: structure and expression of !1the 110 kd catalytic subunit. !$#cross-references MUID:92354059; PMID:1322797 !$#accession A43322 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA; protein !'##residues 1-1068 ##label HIL !'##cross-references GB:M93252; NID:g163519; PIDN:AAA30698.1; !1PID:g163520 !'##experimental_source brain !'##note sequence extracted from NCBI backbone (NCBIP:110292) CLASSIFICATION #superfamily phosphatidylinositol 3-kinase KEYWORDS phosphotransferase SUMMARY #length 1068 #molecular-weight 124327 #checksum 8628 SEQUENCE /// ENTRY I38110 #type complete TITLE 1-phosphatidylinositol 3-kinase (EC 2.7.1.137) alpha isoform - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS I38110; S44127 REFERENCE A55636 !$#authors Volinia, S.; Hiles, I.; Ormondroyd, E.; Nizetic, D.; !1Antonacci, R.; Rocchi, M.; Waterfield, M.D. !$#journal Genomics (1994) 24:472-477 !$#title Molecular cloning, cDNA sequence, and chromosomal !1localization of the human phosphatidylinositol 3-kinase p110 !1alpha (PIK3CA) gene. !$#cross-references MUID:95229146; PMID:7713498 !$#accession I38110 !'##status preliminary !'##molecule_type mRNA !'##residues 1-1068 ##label RES !'##cross-references EMBL:Z29090; NID:g472990; PIDN:CAA82333.1; !1PID:g472991 GENETICS !$#gene GDB:PIK3CA !'##cross-references GDB:370915; OMIM:171834 !$#map_position 3q26.3-3q26.3 CLASSIFICATION #superfamily phosphatidylinositol 3-kinase KEYWORDS phosphotransferase SUMMARY #length 1068 #molecular-weight 124411 #checksum 9584 SEQUENCE /// ENTRY S57219 #type complete TITLE 1-phosphatidylinositol 3-kinase (EC 2.7.1.137) Vps34-type [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 27-Oct-1995 #sequence_revision 03-Nov-1995 #text_change 01-Feb-2002 ACCESSIONS S57219 REFERENCE S57219 !$#authors Volinia, S.; Dhand, R.; Vanhaesebroeck, B.; MacDougall, !1L.K.; Stein, R.; Zvelebil, M.J.; Domin, J.; Panaretou, C.; !1Waterfield, M.D. !$#journal EMBO J. (1995) 14:3339-3348 !$#title A human phosphatidylinositol 3-kinase complex related to the !1yeast Vps34p-Vps15p protein sorting system. !$#cross-references MUID:95354652; PMID:7628435 !$#accession S57219 !'##molecule_type mRNA !'##residues 1-887 ##label VOL FUNCTION !$#description converts ATP and 1-phosphatidyl-1D-myo-inositol to ADP and !11-phosphatidyl-1D-myo-inositol 3-phosphate [validated; !1MUID:95354652] !$#pathway required for vacuolar sorting and segregation; involved in !1both internalization and delivery steps of endocytosis !$#note specific for phosphatidylinositol, inactive on !1phosphatidylinositol-3-phosphate and !1phosphatidylinositol-4-phosphate CLASSIFICATION #superfamily slime mold phosphatidylinositol 3-kinase KEYWORDS phosphotransferase; protein trafficking SUMMARY #length 887 #molecular-weight 100917 #checksum 6781 SEQUENCE /// ENTRY A59003 #type complete TITLE phosphoinositide 3-kinase (EC 2.7.1.-) - slime mold (Dictyostelium discoideum) ORGANISM #formal_name Dictyostelium discoideum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A59003 REFERENCE A59003 !$#authors Zhou, K.; Takegawa, K.; Emr, S.D.; Firtel, R.A. !$#journal Mol. Cell. Biol. (1995) 15:5645-5656 !$#title A phosphatidylinositol (PI) kinase gene family in !1Dictyostelium discoideum: biological roles of putative !1mammalian p110 and yeast Vps34p PI 3-kinase homologs during !1growth and development. !$#cross-references MUID:96009592; PMID:7565716 !$#accession A59003 !'##status preliminary !'##molecule_type mRNA !'##residues 1-816 ##label ZHO !'##cross-references GB:U23480; NID:g733529; PIDN:AAA85726.1; !1PID:g733530 CLASSIFICATION #superfamily slime mold phosphatidylinositol 3-kinase KEYWORDS phosphotransferase SUMMARY #length 816 #molecular-weight 94646 #checksum 731 SEQUENCE /// ENTRY T52538 #type complete TITLE 1-phosphatidylinositol 3-kinase (EC 2.7.1.137) Vps34 [validated] - fission yeast (Schizosaccharomyces pombe) ORGANISM #formal_name Schizosaccharomyces pombe DATE 24-Oct-2000 #sequence_revision 24-Oct-2000 #text_change 01-Feb-2002 ACCESSIONS T52538; PC4002 REFERENCE Z26107 !$#authors Takegawa, K.; DeWald, D.B.; Emr, S.E. !$#journal J. Cell Sci. (1995) 108:3745-3756 !$#title Schizosaccharomyces pombe Vps34p, a !1phosphatidylinositol-specific PI 3-kinase essential for !1normal cell growth and vacuole morphology. !$#cross-references PMID:8719881 !$#accession T52538 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-801 ##label TAK !'##cross-references EMBL:U32583; PIDN:AAC49133.1 REFERENCE PC4002 !$#authors Kimura, K.; Miyake, S.; Makuuchi, M.; Morita, R.; Usui, T.; !1Yoshida, M.; Horinouchi, S.; Fukui, Y. !$#journal Biosci. Biotechnol. Biochem. (1995) 59:678-682 !$#title Phosphatidylinositol-3 kinase in fission yeast: A possible !1role in stress responses. !$#cross-references MUID:95290763; PMID:7772832 !$#accession PC4002 !'##molecule_type DNA !'##residues 138-163,'K',165-235,'I',237-641,'T',643-801 ##label KIM GENETICS !$#gene vps34 FUNCTION !$#description converts ATP and 1-phosphatidyl-1D-myo-inositol to ADP and !11-phosphatidyl-1D-myo-inositol 3-phosphate [validated; !1PMID:8719881] !$#pathway required for vacuolar sorting and segregation; involved in !1both internalization and delivery steps of endocytosis !$#note specific for phosphatidylinositol, inactive on !1phosphatidylinositol-3-phosphate and !1phosphatidylinositol-4-phosphate CLASSIFICATION #superfamily slime mold phosphatidylinositol 3-kinase KEYWORDS phosphotransferase; protein trafficking SUMMARY #length 801 #molecular-weight 92134 #checksum 4119 SEQUENCE /// ENTRY A36369 #type complete TITLE 1-phosphatidylinositol 3-kinase (EC 2.7.1.137) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein L9672.10; protein YLR240w; vacuolar protein-sorting protein VPS34 ORGANISM #formal_name Saccharomyces cerevisiae DATE 28-Mar-1991 #sequence_revision 28-Mar-1991 #text_change 01-Feb-2002 ACCESSIONS A36369; S59386 REFERENCE A36369 !$#authors Herman, P.K.; Emr, S.D. !$#journal Mol. Cell. Biol. (1990) 10:6742-6754 !$#title Characterization of VPS34, a gene required for vacuolar !1protein sorting and vacuole segregation in Saccharomyces !1cerevisiae. !$#cross-references MUID:91061783; PMID:2247081 !$#accession A36369 !'##molecule_type DNA !'##residues 1-875 ##label HER !'##cross-references GB:X53531; NID:g4783; PIDN:CAA37610.1; PID:g4784 REFERENCE S59386 !$#authors Johnson, D. !$#submission submitted to the EMBL Data Library, February 1995 !$#description The sequence of S. cerevisiae cosmid 9672. !$#accession S59386 !'##molecule_type DNA !'##residues 1-875 ##label JOH !'##cross-references EMBL:U20865; NID:g662330; PID:g662340; MIPS:YLR240w !'##experimental_source strain S288C (AB972) GENETICS !$#gene SGD:VPS34; VPT29; END12 !'##cross-references SGD:S0004230; MIPS:YLR240w !$#map_position 12R FUNCTION !$#description converts ATP and 1-phosphatidyl-1D-myo-inositol to ADP and !11-phosphatidyl-1D-myo-inositol 3-phosphate !$#pathway required for vacuolar sorting and segregation; involved in !1both internalization and delivery steps of endocytosis !$#note specific for phosphatidylinositol, inactive on !1phosphatidylinositol-3-phosphate and !1phosphatidylinositol-4-phosphate CLASSIFICATION #superfamily slime mold phosphatidylinositol 3-kinase KEYWORDS phosphotransferase SUMMARY #length 875 #molecular-weight 100920 #checksum 615 SEQUENCE /// ENTRY JC5500 #type complete TITLE phosphoinositide 3-kinase (EC 2.7.1.-) - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS JC5500 REFERENCE JC5500 !$#authors Brown, R.A.; Ho, L.K.F.; Weber-Hall, S.J.; Shipley, J.M.; !1Fry, M.J. !$#journal Biochem. Biophys. Res. Commun. (1997) 233:537-544 !$#title Identification and cDNA cloning of a novel mammalian C2 !1domain-containing phosphoinositide 3-kinase, HsC2-PI3K. !$#cross-references MUID:97289668; PMID:9144573 !$#accession JC5500 !'##molecule_type mRNA !'##residues 1-1634 ##label BRO !'##cross-references GB:Y11312; NID:g2808446; PIDN:CAA72168.1; !1PID:g2076604 !'##experimental_source breast cell COMMENT This enzyme is involved in receptor signal transduction, in !1a signalling complex which mediates intracellular protein !1trafficking, and in the regulation of cell proliferation and !1cell surivival. GENETICS !$#gene GDB:PIK3C2B; C2-PI3K; PI3K-C2beta !'##cross-references GDB:9837703; OMIM:602838 !$#map_position 1q32-1q32 CLASSIFICATION #superfamily HsC2 phosphatidylinositol 3-kinase; protein !1kinase C C2 region homology KEYWORDS phosphotransferase FEATURE !$156-162,169-174 #domain SH3 #status predicted #label SH3\ !$1037-1320 #domain catalytic #status predicted #label CAT\ !$1498-1612 #domain protein kinase C C2 region homology #label !8KC2A SUMMARY #length 1634 #molecular-weight 184856 #checksum 1177 SEQUENCE /// ENTRY KIZPMN #type complete TITLE protein kinase cdr1 (EC 2.7.1.-) - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES mitosis inducer nim1 ORGANISM #formal_name Schizosaccharomyces pombe DATE 28-Dec-1987 #sequence_revision 07-Jun-1996 #text_change 11-Jun-1999 ACCESSIONS S16153; A25958 REFERENCE S16153 !$#authors Feilotter, H.; Nurse, P.; Young, P.G. !$#journal Genetics (1991) 127:309-318 !$#title Genetic and molecular analysis of cdr1/nim1 in !1Schizosaccharomyces pombe. !$#cross-references MUID:91169281; PMID:2004705 !$#accession S16153 !'##status preliminary !'##molecule_type DNA !'##residues 1-593 ##label FEI !'##cross-references EMBL:X57549; NID:g4928; PIDN:CAA40774.1; PID:g4929 !'##note the authors translated the codon ATT for residue 570 as Ala REFERENCE A25958 !$#authors Russell, P.; Nurse, P. !$#journal Cell (1987) 49:569-576 !$#title The mitotic inducer nim1+ functions in a regulatory network !1of protein kinase homologs controlling the initiation of !1mitosis. !$#cross-references MUID:87187654; PMID:3453113 !$#accession A25958 !'##molecule_type DNA !'##residues 1-356,'LNKFRTKASE',367,'AAY' ##label RUS !'##cross-references GB:M16509; NID:g173414; PIDN:AAA35317.1; !1PID:g173415 GENETICS !$#gene nim1+ FUNCTION !$#description a dose-dependent mitotic inducer; phosphorylates and !1inactivates the mitosis inhibitor protein kinase wee1 CLASSIFICATION #superfamily protein kinase cdr1; protein kinase homology KEYWORDS ATP; cell cycle control; mitosis; phosphotransferase; !1serine/threonine-specific protein kinase FEATURE !$10-258 #domain protein kinase homology #label KIN\ !$18-26 #region protein kinase ATP-binding motif\ !$41 #active_site Lys #status predicted SUMMARY #length 593 #molecular-weight 67044 #checksum 6758 SEQUENCE /// ENTRY S51025 #type complete TITLE [hydroxymethylglutaryl-CoA reductase (NADPH2)] kinase (EC 2.7.1.109) - human ALTERNATE_NAMES AMPK CONTAINS [acetyl-CoA carboxylase] kinase (EC 2.7.1.128); [hydroxymethylglutaryl-CoA reductase (NADPH)] kinase (EC 2.7.1.109) ORGANISM #formal_name Homo sapiens #common_name man DATE 01-Aug-1995 #sequence_revision 01-Sep-1995 #text_change 03-Jun-2002 ACCESSIONS S51025; I38503 REFERENCE S51025 !$#authors Beri, R.K.; Marley, A.E.; See, C.G.; Sopwith, W.F.; Aguan, !1K.; Carling, D.; Scott, J.; Carey, F. !$#journal FEBS Lett. (1994) 356:117-121 !$#title Molecular cloning, expression and chromosomal localisation !1of human AMP-activated protein kinase. !$#cross-references MUID:95080410; PMID:7988703 !$#accession S51025 !'##status preliminary !'##molecule_type mRNA !'##residues 1-552 ##label BER REFERENCE I38503 !$#authors Aguan, K.; Scott, J.; See, C.G.; Sarkar, N.H. !$#journal Gene (1994) 149:345-350 !$#title Characterization and chromosomal localization of the human !1homologue of a rat AMP-activated protein kinase-encoding !1gene: a major regulator of lipid metabolism in mammals. !$#cross-references MUID:95047501; PMID:7959015 !$#accession I38503 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-179,'T',181-270,'G',272-402,'RQ',405-552 ##label RES !'##cross-references EMBL:U06454; NID:g758366; PIDN:AAA64745.1; !1PID:g758367 GENETICS !$#gene GDB:PRKAA2; PRKAA; AMPK; hAMPK !'##cross-references GDB:451905; OMIM:600497 !$#map_position 1p31-1p31 FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP !$#note in vivo substrates include hydroxymethylglutaryl-CoA !1reductase (NADPH) and acetyl-CoA carboxylase CLASSIFICATION #superfamily AMP-activated protein kinase; protein kinase !1homology KEYWORDS ATP; magnesium; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$14-268 #domain protein kinase homology #label KIN\ !$22-30 #region protein kinase ATP-binding motif\ !$45,64,139,141 #active_site Lys, Glu, Asp, Lys #status predicted\ !$144,148 #binding_site magnesium (Asn, Asp) #status predicted SUMMARY #length 552 #molecular-weight 62319 #checksum 5556 SEQUENCE /// ENTRY A53621 #type complete TITLE [hydroxymethylglutaryl-CoA reductase (NADPH2)] kinase (EC 2.7.1.109) - rat CONTAINS [acetyl-CoA carboxylase] kinase (EC 2.7.1.128); [hydroxymethylglutaryl-CoA reductase (NADPH)] kinase (EC 2.7.1.109) ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 07-Jul-1995 #sequence_revision 07-Jul-1995 #text_change 03-Jun-2002 ACCESSIONS A53621; S53729 REFERENCE A53621 !$#authors Carling, D.; Aguan, K.; Woods, A.; Verhoeven, A.J.M.; Beri, !1R.K.; Brennan, C.H.; Sidebottom, C.; Davison, M.D.; Scott, !1J. !$#journal J. Biol. Chem. (1994) 269:11442-11448 !$#title Mammalian AMP-activated protein kinase is homologous to !1yeast and plant protein kinases involved in the regulation !1of carbon metabolism. !$#cross-references MUID:94209324; PMID:7908907 !$#accession A53621 !'##status preliminary !'##molecule_type mRNA !'##residues 1-552 ##label CAR !'##cross-references GB:Z29486; NID:g488375; PIDN:CAA82620.1; !1PID:g488376 REFERENCE S53729 !$#authors Gao, G.; Widmer, J.; Stapleton, D.; Teh, T.; Cox, T.; Kemp, !1B.E.; Witters, L.A. !$#journal Biochim. Biophys. Acta (1995) 1266:73-82 !$#title Catalytic subunits of the porcine and rat 5'-AMP-activated !1protein kinase are members of the SNF1 protein kinase !1family. !$#cross-references MUID:95234757; PMID:7718624 !$#accession S53729 !'##status preliminary !'##molecule_type mRNA !'##residues 1-354,'S',356-461,'D',463-552 ##label GAO !'##cross-references GB:U12149; NID:g862472; PIDN:AAA85033.1; !1PID:g862473 FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP CLASSIFICATION #superfamily AMP-activated protein kinase; protein kinase !1homology KEYWORDS ATP; magnesium; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$14-268 #domain protein kinase homology #label KIN\ !$22-30 #region protein kinase ATP-binding motif\ !$45,64,139,141 #active_site Lys, Glu, Asp, Lys #status predicted\ !$144,148 #binding_site magnesium (Asn, Asp) #status predicted SUMMARY #length 552 #molecular-weight 62257 #checksum 5575 SEQUENCE /// ENTRY S44859 #type complete TITLE serine/threonine-specific protein kinase (EC 2.7.1.-) PAR2.3 - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 20-Feb-1995 #sequence_revision 20-Feb-1995 #text_change 11-Jun-1999 ACCESSIONS S44859 REFERENCE S44857 !$#authors Wilson, R. !$#submission submitted to the EMBL Data Library, March 1994 !$#description The sequence of C. elegans plasmid pAR2. !$#accession S44859 !'##status preliminary !'##molecule_type DNA !'##residues 1-622 ##label WIL !'##cross-references EMBL:U00025; NID:g458884; PIDN:AAA50618.1; !1PID:g458887 GENETICS !$#introns 40/1; 148/3; 236/1; 305/3; 322/3; 507/1; 552/1; 581/3 FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP CLASSIFICATION #superfamily AMP-activated protein kinase; protein kinase !1homology KEYWORDS ATP; magnesium; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$22-276 #domain protein kinase homology #label KIN\ !$30-38 #region protein kinase ATP-binding motif\ !$53,72,147,149 #active_site Lys, Glu, Asp, Lys #status predicted\ !$152,156 #binding_site magnesium (Asn, Asp) #status predicted SUMMARY #length 622 #molecular-weight 69515 #checksum 4347 SEQUENCE /// ENTRY A26030 #type complete TITLE serine/threonine-specific protein kinase (EC 2.7.1.-) SNF1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YDR477w ORGANISM #formal_name Saccharomyces cerevisiae DATE 20-Aug-1987 #sequence_revision 20-Aug-1987 #text_change 23-Mar-2001 ACCESSIONS A26030; S69644 REFERENCE A26030 !$#authors Celenza, J.L.; Carlson, M. !$#journal Science (1986) 233:1175-1180 !$#title A yeast gene that is essential for release from glucose !1repression encodes a protein kinase. !$#cross-references MUID:86289463; PMID:3526554 !$#accession A26030 !'##molecule_type DNA !'##residues 1-633 ##label CEL !'##cross-references EMBL:M13971; NID:g172629; PIDN:AAA35058.1; !1PID:g172630 REFERENCE S69554 !$#authors Dietrich, F.S. !$#submission submitted to the EMBL Data Library, August 1995 !$#description The sequence of S. cerevisiae cosmids 9410, 8035, 8166, and !19787. !$#accession S69644 !'##molecule_type DNA !'##residues 1-633 ##label DIE !'##cross-references EMBL:U33050; NID:g927726; PIDN:AAB64904.1; !1PID:g927732; GSPDB:GN00004; MIPS:YDR477w GENETICS !$#gene SGD:SNF1; MIPS:YDR477w !'##cross-references SGD:S0002885; MIPS:YDR477w !$#map_position 4R FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP !$#note required for expression of glucose-repressed genes in !1response to glucose deprivation CLASSIFICATION #superfamily AMP-activated protein kinase; protein kinase !1homology KEYWORDS ATP; autophosphorylation; magnesium; nucleus; !1phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$53-306 #domain protein kinase homology #label KIN\ !$61-69 #region protein kinase ATP-binding motif\ !$84,103,177,179 #active_site Lys, Glu, Asp, Lys #status predicted\ !$182,186 #binding_site magnesium (Asn, Asp) #status predicted\ !$210 #binding_site phosphate (Thr) (covalent) (by !8unidentified kinase) #status predicted SUMMARY #length 633 #molecular-weight 72045 #checksum 7112 SEQUENCE /// ENTRY JC1446 #type complete TITLE serine/threonine-specific protein kinase (EC 2.7.1.-) AK21 - Arabidopsis thaliana ALTERNATE_NAMES protein kinase SNF1 homolog ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 11-Jun-1999 ACCESSIONS JC1446; S58266; S66334 REFERENCE JC1446 !$#authors LeGuen, L.; Thomas, M.; Bianchi, M.; Halford, N.G.; Kreis, !1M. !$#journal Gene (1992) 120:249-254 !$#title Structure and expression of a gene from Arabidopsis thaliana !1encoding a protein related to SNF1 protein kinase. !$#cross-references MUID:93013041; PMID:1339373 !$#accession JC1446 !'##molecule_type DNA !'##residues 1-512 ##label LEG !'##cross-references GB:M93023; NID:g166599; PIDN:AAA32736.1; !1PID:g166600 REFERENCE S58256 !$#authors Thuemmler, F.; Kirchner, M.; Teuber, R.; Dittrich, P. !$#submission submitted to the EMBL Data Library, May 1995 !$#description Differential accumulation of the transcripts of 22 novel !1protein kinase genes in Arabidopsis thaliana. !$#accession S58266 !'##status preliminary !'##molecule_type DNA !'##residues 144-198 ##label THU !'##cross-references EMBL:X86966; NID:g928909; PIDN:CAA60529.1; !1PID:g928910 REFERENCE S66314 !$#authors Thuemmler, F.; Kirchner, M.; Teuber, R.; Dittrich, P. !$#journal Plant Mol. Biol. (1995) 29:551-565 !$#title Differential accumulation of the transcripts of 22 novel !1protein kinase genes in Arabidopsis thaliana. !$#cross-references MUID:96123233; PMID:8534852 !$#accession S66334 !'##molecule_type DNA !'##residues 144-198 ##label TH2 !'##cross-references EMBL:X86966; NID:g928909; PIDN:CAA60529.1; !1PID:g928910 COMMENT This enzyme plays an important role in a signal transduction !1cascade regulating gene expression and carbohydrate !1metabolism in higher plants. GENETICS !$#gene AKin10; AK21 !$#introns 64/1; 125/3; 186/3; 230/3; 292/3; 322/3; 350/3; 396/3; 475/3 FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP CLASSIFICATION #superfamily AMP-activated protein kinase; protein kinase !1homology KEYWORDS ATP; magnesium; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$17-271 #domain protein kinase homology #label KIN\ !$25-33 #region protein kinase ATP-binding motif\ !$48,67,142,144 #active_site Lys, Glu, Asp, Lys #status predicted\ !$147,151 #binding_site magnesium (Asn, Asp) #status predicted SUMMARY #length 512 #molecular-weight 58373 #checksum 3477 SEQUENCE /// ENTRY A56009 #type complete TITLE serine/threonine-specific protein kinase (EC 2.7.1.-) NPK5 - common tobacco ORGANISM #formal_name Nicotiana tabacum #common_name common tobacco DATE 28-Apr-1995 #sequence_revision 28-Apr-1995 #text_change 16-Jun-2000 ACCESSIONS A56009 REFERENCE A56009 !$#authors Muranaka, T.; Banno, H.; Machida, Y. !$#journal Mol. Cell. Biol. (1994) 14:2958-2965 !$#title Characterization of tobacco protein kinase NPK5, a homolog !1of Saccharomyces cerevisiae SNF1 that constitutively !1activates expression of the glucose-repressible SUC2 gene !1for a secreted invertase of Saccharomyces cerevisiae. !$#cross-references MUID:94217693; PMID:8164654 !$#accession A56009 !'##status preliminary !'##molecule_type mRNA !'##residues 1-511 ##label MUR !'##cross-references GB:D26602; NID:g496384; PIDN:BAA05649.1; !1PID:g496385 FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP CLASSIFICATION #superfamily AMP-activated protein kinase; protein kinase !1homology KEYWORDS ATP; magnesium; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$17-271 #domain protein kinase homology #label KIN\ !$25-33 #region protein kinase ATP-binding motif\ !$48,67,142,144 #active_site Lys, Glu, Asp, Lys #status predicted\ !$147,151 #binding_site magnesium (Asn, Asp) #status predicted SUMMARY #length 511 #molecular-weight 58339 #checksum 7683 SEQUENCE /// ENTRY S59941 #type fragment TITLE serine/threonine-specific protein kinase (EC 2.7.1.-) BKIN2 - barley (fragment) ORGANISM #formal_name Hordeum vulgare #common_name barley DATE 15-Feb-1996 #sequence_revision 01-Mar-1996 #text_change 26-Feb-1999 ACCESSIONS S59941 REFERENCE S59941 !$#authors Hannappel, U.; Vicente-Carbajosa, J.; Barker, J.H.A.; !1Shewry, P.R.; Halford, N.G. !$#journal Plant Mol. Biol. (1995) 27:1235-1240 !$#title Differential expression of two barley SNF1-related protein !1kinase genes. !$#cross-references MUID:95284374; PMID:7766906 !$#accession S59941 !'##status preliminary !'##molecule_type mRNA !'##residues 1-473 ##label HAN !'##cross-references EMBL:X82548 GENETICS !$#gene BKIN2 FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP CLASSIFICATION #superfamily AMP-activated protein kinase; protein kinase !1homology KEYWORDS ATP; magnesium; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$1-244 #domain protein kinase homology (fragment) #label !8KIN\ !$21,40,115,117 #active_site Lys, Glu, Asp, Lys #status predicted\ !$120,124 #binding_site magnesium (Asn, Asp) #status predicted SUMMARY #length 473 #checksum 9644 SEQUENCE /// ENTRY A41361 #type complete TITLE serine/threonine-specific protein kinase (EC 2.7.1.-) RKIN1 - rye ORGANISM #formal_name Secale cereale #common_name rye DATE 12-Jun-1992 #sequence_revision 12-Jun-1992 #text_change 11-Jun-1999 ACCESSIONS A41361 REFERENCE A41361 !$#authors Alderson, A.; Sabelli, P.A.; Dickinson, J.R.; Cole, D.; !1Richardson, M.; Kreis, M.; Shewry, P.R.; Halford, N.G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:8602-8605 !$#title Complementation of snf1, a mutation affecting global !1regulation of carbon metabolism in yeast, by a plant protein !1kinase cDNA. !$#cross-references MUID:92020901; PMID:1924320 !$#accession A41361 !'##molecule_type mRNA !'##residues 1-502 ##label ALD !'##cross-references GB:M74113; NID:g169835; PIDN:AAA33921.1; !1PID:g169836 FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP CLASSIFICATION #superfamily AMP-activated protein kinase; protein kinase !1homology KEYWORDS ATP; autophosphorylation; magnesium; phosphoprotein; !1phosphotransferase; serine/threonine-specific protein kinase FEATURE !$12-269 #domain protein kinase homology #label KIN\ !$20-28 #region protein kinase ATP-binding motif\ !$43,62,140,142 #active_site Lys, Glu, Asp, Lys #status predicted\ !$145,149 #binding_site magnesium (Asn, Asp) #status predicted SUMMARY #length 502 #molecular-weight 57710 #checksum 8190 SEQUENCE /// ENTRY S60303 #type complete TITLE serine/threonine-specific protein kinase (EC 2.7.1.-) BKIN12 (version 1) - barley ORGANISM #formal_name Hordeum vulgare #common_name barley DATE 20-Jul-1996 #sequence_revision 27-Feb-1997 #text_change 11-Jun-1999 ACCESSIONS S60303; S24578 REFERENCE S60303 !$#authors Halford, N.G.; Vicente-Carbajosa, J.; Sabelli, P.A.; Shewry, !1P.R.; Hannappel, U.; Kreis, M. !$#journal Plant J. (1992) 2:791-797 !$#title Molecular analyses of a barley multigene family homologous !1to the yeast protein kinase gene SNF1. !$#cross-references MUID:93258420; PMID:1302632 !$#accession S60303 !'##status preliminary !'##molecule_type DNA !'##residues 1-513 ##label HAL !'##cross-references EMBL:X65606; NID:g18931; PIDN:CAA46556.1; !1PID:g18932 GENETICS !$#introns 62/1; 126/3; 187/3; 231/3; 293/3; 323/3; 351/3; 398/3; 476/3 FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP CLASSIFICATION #superfamily AMP-activated protein kinase; protein kinase !1homology KEYWORDS ATP; magnesium; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$15-272 #domain protein kinase homology #label KIN\ !$23-31 #region protein kinase ATP-binding motif\ !$46,65,143,145 #active_site Lys, Glu, Asp, Lys #status predicted\ !$148,152 #binding_site magnesium (Asn, Asp) #status predicted SUMMARY #length 513 #molecular-weight 58715 #checksum 9344 SEQUENCE /// ENTRY S60304 #type complete TITLE serine/threonine-specific protein kinase (EC 2.7.1.-) BKIN12 (version 2) - barley ORGANISM #formal_name Hordeum vulgare #common_name barley DATE 19-Mar-1997 #sequence_revision 15-Aug-1997 #text_change 11-Jun-1999 ACCESSIONS S60304; S24579 REFERENCE S60303 !$#authors Halford, N.G.; Vicente-Carbajosa, J.; Sabelli, P.A.; Shewry, !1P.R.; Hannappel, U.; Kreis, M. !$#journal Plant J. (1992) 2:791-797 !$#title Molecular analyses of a barley multigene family homologous !1to the yeast protein kinase gene SNF1. !$#cross-references MUID:93258420; PMID:1302632 !$#accession S60304 !'##status preliminary !'##molecule_type mRNA !'##residues 1-513 ##label HAL !'##cross-references EMBL:X65604 REFERENCE S24578 !$#authors Halford, N.G. !$#submission submitted to the EMBL Data Library, April 1992 !$#accession S24579 !'##status preliminary !'##molecule_type mRNA !'##residues 1-61,'A',63-513 ##label HA2 !'##cross-references EMBL:X65604; NID:g18933; PIDN:CAA46554.1; !1PID:g18934 FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP CLASSIFICATION #superfamily AMP-activated protein kinase; protein kinase !1homology KEYWORDS ATP; magnesium; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$15-272 #domain protein kinase homology #label KIN\ !$23-31 #region protein kinase ATP-binding motif\ !$46,65,143,145 #active_site Lys, Glu, Asp, Lys #status predicted\ !$148,152 #binding_site magnesium (Asn, Asp) #status predicted SUMMARY #length 513 #molecular-weight 58841 #checksum 1033 SEQUENCE /// ENTRY A59309 #type complete TITLE interferon-inducible RNA-dependent, translation initiation factor alpha kinase 2 (EC 2.7.1.-) [similarity] - mouse ALTERNATE_NAMES p65 kinase; protein kinase TIK ORGANISM #formal_name Mus musculus #common_name house mouse DATE 16-Jun-2000 #sequence_revision 16-Jun-2000 #text_change 16-Jun-2000 ACCESSIONS A59309; A40813; A45258 REFERENCE A59309 !$#authors Tanaka, H.; Samuel, C.E. !$#journal Gene (1995) 153:283-284 !$#title Sequence of the murine interferon-inducible RNA-dependent !1protein kinase (PKR) deduced from genomic clones. !$#cross-references MUID:95180736; PMID:7533117 !$#accession A59309 !'##molecule_type DNA !'##residues 1-515 ##label ICE !'##cross-references GB:U09928; NID:g536916; PIDN:AAC24729.1; !1PID:g536918 !'##experimental_source strain DBA/2J; tissue type liver; dev stage !1adult REFERENCE A40813 !$#authors Icely, P.L.; Gros, P.; Bergeron, J.J.M.; Devault, A.; Afar, !1D.E.H.; Bell, J.C. !$#journal J. Biol. Chem. (1991) 266:16073-16077 !$#title TIK, a novel serine/threonine kinase, is recognized by !1antibodies directed against phosphotyrosine. !$#cross-references MUID:91340757; PMID:1714905 !$#accession A40813 !'##molecule_type mRNA !'##residues 1-51,'G',53-59,'T',61-86,'C',88-509,'E',511,'KHMLGPF' !1##label IC2 !'##cross-references GB:M65029; NID:g201067; PIDN:AAA40150.1; !1PID:g201068 !'##experimental_source cell line L1210; cell type Lymphocytic Leukemia !'##note the authors translated the codon AAT for residue 112 as Leu, !1and TAT for residue 113 as Ile REFERENCE A45258 !$#authors Feng, G.; Chong, K.; Kumar, A.; Williams, B.R.G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:5447-5451 !$#title Identification of double-stranded RNA-binding domains in the !1interferon-induced double-stranded RNA-activated p68 kinase. !$#cross-references MUID:92302260; PMID:1351683 !$#accession A45258 !'##molecule_type mRNA !'##residues 1-280,'DR',283-515 ##label FEN !'##cross-references GB:M93567; NID:g201067 !'##experimental_source cell line FM3; mammary tumor !'##note the translated sequence in GenBank entry MUSSTKINA, release !1114, (PIDN:AAA40150.1) differs from the published sequence !1in having 144-Ile GENETICS !$#gene MGI:Eif2ak2; PKR !'##cross-references MGI:1353449 !$#map_position 17:40.0 CLASSIFICATION #superfamily protein kinase TIK; double-stranded RNA-binding !1repeat homology; protein kinase homology KEYWORDS autophosphorylation; phosphoprotein; phosphotransferase; RNA !1binding; serine/threonine-specific protein kinase FEATURE !$5-77 #domain double-stranded RNA-binding repeat homology !8#label DSR\ !$240-502 #domain protein kinase homology #label KIN SUMMARY #length 515 #molecular-weight 58280 #checksum 642 SEQUENCE /// ENTRY S50216 #type complete TITLE translation initiation factor eIF-2 alpha chain kinase (EC 2.7.1.-) - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S50216 REFERENCE S50216 !$#authors Mellor, H.; Flowers, K.M.; Kimball, S.R.; Jefferson, L.S. !$#journal Biochim. Biophys. Acta (1994) 1219:693-696 !$#title Cloning and characterization of a cDNA encoding rat PKR, the !1double-stranded RNA-dependent eukaryotic initiation factor-2 !1kinase. !$#cross-references MUID:95035100; PMID:7948027 !$#accession S50216 !'##status preliminary; translation not shown !'##molecule_type mRNA !'##residues 1-513 ##label MEL !'##cross-references EMBL:L29281; NID:g468372; PIDN:AAA61926.1; !1PID:g468373 CLASSIFICATION #superfamily protein kinase TIK; double-stranded RNA-binding !1repeat homology; protein kinase homology KEYWORDS autophosphorylation; phosphoprotein; phosphotransferase; RNA !1binding; serine/threonine-specific protein kinase FEATURE !$5-77 #domain double-stranded RNA-binding repeat homology !8#label DSR\ !$234-500 #domain protein kinase homology #label KIN SUMMARY #length 513 #molecular-weight 58258 #checksum 6338 SEQUENCE /// ENTRY JC5225 #type complete TITLE dsRNA-activated protein kinase (EC 2.7.1.-) - human ALTERNATE_NAMES p68 kinase; protein kinase P1/eIF-2 alpha ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JC5225; A39650 REFERENCE JC5225 !$#authors Kuhen, K.L.; Shen, X.; Samuel, C.E. !$#journal Gene (1996) 178:191-193 !$#title Mechanism of interferon action sequence of the human !1interferon-inducible RNA-dependent protein kinase (PKR) !1deduced from genomic clones. !$#cross-references MUID:97080568; PMID:8921913 !$#accession JC5225 !'##molecule_type DNA !'##residues 1-551 ##label KUH !'##cross-references GB:U50632 REFERENCE A39650 !$#authors Meurs, E.; Chong, K.; Galabru, J.; Thomas, N.S.B.; Kerr, !1I.M.; Williams, B.R.G.; Hovanessian, A.G. !$#journal Cell (1990) 62:379-390 !$#title Molecular cloning and characterization of the human !1double-stranded RNA-activated protein kinase induced by !1interferon. !$#cross-references MUID:90322433; PMID:1695551 !$#accession A39650 !'##molecule_type mRNA !'##residues 1-215,'IY',219-551 ##label MEU !'##cross-references GB:M35663 COMMENT This enzyme plays roles in the regulation of protein !1synthesis in interferon-treated and virus-infected cells, !1and in the control of cell growth and differentation in !1uninfected cells. COMMENT Autophosphorylation is dependent on the presence of !1double-stranded RNA (dsRNA). Phosphorylation of exogenous !1substrates, such as translation initiation factor eIF2 alpha !1chain, is dependent on the phosphorylation state of the !1kinase rather than on dsRNA. GENETICS !$#gene GDB:PRKR; PKR !'##cross-references GDB:136275; OMIM:176871 !$#map_position 2p22-2p21 !$#introns 40/2; 80/3; 130/2; 172/3; 198/2; 229/3; 241/2; 262/2; 303/2; !1356/2; 416/3; 459/3; 493/3; 511/3 CLASSIFICATION #superfamily protein kinase TIK; double-stranded RNA-binding !1repeat homology; protein kinase homology KEYWORDS autophosphorylation; phosphoprotein; phosphotransferase; RNA !1binding; serine/threonine-specific protein kinase FEATURE !$6-78 #domain double-stranded RNA-binding repeat homology !8#label DSR\ !$265-538 #domain protein kinase homology #label KIN SUMMARY #length 551 #molecular-weight 62094 #checksum 5614 SEQUENCE /// ENTRY JC1515 #type complete TITLE calcium-dependent protein kinase (EC 2.7.1.-) - rice ORGANISM #formal_name Oryza sativa #common_name rice DATE 14-Jul-1994 #sequence_revision 14-Jul-1994 #text_change 16-Jun-2000 ACCESSIONS JC1515 REFERENCE JC1515 !$#authors Kawasaki, T.; Hayashida, N.; Baba, T.; Shinozaki, K.; !1Shimada, H. !$#journal Gene (1993) 129:183-189 !$#title The gene encoding a calcium-dependent protein kinase located !1near the sbe1 gene encoding starch branching enzyme I is !1specifically expressed in developing rice seeds. !$#cross-references MUID:93314961; PMID:8325505 !$#accession JC1515 !'##molecule_type mRNA !'##residues 1-534 ##label KAW !'##cross-references GB:D13436; NID:g435465; PIDN:BAA02698.1; !1PID:g435466 !'##experimental_source seed COMMENT This enzyme is involved in the synthesis of seed storage !1proteins during seed development. GENETICS !$#gene spk CLASSIFICATION #superfamily calcium-dependent protein kinase; calmodulin !1repeat homology; protein kinase homology KEYWORDS ATP; calcium binding; EF hand; phosphotransferase FEATURE !$71-331 #domain protein kinase homology #label KIN\ !$79-87 #region protein kinase ATP-binding motif\ !$374-405 #domain calmodulin repeat homology #label EF1\ !$409-440 #domain calmodulin repeat homology #label EF2\ !$444-476 #domain calmodulin repeat homology #label EF3\ !$478-510 #domain calmodulin repeat homology #label EF4\ !$102 #active_site Lys #status predicted SUMMARY #length 534 #molecular-weight 60572 #checksum 5367 SEQUENCE /// ENTRY S71770 #type complete TITLE calcium-dependent protein kinase (EC 2.7.1.-) - mung bean ORGANISM #formal_name Vigna radiata #common_name mung bean DATE 14-May-1999 #sequence_revision 14-May-1999 #text_change 11-Jun-1999 ACCESSIONS S71770 REFERENCE S71770 !$#authors Botella, J.R.; Arteca, J.M.; Somodevilla, M.; Arteca, R.N. !$#journal Plant Mol. Biol. (1996) 30:1129-1137 !$#title Calcium-dependent protein kinase gene expression in response !1to physical and chemical stimuli in mungbean (Vigna !1radiata). !$#cross-references MUID:96311003; PMID:8704124 !$#accession S71770 !'##molecule_type mRNA !'##residues 1-487 ##label BOT !'##cross-references EMBL:U08140; NID:g967124; PIDN:AAC49405.1; !1PID:g967125 !'##experimental_source strain Rwilcz, cv. Berken, clone pVr-CDPK-1 CLASSIFICATION #superfamily calcium-dependent protein kinase; calmodulin !1repeat homology; protein kinase homology KEYWORDS ATP; calcium binding; EF hand; phosphotransferase; serine/ !1threonine-specific protein kinase; tandem repeat FEATURE !$22-282 #domain protein kinase homology #label KIN\ !$30-38 #region protein kinase ATP-binding motif\ !$325-357 #domain calmodulin repeat homology #label EF2\ !$361-393 #domain calmodulin repeat homology #label EF3\ !$397-429 #domain calmodulin repeat homology #label EF4\ !$431-463 #domain calmodulin repeat homology #label EF5\ !$53 #active_site Lys #status predicted SUMMARY #length 487 #molecular-weight 54700 #checksum 4454 SEQUENCE /// ENTRY T03271 #type complete TITLE calcium-dependent protein kinase (EC 2.7.1.-) 1 - maize ORGANISM #formal_name Zea mays #common_name maize DATE 14-May-1999 #sequence_revision 14-May-1999 #text_change 16-Jun-2000 ACCESSIONS T03271 REFERENCE Z14873 !$#authors Berberich, T.; Kusano, T. !$#journal Mol. Gen. Genet. (1996) 254:275-283 !$#title Cycloheximide induces a subset of low temperature-inducible !1genes in maize. !$#accession T03271 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-492 ##label BER !'##cross-references EMBL:D84408; PIDN:BAA12338.1 !'##experimental_source strain honey bantum !'##note low temperature-inducible GENETICS !$#gene CDPK1 CLASSIFICATION #superfamily calcium-dependent protein kinase; calmodulin !1repeat homology; protein kinase homology KEYWORDS ATP; calcium binding; EF hand; phosphotransferase; serine/ !1threonine-specific protein kinase; tandem repeat FEATURE !$25-285 #domain protein kinase homology #label KIN\ !$33-41 #region protein kinase ATP-binding motif\ !$328-360 #domain calmodulin repeat homology #label EF1\ !$364-396 #domain calmodulin repeat homology #label EF2\ !$400-432 #domain calmodulin repeat homology #label EF3\ !$434-466 #domain calmodulin repeat homology #label EF4\ !$56 #active_site Lys #status predicted SUMMARY #length 492 #molecular-weight 54734 #checksum 7123 SEQUENCE /// ENTRY T03263 #type complete TITLE calcium-dependent protein kinase (EC 2.7.1.-) 7 - maize ORGANISM #formal_name Zea mays #common_name maize DATE 14-May-1999 #sequence_revision 14-May-1999 #text_change 21-Jul-2000 ACCESSIONS T03263 REFERENCE Z14815 !$#authors Saijo, Y.; Hata, S.; Sheen, J.; Izui, K. !$#journal Biochim. Biophys. Acta (1997) 1350:109-114 !$#title CDNA cloning and prokaryotic expression of a maize !1calcium-dependent protein kinase. !$#cross-references MUID:97201047; PMID:9048876 !$#accession T03263 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-554 ##label SAI !'##cross-references EMBL:D87042; NID:g1504051; PIDN:BAA13232.1; !1PID:g1504052 !'##experimental_source strain inbred line H84, clone CDPK7 CLASSIFICATION #superfamily calcium-dependent protein kinase; calmodulin !1repeat homology; protein kinase homology KEYWORDS ATP; calcium binding; EF hand; phosphotransferase; serine/ !1threonine-specific protein kinase; tandem repeat FEATURE !$89-349 #domain protein kinase homology #label KIN\ !$97-105 #region protein kinase ATP-binding motif\ !$392-424 #domain calmodulin repeat homology #label EF1\ !$428-460 #domain calmodulin repeat homology #label EF2\ !$464-496 #domain calmodulin repeat homology #label EF3\ !$498-530 #domain calmodulin repeat homology #label EF4\ !$120 #active_site Lys #status predicted SUMMARY #length 554 #molecular-weight 61056 #checksum 4641 SEQUENCE /// ENTRY A43713 #type complete TITLE calcium-dependent protein kinase (EC 2.7.1.-) - soybean ORGANISM #formal_name Glycine max #common_name soybean DATE 03-Mar-1993 #sequence_revision 14-Jul-1994 #text_change 11-Jun-1999 ACCESSIONS A43713 REFERENCE A43713 !$#authors Harper, J.F.; Sussman, M.R.; Schaller, G.E.; Putnam-Evans, !1C.; Charbonneau, H.; Harmon, A.C. !$#journal Science (1991) 252:951-954 !$#title A calcium-dependent protein kinase with a regulatory domain !1similar to calmodulin. !$#cross-references MUID:91240279; PMID:1852075 !$#accession A43713 !'##molecule_type mRNA !'##residues 1-508 ##label HAR !'##cross-references EMBL:M64987; NID:g169930; PIDN:AAB00806.1; !1PID:g169931 CLASSIFICATION #superfamily calcium-dependent protein kinase; calmodulin !1repeat homology; protein kinase homology KEYWORDS ATP; calcium binding; EF hand; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$32-292 #domain protein kinase homology #label KIN\ !$40-48 #region protein kinase ATP-binding motif\ !$335-367 #domain calmodulin repeat homology #label EF1\ !$371-403 #domain calmodulin repeat homology #label EF2\ !$407-439 #domain calmodulin repeat homology #label EF3\ !$441-473 #domain calmodulin repeat homology #label EF4\ !$63 #active_site Lys #status predicted SUMMARY #length 508 #molecular-weight 57169 #checksum 1545 SEQUENCE /// ENTRY S71776 #type complete TITLE calcium-dependent protein kinase (EC 2.7.1.-) 9 - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 14-May-1999 #sequence_revision 14-May-1999 #text_change 18-Jun-1999 ACCESSIONS S71776; S71775; S71902; S71196 REFERENCE S71774 !$#authors Hong, Y.; Takano, M.; Liu, C.M.; Gasch, A.; Chye, M.L.; !1Chua, N.H. !$#journal Plant Mol. Biol. (1996) 30:1259-1275 !$#title Expression of three members of the calcium-dependent protein !1kinase gene family in Arabidopsis thaliana. !$#cross-references MUID:96311013; PMID:8704134 !$#accession S71776 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-490 ##label HON !'##cross-references EMBL:U20626 !$#accession S71775 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-490 ##label HOF !'##cross-references EMBL:U20388 REFERENCE S71197 !$#authors Hong, Y.; Takano, M.; Liu, C.M.; Gasch, A.; Chye, M.L.; Tan, !1C.T.; Koh, C.C.; Chua, N.H. !$#submission submitted to the EMBL Data Library, February 1995 !$#description Expression of the calcium-dependent protein kinase gene !1family in Arabidopsis thaliana. !$#accession S71902 !'##molecule_type DNA !'##residues 1-164,'S',166-239,'E',241-300,'KF',303-350,'S',352-490 !1##label HOW !'##cross-references EMBL:U20626; NID:g836945; PIDN:AAA67657.1; !1PID:g836946 REFERENCE S71196 !$#authors Hong, Y.; Takano, M.; Liu, C.M.; Gasch, A.; Chye, M.L.; Tan, !1C.T.; Koh, C.C.; Chua, N.H. !$#submission submitted to the EMBL Data Library, January 1995 !$#description Expression of the calcium dependent protein kinase gene !1family in Arabidopsis thaliana. !$#accession S71196 !'##molecule_type mRNA !'##residues 1-164,'S',166-239,'E',241-300,'KF',303-350,'S',352-490 !1##label HOA !'##cross-references EMBL:U20388; NID:g836937; PIDN:AAA67653.1; !1PID:g836938 GENETICS !$#gene CDPK9 !$#introns 177/1; 225/1; 276/1; 370/3; 445/3 CLASSIFICATION #superfamily calcium-dependent protein kinase; calmodulin !1repeat homology; protein kinase homology KEYWORDS ATP; calcium binding; EF hand; phosphotransferase; serine/ !1threonine-specific protein kinase; tandem repeat FEATURE !$20-280 #domain protein kinase homology #label KIN\ !$28-36 #region protein kinase ATP-binding motif\ !$323-355 #domain calmodulin repeat homology #label EF1\ !$359-391 #domain calmodulin repeat homology #label EF2\ !$395-427 #domain calmodulin repeat homology #label EF3\ !$429-461 #domain calmodulin repeat homology #label EF4\ !$51 #active_site Lys #status predicted SUMMARY #length 490 #molecular-weight 55215 #checksum 1122 SEQUENCE /// ENTRY S46284 #type complete TITLE calcium-dependent protein kinase (EC 2.7.1.-) 2 - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 14-May-1999 #sequence_revision 14-May-1999 #text_change 16-Jun-2000 ACCESSIONS S46284 REFERENCE S46283 !$#authors Urao, T.; Katagiri, T.; Mizoguchi, T.; Yamaguchi-Shinozaki, !1K.; Hayashida, N.; Shinozaki, K. !$#journal Mol. Gen. Genet. (1994) 244:331-340 !$#title Two genes that encode Ca(2+)-dependent protein kinases are !1induced by drought and high-salt stresses in Arabidopsis !1thaliana. !$#cross-references MUID:94359455; PMID:8078458 !$#accession S46284 !'##molecule_type mRNA !'##residues 1-495 ##label URA !'##cross-references EMBL:D21806; NID:g1235717; PIDN:BAA04830.1; !1PID:g604881 GENETICS !$#gene CDPK2 CLASSIFICATION #superfamily calcium-dependent protein kinase; calmodulin !1repeat homology; protein kinase homology KEYWORDS ATP; calcium binding; EF hand; phosphotransferase; serine/ !1threonine-specific protein kinase; tandem repeat FEATURE !$24-284 #domain protein kinase homology #label KIN\ !$32-40 #region protein kinase ATP-binding motif\ !$327-359 #domain calmodulin repeat homology #label EF1\ !$363-395 #domain calmodulin repeat homology #label EF2\ !$399-431 #domain calmodulin repeat homology #label EF3\ !$433-465 #domain calmodulin repeat homology #label EF4\ !$55 #active_site Lys #status predicted SUMMARY #length 495 #molecular-weight 55866 #checksum 3049 SEQUENCE /// ENTRY A49082 #type complete TITLE calcium-dependent protein kinase (EC 2.7.1.-) AK1 - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 14-May-1999 #sequence_revision 14-May-1999 #text_change 11-Jun-1999 ACCESSIONS A49082 REFERENCE A49082 !$#authors Harper, J.F.; Binder, B.M.; Sussman, M.R. !$#journal Biochemistry (1993) 32:3282-3290 !$#title Calcium and lipid regulation of an Arabidopsis protein !1kinase expressed in Escherichia coli. !$#cross-references MUID:93213795; PMID:7916621 !$#contents ecotype Columbia !$#accession A49082 !'##status preliminary !'##molecule_type mRNA !'##residues 1-610 ##label HAR !'##cross-references GB:L14771; NID:g289189; PIDN:AAA32761.1; !1PID:g304105 !'##note sequence extracted from NCBI backbone (NCBIN:128903, !1NCBIP:128904) CLASSIFICATION #superfamily calcium-dependent protein kinase; calmodulin !1repeat homology; protein kinase homology KEYWORDS ATP; calcium binding; EF hand; phosphotransferase; serine/ !1threonine-specific protein kinase; tandem repeat FEATURE !$148-408 #domain protein kinase homology #label KIN\ !$156-164 #region protein kinase ATP-binding motif\ !$451-483 #domain calmodulin repeat homology #label EF1\ !$487-519 #domain calmodulin repeat homology #label EF2\ !$523-555 #domain calmodulin repeat homology #label EF3\ !$557-589 #domain calmodulin repeat homology #label EF4\ !$179 #active_site Lys #status predicted SUMMARY #length 610 #molecular-weight 68253 #checksum 6903 SEQUENCE /// ENTRY T02784 #type complete TITLE calcium-dependent protein kinase (EC 2.7.1.-) - maize (strain W64A) ORGANISM #formal_name Zea mays #common_name maize DATE 14-May-1999 #sequence_revision 14-May-1999 #text_change 16-Jun-2000 ACCESSIONS T02784 REFERENCE Z14736 !$#authors Murillo, I.; Jaeck, E.; Cordero, M.; San Segundo, B. !$#submission submitted to the EMBL Data Library, July 1998 !$#description A calcium-dependent protein kinase possibly involved in !1pathogen defense in maize plants: molecular cloning, !1induction by fungal elicitors and coordinated expression !1with the pathogenesis-related PRms gene. !$#accession T02784 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-639 ##label MUR !'##cross-references EMBL:AJ007366; PIDN:CAA07481.1 !'##experimental_source strain W64A; seed FUNCTION !$#description probably involved in pathogen defense in maize plants CLASSIFICATION #superfamily calcium-dependent protein kinase; calmodulin !1repeat homology; protein kinase homology KEYWORDS ATP; calcium binding; EF hand; phosphotransferase; serine/ !1threonine-specific protein kinase; tandem repeat FEATURE !$151-411 #domain protein kinase homology #label KIN\ !$159-167 #region protein kinase ATP-binding motif\ !$454-486 #domain calmodulin repeat homology #label EF1\ !$490-522 #domain calmodulin repeat homology #label EF2\ !$526-558 #domain calmodulin repeat homology #label EF3\ !$560-592 #domain calmodulin repeat homology #label EF4\ !$182 #active_site Lys #status predicted SUMMARY #length 639 #molecular-weight 69516 #checksum 8709 SEQUENCE /// ENTRY T03024 #type fragment TITLE calcium-dependent protein kinase (EC 2.7.1.-), calmodulin-independent - maize (fragment) ORGANISM #formal_name Zea mays #common_name maize DATE 14-May-1999 #sequence_revision 14-May-1999 #text_change 23-Jul-1999 ACCESSIONS T03024 REFERENCE A58356 !$#authors Estruch, J.J.; Kadwell, S.; Merlin, E.; Crossland, L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1994) 91:8837-8841 !$#title Cloning and characterization of a maize pollen-specific !1calcium-dependent calmodulin-independent protein kinase. !$#cross-references MUID:94377448; PMID:8090732 !$#accession T03024 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-465 ##label EST !'##cross-references EMBL:L27484; NID:g639721; PIDN:AAA61682.1; !1PID:g639722 !'##experimental_source pollen GENETICS !$#gene CDPK !$#introns 210/1; 261/1; 299/3; 355/3; 398/2; 431/3 CLASSIFICATION #superfamily calcium-dependent protein kinase; calmodulin !1repeat homology; protein kinase homology KEYWORDS ATP; calcium binding; EF hand; phosphotransferase; serine/ !1threonine-specific protein kinase; tandem repeat FEATURE !$6-266 #domain protein kinase homology #label KIN\ !$14-22 #region protein kinase ATP-binding motif\ !$309-341 #domain calmodulin repeat homology #label EF1\ !$345-377 #domain calmodulin repeat homology #label EF2\ !$381-413 #domain calmodulin repeat homology #label EF3\ !$415-448 #domain calmodulin repeat homology #label EF4\ !$37 #active_site Lys #status predicted SUMMARY #length 465 #checksum 3586 SEQUENCE /// ENTRY T01989 #type complete TITLE calcium-dependent protein kinase (EC 2.7.1.-) 1 - common tobacco ORGANISM #formal_name Nicotiana tabacum #common_name common tobacco DATE 14-May-1999 #sequence_revision 14-May-1999 #text_change 18-Jun-1999 ACCESSIONS T01989 REFERENCE Z14483 !$#authors Yoon, G.M.; Cho, H.S.; Liu, J.R.; Pai, H.S. !$#submission submitted to the EMBL Data Library, June 1998 !$#description Characterization of NtCDPK1, a calcium-dependent protein !1kinase in Nicotiana tabacum. !$#accession T01989 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-540 ##label YOO !'##cross-references EMBL:AF072908; NID:g3283995; PIDN:AAC25423.1; !1PID:g3283996 GENETICS !$#gene CDPK1 CLASSIFICATION #superfamily calcium-dependent protein kinase; calmodulin !1repeat homology; protein kinase homology KEYWORDS ATP; calcium binding; EF hand; phosphotransferase; serine/ !1threonine-specific protein kinase; tandem repeat FEATURE !$91-351 #domain protein kinase homology #label KIN\ !$99-107 #region protein kinase ATP-binding motif\ !$393-425 #domain calmodulin repeat homology #label EF1\ !$429-461 #domain calmodulin repeat homology #label EF2\ !$465-497 #domain calmodulin repeat homology #label EF3\ !$499-532 #domain calmodulin repeat homology #label EF4\ !$122 #active_site Lys #status predicted SUMMARY #length 540 #molecular-weight 61589 #checksum 2008 SEQUENCE /// ENTRY T02259 #type complete TITLE calcium-dependent protein kinase (EC 2.7.1.-) 2 - maize ORGANISM #formal_name Zea mays #common_name maize DATE 14-May-1999 #sequence_revision 14-May-1999 #text_change 11-Jun-1999 ACCESSIONS T02259 REFERENCE Z14644 !$#authors Patil, S.; Bhatia, A.; Poovaiah, B.W. !$#submission submitted to the EMBL Data Library, June 1995 !$#description Cloning and characterization of CDPK isoforms from corn !1root. !$#accession T02259 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-513 ##label PAT !'##cross-references EMBL:U28376; NID:g886820; PIDN:AAA69507.1; !1PID:g886821 !'##experimental_source strain Merrit; root tip GENETICS !$#gene MZECDPK2 CLASSIFICATION #superfamily calcium-dependent protein kinase; calmodulin !1repeat homology; protein kinase homology KEYWORDS ATP; calcium binding; EF hand; phosphotransferase; serine/ !1threonine-specific protein kinase; tandem repeat FEATURE !$63-323 #domain protein kinase homology #label KIN\ !$71-79 #region protein kinase ATP-binding motif\ !$366-398 #domain calmodulin repeat homology #label EF1\ !$402-434 #domain calmodulin repeat homology #label EF2\ !$438-470 #domain calmodulin repeat homology #label EF3\ !$472-505 #domain calmodulin repeat homology #label EF4\ !$94 #active_site Lys #status predicted SUMMARY #length 513 #molecular-weight 58081 #checksum 1196 SEQUENCE /// ENTRY T02993 #type complete TITLE calcium-dependent protein kinase (EC 2.7.1.-) 9 - maize ORGANISM #formal_name Zea mays #common_name maize DATE 14-May-1999 #sequence_revision 14-May-1999 #text_change 21-Jul-2000 ACCESSIONS T02993 REFERENCE Z14815 !$#authors Saijo, Y.; Hata, S.; Sheen, J.; Izui, K. !$#journal Biochim. Biophys. Acta (1997) 1350:109-114 !$#title CDNA cloning and prokaryotic expression of a maize !1calcium-dependent protein kinase. !$#cross-references MUID:97201047; PMID:9048876 !$#accession T02993 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-531 ##label SAI !'##cross-references EMBL:D85039; NID:g1330253; PIDN:BAA12715.1; !1PID:g1330254 !'##experimental_source strain inbred line H84, clone CDPK9 GENETICS !$#note BAA12715.1 CLASSIFICATION #superfamily calcium-dependent protein kinase; calmodulin !1repeat homology; protein kinase homology KEYWORDS ATP; calcium binding; EF hand; phosphotransferase; serine/ !1threonine-specific protein kinase; tandem repeat FEATURE !$81-341 #domain protein kinase homology #label KIN\ !$89-97 #region protein kinase ATP-binding motif\ !$384-416 #domain calmodulin repeat homology #label EF1\ !$420-452 #domain calmodulin repeat homology #label EF2\ !$456-488 #domain calmodulin repeat homology #label EF3\ !$490-523 #domain calmodulin repeat homology #label EF4\ !$112 #active_site Lys #status predicted SUMMARY #length 531 #molecular-weight 59352 #checksum 6539 SEQUENCE /// ENTRY S56652 #type complete TITLE calcium-dependent protein kinase (EC 2.7.1.-) 2 - rice ORGANISM #formal_name Oryza sativa #common_name rice DATE 14-May-1999 #sequence_revision 14-May-1999 #text_change 11-Jun-1999 ACCESSIONS S56652 REFERENCE S56651 !$#authors Breviario, D.; Morello, L.; Giani, S. !$#journal Plant Mol. Biol. (1995) 27:953-967 !$#title Molecular cloning of two novel rice cDNA sequences encoding !1putative calcium-dependent protein kinases. !$#cross-references MUID:95284352; PMID:7766885 !$#accession S56652 !'##status preliminary !'##molecule_type mRNA !'##residues 1-533 ##label BRE !'##cross-references EMBL:X81394; NID:g587497; PIDN:CAA57157.1; !1PID:g587498 CLASSIFICATION #superfamily calcium-dependent protein kinase; calmodulin !1repeat homology; protein kinase homology KEYWORDS ATP; calcium binding; EF hand; phosphotransferase; serine/ !1threonine-specific protein kinase; tandem repeat FEATURE !$83-343 #domain protein kinase homology #label KIN\ !$91-99 #region protein kinase ATP-binding motif\ !$385-417 #domain calmodulin repeat homology #label EF1\ !$421-453 #domain calmodulin repeat homology #label EF2\ !$457-489 #domain calmodulin repeat homology #label EF3\ !$492-524 #domain calmodulin repeat homology #label EF4\ !$114 #active_site Lys #status predicted SUMMARY #length 533 #molecular-weight 59521 #checksum 8180 SEQUENCE /// ENTRY S46283 #type complete TITLE calcium-dependent protein kinase (EC 2.7.1.-) 1 - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 14-May-1999 #sequence_revision 14-May-1999 #text_change 16-Jun-2000 ACCESSIONS S46283 REFERENCE S46283 !$#authors Urao, T.; Katagiri, T.; Mizoguchi, T.; Yamaguchi-Shinozaki, !1K.; Hayashida, N.; Shinozaki, K. !$#journal Mol. Gen. Genet. (1994) 244:331-340 !$#title Two genes that encode Ca(2+)-dependent protein kinases are !1induced by drought and high-salt stresses in Arabidopsis !1thaliana. !$#cross-references MUID:94359455; PMID:8078458 !$#accession S46283 !'##molecule_type mRNA !'##residues 1-493 ##label URA !'##cross-references EMBL:D21805; NID:g1235716; PIDN:BAA04829.1; !1PID:g604880 GENETICS !$#gene CDPK1 CLASSIFICATION #superfamily calcium-dependent protein kinase; calmodulin !1repeat homology; protein kinase homology KEYWORDS ATP; calcium binding; EF hand; phosphotransferase; serine/ !1threonine-specific protein kinase; tandem repeat FEATURE !$9-269 #domain protein kinase homology #label KIN\ !$17-25 #region protein kinase ATP-binding motif\ !$312-344 #domain calmodulin repeat homology #label EF1\ !$348-380 #domain calmodulin repeat homology #label EF2\ !$384-416 #domain calmodulin repeat homology #label EF3\ !$420-452 #domain calmodulin repeat homology #label EF4\ !$40 #active_site Lys #status predicted SUMMARY #length 493 #molecular-weight 55685 #checksum 7693 SEQUENCE /// ENTRY T02139 #type complete TITLE calcium-dependent protein kinase (EC 2.7.1.-) F8K4.14 - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 14-May-1999 #sequence_revision 14-May-1999 #text_change 18-Jun-1999 ACCESSIONS T02139 REFERENCE Z14574 !$#authors Vysotskaia, V.S.; Schwartz, J.R.; Toriumi, M.; Kwan, A.; Yu, !1G.; Oji, O.; Liu, S.; Li, J.; Araujo, R.; Au, M.; Brendel, !1V.; Buehler, E.; Conway, A.B.; Conway, A.R.; Dewar, K.; !1Feng, J.; Kim, C.; Kurtz, D.; Li, Y.; Palm, C.J.; Shinn, P.; !1Sun, H.; Davis, R.W.; Ecker, J.R.; Federspiel, N.A.; !1Theologis, A. !$#submission submitted to the EMBL Data Library, August 1998 !$#description Arabidopsis thaliana chromosome 1 BAC F8K4 sequence. !$#accession T02139 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-553 ##label VYS !'##cross-references EMBL:AC004392; NID:g3282170; PIDN:AAC28510.1; !1PID:g3367525 GENETICS !$#map_position 1 !$#introns 140/3; 256/1; 304/1; 355/1; 393/3; 449/3; 492/2; 525/3 !$#note F8K4.14 CLASSIFICATION #superfamily calcium-dependent protein kinase; calmodulin !1repeat homology; protein kinase homology KEYWORDS ATP; calcium binding; EF hand; phosphotransferase; serine/ !1threonine-specific protein kinase; tandem repeat FEATURE !$96-359 #domain protein kinase homology #label KIN\ !$104-112 #region protein kinase ATP-binding motif\ !$402-434 #domain calmodulin repeat homology #label EF1\ !$438-470 #domain calmodulin repeat homology #label EF2\ !$474-506 #domain calmodulin repeat homology #label EF3\ !$508-541 #domain calmodulin repeat homology #label EF4\ !$127 #active_site Lys #status predicted SUMMARY #length 553 #molecular-weight 63175 #checksum 1325 SEQUENCE /// ENTRY S56651 #type complete TITLE calcium-dependent protein kinase (EC 2.7.1.-) 11 - rice ORGANISM #formal_name Oryza sativa #common_name rice DATE 14-May-1999 #sequence_revision 14-May-1999 #text_change 11-Jun-1999 ACCESSIONS S56651 REFERENCE S56651 !$#authors Breviario, D.; Morello, L.; Giani, S. !$#journal Plant Mol. Biol. (1995) 27:953-967 !$#title Molecular cloning of two novel rice cDNA sequences encoding !1putative calcium-dependent protein kinases. !$#cross-references MUID:95284352; PMID:7766885 !$#accession S56651 !'##status preliminary !'##molecule_type mRNA !'##residues 1-542 ##label BRE !'##cross-references EMBL:X81393; NID:g587499; PIDN:CAA57156.1; !1PID:g587500 CLASSIFICATION #superfamily calcium-dependent protein kinase; calmodulin !1repeat homology; protein kinase homology KEYWORDS ATP; calcium binding; EF hand; phosphotransferase; serine/ !1threonine-specific protein kinase; tandem repeat FEATURE !$77-337 #domain protein kinase homology #label KIN\ !$85-93 #region protein kinase ATP-binding motif\ !$380-412 #domain calmodulin repeat homology #label EF1\ !$416-448 #domain calmodulin repeat homology #label EF2\ !$452-484 #domain calmodulin repeat homology #label EF3\ !$486-518 #domain calmodulin repeat homology #label EF4\ !$108 #active_site Lys #status predicted SUMMARY #length 542 #molecular-weight 61166 #checksum 4724 SEQUENCE /// ENTRY S71774 #type complete TITLE calcium-dependent protein kinase (EC 2.7.1.-) 6 - Arabidopsis thaliana ALTERNATE_NAMES protein F9D16.120 ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 14-May-1999 #sequence_revision 23-Jul-1999 #text_change 23-Jul-1999 ACCESSIONS T05597; S71774; S71901; S71197 REFERENCE Z15419 !$#authors Bevan, M.; Wedler, H.; Wedler, E.; Wambutt, R.; Hoheisel, !1J.; Mewes, H.W.; Mayer, K.F.X.; Schueller, C. !$#submission submitted to the Protein Sequence Database, February 1999 !$#accession T05597 !'##molecule_type DNA !'##residues 1-529 ##label BEV !'##cross-references EMBL:AL035394 !'##experimental_source cultivar Columbia; BAC clone F9D16 REFERENCE S71774 !$#authors Hong, Y.; Takano, M.; Liu, C.M.; Gasch, A.; Chye, M.L.; !1Chua, N.H. !$#journal Plant Mol. Biol. (1996) 30:1259-1275 !$#title Expression of three members of the calcium-dependent protein !1kinase gene family in Arabidopsis thaliana. !$#cross-references MUID:96311013; PMID:8704134 !$#accession S71774 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-448,'K',450-529 ##label HON !'##cross-references EMBL:U20625 REFERENCE S71197 !$#authors Hong, Y.; Takano, M.; Liu, C.M.; Gasch, A.; Chye, M.L.; Tan, !1C.T.; Koh, C.C.; Chua, N.H. !$#submission submitted to the EMBL Data Library, February 1995 !$#description Expression of the calcium-dependent protein kinase gene !1family in Arabidopsis thaliana. !$#accession S71901 !'##molecule_type DNA !'##residues 1-529 ##label HOA !'##cross-references EMBL:U20625; NID:g836943; PIDN:AAA67656.1; !1PID:g836944 !$#accession S71197 !'##molecule_type mRNA !'##residues 1-529 ##label HOW !'##cross-references EMBL:U20623; NID:g836939; PIDN:AAA67654.1; !1PID:g836940 GENETICS !$#gene CDPK6 !$#map_position 4 !$#introns 137/2; 233/1; 281/1; 332/1; 370/3; 426/3; 469/2; 502/3 !$#note F9D16.120 CLASSIFICATION #superfamily calcium-dependent protein kinase; calmodulin !1repeat homology; protein kinase homology KEYWORDS ATP; calcium binding; EF hand; phosphotransferase; serine/ !1threonine-specific protein kinase; tandem repeat FEATURE !$76-336 #domain protein kinase homology #label KIN\ !$84-92 #region protein kinase ATP-binding motif\ !$379-411 #domain calmodulin repeat homology #label EF1\ !$415-447 #domain calmodulin repeat homology #label EF2\ !$451-483 #domain calmodulin repeat homology #label EF3\ !$485-518 #domain calmodulin repeat homology #label EF4\ !$107 #active_site Lys #status predicted SUMMARY #length 529 #molecular-weight 59336 #checksum 7518 SEQUENCE /// ENTRY S71778 #type complete TITLE calcium-dependent protein kinase (EC 2.7.1.-) 19 - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 14-May-1999 #sequence_revision 14-May-1999 #text_change 18-Jun-1999 ACCESSIONS S71778; S71777; S71198 REFERENCE S71774 !$#authors Hong, Y.; Takano, M.; Liu, C.M.; Gasch, A.; Chye, M.L.; !1Chua, N.H. !$#journal Plant Mol. Biol. (1996) 30:1259-1275 !$#title Expression of three members of the calcium-dependent protein !1kinase gene family in Arabidopsis thaliana. !$#cross-references MUID:96311013; PMID:8704134 !$#accession S71778 !'##molecule_type DNA !'##residues 1-533 ##label HON !'##cross-references EMBL:U20627; NID:g836947; PIDN:AAA67658.1; !1PID:g836948 !$#accession S71777 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 56-533 ##label HOW !'##cross-references EMBL:U20624 GENETICS !$#gene CDPK19 !$#introns 170/3; 211/1; 260/1; 311/1; 349/3; 406/3; 483/3 CLASSIFICATION #superfamily calcium-dependent protein kinase; calmodulin !1repeat homology; protein kinase homology KEYWORDS ATP; calcium binding; EF hand; phosphotransferase; serine/ !1threonine-specific protein kinase; tandem repeat FEATURE !$55-315 #domain protein kinase homology #label KIN\ !$63-71 #region protein kinase ATP-binding motif\ !$358-390 #domain calmodulin repeat homology #label EF1\ !$395-427 #domain calmodulin repeat homology #label EF2\ !$431-463 #domain calmodulin repeat homology #label EF3\ !$467-499 #domain calmodulin repeat homology #label EF4\ !$86 #active_site Lys #status predicted SUMMARY #length 533 #molecular-weight 59940 #checksum 4193 SEQUENCE /// ENTRY S57347 #type complete TITLE Ca2+/calmodulin-dependent protein kinase (EC 2.7.1.123) I - human ALTERNATE_NAMES CaMKI ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S57347 REFERENCE S57347 !$#authors Haribabu, B.; Hook, S.S.; Selbert, M.A.; Goldstein, E.G.; !1Tomhave, E.D.; Edelman, A.M.; Snyderman, R.; Means, A.R. !$#journal EMBO J. (1995) 14:3679-3686 !$#title Human calcium-calmodulin dependent protein kinase I: cDNA !1cloning, domain structure and activation by phosphorylation !1at threonine-177 by calcium-calmodulin dependent protein !1kinase I kinase. !$#cross-references MUID:95369239; PMID:7641687 !$#accession S57347 !'##status preliminary; nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-370 ##label HAR !'##cross-references EMBL:L41816; NID:g790789; PIDN:AAA99458.1; !1PID:g790790 GENETICS !$#gene GDB:CAMK1 !'##cross-references GDB:642249 CLASSIFICATION #superfamily Ca2+/calmodulin-dependent protein kinase I; !1protein kinase homology KEYWORDS ATP; autophosphorylation; calmodulin binding; !1phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$18-276 #domain protein kinase homology #label KIN\ !$26-34 #region protein kinase ATP-binding motif\ !$293-299 #region autoinhibitory\ !$302-314 #region calmodulin binding\ !$177 #binding_site phosphate (Thr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 370 #molecular-weight 41337 #checksum 6801 SEQUENCE /// ENTRY S50193 #type complete TITLE Ca2+/calmodulin-dependent protein kinase (EC 2.7.1.123) I - rat ALTERNATE_NAMES CaMKI ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S50193; A49682; A46038 REFERENCE S50193 !$#authors Cho, F.S.; Phillips, K.S.; Bogucki, B.; Weaver, T.E. !$#journal Biochim. Biophys. Acta (1994) 1224:156-160 !$#title Characterization of a rat cDNA clone encoding calcium/ !1calmodulin-dependent protein kinase I. !$#cross-references MUID:95035115; PMID:7948038 !$#accession S50193 !'##status preliminary !'##molecule_type mRNA !'##residues 1-374 ##label CHO !'##cross-references EMBL:L26288; NID:g439613; PIDN:AAA66944.1; !1PID:g439614 REFERENCE A49682 !$#authors Picciotto, M.R.; Czernik, A.J.; Nairn, A.C. !$#journal J. Biol. Chem. (1993) 268:26512-26521 !$#title Calcium/calmodulin-dependent protein kinase I. cDNA cloning !1and identification of autophosphorylation site. !$#cross-references MUID:94075341; PMID:8253780 !$#accession A49682 !'##status preliminary !'##molecule_type mRNA !'##residues 1-111,'G',113-117,'R',119-308,'R',310-322,'HQPG',327,'T', !1329,'TDS' ##label PIC !'##cross-references GB:L24907; NID:g406112; PIDN:AAA19670.1; !1PID:g406113 REFERENCE A46038 !$#authors Mochizuki, H.; Ito, T.; Hidaka, H. !$#journal J. Biol. Chem. (1993) 268:9143-9147 !$#title Purification and characterization of Ca2+/ !1calmodulin-dependent protein kinase V from rat cerebrum. !$#cross-references MUID:93232082; PMID:8386178 !$#accession A46038 !'##status preliminary !'##molecule_type protein !'##residues 12-36,'T' ##label MOC !'##experimental_source cerebrum !'##note sequence extracted from NCBI backbone (NCBIP:129927) CLASSIFICATION #superfamily Ca2+/calmodulin-dependent protein kinase I; !1protein kinase homology KEYWORDS ATP; autophosphorylation; calmodulin binding; !1phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$18-276 #domain protein kinase homology #label KIN\ !$26-34 #region protein kinase ATP-binding motif\ !$293-299 #region autoinhibitory\ !$302-314 #region calmodulin binding\ !$177 #binding_site phosphate (Thr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 374 #molecular-weight 41638 #checksum 5948 SEQUENCE /// ENTRY S04365 #type complete TITLE Ca2+/calmodulin-dependent protein kinase (EC 2.7.1.123) II alpha chain - mouse ALTERNATE_NAMES CaMKII alpha chain ORGANISM #formal_name Mus musculus #common_name house mouse DATE 04-Dec-1992 #sequence_revision 04-Dec-1992 #text_change 11-Jun-1999 ACCESSIONS S04365; S05279 REFERENCE S04365 !$#authors Hanley, R.M.; Payne, M.E.; Cruzalegui, F.; Christenson, !1M.A.; Means, A.R. !$#journal Nucleic Acids Res. (1989) 17:3992 !$#title Sequence of the cDNA for the alpha subunit of calmodulin !1kinase II from mouse brain. !$#cross-references MUID:89282416; PMID:2543961 !$#accession S04365 !'##molecule_type mRNA !'##residues 1-478 ##label HAN !'##cross-references EMBL:X14836 REFERENCE S05279 !$#authors Hanley, R.M. !$#submission submitted to the EMBL Data Library, March 1989 !$#accession S05279 !'##molecule_type mRNA !'##residues 1-39,'P',41-271,'S',273-478 ##label HA2 !'##cross-references EMBL:X14836; NID:g50416; PIDN:CAA32946.1; !1PID:g50417 COMPLEX heteromultimer composed of 10-12 chains (alpha, beta, gamma, !1delta) generally in proportion to their concentration in the !1cell FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP !$#note acts on a variety of intracellular proteins; alpha and beta !1chains are expressed in nervous tissue CLASSIFICATION #superfamily Ca2+/calmodulin-dependent protein kinase II; !1protein kinase homology KEYWORDS ATP; autophosphorylation; calmodulin binding; !1phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$11-271 #domain protein kinase homology #label KIN\ !$19-27 #region protein kinase ATP-binding motif\ !$286-310 #region calmodulin binding #status predicted\ !$42,60,135,137 #active_site Lys, Glu, Asp, Lys #status predicted\ !$286 #binding_site phosphate (Thr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 478 #molecular-weight 54325 #checksum 9461 SEQUENCE /// ENTRY A30355 #type complete TITLE Ca2+/calmodulin-dependent protein kinase (EC 2.7.1.123) II alpha chain - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 22-Jan-1993 #sequence_revision 22-Jan-1993 #text_change 11-Jun-1999 ACCESSIONS A30355; A43611; JH0178; A31235; S29078; I59161 REFERENCE A30355 !$#authors Lin, C.R.; Kapiloff, M.S.; Durgerian, S.; Tatemoto, K.; !1Russo, A.F.; Hanson, P.; Schulman, H.; Rosenfeld, M.G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:5962-5966 !$#title Molecular cloning of a brain-specific calcium/ !1calmodulin-dependent protein kinase. !$#cross-references MUID:87289722; PMID:3475713 !$#accession A30355 !'##molecule_type mRNA !'##residues 1-478 ##label LIN !'##cross-references GB:J02942; NID:g206178; PIDN:AAA41870.1; !1PID:g206179 REFERENCE A43611 !$#authors Hanley, R.M.; Means, A.R.; Ono, T.; Kemp, B.E.; Burgin, !1K.E.; Waxham, N.; Kelly, P.T. !$#journal Science (1987) 237:293-297 !$#title Functional analysis of a complementary DNA for the !150-kilodalton subunit of calmodulin kinase II. !$#cross-references MUID:87263392; PMID:3037704 !$#accession A43611 !'##molecule_type mRNA !'##residues 132-327 ##label HAN !'##cross-references GB:M16960 REFERENCE JH0178 !$#authors Bulleit, R.F.; Bennett, M.K.; Molloy, S.S.; Hurley, J.B.; !1Kennedy, M.B. !$#journal Neuron (1988) 1:63-72 !$#title Conserved and variable regions in the subunits of brain type !1II Ca2+/calmodulin-dependent protein kinase. !$#cross-references MUID:90166481; PMID:2856087 !$#accession JH0178 !'##molecule_type mRNA !'##residues 1-478 ##label BUL !'##experimental_source brain REFERENCE A31235 !$#authors Thiel, G.; Czernik, A.J.; Gorelick, F.; Nairn, A.C.; !1Greengard, P. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:6337-6341 !$#title Ca(2)+/calmodulin-dependent protein kinase II: !1identification of threonine-286 as the autophosphorylation !1site in the alpha-subunit associated with the generation of !1Ca(2)+-independent activity. !$#cross-references MUID:88320438; PMID:2842767 !$#accession A31235 !'##molecule_type protein !'##residues 'X',283-288,'X',290-299 ##label THI REFERENCE S29078 !$#authors Benfenati, F.; Valtorta, F.; Rubenstein, J.L.; Gorelick, !1F.S.; Greengard, P.; Czernik, A.J. !$#journal Nature (1992) 359:417-420 !$#title Synaptic vesicle-associated Ca(2+)/calmodulin-dependent !1protein kinase II is a binding protein for synapsin I. !$#cross-references MUID:93024899; PMID:1328883 !$#accession S29078 !'##status preliminary !'##molecule_type protein !'##residues 231-236,238-246,'X',461,'X',463-474,'X',476 ##label BEN REFERENCE I59161 !$#authors Sunyer, T.; Sahyoun, N. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:278-282 !$#title Sequence analysis and DNA-protein interactions within the 5' !1flanking region of the Ca-2+/calmodulin-dependent protein !1kinase II alpha-subunit gene. !$#cross-references MUID:90115857; PMID:2153289 !$#accession I59161 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-6 ##label RES !'##cross-references GB:M29699; NID:g203208; PIDN:AAA40841.1; !1PID:g203209 !'##experimental_source brain COMPLEX heteromultimer composed of 10-12 chains (alpha, beta, gamma, !1delta) generally in proportion to their concentration in the !1cell FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP !$#note acts on a variety of intracellular proteins; alpha and beta !1chains are expressed in nervous tissue CLASSIFICATION #superfamily Ca2+/calmodulin-dependent protein kinase II; !1protein kinase homology KEYWORDS ATP; autophosphorylation; calmodulin binding; !1phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$11-271 #domain protein kinase homology #label KIN\ !$19-27 #region protein kinase ATP-binding motif\ !$286-310 #region calmodulin binding #status predicted\ !$42,60,135,137 #active_site Lys, Glu, Asp, Lys #status predicted\ !$286 #binding_site phosphate (Thr) (covalent) (by !8autophosphorylation) #status predicted\ !$314 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 478 #molecular-weight 54114 #checksum 8207 SEQUENCE /// ENTRY B46619 #type complete TITLE Ca2+/calmodulin-dependent protein kinase (EC 2.7.1.123) II gamma chain, splice form B - human CONTAINS Ca2+/calmodulin-dependent protein kinase II gamma chain, splice form C ORGANISM #formal_name Homo sapiens #common_name man DATE 21-Sep-1993 #sequence_revision 18-Nov-1994 #text_change 01-Dec-2000 ACCESSIONS B46619; A46619; JC5637 REFERENCE A46619 !$#authors Nghiem, P.; Saati, S.M.; Martens, C.L.; Gardner, P.; !1Schulman, H. !$#journal J. Biol. Chem. (1993) 268:5471-5479 !$#title Cloning and analysis of two new isoforms of multifunctional !1Ca2+/calmodulin-dependent protein kinase. Expression in !1multiple human tissues. !$#cross-references MUID:93194838; PMID:8449910 !$#accession B46619 !'##molecule_type mRNA !'##residues 1-518 ##label NGH1 !'##cross-references GB:L07044; NID:g291894 !'##experimental_source Jurkat T cells !'##note sequence extracted from NCBI backbone (NCBIN:127699, !1NCBIP:127703) !$#accession A46619 !'##molecule_type mRNA !'##residues 1-330,354-518 ##label NGH2 !'##cross-references GB:L07043; NID:g291893 !'##experimental_source Jurkat T cells !'##note the sequence in GenBank entry HUMCCDPKA, release 103, !1(PID:g2204281) incorrectly translates an internal CTG codon !1for Leu as an initiator and fails to include the full !1published sequence !'##note sequence extracted from NCBI backbone (NCBIN:127696, !1NCBIP:127698) REFERENCE JC5636 !$#authors Breen, M.A.; Ashcroft, S.J.H. !$#journal Biochem. Biophys. Res. Commun. (1997) 236:473-478 !$#title Human islets of Langerhans express multiple isoforms of !1calcium/calmodulin-dependent protein kinase II. !$#cross-references MUID:97382459; PMID:9240463 !$#accession JC5637 !'##molecule_type mRNA !'##residues 1-384,386-518 ##label BRE !'##cross-references GB:U66063 !'##experimental_source islet COMMENT This enzyme is a ubiquitous serine/threonine protein kinase. !1It plays a role in glucose-stimulated insulin release. GENETICS !$#gene GDB:CAMKG !'##cross-references GDB:138469 !$#map_position 10q22-10q22 COMPLEX heteromultimer composed of 10-12 alpha, beta, gamma, and !1delta chains generally in proportion to their concentration !1in the cell FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP !$#note acts on a variety of intracellular proteins; gamma and delta !1chains are expressed in most tissues CLASSIFICATION #superfamily Ca2+/calmodulin-dependent protein kinase II; !1protein kinase homology KEYWORDS ATP; autophosphorylation; calmodulin binding; !1phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$12-272 #domain protein kinase homology #label KIN\ !$20-28 #region protein kinase ATP-binding motif\ !$287-311 #region calmodulin binding #status predicted\ !$43,61,136,138 #active_site Lys, Glu, Asp, Lys #status predicted\ !$287 #binding_site phosphate (Thr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 518 #molecular-weight 58365 #checksum 5043 SEQUENCE /// ENTRY S43845 #type complete TITLE Ca2+/calmodulin-dependent protein kinase (EC 2.7.1.123) II gamma-b chain - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 20-Oct-1994 #sequence_revision 10-Nov-1995 #text_change 28-May-1999 ACCESSIONS S43845 REFERENCE S43845 !$#authors Zhou, Z.L.; Ikebe, M. !$#journal Biochem. J. (1994) 299:489-495 !$#title New isoforms of Ca(2+)/calmodulin-dependent protein kinase !1II in smooth muscle. !$#cross-references MUID:94226614; PMID:8172610 !$#accession S43845 !'##molecule_type mRNA !'##residues 1-518 ##label ZHO !'##cross-references GB:S71570; NID:g560650; PIDN:AAB30670.1; !1PID:g560651 COMPLEX heteromultimer composed of 10-12 chains (alpha, beta, gamma, !1delta) generally in proportion to their concentration in the !1cell FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP !$#note acts on a variety of intracellular proteins; gamma and delta !1chains are expressed in most tissues CLASSIFICATION #superfamily Ca2+/calmodulin-dependent protein kinase II; !1protein kinase homology KEYWORDS ATP; autophosphorylation; calmodulin binding; !1phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$12-272 #domain protein kinase homology #label KIN\ !$20-28 #region protein kinase ATP-binding motif\ !$287-311 #region calmodulin binding #status predicted\ !$43,61,136,138 #active_site Lys, Glu, Asp, Lys #status predicted\ !$287 #binding_site phosphate (Thr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 518 #molecular-weight 58678 #checksum 4594 SEQUENCE /// ENTRY A31908 #type complete TITLE Ca2+/calmodulin-dependent protein kinase (EC 2.7.1.123) II gamma-a chain - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 21-May-1990 #sequence_revision 21-May-1990 #text_change 11-Jun-1999 ACCESSIONS A31908 REFERENCE A31908 !$#authors Tobimatsu, T.; Kameshita, I.; Fujisawa, H. !$#journal J. Biol. Chem. (1988) 263:16082-16086 !$#title Molecular cloning of the cDNA encoding the third polypeptide !1(gamma) of brain calmodulin-dependent protein kinase II. !$#cross-references MUID:89034067; PMID:2846534 !$#accession A31908 !'##molecule_type mRNA !'##residues 1-527 ##label TOB !'##cross-references GB:J04063; NID:g206151; PIDN:AAA41857.1; !1PID:g206152 COMPLEX heteromultimer composed of 10-12 chains (alpha, beta, gamma, !1delta) generally in proportion to their concentration in the !1cell FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP !$#note acts on a variety of intracellular proteins; gamma and delta !1chains are expressed in most tissues CLASSIFICATION #superfamily Ca2+/calmodulin-dependent protein kinase II; !1protein kinase homology KEYWORDS ATP; autophosphorylation; calmodulin binding; !1phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$12-272 #domain protein kinase homology #label KIN\ !$20-28 #region protein kinase ATP-binding motif\ !$287-311 #region calmodulin binding #status predicted\ !$43,61,136,138 #active_site Lys, Glu, Asp, Lys #status predicted\ !$287 #binding_site phosphate (Thr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 527 #molecular-weight 59038 #checksum 7832 SEQUENCE /// ENTRY A45025 #type complete TITLE Ca2+/calmodulin-dependent protein kinase (EC 2.7.1.123) II beta chain - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Jun-1993 #sequence_revision 18-Nov-1994 #text_change 11-Jun-1999 ACCESSIONS A45025; S18915 REFERENCE A45025 !$#authors Karls, U.; Muller, U.; Gilbert, D.J.; Copeland, N.G.; !1Jenkins, N.A.; Harbers, K. !$#journal Mol. Cell. Biol. (1992) 12:3644-3652 !$#title Structure, expression, and chromosome location of the gene !1for the beta subunit of brain-specific Ca2+/ !1calmodulin-dependent protein kinase II identified by !1transgene integration in an embryonic lethal mouse mutant. !$#cross-references MUID:92334366; PMID:1321343 !$#accession A45025 !'##status preliminary !'##molecule_type mRNA !'##residues 1-542 ##label KAR !'##cross-references GB:X63615; GB:S40077; NID:g50275; PIDN:CAA45160.1; !1PID:g50276 !'##experimental_source BALB/c, brain !'##note sequence inconsistent with the nucleotide translation !'##note sequence extracted from NCBI backbone (NCBIN:108750, !1NCBIP:108751) REFERENCE S18915 !$#authors Karls, U.; Mueller, U.; Gilbert, D.J.; Copeland, N.G.; !1Jenkins, N.A.; Harbers, K. !$#submission submitted to the EMBL Data Library, December 1991 !$#accession S18915 !'##status preliminary !'##molecule_type mRNA !'##residues 1-542 ##label KA2 !'##cross-references EMBL:X63615; NID:g50275; PIDN:CAA45160.1; !1PID:g50276 COMPLEX heteromultimer composed of 10-12 chains (alpha, beta, gamma, !1delta) generally in proportion to their concentration in the !1cell FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP !$#note acts on a variety of intracellular proteins; alpha and beta !1chains are expressed in nervous tissue CLASSIFICATION #superfamily Ca2+/calmodulin-dependent protein kinase II; !1protein kinase homology KEYWORDS ATP; autophosphorylation; calmodulin binding; !1phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$12-272 #domain protein kinase homology #label KIN\ !$20-28 #region protein kinase ATP-binding motif\ !$287-311 #region calmodulin binding #status predicted\ !$43,61,136,138 #active_site Lys, Glu, Asp, Lys #status predicted\ !$287 #binding_site phosphate (Thr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 542 #molecular-weight 60474 #checksum 3110 SEQUENCE /// ENTRY A26464 #type complete TITLE Ca2+/calmodulin-dependent protein kinase (EC 2.7.1.123) II beta chain - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 11-Jun-1999 ACCESSIONS A26464 REFERENCE A26464 !$#authors Bennett, M.K.; Kennedy, M.B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:1794-1798 !$#title Deduced primary structure of the beta-subunit of brain type !1II Ca(2)+/calmodulin-dependent protein kinase determined by !1molecular cloning. !$#cross-references MUID:87175563; PMID:3470758 !$#accession A26464 !'##molecule_type mRNA !'##residues 1-542 ##label BEN !'##cross-references GB:M16112; NID:g206170; PIDN:AAA41866.1; !1PID:g206171 COMPLEX heteromultimer composed of 10-12 chains (alpha, beta, gamma, !1delta) generally in proportion to their concentration in the !1cell FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP !$#note acts on a variety of intracellular proteins; alpha and beta !1chains are expressed in nervous tissue CLASSIFICATION #superfamily Ca2+/calmodulin-dependent protein kinase II; !1protein kinase homology KEYWORDS ATP; autophosphorylation; calmodulin binding; !1phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$12-272 #domain protein kinase homology #label KIN\ !$20-28 #region protein kinase ATP-binding motif\ !$287-311 #region calmodulin binding #status predicted\ !$43,61,136,138 #active_site Lys, Glu, Asp, Lys #status predicted\ !$287 #binding_site phosphate (Thr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 542 #molecular-weight 60401 #checksum 3073 SEQUENCE /// ENTRY A34366 #type complete TITLE Ca2+/calmodulin-dependent protein kinase (EC 2.7.1.123) II delta chain - rat CONTAINS Ca2+/calmodulin-dependent protein kinase II delta chain, various splice forms ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 08-Jun-1990 #sequence_revision 08-Jun-1990 #text_change 11-Jun-1999 ACCESSIONS A34366; S39023; S39024; S39025; S39026; S39027; C47170 REFERENCE A34366 !$#authors Tobimatsu, T.; Fujisawa, H. !$#journal J. Biol. Chem. (1989) 264:17907-17912 !$#title Tissue-specific expression of four types of rat !1calmodulin-dependent protein kinase II mRNAs. !$#cross-references MUID:90036861; PMID:2553697 !$#accession A34366 !'##status preliminary !'##molecule_type mRNA !'##residues 1-533 ##label TOB !'##cross-references GB:J05072; NID:g203266; PIDN:AAA40866.1; !1PID:g203267 REFERENCE S39023 !$#authors Mayer, P.; Moehlig, M.; Schatz, H.; Pfeiffer, A. !$#journal FEBS Lett. (1993) 333:315-318 !$#title New isoforms of multifunctional calcium/calmodulin-dependent !1protein kinase II. !$#cross-references MUID:94039784; PMID:8224201 !$#accession S39023 !'##molecule_type mRNA !'##residues 318-328,363-371,504-533 ##label MAY !$#accession S39024 !'##molecule_type mRNA !'##residues 318-371,504-511,'N' ##label MA2 !$#accession S39025 !'##molecule_type mRNA !'##residues 318-328,363-371,504-511,'N' ##label MA3 !$#accession S39026 !'##molecule_type mRNA !'##residues 318-349,364-371,504-533 ##label MA4 !$#accession S39027 !'##status preliminary !'##molecule_type mRNA !'##residues 318-349,364-371,504-511,'N' ##label MA5 REFERENCE A47170 !$#authors Schworer, C.M.; Rothblum, L.I.; Thekkumkara, T.J.; Singer, !1H.A. !$#journal J. Biol. Chem. (1993) 268:14443-14449 !$#title Identification of novel isoforms of the delta subunit of !1Ca2+/calmodulin-dependent protein kinase II. Differential !1expression in rat brain and aorta. !$#cross-references MUID:93300844; PMID:8390994 !$#accession C47170 !'##status preliminary !'##molecule_type mRNA !'##residues 314-349,364-368 ##label SCH !'##cross-references GB:L13408; NID:g349086 !'##experimental_source skeletal muscle !'##note sequence extracted from NCBI backbone (NCBIN:134450, !1NCBIP:134453) COMPLEX heteromultimer composed of 10-12 alpha, beta, gamma, and !1delta chains generally in proportion to their concentration !1in the cell FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP !$#note acts on a variety of intracellular proteins; gamma and delta !1chains are expressed in most tissues CLASSIFICATION #superfamily Ca2+/calmodulin-dependent protein kinase II; !1protein kinase homology KEYWORDS ATP; autophosphorylation; calmodulin binding; !1phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$12-272 #domain protein kinase homology #label KIN\ !$20-28 #region protein kinase ATP-binding motif\ !$287-311 #region calmodulin binding #status predicted\ !$43,61,136,138 #active_site Lys, Glu, Asp, Lys #status predicted\ !$287 #binding_site phosphate (Thr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 533 #molecular-weight 60080 #checksum 7220 SEQUENCE /// ENTRY JU0270 #type complete TITLE Ca2+/calmodulin-dependent protein kinase (EC 2.7.1.123) II alpha chain - fruit fly (Drosophila melanogaster) CONTAINS Ca2+/calmodulin-dependent protein kinase II alpha chain, 55.5K splice form; Ca2+/calmodulin-dependent protein kinase II alpha chain, 58.4K splice form ORGANISM #formal_name Drosophila melanogaster DATE 30-Jun-1992 #sequence_revision 14-May-1999 #text_change 14-May-1999 ACCESSIONS C44412; A44412; JU0270 REFERENCE A44412 !$#authors Ohsako, S.; Nishida, Y.; Ryo, H.; Yamauchi, T. !$#journal J. Biol. Chem. (1993) 268:2052-2062 !$#title Molecular characterization and expression of the Drosophila !1Ca2+/calmodulin-dependent protein kinase II gene. !1Identification of four forms of the enzyme generated from a !1single gene by alternative splicing. !$#cross-references MUID:93131962; PMID:8380587 !$#accession C44412 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-218,'HD',221-516 ##label OHS1 !'##note sequence extracted from NCBI backbone (NCBIP:124126) !$#accession A44412 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-218,'HD',221-346,373-516 ##label OHS2 !'##experimental_source head !'##note sequence extracted from NCBI backbone (NCBIP:123124) REFERENCE JU0270 !$#authors Cho, K.O.; Wall, J.B.; Pugh, P.C.; Ito, M.; Mueller, S.A.; !1Kennedy, M.B. !$#journal Neuron (1991) 7:439-450 !$#title The alpha subunit of type II Ca2+/calmodulin-dependent !1protein kinase is highly conserved in Drosophila. !$#cross-references MUID:92000690; PMID:1910789 !$#accession JU0270 !'##molecule_type mRNA !'##residues 1-346,373-516 ##label CHO COMMENT For another splice form see PIR:D44412. GENETICS !$#gene FlyBase:CaMKII !'##cross-references FlyBase:FBgn0004624 !$#map_position 4 102E/F COMPLEX heteromultimer composed of 10-12 chains (alpha, beta, gamma, !1delta) generally in proportion to their concentration in the !1cell FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP !$#note acts on a variety of intracellular proteins; alpha and beta !1chains are expressed in nervous tissue CLASSIFICATION #superfamily Ca2+/calmodulin-dependent protein kinase II; !1protein kinase homology KEYWORDS alternative splicing; ATP; autophosphorylation; calmodulin !1binding; phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$1-516 #product Ca2+/calmodulin-dependent protein kinase II !8alpha chain, 58.4K splice form #status predicted !8#label SF1\ !$1-346,373-516 #product Ca2+/calmodulin-dependent protein kinase II !8alpha chain, 55.5K splice form #status predicted !8#label SF2\ !$12-272 #domain protein kinase homology #label KIN\ !$20-28 #region protein kinase ATP-binding motif\ !$287-311 #region calmodulin binding #status predicted\ !$43,61,136,138 #active_site Lys, Glu, Asp, Lys #status predicted\ !$287,306 #binding_site phosphate (Thr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 516 #molecular-weight 58386 #checksum 5860 SEQUENCE /// ENTRY A53036 #type complete TITLE Ca2+/calmodulin-dependent protein kinase (EC 2.7.1.123) IV - human ALTERNATE_NAMES Ca2+/calmodulin-dependent protein kinase Gr; CaM-kinase IV ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A53036; JC2261; I53768 REFERENCE A53036 !$#authors Mosialos, G.; Hanissian, S.H.; Jawahar, S.; Vara, L.; Kieff, !1E.; Chatila, T.A. !$#journal J. Virol. (1994) 68:1697-1705 !$#title A Ca(2+)/calmodulin-dependent protein kinase, CaM kinase-Gr, !1expressed after transformation of primary human B !1lymphocytes by Epstein-Barr virus (EBV) is induced by the !1EBV oncogene LMP1. !$#cross-references MUID:94149862; PMID:8107230 !$#accession A53036 !'##status preliminary !'##molecule_type mRNA !'##residues 1-473 ##label MSO !'##cross-references GB:L24959; NID:g407005; PIDN:AAA18251.1; !1PID:g407006 REFERENCE JC2261 !$#authors Kitani, T.; Okuno, S.; Fujisawa, H. !$#journal J. Biochem. (1994) 115:637-640 !$#title cDNA cloning and expression of human calmodulin-dependent !1protein kinase IV. !$#cross-references MUID:94375404; PMID:8089075 !$#accession JC2261 !'##molecule_type mRNA !'##residues 1-473 ##label KIT !'##cross-references GB:D30742; NID:g487908; PIDN:BAA06403.1; !1PID:g871845 REFERENCE I53768 !$#authors Bland, M.M.; Monroe, R.S.; Ohmstede, C. !$#journal Gene (1994) 142:191-197 !$#title The cDNA sequence and characterization of the Ca2+/ !1calmodulin-dependent protein kinase-Gr from human brain and !1thymus. !$#cross-references MUID:94252566; PMID:8194751 !$#accession I53768 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-473 ##label RES !'##cross-references GB:L17000; NID:g306478; PIDN:AAA35639.1; !1PID:g306479 COMMENT This protein is a Ca2+-responsive multifunctional protein !1kinase, which occurs abundantly in the brain and thymus and !1plays important roles in the functioning of Ca2+ in the !1central nervous system and in the immune system. GENETICS !$#gene GDB:ILK !'##cross-references GDB:6155815; OMIM:602366 !$#map_position 11p15.5-11p15.4 CLASSIFICATION #superfamily Ca2+/calmodulin-dependent protein kinase; !1protein kinase homology KEYWORDS ATP; calcium binding; calmodulin binding; phosphoprotein; !1phosphotransferase; serine/threonine-specific protein kinase FEATURE !$44-300 #domain protein kinase homology #label KIN\ !$52-60 #region protein kinase ATP-binding motif\ !$320-329 #region calmodulin binding #status predicted\ !$8,12,15 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 473 #molecular-weight 51925 #checksum 7953 SEQUENCE /// ENTRY TVRTC4 #type complete TITLE Ca2+/calmodulin-dependent protein kinase (EC 2.7.1.123) IV - rat ALTERNATE_NAMES Ca2+/calmodulin-dependent protein kinase Gr CONTAINS calspermin ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 11-Jun-1999 ACCESSIONS A41103; A41237; A32865; A41250; A32035; A60255; I53706 REFERENCE A41103 !$#authors Ohmstede, C.A.; Bland, M.M.; Merrill, B.M.; Sahyoun, N. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:5784-5788 !$#title Relationship of genes encoding Ca(2+)/calmodulin-dependent !1protein kinase Gr and calspermin: a gene within a gene. !$#cross-references MUID:91288548; PMID:1648230 !$#accession A41103 !'##molecule_type DNA !'##residues 47-141,'NE',144-474 ##label OH1 !'##cross-references GB:M74488; NID:g203219; PIDN:AAA40845.1; !1PID:g203220 !'##note this sequence has been revised in reference A41237 !'##note part of this sequence was confirmed by sequencing of cDNA to !1mRNA REFERENCE A41237 !$#authors Ohmstede, C.A.; Bland, M.M.; Merrill, B.M.; Sahyoun, N. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:9375 !$#accession A41237 !'##molecule_type DNA !'##residues 142-143 ##label OH2 !'##cross-references GB:M63334 !'##note this is a revision to the sequence from reference A41103 REFERENCE A32865 !$#authors Ohmstede, C.A.; Jensen, K.F.; Sahyoun, N.E. !$#journal J. Biol. Chem. (1989) 264:5866-5875 !$#title Ca(2+)/calmodulin-dependent protein kinase enriched in !1cerebellar granule cells. Identification of a novel neuronal !1calmodulin-dependent protein kinase. !$#cross-references MUID:89174647; PMID:2538431 !$#accession A32865 !'##molecule_type mRNA !'##residues 250-474 ##label OH3 !'##cross-references GB:J04600; NID:g206172; PIDN:AAA41867.1; !1PID:g206173 REFERENCE A41250 !$#authors Means, A.R.; Cruzalegui, F.; LeMagueresse, B.; Needleman, !1D.S.; Slaughter, G.R.; Ono, T. !$#journal Mol. Cell. Biol. (1991) 11:3960-3971 !$#title A novel Ca(2+)/calmodulin-dependent protein kinase and a !1male germ cell-specific calmodulin-binding protein are !1derived from the same gene. !$#cross-references MUID:91304387; PMID:1649385 !$#accession A41250 !'##molecule_type mRNA !'##residues 1-371,'M',373-408,'Q',410-474 ##label MEA !'##cross-references GB:M64757 REFERENCE A32035 !$#authors Ono, T.; Slaughter, G.R.; Cook, R.G.; Means, A.R. !$#journal J. Biol. Chem. (1989) 264:2081-2087 !$#title Molecular cloning sequence and distribution of rat !1calspermin, a high affinity calmodulin-binding protein. !$#cross-references MUID:89123272; PMID:2914893 !$#accession A32035 !'##molecule_type mRNA !'##residues 306-371,'M',373-474 ##label ON1 !'##cross-references GB:J04446; NID:g203642; PIDN:AAA40990.1; !1PID:g203643 REFERENCE A60255 !$#authors Ono, T.; Means, A.R. !$#journal Adv. Exp. Med. Biol. (1989) 255:263-268 !$#title Calspermin is a testis specific calmodulin-binding protein !1closely related to Ca(2+)/calmodulin-dependent protein !1kinases. !$#cross-references MUID:90144189; PMID:2618865 !$#accession A60255 !'##molecule_type protein !'##residues 335-363 ##label ON2 !'##note the amino end of calspermin was blocked REFERENCE I53706 !$#authors Bland, M.M. !$#journal Gene (1993) 137:351-352 !$#title Identification of alternate 5' untranslated regions in the !1gene encoding Ca2+/calmodulin-dependent kinase-G1. !$#cross-references MUID:94131312; PMID:8299971 !$#accession I53706 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-37 ##label RES !'##cross-references GB:L16999; NID:g310086; PIDN:AAA17443.1; !1PID:g310087 COMMENT Ca2+/calmodulin-dependent protein kinase IV is enriched in !1cerebellar granule cells. Calspermin is derived from the !1same gene by alternative splicing and is a !1calmodulin-binding protein found in sperm cells. CLASSIFICATION #superfamily Ca2+/calmodulin-dependent protein kinase; !1protein kinase homology KEYWORDS alternative splicing; ATP; calmodulin binding; !1phosphotransferase; serine/threonine-specific protein kinase FEATURE !$40-296 #domain protein kinase homology #label KIN\ !$48-57 #region protein kinase ATP-binding motif\ !$306-474 #product calspermin #status predicted #label CSP\ !$318-337 #region calmodulin binding #status predicted\ !$71 #active_site Lys #status predicted SUMMARY #length 474 #molecular-weight 53133 #checksum 5067 SEQUENCE /// ENTRY S17656 #type complete TITLE Ca2+/calmodulin-dependent protein kinase (EC 2.7.1.123) IV - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S17656; A29878; I49571 REFERENCE S17656 !$#authors Jones, D.A.; Glod, J.; Wilson-Shaw, D.; Hahn, W.E.; Sikela, !1J.M. !$#journal FEBS Lett. (1991) 289:105-109 !$#title cDNA sequence and differential expression of the mouse Ca !1(2+)/calmodulin-dependent protein kinase IV gene. !$#cross-references MUID:91372388; PMID:1893997 !$#accession S17656 !'##molecule_type mRNA !'##residues 1-469 ##label JON !'##cross-references EMBL:X58995; NID:g50366; PIDN:CAA41741.1; !1PID:g50367 REFERENCE A29878 !$#authors Sikela, J.M.; Hahn, W.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:3038-3042 !$#title Screening an expression library with a ligand probe: !1isolation and sequence of a cDNA corresponding to a brain !1calmodulin-binding protein. !$#cross-references MUID:87204263; PMID:3033675 !$#accession A29878 !'##molecule_type mRNA !'##residues 315-469 ##label SIK !'##cross-references GB:M16206; NID:g200360; PIDN:AAA39933.1; !1PID:g387512 REFERENCE I49571 !$#authors Sikela, J.M.; Law, M.L.; Kao, F. !$#journal Genomics (1989) 4:21-27 !$#title Chromosomal localization of the human gene for brain Ca2+/ !1calmodulin-dependent protein kinase type IV. !$#cross-references MUID:89122027; PMID:2536634 !$#accession I49571 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 250-277,'CFGI',281-301,'T',303-338,'X',340-469 ##label RES !'##cross-references GB:J03057; NID:g192366; PIDN:AAA37366.1; !1PID:g192367 !'##experimental_source brain CLASSIFICATION #superfamily Ca2+/calmodulin-dependent protein kinase; !1protein kinase homology KEYWORDS alternative splicing; ATP; calmodulin binding; !1phosphotransferase; serine/threonine-specific protein kinase FEATURE !$40-296 #domain protein kinase homology #label KIN\ !$48-56 #region protein kinase ATP-binding motif\ !$306-469 #product calspermin #status predicted #label CSP\ !$318-337 #region calmodulin binding #status predicted\ !$71 #active_site Lys #status predicted SUMMARY #length 469 #molecular-weight 52627 #checksum 1059 SEQUENCE /// ENTRY I38344 #type complete TITLE titin, cardiac muscle [validated] - human ALTERNATE_NAMES connectin CONTAINS serine/threonine-specific protein kinase (EC 2.7.1.-) ORGANISM #formal_name Homo sapiens #common_name man DATE 12-Aug-1996 #sequence_revision 12-Aug-1996 #text_change 15-Sep-2000 ACCESSIONS I38344; I38345; S20898; S20897; S20899; S63665; S37393 REFERENCE A57430 !$#authors Labeit, S.; Kolmerer, B. !$#journal Science (1995) 270:293-296 !$#title Titins: giant proteins in charge of muscle ultrastructure !1and elasticity. !$#cross-references MUID:96026330; PMID:7569978 !$#accession I38344 !'##status nucleic acid sequence not shown; translation not shown; !1translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-26926 ##label LAB1 !'##cross-references EMBL:X90568; NID:g1017424; PID:g1017425 REFERENCE I38345 !$#authors Musco, G.; Tziatzios, C.; Schuck, P.; Pastore, A. !$#journal Biochemistry (1995) 34:553-561 !$#title Dissecting titin into its structural motifs: identification !1of an alpha-helix motif near the titin N-terminus. !$#cross-references MUID:95119041; PMID:7819249 !$#accession I38345 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1977-2014 ##label MUS !'##cross-references EMBL:X83270; NID:g602579; PIDN:CAA58243.1; !1PID:g602580 !'##note conformation and properties are reported for a synthetic !1peptide corresponding to the translated fragment shown REFERENCE S20897 !$#authors Labeit, S.; Gautel, M.; Lakey, A.; Trinick, J. !$#journal EMBO J. (1992) 11:1711-1716 !$#title Towards a molecular understanding of titin. !$#cross-references MUID:92258380; PMID:1582406 !$#accession S20898 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 13597-14200,'I',14202-14696 ##label LAB2 !'##cross-references EMBL:X64698; NID:g37192; PIDN:CAA45939.1; !1PID:g37193 !$#accession S20897 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type mRNA !'##residues 16330-16382,'S',16384-16756,'F',16758-16860 ##label LAB3 !'##cross-references EMBL:X64699; NID:g37190; PIDN:CAA45940.1; !1PID:g37191 !$#accession S20899 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type mRNA !'##residues 'P',22278-22431,'R',22433-22448,'G',22450-22453,'Q', !122455-22480,'TR',22483-22669,'N',22671-22696,'SA', !122699-23323,'L',23325-25376 ##label LAB4 !'##cross-references EMBL:X64697; NID:g37190; PIDN:CAA45938.1; !1PID:g37195 REFERENCE S63665 !$#authors Kolmerer, B.; Olivieri, N.; Witt, C.C.; Herrmann, B.G.; !1Labeit, S. !$#journal J. Mol. Biol. (1996) 256:556-563 !$#title Genomic organization of M line titin and its tissue-specific !1expression in two distinct isoforms. !$#cross-references MUID:96177761; PMID:8604138 !$#accession S63665 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 26729-26825 ##label KOL !'##cross-references EMBL:X92412; NID:g1236761 REFERENCE S37393 !$#authors Gautel, M.; Leonard, K.; Labeit, S. !$#journal EMBO J. (1993) 12:3827-3834 !$#title Phosphorylation of KSP motifs in the C-terminal region of !1titin in differentiating myoblasts. !$#cross-references MUID:94008990; PMID:8404852 !$#accession S37393 !'##molecule_type mRNA !'##residues 26831-26926 ##label GAU REFERENCE A66736 !$#authors Improta, S.; Politou, A.S.; Pastore, A. !$#submission submitted to the Brookhaven Protein Data Bank, February 1996 !$#cross-references PDB:1TIT !$#contents annotation; conformation by (1)H-NMR, residues 5253-5341 REFERENCE A66201 !$#authors Pfuhl, M.; Pastore, A. !$#submission submitted to the Brookhaven Protein Data Bank, August 1996 !$#cross-references PDB:1NCT !$#contents annotation; conformation by (1)H-NMR, residues 'S', !126059-26155 GENETICS !$#gene GDB:TTN !'##cross-references GDB:127867; OMIM:188840 !$#map_position 2q31-2q32 FUNCTION !$#description structural protein forming filaments in striated muscle CLASSIFICATION #superfamily titin; fibronectin type III repeat homology; !1immunoglobulin homology; protein kinase homology KEYWORDS alternative splicing; calmodulin binding; cardiac muscle; !1duplication; glycoprotein; heart; phosphoprotein; !1phosphotransferase; serine/threonine-specific protein !1kinase; skeletal muscle; structural protein FEATURE !$24752-25008 #domain protein kinase homology #label KIN\ !$84,177,905,2276, !$2378,2459,2481, !$2563,2669,2763, !$2896,3088,3179, !$3384,3432,3628, !$3772,4068,4318, !$5047,5246,5823, !$6213,6264,6699, !$6800,7083,7300, !$7506,7597,8338, !$8447,8455,8719, !$8938,9375,10130, !$10133,10177,10398, !$11066,11488,11515, !$11635,11949,12170, !$12478,12526,12645, !$12875,13001,13036, !$13295,13540,13787, !$13986,14085,14529, !$14870,14910,15438, !$15704,16397,16520, !$16695 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$16780,16976,17579, !$17602,17667,17681, !$17845,17899,18121, !$18188,18209,18336, !$18670,18680,18685, !$18707,18945,19198, !$19238,19346,19753, !$19786,20034,20056, !$20183,20324,20426, !$20840,21270,21407, !$21538,21566,21665, !$21900,21935,22295, !$22495,22627,22897, !$23024,23318,23883, !$24012,24177,24290, !$24447,24642,24840, !$25201,25927,26133, !$26283,26682,26698, !$26811 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$26171,26178,26184, !$26190 #binding_site phosphate (Ser) (covalent) #status !8experimental SUMMARY #length 26926 #molecular-weight 2993497 #checksum 431 SEQUENCE /// ENTRY I37275 #type complete TITLE death-associated protein kinase (EC 2.7.1.-) - human ALTERNATE_NAMES calmodulin-dependent protein kinase homolog; DAP kinase ORGANISM #formal_name Homo sapiens #common_name man DATE 16-Feb-1996 #sequence_revision 16-Feb-1996 #text_change 10-Jul-1998 ACCESSIONS I37275; S39269 REFERENCE A55614 !$#authors Deiss, L.P.; Feinstein, E.; Berissi, H.; Cohen, O.; Kimchi, !1A. !$#journal Genes Dev. (1995) 9:15-30 !$#title Identification of a novel serine/threonine kinase and a !1novel 15-kD protein as potential mediators of the gamma !1interferon-induced cell death. !$#cross-references MUID:95129831; PMID:7828849 !$#accession I37275 !'##molecule_type mRNA !'##residues 1-1423 ##label RES !'##cross-references EMBL:X76104; NID:g434846; PID:g434847 GENETICS !$#gene GDB:DAPK1; DAPK !'##cross-references GDB:555932; OMIM:600831 !$#map_position 9q34.1-9q34.1 FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP !$#pathway apoptosis !$#note activity is calmodulin dependent CLASSIFICATION #superfamily death-associated protein kinase; ankyrin repeat !1homology; protein kinase homology KEYWORDS apoptosis; ATP; calmodulin binding; phosphotransferase; !1serine/threonine-specific protein kinase; tandem repeat FEATURE !$11-267 #domain protein kinase homology #label KIN\ !$19-27 #region protein kinase ATP-binding motif\ !$285-308 #region calmodulin binding #status predicted\ !$370-402 #domain ankyrin repeat homology #label AN1\ !$403-435 #domain ankyrin repeat homology #label AN2\ !$436-468 #domain ankyrin repeat homology #label AN3\ !$470-502 #domain ankyrin repeat homology #label AN4\ !$503-535 #domain ankyrin repeat homology #label AN5\ !$536-568 #domain ankyrin repeat homology #label AN6\ !$569-601 #domain ankyrin repeat homology #label AN7\ !$602-634 #domain ankyrin repeat homology #label AN8\ !$42,64,139,141 #active_site Lys, Glu, Asp, Lys #status predicted SUMMARY #length 1423 #molecular-weight 159161 #checksum 6280 SEQUENCE /// ENTRY S68235 #type complete TITLE myosin-light-chain kinase (EC 2.7.1.117), 210K, nonmuscle - chicken CONTAINS myosin-light-chain kinase, 108K, smooth muscle; telokin ORGANISM #formal_name Gallus gallus #common_name chicken DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S68235; A37099; B44389; A44389; S28227; S78216; A35093; !1A25810; S11652 REFERENCE S68235 !$#authors Watterson, D.M.; Collinge, M.; Lukas, T.J.; Van Eldik, L.J.; !1Birukov, K.G.; Stepanova, O.V.; Shirinsky, V.P. !$#journal FEBS Lett. (1995) 373:217-220 !$#title Multiple gene products are produced from a novel protein !1kinase transcription region. !$#cross-references MUID:96033976; PMID:7589469 !$#accession S68235 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-1906 ##label WAT !'##cross-references EMBL:X52876; NID:g992992; PIDN:CAA37056.1; !1PID:g992993 REFERENCE A37099 !$#authors Shoemaker, M.O.; Lau, W.; Shattuck, R.L.; Kwiatkowski, A.P.; !1Matrisian, P.E.; Guerra-Santos, L.; Wilson, E.; Lukas, T.J.; !1Van Eldik, L.J.; Watterson, D.M. !$#journal J. Cell Biol. (1990) 111:1107-1125 !$#title Use of DNA sequence and mutant analyses and antisense !1oligodeoxynucleotides to examine the molecular basis of !1nonmuscle myosin light chain kinase autoinhibition, !1calmodulin recognition, and activity. !$#cross-references MUID:90361738; PMID:2202734 !$#accession A37099 !'##molecule_type mRNA !'##residues 649-1906 ##label SHO !'##cross-references EMBL:X52876 REFERENCE A44389 !$#authors Collinge, M.; Matrisian, P.E.; Zimmer, W.E.; Shattuck, R.L.; !1Lukas, T.J.; Van Eldik, L.J.; Watterson, D.M. !$#journal Mol. Cell. Biol. (1992) 12:2359-2371 !$#title Structure and expression of a calcium-binding protein gene !1contained within a calmodulin-regulated protein kinase gene. !$#cross-references MUID:92236611; PMID:1373815 !$#accession B44389 !'##status preliminary !'##molecule_type DNA !'##residues 1695-1906 ##label COL !'##cross-references GB:M88284; NID:g212237; PIDN:AAB53767.1; !1PID:g212238 !$#accession A44389 !'##status preliminary !'##molecule_type mRNA !'##residues 1750-1906 ##label CO2 !'##cross-references GB:M88283; NID:g211371; PIDN:AAA48647.1; !1PID:g211372 REFERENCE S28227 !$#authors Yoshikai, S.I.; Ikebe, M. !$#journal Arch. Biochem. Biophys. (1992) 299:242-247 !$#title Molecular cloning of the chicken gizzard telokin gene and !1cDNA. !$#cross-references MUID:93073972; PMID:1444462 !$#accession S28227 !'##molecule_type mRNA !'##residues 1750-1906 ##label YOS !'##cross-references EMBL:M96655; NID:g212744; PIDN:AAA49083.1; !1PID:g212745 !$#accession S78216 !'##molecule_type DNA !'##residues 1750-1906 ##label YOW !'##cross-references EMBL:M96987 REFERENCE A35093 !$#authors Olson, N.J.; Pearson, R.B.; Needleman, D.S.; Hurwitz, M.Y.; !1Kemp, B.E.; Means, A.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:2284-2288 !$#title Regulatory and structural motifs of chicken gizzard myosin !1light chain kinase. !$#cross-references MUID:90192792; PMID:2315320 !$#accession A35093 !'##status preliminary !'##molecule_type mRNA !'##residues 935-1438,'Q',1440-1906 ##label OLS !'##cross-references GB:M31048; NID:g212660; PIDN:AAA49069.1; !1PID:g212661 REFERENCE A25810 !$#authors Guerriero Jr., V.; Russo, M.A.; Olson, N.J.; Putkey, J.A.; !1Means, A.R. !$#journal Biochemistry (1986) 25:8372-8381 !$#title Domain organization of chicken gizzard myosin light chain !1kinase deduced from a cloned cDNA. !$#cross-references MUID:87157587; PMID:3030394 !$#accession A25810 !'##molecule_type mRNA !'##residues 1258-1438,'Q',1440-1906 ##label GUE GENETICS !$#introns 1735/3; 1779/1; 1819/1 CLASSIFICATION #superfamily myosin-light-chain kinase, nonmuscle; !1fibronectin type III repeat homology; immunoglobulin !1homology; protein kinase homology KEYWORDS alternative initiators; ATP; calmodulin binding; !1phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$542-599 #domain immunoglobulin homology #label IMM1\ !$935-1906 #product myosin-light-chain kinase, 108K, smooth !8muscle (from 5.5kb transcript) #status predicted !8#label ALT\ !$1098-1158 #domain immunoglobulin homology #label IMM2\ !$1451-1708 #domain protein kinase homology #label KIN\ !$1459-1467 #region protein kinase ATP-binding motif\ !$1750-1906 #product telokin (kinase-related protein KRP) (from !82.7 kb transkript) #status predicted #label TKN\ !$1808-1869 #domain immunoglobulin homology #label IMM3 SUMMARY #length 1906 #molecular-weight 210445 #checksum 705 SEQUENCE /// ENTRY JP0078 #type complete TITLE LIM protein kinase (EC 2.7.1.-) 1 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS JP0078 REFERENCE JP0078 !$#authors Mizuno, K.; Okano, I.; Ohashi, K.; Nunoue, K.; Kuma, K.; !1Miyata, T.; Nakamura, T. !$#journal Oncogene (1994) 9:1605-1612 !$#title Identification of a human cDNA encoding a novel protein !1kinase with two repeats of the LIM/double zinc finger motif. !$#cross-references MUID:94239736; PMID:8183554 !$#accession JP0078 !'##molecule_type mRNA !'##residues 1-647 ##label MIZ !'##cross-references DDBJ:D26309; NID:g565279; PIDN:BAA05371.1; !1PID:g565280 COMMENT This enzyme plays a central role in the regulation of !1intracellular signal transduction pathways involved in cell !1proliferation, differention, and metabolism. GENETICS !$#gene GDB:LIMK1 !'##cross-references GDB:364125; OMIM:601329 !$#map_position 7q11.23-7q11.23 CLASSIFICATION #superfamily LIM protein kinase; LIM metal-binding repeat !1homology; protein kinase homology KEYWORDS ATP; duplication; phosphotransferase; serine/threonine/ !1tyrosine-specific protein kinase; zinc finger FEATURE !$25-75 #domain LIM metal-binding repeat homology #label !8LIM1\ !$84-137 #domain LIM metal-binding repeat homology #label !8LIM2\ !$337-611 #domain protein kinase homology #label KIN\ !$345-353 #region protein kinase ATP-binding motif\ !$496-506 #region basic SUMMARY #length 647 #molecular-weight 72584 #checksum 1962 SEQUENCE /// ENTRY I48737 #type complete TITLE LIM protein kinase (EC 2.7.1.-) 1 - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS I48737; I49123; I49125 REFERENCE I48737 !$#authors Proeschel, C.; Blouin, M.J.; Gutowski, N.J.; Ludwig, R.; !1Noble, M. !$#journal Oncogene (1995) 11:1271-1281 !$#title Limk1 is predominantly expressed in neural tissues and !1phosphorylates serine, threonine and tyrosine residues in !1vitro. !$#cross-references MUID:96017801; PMID:7478547 !$#accession I48737 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-647 ##label RES !'##cross-references EMBL:X86569; NID:g1051159; PIDN:CAA60377.1; !1PID:g1051160 REFERENCE I49123 !$#authors Bernard, O.; Ganiatsas, S.; Kannourakis, G.; Dringen, R. !$#journal Cell Growth Differ. (1994) 5:1159-1171 !$#title Kiz-1, a protein with LIM zinc finger and kinase domains, is !1expressed mainly in neurons. !$#cross-references MUID:95151637; PMID:7848918 !$#accession I49123 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 15-522,'P',524-647 ##label RE2 !'##cross-references EMBL:U14166; NID:g595789; PIDN:AAC52147.1; !1PID:g595790 REFERENCE I49125 !$#authors Cheng, A.K.; Robertson, E.J. !$#journal Mech. Dev. (1995) 52:187-197 !$#title The murine LIM kinase gene (limk) encodes a novel serine !1threonine kinase expressed predominantly in trophoblast !1giant cells and the developing nervous system. !$#cross-references MUID:96081363; PMID:8541208 !$#accession I49125 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-199,'EC',202-268,'GSQ',272-325,'C',328-647 ##label RE3 !'##cross-references EMBL:U15159; NID:g551544; PIDN:AAC52254.1; !1PID:g551545 GENETICS !$#gene mLimk1 CLASSIFICATION #superfamily LIM protein kinase; LIM metal-binding repeat !1homology; protein kinase homology KEYWORDS ATP; duplication; phosphotransferase; serine/threonine/ !1tyrosine-specific protein kinase; zinc finger FEATURE !$25-75 #domain LIM metal-binding repeat homology #label !8LIM1\ !$84-137 #domain LIM metal-binding repeat homology #label !8LIM2\ !$337-611 #domain protein kinase homology #label KIN\ !$345-353 #region protein kinase ATP-binding motif SUMMARY #length 647 #molecular-weight 72793 #checksum 4255 SEQUENCE /// ENTRY I58353 #type complete TITLE LIM protein kinase (EC 2.7.1.-) 1 [similarity] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 16-Jun-2000 #sequence_revision 16-Jun-2000 #text_change 21-Jul-2000 ACCESSIONS I58353 REFERENCE I58353 !$#authors Nunoue, K.; Ohashi, K.; Okano, I.; Mizuno, K. !$#journal Oncogene (1995) 11:701-710 !$#title LIMK-1 and LIMK-2, two members of a LIM motif-containing !1protein kinase family. !$#cross-references MUID:95380177; PMID:7651734 !$#accession I58353 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-647 ##label RES !'##cross-references GB:D31873; NID:g1684611; PIDN:BAA06672.1; !1PID:g1000682 !'##experimental_source strain Wistar; tissue brain GENETICS !$#gene limk-1 CLASSIFICATION #superfamily LIM protein kinase; LIM metal-binding repeat !1homology; protein kinase homology KEYWORDS ATP; duplication; phosphotransferase; serine/threonine/ !1tyrosine-specific protein kinase; zinc finger FEATURE !$25-75 #domain LIM metal-binding repeat homology #label !8LIM1\ !$84-137 #domain LIM metal-binding repeat homology #label !8LIM2\ !$337-611 #domain protein kinase homology #label KIN\ !$345-353 #region protein kinase ATP-binding motif SUMMARY #length 647 #molecular-weight 72593 #checksum 2680 SEQUENCE /// ENTRY A59196 #type complete TITLE LIM motif-containing protein kinase (EC 2.7.1.-) 2, splice form a - human ALTERNATE_NAMES LIM-2a protein ORGANISM #formal_name Homo sapiens #common_name man DATE 03-Mar-2000 #sequence_revision 03-Mar-2000 #text_change 17-Nov-2000 ACCESSIONS A59196; PC4291 REFERENCE A59196 !$#authors Okano, I.; Hiraoka, J.; Otera, H.; Nunoue, K.; Ohashi, K.; !1Iwashita, S.; Hirai, M.; Mizuno, K. !$#journal J. Biol. Chem. (1995) 270:31321-31330 !$#title Identification and characterization of a novel family of !1serine/threonine kinases containing two N-terminal LIM !1motifs. !$#cross-references MUID:96125122; PMID:8537403 !$#accession A59196 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-638 ##label MIZ !'##cross-references GB:D45906; NID:g1805593; PIDN:BAA08312.1; !1PID:g1136291 !'##experimental_source cell type HepG2 REFERENCE PC4291 !$#authors Osada, H.; Hasada, K.; Inazawa, J.; Uchida, K.; Ueda, R.; !1Takahashi, T.; Takahashi, T. !$#journal Biochem. Biophys. Res. Commun. (1996) 229:582-589 !$#title Subcellular localization and protein interaction of the !1human LIMK2 gene expressing alternative transcripts with !1tissue-specific regulation. !$#cross-references MUID:97127445; PMID:8954941 !$#accession PC4291 !'##molecule_type mRNA !'##residues 1-80 ##label OSA COMMENT For splice form b, see PIR:T17251. COMMENT This protein has two LIM domains, a PDZ domain, and a kinase !1domain. It plays a role in differentiation and oncogenesis !1of the lung. GENETICS !$#gene GDB:LIMK2; limk2a !'##cross-references GDB:6276657 !$#map_position 22q12-22q12 CLASSIFICATION #superfamily LIM protein kinase; LIM metal-binding repeat !1homology; protein kinase homology KEYWORDS alternative splicing; ATP; duplication; phosphotransferase; !1serine/threonine/tyrosine-specific protein kinase; zinc !1finger FEATURE !$12-63 #domain LIM metal-binding repeat homology #label !8LIM1\ !$12-37 #region zinc finger CCHC motif\ !$40-63 #region zinc finger CCCD motif\ !$72-124 #domain LIM metal-binding repeat homology #label !8LIM2\ !$72-95 #region zinc finger CCHC motif\ !$98-124 #region zinc finger CCCC motif\ !$329-608 #domain protein kinase homology #label KIN\ !$337-345 #region protein kinase ATP-binding motif SUMMARY #length 638 #molecular-weight 72231 #checksum 4785 SEQUENCE /// ENTRY T17251 #type complete TITLE LIM motif-containing protein kinase (EC 2.7.1.-) 2, splice form b - human ALTERNATE_NAMES LIM-2b protein; protein DKFZp586K0922.1 ORGANISM #formal_name Homo sapiens #common_name man DATE 03-Mar-2000 #sequence_revision 03-Mar-2000 #text_change 01-Dec-2000 ACCESSIONS T17251; PC4292 REFERENCE Z18722 !$#authors Koehrer, K.; Beyer, A.; Mewes, H.W.; Gassenhuber, J.; !1Wiemann, S. !$#submission submitted to the Protein Sequence Database, September 1999 !$#accession T17251 !'##molecule_type mRNA !'##residues 1-617 ##label KOE !'##cross-references EMBL:AL117466; NID:g5911930; PIDN:CAB55941.1; !1PID:g5911931 !'##experimental_source adult uterus; clone DKFZp586K0922 REFERENCE PC4291 !$#authors Osada, H.; Hasada, K.; Inazawa, J.; Uchida, K.; Ueda, R.; !1Takahashi, T.; Takahashi, T. !$#journal Biochem. Biophys. Res. Commun. (1996) 229:582-589 !$#title Subcellular localization and protein interaction of the !1human LIMK2 gene expressing alternative transcripts with !1tissue-specific regulation. !$#cross-references MUID:97127445; PMID:8954941 !$#accession PC4292 !'##molecule_type mRNA !'##residues 1-34 ##label OSA COMMENT For splice form a, see PIR:A59196. COMMENT This protein has two LIM domains, a PDZ domain, and a kinase !1domain. It plays a role in differentiation and oncogenesis !1of the lung. GENETICS !$#gene GDB:LIMK2 !'##cross-references GDB:6276657 !$#map_position 22q12-22q12 !$#note DKFZp586K0922.1 CLASSIFICATION #superfamily LIM protein kinase; LIM metal-binding repeat !1homology; protein kinase homology KEYWORDS alternative splicing; ATP; duplication; phosphotransferase; !1serine/threonine/tyrosine-specific protein kinase; zinc !1finger FEATURE !$19-42 #region zinc finger CCCD motif\ !$51-103 #domain LIM metal-binding repeat homology #label !8LIM2\ !$51-74 #region zinc finger CCHC motif\ !$77-103 #region zinc finger CCCC motif\ !$308-587 #domain protein kinase homology #label KIN\ !$316-324 #region protein kinase ATP-binding motif SUMMARY #length 617 #molecular-weight 69904 #checksum 8357 SEQUENCE /// ENTRY I78846 #type complete TITLE LIM motif-containing protein kinase (EC 2.7.1.-) 2, splice form a [similarity] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 16-Jun-2000 #sequence_revision 16-Jun-2000 #text_change 21-Jul-2000 ACCESSIONS I78846 REFERENCE I58353 !$#authors Nunoue, K.; Ohashi, K.; Okano, I.; Mizuno, K. !$#journal Oncogene (1995) 11:701-710 !$#title LIMK-1 and LIMK-2, two members of a LIM motif-containing !1protein kinase family. !$#cross-references MUID:95380177; PMID:7651734 !$#accession I78846 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-638 ##label RES !'##cross-references GB:D31874; NID:g1684612; PIDN:BAA06673.1; !1PID:g1000684 !'##experimental_source strain Wistar; tissue brain GENETICS !$#gene limk-2a CLASSIFICATION #superfamily LIM protein kinase; LIM metal-binding repeat !1homology; protein kinase homology KEYWORDS alternative splicing; ATP; duplication; phosphotransferase; !1serine/threonine/tyrosine-specific protein kinase; zinc !1finger FEATURE !$12-63 #domain LIM metal-binding repeat homology #label !8LIM1\ !$72-124 #domain LIM metal-binding repeat homology #label !8LIM2\ !$329-608 #domain protein kinase homology #label KIN\ !$337-345 #region protein kinase ATP-binding motif SUMMARY #length 638 #molecular-weight 72201 #checksum 5353 SEQUENCE /// ENTRY I78847 #type complete TITLE LIM motif-containing protein kinase (EC 2.7.1.-) 2, splice form b [similarity] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 16-Jun-2000 #sequence_revision 16-Jun-2000 #text_change 21-Jul-2000 ACCESSIONS I78847; I78849 REFERENCE I58353 !$#authors Nunoue, K.; Ohashi, K.; Okano, I.; Mizuno, K. !$#journal Oncogene (1995) 11:701-710 !$#title LIMK-1 and LIMK-2, two members of a LIM motif-containing !1protein kinase family. !$#cross-references MUID:95380177; PMID:7651734 !$#accession I78847 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-617 ##label RES !'##cross-references GB:D31875; NID:g1684613; PIDN:BAA06674.1; !1PID:g1000686 !$#accession I78849 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-163 ##label RE2 !'##cross-references GB:D31877; NID:g1684615; PIDN:BAA06676.1; !1PID:g1000690 GENETICS RES1 !$#gene limk-2b GENETICS RES2 !$#gene limk-2d CLASSIFICATION #superfamily LIM protein kinase; LIM metal-binding repeat !1homology; protein kinase homology KEYWORDS alternative splicing; ATP; duplication; phosphotransferase; !1serine/threonine/tyrosine-specific protein kinase; zinc !1finger FEATURE !$51-103 #domain LIM metal-binding repeat homology #label !8LIM2\ !$308-587 #domain protein kinase homology #label KIN\ !$316-324 #region protein kinase ATP-binding motif SUMMARY #length 617 #molecular-weight 69834 #checksum 8449 SEQUENCE /// ENTRY JP0079 #type complete TITLE LIM protein kinase (EC 2.7.1.-) - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS JP0079 REFERENCE JP0079 !$#authors Ohashi, K.; Toshima, J.; Tajinda, K.; Nakamura, T.; Mizuno, !1K. !$#journal J. Biochem. (1994) 116:636-642 !$#title Molecular cloning of a chicken lung cDNA encoding a novel !1protein kinase with N-terminal two LIM/double zinc finger !1motifs. !$#cross-references MUID:95155277; PMID:7852284 !$#accession JP0079 !'##molecule_type mRNA !'##residues 1-642 ##label OHA !'##cross-references DDBJ:D26310; NID:g1402513; PIDN:BAA05372.1; !1PID:g643086 COMMENT This protein plays an important role in the regulation of !1diverse cell functions. CLASSIFICATION #superfamily LIM protein kinase; LIM metal-binding repeat !1homology; protein kinase homology KEYWORDS ATP; duplication; phosphotransferase; serine/threonine/ !1tyrosine-specific protein kinase; zinc finger FEATURE !$12-63 #domain LIM metal-binding repeat homology #label !8LIM1\ !$72-124 #domain LIM metal-binding repeat homology #label !8LIM2\ !$329-608 #domain protein kinase homology #label KIN\ !$337-345 #region protein kinase ATP-binding motif\ !$496-506 #region basic SUMMARY #length 642 #molecular-weight 72467 #checksum 6974 SEQUENCE /// ENTRY TVHUSC #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) src, neuronal - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1989 #sequence_revision 07-Oct-1994 #text_change 16-Jun-2000 ACCESSIONS A26891; A61083; B61083; A23287; A28832; B34704 REFERENCE A26891 !$#authors Tanaka, A.; Gibbs, C.P.; Arthur, R.R.; Anderson, S.K.; Kung, !1H.J.; Fujita, D.J. !$#journal Mol. Cell. Biol. (1987) 7:1978-1983 !$#title DNA sequence encoding the amino-terminal region of the human !1c-src protein: implications of sequence divergence among !1src-type kinase oncogenes. !$#cross-references MUID:87257903; PMID:3299057 !$#accession A26891 !'##molecule_type mRNA !'##residues 1-117;124-191 ##label TAN !'##cross-references GB:M16237 REFERENCE A61083 !$#authors Pyper, J.M.; Bolen, J.B. !$#journal J. Neurosci. Res. (1989) 24:89-96 !$#title Neuron-specific splicing of C-SRC RNA in human brain. !$#cross-references MUID:90040822; PMID:2681803 !$#accession A61083 !'##molecule_type mRNA !'##residues 98-145 ##label PYP !$#accession B61083 !'##molecule_type mRNA !'##residues 98-117;124-145 ##label PY2 REFERENCE A23287 !$#authors Anderson, S.K.; Gibbs, C.P.; Tanaka, A.; Kung, H.J.; Fujita, !1D.J. !$#journal Mol. Cell. Biol. (1985) 5:1122-1129 !$#title Human cellular src gene: Nucleotide sequence and derived !1amino acid sequence of the region coding for the !1carboxy-terminal two-thirds of pp60(c-src). !$#cross-references MUID:85213483; PMID:2582238 !$#accession A23287 !'##molecule_type mRNA !'##residues 192-542 ##label AND !'##cross-references GB:X02647; NID:g36588; PIDN:CAA26485.1; !1PID:g1848077 REFERENCE A28832 !$#authors Parker, R.C.; Mardon, G.; Lebo, R.V.; Varmus, H.E.; Bishop, !1J.M. !$#journal Mol. Cell. Biol. (1985) 5:831-838 !$#title Isolation of duplicated human c-src genes located on !1chromosomes 1 and 20. !$#cross-references MUID:85187981; PMID:2581127 !$#accession A28832 !'##molecule_type mRNA !'##residues 382-542 ##label PAR REFERENCE A34704 !$#authors Pyper, J.M.; Bolen, J.B. !$#journal Mol. Cell. Biol. (1990) 10:2035-2040 !$#title Identification of a novel neuronal C-SRC exon expressed in !1human brain. !$#cross-references MUID:90220588; PMID:1691439 !$#accession B34704 !'##molecule_type mRNA !'##residues 118-123 ##label PY3 GENETICS !$#gene GDB:SRC !'##cross-references GDB:120750; OMIM:190090 !$#map_position 20q11.2-20q11.2 !$#introns 84/1; 117/2; 123/2; 156/2; 191/1; 241/1; 293/1; 353/1; 378/ !13; 430/1; 474/1 FUNCTION !$#description catalyzes the phosphorylation of a peptidyl tyrosine residue !1by ATP CLASSIFICATION #superfamily protein-tyrosine kinase src; protein kinase !1homology; SH2 homology; SH3 homology KEYWORDS ATP; autophosphorylation; blocked amino end; lipoprotein; !1myristylation; phosphoprotein; phosphotransferase; !1proto-oncogene; transforming protein; tyrosine-specific !1protein kinase FEATURE !$1-542 #product protein-tyrosine kinase src, neuronal !8#status predicted #label MAT\ !$1-117,124-542 #product protein-tyrosine kinase src, short form !8#status predicted #label MA2\ !$91-146 #domain SH3 homology #label SH3\ !$157-254 #domain SH2 homology #label SH2\ !$274-532 #domain protein kinase homology #label KIN\ !$282-290 #region protein kinase ATP-binding motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$304 #active_site Lys #status predicted\ !$425,536 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 542 #molecular-weight 60588 #checksum 9802 SEQUENCE /// ENTRY A43610 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) src, neuronal [similarity] - mouse ALTERNATE_NAMES Rouse sarcoma oncogene ORGANISM #formal_name Mus musculus #common_name house mouse DATE 16-Jun-2000 #sequence_revision 16-Jun-2000 #text_change 16-Jun-2000 ACCESSIONS A43610 REFERENCE A43610 !$#authors Martinez, R.; Mathey-Prevot, B.; Bernards, A.; Baltimore, D. !$#journal Science (1987) 237:411-415 !$#title Neuronal pp60(c-src) contains a six-amino acid insertion !1relative to its non-neuronal counterpart. !$#cross-references MUID:87263406; PMID:2440106 !$#accession A43610 !'##molecule_type mRNA !'##residues 1-541 ##label MAR !'##cross-references GB:M17031; NID:g201056; PIDN:AAA40135.1; !1PID:g201057 COMMENT The neuronal c-src has an 6 residue insertion of RLVNVR !1within the amino-terminus which is not present in normal !1pp60-c-src shown here. GENETICS !$#gene Src !'##cross-references MGI:98397 !$#map_position 2:91.0 CLASSIFICATION #superfamily protein-tyrosine kinase src; protein kinase !1homology; SH2 homology; SH3 homology KEYWORDS ATP; autophosphorylation; blocked amino end; lipoprotein; !1myristylation; phosphoprotein; phosphotransferase; !1tyrosine-specific protein kinase FEATURE !$90-145 #domain SH3 homology #label SH3\ !$156-253 #domain SH2 homology #label SH2\ !$273-531 #domain protein kinase homology #label KIN\ !$281-289 #region protein kinase ATP-binding motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$303 #active_site Lys #status predicted\ !$424,535 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 541 #molecular-weight 60618 #checksum 7863 SEQUENCE /// ENTRY TVCHS #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) src - chicken ALTERNATE_NAMES kinase-related transforming protein src ORGANISM #formal_name Gallus gallus #common_name chicken DATE 19-Feb-1984 #sequence_revision 07-Oct-1994 #text_change 21-Jul-2000 ACCESSIONS A00630; I50217; A41256; C35650; A32432 REFERENCE A00630 !$#authors Takeya, T.; Hanafusa, H. !$#journal Cell (1983) 32:881-890 !$#title Structure and sequence of the cellular gene homologous to !1the RSV sec gene and the mechanism for generating the !1transforming virus. !$#cross-references MUID:83155664; PMID:6299580 !$#accession A00630 !'##molecule_type DNA !'##residues 1-500,'R',502-533 ##label TAK !'##cross-references GB:J00844; NID:g212700 REFERENCE A90838 !$#authors Takeya, T.; Hanafusa, H. !$#journal Cell (1983) 34:319 !$#contents annotation; erratum, correct translation of residue 526 REFERENCE I50217 !$#authors Takeya, T.; Hanafusa, H. !$#journal J. Virol. (1982) 44:12-18 !$#title DNA sequence of the viral and cellular src gene of chickens: !1II comparison of the src genes of two strains of avian !1sarcoma virus and of the cellular homolog. !$#cross-references MUID:83059861; PMID:6292480 !$#accession I50217 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-7 ##label TA2 !'##cross-references GB:J00908; NID:g211690; PIDN:AAA48732.1; !1PID:g211691 !'##note the authors translated the codons AAC and CAG for residues 301 !1and 526 as Thr and Glu, respectively REFERENCE A41256 !$#authors Dorai, T.; Levy, J.B.; Kang, L.; Brugge, J.S.; Wang, L.H. !$#journal Mol. Cell. Biol. (1991) 11:4165-4176 !$#title Analysis of cDNAs of the proto-oncogene c-src: heterogeneity !1in 5' exons and possible mechanism for the genesis of the 3' !1end of v-src. !$#cross-references MUID:91304409; PMID:1712905 !$#accession A41256 !'##molecule_type mRNA !'##residues 484-533 ##label DOR1 !'##cross-references GB:S43579; NID:g1679964; PIDN:AAB19353.1; !1PID:g233061 !'##note the authors translated the codon CAG for residue 527 as Glu REFERENCE A35650 !$#authors Dorai, T.; Wang, L.H. !$#journal Mol. Cell. Biol. (1990) 10:4068-4079 !$#title An alternative non-tyrosine protein kinase product of the !1c-src gene in chicken skeletal muscle. !$#cross-references MUID:90318371; PMID:2115117 !$#accession C35650 !'##molecule_type mRNA !'##residues 1-182,'DPCIPLPSCLC' ##label DOR2 !'##cross-references GB:M57290; NID:g212703; PIDN:AAA49078.1; !1PID:g212706 !'##note alternatively spliced mRNA exclusively replaces the long form !1in skeletal muscle shortly before hatching !'##note this ORF appears not to be translated REFERENCE A32432 !$#authors Shenoy, S.; Choi, J.K.; Bagrodia, S.; Copeland, T.D.; !1Maller, J.L.; Shalloway, D. !$#journal Cell (1989) 57:763-774 !$#title Purified maturation promoting factor phosphorylates pp60 !1(c-src) at the sites phosphorylated during fibroblast !1mitosis. !$#cross-references MUID:89249341; PMID:2470512 !$#accession A32432 !'##molecule_type protein !'##residues 2-88 ##label SHE !'##note 34-Thr, 46-Thr, and 72-Ser are phosphorylated during mitosis GENETICS !$#gene src CLASSIFICATION #superfamily protein-tyrosine kinase src; protein kinase !1homology; SH2 homology; SH3 homology KEYWORDS alternative splicing; ATP; autophosphorylation; blocked !1amino end; lipoprotein; myristylation; phosphoprotein; !1phosphotransferase; proto-oncogene; tyrosine-specific !1protein kinase FEATURE !$88-137 #domain SH3 homology #label SH3\ !$148-245 #domain SH2 homology #label SH2\ !$265-523 #domain protein kinase homology #label KIN\ !$273-281 #region protein kinase ATP-binding motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$12,48 #binding_site phosphate (Ser) (covalent) (by protein !8kinase C) #status predicted\ !$17 #binding_site phosphate (Ser) (covalent) (by protein !8kinase A) #status predicted\ !$34,46 #binding_site phosphate (Thr) (covalent) #status !8experimental\ !$72 #binding_site phosphate (Ser) (covalent) #status !8experimental\ !$295 #active_site Lys #status predicted\ !$416,527 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 533 #molecular-weight 60023 #checksum 238 SEQUENCE /// ENTRY A34104 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) src 1 [similarity] - African clawed frog ALTERNATE_NAMES kinase-related transforming protein (src); kinase-related transforming protein (src) 1 ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 16-Jun-2000 #sequence_revision 16-Jun-2000 #text_change 16-Jun-2000 ACCESSIONS A34104; I51564 REFERENCE A34104 !$#authors Steele, R.E.; Unger, T.F.; Mardis, M.J.; Fero, J.B. !$#journal J. Biol. Chem. (1989) 264:10649-10653 !$#title The two Xenopus laevis SRC genes are co-expressed and each !1produces functional pp(60src). !$#cross-references MUID:89278134; PMID:2499582 !$#accession A34104 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-532 ##label STE !'##cross-references GB:M24704; GB:J04822; NID:g214804; PIDN:AAA49962.1; !1PID:g214805 REFERENCE I51564 !$#authors Steele, R.E.; Chosn, R.; Ral, B.B.A.; Winokur, S.T.; Unger, !1T.F. !$#journal Oncogene (1992) 7:2345-2350 !$#title Structural organization of a src gene from xenopus laevis. !$#cross-references MUID:93064714; PMID:1437158 !$#accession I51564 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-113 ##label ST2 !'##cross-references GB:M33646; NID:g214808; PIDN:AAA49963.1; !1PID:g214810 GENETICS !$#introns 80/1 CLASSIFICATION #superfamily protein-tyrosine kinase src; protein kinase !1homology; SH2 homology; SH3 homology KEYWORDS ATP; autophosphorylation; blocked amino end; lipoprotein; !1myristylation; phosphoprotein; phosphotransferase; !1tyrosine-specific protein kinase FEATURE !$87-136 #domain SH3 homology #label SH3\ !$147-244 #domain SH2 homology #label SH2\ !$264-522 #domain protein kinase homology #label KIN\ !$272-280 #region protein kinase ATP-binding motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$294 #active_site Lys #status predicted\ !$415,526 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 532 #molecular-weight 59856 #checksum 7110 SEQUENCE /// ENTRY TVFV60 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) src - Rous sarcoma virus ORGANISM #formal_name Rous sarcoma virus DATE 22-May-1981 #sequence_revision 17-Dec-1982 #text_change 24-Sep-1999 ACCESSIONS A38017; A00631; S02726; A38018 REFERENCE A38017 !$#authors Czernilofsky, A.P.; Levinson, A.D.; Varmus, H.E.; Bishop, !1J.M.; Tischer, E.; Goodman, H. !$#journal Nature (1983) 301:736-738 !$#title Corrections to the nucleotide sequence of the src gene of !1Rous sarcoma virus. !$#cross-references MUID:83141780; PMID:6298633 !$#accession A38017 !'##molecule_type DNA !'##residues 1-526 ##label CZE !'##cross-references GB:L29199; GB:J02018; GB:J02026; GB:J02352; !1GB:K01194; GB:K01195; GB:N00021; NID:g459672; !1PIDN:AAA42563.1; PID:g459677 !'##experimental_source strain Schmidt-Ruppin REFERENCE A00630 !$#authors Takeya, T.; Hanafusa, H. !$#journal Cell (1983) 32:881-890 !$#title Structure and sequence of the cellular gene homologous to !1the RSV sec gene and the mechanism for generating the !1transforming virus. !$#cross-references MUID:83155664; PMID:6299580 !$#accession A00631 !'##molecule_type DNA !'##residues 1-62,'D',64-95,'T',97-123,'V',125-300,'N',302-526 ##label !1TAK !'##experimental_source strain Schmidt-Ruppin REFERENCE S02726 !$#authors Barnier, J.V.; Dezelee, P.; Marx, M.; Calothy, G. !$#journal Nucleic Acids Res. (1989) 17:1252 !$#title Nucleotide sequence of the src gene of the Schmidt-Ruppin !1strain of Rous Sarcoma virus type E. !$#cross-references MUID:89160256; PMID:2537953 !$#accession S02726 !'##molecule_type DNA !'##residues 1-9,'G',11-62,'D',64-123,'V',125-319,'K',321-495,'S', !1497-526 ##label BAR !'##cross-references EMBL:X13745; NID:g61908; PIDN:CAA32012.1; !1PID:g61909 REFERENCE A38018 !$#authors Takeya, T.; Feldman, R.A.; Hanafusa, H. !$#journal J. Virol. (1982) 44:1-11 !$#title DNA sequence of the viral and cellular src gene of chickens: !1I. Complete nucleotide sequence of an EcoRI fragment of !1recovered avian sarcoma virus which codes for gp37 and !1pp60-src. !$#cross-references MUID:83059858; PMID:6292477 !$#accession A38018 !'##molecule_type DNA !'##residues 1-15,'C',17-94,'RT',97-116,'D',118-337,'T',339-526 ##label !1TA2 !'##cross-references GB:K00928; NID:g210187; PIDN:AAA42565.1; !1PID:g210189 !'##experimental_source strain rASV1441 REFERENCE A38019 !$#authors Neil, J.C.; Ghysdael, J.; Vogt, P.K.; Smart, J.E. !$#journal Nature (1981) 291:675-677 !$#title Homologous tyrosine phosphorylation sites in !1transformation-specific gene products of distinct avian !1sarcoma viruses. !$#cross-references MUID:81220979; PMID:6264320 !$#contents annotation; phosphorylation site COMMENT The sequence from the Schmidt-Ruppin strain is shown. GENETICS !$#gene src CLASSIFICATION #superfamily protein-tyrosine kinase src; protein kinase !1homology; SH2 homology; SH3 homology KEYWORDS ATP; autophosphorylation; blocked amino end; lipoprotein; !1myristylation; oncogene; phosphoprotein; phosphotransferase; !1tyrosine-specific protein kinase FEATURE !$88-137 #domain SH3 homology #label SH3\ !$148-245 #domain SH2 homology #label SH2\ !$265-523 #domain protein kinase homology #label KIN\ !$273-281 #region protein kinase ATP-binding motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$295 #active_site Lys #status predicted\ !$416 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status experimental SUMMARY #length 526 #molecular-weight 58984 #checksum 9974 SEQUENCE /// ENTRY B34104 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) src 2 [similarity] - African clawed frog ALTERNATE_NAMES kinase-related transforming protein (src); kinase-related transforming protein (src) 2 ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 16-Jun-2000 #sequence_revision 16-Jun-2000 #text_change 16-Jun-2000 ACCESSIONS B34104; I51563 REFERENCE A34104 !$#authors Steele, R.E.; Unger, T.F.; Mardis, M.J.; Fero, J.B. !$#journal J. Biol. Chem. (1989) 264:10649-10653 !$#title The two Xenopus laevis SRC genes are co-expressed and each !1produces functional pp(60src). !$#cross-references MUID:89278134; PMID:2499582 !$#accession B34104 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-532 ##label STE !'##cross-references GB:M23422; GB:J04822; NID:g214796; PIDN:AAA49961.1; !1PID:g214797 REFERENCE I51563 !$#authors Steele, R.E. !$#journal Nucleic Acids Res. (1985) 13:1747-1761 !$#title Two divergent cellular src genes are expressed in Xenopus !1laevis. !$#cross-references MUID:85215578; PMID:2987836 !$#accession I51563 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 439-492 ##label ST2 !'##cross-references GB:M30858; NID:g214799; PIDN:AAA51644.1; !1PID:g555569 GENETICS !$#gene src !$#introns 464/1 CLASSIFICATION #superfamily protein-tyrosine kinase src; protein kinase !1homology; SH2 homology; SH3 homology KEYWORDS ATP; autophosphorylation; blocked amino end; lipoprotein; !1myristylation; phosphoprotein; phosphotransferase; !1tyrosine-specific protein kinase FEATURE !$87-136 #domain SH3 homology #label SH3\ !$147-244 #domain SH2 homology #label SH2\ !$264-522 #domain protein kinase homology #label KIN\ !$272-280 #region protein kinase ATP-binding motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$294 #active_site Lys #status predicted\ !$415,526 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 532 #molecular-weight 59736 #checksum 7595 SEQUENCE /// ENTRY TVHULY #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) lyn, splice form A - human CONTAINS protein-tyrosine kinase lyn, splice form B ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 18-Feb-2000 ACCESSIONS A26719; D38268; PH0949; I53715 REFERENCE A26719 !$#authors Yamanashi, Y.; Fukushige, S.I.; Semba, K.; Sukegawa, J.; !1Miyajima, N.; Matsubara, K.; Yamamoto, T.; Toyoshima, K. !$#journal Mol. Cell. Biol. (1987) 7:237-243 !$#title The yes-related cellular gene lyn encodes a possible !1tyrosine kinase similar to p56lck. !$#cross-references MUID:87172710; PMID:3561390 !$#accession A26719 !'##molecule_type mRNA !'##residues 1-512 ##label YAM !'##cross-references GB:M16038; NID:g187268; PIDN:AAA59540.1; !1PID:g307144 REFERENCE A38268 !$#authors Partanen, J.; Maekelae, T.P.; Alitalo, R.; Lehvaeslaiho, H.; !1Alitalo, K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:8913-8917 !$#title Putative tyrosine kinases expressed in K-562 human leukemia !1cells. !$#cross-references MUID:91062389; PMID:2247464 !$#accession D38268 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 369-424 ##label PAR REFERENCE PH0949 !$#authors Bielke, W.; Ziemieki, A.; Kappos, L.; Miescher, G.C. !$#journal Biochem. Biophys. Res. Commun. (1992) 186:1403-1409 !$#title Expression of the B cell-associated tyrosine kinase gene lyn !1in primary neuroblastoma tumours and its modulation during !1the differentiation of neuroblastoma cell lines. !$#cross-references MUID:92378604; PMID:1510669 !$#accession PH0949 !'##molecule_type mRNA !'##residues 369-424 ##label BIE !'##experimental_source neuroblastoma SK-IN cell REFERENCE I53715 !$#authors Rider, L.G.; Raben, N.; Miller, L.; Jelsema, C. !$#journal Gene (1994) 138:219-222 !$#title The cDNAs encoding two forms of the LYN protein tyrosine !1kinase are expressed in rat mast cells and human myeloid !1cells. !$#cross-references MUID:94171041; PMID:8125304 !$#accession I53715 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-24,46-512 ##label RID !'##cross-references GB:M79321; NID:g187270; PIDN:AAB50019.1; !1PID:g187271 !'##experimental_source splice form B GENETICS !$#gene GDB:LYN !'##cross-references GDB:120159; OMIM:165120 !$#map_position 8q13-8qter FUNCTION !$#description catalyzes the phosphorylation of a peptidyl tyrosine residue !1by ATP CLASSIFICATION #superfamily protein-tyrosine kinase src; protein kinase !1homology; SH2 homology; SH3 homology KEYWORDS alternative splicing; ATP; autophosphorylation; blocked !1amino end; lipoprotein; myristylation; phosphoprotein; !1phosphotransferase; proto-oncogene; thiolester bond; !1transforming protein; tyrosine-specific protein kinase FEATURE !$2-512 #product protein-tyrosine kinase lyn, splice form A !8#status predicted #label MATA\ !$2-24,46-512 #product protein-tyrosine kinase lyn, splice form B !8#status predicted #label MATB\ !$70-118 #domain SH3 homology #label SH3\ !$129-226 #domain SH2 homology #label SH2\ !$245-504 #domain protein kinase homology #label KIN\ !$253-261 #region protein kinase ATP-binding motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$275 #active_site Lys #status predicted\ !$397,508 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 512 #molecular-weight 58574 #checksum 3041 SEQUENCE /// ENTRY I56160 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) lyn, splice form A - rat CONTAINS protein-tyrosine kinase lyn, splice form B ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 18-Feb-2000 #sequence_revision 18-Feb-2000 #text_change 18-Feb-2000 ACCESSIONS I56160; I67811; I67812 REFERENCE I56160 !$#authors Minoguchi, K.; Nishikata, H.; Siraganian, R.P. !$#journal J. Immunol. (1993) 150:222 !$#title Bacterially expressed rat p56lyn binds several proteins in !1rat basophilic leukemia cells including pp72, a tyrosine !1phosphorylated protein prominent in activated cells. !$#accession I56160 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-512 ##label MIN !'##cross-references GB:L14951; NID:g294582; PIDN:AAA41549.1; !1PID:g294583 REFERENCE I53715 !$#authors Rider, L.G.; Raben, N.; Miller, L.; Jelsema, C. !$#journal Gene (1994) 138:219-222 !$#title The cDNAs encoding two forms of the LYN protein tyrosine !1kinase are expressed in rat mast cells and human myeloid !1cells. !$#cross-references MUID:94171041; PMID:8125304 !$#accession I67811 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-230,'L',232-307,'A',309-418,'Y',420-512 ##label RID1 !'##cross-references GB:L14782; NID:g294578; PIDN:AAA20944.1; !1PID:g294579 !'##note in Genbank entry RATLYNATYR, release 116.0, PIDN:AAA20944.1, !1the source is designated Rattus rattus !$#accession I67812 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-24,46-230,'L',232-307,'A',309-418,'Y',420-512 ##label !1RID2 !'##cross-references GB:L14823; NID:g294580; PIDN:AAA20945.1; !1PID:g294581 !'##note in Genbank entry RATLYNBTYR, release 116.0, PIDN:AAA20945.1, !1the source is designated Rattus rattus CLASSIFICATION #superfamily protein-tyrosine kinase src; protein kinase !1homology; SH2 homology; SH3 homology KEYWORDS alternative splicing; ATP; autophosphorylation; blocked !1amino end; lipoprotein; myristylation; phosphoprotein; !1phosphotransferase; thiolester bond; tyrosine-specific !1protein kinase FEATURE !$2-512 #product protein-tyrosine kinase lyn, splice form A !8#status predicted #label MATA\ !$2-24,46-512 #product protein-tyrosine kinase lyn, splice form B !8#status predicted #label MATB\ !$70-118 #domain SH3 homology #label SH3\ !$129-226 #domain SH2 homology #label SH2\ !$245-504 #domain protein kinase homology #label KIN\ !$253-261 #region protein kinase ATP-binding motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$275 #active_site Lys #status predicted\ !$397,508 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 512 #molecular-weight 58660 #checksum 3032 SEQUENCE /// ENTRY A39719 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) lyn, long splice form - mouse CONTAINS protein-tyrosine kinase lyn, short splice form ORGANISM #formal_name Mus musculus #common_name house mouse DATE 18-Feb-2000 #sequence_revision 18-Feb-2000 #text_change 03-Mar-2000 ACCESSIONS A39719; B39719; A39750; B39750 REFERENCE A39719 !$#authors Stanley, E.; Ralph, S.; McEwen, S.; Boulet, I.; Holtzman, !1D.A.; Lock, P.; Dunn, A.R. !$#journal Mol. Cell. Biol. (1991) 11:3399-3406 !$#title Alternatively spliced murine lyn mRNAs encode distinct !1proteins. !$#cross-references MUID:91260688; PMID:1710766 !$#accession A39719 !'##molecule_type mRNA !'##residues 1-512 ##label STA1 !'##cross-references GB:M64608; NID:g198938; PIDN:AAA39470.1; !1PID:g198939 !$#accession B39719 !'##molecule_type mRNA !'##residues 1-24,46-512 ##label STA2 !'##cross-references GB:M64608 REFERENCE A39750 !$#authors Yi, T.; Bolen, J.B.; Ihle, J.N. !$#journal Mol. Cell. Biol. (1991) 11:2391-2398 !$#title Hematopoietic cells express two forms of lyn kinase !1differing by 21 amino acids in the amino terminus. !$#cross-references MUID:91203857; PMID:2017160 !$#accession A39750 !'##molecule_type mRNA !'##residues 1-76,'F',78-160,'I',162-278,'L',280-390,'I',392-424,'D', !1426-512 ##label YI1 !'##cross-references GB:M57696; NID:g198940; PIDN:AAA39471.1; !1PID:g198941 !$#accession B39750 !'##molecule_type mRNA !'##residues 1-24,46-76,'F',78-160,'I',162-278,'L',280-390,'I',392-424, !1'D',426-512 ##label YI2 !'##cross-references GB:M57697; NID:g198942; PIDN:AAA39472.1; !1PID:g198943 CLASSIFICATION #superfamily protein-tyrosine kinase src; protein kinase !1homology; SH2 homology; SH3 homology KEYWORDS alternative splicing; ATP; autophosphorylation; blocked !1amino end; lipoprotein; myristylation; phosphoprotein; !1phosphotransferase; tyrosine-specific protein kinase FEATURE !$1-512 #product protein-tyrosine kinase lyn, long splice !8form #status predicted #label MATL\ !$1-24,46-512 #product protein-tyrosine kinase lyn, short splice !8form #status predicted #label MATS\ !$70-118 #domain SH3 homology #label SH3\ !$129-226 #domain SH2 homology #label SH2\ !$245-504 #domain protein kinase homology #label KIN\ !$253-261 #region protein kinase ATP-binding motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$275 #active_site Lys #status predicted\ !$397,508 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 512 #molecular-weight 58811 #checksum 2609 SEQUENCE /// ENTRY A43806 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) fyn [similarity] - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 16-Jun-2000 #sequence_revision 16-Jun-2000 #text_change 16-Jun-2000 ACCESSIONS A43806 REFERENCE A43806 !$#authors Steele, R.E.; Deng, J.C.; Ghosn, C.R.; Fero, J.B. !$#journal Oncogene (1990) 5:369-376 !$#title Structure and expression of fyn genes in Xenopus laevis. !$#cross-references MUID:90191723; PMID:2179818 !$#accession A43806 !'##molecule_type mRNA !'##residues 1-537 ##label STE !'##cross-references GB:X52188; GB:X52189; NID:g64701; PIDN:CAA36435.1; !1PID:g64702 CLASSIFICATION #superfamily protein-tyrosine kinase src; protein kinase !1homology; SH2 homology; SH3 homology KEYWORDS ATP; autophosphorylation; blocked amino end; lipoprotein; !1myristylation; phosphoprotein; phosphotransferase; !1tyrosine-specific protein kinase FEATURE !$89-138 #domain SH3 homology #label SH3\ !$149-246 #domain SH2 homology #label SH2\ !$269-527 #domain protein kinase homology #label KIN\ !$277-285 #region protein kinase ATP-binding motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$299 #active_site Lys #status predicted\ !$420,531 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 537 #molecular-weight 60846 #checksum 2563 SEQUENCE /// ENTRY A44991 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) fyn [similarity] - mouse ALTERNATE_NAMES kinase-related transforming protein (fyn) ORGANISM #formal_name Mus musculus #common_name house mouse DATE 16-Jun-2000 #sequence_revision 16-Jun-2000 #text_change 16-Jun-2000 ACCESSIONS A44991 REFERENCE A44991 !$#authors Cooke, M.P.; Perlmutter, R.M. !$#journal New Biol. (1989) 1:66-74 !$#title Expression of a novel form of the fyn proto-oncogene in !1hematopoietic cells. !$#cross-references MUID:91175680; PMID:2488273 !$#accession A44991 !'##status preliminary !'##molecule_type mRNA !'##residues 1-534 ##label COO !'##cross-references GB:M27266; NID:g193357; PIDN:AAA37644.1; !1PID:g309241 !'##note in the authors' translation an additional residue Leu was shown !1after Lys, for residue 459 CLASSIFICATION #superfamily protein-tyrosine kinase src; protein kinase !1homology; SH2 homology; SH3 homology KEYWORDS ATP; autophosphorylation; blocked amino end; lipoprotein; !1myristylation; phosphoprotein; phosphotransferase; !1tyrosine-specific protein kinase FEATURE !$89-138 #domain SH3 homology #label SH3\ !$149-246 #domain SH2 homology #label SH2\ !$266-524 #domain protein kinase homology #label KIN\ !$274-282 #region protein kinase ATP-binding motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$296 #active_site Lys #status predicted\ !$417,528 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 534 #molecular-weight 60057 #checksum 2574 SEQUENCE /// ENTRY S33568 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) fyn [similarity] - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 16-Jun-2000 #sequence_revision 16-Jun-2000 #text_change 16-Jun-2000 ACCESSIONS S33568; S36351; S20807 REFERENCE S33568 !$#authors Sudol, M.; Greulich, H.; Newman, L.; Sarkar, A.; Sukegawa, !1J.; Yamamoto, T. !$#journal Oncogene (1993) 8:823-831 !$#title A novel Yes-related kinase, Yrk, is expressed at elevated !1levels in neural and hematopoietic tissues. !$#cross-references MUID:93205395; PMID:8455940 !$#accession S33568 !'##molecule_type mRNA !'##residues 1-534 ##label SUD1 !'##cross-references EMBL:X52841 REFERENCE S36351 !$#authors Sudol, M. !$#submission submitted to the EMBL Data Library, May 1990 !$#accession S36351 !'##molecule_type mRNA !'##residues 1-348,'I',350-534 ##label SUD2 !'##cross-references EMBL:X52841; NID:g62861; PIDN:CAA37025.1; !1PID:g62862 GENETICS !$#gene fyn CLASSIFICATION #superfamily protein-tyrosine kinase src; protein kinase !1homology; SH2 homology; SH3 homology KEYWORDS ATP; autophosphorylation; phosphoprotein; !1phosphotransferase; proto-oncogene; transforming protein; !1tyrosine-specific protein kinase FEATURE !$89-138 #domain SH3 homology #label SH3\ !$149-246 #domain SH2 homology #label SH2\ !$266-524 #domain protein kinase homology #label KIN\ !$274-282 #region protein kinase ATP-binding motif\ !$296 #binding_site ATP (Lys) #status predicted\ !$296 #active_site Lys #status predicted\ !$417,528 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 534 #molecular-weight 60267 #checksum 4864 SEQUENCE /// ENTRY OKHULK #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) lck - human ALTERNATE_NAMES kinase-related transforming protein (lck) ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 28-Jan-2000 ACCESSIONS JQ0152; S07822; S07200; S01879; S07143; A32797; I57636 REFERENCE JQ0152 !$#authors Rouer, E.; Van Huynh, T.; de Souza, S.L.; Lang, M.C.; !1Fischer, S.; Benarous, R. !$#journal Gene (1989) 84:105-113 !$#title Structure of the human lck gene: differences in genomic !1organisation within src-related genes affect only N-terminal !1exons. !$#cross-references MUID:90108697; PMID:2558056 !$#accession JQ0152 !'##molecule_type DNA !'##residues 1-509 ##label ROU !'##cross-references EMBL:X14053 REFERENCE S07822 !$#authors Perlmutter, R.M.; Marth, J.D.; Lewis, D.B.; Peet, R.; !1Ziegler, S.F.; Wilson, C.B. !$#journal J. Cell. Biochem. (1988) 38:117-126 !$#title Structure and expression of lck transcripts in human !1lymphoid cells. !$#cross-references MUID:89123626; PMID:3265417 !$#accession S07822 !'##molecule_type mRNA !'##residues 1-86,'P',88-509 ##label PER !'##cross-references EMBL:X13529; NID:g34294; PIDN:CAA31884.1; !1PID:g34295 REFERENCE S07200 !$#authors Koga, Y.; Caccia, N.; Toyonaga, B.; Spolski, R.; Yanagi, Y.; !1Yoshikai, Y.; Mak, T.W. !$#journal Eur. J. Immunol. (1986) 16:1643-1646 !$#title A human T cell-specific cDNA clone (YT16) encodes a protein !1with extensive homology to a family of protein-tyrosine !1kinases. !$#cross-references MUID:87133831; PMID:3493153 !$#accession S07200 !'##molecule_type mRNA !'##residues 1-205,'ASAITPI',212-257,'RCGW',262,'TTT',266,'T',268-281, !1'AGRLP',287-503,'STA' ##label KOG !'##cross-references EMBL:X05027; NID:g36807; PIDN:CAA28691.1; !1PID:g36808 REFERENCE S01879 !$#authors Veillette, A.; Foss, F.M.; Sausville, E.A.; Bolen, J.B.; !1Rosen, N. !$#journal Oncogene Res. (1987) 1:357-374 !$#title Expression of the lck tyrosine kinase gene in human colon !1carcinoma and other non-lymphoid human tumor cell lines. !$#cross-references MUID:88217332; PMID:2835736 !$#accession S01879 !'##molecule_type mRNA !'##residues 368-471,'H',473-509 ##label VEI !'##cross-references EMBL:X06369; NID:g34288; PIDN:CAA29667.1; !1PID:g34289 REFERENCE S07143 !$#authors Trevillyan, J.M.; Lin, Y.; Chen, S.J.; Phillips, C.A.; !1Canna, C.; Linna, T.J. !$#journal Biochim. Biophys. Acta (1986) 888:286-295 !$#title Human T lymphocytes express a protein-tyrosine kinase !1homologous to p56(LSTRA). !$#cross-references MUID:87000726; PMID:3489486 !$#accession S07143 !'##molecule_type mRNA !'##residues 'A',376-509 ##label TRE !'##cross-references EMBL:X04476; NID:g35779; PIDN:CAA28165.1; !1PID:g35780 REFERENCE A32797 !$#authors Takadera, T.; Leung, S.; Gernone, A.; Koga, Y.; Takihara, !1Y.; Miyamoto, N.G.; Mak, T.W. !$#journal Mol. Cell. Biol. (1989) 9:2173-2180 !$#title Structure of the two promoters of the human lck gene: !1differential accumulation of two classes of lck transcripts !1in T cells. !$#cross-references MUID:89313764; PMID:2787474 !$#accession A32797 !'##molecule_type DNA !'##residues 1-35 ##label TAK !'##cross-references GB:M26692; NID:g341523; PIDN:AAA59503.1; !1PID:g349702 REFERENCE I57636 !$#authors Garvin, A.M.; Pawar, S.; Marth, J.D.; Perlmutter, R.M. !$#journal Mol. Cell. Biol. (1988) 8:3058-3064 !$#title Structure of the murine lck gene and its rearrangement in a !1murine lymphoma cell line. !$#cross-references MUID:89096891; PMID:2850479 !$#accession I57636 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-35,'VR' ##label RES !'##cross-references GB:M21510; NID:g187031; PIDN:AAA59501.1; !1PID:g553522 COMMENT Protein tyrosine kinases play important roles in the control !1of cell growth and differentiation. GENETICS !$#gene GDB:LCK !'##cross-references GDB:119360; OMIM:153390 !$#map_position 1p35-1p34.3 !$#introns 35/3; 63/1; 93/2; 126/2; 161/1; 211/1; 262/1; 322/1; 347/3; !1399/1; 443/1 FUNCTION !$#description catalyzes the phosphorylation of a peptidyl tyrosine residue !1by ATP CLASSIFICATION #superfamily protein-tyrosine kinase src; protein kinase !1homology; SH2 homology; SH3 homology KEYWORDS ATP; autophosphorylation; blocked amino end; lipoprotein; !1myristylation; phosphoprotein; phosphotransferase; !1thiolester bond; tyrosine-specific protein kinase FEATURE !$2-509 #product protein-tyrosine kinase lck #status !8predicted #label MAT\ !$68-116 #domain SH3 homology #label SH3\ !$127-224 #domain SH2 homology #label SH2\ !$243-501 #domain protein kinase homology #label KIN\ !$251-259 #region protein kinase ATP-binding motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3,5 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$273 #active_site Lys #status predicted\ !$394,505 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 509 #molecular-weight 58000 #checksum 1143 SEQUENCE /// ENTRY I48845 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) lck, lymphocyte - mouse ALTERNATE_NAMES p56; protein-tyrosine kinase tck ORGANISM #formal_name Mus musculus #common_name house mouse DATE 18-Feb-2000 #sequence_revision 18-Feb-2000 #text_change 03-Mar-2000 ACCESSIONS I48845; A23639; I57629; I77452 REFERENCE I48845 !$#authors Voronova, A.F.; Sefton, B.M. !$#journal Nature (1986) 319:682-685 !$#title Expression of a new tyrosine protein kinase is stimulated by !1retrovirus promoter insertion. !$#cross-references MUID:86146842; PMID:3081813 !$#accession I48845 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-509 ##label VOR1 !'##cross-references EMBL:X03533; NID:g54813; PIDN:CAA27234.1; !1PID:g54814 REFERENCE A23639 !$#authors Marth, J.D.; Peet, R.; Krebs, E.G.; Perimutter, R.M. !$#journal Cell (1985) 43:393-404 !$#title A lymphocyte-specific protein-tyrosine kinase gene is !1rearranged and overexpressed in the murine T cell lymphoma !1LSTRA. !$#cross-references MUID:86079521; PMID:2416464 !$#accession A23639 !'##molecule_type mRNA !'##residues 1-282,'VP',285-509 ##label MAR !'##cross-references GB:M12056; NID:g198763 !'##note the sequence is revised in GenBank entry MUSLCK, release 116.0, !1(PIDN:AAB59674.1) REFERENCE I57629 !$#authors Voronova, A.F.; Adler, H.T.; Sefton, B.M. !$#journal Mol. Cell. Biol. (1987) 7:4407-4413 !$#title Two lck transcripts containing different 5' untranslated !1regions are present in t cells. !$#cross-references MUID:88142832; PMID:3501824 !$#accession I57629 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-11 ##label VOR !'##cross-references GB:M18098; NID:g198766; PIDN:AAA39421.1; !1PID:g198767 REFERENCE I57636 !$#authors Garvin, A.M.; Pawar, S.; Marth, J.D.; Perlmutter, R.M. !$#journal Mol. Cell. Biol. (1988) 8:3058-3064 !$#title Structure of the murine lck gene and its rearrangement in a !1murine lymphoma cell line. !$#cross-references MUID:89096891; PMID:2850479 !$#accession I77452 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-35,'VR' ##label GAR !'##cross-references GB:M21511; NID:g198768; PIDN:AAA39422.1; !1PID:g554186 CLASSIFICATION #superfamily protein-tyrosine kinase src; protein kinase !1homology; SH2 homology; SH3 homology KEYWORDS ATP; autophosphorylation; blocked amino end; kinase-related !1transforming protein; lipoprotein; myristylation; !1phosphoprotein; phosphotransferase; tyrosine-specific !1protein kinase FEATURE !$68-116 #domain SH3 homology #label SH3\ !$127-224 #domain SH2 homology #label SH2\ !$243-501 #domain protein kinase homology #label KIN\ !$251-259 #region protein kinase ATP-binding motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$273 #active_site Lys #status predicted\ !$394,505 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 509 #molecular-weight 57942 #checksum 1421 SEQUENCE /// ENTRY A39939 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) tkl [similarity] - chicken ALTERNATE_NAMES kinase-related transforming protein (tkl); T-cell surface antigen associated protein tkl ORGANISM #formal_name Gallus gallus #common_name chicken DATE 16-Jun-2000 #sequence_revision 16-Jun-2000 #text_change 16-Jun-2000 ACCESSIONS A42126; A39939 REFERENCE A42126 !$#authors Chow, L.M.; Ratcliffe, M.J.; Veillette, A. !$#journal Mol. Cell. Biol. (1992) 12:1226-1233 !$#title tkl is the avian homolog of the mammalian lck tyrosine !1protein kinase gene. !$#cross-references MUID:92186854; PMID:1545804 !$#accession A42126 !'##molecule_type mRNA !'##residues 1-88 ##label CHO !'##cross-references GB:M85043 !'##experimental_source thymus, spleen !'##note sequence extracted from NCBI backbone (NCBIN:88831, !1NCBIP:88833) REFERENCE A39939 !$#authors Strebhardt, K.; Mullins, J.I.; Bruck, C.; !1Ruebsamen-Waigmann, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:8778-8782 !$#title Additional member of the protein-tyrosine kinase family: the !1src-and lck-related protooncogene c-tkl. !$#cross-references MUID:88097370; PMID:3321053 !$#accession A39939 !'##molecule_type mRNA !'##residues 52-507 ##label STR !'##cross-references GB:J03579; NID:g212712; PIDN:AAA49081.1; !1PID:g212713 CLASSIFICATION #superfamily protein-tyrosine kinase src; protein kinase !1homology; SH2 homology; SH3 homology KEYWORDS ATP; autophosphorylation; blocked amino end; lipoprotein; !1myristylation; phosphoprotein; phosphotransferase; surface !1antigen; tyrosine-specific protein kinase FEATURE !$66-114 #domain SH3 homology #label SH3\ !$125-222 #domain SH2 homology #label SH2\ !$241-499 #domain protein kinase homology #label KIN\ !$249-257 #region protein kinase ATP-binding motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$392,503 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 507 #molecular-weight 58011 #checksum 4536 SEQUENCE /// ENTRY JQ1321 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) hck - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 04-Feb-2000 ACCESSIONS JQ1321; S18974 REFERENCE JQ1321 !$#authors Okano, Y.; Sugimoto, Y.; Fukuoka, M.; Matsui, A.; Nagata, !1K.; Nozawa, Y. !$#journal Biochem. Biophys. Res. Commun. (1991) 181:1137-1144 !$#title Identification of rat cDNA encoding hck tyrosine kinase from !1megakaryocytes. !$#cross-references MUID:92109719; PMID:1764064 !$#accession JQ1321 !'##molecule_type mRNA !'##residues 1-503 ##label OKA !'##cross-references GB:S74141; NID:g241436; PIDN:AAB20754.1; !1PID:g241437 !'##experimental_source megakaryocyte REFERENCE S18974 !$#authors Rema, V.; Swarup, G. !$#submission submitted to the EMBL Data Library, December 1991 !$#accession S18974 !'##status preliminary !'##molecule_type mRNA !'##residues 1-50,'V',52-204,'R',206-305,'T',307-503 ##label REM !'##cross-references EMBL:X62345; NID:g57581; PIDN:CAA44218.1; !1PID:g57582 GENETICS !$#gene hck CLASSIFICATION #superfamily protein-tyrosine kinase src; protein kinase !1homology; SH2 homology; SH3 homology KEYWORDS ATP; autophosphorylation; blocked amino end; kinase-related !1transforming protein; lipoprotein; myristylation; !1phosphoprotein; phosphotransferase; thiolester bond; !1tyrosine-specific protein kinase FEATURE !$62-110 #domain SH3 homology #label SH3\ !$121-218 #domain SH2 homology #label SH2\ !$237-495 #domain protein kinase homology #label KIN\ !$245-253 #region protein kinase ATP-binding motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$267 #active_site Lys #status predicted\ !$388 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 503 #molecular-weight 57016 #checksum 7976 SEQUENCE /// ENTRY A40092 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) blk [validated] - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 16-Jun-2000 #sequence_revision 16-Jun-2000 #text_change 16-Jun-2000 ACCESSIONS A40092 REFERENCE A40092 !$#authors Dymecki, S.M.; Niederhuber, J.E.; Desiderio, S.V. !$#journal Science (1990) 247:332-336 !$#title Specific expression of a tyrosine kinase gene, blk, in B !1lymphoid cells. !$#cross-references MUID:90117147; PMID:2404338 !$#accession A40092 !'##molecule_type mRNA !'##residues 1-499 ##label DYM !'##cross-references GB:M30903; NID:g202076; PIDN:AAA40453.1; !1PID:g202077 GENETICS !$#gene MGI:Blk !'##cross-references MGI:88169 !$#map_position 14:28.0 CLASSIFICATION #superfamily protein-tyrosine kinase src; protein kinase !1homology; SH2 homology; SH3 homology KEYWORDS ATP; autophosphorylation; blocked amino end; lipoprotein; !1myristylation; phosphoprotein; phosphotransferase; !1tyrosine-specific protein kinase FEATURE !$59-107 #domain SH3 homology #label SH3\ !$118-214 #domain SH2 homology #label SH2\ !$233-491 #domain protein kinase homology #label KIN\ !$241-249 #region protein kinase ATP-binding motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$263 #active_site Lys #status predicted SUMMARY #length 499 #molecular-weight 56644 #checksum 4536 SEQUENCE /// ENTRY A45501 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) yes [similarity] - African clawed frog ALTERNATE_NAMES kinase-related transforming protein (yes) ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 16-Jun-2000 #sequence_revision 16-Jun-2000 #text_change 16-Jun-2000 ACCESSIONS A45501; S08517 REFERENCE A45501 !$#authors Steele, R.E.; Irwin, M.Y.; Knudsen, C.L.; Collett, J.W.; !1Fero, J.B. !$#journal Oncogene Res. (1989) 1:223-233 !$#title The yes proto-oncogene is present in amphibians and !1contributes to the maternal RNA pool in the oocyte. !$#accession A45501 !'##molecule_type mRNA !'##residues 1-537 ##label STE !'##cross-references GB:X14377 REFERENCE S08517 !$#authors Steele, R.E.; Irwin, M.Y.; Knudsen, C.L.; Collett, J.W.; !1Fero, J.B. !$#submission submitted to the EMBL Data Library, February 1989 !$#accession S08517 !'##molecule_type mRNA !'##residues 1-250,'S',252-537 ##label ST2 !'##cross-references EMBL:X14377; NID:g65272; PIDN:CAA32551.1; !1PID:g65273 GENETICS !$#gene yes CLASSIFICATION #superfamily protein-tyrosine kinase src; protein kinase !1homology; SH2 homology; SH3 homology KEYWORDS ATP; autophosphorylation; blocked amino end; kinase-related !1transforming protein; lipoprotein; myristylation; !1phosphoprotein; phosphotransferase; tyrosine-specific !1protein kinase FEATURE !$92-141 #domain SH3 homology #label SH3\ !$152-249 #domain SH2 homology #label SH2\ !$269-527 #domain protein kinase homology #label KIN\ !$277-285 #region protein kinase ATP-binding motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$299 #active_site Lys #status predicted\ !$420,531 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 537 #molecular-weight 60371 #checksum 7604 SEQUENCE /// ENTRY S24550 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) 1 [similarity] - freshwater sponge (Spongilla lacustris) ALTERNATE_NAMES src-type tyrosine kinase 1 ORGANISM #formal_name Spongilla lacustris DATE 16-Jun-2000 #sequence_revision 16-Jun-2000 #text_change 16-Jun-2000 ACCESSIONS S24550 REFERENCE S24550 !$#authors Raulf, F. !$#submission submitted to the EMBL Data Library, September 1991 !$#accession S24550 !'##molecule_type mRNA !'##residues 1-505 ##label RAU !'##cross-references EMBL:X61601; NID:g10149; PIDN:CAA43798.1; !1PID:g10150 GENETICS !$#gene srk1 CLASSIFICATION #superfamily protein-tyrosine kinase src; protein kinase !1homology; SH2 homology; SH3 homology KEYWORDS ATP; blocked amino end; lipoprotein; myristylation; !1phosphotransferase; thiolester bond; tyrosine-specific !1protein kinase FEATURE !$61-111 #domain SH3 homology #label SH3\ !$122-214 #domain SH2 homology #label SH2\ !$238-496 #domain protein kinase homology #label KIN\ !$246-254 #region protein kinase ATP-binding motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$4,5 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$268 #active_site Lys #status predicted SUMMARY #length 505 #molecular-weight 57693 #checksum 3389 SEQUENCE /// ENTRY S24553 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) 4 [similarity] - freshwater sponge (Spongilla lacustris) ALTERNATE_NAMES src-type tyrosine kinase 4 ORGANISM #formal_name Spongilla lacustris DATE 16-Jun-2000 #sequence_revision 16-Jun-2000 #text_change 16-Jun-2000 ACCESSIONS S24553 REFERENCE S24550 !$#authors Raulf, F. !$#submission submitted to the EMBL Data Library, September 1991 !$#accession S24553 !'##molecule_type mRNA !'##residues 1-506 ##label RAU !'##cross-references EMBL:X61604; NID:g10155; PIDN:CAA43801.1; !1PID:g10156 GENETICS !$#gene srk4 CLASSIFICATION #superfamily protein-tyrosine kinase src; protein kinase !1homology; SH2 homology; SH3 homology KEYWORDS ATP; blocked amino end; lipoprotein; myristylation; !1phosphotransferase; thiolester bond; tyrosine-specific !1protein kinase FEATURE !$61-111 #domain SH3 homology #label SH3\ !$122-214 #domain SH2 homology #label SH2\ !$238-496 #domain protein kinase homology #label KIN\ !$246-254 #region protein kinase ATP-binding motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$4,5 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$268 #active_site Lys #status predicted SUMMARY #length 506 #molecular-weight 57561 #checksum 9002 SEQUENCE /// ENTRY TVFVMT #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) src - Rous sarcoma virus (strain PA101T) ORGANISM #formal_name Rous sarcoma virus DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 07-Nov-1997 ACCESSIONS A42994 REFERENCE A42994 !$#authors Dezelee, P.; Barnier, J.V.; Hampe, A.; Laugier, D.; Marx, !1M.; Galibert, F.; Calothy, G. !$#journal Virology (1992) 189:556-567 !$#title Small deletion in v-src SH3 domain of a transformation !1defective mutant of Rous sarcoma virus restores wild type !1transforming properties. !$#cross-references MUID:92351554; PMID:1322589 !$#accession A42994 !'##molecule_type DNA !'##residues 1-523 ##label DEZ !'##cross-references GB:M84475 GENETICS !$#gene src CLASSIFICATION #superfamily protein-tyrosine kinase src; protein kinase !1homology; SH2 homology; SH3 homology KEYWORDS ATP; autophosphorylation; blocked amino end; lipoprotein; !1myristylation; oncogene; phosphoprotein; phosphotransferase; !1tyrosine-specific protein kinase FEATURE !$85-134 #domain SH3 homology #label SH3\ !$145-242 #domain SH2 homology #label SH2\ !$262-520 #domain protein kinase homology #label KIN\ !$270-278 #region protein kinase ATP-binding motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$292 #active_site Lys #status predicted\ !$413 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status experimental SUMMARY #length 523 #molecular-weight 58778 #checksum 9950 SEQUENCE /// ENTRY TVFVPR #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) src - avian sarcoma virus PR2257 ORGANISM #formal_name avian sarcoma virus PR2257 DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 11-Jun-1999 ACCESSIONS A30174 REFERENCE A30174 !$#authors Geryk, J.; Dezelee, P.; Barnier, J.V.; Svoboda, J.; Nehyba, !1J.; Karakoz, I.; Rynditch, A.V.; Yatsula, B.A.; Calothy, G. !$#journal J. Virol. (1989) 63:481-492 !$#title Transduction of the cellular src gene and 3' adjacent !1sequences in avian sarcoma virus PR2257. !$#cross-references MUID:89094972; PMID:2463376 !$#accession A30174 !'##molecule_type DNA !'##residues 1-587 ##label GER !'##cross-references GB:M21526; NID:g210264; PIDN:AAA42583.1; !1PID:g210265 GENETICS !$#gene src CLASSIFICATION #superfamily protein-tyrosine kinase src; protein kinase !1homology; SH2 homology; SH3 homology KEYWORDS ATP; autophosphorylation; blocked amino end; lipoprotein; !1myristylation; oncogene; phosphoprotein; phosphotransferase; !1transforming protein; tyrosine-specific protein kinase FEATURE !$88-137 #domain SH3 homology #label SH3\ !$148-245 #domain SH2 homology #label SH2\ !$265-523 #domain protein kinase homology #label KIN\ !$273-281 #region protein kinase ATP-binding motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$295 #active_site Lys #status predicted\ !$416 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 587 #molecular-weight 65800 #checksum 2040 SEQUENCE /// ENTRY TVFVR #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) src - Rous sarcoma virus (strain Prague C) ORGANISM #formal_name Rous sarcoma virus DATE 01-Sep-1981 #sequence_revision 17-Dec-1982 #text_change 07-Nov-1997 ACCESSIONS A00632 REFERENCE A00632 !$#authors Schwartz, D.; Tizard, R.; Gilbert, W. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession A00632 !'##molecule_type genomic RNA !'##residues 1-526 ##label SCH !'##note as a result of base variations, residues 242 and 288 may be !1replaced by Thr and Gly, respectively REFERENCE A38019 !$#authors Neil, J.C.; Ghysdael, J.; Vogt, P.K.; Smart, J.E. !$#journal Nature (1981) 291:675-677 !$#title Homologous tyrosine phosphorylation sites in !1transformation-specific gene products of distinct avian !1sarcoma viruses. !$#cross-references MUID:81220979; PMID:6264320 !$#contents annotation; phosphorylation site GENETICS !$#gene src CLASSIFICATION #superfamily protein-tyrosine kinase src; protein kinase !1homology; SH2 homology; SH3 homology KEYWORDS ATP; autophosphorylation; blocked amino end; lipoprotein; !1myristylation; oncogene; phosphoprotein; phosphotransferase; !1tyrosine-specific protein kinase FEATURE !$88-137 #domain SH3 homology #label SH3\ !$148-245 #domain SH2 homology #label SH2\ !$265-523 #domain protein kinase homology #label KIN\ !$273-281 #region protein kinase ATP-binding motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$295 #active_site Lys #status predicted\ !$416 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status experimental SUMMARY #length 526 #molecular-weight 59130 #checksum 8117 SEQUENCE /// ENTRY OKFVYR #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) src - Rous sarcoma virus (strain H-19) ALTERNATE_NAMES kinase-related transforming protein src ORGANISM #formal_name Rous sarcoma virus DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 11-Jun-1999 ACCESSIONS S09609 REFERENCE S09609 !$#authors Bodor, J.; Poliak, E.; Pichrtova, J.; Geryk, J.; Svoboda, J. !$#journal Nucleic Acids Res. (1989) 17:8869 !$#title Complete nucleotide sequence of LTR, v-src, LTR provirus !1H-19. !$#cross-references MUID:90067864; PMID:2587228 !$#accession S09609 !'##status translation not shown !'##molecule_type DNA !'##residues 1-526 ##label BOD !'##cross-references EMBL:X15345; NID:g61706; PIDN:CAA33404.1; !1PID:g61707 GENETICS !$#gene src CLASSIFICATION #superfamily protein-tyrosine kinase src; protein kinase !1homology; SH2 homology; SH3 homology KEYWORDS ATP; autophosphorylation; blocked amino end; lipoprotein; !1myristylation; oncogene; phosphoprotein; phosphotransferase; !1transforming protein; tyrosine-specific protein kinase FEATURE !$88-137 #domain SH3 homology #label SH3\ !$148-245 #domain SH2 homology #label SH2\ !$265-523 #domain protein kinase homology #label KIN\ !$273-281 #region protein kinase ATP-binding motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$295 #active_site Lys #status predicted\ !$416 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 526 #molecular-weight 59075 #checksum 7672 SEQUENCE /// ENTRY TVFVS2 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) src - avian sarcoma virus S2 ORGANISM #formal_name avian sarcoma virus S2 DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 07-Nov-1997 ACCESSIONS B25375 REFERENCE A25375 !$#authors Ikawa, S.; Hagino-Yamagishi, K.; Kawai, S.; Yamamoto, T.; !1Toyoshima, K. !$#journal Mol. Cell. Biol. (1986) 6:2420-2428 !$#title Activation of the cellular src gene by transducing !1retrovirus. !$#cross-references MUID:87064539; PMID:3097513 !$#accession B25375 !'##molecule_type DNA !'##residues 1-557 ##label IKA GENETICS !$#gene src CLASSIFICATION #superfamily protein-tyrosine kinase src; protein kinase !1homology; SH2 homology; SH3 homology KEYWORDS ATP; autophosphorylation; blocked amino end; lipoprotein; !1myristylation; oncogene; phosphoprotein; phosphotransferase; !1transforming protein; tyrosine-specific protein kinase FEATURE !$88-137 #domain SH3 homology #label SH3\ !$148-245 #domain SH2 homology #label SH2\ !$265-523 #domain protein kinase homology #label KIN\ !$273-281 #region protein kinase ATP-binding motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$295 #active_site Lys #status predicted\ !$416 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 557 #molecular-weight 62582 #checksum 7810 SEQUENCE /// ENTRY TVFVS1 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) src - avian sarcoma virus S1 ORGANISM #formal_name avian sarcoma virus S1 DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 07-Nov-1997 ACCESSIONS A25375 REFERENCE A25375 !$#authors Ikawa, S.; Hagino-Yamagishi, K.; Kawai, S.; Yamamoto, T.; !1Toyoshima, K. !$#journal Mol. Cell. Biol. (1986) 6:2420-2428 !$#title Activation of the cellular src gene by transducing !1retrovirus. !$#cross-references MUID:87064539; PMID:3097513 !$#accession A25375 !'##molecule_type DNA !'##residues 1-568 ##label IKA GENETICS !$#gene src CLASSIFICATION #superfamily protein-tyrosine kinase src; protein kinase !1homology; SH2 homology; SH3 homology KEYWORDS ATP; autophosphorylation; blocked amino end; lipoprotein; !1myristylation; phosphoprotein; phosphotransferase; !1transforming protein; tyrosine-specific protein kinase FEATURE !$88-137 #domain SH3 homology #label SH3\ !$148-245 #domain SH2 homology #label SH2\ !$265-523 #domain protein kinase homology #label KIN\ !$273-281 #region protein kinase ATP-binding motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$295 #active_site Lys #status predicted\ !$416 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 568 #molecular-weight 63632 #checksum 4430 SEQUENCE /// ENTRY TVHUSY #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) fyn, splice form B [validated] - human ALTERNATE_NAMES fynB; p59(fyn); protein-tyrosine kinase slk; protein-tyrosine kinase syn; proto-oncogene fyn ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 23-Mar-2001 ACCESSIONS A24314; A25389; I59120; I79512 REFERENCE A24314 !$#authors Semba, K.; Nishizawa, M.; Miyajima, N.; Yoshida, M.C.; !1Sukegawa, J.; Yamanashi, Y.; Sasaki, M.; Yamamoto, T.; !1Toyoshima, K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:5459-5463 !$#title yes-related protooncogene, syn, belongs to the !1protein-tyrosine kinase family. !$#cross-references MUID:86287278; PMID:3526330 !$#accession A24314 !'##molecule_type mRNA !'##residues 1-537 ##label SEM !'##cross-references GB:M14333; NID:g181171; PIDN:AAC08285.1; !1PID:g181172 REFERENCE A25389 !$#authors Kawakami, T.; Pennington, C.Y.; Robbins, K.C. !$#journal Mol. Cell. Biol. (1986) 6:4195-4201 !$#title Isolation and oncogenic potential of a novel human src-like !1gene. !$#cross-references MUID:87089775; PMID:3099169 !$#accession A25389 !'##molecule_type mRNA !'##residues 1-183,'S',185-436,'R',438-537 ##label KAW1 !'##cross-references GB:M14676; NID:g338227; PIDN:AAA36615.1; !1PID:g338228 !'##note the authors translated the codon GAA for residue 265 as Gln and !1GGA for residue 278 as Gln REFERENCE I59120 !$#authors Kawakami, T.; Kawakami, Y.; Aaronson, S.A.; Robbins, K.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:3870-3874 !$#title Acquisition of transforming properties by FYN, a normal !1SRC-related human gene. !$#cross-references MUID:88234523; PMID:3287380 !$#accession I59120 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 514-522 ##label KAW2 !'##cross-references GB:M20284; NID:g182842; PIDN:AAA52491.1; !1PID:g182843 !'##experimental_source clone pFYN(c)-11; termination mutant p56(fyn) !$#accession I79512 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 514-524,'QRS' ##label KAW3 !'##cross-references GB:M20285; NID:g182844; PIDN:AAA52492.1; !1PID:g182845 !'##experimental_source clone pFYN(c)-21; recombinant mutant p57(fyn) REFERENCE A58826 !$#authors Peters, D.J.; McGrew, B.R.; Perron, D.C.; Liptak, L.M.; !1Laudano, A.P. !$#journal Oncogene (1990) 5:1313-1319 !$#title In vivo phosphorylation and membrane association of the fyn !1proto-oncogene product in IM-9 human lymphoblasts. !$#cross-references MUID:91016431; PMID:1699196 !$#contents annotation; myristylation; Tyr-531 phosphorylation REFERENCE A51398 !$#authors Noble, M.; Musacchio, A.; Saraste, M.; Wierenga, R. !$#submission submitted to the Brookhaven Protein Data Bank, May 1993 !$#cross-references PDB:1SHF !$#contents annotation; X-ray crystallography, 1.9 angstroms, residues !184-142 REFERENCE A58827 !$#authors Noble, M.E.M.; Musacchio, A.; Saraste, M.; Courtneidge, !1S.A.; Wierenga, R.K. !$#journal EMBO J. (1993) 12:2617-2624 !$#title Crystal structure of the SH3 domain in human Fyn; comparison !1of the three-dimensional structures of SH3 domains in !1tyrosine kinases and spectrin. !$#cross-references MUID:93327750; PMID:7687536 !$#contents annotation; X-ray crystallography, 1.9 angstroms REFERENCE A65653 !$#authors Musacchio, A.; Saraste, M.; Wilmanns, M. !$#submission submitted to the Brookhaven Protein Data Bank, May 1995 !$#cross-references PDB:1FYN !$#contents annotation; X-ray crystallography, 2.3 angstroms, residues !181-142 REFERENCE A58828 !$#authors Musacchio, A.; Saraste, M.; Wilmanns, M. !$#journal Nat. Struct. Biol. (1994) 1:546-551 !$#title High-resolution crystal structures of tyrosine kinase SH3 !1domains complexed with proline-rich peptides. !$#cross-references MUID:95393198; PMID:7664083 !$#contents annotation; X-ray crystallography, 2.3 angstroms REFERENCE A66268 !$#authors Morton, C.J.; Pugh, D.J.R.; Campbell, I.D. !$#submission submitted to the Brookhaven Protein Data Bank, April 1996 !$#cross-references PDB:1NYF !$#contents annotation; conformation by (1)H-NMR, residues 84-141 REFERENCE A66269 !$#authors Morton, C.J.; Pugh, D.J.R.; Campbell, I.D. !$#submission submitted to the Brookhaven Protein Data Bank, April 1996 !$#cross-references PDB:1NYG !$#contents annotation; conformation by (1)H-NMR, residues 84-141 GENETICS !$#gene GDB:FYN !'##cross-references GDB:118797; OMIM:137025 !$#map_position 6q21-6q21 COMPLEX monomer FUNCTION !$#description catalyzes the phosphorylation of a peptidyl tyrosine residue !1by ATP CLASSIFICATION #superfamily protein-tyrosine kinase src; protein kinase !1homology; SH2 homology; SH3 homology KEYWORDS alternative splicing; ATP; autophosphorylation; blocked !1amino end; lipoprotein; monomer; myristylation; !1phosphoprotein; phosphotransferase; proto-oncogene; !1thiolester bond; transforming protein; tyrosine-specific !1protein kinase FEATURE !$89-138 #domain SH3 homology #label SH3\ !$149-246 #domain SH2 homology #label SH2\ !$269-527 #domain protein kinase homology #label KIN\ !$277-285 #region protein kinase ATP-binding motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3,6 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$299 #active_site Lys #status predicted\ !$420 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted\ !$531 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status experimental SUMMARY #length 537 #molecular-weight 60761 #checksum 9747 SEQUENCE /// ENTRY TVHUHC #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) hck - human ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1989 #sequence_revision 10-Nov-1995 #text_change 11-Jun-1999 ACCESSIONS A27811; A27812; JC1149; C38268; S31103 REFERENCE A27811 !$#authors Quintrell, N.; Lebo, R.; Varmus, H.; Bishop, J.M.; !1Pettenati, M.J.; Le Beau, M.M.; Diaz, M.O.; Rowley, J.D. !$#journal Mol. Cell. Biol. (1987) 7:2267-2275 !$#title Identification of a human gene (HCK) that encodes a !1protein-tyrosine kinase and is expressed in hemopoietic !1cells. !$#cross-references MUID:87257942; PMID:3496523 !$#accession A27811 !'##molecule_type mRNA !'##residues 1-505 ##label QUI !'##cross-references GB:M16591 !'##note the codon given for 3-Cys (TCG) is inconsistent with the !1authors' translation REFERENCE A27812 !$#authors Ziegler, S.F.; Marth, J.D.; Lewis, D.B.; Perlmutter, R.M. !$#journal Mol. Cell. Biol. (1987) 7:2276-2285 !$#title Novel protein-tyrosine kinase gene (hck) preferentially !1expressed in cells of hematopoietic origin. !$#cross-references MUID:87257943; PMID:3453117 !$#accession A27812 !'##molecule_type mRNA !'##residues 1-505 ##label ZIE !'##cross-references GB:M16592; NID:g183913; PIDN:AAA52644.1; !1PID:g306833 REFERENCE JC1149 !$#authors Hradetzky, D.; Strebhardt, K.; Ruebsamen-Waigmann, H. !$#journal Gene (1992) 113:275-280 !$#title The genomic locus of the human hemopoietic-specific cell !1protein tyrosine kinase (PTK)-encoding gene (HCK) confirms !1conservation of exon-intron structure among human PTKs of !1the src family. !$#cross-references MUID:92241680; PMID:1572549 !$#accession JC1149 !'##molecule_type DNA !'##residues 157-505 ##label HRA !'##cross-references EMBL:X59741 REFERENCE A38268 !$#authors Partanen, J.; Maekelae, T.P.; Alitalo, R.; Lehvaeslaiho, H.; !1Alitalo, K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:8913-8917 !$#title Putative tyrosine kinases expressed in K-562 human leukemia !1cells. !$#cross-references MUID:91062389; PMID:2247464 !$#accession C38268 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type mRNA !'##residues 362-417 ##label PAR GENETICS !$#gene GDB:HCK !'##cross-references GDB:119303; OMIM:142370 !$#map_position 20q11-20q12 !$#introns 207/1; 258/1; 318/1; 343/3; 395/1; 439/1 FUNCTION !$#description catalyzes the phosphorylation of a peptidyl tyrosine residue !1by ATP CLASSIFICATION #superfamily protein-tyrosine kinase src; protein kinase !1homology; SH2 homology; SH3 homology KEYWORDS ATP; autophosphorylation; blocked amino end; lipoprotein; !1myristylation; phosphoprotein; phosphotransferase; !1thiolester bond; transforming protein; tyrosine-specific !1protein kinase FEATURE !$2-505 #product protein-tyrosine kinase hck #status !8predicted #label MAT\ !$64-112 #domain SH3 homology #label SH3\ !$123-220 #domain SH2 homology #label SH2\ !$239-497 #domain protein kinase homology #label KIN\ !$247-255 #region protein kinase ATP-binding motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$269 #active_site Lys #status predicted\ !$390 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 505 #molecular-weight 57312 #checksum 7314 SEQUENCE /// ENTRY TVMSHC #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) hck - mouse ALTERNATE_NAMES kinase-related transforming protein (bmk) ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 28-Jan-2000 ACCESSIONS A27282; A39973 REFERENCE A27282 !$#authors Klemsz, M.J.; McKercher, S.R.; Maki, R.A. !$#journal Nucleic Acids Res. (1987) 15:9600 !$#title Nucleotide sequence of the mouse hck gene. !$#cross-references MUID:88067781; PMID:3684607 !$#accession A27282 !'##molecule_type mRNA !'##residues 1-503 ##label KLE !'##cross-references GB:Y00487; NID:g51209; PIDN:CAA68544.1; PID:g51210 REFERENCE A39973 !$#authors Holtzman, D.A.; Cook, W.D.; Dunn, A.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:8325-8329 !$#title Isolation and sequence of a cDNA corresponding to a !1src-related gene expressed in murine hemopoietic cells. !$#cross-references MUID:88068587; PMID:3317404 !$#accession A39973 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-503 ##label HOL !'##cross-references GB:J03023; NID:g192212; PIDN:AAA37305.1; !1PID:g309118 GENETICS !$#gene hck CLASSIFICATION #superfamily protein-tyrosine kinase src; protein kinase !1homology; SH2 homology; SH3 homology KEYWORDS ATP; autophosphorylation; blocked amino end; lipoprotein; !1myristylation; phosphoprotein; phosphotransferase; !1thiolester bond; transforming protein; tyrosine-specific !1protein kinase FEATURE !$62-110 #domain SH3 homology #label SH3\ !$121-218 #domain SH2 homology #label SH2\ !$237-495 #domain protein kinase homology #label KIN\ !$245-253 #region protein kinase ATP-binding motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$267 #active_site Lys #status predicted\ !$388,499 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 503 #molecular-weight 56941 #checksum 8038 SEQUENCE /// ENTRY TVHUYS #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) yes-1 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 11-Jun-1999 ACCESSIONS A26714 REFERENCE A26714 !$#authors Sukegawa, J.; Semba, K.; Yamanashi, Y.; Nishizawa, M.; !1Miyajima, N.; Yamamoto, T.; Toyoshima, K. !$#journal Mol. Cell. Biol. (1987) 7:41-47 !$#title Characterization of cDNA clones for the human c-yes gene. !$#cross-references MUID:87172733; PMID:2436037 !$#accession A26714 !'##molecule_type mRNA !'##residues 1-543 ##label SUK !'##cross-references GB:M15990; NID:g181267; PIDN:AAA35735.1; !1PID:g181268 GENETICS !$#gene GDB:YES1 !'##cross-references GDB:119637; OMIM:164880 !$#map_position 18p11.31-18p11.22 FUNCTION !$#description catalyzes the phosphorylation of a peptidyl tyrosine residue !1by ATP CLASSIFICATION #superfamily protein-tyrosine kinase src; protein kinase !1homology; SH2 homology; SH3 homology KEYWORDS ATP; autophosphorylation; blocked amino end; lipoprotein; !1myristylation; phosphoprotein; phosphotransferase; !1proto-oncogene; thiolester bond; transforming protein; !1tyrosine-specific protein kinase FEATURE !$2-543 #product protein-tyrosine kinase yes-1 #status !8predicted #label MAT\ !$98-147 #domain SH3 homology #label SH3\ !$158-255 #domain SH2 homology #label SH2\ !$275-533 #domain protein kinase homology #label KIN\ !$283-291 #region protein kinase ATP-binding motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$305 #active_site Lys #status predicted\ !$426 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 543 #molecular-weight 60801 #checksum 2707 SEQUENCE /// ENTRY TVFVG9 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) yes - avian sarcoma virus Y73 ORGANISM #formal_name avian sarcoma virus Y73 #note host Gallus gallus (chicken) DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 23-Feb-1997 ACCESSIONS A00633 REFERENCE A00633 !$#authors Kitamura, N.; Kitamura, A.; Toyoshima, K.; Hirayama, Y.; !1Yoshida, M. !$#journal Nature (1982) 297:205-208 !$#title Avian sarcoma virus Y73 genome sequence and structural !1similarity of its transforming gene product to that of Rous !1sarcoma virus. !$#cross-references MUID:82195528; PMID:6281656 !$#accession A00633 !'##molecule_type genomic RNA !'##residues 1-528 ##label KIT COMMENT This protein is synthesized as a gag-yes polyprotein. GENETICS !$#gene yes CLASSIFICATION #superfamily protein-tyrosine kinase src; protein kinase !1homology; SH2 homology; SH3 homology KEYWORDS ATP; autophosphorylation; oncogene; phosphoprotein; !1phosphotransferase; transforming protein; tyrosine-specific !1protein kinase FEATURE !$88-137 #domain SH3 homology #label SH3\ !$148-245 #domain SH2 homology #label SH2\ !$265-523 #domain protein kinase homology #label KIN\ !$273-281 #region protein kinase ATP-binding motif\ !$295 #active_site Lys #status predicted\ !$416 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 528 #molecular-weight 59250 #checksum 5679 SEQUENCE /// ENTRY TVCHYS #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) yes - chicken ALTERNATE_NAMES kinase-related transforming protein yes ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Jun-1991 #sequence_revision 31-Dec-1991 #text_change 28-Jan-2000 ACCESSIONS S03324; S05283; S01689 REFERENCE S03324 !$#authors Zheng, X.; Podell, S.; Sefton, B.M.; Kaplan, P.L. !$#journal Oncogene (1989) 4:99-104 !$#title The sequence of chicken c-yes and p61(c-yes). !$#cross-references MUID:89128204; PMID:2464785 !$#accession S03324 !'##molecule_type mRNA !'##residues 1-541 ##label ZHE !'##cross-references EMBL:X13207 REFERENCE S05283 !$#authors Kaplan, P.L. !$#submission submitted to the EMBL Data Library, October 1988 !$#accession S05283 !'##molecule_type mRNA !'##residues 1-66,'IHPLR',72-81,'Q',83-541 ##label KAP !'##cross-references EMBL:X13207; NID:g63362; PIDN:CAA31595.1; !1PID:g63363 REFERENCE S01689 !$#authors Sudol, M.; Kieswetter, C.; Zhao, Y.H.; Dorai, T.; Wang, !1L.H.; Hanafusa, H. !$#journal Nucleic Acids Res. (1988) 16:9876 !$#title Nucleotide sequence of a cDNA for the chick yes !1proto-oncogene: comparison with the viral yes gene. !$#cross-references MUID:89041591; PMID:3054816 !$#accession S01689 !'##molecule_type mRNA !'##residues 1-237,'S',239-541 ##label SUD !'##cross-references EMBL:X12461 GENETICS !$#gene yes CLASSIFICATION #superfamily protein-tyrosine kinase src; protein kinase !1homology; SH2 homology; SH3 homology KEYWORDS ATP; autophosphorylation; blocked amino end; lipoprotein; !1myristylation; phosphoprotein; phosphotransferase; !1proto-oncogene; thiolester bond; tyrosine-specific protein !1kinase FEATURE !$2-541 #product protein-tyrosine kinase yes #status !8predicted #label MAT\ !$96-145 #domain SH3 homology #label SH3\ !$156-253 #domain SH2 homology #label SH2\ !$273-531 #domain protein kinase homology #label KIN\ !$281-289 #region protein kinase ATP-binding motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$303 #active_site Lys #status predicted\ !$424,535 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 541 #molecular-weight 60792 #checksum 4288 SEQUENCE /// ENTRY TVHUFR #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) fgr - human ALTERNATE_NAMES kinase-related transforming protein (fgr) ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1988 #sequence_revision 30-Sep-1989 #text_change 21-Jul-2000 ACCESSIONS A27676; A28353; A24842; A45930; S24306 REFERENCE A27676 !$#authors Katamine, S.; Notario, V.; Rao, C.D.; Miki, T.; Cheah, !1M.S.C.; Tronick, S.R.; Robbins, K.C. !$#journal Mol. Cell. Biol. (1988) 8:259-266 !$#title Primary structure of the human fgr proto-oncogene product !1p55(c-fgr). !$#cross-references MUID:88094395; PMID:3275868 !$#accession A27676 !'##molecule_type mRNA !'##residues 1-529 ##label REA !'##cross-references GB:M19722; GB:J03429; NID:g182573; PIDN:AAA52451.1; !1PID:g182574 REFERENCE A28353 !$#authors Inoue, K.; Ikawa, S.; Semba, K.; Sukegawa, J.; Yamamoto, T.; !1Toyoshima, K. !$#journal Oncogene (1987) 1:301-304 !$#title Isolation and sequencing of cDNA clones homologous to the !1v-fgr oncogene from a human B lymphocyte cell line, IM-9. !$#cross-references MUID:88262220; PMID:3330776 !$#accession A28353 !'##molecule_type mRNA !'##residues 1-143 ##label INO REFERENCE A24842 !$#authors Nishizawa, M.; Semba, K.; Yoshida, M.C.; Yamamoto, T.; !1Sasaki, M.; Toyoshima, K. !$#journal Mol. Cell. Biol. (1986) 6:511-517 !$#title Structure, expression, and chromosomal location of the human !1c-fgr gene. !$#cross-references MUID:87064334; PMID:3023853 !$#accession A24842 !'##molecule_type DNA !'##residues 111-416 ##label REB !'##cross-references GB:M12724; NID:g182581; PIDN:AAA52762.1; !1PID:g553286 REFERENCE A45930 !$#authors Brickell, P.M.; Patel, M. !$#journal Br. J. Cancer (1988) 58:704-709 !$#title Structure and expression of c-fgr protooncogene mRNA in !1Epstein-Barr virus converted cell lines. !$#cross-references MUID:89134667; PMID:2852026 !$#accession A45930 !'##molecule_type mRNA !'##residues 1-177;524-529 ##label BRI !'##cross-references GB:M27454 REFERENCE S24306 !$#authors Patel, M.; Leevers, S.J.; Brickell, P.M. !$#journal Oncogene (1990) 5:201-206 !$#title Structure of the complete human c-fgr proto-oncogene and !1identification of multiple transcriptional start sites. !$#cross-references MUID:90206622; PMID:1690869 !$#accession S24306 !'##status translation not shown !'##molecule_type DNA !'##residues 1-142 ##label PAT !'##cross-references EMBL:X52207; NID:g29893; PIDN:CAA36457.2; !1PID:g6006522 GENETICS !$#gene GDB:FGR !'##cross-references GDB:120615; OMIM:164940 !$#map_position 1p36.2-1p36.1 FUNCTION !$#description catalyzes the phosphorylation of a peptidyl tyrosine residue !1by ATP CLASSIFICATION #superfamily protein-tyrosine kinase src; protein kinase !1homology; SH2 homology; SH3 homology KEYWORDS ATP; autophosphorylation; blocked amino end; lipoprotein; !1myristylation; phosphoprotein; phosphotransferase; !1proto-oncogene; thiolester bond; transforming protein; !1tyrosine-specific protein kinase FEATURE !$84-133 #domain SH3 homology #label SH3\ !$144-241 #domain SH2 homology #label SH2\ !$261-519 #domain protein kinase homology #label KIN\ !$269-277 #region protein kinase ATP-binding motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3,6 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$291 #active_site Lys #status predicted\ !$523 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 529 #molecular-weight 59478 #checksum 2467 SEQUENCE /// ENTRY TVHAST #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) stk - Hydra attenuata ORGANISM #formal_name Hydra attenuata DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 04-Feb-2000 ACCESSIONS A34094 REFERENCE A34094 !$#authors Bosch, T.C.G.; Unger, T.F.; Fisher, D.A.; Steele, R.E. !$#journal Mol. Cell. Biol. (1989) 9:4141-4151 !$#title Structure and expression of STK, a src-related gene in the !1simple metazoan Hydra attenuata. !$#cross-references MUID:90066418; PMID:2479820 !$#accession A34094 !'##molecule_type mRNA !'##residues 1-509 ##label BOS !'##cross-references GB:M25245; NID:g159273; PIDN:AAA29217.1; !1PID:g159274 GENETICS !$#gene stk CLASSIFICATION #superfamily protein-tyrosine kinase src; protein kinase !1homology; SH2 homology; SH3 homology KEYWORDS ATP; autophosphorylation; blocked amino end; lipoprotein; !1myristylation; phosphoprotein; phosphotransferase; !1thiolester bond; transforming protein; tyrosine-specific !1protein kinase FEATURE !$66-115 #domain SH3 homology #label SH3\ !$126-218 #domain SH2 homology #label SH2\ !$238-497 #domain protein kinase homology #label KIN\ !$246-254 #region protein kinase ATP-binding motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$4 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$268 #active_site Lys #status predicted\ !$390 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 509 #molecular-weight 56885 #checksum 8721 SEQUENCE /// ENTRY S49016 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) brk - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S49016 REFERENCE S49016 !$#authors Mitchell, P.J.; Barker, K.T.; Martindale, J.E.; Kamalati, !1T.; Lowe, P.N.; Page, M.J.; Gusterson, B.A.; Crompton, M.R. !$#journal Oncogene (1994) 9:2383-2390 !$#title Cloning and characterisation of cDNAs encoding a novel !1non-receptor tyrosine kinase, brk, expressed in human breast !1tumours. !$#cross-references MUID:94309916; PMID:8036022 !$#accession S49016 !'##status preliminary !'##molecule_type mRNA !'##residues 1-451 ##label MIT !'##cross-references EMBL:X78549; NID:g515025; PIDN:CAA55295.1; !1PID:g515026 GENETICS !$#gene GDB:BRK !'##cross-references GDB:378058 CLASSIFICATION #superfamily protein-tyrosine kinase src; protein kinase !1homology; SH2 homology; SH3 homology KEYWORDS ATP; phosphotransferase; tyrosine-specific protein kinase FEATURE !$15-67 #domain SH3 homology #label SH3\ !$78-170 #domain SH2 homology #label SH2\ !$189-448 #domain protein kinase homology #label KIN\ !$197-205 #region protein kinase ATP-binding motif SUMMARY #length 451 #molecular-weight 51834 #checksum 5817 SEQUENCE /// ENTRY JH0559 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) CSK - human ALTERNATE_NAMES protein-tyrosine kinase cyl; protein-tyrosine kinase T2 ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1992 #sequence_revision 20-Aug-1994 #text_change 21-Jul-2000 ACCESSIONS JH0559; S38818; S19024; S19025 REFERENCE JH0559 !$#authors Braeuninger, A.; Holtrich, U.; Strebhardt, K.; !1Ruebsamen-Waigmann, H. !$#journal Gene (1992) 110:205-211 !$#title Isolation and characterization of a human gene that encodes !1a new subclass of protein tyrosine kinases. !$#cross-references MUID:92165060; PMID:1371489 !$#accession JH0559 !'##molecule_type mRNA !'##residues 1-450 ##label BRA !'##cross-references EMBL:X59932; NID:g30255; PIDN:CAA42556.1; !1PID:g30256 !'##experimental_source lung REFERENCE S38818 !$#authors Braeuninger, A.; Karn, T.; Strebhardt, K.; !1Ruebsamen-Waigmann, H. !$#journal Oncogene (1993) 8:1365-1369 !$#title Characterization of the human CSK locus. !$#cross-references MUID:93241739; PMID:7683131 !$#accession S38818 !'##status preliminary !'##molecule_type DNA !'##residues 1-450 ##label BR2 !'##cross-references EMBL:X74765; NID:g402582; PIDN:CAB58562.1; !1PID:g6077093 REFERENCE S19024 !$#authors Partanen, J.; Armstrong, E.; Bergman, M.; Maekelae, T.P.; !1Hirvonen, H.; Huebner, K.; Alitalo, K. !$#journal Oncogene (1991) 6:2013-2018 !$#title cyl encodes a putative cytoplasmic tyrosine kinase lacking !1the conserved tyrosine autophosphorylation site (Y416(src)). !$#cross-references MUID:92050797; PMID:1945408 !$#accession S19024 !'##status preliminary !'##molecule_type mRNA !'##residues 1-450 ##label PAR !'##cross-references EMBL:X60114; NID:g30314; PIDN:CAA42713.1; !1PID:g30315 REFERENCE S19025 !$#authors Holtrich, U.; Braeuninger, A.; Strebhardt, K.; !1Ruebsamen-Waigmann, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:10411-10415 !$#title Two additional protein-tyrosine kinases expressed in human !1lung: fourth member of the fibroblast growth factor receptor !1family and an intracellular protein-tyrosine kinase. !$#cross-references MUID:92073297; PMID:1720539 !$#accession S19025 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type mRNA !'##residues 1-450 ##label HOL !'##cross-references EMBL:X59932; NID:g30255; PIDN:CAA42556.1; !1PID:g30256 !'##note this sequence was submitted to the EMBL Data Library, June 1991 COMMENT This protein lacks the N-myristylation and !1autophosphorylation sites present in src and its close !1relations. GENETICS !$#gene GDB:CSK !'##cross-references GDB:131642; OMIM:124095 !$#map_position 15q23-15q25 !$#introns 5/3; 43/3; 81/2; 154/3; 186/1; 208/1; 241/2; 271/3; 296/2; !1361/3; 390/3 FUNCTION !$#description catalyzes the phosphorylation of a peptidyl tyrosine residue !1by ATP CLASSIFICATION #superfamily protein-tyrosine kinase src; protein kinase !1homology; SH2 homology; SH3 homology KEYWORDS ATP; phosphotransferase; tyrosine-specific protein kinase FEATURE !$16-65 #domain SH3 homology #label SH3\ !$82-171 #domain SH2 homology #label SH2\ !$193-447 #domain protein kinase homology #label KIN\ !$201-209 #region protein kinase ATP-binding motif\ !$222 #active_site Lys #status predicted SUMMARY #length 450 #molecular-weight 50704 #checksum 8131 SEQUENCE /// ENTRY S15094 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) CSK - rat ALTERNATE_NAMES c-src kinase; tyro-13 kinase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 11-Jun-1999 ACCESSIONS S15094; S18500; PT0195 REFERENCE S15094 !$#authors Nada, S.; Okada, M.; MacAuley, A.; Cooper, J.A.; Nakagawa, !1H. !$#journal Nature (1991) 351:69-72 !$#title Cloning of a complementary DNA for a protein-tyrosine kinase !1that specifically phosphorylates a negative regulatory site !1of p60(c-src). !$#cross-references MUID:91226538; PMID:1709258 !$#accession S15094 !'##molecule_type mRNA !'##residues 1-450 ##label NAD1 !'##cross-references EMBL:X58631; NID:g57507; PIDN:CAA41484.1; !1PID:g57508 !$#accession S18500 !'##molecule_type protein !'##residues 44-49;54-67;77-86;126-137;330-337;352-360;367-376;394-401 !1##label NAD REFERENCE PT0183 !$#authors Lai, C.; Lemke, G. !$#journal Neuron (1991) 6:691-704 !$#title An extended family of protein-tyrosine kinase genes !1differentially expressed in the vertebrate nervous system. !$#cross-references MUID:91222560; PMID:2025425 !$#accession PT0195 !'##molecule_type mRNA !'##residues 319-367 ##label LAI !'##experimental_source sciatic nerve GENETICS !$#gene tyro-13 CLASSIFICATION #superfamily protein-tyrosine kinase src; protein kinase !1homology; SH2 homology; SH3 homology KEYWORDS ATP; autophosphorylation; phosphoprotein; !1phosphotransferase; tyrosine-specific protein kinase FEATURE !$16-65 #domain SH3 homology #label SH3\ !$82-171 #domain SH2 homology #label SH2\ !$193-447 #domain protein kinase homology #label KIN\ !$201-209 #region protein kinase ATP-binding motif\ !$222 #active_site Lys #status predicted SUMMARY #length 450 #molecular-weight 50746 #checksum 8850 SEQUENCE /// ENTRY TVFFDS #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) src2 - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 11-Jun-1999 ACCESSIONS A27807 REFERENCE A27807 !$#authors Gregory, R.J.; Kammermeyer, K.L.; Vincent III, W.S.; !1Wadsworth, S.G. !$#journal Mol. Cell. Biol. (1987) 7:2119-2127 !$#title Primary sequence and developmental expression of a novel !1Drosophila melanogaster src gene. !$#cross-references MUID:87257924; PMID:3110602 !$#accession A27807 !'##molecule_type mRNA !'##residues 1-590 ##label GRE !'##cross-references GB:M16599; NID:g158498; PIDN:AAA28912.1; !1PID:g158499 !'##note the gene is designated as Dsrc28C GENETICS !$#gene src2 !'##cross-references FlyBase:FBgn0003502 !$#map_position 29A CLASSIFICATION #superfamily protein-tyrosine kinase src; protein kinase !1homology; SH2 homology; SH3 homology KEYWORDS ATP; autophosphorylation; phosphoprotein; !1phosphotransferase; transforming protein; tyrosine-specific !1protein kinase FEATURE !$152-201 #domain SH3 homology #label SH3\ !$214-307 #domain SH2 homology #label SH2\ !$328-588 #domain protein kinase homology #label KIN\ !$336-344 #region protein kinase ATP-binding motif\ !$358 #active_site Lys #status predicted\ !$481 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 590 #molecular-weight 65887 #checksum 6786 SEQUENCE /// ENTRY TVFFS #type fragment TITLE protein-tyrosine kinase (EC 2.7.1.112) src - fruit fly (Drosophila sp.) (fragment) ORGANISM #formal_name Drosophila sp. DATE 15-Nov-1984 #sequence_revision 15-Nov-1984 #text_change 23-Feb-1997 ACCESSIONS A00634 REFERENCE A00628 !$#authors Hoffmann, F.M.; Fresco, L.D.; Hoffman-Falk, H.; Shilo, B.Z. !$#journal Cell (1983) 35:393-401 !$#title Nucleotide sequences of the Drosophila src and abl homologs: !1conservation and variability in the src family oncogenes. !$#cross-references MUID:84082064; PMID:6317185 !$#accession A00634 !'##molecule_type DNA !'##residues 1-308 ##label HOF GENETICS !$#gene src !'##cross-references FlyBase:FBgn0003501 !$#introns 104/3 CLASSIFICATION #superfamily protein-tyrosine kinase src; protein kinase !1homology; SH2 homology; SH3 homology KEYWORDS ATP; autophosphorylation; phosphoprotein; !1phosphotransferase; tyrosine-specific protein kinase FEATURE !$38-299 #domain protein kinase homology #label KIN\ !$46-54 #region protein kinase ATP-binding motif\ !$68 #active_site Lys #status predicted\ !$190 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 308 #checksum 8338 SEQUENCE /// ENTRY S43532 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) spk-1 - planarian (Dugesia tigrina) ORGANISM #formal_name Dugesia tigrina DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 04-Feb-2000 ACCESSIONS S43532 REFERENCE S43532 !$#authors Burgaya, F.; Garcia-Fernandez, J.; Riutort, M.; Baguna, J.; !1Salo, E. !$#journal Oncogene (1994) 9:1267-1272 !$#title Structure and expression of Spk-1, an src-related gene !1product found in the planarian Dugesia (G) tigrina. !$#cross-references MUID:94181282; PMID:7510865 !$#accession S43532 !'##status preliminary !'##molecule_type mRNA !'##residues 1-497 ##label BUR !'##cross-references EMBL:X75310; NID:g471299; PIDN:CAA53058.1; !1PID:g471300 !'##note the authors translated the codon AAT for residue 176 as Asp and !1AGG for residue 356 as Thr CLASSIFICATION #superfamily protein-tyrosine kinase src; protein kinase !1homology; SH2 homology; SH3 homology KEYWORDS ATP; blocked amino end; lipoprotein; myristylation; !1phosphotransferase; thiolester bond; tyrosine-specific !1protein kinase FEATURE !$40-89 #domain SH3 homology #label SH3\ !$102-200 #domain SH2 homology #label SH2\ !$218-486 #domain protein kinase homology #label KIN\ !$226-234 #region protein kinase ATP-binding motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$9 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 497 #molecular-weight 57447 #checksum 4629 SEQUENCE /// ENTRY T01380 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) tec, splice form IV [similarity] - mouse CONTAINS protein tyrosine kinase tec, splice form III ORGANISM #formal_name Mus musculus #common_name house mouse DATE 16-Jun-2000 #sequence_revision 16-Jun-2000 #text_change 21-Jul-2000 ACCESSIONS T01380; JU0227; JU0228; JH0118 REFERENCE Z14312 !$#authors Mano, H.; Mano, K.; Tang, B.; Koehler, M.; Yi, T.; Gilbert, !1D.J.; Jenkins, N.A.; Copeland, N.G.; Ihle, J.N. !$#journal Oncogene (1993) 8:417-424 !$#title Expression of a novel form of Tec kinase in hematopoietic !1cells and mapping of the gene to chromosome 5 near Kit. !$#cross-references MUID:93149603; PMID:7678927 !$#accession T01380 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-630 ##label MAN1 !'##cross-references EMBL:S53716; NID:g264520; PIDN:AAA13515.2; !1PID:g5705900 REFERENCE JU0227 !$#authors Mano, H.; Sato, K.; Yazaki, Y.; Hirai, H. !$#submission submitted to JIPID, March 1993 !$#description The Tec protein-tyrosine kinase is involved in the IL-3 !1signaling pathway in a murine myeloid cell line. !$#accession JU0227 !'##molecule_type mRNA !'##residues 1-150,'RC',153-223,246-355,'A',357-482,'F',484-522,'C', !1524-589,'S',591-610,'F',612-630 ##label MAN2 !'##experimental_source splice form III REFERENCE JU0228 !$#authors Mano, H.; Sato, K.; Yazaki, Y.; Hirai, H. !$#submission submitted to JIPID, April 1993 !$#accession JU0228 !'##molecule_type DNA !'##residues 1-150,'RC',153-355,'A',357-482,'F',484-522,'C',524-589,'S', !1591-610,'F',612-630 ##label MAN3 !'##experimental_source myeloid; splice form IV REFERENCE JH0112 !$#authors Wilks, A.F.; Kurban, R.R.; Hovens, C.M.; Ralph, S.J. !$#journal Gene (1989) 85:67-74 !$#title The application of the polymerase chain reaction to cloning !1members of the protein tyrosine kinase family. !$#cross-references MUID:90152381; PMID:2482828 !$#accession JH0118 !'##molecule_type mRNA !'##residues 485-534,'E',536-549,'Y',551 ##label WIL !'##cross-references GB:M33427; NID:g200579; PIDN:AAA40018.1; !1PID:g200580 !'##experimental_source haemopoietic cell, clone W3.13 !'##note the authors translated the codon TAT for residue 550 as Phe GENETICS !$#gene tec !$#map_position 5 CLASSIFICATION #superfamily protein-tyrosine kinase tec; pleckstrin repeat !1homology; protein kinase homology; SH2 homology; SH3 !1homology KEYWORDS ATP; kinase-related transforming protein; phosphoprotein; !1phosphotransferase; tyrosine-specific protein kinase FEATURE !$1-630 #product protein-tyrosine kinase (EC 2.7.1.112) tec, !8splice form IV #status predicted #label SF4\ !$1-223,246-630 #product protein-tyrosine kinase (EC 2.7.1.112) tec, !8splice form III #status predicted #label SF3\ !$3-109 #domain pleckstrin repeat homology #label PLK\ !$185-233 #domain SH3 homology #label SH3\ !$246-344 #domain SH2 homology #label SH2\ !$367-625 #domain protein kinase homology #label KIN\ !$375-383 #region protein kinase ATP-binding motif\ !$515 #active_site Asp (aspartylphosphate intermediate) !8#status predicted\ !$518 #binding_site phosphate (Tyr) (covalent) #status !8predicted SUMMARY #length 630 #molecular-weight 73426 #checksum 5740 SEQUENCE /// ENTRY S33253 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112), T-cell-specific itk/ tsk/emt - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S33253 REFERENCE S33253 !$#authors Tanaka, N.; Asao, H.; Ohtani, K.; Nakamura, M.; Sugamura, K. !$#journal FEBS Lett. (1993) 324:1-5 !$#title A novel human tyrosine kinase gene inducible in T cells by !1interleukin 2. !$#cross-references MUID:93279365; PMID:8504851 !$#accession S33253 !'##status preliminary !'##molecule_type mRNA !'##residues 1-620 ##label TAN !'##cross-references EMBL:D13720; NID:g399657; PIDN:BAA02873.1; !1PID:g399658 GENETICS !$#gene GDB:ITK; EMT !'##cross-references GDB:207268; OMIM:186973 !$#map_position 5q31-5q32 CLASSIFICATION #superfamily protein-tyrosine kinase tec; pleckstrin repeat !1homology; protein kinase homology; SH2 homology; SH3 !1homology KEYWORDS ATP; autophosphorylation; phosphoprotein; !1phosphotransferase; tyrosine-specific protein kinase FEATURE !$3-109 #domain pleckstrin repeat homology #label PLK\ !$178-226 #domain SH3 homology #label SH3\ !$239-338 #domain SH2 homology #label SH2\ !$361-619 #domain protein kinase homology #label KIN\ !$369-377 #region protein kinase ATP-binding motif SUMMARY #length 620 #molecular-weight 71830 #checksum 8123 SEQUENCE /// ENTRY A43030 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) itk/emt - mouse ALTERNATE_NAMES interleukin-2 inducible protein-tyrosine kinase (itk); p72 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 18-Feb-2000 #sequence_revision 18-Feb-2000 #text_change 18-Feb-2000 ACCESSIONS A43030; A47333; JN0472 REFERENCE A43030 !$#authors Siliciano, J.D.; Morrow, T.A.; Desiderio, S.V. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:11194-11198 !$#title itk, a T-cell-specific tyrosine kinase gene inducible by !1interleukin 2. !$#cross-references MUID:93087493; PMID:1280821 !$#accession A43030 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-625 ##label SIL !'##cross-references GB:L00619; NID:g198462; PIDN:AAA39337.1; !1PID:g198463 !'##experimental_source CTLL-2 T-cells !'##note sequence extracted from NCBI backbone (NCBIP:119755) REFERENCE A47333 !$#authors Heyeck, S.D.; Berg, L.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:669-673 !$#title Developmental regulation of a murine T-cell-specific !1tyrosine kinase gene, Tsk. !$#cross-references MUID:93133848; PMID:8421704 !$#accession A47333 !'##status preliminary !'##molecule_type mRNA !'##residues 1-81,88-157,'R',159-625 ##label HEY !'##cross-references GB:L05631; NID:g293854; PIDN:AAA40518.1; !1PID:g293855 !'##note sequence extracted from NCBI backbone (NCBIN:122843, !1NCBIP:122846) REFERENCE JN0471 !$#authors Yamada, N.; Kawakami, Y.; Kimura, H.; Fukamachi, H.; Baier, !1G.; Altman, A.; Kato, T.; Inagaki, Y.; Kawakami, T. !$#journal Biochem. Biophys. Res. Commun. (1993) 192:231-240 !$#title Structure and expression of novel protein-tyrosine kinases, !1Emb and Emt, in the hematopoietic cells. !$#cross-references MUID:93236578; PMID:8476425 !$#accession JN0472 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-81,88-534,'S',536-539,'C',541-625 ##label YAM !'##cross-references GB:L10628; NID:g193018 !'##note this translation is not annotated in GenBank entry MUSEMTX, !1release 116.0 GENETICS !$#gene itk; emt CLASSIFICATION #superfamily protein-tyrosine kinase tec; pleckstrin repeat !1homology; protein kinase homology; SH2 homology; SH3 !1homology KEYWORDS ATP; autophosphorylation; phosphoprotein; !1phosphotransferase; tyrosine-specific protein kinase FEATURE !$3-115 #domain pleckstrin repeat homology #label PLK\ !$159-169 #region proline-rich\ !$184-232 #domain SH3 homology #label SH3\ !$245-343 #domain SH2 homology #label SH2\ !$366-624 #domain protein kinase homology #label KIN\ !$374-382 #region protein kinase ATP-binding motif\ !$517 #binding_site phosphate (Tyr) (covalent) #status !8predicted SUMMARY #length 625 #molecular-weight 72291 #checksum 382 SEQUENCE /// ENTRY TVMVRR #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) fgr - feline sarcoma virus (strain Gardner-Rasheed) ORGANISM #formal_name feline sarcoma virus #note host Felis sp. (cat) DATE 27-Nov-1985 #sequence_revision 26-May-1995 #text_change 31-Mar-2000 ACCESSIONS A00653; A03937 REFERENCE A00653 !$#authors Naharro, G.; Robbins, K.C.; Reddy, E.P. !$#journal Science (1984) 223:63-66 !$#title Gene product of v-fgr onc: hybrid protein containing a !1portion of actin and a tyrosine-specific protein kinase. !$#cross-references MUID:84097512; PMID:6318314 !$#accession A00653 !'##molecule_type DNA !'##residues 1-663 ##label NAH !'##cross-references GB:X00255; GB:K01487; NID:g61542; PIDN:CAA25063.1; !1PID:g61543 !'##note the authors translated the codon GAT for residue 14 as Glu COMMENT This protein is synthesized as a gag-fgr polyprotein. GENETICS !$#gene fgr CLASSIFICATION #superfamily feline sarcoma virus protein-tyrosine kinase !1fgr; protein kinase homology; SH2 homology KEYWORDS ATP; autophosphorylation; oncogene; phosphoprotein; !1phosphotransferase; polyprotein; transforming protein; !1tyrosine-specific protein kinase FEATURE !$1-118 #region gag polyprotein similarity\ !$141-268 #region actin similarity\ !$285-382 #domain SH2 homology #label SH2\ !$402-660 #domain protein kinase homology #label KIN\ !$410-418 #region protein kinase ATP-binding motif\ !$432 #active_site Lys #status predicted SUMMARY #length 663 #molecular-weight 74916 #checksum 4874 SEQUENCE /// ENTRY A53596 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) syk - human ALTERNATE_NAMES protein-tyrosine kinase Syk41 CONTAINS protein-tyrosine kinase Syk11 ORGANISM #formal_name Homo sapiens #common_name man DATE 07-Oct-1994 #sequence_revision 23-May-1997 #text_change 21-Jul-2000 ACCESSIONS A53596; JC2198; JC2197; I38137 REFERENCE A53596 !$#authors Law, C.L.; Sidorenko, S.P.; Chandran, K.A.; Draves, K.E.; !1Chan, A.C.; Weiss, A.; Edelhoff, S.; Disteche, C.M.; Clark, !1E.A. !$#journal J. Biol. Chem. (1994) 269:12310-12319 !$#title Molecular cloning of human Syk. A B cell protein-tyrosine !1kinase associated with the surface immunoglobulin M-B cell !1receptor complex. !$#cross-references MUID:94216354; PMID:8163536 !$#accession A53596 !'##status preliminary !'##molecule_type mRNA !'##residues 1-635 ##label LAW !'##cross-references GB:L28824; NID:g479012; PIDN:AAA36526.1; !1PID:g479013 REFERENCE JC2197 !$#authors Yagi, S.; Suzuki, K.; Hasegawa, A.; Okumura, K.; Ra, C. !$#journal Biochem. Biophys. Res. Commun. (1994) 200:28-34 !$#title Cloning of the cDNA for the deleted syk kinase homologous to !1ZAP-70 from human basophilic leukemia cell line (KU812). !$#cross-references MUID:94220098; PMID:7513161 !$#accession JC2198 !'##molecule_type mRNA !'##residues 1-281,283-305,'A',306-635 ##label YAG !'##cross-references GB:Z29630; NID:g496899 !'##experimental_source blood, basophilic leukemia cell line KU812 !$#accession JC2197 !'##molecule_type mRNA !'##residues 1-282,306-635 ##label YA2 !'##cross-references GB:Z29630; NID:g496899; PIDN:CAA82737.1; !1PID:g496900 !'##experimental_source blood, basophilic leukemia cell line KU812 REFERENCE I38137 !$#authors Muller, B.; Cooper, L.; Terhorst, C. !$#journal Immunogenetics (1994) 39:359-362 !$#title Molecular cloning of the human homologue to the pig !1protein-tyrosine kinase syk. !$#cross-references MUID:94222446; PMID:8168854 !$#accession I38137 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 6-118,'A',120-249,'P',251-635 ##label RES !'##cross-references EMBL:X73568; NID:g515870; PIDN:CAA51970.1; !1PID:g515871 GENETICS !$#gene GDB:SYK !'##cross-references GDB:354405; OMIM:600085 !$#map_position 9q22-9q22 FUNCTION !$#description catalyzes the phosphorylation of a peptidyl tyrosine residue !1by ATP CLASSIFICATION #superfamily protein-tyrosine kinase ZAP-70; protein kinase !1homology; SH2 homology KEYWORDS ATP; autophosphorylation; phosphoprotein; !1phosphotransferase; tyrosine-specific protein kinase FEATURE !$15-107 #domain SH2 homology #label SH2A\ !$168-259 #domain SH2 homology #label SH2B\ !$369-633 #domain protein kinase homology #label KIN\ !$377-385 #region protein kinase ATP-binding motif SUMMARY #length 635 #molecular-weight 72066 #checksum 2334 SEQUENCE /// ENTRY A56707 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) syk, splice form B - rat CONTAINS protein-tyrosine kinase Syk, splice form A ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 19-Oct-1995 #sequence_revision 23-May-1997 #text_change 10-Sep-1999 ACCESSIONS A56707; B56707; A48875 REFERENCE A56707 !$#authors Rowley, R.B.; Bolen, J.B.; Fargnoli, J. !$#journal J. Biol. Chem. (1995) 270:12659-12664 !$#title Molecular cloning of rodent p72(Syk). Evidence of !1alternative mRNA splicing. !$#cross-references MUID:95279402; PMID:7759516 !$#accession A56707 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-628 ##label ROW !'##cross-references GB:U21684 !$#accession B56707 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-275,299-628 ##label RO2 !'##cross-references GB:U21683 REFERENCE A48875 !$#authors Benhamou, M.; Ryba, N.J.P.; Nishikata, H.; Kihara, H.; !1Siraganian, R.P. !$#journal J. Biol. Chem. (1993) 268:23318-23324 !$#title Protein tyrosine kinase p72syk in high affinity IgE receptor !1signaling: identification as a component of pp72 and !1association with the gamma chain of the receptor after !1receptor aggregation. !$#cross-references MUID:94043123; PMID:7693687 !$#accession A48875 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 15-22,'E',23-263,'M',265-269,'S',271-444,'EL',447-628 !1##label RES !'##cross-references GB:L20838; NID:g416152; PIDN:AAA42308.1; !1PID:g416153 CLASSIFICATION #superfamily protein-tyrosine kinase ZAP-70; protein kinase !1homology; SH2 homology KEYWORDS alternative splicing; ATP; autophosphorylation; !1phosphoprotein; phosphotransferase; tyrosine-specific !1protein kinase FEATURE !$1-628 #product protein-tyrosine kinase syk, splice form B !8#status predicted #label PRB\ !$1-275,299-628 #product protein-tyrosine kinase syk, splice form A !8#status predicted #label PRA\ !$14-105 #domain SH2 homology #label SH2A\ !$166-257 #domain SH2 homology #label SH2B\ !$362-626 #domain protein kinase homology #label KIN\ !$370-378 #region protein kinase ATP-binding motif SUMMARY #length 628 #molecular-weight 71431 #checksum 6141 SEQUENCE /// ENTRY A40802 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) syk 72K chain - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A40802 REFERENCE A40802 !$#authors Taniguchi, T.; Kobayashi, T.; Kondo, J.; Takahashi, K.; !1Nakamura, H.; Suzuki, J.; Nagai, K.; Yamada, T.; Nakamura, !1S.; Yamamura, H. !$#journal J. Biol. Chem. (1991) 266:15790-15796 !$#title Molecular cloning of a porcine gene syk that encodes a !172-kDa protein-tyrosine kinase showing high susceptibility !1to proteolysis. !$#cross-references MUID:91340718; PMID:1874735 !$#accession A40802 !'##molecule_type mRNA !'##residues 1-628 ##label TAN !'##cross-references GB:M73237; NID:g164630; PIDN:AAA31112.1; !1PID:g164631 CLASSIFICATION #superfamily protein-tyrosine kinase ZAP-70; protein kinase !1homology; SH2 homology KEYWORDS ATP; autophosphorylation; phosphoprotein; !1phosphotransferase; tyrosine-specific protein kinase FEATURE !$10-102 #domain SH2 homology #label SH2A\ !$163-253 #domain SH2 homology #label SH2B\ !$362-626 #domain protein kinase homology #label KIN\ !$370-378 #region protein kinase ATP-binding motif SUMMARY #length 628 #molecular-weight 71619 #checksum 4794 SEQUENCE /// ENTRY A41687 #type complete TITLE ribosomal protein S6 kinase (EC 2.7.1.-), long splice form - human ALTERNATE_NAMES insulin/mitogen-activated cytosolic p70 S6 kinase (S6K); nuclear p85 S6 kinase CONTAINS ribosomal protein S6 kinase short splice form; ribosomal protein S6 kinase, long splice form ORGANISM #formal_name Homo sapiens #common_name man DATE 05-Feb-1999 #sequence_revision 05-Feb-1999 #text_change 11-Jun-1999 ACCESSIONS A41687; B41687 REFERENCE A41687 !$#authors Grove, J.R.; Banerjee, P.; Balasubramanyam, A.; Coffer, !1P.J.; Price, D.J.; Avruch, J.; Woodgett, J.R. !$#journal Mol. Cell. Biol. (1991) 11:5541-5550 !$#title Cloning and expression of two human p70 S6 kinase !1polypeptides differing only at their amino termini. !$#cross-references MUID:92017834; PMID:1922062 !$#accession A41687 !'##molecule_type mRNA !'##residues 1-525 ##label GRO1 !'##cross-references GB:M60724; NID:g189507; PIDN:AAA36410.1; !1PID:g189508 !$#accession B41687 !'##molecule_type mRNA !'##residues 24-525 ##label GRO2 !'##cross-references GB:M60725; NID:g189509; PIDN:AAA36411.1; !1PID:g189510 COMMENT This enzyme phosphorylates ribosomal protein S6 (see !1PIR:R3HU6). The long splice form localizes in the nucleus. GENETICS !$#gene GDB:RPS6KB1 !'##cross-references GDB:365650 COMPLEX monomer FUNCTION !$#description catalyzes the phosphorylation by ATP of specific serine !1residues in ribosomal protein S6 !$#note reversibly activated by phosphorylation CLASSIFICATION #superfamily ribosomal protein S6 kinase; protein kinase !1homology KEYWORDS alternative initiators; ATP; monomer; nucleus; !1phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$1-525 #product ribosomal protein S6 kinase, long splice !8form #status predicted #label SFL\ !$2-19 #region nuclear location signal\ !$24-525 #product ribosomal protein S6 kinase, short splice !8form #status predicted #label SFS\ !$89-352 #domain protein kinase homology #label KIN\ !$97-105 #region protein kinase ATP-binding motif\ !$423-450 #region autoinhibitory\ !$434,441,447,452 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$444 #binding_site phosphate (Thr) (covalent) #status !8predicted SUMMARY #length 525 #molecular-weight 59139 #checksum 3800 SEQUENCE /// ENTRY TVRTK6 #type complete TITLE ribosomal protein S6 kinase (EC 2.7.1.-), 70K - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 11-Jun-1999 ACCESSIONS A36484; A34992; A38279 REFERENCE A36484 !$#authors Banerjee, P.; Ahmad, M.F.; Grove, J.R.; Kozlosky, C.; Price, !1D.J.; Avruch, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:8550-8554 !$#title Molecular structure of a major insulin/mitogen-activated !170-kDa S6 protein kinase. !$#cross-references MUID:91046033; PMID:2236064 !$#accession A36484 !'##molecule_type mRNA !'##residues 1-525 ##label BAN1 !'##cross-references GB:M58340; GB:M37777; NID:g206841; PIDN:AAA42104.1; !1PID:g206842 !$#accession A34992 !'##molecule_type protein !'##residues 57-64;105-108;195,'S', !1197-202;206-223;262-264;336-353;438-442;444-450;492,'X', !1494-498;'T',518-521 ##label BAN REFERENCE A38279 !$#authors Kozma, S.C.; Ferrari, S.; Bassand, P.; Siegmann, M.; Totty, !1N.; Thomas, G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:7365-7369 !$#title Cloning of the mitogen-activated S6 kinase from rat liver !1reveals an enzyme of the second messenger subfamily. !$#cross-references MUID:91017506; PMID:1699226 !$#accession A38279 !'##status preliminary !'##molecule_type mRNA !'##residues 24-366,'P',368-525 ##label KOZ !'##cross-references GB:M57428; GB:M35864; NID:g206839; PIDN:AAA42103.1; !1PID:g206840 CLASSIFICATION #superfamily ribosomal protein S6 kinase; protein kinase !1homology KEYWORDS ATP; phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$1-88 #domain amino-terminal #label NTD\ !$29-46 #region acidic\ !$89-352 #domain protein kinase homology #label KIN\ !$97-105 #region protein kinase ATP-binding motif\ !$353-420 #domain catalytic domain extension #label CDE\ !$421-525 #domain carboxyl-terminal #label CTD\ !$123 #active_site Lys #status predicted\ !$434,441,447,452 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$444 #binding_site phosphate (Thr) (covalent) #status !8predicted SUMMARY #length 525 #molecular-weight 59190 #checksum 4146 SEQUENCE /// ENTRY S12906 #type complete TITLE probable ribosomal protein S6 kinase (EC 2.7.1.-), 59K - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S12906 REFERENCE S12906 !$#authors Harmann, B.; Kilimann, M.W. !$#journal FEBS Lett. (1990) 273:248-252 !$#title cDNA encoding a 59 kDa homolog of ribosomal protein S6 !1kinase from rabbit liver. !$#cross-references MUID:91032193; PMID:1699810 !$#accession S12906 !'##molecule_type mRNA !'##residues 1-525 ##label HAR !'##cross-references EMBL:X54415; NID:g1561; PIDN:CAA38279.1; PID:g1562 CLASSIFICATION #superfamily ribosomal protein S6 kinase; protein kinase !1homology KEYWORDS ATP; phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$89-352 #domain protein kinase homology #label KIN\ !$97-105 #region protein kinase ATP-binding motif SUMMARY #length 525 #molecular-weight 59109 #checksum 4024 SEQUENCE /// ENTRY B32571 #type complete TITLE ribosomal protein S6 kinase II (EC 2.7.1.-) alpha chain homolog (clone Mu6A) - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B32571 REFERENCE A93113 !$#authors Alcorta, D.A.; Crews, C.M.; Sweet, L.J.; Bankston, L.; !1Jones, S.W.; Erikson, R.L. !$#journal Mol. Cell. Biol. (1989) 9:3850-3859 !$#title Sequence and expression of chicken and mouse rsk: homologs !1of Xenopus laevis ribosomal S6 kinase. !$#cross-references MUID:89384612; PMID:2779569 !$#accession B32571 !'##molecule_type mRNA !'##residues 1-724 ##label ALC !'##cross-references GB:M23489 CLASSIFICATION #superfamily ribosomal protein S6 kinase II; protein kinase !1homology KEYWORDS ATP; phosphotransferase; serine/threonine-specific protein !1kinase FEATURE !$60-310 #domain protein kinase homology #label KIN1\ !$68-76 #region protein kinase ATP-binding motif\ !$405-664 #domain protein kinase homology #label KIN2 SUMMARY #length 724 #molecular-weight 81594 #checksum 4206 SEQUENCE /// ENTRY A32571 #type complete TITLE ribosomal protein S6 kinase II (EC 2.7.1.-) alpha chain homolog - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A32571 REFERENCE A93113 !$#authors Alcorta, D.A.; Crews, C.M.; Sweet, L.J.; Bankston, L.; !1Jones, S.W.; Erikson, R.L. !$#journal Mol. Cell. Biol. (1989) 9:3850-3859 !$#title Sequence and expression of chicken and mouse rsk: homologs !1of Xenopus laevis ribosomal S6 kinase. !$#cross-references MUID:89384612; PMID:2779569 !$#accession A32571 !'##molecule_type mRNA !'##residues 1-752 ##label ALC !'##cross-references GB:M28488; NID:g551555; PIDN:AAA21877.1; !1PID:g551556 CLASSIFICATION #superfamily ribosomal protein S6 kinase II; protein kinase !1homology KEYWORDS ATP; phosphotransferase; serine/threonine-specific protein !1kinase FEATURE !$78-339 #domain protein kinase homology #label KIN1\ !$86-94 #region protein kinase ATP-binding motif\ !$433-692 #domain protein kinase homology #label KIN2 SUMMARY #length 752 #molecular-weight 84439 #checksum 3573 SEQUENCE /// ENTRY B30001 #type complete TITLE ribosomal protein S6 kinase (EC 2.7.1.-) II alpha chain - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 24-Sep-1999 ACCESSIONS B30001 REFERENCE A30001 !$#authors Jones, S.W.; Erikson, E.; Blenis, J.; Maller, J.L.; Erikson, !1R.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:3377-3381 !$#title A Xenopus ribosomal protein S6 kinase has two apparent !1kinase domains that are each similar to distinct protein !1kinases. !$#cross-references MUID:88217904; PMID:3368449 !$#accession B30001 !'##molecule_type mRNA !'##residues 1-733 ##label JON !'##cross-references GB:M20187; NID:g214786; PIDN:AAA49958.1; !1PID:g214787; GB:J03775 CLASSIFICATION #superfamily ribosomal protein S6 kinase II; protein kinase !1homology KEYWORDS ATP; phosphotransferase; serine/threonine-specific protein !1kinase FEATURE !$60-321 #domain protein kinase homology #label KIN1\ !$68-76 #region protein kinase ATP-binding motif\ !$414-673 #domain protein kinase homology #label KIN2\ !$422-430 #region protein kinase ATP-binding motif #status !8atypical SUMMARY #length 733 #molecular-weight 82638 #checksum 3859 SEQUENCE /// ENTRY S45917 #type complete TITLE probable serine/threonine-specific protein kinase (EC 2.7.1.-) YBR059c - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein YBR0519 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S45917 REFERENCE S45906 !$#authors Aljinovic, G.; Pohl, F.M.; Pohl, T.M. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S45917 !'##molecule_type DNA !'##residues 1-1108 ##label ALJ !'##cross-references EMBL:Z35928; NID:g536298; PIDN:CAA85002.1; !1PID:g536299; GSPDB:GN00002; MIPS:YBR059c !'##experimental_source strain S288C GENETICS !$#gene SGD:AKL1; MIPS:YBR059c !'##cross-references SGD:S0000263 !$#map_position 2R CLASSIFICATION #superfamily yeast probable serine/threonine-specific !1protein kinase YBR059c; protein kinase homology KEYWORDS ATP; phosphotransferase; serine/threonine-specific protein !1kinase FEATURE !$33-319 #domain protein kinase homology #label KIN SUMMARY #length 1108 #molecular-weight 123989 #checksum 4503 SEQUENCE /// ENTRY S27381 #type complete TITLE probable serine/threonine-specific protein kinase (EC 2.7.1.-) YKL116c - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES probable protein kinase YKL516 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S27381; S37944 REFERENCE S22267 !$#authors Jacquier, A.; Legrain, P.; Dujon, B. !$#journal Yeast (1992) 8:121-132 !$#title Sequence of a 10.7 kb segment of yeast chromosome XI !1identifies the APN1 and the BAF1 loci and reveals one tRNA !1gene and several new open reading frames including homologs !1to RAD2 and kinases. !$#cross-references MUID:92221689; PMID:1561835 !$#accession S27381 !'##molecule_type DNA !'##residues 1-518 ##label JAC !'##cross-references GB:S93804; NID:g248391; PIDN:AAB21999.1; !1PID:g248393 !'##experimental_source strain S288C REFERENCE S37938 !$#authors Jacquier, A.; Legrain, P.; Colleaux, L.; Richard, G.F.; !1Thierry, A.; Dujon, B. !$#submission submitted to the Protein Sequence Database, March 1994 !$#accession S37944 !'##molecule_type DNA !'##residues 1-518 ##label JA2 !'##cross-references EMBL:Z28115; NID:g486193; PIDN:CAA81955.1; !1PID:g486194; GSPDB:GN00011; MIPS:YKL116c !'##experimental_source strain S288C GENETICS !$#gene SGD:PRR1; MIPS:YKL116c !'##cross-references SGD:S0001599 !$#map_position 11L CLASSIFICATION #superfamily yeast probable serine/threonine-specific !1protein kinase YKL116c; protein kinase homology KEYWORDS ATP; phosphotransferase; serine/threonine-specific protein !1kinase FEATURE !$190-499 #domain protein kinase homology #label KIN\ !$354 #active_site Asp #status predicted SUMMARY #length 518 #molecular-weight 58955 #checksum 3669 SEQUENCE /// ENTRY S38001 #type complete TITLE probable serine/threonine-specific protein kinase (EC 2.7.1.-) YKL171w - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YKL635 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S38001; S44590; S38410 REFERENCE S37976 !$#authors Vandenbol, M.; Bolle, P.A.; Dion, C.; Portetelle, D.; !1Hilger, F. !$#submission submitted to the Protein Sequence Database, March 1994 !$#accession S38001 !'##molecule_type DNA !'##residues 1-928 ##label VAN !'##cross-references EMBL:Z28171; NID:g486299; PIDN:CAA82013.1; !1PID:g486300; GSPDB:GN00011; MIPS:YKL171w !'##experimental_source strain S288C REFERENCE S44583 !$#authors Vandenbol, M.; Bolle, P.A.; Dion, C.; Portetelle, D.; !1Hilger, F. !$#journal Yeast (1994) 10:25-33 !$#title Sequencing and analysis of a 20.5 kb DNA segment located on !1the left arm of yeast chromosome XI. !$#accession S44590 !'##status translation not shown !'##molecule_type DNA !'##residues 1-928 ##label VA2 !'##cross-references EMBL:Z26878; NID:g407503; PIDN:CAA81516.1; !1PID:g407511 !'##experimental_source strain S288C GENETICS !$#gene MIPS:YKL171w !'##cross-references SGD:S0001654 !$#map_position 11L CLASSIFICATION #superfamily yeast probable serine/threonine-specific !1protein kinase YKL171w; protein kinase homology KEYWORDS ATP; phosphotransferase; serine/threonine-specific protein !1kinase FEATURE !$447-729 #domain protein kinase homology #label KIN\ !$580 #active_site Asp #status predicted SUMMARY #length 928 #molecular-weight 103955 #checksum 3151 SEQUENCE /// ENTRY S67561 #type complete TITLE protein kinase RPK1 (EC 2.7.1.-) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein D2785; protein YDL028c; spindle pole body duplication protein MPS1 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S67561; S46425; S55256 REFERENCE S67560 !$#authors Paulin, L.; Saren, A.M.; Laamanen, P. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67561 !'##molecule_type DNA !'##residues 1-764 ##label PAU !'##cross-references EMBL:Z74076; NID:g1431003; PIDN:CAA98587.1; !1PID:g1431004; GSPDB:GN00004; MIPS:YDL028c !'##experimental_source strain S288C REFERENCE S46425 !$#authors Poch, O.; Schwob, E.; de Fraipont, F.; Camasses, A.; !1Bordonne, R.; Martin, R.P. !$#journal Mol. Gen. Genet. (1994) 243:641-653 !$#title RPK1, an essential yeast protein kinase involved in the !1regulation of the onset of mitosis, shows homology to !1mammalian dual-specificity kinases. !$#cross-references MUID:94301294; PMID:8028580 !$#accession S46425 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-145,'S',147-210,'TKR',214-764 ##label POC !'##cross-references GB:L08909; NID:g1197057; PIDN:AAA88731.1; !1PID:g1197058 REFERENCE S55256 !$#authors Lauze, E.; Stoelcker, B.; Luca, F.C.; Weiss, E.; Schutz, !1A.R.; Winey, M. !$#journal EMBO J. (1995) 14:1655-1663 !$#title Yeast spindle pole body duplication gene MPS1 encodes an !1essential dual specificity protein kinase. !$#cross-references MUID:95255223; PMID:7737118 !$#accession S55256 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type DNA !'##residues 446-491,'IERP',497-715 ##label LAU GENETICS !$#gene SGD:MPS1; RPK1; MIPS:YDL028c !'##cross-references SGD:S0002186; MIPS:YDL028c !$#map_position 4L CLASSIFICATION #superfamily yeast protein kinase RPK1; protein kinase !1homology KEYWORDS phosphotransferase FEATURE !$438-716 #domain protein kinase homology #label KIN SUMMARY #length 764 #molecular-weight 86827 #checksum 1736 SEQUENCE /// ENTRY S40400 #type complete TITLE protein kinase SWE1 (EC 2.7.1.-) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein J0406; protein YJL187c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S40400; S56970; S39999 REFERENCE S40400 !$#authors Booher, R.N.; Deshaies, R.J.; Kirschner, M.W. !$#journal EMBO J. (1993) 12:3417-3426 !$#title Properties of Saccharomyces cerevisiae wee 1 and its !1differential regulation of p34(CDC28) in response to G(1) !1and G(2) cyclins. !$#cross-references MUID:94074541; PMID:8253069 !$#accession S40400 !'##molecule_type DNA !'##residues 1-819 ##label BOO !'##cross-references EMBL:X73966; NID:g397528; PIDN:CAA52150.1; !1PID:g397529 REFERENCE S56937 !$#authors Obermaier, B.; Piravandi, E.; Rinke, M.; Domdey, H. !$#submission submitted to the Protein Sequence Database, September 1995 !$#accession S56970 !'##molecule_type DNA !'##residues 1-819 ##label OBE !'##cross-references EMBL:Z49462; NID:g1008394; PIDN:CAA89482.1; !1PID:g1008395; GSPDB:GN00010; MIPS:YJL187c GENETICS !$#gene SGD:SWE1; MIPS:YJL187c !'##cross-references SGD:S0003723; MIPS:YJL187c !$#map_position 10L CLASSIFICATION #superfamily yeast protein kinase SWE1; protein kinase !1homology KEYWORDS ATP; phosphotransferase; serine/threonine-specific protein !1kinase FEATURE !$442-793 #domain protein kinase homology #label KIN\ !$450-458 #region ATP binding #status predicted\ !$579 #active_site Asp #status predicted SUMMARY #length 819 #molecular-weight 92467 #checksum 7215 SEQUENCE /// ENTRY A39360 #type complete TITLE protein kinase (EC 2.7.1.37) akt1 [validated] - human ALTERNATE_NAMES protein kinase B alpha; RAC-PK-alpha; serine/ threonine-specific protein kinase RAC alpha ORGANISM #formal_name Homo sapiens #common_name man DATE 20-Mar-1992 #sequence_revision 12-May-1994 #text_change 30-Sep-2001 ACCESSIONS A39360; S36389; S18000; S20836 REFERENCE A39360 !$#authors Jones, P.F.; Jakubowicz, T.; Pitossi, F.J.; Maurer, F.; !1Hemmings, B.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:4171-4175 !$#title Molecular cloning and identification of a serine/threonine !1protein kinase of the second-messenger subfamily. !$#cross-references MUID:91239529; PMID:1851997 !$#accession A39360 !'##molecule_type mRNA !'##residues 1-480 ##label JON !'##cross-references GB:M63167; NID:g190827; PIDN:AAA36539.1; !1PID:g190828 REFERENCE S24423 !$#authors Coffer, P.J.; Woodgett, J.R. !$#journal Eur. J. Biochem. (1992) 205:1217 !$#cross-references MUID:92249329; PMID:1533586 !$#contents erratum !$#accession S36389 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type mRNA !'##residues 63-172,'A',175-201,'Q',203-211,'R',213-245,'A',247-408,'T', !1410-475,'P',477,'A',479-480 ##label COF1 !'##cross-references EMBL:X61037; NID:g35480; PIDN:CAA43372.1; !1PID:g35481 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1991 !'##note this a revision to the sequence from reference S17999 REFERENCE S17999 !$#authors Coffer, P.J.; Woodgett, J.R. !$#journal Eur. J. Biochem. (1991) 201:475-481 !$#title Molecular cloning and characterisation of a novel putative !1protein-serine kinase related to the cAMP-dependent and !1protein kinase C families. !$#cross-references MUID:92037600; PMID:1718748 !$#accession S18000 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 63-70,'TPSSSAACSGPLSSNAPSMWRLLRSGGVDNRHPDCGRRPQ', !1'EAGGGGDGLPVGLTQRQLRGRRDGGVPGQAQAP',145-172,'AA',175-201, !1'Q',203-211,'R',213-245,'A',247-408,'T',410-475,'P',477,'A', !1479-480 ##label COF2 !'##cross-references EMBL:X61037 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1991 !'##note this sequence has been revised in reference S24423 REFERENCE S20836 !$#authors Coffer, P. !$#submission submitted to the EMBL Data Library, July 1991 !$#accession S20836 !'##molecule_type mRNA !'##residues 63-70,'TPSSSAACSGPLSSNAPSMWRLLRSGGVDNRHPDCGRRPQ', !1'EAGGGGDGLPVGLTQRQLRGRRDGGVPGQAQAP',145-172,'A',175-201,'Q', !1203-211,'R',213-245,'A',247-408,'T',410-475,'P',477,'A', !1479-480 ##label COF3 !'##cross-references EMBL:X61037 !'##note this sequence has been revised in reference S24423 REFERENCE A64192 !$#authors Alessi, D.R.; Andjelkovic, M.; Caudwell, B.; Cron, P.; !1Morrice, N.; Cohen, P.; Hemmings, B.A. !$#journal EMBO J. (1996) 15:6541-6551 !$#title Mechanism of activation of protein kinase B by insulin and !1IGF-1. !$#cross-references MUID:97133284; PMID:8978681 !$#contents annotation; phosphorylation sites REFERENCE A64193 !$#authors Toker, A.; Newton, A.C. !$#journal J. Biol. Chem. (2000) 275:8271-8274 !$#title Akt/protein kinase B is regulated by autophosphorylation at !1the hypothetical PDK-2 site. !$#cross-references MUID:20187529; PMID:10722653 !$#contents annotation; autophosphorylation site COMMENT Akt1 is ubiquitous as an inactive multimeric complex. It !1binds phosphatidyl-3,4,5-trisphosphate (PIP3) and is then !1partially activated after phosphorylation by the !1phosphoinositide-dependent protein kinase 1 complex. Akt1 !1can then autophosphorylate and become fully active. GENETICS !$#gene GDB:AKT1; RAC; PKB !'##cross-references GDB:118989; OMIM:164730 !$#map_position 14q32.32-14q32.32 FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP [validated, !1PMID:9859994; PMID:9812896; PMID:10722653; PMID:10469573] !$#pathway signal transduction pathways regulating various processes !1including insulin and insulin-like growth factor 1 mediated !1cellular survival, apoptosis inhibition, and regulation of !1nitric oxide production CLASSIFICATION #superfamily protein kinase akt; pleckstrin repeat homology; !1protein kinase homology KEYWORDS ATP; autophosphorylation; phosphoprotein; !1phosphotransferase; proto-oncogene; serine/ !1threonine-specific protein kinase; signal transduction FEATURE !$4-106 #domain pleckstrin repeat homology #label PLK\ !$148-408 #domain protein kinase homology #label KIN\ !$156-164 #region protein kinase ATP-binding motif\ !$179 #active_site Lys #status predicted\ !$308 #binding_site phosphate (Thr) (covalent) (by !8phosphoinositide-dependent protein kinase 1) #status !8experimental\ !$473 #binding_site phosphate (Ser) (covalent) (by !8autophosphorylation) #status experimental SUMMARY #length 480 #molecular-weight 55716 #checksum 9834 SEQUENCE /// ENTRY JC2437 #type complete TITLE protein kinase (EC 2.7.1.37) akt1 [validated] - rat ALTERNATE_NAMES protein kinase B alpha; RAC-PK-alpha; serine/ threonine-specific protein kinase RAC alpha ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-2001 #sequence_revision 31-Mar-2001 #text_change 20-Apr-2001 ACCESSIONS JC2437 REFERENCE JC2437 !$#authors Konishi, H.; Shinomura, T.; Kuroda, S.; Ono, Y.; Kikkawa, U. !$#journal Biochem. Biophys. Res. Commun. (1994) 205:817-825 !$#title Molecular cloning of rat RAC protein kinase alpha and beta !1and their association with protein kinase C zeta. !$#cross-references MUID:95091823; PMID:7999118 !$#accession JC2437 !'##molecule_type mRNA !'##residues 1-480 ##label KON !'##cross-references DDBJ:D30040; NID:g485402; PIDN:BAA06279.1; !1PID:g485403 !'##experimental_source testis FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP [validated, !1MUID:96063640] !$#pathway signal transduction pathways regulating various processes CLASSIFICATION #superfamily protein kinase akt; pleckstrin repeat homology; !1protein kinase homology KEYWORDS ATP; autophosphorylation; phosphoprotein; !1phosphotransferase; proto-oncogene; serine/ !1threonine-specific protein kinase; signal transduction FEATURE !$4-106 #domain pleckstrin repeat homology #label PLK\ !$148-408 #domain protein kinase homology #label KIN\ !$156-164 #region protein kinase ATP-binding motif\ !$179 #active_site Lys #status predicted\ !$308 #binding_site phosphate (Thr) (covalent) (by !8phosphoinositide-dependent protein kinase 1) #status !8predicted\ !$473 #binding_site phosphate (Ser) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 480 #molecular-weight 55735 #checksum 958 SEQUENCE /// ENTRY S33364 #type complete TITLE protein kinase (EC 2.7.1.37) akt1 [similarity] - mouse ALTERNATE_NAMES protein kinase B alpha; RAC-PK-alpha; serine/ threonine-specific protein kinase RAC alpha ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 20-Apr-2001 ACCESSIONS S33364 REFERENCE S33364 !$#authors Bellacosa, A.; Franke, T.F.; Gonzalez-Portal, M.E.; Datta, !1K.; Taguchi, T.; Gardner, J.; Cheng, J.Q.; Testa, J.R.; !1Tsichlis, P.N. !$#journal Oncogene (1993) 8:745-754 !$#title Structure, expression and chromosomal mapping of c-akt: !1relationship to v-akt and its implications. !$#cross-references MUID:93173519; PMID:8437858 !$#accession S33364 !'##status preliminary !'##molecule_type mRNA !'##residues 1-480 ##label BEL !'##cross-references EMBL:X65687; NID:g287806; PIDN:CAA46620.1; !1PID:g287807 GENETICS !$#gene MGI:Akt !'##cross-references MGI:87986 !$#map_position 12 FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP !$#pathway signal transduction pathways regulating various processes CLASSIFICATION #superfamily protein kinase akt; pleckstrin repeat homology; !1protein kinase homology KEYWORDS ATP; autophosphorylation; phosphoprotein; !1phosphotransferase; proto-oncogene; serine/ !1threonine-specific protein kinase; signal transduction FEATURE !$4-106 #domain pleckstrin repeat homology #label PLK\ !$148-408 #domain protein kinase homology #label KIN\ !$156-164 #region protein kinase ATP-binding motif\ !$179 #active_site Lys #status predicted\ !$308 #binding_site phosphate (Thr) (covalent) (by !8phosphoinositide-dependent protein kinase 1) #status !8predicted\ !$473 #binding_site phosphate (Ser) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 480 #molecular-weight 55707 #checksum 509 SEQUENCE /// ENTRY S62117 #type complete TITLE protein kinase (EC 2.7.1.37) akt1 [similarity] - bovine ALTERNATE_NAMES protein kinase B alpha; RAC-PK-alpha; serine/ threonine-specific protein kinase RAC alpha ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 14-Dec-2001 ACCESSIONS S62117; S24423; S17999; S15714; S36388 REFERENCE S62117 !$#authors Coffer, P.J.; Woodgett, J.R. !$#submission submitted to the EMBL Data Library, December 1991 !$#accession S62117 !'##molecule_type mRNA !'##residues 1-480 ##label COF !'##cross-references EMBL:X61036; NID:g630; PIDN:CAA43371.1; PID:g631 !'##note this is a revision to the sequence from reference S17999 REFERENCE S24423 !$#authors Coffer, P.J.; Woodgett, J.R. !$#journal Eur. J. Biochem. (1992) 205:1217 !$#cross-references MUID:92249329; PMID:1533586 !$#contents erratum !$#accession S24423 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 70-78,'N',80-145 ##label COW !'##cross-references EMBL:X61036 !'##note this is a revision to the sequence from reference S17999 REFERENCE S17999 !$#authors Coffer, P.J.; Woodgett, J.R. !$#journal Eur. J. Biochem. (1991) 201:475-481 !$#title Molecular cloning and characterisation of a novel putative !1protein-serine kinase related to the cAMP-dependent and !1protein kinase C families. !$#cross-references MUID:92037600; PMID:1718748 !$#accession S17999 !'##molecule_type mRNA !'##residues 1-70, !1'TPSSSAACSGPRSSSARSTWRRPRSGGVDHRHPDGGRRAQEAGGGDDGLPVGLTRRELG !1GRGDGGVAGQAQAP',145-480 ##label COF2 !'##cross-references EMBL:X61036 !'##note this sequence has been revised in references S62117 and S24423 FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP !$#pathway signal transduction pathways regulating various processes CLASSIFICATION #superfamily protein kinase akt; pleckstrin repeat homology; !1protein kinase homology KEYWORDS ATP; autophosphorylation; phosphoprotein; !1phosphotransferase; proto-oncogene; serine/ !1threonine-specific protein kinase; signal transduction FEATURE !$4-106 #domain pleckstrin repeat homology #label PLK\ !$148-408 #domain protein kinase homology #label KIN\ !$156-164 #region protein kinase ATP-binding motif\ !$179 #active_site Lys #status predicted\ !$308 #binding_site phosphate (Thr) (covalent) (by !8phosphoinositide-dependent protein kinase 1) #status !8predicted\ !$473 #binding_site phosphate (Ser) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 480 #molecular-weight 55617 #checksum 1131 SEQUENCE /// ENTRY A46288 #type complete TITLE protein kinase (EC 2.7.1.37) akt2 - human ALTERNATE_NAMES protein kinase B beta; RAC-PK-beta; serine/ threonine-specific protein kinase RAC beta ORGANISM #formal_name Homo sapiens #common_name man DATE 22-Sep-1993 #sequence_revision 12-May-1994 #text_change 31-Mar-2001 ACCESSIONS A46288 REFERENCE A46288 !$#authors Cheng, J.Q.; Godwin, A.K.; Bellacosa, A.; Taguchi, T.; !1Franke, T.F.; Hamilton, T.C.; Tsichlis, P.N.; Testa, J.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:9267-9271 !$#title AKT2, a putative oncogene encoding a member of a subfamily !1of protein-serine/threonine kinases, is amplified in human !1ovarian carcinomas. !$#cross-references MUID:93028445; PMID:1409633 !$#accession A46288 !'##molecule_type mRNA !'##residues 1-481 ##label CHE !'##cross-references GB:M95936; NID:g178325; PIDN:AAA58364.1; !1PID:g178326 !'##note sequence extracted from NCBI backbone (NCBIP:115859) COMMENT This protein is amplified in some pancreatic, ovarian, and !1other carcinomas. GENETICS !$#gene GDB:AKT2 !'##cross-references GDB:135660; OMIM:164731 !$#map_position 19q13.2-19q13.2 FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP !$#pathway signal transduction pathways regulating various processes CLASSIFICATION #superfamily protein kinase akt; pleckstrin repeat homology; !1protein kinase homology KEYWORDS ATP; phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$4-106 #domain pleckstrin repeat homology #label PLK\ !$150-409 #domain protein kinase homology #label KIN\ !$158-166 #region protein kinase ATP-binding motif\ !$181 #active_site Lys #status predicted SUMMARY #length 481 #molecular-weight 55768 #checksum 7390 SEQUENCE /// ENTRY JC2438 #type complete TITLE protein kinase (EC 2.7.1.37) akt2 [validated] - rat ALTERNATE_NAMES protein kinase B beta; RAC-PK-beta; serine/ threonine-specific protein kinase RAC beta ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-2001 #sequence_revision 31-Mar-2001 #text_change 31-Mar-2001 ACCESSIONS JC2438 REFERENCE JC2437 !$#authors Konishi, H.; Shinomura, T.; Kuroda, S.; Ono, Y.; Kikkawa, U. !$#journal Biochem. Biophys. Res. Commun. (1994) 205:817-825 !$#title Molecular cloning of rat RAC protein kinase alpha and beta !1and their association with protein kinase C zeta. !$#cross-references MUID:95091823; PMID:7999118 !$#accession JC2438 !'##molecule_type mRNA !'##residues 1-481 ##label KON !'##cross-references DDBJ:D30041; NID:g485404; PIDN:BAA06280.1; !1PID:g485405 !'##experimental_source testis FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP [validated, !1MUID:96063640] !$#pathway signal transduction pathways regulating various processes !1including myoblast differentiation CLASSIFICATION #superfamily protein kinase akt; pleckstrin repeat homology; !1protein kinase homology KEYWORDS ATP; phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$4-106 #domain pleckstrin repeat homology #label PLK\ !$150-409 #domain protein kinase homology #label KIN\ !$158-166 #region protein kinase ATP-binding motif\ !$181 #active_site Lys #status predicted SUMMARY #length 481 #molecular-weight 55543 #checksum 7529 SEQUENCE /// ENTRY A59380 #type complete TITLE protein kinase (EC 2.7.1.37) akt3 long splice form [similarity] - human ALTERNATE_NAMES protein kinase B gamma; RAC-PK-gamma; serine/ threonine-specific protein kinase RAC gamma ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-2001 #sequence_revision 31-Mar-2001 #text_change 20-Apr-2001 ACCESSIONS A59380; A59379 REFERENCE A59380 !$#authors Brodbeck, D.; Cron, P.; Hemmings, B.A. !$#journal J. Biol. Chem. (1999) 274:9133-9136 !$#title A human protein kinase Bgamma with regulatory !1phosphorylation sites in the activation loop and in the !1C-terminal hydrophobic domain. !$#cross-references MUID:99194749; PMID:10092583 !$#accession A59380 !'##status preliminary !'##molecule_type DNA !'##residues 1-479 ##label BRO !'##cross-references GB:AAD29089; NID:g4757579; PIDN:AAD29089.1 REFERENCE A59379 !$#authors Masure, S.; Haefner, B.; Wesselink, J.J.; Hoefnagel, E.; !1Mortier, E.; Verhasselt, P.; Tuytelaars, A.; Gordon, R.; !1Richardson, A. !$#journal Eur. J. Biochem. (1999) 265:353-360 !$#title Molecular cloning, expression and characterization of the !1human serine/threonine kinase Akt-3. !$#cross-references MUID:99421751; PMID:10491192 !$#accession A59379 !'##status preliminary !'##molecule_type DNA !'##residues 1-479 ##label MAS !'##cross-references GB:CAB53537; NID:g5804886; PIDN:CAB53537.1 GENETICS !$#gene GDB:AKT3; PKBG; PRKBG; RAC-gamma !'##cross-references GDB:9954867 !$#map_position 1q44-1q44 FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP !$#pathway signal transduction pathways regulating various processes CLASSIFICATION #superfamily protein kinase akt; pleckstrin repeat homology; !1protein kinase homology KEYWORDS ATP; autophosphorylation; phosphoprotein; !1phosphotransferase; proto-oncogene; serine/ !1threonine-specific protein kinase; signal transduction FEATURE !$7-108 #domain pleckstrin repeat homology #label PLK\ !$149-408 #domain protein kinase homology #label KIN\ !$157-165 #region protein kinase ATP-binding motif\ !$177 #active_site Lys #status predicted\ !$305 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$474 #binding_site phosphate (Ser) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 479 #molecular-weight 55774 #checksum 7556 SEQUENCE /// ENTRY T17287 #type complete TITLE protein kinase (EC 2.7.1.37) akt3 short splice form - human ALTERNATE_NAMES protein kinase B gamma; RAC-PK-gamma; serine/ threonine-specific protein kinase RAC gamma ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-2001 #sequence_revision 31-Mar-2001 #text_change 31-Mar-2001 ACCESSIONS T17287 REFERENCE Z18723 !$#authors Poustka, A.; Klein, M.; Mewes, H.W.; Gassenhuber, J.; !1Wiemann, S. !$#submission submitted to the Protein Sequence Database, September 1999 !$#accession T17287 !'##molecule_type mRNA !'##residues 1-462 ##label POU !'##cross-references EMBL:AL117525; GB:CAB55977; NID:g5912043; !1PIDN:CAB55977.1 !'##experimental_source adult testis; clone DKFZp434N0250 REFERENCE A64199 !$#authors Nakatani, K.; Thompson, D.A.; Barthel, A.; Sakaue, H.; Liu, !1W.; Weigel, R.J.; Roth, R.A. !$#journal J. Biol. Chem. (1999) 274:21528-21532 !$#title Up-regulation of Akt3 in estrogen receptor-deficient breast !1cancers and amdrpgem-independent prostate cancer lines. !$#cross-references PMID:10419456 !$#contents annotation COMMENT This protein is increased in estrogen receptor-negative !1breast cancers and androgen-independent prostate cancers. GENETICS !$#gene GDB:AKT3 !'##cross-references GDB:9954867 !$#map_position 1q44-1q44 FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP !$#pathway signal transduction pathways regulating various processes CLASSIFICATION #superfamily protein kinase akt; pleckstrin repeat homology; !1protein kinase homology KEYWORDS ATP; phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$4-105 #domain pleckstrin repeat homology #label PLK\ !$146-405 #domain protein kinase homology #label KIN\ !$154-162 #region protein kinase ATP-binding motif\ !$177 #active_site Lys #status predicted SUMMARY #length 462 #molecular-weight 53589 #checksum 8813 SEQUENCE /// ENTRY JC4345 #type complete TITLE protein kinase (EC 2.7.1.37) akt3 [validated] - rat ALTERNATE_NAMES protein kinase B gamma; RAC-PK-gamma; serine/ threonine-specific protein kinase RAC gamma ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-2001 #sequence_revision 31-Mar-2001 #text_change 31-Mar-2001 ACCESSIONS JC4345 REFERENCE JC4345 !$#authors Konishi, H.; Kuroda, S.; Tanaka, M.; Matsuzaki, H.; Ono, Y.; !1Kameyama, K.; Haga, T.; Kikkawa, U. !$#journal Biochem. Biophys. Res. Commun. (1995) 216:526-534 !$#title Molecular cloning and characterization of a new member of !1the RAC protein kinase family: Association of the pleckstrin !1homology domain of three types of RAC protein kinase with !1protein kinase C subspecies and beta gamma subunits of G !1proteins. !$#cross-references MUID:96063640; PMID:7488143 !$#accession JC4345 !'##molecule_type mRNA !'##residues 1-454 ##label KON !'##cross-references DDBJ:D49836; NID:g1136777; PIDN:BAA08637.1; !1PID:g1401040 !'##experimental_source brain FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP [validated, !1MUID:96063640] !$#pathway signal transduction pathways regulating various processes CLASSIFICATION #superfamily protein kinase akt; pleckstrin repeat homology; !1protein kinase homology KEYWORDS ATP; phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$4-105 #domain pleckstrin repeat homology #label PLK\ !$146-405 #domain protein kinase homology #label KIN\ !$154-162 #region protein kinase ATP-binding motif\ !$177 #active_site Lys #status predicted SUMMARY #length 454 #molecular-weight 52849 #checksum 9173 SEQUENCE /// ENTRY A55888 #type complete TITLE protein kinase (EC 2.7.1.37) akt [similarity] - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES protein kinase B; RAC-PK; serine/threonine-specific protein kinase RAC ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 20-Apr-2001 ACCESSIONS A55888 REFERENCE A55888 !$#authors Andjelkovic, M.; Jones, P.F.; Grossniklaus, U.; Cron, P.; !1Schier, A.F.; Dick, M.; Bilbe, G.; Hemmings, B.A. !$#journal J. Biol. Chem. (1995) 270:4066-4075 !$#title Developmental regulation of expression and activity of !1multiple forms of the Drosophila RAC protein kinase. !$#cross-references MUID:95181376; PMID:7876156 !$#accession A55888 !'##status preliminary !'##molecule_type DNA !'##residues 1-611 ##label AND !'##cross-references GB:X83510 GENETICS !$#gene FlyBase:RacPK !'##cross-references FlyBase:FBgn0013324 !$#start_codon ACG !$#introns 261/3; 327/3; 457/3; 535/3; 584/3 FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP !$#pathway signal transduction pathways regulating various processes CLASSIFICATION #superfamily protein kinase akt; pleckstrin repeat homology; !1protein kinase homology KEYWORDS ATP; autophosphorylation; phosphoprotein; !1phosphotransferase; serine/threonine-specific protein !1kinase; signal transduction FEATURE !$105-209 #domain pleckstrin repeat homology #label PLK\ !$264-523 #domain protein kinase homology #label KIN\ !$272-280 #region protein kinase ATP-binding motif\ !$295 #active_site Lys #status predicted\ !$423 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$586 #binding_site phosphate (Ser) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 611 #molecular-weight 68514 #checksum 8467 SEQUENCE /// ENTRY T43232 #type complete TITLE protein kinase (EC 2.7.1.37) akt-1 splice form a [similarity] - Caenorhabditis elegans ALTERNATE_NAMES PKB; protein kinase B ORGANISM #formal_name Caenorhabditis elegans DATE 31-Mar-2001 #sequence_revision 31-Mar-2001 #text_change 20-Apr-2001 ACCESSIONS T43232; T19224 REFERENCE Z22355 !$#authors Paradis, S.; Ruvkun, G. !$#journal Genes Dev. (1998) 12:2488-2498 !$#title Caenorhabditis elegans Akt/PKB transduces insulin !1receptor-like signals from AGE-1 PI3 kinase to the DAF-16 !1transcription factor. !$#cross-references MUID:98382502; PMID:9716402 !$#accession T43232 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-541 ##label PAR !'##cross-references EMBL:AF072379; NID:g3694828; PIDN:AAC62466.1; !1PID:g3694829 REFERENCE Z19092 !$#authors McMurray, A. !$#submission submitted to the EMBL Data Library, June 1996 !$#accession T19224 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-541 ##label WIL !'##cross-references EMBL:Z73969; PIDN:CAA98240.1; GSPDB:GN00023; !1CESP:C12D8.10a !'##experimental_source clone C12D8 GENETICS !$#gene akt-1; C12D8.10 !$#map_position 5 !$#introns 35/2; 71/3; 134/3; 188/3; 254/3; 318/3; 361/3; 482/3 FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP !$#pathway signal transduction pathways regulating metabolism, !1development, and longevity CLASSIFICATION #superfamily protein kinase akt; pleckstrin repeat homology; !1protein kinase homology KEYWORDS alternative splicing; ATP; autophosphorylation; !1phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase; signal transduction FEATURE !$14-116 #domain pleckstrin repeat homology #label PLK\ !$191-450 #domain protein kinase homology #label KIN\ !$199-207 #region protein kinase ATP-binding motif\ !$222 #active_site Lys #status predicted\ !$350 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$517 #binding_site phosphate (Ser) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 541 #molecular-weight 62199 #checksum 2380 SEQUENCE /// ENTRY T43233 #type complete TITLE protein kinase (EC 2.7.1.37) akt-1 splice form b [similarity] - Caenorhabditis elegans ALTERNATE_NAMES PKB; protein kinase B ORGANISM #formal_name Caenorhabditis elegans DATE 31-Mar-2001 #sequence_revision 31-Mar-2001 #text_change 20-Apr-2001 ACCESSIONS T43233; T19222 REFERENCE Z22355 !$#authors Paradis, S.; Ruvkun, G. !$#journal Genes Dev. (1998) 12:2488-2498 !$#title Caenorhabditis elegans Akt/PKB transduces insulin !1receptor-like signals from AGE-1 PI3 kinase to the DAF-16 !1transcription factor. !$#cross-references MUID:98382502; PMID:9716402 !$#accession T43233 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-546 ##label PAR !'##cross-references EMBL:AF072380; NID:g3694830; PIDN:AAC62467.1; !1PID:g3694831 REFERENCE Z19092 !$#authors McMurray, A. !$#submission submitted to the EMBL Data Library, June 1996 !$#accession T19222 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-546 ##label WIL !'##cross-references EMBL:Z73969; PIDN:CAA98238.1; GSPDB:GN00023; !1CESP:C12D8.10b !'##experimental_source clone C12D8 GENETICS !$#gene akt-1; C12D8.10 !$#map_position 5 !$#introns 35/2; 71/3; 134/3; 188/3; 254/3; 323/3; 366/3; 487/3 FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP !$#pathway signal transduction pathways regulating metabolism, !1development, and longevity CLASSIFICATION #superfamily protein kinase akt; pleckstrin repeat homology; !1protein kinase homology KEYWORDS alternative splicing; ATP; autophosphorylation; !1phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase; signal transduction FEATURE !$14-116 #domain pleckstrin repeat homology #label PLK\ !$191-455 #domain protein kinase homology #label KIN\ !$199-207 #region protein kinase ATP-binding motif\ !$222 #active_site Lys #status predicted\ !$355 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$522 #binding_site phosphate (Ser) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 546 #molecular-weight 62743 #checksum 5444 SEQUENCE /// ENTRY T21523 #type complete TITLE protein kinase (EC 2.7.1.37) akt-2 long splice form [similarity] - Caenorhabditis elegans ALTERNATE_NAMES PKB; protein kinase B ORGANISM #formal_name Caenorhabditis elegans DATE 31-Mar-2001 #sequence_revision 31-Mar-2001 #text_change 20-Apr-2001 ACCESSIONS T21523; T23878 REFERENCE Z19434 !$#authors McMurray, A. !$#submission submitted to the EMBL Data Library, September 1998 !$#accession T21523 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-528 ##label WIL !'##cross-references EMBL:AL031621; PIDN:CAA20936.1; GSPDB:GN00028; !1CESP:F28H6.1 !'##experimental_source clone F28H6 REFERENCE Z19812 !$#authors McMurray, A. !$#submission submitted to the EMBL Data Library, March 1997 !$#accession T23878 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-528 ##label WI2 !'##cross-references EMBL:Z92837; PIDN:CAB07403.1; GSPDB:GN00028; !1CESP:F28H6.1 !'##experimental_source clone R03E1 GENETICS !$#gene akt-2; CESP:F28H6.1 !$#map_position X !$#introns 32/2; 68/3; 135/3; 175/3; 241/3; 285/2; 305/3; 348/3; 469/3 FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP !$#pathway signal transduction pathways regulating metabolism, !1development, and longevity CLASSIFICATION #superfamily protein kinase akt; pleckstrin repeat homology; !1protein kinase homology KEYWORDS alternative splicing; ATP; autophosphorylation; !1phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase; signal transduction FEATURE !$11-113 #domain pleckstrin repeat homology #label PLK\ !$178-437 #domain protein kinase homology #label KIN\ !$186-194 #region protein kinase ATP-binding motif\ !$209 #active_site Lys #status predicted\ !$337 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$505 #binding_site phosphate (Ser) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 528 #molecular-weight 61058 #checksum 9548 SEQUENCE /// ENTRY T43234 #type complete TITLE protein kinase (EC 2.7.1.37) akt-2 short splice form [similarity] - Caenorhabditis elegans ALTERNATE_NAMES PKB; protein kinase B ORGANISM #formal_name Caenorhabditis elegans DATE 31-Mar-2001 #sequence_revision 31-Mar-2001 #text_change 31-Mar-2001 ACCESSIONS T43234 REFERENCE Z22355 !$#authors Paradis, S.; Ruvkun, G. !$#journal Genes Dev. (1998) 12:2488-2498 !$#title Caenorhabditis elegans Akt/PKB transduces insulin !1receptor-like signals from AGE-1 PI3 kinase to the DAF-16 !1transcription factor. !$#cross-references MUID:98382502; PMID:9716402 !$#accession T43234 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-483 ##label PAR !'##cross-references EMBL:AF072381; NID:g3694832; PIDN:AAC62468.1; !1PID:g3694833 GENETICS !$#gene akt-2 FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP !$#pathway signal transduction pathways regulating metabolism, !1development, and longevity CLASSIFICATION #superfamily protein kinase akt; pleckstrin repeat homology; !1protein kinase homology KEYWORDS alternative splicing; ATP; phosphoprotein; !1phosphotransferase; serine/threonine-specific protein !1kinase; signal transduction FEATURE !$11-113 #domain pleckstrin repeat homology #label PLK\ !$178-437 #domain protein kinase homology #label KIN\ !$186-194 #region protein kinase ATP-binding motif\ !$209 #active_site Lys #status predicted\ !$337 #binding_site phosphate (Thr) (covalent) #status !8predicted SUMMARY #length 483 #molecular-weight 55756 #checksum 2821 SEQUENCE /// ENTRY A40831 #type complete TITLE gag-akt polyprotein - AKT8 murine leukemia virus CONTAINS amino end of core protein p30; core protein p15; inner coat protein p12; kinase-related transforming protein akt (EC 2.7.1.-) ORGANISM #formal_name AKT8 murine leukemia virus DATE 12-Feb-1993 #sequence_revision 12-May-1994 #text_change 16-Jul-1999 ACCESSIONS A40831; B40831 REFERENCE A40831 !$#authors Bellacosa, A.; Testa, J.R.; Staal, S.P.; Tsichlis, P.N. !$#journal Science (1991) 254:274-277 !$#title A retroviral oncogene, akt, encoding a serine-threonine !1kinase containing an SH2-like region. !$#cross-references MUID:92022574; PMID:1833819 !$#accession A40831 !'##molecule_type DNA !'##residues 1-262 ##label BEL !'##cross-references GB:M80675 !$#accession B40831 !'##molecule_type DNA !'##residues 262-763 ##label BE2 !'##cross-references GB:M80675 GENETICS !$#gene gag-akt CLASSIFICATION #superfamily gag-akt polyprotein; pleckstrin repeat !1homology; protein kinase homology KEYWORDS ATP; core protein; glycoprotein; oncogene; phosphoprotein; !1phosphotransferase; polyprotein; serine/threonine-specific !1protein kinase FEATURE !$1-129 #product core protein p15 #status predicted #label !8CP1\ !$130-214 #product inner coat protein p12 #status predicted !8#label CP2\ !$284-763 #product kinase-related transforming protein akt !8#status predicted #label AKT\ !$287-389 #domain pleckstrin repeat homology #label PLK\ !$431-691 #domain protein kinase homology #label KIN\ !$439-447 #region protein kinase ATP-binding motif\ !$25,337 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$462 #active_site Lys #status predicted\ !$609 #binding_site phosphate (Tyr) (covalent) #status !8predicted SUMMARY #length 763 #molecular-weight 86360 #checksum 4879 SEQUENCE /// ENTRY TVHUMD #type complete TITLE macrophage colony-stimulating factor 1 receptor precursor - human CONTAINS protein-tyrosine kinase (EC 2.7.1.112) csf1r/fms ORGANISM #formal_name Homo sapiens #common_name man DATE 28-Dec-1987 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS S08123; A24533; I56672; I57648; I59083; I52772 REFERENCE S08123 !$#authors Hampe, A.; Shamoon, B.M.; Gobet, M.; Sherr, C.J.; Galibert, !1F. !$#journal Oncogene Res. (1989) 4:9-17 !$#title Nucleotide sequence and structural organization of the human !1FMS proto-oncogene. !$#cross-references MUID:89239490; PMID:2524025 !$#accession S08123 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-972 ##label HAM !'##cross-references GB:U63963; EMBL:X14720; NID:g1915975; !1PIDN:AAB51696.1; PID:g1915976 !'##note this sequence was submitted to the EMBL Data Library, March !11989 REFERENCE A24533 !$#authors Coussens, L.; Van Beveren, C.; Smith, D.; Chen, E.; !1Mitchell, R.L.; Isacke, C.M.; Verma, I.M.; Ullrich, A. !$#journal Nature (1986) 320:277-280 !$#title Structural alteration of viral homologue of receptor !1proto-oncogene fms at carboxyl terminus. !$#cross-references MUID:86175013; PMID:2421165 !$#accession A24533 !'##molecule_type mRNA !'##residues 1-53,'A',55-972 ##label COU !'##cross-references GB:J03149 !'##note the authors translated the codon GCA for residue 54 as Pro REFERENCE I56672 !$#authors Wheeler, E.F.; Roussel, M.F.; Hampe, A.; Walker, M.H.; !1Fried, V.A.; Look, A.T.; Rettenmier, C.W.; Sherr, C.J. !$#journal J. Virol. (1986) 59:224-233 !$#title The amino-terminal domain of the v-fms oncogene product !1includes a functional signal peptide that directs synthesis !1of a transforming glycoprotein in the absence of feline !1leukemia virus gag sequences. !$#cross-references MUID:86281820; PMID:3525854 !$#accession I56672 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-16 ##label RES !'##cross-references GB:M14002; NID:g182676; PIDN:AAA35849.1; !1PID:g553292 REFERENCE I57648 !$#authors Visvader, J.; Verma, I.M. !$#journal Mol. Cell. Biol. (1989) 9:1336-1341 !$#title Differential transcription of exon 1 of the human c-fms gene !1in placental trophoblasts and monocytes. !$#cross-references MUID:89261741; PMID:2524648 !$#accession I57648 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-16 ##label RE2 !'##cross-references GB:M25786; NID:g349454; PIDN:AAA58421.1; !1PID:g553224 REFERENCE I59083 !$#authors Browning, P.J.; Bunn, H.F.; Cline, A.; Shuman, M.; Nienhuis, !1A.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:7800-7804 !$#title Replacement' of COOH-terminal truncation of v-fms with c-fms !1sequences markedly reduces transformation potential. !$#cross-references MUID:87017034; PMID:3532121 !$#accession I59083 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 874-972 ##label RE3 !'##cross-references GB:M14193; NID:g182521; PIDN:AAA35834.1; !1PID:g182522 REFERENCE I52772 !$#authors Nienhuis, A.W.; Bunn, H.F.; Turner, P.H.; Gopal, T.V.; Nash, !1W.G.; O'Brien, S. !$#journal Cell (1985) 42:421-428 !$#title Expression of the human c-fms proto-oncogene in !1hematopoietic cells and its deletion in the 5q- syndrome. !$#cross-references MUID:85282599; PMID:4028159 !$#accession I52772 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 244-295 ##label RE4 !'##cross-references GB:M11067; NID:g182674; PIDN:AAA35848.1; !1PID:g442423 GENETICS !$#gene GDB:CSF1R; FMS !'##cross-references GDB:120600; OMIM:164770 !$#map_position 5q33.2-5q33.3 !$#introns 17/1; 103/1; 198/1; 243/3; 297/1; 361/2; 400/1; 440/2; 504/ !11; 542/3; 585/1; 620/1; 657/1; 711/2; 741/1; 773/3; 814/3; !1852/1; 885/2; 921/3 CLASSIFICATION #superfamily macrophage colony-stimulating factor 1 !1receptor; immunoglobulin homology; protein kinase homology KEYWORDS ATP; autophosphorylation; glycoprotein; kinase-related !1transforming protein; magnesium; phosphoprotein; !1phosphotransferase; proto-oncogene; receptor; transmembrane !1protein; tyrosine-specific protein kinase FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-972 #product macrophage colony-stimulating factor 1 !8receptor #status predicted #label MAT\ !$24-512 #domain extracellular #status predicted #label EXT\ !$35-86 #domain immunoglobulin homology #label IMM1\ !$120-179 #domain immunoglobulin homology #label IMM2\ !$217-280 #domain immunoglobulin homology #label IMM3\ !$316-383 #domain immunoglobulin homology #label IMM4\ !$412-487 #domain immunoglobulin homology #label IMM5\ !$513-537 #domain transmembrane #status predicted #label TMM\ !$538-972 #domain intracellular #status predicted #label INT\ !$580-917 #domain protein kinase homology #label KIN\ !$588-596 #region protein kinase ATP-binding motif\ !$42-84,127-177, !$224-278,419-485 #disulfide_bonds #status predicted\ !$45,73,153,240,275, !$302,335,353,412, !$428,480 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$616,633,778 #active_site Lys, Glu, Asp #status predicted\ !$783,796 #binding_site magnesium (Asn, Asp) #status predicted SUMMARY #length 972 #molecular-weight 107983 #checksum 2888 SEQUENCE /// ENTRY TVCTMD #type complete TITLE macrophage colony-stimulating factor 1 receptor precursor - cat CONTAINS protein-tyrosine kinase (EC 2.7.1.112) csf1r/fms ORGANISM #formal_name Felis silvestris catus #common_name domestic cat DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 13-Jun-1997 ACCESSIONS A31636 REFERENCE A31636 !$#authors Woolford, J.; McAuliffe, A.; Rohrschneider, L.R. !$#journal Cell (1988) 55:965-977 !$#title Activation of the feline c-fms proto-oncogene: multiple !1alterations are required to generate a fully transformed !1phenotype. !$#cross-references MUID:89077553; PMID:2849512 !$#accession A31636 !'##molecule_type mRNA !'##residues 1-980 ##label WOO !'##cross-references EMBL:X03663 GENETICS !$#gene fms CLASSIFICATION #superfamily macrophage colony-stimulating factor 1 !1receptor; immunoglobulin homology; protein kinase homology KEYWORDS ATP; autophosphorylation; glycoprotein; kinase-related !1transforming protein; magnesium; phosphoprotein; !1phosphotransferase; proto-oncogene; receptor; transmembrane !1protein; tyrosine-specific protein kinase FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-980 #product macrophage colony-stimulating factor 1 !8receptor #status predicted #label MAT\ !$24-509 #domain extracellular #status predicted #label EXT\ !$35-86 #domain immunoglobulin homology #label IMM1\ !$120-179 #domain immunoglobulin homology #label IMM2\ !$217-280 #domain immunoglobulin homology #label IMM3\ !$316-381 #domain immunoglobulin homology #label IMM4\ !$410-484 #domain immunoglobulin homology #label IMM5\ !$510-534 #domain transmembrane #status predicted #label TMM\ !$535-980 #domain intracellular #status predicted #label INT\ !$577-915 #domain protein kinase homology #label KIN\ !$585-593 #region protein kinase ATP-binding motif\ !$42-84,127-177, !$224-278,417-482 #disulfide_bonds #status predicted\ !$45,73,94,153,275, !$302,335,410,477,490 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$613,630,776 #active_site Lys, Glu, Asp #status predicted\ !$781,794 #binding_site magnesium (Asn, Asp) #status predicted SUMMARY #length 980 #molecular-weight 108506 #checksum 7338 SEQUENCE /// ENTRY TVMVMD #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) fms precursor - feline sarcoma virus (strain McDonough) ORGANISM #formal_name feline sarcoma virus #note host Felis sp. (cat) DATE 27-Nov-1985 #sequence_revision 31-Dec-1991 #text_change 13-Jun-1997 ACCESSIONS A00654 REFERENCE A00654 !$#authors Hampe, A.; Gobet, M.; Sherr, C.J.; Galibert, F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:85-89 !$#title Nucleotide sequence of the feline retroviral oncogene v-fms !1shows unexpected homology with oncogenes encoding !1tyrosine-specific protein kinases. !$#cross-references MUID:84119469; PMID:6582485 !$#accession A00654 !'##molecule_type DNA !'##residues 1-941 ##label HAM COMMENT This protein is synthesized as a gag-fms polyprotein. GENETICS !$#gene fms CLASSIFICATION #superfamily macrophage colony-stimulating factor 1 !1receptor; immunoglobulin homology; protein kinase homology KEYWORDS ATP; autophosphorylation; glycoprotein; kinase-related !1transforming protein; magnesium; oncogene; phosphoprotein; !1phosphotransferase; receptor; transmembrane protein; !1tyrosine-specific protein kinase FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-941 #product protein-tyrosine kinase fms #status !8predicted #label MAT\ !$24-509 #domain extracellular #status predicted #label EXT\ !$35-86 #domain immunoglobulin homology #label IMM1\ !$120-179 #domain immunoglobulin homology #label IMM2\ !$217-280 #domain immunoglobulin homology #label IMM3\ !$316-381 #domain immunoglobulin homology #label IMM4\ !$410-484 #domain immunoglobulin homology #label IMM5\ !$510-534 #domain transmembrane #status predicted #label TMM\ !$535-941 #domain intracellular #status predicted #label INT\ !$577-915 #domain protein kinase homology #label KIN\ !$585-593 #region protein kinase ATP-binding motif\ !$42-84,127-177, !$224-278,417-482 #disulfide_bonds #status predicted\ !$45,73,94,153,275, !$286,302,335,410, !$477,490 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$613,630,776 #active_site Lys, Glu, Asp #status predicted\ !$781,794 #binding_site magnesium (Asn, Asp) #status predicted SUMMARY #length 941 #molecular-weight 104711 #checksum 3513 SEQUENCE /// ENTRY TVMSMD #type complete TITLE macrophage colony-stimulating factor 1 receptor precursor - mouse CONTAINS protein-tyrosine kinase (EC 2.7.1.112) csf1r/fms ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 02-Jun-2000 ACCESSIONS S01880 REFERENCE S01880 !$#authors Rothwell, V.M.; Rohrschneider, L.R. !$#journal Oncogene Res. (1987) 1:311-324 !$#title Murine c-fms cDNA: cloning, sequence analysis and retroviral !1expression. !$#cross-references MUID:88217329; PMID:2966922 !$#accession S01880 !'##molecule_type mRNA !'##residues 1-976 ##label ROT !'##cross-references EMBL:X06368 GENETICS !$#gene fms CLASSIFICATION #superfamily macrophage colony-stimulating factor 1 !1receptor; immunoglobulin homology; protein kinase homology KEYWORDS ATP; autophosphorylation; glycoprotein; kinase-related !1transforming protein; magnesium; phosphoprotein; !1phosphotransferase; proto-oncogene; receptor; transmembrane !1protein; tyrosine-specific protein kinase FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-976 #product macrophage colony-stimulating factor 1 !8receptor #status predicted #label MAT\ !$20-515 #domain extracellular #status predicted #label EXT\ !$35-86 #domain immunoglobulin homology #label IMM1\ !$120-179 #domain immunoglobulin homology #label IMM2\ !$217-280 #domain immunoglobulin homology #label IMM3\ !$316-381 #domain immunoglobulin homology #label IMM4\ !$410-485 #domain immunoglobulin homology #label IMM5\ !$516-535 #domain transmembrane #status predicted #label TMM\ !$536-976 #domain intracellular #status predicted #label INT\ !$578-914 #domain protein kinase homology #label KIN\ !$586-594 #region protein kinase ATP-binding motif\ !$42-84,127-177, !$224-278,417-483 #disulfide_bonds #status predicted\ !$45,73,302,335,389, !$410,449,478,491 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$614,631,776 #active_site Lys, Glu, Asp #status predicted\ !$781,794 #binding_site magnesium (Asn, Asp) #status predicted SUMMARY #length 976 #molecular-weight 109000 #checksum 5114 SEQUENCE /// ENTRY TVHUKT #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112), receptor type kit precursor - human ALTERNATE_NAMES mast/stem cell growth factor receptor; tyrosine kinase receptor c-kit ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 21-Jul-2000 ACCESSIONS S01426; PC1015; A41815; B41815; C41815; I37948; I56954; !1I54336 REFERENCE S01426 !$#authors Yarden, Y.; Kuang, W.J.; Yang-Feng, T.; Coussens, L.; !1Munemitsu, S.; Dull, T.J.; Chen, E.; Schlessinger, J.; !1Francke, U.; Ullrich, A. !$#journal EMBO J. (1987) 6:3341-3351 !$#title Human proto-oncogene c-kit: a new cell surface receptor !1tyrosine kinase for an unidentified ligand. !$#cross-references MUID:88111521; PMID:2448137 !$#accession S01426 !'##molecule_type mRNA !'##residues 1-976 ##label YAR !'##cross-references GB:X06182; NID:g34084; PIDN:CAA29548.1; PID:g34085 REFERENCE PC1015 !$#authors Hu, W.X.; Cornu, F.; Andre, C.; Galibert, F. !$#journal Chinese Biochem. J. (1991) 7:618-629 !$#title Nucleotide sequece of two neighbouring fragments of human !1c-kit proto-oncogene and its characterization. !$#accession PC1015 !'##molecule_type DNA !'##residues 412-713 ##label HUW !'##note article in Chinese with English abstract REFERENCE A41815 !$#authors Spritz, R.A.; Giebel, L.B.; Holmes, S.A. !$#journal Am. J. Hum. Genet. (1992) 50:261-269 !$#title Dominant negative and loss of function mutations of the !1c-kit (mast/stem cell growth factor receptor) proto-oncogene !1in human piebaldism. !$#cross-references MUID:92133600; PMID:1370874 !$#accession A41815 !'##molecule_type DNA !'##residues 579-583,'L',585-589 ##label SPR !'##cross-references GB:S78839; NID:g244084; PIDN:AAB21234.1; !1PID:g244085 !'##note sequence extracted from NCBI backbone (NCBIN:78839, !1NCBIP:78842) !'##note disease-related mutant from patient with piebaldism !$#accession B41815 !'##molecule_type DNA !'##residues 637-641,'SPELPW' ##label SP2 !'##cross-references GB:S78843; NID:g244086; PIDN:AAB21235.1; !1PID:g244087 !'##note sequence extracted from NCBI backbone (NCBIN:78843, !1NCBIP:78844) !'##note disease-related mutant from patient with piebaldism !$#accession C41815 !'##molecule_type DNA !'##residues 556-560,'GGDKWK' ##label SP3 !'##cross-references GB:S78845; NID:g244088; PIDN:AAB21236.1; !1PID:g244089 !'##note sequence extracted from NCBI backbone (NCBIN:78845, !1NCBIP:78846) !'##note disease-related mutant from patient with piebaldism REFERENCE I37948 !$#authors Giebel, L.B.; Strunk, K.M.; Holmes, S.A.; Spritz, R.A. !$#journal Oncogene (1992) 7:2207-2217 !$#title Organization and nucleotide sequence of the human KIT (mast/ !1stem cell growth factor receptor) proto-oncogene. !$#cross-references MUID:93064697; PMID:1279499 !$#accession I37948 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-976 ##label RES !'##cross-references EMBL:X69301; NID:g34089; PIDN:CAA49159.1; !1PID:g825686 !'##note an alternative splice form omitting residues 510-513 is !1described REFERENCE I56954 !$#authors Yamamoto, K.; Tojo, A.; Aoki, N.; Shibuya, M. !$#journal Jpn. J. Cancer Res. (1993) 84:1136-1144 !$#title Characterization of the promoter region of the human c-kit !1proto-oncogene. !$#cross-references MUID:94103107; PMID:7506248 !$#accession I56954 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-22 ##label RE2 !'##cross-references GB:S67773; NID:g459358; PIDN:AAB29529.1; !1PID:g459359 REFERENCE I54336 !$#authors Spritz, R.A.; Holmes, S.A.; Berg, S.Z.; Nordlund, J.J.; !1Fukai, K. !$#journal Hum. Mol. Genet. (1993) 2:1499-1500 !$#title A recurrent deletion in the KIT (mast/stem cell growth !1factor receptor) proto-oncogene is a frequent cause of human !1piebaldism. !$#cross-references MUID:94061059; PMID:7694728 !$#accession I54336 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 242-250 ##label RE3 !'##cross-references GB:S67686; NID:g460545; PIDN:AAD13996.1; !1PID:g4261696 GENETICS !$#gene GDB:KIT !'##cross-references GDB:120117; OMIM:164920 !$#map_position 4q12-4q12 !$#introns 23/1; 113/1; 207/1; 252/3; 309/1; 372/2; 411/1; 449/2; 514/ !11; 549/3; 592/1; 627/1; 664/1; 714/2; 745/1; 787/3; 828/3; !1866/1; 899/2; 934/3 !$#note defects in this gene may result in piebaldism FUNCTION !$#description catalyzes the phosphorylation of a peptidyl tyrosine residue !1by ATP CLASSIFICATION #superfamily macrophage colony-stimulating factor 1 !1receptor; immunoglobulin homology; protein kinase homology KEYWORDS alternative splicing; ATP; autophosphorylation; !1glycoprotein; kinase-related transforming protein; !1magnesium; phosphoprotein; phosphotransferase; !1proto-oncogene; receptor; transmembrane protein; !1tyrosine-specific protein kinase FEATURE !$1-976 #product protein-tyrosine kinase kit precursor, long !8form #status predicted #label MATL\ !$1-509,514-976 #product protein-tyrosine kinase kit precursor, short !8form #status predicted #label MATS\ !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-976 #product protein-tyrosine kinase kit #status !8predicted #label MAT\ !$23-520 #domain extracellular #status predicted #label EXT\ !$51-99 #domain immunoglobulin homology #label IMM1\ !$129-188 #domain immunoglobulin homology #label IMM2\ !$226-292 #domain immunoglobulin homology #label IMM3\ !$328-394 #domain immunoglobulin homology #label IMM4\ !$423-493 #domain immunoglobulin homology #label IMM5\ !$521-543 #domain transmembrane #status predicted #label TMM\ !$544-976 #domain intracellular #status predicted #label INT\ !$587-931 #domain protein kinase homology #label KIN\ !$595-603 #region protein kinase ATP-binding motif\ !$58-97,136-186, !$233-290,428-491 #disulfide_bonds #status predicted\ !$130,145,283,293, !$300,320,352,367, !$463,486 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$623,640,792 #active_site Lys, Glu, Asp #status predicted\ !$797,810 #binding_site magnesium (Asn, Asp) #status predicted SUMMARY #length 976 #molecular-weight 109864 #checksum 926 SEQUENCE /// ENTRY TVMSKT #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112), receptor type kit precursor - mouse ALTERNATE_NAMES tyrosine kinase receptor c-kit ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 31-Mar-2000 ACCESSIONS S00474; B44876; I49596 REFERENCE S00474 !$#authors Qiu, F.; Ray, P.; Brown, K.; Barker, P.E.; Jhanwar, S.; !1Ruddle, F.H.; Besmer, P. !$#journal EMBO J. (1988) 7:1003-1011 !$#title Primary structure of c-kit: relationship with the CSF-1/PDGF !1receptor kinase family--oncogenic activation of v-kit !1involves deletion of extracellular domain and C terminus. !$#cross-references MUID:88296403; PMID:2456920 !$#accession S00474 !'##molecule_type mRNA !'##residues 1-975 ##label QIU !'##cross-references GB:Y00864; NID:g50423; PIDN:CAA68772.1; PID:g50424 REFERENCE A44876 !$#authors Rossi, P.; Marziali, G.; Albanesi, C.; Charlesworth, A.; !1Geremia, R.; Sorrentino, V. !$#journal Dev. Biol. (1992) 152:203-207 !$#title A novel c-kit transcript, potentially encoding a truncated !1receptor, originates within a kit gene intron in mouse !1spermatids. !$#cross-references MUID:92331813; PMID:1378413 !$#accession B44876 !'##molecule_type DNA !'##residues 771-814 ##label ROS !'##note sequence extracted from NCBI backbone (NCBIN:108837, !1NCBIP:108840) REFERENCE I49596 !$#authors Yasuda, H.; Galli, S.J.; Geissler, E.N. !$#journal Biochem. Biophys. Res. Commun. (1993) 191:893-901 !$#title Cloning and functional analysis of the mouse c-kit promoter. !$#cross-references MUID:93221533; PMID:7682073 !$#accession I49596 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-22 ##label RES !'##cross-references GB:L11358; NID:g293325; PIDN:AAA37420.1; !1PID:g293326 GENETICS !$#gene kit; c-kit !$#map_position 5 CLASSIFICATION #superfamily macrophage colony-stimulating factor 1 !1receptor; immunoglobulin homology; protein kinase homology KEYWORDS ATP; autophosphorylation; glycoprotein; kinase-related !1transforming protein; magnesium; phosphoprotein; !1phosphotransferase; proto-oncogene; receptor; transmembrane !1protein; tyrosine-specific protein kinase FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-975 #product protein-tyrosine kinase kit #status !8predicted #label KTC\ !$23-519 #domain extracellular #status predicted #label EXT\ !$51-100 #domain immunoglobulin homology #label IMM1\ !$130-189 #domain immunoglobulin homology #label IMM2\ !$227-295 #domain immunoglobulin homology #label IMM3\ !$331-397 #domain immunoglobulin homology #label IMM4\ !$426-496 #domain immunoglobulin homology #label IMM5\ !$520-542 #domain transmembrane #status predicted #label TMM\ !$543-975 #domain intracellular #status predicted #label INT\ !$586-929 #domain protein kinase homology #label KIN\ !$594-602 #region protein kinase ATP-binding motif\ !$58-98,137-187, !$234-293,431-494 #disulfide_bonds #status predicted\ !$146,296,303,323, !$355,370,466,489 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$622,639,790 #active_site Lys, Glu, Asp #status predicted\ !$795,808 #binding_site magnesium (Asn, Asp) #status predicted SUMMARY #length 975 #molecular-weight 109001 #checksum 5337 SEQUENCE /// ENTRY A49814 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112), receptor type kit precursor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A49814; S49088 REFERENCE A49814 !$#authors Tsujimura, T.; Hirota, S.; Nomura, S.; Niwa, Y.; Yamazaki, !1M.; Tono, T.; Morii, E.; Kim, H.M.; Kondo, K.; Nishimune, !1Y.; Kitamura, Y. !$#journal Blood (1991) 78:1942-1946 !$#title Characterization of Ws mutant allele of rats: a 12-base !1deletion in tyrosine kinase domain of c-kit gene. !$#cross-references MUID:92003944; PMID:1912577 !$#accession A49814 !'##status preliminary !'##molecule_type mRNA !'##residues 1-978 ##label TSU !'##cross-references GB:D12524; NID:g220707; PIDN:BAA02094.1; !1PID:g220708 REFERENCE S49088 !$#authors Tsujimura, T.; Tono, T.; Yamazaki, M.; Nomura, S.; Kitamura, !1Y. !$#submission submitted to the EMBL Data Library, October 1991 !$#description Two isoforms of rat c-kit receptor tyrosine kinase. !$#accession S49088 !'##status preliminary !'##molecule_type mRNA !'##residues 1-511,516-978 ##label TS2 !'##cross-references EMBL:X62491; NID:g509135; PIDN:CAA44354.1; !1PID:g509136 CLASSIFICATION #superfamily macrophage colony-stimulating factor 1 !1receptor; immunoglobulin homology; protein kinase homology KEYWORDS ATP; autophosphorylation; phosphotransferase; !1tyrosine-specific protein kinase FEATURE !$129-188 #domain immunoglobulin homology #label IMM\ !$589-932 #domain protein kinase homology #label KIN\ !$597-605 #region protein kinase ATP-binding motif SUMMARY #length 978 #molecular-weight 109341 #checksum 4753 SEQUENCE /// ENTRY JN0677 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112), receptor type kit precursor - chicken ALTERNATE_NAMES tyrosine kinase receptor kit ORGANISM #formal_name Gallus gallus #common_name chicken DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS JN0677 REFERENCE JN0677 !$#authors Sasaki, E.; Okamura, H.; Chikamune, T.; Kanai, Y.; Watanabe, !1M.; Naito, M.; Sakurai, M. !$#journal Gene (1993) 128:257-261 !$#title Cloning and expression of the chicken c-kit proto-oncogene. !$#cross-references MUID:93292995; PMID:7685729 !$#accession JN0677 !'##molecule_type mRNA !'##residues 1-960 ##label SAS !'##cross-references DDBJ:D13225; NID:g303532; PIDN:BAA02506.1; !1PID:g303533 !'##experimental_source brain CLASSIFICATION #superfamily macrophage colony-stimulating factor 1 !1receptor; immunoglobulin homology; protein kinase homology KEYWORDS ATP; autophosphorylation; glycoprotein; kinase-related !1transforming protein; magnesium; membrane protein; !1phosphoprotein; phosphotransferase; proto-oncogene; !1receptor; tyrosine-specific protein kinase FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-960 #product tyrosine kinase receptor #status predicted !8#label MAT\ !$314-380 #domain immunoglobulin homology #label IMM\ !$573-916 #domain protein kinase homology #label KIN\ !$581-589 #region protein kinase ATP-binding motif\ !$76,135,149,269,286, !$306,318,338,356, !$453,469 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 960 #molecular-weight 107311 #checksum 3078 SEQUENCE /// ENTRY PFHUGA #type complete TITLE platelet-derived growth factor receptor alpha precursor - human CONTAINS protein-tyrosine kinase (EC 2.7.1.112) ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 11-Jun-1999 ACCESSIONS A40162; A32941 REFERENCE A40162 !$#authors Matsui, T.; Heidaran, M.; Miki, T.; Popescu, N.; La !1Rochelle, W.; Kraus, M.; Pierce, J.; Aaronson, S. !$#journal Science (1989) 243:800-804 !$#title Isolation of a novel receptor cDNA establishes the existence !1of two PDGF receptor genes. !$#cross-references MUID:89130149; PMID:2536956 !$#accession A40162 !'##molecule_type mRNA !'##residues 1-1089 ##label MATS !'##cross-references GB:M21574; NID:g189733; PIDN:AAA96715.1; !1PID:g189734 REFERENCE A32941 !$#authors Claesson-Welsh, L.; Eriksson, A.; Westermark, B.; Heldin, !1C.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:4917-4921 !$#title cDNA cloning and expression of the human A-type !1platelet-derived growth factor (PDGF) receptor establishes !1structural similarity to the B-type PDGF receptor. !$#cross-references MUID:89296915; PMID:2544881 !$#accession A32941 !'##molecule_type mRNA !'##residues 1-1089 ##label CLA !'##cross-references GB:M22734; NID:g189725; PIDN:AAA60048.1; !1PID:g189726 COMMENT The extracellular domain is predicted to include five !1immunoglobulin-like domains. GENETICS !$#gene GDB:PDGFRA !'##cross-references GDB:120267; OMIM:173490 !$#map_position 4q11-4q12 CLASSIFICATION #superfamily macrophage colony-stimulating factor 1 !1receptor; immunoglobulin homology; protein kinase homology KEYWORDS ATP; autophosphorylation; dimer; glycoprotein; growth factor !1receptor; phosphoprotein; phosphotransferase; transmembrane !1protein; tyrosine-specific protein kinase FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-1089 #product platelet-derived growth factor receptor !8alpha #status predicted #label MAT\ !$25-524 #domain extracellular #status predicted #label EXT\ !$42-102 #domain immunoglobulin homology #label IMM1\ !$143-191 #domain immunoglobulin homology #label IMM2\ !$228-292 #domain immunoglobulin homology #label IMM3\ !$428-503 #domain immunoglobulin homology #label IMM4\ !$525-548 #domain transmembrane #status predicted #label TMM\ !$549-1089 #domain intracellular #status predicted #label INT\ !$591-957 #domain protein kinase homology #label KIN\ !$599-607 #region protein kinase ATP-binding motif\ !$42,76,103,179,353, !$359,458,468 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$49-100,150-189, !$235-290,435-501 #disulfide_bonds #status predicted\ !$627 #active_site Lys #status predicted\ !$849 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 1089 #molecular-weight 122668 #checksum 4547 SEQUENCE /// ENTRY PFRTGA #type complete TITLE platelet-derived growth factor receptor alpha precursor - rat CONTAINS protein-tyrosine kinase (EC 2.7.1.112) ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 11-Jun-1999 ACCESSIONS A34710; S33767; S25100 REFERENCE A34710 !$#authors Lee, K.H.; Bowen-Pope, D.F.; Reed, R.R. !$#journal Mol. Cell. Biol. (1990) 10:2237-2246 !$#title Isolation and characterization of the alpha platelet-derived !1growth factor receptor from rat olfactory epithelium. !$#cross-references MUID:90220609; PMID:2157969 !$#accession A34710 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-1088 ##label LEE !'##cross-references GB:M63837; NID:g202929; PIDN:AAA40743.1; !1PID:g202930 !'##note in the authors' translation an additional residue, Val, is !1shown after position 850 REFERENCE S33764 !$#authors Herren, B.; Weyer, K.A.; Rouge, M.; Loetscher, P.; Pech, M. !$#journal Biochim. Biophys. Acta (1993) 1173:294-302 !$#title Conservation in sequence and affinity of human and rodent !1PDGF ligands and receptors. !$#cross-references MUID:93305723; PMID:8318539 !$#accession S33767 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 33-149,'R',151-518,'T',520-523 ##label HER1 !'##cross-references EMBL:Z14118; NID:g56863; PIDN:CAA78488.1; !1PID:g56864 !'##experimental_source strain Sprague Dawley REFERENCE S25096 !$#authors Herren, B.; Weyer, K.A.; Rouge, M.; Loetscher, P.; Pech, M. !$#submission submitted to the EMBL Data Library, July 1992 !$#description Cross-species conservation in sequence and function of PDGF !1ligands and receptors. !$#accession S25100 !'##molecule_type mRNA !'##residues 33-149,'R',151-518,'T',520-523 ##label HER2 !'##cross-references EMBL:Z14118; NID:g56863; PIDN:CAA78488.1; !1PID:g56864 CLASSIFICATION #superfamily macrophage colony-stimulating factor 1 !1receptor; immunoglobulin homology; protein kinase homology KEYWORDS ATP; autophosphorylation; glycoprotein; heterodimer; !1homodimer; phosphoprotein; phosphotransferase; receptor; !1transmembrane protein; tyrosine-specific protein kinase FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-1088 #product platelet-derived growth factor receptor !8alpha #status predicted #label MAT\ !$24-523 #domain extracellular #status predicted #label EXT\ !$41-101 #domain immunoglobulin homology #label IMM1\ !$142-190 #domain immunoglobulin homology #label IMM2\ !$227-291 #domain immunoglobulin homology #label IMM3\ !$427-502 #domain immunoglobulin homology #label IMM4\ !$524-547 #domain transmembrane #status predicted #label TMM\ !$548-1088 #domain intracellular #status predicted #label INT\ !$590-956 #domain protein kinase homology #label KIN\ !$598-606 #region protein kinase ATP-binding motif\ !$48-99,149-188, !$234-289,434-500 #disulfide_bonds #status predicted\ !$75,76,88,102,178, !$352,358,457,467 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$626 #active_site Lys #status predicted\ !$848 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 1088 #molecular-weight 122641 #checksum 764 SEQUENCE /// ENTRY S33727 #type complete TITLE platelet-derived growth factor receptor alpha precursor - mouse CONTAINS protein-tyrosine kinase (EC 2.7.1.112) ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 31-Mar-2000 ACCESSIONS I57511; S33727 REFERENCE I57511 !$#authors Stiles, C.D.; Wang, C. !$#journal Mol. Cell. Biol. (1990) 10:6781-6784 !$#title Retinoic acid promotes transcription of the platelet-derived !1growth factor alpha-receptor gene. !$#cross-references MUID:91061789; PMID:2174116 !$#accession I57511 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-1089 ##label RES !'##cross-references GB:M57683; NID:g199783; PIDN:AAA39733.1; !1PID:g199784 GENETICS !$#gene PDGF-alpha-R CLASSIFICATION #superfamily macrophage colony-stimulating factor 1 !1receptor; immunoglobulin homology; protein kinase homology KEYWORDS ATP; glycoprotein; growth factor receptor; !1phosphotransferase; transmembrane protein; tyrosine-specific !1protein kinase FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$228-292 #domain immunoglobulin homology #label IMM\ !$591-957 #domain protein kinase homology #label KIN\ !$599-607 #region protein kinase ATP-binding motif\ !$42,76,89,103,179, !$353,359,458,468,506 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1089 #molecular-weight 122660 #checksum 7667 SEQUENCE /// ENTRY PFHUGB #type complete TITLE platelet-derived growth factor receptor beta precursor - human CONTAINS protein-tyrosine kinase (EC 2.7.1.112) ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 11-Jun-1999 ACCESSIONS A28206; A31195; A38268; A31925; B31925; C31925 REFERENCE A28206 !$#authors Gronwald, R.G.K.; Grant, F.J.; Haldeman, B.A.; Hart, C.E.; !1O'Hara, P.J.; Hagen, F.S.; Ross, R.; Bowen-Pope, D.F.; !1Murray, M.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:3435-3439 !$#title Cloning and expression of a cDNA coding for the human !1platelet-derived growth factor receptor: evidence for more !1than one receptor class. !$#cross-references MUID:88217915; PMID:2835772 !$#accession A28206 !'##molecule_type mRNA !'##residues 1-1106 ##label GRO !'##cross-references GB:J03278; NID:g189731; PIDN:AAA60049.1; !1PID:g189732 REFERENCE A31195 !$#authors Claesson-Welsh, L.; Eriksson, A.; Moren, A.; Severinsson, !1L.; Ek, B.; Oestman, A.; Betsholtz, C.; Heldin, C.H. !$#journal Mol. Cell. Biol. (1988) 8:3476-3486 !$#title cDNA cloning and expression of a human platelet-derived !1growth factor (PDGF) receptor specific for !1beta-chain-containing PDGF molecules. !$#cross-references MUID:89096941; PMID:2850496 !$#accession A31195 !'##molecule_type mRNA !'##residues 1-240,'D',242-1106 ##label CLA !'##cross-references GB:M21616; NID:g189729; PIDN:AAA36427.1; !1PID:g189730 REFERENCE A38268 !$#authors Partanen, J.; Maekelae, T.P.; Alitalo, R.; Lehvaeslaiho, H.; !1Alitalo, K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:8913-8917 !$#title Putative tyrosine kinases expressed in K-562 human leukemia !1cells. !$#cross-references MUID:91062389; PMID:2247464 !$#accession A38268 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 828-884 ##label PAR REFERENCE A90908 !$#authors Roberts, W.M.; Look, A.T.; Roussel, M.F.; Sherr, C.J. !$#journal Cell (1988) 55:655-661 !$#title Tandem linkage of human CSF-1 receptor (c-fms) and PDGF !1receptor genes. !$#cross-references MUID:89028677; PMID:2846185 !$#accession A31925 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 676-727 ##label ROB !$#accession B31925 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 901-932 ##label RO2 !$#accession C31925 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1047-1106 ##label RO3 COMMENT The extracellular domain is predicted to include five !1immunoglobulin-like domains. GENETICS !$#gene GDB:PDGFRB !'##cross-references GDB:120710; OMIM:173410 !$#map_position 5q31-5q32 CLASSIFICATION #superfamily macrophage colony-stimulating factor 1 !1receptor; immunoglobulin homology; protein kinase homology KEYWORDS ATP; autophosphorylation; glycoprotein; growth factor !1receptor; heterodimer; homodimer; phosphoprotein; !1phosphotransferase; transmembrane protein; tyrosine-specific !1protein kinase FEATURE !$1-32 #domain signal sequence #status predicted #label SIG\ !$33-1106 #product platelet-derived growth factor receptor beta !8#status predicted #label MAT\ !$33-531 #domain extracellular #status predicted #label EXT\ !$47-102 #domain immunoglobulin homology #label IMM1\ !$142-192 #domain immunoglobulin homology #label IMM2\ !$228-293 #domain immunoglobulin homology #label IMM3\ !$429-510 #domain immunoglobulin homology #label IMM4\ !$532-555 #domain transmembrane #status predicted #label TMM\ !$556-1106 #domain intracellular #status predicted #label INT\ !$598-965 #domain protein kinase homology #label KIN\ !$606-614 #region protein kinase ATP-binding motif\ !$45,89,103,215,230, !$292,307,354,371, !$468,479 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$54-100,149-190, !$235-291,436-508 #disulfide_bonds #status predicted\ !$634 #active_site Lys #status predicted\ !$857 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 1106 #molecular-weight 123967 #checksum 5867 SEQUENCE /// ENTRY PFMSRB #type complete TITLE platelet-derived growth factor receptor beta precursor - mouse CONTAINS protein-tyrosine kinase (EC 2.7.1.112) ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 10-Sep-1999 ACCESSIONS A25742 REFERENCE A25742 !$#authors Yarden, Y.; Escobedo, J.A.; Kuang, W.J.; Yang-Feng, T.L.; !1Daniel, T.O.; Tremble, P.M.; Chen, E.Y.; Ando, M.E.; !1Harkins, R.N.; Francke, U.; Fried, V.A.; Ullrich, A.; !1Williams, L.T. !$#journal Nature (1986) 323:226-232 !$#title Structure of the receptor for platelet-derived growth factor !1helps define a family of closely related growth factor !1receptors. !$#cross-references MUID:87014762; PMID:3020426 !$#accession A25742 !'##molecule_type mRNA !'##residues 1-1098 ##label YAR !'##cross-references EMBL:X04367; NID:g53618; PIDN:CAA27882.1; !1PID:g53619 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing COMMENT The extracellular domain is predicted to include five !1immunoglobulin-like domains. COMMENT The purified receptor was found be ubiquitinated. CLASSIFICATION #superfamily macrophage colony-stimulating factor 1 !1receptor; immunoglobulin homology; protein kinase homology KEYWORDS ATP; autophosphorylation; glycoprotein; growth factor !1receptor; heterodimer; homodimer; phosphoprotein; !1phosphotransferase; transmembrane protein; tyrosine-specific !1protein kinase FEATURE !$1-31 #domain signal sequence #status predicted #label SIG\ !$32-1098 #product platelet-derived growth factor receptor beta !8#status predicted #label MAT\ !$32-530 #domain extracellular #status predicted #label EXT\ !$46-101 #domain immunoglobulin homology #label IMM1\ !$141-191 #domain immunoglobulin homology #label IMM2\ !$227-292 #domain immunoglobulin homology #label IMM3\ !$428-509 #domain immunoglobulin homology #label IMM4\ !$531-554 #domain transmembrane #status predicted #label TMM\ !$555-1098 #domain intracellular #status predicted #label INT\ !$597-964 #domain protein kinase homology #label KIN\ !$605-613 #region protein kinase ATP-binding motif\ !$44,88,102,214,291, !$306,353,370,444, !$467,478 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$53-99,148-189, !$234-290,435-507 #disulfide_bonds #status predicted\ !$633 #active_site Lys #status predicted\ !$856 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 1098 #molecular-weight 122805 #checksum 3508 SEQUENCE /// ENTRY FOMVHZ #type complete TITLE gag-kit polyprotein precursor - feline sarcoma virus (strain Hardy-Zuckerman 4) CONTAINS amino end of core protein p30; core protein p12; core protein p15; protein-tyrosine kinase (EC 2.7.1.112) kit ORGANISM #formal_name feline sarcoma virus #note host Felis sp. (cat) DATE 04-Dec-1986 #sequence_revision 12-May-1994 #text_change 11-Jun-1999 ACCESSIONS A03936; A00655 REFERENCE A00655 !$#authors Besmer, P.; Murphy, J.E.; George, P.C.; Qiu, F.; Bergold, !1P.J.; Lederman, L.; Snyder Jr., H.W.; Brodeur, D.; !1Zuckerman, E.E.; Hardy, W.D. !$#journal Nature (1986) 320:415-421 !$#title A new acute transforming feline retrovirus and relationship !1of its oncogene v-kit with the protein kinase gene family. !$#cross-references MUID:86175044; PMID:3007997 !$#accession A03936 !'##molecule_type DNA !'##residues 1-790 ##label BES !'##cross-references GB:X03711; NID:g61535; PIDN:CAA27339.1; PID:g61536 GENETICS !$#gene gag-kit CLASSIFICATION #superfamily feline sarcoma virus gag-kit polyprotein; !1protein kinase homology KEYWORDS ATP; core protein; oncogene; phosphotransferase; !1polyprotein; transforming protein; tyrosine-specific protein !1kinase FEATURE !$1-74 #domain leader peptide #status predicted #label LDP\ !$75-781 #product gag-kit polyprotein #status predicted #label !8MAT\ !$75-201 #product core protein p15 #status predicted #label !8C15\ !$202-271 #product core protein p12 #status predicted #label !8C12\ !$272-414 #product core protein p30 (fragment) #status !8predicted #label P30\ !$439-783 #domain protein kinase homology #label KIN\ !$447-455 #region protein kinase ATP-binding motif\ !$475 #active_site Lys #status predicted SUMMARY #length 790 #molecular-weight 88285 #checksum 5222 SEQUENCE /// ENTRY TVHUME #type complete TITLE hepatocyte growth factor receptor precursor - human CONTAINS protein-tyrosine kinase (EC 2.7.1.112) met ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1991 #sequence_revision 30-Sep-1992 #text_change 11-Jun-1999 ACCESSIONS A40175; A28303; A93749; A93369; A53761; I57632; A30008; !1B24569 REFERENCE A40175 !$#authors Giordano, S. !$#submission submitted to the EMBL Data Library, November 1990 !$#accession A40175 !'##molecule_type mRNA !'##residues 1-1390 ##label GIO !'##cross-references EMBL:X54559 REFERENCE A28303 !$#authors Park, M.; Dean, M.; Kaul, K.; Braun, M.J.; Gonda, M.A.; !1Vande Woude, G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:6379-6383 !$#title Sequence of MET protooncogene cDNA has features !1characteristic of the tyrosine kinase family of !1growth-factor receptors. !$#cross-references MUID:87317655; PMID:2819873 !$#accession A28303 !'##molecule_type mRNA !'##residues 1-755,'TWWKEPLNIVSFLFCFAS',756-1190,'A',1192-1390 ##label !1PAR !'##cross-references GB:J02958; NID:g187558; PIDN:AAA59591.1; !1PID:g307196 REFERENCE A93749 !$#authors Chan, A.M.L.; King, H.W.S.; Tempest, P.R.; Deakin, E.A.; !1Cooper, C.S.; Brookes, P. !$#journal Oncogene (1987) 1:229-233 !$#title Primary structure of the met protein tyrosine kinase domain. !$#cross-references MUID:88143699; PMID:3325883 !$#accession A93749 !'##molecule_type mRNA !'##residues 'VNETRECQSLRLELEKLNNQLKALTEKNKELEIAQDRNIAIQSQ', !1'FTRTKEELEAEKRDLIRTNERLSQELEYLT',1010-1271,'L',1273-1390 !1##label CHA !'##cross-references GB:U08818; NID:g487741; PIDN:AAB60323.1; !1PID:g487742 !'##note this activated met oncogene is the product of gene !1rearrangement REFERENCE A93369 !$#authors Dean, M.; Park, M.; Le Beau, M.M.; Robins, T.S.; Diaz, M.O.; !1Rowley, J.D.; Blair, D.G.; Vande Woude, G.F. !$#journal Nature (1985) 318:385-388 !$#title The human met oncogene is related to the tyrosine kinase !1oncogenes. !$#cross-references MUID:86065462; PMID:4069211 !$#accession A93369 !'##molecule_type DNA !'##residues 1267-1390 ##label DEA !'##cross-references GB:M35074; NID:g187555; PIDN:AAA59590.1; !1PID:g386868 REFERENCE A53761 !$#authors Gambarotta, G.; Pistoi, S.; Giordano, S.; Comoglio, P.M.; !1Santoro, C. !$#journal J. Biol. Chem. (1994) 269:12852-12857 !$#title Structure and inducible regulation of the human MET !1promoter. !$#cross-references MUID:94230365; PMID:8175700 !$#accession A53761 !'##molecule_type mRNA !'##residues 1-14 ##label GAM REFERENCE A40179 !$#authors Ferracini, R.; Longati, P.; Naldini, L.; Vigna, E.; !1Comoglio, P.M. !$#journal J. Biol. Chem. (1991) 266:19558-19564 !$#title Identification of the major autophosphorylation site of the !1Met/hepatocyte growth factor receptor tyrosine kinase. !$#cross-references MUID:92011756; PMID:1655790 !$#contents annotation; autophosphorylation site REFERENCE I57632 !$#authors Dean, M.; Park, M.; Vande Woude, G.F. !$#journal Mol. Cell. Biol. (1987) 7:921-924 !$#title Characterization of the rearranged tpr-met oncogene !1breakpoint. !$#cross-references MUID:87144265; PMID:3821733 !$#accession I57632 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 963-1009 ##label RES !'##cross-references GB:M15325; NID:g187531; PIDN:AAA59585.1; !1PID:g187532 COMMENT The receptor is a dimer of disulfide-bonded 50K alpha and !1145K beta chains that arise by cleavage of the precursor. !1Activity is regulated by phosphorylation of serine and !1tyrosine residues. GENETICS !$#gene GDB:MET !'##cross-references GDB:120178; OMIM:164860 !$#map_position 7q31-7q31 CLASSIFICATION #superfamily hepatocyte growth factor receptor; protein !1kinase homology KEYWORDS ATP; autophosphorylation; glycoprotein; phosphoprotein; !1phosphotransferase; proto-oncogene; receptor; transmembrane !1protein; tyrosine-specific protein kinase FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-303 #product hepatocyte growth factor receptor alpha !8chain #status predicted #label ALP\ !$308-1390 #product hepatocyte growth factor receptor beta chain !8#status predicted #label BET\ !$933-955 #domain transmembrane #status predicted #label TMN\ !$1076-1344 #domain protein kinase homology #label KIN\ !$1084-1092 #region protein kinase ATP-binding motif\ !$45,106,149,202,399, !$405,635,785,930 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$1110 #active_site Lys #status experimental\ !$1235 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status experimental SUMMARY #length 1390 #molecular-weight 155526 #checksum 2959 SEQUENCE /// ENTRY S01254 #type complete TITLE hepatocyte growth factor receptor precursor - mouse CONTAINS protein-tyrosine kinase (EC 2.7.1.112) met ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S01254; JH0115; A45453 REFERENCE S01254 !$#authors Chan, A.M.L.; King, H.W.S.; Deakin, E.A.; Tempest, P.R.; !1Hilkens, J.; Kroezen, V.; Edwards, D.R.; Wills, A.J.; !1Brookes, P.; Cooper, C.S. !$#journal Oncogene (1988) 2:593-599 !$#title Characterization of the mouse met proto-oncogene. !$#cross-references MUID:88262253; PMID:2838789 !$#accession S01254 !'##molecule_type mRNA !'##residues 1-1379 ##label CHA !'##cross-references EMBL:Y00671; NID:g53058; PIDN:CAA68680.1; !1PID:g53059 REFERENCE JH0112 !$#authors Wilks, A.F.; Kurban, R.R.; Hovens, C.M.; Ralph, S.J. !$#journal Gene (1989) 85:67-74 !$#title The application of the polymerase chain reaction to cloning !1members of the protein tyrosine kinase family. !$#cross-references MUID:90152381; PMID:2482828 !$#accession JH0115 !'##molecule_type mRNA !'##residues 'I',1200-1254,'R',1256-1260,'T',1262-1268 ##label WIL !'##experimental_source hemopoietic cell !'##note the authors translated the codon ACG for residue 1261 as Lys REFERENCE A45453 !$#authors Weidner, K.M.; Sachs, M.; Birchmeier, W. !$#journal J. Cell Biol. (1993) 121:145-154 !$#title The Met receptor tyrosine kinase transduces motility, !1proliferation, and morphogenic signals of scatter factor/ !1hepatocyte growth factor in epithelial cells. !$#cross-references MUID:93209981; PMID:8384622 !$#accession A45453 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 924-935 ##label WEI GENETICS !$#gene met CLASSIFICATION #superfamily hepatocyte growth factor receptor; protein !1kinase homology KEYWORDS ATP; autophosphorylation; glycoprotein; phosphoprotein; !1phosphotransferase; proto-oncogene; receptor; transmembrane !1protein; tyrosine-specific protein kinase FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-929 #domain extracellular #status predicted #label EXT\ !$25-302 #product hepatocyte growth factor receptor alpha !8chain #status predicted #label ACH\ !$308-1379 #product hepatocyte growth factor receptor beta chain !8#status predicted #label BCH\ !$930-954 #domain transmembrane #status predicted #label TMM\ !$955-1379 #domain intracellular #status predicted #label INT\ !$1074-1342 #domain protein kinase homology #label KIN\ !$1082-1090 #region protein kinase ATP-binding motif\ !$1108 #active_site Lys #status predicted\ !$1233 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 1379 #molecular-weight 153547 #checksum 6033 SEQUENCE /// ENTRY JC5148 #type complete TITLE hepatocyte growth factor receptor precursor - African clawed frog CONTAINS protein-tyrosine kinase (EC 2.7.1.112) c-Met ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS JC5148 REFERENCE JC5148 !$#authors Aoki, S.; Takahashi, K.; Matsumoto, K.; Nakamura, T. !$#journal J. Biochem. (1996) 120:961-968 !$#title Molecular cloning of the Xenopus c-met/hepatocyte growth !1factor receptor and its regional expression during early !1development. !$#cross-references MUID:97137526; PMID:8982863 !$#accession JC5148 !'##status preliminary !'##molecule_type mRNA !'##residues 1-1375 ##label AOK !'##cross-references GB:AB027411; NID:g4877403; PIDN:BAA77764.1; !1PID:g4877404 COMMENT This protein is involved in early multiple organogenesis in !1Xenopus embryos. GENETICS !$#gene c-met CLASSIFICATION #superfamily hepatocyte growth factor receptor; protein !1kinase homology KEYWORDS ATP; glycoprotein; growth factor receptor; phosphoprotein; !1phosphotransferase; tyrosine-specific protein kinase FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$1070-1338 #domain protein kinase homology #label KIN\ !$1078-1086 #region protein kinase ATP-binding motif SUMMARY #length 1375 #molecular-weight 153563 #checksum 1947 SEQUENCE /// ENTRY A48196 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112), receptor type sea - chicken CONTAINS protein-tyrosine kinase (EC 2.7.1.112) ORGANISM #formal_name Gallus gallus #common_name chicken DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A48196 REFERENCE A48196 !$#authors Huff, J.L.; Jelinek, M.A.; Borgman, C.A.; Lansing, T.J.; !1Parsons, J.T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:6140-6144 !$#title The protooncogene c-sea encodes a transmembrane !1protein-tyrosine kinase related to the Met/hepatocyte growth !1factor/scatter factor receptor. !$#cross-references MUID:93317639; PMID:8392188 !$#accession A48196 !'##status preliminary !'##molecule_type mRNA !'##residues 1-1404 ##label HUF !'##cross-references GB:L12024; NID:g348727; PIDN:AAA48729.1; !1PID:g348728 !'##note authors translated the codon AAC for residue 783 as Asp CLASSIFICATION #superfamily hepatocyte growth factor receptor; protein !1kinase homology KEYWORDS ATP; phosphotransferase; transmembrane protein; !1tyrosine-specific protein kinase FEATURE !$1087-1355 #domain protein kinase homology #label KIN\ !$1095-1103 #region protein kinase ATP-binding motif SUMMARY #length 1404 #molecular-weight 153849 #checksum 4163 SEQUENCE /// ENTRY I38185 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112), receptor type ron - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS I38185; S31736 REFERENCE I38185 !$#authors Ronsin, C.; Muscatelli, F.; Mattei, M.G.; Breathnach, R. !$#journal Oncogene (1993) 8:1195-1202 !$#title A novel putative receptor protein tyrosine kinase of the met !1family. !$#cross-references MUID:93241719; PMID:8386824 !$#accession I38185 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-1400 ##label RES !'##cross-references EMBL:X70040; NID:g36109; PIDN:CAA49634.1; !1PID:g36110 GENETICS !$#gene GDB:MST1R; RON !'##cross-references GDB:251941; OMIM:600168 !$#map_position 3p21.3-3p21.3 CLASSIFICATION #superfamily hepatocyte growth factor receptor; protein !1kinase homology KEYWORDS ATP; phosphotransferase; receptor; transmembrane protein; !1tyrosine-specific protein kinase FEATURE !$1080-1348 #domain protein kinase homology #label KIN\ !$1088-1096 #region protein kinase ATP-binding motif SUMMARY #length 1400 #molecular-weight 152226 #checksum 3589 SEQUENCE /// ENTRY I48751 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112), receptor type ron-like - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS I48751 REFERENCE I48751 !$#authors Iwama, A.; Okano, K.; Sudo, T.; Matsuda, Y.; Suda, T. !$#journal Blood (1994) 83:3160-3169 !$#title Molecular cloning of a novel receptor tyrosine kinase gene, !1STK, derived from enriched hematopoietic stem cells. !$#cross-references MUID:94250897; PMID:8193352 !$#accession I48751 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-1378 ##label RES !'##cross-references EMBL:X74736; NID:g515880; PIDN:CAA52754.1; !1PID:g602072 GENETICS !$#gene STK CLASSIFICATION #superfamily hepatocyte growth factor receptor; protein !1kinase homology KEYWORDS ATP; phosphotransferase; receptor; transmembrane protein; !1tyrosine-specific protein kinase FEATURE !$1057-1325 #domain protein kinase homology #label KIN\ !$1065-1073 #region protein kinase ATP-binding motif SUMMARY #length 1378 #molecular-weight 150537 #checksum 7663 SEQUENCE /// ENTRY JC4860 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) receptor sea-related precursor - African clawed frog ALTERNATE_NAMES Ron/HLP receptor, Xron ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS JC4860 REFERENCE JC4860 !$#authors Nakamura, T.; Aoki, S.; Takahashi, T.; Matsumoto, K.; !1Kiyohara, T.; Nakamura, T. !$#journal Biochem. Biophys. Res. Commun. (1996) 224:564-573 !$#title Cloning and expression of xenopus HGF-like protein (HLP) and !1Ron/HLP receptor implicate their involvement in early neural !1development. !$#cross-references MUID:96295526; PMID:8702427 !$#accession JC4860 !'##molecule_type mRNA !'##residues 1-1369 ##label NAK !'##cross-references GB:D87758; NID:g1545820; PIDN:BAA13459.1; !1PID:g1545821 COMMENT This receptor plays a role in development of embryonic !1neural tissue. GENETICS !$#gene Xron CLASSIFICATION #superfamily hepatocyte growth factor receptor; protein !1kinase homology KEYWORDS ATP; growth factor receptor; phosphotransferase; receptor; !1transmembrane protein; tyrosine-specific protein kinase FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-943 #domain extracellular #status predicted #label EXT\ !$944-961 #domain transmembrane #status predicted #label TMM\ !$962-1369 #domain intracellular #status predicted #label INT\ !$1024-1285 #domain tyrosine kinase #status predicted #label TRK\ !$1055-1323 #domain protein kinase homology #label KIN\ !$1063-1071 #region protein kinase ATP-binding motif SUMMARY #length 1369 #molecular-weight 151808 #checksum 8153 SEQUENCE /// ENTRY TVFVSA #type fragment TITLE env-sea polyprotein - avian erythroblastosis virus (strain S13) (fragment) CONTAINS protein-tyrosine kinase (EC 2.7.1.112) sea ORGANISM #formal_name avian erythroblastosis virus DATE 30-Jun-1991 #sequence_revision 05-May-1995 #text_change 18-Feb-2000 ACCESSIONS A33902; B33902 REFERENCE A33902 !$#authors Smith, D.R.; Vogt, P.K.; Hayman, M.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:5291-5295 !$#title The v-sea oncogene of avian erythroblastosis retrovirus S13: !1another member of the protein-tyrosine kinase gene family. !$#cross-references MUID:89315783; PMID:2546151 !$#accession A33902 !'##molecule_type DNA !'##residues 1-596 ##label SMI !'##cross-references EMBL:M25158 GENETICS !$#gene env-sea CLASSIFICATION #superfamily avian erythroblastosis virus env-sea !1polyprotein; protein kinase homology KEYWORDS ATP; autophosphorylation; oncogene; phosphoprotein; !1phosphotransferase; transforming protein; tyrosine-specific !1protein kinase FEATURE !$1-226 #region env polyprotein gene-derived\ !$227-596 #region protein-tyrosine kinase sea gene-derived\ !$284-552 #domain protein kinase homology #label KIN\ !$292-300 #region protein kinase ATP-binding motif\ !$318 #active_site Lys #status predicted SUMMARY #length 596 #checksum 892 SEQUENCE /// ENTRY GQHUE #type complete TITLE epidermal growth factor receptor precursor - human CONTAINS protein-tyrosine kinase (EC 2.7.1.112) erbB ORGANISM #formal_name Homo sapiens #common_name man DATE 15-Nov-1984 #sequence_revision 27-Nov-1985 #text_change 11-Jun-1999 ACCESSIONS A00641; A25772; S30024; A38672; A00642; A43615; A23062; !1A05281; A60143; A33331 REFERENCE A00641 !$#authors Ullrich, A.; Coussens, L.; Hayflick, J.S.; Dull, T.J.; Gray, !1A.; Tam, A.W.; Lee, J.; Yarden, Y.; Libermann, T.A.; !1Schlessinger, J.; Downward, J.; Mayes, E.L.V.; Whittle, N.; !1Waterfield, M.D.; Seeburg, P.H. !$#journal Nature (1984) 309:418-425 !$#title Human epidermal growth factor receptor cDNA sequence and !1aberrant expression of the amplified gene in A431 epidermoid !1carcinoma cells. !$#cross-references MUID:84219729; PMID:6328312 !$#accession A00641 !'##molecule_type mRNA !'##residues 1-1210 ##label ULL !'##cross-references EMBL:X00588; NID:g31113; PIDN:CAA25240.1; !1PID:g757924 !'##note the authors translated the codon AAG for residue 540 as Asn REFERENCE A25772 !$#authors Ishii, S.; Xu, Y.; Stratton, R.H.; Roe, B.A.; Merlino, G.T.; !1Pastan, I. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:4920-4924 !$#title Characterization and sequence of the promoter region of the !1human epidermal growth factor receptor gene. !$#cross-references MUID:85270438; PMID:2991899 !$#accession A25772 !'##status translation not shown !'##molecule_type DNA !'##residues 1-29 ##label ISH !'##cross-references GB:M11234; NID:g181981; PIDN:AAA52370.1; !1PID:g553272 REFERENCE S30024 !$#authors Haley, J.; Whittle, N.; Bennett, P.; Kinchington, D.; !1Ullrich, A.; Waterfield, M. !$#journal Oncogene Res. (1987) 1:375-396 !$#title The human EGF receptor gene: structure of the 110 kb locus !1and identification of sequences regulating its !1transcription. !$#cross-references MUID:88217333; PMID:3329716 !$#accession S30024 !'##molecule_type DNA !'##residues 1-29 ##label HA2 !'##cross-references EMBL:X06370; NID:g31118; PIDN:CAA29668.1; !1PID:g31119 REFERENCE A38672 !$#authors Haley, J.D.; Waterfield, M.D. !$#journal J. Biol. Chem. (1991) 266:1746-1753 !$#title Contributory effects of de Novo transcription and premature !1transcript termination in the regulation of human epidermal !1growth factor receptor proto-oncogene RNA synthesis. !$#cross-references MUID:91107677; PMID:1988448 !$#accession A38672 !'##molecule_type DNA !'##residues 1-29 ##label HAL !'##cross-references GB:M38425; NID:g181977; PIDN:AAA63171.1; !1PID:g553271 !'##experimental_source carcinoma cell line A431-7 REFERENCE A00642 !$#authors Xu, Y.; Ishii, S.; Clark, A.J.L.; Sullivan, M.; Wilson, !1R.K.; Ma, D.P.; Roe, B.A.; Merlino, G.T.; Pastan, I. !$#journal Nature (1984) 309:806-810 !$#title Human epidermal growth factor receptor cDNA is homologous to !1a variety of RNAs overproduced in A431 carcinoma cells. !$#cross-references MUID:84245835; PMID:6330563 !$#accession A00642 !'##molecule_type mRNA !'##residues 'RCAWRRA',150-187,'KSVIQAV',195,'M',197,'A',199-222,'S', !1224-304,'RA',307-321,'A',323-372,374-502,504,'GSAMP',510, !1'A',512,'R',514-517,'RA',521-539,'N',541-667,'IG',670-676, !1'A',678-794,'SAG',798-799,'TD',802-811,'R',813-942 ##label !1XUY !'##experimental_source A431 human carcinoma cells, which have large !1numbers of EGF receptors (a 30-fold amplification of DNA !1sequence and possible rearrangements) and elevated !1EGF-binding capacity REFERENCE A43615 !$#authors Lin, C.R.; Chen, W.S.; Kruiger, W.; Stolarsky, L.S.; Weber, !1W.; Evans, R.M.; Verma, I.M.; Gill, G.N.; Rosenfeld, M.G. !$#journal Science (1984) 224:843-848 !$#title Expression cloning of human EGF receptor complementary DNA: !1gene amplification and three related messenger RNA products !1in A431 cells. !$#cross-references MUID:84196372; PMID:6326261 !$#accession A43615 !'##molecule_type mRNA !'##residues 713-964 ##label LIN !'##experimental_source epidermoid carcinoma cell line A431 REFERENCE A23062 !$#authors Simmen, F.A.; Gope, M.L.; Schulz, T.Z.; Wright, D.A.; !1Carpenter, G.; O'Malley, B.W. !$#journal Biochem. Biophys. Res. Commun. (1984) 124:125-132 !$#cross-references MUID:85046483; PMID:6093780 !$#accession A23062 !'##molecule_type mRNA !'##residues 1028-1210 ##label SIM REFERENCE A05281 !$#authors Weber, W.; Gill, G.N.; Speiss, J. !$#journal Science (1984) 224:294-297 !$#cross-references MUID:84172183; PMID:6324343 !$#accession A05281 !'##molecule_type protein !'##residues 25-30,'S',32-51;454-467 ##label WEB REFERENCE A60143 !$#authors Russo, M.W.; Lukas, T.J.; Cohen, S.; Staros, J.V. !$#journal J. Biol. Chem. (1985) 260:5205-5208 !$#title Identification of residues in the nucleotide binding site of !1the epidermal growth factor receptor/kinase. !$#cross-references MUID:85182650; PMID:2985580 !$#accession A60143 !'##molecule_type protein !'##residues 740-744,'X',746-747 ##label RUS REFERENCE A38023 !$#authors Mroczkowski, B.; Mosig, G.; Cohen, S. !$#journal Nature (1984) 309:270-273 !$#title ATP-stimulated interaction between epidermal growth factor !1receptor and supercoiled DNA. !$#cross-references MUID:84191554; PMID:6325948 !$#contents annotation; receptor activity !$#note the EGF receptor (and other tyrosine kinases) can nick !1double-stranded DNA REFERENCE A33331 !$#authors Chen, W.S.; Lazar, C.S.; Lund, K.A.; Welsh, J.B.; Chang, !1C.P.; Walton, G.M.; Der, C.J.; Wiley, H.S.; Gill, G.N.; !1Rosenfeld, M.G. !$#journal Cell (1989) 59:33-43 !$#title Functional independence of the epidermal growth factor !1receptor from a domain required for ligand-induced !1internalization and calcium regulation. !$#cross-references MUID:90003233; PMID:2790960 !$#contents annotation; internalization signal COMMENT Binding of EGF to the receptor leads to internalization of !1the EGF-receptor complex, induction of the tyrosine kinase !1activity, stimulation of cell DNA synthesis, and cell !1proliferation. GENETICS !$#gene GDB:EGFR !'##cross-references GDB:120610; OMIM:131550 !$#map_position 7p12.3-7p12.1 CLASSIFICATION #superfamily epidermal growth factor receptor; protein !1kinase homology KEYWORDS ATP; autophosphorylation; duplication; glycoprotein; !1phosphoprotein; phosphotransferase; proto-oncogene; !1receptor; transmembrane protein; tyrosine-specific protein !1kinase FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-1210 #product EGF receptor #status predicted #label MAT\ !$25-645 #domain extracellular #status predicted #label EXT\ !$75-300 #domain EGF receptor extracellular domain repeat !8#label EE1\ !$390-600 #domain EGF receptor extracellular domain repeat !8#label EE2\ !$646-668 #domain transmembrane #status predicted #label TMM\ !$669-1210 #domain intracellular #status predicted #label INT\ !$710-975 #domain protein kinase homology #label KIN\ !$718-726 #region protein kinase ATP-binding motif\ !$999-1046 #region coated-pit mediated internalization signal\ !$1047-1210 #region inhibitory\ !$128,175,352,413, !$444,528,603 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$745 #active_site Lys #status experimental SUMMARY #length 1210 #molecular-weight 134290 #checksum 1521 SEQUENCE /// ENTRY TVCHLV #type complete TITLE epidermal growth factor receptor precursor - chicken CONTAINS protein-tyrosine kinase (EC 2.7.1.112) erbB ORGANISM #formal_name Gallus gallus #common_name chicken DATE 28-Feb-1986 #sequence_revision 05-May-1995 #text_change 04-Feb-2000 ACCESSIONS A27720; A00643 REFERENCE A27720 !$#authors Lax, I.; Johnson, A.; Howk, R.; Sap, J.; Bellot, F.; !1Winkler, M.; Ullrich, A.; Vennstrom, B.; Schlessinger, J.; !1Givol, D. !$#journal Mol. Cell. Biol. (1988) 8:1970-1978 !$#title Chicken epidermal growth factor (EGF) receptor: cDNA !1cloning, expression in mouse cells, and differential binding !1of EGF and transforming growth factor alpha. !$#cross-references MUID:88261272; PMID:3260329 !$#accession A27720 !'##molecule_type mRNA !'##residues 1-1223 ##label LAX !'##cross-references GB:M20386 REFERENCE A00643 !$#authors Nilsen, T.W.; Maroney, P.A.; Goodwin, R.G.; Rottman, F.M.; !1Crittenden, L.B.; Raines, M.A.; Kung, H.J. !$#journal Cell (1985) 41:719-726 !$#title c-erbB activation in ALV-induced erythroblastosis: novel RNA !1processing and promoter insertion result in expression of an !1amino-truncated EGF receptor. !$#cross-references MUID:85228222; PMID:2988784 !$#accession A00643 !'##molecule_type mRNA !'##residues 585-1223 ##label NIL !'##cross-references GB:M10066 GENETICS !$#gene erbB CLASSIFICATION #superfamily epidermal growth factor receptor; protein !1kinase homology KEYWORDS alternative splicing; ATP; autophosphorylation; !1glycoprotein; growth factor receptor; oncogene; !1phosphoprotein; phosphotransferase; transforming protein; !1transmembrane protein; tyrosine-specific protein kinase FEATURE !$1-30 #domain signal sequence #status predicted #label SIG\ !$31-1223 #product epidermal growth factor receptor #status !8predicted #label MAT\ !$31-654 #domain extracellular #status predicted #label EXT\ !$81-307 #domain EGF receptor extracellular domain repeat !8#label EE1\ !$397-610 #domain EGF receptor extracellular domain repeat !8#label EE2\ !$655-677 #domain transmembrane #status predicted #label TMM\ !$678-1223 #domain intracellular #status predicted #label INT\ !$719-984 #domain protein kinase homology #label KIN\ !$727-735 #region protein kinase ATP-binding motif\ !$136,202,280,361, !$370,422,575,580, !$615,635 #binding_site carbohydrate (Thr) (covalent) #status !8predicted\ !$192,650 #binding_site carbohydrate (Ser) (covalent) #status !8predicted\ !$687 #binding_site phosphate (Thr) (covalent) (by protein !8kinase C) #status predicted\ !$754 #active_site Lys #status predicted\ !$1100,1183,1208 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 1223 #molecular-weight 136089 #checksum 6358 SEQUENCE /// ENTRY S06142 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) mrk-Y precursor - southern platyfish ALTERNATE_NAMES epidermal growth factor receptor homolog; kinase-related transforming protein Tu; melanoma-inducing protein ORGANISM #formal_name Xiphophorus maculatus #common_name southern platyfish DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 18-Feb-2000 ACCESSIONS S06142; S13809 REFERENCE S06142 !$#authors Wittbrodt, J.; Adam, D.; Malitschek, B.; Maeueler, W.; !1Raulf, F.; Telling, A.; Robertson, S.M.; Schartl, M. !$#journal Nature (1989) 341:415-421 !$#title Novel putative receptor tyrosine kinase encoded by the !1melanoma-inducing Tu locus in Xiphophorus. !$#cross-references MUID:90015140; PMID:2797166 !$#accession S06142 !'##molecule_type DNA !'##residues 1-1166 ##label WIT !'##cross-references EMBL:X16891; NID:g65290; PIDN:CAA34770.1; !1PID:g65291 REFERENCE S13807 !$#authors Adam, D.; Maeueler, W.; Schartl, M. !$#journal Oncogene (1991) 6:73-80 !$#title Transcriptional activation of the melanoma inducing Xmrk !1oncogene in Xiphophorus. !$#cross-references MUID:91125882; PMID:1846957 !$#accession S13809 !'##status preliminary; translation not shown !'##molecule_type DNA !'##residues 821-1025,'N',1027-1098,'A',1100-1166 ##label ADA !'##cross-references EMBL:X56319; NID:g65284; PIDN:CAA39763.1; !1PID:g65285 GENETICS !$#gene mrk !$#map_position Y !$#introns 872/3; 898/1; 947/1; 979/3; 1025/3; 1056/1 CLASSIFICATION #superfamily epidermal growth factor receptor; protein !1kinase homology KEYWORDS ATP; growth factor receptor; phosphotransferase; !1transmembrane protein; tyrosine-specific protein kinase FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-1166 #product kinase-related transforming protein (Tu) !8#status predicted #label MAT\ !$707-972 #domain protein kinase homology #label KIN\ !$715-723 #region protein kinase ATP-binding motif SUMMARY #length 1166 #molecular-weight 129876 #checksum 9663 SEQUENCE /// ENTRY GQFFE #type complete TITLE epidermal growth factor receptor - fruit fly (Drosophila melanogaster) CONTAINS protein-tyrosine kinase (EC 2.7.1.112) erbB ORGANISM #formal_name Drosophila melanogaster DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 11-Jun-1999 ACCESSIONS A00640; A38021 REFERENCE A00640 !$#authors Livneh, E.; Glazer, L.; Segal, D.; Schlessinger, J.; Shilo, !1B.Z. !$#journal Cell (1985) 40:599-607 !$#title The Drosophila EGF receptor gene homolog: conservation of !1both hormone binding and kinase domains. !$#cross-references MUID:85124611; PMID:2982499 !$#accession A00640 !'##molecule_type DNA !'##residues 1-1330 ##label LIV !'##cross-references EMBL:K03054 REFERENCE A38021 !$#authors Wadsworth, S.C.; Vincent III, W.S.; Bilodeau-Wentworth, D. !$#journal Nature (1985) 314:178-180 !$#title A Drosophila genomic sequence with homology to human !1epidermal growth factor receptor. !$#cross-references MUID:85137938; PMID:2983232 !$#accession A38021 !'##molecule_type DNA !'##residues 'A',832-866,'V',868-943,'QTPSLVK' ##label WAD !'##cross-references EMBL:X02293; NID:g7922; PIDN:CAA26157.1; !1PID:g929565 COMMENT This sequence is tentative because the introns have not been !1identified. GENETICS !$#gene FlyBase:Egfr !'##cross-references FlyBase:FBgn0003731 !$#map_position 2 57F CLASSIFICATION #superfamily epidermal growth factor receptor; protein !1kinase homology KEYWORDS ATP; autophosphorylation; duplication; glycoprotein; !1phosphoprotein; phosphotransferase; receptor; transmembrane !1protein; tyrosine-specific protein kinase FEATURE !$1-732 #domain extracellular #status predicted #label EXT\ !$733-764 #domain transmembrane #status predicted #label TMM\ !$765-1330 #domain intracellular #status predicted #label INT\ !$808-1072 #domain protein kinase homology #label KIN\ !$816-824 #region protein kinase ATP-binding motif\ !$122,300,324,363, !$518,688,695,700 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$774 #binding_site phosphate (Thr) (covalent) (by protein !8kinase C) #status predicted\ !$843 #active_site Lys #status predicted\ !$1181 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 1330 #molecular-weight 148824 #checksum 7408 SEQUENCE /// ENTRY A24571 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) erbB2 precursor - human ALTERNATE_NAMES c-erb-B-2 protein precursor; kinase-related transforming protein erbB2; v-erbB-related protein HER-2/neu ORGANISM #formal_name Homo sapiens #common_name man DATE 25-Oct-1987 #sequence_revision 06-Dec-1996 #text_change 11-Jun-1999 ACCESSIONS A24571; A25491; A44188; B44188; I59509; I57622 REFERENCE A24571 !$#authors Yamamoto, T.; Ikawa, S.; Akiyama, T.; Semba, K.; Nomura, N.; !1Miyajima, N.; Saito, T.; Toyoshima, K. !$#journal Nature (1986) 319:230-234 !$#title Similarity of protein encoded by the human c-erb-B-2 gene to !1epidermal growth factor receptor. !$#cross-references MUID:86118663; PMID:3003577 !$#accession A24571 !'##molecule_type mRNA !'##residues 1-1255 ##label YAM !'##cross-references GB:X03363; NID:g31197; PIDN:CAA27060.1; PID:g31198 REFERENCE A25491 !$#authors Semba, K.; Kamata, N.; Toyoshima, K.; Yamamoto, T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:6497-6501 !$#title A v-erbB-related protooncogene, c-erbB-2, is distinct from !1the c-erbB-1/epidermal growth factor-receptor gene and is !1amplified in a human salivary adenocarcinoma. !$#cross-references MUID:86016729; PMID:2995967 !$#accession A25491 !'##molecule_type DNA !'##residues 737-1031 ##label SEM !'##cross-references GB:M11767; NID:g182163; PIDN:AAA35808.1; !1PID:g553282 REFERENCE A44188 !$#authors Coussens, L.; Yang-Feng, T.L.; Liao, Y.C.; Chen, E.; Gray, !1A.; McGrath, J.; Seeburg, P.H.; Libermann, T.A.; !1Schlessinger, J.; Francke, U.; Levinson, A.; Ullrich, A. !$#journal Science (1985) 230:1132-1139 !$#title Tyrosine kinase receptor with extensive homology to EGF !1receptor shares chromosomal location with neu oncogene. !$#cross-references MUID:86070181; PMID:2999974 !$#accession A44188 !'##molecule_type DNA !'##residues 740-910 ##label COU1 !'##cross-references GB:M12036; NID:g183988; PIDN:AAA35978.1; !1PID:g183989 !$#accession B44188 !'##molecule_type mRNA !'##residues 1-517,'RALL',522,'S',524-654,'V',656-1169,'A',1171-1255 !1##label COU2 !'##cross-references GB:M11730; NID:g183986 REFERENCE I59509 !$#authors King, C.R.; Kraus, M.H.; Aaronson, S.A. !$#journal Science (1985) 229:974-976 !$#title Amplification of a novel v-erbB-related gene in a human !1mammary carcinoma. !$#cross-references MUID:85272597; PMID:2992089 !$#accession I59509 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 832-909 ##label REX !'##cross-references GB:L29395; NID:g459807; PIDN:AAA35809.1; !1PID:g459808 REFERENCE I57622 !$#authors Tal, M.; King, C.R.; Kraus, M.H.; Ullrich, A.; Schlessinger, !1J.; Givol, D. !$#journal Mol. Cell. Biol. (1987) 7:2597-2601 !$#title Human HER2 (neu) promoter: evidence for multiple mechanisms !1for transcriptional initiation. !$#cross-references MUID:87286898; PMID:3039351 !$#accession I57622 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-191 ##label TAL !'##cross-references GB:M16792; NID:g183983; PIDN:AAA58637.1; !1PID:g553332 COMMENT Amplification and overexpression of this erbB-related gene !1occurs in about 30% of human breast and ovarian cancers. GENETICS !$#gene GDB:ERBB2; NGL; NEU; HER-2 !'##cross-references GDB:120613; OMIM:164870 !$#map_position 17q21.1-17q21.1 !$#introns 25/1; 75/3; 147/1; 883/3 !$#note the list of introns is incomplete FUNCTION !$#description catalyzes the phosphorylation of a peptidyl tyrosine residue !1by ATP CLASSIFICATION #superfamily epidermal growth factor receptor; protein !1kinase homology KEYWORDS ATP; autophosphorylation; duplication; glycoprotein; !1phosphoprotein; phosphotransferase; proto-oncogene; !1receptor; transforming protein; transmembrane protein; !1tyrosine-specific protein kinase FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-1255 #product protein-tyrosine kinase erbB2 #status !8predicted #label MAT\ !$22-653 #domain extracellular #status predicted #label EXT\ !$70-304 #domain EGF receptor extracellular domain repeat !8#label EE1\ !$395-605 #domain EGF receptor extracellular domain repeat !8#label EE2\ !$654-675 #domain transmembrane #status predicted #label TMM\ !$676-1255 #domain intracellular #status predicted #label INT\ !$718-983 #domain protein kinase homology #label KIN\ !$726-734 #region protein kinase ATP-binding motif\ !$68,124,187,259,530, !$571,629 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$686 #binding_site phosphate (Thr) (covalent) (by protein !8kinase C) #status predicted\ !$753 #active_site Lys #status predicted\ !$1139,1221,1222,1248 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 1255 #molecular-weight 137909 #checksum 9382 SEQUENCE /// ENTRY TVRTNU #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) neu precursor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 11-Jun-1999 ACCESSIONS A24562; A61204 REFERENCE A24562 !$#authors Bargmann, C.I.; Hung, M.C.; Weinberg, R.A. !$#journal Nature (1986) 319:226-230 !$#title The neu oncogene encodes an epidermal growth factor !1receptor-related protein. !$#cross-references MUID:86118662; PMID:3945311 !$#accession A24562 !'##molecule_type mRNA !'##residues 1-1260 ##label BAR !'##cross-references EMBL:X03362; NID:g56745; PIDN:CAA27059.1; !1PID:g56746 REFERENCE A61204 !$#authors Masui, T.; Mann, A.M.; Macatee, T.L.; Garland, E.M.; !1Okamura, T.; Smith, R.A.; Cohen, S.M. !$#journal Carcinogenesis (1991) 12:1975-1978 !$#title Direct DNA sequencing of the rat neu oncogene transmembrane !1domain reveals no mutation in urinary bladder carcinomas !1induced by N-butyl-N-(4-hydroxybutyl)nitrosamine, N-[4- !1(5-nitro-2-furyl)-2-thiazolyl]formamide or !1N-methyl-N-nitrosourea. !$#cross-references MUID:92035293; PMID:1682063 !$#accession A61204 !'##status preliminary !'##molecule_type DNA !'##residues 637-663,'V',665-702 ##label MAS !'##note authors translated the codon GCA for residue 25 as Val GENETICS !$#gene neu CLASSIFICATION #superfamily epidermal growth factor receptor; protein !1kinase homology KEYWORDS ATP; autophosphorylation; duplication; glycoprotein; !1phosphoprotein; phosphotransferase; proto-oncogene; !1transforming protein; transmembrane protein; !1tyrosine-specific protein kinase FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-1260 #product protein-tyrosine kinase neu #status !8predicted #label MAT\ !$658-680 #domain transmembrane #status predicted #label TMN\ !$723-988 #domain protein kinase homology #label KIN\ !$731-739 #region protein kinase ATP-binding motif\ !$71,191,263,535,576, !$634 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$691 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$758 #active_site Lys #status predicted\ !$882,1227,1253 #binding_site phosphate (Tyr) (covalent) #status !8predicted SUMMARY #length 1260 #molecular-weight 139219 #checksum 5917 SEQUENCE /// ENTRY TVFVLV #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) erbB - avian leukosis virus CONTAINS amino end of gag protein; env protein fragment; protein-tyrosine kinase ORGANISM #formal_name avian leukosis virus, ALV DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 11-Jun-1999 ACCESSIONS B00643; A00643 REFERENCE A00643 !$#authors Nilsen, T.W.; Maroney, P.A.; Goodwin, R.G.; Rottman, F.M.; !1Crittenden, L.B.; Raines, M.A.; Kung, H.J. !$#journal Cell (1985) 41:719-726 !$#title c-erbB activation in ALV-induced erythroblastosis: novel RNA !1processing and promoter insertion result in expression of an !1amino-truncated EGF receptor. !$#cross-references MUID:85228222; PMID:2988784 !$#accession B00643 !'##molecule_type mRNA !'##residues 1-698 ##label NIL !'##cross-references GB:M10066; GB:M13881; NID:g211749; PIDN:AAA48763.1; !1PID:g211750 !'##note in Genbank entry CHKERBBF, release 109.0, the source is !1designated as Gallus gallus COMMENT This protein is synthesized as a gag-env-erbB protein. GENETICS !$#gene gag-env-erbB CLASSIFICATION #superfamily epidermal growth factor receptor; protein !1kinase homology KEYWORDS ATP; oncogene; phosphotransferase; transforming protein; !1tyrosine-specific protein kinase FEATURE !$1-6 #product gag protein (fragment) #status predicted !8#label GAG\ !$7-59 #product env protein (fragment) #status predicted !8#label ENV\ !$60-698 #product protein-tyrosine kinase erbB #status !8predicted #label ERB\ !$194-459 #domain protein kinase homology #label KIN\ !$202-210 #region protein kinase ATP-binding motif\ !$229 #active_site Lys #status predicted SUMMARY #length 698 #molecular-weight 77798 #checksum 8260 SEQUENCE /// ENTRY TVYUH #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) erbB - avian erythroblastosis virus (strain H) ORGANISM #formal_name avian erythroblastosis virus DATE 18-Apr-1984 #sequence_revision 18-Apr-1984 #text_change 11-Jun-1999 ACCESSIONS A00644; A38022 REFERENCE A00644 !$#authors Yamamoto, T.; Nishida, T.; Miyajima, N.; Kawai, S.; Ooi, T.; !1Toyoshima, K. !$#journal Cell (1983) 35:71-78 !$#title The erbB gene of avian erythroblastosis virus is a member of !1the src gene family. !$#cross-references MUID:84026539; PMID:6313229 !$#accession A00644 !'##molecule_type DNA !'##residues 1-604 ##label YAM !'##cross-references GB:K01216; NID:g209676; PIDN:AAA42400.1; !1PID:g209678 REFERENCE A38022 !$#authors Debuire, B.; Henry, C.; Benaissa, M.; Biserte, G.; Claverie, !1J.M.; Saule, S.; Martin, P.; Stehelin, D. !$#journal Science (1984) 224:1456-1459 !$#title Sequencing the erbA gene of avian erythroblastosis virus !1reveals a new type of oncogene. !$#cross-references MUID:84223957; PMID:6328658 !$#accession A38022 !'##molecule_type DNA !'##residues 1-28,'W',30-139,'F',141-145,'V',147-152 ##label DEB !'##cross-references GB:K02006 GENETICS !$#gene erbB CLASSIFICATION #superfamily epidermal growth factor receptor; protein !1kinase homology KEYWORDS ATP; oncogene; phosphotransferase; transforming protein; !1tyrosine-specific protein kinase FEATURE !$130-395 #domain protein kinase homology #label KIN\ !$138-146 #region protein kinase ATP-binding motif\ !$165 #active_site Lys #status predicted SUMMARY #length 604 #molecular-weight 67633 #checksum 9121 SEQUENCE /// ENTRY TVFVEB #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) erbB - avian erythroblastosis virus (strain ES4) ORGANISM #formal_name avian erythroblastosis virus DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 11-Jun-1999 ACCESSIONS A25231; B25231 REFERENCE A25231 !$#authors Choi, O.R.; Trainor, C.; Graf, T.; Beug, H.; Engel, J.D. !$#journal Mol. Cell. Biol. (1986) 6:1751-1759 !$#title A single amino acid substitution in v-erbB confers a !1thermolabile phenotype to ts167 avian erythroblastosis !1virus-transformed erythroid cells. !$#cross-references MUID:87064458; PMID:2878364 !$#accession A25231 !'##molecule_type DNA !'##residues 1-540 ##label CHO !'##cross-references GB:M13179; NID:g209679; PIDN:AAA42401.1; !1PID:g209680 !'##note the authors translated the codon AAG for residue 157 as Gly, !1ATG for residue 253 as Leu, and ATC for residue 521 as Met GENETICS !$#gene erbB CLASSIFICATION #superfamily epidermal growth factor receptor; protein !1kinase homology KEYWORDS ATP; oncogene; phosphotransferase; transforming protein; !1tyrosine-specific protein kinase FEATURE !$130-395 #domain protein kinase homology #label KIN\ !$138-146 #region protein kinase ATP-binding motif\ !$165 #active_site Lys #status predicted SUMMARY #length 540 #molecular-weight 60390 #checksum 7223 SEQUENCE /// ENTRY INHUR #type complete TITLE insulin receptor precursor [validated] - human CONTAINS insulin receptor precursor splice form 1; insulin receptor precursor splice form 2; protein-tyrosine kinase (EC 2.7.1.112) ORGANISM #formal_name Homo sapiens #common_name man DATE 05-Jun-1987 #sequence_revision 07-Jul-1995 #text_change 08-Dec-2000 ACCESSIONS A37348; A32214; A32278; B32278; A05275; A61520; A05274; !1S12553; S03360; S02677; A36103; C54170; D54170; I55255; !1I57702; I59537; I83057; I60112 REFERENCE A37348 !$#authors Seino, S.; Seino, M.; Bell, G.I. !$#journal Diabetes (1990) 39:123-128 !$#title Human insulin-receptor gene. Partial sequence and !1amplification of exons by polymerase chain reaction. !$#cross-references MUID:91006864; PMID:2210055 !$#accession A37348 !'##molecule_type DNA !'##residues 1-1382 ##label SEI !'##cross-references GB:M32823; GB:M32824; GB:M32825; GB:M32826; !1GB:M32827; GB:M32828; GB:M32829; GB:M32830; GB:M32831; !1GB:M32832; GB:M32833; GB:M32834; GB:M32835; GB:M32836; !1GB:M32837; GB:M32838; GB:M32839; GB:M32840; GB:M32841; !1GB:M32842; GB:M32972; NID:g186462; PIDN:AAA59452.1; !1PID:g386830 !'##experimental_source fetal liver REFERENCE A32214 !$#authors Seino, S.; Seino, M.; Nishi, S.; Bell, G.I. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:114-118 !$#title Structure of the human insulin receptor gene and !1characterization of its promoter. !$#cross-references MUID:89098861; PMID:2911561 !$#accession A32214 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type DNA; mRNA !'##residues 1-34;1005-1382 ##label SE2 !'##cross-references GB:M23100 REFERENCE A32278 !$#authors Seino, S.; Bell, G.I. !$#journal Biochem. Biophys. Res. Commun. (1989) 159:312-316 !$#title Alternative splicing of human insulin receptor messenger !1RNA. !$#cross-references MUID:89165872; PMID:2538124 !$#accession A32278 !'##molecule_type mRNA !'##residues 698-704;728-772;903-909 ##label SE3 !'##cross-references GB:M24555 !'##note splice form 2 !$#accession B32278 !'##molecule_type mRNA !'##residues 698-704;728-744,757-772;903-909 ##label SE4 !'##note splice form 1 REFERENCE A05275 !$#authors Ebina, Y.; Ellis, L.; Jarnagin, K.; Edery, M.; Graf, L.; !1Clauser, E.; Ou, J.; Masiarz, F.; Kan, Y.W.; Goldfine, I.D.; !1Roth, R.A.; Rutter, W.J. !$#journal Cell (1985) 40:747-758 !$#cross-references MUID:85176928; PMID:2859121 !$#accession A05275 !'##molecule_type mRNA !'##residues 'GGLRGRVGAHTRRTRGPQRSWGPPRSMTPAGQRRAPDPRRPRAPAA',1-170,'H', !1172-447,'T',449-491,'K',493-1382 ##label EBI !'##cross-references GB:M10051 !'##note the authors found a long open reading frame containing two !1possible initiation sites REFERENCE A61520 !$#authors Araki, E.; Shimada, F.; Fukushima, H.; Mori, M.; Shichiri, !1M.; Ebina, Y. !$#journal Diabetes Res. Clin. Pract. (1989) 7(Suppl.1):S31-S33 !$#title Characterization of the promoter region of the human insulin !1receptor gene. !$#cross-references MUID:90032206; PMID:2806055 !$#contents sequence correction !$#accession A61520 !'##molecule_type DNA !'##residues 1-33 ##label ARA !'##note authors redetermined transcription initiation site REFERENCE A05274 !$#authors Ullrich, A.; Bell, J.R.; Chen, E.Y.; Herrera, R.; !1Petruzzelli, L.M.; Dull, T.J.; Gray, A.; Coussens, L.; Liao, !1Y.C.; Tsubokawa, M.; Mason, A.; Seeburg, P.H.; Grunfeld, C.; !1Rosen, O.M.; Ramachandran, J. !$#journal Nature (1985) 313:756-761 !$#cross-references MUID:85137889; PMID:2983222 !$#accession A05274 !'##molecule_type mRNA !'##residues 1-744,757-899,'DT',902-1277,'N',1279-1382 ##label ULL !'##cross-references GB:X02160 !'##note splice form 1 REFERENCE S12553 !$#authors Mosthaf, L.; Grako, K.; Dull, T.J.; Coussens, L.; Ullrich, !1A.; McClain, D.A. !$#journal EMBO J. (1990) 9:2409-2413 !$#title Functionally distinct insulin receptors generated by !1tissue-specific alternative splicing. !$#cross-references MUID:90316094; PMID:2369896 !$#accession S12553 !'##molecule_type mRNA !'##residues 744-823 ##label MOS !'##note splice form 1, called HIR-A, has a higher affinity for insulin !1than splice form 2, called HIR-B, when these receptors are !1expressed in rat !'##note splice form 1 is expressed in adult peripheral nerve, skin, !1kidney, striated muscle, and fibroblasts and is exclusively !1expressed in adult spleen and peripheral blood lymphocytes; !1splice form 2 is predominantly expressed in adult liver REFERENCE S03360 !$#authors Fujita-Yamaguchi, Y.; Hawke, D.H.; Shively, J.E.; Choi, S. !$#journal Protein Seq. Data Anal. (1987) 1:3-6 !$#title Partial amino acid sequence analyses of human placental !1insulin receptor. !$#cross-references MUID:88190050; PMID:3447155 !$#accession S03360 !'##molecule_type protein !'##residues 194-208;347-358;582-589;595-600,'N', !1602-603;610-641;722-729;820-829,'E',831-833 ##label FUJ REFERENCE S02677 !$#authors Tavare, J.M.; Denton, R.M. !$#journal Biochem. J. (1988) 252:607-615 !$#title Studies on the autophosphorylation of the insulin receptor !1from human placenta: analysis of the sites phosphorylated by !1two-dimensional peptide mapping. !$#cross-references MUID:88326279; PMID:3166375 !$#accession S02677 !'##molecule_type protein !'##residues 927-956;981-1020;1183-1195;1353-1369 ##label TAV !'##note tyrosine autophosphorylation sites determined REFERENCE A36103 !$#authors Xu, Q.Y.; Paxton, R.J.; Fujita-Yamaguchi, Y. !$#journal J. Biol. Chem. (1990) 265:18673-18681 !$#title Substructural analysis of the insulin receptor by !1microsequence analyses of limited tryptic fragments isolated !1by sodium dodecyl sulfate-polyacrylamide gel electrophoresis !1in the absence or presence of dithiothreitol. !$#cross-references MUID:91009374; PMID:2211730 !$#accession A36103 !'##molecule_type protein !'##residues 28-34,'X',36-44;192-195,'X',197-205;'X',299-300,'XX', !1303-306,'X',308-309,'PX',312-314;610-621,'XX',624,'X', !1626-627;763-768,'X',770-775,'X',777-780 ##label XUA REFERENCE A54170 !$#authors Kasuya, J.; Paz, I.B.; Maddux, B.A.; Goldfine, I.D.; Hefta, !1S.A.; Fujita-Yamaguchi, Y. !$#journal Biochemistry (1993) 32:13531-13536 !$#title Characterization of human placental insulin-like growth !1factor-I/insulin hybrid receptors by protein microsequencing !1and purification. !$#cross-references MUID:94079885; PMID:8257688 !$#accession C54170 !'##molecule_type protein !'##residues 28-34,'X',36-38,'X',40,'X',42,'X',44-45 ##label KAS !'##experimental_source placenta !'##note sequence extracted from NCBI backbone (NCBIP:141174) and !1corrected to correspond with the published sequence !$#accession D54170 !'##molecule_type protein !'##residues 763-765,'X',767-768,'X',770-775,'X',777-781,'X' ##label KA2 !'##experimental_source placenta !'##note sequence extracted from NCBI backbone (NCBIP:141175) and !1corrected to correspond with the published sequence REFERENCE A44709 !$#authors Schaeffer, L.; Ljungqvist, L. !$#journal Biochem. Biophys. Res. Commun. (1992) 189:650-653 !$#title Identification of a disulfide bridge connecting the !1alpha-subunits of the extracellular domain of the insulin !1receptor. !$#cross-references MUID:93112026; PMID:1472036 !$#contents annotation; disulfide bond assignments REFERENCE A44710 !$#authors Hubbard, S.R.; Wei, L.; Ellis, L.; Hendrickson, W.A. !$#journal Nature (1994) 372:746-754 !$#title Crystal structure of the tyrosine kinase domain of the human !1insulin receptor. !$#cross-references MUID:95089813; PMID:7997262 !$#contents annotation; X-ray crystallography, 2.1 angstroms !$#note unphosphorylated Tyr-1189 binds Asp-1159, blocking access to !1the active site by ATP; when phosphorylated, Tyr-1189 moves !1toward Arg-1158 and other basic residues, opening access to !1the active site REFERENCE I55255 !$#authors Araki, E.; Shimada, F.; Uzawa, H.; Mori, M.; Ebina, Y. !$#journal J. Biol. Chem. (1987) 262:16186-16191 !$#title Characterization of the promoter region of the human insulin !1receptor gene. Evidence for promoter activity. !$#cross-references MUID:88058985; PMID:3680248 !$#accession I55255 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-33 ##label RES !'##cross-references GB:J03466; NID:g186469; PIDN:AAA59175.1; !1PID:g463119 REFERENCE I57702 !$#authors McKeon, C.; Moncada, V.; Pham, T.; Salvatore, P.; Kadowaki, !1T.; Accili, D.; Taylor, S.I. !$#journal Mol. Endocrinol. (1990) 4:647-656 !$#title Structural and functional analysis of the insulin receptor !1promoter. !$#cross-references MUID:91125373; PMID:2280779 !$#accession I57702 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-33 ##label RE2 !'##cross-references GB:M76592; NID:g186476; PIDN:AAC37604.1; !1PID:g553512 REFERENCE I59537 !$#authors Taira, M.; Taira, M.; Hashimoto, N.; Shimada, F.; Suzuki, !1Y.; Kanatsuka, A.; Nakamura, F.; Ebina, Y.; Tatibana, M.; !1Makino, H. !$#journal Science (1989) 245:63-66 !$#title Human diabetes associated with a deletion of the tyrosine !1kinase domain of the insulin receptor. !$#cross-references MUID:89298408; PMID:2544997 !$#accession I59537 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1006-1123 ##label RE3 !'##cross-references GB:M27197; NID:g186466; PIDN:AAA86791.1; !1PID:g186468 REFERENCE I60112 !$#authors Elbein, S.C. !$#journal Diabetes (1989) 38:737-743 !$#title Molecular and clinical characterization of an insertional !1polymorphism of the insulin-receptor gene. !$#cross-references MUID:89252471; PMID:2566545 !$#accession I83057 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 895-1086 ##label RE4 !'##cross-references GB:M29930; NID:g186473; PIDN:AAA59177.1; !1PID:g186474 !$#accession I60112 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 895-1086 ##label RE5 !'##cross-references GB:M29929; NID:g186471; PIDN:AAA59176.1; !1PID:g186472 COMMENT The beta chain contains an ATP binding site, a tyrosine !1autophosphorylation site, an unlocated covalent binding site !1for palmitate on threonine or serine, and an unlocated !1covalent binding site for myristate on lysine. COMMENT Autophosphorylation increases kinase activity and makes it !1more insulin-independent. GENETICS !$#gene GDB:INSR !'##cross-references GDB:119352; OMIM:147670 !$#map_position 19p13.3-19p13.3 !$#introns 34/1; 218/1; 325/1; 375/1; 423/2; 495/1; 537/1; 621/1; 677/ !11; 744/2; 756/2; 848/1; 894/3; 948/1; 982/2; 1005/1; 1086/3; !11123/3; 1177/1; 1220/2; 1265/2 !$#note abnormalities in this protein lead to type A insulin !1resistance syndrome, acanthosis nigricans, leprechaunism, !1and Rabson-Mendenhall syndrome COMPLEX heterotetramer of 2 alpha and 2 beta chains; alpha and beta !1chains are derived from a single polypeptide precursor by !1enzymatic cleavage and are linked by disulfide bonds; in the !1tetramer the two alpha chains are disulfide bonded; also !1naturally forms a disulfide bonded hybrid tetramer with !1insulin-like growth factor receptor (see PIR:IGHUR1) FUNCTION !$#description membrane glycoprotein that mediates the rapid metabolic and !1long-term growth-promoting effects of insulin; insulin binds !1to the extracellular alpha chains, stimulating the beta !1chain tyrosine-kinase activity; the beta chain !1tyrosine-kinase undergoes autophosphorylation and catalyzes !1phosphorylation of intracellular proteins CLASSIFICATION #superfamily insulin receptor; protein kinase homology KEYWORDS alternative splicing; ATP; autophosphorylation; !1glycoprotein; hormone receptor; kinase-related transforming !1protein; phosphoprotein; phosphotransferase; transmembrane !1protein; tyrosine-specific protein kinase FEATURE !$1-1382 #product insulin receptor precursor splice form 2 !8#status predicted #label SF2\ !$1-744,757-1382 #product insulin receptor precursor splice form 1 !8#status predicted #label SF1\ !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-758 #product insulin receptor alpha chain #status !8experimental #label ALP\ !$182-339 #region cysteine-rich\ !$763-1382 #product insulin receptor beta chain #status !8experimental #label BET\ !$957-979 #domain transmembrane #status predicted #label TMN\ !$1021-1297 #domain protein kinase homology #label KIN\ !$1029-1037 #region protein kinase ATP-binding motif\ !$43,769,782 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$52,105,138,242,282, !$322,364,424,445, !$541,633,651,698, !$920,933,1060 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$462-495 #disulfide_bonds #status experimental\ !$551 #disulfide_bonds interchain #status experimental\ !$1057,1159 #active_site Lys, Asp #status predicted\ !$1185,1189,1190, !$1355,1361 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status experimental SUMMARY #length 1382 #molecular-weight 156317 #checksum 7692 SEQUENCE /// ENTRY IGHUR1 #type complete TITLE insulin-like growth factor 1 receptor precursor - human ALTERNATE_NAMES IGF-I receptor CONTAINS insulin-like growth factor 1 receptor alpha chain; insulin-like growth factor 1 receptor beta chain; protein-tyrosine kinase (EC 2.7.1.112) ORGANISM #formal_name Homo sapiens #common_name man DATE 24-Jun-1987 #sequence_revision 10-May-1996 #text_change 18-Feb-2000 ACCESSIONS A25690; B38268; PQ0159; A54170; B54170 REFERENCE A25690 !$#authors Ullrich, A.; Gray, A.; Tam, A.W.; Yang-Feng, T.; Tsubokawa, !1M.; Collins, C.; Henzel, W.; Le Bon, T.; Kathuria, S.; Chen, !1E.; Jacobs, S.; Francke, U.; Ramachandran, J.; !1Fujita-Yamaguchi, Y. !$#journal EMBO J. (1986) 5:2503-2512 !$#cross-references MUID:87053815; PMID:2877871 !$#accession A25690 !'##molecule_type mRNA !'##residues 1-1367 ##label ULL !'##cross-references EMBL:M24599; GB:X04434; NID:g33058; !1PIDN:CAA28030.1; PID:g804990 !'##experimental_source placenta !'##note parts of this sequence were confirmed by peptide sequencing REFERENCE A38268 !$#authors Partanen, J.; Maekelae, T.P.; Alitalo, R.; Lehvaeslaiho, H.; !1Alitalo, K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:8913-8917 !$#title Putative tyrosine kinases expressed in K-562 human leukemia !1cells. !$#cross-references MUID:91062389; PMID:2247464 !$#accession B38268 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type mRNA !'##residues 1137-1193 ##label PAR REFERENCE PQ0159 !$#authors Cooke, D.W.; Bankert, L.A.; Roberts Jr., C.T.; LeRoith, D.; !1Casella, S.J. !$#journal Biochem. Biophys. Res. Commun. (1991) 177:1113-1120 !$#title Analysis of the human type I insulin-like growth factor !1receptor promotor region. !$#cross-references MUID:91282751; PMID:1711844 !$#accession PQ0159 !'##status translation not shown !'##molecule_type DNA !'##residues 1-31 ##label COO !'##cross-references GB:M69229; NID:g184837; PIDN:AAB59399.1; !1PID:g184838 REFERENCE A54170 !$#authors Kasuya, J.; Paz, I.B.; Maddux, B.A.; Goldfine, I.D.; Hefta, !1S.A.; Fujita-Yamaguchi, Y. !$#journal Biochemistry (1993) 32:13531-13536 !$#title Characterization of human placental insulin-like growth !1factor-I/insulin hybrid receptors by protein microsequencing !1and purification. !$#cross-references MUID:94079885; PMID:8257688 !$#accession A54170 !'##molecule_type protein !'##residues 31-32,'X',34-39,'X',41-45 ##label KAS !'##experimental_source placenta !'##note sequence extracted from NCBI backbone (NCBIP:141172) and !1corrected to correspond with the published sequence !$#accession B54170 !'##molecule_type protein !'##residues 741-746,'X',748-750 ##label KA2 !'##experimental_source placenta GENETICS !$#gene GDB:IGF1R !'##cross-references GDB:120082; OMIM:147370 !$#map_position 15q26.1-15qter COMPLEX heterotetramer of 2 alpha and 2 beta chains; alpha and beta !1chains are derived from a single polypeptide precursor by !1enzymatic cleavage and are linked by disulfide bonds; in the !1tetramer the two alpha chains are disulfide bonded; also !1naturally forms a disulfide bonded hybrid tetramer with !1insulin receptor (see PIR:INHUR) FUNCTION !$#description membrane glycoprotein that mediates the effects of !1insulin-like growth hormone 1; insulin-like growth hormone 1 !1binds to the extracellular alpha chains, stimulating the !1beta chain tyrosine-kinase activity; the beta chain !1tyrosine-kinase undergoes autophosphorylation and catalyzes !1phosphorylation of intracellular proteins CLASSIFICATION #superfamily insulin receptor; protein kinase homology KEYWORDS ATP; autophosphorylation; glycoprotein; growth factor !1receptor; phosphoprotein; phosphotransferase; transmembrane !1protein; tyrosine-specific protein kinase FEATURE !$1-30 #domain signal sequence #status predicted #label SIG\ !$31-736 #product insulin-like growth factor 1 receptor alpha !8chain #status predicted #label ALP\ !$178-332 #region cysteine-rich\ !$741-1367 #product insulin-like growth factor 1 receptor beta !8chain #status predicted #label BET\ !$936-958 #domain transmembrane #status predicted #label TMM\ !$997-1273 #domain protein kinase homology #label KIN\ !$1005-1013 #region protein kinase ATP-binding motif\ !$102,135,244,314, !$417,438,534,607, !$622,640,756,764, !$900,913 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$455-488 #disulfide_bonds #status predicted\ !$544 #disulfide_bonds interchain #status predicted\ !$747 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$1033,1135 #active_site Lys, Asp #status predicted\ !$1161,1165,1166,1346 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status experimental SUMMARY #length 1367 #molecular-weight 154792 #checksum 5371 SEQUENCE /// ENTRY A56081 #type complete TITLE insulin receptor - fruit fly (Drosophila melanogaster) CONTAINS protein-tyrosine kinase (EC 2.7.1.-) ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A56081; A26378; A24147 REFERENCE A56081 !$#authors Ruan, Y.; Chen, C.; Cao, Y.; Garofalo, R.S. !$#journal J. Biol. Chem. (1995) 270:4236-4243 !$#title The Drosophila insulin receptor contains a novel !1carboxyl-terminal extension likely to play an important role !1in signal transduction. !$#cross-references MUID:95181404; PMID:7876183 !$#accession A56081 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-2148 ##label RUA !'##cross-references GB:U18351 REFERENCE A26378 !$#authors Nishida, Y.; Hata, M.; Nishizuka, Y.; Rutter, W.J.; Ebina, !1Y. !$#journal Biochem. Biophys. Res. Commun. (1986) 141:474-481 !$#title Cloning of a Drosophila cDNA encoding a polypeptide similar !1to the human insulin receptor precursor. !$#cross-references MUID:87100165; PMID:3099787 !$#accession A26378 !'##molecule_type mRNA !'##residues 656,'PPPPPPPL',665-682,'G',684,'R',686-726,'LAAI',731, !1733-867,'TQL',871,'AVTIHAMIAG',882-936,940-957,'NLMA', !1963-1164,1166-1190,'SAAIIH',1197-1227,'ATFSLGRHQL', !11237-1266,'RLQPDCRLFN',1277,'AQR',1281,'PLQLQ',1287-1460, !1'VE',1463-1472,'RSGMRPDDVS',1483,'IAWM',1489-1502,'V', !11504-1685,'H',1687-1709,'S',1711-1756 ##label NIS !'##cross-references GB:M14778; NID:g157759; PIDN:AAA28644.1; !1PID:g157760 REFERENCE A24147 !$#authors Petruzzelli, L.; Herrera, R.; Arenas-Garcia, R.; Fernandez, !1R.; Birnbaum, M.J.; Rosen, O.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:4710-4714 !$#title Isolation of a Drosophila genomic sequence homologous to the !1kinase domain of the human insulin receptor and detection of !1the phosphorylated Drosophila receptor with an anti-peptide !1antibody. !$#cross-references MUID:86259667; PMID:3014506 !$#accession A24147 !'##molecule_type DNA !'##residues 'LIQQ',1308-1476,'DGHDDVS',1484-1522,'PF',1525-1572, !1'QAWCLLLVPVT',1583-1594,'I',1596,'SLWRSP' ##label PET !'##cross-references GB:M13568; NID:g157761; PIDN:AAA28645.1; !1PID:g157762 !'##experimental_source unspecified Drosophila species GENETICS !$#gene FlyBase:InR !'##cross-references FlyBase:FBgn0013984 CLASSIFICATION #superfamily Drosophila insulin receptor; protein kinase !1homology KEYWORDS ATP; glycoprotein; hormone receptor; kinase-related !1transforming protein; phosphotransferase; protein kinase; !1transmembrane protein FEATURE !$1315-1331 #domain transmembrane #status predicted #label TMM\ !$1373-1661 #domain protein kinase homology #label KIN\ !$1381-1389 #region protein kinase ATP-binding motif SUMMARY #length 2148 #molecular-weight 240167 #checksum 7335 SEQUENCE /// ENTRY A45558 #type complete TITLE epidermal growth factor receptor homolog precursor - fluke (Schistosoma mansoni) CONTAINS protein-tyrosine kinase (EC 2.7.1.112) ORGANISM #formal_name Schistosoma mansoni DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A45558; S27836 REFERENCE A45558 !$#authors Shoemaker, C.B.; Ramachandran, H.; Landa, A.; dos Reis, !1M.G.; Stein, L.D. !$#journal Mol. Biochem. Parasitol. (1992) 53:17-32 !$#title Alternative splicing of the Schistosoma mansoni gene !1encoding a homologue of epidermal growth factor receptor. !$#cross-references MUID:92365727; PMID:1501637 !$#accession A45558 !'##status preliminary !'##molecule_type mRNA !'##residues 1-1717 ##label SHO !'##cross-references EMBL:M86396; NID:g160957; PIDN:AAA29866.1; !1PID:g160958 !'##note sequence extracted from NCBI backbone (NCBIP:111129) GENETICS !$#gene SER CLASSIFICATION #superfamily fluke epidermal growth factor receptor homolog !11; protein kinase homology KEYWORDS alternative splicing; ATP; autophosphorylation; !1glycoprotein; phosphoprotein; phosphotransferase; receptor; !1transmembrane protein; tyrosine-specific protein kinase FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-1717 #product epidermal growth factor receptor homolog 1 !8#status predicted #label MAT\ !$1018-1323 #domain protein kinase homology #label KIN\ !$1026-1034 #region protein kinase ATP-binding motif SUMMARY #length 1717 #molecular-weight 192303 #checksum 5403 SEQUENCE /// ENTRY TVHUTT #type complete TITLE nerve growth factor receptor precursor, high affinity - human ALTERNATE_NAMES receptor tyrosine kinase trkA CONTAINS protein-tyrosine kinase (EC 2.7.1.112) ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1988 #sequence_revision 30-Jun-1991 #text_change 11-Jun-1999 ACCESSIONS A30124; S02366; A25184 REFERENCE A30124 !$#authors Martin-Zanca, D.; Oskam, R.; Mitra, G.; Copeland, T.; !1Barbacid, M. !$#journal Mol. Cell. Biol. (1989) 9:24-33 !$#title Molecular and biochemical characterization of the human trk !1proto-oncogene. !$#cross-references MUID:89181575; PMID:2927393 !$#accession A30124 !'##molecule_type mRNA !'##residues 1-790 ##label MAR1 !'##cross-references GB:M23102; NID:g339917; PIDN:AAA36770.1; !1PID:g339918 REFERENCE S00261 !$#authors Kozma, S.C.; Redmond, S.M.S.; Xiao-Chang, F.; Saurer, S.M.; !1Groner, B.; Hynes, N.E. !$#journal EMBO J. (1988) 7:147-154 !$#title Activation of the receptor kinase domain of the trk oncogene !1by recombination with two different cellular sequences. !$#cross-references MUID:88196074; PMID:2966065 !$#accession S02366 !'##molecule_type mRNA !'##residues 393-758,'HG',761-790 ##label KOZ !'##cross-references EMBL:X06704; GB:Y00100; NID:g37399; !1PIDN:CAA29888.1; PID:g37400 REFERENCE A25184 !$#authors Martin-Zanca, D.; Hughes, S.H.; Barbacid, M. !$#journal Nature (1986) 319:743-748 !$#title A human oncogene formed by the fusion of truncated !1tropomyosin and protein tyrosine kinase sequences. !$#cross-references MUID:86146854; PMID:2869410 !$#accession A25184 !'##molecule_type mRNA !'##residues 393-762, !1'SNATASRMCTPGCKPWPRHLLSTWMSWARGPAQGLGVVSRNTGACPQHPP' ##label !1MAR2 !'##cross-references EMBL:X03541; NID:g37402; PIDN:CAA27243.1; !1PID:g37403 !'##note the difference at the carboxyl end is due to a frameshift COMMENT The proto-oncogene trkA is activated by gene fusion. The !1amino end of several different cellular proteins has been !1found fused with the protein tyrosine kinase domain encoded !1by trkA. GENETICS !$#gene GDB:NTRK1; TRK !'##cross-references GDB:127897; OMIM:191315 !$#map_position 1q21-1q22 FUNCTION !$#description regulation of nervous system development; receptor for nerve !1growth factor; also binds neurotrophin-3 and neurotrophin-4 CLASSIFICATION #superfamily nerve growth factor receptor, high affinity; !1leucine-rich alpha-2-glycoprotein repeat homology; protein !1kinase homology KEYWORDS ATP; autophosphorylation; glycoprotein; growth factor !1receptor; phosphoprotein; phosphotransferase; !1proto-oncogene; tandem repeat; transforming protein; !1transmembrane protein; tyrosine-specific protein kinase FEATURE !$1-32 #domain signal sequence #status predicted #label SIG\ !$33-790 #product nerve growth factor receptor, high-affinity !8#status predicted #label MAT\ !$33-415 #domain extracellular #status predicted #label EXT\ !$67-91 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR1\ !$92-115 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR2\ !$116-138 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR3\ !$139-150 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #status atypical #label LRR4\ !$416-432 #domain transmembrane #status predicted #label TMN\ !$433-790 #domain cytosolic #status predicted #label CYT\ !$502-782 #domain protein kinase homology #label KIN\ !$510-518 #region protein kinase ATP-binding motif\ !$67,95,121,188,202, !$253,262,281,318, !$323,338,358,395 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$538 #active_site Lys #status predicted\ !$674 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted\ !$785 #binding_site phosphate (Tyr) (covalent) #status !8predicted SUMMARY #length 790 #molecular-weight 86878 #checksum 4626 SEQUENCE /// ENTRY TVRTTB #type complete TITLE nerve growth factor receptor precursor, high affinity - rat ALTERNATE_NAMES receptor tyrosine kinase trkA CONTAINS protein-tyrosine kinase (EC 2.7.1.112) ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 02-Jun-2000 ACCESSIONS A41981 REFERENCE A41981 !$#authors Meakin, S.O.; Suter, U.; Drinkwater, C.C.; Welcher, A.A.; !1Shooter, E.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:2374-2378 !$#title The rat trk protooncogene product exhibits properties !1characteristic of the slow nerve growth factor receptor. !$#cross-references MUID:92196121; PMID:1312719 !$#accession A41981 !'##molecule_type mRNA !'##residues 1-799 ##label MEA !'##cross-references GB:M85214; NID:g207481; PIDN:AAA42286.1; !1PID:g207482 !'##note sequence extracted from NCBI backbone (NCBIN:88433, !1NCBIP:88434) !'##note in Genbank entry RATTRKPREC, release 113.0, the source is !1designated as Rattus rattus, cell line PC-12 COMMENT The proto-oncogene trkA is activated by gene fusion. The !1amino end of several different cellular proteins has been !1found fused with the protein tyrosine kinase domain encoded !1by trkA. FUNCTION !$#description regulation of nervous system development; receptor for nerve !1growth factor; also binds neurotrophin-3 and neurotrophin-4 CLASSIFICATION #superfamily nerve growth factor receptor, high affinity; !1leucine-rich alpha-2-glycoprotein repeat homology; protein !1kinase homology KEYWORDS ATP; autophosphorylation; glycoprotein; growth factor !1receptor; phosphoprotein; phosphotransferase; !1proto-oncogene; tandem repeat; transforming protein; !1transmembrane protein; tyrosine-specific protein kinase FEATURE !$1-32 #domain signal sequence #status predicted #label SIG\ !$33-799 #product nerve growth factor receptor, high-affinity !8#status predicted #label MAT\ !$33-424 #domain extracellular #status predicted #label EXT\ !$67-91 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR1\ !$92-115 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR2\ !$116-138 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR3\ !$139-150 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #status atypical #label LRR4\ !$425-441 #domain transmembrane #status predicted #label TMN\ !$442-799 #domain cytosolic #status predicted #label CYT\ !$511-791 #domain protein kinase homology #label KIN\ !$519-527 #region protein kinase ATP-binding motif\ !$67,121,190,204,255, !$264,320,325,341, !$361,404 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$547 #active_site Lys #status predicted\ !$683 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted\ !$794 #binding_site phosphate (Tyr) (covalent) #status !8predicted SUMMARY #length 799 #molecular-weight 87868 #checksum 3083 SEQUENCE /// ENTRY A56853 #type complete TITLE brain-derived neurotrophic factor receptor precursor - human ALTERNATE_NAMES receptor tyrosine kinase trkB CONTAINS protein-tyrosine kinase (EC 2.7.1.112) ORGANISM #formal_name Homo sapiens #common_name man DATE 11-Aug-1995 #sequence_revision 11-Aug-1995 #text_change 11-Jun-1999 ACCESSIONS A56853; I56557 REFERENCE A56853 !$#authors Nakagawara, A.; Liu, X.G.; Ikegaki, N.; White, P.S.; !1Yamashiro, D.J.; Nycum, L.M.; Biegel, J.A.; Brodeur, G.M. !$#journal Genomics (1995) 25:538-546 !$#title Cloning and chromosomal localization of the human TRK-B !1tyrosine kinase receptor gene (NTRK2). !$#cross-references MUID:95309922; PMID:7789988 !$#accession A56853 !'##molecule_type mRNA !'##residues 1-822 ##label NAK !'##cross-references GB:U12140; NID:g525313; PIDN:AAC51371.1; !1PID:g530791 REFERENCE I56557 !$#authors Shelton, D.L.; Sutherland, J.; Gripp, J.; Camerato, T.; !1Armanini, M.P.; Phillips, H.S.; Carroll, K.; Spencer, S.D.; !1Levinson, A.D. !$#journal J. Neurosci. (1995) 15:477-491 !$#title Human trks: molecular cloning, tissue distribution, and !1expression of extracellular domain immunoadhesins. !$#cross-references MUID:95123473; PMID:7823156 !$#accession I56557 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-822 ##label SHE !'##cross-references GB:S76473; NID:g913717; PIDN:AAB33109.1; !1PID:g913718 GENETICS !$#gene GDB:NTRK2; trkB !'##cross-references GDB:127898; OMIM:600456 !$#map_position 9q22.1-9q22.1 FUNCTION !$#description regulation of nervous system development; receptor for !1brain-derived neurotrophic factor; also binds neurotrophin-4 CLASSIFICATION #superfamily nerve growth factor receptor, high affinity; !1leucine-rich alpha-2-glycoprotein repeat homology; protein !1kinase homology KEYWORDS alternative splicing; ATP; autophosphorylation; !1glycoprotein; growth factor receptor; phosphoprotein; !1phosphotransferase; tandem repeat; transmembrane protein; !1tyrosine-specific protein kinase FEATURE !$1-31 #domain signal sequence #status predicted #label SIG\ !$32-822 #product brain-derived neurotrophic factor receptor !8#status predicted #label MAT\ !$32-435 #domain extracellular #status predicted #label EXT\ !$67-91 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR1\ !$92-115 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR2\ !$116-138 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR3\ !$139-150 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #status atypical #label LRR4\ !$436-452 #domain transmembrane #status predicted #label TMN\ !$453-822 #domain cytosolic #status predicted #label CYT\ !$536-814 #domain protein kinase homology #label KIN\ !$544-552 #region protein kinase ATP-binding motif\ !$67,95,121,178,205, !$241,254,280,325, !$338,350,412 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$572 #active_site Lys #status predicted\ !$706 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted\ !$817 #binding_site phosphate (Tyr) (covalent) #status !8predicted SUMMARY #length 822 #molecular-weight 91998 #checksum 9157 SEQUENCE /// ENTRY I73631 #type complete TITLE brain-derived neurotrophic factor receptor precursor, short splice form - human ALTERNATE_NAMES neurotrophin receptor trkB; truncated receptor tyrosine kinase trkB ORGANISM #formal_name Homo sapiens #common_name man DATE 02-Aug-1996 #sequence_revision 02-Aug-1996 #text_change 11-Jun-1999 ACCESSIONS I73631; I38357; S66384; S44129 REFERENCE I56557 !$#authors Shelton, D.L.; Sutherland, J.; Gripp, J.; Camerato, T.; !1Armanini, M.P.; Phillips, H.S.; Carroll, K.; Spencer, S.D.; !1Levinson, A.D. !$#journal J. Neurosci. (1995) 15:477-491 !$#title Human trks: molecular cloning, tissue distribution, and !1expression of extracellular domain immunoadhesins. !$#cross-references MUID:95123473; PMID:7823156 !$#accession I73631 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-477 ##label RES !'##cross-references GB:S76474; NID:g913719; PIDN:AAB33110.1; !1PID:g913720 REFERENCE I38357 !$#authors Allen, S.J.; Dawbarn, D.; Eckford, S.D.; Wilcock, G.K.; !1Ashcroft, M.; Colebrook, S.M.; Feeney, R.; MacGowan, S.H. !$#journal Neuroscience (1994) 60:825-834 !$#title Cloning of a non-catalytic form of human trkB and !1distribution of messenger RNA for trkB in human brain. !$#cross-references MUID:95022162; PMID:7936202 !$#accession I38357 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-477 ##label RE2 !'##cross-references EMBL:X75958; NID:g473007; PIDN:CAA53571.1; !1PID:g473008 REFERENCE S66384 !$#authors Haniu, M.; Talvenheimo, J.; Le, J.; Katta, V.; Welcher, A.; !1Rohde, M.F. !$#journal Arch. Biochem. Biophys. (1995) 322:256-264 !$#title Extracellular domain of neurotrophin receptor trkB: !1disulfide structure, N-glycosylation sites, and ligand !1binding. !$#cross-references MUID:96004804; PMID:7574684 !$#accession S66384 !'##molecule_type protein !'##residues !132-37;38-42;43-57;143-155;167-179;183-199;302-308;329-333; !1334-337,'X',339-348;414-429 ##label HAN COMMENT This form of the receptor is missing the protein kinase !1domain. GENETICS !$#gene GDB:NTRK2; trkB !'##cross-references GDB:127898; OMIM:600456 !$#map_position 9q22.1-9q22.1 CLASSIFICATION #superfamily nerve growth factor receptor, high affinity; !1leucine-rich alpha-2-glycoprotein repeat homology; protein !1kinase homology KEYWORDS alternative splicing; glycoprotein; growth factor receptor; !1tandem repeat; transmembrane protein FEATURE !$1-31 #domain signal sequence #status predicted #label SIG\ !$32-477 #product brain-derived neurotrophic factor receptor, !8short splice form #status predicted #label MAT\ !$32-435 #domain extracellular #status predicted #label EXT\ !$67-91 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR1\ !$92-115 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR2\ !$116-138 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR3\ !$139-150 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #status atypical #label LRR4\ !$436-452 #domain transmembrane #status predicted #label TMN\ !$453-477 #domain cytosolic #status predicted #label CYT\ !$32-38,36-45, !$152-176,154-194, !$218-266,302-345 #disulfide_bonds #status experimental\ !$67,95,121,178,205, !$241,254,280,325, !$338,350,412 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 477 #molecular-weight 53051 #checksum 5271 SEQUENCE /// ENTRY S06943 #type complete TITLE brain-derived neurotrophic factor receptor precursor - mouse ALTERNATE_NAMES receptor tyrosine kinase trkB CONTAINS protein-tyrosine kinase (EC 2.7.1.112) ORGANISM #formal_name Mus musculus #common_name house mouse DATE 22-Jan-1993 #sequence_revision 22-Jan-1993 #text_change 11-Jun-1999 ACCESSIONS S06943 REFERENCE S06943 !$#authors Klein, R.; Parada, L.F.; Coulier, F.; Barbacid, M. !$#journal EMBO J. (1989) 8:3701-3709 !$#title trkB, a novel tyrosine protein kinase receptor expressed !1during mouse neural development. !$#cross-references MUID:90059970; PMID:2555172 !$#accession S06943 !'##molecule_type mRNA !'##residues 1-821 ##label KLE !'##cross-references EMBL:X17647; NID:g55505; PIDN:CAA35636.1; !1PID:g55506 GENETICS !$#gene trkB FUNCTION !$#description regulation of nervous system development; receptor for !1brain-derived neurotrophic factor; also binds neurotrophin-4 CLASSIFICATION #superfamily nerve growth factor receptor, high affinity; !1leucine-rich alpha-2-glycoprotein repeat homology; protein !1kinase homology KEYWORDS alternative splicing; ATP; autophosphorylation; !1glycoprotein; growth factor receptor; phosphoprotein; !1phosphotransferase; tandem repeat; transmembrane protein; !1tyrosine-specific protein kinase FEATURE !$1-31 #domain signal sequence #status predicted #label SIG\ !$32-821 #product brain-derived neurotrophic factor receptor !8#status predicted #label MAT\ !$32-434 #domain extracellular #status predicted #label EXT\ !$67-91 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR1\ !$92-115 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR2\ !$116-138 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR3\ !$139-150 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #status atypical #label LRR4\ !$435-451 #domain transmembrane #status predicted #label TMN\ !$452-821 #domain cytosolic #status predicted #label CYT\ !$535-813 #domain protein kinase homology #label KIN\ !$543-551 #region protein kinase ATP-binding motif\ !$67,95,121,178,205, !$241,254,280,325, !$338,350,411 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$571 #active_site Lys #status predicted\ !$706 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted\ !$816 #binding_site phosphate (Tyr) (covalent) #status !8predicted SUMMARY #length 821 #molecular-weight 92132 #checksum 4037 SEQUENCE /// ENTRY A35104 #type complete TITLE brain-derived neurotrophic factor receptor precursor, short splice form - mouse ALTERNATE_NAMES truncated receptor tyrosine kinase trkB ORGANISM #formal_name Mus musculus #common_name house mouse DATE 07-Sep-1990 #sequence_revision 06-Nov-1992 #text_change 11-Jun-1999 ACCESSIONS A35104 REFERENCE A35104 !$#authors Klein, R.; Conway, D.; Parada, L.F.; Barbacid, M. !$#journal Cell (1990) 61:647-656 !$#title The trkB tyrosine protein kinase gene codes for a second !1neurogenic receptor that lacks the catalytic kinase domain. !$#cross-references MUID:90263089; PMID:2160854 !$#accession A35104 !'##status preliminary !'##molecule_type mRNA !'##residues 1-476 ##label KLE !'##cross-references GB:M33385; NID:g202158; PIDN:AAA40482.1; !1PID:g202159 COMMENT This form of the receptor is missing the protein kinase !1domain. CLASSIFICATION #superfamily nerve growth factor receptor, high affinity; !1leucine-rich alpha-2-glycoprotein repeat homology; protein !1kinase homology KEYWORDS alternative splicing; glycoprotein; growth factor receptor; !1tandem repeat; transmembrane protein FEATURE !$1-31 #domain signal sequence #status predicted #label SIG\ !$32-476 #product brain-derived neurotrophic factor receptor, !8short splice form #status predicted #label MAT\ !$32-434 #domain extracellular #status predicted #label EXT\ !$67-91 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR1\ !$92-115 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR2\ !$116-138 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR3\ !$139-150 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #status atypical #label LRR4\ !$435-451 #domain transmembrane #status predicted #label TMN\ !$452-476 #domain cytosolic #status predicted #label CYT\ !$67,95,121,178,205, !$241,254,280,325, !$338,350,411 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 476 #molecular-weight 53185 #checksum 9282 SEQUENCE /// ENTRY A39667 #type complete TITLE brain-derived neurotrophic factor receptor precursor - rat ALTERNATE_NAMES receptor tyrosine kinase trkB.FL CONTAINS protein-tyrosine kinase (EC 2.7.1.112) ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 27-Nov-1991 #sequence_revision 27-Nov-1991 #text_change 11-Jun-1999 ACCESSIONS A39667 REFERENCE A39667 !$#authors Middlemas, D.S.; Lindberg, R.A.; Hunter, T. !$#journal Mol. Cell. Biol. (1991) 11:143-153 !$#title trkB, a neural receptor protein-tyrosine kinase: evidence !1for a full-length and two truncated receptors. !$#cross-references MUID:91094826; PMID:1846020 !$#accession A39667 !'##status preliminary !'##molecule_type mRNA !'##residues 1-821 ##label MID !'##cross-references GB:M55291; NID:g207473; PIDN:AAA42279.1; !1PID:g207474 FUNCTION !$#description regulation of nervous system development; receptor for !1brain-derived neurotrophic factor; also binds neurotrophin-4 CLASSIFICATION #superfamily nerve growth factor receptor, high affinity; !1leucine-rich alpha-2-glycoprotein repeat homology; protein !1kinase homology KEYWORDS alternative splicing; ATP; autophosphorylation; !1glycoprotein; growth factor receptor; phosphoprotein; !1phosphotransferase; tandem repeat; transmembrane protein; !1tyrosine-specific protein kinase FEATURE !$1-31 #domain signal sequence #status predicted #label SIG\ !$32-821 #product brain-derived neurotrophic factor receptor !8#status predicted #label MAT\ !$32-434 #domain extracellular #status predicted #label EXT\ !$67-91 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR1\ !$92-115 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR2\ !$116-138 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR3\ !$139-150 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #status atypical #label LRR4\ !$435-451 #domain transmembrane #status predicted #label TMN\ !$452-821 #domain cytosolic #status predicted #label CYT\ !$535-813 #domain protein kinase homology #label KIN\ !$543-551 #region protein kinase ATP-binding motif\ !$67,95,121,178,205, !$241,254,280,325, !$338,350,411 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$571 #active_site Lys #status predicted\ !$705 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted\ !$816 #binding_site phosphate (Tyr) (covalent) #status !8predicted SUMMARY #length 821 #molecular-weight 92185 #checksum 4298 SEQUENCE /// ENTRY B39667 #type complete TITLE brain-derived neurotrophic factor receptor precursor, splice form T1 - rat ALTERNATE_NAMES truncated receptor tyrosine kinase trkB.T1 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 27-Nov-1991 #sequence_revision 27-Nov-1991 #text_change 11-Jun-1999 ACCESSIONS B39667 REFERENCE A39667 !$#authors Middlemas, D.S.; Lindberg, R.A.; Hunter, T. !$#journal Mol. Cell. Biol. (1991) 11:143-153 !$#title trkB, a neural receptor protein-tyrosine kinase: evidence !1for a full-length and two truncated receptors. !$#cross-references MUID:91094826; PMID:1846020 !$#accession B39667 !'##status preliminary !'##molecule_type mRNA !'##residues 1-476 ##label MID !'##cross-references GB:M55292; NID:g207475; PIDN:AAA42280.1; !1PID:g207476 COMMENT This form of the receptor is missing the protein kinase !1domain. CLASSIFICATION #superfamily nerve growth factor receptor, high affinity; !1leucine-rich alpha-2-glycoprotein repeat homology; protein !1kinase homology KEYWORDS alternative splicing; glycoprotein; growth factor receptor; !1tandem repeat; transmembrane protein FEATURE !$1-31 #domain signal sequence #status predicted #label SIG\ !$32-476 #product brain-derived neurotrophic factor receptor, !8splice form T1 #status predicted #label MAT\ !$32-434 #domain extracellular #status predicted #label EXT\ !$67-91 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR1\ !$92-115 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR2\ !$116-138 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR3\ !$139-150 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #status atypical #label LRR4\ !$435-451 #domain transmembrane #status predicted #label TMN\ !$452-476 #domain cytosolic #status predicted #label CYT\ !$67,95,121,178,205, !$241,254,280,325, !$338,350,411 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 476 #molecular-weight 53211 #checksum 9558 SEQUENCE /// ENTRY C39667 #type complete TITLE brain-derived neurotrophic factor receptor precursor, splice form T2 - rat ALTERNATE_NAMES truncated receptor tyrosine kinase trkB.T2 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 27-Nov-1991 #sequence_revision 27-Nov-1991 #text_change 11-Jun-1999 ACCESSIONS C39667 REFERENCE A39667 !$#authors Middlemas, D.S.; Lindberg, R.A.; Hunter, T. !$#journal Mol. Cell. Biol. (1991) 11:143-153 !$#title trkB, a neural receptor protein-tyrosine kinase: evidence !1for a full-length and two truncated receptors. !$#cross-references MUID:91094826; PMID:1846020 !$#accession C39667 !'##status preliminary !'##molecule_type mRNA !'##residues 1-474 ##label MID !'##cross-references GB:M55293; NID:g207477; PIDN:AAA42281.1; !1PID:g207478 COMMENT This form of the receptor is missing the protein kinase !1domain. CLASSIFICATION #superfamily nerve growth factor receptor, high affinity; !1leucine-rich alpha-2-glycoprotein repeat homology; protein !1kinase homology KEYWORDS alternative splicing; glycoprotein; growth factor receptor; !1tandem repeat; transmembrane protein FEATURE !$1-31 #domain signal sequence #status predicted #label SIG\ !$32-474 #product brain-derived neurotrophic factor receptor, !8splice form T2 #status predicted #label MAT\ !$32-434 #domain extracellular #status predicted #label EXT\ !$67-91 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR1\ !$92-115 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR2\ !$116-138 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR3\ !$139-150 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #status atypical #label LRR4\ !$435-451 #domain transmembrane #status predicted #label TMN\ !$452-474 #domain cytosolic #status predicted #label CYT\ !$67,95,121,178,205, !$241,254,280,325, !$338,350,411 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 474 #molecular-weight 52971 #checksum 6725 SEQUENCE /// ENTRY S44098 #type complete TITLE brain-derived neurotrophic factor receptor precursor - chicken ALTERNATE_NAMES receptor tyrosine kinase trkB CONTAINS protein-tyrosine kinase (EC 2.7.1.112) ORGANISM #formal_name Gallus gallus #common_name chicken DATE 13-Jan-1995 #sequence_revision 13-Jan-1995 #text_change 11-Jun-1999 ACCESSIONS S59939; S42175; S44098 REFERENCE S59938 !$#authors Vinh, N.Q.; Erdmann, K.S.; Heumann, R. !$#journal Gene (1994) 149:383-384 !$#title Cloning and sequence analysis of a cDNA encoding a novel !1truncated form of the chicken TrkB receptor. !$#cross-references MUID:95047511; PMID:7959025 !$#accession S59939 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type mRNA !'##residues 1-818 ##label VI2 !'##cross-references EMBL:X77251; NID:g563881; PIDN:CAA54468.1; !1PID:g472934 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1994 REFERENCE S42175 !$#authors Dechant, G.; Biffo, S.; Okazawa, H.; Kolbeck, R.; !1Pottgiesser, J.; Barde, Y.A. !$#journal Development (1993) 119:545-558 !$#title Expression and binding characteristics of the BDNF receptor !1chick trkB. !$#cross-references MUID:94116452; PMID:8287802 !$#accession S42175 !'##status preliminary !'##molecule_type mRNA !'##residues 1-818 ##label DEC !'##cross-references EMBL:X74109; NID:g407798; PIDN:CAA52210.1; !1PID:g407799 GENETICS !$#gene trkB FUNCTION !$#description regulation of nervous system development; receptor for !1brain-derived neurotrophic factor; also binds neurotrophin-4 CLASSIFICATION #superfamily nerve growth factor receptor, high affinity; !1leucine-rich alpha-2-glycoprotein repeat homology; protein !1kinase homology KEYWORDS alternative splicing; ATP; autophosphorylation; !1glycoprotein; growth factor receptor; phosphoprotein; !1phosphotransferase; tandem repeat; transmembrane protein; !1tyrosine-specific protein kinase FEATURE !$1-31 #domain signal sequence #status predicted #label SIG\ !$32-818 #product brain-derived neurotrophic factor receptor !8#status predicted #label MAT\ !$32-432 #domain extracellular #status predicted #label EXT\ !$66-90 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR1\ !$91-114 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR2\ !$115-137 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR3\ !$138-149 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #status atypical #label LRR4\ !$433-449 #domain transmembrane #status predicted #label TMN\ !$450-818 #domain cytosolic #status predicted #label CYT\ !$532-810 #domain protein kinase homology #label KIN\ !$540-548 #region protein kinase ATP-binding motif\ !$66,94,120,199,204, !$253,287,324,337, !$349,408 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$568 #active_site Lys #status predicted\ !$702 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted\ !$813 #binding_site phosphate (Tyr) (covalent) #status !8predicted SUMMARY #length 818 #molecular-weight 91736 #checksum 548 SEQUENCE /// ENTRY S44099 #type complete TITLE brain-derived neurotrophic factor receptor precursor, splice form T3 - chicken ALTERNATE_NAMES truncated receptor tyrosine kinase trkB.T3 ORGANISM #formal_name Gallus gallus #common_name chicken DATE 13-Jan-1995 #sequence_revision 13-Jan-1995 #text_change 11-Jun-1999 ACCESSIONS S59938; S44099 REFERENCE S59938 !$#authors Vinh, N.Q.; Erdmann, K.S.; Heumann, R. !$#journal Gene (1994) 149:383-384 !$#title Cloning and sequence analysis of a cDNA encoding a novel !1truncated form of the chicken TrkB receptor. !$#cross-references MUID:95047511; PMID:7959025 !$#accession S59938 !'##status preliminary !'##molecule_type mRNA !'##residues 1-520 ##label VI2 !'##cross-references EMBL:X77252; NID:g472935; PIDN:CAA54469.1; !1PID:g472936 COMMENT This form of the receptor is missing the protein kinase !1domain. GENETICS !$#gene trkB CLASSIFICATION #superfamily nerve growth factor receptor, high affinity; !1leucine-rich alpha-2-glycoprotein repeat homology; protein !1kinase homology KEYWORDS alternative splicing; glycoprotein; growth factor receptor; !1tandem repeat; transmembrane protein FEATURE !$1-31 #domain signal sequence #status predicted #label SIG\ !$32-520 #product brain-derived neurotrophic factor receptor, !8splice form T3 #status predicted #label MAT\ !$32-432 #domain extracellular #status predicted #label EXT\ !$66-90 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR1\ !$91-114 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR2\ !$115-137 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR3\ !$138-149 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #status atypical #label LRR4\ !$433-449 #domain transmembrane #status predicted #label TMN\ !$450-520 #domain intracellular #status predicted #label INT\ !$66,94,120,199,204, !$226,253,287,324, !$337,349,408 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 520 #molecular-weight 57877 #checksum 5671 SEQUENCE /// ENTRY I73632 #type complete TITLE neurotrophin-3 receptor precursor - human ALTERNATE_NAMES receptor tyrosine kinase trkC CONTAINS protein-tyrosine kinase (EC 2.7.1.112) ORGANISM #formal_name Homo sapiens #common_name man DATE 02-Aug-1996 #sequence_revision 02-Aug-1996 #text_change 11-Jun-1999 ACCESSIONS I73632 REFERENCE I56557 !$#authors Shelton, D.L.; Sutherland, J.; Gripp, J.; Camerato, T.; !1Armanini, M.P.; Phillips, H.S.; Carroll, K.; Spencer, S.D.; !1Levinson, A.D. !$#journal J. Neurosci. (1995) 15:477-491 !$#title Human trks: molecular cloning, tissue distribution, and !1expression of extracellular domain immunoadhesins. !$#cross-references MUID:95123473; PMID:7823156 !$#accession I73632 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-839 ##label RES !'##cross-references GB:S76475; NID:g913721; PIDN:AAB33111.1; !1PID:g913722 GENETICS !$#gene GDB:NTRK3; TRKC !'##cross-references GDB:127899; OMIM:191316 !$#map_position 15q24-15q25 FUNCTION !$#description regulation of nervous system development; receptor for !1neurotrophin-3 CLASSIFICATION #superfamily nerve growth factor receptor, high affinity; !1leucine-rich alpha-2-glycoprotein repeat homology; protein !1kinase homology KEYWORDS ATP; autophosphorylation; brain; glycoprotein; growth factor !1receptor; phosphoprotein; phosphotransferase; tandem repeat; !1transmembrane protein; tyrosine-specific protein kinase FEATURE !$1-31 #domain signal sequence #status predicted #label SIG\ !$32-839 #product neurotrophin-3 receptor #status predicted !8#label MAT\ !$32-436 #domain extracellular #status predicted #label EXT\ !$79-103 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR1\ !$104-127 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR2\ !$128-150 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR3\ !$151-162 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #status atypical #label LRR4\ !$437-453 #domain transmembrane #status predicted #label TMN\ !$454-839 #domain cytosolic #status predicted #label CYT\ !$536-831 #domain protein kinase homology #label KIN\ !$544-552 #region protein kinase ATP-binding motif\ !$72,79,133,163,203, !$218,232,259,267, !$272,294,375,388 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$572 #active_site Lys #status predicted\ !$709 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted\ !$834 #binding_site phosphate (Tyr) (covalent) #status !8predicted SUMMARY #length 839 #molecular-weight 94454 #checksum 6438 SEQUENCE /// ENTRY A40026 #type complete TITLE neurotrophin-3 receptor precursor - pig ALTERNATE_NAMES receptor tyrosine kinase trkC CONTAINS protein-tyrosine kinase (EC 2.7.1.112) ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 17-Jan-1992 #sequence_revision 17-Jan-1992 #text_change 11-Jun-1999 ACCESSIONS A40026 REFERENCE A40026 !$#authors Lamballe, F.; Klein, R.; Barbacid, M. !$#journal Cell (1991) 66:967-979 !$#title trkC, a new member of the trk family of tyrosine protein !1kinases, is a receptor for neurotrophin-3. !$#cross-references MUID:91364178; PMID:1653651 !$#accession A40026 !'##molecule_type mRNA !'##residues 1-825 ##label LAM !'##cross-references GB:M80800; NID:g164698; PIDN:AAA31130.1; !1PID:g164699 !'##experimental_source adult brain FUNCTION !$#description regulation of nervous system development; receptor for !1neurotrophin-3 CLASSIFICATION #superfamily nerve growth factor receptor, high affinity; !1leucine-rich alpha-2-glycoprotein repeat homology; protein !1kinase homology KEYWORDS ATP; autophosphorylation; brain; glycoprotein; growth factor !1receptor; phosphoprotein; phosphotransferase; tandem repeat; !1transmembrane protein; tyrosine-specific protein kinase FEATURE !$1-31 #domain signal sequence #status predicted #label SIG\ !$32-825 #product neurotrophin-3 receptor #status predicted !8#label MAT\ !$32-436 #domain extracellular #status predicted #label EXT\ !$79-103 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR1\ !$104-127 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR2\ !$128-150 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR3\ !$151-162 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #status atypical #label LRR4\ !$437-453 #domain transmembrane #status predicted #label TMN\ !$454-825 #domain cytosolic #status predicted #label CYT\ !$536-817 #domain protein kinase homology #label KIN\ !$544-552 #region protein kinase ATP-binding motif\ !$68,72,79,133,163, !$203,218,232,259, !$267,272,294,375,388 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$572 #active_site Lys #status predicted\ !$709 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted\ !$820 #binding_site phosphate (Tyr) (covalent) #status !8predicted SUMMARY #length 825 #molecular-weight 93129 #checksum 4457 SEQUENCE /// ENTRY S35695 #type complete TITLE neurotrophin-3 receptor precursor - chicken ALTERNATE_NAMES receptor tyrosine kinase trkC CONTAINS protein-tyrosine kinase (EC 2.7.1.112) ORGANISM #formal_name Gallus gallus #common_name chicken DATE 10-Dec-1993 #sequence_revision 03-Nov-1995 #text_change 11-Jun-1999 ACCESSIONS S35695 REFERENCE S35695 !$#authors Okazawa, H.; Kamei, M.; Kanazawa, I. !$#journal FEBS Lett. (1993) 329:171-177 !$#title Molecular cloning and expression of a novel truncated form !1of chicken trkC. !$#cross-references MUID:93359043; PMID:8394830 !$#accession S35695 !'##molecule_type mRNA !'##residues 1-803 ##label OKA !'##cross-references EMBL:X59669; NID:g416429; PIDN:CAA42202.1; !1PID:g416430 !'##note the authors translated the codon AAC for residue 105 as Val, !1CTG for residue 108 as Gln, ATC for residue 150 as Thr, and !1ATT for residue 326 as Asn FUNCTION !$#description regulation of nervous system development; receptor for !1neurotrophin-3 CLASSIFICATION #superfamily nerve growth factor receptor, high affinity; !1leucine-rich alpha-2-glycoprotein repeat homology; protein !1kinase homology KEYWORDS alternative splicing; ATP; autophosphorylation; brain; !1glycoprotein; growth factor receptor; phosphoprotein; !1phosphotransferase; tandem repeat; transmembrane protein; !1tyrosine-specific protein kinase FEATURE !$1-10 #domain signal sequence #status predicted #label SIG\ !$11-803 #product neurotrophin-3 receptor #status predicted !8#label MAT\ !$11-417 #domain extracellular #status predicted #label EXT\ !$58-82 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR1\ !$83-106 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR2\ !$107-129 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR3\ !$130-141 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #status atypical #label LRR4\ !$418-434 #domain transmembrane #status predicted #label TMN\ !$435-803 #domain cytosolic #status predicted #label CYT\ !$514-795 #domain protein kinase homology #label KIN\ !$522-530 #region protein kinase ATP-binding motif\ !$47,51,58,142,182, !$197,211,238,246, !$251,273,354,367 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$550 #active_site Lys #status predicted\ !$687 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted\ !$798 #binding_site phosphate (Tyr) (covalent) #status !8predicted SUMMARY #length 803 #molecular-weight 90636 #checksum 1617 SEQUENCE /// ENTRY A58674 #type complete TITLE neurotrophin-3 receptor precursor, short splice form - chicken ALTERNATE_NAMES truncated receptor tyrosine kinase trkC ORGANISM #formal_name Gallus gallus #common_name chicken DATE 19-Nov-1997 #sequence_revision 21-Nov-1997 #text_change 21-Nov-1997 ACCESSIONS A58674 REFERENCE S35695 !$#authors Okazawa, H.; Kamei, M.; Kanazawa, I. !$#journal FEBS Lett. (1993) 329:171-177 !$#title Molecular cloning and expression of a novel truncated form !1of chicken trkC. !$#cross-references MUID:93359043; PMID:8394830 !$#accession A58674 !'##molecule_type mRNA !'##residues 1-525 ##label OKA !'##note the authors translated the codon AAC for residue 105 as Val, !1CTG for residue 108 as Gln, ATC for residue 150 as Thr, and !1ATT for residue 326 as Asn COMMENT This form of the receptor is missing the protein kinase !1domain. CLASSIFICATION #superfamily nerve growth factor receptor, high affinity; !1leucine-rich alpha-2-glycoprotein repeat homology; protein !1kinase homology KEYWORDS alternative splicing; brain; glycoprotein; growth factor !1receptor; tandem repeat; transmembrane protein FEATURE !$1-10 #domain signal sequence #status predicted #label SIG\ !$11-525 #product neurotrophin-3 receptor, short form #status !8predicted #label MAT\ !$11-417 #domain extracellular #status predicted #label EXT\ !$58-82 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR1\ !$83-106 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR2\ !$107-129 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR3\ !$130-141 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #status atypical #label LRR4\ !$418-434 #domain transmembrane #status predicted #label TMN\ !$435-525 #domain cytosolic #status predicted #label CYT\ !$47,51,58,142,182, !$197,211,238,246, !$251,273,354,367 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 525 #molecular-weight 58814 #checksum 5679 SEQUENCE /// ENTRY A48289 #type complete TITLE neurotrophic receptor ror precursor - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES trk-related receptor CONTAINS protein-tyrosine kinase (EC 2.7.1.112) ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 17-Nov-2000 ACCESSIONS A48289 REFERENCE A48289 !$#authors Wilson, C.; Goberdhan, D.C.I.; Steller, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:7109-7113 !$#title Dror, a potential neurotrophic receptor gene, encodes a !1Drosophila homolog of the vertebrate Ror family of !1Trk-related receptor tyrosine kinases. !$#cross-references MUID:93348222; PMID:8394009 !$#accession A48289 !'##status preliminary !'##molecule_type mRNA !'##residues 1-685 ##label WIL !'##cross-references GB:L20297; NID:g348103; PIDN:AAA28860.1; !1PID:g348104 GENETICS !$#gene FlyBase:bsk !'##cross-references FlyBase:FBgn0010407 CLASSIFICATION #superfamily Drosophila neurotrophic receptor ror; kringle !1homology; protein kinase homology KEYWORDS ATP; glycoprotein; kringle; phosphotransferase; !1transmembrane protein; tyrosine-specific protein kinase FEATURE !$237-310 #domain kringle homology #label KRG\ !$314-338 #domain transmembrane #status predicted #label TM1\ !$408-677 #domain protein kinase homology #label KIN\ !$416-424 #region protein kinase ATP-binding motif\ !$45,63,129,144,250 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 685 #molecular-weight 78142 #checksum 8512 SEQUENCE /// ENTRY A47299 #type complete TITLE ror-related receptor RTK - Pacific electric ray CONTAINS protein-tyrosine kinase (EC 2.7.1.112) ORGANISM #formal_name Torpedo californica #common_name Pacific electric ray DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-May-2000 ACCESSIONS A47299 REFERENCE A47299 !$#authors Jennings, C.G.; Dyer, S.M.; Burden, S.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:2895-2899 !$#title Muscle-specific trk-related receptor with a kringle domain !1defines a distinct class of receptor tyrosine kinases. !$#cross-references MUID:93219391; PMID:8385349 !$#accession A47299 !'##status preliminary !'##molecule_type mRNA !'##residues 1-946 ##label JEN !'##cross-references GB:L11311; NID:g290857; PIDN:AAA49285.1; !1PID:g290858 !'##experimental_source electric organ !'##note sequence extracted from NCBI backbone (NCBIN:128724, !1NCBIP:128726) CLASSIFICATION #superfamily Torpedo ror-related receptor; immunoglobulin !1homology; kringle homology; protein kinase homology KEYWORDS ATP; glycoprotein; kringle; phosphotransferase; !1transmembrane protein; tyrosine-specific protein kinase FEATURE !$44-103 #domain immunoglobulin homology #label IM1\ !$137-195 #domain immunoglobulin homology #label IM2\ !$229-287 #domain immunoglobulin homology #label IM3\ !$464-542 #domain kringle homology #label KR3\ !$572-588 #domain transmembrane #status predicted #label TMN\ !$650-940 #domain protein kinase homology #label KIN\ !$658-666 #region protein kinase ATP-binding motif\ !$225,340,477,544 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 946 #molecular-weight 105892 #checksum 8717 SEQUENCE /// ENTRY I48697 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) nsk2 precursor, splice form 1 - mouse ALTERNATE_NAMES receptor-type tyrosine kinase CONTAINS protein-tyrosine kinase nsk2 precursor, splice form 3 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 19-May-2000 #sequence_revision 19-May-2000 #text_change 19-May-2000 ACCESSIONS I48697; S60740 REFERENCE I48696 !$#authors Ganju, P.; Walls, E.; Brennan, J.; Reith, A.D. !$#journal Oncogene (1995) 11:281-290 !$#title Cloning and developmental expression of Nsk2, a novel !1receptor tyrosine kinase implicated in skeletal myogenesis. !$#cross-references MUID:95349951; PMID:7624144 !$#accession I48697 !'##status nucleic acid sequence not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-881 ##label GAN1 !'##cross-references EMBL:X86445; NID:g929725; PIDN:CAA60166.1; !1PID:g929726 !'##experimental_source splice form 1 !$#accession S60740 !'##molecule_type DNA !'##residues 1-456,'A',466-881 ##label GAN2 !'##cross-references EMBL:X86445; NID:g929725 !'##experimental_source splice form 3 COMMENT For alternate splice forms see PIR:I48696. GENETICS !$#gene nsk2 !'##cross-references MGI:103308 CLASSIFICATION #superfamily mouse ror-related receptor; immunoglobulin !1homology; protein kinase homology KEYWORDS ATP; glycoprotein; phosphotransferase; receptor; !1transmembrane protein; tyrosine-specific protein kinase FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-881 #product protein-tyrosine kinase nsk2, splice form 1 !8#status predicted #label MAT1\ !$22-456,'A',466-881 #product protein-tyrosine kinase nsk2, splice form 3 !8#status predicted #label MAT3\ !$42-101 #domain immunoglobulin homology #label IMM1\ !$135-192 #domain immunoglobulin homology #label IMM2\ !$226-284 #domain immunoglobulin homology #label IMM3\ !$498-518 #domain transmembrane #status predicted #label TRM\ !$575-865 #domain protein kinase homology #label KIN\ !$583-591 #region protein kinase ATP-binding motif\ !$222,462 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 881 #molecular-weight 98435 #checksum 3041 SEQUENCE /// ENTRY I48696 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) nsk2 precursor, splice form 2 - mouse ALTERNATE_NAMES receptor-type tyrosine kinase CONTAINS protein-tyrosine kinase nsk2 precursor, splice form 4 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 19-May-2000 #sequence_revision 19-May-2000 #text_change 19-May-2000 ACCESSIONS I48696; S60738 REFERENCE I48696 !$#authors Ganju, P.; Walls, E.; Brennan, J.; Reith, A.D. !$#journal Oncogene (1995) 11:281-290 !$#title Cloning and developmental expression of Nsk2, a novel !1receptor tyrosine kinase implicated in skeletal myogenesis. !$#cross-references MUID:95349951; PMID:7624144 !$#accession I48696 !'##status nucleic acid sequence not shown; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-871 ##label GAN1 !'##cross-references EMBL:X86444; NID:g929723; PIDN:CAA60165.1; !1PID:g929724 !'##experimental_source splice form 2 !$#accession S60738 !'##molecule_type DNA !'##residues 1-456,'A',466-871 ##label GAN2 !'##cross-references EMBL:X86444; NID:g929723 !'##experimental_source splice form 4 COMMENT For alternate splice forms see PIR:I48697. GENETICS !$#gene nsk2 !'##cross-references MGI:103308 CLASSIFICATION #superfamily mouse ror-related receptor; immunoglobulin !1homology; protein kinase homology KEYWORDS ATP; glycoprotein; phosphotransferase; receptor; !1transmembrane protein; tyrosine-specific protein kinase FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-871 #product protein-tyrosine kinase nsk2, splice form 2 !8#status predicted #label MAT2\ !$22-456,'A',466-871 #product protein-tyrosine kinase nsk2, splice form 4 !8#status predicted #label MAT4\ !$42-101 #domain immunoglobulin homology #label IMM1\ !$135-192 #domain immunoglobulin homology #label IMM2\ !$226-284 #domain immunoglobulin homology #label IMM3\ !$498-518 #domain transmembrane #status predicted #label TRM\ !$575-865 #domain protein kinase homology #label KIN\ !$583-591 #region protein kinase ATP-binding motif\ !$222,462 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 871 #molecular-weight 97047 #checksum 6731 SEQUENCE /// ENTRY JQ1486 #type complete TITLE activin receptor II precursor - human CONTAINS serine/threonine-specific protein kinase (EC 2.7.1.-) ORGANISM #formal_name Homo sapiens #common_name man DATE 17-Jul-1992 #sequence_revision 19-Oct-1995 #text_change 21-Jul-2000 ACCESSIONS JQ1486; S18908; S22345 REFERENCE JQ1486 !$#authors Donaldson, C.J.; Mathews, L.S.; Vale, W.W. !$#journal Biochem. Biophys. Res. Commun. (1992) 184:310-316 !$#title Molecular cloning and binding properties of the human type !1II activin receptor. !$#cross-references MUID:92231944; PMID:1314589 !$#accession JQ1486 !'##molecule_type mRNA !'##residues 1-513 ##label DON !'##cross-references GB:M93415; NID:g178049; PIDN:AAA35504.1; !1PID:g178050 !'##experimental_source testis REFERENCE S18908 !$#authors Geiser, A.G. !$#submission submitted to the EMBL Data Library, December 1991 !$#accession S18908 !'##molecule_type mRNA !'##residues 1-513 ##label GEI !'##cross-references EMBL:X62381; NID:g28347; PIDN:CAA44245.1; !1PID:g28348 !'##experimental_source mammary gland epithelial cell line B5-589 REFERENCE S22345 !$#authors Matzuk, M.M.; Bradley, A. !$#journal Biochim. Biophys. Acta (1992) 1130:105-108 !$#title Cloning of the human activin receptor cDNA reveals high !1evolutionary conservation. !$#cross-references MUID:92182002; PMID:1311955 !$#accession S22345 !'##molecule_type mRNA !'##residues 1-513 ##label MATZ !'##cross-references EMBL:X63128; NID:g3928172; PIDN:CAA44839.1; !1PID:g28350 COMMENT This protein binds activin A. GENETICS !$#gene GDB:ACVR2 !'##cross-references GDB:132411 !$#map_position 11q13-11q13 CLASSIFICATION #superfamily activin receptor II; protein kinase homology KEYWORDS ATP; glycoprotein; phosphotransferase; receptor; serine/ !1threonine-specific protein kinase; transmembrane protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-513 #product activin receptor II #status predicted #label !8MAT\ !$20-138 #domain extracellular #status predicted #label EXT\ !$139-160 #domain transmembrane #status predicted #label TM1\ !$161-513 #domain intracellular #status predicted #label INT\ !$190-486 #domain protein kinase homology #label KIN\ !$199-206 #region protein kinase ATP-binding motif\ !$43,66 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$219 #active_site Lys #status predicted SUMMARY #length 513 #molecular-weight 57847 #checksum 205 SEQUENCE /// ENTRY A42635 #type complete TITLE activin receptor STK8 precursor - African clawed frog ALTERNATE_NAMES ActRIIB CONTAINS protein kinase STK8 (EC 2.7.1.-) ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 04-Mar-1993 #sequence_revision 19-Oct-1995 #text_change 13-Jun-1997 ACCESSIONS A42635; S21233 REFERENCE A42635 !$#authors Mathews, L.S.; Vale, W.W.; Kintner, C.R. !$#journal Science (1992) 255:1702-1705 !$#title Cloning of a second type of activin receptor and functional !1characterization in Xenopus embryos. !$#cross-references MUID:92205349; PMID:1313188 !$#accession A42635 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type mRNA !'##residues 1-510 ##label MATH !'##cross-references GB:M88594 !'##experimental_source embryo !'##note sequence extracted from NCBI backbone (NCBIP:93126) REFERENCE S21171 !$#authors Nishimatsu, S.; Oda, S.; Murakami, K.; Ueno, N. !$#journal FEBS Lett. (1992) 303:81-84 !$#title Multiple genes for Xenopus activin receptor expressed during !1early embryogenesis. !$#cross-references MUID:92275088; PMID:1317302 !$#accession S21233 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-510 ##label NIS CLASSIFICATION #superfamily activin receptor II; protein kinase homology KEYWORDS ATP; glycoprotein; phosphotransferase; receptor; serine/ !1threonine-specific protein kinase; transmembrane protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-510 #product activin receptor II #status predicted #label !8MAT\ !$20-135 #domain extracellular #status predicted #label EXT\ !$136-157 #domain transmembrane #status predicted #label TM1\ !$158-510 #domain intracellular #status predicted #label INT\ !$186-483 #domain protein kinase homology #label KIN\ !$195-202 #region protein kinase ATP-binding motif\ !$43,66 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$215 #active_site Lys #status predicted SUMMARY #length 510 #molecular-weight 57782 #checksum 8223 SEQUENCE /// ENTRY A56926 #type complete TITLE activin receptor II STK3 precursor - African clawed frog ALTERNATE_NAMES activin receptor 1 CONTAINS protein kinase STK3 (EC 2.7.1.-) ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 08-Sep-1995 #sequence_revision 19-Oct-1995 #text_change 11-Jun-1999 ACCESSIONS A56926; S21234 REFERENCE A56926 !$#authors Hemmati-Brivanlou, A.; Wright, D.A.; Melton, D.A. !$#journal Dev. Dyn. (1992) 194:1-11 !$#title Embryonic expression and functional analysis of a Xenopus !1activin receptor. !$#cross-references MUID:93043515; PMID:1384808 !$#accession A56926 !'##molecule_type mRNA !'##residues 1-510 ##label HEM !'##cross-references GB:S49438; NID:g260043; PIDN:AAB24192.1; !1PID:g260044 !'##experimental_source oocytes !'##note sequence extracted from NCBI backbone (NCBIN:118655, !1NCBIP:118656) REFERENCE S21171 !$#authors Nishimatsu, S.; Oda, S.; Murakami, K.; Ueno, N. !$#journal FEBS Lett. (1992) 303:81-84 !$#title Multiple genes for Xenopus activin receptor expressed during !1early embryogenesis. !$#cross-references MUID:92275088; PMID:1317302 !$#accession S21234 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type mRNA !'##residues 1-216,'F',218-478,'I',480-510 ##label NIS !'##experimental_source stage 5-6 embryos FUNCTION !$#description receptor for activin, which induces mesoderm formation in !1embryogenesis and may play a role in neurogenesis at a later !1stage CLASSIFICATION #superfamily activin receptor II; protein kinase homology KEYWORDS ATP; glycoprotein; phosphotransferase; receptor; serine/ !1threonine-specific protein kinase; transmembrane protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-510 #product activin receptor II #status predicted #label !8MAT\ !$20-135 #domain extracellular #status predicted #label EXT\ !$136-157 #domain transmembrane #status predicted #label TMM\ !$158-510 #domain intracellular #status predicted #label INT\ !$186-483 #domain protein kinase homology #label KIN\ !$195-202 #region protein kinase ATP-binding motif\ !$43,66 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$215 #active_site Lys #status predicted SUMMARY #length 510 #molecular-weight 57780 #checksum 9403 SEQUENCE /// ENTRY TVHUFG #type complete TITLE fibroblast growth factor receptor 1 precursor - human ALTERNATE_NAMES basic fibroblast growth factor receptor; heparin-binding growth factor receptor (HBGFR) alpha-a1 CONTAINS HBGFR 3; HBGFR alpha b1; HBGFR beta a1; HBGFR beta b1; HBGFR gamma a1; HBGFR gamma b1; protein-tyrosine kinase (EC 2.7.1.112) flg ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1989 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS S11692; B40862; S09226; A61533; A61536; S26739; S26738; !1S17374; S17375; S17377; S17376; A35479; A36464; B36464; !1E36464; A28361; S25420; PC2394 REFERENCE S11691 !$#authors Dionne, C.A.; Crumley, G.; Bellot, F.; Kaplow, J.M.; !1Searfoss, G.; Ruta, M.; Burgess, W.H.; Jaye, M.; !1Schlessinger, J. !$#journal EMBO J. (1990) 9:2685-2692 !$#title Cloning and expression of two distinct high-affinity !1receptors cross-reacting with acidic and basic fibroblast !1growth factors. !$#cross-references MUID:90360977; PMID:1697263 !$#accession S11692 !'##molecule_type mRNA !'##residues 1-822 ##label DIO !'##cross-references EMBL:X52833; NID:g31377; PIDN:CAA37015.1; !1PID:g31378 REFERENCE A40862 !$#authors Hou, J.; Kan, M.; McKeehan, K.; McBride, G.; Adams, P.; !1McKeehan, W.L. !$#journal Science (1991) 251:665-668 !$#title Fibroblast growth factor receptors from liver vary in three !1structural domains. !$#cross-references MUID:91126480; PMID:1846977 !$#accession B40862 !'##molecule_type mRNA !'##residues 1-822 ##label HOU !'##cross-references GB:M63887 !'##note potentially twelve variants may arise by alternative splicing !1in liver cells REFERENCE S09226 !$#authors Isacchi, A.; Bergonzoni, L.; Sarmientos, P. !$#journal Nucleic Acids Res. (1990) 18:1906 !$#title Complete sequence of a human receptor for acidic and basic !1fibroblast growth factors. !$#cross-references MUID:90245600; PMID:2159626 !$#accession S09226 !'##molecule_type mRNA !'##residues 1-816,'R',818-822 ##label ISA !'##cross-references EMBL:X51803; NID:g31367; PIDN:CAA36101.1; !1PID:g31368 REFERENCE A61533 !$#authors Wennstroem, S.; Sandstroem, C.; Claesson-Welsh, L. !$#journal Growth Factors (1991) 4:197-208 !$#title cDNA cloning and expression of a human FGF receptor which !1binds acidic and basic FGF. !$#cross-references MUID:92118394; PMID:1722683 !$#accession A61533 !'##molecule_type mRNA !'##residues 1-147,150-193,'S',195-822 ##label WEN !'##cross-references GB:M34641; NID:g182529; PIDN:AAA35835.1; !1PID:g182530 !'##experimental_source teracarcinoma cell line Tera-2 REFERENCE A61536 !$#authors Kiefer, M.C.; Baird, A.; Nguyen, T.; George-Nascimento, !1C.G.; Mason, O.B.; Boley, L.J.; Valenzuela, P.; Barr, P.J. !$#journal Growth Factors (1991) 5:115-127 !$#title Molecular cloning of a human basic fibroblast growth factor !1receptor cDNA and expression of a biologically active !1extracellular domain in a baculovirus system. !$#cross-references MUID:92118399; PMID:1662973 !$#accession A61536 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-147,150-822 ##label KIE REFERENCE S19167 !$#authors Tronick, S.R. !$#submission submitted to the EMBL Data Library, January 1991 !$#accession S26739 !'##status preliminary !'##molecule_type mRNA !'##residues 1-822 ##label TR1 !'##cross-references EMBL:X57121; NID:g31392; PIDN:CAA40403.1; !1PID:g31393 !$#accession S26738 !'##molecule_type mRNA !'##residues 1-147,150-822 ##label TR2 !'##cross-references EMBL:X57120; NID:g31390; PIDN:CAA40402.1; !1PID:g31391 REFERENCE S17373 !$#authors Eisemann, A.; Ahn, J.A.; Graziani, G.; Tronick, S.R.; Ron, !1D. !$#journal Oncogene (1991) 6:1195-1202 !$#title Alternative splicing generates at least five different !1isoforms of the human basic-FGF receptor. !$#cross-references MUID:91319400; PMID:1650441 !$#accession S17374 !'##molecule_type mRNA !'##residues 1-30,120-147,150-822 ##label EI4 !'##cross-references EMBL:X57122; NID:g31386; PIDN:CAA40404.1; !1PID:g31387 !'##note the sequence from Fig. 3 is inconsistent with that from Fig. 1 !1in lacking 25-Pro !'##note this form is designated isoform I !$#accession S17375 !'##molecule_type mRNA !'##residues 1-30,120-822 ##label EI3 !'##cross-references EMBL:X57119; NID:g31388; PIDN:CAA40401.1; !1PID:g31389 !'##note the sequence from Fig. 3 is inconsistent with that from Fig. 1 !1in lacking 25-Pro; nucleotide sequence not complete !'##note this form is designated isoform II !$#accession S17377 !'##molecule_type mRNA !'##residues 1-90,'D',91-822 ##label EI2 !'##cross-references EMBL:X57121 !'##note the sequence from Fig. 3 is inconsistent with that from Fig. 1 !1in lacking 25-Pro; nucleotide sequence not complete !'##note this form is designated isoform III !$#accession S17376 !'##molecule_type mRNA !'##residues 1-90,'D',91-147,150-822 ##label EIS !'##cross-references EMBL:X57120 !'##note this form is designated isoform IV REFERENCE A35479 !$#authors Itoh, N.; Terachi, T.; Ohta, M.; Seo, M.K. !$#journal Biochem. Biophys. Res. Commun. (1990) 169:680-685 !$#title The complete amino acid sequence of the shorter form of !1human basic fibroblast growth factor receptor deduced from !1its cDNA. !$#cross-references MUID:90290512; PMID:2162671 !$#accession A35479 !'##molecule_type mRNA !'##residues 1-30,120-147,150-468,'L',470-822 ##label ITO !'##cross-references GB:M37722; NID:g179413; PIDN:AAA75007.1; !1PID:g179415 !'##note both the longer and shorter forms are expressed in the placenta REFERENCE A36464 !$#authors Johnson, D.E.; Lee, P.L.; Lu, J.; Williams, L.T. !$#journal Mol. Cell. Biol. (1990) 10:4728-4736 !$#title Diverse forms of a receptor for acidic and basic fibroblast !1growth factors. !$#cross-references MUID:90355989; PMID:2167437 !$#accession A36464 !'##molecule_type mRNA !'##residues 1-30,120-822 ##label JOH !'##cross-references GB:M34185; NID:g182531; PIDN:AAA35836.1; !1PID:g182532 !$#accession B36464 !'##molecule_type mRNA !'##residues 1-30,120-147,150-191,'E',193-822 ##label JO2 !'##cross-references GB:M34186; NID:g182533; PIDN:AAA35837.1; !1PID:g182534 !$#accession E36464 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 71-132 ##label JO3 REFERENCE A28361 !$#authors Ruta, M.; Howk, R.; Ricca, G.; Drohan, W.; Zabelshansky, M.; !1Laureys, G.; Barton, D.E.; Francke, U.; Schlessinger, J.; !1Givol, D. !$#journal Oncogene (1988) 3:9-15 !$#title A novel protein tyrosine kinase gene whose expression is !1modulated during endothelial cell differentiation. !$#accession A28361 !'##molecule_type mRNA !'##residues 201-671,'IYLTGS',677-822 ##label RUT !'##cross-references EMBL:Y00665 REFERENCE S25420 !$#authors Hattori, Y.; Odagiri, H.; Katoh, O.; Sakamoto, H.; Morita, !1T.; Shimotohno, K.; Tobinai, K.; Sugimura, T.; Terada, M. !$#journal Cancer Res. (1992) 52:3367-3371 !$#title K-sam-related gene, N-sam, encodes fibroblast growth factor !1receptor and is expressed in T-lymphocytic tumors. !$#cross-references MUID:92282615; PMID:1317750 !$#accession S25420 !'##status preliminary !'##molecule_type mRNA !'##residues 1-822 ##label HAT !'##cross-references EMBL:X66945; NID:g35109; PIDN:CAA47375.1; !1PID:g35110 REFERENCE PC2394 !$#authors Rusnati, M.; Coltrini, D.; Caccia, P.; Dell'Era, P.; !1Zoppetti, G.; Oreste, P.; Valsasina, B.; Presta, M. !$#journal Biochem. Biophys. Res. Commun. (1994) 203:450-458 !$#title Distinct role of 2-O-, N-, and 6-O-sulfate groups of heparin !1in the formation of the ternary complex with basic !1fibroblast growth factor and soluble FGF receptor-1. !$#cross-references MUID:94354840; PMID:8074689 !$#accession PC2394 !'##molecule_type protein !'##residues 81-100 ##label RUS !'##experimental_source recombinant soluble form of extracellular domain !1after expression in E. coli !'##note this sequence represents the amino end of a 33K fragment !1protected from trypsin degradation by the presence of !1heparin COMMENT This receptor binds acidic and basic fibroblast growth !1factors with high affinity. GENETICS !$#gene GDB:FGFR1; FLT2 !'##cross-references GDB:119913; OMIM:136350 !$#map_position 8p11.2-8p11.1 CLASSIFICATION #superfamily basic fibroblast growth factor receptor 1; !1immunoglobulin homology; protein kinase homology KEYWORDS alternative splicing; ATP; autophosphorylation; duplication; !1glycoprotein; growth factor receptor; heparin binding; !1magnesium; phosphoprotein; phosphotransferase; transmembrane !1protein; tyrosine-specific protein kinase FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-822 #product fibroblast growth factor receptor 1, form !8alpha a1 #status predicted #label MAT\ !$22-427,430-822 #product fibroblast growth factor receptor 1, form !8alpha b1 #status predicted #label MAT4\ !$22-376 #domain extracellular #status predicted #label EXT\ !$22-147,150-822 #product fibroblast growth factor receptor 1, form 3 !8#status predicted #label MAT7\ !$22-30,120-822 #product fibroblast growth factor receptor 1, form !8beta a1 #status predicted #label MAT2\ !$22-30,120-427, !$430-822 #product fibroblast growth factor receptor 1, form !8beta b1 #status predicted #label MAT5\ !$126-133 #region acidic\ !$161-822 #product fibroblast growth factor receptor 1, form !8gamma a1 #status predicted #label MAT3\ !$161-427,430-822 #product fibroblast growth factor receptor 1, form !8gamma b1 #status predicted #label MAT6\ !$171-232 #domain immunoglobulin homology #label IMM\ !$377-397 #domain transmembrane #status predicted #label TMM\ !$398-822 #domain intracellular #status predicted #label INT\ !$476-761 #domain protein kinase homology #label KIN\ !$484-492 #region protein kinase ATP-binding motif\ !$55-101,178-230, !$277-341 #disulfide_bonds #status predicted\ !$77,117,227,240,264, !$296,317,330 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$514,531,623 #active_site Lys, Glu, Asp #status predicted\ !$628,641 #binding_site magnesium (Asn, Asp) #status predicted\ !$654 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 822 #molecular-weight 91867 #checksum 2246 SEQUENCE /// ENTRY TVMSFG #type complete TITLE fibroblast growth factor receptor 1 precursor - mouse ALTERNATE_NAMES basic fibroblast growth factor receptor CONTAINS protein-tyrosine kinase (EC 2.7.1.112) flg ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS A34849; B34849; S09953; A35794; A43025; PC2277 REFERENCE A34849 !$#authors Reid, H.H.; Wilks, A.F.; Bernard, O. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:1596-1600 !$#title Two forms of the basic fibroblast growth factor !1receptor-like mRNA are expressed in the developing mouse !1brain. !$#cross-references MUID:90160373; PMID:1689490 !$#accession A34849 !'##molecule_type mRNA !'##residues 1-822 ##label REI !'##cross-references GB:M28998; NID:g192164; PIDN:AAA37290.1; !1PID:g309116 !$#accession B34849 !'##molecule_type mRNA !'##residues 1-30,120-822 ##label RE2 !'##cross-references GB:M28998 !'##note the shorter form is expressed at higher levels in neuronal !1cells at early stages of development REFERENCE S09953 !$#authors Safran, A.; Avivi, A.; Orr-Urtereger, A.; Neufeld, G.; !1Lonai, P.; Givol, D.; Yarden, Y. !$#journal Oncogene (1990) 5:635-643 !$#title The murine flg gene encodes a receptor for fibroblast growth !1factor. !$#cross-references MUID:90265603; PMID:2161096 !$#accession S09953 !'##molecule_type mRNA !'##residues 1-147,150-255,'ILQ',259-439,'A',441-755,'R',757-822 ##label !1SAF !'##cross-references EMBL:X51893; NID:g50959; PIDN:CAA36175.1; !1PID:g50960 REFERENCE A35794 !$#authors Mansukhani, A.; Moscatelli, D.; Talarico, D.; Levytska, V.; !1Basilico, C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:4378-4382 !$#title A murine fibroblast growth factor (FGF) receptor expressed !1in CHO cells is activated by basic FGF and Kaposi FGF. !$#cross-references MUID:90272715; PMID:2161540 !$#accession A35794 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-30,120-228,'S',230-255,'ILQ',259-269,'A',271-543,'M', !1545-628,'LV',631-755,'R',757-764,'D',766-822 ##label MAN !'##cross-references GB:M33760 REFERENCE A43025 !$#authors Basilico, C. !$#submission submitted to GenBank, March 1990 !$#accession A43025 !'##molecule_type mRNA !'##residues 1-30,120-228,'S',230-255,'ILQ',259-269,'A',271-543,'M', !1545-755,'R',757-764,'D',766-822 ##label BAS !'##cross-references GB:M33760; NID:g193298; PIDN:AAA37622.1; !1PID:g309240 REFERENCE PC2277 !$#authors Harada, T.; Saito, H.; Kouhara, H.; Kurebayashi, S.; !1Kasayama, S.; Terakawa, N.; Kishimoto, T.; Sato, B. !$#journal Biochem. Biophys. Res. Commun. (1994) 205:1057-1063 !$#title Murine fibroblast growth factor receptor 1 gene generates !1multiple messenger RNAs containing two open reading frames !1via alternative splicing. !$#cross-references MUID:95100926; PMID:7802632 !$#accession PC2277 !'##molecule_type DNA !'##residues 1-15 ##label HAR !'##cross-references GB:S74765; NID:g833887; PIDN:AAB32845.1; !1PID:g833889 COMMENT This protein mediates the biological actions of !1heparin-binding growth factors. CLASSIFICATION #superfamily basic fibroblast growth factor receptor 1; !1immunoglobulin homology; protein kinase homology KEYWORDS alternative splicing; ATP; autophosphorylation; duplication; !1glycoprotein; growth factor receptor; magnesium; !1phosphoprotein; phosphotransferase; transmembrane protein; !1tyrosine-specific protein kinase FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-822 #product fibroblast growth factor receptor 1 #status !8predicted #label MAT\ !$22-376 #domain extracellular #status predicted #label EXT\ !$22-30,120-822 #product fibroblast growth factor receptor 1, short !8form #status predicted #label MAT2\ !$126-133 #region acidic\ !$171-232 #domain immunoglobulin homology #label IMM\ !$377-397 #domain transmembrane #status predicted #label TMM\ !$398-822 #domain intracellular #status predicted #label INT\ !$476-761 #domain protein kinase homology #label KIN\ !$484-492 #region protein kinase ATP-binding motif\ !$55-101,178-230, !$277-341 #disulfide_bonds #status predicted\ !$77,117,227,240,264, !$296,317,330 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$514,531,623 #active_site Lys, Glu, Asp #status predicted\ !$628,641 #binding_site magnesium (Asn, Asp) #status predicted\ !$654 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 822 #molecular-weight 91928 #checksum 2081 SEQUENCE /// ENTRY TVCHFG #type complete TITLE fibroblast growth factor receptor 1 precursor - chicken ALTERNATE_NAMES basic fibroblast growth factor receptor CONTAINS protein-tyrosine kinase (EC 2.7.1.112) cek1 ORGANISM #formal_name Gallus gallus #common_name chicken DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS A41345; A33908 REFERENCE A41345 !$#authors Lee, P.L.; Johnson, D.E.; Cousens, L.S.; Fried, V.A.; !1Williams, L.T. !$#journal Science (1989) 245:57-60 !$#title Purification and complementary DNA cloning of a receptor for !1basic fibroblast growth factor. !$#cross-references MUID:89298406; PMID:2544996 !$#accession A41345 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type mRNA !'##residues 1-819 ##label LEE !'##note part of the sequence was confirmed by protein sequencing REFERENCE A33908 !$#authors Pasquale, E.B.; Singer, S.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:5449-5453 !$#title Identification of a developmentally regulated !1protein-tyrosine kinase by using anti-phosphotyrosine !1antibodies to screen a cDNA expression library. !$#cross-references MUID:89315814; PMID:2473471 !$#accession A33908 !'##molecule_type mRNA !'##residues 1-89,'A',91-685,'M',687-819 ##label PAS !'##cross-references GB:M24637 !'##note this protein is expressed in embryonic tissues and, at low !1levels, in adult brain GENETICS !$#gene cek1 CLASSIFICATION #superfamily basic fibroblast growth factor receptor 1; !1immunoglobulin homology; protein kinase homology KEYWORDS ATP; autophosphorylation; duplication; glycoprotein; growth !1factor receptor; magnesium; phosphoprotein; !1phosphotransferase; transmembrane protein; tyrosine-specific !1protein kinase FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-819 #product fibroblast growth factor receptor 1 #status !8predicted #label MAT\ !$22-374 #domain extracellular #status predicted #label EXT\ !$125-132 #region acidic\ !$169-230 #domain immunoglobulin homology #label IMM\ !$375-395 #domain transmembrane #status predicted #label TMM\ !$396-819 #domain intracellular #status predicted #label INT\ !$474-759 #domain protein kinase homology #label KIN\ !$482-490 #region protein kinase ATP-binding motif\ !$54-100,176-228, !$275-339 #disulfide_bonds #status predicted\ !$76,116,225,238,262, !$294,315,328 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$512,529,621 #active_site Lys, Glu, Asp #status predicted\ !$626,639 #binding_site magnesium (Asn, Asp) #status predicted\ !$652 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 819 #molecular-weight 91661 #checksum 4234 SEQUENCE /// ENTRY A39752 #type complete TITLE fibroblast growth factor receptor A1 precursor - African clawed frog CONTAINS fibroblast growth factor receptor A1, short splice form; protein-tyrosine kinase (EC 2.7.1.112) ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 07-Feb-1992 #sequence_revision 19-Jan-1996 #text_change 16-Jul-1999 ACCESSIONS A39752; B39752 REFERENCE A39752 !$#authors Friesel, R.; Dawid, I.B. !$#journal Mol. Cell. Biol. (1991) 11:2481-2488 !$#title cDNA cloning and developmental expression of fibroblast !1growth factor receptors from Xenopus laevis. !$#cross-references MUID:91203867; PMID:1850097 !$#accession A39752 !'##molecule_type mRNA !'##residues 1-814 ##label FRI !'##cross-references GB:M55163; NID:g214893; PIDN:AAA49990.1; !1PID:g214894 !$#accession B39752 !'##molecule_type mRNA !'##residues 1-30,119-814 ##label FR2 !'##cross-references GB:M55163 CLASSIFICATION #superfamily basic fibroblast growth factor receptor 1; !1immunoglobulin homology; protein kinase homology KEYWORDS alternative splicing; ATP; autophosphorylation; duplication; !1glycoprotein; growth factor receptor; magnesium; !1phosphoprotein; phosphotransferase; transmembrane protein; !1tyrosine-specific protein kinase FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-814 #product fibroblast growth factor receptor A1, long !8splice form #status experimental #label MAT\ !$22-372 #domain extracellular #status predicted #label EXT\ !$22-30,119-814 #product fibroblast growth factor receptor A1, short !8splice form #status experimental #label ALT\ !$47-102 #domain immunoglobulin homology #label IM1\ !$125-132 #region acidic\ !$167-228 #domain immunoglobulin homology #label IM2\ !$266-339 #domain immunoglobulin homology #label IM3\ !$373-393 #domain transmembrane #status predicted #label TMM\ !$394-814 #domain intracellular #status predicted #label INT\ !$472-757 #domain protein kinase homology #label KIN\ !$480-488 #region protein kinase ATP-binding motif\ !$54-100,174-226, !$273-337 #disulfide_bonds #status predicted\ !$76,116,133,177,223, !$236,260,292,313,326 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$510,527,619 #active_site Lys, Glu, Asp #status predicted\ !$624,637 #binding_site magnesium (Asn, Asp) #status predicted\ !$650 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 814 #molecular-weight 90681 #checksum 64 SEQUENCE /// ENTRY A36477 #type complete TITLE fibroblast growth factor receptor A2 precursor - African clawed frog CONTAINS fibroblast growth factor receptor A2, short splice form; protein-tyrosine kinase (EC 2.7.1.112) ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 08-Mar-1991 #sequence_revision 19-Jan-1996 #text_change 16-Jul-1999 ACCESSIONS A36477; C39752 REFERENCE A36477 !$#authors Musci, T.J.; Amaya, E.; Kirschner, M.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:8365-8369 !$#title Regulation of the fibroblast growth factor receptor in early !1Xenopus embryos. !$#cross-references MUID:91045998; PMID:2172985 !$#accession A36477 !'##molecule_type mRNA !'##residues 1-812 ##label MUS !'##cross-references GB:U24491; GB:M37201; NID:g857677; PIDN:AAA86868.1; !1PID:g857678 !'##note 45-Arg, 49-Thr, 50-Val, and 64-Ser also found REFERENCE A39752 !$#authors Friesel, R.; Dawid, I.B. !$#journal Mol. Cell. Biol. (1991) 11:2481-2488 !$#title cDNA cloning and developmental expression of fibroblast !1growth factor receptors from Xenopus laevis. !$#cross-references MUID:91203867; PMID:1850097 !$#accession C39752 !'##molecule_type mRNA !'##residues 1-30,119-189,'G',191-418,'L',420-636,'R',638-788,'V', !1790-812 ##label FRI !'##cross-references GB:M62322; NID:g214899; PIDN:AAA49993.1; !1PID:g214900 CLASSIFICATION #superfamily basic fibroblast growth factor receptor 1; !1immunoglobulin homology; protein kinase homology KEYWORDS alternative splicing; ATP; autophosphorylation; duplication; !1glycoprotein; growth factor receptor; magnesium; !1phosphoprotein; phosphotransferase; transmembrane protein; !1tyrosine-specific protein kinase FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-812 #product fibroblast growth factor receptor A2, long !8splice form #status predicted #label MAT\ !$22-372 #domain extracellular #status predicted #label EXT\ !$22-30,119-812 #product fibroblast growth factor receptor A2, short !8splice form #status predicted #label ALT\ !$47-102 #domain immunoglobulin homology #label IM1\ !$125-132 #region acidic\ !$167-228 #domain immunoglobulin homology #label IM2\ !$266-339 #domain immunoglobulin homology #label IM3\ !$373-393 #domain transmembrane #status predicted #label TMM\ !$394-812 #domain intracellular #status predicted #label INT\ !$470-755 #domain protein kinase homology #label KIN\ !$478-486 #region protein kinase ATP-binding motif\ !$54-100,174-226, !$273-337 #disulfide_bonds #status predicted\ !$76,116,133,177,223, !$236,260,292,313,326 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$508,525,617 #active_site Lys, Glu, Asp #status predicted\ !$622,635 #binding_site magnesium (Asn, Asp) #status predicted\ !$648 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 812 #molecular-weight 90502 #checksum 7510 SEQUENCE /// ENTRY TVMSBK #type complete TITLE fibroblast growth factor receptor bek precursor - mouse ALTERNATE_NAMES bek transforming protein; fibroblast growth factor receptor 2; keratinocyte growth factor receptor CONTAINS protein-tyrosine kinase (EC 2.7.1.112) bek ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Jun-1991 #sequence_revision 13-Mar-1997 #text_change 16-Jul-1999 ACCESSIONS A44142; A31378 REFERENCE A44142 !$#authors Mansukhani, A.; Dell'Era, P.; Moscatelli, D.; Kornbluth, S.; !1Hanafusa, H.; Basilico, C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:3305-3309 !$#title Characterization of the murine BEK fibroblast growth factor !1(FGF) receptor: activation by three members of the FGF !1family and requirement for heparin. !$#cross-references MUID:92228773; PMID:1373495 !$#accession A44142 !'##status preliminary; nucleic acid sequence not shown; not compared !1with conceptual translation !'##molecule_type mRNA !'##residues 1-821 ##label MAN !'##cross-references GB:M86441 REFERENCE A31378 !$#authors Kornbluth, S.; Paulson, K.E.; Hanafusa, H. !$#journal Mol. Cell. Biol. (1988) 8:5541-5544 !$#title Novel tyrosine kinase identified by phosphotyrosine antibody !1screening of cDNA libraries. !$#cross-references MUID:89219016; PMID:2468999 !$#accession A31378 !'##molecule_type mRNA !'##residues 477-821 ##label KOR !'##cross-references GB:M23362; NID:g533219; PIDN:AAA37285.1; !1PID:g533220 GENETICS !$#gene bek CLASSIFICATION #superfamily basic fibroblast growth factor receptor 1; !1immunoglobulin homology; protein kinase homology KEYWORDS ATP; autophosphorylation; duplication; glycoprotein; growth !1factor receptor; magnesium; phosphoprotein; !1phosphotransferase; transmembrane protein; tyrosine-specific !1protein kinase FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-821 #product fibroblast growth factor receptor bek !8#status predicted #label MAT\ !$172-233 #domain immunoglobulin homology #label IMM\ !$378-398 #domain transmembrane #status predicted #label TMM\ !$479-764 #domain protein kinase homology #label KIN\ !$487-495 #region protein kinase ATP-binding motif\ !$62-107,179-231, !$278-342 #disulfide_bonds #status predicted\ !$83,123,147,241,265, !$297,318,331 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$517,534,626 #active_site Lys, Glu, Asp #status predicted\ !$657 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 821 #molecular-weight 92032 #checksum 6746 SEQUENCE /// ENTRY TVHUF2 #type complete TITLE fibroblast growth factor receptor 2 precursor - human ALTERNATE_NAMES fibroblast growth factor receptor K-sam CONTAINS protein-tyrosine kinase (EC 2.7.1.112) bek; receptor-like protein-tyrosine kinase TK14 ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1993 #sequence_revision 19-Jan-1996 #text_change 16-Jul-1999 ACCESSIONS A42691; B42691; S11691; A36210; B44775; D44775 REFERENCE A42691 !$#authors Katoh, M.; Hattori, Y.; Sasaki, H.; Tanaka, M.; Sugano, K.; !1Yazaki, Y.; Sugimura, T.; Terada, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:2960-2964 !$#title K-sam gene encodes secreted as well as transmembrane !1receptor tyrosine kinase. !$#cross-references MUID:92212948; PMID:1313574 !$#accession A42691 !'##molecule_type mRNA !'##residues 1-821 ##label KAT !'##cross-references GB:M87770; NID:g186779; PIDN:AAA59470.1; !1PID:g186780 !$#accession B42691 !'##molecule_type mRNA !'##residues 1-313,430-821 ##label KA2 !'##cross-references GB:M87771; NID:g186781; PIDN:AAA59471.1; !1PID:g186782 REFERENCE S11691 !$#authors Dionne, C.A.; Crumley, G.; Bellot, F.; Kaplow, J.M.; !1Searfoss, G.; Ruta, M.; Burgess, W.H.; Jaye, M.; !1Schlessinger, J. !$#journal EMBO J. (1990) 9:2685-2692 !$#title Cloning and expression of two distinct high-affinity !1receptors cross-reacting with acidic and basic fibroblast !1growth factors. !$#cross-references MUID:90360977; PMID:1697263 !$#accession S11691 !'##molecule_type mRNA !'##residues 1-821 ##label DIO !'##cross-references EMBL:X52832; NID:g31373; PIDN:CAA37014.1; !1PID:g31374 REFERENCE A36210 !$#authors Houssaint, E.; Blanquet, P.R.; Champion-Arnaud, P.; Gesnel, !1M.C.; Torriglia, A.; Courtois, Y.; Breathnach, R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:8180-8184 !$#title Related fibroblast growth factor receptor genes exist in the !1human genome. !$#cross-references MUID:91045961; PMID:2172978 !$#accession A36210 !'##molecule_type mRNA !'##residues 1-313,'VLK',314-428,431-821 ##label HOU !'##cross-references GB:M55614; GB:M37715; NID:g339710; PIDN:AAA61188.1; !1PID:g339711 REFERENCE A44775 !$#authors Champion-Arnaud, P.; Ronsin, C.; Gilbert, E.; Gesnel, M.C.; !1Houssaint, E.; Breathnach, R. !$#journal Oncogene (1991) 6:979-987 !$#title Multiple mRNAs code for proteins related to the BEK !1fibroblast growth factor receptor. !$#cross-references MUID:91296403; PMID:1648704 !$#accession B44775 !'##molecule_type DNA !'##residues 263-361 ##label CH2 !'##cross-references GB:S40858; NID:g232799; PIDN:AAB19320.1; !1PID:g232800 !$#accession D44775 !'##molecule_type DNA !'##residues 759-821 ##label CHA !'##cross-references GB:S41873 COMMENT This receptor binds basic fibroblast growth factor and, with !1lower affinity, acidic fibroblast growth factor. An !1alternatively spliced product binds keratinocyte growth !1factor. GENETICS !$#gene GDB:FGFR2 !'##cross-references GDB:127273; OMIM:176943 !$#map_position 10q25.3-10q26 CLASSIFICATION #superfamily basic fibroblast growth factor receptor 1; !1immunoglobulin homology; protein kinase homology KEYWORDS alternative splicing; ATP; autophosphorylation; duplication; !1glycoprotein; growth factor receptor; magnesium; !1phosphoprotein; phosphotransferase; transmembrane protein; !1tyrosine-specific protein kinase FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-821 #product fibroblast growth factor receptor 2 #status !8predicted #label MAT\ !$22-377 #domain extracellular #status predicted #label EXT\ !$132-138 #region acidic\ !$172-233 #domain immunoglobulin homology #label IMM\ !$378-398 #domain transmembrane #status predicted #label TMM\ !$399-821 #domain intracellular #status predicted #label INT\ !$479-764 #domain protein kinase homology #label KIN\ !$487-495 #region protein kinase ATP-binding motif\ !$62-107,179-231, !$278-342 #disulfide_bonds #status predicted\ !$83,123,228,241,265, !$297,318,331 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$517,534,626 #active_site Lys, Glu, Asp #status predicted\ !$631,644 #binding_site magnesium (Asn, Asp) #status predicted\ !$657 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 821 #molecular-weight 92024 #checksum 6308 SEQUENCE /// ENTRY A49123 #type complete TITLE fibroblast growth factor receptor 2 precursor - African clawed frog CONTAINS protein-tyrosine kinase (EC 2.7.1.112) ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 21-Jan-1994 #sequence_revision 27-Oct-1995 #text_change 16-Jul-1999 ACCESSIONS A49123; S25060 REFERENCE A49123 !$#authors Friesel, R.; Brown, S.A. !$#journal Development (1992) 116:1051-1058 !$#title Spatially restricted expression of fibroblast growth factor !1receptor-2 during Xenopus development. !$#cross-references MUID:93201992; PMID:1284237 !$#accession A49123 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type mRNA !'##residues 1-813 ##label FRI !'##cross-references EMBL:X65943 !'##note sequence extracted from NCBI backbone (NCBIP:128003) REFERENCE S25060 !$#authors Brown, S.N.; Friesel, R.E. !$#submission submitted to the EMBL Data Library, May 1992 !$#description Xenopus fibroblast growth factor receptor-2: cloning, !1expression and developmental regulation. !$#accession S25060 !'##molecule_type mRNA !'##residues 1-632,'A',634-813 ##label BRO !'##cross-references EMBL:X65943; NID:g64694; PIDN:CAA46758.1; !1PID:g64695 FUNCTION !$#description receptor mediating fibroblast growth factor roles in !1patterning of developing central nervous system !$#note expressed from embryonic stage 11 through tadpole stages CLASSIFICATION #superfamily basic fibroblast growth factor receptor 1; !1immunoglobulin homology; protein kinase homology KEYWORDS ATP; autophosphorylation; duplication; embryo; glycoprotein; !1growth factor receptor; magnesium; phosphoprotein; !1phosphotransferase; transmembrane protein; tyrosine-specific !1protein kinase FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-813 #product fibroblast growth factor receptor 2 #status !8predicted #label MAT\ !$18-367 #domain extracellular #status predicted #label EXT\ !$124-130 #region acidic\ !$163-223 #domain immunoglobulin homology #label IMM\ !$368-388 #domain transmembrane #status predicted #label TMM\ !$389-813 #domain intracellular #status predicted #label INT\ !$469-754 #domain protein kinase homology #label KIN\ !$477-485 #region protein kinase ATP-binding motif\ !$58-103,170-221, !$268-332 #disulfide_bonds #status predicted\ !$79,115,231,255,287, !$308,321 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$507,524,616 #active_site Lys, Glu, Asp #status predicted\ !$621,634 #binding_site magnesium (Asn, Asp) #status predicted\ !$647 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 813 #molecular-weight 91425 #checksum 5359 SEQUENCE /// ENTRY TVHUF3 #type complete TITLE fibroblast growth factor receptor 3 precursor - human CONTAINS protein-tyrosine kinase (EC 2.7.1.112) ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS A38576; A55273; E38269; I51880 REFERENCE A38576 !$#authors Keegan, K.; Johnson, D.E.; Williams, L.T.; Hayman, M.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:1095-1099 !$#title Isolation of an additional member of the fibroblast growth !1factor receptor family, FGFR-3. !$#cross-references MUID:91142118; PMID:1847508 !$#accession A38576 !'##molecule_type mRNA !'##residues 1-806 ##label KEE !'##cross-references GB:M58051; NID:g182568; PIDN:AAA52450.1; !1PID:g182569 REFERENCE A55273 !$#authors Thompson, L.M.; Plummer, S.; Schalling, M.; Altherr, M.R.; !1Gusella, J.F.; Housman, D.E.; Wasmuth, J.J. !$#journal Genomics (1991) 11:1133-1142 !$#title A gene encoding a fibroblast growth factor receptor isolated !1from the Huntington disease gene region of human chromosome !14. !$#cross-references MUID:92147110; PMID:1664411 !$#accession A55273 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 76-394,'V',396-806 ##label THO !'##cross-references GB:M64347; NID:g182564; PIDN:AAA58470.1; !1PID:g182565 !'##note sequence extracted from NCBI backbone (NCBIP:80296) REFERENCE A38268 !$#authors Partanen, J.; Maekelae, T.P.; Alitalo, R.; Lehvaeslaiho, H.; !1Alitalo, K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:8913-8917 !$#title Putative tyrosine kinases expressed in K-562 human leukemia !1cells. !$#cross-references MUID:91062389; PMID:2247464 !$#accession E38269 !'##molecule_type mRNA !'##residues 619-675 ##label PAR !'##cross-references GB:M37782 REFERENCE I51880 !$#authors Bellus, G.A.; Hefferon, T.W.; Ortiz de Luna, R.I.; Hecht, !1J.T.; Horton, W.A.; Machado, M.; Kaitila, I.; McIntosh, I.; !1Francomano, C.A. !$#journal Am. J. Hum. Genet. (1995) 56:368-373 !$#title Achondroplasia is defined by recurrent G380R mutations of !1FGFR3. !$#cross-references MUID:95150025; PMID:7847369 !$#accession I51880 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 361-379,'R',381-415 ##label RES !'##cross-references GB:S76733; NID:g914201; PIDN:AAB33323.1; !1PID:g914202 !'##note this sequence represents a mutant form associated with !1achondroplasia GENETICS !$#gene GDB:FGFR3 !'##cross-references GDB:127526; OMIM:100800; OMIM:134934 !$#map_position 4p16.3-4p16.3 FUNCTION !$#description receptor for both acidic and basic fibroblast growth factors CLASSIFICATION #superfamily basic fibroblast growth factor receptor 1; !1immunoglobulin homology; protein kinase homology KEYWORDS ATP; autophosphorylation; duplication; glycoprotein; growth !1factor receptor; magnesium; phosphoprotein; !1phosphotransferase; transmembrane protein; tyrosine-specific !1protein kinase FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-806 #product fibroblast growth factor receptor 3 #status !8predicted #label MAT\ !$23-375 #domain extracellular #status predicted #label EXT\ !$133-139 #region acidic\ !$268-341 #domain immunoglobulin homology #label IMM\ !$376-396 #domain transmembrane #status predicted #label TMM\ !$397-806 #domain intracellular #status predicted #label INT\ !$470-755 #domain protein kinase homology #label KIN\ !$478-486 #region protein kinase ATP-binding motif\ !$61-109,176-228, !$275-339 #disulfide_bonds #status predicted\ !$98,225,262,294,315, !$328 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$508,525,617 #active_site Lys, Glu, Asp #status predicted\ !$622,635 #binding_site magnesium (Asn, Asp) #status predicted\ !$648 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 806 #molecular-weight 87709 #checksum 8278 SEQUENCE /// ENTRY TVHU2F #type complete TITLE fibroblast growth factor receptor flg-2 precursor - human CONTAINS protein-tyrosine kinase (EC 2.7.1.112) flg-2 ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jun-2000 ACCESSIONS A60350; S21843 REFERENCE A60350 !$#authors Avivi, A.; Zimmer, Y.; Yayon, A.; Yarden, Y.; Givol, D. !$#journal Oncogene (1991) 6:1089-1092 !$#title Flg-2, a new member of the family of fibroblast growth !1factor receptors. !$#cross-references MUID:91296390; PMID:1648703 !$#accession A60350 !'##molecule_type mRNA !'##residues 1-800 ##label AVI !'##cross-references EMBL:X58255; NID:g31382; PIDN:CAA41209.1; !1PID:g31383 !'##experimental_source keratinocytes COMMENT This may be a receptor for keratinocyte growth factor. GENETICS !$#gene GDB:FGFR2; JWS; CFD1; KGF; FLG2 !'##cross-references GDB:127273; OMIM:176943 !$#map_position 10q25.3-10q26 CLASSIFICATION #superfamily basic fibroblast growth factor receptor 1; !1immunoglobulin homology; protein kinase homology KEYWORDS ATP; autophosphorylation; duplication; glycoprotein; growth !1factor receptor; magnesium; phosphoprotein; !1phosphotransferase; transmembrane protein; tyrosine-specific !1protein kinase FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-800 #product fibroblast growth factor receptor flg-2 !8#status predicted #label MAT\ !$22-369 #domain extracellular #status predicted #label EXT\ !$131-137 #region acidic\ !$262-335 #domain immunoglobulin homology #label IMM\ !$370-390 #domain transmembrane #status predicted #label TMM\ !$391-800 #domain intracellular #status predicted #label INT\ !$464-749 #domain protein kinase homology #label KIN\ !$472-480 #region protein kinase ATP-binding motif\ !$59-107,170-222, !$269-333 #disulfide_bonds #status predicted\ !$96,219,256,288,309, !$322 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$502,519,611 #active_site Lys, Glu, Asp #status predicted\ !$616,629 #binding_site magnesium (Asn, Asp) #status predicted\ !$642 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 800 #molecular-weight 87691 #checksum 14 SEQUENCE /// ENTRY TVHUF4 #type complete TITLE fibroblast growth factor receptor 4 precursor - human ALTERNATE_NAMES protein-tyrosine kinase tkf CONTAINS protein-tyrosine kinase (EC 2.7.1.112) ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS S15345; A46615; A41598; D38269 REFERENCE S15345 !$#authors Partanen, J.; Maekelae, T.P.; Eerola, E.; Korhonen, J.; !1Hirvonen, H.; Claesson-Welsh, L.; Alitalo, K. !$#journal EMBO J. (1991) 10:1347-1354 !$#title FGFR-4, a novel acidic fibroblast growth factor receptor !1with a distinct expression pattern. !$#cross-references MUID:91224085; PMID:1709094 !$#accession S15345 !'##molecule_type mRNA !'##residues 1-802 ##label PAR !'##cross-references EMBL:X57205; NID:g31371; PIDN:CAA40490.1; !1PID:g31372 !'##note binds acidic but not basic fibroblast growth factor with high !1affinity REFERENCE A46615 !$#authors Ron, D.; Reich, R.; Chedid, M.; Lengel, C.; Cohen, O.E.; !1Chan, A.M.; Neufeld, G.; Miki, T.; Tronick, S.R. !$#journal J. Biol. Chem. (1993) 268:5388-5394 !$#title Fibroblast growth factor receptor 4 is a high affinity !1receptor for both acidic and basic fibroblast growth factor !1but not for keratinocyte growth factor. !$#cross-references MUID:93194827; PMID:7680645 !$#accession A46615 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type mRNA !'##residues 1-296,'D',298-802 ##label RON !'##experimental_source mammary epithelial cell line B5/589 !'##note sequence extracted from NCBI backbone (NCBIP:127650) !'##note binds acidic and basic fibroblast growth factors with high !1affinity REFERENCE S19025 !$#authors Holtrich, U.; Braeuninger, A.; Strebhardt, K.; !1Ruebsamen-Waigmann, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:10411-10415 !$#title Two additional protein-tyrosine kinases expressed in human !1lung: fourth member of the fibroblast growth factor receptor !1family and an intracellular protein-tyrosine kinase. !$#cross-references MUID:92073297; PMID:1720539 !$#accession A41598 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type mRNA !'##residues 399-534,'M',536-799,'SG',800-802 ##label HOL !'##experimental_source lung REFERENCE A38268 !$#authors Partanen, J.; Maekelae, T.P.; Alitalo, R.; Lehvaeslaiho, H.; !1Alitalo, K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:8913-8917 !$#title Putative tyrosine kinases expressed in K-562 human leukemia !1cells. !$#cross-references MUID:91062389; PMID:2247464 !$#accession D38269 !'##molecule_type mRNA !'##residues 614-670 ##label PA2 !'##cross-references GB:M37781 !'##experimental_source K-562 leukemia cell line GENETICS !$#gene GDB:FGFR4 !'##cross-references GDB:127929; OMIM:134935 !$#map_position 5q33.2-5qter FUNCTION !$#description receptor mediating effects of fibroblast growth factor !$#note expressed in normal lung; expressed in some carcinomas CLASSIFICATION #superfamily basic fibroblast growth factor receptor 1; !1immunoglobulin homology; protein kinase homology KEYWORDS ATP; autophosphorylation; duplication; glycoprotein; growth !1factor receptor; magnesium; phosphoprotein; !1phosphotransferase; transmembrane protein; tyrosine-specific !1protein kinase FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-802 #product fibroblast growth factor receptor 4 #status !8predicted #label MAT\ !$25-369 #domain extracellular #status predicted #label EXT\ !$50-103 #domain immunoglobulin homology #label IM1\ !$165-226 #domain immunoglobulin homology #label IM2\ !$264-335 #domain immunoglobulin homology #label IM3\ !$370-390 #domain transmembrane #status predicted #label TMM\ !$391-802 #domain intracellular #status predicted #label INT\ !$465-750 #domain protein kinase homology #label KIN\ !$473-481 #region protein kinase ATP-binding motif\ !$57-101,172-224, !$271-333 #disulfide_bonds #status predicted\ !$112,258,290,311,322 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$503,520,612 #active_site Lys, Glu, Asp #status predicted\ !$617,630 #binding_site magnesium (Asn, Asp) #status predicted\ !$643 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 802 #molecular-weight 87938 #checksum 2185 SEQUENCE /// ENTRY JC1450 #type complete TITLE fibroblast growth factor receptor 4 - rat CONTAINS protein-tyrosine kinase (EC 2.7.1.112) ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 01-Dec-2000 ACCESSIONS JC1450; PT0191 REFERENCE JC1450 !$#authors Horlick, R.A.; Stack, S.L.; Cooke, G.M. !$#journal Gene (1992) 120:291-295 !$#title Cloning, expression and tissue distribution of the gene !1encoding rat fibroblast growth factor receptor subtype 4. !$#cross-references MUID:93013049; PMID:1398143 !$#accession JC1450 !'##molecule_type mRNA !'##residues 1-650 ##label HOR !'##cross-references GB:M91599; NID:g204137; PIDN:AAA41157.1; !1PID:g204138 REFERENCE PT0183 !$#authors Lai, C.; Lemke, G. !$#journal Neuron (1991) 6:691-704 !$#title An extended family of protein-tyrosine kinase genes !1differentially expressed in the vertebrate nervous system. !$#cross-references MUID:91222560; PMID:2025425 !$#accession PT0191 !'##molecule_type mRNA !'##residues 465-518 ##label LAI !'##experimental_source sciatic nerve GENETICS !$#gene FGFR4; tyro-9 FUNCTION !$#description receptor mediating effects of fibroblast growth factor !$#note expressed in normal lung; expressed in some carcinomas CLASSIFICATION #superfamily basic fibroblast growth factor receptor 1; !1immunoglobulin homology; protein kinase homology KEYWORDS ATP; autophosphorylation; duplication; glycoprotein; growth !1factor receptor; magnesium; phosphoprotein; !1phosphotransferase; transmembrane protein; tyrosine-specific !1protein kinase FEATURE !$11-72 #domain immunoglobulin homology #label IM1\ !$110-181 #domain immunoglobulin homology #label IM2\ !$218-238 #domain transmembrane #status predicted #label TMM\ !$239-650 #domain intracellular #status predicted #label INT\ !$313-598 #domain protein kinase homology #label KIN\ !$321-329 #region protein kinase ATP-binding motif\ !$104,136,157,168 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$351,368,460 #active_site Lys, Glu, Asp #status predicted\ !$465,478 #binding_site magnesium (Asn, Asp) #status predicted\ !$491 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 650 #molecular-weight 71858 #checksum 8548 SEQUENCE /// ENTRY A41527 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) axl precursor, major splice form - human ALTERNATE_NAMES transforming protein axl; UFO receptor ORGANISM #formal_name Homo sapiens #common_name man DATE 28-May-1992 #sequence_revision 05-Jan-1996 #text_change 04-Feb-2000 ACCESSIONS A41527; B41527; B38269; I39203; G02782 REFERENCE A41527 !$#authors O'Bryan, J.P.; Frye, R.A.; Cogswell, P.C.; Neubauer, A.; !1Kitch, B.; Prokop, C.; Espinosa III, R.; Le Beau, M.M.; !1Earp, H.S.; Liu, E.T. !$#journal Mol. Cell. Biol. (1991) 11:5016-5031 !$#title axl, a transforming gene isolated from primary human myeloid !1leukemia cells, encodes a novel receptor tyrosine kinase. !$#cross-references MUID:92017777; PMID:1656220 !$#accession A41527 !'##molecule_type mRNA !'##residues 1-894 ##label OAB !'##cross-references GB:M76125 !'##experimental_source axl(+) !$#accession B41527 !'##status preliminary !'##molecule_type mRNA !'##residues 1-337,'K',339-428,438-894 ##label OBR !'##cross-references GB:M76125; NID:g292869; PIDN:AAA61243.1; !1PID:g292870 !'##experimental_source axl(-) !'##note the authors translated the codon AAG for residue 338 as Leu REFERENCE A38268 !$#authors Partanen, J.; Maekelae, T.P.; Alitalo, R.; Lehvaeslaiho, H.; !1Alitalo, K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:8913-8917 !$#title Putative tyrosine kinases expressed in K-562 human leukemia !1cells. !$#cross-references MUID:91062389; PMID:2247464 !$#accession B38269 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type mRNA !'##residues 674-730 ##label PAR !'##cross-references GB:M59373; GB:M37781 REFERENCE I39203 !$#authors Schulz, A.S.; Schleithoff, L.; Faust, M.; Bartram, C.R.; !1Janssen, J.W. !$#journal Oncogene (1993) 8:509-513 !$#title The genomic structure of the human UFO receptor. !$#cross-references MUID:93149614; PMID:8381225 !$#accession I39203 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-28 ##label SCH !'##cross-references EMBL:X66030; NID:g37594; PIDN:CAA46829.1; !1PID:g37595 REFERENCE G09377 !$#authors Mitchell, P.J. !$#submission submitted to the EMBL Data Library, December 1990 !$#accession G02782 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-302,'P',304-429,'E',431-638,'G',640-894 ##label MIT !'##cross-references EMBL:X57019; NID:g37592; PIDN:CAA40338.1; !1PID:g37593 COMMENT This protein is overexpressed in chronic myelogenous !1leukemia and induces neoplastic transformation. GENETICS !$#gene GDB:AXL; UFO !'##cross-references GDB:133764; OMIM:109135 !$#map_position 19q13.1-19q13.1 FUNCTION !$#description catalyzes the phosphorylation of a peptidyl tyrosine residue !1by ATP CLASSIFICATION #superfamily protein-tyrosine kinase axl; fibronectin type !1III repeat homology; immunoglobulin homology; protein kinase !1homology KEYWORDS alternative splicing; ATP; autophosphorylation; duplication; !1glycoprotein; leukemia; magnesium; phosphoprotein; !1phosphotransferase; receptor; transforming protein; !1transmembrane protein; tyrosine-specific protein kinase FEATURE !$1-32 #domain signal sequence #status predicted #label SIG\ !$33-894 #product protein-tyrosine kinase axl, major splice !8form #status predicted #label MAJ\ !$49-119 #domain immunoglobulin homology #label IM1\ !$153-207 #domain immunoglobulin homology #label IM2\ !$224-320 #domain fibronectin type III repeat homology #label !8FN3A\ !$333-417 #domain fibronectin type III repeat homology #label !8FN3B\ !$448-472 #domain transmembrane #status predicted #label TMM\ !$534-810 #domain protein kinase homology #label KIN\ !$542-550 #region protein kinase ATP-binding motif\ !$43,157,198,339,345, !$401 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$567,585,672 #active_site Lys, Glu, Asp #status predicted\ !$677,690 #binding_site magnesium (Asn, Asp) #status predicted\ !$703 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted\ !$779,821 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 894 #molecular-weight 98336 #checksum 970 SEQUENCE /// ENTRY A53743 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) tyro3 precursor - human ALTERNATE_NAMES protein-tyrosine kinase sky; receptor-type tyrosine kinase rse ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A53743; JP0077; JC2145; S32765; S32219 REFERENCE A53743 !$#authors Mark, M.R.; Scadden, D.T.; Wang, Z.; Gu, Q.; Goddard, A.; !1Godowski, P.J. !$#journal J. Biol. Chem. (1994) 269:10720-10728 !$#title rse, a novel receptor-type tyrosine kinase with homology to !1Axl/Ufo, is expressed at high levels in the brain. !$#cross-references MUID:94193774; PMID:7511603 !$#accession A53743 !'##status preliminary !'##molecule_type mRNA !'##residues 1-890 ##label MAR !'##cross-references GB:U05682; NID:g463469; PIDN:AAA19236.1; !1PID:g463470 REFERENCE JP0077 !$#authors Ohashi, K.; Mizuno, K.; Kuma, K.; Miyata, T.; Nakamura, T. !$#journal Oncogene (1994) 9:699-705 !$#title Cloning of the cDNA for a novel receptor tyrosine kinase, !1Sky, predominantly expressed in brain. !$#cross-references MUID:94150991; PMID:8108112 !$#accession JP0077 !'##molecule_type mRNA !'##residues 1-890 ##label OHA !'##cross-references DDBJ:D17517; NID:g624880; PIDN:BAA04467.1; !1PID:g624881 !'##experimental_source hepatoma HepG2 cell REFERENCE JC2145 !$#authors Polvi, A.; Armstrong, E.; Lai, C.; Lemke, G.; Huebner, K.; !1Spritz, R.A.; Guida, L.C.; Nicholls, R.D.; Alitalo, K. !$#journal Gene (1993) 134:289-293 !$#title The human TYRO3 gene and pseudogene are located in !1chromosome 15q14-q25. !$#cross-references MUID:94085793; PMID:8262388 !$#accession JC2145 !'##molecule_type mRNA !'##residues 519-790 ##label POL !'##cross-references EMBL:X72886; NID:g296020; PIDN:CAA51396.1; !1PID:g312336 REFERENCE S32219 !$#authors Polvi, A.; Armstrong, E.; Lai, C.; Lemke, G.; Huebner, K.; !1Alitalo, K. !$#submission submitted to the EMBL Data Library, March 1993 !$#description Human Tyro3 gene and pseudogene in chromosome 15pter-q25. !$#accession S32765 !'##status preliminary !'##molecule_type mRNA !'##residues 519-790 ##label PO2 !'##cross-references EMBL:X72886; NID:g296020; PIDN:CAA51396.1; !1PID:g312336 GENETICS !$#gene GDB:TYRO3 !'##cross-references GDB:134764; OMIM:600341 !$#map_position 15q15.1-15q21.1 CLASSIFICATION #superfamily protein-tyrosine kinase axl; fibronectin type !1III repeat homology; immunoglobulin homology; protein kinase !1homology KEYWORDS ATP; brain; glycoprotein; growth factor receptor; !1phosphotransferase; transforming protein; transmembrane !1protein; tyrosine-specific protein kinase FEATURE !$1-41 #domain (or 7-41) signal sequence #status predicted !8#label SIG\ !$42-890 #product protein-tyrosine kinase tyro3 #status !8predicted #label MAT\ !$60-119 #domain immunoglobulin homology #label IMM1\ !$156-205 #domain immunoglobulin homology #label IMM2\ !$224-309 #domain fibronectin type III repeat homology #label !8FN3A\ !$322-405 #domain fibronectin type III repeat homology #label !8FN3B\ !$429-451 #domain transmembrane #status predicted #label TMM\ !$516-793 #domain protein kinase homology #label KIN\ !$524-532 #region protein kinase ATP-binding motif\ !$63,191,230,240,293, !$366,380 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 890 #molecular-weight 96904 #checksum 4777 SEQUENCE /// ENTRY JC4166 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) tyro3 precursor - rat ALTERNATE_NAMES protein-tyrosine kinase sky; receptor-type tyrosine kinase rse ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS JC4166; PT0185 REFERENCE JC4166 !$#authors Ohashi, K.; Honda, S.; Ichinomiya, N.; Nakamura, T.; Mizuno, !1K. !$#journal J. Biochem. (1995) 117:1267-1275 !$#title Molecular cloning and in situ localization in the brain of !1rat Sky receptor tyrosine kinase. !$#cross-references MUID:96104999; PMID:7490270 !$#accession JC4166 !'##molecule_type mRNA !'##residues 1-880 ##label OHA !'##cross-references DDBJ:D37880; NID:g1498195; PIDN:BAA07119.1; !1PID:g829057 !'##experimental_source brain !'##note It is uncertain whether Met-1 or Met-7 is the initiator REFERENCE PT0183 !$#authors Lai, C.; Lemke, G. !$#journal Neuron (1991) 6:691-704 !$#title An extended family of protein-tyrosine kinase genes !1differentially expressed in the vertebrate nervous system. !$#cross-references MUID:91222560; PMID:2025425 !$#accession PT0185 !'##molecule_type mRNA !'##residues 650-703 ##label LAI !'##experimental_source sciatic nerve COMMENT This receptor plays an important role in development, !1function, and maintenance of specific neuronal populations !1in the central nervous system. GENETICS !$#gene tyro-3 CLASSIFICATION #superfamily protein-tyrosine kinase axl; fibronectin type !1III repeat homology; immunoglobulin homology; protein kinase !1homology KEYWORDS ATP; glycoprotein; growth factor receptor; !1phosphotransferase; transforming protein; transmembrane !1protein; tyrosine-specific protein kinase FEATURE !$1-31 #domain (or 7-31) signal sequence #status predicted !8#label SIG\ !$32-880 #product (or 32-874) protein-tyrosine kinase tyro3 !8#status predicted #label MAT\ !$50-109 #domain immunoglobulin homology #label IMM1\ !$146-195 #domain immunoglobulin homology #label IMM2\ !$214-299 #domain fibronectin type III repeat homology #label !8FN3A\ !$312-395 #domain fibronectin type III repeat homology #label !8FN3B\ !$419-441 #domain transmembrane #status predicted #label TMM\ !$506-783 #domain protein kinase homology #label KIN\ !$514-522 #region protein kinase ATP-binding motif\ !$515-766 #domain cytoplasmic tyrosine kinase #status predicted !8#label CTK\ !$53,75,181,220,230, !$283,356,370 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 880 #molecular-weight 95918 #checksum 2454 SEQUENCE /// ENTRY A49714 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) c-eyk precursor - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 04-Feb-2000 ACCESSIONS A49714 REFERENCE A49714 !$#authors Jia, R.; Hanafusa, H. !$#journal J. Biol. Chem. (1994) 269:1839-1844 !$#title The proto-oncogene of v-eyk (v-ryk) is a novel receptor-type !1protein tyrosine kinase with extracellular Ig/FN-III !1domains. !$#cross-references MUID:94124527; PMID:7507487 !$#accession A49714 !'##status preliminary !'##molecule_type mRNA !'##residues 1-974 ##label JIA !'##cross-references GB:L21719; NID:g438522; PIDN:AAC38010.1; !1PID:g438523 CLASSIFICATION #superfamily protein-tyrosine kinase axl; fibronectin type !1III repeat homology; immunoglobulin homology; protein kinase !1homology KEYWORDS ATP; glycoprotein; phosphotransferase; transmembrane !1protein; tyrosine-specific protein kinase FEATURE !$201-254 #domain immunoglobulin homology #label IMM\ !$575-851 #domain protein kinase homology #label KIN\ !$583-591 #region protein kinase ATP-binding motif SUMMARY #length 974 #molecular-weight 106165 #checksum 5341 SEQUENCE /// ENTRY S24066 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112), receptor type tie precursor - human ORGANISM #formal_name Homo sapiens #common_name man DATE 19-Feb-1994 #sequence_revision 11-Aug-1995 #text_change 21-Jul-2000 ACCESSIONS S24066; C38269; I52613 REFERENCE S24066 !$#authors Partanen, J.; Armstrong, E.; Maekelae, T.P.; Korhonen, J.; !1Sandberg, M.; Renkonen, R.; Knuutila, S.; Huebner, K.; !1Alitalo, K. !$#journal Mol. Cell. Biol. (1992) 12:1698-1707 !$#title A novel endothelial cell surface receptor tyrosine kinase !1with extracellular epidermal growth factor homology domains. !$#cross-references MUID:92195316; PMID:1312667 !$#accession S24066 !'##molecule_type mRNA !'##residues 1-1138 ##label PAR !'##cross-references EMBL:X60957 REFERENCE A38268 !$#authors Partanen, J.; Maekelae, T.P.; Alitalo, R.; Lehvaeslaiho, H.; !1Alitalo, K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:8913-8917 !$#title Putative tyrosine kinases expressed in K-562 human leukemia !1cells. !$#cross-references MUID:91062389; PMID:2247464 !$#accession C38269 !'##status preliminary; nucleic acid sequence not shown; not compared !1with conceptual translation !'##molecule_type mRNA !'##residues 981-1034 ##label PAW !'##experimental_source clone JTK14 REFERENCE I52613 !$#authors Korhonen, J.; Lahtinen, I.; Halmekyto, M.; Alhonen, L.; !1Janne, J.; Dumont, D.; Alitalo, K. !$#journal Blood (1995) 86:1828-1835 !$#title Endothelial-specific gene expression directed by the tie !1gene promoter in vivo. !$#cross-references MUID:95383653; PMID:7655012 !$#accession I52613 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-19 ##label RES !'##cross-references GB:S79347; NID:g1086921; PIDN:AAD14299.1; !1PID:g4261999 GENETICS !$#gene GDB:TIE; JTK14 !'##cross-references GDB:212873; OMIM:600222 !$#map_position 1p34-1p33 FUNCTION !$#description catalyzes the phosphorylation of a peptidyl tyrosine residue !1by ATP CLASSIFICATION #superfamily protein-tyrosine kinase, receptor type tie; EGF !1homology; fibronectin type III repeat homology; !1immunoglobulin homology; protein kinase homology KEYWORDS ATP; autophosphorylation; duplication; glycoprotein; !1phosphoprotein; phosphotransferase; receptor; tandem repeat; !1transmembrane protein; tyrosine-specific protein kinase FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-1138 #product protein-tyrosine kinase, receptor-type tie !8#status predicted #label MAT\ !$36-107 #domain immunoglobulin homology #label IM1\ !$215-255 #domain EGF homology #label EG1\ !$259-302 #domain EGF homology #label EG2\ !$306-344 #domain EGF homology #label EG3\ !$365-428 #domain immunoglobulin homology #label IM2\ !$449-530 #domain fibronectin type III repeat homology #label !8FN3A\ !$542-633 #domain fibronectin type III repeat homology #label !8FN3B\ !$642-730 #domain fibronectin type III repeat homology #label !8FN3C\ !$761-786 #domain transmembrane #status predicted #label TMM\ !$837-1114 #domain protein kinase homology #label KIN\ !$845-853 #region protein kinase ATP-binding motif\ !$43-105,372-426 #disulfide_bonds #status predicted\ !$83,161,503,596,709 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$870,887,979 #active_site Lys, Glu, Asp #status predicted SUMMARY #length 1138 #molecular-weight 125055 #checksum 7149 SEQUENCE /// ENTRY S57845 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112), receptor type tie precursor - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 28-Oct-1995 #sequence_revision 03-Nov-1995 #text_change 16-Jul-1999 ACCESSIONS S57845; S32690 REFERENCE S57845 !$#authors Sato, T.N.; Qin, Y.; Kozak, C.A.; Audus, K.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:9355-9358 !$#title tie-1 and tie-2 define another class of putative receptor !1tyrosine kinase genes expressed in early embryonic vascular !1system. !$#cross-references MUID:94022374; PMID:8415706 !$#accession S57845 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type mRNA !'##residues 1-1136 ##label SAT !'##cross-references EMBL:X71423; NID:g296575; PIDN:CAA50554.1; !1PID:g296576 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1March 1993 CLASSIFICATION #superfamily protein-tyrosine kinase, receptor type tie; EGF !1homology; fibronectin type III repeat homology; !1immunoglobulin homology; protein kinase homology KEYWORDS ATP; autophosphorylation; duplication; glycoprotein; !1phosphoprotein; phosphotransferase; receptor; tandem repeat; !1transmembrane protein; tyrosine-specific protein kinase FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-1136 #product protein-tyrosine kinase, receptor type tie !8#status predicted #label MAT\ !$36-108 #domain immunoglobulin homology #label IM1\ !$213-253 #domain EGF homology #label EG1\ !$257-300 #domain EGF homology #label EG2\ !$304-342 #domain EGF homology #label EG3\ !$363-426 #domain immunoglobulin homology #label IM2\ !$447-528 #domain fibronectin type III repeat homology #label !8FN3A\ !$540-631 #domain fibronectin type III repeat homology #label !8FN3B\ !$640-728 #domain fibronectin type III repeat homology #label !8FN3C\ !$759-784 #domain transmembrane #status predicted #label TMM\ !$835-1112 #domain protein kinase homology #label KIN\ !$843-851 #region protein kinase ATP-binding motif\ !$43-106,370-424 #disulfide_bonds #status predicted\ !$84,159,501,594,707 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$868,885,977 #active_site Lys, Glu, Asp #status predicted SUMMARY #length 1136 #molecular-weight 124952 #checksum 16 SEQUENCE /// ENTRY JN0711 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112), receptor type tie precursor - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 14-Jul-1994 #sequence_revision 14-Jul-1994 #text_change 16-Jul-1999 ACCESSIONS JN0711; S33141; S57847; A48926; I65403 REFERENCE JN0711 !$#authors Iwama, A.; Hamaguchi, I.; Hashiyama, M.; Murayama, Y.; !1Yasunaga, K.; Suda, T. !$#journal Biochem. Biophys. Res. Commun. (1993) 195:301-309 !$#title Molecular cloning and characterization of mouse TIE and TEK !1receptor tyrosine kinase genes and their expression in !1hematopoietic stem cells. !$#cross-references MUID:93371421; PMID:8395828 !$#accession JN0711 !'##molecule_type mRNA !'##residues 1-1134 ##label IWA !'##cross-references GB:X73960; NID:g402601; PIDN:CAA52148.1; !1PID:g402602 REFERENCE S32690 !$#authors Sato, T.N.; Qin, Y.; Kozak, C.A.; Andus, K.L. !$#submission submitted to the EMBL Data Library, March 1993 !$#accession S33141 !'##molecule_type mRNA !'##residues 1-598,'L',600-1134 ##label SAT !'##cross-references EMBL:X71425; NID:g296610; PIDN:CAA50556.1; !1PID:g296611 REFERENCE S57845 !$#authors Sato, T.N.; Qin, Y.; Kozak, C.A.; Audus, K.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:9355-9358 !$#title tie-1 and tie-2 define another class of putative receptor !1tyrosine kinase genes expressed in early embryonic vascular !1system. !$#cross-references MUID:94022374; PMID:8415706 !$#accession S57847 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type mRNA !'##residues 1-598,'L',600-1134 ##label SA2 !'##cross-references EMBL:X71425; NID:g296610; PIDN:CAA50556.1; !1PID:g296611 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1March 1993 REFERENCE A48926 !$#authors Korhonen, J.; Partanen, J.; Armstrong, E.; Vaahtokari, A.; !1Elenius, K.; Jalkanen, M.; Alitalo, K. !$#journal Blood (1992) 80:2548-2555 !$#title Enhanced expression of the tie receptor tyrosine kinase in !1endothelial cells during neovascularization. !$#cross-references MUID:93043301; PMID:1384789 !$#accession A48926 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 221-352;740-890 ##label KOR !'##note sequence extracted from NCBI backbone (NCBIP:118660, !1NCBIP:118662) REFERENCE I52613 !$#authors Korhonen, J.; Lahtinen, I.; Halmekyto, M.; Alhonen, L.; !1Janne, J.; Dumont, D.; Alitalo, K. !$#journal Blood (1995) 86:1828-1835 !$#title Endothelial-specific gene expression directed by the tie !1gene promoter in vivo. !$#cross-references MUID:95383653; PMID:7655012 !$#accession I65403 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-19 ##label RES !'##cross-references GB:S79346; NID:g1086920 CLASSIFICATION #superfamily protein-tyrosine kinase, receptor type tie; EGF !1homology; fibronectin type III repeat homology; !1immunoglobulin homology; protein kinase homology KEYWORDS ATP; autophosphorylation; duplication; glycoprotein; !1phosphoprotein; phosphotransferase; receptor; tandem repeat; !1transmembrane protein; tyrosine-specific protein kinase FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-1134 #product protein-tyrosine kinase, receptor type tie !8#status predicted #label MAT\ !$36-105 #domain immunoglobulin homology #label IM1\ !$213-253 #domain EGF homology #label EG1\ !$257-300 #domain EGF homology #label EG2\ !$304-342 #domain EGF homology #label EG3\ !$363-426 #domain immunoglobulin homology #label IM2\ !$447-528 #domain fibronectin type III repeat homology #label !8FN3A\ !$540-629 #domain fibronectin type III repeat homology #label !8FN3B\ !$638-726 #domain fibronectin type III repeat homology #label !8FN3C\ !$757-782 #domain transmembrane #status predicted #label TMM\ !$833-1110 #domain protein kinase homology #label KIN\ !$841-849 #region protein kinase ATP-binding motif\ !$43-103,370-424 #disulfide_bonds #status predicted\ !$81,159,501,592,705 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$866,883,975 #active_site Lys, Glu, Asp #status predicted SUMMARY #length 1134 #molecular-weight 124698 #checksum 341 SEQUENCE /// ENTRY I58388 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112), receptor type tek precursor - human ORGANISM #formal_name Homo sapiens #common_name man DATE 02-Jul-1996 #sequence_revision 02-Jul-1996 #text_change 16-Jul-1999 ACCESSIONS I58388 REFERENCE I58388 !$#authors Ziegler, S.F.; Bird, T.A.; Schneringer, J.A.; Schooley, !1K.A.; Baum, P.R. !$#journal Oncogene (1993) 8:663-670 !$#title Molecular cloning and characterization of a novel receptor !1protein tyrosine kinase from human placenta. !$#cross-references MUID:93173509; PMID:8382358 !$#accession I58388 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-1124 ##label RES !'##cross-references GB:L06139; NID:g292823; PIDN:AAA61139.1; !1PID:g292824 GENETICS !$#gene GDB:TEK !'##cross-references GDB:344185; OMIM:600221 !$#map_position 9p21-9p21 FUNCTION !$#description catalyzes the phosphorylation of a peptidyl tyrosine residue !1by ATP CLASSIFICATION #superfamily protein-tyrosine kinase, receptor type tie; EGF !1homology; fibronectin type III repeat homology; !1immunoglobulin homology; protein kinase homology KEYWORDS ATP; autophosphorylation; duplication; glycoprotein; !1phosphoprotein; phosphotransferase; receptor; tandem repeat; !1transmembrane protein; tyrosine-specific protein kinase FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-1124 #product protein-tyrosine kinase, receptor type tek !8#status predicted #label MAT\ !$37-104 #domain immunoglobulin homology #label IM1\ !$135-137 #region cell attachment (R-G-D) motif\ !$211-251 #domain EGF homology #label EG1\ !$255-298 #domain EGF homology #label EG2\ !$302-340 #domain EGF homology #label EG3\ !$364-426 #domain immunoglobulin homology #label IM2\ !$447-527 #domain fibronectin type III repeat homology #label !8FN3A\ !$542-625 #domain fibronectin type III repeat homology #label !8FN3B\ !$638-720 #domain fibronectin type III repeat homology #label !8FN3C\ !$752-772 #domain transmembrane #status predicted #label TMM\ !$822-1099 #domain protein kinase homology #label KIN\ !$830-838 #region protein kinase ATP-binding motif\ !$140,158,399,438, !$464,560,596,649,691 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$855,872,964 #active_site Lys, Glu, Asp #status predicted SUMMARY #length 1124 #molecular-weight 125810 #checksum 6303 SEQUENCE /// ENTRY S57846 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112), receptor type tek precursor - bovine ALTERNATE_NAMES receptor tyrosine kinase tie-2 ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 28-Oct-1995 #sequence_revision 03-Nov-1995 #text_change 16-Jul-1999 ACCESSIONS S57846; S32691 REFERENCE S57845 !$#authors Sato, T.N.; Qin, Y.; Kozak, C.A.; Audus, K.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:9355-9358 !$#title tie-1 and tie-2 define another class of putative receptor !1tyrosine kinase genes expressed in early embryonic vascular !1system. !$#cross-references MUID:94022374; PMID:8415706 !$#accession S57846 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type mRNA !'##residues 1-1125 ##label SAT !'##cross-references EMBL:X71424; NID:g296577; PIDN:CAA50555.1; !1PID:g296578 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1March 1993 REFERENCE S32690 !$#authors Sato, T.N.; Qin, Y.; Kozak, C.A.; Andus, K.L. !$#submission submitted to the EMBL Data Library, March 1993 !$#accession S32691 !'##molecule_type mRNA !'##residues 1-1125 ##label SA2 !'##cross-references EMBL:X71424; NID:g296577; PIDN:CAA50555.1; !1PID:g296578 CLASSIFICATION #superfamily protein-tyrosine kinase, receptor type tie; EGF !1homology; fibronectin type III repeat homology; !1immunoglobulin homology; protein kinase homology KEYWORDS ATP; autophosphorylation; duplication; glycoprotein; !1phosphoprotein; phosphotransferase; receptor; tandem repeat; !1transmembrane protein; tyrosine-specific protein kinase FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-1125 #product protein-tyrosine kinase, receptor type tek !8#status predicted #label MAT\ !$37-104 #domain immunoglobulin homology #label IM1\ !$135-137 #region cell attachment (R-G-D) motif\ !$211-251 #domain EGF homology #label EG1\ !$255-298 #domain EGF homology #label EG2\ !$302-340 #domain EGF homology #label EG3\ !$364-426 #domain immunoglobulin homology #label IM2\ !$447-527 #domain fibronectin type III repeat homology #label !8FN3A\ !$542-626 #domain fibronectin type III repeat homology #label !8FN3B\ !$639-721 #domain fibronectin type III repeat homology #label !8FN3C\ !$753-773 #domain transmembrane #status predicted #label TMM\ !$823-1100 #domain protein kinase homology #label KIN\ !$831-839 #region protein kinase ATP-binding motif\ !$140,158,399,438, !$464,560,597,650,692 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$856,873,965 #active_site Lys, Glu, Asp #status predicted SUMMARY #length 1125 #molecular-weight 125926 #checksum 5 SEQUENCE /// ENTRY JN0712 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112), receptor type tek precursor - mouse ALTERNATE_NAMES protein-tyrosine kinase, receptor type tie-2 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 27-Jun-1994 #sequence_revision 27-Jun-1994 #text_change 16-Jul-1999 ACCESSIONS JN0712; S57848; S43495; S43494; S33142 REFERENCE JN0711 !$#authors Iwama, A.; Hamaguchi, I.; Hashiyama, M.; Murayama, Y.; !1Yasunaga, K.; Suda, T. !$#journal Biochem. Biophys. Res. Commun. (1993) 195:301-309 !$#title Molecular cloning and characterization of mouse TIE and TEK !1receptor tyrosine kinase genes and their expression in !1hematopoietic stem cells. !$#cross-references MUID:93371421; PMID:8395828 !$#accession JN0712 !'##molecule_type mRNA !'##residues 1-1123 ##label IWA REFERENCE S57845 !$#authors Sato, T.N.; Qin, Y.; Kozak, C.A.; Audus, K.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:9355-9358 !$#title tie-1 and tie-2 define another class of putative receptor !1tyrosine kinase genes expressed in early embryonic vascular !1system. !$#cross-references MUID:94022374; PMID:8415706 !$#accession S57848 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type mRNA !'##residues 1-786,788-1123 ##label SAT !'##cross-references EMBL:X71426; NID:g296612; PIDN:CAA50557.1; !1PID:g296613 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1March 1993 REFERENCE S43495 !$#authors Dumont, D.J. !$#submission submitted to the EMBL Data Library, April 1993 !$#accession S43495 !'##molecule_type mRNA !'##residues 1-537,'C',539-735,'G',737-786,788-1123 ##label DUM !'##cross-references EMBL:X67553; NID:g297158; PIDN:CAA47857.1; !1PID:g297159 REFERENCE S43494 !$#authors Dumont, D.J.; Yamaguchi, T.P.; Conlon, R.A.; Rossant, J.; !1Breitman, M.L. !$#journal Oncogene (1992) 7:1471-1480 !$#title tek, a novel tyrosine kinase gene located on mouse !1chromosome 4, is expressed in endothelial cells and their !1presumptive precursors. !$#cross-references MUID:92334855; PMID:1630810 !$#accession S43494 !'##molecule_type mRNA !'##residues 823-1123 ##label DUW !'##cross-references EMBL:X67553 COMMENT Receptor tyrosine kinase-ligand systems play an important !1role in the constitutive hematopoiesis, as seen in c-fms/ !1M-CSF and c-kit/steel factors. GENETICS !$#map_position 4 CLASSIFICATION #superfamily protein-tyrosine kinase, receptor type tie; EGF !1homology; fibronectin type III repeat homology; !1immunoglobulin homology; protein kinase homology KEYWORDS ATP; autophosphorylation; duplication; glycoprotein; !1phosphoprotein; phosphotransferase; receptor; tandem repeat; !1transmembrane protein; tyrosine-specific protein kinase FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-1123 #product protein-tyrosine kinase, receptor type tie-2 !8#status predicted #label MAT\ !$37-104 #domain immunoglobulin homology #label IM1\ !$135-137 #region cell attachment (R-G-D) motif\ !$211-251 #domain EGF homology #label EG1\ !$255-298 #domain EGF homology #label EG2\ !$302-340 #domain EGF homology #label EG3\ !$364-426 #domain immunoglobulin homology #label IM2\ !$447-525 #domain fibronectin type III repeat homology #label !8FN3A\ !$540-624 #domain fibronectin type III repeat homology #label !8FN3B\ !$637-719 #domain fibronectin type III repeat homology #label !8FN3C\ !$751-771 #domain transmembrane #status predicted #label TMM\ !$821-1098 #domain protein kinase homology #label KIN\ !$829-837 #region protein kinase ATP-binding motif\ !$140,158,399,438, !$464,558,595,648,690 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$854,871,963 #active_site Lys, Glu, Asp #status predicted SUMMARY #length 1123 #molecular-weight 125799 #checksum 2445 SEQUENCE /// ENTRY JH0771 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112), receptor type hyk precursor - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Jun-1993 #sequence_revision 10-Jun-1993 #text_change 21-Jul-2000 ACCESSIONS JH0771 REFERENCE JH0771 !$#authors Horita, K.; Yagi, T.; Kohmura, N.; Tomooka, Y.; Ikawa, Y.; !1Aizawa, S. !$#journal Biochem. Biophys. Res. Commun. (1992) 189:1747-1753 !$#title A novel tyrosine kinase, hyk, expressed in murine embryonic !1stem cells. !$#cross-references MUID:93129253; PMID:1282811 !$#accession JH0771 !'##molecule_type mRNA !'##residues 1-1125 ##label HOR !'##cross-references GB:D13738; NID:g220439; PIDN:BAA02883.1; !1PID:g220440 GENETICS !$#gene hyk CLASSIFICATION #superfamily protein-tyrosine kinase, receptor type tie; EGF !1homology; fibronectin type III repeat homology; !1immunoglobulin homology; protein kinase homology KEYWORDS ATP; autophosphorylation; duplication; glycoprotein; !1phosphoprotein; phosphotransferase; receptor; tandem repeat; !1transmembrane protein; tyrosine-specific protein kinase FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-1125 #product protein-tyrosine kinase, receptor type hyk !8#status predicted #label MAT\ !$37-104 #domain immunoglobulin homology #label IM1\ !$135-137 #region cell attachment (R-G-D) motif\ !$212-252 #domain EGF homology #label EG1\ !$256-299 #domain EGF homology #label EG2\ !$303-341 #domain EGF homology #label EG3\ !$365-427 #domain immunoglobulin homology #label IM2\ !$448-526 #domain fibronectin type III repeat homology #label !8FN3A\ !$541-625 #domain fibronectin type III repeat homology #label !8FN3B\ !$638-720 #domain fibronectin type III repeat homology #label !8FN3C\ !$752-773 #domain transmembrane #status predicted #label TMM\ !$823-1100 #domain protein kinase homology #label KIN\ !$831-839 #region protein kinase ATP-binding motif\ !$140,158,400,439, !$465,559,596,649,691 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$856,873,965 #active_site Lys, Glu, Asp #status predicted SUMMARY #length 1125 #molecular-weight 126313 #checksum 8642 SEQUENCE /// ENTRY S05582 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) ret precursor - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S05582; S03850 REFERENCE S05582 !$#authors Takahashi, M.; Buma, Y.; Hiai, H. !$#journal Oncogene (1989) 4:805-806 !$#title Isolation of ret proto-oncogene cDNA with an amino-terminal !1signal sequence. !$#cross-references MUID:89282215; PMID:2660074 !$#accession S05582 !'##molecule_type mRNA !'##residues 1-280 ##label TAK !'##cross-references EMBL:X15262; NID:g36000; PIDN:CAA33333.1; !1PID:g36001 REFERENCE S03850 !$#authors Takahashi, M.; Buma, Y.; Iwamoto, T.; Inaguma, Y.; Ikeda, !1H.; Hiai, H. !$#journal Oncogene (1988) 3:571-578 !$#title Cloning and expression of the ret proto-oncogene encoding a !1tyrosine kinase with two potential transmembrane domains. !$#cross-references MUID:90272230; PMID:3078962 !$#accession S03850 !'##molecule_type mRNA !'##residues 255-1114 ##label TAK2 !'##cross-references EMBL:X12949; NID:g38274; PIDN:CAA31408.1; !1PID:g38275 GENETICS !$#gene GDB:RET !'##cross-references GDB:120346; OMIM:164761 !$#map_position 10q11.2-10q11.2 CLASSIFICATION #superfamily protein-tyrosine kinase ret; protein kinase !1homology KEYWORDS ATP; phosphotransferase; proto-oncogene; transforming !1protein; transmembrane protein; tyrosine-specific protein !1kinase FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-1114 #product protein-tyrosine kinase ret #status !8predicted #label MAT\ !$636-657 #domain transmembrane #status predicted #label TMM\ !$722-1012 #domain protein kinase homology #label KIN\ !$730-738 #region protein kinase ATP-binding motif\ !$758 #active_site Lys #status predicted SUMMARY #length 1114 #molecular-weight 124317 #checksum 8917 SEQUENCE /// ENTRY S29926 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) ret - mouse ALTERNATE_NAMES gene ret proto-oncogene protein ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS I48735; S29926 REFERENCE I48735 !$#authors Iwamoto, T.; Taniguchi, M.; Asai, N.; Ohkusu, K.; Nakashima, !1I.; Takahashi, M. !$#journal Oncogene (1993) 8:1087-1091 !$#title cDNA cloning of mouse ret proto-oncogene and its sequence !1similarity to the cadherin superfamily. !$#cross-references MUID:93205390; PMID:8455936 !$#accession I48735 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-1115 ##label RES !'##cross-references EMBL:X67812; NID:g53973; PIDN:CAA48013.1; !1PID:g53974 CLASSIFICATION #superfamily protein-tyrosine kinase ret; protein kinase !1homology KEYWORDS ATP; phosphotransferase; transmembrane protein; !1tyrosine-specific protein kinase FEATURE !$723-1013 #domain protein kinase homology #label KIN\ !$731-739 #region protein kinase ATP-binding motif SUMMARY #length 1115 #molecular-weight 123728 #checksum 4526 SEQUENCE /// ENTRY S57450 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) ret - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S57450 REFERENCE S57450 !$#authors Robertson, K.; Mason, I. !$#submission submitted to the EMBL Data Library, June 1995 !$#description Expression of ret in the chicken embryo suggests roles in !1regionalisation of the vagal neural tube and somites and in !1development of multiple neural crest lineages. !$#accession S57450 !'##status preliminary !'##molecule_type mRNA !'##residues 1-1064 ##label ROB !'##cross-references EMBL:Z49898; NID:g871041; PIDN:CAA90078.1; !1PID:g871042 CLASSIFICATION #superfamily protein-tyrosine kinase ret; protein kinase !1homology KEYWORDS ATP; autophosphorylation; glycoprotein; phosphoprotein; !1phosphotransferase; receptor; transmembrane protein; !1tyrosine-specific protein kinase FEATURE !$714-1004 #domain protein kinase homology #label KIN\ !$722-730 #region protein kinase ATP-binding motif SUMMARY #length 1064 #molecular-weight 120463 #checksum 6699 SEQUENCE /// ENTRY TVHUFE #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) fer - human ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 11-Jun-1999 ACCESSIONS A31943; I57573 REFERENCE A31943 !$#authors Hao, Q.L.; Heisterkamp, N.; Groffen, J. !$#journal Mol. Cell. Biol. (1989) 9:1587-1593 !$#title Isolation and sequence analysis of a novel human tyrosine !1kinase gene. !$#cross-references MUID:89261786; PMID:2725517 !$#accession A31943 !'##molecule_type mRNA !'##residues 1-822 ##label HAO !'##cross-references GB:J03358; NID:g339714; PIDN:AAA61190.1; !1PID:g339715 GENETICS !$#gene GDB:FER !'##cross-references GDB:125243; OMIM:176942 !$#map_position 5q12-5q14 FUNCTION !$#description catalyzes the phosphorylation of a peptidyl tyrosine residue !1by ATP CLASSIFICATION #superfamily protein-tyrosine kinase fps; protein kinase !1homology; SH2 homology KEYWORDS ATP; autophosphorylation; blocked amino end; lipoprotein; !1myristylation; phosphoprotein; phosphotransferase; !1proto-oncogene; transforming protein; tyrosine-specific !1protein kinase FEATURE !$2-822 #product protein-tyrosine kinase fer #status !8predicted #label MAT\ !$460-546 #domain SH2 homology #label SH2\ !$561-821 #domain protein kinase homology #label KIN\ !$569-577 #region protein kinase ATP-binding motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$591 #active_site Lys #status predicted SUMMARY #length 822 #molecular-weight 94623 #checksum 3328 SEQUENCE /// ENTRY TVHUFF #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) fes/fps - human ORGANISM #formal_name Homo sapiens #common_name man DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 11-Jun-1999 ACCESSIONS A24673; A60188 REFERENCE A24673 !$#authors Roebroek, A.J.M.; Schalken, J.A.; Verbeek, J.S.; Van den !1Ouweland, A.M.W.; Onnekink, C.; Bloemers, H.P.J.; Van de !1Ven, W.J.M. !$#journal EMBO J. (1985) 4:2897-2903 !$#title The structure of the human c-fes/fps proto-oncogene. !$#cross-references MUID:86055727; PMID:4065096 !$#accession A24673 !'##molecule_type DNA !'##residues 1-822 ##label ROE !'##cross-references GB:X06292; GB:M14209; GB:M14589; NID:g31348; !1PIDN:CAA29619.1; PID:g31349 REFERENCE A60188 !$#authors Alcalay, M.; Antolini, F.; Van de Ven, W.J.; Lanfrancone, !1L.; Grignani, F.; Pelicci, P.G. !$#journal Oncogene (1990) 5:267-275 !$#title Characterization of human and mouse c-fes cDNA clones and !1identification of the 5' end of the gene. !$#cross-references MUID:90191711; PMID:2179816 !$#accession A60188 !'##molecule_type mRNA !'##residues 1-718,'S',720-822 ##label ALC !'##cross-references GB:X52192; NID:g29890; PIDN:CAA36438.1; PID:g29891 !'##note the authors translated the codon TCC for residue 719 as Leu GENETICS !$#gene GDB:FES !'##cross-references GDB:119906; OMIM:190030 !$#map_position 15q26.1-15q26.1 !$#introns 71/3; 129/3; 162/1; 223/2; 269/2; 309/2; 350/2; 412/3; 440/ !13; 510/3; 51/3; 569/3; 609/2; 641/1; 682/2; 735/1; 776/1 FUNCTION !$#description catalyzes the phosphorylation of a peptidyl tyrosine residue !1by ATP CLASSIFICATION #superfamily protein-tyrosine kinase fps; protein kinase !1homology; SH2 homology KEYWORDS ATP; autophosphorylation; blocked amino end; lipoprotein; !1myristylation; phosphoprotein; phosphotransferase; !1proto-oncogene; transforming protein; tyrosine-specific !1protein kinase FEATURE !$2-822 #product protein-tyrosine kinase fes/fps #status !8predicted #label MAT\ !$460-545 #domain SH2 homology #label SH2\ !$559-821 #domain protein kinase homology #label KIN\ !$567-575 #region protein kinase ATP-binding motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$590 #active_site Lys #status predicted SUMMARY #length 822 #molecular-weight 93496 #checksum 7719 SEQUENCE /// ENTRY TVCTFF #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) fes/fps - cat ORGANISM #formal_name Felis silvestris catus #common_name domestic cat DATE 30-Sep-1989 #sequence_revision 30-Jun-1992 #text_change 23-Feb-1997 ACCESSIONS A27824 REFERENCE A27824 !$#authors Roebroek, A.J.M.; Schalken, J.A.; Onnekink, C.; Bloemers, !1H.P.J.; Van de Ven, W.J.M. !$#journal J. Virol. (1987) 61:2009-2016 !$#title Structure of the feline c-fes/fps proto-oncogene: genesis of !1a retroviral oncogene. !$#cross-references MUID:87198954; PMID:3553615 !$#accession A27824 !'##molecule_type DNA !'##residues 1-820 ##label ROE GENETICS !$#gene fes/fps CLASSIFICATION #superfamily protein-tyrosine kinase fps; protein kinase !1homology; SH2 homology KEYWORDS ATP; autophosphorylation; phosphoprotein; !1phosphotransferase; proto-oncogene; transforming protein; !1tyrosine-specific protein kinase FEATURE !$458-543 #domain SH2 homology #label SH2\ !$557-819 #domain protein kinase homology #label KIN\ !$565-573 #region protein kinase ATP-binding motif\ !$588 #active_site Lys #status predicted\ !$711 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 820 #molecular-weight 92973 #checksum 4211 SEQUENCE /// ENTRY TVMVGC #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) fes - feline sarcoma virus (strain Gardner-Arnstein) ORGANISM #formal_name feline sarcoma virus #note host Felis sp. (cat) DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 23-Feb-1997 ACCESSIONS A00651 REFERENCE A00651 !$#authors Hampe, A.; Laprevotte, I.; Galibert, F.; Fedele, L.A.; !1Sherr, C.J. !$#journal Cell (1982) 30:775-785 !$#title Nucleotide sequences of feline retroviral oncogenes (v-fes) !1provide evidence for a family of typrosine-specific protein !1kinase genes. !$#cross-references MUID:83050963; PMID:6183005 !$#accession A00651 !'##molecule_type DNA !'##residues 1-609 ##label HAM COMMENT This protein is synthesized as a gag-fes polyprotein. GENETICS !$#gene fes CLASSIFICATION #superfamily protein-tyrosine kinase fps; protein kinase !1homology; SH2 homology KEYWORDS ATP; autophosphorylation; oncogene; phosphoprotein; !1phosphotransferase; transforming protein; tyrosine-specific !1protein kinase FEATURE !$247-332 #domain SH2 homology #label SH2\ !$346-608 #domain protein kinase homology #label KIN\ !$354-362 #region protein kinase ATP-binding motif\ !$377 #active_site Lys #status predicted SUMMARY #length 609 #molecular-weight 68769 #checksum 675 SEQUENCE /// ENTRY TVMVCS #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) fes - feline sarcoma virus (strain Snyder-Theilen) ORGANISM #formal_name feline sarcoma virus #note host Felis sp. (cat) DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 23-Feb-1997 ACCESSIONS A00652 REFERENCE A00651 !$#authors Hampe, A.; Laprevotte, I.; Galibert, F.; Fedele, L.A.; !1Sherr, C.J. !$#journal Cell (1982) 30:775-785 !$#title Nucleotide sequences of feline retroviral oncogenes (v-fes) !1provide evidence for a family of typrosine-specific protein !1kinase genes. !$#cross-references MUID:83050963; PMID:6183005 !$#accession A00652 !'##molecule_type DNA !'##residues 1-477 ##label HAM COMMENT This protein is synthesized as a gag-fes polyprotein. GENETICS !$#gene fes CLASSIFICATION #superfamily protein-tyrosine kinase fps; protein kinase !1homology; SH2 homology KEYWORDS ATP; autophosphorylation; oncogene; phosphoprotein; !1phosphotransferase; transforming protein; tyrosine-specific !1protein kinase FEATURE !$115-200 #domain SH2 homology #label SH2\ !$214-476 #domain protein kinase homology #label KIN\ !$222-230 #region protein kinase ATP-binding motif\ !$245 #active_site Lys #status predicted SUMMARY #length 477 #molecular-weight 53756 #checksum 7012 SEQUENCE /// ENTRY TVFVFP #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) fps - avian sarcoma virus PRCII ORGANISM #formal_name avian sarcoma virus PRCII #note host Gallus gallus (chicken) DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 23-Feb-1997 ACCESSIONS A00650 REFERENCE A00650 !$#authors Huang, C.C.; Hammond, C.; Bishop, J.M. !$#journal J. Virol. (1984) 50:125-131 !$#title Nucleotide sequence of v-fps in the PRCII strain of avian !1sarcoma virus. !$#cross-references MUID:84138803; PMID:6321783 !$#accession A00650 !'##molecule_type DNA !'##residues 1-533 ##label HUA COMMENT This protein is synthesized as a gag-fps polyprotein. GENETICS !$#gene fps CLASSIFICATION #superfamily protein-tyrosine kinase fps; protein kinase !1homology; SH2 homology KEYWORDS ATP; autophosphorylation; oncogene; phosphoprotein; !1phosphotransferase; transforming protein; tyrosine-specific !1protein kinase FEATURE !$171-256 #domain SH2 homology #label SH2\ !$270-532 #domain protein kinase homology #label KIN\ !$278-286 #region protein kinase ATP-binding motif\ !$301 #active_site Lys #status predicted SUMMARY #length 533 #molecular-weight 60506 #checksum 1279 SEQUENCE /// ENTRY TVFVF #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) fps - Fujinami sarcoma virus ORGANISM #formal_name Fujinami sarcoma virus #note host Gallus gallus (chicken) DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 23-Feb-1997 ACCESSIONS A00636 REFERENCE A00636 !$#authors Shibuya, M.; Hanafusa, H. !$#journal Cell (1982) 30:787-795 !$#title Nucleotide sequence of Fujinami sarcoma virus: evolutionary !1relationship of its transforming gene with transforming !1genes of other sarcoma viruses. !$#cross-references MUID:83050964; PMID:6291784 !$#accession A00636 !'##molecule_type genomic RNA !'##residues 1-873 ##label SHI COMMENT This protein is synthesized as a gag-fps polyprotein. GENETICS !$#gene fps CLASSIFICATION #superfamily protein-tyrosine kinase fps; protein kinase !1homology; SH2 homology KEYWORDS ATP; autophosphorylation; oncogene; phosphoprotein; !1phosphotransferase; polyprotein; transforming protein; !1tyrosine-specific protein kinase FEATURE !$511-596 #domain SH2 homology #label SH2\ !$610-872 #domain protein kinase homology #label KIN\ !$618-626 #region protein kinase ATP-binding motif\ !$641 #active_site Lys #status predicted SUMMARY #length 873 #molecular-weight 99536 #checksum 2491 SEQUENCE /// ENTRY TVFVFS #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) fps (clone ts) - Fujinami sarcoma virus ORGANISM #formal_name Fujinami sarcoma virus DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 11-Jun-1999 ACCESSIONS A26898 REFERENCE A26898 !$#authors Chen, L.H.; Hatada, E.; Wheatley, W.; Lee, W.H. !$#journal Virology (1986) 155:106-119 !$#title Single amino acid substitution, from Glu-1025 to Asp, of the !1fps oncogenic protein causes temperature sensitivity in !1transformation and kinase activity. !$#cross-references MUID:87044080; PMID:2877522 !$#accession A26898 !'##molecule_type DNA !'##residues 1-873 ##label CHE !'##cross-references GB:M14930; NID:g209688; PIDN:AAA42403.1; !1PID:g209689 COMMENT This protein is synthesized as a gag-fps polyprotein. GENETICS !$#gene fps CLASSIFICATION #superfamily protein-tyrosine kinase fps; protein kinase !1homology; SH2 homology KEYWORDS ATP; autophosphorylation; oncogene; phosphoprotein; !1phosphotransferase; transforming protein; tyrosine-specific !1protein kinase FEATURE !$511-596 #domain SH2 homology #label SH2\ !$610-872 #domain protein kinase homology #label KIN\ !$618-626 #region protein kinase ATP-binding motif\ !$641 #active_site Lys #status predicted SUMMARY #length 873 #molecular-weight 99447 #checksum 2493 SEQUENCE /// ENTRY OKFFPS #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112), fps/fes homolog - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES kinase-related transforming protein (fps) ORGANISM #formal_name Drosophila melanogaster DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 11-Jun-1999 ACCESSIONS A39670; S11628 REFERENCE A39670 !$#authors Katzen, A.L.; Montarras, D.; Jackson, J.; Paulson, R.F.; !1Kornberg, T.; Bishop, J.M. !$#journal Mol. Cell. Biol. (1991) 11:226-239 !$#title A gene related to the proto-oncogene fps/fes is expressed at !1diverse times during the life cycle of Drosophila !1melanogaster. !$#cross-references MUID:91094836; PMID:1898762 !$#accession A39670 !'##molecule_type mRNA !'##residues 1-803 ##label KA2 !'##cross-references EMBL:X52844; NID:g7971; PIDN:CAA37036.1; PID:g7972 GENETICS !$#gene dfps85D !'##cross-references FlyBase:FBgn0000723 CLASSIFICATION #superfamily protein-tyrosine kinase fps; protein kinase !1homology; SH2 homology KEYWORDS ATP; autophosphorylation; phosphoprotein; !1phosphotransferase; proto-oncogene; transforming protein; !1tyrosine-specific protein kinase FEATURE !$438-525 #domain SH2 homology #label SH2\ !$539-799 #domain protein kinase homology #label KIN\ !$547-555 #region protein kinase ATP-binding motif\ !$570 #active_site Lys #status predicted SUMMARY #length 803 #molecular-weight 92489 #checksum 2040 SEQUENCE /// ENTRY TVHUA #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) abl - human ALTERNATE_NAMES kinase-related transforming protein p150 ORGANISM #formal_name Homo sapiens #common_name man DATE 03-Aug-1984 #sequence_revision 17-Nov-1995 #text_change 04-Feb-2000 ACCESSIONS S08519; A25582; A00625; E38268 REFERENCE S08519 !$#authors Fainstein, E.; Einat, M.; Gokkel, E.; Marcelle, C.; Croce, !1C.M.; Gale, R.P.; Canaani, E. !$#journal Oncogene (1989) 4:1477-1481 !$#title Nucleotide sequence analysis of human abl and bcr-abl cDNAs. !$#cross-references MUID:90082420; PMID:2687768 !$#accession S08519 !'##molecule_type mRNA !'##residues 1-1130 ##label FAI !'##cross-references EMBL:X16416 REFERENCE A25582 !$#authors Shtivelman, E.; Lifshitz, B.; Gale, R.P.; Roe, B.A.; !1Canaani, E. !$#journal Cell (1986) 47:277-284 !$#title Alternative splicing of RNAs transcribed from the human abl !1gene and from the bcr-abl fused gene. !$#cross-references MUID:87028219; PMID:3021337 !$#accession A25582 !'##molecule_type mRNA !'##residues 1-139,'P',141-158,'S',160-444,'R',446-458,'K',460-718,'V', !1720-836,'W',838-862,'R',864-893,'K',895-916,'R',918,'G', !1920-951,'G',953-967,'P',969-982,'L',983-1020,'P',1023-1044, !1'G',1046-1102,'S',1104-1130 ##label SHT !'##note the authors translated the codon GAG for residues 279, 282, !1527, 549, and 581 as Gly REFERENCE A00625 !$#authors Groffen, J.; Heisterkamp, N.; Reynolds Jr., F.H.; !1Stephenson, J.R. !$#journal Nature (1983) 304:167-169 !$#title Homology between phosphotyrosine acceptor site of human !1c-abl and viral oncogene products. !$#cross-references MUID:83245023; PMID:6191223 !$#accession A00625 !'##molecule_type DNA !'##residues 360-423,'GK',426 ##label GRO REFERENCE A38268 !$#authors Partanen, J.; Maekelae, T.P.; Alitalo, R.; Lehvaeslaiho, H.; !1Alitalo, K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:8913-8917 !$#title Putative tyrosine kinases expressed in K-562 human leukemia !1cells. !$#cross-references MUID:91062389; PMID:2247464 !$#accession E38268 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type mRNA !'##residues 365-420 ##label PAR GENETICS !$#gene GDB:ABL1 !'##cross-references GDB:119640; OMIM:189980 !$#map_position 9q34.1-9q34.1 FUNCTION !$#description catalyzes the phosphorylation of a peptidyl tyrosine residue !1by ATP CLASSIFICATION #superfamily human protein-tyrosine kinase abl; protein !1kinase homology; SH2 homology; SH3 homology KEYWORDS ATP; autophosphorylation; glycoprotein; phosphoprotein; !1phosphotransferase; tyrosine-specific protein kinase FEATURE !$68-116 #domain SH3 homology #label SH3\ !$127-217 #domain SH2 homology #label SH2\ !$240-500 #domain protein kinase homology #label KIN\ !$248-256 #region protein kinase ATP-binding motif\ !$146,770 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$271 #active_site Lys #status predicted\ !$393 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 1130 #molecular-weight 122958 #checksum 6762 SEQUENCE /// ENTRY FOMVGM #type complete TITLE gag-abl polyprotein - Abelson murine leukemia virus CONTAINS amino end of core shell protein p30; core protein p15; inner coat protein p12; protein-tyrosine kinase (EC 2.7.1.112) abl ORGANISM #formal_name Abelson murine leukemia virus #note host Mus sp. (mouse) DATE 14-Nov-1983 #sequence_revision 09-Sep-1994 #text_change 11-Jun-1999 ACCESSIONS A03931; A00627; A93955 REFERENCE A93955 !$#authors Reddy, E.P.; Smith, M.J.; Srinivasan, A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:3623-3627 !$#title Nucleotide sequence of Abelson murine leukemia virus genome: !1structural similarity of its transforming gene product to !1other onc gene products with tyrosine-specific kinase !1activity. !$#cross-references MUID:83221648; PMID:6304726 !$#accession A03931 !'##molecule_type DNA !'##residues 1-981 ##label RED !'##cross-references GB:J02009; NID:g331887; PIDN:AAA46471.1; !1PID:g331888 !'##note the authors translated the codon GGA for residue 186 as Glu REFERENCE A93980 !$#authors Reddy, E.P.; Smith, M.J.; Srinivasan, A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:7372 !$#contents annotation; erratum, residues 588-746 GENETICS !$#gene gag-abl CLASSIFICATION #superfamily Abelson murine leukemia virus gag-abl !1polyprotein; protein kinase homology; SH2 homology KEYWORDS ATP; core protein; oncogene; phosphotransferase; !1polyprotein; transforming protein; tyrosine-specific protein !1kinase FEATURE !$1-131 #product core protein p15 #status predicted #label !8P15\ !$132-215 #product inner coat protein p12 #status predicted !8#label P12\ !$216-235 #region amino end of core shell protein p30\ !$248-338 #domain SH2 homology #label SH2\ !$361-621 #domain protein kinase homology #label KIN\ !$369-377 #region protein kinase ATP-binding motif\ !$392 #active_site Lys #status predicted SUMMARY #length 981 #molecular-weight 107494 #checksum 6903 SEQUENCE /// ENTRY TVFFA #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) abl - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 15-Nov-1984 #sequence_revision 30-Sep-1989 #text_change 11-Jun-1999 ACCESSIONS A28128; A00628 REFERENCE A28128 !$#authors Henkemeyer, M.J.; Bennett, R.L.; Gertler, F.B.; Hoffmann, !1F.M. !$#journal Mol. Cell. Biol. (1988) 8:843-853 !$#title DNA sequence, structure, and tyrosine kinase activity of the !1Drosophila melanogaster Abelson proto-oncogene homolog. !$#cross-references MUID:88174728; PMID:2832740 !$#accession A28128 !'##molecule_type DNA !'##residues 1-1520 ##label HEN !'##cross-references GB:M19692; GB:M18402; NID:g158598; PIDN:AAA28934.1; !1PID:g158600 REFERENCE A00628 !$#authors Hoffmann, F.M.; Fresco, L.D.; Hoffman-Falk, H.; Shilo, B.Z. !$#journal Cell (1983) 35:393-401 !$#title Nucleotide sequences of the Drosophila src and abl homologs: !1conservation and variability in the src family oncogenes. !$#cross-references MUID:84082064; PMID:6317185 !$#accession A00628 !'##molecule_type DNA !'##residues 'A',375,'AQ',378-644,'VGDV' ##label HOF !'##cross-references GB:K01042; NID:g157175; PIDN:AAA28443.1; !1PID:g157176 GENETICS !$#gene abl !'##cross-references FlyBase:FBgn0000017 !$#introns 112/1; 130/1; 310/2; 449/1; 644/3; 735/1; 775/2; 805/1; !11350/1 CLASSIFICATION #superfamily Drosophila protein-tyrosine kinase abl; protein !1kinase homology; SH2 homology; SH3 homology KEYWORDS ATP; autophosphorylation; phosphoprotein; !1phosphotransferase; transforming protein; tyrosine-specific !1protein kinase FEATURE !$211-260 #domain SH3 homology #label SH3\ !$271-363 #domain SH2 homology #label SH2\ !$386-646 #domain protein kinase homology #label KIN\ !$394-402 #region protein kinase ATP-binding motif\ !$417 #active_site Lys #status predicted SUMMARY #length 1520 #molecular-weight 161835 #checksum 352 SEQUENCE /// ENTRY TVHUY2 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) tyk2 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 04-Mar-1993 #sequence_revision 17-Nov-1995 #text_change 11-Jun-1999 ACCESSIONS S12127; A42999; B60189; F38268 REFERENCE S12127 !$#authors Firmbach-Kraft, I.; Byers, M.; Shows, T.; Dalla-Favera, R.; !1Krolewski, J.J. !$#journal Oncogene (1990) 5:1329-1336 !$#title tyk2, prototype of a novel class of non-receptor tyrosine !1kinase genes. !$#cross-references MUID:91016433; PMID:2216457 !$#accession S12127 !'##molecule_type mRNA !'##residues 1-1187 ##label FIR !'##cross-references EMBL:X54637; NID:g37503; PIDN:CAA38449.1; !1PID:g37504 REFERENCE A42999 !$#authors Velazquez, L.; Fellous, M.; Stark, G.R.; Pellegrini, S. !$#journal Cell (1992) 70:313-322 !$#title A protein tyrosine kinase in the interferon alpha/beta !1signaling pathway. !$#cross-references MUID:92346718; PMID:1386289 !$#accession A42999 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type mRNA !'##residues 289-683,'I',685-868,'L',870-881,'P',883-886,'SD',889-890, !1'V',892-1016,'QH',1019-1187 ##label VEL !'##experimental_source Daudi cell line !'##note sequence extracted from NCBI backbone (NCBIP:110000) REFERENCE A60189 !$#authors Krolewski, J.J.; Lee, R.; Eddy, R.; Shows, T.B.; !1Dalla-Favera, R. !$#journal Oncogene (1990) 5:277-282 !$#title Identification and chromosomal mapping of new human tyrosine !1kinase genes. !$#cross-references MUID:90191712; PMID:2156206 !$#accession B60189 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1007-1162 ##label KRO !'##cross-references GB:X54637 REFERENCE A38268 !$#authors Partanen, J.; Maekelae, T.P.; Alitalo, R.; Lehvaeslaiho, H.; !1Alitalo, K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:8913-8917 !$#title Putative tyrosine kinases expressed in K-562 human leukemia !1cells. !$#cross-references MUID:91062389; PMID:2247464 !$#accession F38268 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type mRNA !'##residues 1025-1082 ##label PAR GENETICS !$#gene GDB:TYK2 !'##cross-references GDB:125368; OMIM:176941 !$#map_position 19p13.2-19p13.2 FUNCTION !$#description catalyzes the phosphorylation of a peptidyl tyrosine residue !1by ATP !$#note links the interferon alpha/beta receptor to the cytoplasmic !1transcription factor in the cascade that mediates activation !1of interferon-responsive genes CLASSIFICATION #superfamily protein-tyrosine kinase tyk2; protein kinase !1homology KEYWORDS ATP; magnesium; phosphotransferase; tyrosine-specific !1protein kinase FEATURE !$587-873 #domain protein kinase homology #label KIN1\ !$894-1172 #domain protein kinase homology #label KIN2\ !$903-911 #region protein kinase ATP-binding motif\ !$930,947,1023 #active_site Lys, Glu, Asp #status predicted\ !$1028,1041 #binding_site magnesium (Asn, Asp) #status predicted SUMMARY #length 1187 #molecular-weight 133659 #checksum 421 SEQUENCE /// ENTRY TVFF7L #type complete TITLE kinase-related protein sevenless - fruit fly (Drosophila melanogaster) CONTAINS protein-tyrosine kinase (EC 2.7.1.112) ORGANISM #formal_name Drosophila melanogaster DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 11-Jun-1999 ACCESSIONS A28912; A60107; A28827 REFERENCE A28912 !$#authors Basler, K.; Hafen, E. !$#journal Cell (1988) 54:299-311 !$#title Control of photoreceptor cell fate by the sevenless protein !1requires a functional tyrosine kinase domain. !$#cross-references MUID:88282538; PMID:2840202 !$#accession A28912 !'##molecule_type DNA !'##residues 1-2554 ##label BAS !'##cross-references GB:J03158; NID:g158418; PIDN:AAA28882.1; !1PID:g158419 REFERENCE A60107 !$#authors Hafen, E.; Basler, K.; Edstroem, J.E.; Rubin, G.M. !$#journal Science (1987) 236:55-63 !$#title Sevenless, a cell-specific homeotic gene of Drosophila, !1encodes a putative transmembrane receptor with a tyrosine !1kinase domain. !$#cross-references MUID:87177965; PMID:2882603 !$#accession A60107 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 2062-2554 ##label HAF REFERENCE A28827 !$#authors Bowtell, D.D.L.; Simon, M.A.; Rubin, G.M. !$#journal Genes Dev. (1988) 2:620-634 !$#title Nucleotide sequence and structure of the sevenless gene of !1Drosophila melanogaster. !$#cross-references MUID:88329706; PMID:3138161 !$#accession A28827 !'##molecule_type DNA; mRNA !'##residues 'RSSAS',1-391,'V',393-1822,'Q',1824-2270,'C',2272-2554 !1##label BOW !'##cross-references GB:X13665 !'##note 392-Met, 1000-Leu, 1364-Val, 1668-Val, 1703-His, 1730-Lys, !11731-Glu, 1741-Met, and 2271-Arg were also found COMMENT The sevenless gene controls the development of the R7 class !1of photoreceptor cells. GENETICS !$#gene sev !'##cross-references FlyBase:FBgn0003366 !$#map_position X10A1-A2 !$#introns 227/3; 252/3; 274/3; 406/3; 486/3; 596/2; 2150/1; 2242/3; !12307/3; 2456/2 CLASSIFICATION #superfamily sevenless; fibronectin type III repeat !1homology; LDL receptor YWTD-containing repeat homology; !1protein kinase homology KEYWORDS ATP; autophosphorylation; glycoprotein; phosphoprotein; !1phosphotransferase; photoreceptor; receptor; transmembrane !1protein; tyrosine-specific protein kinase FEATURE !$102-122 #domain transmembrane #status predicted #label TMN1\ !$437-528 #domain fibronectin type III repeat homology #label !8FN3\ !$2124-2147 #domain transmembrane #status predicted #label TMN2\ !$2207-2488 #domain protein kinase homology #label KIN\ !$2215-2223 #region protein kinase ATP-binding motif\ !$129,481,505,617, !$647,966,1228,1313, !$1353,1550,1557, !$1639,1725,1756, !$1804,1889,1947,2073 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$2242 #active_site Lys #status predicted SUMMARY #length 2554 #molecular-weight 287108 #checksum 3353 SEQUENCE /// ENTRY TVCHSR #type complete TITLE kinase-related protein ros precursor - chicken ALTERNATE_NAMES sevenless homolog c-ros CONTAINS protein-tyrosine kinase (EC 2.7.1.112) ros ORGANISM #formal_name Gallus gallus #common_name chicken DATE 31-Dec-1989 #sequence_revision 07-Oct-1994 #text_change 16-Jun-2000 ACCESSIONS A60197; A28357; A25225 REFERENCE A60197 !$#authors Chen, J.; Heller, D.; Poon, B.; Kang, L.; Wang, L.H. !$#journal Oncogene (1991) 6:257-264 !$#title The proto-oncogene c-ros codes for a transmembrane tyrosine !1protein kinase sharing sequence and structural homology with !1sevenless protein of Drosophila melanogaster. !$#cross-references MUID:91156299; PMID:1900358 !$#accession A60197 !'##molecule_type mRNA !'##residues 1-2311 ##label CHE !'##note authors translated the codon GGA for residue 961 as Ser, AAT !1for residue 962 as Ser, TCT for residue 963 as Gly, TCA for !1residue 964 as Asn, and GCT for residue 1377 as Gly REFERENCE A28357 !$#authors Podell, S.B.; Sefton, B.M. !$#journal Oncogene (1987) 2:9-14 !$#title Chicken proto-oncogene c-ros cDNA clones: identification of !1a c-ros RNA transcript and deduction of the amino acid !1sequence of the carboxyl terminus of the c-ros product. !$#cross-references MUID:88143715; PMID:3325887 !$#accession A28357 !'##molecule_type mRNA !'##residues 2010-2139,'LP',2142-2311 ##label POD !'##cross-references GB:X06770; NID:g63775; PIDN:CAA29938.1; !1PID:g1334743 REFERENCE A25225 !$#authors Neckameyer, W.S.; Shibuya, M.; Hsu, M.T.; Wang, L.H. !$#journal Mol. Cell. Biol. (1986) 6:1478-1486 !$#title Proto-oncogene c-ros codes for a molecule with structural !1features common to those of growth factor receptors and !1displays tissue-specific and developmentally regulated !1expression. !$#cross-references MUID:87064428; PMID:3023892 !$#accession A25225 !'##molecule_type DNA !'##residues 1868-2139,'LP',2142-2254, !1'SSTKLLRVSLGSAVPTAFAQTCNSVNVESQNGLGWKGP' ##label NEC !'##cross-references GB:M13013; NID:g212636; PIDN:AAA49058.1; !1PID:g212637 GENETICS !$#gene ros CLASSIFICATION #superfamily kinase-related protein ros; LDL receptor !1YWTD-containing repeat homology; protein kinase homology KEYWORDS ATP; autophosphorylation; glycoprotein; phosphoprotein; !1phosphotransferase; proto-oncogene; transforming protein; !1transmembrane protein; tyrosine-specific protein kinase FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-2311 #product kinase-related protein ros #status predicted !8#label MAT\ !$28-1873 #domain extracellular #status predicted #label EXT\ !$344-387 #domain LDL receptor YWTD-containing repeat homology !8#label YW1\ !$475-512 #domain LDL receptor YWTD-containing repeat homology !8#label YWA\ !$715-758 #domain LDL receptor YWTD-containing repeat homology !8#label YW2\ !$759-799 #domain LDL receptor YWTD-containing repeat homology !8#label YW3\ !$800-839 #domain LDL receptor YWTD-containing repeat homology !8#label YW4\ !$844-889 #domain LDL receptor YWTD-containing repeat homology !8#label YW5\ !$894-934 #domain LDL receptor YWTD-containing repeat homology !8#label YW6\ !$1546-1587 #domain LDL receptor YWTD-containing repeat homology !8#label YW7\ !$1874-1899 #domain transmembrane #status predicted #label TMN\ !$1900-2311 #domain intracellular #status predicted #label INT\ !$1959-2239 #domain protein kinase homology #label KIN\ !$1967-1975 #region protein kinase ATP-binding motif\ !$49,65,77,123,132, !$265,287,307,333, !$377,480,607,628, !$706,714,911,940, !$962,971,1110,1154, !$1180,1233,1255, !$1282,1316,1470, !$1509,1588,1628, !$1682,1696,1730, !$1792,1795,1822 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$1996 #active_site Lys #status predicted\ !$2127,2131,2132 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 2311 #molecular-weight 260958 #checksum 5244 SEQUENCE /// ENTRY TVHURS #type complete TITLE kinase-related protein ros-1 precursor - human ALTERNATE_NAMES protein-tyrosine kinase mcf3 (activated ros-1) CONTAINS protein-tyrosine kinase (EC 2.7.1.112) ros-1 ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1988 #sequence_revision 07-Oct-1994 #text_change 11-Jun-1999 ACCESSIONS A35512; A25223; A24421; A33081 REFERENCE A35512 !$#authors Birchmeier, C.; O'Neill, K.; Riggs, M.; Wigler, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:4799-4803 !$#title Characterization of ROS1 cDNA from a human glioblastoma cell !1line. !$#cross-references MUID:90280463; PMID:2352949 !$#accession A35512 !'##molecule_type mRNA !'##residues 1-2212,'N',2214-2227,'QC',2229-2347 ##label BIR !'##cross-references GB:M34353 !'##experimental_source glioblastoma cell line SW-1088 REFERENCE A25223 !$#authors Matsushime, H.; Wang, L.H.; Shibuya, M. !$#journal Mol. Cell. Biol. (1986) 6:3000-3004 !$#title Human c-ros-1 gene homologous to the v-ros sequence of UR2 !1sarcoma virus encodes for a transmembrane receptorlike !1molecule. !$#cross-references MUID:87064611; PMID:3023956 !$#accession A25223 !'##molecule_type DNA !'##residues 1790-2245,'KFDSSEFSSFRCTVN' ##label MA2 !'##cross-references GB:M13368 !'##experimental_source placenta !'##note the differences after residue 2245 result from the authors' !1misinterpretation of a splice junction and consequent !1translation from the intron sequence REFERENCE A24421 !$#authors Birchmeier, C.; Birnbaum, D.; Waitches, G.; Fasano, O.; !1Wigler, M. !$#journal Mol. Cell. Biol. (1986) 6:3109-3116 !$#title Characterization of an activated human ros gene. !$#cross-references MUID:87064625; PMID:3785223 !$#accession A24421 !'##molecule_type mRNA !'##residues 1854-2261,'A',2263-2347 ##label BI2 !'##cross-references GB:M13880; NID:g337482; PIDN:AAA36580.1; !1PID:g337483 !'##experimental_source tumor cells !'##note the mcf3 oncogene was formed by DNA rearrangement involving !1fusion of at least three separate segments of DNA GENETICS !$#gene GDB:ROS1 !'##cross-references GDB:120351; OMIM:165020 !$#map_position 6q22-6q22 !$#introns 1853/1; 1881/1; 1926/2; 1980/3; 2002/2; 2045/3; 2078/2; !12145/2; 2190/2 CLASSIFICATION #superfamily kinase-related protein ros; LDL receptor !1YWTD-containing repeat homology; protein kinase homology KEYWORDS ATP; autophosphorylation; glycoprotein; kinase-related !1transforming protein; phosphoprotein; phosphotransferase; !1proto-oncogene; transmembrane protein; tyrosine-specific !1protein kinase FEATURE !$1-36 #domain signal sequence #status predicted #label SIG\ !$37-2347 #product kinase-related protein ROS1 #status !8predicted #label MAT\ !$37-1859 #domain extracellular #status predicted #label EXT\ !$335-378 #domain LDL receptor YWTD-containing repeat homology !8#label YW1\ !$466-503 #domain LDL receptor YWTD-containing repeat homology !8#label YWA\ !$715-757 #domain LDL receptor YWTD-containing repeat homology !8#label YW2\ !$758-798 #domain LDL receptor YWTD-containing repeat homology !8#label YW3\ !$799-838 #domain LDL receptor YWTD-containing repeat homology !8#label YW4\ !$843-888 #domain LDL receptor YWTD-containing repeat homology !8#label YW5\ !$893-933 #domain LDL receptor YWTD-containing repeat homology !8#label YW6\ !$1532-1574 #domain LDL receptor YWTD-containing repeat homology !8#label YW7\ !$1860-1883 #domain transmembrane #status predicted #label TMN\ !$1884-2347 #domain intracellular #status predicted #label INT\ !$1943-2222 #domain protein kinase homology #label KIN\ !$1951-1959 #region protein kinase ATP-binding motif\ !$52,114,123,324,352, !$471,607,628,706, !$714,732,939,961, !$1015,1087,1090, !$1211,1272,1330, !$1458,1461,1474, !$1499,1565,1669, !$1715,1738,1808 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$1980 #active_site Lys #status predicted\ !$2110,2114,2115 #binding_site phosphate (Tyr) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 2347 #molecular-weight 263941 #checksum 5290 SEQUENCE /// ENTRY TVBEI1 #type complete TITLE 44K protein kinase (EC 2.7.1.-) - ictalurid herpesvirus 1 (strain auburn 1) ORGANISM #formal_name ictalurid herpesvirus 1 #note host Ictalurus punctatus (channel catfish) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 11-Jun-1999 ACCESSIONS F36787 REFERENCE A36804 !$#authors Davison, A.J. !$#submission submitted to GenBank, January 1992 !$#description Channel catfish virus: a new type of herpesvirus. !$#accession F36787 !'##molecule_type DNA !'##residues 1-391 ##label DAV !'##cross-references GB:M75136; NID:g331209; PIDN:AAA88117.1; !1PID:g331224 REFERENCE A39447 !$#authors Davison, A.J. !$#journal Virology (1992) 186:9-14 !$#title Channel catfish virus: a new type of herpesvirus. !$#cross-references MUID:92087490; PMID:1727613 !$#contents annotation !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 14 CLASSIFICATION #superfamily ictalurid herpesvirus 44K protein kinase KEYWORDS phosphotransferase; serine/threonine-specific protein kinase SUMMARY #length 391 #molecular-weight 44003 #checksum 765 SEQUENCE /// ENTRY TVBEI2 #type complete TITLE 42.4K protein kinase (EC 2.7.1.-) - ictalurid herpesvirus 1 (strain auburn 1) ORGANISM #formal_name ictalurid herpesvirus 1 #note host Ictalurus punctatus (channel catfish) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 11-Jun-1999 ACCESSIONS G36787 REFERENCE A36804 !$#authors Davison, A.J. !$#submission submitted to GenBank, January 1992 !$#description Channel catfish virus: a new type of herpesvirus. !$#accession G36787 !'##molecule_type DNA !'##residues 1-380 ##label DAV !'##cross-references GB:M75136; NID:g331209; PIDN:AAA88118.1; !1PID:g331225 REFERENCE A39447 !$#authors Davison, A.J. !$#journal Virology (1992) 186:9-14 !$#title Channel catfish virus: a new type of herpesvirus. !$#cross-references MUID:92087490; PMID:1727613 !$#contents annotation !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 15 CLASSIFICATION #superfamily ictalurid herpesvirus 44K protein kinase KEYWORDS phosphotransferase; serine/threonine-specific protein kinase SUMMARY #length 380 #molecular-weight 42419 #checksum 373 SEQUENCE /// ENTRY TVBEI3 #type complete TITLE 42.9K protein kinase (EC 2.7.1.-) - ictalurid herpesvirus 1 (strain auburn 1) ORGANISM #formal_name ictalurid herpesvirus 1 #note host Ictalurus punctatus (channel catfish) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 11-Jun-1999 ACCESSIONS H36787 REFERENCE A36804 !$#authors Davison, A.J. !$#submission submitted to GenBank, January 1992 !$#description Channel catfish virus: a new type of herpesvirus. !$#accession H36787 !'##molecule_type DNA !'##residues 1-387 ##label DAV !'##cross-references GB:M75136; NID:g331209; PIDN:AAA88119.1; !1PID:g331226 REFERENCE A39447 !$#authors Davison, A.J. !$#journal Virology (1992) 186:9-14 !$#title Channel catfish virus: a new type of herpesvirus. !$#cross-references MUID:92087490; PMID:1727613 !$#contents annotation !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 16 CLASSIFICATION #superfamily ictalurid herpesvirus 44K protein kinase KEYWORDS phosphotransferase; serine/threonine-specific protein kinase SUMMARY #length 387 #molecular-weight 42938 #checksum 6645 SEQUENCE /// ENTRY TVBEI5 #type complete TITLE 74.1K protein kinase (EC 2.7.1.-) - ictalurid herpesvirus 1 (strain auburn 1) ORGANISM #formal_name ictalurid herpesvirus 1 #note host Ictalurus punctatus (channel catfish) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 11-Jun-1999 ACCESSIONS I36793 REFERENCE A36804 !$#authors Davison, A.J. !$#submission submitted to GenBank, January 1992 !$#description Channel catfish virus: a new type of herpesvirus. !$#accession I36793 !'##molecule_type DNA !'##residues 1-673 ##label DAV !'##cross-references GB:M75136; NID:g331209; PIDN:AAA88176.1; !1PID:g331282 REFERENCE A39447 !$#authors Davison, A.J. !$#journal Virology (1992) 186:9-14 !$#title Channel catfish virus: a new type of herpesvirus. !$#cross-references MUID:92087490; PMID:1727613 !$#contents annotation !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 74 CLASSIFICATION #superfamily ictalurid herpesvirus 74.1K protein kinase; !1protein kinase homology KEYWORDS ATP; phosphotransferase; serine/threonine-specific protein !1kinase FEATURE !$124-375 #domain protein kinase homology #label KIN SUMMARY #length 673 #molecular-weight 74132 #checksum 4789 SEQUENCE /// ENTRY TVBEI4 #type complete TITLE 106.6K protein kinase (EC 2.7.1.-) - ictalurid herpesvirus 1 (strain auburn 1) ORGANISM #formal_name ictalurid herpesvirus 1 #note host Ictalurus punctatus (channel catfish) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 11-Jun-1999 ACCESSIONS H36793 REFERENCE A36804 !$#authors Davison, A.J. !$#submission submitted to GenBank, January 1992 !$#description Channel catfish virus: a new type of herpesvirus. !$#accession H36793 !'##molecule_type DNA !'##residues 1-962 ##label DAV !'##cross-references GB:M75136; NID:g331209; PIDN:AAA88175.1; !1PID:g331281 REFERENCE A39447 !$#authors Davison, A.J. !$#journal Virology (1992) 186:9-14 !$#title Channel catfish virus: a new type of herpesvirus. !$#cross-references MUID:92087490; PMID:1727613 !$#contents annotation !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 73 CLASSIFICATION #superfamily ictalurid herpesvirus 74.1K protein kinase; !1protein kinase homology KEYWORDS ATP; phosphotransferase; serine/threonine-specific protein !1kinase FEATURE !$299-567 #domain protein kinase homology #label KIN\ !$307-315 #region protein kinase ATP-binding motif\ !$324 #active_site Lys #status predicted SUMMARY #length 962 #molecular-weight 106567 #checksum 3482 SEQUENCE /// ENTRY JQ1677 #type complete TITLE S-receptor kinase (EC 2.7.1.-) precursor - rape ORGANISM #formal_name Brassica napus #common_name rape DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 11-Jun-1999 ACCESSIONS JQ1677 REFERENCE JQ1677 !$#authors Goring, D.R.; Rothstein, S.J. !$#journal Plant Cell (1992) 4:1273-1281 !$#title The S-locus receptor kinase gene in a self-incompatible !1Brassica napus line encodes a functional serine/threonine !1kinase. !$#cross-references MUID:93076111; PMID:1332796 !$#accession JQ1677 !'##molecule_type mRNA !'##residues 1-858 ##label GOR !'##cross-references GB:M97667; NID:g167180; PIDN:AAA33008.1; !1PID:g167181 !'##experimental_source subspecies oleifera, cv. Westar GENETICS !$#gene SRK !$#note locus is highly polymorphic FUNCTION !$#description involved in preventing fertilization between plants having !1the same S-locus genotypes CLASSIFICATION #superfamily S-receptor kinase; protein kinase homology; !1S-locus-specific glycoprotein homology KEYWORDS ATP; glycoprotein; magnesium; phosphotransferase; receptor; !1serine/threonine-specific protein kinase; signal !1transduction; transmembrane protein FEATURE !$1-31 #domain signal sequence #status predicted #label SIG\ !$32-858 #product S-receptor kinase #status predicted #label !8MAT\ !$42-437 #domain S-locus-specific glycoprotein homology #label !8SSG\ !$448-467 #domain transmembrane #status predicted #label TMM\ !$527-814 #domain protein kinase homology #label KIN\ !$535-543 #region protein kinase ATP-binding motif\ !$48,116,123,152,248, !$393 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$557,573,654,656 #active_site Lys, Glu, Asp, Lys #status predicted\ !$659,663 #binding_site magnesium (Asn, Asp) #status predicted SUMMARY #length 858 #molecular-weight 97908 #checksum 5111 SEQUENCE /// ENTRY S31429 #type complete TITLE S-receptor kinase (EC 2.7.1.-) precursor - wild cabbage ORGANISM #formal_name Brassica oleracea #common_name wild cabbage DATE 13-Jan-1995 #sequence_revision 13-Jan-1995 #text_change 08-Dec-2000 ACCESSIONS S31429; S39913 REFERENCE S31429 !$#authors Oldknow, J.; Franklin, T.M.; Trick, M. !$#submission submitted to the EMBL Data Library, December 1992 !$#description An unusual SLG/SRK gene pair linked to the S-locus of a !1self-incompatible Brassica line. !$#accession S31429 !'##status preliminary !'##molecule_type DNA !'##residues 1-857 ##label OLD !'##cross-references EMBL:Z18921; NID:g17908; PIDN:CAA79355.1; !1PID:g17909 REFERENCE S39908 !$#authors Kumar, V.; Trick, M. !$#journal Mol. Gen. Genet. (1993) 241:440-446 !$#title Sequence complexity of the S receptor kinase gene family in !1Brassica. !$#cross-references MUID:94067027; PMID:8246898 !$#accession S39913 !'##molecule_type DNA !'##residues 559-708 ##label KUM GENETICS !$#gene SRK !$#introns 439/1; 482/1; 545/3; 615/1; 694/2; 744/3 !$#note locus is highly polymorphic FUNCTION !$#description involved in preventing fertilization between plants having !1the same S-locus genotypes CLASSIFICATION #superfamily S-receptor kinase; protein kinase homology; !1S-locus-specific glycoprotein homology KEYWORDS ATP; glycoprotein; magnesium; phosphotransferase; receptor; !1serine/threonine-specific protein kinase; signal !1transduction; transmembrane protein FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-857 #product S-receptor kinase #status predicted #label !8MAT\ !$37-437 #domain S-locus-specific glycoprotein homology #label !8SSG\ !$448-467 #domain transmembrane #status predicted #label TMM\ !$527-813 #domain protein kinase homology #label KIN\ !$535-543 #region protein kinase ATP-binding motif\ !$43,114,121,216,262, !$316,391 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$556,572,653,655 #active_site Lys, Glu, Asp, Lys #status predicted\ !$658,662 #binding_site magnesium (Asn, Asp) #status predicted SUMMARY #length 857 #molecular-weight 97596 #checksum 8943 SEQUENCE /// ENTRY JC2482 #type fragment TITLE S-receptor kinase (EC 2.7.1.-) 12 precursor - field mustard (fragment) ALTERNATE_NAMES receptor protein kinase K, SRK12 ORGANISM #formal_name Brassica campestris #common_name field mustard DATE 22-Apr-1995 #sequence_revision 01-Aug-1997 #text_change 26-Feb-1999 ACCESSIONS JC2482 REFERENCE JC2481 !$#authors Yamakawa, S.; Watanabe, M.; Hinata, K.; Suzuki, A.; Isogai, !1A. !$#journal Biosci. Biotechnol. Biochem. (1995) 59:161-162 !$#title The sequences of S-receptor kinase (SRK) involved in !1self-incompatibility and their homologies to S-locus !1glycoproteins of Brassica campestris. !$#cross-references MUID:95201375; PMID:7765971 !$#accession JC2482 !'##molecule_type mRNA !'##residues 1-856 ##label YAM !'##cross-references DDBJ:D38564 GENETICS !$#gene SRK !$#note locus is highly polymorphic FUNCTION !$#description involved in preventing fertilization between plants having !1the same S-locus genotypes CLASSIFICATION #superfamily S-receptor kinase; protein kinase homology; !1S-locus-specific glycoprotein homology KEYWORDS ATP; glycoprotein; magnesium; phosphotransferase; receptor; !1serine/threonine-specific protein kinase; signal !1transduction; transmembrane protein FEATURE !$1-31 #domain signal sequence (fragment) #status predicted !8#label SIG\ !$32-856 #product S-receptor kinase 12 #status predicted !8#label MAT\ !$42-436 #domain S-locus-specific glycoprotein homology #label !8SSG\ !$447-466 #domain transmembrane #status predicted #label TMM\ !$526-812 #domain protein kinase homology #label KIN\ !$534-542 #region protein kinase ATP-binding motif\ !$48,79,123,217,247, !$317,392 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$555,571,652,654 #active_site Lys, Glu, Asp, Lys #status predicted\ !$657,661 #binding_site magnesium (Asn, Asp) #status predicted SUMMARY #length 856 #checksum 5637 SEQUENCE /// ENTRY JC2481 #type complete TITLE S-receptor kinase (EC 2.7.1.-) 8 precursor - field mustard ALTERNATE_NAMES receptor protein kinase 8, 5RK 8 ORGANISM #formal_name Brassica campestris #common_name field mustard DATE 22-Apr-1995 #sequence_revision 26-May-1995 #text_change 16-Jun-2000 ACCESSIONS JC2481 REFERENCE JC2481 !$#authors Yamakawa, S.; Watanabe, M.; Hinata, K.; Suzuki, A.; Isogai, !1A. !$#journal Biosci. Biotechnol. Biochem. (1995) 59:161-162 !$#title The sequences of S-receptor kinase (SRK) involved in !1self-incompatibility and their homologies to S-locus !1glycoproteins of Brassica campestris. !$#cross-references MUID:95201375; PMID:7765971 !$#accession JC2481 !'##molecule_type mRNA !'##residues 1-858 ##label YAM !'##cross-references DDBJ:D38563; NID:g757504; PIDN:BAA07576.1; !1PID:g757505 GENETICS !$#gene SRK !$#note locus is highly polymorphic FUNCTION !$#description involved in preventing fertilization between plants having !1the same S-locus genotypes CLASSIFICATION #superfamily S-receptor kinase; protein kinase homology; !1S-locus-specific glycoprotein homology KEYWORDS ATP; glycoprotein; magnesium; phosphotransferase; receptor; !1serine/threonine-specific protein kinase; signal !1transduction; transmembrane protein FEATURE !$1-29 #domain signal sequence #status predicted #label SIG\ !$30-858 #product S-receptor kinase 8 #status predicted #label !8MAT\ !$40-433 #domain S-locus-specific glycoprotein homology #label !8SSG\ !$444-468 #domain transmembrane #status predicted #label TMM\ !$528-814 #domain protein kinase homology #label KIN\ !$536-544 #region protein kinase ATP-binding motif\ !$46,95,114,121,245, !$261,314,389 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$557,573,654,656 #active_site Lys, Glu, Asp, Lys #status predicted\ !$659,663 #binding_site magnesium (Asn, Asp) #status predicted SUMMARY #length 858 #molecular-weight 97884 #checksum 5127 SEQUENCE /// ENTRY A41369 #type complete TITLE S-receptor kinase (EC 2.7.1.-) 6 precursor - wild cabbage ORGANISM #formal_name Brassica oleracea #common_name wild cabbage DATE 12-Jun-1992 #sequence_revision 12-Jun-1992 #text_change 11-Jun-1999 ACCESSIONS A41369 REFERENCE A41369 !$#authors Stein, J.C.; Howlett, B.; Boyes, D.C.; Nasrallah, M.E.; !1Nasrallah, J.B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:8816-8820 !$#title Molecular cloning of a putative receptor protein kinase gene !1encoded at the self-incompatibility locus of Brassica !1oleracea. !$#cross-references MUID:92020942; PMID:1681543 !$#accession A41369 !'##molecule_type DNA !'##residues 1-857 ##label STE !'##cross-references GB:M76647; NID:g167166; PIDN:AAA33000.1; !1PID:g167167 !'##experimental_source S6S6 homozygote kale GENETICS !$#gene SRK !$#note locus is highly polymorphic FUNCTION !$#description involved in preventing fertilization between plants having !1the same S-locus genotypes CLASSIFICATION #superfamily S-receptor kinase; protein kinase homology; !1S-locus-specific glycoprotein homology KEYWORDS ATP; glycoprotein; magnesium; phosphotransferase; receptor; !1serine/threonine-specific protein kinase; signal !1transduction; transmembrane protein FEATURE !$1-30 #domain signal sequence #status predicted #label SIG\ !$31-857 #product S-receptor kinase #status predicted #label !8MAT\ !$41-436 #domain S-locus-specific glycoprotein homology #label !8SSG\ !$447-466 #domain transmembrane #status predicted #label TMM\ !$526-813 #domain protein kinase homology #label KIN\ !$534-542 #region protein kinase ATP-binding motif\ !$47,120,196,260,314, !$389,442 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$556,572,653,655 #active_site Lys, Glu, Asp, Lys #status predicted\ !$658,662 #binding_site magnesium (Asn, Asp) #status predicted SUMMARY #length 857 #molecular-weight 98077 #checksum 5319 SEQUENCE /// ENTRY S51527 #type complete TITLE S-receptor kinase (EC 2.7.1.-) A14 precursor - rape ORGANISM #formal_name Brassica napus #common_name rape DATE 19-Mar-1997 #sequence_revision 19-Mar-1997 #text_change 11-Jun-1999 ACCESSIONS S51527 REFERENCE S51527 !$#authors Glavin, T.L.; Goring, D.R.; Schafer, U.; Rothstein, S.J. !$#journal Mol. Gen. Genet. (1994) 244:630-637 !$#title Features of the extracellular domain of the S-locus receptor !1kinase from Brassica. !$#cross-references MUID:95058917; PMID:7969032 !$#accession S51527 !'##molecule_type mRNA !'##residues 1-849 ##label GLA !'##cross-references EMBL:U00443; NID:g392556; PIDN:AAA62232.1; !1PID:g392557 !'##experimental_source subspecies oleifera, cv. T2 GENETICS !$#gene SRK !$#note locus is highly polymorphic FUNCTION !$#description involved in preventing fertilization between plants having !1the same S-locus genotypes CLASSIFICATION #superfamily S-receptor kinase; protein kinase homology; !1S-locus-specific glycoprotein homology KEYWORDS ATP; glycoprotein; magnesium; phosphotransferase; receptor; !1serine/threonine-specific protein kinase; signal !1transduction; transmembrane protein FEATURE !$1-30 #domain signal sequence #status predicted #label SIG\ !$31-849 #product S-receptor kinase #status predicted #label !8MAT\ !$41-433 #domain S-locus-specific glycoprotein homology #label !8SSG\ !$444-463 #domain transmembrane #status predicted #label TMN\ !$523-805 #domain protein kinase homology #label KIN\ !$531-539 #region protein kinase ATP-binding motif\ !$47,113,120,244,260, !$389 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$553,569,650,652 #active_site Lys, Glu, Asp, Lys #status predicted\ !$655,659 #binding_site magnesium (Asn, Asp) #status predicted SUMMARY #length 849 #molecular-weight 96292 #checksum 3095 SEQUENCE /// ENTRY S70769 #type complete TITLE S-receptor kinase (EC 2.7.1.-) Ark1 precursor - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 28-Oct-1996 #sequence_revision 27-Feb-1997 #text_change 11-Jun-1999 ACCESSIONS S70769; S71184 REFERENCE S70769 !$#authors Tobias, C.M.; Howlett, B.; Nasrallah, J.B. !$#submission submitted to the EMBL Data Library, January 1992 !$#description An Arabidopsis thaliana gene with sequence similarity to the !1S-locus receptor kinase of Brassica oleracea: Sequence and !1expression. !$#accession S70769 !'##molecule_type DNA !'##residues 1-843 ##label TOB !'##cross-references EMBL:M80238; NID:g166691; PIDN:AAA32786.1; !1PID:g166692 !'##experimental_source strain Columbia GENETICS !$#introns 427/1; 472/1; 535/3; 606/1; 685/2; 735/3 CLASSIFICATION #superfamily S-receptor kinase; protein kinase homology; !1S-locus-specific glycoprotein homology KEYWORDS ATP; glycoprotein; magnesium; phosphotransferase; receptor; !1serine/threonine-specific protein kinase; signal !1transduction; transmembrane protein FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-843 #product S-receptor kinase #status predicted #label !8MAT\ !$35-425 #domain S-locus-specific glycoprotein homology #label !8SSG\ !$436-457 #domain transmembrane #status predicted #label TMM\ !$517-801 #domain protein kinase homology #label KIN\ !$525-533 #region protein kinase ATP-binding motif\ !$41,92,116,236,381 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$547,563,644,646 #active_site Lys, Glu, Asp, Lys #status predicted\ !$649,653 #binding_site magnesium (Asn, Asp) #status predicted SUMMARY #length 843 #molecular-weight 95945 #checksum 1976 SEQUENCE /// ENTRY T05180 #type complete TITLE S-receptor kinase (EC 2.7.1.-) ARK3 precursor - Arabidopsis thaliana ALTERNATE_NAMES protein T6K22.110 ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 13-Aug-1999 #sequence_revision 13-Aug-1999 #text_change 13-Aug-1999 ACCESSIONS T05180 REFERENCE Z15400 !$#authors Bevan, M.; Peters, S.A.; van Staveren, M.; Dirkse, W.; !1Stiekema, W.; Bancroft, I.; Mewes, H.W.; Mayer, K.F.X.; !1Schueller, C. !$#submission submitted to the Protein Sequence Database, August 1998 !$#accession T05180 !'##molecule_type DNA !'##residues 1-850 ##label BEV !'##cross-references EMBL:AL031187 !'##experimental_source cultivar Columbia; BAC clone T6K22 GENETICS !$#gene ARK3 !$#map_position 4 !$#introns 433/1; 478/1; 542/3; 613/1; 692/2; 742/3 !$#note T6K22.110 FUNCTION !$#description involved in preventing fertilization between plants having !1the same S-locus genotypes CLASSIFICATION #superfamily S-receptor kinase; protein kinase homology; !1S-locus-specific glycoprotein homology KEYWORDS ATP; glycoprotein; magnesium; phosphotransferase; receptor; !1serine/threonine-specific protein kinase; signal !1transduction; transmembrane protein FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-850 #product S-receptor kinase #status predicted #label !8MAT\ !$37-431 #domain S-locus-specific glycoprotein homology #label !8SSG\ !$442-463 #domain transmembrane #status predicted #label TMM\ !$524-807 #domain protein kinase homology #label KIN\ !$532-540 #region protein kinase ATP-binding motif\ !$43,118,242,311,387, !$437 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$554,570,651,653 #active_site Lys, Glu, Asp, Lys #status predicted\ !$656,660 #binding_site magnesium (Asn, Asp) #status predicted SUMMARY #length 850 #molecular-weight 96465 #checksum 898 SEQUENCE /// ENTRY T05179 #type complete TITLE S-receptor kinase (EC 2.7.1.-) T6K22.100 precursor - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 13-Aug-1999 #sequence_revision 13-Aug-1999 #text_change 13-Aug-1999 ACCESSIONS T05179 REFERENCE Z15400 !$#authors Bevan, M.; Peters, S.A.; van Staveren, M.; Dirkse, W.; !1Stiekema, W.; Bancroft, I.; Mewes, H.W.; Mayer, K.F.X.; !1Schueller, C. !$#submission submitted to the Protein Sequence Database, August 1998 !$#accession T05179 !'##molecule_type DNA !'##residues 1-844 ##label BEV !'##cross-references EMBL:AL031187 !'##experimental_source cultivar Columbia; BAC clone T6K22 GENETICS !$#map_position 4 !$#introns 433/1; 478/1; 540/3; 603/1; 683/2; 733/3 !$#note T6K22.100 FUNCTION !$#description involved in preventing fertilization between plants having !1the same S-locus genotypes CLASSIFICATION #superfamily S-receptor kinase; protein kinase homology; !1S-locus-specific glycoprotein homology KEYWORDS ATP; glycoprotein; magnesium; phosphotransferase; receptor; !1serine/threonine-specific protein kinase; signal !1transduction; transmembrane protein FEATURE !$1-29 #domain signal sequence #status predicted #label SIG\ !$30-844 #product S-receptor kinase #status predicted #label !8MAT\ !$40-431 #domain S-locus-specific glycoprotein homology #label !8SSG\ !$442-463 #domain transmembrane #status predicted #label TMM\ !$522-801 #domain protein kinase homology #label KIN\ !$530-538 #region protein kinase ATP-binding motif\ !$46,120,147,243,387 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$544,560,642,644 #active_site Lys, Glu, Asp, Lys #status predicted\ !$647,651 #binding_site magnesium (Asn, Asp) #status predicted SUMMARY #length 844 #molecular-weight 96262 #checksum 4061 SEQUENCE /// ENTRY T05753 #type complete TITLE S-receptor kinase (EC 2.7.1.-) M4I22.100 precursor - Arabidopsis thaliana ALTERNATE_NAMES protein M4I22.100 ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 13-Aug-1999 #sequence_revision 13-Aug-1999 #text_change 13-Aug-1999 ACCESSIONS T05753 REFERENCE Z15450 !$#authors Bevan, M.; Reichert, B.J.; Barel, E.; Hoheisel, J.; Mewes, !1H.W.; Mayer, K.F.X.; Schueller, C. !$#submission submitted to the Protein Sequence Database, June 1998 !$#accession T05753 !'##status preliminary !'##molecule_type DNA !'##residues 1-772 ##label BEV !'##cross-references EMBL:AL030978 !'##experimental_source cultivar Columbia; BAC clone M4I22 GENETICS !$#map_position 4 !$#introns 43/1; 418/1; 470/3; 620/2; 670/3 !$#note M4I22.100 FUNCTION !$#description involved in preventing fertilization between plants having !1the same S-locus genotypes CLASSIFICATION #superfamily S-receptor kinase; protein kinase homology; !1S-locus-specific glycoprotein homology KEYWORDS ATP; glycoprotein; magnesium; phosphotransferase; receptor; !1serine/threonine-specific protein kinase; signal !1transduction; transmembrane protein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$21-772 #product S-receptor kinase M4I22.100 #status !8predicted #label MAT\ !$30-416 #domain S-locus-specific glycoprotein homology #label !8SSG\ !$452-733 #domain protein kinase homology #label KIN\ !$460-468 #region protein kinase ATP-binding motif\ !$30,84,178,370 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$482,498,579,581 #active_site Lys, Glu, Asp, Lys #status predicted\ !$584,588 #binding_site magnesium (Asn, Asp) #status predicted SUMMARY #length 772 #molecular-weight 87810 #checksum 6445 SEQUENCE /// ENTRY T05754 #type complete TITLE S-receptor kinase (EC 2.7.1.-) M4I22.110 precursor - Arabidopsis thaliana ALTERNATE_NAMES protein M4I22.110 ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 13-Aug-1999 #sequence_revision 13-Aug-1999 #text_change 13-Aug-1999 ACCESSIONS T05754 REFERENCE Z15450 !$#authors Bevan, M.; Reichert, B.J.; Barel, E.; Hoheisel, J.; Mewes, !1H.W.; Mayer, K.F.X.; Schueller, C. !$#submission submitted to the Protein Sequence Database, June 1998 !$#accession T05754 !'##status preliminary !'##molecule_type DNA !'##residues 1-815 ##label BEV !'##cross-references EMBL:AL030978 !'##experimental_source cultivar Columbia; BAC clone M4I22 GENETICS !$#map_position 4 !$#introns 471/1; 516/3; 587/1; 666/2; 716/3 !$#note M4I22.110 FUNCTION !$#description involved in preventing fertilization between plants having !1the same S-locus genotypes CLASSIFICATION #superfamily S-receptor kinase; protein kinase homology; !1S-locus-specific glycoprotein homology KEYWORDS ATP; glycoprotein; magnesium; phosphotransferase; receptor; !1serine/threonine-specific protein kinase; signal !1transduction; transmembrane protein FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-815 #product S-receptor kinase #status predicted #label !8MAT\ !$33-431 #domain S-locus-specific glycoprotein homology #label !8SSG\ !$442-461 #domain transmembrane #status predicted #label TMM\ !$498-778 #domain protein kinase homology #label KIN\ !$506-514 #region protein kinase ATP-binding motif\ !$93,249,265,385 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$528,544,625,627 #active_site Lys, Glu, Asp, Lys #status predicted\ !$630,634 #binding_site magnesium (Asn, Asp) #status predicted SUMMARY #length 815 #molecular-weight 91874 #checksum 1614 SEQUENCE /// ENTRY T05181 #type complete TITLE S-receptor kinase (EC 2.7.1.-) T6K22.120 precursor - Arabidopsis thaliana ALTERNATE_NAMES protein F18E5.10; protein T6K22.120 ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 16-Jul-1999 #sequence_revision 16-Jul-1999 #text_change 13-Aug-1999 ACCESSIONS T05181; T05147 REFERENCE Z15400 !$#authors Bevan, M.; Peters, S.A.; van Staveren, M.; Dirkse, W.; !1Stiekema, W.; Bancroft, I.; Mewes, H.W.; Mayer, K.F.X.; !1Schueller, C. !$#submission submitted to the Protein Sequence Database, August 1998 !$#accession T05181 !'##molecule_type DNA !'##residues 1-849 ##label BEV !'##cross-references EMBL:AL031187 !'##experimental_source cultivar Columbia; BAC clone T6K22 !$#accession T05147 !'##molecule_type DNA !'##residues 1-693 ##label BE2 !'##cross-references EMBL:ALO22603 !'##experimental_source cultivar Columbia; BAC clone F18E5 GENETICS !$#map_position 4 !$#introns 467/1; 545/3; 616/1; 695/2; 744/3 !$#note T6K22.120; F18E5.10 FUNCTION !$#description involved in preventing fertilization between plants having !1the same S-locus genotypes CLASSIFICATION #superfamily S-receptor kinase; protein kinase homology; !1S-locus-specific glycoprotein homology KEYWORDS ATP; glycoprotein; magnesium; phosphotransferase; receptor; !1serine/threonine-specific protein kinase; signal !1transduction; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-849 #product S-receptor kinase T6K22.120 #status !8predicted #label MAT\ !$34-430 #domain S-locus-specific glycoprotein homology #label !8SSG\ !$439-460 #domain transmembrane #status predicted #label TMM\ !$527-806 #domain protein kinase homology #label KIN\ !$535-543 #region protein kinase ATP-binding motif\ !$110,191,210,230, !$273,282,333,349 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$557,573,654,656 #active_site Lys, Glu, Asp, Lys #status predicted\ !$659,663 #binding_site magnesium (Asn, Asp) #status predicted SUMMARY #length 849 #molecular-weight 95167 #checksum 5516 SEQUENCE /// ENTRY T02053 #type complete TITLE S-receptor kinase (EC 2.7.1.-) KIK1 precursor - maize ALTERNATE_NAMES KI domain interacting kinase 1 ORGANISM #formal_name Zea mays #common_name maize DATE 13-Aug-1999 #sequence_revision 13-Aug-1999 #text_change 20-Aug-1999 ACCESSIONS T02053 REFERENCE Z14523 !$#authors Braun, D.M.; Stone, J.M.; Walker, J.C. !$#submission submitted to the EMBL Data Library, December 1996 !$#description Multiple receptor-like protein kinases interact with the KI !1domain of KAPP: implications for transmembrane signaling in !1plants. !$#accession T02053 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-848 ##label BRA !'##cross-references EMBL:U82481; NID:g2735016; PIDN:AAB93834.1; !1PID:g2735017 !'##experimental_source strain B73 GENETICS !$#gene KIK1 FUNCTION !$#description involved in preventing fertilization between plants having !1the same S-locus genotypes CLASSIFICATION #superfamily S-receptor kinase; protein kinase homology; !1S-locus-specific glycoprotein homology KEYWORDS ATP; glycoprotein; magnesium; phosphotransferase; receptor; !1serine/threonine-specific protein kinase; signal !1transduction; transmembrane protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-848 #product S-receptor kinase KIK1 #status predicted !8#label MAT\ !$33-435 #domain S-locus-specific glycoprotein homology #label !8SSG\ !$444-465 #domain transmembrane #status predicted #label TMM\ !$528-808 #domain protein kinase homology #label KIN\ !$536-544 #region protein kinase ATP-binding motif\ !$111,123,218,263, !$274,340,356,393 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$558,574,655,657 #active_site Lys, Glu, Asp, Lys #status predicted\ !$660,664 #binding_site magnesium (Asn, Asp) #status predicted SUMMARY #length 848 #molecular-weight 94065 #checksum 5391 SEQUENCE /// ENTRY T09349 #type complete TITLE S-receptor kinase (EC 2.7.1.-) T26M18.110 precursor - Arabidopsis thaliana ALTERNATE_NAMES KI domain interacting kinase 1-like protein; protein T26M18.110 ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 13-Aug-1999 #sequence_revision 13-Aug-1999 #text_change 15-Oct-1999 ACCESSIONS T09349 REFERENCE Z16650 !$#authors Bevan, M.; Hilbert, H.; Braun, M.; Holzer, E.; Brandt, A.; !1Duesterhoeft, A.; Bancroft, I.; Mewes, H.W.; Mayer, K.F.X.; !1Lemcke, K.; Schueller, C. !$#submission submitted to the Protein Sequence Database, June 1999 !$#accession T09349 !'##molecule_type DNA !'##residues 1-849 ##label BEV !'##cross-references EMBL:AL078606; ATSP:T26M18.110; GSPDB:GN00062 !'##experimental_source cultivar Columbia; BAC clone T26M18 GENETICS !$#gene ATSP:T26M18.110 !$#map_position 4 !$#introns 457/1; 502/1; 553/3; 624/1; 703/2; 753/3 FUNCTION !$#description involved in preventing fertilization between plants having !1the same S-locus genotypes CLASSIFICATION #superfamily S-receptor kinase; protein kinase homology; !1S-locus-specific glycoprotein homology KEYWORDS ATP; glycoprotein; magnesium; phosphotransferase; receptor; !1serine/threonine-specific protein kinase; signal !1transduction; transmembrane protein FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-849 #product S-receptor kinase T26M18.110 #status !8predicted #label MAT\ !$35-450 #domain S-locus-specific glycoprotein homology #label !8SSG\ !$467-484 #domain transmembrane #status predicted #label TMM\ !$535-814 #domain protein kinase homology #label KIN\ !$543-551 #region protein kinase ATP-binding motif\ !$111,148,172,232,450 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$565,581,662,664 #active_site Lys, Glu, Asp, Lys #status predicted\ !$667,671 #binding_site magnesium (Asn, Asp) #status predicted SUMMARY #length 849 #molecular-weight 95815 #checksum 84 SEQUENCE /// ENTRY T00534 #type complete TITLE S-receptor kinase (EC 2.7.1.-) T20K24.15 precursor - Arabidopsis thaliana ALTERNATE_NAMES protein T20K24.15 ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 13-Aug-1999 #sequence_revision 13-Aug-1999 #text_change 02-Mar-2001 ACCESSIONS T00534; H84572 REFERENCE Z14167 !$#authors Rounsley, S.D.; Kaul, S.; Lin, X.; Ketchum, K.A.; Crosby, !1M.L.; Brandon, R.C.; Sykes, S.M.; Mason, T.M.; Kerlavage, !1A.R.; Adams, M.D.; Somerville, C.R.; Venter, J.C. !$#submission submitted to the EMBL Data Library, July 1997 !$#description Arabidopsis thaliana chromosome II BAC T20K24 genomic !1sequence. !$#accession T00534 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-828 ##label ROU !'##cross-references EMBL:AC002392; NID:g3176701; PIDN:AAD12030.1; !1PID:g3176715 !'##experimental_source cultivar Columbia REFERENCE A84420 !$#authors Lin, X.; Kaul, S.; Rounsley, S.D.; Shea, T.P.; Benito, M.I.; !1Town, C.D.; Fujii, C.Y.; Mason, T.M.; Bowman, C.L.; !1Barnstead, M.E.; Feldblyum, T.V.; Buell, C.R.; Ketchum, !1K.A.; Lee, J.J.; Ronning, C.M.; Koo, H.; Moffat, K.S.; !1Cronin, L.A.; Shen, M.; VanAken, S.E.; Umayam, L.; Tallon, !1L.J.; Gill, J.E.; Adams, M.D.; Carrera, A.J.; Creasy, T.H.; !1Goodman, H.M.; Somerville, C.R.; Copenhaver, G.P.; Preuss, !1D.; Nierman, W.C.; White, O.; Eisen, J.A.; Salzberg, S.L.; !1Fraser, C.M.; Venter, J.C. !$#journal Nature (1999) 402:761-768 !$#title Sequence and analysis of chromosome 2 of the plant !1Arabidopsis thaliana. !$#cross-references MUID:20083487; PMID:10617197 !$#accession H84572 !'##status preliminary !'##molecule_type DNA !'##residues 1-828 ##label STO !'##cross-references GB:AE002093; NID:g3176715; PIDN:AAD12030.1; !1GSPDB:GN00139 GENETICS !$#gene T20K24.15; At2g19130 !$#map_position 2 FUNCTION !$#description involved in preventing fertilization between plants having !1the same S-locus genotypes CLASSIFICATION #superfamily S-receptor kinase; protein kinase homology; !1S-locus-specific glycoprotein homology KEYWORDS ATP; glycoprotein; magnesium; phosphotransferase; receptor; !1serine/threonine-specific protein kinase; signal !1transduction; transmembrane protein FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-828 #product S-receptor kinase T20K24.15 #status !8predicted #label MAT\ !$31-425 #domain S-locus-specific glycoprotein homology #label !8SSG\ !$440-463 #domain transmembrane #status predicted #label TMM\ !$493-772 #domain protein kinase homology #label KIN\ !$499-507 #region protein kinase ATP-binding motif\ !$85,113,203,234,240, !$255 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$521,536,619,621 #active_site Lys, Glu, Asp, Lys #status predicted\ !$624,628 #binding_site magnesium (Asn, Asp) #status predicted SUMMARY #length 828 #molecular-weight 92342 #checksum 1675 SEQUENCE /// ENTRY T02753 #type complete TITLE S-receptor kinase (EC 2.7.1.-) PK3 precursor - maize ORGANISM #formal_name Zea mays #common_name maize DATE 13-Aug-1999 #sequence_revision 13-Aug-1999 #text_change 16-Jun-2000 ACCESSIONS T02753 REFERENCE Z14719 !$#authors Zhang, R.; Xia, J.; Cook, S.; Pryor, A.J. !$#submission submitted to the EMBL Data Library, August 1998 !$#description Cloning of a S-domain RLK gene in Zea mays. !$#accession T02753 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-826 ##label ZHA !'##cross-references EMBL:AJ010166; PIDN:CAA09029.1 !'##experimental_source cultivar B73; seed GENETICS !$#gene pk3 FUNCTION !$#description involved in preventing fertilization between plants having !1the same S-locus genotypes CLASSIFICATION #superfamily S-receptor kinase; protein kinase homology; !1S-locus-specific glycoprotein homology KEYWORDS ATP; glycoprotein; magnesium; phosphotransferase; receptor; !1serine/threonine-specific protein kinase; signal !1transduction; transmembrane protein FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-826 #product S-receptor kinase T20K24.15 #status !8predicted #label MAT\ !$29-432 #domain S-locus-specific glycoprotein homology #label !8SSG\ !$442-465 #domain transmembrane #status predicted #label TMM\ !$498-772 #domain protein kinase homology #label KIN\ !$504-512 #region protein kinase ATP-binding motif\ !$25,55,119,125,144, !$169,209,244,348, !$389,398 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$526,541,621,623 #active_site Lys, Glu, Asp, Lys #status predicted\ !$626,630 #binding_site magnesium (Asn, Asp) #status predicted SUMMARY #length 826 #molecular-weight 90631 #checksum 9970 SEQUENCE /// ENTRY S10930 #type complete TITLE S-receptor kinase (EC 2.7.1.-) homolog PK1 precursor - maize ORGANISM #formal_name Zea mays #common_name maize DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S10930; S16634; S33532; S29624 REFERENCE S10930 !$#authors Walker, J.C.; Zhang, R. !$#journal Nature (1990) 345:743-746 !$#title Relationship of a putative receptor protein kinase from !1maize to the S-locus glycoproteins of Brassica. !$#cross-references MUID:90294911; PMID:2163028 !$#accession S10930 !'##molecule_type mRNA !'##residues 1-817 ##label WAL1 !'##cross-references EMBL:X52384; NID:g22431; PIDN:CAA36611.1; !1PID:g22432 REFERENCE S16634 !$#authors Walker, J.C. !$#submission submitted to the EMBL Data Library, April 1990 !$#accession S16634 !'##molecule_type mRNA !'##residues 1-78,'P',80-817 ##label WAL !'##cross-references EMBL:X52384 REFERENCE S33532 !$#authors Zhang, R.; Walker, J.C. !$#journal Plant Mol. Biol. (1993) 21:1171-1174 !$#title Structure and expression of the S locus-related genes of !1maize. !$#cross-references MUID:93257631; PMID:8490135 !$#accession S33532 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-78,'P',80-119,'G',122-817 ##label ZHA !'##cross-references EMBL:X67733 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1992 CLASSIFICATION #superfamily S-receptor kinase; protein kinase homology; !1S-locus-specific glycoprotein homology KEYWORDS ATP; glycoprotein; magnesium; phosphotransferase; receptor; !1serine/threonine-specific protein kinase; signal !1transduction; transmembrane protein FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-817 #product S-receptor kinase homolog PK1 #status !8predicted #label MAT\ !$39-426 #domain S-locus-specific glycoprotein homology #label !8SSG\ !$480-498 #domain transmembrane #status predicted #label TMN\ !$534-817 #domain protein kinase homology #label KIN\ !$540-548 #region protein kinase ATP-binding motif\ !$83,128,228,279,329, !$339 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$562,577,658,660 #active_site Lys, Glu, Asp, Lys #status predicted\ !$663,667 #binding_site magnesium (Asn, Asp) #status predicted SUMMARY #length 817 #molecular-weight 91119 #checksum 6302 SEQUENCE /// ENTRY S27754 #type complete TITLE S-receptor kinase (EC 2.7.1.-) homolog 2 precursor - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S27754 REFERENCE S27754 !$#authors Walker, J.C. !$#submission submitted to the EMBL Data Library, February 1992 !$#description Receptor-like protein kinase genes of Arabidopsis thaliana. !$#accession S27754 !'##molecule_type mRNA !'##residues 1-832 ##label WAL !'##cross-references EMBL:M84658; NID:g166845; PIDN:AAA32857.1; !1PID:g166846 CLASSIFICATION #superfamily S-receptor kinase; protein kinase homology; !1S-locus-specific glycoprotein homology KEYWORDS ATP; glycoprotein; magnesium; phosphotransferase; receptor; !1serine/threonine-specific protein kinase; signal !1transduction; transmembrane protein FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-832 #product S-receptor kinase homolog 2 #status !8predicted #label MAT\ !$37-448 #domain S-locus-specific glycoprotein homology #label !8SSG\ !$531-806 #domain protein kinase homology #label KIN\ !$537-545 #region protein kinase ATP-binding motif\ !$29,92,100,178,240, !$251,361,446 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$563,579,657,659 #active_site Lys, Glu, Asp, Lys #status predicted\ !$662,666 #binding_site magnesium (Asn, Asp) #status predicted SUMMARY #length 832 #molecular-weight 93805 #checksum 9174 SEQUENCE /// ENTRY S50767 #type complete TITLE S-receptor kinase (EC 2.7.1.-) homolog precursor - rice ORGANISM #formal_name Oryza sativa #common_name rice DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S50767 REFERENCE S50767 !$#authors Zhao, Y.; Feng, X.H.; Watson, J.C.; Bottino, P.J.; Kung, !1S.D. !$#journal Plant Mol. Biol. (1994) 26:791-803 !$#title Molecular cloning and biochemical characterization of a !1receptor-like serine/threonine kinase from rice. !$#cross-references MUID:95093022; PMID:7999995 !$#accession S50767 !'##molecule_type mRNA !'##residues 1-824 ##label ZHA !'##cross-references EMBL:L27821; NID:g450299; PIDN:AAA33915.1; !1PID:g450300 CLASSIFICATION #superfamily S-receptor kinase; protein kinase homology; !1S-locus-specific glycoprotein homology KEYWORDS ATP; glycoprotein; magnesium; phosphotransferase; receptor; !1serine/threonine-specific protein kinase; signal !1transduction; transmembrane protein FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-824 #product S-receptor kinase homolog PK10 #status !8predicted #label MAT\ !$435-458 #domain transmembrane #status predicted #label TMM\ !$500-777 #domain protein kinase homology #label KIN\ !$506-514 #region protein kinase ATP-binding motif\ !$60,72,189,235,262, !$366,377,407 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$528,543,625,627 #active_site Lys, Glu, Asp, Lys #status predicted\ !$630,634 #binding_site magnesium (Asn, Asp) #status predicted SUMMARY #length 824 #molecular-weight 89870 #checksum 6417 SEQUENCE /// ENTRY A57676 #type complete TITLE protein kinase Xa21 (EC 2.7.1.-), receptor type precursor - rice ORGANISM #formal_name Oryza sativa #common_name rice DATE 08-Feb-1996 #sequence_revision 08-Feb-1996 #text_change 11-Jun-1999 ACCESSIONS A57676 REFERENCE A57676 !$#authors Song, W.Y.; Wang, G.L.; Chen, L.L.; Kim, H.S.; Pi, L.Y.; !1Holsten, T.; Gardner, J.; Wang, B.; Zhai, W.X.; Zhu, L.H.; !1Fauquet, C.; Ronald, P. !$#journal Science (1995) 270:1804-1806 !$#title A receptor kinase-like protein encoded by the rice disease !1resistance gene, Xa21. !$#cross-references MUID:96106403; PMID:8525370 !$#accession A57676 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-1025 ##label SON !'##cross-references GB:U37133; NID:g1122442; PIDN:AAC49123.1; !1PID:g1122443 GENETICS !$#gene Xa21 !$#note confers resistance against the bacterial pathogen !1Xanthomonas oryzae pv. oryzae race 6 CLASSIFICATION #superfamily protein kinase Xa21; leucine-rich !1alpha-2-glycoprotein repeat homology; protein kinase !1homology KEYWORDS ATP; glycoprotein; magnesium; phosphotransferase; receptor; !1serine/threonine-specific protein kinase; tandem repeat; !1transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-1025 #product protein kinase Xa21 #status predicted #label !8MAT\ !$80-103 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR1\ !$104-127 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR2\ !$128-151 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR3\ !$152-176 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR4\ !$177-200 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR5\ !$201-224 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR6\ !$225-248 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR7\ !$249-273 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR8\ !$274-297 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR9\ !$298-321 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR10\ !$322-345 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR11\ !$352-375 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR12\ !$377-400 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR13\ !$401-424 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR14\ !$425-448 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR15\ !$449-472 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR16\ !$473-496 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR17\ !$498-521 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR18\ !$522-545 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR19\ !$546-569 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR20\ !$570-593 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR21\ !$594-618 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR22\ !$706-1011 #domain protein kinase homology #label KIN\ !$714-722 #region protein kinase ATP-binding motif\ !$55,90,101,198,235, !$246,295,322,349, !$373,435,446,470, !$483,503,580,599 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$736,752,842,844 #active_site Lys, Glu, Asp, Lys #status predicted\ !$847,851 #binding_site magnesium (Asn, Asp) #status predicted SUMMARY #length 1025 #molecular-weight 111337 #checksum 9034 SEQUENCE /// ENTRY S27756 #type complete TITLE receptor-like protein kinase 5 (EC 2.7.1.-) precursor - Arabidopsis thaliana ALTERNATE_NAMES protein F20O9.180 ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 17-Apr-1993 #sequence_revision 17-Apr-1993 #text_change 11-Jun-1999 ACCESSIONS S27756; T04620 REFERENCE S27754 !$#authors Walker, J.C. !$#submission submitted to the EMBL Data Library, February 1992 !$#description Receptor-like protein kinase genes of Arabidopsis thaliana. !$#accession S27756 !'##molecule_type mRNA !'##residues 1-999 ##label WAL !'##cross-references EMBL:M84660; NID:g166849; PIDN:AAA32859.1; !1PID:g166850 !'##experimental_source strain Columbia REFERENCE Z15380 !$#authors Bevan, M.; Rose, M.; Hempel, S.; Entian, K.D.; Hoheisel, J.; !1Mewes, H.W.; Mayer, K.F.X.; Schueller, C. !$#submission submitted to the Protein Sequence Database, October 1998 !$#accession T04620 !'##molecule_type DNA !'##residues 1-999 ##label BEV !'##cross-references EMBL:AL021749 !'##experimental_source cultivar Columbia; BAC clone F20O9 GENETICS !$#gene RLK5 !$#map_position 4 !$#introns 868/1 !$#note F20O9.180 CLASSIFICATION #superfamily protein kinase Xa21; leucine-rich !1alpha-2-glycoprotein repeat homology; protein kinase !1homology KEYWORDS ATP; autophosphorylation; glycoprotein; magnesium; !1phosphotransferase; receptor; serine/threonine-specific !1protein kinase; tandem repeat; transmembrane protein FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-999 #product receptor-like protein kinase #status !8predicted #label MAT\ !$66-89 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR1\ !$90-114 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR2\ !$115-139 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR3\ !$140-163 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR4\ !$164-187 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR5\ !$188-212 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR6\ !$213-236 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR7\ !$237-260 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR8\ !$261-284 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR9\ !$285-307 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR10\ !$308-331 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR11\ !$332-355 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR12\ !$356-379 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR13\ !$380-403 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR14\ !$404-427 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR15\ !$428-451 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR16\ !$452-475 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR17\ !$476-499 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR18\ !$500-523 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR19\ !$524-547 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR20\ !$548-570 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR21\ !$571-593 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR22\ !$681-971 #domain protein kinase homology #label KIN\ !$689-697 #region protein kinase ATP-binding motif\ !$98,102,150,185,210, !$269,282,452,576 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$711,737,819,821 #active_site Lys, Glu, Asp, Lys #status predicted\ !$824,828 #binding_site magnesium (Asn, Asp) #status predicted SUMMARY #length 999 #molecular-weight 109094 #checksum 2103 SEQUENCE /// ENTRY JQ1674 #type complete TITLE protein kinase TMK1 (EC 2.7.1.-), receptor type precursor - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 11-Jun-1999 ACCESSIONS JQ1674 REFERENCE JQ1674 !$#authors Chang, C.; Schaller, G.E.; Patterson, S.E.; Kwok, S.F.; !1Meyerowitz, E.M.; Bleecker, A.B. !$#journal Plant Cell (1992) 4:1263-1271 !$#title The TMK1 gene from Arabidopsis codes for a protein with !1structural and biochemical characteristics of a receptor !1protein kinase. !$#cross-references MUID:93076110; PMID:1332795 !$#accession JQ1674 !'##molecule_type DNA !'##residues 1-942 ##label CHA !'##cross-references GB:L00670; NID:g166887; PIDN:AAA32876.1; !1PID:g166888 CLASSIFICATION #superfamily protein kinase Xa21; leucine-rich !1alpha-2-glycoprotein repeat homology; protein kinase !1homology KEYWORDS ATP; autophosphorylation; glycoprotein; phosphotransferase; !1receptor; serine/threonine-specific protein kinase; tandem !1repeat; transmembrane protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-942 #product protein kinase TMK1 #status predicted #label !8MAT\ !$65-88 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR1\ !$89-111 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR2\ !$112-135 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR3\ !$136-160 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR4\ !$161-186 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR5\ !$187-209 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR6\ !$210-232 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR7\ !$233-255 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR8\ !$256-279 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR9\ !$280-299 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR10\ !$300-323 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR11\ !$324-346 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR12\ !$363-386 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR14\ !$387-410 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR15\ !$411-434 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR16\ !$480-503 #domain transmembrane #status predicted #label TMM\ !$586-872 #domain protein kinase homology #label KIN\ !$594-602 #region protein kinase ATP-binding motif\ !$86,99,158,164,171, !$363,533,587 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$616,634,717,719 #active_site Lys, Glu, Asp, Lys #status predicted SUMMARY #length 942 #molecular-weight 102387 #checksum 2851 SEQUENCE /// ENTRY A41090 #type complete TITLE serine/threonine-specific protein kinase (EC 2.7.1.-) pkn1 - Myxococcus xanthus ORGANISM #formal_name Myxococcus xanthus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A41090 REFERENCE A41090 !$#authors Munoz-Dorado, J.; Inouye, S.; Inouye, M. !$#journal Cell (1991) 67:995-1006 !$#title A gene encoding a protein serine/threonine kinase is !1required for normal development of Myxococcus xanthus, a !1gram-negative bacterium. !$#cross-references MUID:92069765; PMID:1835671 !$#accession A41090 !'##molecule_type DNA !'##residues 1-693 ##label MUN !'##cross-references GB:M73498; NID:g150104; PIDN:AAA25402.1; !1PID:g150105 GENETICS !$#gene pkn1 CLASSIFICATION #superfamily Myxococcus xanthus serine/threonine-specific !1protein kinase pkn1; protein kinase homology KEYWORDS phosphotransferase; serine/threonine-specific protein kinase FEATURE !$57-319 #domain protein kinase homology #label KIN SUMMARY #length 693 #molecular-weight 74173 #checksum 6486 SEQUENCE /// ENTRY A57060 #type complete TITLE serine/threonine-specific protein kinase pkn2 (EC 2.7.1.-) - Myxococcus xanthus ORGANISM #formal_name Myxococcus xanthus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A57060; S21533; S21534 REFERENCE A57060 !$#authors Udo, H.; Munoz-Dorado, J.; Inouye, M.; Inouye, S. !$#journal Genes Dev. (1995) 9:972-983 !$#title Myxococcus xanthus, a gram-negative bacterium, contains a !1transmembrane protein serine/threonine kinase that blocks !1the secretion of beta-lactamase by phosphorylation. !$#cross-references MUID:95293229; PMID:7774814 !$#accession A57060 !'##status preliminary !'##molecule_type DNA !'##residues 1-830 ##label UDO !'##cross-references GB:M94857; NID:g704419; PIDN:AAA98813.1; !1PID:g704420 !'##note this is a revision to the sequence from reference S21533 REFERENCE S21533 !$#authors Munoz-Durado, X.Y.Z.; Inouye, M.; Inouye, S. !$#submission submitted to the EMBL Data Library, May 1992 !$#description A eukaryotic-like protein threonine kinase (PKN2) required !1for the maintainence of the stationary phase cells and !1normal development of Myxococcus xanthus. !$#accession S21533 !'##molecule_type DNA !'##residues 1-59,'P',61-370,'SD' ##label MUN !'##cross-references EMBL:X66408 !'##note this sequence has been revised in reference A57060 !$#accession S21534 !'##molecule_type DNA !'##residues 398-830 ##label MUW !'##cross-references EMBL:X66408 !'##note this sequence has been revised in reference A57060 GENETICS !$#gene pkn2 !$#start_codon GTG CLASSIFICATION #superfamily Myxococcus xanthus serine/threonine-specific !1protein kinase pkn2; protein kinase homology KEYWORDS phosphotransferase FEATURE !$11-277 #domain protein kinase homology #label KIN SUMMARY #length 830 #molecular-weight 87679 #checksum 4687 SEQUENCE /// ENTRY S77406 #type complete TITLE protein kinase pknA (EC 2.7.1.-), 54K - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein slr1225 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S77406 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S77406 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-495 ##label KAN !'##cross-references EMBL:D90906; GB:AB001339; NID:g1652492; !1PIDN:BAA17509.1; PID:g1652588 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene pknA CLASSIFICATION #superfamily Synechocystis sp. protein kinase pknA, 54K; !1protein kinase homology KEYWORDS phosphotransferase; protein kinase FEATURE !$44-315 #domain protein kinase homology #label KIN SUMMARY #length 495 #molecular-weight 53872 #checksum 3206 SEQUENCE /// ENTRY S77034 #type complete TITLE protein kinase pknA (EC 2.7.1.-), 55K - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein sll0776 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S77034 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S77034 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-505 ##label KAN !'##cross-references EMBL:D64005; GB:AB001339; NID:g1001779; !1PIDN:BAA10726.1; PID:g1006577 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene pknA CLASSIFICATION #superfamily Synechocystis sp. protein kinase pknA, 55K; !1protein kinase homology KEYWORDS phosphotransferase; protein kinase FEATURE !$7-268 #domain protein kinase homology #label KIN SUMMARY #length 505 #molecular-weight 55213 #checksum 5465 SEQUENCE /// ENTRY S76132 #type complete TITLE protein kinase pknA (EC 2.7.1.-), 63K - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein slr1697 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S76132 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76132 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-574 ##label KAN !'##cross-references EMBL:D90914; GB:AB001339; NID:g1653477; !1PIDN:BAA18391.1; PID:g1653478 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene pknA CLASSIFICATION #superfamily Synechocystis sp. protein kinase pknA, 63K; !1protein kinase homology KEYWORDS phosphotransferase; protein kinase FEATURE !$32-297 #domain protein kinase homology #label KIN SUMMARY #length 574 #molecular-weight 63079 #checksum 9246 SEQUENCE /// ENTRY S76953 #type complete TITLE protein kinase (EC 2.7.1.-), 58K - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein slr0599 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S76953 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76953 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-535 ##label KAN !'##cross-references EMBL:D90917; GB:AB001339; NID:g1653836; !1PIDN:BAA18865.1; PID:g1653955 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily Synechocystis sp. protein kinase, 58K; protein !1kinase homology KEYWORDS phosphotransferase; protein kinase FEATURE !$10-274 #domain protein kinase homology #label KIN SUMMARY #length 535 #molecular-weight 58141 #checksum 6187 SEQUENCE /// ENTRY JC4070 #type complete TITLE protein kinase (EC 2.7.1.37) A - Streptomyces coelicolor (strain A3-2) ALTERNATE_NAMES serine/threonine protein kinase A ORGANISM #formal_name Streptomyces coelicolor DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS JC4070 REFERENCE JC4070 !$#authors Urabe, H.; Ogawara, H. !$#journal Gene (1995) 153:99-104 !$#title Cloning, sequencing and expression of serine/threonine !1kinase-encoding genes from Streptomyces coelicolor A3(2). !$#cross-references MUID:95189113; PMID:7883195 !$#accession JC4070 !'##molecule_type DNA !'##residues 1-543 ##label URA !'##cross-references GB:D86821; DDBJ:D26539; NID:g1483185; !1PIDN:BAA13168.1; PID:g666024 GENETICS !$#gene pkaA CLASSIFICATION #superfamily Streptomyces coelicolor protein kinase A; !1protein kinase homology KEYWORDS phosphotransferase; serine/threonine-specific protein kinase FEATURE !$6-275 #domain protein kinase homology #label KIN SUMMARY #length 543 #molecular-weight 58181 #checksum 660 SEQUENCE /// ENTRY S49611 #type complete TITLE probable serine/threonine-specific protein kinase pkpA (EC 2.7.1.-) - Phycomyces blakesleeanus ORGANISM #formal_name Phycomyces blakesleeanus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S49611; S59578 REFERENCE S49611 !$#authors Ruiz-Perez, V.; Murillo, F.; Torres-Martinez, S. !$#submission submitted to the EMBL Data Library, November 1994 !$#description A novel serine/threonine protein kinase in the fungus !1Phycomyces blakesleeanus. !$#accession S49611 !'##molecule_type DNA !'##residues 1-633 ##label RUI !'##cross-references EMBL:Z46636 REFERENCE S59578 !$#authors Ruiz-Perez, V.L.; Murillo, F.J.; Torres-Martinez, S. !$#journal Curr. Genet. (1995) 28:309-316 !$#title PkpA, a novel Phycomyces blakesleeanus serine/threonine !1protein kinase. !$#cross-references MUID:96120859; PMID:8590476 !$#accession S59578 !'##molecule_type DNA !'##residues 1-9;39-346 ##label RUW !'##cross-references EMBL:Z46636 !'##note only part of the coding region is given GENETICS !$#gene pkpA !$#introns 60/1; 248/3; 277/2; 339/3; 534/1 CLASSIFICATION #superfamily Phycomyces blakesleeanus probable serine/ !1threonine-specific protein kinase pkpA; protein kinase !1homology KEYWORDS phosphotransferase; protein kinase FEATURE !$34-289 #domain protein kinase homology #label KIN SUMMARY #length 633 #molecular-weight 71922 #checksum 9644 SEQUENCE /// ENTRY JC5298 #type complete TITLE protein kinase (EC 2.7.1.37) gPK1 - Giardia lamblia ORGANISM #formal_name Giardia lamblia DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JC5298 REFERENCE JC5298 !$#authors Chen, N.; Upcroft, J.A.; Upcroft, P. !$#journal Gene (1996) 177:191-194 !$#title A novel protein kinase gene family in Giardia duodenalis. !$#cross-references MUID:97080521; PMID:8921866 !$#accession JC5298 !'##molecule_type DNA !'##residues 1-443 ##label CHE !'##cross-references GB:L76195 !'##experimental_source strain WB-IB COMMENT This enzyme plays roles in general cell function including !1signal transduction, cell cycle regulation, and stress !1responsess. GENETICS !$#gene gPK1 CLASSIFICATION #superfamily Giardia lamblia protein kinase gPK1; protein !1kinase homology KEYWORDS phosphotransferase FEATURE !$98-355 #domain protein kinase homology #label KIN SUMMARY #length 443 #molecular-weight 48231 #checksum 2817 SEQUENCE /// ENTRY WMBE71 #type complete TITLE protein-serine/threonine kinase (EC 2.7.1.-) - human herpesvirus 1 (strain 17) ALTERNATE_NAMES UL13 protein ORGANISM #formal_name human herpesvirus 1 #note host Homo sapiens (man) DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 16-Jun-2000 ACCESSIONS A03738; D30083 REFERENCE A93620 !$#authors McGeoch, D.J.; Dolan, A.; Frame, M.C. !$#journal Nucleic Acids Res. (1986) 14:3435-3448 !$#title DNA sequence of the region in the genome of herpes simplex !1virus type 1 containing the exonuclease gene and !1neighbouring genes. !$#cross-references MUID:86205244; PMID:3010237 !$#accession A03738 !'##molecule_type DNA !'##residues 1-518 ##label MCG !'##cross-references GB:X03839; NID:g59841; PIDN:CAA27454.1; PID:g59845 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession D30083 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-518 ##label MC2 !'##cross-references GB:X14112; NID:g1944536; PIDN:CAA32326.1; !1PID:g59514 GENETICS !$#gene UL13 !$#map_position 0.16-0.20 CLASSIFICATION #superfamily herpesvirus protein-serine/threonine kinase; !1protein kinase homology KEYWORDS ATP; phosphotransferase; serine/threonine-specific protein !1kinase FEATURE !$149-500 #domain protein kinase homology #label KIN\ !$157-164 #region protein kinase ATP-binding motif\ !$176 #active_site Lys #status predicted SUMMARY #length 518 #molecular-weight 57196 #checksum 5 SEQUENCE /// ENTRY WZBE47 #type complete TITLE protein-serine/threonine kinase (EC 2.7.1.-) - human herpesvirus 3 ALTERNATE_NAMES gene 47 protein ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus #note host Homo sapiens (man) DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 11-Jun-1999 ACCESSIONS C27344 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession C27344 !'##molecule_type DNA !'##residues 1-510 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27930.1; !1PID:g60036 GENETICS !$#gene 47 CLASSIFICATION #superfamily herpesvirus protein-serine/threonine kinase; !1protein kinase homology KEYWORDS ATP; phosphotransferase; serine/threonine-specific protein !1kinase FEATURE !$130-480 #domain protein kinase homology #label KIN\ !$138-145 #region protein kinase ATP-binding motif\ !$157 #active_site Lys #status predicted SUMMARY #length 510 #molecular-weight 57350 #checksum 9028 SEQUENCE /// ENTRY WZBEE2 #type complete TITLE protein-serine/threonine kinase (EC 2.7.1.-) - equine herpesvirus 1 (strain Ab4p) ALTERNATE_NAMES gene 49 protein ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 11-Jun-1999 ACCESSIONS D36800 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession D36800 !'##molecule_type DNA !'##residues 1-594 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02484.1; !1PID:g330840 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 49 CLASSIFICATION #superfamily herpesvirus protein-serine/threonine kinase; !1protein kinase homology KEYWORDS ATP; phosphotransferase; serine/threonine-specific protein !1kinase FEATURE !$221-569 #domain protein kinase homology #label KIN\ !$229-236 #region protein kinase ATP-binding motif\ !$248 #active_site Lys #status predicted SUMMARY #length 594 #molecular-weight 65247 #checksum 6982 SEQUENCE /// ENTRY WZBEN3 #type complete TITLE protein-serine/threonine kinase (EC 2.7.1.-) - suid herpesvirus 1 (strain NIA-3) ALTERNATE_NAMES UL13 protein ORGANISM #formal_name suid herpesvirus 1 DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 11-Jun-1999 ACCESSIONS B42744 REFERENCE A42744 !$#authors de Wind, N.; Domen, J.; Berns, A. !$#journal J. Virol. (1992) 66:5200-5209 !$#title Herpesviruses encode an unusual protein-serine/threonine !1kinase which is nonessential for growth in cultured cells. !$#cross-references MUID:92365105; PMID:1323689 !$#accession B42744 !'##molecule_type DNA !'##residues 1-398 ##label DEW !'##cross-references GB:M94870; NID:g334092; PIDN:AAA47481.1; !1PID:g334094 GENETICS !$#gene UL13 CLASSIFICATION #superfamily herpesvirus protein-serine/threonine kinase; !1protein kinase homology KEYWORDS ATP; phosphotransferase; serine/threonine-specific protein !1kinase FEATURE !$78-378 #domain protein kinase homology #label KIN\ !$86-93 #region protein kinase ATP-binding motif\ !$103 #active_site Lys #status predicted SUMMARY #length 398 #molecular-weight 41416 #checksum 440 SEQUENCE /// ENTRY S68455 #type complete TITLE serine/threonine-specific protein kinase (EC 2.7.1.-) ILK [validated] - human ALTERNATE_NAMES integrin-linked protein kinase ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-May-2000 ACCESSIONS S68455 REFERENCE S68455 !$#authors Hannigan, G.E.; Leung-Hagesteijn, C.; Fitz-Gibbon, L.; !1Coppolino, M.G.; Radeva, G.; Filmus, J.; Bell, J.C.; Dedhar, !1S. !$#journal Nature (1996) 379:91-96 !$#title Regulation of cell adhesion and anchorage-dependent growth !1by a new beta(1)-integrin-linked protein kinase. !$#cross-references MUID:96135142; PMID:8538749 !$#accession S68455 !'##molecule_type mRNA !'##residues 1-451 ##label HAN !'##cross-references EMBL:U40282; NID:g2648173; PID:g2648174 GENETICS !$#gene GDB:ILK !'##cross-references GDB:6155815; OMIM:602366 !$#map_position 11p15.5-11p15.4 CLASSIFICATION #superfamily human serine/threonine-specific protein kinase !1ILK; ankyrin repeat homology; protein kinase homology KEYWORDS integrin binding; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$33-65 #domain ankyrin repeat homology #label AN11\ !$66-98 #domain ankyrin repeat homology #label AN13\ !$99-131 #domain ankyrin repeat homology #label AN12\ !$191-451 #domain protein kinase homology #label KIN SUMMARY #length 451 #molecular-weight 51322 #checksum 6400 SEQUENCE /// ENTRY JE0240 #type complete TITLE LIM kinase (EC 2.7.1.-) tLimk2 - mouse ALTERNATE_NAMES LIM-kinase 2t-1 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS JE0240; JE0249 REFERENCE JE0240 !$#authors Ikebe, C.; Ohashi, K.; Mizuno, K. !$#journal Biochem. Biophys. Res. Commun. (1998) 246:307-312 !$#title Identification of testis-specific (Limk2t) and !1brain-specific (Limk2c) isoforms of mouse LIM-kinase 2 gene !1transcripts. !$#cross-references MUID:98273274; PMID:9610354 !$#accession JE0240 !'##status preliminary !'##molecule_type mRNA !'##residues 1-451 ##label IKE !'##cross-references DDBJ:AB012092; NID:g3273203; PIDN:BAA31147.1; !1PID:g3273204 REFERENCE JE0249 !$#authors Takahashi, H.; Koshimizu, U.; Nakamura, T. !$#journal Biochem. Biophys. Res. Commun. (1998) 249:138-145 !$#title A novel transcript encoding truncated LIM kinase 2 is !1specifically expressed in male germ cells undergoing !1meiosis. !$#cross-references MUID:98381040; PMID:9705845 !$#accession JE0249 !'##status preliminary !'##molecule_type mRNA !'##residues 1-451 ##label TAK !'##cross-references DDBJ:AB012291; NID:g3445493; PIDN:BAA32437.1; !1PID:g3445494 CLASSIFICATION #superfamily mouse LIM kinase tLimk2; protein kinase !1homology KEYWORDS phosphotransferase FEATURE !$142-421 #domain protein kinase homology #label KIN SUMMARY #length 451 #molecular-weight 51173 #checksum 52 SEQUENCE /// ENTRY JC6534 #type complete TITLE protein kinase 1 (EC 2.7.1.-), testis-specific - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS JC6534 REFERENCE JC6534 !$#authors Toshima, J.; Nakagawara, K.; Mori, M.; Noda, T.; Mizuno, K. !$#journal Gene (1998) 206:237-245 !$#title Structural organization and chromosomal localization of the !1mouse Tesk1 (testis-specific protein kinase 1) gene. !$#cross-references MUID:98137797; PMID:9469938 !$#accession JC6534 !'##molecule_type mRNA !'##residues 1-627 ##label TOS !'##cross-references DDBJ:AB003494; NID:g2957009; PIDN:BAA25125.1; !1PID:g2957010 !'##experimental_source 129/SV COMMENT This enzyme is a protein serine-threonine kinase involved in !1spermatogenesis. GENETICS !$#gene Tesk1 !$#map_position 4A5-C1 !$#introns 68/3; 109/2; 125/3; 174/3; 202/2; 232/3; 260/3; 290/3; 334/1 CLASSIFICATION #superfamily mouse protein kinase 1 testis-specific; protein !1kinase homology KEYWORDS phosphotransferase; serine/threonine-specific protein !1kinase; spermatogenesis FEATURE !$50-313 #domain protein kinase homology #label KIN SUMMARY #length 627 #molecular-weight 68023 #checksum 2451 SEQUENCE /// ENTRY A45703 #type complete TITLE probable serine/threonine-specific protein kinase (EC 2.7.1.-) j9L - African swine fever virus ORGANISM #formal_name African swine fever virus, ASFV DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A45703; S27892 REFERENCE A45703 !$#authors Baylis, S.A.; Banham, A.H.; Vydelingum, S.; Dixon, L.K.; !1Smith, G.L. !$#journal J. Virol. (1993) 67:4549-4556 !$#title African swine fever virus encodes a serine protein kinase !1which is packaged into virions. !$#cross-references MUID:93323195; PMID:8331722 !$#accession A45703 !'##status preliminary !'##molecule_type DNA !'##residues 1-299 ##label BAY !'##cross-references GB:X72954; NID:g397077; PIDN:CAA51459.1; !1PID:g397078 !'##experimental_source strain Malawi (LIL20/1) REFERENCE S27892 !$#authors Roberts, P.C.; Lu, Z.; Rock, D.L. !$#submission submitted to the EMBL Data Library, July 1992 !$#description Three adjacent genes of African swine fever virus with !1homologies to essential poxvirus genes. !$#accession S27892 !'##molecule_type DNA !'##residues 1-299 ##label ROB !'##cross-references EMBL:M88275; NID:g210602; PIDN:AAA03220.1; !1PID:g210603 GENETICS !$#gene j9L CLASSIFICATION #superfamily African swine fever virus probable serine/ !1threonine-specific protein kinase j9L; protein kinase !1homology KEYWORDS phosphotransferase; serine/threonine-specific protein kinase FEATURE !$37-277 #domain protein kinase homology #label KIN SUMMARY #length 299 #molecular-weight 35112 #checksum 9225 SEQUENCE /// ENTRY JC5299 #type complete TITLE protein kinase (EC 2.7.1.37) gPK2 - Giardia lamblia ORGANISM #formal_name Giardia lamblia DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JC5299 REFERENCE JC5298 !$#authors Chen, N.; Upcroft, J.A.; Upcroft, P. !$#journal Gene (1996) 177:191-194 !$#title A novel protein kinase gene family in Giardia duodenalis. !$#cross-references MUID:97080521; PMID:8921866 !$#accession JC5299 !'##molecule_type DNA !'##residues 1-300 ##label CHE !'##cross-references GB:L76196; NID:g1929883; PIDN:AAB51602.1; !1PID:g1932709 !'##experimental_source strain WB-IB COMMENT This enzyme plays roles in general cell function including !1signal transduction, cell cycle regulation, and stress !1responsess. GENETICS !$#gene gPK2 CLASSIFICATION #superfamily Giardia lamblia protein kinase gPK2; protein !1kinase homology KEYWORDS ATP; phosphotransferase; protein kinase FEATURE !$26-288 #domain protein kinase homology #label KIN SUMMARY #length 300 #molecular-weight 32446 #checksum 1483 SEQUENCE /// ENTRY OKBYS1 #type complete TITLE cell division control protein CKS1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein kinase CDC28 regulator CKS1; protein YBR1011; protein YBR135w ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 21-Jul-2000 ACCESSIONS A32793; S46577; S46004; S46662; S47953; S05763 REFERENCE A32793 !$#authors Hadwiger, J.A.; Wittenberg, C.; Mendenhall, M.D.; Reed, S.I. !$#journal Mol. Cell. Biol. (1989) 9:2034-2041 !$#title The Saccharomyces cerevisiae CKS1 gene, a homolog of the !1Schizosaccharomyces pombe suc1(+) gene, encodes a subunit of !1the Cdc28 protein kinase complex. !$#cross-references MUID:89313749; PMID:2664468 !$#accession A32793 !'##molecule_type DNA !'##residues 1-150 ##label HAD !'##cross-references EMBL:M26033; NID:g172178; PIDN:AAA34879.1; !1PID:g172179 REFERENCE S46569 !$#authors Becam, A.M.; Cullin, C.; Grzybowska, E.; Lacroute, F.; Nasr, !1F.; Ozier-Kalogeropoulos, O.; Palucha, A.; Slonimski, P.P.; !1Zagulski, M.; Herbert, C.J. !$#journal Yeast (1994) 10(Suppl.A):S1-S11 !$#title The sequence of 29.7kb from the right arm of chromosome II !1reveals 13 complete open reading frames, of which ten !1correspond to new genes. !$#cross-references MUID:94378717; PMID:8091856 !$#accession S46577 !'##molecule_type DNA !'##residues 1-150 ##label BEC !'##cross-references EMBL:X75891; NID:g496856; PIDN:CAA53493.1; !1PID:g496865 REFERENCE S45995 !$#authors Becam, A.M.; Herbert, C.J.; Nasr, F.; Slonimski, P.P.; !1Zagulski, M. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S46004 !'##molecule_type DNA !'##residues 1-150 ##label BE2 !'##cross-references EMBL:Z36004; NID:g536427; PIDN:CAA85092.1; !1PID:g536428; GSPDB:GN00002; MIPS:YBR135w REFERENCE S46662 !$#authors Kato, R.; Ogawa, H. !$#submission submitted to the EMBL Data Library, May 1992 !$#description An essential gene, ESR1, is required for mitotic cell !1growth, DNA repair and meiotic recombination in !1Saccharomyces cerevisiae. !$#accession S46662 !'##molecule_type DNA !'##residues 32-150 ##label KAT !'##cross-references EMBL:D11088; NID:g506874; PIDN:BAA01859.1; !1PID:g506875 REFERENCE S47953 !$#authors Kato, R.; Ogawa, H. !$#journal Nucleic Acids Res. (1994) 22:3104-3112 !$#title An essential gene, ESR1, is required for mitotic cell !1growth, DNA repair and meiotic recombination in !1Saccharomyces cerevisiae. !$#cross-references MUID:94344772; PMID:8065923 !$#accession S47953 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 32-150 ##label KA2 !'##cross-references EMBL:D11088; NID:g506874; PIDN:BAA01859.1; !1PID:g506875 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1May 1992 GENETICS !$#gene SGD:CKS1; MIPS:YBR135w !'##cross-references SGD:S0000339; MIPS:YBR135w !$#map_position 2R FUNCTION !$#description binds the cyclin-dependent protein kinase CDC28 (see !1PIR:TVBY8) to form the active complex CLASSIFICATION #superfamily cell division control protein CKS1 KEYWORDS cell cycle control FEATURE !$118-137 #region glutamine-rich SUMMARY #length 150 #molecular-weight 17795 #checksum 5059 SEQUENCE /// ENTRY OKBYN2 #type complete TITLE protein kinase GCN2 (EC 2.7.1.-) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein D9954.16; protein YDR283c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1991 #sequence_revision 07-Feb-1997 #text_change 05-Nov-1999 ACCESSIONS S70139; S05781; A27723; A33927 REFERENCE S70124 !$#authors Le, T. !$#submission submitted to the EMBL Data Library, May 1996 !$#description The sequence of S. cerevisiae cosmid 9954. !$#accession S70139 !'##molecule_type DNA !'##residues 1-1659 ##label LET !'##cross-references EMBL:U51030; NID:g1332633; PIDN:AAB64461.1; !1PID:g1332634; GSPDB:GN00004; MIPS:YDR283c REFERENCE A33927 !$#authors Wek, R.C.; Jackson, B.M.; Hinnebusch, A.G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:4579-4583 !$#title Juxtaposition of domains homologous to protein kinases and !1histidyl-tRNA synthetases in GCN2 protein suggests a !1mechanism for coupling GCN4 expression to amino acid !1availability. !$#cross-references MUID:89282814; PMID:2660141 !$#accession S05781 !'##molecule_type DNA !'##residues 70-1659 ##label WEK !'##cross-references EMBL:M27082; NID:g171577; PIDN:AAA34636.1; !1PID:g171578 REFERENCE A27723 !$#authors Roussou, I.; Thireos, G.; Hauge, B.M. !$#journal Mol. Cell. Biol. (1988) 8:2132-2139 !$#title Transcriptional-translational regulatory circuit in !1Saccharomyces cerevisiae which involves the GCN4 !1transcriptional activator and the GCN2 protein kinase. !$#cross-references MUID:88261291; PMID:3290651 !$#accession A27723 !'##molecule_type DNA !'##residues 73-219,'NY',222,'G',224,'IA',227-270,'YVF',274,'NHGKS', !1280-369,376,'VFGS',381,'DCLKDWRPYTNWE',393,'SSMYQLRNRDPG', !1397,'GCR',401,'W',403,'HYARV',409,'SLHLWL',416,'CFE',421, !1'AIEIST',433-474,'M',476-588,'A',590-591,'DHDMLLTLKRLHFS', !1606-639,'MI',642-726,'C',728-838,'K',840-953,'Q',955-1050, !1'LGNMEELKIMLLRGF',1066,'QRP',1070,1072,'TVRRM',1078,'MKC', !11081,'TRA',1087,'PSCS',1092,'NMI' ##label ROU !'##cross-references EMBL:M20487 !'##note the authors translated the codon CAA for residue 881 as Glu !'##note this sequence is very different in certain regions due to !1frameshift errors GENETICS !$#gene SGD:GCN2; MIPS:YDR283c !'##cross-references SGD:S0002691; MIPS:YDR283c !$#map_position 4R CLASSIFICATION #superfamily GCN2 protein; histidine-tRNA ligase homology; !1protein kinase homology KEYWORDS ATP; phosphotransferase; serine/threonine-specific protein !1kinase FEATURE !$597-981 #domain protein kinase homology #label KIN\ !$605-613 #region protein kinase ATP-binding motif\ !$1027-1453 #domain histidine-tRNA ligase homology #label HTL\ !$628 #active_site Lys #status predicted SUMMARY #length 1659 #molecular-weight 190192 #checksum 3395 SEQUENCE /// ENTRY A39616 #type complete TITLE protein kinase RAD53 (EC 2.7.1.-) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein P2588; protein YPL153c; SPK1 protein ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 21-Jul-2000 ACCESSIONS A39616; S65164; S69446; S13321 REFERENCE A39616 !$#authors Stern, D.F.; Zheng, P.; Beidler, D.R.; Zerillo, C. !$#journal Mol. Cell. Biol. (1991) 11:987-1001 !$#title Spk1, a new kinase from Saccharomyces cerevisiae, !1phosphorylates proteins on serine, threonine, and tyrosine. !$#cross-references MUID:91117267; PMID:1899289 !$#accession A39616 !'##molecule_type DNA !'##residues 1-821 ##label STE !'##cross-references GB:M55623; NID:g172656; PIDN:AAA35070.1; !1PID:g172657 !'##experimental_source strain S288C REFERENCE A54697 !$#authors Zheng, P.; Fay, D.S.; Burton, J.; Xiao, H.; Pinkham, J.L.; !1Stern, D.F. !$#journal Mol. Cell. Biol. (1993) 13:5829-5842 !$#title SPK1 is an essential S-phage-specific gene of Saccharomyces !1cerevisiae that encodes a nuclear serine/threonine/tyrosine !1kinase. !$#cross-references MUID:93361015; PMID:8355715 !$#contents annotation REFERENCE S65154 !$#authors Purnelle, B.; Coster, F.; Goffeau, A. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S65164 !'##molecule_type DNA !'##residues 1-821 ##label PUR !'##cross-references EMBL:Z73509; NID:g1370325; PIDN:CAA97858.1; !1PID:g1370326; GSPDB:GN00016; MIPS:YPL153c !'##experimental_source strain S288C (AB972) REFERENCE S69428 !$#authors Purnelle, B.; Comblez, S.; Coster, F.; Naveau, F.; Goffeau, !1A. !$#submission submitted to the EMBL Data Library, March 1996 !$#description The sequence of 55 kb on the left arm of yeast chromosome !1XVI identifies 28 open reading frames including 18 unknown !1among which a new putative serine/threonine protein kinase, !1a homologue to the human phosphotyrosyl phosphatase !1activator PTPA and a homologue to the plant pleiotropic !1regulator PRL1 of PP1 and PP2a phosphatases. !$#accession S69446 !'##molecule_type DNA !'##residues 1-821 ##label PUW !'##cross-references EMBL:X96770; NID:g1403537; PIDN:CAA65568.1; !1PID:g1403556 GENETICS !$#gene SGD:RAD53; SPK1; MEC2; SAD1; MIPS:YPL153c !'##cross-references SGD:S0006074; MIPS:YPL153c !$#map_position 16L FUNCTION !$#description serine/threonine-specific protein kinase !$#note contains low activity as tyrosine-specific protein kinase CLASSIFICATION #superfamily protein kinase SPK1; kinase interaction domain !1homology; protein kinase homology KEYWORDS ATP; cell cycle control; nucleus; phosphotransferase; !1serine/threonine-specific protein kinase FEATURE !$68-133 #domain kinase interaction domain homology #label !8KIH\ !$196-466 #domain protein kinase homology #label KIN\ !$204-213 #region protein kinase ATP-binding motif\ !$227 #active_site Lys #status predicted SUMMARY #length 821 #molecular-weight 91962 #checksum 9810 SEQUENCE /// ENTRY S43941 #type complete TITLE protein kinase DUN1 (EC 2.7.1.-) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein D2370; protein YDL101c ORGANISM #formal_name Saccharomyces cerevisiae DATE 13-Jan-1995 #sequence_revision 13-Jan-1995 #text_change 16-Jun-2000 ACCESSIONS S43941; S67643; S67418; S72106 REFERENCE S43941 !$#authors Zhou, Z.; Elledge, S.J. !$#journal Cell (1993) 75:1119-1127 !$#title DUN1 encodes a protein kinase that controls the DNA damage !1response in yeast. !$#cross-references MUID:94084787; PMID:8261511 !$#accession S43941 !'##molecule_type DNA !'##residues 1-513 ##label ZHO !'##cross-references EMBL:L25548; NID:g435616; PIDN:AAA16324.1; !1PID:g435617 REFERENCE S67629 !$#authors Ballesta, J.P.G.; Remacha, M.; Soler-Mira, A.; Jimenez, A.; !1Garcia-Cantalejo, J.M.; Boskovic, J.; del Rey, F.; Revuelta, !1J.L.; Buitrago, M.J.; Sanz, J.E. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67643 !'##molecule_type DNA !'##residues 1-513 ##label BAL !'##cross-references EMBL:Z74149; NID:g1431139; PIDN:CAA98668.1; !1PID:g1431140; GSPDB:GN00004; MIPS:YDL101c !'##experimental_source strain S288C REFERENCE S67406 !$#authors Boskovic, J.; Saiz, J.E.; Soler-Mira, A.; Garcia-Cantalejo, !1J.; Revuelta, J.L.; Jiminez, A.; Ballesta, J.P.G.; del Rey, !1F.; Remacha, M. !$#submission submitted to the EMBL Data Library, February 1996 !$#accession S67418 !'##molecule_type DNA !'##residues 1-513 ##label BOS !'##cross-references EMBL:X95644; NID:g1199535; PIDN:CAA64912.1; !1PID:g1199548 REFERENCE S72094 !$#authors Saiz, J.E.; Buitrago, M.J.; Garcia, R.; Revuelta, J.L.; del !1Rey, F. !$#journal Yeast (1996) 12:1077-1084 !$#title The sequence of a 20.3 kb DNA fragment from the left arm of !1Saccharomyces cerevisiae chromosome IV contains the KIN28, !1MSS2, PHO2, POL3 and DUN1 genes, and six new open reading !1frames. !$#cross-references MUID:97051597; PMID:8896274 !$#accession S72106 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-513 ##label SAI !'##cross-references EMBL:X95644; NID:g1199535; PIDN:CAA64912.1; !1PID:g1199548 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1February 1996 GENETICS !$#gene SGD:DUN1; MIPS:YDL101c !'##cross-references MIPS:YDL101c; SGD:S0002259 !$#map_position 4L FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP; control of DNA !1damage response; serine/threonine-specific protein kinase CLASSIFICATION #superfamily protein kinase DUN1; kinase interaction domain !1homology; protein kinase homology KEYWORDS ATP; nucleus; phosphoprotein; phosphotransferase; serine/ !1threonine-specific protein kinase FEATURE !$58-128 #domain kinase interaction domain homology #label !8KIH\ !$198-480 #domain protein kinase homology #label KIN\ !$206-214 #region protein kinase ATP-binding motif SUMMARY #length 513 #molecular-weight 58632 #checksum 2792 SEQUENCE /// ENTRY S20174 #type complete TITLE protein kinase MEK1 (EC 2.7.1.-) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES meiotic protein kinase mek1; probable protein kinase MRE4; protein O6357; protein YOR351c ORGANISM #formal_name Saccharomyces cerevisiae DATE 23-Apr-1993 #sequence_revision 23-Apr-1993 #text_change 21-Jul-2000 ACCESSIONS S20174; A41637; S67263; S67260; S67405; S18055; S19065 REFERENCE S20174 !$#authors Leem, S.H.; Ogawa, H. !$#journal Nucleic Acids Res. (1992) 20:449-457 !$#title The MRE4 gene encodes a novel protein kinase homologue !1required for meiotic recombination in Saccharomyces !1cerevisiae. !$#cross-references MUID:92158649; PMID:1741279 !$#accession S20174 !'##molecule_type DNA !'##residues 1-497 ##label LEE !'##cross-references EMBL:X63112; NID:g3968; PIDN:CAA44825.1; PID:g3969 REFERENCE A41637 !$#authors Rockmill, B.; Roeder, G.S. !$#journal Genes Dev. (1991) 5:2392-2404 !$#title A meiosis-specific protein kinase homolog required for !1chromosome synapsis and recombination. !$#cross-references MUID:92090720; PMID:1752435 !$#accession A41637 !'##molecule_type DNA !'##residues 1-497 ##label ROF !'##cross-references GB:X61208; NID:g4001; PIDN:CAA43522.1; PID:g4002 REFERENCE S67261 !$#authors Delius, H.; Hebling, U.; Hofmann, B. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67263 !'##molecule_type DNA !'##residues 1-497 ##label DEL !'##cross-references EMBL:Z75259; NID:g1420763; PIDN:CAA99680.1; !1PID:g1420764; GSPDB:GN00015; MIPS:YOR351c !'##experimental_source strain S288C REFERENCE S67246 !$#authors Goffeau, A.; Purnelle, B. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67260 !'##molecule_type DNA !'##residues 150-497 ##label GOF !'##cross-references EMBL:Z75259; GSPDB:GN00015; MIPS:YOR351c !'##experimental_source strain S288C REFERENCE S67392 !$#authors Purnelle, B.; Goffeau, A. !$#submission submitted to the EMBL Data Library, February 1996 !$#description Nucleotide sequence analysis of a 40 kb segment on the right !1arm of yeast chromosome XV reveals 18 open reading frames !1among which a new pyruvate kinase and three homologues to !1chromosome I genes. !$#accession S67405 !'##molecule_type DNA !'##residues 150-497 ##label PUR !'##cross-references EMBL:X95720; NID:g1199839; PIDN:CAA65038.1; !1PID:g1199853 GENETICS !$#gene SGD:MEK1; MRE4; MIPS:YOR351c !'##cross-references SGD:S0005878; MIPS:YOR351c !$#map_position 15R FUNCTION !$#description catalyzes the formation of peptidyl-serine-phosphate or !1peptidyl-threonine-phosphate using ATP !$#pathway meiosis; DNA recombination CLASSIFICATION #superfamily protein kinase DUN1; kinase interaction domain !1homology; protein kinase homology KEYWORDS ATP; phosphotransferase; serine/threonine-specific protein !1kinase FEATURE !$49-119 #domain kinase interaction domain homology #label !8KIH\ !$160-444 #domain protein kinase homology #label KIN\ !$168-176 #region protein kinase ATP-binding motif SUMMARY #length 497 #molecular-weight 56849 #checksum 4229 SEQUENCE /// ENTRY OKBY8W #type complete TITLE probable protein kinase YCR008w (EC 2.7.1.-) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YCR046; protein YCR101 ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 21-Jul-2000 ACCESSIONS S17470; S19505; S26737; S19768; S20183 REFERENCE S17470 !$#authors Skala, J.; Purnelle, B.; Crouzet, M.; Aigle, M.; Goffeau, A. !$#journal Yeast (1991) 7:651-655 !$#title The open reading frame YCR101 located on chromosome III from !1Saccharomyces cerevisiae is a putative protein kinase. !$#cross-references MUID:92116650; PMID:1767593 !$#accession S17470 !'##molecule_type DNA !'##residues 1-603 ##label SKA !'##cross-references GB:S76380; NID:g242394; PIDN:AAB20894.1; !1PID:g242395 REFERENCE S19452 !$#authors Aigle, M.; Biteau, N.; Crouzet, M. !$#submission submitted to the Protein Sequence Database, March 1992 !$#accession S19505 !'##molecule_type DNA !'##residues 1-240 ##label AIG !'##cross-references EMBL:X59720; GSPDB:GN00003; MIPS:YCR008w REFERENCE S22265 !$#authors Biteau, N.; Fremaux, C.; Hebrard, S.; Menara, A.; Aigle, M.; !1Crouzet, M. !$#journal Yeast (1992) 8:61-70 !$#title The complete sequence of a 10.8kb fragment to the right of !1the chromosome III centromere of Saccharomyces cerevisiae. !$#cross-references MUID:92254505; PMID:1580102 !$#accession S26737 !'##status translation not shown !'##molecule_type DNA !'##residues 1-240 ##label BIT !'##cross-references EMBL:X59720 REFERENCE S19420 !$#authors Goffeau, A.; Purnelle, B.; Skala, J. !$#submission submitted to the Protein Sequence Database, March 1992 !$#accession S19768 !'##molecule_type DNA !'##residues 237-603 ##label GOF !'##cross-references EMBL:X59720; GSPDB:GN00003; MIPS:YCR008w REFERENCE S25353 !$#authors Skala, J.; Purnelle, B.; Goffeau, A. !$#journal Yeast (1992) 8:409-417 !$#title The complete sequence of a 10.8 kb segment distal of SUF2 on !1the right arm of chromosome III from Saccharomyces !1cerevisiae reveals seven open reading frames including the !1RVS161, ADP1 and PGK genes. !$#cross-references MUID:92327849; PMID:1626432 !$#contents annotation GENETICS !$#gene SGD:SAT4; MIPS:YCR008w !'##cross-references SGD:S0000601; MIPS:YCR008w !$#map_position 3R CLASSIFICATION #superfamily probable protein kinase YCR008W; protein kinase !1homology KEYWORDS ATP; phosphotransferase; serine/threonine-specific protein !1kinase FEATURE !$314-588 #domain protein kinase homology #label KIN\ !$322-330 #region protein kinase ATP-binding motif\ !$353 #active_site Lys #status predicted SUMMARY #length 603 #molecular-weight 66665 #checksum 1220 SEQUENCE /// ENTRY A39723 #type complete TITLE protein kinase byr2 (EC 2.7.1.-) - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES protein kinase ste8 ORGANISM #formal_name Schizosaccharomyces pombe DATE 14-Feb-1992 #sequence_revision 14-Feb-1992 #text_change 15-Sep-2000 ACCESSIONS A39723; S30094; T39860; T40139 REFERENCE A39723 !$#authors Wang, Y.; Xu, H.P.; Riggs, M.; Rodgers, L.; Wigler, M. !$#journal Mol. Cell. Biol. (1991) 11:3554-3563 !$#title byr2, a Schizosaccharomyces pombe gene encoding a protein !1kinase capable of partial suppression of the ras1 mutant !1phenotype. !$#cross-references MUID:91260705; PMID:2046669 !$#accession A39723 !'##status preliminary !'##molecule_type DNA !'##residues 1-659 ##label WAN !'##cross-references GB:M74293; NID:g173352; PIDN:AAA35289.1; !1PID:g173353 REFERENCE S30094 !$#authors Styrkarsdottir, U.; Egel, R.; Nielsen, O. !$#journal Mol. Gen. Genet. (1992) 235:122-130 !$#title Functional conservation between Schizosaccharomyces pombe !1ste8 and Saccharomyces cerevisiae STE11 protein kinases in !1yeast signal transduction. !$#cross-references MUID:93062799; PMID:1435723 !$#accession S30094 !'##molecule_type DNA !'##residues 1-659 ##label STY !'##cross-references EMBL:X68851; NID:g5106; PIDN:CAA48731.1; PID:g5107 REFERENCE Z21886 !$#authors Wood, V.; Rajandream, M.A.; Barrell, B.G.; Skelton, J.; !1Churcher, C.M. !$#submission submitted to the EMBL Data Library, August 1997 !$#accession T39860 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-659 ##label WOO !'##cross-references EMBL:Z98270; PIDN:CAB10981.1; GSPDB:GN00067; !1SPDB:SPBC1D7.05c !'##experimental_source strain 972h-; cosmid c1D7 REFERENCE Z21907 !$#authors Wood, V.; Rajandream, M.A.; Barrell, B.G.; Skelton, J.; !1Churcher, C.M. !$#submission submitted to the EMBL Data Library, June 1997 !$#accession T40139 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 298-659 ##label WO2 !'##cross-references EMBL:Z97211; PIDN:CAB10150.1; GSPDB:GN00067; !1SPDB:SPBC2F12.01 !'##experimental_source strain 972h-; cosmid c2F12 GENETICS !$#gene byr2; ste8 !$#map_position 2 CLASSIFICATION #superfamily protein kinase byr2; protein kinase homology; !1SAM homology KEYWORDS ATP; phosphotransferase; serine/threonine-specific protein !1kinase FEATURE !$1-66 #domain SAM homology #label SAM\ !$392-658 #domain protein kinase homology #label KIN\ !$400-408 #region protein kinase ATP-binding motif SUMMARY #length 659 #molecular-weight 73632 #checksum 9418 SEQUENCE /// ENTRY S51380 #type complete TITLE protein kinase STE11 (EC 2.7.1.-) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein L8039.10; protein YLR362w ORGANISM #formal_name Saccharomyces cerevisiae DATE 23-Feb-1995 #sequence_revision 11-Aug-1995 #text_change 21-Jul-2000 ACCESSIONS S51380; A36456 REFERENCE S51377 !$#authors Du, Z. !$#submission submitted to the EMBL Data Library, December 1994 !$#description The sequence of S. cerevisiae cosmid 8039. !$#accession S51380 !'##molecule_type DNA !'##residues 1-738 ##label DUZ !'##cross-references EMBL:U19103; NID:g609404; PIDN:AAB67571.1; !1PID:g609414; GSPDB:GN00012; MIPS:YLR362w REFERENCE A36456 !$#authors Rhodes, N.; Connell, L.; Errede, B. !$#journal Genes Dev. (1990) 4:1862-1874 !$#title STE11 is a protein kinase required for cell-type-specific !1transcription and signal transduction in yeast. !$#cross-references MUID:91115076; PMID:2276621 !$#accession A36456 !'##molecule_type DNA !'##residues 1-717 ##label RHO !'##cross-references GB:X53431 GENETICS !$#gene SGD:STE11; MIPS:YLR362w !'##cross-references SGD:S0004354; MIPS:YLR362w !$#map_position 12R CLASSIFICATION #superfamily protein kinase byr2; protein kinase homology; !1SAM homology KEYWORDS ATP; phosphotransferase; protein kinase FEATURE !$38-104 #domain SAM homology #label SAM\ !$434-733 #domain protein kinase homology #label KIN\ !$442-450 #region protein kinase ATP-binding motif SUMMARY #length 738 #molecular-weight 83217 #checksum 2282 SEQUENCE /// ENTRY A37913 #type complete TITLE serine/threonine-specific protein kinase (EC 2.7.1.-) mik1 - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES mitosis inhibitor protein kinase ORGANISM #formal_name Schizosaccharomyces pombe DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Dec-1999 ACCESSIONS A37913; T40626 REFERENCE A37913 !$#authors Lundgren, K.; Walworth, N.; Booher, R.; Dembski, M.; !1Kirschner, M.; Beach, D. !$#journal Cell (1991) 64:1111-1122 !$#title mik1 and wee1 cooperate in the inhibitory tyrosine !1phosphorylation of cdc2. !$#cross-references MUID:91168259; PMID:1706223 !$#accession A37913 !'##status preliminary !'##molecule_type mRNA !'##residues 1-581 ##label LUN !'##cross-references GB:M60834; NID:g173413; PIDN:AAA91278.1; !1PID:g1213637 REFERENCE Z21941 !$#authors Lyne, M.; Rajandream, M.A.; Barrell, B.G.; Rieger, M. !$#submission submitted to the EMBL Data Library, December 1998 !$#accession T40626 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-581 ##label LYN !'##cross-references EMBL:AL034563; PIDN:CAA22534.1; GSPDB:GN00067; !1SPDB:SPBC660.14 !'##experimental_source strain 972h-; cosmid c660 GENETICS !$#gene SPBC660.14 !$#map_position 2 !$#introns 403/3 CLASSIFICATION #superfamily fission yeast mik1 protein; protein kinase !1homology KEYWORDS ATP; phosphotransferase; serine/threonine-specific protein !1kinase FEATURE !$287-558 #domain protein kinase homology #label KIN SUMMARY #length 581 #molecular-weight 65933 #checksum 1243 SEQUENCE /// ENTRY A34076 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112) receptor type eph 1 precursor - human ALTERNATE_NAMES receptor tyrosine kinase eph ORGANISM #formal_name Homo sapiens #common_name man DATE 22-Oct-1999 #sequence_revision 22-Oct-1999 #text_change 04-Feb-2000 ACCESSIONS A34076; S44280 REFERENCE A34076 !$#authors Hirai, H.; Maru, Y.; Hagiwara, K.; Nishida, J.; Takaku, F. !$#journal Science (1987) 238:1717-1720 !$#title A novel putative tyrosine kinase receptor encoded by the eph !1gene. !$#cross-references MUID:88070650; PMID:2825356 !$#accession A34076 !'##molecule_type mRNA !'##residues 1-984 ##label HIR !'##cross-references GB:M18391; NID:g339716; PIDN:AAA36747.1; !1PID:g339717 !'##note the sequence in GenBank entry HUMTKR, release 111.0, has the !1codons GCG for 398-Ala rather than the published GGG, and !1GCA for 716-Gly rather than the published GGA REFERENCE S44280 !$#authors Tuzi, N.L. !$#submission submitted to the EMBL Data Library, November 1993 !$#description An EGFR/eph chimeric receptor possesses ligand stimulated !1tyrosine kinase activity and promotes cell growth. !$#accession S44280 !'##molecule_type mRNA !'##residues 286-397,'A',399-580,'QRDRATDVDREDKLWLKPYVDLQAYEDPAQGALDF', !1583,625-984 ##label TUZ !'##cross-references EMBL:Z27409; NID:g482916; PIDN:CAA81796.1; !1PID:g482917 GENETICS !$#gene GDB:EPHT1; EPH; EPHT !'##cross-references GDB:119875; OMIM:179610 !$#map_position 7q32-7q36 CLASSIFICATION #superfamily protein-tyrosine kinase, receptor type eph; !1fibronectin type III repeat homology; protein kinase !1homology; SAM homology KEYWORDS ATP; autophosphorylation; glycoprotein; kinase-related !1transforming protein; phosphoprotein; phosphotransferase; !1transmembrane protein; tyrosine-specific protein kinase FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-984 #product protein-tyrosine kinase receptor type eph 1 !8#status predicted #label MAT\ !$548-568 #domain transmembrane #status predicted #label TMM\ !$630-895 #domain protein kinase homology #label KIN\ !$638-646 #region protein kinase ATP-binding motif\ !$918-984 #domain SAM homology #label SAM\ !$59,338,414,478 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 984 #molecular-weight 108802 #checksum 5598 SEQUENCE /// ENTRY H69878 #type complete TITLE probable protein kinase (EC 2.7.1.-) yloP - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS H69878 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69878 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-648 ##label KUN !'##cross-references GB:Z99112; GB:AL009126; NID:g2633902; !1PIDN:CAB13450.1; PID:g2633949 !'##experimental_source strain 168 GENETICS !$#gene yloP CLASSIFICATION #superfamily Bacillus subtilis probable protein kinase yloP; !1protein kinase homology KEYWORDS ATP; phosphotransferase; protein kinase FEATURE !$9-269 #domain protein kinase homology #label KIN SUMMARY #length 648 #molecular-weight 71866 #checksum 3689 SEQUENCE /// ENTRY A25962 #type complete TITLE mitosis inhibitor protein kinase wee1 - fission yeast (Schizosaccharomyces pombe) CONTAINS probable serine/threonine-specific protein kinase (EC 2.7.1.-) ORGANISM #formal_name Schizosaccharomyces pombe DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Dec-1999 ACCESSIONS A25962; T41196 REFERENCE A25962 !$#authors Russell, P.; Nurse, P. !$#journal Cell (1987) 49:559-567 !$#title Negative regulation of mitosis by wee1+, a gene encoding a !1protein kinase homolog. !$#cross-references MUID:87187653; PMID:3032459 !$#accession A25962 !'##molecule_type DNA !'##residues 1-877 ##label RUS !'##cross-references GB:M16508; NID:g173531; PIDN:AAA35354.1; !1PID:g173532 REFERENCE Z21978 !$#authors Wood, V.; Rajandream, M.A.; Barrell, B.G.; Jimenez Martinez, !1J. !$#submission submitted to the EMBL Data Library, July 1999 !$#accession T41196 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-877 ##label WOO !'##cross-references EMBL:AL109736; PIDN:CAB52150.1; GSPDB:GN00068 !'##experimental_source strain 972h-; cosmid c18B5 GENETICS !$#gene SPBC18B5.03 !$#map_position 3 CLASSIFICATION #superfamily fission yeast mitosis inhibitor wee1+; protein !1kinase homology KEYWORDS ATP; phosphotransferase; serine/threonine-specific protein !1kinase FEATURE !$564-840 #domain protein kinase homology #label KIN SUMMARY #length 877 #molecular-weight 96260 #checksum 324 SEQUENCE /// ENTRY S37869 #type complete TITLE probable serine/threonine-specific protein kinase (EC 2.7.1.-) ELM1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YKL048c; protein YKL261 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 12-Nov-1999 ACCESSIONS S37869; S40656; S27425; A54690 REFERENCE S37851 !$#authors Purnelle, B.; Skala, J.; van Dyck, L.; Tettelin, H.; !1Goffeau, A. !$#submission submitted to the Protein Sequence Database, March 1994 !$#accession S37869 !'##molecule_type DNA !'##residues 1-640 ##label PUR !'##cross-references EMBL:Z28048; NID:g486146; PIDN:CAA81883.1; !1PID:g486147; GSPDB:GN00011; MIPS:YKL048c !'##experimental_source strain S288C REFERENCE S40650 !$#authors Purnelle, B.; Tettelin, H.; van Dyck, L.; Skala, J.; !1Goffeau, A. !$#journal Yeast (1993) 9:1379-1384 !$#title The sequence of a 17.5 kb DNA fragment on the left arm of !1yeast chromosome XI identifies the protein kinase gene ELM1, !1the DNA primase gene PRI2, a new gene encoding a putative !1histone and seven new open reading frames. !$#cross-references MUID:94205268; PMID:8154189 !$#accession S40656 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-640 ##label PU2 !'##cross-references EMBL:X71621 !'##experimental_source strain S288C REFERENCE S27425 !$#authors Myers, A.M.; Blacketer, M.J.; Madaule, P. !$#submission submitted to the EMBL Data Library, December 1991 !$#description The yeast gene ELM1 codes for a protein kinase homolog !1required for normal cell morphology. !$#accession S27425 !'##molecule_type DNA !'##residues 1-389,'Y',391-483,'SD',486-538,'KRVILSFVI',540,'NPNTYQ', !1543-544,'D',548,'TKEF',550 ##label MYE !'##cross-references EMBL:M81258; NID:g171451; PIDN:AAA02892.1; !1PID:g171452 REFERENCE A54690 !$#authors Blacketer, M.J.; Koehler, C.M.; Coats, S.G.; Myers, A.M.; !1Madaule, P. !$#journal Mol. Cell. Biol. (1993) 13:5567-5581 !$#title Regulation of dimorphism in Saccharomyces cerevisiae: !1involvement of the novel protein kinase homolog Elm1p and !1protein phosphatase 2A. !$#cross-references MUID:93360991; PMID:8395007 !$#accession A54690 !'##status preliminary; nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-389,'Y',391-483,'SD',486-538,'KRVILSFVIEN',550, !1'NTYQSHDKT',560,'EF',563 ##label BLA !'##cross-references GB:M81258; NID:g171451; PIDN:AAA02892.1; !1PID:g171452 !'##note authors translated the codon TAT for residue 390 as Glu, and !1TCG for residue 484 as Thr GENETICS !$#gene SGD:ELM1; MIPS:YKL048c !'##cross-references SGD:S0001531; MIPS:YKL048c !$#map_position 11L CLASSIFICATION #superfamily yeast probable protein kinase ELM1; protein !1kinase homology KEYWORDS ATP; phosphotransferase; serine/threonine-specific protein !1kinase FEATURE !$86-409 #domain protein kinase homology #label KIN SUMMARY #length 640 #molecular-weight 72149 #checksum 1183 SEQUENCE /// ENTRY S64767 #type complete TITLE probable serine/threonine-specific protein kinase (EC 2.7.1.-) KNS1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein L1224; protein YLL019c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S64767; S17245; S69387; S30783 REFERENCE S64761 !$#authors Goffeau, A.; Purnelle, B. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64767 !'##molecule_type DNA !'##residues 1-737 ##label GOF !'##cross-references EMBL:Z73125; NID:g1360192; PIDN:CAA97468.1; !1PID:g1360194; GSPDB:GN00012; MIPS:YLL019c !'##experimental_source strain S288C REFERENCE S17245 !$#authors Padmanabha, R.; Gehrung, S.; Snyder, M. !$#journal Mol. Gen. Genet. (1991) 229:1-9 !$#title The KNS1 gene of Saccharomyces cerevisiae encodes a !1nonessential protein kinase homologue that is distantly !1related to members of the CDC28/cdc2 gene family. !$#cross-references MUID:91375437; PMID:1910150 !$#accession S17245 !'##molecule_type DNA !'##residues 17-410,'GS',413,'AL',417,'SGHC',422-737 ##label PAD !'##cross-references EMBL:M85200 REFERENCE S69380 !$#authors Purnelle, B.; Goffeau, A. !$#submission submitted to the EMBL Data Library, April 1996 !$#description The sequence of 32 kb on the left arm of yeast chromosome !1XII reveals 14 open reading frames among which HSP104, SSA2, !1SPA2, KNS1, DPS1/APS, SDC25, a new member of the !1seripauperins family and a new ABC transporter homologous to !1the human multidrug resistance protein. !$#accession S69387 !'##molecule_type DNA !'##residues 1-737 ##label PUR !'##cross-references EMBL:X97560; NID:g1297003; PIDN:CAA66171.1; !1PID:g1297011 GENETICS !$#gene SGD:KNS1; MIPS:YLL019c !'##cross-references SGD:S0003942; MIPS:YLL019c !$#map_position 12L CLASSIFICATION #superfamily yeast probable protein kinase KNS1; protein !1kinase homology KEYWORDS ATP; phosphotransferase; serine/threonine-specific protein !1kinase FEATURE !$311-606 #domain protein kinase homology #label KIN SUMMARY #length 737 #molecular-weight 83842 #checksum 9768 SEQUENCE /// ENTRY S47452 #type complete TITLE probable serine/threonine-specific protein kinase (EC 2.7.1.-) YMR291w - yeast (Saccharomyces cerevisiae) ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S47452 REFERENCE S47445 !$#authors Barrell, B.G. !$#submission submitted to the EMBL Data Library, August 1994 !$#accession S47452 !'##molecule_type DNA !'##residues 1-586 ##label BAR !'##cross-references EMBL:X80836; NID:g1289327; PIDN:CAA56800.1; !1PID:g530348; GSPDB:GN00013; MIPS:YMR291w GENETICS !$#gene MIPS:YMR291w !'##cross-references SGD:S0004905 !$#map_position 13R CLASSIFICATION #superfamily yeast probable protein kinase YMR291w; protein !1kinase homology KEYWORDS ATP; phosphotransferase; serine/threonine-specific protein !1kinase FEATURE !$37-351 #domain protein kinase homology #label KIN SUMMARY #length 586 #molecular-weight 66219 #checksum 5460 SEQUENCE /// ENTRY S45285 #type complete TITLE probable serine/threonine-specific protein kinase (EC 2.7.1.-) - Entamoeba histolytica ORGANISM #formal_name Entamoeba histolytica DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S45285 REFERENCE S45285 !$#authors Lohia, A.; Samuelson, J. !$#journal Biochim. Biophys. Acta (1994) 1222:122-124 !$#title Molecular cloning of an Entamoeba histolytica gene encoding !1a putative mos family serine/threonine-kinase. !$#cross-references MUID:94242791; PMID:8186259 !$#accession S45285 !'##status preliminary !'##molecule_type DNA !'##residues 1-290 ##label LOH !'##cross-references EMBL:L05668; NID:g158974; PIDN:AAA19876.1; !1PID:g158975 !'##note the authors translated the codon TTA for residue 177 as Ser, !1ATG for residue 178 as Leu, and ACA for residue 179 as Met CLASSIFICATION #superfamily Entamoeba histolytica serine/threonine-specific !1protein kinase; protein kinase homology KEYWORDS ATP; phosphotransferase; serine/threonine-specific protein !1kinase FEATURE !$20-285 #domain protein kinase homology #label KIN SUMMARY #length 290 #molecular-weight 33541 #checksum 256 SEQUENCE /// ENTRY JE0201 #type complete TITLE protein-tyrosine kinase (EC 2.7.1.112), receptor type DjPTK1 - planarian (Dugesia japonica) ORGANISM #formal_name Dugesia japonica DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS JE0201 REFERENCE JE0201 !$#authors Ogawa, K.; Wakayama, A.; Kunisada, T.; Orii, H.; Watanabe, !1K.; Agata, K. !$#journal Biochem. Biophys. Res. Commun. (1998) 248:204-209 !$#title Identification of a receptor tyrosine kinase involved in !1germ cell differentiation in planarians. !$#cross-references MUID:98340876; PMID:9675112 !$#accession JE0201 !'##molecule_type mRNA !'##residues 1-666 ##label OGA !'##cross-references DDBJ:AB014508; NID:g3395376; PIDN:BAA32059.1; !1PID:g3395377 COMMENT This protein belongs to the FGFR/PDGF family. GENETICS !$#gene DjPTK1 !$#start_codon TTG CLASSIFICATION #superfamily planarian receptor protein tyrosine kinase !1DjPTK1; protein kinase homology KEYWORDS ATP; phosphotransferase; tyrosine-specific protein kinase FEATURE !$362-643 #domain protein kinase homology #label KIN SUMMARY #length 666 #molecular-weight 75901 #checksum 5301 SEQUENCE /// ENTRY S44734 #type complete TITLE probable protein-tyrosine kinase (EC 2.7.1.112) - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 31-Mar-2000 ACCESSIONS S44734 REFERENCE S44732 !$#authors Wilson, R. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Sequence of the C. elegans cosmid B0523. !$#accession S44734 !'##status preliminary !'##molecule_type DNA !'##residues 1-363 ##label WIL !'##cross-references EMBL:L07143 GENETICS !$#introns 158/3; 262/3; 321/3 CLASSIFICATION #superfamily Caenorhabditis elegans tyrosine kinase; protein !1kinase homology KEYWORDS ATP; phosphotransferase; tyrosine-specific protein kinase FEATURE !$132-359 #domain protein kinase homology #label KIN SUMMARY #length 363 #molecular-weight 41013 #checksum 2247 SEQUENCE /// ENTRY KIECM #type complete TITLE homoserine kinase (EC 2.7.1.39) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 22-May-1981 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS S56630; C64720; A00658; S40532 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56630 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-310 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97302.1; !1PID:g537246 !'##experimental_source strain K-12, substrain MG1655 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64720 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-310 ##label BLAT !'##cross-references GB:AE000111; GB:U00096; NID:g1786181; !1PIDN:AAC73114.1; PID:g1786184; UWGP:b0003 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A00658 !$#authors Cossart, P.; Katinka, M.; Yaniv, M. !$#journal Nucleic Acids Res. (1981) 9:339-347 !$#title Nucleotide sequence of the thrB gene of Escherichia coli, !1and its two adjacent regions; the thrAB and thrBC junctions. !$#cross-references MUID:81150470; PMID:6259626 !$#accession A00658 !'##molecule_type DNA !'##residues 1-165,'Q',167,'LMSGCGCWRIRGLKSRRQKQGY',191-310 ##label COS REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40532 !'##molecule_type DNA !'##residues 1-41,'Q',43-165,'Q',167,'LMSGCGCSRIRGLKSRRQKQGY',191-310 !1##label YUR !'##cross-references EMBL:D10483; NID:g216434; PIDN:BAA01287.1; !1PID:g216436 !'##experimental_source strain K-12 GENETICS !$#gene thrB !$#map_position 0 min FUNCTION !$#description catalyzes the conversion of homoserine to phosphohomoserine !1using ATP !$#pathway threonine biosynthesis CLASSIFICATION #superfamily homoserine kinase KEYWORDS ATP; phosphotransferase; threonine biosynthesis SUMMARY #length 310 #molecular-weight 33623 #checksum 3454 SEQUENCE /// ENTRY KIFKMG #type complete TITLE homoserine kinase (EC 2.7.1.39) - Corynebacterium glutamicum ORGANISM #formal_name Corynebacterium glutamicum DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 11-Jun-1999 ACCESSIONS S00866; S18261; S07385 REFERENCE S00865 !$#authors Peoples, O.P.; Liebl, W.; Bodis, M.; Maeng, P.J.; Follettie, !1M.T.; Archer, J.A.; Sinskey, A.J. !$#journal Mol. Microbiol. (1988) 2:63-72 !$#title Nucleotide sequence and fine structural analysis of the !1Corynebacterium glutamicum hom-thrB operon. !$#cross-references MUID:88216182; PMID:2835591 !$#accession S00866 !'##molecule_type DNA !'##residues 1-309 ##label PEO !'##cross-references EMBL:Y00546; NID:g40502; PIDN:CAA68615.1; !1PID:g40504 !$#accession S18261 !'##molecule_type protein !'##residues 2-11 ##label PEO2 REFERENCE S07385 !$#authors Mateos, L.M.; del Real, G.; Aguilar, A.; Martin, J.F. !$#journal Nucleic Acids Res. (1987) 15:3922 !$#title Nucleotide sequence of the homoserine kinase (thr B) gene of !1Brevibacterium lactofermentum. !$#cross-references MUID:87231082; PMID:3035505 !$#accession S07385 !'##molecule_type DNA !'##residues 1-245,'V',247-309 ##label MATE !'##cross-references EMBL:Y00140; NID:g39587; PIDN:CAA68332.1; !1PID:g39588 !'##note the source is designated as Brevibacterium lactofermentum GENETICS !$#gene thrB CLASSIFICATION #superfamily homoserine kinase KEYWORDS ATP; phosphotransferase FEATURE !$2-309 #product homoserine kinase #status experimental !8#label MAT SUMMARY #length 309 #molecular-weight 32620 #checksum 3732 SEQUENCE /// ENTRY S27981 #type complete TITLE homoserine kinase (EC 2.7.1.39) - Pseudomonas aeruginosa ORGANISM #formal_name Pseudomonas aeruginosa DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 11-Jun-1999 ACCESSIONS S27981; S19920 REFERENCE S27979 !$#authors Clepet, C.; Borne, F.; Krishnapillai, V.; Baird, C.; Patte, !1J.C.; Cami, B. !$#journal Mol. Microbiol. (1992) 6:3109-3119 !$#title Isolation, organization and expression of the Pseudomonas !1aeruginosa threonine genes. !$#cross-references MUID:93086420; PMID:1333566 !$#accession S27981 !'##molecule_type DNA !'##residues 1-316 ##label CLE !'##cross-references EMBL:X65034; NID:g45424; PIDN:CAA46169.1; !1PID:g45425 GENETICS !$#gene thrB !$#map_position 10 min CLASSIFICATION #superfamily Pseudomonas homoserine kinase KEYWORDS phosphotransferase; threonine biosynthesis SUMMARY #length 316 #molecular-weight 35279 #checksum 4340 SEQUENCE /// ENTRY KIHUPR #type complete TITLE pyruvate kinase (EC 2.7.1.40), erythrocyte splice form R - human ALTERNATE_NAMES PK-R-type isozyme; pyruvate kinase isoform R (erythroid) ORGANISM #formal_name Homo sapiens #common_name man DATE 01-Dec-1989 #sequence_revision 05-Dec-1997 #text_change 26-Feb-1999 ACCESSIONS I52269; A40991; PN0451 REFERENCE I52269 !$#authors Kanno, H.; Fujii, H.; Miwa, S. !$#journal Biochem. Biophys. Res. Commun. (1992) 188:516-523 !$#title Structural analysis of human Pyruvate kinase L-gene and !1identification of the promoter activity in Erythroid cells. !$#cross-references MUID:93075125; PMID:1445295 !$#accession I52269 !'##status nucleic acid sequence not shown; translation not shown; !1translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-33,'VPLTTQQCGADPQRGRPREVCSGME',34-574 ##label KAN !'##cross-references GB:D13243; NID:g220048; PID:g220050 !'##note following the authors' interpretation the GenBank sequence uses !1an intron with non-standard splice boundaries REFERENCE A40991 !$#authors Kanno, H.; Fujii, H.; Hirono, A.; Miwa, S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:8218-8221 !$#title cDNA cloning of human R-type pyruvate kinase and !1identification of a single amino acid substitution (Thr(384) !1--> Met) affecting enzymatic stability in a pyruvate kinase !1variant (PK Tokyo) associated with hereditary hemolytic !1anemia. !$#cross-references MUID:91376115; PMID:1896471 !$#accession A40991 !'##molecule_type mRNA !'##residues 1-37;570-574 ##label KA3 !'##cross-references GB:D90465 !'##experimental_source reticulocyte cDNA library REFERENCE PN0451 !$#authors Kanno, H.; Fujii, H.; Tsujino, G.; Miwa, S. !$#journal Biochem. Biophys. Res. Commun. (1993) 192:46-52 !$#title Molecular basis of impaired pyruvate kinase isozyme !1conversion in erythriod cells: A single amino acid !1substitution near the active site and decreased mRNA content !1of the R-type PK. !$#cross-references MUID:93236593; PMID:8476433 !$#accession PN0451 !'##molecule_type mRNA !'##residues 365-380,'P',382-431 ##label KA2 GENETICS !$#gene GDB:PKLR !'##cross-references GDB:120294; OMIM:266200 !$#map_position 1q21-1q21 !$#introns 34/1; 95/1; 125/3; 169/3; 232/1; 322/2; 372/3; 423/3; 479/2; !1540/1 !$#note alternative promoters are used for the erythrocyte (R) and !1hepatic (L) forms COMPLEX homotetramer FUNCTION !$#description catalyzes the transphosphorylation of phosphoenolpyruvate !1and ADP to pyruvic acid and ATP !$#pathway glycolysis CLASSIFICATION #superfamily pyruvate kinase KEYWORDS alternative initiators; alternative splicing; ATP !1biosynthesis; erythrocyte; glycolysis; homotetramer; !1magnesium; metalloprotein; phosphoprotein; !1phosphotransferase; potassium FEATURE !$43 #binding_site phosphate (Ser) (covalent) (by !8cAMP-dependent kinase) #status predicted\ !$116,286,337 #binding_site substrate phosphate (Arg, Ser, Arg) !8#status predicted\ !$313 #active_site Lys #status predicted\ !$315,336,337 #binding_site magnesium (Glu, Ala, Arg) #status !8predicted\ !$372,407 #binding_site potassium (Gln, Glu) #status predicted SUMMARY #length 574 #molecular-weight 61804 #checksum 7891 SEQUENCE /// ENTRY KIHUPL #type complete TITLE pyruvate kinase (EC 2.7.1.40), hepatic splice form L - human ALTERNATE_NAMES PK-L-type isozyme; pyruvate kinase isoform L (liver) ORGANISM #formal_name Homo sapiens #common_name man DATE 01-Dec-1989 #sequence_revision 05-Dec-1997 #text_change 11-Jun-1999 ACCESSIONS I52269; A30150; A29414; PN0451 REFERENCE I52269 !$#authors Kanno, H.; Fujii, H.; Miwa, S. !$#journal Biochem. Biophys. Res. Commun. (1992) 188:516-523 !$#title Structural analysis of human Pyruvate kinase L-gene and !1identification of the promoter activity in Erythroid cells. !$#cross-references MUID:93075125; PMID:1445295 !$#accession I52269 !'##status nucleic acid sequence not shown; translation not shown; !1translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 'MSIQENISSLQLRSWVSKSQRDLAKSILIGAPGVPLTTQQCGADPQRGRPREVCSG', !11-543 ##label KAN !'##cross-references GB:D13243; NID:g220048; PID:g220050 !'##note following the authors' interpretation the GenBank translation !1starts with the R form initiator and uses an intron with !1non-standard splice boundaries REFERENCE A30150 !$#authors Tani, K.; Fujii, H.; Nagata, S.; Miwa, S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:1792-1795 !$#title Human liver type pyruvate kinase: complete amino acid !1sequence and the expression in mammalian cells. !$#cross-references MUID:88158079; PMID:3126495 !$#accession A30150 !'##molecule_type mRNA !'##residues 1-98,'T',100-200,'S',202-349,'P',351-391,'R',393-543 !1##label TAN1 !'##cross-references EMBL:M15465; NID:g189995; PIDN:AAA60104.1; !1PID:g189996 REFERENCE A29414 !$#authors Tani, K.; Fujii, H.; Tsutsumi, H.; Sukegawa, J.; Toyoshima, !1K.; Yoshida, M.C.; Noguchi, T.; Tanaka, T.; Miwa, S. !$#journal Biochem. Biophys. Res. Commun. (1987) 143:431-438 !$#title Human liver type pyruvate kinase: cDNA cloning and !1chromosomal assignment. !$#cross-references MUID:87184521; PMID:3566732 !$#accession A29414 !'##molecule_type mRNA !'##residues 439-543 ##label TAN2 !'##cross-references GB:J03640; NID:g189995 GENETICS !$#gene GDB:PKLR !'##cross-references GDB:120294; OMIM:266200 !$#map_position 1q21-1q21 !$#introns 3/1; 64/1; 94/3; 138/3; 201/1; 291/2; 341/3; 392/3; 448/2; !1509/1 !$#note alternative promoters are used for the erythrocyte (R) and !1hepatic (L) forms COMPLEX homotetramer FUNCTION !$#description catalyzes the transphosphorylation of phosphoenolpyruvate !1and ADP to pyruvic acid and ATP !$#pathway glycolysis; gluconeogenesis CLASSIFICATION #superfamily pyruvate kinase KEYWORDS alternative initiators; alternative splicing; ATP !1biosynthesis; gluconeogenesis; glycolysis; homotetramer; !1liver; magnesium; metalloprotein; phosphoprotein; !1phosphotransferase; potassium FEATURE !$12 #binding_site phosphate (Ser) (covalent) (by !8cAMP-dependent kinase) #status predicted\ !$85,255,306 #binding_site substrate phosphate (Arg, Ser, Arg) !8#status predicted\ !$282 #active_site Lys #status predicted\ !$284,305,306 #binding_site magnesium (Glu, Ala, Arg) #status !8predicted\ !$341,376 #binding_site potassium (Gln, Glu) #status predicted SUMMARY #length 543 #molecular-weight 58468 #checksum 242 SEQUENCE /// ENTRY KIRTPR #type complete TITLE pyruvate kinase (EC 2.7.1.40), erythrocyte splice form R - rat ALTERNATE_NAMES phosphoenol transphosphorylase, R type ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 05-Dec-1997 ACCESSIONS A27427 REFERENCE A27427 !$#authors Noguchi, T.; Yamada, K.; Inoue, H.; Matsuda, T.; Tanaka, T. !$#journal J. Biol. Chem. (1987) 262:14366-14371 !$#title The L- and R-type isozymes of rat pyruvate kinase are !1produced from a single gene by use of different promoters. !$#cross-references MUID:88007696; PMID:3654663 !$#accession A27427 !'##molecule_type DNA !'##residues 1-574 ##label NOG !'##cross-references GB:M17091; GB:J03455; NID:g206211 GENETICS !$#gene L-PK !$#introns 34/1; 95/1; 125/3; 169/3; 232/1; 322/2; 372/3; 423/3; 479/2; !1540/1 !$#note alternative promoters are used for the erythrocyte (R) and !1hepatic (L) forms COMPLEX homotetramer FUNCTION !$#description catalyzes the transphosphorylation of phosphoenolpyruvate !1and ADP to pyruvic acid and ATP !$#pathway glycolysis CLASSIFICATION #superfamily pyruvate kinase KEYWORDS alternative initiators; alternative splicing; ATP !1biosynthesis; erythrocyte; glycolysis; homotetramer; !1magnesium; metalloprotein; phosphoprotein; !1phosphotransferase; potassium FEATURE !$43 #binding_site phosphate (Ser) (covalent) (by !8cAMP-dependent kinase) #status predicted\ !$116,286,337 #binding_site substrate phosphate (Arg, Ser, Arg) !8#status predicted\ !$313 #active_site Lys #status predicted\ !$315,336,337 #binding_site magnesium (Glu, Ala, Arg) #status !8predicted\ !$372,407 #binding_site potassium (Gln, Glu) #status predicted SUMMARY #length 574 #molecular-weight 62199 #checksum 8520 SEQUENCE /// ENTRY KIRTPL #type complete TITLE pyruvate kinase (EC 2.7.1.40), hepatic splice form L - rat ALTERNATE_NAMES L-type pyruvate kinase; phosphoenol transphosphorylase, L type ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1989 #sequence_revision 01-Dec-2000 #text_change 01-Dec-2000 ACCESSIONS A92940; A91160; A23612; A24873; A27392 REFERENCE A92940 !$#authors Cognet, M.; Lone, Y.C.; Vaulont, S.; Kahn, A.; Marie, J. !$#journal J. Mol. Biol. (1987) 196:11-25 !$#title Structure of the rat L-type pyruvate kinase gene. !$#cross-references MUID:88011310; PMID:3309348 !$#accession A92940 !'##molecule_type DNA !'##residues 1-543 ##label COG !'##cross-references GB:X05684; NID:g56604; PIDN:CAA29169.1; PID:g297533 REFERENCE A91160 !$#authors Inoue, H.; Noguchi, T.; Tanaka, T. !$#journal Eur. J. Biochem. (1986) 154:465-469 !$#title Complete amino acid sequence of rat L-type pyruvate kinase !1deduced from the cDNA sequence. !$#cross-references MUID:86108360; PMID:3002799 !$#accession A91160 !'##molecule_type mRNA !'##residues 1-543 ##label INO !'##cross-references GB:M17685; GB:X03403; GB:X03430; NID:g206201; !1PIDN:AAA41881.1; PID:g206202 REFERENCE A23612 !$#authors Lone, Y.C.; Simon, M.P.; Kahn, A.; Marie, J. !$#journal FEBS Lett. (1986) 195:97-100 !$#title Complete nucleotide and deduced amino acid sequences of rat !1L-type pyruvate kinase. !$#cross-references MUID:86108907; PMID:3080337 !$#accession A23612 !'##molecule_type mRNA !'##residues 1-466,'G',468-469,'K',471-543 ##label LON !'##cross-references GB:M11709; GB:X03403; GB:X03430; NID:g206198; !1PIDN:AAA41880.1; PID:g206199 !'##note the authors translated the codon GGA for residue 467 as Arg COMMENT This splice form is specific to the liver, kidney, and small !1intestine. GENETICS !$#gene L-PK !$#introns 3/1; 64/1; 94/3; 138/3; 201/1; 291/2; 341/3; 392/3; 448/2; !1509/1 !$#note alternative promoters are used for the erythrocyte (R) and !1hepatic (L) forms COMPLEX homotetramer FUNCTION !$#description catalyzes the transphosphorylation of phosphoenolpyruvate !1and ADP to pyruvic acid and ATP !$#pathway glycolysis; gluconeogenesis CLASSIFICATION #superfamily pyruvate kinase KEYWORDS alternative initiators; alternative splicing; ATP !1biosynthesis; gluconeogenesis; glycolysis; homotetramer; !1liver; magnesium; metalloprotein; phosphoprotein; !1phosphotransferase; potassium FEATURE !$12 #binding_site phosphate (Ser) (covalent) (by !8cAMP-dependent kinase) #status predicted\ !$85,255,306 #binding_site substrate phosphate (Arg, Ser, Arg) !8#status predicted\ !$282 #active_site Lys #status predicted\ !$284,305,306 #binding_site magnesium (Glu, Ala, Arg) #status !8predicted\ !$341,376 #binding_site potassium (Gln, Glu) #status predicted SUMMARY #length 543 #molecular-weight 58703 #checksum 2363 SEQUENCE /// ENTRY S30038 #type complete TITLE pyruvate kinase (EC 2.7.1.40), muscle splice form M2 - human ALTERNATE_NAMES ATP:2-O-phosphotransferase; cytosolic thyroid hormone-binding protein p58; phosphoenol transphosphorylase; phosphoenolpyruvate kinase; pyruvate kinase M2 isozyme ORGANISM #formal_name Homo sapiens #common_name man DATE 08-Dec-1993 #sequence_revision 10-Nov-1995 #text_change 11-Jun-1999 ACCESSIONS S30038; JT0486; A33983 REFERENCE S16071 !$#authors Takenaka, M.; Noguchi, T.; Sadahiro, S.; Hirai, H.; Yamada, !1K.; Matsuda, T.; Imai, E.; Tanaka, T. !$#journal Eur. J. Biochem. (1991) 198:101-106 !$#title Isolation and characterization of the human pyruvate kinase !1M gene. !$#cross-references MUID:91249787; PMID:2040271 !$#accession S30038 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-531 ##label TAK !'##cross-references EMBL:X56494; NID:g35504; PIDN:CAA39849.1; !1PID:g35505 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1990 REFERENCE JT0486 !$#authors Tani, K.; Yoshida, M.C.; Satoh, H.; Mitamura, K.; Noguchi, !1T.; Tanaka, T.; Fujii, H.; Miwa, S. !$#journal Gene (1988) 73:509-516 !$#title Human M2-type pyruvate kinase: cDNA cloning, chromosomal !1assignment and expression in hepatoma. !$#cross-references MUID:89211988; PMID:2854097 !$#accession JT0486 !'##molecule_type mRNA !'##residues 1-338,'R',340-378,'N',380-531 ##label TAN !'##cross-references GB:M23725; NID:g189997; PIDN:AAA36449.1; !1PID:g189998 !'##note translation of initiator Met is not shown REFERENCE A33983 !$#authors Kato, H.; Fukuda, T.; Parkison, C.; McPhie, P.; Cheng, S.Y. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:7861-7865 !$#title Cytosolic thyroid hormone-binding protein is a monomer of !1pyruvate kinase. !$#cross-references MUID:90046696; PMID:2813362 !$#accession A33983 !'##molecule_type mRNA !'##residues 1-102,'Y',104-131,'L',133-338,'R',340-531 ##label KAT !'##cross-references GB:M26252; NID:g338826; PIDN:AAA36672.1; !1PID:g338827 !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing COMMENT Splice form M2 is found at least as a minor form in all !1adult tissues, and as the only form in fetal tissues. It is !1replaced as the major form in adult skeletal muscle, heart !1and brain by splice form M1. GENETICS !$#gene GDB:PKM2 !'##cross-references GDB:120295; OMIM:179050 !$#map_position 15q22.2-q22.3 !$#introns 52/1; 82/3; 126/3; 189/1; 279/2; 329/3; 380/3; 436/2; 497/1 COMPLEX monomer; homotetramer in the presence of fructose 1, !16-bisphosphate FUNCTION !$#description catalyzes the transphosphorylation of phosphoenolpyruvate !1and ADP to pyruvic acid and ATP !$#pathway glycolysis !$#note catalytic activity is inhibited by the specific binding of !1thyroid hormone to the monomeric form CLASSIFICATION #superfamily pyruvate kinase KEYWORDS acetylated amino end; alternative splicing; ATP !1biosynthesis; glycolysis; homotetramer; magnesium; !1metalloprotein; monomer; muscle; phosphotransferase; !1potassium FEATURE !$2-531 #product pyruvate kinase muscle splice form M2 !8#status predicted #label MAT\ !$2 #modified_site blocked amino end (Ser) (in mature !8form) (probably acetylated) #status experimental\ !$73,243,294 #binding_site substrate phosphate (Arg, Ser, Arg) !8#status predicted\ !$270 #active_site Lys #status predicted\ !$272,293,294 #binding_site magnesium (Glu, Ala, Arg) #status !8predicted\ !$329,364 #binding_site potassium (Gln, Glu) #status predicted SUMMARY #length 531 #molecular-weight 57877 #checksum 7902 SEQUENCE /// ENTRY S64635 #type complete TITLE pyruvate kinase (EC 2.7.1.40), muscle splice form M1 - human ALTERNATE_NAMES pyruvate kinase isozyme M1 ORGANISM #formal_name Homo sapiens #common_name man DATE 16-May-1996 #sequence_revision 24-May-1996 #text_change 05-Dec-1997 ACCESSIONS S64635; S16071 REFERENCE S64635 !$#authors Takenaka, M. !$#submission submitted to the EMBL Data Library, November 1990 !$#accession S64635 !'##molecule_type DNA !'##residues 1-531 ##label TAK !'##cross-references EMBL:X56494 REFERENCE S16071 !$#authors Takenaka, M.; Noguchi, T.; Sadahiro, S.; Hirai, H.; Yamada, !1K.; Matsuda, T.; Imai, E.; Tanaka, T. !$#journal Eur. J. Biochem. (1991) 198:101-106 !$#title Isolation and characterization of the human pyruvate kinase !1M gene. !$#cross-references MUID:91249787; PMID:2040271 !$#accession S16071 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 381-435 ##label TIM !'##cross-references EMBL:X56494; NID:g35504 !'##note this splice form is not annotated in GenBank entry HSPKM12, !1release 103.0 COMMENT Splice form M1 is the major form in adult skeletal muscle, !1heart and brain tissue. GENETICS !$#gene GDB:PKM2 !'##cross-references GDB:120295; OMIM:179050 !$#map_position 15q22.2-q22.3 !$#introns 52/1; 82/3; 126/3; 189/1; 279/2; 329/3; 380/3; 436/2; 497/1 COMPLEX homotetramer FUNCTION !$#description catalyzes the transphosphorylation of phosphoenolpyruvate !1and ADP to pyruvic acid and ATP !$#pathway glycolysis CLASSIFICATION #superfamily pyruvate kinase KEYWORDS acetylated amino end; alternative splicing; ATP !1biosynthesis; glycolysis; homotetramer; magnesium; !1metalloprotein; muscle; phosphotransferase; potassium FEATURE !$2-531 #product pyruvate kinase muscle splice form M1 !8#status predicted #label MAT\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status predicted\ !$73,243,294 #binding_site substrate phosphate (Arg, Ser, Arg) !8#status predicted\ !$270 #active_site Lys #status predicted\ !$272,293,294 #binding_site magnesium (Glu, Ala, Arg) #status !8predicted\ !$329,364 #binding_site potassium (Gln, Glu) #status predicted SUMMARY #length 531 #molecular-weight 58003 #checksum 7310 SEQUENCE /// ENTRY A25091 #type complete TITLE pyruvate kinase (EC 2.7.1.40), muscle splice form M1 [validated] - cat ORGANISM #formal_name Felis silvestris catus #common_name domestic cat DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 15-Sep-2000 ACCESSIONS A25091; A20242; A18793 REFERENCE A25091 !$#authors Muirhead, H.; Clayden, D.A.; Barford, D.; Lorimer, C.G.; !1Fothergill-Gilmore, L.A.; Schiltz, E.; Schmitt, W. !$#journal EMBO J. (1986) 5:475-481 !$#title The structure of cat muscle pyruvate kinase. !$#cross-references MUID:86220125; PMID:3519210 !$#contents sequence; X-ray crystallography, 2.6 angstroms !$#accession A25091 !'##molecule_type protein !'##residues 1-530 ##label MUI REFERENCE A94659 !$#authors Harkins, R.N.; Nocton, J.C.; Russell, M.P.; Fothergill, !1L.A.; Muirhead, H. !$#journal Eur. J. Biochem. (1983) 136:341-346 !$#title A comparison of the structure and activity of cat and trout !1muscle pyruvate kinases. !$#cross-references MUID:84028655; PMID:6628384 !$#accession A20242 !'##molecule_type protein !'##residues 313-329 ##label HAR REFERENCE A18793 !$#authors McAleese, S.M.; Hoar, C.G.; Dunbar, B.; Fothergill, L.A. !$#journal Biochem. Soc. Trans. (1982) 10:444-445 !$#title Hydroxylamine cleavage of cat skeletal-muscle pyruvate !1kinase: separation of the fragments and N-terminal sequence !1analysis. !$#accession A18793 !'##molecule_type protein !'##residues 199-207,'A',209-224,'FE',227-230,'Q',232-233,'R',235 !1##label MCA REFERENCE A66379 !$#authors Allen, S.C.; Muirhead, H. !$#submission submitted to the Brookhaven Protein Data Bank, July 1995 !$#cross-references PDB:1PKM !$#contents annotation; X-ray crystallography, 2.6 angstroms, residues !112-530 COMMENT Splice form M1 is the major form in adult skeletal muscle, !1heart and brain tissue. COMPLEX homotetramer FUNCTION !$#description catalyzes the transphosphorylation of phosphoenolpyruvate !1and ADP to pyruvic acid and ATP !$#pathway glycolysis CLASSIFICATION #superfamily pyruvate kinase KEYWORDS acetylated amino end; alternative splicing; ATP !1biosynthesis; glycolysis; homotetramer; magnesium; !1metalloprotein; muscle; phosphotransferase; potassium FEATURE !$1-530 #product pyruvate kinase muscle splice form M1 !8#status experimental #label MAT\ !$1 #modified_site blocked amino end (Ser) (probably !8acetylated) #status experimental\ !$72,242,293 #binding_site substrate phosphate (Arg, Ser, Arg) !8#status experimental\ !$269 #active_site Lys #status predicted\ !$271,292,293 #binding_site magnesium (Glu, Ala, Arg) #status !8experimental\ !$328,363 #binding_site potassium (Gln, Glu) #status !8experimental SUMMARY #length 530 #molecular-weight 57914 #checksum 6077 SEQUENCE /// ENTRY KICHPM #type complete TITLE pyruvate kinase (EC 2.7.1.40), muscle - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 11-Jun-1999 ACCESSIONS I50408; A00659 REFERENCE I50408 !$#authors Lonberg, N.; Gilbert, W. !$#journal Cell (1985) 40:81-90 !$#title Intron/exon structure of the chicken pyruvate kinase gene. !$#cross-references MUID:85099332; PMID:2981634 !$#accession I50408 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-530 ##label LO2 !'##cross-references GB:M18793; NID:g212569; PIDN:AAA49020.1; !1PID:g212571 REFERENCE A00659 !$#authors Lonberg, N.; Gilbert, W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:3661-3665 !$#title Primary structure of chicken muscle pyruvate kinase mRNA. !$#cross-references MUID:83221656; PMID:6574503 !$#accession A00659 !'##molecule_type mRNA !'##residues 1-530 ##label LON !'##cross-references GB:J00903; NID:g212572; PIDN:AAA49021.1; !1PID:g212573 GENETICS !$#introns 51/1; 81/3; 125/3; 188/1; 278/2; 328/3; 379/3; 435/2; 496/1 CLASSIFICATION #superfamily pyruvate kinase KEYWORDS acetylated amino end; ATP biosynthesis; glycolysis; !1homotetramer; magnesium; metalloprotein; muscle; !1phosphotransferase; potassium FEATURE !$2-530 #product pyruvate kinase, muscle #status predicted !8#label MAT\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status predicted\ !$72,242,293 #binding_site substrate phosphate (Arg, Ser, Arg) !8#status predicted\ !$269 #active_site Lys #status predicted\ !$271,292,293 #binding_site magnesium (Glu, Ala, Arg) #status !8predicted\ !$328,363 #binding_site potassium (Gln, Glu) #status predicted SUMMARY #length 530 #molecular-weight 58014 #checksum 2433 SEQUENCE /// ENTRY KIBYP #type complete TITLE pyruvate kinase (EC 2.7.1.40) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YAL038w ORGANISM #formal_name Saccharomyces cerevisiae DATE 17-May-1985 #sequence_revision 31-Mar-1991 #text_change 21-Jul-2000 ACCESSIONS S05764; A00660; S51981 REFERENCE S05764 !$#authors McNally, T.; Purvis, I.J.; Fothergill-Gilmore, L.A.; Brown, !1A.J.P. !$#journal FEBS Lett. (1989) 247:312-316 !$#title The yeast pyruvate kinase gene does not contain a string of !1non-preferred codons: revised nucleotide sequence. !$#cross-references MUID:89232143; PMID:2653861 !$#accession S05764 !'##molecule_type DNA !'##residues 1-500 ##label MCN !'##cross-references EMBL:X14400; NID:g5264; PIDN:CAA32573.1; PID:g5265 REFERENCE A00660 !$#authors Burke, R.L.; Tekamp-Olson, P.; Najarian, R. !$#journal J. Biol. Chem. (1983) 258:2193-2201 !$#title The isolation, characterization, and sequence of the !1pyruvate kinase gene of Saccharomyces cerevisiae. !$#cross-references MUID:83109047; PMID:6185493 !$#accession A00660 !'##molecule_type DNA !'##residues 1-381,'SLPR',387-500 ##label BUR !'##cross-references EMBL:V01321; NID:g4179; PIDN:CAA24631.1; PID:g4180 REFERENCE S51956 !$#authors Bussey, H.; Kaback, D.B.; Zhong, W.; Vo, D.T.; Clark, M.W.; !1Fortin, N.; Hall, J.; Ouellette, B.F.F.; Keng, T.; Barton, !1A.B.; Su, Y.; Davies, C.K.; Storms, R.K. !$#submission submitted to the EMBL Data Library, August 1994 !$#description The sequence of chromosome 1 of Saccharomyces cerevisiae. !$#accession S51981 !'##molecule_type DNA !'##residues 1-500 ##label BUS !'##cross-references EMBL:U12980; NID:g1326053; PIDN:AAC04993.1; !1PID:g595546; GSPDB:GN00001; MIPS:YAL038w GENETICS !$#gene SGD:CDC19; PYK1; MIPS:YAL038w !'##cross-references SGD:S0000036; MIPS:YAL038w !$#map_position 1L CLASSIFICATION #superfamily pyruvate kinase KEYWORDS ATP biosynthesis; glycolysis; magnesium; metalloprotein; !1phosphoprotein; phosphotransferase; potassium FEATURE !$22 #binding_site phosphate (Ser) (covalent) (by !8cAMP-dependent kinase) #status predicted\ !$49,213,264 #binding_site substrate phosphate (Arg, Ser, Arg) !8#status predicted\ !$240 #active_site Lys #status predicted\ !$242,263,264 #binding_site magnesium (Glu, Ala, Arg) #status !8predicted\ !$299,334 #binding_site potassium (Gln, Glu) #status predicted SUMMARY #length 500 #molecular-weight 54544 #checksum 3181 SEQUENCE /// ENTRY S17648 #type complete TITLE pyruvate kinase (EC 2.7.1.40) isoform 1 - Trypanosoma brucei ORGANISM #formal_name Trypanosoma brucei DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S17648 REFERENCE S17648 !$#authors Allert, S.; Ernest, I.; Poliszczak, A.; Opperdoes, F.R.; !1Michels, P.A.M. !$#journal Eur. J. Biochem. (1991) 200:19-27 !$#title Molecular cloning and analysis of two tandemly linked genes !1for pyruvate kinase of Trypanosoma brucei. !$#cross-references MUID:91348039; PMID:1879424 !$#accession S17648 !'##molecule_type DNA !'##residues 1-499 ##label ALL !'##cross-references EMBL:X57950; NID:g10947; PIDN:CAA41018.1; !1PID:g10948 !'##experimental_source strain 427 FUNCTION !$#description catalyzes the transphosphorylation of phosphoenolpyruvate !1and ADP to pyruvic acid and ATP !$#pathway glycolysis CLASSIFICATION #superfamily pyruvate kinase KEYWORDS ATP biosynthesis; glycolysis; magnesium; metalloprotein; !1phosphotransferase; potassium FEATURE !$50,212,263 #binding_site substrate phosphate (Arg, Ser, Arg) !8#status predicted\ !$239 #active_site Lys #status predicted\ !$298,333 #binding_site potassium (Gln, Glu) #status predicted SUMMARY #length 499 #molecular-weight 54466 #checksum 6773 SEQUENCE /// ENTRY D64925 #type complete TITLE pyruvate kinase (EC 2.7.1.40) [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES fructose-1,6-bisphosphate dependent pyruvate kinase ORGANISM #formal_name Escherichia coli DATE 12-Sep-1997 #sequence_revision 17-Sep-1997 #text_change 01-Mar-2002 ACCESSIONS D64925; S29004; S13434; S03397 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64925 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-470 ##label BLAT !'##cross-references GB:AE000262; GB:U00096; NID:g1787955; !1PIDN:AAC74746.1; PID:g1787965; UWGP:b1676 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S29004 !$#authors Ohara, O.; Dorit, R.L.; Gilbert, W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:6883-6887 !$#title Direct genomic sequencing of bacterial DNA: The pyruvate !1kinase I gene of Escherichia coli. !$#cross-references MUID:89386643; PMID:2674937 !$#accession S29004 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-450,'YGFWCTGTERHY' ##label OHA !'##cross-references EMBL:M24636; NID:g147275; PIDN:AAA24392.1; !1PID:g147276 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1May 1989 REFERENCE S13434 !$#authors Valentini, G.; Stoppini, M.; Speranza, M.L.; Malcovati, M.; !1Ferri, G. !$#journal Biol. Chem. Hoppe-Seyler (1991) 372:91-93 !$#title Bacterial pyruvate kinases have a shorter N-terminal domain. !$#cross-references MUID:91315755; PMID:1859631 !$#accession S13434 !'##molecule_type protein !'##residues 1-43,'S',45-48 ##label VAL REFERENCE S03397 !$#authors Speranza, M.L.; Valentini, G.; Iadarola, P.; Stoppini, M.; !1Malcovati, M.; Ferri, G. !$#journal Biol. Chem. Hoppe-Seyler (1989) 370:211-216 !$#title Primary structure of three peptides at the catalytic and !1allosteric sites of the fructose-1,6-bisphosphate-activated !1pyruvate kinase from Escherichia coli. !$#cross-references MUID:89228557; PMID:2653362 !$#accession S03397 !'##status preliminary !'##molecule_type protein !'##residues 293-319;369-378,'N',380-385;389-400,'D',402-404 ##label SPE !'##experimental_source strain J53/R387 REFERENCE A66380 !$#authors Mattevi, A. !$#submission submitted to the Brookhaven Protein Data Bank, April 1995 !$#cross-references PDB:1PKY !$#contents annotation; X-ray crystallography, 2.5 angstroms, residues !11-278,'M',280-344;351-470 GENETICS !$#gene pykF FUNCTION !$#description catalyzes the transphosphorylation of phosphoenolpyruvate !1and ADP to pyruvic acid and ATP !$#pathway glycolysis CLASSIFICATION #superfamily pyruvate kinase KEYWORDS ATP biosynthesis; glycolysis; magnesium; metalloprotein; !1phosphotransferase; potassium FEATURE !$32,192,244 #binding_site substrate phosphate (Arg, Ser, Arg) !8#status experimental\ !$220 #active_site Lys #status predicted\ !$222,243,244 #binding_site magnesium (Glu, Ala, Arg) #status !8experimental\ !$279,314 #binding_site potassium (Gln, Glu) #status !8experimental SUMMARY #length 470 #molecular-weight 50729 #checksum 430 SEQUENCE /// ENTRY B40620 #type complete TITLE pyruvate kinase (EC 2.7.1.40) - Lactococcus lactis subsp. lactis (strain LM0230) ORGANISM #formal_name Lactococcus lactis subsp. lactis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 02-Jun-2000 ACCESSIONS B40620 REFERENCE A40620 !$#authors Llanos, R.M.; Harris, C.J.; Hillier, A.J.; Davidson, B.E. !$#journal J. Bacteriol. (1993) 175:2541-2551 !$#title Identification of a novel operon in Lactococcus lactis !1encoding three enzymes for lactic acid synthesis: !1phosphofructokinase, pyruvate kinase, and lactate !1dehydrogenase. !$#cross-references MUID:93239679; PMID:8478320 !$#accession B40620 !'##status preliminary !'##molecule_type DNA !'##residues 1-502 ##label LLA !'##cross-references GB:L07920; NID:g308856; PIDN:AAA99895.1; !1PID:g308858 !'##experimental_source subsp. lactis LM0230 !'##note sequence extracted from NCBI backbone (NCBIN:130458, !1NCBIP:130460) CLASSIFICATION #superfamily pyruvate kinase KEYWORDS phosphotransferase SUMMARY #length 502 #molecular-weight 54285 #checksum 5647 SEQUENCE /// ENTRY C64130 #type complete TITLE pyruvate kinase (EC 2.7.1.40) - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C64130 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession C64130 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-478 ##label TIGR !'##cross-references GB:U32831; GB:L42023; NID:g1574407; !1PIDN:AAC23216.1; PID:g1574410; TIGR:HI1573 GENETICS !$#gene pykA FUNCTION !$#description catalyzes the conversion of phosphoenolpyruvate to pyruvate !1with the concomitant phosphorylation of ADP to ATP !$#pathway glycolysis !$#note requires magnesium and potassium CLASSIFICATION #superfamily pyruvate kinase KEYWORDS glycolysis; magnesium; phosphotransferase; potassium FEATURE !$223 #active_site Lys #status predicted\ !$225,249,250 #binding_site magnesium (Glu, Ala, Arg) #status !8predicted SUMMARY #length 478 #molecular-weight 51054 #checksum 1171 SEQUENCE /// ENTRY S27330 #type complete TITLE pyruvate kinase (EC 2.7.1.40) isoform 1 - Bacillus stearothermophilus ORGANISM #formal_name Bacillus stearothermophilus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S27330 REFERENCE S27330 !$#authors Walker, D.; Chia, W.N.; Muirhead, H. !$#journal J. Mol. Biol. (1992) 228:265-276 !$#title Key residues in the allosteric transition of Bacillus !1stearothermophilus pyruvate kinase identified by !1site-directed mutagenesis. !$#cross-references MUID:93078262; PMID:1447787 !$#accession S27330 !'##molecule_type DNA !'##residues 1-494 ##label WAL !'##cross-references EMBL:X57859; NID:g47827; PIDN:CAA40994.1; !1PID:g47828 !'##experimental_source strain NCA1503 !'##note the authors translated the codon CAA for residue 217 as Lys, !1CTC for residue 370 as Ser, and AAG for residue 447 as Glu GENETICS !$#gene pk FUNCTION !$#description catalyzes the transphosphorylation of phosphoenolpyruvate !1and ADP to pyruvic acid and ATP !$#pathway glycolysis CLASSIFICATION #superfamily pyruvate kinase KEYWORDS ATP biosynthesis; glycolysis; magnesium; metalloprotein; !1phosphotransferase; potassium FEATURE !$33,193,245 #binding_site substrate phosphate (Arg, Ser, Arg) !8#status predicted\ !$221 #active_site Lys #status predicted\ !$280,315 #binding_site potassium (Gln, Glu) #status predicted SUMMARY #length 494 #molecular-weight 52947 #checksum 8838 SEQUENCE /// ENTRY JC4219 #type complete TITLE pyruvate kinase (EC 2.7.1.40) - Bacillus psychrophilus ALTERNATE_NAMES ATP:pyruvate 2-O-phosphotransferase ORGANISM #formal_name Bacillus psychrophilus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS JC4219 REFERENCE JC4218 !$#authors Tanaka, K.; Sakai, H.; Ohta, T.; Matsuzawa, H. !$#journal Biosci. Biotechnol. Biochem. (1995) 59:1536-1542 !$#title Molecular cloning of the genes for pyruvate kinase of two !1Bacilli, Bacillus psychrophilus and Bacillus licheniformis, !1and comparison of the properties of the enzymes produced in !1Escherichia coli. !$#cross-references MUID:96032212; PMID:7549104 !$#accession JC4219 !'##molecule_type DNA !'##residues 1-586 ##label TAN !'##cross-references DDBJ:D31954; NID:g1041096; PIDN:BAA06725.1; !1PID:g1041097 COMMENT This allosteric enzyme is activated by AMP or ribose !15-phosphate, and inhibited by ATP or fructose 1, !16-bisphosphate. It has a characteristic carboxyl-terminal !1extension sequence of about 110 amino acid residues. FUNCTION !$#description catalyzes the transphosphorylation of phosphoenolpyruvate !1and ADP to pyruvic acid and ATP !$#pathway glycolysis CLASSIFICATION #superfamily pyruvate kinase KEYWORDS ATP biosynthesis; glycolysis; magnesium; metalloprotein; !1phosphotransferase; potassium FEATURE !$32,192,244 #binding_site substrate phosphate (Arg, Ser, Arg) !8#status predicted\ !$220 #active_site Lys #status predicted\ !$279,314 #binding_site potassium (Gln, Glu) #status predicted SUMMARY #length 586 #molecular-weight 62570 #checksum 3204 SEQUENCE /// ENTRY S61571 #type complete TITLE suppressor protein MSS4 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YD8142A.05; protein YDR208w CONTAINS probable protein kinase (EC 2.7.1.-) ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S61571; S43271 REFERENCE S61117 !$#authors Murphy, L.; Harris, D. !$#submission submitted to the EMBL Data Library, December 1995 !$#accession S61571 !'##molecule_type DNA !'##residues 1-779 ##label MUR !'##cross-references EMBL:Z68194; NID:g1204148; PIDN:CAA92347.1; !1PID:g1122336; GSPDB:GN00004; MIPS:YDR208w !'##experimental_source strain AB972 REFERENCE S43271 !$#authors Yoshida, S.; Ohya, Y.; Nakano, A.; Anraku, Y. !$#journal Mol. Gen. Genet. (1994) 242:631-640 !$#title Genetic interactions among genes involved in the STT4-PKC1 !1pathway of Saccharomyces cerevisiae. !$#cross-references MUID:94203175; PMID:8152413 !$#accession S43271 !'##molecule_type DNA !'##residues 1-609,'L',611-779 ##label YOS !'##cross-references EMBL:D13716; NID:g493718; PIDN:BAA02869.1; !1PID:g493719 GENETICS !$#gene SGD:MSS4; MIPS:YDR208w !'##cross-references SGD:S0002616; MIPS:YDR208w !$#map_position 4R CLASSIFICATION #superfamily suppressor protein MSS4; !11-phosphatidylinositol-4-phosphate 5-kinase homology KEYWORDS phosphotransferase FEATURE !$334-756 #domain 1-phosphatidylinositol-4-phosphate 5-kinase !8homology #label PIK SUMMARY #length 779 #molecular-weight 89320 #checksum 4225 SEQUENCE /// ENTRY S56274 #type complete TITLE FAB1 protein - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YFR019w ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S56274; A55997 REFERENCE S56186 !$#authors Murakami, Y.; Naitou, M.; Hagiwara, H.; Shibata, T.; Ozawa, !1M.; Sasanuma, S.I.; Sasanuma, M.; Tsuchiya, Y.; Soeda, E.; !1Yokoyama, K.; Yamazaki, M.; Tashiro, H.; Eki, T. !$#submission submitted to the EMBL Data Library, May 1995 !$#description Analysis of the nucleotide sequence of chromosome VI from !1Saccaromyces cerevisiae. !$#accession S56274 !'##molecule_type DNA !'##residues 1-2278 ##label MUR !'##cross-references EMBL:D50617; NID:g836685; PIDN:BAA09258.1; !1PID:g836774; GSPDB:GN00006; MIPS:YFR019w REFERENCE A55997 !$#authors Yamamoto, A.; Koshland, D. !$#submission submitted to GenBank, August 1993 !$#description FAB1: a novel gene required for endocytic-vacuolar pathway !1and nuclear migration. !$#accession A55997 !'##molecule_type DNA !'##residues 1-2274,'R',2276-2278 ##label YAM !'##cross-references GB:U01017; NID:g392993; PIDN:AAA81360.1; !1PID:g398498 GENETICS !$#gene SGD:FAB1; MIPS:YFR019w !'##cross-references SGD:S0001915; MIPS:YFR019w !$#map_position 6R CLASSIFICATION #superfamily FAB1 protein; !11-phosphatidylinositol-4-phosphate 5-kinase homology FEATURE !$1911-2266 #domain 1-phosphatidylinositol-4-phosphate 5-kinase !8homology #label PIK SUMMARY #length 2278 #molecular-weight 257447 #checksum 9841 SEQUENCE /// ENTRY WQECMM #type complete TITLE phosphotransferase system enzyme II (EC 2.7.1.69), mannose-specific, factor IID - Escherichia coli (strain K-12) ALTERNATE_NAMES mannose permease, factor II-M; protein-Npi-phosphohistidine-mannose phosphotransferase, factor II-M; protein-Npi-phosphohistidine-sugar phosphotransferase, mannose-specific enzyme II-M ORGANISM #formal_name Escherichia coli DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 01-Mar-2002 ACCESSIONS A30288; C64943 REFERENCE A92634 !$#authors Erni, B.; Zanolari, B.; Kocher, H.P. !$#journal J. Biol. Chem. (1987) 262:5238-5247 !$#title The mannose permease of Escherichia coli consists of three !1different proteins. Amino acid sequence and function in !1sugar transport, sugar phosphorylation, and penetration of !1phage lambda DNA. !$#cross-references MUID:87165962; PMID:2951378 !$#accession A30288 !'##molecule_type DNA !'##residues 1-286 ##label ERN !'##cross-references GB:J02699; NID:g147401; PIDN:AAA24445.1; !1PID:g147404 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64943 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-286 ##label BLAT !'##cross-references GB:AE000276; GB:U00096; NID:g1788117; !1PIDN:AAC74889.1; PID:g1788122; UWGP:b1819 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene manZ; ptsM !$#map_position 40 min !$#start_codon GTG FUNCTION !$#description mannose transporter of bacterial phosphotransferase system !1mediates uptake of mannose, glucose and related hexoses by a !1mechanism that couples translocation with phosphorylation of !1the substrate !$#note is a component of phosphoenolpyruvate-glycose !1phosphotransferase system (PTS); PTS comprises two general !1proteins (HPr and enzyme I) and a sugar-specific complex !1(enzyme II); the phosphoryl group is transferred from !1phosphoenolpyruvate to enzyme I, to HPr, to the enzyme II !1complex, and finally to the sugar substrate as it crosses !1the membrane CLASSIFICATION #superfamily phosphotransferase system mannose-specific !1enzyme II, factor II-M KEYWORDS phosphotransferase; sugar transport system; transmembrane !1protein FEATURE !$141-157 #domain transmembrane #status predicted #label TM1\ !$191-207 #domain transmembrane #status predicted #label TM2\ !$241-257 #domain transmembrane #status predicted #label TM3\ !$267-283 #domain transmembrane #status predicted #label TM4 SUMMARY #length 286 #molecular-weight 31303 #checksum 8541 SEQUENCE /// ENTRY WQECMP #type complete TITLE phosphotransferase system enzyme II (EC 2.7.1.69), mannose-specific, factor IIC - Escherichia coli (strain K-12) ALTERNATE_NAMES mannose permease, factor II-P; phosphotransferase system enzyme II-B, mannose-specific; phosphotransferase system enzyme II-P, mannose-specific; protein-Npi-phosphohistidine-mannose phosphotransferase, factor II-P; protein-Npi-phosphohistidine-sugar phosphotransferase, mannose-specific enzyme II-P ORGANISM #formal_name Escherichia coli DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 01-Mar-2002 ACCESSIONS A30285; S07697; B64943 REFERENCE A92634 !$#authors Erni, B.; Zanolari, B.; Kocher, H.P. !$#journal J. Biol. Chem. (1987) 262:5238-5247 !$#title The mannose permease of Escherichia coli consists of three !1different proteins. Amino acid sequence and function in !1sugar transport, sugar phosphorylation, and penetration of !1phage lambda DNA. !$#cross-references MUID:87165962; PMID:2951378 !$#accession A30285 !'##molecule_type DNA !'##residues 1-266 ##label ERN !'##cross-references GB:J02699; NID:g147401; PIDN:AAA24444.1; !1PID:g147403 REFERENCE S06431 !$#authors Saris, P.E.J.; Liljestroem, P.; Palva, E.T. !$#journal FEMS Microbiol. Lett. (1988) 49:69-73 !$#title Nucleotide sequence of manX(ptsL) encoding the enzyme III !1(Man) (II-A(Man)) function in the phosphotransferase system !1of Escherichia coli K-12. !$#accession S07697 !'##molecule_type DNA !'##residues 1-40,'YRSWGYENRYYYRWYAGNDRAGLDEHRCC' ##label SAR !'##cross-references EMBL:X17443; NID:g41975; PIDN:CAA35498.1; !1PID:g41977 !'##note the nucleotide sequences in references S06431 and A30285 differ !1by a frameshift in codon 41 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64943 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-266 ##label BLAT !'##cross-references GB:AE000276; GB:U00096; NID:g1788117; !1PIDN:AAC74888.1; PID:g1788121; UWGP:b1818 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene manY; ptsP; pel !$#map_position 40 min FUNCTION !$#description mannose transporter of bacterial phosphotransferase system !1mediates uptake of mannose, glucose and related hexoses by a !1mechanism that couples translocation with phosphorylation of !1the substrate !$#note component of phosphoenolpyruvate-sugar phosphotransferase !1system (PTS); PTS comprises two general proteins (HPr and !1enzyme I) and a sugar-specific complex (enzyme II); the !1phosphoryl group is transferred from phosphoenolpyruvate to !1enzyme I, to HPr, to the enzyme II complex, and finally to !1the sugar substrate as it crosses the membrane CLASSIFICATION #superfamily phosphotransferase system mannose-specific !1enzyme II, factor II-P KEYWORDS phosphotransferase; sugar transport system; transmembrane !1protein FEATURE !$8-24 #domain transmembrane #status predicted #label TM1\ !$36-52 #domain transmembrane #status predicted #label TM2\ !$70-86 #domain transmembrane #status predicted #label TM3\ !$96-112 #domain transmembrane #status predicted #label TM4\ !$144-160 #domain transmembrane #status predicted #label TM5\ !$182-198 #domain transmembrane #status predicted #label TM6\ !$223-239 #domain transmembrane #status predicted #label TM7 SUMMARY #length 266 #molecular-weight 27636 #checksum 4199 SEQUENCE /// ENTRY WQECM3 #type complete TITLE phosphotransferase system enzyme II (EC 2.7.1.69), mannose-specific, factor IIAB - Escherichia coli (strain K-12) ALTERNATE_NAMES mannose permease, factor III; phosphotransferase system enzyme II-A, mannose-specific; phosphotransferase system enzyme III, mannose-specific; protein-Npi-phosphohistidine-mannose phosphotransferase, factor III; protein-Npi-phosphohistidine-sugar phosphotransferase, mannose-specific enzyme III ORGANISM #formal_name Escherichia coli DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 01-Mar-2002 ACCESSIONS A30286; S06431; A64943 REFERENCE A92634 !$#authors Erni, B.; Zanolari, B.; Kocher, H.P. !$#journal J. Biol. Chem. (1987) 262:5238-5247 !$#title The mannose permease of Escherichia coli consists of three !1different proteins. Amino acid sequence and function in !1sugar transport, sugar phosphorylation, and penetration of !1phage lambda DNA. !$#cross-references MUID:87165962; PMID:2951378 !$#accession A30286 !'##molecule_type DNA !'##residues 1-323 ##label ERN !'##cross-references GB:J02699; NID:g147401; PIDN:AAA24443.1; !1PID:g147402 REFERENCE S06431 !$#authors Saris, P.E.J.; Liljestroem, P.; Palva, E.T. !$#journal FEMS Microbiol. Lett. (1988) 49:69-73 !$#title Nucleotide sequence of manX(ptsL) encoding the enzyme III !1(Man) (II-A(Man)) function in the phosphotransferase system !1of Escherichia coli K-12. !$#accession S06431 !'##molecule_type DNA !'##residues 'MGWGCRAGCLKRQKV',24-34,'N',36-100,'R',102-141,'G',143-323 !1##label SAR !'##cross-references EMBL:X17443; NID:g41975; PIDN:CAA35497.1; !1PID:g41976 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64943 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-323 ##label BLAT !'##cross-references GB:AE000276; GB:U00096; NID:g1788117; !1PIDN:AAC74887.1; PID:g1788120; UWGP:b1817 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene manX; ptsL; gptB !$#map_position 40 min !$#start_codon GTG COMPLEX homodimer FUNCTION !$#description mannose transporter of bacterial phosphotransferase system !1mediates uptake of mannose, glucose and related hexoses by a !1mechanism that couples translocation with phosphorylation of !1the substrate !$#note is a component of phosphoenolpyruvate-glycose !1phosphotransferase system (PTS); PTS comprises two general !1proteins (HPr and enzyme I) and a sugar-specific complex !1(enzyme II); the phosphoryl group is transferred from !1phosphoenolpyruvate to enzyme I, to HPr, to the enzyme II !1complex, and finally to the sugar substrate as it crosses !1the membrane CLASSIFICATION #superfamily phosphotransferase system mannose-specific !1enzyme II, factor III KEYWORDS homodimer; membrane-associated protein; phosphohistidine; !1phosphoprotein; phosphotransferase; sugar transport system FEATURE !$175 #active_site His (phosphohistidine intermediate) !8#status predicted SUMMARY #length 323 #molecular-weight 35047 #checksum 2060 SEQUENCE /// ENTRY WQEC2M #type complete TITLE phosphotransferase system enzyme II (EC 2.7.1.69), mannitol-specific - Escherichia coli (strain K-12) ALTERNATE_NAMES mannitol permease; protein-N(pi)-phosphohistidine-mannitol phosphotransferase ORGANISM #formal_name Escherichia coli DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 01-Mar-2002 ACCESSIONS A00661; S47820; A65160 REFERENCE A00661 !$#authors Lee, C.A.; Saier Jr., M.H. !$#journal J. Biol. Chem. (1983) 258:10761-10767 !$#title Mannitol-specific enzyme II of the bacterial !1phosphotransferse system. III. The nucleotide sequence of !1the permease gne. !$#cross-references MUID:83291014; PMID:6309813 !$#accession A00661 !'##molecule_type DNA !'##residues 1-637 ##label LEE !'##cross-references EMBL:V01503; GB:K00051; NID:g42033; !1PIDN:CAA24748.1; PID:g42034 REFERENCE A44533 !$#authors Pas, H.H.; Robillard, G.T. !$#journal Biochemistry (1988) 27:5835-5839 !$#title S-Phosphocysteine and phosphohistidine are intermediates in !1the phosphoenolpyruvate-dependent mannitol transport !1catalyzed by Escherichia coli EII(Mtl). !$#cross-references MUID:89050920; PMID:3142516 !$#contents annotation; active sites REFERENCE A44534 !$#authors Sugiyama, J.E.; Mahmoodian, S.; Jacobson, G.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:9603-9607 !$#title Membrane topology analysis of Escherichia coli mannitol !1permease by using a nested-deletion method to create !1mtlA-phoA fusions. !$#cross-references MUID:92052139; PMID:1946374 !$#contents annotation; membrane topology REFERENCE S47666 !$#authors Plunkett, G. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S47820 !'##molecule_type DNA !'##residues 1-637 ##label PLU !'##cross-references EMBL:U00039; NID:g466582; PIDN:AAB18576.1; !1PID:g466737 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65160 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-637 ##label BLAT !'##cross-references GB:AE000438; GB:U00096; NID:g2367251; !1PIDN:AAC76623.1; PID:g1790027; UWGP:b3599 !'##experimental_source strain K-12, substrain MG1655 COMMENT This protein is phosphorylated first at the histidine active !1site, from which the phosphoryl group is transferred to the !1cysteine active site. GENETICS !$#gene mtlA !$#map_position 81 min FUNCTION !$#description this enzyme, a transmembrane component of the !1phosphoenolpyruvate-dependent sugar phosphotransferase !1system, catalyzes the concomitant transport and !1phosphorylation of mannitol; the phosphoryl group from !1phosphoenolpyruvate is transferred to phosphoryl carrier !1protein HPr by enzyme I and then from phospho-HPr to !1mannitol by enzyme II CLASSIFICATION #superfamily phosphotransferase system mannitol-specific !1enzyme II; phosphotransferase system mannitol-specific !1enzyme II factor II homology; phosphotransferase system !1mannitol-specific enzyme II factor III homology KEYWORDS phosphohistidine; phosphoprotein; phosphotransferase; sugar !1transport system; transmembrane protein FEATURE !$1-24 #domain intracellular #status predicted #label INT1\ !$8-453 #domain phosphotransferase system mannitol-specific !8enzyme II factor II homology #label PT2M\ !$25-44 #domain transmembrane #status predicted #label TM1\ !$51-69 #domain transmembrane #status predicted #label TM2\ !$70-134 #domain intracellular #status predicted #label INT2\ !$135-154 #domain transmembrane #status predicted #label TM3\ !$166-184 #domain transmembrane #status predicted #label TM4\ !$185-271 #domain intracellular #status predicted #label INT3\ !$272-291 #domain transmembrane #status predicted #label TM5\ !$313-333 #domain transmembrane #status predicted #label TM6\ !$334-637 #domain intracellular #status predicted #label INT4\ !$509-634 #domain phosphotransferase system mannitol-specific !8enzyme II factor III homology #label PT3M\ !$384 #active_site Cys (phosphocysteine intermediate) !8#status experimental\ !$554 #active_site His (phosphohistidine intermediate) !8#status experimental SUMMARY #length 637 #molecular-weight 67972 #checksum 6478 SEQUENCE /// ENTRY S22385 #type complete TITLE phosphotransferase system enzyme II (EC 2.7.1.69), mannitol-specific, factor II - Staphylococcus carnosus ORGANISM #formal_name Staphylococcus carnosus DATE 22-Nov-1993 #sequence_revision 30-May-1997 #text_change 11-Jun-1999 ACCESSIONS S68193; S74271; S22385 REFERENCE S68193 !$#authors Pogge von Strandmann, R.; Weigt, C.; Fischer, R.; Meyer, !1H.E.; Kalbitzer, H.R.; Hengstenberg, W. !$#journal Eur. J. Biochem. (1995) 233:116-122 !$#title Expression, purification and characterization of the enzyme !1II mannitol-specific domain from Staphylococcus carnosus and !1determination of the active-site cysteine residue. !$#cross-references MUID:96061939; PMID:7588734 !$#accession S68193 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-518 ##label POG !'##cross-references EMBL:X56333; NID:g633649; PIDN:CAA39769.1; !1PID:g633650 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1990 !'##note this is a revision to the sequence from reference S22385 !$#accession S74271 !'##molecule_type protein !'##residues 348-357 ##label POE REFERENCE S22385 !$#authors Fischer, R.; Hengstenberg, W. !$#journal Eur. J. Biochem. (1992) 204:963-969 !$#title Mannitol-specific enzyme II of the !1phosphoenolpyruvate-dependent phosphotransferase system of !1Staphylococcus carnosus. Sequence and expression in !1Escherichia coli and structural comparison with the enzyme !1II(mannitol) of Escherichia coli. !$#cross-references MUID:92201209; PMID:1551396 !$#accession S22385 !'##molecule_type DNA !'##residues 4-454,'F',456-507,'D' ##label FIS !'##cross-references EMBL:X56333; GB:S88885; NID:g633649; !1PIDN:CAA39769.1; PID:g633650 !'##note this sequence has been revised in reference S68193 GENETICS !$#gene mtlA CLASSIFICATION #superfamily phosphotransferase system mannitol-specific !1enzyme II factor II; phosphotransferase system !1mannitol-specific enzyme II factor II homology KEYWORDS phosphoprotein; phosphotransferase; sugar transport system; !1transmembrane protein FEATURE !$16-501 #domain phosphotransferase system mannitol-specific !8enzyme II factor II homology #label PT2M\ !$432 #active_site Cys (phosphocysteine intermediate) !8#status experimental SUMMARY #length 518 #molecular-weight 55685 #checksum 9420 SEQUENCE /// ENTRY S36123 #type complete TITLE phosphotransferase system enzyme II (EC 2.7.1.69) factor II, mannitol-specific, cryptic - Escherichia coli (strain K-12) ALTERNATE_NAMES protein-Npi-phosphohistidine-sugar phosphotransferase ORGANISM #formal_name Escherichia coli DATE 20-Feb-1995 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS D65078; S36123; S34370 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65078 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-462 ##label BLAT !'##cross-references GB:AE000376; GB:U00096; NID:g2367176; !1PIDN:AAC75970.1; PID:g1789301; UWGP:b2933 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S36122 !$#authors Sprenger, G.A. !$#journal Biochim. Biophys. Acta (1993) 1158:103-106 !$#title Two open reading frames adjacent to the Escherichia coli !1K-12 transketolase (tkt) gene show high similarity to the !1mannitol phosphotransferase system enzymes from Escherichia !1coli and various Gram-positive bacteria. !$#cross-references MUID:93357262; PMID:8353127 !$#accession S36123 !'##status preliminary !'##molecule_type DNA !'##residues 1-273,'IEF',276-414,'GCR',418,'SGRLHPWPR',424,'WK',427,'A', !1429,'ETGVRN',436-446,'LRCGPVNSV' ##label SPR !'##cross-references EMBL:X72677; NID:g312761; PIDN:CAA51229.1; !1PID:g312763 GENETICS !$#gene cmtA CLASSIFICATION #superfamily phosphotransferase system mannitol-specific !1enzyme II factor II; phosphotransferase system !1mannitol-specific enzyme II factor II homology KEYWORDS phosphoprotein; phosphotransferase; sugar transport system; !1transmembrane protein FEATURE !$9-444 #domain phosphotransferase system mannitol-specific !8enzyme II factor II homology #label PT2M\ !$377 #active_site Cys (phosphocysteine intermediate) !8#status predicted SUMMARY #length 462 #molecular-weight 48971 #checksum 33 SEQUENCE /// ENTRY WQSO3M #type complete TITLE phosphotransferase system enzyme II (EC 2.7.1.69), mannitol-specific, factor III - Enterococcus faecalis ALTERNATE_NAMES phosphotransferase system mannitol-specific enzyme III ORGANISM #formal_name Enterococcus faecalis DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 11-Jun-1999 ACCESSIONS A39435 REFERENCE A39435 !$#authors Fischer, R.; von Strandmann, R.P.; Hengstenberg, W. !$#journal J. Bacteriol. (1991) 173:3709-3715 !$#title Mannitol-specific phosphoenolpyruvate-dependent !1phosphotransferase system of Enterococcus faecalis: !1molecular cloning and nucleotide sequences of the enzyme III !1(Mtl) gene and the mannitol-1-phosphate dehydrogenase gene, !1expression in Escherichia coli, and comparison of the gene !1products with similar enzymes. !$#cross-references MUID:91267934; PMID:1904856 !$#accession A39435 !'##molecule_type DNA !'##residues 1-145 ##label FIS !'##cross-references GB:M38386; NID:g148312; PIDN:AAA24779.1; !1PID:g148313 COMMENT This soluble component of the mannitol phosphotransferase !1system is phosphorylated in a reaction involving enzyme I !1and phosphoryl carrier protein HPr. The phosphoryl group is !1then transferred from enzyme III to enzyme II, which !1catalyzes the concomitant uptake and phosphorylation of !1mannitol. GENETICS !$#gene mtlF CLASSIFICATION #superfamily phosphotransferase system mannitol-specific !1enzyme II factor III; phosphotransferase system !1mannitol-specific enzyme II factor III homology KEYWORDS phosphohistidine; phosphoprotein; phosphotransferase; sugar !1transport system FEATURE !$17-143 #domain phosphotransferase system mannitol-specific !8enzyme II factor III homology #label PT3M\ !$62 #active_site His (phosphohistidine intermediate) !8#status predicted SUMMARY #length 145 #molecular-weight 15876 #checksum 3785 SEQUENCE /// ENTRY B44798 #type complete TITLE phosphotransferase system enzyme II (EC 2.7.1.69), mannitol-specific, factor III - Streptococcus mutans ORGANISM #formal_name Streptococcus mutans DATE 24-Mar-1993 #sequence_revision 31-Jan-1997 #text_change 11-Jun-1999 ACCESSIONS B44798 REFERENCE A44798 !$#authors Honeyman, A.L.; Curtiss III, R. !$#journal Infect. Immun. (1992) 60:3369-3375 !$#title Isolation, characterization, and nucleotide sequence of the !1Streptococcus mutans mannitol-phosphate dehydrogenase gene !1and the mannitol-specific factor III gene of the !1phosphoenolpyruvate phosphotransferase system. !$#cross-references MUID:92348013; PMID:1322373 !$#accession B44798 !'##status preliminary !'##molecule_type DNA !'##residues 1-145 ##label HON !'##cross-references GB:M94225; NID:g153743; PIDN:AAA26941.1; !1PID:g153745 !'##experimental_source strain UA130, serotype c !'##note sequence extracted from NCBI backbone (NCBIN:109750, !1NCBIP:109752) CLASSIFICATION #superfamily phosphotransferase system mannitol-specific !1enzyme II factor III; phosphotransferase system !1mannitol-specific enzyme II factor III homology KEYWORDS phosphohistidine; phosphoprotein; phosphotransferase FEATURE !$16-142 #domain phosphotransferase system mannitol-specific !8enzyme II factor III homology #label PT3M\ !$61 #active_site His (phosphohistidine intermediate) !8#status predicted SUMMARY #length 145 #molecular-weight 15878 #checksum 6529 SEQUENCE /// ENTRY JQ0088 #type complete TITLE phosphotransferase system enzyme II (EC 2.7.1.69), mannitol-specific, factor III - Staphylococcus carnosus ORGANISM #formal_name Staphylococcus carnosus DATE 07-Jun-1990 #sequence_revision 31-Jan-1997 #text_change 11-Jun-1999 ACCESSIONS JQ0088 REFERENCE JQ0088 !$#authors Fisher, R.; Eisermann, R.; Reiche, B.; Hengstenberg, W. !$#journal Gene (1989) 82:249-257 !$#title Cloning, sequencing and overexpression of the !1mannitol-specific enzyme-III-encoding gene of Staphylococcus !1carnosus. !$#cross-references MUID:90060814; PMID:2684783 !$#accession JQ0088 !'##molecule_type DNA !'##residues 1-144 ##label FIS !'##cross-references GB:M30781; NID:g153048; PIDN:AAA26656.1; !1PID:g153049 COMMENT This enzyme is a soluble enzyme of the !1phosphoenolpyruvate-dependent phosphotransferase system of !1S. carnosus. CLASSIFICATION #superfamily phosphotransferase system mannitol-specific !1enzyme II factor III; phosphotransferase system !1mannitol-specific enzyme II factor III homology KEYWORDS phosphohistidine; phosphoprotein; phosphotransferase FEATURE !$18-140 #domain phosphotransferase system mannitol-specific !8enzyme II factor III homology #label PT3M\ !$63 #active_site His (phosphohistidine intermediate) !8#status predicted SUMMARY #length 144 #molecular-weight 15566 #checksum 2212 SEQUENCE /// ENTRY JE0023 #type complete TITLE fructose phosphotransferase protein - Salmonella typhimurium ALTERNATE_NAMES FPr protein; phosphoenolpyruvate-fructose phosphotransferase system, 39K protein ORGANISM #formal_name Salmonella typhimurium DATE 31-Dec-1991 #sequence_revision 31-Jan-1997 #text_change 11-Jun-1999 ACCESSIONS JE0023 REFERENCE JE0023 !$#authors Geerse, R.H.; Izzo, F.; Postma, P.W. !$#journal Mol. Gen. Genet. (1989) 216:517-525 !$#title The PEP: fructose phosphotransferase system in Salmonella !1typhimurium: FPr combines Enzyme IIIFru and pseudo-HPr !1activities. !$#cross-references MUID:89313694; PMID:2546043 !$#accession JE0023 !'##molecule_type DNA !'##residues 1-376 ##label GEE !'##cross-references EMBL:X14243; NID:g47688; PIDN:CAA32459.1; !1PID:g47689 GENETICS !$#gene fruF CLASSIFICATION #superfamily fructose phosphotransferase protein; !1phosphotransferase system mannitol-specific enzyme II factor !1III homology; phosphotransferase system !1phosphohistidine-containing protein homology KEYWORDS phosphohistidine; phosphoprotein; phosphotransferase system; !1sugar transport system FEATURE !$17-140 #domain phosphotransferase system mannitol-specific !8enzyme II factor III homology #label PT3M\ !$292-371 #domain phosphotransferase system !8phosphohistidine-containing protein homology #label !8HPR\ !$299 #active_site His (phosphohistidine intermediate) !8#status predicted\ !$333 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 376 #molecular-weight 39593 #checksum 2861 SEQUENCE /// ENTRY S10639 #type complete TITLE fructose phosphotransferase multiphosphoryltransfer protein - Rhodobacter capsulatus ORGANISM #formal_name Rhodobacter capsulatus DATE 04-Feb-1994 #sequence_revision 31-Jan-1997 #text_change 11-Jun-1999 ACCESSIONS S10639 REFERENCE S10639 !$#authors Wu, L.F.; Tomich, J.M.; Saier Jr., M.H. !$#journal J. Mol. Biol. (1990) 213:687-703 !$#title Structure and evolution of a multidomain multiphosphoryl !1transfer protein. Nucleotide sequence of the fruB(HI) gene !1in Rhodobacter capsulatus and comparisons with homologous !1genes from other organisms. !$#cross-references MUID:90294288; PMID:2193161 !$#accession S10639 !'##status preliminary !'##molecule_type DNA !'##residues 1-827 ##label WUL !'##cross-references EMBL:X53150; NID:g46018; PIDN:CAA37301.1; !1PID:g581492 GENETICS !$#gene fruB !$#start_codon GTG CLASSIFICATION #superfamily fructose phosphotransferase !1multiphosphoryltransfer protein; phosphotransferase system !1enzyme I homology; phosphotransferase system !1mannitol-specific enzyme II factor III homology; !1phosphotransferase system phosphohistidine-containing !1protein homology KEYWORDS phosphocarrier protein; phosphohistidine; phosphoprotein; !1phosphotransferase system; sugar transport system FEATURE !$17-140 #domain phosphotransferase system mannitol-specific !8enzyme II factor III homology #label PT3M\ !$164-240 #domain phosphotransferase system !8phosphohistidine-containing protein homology #label !8HPR\ !$274-823 #domain phosphotransferase system enzyme I homology !8#label PT1\ !$171 #active_site His (phosphohistidine intermediate) !8#status predicted\ !$202 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 827 #molecular-weight 86393 #checksum 79 SEQUENCE /// ENTRY S51680 #type complete TITLE fructose phosphotransferase multiphosphoryltransfer protein - Xanthomonas campestris CONTAINS phosphocarrier protein HPr; phosphotransferase system enzyme I (EC 2.7.3.9); phosphotransferase system enzyme II (EC 2.7.1.69), fructose-specific, factor III ORGANISM #formal_name Xanthomonas campestris DATE 07-May-1995 #sequence_revision 31-Jan-1997 #text_change 11-Jun-1999 ACCESSIONS S51680 REFERENCE S51680 !$#authors De Crecy-Lagard, V.; Danchin, A. !$#submission submitted to the EMBL Data Library, September 1994 !$#description Phosphotransferase system of Xanthomonas compestris pv. !1campestris : characterization of the fruB gene. !$#accession S51680 !'##status preliminary !'##molecule_type DNA !'##residues 1-837 ##label DEC !'##cross-references EMBL:Z37113; NID:g603896; PIDN:CAA85482.1; !1PID:g603897 GENETICS !$#gene fruB !$#start_codon TTG CLASSIFICATION #superfamily fructose phosphotransferase !1multiphosphoryltransfer protein; phosphotransferase system !1enzyme I homology; phosphotransferase system !1mannitol-specific enzyme II factor III homology; !1phosphotransferase system phosphohistidine-containing !1protein homology KEYWORDS phosphocarrier protein; phosphohistidine; phosphoprotein; !1phosphotransferase system; sugar transport system FEATURE !$22-145 #domain phosphotransferase system mannitol-specific !8enzyme II factor III homology #label PT3M\ !$168-244 #domain phosphotransferase system !8phosphohistidine-containing protein homology #label !8HPR\ !$275-826 #domain phosphotransferase system enzyme I homology !8#label PT1\ !$175 #active_site His (phosphohistidine intermediate) !8#status predicted\ !$206 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 837 #molecular-weight 88442 #checksum 3102 SEQUENCE /// ENTRY B64069 #type complete TITLE fructose phosphotransferase multiphosphoryltransfer protein - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES fructose-permease IIA/FPR component (fruB) homolog ORGANISM #formal_name Haemophilus influenzae DATE 18-Aug-1995 #sequence_revision 31-Jan-1997 #text_change 11-Jun-1999 ACCESSIONS B64069 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession B64069 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-499 ##label TIGR !'##cross-references GB:U32727; GB:L42023; NID:g1573415; !1PIDN:AAC22107.1; PID:g1573424; TIGR:HI0448 !'##note named as homolog to a protein from Escherichia coli CLASSIFICATION #superfamily fructose phosphotransferase !1multiphosphoryltransfer protein homolog; phosphotransferase !1system mannitol-specific enzyme II factor III homology; !1phosphotransferase system phosphohistidine-containing !1protein homology KEYWORDS duplication; phosphohistidine; phosphoprotein; !1phosphotransferase system; sugar transport system FEATURE !$17-140 #domain phosphotransferase system mannitol-specific !8enzyme II factor III homology #label PT3M\ !$293-372 #domain phosphotransferase system !8phosphohistidine-containing protein homology #label !8HPR1\ !$417-496 #domain phosphotransferase system !8phosphohistidine-containing protein homology #label !8HPR2\ !$300 #active_site His (phosphohistidine intermediate) !8#status predicted\ !$334 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$424 #active_site His (phosphohistidine intermediate) !8#status predicted\ !$458 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 499 #molecular-weight 53007 #checksum 7317 SEQUENCE /// ENTRY WQEBST #type complete TITLE phosphotransferase system enzyme II (EC 2.7.1.69), sucrose-specific, factor II - Salmonella typhimurium plasmid pUR400 ALTERNATE_NAMES phosphotransferase system enzyme II-sucrose; protein-Npi-phosphohistidine-sugar phosphotransferase, sucrose-specific, enzyme II; sucrose transporter, enzyme II ORGANISM #formal_name Salmonella typhimurium DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 11-Jun-1999 ACCESSIONS S01036; S62329; S35016 REFERENCE S01036 !$#authors Ebner, R.; Lengeler, J.W. !$#journal Mol. Microbiol. (1988) 2:9-17 !$#title DNA sequence of the gene scrA encoding the sucrose transport !1protein enzyme-II(Scr) of the phosphotransferase system from !1enteric bacteria: homology of the enzyme-II(Scr) and !1enzyme-II(Bgl) proteins. !$#cross-references MUID:88216186; PMID:3285123 !$#accession S01036 !'##molecule_type DNA !'##residues 1-455 ##label EBN !'##cross-references EMBL:Y00541; NID:g47925; PIDN:CAA68605.1; !1PID:g47926 REFERENCE S62329 !$#authors Titgemeyer, F.; Jahreis, K.; Ebner, R.; Lengeler, J.W. !$#journal Mol. Gen. Genet. (1996) 250:197-206 !$#title Molecular analysis of the scrA and scrB genes from !1Klebsiella pneumoniae and plasmid pUR400, which encode the !1sucrose transport protein Enzyme II(Scr) of the !1phosphotransferase system and a sucrose-6-phosphate !1invertase. !$#cross-references MUID:96188840; PMID:8628219 !$#accession S62329 !'##molecule_type DNA !'##residues 1-7,9-24,'HC',26-36,38-46,49-76,78-140,'N','A',145-207,'E', !1211-230,'V','EKL',238,'R',240-264,266-278,280-313,315-344, !1346-391,393-403,405-434,'IAFV',439,'FS',442,448-455 ##label !1TIT REFERENCE S35014 !$#authors Jahreis, K.; Lengeler, J.W. !$#journal Mol. Microbiol. (1993) 9:195-209 !$#title Molecular analysis of two ScrR repressors and of a ScrR-FruR !1hybrid repressor for sucrose and D-fructose specific !1regulons from enteric bacteria. !$#cross-references MUID:94018607; PMID:8412665 !$#accession S35016 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-24,'HC',26-435,'IAFGVAFTV',445-455 ##label JAH !'##cross-references EMBL:X67750; NID:g395262; PIDN:CAA47973.1; !1PID:g395263 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1992 GENETICS !$#gene scrA !$#genome plasmid CLASSIFICATION #superfamily phosphotransferase system sucrose-specific !1enzyme II, factor II KEYWORDS membrane protein; phosphoprotein; phosphotransferase; sugar !1transport system FEATURE !$308 #active_site His #status predicted SUMMARY #length 455 #molecular-weight 47800 #checksum 6990 SEQUENCE /// ENTRY B32243 #type complete TITLE phosphotransferase system enzyme II (EC 2.7.1.69), sucrose-specific - Streptococcus mutans ORGANISM #formal_name Streptococcus mutans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B32243 REFERENCE A32243 !$#authors Sato, Y.; Poy, F.; Jacobson, G.R.; Kuramitsu, H.K. !$#journal J. Bacteriol. (1989) 171:263-271 !$#title Characterization and sequence analysis of the scrA gene !1encoding enzyme II(scr) of the Streptococcus mutans !1phosphoenolpyruvate-dependent sucrose phosphotransferase !1system. !$#cross-references MUID:89123027; PMID:2536656 !$#accession B32243 !'##status preliminary !'##molecule_type DNA !'##residues 1-664 ##label SAT !'##cross-references GB:M22711; NID:g153799; PIDN:AAA26971.1; !1PID:g153801 CLASSIFICATION #superfamily phosphotransferase system enzyme II !1sucrose-specific; phosphotransferase system glucose-specific !1enzyme II, factor III homology KEYWORDS phosphoprotein; phosphotransferase FEATURE !$511-664 #domain phosphotransferase system glucose-specific !8enzyme II, factor III homology #label PT3G SUMMARY #length 664 #molecular-weight 69988 #checksum 2327 SEQUENCE /// ENTRY WQEC2G #type complete TITLE phosphotransferase system enzyme II (EC 2.7.1.69), glucose-specific, factor II - Escherichia coli (strain K-12) ALTERNATE_NAMES glucose-permease, factor II; phosphotransferase system enzyme II-Glc; protein-N(pi)-phosphohistidine-glucose phosphotransferase, factor II ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 01-Mar-2002 ACCESSIONS A25336; B64854 REFERENCE A25336 !$#authors Erni, B.; Zanolari, B. !$#journal J. Biol. Chem. (1986) 261:16398-16403 !$#title Glucose-permease of the bacterial phosphotransferase system; !1gene cloning, overproduction, and amino acid sequence of !1enzyme II-Glc. !$#cross-references MUID:87057327; PMID:3023349 !$#accession A25336 !'##molecule_type DNA !'##residues 1-477 ##label ERN !'##cross-references GB:J02618; NID:g147392; PIDN:AAA24437.1; !1PID:g147393 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64854 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-477 ##label BLAT !'##cross-references GB:AE000210; GB:U00096; NID:g1787332; !1PIDN:AAC74185.1; PID:g1787343; UWGP:b1101 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ptsG; glcA; umg !$#map_position 24 min !$#start_codon GTG FUNCTION !$#description mediates transport of glucose across the cytoplasmic !1membrane concomitant with sugar phosphorylation; is also a !1chemoreceptor monitoring the environment for changes in !1sugar concentration CLASSIFICATION #superfamily phosphotransferase system glucose-specific !1enzyme II, factor II; phosphotransferase system !1glucose-specific enzyme II, factor II homology KEYWORDS phosphoprotein; phosphotransferase; sugar transport system; !1transmembrane protein FEATURE !$1-477 #domain phosphotransferase system glucose-specific !8enzyme II, factor II homology #label PT2G\ !$16-32 #domain transmembrane #status predicted #label TM1\ !$55-71 #domain transmembrane #status predicted #label TM2\ !$80-96 #domain transmembrane #status predicted #label TM3\ !$116-132 #domain transmembrane #status predicted #label TM4\ !$155-171 #domain transmembrane #status predicted #label TM5\ !$280-296 #domain transmembrane #status predicted #label TM6\ !$313-329 #domain transmembrane #status predicted #label TM7\ !$356-372 #domain transmembrane #status predicted #label TM8\ !$443-459 #domain transmembrane #status predicted #label TM9\ !$421 #active_site Cys (phosphocysteine intermediate) !8#status predicted SUMMARY #length 477 #molecular-weight 50676 #checksum 4218 SEQUENCE /// ENTRY S36620 #type complete TITLE phosphotransferase system enzyme II (EC 2.7.1.69), glucose-specific, factor II - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S36620 REFERENCE S36620 !$#authors Stolz, B.; Wehrli, C.; Erni, B. !$#submission submitted to the EMBL Data Library, August 1993 !$#accession S36620 !'##molecule_type DNA !'##residues 1-477 ##label STO !'##cross-references EMBL:X74629; NID:g397362; PIDN:CAA52702.1; !1PID:g397363 !'##experimental_source strain SB3507 GENETICS !$#gene ptsG FUNCTION !$#description mediates transport of glucose across the cytoplasmic !1membrane concomitant with sugar phosphorylation; is also a !1chemoreceptor monitoring the environment for changes in !1sugar concentration CLASSIFICATION #superfamily phosphotransferase system glucose-specific !1enzyme II, factor II; phosphotransferase system !1glucose-specific enzyme II, factor II homology KEYWORDS phosphoprotein; phosphotransferase; sugar transport system; !1transmembrane protein FEATURE !$1-477 #domain phosphotransferase system glucose-specific !8enzyme II, factor II homology #label PT2G\ !$16-32 #domain transmembrane #status predicted #label TM1\ !$55-71 #domain transmembrane #status predicted #label TM2\ !$80-96 #domain transmembrane #status predicted #label TM3\ !$116-132 #domain transmembrane #status predicted #label TM4\ !$155-171 #domain transmembrane #status predicted #label TM5\ !$280-296 #domain transmembrane #status predicted #label TM6\ !$313-329 #domain transmembrane #status predicted #label TM7\ !$356-372 #domain transmembrane #status predicted #label TM8\ !$443-459 #domain transmembrane #status predicted #label TM9\ !$421 #active_site Cys (phosphocysteine intermediate) !8#status predicted SUMMARY #length 477 #molecular-weight 50521 #checksum 3669 SEQUENCE /// ENTRY D69810 #type complete TITLE phosphotransferase system enzyme II (EC 2.7.1.69) factor II homolog yflF - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS D69810 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D69810 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-452 ##label KUN !'##cross-references GB:Z99108; GB:AL009126; NID:g2633055; !1PIDN:CAB12599.1; PID:g2633094 !'##experimental_source strain 168 GENETICS !$#gene yflF FUNCTION !$#description mediates transport of glucose across the cytoplasmic !1membrane concomitant with sugar phosphorylation; is also a !1chemoreceptor monitoring the environment for changes in !1sugar concentration CLASSIFICATION #superfamily phosphotransferase system glucose-specific !1enzyme II, factor II; phosphotransferase system !1glucose-specific enzyme II, factor II homology KEYWORDS phosphoprotein; phosphotransferase; sugar transport system; !1transmembrane protein FEATURE !$1-452 #domain phosphotransferase system glucose-specific !8enzyme II, factor II homology #label PT2G\ !$12-28 #domain transmembrane #status predicted #label TM01\ !$46-62 #domain transmembrane #status predicted #label TM02\ !$94-110 #domain transmembrane #status predicted #label TM03\ !$133-149 #domain transmembrane #status predicted #label TM04\ !$253-269 #domain transmembrane #status predicted #label TM05\ !$286-302 #domain transmembrane #status predicted #label TM06\ !$329-345 #domain transmembrane #status predicted #label TM07\ !$419-436 #domain transmembrane #status predicted #label TM08\ !$397 #active_site Cys (phosphocysteine intermediate) !8#status predicted SUMMARY #length 452 #molecular-weight 48580 #checksum 7452 SEQUENCE /// ENTRY D70180 #type complete TITLE phosphotransferase system enzyme II (EC 2.7.1.69), glucose-specific, factor II - Lyme disease spirochete ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS D70180 REFERENCE A70100 !$#authors Fraser, C.M.; Casjens, S.; Huang, W.M.; Sutton, G.G.; !1Clayton, R.; Lathigra, R.; White, O.; Ketchum, K.A.; Dodson, !1R.; Hickey, E.K.; Gwinn, M.; Dougherty, B.; Tomb, J.F.; !1Fleischmann, R.D.; Richardson, D.; Peterson, J.; Kerlavage, !1A.R.; Quackenbush, J.; Salzberg, S.; Hanson, M.; Vugt, R.V.; !1Palmer, N.; Adams, M.D.; Gocayne, J.; Weidman, J.; !1Utterback, T.; Watthey, L.; McDonald, L.; Artiach, P.; !1Bowman, C.; Garland, S.; Fujii, C.; Cotton, M.D.; Horst, K.; !1Roberts, K.; Hatch, B.; Smith, H.O.; Venter, J.C. !$#journal Nature (1997) 390:580-586 !$#title Genomic sequence of a Lyme disease spirochaete, Borrelia !1burgdorferi. !$#cross-references MUID:98065943; PMID:9403685 !$#accession D70180 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-514 ##label KLE !'##cross-references GB:AE001166; GB:AE000783; NID:g2688571; !1PIDN:AAC66998.1; PID:g2688579; TIGR:BB0645 !'##experimental_source strain B31 FUNCTION !$#description mediates transport of glucose across the cytoplasmic !1membrane concomitant with sugar phosphorylation; is also a !1chemoreceptor monitoring the environment for changes in !1sugar concentration CLASSIFICATION #superfamily phosphotransferase system glucose-specific !1enzyme II, factor II; phosphotransferase system !1glucose-specific enzyme II, factor II homology KEYWORDS phosphoprotein; phosphotransferase; sugar transport system; !1transmembrane protein FEATURE !$1-514 #domain phosphotransferase system glucose-specific !8enzyme II, factor II homology #label PT2G\ !$15-31 #domain transmembrane #status predicted #label TM01\ !$66-82 #domain transmembrane #status predicted #label TM02\ !$92-108 #domain transmembrane #status predicted #label TM03\ !$134-150 #domain transmembrane #status predicted #label TM04\ !$173-189 #domain transmembrane #status predicted #label TM05\ !$308-324 #domain transmembrane #status predicted #label TM06\ !$341-357 #domain transmembrane #status predicted #label TM07\ !$388-404 #domain transmembrane #status predicted #label TM08\ !$480-497 #domain transmembrane #status predicted #label TM09\ !$459 #active_site Cys (phosphocysteine intermediate) !8#status predicted SUMMARY #length 514 #molecular-weight 55842 #checksum 7114 SEQUENCE /// ENTRY A70220 #type complete TITLE phosphotransferase system enzyme II (EC 2.7.1.69), maltose- and glucose-specific, factor II - Lyme disease spirochete plasmid B/cp26 ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A70220 REFERENCE A70100 !$#authors Fraser, C.M.; Casjens, S.; Huang, W.M.; Sutton, G.G.; !1Clayton, R.; Lathigra, R.; White, O.; Ketchum, K.A.; Dodson, !1R.; Hickey, E.K.; Gwinn, M.; Dougherty, B.; Tomb, J.F.; !1Fleischmann, R.D.; Richardson, D.; Peterson, J.; Kerlavage, !1A.R.; Quackenbush, J.; Salzberg, S.; Hanson, M.; Vugt, R.V.; !1Palmer, N.; Adams, M.D.; Gocayne, J.; Weidman, J.; !1Utterback, T.; Watthey, L.; McDonald, L.; Artiach, P.; !1Bowman, C.; Garland, S.; Fujii, C.; Cotton, M.D.; Horst, K.; !1Roberts, K.; Hatch, B.; Smith, H.O.; Venter, J.C. !$#journal Nature (1997) 390:580-586 !$#title Genomic sequence of a Lyme disease spirochaete, Borrelia !1burgdorferi. !$#cross-references MUID:98065943; PMID:9403685 !$#accession A70220 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-542 ##label KLE !'##cross-references GB:AE000792; NID:g3253098; PIDN:AAC66326.1; !1PID:g2689888; TIGR:BBB29 !'##experimental_source strain B31 GENETICS !$#genome plasmid FUNCTION !$#description mediates transport of glucose across the cytoplasmic !1membrane concomitant with sugar phosphorylation; is also a !1chemoreceptor monitoring the environment for changes in !1sugar concentration CLASSIFICATION #superfamily phosphotransferase system glucose-specific !1enzyme II, factor II; phosphotransferase system !1glucose-specific enzyme II, factor II homology KEYWORDS phosphoprotein; phosphotransferase; sugar transport system; !1transmembrane protein FEATURE !$6-542 #domain phosphotransferase system glucose-specific !8enzyme II, factor II homology #label PT2G\ !$21-37 #domain transmembrane #status predicted #label TM01\ !$76-92 #domain transmembrane #status predicted #label TM02\ !$102-118 #domain transmembrane #status predicted #label TM03\ !$162-178 #domain transmembrane #status predicted #label TM04\ !$201-217 #domain transmembrane #status predicted #label TM05\ !$337-353 #domain transmembrane #status predicted #label TM06\ !$371-387 #domain transmembrane #status predicted #label TM07\ !$418-434 #domain transmembrane #status predicted #label TM08\ !$510-527 #domain transmembrane #status predicted #label TM09\ !$488 #active_site Cys (phosphocysteine intermediate) !8#status predicted SUMMARY #length 542 #molecular-weight 58937 #checksum 4346 SEQUENCE /// ENTRY G64918 #type complete TITLE phosphotransferase system enzyme II (EC 2.7.1.69) factor II, maltose- and glucose-specific - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS G64918; B42477; PV0011 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64918 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-530 ##label BLAT !'##cross-references GB:AE000258; GB:U00096; NID:g2367121; !1PIDN:AAC74693.1; PID:g1787908; UWGP:b1621 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A42477 !$#authors Reidl, J.; Boos, W. !$#journal J. Bacteriol. (1991) 173:4862-4876 !$#title The malX malY operon of Escherichia coli encodes a novel !1enzyme II of the phosphotransferase system recognizing !1glucose and maltose and an enzyme abolishing the endogenous !1induction of the maltose system. !$#cross-references MUID:91310596; PMID:1856179 !$#accession B42477 !'##status preliminary !'##molecule_type DNA !'##residues 1-143,'Y',145-295,'N',297-431,'R',433-530 ##label REI !'##cross-references GB:M60722; NID:g146690; PIDN:AAA24098.1; !1PID:g146692 REFERENCE JV0031 !$#authors Reidl, J.; Roemisch, K.; Ehrmann, M.; Boos, W. !$#journal J. Bacteriol. (1989) 171:4888-4899 !$#title MalI, a novel protein involved in regulation of the maltose !1system of Escherichia coli, is highly homologous to the !1repressor proteins GalR, CytR, and LacI. !$#cross-references MUID:89359124; PMID:2670898 !$#accession PV0011 !'##molecule_type DNA !'##residues 1-119, !1'AFCQPRMPRLKRRTKNAKAFHDKMRKLTFRASNETDVLITAFYSLHGDPREF' !1##label RE2 !'##cross-references GB:M28539; NID:g146707; PIDN:AAA24103.1; !1PID:g146708 GENETICS !$#gene malX !$#map_position 36 min FUNCTION !$#description mediates transport of glucose and maltose across the !1cytoplasmic membrane concomitant with sugar phosphorylation; !1is also a chemoreceptor monitoring the environment for !1changes in sugar concentration CLASSIFICATION #superfamily phosphotransferase system glucose-specific !1enzyme II, factor II; phosphotransferase system !1glucose-specific enzyme II, factor II homology KEYWORDS phosphoprotein; phosphotransferase; sugar transport system; !1transmembrane protein FEATURE !$7-528 #domain phosphotransferase system glucose-specific !8enzyme II, factor II homology #label PT2G\ !$22-38 #domain transmembrane #status predicted #label TM01\ !$73-89 #domain transmembrane #status predicted #label TM02\ !$99-115 #domain transmembrane #status predicted #label TM03\ !$146-162 #domain transmembrane #status predicted #label TM04\ !$185-201 #domain transmembrane #status predicted #label TM05\ !$321-337 #domain transmembrane #status predicted #label TM06\ !$354-370 #domain transmembrane #status predicted #label TM07\ !$399-415 #domain transmembrane #status predicted #label TM08\ !$493-510 #domain transmembrane #status predicted #label TM09\ !$471 #active_site Cys (phosphocysteine intermediate) !8#status predicted SUMMARY #length 530 #molecular-weight 56627 #checksum 1161 SEQUENCE /// ENTRY S07661 #type complete TITLE probable phosphotransferase system enzyme II (EC 2.7.1.69) - Klebsiella pneumoniae ALTERNATE_NAMES hypothetical protein 162 (rpoN 3'-region) ORGANISM #formal_name Klebsiella pneumoniae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S07661 REFERENCE S07659 !$#authors Merrick, M.J.; Coppard, J.R. !$#journal Mol. Microbiol. (1989) 3:1765-1775 !$#title Mutations in genes downstream of the rpoN gene (encoding !1sigma54) of Klebsiella pneumoniae affect expression from !1sigma54-dependent promoters. !$#cross-references MUID:90158124; PMID:2695747 !$#accession S07661 !'##molecule_type DNA !'##residues 1-162 ##label MER !'##cross-references EMBL:X16335; NID:g43924; PIDN:CAA34392.1; !1PID:g43927 CLASSIFICATION #superfamily phosphotransferase system enzyme II; !1phosphotransferase system mannitol-specific enzyme II factor !1III homology KEYWORDS phosphoprotein; phosphotransferase FEATURE !$27-154 #domain phosphotransferase system mannitol-specific !8enzyme II factor III homology #label PT3M SUMMARY #length 162 #molecular-weight 17720 #checksum 6558 SEQUENCE /// ENTRY WQEC2N #type complete TITLE phosphotransferase system enzyme II (EC 2.7.1.69), N-acetylglucosamine-specific - Escherichia coli (strain K-12) ALTERNATE_NAMES protein-N(pi)-phosphohistidine-N-acetylglucosamine phosphotransferase ORGANISM #formal_name Escherichia coli DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 01-Mar-2002 ACCESSIONS B29895; A28896; F64802 REFERENCE A91590 !$#authors Rogers, M.J.; Ohgi, T.; Plumbridge, J.; Soell, D. !$#journal Gene (1988) 62:197-207 !$#title Nucleotide sequences of the Escherichia coli nagE and nagB !1genes: the structural genes for the N-acetylglucosamine !1transport protein of the bacterial phosphoenolpyruvate:sugar !1phosphotransferase system and for glucosamine-6-phosphate !1deaminase. !$#cross-references MUID:88212176; PMID:3284790 !$#accession B29895 !'##molecule_type DNA !'##residues 1-648 ##label ROG !'##cross-references GB:M19284; GB:M17907; GB:M21684; NID:g146911; !1PIDN:AAA24192.1; PID:g146913 REFERENCE A28896 !$#authors Peri, K.G.; Waygood, E.B. !$#journal Biochemistry (1988) 27:6054-6061 !$#title Sequence of cloned enzyme II-N-acetylglucosamine-of the !1phosphoenolpyruvate: N-acetylglucosamine phosphotransferase !1system of Escherichia coli. !$#cross-references MUID:89050950; PMID:3056518 !$#accession A28896 !'##molecule_type DNA !'##residues 1-648 ##label PER !'##cross-references GB:M19284; GB:M21684; NID:g146911; PIDN:AAA24192.1; !1PID:g146913 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64802 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-648 ##label BLAT !'##cross-references GB:AE000171; GB:U00096; NID:g1786888; !1PIDN:AAC73773.1; PID:g1786894; UWGP:b0679 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene nagE; pstN !$#map_position 16 min CLASSIFICATION #superfamily phosphotransferase system !1N-acetylglucosamine-specific enzyme II; phosphotransferase !1system glucose-specific enzyme II, factor II homology; !1phosphotransferase system glucose-specific enzyme II, factor !1III homology KEYWORDS phosphohistidine; phosphoprotein; phosphotransferase; sugar !1transport system; transmembrane protein FEATURE !$1-468 #domain phosphotransferase system glucose-specific !8enzyme II, factor II homology #label PT2G\ !$14-30 #domain transmembrane #status predicted #label TM1\ !$44-60 #domain transmembrane #status predicted #label TM2\ !$74-90 #domain transmembrane #status predicted #label TM3\ !$94-110 #domain transmembrane #status predicted #label TM4\ !$132-148 #domain transmembrane #status predicted #label TM5\ !$236-252 #domain transmembrane #status predicted #label TM6\ !$260-276 #domain transmembrane #status predicted #label TM7\ !$282-298 #domain transmembrane #status predicted #label TM8\ !$301-317 #domain transmembrane #status predicted #label TM9\ !$339-355 #domain transmembrane #status predicted #label TM10\ !$495-648 #domain phosphotransferase system glucose-specific !8enzyme II, factor III homology #label PT3G\ !$412 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$569 #active_site His (phosphohistidine intermediate) !8#status predicted SUMMARY #length 648 #molecular-weight 68346 #checksum 4523 SEQUENCE /// ENTRY S18607 #type complete TITLE phosphotransferase system enzyme II (EC 2.7.1.69), N-acetylglucosamine-specific - Klebsiella pneumoniae ORGANISM #formal_name Klebsiella pneumoniae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S18607 REFERENCE S18607 !$#authors Vogler, A.P.; Lengeler, J.W. !$#journal Mol. Gen. Genet. (1991) 230:270-276 !$#title Comparison of the sequences of the nagE operons from !1Klebsiella pneumoniae and Escherichia coli K12: Enhanced !1variability of the enzyme II(N-acetylglucosamine) in regions !1connecting functional domains. !$#cross-references MUID:92079906; PMID:1745234 !$#accession S18607 !'##status preliminary !'##molecule_type DNA !'##residues 1-651 ##label VOG !'##cross-references EMBL:X63289; NID:g43818; PIDN:CAA44923.1; !1PID:g43819 GENETICS !$#gene nagE CLASSIFICATION #superfamily phosphotransferase system !1N-acetylglucosamine-specific enzyme II; phosphotransferase !1system glucose-specific enzyme II, factor II homology; !1phosphotransferase system glucose-specific enzyme II, factor !1III homology KEYWORDS phosphotransferase; sugar transport system FEATURE !$1-468 #domain phosphotransferase system glucose-specific !8enzyme II, factor II homology #label PT2G\ !$497-650 #domain phosphotransferase system glucose-specific !8enzyme II, factor III homology #label PT3G SUMMARY #length 651 #molecular-weight 68179 #checksum 1686 SEQUENCE /// ENTRY WQBSGS #type complete TITLE phosphotransferase system enzyme II (EC 2.7.1.69), glucose-specific, factor II [validated] - Bacillus subtilis ALTERNATE_NAMES glucose permease; phosphoenolpyruvate:glucose phosphotransferase system enzyme II, glucose-specific; protein-Npi-phosphohistidine-sugar phosphotransferase, glucose-specific, factor II; PTS glucose-specific enzyme IIABC component ptsG ORGANISM #formal_name Bacillus subtilis DATE 31-Mar-1991 #sequence_revision 31-Dec-1992 #text_change 15-Sep-2000 ACCESSIONS S25083; A36101; S15272; S04174; S04175; A57142; E69683; !1S22752 REFERENCE S25083 !$#authors Zagorec, M.; Postma, P.W. !$#journal Mol. Gen. Genet. (1992) 234:325-328 !$#title Cloning and nucleotide sequence of the ptsG gene of Bacillus !1subtilis. !$#cross-references MUID:92375001; PMID:1508157 !$#accession S25083 !'##molecule_type DNA !'##residues 1-699 ##label ZAG !'##cross-references EMBL:Z11744; NID:g39955; PIDN:CAA77803.1; !1PID:g39956 REFERENCE A36101 !$#authors Sutrina, S.L.; Reddy, P.; Saier Jr., M.H.; Reizer, J. !$#journal J. Biol. Chem. (1990) 265:18581-18589 !$#title The glucose permease of Bacillus subtilis is a single !1polypeptide chain that functions to energize the sucrose !1permease. !$#cross-references MUID:91009360; PMID:2120236 !$#accession A36101 !'##molecule_type DNA !'##residues 483-558 ##label SUT !'##cross-references GB:M60344; NID:g143017; PIDN:AAA22498.1; !1PID:g143018 REFERENCE S15272 !$#authors Gonzy-Treboul, G.; de Waard, J.H.; Zagorec, M.; Postma, P.W. !$#journal Mol. Microbiol. (1991) 5:1241-1249 !$#title The glucose permease of the phosphotransferase system of !1Bacillus subtilis: evidence for II(Glc) and III(Glc) !1domains. !$#cross-references MUID:92065821; PMID:1956301 !$#accession S15272 !'##molecule_type DNA !'##residues 249-699 ##label MOL !'##cross-references EMBL:Z11744; NID:g39955 REFERENCE S04174 !$#authors Gonzy-Treboul, G.; Zagorec, M.; Rain-Guion, M.C.; Steinmetz, !1M. !$#journal Mol. Microbiol. (1989) 3:103-112 !$#title Phosphoenolpyruvate:sugar phosphotransferase system of !1Bacillus subtilis: nucleotide sequence of ptsX, ptsH and the !15'-end of ptsI and evidence for a ptsHI operon. !$#cross-references MUID:89237891; PMID:2497294 !$#accession S04174 !'##molecule_type DNA !'##residues 361-517,'SLDLSRKHLLKRK' ##label GO1 !'##cross-references EMBL:X12832; NID:g48679; PIDN:CAA31315.1; !1PID:g48680 !$#accession S04175 !'##molecule_type DNA !'##residues 'M',539-699 ##label GO2 !'##cross-references EMBL:X12832; NID:g48679; PIDN:CAA31316.1; !1PID:g580912 !'##note these sequences have been revised in reference S15272 REFERENCE A57142 !$#authors Tolner, B.; Ubbink-Kok, T.; Poolman, B.; Konings, W.N. !$#journal J. Bacteriol. (1995) 177:2863-2869 !$#title Characterization of the proton/glutamate symport protein of !1Bacillus subtilis and its functional expression in !1Escherichia coli. !$#cross-references MUID:95270606; PMID:7751298 !$#accession A57142 !'##status preliminary !'##molecule_type DNA !'##residues 568-572,'E',574-577,'E',579-582,'I',584-587,'K',589-590, !1'A',592,'AD',595,'E',597,'VSI',601-608,'FM',611,'A',613-614, !1'T',616-620,'V',622-626,'K',628,'N',630-633,'EAH',637,'TS', !1640,'QA',643,'KQ',646,'EL',649-650,'TF',653-654,'NYI',658, !1'QHAA',663,'AI',666-667,'VI',670-672,'TS',675,692-693,'LKH', !1697,'QMK' ##label TOL !'##cross-references GB:U15147; NID:g558838; PIDN:AAA82877.1; !1PID:g558839 REFERENCE A51205 !$#authors Liao, D.I.; Herzberg, O. !$#submission submitted to the Brookhaven Protein Data Bank, September !11991 !$#cross-references PDB:1GPR !$#contents annotation; X-ray crystallography, 1.9 angstroms, residues !1541-698 REFERENCE A58685 !$#authors Kapadia, G.; Chen, C.C.H.; Reddy, P.; Saier Jr., M.H.; !1Reizer, J.; Herzberg, O. !$#journal J. Mol. Biol. (1991) 221:1079-1080 !$#title Crystallization of the IIA domain of the glucose permease of !1Bacillus subtilis. !$#cross-references MUID:92046050; PMID:1942043 !$#contents annotation REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69683 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-699 ##label KUN !'##cross-references GB:Z99111; GB:AL009126; NID:g2633699; !1PIDN:CAB13262.1; PID:g2633760 !'##experimental_source strain 168 GENETICS !$#gene ptsG FUNCTION !$#description transfers a phosphate group from phosphocarrier protein to a !1sugar which is translocated inside the cell CLASSIFICATION #superfamily phosphotransferase system !1N-acetylglucosamine-specific enzyme II; phosphotransferase !1system glucose-specific enzyme II, factor II homology; !1phosphotransferase system glucose-specific enzyme II, factor !1III homology KEYWORDS phosphohistidine; phosphoprotein; phosphotransferase; sugar !1transport system FEATURE !$1-517 #domain phosphotransferase system glucose-specific !8enzyme II, factor II homology #label PT2G\ !$546-699 #domain phosphotransferase system glucose-specific !8enzyme II, factor III homology #label PT3G\ !$461 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$620 #active_site His (phosphohistidine intermediate) !8#status predicted SUMMARY #length 699 #molecular-weight 75525 #checksum 64 SEQUENCE /// ENTRY S46952 #type complete TITLE phosphotransferase system enzyme II (EC 2.7.1.69), glucose-specific, factor IIA - Staphylococcus carnosus ALTERNATE_NAMES glucose permease; phosphoenolpyruvate:glucose phosphotransferase system enzyme II, glucose-specific; phosphotransferase system enzyme II, glucose-specific, factor 1; protein-Npi-phosphohistidine-sugar phosphotransferase, glucose-specific, factor II ORGANISM #formal_name Staphylococcus carnosus DATE 06-Jan-1995 #sequence_revision 31-Jan-1997 #text_change 11-Jun-1999 ACCESSIONS S46952; S63605 REFERENCE S46952 !$#authors Christiansen, I.; Hengstenberg, W. !$#submission submitted to the EMBL Data Library, July 1994 !$#description Staphylococcal phosphoenolpyruvate-dependent !1phosphotransferase system: molecular cloning and nucleotide !1sequence of the Staphylococcus carnosus ptsG gene and !1expression in E.coli. !$#accession S46952 !'##status preliminary !'##molecule_type DNA !'##residues 1-675 ##label CHR !'##cross-references EMBL:X80415; NID:g515383; PID:g515384 !'##experimental_source strain TM300 REFERENCE S63605 !$#authors Christiansen, I.; Hengstenberg, W. !$#journal Mol. Gen. Genet. (1996) 250:375-379 !$#title Cloning and sequencing of two genes from Staphylococcus !1carnosus coding for glucose-specific PTS and their !1expression in Escherichia coli K-12. !$#cross-references MUID:96180655; PMID:8602153 !$#accession S63605 !'##status preliminary !'##molecule_type DNA !'##residues 1-675 ##label CH2 !'##cross-references EMBL:X93360; NID:g1072417; PIDN:CAA63742.1; !1PID:g1072418 !'##experimental_source strain TM300 GENETICS !$#gene glcA; ptsG CLASSIFICATION #superfamily phosphotransferase system !1N-acetylglucosamine-specific enzyme II; phosphotransferase !1system glucose-specific enzyme II, factor II homology; !1phosphotransferase system glucose-specific enzyme II, factor !1III homology KEYWORDS phosphohistidine; phosphoprotein; phosphotransferase; sugar !1transport system FEATURE !$1-503 #domain phosphotransferase system glucose-specific !8enzyme II, factor II homology #label PT2G\ !$525-675 #domain phosphotransferase system glucose-specific !8enzyme II, factor III homology #label PT3G\ !$447 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$599 #active_site His (phosphohistidine intermediate) !8#status predicted SUMMARY #length 675 #molecular-weight 73110 #checksum 8132 SEQUENCE /// ENTRY S46953 #type complete TITLE phosphotransferase system enzyme II (EC 2.7.1.69), glucose-specific, factor IIB - Staphylococcus carnosus ALTERNATE_NAMES glucose permease; phosphoenolpyruvate:glucose phosphotransferase system enzyme II, glucose-specific; protein-Npi-phosphohistidine-sugar phosphotransferase, glucose-specific, factor II ORGANISM #formal_name Staphylococcus carnosus DATE 06-Jan-1995 #sequence_revision 31-Jan-1997 #text_change 11-Jun-1999 ACCESSIONS S63606; S46953 REFERENCE S63605 !$#authors Christiansen, I.; Hengstenberg, W. !$#journal Mol. Gen. Genet. (1996) 250:375-379 !$#title Cloning and sequencing of two genes from Staphylococcus !1carnosus coding for glucose-specific PTS and their !1expression in Escherichia coli K-12. !$#cross-references MUID:96180655; PMID:8602153 !$#accession S63606 !'##status preliminary !'##molecule_type DNA !'##residues 1-692 ##label CHR !'##cross-references EMBL:X93360; NID:g1072417; PIDN:CAA63743.1; !1PID:g1072419 REFERENCE S46952 !$#authors Christiansen, I.; Hengstenberg, W. !$#submission submitted to the EMBL Data Library, July 1994 !$#description Staphylococcal phosphoenolpyruvate-dependent !1phosphotransferase system: molecular cloning and nucleotide !1sequence of the Staphylococcus carnosus ptsG gene and !1expression in E.coli. !$#accession S46953 !'##molecule_type DNA !'##residues 1-506 ##label CH2 !'##cross-references EMBL:X80415; NID:g515383; PID:g515385 GENETICS !$#gene glcB; ptsG CLASSIFICATION #superfamily phosphotransferase system !1N-acetylglucosamine-specific enzyme II; phosphotransferase !1system glucose-specific enzyme II, factor II homology; !1phosphotransferase system glucose-specific enzyme II, factor !1III homology KEYWORDS phosphohistidine; phosphoprotein; phosphotransferase; sugar !1transport system FEATURE !$4-519 #domain phosphotransferase system glucose-specific !8enzyme II, factor II homology #label PT2G\ !$541-691 #domain phosphotransferase system glucose-specific !8enzyme II, factor III homology #label PT3G\ !$463 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$615 #active_site His (phosphohistidine intermediate) !8#status predicted SUMMARY #length 692 #molecular-weight 75343 #checksum 168 SEQUENCE /// ENTRY WQEC2S #type complete TITLE phosphotransferase system enzyme II (EC 2.7.1.69), sorbitol-specific, factor II - Escherichia coli (strain K-12) ALTERNATE_NAMES phosphotransferase system enzyme II, glucitol-specific, factor II; protein-N(pi)-phosphohistidine-glucitol phosphotransferase, factor II ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 01-Mar-2002 ACCESSIONS A26725; I41071; B65050; C65050 REFERENCE A92638 !$#authors Yamada, M.; Saier Jr., M.H. !$#journal J. Biol. Chem. (1987) 262:5455-5463 !$#title Glucitol-specific enzymes of the phosphotransferase system !1in Escherichia coli: nucleotide sequence of the gut operon. !$#cross-references MUID:87194727; PMID:3553176 !$#accession A26725 !'##molecule_type DNA !'##residues 1-506 ##label YAM !'##cross-references GB:J02708; GB:M36721; NID:g146277; PID:g146278 REFERENCE I41017 !$#authors Wang, M.X.; Church, G.M. !$#journal Nature (1992) 360:606-610 !$#title A whole genome approach to in vivo DNA-protein interactions !1in E. coli. !$#cross-references MUID:93096050; PMID:1334233 !$#accession I41071 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-10 ##label WAN !'##cross-references EMBL:X70016; NID:g312554; PIDN:CAA49614.1; !1PID:g312555 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65050 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-20,'K',22-180,'HLAGATS' ##label BLA1 !'##cross-references GB:AE000354; GB:U00096; NID:g2367149; !1PIDN:AAC75744.1; PID:g1789054; UWGP:b2702 !'##experimental_source strain K-12, substrain MG1655 !$#accession C65050 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 188-314,'F',316-416,'F',418-506 ##label BLA2 !'##cross-references GB:AE000354; GB:U00096; NID:g2367149; !1PIDN:AAC75745.1; PID:g1789055; UWGP:b2703 !'##experimental_source strain K-12, substrain MG1655 !'##note a frameshift error apparently disrupts the sequence in this !1report COMMENT This enzyme is phosphorylated by sorbitol-specific !1phosphotransferase system enzyme II factor III (see !1PIR:WQEC3S). GENETICS !$#gene gutA; srlA; srlA_1; srlA_2; sbl !$#map_position 58 min FUNCTION !$#description transfers phosphate from itself to extracellular glucitol or !1sorbitol to form intracellular glucitol-6-phosphate or !1sorbitol-6-phosphate !$#pathway sugar transport system CLASSIFICATION #superfamily phosphotransferase system sorbitol-specific !1enzyme II, factor II KEYWORDS phosphoprotein; phosphotransferase; sugar transport system; !1transmembrane protein FEATURE !$458 #active_site Cys (phosphocysteine intermediate) !8#status predicted SUMMARY #length 506 #molecular-weight 54009 #checksum 1791 SEQUENCE /// ENTRY WQECP3 #type complete TITLE phosphotransferase system enzyme II (EC 2.7.1.69), glucose-specific, factor III - Escherichia coli (strain K-12) ALTERNATE_NAMES phosphotransferase system, enzyme III-Glc ORGANISM #formal_name Escherichia coli DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 01-Mar-2002 ACCESSIONS C29785; C32345; I41184; H65015 REFERENCE A29785 !$#authors Saffen, D.W.; Presper, K.A.; Doering, T.L.; Roseman, S. !$#journal J. Biol. Chem. (1987) 262:16241-16253 !$#title Sugar transport by the bacterial phosphotransferase system. !1Molecular cloning and structural analysis of the Escherichia !1coli ptsH, ptsI, and crr genes. !$#cross-references MUID:88058992; PMID:2960675 !$#accession C29785 !'##molecule_type mRNA !'##residues 1-169 ##label SAF !'##cross-references GB:J02796; NID:g147397; PIDN:AAA24442.1; !1PID:g147400 REFERENCE A32345 !$#authors De Reuse, H.; Danchin, A. !$#journal J. Bacteriol. (1988) 170:3827-3837 !$#title The ptsH, ptsI, and crr genes of the Escherichia coli !1phosphoenolpyruvate-dependent phosphotransferase system: a !1complex operon with several modes of transcription. !$#cross-references MUID:88314869; PMID:2457575 !$#accession C32345 !'##molecule_type DNA !'##residues 1-169 ##label DER !'##cross-references GB:M21994; NID:g147261; PIDN:AAA24386.1; !1PID:g147265 REFERENCE I41151 !$#authors Hall, B.G.; Sharp, P.M. !$#journal Mol. Biol. Evol. (1992) 9:654-665 !$#title Molecular population genetics of Escherichia coli: DNA !1sequence diversity at the celC, crr and gutB loci of natural !1isolates. !$#cross-references MUID:92334137; PMID:1630305 !$#accession I41184 !'##status preliminary !'##molecule_type DNA !'##residues 1-169 ##label RES !'##cross-references GB:M93598; NID:g145624; PIDN:AAA23613.1; !1PID:g145625 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65015 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-169 ##label BLAT !'##cross-references GB:AE000329; GB:U00096; NID:g2367137; !1PIDN:AAC75470.1; PID:g1788757; UWGP:b2417 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene crr !$#map_position 52 min FUNCTION !$#description the phosphoenolpyruvate-glycose phosphotransferase system !1(PTS) comprises two general proteins (Hpr and enzyme I) and !1a sugar-specific complex (enzyme II), which consists of a !1pair of factors (II-A/II-B or III/II), lipid, and divalent !1cation; the phosphoryl group is transferred from !1phosphoenolpyruvate to enzyme I, to Hpr, to II-A (or III), !1to II-B (or II), and finally to the sugar substrate as it !1crosses the cell membrane !$#note this protein in the dephosphorylated form acts as an !1inhibitor of certain non-PTS sugar transport systems, !1whereas the phosphorylated protein may be an activator for !1adenylate cyclase and therefore affects the cAMP !1concentration in the cell CLASSIFICATION #superfamily phosphotransferase system glucose-specific !1enzyme II, factor III; phosphotransferase system !1glucose-specific enzyme II, factor III homology KEYWORDS phosphoprotein; phosphotransferase; sugar transport system FEATURE !$17-169 #domain phosphotransferase system glucose-specific !8enzyme II, factor III homology #label PT3G SUMMARY #length 169 #molecular-weight 18251 #checksum 5581 SEQUENCE /// ENTRY WQEB3T #type complete TITLE phosphotransferase system enzyme II (EC 2.7.1.69), glucose-specific, factor III - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 11-Jun-1999 ACCESSIONS A03405 REFERENCE A03405 !$#authors Nelson, S.O.; Schuitema, A.R.J.; Benne, R.; van der Ploeg, !1L.H.T.; Plijter, J.S.; Aan, F.; Postma, P.W. !$#journal EMBO J. (1984) 3:1587-1593 !$#title Molecular cloning, sequencing, and expression of the crr !1gene: the structural gene for III(Glc) of the bacterial !1PEP:glucose phosphotransferse system. !$#cross-references MUID:84261459; PMID:6086327 !$#accession A03405 !'##molecule_type DNA !'##residues 1-169 ##label NEL !'##cross-references GB:X05210; NID:g47657; PIDN:CAA28837.1; PID:g47658 COMMENT This phosphocarrier protein is one of the components of the !1glucose-specific phosphotransferase system, a major !1carbohydrate active-transport system. The phosphoryl group !1from phosphoenolpyruvate is transferred to phosphocarrier !1protein HPr by enzyme I, from phospho-HPr to factor III, and !1then from phospho-factor III to glucose by enzyme II. COMMENT The nonphosphorylated factor III is an inhibitor for uptake !1of certain sugars such as maltose, melibiose, lactose, and !1glycerol. Phosphorylated factor III, however, may be an !1activator for adenylate cyclase. It is an important !1regulatory protein for cell metabolism. GENETICS !$#gene crr !$#map_position 48 CLASSIFICATION #superfamily phosphotransferase system glucose-specific !1enzyme II, factor III; phosphotransferase system !1glucose-specific enzyme II, factor III homology KEYWORDS phosphoprotein; phosphotransferase; sugar transport system FEATURE !$17-169 #domain phosphotransferase system glucose-specific !8enzyme II, factor III homology #label PT3G SUMMARY #length 169 #molecular-weight 18247 #checksum 5496 SEQUENCE /// ENTRY WQEC3S #type complete TITLE phosphotransferase system enzyme II (EC 2.7.1.69), sorbitol-specific, factor III - Escherichia coli (strain K-12) ALTERNATE_NAMES phosphotransferase enzyme III, glucitol-specific; protein-N (pi)-phosphohistidine-glucitol phosphotransferase, factor III ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 01-Mar-2002 ACCESSIONS B26725; D65050 REFERENCE A92638 !$#authors Yamada, M.; Saier Jr., M.H. !$#journal J. Biol. Chem. (1987) 262:5455-5463 !$#title Glucitol-specific enzymes of the phosphotransferase system !1in Escherichia coli: nucleotide sequence of the gut operon. !$#cross-references MUID:87194727; PMID:3553176 !$#accession B26725 !'##molecule_type DNA !'##residues 1-123 ##label YAM !'##cross-references GB:J02708; GB:M36721; NID:g3002464; !1PIDN:AAC13412.1; PID:g146279 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65050 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-123 ##label BLAT !'##cross-references GB:AE000354; GB:U00096; NID:g2367149; !1PIDN:AAC75746.1; PID:g1789056; UWGP:b2704 !'##experimental_source strain K-12, substrain MG1655 COMMENT This enzyme acts to phosphorylate sorbitol-specific !1phosphotransferase system enzyme II factor II (see !1PIR:WQEC2S) using the phosphotransferase system !1phosphohistidine-containing protein (see PIR:WQECPH). GENETICS !$#gene gutB; srlB !$#map_position 58 min FUNCTION !$#description catalyzes the transfer of phosphate from the !1phosphotransferase system phosphohistidine-containing !1protein to a specific phosphotransferase system enzyme II !1factor II !$#pathway sugar transport system CLASSIFICATION #superfamily phosphotransferase system sorbitol-specific !1enzyme II, factor III KEYWORDS phosphohistidine; phosphoprotein; phosphotransferase; sugar !1transport system FEATURE !$43 #active_site His (phosphohistidine intermediate) !8#status predicted SUMMARY #length 123 #molecular-weight 13304 #checksum 9161 SEQUENCE /// ENTRY WQSA3L #type complete TITLE phosphotransferase system enzyme II (EC 2.7.1.69), lactose-specific, factor III - Staphylococcus aureus ORGANISM #formal_name Staphylococcus aureus DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 20-Feb-1998 ACCESSIONS A03406; A28474 REFERENCE A03406 !$#authors Stuber, K.; Deutscher, J.; Sobek, H.M.; Hengstenberg, W.; !1Beyreuther, K. !$#journal Biochemistry (1985) 24:1164-1168 !$#title Amino acid sequence of the amphiphilic phosphocarrier !1protein factor III(Lac) of the lactose-specific !1phosphotransferase system of Staphylococcus. !$#cross-references MUID:86159654; PMID:4096897 !$#accession A03406 !'##molecule_type protein !'##residues 1-103 ##label STU REFERENCE A92619 !$#authors Breidt Jr., F.; Hengstenberg, W.; Finkeldei, U.; Stewart, !1G.C. !$#journal J. Biol. Chem. (1987) 262:16444-16449 !$#title Identification of the genes for the lactose-specific !1components of the phosphotransferase system in the lac !1operon of Staphylococcus aureus. !$#cross-references MUID:88059023; PMID:2824493 !$#accession A28474 !'##molecule_type DNA !'##residues 1-51,'E',53-80,'L',82-92,'M',94,'H',96-103 ##label BRE COMMENT This phosphocarrier protein is one of the components of the !1lactose-specific phosphotransferase system, a major !1carbohydrate active-transport system. The phosphoryl group !1from phosphoenolpyruvate is transferred to phosphocarrier !1protein HPr by enzyme I, from phospho-HPr to factor III, and !1then from phospho-factor III to lactose by enzyme II. COMMENT This amphiphilic protein, a trimer of identical chains, !1catalyzes the phosphotransfer between the cytoplasmic water !1phase and the membrane lipid phase, changing from a !1hydrophilic protein to a hydrophobic component of the !1membrane-bound phosphotransferase complex upon !1phosphorylation of His-82. CLASSIFICATION #superfamily phosphotransferase system lactose-specific !1enzyme II, factor III KEYWORDS membrane-associated protein; phosphohistidine; !1phosphoprotein; phosphotransferase; sugar transport system FEATURE !$82 #active_site His (phosphohistidine intermediate) !8#status experimental SUMMARY #length 103 #molecular-weight 11366 #checksum 643 SEQUENCE /// ENTRY A23696 #type complete TITLE phosphotransferase system enzyme III (EC 2.7.-.-) - Lactococcus lactis ORGANISM #formal_name Lactococcus lactis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A23696; F39778 REFERENCE A23696 !$#authors de Vos, W.M.; Boerrigter, I.; van Rooyen, R.J.; Reiche, B.; !1Hengstenberg, W. !$#journal J. Biol. Chem. (1990) 265:22554-22560 !$#title Characterization of the lactose-specific enzymes of the !1phosphotransferase system in Lactococcus lactis. !$#cross-references MUID:91093107; PMID:2125052 !$#accession A23696 !'##status preliminary !'##molecule_type DNA !'##residues 1-105 ##label DEV !'##cross-references GB:M60447; GB:J05748; NID:g149404; PIDN:AAA25181.1; !1PID:g149410 REFERENCE A39778 !$#authors van Rooijen, R.J.; van Schalkwijk, S.; de Vos, W.M. !$#journal J. Biol. Chem. (1991) 266:7176-7181 !$#title Molecular cloning, characterization, and nucleotide sequence !1of the tagatose 6-phosphate pathway gene cluster of the !1lactose operon of Lactococcus lactis. !$#cross-references MUID:91201377; PMID:1901863 !$#accession F39778 !'##status preliminary !'##molecule_type DNA !'##residues 1-11 ##label VAN !'##cross-references GB:J05748 CLASSIFICATION #superfamily phosphotransferase system lactose-specific !1enzyme II, factor III KEYWORDS phosphoprotein; phosphotransferase SUMMARY #length 105 #molecular-weight 11448 #checksum 220 SEQUENCE /// ENTRY G43258 #type complete TITLE phosphotransferase system enzyme II (EC 2.7.1.69), lactose-specific, factor III - Streptococcus mutans ALTERNATE_NAMES phosphotransferase system enzyme III, lactose-specific ORGANISM #formal_name Streptococcus mutans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS G43258; S27705 REFERENCE A43258 !$#authors Rosey, E.L.; Stewart, G.C. !$#journal J. Bacteriol. (1992) 174:6159-6170 !$#title Nucleotide and deduced amino acid sequences of the lacR, !1lacABCD, and lacFE genes encoding the repressor, tagatose !16-phosphate gene cluster, and sugar-specific !1phosphotransferase system components of the lactose operon !1of Streptococcus mutans. !$#cross-references MUID:93015655; PMID:1400164 !$#accession G43258 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-104 ##label ROS !'##cross-references EMBL:M80797; NID:g153671; PIDN:AAA26908.1; !1PID:g153677 !'##note sequence extracted from NCBI backbone (NCBIP:115206) GENETICS !$#gene lacF CLASSIFICATION #superfamily phosphotransferase system lactose-specific !1enzyme II, factor III KEYWORDS phosphoprotein; phosphotransferase SUMMARY #length 104 #molecular-weight 11399 #checksum 5040 SEQUENCE /// ENTRY B29898 #type complete TITLE phosphotransferase system enzyme II (EC 2.7.1.69), lactose-specific, factor III - Lactobacillus casei ALTERNATE_NAMES lactose-specific factor IV ORGANISM #formal_name Lactobacillus casei DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B29898 REFERENCE A91591 !$#authors Alpert, C.A.; Chassy, B.M. !$#journal Gene (1988) 62:277-288 !$#title Molecular cloning and nucleotide sequence of the factor III !1(lac) gene of Lactobacillus casei. !$#cross-references MUID:88212183; PMID:3130296 !$#accession B29898 !'##molecule_type DNA !'##residues 1-112 ##label ALP !'##cross-references GB:M20150; NID:g149543; PIDN:AAA25239.1; !1PID:g149545 CLASSIFICATION #superfamily phosphotransferase system lactose-specific !1enzyme II, factor III KEYWORDS phosphocarrier protein; phosphoprotein; phosphotransferase; !1sugar transport SUMMARY #length 112 #molecular-weight 12496 #checksum 7090 SEQUENCE /// ENTRY KIBPD4 #type complete TITLE deoxynucleotide monophosphate kinase (EC 2.7.1.-) - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 11-Jun-1999 ACCESSIONS C92919; B93414; S04612; A04309 REFERENCE A92919 !$#authors Broida, J.; Abelson, J. !$#journal J. Mol. Biol. (1985) 185:545-563 !$#title Sequence organization and control of transcription in the !1bacteriophage T4 tRNA region. !$#cross-references MUID:86037230; PMID:4057254 !$#accession C92919 !'##molecule_type DNA !'##residues 1-241 ##label BRO !'##cross-references GB:X03016; GB:J02511; GB:J02516; GB:J02517; !1GB:V00861; GB:V00862; NID:g15386; PIDN:CAA26800.1; !1PID:g15387 REFERENCE A93414 !$#authors Herrmann, R. !$#journal Nucleic Acids Res. (1982) 10:1105-1112 !$#title Nucleotide sequence of the bacteriophge T4 gene 57 and a !1deduced amino acid sequence. !$#cross-references MUID:82150240; PMID:7063418 !$#accession B93414 !'##molecule_type DNA !'##residues 148-241 ##label HER !'##cross-references GB:X03016; GB:J02516 REFERENCE S04608 !$#authors Koch, T.; Lamm, N.; Rueger, W. !$#journal Nucleic Acids Res. (1989) 17:4392 !$#title Sequencing, cloning and overexpression of genes of !1bacteriophage T4 between map positions 74.325 and 77.184. !$#cross-references MUID:89296504; PMID:2740234 !$#accession S04612 !'##status translation not shown !'##molecule_type DNA !'##residues 1-27 ##label KOC !'##cross-references EMBL:X14845; NID:g15218; PIDN:CAA32953.1; !1PID:g15223 GENETICS !$#gene 1 CLASSIFICATION #superfamily phage T4 deoxynucleotide monophosphate kinase KEYWORDS phosphotransferase SUMMARY #length 241 #molecular-weight 27329 #checksum 9656 SEQUENCE /// ENTRY KIBPP4 #type complete TITLE polynucleotide kinase (EC 2.7.1.-) - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 11-Jun-1999 ACCESSIONS A24642 REFERENCE A24642 !$#authors Midgley, C.A.; Murray, N.E. !$#journal EMBO J. (1985) 4:2695-2703 !$#title T4 polynucleotide kinase; cloning of the gene (pseT) and !1amplification of its product. !$#cross-references MUID:86030251; PMID:2996886 !$#accession A24642 !'##molecule_type DNA !'##residues 1-301 ##label MID !'##cross-references GB:X03007; NID:g15363; PIDN:CAA26792.1; PID:g15364 GENETICS !$#gene pseT CLASSIFICATION #superfamily phage T4 polynucleotide kinase KEYWORDS phosphotransferase SUMMARY #length 301 #molecular-weight 34620 #checksum 4427 SEQUENCE /// ENTRY KIECS #type complete TITLE shikimate kinase (EC 2.7.1.71) II - Escherichia coli (strain K-12) ALTERNATE_NAMES ATP:shikimate 3-phosphotransferase ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 01-Mar-2002 ACCESSIONS A90333; A91812; D64767; A25197; A26018 REFERENCE A90333 !$#authors Millar, G.; Lewendon, A.; Hunter, M.G.; Coggins, J.R. !$#journal Biochem. J. (1986) 237:427-437 !$#title The cloning and expression of the aroL gene from Escherichia !1coli K12; purification and complete amino acid sequence of !1shikimate kinase II, the aroL-gene product. !$#cross-references MUID:87099857; PMID:3026317 !$#accession A90333 !'##molecule_type DNA !'##residues 1-174 ##label MIL !'##cross-references GB:X04064; NID:g40983; PIDN:CAA27696.1; PID:g40984 !'##experimental_source strain K12 REFERENCE A91812 !$#authors DeFeyter, R.C.; Davidson, B.E.; Pittard, J. !$#journal J. Bacteriol. (1986) 165:233-239 !$#title Nucleotide sequence of the transcription unit containing the !1aroL and aroM genes from Escherichia coli K-12. !$#cross-references MUID:86085676; PMID:3001025 !$#accession A91812 !'##molecule_type DNA !'##residues 1-174 ##label DEF !'##cross-references GB:M13045; NID:g145381; PIDN:AAA83833.1; !1PID:g145382 !'##experimental_source K12 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64767 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-174 ##label BLAT !'##cross-references GB:AE000145; GB:U00096; NID:g1786580; !1PIDN:AAC73491.1; PID:g1786587; UWGP:b0388 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene aroL !$#map_position 9 min FUNCTION !$#description catalyzes phosphorylation of shikimic acid to shikimate !13-phosphate !$#pathway aromatic amino acid biosynthesis !$#note magnesium cofactor; other divalent cations are less !1effective CLASSIFICATION #superfamily shikimate kinase; shikimate kinase homology KEYWORDS aromatic amino acid biosynthesis; ATP; magnesium; nucleotide !1binding; P-loop; phosphotransferase FEATURE !$1-113 #domain shikimate kinase homology #label SKI\ !$9-16 #region nucleotide-binding motif A (P-loop) SUMMARY #length 174 #molecular-weight 19151 #checksum 8818 SEQUENCE /// ENTRY S09613 #type complete TITLE shikimate kinase (EC 2.7.1.71) - Erwinia chrysanthemi ALTERNATE_NAMES ATP:shikimate 3-phosphotransferase ORGANISM #formal_name Erwinia chrysanthemi DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S09613 REFERENCE S09613 !$#authors Minton, N.P.; Whitehead, P.J.; Atkinson, T.; Gilbert, H.J. !$#journal Nucleic Acids Res. (1989) 17:1769 !$#title Nucleotide sequence of an Erwinia chrysanthemi gene encoding !1shikimate kinase. !$#cross-references MUID:89160340; PMID:2537963 !$#accession S09613 !'##molecule_type DNA !'##residues 1-173 ##label MIN !'##cross-references EMBL:X14777; NID:g42965; PIDN:CAA32883.1; !1PID:g42966 FUNCTION !$#description catalyzes phosphorylation of shikimic acid to shikimate !13-phosphate !$#pathway aromatic amino acid biosynthesis !$#note magnesium cofactor; other divalent cations are less !1effective CLASSIFICATION #superfamily shikimate kinase; shikimate kinase homology KEYWORDS aromatic amino acid biosynthesis; ATP; magnesium; !1phosphotransferase FEATURE !$1-113 #domain shikimate kinase homology #label SKI SUMMARY #length 173 #molecular-weight 18956 #checksum 6572 SEQUENCE /// ENTRY I39782 #type complete TITLE shikimate kinase (EC 2.7.1.71) aroI - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS I39782; E69590 REFERENCE I39782 !$#authors Nakane, A.; Ogawa, K.; Nakamura, K.; Yamane, K. !$#journal J. Ferment. Bioeng. (1994) 77:312-314 !$#title Nucleotide sequence of the shikimate kinase gene (aroI) of !1Bacillus subtilis. !$#accession I39782 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-186 ##label RES !'##cross-references GB:D63474; NID:g914922; PIDN:BAA09761.1; !1PID:g474964 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69590 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-186 ##label KUN !'##cross-references GB:Z99105; GB:AL009126; NID:g2632457; !1PIDN:CAB12109.1; PID:g2632601 !'##experimental_source strain 168 GENETICS !$#gene aroI CLASSIFICATION #superfamily shikimate kinase; shikimate kinase homology KEYWORDS aromatic amino acid biosynthesis; ATP; magnesium; !1phosphotransferase FEATURE !$10-124 #domain shikimate kinase homology #label SKI SUMMARY #length 186 #molecular-weight 21863 #checksum 3401 SEQUENCE /// ENTRY S21584 #type complete TITLE shikimate kinase (EC 2.7.1.71) precursor - tomato ORGANISM #formal_name Lycopersicon esculentum #common_name tomato DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S21584 REFERENCE S21584 !$#authors Schmid, J.; Schaller, A.; Leibinger, U.; Boll, W.; Amrhein, !1N. !$#submission submitted to the EMBL Data Library, December 1991 !$#description In vitro synthesized tomato shikimate kinase precursor is !1enzymatically active and can be imported into chloroplasts. !$#accession S21584 !'##status preliminary !'##molecule_type mRNA !'##residues 1-300 ##label SCH !'##cross-references EMBL:X63560; NID:g19348; PIDN:CAA45121.1; !1PID:g19349 CLASSIFICATION #superfamily shikimate kinase; shikimate kinase homology KEYWORDS aromatic amino acid biosynthesis; ATP; chloroplast; !1magnesium; phosphotransferase FEATURE !$103-216 #domain shikimate kinase homology #label SKI SUMMARY #length 300 #molecular-weight 33719 #checksum 7279 SEQUENCE /// ENTRY F64054 #type complete TITLE shikimate kinase (EC 2.7.1.71) - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS F64054 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession F64054 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-180 ##label TIGR !'##cross-references GB:U32705; GB:L42023; NID:g1573156; !1PIDN:AAC21875.1; PID:g1573166; TIGR:HI0207 CLASSIFICATION #superfamily shikimate kinase; shikimate kinase homology KEYWORDS phosphotransferase FEATURE !$3-116 #domain shikimate kinase homology #label SKI SUMMARY #length 180 #molecular-weight 20292 #checksum 8689 SEQUENCE /// ENTRY S74659 #type complete TITLE shikimate kinase (EC 2.7.1.71) aroK - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES hypothetical protein sll1669 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S74659 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74659 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-189 ##label KAN !'##cross-references EMBL:D90900; GB:AB001339; NID:g1651768; !1PIDN:BAA16811.1; PID:g1651884 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene aroK CLASSIFICATION #superfamily shikimate kinase; shikimate kinase homology KEYWORDS aromatic amino acid biosynthesis; ATP; magnesium; !1phosphotransferase FEATURE !$11-123 #domain shikimate kinase homology #label SKI SUMMARY #length 189 #molecular-weight 20697 #checksum 6011 SEQUENCE /// ENTRY S52581 #type complete TITLE shikimate kinase (EC 2.7.1.71) - Lactococcus lactis ORGANISM #formal_name Lactococcus lactis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S52581 REFERENCE S52579 !$#authors Griffin, H.G.; Gasson, M.J. !$#journal Mol. Gen. Genet. (1995) 246:119-127 !$#title Genetic aspects of aromatic amino acid biosynthesis in !1Lactococcus lactis. !$#cross-references MUID:95124293; PMID:7823907 !$#accession S52581 !'##status preliminary !'##molecule_type DNA !'##residues 1-162 ##label GRI !'##cross-references EMBL:X78413; NID:g683581; PIDN:CAA55181.1; !1PID:g683584 CLASSIFICATION #superfamily shikimate kinase; shikimate kinase homology KEYWORDS phosphotransferase FEATURE !$1-107 #domain shikimate kinase homology #label SKI SUMMARY #length 162 #molecular-weight 18528 #checksum 6145 SEQUENCE /// ENTRY A65134 #type complete TITLE shikimate kinase (EC 2.7.1.71) I - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS A65134; I41143; S49529; A41967; S25243; S31741 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65134 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-240 ##label BLAT !'##cross-references GB:AE000414; GB:U00096; NID:g1789783; !1PIDN:AAC76415.1; PID:g1789792; UWGP:b3390 !'##experimental_source strain K-12, substrain MG1655 REFERENCE I41143 !$#authors Whipp, M.J.; Pittard, A.J. !$#journal J. Bacteriol. (1995) 177:1627-1629 !$#title A reassessment of the relationship between aroK- and !1aroL-encoded shikimate kinase enzymes of Escherichia coli. !$#cross-references MUID:95189744; PMID:7883721 !$#accession I41143 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 68-240 ##label RES !'##cross-references GB:L39822; NID:g662834; PIDN:AAB59099.1; !1PID:g662835 REFERENCE S49529 !$#authors Griffin, H.G.; Gasson, M.J. !$#submission submitted to the EMBL Data Library, July 1994 !$#description The gene encoding shikimate kinase I from E. coli. !$#accession S49529 !'##status preliminary !'##molecule_type DNA !'##residues 68-240 ##label GRI !'##cross-references EMBL:X80167; NID:g560828; PIDN:CAA56448.1; !1PID:g560829 REFERENCE A41967 !$#authors Lobner-Olesen, A.; Marinus, M.G. !$#journal J. Bacteriol. (1992) 174:525-529 !$#title Identification of the gene (aroK) encoding shikimic acid !1kinase I of Escherichia coli. !$#cross-references MUID:92105021; PMID:1309529 !$#accession A41967 !'##status preliminary !'##molecule_type DNA !'##residues 'MRFQFMSCRA',50-164,'ALSFILKRPSKSNLHARSG' ##label LOB1 !'##cross-references GB:M76389; GB:M76677; NID:g145379; PIDN:AAC36834.1; !1PID:g145380 !'##note sequence extracted from NCBI backbone (NCBIN:75629, !1NCBIP:75630) REFERENCE S25243 !$#authors Lobner-Olesen, A.; Boye, E.; Marinus, M.G. !$#journal Mol. Microbiol. (1992) 6:1841-1851 !$#title Expression of the Escherichia coli dam gene. !$#cross-references MUID:92334160; PMID:1630320 !$#accession S25243 !'##molecule_type DNA !'##residues 'MRFQFMSCRA',50-164,'ALSFILKRPSKSNLHARSG' ##label LOB2 !'##cross-references EMBL:M76389; NID:g145379; PIDN:AAC36834.1; !1PID:g145380; EMBL:Z19601; NID:g41221; PID:g41224 GENETICS !$#gene aroK !$#map_position 27 min CLASSIFICATION #superfamily shikimate kinase; shikimate kinase homology KEYWORDS phosphotransferase FEATURE !$70-183 #domain shikimate kinase homology #label SKI SUMMARY #length 240 #molecular-weight 26973 #checksum 2487 SEQUENCE /// ENTRY KISM6G #type complete TITLE streptomycin 6-kinase (EC 2.7.1.72) - Streptomyces griseus ALTERNATE_NAMES streptidine kinase; streptomycin phosphotransferase ORGANISM #formal_name Streptomyces griseus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 11-Jun-1999 ACCESSIONS S06355; S18495; A37235 REFERENCE S06355 !$#authors Distler, J.; Braun, C.; Ebert, A.; Piepersberg, W. !$#journal Mol. Gen. Genet. (1987) 208:204-210 !$#title Gene cluster for streptomycin biosynthesis in Streptomyces !1griseus: analysis of a central region including the major !1resistance gene. !$#cross-references MUID:87286403; PMID:3039306 !$#accession S06355 !'##molecule_type DNA !'##residues 1-307 ##label DIS !'##cross-references EMBL:X05647; NID:g47075; PIDN:CAA29134.1; !1PID:g47076 !$#accession S18495 !'##molecule_type protein !'##residues 2-15 ##label DIS2 REFERENCE A37235 !$#authors Lim, C.K.; Smith, M.C.M.; Petty, J.; Baumberg, S.; Wootton, !1J.C. !$#journal J. Gen. Microbiol. (1989) 135:3289-3302 !$#title Streptomyces griseus streptomycin phosphotransferase: !1expression of its gene in Escherichia coli and sequence !1homology with other antibiotic phosphotransferases and with !1eukaryotic protein kinases. !$#cross-references MUID:90257580; PMID:2561487 !$#accession A37235 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type DNA !'##residues 1-43,'R',45-150,'P',152-209,'S',211-261,'A',263-271,'A', !1272-298,'S',300-307 ##label LIM GENETICS !$#gene aphD CLASSIFICATION #superfamily streptomycin 6-kinase KEYWORDS antibiotic resistance; ATP; phosphotransferase FEATURE !$2-307 #product streptomycin 6-kinase #status experimental !8#label MAT SUMMARY #length 307 #molecular-weight 33244 #checksum 2163 SEQUENCE /// ENTRY KISM6C #type complete TITLE streptomycin 6-kinase (EC 2.7.1.72) - Streptomyces glaucescens ALTERNATE_NAMES streptomycin phosphotransferase ORGANISM #formal_name Streptomyces glaucescens DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 11-Jun-1999 ACCESSIONS S07039 REFERENCE S06354 !$#authors Voegtli, M.; Huetter, R. !$#journal Mol. Gen. Genet. (1987) 208:195-203 !$#title Characterization of the hydroxystreptomycin !1phosphotransferase gene (sph) of Streptomyces glaucescens: !1nucleotide sequence and promoter analysis. !$#cross-references MUID:87286402; PMID:3039305 !$#accession S07039 !'##molecule_type DNA !'##residues 1-307 ##label VOE !'##cross-references EMBL:X05648; NID:g47104; PIDN:CAA29136.1; !1PID:g47106 GENETICS !$#gene sph CLASSIFICATION #superfamily streptomycin 6-kinase KEYWORDS antibiotic resistance; ATP; phosphotransferase SUMMARY #length 307 #molecular-weight 33153 #checksum 46 SEQUENCE /// ENTRY A38585 #type complete TITLE deoxycytidine kinase (EC 2.7.1.74) - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A38585; S14321 REFERENCE A38585 !$#authors Chottiner, E.G.; Shewach, D.S.; Datta, N.S.; Ashcraft, E.; !1Gribbin, D.; Ginsburg, D.; Fox, I.H.; Mitchell, B.S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:1531-1535 !$#title Cloning and expression of human deoxycytidine kinase cDNA. !$#cross-references MUID:91142207; PMID:1996353 !$#accession A38585 !'##molecule_type mRNA !'##residues 1-260 ##label CHO !'##cross-references GB:M60527; NID:g181509; PIDN:AAA35752.1; !1PID:g181510 REFERENCE S14321 !$#authors Eriksson, S.; Cederlund, E.; Bergman, T.; Joernvall, H.; !1Bohman, C. !$#journal FEBS Lett. (1991) 280:363-366 !$#title Characterization of human deoxycytidine kinase. Correlation !1with cDNA sequences. !$#cross-references MUID:91192170; PMID:2013338 !$#accession S14321 !'##molecule_type protein !'##residues 35-44,'X',46-47,'X',49-56;163-168,'X',170-181;223-236 !1##label ERI !'##note the amino end is blocked GENETICS !$#gene GDB:DCK !'##cross-references GDB:126810; OMIM:125450 !$#map_position 4q13.3-4q21.1 CLASSIFICATION #superfamily human deoxycytidine kinase KEYWORDS ATP; blocked amino end; homodimer; phosphotransferase SUMMARY #length 260 #molecular-weight 30518 #checksum 8023 SEQUENCE /// ENTRY S66044 #type complete TITLE deoxypurine kinase (EC 2.7.1.-) yaaF - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S66044; F69736 REFERENCE S65967 !$#authors Ogasawara, N.; Nakai, S.; Yoshikawa, H. !$#journal DNA Res. (1994) 1:1-14 !$#title Systematic sequencing of the 180 kilobase region of the !1Bacillus subtilis chromosome containing the replication !1origin. !$#cross-references MUID:96051385; PMID:7584024 !$#accession S66044 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-217 ##label OGA !'##cross-references EMBL:D26185; NID:g467326; PIDN:BAA05250.1; !1PID:g467404 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1993 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69736 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-217 ##label KUN !'##cross-references GB:Z99104; GB:AL009126; NID:g2632267; !1PIDN:CAB11790.1; PID:g2632281 !'##experimental_source strain 168 GENETICS !$#gene yaaF CLASSIFICATION #superfamily Lactobacillus acidophilus deoxyadenosine kinase KEYWORDS phosphotransferase SUMMARY #length 217 #molecular-weight 25444 #checksum 714 SEQUENCE /// ENTRY G70129 #type complete TITLE deoxyguanosine/deoxyadenosine kinase I (EC 2.7.1.-) subunit 2 dck homolog - Lyme disease spirochete ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS G70129 REFERENCE A70100 !$#authors Fraser, C.M.; Casjens, S.; Huang, W.M.; Sutton, G.G.; !1Clayton, R.; Lathigra, R.; White, O.; Ketchum, K.A.; Dodson, !1R.; Hickey, E.K.; Gwinn, M.; Dougherty, B.; Tomb, J.F.; !1Fleischmann, R.D.; Richardson, D.; Peterson, J.; Kerlavage, !1A.R.; Quackenbush, J.; Salzberg, S.; Hanson, M.; Vugt, R.V.; !1Palmer, N.; Adams, M.D.; Gocayne, J.; Weidman, J.; !1Utterback, T.; Watthey, L.; McDonald, L.; Artiach, P.; !1Bowman, C.; Garland, S.; Fujii, C.; Cotton, M.D.; Horst, K.; !1Roberts, K.; Hatch, B.; Smith, H.O.; Venter, J.C. !$#journal Nature (1997) 390:580-586 !$#title Genomic sequence of a Lyme disease spirochaete, Borrelia !1burgdorferi. !$#cross-references MUID:98065943; PMID:9403685 !$#accession G70129 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-205 ##label KLE !'##cross-references GB:AE001134; GB:AE000783; NID:g2688133; !1PIDN:AAC66630.1; PID:g2688138; TIGR:BB0239 !'##experimental_source strain B31 CLASSIFICATION #superfamily Lactobacillus acidophilus deoxyadenosine kinase KEYWORDS phosphotransferase SUMMARY #length 205 #molecular-weight 24116 #checksum 3453 SEQUENCE /// ENTRY S66045 #type complete TITLE deoxypurine kinase (EC 2.7.1.-) yaaG - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S66045; G69736 REFERENCE S65967 !$#authors Ogasawara, N.; Nakai, S.; Yoshikawa, H. !$#journal DNA Res. (1994) 1:1-14 !$#title Systematic sequencing of the 180 kilobase region of the !1Bacillus subtilis chromosome containing the replication !1origin. !$#cross-references MUID:96051385; PMID:7584024 !$#accession S66045 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-207 ##label OGA !'##cross-references EMBL:D26185; NID:g467326; PIDN:BAA05251.1; !1PID:g467405 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1993 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69736 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-207 ##label KUN !'##cross-references GB:Z99104; GB:AL009126; NID:g2632267; !1PIDN:CAB11791.1; PID:g2632282 !'##experimental_source strain 168 GENETICS !$#gene yaaG CLASSIFICATION #superfamily Lactobacillus acidophilus deoxyadenosine kinase KEYWORDS phosphotransferase SUMMARY #length 207 #molecular-weight 24145 #checksum 8081 SEQUENCE /// ENTRY PKECT9 #type complete TITLE kanamycin kinase (EC 2.7.1.95) I - Escherichia coli ALTERNATE_NAMES aminoglycoside 3'-phosphotransferase, type 1; aphA1 protein; neomycin-kanamycin phosphotransferase, type I ORGANISM #formal_name Escherichia coli DATE 29-Jul-1981 #sequence_revision 29-Jul-1981 #text_change 21-Jul-2000 ACCESSIONS A00662; A26988; I41094; S49613; I51987 REFERENCE A92864 !$#authors Oka, A.; Sugisaki, H.; Takanami, M. !$#journal J. Mol. Biol. (1981) 147:217-226 !$#title Nucleotide sequence of the kanamycin resistance transposon !1Tn903. !$#cross-references MUID:82033200; PMID:6270337 !$#accession A00662 !'##molecule_type DNA !'##residues 1-271 ##label OKA !'##cross-references GB:V00359; GB:J01839; NID:g43025; PIDN:CAA23656.1; !1PID:g43027 !'##note this enzyme is encoded by the kanamycin resistance transposon !1Tn903 REFERENCE A26988 !$#authors Vakulenko, S.; Kalman, M.; Horvath, B.; Simoncsits, A. !$#journal Nucleic Acids Res. (1987) 15:8111 !$#title The nucleotide sequence of an aminoglycoside !13'-phosphotransferase gene from E. coli. !$#cross-references MUID:88040434; PMID:2823223 !$#accession A26988 !'##molecule_type DNA !'##residues 1-18,'L',20-26,'R',28-47,'N',49-76,'A',78-119,'N',121-271 !1##label VAK !'##cross-references GB:Y00452; NID:g40920; PIDN:CAA68507.1; PID:g40921 !'##note the authors translated the codon AAT for residue 120 as Ile REFERENCE I41094 !$#authors Heidekamp, F.; Baas, P.D.; van Boom, J.H.; Veeneman, G.H.; !1Zipursky, S.L.; Jansz, H.S. !$#journal Nucleic Acids Res. (1981) 9:3335-3354 !$#title Construction and characterization of recombinant plasmid !1DNAs containing sequences of the origin of bacteriophage phi !1X174 DNA replication. !$#cross-references MUID:82014911; PMID:6269080 !$#accession I41094 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 31-145 ##label RES !'##cross-references EMBL:V00293; NID:g41850; PIDN:CAA23568.1; !1PID:g929579 REFERENCE S49612 !$#authors Tavakoli, N.P.; Comanducci, A.; Dodd, H.; Bennett, P.M. !$#submission submitted to the EMBL Data Library, November 1994 !$#description pUB2380 carries a putative transposable element (IS1294) !1capable of mediating one-ended transposition. !$#accession S49613 !'##status preliminary !'##molecule_type DNA !'##residues 1-12,'Q',14-79,'L',81-125,'A',127-271 ##label TAV !'##cross-references EMBL:X82430; NID:g572684; PID:g572686 REFERENCE I51987 !$#authors Menard, R.; Molinas, C.; Arthur, M.; Duval, J.; Courvalin, !1P.; Leclercq, R. !$#journal Antimicrob. Agents Chemother. (1993) 37:78-83 !$#title Overproduction of 3'-aminoglycoside phosphotransferase type !1I confers resistance to tobramycin in Escherichia coli. !$#cross-references MUID:93159149; PMID:8381641 !$#accession I51987 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-18,'L',20-42 ##label RE2 !'##cross-references GB:S54065; NID:g265033; PIDN:AAD13871.1; !1PID:g4261571 GENETICS !$#gene APH; aphA1 CLASSIFICATION #superfamily kanamycin kinase KEYWORDS antibiotic resistance; ATP; phosphotransferase FEATURE !$198 #active_site Asp #status predicted SUMMARY #length 271 #molecular-weight 30979 #checksum 1131 SEQUENCE /// ENTRY PKECT5 #type complete TITLE kanamycin kinase (EC 2.7.1.95) II - Escherichia coli ALTERNATE_NAMES aminoglycoside 3'-phosphotransferase, type II; neomycin-kanamycin phosphotransferase, type II ORGANISM #formal_name Escherichia coli DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 24-Sep-1999 ACCESSIONS A00663; S48095 REFERENCE A00663 !$#authors Beck, E.; Ludwig, G.; Auerswald, E.A.; Reiss, B.; Schaller, !1H. !$#journal Gene (1982) 19:327-336 !$#title Nucleotide sequence and exact localization of the neomyclin !1phosphotransferse gene from transposon Tn 5. !$#cross-references MUID:83106478; PMID:6295884 !$#accession A00663 !'##molecule_type DNA !'##residues 1-264 ##label BEC !'##cross-references GB:U32991; NID:g1163175; PIDN:AAA85506.1; !1PID:g1000123 !'##note this enzyme is encoded by the kanamycin and neomycin resistance !1transposon Tn5 REFERENCE S48094 !$#authors Posfai, G.; Koob, M.; Hradecna, Z.; Hasan, N.; Filutowicz, !1M.; Szybalski, W. !$#journal Nucleic Acids Res. (1994) 22:2392-2398 !$#title In vivo excision and amplification of large segments of the !1Escherichia coli genome. !$#cross-references MUID:94310070; PMID:8036169 !$#accession S48095 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-264 ##label POS !'##cross-references EMBL:U08460; NID:g475708; PID:g475709 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1994 GENETICS !$#gene neo CLASSIFICATION #superfamily kanamycin kinase KEYWORDS antibiotic resistance; ATP; phosphotransferase FEATURE !$190 #active_site Asp #status predicted SUMMARY #length 264 #molecular-weight 29047 #checksum 4690 SEQUENCE /// ENTRY PKBSK #type complete TITLE kanamycin kinase (EC 2.7.1.95) - Bacillus circulans ALTERNATE_NAMES aminoglycoside 3'-phosphotransferase; neomycin/kanamycin phosphotransferase ORGANISM #formal_name Bacillus circulans DATE 18-Apr-1984 #sequence_revision 18-Apr-1984 #text_change 01-Dec-2000 ACCESSIONS A00664; S10675; T17886 REFERENCE A00664 !$#authors Herbert, C.J.; Giles, I.G.; Akhtar, M. !$#journal FEBS Lett. (1983) 160:67-71 !$#title The sequence of an antibiotic resistance gene from an !1antibiotic-producing bacterium. Homologies with transposon !1genes. !$#cross-references MUID:83287774; PMID:6193008 !$#accession A00664 !'##molecule_type DNA !'##residues 1-262 ##label HER !'##cross-references EMBL:X03364 REFERENCE S10675 !$#authors Sarwar, M.; Akhtar, M. !$#journal Biochem. J. (1990) 268:671-677 !$#title Cloning of aminoglycoside phosphotransferase (APH) gene from !1antibiotic- producing strain of Bacillus circulans into a !1high-expression vector, pKK223-3. Purification, properties !1and location of the enzyme. !$#cross-references MUID:90303260; PMID:2163618 !$#accession S10675 !'##molecule_type protein !'##residues 'X',2,'QX',5-7,'X',9-12 ##label SAR REFERENCE Z18808 !$#authors Aubert-Pivert, E.; Davies, J. !$#journal Gene (1994) 147:1-11 !$#title Biosynthesis of butirosin in Bacillus circulans NRRL B3312: !1identification by sequence analysis and insertional !1mutagenesis of the butB gene involved in antibiotic !1production. !$#cross-references MUID:94374689; PMID:7522196 !$#accession T17886 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-25 ##label AUB !'##cross-references EMBL:L20421; NID:g304142; PID:g688437; !1PIDN:AAA62589.1 GENETICS !$#gene aphA4; butA FUNCTION !$#pathway butirosin biosynthesis CLASSIFICATION #superfamily kanamycin kinase KEYWORDS antibiotic resistance; ATP; monomer; periplasmic space; !1phosphotransferase FEATURE !$187 #active_site Asp #status predicted SUMMARY #length 262 #molecular-weight 29899 #checksum 6174 SEQUENCE /// ENTRY PKSOJF #type complete TITLE kanamycin kinase (EC 2.7.1.95) - Enterococcus faecalis plasmid pJH1 ALTERNATE_NAMES aminoglycoside 3'-phosphotransferase; neomycin-kanamycin phosphotransferase ORGANISM #formal_name Enterococcus faecalis DATE 18-Apr-1984 #sequence_revision 18-Apr-1984 #text_change 24-Sep-1999 ACCESSIONS A00665 REFERENCE A00665 !$#authors Trieu-Cuot, P.; Courvalin, P. !$#journal Gene (1983) 23:331-341 !$#title Nucleotide sequence of the Streptococcus faecalis plasmid !1gene encoding the 3'5''-aminoglycoside phosphotransferase !1type III. !$#cross-references MUID:84029883; PMID:6313476 !$#accession A00665 !'##molecule_type DNA !'##residues 1-264 ##label TRI !'##cross-references GB:V01547; NID:g47033; PIDN:CAA24789.1; PID:g47034 GENETICS !$#genome plasmid CLASSIFICATION #superfamily kanamycin kinase KEYWORDS antibiotic resistance; ATP; phosphotransferase FEATURE !$190 #active_site Asp #status predicted SUMMARY #length 264 #molecular-weight 30974 #checksum 1180 SEQUENCE /// ENTRY PKSAF #type complete TITLE kanamycin kinase (EC 2.7.1.95) - Staphylococcus aureus ALTERNATE_NAMES aminoglycoside 3'-phosphotransferase; neomycin-kanamycin phosphotransferase ORGANISM #formal_name Staphylococcus aureus DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 13-Sep-1997 ACCESSIONS A26220; A00665 REFERENCE A93054 !$#authors Gray, G.S.; Fitch, W.M. !$#journal Mol. Biol. Evol. (1983) 1:57-66 !$#title Evolution of antibiotic resistance genes: the DNA sequence !1of a kanamycin resistance gene from Staphylococcus aureus. !$#cross-references MUID:88174299; PMID:6100986 !$#accession A26220 !'##molecule_type DNA !'##residues 1-263 ##label GRA CLASSIFICATION #superfamily kanamycin kinase KEYWORDS antibiotic resistance; ATP; phosphotransferase FEATURE !$189 #active_site Asp #status predicted SUMMARY #length 263 #molecular-weight 30875 #checksum 9663 SEQUENCE /// ENTRY PKSMR #type complete TITLE kanamycin kinase (EC 2.7.1.95) - Streptomyces fradiae ALTERNATE_NAMES aminoglycoside 3'-phosphotransferase; neomycin-kanamycin phosphotransferase ORGANISM #formal_name Streptomyces fradiae DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 11-Jun-1999 ACCESSIONS A00666; S28370 REFERENCE A00666 !$#authors Thompson, C.J.; Gray, G.S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:5190-5194 !$#title Nucleotide sequence of a streptomycete aminoglycoside !1phosphotransferase gene and its relationship to !1phosphotransferses encoded by resistance plasmids. !$#cross-references MUID:83299940; PMID:6310563 !$#accession A00666 !'##molecule_type DNA !'##residues 1-268 ##label THO !'##cross-references GB:K00432; NID:g153160; PIDN:AAA26699.1; !1PID:g153161 !'##experimental_source ATCC 10745 REFERENCE S28369 !$#authors Bibb, M.J.; Bibb, M.J.; Ward, J.M.; Cohen, S.N. !$#journal Mol. Gen. Genet. (1985) 199:26-36 !$#title Nucleotide sequences encoding and promoting expression of !1three antibiotic resistance genes indigenous to !1Streptomyces. !$#cross-references MUID:85213103; PMID:2987648 !$#accession S28370 !'##molecule_type DNA !'##residues 1-71 ##label BIB !'##cross-references EMBL:X02394; NID:g47022; PIDN:CAA26236.1; !1PID:g47023 GENETICS !$#gene aph CLASSIFICATION #superfamily kanamycin kinase KEYWORDS antibiotic resistance; ATP; phosphotransferase FEATURE !$188 #active_site Asp #status predicted SUMMARY #length 268 #molecular-weight 29986 #checksum 4592 SEQUENCE /// ENTRY PKSMK #type complete TITLE kanamycin kinase (EC 2.7.1.95) - Streptomyces sp. ALTERNATE_NAMES aminoglycoside 3'-phosphotransferase; neomycin-kanamycin phosphotransferase ORGANISM #formal_name Streptomyces sp. DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 11-Jun-1999 ACCESSIONS JT0330 REFERENCE JT0330 !$#authors Hoshiko, S.; Nojiri, C.; Matsunaga, K.; Katsumata, K.; !1Satoh, E.; Nagaoka, K. !$#journal Gene (1988) 68:285-296 !$#title Nucleotide sequence of the ribostamycin phosphotransferase !1gene and of its control region in Streptomyces !1ribosidificus. !$#cross-references MUID:89121511; PMID:2851496 !$#accession JT0330 !'##molecule_type DNA !'##residues 1-263 ##label HOS !'##cross-references GB:M22126; NID:g153434; PIDN:AAC32025.1; !1PID:g153435 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing GENETICS !$#gene rph CLASSIFICATION #superfamily kanamycin kinase KEYWORDS antibiotic resistance; ATP; phosphotransferase FEATURE !$110-121 #region substrate binding #status predicted\ !$179-190 #region ATP binding #status predicted\ !$183 #active_site Asp #status predicted SUMMARY #length 263 #molecular-weight 29575 #checksum 6557 SEQUENCE /// ENTRY A53239 #type complete TITLE aminoglycoside-O-phosphoryl-transferase (EC 2.7.1.-) type Vc - Micromonospora chalcea ALTERNATE_NAMES APH(3')-Vc ORGANISM #formal_name Micromonospora chalcea DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A53239 REFERENCE A53239 !$#authors Salauze, D.; Davies, J. !$#journal J. Antibiot. (1991) 44:1432-1443 !$#title Isolation and characterisation of an aminoglycoside !1phosphotransferase from neomycin-producing Micromonospora !1chalcea; comparison with that of Streptomyces fradiae and !1other producers of 4,6-disubstituted 2-deoxystreptamine !1antibiotics. !$#cross-references MUID:92138369; PMID:1663923 !$#accession A53239 !'##status preliminary !'##molecule_type DNA !'##residues 1-264 ##label SAL !'##cross-references GB:S81599; NID:g244648; PIDN:AAB21326.1; !1PID:g244649 !'##experimental_source 69-683 !'##note sequence extracted from NCBI backbone (NCBIN:81599, !1NCBIP:81602) CLASSIFICATION #superfamily kanamycin kinase KEYWORDS ATP; phosphotransferase SUMMARY #length 264 #molecular-weight 29827 #checksum 1188 SEQUENCE /// ENTRY JH0123 #type complete TITLE streptomycin phosphotransferase (EC 2.7.1.-) - Escherichia coli plasmid RSF1010 ORGANISM #formal_name Escherichia coli DATE 31-Dec-1991 #sequence_revision 16-Aug-1996 #text_change 11-Jun-1999 ACCESSIONS JH0123; PS0287 REFERENCE JH0123 !$#authors Scholz, P.; Haring, V.; Wittmann-Liebold, B.; Ashman, K.; !1Bagdasarian, M.; Scherzinger, E. !$#journal Gene (1989) 75:271-288 !$#title Complete nucleotide sequence and gene organization of the !1broad-host-range plasmid RSF1010. !$#cross-references MUID:89232758; PMID:2653965 !$#accession JH0123 !'##molecule_type DNA !'##residues 1-267 ##label SCH1 !'##cross-references GB:M28829; NID:g152577; PIDN:AAA26442.1; !1PID:g551976 !$#accession PS0287 !'##molecule_type protein !'##residues 1-10 ##label SCH2 GENETICS !$#gene strA !$#genome plasmid !$#start_codon TTG !$#note the plasmid RSF1010 is a naturally occurring !1broad-host-range plasmid belonging to the E. coli !1incompatibility group Q and encoding resistance to !1streptomycin and sulfonamides !$#note the gene name strA is not to be confused with the E. coli !1genomic strA gene, which codes for ribosomal protein S12 !1(see R3EC12) CLASSIFICATION #superfamily kanamycin kinase KEYWORDS ATP; phosphotransferase FEATURE !$184 #active_site Asp #status predicted SUMMARY #length 267 #molecular-weight 29595 #checksum 6042 SEQUENCE /// ENTRY WGSMHH #type complete TITLE hygromycin B phosphotransferase (EC 2.7.1.-) - Streptomyces hygroscopicus ORGANISM #formal_name Streptomyces hygroscopicus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 24-Sep-1999 ACCESSIONS A23507 REFERENCE A23507 !$#authors Zalacain, M.; Gonzalez, A.; Guerrero, M.C.; Mattaliano, !1R.J.; Malpartida, F.; Jimenez, A. !$#journal Nucleic Acids Res. (1986) 14:1565-1581 !$#title Nucleotide sequence of the hygromycin B phosphotransferase !1gene from Streptomyces hygroscopicus. !$#cross-references MUID:86148493; PMID:3005976 !$#accession A23507 !'##molecule_type DNA !'##residues 1-332 ##label ZAL !'##cross-references GB:X03615; NID:g47133; PIDN:CAA27276.1; PID:g581682 COMMENT This phosphotransferase modifies hygromycin B, an !1aminoglycoside antibiotic produced only by Streptomyces !1hydroscopicus. GENETICS !$#gene hyg !$#start_codon GTG CLASSIFICATION #superfamily Streptomyces hygromycin B phosphotransferase KEYWORDS antibiotic resistance; phosphotransferase SUMMARY #length 332 #molecular-weight 37053 #checksum 6213 SEQUENCE /// ENTRY WGECH #type complete TITLE hygromycin-B kinase (EC 2.7.1.119) - Escherichia coli plasmids ORGANISM #formal_name Escherichia coli DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 11-Jun-1999 ACCESSIONS A00668; A04603 REFERENCE A00668 !$#authors Kaster, K.R.; Burgett, S.G.; Rao, R.N.; Ingolia, T.D. !$#journal Nucleic Acids Res. (1983) 11:6895-6911 !$#title Analysis of a bacterial hygromycin B resistance gene by !1transcriptional and translational fusions and by DNA !1sequencing. !$#cross-references MUID:84041492; PMID:6314265 !$#accession A00668 !'##molecule_type DNA !'##residues 1-341 ##label KAS !'##cross-references GB:V01499; NID:g40922; PIDN:CAA24743.1; PID:g40923 !'##note sequence encoded by Plasmid pKC222, which is derived from !1naturally occurring plasmid pKC203 REFERENCE A04603 !$#authors Gritz, L.; Davies, J. !$#journal Gene (1983) 25:179-188 !$#title Plasmid-encoded hygromycin B resistance: the sequence of !1hygromycin B phosphotransferase gene and its expression in !1Escherichia coli and Saccharomyces cerevisiae. !$#cross-references MUID:84109554; PMID:6319235 !$#accession A04603 !'##molecule_type DNA !'##residues 1-341 ##label GRI !'##cross-references GB:K01193; NID:g150775; PIDN:AAA92252.1; !1PID:g150776 !'##note sequence encoded by Plasmid pJR225 COMMENT This phosphotransferase modifies hygromycin B, an !1aminoglycoside antibiotic produced by Streptomyces !1hygroscopicus. GENETICS !$#gene hph !$#genome plasmid CLASSIFICATION #superfamily hygromycin B phosphotransferase KEYWORDS antibiotic resistance; phosphotransferase SUMMARY #length 341 #molecular-weight 38032 #checksum 2442 SEQUENCE /// ENTRY KIRTFB #type complete TITLE 6-phosphofructo-2-kinase (EC 2.7.1.105) / fructose-2, 6-bisphosphate 2-phosphatase (EC 3.1.3.46), hepatic - rat ALTERNATE_NAMES 6-phosphofructo-2-kinase / fructose-2,6-bisphosphatase, hepatic CONTAINS 6-phosphofructo-2-kinase (EC 2.7.1.105); fructose-2, 6-bisphosphate 2-phosphatase (EC 3.1.3.46) ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 19-Jan-2001 ACCESSIONS S11761; S00188; A30441; A26644; A30442; A28520; A21957; !1B33503; S06790; A31954; A43639; S38827; S55998; S65353; !1A27374 REFERENCE S05203 !$#authors Crepin, K.M.; Darville, M.I.; Hue, L.; Rousseau, G.G. !$#journal Eur. J. Biochem. (1989) 183:433-440 !$#title Characterization of distinct mRNAs coding for putative !1isozymes of 6-phosphofructo-2-kinase/fructose-2, !16-bisphosphatase. !$#cross-references MUID:89338416; PMID:2547611 !$#accession S11761 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-471 ##label CRE !'##cross-references EMBL:X15580; NID:g56923; PIDN:CAA33607.1; !1PID:g1200133 REFERENCE S00188 !$#authors Darville, M.I.; Crepin, K.M.; Vandekerckhove, J.; van Damme, !1J.; Octave, J.N.; Rider, M.H.; Marchand, M.J.; Hue, L.; !1Rousseau, G.G. !$#journal FEBS Lett. (1987) 224:317-321 !$#title Complete nucleotide sequence coding for rat liver !16-phosphofructo-2-kinase/fructose-2,6-bisphosphatase derived !1from a cDNA clone. !$#cross-references MUID:88083556; PMID:2856848 !$#accession S00188 !'##molecule_type mRNA !'##residues 1-471 ##label DAR !'##cross-references EMBL:Y00702; NID:g56884; PIDN:CAA68694.1; !1PID:g56885 !$#accession A30441 !'##molecule_type protein !'##residues !116-29;65-74;90-105;123-137;189-195;240-252;259-266;309-324; !1459-471 ##label DAR2 REFERENCE A26644 !$#authors Colosia, A.D.; Lively, M.; El-Maghrabi, M.R.; Pilkis, S.J. !$#journal Biochem. Biophys. Res. Commun. (1987) 143:1092-1098 !$#title Isolation of a cDNA clone for rat liver 6-phosphofructo !12-kinase/fructose 2,6-bisphosphatase. !$#cross-references MUID:87184586; PMID:3032183 !$#accession A26644 !'##molecule_type mRNA !'##residues 168-471 ##label COL !'##cross-references GB:M15685; NID:g202555; PIDN:AAA40624.1; !1PID:g202556 !$#accession A30442 !'##molecule_type protein !'##residues 2-134,'Y',136-137,'F',139-471 ##label COL2 REFERENCE A28520 !$#authors Lively, M.O.; El-Maghrabi, M.R.; Pilkis, J.; D'Angelo, G.; !1Colosia, A.D.; Ciavola, J.A.; Fraser, B.A.; Pilkis, S.J. !$#journal J. Biol. Chem. (1988) 263:839-849 !$#title Complete amino acid sequence of rat liver !16-phosphofructo-2-kinase/fructose-2,6-bisphosphatase. !$#cross-references MUID:88087209; PMID:2826464 !$#accession A28520 !'##molecule_type protein !'##residues 2-134,'Y',136-471 ##label LIV REFERENCE A21957 !$#authors Murray, K.J.; El-Maghrabi, M.R.; Kountz, P.D.; Lukas, T.J.; !1Soderling, T.R.; Pilkis, S.J. !$#journal J. Biol. Chem. (1984) 259:7673-7681 !$#title Amino acid sequence of the phosphorylation site of rat liver !16-phosphofructo-2-kinase/fructose-2,6-bisphosphatase. !$#cross-references MUID:84239705; PMID:6330071 !$#accession A21957 !'##status preliminary !'##molecule_type protein !'##residues 26-37 ##label MUR REFERENCE A33503 !$#authors Kitamura, K.; Uyeda, K.; Kangawa, K.; Matsuo, H. !$#journal J. Biol. Chem. (1989) 264:9799-9806 !$#title Purification and characterization of rat skeletal muscle !1fructose-6-phosphate,2-kinase:fructose-2,6-bisphosphatase. !$#cross-references MUID:89255547; PMID:2542332 !$#accession B33503 !'##status preliminary !'##molecule_type protein !'##residues 16-29,32-49 ##label KIT REFERENCE S06790 !$#authors Crepin, K.M.; Darville, M.I.; Michel, A.; Hue, L.; Rousseau, !1G.G. !$#journal Biochem. J. (1989) 264:151-160 !$#title Cloning and expression in Escherichia coli of a rat hepatoma !1cell cDNA coding for 6-phosphofructo-2-kinase/fructose-2, !16-bisphosphatase. !$#cross-references MUID:90104268; PMID:2557826 !$#accession S06790 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 5,'E',7,'KASK',12,'TA',34-471 ##label CR2 REFERENCE A31954 !$#authors Colosia, A.D.; Marker, A.J.; Lange, A.J.; El-Maghrabi, M.R.; !1Granner, D.K.; Tauler, A.; Pilkis, J.; Pilkis, S.J. !$#journal J. Biol. Chem. (1988) 263:18669-18677 !$#title Induction of rat liver 6-phosphofructo-2-kinase/fructose-2, !16-bisphosphatase mRNA by refeeding and insulin. !$#cross-references MUID:89066654; PMID:2848802 !$#accession A31954 !'##molecule_type mRNA !'##residues 1-134,'Y',136-471 ##label CO2 !'##cross-references GB:J04197; NID:g202557; PIDN:AAA79008.1; !1PID:g202558 REFERENCE A43639 !$#authors Lange, A.J.; Kummel, L.; El-Maghrabi, M.R.; Tauler, A.; !1Colosia, A.; Marker, A.; Pilkis, S.J. !$#journal Biochem. Biophys. Res. Commun. (1989) 162:753-760 !$#title Sequence of the 5'-flanking region of the rat !16-phosphofructo-2-kinase/fructose 2,6-bisphosphatase gene: !1regulation by glucocorticoids. !$#cross-references MUID:89334886; PMID:2547373 !$#accession A43639 !'##status preliminary !'##molecule_type DNA !'##residues 1-33 ##label LAN !'##cross-references GB:M27886 REFERENCE A33722 !$#authors Darville, M.I.; Crepin, K.M.; Hue, L.; Rousseau, G.G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:6543-6547 !$#title 5' flanking sequence and structure of a gene encoding rat !16-phosphofructo-2-kinase/fructose-2,6-bisphosphatase. !$#cross-references MUID:89367285; PMID:2549541 !$#accession S38827 !'##status preliminary; translation not shown !'##molecule_type DNA !'##residues 1-32 ##label DA2 !'##cross-references EMBL:M26216; NID:g206096; PIDN:AAA02889.1; !1PID:g404588 REFERENCE S55998 !$#authors Rosa, J.L.; Perez, J.X.; Ventura, F.; Tauler, A.; Gil, J.; !1Shimoyama, M.; Pilkis, S.J.; Bartrons, R. !$#journal Biochem. J. (1995) 309:119-125 !$#title Role of the N-terminal region in covalent modification of !16-phosphofructo-2-kinase/fructose-2,6-bisphosphatase: !1comparison of phosphorylation and ADP-ribosylation. !$#cross-references MUID:95344356; PMID:7619045 !$#accession S55998 !'##status preliminary !'##molecule_type protein !'##residues 26-37 ##label ROS REFERENCE A58020 !$#authors Vertommen, D.; Bertrand, L.; Sontag, B.; Di Pietro, A.; !1Louckx, M.P.; Vidal, H.; Hue, L.; Rider, M.H. !$#journal J. Biol. Chem. (1996) 271:17875-17880 !$#title The ATP-binding site in the 2-kinase domain of liver !16-phosphofructo-2-kinase/fructose-2,6-bisphosphatase. Study !1of the role of Lys-54 and Thr-55 by site-directed !1mutagenesis. !$#cross-references MUID:96279327; PMID:8663445 !$#contents annotation REFERENCE S65353 !$#authors Rider, M.H.; Puype, M.; van Damme, J.; Gevaert, K.; de !1Boeck, S.; D'Alayer, J.; Rasmussen, H.H.; Celis, J.E.; !1Vandekerckhove, J. !$#journal Eur. J. Biochem. (1995) 230:258-265 !$#title An agarose-based gel-concentration system for microsequence !1and mass spectrometric characterization of proteins !1previously purified in polyacrylamide gels starting at low !1picomole levels. !$#cross-references MUID:95324533; PMID:7601109 !$#accession S65353 !'##molecule_type protein !'##residues !14-12;15-29;32-53;55-61;66-74;75-82;90-105;123-137;154-172; !1232-239;259-267;269-279;282-292;294-300;309-324;358-361; !1365-374;375-384;408-416;449-458;459-471 ##label RID REFERENCE A27374 !$#authors Pilkis, S.J.; Lively, M.O.; El-Maghrabi, M.R. !$#journal J. Biol. Chem. (1987) 262:12672-12675 !$#title Active site sequence of hepatic fructose-2,6-bisphosphatase. !1Homology in primary structure with phosphoglycerate mutase. !$#cross-references MUID:87308301; PMID:3040762 !$#accession A27374 !'##molecule_type protein !'##residues 254-267 ##label PIL GENETICS !$#introns 106/2 COMPLEX homodimer CLASSIFICATION #superfamily 6-phosphofructo-2-kinase / fructose-2, !16-bisphosphate 2-phosphatase; phosphoglycerate mutase !1homology KEYWORDS acetylated amino end; alternative splicing; ATP; homodimer; !1liver; multifunctional enzyme; nucleotide binding; P-loop; !1phosphohistidine; phosphoprotein; phosphoric monoester !1hydrolase; phosphotransferase FEATURE !$2-471 #product 6-phosphofructo-2-kinase / fructose-2, !86-bisphosphate 2-phosphatase #status experimental !8#label MAT\ !$49-56 #region nucleotide-binding motif A (P-loop)\ !$254-426 #domain phosphoglycerate mutase homology #label PGMH\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental\ !$33 #binding_site phosphate (Ser) (covalent) (by !8cAMP-dependent kinase) #status experimental\ !$55 #binding_site ATP (Lys) #status experimental\ !$259 #active_site His (phosphohistidine intermediate) !8#status experimental SUMMARY #length 471 #molecular-weight 54763 #checksum 363 SEQUENCE /// ENTRY S12732 #type complete TITLE 6-phosphofructo-2-kinase (EC 2.7.1.105) / fructose-2, 6-bisphosphate 2-phosphatase (EC 3.1.3.46), hepatic - human ALTERNATE_NAMES fructose-2,6-bisphosphatase, hepatic CONTAINS 6-phosphofructo-2-kinase (EC 2.7.1.105); fructose-2, 6-bisphosphate 2-phosphatase (EC 3.1.3.46) ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S12732; A27654 REFERENCE S12732 !$#authors Lange, A.J.; Pilkis, S.J. !$#journal Nucleic Acids Res. (1990) 18:3652 !$#title Sequence of human liver 6-phosphofructo-2-kinase/fructose-2, !16-bisphosphatase. !$#cross-references MUID:90301497; PMID:2163524 !$#accession S12732 !'##molecule_type mRNA !'##residues 1-471 ##label LAN !'##cross-references EMBL:X52638; NID:g35502; PIDN:CAA36861.1; !1PID:g35503 REFERENCE A27654 !$#authors Algaier, J.; Uyeda, K. !$#journal Biochem. Biophys. Res. Commun. (1988) 153:328-333 !$#title Molecular cloning, sequence analysis, and expression of a !1human liver cDNA coding for fructose-6-P,2-kinase: !1fructose-2,6-bisphosphatase. !$#cross-references MUID:88240421; PMID:2837207 !$#accession A27654 !'##molecule_type mRNA !'##residues 94-304,'H',306-358,'H',360-396,'HA',399-471 ##label ALG !'##cross-references GB:M19938; NID:g182312; PIDN:AAA35818.1; !1PID:g182313 !'##note the authors translated the codon TAC for residue 253 as Thr COMMENT This sequence, the C-terminal of the bifunctional enzyme !1fructose-6-phosphate,2-kinase/fructose-2,6-bisphosphatase, !1specifically codes for the fructose-2,6-bisphosphatase. The !1active sites of the kinase and phosphatase are distinctly in !1two separate domains. GENETICS !$#gene GDB:PFKFB1; PFRX !'##cross-references GDB:125375; OMIM:311790 !$#map_position Xp11.21-Xp11.21 CLASSIFICATION #superfamily 6-phosphofructo-2-kinase / fructose-2, !16-bisphosphate 2-phosphatase; phosphoglycerate mutase !1homology KEYWORDS ATP; liver; multifunctional enzyme; nucleotide binding; !1P-loop; phosphohistidine; phosphoprotein; phosphoric !1monoester hydrolase; phosphotransferase FEATURE !$49-56 #region nucleotide-binding motif A (P-loop)\ !$254-426 #domain phosphoglycerate mutase homology #label PGMH\ !$55 #binding_site ATP (Lys) #status predicted\ !$259 #active_site His (phosphohistidine intermediate) !8#status predicted SUMMARY #length 471 #molecular-weight 54700 #checksum 865 SEQUENCE /// ENTRY A44872 #type complete TITLE 6-phosphofructo-2-kinase (EC 2.7.1.105) / fructose-2, 6-bisphosphate 2-phosphatase (EC 3.1.3.46), hepatic isoform - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS A44872 REFERENCE A44872 !$#authors Lange, A.J.; el-Maghrabi, M.R.; Pilkis, S.J. !$#journal Arch. Biochem. Biophys. (1991) 290:258-263 !$#title Isolation of bovine liver 6-phosphofructo-2-kinase/ !1fructose-2,6-bisphosphatase cDNA: bovine liver and heart !1forms of the enzyme are separate gene products. !$#cross-references MUID:91378600; PMID:1654864 !$#accession A44872 !'##status preliminary !'##molecule_type mRNA !'##residues 1-471 ##label LAN !'##cross-references GB:S55569; NID:g235762; PIDN:AAB19845.1; !1PID:g235763 !'##experimental_source liver !'##note sequence extracted from NCBI backbone (NCBIN:55569, !1NCBIP:55570) !'##note the sequence from Fig. 3 is inconsistent with that from Fig. 2 !1in having 85-Asp, 89-Arg, 419-Pro, and 420-Ser CLASSIFICATION #superfamily 6-phosphofructo-2-kinase / fructose-2, !16-bisphosphate 2-phosphatase; phosphoglycerate mutase !1homology KEYWORDS ATP; liver; multifunctional enzyme; nucleotide binding; !1P-loop; phosphohistidine; phosphoprotein; phosphoric !1monoester hydrolase; phosphotransferase FEATURE !$49-56 #region nucleotide-binding motif A (P-loop)\ !$254-426 #domain phosphoglycerate mutase homology #label PGMH\ !$55 #binding_site ATP (Lys) #status predicted\ !$259 #active_site His (phosphohistidine intermediate) !8#status predicted SUMMARY #length 471 #molecular-weight 54657 #checksum 9190 SEQUENCE /// ENTRY JC1470 #type complete TITLE 6-phosphofructo-2-kinase (EC 2.7.1.105) / fructose-2, 6-bisphosphate 2-phosphatase (EC 3.1.3.46) - chicken CONTAINS 6-phosphofructo-2-kinase (EC 2.7.1.105); fructose-2, 6-bisphosphate 2-phosphatase (EC 3.1.3.46) ORGANISM #formal_name Gallus gallus #common_name chicken DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS JC1470 REFERENCE JC1470 !$#authors Li, L.; Lange, A.J.; Pilkis, S.J. !$#journal Biochem. Biophys. Res. Commun. (1993) 190:397-405 !$#title Isolation of a cDNA for chicken liver !16-phosphofructo-2-kinase/fructose-2,6-bisphosphatase. !$#cross-references MUID:93151820; PMID:7916593 !$#accession JC1470 !'##molecule_type mRNA !'##residues 1-469 ##label LIL !'##cross-references GB:S54076; NID:g298235; PIDN:AAB25213.1; !1PID:g298236 !'##experimental_source liver COMMENT This bifunctional enzyme catalyzes both the synthesis and !1degradation of fructose-2,6-bisphosphate. CLASSIFICATION #superfamily 6-phosphofructo-2-kinase / fructose-2, !16-bisphosphate 2-phosphatase; phosphoglycerate mutase !1homology KEYWORDS ATP; multifunctional enzyme; nucleotide binding; P-loop; !1phosphohistidine; phosphoprotein; phosphoric monoester !1hydrolase; phosphotransferase FEATURE !$47-54 #region nucleotide-binding motif A (P-loop)\ !$253-424 #domain phosphoglycerate mutase homology #label PGMH\ !$53 #binding_site ATP (Lys) #status predicted\ !$258 #active_site His (phosphohistidine intermediate) !8#status predicted SUMMARY #length 469 #molecular-weight 54255 #checksum 8643 SEQUENCE /// ENTRY A35350 #type complete TITLE protein kinase C inhibitor - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Aug-1990 #sequence_revision 31-Aug-1990 #text_change 11-Sep-1998 ACCESSIONS A35350 REFERENCE A35350 !$#authors Pearson, J.D.; DeWald, D.B.; Mathews, W.R.; Mozier, N.M.; !1Zuercher-Neely, H.A.; Heinrikson, R.L.; Morris, M.A.; !1McCubbin, W.D.; McDonald, J.R.; Fraser, E.D.; Vogel, H.J.; !1Kay, C.M.; Walsh, M.P. !$#journal J. Biol. Chem. (1990) 265:4583-4591 !$#title Amino acid sequence and characterization of a protein !1inhibitor of protein kinase C. !$#cross-references MUID:90170969; PMID:2307677 !$#accession A35350 !'##molecule_type protein !'##residues 1-125 ##label PEA COMMENT This protein was shown experimentally to bind Zn(2+). This !1binding was not affected by a 10-fold molar excess of Ca(2+) !1or Mg(2+). CLASSIFICATION #superfamily protein kinase C inhibitor; histidine triad !1homology KEYWORDS acetylated amino end; homodimer; protein kinase inhibitor; !1zinc FEATURE !$16-116 #domain histidine triad homology #label HIT\ !$109-113 #region histidine triad motif\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental SUMMARY #length 125 #molecular-weight 13648 #checksum 4966 SEQUENCE /// ENTRY A58802 #type complete TITLE probable tumor suppressor FHIT - human ALTERNATE_NAMES 5',5'''-P1,P4-tetraphosphate asymmetrical hydrolase homolog; fragile histidine triad protein ORGANISM #formal_name Homo sapiens #common_name man DATE 24-Apr-1998 #sequence_revision 24-Apr-1998 #text_change 11-Jun-1999 ACCESSIONS A58802 REFERENCE A58802 !$#authors Ohta, M.; Hiroshi, I.; Cotticelli, M.G.; Kastury, K.; Baffa, !1R.; Palazzo, J.; Siprashvili, Z.; Mori, M.; McCue, P.; !1Druck, T.; Croce, C.M.; Huebner, K. !$#journal Cell (1996) 84:587-597 !$#title The FHIT gene, spanning the chromosome 3p14.2 fragile site !1and renal carcinoma-associated t(3;8) breakpoint, is !1abnormal in digestive tract cancers. !$#cross-references MUID:96178471; PMID:8598045 !$#accession A58802 !'##molecule_type mRNA !'##residues 1-147 ##label OHT !'##cross-references GB:U46922; NID:g1203835; PIDN:AAA99013.1; !1PID:g1203836 GENETICS !$#gene GDB:FHIT !'##cross-references GDB:4250809; OMIM:601153 !$#map_position 3p14.2-3p14.2 CLASSIFICATION #superfamily histidine triad protein FHIT; histidine triad !1homology KEYWORDS tumor suppressor FEATURE !$3-101 #domain histidine triad homology #label HIT\ !$94-98 #region histidine triad motif SUMMARY #length 147 #molecular-weight 16858 #checksum 4597 SEQUENCE /// ENTRY S64700 #type complete TITLE bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) (EC 3.6.1.17) - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES diadenosine 5',5'''-P1,P4-tetraphosphate asymmetrical hydrolase ORGANISM #formal_name Schizosaccharomyces pombe DATE 28-Oct-1996 #sequence_revision 13-Mar-1997 #text_change 11-Jan-2000 ACCESSIONS S64700; T41374 REFERENCE S64700 !$#authors Huang, Y.; Garrison, P.N.; Barnes, L.D. !$#journal Biochem. J. (1995) 312:925-932 !$#title Cloning of the Schizosaccharomyces pombe gene encoding !1diadenosine 5',5'''-P(1),P(4)-tetraphosphate (Ap(4)A) !1asymmetrical hydrolase: sequence similarity with the !1histidine triad (HIT) protein family. !$#cross-references MUID:96128081; PMID:8554540 !$#accession S64700 !'##status preliminary !'##molecule_type DNA !'##residues 1-182 ##label HUA !'##cross-references EMBL:U32615; NID:g965074; PIDN:AAC49143.1; !1PID:g965075 REFERENCE Z21918 !$#authors Wood, V.; Rajandream, M.A.; Barrell, B.G.; Hilbert, H.; !1Duesterhoeft, A. !$#submission submitted to the EMBL Data Library, March 1998 !$#accession T41374 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-182 ##label WOO !'##cross-references EMBL:Z97052; PIDN:CAB09779.1; GSPDB:GN00068; !1SPDB:SPCC4G3.02 !'##experimental_source strain 972h-; cosmid c4G3 GENETICS !$#gene aph1; SPCC4G3.02 !$#map_position 3 !$#introns 21/3; 55/3; 84/3 CLASSIFICATION #superfamily histidine triad protein FHIT; histidine triad !1homology KEYWORDS hydrolase FEATURE !$5-102 #domain histidine triad homology #label HIT\ !$95-99 #region histidine triad motif SUMMARY #length 182 #molecular-weight 20685 #checksum 3823 SEQUENCE /// ENTRY S61191 #type complete TITLE asymmetrical hydrolase homolog YDR305c - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein D9740.15 ORGANISM #formal_name Saccharomyces cerevisiae DATE 23-Feb-1996 #sequence_revision 01-Mar-1996 #text_change 23-Mar-2001 ACCESSIONS S61191 REFERENCE S61160 !$#authors Ding, H. !$#submission submitted to the EMBL Data Library, June 1995 !$#description The sequence of S. cerevisiae cosmid 9740. !$#accession S61191 !'##molecule_type DNA !'##residues 1-217 ##label DIN !'##cross-references EMBL:U28374; NID:g849207; PIDN:AAB64741.1; !1PID:g849222; GSPDB:GN00004; MIPS:YDR305c GENETICS !$#gene SGD:HNT2; MIPS:YDR305c !'##cross-references SGD:S0002713; MIPS:YDR305c !$#map_position 4R !$#introns 29/3 CLASSIFICATION #superfamily histidine triad protein FHIT; histidine triad !1homology FEATURE !$16-114 #domain histidine triad homology #label HIT\ !$107-111 #region histidine triad motif SUMMARY #length 217 #molecular-weight 24784 #checksum 5593 SEQUENCE /// ENTRY S09156 #type complete TITLE diacylglycerol kinase (EC 2.7.1.107) alpha - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S09156; A33237 REFERENCE S09156 !$#authors Sakane, F.; Yamada, K.; Kanoh, H.; Yokoyama, C.; Tanabe, T. !$#journal Nature (1990) 344:345-348 !$#title Porcine diacylglycerol kinase sequence has zinc finger and !1E-F hand motifs. !$#cross-references MUID:90190867; PMID:2156169 !$#accession S09156 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-734 ##label SAK !'##cross-references GB:X53256; NID:g1938; PIDN:CAA37347.1; PID:g1939 !$#accession A33237 !'##molecule_type protein !'##residues 4-17;120-132;165-174;249-258;411-430;447-460 ##label SAK2 CLASSIFICATION #superfamily human diacylglycerol kinase; calmodulin repeat !1homology; protein kinase C zinc-binding repeat homology KEYWORDS ATP; calcium binding; duplication; EF hand; !1phosphotransferase; zinc FEATURE !$109-141 #domain calmodulin repeat homology #label EF1\ !$154-186 #domain calmodulin repeat homology #label EF2\ !$205-252 #domain protein kinase C zinc-binding repeat homology !8#label KZ1\ !$269-318 #domain protein kinase C zinc-binding repeat homology !8#label KZ2 SUMMARY #length 734 #molecular-weight 82605 #checksum 7932 SEQUENCE /// ENTRY I59282 #type complete TITLE diacylglycerol kinase (EC 2.7.1.107) gamma - rat ORGANISM #formal_name Rattus sp. #common_name rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS I59282 REFERENCE I59282 !$#authors Goto, K.; Funayama, M.; Kondo, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1994) 91:13042-13046 !$#title Cloning and expression of a cytoskeleton-associated !1diacylglycerol kinase that is dominantly expressed in !1cerebellum. !$#cross-references MUID:95108095; PMID:7809169 !$#accession I59282 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-788 ##label RES !'##cross-references GB:D38448; NID:g643598; PIDN:BAA07480.1; !1PID:g784935 CLASSIFICATION #superfamily human diacylglycerol kinase; calmodulin repeat !1homology; protein kinase C zinc-binding repeat homology KEYWORDS ATP; calcium binding; duplication; EF hand; !1phosphotransferase; zinc FEATURE !$172-204 #domain calmodulin repeat homology #label EF1\ !$217-249 #domain calmodulin repeat homology #label EF2\ !$269-318 #domain protein kinase C zinc-binding repeat homology !8#label KZ1\ !$334-380 #domain protein kinase C zinc-binding repeat homology !8#label KZ2 SUMMARY #length 788 #molecular-weight 88521 #checksum 7683 SEQUENCE /// ENTRY S28273 #type complete TITLE diacylglycerol kinase (EC 2.7.1.107) - Caenorhabditis elegans ALTERNATE_NAMES hypothetical protein F54G8.2 ORGANISM #formal_name Caenorhabditis elegans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S28273 REFERENCE S28273 !$#authors Sulston, J. !$#submission submitted to the EMBL Data Library, December 1992 !$#accession S28273 !'##molecule_type DNA !'##residues 1-827 ##label SUL !'##cross-references EMBL:Z19155; NID:g6712; PID:g6713 GENETICS !$#introns 17/1; 44/3; 59/3; 153/1; 192/1; 233/3; 273/3; 314/1; 341/1; !1377/3; 602/3; 654/3; 723/3; 755/2 CLASSIFICATION #superfamily human diacylglycerol kinase; calmodulin repeat !1homology; protein kinase C zinc-binding repeat homology KEYWORDS ATP; calcium binding; duplication; EF hand; !1phosphotransferase; zinc FEATURE !$185-217 #domain calmodulin repeat homology #label EF1\ !$230-262 #domain calmodulin repeat homology #label EF2\ !$281-331 #domain protein kinase C zinc-binding repeat homology !8#label KZ1\ !$345-390 #domain protein kinase C zinc-binding repeat homology !8#label KZ2 SUMMARY #length 827 #molecular-weight 93296 #checksum 4587 SEQUENCE /// ENTRY A42924 #type complete TITLE [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] kinase (EC 2.7.1.115) - rat ALTERNATE_NAMES branched-chain alpha-keto acid dehydrogenase kinase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A42924 REFERENCE A42924 !$#authors Popov, K.M.; Zhao, Y.; Shimomura, Y.; Kuntz, M.J.; Harris, !1R.A. !$#journal J. Biol. Chem. (1992) 267:13127-13130 !$#title Branched-chain alpha-ketoacid dehydrogenase kinase. !1Molecular cloning, expression, and sequence similarity with !1histidine protein kinases. !$#cross-references MUID:92317014; PMID:1377677 !$#accession A42924 !'##status preliminary !'##molecule_type mRNA !'##residues 1-412 ##label POP !'##cross-references GB:M93271; NID:g203152; PIDN:AAA40818.1; !1PID:g203153 !'##experimental_source heart !'##note sequence extracted from NCBI backbone (NCBIN:107740, !1NCBIP:107741) CLASSIFICATION #superfamily branched-chain alpha-keto acid dehydrogenase !1kinase KEYWORDS mitochondrion; oxidoreductase; phosphotransferase SUMMARY #length 412 #molecular-weight 46390 #checksum 3154 SEQUENCE /// ENTRY A55305 #type complete TITLE [pyruvate dehydrogenase (lipoamide)] kinase (EC 2.7.1.99) 2 precursor [validated] - rat ALTERNATE_NAMES pyruvate dehydrogenase kinase activator protein; [pyruvate dehydrogenase (lipoamide)] kinase p45 chain ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 18-Aug-2000 #sequence_revision 18-Aug-2000 #text_change 18-Aug-2000 ACCESSIONS A55305; S29190 REFERENCE A55305 !$#authors Popov, K.M.; Kedishvili, N.Y.; Zhao, Y.; Gudi, R.; Harris, !1R.A. !$#journal J. Biol. Chem. (1994) 269:29720-29724 !$#title Molecular cloning of the p45 subunit of pyruvate !1dehydrogenase kinase. !$#cross-references MUID:95050824; PMID:7961963 !$#accession A55305 !'##status not compared with conceptual translation !'##molecule_type mRNA; protein !'##residues 1-407 ##label POP !'##cross-references GB:U10357; NID:g694002; PIDN:AAB54084.1; !1PID:g694003 !'##note parts of this sequence, including the amino end of the mature !1protein, were confirmed by peptide sequencing REFERENCE S29190 !$#authors Priestman, D.A.; Mistry, S.C.; Kerbey, A.L.; Randle, P.J. !$#journal FEBS Lett. (1992) 308:83-86 !$#title Purification and partial characterization of rat liver !1pyruvate dehydrogenase kinase activator protein (free !1pyruvate dehydrogenase kinase). !$#cross-references MUID:92354776; PMID:1644204 !$#accession S29190 !'##molecule_type protein !'##residues 9-16,'IE' ##label PRI COMMENT This protein inactivates the pyruvate dehydrogenase complex !1by phosphorylating its E1 component alpha chain. CLASSIFICATION #superfamily branched-chain alpha-keto acid dehydrogenase !1kinase KEYWORDS mitochondrion; oxidoreductase; phosphotransferase FEATURE !$1-8 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$9-407 #product [pyruvate dehydrogenase (lipoamide)] kinase !82 #status experimental #label MAT SUMMARY #length 407 #molecular-weight 46105 #checksum 1191 SEQUENCE /// ENTRY KIECID #type complete TITLE [isocitrate dehydrogenase (NADP)] kinase (EC 2.7.1.116) / phosphatase (EC 3.1.3.-) precursor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 31-Oct-1997 #text_change 03-Jun-2002 ACCESSIONS G65208; B32016; B31837; A28666; A30763 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65208 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-578 ##label BLAT !'##cross-references GB:AE000474; GB:U00096; NID:g1790440; !1PIDN:AAC76986.1; PID:g1790446; UWGP:b4016 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A32016 !$#authors Klumpp, D.J.; Plank, D.W.; Bowdin, L.J.; Stueland, C.S.; !1Chung, T.; LaPorte, D.C. !$#journal J. Bacteriol. (1988) 170:2763-2769 !$#title Nucleotide sequence of aceK, the gene encoding isocitrate !1dehydrogenase kinase/phosphatase. !$#cross-references MUID:88227861; PMID:2836370 !$#accession B32016 !'##molecule_type DNA !'##residues 1-415,'DG',418-578 ##label KLU !'##cross-references GB:M20714; NID:g146442; PIDN:AAA24010.1; !1PID:g146444 !'##note submitted to GenBank, September 1988 REFERENCE A31837 !$#authors Matsuoka, M.; McFadden, B.A. !$#journal J. Bacteriol. (1988) 170:4528-4536 !$#title Isolation, hyperexpression, and sequencing of the aceA gene !1encoding isocitrate lyase in Escherichia coli. !$#cross-references MUID:89008064; PMID:3049537 !$#accession B31837 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-55 ##label MAT !'##cross-references GB:M22621; NID:g340728; PIDN:AAC13651.1; !1PID:g556178 REFERENCE A28666 !$#authors Cortay, J.C.; Bleicher, F.; Rieul, C.; Reeves, H.C.; !1Cozzone, A.J. !$#journal J. Bacteriol. (1988) 170:89-97 !$#title Nucleotide sequence and expression of the aceK gene coding !1for isocitrate dehydrogenase kinase/phosphatase in !1Escherichia coli. !$#cross-references MUID:88086929; PMID:2826408 !$#accession A28666 !'##molecule_type DNA !'##residues 1-91,'ITRASRLRRA',102,'LTPCTVGYLTTAR',116,'L',118, !1'SGFLSLALSQSAA',132,'VPF',136,'PAGQRLSPRSRLGISTDARYQ', !1137-138,'T',140,'AP','A',166-578 ##label COR !'##cross-references GB:M18974; NID:g146433; PIDN:AAA24007.1; !1PID:g146434 GENETICS !$#gene aceK !$#map_position 91 min FUNCTION KIN !$#description s a kinase, catalyzes the phosphorylation of a serine !1residue in isocitrate dehydrogenase (IDH) by ATP !$#note phosphorylation inactivates IDH, shutting down the !1tricarboxylic acid cycle and diverting intermediate !1metabolites to the glyoxylate bypass pathway FUNCTION PHO !$#description as a phosphatase, catalyzes the dephosphorylation of !1isocitrate dehydrogenase (IDH) !$#note dephosphorylation activates IDH, reenabling the !1tricarboxylic acid cycle CLASSIFICATION #superfamily isocitrate dehydrogenase kinase KEYWORDS ATP; phosphoric monoester hydrolase; phosphotransferase FEATURE !$336 #active_site Lys #status predicted SUMMARY #length 578 #molecular-weight 67698 #checksum 2542 SEQUENCE /// ENTRY A43100 #type complete TITLE ataxia telangiectasia-associated protein - human CONTAINS 1-phosphatidylinositol 3-kinase (EC 2.7.1.137) ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A43100 REFERENCE A43100 !$#authors Savitsky, K.; Bar-Shira, A.; Gilad, S.; Rotman, G.; Ziv, Y.; !1Vanagaite, L.; Tagle, D.A.; Smith, S.; Uziel, T.; Sfez, S.; !1Ashkenazi, M.; Pecker, I.; Frydman, M.; Harnik, R.; !1Patanjali, S.R.; Simmons, A.; Clines, G.A.; Sartiel, A.; !1Gatti, R.A.; Chessa, L.; Sanal, O.; Lavin, M.F.; Jaspers, !1N.G.J.; Taylor, A.M.R.; Arlett, C.F.; Miki, T.; Weissman, !1S.M.; Lovett, M.; Collins, F.S.; Shiloh, Y. !$#journal Science (1995) 268:1749-1753 !$#title A single ataxia telangiectasia gene with a product similar !1to PI-3 kinase. !$#cross-references MUID:95312868; PMID:7792600 !$#accession A43100 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-1708 ##label SAV !'##cross-references GB:U26455; NID:g870785; PIDN:AAA86520.1; !1PID:g870786 !'##experimental_source fibroblast GENETICS !$#gene GDB:ATM !'##cross-references GDB:593364; OMIM:208900 !$#map_position 11q22.3-11q22.3 !$#note alternatively spliced transcripts of the single gene may be !1produced !$#note mutations to this gene were found in AT patients from all !1complementation groups (including A, C, and DC) FUNCTION !$#description normal protein may function in detection of DNA damage and/ !1or blockage of cell growth and division until DNA damage is !1repaired CLASSIFICATION #superfamily ataxia telangiectasia-associated protein KEYWORDS apoptosis; cell cycle control; DNA repair; leukemia; !1lymphoma; phosphotransferase SUMMARY #length 1708 #molecular-weight 195977 #checksum 1895 SEQUENCE /// ENTRY S38040 #type complete TITLE 1-phosphatidylinositol 3-kinase (EC 2.7.1.137) TOR2 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YKL203c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 12-Nov-1999 ACCESSIONS S38040; S38041; S35106 REFERENCE S38024 !$#authors Maia e Silva, A.; Bossier, P.; Vilela, C.; Fernandes, L.; !1Soares, H.; Guerreiro, P.; Rodrigues-Pousada, C. !$#submission submitted to the Protein Sequence Database, March 1994 !$#accession S38040 !'##molecule_type DNA !'##residues 1-2360 ##label MAI !'##cross-references EMBL:Z28203; GSPDB:GN00011; MIPS:YKL203c !'##experimental_source strain S288C REFERENCE S37897 !$#authors Pohl, T.M.; Pohl, F.M. !$#submission submitted to the Protein Sequence Database, March 1994 !$#accession S38041 !'##molecule_type DNA !'##residues 1902-2473 ##label POH !'##cross-references EMBL:Z28203; GSPDB:GN00011; MIPS:YKL203c !'##experimental_source strain S288C REFERENCE S35106 !$#authors Kunz, J.; Henriquez, R.; Schneider, U.; Deuter-Reinhard, M.; !1Movva, N.R.; Hall, M.N. !$#journal Cell (1993) 73:585-596 !$#title Target of rapamycin in yeast, TOR2, is an essential !1phosphatidylinositol kinase homolog required for G(1) !1progression. !$#cross-references MUID:93258821; PMID:8387896 !$#accession S35106 !'##molecule_type DNA !'##residues 1-1472,'G',1473-2473 ##label KUN !'##cross-references EMBL:X71416; NID:g298027; PIDN:CAA50548.1; !1PID:g298028 GENETICS !$#gene SGD:TOR2; MIPS:YKL203c !'##cross-references SGD:S0001686; MIPS:YKL203c !$#map_position 11L CLASSIFICATION #superfamily yeast TOR2 protein KEYWORDS phosphotransferase SUMMARY #length 2473 #molecular-weight 281508 #checksum 2099 SEQUENCE /// ENTRY KIECAA #type complete TITLE acetate kinase (EC 2.7.2.1) - Escherichia coli (strain K-12) ALTERNATE_NAMES acetokinase ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 01-Mar-2002 ACCESSIONS JT0498; JX0358; F65001 REFERENCE JT0498 !$#authors Matsuyama, A.; Yamamoto, H.; Nakano, E. !$#journal J. Bacteriol. (1989) 171:577-580 !$#title Cloning, expression, and nucleotide sequence of the !1Escherichia coli K-12 ackA gene. !$#cross-references MUID:89123075; PMID:2536666 !$#accession JT0498 !'##molecule_type DNA !'##residues 1-400 ##label MAT !'##cross-references GB:M22956; NID:g145170; PIDN:AAA23406.1; !1PID:g145171 !'##experimental_source strain K12 !'##note parts of the sequence were confirmed by protein sequencing REFERENCE JX0357 !$#authors Kakuda, H.; Hosono, K.; Shiroishi, K.; Ichihara, S. !$#journal J. Biochem. (1994) 116:916-922 !$#title Identification and characterization of the ackA (acetate !1kinase A)-pta (phosphotransacetylase) operon and !1complementation analysis of acetate utilization by an !1ackA-pta deletion mutant of Escherichia coli. !$#cross-references MUID:95189796; PMID:7883769 !$#accession JX0358 !'##molecule_type DNA !'##residues 376-400 ##label KAK !'##cross-references DDBJ:D17576 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65001 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-400 ##label BLAT !'##cross-references GB:AE000318; GB:U00096; NID:g1788623; !1PIDN:AAC75356.1; PID:g1788633; UWGP:b2296 !'##experimental_source strain K-12, substrain MG1655 COMMENT Acetate kinase catalyzes the conversion of acetylphosphate !1to acetate while ADP is converted to ATP. It is involved in !1the activation of acetate to acetyl coA and the secretion of !1acetate. During anaerobic growth of the organism, this !1enzyme is also involved in the synthesis of most of the ATP !1formed catabolically. GENETICS !$#gene ackA CLASSIFICATION #superfamily acetate kinase KEYWORDS phosphotransferase SUMMARY #length 400 #molecular-weight 43290 #checksum 5212 SEQUENCE /// ENTRY G64189 #type complete TITLE acetate kinase (EC 2.7.2.1) - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS G64189 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession G64189 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-401 ##label TIGR !'##cross-references GB:U32800; GB:L42023; NID:g1574133; !1PIDN:AAC22858.1; PID:g1574134; TIGR:HI1204 CLASSIFICATION #superfamily acetate kinase KEYWORDS phosphotransferase SUMMARY #length 401 #molecular-weight 43757 #checksum 2171 SEQUENCE /// ENTRY B49935 #type complete TITLE acetate kinase (EC 2.7.2.1) ackA - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS B49935; C69581 REFERENCE A49935 !$#authors Grundy, F.J.; Waters, D.A.; Allen, S.H.G.; Henkin, T.M. !$#journal J. Bacteriol. (1993) 175:7348-7355 !$#title Regulation of the Bacillus subtilis acetate kinase gene by !1CcpA. !$#cross-references MUID:94042910; PMID:8226682 !$#accession B49935 !'##status preliminary !'##molecule_type DNA !'##residues 1-395 ##label GRU !'##cross-references GB:L17320; NID:g405132; PIDN:AAC36857.1; !1PID:g405134 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69581 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-395 ##label KUN !'##cross-references GB:Z99119; GB:AL009126; NID:g2635411; !1PIDN:CAB14925.1; PID:g2635431 !'##experimental_source strain 168 GENETICS !$#gene ackA CLASSIFICATION #superfamily acetate kinase KEYWORDS phosphotransferase SUMMARY #length 395 #molecular-weight 43137 #checksum 1207 SEQUENCE /// ENTRY B49338 #type complete TITLE acetate kinase (EC 2.7.2.1) - Methanosarcina thermophila ORGANISM #formal_name Methanosarcina thermophila DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B49338 REFERENCE A49338 !$#authors Latimer, M.T.; Ferry, J.G. !$#journal J. Bacteriol. (1993) 175:6822-6829 !$#title Cloning, sequence analysis, and hyperexpression of the genes !1encoding phosphotransacetylase and acetate kinase from !1Methanosarcina thermophila. !$#cross-references MUID:94042843; PMID:8226623 !$#accession B49338 !'##status preliminary !'##molecule_type DNA !'##residues 1-408 ##label LAT !'##cross-references GB:L23147; NID:g349832; PIDN:AAA72042.1; !1PID:g349834 CLASSIFICATION #superfamily acetate kinase KEYWORDS phosphotransferase SUMMARY #length 408 #molecular-weight 44337 #checksum 7806 SEQUENCE /// ENTRY Q3ECTD #type complete TITLE exuR-tdcC intergenic region acetate kinase homolog - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS H65100; JS0152; B30197 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65100 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-406 ##label BLAT !'##cross-references GB:AE000393; GB:U00096; NID:g1789499; !1PIDN:AAC76150.1; PID:g1789503; UWGP:b3115 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A30197 !$#authors Goss, T.J.; Schweizer, H.P.; Datta, P. !$#journal J. Bacteriol. (1988) 170:5352-5359 !$#title Molecular characterization of the tdc operon of Escherichia !1coli K-12. !$#cross-references MUID:89033926; PMID:3053659 !$#accession JS0152 !'##molecule_type DNA !'##residues 5-124,'P',126-132,'RSNY',137,'RA' ##label GOS !'##cross-references GB:M23638; NID:g147924; PIDN:AAA24663.1; !1PID:g147927 !'##experimental_source strain K12 COMMENT This protein is paralogous to the acetate kinase ackA, which !1catalyzes the conversion of acetylphosphate to acetate while !1ADP is converted to ATP. See PIR:KIECAA. GENETICS !$#gene yhaA !$#map_position 67 min CLASSIFICATION #superfamily acetate kinase KEYWORDS phosphotransferase SUMMARY #length 406 #molecular-weight 43928 #checksum 8548 SEQUENCE /// ENTRY B65071 #type complete TITLE probable carbamate kinase (EC 2.7.2.2) b2874 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS B65071 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65071 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-310 ##label BLAT !'##cross-references GB:AE000370; GB:U00096; NID:g2367170; !1PIDN:AAC75912.1; PID:g1789238; UWGP:b2874 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily carbamate kinase KEYWORDS phosphotransferase SUMMARY #length 310 #molecular-weight 33071 #checksum 8136 SEQUENCE /// ENTRY S73855 #type complete TITLE carbamate kinase (EC 2.7.2.2) arcC - Mycoplasma pneumoniae (strain ATCC 29342) ALTERNATE_NAMES hypothetical protein F10_orf309 ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Dec-1999 ACCESSIONS S73855 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73855 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-309 ##label HIM !'##cross-references EMBL:AE000052; GB:U00089; NID:g1674223; !1PIDN:AAB96177.1; PID:g1674225 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#gene arcC !$#genetic_code SGC3 CLASSIFICATION #superfamily carbamate kinase KEYWORDS phosphotransferase SUMMARY #length 309 #molecular-weight 32785 #checksum 2842 SEQUENCE /// ENTRY C64759 #type complete TITLE probable carbamate kinase (EC 2.7.2.2) yahI - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS C64759 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64759 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-316 ##label BLAT !'##cross-references GB:AE000139; GB:U00096; NID:g1786510; !1PIDN:AAC73426.1; PID:g1786516; UWGP:b0323 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yahI CLASSIFICATION #superfamily carbamate kinase KEYWORDS phosphotransferase SUMMARY #length 316 #molecular-weight 33931 #checksum 4592 SEQUENCE /// ENTRY S02137 #type complete TITLE carbamate kinase (EC 2.7.2.2) - Pseudomonas aeruginosa (strain PAO1) ORGANISM #formal_name Pseudomonas aeruginosa DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 31-Dec-2000 ACCESSIONS S02137; D82999 REFERENCE S02137 !$#authors Baur, H.; Luethi, E.; Stalon, V.; Mercenier, A.; Haas, D. !$#journal Eur. J. Biochem. (1989) 179:53-60 !$#title Sequence analysis and expression of the arginine-deiminase !1and carbamate-kinase genes of Pseudomonas aeruginosa. !$#cross-references MUID:89137094; PMID:2537202 !$#accession S02137 !'##molecule_type DNA !'##residues 1-310 ##label BAU !'##cross-references EMBL:X14693; NID:g45289; PIDN:CAA32823.1; !1PID:g45290 REFERENCE A82950 !$#authors Stover, C.K.; Pham, X.Q.; Erwin, A.L.; Mizoguchi, S.D.; !1Warrener, P.; Hickey, M.J.; Brinkman, F.S.L.; Hufnagle, !1W.O.; Kowalik, D.J.; Lagrou, M.; Garber, R.L.; Goltry, L.; !1Tolentino, E.; Westbrook-Wadman, S.; Yuan, Y.; Brody, L.L.; !1Coulter, S.N.; Folger, K.R.; Kas, A.; Larbig, K.; Lim, R.M.; !1Smith, K.A.; Spencer, D.H.; Wong, G.K.S.; Wu, Z.; Paulsen, !1I.T.; Reizer, J.; Saier, M.H.; Hancock, R.E.W.; Lory, S.; !1Olson, M.V. !$#journal Nature (2000) 406:959-964 !$#title Complete genome sequence of Pseudomonas aeruginosa PA01, an !1opportunistic pathogen. !$#cross-references MUID:20437337; PMID:10984043 !$#accession D82999 !'##status preliminary !'##molecule_type DNA !'##residues 1-310 ##label STO !'##cross-references GB:AE004930; GB:AE004091; NID:g9951472; !1PIDN:AAG08558.1; GSPDB:GN00131; PASP:PA5173 !'##experimental_source strain PAO1 GENETICS !$#gene arcC; PA5173 CLASSIFICATION #superfamily carbamate kinase KEYWORDS phosphotransferase SUMMARY #length 310 #molecular-weight 33080 #checksum 5798 SEQUENCE /// ENTRY G64079 #type complete TITLE carbamate kinase (EC 2.7.2.2) - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS G64079 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession G64079 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-310 ##label TIGR !'##cross-references GB:U32741; GB:L42023; NID:g1573582; !1PIDN:AAC22252.1; PID:g1573584; TIGR:HI0595 CLASSIFICATION #superfamily carbamate kinase KEYWORDS phosphotransferase SUMMARY #length 310 #molecular-weight 33440 #checksum 183 SEQUENCE /// ENTRY S76941 #type complete TITLE carbamate kinase (EC 2.7.2.2) - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S76941 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76941 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-308 ##label KAN !'##cross-references EMBL:D90917; GB:AB001339; NID:g1653836; !1PIDN:BAA18853.1; PID:g1653943 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily carbamate kinase KEYWORDS phosphotransferase SUMMARY #length 308 #molecular-weight 32935 #checksum 7909 SEQUENCE /// ENTRY H64783 #type complete TITLE carbamate kinase (EC 2.7.2.2) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS H64783 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64783 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-297 ##label BLAT !'##cross-references GB:AE000158; GB:U00096; NID:g1786728; !1PIDN:AAC73623.1; PID:g1786732; UWGP:b0521 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene arcC; ybcF CLASSIFICATION #superfamily carbamate kinase KEYWORDS phosphotransferase SUMMARY #length 297 #molecular-weight 31644 #checksum 3886 SEQUENCE /// ENTRY KIHUG #type complete TITLE phosphoglycerate kinase (EC 2.7.2.3) - human ALTERNATE_NAMES primer recognition protein 2 ORGANISM #formal_name Homo sapiens #common_name man DATE 14-Nov-1983 #sequence_revision 23-Aug-1996 #text_change 24-Sep-1999 ACCESSIONS I59050; A00669; A92279; A35739; A22426; I59539 REFERENCE I59050 !$#authors Michelson, A.M.; Blake, C.C.; Evans, S.T.; Orkin, S.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:6965-6969 !$#title Structure of the human phosphoglycerate kinase gene and the !1intron-mediated evolution and dispersal of the !1nucleotide-binding domain. !$#cross-references MUID:86016816; PMID:2995995 !$#accession I59050 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-417 ##label RE2 !'##cross-references GB:M11968; NID:g189920; PIDN:AAA60079.1; !1PID:g387021 REFERENCE A93962 !$#authors Michelson, A.M.; Markham, A.F.; Orkin, S.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:472-476 !$#title Isolation and DNA sequence of a full-length cDNA clone for !1human X chromosome-encoded phosphoglycerate kinase. !$#cross-references MUID:83169680; PMID:6188151 !$#accession A00669 !'##molecule_type mRNA !'##residues 1-417 ##label MIC !'##cross-references GB:L00160; GB:J00288; NID:g189904; PIDN:AAA60078.1; !1PID:g387020 !'##experimental_source liver REFERENCE A92279 !$#authors Huang, I.Y.; Welch, C.D.; Yoshida, A. !$#journal J. Biol. Chem. (1980) 255:6412-6420 !$#title Complete amino acid sequence of human phosphoglycerate !1kinase. Cyanogen bromide peptides and complete amino acid !1sequence. !$#cross-references MUID:80227775; PMID:7391027 !$#accession A92279 !'##molecule_type protein !'##residues 2-39,'K',40-52,'D',54-109,'D',111-275,'D',277-299,'E', !1301-336,'D',338-385,'Q',387-417 ##label HUA !'##experimental_source erythrocytes REFERENCE A35739 !$#authors Jindal, H.K.; Vishwanatha, J.K. !$#journal J. Biol. Chem. (1990) 265:6540-6543 !$#title Functional identity of a primer recognition protein as !1phosphoglycerate kinase. !$#cross-references MUID:90216667; PMID:2324090 !$#accession A35739 !'##molecule_type protein !'##residues 2-6;42-48;142-151;247-264;298-322;324-330;383-406 ##label !1JIN REFERENCE A22426 !$#authors Singer-Sam, J.; Keith, D.H.; Tani, K.; Simmer, R.L.; !1Shively, L.; Lindsay, S.; Yoshida, A.; Riggs, A.D. !$#journal Gene (1984) 32:409-417 !$#title Sequence of the promoter region of the gene for human !1X-linked 3-phosphoglycerate kinase. !$#cross-references MUID:85155507; PMID:6099325 !$#accession A22426 !'##molecule_type DNA !'##residues 1-21 ##label SIN REFERENCE I59539 !$#authors Pfeifer, G.P.; Steigerwald, S.D.; Mueller, P.R.; Wold, B.; !1Riggs, A.D. !$#journal Science (1989) 246:810-813 !$#title Genomic sequencing and methylation analysis by ligation !1mediated PCR. !$#cross-references MUID:90049205; PMID:2814502 !$#accession I59539 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-14 ##label RES !'##cross-references GB:M34017; NID:g189993; PIDN:AAA60103.1; !1PID:g189994 COMMENT The structure consists of two discrete, globular domains !1that are joined by residues 187-190 and correspond to the !1amino- and carboxyl-terminal halves of the sequence, except !1that residues 406-417 form a helix associated with the !1amino-terminal domain. COMMENT Residues thought to be involved in ADP-ATP binding are !1Glu-344 to ribose and Lys-220 to the alpha-phosphate group. !1The adenine ring is in a slot bounded by residues 213-215, !1237-239, and 340-342. GENETICS !$#gene GDB:PGK1 !'##cross-references GDB:120282; OMIM:311800 !$#map_position Xq13.3-Xq13.3 !$#introns 22/2; 39/2; 91/2; 139/3; 174/2; 214/2; 252/3; 312/3; 372/1; !1405/1 CLASSIFICATION #superfamily phosphoglycerate kinase KEYWORDS ATP; blocked amino end; gluconeogenesis; glycolysis; !1phosphotransferase FEATURE !$2 #modified_site blocked amino end (Ser) (in mature !8form) (probably acetylated) #status experimental\ !$220,344 #binding_site ATP (Lys, Glu) #status predicted SUMMARY #length 417 #molecular-weight 44614 #checksum 3110 SEQUENCE /// ENTRY KIHOG #type complete TITLE phosphoglycerate kinase (EC 2.7.2.3) - horse ORGANISM #formal_name Equus caballus #common_name domestic horse DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 28-Feb-1997 ACCESSIONS A92292; A00669 REFERENCE A92292 !$#authors Merrett, M. !$#journal J. Biol. Chem. (1981) 256:10293-10305 !$#title Primary structure of 3-phosphoglycerate kinase from horse !1muscle. II. Amino acid sequence of cyanogen bromide peptides !1CB1-CB4 and CB6-CB14, sequence of methionine-containing !1regions, and complete sequence of the enzyme. !$#cross-references MUID:82030789; PMID:7287713 !$#accession A92292 !'##molecule_type protein !'##residues 1-416 ##label MER REFERENCE A93209 !$#authors Banks, R.D.; Blake, C.C.F.; Evans, P.R.; Haser, R.; Rice, !1D.W.; Hardy, G.W.; Merrett, M.; Phillips, A.W. !$#journal Nature (1979) 279:773-777 !$#title Sequence, structure and activity of phosphoglycerate kinase: !1a possible hinge-bending enzyme. !$#cross-references MUID:79199779; PMID:450128 !$#contents annotation; X-ray crystallography, 2.5 angstroms; muscle COMMENT The structure consists of two discrete, globular domains !1that are joined by residues 186-189 and correspond to the !1amino- and carboxyl-terminal halves of the sequence, except !1that residues 405-416 form a helix associated with the !1amino-terminal domain. COMMENT Residues thought to be involved in ADP-ATP binding are !1Glu-343 to ribose and Lys-219 to the alpha-phosphate group. !1The adenine ring is in a slot bounded by residues 212-214, !1236-238, and 339-341. CLASSIFICATION #superfamily phosphoglycerate kinase KEYWORDS acetylated amino end; ATP; gluconeogenesis; glycolysis; !1phosphotransferase FEATURE !$1 #modified_site acetylated amino end (Ser) #status !8experimental\ !$219,343 #binding_site ATP (Lys, Glu) #status experimental SUMMARY #length 416 #molecular-weight 44494 #checksum 1604 SEQUENCE /// ENTRY KIFFPG #type complete TITLE phosphoglycerate kinase (EC 2.7.2.3) - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 11-Jun-1999 ACCESSIONS S30111; S25673 REFERENCE S30111 !$#authors Roselli-Rehfuss, L.; Ye, F.; Lissemore, J.L.; Sullivan, D.T. !$#journal Mol. Gen. Genet. (1992) 235:213-220 !$#title Structure and expression of the phosphoglycerate kinase !1(Pgk) gene of Drosophila melanogaster. !$#cross-references MUID:93101123; PMID:1465095 !$#accession S30111 !'##molecule_type DNA !'##residues 1-415 ##label ROS !'##cross-references EMBL:Z14029; NID:g11175; PIDN:CAA78404.1; !1PID:g11176 !'##experimental_source strain Oregon-R !'##note the authors translated the codon AAG for residue 139 as Cys GENETICS !$#gene pgk !'##cross-references FlyBase:FBgn0003075 !$#map_position II,23,A1-2 !$#introns 21/2; 336/2 CLASSIFICATION #superfamily phosphoglycerate kinase KEYWORDS ATP; gluconeogenesis; glycolysis; phosphotransferase FEATURE !$218,342 #binding_site ATP (Lys, Glu) #status predicted SUMMARY #length 415 #molecular-weight 43946 #checksum 8597 SEQUENCE /// ENTRY KIBYG #type complete TITLE phosphoglycerate kinase (EC 2.7.2.3) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YCR012w ORGANISM #formal_name Saccharomyces cerevisiae DATE 13-Jun-1983 #sequence_revision 12-May-1995 #text_change 21-Jul-2000 ACCESSIONS S19422; A00670; S07616; A38794; A91758; A93422; B93422; !1S05733 REFERENCE S19420 !$#authors Goffeau, A.; Purnelle, B.; Skala, J. !$#submission submitted to the Protein Sequence Database, March 1992 !$#accession S19422 !'##molecule_type DNA !'##residues 1-416 ##label GOF !'##cross-references EMBL:X59720; NID:g1907116; PIDN:CAA42329.1; !1PID:g1907155; GSPDB:GN00003; MIPS:YCR012w REFERENCE A93451 !$#authors Hitzeman, R.A.; Hagie, F.E.; Hayflick, J.S.; Chen, C.Y.; !1Seeburg, P.H.; Derynck, R. !$#journal Nucleic Acids Res. (1982) 10:7791-7808 !$#title The primary structure of the Saccharomyces cerevisiae gene !1for 3-phosphoglycerate kinase. !$#cross-references MUID:83116992; PMID:6296791 !$#accession A00670 !'##molecule_type DNA !'##residues 1-99,'G',101-416 ##label HIT !'##cross-references EMBL:J01342; NID:g172143; PIDN:AAA88729.1; !1PID:g1197055 REFERENCE S07616 !$#authors Perkins, R.E.; Conroy, S.C.; Dunbar, B.; Fothergill, L.A.; !1Tuite, M.F.; Dobson, M.J.; Kingsman, S.M.; Kingsman, A.J. !$#journal Biochem. J. (1983) 211:199-218 !$#title The complete amino acid sequence of yeast phosphoglycerate !1kinase. !$#cross-references MUID:83256430; PMID:6347186 !$#accession S07616 !'##molecule_type DNA !'##residues 1-99,'G',101-208;282-416 ##label PER !'##cross-references EMBL:K00553 !'##note the authors translated the codon GAA for residue 143 as Phe !$#accession A38794 !'##molecule_type protein !'##residues 175-416 ##label PER2 REFERENCE A91758 !$#authors Fattoum, A.; Roustan, C.; Karoui, D.; Feinberg, J.; Pradel, !1L.A.; Gregoire, J.; Rochat, H. !$#journal Int. J. Pept. Protein Res. (1981) 17:393-400 !$#title Structural studies on yeast 3-phosphoglycerate kinase. !$#cross-references MUID:82029924; PMID:7287307 !$#accession A91758 !'##molecule_type protein !'##residues 2,'G';175-184,'S',186-190,'I',192-202;239-261,'Q',263-270 !1##label FAT REFERENCE A93422 !$#authors Dobson, M.J.; Tuite, M.F.; Roberts, N.A.; Kingsman, A.J.; !1Kingsman, S.M.; Perkins, R.E.; Conroy, S.C.; Dunbar, B.; !1Fothergill, L.A. !$#journal Nucleic Acids Res. (1982) 10:2625-2637 !$#title Conservation of high efficiency promoter sequences in !1Saccharomyces cerevisiae. !$#cross-references MUID:82196896; PMID:6281737 !$#accession A93422 !'##molecule_type protein !'##residues 268-285,'T',287-292,'S',294-313,'T',315,'T',317-318,'E', !1320-329,'TV',332,'L',334-360,'T',362-365,'S',367-398 ##label !1DOB !$#accession B93422 !'##molecule_type DNA !'##residues 1-7 ##label DOB2 REFERENCE S05733 !$#authors Hoekema, A.; Kastelein, R.A.; Vasser, M.; de Boer, H.A. !$#journal Mol. Cell. Biol. (1987) 7:2914-2924 !$#title Codon replacement in the PGK1 gene of Saccharomyces !1cerevisiae: experimental approach to study the role of !1biased codon usage in gene expression. !$#cross-references MUID:88038832; PMID:2823108 !$#accession S05733 !'##molecule_type DNA !'##residues 1-99,'G',101-166 ##label HOE !'##cross-references EMBL:M17195; NID:g209594; PID:g209595 REFERENCE S05756 !$#authors Watson, H.C.; Walker, N.P.C.; Shaw, P.J.; Bryant, T.N.; !1Wendell, P.L.; Fothergill, L.A.; Perkins, R.E.; Conroy, !1S.C.; Dobson, M.J.; Tuite, M.F.; Kingsman, A.J.; Kingsman, !1S.M. !$#journal EMBO J. (1982) 1:1635-1640 !$#title Sequence and structure of yeast phosphoglycerate kinase. !$#cross-references MUID:84207923; PMID:6765200 !$#contents annotation; X-ray crystallography REFERENCE S25353 !$#authors Skala, J.; Purnelle, B.; Goffeau, A. !$#journal Yeast (1992) 8:409-417 !$#title The complete sequence of a 10.8 kb segment distal of SUF2 on !1the right arm of chromosome III from Saccharomyces !1cerevisiae reveals seven open reading frames including the !1RVS161, ADP1 and PGK genes. !$#cross-references MUID:92327849; PMID:1626432 !$#contents annotation GENETICS !$#gene SGD:PGK1; MIPS:YCR012w !'##cross-references SGD:S0000605; MIPS:YCR012w !$#map_position 3R CLASSIFICATION #superfamily phosphoglycerate kinase KEYWORDS acetylated amino end; ATP; gluconeogenesis; glycolysis; !1phosphotransferase FEATURE !$2-416 #product phosphoglycerate kinase #status experimental !8#label MAT\ !$2-185 #domain phosphoglycerate binding #status predicted !8#label PHO\ !$190-403 #domain ATP binding #status predicted #label ATP\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental\ !$218,342 #binding_site ATP (Lys, Glu) #status predicted SUMMARY #length 416 #molecular-weight 44837 #checksum 3646 SEQUENCE /// ENTRY KIVKGL #type complete TITLE phosphoglycerate kinase (EC 2.7.2.3) - yeast (Kluyveromyces marxianus var. lactis) ORGANISM #formal_name Kluyveromyces marxianus var. lactis, Candida sphaerica DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 11-Jun-1999 ACCESSIONS S07878 REFERENCE S07878 !$#authors Fournier, A.; Fleer, R.; Yeh, P.; Mayaux, J.F. !$#journal Nucleic Acids Res. (1990) 18:365 !$#title The primary structure of the 3-phosphoglycerate kinase (PGK) !1gene from Kluyveromyces lactis. !$#cross-references MUID:90221823; PMID:2326170 !$#accession S07878 !'##molecule_type DNA !'##residues 1-416 ##label FOU !'##cross-references EMBL:X17654; NID:g2866; PIDN:CAA35646.1; PID:g2867 GENETICS !$#gene pgk CLASSIFICATION #superfamily phosphoglycerate kinase KEYWORDS ATP; gluconeogenesis; glycolysis; phosphotransferase FEATURE !$218,342 #binding_site ATP (Lys, Glu) #status predicted SUMMARY #length 416 #molecular-weight 44527 #checksum 5052 SEQUENCE /// ENTRY TVTQGR #type complete TITLE phosphoglycerate kinase (EC 2.7.2.3) - fungus (Trichoderma reesei) ORGANISM #formal_name Trichoderma reesei DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 11-Jun-1999 ACCESSIONS S07803 REFERENCE S07803 !$#authors Vanhanen, S.; Penttilae, M.; Lehtovaara, P.; Knowles, J. !$#journal Curr. Genet. (1989) 15:181-186 !$#title Isolation and characterization of the 3-phosphoglycerate !1kinase gene (pgk) from the filamentous fungus Trichoderma !1reesei. !$#cross-references MUID:89354667; PMID:2670282 !$#accession S07803 !'##molecule_type DNA !'##residues 1-416 ##label VAN !'##cross-references EMBL:X15764; NID:g5189; PIDN:CAA33770.1; PID:g5190 GENETICS !$#gene pgk !$#introns 22/3; 163/1 CLASSIFICATION #superfamily phosphoglycerate kinase KEYWORDS ATP; gluconeogenesis; glycolysis; phosphotransferase FEATURE !$220,343 #binding_site ATP (Lys, Glu) #status predicted SUMMARY #length 416 #molecular-weight 44406 #checksum 8690 SEQUENCE /// ENTRY TVPLGC #type complete TITLE phosphoglycerate kinase (EC 2.7.2.3) - Penicillium chrysogenum ORGANISM #formal_name Penicillium chrysogenum DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 11-Jun-1999 ACCESSIONS S02040; S43917 REFERENCE S02040 !$#authors van Solingen, P.; Muurling, H.; Koekman, B.; van den Berg, !1J. !$#journal Nucleic Acids Res. (1988) 16:11823 !$#title Sequence of the Penicillium chrysogenum phosphoglycerate !1kinase gene. !$#cross-references MUID:89098338; PMID:3145495 !$#accession S02040 !'##molecule_type DNA !'##residues 1-415 ##label VAN !'##cross-references EMBL:X13379; NID:g3158; PIDN:CAA31756.1; PID:g3159 REFERENCE S43917 !$#authors Hoskins, I.C.; Roberts, C.F. !$#journal Mol. Gen. Genet. (1994) 243:270-276 !$#title Expression of the 3-phosphoglycerate kinase gene (pgkA) of !1Penicillium chrysogenum. !$#cross-references MUID:94247366; PMID:8190080 !$#accession S43917 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-22;401-415 ##label HOS GENETICS !$#gene pgkA !$#introns 22/3; 162/1 CLASSIFICATION #superfamily phosphoglycerate kinase KEYWORDS ATP; gluconeogenesis; glycolysis; phosphotransferase FEATURE !$219,342 #binding_site ATP (Lys, Glu) #status predicted SUMMARY #length 415 #molecular-weight 44022 #checksum 5046 SEQUENCE /// ENTRY TVUT4B #type complete TITLE phosphoglycerate kinase (EC 2.7.2.3) A (allele 4) - Trypanosoma brucei ORGANISM #formal_name Trypanosoma brucei DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 11-Jun-1999 ACCESSIONS S02233 REFERENCE S00748 !$#authors le Blancq, S.M.; Swinkels, B.W.; Gibson, W.C.; Borst, P. !$#journal J. Mol. Biol. (1988) 200:439-447 !$#title Evidence for gene conversion between the phosphoglycerate !1kinase genes of Trypanosoma brucei. !$#cross-references MUID:88286728; PMID:3267227 !$#accession S02233 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-508 ##label LEB !'##cross-references EMBL:X05890; NID:g10492; PIDN:CAA29319.1; !1PID:g10493 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1September 1987 CLASSIFICATION #superfamily phosphoglycerate kinase KEYWORDS ATP; glycolysis; phosphotransferase FEATURE !$312,434 #binding_site ATP (Lys, Glu) #status predicted SUMMARY #length 508 #molecular-weight 55668 #checksum 5682 SEQUENCE /// ENTRY TVUT2B #type complete TITLE phosphoglycerate kinase (EC 2.7.2.3) A (allele 2) - Trypanosoma brucei ORGANISM #formal_name Trypanosoma brucei DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 11-Jun-1999 ACCESSIONS S00748 REFERENCE S00748 !$#authors le Blancq, S.M.; Swinkels, B.W.; Gibson, W.C.; Borst, P. !$#journal J. Mol. Biol. (1988) 200:439-447 !$#title Evidence for gene conversion between the phosphoglycerate !1kinase genes of Trypanosoma brucei. !$#cross-references MUID:88286728; PMID:3267227 !$#accession S00748 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-505 ##label LEB !'##cross-references EMBL:X05889; NID:g10488; PIDN:CAA29316.1; !1PID:g10489 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1September 1987 CLASSIFICATION #superfamily phosphoglycerate kinase KEYWORDS ATP; glycolysis; phosphotransferase FEATURE !$312,434 #binding_site ATP (Lys, Glu) #status predicted SUMMARY #length 505 #molecular-weight 55375 #checksum 4355 SEQUENCE /// ENTRY A45593 #type complete TITLE phosphoglycerate kinase (EC 2.7.2.3), glycosomal - Trypanosoma brucei ORGANISM #formal_name Trypanosoma brucei DATE 22-Apr-1993 #sequence_revision 02-Jun-1994 #text_change 11-Jun-1999 ACCESSIONS A45593 REFERENCE A45593 !$#authors Alexander, K.; Parsons, M. !$#journal Mol. Biochem. Parasitol. (1991) 46:1-10 !$#title A phosphoglycerate kinase-like molecule localized to !1glycosomal microbodies: evidence that the topogenic signal !1is not at the C-terminus. !$#cross-references MUID:91304507; PMID:1852165 !$#accession A45593 !'##molecule_type DNA !'##residues 1-509 ##label ALE !'##cross-references GB:M37784; NID:g295366; PIDN:AAA32119.1; !1PID:g295367 !'##experimental_source EATRO 164 !'##note sequence extracted from NCBI backbone (NCBIN:42855, !1NCBIP:42870) CLASSIFICATION #superfamily phosphoglycerate kinase KEYWORDS ATP; glycosome; phosphotransferase SUMMARY #length 509 #molecular-weight 55747 #checksum 9972 SEQUENCE /// ENTRY KIUTGC #type complete TITLE phosphoglycerate kinase (EC 2.7.2.3), cytosolic (allele 2) - Trypanosoma brucei ALTERNATE_NAMES phosphoglycerate kinase B ORGANISM #formal_name Trypanosoma brucei DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 11-Jun-1999 ACCESSIONS A25119 REFERENCE A25119 !$#authors Osinga, K.A.; Swinkels, B.W.; Gibson, W.C.; Borst, P.; !1Veeneman, G.H.; Van Boom, J.H.; Michels, P.A.M.; Opperdoes, !1F.R. !$#journal EMBO J. (1985) 4:3811-3817 !$#title Topogenesis of microbody enzymes: a sequence comparison of !1the genes for the glycosomal (microbody) and cytosolic !1phosphoglycerate kinases of Trypanosoma brucei. !$#cross-references MUID:86136022; PMID:3004970 !$#accession A25119 !'##molecule_type DNA !'##residues 1-421 ##label OSI !'##cross-references GB:X03370; NID:g10496; PIDN:CAA27068.1; PID:g10497 COMMENT In T. brucei, three genes code for phosphoglycerate kinase !1isozymes, which are transported to different cell !1compartments. CLASSIFICATION #superfamily phosphoglycerate kinase KEYWORDS ATP; gluconeogenesis; glycolysis; phosphotransferase FEATURE !$224,346 #binding_site ATP (Lys, Glu) #status predicted SUMMARY #length 421 #molecular-weight 45154 #checksum 2613 SEQUENCE /// ENTRY KIUTGG #type complete TITLE phosphoglycerate kinase (EC 2.7.2.3), glycosomal (allele 2) - Trypanosoma brucei ALTERNATE_NAMES phosphoglycerate kinase C ORGANISM #formal_name Trypanosoma brucei DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 11-Jun-1999 ACCESSIONS B25119 REFERENCE A25119 !$#authors Osinga, K.A.; Swinkels, B.W.; Gibson, W.C.; Borst, P.; !1Veeneman, G.H.; Van Boom, J.H.; Michels, P.A.M.; Opperdoes, !1F.R. !$#journal EMBO J. (1985) 4:3811-3817 !$#title Topogenesis of microbody enzymes: a sequence comparison of !1the genes for the glycosomal (microbody) and cytosolic !1phosphoglycerate kinases of Trypanosoma brucei. !$#cross-references MUID:86136022; PMID:3004970 !$#accession B25119 !'##molecule_type DNA !'##residues 1-440 ##label OSI !'##cross-references GB:X03370; NID:g10496; PIDN:CAA27069.1; PID:g10498 COMMENT This is one of the three isozymes of T. brucei !1phosphoglycerate kinase; it is transported to glycosomes, !1which belong to a group of subcellular organelles called !1microbodies. CLASSIFICATION #superfamily phosphoglycerate kinase KEYWORDS ATP; gluconeogenesis; glycolysis; glycosome; !1phosphotransferase FEATURE !$223,345 #binding_site ATP (Lys, Glu) #status predicted SUMMARY #length 440 #molecular-weight 47118 #checksum 1365 SEQUENCE /// ENTRY TVUTGB #type complete TITLE phosphoglycerate kinase (EC 2.7.2.3), glycosomal (allele 4) - Trypanosoma brucei ALTERNATE_NAMES phosphoglycerate kinase C ORGANISM #formal_name Trypanosoma brucei DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 11-Jun-1999 ACCESSIONS S02235 REFERENCE S00748 !$#authors le Blancq, S.M.; Swinkels, B.W.; Gibson, W.C.; Borst, P. !$#journal J. Mol. Biol. (1988) 200:439-447 !$#title Evidence for gene conversion between the phosphoglycerate !1kinase genes of Trypanosoma brucei. !$#cross-references MUID:88286728; PMID:3267227 !$#accession S02235 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-440 ##label LEB !'##cross-references EMBL:X05890; NID:g10492; PIDN:CAA29321.1; !1PID:g10495 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1September 1987 CLASSIFICATION #superfamily phosphoglycerate kinase KEYWORDS ATP; glycolysis; glycosome; phosphotransferase FEATURE !$223,345 #binding_site ATP (Lys, Glu) #status predicted SUMMARY #length 440 #molecular-weight 47176 #checksum 1311 SEQUENCE /// ENTRY TVUTG4 #type complete TITLE phosphoglycerate kinase (EC 2.7.2.3), cytosolic (allele 4) - Trypanosoma brucei ALTERNATE_NAMES phosphoglycerate kinase B ORGANISM #formal_name Trypanosoma brucei DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 11-Jun-1999 ACCESSIONS S02234 REFERENCE S00748 !$#authors le Blancq, S.M.; Swinkels, B.W.; Gibson, W.C.; Borst, P. !$#journal J. Mol. Biol. (1988) 200:439-447 !$#title Evidence for gene conversion between the phosphoglycerate !1kinase genes of Trypanosoma brucei. !$#cross-references MUID:88286728; PMID:3267227 !$#accession S02234 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-420 ##label LEB !'##cross-references EMBL:X05890; NID:g10492; PIDN:CAA29320.1; !1PID:g10494 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1September 1987 CLASSIFICATION #superfamily phosphoglycerate kinase KEYWORDS ATP; gluconeogenesis; glycolysis; phosphotransferase FEATURE !$223,345 #binding_site ATP (Lys, Glu) #status predicted SUMMARY #length 420 #molecular-weight 45087 #checksum 8922 SEQUENCE /// ENTRY KICRGF #type complete TITLE phosphoglycerate kinase (EC 2.7.2.3) A, glycosomal - Crithidia fasciculata ORGANISM #formal_name Crithidia fasciculata DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 11-Jun-1999 ACCESSIONS S14463 REFERENCE S14463 !$#authors Swinkels, B.W.; Opperdoes, F.R.; Veenhuis, M.; Borst, P. !$#submission submitted to the EMBL Data Library, December 1989 !$#accession S14463 !'##molecule_type DNA !'##residues 1-505 ##label SWI !'##cross-references EMBL:X17251; NID:g6987; PIDN:CAA35114.1; PID:g6988 GENETICS !$#gene pgk-A CLASSIFICATION #superfamily phosphoglycerate kinase KEYWORDS ATP; gluconeogenesis; glycolysis; glycosome; !1phosphotransferase FEATURE !$308,430 #binding_site ATP (Lys, Glu) #status predicted SUMMARY #length 505 #molecular-weight 54757 #checksum 7460 SEQUENCE /// ENTRY TVCRGC #type complete TITLE phosphoglycerate kinase (EC 2.7.2.3), cytosolic - Crithidia fasciculata ALTERNATE_NAMES phosphoglycerate kinase B ORGANISM #formal_name Crithidia fasciculata DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 11-Jun-1999 ACCESSIONS S00486 REFERENCE S00486 !$#authors Swinkels, B.W.; Evers, R.; Borst, P. !$#journal EMBO J. (1988) 7:1159-1165 !$#title The topogenic signal of the glycosomal (microbody) !1phosphoglycerate kinase of Crithidia fasciculata resides in !1a carboxy-terminal extension. !$#cross-references MUID:88296420; PMID:3402434 !$#accession S00486 !'##molecule_type DNA !'##residues 1-417 ##label SWI !'##cross-references EMBL:X07458; NID:g6982; PIDN:CAA30341.1; PID:g6983 !'##note the authors translated the codon GAC for residue 173 as Thr, !1CAA for residue 292 as Lys, and GGC for residue 293 as Ala CLASSIFICATION #superfamily phosphoglycerate kinase KEYWORDS ATP; gluconeogenesis; glycolysis; phosphotransferase FEATURE !$220,342 #binding_site ATP (Lys, Glu) #status predicted SUMMARY #length 417 #molecular-weight 44602 #checksum 3677 SEQUENCE /// ENTRY TVCRGG #type complete TITLE phosphoglycerate kinase (EC 2.7.2.3), glycosomal - Crithidia fasciculata ALTERNATE_NAMES phosphoglycerate kinase C ORGANISM #formal_name Crithidia fasciculata DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 11-Jun-1999 ACCESSIONS S00487 REFERENCE S00486 !$#authors Swinkels, B.W.; Evers, R.; Borst, P. !$#journal EMBO J. (1988) 7:1159-1165 !$#title The topogenic signal of the glycosomal (microbody) !1phosphoglycerate kinase of Crithidia fasciculata resides in !1a carboxy-terminal extension. !$#cross-references MUID:88296420; PMID:3402434 !$#accession S00487 !'##molecule_type DNA !'##residues 1-455 ##label SWI !'##cross-references EMBL:X07459; NID:g6984; PIDN:CAA30342.1; PID:g6985 !'##note the authors translated the codon GAC for residue 173 as Thr, !1CAA for residue 292 as Lys, and GGC for residue 293 as Ala CLASSIFICATION #superfamily phosphoglycerate kinase KEYWORDS ATP; glycolysis; glycosome; phosphotransferase FEATURE !$220,342 #binding_site ATP (Lys, Glu) #status predicted SUMMARY #length 455 #molecular-weight 47843 #checksum 8443 SEQUENCE /// ENTRY TVECG #type complete TITLE phosphoglycerate kinase (EC 2.7.2.3) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 01-Mar-2002 ACCESSIONS S04733; E65077 REFERENCE S04730 !$#authors Alefounder, P.R.; Perham, R.N. !$#journal Mol. Microbiol. (1989) 3:723-732 !$#title Identification, molecular cloning and sequence analysis of a !1gene cluster encoding the class II fructose 1,6-bisphosphate !1aldolase, 3-phosphoglycerate kinase and a putative second !1glyceraldehyde 3-phosphate dehydrogenase of Escherichia !1coli. !$#cross-references MUID:89313302; PMID:2546007 !$#accession S04733 !'##molecule_type DNA !'##residues 1-387 ##label ALE !'##cross-references EMBL:X14436; NID:g41417; PIDN:CAA32604.1; !1PID:g41422 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65077 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-387 ##label BLAT !'##cross-references GB:AE000376; GB:U00096; NID:g2367176; !1PIDN:AAC75963.1; PID:g1789294; UWGP:b2926 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene pgk !$#map_position 63 min CLASSIFICATION #superfamily phosphoglycerate kinase KEYWORDS ATP; gluconeogenesis; glycolysis; phosphotransferase FEATURE !$197,314 #binding_site ATP (Lys, Glu) #status predicted SUMMARY #length 387 #molecular-weight 41118 #checksum 156 SEQUENCE /// ENTRY KIZYG #type complete TITLE phosphoglycerate kinase (EC 2.7.2.3) - Zymomonas mobilis ORGANISM #formal_name Zymomonas mobilis DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 11-Jun-1999 ACCESSIONS A27745 REFERENCE A27745 !$#authors Conway, T.; Ingram, L.O. !$#journal J. Bacteriol. (1988) 170:1926-1933 !$#title Phosphoglycerate kinase gene from Zymomonas mobilis: !1cloning, sequencing, and localization within the gap operon. !$#cross-references MUID:88169526; PMID:2832389 !$#accession A27745 !'##molecule_type DNA !'##residues 1-397 ##label CON !'##cross-references GB:M19376; NID:g155603; PIDN:AAA27699.1; !1PID:g155604 COMMENT This enzyme catalyzes the first glycolytic reaction to !1produce ATP by transferring a phosphoryl group from !1bis-phosphoglycerate to ADP. GENETICS !$#gene pgk CLASSIFICATION #superfamily phosphoglycerate kinase KEYWORDS ATP; gluconeogenesis; glycolysis; phosphotransferase FEATURE !$202,324 #binding_site ATP (Lys, Glu) #status predicted SUMMARY #length 397 #molecular-weight 41387 #checksum 1389 SEQUENCE /// ENTRY TVTWG #type complete TITLE phosphoglycerate kinase (EC 2.7.2.3) - Thermus aquaticus ORGANISM #formal_name Thermus aquaticus DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 11-Jun-1999 ACCESSIONS S01307; A38802 REFERENCE S01307 !$#authors Bowen, D.; Littlechild, J.A.; Fothergill, J.E.; Watson, !1H.C.; Hall, L. !$#journal Biochem. J. (1988) 254:509-517 !$#title Nucleotide sequence of the phosphoglycerate kinase gene from !1the extreme thermophile Thermus thermophilus. Comparison of !1the deduced amino acid sequence with that of the mesophilic !1yeast phosphoglycerate kinase. !$#cross-references MUID:89025722; PMID:3052437 !$#accession S01307 !'##molecule_type DNA !'##residues 1-390 ##label BOW !'##cross-references EMBL:X12464; NID:g48248; PIDN:CAA31006.1; !1PID:g48249 !$#accession A38802 !'##molecule_type protein !'##residues 2-25;34-42;44-50,'X',52-55;134-147;149-157;257-266;363-372 !1##label BOW2 !'##note the source is designated as Thermus thermophilus CLASSIFICATION #superfamily phosphoglycerate kinase KEYWORDS ATP; gluconeogenesis; glycolysis; phosphotransferase FEATURE !$2-390 #product phosphoglycerate kinase #status experimental !8#label MAT\ !$198,320 #binding_site ATP (Lys, Glu) #status predicted SUMMARY #length 390 #molecular-weight 41777 #checksum 765 SEQUENCE /// ENTRY KIBSGM #type complete TITLE phosphoglycerate kinase (EC 2.7.2.3) - Bacillus megaterium ORGANISM #formal_name Bacillus megaterium DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 21-Jan-2000 ACCESSIONS S13125; JQ1954 REFERENCE S13125 !$#authors Schlaepfer, B.S.; Branlant, C.; Branlant, G.; Zuber, H. !$#journal Nucleic Acids Res. (1990) 18:6423 !$#title Nucleotide sequence of the phosphoglycerate kinase gene from !1Bacillus megaterium. !$#cross-references MUID:91057129; PMID:2123031 !$#accession S13125 !'##molecule_type DNA !'##residues 1-394 ##label SCH !'##cross-references EMBL:X54519; NID:g39642; PIDN:CAA38375.1; !1PID:g39643 !'##experimental_source DSM 319 REFERENCE JQ1952 !$#authors Schlaepfer, B.S.; Zuber, H. !$#journal Gene (1992) 122:53-62 !$#title Cloning and sequencing of the genes encoding !1glyceraldehyde-3-phosphate dehydrogenase, phosphoglycerate !1kinase and triosephosphate isomerase (gap operon) from !1mesophilic Bacillus megaterium: comparison with !1corresponding sequences from thermophilic Bacillus !1stearothermophilus. !$#cross-references MUID:93083995; PMID:1452037 !$#accession JQ1954 !'##molecule_type DNA !'##residues 1-394 ##label SC2 !'##cross-references GB:M87647; NID:g143315; PIDN:AAA73203.1; !1PID:g143318 !'##experimental_source strain DSM319 GENETICS !$#gene pgk CLASSIFICATION #superfamily phosphoglycerate kinase KEYWORDS ATP; gluconeogenesis; glycolysis; phosphotransferase FEATURE !$201,323 #binding_site ATP (Lys, Glu) #status predicted SUMMARY #length 394 #molecular-weight 42457 #checksum 2685 SEQUENCE /// ENTRY TVWTGY #type complete TITLE phosphoglycerate kinase (EC 2.7.2.3), cytosolic - wheat ORGANISM #formal_name Triticum aestivum #common_name common wheat DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 11-Jun-1999 ACCESSIONS S05966 REFERENCE S05966 !$#authors Longstaff, M.; Raines, C.A.; McMorrow, E.M.; Bradbeer, J.W.; !1Dyer, T.A. !$#journal Nucleic Acids Res. (1989) 17:6569-6580 !$#title Wheat phosphoglycerate kinase: evidence for recombination !1between the genes for the chloroplastic and cytosolic !1enzymes. !$#cross-references MUID:89385983; PMID:2780287 !$#accession S05966 !'##molecule_type mRNA !'##residues 1-401 ##label LON !'##cross-references EMBL:X15232; NID:g21834; PIDN:CAA33302.1; !1PID:g21835 GENETICS !$#map_position 6 CLASSIFICATION #superfamily phosphoglycerate kinase KEYWORDS ATP; gluconeogenesis; glycolysis; phosphotransferase FEATURE !$206,328 #binding_site ATP (Lys, Glu) #status predicted SUMMARY #length 401 #molecular-weight 42122 #checksum 4351 SEQUENCE /// ENTRY TVWTGC #type complete TITLE phosphoglycerate kinase (EC 2.7.2.3) precursor, chloroplast - wheat ORGANISM #formal_name Triticum aestivum #common_name common wheat DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 11-Jun-1999 ACCESSIONS S05967 REFERENCE S05966 !$#authors Longstaff, M.; Raines, C.A.; McMorrow, E.M.; Bradbeer, J.W.; !1Dyer, T.A. !$#journal Nucleic Acids Res. (1989) 17:6569-6580 !$#title Wheat phosphoglycerate kinase: evidence for recombination !1between the genes for the chloroplastic and cytosolic !1enzymes. !$#cross-references MUID:89385983; PMID:2780287 !$#accession S05967 !'##molecule_type mRNA !'##residues 1-480 ##label LON !'##cross-references EMBL:X15233; NID:g21832; PIDN:CAA33303.1; !1PID:g21833 GENETICS !$#map_position 1 CLASSIFICATION #superfamily phosphoglycerate kinase KEYWORDS ATP; Calvin cycle; chloroplast; phosphotransferase FEATURE !$1-72 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$73-480 #product phosphoglycerate kinase #status predicted !8#label MAT\ !$277,399 #binding_site ATP (Lys, Glu) #status predicted SUMMARY #length 480 #molecular-weight 49839 #checksum 9104 SEQUENCE /// ENTRY B64233 #type complete TITLE phosphoglycerate kinase (EC 2.7.2.3) - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 17-Nov-1995 #sequence_revision 23-Aug-1996 #text_change 07-Dec-1999 ACCESSIONS B64233 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession B64233 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-416 ##label TIGR !'##cross-references GB:U39711; GB:L43967; NID:g1045997; PID:g1045999; !1TIGR:MG300 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 !$#start_codon GTG CLASSIFICATION #superfamily phosphoglycerate kinase KEYWORDS ATP; phosphotransferase FEATURE !$221,344 #binding_site ATP (Lys, Glu) #status predicted SUMMARY #length 416 #molecular-weight 45379 #checksum 488 SEQUENCE /// ENTRY A69119 #type complete TITLE 2-phosphoglycerate kinase (EC 2.7.2.-) - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A69119 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession A69119 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-306 ##label MTH !'##cross-references GB:AE000940; GB:AE000666; NID:g2623011; !1PIDN:AAB86349.1; PID:g2623021 !'##experimental_source strain Delta H GENETICS !$#gene MTH1883 CLASSIFICATION #superfamily 2-phosphoglycerate kinase KEYWORDS phosphotransferase SUMMARY #length 306 #molecular-weight 34883 #checksum 9614 SEQUENCE /// ENTRY A64485 #type complete TITLE 2-phosphoglycerate kinase (EC 2.7.2.-) - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A64485 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession A64485 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-309 ##label BUL !'##cross-references GB:U67589; GB:L77117; NID:g2826417; !1PIDN:AAB99494.1; PID:g1592120; TIGR:MJ1482 GENETICS !$#map_position FOR1453393-1454322 CLASSIFICATION #superfamily 2-phosphoglycerate kinase KEYWORDS phosphotransferase SUMMARY #length 309 #molecular-weight 35544 #checksum 3680 SEQUENCE /// ENTRY D69112 #type complete TITLE 2-phosphoglycerate kinase (EC 2.7.2.-) - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS D69112 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession D69112 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-321 ##label MTH !'##cross-references GB:AE000936; GB:AE000666; NID:g2622959; !1PIDN:AAB86301.1; PID:g2622969 !'##experimental_source strain Delta H GENETICS !$#gene MTH1835 !$#start_codon TTG CLASSIFICATION #superfamily 2-phosphoglycerate kinase KEYWORDS phosphotransferase SUMMARY #length 321 #molecular-weight 36641 #checksum 6058 SEQUENCE /// ENTRY KIBYD #type complete TITLE aspartate kinase (EC 2.7.2.4) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YER052c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 23-Mar-2001 ACCESSIONS A35888; S50555; A28355; S11170 REFERENCE A35888 !$#authors Rafalski, J.A.; Falco, S.C. !$#journal J. Biol. Chem. (1990) 265:15346 !$#cross-references MUID:90368723; PMID:2168408 !$#contents erratum !$#accession A35888 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-527 ##label RAF !'##cross-references GB:J03526; NID:g171692; PIDN:AAA34681.1; !1PID:g171693 REFERENCE S50432 !$#authors Dietrich, F.S. !$#submission submitted to the EMBL Data Library, December 1994 !$#description The sequence of S. cerevisiae cosmids 9379, 9581, and lambda !1clone 4678. !$#accession S50555 !'##molecule_type DNA !'##residues 1-527 ##label DIE !'##cross-references EMBL:U18796; NID:g603265; PIDN:AAB64587.1; !1PID:g603285; GSPDB:GN00005; MIPS:YER052c REFERENCE A28355 !$#authors Rafalski, J.A.; Falco, S.C. !$#journal J. Biol. Chem. (1988) 263:2146-2151 !$#title Structure of the yeast HOM3 gene which encodes !1aspartokinase. !$#cross-references MUID:88115350; PMID:2892836 !$#accession A28355 !'##molecule_type DNA !'##residues 1-408,'FQMQTH' ##label RAF2 !'##cross-references GB:J03526 !'##note this sequence has been revised in reference A35888 GENETICS !$#gene SGD:HOM3; MIPS:YER052c !'##cross-references SGD:S0000854; MIPS:YER052c !$#map_position 5R CLASSIFICATION #superfamily aspartate kinase; aspartate kinase homology KEYWORDS ATP; methionine biosynthesis; phosphotransferase; threonine !1biosynthesis FEATURE !$14-501 #domain aspartate kinase homology #label DKI SUMMARY #length 527 #molecular-weight 58109 #checksum 2192 SEQUENCE /// ENTRY DEECK #type complete TITLE thrA bifunctional enzyme [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES aspartokinase I / homoserine dehydrogenase I; protein f132 CONTAINS aspartate kinase (EC 2.7.2.4) I [validated]; homoserine dehydrogenase (EC 1.1.1.3) I [validated] ORGANISM #formal_name Escherichia coli DATE 31-Dec-1980 #sequence_revision 10-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS B64720; S56629; A00671; A15659; A14560; S40531; I57719; !1I69970; I73480 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64720 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-820 ##label BLAT !'##cross-references GB:AE000111; GB:U00096; NID:g1786181; !1PIDN:AAC73113.1; PID:g1786183; UWGP:b0002 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56629 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-820 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97301.1; !1PID:g537245 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A00671 !$#authors Cossart, P. !$#citation unpublished results, cited by Zakin, M.M., Duchange, N., !1Ferrara, P., and Cohen, G.N., in J. Biol. Chem. 258, !13028-3031, 1983 !$#accession A00671 !'##molecule_type DNA !'##residues 1-229,'N',231-374,'L',376-392,'A',394-405,'L',407-552,'N', !1554-606,'I',608-657,'R',659-820 ##label COS1 REFERENCE A15659 !$#authors Katinka, M.; Cossart, P.; Sibilli, L.; Saint-Girons, I.; !1Chalvignac, M.A.; Le Bras, G.; Cohen, G.N.; Yaniv, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1980) 77:5730-5733 !$#title Nucleotide sequence of the thrA gene of Escherichia coli. !$#cross-references MUID:81077247; PMID:7003595 !$#accession A15659 !'##molecule_type DNA !'##residues 1-10,'L',12-229,'N',231-374,'L',376-392,'A',394-405,'L', !1407-552,'N',554-606,'I',608-657,'R',659-820 ##label KAT !'##cross-references GB:J01706; EMBL:V00360; NID:g147977; !1PIDN:AAA83914.1; PID:g147979 !'##note this sequence has been revised in reference A00671 REFERENCE A14560 !$#authors Sibilli, L.; Le Bras, G.; Cossart, P.; Chalvignac, M.A.; Le !1Bras, G.; Briley, P.A.; Cohen, G.N. !$#journal Biochimie (1979) 61:733-739 !$#title The primary structure of Escherichia coli K 12 aspartokinase !1I-homoserine dehydrogenase I: sequence of cyanogen bromide !1peptide CB 3. !$#cross-references MUID:80043179; PMID:387092 !$#accession A14560 !'##molecule_type protein !'##residues 51-112,'E',114-129 ##label SIB REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40531 !'##molecule_type DNA !'##residues 1-10,'L',12-229,'N',231-374,'L',376-392,'A',394-405,'L', !1407-552,'N',554-606,'I',608-657,'R',659-820 ##label YUR !'##cross-references EMBL:D10483; NID:g216434; PIDN:BAA01286.1; !1PID:g216435 !'##experimental_source strain K-12 REFERENCE I57719 !$#authors Cossart, P.; Katinka, M.; Yaniv, M. !$#journal Mol. Gen. Genet. (1979) 175:39-44 !$#title Construction and expression of a hybrid plasmid containing !1the Escherichia coli thr-A and thr-B genes. !$#cross-references MUID:80077291; PMID:390305 !$#accession I57719 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 553-586,'IT' ##label COS2 !'##cross-references GB:M10644; NID:g147982; PIDN:AAA24671.1; !1PID:g147983 REFERENCE I55222 !$#authors Gardner, J.F. !$#journal J. Biol. Chem. (1982) 257:3896-3904 !$#title Initiation, pausing, and termination of transcription in the !1threonine operon regulatory region of Escherichia coli. !$#cross-references MUID:82142573; PMID:6277952 !$#accession I69970 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-10 ##label GAR !'##cross-references EMBL:X68872; NID:g43073; PIDN:CAA48734.1; !1PID:g43075 REFERENCE I56399 !$#authors Lynn, S.P.; Bauer, C.E.; Chapman, K.A.; Gardner, J.F. !$#journal J. Mol. Biol. (1985) 183:529-541 !$#title Identification and characterization of mutants affecting !1transcription termination at the threonine operon !1attenuator. !$#cross-references MUID:85264808; PMID:2410621 !$#accession I73480 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-10 ##label LYN !'##cross-references GB:M28570; NID:g290476; PIDN:AAA24673.1; !1PID:g290478 GENETICS !$#gene thrA; thrA1; thrA2 !$#map_position 0 min FUNCTION ASP !$#description as aspartate kinase, catalyzes the phosphorylation by ATP of !1aspartate !$#pathway aspartate metabolism !$#note regulated allosterically by L-threonine FUNCTION HOM !$#description as homoserine dehydrogenase catalyzes the reduction by NADH !1of aspartate beta-semialdehyde to homoserine !$#pathway glycine metabolism; serine metabolism; threonine !1biosynthesis CLASSIFICATION #superfamily thrA bifunctional enzyme; aspartate kinase !1homology; homoserine dehydrogenase homology KEYWORDS allosteric regulation; homotetramer; multifunctional enzyme; !1oxidoreductase; phosphotransferase; threonine biosynthesis FEATURE !$1-460 #domain aspartate kinase homology #label DKI\ !$463-719 #domain homoserine dehydrogenase homology #label HSD\ !$467-495 #region beta-alpha-beta NAD(P) nucleotide-binding !8fold SUMMARY #length 820 #molecular-weight 89119 #checksum 8053 SEQUENCE /// ENTRY DEECK2 #type complete TITLE metL bifunctional enzyme - Escherichia coli (strain K-12) ALTERNATE_NAMES aspartokinase II/homoserine dehydrogenase II CONTAINS aspartate kinase (EC 2.7.2.4) II; homoserine dehydrogenase (EC 1.1.1.3) II ORGANISM #formal_name Escherichia coli DATE 19-Feb-1984 #sequence_revision 22-Nov-1996 #text_change 01-Mar-2002 ACCESSIONS S40883; A00672; G65200 REFERENCE S40802 !$#authors Plunkett III, G.; Burland, V.; Daniels, D.L.; Blattner, F.R. !$#journal Nucleic Acids Res. (1993) 21:3391-3398 !$#title Analysis of the Escherichia coli genome. III. DNA sequence !1of the region from 87.2 to 89.2 minutes. !$#cross-references MUID:93347969; PMID:8346018 !$#accession S40883 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-810 ##label PLU !'##cross-references EMBL:L19201; NID:g304961; PIDN:AAB03072.1; !1PID:g305043 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1993 REFERENCE A00672 !$#authors Zakin, M.M.; Duchange, N.; Ferrara, P.; Cohen, G.N. !$#journal J. Biol. Chem. (1983) 258:3028-3031 !$#title Nucleotide sequence of the metL gene of Escherichia coli. !1Its product, the bifunctional aspartokinase II-homoserine !1dehydrogenase II, and the bifunctional product of the thrA !1gene, aspartokinase I-homoserine dehydrogenase I, derive !1from a common ancestor. !$#cross-references MUID:83135751; PMID:6298218 !$#accession A00672 !'##molecule_type DNA !'##residues 2-55,'R',57-58,'S',60-673,'S',675-761,'R',763-810 ##label !1ZAK !'##cross-references EMBL:V00305 !'##note the authors translated the codon CGA for residue 762 as Ala; !1the codon given for residue 333 (GGG) is inconsistent with !1the authors' translation and is corrected to GCG in the EMBL !1Data Library REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65200 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-810 ##label BLAT !'##cross-references GB:AE000468; GB:U00096; NID:g1790374; !1PIDN:AAC76922.1; PID:g1790376; UWGP:b3940 !'##experimental_source strain K-12, substrain MG1655 COMMENT This protein catalyzes two nonconsecutive reactions in the !1common biosynthetic pathway leading from aspartate to !1diaminopimelate and lysine, to methionine, and to threonine !1and isoleucine. The enzyme activities are regulated !1allosterically by methionine. GENETICS !$#gene metL !$#map_position 89 min CLASSIFICATION #superfamily thrA bifunctional enzyme; aspartate kinase !1homology; homoserine dehydrogenase homology KEYWORDS homodimer; isoleucine biosynthesis; lysine biosynthesis; !1methionine biosynthesis; multifunctional enzyme; !1oxidoreductase; phosphotransferase; threonine biosynthesis FEATURE !$12-453 #domain aspartate kinase homology #label DKI\ !$456-712 #domain homoserine dehydrogenase homology #label HSD\ !$460-488 #region beta-alpha-beta NAD(P) nucleotide-binding !8fold SUMMARY #length 810 #molecular-weight 88887 #checksum 9911 SEQUENCE /// ENTRY KIECAE #type complete TITLE acetylglutamate kinase (EC 2.7.2.8) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 01-Mar-2002 ACCESSIONS JT0331; B65203; B30776 REFERENCE JT0331 !$#authors Parsot, C.; Boyen, A.; Cohen, G.N.; Glansdorff, N. !$#journal Gene (1988) 68:275-283 !$#title Nucleotide sequence of Escherichia coli argB and argC genes: !1comparison of N-acetylglutamate kinase and !1N-acetylglutamate-gamma-semialdehyde dehydrogenase with !1homologous and analogous enzymes. !$#cross-references MUID:89121510; PMID:2851495 !$#accession JT0331 !'##molecule_type DNA !'##residues 1-258 ##label PAR !'##cross-references GB:M21446; NID:g145332; PIDN:AAA23478.1; !1PID:g145334 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65203 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-258 ##label BLAT !'##cross-references GB:AE000470; GB:U00096; NID:g2367332; !1PIDN:AAC76941.1; PID:g1790397; UWGP:b3959 !'##experimental_source strain K-12, substrain MG1655 COMMENT In arginine biosynthesis glutamate is first converted to !1N-acetylglutamate, which leads to N-acetylglutamylphosphate !1and then to N-acetylglutamate semialdehyde. The latter two !1reactions are catalyzed by acetylglutamate kinase and !1N-acetyl-gamma-glutamyl-phosphate reductase. GENETICS !$#gene argB !$#map_position 90 min CLASSIFICATION #superfamily acetylglutamate kinase KEYWORDS arginine biosynthesis; phosphotransferase SUMMARY #length 258 #molecular-weight 27159 #checksum 2227 SEQUENCE /// ENTRY KIECEG #type complete TITLE glutamate 5-kinase (EC 2.7.2.11) - Escherichia coli (strain K-12) ALTERNATE_NAMES gamma-glutamyl kinase ORGANISM #formal_name Escherichia coli DATE 31-Dec-1988 #sequence_revision 12-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS C64749; A31001; C31001; B31001 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64749 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-367 ##label BLAT !'##cross-references GB:AE000132; GB:U00096; NID:g2367098; !1PIDN:AAC73346.1; PID:g1786437; UWGP:b0242 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A93531 !$#authors Deutch, A.H.; Rushlow, K.E.; Smith, C.J. !$#journal Nucleic Acids Res. (1984) 12:6337-6355 !$#title Analysis of the Escherichia coli proBA locus by DNA and !1protein sequencing. !$#cross-references MUID:84297232; PMID:6089111 !$#accession A31001 !'##molecule_type DNA !'##residues 1-142,'A',144-367 ##label DE1 !'##cross-references GB:D83536; NID:g4902908; PIDN:BAA77911.1; !1PID:g4902977 !$#accession C31001 !'##molecule_type protein !'##residues 1-6;8-12 ##label DE2 COMMENT This enzyme catalyzes the ATP-dependent phosphorylation of !1glutamate to form glutamate-5-phosphate and ADP, the first !1enzymatic reaction of the proline biosynthesis pathway. GENETICS !$#gene proB !$#map_position 6 min FUNCTION !$#pathway amino acid metabolism CLASSIFICATION #superfamily glutamate 5-kinase KEYWORDS phosphotransferase; proline biosynthesis FEATURE !$1-367 #product glutamate 5-kinase #status experimental !8#label MAT SUMMARY #length 367 #molecular-weight 39056 #checksum 7888 SEQUENCE /// ENTRY KISEEM #type complete TITLE glutamate 5-kinase (EC 2.7.2.11) - Serratia marcescens ORGANISM #formal_name Serratia marcescens DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 11-Jun-1999 ACCESSIONS A49753; S11644 REFERENCE A49753 !$#authors Omori, K.; Suzuki, S.I.; Imai, Y.; Komatsubara, S. !$#journal J. Gen. Microbiol. (1991) 137:509-517 !$#title Analysis of the Serratia marcescens proBA operon and !1feedback control of proline biosynthesis. !$#cross-references MUID:91237315; PMID:1851803 !$#accession A49753 !'##molecule_type DNA !'##residues 1-367 ##label OMO !'##cross-references GB:X53086; NID:g47251; PIDN:CAA37254.1; PID:g47253 GENETICS !$#gene proB CLASSIFICATION #superfamily glutamate 5-kinase KEYWORDS phosphotransferase; proline biosynthesis SUMMARY #length 367 #molecular-weight 39169 #checksum 7983 SEQUENCE /// ENTRY KIHUCM #type complete TITLE creatine kinase (EC 2.7.3.2) chain M [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1990 #sequence_revision 22-Apr-1995 #text_change 08-Dec-2000 ACCESSIONS A31793; A61609; A26387; A35238; I51859 REFERENCE A31793 !$#authors Trask, R.V.; Strauss, A.W.; Billadello, J.J. !$#journal J. Biol. Chem. (1988) 263:17142-17149 !$#title Developmental regulation and tissue-specific expression of !1the human muscle creatine kinase gene. !$#cross-references MUID:89034220; PMID:2903158 !$#accession A31793 !'##molecule_type DNA !'##residues 1-381 ##label TRA !'##cross-references GB:M21494; NID:g180586; PIDN:AAA96609.1; !1PID:g180588 REFERENCE A61609 !$#authors Bailly, J.; MacKenzie, A.E.; Leblond, S.; Korneluk, R.G. !$#journal Hum. Genet. (1991) 86:457-462 !$#title Assessment of a creatine kinase isoform M defect as a cause !1of myotonic dystrophy and the characterization of two novel !1CKMM polymorphisms. !$#cross-references MUID:91200803; PMID:2016086 !$#accession A61609 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-268,'C',270-381 ##label BAI !'##note the authors translated the codon CAC for residue 269 as Cys REFERENCE A26387 !$#authors Perryman, M.B.; Kerner, S.A.; Bohlmeyer, T.J.; Roberts, R. !$#journal Biochem. Biophys. Res. Commun. (1986) 140:981-989 !$#title Isolation and sequence analysis of a full-length cDNA for !1human M creatine kinase. !$#cross-references MUID:87048887; PMID:3778496 !$#accession A26387 !'##molecule_type mRNA !'##residues 1-46,'I',48-129,'P',131-192,'Q',194-209,'H',211-214,'P', !1216-323,'A',325-381 ##label PER !'##cross-references GB:M14780; NID:g180575; PIDN:AAA52025.1; !1PID:g180576 !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing REFERENCE A35238 !$#authors Hamburg, R.J.; Friedman, D.L.; Olson, E.N.; Ma, T.S.; !1Cortez, M.D.; Goodman, C.; Puleo, P.R.; Perryman, M.B. !$#journal J. Biol. Chem. (1990) 265:6403-6409 !$#title Muscle creatine kinase isoenzyme expression in adult human !1brain. !$#cross-references MUID:90202921; PMID:1690725 !$#accession A35238 !'##molecule_type protein !'##residues 1-30 ##label HAM !'##experimental_source brain !'##note the presence of 1-Met is not explained REFERENCE I51859 !$#authors Nigro, J.M.; Schweinfest, C.W.; Rajkovic, A.; Pavlovic, J.; !1Jamal, S.; Dottin, R.P.; Hart, J.T.; Kamarck, M.E.; Rae, !1P.M.M.; Carty, M.D.; Martin-DeLeon, P. !$#journal Am. J. Hum. Genet. (1987) 40:115-125 !$#title cDNA cloning and mapping of the human creatine kinase M gene !1to 19q13. !$#cross-references MUID:87181666; PMID:3031982 !$#accession I51859 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 257-297,'X',299-327 ##label RES !'##cross-references GB:M16440; NID:g180577; PIDN:AAA52026.1; !1PID:g553231 GENETICS !$#gene GDB:CKM !'##cross-references GDB:120591; OMIM:123310 !$#map_position 19q13.2-19q13.2 !$#introns 65/1; 116/3; 161/1; 218/2; 259/3; 323/1 !$#note the first intron occurs before the initiator codon COMPLEX homodimer; heterodimer with chain B FUNCTION !$#description catalyzes the reversible phosphorylation of creatine with !1ATP to phosphocreatine and ADP !$#note with this enzyme phosphocreatine in muscle serves as a !1reservoir to regenerate ATP consumed during muscle !1contraction CLASSIFICATION #superfamily creatine kinase; creatine kinase repeat !1homology KEYWORDS dimer; muscle; phosphotransferase FEATURE !$2-381 #product creatine kinase chain M #status experimental !8#label MAT\ !$20-379 #domain creatine kinase repeat homology #label CKR\ !$283 #active_site Cys #status predicted SUMMARY #length 381 #molecular-weight 43101 #checksum 3362 SEQUENCE /// ENTRY KIRBCM #type complete TITLE creatine kinase (EC 2.7.3.2) chain M - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 30-Nov-1980 #sequence_revision 28-Aug-1985 #text_change 11-Jun-1999 ACCESSIONS A00673; I46695; A60810; A55838 REFERENCE A94034 !$#authors Pickering, L.; Pang, H.; Biemann, K.; Munro, H.; Schimmel, !1P. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:2310-2314 !$#title Two tissue-specific isozymes of creatine kinase have closely !1matched amino acid sequences. !$#cross-references MUID:85190487; PMID:3857581 !$#accession A00673 !'##molecule_type mRNA !'##residues 1-381 ##label PIC REFERENCE I46695 !$#authors Putney, S.D.; Herlihy, W.C.; Royal, N.; Pang, H.; Aposhian, !1H.V.; Pickering, L.; Belagaje, R.M.; Biemann, K.; Page, D.; !1Kuby, S.; Schimmel, P.R. !$#journal J. Biol. Chem. (1984) 259:14317-14320 !$#title Rabbit muscle creatine phosphokinase: cDNA cloning, primary !1structure, and detection of human homologues. !$#cross-references MUID:85054889; PMID:6094551 !$#accession I46695 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-381 ##label PUT !'##cross-references GB:K02831; NID:g164897; PIDN:AAA31205.1; !1PID:g164898 REFERENCE A60810 !$#authors Yuen, S.; Hunkapiller, M.W.; Wilson, K.J.; Yuan, P.M. !$#journal Anal. Biochem. (1988) 168:5-15 !$#title Applications of tandem microbore liquid chromatography and !1sodium dodecyl sulfate-polyacrylamide gel electrophoresis/ !1electroblotting in microsequence analysis. !$#cross-references MUID:88207910; PMID:3364717 !$#accession A60810 !'##molecule_type protein !'##residues 2-5,'XX',8-17 ##label YUE !'##experimental_source muscle REFERENCE A90252 !$#authors Atherton, R.S.; Laws, J.F.; Miles, B.J.; Thomson, A.R. !$#journal Biochem. J. (1970) 120:589-600 !$#title Brain adenosine 5'-triphosphate-creatine phosphotransferase. !1Purification, thiol group reactivity and the amino acid !1sequence around the reactive thiol groups. !$#cross-references MUID:71110294; PMID:5499971 !$#contents annotation; active site REFERENCE A55838 !$#authors Olcott, M.C.; Bradley, M.L.; Haley, B.E. !$#journal Biochemistry (1994) 33:11935-11941 !$#title Photoaffinity labeling of creatine kinase with 2-azido- and !18-azidoadenosine triphosphate: identification of two !1peptides from the ATP-binding domain. !$#cross-references MUID:95001905; PMID:7918412 !$#accession A55838 !'##molecule_type protein !'##residues 237-242;267-275,'X',277-282,'X',284-291,'X' ##label OLC COMMENT The active enzyme is a dimer of identical or nonidentical !1chains, with MM being the major form in skeletal muscle and !1myocardium, MB existing in myocardium, and BB existing in !1many tissues, especially brain. The sequences of M and B !1chains are about 80% identical. CLASSIFICATION #superfamily creatine kinase; creatine kinase repeat !1homology KEYWORDS ATP; phosphotransferase FEATURE !$20-379 #domain creatine kinase repeat homology #label CKR\ !$283 #active_site Cys #status experimental SUMMARY #length 381 #molecular-weight 43112 #checksum 1425 SEQUENCE /// ENTRY KIRTCM #type complete TITLE creatine kinase (EC 2.7.3.2) chain M - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 01-Dec-2000 ACCESSIONS A00674; I53407 REFERENCE A00674 !$#authors Benfield, P.A.; Zivin, R.A.; Miller, L.S.; Sowder, R.; !1Smythers, G.W.; Henderson, L.; Oroszlan, S.; Pearson, M.L. !$#journal J. Biol. Chem. (1984) 259:14979-14984 !$#title Isolation and sequence analysis of cDNA clones coding for !1rat skeletal muscle creatine kinase. !$#cross-references MUID:85054996; PMID:6209281 !$#accession A00674 !'##molecule_type mRNA !'##residues 1-381 ##label BEN !'##cross-references GB:M10140; NID:g203477; PIDN:AAA40935.1; !1PID:g203478 !'##experimental_source strain F344/N Fisher !'##note most of the sequence was confirmed by protein sequencing REFERENCE I53407 !$#authors Benfield, P.A.; Zivin, R.A.; Shearman, C.W.; Graf, D.; !1Henderson, L.; Oroszlan, S.; Pearson, M.L. !$#journal Exp. Biol. Med. (1984) 9:187-194 !$#title The nucleotide sequence of rat muscle creatine kinase cDNA !1and ckm transcription during myogenesis in an RNA polymerase !1II mutant of L6 myoblasts. !$#accession I53407 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 'N',88-381 ##label RES !'##cross-references GB:M14864; NID:g203479; PIDN:AAA40936.1; !1PID:g203480 CLASSIFICATION #superfamily creatine kinase; creatine kinase repeat !1homology KEYWORDS phosphotransferase FEATURE !$20-379 #domain creatine kinase repeat homology #label CKR\ !$283 #active_site Cys #status predicted SUMMARY #length 381 #molecular-weight 43019 #checksum 869 SEQUENCE /// ENTRY KICHCM #type complete TITLE creatine kinase (EC 2.7.3.2) chain M - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 11-Jun-1999 ACCESSIONS A00675; I50200 REFERENCE A00675 !$#authors Kwiatkowski, R.W.; Schweinfest, C.W.; Dottin, R.P. !$#journal Nucleic Acids Res. (1984) 12:6925-6934 !$#title Molecular cloning and the complete nucleotide sequence of !1the creatine kinase-M cDNA from chicken. !$#cross-references MUID:85014143; PMID:6091045 !$#accession A00675 !'##molecule_type mRNA !'##residues 1-381 ##label KWI !'##cross-references GB:X00954; GB:M35380; NID:g63552; PIDN:CAA25465.1; !1PID:g63553 REFERENCE I50200 !$#authors Ordahl, C.P.; Evans, G.L.; Cooper, T.A.; Kunz, G.; Perriard, !1J. !$#journal J. Biol. Chem. (1984) 259:15224-15227 !$#title Complete cDNA-derived amino acid sequence of chick muscle !1creatine kinase. !$#cross-references MUID:85080008; PMID:6096363 !$#accession I50200 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-381 ##label ORD !'##cross-references GB:M10012; NID:g211527; PIDN:AAA48689.1; !1PID:g211528 CLASSIFICATION #superfamily creatine kinase; creatine kinase repeat !1homology KEYWORDS phosphotransferase FEATURE !$20-379 #domain creatine kinase repeat homology #label CKR\ !$283 #active_site Cys #status predicted SUMMARY #length 381 #molecular-weight 43328 #checksum 65 SEQUENCE /// ENTRY KIRYCM #type complete TITLE creatine kinase (EC 2.7.3.2) chain M - marbled electric ray ORGANISM #formal_name Torpedo marmorata #common_name marbled electric ray DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 11-Jun-1999 ACCESSIONS A00676 REFERENCE A00676 !$#authors Giraudat, J.; Devillers-Thiery, A.; Perriard, J.C.; !1Changeux, J.P. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:7313-7317 !$#title Complete nucleotide sequence of Torpedo marmorata mRNA !1coding for the 43,000-dalton upsilon-2 protein: !1muscle-specific creatine kinase. !$#cross-references MUID:85063781; PMID:6095285 !$#accession A00676 !'##molecule_type mRNA !'##residues 1-381 ##label GIR !'##cross-references GB:M11508; NID:g213228; PIDN:AAA49277.1; !1PID:g213229 COMMENT This electric ray muscle-specific creatine kinase (MM !1isozyme) is isolated from the electric organ, which derives !1embryologically from skeletal muscle. It may be involved in !1the electrical discharge process. CLASSIFICATION #superfamily creatine kinase; creatine kinase repeat !1homology KEYWORDS phosphotransferase FEATURE !$20-379 #domain creatine kinase repeat homology #label CKR\ !$283 #active_site Cys #status predicted SUMMARY #length 381 #molecular-weight 42974 #checksum 9635 SEQUENCE /// ENTRY KIRYCT #type complete TITLE creatine kinase (EC 2.7.3.2) chain M - Pacific electric ray ORGANISM #formal_name Torpedo californica #common_name Pacific electric ray DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 11-Jun-1999 ACCESSIONS A00677 REFERENCE A00677 !$#authors West, B.L.; Babbitt, P.C.; Mendez, B.; Baxter, J.D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:7007-7011 !$#title Creatine kinase protein sequence encoded by a cDNA made from !1Torpedo californica electric organ mRNA. !$#cross-references MUID:85063721; PMID:6594677 !$#accession A00677 !'##molecule_type mRNA !'##residues 1-381 ##label WES !'##cross-references GB:M36427; NID:g213230; PIDN:AAA49278.1; !1PID:g213231 CLASSIFICATION #superfamily creatine kinase; creatine kinase repeat !1homology KEYWORDS phosphotransferase FEATURE !$20-379 #domain creatine kinase repeat homology #label CKR\ !$283 #active_site Cys #status predicted SUMMARY #length 381 #molecular-weight 42934 #checksum 8897 SEQUENCE /// ENTRY KIHUCB #type complete TITLE creatine kinase (EC 2.7.3.2) chain B - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 11-Jun-1999 ACCESSIONS S15935; A28364; A27174; A27034; I55544 REFERENCE S15935 !$#authors Mariman, E.C.M.; Schepens, J.T.G.; Wieringa, B. !$#journal Nucleic Acids Res. (1989) 17:6385 !$#title Complete nucleotide sequence of the human creatine kinase B !1gene. !$#cross-references MUID:89366665; PMID:2771648 !$#accession S15935 !'##status translation not shown !'##molecule_type DNA !'##residues 1-381 ##label MAR !'##cross-references EMBL:X15334; NID:g29962; PIDN:CAA33389.1; !1PID:g29963 REFERENCE A28364 !$#authors Daouk, G.H.; Kaddurah-Daouk, R.; Putney, S.; Kingston, R.; !1Schimmel, P. !$#journal J. Biol. Chem. (1988) 263:2442-2446 !$#title Isolation of a functional human gene for brain creatine !1kinase. !$#cross-references MUID:88115393; PMID:2828370 !$#accession A28364 !'##molecule_type DNA !'##residues 1-77,'G',79-97 ##label DAO !'##cross-references GB:J03531; GB:M22354; GB:M22355; GB:M22356; !1NID:g180558; PIDN:AAA52024.1; PID:g180560 !'##note the authors translated the codon AAC for residue 28 as Asp and !1GAG for residue 94 as Gln REFERENCE A27174 !$#authors Mariman, E.C.M.; Broers, C.A.M.; Claesen, C.A.A.; Tesser, !1G.I.; Wieringa, B. !$#journal Genomics (1987) 1:126-137 !$#title Structure and expression of the human creatine kinase B !1gene. !$#cross-references MUID:88085186; PMID:3692484 !$#accession A27174 !'##molecule_type mRNA !'##residues 1-381 ##label MAR2 !'##cross-references GB:J03036; GB:M21237; GB:M21238; GB:M21239; !1GB:M21240; GB:M21241; GB:M21242 REFERENCE A27034 !$#authors Villarreal-Levy, G.; Ma, T.S.; Kerner, S.A.; Roberts, R.; !1Perryman, M.B. !$#journal Biochem. Biophys. Res. Commun. (1987) 144:1116-1127 !$#title Human creatine kinase: isolation and sequence analysis of !1cDNA clones for the B subunit, development of subunit !1specific probes and determination of gene copy number. !$#cross-references MUID:87213302; PMID:3034271 !$#accession A27034 !'##molecule_type mRNA !'##residues 1-40,'DV',43-97,'RR',100-104,'DD',107-131,'A',133-214,'AR', !1217-295,'D',297-381 ##label VIL !'##cross-references GB:M16451; NID:g180571; PIDN:AAA76851.1; !1PID:g180572 REFERENCE I55544 !$#authors Kaye, F.J.; McBride, O.W.; Battey, J.F.; Gazdar, A.F.; !1Sausville, E.A. !$#journal J. Clin. Invest. (1987) 79:1412-1420 !$#title Human creatine kinase-B complementary DNA. Nucleotide !1sequence, gene expression in lung cancer, and chromosomal !1assignment to two distinct loci. !$#cross-references MUID:87195439; PMID:2883200 !$#accession I55544 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-77,'G',79-129,'G',131-381 ##label RES !'##cross-references GB:M16364; NID:g180554; PIDN:AAA76850.1; !1PID:g180555 GENETICS !$#gene GDB:CKB; CKBB !'##cross-references GDB:120590; OMIM:123280 !$#map_position 14q32.3-14q32.3 !$#introns 65/1; 116/3; 161/1; 218/2; 259/3; 323/1 COMPLEX homodimer; heterodimer with chain M FUNCTION !$#description catalyzes the reversible phosphorylation of creatine with !1ATP to phosphocreatine and ADP CLASSIFICATION #superfamily creatine kinase; creatine kinase repeat !1homology KEYWORDS brain; dimer; phosphotransferase FEATURE !$2-381 #product creatine kinase chain B #status predicted !8#label MAT\ !$20-379 #domain creatine kinase repeat homology #label CKR\ !$283 #active_site Cys #status predicted SUMMARY #length 381 #molecular-weight 42644 #checksum 8843 SEQUENCE /// ENTRY KIRTCB #type complete TITLE creatine kinase (EC 2.7.3.2) chain B - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 11-Jun-1999 ACCESSIONS A23980; JT0277; A35682; B35682 REFERENCE A23980 !$#authors Benfield, P.A.; Henderson, L.; Pearson, M.L. !$#journal Gene (1985) 39:263-267 !$#title Expression of a rat brain creatine kinase-beta-galactosidase !1fusion protein in Escherichia coli and derivation of the !1complete amino acid sequence of rat brain creatine kinase. !$#cross-references MUID:86137395; PMID:3005113 !$#accession A23980 !'##molecule_type mRNA !'##residues 1-381 ##label BEN !'##cross-references GB:M14400; NID:g203469; PIDN:AAA40930.1; !1PID:g203470 !'##note the authors translated the codon CAG for residue 58 as Glu REFERENCE JT0277 !$#authors Benfield, P.A.; Graf, D.; Korolkoff, P.N.; Hobson, G.; !1Pearson, M.L. !$#journal Gene (1988) 63:227-243 !$#title Isolation of four rat creatine kinase genes and !1identification of multiple potential promoter sequences !1within the rat brain creatine kinase promoter region. !$#cross-references MUID:88255869; PMID:2838389 !$#accession JT0277 !'##molecule_type DNA !'##residues 1-205,'A',207-381 ##label BE2 !'##cross-references GB:M18668; GB:M26669; NID:g203473; PIDN:AAA40932.1; !1PID:g203474 REFERENCE A35682 !$#authors Pentecost, B.T.; Mattheiss, L.; Dickerman, H.W.; Kumar, S.A. !$#journal Mol. Endocrinol. (1990) 4:1000-1010 !$#title Estrogen regulation of creatine kinase-B in the rat uterus. !$#cross-references MUID:91133434; PMID:2284002 !$#accession A35682 !'##molecule_type DNA !'##residues 1-17,'A',19-20 ##label PEN !'##cross-references GB:M57665; NID:g203471; PIDN:AAA40931.1; !1PID:g203472 !$#accession B35682 !'##molecule_type mRNA !'##residues 'A',19-182,'EQ',185-381 ##label PE2 COMMENT Creatine kinase catalyzes the reversible transfer of a !1phosphoryl group between ATP and creatine. GENETICS !$#gene ckb !$#introns 65/1; 116/3; 161/1; 218/2; 259/3; 323/1 CLASSIFICATION #superfamily creatine kinase; creatine kinase repeat !1homology KEYWORDS phosphotransferase FEATURE !$20-379 #domain creatine kinase repeat homology #label CKR\ !$283 #active_site Cys #status predicted SUMMARY #length 381 #molecular-weight 42712 #checksum 9387 SEQUENCE /// ENTRY KIRBCB #type complete TITLE creatine kinase (EC 2.7.3.2) chain B - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 11-Jun-1999 ACCESSIONS A00678 REFERENCE A94034 !$#authors Pickering, L.; Pang, H.; Biemann, K.; Munro, H.; Schimmel, !1P. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:2310-2314 !$#title Two tissue-specific isozymes of creatine kinase have closely !1matched amino acid sequences. !$#cross-references MUID:85190487; PMID:3857581 !$#accession A00678 !'##molecule_type mRNA !'##residues 1-381 ##label PIC !'##cross-references GB:M11306; NID:g164879; PIDN:AAA31201.1; !1PID:g164880 COMMENT The active enzyme is a dimer of identical or nonidentical !1chains, with MM being the major form in skeletal muscle and !1myocardium, MB existing in myocardium, and BB existing in !1many tissues, especially brain. The sequences of M and B !1chains are about 80% identical. CLASSIFICATION #superfamily creatine kinase; creatine kinase repeat !1homology KEYWORDS phosphotransferase FEATURE !$20-379 #domain creatine kinase repeat homology #label CKR\ !$283 #active_site Cys #status predicted SUMMARY #length 381 #molecular-weight 42663 #checksum 8256 SEQUENCE /// ENTRY AKLO #type complete TITLE arginine kinase (EC 2.7.3.3) - European lobster ORGANISM #formal_name Homarus gammarus #common_name European lobster DATE 03-May-1994 #sequence_revision 12-May-1994 #text_change 11-May-2000 ACCESSIONS A48590; A08880; A13048; A11475; B11475; A05221; S36043 REFERENCE A48590 !$#authors Dumas, C.; Camonis, J. !$#journal J. Biol. Chem. (1993) 268:21599-21605 !$#title Cloning and sequence analysis of the cDNA for arginine !1kinase of lobster muscle. !$#cross-references MUID:94012736; PMID:8408011 !$#accession A48590 !'##molecule_type mRNA !'##residues 1-356 ##label DUM !'##cross-references EMBL:X68703; NID:g311349; PIDN:CAA48654.1; !1PID:g311350 REFERENCE A05221 !$#authors Regnouf, F.; Kassab, R.; Debuire, B.; Richard, C.; Han, K.K. !$#journal Int. J. Pept. Protein Res. (1981) 17:143-155 !$#title Primary structure of lobster-muscle arginine kinase. !$#cross-references MUID:81191188; PMID:6262257 !$#contents annotation !$#note parts of this sequence, including the amino and carboxyl !1ends of the mature protein, were confirmed by protein !1sequencing but the peptides were not correctly aligned REFERENCE A08880 !$#authors Han, K.K.; Debuire, B.; Dautrevaux, M.; Biserte, G.; !1Fattoum, A.; Regnouf, F.; Kassab, R.; Pradel, L.A. !$#journal C. R. Acad. Sci. Hebd. Seances Acad. Sci. D (1972) !1274:324-326 !$#title Sequence des amino-acides d'un fragment obtenu par coupure !1de l'arginine-kinase de Homard (Homarus gammarus L.) par le !1bromure de cyanogene. !$#cross-references MUID:72128041; PMID:4622086 !$#accession A08880 !'##molecule_type protein !'##residues 132-133,'F',135,'YEAQYDCTPL',146-148 ##label HAN REFERENCE A13048 !$#authors Debuire, B.; Han, K.K.; Dautrevaux, M.; Biserte, G.; !1Regnouf, F.; Kassab, R. !$#journal J. Biochem. (1977) 81:611-619 !$#title Amino acid sequence of a cyanogen bromide fragment !1containing the two tryptophanyl residues of lobster arginine !1kinase (Homarus vulgaris). !$#cross-references MUID:77187746; PMID:16871 !$#accession A13048 !'##molecule_type protein !'##residues 174-182,'NN',185-191,'N',193-211,'DN',215,'V',217-218, !1'HKL',221,'P',222,'Q',224,'QNVKS',230-231 ##label DEB1 REFERENCE A91769 !$#authors Debuire, B.; Han, K.K.; Dautrevaux, M.; Biserte, G. !$#journal Int. J. Pept. Protein Res. (1975) 7:69-80 !$#title Isolation and characterization of the cyanogen bromide !1fragments of lobster arginine kinase (Homarus vulgaris). !$#cross-references MUID:75132674; PMID:164417 !$#accession A11475 !'##molecule_type protein !'##residues 234-235 ##label DEB2 !$#accession B11475 !'##molecule_type protein !'##residues 332-334,'Z',336,'Z',338-340,'Z',342 ##label DEB3 CLASSIFICATION #superfamily creatine kinase; creatine kinase repeat !1homology KEYWORDS acetylated amino end; muscle; phosphoprotein; !1phosphotransferase FEATURE !$2-356 #product arginine kinase #status experimental #label !8MAT\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental\ !$271 #active_site Cys (phosphocysteine intermediate) !8#status predicted SUMMARY #length 356 #molecular-weight 39983 #checksum 7917 SEQUENCE /// ENTRY A43736 #type complete TITLE creatine kinase (EC 2.7.3.2) - sea urchin (Strongylocentrotus purpuratus) ORGANISM #formal_name Strongylocentrotus purpuratus #common_name purple urchin DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A43736 REFERENCE A43736 !$#authors Wothe, D.D.; Charbonneau, H.; Shapiro, B.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:5203-5207 !$#title The phosphocreatine shuttle of sea urchin sperm: flagellar !1creatine kinase resulted from a gene triplication. !$#cross-references MUID:90311370; PMID:2367531 !$#accession A43736 !'##status preliminary !'##molecule_type mRNA !'##residues 1-1174 ##label WOT !'##cross-references EMBL:M33763; NID:g161472; PIDN:AAA30049.1; !1PID:g161473 CLASSIFICATION #superfamily flagellar creatine kinase; creatine kinase !1repeat homology KEYWORDS phosphotransferase FEATURE !$61-420 #domain creatine kinase repeat homology #label CKR1\ !$434-793 #domain creatine kinase repeat homology #label CKR2\ !$808-1167 #domain creatine kinase repeat homology #label CKR3 SUMMARY #length 1174 #molecular-weight 130868 #checksum 6889 SEQUENCE /// ENTRY WQECPI #type complete TITLE phosphotransferase system enzyme I (EC 2.7.3.9) [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 01-Mar-2002 ACCESSIONS B29785; B32345; B24035; H28181; G65015 REFERENCE A29785 !$#authors Saffen, D.W.; Presper, K.A.; Doering, T.L.; Roseman, S. !$#journal J. Biol. Chem. (1987) 262:16241-16253 !$#title Sugar transport by the bacterial phosphotransferase system. !1Molecular cloning and structural analysis of the Escherichia !1coli ptsH, ptsI, and crr genes. !$#cross-references MUID:88058992; PMID:2960675 !$#accession B29785 !'##molecule_type mRNA !'##residues 1-575 ##label SAF !'##cross-references GB:J02796; NID:g147397; PIDN:AAA24441.1; !1PID:g147399 REFERENCE A32345 !$#authors De Reuse, H.; Danchin, A. !$#journal J. Bacteriol. (1988) 170:3827-3837 !$#title The ptsH, ptsI, and crr genes of the Escherichia coli !1phosphoenolpyruvate-dependent phosphotransferase system: a !1complex operon with several modes of transcription. !$#cross-references MUID:88314869; PMID:2457575 !$#accession B32345 !'##molecule_type DNA !'##residues 1-575 ##label DER1 !'##cross-references GB:M21994; NID:g147261; PIDN:AAA24385.1; !1PID:g147264 REFERENCE A24035 !$#authors De Reuse, H.; Roy, A.; Danchin, A. !$#journal Gene (1985) 35:199-207 !$#title Analysis of the ptsH-ptsI-crr region in Escherichia coli !1K-12: nucleotide sequence of the ptsH gene. !$#cross-references MUID:85286351; PMID:2411636 !$#accession B24035 !'##molecule_type DNA !'##residues 1-56 ##label DER2 !'##cross-references GB:M10425; NID:g147394; PIDN:AAA24439.1; !1PID:g147396 REFERENCE A28181 !$#authors Byrne, C.R.; Monroe, R.S.; Ward, K.A.; Kredich, N.M. !$#journal J. Bacteriol. (1988) 170:3150-3157 !$#title DNA sequences of the cysK regions of Salmonella typhimurium !1and Escherichia coli and linkage of the cysK regions to !1ptsH. !$#cross-references MUID:88257033; PMID:3290198 !$#accession H28181 !'##status preliminary !'##molecule_type DNA !'##residues 1-54 ##label BYR !'##cross-references GB:M21451; NID:g145684; PIDN:AAA23656.1; !1PID:g145688 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65015 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-575 ##label BLAT !'##cross-references GB:AE000329; GB:U00096; NID:g2367137; !1PIDN:AAC75469.1; PID:g1788756; UWGP:b2416 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A68446 !$#authors Garrett, D.S.; Gronenborn, A.M.; Clore, G.M. !$#submission submitted to the Brookhaven Protein Data Bank, January 1997 !$#cross-references PDB:1EZA !$#contents annotation; conformation by (1)H-, (13)C-, and (15)N-NMR, !1residues 1-258,'R' REFERENCE A59022 !$#authors Garrett, D.S.; Seok, Y.J.; Liao, D.I.; Peterkofsky, A.; !1Gronenborn, A.M.; Clore, G.M. !$#journal Biochemistry (1997) 36:2517-2530 !$#title Solution structure of the 30 kDa N-terminal domain of enzyme !1I of the Escherichia coli phosphoenolpyruvate:sugar !1phosphotransferase system by multidimensional NMR. !$#cross-references MUID:97207064; PMID:9054557 !$#contents annotation; conformation by (1)H-, (13)C-, and (15)N-NMR REFERENCE A67861 !$#authors Liao, D.I.; Davies, D.R. !$#submission submitted to the Brookhaven Protein Data Bank, May 1996 !$#cross-references PDB:1ZYM !$#contents annotation; X-ray crystallography, 2.5 angstroms, residues !13-249 REFERENCE A59023 !$#authors Liao, D.I.; Silverton, E.; Seok, Y.J.; Lee, B.R.; !1Peterkofsky, A.; Davies, D.R. !$#journal Structure (1996) 4:861-872 !$#title The first step in sugar transport: crystal structure of the !1amino terminal domain of enzyme I of the E. coli PEP:sugar !1phosphotransferase system ad a model of the phosphotransfer !1complex with HPr. !$#cross-references MUID:96434331; PMID:8805571 !$#contents annotation; X-ray crystallography, 2.5 angstroms COMMENT This enzyme acts on the phosphotransferase system !1phosphohistidine-containing protein (see PIR:WQECPH). GENETICS !$#gene ptsI !$#map_position 52 min COMPLEX autophosphorylation requires dimerization FUNCTION !$#description catalyzes the phosphorylation of the phosphotransferase !1system phosphohistidine-containing protein by !1phosphoenolpyruvate CLASSIFICATION #superfamily phosphotransferase system enzyme I; !1phosphotransferase system enzyme I homology KEYWORDS homodimer; phosphohistidine; phosphoprotein; !1phosphotransferase; sugar transport system FEATURE !$2-561 #domain phosphotransferase system enzyme I homology !8#label PT1\ !$189 #active_site His (phosphohistidine intermediate) !8#status experimental SUMMARY #length 575 #molecular-weight 63561 #checksum 7091 SEQUENCE /// ENTRY WQEBPI #type complete TITLE phosphotransferase system enzyme I (EC 2.7.3.9) - Salmonella typhimurium CONTAINS phosphoenolpyruvate-protein phosphotransferase (EC 2.7.3.9) ORGANISM #formal_name Salmonella typhimurium DATE 30-Jun-1990 #sequence_revision 30-Sep-1992 #text_change 08-Sep-2000 ACCESSIONS A41027; D28181 REFERENCE A41027 !$#authors LiCalsi, C.; Crocenzi, T.S.; Freire, E.; Roseman, S. !$#journal J. Biol. Chem. (1991) 266:19519-19527 !$#title Sugar transport by the bacterial phosphotransferase system. !1Structural and thermodynamic domains of enzyme I of !1Salmonella typhimurium. !$#cross-references MUID:92011751; PMID:1655788 !$#accession A41027 !'##molecule_type DNA !'##residues 1-575 ##label LIC !'##cross-references GB:M76176; NID:g153956; PIDN:AAA27060.1; !1PID:g153957 !'##note part of this sequence was confirmed by protein sequencing REFERENCE A28181 !$#authors Byrne, C.R.; Monroe, R.S.; Ward, K.A.; Kredich, N.M. !$#journal J. Bacteriol. (1988) 170:3150-3157 !$#title DNA sequences of the cysK regions of Salmonella typhimurium !1and Escherichia coli and linkage of the cysK regions to !1ptsH. !$#cross-references MUID:88257033; PMID:3290198 !$#accession D28181 !'##molecule_type DNA !'##residues 1-299 ##label BYR !'##cross-references GB:M76176; NID:g153956; PIDN:AAA27060.1; !1PID:g153957 COMMENT The phosphoenolpyruvate-glycose phosphotransferase system !1(PTS) comprises two general proteins (Hpr and enzyme I) and !1a sugar-specific complex (enzyme II), which consists of a !1pair of factors (II-A/II-B or III/II), lipid, and divalent !1cation. The phosphoryl group is transferred from !1phosphoenolpyruvate to enzyme I, to Hpr, to II-A (or III), !1to II-B (or II), and finally to the sugar substrate as it !1crosses the cell membrane. GENETICS !$#gene ptsI !$#map_position 49 min CLASSIFICATION #superfamily phosphotransferase system enzyme I; !1phosphotransferase system enzyme I homology KEYWORDS phosphoprotein; phosphotransferase; sugar transport system FEATURE !$2-561 #domain phosphotransferase system enzyme I homology !8#label PT1 SUMMARY #length 575 #molecular-weight 63368 #checksum 5502 SEQUENCE /// ENTRY B42374 #type complete TITLE phosphotransferase system enzyme I (EC 2.7.3.9) - Staphylococcus carnosus ORGANISM #formal_name Staphylococcus carnosus DATE 10-Jul-1992 #sequence_revision 31-Jan-1997 #text_change 11-Jun-1999 ACCESSIONS B42374; S17075 REFERENCE A42374 !$#authors Kohlbrecher, D.; Eisermann, R.; Hengstenberg, W. !$#journal J. Bacteriol. (1992) 174:2208-2214 !$#title Staphylococcal phosphoenolpyruvate-dependent !1phosphotransferase system: molecular cloning and nucleotide !1sequence of the Staphylococcus carnosus ptsI gene and !1expression and complementation studies of the gene product. !$#cross-references MUID:92202148; PMID:1551842 !$#accession B42374 !'##status preliminary !'##molecule_type DNA !'##residues 1-574 ##label KOH !'##cross-references GB:M69050; NID:g153073; PIDN:AAA26664.1; !1PID:g153075 REFERENCE S15367 !$#authors Eisermann, R.; Fischer, R.; Kessler, U.; Neubauer, A.; !1Hengstenberg, W. !$#journal Eur. J. Biochem. (1991) 197:9-14 !$#title Staphylococcal phosphoenolpyruvate-dependent !1phosphotransferase system. Purification and protein !1sequencing of the Staphylococcus carnosus !1histidine-containing protein, and cloning and DNA sequencing !1of the ptsH gene. !$#cross-references MUID:91200066; PMID:1901791 !$#accession S17075 !'##status preliminary !'##molecule_type DNA !'##residues 1-90 ##label EIS !'##cross-references EMBL:X60766; NID:g46907; PIDN:CAA43176.1; !1PID:g46909 CLASSIFICATION #superfamily phosphotransferase system enzyme I; !1phosphotransferase system enzyme I homology KEYWORDS phosphoprotein; phosphotransferase; sugar transport system FEATURE !$5-563 #domain phosphotransferase system enzyme I homology !8#label PT1 SUMMARY #length 574 #molecular-weight 63369 #checksum 7968 SEQUENCE /// ENTRY JC1375 #type complete TITLE phosphotransferase system enzyme I (EC 2.7.3.9) - Streptococcus salivarius ALTERNATE_NAMES phosphoenolpyruvate-sugar phosphotransferase transport system enzyme I ORGANISM #formal_name Streptococcus salivarius DATE 30-Sep-1993 #sequence_revision 31-Jan-1997 #text_change 11-Jun-1999 ACCESSIONS JC1375 REFERENCE JC1375 !$#authors Gagnon, G.; Vadeboncoeur, C.; Levesque, R.C.; Frenette, M. !$#journal Gene (1992) 121:71-78 !$#title Cloning, sequencing and expression in Escherichia coli of !1the ptsI gene encoding enzyme I of the !1phosphoenolpyruvate:sugar phosphotransferase transport !1system from Streptococcus salivarius. !$#cross-references MUID:93051364; PMID:1427100 !$#accession JC1375 !'##molecule_type DNA !'##residues 1-577 ##label GAG !'##cross-references GB:M81756; NID:g153614; PIDN:AAA26873.1; !1PID:g153615 GENETICS !$#gene ptsI CLASSIFICATION #superfamily phosphotransferase system enzyme I; !1phosphotransferase system enzyme I homology KEYWORDS phosphoprotein; phosphotransferase; sugar transport system FEATURE !$5-565 #domain phosphotransferase system enzyme I homology !8#label PT1 SUMMARY #length 577 #molecular-weight 63046 #checksum 1035 SEQUENCE /// ENTRY C46238 #type complete TITLE phosphotransferase system enzyme I (EC 2.7.3.9) - Bacillus subtilis ALTERNATE_NAMES phosphoenolpyruvate-protein phosphotransferase ORGANISM #formal_name Bacillus subtilis DATE 31-Dec-1993 #sequence_revision 31-Jan-1997 #text_change 16-Jun-2000 ACCESSIONS C46238; A47084; S04178; G69683 REFERENCE A46238 !$#authors Reizer, J.; Hoischen, C.; Reizer, A.; Pham, T.N.; Saier Jr., !1M.H. !$#journal Protein Sci. (1993) 2:506-521 !$#title Sequence analyses and evolutionary relationships among the !1energy-coupling proteins Enzyme I and HPr of the bacterial !1phosphoenolpyruvate: sugar phosphotransferase system. !$#cross-references MUID:93299364; PMID:7686067 !$#accession C46238 !'##molecule_type DNA !'##residues 1-67,88-570 ##label REI1 !'##cross-references GB:M98359; NID:g1943574; PIDN:AAB52374.1; !1PID:g1943575 !'##note sequence extracted from NCBI backbone (NCBIN:134327, !1NCBIP:134330) REFERENCE A47084 !$#authors Fajardo-Cavazos, P.; Salazar, C.; Nicholson, W.L. !$#journal J. Bacteriol. (1993) 175:1735-1744 !$#title Molecular cloning and characterization of the Bacillus !1subtilis spore photoproduct lyase (spl) gene, which is !1involved in repair of UV radiation-induced DNA damage during !1spore germination. !$#cross-references MUID:93194799; PMID:8449881 !$#accession A47084 !'##molecule_type DNA !'##residues 398-570 ##label FAJ !'##cross-references GB:L08809; NID:g289267; PIDN:AAA22414.1; !1PID:g289268 !'##experimental_source strain 168 !'##note sequence extracted from NCBI backbone (NCBIN:127497, !1NCBIP:127499) REFERENCE S04174 !$#authors Gonzy-Treboul, G.; Zagorec, M.; Rain-Guion, M.C.; Steinmetz, !1M. !$#journal Mol. Microbiol. (1989) 3:103-112 !$#title Phosphoenolpyruvate:sugar phosphotransferase system of !1Bacillus subtilis: nucleotide sequence of ptsX, ptsH and the !15'-end of ptsI and evidence for a ptsHI operon. !$#cross-references MUID:89237891; PMID:2497294 !$#accession S04178 !'##molecule_type DNA !'##residues 1-102 ##label GON !'##cross-references EMBL:X12832; NID:g48679; PIDN:CAA31318.1; !1PID:g48683 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69683 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-67,88-570 ##label KUN !'##cross-references GB:Z99111; GB:AL009126; NID:g2633699; !1PIDN:CAB13264.1; PID:g2633762 !'##experimental_source strain 168 GENETICS !$#gene ptsI CLASSIFICATION #superfamily phosphotransferase system enzyme I; !1phosphotransferase system enzyme I homology KEYWORDS phosphoprotein; phosphotransferase; sugar transport system FEATURE !$4-561 #domain phosphotransferase system enzyme I homology !8#label PT1 SUMMARY #length 570 #molecular-weight 63079 #checksum 8196 SEQUENCE /// ENTRY D64247 #type complete TITLE phosphotransferase system enzyme I (EC 2.7.3.9) - Mycoplasma genitalium ALTERNATE_NAMES PEP-dependent HPr protein kinase phosphoryltransferase (ptsI) ORGANISM #formal_name Mycoplasma genitalium DATE 17-Nov-1995 #sequence_revision 31-Jan-1997 #text_change 07-Dec-1999 ACCESSIONS D64247; T09764 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession D64247 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-572 ##label TIGR !'##cross-references GB:U39729; GB:L43967; NID:g1046140; PID:g1046145; !1TIGR:MG429 !'##experimental_source strain G-37 REFERENCE Z16818 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.L.; Nguyen, !1D.T.; Utterback, T.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Venter, J.C. !$#submission submitted to the EMBL Data Library, October 1998 !$#accession T09764 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-572 ##label FRA !'##cross-references EMBL:U39725; NID:g3845017; PIDN:AAC72450.1; !1PID:g3845022 !'##experimental_source isolate G37 GENETICS !$#gene MG429 !$#genetic_code SGC3 CLASSIFICATION #superfamily phosphotransferase system enzyme I; !1phosphotransferase system enzyme I homology KEYWORDS phosphotransferase; sugar transport system FEATURE !$4-557 #domain phosphotransferase system enzyme I homology !8#label PT1 SUMMARY #length 572 #molecular-weight 64201 #checksum 5372 SEQUENCE /// ENTRY B38120 #type complete TITLE probable phosphotransferase system enzyme I (EC 2.7.3.9) phbI - Alcaligenes eutrophus ORGANISM #formal_name Alcaligenes eutrophus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B38120 REFERENCE A38120 !$#authors Pries, A.; Priefert, H.; Krueger, N.; Steinbuechel, A. !$#journal J. Bacteriol. (1991) 173:5843-5853 !$#title Identification and characterization of two Alcaligenes !1eutrophus gene loci relevant to the poly(beta-hydroxybutyric !1acid)-leaky phenotype which exhibit homology to ptsH and !1ptsI of Escherichia coli. !$#cross-references MUID:91358378; PMID:1653223 !$#accession B38120 !'##status preliminary !'##molecule_type DNA !'##residues 1-592 ##label PRI !'##cross-references GB:M69036; NID:g141961; PIDN:AAA21978.1; !1PID:g141963 CLASSIFICATION #superfamily phosphotransferase system enzyme I; !1phosphotransferase system enzyme I homology KEYWORDS phosphoprotein; phosphotransferase FEATURE !$5-576 #domain phosphotransferase system enzyme I homology !8#label PT1 SUMMARY #length 592 #molecular-weight 65207 #checksum 8444 SEQUENCE /// ENTRY QQBEJ5 #type complete TITLE phosphotransferase (EC 2.7.1.-) - human cytomegalovirus (strain AD169) ALTERNATE_NAMES HSRF3 protein ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 #note host Homo sapiens (man) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 11-Jun-1999 ACCESSIONS S09862 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09862 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-707 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35333.1; !1PID:g1780876 !'##note possible protein-coding frames are given !'##note the DNA sequence was submitted to EMBL, December 1989, in !1computer-readable form CLASSIFICATION #superfamily human cytomegalovirus phosphotransferase KEYWORDS phosphotransferase SUMMARY #length 707 #molecular-weight 78232 #checksum 7950 SEQUENCE /// ENTRY QQBEH5 #type complete TITLE phosphotransferase (EC 2.7.1.-) - human herpesvirus 6 (strain Uganda-1102) ORGANISM #formal_name human herpesvirus 6 DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 11-Jun-1999 ACCESSIONS E36769 REFERENCE A33560 !$#authors Lawrence, G.L.; Chee, M.; Craxton, M.A.; Gompels, U.A.; !1Honess, R.W.; Barrell, B.G. !$#journal J. Virol. (1990) 64:287-299 !$#title Human herpesvirus 6 is closely related to human !1cytomegalovirus. !$#cross-references MUID:90080132; PMID:2152817 !$#accession E36769 !'##molecule_type DNA !'##residues 1-562 ##label LAW !'##cross-references GB:M68963; GB:M28243; NID:g325494; PIDN:AAA65577.1; !1PID:g325509 CLASSIFICATION #superfamily human cytomegalovirus phosphotransferase KEYWORDS phosphotransferase SUMMARY #length 562 #molecular-weight 63717 #checksum 1920 SEQUENCE /// ENTRY KIHUA #type complete TITLE adenylate kinase (EC 2.7.4.3) 1 - human (tentative sequence) ALTERNATE_NAMES myokinase ORGANISM #formal_name Homo sapiens #common_name man DATE 23-Oct-1981 #sequence_revision 23-Oct-1981 #text_change 31-Mar-2000 ACCESSIONS A33508; A00679 REFERENCE A33508 !$#authors Matsuura, S.; Igarashi, M.; Tanizawa, Y.; Yamada, M.; Kishi, !1F.; Kajii, T.; Fujii, H.; Miwa, S.; Sakurai, M.; Nakazawa, !1A. !$#journal J. Biol. Chem. (1989) 264:10148-10155 !$#title Human adenylate kinase deficiency associated with hemolytic !1anemia. A single base substitution affecting solubility and !1catalytic activity of the cytosolic adenylate kinase. !$#cross-references MUID:89255503; PMID:2542324 !$#accession A33508 !'##molecule_type DNA !'##residues 1-126,'Q',128-180,'S',182-194 ##label MAT !'##cross-references GB:J04809; NID:g178321; PIDN:AAA51686.1; !1PID:g178322 !'##note this sequence may be a less common allele found in Japanese !1populations REFERENCE A00679 !$#authors von Zabern, I.; Wittmann-Liebold, B.; Untucht-Grau, R.; !1Schirmer, R.H.; Pai, E.F. !$#journal Eur. J. Biochem. (1976) 68:281-290 !$#title Primary and tertiary structure of the principal human !1adenylate kinase. !$#cross-references MUID:77003085; PMID:183954 !$#accession A00679 !'##molecule_type protein !'##residues 1-194 ##label VON !'##experimental_source skeletal muscle !'##note this sequence represents the AK1(1) allele, the most common of !1at least five alleles COMMENT This form of the enzyme is expressed in the cytoplasm of !1skeletal muscle and brain cells, and erythrocytes. COMMENT A deficiency of this enzyme in erythrocytes is a cause of !1hemolytic anemia. GENETICS !$#gene GDB:AK1 !'##cross-references GDB:119664; OMIM:103000 !$#map_position 9q34.1-9q34.1 !$#introns 3/1; 15/1; 69/3; 108/3; 172/3 !$#note the first intron occurs before the initiator codon COMPLEX monomer FUNCTION !$#description catalyzes the reversible phosphorylation of adenine !1monophosphate with adenosine triphosphate to form two !1adenosine diphosphates in the presence of magnesium CLASSIFICATION #superfamily adenylate kinase KEYWORDS acetylated amino end; ATP; P-loop; phosphotransferase FEATURE !$15-22 #region nucleotide-binding motif A (P-loop) #status !8atypical\ !$89-94 #region nucleotide-binding motif B #status atypical\ !$1 #modified_site acetylated amino end (Met) #status !8experimental\ !$25,36,38,93 #active_site Cys, His, Ser, Asp #status predicted\ !$44,128,138,149 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 194 #molecular-weight 21705 #checksum 1665 SEQUENCE /// ENTRY KIRBA #type complete TITLE adenylate kinase (EC 2.7.4.3) - rabbit ALTERNATE_NAMES ATP-AMP transphosphorylase; myokinase ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 24-Jul-1997 ACCESSIONS A00680 REFERENCE A00680 !$#authors Kuby, S.A.; Palmieri, R.H.; Frischat, A.; Fischer, A.H.; Wu, !1L.H.; Maland, L.; Manship, M. !$#journal Biochemistry (1984) 23:2393-2399 !$#title Studies on adenosine triphosphate transphosphorylases. Amino !1acid sequence of rabbit muscle ATP-AMP transphosphorylase. !$#cross-references MUID:85000428; PMID:6089869 !$#accession A00680 !'##molecule_type protein !'##residues 1-194 ##label KUB FUNCTION !$#description catalyzes the reversible phosphorylation of adenine !1monophosphate with adenosine triphosphate to form two !1adenosine diphosphates in the presence of magnesium CLASSIFICATION #superfamily adenylate kinase KEYWORDS acetylated amino end; ATP; P-loop; phosphotransferase FEATURE !$15-22 #region nucleotide-binding motif A (P-loop) #status !8atypical\ !$89-94 #region nucleotide-binding motif B #status atypical\ !$1 #modified_site acetylated amino end (Met) #status !8experimental\ !$25,36,38,93 #active_site Cys, His, Ser, Asp #status predicted\ !$44,128,138,149 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 194 #molecular-weight 21638 #checksum 9723 SEQUENCE /// ENTRY KIBOA #type complete TITLE adenylate kinase (EC 2.7.4.3) - bovine ALTERNATE_NAMES ATP-AMP transphosphorylase; myokinase ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 24-Jul-1997 ACCESSIONS A00681 REFERENCE A00681 !$#authors Kuby, S.A. !$#citation unpublished results, cited by Kuby, S.A., Palmieri, R.H., !1Frischat, A., Fische, A.H., Wu, L.H., Maland, L., and !1Manship, M., Biochemistry 23, 2393-2399, 1984 !$#accession A00681 !'##molecule_type protein !'##residues 1-194 ##label KUB FUNCTION !$#description catalyzes the reversible phosphorylation of adenine !1monophosphate with adenosine triphosphate to form two !1adenosine diphosphates in the presence of magnesium CLASSIFICATION #superfamily adenylate kinase KEYWORDS acetylated amino end; ATP; P-loop; phosphotransferase FEATURE !$15-22 #region nucleotide-binding motif A (P-loop) #status !8atypical\ !$89-94 #region nucleotide-binding motif B #status atypical\ !$1 #modified_site acetylated amino end (Met) #status !8experimental\ !$25,36,38,93 #active_site Cys, His, Ser, Asp #status predicted\ !$44,128,138,149 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 194 #molecular-weight 21659 #checksum 952 SEQUENCE /// ENTRY KIPGA #type complete TITLE adenylate kinase (EC 2.7.4.3) [validated] - pig ALTERNATE_NAMES myokinase ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 15-Sep-2000 ACCESSIONS A00682 REFERENCE A91218 !$#authors Heil, A.; Mueller, G.; Noda, L.; Pinder, T.; Schirmer, H.; !1Schirmer, I.; von Zabern, I. !$#journal Eur. J. Biochem. (1974) 43:131-144 !$#title The amino-acid sequence of porcine adenylate kinase from !1skeletal muscle. !$#cross-references MUID:74267087; PMID:4366177 !$#accession A00682 !'##molecule_type protein !'##residues 1-194 ##label HEI !'##experimental_source skeletal muscle REFERENCE A50563 !$#authors Schulz, G.E. !$#submission submitted to the Brookhaven Protein Data Bank, November 1987 !$#cross-references PDB:3ADK !$#contents annotation; X-ray crystallography, 2.1 angstroms, residues !11-194 REFERENCE A58438 !$#authors Dreusicke, D.; Karplus, P.A.; Schulz, G.E. !$#journal J. Mol. Biol. (1988) 199:359-371 !$#title Refined structure of porcine cytosolic adenylate kinase at !12.1 angstroms resolution. !$#cross-references MUID:88172480; PMID:2832612 !$#contents annotation; X-ray crystallography, 2.1 angstroms REFERENCE A93170 !$#authors Schulz, G.E.; Elzinga, M.; Marx, F.; Schirmer, R.H. !$#journal Nature (1974) 250:120-123 !$#title Three-dimensional structure of adenyl kinase. !$#cross-references MUID:74277369; PMID:4367210 !$#contents annotation; X-ray crystallography, 3.0 angstroms FUNCTION !$#description catalyzes the reversible phosphorylation of adenine !1monophosphate with adenosine triphosphate to form two !1adenosine diphosphates in the presence of magnesium CLASSIFICATION #superfamily adenylate kinase KEYWORDS acetylated amino end; ATP; P-loop; phosphotransferase; !1skeletal muscle FEATURE !$1-194 #product adenylate kinase #status experimental #label !8MAT\ !$15-22 #region nucleotide-binding motif A (P-loop) #status !8atypical\ !$89-94 #region nucleotide-binding motif B #status atypical\ !$1 #modified_site acetylated amino end (Met) #status !8experimental\ !$25,36,38,93 #active_site Cys, His, Ser, Asp #status predicted\ !$44,128,138,149 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 194 #molecular-weight 21639 #checksum 362 SEQUENCE /// ENTRY KICAC #type complete TITLE adenylate kinase (EC 2.7.4.3), cytosolic - common carp ORGANISM #formal_name Cyprinus carpio #common_name common carp DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 24-Jul-1997 ACCESSIONS S00394; A31220 REFERENCE S00394 !$#authors Reuner, C.; Hable, M.; Wilmanns, M.; Kiefer, E.; Schiltz, !1E.; Schulz, G.E. !$#journal Protein Seq. Data Anal. (1988) 1:335-343 !$#title Amino acid sequence and three-dimensional structure of !1cytosolic adenylate kinase from carp muscle. !$#cross-references MUID:89128814; PMID:2851785 !$#accession S00394 !'##molecule_type protein !'##residues 1-193 ##label REU FUNCTION !$#description catalyzes the reversible phosphorylation of adenine !1monophosphate with adenosine triphosphate to form two !1adenosine diphosphates in the presence of magnesium CLASSIFICATION #superfamily adenylate kinase KEYWORDS acetylated amino end; ATP; muscle; P-loop; !1phosphotransferase FEATURE !$14-21 #region nucleotide-binding motif A (P-loop) #status !8atypical\ !$88-93 #region nucleotide-binding motif B #status atypical\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$24,35,37,92 #active_site Cys, His, Ser, Asp #status predicted\ !$43,127,137,148 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 193 #molecular-weight 21357 #checksum 5839 SEQUENCE /// ENTRY KIHUA3 #type complete TITLE nucleoside-triphosphate-adenylate kinase (EC 2.7.4.10) 3 - human ALTERNATE_NAMES adenylate kinase 3 ORGANISM #formal_name Homo sapiens #common_name man DATE 17-Apr-1993 #sequence_revision 23-Mar-1995 #text_change 03-Jun-2002 ACCESSIONS A42820; S16380; S16381 REFERENCE A42820 !$#authors Xu, G.; O'Connell, P.; Stevens, J.; White, R. !$#journal Genomics (1992) 13:537-542 !$#title Characterization of human adenylate kinase 3 (AK3) cDNA and !1mapping of the AK3 pseudogene to an intron of the NF1 gene. !$#cross-references MUID:92347846; PMID:1639383 !$#accession A42820 !'##molecule_type mRNA !'##residues 1-223 ##label XUG !'##cross-references EMBL:X60673; NID:g28576; PIDN:CAA43088.1; !1PID:g28577; GB:S41502 !'##experimental_source frontal-cortex !'##note sequence extracted from NCBI backbone (NCBIN:109644, !1NCBIP:109645) COMMENT This isozyme is found in the mitochondrial matrix. GENETICS !$#gene GDB:AK3 !'##cross-references GDB:118988; OMIM:103030 !$#map_position 9pter-9p13 FUNCTION !$#description catalyzes the reversible phosphorylation of adenine !1monophosphate with nucleoside triphosphate to adenosine !1diphosphate and nucleoside diphosphate in the presence of !1magnesium !$#note GTP is preferred to ATP as a substrate CLASSIFICATION #superfamily adenylate kinase KEYWORDS ATP; mitochondrial matrix; mitochondrion; P-loop; !1phosphotransferase FEATURE !$12-19 #region nucleotide-binding motif A (P-loop) #status !8atypical\ !$85-89 #region nucleotide-binding motif B #status atypical\ !$22,33,35,88 #active_site Cys, His, Ser, Asp #status predicted SUMMARY #length 223 #molecular-weight 25268 #checksum 2955 SEQUENCE /// ENTRY KIBYA #type complete TITLE adenylate kinase (EC 2.7.4.3) [validated] - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES ATP-AMP transphosphorylase; protein YD9934.11; protein YDR226w ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 15-Sep-2000 ACCESSIONS S05799; A32539; S53987; A26855; A25411; S59433; S47475; !1S47934; S47949 REFERENCE S05799 !$#authors Magdolen, V.; Oechsner, U.; Bandlow, W. !$#journal Curr. Genet. (1987) 12:405-411 !$#title The complete nucleotide sequence of the gene coding for !1yeast adenylate kinase. !$#cross-references MUID:88194690; PMID:2834097 !$#accession S05799 !'##molecule_type DNA !'##residues 1-222 ##label MAG !'##cross-references EMBL:X06304; NID:g3356; PIDN:CAA29624.1; PID:g3357 REFERENCE A32539 !$#authors Konrad, M. !$#journal J. Biol. Chem. (1988) 263:19468-19474 !$#title Analysis and in vivo disruption of the gene coding for !1adenylate kinase (ADK1) in the yeast Saccharomyces !1cerevisiae. !$#cross-references MUID:89066766; PMID:2848829 !$#accession A32539 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-222 ##label KON !'##cross-references EMBL:M18455; NID:g171030; PIDN:AAA66319.1; !1PID:g171032 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1988 REFERENCE S53985 !$#authors Davies, C.J.; Hutchison III, C.A. !$#journal Nucleic Acids Res. (1995) 23:507-514 !$#title Insertion site specificity of the transposon Tn3. !$#cross-references MUID:95192063; PMID:7885847 !$#accession S53987 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-222 ##label DAV !'##cross-references GB:U13239; GB:L35344; GB:Z36548; NID:g532747; !1PIDN:AAC33143.1; PID:g532750 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 !'##note the cited EMBL accession number, U13239, is not in GenBank !1release 101.0 REFERENCE A26855 !$#authors Proba, K.; Tomasselli, A.G.; Nielsen, P.; Schulz, G.E. !$#journal Nucleic Acids Res. (1987) 15:7187 !$#title The cDNA sequence encoding cytosolic adenylate kinase from !1baker's yeast (Saccharomyces cerevisiae). !$#cross-references MUID:88015563; PMID:2821496 !$#accession A26855 !'##molecule_type mRNA !'##residues 1-138,'R',140-222 ##label PRO !'##cross-references EMBL:Y00413; NID:g3340; PIDN:CAA68471.1; PID:g3341 !'##note the authors translated the codon GAA for residues 115 and 153 !1as Gly and CGC for residue 139 as Ala REFERENCE A25411 !$#authors Tomasselli, A.G.; Mast, E.; Janes, W.; Schiltz, E. !$#journal Eur. J. Biochem. (1986) 155:111-119 !$#title The complete amino acid sequence of adenylate kinase from !1baker's yeast. !$#cross-references MUID:86136113; PMID:3004985 !$#accession A25411 !'##molecule_type protein !'##residues 3-221,'N' ##label TOM REFERENCE S59423 !$#authors Murphy, L.; Harris, D. !$#submission submitted to the EMBL Data Library, March 1995 !$#accession S59433 !'##molecule_type DNA !'##residues 1-222 ##label MUR !'##cross-references EMBL:Z48612; NID:g728671; PIDN:CAA88506.1; !1PID:g728682; GSPDB:GN00004; MIPS:YDR226w !'##experimental_source strain AB972 REFERENCE A65089 !$#authors Abele, U.; Schulz, G.E. !$#submission submitted to the Brookhaven Protein Data Bank, July 1995 !$#cross-references PDB:1AKY !$#contents annotation; X-ray crystallography, 1.63 angstroms, residues !15-221,'N' REFERENCE A56505 !$#authors Abele, U.; Schulz, G.E. !$#journal Protein Sci. (1995) 4:1262-1271 !$#title High-resolution structures of adenylate kinase from yeast !1ligated with inhibitor Ap-5A, showing the pathway of !1phosphoryl transfer. !$#cross-references MUID:95400193; PMID:7670369 !$#contents annotation; X-ray crystallography, 1.63 angstroms GENETICS !$#gene SGD:ADK1; AKY1; MIPS:YDR226w !'##cross-references SGD:S0002634; MIPS:YDR226w !$#map_position 4R FUNCTION !$#description catalyzes the reversible phosphorylation of adenine !1monophosphate with adenosine triphosphate to form two !1adenosine diphosphates in the presence of magnesium CLASSIFICATION #superfamily adenylate kinase KEYWORDS acetylated amino end; ATP; P-loop; phosphotransferase FEATURE !$3-222 #product adenylate kinase #status experimental #label !8MAT\ !$13-20 #region nucleotide-binding motif A (P-loop) #status !8atypical\ !$87-92 #region nucleotide-binding motif B #status atypical\ !$3 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental\ !$34,91 #active_site His, Asp #status predicted SUMMARY #length 222 #molecular-weight 24255 #checksum 2582 SEQUENCE /// ENTRY KIECA #type complete TITLE adenylate kinase (EC 2.7.4.3) [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES ATP-AMP transphosphorylase ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 01-Mar-2002 ACCESSIONS A24275; S25734; A64778 REFERENCE A24275 !$#authors Brune, M.; Schumann, R.; Wittinghofer, F. !$#journal Nucleic Acids Res. (1985) 13:7139-7151 !$#title Cloning and sequencing of the adenylate kinase gene (adk) of !1Escherichia coli. !$#cross-references MUID:86041903; PMID:2997739 !$#accession A24275 !'##molecule_type DNA !'##residues 1-214 ##label BRU !'##cross-references GB:X03038; NID:g40903; PIDN:CAA26840.1; PID:g40904 !'##experimental_source K-12 REFERENCE S16118 !$#authors Miyamoto, K.; Nakahigashi, K.; Nishimura, K.; Inokuchi, H. !$#journal J. Mol. Biol. (1991) 219:393-398 !$#title Isolation and characterization of visible light-sensitive !1mutants of Escherichia coli K12. !$#cross-references MUID:91269316; PMID:2051480 !$#accession S25734 !'##status translation not shown !'##molecule_type DNA !'##residues 108-214 ##label MIY !'##cross-references EMBL:D90259; NID:g285769; PIDN:BAA14303.1; !1PID:g216516 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64778 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-214 ##label BLAT !'##cross-references GB:AE000153; GB:U00096; NID:g1786671; !1PIDN:AAC73576.1; PID:g1786680; UWGP:b0474 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A40519 !$#authors Rose, T.; Brune, M.; Wittinghofer, A.; Le Blay, K.; !1Surewicz, W.K.; Mantsch, H.H.; Barzu, O.; Gilles, A.M. !$#journal J. Biol. Chem. (1991) 266:10781-10786 !$#title Structural and catalytic properties of a deletion derivative !1(delta-133-157) of Escherichia coli adenylate kinase. !$#cross-references MUID:91250371; PMID:2040598 !$#contents annotation; deletion mutant characterization !$#note a construct lacking residues 133-157, corresponding to the !1insert found in large size variants of adenylate kinase such !1as those of Escherichia coli, yeast, and mitochondria, !1functioned at 7% of maximum levels for wild type enzyme REFERENCE A52276 !$#authors Berry, M.B.; Meador, B.; Bilderback, T.; Liang, P.; Glaser, !1M.; Phillips Jr., G.N. !$#submission submitted to the Brookhaven Protein Data Bank, February 1994 !$#cross-references PDB:1ANK !$#contents annotation; X-ray crystallography, 2.0 angstroms, residues !11-214 GENETICS !$#gene adk; plsA; dnaW !$#map_position 11 min FUNCTION !$#description catalyzes reversible phosphorylation of AMP with ATP to form !1two ADP !$#note magnesium required CLASSIFICATION #superfamily adenylate kinase KEYWORDS ATP; P-loop; phosphotransferase FEATURE !$7-14 #region nucleotide-binding motif A (P-loop) #status !8atypical\ !$80-85 #region nucleotide-binding motif B #status atypical\ !$30,84 #active_site Ser, Asp #status predicted SUMMARY #length 214 #molecular-weight 23586 #checksum 4470 SEQUENCE /// ENTRY KIBSAF #type complete TITLE adenylate kinase (EC 2.7.4.3) - Bacillus stearothermophilus ALTERNATE_NAMES ATP-AMP transphosphorylase ORGANISM #formal_name Bacillus stearothermophilus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 19-Jan-2001 ACCESSIONS B42196; S20226 REFERENCE A42196 !$#authors Glaser, P.; Presecan, E.; Delepierre, M.; Surewicz, W.K.; !1Mantsch, H.H.; Barzu, O.; Gilles, A.M. !$#journal Biochemistry (1992) 31:3038-3043 !$#title Zinc, a novel structural element found in the family of !1bacterial adenylate kinases. !$#cross-references MUID:92207915; PMID:1554691 !$#accession B42196 !'##molecule_type DNA !'##residues 1-217 ##label GLA !'##cross-references GB:M88104; NID:g142444; PIDN:AAA22205.1; !1PID:g142446 REFERENCE S20226 !$#authors Schiltz, E.; Buerkle, S.; Stiehle, H.; Mader, B.; Schulz, !1G.E. !$#submission submitted to the Protein Sequence Database, April 1992 !$#accession S20226 !'##molecule_type protein !'##residues 1-217 ##label SCH GENETICS !$#gene adk FUNCTION !$#description catalyzes reversible phosphorylation of AMP with ATP to form !1two ADP !$#note magnesium required CLASSIFICATION #superfamily adenylate kinase KEYWORDS ATP; P-loop; phosphotransferase; zinc finger FEATURE !$7-14 #region nucleotide-binding motif A (P-loop) #status !8atypical\ !$80-85 #region nucleotide-binding motif B #status atypical\ !$130-153 #region zinc finger CCCC motif\ !$28,30,84 #active_site His, Ser, Asp #status predicted\ !$150-153 #disulfide_bonds #status predicted SUMMARY #length 217 #molecular-weight 24143 #checksum 1295 SEQUENCE /// ENTRY KIPC #type complete TITLE adenylate kinase (EC 2.7.4.3) - Paracoccus denitrificans ORGANISM #formal_name Paracoccus denitrificans DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 28-Feb-1997 ACCESSIONS S02814; S04820 REFERENCE S02814 !$#authors Spuergin, P.; Tomasselli, A.G.; Schiltz, E. !$#journal Eur. J. Biochem. (1989) 179:621-628 !$#title The amino acid sequence of adenylate kinase from Paracoccus !1denitrificans and its relationship to mitochondrial and !1microbial adenylate kinases. !$#cross-references MUID:89153098; PMID:2537726 !$#accession S02814 !'##molecule_type protein !'##residues 1-217 ##label SPU FUNCTION !$#description catalyzes the reversible phosphorylation of adenine !1monophosphate with adenosine triphosphate to form two !1adenosine diphosphates in the presence of magnesium CLASSIFICATION #superfamily adenylate kinase KEYWORDS ATP; P-loop; phosphotransferase FEATURE !$8-15 #region nucleotide-binding motif A (P-loop) #status !8atypical\ !$79-84 #region nucleotide-binding motif B #status atypical\ !$31,83 #active_site Ser, Asp #status predicted\ !$129 #active_site His #status predicted\ !$149-152 #disulfide_bonds #status experimental SUMMARY #length 217 #molecular-weight 23634 #checksum 4927 SEQUENCE /// ENTRY KIYMC #type complete TITLE adenylate kinase (EC 2.7.4.3) - Mycoplasma capricolum ORGANISM #formal_name Mycoplasma capricolum DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 07-Dec-1999 ACCESSIONS S02851 REFERENCE S02830 !$#authors Ohkubo, S.; Muto, A.; Kawauchi, Y.; Yamao, F.; Osawa, S. !$#journal Mol. Gen. Genet. (1987) 210:314-322 !$#title The ribosomal protein gene cluster of Mycoplasma capricolum. !$#cross-references MUID:88142549; PMID:3481422 !$#accession S02851 !'##molecule_type DNA !'##residues 1-213 ##label OHK !'##cross-references EMBL:X06414; NID:g44207; PIDN:CAA29724.1; !1PID:g44229 GENETICS !$#gene adk !$#genetic_code SGC3 FUNCTION !$#description catalyzes the reversible phosphorylation of adenine !1monophosphate with adenosine triphosphate to form two !1adenosine diphosphates in the presence of magnesium CLASSIFICATION #superfamily adenylate kinase KEYWORDS ATP; P-loop; phosphotransferase FEATURE !$7-14 #region nucleotide-binding motif A (P-loop) #status !8atypical\ !$78-83 #region nucleotide-binding motif B #status atypical\ !$30,82 #active_site Ser, Asp #status predicted SUMMARY #length 213 #molecular-weight 24616 #checksum 5992 SEQUENCE /// ENTRY A33386 #type complete TITLE nucleoside-diphosphate kinase (EC 2.7.4.6) nm23-H1g - human ALTERNATE_NAMES nm23-H1g protein; probable metastatic suppressor nm23-H1 ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A33386; S45376; A39838; A43931; A56882; B43931; C43931 REFERENCE A33386 !$#authors Rosengard, A.M.; Krutzsch, H.C.; Shearn, A.; Biggs, J.R.; !1Barker, E.; Margulies, I.M.K.; King, C.R.; Liotta, L.A.; !1Steeg, P.S. !$#journal Nature (1989) 342:177-180 !$#title Reduced Nm23/Awd protein in tumour metastasis and aberrant !1Drosophila development. !$#cross-references MUID:90044071; PMID:2509941 !$#accession A33386 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-152 ##label ROS !'##cross-references GB:X75598; NID:g468541; PIDN:CAA53270.1; !1PID:g468542 REFERENCE S45376 !$#authors Dooley, S.; Seib, T.; Engel, M.; Theisinger, B.; Janz, H.; !1Piontek, K.; Zang, K.D.; Welter, C. !$#journal Hum. Genet. (1994) 93:63-66 !$#title Isolation and characterization of the human genomic locus !1coding for the putative metastasis control gene nm23-H1. !$#cross-references MUID:94095204; PMID:8270257 !$#accession S45376 !'##status preliminary !'##molecule_type DNA !'##residues 1-152 ##label DOO !'##cross-references EMBL:X75598; NID:g468541; PIDN:CAA53270.1; !1PID:g468542 REFERENCE A39838 !$#authors Gilles, A.M.; Presecan, E.; Vonica, A.; Lascu, I. !$#journal J. Biol. Chem. (1991) 266:8784-8789 !$#title Nucleoside diphosphate kinase from human erythrocytes. !1Structural characterization of the two polypeptide chains !1responsible for heterogeneity of the hexameric enzyme. !$#cross-references MUID:91224972; PMID:1851158 !$#accession A39838 !'##molecule_type protein !'##residues 1-152 ##label GIL REFERENCE A43931 !$#authors Hailat, N.; Keim, D.R.; Melhem, R.F.; Zhu, X.X.; Eckerskorn, !1C.; Brodeur, G.M.; Reynolds, C.P.; Seeger, R.C.; Lottspeich, !1F.; Strahler, J.R.; Hanash, S.M. !$#journal J. Clin. Invest. (1991) 88:341-345 !$#title High levels of p19/nm23 protein in neuroblastoma are !1associated with advanced stage disease and with N-myc gene !1amplification. !$#cross-references MUID:91277302; PMID:2056128 !$#accession A43931 !'##molecule_type protein !'##residues 7-18;40-49;89-94 ##label HAI !'##note sequence modified after extraction from NCBI backbone REFERENCE A56882 !$#authors Wang, L.; Patel, U.; Ghosh, L.; Chen, H.C.; Banerjee, S. !$#journal Cancer Res. (1993) 53:717-720 !$#title Mutation in the nm23 gene is associated with metastasis in !1colorectal cancer. !$#cross-references MUID:93153759; PMID:7916650 !$#accession A56882 !'##molecule_type mRNA !'##residues 1-86,'SAYKLAGTLYMAVILWRVQRRRSACGFTLRNW' ##label WAN !'##note mutant sequence shown (tumor 10) was extracted from NCBI !1backbone; wild type sequences were also found !'##note sequence extracted from NCBI backbone (NCBIN:124581, !1NCBIP:124584) GENETICS !$#gene GDB:NME1; nm23-H1 !'##cross-references GDB:127965; OMIM:156490 !$#map_position 17q21-17q22 !$#introns 43/1; 77/2; 114/2 CLASSIFICATION #superfamily nucleoside-diphosphate kinase KEYWORDS ATP binding; blocked amino end; hexamer; phosphohistidine; !1phosphoprotein; phosphotransferase FEATURE !$15-19 #region ATP binding #status predicted\ !$118 #active_site His (phosphohistidine intermediate) !8#status predicted SUMMARY #length 152 #molecular-weight 17149 #checksum 7241 SEQUENCE /// ENTRY T39099 #type complete TITLE nucleoside-diphosphate kinase (EC 2.7.4.6) [validated] - fission yeast (Schizosaccharomyces pombe) ORGANISM #formal_name Schizosaccharomyces pombe DATE 18-Feb-2000 #sequence_revision 18-Feb-2000 #text_change 16-Jun-2000 ACCESSIONS T39099; T43425 REFERENCE Z21827 !$#authors Wedler, H.; Duesterhoeft, A.; Wood, V.; Rajandream, M.A.; !1Barrell, B.G. !$#submission submitted to the EMBL Data Library, September 1999 !$#accession T39099 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-151 ##label WED !'##cross-references EMBL:AL117212; PIDN:CAB55286.1; GSPDB:GN00066; !1SPDB:SPAC806.07 !'##experimental_source strain 972h-; cosmid c806 REFERENCE Z16548 !$#authors Izumiya, H.; Yamamoto, M. !$#journal J. Biol. Chem. (1995) 270:27859-64 !$#title Cloning and functional analysis of the ndk1 gene encoding !1nucleoside-diphosphate kinase in Schizosaccharomyces pombe. !$#cross-references MUID:7499258; PMID:7499258 !$#accession T43425 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-151 ##label IZU !'##cross-references EMBL:D63678; PIDN:BAA09829.1 GENETICS !$#gene ndk1; SPAC806.07 !$#map_position 1 FUNCTION !$#description EC 2.7.4.6 [validated, MUID:96070921] CLASSIFICATION #superfamily nucleoside-diphosphate kinase KEYWORDS phosphotransferase SUMMARY #length 151 #molecular-weight 17012 #checksum 4199 SEQUENCE /// ENTRY F70157 #type complete TITLE nucleoside-diphosphate kinase (EC 2.7.4.6) ndk homolog - Lyme disease spirochete ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS F70157 REFERENCE A70100 !$#authors Fraser, C.M.; Casjens, S.; Huang, W.M.; Sutton, G.G.; !1Clayton, R.; Lathigra, R.; White, O.; Ketchum, K.A.; Dodson, !1R.; Hickey, E.K.; Gwinn, M.; Dougherty, B.; Tomb, J.F.; !1Fleischmann, R.D.; Richardson, D.; Peterson, J.; Kerlavage, !1A.R.; Quackenbush, J.; Salzberg, S.; Hanson, M.; Vugt, R.V.; !1Palmer, N.; Adams, M.D.; Gocayne, J.; Weidman, J.; !1Utterback, T.; Watthey, L.; McDonald, L.; Artiach, P.; !1Bowman, C.; Garland, S.; Fujii, C.; Cotton, M.D.; Horst, K.; !1Roberts, K.; Hatch, B.; Smith, H.O.; Venter, J.C. !$#journal Nature (1997) 390:580-586 !$#title Genomic sequence of a Lyme disease spirochaete, Borrelia !1burgdorferi. !$#cross-references MUID:98065943; PMID:9403685 !$#accession F70157 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-169 ##label KLE !'##cross-references GB:AE001151; GB:AE000783; NID:g2688371; !1PIDN:AAC66829.1; PID:g2688377; TIGR:BB0463 !'##experimental_source strain B31 CLASSIFICATION #superfamily nucleoside-diphosphate kinase KEYWORDS phosphotransferase SUMMARY #length 169 #molecular-weight 19377 #checksum 5749 SEQUENCE /// ENTRY F70437 #type complete TITLE nucleoside-diphosphate kinase (EC 2.7.4.6) - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS F70437 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession F70437 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-142 ##label AQF !'##cross-references GB:AE000746; NID:g2983925; PIDN:AAC07481.1; !1PID:g2983932; GB:AE000657 !'##experimental_source strain VF5 GENETICS !$#gene ndk CLASSIFICATION #superfamily nucleoside-diphosphate kinase KEYWORDS ATP binding; hexamer; phosphohistidine; phosphoprotein; !1phosphotransferase; pyrimidine nucleotide biosynthesis FEATURE !$14-18 #region ATP binding #status predicted\ !$120 #active_site His (phosphohistidine intermediate) !8#status predicted SUMMARY #length 142 #molecular-weight 15942 #checksum 8862 SEQUENCE /// ENTRY KIPGGU #type complete TITLE guanylate kinase (EC 2.7.4.8) - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 19-Jan-2001 ACCESSIONS S23776; S32545 REFERENCE S23776 !$#authors Zschocke, P.D.; Schiltz, E.; Schulz, G.E. !$#submission submitted to the Protein Sequence Database, September 1992 !$#accession S23776 !'##molecule_type protein !'##residues 1-197 ##label ZSC REFERENCE S32545 !$#authors Zschocke, P.D.; Schiltz, E.; Schulz, G.E. !$#journal Eur. J. Biochem. (1993) 213:263-269 !$#title Purification and sequence determination of guanylate kinase !1from pig brain. !$#cross-references MUID:93238695; PMID:8097461 !$#accession S32545 !'##status preliminary !'##molecule_type protein !'##residues 1-197 ##label ZS2 CLASSIFICATION #superfamily guanylate kinase; guanylate kinase homology KEYWORDS acetylated amino end; ATP; magnesium; monomer; nucleotide !1binding; P-loop; phosphotransferase FEATURE !$4-188 #domain guanylate kinase homology #label GKI\ !$10-17 #region nucleotide-binding motif A (P-loop)\ !$35-82 #region GMP binding #status predicted\ !$1 #modified_site acetylated amino end (Gly) #status !8experimental\ !$16 #binding_site ATP (Lys) #status predicted SUMMARY #length 197 #molecular-weight 21789 #checksum 2414 SEQUENCE /// ENTRY KIBYGU #type complete TITLE guanylate kinase (EC 2.7.4.8) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YDR454c ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1993 #sequence_revision 31-Dec-1993 #text_change 23-Mar-2001 ACCESSIONS A45097; S04818; S04819; S69733 REFERENCE A45097 !$#authors Konrad, M. !$#journal J. Biol. Chem. (1992) 267:25652-25655 !$#title Cloning and expression of the essential gene for guanylate !1kinase from yeast. !$#cross-references MUID:93100268; PMID:1334480 !$#accession A45097 !'##molecule_type DNA !'##residues 1-187 ##label KON !'##cross-references EMBL:L04683; NID:g171624; PIDN:AAA34657.1; !1PID:g171625 !'##note sequence extracted from NCBI backbone (NCBIP:120804) REFERENCE S04818 !$#authors Berger, A.; Schiltz, E.; Schulz, G.E. !$#journal Eur. J. Biochem. (1989) 184:433-443 !$#title Guanylate kinase from Saccharomyces cerevisiae. Isolation !1and characterization, crystallization and preliminary X-ray !1analysis, amino acid sequence and comparison with adenylate !1kinases. !$#cross-references MUID:90005494; PMID:2551688 !$#accession S04818 !'##molecule_type protein !'##residues 2-187 ##label BER1 REFERENCE S04819 !$#authors Berger, A.; Schiltz, E.; Schulz, G.E. !$#submission submitted to the Protein Sequence Database, July 1989 !$#accession S04819 !'##molecule_type protein !'##residues 2-187 ##label BER2 REFERENCE S21800 !$#authors Stehle, T.; Schulz, G.E. !$#journal J. Mol. Biol. (1992) 224:1127-1141 !$#title Refined structure of the complex between guanylate kinase !1and its substrate GMP at 2.0 A resolution. !$#cross-references MUID:92235848; PMID:1314905 !$#contents annotation; X-ray crystallography, 2.0 angstroms REFERENCE S69555 !$#authors Dietrich, F.S. !$#submission submitted to the EMBL Data Library, August 1995 !$#description The sequence of S. cerevisiae lambda 3641 and cosmids 9461, !19831, and 9410. !$#accession S69733 !'##molecule_type DNA !'##residues 1-187 ##label DIE !'##cross-references EMBL:U33007; NID:g927685; PIDN:AAB64881.1; !1PID:g927715; GSPDB:GN00004; MIPS:YDR454c GENETICS !$#gene SGD:GUK1; MIPS:YDR454c !'##cross-references SGD:S0002862; MIPS:YDR454c !$#map_position 4R CLASSIFICATION #superfamily guanylate kinase; guanylate kinase homology KEYWORDS acetylated amino end; ATP; magnesium; monomer; nucleotide !1binding; P-loop; phosphotransferase FEATURE !$2-187 #product guanylate kinase #status experimental #label !8MAT\ !$3-187 #domain guanylate kinase homology #label GKI\ !$9-16 #region nucleotide-binding motif A (P-loop)\ !$34-81 #region GMP binding #status experimental\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental\ !$15 #binding_site ATP (Lys) #status predicted SUMMARY #length 187 #molecular-weight 20637 #checksum 7601 SEQUENCE /// ENTRY KIECGU #type complete TITLE guanylate kinase (EC 2.7.4.8) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 01-Mar-2002 ACCESSIONS S43041; B65166; S24192 REFERENCE S43040 !$#authors Gentry, D.; Bengra, C.; Ikehara, K.; Cashel, M. !$#journal J. Biol. Chem. (1993) 268:14316-14321 !$#title Guanylate kinase of Escherichia coli K-12. !$#cross-references MUID:93300828; PMID:8390989 !$#accession S43041 !'##molecule_type DNA !'##residues 1-207 ##label GEN !'##cross-references EMBL:M84400; NID:g146228; PIDN:AAB88711.1; !1PID:g146230 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65166 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-207 ##label BLAT !'##cross-references GB:AE000442; GB:U00096; NID:g2367253; !1PIDN:AAC76672.1; PID:g1790080; UWGP:b3648 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene gmk CLASSIFICATION #superfamily guanylate kinase; guanylate kinase homology KEYWORDS ATP; magnesium; monomer; nucleotide binding; P-loop; !1phosphotransferase FEATURE !$5-187 #domain guanylate kinase homology #label GKI\ !$11-18 #region nucleotide-binding motif A (P-loop)\ !$37-84 #region GMP binding #status predicted\ !$17 #binding_site ATP (Lys) #status predicted SUMMARY #length 207 #molecular-weight 23592 #checksum 9303 SEQUENCE /// ENTRY I36854 #type complete TITLE guanylate kinase-related protein J10R - variola major virus (strains India-1967 and Bangladesh-1975) ALTERNATE_NAMES A57R protein homolog; hypothetical protein J8R ORGANISM #formal_name variola major virus DATE 24-Nov-1999 #sequence_revision 24-Nov-1999 #text_change 24-May-2001 ACCESSIONS I36854; S46852; T28599 REFERENCE A36859 !$#authors Blinov, V.M. !$#submission submitted to GenBank, November 1992 !$#accession I36854 !'##molecule_type DNA !'##residues 1-151 ##label BLI !'##cross-references GB:X69198; NID:g456758; PIDN:CAA49109.1; !1PID:g457059 !'##experimental_source strain India-1967 REFERENCE S46842 !$#authors Kolykhalov, A.A.; Blinov, V.M.; Frolov, I.V.; Totmenin, !1A.V.; Shchelkunov, S.N.; Sandakhchiev, L.S. !$#submission submitted to the EMBL Data Library, April 1992 !$#description Nucleotide sequence analysis of the region of variola virus !1HindIII-J genome fragment. !$#accession S46852 !'##molecule_type DNA !'##residues 1-83 ##label KOL !'##cross-references EMBL:X67118; NID:g516399; PIDN:CAA47553.1; !1PID:g516411 !'##experimental_source strain India-1967 REFERENCE Z20488 !$#authors Massung, R.F.; Esposito, J.J.; Liu, L.I.; Qi, J.; Utterback, !1T.R.; Knight, J.C.; Aubin, L.; Yuran, T.E.; Parsons, J.M.; !1Loparev, V.N. !$#journal Nature (1993) 366:748-751 !$#title Potential virulence determinants in terminal regions of !1variola smallpox virus genome. !$#cross-references MUID:94088747; PMID:8264798 !$#accession T28599 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-151 ##label MAS !'##cross-references EMBL:L22579; NID:g623595; PIDN:AAA60909.1; !1PID:g439078 !'##experimental_source strain Bangladesh-1975 COMMENT This protein lacks the amino end of the guanylate kinase !1homology domain, which includes the ATP-binding P-loop. GENETICS !$#gene J10R; J8R CLASSIFICATION #superfamily guanylate kinase; guanylate kinase homology SUMMARY #length 151 #molecular-weight 17445 #checksum 4420 SEQUENCE /// ENTRY KIBYT8 #type complete TITLE dTMP kinase (EC 2.7.4.9) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein J1715; protein YJR057w; start control protein CDC8; thymidylate kinase ORGANISM #formal_name Saccharomyces cerevisiae DATE 28-Aug-1985 #sequence_revision 19-Oct-1995 #text_change 19-Jan-2001 ACCESSIONS S57076; A00683; A26127; S23299; S71679; S23301 REFERENCE S57052 !$#authors Huang, M.E.; Chuat, J.C.; Galibert, F. !$#submission submitted to the Protein Sequence Database, September 1995 !$#accession S57076 !'##molecule_type DNA !'##residues 1-216 ##label MAN !'##cross-references EMBL:Z49557; NID:g1015724; PIDN:CAA89585.1; !1PID:g1015725; GSPDB:GN00010; MIPS:YJR057w REFERENCE A00683 !$#authors Jong, A.Y.S.; Kuo, C.L.; Campbell, J.L. !$#journal J. Biol. Chem. (1984) 259:11052-11059 !$#title The CDC8 gene of yeast encodes thymidylate kinase. !$#cross-references MUID:84289538; PMID:6088527 !$#accession A00683 !'##molecule_type DNA !'##residues 1-187,'D',189-216 ##label JON !'##cross-references EMBL:K02116; NID:g172985; PIDN:AAA35158.1; !1PID:g172986 REFERENCE A26127 !$#authors Rothstein, R.; Helms, C.; Rosenberg, N. !$#journal Mol. Cell. Biol. (1987) 7:1198-1207 !$#title Concerted deletions and inversions are caused by mitotic !1recombination between delta sequences in Saccharomyces !1cerevisiae. !$#cross-references MUID:87172788; PMID:3550432 !$#accession A26127 !'##molecule_type DNA !'##residues 1-108;134-216 ##label ROT !'##cross-references EMBL:M15468 REFERENCE S23299 !$#authors Birkenmeyer, L.G.; Hill, J.C.; Dumas, L.B. !$#journal Mol. Cell. Biol. (1984) 4:583-590 !$#title Saccharomyces cerevisiae CDC8 gene and its product. !$#cross-references MUID:84191140; PMID:6371491 !$#accession S23299 !'##molecule_type DNA !'##residues 1-216 ##label BIR1 !'##cross-references EMBL:K01783 !'##note the authors translated the codon TGG for residue 197 as Cys REFERENCE S71676 !$#authors Huang, M.E.; Manus, V.; Chuat, J.C.; Galibert, F. !$#journal Yeast (1996) 12:869-875 !$#title Analysis of a 62 kb DNA sequence of chromosome X reveals 36 !1open reading frames and a gene cluster with a counterpart on !1chromosome XI. !$#cross-references MUID:96437976; PMID:8840504 !$#accession S71679 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-216 ##label HUA !'##cross-references EMBL:L47993; NID:g1019675; PIDN:AAB39283.1; !1PID:g1019679 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1995 GENETICS !$#gene SGD:CDC8; MIPS:YJR057w !'##cross-references SGD:S0003818; MIPS:YJR057w !$#map_position 10R CLASSIFICATION #superfamily dTMP kinase KEYWORDS ATP; nucleotide binding; P-loop; phosphotransferase; !1pyrimidine deoxynucleotide metabolism FEATURE !$12-19 #region nucleotide-binding motif A (P-loop)\ !$18 #binding_site ATP (Lys) #status predicted SUMMARY #length 216 #molecular-weight 24687 #checksum 5194 SEQUENCE /// ENTRY KIVZ5W #type complete TITLE dTMP kinase (EC 2.7.4.9) - vaccinia virus ALTERNATE_NAMES A48R protein; SalF11R protein; thymidylate kinase ORGANISM #formal_name vaccinia virus #note host Homo sapiens (man) DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 19-Jan-2001 ACCESSIONS E42522; JQ1786; S06181; T37434 REFERENCE A42501 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:517-563 !$#title Appendix to "The complete DNA sequence of vaccinia virus". !$#accession E42522 !'##molecule_type DNA !'##residues 1-204 ##label GOE !'##cross-references GB:M35027; NID:g335317; PIDN:AAA48180.1; !1PID:g335528 !'##experimental_source strain Copenhagen REFERENCE JQ1767 !$#authors Smith, G.L.; Chan, Y.S.; Howard, S.T. !$#journal J. Gen. Virol. (1991) 72:1349-1376 !$#title Nucleotide sequence of 42kbp of vaccinia virus strain WR !1from near the right inverted terminal repeat. !$#cross-references MUID:91259063; PMID:2045793 !$#accession JQ1786 !'##molecule_type DNA !'##residues 1-204 ##label SMI !'##cross-references DDBJ:D11079; NID:g222717; PIDN:BAA01822.1; !1PID:g222737 !'##experimental_source strain strain WR REFERENCE A42531 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:247-266 !$#title The complete DNA sequence of vaccinia virus. !$#cross-references MUID:91021027; PMID:2219722 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given REFERENCE S06181 !$#authors Smith, G.L.; de Carlos, A.; Chan, Y.S. !$#journal Nucleic Acids Res. (1989) 17:7581-7590 !$#title Vaccinia virus encodes a thymidylate kinase gene: sequence !1and transcriptional mapping. !$#cross-references MUID:90016845; PMID:2552411 !$#accession S06181 !'##molecule_type DNA !'##residues 1-204 ##label SM2 !'##cross-references EMBL:X16259; NID:g62231; PIDN:CAA34345.1; !1PID:g62232 REFERENCE Z20877 !$#authors Antoine, G.; Scheiflinger, F.; Falkner, F.G.; Dorner, F. !$#submission submitted to the EMBL Data Library, March 1997 !$#description The complete genomic sequence of the Modified Vaccinia !1Ankara (MVA) strain. !$#accession T37434 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-204 ##label ANT !'##cross-references EMBL:U94848; PIDN:AAB96539.1 !'##experimental_source strain Ankara GENETICS !$#gene tmpK !$#note MVA161R CLASSIFICATION #superfamily dTMP kinase KEYWORDS ATP; nucleotide binding; nucleotide biosynthesis; P-loop; !1phosphotransferase FEATURE !$11-18 #region nucleotide-binding motif A (P-loop)\ !$17 #binding_site ATP (Lys) #status predicted SUMMARY #length 204 #molecular-weight 23218 #checksum 1687 SEQUENCE /// ENTRY KIHUR2 #type complete TITLE ribose-phosphate diphosphokinase (EC 2.7.6.1) catalytic chain II - human ALTERNATE_NAMES phosphoribosylpyrophosphate synthetase II ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 03-Jun-2002 ACCESSIONS S02778; S09668; S21227; S64002; A60257 REFERENCE S02778 !$#authors Iizasa, T.; Taira, M.; Shimada, H.; Ishijima, S.; Tatibana, !1M. !$#journal FEBS Lett. (1989) 244:47-50 !$#title Molecular cloning and sequencing of human cDNA for !1phosphoribosyl pyrophosphate synthetase subunit II. !$#cross-references MUID:89171273; PMID:2538352 !$#accession S02778 !'##molecule_type mRNA !'##residues 1-318 ##label IIZ !'##cross-references GB:Y00971; NID:g35699; PIDN:CAA68785.1; PID:g35700 REFERENCE S07587 !$#authors Roessler, B.J.; Bell, G.; Heidler, S.; Seino, S.; Becker, !1M.; Palella, T.D. !$#journal Nucleic Acids Res. (1990) 18:193 !$#title Cloning of two distinct copies of human !1phosphoribosylpyrophosphate synthetase cDNA. !$#cross-references MUID:90174926; PMID:2155397 !$#accession S09668 !'##molecule_type mRNA !'##residues 1-17,'KI',20-40,'C',42-81,'A',83-159,'S',161-162,'R', !1164-284,'S',286-318 ##label ROE !'##cross-references GB:X15331 REFERENCE S21093 !$#authors Ishizuka, T.; Iizasa, T.; Taira, M.; Ishijima, S.; Sonoda, !1T.; Shimada, H.; Nagatake, N.; Tatibana, M. !$#journal Biochim. Biophys. Acta (1992) 1130:139-148 !$#title Promoter regions of the human X-linked housekeeping genes !1PRPS1 and PRPS2 encoding phosphoribosylpyrophosphate !1synthetase subunit I and II isoforms. !$#cross-references MUID:92223087; PMID:1314091 !$#accession S21227 !'##molecule_type DNA !'##residues 1-102 ##label ISH REFERENCE S64002 !$#authors Ishizuka, T.; Iizasa, T.; Taira, M.; Ishijima, S.; Sonoda, !1T.; Shimada, H.; Nagatake, N.; Tatibana, M. !$#submission submitted to the EMBL Data Library, January 1994 !$#description Promoter regions of the human X-linked housekeeping genes !1PRPS1 and PRPS2 encoding phosphoribosylpyrophosphate !1synthetase subunit I and II isoforms. !$#accession S64002 !'##molecule_type DNA !'##residues 1-40 ##label ISW !'##cross-references EMBL:D28134; NID:g456707; PIDN:BAA05676.1; !1PID:g2160402 COMMENT This enzyme is utilized by both the de novo and the salvage !1pathways by which endogenously formed or exogenously added !1pyrimidine, purine, or pyridine bases are converted to the !1corresponding ribonucleoside monophosphates. Both inorganic !1phosphate and magnesium ion are required for enzyme !1stability and activity. COMMENT This enzyme exists in various tissues in many active forms; !1they are oligomeric complexes of nonidentical chains of !1different molecular weights. GENETICS !$#gene GDB:PRPS2 !'##cross-references GDB:120320; OMIM:311860 !$#map_position Xp22.3-Xp22.2 !$#introns 41/2 !$#note the list of introns may be incomplete CLASSIFICATION #superfamily ribose-phosphate pyrophosphokinase catalytic !1chain KEYWORDS alternative splicing; diphosphotransferase; magnesium; !1nucleotide biosynthesis FEATURE !$212-227 #region phosphoribosylpyrophosphate binding #status !8predicted\ !$128,130,139,143 #binding_site magnesium (Asp, His, Asp, Asp) #status !8predicted SUMMARY #length 318 #molecular-weight 34769 #checksum 148 SEQUENCE /// ENTRY KIRTR2 #type complete TITLE ribose-phosphate diphosphokinase (EC 2.7.6.1) catalytic chain II - rat ALTERNATE_NAMES phosphoribosylpyrophosphate synthetase II ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 03-Jun-2002 ACCESSIONS B29463; S06752; I70048 REFERENCE A29463 !$#authors Taira, M.; Ishijima, S.; Kita, K.; Yamada, K.; Iizasa, T.; !1Tatibana, M. !$#journal J. Biol. Chem. (1987) 262:14867-14870 !$#title Nucleotide and deduced amino acid sequences of two distinct !1cDNAs for rat phosphoribosylpyrophosphate synthetase. !$#cross-references MUID:88033052; PMID:2822704 !$#accession B29463 !'##molecule_type mRNA !'##residues 1-318 ##label TAI !'##cross-references EMBL:M17259; EMBL:J03471; NID:g206433; !1PIDN:AAA41964.1; PID:g206434 !'##experimental_source liver REFERENCE S06752 !$#authors Ishijima, S.; Taira, M.; Tatibana, M. !$#journal Nucleic Acids Res. (1989) 17:8859 !$#title Complete cDNA sequence of rat phosphoribosylpyrophosphate !1synthetase subunit II (PRS II). !$#cross-references MUID:90067854; PMID:2555778 !$#accession S06752 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-318 ##label ISH !'##cross-references EMBL:X16555; NID:g56978; PIDN:CAA34556.1; !1PID:g56979 COMMENT This enzyme is utilized by both the de novo and the salvage !1pathways by which endogenously formed or exogenously added !1pyrimidine, purine, or pyridine bases are converted to the !1corresponding ribonucleoside monophosphates. Both inorganic !1phosphate and magnesium ion are required for enzyme !1stability and activity. COMMENT This enzyme exists in various tissues in many active forms; !1they are oligomeric complexes of nonidentical chains of !1different molecular weights. Chain III is testis-specific. GENETICS !$#gene PRPS2 CLASSIFICATION #superfamily ribose-phosphate pyrophosphokinase catalytic !1chain KEYWORDS alternative splicing; diphosphotransferase; magnesium; !1nucleotide biosynthesis FEATURE !$212-227 #region phosphoribosylpyrophosphate binding #status !8predicted\ !$128,130,139,143 #binding_site magnesium (Asp, His, Asp, Asp) #status !8predicted SUMMARY #length 318 #molecular-weight 34813 #checksum 1308 SEQUENCE /// ENTRY KIHUR1 #type complete TITLE ribose-phosphate diphosphokinase (EC 2.7.6.1) catalytic chain I - human ALTERNATE_NAMES phosphoribosylpyrophosphate synthetase I ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 03-Jun-2002 ACCESSIONS JX0159; S07587; S21093 REFERENCE JX0159 !$#authors Sonoda, T.; Taira, M.; Ishijima, S.; Ishizuka, T.; Iizaka, !1T.; Tatibana, M. !$#journal J. Biochem. (1991) 109:361-364 !$#title Complete nucleotide sequence of human phosphoribosyl !1pyrophosphate synthetase subunit I (PRS I) cDNA and a !1comparison with human and rat PRPS gene families. !$#cross-references MUID:91324322; PMID:1650777 !$#accession JX0159 !'##molecule_type mRNA !'##residues 1-318 ##label SON !'##cross-references GB:D00860; NID:g220019; PIDN:BAA00733.1; !1PID:g220020 REFERENCE S07587 !$#authors Roessler, B.J.; Bell, G.; Heidler, S.; Seino, S.; Becker, !1M.; Palella, T.D. !$#journal Nucleic Acids Res. (1990) 18:193 !$#title Cloning of two distinct copies of human !1phosphoribosylpyrophosphate synthetase cDNA. !$#cross-references MUID:90174926; PMID:2155397 !$#accession S07587 !'##molecule_type mRNA !'##residues 1-318 ##label ROE !'##cross-references GB:X15331; GB:M25042; NID:g35701; PIDN:CAA33386.1; !1PID:g35702 REFERENCE S21093 !$#authors Ishizuka, T.; Iizasa, T.; Taira, M.; Ishijima, S.; Sonoda, !1T.; Shimada, H.; Nagatake, N.; Tatibana, M. !$#journal Biochim. Biophys. Acta (1992) 1130:139-148 !$#title Promoter regions of the human X-linked housekeeping genes !1PRPS1 and PRPS2 encoding phosphoribosylpyrophosphate !1synthetase subunit I and II isoforms. !$#cross-references MUID:92223087; PMID:1314091 !$#accession S21093 !'##status preliminary !'##molecule_type DNA !'##residues 1-41 ##label ISH COMMENT This enzyme is utilized by both the de novo and the salvage !1pathways by which endogenously formed or exogenously added !1pyrimidine, purine, or pyridine bases are converted to the !1corresponding ribonucleoside monophosphates. Both inorganic !1phosphate and magnesium ion are required for enzyme !1stability and activity. COMMENT This enzyme exists in various tissues in many active forms; !1they are oligomeric complexes of nonidentical chains of !1different molecular weights. Chain III is testis-specific. GENETICS !$#gene GDB:PRPS1 !'##cross-references GDB:120318; OMIM:311850 !$#map_position Xq22-Xq24 CLASSIFICATION #superfamily ribose-phosphate pyrophosphokinase catalytic !1chain KEYWORDS alternative splicing; diphosphotransferase; magnesium; !1nucleotide biosynthesis FEATURE !$212-227 #region phosphoribosylpyrophosphate binding #status !8predicted\ !$128,130,139,143 #binding_site magnesium (Asp, His, Asp, Asp) #status !8predicted SUMMARY #length 318 #molecular-weight 34834 #checksum 938 SEQUENCE /// ENTRY KIRTR1 #type complete TITLE ribose-phosphate diphosphokinase (EC 2.7.6.1) catalytic chain I - rat ALTERNATE_NAMES phosphoribosylpyrophosphate synthetase I ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 03-Jun-2002 ACCESSIONS A35465; A29463; S06753; A60260; I55270 REFERENCE A35465 !$#authors Shimada, H.; Taira, M.; Yamada, K.; Iizasa, T.; Tatibana, M. !$#journal J. Biol. Chem. (1990) 265:3956-3960 !$#title Structure of the rat PRPS1 gene encoding !1phosphoribosylpyrophosphate synthetase subunit I. !$#cross-references MUID:90154083; PMID:2154494 !$#accession A35465 !'##molecule_type DNA !'##residues 1-318 ##label SHI !'##cross-references GB:M31084; GB:J05251; NID:g206422; PIDN:AAA41959.1; !1PID:g206424 REFERENCE A29463 !$#authors Taira, M.; Ishijima, S.; Kita, K.; Yamada, K.; Iizasa, T.; !1Tatibana, M. !$#journal J. Biol. Chem. (1987) 262:14867-14870 !$#title Nucleotide and deduced amino acid sequences of two distinct !1cDNAs for rat phosphoribosylpyrophosphate synthetase. !$#cross-references MUID:88033052; PMID:2822704 !$#accession A29463 !'##molecule_type mRNA !'##residues 1-318 ##label TAI !'##cross-references EMBL:M29392; NID:g206425; PIDN:AAA41960.1; !1PID:g206426 !'##experimental_source liver REFERENCE S06753 !$#authors Ishijima, S.; Taira, M.; Tatibana, M. !$#journal Nucleic Acids Res. (1989) 17:8860 !$#title Complete cDNA sequence of rat phosphoribosylpyrophosphate !1synthetase subunit I (PRS I). !$#cross-references MUID:90067855; PMID:2555779 !$#accession S06753 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-318 ##label ISH !'##cross-references EMBL:X16554; NID:g56976; PIDN:CAA34555.1; !1PID:g56977 REFERENCE A60260 !$#authors Kita, K.; Otsuki, T.; Ishizuka, T.; Ishijima, S.; Tatibana, !1M. !$#journal Adv. Exp. Med. Biol. (1989) 253B:1-6 !$#title Rat liver phosphoribosylpyrophosphate synthetase: existence !1as heterogeneous aggregates and identification of the !1catalytic subunit. !$#cross-references MUID:90119164; PMID:2558528 !$#accession A60260 !'##molecule_type protein !'##residues 2-21 ##label KIT COMMENT This enzyme is utilized by both the de novo and the salvage !1pathways by which endogenously formed or exogenously added !1pyrimidine, purine, or pyridine bases are converted to the !1corresponding ribonucleoside monophosphates. Both inorganic !1phosphate and magnesium ion are required for enzyme !1stability and activity. COMMENT This enzyme exists in various tissues in many active forms; !1they are oligomeric complexes of nonidentical chains of !1different molecular weights. GENETICS !$#gene PRPS1 !$#introns 41/2; 102/3; 135/3; 177/2; 265/2 288/3 CLASSIFICATION #superfamily ribose-phosphate pyrophosphokinase catalytic !1chain KEYWORDS alternative splicing; diphosphotransferase; magnesium; !1nucleotide biosynthesis FEATURE !$212-227 #region phosphoribosylpyrophosphate binding #status !8predicted\ !$128,130,139,143 #binding_site magnesium (Asp, His, Asp, Asp) #status !8predicted SUMMARY #length 318 #molecular-weight 34834 #checksum 938 SEQUENCE /// ENTRY KIHUR3 #type complete TITLE ribose-phosphate diphosphokinase (EC 2.7.6.1) catalytic chain III - human ALTERNATE_NAMES phosphoribosylpyrophosphate synthetase III ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 03-Jun-2002 ACCESSIONS A37893 REFERENCE A37893 !$#authors Taira, M.; Iizasa, T.; Shimada, H.; Kudoh, J.; Shimizu, N.; !1Tatibana, M. !$#journal J. Biol. Chem. (1990) 265:16491-16497 !$#title A human testis-specific mRNA for phosphoribosylpyrophosphate !1synthetase that initiates from a non-AUG codon. !$#cross-references MUID:90375519; PMID:2168892 !$#accession A37893 !'##molecule_type mRNA !'##residues 1-318 ##label TAI !'##cross-references GB:J05608; GB:M57423; NID:g190521; PIDN:AAB59463.1; !1PID:g190522 COMMENT This enzyme is utilized by both the de novo and the salvage !1pathways by which endogenously formed or exogenously added !1pyrimidine, purine, or pyridine bases are converted to the !1corresponding ribonucleoside monophosphates. Both inorganic !1phosphate and magnesium ion are required for enzyme !1stability and activity. COMMENT This enzyme exists in various tissues in many active forms; !1they are oligomeric complexes of nonidentical chains of !1different molecular weights. Chain III is testis-specific. GENETICS !$#gene PRPS3 !$#start_codon ACG CLASSIFICATION #superfamily ribose-phosphate pyrophosphokinase catalytic !1chain KEYWORDS diphosphotransferase; magnesium; nucleotide biosynthesis; !1testis FEATURE !$212-227 #region phosphoribosylpyrophosphate binding #status !8predicted\ !$128,130,139,143 #binding_site magnesium (Asp, His, Asp, Asp) #status !8predicted SUMMARY #length 318 #molecular-weight 34839 #checksum 1836 SEQUENCE /// ENTRY KIEBRT #type complete TITLE ribose-phosphate diphosphokinase (EC 2.7.6.1) - Salmonella typhimurium ALTERNATE_NAMES phosphoribosylpyrophosphate synthetase ORGANISM #formal_name Salmonella typhimurium DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 03-Jun-2002 ACCESSIONS A30408; A37270 REFERENCE A30408 !$#authors Bower, S.G.; Hove-Jensen, B.; Switzer, R.L. !$#journal J. Bacteriol. (1988) 170:3243-3248 !$#title Structure of the gene encoding phosphoribosylpyrophosphate !1synthetase (prsA) in Salmonella typhimurium. !$#cross-references MUID:88257047; PMID:2838463 !$#accession A30408 !'##molecule_type DNA !'##residues 1-315 ##label BOW !'##cross-references GB:M19488; NID:g154284; PIDN:AAA27196.1; !1PID:g154285 REFERENCE A37270 !$#authors Harlow, K.W.; Switzer, R.L. !$#journal J. Biol. Chem. (1990) 265:5487-5493 !$#title Chemical modification of Salmonella typhimurium !1phosphoribosylpyrophosphate synthetase with 5'- !1(p-fluorosulfonylbenzoyl)adenosine. Identification of an !1active site histidine. !$#cross-references MUID:90202783; PMID:2156819 !$#accession A37270 !'##molecule_type protein !'##residues 2-32;74-116;125-295;313-315 ##label HAR GENETICS !$#gene prsA !$#map_position 35 min FUNCTION !$#description utilizes by both de novo and salvage pathways by which !1endogenously formed or exogenously added pyrimidine, purine, !1or pyridine bases are converted to the corresponding !1ribonucleoside monophosphates !$#pathway nucleotide biosynthesis !$#note inorganic phosphate and magnesium ion are required for !1enzyme stability and activity CLASSIFICATION #superfamily ribose-phosphate pyrophosphokinase catalytic !1chain KEYWORDS diphosphotransferase; magnesium; nucleotide biosynthesis FEATURE !$2-315 #product ribose-phosphate pyrophosphokinase #status !8experimental #label MAT\ !$216-228 #region phosphoribosylpyrophosphate binding\ !$129,131,140,144 #binding_site magnesium (Asp, His, Asp, Asp) #status !8predicted SUMMARY #length 315 #molecular-weight 34216 #checksum 3377 SEQUENCE /// ENTRY KIECRY #type complete TITLE ribose-phosphate diphosphokinase (EC 2.7.6.1) [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES phosphoribosylpyrophosphate synthetase ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 05-Dec-1997 #text_change 03-Jun-2002 ACCESSIONS D64867; A23528 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64867 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-315 ##label BLAT !'##cross-references GB:AE000219; GB:U00096; NID:g1787453; !1PIDN:AAC74291.1; PID:g1787458; UWGP:b1207 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A23528 !$#authors Hove-Jensen, B.; Harlow, K.W.; King, C.J.; Switzer, R.L. !$#journal J. Biol. Chem. (1986) 261:6765-6771 !$#title Phosphoribosylpyrophosphate synthetase of Escherichia coli: !1properties of the purified enzyme and primary structure of !1the prs gene. !$#cross-references MUID:86196114; PMID:3009477 !$#accession A23528 !'##molecule_type DNA !'##residues 1-126,'I',128-315 ##label HOV !'##cross-references GB:M13174; NID:g147378; PIDN:AAA24431.1; !1PID:g147379 GENETICS !$#gene prsA; prs !$#map_position 26 min !$#start_codon GTG FUNCTION !$#description EC 2.7.6.1 [validated, MUID:86196114] !$#note this enzyme is utilized by both the de novo and the salvage !1pathways by which endogenously formed or exogenously added !1pyrimidine, purine, or pyridine bases are converted to the !1corresponding ribonucleoside monophosphates !$#note both inorganic phosphate and magnesium ion are required for !1enzyme stability and activity CLASSIFICATION #superfamily ribose-phosphate pyrophosphokinase catalytic !1chain KEYWORDS diphosphotransferase; magnesium; nucleotide biosynthesis FEATURE !$2-315 #product ribose-phosphate pyrophosphokinase #status !8experimental #label MAT\ !$216-228 #region phosphoribosylpyrophosphate binding\ !$129,131,140,144 #binding_site magnesium (Asp, His, Asp, Asp) #status !8predicted SUMMARY #length 315 #molecular-weight 34218 #checksum 4317 SEQUENCE /// ENTRY KIBSRS #type complete TITLE ribose-phosphate diphosphokinase (EC 2.7.6.1) prs - Bacillus subtilis ALTERNATE_NAMES phosphoribosylpyrophosphate synthetase ORGANISM #formal_name Bacillus subtilis DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 03-Jun-2002 ACCESSIONS S05372; S66081; A69683 REFERENCE S05371 !$#authors Nilsson, D.; Hove-Jensen, B.; Arnvig, K. !$#journal Mol. Gen. Genet. (1989) 218:565-571 !$#title Primary structure of the tms and prs genes of Bacillus !1subtilis. !$#cross-references MUID:90066361; PMID:2555671 !$#accession S05372 !'##molecule_type DNA !'##residues 1-317 ##label NIL !'##cross-references GB:X16518; NID:g40216; PIDN:CAA34523.1; PID:g40218 REFERENCE S65967 !$#authors Ogasawara, N.; Nakai, S.; Yoshikawa, H. !$#journal DNA Res. (1994) 1:1-14 !$#title Systematic sequencing of the 180 kilobase region of the !1Bacillus subtilis chromosome containing the replication !1origin. !$#cross-references MUID:96051385; PMID:7584024 !$#accession S66081 !'##status preliminary !'##molecule_type DNA !'##residues 1-317 ##label OGA !'##cross-references EMBL:D26185; NID:g467326; PIDN:BAA05286.1; !1PID:g467440 !'##experimental_source strain 168, substrain Marburg REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69683 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-317 ##label KUN !'##cross-references GB:Z99104; GB:AL009126; NID:g2632267; !1PIDN:CAB11827.1; PID:g2632318 !'##experimental_source strain 168 GENETICS !$#gene prs FUNCTION !$#description catalyzes formation of phoshoribosylpyrophosphate from ATP !1and ribose 5-phosphate !$#pathway nucleotide biosynthesis !$#note inorganic phosphate and magnesium ion are required for !1enzyme stability and activity CLASSIFICATION #superfamily ribose-phosphate pyrophosphokinase catalytic !1chain KEYWORDS diphosphotransferase; magnesium; nucleotide biosynthesis FEATURE !$220-232 #region phosphoribosylpyrophosphate binding\ !$134,136,145,149 #binding_site magnesium (Asp, His, Asp, Asp) #status !8predicted SUMMARY #length 317 #molecular-weight 34868 #checksum 5525 SEQUENCE /// ENTRY JC5093 #type complete TITLE ribose-phosphate diphosphokinase (EC 2.7.6.1) - Bacillus caldolyticus ALTERNATE_NAMES phosphoribosylpyrophosphate synthetase; S-phospho-alpha-D-ribosyl 1-diphosphate synthase ORGANISM #formal_name Bacillus caldolyticus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS JC5093; S51152 REFERENCE JC5093 !$#authors Krath, B.N.; Hove-Jensen, B. !$#journal Gene (1996) 176:73-79 !$#title Bacillus caldolyticus prs gene encoding !1phosphoribosyl-diphosphate synthase. !$#cross-references MUID:97075912; PMID:8918235 !$#accession JC5093 !'##molecule_type DNA !'##residues 1-315 ##label KRA !'##cross-references EMBL:X83708; NID:g633145; PIDN:CAA58682.1; !1PID:g633147 !'##experimental_source DSM 405 !'##note the authors translated the codon CGT for residue 294 as Gly and !1CCG for residue 295 as Arg GENETICS !$#gene prs FUNCTION !$#description utilizes by both de novo and salvage pathways by which !1endogenously formed or exogenously added pyrimidine, purine, !1or pyridine bases are converted to the corresponding !1ribonucleoside monophosphates !$#pathway nucleotide biosynthesis !$#note inorganic phosphate and magnesium ion are required for !1enzyme stability and activity CLASSIFICATION #superfamily ribose-phosphate pyrophosphokinase catalytic !1chain KEYWORDS diphosphotransferase; magnesium; nucleotide biosynthesis FEATURE !$218-230 #region phosphoribosylpyrophosphate binding\ !$132,134,143,147 #binding_site magnesium (Asp, His, Asp, Asp) #status !8predicted SUMMARY #length 315 #molecular-weight 34533 #checksum 1126 SEQUENCE /// ENTRY A43325 #type complete TITLE 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase (EC 2.7.6.3) folK [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase; 7, 8-dihydro-6-hydroxymethylpterin-pyrophosphokinase; protein b0142 ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS A43325; S45211; F64737; A41380 REFERENCE A43325 !$#authors Talarico, T.L.; Ray, P.H.; Dev, I.K.; Merrill, B.M.; Dallas, !1W.S. !$#journal J. Bacteriol. (1992) 174:5971-5977 !$#title Cloning, sequence analysis, and overexpression of !1Escherichia coli folK, the gene coding for 7, !18-dihydro-6-hydroxymethylpterin-pyrophosphokinase. !$#cross-references MUID:92394901; PMID:1325970 !$#accession A43325 !'##molecule_type DNA !'##residues 1-159 ##label TAL !'##cross-references GB:L06495; NID:g146012; PIDN:AAB53446.1; !1PID:g146013 !'##experimental_source E. coli MC4100 !'##note sequence extracted from NCBI backbone (NCBIN:113052, !1NCBIP:113055) REFERENCE S45181 !$#authors Fujita, N. !$#submission submitted to the EMBL Data Library, January 1994 !$#accession S45211 !'##molecule_type DNA !'##residues 1-159 ##label FUJ !'##cross-references EMBL:D26562; NID:g473770; PIDN:BAA05590.1; !1PID:g473801 !'##experimental_source strain K-12, substrain W3110 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64737 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-159 ##label BLAT !'##cross-references GB:AE000123; GB:U00096; NID:g1786327; !1PIDN:AAC73253.1; PID:g1786335; UWGP:b0142 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A41380 !$#authors Talarico, T.L.; Dev, I.K.; Dallas, W.S.; Ferone, R.; Ray, !1P.H. !$#journal J. Bacteriol. (1991) 173:7029-7032 !$#title Purification and partial characterization of 7, !18-dihydro-6-hydroxymethylpterin-pyrophosphokinase and 7, !18-dihydropteroate synthase from Escherichia coli MC4100. !$#cross-references MUID:92041593; PMID:1657875 !$#accession A41380 !'##molecule_type protein !'##residues 2-21,'X',23-29 ##label TA2 !'##experimental_source strain MC4100 REFERENCE A78062 !$#authors Xiao, B.; Shi, G.; Chen, X.; Yan, H.; Ji, X. !$#submission submitted to the Protein Data Bank, September 1998 !$#cross-references PDB:1HKA !$#contents annotation; X-ray crystallography, 1.50 angstroms, residues !12-159 GENETICS !$#gene folK !$#map_position 4 min CLASSIFICATION #superfamily !12-amino-4-hydroxy-6-hydroxymethyldihydropteridine !1pyrophosphokinase; !12-amino-4-hydroxy-6-hydroxymethyldihydropteridine !1pyrophosphokinase homology KEYWORDS diphosphotransferase; folate biosynthesis; monomer FEATURE !$2-159 #product !82-amino-4-hydroxy-6-hydroxymethyldihydropteridine !8pyrophosphokinase #status experimental #label MAT\ !$6-139 #domain !82-amino-4-hydroxy-6-hydroxymethyldihydropteridine !8pyrophosphokinase homology #label AHP SUMMARY #length 159 #molecular-weight 18079 #checksum 2160 SEQUENCE /// ENTRY C64046 #type complete TITLE 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase (EC 2.7.6.3) - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase; 7, 8-dihydro-6-hydroxymethylpterin pyrophosphokinase ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS C64046 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession C64046 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-168 ##label TIGR !'##cross-references GB:L42023; TIGR:HI0064 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily !12-amino-4-hydroxy-6-hydroxymethyldihydropteridine !1pyrophosphokinase; !12-amino-4-hydroxy-6-hydroxymethyldihydropteridine !1pyrophosphokinase homology KEYWORDS diphosphotransferase; folate biosynthesis FEATURE !$14-146 #domain !82-amino-4-hydroxy-6-hydroxymethyldihydropteridine !8pyrophosphokinase homology #label AHP SUMMARY #length 168 #molecular-weight 19313 #checksum 7095 SEQUENCE /// ENTRY S66109 #type complete TITLE 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase (EC 2.7.6.3) - Bacillus subtilis ALTERNATE_NAMES 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase; 7, 8-dihydro-6-hydroxymethylpterin pyrophosphokinase ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S66109; F37854; F69626 REFERENCE S65967 !$#authors Ogasawara, N.; Nakai, S.; Yoshikawa, H. !$#journal DNA Res. (1994) 1:1-14 !$#title Systematic sequencing of the 180 kilobase region of the !1Bacillus subtilis chromosome containing the replication !1origin. !$#cross-references MUID:96051385; PMID:7584024 !$#accession S66109 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-167 ##label OGA !'##cross-references EMBL:D26185; NID:g467326; PIDN:BAA05314.1; !1PID:g467468 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1993 REFERENCE A37854 !$#authors Slock, J.; Stahly, D.P.; Han, C.Y.; Six, E.W.; Crawford, !1I.P. !$#journal J. Bacteriol. (1990) 172:7211-7226 !$#title An apparent Bacillus subtilis folic acid biosynthetic operon !1containing pab, an amphibolic trpG gene, a third gene !1required for synthesis of para-aminobenzoic acid, and the !1dihydropteroate synthase gene. !$#cross-references MUID:91072277; PMID:2123867 !$#accession F37854 !'##molecule_type DNA !'##residues 1-162 ##label SLO !'##cross-references GB:M34053 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69626 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-167 ##label KUN !'##cross-references GB:Z99104; GB:AL009126; NID:g2632267; !1PIDN:CAB11855.1; PID:g2632346 !'##experimental_source strain 168 GENETICS !$#gene folK CLASSIFICATION #superfamily !12-amino-4-hydroxy-6-hydroxymethyldihydropteridine !1pyrophosphokinase; !12-amino-4-hydroxy-6-hydroxymethyldihydropteridine !1pyrophosphokinase homology KEYWORDS diphosphotransferase; folate biosynthesis FEATURE !$7-139 #domain !82-amino-4-hydroxy-6-hydroxymethyldihydropteridine !8pyrophosphokinase homology #label AHP SUMMARY #length 167 #molecular-weight 19058 #checksum 2554 SEQUENCE /// ENTRY C70315 #type complete TITLE 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase (EC 2.7.6.3) - Aquifex aeolicus ALTERNATE_NAMES 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase; 7, 8-dihydro-6-hydroxymethylpterin pyrophosphokinase ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS C70315 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession C70315 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-160 ##label AQF !'##cross-references GB:AE000676; NID:g2982884; PIDN:AAC06507.1; !1PID:g2982888; GB:AE000657 !'##experimental_source strain VF5 GENETICS !$#gene folK CLASSIFICATION #superfamily !12-amino-4-hydroxy-6-hydroxymethyldihydropteridine !1pyrophosphokinase; !12-amino-4-hydroxy-6-hydroxymethyldihydropteridine !1pyrophosphokinase homology KEYWORDS diphosphotransferase; folate biosynthesis FEATURE !$6-136 #domain !82-amino-4-hydroxy-6-hydroxymethyldihydropteridine !8pyrophosphokinase homology #label AHP SUMMARY #length 160 #molecular-weight 18838 #checksum 3318 SEQUENCE /// ENTRY S74599 #type complete TITLE 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase (EC 2.7.6.3) - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase; 7, 8-dihydro-6-hydroxymethylpterin pyrophosphokinase; hypothetical protein slr1093 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S74599 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74599 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-195 ##label KAN !'##cross-references EMBL:D90900; GB:AB001339; NID:g1651768; !1PIDN:BAA16751.1; PID:g1651824 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene folK CLASSIFICATION #superfamily !12-amino-4-hydroxy-6-hydroxymethyldihydropteridine !1pyrophosphokinase; !12-amino-4-hydroxy-6-hydroxymethyldihydropteridine !1pyrophosphokinase homology KEYWORDS diphosphotransferase; folate biosynthesis FEATURE !$18-149 #domain !82-amino-4-hydroxy-6-hydroxymethyldihydropteridine !8pyrophosphokinase homology #label AHP SUMMARY #length 195 #molecular-weight 21237 #checksum 776 SEQUENCE /// ENTRY G70955 #type complete TITLE probable 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase (EC 2.7.6.3) - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS G70955 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession G70955 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-188 ##label COL !'##cross-references GB:Z95557; GB:AL123456; NID:g3242276; !1PIDN:CAB08938.1; PID:g2113970 !'##experimental_source strain H37Rv GENETICS !$#gene folK CLASSIFICATION #superfamily !12-amino-4-hydroxy-6-hydroxymethyldihydropteridine !1pyrophosphokinase; !12-amino-4-hydroxy-6-hydroxymethyldihydropteridine !1pyrophosphokinase homology KEYWORDS diphosphotransferase; folate biosynthesis FEATURE !$6-144 #domain !82-amino-4-hydroxy-6-hydroxymethyldihydropteridine !8pyrophosphokinase homology #label AHP SUMMARY #length 188 #molecular-weight 20731 #checksum 7382 SEQUENCE /// ENTRY A36704 #type complete TITLE 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase (EC 2.7.6.3) - Streptococcus pneumoniae ALTERNATE_NAMES 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase; 7, 8-dihydro-6-hydroxymethylpterin pyrophosphokinase CONTAINS 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase (EC 2.7.6.3); dihydroneopterin aldolase (EC 4.1.2.25) ORGANISM #formal_name Streptococcus pneumoniae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS A36704 REFERENCE A36704 !$#authors Lopez, P.; Greenberg, B.; Lacks, S.A. !$#journal J. Bacteriol. (1990) 172:4766-4774 !$#title DNA sequence of folate biosynthesis gene sulD, encoding !1hydroxymethyldihydropterin pyrophosphokinase in !1Streptococcus pneumoniae, and characterization of the !1enzyme. !$#cross-references MUID:90368525; PMID:2168367 !$#accession A36704 !'##status preliminary !'##molecule_type DNA !'##residues 1-270 ##label LOP !'##cross-references GB:M58706 GENETICS !$#gene sulD CLASSIFICATION #superfamily bifunctional folate biosynthesis enzyme sulD; !12-amino-4-hydroxy-6-hydroxymethyldihydropteridine !1pyrophosphokinase homology; dihydroneopterin aldolase !1homology KEYWORDS aldehyde-lyase; carbon-carbon lyase; diphosphotransferase; !1folate biosynthesis FEATURE !$2-119 #domain dihydroneopterin aldolase homology #label !8DHA\ !$124-255 #domain !82-amino-4-hydroxy-6-hydroxymethyldihydropteridine !8pyrophosphokinase homology #label AHP SUMMARY #length 270 #molecular-weight 30946 #checksum 8143 SEQUENCE /// ENTRY S28666 #type complete TITLE multifunctional folic acid synthesis protein - Pneumocystis carinii CONTAINS dihydroneopterin aldolase (EC 4.1.2.25) ORGANISM #formal_name Pneumocystis carinii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Sep-2000 ACCESSIONS S28666 REFERENCE S28666 !$#authors Volpe, F.; Dyer, M.; Scaife, J.G.; Darby, G.; Stammers, !1D.K.; Delves, C.J. !$#journal Gene (1992) 112:213-218 !$#title The multifunctional folic acid synthesis fas gene of !1Pneumocystis carinii appears to encode dihydropteroate !1synthase and hydroxymethyldihydropterin pyrophosphokinase. !$#cross-references MUID:92210001; PMID:1313386 !$#accession S28666 !'##molecule_type DNA !'##residues 1-740 ##label DEL !'##cross-references EMBL:M86602; NID:g169413; PIDN:AAA33790.1; !1PID:g169414 GENETICS !$#gene fas !$#introns 222/3; 351/3; 421/2 CLASSIFICATION #superfamily fasB-fasC-fasD multifunctional enzyme; !12-amino-4-hydroxy-6-hydroxymethyldihydropteridine !1pyrophosphokinase homology; dihydroneopterin aldolase !1homology; dihydropteroate synthase homology KEYWORDS aldehyde-lyase; carbon-carbon lyase; diphosphotransferase; !1folate biosynthesis FEATURE !$39-153 #domain dihydroneopterin aldolase homology #label !8DHA\ !$161-276 #domain dihydroneopterin aldolase homology #label !8DHA2\ !$298-429 #domain !82-amino-4-hydroxy-6-hydroxymethyldihydropteridine !8pyrophosphokinase homology #label AHP\ !$473-720 #domain dihydropteroate synthase homology #label DHS SUMMARY #length 740 #molecular-weight 83961 #checksum 8996 SEQUENCE /// ENTRY S63229 #type complete TITLE probable multifunctional folic acid synthesis protein YNL256w - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein N0848 CONTAINS dihydroneopterin aldolase (EC 4.1.2.25) ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S63229 REFERENCE S63220 !$#authors Sen-Gupta, M.; Gueldener, U.; Beinhauer, J.; Fiedler, T.; !1Hegemann, J.H. !$#submission submitted to the Protein Sequence Database, April 1996 !$#accession S63229 !'##molecule_type DNA !'##residues 1-864 ##label SEN !'##cross-references EMBL:Z71532; NID:g1302304; PIDN:CAA96163.1; !1PID:g1302305; GSPDB:GN00014; MIPS:YNL256w !'##experimental_source strain S288C GENETICS !$#gene SGD:FOL1; MIPS:YNL256w !'##cross-references SGD:S0005200 !$#map_position 14L CLASSIFICATION #superfamily fasB-fasC-fasD multifunctional enzyme; !12-amino-4-hydroxy-6-hydroxymethyldihydropteridine !1pyrophosphokinase homology; dihydroneopterin aldolase !1homology; dihydropteroate synthase homology KEYWORDS aldehyde-lyase; carbon-carbon lyase; diphosphotransferase; !1folate biosynthesis FEATURE !$62-178 #domain dihydroneopterin aldolase homology #label !8DHA1\ !$187-299 #domain dihydroneopterin aldolase homology #label !8DHA2\ !$342-480 #domain !82-amino-4-hydroxy-6-hydroxymethyldihydropteridine !8pyrophosphokinase homology #label AHP\ !$546-844 #domain dihydropteroate synthase homology #label DHS SUMMARY #length 864 #molecular-weight 97675 #checksum 9678 SEQUENCE /// ENTRY RNBP17 #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) - phage T7 ORGANISM #formal_name phage T7 #note host Escherichia coli DATE 01-Sep-1981 #sequence_revision 23-Oct-1981 #text_change 11-Jun-1999 ACCESSIONS A94615; A92867; A92866; JN0398; S42289; S42668; A00684; !1S43501 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession A94615 !'##molecule_type DNA !'##residues 1-883 ##label DUN REFERENCE A92867 !$#authors Stahl, S.J.; Zinn, K. !$#journal J. Mol. Biol. (1981) 148:481-485 !$#title Nucleotide sequence of the cloned gene for bacteriophage T7 !1RNA. !$#cross-references MUID:82078043; PMID:7310873 !$#accession A92867 !'##molecule_type DNA !'##residues 1-883 ##label STA !'##cross-references GB:V01127; NID:g15498; PIDN:CAA24333.1; PID:g15505 REFERENCE A92866 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1981) 148:303-330 !$#title Nucleotide sequence from the genetic left end of !1bacteriophage T7 DNA to the beginning of gene 4. !$#cross-references MUID:82078034; PMID:7310871 !$#accession A92866 !'##molecule_type DNA !'##residues 1-59;829-883 ##label DUN2 !'##cross-references GB:V01127 REFERENCE JN0398 !$#authors Grachev, M.A.; Pletnev, A.G. !$#journal Bioorg. Khim. (1984) 10:824-843 !$#title T7 phage RNA polymerase: cloning and sequencing of gene. !$#cross-references MUID:85046624; PMID:6093820 !$#accession JN0398 !'##molecule_type DNA !'##residues 1-387,'D',389,'ARKSRRIS',398,'EFM',402, !1'EQANKFANHKAIWFPYNMD',420,'R',422;425-442,'L',444-473,'P', !1475-622,'H',624-664,'P',666-883 ##label GRA !'##cross-references GB:M38308; NID:g216011; PIDN:AAA32569.1; !1PID:g216012 !'##note the authors translated the codon ACC for residue 342 as Tyr !'##note the sequence differences between residues 389 and 422 are due !1to frameshift errors REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42289 !'##molecule_type DNA !'##residues 1-883 ##label DUW !'##cross-references EMBL:V01146 REFERENCE S42668 !$#authors Moffatt, B.A.; Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1984) 173:265-269 !$#title Nucleotide sequence of the gene for bacteriophage T7 RNA !1polymerase. !$#cross-references MUID:84164887; PMID:6708104 !$#accession S42668 !'##molecule_type DNA !'##residues 1-387,'DKARKSRRIS',398,'EFM',402,'EQANKFANHKAIWFPYNMD',420, !1'R',422-442,'L',444-473,'P',475-883 ##label MOF !'##cross-references EMBL:V01146 COMMENT T7 polymerase, which is expressed in the early stage of !1lytic development, is responsible for the transcription of !1the late genes of T7. It is rifampicin-resistant and appears !1to function as a single polypeptide. GENETICS !$#gene 1 !$#map_position 7.93-14.55 CLASSIFICATION #superfamily phage T7 DNA-directed RNA polymerase KEYWORDS nucleotidyltransferase; transcription SUMMARY #length 883 #molecular-weight 98091 #checksum 5174 SEQUENCE /// ENTRY RNBPT3 #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) - phage T3 ALTERNATE_NAMES gene 1 protein ORGANISM #formal_name phage T3 DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 11-Jun-1999 ACCESSIONS A29060; S07281 REFERENCE A29060 !$#authors McGraw, N.J.; Bailey, J.N.; Cleaves, G.R.; Dembinski, D.R.; !1Gocke, C.R.; Joliffe, L.K.; MacWright, R.S.; McAllister, !1W.T. !$#journal Nucleic Acids Res. (1985) 13:6753-6766 !$#title Sequence and analysis of the gene for bacteriophage T3 RNA !1polymerase. !$#cross-references MUID:86041870; PMID:3903658 !$#accession A29060 !'##molecule_type DNA !'##residues 1-884 ##label MCG !'##cross-references GB:X02981; NID:g15561; PIDN:CAA26719.1; PID:g15562 REFERENCE S07281 !$#authors Schmitt, M.P.; Beck, P.J.; Kearney, C.A.; Spence, J.L.; !1DiGiovanni, D.; Condreay, J.P.; Molineux, I.J. !$#journal J. Mol. Biol. (1987) 193:479-495 !$#title Sequence of a conditionally essential region of !1bacteriophage T3, including the primary origin of DNA !1replication. !$#cross-references MUID:87226207; PMID:3586029 !$#accession S07281 !'##status translation not shown !'##molecule_type DNA !'##residues 855-884 ##label SCH !'##cross-references EMBL:X05031; NID:g15719; PIDN:CAA28696.1; !1PID:g15720 GENETICS !$#gene 1 CLASSIFICATION #superfamily phage T7 DNA-directed RNA polymerase KEYWORDS early protein; nucleotidyltransferase; transcription SUMMARY #length 884 #molecular-weight 98789 #checksum 872 SEQUENCE /// ENTRY RNBPK1 #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) - phage K11 ORGANISM #formal_name phage K11 DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 11-Jun-1999 ACCESSIONS S10530 REFERENCE S10530 !$#authors Dietz, A.; Weisser, H.J.; Koessel, H.; Hausmann, R. !$#journal Mol. Gen. Genet. (1990) 221:283-286 !$#title The gene for Klebsiella bacteriophage K11 RNA polymerase: !1sequence and comparison with the homologous genes of phages !1T7, T3, and SP6. !$#cross-references MUID:90318328; PMID:2370850 !$#accession S10530 !'##molecule_type DNA !'##residues 1-906 ##label DIE !'##cross-references EMBL:X53238; NID:g14984; PIDN:CAA37330.1; !1PID:g14985 GENETICS !$#gene 1 CLASSIFICATION #superfamily phage T7 DNA-directed RNA polymerase KEYWORDS nucleotidyltransferase; transcription SUMMARY #length 906 #molecular-weight 101127 #checksum 4618 SEQUENCE /// ENTRY S07380 #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) - Salmonella phage SP6 ORGANISM #formal_name Salmonella phage SP6 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S07380; S09058 REFERENCE S07380 !$#authors Kotani, H.; Ishizaki, Y.; Hiraoka, N.; Obayashi, A. !$#journal Nucleic Acids Res. (1987) 15:2653-2664 !$#title Nucleotide sequence and expression of the cloned gene of !1bacteriophage SP6 RNA polymerase. !$#cross-references MUID:87174790; PMID:3031606 !$#accession S07380 !'##molecule_type DNA !'##residues 1-874 ##label KOT1 !'##cross-references EMBL:Y00105 !'##note the authors translated the codon GCA for residue 162 as Gln REFERENCE S09058 !$#authors Kotani, H. !$#submission submitted to the EMBL Data Library, March 1987 !$#accession S09058 !'##molecule_type DNA !'##residues 1-844,'V',846-874 ##label KOT2 !'##cross-references EMBL:Y00105; NID:g15462; PIDN:CAA68288.1; !1PID:g15463 CLASSIFICATION #superfamily phage T7 DNA-directed RNA polymerase KEYWORDS nucleotidyltransferase; transcription SUMMARY #length 874 #molecular-weight 98562 #checksum 9450 SEQUENCE /// ENTRY RNVZ19 #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) 19K chain - vaccinia virus ALTERNATE_NAMES A5R protein ORGANISM #formal_name vaccinia virus #note host Homo sapiens (man) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 18-Feb-2000 ACCESSIONS B41806; E41806; G42517; T37392 REFERENCE A41806 !$#authors Ahn, B.Y.; Rosel, J.; Cole, N.B.; Moss, B. !$#journal J. Virol. (1992) 66:971-982 !$#title Identification and expression of rpo19, a vaccinia virus !1gene encoding a 19-kilodalton DNA-dependent RNA polymerase !1subunit. !$#cross-references MUID:92114202; PMID:1731116 !$#accession B41806 !'##molecule_type DNA !'##residues 1-164 ##label AHN1 !'##cross-references GB:M76473; NID:g335803; PIDN:AAA48337.1; !1PID:g335804 !$#accession E41806 !'##molecule_type protein !'##residues 44-70;96-114;133-156 ##label AHN2 !'##experimental_source strain WR REFERENCE A33172 !$#authors Johnson, G.P. !$#submission submitted to GenBank, June 1990 !$#accession G42517 !'##molecule_type DNA !'##residues 1-164 ##label JOH !'##cross-references GB:M35027; NID:g335317; PIDN:AAA48122.1; !1PID:g335470 !'##experimental_source strain Copenhagen REFERENCE Z20877 !$#authors Antoine, G.; Scheiflinger, F.; Falkner, F.G.; Dorner, F. !$#submission submitted to the EMBL Data Library, March 1997 !$#description The complete genomic sequence of the Modified Vaccinia !1Ankara (MVA) strain. !$#accession T37392 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-164 ##label ANT !'##cross-references EMBL:U94848; PIDN:AAB96519.1 !'##experimental_source strain Ankara GENETICS !$#note MVA116R CLASSIFICATION #superfamily vaccinia virus DNA-directed RNA polymerase 19K !1polypeptide KEYWORDS early protein; nucleotidyltransferase SUMMARY #length 164 #molecular-weight 18996 #checksum 7157 SEQUENCE /// ENTRY RNVZ22 #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) 22K chain [similarity] - vaccinia virus (strains Ankara, WR and Copenhagen) ALTERNATE_NAMES J4R protein ORGANISM #formal_name vaccinia virus #note host Homo sapiens (man) DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 18-Feb-2000 ACCESSIONS A25734; I23092; G42513; T37364 REFERENCE A25734 !$#authors Broyles, S.S.; Moss, B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:3141-3145 !$#title Homology between RNA polymerases of poxviruses, prokaryotes, !1and eukaryotes: nucleotide sequence and transcriptional !1analysis of vaccinia virus genes encoding 147-kDa and 22-kDa !1subunits. !$#cross-references MUID:86205852; PMID:3517852 !$#accession A25734 !'##molecule_type DNA !'##residues 1-185 ##label BRO !'##cross-references GB:M13209; GB:M14122; NID:g335739; PIDN:AAB59833.1; !1PID:g335740 !'##experimental_source strain WR REFERENCE A23092 !$#authors Plucienniczak, A.; Schroeder, E.; Zettlmeissl, G.; Streeck, !1R.E. !$#journal Nucleic Acids Res. (1985) 13:985-998 !$#title Nucleotide sequence of a cluster of early and late genes in !1a conserved segment of the vaccinia virus genome. !$#cross-references MUID:85215527; PMID:2987815 !$#accession I23092 !'##molecule_type DNA !'##residues 1-185 ##label PLU !'##cross-references GB:X01978; GB:J02424; GB:J02425; GB:K02376; !1GB:M15211; GB:V01537; NID:g61387; PIDN:CAA26018.1; !1PID:g61397 !'##experimental_source strain WR REFERENCE A42501 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:517-563 !$#title Appendix to "The complete DNA sequence of vaccinia virus". !$#accession G42513 !'##molecule_type DNA !'##residues 1-185 ##label GOE !'##cross-references GB:M35027; NID:g335317; PIDN:AAA48084.1; !1PID:g335432 !'##experimental_source strain Copenhagen REFERENCE A42531 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:247-266 !$#title The complete DNA sequence of vaccinia virus. !$#cross-references MUID:91021027; PMID:2219722 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given REFERENCE Z20877 !$#authors Antoine, G.; Scheiflinger, F.; Falkner, F.G.; Dorner, F. !$#submission submitted to the EMBL Data Library, March 1997 !$#description The complete genomic sequence of the Modified Vaccinia !1Ankara (MVA) strain. !$#accession T37364 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-185 ##label ANT !'##cross-references EMBL:U94848; PIDN:AAB96505.1 !'##experimental_source strain Ankara GENETICS !$#note MVA088R CLASSIFICATION #superfamily vaccinia virus DNA-directed RNA polymerase 22K !1polypeptide KEYWORDS early protein; nucleotidyltransferase; transcription SUMMARY #length 185 #molecular-weight 21342 #checksum 3437 SEQUENCE /// ENTRY RNVZ30 #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) 30K chain - vaccinia virus (strain WR) ALTERNATE_NAMES 30K transcription factor E4L ORGANISM #formal_name vaccinia virus DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 11-Jun-1999 ACCESSIONS A36406; C35928 REFERENCE A36406 !$#authors Broyles, S.S.; Pennington, M.J. !$#journal J. Virol. (1990) 64:5376-5382 !$#title Vaccinia virus gene encoding a 30-kilodalton subunit of the !1viral DNA-dependent RNA polymerase. !$#cross-references MUID:91012780; PMID:2214020 !$#accession A36406 !'##molecule_type DNA !'##residues 1-259 ##label BRO !'##cross-references EMBL:M59813; NID:g335759; PIDN:AAA48306.1; !1PID:g335760 REFERENCE A35928 !$#authors Ahn, B.Y.; Gershon, P.D.; Jones, E.V.; Moss, B. !$#journal Mol. Cell. Biol. (1990) 10:5433-5441 !$#title Identification of rpo30, a vaccinia virus RNA polymerase !1gene with structural similarity to a eucaryotic !1transcription elongation factor. !$#cross-references MUID:90377234; PMID:2398897 !$#accession C35928 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-259 ##label AHN !'##cross-references GB:M36339; NID:g335747; PIDN:AAB59824.1; !1PID:g335751 GENETICS !$#gene rpo30 CLASSIFICATION #superfamily vaccinia virus DNA-directed RNA polymerase 30K !1polypeptide KEYWORDS DNA binding; early protein; nucleotidyltransferase; !1transcription; zinc finger SUMMARY #length 259 #molecular-weight 29826 #checksum 3755 SEQUENCE /// ENTRY RNVZ35 #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) 35K chain - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 11-Jun-1999 ACCESSIONS A39460; S29913 REFERENCE A39460 !$#authors Amegadzie, B.Y.; Ahn, B.Y.; Moss, B. !$#journal J. Biol. Chem. (1991) 266:13712-13718 !$#title Identification, sequence, and expression of the gene !1encoding a Mr 35,000 subunit of the vaccinia virus !1DNA-dependent RNA polymerase. !$#cross-references MUID:91310644; PMID:1856205 !$#accession A39460 !'##molecule_type DNA !'##residues 1-305 ##label AM1 !'##cross-references GB:M61187; NID:g335782; PIDN:AAA48326.1; !1PID:g335789 REFERENCE S29907 !$#authors Amegadzie, B.Y. !$#submission submitted to the EMBL Data Library, January 1991 !$#accession S29913 !'##status preliminary !'##molecule_type DNA !'##residues 1-305 ##label AM2 !'##cross-references EMBL:X57318; NID:g62239; PIDN:CAA40579.1; !1PID:g62246 CLASSIFICATION #superfamily vaccinia virus DNA-directed RNA polymerase 35K !1polypeptide KEYWORDS early protein; nucleotidyltransferase; transcription SUMMARY #length 305 #molecular-weight 35358 #checksum 9964 SEQUENCE /// ENTRY RNVZC5 #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) 35K chain - vaccinia virus (strain Copenhagen) ORGANISM #formal_name vaccinia virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 11-Jun-1999 ACCESSIONS D42520 REFERENCE A42501 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:517-563 !$#title Appendix to "The complete DNA sequence of vaccinia virus". !$#accession D42520 !'##molecule_type DNA !'##residues 1-305 ##label GOE !'##cross-references GB:M35027; NID:g335317; PIDN:AAA48154.1; !1PID:g335502 REFERENCE A42531 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:247-266 !$#title The complete DNA sequence of vaccinia virus. !$#cross-references MUID:91021027; PMID:2219722 !$#contents annotation; possible protein-coding frames CLASSIFICATION #superfamily vaccinia virus DNA-directed RNA polymerase 35K !1polypeptide KEYWORDS early protein; nucleotidyltransferase; transcription SUMMARY #length 305 #molecular-weight 35393 #checksum 9638 SEQUENCE /// ENTRY WMVZM4 #type fragment TITLE DNA-directed RNA polymerase (EC 2.7.7.6) 35K polypeptide - sheep pox virus (isolate Kenya sheep-1, KS-1) (fragment) ORGANISM #formal_name sheep pox virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 11-Jun-1999 ACCESSIONS D33325 REFERENCE A33325 !$#authors Gershon, P.D.; Ansell, D.M.; Black, D.N. !$#journal J. Virol. (1989) 63:4703-4708 !$#title A comparison of the genome organization of capripoxvirus !1with that of the orthopoxviruses. !$#cross-references MUID:90012320; PMID:2795717 !$#accession D33325 !'##molecule_type DNA !'##residues 1-126 ##label GER !'##cross-references GB:M30039; NID:g323258; PIDN:AAC32900.1; !1PID:g323262 CLASSIFICATION #superfamily vaccinia virus DNA-directed RNA polymerase 35K !1polypeptide KEYWORDS nucleotidyltransferase SUMMARY #length 126 #checksum 8784 SEQUENCE /// ENTRY A34588 #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) chain RPB5 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YBR1204; protein YBR154c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A34588; S30138; S46025; S37316 REFERENCE A34588 !$#authors Woychik, N.A.; Liao, S.M.; Kolodziej, P.A.; Young, R.A. !$#journal Genes Dev. (1990) 4:313-323 !$#title Subunits shared by eukaryotic nuclear RNA polymerases. !$#cross-references MUID:90249736; PMID:2186966 !$#accession A34588 !'##molecule_type DNA !'##residues 1-215 ##label WOY !'##cross-references EMBL:X53287; NID:g287821; PIDN:CAA37381.1; !1PID:g287822 REFERENCE S30136 !$#authors Baur, A.; Schaaff-Gerstenschlaeger, I.; Boles, E.; Miosga, !1T.; Rose, M.; Zimmermann, F.K. !$#journal Yeast (1993) 9:289-293 !$#title Sequence of a 4.8 kb fragment of Saccharomyces cerevisiae !1chromosome II including three essential open reading frames. !$#cross-references MUID:93255907; PMID:8488729 !$#accession S30138 !'##status translation not shown !'##molecule_type DNA !'##residues 1-215 ##label BAU !'##cross-references EMBL:X71329; NID:g396752; PIDN:CAA50472.1; !1PID:g396754 REFERENCE S46013 !$#authors Entian, K.D.; Koetter, P.; Rose, M.; Becker, J.; Grey, M.; !1Li, Z.; Niegemann, E.; Schenk-Groeninger, R.; Servos, J.; !1Wehner, E.; Wolter, R.; Brendel, M.; Bauer, J.; Braun, H.; !1Dern, K.; Duesterhus, S.; Gruenbein, R.; Hedges, D.; Kiesau, !1P.; Korol, S.; Krems, B.; Proft, M.; Siegers, K.; Baur, A.; !1Boles, E.; Miosga, T.; Schaaff-Gerstenschlaeger, I.; !1Zimmermann, F.K. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S46025 !'##molecule_type DNA !'##residues 1-215 ##label ENT !'##cross-references EMBL:Z36023; NID:g536483; PIDN:CAA85113.1; !1PID:g536484; GSPDB:GN00002; MIPS:YBR154c GENETICS !$#gene SGD:RPB5; MIPS:YBR154c !'##cross-references SGD:S0000358; MIPS:YBR154c !$#map_position 2R CLASSIFICATION #superfamily DNA-directed RNA polymerase chain RPB5 KEYWORDS nucleotidyltransferase; nucleus; transcription SUMMARY #length 215 #molecular-weight 25079 #checksum 6993 SEQUENCE /// ENTRY S23795 #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) chain H - Methanococcus vannielii ALTERNATE_NAMES DNA-dependent RNA polymerase chain H ORGANISM #formal_name Methanococcus vannielii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S23795; S47159 REFERENCE S20107 !$#authors Klenk, H.P.; Palm, P.; Lottspeich, F.; Zillig, W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:407-410 !$#title Component H of the DNA-dependent RNA polymerases of Archaea !1is homologous to a subunit shared by the three eucaryal !1nuclear RNA polymerases. !$#cross-references MUID:92108064; PMID:1729711 !$#accession S23795 !'##molecule_type DNA !'##residues 1-78 ##label KLE !'##cross-references EMBL:X59151; NID:g44746; PIDN:CAA41862.1; !1PID:g809732 !'##experimental_source DSM 1224 REFERENCE S47159 !$#authors Palm, P.; Arnold-Ammer, I.; Lechner, K.A.; Zillig, W. !$#submission submitted to the EMBL Data Library, June 1993 !$#description DNA sequence of the genes of the large subunits of the DNA !1dependent RNA-polymerase of Methanococcus vannielii. !$#accession S47159 !'##molecule_type DNA !'##residues 1-78 ##label PAL !'##cross-references EMBL:X73293; NID:g505288; PIDN:CAA51725.1; !1PID:g581387 !'##experimental_source DSM 1224 GENETICS !$#gene rpoH !$#start_codon GTG CLASSIFICATION #superfamily DNA-directed RNA polymerase chain H KEYWORDS nucleotidyltransferase; transcription SUMMARY #length 78 #molecular-weight 8707 #checksum 3405 SEQUENCE /// ENTRY A25968 #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) 40K chain - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein P8283.18; protein YPR110c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A25968; S59775 REFERENCE A25968 !$#authors Mann, C.; Buhler, J.M.; Treich, I.; Sentenac, A. !$#journal Cell (1987) 48:627-637 !$#title RPC40, a unique gene for a subunit shared between yeast RNA !1polymerases A and C. !$#cross-references MUID:87131075; PMID:3815519 !$#accession A25968 !'##molecule_type DNA !'##residues 1-335 ##label MAN !'##cross-references EMBL:M15499; NID:g172473; PIDN:AAA34999.1; !1PID:g172474 REFERENCE S59764 !$#authors Nelson, J. !$#submission submitted to the EMBL Data Library, July 1995 !$#description The sequence of S. cerevisiae cosmid 8283. !$#accession S59775 !'##molecule_type DNA !'##residues 1-335 ##label NEL !'##cross-references EMBL:U32445; NID:g914969; PIDN:AAB68080.1; !1PID:g914981; GSPDB:GN00016; MIPS:YPR110c GENETICS !$#gene SGD:RPC40; RPC5; MIPS:YPR110c !'##cross-references SGD:S0006314; MIPS:YPR110c !$#map_position 16R CLASSIFICATION #superfamily Saccharomyces cerevisiae DNA-directed RNA !1polymerase 40K chain KEYWORDS nucleotidyltransferase; nucleus; transcription SUMMARY #length 335 #molecular-weight 37686 #checksum 3227 SEQUENCE /// ENTRY RNECA #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) alpha chain - Escherichia coli (strain K-12) ALTERNATE_NAMES transcriptase alpha chain ORGANISM #formal_name Escherichia coli DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 01-Mar-2002 ACCESSIONS A22884; D23807; A91437; A90725; A92243; I77539; I77541; !1I77543; B65122; A00685; S14232 REFERENCE A22884 !$#authors Meek, D.W.; Hayward, R.S. !$#journal Nucleic Acids Res. (1984) 12:5813-5821 !$#title Nucleotide sequence of the rpoA-rplQ DNA of Escherichia !1coli: a second regulatory binding site for protein S4? !$#cross-references MUID:84272255; PMID:6379605 !$#accession A22884 !'##molecule_type DNA !'##residues 1-329 ##label MEE !'##cross-references GB:J01685; GB:X00766; NID:g147713; PIDN:AAA24577.1; !1PID:g147715 REFERENCE A23807 !$#authors Bedwell, D.; Davis, G.; Gosink, M.; Post, L.; Nomura, M.; !1Kestler, H.; Zengel, J.M.; Lindahl, L. !$#journal Nucleic Acids Res. (1985) 13:3891-3903 !$#title Nucleotide sequence of the alpha ribosomal protein operon of !1Escherichia coli. !$#cross-references MUID:85242076; PMID:2989779 !$#accession D23807 !'##molecule_type DNA !'##residues 1-329 ##label BED REFERENCE A91437 !$#authors Ovchinnikov, Y.A.; Lipkin, V.M.; Modyanov, N.N.; Chertov, !1O.Y.; Smirnov, Y.V. !$#journal FEBS Lett. (1977) 76:108-111 !$#title Primary structure of alpha-subunit of DNA-dependent RNA !1polymerase from Escherichia coli. !$#cross-references MUID:77162615; PMID:323055 !$#accession A91437 !'##molecule_type protein !'##residues 1-329 ##label OVC REFERENCE A90725 !$#authors Modyanov, N.N.; Lipkin, V.M.; Smirnov, Y.V.; Shuvaeva, T.M.; !1Kocherginskaya, S.A. !$#journal Bioorg. Khim. (1978) 4:437-449 !$#title The primary structure of alpha-subunit of DNA-dependent RNA !1polymerase from E. coli. V. The cyanogen bromide peptides. !$#accession A90725 !'##molecule_type protein !'##residues 1-329 ##label MOD !'##note article in Russian with English abstract REFERENCE A92243 !$#authors Post, L.E.; Nomura, M. !$#journal J. Biol. Chem. (1979) 254:10604-10606 !$#title Nucleotide sequence of the intercistronic region preceding !1the gene for RNA polymerase subunit alpha in Escherichia !1coli. !$#cross-references MUID:80049646; PMID:387752 !$#accession A92243 !'##molecule_type DNA !'##residues 1-159 ##label POS !'##cross-references GB:V00353; NID:g42904; PIDN:CAA23646.1; PID:g42906 REFERENCE S14232 !$#authors Igarashi, K.; Fujita, N.; Ishihama, A. !$#journal Nucleic Acids Res. (1990) 18:5945-5948 !$#title Sequence analysis of two temperature-sensitive mutations in !1the alpha subunit gene (rpoA) of Escherichia coli RNA !1polymerase. !$#cross-references MUID:91045051; PMID:2235479 !$#contents annotation !$#note versions with single substitutions of Cys for Arg at !1positions 45 or 191 are temperature-sensitive mutants REFERENCE I57736 !$#authors Schnier, J.; Isono, S.; Cumberlidge, A.G.; Isono, K. !$#journal Mol. Gen. Genet. (1985) 199:265-270 !$#title Unstable mutations caused by regional tandem multiplications !1in the gene for ribosomal protein S4 show thermosensitivity !1in Escherichia coli. !$#cross-references MUID:85267249; PMID:3894886 !$#accession I77539 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-8 ##label RES !'##cross-references GB:M29822; NID:g147735; PIDN:AAA24590.1; !1PID:g147737 !$#accession I77541 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-9 ##label RE2 !'##cross-references GB:M29823; NID:g147738; PIDN:AAA24592.1; !1PID:g147740 !$#accession I77543 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-12 ##label RE3 !'##cross-references GB:M29824; NID:g147741; PIDN:AAA24594.1; !1PID:g147743 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65122 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-329 ##label BLAT !'##cross-references GB:AE000407; GB:U00096; NID:g2367211; !1PIDN:AAC76320.1; PID:g1789690; UWGP:b3295 !'##experimental_source strain K-12, substrain MG1655 COMMENT The DNA-directed RNA polymerase, also called transcriptase, !1catalyzes RNA synthesis using a DNA template. The enzyme !1consists of the sigma chain and the core enzyme. The sigma !1chain is an initiation factor that promotes attachment of !1the enzyme to specific initiation sites and then is !1released. The core enzyme is composed of two alpha chains, !1one beta chain, and one beta' chain. GENETICS !$#gene rpoA !$#map_position 72 min CLASSIFICATION #superfamily DNA-directed RNA polymerase alpha chain KEYWORDS nucleotidyltransferase; transcription SUMMARY #length 329 #molecular-weight 36511 #checksum 1179 SEQUENCE /// ENTRY A41658 #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) alpha chain - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A41658 REFERENCE A41658 !$#authors Lombardo, M.J.; Bagga, D.; Miller, C.G. !$#journal J. Bacteriol. (1991) 173:7511-7518 !$#title Mutations in rpoA affect expression of anaerobically !1regulated genes in Salmonella typhimurium. !$#cross-references MUID:92041662; PMID:1938946 !$#accession A41658 !'##molecule_type DNA !'##residues 1-329 ##label LOM !'##cross-references GB:M77750; NID:g154352; PIDN:AAA27214.1; !1PID:g154353 GENETICS !$#gene rpoA CLASSIFICATION #superfamily DNA-directed RNA polymerase alpha chain KEYWORDS nucleotidyltransferase; transcription SUMMARY #length 329 #molecular-weight 36511 #checksum 1179 SEQUENCE /// ENTRY RNNTA #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) alpha chain - common tobacco chloroplast ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 17-Feb-1995 ACCESSIONS A00686 REFERENCE A00149 !$#authors Sugiura, M. !$#submission submitted to the EMBL Data Library, August 1986 !$#accession A00686 !'##molecule_type DNA !'##residues 1-337 ##label SUG !'##experimental_source cv. Bright Yellow 4 REFERENCE A38013 !$#authors Shinozaki, K.; Ohme, M.; Tanaka, M.; Wakasugi, T.; !1Hayashida, N.; Matsubayashi, T.; Zaita, N.; Chunwongse, J.; !1Obokata, J.; Yamaguchi-Shinozaki, K.; Ohto, C.; Torazawa, !1K.; Meng, B.Y.; Sugita, M.; Deno, H.; Kamogashira, T.; !1Yamada, K.; Kusuda, J.; Takaiwa, F.; Kato, A.; Tohdoh, N.; !1Shimada, H.; Sugiura, M. !$#journal EMBO J. (1986) 5:2043-2049 !$#title The complete nucleotide sequence of the tobacco chloroplast !1genome: its gene organization and expression. !$#contents annotation; gene organization, sites, features GENETICS !$#gene rpoA !$#genome chloroplast CLASSIFICATION #superfamily DNA-directed RNA polymerase alpha chain KEYWORDS chloroplast; nucleotidyltransferase; transcription SUMMARY #length 337 #molecular-weight 38612 #checksum 1897 SEQUENCE /// ENTRY S04384 #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) alpha chain - garden pea chloroplast ORGANISM #formal_name chloroplast Pisum sativum #common_name garden pea DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S04384 REFERENCE S04382 !$#authors Purton, S.; Gray, J.C. !$#journal Mol. Gen. Genet. (1989) 217:77-84 !$#title The plastid rpoA gene encoding a protein homologous to the !1bacterial RNA polymerase alpha subunit is expressed in pea !1chloroplasts. !$#cross-references MUID:89364695; PMID:2671652 !$#accession S04384 !'##molecule_type DNA !'##residues 1-334 ##label PUR !'##cross-references EMBL:X15645; NID:g12178; PIDN:CAA33668.1; !1PID:g12180 GENETICS !$#gene rpoA !$#genome chloroplast CLASSIFICATION #superfamily DNA-directed RNA polymerase alpha chain KEYWORDS chloroplast; nucleotidyltransferase; transcription SUMMARY #length 334 #molecular-weight 38933 #checksum 1679 SEQUENCE /// ENTRY RNRZA #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) alpha chain - rice chloroplast ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 11-Jun-1999 ACCESSIONS JQ0258; S05138 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0258 !'##molecule_type DNA !'##residues 1-337 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05138 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-337 ##label HIR !'##cross-references EMBL:X15901; NID:g11957; PIDN:CAA33979.1; !1PID:g12018 !'##experimental_source cv. Nihonbare GENETICS !$#gene rpoA !$#map_position CP75343-74330 !$#genome chloroplast CLASSIFICATION #superfamily DNA-directed RNA polymerase alpha chain KEYWORDS chloroplast; nucleotidyltransferase; transcription SUMMARY #length 337 #molecular-weight 38667 #checksum 8737 SEQUENCE /// ENTRY RNWTA #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) alpha chain - wheat chloroplast ORGANISM #formal_name chloroplast Triticum aestivum #common_name common wheat #variety cv. Mardler DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 11-Jun-1999 ACCESSIONS S05314; S14963 REFERENCE S05314 !$#authors Hird, S.M.; Dyer, T.A.; Gray, J.C. !$#journal Nucleic Acids Res. (1989) 17:6394 !$#title Nucleotide sequence of the rpoA gene in wheat chloroplast !1DNA. !$#cross-references MUID:89366674; PMID:2671938 !$#accession S05314 !'##molecule_type DNA !'##residues 1-339 ##label HIR !'##cross-references EMBL:X15595; NID:g12371; PIDN:CAA33618.1; !1PID:g12372 !'##experimental_source cv. Mardler REFERENCE S14960 !$#authors Hird, S.M.; Wilson, R.J.; Dyer, T.A.; Gray, J.C. !$#journal Plant Mol. Biol. (1991) 16:745-747 !$#title Nucleotide sequence of the wheat chloroplast petB and petD !1genes encoding apocytochrome b-563 and subunit IV of the !1cytochrome bf complex. !$#cross-references MUID:91329710; PMID:1868207 !$#accession S14963 !'##molecule_type DNA !'##residues 322-339 ##label HIW !'##cross-references EMBL:X54751; NID:g12361; PIDN:CAA38553.1; !1PID:g804974 GENETICS !$#gene rpoA !$#genome chloroplast CLASSIFICATION #superfamily DNA-directed RNA polymerase alpha chain KEYWORDS chloroplast; nucleotidyltransferase; transcription SUMMARY #length 339 #molecular-weight 38703 #checksum 3164 SEQUENCE /// ENTRY RNZMA #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) alpha chain - maize chloroplast ALTERNATE_NAMES RNA polymerase 38K chain ORGANISM #formal_name chloroplast Zea mays #common_name maize DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 11-Jun-1999 ACCESSIONS S00977; C34846 REFERENCE S00976 !$#authors Ruf, M.; Koessel, H. !$#journal Nucleic Acids Res. (1988) 16:5741-5754 !$#title Structure and expression of the gene coding for the !1alpha-subunit of DNA-dependent RNA polymerase from the !1chloroplast genome of Zea mays. !$#cross-references MUID:88289331; PMID:3399379 !$#accession S00977 !'##molecule_type DNA !'##residues 1-341 ##label RUF !'##cross-references EMBL:X07810; NID:g12466; PIDN:CAA30670.1; !1PID:g12467 REFERENCE A34846 !$#authors Hu, J.; Bogorad, L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:1531-1535 !$#title Maize chloroplast RNA polymerase: the 180-, 120-, and !138-kilodalton polypeptides are encoded in chloroplast genes. !$#cross-references MUID:90160360; PMID:2304916 !$#accession C34846 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-18 ##label HUJ GENETICS !$#gene rpoA !$#genome chloroplast CLASSIFICATION #superfamily DNA-directed RNA polymerase alpha chain KEYWORDS chloroplast; nucleotidyltransferase; transcription SUMMARY #length 341 #molecular-weight 38958 #checksum 448 SEQUENCE /// ENTRY RNLVA #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) alpha chain - liverwort (Marchantia polymorpha) chloroplast ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 11-Jun-1999 ACCESSIONS A00687; S01565 REFERENCE A00150 !$#authors Ohyama, K. !$#submission submitted to the EMBL Data Library, October 1986 !$#accession A00687 !'##molecule_type DNA !'##residues 1-340 ##label OHY REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features REFERENCE S01529 !$#authors Fukuzawa, H.; Kohchi, T.; Sano, T.; Shirai, H.; Umesono, K.; !1Inokuchi, H.; Ozeki, H.; Ohyama, K. !$#journal J. Mol. Biol. (1988) 203:333-351 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. III. Gene organization of the large !1single copy region from rbcL to trnI(CAU). !$#cross-references MUID:89068687; PMID:3199436 !$#accession S01565 !'##molecule_type DNA !'##residues 1-340 ##label FUK !'##cross-references EMBL:X04465; NID:g11640; PIDN:CAA28117.1; !1PID:g11706 GENETICS !$#gene rpoA !$#genome chloroplast CLASSIFICATION #superfamily DNA-directed RNA polymerase alpha chain KEYWORDS chloroplast; nucleotidyltransferase; transcription SUMMARY #length 340 #molecular-weight 39240 #checksum 3318 SEQUENCE /// ENTRY RNECB #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) beta chain - Escherichia coli (strain K-12) ALTERNATE_NAMES transcriptase beta chain ORGANISM #formal_name Escherichia coli DATE 31-Oct-1980 #sequence_revision 12-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS F65205; A91109; JN0244; S12576; A91472; A00689; I52540; !1I52542; I52541; I52539; A00688 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65205 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1342 ##label BLAT !'##cross-references GB:AE000472; GB:U00096; NID:g2367333; !1PIDN:AAC76961.1; PID:g1790419; UWGP:b3987 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A91109 !$#authors Ovchinnikov, Y.A.; Monastyrskaya, G.S.; Gubanov, V.V.; !1Guryev, S.O.; Chertov, O.Y.; Modyanov, N.N.; Grinkevich, !1V.A.; Makarova, I.A.; Marchenko, T.V.; Polovnikova, I.N.; !1Lipkin, V.M.; Sverdlov, E.D. !$#journal Eur. J. Biochem. (1981) 116:621-629 !$#title The primary structure of Escherichia coli RNA polymrase. !1Nucleotide sequence of the rpoB gene and amino-acid sequence !1of the beta-subunit. !$#cross-references MUID:81260785; PMID:6266829 !$#accession A91109 !'##molecule_type DNA !'##residues 1-515,'V',517-1342 ##label OVC !'##cross-references GB:V00339; GB:J01678; GB:K00449; NID:g42813; !1PIDN:CAA23625.1; PID:g42818 !'##note most of this sequence was confirmed by amino acid analysis REFERENCE JN0244 !$#authors Ovchinnikov, Y.A.; Sverdlov, E.D.; Lipkin, V.M.; !1Monastyrskaya, G.S.; Chertov, O.Y.; Gubanov, V.V.; Guryer, !1S.O.; Modyanov, N.N.; Grinkevich, V.A.; Makarova, I.A.; !1Marchenko, T.V.; Polovnikova, I.N. !$#journal Bioorg. Khim. (1980) 6:655-665 !$#title Primary structure of RNA polymerase from E. coli; nucleotide !1sequence of EcoR1-C fragment of gene rpoB and amino acid !1sequence of the corresponding fragment of beta-subunit. !$#accession JN0244 !'##status preliminary !'##molecule_type DNA !'##residues 187-515,'V',517-1144 ##label OV2 REFERENCE S12572 !$#authors Post, L.E.; Strycharz, G.D.; Nomura, M.; Lewis, H.; Dennis, !1P.P. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1979) 76:1697-1701 !$#title Nucleotide sequence of the ribosomal protein gene cluster !1adjacent to the gene for RNA polymerase subunit beta in !1Escherichia coli. !$#cross-references MUID:79201667; PMID:377281 !$#accession S12576 !'##molecule_type DNA !'##residues 1-33 ##label POS !'##cross-references EMBL:V00339 REFERENCE A91472 !$#authors Delcuve, G.; Downing, W.; Lewis, H.; Dennis, P.P. !$#journal Gene (1980) 11:367-373 !$#title Nucleotide sequence of the proximal portion of the RNA !1polymerase beta subunit gene of Escherichia coli. !$#cross-references MUID:81165543; PMID:7011900 !$#accession A91472 !'##molecule_type DNA !'##residues 1-105,'G',108-383,'CSRTCSSP' ##label DEL !'##cross-references GB:V00341; NID:g42823; PIDN:CAA23629.1; PID:g42824 REFERENCE A00689 !$#authors Gurevitch, A.I.; Avakov, A.E.; Kolosov, M.N. !$#journal Bioorg. Khim. (1979) 5:1735-1738 !$#title The nucleotide sequence at the proximal end of rpoB gene of !1Escherichia coli. !$#accession A00689 !'##status significant sequence differences !'##molecule_type DNA REFERENCE I52540 !$#authors Monastyrskaya, G.S.; Gubanov, V.V.; Guryev, S.O.; Lipkin, !1V.M.; Sverdlov, E.D. !$#journal Bioorg. Khim. (1980) 6:1423-1426 !$#title Primary structure of RNA polymerase from E.coli: Nucleotide !1sequence of the rpoB gene fragment and corresponding !1N-terminal amino acid sequence of the beta-subunit. !$#accession I52540 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-188 ##label RES !'##cross-references GB:M38292; NID:g147717; PIDN:AAA24579.1; !1PID:g147718 REFERENCE I52542 !$#authors Sverdlov, E.D.; Lipkin, V.M.; Monastyrskaya, G.S.; Gubanov, !1V.V.; Guryev, S.O.; Chertov, O.Y. !$#journal Bioorg. Khim. (1980) 6:309-312 !$#title The nucleotide sequence of strong RNA polymerase binding !1site within the E.coli rpoB structural gene. !$#accession I52542 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 187-354 ##label RE2 !'##cross-references GB:M38304; NID:g147719; PIDN:AAA24580.1; !1PID:g551832 REFERENCE I52541 !$#authors Gurevich, A.I.; Igoshin, A.V.; Kolosov, M.N. !$#journal Bioorg. Khim. (1980) 6:1580-1584 !$#title Structure of a central part of E.coli operon rpoBC. !1Nucleotide sequence of the gene for beta subunit of RNA !1polymerase. !$#accession I52541 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1143-1342 ##label RE3 !'##cross-references GB:M38303; NID:g147724; PIDN:AAA24583.1; !1PID:g147725 REFERENCE I52539 !$#authors Monastyrskaya, G.S.; Gubanov, V.V.; Guryev, S.O.; Lipkin, !1V.M.; Sverdlov, E.D. !$#journal Bioorg. Khim. (1980) 6:1106-1109 !$#title Primary structure of EcoRI-F fragment of rpoB, C genes and !1corresponding fragments of beta- and beta'-subunits of RNA !1polymerase from E.coli. !$#accession I52539 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1143-1342 ##label RE4 !'##cross-references GB:M38293; NID:g147721; PIDN:AAA24581.1; !1PID:g147722 GENETICS !$#gene rpoB !$#map_position 90 min COMPLEX the active enzyme consists of the sigma chain and the core !1enzyme; the sigma chain is an initiation factor that !1promotes attachment of the enzyme to specific initiation !1sites and then is released; the core enzyme is composed of !1two alpha chains, one beta chain, and one beta' chain. FUNCTION !$#description part of the catalytic component of the active enzyme that !1catalyzes RNA synthesis using a DNA template CLASSIFICATION #superfamily DNA-directed RNA polymerase beta chain KEYWORDS nucleotidyltransferase; transcription SUMMARY #length 1342 #molecular-weight 150631 #checksum 8598 SEQUENCE /// ENTRY S32680 #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) beta chain - Buchnera aphidicola ORGANISM #formal_name Buchnera aphidicola DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S32680 REFERENCE S32679 !$#authors Clark, M.A.; Baumann, L.; Baumann, P. !$#submission submitted to the EMBL Data Library, April 1992 !$#description Sequence analysis of an aphid endosymbiont DNA fragment !1containing rpoB (beta-subunit of RNA polymerase) and !1portions of rplL and rpoC. !$#accession S32680 !'##molecule_type DNA !'##residues 1-1342 ##label CLA !'##cross-references EMBL:Z11913; NID:g296967; PIDN:CAA77970.1; !1PID:g296969 CLASSIFICATION #superfamily DNA-directed RNA polymerase beta chain KEYWORDS nucleotidyltransferase; transcription SUMMARY #length 1342 #molecular-weight 152060 #checksum 4082 SEQUENCE /// ENTRY H64073 #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) beta chain - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS H64073 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession H64073 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1343 ##label TIGR !'##cross-references GB:U32733; GB:L42023; NID:g1573493; !1PIDN:AAC22173.1; PID:g1573496; TIGR:HI0515 CLASSIFICATION #superfamily DNA-directed RNA polymerase beta chain KEYWORDS nucleotidyltransferase; transcription SUMMARY #length 1343 #molecular-weight 149783 #checksum 1685 SEQUENCE /// ENTRY RNEBBT #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) beta chain - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 11-Jun-1999 ACCESSIONS S01794 REFERENCE S01794 !$#authors Lisitsyn, N.A.; Monastyrskaya, G.S.; Sverdlov, E.D. !$#journal Eur. J. Biochem. (1988) 177:363-369 !$#title Genes coding for RNA polymerase beta subunit in bacteria. !1Structure/function analysis. !$#cross-references MUID:89052707; PMID:3056723 !$#accession S01794 !'##molecule_type DNA !'##residues 1-1342 ##label LIS !'##cross-references GB:X04642; GB:M37431; GB:X04860; GB:X13854; !1NID:g47918; PIDN:CAA28302.1; PID:g47919 GENETICS !$#gene rpoB CLASSIFICATION #superfamily DNA-directed RNA polymerase beta chain KEYWORDS nucleotidyltransferase; transcription SUMMARY #length 1342 #molecular-weight 150557 #checksum 7978 SEQUENCE /// ENTRY RNNTB #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) beta chain - common tobacco chloroplast ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 21-Jul-2000 ACCESSIONS A24865; A00690 REFERENCE A24865 !$#authors Ohme, M.; Tanaka, M.; Chunwongse, J.; Shinozaki, K.; !1Sugiura, M. !$#journal FEBS Lett. (1986) 200:87-90 !$#title A tobacco chloroplast DNA sequence possibly coding for a !1polypeptide similar to E. coli RNA polymerase beta-subunit. !$#cross-references MUID:86192857; PMID:3516726 !$#accession A24865 !'##molecule_type DNA !'##residues 1-1070 ##label OHM !'##cross-references GB:M28017; NID:g11780; PIDN:CAA31238.1; PID:g11781 REFERENCE A38013 !$#authors Shinozaki, K.; Ohme, M.; Tanaka, M.; Wakasugi, T.; !1Hayashida, N.; Matsubayashi, T.; Zaita, N.; Chunwongse, J.; !1Obokata, J.; Yamaguchi-Shinozaki, K.; Ohto, C.; Torazawa, !1K.; Meng, B.Y.; Sugita, M.; Deno, H.; Kamogashira, T.; !1Yamada, K.; Kusuda, J.; Takaiwa, F.; Kato, A.; Tohdoh, N.; !1Shimada, H.; Sugiura, M. !$#journal EMBO J. (1986) 5:2043-2049 !$#title The complete nucleotide sequence of the tobacco chloroplast !1genome: its gene organization and expression. !$#contents annotation; gene organization, sites, features GENETICS !$#gene rpoB !$#genome chloroplast CLASSIFICATION #superfamily DNA-directed RNA polymerase beta chain KEYWORDS chloroplast; nucleotidyltransferase; transcription SUMMARY #length 1070 #molecular-weight 120546 #checksum 1605 SEQUENCE /// ENTRY RNRZB #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) beta chain - rice chloroplast ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 11-Jun-1999 ACCESSIONS JQ0213; S05093 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0213 !'##molecule_type DNA !'##residues 1-1075 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05093 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1075 ##label HIR !'##cross-references EMBL:X15901; NID:g11957; PIDN:CAA33986.1; !1PID:g11971 !'##experimental_source cv. Nihonbare GENETICS !$#gene rpoB !$#map_position CP19214-22441 !$#genome chloroplast CLASSIFICATION #superfamily DNA-directed RNA polymerase beta chain KEYWORDS chloroplast; nucleotidyltransferase; transcription SUMMARY #length 1075 #molecular-weight 121641 #checksum 7923 SEQUENCE /// ENTRY RNZMB #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) beta chain - maize chloroplast ALTERNATE_NAMES RNA polymerase 120K chain ORGANISM #formal_name chloroplast Zea mays #common_name maize DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 11-Jun-1999 ACCESSIONS S12800; S58542; B34846; S08246 REFERENCE S12800 !$#authors Igloi, G.L.; Meinke, A.; Doery, I.; Koessel, H. !$#journal Mol. Gen. Genet. (1990) 221:379-394 !$#title Nucleotide sequence of the maize chloroplast rpo B/C(1)/C(2) !1operon: comparison between the derived protein primary !1structures from various organisms with respect to functional !1domains. !$#cross-references MUID:90340289; PMID:2381419 !$#accession S12800 !'##molecule_type DNA !'##residues 1-1075 ##label IGL1 !'##cross-references EMBL:X17318; NID:g12479; PIDN:CAA35195.1; !1PID:g12480 REFERENCE S58531 !$#authors Maier, R.M.; Neckermann, K.; Igloi, G.L.; Koessel, H. !$#journal J. Mol. Biol. (1995) 251:614-628 !$#title Complete sequence of the maize chloroplast genome: gene !1content, hotspots of divergence and fine tuning of genetic !1information by transcript editing. !$#cross-references MUID:95395841; PMID:7666415 !$#accession S58542 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1075 ##label MAI !'##cross-references EMBL:X86563; NID:g902200; PIDN:CAA60276.1; !1PID:g902212 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1995 REFERENCE A34846 !$#authors Hu, J.; Bogorad, L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:1531-1535 !$#title Maize chloroplast RNA polymerase: the 180-, 120-, and !138-kilodalton polypeptides are encoded in chloroplast genes. !$#cross-references MUID:90160360; PMID:2304916 !$#accession B34846 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-18 ##label HUJ GENETICS !$#gene rpoB !$#genome chloroplast CLASSIFICATION #superfamily DNA-directed RNA polymerase beta chain KEYWORDS chloroplast; nucleotidyltransferase; transcription SUMMARY #length 1075 #molecular-weight 121570 #checksum 3641 SEQUENCE /// ENTRY RNLVB #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) beta chain - liverwort (Marchantia polymorpha) chloroplast ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 11-Jun-1999 ACCESSIONS A00691; S01573 REFERENCE A00150 !$#authors Ohyama, K. !$#submission submitted to the EMBL Data Library, October 1986 !$#accession A00691 !'##molecule_type DNA !'##residues 1-1065 ##label OHY REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features REFERENCE S01567 !$#authors Umesono, K.; Inokuchi, H.; Shiki, Y.; Takeuchi, M.; Chang, !1Z.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Ohyama, K.; Ozeki, !1H. !$#journal J. Mol. Biol. (1988) 203:299-331 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. II. Gene organization of the large !1single copy region from rps'12 to atpB. !$#cross-references MUID:89068686; PMID:2974085 !$#accession S01573 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-1065 ##label UME !'##cross-references GB:X04465; GB:Y00686; NID:g11640; PIDN:CAA28061.1; !1PID:g11647 GENETICS !$#gene rpoB !$#genome chloroplast CLASSIFICATION #superfamily DNA-directed RNA polymerase beta chain KEYWORDS chloroplast; nucleotidyltransferase; transcription SUMMARY #length 1065 #molecular-weight 120446 #checksum 6996 SEQUENCE /// ENTRY RNEGB #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) beta chain - Euglena gracilis chloroplast ORGANISM #formal_name chloroplast Euglena gracilis DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 11-Jun-1999 ACCESSIONS S09210 REFERENCE S09210 !$#authors Yepiz-Plascencia, G.M.; Radebaugh, C.A.; Hallick, R.B. !$#journal Nucleic Acids Res. (1990) 18:1869-1878 !$#title The Euglena gracilis chloroplast rpoB gene. Novel gene !1organization and transcription of the RNA polymerase subunit !1operon. !$#cross-references MUID:90245579; PMID:2110656 !$#accession S09210 !'##molecule_type DNA !'##residues 1-1082 ##label YEP !'##cross-references EMBL:X17191; NID:g11501; PIDN:CAA35052.1; !1PID:g311709 !'##note the authors translated the codon CGT for residue 132 as Gly GENETICS !$#gene rpoB !$#genome chloroplast !$#introns 13/3; 89/2; 117/1; 154/3; 227/3; 241/1; 288/2; 732/3 CLASSIFICATION #superfamily DNA-directed RNA polymerase beta chain KEYWORDS chloroplast; nucleotidyltransferase; transcription SUMMARY #length 1082 #molecular-weight 124531 #checksum 6067 SEQUENCE /// ENTRY RNZQBF #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) beta chain - Plasmodium falciparum plastid ORGANISM #formal_name plastid Plasmodium falciparum DATE 31-Dec-1990 #sequence_revision 15-May-1998 #text_change 16-Jun-2000 ACCESSIONS S72282; S10438 REFERENCE S72277 !$#authors Wilson, R.J.M.; Denny, P.W.; Preiser, P.R.; Rangachari, K.; !1Roberts, K.; Roy, A.; Whyte, A.; Strath, M.; Moore, D.J.; !1Moore, P.W.; Williamson, D.H. !$#journal J. Mol. Biol. (1996) 261:155-172 !$#title Complete gene map of the plastid-like DNA of the malaria !1parasite Plasmodium falciparum. !$#cross-references MUID:96346169; PMID:8757284 !$#accession S72282 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1024 ##label WIL !'##cross-references EMBL:X95275; NID:g1171583; PIDN:CAA64572.1; !1PID:g1171587 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1996 REFERENCE S10438 !$#authors Gardner, M.J.; Williamson, D.H.; Wilson, R.J.M. !$#submission submitted to the EMBL Data Library, March 1990 !$#accession S10438 !'##molecule_type DNA !'##residues 328-1024 ##label GAR !'##cross-references EMBL:X52177; NID:g9879; PIDN:CAA36427.1; PID:g9880 GENETICS !$#gene rpoB !$#genome plastid !$#note this apparently degenerate plastid is referred to as the !1apicoplast CLASSIFICATION #superfamily DNA-directed RNA polymerase beta chain KEYWORDS nucleotidyltransferase; plastid; transcription SUMMARY #length 1024 #molecular-weight 122185 #checksum 4893 SEQUENCE /// ENTRY RNZQ2L #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) II large chain - malaria parasite (Plasmodium falciparum) ORGANISM #formal_name Plasmodium falciparum DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 09-Jun-2000 ACCESSIONS S07485 REFERENCE S07485 !$#authors Li, W.B.; Bzik, D.J.; Gu, H.; Tanaka, M.; Fox, B.A.; !1Inselburg, J. !$#journal Nucleic Acids Res. (1989) 17:9621-9636 !$#title An enlarged largest subunit of Plasmodium falciparum RNA !1polymerase II defines conserved and variable RNA polymerase !1domains. !$#cross-references MUID:90098832; PMID:2690004 !$#accession S07485 !'##molecule_type DNA !'##residues 1-2452 ##label LIW !'##cross-references EMBL:X16561; NID:g9942; PIDN:CAA34560.1; PID:g9943 GENETICS !$#map_position 3 CLASSIFICATION #superfamily Plasmodium DNA-directed RNA polymerase II large !1chain KEYWORDS DNA binding; nucleotidyltransferase; phosphoprotein; tandem !1repeat; transcription; zinc finger FEATURE !$68-84 #region zinc finger CCHH motif\ !$2247-2384 #region 7-residue repeats\ !$376 #binding_site ATP/GTP (Lys) #status predicted SUMMARY #length 2452 #molecular-weight 278166 #checksum 3852 SEQUENCE /// ENTRY S21054 #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) II largest chain - human ALTERNATE_NAMES DNA-directed RNA polymerase B largest chain ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S21054; S18987 REFERENCE S21054 !$#authors Wintzerith, M.; Acker, J.; Vicaire, S.; Vigneron, M.; !1Kedinger, C. !$#journal Nucleic Acids Res. (1992) 20:910 !$#title Complete sequence of the human RNA polymerase II largest !1subunit. !$#cross-references MUID:92178992; PMID:1542581 !$#accession S21054 !'##molecule_type mRNA !'##residues 1-1970 ##label WIN !'##cross-references EMBL:X63564; NID:g36123; PIDN:CAA45125.1; !1PID:g36124 GENETICS !$#gene GDB:POLR2A; POLRA !'##cross-references GDB:120306; OMIM:180660 !$#map_position 17p13.1-17p13.1 CLASSIFICATION #superfamily human DNA-directed RNA polymerase II largest !1chain KEYWORDS DNA binding; nucleotidyltransferase; tandem repeat; !1transcription; zinc finger FEATURE !$71-87 #region zinc finger CCHH motif SUMMARY #length 1970 #molecular-weight 217204 #checksum 3419 SEQUENCE /// ENTRY A28490 #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) II largest chain - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A28490; A23566 REFERENCE A28490 !$#authors Ahearn Jr., J.M.; Bartolomei, M.S.; West, M.L.; Cisek, L.J.; !1Corden, J.L. !$#journal J. Biol. Chem. (1987) 262:10695-10705 !$#title Cloning and sequence analysis of the mouse genomic locus !1encoding the largest subunit of RNA polymerase II. !$#cross-references MUID:87280135; PMID:3038894 !$#accession A28490 !'##molecule_type DNA !'##residues 1-1932 ##label AHE !'##cross-references GB:M14101 REFERENCE A23566 !$#authors Corden, J.L.; Cadena, D.L.; Ahearn Jr., J.M.; Dahmus, M.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:7934-7938 !$#title A unique structure at the carboxyl terminus of the largest !1subunit of eukaryotic RNA polymerase II. !$#cross-references MUID:86068017; PMID:2999785 !$#accession A23566 !'##molecule_type mRNA !'##residues 1549-1932 ##label COR !'##cross-references GB:M12130 GENETICS !$#gene RPII215 CLASSIFICATION #superfamily human DNA-directed RNA polymerase II largest !1chain KEYWORDS DNA binding; nucleotidyltransferase; tandem repeat; !1transcription; zinc finger SUMMARY #length 1932 #molecular-weight 213479 #checksum 5370 SEQUENCE /// ENTRY RNFF2L #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) II 215K chain [validated] - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 04-Dec-1986 #sequence_revision 31-Mar-1993 #text_change 28-Jul-2000 ACCESSIONS S04457; A00693; B27677; S60151 REFERENCE S04457 !$#authors Jokerst, R.S.; Weeks, J.R.; Zehring, W.A.; Greenleaf, A.L. !$#journal Mol. Gen. Genet. (1989) 215:266-275 !$#title Analysis of the gene encoding the largest subunit of RNA !1polymerase II in Drosophila. !$#cross-references MUID:89218930; PMID:2496296 !$#accession S04457 !'##molecule_type DNA !'##residues 1-1896 ##label JOK !'##cross-references EMBL:M27431; NID:g158331; PIDN:AAA28868.1; !1PID:g158332 REFERENCE A00693 !$#authors Biggs, J.; Searles, L.L.; Greenleaf, A.L. !$#journal Cell (1985) 42:611-621 !$#title Structure of the eukaryotic transcription apparatus: !1features of the gene for the largest subunit of Drosophila !1RNA polymerase II. !$#cross-references MUID:85282618; PMID:2992806 !$#accession A00693 !'##molecule_type DNA !'##residues 1-318,'GYAKV',325-449,'G',451-454,'RCTT',459-462, !1'VTGESVASS' ##label BIG !'##cross-references EMBL:M11798 !'##note this sequence has been revised in reference S04457 !'##note the authors translated the codon AAC for residue 451 as Thr REFERENCE A93104 !$#authors Allison, L.A.; Wong, J.K.C.; Fitzpatrick, V.D.; Moyle, M.; !1Ingles, C.J. !$#journal Mol. Cell. Biol. (1988) 8:321-329 !$#title The C-terminal domain of the largest subunit of RNA !1polymerase II of Saccharomyces cerevisiae, Drosophila !1melanogaster, and mammals: a conserved structure with an !1essential function. !$#cross-references MUID:88094402; PMID:3122024 !$#accession B27677 !'##molecule_type DNA !'##residues 1441-1484;'I',1527-1889 ##label ALL !'##cross-references EMBL:M19537; NID:g158147; PIDN:AAA28827.1; !1PID:g158148 REFERENCE S60151 !$#authors Petersen, G.; Song, D.; Huegle-Doerr, B.; Oldenburg, I.; !1Bautz, E.K.F. !$#journal Mol. Gen. Genet. (1995) 249:425-431 !$#title Mapping of linear epitopes recognized by monoclonal !1antibodies with gene-fragment phage display libraries. !$#cross-references MUID:96133682; PMID:8552047 !$#accession S60151 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 778-827 ##label PET GENETICS !$#gene RPO21; RpII215 !'##cross-references FlyBase:FBgn0003277 !$#map_position X 10C, X 35.7 !$#introns 27/3; 775/3; 1526/1 FUNCTION !$#description EC 2.7.7.6 [validated, MUID:88094402]; essential for proper !1initiation of transcription CLASSIFICATION #superfamily human DNA-directed RNA polymerase II largest !1chain KEYWORDS DNA binding; nucleotidyltransferase; tandem repeat; !1transcription; zinc finger FEATURE !$67-83 #region zinc finger CCHH motif\ !$1581-1883 #region 7-residue repeats\ !$349 #binding_site ATP/GTP (Lys) #status predicted SUMMARY #length 1896 #molecular-weight 210045 #checksum 5473 SEQUENCE /// ENTRY A34092 #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) II large chain - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A34092 REFERENCE A34092 !$#authors Bird, D.M.; Riddle, D.L. !$#journal Mol. Cell. Biol. (1989) 9:4119-4130 !$#title Molecular cloning and sequencing of ama-1, the gene encoding !1the largest subunit of Caenorhabditis elegans RNA polymerase !1II. !$#cross-references MUID:90066416; PMID:2586513 !$#accession A34092 !'##status preliminary !'##molecule_type DNA !'##residues 1-1859 ##label BIR !'##cross-references GB:M29235; NID:g156404; PIDN:AAA28126.1; !1PID:g156405 !'##note the authors failed to translated the codon GAG for residue 917 !1as Glu, and CAT for residue 1392 as His CLASSIFICATION #superfamily human DNA-directed RNA polymerase II largest !1chain KEYWORDS DNA binding; nucleotidyltransferase; tandem repeat; !1transcription; zinc finger SUMMARY #length 1859 #molecular-weight 204631 #checksum 3511 SEQUENCE /// ENTRY JDMU1 #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) II largest chain - Arabidopsis thaliana ALTERNATE_NAMES DNA-directed RNA polymerase II 205K chain; protein F4B14.70 ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 31-Mar-1993 #sequence_revision 11-Jun-1999 #text_change 20-Aug-1999 ACCESSIONS T04690; S12071; S27346; S11960 REFERENCE Z15380 !$#authors Bevan, M.; Rose, M.; Hempel, S.; Entian, K.D.; Hoheisel, J.; !1Mewes, H.W.; Mayer, K.F.X.; Schueller, C. !$#submission submitted to the Protein Sequence Database, October 1998 !$#accession T04690 !'##molecule_type DNA !'##residues 1-1834 ##label BEV !'##cross-references EMBL:AL031986 !'##experimental_source cultivar Columbia; BAC clone F4B14 REFERENCE S12071 !$#authors Nawrath, C.; Schell, J.; Koncz, C. !$#journal Mol. Gen. Genet. (1990) 223:65-75 !$#title Homologous domains of the largest subunit of eucaryotic RNA !1polymerase II are conserved in plants. !$#cross-references MUID:91080867; PMID:2259344 !$#accession S12071 !'##molecule_type DNA !'##residues 1-421,'S',423-732,'D',734-1055,'R',1057-1714,'SPTSPSY', !11715-1834 ##label NAW1 !'##cross-references EMBL:X52954; NID:g16504; PIDN:CAA37130.1; !1PID:g16505 !'##experimental_source cv. Columbia !'##note the authors translated the codon AGC for residue 1755 as Arg !$#accession S27346 !'##molecule_type mRNA !'##residues 510-732,'D',734-1055,'R',1057-1714,'SPTSPSY',1715-1834 !1##label NAW2 !'##experimental_source cv. Columbia REFERENCE S11960 !$#authors Dietrich, M.A.; Prenger, J.P.; Guilfoyle, T.J. !$#journal Plant Mol. Biol. (1990) 15:207-223 !$#title Analysis of the genes encoding the largest subunit of RNA !1polymerase II in Arabidopsis and soybean. !$#cross-references MUID:91355869; PMID:2103447 !$#accession S11960 !'##molecule_type DNA !'##residues 1-116,125-192,'NSKEE',198-297,'R',299-302,'R',304-400,'KE', !1403,'VDYGPHPPPGKTGA',412-439, !1'RYVLLSYSIHSTHKRLFLEVVIFMLSWSQ',441-1082,'P',1084-1834 !1##label DIE !'##cross-references EMBL:X52494; NID:g16493; PIDN:CAA36735.1; !1PID:g16494 !'##note the authors translated the codon CCT for residue 1083 as Ala GENETICS !$#gene rpII215; RPB1 !$#map_position 4 !$#introns 28/3; 123/3; 218/3; 271/3; 325/3; 411/1; 440/3; 552/3; 648/ !12; 734/3; 1755/2; 1779/2 !$#note F4B14.70 CLASSIFICATION #superfamily human DNA-directed RNA polymerase II largest !1chain KEYWORDS DNA binding; nucleotidyltransferase; phosphoprotein; tandem !1repeat; transcription; zinc finger FEATURE !$66-109 #region zinc finger CCCC motif\ !$1531-1812 #region 7-residue repeats SUMMARY #length 1834 #molecular-weight 204222 #checksum 4118 SEQUENCE /// ENTRY S26849 #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) II largest chain - fission yeast (Schizosaccharomyces pombe) ORGANISM #formal_name Schizosaccharomyces pombe DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Dec-1999 ACCESSIONS S26849; T40055 REFERENCE S26849 !$#authors Azuma, Y.; Yamagishi, M.; Ueshima, R.; Ishihama, A. !$#journal Nucleic Acids Res. (1991) 19:461-468 !$#title Cloning and sequence determination of the !1Schizosaccharomyces pombe rpb1 gene encoding the largest !1subunit of RNA polymerase II. !$#cross-references MUID:91187661; PMID:2011520 !$#accession S26849 !'##molecule_type DNA !'##residues 1-1752 ##label AZU !'##cross-references EMBL:X56564; NID:g5054; PIDN:CAA39916.1; PID:g5055 !'##note the authors did not translate the codon for residue 1464 REFERENCE Z21902 !$#authors McDougall, R.C.; Rajandream, M.A.; Barrell, B.G.; Stevens, !1K.; Badcock, K.; Churcher, C.M. !$#submission submitted to the EMBL Data Library, October 1999 !$#accession T40055 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-1752 ##label MCD !'##cross-references EMBL:AL121795; PIDN:CAB57941.1; GSPDB:GN00067; !1SPDB:SPBC28F2.12 !'##experimental_source strain 972h-; cosmid c28F2 GENETICS !$#gene SPBC28F2.12 !$#map_position 2 !$#introns 5/3; 14/2; 38/3; 64/1; 84/1; 119/3 CLASSIFICATION #superfamily human DNA-directed RNA polymerase II largest !1chain KEYWORDS DNA binding; nucleotidyltransferase; tandem repeat; !1transcription; zinc finger SUMMARY #length 1752 #molecular-weight 194161 #checksum 8039 SEQUENCE /// ENTRY RNBY2L #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) II 215K chain - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein D2150; protein YDL140c; RNA polymerase II largest chain ORGANISM #formal_name Saccharomyces cerevisiae DATE 04-Dec-1986 #sequence_revision 23-Aug-1996 #text_change 21-Jul-2000 ACCESSIONS S67686; A00692; S64647; S20985 REFERENCE S67677 !$#authors Saluz, H.P.; Woelfl, S.; Hanemann, V. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67686 !'##molecule_type DNA !'##residues 1-1733 ##label SAL !'##cross-references EMBL:Z74188; NID:g1431216; PIDN:CAA98713.1; !1PID:g1431217; GSPDB:GN00004; MIPS:YDL140c !'##experimental_source strain S288C REFERENCE A90870 !$#authors Allison, L.A.; Moyle, M.; Shales, M.; Ingles, C.J. !$#journal Cell (1985) 42:599-610 !$#title Extensive homology among the largest subunits of eukaryotic !1and prokaryotic RNA polymerases. !$#cross-references MUID:85282617; PMID:3896517 !$#accession A00692 !'##molecule_type DNA !'##residues 1-1513,'V',1515-1523,'A',1525-1555,1563-1607,'M',1609-1733 !1##label ALL !'##cross-references EMBL:X03128; NID:g4397; PIDN:CAA26904.1; PID:g4398 REFERENCE S64646 !$#authors Cronan Jr., J.E.; Wallace, J.C. !$#journal FEMS Microbiol. Lett. (1995) 130:221-230 !$#title The gene encoding the biotin-apoprotein ligase of !1Saccharomyces cerevisiae. !$#cross-references MUID:95377607; PMID:7649444 !$#accession S64647 !'##status translation not shown !'##molecule_type DNA !'##residues 1669-1733 ##label CRO !'##cross-references EMBL:U27182; NID:g886080; PIDN:AAC49058.1; !1PID:g886082 GENETICS !$#gene SGD:RPO21; MIPS:YDL140c !'##cross-references SGD:S0002299; MIPS:YDL140c !$#map_position 4L CLASSIFICATION #superfamily human DNA-directed RNA polymerase II largest !1chain KEYWORDS DNA binding; nucleotidyltransferase; tandem repeat; !1transcription; zinc finger FEATURE !$1567-1733 #region 7-residue repeats SUMMARY #length 1733 #molecular-weight 191610 #checksum 5698 SEQUENCE /// ENTRY A34374 #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) I largest chain - Trypanosoma brucei ORGANISM #formal_name Trypanosoma brucei DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A34374; S19264; S04272; S06857 REFERENCE A34374 !$#authors Smith, J.L.; Levin, J.R.; Agabian, N. !$#journal J. Biol. Chem. (1989) 264:18091-18099 !$#title Molecular characterization of the Trypanosoma brucei RNA !1polymerase I and III largest subunit genes. !$#cross-references MUID:90036885; PMID:2808366 !$#accession A34374 !'##status preliminary !'##molecule_type DNA !'##residues 1-1781 ##label SMI !'##cross-references GB:M27164; NID:g162218; PIDN:AAA30231.1; !1PID:g162219; GB:J05074 REFERENCE S19264 !$#authors Cornelissen, A.W.C.A. !$#submission submitted to the EMBL Data Library, September 1989 !$#accession S19264 !'##molecule_type DNA !'##residues 38-1506,'G',1508-1576,'A',1578-1781 ##label COR !'##cross-references EMBL:X14399; NID:g10521; PIDN:CAA32572.1; !1PID:g10522 !'##note this is a revision to the sequence from reference S04272 REFERENCE S06857 !$#authors Jess, W.; Hammer, A.; Cornelissen, A.W.C.A. !$#journal FEBS Lett. (1989) 258:180A !$#contents annotation; erratum !$#note this is a revision to the sequence from reference S04272 REFERENCE S04272 !$#authors Jess, W.; Hammer, A.; Cornelissen, A.W.C.A. !$#journal FEBS Lett. (1989) 249:123-128 !$#title Complete sequence of the gene encoding the largest subunit !1of RNA polymerase I of Trypanosoma brucei. !$#cross-references MUID:89252063; PMID:2542092 !$#accession S04272 !'##molecule_type DNA !'##residues 38-1506,'G',1508-1576,'A',1578-1646,1779-1780, !1'TKLAPLIFGIWEHTSALSLDTLRFTMSSINYSTATMSTRGTCRSSPIRLPTEGDGRTSI !1SLVSYQRARAHCFR' ##label JES !'##cross-references EMBL:X14399 !'##note the difference at the carboxyl end is due to a frameshift !1error; this sequence has been revised in reference S19264 GENETICS !$#gene trp11 CLASSIFICATION #superfamily Trypanosoma DNA-directed RNA polymerase I !1largest chain KEYWORDS DNA binding; nucleotidyltransferase; nucleus; transcription; !1zinc finger SUMMARY #length 1781 #molecular-weight 195903 #checksum 9711 SEQUENCE /// ENTRY S22812 #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) III largest chain - Giardia lamblia ORGANISM #formal_name Giardia lamblia DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S22812 REFERENCE S22811 !$#authors Lanzendoerfer, M.; Palm, P.; Grampp, B.; Peattie, D.A.; !1Zillig, W. !$#journal Nucleic Acids Res. (1992) 20:1145 !$#title Nucleotide sequence of the gene encoding the largest subunit !1of the DNA-dependent RNA polymerase III of Giardia lamblia. !$#cross-references MUID:92195823; PMID:1549483 !$#accession S22812 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1735 ##label LAN !'##cross-references EMBL:X60325 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1September 1991 GENETICS !$#gene rpoA3 CLASSIFICATION #superfamily Giardia DNA-directed RNA polymerase III largest !1chain KEYWORDS DNA binding; nucleotidyltransferase; nucleus; transcription; !1zinc finger SUMMARY #length 1735 #molecular-weight 193191 #checksum 769 SEQUENCE /// ENTRY RNBY3L #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) III 160K chain - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein O3254; protein YOR116c; protein YOR3254c ORGANISM #formal_name Saccharomyces cerevisiae DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 21-Jul-2000 ACCESSIONS A00694; S61002; S61674; S67001; S63879 REFERENCE A90870 !$#authors Allison, L.A.; Moyle, M.; Shales, M.; Ingles, C.J. !$#journal Cell (1985) 42:599-610 !$#title Extensive homology among the largest subunits of eukaryotic !1and prokaryotic RNA polymerases. !$#cross-references MUID:85282617; PMID:3896517 !$#accession A00694 !'##molecule_type DNA !'##residues 1-1460 ##label ALL !'##cross-references EMBL:X03129; NID:g4399; PIDN:CAA26905.1; PID:g4400 REFERENCE S60983 !$#authors Wiemann, S.; Rechmann, S.; Benes, V.; Voss, H.; Schwager, !1C.; Vlcek, C.; Stegemann, J.; Zimmermann, J.; Erfle, H.; !1Paces, V.; Ansorge, W. !$#submission submitted to the EMBL Data Library, August 1995 !$#description Sequencing of 51 kilobases on the right arm of chromosome XV !1from S. cerevisiae reveals 30 open reading frames. !$#accession S61002 !'##molecule_type DNA !'##residues 1-1460 ##label WIE !'##cross-references EMBL:X90518; NID:g1050808; PIDN:CAA62123.1; !1PID:g1050828 REFERENCE S61643 !$#authors Benes, V.; Andrade, M.A.; Rechmann, S.; Teodoru, C.; !1Banrevi, A.; Sander, C.; Valencia, A.; Ansorge, W.; Voss, H. !$#submission submitted to the EMBL Data Library, December 1995 !$#description Nucleotide sequence and analysis of a 130 kb fragment of !1yeast chromosome XV. !$#accession S61674 !'##molecule_type DNA !'##residues 1-1460 ##label BEN !'##cross-references EMBL:X94335; NID:g1262139; PIDN:CAA64036.1; !1PID:g1164961 REFERENCE S66965 !$#authors Voss, H.; Benes, V.; Rechmann, S.; Teodoru, C.; Schwager, !1C.; Paces, V.; Ansorge, W. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67001 !'##molecule_type DNA !'##residues 1-1460 ##label VOS !'##cross-references EMBL:Z75024; NID:g1420308; PIDN:CAA99314.1; !1PID:g1420309; GSPDB:GN00015; MIPS:YOR116c !'##experimental_source strain S288C REFERENCE S63860 !$#authors Wiemann, S.; Rechmann, S.; Benes, V.; Voss, H.; Schwager, !1C.; Vlcek, C.; Stegemann, J.; Zimmermann, J.; Erfle, H.; !1Paces, V.; Ansorge, W. !$#journal Yeast (1996) 12:281-288 !$#title Sequencing and analysis of 51 kb on the right arm of !1chromosome XV from Saccharomyces cerevisiae reveals 30 open !1reading frames. !$#cross-references MUID:97060020; PMID:8904341 !$#accession S63879 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1460 ##label WIW !'##cross-references EMBL:X90518; NID:g1050808; PIDN:CAA62123.1; !1PID:g1050828 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1995 COMMENT The 160K polypeptide is the largest component of the yeast !1RNA polymerase III, a zinc-containing enzyme that catalyzes !1the transcription of 5S and tRNA genes. GENETICS !$#gene SGD:RPO31; MIPS:YOR116c !'##cross-references SGD:S0005642; MIPS:YOR116c !$#map_position 15R CLASSIFICATION #superfamily yeast DNA-directed RNA polymerase III 160K !1chain KEYWORDS DNA binding; nucleotidyltransferase; nucleus; transcription; !1zinc finger SUMMARY #length 1460 #molecular-weight 162300 #checksum 1894 SEQUENCE /// ENTRY S01393 #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) III 170K chain - Trypanosoma brucei brucei ORGANISM #formal_name Trypanosoma brucei brucei DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S01393 REFERENCE S01393 !$#authors Koeck, J.; Evers, R.; Cornelissen, A.W.C.A. !$#journal Nucleic Acids Res. (1988) 16:8753-8772 !$#title Structure and sequence of the gene for the largest subunit !1of trypanosomal RNA polymerase III. !$#cross-references MUID:89016560; PMID:3174432 !$#accession S01393 !'##molecule_type DNA !'##residues 1-1530 ##label KOE !'##cross-references EMBL:X12494; NID:g10523; PIDN:CAA31014.1; !1PID:g10524 CLASSIFICATION #superfamily yeast DNA-directed RNA polymerase III 160K !1chain KEYWORDS DNA binding; nucleotidyltransferase; nucleus; transcription; !1zinc finger SUMMARY #length 1530 #molecular-weight 170271 #checksum 1284 SEQUENCE /// ENTRY RNECC #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) beta' chain - Escherichia coli (strain K-12) ALTERNATE_NAMES transcriptase beta' chain ORGANISM #formal_name Escherichia coli DATE 18-Aug-1982 #sequence_revision 17-Dec-1982 #text_change 01-Mar-2002 ACCESSIONS A00695; I52543; I65347; I52544; I65348; G65205; A00696 REFERENCE A00695 !$#authors Ovchinnikov, Y.A.; Monastyrskaya, G.S.; Gubanov, V.V.; !1Guryev, S.O.; Salomatina, I.S.; Shuvaeva, T.M.; Lipkin, !1V.M.; Sverdlov, E.D. !$#journal Nucleic Acids Res. (1982) 10:4035-4044 !$#title The primary structure of Escherichia coli RNA polymerase. !1Nucleotide sequence of the rpoC gene and amino acid sequence !1of the beta'-subunit. !$#cross-references MUID:82274235; PMID:6287430 !$#accession A00695 !'##molecule_type DNA !'##residues 1-1407 ##label OVC !'##note the authors translated the codon GAA for residues 295 as Gly !'##note most of this sequence was confirmed by amino acid analysis REFERENCE I52543 !$#authors Ovchinnikov, Y.A.; Monastyrskaya, G.S.; Gubanov, V.V.; !1Salomatina, I.S.; Shuvaeva, T.M.; Lipkin, V.M.; Sverdlov, !1E.D. !$#journal Bioorg. Khim. (1981) 7:1107-1112 !$#title Primary structure of RNA polymerase from E.coli. Nucleotide !1sequence of E.coli DNA fragment containing a part of the !1rpoC gene and the corresponding C-terminal amino acid !1sequence of beta-' subunit. !$#accession I52543 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 987-1407 ##label RES !'##cross-references GB:M38288; NID:g147323; PIDN:AAA24408.1; !1PID:g147324 REFERENCE I52539 !$#authors Monastyrskaya, G.S.; Gubanov, V.V.; Guryev, S.O.; Lipkin, !1V.M.; Sverdlov, E.D. !$#journal Bioorg. Khim. (1980) 6:1106-1109 !$#title Primary structure of EcoRI-F fragment of rpoB, C genes and !1corresponding fragments of beta- and beta'-subunits of RNA !1polymerase from E.coli. !$#accession I65347 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-176 ##label RE2 !'##cross-references GB:M38293; NID:g147721; PIDN:AAA24582.1; !1PID:g147723 REFERENCE I52544 !$#authors Monastyrskaya, G.S.; Guryev, S.O.; Kalinina, N.F.; Sorokin, !1A.V.; Salomatina, I.S.; Shuvaeva, T.M.; Lipkin, V.M.; !1Sverdlov, E.D.; Ovchinnikov, Y.A. !$#journal Bioorg. Khim. (1982) 8:130-134 !$#title Primary structure of EcoRI-D fragment of rpoC gene and !1corresponding fragment of beta-subunit of RNA polymerase !1from E.coli. !$#accession I52544 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 175-864,'Q',866-988 ##label RE3 !'##cross-references GB:M38305; NID:g147729; PIDN:AAA24586.1; !1PID:g147730 REFERENCE I52541 !$#authors Gurevich, A.I.; Igoshin, A.V.; Kolosov, M.N. !$#journal Bioorg. Khim. (1980) 6:1580-1584 !$#title Structure of a central part of E.coli operon rpoBC. !1Nucleotide sequence of the gene for beta subunit of RNA !1polymerase. !$#accession I65348 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-12,'E',14-18,'T',20-21,'V',23-24,'V',26-67,'H',69,'RPR', !173-91,'A',93-102,'S',104-113,'M',115-150,'V',152-176 ##label !1RE4 !'##cross-references GB:M38303; NID:g147724; PIDN:AAA24584.1; !1PID:g147726 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65205 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-1407 ##label BLAT !'##cross-references GB:AE000472; GB:U00096; NID:g2367333; !1PIDN:AAC76962.1; PID:g2367335; UWGP:b3988 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A00696 !$#authors Squires, C.; Krainer, A.; Barry, G.; Shen, W.F.; Squires, !1C.L. !$#journal Nucleic Acids Res. (1981) 9:6827-6840 !$#title Nucleotide sequence at the end of the gene for the RNA !1polymerase beta' subunit (rpoC). !$#cross-references MUID:82150271; PMID:6278450 !$#accession A00696 !'##molecule_type DNA !'##residues 1073-1132,'ASPVVCRALRTCSKHVVRKSRQSWLKSAVSFPSVKKPKVNVVWLS', !11178-1383,'G',1385-1407 ##label SQU !'##experimental_source strain K12 GENETICS !$#gene rpoC !$#map_position 90 min COMPLEX the enzyme consists of the sigma chain and the core enzyme; !1the sigma chain is an initiation factor that promotes !1attachment of the enzyme to specific initiation sites and !1then is released; the core enzyme is composed of two alpha !1chains, one beta chain, and one beta' chain FUNCTION !$#description the DNA-directed RNA polymerase, also called transcriptase, !1catalyzes RNA synthesis using a DNA template CLASSIFICATION #superfamily Escherichia coli DNA-directed RNA polymerase !1beta' chain KEYWORDS nucleotidyltransferase; transcription SUMMARY #length 1407 #molecular-weight 155159 #checksum 2789 SEQUENCE /// ENTRY G64073 #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) beta' chain - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 18-Aug-1995 #sequence_revision 18-Aug-1995 #text_change 11-Jun-1999 ACCESSIONS G64073 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession G64073 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1415 ##label TIGR !'##cross-references GB:U32733; GB:L42023; NID:g1573493; !1PIDN:AAC22172.1; PID:g1573495; TIGR:HI0514 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily Escherichia coli DNA-directed RNA polymerase !1beta' chain KEYWORDS nucleotidyltransferase; transcription SUMMARY #length 1415 #molecular-weight 157209 #checksum 4059 SEQUENCE /// ENTRY RNVZ47 #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) 147K chain - vaccinia virus ALTERNATE_NAMES J6R protein ORGANISM #formal_name vaccinia virus DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 11-Jun-1999 ACCESSIONS B25734; I42513; A37518; J23092 REFERENCE A25734 !$#authors Broyles, S.S.; Moss, B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:3141-3145 !$#title Homology between RNA polymerases of poxviruses, prokaryotes, !1and eukaryotes: nucleotide sequence and transcriptional !1analysis of vaccinia virus genes encoding 147-kDa and 22-kDa !1subunits. !$#cross-references MUID:86205852; PMID:3517852 !$#accession B25734 !'##molecule_type DNA !'##residues 1-1287 ##label BRO !'##cross-references GB:M13209; NID:g335739; PIDN:AAB59835.1; !1PID:g335741 !'##experimental_source strain WR REFERENCE A42501 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:517-563 !$#title Appendix to "The complete DNA sequence of vaccinia virus". !$#accession I42513 !'##molecule_type DNA !'##residues 1-488,'K',490-1005,'NITLRKET',1015-1024,'R',1026-1113,'D', !11115-1287 ##label GOE !'##cross-references GB:M35027; NID:g335317; PIDN:AAA48086.1; !1PID:g335434 !'##experimental_source strain Copenhagen REFERENCE A42531 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:247-266 !$#title The complete DNA sequence of vaccinia virus. !$#cross-references MUID:91021027; PMID:2219722 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given REFERENCE A23092 !$#authors Plucienniczak, A.; Schroeder, E.; Zettlmeissl, G.; Streeck, !1R.E. !$#journal Nucleic Acids Res. (1985) 13:985-998 !$#title Nucleotide sequence of a cluster of early and late genes in !1a conserved segment of the vaccinia virus genome. !$#cross-references MUID:85215527; PMID:2987815 !$#accession A37518 !'##molecule_type DNA !'##residues 1-61,'Q',63-82,'T',84-111 ##label PLU !'##cross-references GB:X01978; GB:J02424; GB:J02425; GB:K02376; !1GB:M15211; GB:V01537; NID:g61387; PIDN:CAA26020.1; !1PID:g61399 !'##experimental_source strain WR CLASSIFICATION #superfamily vaccinia virus DNA-directed RNA polymerase 147K !1chain KEYWORDS nucleotidyltransferase; transcription SUMMARY #length 1287 #molecular-weight 146948 #checksum 9422 SEQUENCE /// ENTRY H36845 #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) chain J6R - variola virus ALTERNATE_NAMES L6R protein ORGANISM #formal_name variola virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 23-Mar-2001 ACCESSIONS H36845; S33097 REFERENCE A36859 !$#authors Blinov, V.M. !$#submission submitted to GenBank, November 1992 !$#accession H36845 !'##status preliminary !'##molecule_type DNA !'##residues 1-1286 ##label BLI !'##cross-references GB:X69198; NID:g456758; PIDN:CAA49024.1; !1PID:g297263 !'##experimental_source strain India-1967, ssp. major, isolate Ind3 REFERENCE S33069 !$#authors Shchelkunov, S.N.; Blinov, V.M.; Totmenin, A.V.; !1Marennikova, S.S.; Kolykhalov, A.A.; Frolov, I.V.; !1Chizhikov, V.E.; Gytorov, V.V.; Gashikov, P.V.; Belanov, !1E.F.; Belavin, P.A.; Resenchuk, S.M.; Andzhaparidze, O.G.; !1Sandakhchiev, L.S. !$#journal Virus Res. (1993) 27:25-35 !$#title Nucleotide sequence analysis of variola virus HindIII M, L, !1I genome fragments. !$#cross-references MUID:93190624; PMID:8383392 !$#accession S33097 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1286 ##label SHC !'##cross-references EMBL:X67119; NID:g62330; PIDN:CAA47582.1; !1PID:g62359 !'##experimental_source strain India-1967, isolate Ind3 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1992 CLASSIFICATION #superfamily vaccinia virus DNA-directed RNA polymerase 147K !1chain KEYWORDS nucleotidyltransferase; transcription SUMMARY #length 1286 #molecular-weight 146782 #checksum 2555 SEQUENCE /// ENTRY A33926 #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) chain A - Halobacterium salinarum ORGANISM #formal_name Halobacterium salinarum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A33926; S03574 REFERENCE A33926 !$#authors Puehler, G.; Leffers, H.; Gropp, F.; Palm, P.; Klenk, H.P.; !1Lottspeich, F.; Garrett, R.A.; Zillig, W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:4569-4573 !$#title Archaebacterial DNA-dependent RNA polymerases testify to the !1evolution of the eukaryotic nuclear genome. !$#cross-references MUID:89282812; PMID:2499884 !$#accession A33926 !'##status preliminary; nucleic acid sequence not shown; not compared !1with conceptual translation !'##molecule_type DNA !'##residues 1-972 ##label PUE !'##note the source is designated as Halobacterium halobium REFERENCE S03572 !$#authors Leffers, H.; Gropp, F.; Lottspeich, F.; Zillig, W.; Garrett, !1R.A. !$#journal J. Mol. Biol. (1989) 206:1-17 !$#title Sequence, organization, transcription and evolution of RNA !1polymerase subunit genes from the archaebacterial extreme !1halophiles Halobacterium halobium and Halococcus morrhuae. !$#cross-references MUID:89199633; PMID:2495365 !$#accession S03574 !'##molecule_type DNA !'##residues 1-201,'L',203-242,244,'M',246-528,'F',530-697,'M',699-972 !1##label LEF !'##cross-references EMBL:X57144; NID:g43538; PIDN:CAA40426.1; !1PID:g43542 !'##note the source is designated as Halobacterium halobium CLASSIFICATION #superfamily Halobacterium DNA-directed RNA polymerase chain !1A KEYWORDS nucleotidyltransferase; transcription SUMMARY #length 972 #molecular-weight 108735 #checksum 8979 SEQUENCE /// ENTRY S02196 #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) chain A - Methanobacterium thermoautotrophicum (strain Winter) ORGANISM #formal_name Methanobacterium thermoautotrophicum #variety strain Winter DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 18-Feb-2000 ACCESSIONS S02196 REFERENCE S02194 !$#authors Berghoefer, B.; Kroeckel, L.; Koertner, C.; Truss, M.; !1Schallenberg, J.; Klein, A. !$#journal Nucleic Acids Res. (1988) 16:8113-8128 !$#title Relatedness of archaebacterial RNA polymerase core subunits !1to their eubacterial and eukaryotic equivalents. !$#cross-references MUID:88335550; PMID:2843811 !$#accession S02196 !'##molecule_type DNA !'##residues 1-865 ##label BER !'##cross-references EMBL:X08038; NID:g44664; PIDN:CAA30838.1; !1PID:g809727 GENETICS !$#start_codon TTG CLASSIFICATION #superfamily Halobacterium DNA-directed RNA polymerase chain !1A KEYWORDS nucleotidyltransferase; transcription SUMMARY #length 865 #molecular-weight 97518 #checksum 7668 SEQUENCE /// ENTRY S25564 #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) chain A' - Thermococcus celer ALTERNATE_NAMES DNA-dependent RNA polymerase chain A' ORGANISM #formal_name Thermococcus celer DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S25564; S27299 REFERENCE S25562 !$#authors Klenk, H.P.; Schwass, V.; Lottspeich, F.; Zillig, W. !$#journal Nucleic Acids Res. (1992) 20:4659 !$#title Nucleotide sequence of the genes encoding the three largest !1subunits of the DNA-dependent RNA polymerase from the !1archaeum Thermococcus celer. !$#cross-references MUID:93027167; PMID:1408768 !$#accession S25564 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-905 ##label KLE !'##cross-references EMBL:X67313; NID:g48138; PIDN:CAA47723.1; !1PID:g48141 !'##experimental_source DSM 2476 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1992 REFERENCE S27298 !$#authors Lottspeich, F. !$#submission submitted to the Protein Sequence Database, February 1993 !$#accession S27299 !'##molecule_type protein !'##residues 2-18 ##label LOT GENETICS !$#gene rpoA1 CLASSIFICATION #superfamily Halobacterium DNA-directed RNA polymerase chain !1A KEYWORDS nucleotidyltransferase; transcription FEATURE !$2-905 #product DNA-directed RNA polymerase chain A' #status !8experimental #label MAT SUMMARY #length 905 #molecular-weight 102724 #checksum 5146 SEQUENCE /// ENTRY S47162 #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) - Methanococcus vannielii ORGANISM #formal_name Methanococcus vannielii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S47162 REFERENCE S47159 !$#authors Palm, P.; Arnold-Ammer, I.; Lechner, K.A.; Zillig, W. !$#submission submitted to the EMBL Data Library, June 1993 !$#description DNA sequence of the genes of the large subunits of the DNA !1dependent RNA-polymerase of Methanococcus vannielii. !$#accession S47162 !'##molecule_type DNA !'##residues 1-889 ##label PAL !'##cross-references EMBL:X73293; NID:g505288; PIDN:CAA51728.1; !1PID:g505292 CLASSIFICATION #superfamily Halobacterium DNA-directed RNA polymerase chain !1A KEYWORDS nucleotidyltransferase; transcription SUMMARY #length 889 #molecular-weight 99097 #checksum 3507 SEQUENCE /// ENTRY B33926 #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) chain A [validated] - Sulfolobus acidocaldarius ORGANISM #formal_name Sulfolobus acidocaldarius DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 18-Aug-2000 ACCESSIONS B33926; S04717 REFERENCE A33926 !$#authors Puehler, G.; Leffers, H.; Gropp, F.; Palm, P.; Klenk, H.P.; !1Lottspeich, F.; Garrett, R.A.; Zillig, W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:4569-4573 !$#title Archaebacterial DNA-dependent RNA polymerases testify to the !1evolution of the eukaryotic nuclear genome. !$#cross-references MUID:89282812; PMID:2499884 !$#accession B33926 !'##status preliminary; nucleic acid sequence not shown; not compared !1with conceptual translation !'##molecule_type DNA !'##residues 1-880 ##label PUE REFERENCE S04714 !$#authors Puehler, G.; Lottspeich, F.; Zillig, W. !$#journal Nucleic Acids Res. (1989) 17:4517-4534 !$#title Organization and nucleotide sequence of the genes encoding !1the large subunits A, B and C of the DNA-dependent RNA !1polymerase of the archaebacterium Sulfolobus acidocaldarius. !$#cross-references MUID:89315197; PMID:2501756 !$#accession S04717 !'##molecule_type DNA !'##residues 1-311,'N',313-560,'N',562-610,'M',612-640,'M',642-880 !1##label PU2 !'##cross-references EMBL:X14818; NID:g46667; PIDN:CAA32925.1; !1PID:g46670 GENETICS !$#gene rpoA FUNCTION !$#description EC 2.7.7.6 [validated, MUID:89315197] CLASSIFICATION #superfamily Halobacterium DNA-directed RNA polymerase chain !1A KEYWORDS nucleotidyltransferase; transcription SUMMARY #length 880 #molecular-weight 99825 #checksum 9710 SEQUENCE /// ENTRY S26723 #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) chain A' - Thermoplasma acidophilum ORGANISM #formal_name Thermoplasma acidophilum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S26723 REFERENCE S26721 !$#authors Klenk, H.P.; Renner, O.; Schwass, V.; Zillig, W. !$#journal Nucleic Acids Res. (1992) 20:5226 !$#title Nucleotide sequence of the genes encoding the subunits H, B, !1A' and A'' of the DNA-dependent RNA polymerase and the !1initiator tRNA from Thermoplasma acidophilum. !$#cross-references MUID:93027268; PMID:1408839 !$#accession S26723 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-885 ##label KLE !'##cross-references EMBL:X68198; NID:g48089; PIDN:CAA48281.1; !1PID:g48092 !'##experimental_source DSM 1728 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1September 1992 GENETICS !$#gene rpoA1 CLASSIFICATION #superfamily Halobacterium DNA-directed RNA polymerase chain !1A KEYWORDS nucleotidyltransferase; transcription SUMMARY #length 885 #molecular-weight 100074 #checksum 6782 SEQUENCE /// ENTRY RNLVC1 #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) beta'-1 chain - liverwort (Marchantia polymorpha) chloroplast ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 11-Jun-1999 ACCESSIONS A00697; S01574 REFERENCE A00150 !$#authors Ohyama, K. !$#submission submitted to the EMBL Data Library, October 1986 !$#accession A00697 !'##molecule_type DNA !'##residues 1-684 ##label OHY REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features REFERENCE S01567 !$#authors Umesono, K.; Inokuchi, H.; Shiki, Y.; Takeuchi, M.; Chang, !1Z.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Ohyama, K.; Ozeki, !1H. !$#journal J. Mol. Biol. (1988) 203:299-331 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. II. Gene organization of the large !1single copy region from rps'12 to atpB. !$#cross-references MUID:89068686; PMID:2974085 !$#accession S01574 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-684 ##label UME !'##cross-references GB:X04465; GB:Y00686; NID:g11640; PIDN:CAA28062.1; !1PID:g453591 GENETICS !$#gene rpoC1 !$#genome chloroplast !$#introns 144/3 CLASSIFICATION #superfamily chloroplast DNA-directed RNA polymerase beta'-1 !1chain KEYWORDS chloroplast; nucleotidyltransferase; transcription SUMMARY #length 684 #molecular-weight 78960 #checksum 2759 SEQUENCE /// ENTRY RNRZC1 #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) beta'-1 chain - rice chloroplast ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 11-Jun-1999 ACCESSIONS JQ0214; S05094 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0214 !'##molecule_type DNA !'##residues 1-682 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05094 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-682 ##label HIR !'##cross-references EMBL:X15901; NID:g11957; PIDN:CAA33987.1; !1PID:g11972 !'##experimental_source cv. Nihonbare GENETICS !$#gene rpoC1 !$#map_position CP22479-24527 !$#genome chloroplast CLASSIFICATION #superfamily chloroplast DNA-directed RNA polymerase beta'-1 !1chain KEYWORDS chloroplast; nucleotidyltransferase; transcription SUMMARY #length 682 #molecular-weight 78129 #checksum 9287 SEQUENCE /// ENTRY RNZMB1 #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) beta'-1 chain - maize chloroplast ORGANISM #formal_name chloroplast Zea mays #common_name maize DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 11-Jun-1999 ACCESSIONS S12801; S58543; S40660; S08247 REFERENCE S12800 !$#authors Igloi, G.L.; Meinke, A.; Doery, I.; Koessel, H. !$#journal Mol. Gen. Genet. (1990) 221:379-394 !$#title Nucleotide sequence of the maize chloroplast rpo B/C(1)/C(2) !1operon: comparison between the derived protein primary !1structures from various organisms with respect to functional !1domains. !$#cross-references MUID:90340289; PMID:2381419 !$#accession S12801 !'##molecule_type DNA !'##residues 1-683 ##label IGL !'##cross-references EMBL:X17318; NID:g12479; PIDN:CAA35196.1; !1PID:g12481 REFERENCE S58531 !$#authors Maier, R.M.; Neckermann, K.; Igloi, G.L.; Koessel, H. !$#journal J. Mol. Biol. (1995) 251:614-628 !$#title Complete sequence of the maize chloroplast genome: gene !1content, hotspots of divergence and fine tuning of genetic !1information by transcript editing. !$#cross-references MUID:95395841; PMID:7666415 !$#accession S58543 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-683 ##label MAI !'##cross-references EMBL:X86563; NID:g902200; PIDN:CAA60277.1; !1PID:g902213 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1995 REFERENCE S40660 !$#authors Hu, J.; Troxler, R.F.; Bogorad, L. !$#journal Nucleic Acids Res. (1991) 19:3431-3434 !$#title Maize chloroplast RNA polymerase: the 78-kilodalton !1polypeptide is encoded by the plastid rpoC1 gene. !$#cross-references MUID:91288227; PMID:2062657 !$#accession S40660 !'##molecule_type DNA !'##residues 1-54 ##label HUJ !'##cross-references EMBL:M31207; NID:g342609; PIDN:AAA84488.1; !1PID:g342610 GENETICS !$#gene rpoC1 !$#genome chloroplast CLASSIFICATION #superfamily chloroplast DNA-directed RNA polymerase beta'-1 !1chain KEYWORDS chloroplast; nucleotidyltransferase; transcription SUMMARY #length 683 #molecular-weight 78322 #checksum 3527 SEQUENCE /// ENTRY RNEGB1 #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) beta'-1 chain - Euglena gracilis chloroplast ORGANISM #formal_name chloroplast Euglena gracilis DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 21-Jan-2000 ACCESSIONS S19258; S09211; S34555; S34922 REFERENCE S19258 !$#authors Hallick, R.B. !$#submission submitted to the EMBL Data Library, November 1989 !$#accession S19258 !'##molecule_type DNA !'##residues 1-586 ##label HAL !'##cross-references EMBL:X17191; NID:g11501; PIDN:CAA35053.1; !1PID:g311710 !'##experimental_source strain Pringsheim Z REFERENCE S09210 !$#authors Yepiz-Plascencia, G.M.; Radebaugh, C.A.; Hallick, R.B. !$#journal Nucleic Acids Res. (1990) 18:1869-1878 !$#title The Euglena gracilis chloroplast rpoB gene. Novel gene !1organization and transcription of the RNA polymerase subunit !1operon. !$#cross-references MUID:90245579; PMID:2110656 !$#accession S09211 !'##molecule_type DNA !'##residues 1-23 ##label YEP !'##cross-references EMBL:X17191 REFERENCE S34494 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.; Monfort, !1A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#submission submitted to the EMBL Data Library, January 1993 !$#description The complete sequence of the Euglena gracilis chloroplast !1genome (tentative). !$#accession S34555 !'##molecule_type DNA !'##residues 1-586 ##label HAL1 !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50137.1; !1PID:g415793 REFERENCE S34862 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.R.; !1Monfort, A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#journal Nucleic Acids Res. (1993) 21:3537-3544 !$#title Complete sequence of Euglena gracilis chloroplast DNA. !$#cross-references MUID:93347989; PMID:8346031 !$#accession S34922 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-586 ##label HAL2 !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50137.1; !1PID:g415793 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1993 GENETICS !$#gene rpoC1 !$#genome chloroplast !$#introns 35/3; 104/2; 126/1; 176/2; 185/3; 267/1; 309/3; 361/1; 406/ !13; 515/3; 569/3 CLASSIFICATION #superfamily chloroplast DNA-directed RNA polymerase beta'-1 !1chain KEYWORDS chloroplast; nucleotidyltransferase; transcription SUMMARY #length 586 #molecular-weight 68141 #checksum 7533 SEQUENCE /// ENTRY RNLVC2 #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) beta'-2 chain - liverwort (Marchantia polymorpha) chloroplast ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 11-Jun-1999 ACCESSIONS A00698; S01575 REFERENCE A00150 !$#authors Ohyama, K. !$#submission submitted to the EMBL Data Library, October 1986 !$#accession A00698 !'##molecule_type DNA !'##residues 1-1386 ##label OHY REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features REFERENCE S01567 !$#authors Umesono, K.; Inokuchi, H.; Shiki, Y.; Takeuchi, M.; Chang, !1Z.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Ohyama, K.; Ozeki, !1H. !$#journal J. Mol. Biol. (1988) 203:299-331 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. II. Gene organization of the large !1single copy region from rps'12 to atpB. !$#cross-references MUID:89068686; PMID:2974085 !$#accession S01575 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-1386 ##label UME !'##cross-references GB:X04465; GB:Y00686; NID:g11640; PIDN:CAA28063.1; !1PID:g11650 GENETICS !$#gene rpoC2 !$#genome chloroplast CLASSIFICATION #superfamily chloroplast DNA-directed RNA polymerase beta'-2 !1chain KEYWORDS chloroplast; nucleotidyltransferase; transcription SUMMARY #length 1386 #molecular-weight 160155 #checksum 3712 SEQUENCE /// ENTRY RNRZC2 #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) beta'-2 chain - rice chloroplast ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 11-Jun-1999 ACCESSIONS JQ0215; S05095 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0215 !'##molecule_type DNA !'##residues 1-1513 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05095 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1513 ##label HIR !'##cross-references EMBL:X15901; NID:g11957; PIDN:CAA33988.1; !1PID:g11973 !'##experimental_source cv. Nihonbare GENETICS !$#gene rpoC2 !$#map_position CP24727-29268 !$#genome chloroplast CLASSIFICATION #superfamily chloroplast DNA-directed RNA polymerase beta'-2 !1chain KEYWORDS chloroplast; nucleotidyltransferase; transcription SUMMARY #length 1513 #molecular-weight 173812 #checksum 2317 SEQUENCE /// ENTRY RNZMB2 #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) beta'-2 chain - maize chloroplast ALTERNATE_NAMES DNA-directed RNA polymerase beta'' chain; RNA polymerase 180K chain ORGANISM #formal_name chloroplast Zea mays #common_name maize DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 11-Jun-1999 ACCESSIONS S12802; S10172; S58544; A34846; S08248 REFERENCE S12800 !$#authors Igloi, G.L.; Meinke, A.; Doery, I.; Koessel, H. !$#journal Mol. Gen. Genet. (1990) 221:379-394 !$#title Nucleotide sequence of the maize chloroplast rpo B/C(1)/C(2) !1operon: comparison between the derived protein primary !1structures from various organisms with respect to functional !1domains. !$#cross-references MUID:90340289; PMID:2381419 !$#accession S12802 !'##molecule_type DNA !'##residues 1-1527 ##label IGL !'##cross-references EMBL:X17318; NID:g12479; PIDN:CAA35197.1; !1PID:g12482 REFERENCE S10172 !$#authors Stahl, D.; Rodermel, S.R.; Subramanian, A.R.; Bogorad, L. !$#journal Nucleic Acids Res. (1990) 18:3073-3074 !$#title Nucleotide sequence of a 3.46 kb region of maize chloroplast !1DNA containing the gene cluster rpoC2-rps2-atpI-atpH. !$#cross-references MUID:90272437; PMID:2140888 !$#accession S10172 !'##molecule_type DNA !'##residues 1316-1527 ##label STA !'##cross-references EMBL:X52270; NID:g12408; PIDN:CAA36511.1; !1PID:g829327 REFERENCE S58531 !$#authors Maier, R.M.; Neckermann, K.; Igloi, G.L.; Koessel, H. !$#journal J. Mol. Biol. (1995) 251:614-628 !$#title Complete sequence of the maize chloroplast genome: gene !1content, hotspots of divergence and fine tuning of genetic !1information by transcript editing. !$#cross-references MUID:95395841; PMID:7666415 !$#accession S58544 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1527 ##label MAI !'##cross-references EMBL:X86563; NID:g902200; PIDN:CAA60278.1; !1PID:g902214 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1995 REFERENCE A34846 !$#authors Hu, J.; Bogorad, L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:1531-1535 !$#title Maize chloroplast RNA polymerase: the 180-, 120-, and !138-kilodalton polypeptides are encoded in chloroplast genes. !$#cross-references MUID:90160360; PMID:2304916 !$#accession A34846 !'##molecule_type DNA !'##residues 1-16 ##label HUJ GENETICS !$#gene rpoC2 !$#map_position 74.6-78.0 !$#genome chloroplast CLASSIFICATION #superfamily chloroplast DNA-directed RNA polymerase beta'-2 !1chain KEYWORDS chloroplast; nucleotidyltransferase; tandem repeat; !1transcription FEATURE !$636-786 #region 7-residue repeats SUMMARY #length 1527 #molecular-weight 176081 #checksum 1156 SEQUENCE /// ENTRY RNEGB2 #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) beta'-2 chain - Euglena gracilis chloroplast ORGANISM #formal_name chloroplast Euglena gracilis DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 21-Jan-2000 ACCESSIONS S19259; S34554; S34921; S09212 REFERENCE S19258 !$#authors Hallick, R.B. !$#submission submitted to the EMBL Data Library, November 1989 !$#accession S19259 !'##molecule_type DNA !'##residues 1-830 ##label HAL !'##cross-references EMBL:X17191; NID:g11501; PIDN:CAA35054.1; !1PID:g311711 !'##experimental_source strain Pringsheim Z REFERENCE S34494 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.; Monfort, !1A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#submission submitted to the EMBL Data Library, January 1993 !$#description The complete sequence of the Euglena gracilis chloroplast !1genome (tentative). !$#accession S34554 !'##molecule_type DNA !'##residues 1-830 ##label HAL1 !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50136.1; !1PID:g415792 REFERENCE S34862 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.R.; !1Monfort, A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#journal Nucleic Acids Res. (1993) 21:3537-3544 !$#title Complete sequence of Euglena gracilis chloroplast DNA. !$#cross-references MUID:93347989; PMID:8346031 !$#accession S34921 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-830 ##label HAL2 !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50136.1; !1PID:g415792 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1993 GENETICS !$#gene rpoC2 !$#genome chloroplast !$#introns 271/3; 365/2 CLASSIFICATION #superfamily chloroplast DNA-directed RNA polymerase beta'-2 !1chain KEYWORDS chloroplast; nucleotidyltransferase; transcription SUMMARY #length 830 #molecular-weight 94756 #checksum 8648 SEQUENCE /// ENTRY RNFF32 #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) III second-largest chain - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 11-Jun-1999 ACCESSIONS S16894 REFERENCE S16894 !$#authors Seifarth, W.; Petersen, G.; Kontermann, R.; Riva, M.; Huet, !1J.; Bautz, E.K.F. !$#journal Mol. Gen. Genet. (1991) 228:424-432 !$#title Identification of the genes coding for the second-largest !1subunits of RNA polymerases I and III of Drosophila !1melanogaster. !$#cross-references MUID:91375428; PMID:1910149 !$#accession S16894 !'##molecule_type DNA !'##residues 1-1135 ##label SEI !'##cross-references EMBL:X58826; NID:g10962; PIDN:CAA41631.1; !1PID:g10963 GENETICS !$#gene RP128 !'##cross-references FlyBase:FBgn0004463 !$#introns 294/1 CLASSIFICATION #superfamily DNA-directed RNA polymerase 132K polypeptide KEYWORDS nucleotidyltransferase; transcription; zinc finger SUMMARY #length 1135 #molecular-weight 128372 #checksum 9078 SEQUENCE /// ENTRY S26722 #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) chain B - Thermoplasma acidophilum ORGANISM #formal_name Thermoplasma acidophilum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S26722 REFERENCE S26721 !$#authors Klenk, H.P.; Renner, O.; Schwass, V.; Zillig, W. !$#journal Nucleic Acids Res. (1992) 20:5226 !$#title Nucleotide sequence of the genes encoding the subunits H, B, !1A' and A'' of the DNA-dependent RNA polymerase and the !1initiator tRNA from Thermoplasma acidophilum. !$#cross-references MUID:93027268; PMID:1408839 !$#accession S26722 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1195 ##label KLE !'##cross-references EMBL:X68198; NID:g48089; PIDN:CAA48280.1; !1PID:g809775 !'##experimental_source DSM 1728 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1September 1992 GENETICS !$#gene rpoB !$#start_codon GTG CLASSIFICATION #superfamily DNA-directed RNA polymerase 132K polypeptide KEYWORDS nucleotidyltransferase; transcription SUMMARY #length 1195 #molecular-weight 134689 #checksum 6180 SEQUENCE /// ENTRY RNVZ8T #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) 132K chain - vaccinia virus ALTERNATE_NAMES A24R protein ORGANISM #formal_name vaccinia virus #note host Homo sapiens (man) DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 11-Jun-1999 ACCESSIONS H42519; A38517 REFERENCE A42501 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:517-563 !$#title Appendix to "The complete DNA sequence of vaccinia virus". !$#accession H42519 !'##molecule_type DNA !'##residues 1-1164 ##label GOE !'##cross-references GB:M35027; NID:g335317; PIDN:AAA48148.1; !1PID:g335496 !'##experimental_source strain Copenhagen REFERENCE A38517 !$#authors Amegadzie, B.Y.; Holmes, M.H.; Cole, N.B.; Jones, E.V.; !1Earl, P.L.; Moss, B. !$#journal Virology (1991) 180:88-98 !$#title Identification, sequence, and expression of the gene !1encoding the second-largest subunit of the vaccinia virus !1DNA-dependent RNA polymerase. !$#cross-references MUID:91082452; PMID:1824607 !$#accession A38517 !'##molecule_type DNA !'##residues 1-1164 ##label AME !'##cross-references EMBL:M37415; NID:g335800; PIDN:AAA72882.1; !1PID:g335801 !'##experimental_source strain WR REFERENCE A42531 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:247-266 !$#title The complete DNA sequence of vaccinia virus. !$#cross-references MUID:91021027; PMID:2219722 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given CLASSIFICATION #superfamily DNA-directed RNA polymerase 132K polypeptide KEYWORDS leucine zipper; nucleotidyltransferase; transcription; zinc !1finger FEATURE !$484-505 #region leucine zipper motif\ !$1087-1106 #region zinc finger CCCC motif SUMMARY #length 1164 #molecular-weight 133363 #checksum 4791 SEQUENCE /// ENTRY RNVZCP #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) 132K chain - cowpox virus (strain Brighton Red) ORGANISM #formal_name cowpox virus DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 11-Jun-1999 ACCESSIONS A31879 REFERENCE A31879 !$#authors Patel, D.D.; Pickup, D.J. !$#journal J. Virol. (1989) 63:1076-1086 !$#title The second-largest subunit of the poxvirus RNA polymerase is !1similar to the corresponding subunits of procaryotic and !1eucaryotic RNA polymerases. !$#cross-references MUID:89125698; PMID:2915377 !$#accession A31879 !'##molecule_type DNA !'##residues 1-1164 ##label PAT !'##cross-references GB:M26173; NID:g323393; PIDN:AAA42919.1; !1PID:g323394 COMMENT This enzyme consists of at least seven subunits whose !1molecular weights are 147K, 132K, 73K, 37K, 23K, 22K, and !120K. GENETICS !$#gene rpo132 CLASSIFICATION #superfamily DNA-directed RNA polymerase 132K polypeptide KEYWORDS nucleotidyltransferase; transcription; zinc finger SUMMARY #length 1164 #molecular-weight 133323 #checksum 4235 SEQUENCE /// ENTRY RNVZCA #type fragment TITLE DNA-directed RNA polymerase (EC 2.7.7.6) 132K polypeptide - sheep pox virus (isolate Kenya sheep-1, KS-1) (fragment) ALTERNATE_NAMES HM1 protein ORGANISM #formal_name sheep pox virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 11-Jun-1999 ACCESSIONS A33325 REFERENCE A33325 !$#authors Gershon, P.D.; Ansell, D.M.; Black, D.N. !$#journal J. Virol. (1989) 63:4703-4708 !$#title A comparison of the genome organization of capripoxvirus !1with that of the orthopoxviruses. !$#cross-references MUID:90012320; PMID:2795717 !$#accession A33325 !'##molecule_type DNA !'##residues 1-919 ##label GER !'##cross-references GB:M30039; NID:g323258; PIDN:AAC32897.1; !1PID:g323259 CLASSIFICATION #superfamily DNA-directed RNA polymerase 132K polypeptide KEYWORDS nucleotidyltransferase; transcription; zinc finger SUMMARY #length 919 #checksum 1366 SEQUENCE /// ENTRY RNECS #type complete TITLE transcription initiation factor sigma 70 - Escherichia coli (strain K-12) ALTERNATE_NAMES DNA-directed RNA polymerase sigma chain; major sigma factor; transcriptase sigma chain ORGANISM #formal_name Escherichia coli DATE 18-Dec-1981 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS A65095; A00699 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65095 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-613 ##label BLAT !'##cross-references GB:AE000388; GB:U00096; NID:g1789441; !1PIDN:AAC76103.1; PID:g1789448; UWGP:b3067 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A00699 !$#authors Burton, Z.; Burgess, R.R.; Lin, J.; Moore, D.; Holder, S.; !1Gross, C.A. !$#journal Nucleic Acids Res. (1981) 9:2889-2903 !$#title The nucleotide sequence of the cloned rpoD gene for the RNA !1polymerase sigma subunit from E. coli K12. !$#cross-references MUID:82014879; PMID:6269063 !$#accession A00699 !'##molecule_type DNA !'##residues 1-148,'N',150-613 ##label BUR !'##cross-references GB:J01687; NID:g147753; PIDN:AAA24601.1; !1PID:g147756 !'##experimental_source K12 COMMENT The DNA-directed RNA polymerase, also called transcriptase, !1catalyzes RNA synthesis using a DNA template. The enzyme !1consists of the sigma factor and the core enzyme. The sigma !1factor is an initiation factor that promotes attachment of !1the enzyme to specific initiation sites and then is !1released. The core enzyme is composed of two alpha chains, !1one beta chain, and one beta' chain. GENETICS !$#gene rpoD !$#map_position 67 min CLASSIFICATION #superfamily transcription initiation factor sigma 70; !1transcription initiation factor sigma katF homology; !1transcription initiation factor sigma region 1 homology KEYWORDS DNA binding; sigma factor; transcription initiation FEATURE !$1-135 #domain transcription initiation factor sigma region !81 homology #label SR1\ !$381-607 #domain transcription initiation factor sigma katF !8homology #label KTF SUMMARY #length 613 #molecular-weight 70263 #checksum 4436 SEQUENCE /// ENTRY RNEBST #type complete TITLE transcription initiation factor sigma 70 - Salmonella typhimurium ALTERNATE_NAMES DNA-directed RNA polymerase sigma chain; major sigma factor; transcriptase sigma chain ORGANISM #formal_name Salmonella typhimurium DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 11-Jun-1999 ACCESSIONS C23985 REFERENCE A91542 !$#authors Erickson, B.D.; Burton, Z.F.; Watanabe, K.K.; Burgess, R.R. !$#journal Gene (1985) 40:67-78 !$#title Nucleotide sequence of the rpsU-dnaG-rpoD operon from !1Salmonella typhimurium and a comparison of this sequence !1with the homologous operon of Escherichia coli. !$#cross-references MUID:86137422; PMID:3005129 !$#accession C23985 !'##molecule_type DNA !'##residues 1-615 ##label ERI !'##cross-references GB:M14427; NID:g154402; PIDN:AAA27242.1; !1PID:g154406 GENETICS !$#gene rpoD CLASSIFICATION #superfamily transcription initiation factor sigma 70; !1transcription initiation factor sigma katF homology; !1transcription initiation factor sigma region 1 homology KEYWORDS DNA binding; sigma factor; transcription initiation FEATURE !$1-137 #domain transcription initiation factor sigma region !81 homology #label SR1\ !$383-609 #domain transcription initiation factor sigma katF !8homology #label KTF SUMMARY #length 615 #molecular-weight 70530 #checksum 1078 SEQUENCE /// ENTRY RNJV7A #type complete TITLE transcription initiation factor sigma 70 - Buchnera aphidicola ALTERNATE_NAMES DNA-directed RNA polymerase sigma chain; major sigma factor; transcriptase sigma chain ORGANISM #formal_name Buchnera aphidicola DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 11-Jun-1999 ACCESSIONS JC1291 REFERENCE JC1291 !$#authors Lai, C.Y.; Baumann, P. !$#journal Gene (1992) 119:113-118 !$#title Sequence analysis of a DNA fragment from Buchnera aphidicola !1(an endosymbiont of aphids) containing genes homologous to !1dnaG, rpoD, cysE, and secB. !$#cross-references MUID:93012960; PMID:1398077 !$#accession JC1291 !'##molecule_type DNA !'##residues 1-617 ##label LAI !'##cross-references GB:M90644; NID:g144135; PIDN:AAA73234.1; !1PID:g144139 GENETICS !$#gene rpoD CLASSIFICATION #superfamily transcription initiation factor sigma 70; !1transcription initiation factor sigma katF homology; !1transcription initiation factor sigma region 1 homology KEYWORDS DNA binding; sigma factor; transcription initiation FEATURE !$1-137 #domain transcription initiation factor sigma region !81 homology #label SR1\ !$385-611 #domain transcription initiation factor sigma katF !8homology #label KTF SUMMARY #length 617 #molecular-weight 71469 #checksum 3318 SEQUENCE /// ENTRY RNPS7A #type complete TITLE transcription initiation factor sigma 70 - Pseudomonas aeruginosa ALTERNATE_NAMES DNA-directed RNA polymerase sigma chain; major sigma factor; transcriptase sigma chain ORGANISM #formal_name Pseudomonas aeruginosa DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 31-Dec-2000 ACCESSIONS S15900; D83572 REFERENCE S15899 !$#authors Tanaka, K.; Takahashi, H. !$#journal Biochim. Biophys. Acta (1991) 1089:113-119 !$#title Cloning and analysis of the gene (rpoDA) for the principal !1sigma factor of Pseudomonas aeruginosa. !$#cross-references MUID:91223089; PMID:1902749 !$#accession S15900 !'##molecule_type DNA !'##residues 1-617 ##label BIO !'##cross-references GB:D90118; NID:g216912; PIDN:BAA14146.1; !1PID:g216913 !'##note the sequence from Fig. 4 is inconsistent with that from Fig. 3 !1in having 313-Gly, and 390-Ser REFERENCE A82950 !$#authors Stover, C.K.; Pham, X.Q.; Erwin, A.L.; Mizoguchi, S.D.; !1Warrener, P.; Hickey, M.J.; Brinkman, F.S.L.; Hufnagle, !1W.O.; Kowalik, D.J.; Lagrou, M.; Garber, R.L.; Goltry, L.; !1Tolentino, E.; Westbrook-Wadman, S.; Yuan, Y.; Brody, L.L.; !1Coulter, S.N.; Folger, K.R.; Kas, A.; Larbig, K.; Lim, R.M.; !1Smith, K.A.; Spencer, D.H.; Wong, G.K.S.; Wu, Z.; Paulsen, !1I.T.; Reizer, J.; Saier, M.H.; Hancock, R.E.W.; Lory, S.; !1Olson, M.V. !$#journal Nature (2000) 406:959-964 !$#title Complete genome sequence of Pseudomonas aeruginosa PA01, an !1opportunistic pathogen. !$#cross-references MUID:20437337; PMID:10984043 !$#accession D83572 !'##status preliminary !'##molecule_type DNA !'##residues 1-617 ##label STO !'##cross-references GB:AE004494; GB:AE004091; NID:g9946446; !1PIDN:AAG03965.1; GSPDB:GN00131; PASP:PA0576 !'##experimental_source strain PAO1 GENETICS !$#gene rpoDA; rpoD; PA0576 CLASSIFICATION #superfamily transcription initiation factor sigma 70; !1transcription initiation factor sigma katF homology; !1transcription initiation factor sigma region 1 homology KEYWORDS DNA binding; sigma factor; transcription initiation FEATURE !$1-137 #domain transcription initiation factor sigma region !81 homology #label SR1\ !$385-611 #domain transcription initiation factor sigma katF !8homology #label KTF SUMMARY #length 617 #molecular-weight 69643 #checksum 2685 SEQUENCE /// ENTRY RNCW7T #type complete TITLE transcription initiation factor sigma 70 - Chlamydia trachomatis ALTERNATE_NAMES DNA-directed RNA polymerase sigma-66 chain sigma-66 ORGANISM #formal_name Chlamydia trachomatis DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 11-Jun-1999 ACCESSIONS A36627; C71494 REFERENCE A36627 !$#authors Koehler, J.E.; Burgess, R.R.; Thompson, N.E.; Stephens, R.S. !$#journal J. Biol. Chem. (1990) 265:13206-13214 !$#title Chlamydia trachomatis RNA polymerase major sigma subunit. !1Sequence and structural comparison of conserved and unique !1regions with Escherichia coli sigma(70) and Bacillus !1subtilis sigma(43). !$#cross-references MUID:90330666; PMID:2142944 !$#accession A36627 !'##molecule_type DNA !'##residues 1-571 ##label KOE !'##cross-references GB:J05546; NID:g144608; PIDN:AAA23165.1; !1PID:g144609 !'##experimental_source strain L2 REFERENCE A71570 !$#authors Stephens, R.S.; Kalman, S.; Lammel, C.J.; Fan, J.; Marathe, !1R.; Aravind, L.; Mitchell, W.P.; Olinger, L.; Tatusov, R.L.; !1Zhao, Q.; Koonin, E.V.; Davis, R.W. !$#journal Science (1998) 282:754-759 !$#title Genome sequence of an obligate intracellular pathogen of !1humans: Chlamydia trachomatis. !$#cross-references MUID:99000809; PMID:9784136 !$#accession C71494 !'##molecule_type DNA !'##residues 1-571 ##label ARN !'##cross-references GB:AE001331; GB:AE001273; NID:g3329046; !1PIDN:AAC68218.1; PID:g3329060 !'##experimental_source serotype D, strain UW-3/Cx GENETICS !$#gene rpoD CLASSIFICATION #superfamily transcription initiation factor sigma 70; !1transcription initiation factor sigma katF homology; !1transcription initiation factor sigma region 1 homology KEYWORDS DNA binding; sigma factor; transcription initiation FEATURE !$1-140 #domain transcription initiation factor sigma region !81 homology #label SR1\ !$323-549 #domain transcription initiation factor sigma katF !8homology #label KTF SUMMARY #length 571 #molecular-weight 66133 #checksum 353 SEQUENCE /// ENTRY RNCW7H #type complete TITLE transcription initiation factor sigma 70 - Chlamydia trachomatis ALTERNATE_NAMES DNA-directed RNA polymerase sigma chain ORGANISM #formal_name Chlamydia trachomatis DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 11-Jun-1999 ACCESSIONS A35258 REFERENCE A35258 !$#authors Engel, J.N.; Ganem, D. !$#journal J. Bacteriol. (1990) 172:2447-2455 !$#title A polymerase chain reaction-based approach to cloning sigma !1factors from eubacteria and its application to the isolation !1of a sigma-70 homolog from Chlamydia trachomatis. !$#cross-references MUID:90236902; PMID:2110143 !$#accession A35258 !'##molecule_type DNA !'##residues 1-571 ##label ENG !'##cross-references GB:M36475; NID:g144615; PIDN:AAA23168.1; !1PID:g144616 CLASSIFICATION #superfamily transcription initiation factor sigma 70; !1transcription initiation factor sigma katF homology; !1transcription initiation factor sigma region 1 homology KEYWORDS DNA binding; sigma factor; transcription initiation FEATURE !$1-140 #domain transcription initiation factor sigma region !81 homology #label SR1\ !$323-549 #domain transcription initiation factor sigma katF !8homology #label KTF SUMMARY #length 571 #molecular-weight 66265 #checksum 4116 SEQUENCE /// ENTRY RNRE7P #type complete TITLE transcription initiation factor sigma 70 - Rickettsia prowazekii ALTERNATE_NAMES DNA-directed RNA polymerase sigma chain rpoD; RP858 ORGANISM #formal_name Rickettsia prowazekii DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 03-Nov-2000 ACCESSIONS JC1379; B71648 REFERENCE JC1379 !$#authors Marks, G.L.; Winkler, H.H.; Wood, D.O. !$#journal Gene (1992) 121:155-160 !$#title Isolation and characterization of the gene coding for the !1major sigma factor of Rickettsia prowazekii DNA-dependent !1RNA polymerase. !$#cross-references MUID:93051352; PMID:1427089 !$#accession JC1379 !'##molecule_type DNA !'##residues 1-635 ##label MAR !'##cross-references GB:U02878; GB:M81312; NID:g434676; PIDN:AAB81404.1; !1PID:g434681 REFERENCE A71630 !$#authors Andersson, S.G.E.; Zomorodipour, A.; Andersson, J.O.; !1Sicheritz-Ponten, T.; Alsmark, U.C.M.; Podowski, R.M.; !1Naeslund, A.K.; Eriksson, A.S.; Winkler, H.H.; Kurland, C.G. !$#journal Nature (1998) 396:133-140 !$#title The genome sequence of Rickettsia prowazekii and the origin !1of mitochondria. !$#cross-references MUID:99039499; PMID:9823893 !$#accession B71648 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-635 ##label AND !'##cross-references GB:AJ235273; GB:AJ235269; NID:g3861237; !1PIDN:CAA15282.1; PID:g3861383; GSPDB:GN00081 !'##experimental_source strain Madrid E COMMENT The sigma chain is an initiation factor that promotes !1attachment of the core enzyme to specific initiation sites. GENETICS !$#gene rpoD; RP858 CLASSIFICATION #superfamily transcription initiation factor sigma 70; !1transcription initiation factor sigma katF homology; !1transcription initiation factor sigma region 1 homology KEYWORDS DNA binding; sigma factor; transcription initiation FEATURE !$1-143 #domain transcription initiation factor sigma region !81 homology #label SR1\ !$388-615 #domain transcription initiation factor sigma katF !8homology #label KTF SUMMARY #length 635 #molecular-weight 73080 #checksum 2474 SEQUENCE /// ENTRY RNAGVS #type complete TITLE transcription initiation factor sigma, vegetative - Agrobacterium tumefaciens ALTERNATE_NAMES DNA-directed RNA polymerase sigma chain ORGANISM #formal_name Agrobacterium tumefaciens DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 11-Jun-1999 ACCESSIONS A36913; S31382 REFERENCE A36913 !$#authors Segal, G.; Ron, E.Z. !$#journal J. Bacteriol. (1993) 175:3026-3030 !$#title Cloning, sequencing, and transcriptional analysis of the !1gene coding for the vegetative sigma factor of Agrobacterium !1tumefaciens. !$#cross-references MUID:93259948; PMID:8491721 !$#accession A36913 !'##status preliminary !'##molecule_type DNA !'##residues 1-684 ##label SEG !'##cross-references EMBL:X69388; NID:g39131; PIDN:CAA49185.1; !1PID:g39132 !'##note sequence extracted from NCBI backbone (NCBIN:131913, !1NCBIP:131914) GENETICS !$#gene sigA CLASSIFICATION #superfamily transcription initiation factor sigma 70; !1transcription initiation factor sigma katF homology; !1transcription initiation factor sigma region 1 homology KEYWORDS DNA binding; sigma factor; transcription initiation FEATURE !$22-166 #domain transcription initiation factor sigma region !81 homology #label SR1\ !$452-678 #domain transcription initiation factor sigma katF !8homology #label KTF SUMMARY #length 684 #molecular-weight 77218 #checksum 8067 SEQUENCE /// ENTRY RNBS43 #type complete TITLE transcription initiation factor sigma A - Bacillus subtilis ALTERNATE_NAMES RNA polymerase major sigma factor sigA; RNA polymerase sigma factor 43; sigma factor A ORGANISM #formal_name Bacillus subtilis DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jun-2000 ACCESSIONS A22626; B37129; G69705; S35604 REFERENCE A22626 !$#authors Gitt, M.A.; Wang, L.F.; Doi, R.H. !$#journal J. Biol. Chem. (1985) 260:7178-7185 !$#title A strong sequence homology exists between the major RNA !1polymerase sigma factors of Bacillus subtilis and !1Escherichia coli. !$#cross-references MUID:85207748; PMID:2987246 !$#accession A22626 !'##molecule_type DNA !'##residues 1-371 ##label GIT !'##cross-references GB:M10089; NID:g143453; PIDN:AAA22709.1; !1PID:g143454 REFERENCE A37129 !$#authors von Wachenfeldt, C.; Hederstedt, L. !$#journal J. Biol. Chem. (1990) 265:13939-13948 !$#title Bacillus subtilis 13-kilodalton cytochrome c-550 encoded by !1cccA consists of a membrane-anchor and a heme domain. !$#cross-references MUID:90338015; PMID:2166045 !$#accession B37129 !'##molecule_type DNA !'##residues 302-371 ##label VON !'##cross-references GB:J05569 REFERENCE S35604 !$#authors Chang, B.Y.; Doi, R.H. !$#journal Biochem. J. (1993) 294:43-47 !$#title Conformational properties of Bacillus subtilis RNA !1polymerase sigma(A) factor during transcription initiation. !$#cross-references MUID:93371380; PMID:8363585 !$#contents annotation !$#note conformational properties study by trypsin sensitivity; !1material purified after cloning and overexpression in E. !1coli REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69705 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-371 ##label KUN !'##cross-references GB:Z99116; GB:Z99117; GB:AL009126; NID:g2634966; !1PIDN:CAB14463.1; PID:g2634967; NID:g2634723; PID:g2634953 !'##experimental_source strain 168 COMMENT Sigma factors are trancription initiation factors that bind !1the DNA-directed RNA polymerase (EC 2.7.7.6) core enzyme to !1form a complex called the holoenzyme. The sigma factor is !1released shortly after transcription begins. COMMENT This protein is the major sigma factor in Bacillus subtilis, !1but is replaced by sigma factors under developmental control !1during specific stages of sporulation. GENETICS !$#gene sigA; rpoD !$#map_position 224 (degrees) CLASSIFICATION #superfamily transcription initiation factor sigma 43; !1transcription initiation factor sigma katF homology; !1transcription initiation factor sigma region 1 homology KEYWORDS DNA binding; sigma factor; transcription initiation FEATURE !$1-139 #domain transcription initiation factor sigma region !81 homology #label SR1\ !$140-366 #domain transcription initiation factor sigma katF !8homology #label KTF SUMMARY #length 371 #molecular-weight 42957 #checksum 5694 SEQUENCE /// ENTRY S17929 #type complete TITLE transcription initiation factor sigma hrdA - Streptomyces coelicolor ORGANISM #formal_name Streptomyces coelicolor DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Dec-1999 ACCESSIONS S17929; T42031; A40116; S11711 REFERENCE S17929 !$#authors Tanaka, K.; Shiina, T.; Takahashi, H. !$#journal Mol. Gen. Genet. (1991) 229:334-340 !$#title Nucleotide sequence of genes hrdA, hrdC, and hrdD from !1Streptomyces coelicolor A3(2) having similarity to rpoD !1genes. !$#cross-references MUID:92049230; PMID:1944221 !$#accession S17929 !'##molecule_type DNA !'##residues 1-396 ##label TAN1 !'##cross-references EMBL:X52980; NID:g48738; PIDN:CAA37172.1; !1PID:g581612 !$#accession T42031 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-396 ##label TAN !'##cross-references EMBL:X52980; PIDN:CAA37172.1 REFERENCE A40116 !$#authors Tanaka, K.; Shiina, T.; Takahashi, H. !$#journal Science (1988) 242:1040-1042 !$#title Multiple principal sigma factor homologs in eubacteria: !1identification of the "rpoD box". !$#cross-references MUID:89058616; PMID:3194753 !$#accession A40116 !'##status preliminary; nucleic acid sequence not shown !'##molecule_type DNA !'##residues 191-242 ##label TAN2 GENETICS !$#gene hrdA !$#start_codon GTG CLASSIFICATION #superfamily transcription initiation factor sigma 43; !1transcription initiation factor sigma katF homology; !1transcription initiation factor sigma region 1 homology KEYWORDS DNA binding; sigma factor; transcription initiation FEATURE !$165-391 #domain transcription initiation factor sigma katF !8homology #label KTF\ !$210-222 #region rpoD box SUMMARY #length 396 #molecular-weight 43747 #checksum 7811 SEQUENCE /// ENTRY JN0442 #type complete TITLE transcription initiation factor sigma homolog hrdA - Streptomyces aureofaciens ORGANISM #formal_name Streptomyces aureofaciens DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JN0442 REFERENCE JN0442 !$#authors Kormanec, J.; Farkasovsky, M.; Poutuckova, L. !$#journal Gene (1992) 122:63-70 !$#title Four genes in Streptomyces aureofaciens containing a domain !1characterstic of principal sigma factors. !$#cross-references MUID:93083996; PMID:1452038 !$#accession JN0442 !'##molecule_type DNA !'##residues 1-393 ##label KOR !'##cross-references GB:M90410; NID:g153303; PIDN:AAA26762.1; !1PID:g153304 GENETICS !$#gene hrdA !$#start_codon GTG CLASSIFICATION #superfamily transcription initiation factor sigma 43; !1transcription initiation factor sigma katF homology; !1transcription initiation factor sigma region 1 homology KEYWORDS DNA binding; sigma factor; transcription initiation FEATURE !$1-151 #domain transcription initiation factor sigma region !81 homology #label SR1\ !$162-388 #domain transcription initiation factor sigma katF !8homology #label KTF SUMMARY #length 393 #molecular-weight 43396 #checksum 8628 SEQUENCE /// ENTRY A42724 #type complete TITLE transcription initiation factor sigma sigA - Anabaena sp. (strain PCC 7120) ORGANISM #formal_name Anabaena sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A42724 REFERENCE A42724 !$#authors Brahamsha, B.; Haselkorn, R. !$#journal J. Bacteriol. (1991) 173:2442-2450 !$#title Isolation and characterization of the gene encoding the !1principal sigma factor of the vegetative cell RNA polymerase !1from the cyanobacterium Anabaena sp. strain PCC 7120. !$#cross-references MUID:91193199; PMID:1901566 !$#accession A42724 !'##status preliminary !'##molecule_type DNA !'##residues 1-390 ##label BRA !'##cross-references GB:M60046; NID:g142107; PIDN:AAA22043.1; !1PID:g142108 CLASSIFICATION #superfamily transcription initiation factor sigma 43; !1transcription initiation factor sigma katF homology; !1transcription initiation factor sigma region 1 homology KEYWORDS DNA binding; sigma factor; transcription initiation FEATURE !$160-385 #domain transcription initiation factor sigma katF !8homology #label KTF SUMMARY #length 390 #molecular-weight 45641 #checksum 8953 SEQUENCE /// ENTRY S24172 #type complete TITLE transcription initiation factor sigma A - Synechococcus sp. ALTERNATE_NAMES RNA polymerase sigma rpoD1 ORGANISM #formal_name Synechococcus sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S24172 REFERENCE S24172 !$#authors Tanaka, K.; Masuda, S.; Takahashi, H. !$#journal Biochim. Biophys. Acta (1992) 1132:94-96 !$#title The complete nucleotide sequence of the gene (rpoD1) !1encoding the principal sigma factor of the RNA polymerase !1from the cyanobacterium Synechococcus sp. strain PCC7942. !$#cross-references MUID:92379100; PMID:1511015 !$#accession S24172 !'##status preliminary !'##molecule_type DNA !'##residues 1-384 ##label TAN CLASSIFICATION #superfamily transcription initiation factor sigma 43; !1transcription initiation factor sigma katF homology; !1transcription initiation factor sigma region 1 homology KEYWORDS DNA binding; transcription initiation FEATURE !$154-379 #domain transcription initiation factor sigma katF !8homology #label KTF SUMMARY #length 384 #molecular-weight 44043 #checksum 9468 SEQUENCE /// ENTRY JC4952 #type complete TITLE transcription initiation factor sigma - Microcystis aeruginosa ALTERNATE_NAMES rpoD1 protein ORGANISM #formal_name Microcystis aeruginosa DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS JC4952; JC5376 REFERENCE JC4952 !$#authors Asayama, M.; Suzuki, H.; Sato, A.; Aida, T.; Tanaka, K.; !1Takahashi, H.; Shirai, M. !$#journal J. Biochem. (1996) 120:752-758 !$#title The rpoD1 gene products is a principal sigma factor of RNA !1polymerase in Microcystis aeruginosa K-81. !$#cross-references MUID:97103466; PMID:8947837 !$#accession JC4952 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-416 ##label ASA !'##cross-references DDBJ:D50318; NID:g786172; PIDN:BAA08853.1; !1PID:g786173 !'##note the complete translation are shown REFERENCE JC5376 !$#authors Asayama, M.; Tanaka, K.; Takahashi, H.; Sato, A.; Aida, T.; !1Shirai, M. !$#journal Gene (1996) 181:213-217 !$#title Cloning, sequencing and characterization of the gene !1encoding a principal sigma factor homolog from the !1cyanobacterium Microcystis aeruginosa K-81. !$#cross-references MUID:97128793; PMID:8973333 !$#accession JC5376 !'##molecule_type DNA !'##residues 1-416 ##label AS2 !'##cross-references DDBJ:D50318; NID:g786172; PIDN:BAA08853.1; !1PID:g786173 !'##experimental_source strain K-81 COMMENT This factor is responsible for the promoter recognition of !1housekeeping genes under normal physiological growth !1conditions. GENETICS !$#gene rpoD1 CLASSIFICATION #superfamily transcription initiation factor sigma 43; !1transcription initiation factor sigma katF homology; !1transcription initiation factor sigma region 1 homology KEYWORDS DNA binding; sigma factor; transcription initiation FEATURE !$186-411 #domain transcription initiation factor sigma katF !8homology #label KTF SUMMARY #length 416 #molecular-weight 48870 #checksum 1759 SEQUENCE /// ENTRY C37165 #type complete TITLE transcription initiation factor sigma spoIIAC - Bacillus licheniformis ALTERNATE_NAMES sporulation locus spoIIA protein C ORGANISM #formal_name Bacillus licheniformis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C37165 REFERENCE A37165 !$#authors Yudkin, M.D.; Appleby, L.; Smith, A.J. !$#journal J. Gen. Microbiol. (1989) 135:767-775 !$#title Nucleotide sequence of the Bacillus licheniformis homologue !1of the sporulation locus spoIIA of Bacillus subtilis. !$#cross-references MUID:90095433; PMID:2513372 !$#accession C37165 !'##molecule_type DNA !'##residues 1-255 ##label YUD !'##cross-references GB:M25260; NID:g304170; PIDN:AAA22797.1; !1PID:g304173 CLASSIFICATION #superfamily transcription sigma factor G; transcription !1initiation factor sigma katF homology KEYWORDS DNA binding; sigma factor; transcription initiation FEATURE !$39-252 #domain transcription initiation factor sigma katF !8homology #label KTF SUMMARY #length 255 #molecular-weight 29641 #checksum 8162 SEQUENCE /// ENTRY A28567 #type complete TITLE transcription initiation sigma factor sigF - Bacillus subtilis ALTERNATE_NAMES stage II sporulation protein spoIIAC ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A28567; C55646; C69706 REFERENCE A28567 !$#authors Yudkin, M.D. !$#journal J. Gen. Microbiol. (1987) 133:475-481 !$#title Structure and function in a Bacillus subtilis !1sporulation-specific sigma factor: molecular nature of !1mutations in spoIIAC. !$#cross-references MUID:88009869; PMID:3116160 !$#accession A28567 !'##molecule_type DNA !'##residues 1-255 ##label YUD !'##cross-references GB:M15744; NID:g143610; PIDN:AAA22788.1; !1PID:g143611 REFERENCE A55646 !$#authors Fort, P.; Piggot, P.J. !$#journal J. Gen. Microbiol. (1984) 130:2147-2153 !$#title Nucleotide sequence of sporulation locus spoIIA in Bacillus !1subtilis. !$#cross-references MUID:84291358; PMID:6088674 !$#accession C55646 !'##molecule_type DNA !'##residues 1-179,'IKSLTTQKKNGLTKLR' ##label FOR !'##cross-references GB:M85047 !'##note this sequence has been corrected in reference A28567 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69706 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-255 ##label KUN !'##cross-references GB:Z99116; GB:AL009126; NID:g2634723; !1PIDN:CAB14277.1; PID:g2634780 !'##experimental_source strain 168 GENETICS !$#gene sigF; spoIIAC CLASSIFICATION #superfamily transcription sigma factor G; transcription !1initiation factor sigma katF homology KEYWORDS DNA binding; sigma factor; sporulation; transcription !1initiation FEATURE !$39-252 #domain transcription initiation factor sigma katF !8homology #label KTF SUMMARY #length 255 #molecular-weight 29372 #checksum 6668 SEQUENCE /// ENTRY A30202 #type complete TITLE transcription initiation sigma factor sigG - Bacillus subtilis ALTERNATE_NAMES RNA polymerase sporulation forespore-specific (late) sigma factor sigG ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A30171; A30202; D69706 REFERENCE A30171 !$#authors Karmazyn-Campelli, C.; Bonamy, C.; Savelli, B.; Stragier, P. !$#journal Genes Dev. (1989) 3:150-157 !$#title Tandem genes encoding sigma-factors for consecutive steps of !1development in Bacillus subtilis. !$#cross-references MUID:89232712; PMID:2497052 !$#accession A30171 !'##molecule_type DNA !'##residues 1-260 ##label KAR !'##cross-references GB:X57547; NID:g39457; PIDN:CAA40771.1; PID:g580764 REFERENCE A30202 !$#authors Masuda, E.S.; Anaguchi, H.; Yamada, K.; Kobayashi, Y. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:7637-7641 !$#title Two developmental genes encoding sigma factor homologs are !1arranged in tandem in Bacillus subtilis. !$#cross-references MUID:89017252; PMID:2459711 !$#accession A30202 !'##molecule_type DNA !'##residues 1-260 ##label MAS !'##cross-references GB:J04077; NID:g143428; PIDN:AAA22703.1; !1PID:g143430 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D69706 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-260 ##label KUN !'##cross-references GB:Z99112; GB:AL009126; NID:g2633902; !1PIDN:CAB13407.1; PID:g2633906 !'##experimental_source strain 168 GENETICS !$#gene sigG; spoIIIG !$#start_codon GTG CLASSIFICATION #superfamily transcription sigma factor G; transcription !1initiation factor sigma katF homology KEYWORDS DNA binding; sigma factor; transcription initiation FEATURE !$45-260 #domain transcription initiation factor sigma katF !8homology #label KTF SUMMARY #length 260 #molecular-weight 30073 #checksum 3467 SEQUENCE /// ENTRY A25944 #type complete TITLE transcription initiation factor sigma B - Bacillus subtilis ALTERNATE_NAMES 37K minor sigma factor rpoF; RNA polymerase chain sigma-37; RNA polymerase general stress sigma factor sigB ORGANISM #formal_name Bacillus subtilis DATE 16-Aug-1988 #sequence_revision 02-Jul-1998 #text_change 16-Jun-2000 ACCESSIONS A27762; A25944; H69705; C36131 REFERENCE A91861 !$#authors Duncan, M.L.; Kalman, S.S.; Thomas, S.M.; Price, C.W. !$#journal J. Bacteriol. (1987) 169:771-778 !$#title Gene encoding the 37,000-dalton minor sigma factor of !1Bacillus subtilis RNA polymerase: isolation, nucleotide !1sequence, chromosomal locus, and cryptic function. !$#cross-references MUID:87109071; PMID:3027048 !$#accession A27762 !'##molecule_type DNA !'##residues 1-264 ##label DUN !'##cross-references GB:M34995; NID:g143457; PIDN:AAA22713.1; !1PID:g143460 REFERENCE A25944 !$#authors Binnie, C.; Lampe, M.; Losick, R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:5943-5947 !$#title Gene encoding the sigma-37 species of RNA polymerase sigma !1factor from Bacillus subtilis. !$#cross-references MUID:86287370; PMID:3016731 !$#accession A25944 !'##molecule_type DNA !'##residues 3-264 ##label BIN !'##cross-references GB:M13927; NID:g143537; PIDN:AAA22754.1; !1PID:g143538 !'##experimental_source strain 168 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69705 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-264 ##label KUN !'##cross-references GB:Z99106; GB:AL009126; NID:g2632653; !1PIDN:CAB12280.1; PID:g2632773 !'##experimental_source strain 168 COMMENT This minor form of sigma factor is present during !1logarithmic growth; disruption of the gene for this protein !1created no observable phenotypic difference. GENETICS !$#gene sigB; rpoF CLASSIFICATION #superfamily transcription sigma factor G; transcription !1initiation factor sigma katF homology KEYWORDS DNA binding; sigma factor; transcription initiation FEATURE !$38-256 #domain transcription initiation factor sigma katF !8homology #label KTF SUMMARY #length 264 #molecular-weight 30145 #checksum 9220 SEQUENCE /// ENTRY A55249 #type complete TITLE transcription initiation factor sigma K precursor - Bacillus subtilis ALTERNATE_NAMES sigma-27; sporulation mother cell-specific (late) RNA polymerase factor sigma K; stage IV sporulation protein CB ORGANISM #formal_name Bacillus subtilis DATE 20-Feb-1993 #sequence_revision 02-Jul-1998 #text_change 16-Jun-2000 ACCESSIONS B43656; A31093; S02441; A28627; A69714; D69712; A55249; !1A55250; B55249; C55249 REFERENCE A43656 !$#authors Sato, T.; Samori, Y.; Kobayashi, Y. !$#journal J. Bacteriol. (1990) 172:1092-1098 !$#title The cisA cistron of Bacillus subtilis sporulation gene !1spoIVC encodes a protein homologous to a site-specific !1recombinase. !$#cross-references MUID:90130265; PMID:2105293 !$#accession B43656 !'##status translation not shown !'##molecule_type DNA !'##residues 1-115,'VITKGGCIHPSLIRFNIYGVRIHNGNFFHDKVNNCFFIFKS' ##label !1SAT !'##cross-references GB:M29040; NID:g142689; PIDN:AAA22315.1; !1PID:g455127 !'##genetics NTER !'##note this sequence represents the open reading frame of the spoIVCB !1locus prior to chromosomal rearrangement REFERENCE A31093 !$#authors Kunkel, B.; Sandman, K.; Panzer, S.; Youngman, P.; Losick, !1R. !$#journal J. Bacteriol. (1988) 170:3513-3522 !$#title The promoter for a sporulation gene in the spoIVC locus of !1Bacillus subtilis and its use in studies of temporal and !1spatial control of gene expression. !$#cross-references MUID:88298658; PMID:2841290 !$#accession A31093 !'##molecule_type DNA !'##residues 1-43 ##label KUNK !'##cross-references GB:M21657; NID:g143637; PIDN:AAA22803.1; !1PID:g143638 !'##genetics NTER REFERENCE S02441 !$#authors Errington, J. !$#journal FEBS Lett. (1987) 224:257-260 !$#title Two separable functional domains in the sigma-subunit of RNA !1polymerase in Bacillus subtilis? !$#cross-references MUID:88083547; PMID:3121385 !$#accession S02441 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 'MPPLFVMN',113-242 ##label ERR1 !'##genetics CTER !'##note this sequence represents the open reading frame of the spoIIIC !1locus prior to chromosomal rearrangement REFERENCE A28627 !$#authors Errington, J.; Rong, S.; Rosenkrantz, M.S.; Sonenshein, A.L. !$#journal J. Bacteriol. (1988) 170:1162-1167 !$#title Transcriptional regulation and structure of the Bacillus !1subtilis sporulation locus spoIIIC. !$#cross-references MUID:88139173; PMID:3125151 !$#accession A28627 !'##molecule_type DNA !'##residues 'MPPLFVMN',113-242 ##label ERR2 !'##cross-references GB:M19299; NID:g143643; PIDN:AAA22805.1; !1PID:g143644 !'##genetics CTER REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69714 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-115,'VITKGGCIHPSLIRFNIYGVRIHNGNFFHDKVNNCFFIFKS' ##label !1KUN1 !'##cross-references GB:Z99117; GB:AL009126; NID:g2634966; !1PIDN:CAB14517.1; PID:g2635021 !'##experimental_source strain 168 !'##genetics NTER !$#accession D69712 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 'MPPLFVMN',113-242 ##label KUN2 !'##cross-references GB:Z99117; GB:AL009126; NID:g2634966; !1PIDN:CAB14580.1; PID:g2635084 !'##experimental_source strain 168 !'##genetics CTER REFERENCE A55249 !$#authors Stragier, P.; Kunkel, B.; Kroos, L.; Losick, R. !$#journal Science (1989) 243:507-512 !$#title Chromosomal rearrangement generating a composite gene for a !1developmental transcription factor. !$#cross-references MUID:89100299; PMID:2536191 !$#contents annotation !$#accession A55249 !'##molecule_type DNA !'##residues 'M',3-115,'VITKGGCIHPSLIRFNIYGVRIHNGNFFHDKVNNCFFIFKS' !1##label STR !'##cross-references GB:M23103; NID:g143641; PIDN:AAA22804.1; !1PID:g143642 !'##note this sequence was not determined in this report; the authors !1use a GTG start codon rather than the preceding ATG codon REFERENCE A55250 !$#authors Kroos, L.; Kunkel, B.; Losick, R. !$#journal Science (1989) 243:526-529 !$#title Switch protein alters specificity of RNA polymerase !1containing a compartment-specific sigma factor. !$#cross-references MUID:89100301; PMID:2492118 !$#accession A55250 !'##molecule_type protein !'##residues 22-34 ##label KRO COMMENT Activity of this mother cell-specific sigma factor is !1coordinated with the expression of the forespore-specific !1factor sigma G. The transmembrane protein BofA !1(bypass-of-forespore, see PIR:B41869) plays a role in signal !1transduction from forespore to mother cell by mediating !1cleavage of the propeptide from the sigma K precursor. COMMENT The mother cell chromosome undergoes a rearrangement to !1assemble a complete gene for the sigma K precursor from the !1spoIVCB and spoIIIC loci. This process need not be !1reversible because the mother cell lyses after the formation !1of the spore from the forespore is complete. COMMENT The rearrangement occurs within 5 nucleotides encoding !1residues 113-114 and is performed by the sigK-creating !1site-specific DNA recombinase cisA/spoIVCA (see PIR:A43656). GENETICS NTER !$#gene spoIVCB; sigK !$#start_codon GTG !$#note locus spoIVCB encodes the amino-terminal portion of sigma K !1precursor after chromosomal rearrangement in mother cell !1compartment; composite gene called sigK GENETICS CTER !$#gene spoIIIC; sigK !$#note locus spoIIIC encodes the carboxyl-terminal portion of sigma !1K precursor after chromosomal rearrangement in mother cell !1compartment; composite gene called sigK CLASSIFICATION #superfamily transcription initiation factor sigma K; !1transcription initiation factor sigma katF homology KEYWORDS DNA binding; sigma factor; sporulation; transcription !1initiation FEATURE !$1-113 #region spoIVCB gene-derived\ !$1-21 #domain propeptide #status predicted #label PRO\ !$22-242 #product transcription initiation factor sigma K !8#status experimental #label MAT\ !$57-226 #domain transcription initiation factor sigma katF !8homology #label KTF\ !$114-242 #region spoIIIC gene-derived SUMMARY #length 242 #molecular-weight 27569 #checksum 4730 SEQUENCE /// ENTRY A39441 #type complete TITLE transcription initiation factor sigma 28 precursor - Bacillus thuringiensis subsp. kurstaki ORGANISM #formal_name Bacillus thuringiensis subsp. kurstaki DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A39441; S27277; A37800; S18772 REFERENCE A39441 !$#authors Adams, L.F.; Brown, K.L.; Whiteley, H.R. !$#journal J. Bacteriol. (1991) 173:3846-3854 !$#title Molecular cloning and characterization of two genes encoding !1sigma factors that direct transcription from a Bacillus !1thuringiensis crystal protein gene promoter. !$#cross-references MUID:91267951; PMID:1904859 !$#accession A39441 !'##molecule_type DNA !'##residues 1-237 ##label ADA !'##cross-references GB:X56696; NID:g40331; PIDN:CAA40024.1; PID:g580953 !'##experimental_source strain HD-1-Dipel !$#accession S27277 !'##molecule_type protein !'##residues 20-37 ##label ADA2 REFERENCE A37800 !$#authors Brown, K.L.; Whiteley, H.R. !$#journal J. Bacteriol. (1990) 172:6682-6688 !$#title Isolation of the second Bacillus thuringiensis RNA !1polymerase that transcribes from a crystal protein gene !1promoter. !$#cross-references MUID:91072211; PMID:1701426 !$#accession A37800 !'##status preliminary !'##molecule_type protein !'##residues 20-37 ##label BRO GENETICS !$#start_codon TTG CLASSIFICATION #superfamily transcription initiation factor sigma K; !1transcription initiation factor sigma katF homology KEYWORDS DNA binding; sigma factor; transcription initiation FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-237 #product transcription initiation factor sigma 28 !8#status experimental #label MAT\ !$55-230 #domain transcription initiation factor sigma katF !8homology #label KTF SUMMARY #length 237 #molecular-weight 27136 #checksum 332 SEQUENCE /// ENTRY JU0083 #type complete TITLE transcription initiation factor sigma E precursor - Bacillus subtilis ALTERNATE_NAMES RNA polymerase sigma factor spoIIGB, sporulation mother cell-specific (early) ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S07337; S08225; B69706; JU0083 REFERENCE S07337 !$#authors Stragier, P.; Bouvier, J.; Bonamy, C.; Szulmajster, J. !$#journal Nature (1984) 312:376-378 !$#title A developmental gene product of Bacillus subtilis homologous !1to the sigma factor of Escherichia coli. !$#cross-references MUID:85061557; PMID:6438529 !$#accession S07337 !'##molecule_type DNA !'##residues 1-239 ##label STR !'##cross-references EMBL:X01180; NID:g40168; PIDN:CAA25620.1; !1PID:g40169 REFERENCE S08223 !$#authors Masuda, E.S.; Anaguchi, H.; Sato, T.; Takeuchi, M.; !1Kobayashi, Y. !$#journal Nucleic Acids Res. (1990) 18:657 !$#title Nucleotide sequence of the sporulation gene spoIIGA from !1Bacillus subtilis. !$#cross-references MUID:90174995; PMID:2106671 !$#accession S08225 !'##molecule_type DNA !'##residues 1-55 ##label MAS !'##cross-references EMBL:X17344; NID:g40165; PIDN:CAA35226.1; !1PID:g40167 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69706 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-65,'I',67-138,'Y',140-239 ##label KUN !'##cross-references GB:Z99112; GB:AL009126; NID:g2633902; !1PIDN:CAB13406.1; PID:g2633905 !'##experimental_source strain 168 COMMENT This sigma factor is activated by processing by the product !1of the spoIIGA gene. GENETICS !$#gene spoIIGB; sigE !$#map_position 135 (degrees) CLASSIFICATION #superfamily transcription initiation factor sigma K; !1transcription initiation factor sigma katF homology KEYWORDS DNA binding; sigma factor; sporulation; transcription !1initiation FEATURE !$64-237 #domain transcription initiation factor sigma katF !8homology #label KTF SUMMARY #length 239 #molecular-weight 27652 #checksum 4266 SEQUENCE /// ENTRY B39441 #type complete TITLE transcription initiation factor sigma 35 precursor - Bacillus thuringiensis subsp. kurstaki ORGANISM #formal_name Bacillus thuringiensis subsp. kurstaki DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B39441; S27282; I40581; S18774 REFERENCE A39441 !$#authors Adams, L.F.; Brown, K.L.; Whiteley, H.R. !$#journal J. Bacteriol. (1991) 173:3846-3854 !$#title Molecular cloning and characterization of two genes encoding !1sigma factors that direct transcription from a Bacillus !1thuringiensis crystal protein gene promoter. !$#cross-references MUID:91267951; PMID:1904859 !$#accession B39441 !'##molecule_type DNA !'##residues 1-239 ##label ADA !'##cross-references EMBL:X56697; NID:g40333; PIDN:CAA40026.1; !1PID:g40335 !'##experimental_source strain HD-1-Dipel !$#accession S27282 !'##molecule_type protein !'##residues 28-52 ##label AD2 CLASSIFICATION #superfamily transcription initiation factor sigma K; !1transcription initiation factor sigma katF homology KEYWORDS DNA binding; sigma factor; transcription initiation FEATURE !$1-27 #domain propeptide #status predicted #label PRO\ !$28-239 #product transcription initiation factor sigma 35 !8#status experimental #label MAT\ !$64-237 #domain transcription initiation factor sigma katF !8homology #label KTF SUMMARY #length 239 #molecular-weight 27636 #checksum 3602 SEQUENCE /// ENTRY RNECKF #type complete TITLE transcription initiation factor sigma katF - Escherichia coli (strain K-12) ALTERNATE_NAMES alternative sigma factor, sigma 38; transcription initiation factor sigma-18 ORGANISM #formal_name Escherichia coli DATE 31-Dec-1991 #sequence_revision 30-Jan-1998 #text_change 01-Mar-2002 ACCESSIONS A65055; S45581; S14901; C55522; S26097; S26748; S26750; !1T45000; S06199; S26749 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65055 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-330 ##label BLAT !'##cross-references GB:AE000358; GB:U00096; NID:g2367156; !1PIDN:AAC75783.1; PID:g1789098; UWGP:b2741 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S45579 !$#authors Takayanagi, Y.; Tanaka, K.; Takahashi, H. !$#journal Mol. Gen. Genet. (1994) 243:525-531 !$#title Structure of the 5' upstream region and the regulation of !1the rpoS gene of Escherichia coli. !$#cross-references MUID:94268497; PMID:8208244 !$#accession S45581 !'##molecule_type DNA !'##residues 1-32,'L',34-72 ##label TAK !'##cross-references EMBL:D17549; NID:g404097; PIDN:BAA21003.1; !1PID:g4433062 REFERENCE S14901 !$#authors Mulvey, M.R.; Loewen, P.C. !$#journal Nucleic Acids Res. (1989) 17:9979-9991 !$#title Nucleotide sequence of katF of Escherichia coli suggests !1KatF protein is a novel sigma transcription factor. !$#cross-references MUID:90098856; PMID:2690013 !$#accession S14901 !'##molecule_type DNA !'##residues 'MFRQGITGRSHL',1-28,'P',30-195,'V',197-327, !1'LPRVSKHLSERPVSSEAGFFCAQ' ##label MUL !'##cross-references EMBL:X16400; NID:g41852; PIDN:CAA34435.1; !1PID:g41853 !'##note it is uncertain whether Met-1 or Met-1 is the initiator !'##note the authors translated the codon GGT for residue 8 as Arg and !1AGG for residue 9 as Gly !'##note in the authors' translation an additional Asn is shown after !1160-Asn, residues 161-169 are displaced one codon to the !1right and 170-His is not shown REFERENCE A55522 !$#authors Ichikawa, J.K.; Li, C.; Fu, J.; Clarke, S. !$#journal J. Bacteriol. (1994) 176:1630-1638 !$#title A gene at 59 minutes on the Escherichia coli chromosome !1encodes a lipoprotein with unusual amino acid repeat !1sequences. !$#cross-references MUID:94179096; PMID:8132457 !$#accession C55522 !'##status preliminary !'##molecule_type DNA !'##residues 1-12 ##label ICH !'##cross-references GB:L07869 REFERENCE S26097 !$#authors Ivanova, A.N. !$#submission submitted to the EMBL Data Library, August 1992 !$#accession S26097 !'##molecule_type DNA !'##residues 'MFRQGITGRSHL',1-24,'L',26-326,'P',328, !1'ARNPANAGAEYRSAVPRVSKHLSERPVSSEAGLFCAQ' ##label IVA !'##cross-references EMBL:Z14966; NID:g41854; PIDN:CAA78689.1; !1PID:g41855 !'##experimental_source strain KatF 1137 REFERENCE S26748 !$#authors Ivanova, A.; Renshaw, M.; Guntaka, R.V.; Eisenstark, A. !$#journal Nucleic Acids Res. (1992) 20:5479-5480 !$#title DNA base sequence variability in katF (putative sigma !1factor) gene of Escherichia coli. !$#cross-references MUID:93065224; PMID:1437569 !$#accession S26748 !'##molecule_type DNA !'##residues 323-326,'P',328,'ARNPANAGAEYRSAVPRVSKHLSERPVSSEAGLFCAQ' !1##label IVW !'##cross-references EMBL:Z14966 !'##experimental_source strain KatF 1137 !$#accession S26750 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 'MFRQGITGRSHL',1-24,'L',26-330 ##label IVF !'##cross-references EMBL:Z14969; NID:g41860; PIDN:CAA78692.1; !1PID:g41861 !'##experimental_source wildtype MP 180 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1992 !'##note only a part of the translation is shown REFERENCE Z22892 !$#authors Carter, P.E.; Thomson-Carter, F.M. !$#submission submitted to the EMBL Data Library, May 1998 !$#description Comparison of the mutS-rpoS region from Escherichia coli !1O157:H7, Verocytotoxin-containing and !1Non-verocytotoxin-containing E.coli. !$#accession T45000 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-32,'E',34-330 ##label CAR !'##cross-references EMBL:AJ006210; PIDN:CAB43502.1 !'##experimental_source strain O157:H7 GENETICS !$#gene rpoS; katF !$#map_position 59.0 min CLASSIFICATION #superfamily transcription initiation factor sigma katF; !1transcription initiation factor sigma katF homology KEYWORDS DNA binding; nucleotidyltransferase; sigma factor; !1transcription initiation FEATURE !$96-322 #domain transcription initiation factor sigma katF !8homology #label KTF SUMMARY #length 330 #molecular-weight 37971 #checksum 7046 SEQUENCE /// ENTRY RGECH #type complete TITLE RNA polymerase sigma32 factor [imported] - Escherichia coli (strain K-12) ALTERNATE_NAMES heat shock regulatory protein ORGANISM #formal_name Escherichia coli DATE 28-Aug-1985 #sequence_revision 21-Nov-1997 #text_change 01-Mar-2002 ACCESSIONS H65142; A00700; A94012; A31092; S47680; A30761 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65142 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-284 ##label BLAT !'##cross-references GB:AE000422; GB:U00096; NID:g1789868; !1PIDN:AAC76486.1; PID:g1789871; UWGP:b3461 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A90851 !$#authors Landick, R.; Vaughn, V.; Lau, E.T.; VanBogelen, R.A.; !1Erickson, J.W.; Neidhardt, F.C. !$#journal Cell (1984) 38:175-182 !$#title Nucleotide sequence of the heat shock regulatory gene of E. !1coli suggests its protein product may be a transcription !1factor. !$#cross-references MUID:84282700; PMID:6088062 !$#accession A00700 !'##molecule_type DNA !'##residues 1,'A',3-14,'G',16-284 ##label LAN !'##cross-references GB:J05516 !'##experimental_source K12 REFERENCE A94012 !$#authors Yura, T.; Tobe, T.; Ito, K.; Osawa, T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:6803-6807 !$#title Heat shock regulatory gene (htpR) of Escherichia coli is !1required for growth at high temperature but is dispensable !1at low temperature. !$#cross-references MUID:85038603; PMID:6387714 !$#accession A94012 !'##molecule_type DNA !'##residues 1-184,'A',186-192,'HA',195-284 ##label YUR !'##cross-references GB:K02177; NID:g146409; PIDN:AAA23991.1; !1PID:g146410 REFERENCE A91877 !$#authors Calendar, R.; Erickson, J.W.; Halling, C.; Nolte, A. !$#journal J. Bacteriol. (1988) 170:3479-3484 !$#title Deletion and insertion mutations in the rpoH gene of !1Escherichia coli that produce functional sigma-32. !$#cross-references MUID:88298653; PMID:2841288 !$#accession A31092 !'##molecule_type DNA !'##residues 1-284 ##label CAL !'##cross-references GB:M20668; NID:g147731; PIDN:AAA24587.1; !1PID:g147732 REFERENCE S47666 !$#authors Plunkett, G. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S47680 !'##status preliminary !'##molecule_type DNA !'##residues 1-284 ##label PLU !'##cross-references EMBL:U00039; NID:g466582; PIDN:AAB18436.1; !1PID:g466597 GENETICS !$#gene rpoH; htpR !$#map_position 76 min FUNCTION !$#description positively controls the synthesis of heat shock proteins, !1the polypeptides preferentially synthesized at elevated !1temperature CLASSIFICATION #superfamily transcription initiation factor sigma katF; !1transcription initiation factor sigma katF homology KEYWORDS DNA binding; heat shock; sigma factor; stress-induced !1protein; transcription initiation FEATURE !$55-284 #domain transcription initiation factor sigma katF !8homology #label KTF SUMMARY #length 284 #molecular-weight 32468 #checksum 7431 SEQUENCE /// ENTRY S04697 #type complete TITLE transcription initiation factor sigma 32 - Citrobacter freundii ALTERNATE_NAMES heat shock regulatory protein htpR ORGANISM #formal_name Citrobacter freundii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S04697 REFERENCE S04697 !$#authors Garvin, L.D.; Hardies, S.C. !$#journal Nucleic Acids Res. (1989) 17:4889 !$#title Nucleotide sequence for the htpR gene from Citrobacter !1freundii. !$#cross-references MUID:89315239; PMID:2664713 !$#accession S04697 !'##molecule_type DNA !'##residues 1-284 ##label GAR !'##cross-references EMBL:X14960; NID:g40468; PIDN:CAA33083.1; !1PID:g40469 GENETICS !$#gene htpR CLASSIFICATION #superfamily transcription initiation factor sigma katF; !1transcription initiation factor sigma katF homology KEYWORDS DNA binding; heat shock; sigma factor; stress-induced !1protein; transcription initiation FEATURE !$55-284 #domain transcription initiation factor sigma katF !8homology #label KTF SUMMARY #length 284 #molecular-weight 32573 #checksum 7736 SEQUENCE /// ENTRY JC4040 #type complete TITLE transcription initiation factor sigma 32 - Pseudomonas aeruginosa ALTERNATE_NAMES heat shock sigma factor 32; rpoH protein ORGANISM #formal_name Pseudomonas aeruginosa DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 31-Dec-2000 ACCESSIONS JC4040; H83598 REFERENCE JC4040 !$#authors Benvenisti, L.; Koby, S.; Rutman, A.; Giladi, H.; Yura, T.; !1Oppenheim, A.B. !$#journal Gene (1995) 155:73-76 !$#title Cloning and primary sequence of the rpoH gene from !1Pseudomonas aeruginosa. !$#cross-references MUID:95212932; PMID:7698670 !$#accession JC4040 !'##molecule_type DNA !'##residues 1-284 ##label BEN !'##cross-references GB:S77322; NID:g998759; PIDN:AAB33935.1; !1PID:g998760 REFERENCE A82950 !$#authors Stover, C.K.; Pham, X.Q.; Erwin, A.L.; Mizoguchi, S.D.; !1Warrener, P.; Hickey, M.J.; Brinkman, F.S.L.; Hufnagle, !1W.O.; Kowalik, D.J.; Lagrou, M.; Garber, R.L.; Goltry, L.; !1Tolentino, E.; Westbrook-Wadman, S.; Yuan, Y.; Brody, L.L.; !1Coulter, S.N.; Folger, K.R.; Kas, A.; Larbig, K.; Lim, R.M.; !1Smith, K.A.; Spencer, D.H.; Wong, G.K.S.; Wu, Z.; Paulsen, !1I.T.; Reizer, J.; Saier, M.H.; Hancock, R.E.W.; Lory, S.; !1Olson, M.V. !$#journal Nature (2000) 406:959-964 !$#title Complete genome sequence of Pseudomonas aeruginosa PA01, an !1opportunistic pathogen. !$#cross-references MUID:20437337; PMID:10984043 !$#accession H83598 !'##status preliminary !'##molecule_type DNA !'##residues 1-284 ##label STO !'##cross-references GB:AE004475; GB:AE004091; NID:g9946221; !1PIDN:AAG03765.1; GSPDB:GN00131; PASP:PA0376 !'##experimental_source strain PAO1 GENETICS !$#gene rpoH; PA0376 CLASSIFICATION #superfamily transcription initiation factor sigma katF; !1transcription initiation factor sigma katF homology KEYWORDS DNA binding; heat shock; sigma factor; stress-induced !1protein; transcription initiation FEATURE !$56-284 #domain transcription initiation factor sigma katF !8homology #label KTF SUMMARY #length 284 #molecular-weight 32581 #checksum 1663 SEQUENCE /// ENTRY H64058 #type complete TITLE transcription initiation factor sigma 32 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS H64058 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession H64058 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-281 ##label TIGR !'##cross-references GB:U32713; GB:L42023; NID:g1573231; !1PIDN:AAC21935.1; PID:g1573235; TIGR:HI0269 CLASSIFICATION #superfamily transcription initiation factor sigma katF; !1transcription initiation factor sigma katF homology KEYWORDS DNA binding; heat shock; sigma factor; stress-induced !1protein; transcription initiation FEATURE !$54-281 #domain transcription initiation factor sigma katF !8homology #label KTF SUMMARY #length 281 #molecular-weight 32033 #checksum 4013 SEQUENCE /// ENTRY S61292 #type complete TITLE transcription initiation factor sigma mysA - Mycobacterium smegmatis ALTERNATE_NAMES sigma factor mysA ORGANISM #formal_name Mycobacterium smegmatis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS S61292; S61289 REFERENCE S61289 !$#authors Predich, M.; Doukhan, L.; Nair, G.; Smith, I. !$#journal Mol. Microbiol. (1995) 15:355-366 !$#title Characterization of RNA polymerase and two sigma-factor !1genes from Mycobacterium smegmatis. !$#cross-references MUID:95264921; PMID:7746156 !$#accession S61292 !'##molecule_type DNA !'##residues 1-466 ##label PRE !'##cross-references EMBL:U09821; NID:g555679; PIDN:AAA85642.1; !1PID:g555680 !$#accession S61289 !'##molecule_type protein !'##residues 452-466 ##label PRW GENETICS !$#gene mysA !$#start_codon GTG CLASSIFICATION #superfamily Streptomyces transcription initiation factor !1sigma; transcription initiation factor sigma katF homology KEYWORDS DNA binding; sigma factor; transcription initiation FEATURE !$235-461 #domain transcription initiation factor sigma katF !8homology #label KTF SUMMARY #length 466 #molecular-weight 51503 #checksum 4548 SEQUENCE /// ENTRY S41307 #type complete TITLE transcription initiation factor sigma - Streptomyces griseus ORGANISM #formal_name Streptomyces griseus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S41307 REFERENCE S41306 !$#authors Marcos, A.T.; Diez, B.; Gutierrez, S.; Fernandez, F.J.; !1Velasco, J.; Martin, J.F. !$#submission submitted to the EMBL Data Library, December 1993 !$#description Organization and expression of the hrdB-sprC gene cluster of !1streptomyces griseus encoding a sigma factor protein and a !1serine protease. Role on growth and sporulation of !1streptomyces. !$#accession S41307 !'##status preliminary !'##molecule_type DNA !'##residues 1-510 ##label MAR !'##cross-references EMBL:X75952; NID:g440164; PIDN:CAA53564.1; !1PID:g581664 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily Streptomyces transcription initiation factor !1sigma; transcription initiation factor sigma katF homology KEYWORDS DNA binding; sigma factor; transcription initiation FEATURE !$279-505 #domain transcription initiation factor sigma katF !8homology #label KTF SUMMARY #length 510 #molecular-weight 55795 #checksum 1415 SEQUENCE /// ENTRY S11712 #type complete TITLE transcription initiation factor sigma hrdB - Streptomyces coelicolor ALTERNATE_NAMES sigma-like transcription factor ORGANISM #formal_name Streptomyces coelicolor DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Dec-1999 ACCESSIONS S11712; JH0496; T42032; B40116 REFERENCE S11711 !$#authors Tanaka, K.; Shiina, T.; Takahashi, H. !$#submission submitted to the EMBL Data Library, May 1990 !$#description Multiple homolog genes for principal sigma subunit of !1Streptomyces coelicolor A3(2). !$#accession S11712 !'##molecule_type DNA !'##residues 1-442 ##label EMB !'##cross-references EMBL:X52983; NID:g48744; PIDN:CAA37175.1; !1PID:g48745 !'##experimental_source strain A3(2) REFERENCE JH0496 !$#authors Shiina, T.; Tanaka, K.; Takahashi, H. !$#journal Gene (1991) 107:145-148 !$#title Sequence of hrdB, an essential gene encoding sigma-like !1transcription factor of Streptomyces coelicolor A3(2): !1homology to principal sigma factors. !$#cross-references MUID:92077425; PMID:1840545 !$#accession JH0496 !'##molecule_type DNA !'##residues 1-429,'QG',432-442 ##label SHI !'##cross-references EMBL:X52983 !'##experimental_source A3[2] !'##note the authors translated the codon CAG for residue 430 as His and !1GGG for residue 431 as Pro !$#accession T42032 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-442 ##label SH2 !'##cross-references EMBL:X52983; PIDN:CAA37175.1 REFERENCE A40116 !$#authors Tanaka, K.; Shiina, T.; Takahashi, H. !$#journal Science (1988) 242:1040-1042 !$#title Multiple principal sigma factor homologs in eubacteria: !1identification of the "rpoD box". !$#cross-references MUID:89058616; PMID:3194753 !$#accession B40116 !'##status preliminary; nucleic acid sequence not shown; not compared !1with conceptual translation !'##molecule_type DNA !'##residues 237-288 ##label TAN COMMENT This protein is the functional homolog of the principal !1sigma factors involved in the transcription of housekeeping !1genes. GENETICS !$#gene hrdB CLASSIFICATION #superfamily Streptomyces transcription initiation factor !1sigma; transcription initiation factor sigma katF homology KEYWORDS DNA binding; sigma factor; transcription initiation FEATURE !$211-437 #domain transcription initiation factor sigma katF !8homology #label KTF SUMMARY #length 442 #molecular-weight 48413 #checksum 4794 SEQUENCE /// ENTRY B70531 #type complete TITLE probable sigA protein - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 18-Nov-2002 ACCESSIONS B70531 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession B70531 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-528 ##label COL !'##cross-references GB:Z96072; GB:AL123456; NID:g3261793; !1PIDN:CAB09463.1; PID:g2181994 !'##experimental_source strain H37Rv GENETICS !$#gene sigA CLASSIFICATION #superfamily Streptomyces transcription initiation factor !1sigma; transcription initiation factor sigma katF homology FEATURE !$297-523 #domain transcription initiation factor sigma katF !8homology #label KTF SUMMARY #length 528 #molecular-weight 57800 #checksum 3019 SEQUENCE /// ENTRY RNPSSN #type complete TITLE transcription initiation factor sigma rpoN - Pseudomonas putida ORGANISM #formal_name Pseudomonas putida DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 24-Jul-1997 ACCESSIONS S15918; S06712 REFERENCE S15918 !$#authors Koehler, T.; Cayrol, J.M.; Ramos, J.L.; Harayama, S. !$#journal Nucleic Acids Res. (1989) 17:10125 !$#title Nucleotide and deduced amino acid sequence of the RpoN !1sigma-factor of Pseudomonas putida. !$#cross-references MUID:90098799; PMID:2602128 !$#accession S15918 !'##status translation not shown !'##molecule_type DNA !'##residues 1-497 ##label KOE !'##cross-references EMBL:X16474 GENETICS !$#gene rpoN CLASSIFICATION #superfamily Pseudomonas transcription initiation factor !1sigma KEYWORDS DNA binding; sigma factor; transcription initiation SUMMARY #length 497 #molecular-weight 56415 #checksum 239 SEQUENCE /// ENTRY RNECO #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) omega chain - Escherichia coli (strain K-12) ALTERNATE_NAMES transcriptase omega chain ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 01-Mar-2002 ACCESSIONS A29038; JV0041; C65166 REFERENCE A29038 !$#authors Gentry, D.R.; Burgess, R.R. !$#journal Gene (1986) 48:33-40 !$#title The cloning and sequence of the gene encoding the omega !1subunit of Escherichia coli RNA polymerase. !$#cross-references MUID:87163514; PMID:3549461 !$#accession A29038 !'##molecule_type DNA !'##residues 1-91 ##label GEN !'##cross-references GB:M15266; NID:g146977; PIDN:AAA24229.1; !1PID:g146978 REFERENCE A30374 !$#authors Sarubbi, E.; Rudd, K.E.; Xiao, H.; Ikehara, K.; Kalman, M.; !1Cashel, M. !$#journal J. Biol. Chem. (1989) 264:15074-15082 !$#title Characterization of the spoT gene of Escherichia coli. !$#cross-references MUID:89359321; PMID:2549050 !$#accession JV0041 !'##molecule_type DNA !'##residues 1-91 ##label SAR !'##cross-references GB:M24503; GB:J04976; NID:g147863; PIDN:AAB00159.1; !1PID:g147864 !'##experimental_source strain JM109 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65166 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-91 ##label BLAT !'##cross-references GB:AE000442; GB:U00096; NID:g2367253; !1PIDN:AAC76673.1; PID:g1790081; UWGP:b3649 !'##experimental_source strain K-12, substrain MG1655 COMMENT In E. coli this protein binds with both the core and the !1holo RNA polymerase; although it copurifies with RNA !1polymerase, reconsititution experiments suggest that it is !1not required for transcription. GENETICS !$#gene rpoZ !$#map_position 82 min CLASSIFICATION #superfamily DNA-directed RNA polymerase omega chain KEYWORDS nucleotidyltransferase; RNA biosynthesis; transcription SUMMARY #length 91 #molecular-weight 10237 #checksum 8833 SEQUENCE /// ENTRY JT0302 #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) delta chain rpoE - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 31-Mar-1992 #sequence_revision 06-Feb-1995 #text_change 16-Jun-2000 ACCESSIONS JT0302; H32354; S55422; H69698 REFERENCE JT0302 !$#authors Lampe, M.; Binnie, C.; Schmidt, R.; Losick, R. !$#journal Gene (1988) 67:13-19 !$#title Cloned gene encoding the delta subunit of Bacillus subtilis !1RNA polymerase. !$#cross-references MUID:88329737; PMID:2843435 !$#accession JT0302 !'##molecule_type DNA !'##residues 1-173 ##label LAM !'##cross-references GB:M21677; NID:g143455; PIDN:AAA22710.1; !1PID:g143456 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE A91883 !$#authors Trach, K.; Chapman, J.W.; Piggot, P.; LeCoq, D.; Hoch, J.A. !$#journal J. Bacteriol. (1988) 170:4194-4208 !$#title Complete sequence and transcriptional analysis of the spo0F !1region of the Bacillus subtilis chromosome. !$#cross-references MUID:88314920; PMID:2457578 !$#accession H32354 !'##molecule_type DNA !'##residues 143-173 ##label TRA !'##cross-references GB:M22039; NID:g460910; PIDN:AAA16800.1; !1PID:g143596 REFERENCE S55414 !$#authors Glaser, P.; Danchin, A. !$#submission submitted to the EMBL Data Library, May 1995 !$#description Cloning and sequencing of the Bacillus subtilis chromosomal !1region from 320 degrees to 321 degrees. !$#accession S55422 !'##molecule_type DNA !'##residues 1-173 ##label GLA !'##cross-references EMBL:Z49782; NID:g853752; PIDN:CAA89869.1; !1PID:g853761 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69698 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-173 ##label KUN !'##cross-references GB:Z99123; GB:AL009126; NID:g2636240; !1PIDN:CAB15744.1; PID:g2636253 !'##experimental_source strain 168 COMMENT This protein binds to the RNA polymerase core enzyme with or !1without a sigma factor and enhances the specificity of !1transcription. Deletion of this protein does not impair !1viability or sporulation. GENETICS !$#gene rpoE !$#start_codon TTG CLASSIFICATION #superfamily DNA-directed RNA polymerase delta chain KEYWORDS nucleotidyltransferase FEATURE !$2-173 #product DNA-directed RNA polymerase delta chain !8#status experimental #label MAT SUMMARY #length 173 #molecular-weight 20399 #checksum 2711 SEQUENCE /// ENTRY RNBY3C #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) III chain C31 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES DNA-directed RNA polymerase C chain C31; DNA-directed RNA polymerase III 31K chain; protein N1769; protein YNL151c ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 21-Jul-2000 ACCESSIONS A36465; A38811; A33656; S42275; S60976; S63103; S63823; !1S12321 REFERENCE A36465 !$#authors Mosrin, C.; Riva, M.; Beltrame, M.; Cassar, E.; Sentenac, !1A.; Thuriaux, P. !$#journal Mol. Cell. Biol. (1990) 10:4737-4743 !$#title The RPC31 gene of Saccharomyces cerevisiae encodes a subunit !1of RNA polymerase C (III) with an acidic tail. !$#cross-references MUID:90355990; PMID:2201900 !$#accession A36465 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-251 ##label MOS !'##cross-references EMBL:X51498; NID:g4376; PIDN:CAA35866.1; PID:g4377 !$#accession A38811 !'##molecule_type protein !'##residues 10-20;58-63 ##label MOS2 REFERENCE A33656 !$#authors Haggren, W.; Kolodrubetz, D. !$#journal Mol. Cell. Biol. (1988) 8:1282-1289 !$#title The Saccharomyces cerevisiae ACP2 gene encodes an essential !1HMG1-like protein. !$#cross-references MUID:88216604; PMID:2835668 !$#accession A33656 !'##molecule_type DNA !'##residues 1-251 ##label HAG !'##cross-references EMBL:M20315 REFERENCE S42275 !$#authors Haggren, W.; Kolodrubetz, D. !$#submission submitted to the EMBL Data Library, February 1989 !$#accession S42275 !'##molecule_type DNA !'##residues 1-11,'R',13-204,'H',206-251 ##label HA2 !'##cross-references EMBL:M20315; NID:g170983; PIDN:AAA34390.1; !1PID:g170984 REFERENCE S60958 !$#authors Nasr, F.; Becam, A.M.; Herbert, C.J. !$#submission submitted to the EMBL Data Library, October 1995 !$#description The sequence of 36.8 kb from the left arm of chromosome XIV !1reveals 24 complete open reading frames: 18 correspond to !1new genes, one of which encodes a protein similar to the !1human myotonic dystrophy kinase. !$#accession S60976 !'##molecule_type DNA !'##residues 1-251 ##label NAS !'##cross-references EMBL:X92517; NID:g1050783; PIDN:CAA63288.1; !1PID:g1050801 REFERENCE S62967 !$#authors Nasr, F.; Becam, A.M.; Herbert, C. !$#submission submitted to the Protein Sequence Database, April 1996 !$#accession S63103 !'##molecule_type DNA !'##residues 1-251 ##label NAW !'##cross-references EMBL:Z71427; NID:g1302107; PIDN:CAA96038.1; !1PID:g1302108; GSPDB:GN00014; MIPS:YNL151c !'##experimental_source strain S288C REFERENCE S63805 !$#authors Nasr, F.; Becam, A.M.; Herbert, C.J. !$#journal Yeast (1996) 12:169-175 !$#title The sequence of 36.8 kb from the left arm of chromosome XIV !1reveals 24 complete open reading frames: 18 correspond to !1new genes, one of which encodes a protein similar to the !1human myotonic dystrophy kinase. !$#cross-references MUID:96287653; PMID:8686380 !$#accession S63823 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-251 ##label NAF !'##cross-references EMBL:X92517; NID:g1050783; PIDN:CAA63288.1; !1PID:g1050801 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1995 GENETICS !$#gene SGD:RPC31; APC2; RPC8; MIPS:YNL151c !'##cross-references SGD:S0005095; MIPS:YNL151c !$#map_position 14L CLASSIFICATION #superfamily DNA-directed RNA polymerase III chain C31 KEYWORDS DNA binding; nucleotidyltransferase; transcription FEATURE !$202-248 #region acidic SUMMARY #length 251 #molecular-weight 27724 #checksum 3034 SEQUENCE /// ENTRY S38627 #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) II 14.4K chain - human ALTERNATE_NAMES DNA-directed RNA polymerase II chain F ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 20-Apr-2000 ACCESSIONS I38175; S38627 REFERENCE I38175 !$#authors Acker, J.; Wintzerith, M.; Vigneron, M.; Kedinger, C. !$#journal DNA Seq. (1994) 4:329-331 !$#title A 14.4 KDa acidic subunit of human RNA polymerase II with a !1putative leucine-zipper. !$#cross-references MUID:95102114; PMID:7803819 !$#accession I38175 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-127 ##label ACK !'##cross-references EMBL:Z27113; NID:g415387; PIDN:CAA81629.1; !1PID:g415388 !'##note submitted to the EMBL Data Library, November 1993 GENETICS !$#gene GDB:POLR2F; RPB6; RPO26 !'##cross-references GDB:250746; OMIM:604414 !$#map_position 22q13.1-22q13.1 CLASSIFICATION #superfamily DNA-directed RNA polymerase chain RPO26 KEYWORDS nucleotidyltransferase; nucleus; transcription SUMMARY #length 127 #molecular-weight 14478 #checksum 6851 SEQUENCE /// ENTRY A56067 #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) II chain RPB6 - Chinese hamster ORGANISM #formal_name Cricetulus griseus #common_name Chinese hamster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A56067 REFERENCE A56067 !$#authors McKune, K.; Woychik, N.A. !$#journal Mol. Cell. Biol. (1994) 14:4155-4159 !$#title Functional substitution of an essential yeast RNA polymerase !1subunit by a highly conserved mammalian counterpart. !$#cross-references MUID:94254872; PMID:8196653 !$#accession A56067 !'##status preliminary !'##molecule_type mRNA !'##residues 1-127 ##label MCK !'##cross-references GB:S69934; NID:g546862; PIDN:AAB30834.1; !1PID:g546863 CLASSIFICATION #superfamily DNA-directed RNA polymerase chain RPO26 KEYWORDS nucleotidyltransferase; transcription SUMMARY #length 127 #molecular-weight 14478 #checksum 6851 SEQUENCE /// ENTRY S53013 #type complete TITLE RNA polymerase chain - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 23-Mar-2001 ACCESSIONS S53013 REFERENCE S53013 !$#authors Vigneron, M. !$#submission submitted to the EMBL Data Library, January 1995 !$#description Two human polypeptides are functionally interchangeable with !1the yeast zinc-binding subunits ABC10 alpha and ABC10 beta !1shared by all three RNA polymerases. !$#accession S53013 !'##status preliminary !'##molecule_type mRNA !'##residues 1-131 ##label VIG !'##cross-references EMBL:Z47726; NID:g717184; PIDN:CAA87655.1; !1PID:g717185 GENETICS !$#gene FlyBase:RpABC14 !'##cross-references FlyBase:FBgn0014025 CLASSIFICATION #superfamily DNA-directed RNA polymerase chain RPO26 SUMMARY #length 131 #molecular-weight 14722 #checksum 9338 SEQUENCE /// ENTRY RNBYR6 #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) chain RPO26 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES DNA-directed RNA polymerase 23K chain; DNA-directed RNA polymerase II sixth subunit; protein P9677.8; protein YPR187w; RPB6 protein ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 03-Dec-1999 ACCESSIONS S13307; A36352; B34588; A38846; S58817 REFERENCE A36352 !$#authors Archambault, J.; Schappert, K.T.; Friesen, J.D. !$#journal Mol. Cell. Biol. (1990) 10:6123-6131 !$#title A suppressor of an RNA polymerase II mutation of !1Saccharomyces cerevisiae encodes a subunit common to RNA !1polymerases I, II, and III. !$#cross-references MUID:91061718; PMID:2247052 !$#accession S13307 !'##molecule_type DNA !'##residues 1-155 ##label ARC1 !'##cross-references EMBL:M33924; NID:g172452; PIDN:AAA34989.1; !1PID:g172453 !$#accession A36352 !'##molecule_type mRNA !'##residues 1-155 ##label ARC2 !'##cross-references GB:M33924; NID:g172452; PIDN:AAA34989.1; !1PID:g172453 REFERENCE A34588 !$#authors Woychik, N.A.; Liao, S.M.; Kolodziej, P.A.; Young, R.A. !$#journal Genes Dev. (1990) 4:313-323 !$#title Subunits shared by eukaryotic nuclear RNA polymerases. !$#cross-references MUID:90249736; PMID:2186966 !$#accession B34588 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-155 ##label WOY1 !'##cross-references GB:X53288; NID:g287823; PIDN:CAA37382.1; !1PID:g287824 !$#accession A38846 !'##molecule_type protein !'##residues 48-60;99-115 ##label WOY2 REFERENCE S58816 !$#authors Miller, N. !$#submission submitted to the EMBL Data Library, April 1995 !$#description The sequence of S. cerevisiae cosmid 9677. !$#accession S58817 !'##molecule_type DNA !'##residues 1-155 ##label MIL !'##cross-references EMBL:U25841; NID:g786295; PIDN:AAB64616.1; !1PID:g786304; GSPDB:GN00016; MIPS:YPR187w COMMENT This protein is a subunit of DNA-directed RNA polymerases I, !1II, and III. GENETICS !$#gene SGD:RPO26; RPB6; MIPS:YPR187w !'##cross-references SGD:S0006391; MIPS:YPR187w !$#map_position 16R !$#introns 7/2 CLASSIFICATION #superfamily DNA-directed RNA polymerase chain RPO26 KEYWORDS nucleotidyltransferase FEATURE !$3-42 #region acidic\ !$65-97 #region basic SUMMARY #length 155 #molecular-weight 17910 #checksum 4345 SEQUENCE /// ENTRY C34588 #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) chain RPB8 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein O5070; protein YOR224c; protein YOR50-14 ORGANISM #formal_name Saccharomyces cerevisiae #variety strain S288C DATE 22-Jan-1993 #sequence_revision 08-Mar-1996 #text_change 21-Jul-2000 ACCESSIONS C34588; S60951; S67117; S71726 REFERENCE A34588 !$#authors Woychik, N.A.; Liao, S.M.; Kolodziej, P.A.; Young, R.A. !$#journal Genes Dev. (1990) 4:313-323 !$#title Subunits shared by eukaryotic nuclear RNA polymerases. !$#cross-references MUID:90249736; PMID:2186966 !$#accession C34588 !'##molecule_type DNA !'##residues 1-146 ##label WOY !'##cross-references GB:X53289; NID:g287825; PIDN:CAA37383.1; !1PID:g287826 REFERENCE S60938 !$#authors Galisson, F.; Dujon, B. !$#submission submitted to the EMBL Data Library, October 1995 !$#description Sequence and analysis of a 33 kb fragment from the right arm !1of chromosome XV of the yeast Saccharomyces cerevisiae. !$#accession S60951 !'##molecule_type DNA !'##residues 1-146 ##label GAL !'##cross-references EMBL:X92441; NID:g1050762; PIDN:CAA63187.1; !1PID:g1050776 REFERENCE S67104 !$#authors Boyer, J.; Fairhead, C.; Gaillon, L.; Galisson, F.; Michaux, !1G.; Thierry, A.; Dujon, B. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67117 !'##molecule_type DNA !'##residues 1-146 ##label BOY !'##cross-references EMBL:Z75132; NID:g1420517; PIDN:CAA99443.1; !1PID:g1420518; GSPDB:GN00015; MIPS:YOR224c !'##experimental_source strain S288C REFERENCE S71713 !$#authors Galisson, F.; Dujon, B. !$#journal Yeast (1996) 12:877-885 !$#title Sequence and analysis of a 33 kb fragment from the right arm !1of chromosome XV of the yeast Saccharomyces cerevisiae. !$#cross-references MUID:96437977; PMID:8840505 !$#accession S71726 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-146 ##label GAW !'##cross-references EMBL:X92441; NID:g1050762; PIDN:CAA63187.1; !1PID:g1050776 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1995 GENETICS !$#gene SGD:RPB8; MIPS:YOR224c !'##cross-references SGD:S0005750; MIPS:YOR224c !$#map_position 15R CLASSIFICATION #superfamily DNA-directed RNA polymerase chain RPB8 KEYWORDS DNA binding; nucleotidyltransferase; nucleus; transcription SUMMARY #length 146 #molecular-weight 16511 #checksum 3499 SEQUENCE /// ENTRY RNBY29 #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) II chain RPB9 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES DNA-directed RNA polymerase 14.5K chain; protein G3271; protein YGL070c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 21-Jul-2000 ACCESSIONS A41016; S19043; S64077 REFERENCE A41016 !$#authors Woychik, N.A.; Lane, W.S.; Young, R.A. !$#journal J. Biol. Chem. (1991) 266:19053-19055 !$#title Yeast RNA polymerase II subunit RPB9 is essential for growth !1at temperature extremes. !$#cross-references MUID:92011681; PMID:1918023 !$#accession A41016 !'##molecule_type DNA !'##residues 1-122 ##label WOY1 !'##cross-references GB:M73060; NID:g172469; PIDN:AAA34997.1; !1PID:g172470 !$#accession S19043 !'##molecule_type protein !'##residues 46-62 ##label WOY2 REFERENCE S64071 !$#authors Rieger, M.; Mueller-Auer, S.; Brueckner, M.; Schaefer, M. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64077 !'##molecule_type DNA !'##residues 1-122 ##label RIE !'##cross-references EMBL:Z72592; NID:g1322580; PIDN:CAA96774.1; !1PID:g1322581; GSPDB:GN00007; MIPS:YGL070c !'##experimental_source strain S288C GENETICS !$#gene SGD:RPB9; MIPS:YGL070c !'##cross-references SGD:S0003038; MIPS:YGL070c !$#map_position 7L CLASSIFICATION #superfamily DNA-directed RNA polymerase II chain RPB9 KEYWORDS nucleotidyltransferase; nucleus; transcription; zinc finger FEATURE !$7-32 #region zinc finger CCCC motif\ !$75-106 #region zinc finger CCCC motif SUMMARY #length 122 #molecular-weight 14288 #checksum 5274 SEQUENCE /// ENTRY S41621 #type complete TITLE DNA-directed RNA polymerase (EC 2.7.7.6) II 14.5K chain - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 24-Sep-1999 ACCESSIONS S41621 REFERENCE S41621 !$#authors Acker, J.; Wintzerith, M.; Vigneron, M.; Kedinger, C. !$#journal Nucleic Acids Res. (1993) 21:5345-5350 !$#title Structure of the gene encoding the 14.5 kDa subunit of human !1RNA polymerase II. !$#cross-references MUID:94089382; PMID:8265347 !$#accession S41621 !'##status preliminary !'##molecule_type DNA !'##residues 1-125 ##label ACK !'##cross-references EMBL:Z23102; NID:g397149; PIDN:CAA80649.1; !1PID:g397150 GENETICS !$#gene GDB:POLR2I !'##cross-references GDB:250749; OMIM:180662 !$#map_position 19q12-19q12 !$#introns 20/2; 38/3; 63/2; 88/2; 105/3 CLASSIFICATION #superfamily DNA-directed RNA polymerase II chain RPB9 KEYWORDS nucleotidyltransferase; nucleus; transcription SUMMARY #length 125 #molecular-weight 14523 #checksum 5231 SEQUENCE /// ENTRY JDVLVH #type fragment TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - hepatitis B virus (subtype adyw) (fragment) ORGANISM #formal_name hepatitis B virus, HBV DATE 18-Dec-1981 #sequence_revision 18-Dec-1981 #text_change 25-Oct-1996 ACCESSIONS A00701 REFERENCE A93217 !$#authors Pasek, M.; Goto, T.; Gilbert, W.; Zink, B.; Schaller, H.; !1MacKay, P.; Leadbetter, G.; Murray, K. !$#journal Nature (1979) 282:575-579 !$#title Hepatitis B virus genes and their expression in E. coli. !$#cross-references MUID:81012115; PMID:399329 !$#accession A00701 !'##molecule_type DNA !'##residues 1-750 ##label PAS CLASSIFICATION #superfamily hepatitis virus DNA-directed DNA polymerase KEYWORDS DNA biosynthesis; nucleotidyltransferase SUMMARY #length 750 #checksum 8293 SEQUENCE /// ENTRY S47406 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - hepatitis B virus (subtype ayw4) ORGANISM #formal_name hepatitis B virus, HBV #variety subtype ayw4 DATE 23-Nov-1994 #sequence_revision 22-Nov-1996 #text_change 11-Jun-1999 ACCESSIONS S47406 REFERENCE S47404 !$#authors Plucienniczak, A. !$#submission submitted to the EMBL Data Library, August 1994 !$#description Molecular cloning and sequencing of two complete genomes of !1polish isolates of human hepatitis B virus. !$#accession S47406 !'##molecule_type DNA !'##residues 1-832 ##label PLU !'##cross-references EMBL:Z35716; NID:g527435; PIDN:CAA84787.1; !1PID:g527438 !'##experimental_source subtype ayw4 GENETICS !$#gene P CLASSIFICATION #superfamily hepatitis virus DNA-directed DNA polymerase KEYWORDS DNA biosynthesis; nucleotidyltransferase SUMMARY #length 832 #molecular-weight 93707 #checksum 8702 SEQUENCE /// ENTRY JDVLVA #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - hepatitis B virus (subtype ayw) ORGANISM #formal_name hepatitis B virus, HBV #variety subtype ayw DATE 18-Dec-1981 #sequence_revision 18-Dec-1981 #text_change 11-Jun-1999 ACCESSIONS A00702; S20748; S53131 REFERENCE A93214 !$#authors Galibert, F.; Mandart, E.; Fitoussi, F.; Tiollais, P.; !1Charnay, P. !$#journal Nature (1979) 281:646-650 !$#title Nucleotide sequence of the hepatitis B virus genome (subtype !1ayw) in E. coli. !$#cross-references MUID:81012091; PMID:399327 !$#accession A00702 !'##molecule_type DNA !'##residues 1-832 ##label GAL !'##experimental_source cloned in Escherichia coli REFERENCE S20745 !$#authors Lai, M.E.; Mazzoleni, A.P.; Balestrieri, A.; Melis, A.; !1Porru, A. !$#submission submitted to the EMBL Data Library, March 1992 !$#description Sequence analysis of HBV genomes isolated from patients with !1HBsAg negative chronic liver disease. !$#accession S20748 !'##molecule_type DNA !'##residues 1-276,'S',278-292,'L',294-458,'H',460-465,'N',467-469,'S', !1471-612,'V',614-677,'G',679-697,'A',699-817,'L',819-832 !1##label LAI !'##cross-references EMBL:X65257; NID:g59429; PIDN:CAA46352.1; !1PID:g59433 !'##experimental_source subtype ayw, patient C REFERENCE S53112 !$#authors Lai, M.E.; Mazzoleni, A.P.; Porru, A.; Balestrieri, A. !$#submission submitted to the EMBL Data Library, March 1995 !$#accession S53131 !'##molecule_type DNA !'##residues 1-16,'D',18-117,'N',119-223,'C',225-245,'M',247-271,'Q', !1273-277,'D',279-291 ##label LA2 !'##cross-references EMBL:X85254 GENETICS !$#gene P CLASSIFICATION #superfamily hepatitis virus DNA-directed DNA polymerase KEYWORDS DNA biosynthesis; nucleotidyltransferase SUMMARY #length 832 #molecular-weight 93676 #checksum 7497 SEQUENCE /// ENTRY JDVLVB #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - hepatitis B virus (subtype ayw, strain pHB320) ORGANISM #formal_name hepatitis B virus, HBV #note host Homo sapiens (man) DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 28-Jul-2000 ACCESSIONS A00703 REFERENCE A05237 !$#authors Bichko, V.; Pushko, P.; Dreilina, D.; Pumpen, P.; Gren, E. !$#journal FEBS Lett. (1985) 185:208-212 !$#title Subtype ayw variant of hepatitis B virus: DNA primary !1structure analysis. !$#cross-references MUID:85204397; PMID:3996597 !$#accession A00703 !'##molecule_type DNA !'##residues 1-832 ##label BIC !'##cross-references GB:X02496; NID:g62280; PIDN:CAB41700.1; !1PID:g4704320 CLASSIFICATION #superfamily hepatitis virus DNA-directed DNA polymerase KEYWORDS DNA biosynthesis; nucleotidyltransferase SUMMARY #length 832 #molecular-weight 93838 #checksum 9500 SEQUENCE /// ENTRY JDVLA1 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - hepatitis B virus (strain alpha1) ORGANISM #formal_name hepatitis B virus, HBV DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 11-Jun-1999 ACCESSIONS C34773 REFERENCE A34773 !$#authors Tong, S.; Li, J.; Vitvitski, L.; Trepo, C. !$#journal Virology (1990) 176:596-603 !$#title Active hepatitis B virus replication in the presence of !1anti-HBe is associated with viral variants containing an !1inactive pre-C region. !$#cross-references MUID:90266476; PMID:2345966 !$#accession C34773 !'##status translation not shown !'##molecule_type DNA !'##residues 1-832 ##label TON !'##cross-references EMBL:M32138; NID:g329667; PIDN:AAA45503.1; !1PID:g329670 GENETICS !$#gene P CLASSIFICATION #superfamily hepatitis virus DNA-directed DNA polymerase KEYWORDS DNA biosynthesis; nucleotidyltransferase SUMMARY #length 832 #molecular-weight 93589 #checksum 8307 SEQUENCE /// ENTRY S20752 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - hepatitis B virus (subtype ayw, patient CI) ORGANISM #formal_name hepatitis B virus, HBV #variety subtype ayw, patient CI DATE 20-Feb-1995 #sequence_revision 22-Nov-1996 #text_change 11-Jun-1999 ACCESSIONS S20752 REFERENCE S20745 !$#authors Lai, M.E.; Mazzoleni, A.P.; Balestrieri, A.; Melis, A.; !1Porru, A. !$#submission submitted to the EMBL Data Library, March 1992 !$#description Sequence analysis of HBV genomes isolated from patients with !1HBsAg negative chronic liver disease. !$#accession S20752 !'##molecule_type DNA !'##residues 1-832 ##label LAI !'##cross-references EMBL:X65258; NID:g59434; PIDN:CAA46356.1; !1PID:g59438 !'##experimental_source subtype ayw, patient CI GENETICS !$#gene P CLASSIFICATION #superfamily hepatitis virus DNA-directed DNA polymerase KEYWORDS DNA biosynthesis; nucleotidyltransferase SUMMARY #length 832 #molecular-weight 93871 #checksum 1001 SEQUENCE /// ENTRY S20757 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - hepatitis B virus (subtype ayw, patient E) ORGANISM #formal_name hepatitis B virus, HBV #variety subtype ayw, patient E DATE 20-Feb-1995 #sequence_revision 22-Nov-1996 #text_change 11-Jun-1999 ACCESSIONS S20757 REFERENCE S20745 !$#authors Lai, M.E.; Mazzoleni, A.P.; Balestrieri, A.; Melis, A.; !1Porru, A. !$#submission submitted to the EMBL Data Library, March 1992 !$#description Sequence analysis of HBV genomes isolated from patients with !1HBsAg negative chronic liver disease. !$#accession S20757 !'##molecule_type DNA !'##residues 1-832 ##label LAI !'##cross-references EMBL:X65259; NID:g59439; PIDN:CAA46361.1; !1PID:g59444 !'##experimental_source subtype ayw, patient E GENETICS !$#gene P CLASSIFICATION #superfamily hepatitis virus DNA-directed DNA polymerase KEYWORDS DNA biosynthesis; nucleotidyltransferase SUMMARY #length 832 #molecular-weight 93793 #checksum 4355 SEQUENCE /// ENTRY JDVLVR #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - hepatitis B virus (subtype adr) ORGANISM #formal_name hepatitis B virus, HBV DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 25-Oct-1996 ACCESSIONS A00704 REFERENCE A93460 !$#authors Ono, Y.; Onda, H.; Sasada, R.; Igarashi, K.; Sugino, Y.; !1Nishioka, K. !$#journal Nucleic Acids Res. (1983) 11:1747-1757 !$#title The complete nucleotide sequences of the cloned hepatitis B !1virus DNA; subtype adr and adw. !$#cross-references MUID:83168919; PMID:6300776 !$#accession A00704 !'##molecule_type DNA !'##residues 1-843 ##label ONO CLASSIFICATION #superfamily hepatitis virus DNA-directed DNA polymerase KEYWORDS DNA biosynthesis; nucleotidyltransferase SUMMARY #length 843 #molecular-weight 94400 #checksum 3044 SEQUENCE /// ENTRY JDVLVS #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - hepatitis B virus (subtype adr, mutant) ORGANISM #formal_name hepatitis B virus, HBV DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 25-Oct-1996 ACCESSIONS S04568 REFERENCE S04568 !$#authors Rho, H.M.; Kim, K.; Hyun, S.W.; Kim, Y.S. !$#journal Nucleic Acids Res. (1989) 17:2124 !$#title The nucleotide sequence and reading frames of a mutant !1hepatitis B virus subtype adr. !$#cross-references MUID:89183619; PMID:2928116 !$#accession S04568 !'##status translation not shown !'##molecule_type DNA !'##residues 1-842 ##label RHO !'##cross-references EMBL:X14193 CLASSIFICATION #superfamily hepatitis virus DNA-directed DNA polymerase KEYWORDS DNA biosynthesis; nucleotidyltransferase SUMMARY #length 842 #molecular-weight 94545 #checksum 8738 SEQUENCE /// ENTRY S43491 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - hepatitis B virus (subtype adr) ORGANISM #formal_name hepatitis B virus, HBV #variety subtype adr DATE 07-Sep-1994 #sequence_revision 22-Nov-1996 #text_change 11-Jun-1999 ACCESSIONS S43491 REFERENCE S12598 !$#authors Loncarevic, I.F.; Zentgraf, H.; Schroeder, C.H. !$#journal Nucleic Acids Res. (1990) 18:4940 !$#title Sequence of a replication competent hepatitis B virus genome !1with a preX open reading frame. !$#cross-references MUID:90370503; PMID:2395664 !$#accession S43491 !'##status translation not shown !'##molecule_type DNA !'##residues 1-843 ##label LON !'##cross-references EMBL:X52939; NID:g457780; PIDN:CAA37113.1; !1PID:g457782 !'##experimental_source subtype adr GENETICS !$#gene P; pol CLASSIFICATION #superfamily hepatitis virus DNA-directed DNA polymerase KEYWORDS DNA biosynthesis; nucleotidyltransferase SUMMARY #length 843 #molecular-weight 94518 #checksum 1375 SEQUENCE /// ENTRY JDVLJ1 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - hepatitis B virus (subtype adw, strain Japan/pJDW233) ORGANISM #formal_name hepatitis B virus, HBV DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 14-Nov-1997 ACCESSIONS D28925 REFERENCE JS0253 !$#authors Okamoto, H.; Tsuda, F.; Sakugawa, H.; Sastrosoewignjo, R.I.; !1Imai, M.; Miyakawa, Y.; Mayumi, M. !$#journal J. Gen. Virol. (1988) 69:2575-2583 !$#title Typing hepatitis B virus by homology in nucleotide sequence: !1comparison of surface antigen subtypes. !$#cross-references MUID:89010694; PMID:3171552 !$#accession D28925 !'##molecule_type DNA !'##residues 1-843 ##label OKA !'##cross-references GB:D00329; NID:g221497 CLASSIFICATION #superfamily hepatitis virus DNA-directed DNA polymerase KEYWORDS DNA biosynthesis; nucleotidyltransferase SUMMARY #length 843 #molecular-weight 94218 #checksum 4517 SEQUENCE /// ENTRY JDVLJ2 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - hepatitis B virus (subtype adw, strain Okinawa/pODW282) ORGANISM #formal_name hepatitis B virus, HBV DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 14-Nov-1997 ACCESSIONS E28925 REFERENCE JS0253 !$#authors Okamoto, H.; Tsuda, F.; Sakugawa, H.; Sastrosoewignjo, R.I.; !1Imai, M.; Miyakawa, Y.; Mayumi, M. !$#journal J. Gen. Virol. (1988) 69:2575-2583 !$#title Typing hepatitis B virus by homology in nucleotide sequence: !1comparison of surface antigen subtypes. !$#cross-references MUID:89010694; PMID:3171552 !$#accession E28925 !'##molecule_type DNA !'##residues 1-843 ##label OKA !'##cross-references GB:D00330; NID:g221498 CLASSIFICATION #superfamily hepatitis virus DNA-directed DNA polymerase KEYWORDS DNA biosynthesis; nucleotidyltransferase SUMMARY #length 843 #molecular-weight 94641 #checksum 4186 SEQUENCE /// ENTRY JDVLJ3 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - hepatitis B virus (subtype adw, strain Indonesia/pIDW420) ORGANISM #formal_name hepatitis B virus, HBV DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 14-Nov-1997 ACCESSIONS F28925 REFERENCE JS0253 !$#authors Okamoto, H.; Tsuda, F.; Sakugawa, H.; Sastrosoewignjo, R.I.; !1Imai, M.; Miyakawa, Y.; Mayumi, M. !$#journal J. Gen. Virol. (1988) 69:2575-2583 !$#title Typing hepatitis B virus by homology in nucleotide sequence: !1comparison of surface antigen subtypes. !$#cross-references MUID:89010694; PMID:3171552 !$#accession F28925 !'##molecule_type DNA !'##residues 1-843 ##label OKA !'##cross-references GB:D00331; NID:g221499 CLASSIFICATION #superfamily hepatitis virus DNA-directed DNA polymerase KEYWORDS DNA biosynthesis; nucleotidyltransferase SUMMARY #length 843 #molecular-weight 94394 #checksum 4575 SEQUENCE /// ENTRY JDVLVD #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - hepatitis B virus (subtype adw2) ORGANISM #formal_name hepatitis B virus, HBV #variety subtype adw2 DATE 18-Dec-1981 #sequence_revision 14-Nov-1983 #text_change 11-Jun-1999 ACCESSIONS A94409; B93212; S47410; A00705; A00706 REFERENCE A94409 !$#authors Valenzuela, P.; Quiroga, M.; Zaldivar, J.; Gray, P.; Rutter, !1W.J. !$#book Animal Virus Genetics, Field, B.N., Jaenisch, R., and Fox, !1C.F., eds., pp.57-70, Academic Press, New York, 1980 !$#contents Dane particles !$#accession A94409 !'##molecule_type DNA !'##residues 1-845 ##label VAL REFERENCE A93212 !$#authors Valenzuela, P.; Gray, P.; Quiroga, M.; Zaldivar, J.; !1Goodman, H.M.; Rutter, W.J. !$#journal Nature (1979) 280:815-819 !$#title Nucleotide sequence of the gene coding for the major protein !1of hepatitis B virus surface antigen. !$#cross-references MUID:79244739; PMID:471053 !$#contents Dane particles !$#accession B93212 !'##molecule_type DNA !'##residues 315-611 ##label VAL2 REFERENCE S47404 !$#authors Plucienniczak, A. !$#submission submitted to the EMBL Data Library, August 1994 !$#description Molecular cloning and sequencing of two complete genomes of !1polish isolates of human hepatitis B virus. !$#accession S47410 !'##molecule_type DNA !'##residues 1-35,'N',37-202,'P',204-229,'H',231-232,'P',234-239,'G', !1241-247,'R',249-311,'S',313-322,'F',324-401,'T',403-450,'V', !1452-845 ##label PLU !'##cross-references EMBL:Z35717; NID:g527440; PIDN:CAA84791.1; !1PID:g527443 !'##experimental_source subtype adw2 REFERENCE A93460 !$#authors Ono, Y.; Onda, H.; Sasada, R.; Igarashi, K.; Sugino, Y.; !1Nishioka, K. !$#journal Nucleic Acids Res. (1983) 11:1747-1757 !$#title The complete nucleotide sequences of the cloned hepatitis B !1virus DNA; subtype adr and adw. !$#cross-references MUID:83168919; PMID:6300776 !$#accession A00705 !'##status translation not shown !'##molecule_type DNA !'##residues 1-35,'N',37-183,191-202,'P',204-206,'P',208-220,'NK', !1223-229,'H',231-232,'P',234-239,'G',241-247,'R',249-309,'A', !1311,'S',313-355,'D',357-401,'T',403-488 ##label ONO !'##experimental_source subtype adw !'##note polymerase gene contains a stop codon corresponding to residue !1489; it is not known if this genome can replicate GENETICS !$#gene P CLASSIFICATION #superfamily hepatitis virus DNA-directed DNA polymerase KEYWORDS DNA biosynthesis; nucleotidyltransferase SUMMARY #length 845 #molecular-weight 94799 #checksum 2391 SEQUENCE /// ENTRY JDVLKS #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - hepatitis B virus (subtype adw, strain 991) ORGANISM #formal_name hepatitis B virus, HBV DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 11-Jun-1999 ACCESSIONS S10382 REFERENCE S10380 !$#authors Koechel, H.G.; Schueler, A.; Lottmann, S.; Thomssen, R. !$#submission submitted to the EMBL Data Library, February 1990 !$#accession S10382 !'##molecule_type DNA !'##residues 1-845 ##label KOE !'##cross-references EMBL:X51970; NID:g1155012; PIDN:CAA36229.1; !1PID:g908856 GENETICS !$#gene P CLASSIFICATION #superfamily hepatitis virus DNA-directed DNA polymerase KEYWORDS DNA biosynthesis; nucleotidyltransferase SUMMARY #length 845 #molecular-weight 94767 #checksum 2244 SEQUENCE /// ENTRY JDVLCP #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - hepatitis B virus (strain LSH, chimpanzee) ORGANISM #formal_name hepatitis B virus, HBV DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jun-2000 ACCESSIONS B28885 REFERENCE A92796 !$#authors Vaudin, M.; Wolstenholme, A.J.; Tsiquaye, K.N.; Zuckerman, !1A.J.; Harrison, T.J. !$#journal J. Gen. Virol. (1988) 69:1383-1389 !$#title The complete nucleotide sequence of the genome of a !1hepatitis B virus isolated from a naturally infected !1chimpanzee. !$#cross-references MUID:88258473; PMID:2838576 !$#accession B28885 !'##molecule_type DNA !'##residues 1-832 ##label VAU !'##cross-references GB:D00220; NID:g221505; PIDN:BAA00158.1; !1PID:g221507 !'##note the authors translated the codon GAA for residue 161 as Gln, !1GGA for residue 219 as Gln, GCA for residue 269 as Val, TCA !1for residue 403 as Pro, ACT for residue 519 as Tyr, CTT for !1residue 552 as His, ATC for residue 604 as Thr, and GAA for !1residue 718 as Gln CLASSIFICATION #superfamily hepatitis virus DNA-directed DNA polymerase KEYWORDS DNA biosynthesis; nucleotidyltransferase SUMMARY #length 832 #molecular-weight 93317 #checksum 1910 SEQUENCE /// ENTRY JQ2229 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - hepatitis B virus (subtype adw4) ORGANISM #formal_name hepatitis B virus, HBV DATE 19-May-1994 #sequence_revision 22-Nov-1996 #text_change 11-Jun-1999 ACCESSIONS JQ2229; S31797 REFERENCE JQ2225 !$#authors Naumann, H.; Schaefer, S.; Yoshida, C.F.T.; Gaspar, A.M.C.; !1Repp, R.; Gerlich, W.H. !$#journal J. Gen. Virol. (1993) 74:1627-1632 !$#title Identification of a new hepatitis B virus (HBV) genotype !1from Brazil that expresses HBV surface antigen subtype adw4. !$#cross-references MUID:93346970; PMID:8345355 !$#accession JQ2229 !'##molecule_type DNA !'##residues 1-843 ##label NAU !'##cross-references EMBL:X69798; NID:g59422; PIDN:CAA49456.1; !1PID:g59427 GENETICS !$#gene P; pol CLASSIFICATION #superfamily hepatitis virus DNA-directed DNA polymerase KEYWORDS DNA biosynthesis; nucleotidyltransferase SUMMARY #length 843 #molecular-weight 94257 #checksum 9551 SEQUENCE /// ENTRY JDVLC #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - woodchuck hepatitis virus (clone 1) ORGANISM #formal_name woodchuck hepatitis virus DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 11-Jun-1999 ACCESSIONS A00707 REFERENCE A92986 !$#authors Galibert, F.; Chen, T.N.; Mandart, E. !$#journal J. Virol. (1982) 41:51-65 !$#title Nucleotide sequence of a cloned woodchuck hepatitis virus !1genome: comparison with the hepatitis B virus sequence. !$#cross-references MUID:82216969; PMID:7086958 !$#accession A00707 !'##molecule_type DNA !'##residues 1-879 ##label GAL !'##cross-references GB:J02442; NID:g336126; PIDN:AAA46759.1; !1PID:g336127 CLASSIFICATION #superfamily hepatitis virus DNA-directed DNA polymerase KEYWORDS DNA biosynthesis; nucleotidyltransferase SUMMARY #length 879 #molecular-weight 99185 #checksum 8623 SEQUENCE /// ENTRY JDVLC2 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - woodchuck hepatitis virus (clone 2) ORGANISM #formal_name woodchuck hepatitis virus DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 11-Jun-1999 ACCESSIONS A00708 REFERENCE A93015 !$#authors Kodama, K.; Ogasawara, N.; Yoshikawa, H.; Murakami, S. !$#journal J. Virol. (1985) 56:978-986 !$#title Nucleotide sequence of a cloned woodchuck hepatitis virus !1genome: evolutional relationship between hepadnaviruses. !$#cross-references MUID:86062931; PMID:3855246 !$#accession A00708 !'##molecule_type DNA !'##residues 1-883 ##label KOD !'##cross-references GB:M11082; NID:g336132; PIDN:AAA19183.1; !1PID:g336134 CLASSIFICATION #superfamily hepatitis virus DNA-directed DNA polymerase KEYWORDS DNA biosynthesis; nucleotidyltransferase SUMMARY #length 883 #molecular-weight 99346 #checksum 593 SEQUENCE /// ENTRY JDVL7 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - woodchuck hepatitis virus (clone 7) ORGANISM #formal_name woodchuck hepatitis virus DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 11-Jun-1999 ACCESSIONS C29969 REFERENCE A94368 !$#authors Cohen, J.I.; Miller, R.H.; Rosenblum, B.; Denniston, K.; !1Gerin, J.L.; Purcell, R.H. !$#journal Virology (1988) 162:12-20 !$#title Sequence comparison of woodchuck hepatitis virus replicative !1forms shows conservation of the genome. !$#cross-references MUID:88101359; PMID:3336938 !$#accession C29969 !'##molecule_type DNA !'##residues 1-884 ##label COH !'##cross-references GB:M18752; NID:g336136; PIDN:AAA46767.1; !1PID:g336138 CLASSIFICATION #superfamily hepatitis virus DNA-directed DNA polymerase KEYWORDS DNA biosynthesis; nucleotidyltransferase SUMMARY #length 884 #molecular-weight 99732 #checksum 4231 SEQUENCE /// ENTRY JDVLW8 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - woodchuck hepatitis virus (clone 8) ORGANISM #formal_name woodchuck hepatitis virus DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 12-Jun-1998 ACCESSIONS A32397 REFERENCE A94222 !$#authors Girones, R.; Cote, P.J.; Hornbuckle, W.E.; Tennant, B.C.; !1Gerin, J.L.; Purcell, R.H.; Miller, R.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:1846-1849 !$#title Complete nucleotide sequence of a molecular clone of !1woodchuck hepatitis virus that is infectious in the natural !1host. !$#cross-references MUID:89184524; PMID:2928306 !$#accession A32397 !'##molecule_type DNA !'##residues 1-884 ##label GIR !'##cross-references GB:J04514; NID:g336146 !'##note this ORF is not annotated in GenBank entry OHVHEPBA, release !1106 GENETICS !$#gene P CLASSIFICATION #superfamily hepatitis virus DNA-directed DNA polymerase KEYWORDS DNA biosynthesis; nucleotidyltransferase SUMMARY #length 884 #molecular-weight 99708 #checksum 2527 SEQUENCE /// ENTRY JDVL59 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - woodchuck hepatitis virus (clone 59) ORGANISM #formal_name woodchuck hepatitis virus DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 11-Jun-1999 ACCESSIONS G29969 REFERENCE A94368 !$#authors Cohen, J.I.; Miller, R.H.; Rosenblum, B.; Denniston, K.; !1Gerin, J.L.; Purcell, R.H. !$#journal Virology (1988) 162:12-20 !$#title Sequence comparison of woodchuck hepatitis virus replicative !1forms shows conservation of the genome. !$#cross-references MUID:88101359; PMID:3336938 !$#accession G29969 !'##molecule_type DNA !'##residues 1-884 ##label COH !'##cross-references GB:M19183; NID:g336141; PIDN:AAA46763.1; !1PID:g336143 CLASSIFICATION #superfamily hepatitis virus DNA-directed DNA polymerase KEYWORDS DNA biosynthesis; nucleotidyltransferase SUMMARY #length 884 #molecular-weight 99399 #checksum 3128 SEQUENCE /// ENTRY JDVL64 #type fragment TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - woodchuck hepatitis virus (clone 64) (fragment) ORGANISM #formal_name woodchuck hepatitis virus DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 11-Jun-1999 ACCESSIONS A29498 REFERENCE A91568 !$#authors Etiemble, J.; Moeroey, T.; Trepo, C.; Tiollais, P.; Buendia, !1M.A. !$#journal Gene (1986) 50:207-214 !$#title Nucleotide sequence of the woodchuck hepatitis virus surface !1antigen mRNAs and the variability of three overlapping viral !1genes. !$#cross-references MUID:87219879; PMID:3582979 !$#accession A29498 !'##molecule_type mRNA !'##residues 1-556 ##label ETI !'##cross-references GB:M15954; NID:g893289; PIDN:AAA69573.1; !1PID:g336155 GENETICS !$#gene P CLASSIFICATION #superfamily hepatitis virus DNA-directed DNA polymerase KEYWORDS DNA biosynthesis; nucleotidyltransferase SUMMARY #length 556 #checksum 3238 SEQUENCE /// ENTRY JDVLS #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - ground squirrel hepatitis virus ORGANISM #formal_name ground squirrel hepatitis virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 11-Jun-1999 ACCESSIONS A00709 REFERENCE A93000 !$#authors Seeger, C.; Ganem, D.; Varmus, H.E. !$#journal J. Virol. (1984) 51:367-375 !$#title Nucleotide sequence of an infectious molecularly cloned !1genome of ground squirrel hepatitis virus. !$#cross-references MUID:84267998; PMID:6086950 !$#accession A00709 !'##molecule_type DNA !'##residues 1-881 ##label SEE !'##cross-references GB:K02715; NID:g325400; PIDN:AAA46756.1; !1PID:g325402 CLASSIFICATION #superfamily hepatitis virus DNA-directed DNA polymerase KEYWORDS DNA biosynthesis; nucleotidyltransferase SUMMARY #length 881 #molecular-weight 99976 #checksum 6194 SEQUENCE /// ENTRY JDVLD #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - duck hepatitis virus ORGANISM #formal_name duck hepatitis virus, DHBV DATE 20-Sep-1984 #sequence_revision 08-Nov-1996 #text_change 11-Jun-1999 ACCESSIONS S12844; S36614; A00710 REFERENCE S12843 !$#authors Mattes, F.; Tong, S.; Teubner, K.; Blum, H.E. !$#journal Nucleic Acids Res. (1990) 18:6140 !$#title Complete nucleotide sequence of a German duck hepatitis B !1virus. !$#cross-references MUID:91045092; PMID:2235507 !$#accession S12844 !'##status translation not shown !'##molecule_type DNA !'##residues 1-836 ##label MAT !'##cross-references EMBL:X12798; NID:g59057 !'##experimental_source isolate DHBV F1-6 !'##note this ORF is not annotated in GenBank entry DHBVF16, release 103 REFERENCE S36614 !$#authors Munshi, A.; Panda, S.K. !$#submission submitted to the EMBL Data Library, August 1993 !$#description Cloning sequencing and sequence comparison of the indian !1isolate. !$#accession S36614 !'##molecule_type DNA !'##residues 1-35,'V',37-81,'I',83-115,'Y',117-176,'Y',178-184,'T', !1186-188,'Y',190-220,'FN',223-284,'R',286-306,'V',308-551, !1'P',553-655,'A',657-836 ##label MUN !'##cross-references EMBL:X74623; NID:g397342; PIDN:CAA52700.1; !1PID:g397344 !'##experimental_source isolate IDHBV REFERENCE A92997 !$#authors Mandart, E.; Kay, A.; Galibert, F. !$#journal J. Virol. (1984) 49:782-792 !$#title Nucleotide sequence of a cloned duck hepatitis B virus !1genome: comparison with woodchuck and human hepatitis B !1virus sequences. !$#cross-references MUID:84138772; PMID:6699938 !$#accession A00710 !'##molecule_type DNA !'##residues 390-734,'A',736-836 ##label MAN !'##cross-references GB:K01834 !'##note only part of the sequence reported in the GenBank entry is !1shown in the published paper CLASSIFICATION #superfamily hepatitis virus DNA-directed DNA polymerase KEYWORDS DNA biosynthesis; nucleotidyltransferase SUMMARY #length 836 #molecular-weight 95321 #checksum 297 SEQUENCE /// ENTRY JDVLBD #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - duck hepatitis virus (strain S5) ORGANISM #formal_name duck hepatitis virus, DHBV #note host (Shanghai brown duck) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 11-Jun-1999 ACCESSIONS A33746 REFERENCE A33746 !$#authors Uchida, M.; Esumi, M.; Shikata, T. !$#journal Virology (1989) 173:600-606 !$#title Molecular cloning and sequence analysis of duck hepatitis B !1virus genomes of a new variant isolated from Shanghai ducks. !$#cross-references MUID:90085807; PMID:2596031 !$#accession A33746 !'##status translation not shown !'##molecule_type DNA !'##residues 1-788 ##label UCH !'##cross-references GB:M32990; NID:g325448; PIDN:AAA45754.1; !1PID:g325450 CLASSIFICATION #superfamily hepatitis virus DNA-directed DNA polymerase KEYWORDS DNA biosynthesis; nucleotidyltransferase SUMMARY #length 788 #molecular-weight 89378 #checksum 9039 SEQUENCE /// ENTRY JDVLWD #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - duck hepatitis virus (strain S31) ORGANISM #formal_name duck hepatitis virus, DHBV #note host (Shanghai white duck) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 11-Jun-1999 ACCESSIONS B33746 REFERENCE A33746 !$#authors Uchida, M.; Esumi, M.; Shikata, T. !$#journal Virology (1989) 173:600-606 !$#title Molecular cloning and sequence analysis of duck hepatitis B !1virus genomes of a new variant isolated from Shanghai ducks. !$#cross-references MUID:90085807; PMID:2596031 !$#accession B33746 !'##status translation not shown !'##molecule_type DNA !'##residues 1-788 ##label UCH !'##cross-references GB:M32991; NID:g325444; PIDN:AAA45751.1; !1PID:g325446 CLASSIFICATION #superfamily hepatitis virus DNA-directed DNA polymerase KEYWORDS DNA biosynthesis; nucleotidyltransferase SUMMARY #length 788 #molecular-weight 89264 #checksum 460 SEQUENCE /// ENTRY JDVLW2 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - duck hepatitis virus (Chinese isolate) ORGANISM #formal_name duck hepatitis virus, DHBV DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 11-Jun-1999 ACCESSIONS S12841 REFERENCE S12840 !$#authors Tong, S.; Mattes, F.; Teubner, K.; Blum, H.E. !$#journal Nucleic Acids Res. (1990) 18:6139 !$#title Complete nucleotide sequence of a Chinese duck hepatitis B !1virus. !$#cross-references MUID:91045091; PMID:2235506 !$#accession S12841 !'##status translation not shown !'##molecule_type DNA !'##residues 1-787 ##label TON !'##cross-references GB:M21953; NID:g325435; PIDN:AAA45745.1; !1PID:g325437 CLASSIFICATION #superfamily hepatitis virus DNA-directed DNA polymerase KEYWORDS DNA biosynthesis; nucleotidyltransferase SUMMARY #length 787 #molecular-weight 89214 #checksum 5230 SEQUENCE /// ENTRY JDVLHH #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - heron hepatitis virus ORGANISM #formal_name heron hepatitis virus, HHBV #note host Ardea cinerea (gray heron) DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 11-Jun-1999 ACCESSIONS A30082 REFERENCE A93037 !$#authors Sprengel, R.; Kaleta, E.F.; Will, H. !$#journal J. Virol. (1988) 62:3832-3839 !$#title Isolation and characterization of a hepatitis B virus !1endemic in herons. !$#cross-references MUID:88333160; PMID:3418788 !$#accession A30082 !'##molecule_type DNA !'##residues 1-788 ##label SPR !'##cross-references GB:M22056; NID:g325452; PIDN:AAA45738.1; !1PID:g325454 CLASSIFICATION #superfamily hepatitis virus DNA-directed DNA polymerase KEYWORDS DNA biosynthesis; nucleotidyltransferase SUMMARY #length 788 #molecular-weight 90070 #checksum 8976 SEQUENCE /// ENTRY S34120 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - Sulfolobus solfataricus ORGANISM #formal_name Sulfolobus solfataricus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S34120 REFERENCE S34120 !$#authors Prangishvili, D.; Klenk, H.P. !$#journal Nucleic Acids Res. (1993) 21:2768 !$#title Nucleotide sequence of the gene for a 74 kDa DNA polymerase !1from the archaeon Sulfolobus solfataricus. !$#cross-references MUID:93324346; PMID:8332474 !$#accession S34120 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-626 ##label PRA !'##cross-references EMBL:X71597; NID:g311954; PIDN:CAA50600.1; !1PID:g311955 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1993 CLASSIFICATION #superfamily Sulfolobus DNA-directed DNA polymerase KEYWORDS nucleotidyltransferase SUMMARY #length 626 #molecular-weight 73531 #checksum 6474 SEQUENCE /// ENTRY DJBEI1 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - ictalurid herpesvirus 1 (strain auburn 1) ORGANISM #formal_name ictalurid herpesvirus 1 #note host Ictalurus punctatus (channel catfish) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 11-Jun-1999 ACCESSIONS D36792 REFERENCE A36804 !$#authors Davison, A.J. !$#submission submitted to GenBank, January 1992 !$#description Channel catfish virus: a new type of herpesvirus. !$#accession D36792 !'##molecule_type DNA !'##residues 1-985 ##label DAV !'##cross-references GB:M75136; NID:g331209; PIDN:AAA88160.1; !1PID:g331267 REFERENCE A39447 !$#authors Davison, A.J. !$#journal Virology (1992) 186:9-14 !$#title Channel catfish virus: a new type of herpesvirus. !$#cross-references MUID:92087490; PMID:1727613 !$#contents annotation !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 57 CLASSIFICATION #superfamily ictalurid herpesvirus DNA-directed DNA !1polymerase KEYWORDS DNA replication; nucleotidyltransferase SUMMARY #length 985 #molecular-weight 113468 #checksum 1895 SEQUENCE /// ENTRY WMAD12 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - human adenovirus 2 ORGANISM #formal_name Mastadenovirus h2 #common_name human adenovirus 2 #note host Homo sapiens (man) DATE 05-Apr-1983 #sequence_revision 05-Apr-1983 #text_change 16-Feb-1997 ACCESSIONS A92351; A92352; A00711 REFERENCE A92351 !$#authors Gingeras, T.R.; Sciaky, D.; Gelinas, R.E.; Bing-Dong, J.; !1Yen, C.E.; Kelly, M.M.; Bullock, P.A.; Parsons, B.L.; !1O'Neill, K.E.; Roberts, R.J. !$#journal J. Biol. Chem. (1982) 257:13475-13491 !$#title Nucleotide sequences from the adenovirus-2 genome. !$#cross-references MUID:83056843; PMID:7142161 !$#accession A92351 !'##molecule_type DNA !'##residues 1-1056 ##label GIN REFERENCE A92352 !$#authors Alestrom, P.; Akusjarvi, G.; Pettersson, M.; Pettersson, U. !$#journal J. Biol. Chem. (1982) 257:13492-13498 !$#title DNA sequence analysis of the region encoding the terminal !1protein and the hypothetical N-gene product of adenovirus !1type 2. !$#cross-references MUID:83056844; PMID:7142162 !$#accession A92352 !'##molecule_type DNA !'##residues 1-1056 ##label ALE CLASSIFICATION #superfamily adenovirus DNA-directed DNA polymerase KEYWORDS DNA binding; DNA replication; nucleotidyltransferase SUMMARY #length 1056 #molecular-weight 120431 #checksum 6480 SEQUENCE /// ENTRY DJAD51 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - human adenovirus 5 ORGANISM #formal_name Mastadenovirus h5 #common_name human adenovirus 5 #note host Homo sapiens (man) DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 11-Jun-1999 ACCESSIONS A00712 REFERENCE A91508 !$#authors Dekker, B.M.M.; van Ormondt, H. !$#journal Gene (1984) 27:115-120 !$#title The nucleotide sequence of fragment HindIII-C of human !1adenovirus type 5 DNA (map positions 17.1-31.7). !$#cross-references MUID:84183604; PMID:6325298 !$#accession A00712 !'##molecule_type DNA !'##residues 1-1056 ##label DEK !'##cross-references EMBL:X02996; NID:g58484; PIDN:CAA26749.1; !1PID:g58495 CLASSIFICATION #superfamily adenovirus DNA-directed DNA polymerase KEYWORDS DNA binding; DNA replication; nucleotidyltransferase SUMMARY #length 1056 #molecular-weight 120399 #checksum 6627 SEQUENCE /// ENTRY DJAD12 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - human adenovirus 12 ORGANISM #formal_name Mastadenovirus h12 #common_name human adenovirus 12 DATE 30-Jun-1989 #sequence_revision 17-May-1996 #text_change 11-Jun-1999 ACCESSIONS S33933; A25770 REFERENCE S33928 !$#authors Sprengel, J. !$#submission submitted to the EMBL Data Library, June 1993 !$#accession S33933 !'##molecule_type DNA !'##residues 1-1061 ##label SPR !'##cross-references EMBL:X73487; NID:g313361; PIDN:CAA51882.1; !1PID:g313367 REFERENCE A91557 !$#authors Shu, L.; Hong, J.S.; Wei, Y.F.; Engler, J.A. !$#journal Gene (1986) 46:187-195 !$#title Nucleotide sequence of the genes encoded in early region 2b !1of human adenovirus type 12. !$#cross-references MUID:87106854; PMID:3803925 !$#accession A25770 !'##molecule_type DNA !'##residues 9-31,'S',33-161,'L',163-180,'YN',183-460,'T',462-574,'F', !1576-891,'T',893-1029,'M',1031-1061 ##label SHU COMMENT This gene is located on the E2B region of the genome. CLASSIFICATION #superfamily adenovirus DNA-directed DNA polymerase KEYWORDS DNA binding; DNA replication; early protein; !1nucleotidyltransferase SUMMARY #length 1061 #molecular-weight 121726 #checksum 856 SEQUENCE /// ENTRY DJHUAC #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) alpha catalytic chain - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 11-Jun-1999 ACCESSIONS S00257; A30440; I57513; S12665 REFERENCE S00257 !$#authors Wong, S.W.; Wahl, A.F.; Yuan, P.M.; Arai, N.; Pearson, B.E.; !1Arai, K.I.; Korn, D.; Hunkapiller, M.W.; Wang, T.S.F. !$#journal EMBO J. (1988) 7:37-47 !$#title Human DNA polymerase alpha gene expression is cell !1proliferation dependent and its primary structure is similar !1to both prokaryotic and eukaryotic replicative DNA !1polymerases. !$#cross-references MUID:88196090; PMID:3359994 !$#accession S00257 !'##molecule_type mRNA !'##residues 1-1462 ##label WON !'##cross-references EMBL:X06745; NID:g35567; PIDN:CAA29920.1; !1PID:g35568 !$#accession A30440 !'##molecule_type protein !'##residues 438-449;495-502;'G', !1838-848;1090-1105;1201-1216;1397-1407;1444-1453 ##label WON2 REFERENCE I57513 !$#authors Pearson, B.E.; Nasheuer, H.P.; Wang, T.S. !$#journal Mol. Cell. Biol. (1991) 11:2081-2095 !$#title Human DNA polymerase alpha gene: sequences controlling !1expression in cycling and serum-stimulated cells. !$#cross-references MUID:91172197; PMID:2005899 !$#accession I57513 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-8 ##label RES !'##cross-references GB:M64481; NID:g181617; PIDN:AAA52318.1; !1PID:g181618 REFERENCE S12665 !$#authors Hsi, K.L.; Copeland, W.C.; Wang, T.S.F. !$#journal Nucleic Acids Res. (1990) 18:6231-6237 !$#title Human DNA polymerase alpha catalytic polypeptide binds ConA !1and RCA and contains a specific labile site in the !1N-terminus. !$#cross-references MUID:91057099; PMID:2243771 !$#accession S12665 !'##molecule_type protein !'##residues 19-37,'C';1406-1425,'C' ##label HSI GENETICS !$#gene GDB:POLA !'##cross-references GDB:120304; OMIM:312040 !$#map_position Xp22.3-Xp21.1 CLASSIFICATION #superfamily herpesvirus DNA-directed DNA polymerase KEYWORDS DNA binding; DNA replication; nucleotidyltransferase; zinc !1finger FEATURE !$654-691 #region zinc finger CHCC motif\ !$1249-1374 #region zinc fingers SUMMARY #length 1462 #molecular-weight 165859 #checksum 2769 SEQUENCE /// ENTRY S20052 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) alpha catalytic chain - Trypanosoma brucei brucei ORGANISM #formal_name Trypanosoma brucei brucei DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S20052; S15729 REFERENCE S20051 !$#authors Leegwater, P.A.J.; Strating, M.; Murphy, N.B.; Kooy, R.F.; !1van der Vliet, P.C.; Overdulve, J.P. !$#journal Nucleic Acids Res. (1991) 19:6441-6447 !$#title The Trypanosoma brucei DNA polymerase alpha core subunit !1gene is developmentally regulated and linked to a !1constitutively expressed open reading frame. !$#cross-references MUID:92093600; PMID:1754381 !$#accession S20052 !'##molecule_type DNA !'##residues 1-1339 ##label LEE !'##cross-references EMBL:X60951; NID:g10499; PIDN:CAA43287.1; !1PID:g10501 !'##note 828-Arg was also found GENETICS !$#gene pola CLASSIFICATION #superfamily herpesvirus DNA-directed DNA polymerase KEYWORDS DNA binding; DNA replication; nucleotidyltransferase; !1nucleus; zinc finger SUMMARY #length 1339 #molecular-weight 151611 #checksum 2668 SEQUENCE /// ENTRY DJZPA #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) alpha - fission yeast (Schizosaccharomyces pombe) ORGANISM #formal_name Schizosaccharomyces pombe DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 10-Dec-1999 ACCESSIONS S15993; T38752; S21818 REFERENCE S15993 !$#authors Damagnez, V.; Tillit, J.; de Recondo, A.M.; Baldacci, G. !$#journal Mol. Gen. Genet. (1991) 226:182-189 !$#title The POL1 gene from the fission yeast, Schizosaccharomyces !1pombe, shows conserved amino acid blocks specific for !1eukaryotic DNA polymerases alpha. !$#cross-references MUID:91238692; PMID:2034212 !$#accession S15993 !'##molecule_type DNA !'##residues 1-1405 ##label MOL !'##cross-references EMBL:X58299; NID:g5008; PIDN:CAA41232.1; PID:g5009 REFERENCE Z21809 !$#authors Oliver, K.; Harris, D.; Wood, V.; Barrell, B.G.; Rajandream, !1M.A. !$#submission submitted to the EMBL Data Library, September 1996 !$#accession T38752 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-1405 ##label OLI !'##cross-references EMBL:Z99296; PIDN:CAB16598.1; GSPDB:GN00066; !1SPDB:SPAC3H5.06c !'##experimental_source strain 972h-; cosmid c3H5 GENETICS MOL1 !$#gene POL1 !$#map_position II GENETICS OLI2 !$#gene SPAC3H5.06c !$#map_position 1 !$#introns 101/1 CLASSIFICATION #superfamily herpesvirus DNA-directed DNA polymerase KEYWORDS DNA binding; DNA replication; nucleotidyltransferase; zinc !1finger FEATURE !$1316-1340 #region zinc finger CCCC motif SUMMARY #length 1405 #molecular-weight 159348 #checksum 4841 SEQUENCE /// ENTRY RNBYL3 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) III large chain - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES DNA-directed DNA polymerase delta large chain; protein D2366; protein YDL102w ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1991 #sequence_revision 23-Aug-1996 #text_change 16-Jun-2000 ACCESSIONS S67644; S19638; S05743; S67417; S72105; S19058 REFERENCE S67629 !$#authors Ballesta, J.P.G.; Remacha, M.; Soler-Mira, A.; Jimenez, A.; !1Garcia-Cantalejo, J.M.; Boskovic, J.; del Rey, F.; Revuelta, !1J.L.; Buitrago, M.J.; Sanz, J.E. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67644 !'##molecule_type DNA !'##residues 1-1097 ##label BAL !'##cross-references EMBL:Z74150; NID:g1431141; PIDN:CAA98669.1; !1PID:g1431142; GSPDB:GN00004; MIPS:YDL102w !'##experimental_source strain S288C REFERENCE S19638 !$#authors Morrison, A.; Sugino, A. !$#journal Nucleic Acids Res. (1992) 20:375 !$#title Nucleotide sequence of the POL3 gene encoding DNA polymerase !1III (delta) of Saccharomyces cerevisiae. !$#cross-references MUID:92158636; PMID:1741270 !$#accession S19638 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-77,'EL',80-1097 ##label MOR !'##cross-references EMBL:X61920; NID:g4190; PIDN:CAA43922.1; PID:g4191 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1September 1991 REFERENCE S05743 !$#authors Boulet, A.; Simon, M.; Faye, G.; Bauer, G.A.; Burgers, !1P.M.J. !$#journal EMBO J. (1989) 8:1849-1854 !$#title Structure and function of the Saccharomyces cerevisiae CDC2 !1gene encoding the large subunit of DNA polymerase III. !$#cross-references MUID:89356661; PMID:2670563 !$#accession S05743 !'##molecule_type DNA !'##residues 1-188,'R',190-203,'D',205-346,'YL',349,'LRNHS',355, !1'VMCYSD',364-646,'HY',650-869,'D',871-972,974-1097 ##label !1BOU !'##cross-references EMBL:X15477; NID:g3479; PIDN:CAA33504.1; PID:g3480 REFERENCE S67406 !$#authors Boskovic, J.; Saiz, J.E.; Soler-Mira, A.; Garcia-Cantalejo, !1J.; Revuelta, J.L.; Jiminez, A.; Ballesta, J.P.G.; del Rey, !1F.; Remacha, M. !$#submission submitted to the EMBL Data Library, February 1996 !$#accession S67417 !'##molecule_type DNA !'##residues 1-1097 ##label BOS !'##cross-references EMBL:X95644; NID:g1199535; PIDN:CAA64911.1; !1PID:g1199547 REFERENCE S72094 !$#authors Saiz, J.E.; Buitrago, M.J.; Garcia, R.; Revuelta, J.L.; del !1Rey, F. !$#journal Yeast (1996) 12:1077-1084 !$#title The sequence of a 20.3 kb DNA fragment from the left arm of !1Saccharomyces cerevisiae chromosome IV contains the KIN28, !1MSS2, PHO2, POL3 and DUN1 genes, and six new open reading !1frames. !$#cross-references MUID:97051597; PMID:8896274 !$#accession S72105 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1097 ##label SAI !'##cross-references EMBL:X95644; NID:g1199535; PIDN:CAA64911.1; !1PID:g1199547 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1February 1996 GENETICS !$#gene SGD:CDC2; POL3; MIPS:YDL102w !'##cross-references MIPS:YDL102w; SGD:S0002260 !$#map_position 4L CLASSIFICATION #superfamily herpesvirus DNA-directed DNA polymerase KEYWORDS DNA binding; DNA replication; heterodimer; !1nucleotidyltransferase; zinc finger FEATURE !$1009-1027 #region zinc finger CCCC motif\ !$1056-1074 #region zinc finger CCCC motif SUMMARY #length 1097 #molecular-weight 124590 #checksum 791 SEQUENCE /// ENTRY JC5757 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) III - yeast (Candida albicans) ALTERNATE_NAMES DNA polymerase III ORGANISM #formal_name Candida albicans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 08-Dec-2000 ACCESSIONS JC5757; S60677 REFERENCE JC5757 !$#authors Nolan, T.; Rosamond, J. !$#journal Gene (1996) 183:159-165 !$#title Isolation and molecular characterisation of the POL3 gene !1from Candida albicans. !$#cross-references MUID:97149294; PMID:8996102 !$#accession JC5757 !'##molecule_type DNA !'##residues 1-1038 ##label NOL !'##cross-references EMBL:X88804 !'##note submitted to the EMBL Data Library, June 1995 COMMENT This enzyme plays a role in DNA replication. GENETICS !$#gene pol3 CLASSIFICATION #superfamily herpesvirus DNA-directed DNA polymerase KEYWORDS nucleotidyltransferase; zinc finger FEATURE !$942-961 #region zinc finger CCCC motif\ !$992-1010 #region zinc finger CCCC motif SUMMARY #length 1038 #molecular-weight 118832 #checksum 5263 SEQUENCE /// ENTRY S19661 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) III large chain - fission yeast (Schizosaccharomyces pombe) ORGANISM #formal_name Schizosaccharomyces pombe DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S19661 REFERENCE S19661 !$#authors Pignede, G.; Bouvier, D.; de Recondo, A.M.; Baldacci, G. !$#journal J. Mol. Biol. (1991) 222:209-218 !$#title Characterization of the POL3 gene product from !1Schizosaccharomyces pombe indicates inter-species !1conservation of the catalytic subunit of DNA polymerase !1delta. !$#cross-references MUID:92071954; PMID:1960723 !$#accession S19661 !'##molecule_type DNA !'##residues 1-1084 ##label PIG !'##cross-references EMBL:X59278; NID:g5010; PIDN:CAA41968.1; PID:g5011 GENETICS !$#introns 77/1 CLASSIFICATION #superfamily herpesvirus DNA-directed DNA polymerase KEYWORDS DNA binding; nucleotidyltransferase; nucleus SUMMARY #length 1084 #molecular-weight 123211 #checksum 7633 SEQUENCE /// ENTRY A42543 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - Chlorella virus PBCV-1 ORGANISM #formal_name Chlorella virus PBCV-1 DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 07-May-1999 ACCESSIONS A42543 REFERENCE A42543 !$#authors Grabherr, R.; Strasser, P.; Van Etten, J.L. !$#journal Virology (1992) 188:721-731 !$#title The DNA polymerase gene from chlorella viruses PBCV-1 and !1NY-2A contains an intron with nuclear splicing sequences. !$#cross-references MUID:92263776; PMID:1585643 !$#accession A42543 !'##molecule_type DNA !'##residues 1-913 ##label GRA !'##cross-references GB:M86836; NID:g323319; PID:g323320 GENETICS !$#introns 682/3 CLASSIFICATION #superfamily herpesvirus DNA-directed DNA polymerase KEYWORDS DNA binding; DNA biosynthesis; DNA replication; exonuclease; !1nucleotidyltransferase FEATURE !$182-199 #region exonuclease pattern A\ !$268-282 #region exonuclease pattern B\ !$388-401 #region exonuclease pattern C SUMMARY #length 913 #molecular-weight 104786 #checksum 8356 SEQUENCE /// ENTRY A41618 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) delta catalytic chain - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A41618; S35455 REFERENCE A41618 !$#authors Chung, D.W.; Zhang, J.; Tan, C.K.; Davie, E.W.; So, A.G.; !1Downey, K.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:11197-11201 !$#title Primary structure of the catalytic subunit of human DNA !1polymerase delta and chromosomal location of the gene. !$#cross-references MUID:92107916; PMID:1722322 !$#accession A41618 !'##status preliminary !'##molecule_type mRNA !'##residues 1-1107 ##label CHU !'##cross-references GB:M80397; NID:g181619; PIDN:AAA58439.1; !1PID:g181620 REFERENCE S35455 !$#authors Yang, C.L.; Chang, L.S.; Zhang, P.; Hao, H.; Zhu, L.; !1Toomey, N.L.; Lee, M.Y.W.T. !$#journal Nucleic Acids Res. (1992) 20:735-745 !$#title Molecular cloning of the cDNA for the catalytic subunit of !1human DNA polymerase delta. !$#cross-references MUID:92178967; PMID:1542570 !$#accession S35455 !'##molecule_type mRNA !'##residues 1-29,'R',31-118,'H',120-172,'N',174-471,'Y',473-775,'G', !1777-1107 ##label YAN !'##cross-references EMBL:M81735; NID:g181621; PIDN:AAA35768.1; !1PID:g181622 GENETICS !$#gene GDB:POLD1; POLD !'##cross-references GDB:129089; OMIM:174761 !$#map_position 19q13.3-19q13.3 CLASSIFICATION #superfamily herpesvirus DNA-directed DNA polymerase KEYWORDS DNA binding; DNA replication; nucleotidyltransferase; !1nucleus; zinc finger SUMMARY #length 1107 #molecular-weight 123634 #checksum 7683 SEQUENCE /// ENTRY A39299 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) delta catalytic chain - bovine ALTERNATE_NAMES DNA-directed DNA polymerase III 125K chain CONTAINS DNA-directed DNA polymerase delta, 116K chain ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A39299 REFERENCE A39299 !$#authors Zhang, J.; Chung, D.W.; Tan, C.K.; Downey, K.M.; Davie, !1E.W.; So, A.G. !$#journal Biochemistry (1991) 30:11742-11750 !$#title Primary structure of the catalytic subunit of calf thymus !1DNA polymerase delta: sequence similarities with other DNA !1polymerases. !$#cross-references MUID:92089082; PMID:1721537 !$#accession A39299 !'##molecule_type mRNA !'##residues 1-1106 ##label ZHA !'##cross-references GB:M80395; NID:g162973; PIDN:AAA30493.1; !1PID:g162974 !'##experimental_source thymus !'##note 131-Glu and 263-Ser were also found by mRNA sequencing !'##note part of this sequence was confirmed by protein sequencing !'##note the amino end of the mature protein was blocked COMMENT A 116K polypeptide was shown to be a degradation product of !1the mature protein with 19 residues removed from the amino !1end and an unknown number of residues removed from the !1carboxyl end. CLASSIFICATION #superfamily herpesvirus DNA-directed DNA polymerase KEYWORDS DNA binding; DNA replication; nucleotidyltransferase; !1nucleus; zinc finger SUMMARY #length 1106 #molecular-weight 123707 #checksum 3031 SEQUENCE /// ENTRY S40243 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) delta chain - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S40243; JT0670 REFERENCE S40243 !$#authors Cullmann, G.; Hindges, R.; Berchtold, M.W.; Huebscher, U. !$#submission submitted to the EMBL Data Library, March 1993 !$#accession S40243 !'##molecule_type mRNA !'##residues 1-1105 ##label CUL !'##cross-references EMBL:Z21848; NID:g438133; PIDN:CAA79895.1; !1PID:g438134 REFERENCE JT0670 !$#authors Cullmann, G.; Hindges, R.; Berchtold, M.W.; Huebscher, U. !$#journal Gene (1993) 134:191-200 !$#title Cloning of a mouse cDNA encoding DNA polymerase delta: !1refinement of the homology boxes. !$#cross-references MUID:94085777; PMID:8262377 !$#accession JT0670 !'##molecule_type DNA !'##residues 1-111,'G',113,'P',115-1034,'Y',1036-1105 ##label CU2 !'##cross-references EMBL:Z21848 !'##note the sequence translated from Z21848 is inconsistent with that !1from this sequence in having 112-Arg, 114-Leu, and 1035-Ser COMMENT Three DNA polymerases alpha, delta and epsilon chains are !1essential. This delta chain is involved in the elongation of !1the short new strands synthesized by alpha chain. GENETICS !$#gene poldelta CLASSIFICATION #superfamily herpesvirus DNA-directed DNA polymerase KEYWORDS DNA replication; heterodimer; nucleotidyltransferase SUMMARY #length 1105 #molecular-weight 123782 #checksum 2837 SEQUENCE /// ENTRY B42543 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - Chlorella virus CV-NY-2A ORGANISM #formal_name Chlorella virus CV-NY-2A DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 11-Jun-1999 ACCESSIONS B42543 REFERENCE A42543 !$#authors Grabherr, R.; Strasser, P.; Van Etten, J.L. !$#journal Virology (1992) 188:721-731 !$#title The DNA polymerase gene from chlorella viruses PBCV-1 and !1NY-2A contains an intron with nuclear splicing sequences. !$#cross-references MUID:92263776; PMID:1585643 !$#accession B42543 !'##molecule_type DNA !'##residues 1-913 ##label GRA !'##cross-references GB:M86837; NID:g323321; PIDN:AAA88827.1; !1PID:g323322 GENETICS !$#introns 682/3 CLASSIFICATION #superfamily herpesvirus DNA-directed DNA polymerase KEYWORDS DNA binding; DNA biosynthesis; DNA replication; exonuclease; !1nucleotidyltransferase FEATURE !$182-199 #region exonuclease pattern A\ !$268-282 #region exonuclease pattern B\ !$388-401 #region exonuclease pattern C SUMMARY #length 913 #molecular-weight 104955 #checksum 3361 SEQUENCE /// ENTRY DJBE2L #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 11-Jun-1999 ACCESSIONS A00713; S33054 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession A00713 !'##molecule_type DNA !'##residues 1-1015 ##label BAN !'##cross-references EMBL:V01555; NID:g59074; PIDN:CAA24805.1; !1PID:g1334913 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region CLASSIFICATION #superfamily herpesvirus DNA-directed DNA polymerase KEYWORDS DNA binding; DNA replication; nucleotidyltransferase SUMMARY #length 1015 #molecular-weight 113417 #checksum 4360 SEQUENCE /// ENTRY DJBEM2 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - saimiriine herpesvirus 1 (strain 11) ORGANISM #formal_name saimiriine herpesvirus 1 #note host Saimiri sciureus (common squirrel monkey) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 11-Jun-1999 ACCESSIONS I36806 REFERENCE A36806 !$#authors Albrecht, J. !$#submission submitted to the EMBL Data Library, January 1992 !$#description Primary structure of the herpesvirus saimiri genome. !$#accession I36806 !'##molecule_type DNA !'##residues 1-1009 ##label ALB !'##cross-references GB:X64346; NID:g60320; PIDN:CAA45632.1; PID:g60330 REFERENCE A37309 !$#authors Albrecht, J.C.; Nicholas, J.; Biller, D.; Cameron, K.R.; !1Biesinger, B.; Newman, C.; Wittmann, S.; Craxton, M.A.; !1Coleman, H.; Fleckenstein, B.; Honess, R.W. !$#journal J. Virol. (1992) 66:5047-5058 !$#title Primary structure of the herpesvirus saimiri genome. !$#cross-references MUID:92333688; PMID:1321287 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 9 CLASSIFICATION #superfamily herpesvirus DNA-directed DNA polymerase KEYWORDS DNA binding; DNA replication; nucleotidyltransferase SUMMARY #length 1009 #molecular-weight 113934 #checksum 1774 SEQUENCE /// ENTRY DJBEK1 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - human herpesvirus 1 (strain KOS) ORGANISM #formal_name human herpesvirus 1 #note host (African green monkey) DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 11-Jun-1999 ACCESSIONS A00714 REFERENCE A00714 !$#authors Gibbs, J.S.; Chiou, H.C.; Hall, J.D.; Mount, D.W.; Retondo, !1M.J.; Weller, S.K.; Coen, D.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:7969-7973 !$#title Sequence and mapping analyses of the herpes simplex virus !1DNA polymerase gene predict a C-terminal substrate binding !1domain. !$#cross-references MUID:86068025; PMID:2999787 !$#accession A00714 !'##molecule_type DNA !'##residues 1-1235 ##label GIB !'##cross-references GB:M10792; NID:g330185; PIDN:AAA66438.1; !1PID:g330186 GENETICS !$#map_position 0.410-0.435 CLASSIFICATION #superfamily herpesvirus DNA-directed DNA polymerase KEYWORDS DNA binding; DNA replication; nucleotidyltransferase SUMMARY #length 1235 #molecular-weight 136519 #checksum 772 SEQUENCE /// ENTRY DJBE16 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - human herpesvirus 1 (strain SC16) ORGANISM #formal_name human herpesvirus 1 DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 11-Jun-1999 ACCESSIONS A26163 REFERENCE A26163 !$#authors Larder, B.A.; Kemp, S.D.; Darby, G. !$#journal EMBO J. (1987) 6:169-175 !$#title Related functional domains in virus DNA polymerases. !$#cross-references MUID:87218463; PMID:3034575 !$#accession A26163 !'##molecule_type DNA !'##residues 1-1235 ##label LAR !'##cross-references GB:X04771; NID:g59839; PIDN:CAA28464.1; PID:g59840 CLASSIFICATION #superfamily herpesvirus DNA-directed DNA polymerase KEYWORDS DNA binding; DNA replication; nucleotidyltransferase SUMMARY #length 1235 #molecular-weight 136466 #checksum 307 SEQUENCE /// ENTRY DJBEAN #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - human herpesvirus 1 (strain Angelotti) ORGANISM #formal_name human herpesvirus 1 DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 11-Jun-1999 ACCESSIONS A25552 REFERENCE A25552 !$#authors Knopf, C.W. !$#journal Nucleic Acids Res. (1986) 14:8225-8226 !$#title Nucleotide sequence of the DNA polymerase gene of herpes !1simplex virus type 1 strain Angelotti. !$#cross-references MUID:87040787; PMID:3022246 !$#accession A25552 !'##molecule_type DNA !'##residues 1-1235 ##label KNO !'##cross-references GB:X04495; NID:g59860; PIDN:CAA28183.1; PID:g59861 CLASSIFICATION #superfamily herpesvirus DNA-directed DNA polymerase KEYWORDS DNA binding; DNA replication; nucleotidyltransferase SUMMARY #length 1235 #molecular-weight 136602 #checksum 2386 SEQUENCE /// ENTRY DJBEV1 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - human herpesvirus 1 ORGANISM #formal_name human herpesvirus 1 #note host Homo sapiens (man) DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 28-May-1999 ACCESSIONS A00715 REFERENCE A93601 !$#authors Quinn, J.P.; McGeoch, D.J. !$#journal Nucleic Acids Res. (1985) 13:8143-8163 !$#title DNA sequence of the region in the genome of herpes simplex !1virus type 1 containing the genes for DNA polymerase and the !1major DNA binding protein. !$#cross-references MUID:86067223; PMID:2999714 !$#accession A00715 !'##molecule_type DNA !'##residues 1-1235 ##label QUI !'##cross-references GB:X03181; GB:M12356; NID:g59862; PIDN:CAA26941.1; !1PID:g59864 !'##experimental_source strain 17 GENETICS !$#map_position 0.41-0.43 CLASSIFICATION #superfamily herpesvirus DNA-directed DNA polymerase KEYWORDS DNA binding; DNA replication; nucleotidyltransferase SUMMARY #length 1235 #molecular-weight 136281 #checksum 8830 SEQUENCE /// ENTRY DJBEH7 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - human herpesvirus 1 (strain 17) ORGANISM #formal_name human herpesvirus 1 DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jun-2000 ACCESSIONS C30085 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession C30085 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1235 ##label MCG !'##cross-references GB:X14112; GB:D00317; GB:D00374; GB:S40593; !1NID:g1944536; PIDN:CAA32323.1; PID:g59530 GENETICS !$#gene UL30 CLASSIFICATION #superfamily herpesvirus DNA-directed DNA polymerase KEYWORDS DNA binding; DNA replication; nucleotidyltransferase SUMMARY #length 1235 #molecular-weight 136420 #checksum 495 SEQUENCE /// ENTRY DJBE21 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - human herpesvirus 2 (strain 186) ORGANISM #formal_name human herpesvirus 2 DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 11-Jun-1999 ACCESSIONS A27315 REFERENCE A27315 !$#authors Tsurumi, T.; Maeno, K.; Nishiyama, Y. !$#journal Gene (1987) 52:129-137 !$#title Nucleotide sequence of the DNA polymerase gene of herpes !1simplex virus type 2 and comparison with the type 1 !1counterpart. !$#cross-references MUID:87277385; PMID:3038677 !$#accession A27315 !'##molecule_type DNA !'##residues 1-1240 ##label TSU !'##cross-references GB:M16321; NID:g330291; PIDN:AAA45853.1; !1PID:g330292 CLASSIFICATION #superfamily herpesvirus DNA-directed DNA polymerase KEYWORDS DNA binding; DNA replication; nucleotidyltransferase SUMMARY #length 1240 #molecular-weight 137354 #checksum 7922 SEQUENCE /// ENTRY DJBE28 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 11-Jun-1999 ACCESSIONS B27214 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession B27214 !'##molecule_type DNA !'##residues 1-1194 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27911.1; !1PID:g60017 GENETICS !$#gene 28 CLASSIFICATION #superfamily herpesvirus DNA-directed DNA polymerase KEYWORDS DNA binding; DNA replication; nucleotidyltransferase SUMMARY #length 1194 #molecular-weight 134047 #checksum 5636 SEQUENCE /// ENTRY DJBEC3 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 11-Jun-1999 ACCESSIONS D36798 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession D36798 !'##molecule_type DNA !'##residues 1-1220 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02465.1; !1PID:g330822 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 30 CLASSIFICATION #superfamily herpesvirus DNA-directed DNA polymerase KEYWORDS DNA binding; DNA replication; nucleotidyltransferase SUMMARY #length 1220 #molecular-weight 135955 #checksum 4769 SEQUENCE /// ENTRY DJBEC1 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - human cytomegalovirus (strain AD169) ALTERNATE_NAMES HFLF2 protein; UL54 protein ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 #note host Homo sapiens (man) DATE 31-Mar-1988 #sequence_revision 31-Dec-1990 #text_change 11-Jun-1999 ACCESSIONS S09817; A25983 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09817 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1242 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35413.1; !1PID:g1780832 !'##note possible protein-coding frames are given !'##note the DNA sequence was submitted to EMBL, December 1989, in !1computer-readable form REFERENCE A25983 !$#authors Kouzarides, T.; Bankier, A.T.; Satchwell, S.C.; Weston, K.; !1Tomlinson, P.; Barrell, B.G. !$#journal J. Virol. (1987) 61:125-133 !$#title Sequence and transcription analysis of the human !1cytomegalovirus DNA polymerase gene. !$#cross-references MUID:87061230; PMID:3023690 !$#accession A25983 !'##molecule_type DNA !'##residues 1-1242 ##label KOU !'##cross-references GB:M14709; NID:g330640; PIDN:AAA45988.1; !1PID:g330642 GENETICS !$#map_position unique long region (U-l) CLASSIFICATION #superfamily herpesvirus DNA-directed DNA polymerase KEYWORDS DNA binding; DNA replication; nucleotidyltransferase SUMMARY #length 1242 #molecular-weight 137101 #checksum 2059 SEQUENCE /// ENTRY DJBEMC #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - murine cytomegalovirus (strain Smith) ORGANISM #formal_name murine cytomegalovirus, murine herpesvirus 1 DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 11-Jun-1999 ACCESSIONS B40780 REFERENCE A40780 !$#authors Elliott, R.; Clark, C.; Jaquish, D.; Spector, D.H. !$#journal Virology (1991) 185:169-186 !$#title Transcription analysis and sequence of the putative murine !1cytomegalovirus DNA polymerase gene. !$#cross-references MUID:92024072; PMID:1718083 !$#accession B40780 !'##molecule_type DNA !'##residues 1-1097 ##label ELL !'##cross-references GB:M73549; NID:g330516; PIDN:AAA45940.1; !1PID:g330518 CLASSIFICATION #superfamily herpesvirus DNA-directed DNA polymerase KEYWORDS DNA binding; DNA replication; nucleotidyltransferase SUMMARY #length 1097 #molecular-weight 123573 #checksum 9958 SEQUENCE /// ENTRY DJBE6S #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - human herpesvirus 6 (strain U1102) ORGANISM #formal_name human herpesvirus 6 #note host Homo sapiens (man) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 01-Dec-2000 ACCESSIONS B40898; T09332 REFERENCE A40898 !$#authors Teo, I.A.; Griffin, B.E.; Jones, M.D. !$#journal J. Virol. (1991) 65:4670-4680 !$#title Characterization of the DNA polymerase gene of human !1herpesvirus 6. !$#cross-references MUID:91333007; PMID:1651403 !$#accession B40898 !'##molecule_type DNA !'##residues 1-1012 ##label TEO !'##cross-references GB:M63804; NID:g325467; PIDN:AAA74631.1; !1PID:g455196 REFERENCE Z16644 !$#authors Nicholas, J.; Martin, M. !$#journal J. Virol. (1994) 68:597-610 !$#title Nucleotide sequence analysis of a 38.5-kilobase-pair region !1of the genome of human herpesvirus 6 encoding human !1cytomegalovirus immediate-early gene homologs and !1transactivating functions. !$#cross-references MUID:94118404; PMID:8289364 !$#accession T09332 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 778-1012 ##label NIC !'##cross-references EMBL:L25528; NID:g451932; PIDN:AAA16745.1; !1PID:g451963 GENETICS !$#gene XILF0 CLASSIFICATION #superfamily herpesvirus DNA-directed DNA polymerase KEYWORDS DNA binding; DNA replication; nucleotidyltransferase SUMMARY #length 1012 #molecular-weight 115819 #checksum 5058 SEQUENCE /// ENTRY DJVZZW #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Feb-1997 ACCESSIONS A25270; A30177 REFERENCE A25270 !$#authors Earl, P.L.; Jones, E.V.; Moss, B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:3659-3663 !$#title Homology between DNA polymerase of poxviruses, !1herpesviruses, and adenoviruses: nucleotide sequence of the !1vaccinia virus DNA polymerase gene. !$#cross-references MUID:86233293; PMID:3012524 !$#accession A25270 !'##molecule_type DNA !'##residues 1-937 ##label EAR !'##cross-references EMBL:M13213 REFERENCE A30177 !$#authors Traktman, P.; Kelvin, M.; Pacheco, S. !$#journal J. Virol. (1989) 63:841-846 !$#title Molecular genetic analysis of vaccinia virus DNA polymerase !1mutants. !$#cross-references MUID:89095014; PMID:2911123 !$#accession A30177 !'##molecule_type DNA !'##residues 251-270,'H',272-673 ##label TRA !'##cross-references EMBL:M24214 COMMENT The phosphonoacetate-resistance (PAA-R) mutant differs from !1that shown in having 313-Phe and 347-Asp. COMMENT The mutants NG26 and ts42 differ from that shown in having !1367-Asp and 586-Lys, respectively. CLASSIFICATION #superfamily herpesvirus DNA-directed DNA polymerase KEYWORDS DNA binding; DNA replication; nucleotidyltransferase SUMMARY #length 937 #molecular-weight 108445 #checksum 3406 SEQUENCE /// ENTRY DJVZ4I #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - vaccinia virus (strain Copenhagen) ALTERNATE_NAMES E9L protein ORGANISM #formal_name vaccinia virus #note host Homo sapiens (man) DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 11-Jun-1999 ACCESSIONS D42509 REFERENCE A42501 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:517-563 !$#title Appendix to "The complete DNA sequence of vaccinia virus". !$#accession D42509 !'##molecule_type DNA !'##residues 1-1006 ##label GOE !'##cross-references GB:M35027; NID:g335317; PIDN:AAA48049.1; !1PID:g335397 !'##experimental_source strain Copenhagen REFERENCE A42531 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:247-266 !$#title The complete DNA sequence of vaccinia virus. !$#cross-references MUID:91021027; PMID:2219722 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given CLASSIFICATION #superfamily herpesvirus DNA-directed DNA polymerase KEYWORDS DNA binding; DNA biosynthesis; nucleotidyltransferase SUMMARY #length 1006 #molecular-weight 116902 #checksum 6282 SEQUENCE /// ENTRY DJVZFP #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - fowlpox virus (strain HP444) ORGANISM #formal_name fowlpox virus DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 11-Jun-1999 ACCESSIONS A26802 REFERENCE A26802 !$#authors Binns, M.M.; Stenzler, L.; Tomley, F.M.; Campbell, J.; !1Boursnell, M.E.G. !$#journal Nucleic Acids Res. (1987) 15:6563-6573 !$#title Identification by a random sequencing strategy of the !1fowlpoxvirus DNA polymerase gene, its nucleotide sequence !1and comparison with other viral DNA polymerases. !$#cross-references MUID:87316919; PMID:2819823 !$#accession A26802 !'##molecule_type DNA !'##residues 1-988 ##label BIN !'##cross-references GB:M31638; GB:Y00415; NID:g325378; PIDN:AAA43821.1; !1PID:g325379 CLASSIFICATION #superfamily herpesvirus DNA-directed DNA polymerase KEYWORDS DNA binding; DNA biosynthesis; nucleotidyltransferase SUMMARY #length 988 #molecular-weight 116658 #checksum 2027 SEQUENCE /// ENTRY DJNVCP #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - Autographa californica nuclear polyhedrosis virus ORGANISM #formal_name Autographa californica nuclear polyhedrosis virus, AcMNPV DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 01-Dec-2000 ACCESSIONS A31832; B72858 REFERENCE A31832 !$#authors Tomalski, M.D.; Wu, J.; Miller, L.K. !$#journal Virology (1988) 167:591-600 !$#title The location, sequence, transcription, and regulation of a !1baculovirus DNA polymerase gene. !$#cross-references MUID:89073763; PMID:3059678 !$#accession A31832 !'##molecule_type DNA !'##residues 1-984 ##label TOM !'##cross-references GB:M20744; NID:g332416; PIDN:AAA46692.1; !1PID:g332417 REFERENCE A72850 !$#authors Ayres, M.D.; Howard, S.C.; Kuzio, J.; Lopez-Ferber, M.; !1Possee, R.D. !$#journal Virology (1994) 202:586-605 !$#title The complete DNA sequence of Autographa californica nuclear !1polyhedrosis virus. !$#cross-references MUID:94303173; PMID:8030224 !$#accession B72858 !'##status preliminary !'##molecule_type DNA !'##residues 1-829,'R',831-984 ##label AYR !'##cross-references GB:L22858; NID:g510708; PIDN:AAA66695.1; !1PID:g559134 GENETICS !$#gene Ac-DNA-pol CLASSIFICATION #superfamily herpesvirus DNA-directed DNA polymerase KEYWORDS DNA binding; DNA biosynthesis; nucleotidyltransferase SUMMARY #length 984 #molecular-weight 114337 #checksum 3843 SEQUENCE /// ENTRY I38950 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) delta regulatory chain - human ALTERNATE_NAMES DNA polymerase delta 2 chain; DNA polymerase delta small chain ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Oct-1998 #sequence_revision 30-Oct-1998 #text_change 11-Jun-1999 ACCESSIONS I38950 REFERENCE I38950 !$#authors Zhang, J.; Tan, C.K.; McMullen, B.; Downey, K.M.; So, A.G. !$#journal Genomics (1995) 29:179-186 !$#title Cloning of the cDNAs for the small subunits of bovine and !1human DNA polymerase delta and chromosomal location of the !1human gene (POLD2). !$#cross-references MUID:96079106; PMID:8530069 !$#accession I38950 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-469 ##label RES !'##cross-references EMBL:U21090; NID:g1008457; PIDN:AAC50216.1; !1PID:g1008458 GENETICS !$#gene GDB:POLD2 !'##cross-references GDB:579578; OMIM:600815 !$#map_position 7pter-7qter COMPLEX heterodimer of catalytic (see PIR:A41618) and regulatory !1chain FUNCTION !$#description DNA polymerase delta is involved in DNA replication and in !1nucleotide excision repair CLASSIFICATION #superfamily human DNA-directed DNA polymerase delta !1regulatory chain KEYWORDS DNA repair; DNA replication; nucleotidyltransferase; nucleus SUMMARY #length 469 #molecular-weight 51289 #checksum 47 SEQUENCE /// ENTRY I46076 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) delta regulatory chain - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Oct-1998 #sequence_revision 30-Oct-1998 #text_change 11-Jun-1999 ACCESSIONS I46076 REFERENCE I38950 !$#authors Zhang, J.; Tan, C.K.; McMullen, B.; Downey, K.M.; So, A.G. !$#journal Genomics (1995) 29:179-186 !$#title Cloning of the cDNAs for the small subunits of bovine and !1human DNA polymerase delta and chromosomal location of the !1human gene (POLD2). !$#cross-references MUID:96079106; PMID:8530069 !$#accession I46076 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-469 ##label ZHA !'##cross-references EMBL:U21091; NID:g1008459; PIDN:AAC48475.1; !1PID:g1008460 !'##note parts of this sequence were determined by protein sequencing COMPLEX heterodimer of catalytic (see PIR:A39299) and regulatory !1chain FUNCTION !$#description DNA polymerase delta is involved in DNA replication and in !1nucleotide excision repair CLASSIFICATION #superfamily human DNA-directed DNA polymerase delta !1regulatory chain KEYWORDS DNA repair; DNA replication; nucleotidyltransferase; nucleus SUMMARY #length 469 #molecular-weight 50886 #checksum 9315 SEQUENCE /// ENTRY S55194 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) III regulatory chain - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES DNA-directed DNA polymerase delta small chain; HUS2 protein; HYS2 protein; protein J1427; protein YJR006w; protein YJR83.7; translation initiation factor 2 alpha subunit ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Oct-1998 #sequence_revision 30-Oct-1998 #text_change 21-Jul-2000 ACCESSIONS S55194; S57021; S59122 REFERENCE S55183 !$#authors de Haan, M.; Smits, P.H.M.; Grivell, L.A. !$#submission submitted to the EMBL Data Library, May 1995 !$#accession S55194 !'##molecule_type DNA !'##residues 1-487 ##label DEH !'##cross-references EMBL:X87611; NID:g854567; PIDN:CAA60928.1; !1PID:g854579 REFERENCE S56771 !$#authors de Haan, M.; Grivell, L.A.; Smits, P.H.M. !$#submission submitted to the Protein Sequence Database, September 1995 !$#accession S57021 !'##molecule_type DNA !'##residues 1-487 ##label ZAG !'##cross-references EMBL:Z49506; NID:g1015629; PIDN:CAA89528.1; !1PID:g1015630; GSPDB:GN00010; MIPS:YJR006w REFERENCE S59122 !$#authors Sugimoto, K.; Sakamoto, Y.; Takahashi, O.; Matsumoto, K. !$#journal Nucleic Acids Res. (1995) 23:3493-3500 !$#title HYS2, an essential gene required for DNA replication in !1Saccharomyces cerevisiae. !$#cross-references MUID:96032843; PMID:7567461 !$#accession S59122 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-155,'H',157-464,'N',466-487 ##label SUG !'##cross-references EMBL:D50324; NID:g987711; PIDN:BAA08859.1; !1PID:g1256943 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1995 GENETICS !$#gene SGD:HUS2; HYS2; MIPS:YJR006w !'##cross-references SGD:S0003766; MIPS:YJR006w !$#map_position 10R COMPLEX heterodimer of catalytic (see PIR:RNBYL3) and regulatory !1chain FUNCTION !$#description DNA polymerase delta is involved in DNA replication and in !1nucleotide excision repair CLASSIFICATION #superfamily human DNA-directed DNA polymerase delta !1regulatory chain KEYWORDS DNA repair; DNA replication; nucleotidyltransferase; nucleus SUMMARY #length 487 #molecular-weight 55295 #checksum 9810 SEQUENCE /// ENTRY DJBPT7 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) phage chain - phage T7 ALTERNATE_NAMES T7 DNA polymerase ORGANISM #formal_name phage T7 DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 11-Jun-1999 ACCESSIONS A00716; S42311 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession A00716 !'##molecule_type DNA !'##residues 1-704 ##label DUN REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42311 !'##molecule_type DNA !'##residues 1-704 ##label DUW !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24412.1; !1PID:g15591 COMMENT T7 DNA polymerase is composed of two chains. One is encoded !1by the phage gene 5 and the other is encoded by the host !1gene tsnC, which codes for thioredoxin. Thioredoxins !1isolated from spinach chloroplasts can be substituted for !1the E. coli subunit and the resultant polymerases exhibit !1the same activity as the wild type. COMMENT In addition to polymerase activity, T7 DNA polymerase !1exhibits a 3' to 5' exonuclease activity. GENETICS !$#gene 5 !$#map_position 35.94-41.23 CLASSIFICATION #superfamily phage T7 DNA-directed DNA polymerase phage !1chain KEYWORDS DNA binding; nucleotidyltransferase SUMMARY #length 704 #molecular-weight 79691 #checksum 3767 SEQUENCE /// ENTRY DJBPT4 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - phage T4 ALTERNATE_NAMES gp 43 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 17-Mar-1987 #sequence_revision 30-Jun-1987 #text_change 11-Jun-1999 ACCESSIONS JS0791; PU0006; A28165; JU0097; A00717 REFERENCE A04303 !$#authors Spicer, E.K.; Konigsberg, W.H. !$#book Bacteriophage T4, Mathews, C.K., Kutter, E.M., Mosig, G., !1and Berget, P.B., eds., pp.291-301, American Society for !1Microbiology, Washington, 1983 !$#title Organization and structure of four T4 genes coding for DNA !1replication proteins. !$#accession JS0791 !'##molecule_type DNA !'##residues 1-898 ##label SPI !$#accession PU0006 !'##molecule_type protein !'##residues 1-22 ##label SP2 REFERENCE A28165 !$#authors Spicer, E.K.; Rush, J.; Fung, C.; Reha-Krantz, L.J.; Karam, !1J.D.; Konigsberg, W.H. !$#journal J. Biol. Chem. (1988) 263:7478-7486 !$#title Primary structure of T4 DNA polymerase. !$#cross-references MUID:88227938; PMID:3286635 !$#accession A28165 !'##molecule_type DNA !'##residues 1-898 ##label SP3 !'##cross-references GB:M10160; GB:J02510; GB:X00769; NID:g2947028; !1PIDN:AAC05397.1; PID:g215908 REFERENCE JF0071 !$#authors Lamm, N.; Wang, Y.; Mathews, C.K.; Rueger, W. !$#journal Eur. J. Biochem. (1988) 172:553-563 !$#title Deoxycytidylate hydroxymethylase gene of bacteriophage T4: !1nucleotide sequence determination and over-expression of the !1gene. !$#cross-references MUID:88166734; PMID:3350013 !$#accession JU0097 !'##molecule_type DNA !'##residues 338-898 ##label LAM !'##cross-references GB:M37159; GB:M28192; NID:g215839; PIDN:AAA21706.1; !1PID:g215840 COMMENT This enzyme is required for both initiation and maintenance !1of viral DNA replication. GENETICS !$#gene 43 !$#map_position 27.201-29.895 CLASSIFICATION #superfamily phage T4 DNA-directed DNA polymerase KEYWORDS DNA binding; DNA replication; nucleotidyltransferase SUMMARY #length 898 #molecular-weight 103609 #checksum 8727 SEQUENCE /// ENTRY DJBPS2 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - phage SPO2 ORGANISM #formal_name phage SPO2 #note host Bacillus subtilis DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 11-Jun-1999 ACCESSIONS A21498 REFERENCE A21498 !$#authors Raden, B.; Rutberg, L. !$#journal J. Virol. (1984) 52:9-15 !$#title Nucleotide sequence of the temperate Bacillus subtilis !1bacteriophage SPO2 DNA polymerase gene L. !$#cross-references MUID:85009880; PMID:6090713 !$#accession A21498 !'##molecule_type DNA !'##residues 1-648 ##label RAD !'##cross-references EMBL:K02752; NID:g216150; PIDN:AAA32600.1; !1PID:g216151 GENETICS !$#gene L !$#start_codon TTG CLASSIFICATION #superfamily phage SPO2 DNA-directed DNA polymerase KEYWORDS DNA binding; DNA replication; nucleotidyltransferase SUMMARY #length 648 #molecular-weight 72579 #checksum 2314 SEQUENCE /// ENTRY DJBPD1 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - phage PRD1 ORGANISM #formal_name phage PRD1 #note host Escherichia coli DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 11-Jun-1999 ACCESSIONS B27328; B40477; A39970 REFERENCE A27328 !$#authors Savilahti, H.; Bamford, D.H. !$#journal Gene (1987) 57:121-130 !$#title The complete nucleotide sequence of the left very early !1region of Escherichia coli bacteriophage PRD1 coding for the !1terminal protein and the DNA polymerase. !$#cross-references MUID:88112855; PMID:3322943 !$#accession B27328 !'##molecule_type DNA !'##residues 1-553 ##label SAV !'##cross-references GB:M22161; NID:g215750; PIDN:AAA32450.1; !1PID:g215752 REFERENCE A40477 !$#authors Bamford, J.K.H.; Haenninen, A.L.; Pakula, T.M.; Ojala, P.M.; !1Kalkkinen, N.; Frilander, M.; Bamford, D.H. !$#journal Virology (1991) 183:658-676 !$#title Genome organization of membrane-containing bacteriophage !1PRD1. !$#cross-references MUID:91306449; PMID:1853567 !$#accession B40477 !'##status translation not shown !'##molecule_type DNA !'##residues 1-553 ##label BAM !'##cross-references GB:M69077; NID:g215765; PIDN:AAA32456.1; !1PID:g215767 REFERENCE A39970 !$#authors Jung, G.; Leavitt, M.C.; Hsieh, J.C.; Ito, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:8287-8291 !$#title Bacteriophage PRD1 DNA polymerase: evolution of DNA !1polymerases. !$#cross-references MUID:88068579; PMID:3479792 !$#accession A39970 !'##molecule_type DNA !'##residues 1-553 ##label JUN !'##cross-references GB:J03018; NID:g215760; PIDN:AAA32452.1; !1PID:g215761 COMMENT This DNA polymerase primes itself by forming a !1phosphodiester bond between 5'-dGMP and a tyrosine residue !1of the terminal protein PIR:TPBPPR. CLASSIFICATION #superfamily phage PRD1 DNA-directed DNA polymerase KEYWORDS DNA binding; nucleotidyltransferase SUMMARY #length 553 #molecular-weight 63336 #checksum 1622 SEQUENCE /// ENTRY DJECI #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) I - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 06-Jul-1982 #sequence_revision 06-Jul-1982 #text_change 01-Mar-2002 ACCESSIONS A92360; S40809; A55715; I56375; C65191; A00718 REFERENCE A92360 !$#authors Joyce, C.M.; Kelley, W.S.; Grindley, N.D.F. !$#journal J. Biol. Chem. (1982) 257:1958-1964 !$#title Nucleotide sequence of the Escherichia coli polA gene and !1primary structure of DNA polymerase I. !$#cross-references MUID:82120160; PMID:6276402 !$#accession A92360 !'##molecule_type DNA !'##residues 1-928 ##label BRO !'##cross-references GB:J01663; GB:J01703; GB:M20780; NID:g147311; !1PIDN:AAA24402.1; PID:g147312 !'##experimental_source strain K12 REFERENCE A92361 !$#authors Brown, W.E.; Stump, K.H.; Kelley, W.S. !$#journal J. Biol. Chem. (1982) 257:1965-1972 !$#title Escherichia coli DNA polymerase I. Sequence characterization !1and secondary structure prediction. !$#cross-references MUID:82120161; PMID:7035456 !$#contents annotation; amino acid composition; partial sequence !1confirming the nucleotide sequence REFERENCE S40802 !$#authors Plunkett III, G.; Burland, V.; Daniels, D.L.; Blattner, F.R. !$#journal Nucleic Acids Res. (1993) 21:3391-3398 !$#title Analysis of the Escherichia coli genome. III. DNA sequence !1of the region from 87.2 to 89.2 minutes. !$#cross-references MUID:93347969; PMID:8346018 !$#accession S40809 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-928 ##label PLU !'##cross-references EMBL:L19201; NID:g304961; PIDN:AAB02998.1; !1PID:g304969 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1993 REFERENCE A55715 !$#authors Pandey, V.N.; Kaushik, N.; Modak, M.J. !$#journal J. Biol. Chem. (1995) 270:2879 !$#accession A55715 !'##status preliminary !'##molecule_type protein !'##residues 759-775 ##label PAN REFERENCE I56375 !$#authors Kelley, W.S.; Joyce, C.M. !$#journal J. Mol. Biol. (1983) 164:529-560 !$#title Genetic characterization of early amber mutations in the !1Escherichia coli polA gene and purification of the amber !1peptides. !$#cross-references MUID:83189123; PMID:6302278 !$#accession I56375 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 284-350 ##label RES !'##cross-references GB:J01664; NID:g147314; PIDN:AAA24404.1; !1PID:g147315 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65191 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-928 ##label BLAT !'##cross-references GB:AE000461; GB:U00096; NID:g2367318; !1PIDN:AAC76861.1; PID:g1790294; UWGP:b3863 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene polA !$#map_position 84 min FUNCTION !$#description a single-chain monomer with multiple functions; catalyzes !1polymerization and 3'-5' and 5'-3' exonucleolytic digestion; !1mild proteolysis of the protein produces two fragments; the !1smaller amino-terminal fragment (1-323) contains the 5'-3' !1exonuclease activity and the larger carboxyl-terminal !1fragment (324-928) carries the polymerase and 3'-5' !1exonuclease activities CLASSIFICATION #superfamily DNA-directed DNA polymerase I KEYWORDS DNA binding; DNA biosynthesis; nucleotidyltransferase SUMMARY #length 928 #molecular-weight 103117 #checksum 3547 SEQUENCE /// ENTRY DJBPT5 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - phage T5 ORGANISM #formal_name phage T5 #note host Escherichia coli DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 11-Jun-1999 ACCESSIONS A33923; PS0178 REFERENCE A33923 !$#authors Leavitt, M.C.; Ito, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:4465-4469 !$#title T5 DNA polymerase: structural-functional relationships to !1other DNA polymerases. !$#cross-references MUID:89282793; PMID:2660138 !$#accession A33923 !'##molecule_type DNA !'##residues 1-829 ##label LEA !'##cross-references GB:M24354; NID:g215987; PIDN:AAA32561.1; !1PID:g215988 REFERENCE PS0178 !$#authors Chatterjee, D.K.; Fujimura, R.K.; Campbell, J.H.; Gerard, !1G.F. !$#journal Gene (1991) 97:13-19 !$#title Cloning and overexpression of the gene encoding !1bacteriophage T5 DNA polymerase. !$#cross-references MUID:91138976; PMID:1995424 !$#accession PS0178 !'##molecule_type DNA !'##residues 'MCNEKLSGRLL',16-167 ##label CHA !'##cross-references GB:M64047; NID:g215971; PIDN:AAA32558.1; !1PID:g215972 !'##note translation of the nucleotide sequence is not complete GENETICS !$#gene T5pol CLASSIFICATION #superfamily DNA-directed DNA polymerase I KEYWORDS DNA binding; DNA biosynthesis; nucleotidyltransferase SUMMARY #length 829 #molecular-weight 94410 #checksum 9684 SEQUENCE /// ENTRY JC1269 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - phage SPO1 ORGANISM #formal_name phage SPO1 #note host Bacillus subtilis DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 11-Jun-1999 ACCESSIONS JC1269; B36077 REFERENCE JC1269 !$#authors Scarlato, V.; Gargano, S. !$#journal Gene (1992) 118:109-113 !$#title The DNA polymerase-encoding gene of Bacillus subtilis !1bacteriophage SPO1. !$#cross-references MUID:92380475; PMID:1324872 !$#accession JC1269 !'##molecule_type DNA !'##residues 1-924 ##label SCA !'##cross-references GB:M84415; NID:g216113; PIDN:AAA03732.1; !1PID:g216114 REFERENCE A36077 !$#authors Goodrich-Blair, H.; Scarlato, V.; Gott, J.M.; Xu, M.Q.; !1Shub, D.A. !$#journal Cell (1990) 63:417-424 !$#title A self-splicing group I intron in the DNA polymerase gene of !1Bacillus subtilis bacteriophage SPO1. !$#cross-references MUID:91004249; PMID:2119891 !$#accession B36077 !'##molecule_type DNA !'##residues 552-642 ##label GOO !'##cross-references GB:M37686 CLASSIFICATION #superfamily DNA-directed DNA polymerase I KEYWORDS DNA binding; DNA biosynthesis; DNA replication; !1nucleotidyltransferase SUMMARY #length 924 #molecular-weight 106808 #checksum 2702 SEQUENCE /// ENTRY A32686 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) precursor, mitochondrial - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein O6234; protein YOR330c ORGANISM #formal_name Saccharomyces cerevisiae DATE 22-Jan-1993 #sequence_revision 17-May-1996 #text_change 16-Jun-2000 ACCESSIONS S62062; A32686; S61955; S67237; S71970 REFERENCE S62058 !$#authors Parle, A.G.; Hand, N.J.; Goulding, S.G.; Wolfe, K.H. !$#submission submitted to the EMBL Data Library, June 1995 !$#description Sequence of 29 kilobases around the PDR10 locus on the right !1arm of Saccharomyces cerevisiae chromosome XV: similarity to !1part of chromosome I. !$#accession S62062 !'##molecule_type DNA !'##residues 1-1254 ##label PAR !'##cross-references EMBL:Z49821; NID:g1163062; PIDN:CAA89977.1; !1PID:g1163066 REFERENCE A32686 !$#authors Foury, F. !$#journal J. Biol. Chem. (1989) 264:20552-20560 !$#title Cloning and sequencing of the nuclear gene MIP1 encoding the !1catalytic subunit of the yeast mitochondrial DNA polymerase. !$#cross-references MUID:90062193; PMID:2684980 !$#accession A32686 !'##molecule_type DNA !'##residues 1-7,'F',9-34,'A',36-89,'N',91-128,'Q',130-221,'V',223-340, !1'A',342-356,'K',358-539,'MN',542-615,'N',617-660,'T', !1662-824,'S',826-977,'P',979-985,'S',987-1025,'E',1027-1055, !1'S',1057-1206,'T',1208-1254 ##label FOU !'##cross-references GB:J05117 REFERENCE S61955 !$#authors Song, J.M.; Cheung, E.; Rabinowitz, J.C. !$#submission submitted to the EMBL Data Library, December 1995 !$#description Cloning and characterization of the Saccharomyces cerevisiae !1FTB1 gene. !$#accession S61955 !'##molecule_type DNA !'##residues 987-1254 ##label SON !'##cross-references EMBL:U42227; NID:g1147766; PIDN:AAA85442.1; !1PID:g1147767 REFERENCE S67233 !$#authors Goulding, S.E.; Hand, N.J.; Parle-McDermott, A.G.; Wolfe, !1K.H. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67237 !'##molecule_type DNA !'##residues 'MDYERTVLKKRSRWGLYVVVEQRGTS',1-1254 ##label GOU !'##cross-references EMBL:Z75238; NID:g1420720; PIDN:CAA99652.1; !1PID:g1420721; GSPDB:GN00015; MIPS:YOR330c !'##experimental_source strain S288C REFERENCE S71966 !$#authors Parle-McDermott, A.G.; Hand, N.J.; Goulding, S.E.; Wolfe, !1K.H. !$#journal Yeast (1996) 12:999-1004 !$#title Sequence of 29 kb around the PDR10 locus on the right arm of !1Saccharomyces cerevisiae chromosome XV: similarity to part !1of chromosome I. !$#cross-references MUID:97051586; PMID:8896263 !$#accession S71970 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1254 ##label PAW !'##cross-references EMBL:Z49821; NID:g1163062; PIDN:CAA89977.1; !1PID:g1163066 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1995 GENETICS !$#gene SGD:MIP1; MIPS:YOR330c !'##cross-references SGD:S0005857; MIPS:YOR330c !$#map_position 15R !$#genome nuclear CLASSIFICATION #superfamily DNA-directed DNA polymerase, mitochondrial KEYWORDS DNA binding; magnesium; mitochondrion; !1nucleotidyltransferase SUMMARY #length 1254 #molecular-weight 143501 #checksum 7981 SEQUENCE /// ENTRY G02434 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) epsilon catalytic chain A [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 20-Apr-2000 ACCESSIONS G02434; A46692 REFERENCE H01252 !$#authors Asahara, H.; Goldsmith, J.S.; Lee, E.; Linn, S. !$#submission submitted to the EMBL Data Library, February 1996 !$#accession G02434 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-2285 ##label ASA !'##cross-references EMBL:U49356; NID:g1206034; PIDN:AAA90924.1; !1PID:g1206035 REFERENCE A46692 !$#authors Kesti, T.; Frantti, H.; Syvaoja, J.E. !$#journal J. Biol. Chem. (1993) 268:10238-10245 !$#title Molecular cloning of the cDNA for the catalytic subunit of !1human DNA polymerase epsilon. !$#cross-references MUID:93252906; PMID:8486689 !$#accession A46692 !'##status preliminary !'##molecule_type mRNA !'##residues 1-68,96-441,'T',444,'AGS',448-1081,'NA',1084-1297,'E', !11299-1371,'P',1373-1518,'TD',1521-2235,'T',2237-2285 ##label !1KES !'##cross-references EMBL:S60080; GB:L09561; NID:g303156; !1PIDN:AAA15448.1; PID:g303157 !'##experimental_source HeLa cells !'##note sequence inconsistent with the nucleotide translation !'##note sequence extracted from NCBI backbone (NCBIN:131270, !1NCBIP:131271) GENETICS !$#gene GDB:POLE !'##cross-references GDB:129548; OMIM:174762 !$#map_position 12q24.3-12q24.3 CLASSIFICATION #superfamily DNA-directed DNA polymerase II KEYWORDS DNA binding; nucleotidyltransferase SUMMARY #length 2285 #molecular-weight 261389 #checksum 9914 SEQUENCE /// ENTRY A36028 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) II catalytic chain - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES DNA-directed DNA polymerase II chain A; protein N0825; protein YNL262w ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A36028; B36028; S60919; S63235; S65121 REFERENCE A36028 !$#authors Morrison, A.; Araki, H.; Clark, A.B.; Hamatake, R.K.; !1Sugino, A. !$#journal Cell (1990) 62:1143-1151 !$#title A third essential DNA polymerase in Saccharomyces !1cerevisiae. !$#cross-references MUID:90381771; PMID:2169349 !$#accession A36028 !'##molecule_type DNA !'##residues 1-2222 ##label MOR !'##cross-references GB:M60416; GB:M36724; NID:g171408; PIDN:AAA88711.1; !1PID:g171409 !$#accession B36028 !'##molecule_type protein !'##residues 1214-1216,'X',1218-1221 ##label MO2 REFERENCE S60909 !$#authors Sen-Gupta, M.; Lyck, R.; Fleig, U.; Niedenthal, R.N.; !1Hegemann, J.M. !$#submission submitted to the EMBL Data Library, October 1995 !$#description The sequence of a 24152 bp segment from the left arm of !1chromosome XIV from Saccharomyces cerevisiae between the !1BNI1 and the POL2 genes. !$#accession S60919 !'##molecule_type DNA !'##residues 1-2221 ##label SEN !'##cross-references EMBL:X92494; NID:g1045236; PIDN:CAA63235.1; !1PID:g1045247 REFERENCE S63235 !$#authors Sen-Gupta, M.; Lyck, R.; Niedenthal, R.K.; Fleig, U.N.; !1Hegemann, J.H. !$#submission submitted to the Protein Sequence Database, April 1996 !$#accession S63235 !'##molecule_type DNA !'##residues 1-2222 ##label SEW !'##cross-references EMBL:Z71538; NID:g1302316; PIDN:CAA96169.1; !1PID:g1302317; GSPDB:GN00014; MIPS:YNL262w !'##experimental_source strain S288C REFERENCE S65111 !$#authors Sen-Gupta, M.; Lyck, R.; Fleig, U.; Niedenthal, R.K.; !1Hegemann, J.H. !$#journal Yeast (1996) 12:505-514 !$#title The sequence of a 24 152 bp segment from the left arm of !1chromosome XIV from Saccharomyces cerevisiae between the !1BNI1 and the POL2 genes. !$#cross-references MUID:96310631; PMID:8740425 !$#accession S65121 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-2221 ##label SEF !'##cross-references EMBL:X92494; NID:g1045236; PIDN:CAA63235.1; !1PID:g1045247 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1995 GENETICS !$#gene SGD:POL2; DUN2; MIPS:YNL262w !'##cross-references SGD:S0005206; MIPS:YNL262w !$#map_position 14L CLASSIFICATION #superfamily DNA-directed DNA polymerase II KEYWORDS DNA binding; nucleotidyltransferase; nucleus; zinc finger SUMMARY #length 2222 #molecular-weight 255669 #checksum 2572 SEQUENCE /// ENTRY S59833 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) II chain B - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES DNA polymerase epsilon chain B; protein P9705.7; protein YPR175w ORGANISM #formal_name Saccharomyces cerevisiae DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 21-Jul-2000 ACCESSIONS S59833; A39698 REFERENCE S59829 !$#authors Pauley, A. !$#submission submitted to the EMBL Data Library, April 1995 !$#description The sequence of S. cerevisiae cosmid 9705. !$#accession S59833 !'##molecule_type DNA !'##residues 1-692 ##label PAU !'##cross-references EMBL:U25842; NID:g786312; PIDN:AAB68109.1; !1PID:g786319; GSPDB:GN00016; MIPS:YPR175w REFERENCE A39698 !$#authors Araki, H.; Hamatake, R.K.; Johnston, L.H.; Sugino, A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:4601-4605 !$#title DPB2, the gene encoding DNA polymerase II subunit B, is !1required for chromosome replication in Saccharomyces !1cerevisiae. !$#cross-references MUID:91271241; PMID:2052544 !$#accession A39698 !'##molecule_type DNA !'##residues 'MELEAS',1-460,'Y',462-523,'R',525-567,'F',569-586,'Q', !1588-646,'I',648-692 ##label ARA !'##cross-references GB:M61710; NID:g171411; PIDN:AAA34576.1; !1PID:g171412 GENETICS !$#gene SGD:DPB2; MIPS:YPR175w !'##cross-references SGD:S0006379; MIPS:YPR175w !$#map_position 16R CLASSIFICATION #superfamily Saccharomyces cerevisiae DNA-directed DNA !1polymerase II chain B KEYWORDS DNA binding; heteropentamer; nucleotidyltransferase; nucleus SUMMARY #length 692 #molecular-weight 78703 #checksum 7879 SEQUENCE /// ENTRY JDEC22 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) II - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 01-Mar-2002 ACCESSIONS S15943; S19262; S40576; JQ0780; A38840; S19263; S12820; !1B36236; D64727; S54807; S65030; JQ0688; JT0943; JU0325 REFERENCE S15943 !$#authors Iwasaki, H.; Ishino, Y.; Toh, H.; Nakata, A.; Shinagawa, H. !$#journal Mol. Gen. Genet. (1991) 226:24-33 !$#title Escherichia coli DNA polymerase II is homologous to !1alpha-like DNA polymerases. !$#cross-references MUID:91238699; PMID:2034216 !$#accession S15943 !'##molecule_type DNA !'##residues 1-783 ##label IWA !'##cross-references EMBL:X54847; NID:g42462; PIDN:CAA38616.1; !1PID:g581193 !'##experimental_source strain K-12, substrain W3110 !$#accession S19262 !'##molecule_type protein !'##residues 2-9 ##label IWA2 REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40576 !'##status preliminary !'##molecule_type DNA !'##residues 'V',2-783 ##label YUR !'##cross-references EMBL:D10483; NID:g216434 !'##experimental_source strain K-12 REFERENCE JQ0780 !$#authors Bonner, C.A.; Hays, S.; McEntee, K.; Goodman, M.F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:7663-7667 !$#title DNA polymerase II is encoded by the DNA damage-inducible !1dinA gene of Escherichia coli. !$#cross-references MUID:91017565; PMID:2217198 !$#accession JQ0780 !'##molecule_type DNA !'##residues 1-256,'DD',259-271,'G',273-458 ##label BON !'##cross-references GB:M37727; NID:g145744; PIDN:AAA23684.1; !1PID:g145746 !$#accession A38840 !'##molecule_type protein !'##residues 2-9,'XQ',12-21,'H',23,'X',25-28 ##label BO2 REFERENCE S19263 !$#authors Chen, H. !$#submission submitted to the EMBL Data Library, June 1990 !$#accession S19263 !'##molecule_type DNA !'##residues 1-171,'A',173-734,'T',736-739,'PGLPTFTTGLRTLSDPPATTRGG', !1763,'NT',766-767,'Y' ##label CHE !'##cross-references EMBL:M35371; NID:g147319; PIDN:AAA24407.1; !1PID:g147320 REFERENCE S12820 !$#authors Chen, H.; Lawrence, C.B.; Bryan, S.K.; Moses, R.E. !$#journal Nucleic Acids Res. (1990) 18:7185-7186 !$#title Aphidicolin inhibits DNA polymerase II of Escherichia coli, !1an alpha-like DNA polymerase. !$#cross-references MUID:91088346; PMID:2124684 !$#accession S12820 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 90-171,'A',173-734,'T',736-739,'PGLPTFTTGLRTLSDPPATTRGG', !1763,'NT',766-767,'Y' ##label CHE2 !'##cross-references EMBL:M35371 REFERENCE A36236 !$#authors Chen, H.; Sun, Y.; Stark, T.; Beattie, W.; Moses, R.E. !$#journal DNA Cell Biol. (1990) 9:631-635 !$#title Nucleotide sequence and deletion analysis of the polB gene !1of Escherichia coli. !$#cross-references MUID:91083835; PMID:2261080 !$#accession B36236 !'##status preliminary !'##molecule_type DNA !'##residues 'V',2-171,'A',173-734,'T',736-739, !1'PGLPTFTTGLRTLSDPPATTRGG',763,'NT',766-767,'Y' ##label CH2 !'##cross-references GB:M35371 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64727 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-783 ##label BLAT !'##cross-references GB:AE000116; GB:U00096; NID:g1786240; !1PIDN:AAC73171.1; PID:g1786246; UWGP:b0060 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S54807 !$#authors Achhammer, G.J. !$#submission submitted to the EMBL Data Library, May 1995 !$#accession S54807 !'##molecule_type mRNA !'##residues 428-444,'LIQSTVPKV',454,'SMPGSREKNIAY',467-482,'RVTN', !1487-510,'L',512-520,'I',522-548 ##label ACH !'##cross-references EMBL:X87158; NID:g809066; PID:g809067 !'##note the source was identified as Physarum polycephalum; this is !1probably a misassignment !'##note compared to Escherichia coli there is 96% sequence identity at !1the DNA level and 81% sequence identity at the protein !1level; the differences are probably due to frameshift errors REFERENCE S65029 !$#authors Achhammer, G.; Winkler, A.; Angerer, B.; Holler, E. !$#journal Curr. Genet. (1995) 28:534-545 !$#title DNA polymerase delta of Physarum polycephalum. !$#cross-references MUID:96132109; PMID:8593684 !$#accession S65030 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type mRNA !'##residues 428-444,'LIQSTVPKV',454,'SMPGSREKNIAY',467-482,'RVTN', !1487-510,'L',512-520,'I',522-542 ##label ACW !'##cross-references EMBL:X87158 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1May 1995 !'##note the source was identified as Physarum polycephalum; this is !1probably a misassignment !'##note compared to Escherichia coli there is 96% sequence identity at !1the DNA level and 81% sequence identity at the protein !1level; the differences are probably due to frameshift errors GENETICS !$#gene polB !$#map_position 2 min !$#start_codon GTG FUNCTION !$#pathway purine metabolism; pyrimidine metabolism CLASSIFICATION #superfamily Escherichia coli DNA-directed DNA polymerase II KEYWORDS DNA binding; DNA biosynthesis; nucleotidyltransferase FEATURE !$2-783 #product DNA-directed DNA polymerase II #status !8experimental #label MAT SUMMARY #length 783 #molecular-weight 90052 #checksum 2286 SEQUENCE /// ENTRY DJEC3A #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) III alpha chain - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 01-Mar-2002 ACCESSIONS C28390; A37441; A40637; H64742 REFERENCE A91855 !$#authors Tomasiewicz, H.G.; McHenry, C.S. !$#journal J. Bacteriol. (1987) 169:5735-5744 !$#title Sequence analysis of the Escherichia coli dnaE gene. !$#cross-references MUID:88058791; PMID:3316192 !$#accession C28390 !'##molecule_type DNA !'##residues 1-1160 ##label TOM !'##cross-references GB:M19334; GB:M18265; GB:M18266; NID:g450760; !1PIDN:AAC36920.1; PID:g146663 !'##note the nucleotide sequence has been corrected in reference A37441 REFERENCE A37441 !$#authors Tomasiewicz, H.G.; McHenry, C.S. !$#journal J. Bacteriol. (1991) 173:4549 !$#cross-references MUID:91294205; PMID:2066347 !$#contents erratum !$#accession A37441 !'##molecule_type DNA !'##residues 156-183 ##label TO2 !'##cross-references GB:M19334; NID:g450760 REFERENCE A40637 !$#authors Li, S.J.; Cronan Jr., J.E. !$#journal J. Bacteriol. (1993) 175:332-340 !$#title Growth rate regulation of Escherichia coli acetyl coenzyme A !1carboxylase, which catalyzes the first committed step of !1lipid biosynthesis. !$#cross-references MUID:93123150; PMID:7678242 !$#accession A40637 !'##status preliminary !'##molecule_type mRNA !'##residues 1070-1160 ##label LI1 !'##cross-references GB:S52931; NID:g263397; PIDN:AAB24889.1; !1PID:g263398 !'##note sequence extracted from NCBI backbone (NCBIN:122313, !1NCBIP:122314) REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64742 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1160 ##label BLAT !'##cross-references GB:AE000127; GB:U00096; NID:g1786370; !1PIDN:AAC73295.1; PID:g1786381; UWGP:b0184 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene dnaE; polC !$#map_position 4 min COMPLEX DNA polymerase III is a multichain complex; alpha, epsilon, !1theta, tau, gamma, delta, delta', psi, chi and beta chains COMPLEX The pol catalytic core is a heterotrimer containing alpha, !1epsilon and theta chains; the pol III'-complex contains a !1dimer of the catalytic core, plus two tau chains and two !1gamma/delta complex subunits; the holoenzyme contains the !1pol III'-complex plus four beta chains. FUNCTION GEN !$#description synthesizes both the lagging and the leading strands of DNA !$#pathway DNA biosynthesis CLASSIFICATION #superfamily DNA-directed DNA polymerase III alpha chain KEYWORDS DNA biosynthesis; DNA replication; nucleotidyltransferase SUMMARY #length 1160 #molecular-weight 129903 #checksum 8714 SEQUENCE /// ENTRY A45915 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) III alpha chain - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jul-2002 ACCESSIONS A45915 REFERENCE A45915 !$#authors Lancy, E.D.; Lifsics, M.R.; Munson, P.; Maurer, R. !$#journal J. Bacteriol. (1989) 171:5581-5586 !$#title Nucleotide sequence of dnaE, the gene for the polymerase !1subunit of DNA polymerase III in Salmonella typhimurium, and !1a variant that facilitates growth in the absence of another !1polymerase subunit. !$#cross-references MUID:90008797; PMID:2676978 !$#accession A45915 !'##status preliminary; translation not shown !'##molecule_type DNA !'##residues 1-1160 ##label LAN !'##cross-references GB:M29701; NID:g153951; PIDN:AAA27057.1; !1PID:g153952 CLASSIFICATION #superfamily DNA-directed DNA polymerase III alpha chain KEYWORDS hydrolase; nucleotidyltransferase SUMMARY #length 1160 #molecular-weight 130118 #checksum 9028 SEQUENCE /// ENTRY H64089 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) III alpha chain - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS H64089 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession H64089 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1159 ##label TIGR !'##cross-references GB:U32757; GB:L42023; NID:g1573740; !1PIDN:AAC22399.1; PID:g1573746; TIGR:HI0739 CLASSIFICATION #superfamily DNA-directed DNA polymerase III alpha chain KEYWORDS DNA replication; nucleotidyltransferase SUMMARY #length 1159 #molecular-weight 129787 #checksum 9191 SEQUENCE /// ENTRY DJEC3G #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) III gamma/tau chain precursor - Escherichia coli (strain K-12) ALTERNATE_NAMES replication elongation factor II-III CONTAINS DNA-directed DNA polymerase III gamma chain; DNA-directed DNA polymerase III tau chain ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 01-Mar-2002 ACCESSIONS A25549; I41053; E64777 REFERENCE A25549 !$#authors Flower, A.M.; McHenry, C.S. !$#journal Nucleic Acids Res. (1986) 14:8091-8101 !$#title The adjacent dnaZ and dnaX genes of Escherichia coli are !1contained within one continuous open reading frame. !$#cross-references MUID:87040775; PMID:3534795 !$#accession A25549 !'##molecule_type DNA !'##residues 1-643 ##label FLO !'##cross-references GB:M38777; NID:g145295; PIDN:AAA23457.1; !1PID:g145297 REFERENCE I41052 !$#authors Yin, K.C.; Blinkowa, A.; Walker, J.R. !$#journal Nucleic Acids Res. (1986) 14:6541-6549 !$#title Nucleotide sequence of the Escherichia coli replication gene !1dnaZX. !$#cross-references MUID:86312915; PMID:3018672 !$#accession I41053 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-643 ##label RES !'##cross-references EMBL:X04275; NID:g41290; PIDN:CAA27827.1; !1PID:g41291 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64777 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-643 ##label BLAT !'##cross-references GB:AE000153; GB:U00096; NID:g1786671; !1PIDN:AAC73572.1; PID:g1786676; UWGP:b0470 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene dnaX; dnaZX !$#map_position 10.4 min COMPLEX DNA polymerase III is a multichain complex; alpha, epsilon, !1theta, tau, gamma, delta, delta', psi, chi and beta chains FUNCTION GEN !$#description DNA synthesis; synthesizes both, the lagging and the leading !1strands in E.coli !$#pathway DNA biosynthesis !$#note core enzyme (catalytic core) contains chains alpha, epsilon !1and theta; alpha chain has basic ability to synthesize DNA, !1epsilon chain has 3'-5' proofreading exonuclease and theta !1chain may be required for assembly; tau allows dimerization !1of the core complex and processivity is increased; the !1addition of the gamma/delta complex generates Pol !1III'-complex; gamma/delta complex binds template; the !1holoenzyme is completed by addition of beta chain which !1clamps the enzyme to DNA FUNCTION TAU !$#description tau chain causes the core to dimerize !$#note tau chain is a full length product of the dnaXZ gene FUNCTION GAM !$#description gamma chain appears to interact with the delta chain; binds !1ATP; gamma/delta complex is composed of chains gamma, delta, !1delta', psi and chi !$#note gamma chain is produced by a programmed ribosomal !1frameshifting CLASSIFICATION #superfamily DNA-directed DNA polymerase III gamma chain KEYWORDS ATP; DNA biosynthesis; DNA replication; nucleotide binding; !1nucleotidyltransferase; P-loop FEATURE !$1-643 #product DNA-directed DNA polymerase III tau chain !8#status predicted #label MAT1\ !$1-431 #product DNA-directed DNA polymerase III gamma chain !8#status predicted #label MAT2\ !$45-52 #region nucleotide-binding motif A (P-loop)\ !$122-126 #region nucleotide-binding motif B SUMMARY #length 643 #molecular-weight 71137 #checksum 9819 SEQUENCE /// ENTRY B69054 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) delta small chain - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 05-Dec-1997 #sequence_revision 05-Dec-1997 #text_change 11-Jun-1999 ACCESSIONS B69054 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession B69054 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-482 ##label MTH !'##cross-references GB:AE000903; GB:AE000666; NID:g2622514; !1PIDN:AAB85882.1; PID:g2622517 !'##experimental_source strain Delta H GENETICS !$#gene MTH1405 CLASSIFICATION #superfamily DNA-directed DNA polymerase delta small chain; !1phosphoesterase core homology KEYWORDS metalloprotein; nucleotidyltransferase FEATURE !$223-321 #domain phosphoesterase core homology #label PEC SUMMARY #length 482 #molecular-weight 54375 #checksum 3013 SEQUENCE /// ENTRY E69473 #type complete TITLE probable DNA-directed DNA polymerase (EC 2.7.7.7) delta small chain - Archaeoglobus fulgidus ALTERNATE_NAMES conserved hypothetical protein AF1790 ORGANISM #formal_name Archaeoglobus fulgidus DATE 05-Dec-1997 #sequence_revision 05-Dec-1997 #text_change 11-Jun-1999 ACCESSIONS E69473 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession E69473 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-488 ##label KLE !'##cross-references GB:AE000979; GB:AE000782; NID:g2689302; !1PIDN:AAB89458.1; PID:g2648756; TIGR:AF1790 CLASSIFICATION #superfamily DNA-directed DNA polymerase delta small chain; !1phosphoesterase core homology KEYWORDS metalloprotein; nucleotidyltransferase FEATURE !$228-326 #domain phosphoesterase core homology #label PEC SUMMARY #length 488 #molecular-weight 54585 #checksum 4487 SEQUENCE /// ENTRY F64387 #type complete TITLE probable DNA-directed DNA polymerase (EC 2.7.7.7) delta small chain - Methanococcus jannaschii ALTERNATE_NAMES hypothetical protein MJ0702 ORGANISM #formal_name Methanococcus jannaschii DATE 13-Sep-1996 #sequence_revision 13-Sep-1996 #text_change 21-Jul-2000 ACCESSIONS F64387 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession F64387 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-594 ##label BUL !'##cross-references GB:U67516; GB:L77117; NID:g2826307; !1PIDN:AAB98694.1; PID:g1591417; TIGR:MJ0702 GENETICS !$#map_position FOR628052-629836 CLASSIFICATION #superfamily DNA-directed DNA polymerase delta small chain; !1phosphoesterase core homology KEYWORDS metalloprotein; nucleotidyltransferase FEATURE !$324-422 #domain phosphoesterase core homology #label PEC SUMMARY #length 594 #molecular-weight 69145 #checksum 9530 SEQUENCE /// ENTRY A71233 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) small chain PH0123 [similarity] - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 14-Dec-2001 ACCESSIONS A71233 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession A71233 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-622 ##label KAW !'##cross-references GB:AP000001; NID:g3236128; PIDN:BAA29192.1; !1PID:g3256509 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0123 CLASSIFICATION #superfamily DNA-directed DNA polymerase delta small chain; !1phosphoesterase core homology KEYWORDS metalloprotein; nucleotidyltransferase FEATURE !$358-455 #domain phosphoesterase core homology #label PEC SUMMARY #length 622 #molecular-weight 70283 #checksum 2617 SEQUENCE /// ENTRY DJEC3B #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) III beta chain - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 28-Aug-1985 #sequence_revision 31-Mar-1988 #text_change 01-Mar-2002 ACCESSIONS A91510; A93996; A22168; I41190; I54000; F65172; A00719; !1B24944 REFERENCE A91510 !$#authors Ohmori, H.; Kimura, M.; Nagata, T.; Sakakibara, Y. !$#journal Gene (1984) 28:159-170 !$#title Structural analysis of the dnaA and dnaN genes of !1Escherichia coli. !$#cross-references MUID:84237568; PMID:6234204 !$#accession A91510 !'##molecule_type DNA !'##residues 1-366 ##label OHM !'##cross-references GB:J01602; NID:g145758; PIDN:AAB59150.1; !1PID:g145761 !'##experimental_source strain K-12 REFERENCE A93996 !$#authors Blanar, M.A.; Sandler, S.J.; Armengod, M.E.; Ream, L.W.; !1Clark, A.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:4622-4626 !$#title Molecular analysis of the recF gene of Escherichia coli. !$#cross-references MUID:84272685; PMID:6379647 !$#accession A93996 !'##molecule_type DNA !'##residues 297-366 ##label BLA !'##cross-references GB:K02179; NID:g147537; PIDN:AAA24510.1; !1PID:g147538 REFERENCE A22168 !$#authors Adachi, T.; Mizuuchi, K.; Menzel, R.; Gellert, M. !$#journal Nucleic Acids Res. (1984) 12:6389-6395 !$#title DNA sequence and transcription of the region upstream of the !1E. coli gyrB gene. !$#cross-references MUID:84297235; PMID:6089112 !$#accession A22168 !'##status preliminary !'##molecule_type DNA !'##residues 342-366 ##label ADA !'##cross-references GB:X04341; GB:X00870; NID:g41643; PIDN:CAA27869.1; !1PID:g41644 !'##experimental_source strain K-12 REFERENCE I41190 !$#authors Armengod, M. !$#journal J. Biol. Chem. (1988) 263:12109-12114 !$#title Transcriptional Organization of the dnaN and recF Genes of !1Escherichia coli K-12. !$#cross-references MUID:88298898; PMID:2841344 !$#accession I41190 !'##status preliminary !'##molecule_type DNA !'##residues 1-14 ##label RES !'##cross-references GB:M19876; NID:g145779; PIDN:AAA23695.1; !1PID:g551800 REFERENCE I54000 !$#authors Armengod, M. !$#journal Gene (1986) 43:183-196 !$#title Overlapping arrangement of the recF and dnaN operons of !1Escherichia coli; Positive and negative control sequences. !$#cross-references MUID:86301872; PMID:3527871 !$#accession I54000 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 143-170 ##label RE2 !'##cross-references GB:M13822; NID:g147541; PIDN:AAA24512.1; !1PID:g147542 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65172 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-366 ##label BLAT !'##cross-references GB:AE000447; GB:U00096; NID:g2367266; !1PIDN:AAC76724.1; PID:g1790136; UWGP:b3701 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene dnaN !$#map_position 83 min COMPLEX DNA polymerase III is a multichain complex; alpha, epsilon, !1theta, tau, gamma, delta, delta', psi, chi and beta chains FUNCTION GEN !$#description DNA synthesis; synthesizes both, the lagging and the leading !1strands in E.coli !$#pathway DNA biosynthesis !$#note core enzyme (catalytic core) contains chains alpha, epsilon !1and theta; alpha chain has basic ability to synthesize DNA, !1epsilon chain has 3'-5' proofreading exonuclease and theta !1chain may be required for assembly; tau allows dimerization !1of the core complex and processivity is increased; the !1addition of the gamma/delta complex generates Pol !1III'-complex; gamma/delta complex binds template; the !1holoenzyme is completed by addition of beta chain which !1clamps the enzyme to DNA FUNCTION BET !$#description beta chain is required for initiation of replication !$#note can slide along duplex DNA bidirectionaly and !1ATP-independent; binds core; crystal structure: forms a !1ring-shaped dimer ('sliding clamp') CLASSIFICATION #superfamily DNA-directed DNA polymerase III beta chain KEYWORDS DNA replication initiation; nucleotidyltransferase SUMMARY #length 366 #molecular-weight 40586 #checksum 9121 SEQUENCE /// ENTRY JQ0734 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) III beta chain - Proteus mirabilis ORGANISM #formal_name Proteus mirabilis DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 11-Jun-1999 ACCESSIONS JQ0734 REFERENCE JQ0729 !$#authors Skovgaard, O. !$#journal Gene (1990) 93:27-34 !$#title Nucleotide sequence of a Proteus mirabilis DNA fragment !1homologous to the 60K-rnpA-rpmH-dnaA-dnaN-recF-gyrB region !1of Escherichia coli. !$#cross-references MUID:91033012; PMID:2172087 !$#accession JQ0734 !'##molecule_type DNA !'##residues 1-367 ##label SKO !'##cross-references GB:M58352; GB:M31295; NID:g150873; PIDN:AAA83959.1; !1PID:g150879 !'##experimental_source strain LM1509 GENETICS !$#gene dnaN CLASSIFICATION #superfamily DNA-directed DNA polymerase III beta chain KEYWORDS DNA replication initiation; nucleotidyltransferase SUMMARY #length 367 #molecular-weight 40747 #checksum 4642 SEQUENCE /// ENTRY DJPS3P #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) III beta chain - Pseudomonas putida ORGANISM #formal_name Pseudomonas putida DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 11-Jun-1999 ACCESSIONS JV0002 REFERENCE JV0002 !$#authors Fujita, M.Q.; Yoshikawa, H.; Ogasawara, N. !$#journal Mol. Gen. Genet. (1989) 215:381-387 !$#title Structure of the dnaA region of Pseudomonas putida: !1conservation among three bacteria, Bacillus subtilis, !1Escherichia coli and P. putida. !$#cross-references MUID:89218947; PMID:2540413 !$#accession JV0002 !'##molecule_type DNA !'##residues 1-367 ##label FUJ !'##cross-references GB:X14791; NID:g45689; PIDN:CAA32894.1; PID:g45691 GENETICS !$#gene dnaN CLASSIFICATION #superfamily DNA-directed DNA polymerase III beta chain KEYWORDS DNA replication initiation; nucleotidyltransferase SUMMARY #length 367 #molecular-weight 40718 #checksum 471 SEQUENCE /// ENTRY A64107 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) III beta chain - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 18-Aug-1995 #sequence_revision 16-Aug-1996 #text_change 11-Jun-1999 ACCESSIONS A64107 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession A64107 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-366 ##label TIGR !'##cross-references GB:U32780; GB:L42023; NID:g1574020; !1PIDN:AAC22654.1; PID:g1574022; TIGR:HI0992 GENETICS !$#gene dnaN CLASSIFICATION #superfamily DNA-directed DNA polymerase III beta chain KEYWORDS DNA replication initiation; nucleotidyltransferase SUMMARY #length 366 #molecular-weight 41631 #checksum 3967 SEQUENCE /// ENTRY JC1159 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) III beta chain - Buchnera aphidicola ORGANISM #formal_name Buchnera aphidicola DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 11-Jun-1999 ACCESSIONS JC1159 REFERENCE JC1154 !$#authors Lai, C.Y.; Baumann, P. !$#journal Gene (1992) 113:175-181 !$#title Genetic analysis of an aphid endosymbiont DNA fragment !1homologous to the rnpA-rpmH-dnaA-dnaN-gyrB region of !1eubacteria. !$#cross-references MUID:92241666; PMID:1572539 !$#accession JC1159 !'##molecule_type DNA !'##residues 1-366 ##label LAI !'##cross-references GB:M80817; NID:g144144; PIDN:AAA73150.1; !1PID:g144150 GENETICS !$#gene dnaN CLASSIFICATION #superfamily DNA-directed DNA polymerase III beta chain KEYWORDS DNA replication initiation; nucleotidyltransferase SUMMARY #length 366 #molecular-weight 42180 #checksum 9766 SEQUENCE /// ENTRY B22930 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) III beta chain dnaN - Bacillus subtilis ALTERNATE_NAMES 42K protein (oriC region) ORGANISM #formal_name Bacillus subtilis DATE 21-May-1988 #sequence_revision 16-Aug-1996 #text_change 16-Jun-2000 ACCESSIONS B22930; S66032; I40393; A69618 REFERENCE A94702 !$#authors Moriya, S.; Ogasawara, N.; Yoshikawa, H. !$#journal Nucleic Acids Res. (1985) 13:2251-2265 !$#title Structure and function of the region of the replication !1origin of the Bacillus subtilis chromosome. III. Nucleotide !1sequence of some 10,000 base pairs in the origin region. !$#cross-references MUID:85215612; PMID:2987847 !$#accession B22930 !'##molecule_type DNA !'##residues 1-378 ##label MOR !'##cross-references GB:D26185; NID:g467326; PIDN:BAA05238.1; !1PID:g467392 REFERENCE A26057 !$#authors Ogasawara, N.; Moriya, S.; von Meyenburg, K.; Hansen, F.G.; !1Yoshikawa, H. !$#journal EMBO J. (1985) 4:3345-3350 !$#title Conservation of genes and their organization in the !1chromosomal replication origin region of Bacillus subtilis !1and Escherichia coli. !$#cross-references MUID:86135970; PMID:3004954 !$#contents annotation REFERENCE S65967 !$#authors Ogasawara, N.; Nakai, S.; Yoshikawa, H. !$#journal DNA Res. (1994) 1:1-14 !$#title Systematic sequencing of the 180 kilobase region of the !1Bacillus subtilis chromosome containing the replication !1origin. !$#cross-references MUID:96051385; PMID:7584024 !$#accession S66032 !'##status preliminary !'##molecule_type DNA !'##residues 1-378 ##label OGA !'##cross-references EMBL:D26185; NID:g467326; PIDN:BAA05238.1; !1PID:g467392 REFERENCE I40391 !$#authors Moriya, S.; Fukuoka, T.; Ogasawara, N.; Yoshikawa, H. !$#journal EMBO J. (1988) 7:2911-2917 !$#title Regulation of initiation of the chromosomal replication by !1DnaA-boxes in the origin region of the Bacillus subtilis !1chromosome. !$#cross-references MUID:89030659; PMID:2846289 !$#accession I40393 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-30 ##label RES !'##cross-references EMBL:X12779; NID:g39878; PIDN:CAA31271.1; !1PID:g39879 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69618 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-378 ##label KUN !'##cross-references GB:Z99104; GB:AL009126; NID:g2632267; !1PIDN:CAB11778.1; PID:g2632269 !'##experimental_source strain 168 GENETICS !$#gene dnaN !$#map_position 0 CLASSIFICATION #superfamily DNA-directed DNA polymerase III beta chain KEYWORDS DNA replication initiation; nucleotidyltransferase SUMMARY #length 378 #molecular-weight 42103 #checksum 9031 SEQUENCE /// ENTRY S54708 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) III beta chain - Staphylococcus aureus ALTERNATE_NAMES dnaN ORGANISM #formal_name Staphylococcus aureus DATE 23-Aug-1995 #sequence_revision 16-Aug-1996 #text_change 16-Aug-1996 ACCESSIONS S54708 REFERENCE S54707 !$#authors Alonso, J.C.; Fisher, L.M. !$#journal Mol. Gen. Genet. (1995) 246:680-686 !$#title Nucleotide sequence of the recF gene cluster from !1Staphylococcus aureus and complementation analysis in !1Bacillus subtilis recF mutants. !$#cross-references MUID:95206242; PMID:7898435 !$#accession S54708 !'##molecule_type DNA !'##residues 1-377 ##label ALO GENETICS !$#gene dnaN CLASSIFICATION #superfamily DNA-directed DNA polymerase III beta chain KEYWORDS DNA replication initiation; nucleotidyltransferase SUMMARY #length 377 #molecular-weight 41913 #checksum 524 SEQUENCE /// ENTRY S35733 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) III beta chain - Spiroplasma citri ALTERNATE_NAMES dnaN ORGANISM #formal_name Spiroplasma citri DATE 13-Jan-1995 #sequence_revision 16-Aug-1996 #text_change 07-Dec-1999 ACCESSIONS S35733 REFERENCE S35732 !$#authors Ye, F.; Laigret, F.; Bove, J. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Nucleotide sequence and genetic organization at the !1replication origin (oriC) region of Spiroplasma citri. !$#accession S35733 !'##molecule_type DNA !'##residues 1-363 ##label YEF !'##cross-references EMBL:Z19108; NID:g49345; PIDN:CAA79522.1; !1PID:g49347 GENETICS !$#gene dnaN !$#genetic_code SGC3 CLASSIFICATION #superfamily DNA-directed DNA polymerase III beta chain KEYWORDS DNA replication initiation; nucleotidyltransferase SUMMARY #length 363 #molecular-weight 41329 #checksum 2105 SEQUENCE /// ENTRY JN0277 #type fragment TITLE DNA-directed DNA polymerase (EC 2.7.7.7) III beta chain - Mycoplasma capricolum (fragment) ORGANISM #formal_name Mycoplasma capricolum DATE 17-Aug-1992 #sequence_revision 16-Aug-1996 #text_change 16-Jun-2000 ACCESSIONS JN0277; PS0193 REFERENCE JN0272 !$#authors Fujita, M.Q.; Yoshikawa, H.; Ogasawara, N. !$#journal Gene (1992) 110:17-23 !$#title Structure of the dnaA and DnaA-box region in the Mycoplasma !1capricolum chromosome: conservation and variations in the !1course of evolution. !$#cross-references MUID:92184110; PMID:1544573 !$#accession JN0277 !'##molecule_type DNA !'##residues 1-210 ##label FUJ !'##cross-references DDBJ:D90426; NID:g216793; PIDN:BAA14416.1; !1PID:g216796 GENETICS !$#gene dnaN !$#genetic_code SGC3 CLASSIFICATION #superfamily DNA-directed DNA polymerase III beta chain KEYWORDS DNA replication initiation; nucleotidyltransferase SUMMARY #length 210 #checksum 178 SEQUENCE /// ENTRY A48647 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) III psi chain - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS A48647; B46739; S56596; C65252 REFERENCE A48647 !$#authors Carter, J.R.; Franden, M.A.; Aebersold, R.; McHenry, C.S. !$#journal J. Bacteriol. (1993) 175:5604-5610 !$#title Identification, isolation, and overexpression of the gene !1encoding the psi subunit of DNA polymerase III holoenzyme. !$#cross-references MUID:93374856; PMID:8366044 !$#accession A48647 !'##status preliminary !'##molecule_type DNA !'##residues 1-137 ##label CAR !'##cross-references GB:L05387; NID:g146389; PIDN:AAA03076.1; !1PID:g146390 REFERENCE A46739 !$#authors Xiao, H.; Crombie, R.; Dong, Z.; Onrust, R.; O'Donnell, M. !$#journal J. Biol. Chem. (1993) 268:11773-11778 !$#title DNA polymerase III accessory proteins. III. holC and holD !1encoding chi and psi. !$#cross-references MUID:93280138; PMID:8389364 !$#accession B46739 !'##status preliminary !'##molecule_type DNA !'##residues 1-137 ##label XIA !'##cross-references GB:L04575; NID:g147386; PIDN:AAA24435.1; !1PID:g147387 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56596 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-137 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97268.1; !1PID:g537212 !'##experimental_source strain K-12, substrain MG1655 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65252 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-137 ##label BLAT !'##cross-references GB:AE000507; GB:U00096; NID:g2367380; !1PIDN:AAC77325.1; PID:g1790831; UWGP:b4372 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene holD COMPLEX DNA polymerase III is a multichain complex; alpha, epsilon, !1theta, tau, gamma, delta, delta', psi, chi and beta chains; !1the gamma/delta subcomplex is composed of chains gamma, !1delta, delta', psi and chi FUNCTION GEN !$#description DNA synthesis; synthesizes both, the lagging and the leading !1strands in E.coli !$#pathway DNA biosynthesis !$#note core enzyme (catalytic core) contains chains alpha, epsilon !1and theta; alpha chain has basic ability to synthesize DNA, !1epsilon chain has 3'-5' proofreading exonuclease and theta !1chain may be required for assembly; tau allows dimerization !1of the core complex and processivity is increased; the !1addition of the gamma/delta complex generates Pol !1III'-complex; gamma/delta complex binds template; the !1holoenzyme is completed by addition of beta chain which !1clamps the enzyme to DNA CLASSIFICATION #superfamily DNA-directed DNA polymerase III psi chain KEYWORDS DNA biosynthesis; DNA replication; nucleotidyltransferase SUMMARY #length 137 #molecular-weight 15174 #checksum 2468 SEQUENCE /// ENTRY S05362 #type complete TITLE probable DNA-directed DNA polymerase (EC 2.7.7.7) - fungus (Ascobolus immersus) mitochondrion plasmid pAI2 ORGANISM #formal_name mitochondrion Ascobolus immersus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S05362 REFERENCE S05362 !$#authors Kempken, F.; Meinhardt, F.; Esser, K. !$#journal Mol. Gen. Genet. (1989) 218:523-530 !$#title In organello replication and viral affinity of linear, !1extrachromosomal DNA of the ascomycete Ascobolus immersus. !$#cross-references MUID:90066356; PMID:2573821 !$#accession S05362 !'##molecule_type DNA !'##residues 1-1202 ##label KEM !'##cross-references EMBL:X15982; NID:g2933; PIDN:CAA34106.1; !1PID:g1370212 GENETICS !$#genome mitochondrion !$#genetic_code SGC3 CLASSIFICATION #superfamily Ascolobus probable DNA-directed DNA polymerase KEYWORDS DNA binding; mitochondrion; nucleotidyltransferase SUMMARY #length 1202 #molecular-weight 138279 #checksum 8777 SEQUENCE /// ENTRY XNPOU #type complete TITLE UTP-glucose-1-phosphate uridylyltransferase (EC 2.7.7.9) - potato ORGANISM #formal_name Solanum tuberosum #common_name potato DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Jun-2002 ACCESSIONS JX0128 REFERENCE JX0128 !$#authors Katsube, T.; Kazuta, Y.; Mori, H.; Nakano, K.; Tanizawa, K.; !1Fukui, T. !$#journal J. Biochem. (1990) 108:321-326 !$#title UDP-glucose pyrophosphorylase from potato tuber: cDNA !1cloning and sequencing. !$#cross-references MUID:91035366; PMID:2229031 !$#accession JX0128 !'##molecule_type DNA !'##residues 1-477 ##label KAT !'##cross-references GB:D00667; NID:g218000; PIDN:BAA00570.1; !1PID:g218001 COMMENT This enzyme catalyzes alpha-D-glucose-1-phosphate and !1nucleoside triphosphates to form nucleotide sugars. It plays !1a central role as a glucosyl donor in cellular metabolic !1pathways. CLASSIFICATION #superfamily UTP-glucose-1-phosphate uridylyltransferase KEYWORDS nucleotidyltransferase SUMMARY #length 477 #molecular-weight 51873 #checksum 7188 SEQUENCE /// ENTRY JC4785 #type complete TITLE UTP-glucose-1-phosphate uridylyltransferase (EC 2.7.7.9) - barley ORGANISM #formal_name Hordeum vulgare #common_name barley DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS JC4785 REFERENCE JC4785 !$#authors Eimert, K.; Villand, P.; Kilian, A.; Kleczkowski, L.A. !$#journal Gene (1996) 170:227-232 !$#title Cloning and characterization of several cDNAs for !1UDP-glucose pyrophosphorylase from barley (Hordeum vulgare) !1tissues. !$#cross-references MUID:96235140; PMID:8666250 !$#accession JC4785 !'##molecule_type mRNA !'##residues 1-473 ##label EIM !'##cross-references EMBL:X91347; NID:g1212995; PIDN:CAA62689.1; !1PID:g1212996 !'##experimental_source seed embryo !'##note UDP-glucose pyrophosphorylase; Glucose-1-phosphate !1uridylytransferase COMMENT This enzyme is a cytosolic soluble protein. It is !1responsible for sythesis and pyrophosphorolysis of !1UDP-glucose. GENETICS !$#gene ue24 CLASSIFICATION #superfamily UTP-glucose-1-phosphate uridylyltransferase KEYWORDS embryo; nucleotidyltransferase; seed SUMMARY #length 473 #molecular-weight 51644 #checksum 2900 SEQUENCE /// ENTRY S30007 #type complete TITLE probable UTP-glucose-1-phosphate uridylyltransferase (EC 2.7.7.9) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein YKL035w; probable UDP-glucose pyrophosphorylase; protein YKL248 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S30007; S37856 REFERENCE S30007 !$#authors Purnelle, B.; Skala, J.; van Dyck, L.; Goffeau, A. !$#journal Yeast (1992) 8:977-986 !$#title The sequence of a 12 kb fragment on the left arm of yeast !1chromosome XI reveals five new open reading frames, !1including a zinc finger protein and a homolog of the !1UDP-glucose pyrophosphorylase from potato. !$#cross-references MUID:93127731; PMID:1481573 !$#accession S30007 !'##molecule_type DNA !'##residues 1-499 ##label PUR !'##cross-references EMBL:X69584; NID:g4789; PIDN:CAA49303.1; PID:g4794 !'##experimental_source strain S288C REFERENCE S37851 !$#authors Purnelle, B.; Skala, J.; van Dyck, L.; Tettelin, H.; !1Goffeau, A. !$#submission submitted to the Protein Sequence Database, March 1994 !$#accession S37856 !'##molecule_type DNA !'##residues 1-499 ##label PU2 !'##cross-references EMBL:Z28035; NID:g486037; PIDN:CAA81872.1; !1PID:g486040; GSPDB:GN00011; MIPS:YKL035w !'##experimental_source strain S288C GENETICS !$#gene SGD:UGP1; MIPS:YKL035w !'##cross-references SGD:S0001518 !$#map_position 11L CLASSIFICATION #superfamily UTP-glucose-1-phosphate uridylyltransferase KEYWORDS nucleotidyltransferase SUMMARY #length 499 #molecular-weight 55987 #checksum 7868 SEQUENCE /// ENTRY S62599 #type complete TITLE UTP-glucose-1-phosphate uridylyltransferase (EC 2.7.7.9), skeletal muscle [validated] - human ALTERNATE_NAMES UDPglucose pyrophosphorylase ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S62599 REFERENCE S62599 !$#authors Duggleby, R.G.; Chao, Y.C.; Huang, J.G.; Peng, H.L.; Chang, !1H.Y. !$#journal Eur. J. Biochem. (1996) 235:173-179 !$#title Sequence differences between human muscle and liver cDNAs !1for UDPglucose pyrophosphorylase and kinetic properties of !1the recombinant enzymes expressed in Escherichia coli. !$#cross-references MUID:96202932; PMID:8631325 !$#accession S62599 !'##status preliminary !'##molecule_type mRNA !'##residues 1-508 ##label DUG !'##cross-references EMBL:U27460; NID:g881393 !'##note in GenBank entry HSU27460 PID:g881394 begins at an Met-12 GENETICS !$#gene GDB:UGP2 !'##cross-references GDB:119626; OMIM:191760 !$#map_position 2pter-2qter CLASSIFICATION #superfamily UTP-glucose-1-phosphate uridylyltransferase KEYWORDS nucleotidyltransferase SUMMARY #length 508 #molecular-weight 56965 #checksum 8869 SEQUENCE /// ENTRY JX0277 #type complete TITLE UTP-glucose-1-phosphate uridylyltransferase (EC 2.7.7.9) - bovine ALTERNATE_NAMES UDPglucose pyrophosphorylase ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS JX0277 REFERENCE JX0277 !$#authors Konishi, Y.; Tanizawa, K.; Muroya, S.; Fukui, T. !$#journal J. Biochem. (1993) 114:61-68 !$#title Molecular cloning, nucleotide sequencing, and affinity !1labeling of bovine liver UDP-glucose pyrophosphorylase. !$#cross-references MUID:94012583; PMID:8407878 !$#accession JX0277 !'##molecule_type mRNA !'##residues 1-508 ##label KON !'##cross-references GB:L14019; NID:g289447; PIDN:AAA30801.1; !1PID:g289448 !'##experimental_source liver CLASSIFICATION #superfamily UTP-glucose-1-phosphate uridylyltransferase KEYWORDS nucleotidyltransferase SUMMARY #length 508 #molecular-weight 56903 #checksum 9359 SEQUENCE /// ENTRY XNDOU #type complete TITLE UTP-glucose-1-phosphate uridylyltransferase (EC 2.7.7.9) - slime mold (Dictyostelium discoideum) ALTERNATE_NAMES glucose-1-phosphate uridylyltransferase; UDPglucose pyrophosphorylase ORGANISM #formal_name Dictyostelium discoideum DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Jun-2002 ACCESSIONS S07383 REFERENCE S07383 !$#authors Ragheb, J.A.; Dottin, R.P. !$#journal Nucleic Acids Res. (1987) 15:3891-3906 !$#title Structure and sequence of a UDP glucose pyrophosphorylase !1gene of Dictyostelium discoideum. !$#cross-references MUID:87231075; PMID:3035502 !$#accession S07383 !'##molecule_type DNA !'##residues 1-511 ##label RAG !'##cross-references EMBL:Y00145; NID:g7384; PIDN:CAA68340.1; PID:g7385 COMMENT This enzyme catalyzes alpha-D-glucose-1-phosphate and !1nucleoside triphosphates to form nucleotide sugars. It plays !1a central role as a glucosyl donor in cellular metabolic !1pathways. GENETICS !$#introns 160/3; 273/1; 361/3 CLASSIFICATION #superfamily UTP-glucose-1-phosphate uridylyltransferase KEYWORDS nucleotidyltransferase SUMMARY #length 511 #molecular-weight 57886 #checksum 8475 SEQUENCE /// ENTRY JC2265 #type complete TITLE UTP-glucose-1-phosphate uridylyltransferase (EC 2.7.7.9) galU [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES UDP-glucose pyrophosphorylase ORGANISM #formal_name Escherichia coli DATE 28-Aug-1985 #sequence_revision 07-Oct-1994 #text_change 03-Jun-2002 ACCESSIONS G64870; JC2265; A55585; S23788; A53297 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64870 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-302 ##label BLAT !'##cross-references GB:AE000222; GB:U00096; NID:g1787486; !1PIDN:AAC74318.1; PID:g1787488; UWGP:b1236 !'##experimental_source strain K-12, substrain MG1655 REFERENCE JC2265 !$#authors Hossain, S.A.; Tanizawa, K.; Kazuta, Y.; Fukui, T. !$#journal J. Biochem. (1994) 115:965-972 !$#title Overproduction and characterization of recombinant !1UDP-glucose pyrophosphorylase from Escherichia coli K-12. !$#cross-references MUID:95050433; PMID:7961613 !$#accession JC2265 !'##molecule_type DNA; protein !'##residues 1-302 ##label HOS !'##cross-references EMBL:X59940; NID:g42025; PIDN:CAA42564.1; !1PID:g42026 !'##experimental_source strain K-12 !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing REFERENCE A55585 !$#authors Weissborn, A.C.; Liu, Q.; Rumley, M.K.; Kennedy, E.P. !$#journal J. Bacteriol. (1994) 176:2611-2618 !$#title UTP:alpha-D-glucose-1-phosphate uridylyltransferase of !1Escherichia coli: isolation and DNA sequence of the galU !1gene and purification of the enzyme. !$#cross-references MUID:94222839; PMID:8169209 !$#accession A55585 !'##molecule_type DNA !'##residues 1-302 ##label WEI !'##cross-references GB:M98830; NID:g146072; PIDN:AAA20118.1; !1PID:g146073 !'##note the amino end of the mature protein was determined by protein !1sequencing REFERENCE A42290 !$#authors Ueguchi, C.; Ito, K. !$#journal J. Bacteriol. (1992) 174:1454-1461 !$#title Multicopy suppression: an approach to understanding !1intracellular functioning of the protein export system. !$#cross-references MUID:92165719; PMID:1537791 !$#accession S23788 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-302 ##label UEG !'##cross-references EMBL:X59940; NID:g42025; PIDN:CAA42564.1; !1PID:g42026 !'##experimental_source strain K-12 REFERENCE A53297 !$#authors Boesl, M.R. !$#journal J. Bacteriol. (1993) 175:7751-7753 !$#title Genetic map of the tyrT region of Escherichia coli from 27.1 !1to 27.7 minutes based exclusively on sequence data. !$#cross-references MUID:94064581; PMID:8244954 !$#accession A53297 !'##status preliminary !'##molecule_type DNA !'##residues 1-9;10-11,293-302 ##label BOE GENETICS !$#gene galU !$#map_position 27 min COMPLEX homotetramer FUNCTION !$#description catalyzes the reaction of UTP and glucose-1-phosphate to !1form UDP-1-glucose and pyrophosphate CLASSIFICATION #superfamily Escherichia coli UTP-glucose-1-phosphate !1uridylyltransferase KEYWORDS homotetramer; magnesium; nucleotidyltransferase FEATURE !$2-302 #product UTP-glucose-1-phosphate uridylyltransferase !8#status experimental #label MAT SUMMARY #length 302 #molecular-weight 32942 #checksum 9509 SEQUENCE /// ENTRY G64095 #type complete TITLE UTP-glucose-1-phosphate uridylyltransferase (EC 2.7.7.9) HI0812 [similarity] - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES UDP-glucose pyrophosphorylase ORGANISM #formal_name Haemophilus influenzae DATE 18-Aug-1995 #sequence_revision 18-Aug-1995 #text_change 03-Jun-2002 ACCESSIONS G64095 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession G64095 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-295 ##label TIGR !'##cross-references GB:L42023; TIGR:HI0812; GB:U32763; NID:g1573817; !1PIDN:AAC22471.1; PID:g1573824 FUNCTION !$#description catalyzes the reaction of UTP and glucose-1-phosphate to !1form UDP-1-glucose and pyrophosphate CLASSIFICATION #superfamily Escherichia coli UTP-glucose-1-phosphate !1uridylyltransferase KEYWORDS nucleotidyltransferase SUMMARY #length 295 #molecular-weight 32279 #checksum 568 SEQUENCE /// ENTRY S41533 #type complete TITLE UTP-glucose-1-phosphate uridylyltransferase (EC 2.7.7.9) galF [similarity] - Shigella flexneri ALTERNATE_NAMES UDP-glucose pyrophosphorylase ORGANISM #formal_name Shigella flexneri DATE 13-Jan-1995 #sequence_revision 13-Jan-1995 #text_change 03-Jun-2002 ACCESSIONS S41533; A55213 REFERENCE S41533 !$#authors Macpherson, D.F.; Manning, P.A.; Morona, R. !$#journal Mol. Microbiol. (1994) 11:281-292 !$#title Characterization of the dTDP-rhamnose biosynthetic genes !1encoded in the rfb locus of Shigella flexneri. !$#cross-references MUID:94224146; PMID:8170390 !$#accession S41533 !'##status preliminary !'##molecule_type DNA !'##residues 1-297 ##label MAC !'##cross-references EMBL:X71970; NID:g506557; PIDN:CAA50766.1; !1PID:g454897 !'##experimental_source serotype 2a REFERENCE A55213 !$#authors Rajakumar, K.; Jost, B.H.; Sasakawa, C.; Okada, N.; !1Yoshikawa, M.; Adler, B. !$#journal J. Bacteriol. (1994) 176:2362-2373 !$#title Nucleotide sequence of the rhamnose biosynthetic operon of !1Shigella flexneri 2a and role of lipopolysaccharide in !1virulence. !$#cross-references MUID:94209238; PMID:8157605 !$#accession A55213 !'##status preliminary !'##molecule_type DNA !'##residues 169-284,'A',286-297 ##label RAJ !'##cross-references GB:L14842; NID:g294894; PIDN:AAA53678.1; !1PID:g294895 !'##experimental_source strain YSH6200 GENETICS !$#gene galF FUNCTION !$#description catalyzes the reaction of UTP and glucose-1-phosphate to !1form UDP-1-glucose and pyrophosphate !$#pathway lipopolysaccaride biosynthesis CLASSIFICATION #superfamily Escherichia coli UTP-glucose-1-phosphate !1uridylyltransferase KEYWORDS nucleotidyltransferase SUMMARY #length 297 #molecular-weight 32817 #checksum 4022 SEQUENCE /// ENTRY A64970 #type complete TITLE UTP-glucose-1-phosphate uridylyltransferase (EC 2.7.7.9) galF [similarity] - Escherichia coli (strain K-12) ALTERNATE_NAMES UDP-glucose pyrophosphorylase ORGANISM #formal_name Escherichia coli #variety strain K-12 DATE 12-Sep-1997 #sequence_revision 17-Sep-1997 #text_change 03-Jun-2002 ACCESSIONS A64970 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64970 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-297 ##label BLAT !'##cross-references GB:AE000295; GB:U00096; NID:g1788354; !1PIDN:AAC75103.1; PID:g1788355; UWGP:b2042 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene galF FUNCTION !$#description catalyzes the reaction of UTP and glucose-1-phosphate to !1form UDP-1-glucose and pyrophosphate CLASSIFICATION #superfamily Escherichia coli UTP-glucose-1-phosphate !1uridylyltransferase KEYWORDS nucleotidyltransferase SUMMARY #length 297 #molecular-weight 32829 #checksum 3778 SEQUENCE /// ENTRY A56146 #type complete TITLE UTP-glucose-1-phosphate uridylyltransferase (EC 2.7.7.9) [similarity] - Klebsiella pneumoniae ALTERNATE_NAMES UDP-glucose pyrophosphorylase ORGANISM #formal_name Klebsiella pneumoniae DATE 03-Oct-1995 #sequence_revision 03-Oct-1995 #text_change 03-Jun-2002 ACCESSIONS A56146 REFERENCE A56146 !$#authors Arakawa, Y.; Wacharotayankun, R.; Nagatsuka, T.; Ito, H.; !1Kato, N.; Ohta, M. !$#journal J. Bacteriol. (1995) 177:1788-1796 !$#title Genomic organization of the Klebsiella pneumoniae cps region !1responsible for serotype K2 capsular polysaccharide !1synthesis in the virulent strain chedid. !$#cross-references MUID:95204345; PMID:7896702 !$#accession A56146 !'##status preliminary !'##molecule_type DNA !'##residues 1-296 ##label ARA !'##cross-references GB:D21242; NID:g747654 !'##experimental_source strain Chedid FUNCTION !$#description catalyzes the reaction of UTP and glucose-1-phosphate to !1form UDP-1-glucose and pyrophosphate !$#pathway lipopolysaccaride biosynthesis CLASSIFICATION #superfamily Escherichia coli UTP-glucose-1-phosphate !1uridylyltransferase KEYWORDS nucleotidyltransferase SUMMARY #length 296 #molecular-weight 32533 #checksum 1949 SEQUENCE /// ENTRY S15298 #type complete TITLE UTP-glucose-1-phosphate uridylyltransferase (EC 2.7.7.9) galF [similarity] - Salmonella typhimurium ALTERNATE_NAMES protein 2.8; UDP-glucose pyrophosphorylase ORGANISM #formal_name Salmonella typhimurium DATE 21-Nov-1993 #sequence_revision 10-Nov-1995 #text_change 03-Jun-2002 ACCESSIONS S15298 REFERENCE S15296 !$#authors Jiang, X.M.; Neal, B.; Santiago, F.; Lee, S.J.; Romana, !1L.K.; Reeves, P.R. !$#journal Mol. Microbiol. (1991) 5:695-713 !$#title Structure and sequence of the rfb (O antigen) gene cluster !1of Salmonella serovar typhimurium (strain LT2). !$#cross-references MUID:91260454; PMID:1710759 !$#accession S15298 !'##status preliminary !'##molecule_type DNA !'##residues 1-297 ##label MOL !'##cross-references EMBL:X56793 !'##experimental_source strain LT2; group B; isolate SL1654 GENETICS !$#gene galF FUNCTION !$#description catalyzes the reaction of UTP and glucose-1-phosphate to !1form UDP-1-glucose and pyrophosphate !$#pathway lipopolysaccaride biosynthesis CLASSIFICATION #superfamily Escherichia coli UTP-glucose-1-phosphate !1uridylyltransferase KEYWORDS nucleotidyltransferase SUMMARY #length 297 #molecular-weight 33024 #checksum 3631 SEQUENCE /// ENTRY D49349 #type complete TITLE UTP-glucose-1-phosphate uridylyltransferase (EC 2.7.7.9) exoN [similarity] - Rhizobium meliloti ALTERNATE_NAMES exoN protein; UDP-glucose pyrophosphorylase ORGANISM #formal_name Rhizobium meliloti DATE 03-May-1994 #sequence_revision 03-May-1994 #text_change 03-Jun-2002 ACCESSIONS D49349; S39959; S37030 REFERENCE A49349 !$#authors Glucksmann, M.A.; Reuber, T.L.; Walker, G.C. !$#journal J. Bacteriol. (1993) 175:7045-7055 !$#title Genes needed for the modification, polymerization, export, !1and processing of succinoglycan by Rhizobium meliloti: a !1model for succinoglycan biosynthesis. !$#cross-references MUID:94042870; PMID:8226646 !$#accession D49349 !'##status preliminary !'##molecule_type DNA !'##residues 1-320 ##label GLU !'##cross-references GB:L20758; NID:g393240; PIDN:AAA16043.1; !1PID:g393242 REFERENCE S39955 !$#authors Becker, A.; Kleickmann, A.; Keller, M.; Arnold, W.; Puehler, !1A. !$#journal Mol. Gen. Genet. (1993) 241:367-379 !$#title Identification and analysis of the Rhizobium meliloti !1exoAMONP genes involved in exopolysaccharide biosynthesis !1and mapping of promoters located on the exoHKLAMONP !1fragment. !$#cross-references MUID:94067019; PMID:8246891 !$#accession S39959 !'##molecule_type DNA !'##residues 1-274,'ARADIGDIVFESVRDMVLSHESRIRAA' ##label BEC !'##cross-references EMBL:Z22636; NID:g605653; PIDN:CAA80348.1; !1PID:g397573 GENETICS !$#gene exoN FUNCTION !$#description catalyzes the reaction of UTP and glucose-1-phosphate to !1form UDP-1-glucose and pyrophosphate CLASSIFICATION #superfamily Escherichia coli UTP-glucose-1-phosphate !1uridylyltransferase KEYWORDS nucleotidyltransferase SUMMARY #length 320 #molecular-weight 34926 #checksum 3845 SEQUENCE /// ENTRY A40650 #type complete TITLE UTP-glucose-1-phosphate uridylyltransferase (EC 2.7.7.9) gtaB [validated] - Bacillus subtilis ALTERNATE_NAMES UDP-glucose pyrophosphorylase ORGANISM #formal_name Bacillus subtilis DATE 03-May-1994 #sequence_revision 03-May-1994 #text_change 03-Jun-2002 ACCESSIONS A40650; B69638 REFERENCE A40650 !$#authors Varon, D.; Boylan, S.A.; Okamoto, K.; Price, C.W. !$#journal J. Bacteriol. (1993) 175:3964-3971 !$#title Bacillus subtilis gtaB encodes UDP-glucose pyrophosphorylase !1and is controlled by stationary-phase transcription factor !1sigma(B). !$#cross-references MUID:93308074; PMID:8320212 !$#accession A40650 !'##status preliminary !'##molecule_type DNA !'##residues 1-292 ##label VAR !'##cross-references GB:L12272; NID:g289286; PIDN:AAA71967.1; !1PID:g289287 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69638 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-292 ##label KUN !'##cross-references GB:Z99122; GB:AL009126; NID:g2636029; !1PIDN:CAB15584.1; PID:g2636093 !'##experimental_source strain 168 GENETICS !$#gene gtaB FUNCTION !$#description catalyzes the reaction of UTP and glucose-1-phosphate to !1form UDP-1-glucose and pyrophosphate CLASSIFICATION #superfamily Escherichia coli UTP-glucose-1-phosphate !1uridylyltransferase KEYWORDS nucleotidyltransferase SUMMARY #length 292 #molecular-weight 33070 #checksum 6078 SEQUENCE /// ENTRY JC4985 #type complete TITLE UTP-glucose-1-phosphate uridylyltransferase (EC 2.7.7.9) [validated] - Xanthomonas campestris ALTERNATE_NAMES UDP-glucose pyrophosphorylase ORGANISM #formal_name Xanthomonas campestris DATE 15-Dec-1996 #sequence_revision 21-Jan-1997 #text_change 03-Jun-2002 ACCESSIONS JC4985 REFERENCE JC4985 !$#authors Wei, C.L.; Lin, N.T.; Weng, S.F.; Tseng, Y.H. !$#journal Biochem. Biophys. Res. Commun. (1996) 226:607-612 !$#title The gene encoding UDP-glucose pyrophosphorylase is required !1for the synthesis of xanthan gum in Xanthomonas campestris. !$#cross-references MUID:96428562; PMID:8831665 !$#accession JC4985 !'##molecule_type DNA !'##residues 1-324 ##label WEI !'##cross-references GB:U65532; NID:g1628574; PIDN:AAB17376.1; !1PID:g1628575 GENETICS !$#map_position Xc17 FUNCTION !$#description catalyzes the reaction of UTP and glucose-1-phosphate to !1form UDP-1-glucose and pyrophosphate CLASSIFICATION #superfamily Escherichia coli UTP-glucose-1-phosphate !1uridylyltransferase KEYWORDS nucleotidyltransferase SUMMARY #length 324 #molecular-weight 35228 #checksum 4005 SEQUENCE /// ENTRY A64250 #type complete TITLE UTP-glucose-1-phosphate uridylyltransferase (EC 2.7.7.9) MG453 [similarity] - Mycoplasma genitalium ALTERNATE_NAMES UDP-glucose pyrophosphorylase ORGANISM #formal_name Mycoplasma genitalium DATE 17-Nov-1995 #sequence_revision 17-Nov-1995 #text_change 03-Jun-2002 ACCESSIONS A64250 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession A64250 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-292 ##label TIGR !'##cross-references GB:L43967; GB:U39732; NID:g3845044; !1PIDN:AAC72473.1; PID:g3845047; TIGR:MG453 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 FUNCTION !$#description catalyzes the reaction of UTP and glucose-1-phosphate to !1form UDP-1-glucose and pyrophosphate CLASSIFICATION #superfamily Escherichia coli UTP-glucose-1-phosphate !1uridylyltransferase KEYWORDS nucleotidyltransferase SUMMARY #length 292 #molecular-weight 32514 #checksum 7308 SEQUENCE /// ENTRY E64466 #type complete TITLE UTP-glucose-1-phosphate uridylyltransferase (EC 2.7.7.9) MJ1334 [similarity] - Methanococcus jannaschii ALTERNATE_NAMES UDP-glucose pyrophosphorylase ORGANISM #formal_name Methanococcus jannaschii DATE 13-Sep-1996 #sequence_revision 13-Sep-1996 #text_change 03-Jun-2002 ACCESSIONS E64466 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession E64466 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-283 ##label BUL !'##cross-references GB:L77117; GB:U67573; TIGR:MJ1334; NID:g2826395; !1PIDN:AAB99341.1; PID:g1591975 GENETICS !$#map_position REV1284127-1283276 FUNCTION !$#description catalyzes the reaction of UTP and glucose-1-phosphate to !1form UDP-1-glucose and pyrophosphate CLASSIFICATION #superfamily Escherichia coli UTP-glucose-1-phosphate !1uridylyltransferase KEYWORDS nucleotidyltransferase SUMMARY #length 283 #molecular-weight 32090 #checksum 6873 SEQUENCE /// ENTRY A41382 #type complete TITLE UTP-glucose-1-phosphate uridylyltransferase (EC 2.7.7.9) [validated] - Acetobacter pasteurianus ALTERNATE_NAMES UDP-glucose pyrophosphorylase ORGANISM #formal_name Acetobacter pasteurianus DATE 28-May-1992 #sequence_revision 28-May-1992 #text_change 03-Jun-2002 ACCESSIONS A41382 REFERENCE A41382 !$#authors Brede, G.; Fjaervik, E.; Valla, S. !$#journal J. Bacteriol. (1991) 173:7042-7045 !$#title Nucleotide sequence and expression analysis of the !1Acetobacter xylinum uridine diphosphoglucose !1pyrophosphorylase gene. !$#cross-references MUID:92041596; PMID:1938907 !$#accession A41382 !'##status preliminary !'##molecule_type DNA !'##residues 1-284 ##label BRE !'##cross-references GB:M76548; NID:g141736; PIDN:AAA21888.1; !1PID:g141737 FUNCTION !$#description catalyzes the reaction of UTP and glucose-1-phosphate to !1form UDP-1-glucose and pyrophosphate CLASSIFICATION #superfamily Escherichia coli UTP-glucose-1-phosphate !1uridylyltransferase KEYWORDS nucleotidyltransferase SUMMARY #length 284 #molecular-weight 30992 #checksum 6621 SEQUENCE /// ENTRY B37760 #type complete TITLE UTP-hexose-1-phosphate uridylyltransferase (EC 2.7.7.10) - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS B37760 REFERENCE A37760 !$#authors Houng, H.S.H.; Kopecko, D.J.; Baron, L.S. !$#journal J. Bacteriol. (1990) 172:4392-4398 !$#title Molecular cloning and physical and functional !1characterization of the Salmonella typhimurium and !1Salmonella typhi galactose utilization operons. !$#cross-references MUID:90330544; PMID:2198256 !$#accession B37760 !'##status preliminary !'##molecule_type DNA !'##residues 1-348 ##label HOU !'##cross-references GB:M33681; NID:g154046; PIDN:AAA27112.1; !1PID:g154048 CLASSIFICATION #superfamily UDPglucose-hexose-1-phosphate !1uridylyltransferase KEYWORDS nucleotidyltransferase SUMMARY #length 348 #molecular-weight 39589 #checksum 7428 SEQUENCE /// ENTRY XNECUD #type complete TITLE UDPglucose-hexose-1-phosphate uridylyltransferase (EC 2.7.7.12) - Escherichia coli (strain K-12) ALTERNATE_NAMES galactose-1-phosphate uridylyltransferase; UTP-hexose-1-phosphate uridylyltransferase (EC 2.7.7.10) ORGANISM #formal_name Escherichia coli DATE 30-Sep-1988 #sequence_revision 31-Mar-1992 #text_change 19-Jul-2002 ACCESSIONS S00722; S00723; A23044; F64811; A25764 REFERENCE S00722 !$#authors Lemaire, H.G.; Mueller-Hill, B. !$#journal Nucleic Acids Res. (1986) 14:7705-7711 !$#title Nucleotide sequences of the galE gene and the galT gene of !1E. coli. !$#cross-references MUID:87040735; PMID:3022232 !$#accession S00722 !'##molecule_type DNA !'##residues 1-28,'LS',32-348 ##label LEM !'##cross-references EMBL:X06226; NID:g41522; PIDN:CAA29574.1; !1PID:g41524 REFERENCE S00723 !$#authors Cornwell, T.L.; Adhya, S.L.; Reznikoff, W.S.; Frey, P.A. !$#journal Nucleic Acids Res. (1987) 15:8116 !$#title The nucleotide sequence of the gal T gene of Escherichia !1coli. !$#cross-references MUID:88040438; PMID:2823224 !$#accession S00723 !'##molecule_type DNA !'##residues 27-38 ##label COR !'##cross-references EMBL:X06226 REFERENCE A93558 !$#authors Debouck, C.; Riccio, A.; Schumperli, D.; McKenney, K.; !1Jeffers, J.; Hughes, C.; Rosenberg, M.; Heusterspreute, M.; !1Brunel, F.; Davison, J. !$#journal Nucleic Acids Res. (1985) 13:1841-1853 !$#title Structure of the galactokinase gene of Escherichia coli, the !1last (?) gene of the gal operon. !$#cross-references MUID:85215584; PMID:3158881 !$#accession A23044 !'##molecule_type DNA !'##residues 294-348 ##label DEB !'##cross-references EMBL:X02306; NID:g41530; PIDN:CAA26171.1; !1PID:g41531 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64811 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-348 ##label BLAT !'##cross-references GB:AE000178; GB:U00096; NID:g1786967; !1PIDN:AAC73845.1; PID:g1786973; UWGP:b0758 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene galT !$#map_position 17 min FUNCTION !$#description nucleotidyltransferase !$#pathway galactose metabolism CLASSIFICATION #superfamily UDPglucose-hexose-1-phosphate !1uridylyltransferase KEYWORDS galactose metabolism; nucleotidyltransferase SUMMARY #length 348 #molecular-weight 39645 #checksum 6072 SEQUENCE /// ENTRY A56685 #type complete TITLE UDPglucose-hexose-1-phosphate uridylyltransferase (EC 2.7.7.12) - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS A56685 REFERENCE A56685 !$#authors Heidenreich, R.A.; Mallee, J.; Segal, S. !$#journal DNA Seq. (1993) 3:311-318 !$#title Rat galactose-1-phosphate uridyltransferase coding sequence, !1transcription start site and genomic organization. !$#cross-references MUID:94003402; PMID:8400361 !$#accession A56685 !'##status preliminary !'##molecule_type DNA !'##residues 1-379 ##label HEI !'##cross-references GB:L05541; NID:g294559; PIDN:AAC37609.1; !1PID:g294560 !'##note authors translated the codon AAG for residue 215 as Glu, and !1TTG for residue 219 as Trp GENETICS !$#introns 28/1; 84/3; 110/1; 126/2; 169/3; 188/3; 229/3; 274/1; 302/1; !1353/3 CLASSIFICATION #superfamily UDPglucose-hexose-1-phosphate !1uridylyltransferase KEYWORDS nucleotidyltransferase SUMMARY #length 379 #molecular-weight 43314 #checksum 3766 SEQUENCE /// ENTRY E64096 #type complete TITLE UDPglucose-hexose-1-phosphate uridylyltransferase (EC 2.7.7.12) - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS E64096; S27987; S21446 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession E64096 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-349 ##label TIGR !'##cross-references GB:U32764; GB:L42023; NID:g1573827; !1PIDN:AAC22479.1; PID:g1573833; TIGR:HI0820 REFERENCE S27986 !$#authors Maskell, D.J.; Szabo, M.J.; Deadman, M.E.; Moxon, E.R. !$#journal Mol. Microbiol. (1992) 6:3051-3063 !$#title The gal locus from Haemophilus influenzae: cloning, !1sequencing and the use of gal mutants to study !1lipopolysaccharide. !$#cross-references MUID:93125127; PMID:1282642 !$#accession S27987 !'##molecule_type DNA !'##residues 1-220,'V',222-228,'V',230-333,'D',335-349 ##label MAS !'##cross-references EMBL:X65934; NID:g43562; PIDN:CAA46730.1; !1PID:g43564 GENETICS !$#gene galT FUNCTION !$#description nucleotidyltransferase CLASSIFICATION #superfamily UDPglucose-hexose-1-phosphate !1uridylyltransferase KEYWORDS galactose metabolism; nucleotidyltransferase SUMMARY #length 349 #molecular-weight 40758 #checksum 1548 SEQUENCE /// ENTRY XNBYUG #type complete TITLE UDPglucose-hexose-1-phosphate uridylyltransferase (EC 2.7.7.12) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES galactose-1-phosphate uridyltransferase; protein YBR018c; protein YBR0226 ORGANISM #formal_name Saccharomyces cerevisiae DATE 17-Mar-1987 #sequence_revision 09-Sep-1994 #text_change 03-Jun-2002 ACCESSIONS S45873; S50813; S05811; A00720; S18725; S18757; S24918; !1S50322 REFERENCE S45862 !$#authors Entian, K.D.; Koetter, P.; Rose, M.; Li, Z.; Thermann, R.; !1Brendel, M.; Baur, A.; Boles, E.; Miosga, T.; !1Schaaff-Gerstenschlaeger, I.; Zimmermann, F.K. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S45873 !'##molecule_type DNA !'##residues 1-366 ##label ENT !'##cross-references EMBL:Z35887; NID:g536219; PIDN:CAA84960.1; !1PID:g536220; GSPDB:GN00002; MIPS:YBR018c !'##experimental_source strain S288C REFERENCE S50812 !$#authors Schaaff-Gerstenschlaeger, I.; Schindwolf, T.; Lehnert, W.; !1Rose, M.; Zimmermann, F.K. !$#journal Yeast (1995) 11:79-83 !$#title Sequence and functional analysis of a 7.2 kb fragment of !1Saccharomyces cerevisiae chromosome II including GAL7 and !1GAL10 and a new essential open reading frame. !$#cross-references MUID:95282516; PMID:7762304 !$#accession S50813 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-366 ##label SCW !'##cross-references EMBL:X81324; NID:g587572; PIDN:CAA57105.1; !1PID:g587574 !'##experimental_source strain S288C !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1September 1994 REFERENCE S05811 !$#authors Tajima, M.; Nogi, Y.; Fukasawa, T. !$#journal Yeast (1985) 1:67-77 !$#title Primary structure of the Saccharomyces cerevisiae GAL7 gene. !$#cross-references MUID:89131252; PMID:2851900 !$#accession S05811 !'##molecule_type DNA !'##residues 1-84,'S',87-266,'A',268-344,'I',346-366 ##label TAJ !'##cross-references EMBL:M12348; NID:g171559; PIDN:AAA34627.1; !1PID:g171560 REFERENCE A91795 !$#authors Citron, B.A.; Donelson, J.E. !$#journal J. Bacteriol. (1984) 158:269-278 !$#title Sequence of the Saccharomyces GAL region and its !1transcription in vivo. !$#cross-references MUID:84185433; PMID:6715281 !$#accession A00720 !'##molecule_type DNA !'##residues 1-10,'Y',12-57,'H',59-184 ##label CIT !'##cross-references EMBL:K01752; NID:g171561; PIDN:AAA34628.1; !1PID:g553128 REFERENCE S18725 !$#authors Nogi, Y.; Fukasawa, T. !$#journal Nucleic Acids Res. (1983) 11:8555-8568 !$#title Nucleotide sequence of the transcriptional initiation region !1of the yeast GAL7 gene. !$#cross-references MUID:84169499; PMID:6324089 !$#accession S18725 !'##status translation not shown !'##molecule_type DNA !'##residues 1-21 ##label NOG !'##cross-references EMBL:X00215 !$#accession S18757 !'##molecule_type protein !'##residues 2-8 ##label NOG2 GENETICS !$#gene SGD:GAL7; MIPS:YBR018c !'##cross-references SGD:S0000222; MIPS:YBR018c !$#map_position 2R FUNCTION !$#description galactose metabolism; nucleotidyltransferase CLASSIFICATION #superfamily UDPglucose-hexose-1-phosphate !1uridylyltransferase KEYWORDS galactose metabolism; nucleotidyltransferase FEATURE !$2-366 #product UDPglucose-hexose-1-phosphate !8uridylyltransferase #status experimental #label MAT SUMMARY #length 366 #molecular-weight 42385 #checksum 4884 SEQUENCE /// ENTRY XNVKUD #type complete TITLE UDPglucose-hexose-1-phosphate uridylyltransferase (EC 2.7.7.12) - yeast (Kluyveromyces marxianus var. lactis) ALTERNATE_NAMES galactose-1-phosphate uridylyltransferase ORGANISM #formal_name Kluyveromyces marxianus var. lactis, Candida sphaerica DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Jun-2002 ACCESSIONS S01408 REFERENCE S01407 !$#authors Webster, T.D.; Dickson, R.C. !$#journal Nucleic Acids Res. (1988) 16:8192-8194 !$#title Nucleotide sequence of the galactose gene cluster of !1Kluyveromyces lactis. !$#cross-references MUID:88335573; PMID:3419917 !$#accession S01408 !'##molecule_type DNA !'##residues 1-370 ##label WEB !'##cross-references EMBL:X07039; NID:g2817; PIDN:CAA30091.1; PID:g2820 GENETICS !$#gene GAL7 CLASSIFICATION #superfamily UDPglucose-hexose-1-phosphate !1uridylyltransferase KEYWORDS galactose metabolism; nucleotidyltransferase SUMMARY #length 370 #molecular-weight 42787 #checksum 4941 SEQUENCE /// ENTRY XNSMUD #type complete TITLE UDPglucose-hexose-1-phosphate uridylyltransferase (EC 2.7.7.12) - Streptomyces sp. ALTERNATE_NAMES hexose-1-phosphate uridylyltransferase; uridyltransferase ORGANISM #formal_name Streptomyces sp. DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Jun-2002 ACCESSIONS A28669 REFERENCE A28669 !$#authors Adams, C.W.; Fornwald, J.A.; Schmidt, F.J.; Rosenberg, M.; !1Brawner, M.E. !$#journal J. Bacteriol. (1988) 170:203-212 !$#title Gene organization and structure of the Streptomyces lividans !1gal operon. !$#cross-references MUID:88086869; PMID:3335481 !$#accession A28669 !'##molecule_type DNA !'##residues 1-317 ##label ADA !'##cross-references GB:M18953; NID:g153259; PIDN:AAA26746.1; !1PID:g153260 !'##note the source is designated as Streptomyces lividans GENETICS !$#gene galT !$#start_codon GTG CLASSIFICATION #superfamily UDPglucose-hexose-1-phosphate !1uridylyltransferase KEYWORDS galactose metabolism; nucleotidyltransferase SUMMARY #length 317 #molecular-weight 35230 #checksum 6297 SEQUENCE /// ENTRY S50145 #type complete TITLE choline-phosphate cytidylyltransferase (EC 2.7.7.15) [validated] - human ALTERNATE_NAMES CTP:choline-phosphate cytidylyltransferase; phosphorylcholine transferase ORGANISM #formal_name Homo sapiens #common_name man DATE 14-Jul-1995 #sequence_revision 10-Nov-1995 #text_change 15-Sep-2000 ACCESSIONS S50145 REFERENCE S50145 !$#authors Kalmar, G.B.; Kay, R.J.; LaChance, A.C.; Cornell, R.B. !$#journal Biochim. Biophys. Acta (1994) 1219:328-334 !$#title Primary structure and expression of a human !1CTP:phosphocholine cytidylyltransferase. !$#cross-references MUID:95002145; PMID:7918629 !$#accession S50145 !'##molecule_type mRNA !'##residues 1-367 ##label KAL !'##cross-references EMBL:L28957; NID:g575485; PIDN:AAA72127.1; !1PID:g575486 REFERENCE A66353 !$#authors Dunne, S.J.; Cornell, R.B.; Johnson, J.E.; Glover, N.R.; !1Tracey, A.S. !$#submission submitted to the Brookhaven Protein Data Bank, June 1996 !$#cross-references PDB:1PEH !$#contents annotation; conformation by (1)H-NMR, residues 256-262,'W', !1264-268 REFERENCE A66354 !$#authors Dunne, S.J.; Cornell, R.B.; Johnson, J.E.; Glover, N.R.; !1Tracey, A.S. !$#submission submitted to the Brookhaven Protein Data Bank, June 1996 !$#cross-references PDB:1PEI !$#contents annotation; conformation by (1)H-NMR, residues 267-288 REFERENCE A58736 !$#authors Johnson, J.E.; Cornell, R.B. !$#journal Biochemistry (1994) 33:4327-4335 !$#title Membrane-binding amphipathic alpha-helical peptide derived !1from CTP:phosphocholine cytidylyltransferase. !$#cross-references MUID:94206942; PMID:8155650 !$#contents annotation; conformation by (1)H-NMR REFERENCE A58737 !$#authors Dunne, S.J.; Cornell, R.B.; Johnson, J.E.; Glover, N.R.; !1Tracey, A.S. !$#journal Biochemistry (1996) 35:11975-11984 !$#title Structure of the membrane binding domain of !1CTP:phosphocholine cytidylyltransferase. !$#cross-references MUID:96406815; PMID:8810902 !$#contents annotation; conformation by (1)H-NMR GENETICS !$#gene GDB:PCYT1; CT; CTPCT !'##cross-references GDB:433387; OMIM:123695 !$#map_position 3q13-3q28 FUNCTION !$#description catalyzes the formation of cytidinediphosphate choline and !1pyrophosphate from cytidinetriphosphate and choline !1phosphate !$#pathway phospholipid biosynthesis !$#note phosphorylation reduces enzyme activity CLASSIFICATION #superfamily choline-phosphate cytidylyltransferase KEYWORDS membrane-associated protein; nucleotidyltransferase; !1nucleus; phospholipid biosynthesis; phosphoprotein FEATURE !$8-16 #region nuclear location signal\ !$256-288 #domain amphipathic helix #status predicted #label !8APH\ !$323 #binding_site phosphate (Ser) (covalent) (by cdc2 !8kinase) #status predicted SUMMARY #length 367 #molecular-weight 41732 #checksum 1272 SEQUENCE /// ENTRY S24935 #type complete TITLE choline-phosphate cytidylyltransferase (EC 2.7.7.15) - mouse ALTERNATE_NAMES CTP:choline-phosphate cytidylyltransferase; phosphorylcholine transferase ORGANISM #formal_name Mus musculus #common_name house mouse DATE 20-Feb-1995 #sequence_revision 20-Feb-1995 #text_change 11-Jun-1999 ACCESSIONS A49366; S24935 REFERENCE A49366 !$#authors Rutherford, M.S.; Rock, C.O.; Jenkins, N.A.; Gilbert, D.J.; !1Tessner, T.G.; Copeland, N.G.; Jackowski, S. !$#journal Genomics (1993) 18:698-701 !$#title The gene for murine CTP:phosphocholine cytidylyltransferase !1(Ctpct) is located on mouse chromosome 16. !$#cross-references MUID:94140374; PMID:8307580 !$#accession A49366 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type mRNA !'##residues 1-302,'N',304-335,'Q',337-354,'K',356-367 ##label RU2 !'##cross-references EMBL:Z12302 REFERENCE S24935 !$#authors Rutherford, M.S.; Tessner, T.G.; Jackowski, S.; Rock, C.O. !$#submission submitted to the EMBL Data Library, June 1992 !$#description The sequence of Murine cytidylyltransferase cDNA. !$#accession S24935 !'##molecule_type mRNA !'##residues 1-367 ##label RUT !'##cross-references EMBL:Z12302; NID:g50536; PIDN:CAA78172.1; !1PID:g50537 FUNCTION !$#description catalyzes the formation of cytidinediphosphate choline and !1pyrophosphate from cytidinetriphosphate and choline !1phosphate !$#pathway phospholipid biosynthesis !$#note phosphorylation reduces enzyme activity CLASSIFICATION #superfamily choline-phosphate cytidylyltransferase KEYWORDS membrane-associated protein; nucleotidyltransferase; !1nucleus; phospholipid biosynthesis; phosphoprotein FEATURE !$8-16 #region nuclear location signal\ !$256-288 #domain amphipathic helix #status predicted #label !8APH\ !$323 #binding_site phosphate (Ser) (covalent) (by cdc2 !8kinase) #status predicted SUMMARY #length 367 #molecular-weight 41667 #checksum 1085 SEQUENCE /// ENTRY A36001 #type complete TITLE choline-phosphate cytidylyltransferase (EC 2.7.7.15) - rat ALTERNATE_NAMES CTP:choline-phosphate cytidylyltransferase; phosphorylcholine transferase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 21-Dec-1990 #sequence_revision 21-Dec-1990 #text_change 11-Jun-1999 ACCESSIONS A36001 REFERENCE A36001 !$#authors Kalmar, G.B.; Kay, R.J.; Lachance, A.; Aebersold, R.; !1Cornell, R.B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:6029-6033 !$#title Cloning and expression of rat liver CTP:phosphocholine !1cytidylyltransferase: an amphipathic protein that controls !1phosphatidylcholine synthesis. !$#cross-references MUID:90349548; PMID:2166941 !$#accession A36001 !'##molecule_type mRNA !'##residues 1-367 ##label KAL !'##cross-references GB:M36071; NID:g203651; PIDN:AAA40995.1; !1PID:g203652 !'##note parts of this sequence were determined by protein sequencing; !1the amino end of the mature protein is blocked FUNCTION !$#description catalyzes the formation of cytidinediphosphate choline and !1pyrophosphate from cytidinetriphosphate and choline !1phosphate !$#pathway phospholipid biosynthesis !$#note phosphorylation reduces enzyme activity CLASSIFICATION #superfamily choline-phosphate cytidylyltransferase KEYWORDS blocked amino end; membrane-associated protein; !1nucleotidyltransferase; nucleus; phospholipid biosynthesis; !1phosphoprotein FEATURE !$8-16 #region nuclear location signal\ !$256-288 #domain amphipathic helix #status predicted #label !8APH\ !$231 #binding_site carbohydrate (Asn) (covalent) #status !8absent\ !$323 #binding_site phosphate (Ser) (covalent) (by cdc2 !8kinase) #status predicted SUMMARY #length 367 #molecular-weight 41727 #checksum 884 SEQUENCE /// ENTRY S44385 #type complete TITLE choline-phosphate cytidylyltransferase (EC 2.7.7.15) - Chinese hamster ALTERNATE_NAMES CTP:choline-phosphate cytidylyltransferase; phosphorylcholine transferase ORGANISM #formal_name Cricetulus griseus #common_name Chinese hamster DATE 13-Jan-1995 #sequence_revision 10-Nov-1995 #text_change 11-Jun-1999 ACCESSIONS S44385 REFERENCE S44385 !$#authors Sweitzer, T.D.; Kent, C. !$#journal Arch. Biochem. Biophys. (1994) 311:107-116 !$#title Expression of wild-type and mutant rat liver CTP: !1phosphocholine cytidylyltransferase in a !1cytidylyltransferase-deficient Chinese hamster ovary cell !1line. !$#cross-references MUID:94241689; PMID:8185307 !$#accession S44385 !'##molecule_type mRNA !'##residues 1-367 ##label SWE !'##cross-references EMBL:L13244; NID:g289979; PIDN:AAA21305.1; !1PID:g289980 !'##note the inactive mutant sequence has 140-His FUNCTION !$#description catalyzes the formation of cytidinediphosphate choline and !1pyrophosphate from cytidinetriphosphate and choline !1phosphate !$#pathway phospholipid biosynthesis CLASSIFICATION #superfamily choline-phosphate cytidylyltransferase KEYWORDS membrane-associated protein; nucleotidyltransferase; !1nucleus; phospholipid biosynthesis; phosphoprotein FEATURE !$8-16 #region nuclear location signal\ !$256-288 #domain amphipathic helix #status predicted #label !8APH\ !$231 #binding_site carbohydrate (Asn) (covalent) #status !8absent\ !$323 #binding_site phosphate (Ser) (covalent) (by cdc2 !8kinase) #status predicted SUMMARY #length 367 #molecular-weight 41716 #checksum 2854 SEQUENCE /// ENTRY XNBYCP #type complete TITLE choline-phosphate cytidylyltransferase (EC 2.7.7.15) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES CTP:choline-phosphate cytidylyltransferase; phosphorylcholine transferase; protein G7729; protein YGR202c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1991 #sequence_revision 01-Dec-1995 #text_change 21-Jul-2000 ACCESSIONS S53925; S00221; S12485; S61931; S64524; S63851 REFERENCE S53922 !$#authors Guerreiro, P.; Barreiros, T.; Soares, H.; Cyrne, L.; Maia e !1Silva, A.; Rodrigues-Pousada, C. !$#submission submitted to the EMBL Data Library, April 1995 !$#description Sequencing of a 17.6 kb segment on the right arm of yeast !1chromosome VII reveals 12 open reading frames, including !1CCT, ADE3 and TR-I genes, homologous to the yeast YAL023 and !1EF1G genes, of the human. !$#accession S53925 !'##molecule_type DNA !'##residues 1-424 ##label GUE !'##cross-references EMBL:Z49133; NID:g790489; PIDN:CAA88995.1; !1PID:g790493 !'##experimental_source strain S288C REFERENCE S00221 !$#authors Tsukagoshi, Y.; Nikawa, J.; Yamashita, S. !$#journal Eur. J. Biochem. (1987) 169:477-486 !$#title Molecular cloning and characterization of the gene encoding !1cholinephosphate cytidylyltransferase in Saccharomyces !1cerevisiae. !$#cross-references MUID:88082780; PMID:2826147 !$#accession S00221 !'##molecule_type DNA !'##residues 1-191,'H',193-424 ##label TSU1 !'##cross-references EMBL:X06598 !'##note in the authors' translation an additional GGA codon is shown !1after 90-Pro and, consequently, the codons for residues !191-104 are displaced one residue to the right; the codon for !1105-Arg is not shown; the nucleotide sequence corresponding !1to codons 91-105 has been corrected in reference S12485 REFERENCE S12485 !$#authors Tsukagoshi, Y.; Nakawa, J.; Yamashita, S. !$#submission submitted to the EMBL Data Library, January 1990 !$#accession S12485 !'##molecule_type DNA !'##residues 1-191,'H',193-424 ##label TSU2 !'##cross-references EMBL:X06598 REFERENCE S61931 !$#authors Tsukagoshi, Y.; Nakawa, J.I.; Yamashita, S. !$#submission submitted to the EMBL Data Library, September 1990 !$#accession S61931 !'##molecule_type DNA !'##residues 1-90,'G',91-104,106-191,'H',193-424 ##label TSU !'##cross-references EMBL:M36827; NID:g171178; PIDN:AAA91962.1; !1PID:g171179 REFERENCE S64517 !$#authors Guerreiro, P.; Barreiros, T.; Cyrne, L.; Soares, H.; Maia e !1Silva, A.; Rodrigues-Pousada, C. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64524 !'##molecule_type DNA !'##residues 1-424 ##label GUW !'##cross-references EMBL:Z72987; NID:g1323360; PIDN:CAA97229.1; !1PID:g1323361; GSPDB:GN00007; MIPS:YGR202c !'##experimental_source strain S288C REFERENCE S63848 !$#authors Guerreiro, P.; Barreiros, T.; Soares, H.; Cyrne, L.; Maia e !1Silva, A.; Rodrigues-Pousada, C. !$#journal Yeast (1996) 12:273-280 !$#title Sequencing of a 17.6 kb segment on the right arm of yeast !1chromosome VII reveals 12 ORFs, including CCT, ADE3 and TR-I !1genes, homologues of the yeast PMT and EF1G genes, of the !1human and bacterial electron-transferring flavoproteins !1(beta-chain) and of the Escherichia coli phosphoserine !1phosphohydrolase, and five new ORFs. !$#cross-references MUID:97060019; PMID:8904340 !$#accession S63851 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-424 ##label GUF !'##cross-references EMBL:Z49133; NID:g790489; PIDN:CAA88995.1; !1PID:g790493 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1995 GENETICS !$#gene SGD:PCT1; CCT1; BSR2; MIPS:YGR202c !'##cross-references SGD:S0003434; MIPS:YGR202c !$#map_position 7R FUNCTION !$#description catalyzes the formation of cytidinediphosphate choline and !1pyrophosphate from cytidinetriphosphate and choline !1phosphate !$#pathway phospholipid biosynthesis CLASSIFICATION #superfamily choline-phosphate cytidylyltransferase KEYWORDS nucleotidyltransferase; nucleus; phospholipid biosynthesis; !1phosphoprotein FEATURE !$25-31 #region nuclear location signal\ !$61-65 #region nuclear location signal SUMMARY #length 424 #molecular-weight 49406 #checksum 157 SEQUENCE /// ENTRY S68187 #type complete TITLE choline-phosphate cytidylyltransferase (EC 2.7.7.15) - malaria parasite (Plasmodium falciparum) ALTERNATE_NAMES CTP:choline-phosphate cytidylyltransferase; phosphorylcholine transferase ORGANISM #formal_name Plasmodium falciparum DATE 28-Oct-1996 #sequence_revision 13-Mar-1997 #text_change 09-Jun-2000 ACCESSIONS S68187 REFERENCE S68187 !$#authors Yeo, H.J.; Sri Widada, J.; Mercereau-Puijalon, O.; Vial, !1H.J. !$#journal Eur. J. Biochem. (1995) 233:62-72 !$#title Molecular cloning of CTP:phosphocholine cytidylyltransferase !1from Plasmodium falciparum. !$#cross-references MUID:96061933; PMID:7588775 !$#accession S68187 !'##molecule_type DNA !'##residues 1-370 ##label YEO !'##cross-references EMBL:X84041; NID:g1054826; PIDN:CAA58860.1; !1PID:g1054827 GENETICS !$#gene CTP !$#introns #status absent FUNCTION !$#description catalyzes the formation of cytidinediphosphate choline and !1pyrophosphate from cytidinetriphosphate and choline !1phosphate !$#pathway phospholipid biosynthesis CLASSIFICATION #superfamily choline-phosphate cytidylyltransferase KEYWORDS membrane-associated protein; nucleotidyltransferase; !1phospholipid biosynthesis FEATURE !$274-294 #domain amphipathic helix #status predicted #label !8AH1\ !$308-324 #domain amphipathic helix #status predicted #label !8AH2 SUMMARY #length 370 #molecular-weight 42630 #checksum 6395 SEQUENCE /// ENTRY S35294 #type complete TITLE probable glucose-1-phosphate thymidylyltransferase (EC 2.7.7.24) - Yersinia enterocolitica ORGANISM #formal_name Yersinia enterocolitica DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S35294; S28577 REFERENCE S35292 !$#authors Zhang, L.; Al-Hendy, A.; Toivanen, P.; Skurnik, M. !$#journal Mol. Microbiol. (1993) 9:309-321 !$#title Genetic organization and sequence of the rfb gene cluster of !1Yersinia enterocolitica serotype O:3: similarities to the !1dTDP-L-rhamnose biosynthesis pathway of Salmonella and to !1the bacterial polysaccharide transport systems. !$#cross-references MUID:94018626; PMID:7692217 !$#accession S35294 !'##molecule_type DNA !'##residues 1-289 ##label ZHA !'##cross-references EMBL:Z18920; NID:g48582; PIDN:CAA79347.1; !1PID:g48585 !'##experimental_source serotype O:3 GENETICS !$#gene rfbA FUNCTION !$#description catalyzes formation of dTDPglucose and pyrophosphate from !1alpha-D-glucose-1-phosphate and dTTP !$#pathway dTDP-L-rhamnose biosynthesis CLASSIFICATION #superfamily glucose-1-phosphate thymidylytransferase KEYWORDS lipopolysaccharide biosynthesis; nucleotidyltransferase SUMMARY #length 289 #molecular-weight 32402 #checksum 6416 SEQUENCE /// ENTRY XNECAD #type complete TITLE AAD(2'') aminoglycoside adenylyltransferase (EC 2.7.7.-) - Escherichia coli plasmid pDGO100 ORGANISM #formal_name Escherichia coli DATE 30-Sep-1988 #sequence_revision 30-Jun-1992 #text_change 18-Aug-2000 ACCESSIONS A25536; S60908; T45121 REFERENCE A25536 !$#authors Cameron, F.H.; Obbink, D.J.G.; Ackerman, V.P.; Hall, R.M. !$#journal Nucleic Acids Res. (1986) 14:8625-8635 !$#title Nucleotide sequence of the AAD(2") aminoglycoside !1adenylyltransferase determinant aadB. Evolutionary !1relationship of this region with those surrounding aadA in !1R538-1 and dhfrII in R388. !$#cross-references MUID:87066734; PMID:3024112 !$#accession A25536 !'##molecule_type DNA !'##residues 1-177 ##label CAM !'##cross-references GB:Z47410; NID:g623029; PIDN:CAA87463.1; !1PID:g1065719 REFERENCE S60908 !$#authors Recchia, G.D.; Hall, R.M. !$#journal Mol. Microbiol. (1995) 15:179-187 !$#title Plasmid evolution by acquisition of mobile gene cassettes: !1plasmid pIE723 contains the aadB gene cassette precisely !1inserted at a secondary site in the IncQ plasmid RSF 1010. !$#cross-references MUID:95272390; PMID:7752893 !$#accession S60908 !'##status preliminary !'##molecule_type DNA !'##residues 1-177 ##label REC !'##cross-references EMBL:U14415; NID:g540196; PIDN:AAA85811.1; !1PID:g540197 REFERENCE Z22920 !$#authors Stokes, H.W.; Tomaras, C.; Parsons, Y.; Hall, R.M. !$#journal Plasmid (1993) 30:39-50 !$#title The partial 3'-conserved segment duplications in the !1integrons In6 from pSa and In7 from pDGO100 have a common !1origin. !$#cross-references MUID:93391548; PMID:8378445 !$#accession T45121 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-177 ##label STO !'##cross-references EMBL:L06418; NID:g149116; PIDN:AAA92745.1; !1PID:g149118 GENETICS !$#gene aadB; aad !$#genome plasmid pDGO100 FUNCTION !$#description this enzyme confers resistance to kanamycin, gentamicin, and !1tobramycin by adenylating the 2"-hydroxyl group of these !1antibiotics CLASSIFICATION #superfamily AAD(2'') aminoglycoside adenylyltransferase KEYWORDS antibiotic resistance; nucleotidyltransferase SUMMARY #length 177 #molecular-weight 19873 #checksum 1006 SEQUENCE /// ENTRY XNKBGP #type complete TITLE gentamycin 2 - Klebsiella pneumoniae transposon Tn4000 and plasmid pBWH1 ALTERNATE_NAMES gentamicin resistance protein ORGANISM #formal_name Klebsiella pneumoniae DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 03-Jun-2002 ACCESSIONS S04170; S19939 REFERENCE S04170 !$#authors Schmidt, F.R.J.; Nuecken, E.J.; Henschke, R.B. !$#submission submitted to the EMBL Data Library, August 1988 !$#description Nucleotide sequence analysis of 2"-aminoglyoside nucleotide !1transferase ANT(2'') from TN4000, its relationship to AAD !1(3'') and impact on TN2 evolution. !$#accession S04170 !'##molecule_type DNA !'##residues 1-177 ##label SCH !'##cross-references EMBL:X12618; NID:g43945; PIDN:CAA31139.1; !1PID:g43946 !'##experimental_source transposon Tn4000 !'##genetics TRA REFERENCE S19939 !$#authors Zieg, J.; Jiang, H.; McCabe, F.; O'Brien, T. !$#submission submitted to the EMBL Data Library, February 1992 !$#description Molecular characterization and comparison of the regions !1encoding gentamicin resistance (aadB) in pBWH1 and pLST1000 !1and their relationship to Tn21 family of transposons and !1elements. !$#accession S19939 !'##molecule_type DNA !'##residues 1-177 ##label ZIE !'##cross-references EMBL:X64368; NID:g43791; PIDN:CAA45721.1; !1PID:g43792 !'##experimental_source plasmid pBWH1 !'##genetics PLA GENETICS TRA !$#gene aadB !$#genome transposon GENETICS PLA !$#gene aadB !$#genome plasmid CLASSIFICATION #superfamily AAD(2'') aminoglycoside adenylyltransferase KEYWORDS antibiotic resistance; gentamicin resistance; !1nucleotidyltransferase SUMMARY #length 177 #molecular-weight 19873 #checksum 1006 SEQUENCE /// ENTRY XNKBLS #type complete TITLE gentamycin 2 - Klebsiella pneumoniae plasmid pLST1000 ALTERNATE_NAMES gentamicin resistance protein ORGANISM #formal_name Klebsiella pneumoniae DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 03-Jun-2002 ACCESSIONS S19940 REFERENCE S19939 !$#authors Zieg, J.; Jiang, H.; McCabe, F.; O'Brien, T. !$#submission submitted to the EMBL Data Library, February 1992 !$#description Molecular characterization and comparison of the regions !1encoding gentamicin resistance (aadB) in pBWH1 and pLST1000 !1and their relationship to Tn21 family of transposons and !1elements. !$#accession S19940 !'##molecule_type DNA !'##residues 1-177 ##label ZIE !'##cross-references EMBL:X64369; NID:g43793; PIDN:CAA45722.1; !1PID:g43794 GENETICS !$#gene aadB !$#genome plasmid CLASSIFICATION #superfamily AAD(2'') aminoglycoside adenylyltransferase KEYWORDS antibiotic resistance; gentamicin resistance; !1nucleotidyltransferase SUMMARY #length 177 #molecular-weight 19861 #checksum 1168 SEQUENCE /// ENTRY XXBSG #type complete TITLE aminoglycoside 6-adenylyltransferase (EC 2.7.7.-) - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jun-2000 ACCESSIONS JU0059; A69580 REFERENCE JU0059 !$#authors Ohmiya, K.; Tanaka, T.; Noguchi, N.; O'Hara, K.; Kono, M. !$#journal Gene (1989) 78:377-378 !$#title Nucleotide sequence of the chromosomal gene coding for the !1aminoglycoside 6-adenylyltransferase from Bacillus subtilis !1Marburg 168. !$#cross-references MUID:89378765; PMID:2550327 !$#accession JU0059 !'##molecule_type DNA !'##residues 1-284 ##label OHM !'##cross-references GB:M26879; NID:g341549; PIDN:AAA22190.1; !1PID:g529016 !'##experimental_source strain Marburg 168 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69580 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-284 ##label KUN !'##cross-references GB:Z99117; GB:AL009126; NID:g2634966; !1PIDN:CAB14620.1; PID:g2635124 !'##experimental_source strain 168 GENETICS !$#gene aadK CLASSIFICATION #superfamily aminoglycoside 6-adenylyltransferase KEYWORDS nucleotidyltransferase SUMMARY #length 284 #molecular-weight 33907 #checksum 8240 SEQUENCE /// ENTRY RNECTA #type complete TITLE tRNA adenylyltransferase (EC 2.7.7.25) - Escherichia coli (strain K-12) ALTERNATE_NAMES tRNA CCA-pyrophosphorylase; tRNA nucleotidyltransferase ORGANISM #formal_name Escherichia coli DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 01-Mar-2002 ACCESSIONS A25215; F65093 REFERENCE A25215 !$#authors Cudny, H.; Lupski, J.R.; Godson, G.N.; Deutscher, M.P. !$#journal J. Biol. Chem. (1986) 261:6444-6449 !$#title Cloning, sequencing, and species relatedness of the !1Escherichia coli cca gene encoding the enzyme tRNA !1nucleotidyltransferase. !$#cross-references MUID:86196066; PMID:3009457 !$#accession A25215 !'##molecule_type DNA !'##residues 1-412 ##label CUD !'##cross-references GB:M12788; NID:g145467; PIDN:AAA23541.1; !1PID:g145468 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65093 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-412 ##label BLAT !'##cross-references GB:AE000387; GB:U00096; NID:g1789431; !1PIDN:AAC76092.1; PID:g1789436; UWGP:b3056 !'##experimental_source strain K-12, substrain MG1655 COMMENT This enzyme, which may be identical with tRNA !1cytidylyltransferase (EC 2.7.7.21), catalyzes the !1incorporation of AMP and CMP residues into tRNAs having !1incomplete CCA 3' ends to form the trinucleotide sequence !1CAA, which is required for all tRNA functions. GENETICS !$#gene cca !$#map_position 67 min !$#start_codon GTG CLASSIFICATION #superfamily Escherichia coli tRNA adenylyltransferase KEYWORDS nucleotidyltransferase SUMMARY #length 412 #molecular-weight 46467 #checksum 553 SEQUENCE /// ENTRY S11180 #type complete TITLE tRNA adenylyltransferase (EC 2.7.7.25) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YER168c; tRNA CCA-pyrophosphorylase ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 21-Jul-2000 ACCESSIONS S11180; S50671 REFERENCE S11180 !$#authors Aebi, M.; Kirchner, G.; Chen, J.Y.; Vijayraghavan, U.; !1Jacobson, A.; Martin, N.C.; Abelson, J. !$#journal J. Biol. Chem. (1990) 265:16216-16220 !$#title Isolation of a temperature-sensitive mutant with an altered !1tRNA nucleotidyltransferase and cloning of the gene encoding !1tRNA nucleotidyltransferase in the yeast Saccharomyces !1cerevisiae. !$#cross-references MUID:90375480; PMID:2204621 !$#accession S11180 !'##molecule_type DNA !'##residues 1-546 ##label AEB !'##cross-references EMBL:M59870; NID:g172993; PIDN:AAA35160.1; !1PID:g172994 REFERENCE S50671 !$#authors Dietrich, F.S. !$#submission submitted to the EMBL Data Library, December 1994 !$#description The sequence of S. cerevisiae cosmids 9163 and 9132. !$#accession S50671 !'##molecule_type DNA !'##residues 1-546 ##label DIE !'##cross-references EMBL:U18922; NID:g603405; PIDN:AAB64695.1; !1PID:g603409; GSPDB:GN00005; MIPS:YER168c GENETICS !$#gene SGD:CCA1; TNT1; MIPS:YER168c !'##cross-references SGD:S0000970; MIPS:YER168c !$#map_position 5R FUNCTION !$#description catalyzes the addition of ATP and CTP to form the -CCA !13'-terminus of tRNA and releasing pyrophosphate CLASSIFICATION #superfamily yeast tRNA adenylyltransferase KEYWORDS alternative initiators; cytosol; mitochondrion; !1nucleotidyltransferase; nucleus SUMMARY #length 546 #molecular-weight 62484 #checksum 3733 SEQUENCE /// ENTRY YUEC #type complete TITLE glucose-1-phosphate adenylyltransferase (EC 2.7.7.27) - Escherichia coli (strain K-12) ALTERNATE_NAMES ADP-glucose pyrophosphorylase; ADP-glucose synthase ORGANISM #formal_name Escherichia coli DATE 30-Nov-1980 #sequence_revision 05-Jan-1996 #text_change 01-Mar-2002 ACCESSIONS A00721; A60934; S32522; A56780; A65139; I41233 REFERENCE A00721 !$#authors Baecker, P.A.; Furlong, C.E.; Preiss, J. !$#journal J. Biol. Chem. (1983) 258:5084-5088 !$#title Biosynthesis of bacterial glycogen. Primary structure of !1Escherichia coli ADP-glucose synthetase as deduced from the !1nucleotide sequence of the glg C gene. !$#cross-references MUID:83161127; PMID:6300111 !$#accession A00721 !'##molecule_type DNA !'##residues 1-160,'V',162-165,'V',167-188,'T',190-295,'K',297-431 !1##label BAE !'##cross-references GB:V00281; GB:S37921; NID:g41555; PIDN:CAA23544.1; !1PID:g41556 !'##experimental_source strain K12 !'##note corrections to this sequence were reported in reference A60934 REFERENCE A60934 !$#authors Kumar, A.; Ghosh, P.; Lee, Y.M.; Hill, M.A.; Preiss, J. !$#journal J. Biol. Chem. (1989) 264:10464-10471 !$#title Biosynthesis of bacterial glycogen. Determination of the !1amino acid changes that alter the regulatory properties of a !1mutant Escherichia coli ADP-glucose synthetase. !$#cross-references MUID:89278107; PMID:2543670 !$#accession A60934 !'##molecule_type DNA !'##residues 140-200 ##label KUM !'##note only differences with respect to reference A00721 are shown REFERENCE S32522 !$#authors Meyer, C.R.; Ghosh, P.; Nadler, S.; Preiss, J. !$#journal Arch. Biochem. Biophys. (1993) 302:64-71 !$#title Cloning, expression, and sequence of an allosteric mutant !1ADPglucose pyrophosphorylase from Escherichia coli B. !$#cross-references MUID:93228367; PMID:8385906 !$#accession S32522 !'##molecule_type DNA !'##residues 1-43,'T',45-431 ##label MEY !'##cross-references GB:S58224; NID:g299129; PIDN:AAB26162.1; !1PID:g299130 REFERENCE A56780 !$#authors Ghosh, P.; Meyer, C.; Remy, E.; Peterson, D.; Preiss, J. !$#journal Arch. Biochem. Biophys. (1992) 296:122-128 !$#title Cloning, expression, and nucleotide sequence of glgC gene !1from an allosteric mutant of Escherichia coli B. !$#cross-references MUID:92296745; PMID:1339262 !$#accession A56780 !'##molecule_type DNA !'##residues 1-66,'C',68-431 ##label GHO !'##experimental_source E. coli B, strain CL1136 !'##note sequence extracted from NCBI backbone (NCBIN:106023, !1NCBIP:106025) !'##note the single amino acid difference in this mutant leads to less !1dependence on the allosteric activator fructose 1, !16-bisphosphate and less inhibition by AMP REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65139 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-431 ##label BLAT !'##cross-references GB:AE000419; GB:U00096; NID:g2367227; !1PIDN:AAC76455.1; PID:g1789837; UWGP:b3430 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A42892 !$#authors Meyer, C.R.; Ghosh, P.; Remy, E.; Preiss, J. !$#journal J. Bacteriol. (1992) 174:4509-4512 !$#title Cloning, expression, and nucleotide sequence of a mutant !1glgC gene from Escherichia coli B. !$#cross-references MUID:92325040; PMID:1320612 !$#accession I41233 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-160,'V',162-165,'V',167-188,'T',190-294,'SK',297-431 !1##label RES !'##cross-references GB:M97226; NID:g146143; PIDN:AAA23873.1; !1PID:g146144 COMMENT Lys-39 and Lys-195 can be modified by reductive !1phosphopyridoxylation; they are involved in allosteric !1activator binding and in substrate binding, respectively. GENETICS !$#gene glgC !$#map_position 75 min FUNCTION !$#description catalyzes the formation of ADPglucose and pyrophosphate from !1alpha-D-glucose 1-phosphate and ATP !$#pathway glycogen/starch biosynthesis (ADPglucose-utilizing) !$#note activated by fructose-1,6-bisphosphate; inhibited by AMP CLASSIFICATION #superfamily glucose-1-phosphate adenylyltransferase KEYWORDS allosteric regulation; glycogen/starch biosynthesis; !1nucleotidyltransferase FEATURE !$39 #binding_site fructose-1,6-bisphosphate (Lys) #status !8experimental\ !$114 #binding_site substrate (Tyr) #status experimental\ !$195 #binding_site substrate (Lys) #status experimental SUMMARY #length 431 #molecular-weight 48697 #checksum 2547 SEQUENCE /// ENTRY A34318 #type complete TITLE glucose-1-phosphate adenylyltransferase (EC 2.7.7.27) precursor - rice ORGANISM #formal_name Oryza sativa #common_name rice DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A34318 REFERENCE A34318 !$#authors Anderson, J.M.; Hnilo, J.; Larson, R.; Okita, T.W.; Morell, !1M.; Preiss, J. !$#journal J. Biol. Chem. (1989) 264:12238-12242 !$#title The encoded primary sequence of a rice seed ADP-glucose !1pyrophosphorylase subunit and its homology to the bacterial !1enzyme. !$#cross-references MUID:89308643; PMID:2545704 !$#accession A34318 !'##status preliminary !'##molecule_type mRNA !'##residues 1-483 ##label AND !'##cross-references GB:J04960; NID:g169758; PIDN:AAA33890.1; !1PID:g169759 FUNCTION !$#description catalyzes the formation of ADPglucose and pyrophosphate from !1alpha-D-glucose 1-phosphate and ATP !$#pathway glycogen/starch biosynthesis (ADPglucose-utilizing) CLASSIFICATION #superfamily glucose-1-phosphate adenylyltransferase KEYWORDS chloroplast; glycogen/starch biosynthesis; !1nucleotidyltransferase SUMMARY #length 483 #molecular-weight 53496 #checksum 8584 SEQUENCE /// ENTRY G64045 #type complete TITLE 3-deoxy-manno-octulosonate cytidylyltransferase (EC 2.7.7.38) - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS G64045 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession G64045 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-254 ##label TIGR !'##cross-references GB:U32691; GB:L42023; NID:g1573004; !1PIDN:AAC21736.1; PID:g1573006; TIGR:HI0058 GENETICS !$#gene kdsB FUNCTION !$#description catalyzes activation of KDO via formation of CMP-KDO, which !1is required for incorporation of KDO into lipid A !$#note requires magnesium CLASSIFICATION #superfamily 3-deoxy-manno-octulosonate cytidylyltransferase KEYWORDS magnesium; nucleotidyltransferase SUMMARY #length 254 #molecular-weight 28255 #checksum 1198 SEQUENCE /// ENTRY WXHU #type complete TITLE DNA nucleotidylexotransferase (EC 2.7.7.31) - human ALTERNATE_NAMES terminal addition enzyme; terminal deoxynucleotidyltransferase (TdT); terminal transferase ORGANISM #formal_name Homo sapiens #common_name man DATE 04-Dec-1986 #sequence_revision 19-Oct-1995 #text_change 11-Jun-1999 ACCESSIONS A23924; I52227; A00722 REFERENCE A23924 !$#authors Peterson, R.C.; Cheung, L.C.; Mattaliano, R.J.; White, S.T.; !1Chang, L.M.S.; Bollum, F.J. !$#journal J. Biol. Chem. (1985) 260:10495-10502 !$#title Expression of human terminal deoxynucleotidyl transferase in !1Escherichia coli. !$#cross-references MUID:85289229; PMID:2863268 !$#accession A23924 !'##molecule_type mRNA !'##residues 1-508 ##label PET !'##cross-references GB:M11722; GB:M28451; NID:g339436; PIDN:AAA36726.1; !1PID:g339437 REFERENCE I52227 !$#authors Koiwai, O.; Morita, A. !$#journal Biochem. Biophys. Res. Commun. (1988) 154:91-100 !$#title Isolation of putative promoter region for human terminal !1deoxynucleotidyltransferase gene. !$#cross-references MUID:88280821; PMID:3395350 !$#accession I52227 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-67 ##label KOI !'##cross-references GB:M21195; NID:g339438; PIDN:AAA61137.1; !1PID:g553787 REFERENCE A93995 !$#authors Peterson, R.C.; Cheung, L.C.; Mattaliano, R.J.; Chang, !1L.M.S.; Bollum, F.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:4363-4367 !$#title Molecular cloning of human terminal !1deoxynucleotidyltransferase. !$#cross-references MUID:84272638; PMID:6087320 !$#accession A00722 !'##molecule_type mRNA !'##residues 271-508 ##label PE2 !'##cross-references GB:K01919; NID:g339434; PIDN:AAA61136.1; !1PID:g339435 COMMENT This magnesium-requiring enzyme catalyzes the polymerization !1of deoxynucleoside triphosphates, elongating !1polydeoxynucleotide chains by terminal addition; it is !1distinct from the replicative deoxynucleotidyltransferase !1(DNA polymerase), which is able to copy a template. COMMENT Although the specific biological role of the enzyme is not !1known, very high levels of enzyme activity have been !1detected in certain acute leukemic cells. This enzyme has !1been a useful tool for the synthesis of model !1polydeoxynucleotides and the construction of recombinant !1DNA. GENETICS !$#gene GDB:DNTT !'##cross-references GDB:119100; OMIM:187410 !$#map_position 10q23-10q24 CLASSIFICATION #superfamily DNA nucleotidylexotransferase KEYWORDS magnesium; nucleotidyltransferase SUMMARY #length 508 #molecular-weight 58308 #checksum 1658 SEQUENCE /// ENTRY A23595 #type complete TITLE DNA nucleotidylexotransferase (EC 2.7.7.31) long form - bovine ALTERNATE_NAMES terminal addition enzyme; terminal deoxyribonucleotidyltransferase (TdT); terminal transferase ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A23595; A60467; A05052; A29948; A32198; PC2127; PC2128; !1I45884 REFERENCE A93633 !$#authors Koiwai, O.; Yokota, T.; Kageyama, T.; Hirose, T.; Yoshida, !1S.; Arai, K. !$#journal Nucleic Acids Res. (1986) 14:5777-5792 !$#title Isolation and characterization of bovine and mouse terminal !1deoxynucleotidyltransferase cDNAs expressible in mammalian !1cells. !$#cross-references MUID:86286588; PMID:3755527 !$#accession A23595 !'##molecule_type mRNA !'##residues 1-302,321-510,520-547 ##label KOI !'##cross-references GB:X04122; NID:g767; PIDN:CAA27734.1; PID:g768 !'##note it is uncertain whether Met-1 or Met-12 is the initiator REFERENCE A60467 !$#authors Evans, R.K.; Beach, C.M.; Coleman, M.S. !$#journal Biochemistry (1989) 28:713-720 !$#title Photoaffinity labeling of terminal deoxynucleotidyl !1transferase. Identification of peptides in the nucleotide !1binding domain. !$#cross-references MUID:89229071; PMID:2713339 !$#accession A60467 !'##molecule_type protein !'##residues 143-179,'X',181-187,'XXXXXX',194-199,'XX',202-230,'XXX', !1234-303;322-363,'X',365-444,'XXXXX',450-510;520-547 ##label !1EVA REFERENCE A93995 !$#authors Peterson, R.C.; Cheung, L.C.; Mattaliano, R.J.; Chang, !1L.M.S.; Bollum, F.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:4363-4367 !$#title Molecular cloning of human terminal !1deoxynucleotidyltransferase. !$#cross-references MUID:84272638; PMID:6087320 !$#accession A05052 !'##molecule_type protein !'##residues 335-348,'X',350-355;366-377,'XX',380-381,'X', !1383-386;521-526,'X',528-533,'X',535-544 ##label PET REFERENCE A29948 !$#authors Pandey, V.; Modak, M.J. !$#journal J. Biol. Chem. (1988) 263:3744-3751 !$#title Biochemistry of terminal deoxynucleotidyltransferase. !1Affinity labeling and identification of the deoxynucleoside !1triphosphate binding domain of terminal !1deoxynucleotidyltransferase. !$#cross-references MUID:88153669; PMID:3346221 !$#accession A29948 !'##molecule_type protein !'##residues 221-226,'X',228-231,'X',235-249 ##label PAN REFERENCE A32198 !$#authors Pandey, V.N.; Modak, M.J. !$#journal J. Biol. Chem. (1989) 264:867-871 !$#title Biochemistry of terminal deoxynucleotidyltransferase. !1Identification and unity of ribo- and deoxyribonucleoside !1triphosphate binding site in terminal !1deoxynucleotidyltransferase. !$#cross-references MUID:89093157; PMID:2910867 !$#accession A32198 !'##molecule_type protein !'##residues 221-226,'X',228-231,'X',235-249 ##label PA2 REFERENCE PC2127 !$#authors Takahara, K.; Hayashi, N.; Fujita-Sagawa, K.; Morishita, T.; !1Hashimoto, Y.; Noda, A. !$#journal Biosci. Biotechnol. Biochem. (1994) 58:786-787 !$#title Alternative splicing of bovine terminal deoxynucleotidyl !1transferase cDNA. !$#cross-references MUID:94264411; PMID:7515727 !$#accession PC2127 !'##molecule_type DNA !'##residues 303-320 ##label TAK !'##cross-references GB:D17451 !$#accession PC2128 !'##molecule_type DNA !'##residues 511-519 ##label TA2 !'##cross-references GB:D17452 REFERENCE I45884 !$#authors Koiwai, O.; Kaneda, T.; Morishita, R. !$#journal Biochem. Biophys. Res. Commun. (1987) 144:185-190 !$#title Analysis of human terminal deoxynucleotidyl transferase cDNA !1expressible in mammalian cells. !$#cross-references MUID:87213162; PMID:3579900 !$#accession I45884 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-13 ##label KO2 !'##cross-references GB:M26146; NID:g951177; PIDN:AAA87354.1; !1PID:g951178 COMMENT This protein can be isolated as a single polypeptide chain !1or as a heterodimer of a 26-kilodalton beta chain and an !18-kilodalton alpha chain. GENETICS !$#gene DNTT CLASSIFICATION #superfamily DNA nucleotidylexotransferase KEYWORDS alternative splicing; magnesium; nucleotidyltransferase FEATURE !$1-510,520-547 #product DNA nucleotidylexotransferase long form I !8#status predicted #label MA1\ !$1-302,321-547 #product DNA nucleotidylexotransferase long form II !8#status predicted #label MA2\ !$1-302,321-510, !$520-547 #product DNA nucleotidylexotransferase short form !8#status predicted #label MAT\ !$224-237 #region substrate binding SUMMARY #length 547 #molecular-weight 62590 #checksum 1883 SEQUENCE /// ENTRY SYECDG #type complete TITLE phosphatidate cytidylyltransferase (EC 2.7.7.41) - Escherichia coli (strain K-12) ALTERNATE_NAMES CDP-diglyceride pyrophosphorylase; CDP-diglyceride synthetase ORGANISM #formal_name Escherichia coli DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 01-Mar-2002 ACCESSIONS A23898; G64741 REFERENCE A23898 !$#authors Icho, T.; Sparrow, C.P.; Raetz, C.R.H. !$#journal J. Biol. Chem. (1985) 260:12078-12083 !$#title Molecular cloning and sequencing of the gene for !1CDP-diglyceride synthetase of Escherichia coli. !$#cross-references MUID:86008268; PMID:2995358 !$#accession A23898 !'##molecule_type DNA !'##residues 1-249 ##label ICH !'##cross-references GB:M11330; NID:g145475; PIDN:AAA23545.1; !1PID:g145476 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64741 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-249 ##label BLAT !'##cross-references GB:AE000127; GB:U00096; NID:g1786370; !1PIDN:AAC73286.1; PID:g1786372; UWGP:b0175 !'##experimental_source strain K-12, substrain MG1655 COMMENT This membrane-bound enzyme catalyzes the formation of !1CDP-diglyceride from phosphatidic acid and CTP; !1CDP-diglyceride then transfers the phosphatidyl moiety to !1various alcohols during phospholipid biosynthesis. GENETICS !$#gene cdsA; cds !$#map_position 4 min CLASSIFICATION #superfamily phosphatidate cytidylyltransferase KEYWORDS nucleotidyltransferase; phospholipid biosynthesis; !1transmembrane protein FEATURE !$20-36 #domain transmembrane #status predicted #label TM1\ !$53-69 #domain transmembrane #status predicted #label TM2\ !$85-101 #domain transmembrane #status predicted #label TM3\ !$112-128 #domain transmembrane #status predicted #label TM4\ !$182-198 #domain transmembrane #status predicted #label TM5\ !$230-246 #domain transmembrane #status predicted #label TM6 SUMMARY #length 249 #molecular-weight 27570 #checksum 310 SEQUENCE /// ENTRY XUECSA #type complete TITLE streptomycin 3 - Escherichia coli transposon Tn7 ALTERNATE_NAMES 3''(9)-O-nucleotidyltransferase ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 03-Jun-2002 ACCESSIONS A24273 REFERENCE A24273 !$#authors Fling, M.E.; Kopf, J.; Richards, C. !$#journal Nucleic Acids Res. (1985) 13:7095-7106 !$#title Nucleotide sequence of the transposon Tn7 gene encoding an !1aminoglycoside-modifying enzyme, 3" !1(9)-O-nucleotidyltransferase. !$#cross-references MUID:86041899; PMID:2997737 !$#accession A24273 !'##molecule_type DNA !'##residues 1-262 ##label FLI !'##cross-references GB:X03043; NID:g43692; PIDN:CAA26848.1; PID:g43693 COMMENT This enzyme catalyzes the reaction transferring the adenylyl !1group from ATP to the hydroxy group on the aminoglycoside !1ring of streptomycin (or the actinamine ring of !1spectinomycin); therefore, it mediates bacterial resistance !1to these antibiotics. GENETICS !$#gene aadA CLASSIFICATION #superfamily streptomycin 3''-adenylyltransferase KEYWORDS antibiotic resistance; nucleotidyltransferase SUMMARY #length 262 #molecular-weight 29203 #checksum 9692 SEQUENCE /// ENTRY S25252 #type complete TITLE streptomycin 3 - Salmonella choleraesuis ORGANISM #formal_name Salmonella choleraesuis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S25252 REFERENCE S25252 !$#authors Leung, K.Y.; Ruschkowski, S.R.; Finlay, B.B. !$#journal Mol. Microbiol. (1992) 6:2453-2460 !$#title Isolation and characterization of the aadA !1aminoglycoside-resistance gene from Salmonella choleraesuis. !$#cross-references MUID:93023874; PMID:1406282 !$#accession S25252 !'##molecule_type DNA !'##residues 1-262 ##label LEU !'##cross-references EMBL:X68089; NID:g46790; PIDN:CAA48215.1; !1PID:g46791 GENETICS !$#gene aadA CLASSIFICATION #superfamily streptomycin 3''-adenylyltransferase KEYWORDS antibiotic resistance; nucleotidyltransferase SUMMARY #length 262 #molecular-weight 29371 #checksum 9903 SEQUENCE /// ENTRY RRBPBM #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) beta chain - phage MS2 ALTERNATE_NAMES RNA replicase beta chain ORGANISM #formal_name phage MS2 DATE 24-Apr-1984 #sequence_revision 23-Oct-1998 #text_change 11-Jun-1999 ACCESSIONS A00723; A58887 REFERENCE A93179 !$#authors Fiers, W.; Contreras, R.; Duerinck, F.; Haegeman, G.; !1Iserentant, D.; Merregaert, J.; Min Jou, W.; Molemans, F.; !1Raeymaekers, A.; van den Berghe, A.; Volckaert, G.; !1Ysebaert, M. !$#journal Nature (1976) 260:500-507 !$#title Complete nucleotide sequence of bacteriophage MS2 RNA: !1primary and secondary structure of the replicase gene. !$#cross-references MUID:76174431; PMID:1264203 !$#accession A00723 !'##molecule_type genomic RNA !'##residues 2-170,'A',172-545 ##label FIE !'##cross-references GB:V00642; GB:J02467; NID:g15081; GB:M24961; !1NID:g215232 !'##note translation of initiator Met is not shown REFERENCE A58887 !$#authors Min Jou, W. !$#submission submitted to the EMBL Data Library, January 1983 !$#contents erratum !$#accession A58887 !'##status translated from GB/EMBL/DDBJ !'##molecule_type genomic RNA !'##residues 1-545 ##label MIN !'##cross-references GB:V00642; GB:J02467; NID:g15081; PIDN:CAA23991.1; !1PID:g15085; GB:M24961; NID:g215232; PID:g215236 !'##note corrects codons for 170-171 from GCCGCG, Ala-Ala to GCGCCG, !1Ala-Pro COMPLEX viral RNA-dependent RNA polymerase is a heterotetramer of !1beta chain and host encoded alpha, gamma, and delta chains, !1respectively ribosomal protein S1 (see PIR:R3EC1), !1translation elongation factor EF-Tu (see PIR:EFECT, !1PIR:EFECTA), and translation elongation factor EF-Ts (see !1PIR:EFECS) CLASSIFICATION #superfamily phage MS2 RNA-directed RNA polymerase KEYWORDS heterotetramer; nucleotidyltransferase FEATURE !$2-545 #product RNA-directed RNA polymerase beta chain !8#status predicted #label MAT SUMMARY #length 545 #molecular-weight 60811 #checksum 4664 SEQUENCE /// ENTRY S08020 #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) beta chain - phage fr ALTERNATE_NAMES replicase ORGANISM #formal_name phage fr DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 23-Mar-2001 ACCESSIONS S08020; JN0376; S13145 REFERENCE S08017 !$#authors Adhin, M.R.; Avots, A.; Berzin, V.; Overbeek, G.P.; van !1Duin, J. !$#submission submitted to the EMBL Data Library, April 1989 !$#description Complete nucleotide sequence of RNA bacteriophage fr. !$#accession S08020 !'##molecule_type genomic RNA !'##residues 1-545 ##label ADH !'##cross-references EMBL:X15031; NID:g15071; PIDN:CAA33138.1; !1PID:g15075 REFERENCE JN0375 !$#authors Berzin, B.M.; Gribanov, B.A.; Tsielens, I.A.; Yansone, H.B.; !1Gren, A.Y. !$#journal Bioorg. Khim. (1981) 7:306-307 !$#title Structure of regulator part of phage fr replicase gene. !$#accession JN0376 !'##molecule_type genomic RNA !'##residues 1-11 ##label BER REFERENCE S13075 !$#authors Adhin, M.R.; Avots, A.; Berzin, V.; Overbeek, G.P.; van !1Duin, J. !$#journal Biochim. Biophys. Acta (1990) 1050:104-109 !$#title Complete nucleotide sequence of the group I RNA !1bacteriophage fr. !$#cross-references MUID:91002624; PMID:2207135 !$#accession S13145 !'##status preliminary !'##molecule_type genomic RNA !'##residues 2-545 ##label AD2 !'##cross-references GB:X15031; NID:g15071; PIDN:CAA33138.1; PID:g15075 CLASSIFICATION #superfamily phage MS2 RNA-directed RNA polymerase KEYWORDS nucleotidyltransferase SUMMARY #length 545 #molecular-weight 61339 #checksum 7899 SEQUENCE /// ENTRY RRBPBG #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) beta chain - phage GA ALTERNATE_NAMES RNA replicase beta chain ORGANISM #formal_name phage GA #note host Escherichia coli DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 16-Jun-2000 ACCESSIONS JS0008; S13984 REFERENCE A92000 !$#authors Inokuchi, Y.; Takahashi, R.; Hirose, T.; Inayama, S.; !1Jacobson, A.B.; Hirashima, A. !$#journal J. Biochem. (1986) 99:1169-1180 !$#title The complete nucleotide sequence of the group II RNA !1coliphage GA. !$#cross-references MUID:86223910; PMID:3711059 !$#accession JS0008 !'##molecule_type genomic RNA !'##residues 1-532 ##label INO !'##cross-references GB:D10027; GB:D00046; GB:X03869; NID:g217784; !1PIDN:BAA00919.1; PID:g217787; NID:g15076; PID:g15080 REFERENCE S07250 !$#authors Inokuchi, Y.; Hirashima, A.; Watanabe, I. !$#journal J. Mol. Biol. (1982) 158:711-730 !$#title Comparison of the nucleotide sequences at the 3'-terminal !1region of RNAs from RNA coliphages. !$#cross-references MUID:83010313; PMID:7120417 !$#accession S13984 !'##status translation not shown !'##molecule_type genomic RNA !'##residues 500-501,'L',503-506,'F',508-532 ##label INW !'##cross-references EMBL:J02455; NID:g215437 COMMENT Bacteriophage GA is a group II RNA coliphage. CLASSIFICATION #superfamily phage MS2 RNA-directed RNA polymerase KEYWORDS lipoprotein; methylated carboxyl end; !1nucleotidyltransferase; prenylated cysteine FEATURE !$529 #binding_site farnesyl (Cys) (covalent) #status !8predicted\ !$529 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted SUMMARY #length 532 #molecular-weight 59928 #checksum 6200 SEQUENCE /// ENTRY RRBPBQ #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) beta chain - phage Q-beta ALTERNATE_NAMES RNA replicase ORGANISM #formal_name phage Q-beta #note host Escherichia coli DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 20-Apr-2001 ACCESSIONS S03340; S13980 REFERENCE S03340 !$#authors Mills, D.R.; Priano, C.; DiMauro, P.; Binderow, B.D. !$#journal J. Mol. Biol. (1989) 205:751-764 !$#title Q-beta replicase: mapping the functional domains of an !1RNA-dependent RNA polymerase. !$#cross-references MUID:89178693; PMID:2538637 !$#accession S03340 !'##molecule_type mRNA !'##residues 1-589 ##label MIL !'##cross-references EMBL:X14764; NID:g15086; PIDN:CAA32872.1; !1PID:g15087 REFERENCE S07250 !$#authors Inokuchi, Y.; Hirashima, A.; Watanabe, I. !$#journal J. Mol. Biol. (1982) 158:711-730 !$#title Comparison of the nucleotide sequences at the 3'-terminal !1region of RNAs from RNA coliphages. !$#cross-references MUID:83010313; PMID:7120417 !$#accession S13980 !'##status translation not shown !'##molecule_type genomic RNA !'##residues 541-574,'T',576,'SSRARRLRLYTRRNLGRGIMAPNCE' ##label INO !'##cross-references EMBL:J02485; NID:g215727 CLASSIFICATION #superfamily phage MS2 RNA-directed RNA polymerase KEYWORDS nucleotidyltransferase SUMMARY #length 589 #molecular-weight 65518 #checksum 4843 SEQUENCE /// ENTRY RRXRBT #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) - bluetongue virus (serotype 10, American isolate) ALTERNATE_NAMES minor core protein VP1 ORGANISM #formal_name bluetongue virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 10-Nov-1995 ACCESSIONS A34296; S10534 REFERENCE A34296 !$#authors Roy, P.; Fukusho, A.; Ritter, G.D.; Lyon, D. !$#journal Nucleic Acids Res. (1988) 16:11759-11767 !$#title Evidence for genetic relationship between RNA and DNA !1viruses from the sequence homology of a putative polymerase !1gene of bluetongue virus with that of vaccinia virus: !1conservation of RNA polymerase genes from diverse species. !$#cross-references MUID:89098323; PMID:2850542 !$#accession A34296 !'##molecule_type genomic RNA !'##residues 1-1302 ##label ROY REFERENCE S10534 !$#authors Roy, P.; Marshall, J.J.A.; French, T.J. !$#journal Curr. Top. Microbiol. Immunol. (1990) 162:43-87 !$#title Structure of the bluetongue virus genome and its encoded !1proteins. !$#cross-references MUID:90345726; PMID:2166648 !$#accession S10534 !'##status preliminary !'##molecule_type genomic RNA !'##residues 1-1302 ##label RO2 GENETICS !$#map_position segment 1 CLASSIFICATION #superfamily bluetongue virus RNA-directed RNA polymerase KEYWORDS nucleotidyltransferase SUMMARY #length 1302 #molecular-weight 149585 #checksum 3619 SEQUENCE /// ENTRY A43377 #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) - rice dwarf virus ALTERNATE_NAMES RNA nucleotidyltransferase (RNA-directed); RNA replicase ORGANISM #formal_name rice dwarf virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jun-2000 ACCESSIONS A43377 REFERENCE A43377 !$#authors Suzuki, N.; Tanimura, M.; Watanabe, Y.; Kusano, T.; !1Kitagawa, Y.; Suda, N.; Kudo, H.; Uyeda, I.; Shikata, E. !$#journal Virology (1992) 190:240-247 !$#title Molecular analysis of rice dwarf phytoreovirus segment S1: !1interviral homology of the putative RNA-dependent RNA !1polymerase between plant- and animal-infecting reoviruses. !$#cross-references MUID:92410600; PMID:1529532 !$#accession A43377 !'##molecule_type genomic RNA !'##residues 1-1444 ##label SUZ !'##cross-references GB:D90198; NID:g222496; PIDN:BAA14222.1; !1PID:g222497 GENETICS !$#map_position segment 1 CLASSIFICATION #superfamily rice dwarf virus RNA-directed RNA polymerase KEYWORDS nucleotidyltransferase; RNA biosynthesis; RNA replication SUMMARY #length 1444 #molecular-weight 164143 #checksum 7907 SEQUENCE /// ENTRY RRWWRH #type complete TITLE genome polyprotein - rabbit hemorrhagic disease virus CONTAINS RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name rabbit hemorrhagic disease virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 29-May-1998 ACCESSIONS A41039 REFERENCE A41039 !$#authors Meyers, G.; Wirblich, C.; Thiel, H.J. !$#journal Virology (1991) 184:664-676 !$#title Rabbit hemorrhagic disease virus--molecular cloning and !1nucleotide sequencing of a calicivirus genome. !$#cross-references MUID:91361557; PMID:1840711 !$#accession A41039 !'##molecule_type genomic RNA !'##residues 1-2344 ##label MEY !'##cross-references GB:M67473 CLASSIFICATION #superfamily rabbit calicivirus RNA-directed RNA polymerase KEYWORDS nucleotidyltransferase SUMMARY #length 2344 #molecular-weight 257192 #checksum 5498 SEQUENCE /// ENTRY RRWWF9 #type complete TITLE genome polyprotein - feline calicivirus (strain F9) CONTAINS RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name feline calicivirus DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 11-Jun-1999 ACCESSIONS A43382; A45538; S23701 REFERENCE A43382 !$#authors Carter, M.J.; Milton, I.D.; Meanger, J.; Bennett, M.; !1Gaskell, R.M.; Turner, P.C. !$#journal Virology (1992) 190:443-448 !$#title The complete nucleotide sequence of a feline calicivirus. !$#cross-references MUID:92410623; PMID:1529544 !$#accession A43382 !'##molecule_type genomic RNA !'##residues 1-1763 ##label CAR !'##cross-references GB:M86379; NID:g323877; PIDN:AAA79326.1; !1PID:g323878 REFERENCE A45538 !$#authors Carter, M.J.; Milton, I.D.; Turner, P.C.; Meanger, J.; !1Bennett, M.; Gaskell, R.M. !$#journal Arch. Virol. (1992) 122:223-235 !$#title Identification and sequence determination of the capsid !1protein gene of feline calicivirus. !$#cross-references MUID:92117861; PMID:1731695 !$#accession A45538 !'##molecule_type genomic RNA !'##residues 1098-1763 ##label CA2 !'##experimental_source strain F9 !'##note sequence extracted from NCBI backbone (NCBIN:77457, !1NCBIP:77458) CLASSIFICATION #superfamily rabbit calicivirus RNA-directed RNA polymerase KEYWORDS nucleotidyltransferase SUMMARY #length 1763 #molecular-weight 195028 #checksum 2051 SEQUENCE /// ENTRY RRVUBY #type complete TITLE genome polyprotein - bunyamwera virus ALTERNATE_NAMES L protein CONTAINS RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name bunyamwera virus DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 11-Jun-1999 ACCESSIONS A33744 REFERENCE A33744 !$#authors Elliott, R.M. !$#journal Virology (1989) 173:426-436 !$#title Nucleotide sequence analysis of the large (L) genomic RNA !1segment of Bunyamwera virus, the prototype of the family !1Bunyaviridae. !$#cross-references MUID:90085791; PMID:2596023 !$#accession A33744 !'##molecule_type genomic RNA !'##residues 1-2238 ##label ELL !'##cross-references GB:X14383; NID:g58712; PIDN:CAA32553.1; PID:g58713 GENETICS !$#map_position segment L CLASSIFICATION #superfamily bunyavirus RNA-directed RNA polymerase KEYWORDS nucleotidyltransferase SUMMARY #length 2238 #molecular-weight 258668 #checksum 9456 SEQUENCE /// ENTRY RRVUTW #type complete TITLE genome polyprotein - tomato spotted wilt virus (strain BR-01) ALTERNATE_NAMES L protein CONTAINS RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name tomato spotted wilt virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 29-May-1998 ACCESSIONS JQ1335 REFERENCE JQ1335 !$#authors de Haan, P.; Kormelink, R.; de Oliveira Resende, R.; van !1Poelwijk, F.; Peters, D.; Goldbach, R. !$#journal J. Gen. Virol. (1991) 71:2207-2216 !$#title Tomato spotted wilt virus L RNA encodes a putative RNA !1polymerase. !$#accession JQ1335 !'##molecule_type genomic RNA !'##residues 1-2875 ##label DEH GENETICS !$#map_position segment L CLASSIFICATION #superfamily bunyavirus RNA-directed RNA polymerase KEYWORDS nucleotidyltransferase SUMMARY #length 2875 #molecular-weight 331500 #checksum 9770 SEQUENCE /// ENTRY RRVUNE #type complete TITLE genome polyprotein - Puumala virus (strain Hallnas B1) ALTERNATE_NAMES L protein CONTAINS RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name Puumala virus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 29-May-1998 ACCESSIONS A40319 REFERENCE A40319 !$#authors Stohwasser, R.; Raab, K.; Darai, G.; Bautz, E.K.F. !$#journal Virology (1991) 183:386-391 !$#title Primary structure of the large (L) RNA segment of !1nephropathia epidemica virus strain Hallnas B1 coding for !1the viral RNA polymerase. !$#cross-references MUID:91272501; PMID:2053288 !$#accession A40319 !'##molecule_type genomic RNA !'##residues 1-2156 ##label STO !'##cross-references GB:M63194 !'##note the source was designated as nephropathia epidemica virus GENETICS !$#map_position segment L CLASSIFICATION #superfamily nephropathia epidemica virus RNA-directed RNA !1polymerase KEYWORDS nucleotidyltransferase SUMMARY #length 2156 #molecular-weight 247048 #checksum 8039 SEQUENCE /// ENTRY S16449 #type complete TITLE genome polyprotein - Seoul virus (strain 80-39) ALTERNATE_NAMES L protein CONTAINS RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name Seoul virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 11-Jun-1999 ACCESSIONS S16449 REFERENCE S16449 !$#authors Antic, D.; Lim, B.U.; Kang, C.Y. !$#journal Virus Res. (1991) 19:59-66 !$#title Nucleotide sequence and coding capacity of the large (L) !1genomic RNA segment of Seoul 80-39 virus, a member of the !1hantavirus genus. !$#cross-references MUID:91327731; PMID:1840713 !$#accession S16449 !'##molecule_type genomic RNA !'##residues 1-2151 ##label ANT !'##cross-references EMBL:X56492; NID:g60440; PIDN:CAA39847.1; !1PID:g60441 GENETICS !$#map_position segment L CLASSIFICATION #superfamily nephropathia epidemica virus RNA-directed RNA !1polymerase KEYWORDS nucleotidyltransferase SUMMARY #length 2151 #molecular-weight 246662 #checksum 4399 SEQUENCE /// ENTRY JQ1621 #type complete TITLE genome polyprotein - Uukuniemi virus (strain S23) ALTERNATE_NAMES L protein CONTAINS RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name Uukuniemi virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jun-2000 ACCESSIONS JQ1621 REFERENCE JQ1621 !$#authors Elliott, R.M.; Dunn, E.; Simons, J.F.; Pettersson, R.F. !$#journal J. Gen. Virol. (1992) 73:1745-1752 !$#title Nucleotide sequence and coding strategy of the Uukuniemi !1virus L RNA segment. !$#cross-references MUID:92333259; PMID:1629699 !$#accession JQ1621 !'##molecule_type genomic RNA !'##residues 1-2103 ##label ELL !'##cross-references DDBJ:D10759; NID:g222688; PIDN:BAA01590.1; !1PID:g222689 GENETICS !$#map_position segment L CLASSIFICATION #superfamily Uukuniemi virus RNA-directed RNA polymerase KEYWORDS nucleotidyltransferase SUMMARY #length 2103 #molecular-weight 241039 #checksum 2140 SEQUENCE /// ENTRY P1IV33 #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) 1 - influenza A virus (strain A/WSN/33) ALTERNATE_NAMES P1 protein; PB1 protein ORGANISM #formal_name influenza A virus DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 07-May-1999 ACCESSIONS A04046; PQ0414 REFERENCE A04046 !$#authors Sivasubramanian, N.; Nayak, D.P. !$#journal J. Virol. (1982) 44:321-329 !$#title Sequence analysis of the polymerase 1 gene and the secondary !1structure prediction of polymerase 1 protein of human !1influenza virus A/WSN/33. !$#cross-references MUID:83059883; PMID:7143569 !$#accession A04046 !'##molecule_type genomic RNA !'##residues 1-757 ##label SIV !'##experimental_source strain A/WSN/33 REFERENCE PQ0408 !$#authors Li, X.S.; Zhao, C.Y.; Gao, H.M.; Zhang, Y.Q.; Ishida, M.; !1Kanegae, Y.; Endo, A.; Nerome, R.; Omoe, K.; Nerome, K. !$#journal J. Gen. Virol. (1992) 73:1329-1337 !$#title Origin and evolutionary characteristics of antigenic !1reassortant influenza A (H1N2) viruses isolated from man in !1China. !$#cross-references MUID:92300326; PMID:1607856 !$#accession PQ0414 !'##molecule_type genomic RNA !'##residues 23-55 ##label LIA !'##experimental_source strain A/Yamagata/120/86 [H1N1] GENETICS !$#map_position segment 2 CLASSIFICATION #superfamily influenza virus RNA-directed RNA polymerase 1 KEYWORDS nucleotidyltransferase SUMMARY #length 757 #molecular-weight 86534 #checksum 9018 SEQUENCE /// ENTRY P1IV34 #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) 1 - influenza A virus (strain A/PR/8/34) ALTERNATE_NAMES P1 protein; PB1 protein ORGANISM #formal_name influenza A virus DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 11-Jun-1999 ACCESSIONS A93418; S11287; A04047; A93415 REFERENCE A93418 !$#authors Winter, G.; Fields, S. !$#journal Nucleic Acids Res. (1982) 10:2135-2143 !$#title Nucleotide sequence of human influenza A/PR/8/34 segment 2. !$#cross-references MUID:82196884; PMID:6281731 !$#accession A93418 !'##molecule_type mRNA !'##residues 1-757 ##label WIN !'##experimental_source strain A/PR/8/34 REFERENCE S11286 !$#authors Robertson, J.S. !$#journal Nucleic Acids Res. (1979) 6:3745-3757 !$#title 5' and 3' terminal nucleotide sequences of the RNA genome !1segments of influenza virus. !$#cross-references MUID:80034428; PMID:493121 !$#accession S11287 !'##molecule_type genomic RNA !'##residues 1-14 ##label ROB !'##cross-references EMBL:J02119; NID:g324893; PIDN:AAA43580.1; !1PID:g554664 !'##experimental_source strain A/FPV/Rostock/34 [H7N1] GENETICS !$#map_position segment 2 CLASSIFICATION #superfamily influenza virus RNA-directed RNA polymerase 1 KEYWORDS nucleotidyltransferase SUMMARY #length 757 #molecular-weight 86570 #checksum 9615 SEQUENCE /// ENTRY P1IV68 #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) 1 - influenza A virus (strain A/NT/60/68) ALTERNATE_NAMES P1 protein; PB1 protein ORGANISM #formal_name influenza A virus DATE 18-Aug-1982 #sequence_revision 12-May-1994 #text_change 19-May-1994 ACCESSIONS A93415; A04047 REFERENCE A93415 !$#authors Bishop, D.H.L.; Huddleston, J.A.; Brownlee, G.G. !$#journal Nucleic Acids Res. (1982) 10:1335-1343 !$#title The complete sequence of RNA segment 2 of influenza A/NT/60/ !168 and its encoded P1 protein. !$#cross-references MUID:82174312; PMID:7041090 !$#accession A93415 !'##molecule_type mRNA !'##residues 1-757 ##label BIS GENETICS !$#map_position segment 2 CLASSIFICATION #superfamily influenza virus RNA-directed RNA polymerase 1 KEYWORDS nucleotidyltransferase SUMMARY #length 757 #molecular-weight 86412 #checksum 8075 SEQUENCE /// ENTRY P1IV61 #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) 1 - influenza A virus (strain A/Ann Arbor/6/60 [H2N2]) ALTERNATE_NAMES P1 protein; PB1 protein ORGANISM #formal_name influenza A virus DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 11-Jun-1999 ACCESSIONS B31831 REFERENCE A31831 !$#authors Cox, N.J.; Kitame, F.; Kendal, A.P.; Maassab, H.F.; Naeve, !1C. !$#journal Virology (1988) 167:554-567 !$#title Identification of sequence changes in the cold-adapted, live !1attenuated influenza vaccine strain, A/Ann Arbor/6/60 !1(H2N2). !$#cross-references MUID:89073759; PMID:2974219 !$#accession B31831 !'##molecule_type genomic RNA !'##residues 1-757 ##label COX !'##cross-references GB:M23972; GB:J04349; GB:M23973; NID:g324941; !1PIDN:AAA43632.1; PID:g324942 GENETICS !$#map_position segment 2 CLASSIFICATION #superfamily influenza virus RNA-directed RNA polymerase 1 KEYWORDS nucleotidyltransferase SUMMARY #length 757 #molecular-weight 86443 #checksum 6815 SEQUENCE /// ENTRY A60008 #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) 1 - influenza A virus (strain A/Victoria/3/75 [H3N2]) ALTERNATE_NAMES P1 protein; PB1 protein ORGANISM #formal_name influenza A virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 07-May-1999 ACCESSIONS A60008 REFERENCE A60008 !$#authors de la Luna, S.; Martinez, C.; Ortin, J. !$#journal Virus Res. (1989) 13:143-156 !$#title Molecular cloning and sequencing of influenza virus A/ !1Victoria/3/75 polymerase genes: sequence evolution and !1prediction of possible functional domains. !$#cross-references MUID:89370813; PMID:2773594 !$#accession A60008 !'##molecule_type mRNA !'##residues 1-757 ##label DEL GENETICS !$#map_position segment 2 CLASSIFICATION #superfamily influenza virus RNA-directed RNA polymerase 1 KEYWORDS nucleotidyltransferase SUMMARY #length 757 #molecular-weight 86451 #checksum 7449 SEQUENCE /// ENTRY B60011 #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) 1 - influenza A virus (strain A/Mallard/NY/6750/78) ALTERNATE_NAMES P1 protein; PB1 protein ORGANISM #formal_name influenza A virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 07-May-1999 ACCESSIONS B60011 REFERENCE A60011 !$#authors Treanor, J.; Kawaoka, Y.; Miller, R.; Webster, R.G.; Murphy, !1B. !$#journal Virus Res. (1989) 14:257-270 !$#title Nucleotide sequence of the avian influenza A/Mallard/NY/ !16750/78 virus polymerase genes. !$#cross-references MUID:90163566; PMID:2483012 !$#accession B60011 !'##molecule_type DNA !'##residues 1-757 ##label TRE GENETICS !$#map_position segment 2 CLASSIFICATION #superfamily influenza virus RNA-directed RNA polymerase 1 KEYWORDS nucleotidyltransferase SUMMARY #length 757 #molecular-weight 86453 #checksum 7457 SEQUENCE /// ENTRY P1IVBL #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) 1 - influenza B virus (strain B/Lee/40) ALTERNATE_NAMES P1 protein; PB1 protein ORGANISM #formal_name influenza B virus DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 11-Jun-1999 ACCESSIONS A24287 REFERENCE A24287 !$#authors Kemdirim, S.; Palefsky, J.; Briedis, D.J. !$#journal Virology (1986) 152:126-135 !$#title Influenza B virus PB1 protein: nucleotide sequence of the !1genome RNA segment predicts a high degree of structural !1homology with the corresponding influenza A virus polymerase !1protein. !$#cross-references MUID:86237097; PMID:3754992 !$#accession A24287 !'##molecule_type mRNA !'##residues 1-752 ##label KEM !'##cross-references GB:M14880; NID:g325275; PIDN:AAA43767.1; !1PID:g325276 GENETICS !$#map_position segment 2 CLASSIFICATION #superfamily influenza virus RNA-directed RNA polymerase 1 KEYWORDS nucleotidyltransferase SUMMARY #length 752 #molecular-weight 84406 #checksum 4605 SEQUENCE /// ENTRY P1IVBC #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) 1 - influenza B virus (strain B/Ann Arbor/1/66 [cold-adapted]) ALTERNATE_NAMES P1 protein; PB1 protein ORGANISM #formal_name influenza B virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 24-Feb-1994 ACCESSIONS C28604 REFERENCE A28604 !$#authors DeBorde, D.C.; Donabedian, A.M.; Herlocher, M.L.; Naeve, !1C.W.; Maassab, H.F. !$#journal Virology (1988) 163:429-443 !$#title Sequence comparison of wild-type and cold-adapted B/Ann !1Arbor/1/66 influenza virus genes. !$#cross-references MUID:88179548; PMID:3354202 !$#accession C28604 !'##molecule_type genomic RNA !'##residues 1-752 ##label DEB GENETICS !$#map_position segment 2 CLASSIFICATION #superfamily influenza virus RNA-directed RNA polymerase 1 KEYWORDS nucleotidyltransferase SUMMARY #length 752 #molecular-weight 84305 #checksum 5024 SEQUENCE /// ENTRY P1IVBW #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) 1 - influenza B virus (strain B/Ann Arbor/1/66 [wild-type]) ALTERNATE_NAMES P1 protein; PB1 protein ORGANISM #formal_name influenza B virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 11-Jun-1999 ACCESSIONS D28604 REFERENCE A28604 !$#authors DeBorde, D.C.; Donabedian, A.M.; Herlocher, M.L.; Naeve, !1C.W.; Maassab, H.F. !$#journal Virology (1988) 163:429-443 !$#title Sequence comparison of wild-type and cold-adapted B/Ann !1Arbor/1/66 influenza virus genes. !$#cross-references MUID:88179548; PMID:3354202 !$#accession D28604 !'##molecule_type genomic RNA !'##residues 1-752 ##label DEB !'##cross-references GB:M20170; NID:g325281; PIDN:AAA43770.1; !1PID:g325282 GENETICS !$#map_position segment 2 CLASSIFICATION #superfamily influenza virus RNA-directed RNA polymerase 1 KEYWORDS nucleotidyltransferase SUMMARY #length 752 #molecular-weight 84321 #checksum 4780 SEQUENCE /// ENTRY P1IV50 #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) 1 - influenza C virus (strain C/JJ/50) ALTERNATE_NAMES P1 protein; PB1 protein ORGANISM #formal_name influenza C virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 11-Jun-1999 ACCESSIONS B34225 REFERENCE A34225 !$#authors Yamashita, M.; Krystal, M.; Palese, P. !$#journal Virology (1989) 171:458-466 !$#title Comparison of the three large polymerase proteins of !1influenza A, B, and C viruses. !$#cross-references MUID:89348004; PMID:2763462 !$#accession B34225 !'##molecule_type genomic RNA !'##residues 1-754 ##label YAM !'##cross-references GB:M28060; NID:g325362; PIDN:AAA43814.1; !1PID:g325363 GENETICS !$#map_position segment 2 CLASSIFICATION #superfamily influenza virus RNA-directed RNA polymerase 1 KEYWORDS nucleotidyltransferase SUMMARY #length 754 #molecular-weight 85983 #checksum 6189 SEQUENCE /// ENTRY P1IVDV #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) 1 - Dhori virus (strain Dhori/India/1313/61) ORGANISM #formal_name Dhori virus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 11-Jun-1999 ACCESSIONS A39145 REFERENCE A39145 !$#authors Lin, D.A.; Roychoudhury, S.; Palese, P.; Clay, W.C.; Fuller, !1F.J. !$#journal Virology (1991) 182:1-7 !$#title Evolutionary relatedness of the predicted gene product of !1RNA segment 2 of the tick-borne Dhori virus and the PB1 !1polymerase gene of influenza viruses. !$#cross-references MUID:91220640; PMID:2024457 !$#accession A39145 !'##molecule_type mRNA !'##residues 1-716 ##label LIN !'##cross-references GB:M65866; NID:g323668; PIDN:AAA42968.1; !1PID:g323669 GENETICS !$#map_position segment 2 CLASSIFICATION #superfamily influenza virus RNA-directed RNA polymerase 1 KEYWORDS nucleotidyltransferase SUMMARY #length 716 #molecular-weight 81292 #checksum 7502 SEQUENCE /// ENTRY P3IV33 #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) 2 - influenza A virus (strain A/WSN/33) ALTERNATE_NAMES P3 protein; PB2 protein ORGANISM #formal_name influenza A virus DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 11-Jun-1999 ACCESSIONS A04044 REFERENCE A04044 !$#authors Kaptein, J.S.; Nayak, D.P. !$#journal J. Virol. (1982) 42:55-63 !$#title Complete nucleotide sequence of the polymerase 3 gene of !1human influenza virus A/WSN/33. !$#cross-references MUID:82217012; PMID:7045393 !$#accession A04044 !'##molecule_type genomic RNA !'##residues 1-759 ##label DEB !'##cross-references GB:J02179; NID:g324913; PIDN:AAA43611.1; !1PID:g324914 GENETICS !$#map_position segment 1 CLASSIFICATION #superfamily influenza virus RNA-directed RNA polymerase 2 KEYWORDS nucleotidyltransferase SUMMARY #length 759 #molecular-weight 85796 #checksum 3540 SEQUENCE /// ENTRY P3IV34 #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) 2 - influenza A virus (strain A/PR/8/34) ALTERNATE_NAMES P3 protein; PB2 protein ORGANISM #formal_name influenza A virus DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 28-May-1999 ACCESSIONS A04045 REFERENCE A90819 !$#authors Fields, S.; Winter, G. !$#journal Cell (1982) 28:303-313 !$#title Nucleotide sequences of influenza virus segments 1 and 3 !1reveal mosaic structure of a small viral RNA segment. !$#cross-references MUID:82137094; PMID:7060132 !$#accession A04045 !'##molecule_type genomic RNA !'##residues 1-759 ##label FIE !'##cross-references GB:V00603; GB:J02153; NID:g60484; PIDN:CAA23855.1; !1PID:g60485 !'##experimental_source strain A/PR/8/34 GENETICS !$#map_position segment 1 CLASSIFICATION #superfamily influenza virus RNA-directed RNA polymerase 2 KEYWORDS nucleotidyltransferase SUMMARY #length 759 #molecular-weight 86012 #checksum 3975 SEQUENCE /// ENTRY P3IV68 #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) 2 - influenza A virus (strain A/NT/60/68) ALTERNATE_NAMES P3 protein; PB2 protein ORGANISM #formal_name influenza A virus DATE 03-Feb-1994 #sequence_revision 03-Feb-1994 #text_change 11-Jun-1999 ACCESSIONS A93458; A04045 REFERENCE A93458 !$#authors Jones, K.L.; Huddleston, J.A.; Brownlee, G.G. !$#journal Nucleic Acids Res. (1983) 11:1555-1566 !$#title The sequence of RNA segment 1 of influenza virus A/NT/60/68 !1and its comparison with the corresponding segment of strains !1A/PR/8/34 and A/WSN/33. !$#cross-references MUID:83143366; PMID:6828387 !$#accession A93458 !'##molecule_type genomic RNA !'##residues 1-759 ##label JON !'##cross-references GB:J02140; NID:g324919; PIDN:AAA43613.1; !1PID:g324920 GENETICS !$#map_position segment 1 CLASSIFICATION #superfamily influenza virus RNA-directed RNA polymerase 2 KEYWORDS nucleotidyltransferase SUMMARY #length 759 #molecular-weight 86046 #checksum 6587 SEQUENCE /// ENTRY P3IV2A #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) chain PB2 - influenza A virus (strain FPV/Rostock/34 [H7N1]) ALTERNATE_NAMES P3 protein ORGANISM #formal_name influenza A virus DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 11-Jun-1999 ACCESSIONS S07417 REFERENCE S07417 !$#authors Roditi, I.J.; Robertson, J.S. !$#journal Virus Res. (1984) 1:65-71 !$#title Nucleotide sequence of the avian influenza virus A/fowl !1plague/Rostock/34 segment 1 encoding the PB2 polypeptide. !$#accession S07417 !'##molecule_type genomic RNA !'##residues 1-759 ##label ROD !'##cross-references EMBL:M21851; NID:g324987; PIDN:AAA43651.1; !1PID:g324988 GENETICS !$#map_position segment 1 CLASSIFICATION #superfamily influenza virus RNA-directed RNA polymerase 2 KEYWORDS nucleotidyltransferase SUMMARY #length 759 #molecular-weight 85720 #checksum 5739 SEQUENCE /// ENTRY A60011 #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) 2 - influenza A virus (strain A/Mallard/NY/6750/78) ALTERNATE_NAMES P3 protein; PB2 protein ORGANISM #formal_name influenza A virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 07-May-1999 ACCESSIONS A60011 REFERENCE A60011 !$#authors Treanor, J.; Kawaoka, Y.; Miller, R.; Webster, R.G.; Murphy, !1B. !$#journal Virus Res. (1989) 14:257-270 !$#title Nucleotide sequence of the avian influenza A/Mallard/NY/ !16750/78 virus polymerase genes. !$#cross-references MUID:90163566; PMID:2483012 !$#accession A60011 !'##molecule_type DNA !'##residues 1-759 ##label TRE GENETICS !$#map_position segment 1 CLASSIFICATION #superfamily influenza virus RNA-directed RNA polymerase 2 KEYWORDS nucleotidyltransferase SUMMARY #length 759 #molecular-weight 85891 #checksum 3891 SEQUENCE /// ENTRY P3IV61 #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) 2 - influenza A virus (strain A/Ann Arbor/6/60 [H2N2]) ALTERNATE_NAMES P3 protein; PB2 protein ORGANISM #formal_name influenza A virus DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 11-Jun-1999 ACCESSIONS A31831 REFERENCE A31831 !$#authors Cox, N.J.; Kitame, F.; Kendal, A.P.; Maassab, H.F.; Naeve, !1C. !$#journal Virology (1988) 167:554-567 !$#title Identification of sequence changes in the cold-adapted, live !1attenuated influenza vaccine strain, A/Ann Arbor/6/60 !1(H2N2). !$#cross-references MUID:89073759; PMID:2974219 !$#accession A31831 !'##molecule_type genomic RNA !'##residues 1-759 ##label COX !'##cross-references GB:M23970; GB:J04349; GB:M23971; NID:g324981; !1PIDN:AAA43648.1; PID:g324982 GENETICS !$#map_position segment 1 CLASSIFICATION #superfamily influenza virus RNA-directed RNA polymerase 2 KEYWORDS nucleotidyltransferase SUMMARY #length 759 #molecular-weight 86087 #checksum 6213 SEQUENCE /// ENTRY P3IVAK #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) 2 - influenza A virus (strain avian/Kiev/59/79 [H1N1]) ORGANISM #formal_name influenza A virus #note host Homo sapiens (man) DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 24-Feb-1994 ACCESSIONS JN0411; S03793; S08338 REFERENCE S03793 !$#authors Petrov, N.A.; Netesov, S.V.; Golovin, S.Y.; Mamaeva, N.V.; !1Mamaev, L.V.; Sivolodova, G.F.; Petrenko, V.A.; Vasilenko, !1S.K. !$#journal Bioorg. Khim. (1987) 13:915-920 !$#title Nucleotide sequence of a full-length DNA copy of the !1influenza virus A/Kiev/59/79 (H1N1) PB2 gene. !$#cross-references MUID:88049805; PMID:3675640 !$#accession JN0411 !'##molecule_type genomic RNA !'##residues 1-759 ##label PET !'##cross-references GB:M38277 GENETICS !$#map_position segment 1 CLASSIFICATION #superfamily influenza virus RNA-directed RNA polymerase 2 KEYWORDS nucleotidyltransferase; RNA replication SUMMARY #length 759 #molecular-weight 86098 #checksum 6758 SEQUENCE /// ENTRY B60008 #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) 2 - influenza A virus (strain A/Victoria/3/75 [H3N2]) ALTERNATE_NAMES P3 protein; PB2 protein ORGANISM #formal_name influenza A virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 07-May-1999 ACCESSIONS B60008; PQ0421; PQ0415 REFERENCE A60008 !$#authors de la Luna, S.; Martinez, C.; Ortin, J. !$#journal Virus Res. (1989) 13:143-156 !$#title Molecular cloning and sequencing of influenza virus A/ !1Victoria/3/75 polymerase genes: sequence evolution and !1prediction of possible functional domains. !$#cross-references MUID:89370813; PMID:2773594 !$#accession B60008 !'##molecule_type mRNA !'##residues 1-759 ##label DEL !'##experimental_source strain A/Victoria/3/75 [H3N2] REFERENCE PQ0408 !$#authors Li, X.S.; Zhao, C.Y.; Gao, H.M.; Zhang, Y.Q.; Ishida, M.; !1Kanegae, Y.; Endo, A.; Nerome, R.; Omoe, K.; Nerome, K. !$#journal J. Gen. Virol. (1992) 73:1329-1337 !$#title Origin and evolutionary characteristics of antigenic !1reassortant influenza A (H1N2) viruses isolated from man in !1China. !$#cross-references MUID:92300326; PMID:1607856 !$#accession PQ0421 !'##molecule_type genomic RNA !'##residues 19-37 ##label LIA1 !'##experimental_source strain A/Guizhou/54/89 [H3N2] !$#accession PQ0415 !'##molecule_type genomic RNA !'##residues 19-37 ##label LIA2 !'##experimental_source strain A/Yamagata/120/86 [H1N1] GENETICS !$#map_position segment 1 CLASSIFICATION #superfamily influenza virus RNA-directed RNA polymerase 2 KEYWORDS nucleotidyltransferase SUMMARY #length 759 #molecular-weight 86125 #checksum 8119 SEQUENCE /// ENTRY P3IVBC #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) 2 - influenza B virus (strain B/Ann Arbor/1/66 [cold-adapted]) ALTERNATE_NAMES P3 protein; PB2 protein ORGANISM #formal_name influenza B virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 11-Jun-1999 ACCESSIONS A28604 REFERENCE A28604 !$#authors DeBorde, D.C.; Donabedian, A.M.; Herlocher, M.L.; Naeve, !1C.W.; Maassab, H.F. !$#journal Virology (1988) 163:429-443 !$#title Sequence comparison of wild-type and cold-adapted B/Ann !1Arbor/1/66 influenza virus genes. !$#cross-references MUID:88179548; PMID:3354202 !$#accession A28604 !'##molecule_type genomic RNA !'##residues 1-770 ##label DEB !'##cross-references GB:M20163; NID:g325265; PIDN:AAA43762.1; !1PID:g325266 GENETICS !$#map_position segment 1 CLASSIFICATION #superfamily influenza virus RNA-directed RNA polymerase 2 KEYWORDS nucleotidyltransferase SUMMARY #length 770 #molecular-weight 88062 #checksum 2770 SEQUENCE /// ENTRY P3IVBW #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) 2 - influenza B virus (strain B/Ann Arbor/1/66 [wild-type]) ALTERNATE_NAMES P3 protein; PB2 protein ORGANISM #formal_name influenza B virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 11-Jun-1999 ACCESSIONS B28604 REFERENCE A28604 !$#authors DeBorde, D.C.; Donabedian, A.M.; Herlocher, M.L.; Naeve, !1C.W.; Maassab, H.F. !$#journal Virology (1988) 163:429-443 !$#title Sequence comparison of wild-type and cold-adapted B/Ann !1Arbor/1/66 influenza virus genes. !$#cross-references MUID:88179548; PMID:3354202 !$#accession B28604 !'##molecule_type genomic RNA !'##residues 1-770 ##label DEB !'##cross-references GB:M20168; NID:g325283; PIDN:AAA43771.1; !1PID:g325284 GENETICS !$#map_position segment 1 CLASSIFICATION #superfamily influenza virus RNA-directed RNA polymerase 2 KEYWORDS nucleotidyltransferase SUMMARY #length 770 #molecular-weight 88025 #checksum 3375 SEQUENCE /// ENTRY P3IV50 #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) 2 - influenza C virus (strain C/JJ/50) ALTERNATE_NAMES P3 protein; PB2 protein ORGANISM #formal_name influenza C virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 11-Jun-1999 ACCESSIONS A34225 REFERENCE A34225 !$#authors Yamashita, M.; Krystal, M.; Palese, P. !$#journal Virology (1989) 171:458-466 !$#title Comparison of the three large polymerase proteins of !1influenza A, B, and C viruses. !$#cross-references MUID:89348004; PMID:2763462 !$#accession A34225 !'##molecule_type genomic RNA !'##residues 1-774 ##label YAM !'##cross-references GB:M28061; NID:g325364; PIDN:AAA43815.1; !1PID:g325365 GENETICS !$#map_position segment 1 CLASSIFICATION #superfamily influenza virus RNA-directed RNA polymerase 2 KEYWORDS nucleotidyltransferase SUMMARY #length 774 #molecular-weight 87825 #checksum 8827 SEQUENCE /// ENTRY P2IV34 #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) 3 - influenza A virus (strain A/PR/8/34) ALTERNATE_NAMES P2 protein; PA protein ORGANISM #formal_name influenza A virus DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 28-May-1999 ACCESSIONS A04048 REFERENCE A90819 !$#authors Fields, S.; Winter, G. !$#journal Cell (1982) 28:303-313 !$#title Nucleotide sequences of influenza virus segments 1 and 3 !1reveal mosaic structure of a small viral RNA segment. !$#cross-references MUID:82137094; PMID:7060132 !$#accession A04048 !'##molecule_type genomic RNA !'##residues 1-716 ##label DEB !'##cross-references GB:V01106; GB:J02152; NID:g60808; PIDN:CAA24295.1; !1PID:g60809 GENETICS !$#map_position segment 3 CLASSIFICATION #superfamily influenza virus RNA-directed RNA polymerase 3 KEYWORDS nucleotidyltransferase SUMMARY #length 716 #molecular-weight 82588 #checksum 7473 SEQUENCE /// ENTRY P2IVWS #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) 3 - influenza A virus (strain A/WSN/33 [H1N1]) ALTERNATE_NAMES P2 protein; PA protein ORGANISM #formal_name influenza A virus DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 11-Jun-1999 ACCESSIONS S08138 REFERENCE S08138 !$#authors Odagiri, T.; Tobita, K. !$#journal Nucleic Acids Res. (1990) 18:654 !$#title Nucleotide sequence of the PA gene of influenza A/WSN/33 !1(H1N1). !$#cross-references MUID:90174992; PMID:2308849 !$#accession S08138 !'##molecule_type mRNA !'##residues 1-716 ##label ODA !'##cross-references EMBL:X17336; NID:g60812; PIDN:CAA35212.1; !1PID:g60813 GENETICS !$#gene PA !$#map_position segment 3 CLASSIFICATION #superfamily influenza virus RNA-directed RNA polymerase 3 KEYWORDS nucleotidyltransferase SUMMARY #length 716 #molecular-weight 82531 #checksum 5052 SEQUENCE /// ENTRY P2IV68 #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) 3 - influenza A virus (strain A/NT/60/68) ALTERNATE_NAMES P2 protein; PA protein ORGANISM #formal_name influenza A virus DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 11-Jun-1999 ACCESSIONS A04049; PQ0422 REFERENCE A04049 !$#authors Bishop, D.H.L.; Jones, K.L.; Huddleston, J.A.; Brownlee, !1G.G. !$#journal Virology (1982) 120:481-489 !$#title Influenza A virus evolution: complete sequences of influenza !1A/NT/60/68 RNA segment 3 and its predicted acidic P !1polypeptide compared with those of influenza A/PR/8/34. !$#cross-references MUID:82251904; PMID:7101732 !$#accession A04049 !'##molecule_type genomic RNA !'##residues 1-716 ##label BIS !'##cross-references GB:J02139; NID:g324905; PIDN:AAA43597.1; !1PID:g324906 !'##experimental_source strain A/NT/60/68 REFERENCE PQ0408 !$#authors Li, X.S.; Zhao, C.Y.; Gao, H.M.; Zhang, Y.Q.; Ishida, M.; !1Kanegae, Y.; Endo, A.; Nerome, R.; Omoe, K.; Nerome, K. !$#journal J. Gen. Virol. (1992) 73:1329-1337 !$#title Origin and evolutionary characteristics of antigenic !1reassortant influenza A (H1N2) viruses isolated from man in !1China. !$#cross-references MUID:92300326; PMID:1607856 !$#accession PQ0422 !'##molecule_type genomic RNA !'##residues 43-75 ##label LIA !'##experimental_source strain A/Guizhou/54/89 [H3N2] GENETICS !$#map_position segment 3 CLASSIFICATION #superfamily influenza virus RNA-directed RNA polymerase 3 KEYWORDS nucleotidyltransferase SUMMARY #length 716 #molecular-weight 82995 #checksum 6279 SEQUENCE /// ENTRY P2IV61 #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) 3 - influenza A virus (strain A/Ann Arbor/6/60 [H2N2]) ALTERNATE_NAMES P2 protein; PA protein ORGANISM #formal_name influenza A virus DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 11-Jun-1999 ACCESSIONS C31831 REFERENCE A31831 !$#authors Cox, N.J.; Kitame, F.; Kendal, A.P.; Maassab, H.F.; Naeve, !1C. !$#journal Virology (1988) 167:554-567 !$#title Identification of sequence changes in the cold-adapted, live !1attenuated influenza vaccine strain, A/Ann Arbor/6/60 !1(H2N2). !$#cross-references MUID:89073759; PMID:2974219 !$#accession C31831 !'##molecule_type genomic RNA !'##residues 1-716 ##label COX !'##cross-references GB:M23974; GB:J04349; GB:M23975; NID:g324925; !1PIDN:AAA43616.1; PID:g324926 GENETICS !$#map_position segment 3 CLASSIFICATION #superfamily influenza virus RNA-directed RNA polymerase 3 KEYWORDS nucleotidyltransferase SUMMARY #length 716 #molecular-weight 82799 #checksum 6576 SEQUENCE /// ENTRY C60008 #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) 3 - influenza A virus (strain A/Victoria/3/75 [H3N2]) ALTERNATE_NAMES P2 protein; PA protein ORGANISM #formal_name influenza A virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 07-May-1999 ACCESSIONS C60008 REFERENCE A60008 !$#authors de la Luna, S.; Martinez, C.; Ortin, J. !$#journal Virus Res. (1989) 13:143-156 !$#title Molecular cloning and sequencing of influenza virus A/ !1Victoria/3/75 polymerase genes: sequence evolution and !1prediction of possible functional domains. !$#cross-references MUID:89370813; PMID:2773594 !$#accession C60008 !'##molecule_type mRNA !'##residues 1-716 ##label DEL GENETICS !$#map_position segment 3 CLASSIFICATION #superfamily influenza virus RNA-directed RNA polymerase 3 KEYWORDS nucleotidyltransferase SUMMARY #length 716 #molecular-weight 82821 #checksum 5518 SEQUENCE /// ENTRY C60011 #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) 3 - influenza A virus (strain A/Mallard/NY/6750/78) ALTERNATE_NAMES P2 protein; PA protein ORGANISM #formal_name influenza A virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 07-May-1999 ACCESSIONS C60011 REFERENCE A60011 !$#authors Treanor, J.; Kawaoka, Y.; Miller, R.; Webster, R.G.; Murphy, !1B. !$#journal Virus Res. (1989) 14:257-270 !$#title Nucleotide sequence of the avian influenza A/Mallard/NY/ !16750/78 virus polymerase genes. !$#cross-references MUID:90163566; PMID:2483012 !$#accession C60011 !'##molecule_type DNA !'##residues 1-716 ##label TRE GENETICS !$#map_position segment 3 CLASSIFICATION #superfamily influenza virus RNA-directed RNA polymerase 3 KEYWORDS nucleotidyltransferase SUMMARY #length 716 #molecular-weight 82299 #checksum 4487 SEQUENCE /// ENTRY P2IVTV #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) 3 - Thogoto virus ALTERNATE_NAMES P2 protein; PA protein ORGANISM #formal_name Thogoto virus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jun-2000 ACCESSIONS A33303 REFERENCE A33303 !$#authors Staunton, D.; Nuttall, P.A.; Bishop, D.H.L. !$#journal J. Gen. Virol. (1989) 70:2811-2817 !$#title Sequence analyses of Thogoto viral RNA segment 3: evidence !1for a distant relationship between an arbovirus and members !1of the Orthomyxoviridae. !$#cross-references MUID:90010988; PMID:2794982 !$#accession A33303 !'##molecule_type genomic RNA !'##residues 1-597 ##label STA !'##cross-references EMBL:D00540; NID:g222655; PIDN:BAA00429.1; !1PID:g222656 GENETICS !$#map_position segment 3 CLASSIFICATION #superfamily influenza virus RNA-directed RNA polymerase 3 KEYWORDS nucleotidyltransferase SUMMARY #length 597 #molecular-weight 68652 #checksum 8057 SEQUENCE /// ENTRY P2IVBS #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) 3 - influenza B virus (strain B/Singapore/222/79) ALTERNATE_NAMES P2 protein; PA protein ORGANISM #formal_name influenza B virus DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 11-Jun-1999 ACCESSIONS A27814 REFERENCE A27814 !$#authors Akoto-Amanfu, E.; Sivasubramanian, N.; Nayak, D.P. !$#journal Virology (1987) 159:147-153 !$#title Primary structure of the polymerase acidic (PA) gene of an !1influenza B virus (B/SING/222/79). !$#cross-references MUID:87265462; PMID:3604058 !$#accession A27814 !'##molecule_type mRNA !'##residues 1-725 ##label AKO !'##cross-references GB:M16711; NID:g325293; PIDN:AAA43776.1; !1PID:g325294 GENETICS !$#map_position segment 3 CLASSIFICATION #superfamily influenza virus RNA-directed RNA polymerase 3 KEYWORDS nucleotidyltransferase SUMMARY #length 725 #molecular-weight 83088 #checksum 9556 SEQUENCE /// ENTRY P2IVBC #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) 3 - influenza B virus (strain B/Ann Arbor/1/66 [cold-adapted]) ALTERNATE_NAMES P2 protein; PA protein ORGANISM #formal_name influenza B virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 11-Jun-1999 ACCESSIONS E28604 REFERENCE A28604 !$#authors DeBorde, D.C.; Donabedian, A.M.; Herlocher, M.L.; Naeve, !1C.W.; Maassab, H.F. !$#journal Virology (1988) 163:429-443 !$#title Sequence comparison of wild-type and cold-adapted B/Ann !1Arbor/1/66 influenza virus genes. !$#cross-references MUID:88179548; PMID:3354202 !$#accession E28604 !'##molecule_type genomic RNA !'##residues 1-726 ##label DEB !'##cross-references GB:M20171; NID:g325271; PIDN:AAA43765.1; !1PID:g325272 GENETICS !$#map_position segment 3 CLASSIFICATION #superfamily influenza virus RNA-directed RNA polymerase 3 KEYWORDS nucleotidyltransferase SUMMARY #length 726 #molecular-weight 83181 #checksum 2318 SEQUENCE /// ENTRY P2IVBW #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) 3 - influenza B virus (strain B/Ann Arbor/1/66 [wild-type]) ALTERNATE_NAMES P2 protein; PA protein ORGANISM #formal_name influenza B virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 11-Jun-1999 ACCESSIONS F28604 REFERENCE A28604 !$#authors DeBorde, D.C.; Donabedian, A.M.; Herlocher, M.L.; Naeve, !1C.W.; Maassab, H.F. !$#journal Virology (1988) 163:429-443 !$#title Sequence comparison of wild-type and cold-adapted B/Ann !1Arbor/1/66 influenza virus genes. !$#cross-references MUID:88179548; PMID:3354202 !$#accession F28604 !'##molecule_type genomic RNA !'##residues 1-726 ##label DEB !'##cross-references GB:M20172; NID:g325273; PIDN:AAA43766.1; !1PID:g325274 GENETICS !$#map_position segment 3 CLASSIFICATION #superfamily influenza virus RNA-directed RNA polymerase 3 KEYWORDS nucleotidyltransferase SUMMARY #length 726 #molecular-weight 83166 #checksum 2837 SEQUENCE /// ENTRY P2IV50 #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) 3 - influenza C virus (strain C/JJ/50) ALTERNATE_NAMES P2 protein; PA protein ORGANISM #formal_name influenza C virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 11-Jun-1999 ACCESSIONS C34225 REFERENCE A34225 !$#authors Yamashita, M.; Krystal, M.; Palese, P. !$#journal Virology (1989) 171:458-466 !$#title Comparison of the three large polymerase proteins of !1influenza A, B, and C viruses. !$#cross-references MUID:89348004; PMID:2763462 !$#accession C34225 !'##molecule_type genomic RNA !'##residues 1-709 ##label YAM !'##cross-references GB:M28062; NID:g325360; PIDN:AAA43813.1; !1PID:g325361 GENETICS !$#map_position segment 3 CLASSIFICATION #superfamily influenza virus RNA-directed RNA polymerase 3 KEYWORDS nucleotidyltransferase SUMMARY #length 709 #molecular-weight 81883 #checksum 9944 SEQUENCE /// ENTRY ZLNZSV #type complete TITLE genome polyprotein - Sendai virus (strain Z) CONTAINS RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name Sendai virus DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 11-Jun-1999 ACCESSIONS A04120 REFERENCE A00878 !$#authors Shioda, T.; Iwasaki, K.; Shibuta, H. !$#journal Nucleic Acids Res. (1986) 14:1545-1563 !$#title Determination of the complete nucleotide sequence of the !1Sendai virus genome RNA and the predicted amino acid !1sequences of the F, HN and L proteins. !$#cross-references MUID:86148492; PMID:3005975 !$#accession A04120 !'##molecule_type genomic RNA !'##residues 1-2228 ##label SHI !'##cross-references GB:X03614; NID:g60898; PIDN:CAA27273.1; PID:g60901 GENETICS !$#gene L CLASSIFICATION #superfamily parainfluenza virus RNA-directed RNA polymerase KEYWORDS ATP; nucleotidyltransferase SUMMARY #length 2228 #molecular-weight 252864 #checksum 4736 SEQUENCE /// ENTRY ZLNZSE #type complete TITLE genome polyprotein - Sendai virus (strain Enders) CONTAINS RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name Sendai virus DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 11-Jun-1999 ACCESSIONS A24293 REFERENCE A24293 !$#authors Morgan, E.M.; Rakestraw, K.M. !$#journal Virology (1986) 154:31-40 !$#title Sequence of the Sendai virus L gene: open reading frames !1upstream of the main coding region suggest that the gene may !1be polycistronic. !$#cross-references MUID:86317720; PMID:3019006 !$#accession A24293 !'##molecule_type genomic RNA !'##residues 1-2048 ##label MOR !'##cross-references GB:M14887; NID:g334975; PIDN:AAA69579.1; !1PID:g334976 GENETICS !$#gene L CLASSIFICATION #superfamily parainfluenza virus RNA-directed RNA polymerase KEYWORDS ATP; nucleotidyltransferase SUMMARY #length 2048 #molecular-weight 231622 #checksum 892 SEQUENCE /// ENTRY ZLNZP3 #type complete TITLE genome polyprotein - parainfluenza virus type 3 CONTAINS RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name parainfluenza virus type 3 #note host Homo sapiens (man) DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 29-May-1998 ACCESSIONS A29246 REFERENCE A29246 !$#authors Galinski, M.S.; Mink, M.A.; Pons, M.W. !$#journal Virology (1988) 165:499-510 !$#title Molecular cloning and sequence analysis of the human !1parainfluenza 3 virus gene encoding the L protein. !$#cross-references MUID:88306242; PMID:2841798 !$#accession A29246 !'##molecule_type genomic RNA !'##residues 1-2233 ##label GAL !'##cross-references GB:M21649 GENETICS !$#gene L CLASSIFICATION #superfamily parainfluenza virus RNA-directed RNA polymerase KEYWORDS ATP; nucleotidyltransferase SUMMARY #length 2233 #molecular-weight 255777 #checksum 1066 SEQUENCE /// ENTRY RRIWMV #type complete TITLE genome polyprotein - Marburg virus (strain Musoke) ALTERNATE_NAMES L protein CONTAINS RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name Marburg virus #note host Homo sapiens (man) DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 11-Jun-1999 ACCESSIONS A42450 REFERENCE A42450 !$#authors Muehlberger, E.; Sanchez, A.; Randolf, A.; Will, C.; Kiley, !1M.P.; Klenk, H.D.; Feldmann, H. !$#journal Virology (1992) 187:534-547 !$#title The nucleotide sequence of the L gene of Marburg virus, a !1filovirus: homologies with paramyxoviruses and !1rhabdoviruses. !$#cross-references MUID:92188528; PMID:1546452 !$#accession A42450 !'##molecule_type genomic RNA !'##residues 1-2330 ##label MUE !'##cross-references GB:M92834; NID:g332178; PIDN:AAA46562.1; !1PID:g332179 GENETICS !$#gene L CLASSIFICATION #superfamily parainfluenza virus RNA-directed RNA polymerase KEYWORDS ATP; nucleotidyltransferase; RNA biosynthesis FEATURE !$1325-1360 #domain ATP binding #status predicted #label AT1\ !$1390-1420 #domain ATP binding #status predicted #label AT2\ !$1560-1593 #domain ATP binding #status predicted #label AT3\ !$1932-1961 #domain ATP binding #status predicted #label AT4 SUMMARY #length 2330 #molecular-weight 267080 #checksum 6641 SEQUENCE /// ENTRY RRNZNV #type complete TITLE genome polyprotein - Newcastle disease virus (strain Beaudette C) CONTAINS RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name Newcastle disease virus DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 11-Jun-1999 ACCESSIONS A26747 REFERENCE A93665 !$#authors Yusoff, K.; Millar, N.S.; Chambers, P.; Emmerson, P.T. !$#journal Nucleic Acids Res. (1987) 15:3961-3976 !$#title Nucleotide sequence analysis of the L gene of Newcastle !1disease virus: homologies with Sendai and vesicular !1stomatitis viruses. !$#cross-references MUID:87230982; PMID:3035486 !$#accession A26747 !'##molecule_type mRNA !'##residues 1-2204 ##label YUS !'##cross-references GB:X05399; NID:g60937; PIDN:CAA28985.1; PID:g60939 GENETICS !$#gene L CLASSIFICATION #superfamily parainfluenza virus RNA-directed RNA polymerase KEYWORDS ATP; nucleotidyltransferase SUMMARY #length 2204 #molecular-weight 248822 #checksum 7364 SEQUENCE /// ENTRY A42548 #type complete TITLE genome polyprotein - mumps virus (strain Miyahara) ALTERNATE_NAMES L protein CONTAINS RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name mumps virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jun-2000 ACCESSIONS A42548 REFERENCE A42548 !$#authors Okazaki, K.; Tanabayashi, K.; Takeuchi, K.; Hishiyama, M.; !1Okazaki, K.; Yamada, A. !$#journal Virology (1992) 188:926-930 !$#title Molecular cloning and sequence analysis of the mumps virus !1gene encoding the L protein and the trailer sequence. !$#cross-references MUID:92263804; PMID:1585659 !$#accession A42548 !'##molecule_type genomic RNA !'##residues 1-2261 ##label OKA !'##cross-references GB:D10575; NID:g222145; PIDN:BAA01432.1; !1PID:g222146 GENETICS !$#gene L CLASSIFICATION #superfamily parainfluenza virus RNA-directed RNA polymerase KEYWORDS ATP; nucleotidyltransferase SUMMARY #length 2261 #molecular-weight 256572 #checksum 1972 SEQUENCE /// ENTRY JQ1532 #type complete TITLE genome polyprotein - simian paramyxovirus SV5 (strain 21004-WR) ALTERNATE_NAMES RNA nucleotidyltransferase (RNA-directed); RNA replicase CONTAINS RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name simian paramyxovirus SV5 DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 29-May-1998 ACCESSIONS JQ1532 REFERENCE JQ1532 !$#authors Higuchi, Y.; Miyahara, Y.; Kawano, M.; Tsurudome, M.; !1Matsumura, H.; Kusagawa, S.; Komada, H.; Nishio, M.; Ito, Y. !$#journal J. Gen. Virol. (1992) 73:1005-1010 !$#title Sequence analysis of the large (L) protein of simian virus !15. !$#cross-references MUID:92341049; PMID:1321873 !$#accession JQ1532 !'##molecule_type mRNA !'##residues 1-2255 ##label HIG !'##cross-references GB:D13868 GENETICS !$#gene L CLASSIFICATION #superfamily parainfluenza virus RNA-directed RNA polymerase KEYWORDS ATP; nucleotidyltransferase; RNA biosynthesis; RNA !1replication SUMMARY #length 2255 #molecular-weight 256052 #checksum 4057 SEQUENCE /// ENTRY JQ1750 #type complete TITLE genome polyprotein - simian paramyxovirus SV41 (strain Toshiba/Chanock) ALTERNATE_NAMES RNA nucleotidyltransferase (RNA-directed); RNA replicase CONTAINS RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name simian paramyxovirus SV41 DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 11-Jun-1999 ACCESSIONS JQ1750 REFERENCE JQ1750 !$#authors Ogawa, M.; Mutsuga, N.; Tsurudome, M.; Kawano, M.; !1Matsumura, H.; Kusagawa, S.; Komada, H.; Nishio, M.; Ito, Y. !$#journal J. Gen. Virol. (1992) 73:2743-2750 !$#title Nucleotide sequence analysis of the simian virus 41 gene !1encoding the large (L) protein and construction of a !1phylogenetic tree for the L proteins of paramyxoviruses. !$#cross-references MUID:93019033; PMID:1328485 !$#accession JQ1750 !'##molecule_type mRNA !'##residues 1-2269 ##label OGA !'##cross-references EMBL:X64275; NID:g433516; PIDN:CAA45569.1; !1PID:g433522 GENETICS !$#gene L CLASSIFICATION #superfamily parainfluenza virus RNA-directed RNA polymerase KEYWORDS ATP; nucleotidyltransferase; RNA biosynthesis; RNA !1replication SUMMARY #length 2269 #molecular-weight 256429 #checksum 9270 SEQUENCE /// ENTRY ZLNZMV #type complete TITLE genome polyprotein - measles virus (strain Udem) CONTAINS RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name measles virus DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 11-Jun-1999 ACCESSIONS A28919 REFERENCE A28919 !$#authors Blumberg, B.M.; Crowley, J.C.; Silverman, J.I.; Menonna, J.; !1Cook, S.D.; Dowling, P.C. !$#journal Virology (1988) 164:487-497 !$#title Measles virus L protein evidences elements of ancestral RNA !1polymerase. !$#cross-references MUID:88219537; PMID:2835864 !$#accession A28919 !'##molecule_type genomic RNA !'##residues 1-2183 ##label BLU !'##cross-references GB:M20865; NID:g331776; PIDN:AAA46430.1; !1PID:g331777 GENETICS !$#gene L CLASSIFICATION #superfamily parainfluenza virus RNA-directed RNA polymerase KEYWORDS ATP; nucleotidyltransferase SUMMARY #length 2183 #molecular-weight 247646 #checksum 1589 SEQUENCE /// ENTRY G48556 #type complete TITLE genome polyprotein - measles virus (strain AIK-C) ALTERNATE_NAMES L protein; RNA nucleotidyltransferase (RNA-directed); RNA replicase CONTAINS RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name measles virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 11-Jun-1999 ACCESSIONS G48556 REFERENCE A48556 !$#authors Mori, T.; Sasaki, K.; Hashimoto, H.; Makino, S. !$#journal Virus Genes (1993) 7:67-81 !$#title Molecular cloning and complete nucleotide sequence of !1genomic RNA of the AIK-C strain of attenuated measles virus. !$#cross-references MUID:93227570; PMID:8470368 !$#accession G48556 !'##molecule_type genomic RNA !'##residues 1-2183 ##label MOR !'##cross-references GB:S58435; NID:g299460; PIDN:AAB26147.1; !1PID:g299467 !'##note sequence extracted from NCBI backbone (NCBIN:129264, !1NCBIP:129274) GENETICS !$#gene L CLASSIFICATION #superfamily parainfluenza virus RNA-directed RNA polymerase KEYWORDS ATP; nucleotidyltransferase; RNA biosynthesis; RNA !1replication SUMMARY #length 2183 #molecular-weight 247754 #checksum 4122 SEQUENCE /// ENTRY A45389 #type complete TITLE genome polyprotein - canine distemper virus (strain Onderstepoort) ALTERNATE_NAMES RNA nucleotidyltransferase (RNA-directed); RNA replicase CONTAINS RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name canine distemper virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 29-May-1998 ACCESSIONS A45389 REFERENCE A45389 !$#authors Sidhu, M.S.; Menonna, J.P.; Cook, S.D.; Dowling, P.C.; Udem, !1S.A. !$#journal Virology (1993) 193:50-65 !$#title Canine distemper virus L gene: sequence and comparison with !1related viruses. !$#cross-references MUID:93174968; PMID:8438585 !$#accession A45389 !'##molecule_type genomic RNA !'##residues 1-2161 ##label SID !'##cross-references GB:L13195; NID:g289531; PID:g289532 GENETICS !$#gene L CLASSIFICATION #superfamily parainfluenza virus RNA-directed RNA polymerase KEYWORDS ATP; nucleotidyltransferase; RNA biosynthesis; RNA !1replication SUMMARY #length 2161 #molecular-weight 246370 #checksum 4916 SEQUENCE /// ENTRY RRNZA2 #type complete TITLE genome polyprotein - human respiratory syncytial virus (strain A2) ALTERNATE_NAMES polymerase L protein CONTAINS RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name human respiratory syncytial virus #note host Homo sapiens (man) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jun-2000 ACCESSIONS A40317; A28319; PS0048 REFERENCE A40317 !$#authors Stec, D.S.; Hill III, M.G.; Collins, P.L. !$#journal Virology (1991) 183:273-287 !$#title Sequence analysis of the polymerase L gene of human !1respiratory syncytial virus and predicted phylogeny of !1nonsegmented negative-strand viruses. !$#cross-references MUID:91272488; PMID:2053282 !$#accession A40317 !'##molecule_type mRNA !'##residues 1-2165 ##label STE !'##cross-references GB:M75730; NID:g333955; PIDN:AAA47418.1; !1PID:g333956 REFERENCE A28319 !$#authors Collins, P.L.; Olmsted, R.A.; Spriggs, M.K.; Johnson, P.R.; !1Buckler-White, A.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:5134-5138 !$#title Gene overlap and site-specific attenuation of transcription !1of the viral polymerase L gene of human respiratory !1syncytial virus. !$#cross-references MUID:87260943; PMID:2440043 !$#accession A28319 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-81 ##label COL !'##cross-references GB:M17245; NID:g333953; PIDN:AAA47417.1; !1PID:g333954 REFERENCE PS0048 !$#authors Johnson, P.R.; Collins, P.L. !$#journal J. Gen. Virol. (1988) 69:2901-2906 !$#title The A and B subgroups of human respiratory syncytial virus: !1comparison of intergenic and gene-overlap sequences. !$#cross-references MUID:89036169; PMID:3183631 !$#accession PS0048 !'##molecule_type mRNA !'##residues 1-18 ##label JOH !'##cross-references GB:D00397; NID:g222551; PID:g2160375 !'##experimental_source strain 18537 !'##note this strain belongs to subgroup B GENETICS !$#gene L CLASSIFICATION #superfamily parainfluenza virus RNA-directed RNA polymerase KEYWORDS ATP; nucleotidyltransferase SUMMARY #length 2165 #molecular-weight 250383 #checksum 6550 SEQUENCE /// ENTRY ZLVN #type complete TITLE genome polyprotein - vesicular stomatitis Indiana virus (strain Mudd-Summers) ALTERNATE_NAMES L protein CONTAINS RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name vesicular stomatitis Indiana virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 29-May-1998 ACCESSIONS A04119 REFERENCE A04119 !$#authors Schubert, M.; Harmison, G.G.; Meier, E. !$#journal J. Virol. (1984) 51:505-514 !$#title Primary structure of the vesicular stomatitis virus !1polymerase (L) gene: evidence for a high frequency of !1mutations. !$#cross-references MUID:84268017; PMID:6086959 !$#accession A04119 !'##molecule_type genomic RNA !'##residues 1-2109 ##label SCH !'##cross-references GB:K02378 GENETICS !$#gene L CLASSIFICATION #superfamily rhabdovirus L protein KEYWORDS nucleotidyltransferase; RNA binding; RNA biosynthesis; !1transmembrane protein FEATURE !$530-549 #region RNA binding #status predicted\ !$1959-1978 #domain transmembrane #status predicted #label TMN SUMMARY #length 2109 #molecular-weight 240982 #checksum 573 SEQUENCE /// ENTRY ZLVNNJ #type complete TITLE genome polyprotein - vesicular stomatitis New Jersey virus (strain Hazelhurst) ALTERNATE_NAMES L protein CONTAINS RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name vesicular stomatitis New Jersey virus DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 11-Jun-1999 ACCESSIONS A28602 REFERENCE A28602 !$#authors Feldhaus, A.L.; Lesnaw, J.A. !$#journal Virology (1988) 163:359-368 !$#title Nucleotide sequence of the L gene of vesicular stomatitis !1virus (New Jersey): identification of conserved domains in !1the New Jersey and Indiana L proteins. !$#cross-references MUID:88179540; PMID:2833012 !$#accession A28602 !'##molecule_type genomic RNA !'##residues 1-2109 ##label FEL !'##cross-references GB:M20166; NID:g336025; PIDN:AAA48440.1; !1PID:g336026 GENETICS !$#gene L CLASSIFICATION #superfamily rhabdovirus L protein KEYWORDS nucleotidyltransferase; RNA binding; RNA biosynthesis; !1transmembrane protein FEATURE !$530-549 #region RNA binding #status predicted\ !$1927-1943 #domain transmembrane #status predicted #label TM1 SUMMARY #length 2109 #molecular-weight 241581 #checksum 4162 SEQUENCE /// ENTRY A46309 #type complete TITLE genome polyprotein - vesicular stomatitis New Jersey virus (strain Ogden) ALTERNATE_NAMES RNA nucleotidyltransferase (RNA-directed); RNA replicase CONTAINS RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name vesicular stomatitis New Jersey virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 11-Jun-1999 ACCESSIONS A46309 REFERENCE A46309 !$#authors Barik, S.; Rud, E.W.; Luk, D.; Banerjee, A.K.; Kang, C.Y. !$#journal Virology (1990) 175:332-337 !$#title Nucleotide sequence analysis of the L gene of vesicular !1stomatitis virus (New Jersey serotype): identification of !1conserved domains in L proteins of nonsegmented !1negative-strand RNA viruses. !$#cross-references MUID:90177235; PMID:2155516 !$#accession A46309 !'##molecule_type genomic RNA !'##residues 1-2109 ##label BAR !'##cross-references GB:M29788; NID:g336029; PIDN:AAA48442.1; !1PID:g336030 GENETICS !$#gene L CLASSIFICATION #superfamily rhabdovirus L protein KEYWORDS nucleotidyltransferase; RNA binding; RNA biosynthesis; RNA !1replication FEATURE !$530-549 #region RNA binding #status predicted SUMMARY #length 2109 #molecular-weight 242111 #checksum 8101 SEQUENCE /// ENTRY ZLVNPV #type complete TITLE genome polyprotein - rabies virus (strain PV) ALTERNATE_NAMES L protein CONTAINS RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name rabies virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 11-Jun-1999 ACCESSIONS A29248; E24887 REFERENCE A29248 !$#authors Tordo, N.; Poch, O.; Ermine, A.; Keith, G.; Rougeon, F. !$#journal Virology (1988) 165:565-576 !$#title Completion of the rabies virus genome sequence !1determination: highly conserved domains among the L !1(polymerase) proteins of unsegmented negative-strand RNA !1viruses. !$#cross-references MUID:88306248; PMID:3407152 !$#accession A29248 !'##molecule_type genomic RNA !'##residues 1-2142 ##label TOR !'##cross-references GB:M13215; GB:M21634; NID:g333585; PIDN:AAA47219.1; !1PID:g333590 REFERENCE A94100 !$#authors Tordo, N.; Poch, O.; Ermine, A.; Keith, G.; Rougeon, F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:3914-3918 !$#title Walking along the rabies genome: is the large G-L intergenic !1region a remnant gene? !$#cross-references MUID:86233343; PMID:3459163 !$#accession E24887 !'##molecule_type DNA !'##residues 1-28 ##label TO2 GENETICS !$#gene L CLASSIFICATION #superfamily rhabdovirus L protein KEYWORDS nucleotidyltransferase; RNA binding; RNA biosynthesis; !1transmembrane protein FEATURE !$543-562 #region RNA binding #status predicted\ !$1965-1982 #domain transmembrane #status predicted #label TN2 SUMMARY #length 2142 #molecular-weight 244484 #checksum 433 SEQUENCE /// ENTRY ZLVNSB #type complete TITLE genome polyprotein - rabies virus (strain SAD B19) ALTERNATE_NAMES L protein CONTAINS RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name rabies virus DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 11-Jun-1999 ACCESSIONS E34746 REFERENCE A34746 !$#authors Conzelmann, K.K.; Cox, J.H.; Schneider, L.G.; Thiel, H.J. !$#journal Virology (1990) 175:485-499 !$#title Molecular cloning and complete nucleotide sequence of the !1attenuated rabies virus SAD B19. !$#cross-references MUID:90223994; PMID:2139267 !$#accession E34746 !'##molecule_type genomic RNA !'##residues 1-2127 ##label CON !'##cross-references GB:M31046; NID:g333556; PIDN:AAA47203.1; !1PID:g333561 GENETICS !$#gene L CLASSIFICATION #superfamily rhabdovirus L protein KEYWORDS nucleotidyltransferase; RNA binding; RNA biosynthesis; !1transmembrane protein FEATURE !$543-562 #region RNA binding #status predicted\ !$1965-1982 #domain transmembrane #status predicted #label TM2 SUMMARY #length 2127 #molecular-weight 242977 #checksum 9107 SEQUENCE /// ENTRY ZLVNSY #type complete TITLE genome polyprotein - Sonchus yellow net virus (ATCC PV-263) ALTERNATE_NAMES L protein CONTAINS RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name Sonchus yellow net virus DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 11-Jun-1999 ACCESSIONS A40230 REFERENCE A40230 !$#authors Choi, T.J.; Kuwata, S.; Koonin, E.V.; Heaton, L.A.; Jackson, !1A.O. !$#journal Virology (1992) 189:31-39 !$#title Structure of the L (polymerase) protein gene of sonchus !1yellow net virus. !$#cross-references MUID:92295567; PMID:1604816 !$#accession A40230 !'##molecule_type genomic RNA !'##residues 1-2116 ##label CHO !'##cross-references GB:M87829; NID:g335137; PIDN:AAA47896.1; !1PID:g335138 GENETICS !$#gene L CLASSIFICATION #superfamily rhabdovirus L protein KEYWORDS nucleotidyltransferase; RNA binding; RNA biosynthesis; !1transmembrane protein FEATURE !$567-586 #region RNA binding #status predicted\ !$1799-1815 #domain transmembrane #status predicted #label TM2 SUMMARY #length 2116 #molecular-weight 241536 #checksum 6747 SEQUENCE /// ENTRY RRXSIB #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) - infectious bursal disease virus ORGANISM #formal_name infectious bursal disease virus #note host Gallus gallus (chicken) DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 11-Jun-1999 ACCESSIONS A28649 REFERENCE A28649 !$#authors Morgan, M.M.; Macreadie, I.G.; Harley, V.R.; Hudson, P.J.; !1Azad, A.A. !$#journal Virology (1988) 163:240-242 !$#title Sequence of the small double-stranded RNA genomic segment of !1infectious bursal disease virus and its deduced 90-kDa !1product. !$#cross-references MUID:88160058; PMID:2831661 !$#accession A28649 !'##molecule_type genomic RNA !'##residues 1-878 ##label MOR !'##cross-references GB:M19336; NID:g331207; PIDN:AAA89177.1; !1PID:g331208 GENETICS !$#map_position segment B (small segment) CLASSIFICATION #superfamily avian infectious bursal disease virus !1RNA-directed RNA polymerase KEYWORDS nucleotidyltransferase; RNA replication SUMMARY #length 878 #molecular-weight 97273 #checksum 2037 SEQUENCE /// ENTRY RRXSI5 #type fragment TITLE RNA-directed RNA polymerase (EC 2.7.7.48) - infectious bursal disease virus (strain 52/70) (fragment) ORGANISM #formal_name infectious bursal disease virus #note host Gallus gallus (chicken) DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jun-2000 ACCESSIONS PS0378 REFERENCE PS0378 !$#authors Bayliss, C.D. !$#citation Ph.D. thesis, University College of Wales, 1990 !$#description Cloning and sequencing of infectious bursal disease virus !1and an investigation of the antigens of the virus. !$#accession PS0378 !'##molecule_type genomic RNA !'##residues 1-525 ##label BAY !'##cross-references DDBJ:D12610; NID:g221897; PIDN:BAA02135.1; !1PID:g221898 GENETICS !$#map_position segment B CLASSIFICATION #superfamily avian infectious bursal disease virus !1RNA-directed RNA polymerase KEYWORDS nucleotidyltransferase; RNA binding; RNA biosynthesis SUMMARY #length 525 #checksum 1905 SEQUENCE /// ENTRY RRXSJA #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) - infectious pancreatic necrosis virus (strain Jasper) ALTERNATE_NAMES VP1 protein ORGANISM #formal_name infectious pancreatic necrosis virus #note host Oncorhynchus sp. (salmon) DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 19-Jan-2001 ACCESSIONS A37946 REFERENCE A37946 !$#authors Duncan, R.; Mason, C.L.; Nagy, E.; Leong, J.A.; Dobos, P. !$#journal Virology (1991) 181:541-552 !$#title Sequence analysis of infectious pancreatic necrosis virus !1genome segment B and its encoded VP1 protein: a putative !1RNA-dependent RNA polymerase lacking the Gly-Asp-Asp motif. !$#cross-references MUID:91196245; PMID:1901682 !$#accession A37946 !'##molecule_type genomic RNA !'##residues 1-845 ##label DUN !'##cross-references GB:M58756; NID:g331313; PIDN:AAA46243.1; !1PID:g331314 !'##note the authors translated the codon GAC for residue 395 as Asn !'##note this protein lacks the GDD motif characteristic of this enzyme !1from single-stranded plus RNA viruses GENETICS !$#map_position segment B CLASSIFICATION #superfamily avian infectious bursal disease virus !1RNA-directed RNA polymerase KEYWORDS nucleotide binding; nucleotidyltransferase; P-loop; RNA !1replication FEATURE !$248-255 #region nucleotide-binding motif A (P-loop) SUMMARY #length 845 #molecular-weight 94466 #checksum 3444 SEQUENCE /// ENTRY RRXSSP #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) - infectious pancreatic necrosis virus (strain Sp) ALTERNATE_NAMES VP1 protein ORGANISM #formal_name infectious pancreatic necrosis virus #note host Oncorhynchus sp. (salmon) DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 19-Jan-2001 ACCESSIONS B37946 REFERENCE A37946 !$#authors Duncan, R.; Mason, C.L.; Nagy, E.; Leong, J.A.; Dobos, P. !$#journal Virology (1991) 181:541-552 !$#title Sequence analysis of infectious pancreatic necrosis virus !1genome segment B and its encoded VP1 protein: a putative !1RNA-dependent RNA polymerase lacking the Gly-Asp-Asp motif. !$#cross-references MUID:91196245; PMID:1901682 !$#accession B37946 !'##molecule_type genomic RNA !'##residues 1-844 ##label DUN !'##cross-references GB:M58756 !'##note the authors translated the codon CTG for residue 188 as Lys, !1GCC for residue 189 as Leu and GTT for residue 190 as Ala !'##note this protein lacks the GDD motif characteristic of this enzyme !1from single-stranded plus RNA viruses GENETICS !$#map_position segment B CLASSIFICATION #superfamily avian infectious bursal disease virus !1RNA-directed RNA polymerase KEYWORDS nucleotide binding; nucleotidyltransferase; P-loop; RNA !1replication FEATURE !$248-255 #region nucleotide-binding motif A (P-loop) SUMMARY #length 844 #molecular-weight 94088 #checksum 6115 SEQUENCE /// ENTRY RRIHM2 #type complete TITLE genome polyprotein 1a - murine hepatitis virus (strain JHM) ALTERNATE_NAMES 1a protein CONTAINS RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name murine hepatitis virus, MHV DATE 30-Sep-1990 #sequence_revision 31-Dec-1992 #text_change 23-Mar-2001 ACCESSIONS A36815; A34072; A43572 REFERENCE A36815 !$#authors Lee, H.J.; Shieh, C.K.; Gorbalenya, A.E.; Koonin, E.V.; La !1Monica, N.; Tuler, J.; Bagdzhardzhyan, A.; Lai, M.M.C. !$#submission submitted to GenBank, February 1991 !$#description The complete sequence (22 kilobases) of murine coronavirus !1gene 1 encoding the putative proteases and RNA polymerase. !$#accession A36815 !'##molecule_type genomic RNA !'##residues 1-4488 ##label LEE !'##cross-references GB:M55148; NID:g331851; PIDN:AAA46457.1; !1PID:g331852 REFERENCE A38547 !$#authors Lee, H.J.; Shieh, C.K.; Gorbalenya, A.E.; Koonin, E.V.; La !1Monica, N.; Tuler, J.; Bagdzhardzhyan, A.; Lai, M.M.C. !$#journal Virology (1991) 180:567-582 !$#title The complete sequence (22 kilobases) of murine coronavirus !1gene 1 encoding the putative proteases and RNA polymerase. !$#cross-references MUID:91111976; PMID:1846489 !$#contents annotation !$#note neither nucleotide nor complete amino acid sequence is given REFERENCE A34072 !$#authors Soe, L.H.; Shieh, C.K.; Baker, S.C.; Chang, M.F.; Lai, !1M.M.C. !$#journal J. Virol. (1987) 61:3968-3976 !$#title Sequence and translation of the murine coronavirus 5'-end !1genomic RNA reveals the N-terminal structure of the putative !1RNA polymerase. !$#cross-references MUID:88062951; PMID:2824826 !$#accession A34072 !'##molecule_type genomic RNA !'##residues 1-595 ##label SOE !'##cross-references GB:M18040; NID:g331873; PIDN:AAA46466.1; !1PID:g555243 REFERENCE A43572 !$#authors Baker, S.C.; La Monica, N.; Shieh, C.K.; Lai, M.M.C. !$#journal Adv. Exp. Med. Biol. (1990) 276:283-289 !$#title Murine coronavirus gene 1 polyprotein contains an !1autoproteolytic activity. !$#cross-references MUID:91353364; PMID:1966414 !$#accession A43572 !'##molecule_type genomic RNA !'##residues 1038-1343 ##label BAK !'##cross-references GB:S51684; NID:g234107; PIDN:AAB19566.1; !1PID:g234108 GENETICS !$#gene 1a CLASSIFICATION #superfamily coronavirus RNA-directed RNA polymerase KEYWORDS nucleotidyltransferase; RNA binding; RNA biosynthesis SUMMARY #length 4488 #molecular-weight 499895 #checksum 3318 SEQUENCE /// ENTRY VFIHB2 #type complete TITLE genome polyprotein - avian infectious bronchitis virus (strain Beaudette) ALTERNATE_NAMES F2 protein CONTAINS RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name avian infectious bronchitis virus, IBV DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 11-Jun-1999 ACCESSIONS B33094 REFERENCE A33094 !$#authors Boursnell, M.E.G.; Brown, T.D.K.; Foulds, I.J.; Green, P.F.; !1Tomley, F.M.; Binns, M.M. !$#journal J. Gen. Virol. (1987) 68:57-77 !$#title Completion of the sequence of the genome of the coronavirus !1avian infectious bronchitis virus. !$#cross-references MUID:87111468; PMID:3027249 !$#accession B33094 !'##molecule_type genomic RNA !'##residues 1-2652 ##label BOU !'##cross-references GB:M94356; GB:M29496; NID:g331170; PIDN:AAA46224.1; !1PID:g331173 CLASSIFICATION #superfamily infectious bronchitis virus RNA-directed RNA !1polymerase KEYWORDS glycoprotein; nucleotidyltransferase; RNA biosynthesis FEATURE !$69,543,711,726,977, !$1004,1240,1304, !$1382,1666,1795, !$1891,2057,2286, !$2317,2483,2550,2640 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 2652 #molecular-weight 300617 #checksum 8662 SEQUENCE /// ENTRY VFIHJH #type complete TITLE genome polyprotein 1b - murine hepatitis virus (strain JHM) ALTERNATE_NAMES 1b protein CONTAINS RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name murine hepatitis virus, MHV DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 11-Jun-1999 ACCESSIONS B36815 REFERENCE A36815 !$#authors Lee, H.J.; Shieh, C.K.; Gorbalenya, A.E.; Koonin, E.V.; La !1Monica, N.; Tuler, J.; Bagdzhardzhyan, A.; Lai, M.M.C. !$#submission submitted to GenBank, February 1991 !$#description The complete sequence (22 kilobases) of murine coronavirus !1gene 1 encoding the putative proteases and RNA polymerase. !$#accession B36815 !'##molecule_type genomic RNA !'##residues 1-2731 ##label LEE !'##cross-references GB:M55148; NID:g331851; PIDN:AAA46458.1; !1PID:g331853 REFERENCE A38547 !$#authors Lee, H.J.; Shieh, C.K.; Gorbalenya, A.E.; Koonin, E.V.; La !1Monica, N.; Tuler, J.; Bagdzhardzhyan, A.; Lai, M.M.C. !$#journal Virology (1991) 180:567-582 !$#title The complete sequence (22 kilobases) of murine coronavirus !1gene 1 encoding the putative proteases and RNA polymerase. !$#cross-references MUID:91111976; PMID:1846489 !$#contents annotation !$#note neither nucleotide nor complete amino acid sequence is given COMMENT This protein may be translated as a 1a-1b polyprotein by a !1ribosomal frameshifting mechanism. GENETICS !$#gene 1b CLASSIFICATION #superfamily infectious bronchitis virus RNA-directed RNA !1polymerase KEYWORDS glycoprotein; nucleotidyltransferase; RNA biosynthesis FEATURE !$269,304,785,1184, !$1287,1524,1842, !$2196,2575,2630, !$2645,2665 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 2731 #molecular-weight 308834 #checksum 5220 SEQUENCE /// ENTRY RRWVEV #type complete TITLE genome polyprotein - equine arteritis virus CONTAINS RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name equine arteritis virus #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 29-May-1998 ACCESSIONS A39925; S10158; B39925 REFERENCE A39925 !$#authors Den Boon, J.A.; Snijder, E.J.; Chirnside, E.D.; De Vries, !1A.A.F.; Horzinek, M.C.; Spaan, W.J.M. !$#journal J. Virol. (1991) 65:2910-2920 !$#title Equine arteritis virus is not a togavirus but belongs to the !1coronaviruslike superfamily. !$#cross-references MUID:91237805; PMID:1851863 !$#accession A39925 !'##molecule_type genomic RNA !'##residues 1-3175 ##label DEN !'##cross-references EMBL:X53459 !'##note a -1 ribosomal frameshift occurs between the codons AAC for !11727-Asn and CUG for 1728-Leu REFERENCE S10158 !$#authors de Vries, A.A.F.; Chirnside, E.D.; Bredenbeek, P.J.; !1Gravestein, L.A.; Horzinek, M.C.; Spaan, W.J.M. !$#journal Nucleic Acids Res. (1990) 18:3241-3247 !$#title All subgenomic mRNAs of equine arteritis virus contain a !1common leader sequence. !$#cross-references MUID:90287699; PMID:2162519 !$#accession S10158 !'##status translation not shown !'##molecule_type genomic RNA !'##residues 1-17 ##label VRI !'##cross-references EMBL:X52277 CLASSIFICATION #superfamily equine arteritis virus RNA-directed RNA !1polymerase KEYWORDS nucleotidyltransferase SUMMARY #length 3175 #molecular-weight 345277 #checksum 9571 SEQUENCE /// ENTRY RRXPTV #type complete TITLE genome polyprotein - Tacaribe virus CONTAINS RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name Tacaribe virus DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 11-Jun-1999 ACCESSIONS A31468 REFERENCE A31468 !$#authors Iapalucci, S.; Lopez, R.; Rey, O.; Lopez, N.; !1Franze-Fernandez, M.T.; Cohen, G.N.; Lucero, M.; Ochoa, A.; !1Zakin, M.M. !$#journal Virology (1989) 170:40-47 !$#title Tacaribe virus L gene encodes a protein of 2210 amino acid !1residues. !$#cross-references MUID:89243206; PMID:2718387 !$#accession A31468 !'##molecule_type genomic RNA !'##residues 1-2210 ##label IAP !'##cross-references GB:J04340; GB:M33513; NID:g335147; PIDN:AAA47901.1; !1PID:g335149 GENETICS !$#map_position segment L CLASSIFICATION #superfamily arenavirus RNA-directed RNA polymerase KEYWORDS nucleotidyltransferase SUMMARY #length 2210 #molecular-weight 252230 #checksum 8170 SEQUENCE /// ENTRY RRXPLC #type complete TITLE genome polyprotein - lymphocytic choriomeningitis virus (strain Armstrong 53b) CONTAINS RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name lymphocytic choriomeningitis virus DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 11-Jun-1999 ACCESSIONS A30181 REFERENCE A30181 !$#authors Salvato, M.; Shimomaye, E.; Oldstone, M.B.A. !$#journal Virology (1989) 169:377-384 !$#title The primary structure of the lymphocytic choriomeningitis !1virus L gene encodes a putative RNA polymerase. !$#cross-references MUID:89204909; PMID:2705303 !$#accession A30181 !'##molecule_type genomic RNA !'##residues 1-2210 ##label SAL !'##cross-references GB:J04331; NID:g331368; PIDN:AAA66591.1; !1PID:g331369 GENETICS !$#map_position segment L CLASSIFICATION #superfamily arenavirus RNA-directed RNA polymerase KEYWORDS nucleotidyltransferase SUMMARY #length 2210 #molecular-weight 254529 #checksum 7158 SEQUENCE /// ENTRY RRVECV #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) - carnation mottle virus ALTERNATE_NAMES RNA nucleotidyltransferase (RNA-directed); RNA replicase ORGANISM #formal_name carnation mottle virus, CarMV DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 25-Oct-1996 ACCESSIONS A04208 REFERENCE A93590 !$#authors Guilley, H.; Carrington, J.C.; Balazs, E.; Jonard, G.; !1Richards, K.; Morris, T.J. !$#journal Nucleic Acids Res. (1985) 13:6663-6677 !$#title Nucleotide sequence and genome organization of carnation !1mottle virus RNA. !$#cross-references MUID:86041863; PMID:3840587 !$#accession A04208 !'##molecule_type genomic RNA !'##residues 1-867 ##label GUI !'##cross-references GB:X02986 !'##note readthrough of two terminators may occur: UAG between codons !1AAA for 245-Lys and GGG for 246-Gly, and UAG between codons !1CAG for 762-Gln and UUG for 763-Leu CLASSIFICATION #superfamily carnation mottle virus RNA-directed RNA !1polymerase; barley yellow dwarf virus RNA-directed RNA !1polymerase homology KEYWORDS nucleotidyltransferase; RNA biosynthesis; RNA replication FEATURE !$470-633 #domain barley yellow dwarf virus RNA-directed RNA !8polymerase homology #label BYD SUMMARY #length 867 #molecular-weight 97407 #checksum 8426 SEQUENCE /// ENTRY RRVETC #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) - turnip crinkle virus ALTERNATE_NAMES RNA nucleotidyltransferase (RNA-directed); RNA replicase CONTAINS 28K protein ORGANISM #formal_name turnip crinkle virus #note host Brassica rapa (turnip) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 25-Oct-1996 ACCESSIONS JA0110 REFERENCE A94394 !$#authors Carrington, J.C.; Heaton, L.A.; Zuidema, D.; Hillman, B.I.; !1Morris, T.J. !$#journal Virology (1989) 170:219-226 !$#title The genome structure of turnip crinkle virus. !$#cross-references MUID:89243179; PMID:2718381 !$#accession JA0110 !'##molecule_type mRNA !'##residues 1-774 ##label CAR !'##cross-references GB:M22445 !'##note readthrough of the terminator UAG may occur between codons CGC !1for 250-Arg and GGG for 251-Gly CLASSIFICATION #superfamily carnation mottle virus RNA-directed RNA !1polymerase; barley yellow dwarf virus RNA-directed RNA !1polymerase homology KEYWORDS nucleotidyltransferase; RNA biosynthesis; RNA replication FEATURE !$1-250 #product 28K protein #status predicted #label PKP\ !$476-638 #domain barley yellow dwarf virus RNA-directed RNA !8polymerase homology #label BYD SUMMARY #length 774 #molecular-weight 87643 #checksum 1925 SEQUENCE /// ENTRY RRWQTN #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) - tobacco necrosis virus (strain A) ALTERNATE_NAMES RNA nucleotidyltransferase (RNA-directed); RNA replicase CONTAINS 23K protein ORGANISM #formal_name tobacco necrosis virus, TNV #note host Phaseolus vulgaris (kidney bean) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 11-Jun-1999 ACCESSIONS A35523 REFERENCE A35523 !$#authors Meulewaeter, F.; Seurinck, J.; van Emmelo, J. !$#journal Virology (1990) 177:699-709 !$#title Genome structure of tobacco necrosis virus strain A. !$#cross-references MUID:90320143; PMID:2371773 !$#accession A35523 !'##molecule_type genomic RNA !'##residues 1-723 ##label MEU !'##cross-references EMBL:M33002; NID:g1172549; PIDN:AAA86434.1; !1PID:g310915 !'##note readthrough of the terminator UAG occurs between codons AAA for !1202-Lys and GGG for 203-Gly CLASSIFICATION #superfamily carnation mottle virus RNA-directed RNA !1polymerase; barley yellow dwarf virus RNA-directed RNA !1polymerase homology KEYWORDS nucleotidyltransferase; RNA biosynthesis; RNA replication FEATURE !$1-202 #product 23K protein #status predicted #label KPP\ !$427-593 #domain barley yellow dwarf virus RNA-directed RNA !8polymerase homology #label BYD SUMMARY #length 723 #molecular-weight 82167 #checksum 2224 SEQUENCE /// ENTRY RRWQTD #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) - tobacco necrosis virus (strain D) ALTERNATE_NAMES RNA nucleotidyltransferase (RNA-directed); RNA replicase CONTAINS 22K protein ORGANISM #formal_name tobacco necrosis virus, TNV DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 25-Oct-1996 ACCESSIONS JU0368 REFERENCE JU0368 !$#authors Coutts, R.H.A.; Rigden, J.E.; Slabas, A.R.; Lomonossoff, !1G.P.; Wise, P.J. !$#journal J. Gen. Virol. (1991) 72:1521-1529 !$#title The complete sequence of tobacco necrosis virus strain D. !$#cross-references MUID:91311404; PMID:1856691 !$#accession JU0368 !'##molecule_type genomic RNA !'##residues 1-724 ##label COU !'##cross-references GB:D00942 !'##note readthrough of the terminator TAG occurs between codons AAA for !1202-Lys and GGA for 203-Gly CLASSIFICATION #superfamily carnation mottle virus RNA-directed RNA !1polymerase; barley yellow dwarf virus RNA-directed RNA !1polymerase homology KEYWORDS nucleotidyltransferase; RNA biosynthesis; RNA replication FEATURE !$1-202 #product 22K protein #status predicted #label KPT\ !$427-597 #domain barley yellow dwarf virus RNA-directed RNA !8polymerase homology #label BYD SUMMARY #length 724 #molecular-weight 82172 #checksum 1740 SEQUENCE /// ENTRY RRVGCN #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) - cucumber necrosis virus ALTERNATE_NAMES RNA nucleotidyltransferase (RNA-directed); RNA replicase CONTAINS 33K protein ORGANISM #formal_name cucumber necrosis virus #note host Cucumis sativus (cucumber) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 11-Jun-1999 ACCESSIONS JA0130; JA0129 REFERENCE A94391 !$#authors Rochon, D.M.; Tremaine, J.H. !$#journal Virology (1989) 169:251-259 !$#title Complete nucleotide sequence of the cucumber necrosis virus !1genome. !$#cross-references MUID:89204896; PMID:2705296 !$#accession JA0130 !'##molecule_type genomic RNA !'##residues 1-817 ##label ROC !'##cross-references GB:M25270; NID:g323338; PIDN:AAA42902.1; !1PID:g323339 !'##note readthrough of the terminator UAG occurs between codons AAA for !1296-Lys and GGA for 297-Gly CLASSIFICATION #superfamily carnation mottle virus RNA-directed RNA !1polymerase; barley yellow dwarf virus RNA-directed RNA !1polymerase homology KEYWORDS nucleotidyltransferase; RNA biosynthesis; RNA replication FEATURE !$1-296 #product 33K protein #status predicted #label TTP\ !$527-694 #domain barley yellow dwarf virus RNA-directed RNA !8polymerase homology #label BYD SUMMARY #length 817 #molecular-weight 92008 #checksum 8499 SEQUENCE /// ENTRY RRVGCT #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) - tomato bushy stunt virus (strain cherry) ALTERNATE_NAMES RNA nucleotidyltransferase (RNA-directed); RNA replicase CONTAINS 33K protein ORGANISM #formal_name tomato bushy stunt virus, TBSV DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 25-Oct-1996 ACCESSIONS A35315 REFERENCE A35315 !$#authors Hearne, P.Q.; Knorr, D.A.; Hillman, B.I.; Morris, T.J. !$#journal Virology (1990) 177:141-151 !$#title The complete genome structure and synthesis of infectious !1RNA from clones of tomato bushy stunt virus. !$#cross-references MUID:90281577; PMID:2353450 !$#accession A35315 !'##molecule_type genomic RNA !'##residues 1-817 ##label HEA !'##cross-references EMBL:M31019 !'##note readthrough of the terminator UAG occurs between codons AAA for !1296-Lys and GGA for 297-Gly CLASSIFICATION #superfamily carnation mottle virus RNA-directed RNA !1polymerase; barley yellow dwarf virus RNA-directed RNA !1polymerase homology KEYWORDS nucleotidyltransferase; RNA biosynthesis; RNA replication FEATURE !$1-296 #product 33K protein #status predicted #label P33\ !$527-694 #domain barley yellow dwarf virus RNA-directed RNA !8polymerase homology #label BYD SUMMARY #length 817 #molecular-weight 92141 #checksum 9530 SEQUENCE /// ENTRY RRVGCR #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) - Cymbidium ringspot virus ALTERNATE_NAMES RNA nucleotidyltransferase (RNA-directed); RNA replicase CONTAINS 33K protein ORGANISM #formal_name Cymbidium ringspot virus DATE 31-Mar-1990 #sequence_revision 01-Dec-2000 #text_change 01-Dec-2000 ACCESSIONS S05456; JS0268 REFERENCE JS0268 !$#authors Grieco, F.; Burgyan, J.; Russo, M. !$#journal Nucleic Acids Res. (1989) 17:6383 !$#title The nucleotide sequence of Cymbidium ringspot virus RNA. !$#cross-references MUID:89366663; PMID:2771646 !$#accession S05456 !'##status preliminary; translation not shown !'##molecule_type genomic RNA !'##residues 1-818 ##label GRI !'##cross-references EMBL:X15511; NID:g59020; PIDN:CAB38439.1; !1PID:g4469160 !$#accession JS0268 !'##molecule_type genomic RNA !'##residues 1-296,298-483,'I',485-818 ##label GR2 !'##cross-references GB:X15511 !'##note readthrough of the terminator TAG occurs between codons AAA for !1296-Lys and GGA for 298-Gly CLASSIFICATION #superfamily carnation mottle virus RNA-directed RNA !1polymerase; barley yellow dwarf virus RNA-directed RNA !1polymerase homology KEYWORDS nucleotidyltransferase; RNA biosynthesis; RNA replication FEATURE !$1-296 #product 33K protein #status predicted #label TTP\ !$528-695 #domain barley yellow dwarf virus RNA-directed RNA !8polymerase homology #label BYD SUMMARY #length 818 #molecular-weight 91946 #checksum 6811 SEQUENCE /// ENTRY RRVQC2 #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) 60.5K chain - barley yellow dwarf virus ALTERNATE_NAMES RNA nucleotidyltransferase (RNA-directed); RNA replicase ORGANISM #formal_name barley yellow dwarf virus, BYDV DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Aug-2000 ACCESSIONS JQ1416; JQ1410; S00947 REFERENCE JQ1409 !$#authors Ueng, P.P.; Vincent, J.R.; Kawata, E.E.; Lei, C.H.; Lister, !1R.M.; Larkins, B.A. !$#journal J. Gen. Virol. (1992) 73:487-492 !$#title Nucleotide sequence analysis of the genomes of the MAV-PS1 !1and P-PAV isolates of barley yellow dwarf virus. !$#cross-references MUID:92166764; PMID:1538199 !$#accession JQ1416 !'##molecule_type genomic RNA !'##residues 1-532 ##label UEN !'##cross-references GB:D11032; DDBJ:D01214; NID:g221098; !1PIDN:BAA01786.1; PID:g221100 !'##experimental_source strain P-PAV !'##note the authors translated the codon ATA for residue 519 as Ala !'##note 530-Asn was also found !$#accession JQ1410 !'##molecule_type genomic RNA !'##residues 1-38,'C',40-71,'Y',73-109,'K',111-138,'I',140-254,'V', !1256-349,'R',351-465,'FQD',469-498,'N',500-528,'HN',531-532 !1##label UE2 !'##cross-references GB:D11028; DDBJ:D01213; NID:g221084; !1PIDN:BAA01780.1; PID:g221086 !'##experimental_source strain MAV-PS1 !'##note the authors translated the codon AGT for residue 196 as Arg !'##note 258-Asn and 290-Ser were also found REFERENCE S00946 !$#authors Miller, W.A.; Waterhouse, P.M.; Gerlach, W.L. !$#journal Nucleic Acids Res. (1988) 16:6097-6111 !$#title Sequence and organization of barley yellow dwarf virus !1genomic RNA. !$#cross-references MUID:88289355; PMID:3399386 !$#accession S00947 !'##molecule_type genomic RNA !'##residues 1-109,'K',111-136,'K',138-260,'M',262-312,'L',314-529,'N', !1531-532 ##label MIL !'##cross-references EMBL:X07653; NID:g58798 !'##experimental_source strain Australian isolate, PAV serotype !'##note the sequence is revised in GenBank entry BYDVPAV, release 117, !1(PIDN:CAA30498.1) COMMENT For an alternative 'transframe' form, see (PIR:A59303). CLASSIFICATION #superfamily barley yellow dwarf virus RNA-directed RNA !1polymerase 60.5K chain; barley yellow dwarf virus !1RNA-directed RNA polymerase homology KEYWORDS nucleotidyltransferase; RNA biosynthesis; RNA replication FEATURE !$230-393 #domain barley yellow dwarf virus RNA-directed RNA !8polymerase homology #label BYD SUMMARY #length 532 #molecular-weight 60436 #checksum 3551 SEQUENCE /// ENTRY B43684 #type complete TITLE probable RNA-directed RNA polymerase (EC 2.7.7.48) 27K/57K chain - red clover necrotic mosaic virus (strain Australia) ALTERNATE_NAMES 27K protein; RNA nucleotidyltransferase (RNA-directed); RNA replicase ORGANISM #formal_name red clover necrotic mosaic virus DATE 31-Dec-1993 #sequence_revision 13-Aug-1999 #text_change 15-Oct-1999 ACCESSIONS T10779; T10780; T10781; A43684; B43684 REFERENCE Z17138 !$#authors Xiong, Z.; Kim, K.H.; Kendall, T.L.; Lommel, S.A. !$#journal Virology (1993) 193:213-221 !$#title Synthesis of the putative red clover necrotic mosaic virus !1RNA polymerase by ribosomal frameshifting in vitro. !$#cross-references MUID:93174929; PMID:8438566 !$#accession T10779 !'##status translated from GB/EMBL/DDBJ !'##molecule_type genomic RNA !'##residues 1-766 ##label XIO !'##cross-references EMBL:J04357; NID:g333772; PIDN:AAB02540.1; !1PID:g1375094 !$#accession T10780 !'##status translated from GB/EMBL/DDBJ !'##molecule_type genomic RNA !'##residues 1-236 ##label XIW !'##cross-references EMBL:J04357; NID:g333772; PIDN:AAB02539.1; !1PID:g333773 !$#accession T10781 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type genomic RNA !'##residues 268-766 ##label XIF !'##cross-references EMBL:J04357; NID:g333772; PIDN:AAB02541.1; !1PID:g333774 REFERENCE A43684 !$#authors Xiong, Z.; Lommel, S.A. !$#journal Virology (1989) 171:543-554 !$#title The complete nucleotide sequence and genome organization of !1red clover necrotic mosaic virus RNA-1. !$#cross-references MUID:89348013; PMID:2763465 !$#accession A43684 !'##status preliminary !'##molecule_type genomic RNA !'##residues 1-236 ##label XI2 !'##cross-references GB:J04357; GB:M24621; NID:g333772; PIDN:AAB02539.1; !1PID:g333773 !'##experimental_source strain Australia !$#accession B43684 !'##molecule_type genomic RNA !'##residues 268-766 ##label XIA !'##cross-references GB:J04357; GB:M24621; NID:g333772; PIDN:AAB02541.1; !1PID:g333774 GENETICS !$#map_position segment 1 !$#introns 236/3 CLASSIFICATION #superfamily barley yellow dwarf virus RNA-directed RNA !1polymerase 60.5K chain; barley yellow dwarf virus !1RNA-directed RNA polymerase homology KEYWORDS nucleotidyltransferase; RNA biosynthesis; RNA replication; !1translational frameshift FEATURE !$1-766 #product probable RNA-directed RNA polymerase, 27K/ !857K chain #status predicted #label MAT1\ !$1-236 #product probable RNA-directed RNA polymerase, 27K !8chain #status predicted #label MAT2\ !$236-237 #region minus-one translational frameshift\ !$268-766 #product probable RNA-directed RNA polymerase, 57K !8chain #status predicted #label MAT3\ !$466-632 #domain barley yellow dwarf virus RNA-directed RNA !8polymerase homology #label BYD SUMMARY #length 766 #molecular-weight 87430 #checksum 4054 SEQUENCE /// ENTRY RRVQLL #type complete TITLE probable RNA-directed RNA polymerase (EC 2.7.7.48) - potato leaf roll virus (strain 1) ORGANISM #formal_name potato leaf roll virus #note host Solanum tuberosum (potato) DATE 31-Mar-1990 #sequence_revision 30-Sep-1991 #text_change 21-Jul-2000 ACCESSIONS JA0119; S24592 REFERENCE JA0119 !$#authors Mayo, M.A.; Robinson, D.J.; Jolly, C.A.; Hyman, L. !$#journal J. Gen. Virol. (1989) 70:1037-1051 !$#title Nucleotide sequence of potato leafroll luteovirus RNA. !$#cross-references MUID:89279282; PMID:2732710 !$#accession JA0119 !'##molecule_type genomic RNA !'##residues 1-616 ##label MAY !'##cross-references EMBL:X14600; NID:g222293; PIDN:BAA00418.1; !1PID:g222294 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1March 1989 CLASSIFICATION #superfamily potato leaf roll virus RNA-directed RNA !1polymerase KEYWORDS nucleotidyltransferase; RNA biosynthesis SUMMARY #length 616 #molecular-weight 69592 #checksum 5648 SEQUENCE /// ENTRY RRVQWA #type complete TITLE probable RNA-directed RNA polymerase (EC 2.7.7.48) - potato leaf roll virus (strain Wageningen) ORGANISM #formal_name potato leaf roll virus DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jun-2000 ACCESSIONS S03548 REFERENCE S03546 !$#authors van der Wilk, F.; Huisman, M.J.; Cornelissen, B.J.C.; !1Huttinga, H.; Goldbach, R. !$#journal FEBS Lett. (1989) 245:51-56 !$#title Nucleotide sequence and organization of potato leafroll !1virus genomic RNA. !$#cross-references MUID:89171329; PMID:2466700 !$#accession S03548 !'##molecule_type genomic RNA !'##residues 1-616 ##label VAN !'##cross-references EMBL:Y07496; NID:g61198; PIDN:CAA68796.1; !1PID:g1335510 CLASSIFICATION #superfamily potato leaf roll virus RNA-directed RNA !1polymerase KEYWORDS nucleotidyltransferase; RNA biosynthesis SUMMARY #length 616 #molecular-weight 69625 #checksum 6417 SEQUENCE /// ENTRY RRVQFL #type complete TITLE probable RNA-directed RNA polymerase (EC 2.7.7.48) - beet western yellows virus (isolate FL1) ORGANISM #formal_name beet western yellows virus DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jun-2000 ACCESSIONS S01940 REFERENCE S01935 !$#authors Veidt, I.; Lot, H.; Leiser, M.; Scheidecker, D.; Guilley, !1H.; Richards, K.; Jonard, G. !$#journal Nucleic Acids Res. (1988) 16:9917-9932 !$#title Nucleotide sequence of beet western yellows virus RNA. !$#cross-references MUID:89057523; PMID:3194229 !$#accession S01940 !'##molecule_type genomic RNA !'##residues 1-586 ##label VEI !'##cross-references EMBL:X13063; NID:g62294; PIDN:CAA31464.1; !1PID:g1334816 CLASSIFICATION #superfamily potato leaf roll virus RNA-directed RNA !1polymerase KEYWORDS nucleotidyltransferase; RNA biosynthesis SUMMARY #length 586 #molecular-weight 66758 #checksum 3138 SEQUENCE /// ENTRY RRXBPM #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) - pea enation mosaic virus ORGANISM #formal_name pea enation mosaic virus, PEMV DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 11-Jun-1999 ACCESSIONS JQ1384 REFERENCE JQ1382 !$#authors Demler, S.A.; de Zoeten, G.A. !$#journal J. Gen. Virol. (1991) 72:1819-1834 !$#title The nucleotide sequence and luteovirus-like nature of RNA 1 !1of an aphid non-transmissible strain of pea enation mosaic !1virus. !$#cross-references MUID:91341468; PMID:1875194 !$#accession JQ1384 !'##molecule_type genomic RNA !'##residues 1-599 ##label DEM !'##cross-references GB:L04573; NID:g294105; PIDN:AAA72297.1; !1PID:g294106 !'##note 66-Ser, 78-Pro, 84-Ile, 93-Ile, 95-Gly, 104-His, 336-Leu, !1359-Lys and 410-Phe were also found GENETICS !$#map_position segment 1 CLASSIFICATION #superfamily potato leaf roll virus RNA-directed RNA !1polymerase KEYWORDS nucleotidyltransferase; RNA biosynthesis SUMMARY #length 599 #molecular-weight 67189 #checksum 1986 SEQUENCE /// ENTRY RRBWSC #type complete TITLE probable RNA-directed RNA polymerase (EC 2.7.7.48) - southern bean mosaic virus (strain cowpea) ORGANISM #formal_name southern bean mosaic virus, SBMV DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 11-Jun-1999 ACCESSIONS B33739 REFERENCE A33739 !$#authors Wu, S.; Rinehart, C.A.; Kaesberg, P. !$#journal Virology (1987) 161:73-80 !$#title Sequence and organization of southern bean mosaic virus !1genomic RNA. !$#cross-references MUID:88044510; PMID:2823471 !$#accession B33739 !'##molecule_type genomic RNA !'##residues 1-956 ##label WUS !'##cross-references GB:M23021; NID:g511859; PIDN:AAA46565.1; !1PID:g511861 CLASSIFICATION #superfamily potato leaf roll virus RNA-directed RNA !1polymerase KEYWORDS nucleotidyltransferase; RNA biosynthesis SUMMARY #length 956 #molecular-weight 104843 #checksum 8128 SEQUENCE /// ENTRY RRWPEM #type complete TITLE genome polyprotein - eggplant mosaic virus ALTERNATE_NAMES RNA nucleotidyltransferase (RNA-directed); RNA replicase CONTAINS RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name eggplant mosaic virus DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 19-Jan-2001 ACCESSIONS JQ0102 REFERENCE JQ0102 !$#authors Osorio-Keese, M.E.; Keese, P.; Gibbs, A. !$#journal Virology (1989) 172:547-554 !$#title Nucleotide sequence of the genome of eggplant mosaic !1tymovirus. !$#cross-references MUID:90021185; PMID:2800336 !$#accession JQ0102 !'##molecule_type genomic RNA !'##residues 1-1839 ##label OSO !'##cross-references EMBL:J04374 CLASSIFICATION #superfamily eggplant mosaic virus RNA-directed RNA !1polymerase KEYWORDS ATP; nucleotide binding; nucleotidyltransferase; P-loop; RNA !1biosynthesis; RNA replication FEATURE !$965-972 #region nucleotide-binding motif A (P-loop)\ !$1027-1032 #region nucleotide-binding motif B\ !$971 #binding_site ATP (Lys) #status predicted SUMMARY #length 1839 #molecular-weight 204731 #checksum 7757 SEQUENCE /// ENTRY RRWPYM #type complete TITLE genome polyprotein - Ononis yellow mosaic virus ALTERNATE_NAMES RNA nucleotidyltransferase (RNA-directed); RNA replicase CONTAINS RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name Ononis yellow mosaic virus DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 19-Jan-2001 ACCESSIONS JQ0106 REFERENCE JQ0106 !$#authors Ding, S.W.; Keese, P.; Gibbs, A. !$#journal Virology (1989) 172:555-563 !$#title Nucleotide sequence of the ononis yellow mosaic tymovirus !1genome. !$#cross-references MUID:90021186; PMID:2800337 !$#accession JQ0106 !'##molecule_type genomic RNA !'##residues 1-1776 ##label DIN !'##cross-references EMBL:J04375; NID:g332572; PIDN:AAA46796.1; !1PID:g332574 CLASSIFICATION #superfamily eggplant mosaic virus RNA-directed RNA !1polymerase KEYWORDS ATP; nucleotide binding; nucleotidyltransferase; P-loop; RNA !1biosynthesis; RNA replication FEATURE !$899-906 #region nucleotide-binding motif A (P-loop)\ !$961-966 #region nucleotide-binding motif B\ !$905 #binding_site ATP (Lys) #status predicted SUMMARY #length 1776 #molecular-weight 198126 #checksum 2690 SEQUENCE /// ENTRY RRWPTM #type complete TITLE genome polyprotein - turnip yellow mosaic virus (strain Australia) ALTERNATE_NAMES RNA nucleotidyltransferase (RNA-directed); RNA replicase CONTAINS RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name turnip yellow mosaic virus, TYMV DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 19-Jan-2001 ACCESSIONS JQ0109 REFERENCE JQ0109 !$#authors Keese, P.; Mackenzie, A.; Gibbs, A. !$#journal Virology (1989) 172:536-546 !$#title Nucleotide sequence of the genome of an Australian isolate !1of turnip yellow mosaic tymovirus. !$#cross-references MUID:90021184; PMID:2800335 !$#accession JQ0109 !'##molecule_type genomic RNA !'##residues 1-1844 ##label KEE !'##cross-references EMBL:J04373; NID:g332244; PIDN:AAA46592.1; !1PID:g332246 CLASSIFICATION #superfamily eggplant mosaic virus RNA-directed RNA !1polymerase KEYWORDS ATP; nucleotide binding; nucleotidyltransferase; P-loop; RNA !1biosynthesis; RNA replication FEATURE !$976-983 #region nucleotide-binding motif A (P-loop)\ !$1038-1043 #region nucleotide-binding motif B\ !$982 #binding_site ATP (Lys) #status predicted SUMMARY #length 1844 #molecular-weight 206509 #checksum 7651 SEQUENCE /// ENTRY JQ0533 #type complete TITLE genome polyprotein - Kennedya yellow mosaic virus (strain Jervis Bay) ALTERNATE_NAMES RNA nucleotidyltransferase (RNA-directed); RNA replicase CONTAINS RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name Kennedya yellow mosaic virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 19-Jan-2001 ACCESSIONS JQ0533 REFERENCE JQ0532 !$#authors Ding, S.; Keese, P.; Gibbs, A. !$#journal J. Gen. Virol. (1990) 71:925-931 !$#title The nucleotide sequence of the genomic RNA of kennedya !1yellow mosaic tymovirus-Jervis Bay isolate: relationships !1with potex- and carlaviruses. !$#cross-references MUID:90218040; PMID:2324710 !$#accession JQ0533 !'##molecule_type genomic RNA !'##residues 1-1874 ##label DIN !'##cross-references GB:D00637; NID:g221969; PIDN:BAA00532.1; !1PID:g221971 CLASSIFICATION #superfamily eggplant mosaic virus RNA-directed RNA !1polymerase KEYWORDS ATP; nucleotide binding; nucleotidyltransferase; P-loop; RNA !1biosynthesis; RNA replication FEATURE !$1002-1009 #region nucleotide-binding motif A (P-loop)\ !$1064-1069 #region nucleotide-binding motif B\ !$1008 #binding_site ATP (Lys) #status predicted SUMMARY #length 1874 #molecular-weight 210028 #checksum 8952 SEQUENCE /// ENTRY JQ1555 #type complete TITLE genome polyprotein - Erysimum latent virus ALTERNATE_NAMES RNA nucleotidyltransferase (RNA-directed); RNA replicase CONTAINS RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name Erysimum latent virus, CLV DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 19-Jan-2001 ACCESSIONS JQ1555 REFERENCE JQ1554 !$#authors Srifah, P.; Keese, P.; Weiller, G.; Gibbs, A. !$#journal J. Gen. Virol. (1992) 73:1437-1447 !$#title Comparisons of the genomic sequences of erysimum latent !1virus and other tymoviruses: A search for the molecular !1basis of their host specificities. !$#cross-references MUID:92300338; PMID:1607861 !$#accession JQ1555 !'##molecule_type genomic RNA !'##residues 1-1748 ##label SRI !'##cross-references GB:AF098523; NID:g3892230; PIDN:AAC80555.1; !1PID:g3892232 CLASSIFICATION #superfamily eggplant mosaic virus RNA-directed RNA !1polymerase KEYWORDS ATP; nucleotide binding; nucleotidyltransferase; P-loop; RNA !1biosynthesis; RNA replication FEATURE !$874-881 #region nucleotide-binding motif A (P-loop)\ !$936-941 #region nucleotide-binding motif B\ !$880 #binding_site ATP (Lys) #status predicted SUMMARY #length 1748 #molecular-weight 193905 #checksum 2698 SEQUENCE /// ENTRY RRWGSM #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) - strawberry mild yellow edge-associated virus ALTERNATE_NAMES RNA nucleotidyltransferase (RNA-directed); RNA replicase ORGANISM #formal_name strawberry mild yellow edge-associated virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 19-Jan-2001 ACCESSIONS JQ1426 REFERENCE JQ1426 !$#authors Jelkmann, W.; Maiss, E.; Martin, R.R. !$#journal J. Gen. Virol. (1992) 73:475-479 !$#title The nucleotide sequence and genome organization of !1strawberry mild yellow edge-associated potexvirus. !$#cross-references MUID:92166762; PMID:1339469 !$#accession JQ1426 !'##molecule_type genomic RNA !'##residues 1-1323 ##label JEL !'##cross-references GB:D12517; DDBJ:D01227; NID:g222631; !1PIDN:BAA02082.1; PID:g222632 CLASSIFICATION #superfamily eggplant mosaic virus RNA-directed RNA !1polymerase KEYWORDS ATP; nucleotide binding; nucleotidyltransferase; P-loop; RNA !1biosynthesis; RNA replication FEATURE !$605-612 #region nucleotide-binding motif A (P-loop)\ !$668-673 #region nucleotide-binding motif B\ !$611 #binding_site ATP (Lys) #status predicted SUMMARY #length 1323 #molecular-weight 149592 #checksum 9897 SEQUENCE /// ENTRY RRWGNV #type complete TITLE genome polyprotein - narcissus mosaic virus ALTERNATE_NAMES RNA nucleotidyltransferase (RNA-directed); RNA replicase CONTAINS RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name narcissus mosaic virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 19-Jan-2001 ACCESSIONS JT0470 REFERENCE JT0470 !$#authors Zuidema, D.; Linthorst, H.J.M.; Huisman, M.J.; Asjes, C.J.; !1Bol, J.F. !$#journal J. Gen. Virol. (1989) 70:267-276 !$#title Nucleotide sequence of narcissus mosaic virus RNA. !$#cross-references MUID:89279206; PMID:2732689 !$#accession JT0470 !'##molecule_type genomic RNA !'##residues 1-1643 ##label ZUI !'##cross-references GB:D13747; GB:D00405; NID:g222107; PIDN:BAA02891.1; !1PID:g222108 CLASSIFICATION #superfamily eggplant mosaic virus RNA-directed RNA !1polymerase KEYWORDS ATP; nucleotide binding; nucleotidyltransferase; P-loop; RNA !1biosynthesis; RNA replication FEATURE !$868-875 #region nucleotide-binding motif A (P-loop)\ !$931-936 #region nucleotide-binding motif B\ !$874 #binding_site ATP (Lys) #status predicted SUMMARY #length 1643 #molecular-weight 186303 #checksum 8014 SEQUENCE /// ENTRY A46350 #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) - white clover mosaic virus (strain O) ALTERNATE_NAMES RNA nucleotidyltransferase (RNA-directed); RNA replicase ORGANISM #formal_name white clover mosaic virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 19-Jan-2001 ACCESSIONS A46350 REFERENCE A46350 !$#authors Beck, D.L.; Forster, R.L.S.; Bevan, M.W.; Boxen, K.A.; Lowe, !1S.C. !$#journal Virology (1990) 177:152-158 !$#title Infectious transcripts and nucleotide sequence of cloned !1cDNA of the potexvirus white clover mosaic virus. !$#cross-references MUID:90281578; PMID:2353451 !$#accession A46350 !'##status translation not shown !'##molecule_type genomic RNA !'##residues 1-1293 ##label BEC !'##cross-references GB:X16636 CLASSIFICATION #superfamily eggplant mosaic virus RNA-directed RNA !1polymerase KEYWORDS ATP; nucleotide binding; nucleotidyltransferase; P-loop; RNA !1biosynthesis; RNA replication FEATURE !$570-577 #region nucleotide-binding motif A (P-loop)\ !$633-638 #region nucleotide-binding motif B\ !$576 #binding_site ATP (Lys) #status predicted SUMMARY #length 1293 #molecular-weight 147442 #checksum 9579 SEQUENCE /// ENTRY WMWGPV #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) - potato virus X (strain X3) ALTERNATE_NAMES RNA nucleotidyltransferase (RNA-directed); RNA replicase ORGANISM #formal_name potato virus X, PVX #note host Nicotiana tabacum cv. Samsun (tobacco) DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 19-Jan-2001 ACCESSIONS JA0102 REFERENCE JA0102 !$#authors Huisman, M.J.; Linthorst, H.J.M.; Bol, J.F.; Cornelissen, !1B.J.C. !$#journal J. Gen. Virol. (1988) 69:1789-1798 !$#title The complete nucleotide sequence of potato virus X and its !1homologies at the amino acid level with various !1plus-stranded RNA viruses. !$#cross-references MUID:88299944; PMID:3404114 !$#accession JA0102 !'##molecule_type mRNA !'##residues 1-1456 ##label HUI !'##cross-references DDBJ:D00344; NID:g222441; PIDN:BAA00249.1; !1PID:g222442 CLASSIFICATION #superfamily eggplant mosaic virus RNA-directed RNA !1polymerase KEYWORDS ATP; nucleotide binding; nucleotidyltransferase; P-loop; RNA !1biosynthesis; RNA replication FEATURE !$735-742 #region nucleotide-binding motif A (P-loop)\ !$797-802 #region nucleotide-binding motif B\ !$741 #binding_site ATP (Lys) #status predicted SUMMARY #length 1456 #molecular-weight 165605 #checksum 6078 SEQUENCE /// ENTRY PN0093 #type complete TITLE genome polyprotein - potato virus M ALTERNATE_NAMES RNA nucleotidyltransferase (RNA-directed); RNA replicase CONTAINS RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name potato virus M DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 19-Jan-2001 ACCESSIONS PN0093; A54333; S21601 REFERENCE PN0093 !$#authors Zavriev, S.K.; Kanyka, K.V.; Levay, K.E. !$#journal Mol. Biol. (Mosk.) (1991) 25:761-769 !$#title The complete nucleotide sequence of potato virus M genomic !1RNA. !$#cross-references MUID:92049299; PMID:1944258 !$#accession PN0093 !'##molecule_type genomic RNA !'##residues 1-1968 ##label ZAV !'##cross-references GB:X53062; NID:g61291; PIDN:CAA37232.1; PID:g61292 !'##note the authors translated the codons GAA for residues 79 and 288 !1as Ile, GTG for residue 529 as Phe, CAC for residues 548 and !1630 as Asn, AGA for residue 646 as Pro, CCA for residue 1251 !1as Val, and ATG for residues 799, 1261, and 1366 as Asn REFERENCE A54333 !$#authors Zavriev, S.K.; Kanyuka, K.V.; Levay, K.E. !$#journal J. Gen. Virol. (1991) 72:9-14 !$#title The genome organization of potato virus M RNA. !$#cross-references MUID:91116326; PMID:1990070 !$#accession A54333 !'##molecule_type genomic RNA !'##residues 1-1968 ##label ZA2 !'##cross-references EMBL:X53062; NID:g61291; PIDN:CAA37232.1; !1PID:g61292 !'##experimental_source strain Russian !'##note authors translated the codon GAA for residue 79 as Ile, GAA for !1residue 288 as Ile, CCG for residue 356 as Arg, GTG for !1residue 529 as Phe, CAC for residue 548 as Asn, CAC for !1residue 630 as Asn, CCC for residue 645 as Arg, AGA for !1residue 646 as Pro, and ATG for residue 779 as Asn !'##note authors translated the codon CGA for residue 882 as Pro, CCA !1for residue 1251 as Val, ATG for residue 1261 as Asn, ATG !1for residue 1366 as Asn, TTT for residue 1380 as Glu, CAC !1for residue 1532 as Asn, CCC for residue 1578 as Arg, CGG !1for residue 1635 as Pro, and CCC for residue 1710 as Arg REFERENCE S21601 !$#authors Zavriev, S.K. !$#submission submitted to the EMBL Data Library, May 1990 !$#accession S21601 !'##status preliminary !'##molecule_type genomic RNA !'##residues 1-37,'N',39-45,47-1968 ##label ZA3 !'##cross-references EMBL:Y53062 !'##experimental_source Russian wild type CLASSIFICATION #superfamily eggplant mosaic virus RNA-directed RNA !1polymerase KEYWORDS ATP; nucleotide binding; nucleotidyltransferase; P-loop; RNA !1biosynthesis; RNA replication FEATURE !$1166-1173 #region nucleotide-binding motif A (P-loop)\ !$1241-1246 #region nucleotide-binding motif B\ !$1172 #binding_site ATP (Lys) #status predicted SUMMARY #length 1968 #molecular-weight 223384 #checksum 4558 SEQUENCE /// ENTRY A45353 #type complete TITLE genome polyprotein - apple chlorotic leaf spot virus (strain P863) ALTERNATE_NAMES RNA nucleotidyltransferase (RNA-directed); RNA replicase CONTAINS RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name apple chlorotic leaf spot virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 19-Jan-2001 ACCESSIONS A45353 REFERENCE A45353 !$#authors German, S.; Candresse, T.; Lanneau, M.; Huet, J.C.; !1Pernollet, J.C.; Dunez, J. !$#journal Virology (1990) 179:104-112 !$#title Nucleotide sequence and genomic organization of apple !1chlorotic leaf spot closterovirus. !$#cross-references MUID:91021011; PMID:2219716 !$#accession A45353 !'##molecule_type genomic RNA !'##residues 1-1884 ##label GER !'##cross-references GB:M58152; NID:g210293; PIDN:AAA42587.1; !1PID:g210294 CLASSIFICATION #superfamily eggplant mosaic virus RNA-directed RNA !1polymerase KEYWORDS ATP; nucleotide binding; nucleotidyltransferase; P-loop; RNA !1biosynthesis; RNA replication FEATURE !$1059-1066 #region nucleotide-binding motif A (P-loop)\ !$1122-1127 #region nucleotide-binding motif B\ !$1065 #binding_site ATP (Lys) #status predicted SUMMARY #length 1884 #molecular-weight 216560 #checksum 8526 SEQUENCE /// ENTRY JQ1734 #type complete TITLE genome polyprotein - shallot virus X ALTERNATE_NAMES RNA nucleotidyltransferase (RNA-directed); RNA replicase CONTAINS RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name shallot virus X DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 19-Jan-2001 ACCESSIONS JQ1734 REFERENCE JQ1734 !$#authors Kanyuka, K.V.; Vishnichenko, V.K.; Levay, K.E.; Kondrikov, !1D.Y.; Ryabov, E.V.; Zavriev, S.K. !$#journal J. Gen. Virol. (1992) 73:2553-2560 !$#title Nucleotide sequence of shallot virus X RNA reveals a !15'-proximal cistron closely related to those of potexviruses !1and a unique arrangement of the 3'-proximal cistrons. !$#cross-references MUID:93019008; PMID:1339468 !$#accession JQ1734 !'##molecule_type genomic RNA !'##residues 1-1718 ##label KAN !'##cross-references GB:M97264; NID:g295078; PIDN:AAA47787.1; !1PID:g295079 CLASSIFICATION #superfamily eggplant mosaic virus RNA-directed RNA !1polymerase KEYWORDS ATP; nucleotide binding; nucleotidyltransferase; P-loop; RNA !1biosynthesis; RNA replication FEATURE !$915-922 #region nucleotide-binding motif A (P-loop)\ !$978-983 #region nucleotide-binding motif B\ !$921 #binding_site ATP (Lys) #status predicted SUMMARY #length 1718 #molecular-weight 194529 #checksum 6046 SEQUENCE /// ENTRY A44059 #type complete TITLE genome polyprotein - apple stem grooving virus (strain P-209) ALTERNATE_NAMES RNA nucleotidyltransferase (RNA-directed); RNA replicase CONTAINS RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name apple stem grooving virus, ASGV DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 19-Jan-2001 ACCESSIONS A44059 REFERENCE A44059 !$#authors Yoshikawa, N.; Sasaki, E.; Kato, M.; Takahashi, T. !$#journal Virology (1992) 191:98-105 !$#title The nucleotide sequence of apple stem grooving capillovirus !1genome. !$#cross-references MUID:93033164; PMID:1413530 !$#accession A44059 !'##molecule_type genomic RNA !'##residues 1-2105 ##label YOS !'##cross-references GB:D14995; NID:g303496; PIDN:BAA03639.1; !1PID:g285608 CLASSIFICATION #superfamily eggplant mosaic virus RNA-directed RNA !1polymerase KEYWORDS ATP; nucleotide binding; nucleotidyltransferase; P-loop; RNA !1biosynthesis; RNA replication FEATURE !$781-788 #region nucleotide-binding motif A (P-loop)\ !$843-848 #region nucleotide-binding motif B\ !$787 #binding_site ATP (Lys) #status predicted SUMMARY #length 2105 #molecular-weight 241239 #checksum 951 SEQUENCE /// ENTRY RRVQBM #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) 38.8K chain - barley yellow dwarf virus (strain MAV-PS1) ALTERNATE_NAMES viral replicase ORGANISM #formal_name barley yellow dwarf virus, BYDV DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jun-2000 ACCESSIONS JQ1409 REFERENCE JQ1409 !$#authors Ueng, P.P.; Vincent, J.R.; Kawata, E.E.; Lei, C.H.; Lister, !1R.M.; Larkins, B.A. !$#journal J. Gen. Virol. (1992) 73:487-492 !$#title Nucleotide sequence analysis of the genomes of the MAV-PS1 !1and P-PAV isolates of barley yellow dwarf virus. !$#cross-references MUID:92166764; PMID:1538199 !$#accession JQ1409 !'##molecule_type genomic RNA !'##residues 1-339 ##label UEN !'##cross-references GB:D11028; DDBJ:D01213; NID:g221084; !1PIDN:BAA01779.1; PID:g221085 CLASSIFICATION #superfamily barley yellow dwarf virus RNA-directed RNA !1polymerase 38.8K chain KEYWORDS nucleotidyltransferase SUMMARY #length 339 #molecular-weight 38811 #checksum 8732 SEQUENCE /// ENTRY RRVQCM #type complete TITLE RNA-directed RNA polymerase (EC 2.7.7.48) 38.8K chain - barley yellow dwarf virus (strain P-PAV) ALTERNATE_NAMES viral replicase ORGANISM #formal_name barley yellow dwarf virus, BYDV DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Aug-2000 ACCESSIONS JQ1415; S00946 REFERENCE JQ1409 !$#authors Ueng, P.P.; Vincent, J.R.; Kawata, E.E.; Lei, C.H.; Lister, !1R.M.; Larkins, B.A. !$#journal J. Gen. Virol. (1992) 73:487-492 !$#title Nucleotide sequence analysis of the genomes of the MAV-PS1 !1and P-PAV isolates of barley yellow dwarf virus. !$#cross-references MUID:92166764; PMID:1538199 !$#accession JQ1415 !'##molecule_type genomic RNA !'##residues 1-339 ##label UEN !'##cross-references GB:D11032; DDBJ:D01214; NID:g221098; !1PIDN:BAA01785.1; PID:g221099 !'##experimental_source strain P-PAV REFERENCE S00946 !$#authors Miller, W.A.; Waterhouse, P.M.; Gerlach, W.L. !$#journal Nucleic Acids Res. (1988) 16:6097-6111 !$#title Sequence and organization of barley yellow dwarf virus !1genomic RNA. !$#cross-references MUID:88289355; PMID:3399386 !$#accession S00946 !'##molecule_type genomic RNA !'##residues 1-94,'S',96-126,'V',128-133,'R',135-222,'K',224-263,'A', !1265-329,'RM',332-339 ##label MIL !'##cross-references EMBL:X07653; NID:g58798 !'##experimental_source strain Australian isolate, PAV serotype !'##note the sequence is revised in GenBank entry BYDVPAV, release 117, !1(PIDN:CAA30498.1) COMMENT For an alternative 'transframe' form, see (PIR:A59303). CLASSIFICATION #superfamily barley yellow dwarf virus RNA-directed RNA !1polymerase 38.8K chain KEYWORDS nucleotidyltransferase SUMMARY #length 339 #molecular-weight 38660 #checksum 9023 SEQUENCE /// ENTRY RREC #type complete TITLE RNA-directed DNA polymerase (EC 2.7.7.49), msDNA specific - Escherichia coli retron Ec86 ALTERNATE_NAMES DNA nucleotidyltransferase (RNA-directed); reverse transcriptase; revertase ORGANISM #formal_name Escherichia coli retron Ec86 DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 11-Jun-1999 ACCESSIONS A31498; S16653 REFERENCE A31498 !$#authors Lim, D.; Maas, W.K. !$#journal Cell (1989) 56:891-904 !$#title Reverse transcriptase-dependent synthesis of a covalently !1linked, branched DNA-RNA compound in E. coli B. !$#cross-references MUID:89168429; PMID:2466573 !$#accession A31498 !'##molecule_type mRNA !'##residues 1-320 ##label LIM !'##cross-references GB:M24408; NID:g341167; PIDN:AAA61471.1; !1PID:g598116 !'##experimental_source E. coli strain B REFERENCE S16652 !$#authors Lim, D. !$#journal Mol. Microbiol. (1991) 5:1863-1872 !$#title Structure of two retrons of Escherichia coli and their !1common chromosomal insertion site. !$#cross-references MUID:92114764; PMID:1722556 !$#accession S16653 !'##molecule_type mRNA !'##residues 1-320 ##label LI2 !'##cross-references EMBL:X60206 !'##experimental_source E. coli strain B GENETICS !$#note insertion site is equivalent to 19 min of E. coli K12 !1genetic map CLASSIFICATION #superfamily reverse transcriptase KEYWORDS nucleotidyltransferase SUMMARY #length 320 #molecular-weight 36423 #checksum 692 SEQUENCE /// ENTRY S28006 #type complete TITLE RNA-directed DNA polymerase (EC 2.7.7.49), msDNA specific - Escherichia coli retron Ec79 ALTERNATE_NAMES DNA nucleotidyltransferase (RNA-directed); reverse transcriptase; revertase ORGANISM #formal_name Escherichia coli retron Ec79 DATE 17-Apr-1993 #sequence_revision 15-Oct-1996 #text_change 11-Jun-1999 ACCESSIONS S28006; S22963 REFERENCE S28005 !$#authors Lim, D. !$#journal Mol. Microbiol. (1992) 6:3531-3542 !$#title Structure and biosynthesis of unbranched multicopy !1single-stranded DNA by reverse transcriptase in a clinical !1Escherichia coli isolate. !$#cross-references MUID:93116591; PMID:1282191 !$#accession S28006 !'##molecule_type DNA !'##residues 1-312 ##label LIM !'##cross-references EMBL:Z12832; NID:g42499; PIDN:CAA78293.1; !1PID:g42501 !'##experimental_source E. coli strain 161 GENETICS !$#note insertion site is equivalent to 6 min of E. coli K12 genetic !1map CLASSIFICATION #superfamily reverse transcriptase KEYWORDS nucleotidyltransferase SUMMARY #length 312 #molecular-weight 35734 #checksum 2668 SEQUENCE /// ENTRY S19248 #type complete TITLE RNA-directed DNA polymerase (EC 2.7.7.49), msDNA specific - Escherichia coli retron Ec107 ALTERNATE_NAMES DNA nucleotidyltransferase (RNA-directed); reverse transcriptase; revertase ORGANISM #formal_name Escherichia coli retron Ec107 DATE 20-Feb-1995 #sequence_revision 15-Oct-1996 #text_change 11-Jun-1999 ACCESSIONS S19248 REFERENCE S19248 !$#authors Herzer, P.J.; Inouye, S.; Inouye, M. !$#journal Mol. Microbiol. (1992) 6:345-354 !$#title Retron Ec107 is inserted into the Escherichia coli genome by !1replacing a palindromic 34bp intergenic sequence. !$#cross-references MUID:92204001; PMID:1372675 !$#accession S19248 !'##status preliminary !'##molecule_type DNA !'##residues 1-319 ##label HER !'##cross-references EMBL:X62583; NID:g42774; PIDN:CAA44468.1; !1PID:g42775 !'##experimental_source E. coli wild strain GENETICS !$#note insertion site is 82 min of E. coli K12 genetic map CLASSIFICATION #superfamily reverse transcriptase KEYWORDS nucleotidyltransferase SUMMARY #length 319 #molecular-weight 36363 #checksum 2019 SEQUENCE /// ENTRY RRYC65 #type complete TITLE RNA-directed DNA polymerase (EC 2.7.7.49), msDNA specific - Myxococcus xanthus retron Mx65 ALTERNATE_NAMES DNA nucleotidyltransferase (RNA-directed); reverse transcriptase; revertase ORGANISM #formal_name Myxococcus xanthus retron Mx65 DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 11-Jun-1999 ACCESSIONS A34864 REFERENCE A34864 !$#authors Inouye, S.; Herzer, P.J.; Inouye, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:942-945 !$#title Two independent retrons with highly diverse reverse !1transcriptases in Myxococcus xanthus. !$#cross-references MUID:90138993; PMID:1689062 !$#accession A34864 !'##molecule_type mRNA !'##residues 1-427 ##label INO !'##cross-references GB:M30609; NID:g150121; PIDN:AAA88323.1; !1PID:g150122 CLASSIFICATION #superfamily reverse transcriptase KEYWORDS nucleotidyltransferase SUMMARY #length 427 #molecular-weight 48024 #checksum 1938 SEQUENCE /// ENTRY RRYC62 #type complete TITLE RNA-directed DNA polymerase (EC 2.7.7.49), msDNA specific - Myxococcus xanthus retron Mx162 ALTERNATE_NAMES DNA nucleotidyltransferase (RNA-directed); reverse transcriptase; revertase ORGANISM #formal_name Myxococcus xanthus retron Mx162 DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 11-Jun-1999 ACCESSIONS A31878 REFERENCE A31878 !$#authors Inouye, S.; Hsu, M.Y.; Eagle, S.; Inouye, M. !$#journal Cell (1989) 56:709-717 !$#title Reverse transcriptase associated with the biosynthesis of !1the branched RNA-linked msDNA in Myxococcus xanthus. !$#cross-references MUID:89136017; PMID:2465092 !$#accession A31878 !'##molecule_type mRNA !'##residues 1-485 ##label INO !'##cross-references GB:M24392; NID:g150123; PIDN:AAA25405.1; !1PID:g150124 CLASSIFICATION #superfamily reverse transcriptase KEYWORDS nucleotidyltransferase SUMMARY #length 485 #molecular-weight 53017 #checksum 1176 SEQUENCE /// ENTRY S16654 #type complete TITLE RNA-directed DNA polymerase (EC 2.7.7.49), msDNA specific - Escherichia coli retron Ec67 ALTERNATE_NAMES DNA nucleotidyltransferase (RNA-directed); reverse transcriptase; revertase ORGANISM #formal_name Escherichia coli retron Ec67 DATE 20-Feb-1995 #sequence_revision 15-Oct-1996 #text_change 11-Jun-1999 ACCESSIONS S16654; JQ0854; I59532 REFERENCE S16652 !$#authors Lim, D. !$#journal Mol. Microbiol. (1991) 5:1863-1872 !$#title Structure of two retrons of Escherichia coli and their !1common chromosomal insertion site. !$#cross-references MUID:92114764; PMID:1722556 !$#accession S16654 !'##status preliminary !'##molecule_type DNA !'##residues 1-646 ##label LIM !'##cross-references EMBL:X60207 !'##experimental_source E. coli isolate 317 from Brazil REFERENCE JQ0851 !$#authors Hsu, M.Y.; Inouye, M.; Inouye, S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:9454-9458 !$#title Retron for the 67-base multicopy single-stranded DNA from !1Escherichia coli: a potential transposable element encoding !1both reverse transcriptase and Dam methylase functions. !$#cross-references MUID:91067724; PMID:1701261 !$#accession JQ0854 !'##molecule_type DNA !'##residues 61-646 ##label HSU !'##cross-references GB:M55249; NID:g145143; PIDN:AAA23403.1; !1PID:g145157 !'##experimental_source E. coli strain Cl-1 REFERENCE I59532 !$#authors Lampson, B.C.; Sun, J.; Hsu, M.Y.; Vallejo-Ramirez, J.; !1Inouye, S.; Inouye, M. !$#journal Science (1989) 243:1033-1038 !$#title Reverse transcriptase in a clinical strain of Escherichia !1coli: production of branched RNA-linked msDNA. !$#cross-references MUID:89162029; PMID:2466332 !$#accession I59532 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 61-106,'R',108-211,'R',213-270,'R',272-320,'R',322-400,'D', !1402-432,'R',434-646 ##label RES !'##cross-references GB:M24363; NID:g598114; PIDN:AAA56874.1; !1PID:g598115 GENETICS !$#note insertion site is equivalent to 19 min of E. coli K12 !1genetic map CLASSIFICATION #superfamily retron Ec67 reverse transcriptase KEYWORDS nucleotidyltransferase SUMMARY #length 646 #molecular-weight 73705 #checksum 7195 SEQUENCE /// ENTRY RMXRR3 #type complete TITLE mRNA guanylyltransferase (EC 2.7.7.50) - reovirus type 3 ALTERNATE_NAMES lambda 2 protein; mRNA capping enzyme ORGANISM #formal_name reovirus type 3 #note host Homo sapiens (man) DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 19-Apr-1996 ACCESSIONS A28471 REFERENCE A28471 !$#authors Seliger, L.S.; Zheng, K.; Shatkin, A.J. !$#journal J. Biol. Chem. (1987) 262:16289-16293 !$#title Complete nucleotide sequence of reovirus L2 gene and deduced !1amino acid sequence of viral mRNA guanylyltransferase. !$#cross-references MUID:88058999; PMID:2824487 !$#accession A28471 !'##molecule_type DNA !'##residues 1-1289 ##label SEL GENETICS !$#map_position segment L2 CLASSIFICATION #superfamily reovirus mRNA guanylyltransferase KEYWORDS core protein; mRNA capping; nucleotidyltransferase; !1transcription SUMMARY #length 1289 #molecular-weight 143975 #checksum 6282 SEQUENCE /// ENTRY XXBYP1 #type complete TITLE ATP adenylyltransferase (EC 2.7.7.53) I - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES diadenosinetetraphosphate alpha-beta-phosphorylase I; protein YCL050c CONTAINS sulfate adenylyltransferase (ADP) (EC 2.7.7.5) ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1991 #sequence_revision 30-Jun-1993 #text_change 16-Jun-2000 ACCESSIONS S12946; S17970; S19380; S07847; A37535; JQ0793 REFERENCE JQ0793 !$#authors Kaushal, V.; Avila, D.M.; Hardies, S.C.; Barnes, L.D. !$#journal Gene (1990) 95:79-84 !$#title Sequencing and enhanced expression of the gene encoding !1diadenosine 5',5'''-P(1), P(4)-tetraphosphate (Ap(4)A) !1phosphorylase in Saccharomyces cerevisiae. !$#cross-references MUID:91071609; PMID:2174812 !$#accession S12946 !'##molecule_type DNA !'##residues 1-321 ##label KAU !'##cross-references GB:M35204; NID:g171425; PIDN:AAA34581.1; !1PID:g171426 !$#accession S17970 !'##molecule_type protein !'##residues 49-78,'W',80-84;281-321 ##label KAU2 REFERENCE S19380 !$#authors Fuller, L.J.; Kelly, A.; Lewis, C.; McKee, R.A.; Pearson, !1B.M. !$#submission submitted to the Protein Sequence Database, March 1992 !$#accession S19380 !'##molecule_type DNA !'##residues 1-321 ##label FUL !'##cross-references EMBL:X59720; NID:g1907116; PIDN:CAA42394.1; !1PID:g5311; GSPDB:GN00003; MIPS:YCL050c REFERENCE S07847 !$#authors Plateau, P.; Fromant, M.; Schmitter, J.M.; Buhler, J.M.; !1Blanquet, S. !$#journal J. Bacteriol. (1989) 171:6437-6445 !$#title Isolation, characterization, and inactivation of the APA1 !1gene encoding yeast diadenosine 5',5'''-P(1),P !1(4)-tetraphosphate phosphorylase. !$#cross-references MUID:90078083; PMID:2556364 !$#accession S07847 !'##molecule_type DNA !'##residues 1-99,'E',101-321 ##label PLA !'##cross-references GB:M31791; NID:g171063; PIDN:AAA34427.1; !1PID:g171064 !$#accession A37535 !'##molecule_type protein !'##residues 15-33;39-99,'E',101-260;263-321 ##label PLA2 GENETICS !$#gene SGD:APA1; DTP1; MIPS:YCL050c !'##cross-references SGD:S0000555; MIPS:YCL050c !$#map_position 3L CLASSIFICATION #superfamily ATP adenylyltransferase KEYWORDS acetylated amino end; blocked amino end; !1nucleotidyltransferase FEATURE !$2-321 #product ATP adenylyltransferase I #status predicted !8#label MAT\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status predicted SUMMARY #length 321 #molecular-weight 36420 #checksum 1699 SEQUENCE /// ENTRY XNECPG #type complete TITLE CDPdiacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase (EC 2.7.8.5) - Escherichia coli (strain K-12) ALTERNATE_NAMES glycerophosphate phosphatidyltransferase; phosphatidylglycerophosphate synthase ORGANISM #formal_name Escherichia coli DATE 30-Sep-1988 #sequence_revision 31-Oct-1997 #text_change 03-Jun-2002 ACCESSIONS E64954; A25663 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64954 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-182 ##label BLAT !'##cross-references GB:AE000284; GB:U00096; NID:g1788214; !1PIDN:AAC74979.1; PID:g1788220; UWGP:b1912 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A25663 !$#authors Gopalakrishnan, A.S.; Chen, Y.C.; Temkin, M.; Dowhan, W. !$#journal J. Biol. Chem. (1986) 261:1329-1338 !$#title Structure and expression of the gene locus encoding the !1phosphatidylglycerophosphate synthase of Escherichia coli. !$#cross-references MUID:86111778; PMID:3003065 !$#accession A25663 !'##molecule_type DNA !'##residues 1-176,'QIC',180,'ISDRFGVIFSKRSKVVKNIVDSSRQVSRMQRIERRH' !1##label GOP GENETICS !$#gene pgsA !$#map_position 42 min FUNCTION !$#description catalyzes the committed step to the synthesis of acidic !1phospholipids; catalyzes the reversible reaction of !1CDP-diacylglycerol and glycerol-3-phosphate to CMP and !1L-1-phosphatidylglycerol-phosphate !$#pathway phospholipid biosynthesis CLASSIFICATION #superfamily CDPdiacylglycerol-glycerol-3-phosphate !13-phosphatidyltransferase KEYWORDS inner membrane; phospholipid biosynthesis; transmembrane !1protein; transferase FEATURE !$8-24 #domain transmembrane #status predicted #label TM1\ !$28-44 #domain transmembrane #status predicted #label TM2\ !$66-82 #domain transmembrane #status predicted #label TM3\ !$153-169 #domain transmembrane #status predicted #label TM4 SUMMARY #length 182 #molecular-weight 20700 #checksum 4009 SEQUENCE /// ENTRY A27409 #type complete TITLE CDP diacylglycerol-inositol 3-phosphatidyltransferase (EC 2.7.8.11) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES CDP diacylglycerol-inositol 3-phosphatidyltransferase; protein P8283.5; protein YPR113w ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS A27409; S59778 REFERENCE A27409 !$#authors Nikawa, J.; Kodaki, T.; Yamashita, S. !$#journal J. Biol. Chem. (1987) 262:4876-4881 !$#title Primary structure and disruption of the phosphatidylinositol !1synthase gene of Saccharomyces cerevisiae. !$#cross-references MUID:87165905; PMID:3031032 !$#accession A27409 !'##molecule_type DNA !'##residues 1-220 ##label NIK !'##cross-references EMBL:J02697; NID:g172172; PIDN:AAA34876.1; !1PID:g172173 REFERENCE S59764 !$#authors Nelson, J. !$#submission submitted to the EMBL Data Library, July 1995 !$#description The sequence of S. cerevisiae cosmid 8283. !$#accession S59778 !'##molecule_type DNA !'##residues 1-220 ##label NEL !'##cross-references EMBL:U32445; NID:g914969; PIDN:AAB68083.1; !1PID:g914984; GSPDB:GN00016; MIPS:YPR113w GENETICS !$#gene SGD:PIS1; MIPS:YPR113w !'##cross-references SGD:S0006317; MIPS:YPR113w !$#map_position 16R CLASSIFICATION #superfamily CDPdiacylglycerol-inositol !13-phosphatidyltransferase KEYWORDS mitochondrion; transferase SUMMARY #length 220 #molecular-weight 24823 #checksum 3589 SEQUENCE /// ENTRY S08395 #type complete TITLE phospho-N-acetylmuramoyl-pentapeptide-transferase (EC 2.7.8.13) mraY - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS S08395; S40597; G64730 REFERENCE S08395 !$#authors Ikeda, M.; Wachi, M.; Ishino, F.; Matsuhashi, M. !$#journal Nucleic Acids Res. (1990) 18:1058 !$#title Nucleotide sequence involving murD and an open reading frame !1ORF-Y spacing murF and ftsW in Escherichia coli. !$#cross-references MUID:90192099; PMID:2179861 !$#accession S08395 !'##molecule_type DNA !'##residues 1-360 ##label IKE !'##cross-references EMBL:X51584; NID:g42058; PIDN:CAA35932.1; !1PID:g42059 REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40597 !'##status preliminary !'##molecule_type DNA !'##residues 1-360 ##label YUR !'##cross-references EMBL:D10483; NID:g216434; PIDN:BAA01352.1; !1PID:g216501 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64730 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-360 ##label BLAT !'##cross-references GB:AE000118; GB:U00096; NID:g1786262; !1PIDN:AAC73198.1; PID:g1786275; UWGP:b0087 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene mraY !$#map_position 2 min FUNCTION !$#pathway peptidoglycan biosynthesis CLASSIFICATION #superfamily !1phospho-N-acetylmuramoyl-pentapeptide-transferase KEYWORDS cell division; peptidoglycan biosynthesis; transferase; !1transmembrane protein FEATURE !$22-38 #domain transmembrane #status predicted #label TM1\ !$73-89 #domain transmembrane #status predicted #label TM2\ !$98-114 #domain transmembrane #status predicted #label TM3\ !$135-151 #domain transmembrane #status predicted #label TM4\ !$172-188 #domain transmembrane #status predicted #label TM5\ !$200-216 #domain transmembrane #status predicted #label TM6\ !$239-255 #domain transmembrane #status predicted #label TM7\ !$268-284 #domain transmembrane #status predicted #label TM8\ !$289-305 #domain transmembrane #status predicted #label TM9\ !$338-354 #domain transmembrane #status predicted #label TM10 SUMMARY #length 360 #molecular-weight 39874 #checksum 5052 SEQUENCE /// ENTRY A64185 #type complete TITLE phospho-N-acetylmuramoyl-pentapeptide-transferase (EC 2.7.8.13) - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A64185 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession A64185 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-360 ##label TIGR !'##cross-references GB:U32793; GB:L42023; NID:g1574683; !1PIDN:AAC22790.1; PID:g1574690; TIGR:HI1135 GENETICS !$#gene mraY FUNCTION !$#pathway peptidoglycan biosynthesis CLASSIFICATION #superfamily !1phospho-N-acetylmuramoyl-pentapeptide-transferase KEYWORDS cell division; peptidoglycan biosynthesis; transferase; !1transmembrane protein FEATURE !$29-45 #domain transmembrane #status predicted #label TM1\ !$77-93 #domain transmembrane #status predicted #label TM2\ !$98-114 #domain transmembrane #status predicted #label TM3\ !$135-151 #domain transmembrane #status predicted #label TM4\ !$172-188 #domain transmembrane #status predicted #label TM5\ !$200-216 #domain transmembrane #status predicted #label TM6\ !$239-255 #domain transmembrane #status predicted #label TM7\ !$268-284 #domain transmembrane #status predicted #label TM8\ !$289-305 #domain transmembrane #status predicted #label TM9\ !$338-354 #domain transmembrane #status predicted #label TM10 SUMMARY #length 360 #molecular-weight 40315 #checksum 8703 SEQUENCE /// ENTRY E64581 #type complete TITLE phospho-N-acetylmuramoyl-pentapeptide-transferase (EC 2.7.8.13) - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS E64581 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession E64581 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-353 ##label TOM !'##cross-references GB:AE000564; GB:AE000511; NID:g2313602; !1PIDN:AAD07559.1; PID:g2313604; TIGR:HP0493 CLASSIFICATION #superfamily !1phospho-N-acetylmuramoyl-pentapeptide-transferase KEYWORDS transferase SUMMARY #length 353 #molecular-weight 39169 #checksum 2085 SEQUENCE /// ENTRY C47691 #type complete TITLE phospho-N-acetylmuramoyl-pentapeptide-transferase (EC 2.7.8.13) mraY - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS C47691; B69660; S23915 REFERENCE A47691 !$#authors Daniel, R.A.; Errington, J. !$#journal J. Gen. Microbiol. (1993) 139:361-370 !$#title DNA sequence of the murE-murD region of Bacillus subtilis !1168. !$#cross-references MUID:93171879; PMID:8436954 !$#accession C47691 !'##molecule_type DNA !'##residues 1-324 ##label DAN !'##cross-references EMBL:Z15056; NID:g40160; PIDN:CAA78768.1; !1PID:g40163 !'##experimental_source 168 !'##note sequence extracted from NCBI backbone (NCBIN:125659, !1NCBIP:125663) REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69660 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-324 ##label KUN !'##cross-references GB:Z99111; GB:AL009126; NID:g2633699; !1PIDN:CAB13392.1; PID:g2633890 !'##experimental_source strain 168 GENETICS !$#gene mraY !$#map_position 133 (degrees) CLASSIFICATION #superfamily !1phospho-N-acetylmuramoyl-pentapeptide-transferase KEYWORDS peptidoglycan biosynthesis; transferase SUMMARY #length 324 #molecular-weight 35589 #checksum 3535 SEQUENCE /// ENTRY S77076 #type complete TITLE phospho-N-acetylmuramoyl-pentapeptide-transferase (EC 2.7.8.13) - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein sll0657 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S77076 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S77076 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-365 ##label KAN !'##cross-references EMBL:D64005; GB:AB001339; NID:g1001779; !1PIDN:BAA10768.1; PID:g1006612 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene mraY CLASSIFICATION #superfamily !1phospho-N-acetylmuramoyl-pentapeptide-transferase KEYWORDS transferase SUMMARY #length 365 #molecular-weight 38575 #checksum 9152 SEQUENCE /// ENTRY C69198 #type complete TITLE phospho-N-acetylmuramoyl-pentapeptide-transferase - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C69198 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession C69198 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-351 ##label MTH !'##cross-references GB:AE000852; GB:AE000666; NID:g2621812; !1PIDN:AAB85239.1; PID:g2621823 !'##experimental_source strain Delta H GENETICS !$#gene MTH735 CLASSIFICATION #superfamily !1phospho-N-acetylmuramoyl-pentapeptide-transferase SUMMARY #length 351 #molecular-weight 37003 #checksum 1700 SEQUENCE /// ENTRY H65036 #type complete TITLE CDPdiacylglycerol-serine O-phosphatidyltransferase (EC 2.7.8.8) - Escherichia coli (strain K-12) ALTERNATE_NAMES phosphatidylserine synthase ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS H65036; JH0368; A40406 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65036 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-452 ##label BLAT !'##cross-references GB:AE000345; GB:U00096; NID:g1788939; !1PIDN:AAC75638.1; PID:g1788940; UWGP:b2585 !'##experimental_source strain K-12, substrain MG1655 REFERENCE JH0368 !$#authors DeChavigny, A.; Heacock, P.N.; Dowhan, W. !$#journal J. Biol. Chem. (1991) 266:5323-5332 !$#title Sequence and inactivation of the pss gene of Escherichia !1coli: phosphatidylethanolamine may not be essential for cell !1viability. !$#cross-references MUID:91161632; PMID:2002065 !$#accession JH0368 !'##molecule_type DNA !'##residues 2-32,'R',34-78,'DD',80-165,'NIA',169-287,'FV',290-309,'S', !1311-452 ##label DEC !'##cross-references GB:M58699; NID:g147388; PIDN:AAA97504.1; !1PID:g147389 REFERENCE A40406 !$#authors DeChavigny, A.; Heacock, P.N.; Dowhan, W. !$#journal J. Biol. Chem. (1991) 266:10710 !$#cross-references MUID:91244856; PMID:2037609 !$#contents erratum !$#accession A40406 !'##status preliminary !'##molecule_type DNA !'##residues 2-32,'R',34-78,'DD',80-165,'NIA',169-287,'FV',290-309,'S', !1311-452 ##label DE2 COMMENT The enzyme catalyzes the committed step to !1phosphatidylethanolamine biosynthesis. GENETICS !$#gene pssA; pss CLASSIFICATION #superfamily Escherichia coli CDPdiacylglycerol-serine !1O-phosphatidyltransferase KEYWORDS transferase FEATURE !$120-155 #region hydrophobic\ !$240-285 #region hydrophobic SUMMARY #length 452 #molecular-weight 52932 #checksum 2618 SEQUENCE /// ENTRY A55537 #type complete TITLE CDPdiacylglycerol-serine O-phosphatidyltransferase (EC 2.7.8.8) pssA [validated] - Bacillus subtilis ALTERNATE_NAMES phosphatidylserine synthase pssA ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS A55537; C69683 REFERENCE A55537 !$#authors Okada, M.; Matsuzaki, H.; Shibuya, I.; Matsumoto, K. !$#journal J. Bacteriol. (1994) 176:7456-7461 !$#title Cloning, sequencing, and expression in Escherichia coli of !1the Bacillus subtilis gene for phosphatidylserine synthase. !$#cross-references MUID:95095912; PMID:8002567 !$#accession A55537 !'##molecule_type DNA !'##residues 1-177 ##label OKA !'##cross-references EMBL:D38022; NID:g532270; PIDN:BAA07225.1; !1PID:g1065993 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69683 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-177 ##label KUN !'##cross-references GB:Z99105; GB:AL009126; NID:g2632457; !1PIDN:CAB12021.1; PID:g2632513 !'##experimental_source strain 168 GENETICS !$#gene pssA !$#start_codon GTG CLASSIFICATION #superfamily Bacillus subtilis CDPdiacylglycerol-serine !1O-phosphatidyltransferase; Bacillus subtilis !1CDPdiacylglycerol-serine O-phosphatidyltransferase homology KEYWORDS manganese; membrane protein; transferase FEATURE !$26-166 #domain Bacillus subtilis CDPdiacylglycerol-serine !8O-phosphatidyltransferase homology #label BSC SUMMARY #length 177 #molecular-weight 19613 #checksum 4465 SEQUENCE /// ENTRY S00080 #type complete TITLE CDPdiacylglycerol-serine O-phosphatidyltransferase (EC 2.7.8.8) CHO1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES phosphatidylserine synthase; protein YER026c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S00080; A41507; S50484 REFERENCE S00080 !$#authors Nikawa, J.I.; Tsukagoshi, Y.; Kodaki, T.; Yamashita, S. !$#journal Eur. J. Biochem. (1987) 167:7-12 !$#title Nucleotide sequence and characterization of the yeast PSS !1gene encoding phosphatidylserine synthase. !$#cross-references MUID:87304241; PMID:3040403 !$#accession S00080 !'##molecule_type DNA !'##residues 1-276 ##label NIK !'##cross-references EMBL:X05944; NID:g4247; PIDN:CAA29376.1; PID:g4248 REFERENCE A41507 !$#authors Kiyono, K.; Miura, K.; Kushima, Y.; Hikiji, T.; Fukushima, !1M.; Shibuya, I.; Ohta, A. !$#journal J. Biochem. (1987) 102:1089-1100 !$#title Primary structure and product characterization of the !1Saccharomyces cerevisiae CHO1 gene that encodes !1phosphatidylserine synthase. !$#cross-references MUID:88139260; PMID:2830250 !$#accession A41507 !'##molecule_type DNA !'##residues 1-276 ##label KIY !'##cross-references GB:D00171 REFERENCE S50433 !$#authors Dietrich, F.S. !$#submission submitted to the EMBL Data Library, December 1994 !$#description The sequence of S. cerevisiae cosmids 9537, 9581, 9495, !19867, and lambda clone 5898. !$#accession S50484 !'##molecule_type DNA !'##residues 1-276 ##label DIE !'##cross-references EMBL:U18778; NID:g603592; PIDN:AAB64559.1; !1PID:g603618; GSPDB:GN00005; MIPS:YER026c GENETICS !$#gene SGD:CHO1; PSS1; PSS; MIPS:YER026c !'##cross-references SGD:S0000828; MIPS:YER026c !$#map_position 5R CLASSIFICATION #superfamily Saccharomyces cerevisiae !1CDPdiacylglycerol-serine O-phosphatidyltransferase; Bacillus !1subtilis CDPdiacylglycerol-serine O-phosphatidyltransferase !1homology KEYWORDS glycoprotein; lipid metabolism; mitochondrion; phospholipid !1biosynthesis; transferase; transmembrane protein FEATURE !$111-247 #domain Bacillus subtilis CDPdiacylglycerol-serine !8O-phosphatidyltransferase homology #label BSC\ !$150-169 #domain transmembrane #status predicted #label TM1\ !$173-190 #domain transmembrane #status predicted #label TM2\ !$220-236 #domain transmembrane #status predicted #label TM3\ !$255-271 #domain transmembrane #status predicted #label TM4\ !$52,60,138,193 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 276 #molecular-weight 30804 #checksum 2064 SEQUENCE /// ENTRY KIZMPO #type complete TITLE pyruvate, phosphate dikinase (EC 2.7.9.1) precursor - maize ORGANISM #formal_name Zea mays #common_name maize DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Jun-2002 ACCESSIONS A29225; PQ0189; A35636; A28155 REFERENCE A29225 !$#authors Matsuoka, M.; Ozeki, Y.; Yamamoto, N.; Hirano, H.; !1Kano-Murakami, Y.; Tanaka, Y. !$#journal J. Biol. Chem. (1988) 263:11080-11083 !$#title Primary structure of maize pyruvate,orthophosphate dikinase !1as deduced from cDNA sequence. !$#cross-references MUID:88298745; PMID:2841317 !$#accession A29225 !'##molecule_type mRNA !'##residues 1-947 ##label MAT1 !'##cross-references GB:J03901 !'##note the sequence of residues 72-89 was confirmed by protein !1sequencing REFERENCE PQ0189 !$#authors Sheen, J. !$#journal Plant Cell (1991) 3:225-245 !$#title Molecular mechanisms underlying the differential expression !1of maize pyruvate, orthophosphate dikinase genes. !$#cross-references MUID:93005696; PMID:1668653 !$#accession PQ0189 !'##molecule_type DNA !'##residues 1,'T',3-154 ##label SHE !'##cross-references GB:S46965; NID:g257804; PIDN:AAB23730.1; !1PID:g257805 REFERENCE A35636 !$#authors Glackin, C.A.; Grula, J.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:3004-3008 !$#title Organ-specific transcripts of different size and abundance !1derive from the same pyruvate, orthophosphate dikinase gene !1in maize. !$#cross-references MUID:90222158; PMID:2158100 !$#accession A35636 !'##status preliminary !'##molecule_type DNA !'##residues 1-75 ##label GLA !'##cross-references GB:X14927; NID:g22449; PIDN:CAA33054.1; PID:g22450 !'##note the authors translated the codon ATC for residue 9 as Thr, GAC !1for residue 21 as Asn, GAC for residue 49 as Asn, and GAC !1for residue 66 as Asn REFERENCE A28155 !$#authors Roeske, C.A.; Kutny, R.M.; Budde, R.J.A.; Chollet, R. !$#journal J. Biol. Chem. (1988) 263:6683-6687 !$#title Sequence of the phosphothreonyl regulatory site peptide from !1inactive maize leaf pyruvate,orthophosphate dikinase. !$#cross-references MUID:88198234; PMID:2834385 !$#accession A28155 !'##molecule_type protein !'##residues 521-535 ##label ROE COMMENT This enzyme catalyzes the phosphorylation of orthophosphate !1and pyruvate using ATP with the formation of AMP, !1pyrophosphate, and phosphoenolpyruvate. GENETICS !$#gene C4ppdkZm1 !$#introns 75/3; 94/3 CLASSIFICATION #superfamily pyruvate,orthophosphate dikinase KEYWORDS chloroplast; homotetramer; phosphohistidine; phosphoprotein; !1transferase FEATURE !$1-71 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$72-947 #product pyruvate,orthophosphate dikinase #status !8experimental #label MAT\ !$527 #binding_site phosphate (Thr) (covalent) (by !8bifunctional regulatory protein) #status !8experimental\ !$529 #active_site His (phosphohistidine intermediate) !8#status predicted SUMMARY #length 947 #molecular-weight 102674 #checksum 6815 SEQUENCE /// ENTRY KIQAPO #type complete TITLE pyruvate, phosphate dikinase (EC 2.7.9.1) - Clostridium symbiosum ORGANISM #formal_name Clostridium symbiosum DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Jun-2002 ACCESSIONS A36231 REFERENCE A36231 !$#authors Pocalyko, D.J.; Carroll, L.J.; Martin, B.M.; Babbitt, P.C.; !1Dunaway-Mariano, D. !$#journal Biochemistry (1990) 29:10757-10765 !$#title Analysis of sequence homologies in plant and bacterial !1pyruvate phosphate dikinase, enzyme I of the bacterial !1phosphoenolpyruvate: sugar phosphotransferase system and !1other PEP-utilizing enzymes. Identification of potential !1catalytic and regulatory motifs. !$#cross-references MUID:91104996; PMID:2176881 !$#accession A36231 !'##molecule_type DNA !'##residues 1-840 ##label POC !'##cross-references GB:M60920; GB:J05295; NID:g143960; PIDN:AAA22917.1; !1PID:g143961 CLASSIFICATION #superfamily pyruvate,orthophosphate dikinase KEYWORDS homodimer; phosphoprotein; transferase FEATURE !$2-840 #product pyruvate,orthophosphate dikinase #status !8experimental #label MAT SUMMARY #length 840 #molecular-weight 93205 #checksum 2568 SEQUENCE /// ENTRY S55478 #type complete TITLE pyruvate, phosphate dikinase (EC 2.7.9.1) - common ice plant ORGANISM #formal_name Mesembryanthemum crystallinum #common_name common ice plant DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S55478; S49497 REFERENCE S55478 !$#authors Fisslthaler, B.; Meyer, G.; Schmitt, J.M. !$#submission submitted to the EMBL Data Library, October 1994 !$#accession S55478 !'##status preliminary !'##molecule_type DNA !'##residues 1-949 ##label FIS !'##cross-references EMBL:X82489; NID:g854264; PIDN:CAA57872.1; !1PID:g854265 REFERENCE S49497 !$#authors Fisslthaler, B.; Meyer, G.; Bohnert, H.J.; Schmitt, J.M. !$#submission submitted to the EMBL Data Library, March 1994 !$#description Age dependent induction of pyrurat-Pi-dikinase in the !1facultative CAM plant Mesembryanthemum crystallinum. !$#accession S49497 !'##molecule_type mRNA !'##residues 1-239,'V',241-581,'SY',584,'RESTT',590-949 ##label FIW !'##cross-references EMBL:X78347; NID:g559470; PIDN:CAA55143.1; !1PID:g559471 GENETICS !$#gene ppd !$#introns 78/3; 97/3; 175/3; 221/3; 276/1; 354/3; 397/3; 457/3; 503/3; !1558/3; 612/3; 642/3; 689/1; 748/2; 791/3; 834/3; 880/3; 906/ !13; 937/2 FUNCTION !$#description catalyzes the reversible phosphorylation of pyruvate and !1phosphate by ATP to phosphoenolpyruvate and diphosphate CLASSIFICATION #superfamily pyruvate,orthophosphate dikinase KEYWORDS phosphohistidine; phosphoprotein; transferase FEATURE !$532 #active_site His (phosphohistidine intermediate) !8#status predicted SUMMARY #length 949 #molecular-weight 103083 #checksum 8704 SEQUENCE /// ENTRY S53297 #type complete TITLE pyruvate, phosphate dikinase (EC 2.7.9.1) - Flaveria pringlei ORGANISM #formal_name Flaveria pringlei DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S53297 REFERENCE S53297 !$#authors Rosche, E.; Streubel, M.; Westhoff, P. !$#journal Plant Mol. Biol. (1994) 26:763-769 !$#title Primary structure of the photosynthetic pyruvate !1orthophosphate dikinase of the C(3) plant Flaveria pringlei !1and expression analysis of pyruvate orthophosphate dikinase !1sequences in C(3), C(3)-C(4) and C(4) Flaveria species. !$#cross-references MUID:95036056; PMID:7948930 !$#accession S53297 !'##status preliminary !'##molecule_type mRNA !'##residues 1-956 ##label ROS !'##cross-references EMBL:X75516; NID:g577775; PIDN:CAA53223.1; !1PID:g577776 GENETICS !$#gene pdk FUNCTION !$#description catalyzes the reversible phosphorylation of pyruvate and !1phosphate by ATP to phosphoenolpyruvate and diphosphate CLASSIFICATION #superfamily pyruvate,orthophosphate dikinase KEYWORDS phosphohistidine; phosphoprotein; transferase FEATURE !$538 #active_site His (phosphohistidine intermediate) !8#status predicted SUMMARY #length 956 #molecular-weight 104553 #checksum 3120 SEQUENCE /// ENTRY ROHU #type complete TITLE thiosulfate sulfurtransferase (EC 2.8.1.1) - human ALTERNATE_NAMES rhodanese; thiosulfate cyanide sulfurtransferase ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1992 #sequence_revision 18-Aug-1995 #text_change 11-Jun-1999 ACCESSIONS JH0461 REFERENCE JH0461 !$#authors Pallini, R.; Guazzi, G.C.; Cannella, C.; Cacace, M.G. !$#journal Biochem. Biophys. Res. Commun. (1991) 180:887-893 !$#title Cloning and sequence analysis of the human liver rhodanese: !1comparison with the bovine and chicken enzymes. !$#cross-references MUID:92062122; PMID:1953758 !$#accession JH0461 !'##molecule_type mRNA !'##residues 1-296 ##label PAL !'##cross-references GB:X59434; GB:S61764; NID:g432375; PIDN:CAA42060.1; !1PID:g432376 !'##experimental_source liver COMMENT A widely distibuted enzyme, it is found in the mitochondrial !1matrix in animal tissues. GENETICS !$#gene GDB:TST !'##cross-references GDB:134043; OMIM:180370 !$#map_position Ypter-Yp11.2 FUNCTION !$#description catalyzes the transfer of sulfur in thiosulfate and other !1compounds to cyanide ion to form thiocyanate ion !$#note physiologically it may function as a general sulfur !1transferase CLASSIFICATION #superfamily thiosulfate sulfurtransferase KEYWORDS mitochondrion; monomer; sulfoprotein; sulfurtransferase FEATURE !$2-296 #product thiosulfate sulfurtransferase #status !8predicted #label MAT\ !$247 #active_site Cys (sulfocysteine intermediate) #status !8predicted SUMMARY #length 296 #molecular-weight 32966 #checksum 1704 SEQUENCE /// ENTRY ROBO #type complete TITLE thiosulfate sulfurtransferase (EC 2.8.1.1) [validated] - bovine ALTERNATE_NAMES rhodanese; thiosulfate cyanide sulfurtransferase ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 24-Apr-1984 #sequence_revision 05-Aug-1994 #text_change 15-Sep-2000 ACCESSIONS A23704; A00727 REFERENCE A23704 !$#authors Miller, D.M.; Delgado, R.; Chirgwin, J.M.; Hardies, S.C.; !1Horowitz, P.M. !$#journal J. Biol. Chem. (1991) 266:4686-4691 !$#title Expression of cloned bovine adrenal rhodanese. !$#cross-references MUID:91161544; PMID:2002017 !$#accession A23704 !'##molecule_type mRNA !'##residues 1-297 ##label MIL !'##cross-references GB:M58561; NID:g163660; PIDN:AAA30753.1; !1PID:g163661 !'##experimental_source adrenal gland REFERENCE A92238 !$#authors Russell, J.; Weng, L.; Keim, P.S.; Heinrikson, R.L. !$#journal J. Biol. Chem. (1978) 253:8102-8108 !$#title The covalent structure of bovine liver rhodanese. Isolation !1and partial structural analysis of cyanogen bromide !1fragments and the complete sequence of the enzyme. !$#cross-references MUID:79048424; PMID:711737 !$#accession A00727 !'##molecule_type protein !'##residues 2-99,'N',101-214,'D',216-219,'N',221-294 ##label RUS !'##experimental_source liver !'##note Val-2 and His-3 are absent in some preparations of rhodanese, !1but these still exhibit complete enzyme activity REFERENCE A50334 !$#authors Hol, W.G.J.; Ploegman, J.H.; Kalk, K.H.; Drent, G. !$#submission submitted to the Brookhaven Protein Data Bank, November 1977 !$#cross-references PDB:1RHD !$#contents annotation; X-ray crystallography, 2.5 angstroms, residues !12-99,'N',101-214,'D',216-219,'N',221-294 REFERENCE A92852 !$#authors Ploegman, J.H.; Drent, G.; Kalk, K.H.; Hol, W.G.J. !$#journal J. Mol. Biol. (1978) 123:557-594 !$#title Structure of bovine liver rhodanese. I. Structure !1determination at 2.5 angstrom resolution and a comparison of !1the conformation and sequence of its two domains. !$#cross-references MUID:79007483; PMID:691057 !$#contents annotation; X-ray crystallography, 2.5 angstroms !$#note the structure consists of two domains of very similar !1conformation, suggesting a common evolutionary origin for !1both domains; however, the sequences of the two domains are !1very different REFERENCE A92239 !$#authors Weng, L.; Heinrikson, R.L.; Westley, J. !$#journal J. Biol. Chem. (1978) 253:8109-8119 !$#title Active site cysteinyl and arginyl residues of rhodanese. A !1novel formation of disulfide bonds in the active site !1promoted by phenylglyoxal. !$#cross-references MUID:79048425; PMID:711738 !$#contents annotation; active site REFERENCE A13902 !$#authors Ploegman, J.H.; Drent, G.; Kalk, K.H.; Hol, W.G.J.; !1Heinrikson, R.L.; Keim, P.; Weng, L.; Russell, J. !$#journal Nature (1978) 273:124-129 !$#title The covalent and tertiary structure of bovine liver !1rhodanese. !$#cross-references MUID:78156434; PMID:643076 !$#contents annotation; active site sulfocysteine COMMENT A widely distibuted enzyme, it is found in the mitochondria !1in animal tissues. COMMENT No disulfide bonds are present. FUNCTION !$#description catalyzes the transfer of sulfur in thiosulfate and other !1compounds to cyanide ion to form thiocyanate ion !$#note physiologically it may function as a general sulfur !1transferase CLASSIFICATION #superfamily thiosulfate sulfurtransferase KEYWORDS mitochondrion; monomer; sulfoprotein; sulfurtransferase FEATURE !$2-294 #product thiosulfate sulfurtransferase #status !8experimental #label MAT\ !$187,250 #binding_site substrate (Arg, Lys) #status predicted\ !$248 #active_site Cys (sulfocysteine intermediate) #status !8experimental SUMMARY #length 297 #molecular-weight 33296 #checksum 7633 SEQUENCE /// ENTRY A37209 #type complete TITLE thiosulfate sulfurtransferase (EC 2.8.1.1), hepatic - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A37209 REFERENCE A37209 !$#authors Kohanski, R.A.; Heinrikson, R.L. !$#journal J. Protein Chem. (1990) 9:369-377 !$#title Primary structure of avian hepatic rhodanese. !$#cross-references MUID:91113289; PMID:2275748 !$#accession A37209 !'##molecule_type protein !'##residues 1-289 ##label KOH CLASSIFICATION #superfamily thiosulfate sulfurtransferase KEYWORDS liver; mitochondrion; sulfoprotein; sulfurtransferase FEATURE !$244 #active_site Cys (sulfocysteine intermediate) #status !8predicted SUMMARY #length 289 #molecular-weight 32286 #checksum 8905 SEQUENCE /// ENTRY I38548 #type complete TITLE alcohol sulfotransferase (EC 2.8.2.2) - human ALTERNATE_NAMES dehydroepiandrosterone sulfotransferase (DHEA-ST); dehydroepiandrosterone-preferring sulphotransferase; hydroxysteroid sulfotransferase (HST) ORGANISM #formal_name Homo sapiens #common_name man DATE 06-Sep-1996 #sequence_revision 06-Sep-1996 #text_change 11-Jun-1999 ACCESSIONS I53037; I38548; I38549; JC1223; S28155; A58735; I37285; !1S52476 REFERENCE I53037 !$#authors Luu-The, V.; Dufort, I.; Paquet, N.; Reimnitz, G.; Labrie, !1F. !$#journal DNA Cell Biol. (1995) 14:511-518 !$#title Structural characterization and expression of the human !1dehydroepiandrosterone sulfotransferase gene. !$#cross-references MUID:95322029; PMID:7598806 !$#accession I53037 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-285 ##label LUU !'##cross-references GB:L36196; NID:g908766; PIDN:AAA75491.1; !1PID:g908768 REFERENCE I38548 !$#authors Otterness, D.M.; Wieben, E.D.; Wood, T.C.; Watson, R.W.G.; !1Madden, B.J.; McCormick, D.J.; Weinshilboum, R.M. !$#journal Mol. Pharmacol. (1992) 41:865-872 !$#title Human liver dehydroepiandrosterone sulfotransferase: !1Molecular cloning and expression of cDNA. !$#cross-references MUID:92269778; PMID:1588921 !$#accession I38548 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-285 ##label OTT1 !'##cross-references EMBL:U08024; NID:g468250; PIDN:AAA17749.1; !1PID:g468251 !$#accession I38549 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-285 ##label OTT2 !'##cross-references EMBL:U08025; NID:g468252; PIDN:AAA17750.1; !1PID:g468253 !'##note parts of this sequence were determined by protein sequencing; !1the amino end of the mature protein is blocked !'##note three electrophoretic forms were observed REFERENCE JC1223 !$#authors Kong, A.N.T.; Yang, L.; Ma, M.; Tao, D.; Bjornsson, T.D. !$#journal Biochem. Biophys. Res. Commun. (1992) 187:448-454 !$#title Molecular cloning of the alcohol/hydroxysteroid form (hSTa) !1of sulfotransferase from human liver. !$#cross-references MUID:92392364; PMID:1520333 !$#accession JC1223 !'##molecule_type mRNA !'##residues 1-158,'V',160-285 ##label KON !'##cross-references GB:S43859; NID:g255072 !'##experimental_source liver !'##note the authors translated the codon AGC for residue 222 as Thr REFERENCE S28155 !$#authors Comer, K.A.; Falany, J.L.; Falany, C.N. !$#journal Biochem. J. (1993) 289:233-240 !$#title Cloning and expression of human liver dehydroepiandrosterone !1sulphotransferase. !$#cross-references MUID:93143674; PMID:7678732 !$#accession S28155 !'##molecule_type mRNA !'##residues 1-89,'S',91-285 ##label COM !'##cross-references GB:X70222; GB:S53620; NID:g312804; PIDN:CAA49755.1; !1PID:g312805; GB:L20000; NID:g306701; PID:g306702 !'##note parts of this sequence were determined by protein sequencing; !1the amino end of the mature protein is blocked REFERENCE A58735 !$#authors Forbes, K.J.; Hagen, M.; Glatt, H.; Hume, R.; Coughtrie, !1M.W. !$#journal Mol. Cell. Endocrinol. (1995) 112:53-60 !$#title Human fetal adrenal hydroxysteroid sulphotransferase: cDNA !1cloning, stable expression in V79 cells and functional !1characterisation of the expressed enzyme. !$#cross-references MUID:96034512; PMID:7589785 !$#accession A58735 !'##molecule_type mRNA !'##residues 1-285 ##label FOR !'##cross-references GB:X84816; NID:g683577; PIDN:CAA59274.1; !1PID:g683578 !'##experimental_source fetal adrenal REFERENCE I37285 !$#authors Otterness, D.M.; Her, C.; Aksoy, S.; Kimura, S.; Wieben, !1E.D.; Weinshilboum, R.M. !$#journal DNA Cell Biol. (1995) 14:331-341 !$#title Human dehydroepiandrosterone sulfotransferase gene: !1molecular cloning and structural characterization. !$#cross-references MUID:95225980; PMID:7710689 !$#accession I37285 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-285 ##label RES !'##cross-references EMBL:U13061; NID:g806716; PIDN:AAC51353.1; !1PID:g806718 GENETICS !$#gene GDB:STD; HST !'##cross-references GDB:132655; OMIM:125263 !$#map_position 19q13.3-19q13.3 !$#introns 46/1; 115/3; 158/1; 189/3; 249/1 COMPLEX homodimer FUNCTION !$#description catalyzes formation of the sulfate esters of alcohols using !13'-phosphoadenosine-5'phosphosulfate and converting it to !1adenosine 3',5'-bisphosphate !$#pathway steroid metabolism; detoxification !$#note sulfates bile acids and steroids, in particular !1dehydroepiandrosterone, in the liver and adrenals CLASSIFICATION #superfamily alcohol sulfotransferase KEYWORDS acetylated amino end; detoxification; homodimer; steroid !1metabolism; sulfotransferase FEATURE !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status predicted SUMMARY #length 285 #molecular-weight 33780 #checksum 9372 SEQUENCE /// ENTRY RDECPA #type complete TITLE phosphoadenylyl-sulfate reductase (thioredoxin) (EC 1.8.4.8) - Escherichia coli (strain K-12) ALTERNATE_NAMES 3'-phosphoadenylylsulfate reductase, thioredoxin dependent; PAPS reductase; PAPS sulfotransferase CONTAINS 3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (EC 2.8.2.-) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 01-Mar-2002 ACCESSIONS S14221; S07486; D34354; F65057; A34134 REFERENCE S14220 !$#authors Krone, F.A.; Westphal, G.; Schwenn, J.D. !$#journal Mol. Gen. Genet. (1991) 225:314-319 !$#title Characterization of the gene cysH and of its product !1phospho-adenylylsulphate reductase from Escherichia coli. !$#cross-references MUID:91172132; PMID:2005873 !$#accession S14221 !'##molecule_type DNA !'##residues 1-244 ##label KRO !'##cross-references EMBL:Y07525; NID:g41197; PIDN:CAA68817.1; !1PID:g41198 REFERENCE A34134 !$#authors Krone, F.A.; Westphal, G.; Meyer, H.E.; Schwenn, J.D. !$#journal FEBS Lett. (1990) 260:6-9 !$#title PAPS-reductase of Escherichia coli. Correlating the !1N-terminal amino acid sequence with the DNA of gene cys H. !$#cross-references MUID:90127409; PMID:2404794 !$#accession S07486 !'##molecule_type protein !'##residues 2-4,7-18 ##label KRO2 REFERENCE A34354 !$#authors Ostrowski, J.; Wu, J.Y.; Rueger, D.C.; Miller, B.E.; Siegel, !1L.M.; Kredich, N.M. !$#journal J. Biol. Chem. (1989) 264:15726-15737 !$#title Characterization of the cysJIH regions of Salmonella !1typhimurium and Escherichia coli B. DNA sequences of cysI !1and cysH and a model for the siroheme-Fe-4S-4 active center !1of sulfite reductase hemoprotein based on amino acid !1homology with spinach nitrite reductase. !$#cross-references MUID:89359425; PMID:2670946 !$#accession D34354 !'##status preliminary !'##molecule_type DNA !'##residues 1-26,'Q',28-225,'S',227-244 ##label OST !'##cross-references GB:M23008; NID:g145679; PIDN:AAA23652.1; !1PID:g145682; GB:J05025; GB:J05057; GB:M27144 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65057 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-244 ##label BLAT !'##cross-references GB:AE000360; GB:U00096; NID:g2367157; !1PIDN:AAC75804.1; PID:g1789121; UWGP:b2762 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene cysH !$#map_position 59 min CLASSIFICATION #superfamily 3'-phosphoadenosine 5'-phosphosulfate reductase KEYWORDS cysteine biosynthesis; oxidoreductase; sulfotransferase FEATURE !$2-244 #product 3'-phosphoadenosine 5'-phosphosulfate !8sulfotransferase #status experimental #label MAT SUMMARY #length 244 #molecular-weight 27976 #checksum 3921 SEQUENCE /// ENTRY C34354 #type complete TITLE phosphoadenylyl-sulfate reductase (thioredoxin) (EC 1.8.4.8) - Salmonella typhimurium ALTERNATE_NAMES 3'-phosphoadenylylsulfate reductase, thioredoxin dependent; PAPS reductase; PAPS sulfotransferase CONTAINS 3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (EC 2.8.2.-) ORGANISM #formal_name Salmonella typhimurium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 24-Aug-2001 ACCESSIONS C34354 REFERENCE A34354 !$#authors Ostrowski, J.; Wu, J.Y.; Rueger, D.C.; Miller, B.E.; Siegel, !1L.M.; Kredich, N.M. !$#journal J. Biol. Chem. (1989) 264:15726-15737 !$#title Characterization of the cysJIH regions of Salmonella !1typhimurium and Escherichia coli B. DNA sequences of cysI !1and cysH and a model for the siroheme-Fe-4S-4 active center !1of sulfite reductase hemoprotein based on amino acid !1homology with spinach nitrite reductase. !$#cross-references MUID:89359425; PMID:2670946 !$#accession C34354 !'##status preliminary !'##molecule_type DNA !'##residues 1-244 ##label OST !'##cross-references GB:M23007; NID:g153928; PIDN:AAA27048.1; !1PID:g153931; GB:J05009; GB:J05025; GB:M27145 CLASSIFICATION #superfamily 3'-phosphoadenosine 5'-phosphosulfate reductase KEYWORDS cysteine biosynthesis; oxidoreductase; sulfotransferase SUMMARY #length 244 #molecular-weight 28027 #checksum 5366 SEQUENCE /// ENTRY S34193 #type complete TITLE phosphoadenylyl-sulfate reductase (thioredoxin) (EC 1.8.4.8) - Thiocapsa roseopersicina ALTERNATE_NAMES 3'-phosphoadenylylsulfate reductase, thioredoxin dependent; PAPS reductase; PAPS sulfotransferase CONTAINS 3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (EC 2.8.2.-) ORGANISM #formal_name Thiocapsa roseopersicina DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 24-Aug-2001 ACCESSIONS S34193 REFERENCE S34190 !$#authors Haverkamp, T.; Gisselmann, G.; Schwenn, J.D. !$#submission submitted to the EMBL Data Library, July 1993 !$#description Structure and function of genes involved in the metabolism !1of sulfite from the sulfur oxidizing purple bacterium !1Thiocapsa roseopersicina. !$#accession S34193 !'##status preliminary !'##molecule_type DNA !'##residues 1-239 ##label HAV !'##cross-references EMBL:Z23169; NID:g1518424; PIDN:CAA80690.1; !1PID:g313354 CLASSIFICATION #superfamily 3'-phosphoadenosine 5'-phosphosulfate reductase KEYWORDS cysteine biosynthesis; oxidoreductase; sulfotransferase SUMMARY #length 239 #molecular-weight 27694 #checksum 1106 SEQUENCE /// ENTRY S28609 #type complete TITLE phosphoadenylyl-sulfate reductase (thioredoxin) (EC 1.8.4.8) - Synechococcus sp. (strain PCC 7942) ALTERNATE_NAMES 3'-phosphoadenylylsulfate reductase, thioredoxin dependent; PAPS reductase; PAPS sulfotransferase CONTAINS 3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (EC 2.8.2.-) ORGANISM #formal_name Synechococcus sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 24-Aug-2001 ACCESSIONS S28609 REFERENCE S28609 !$#authors Niehaus, A.; Gisselmann, G.; Schwenn, J.D. !$#journal Plant Mol. Biol. (1992) 20:1179-1183 !$#title Primary structure of the Synechococcus PCC 7942 PAPS !1reductase gene. !$#cross-references MUID:93099269; PMID:1463852 !$#accession S28609 !'##molecule_type DNA !'##residues 1-232 ##label NIE !'##cross-references EMBL:M84476; NID:g154543; PIDN:AAA27328.1; !1PID:g154544 GENETICS !$#gene par CLASSIFICATION #superfamily 3'-phosphoadenosine 5'-phosphosulfate reductase KEYWORDS cysteine biosynthesis; oxidoreductase; sulfotransferase SUMMARY #length 232 #molecular-weight 26636 #checksum 8930 SEQUENCE /// ENTRY A41771 #type complete TITLE 3-oxoacid CoA-transferase (EC 2.8.3.5) precursor, mitochondrial [validated] - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 26-May-2000 ACCESSIONS A41771; S27952 REFERENCE A41771 !$#authors Lin, T.W.; Bridger, W.A. !$#journal J. Biol. Chem. (1992) 267:975-978 !$#title Sequence of a cDNA clone encoding pig heart mitochondrial !1CoA transferase. !$#cross-references MUID:92112838; PMID:1730685 !$#accession A41771 !'##molecule_type mRNA !'##residues 1-520 ##label LIN !'##cross-references EMBL:M80534; NID:g164422; PIDN:AAA31019.1; !1PID:g164423 !'##experimental_source heart !'##note sequence extracted from NCBI backbone (NCBIP:75613) !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing FUNCTION !$#description EC 2.8.3.5 [validated, MUID:92112838] CLASSIFICATION #superfamily 3-oxoacid CoA-transferase; 3-oxoadipate !1CoA-transferase alpha chain homology; 3-oxoadipate !1CoA-transferase beta chain homology KEYWORDS CoA-transferase; homodimer; ketone body metabolism; !1mitochondrion FEATURE !$1-39 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$38-274 #domain 3-oxoadipate CoA-transferase alpha chain !8homology #label BACA\ !$40-520 #product 3-oxoacid CoA-transferase #status !8experimental #label MAT\ !$302-506 #domain 3-oxoadipate CoA-transferase beta chain !8homology #label BACB\ !$344 #active_site Glu #status predicted SUMMARY #length 520 #molecular-weight 56406 #checksum 1509 SEQUENCE /// ENTRY A42985 #type complete TITLE 3-oxoadipate CoA-transferase (EC 2.8.3.6) alpha chain - Pseudomonas putida ORGANISM #formal_name Pseudomonas putida DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A42985 REFERENCE A42985 !$#authors Parales, R.E.; Harwood, C.S. !$#journal J. Bacteriol. (1992) 174:4657-4666 !$#title Characterization of the genes encoding beta-ketoadipate: !1succinyl-coenzyme A transferase in Pseudomonas putida. !$#cross-references MUID:92325057; PMID:1624453 !$#accession A42985 !'##status preliminary !'##molecule_type DNA !'##residues 1-231 ##label PAR !'##cross-references GB:M88763; NID:g151426; PIDN:AAA25922.1; !1PID:g551938 !'##note sequence extracted from NCBI backbone (NCBIN:108150, !1NCBIP:108152) GENETICS !$#gene pacI CLASSIFICATION #superfamily 3-oxoadipate CoA-transferase alpha chain; !13-oxoadipate CoA-transferase alpha chain homology KEYWORDS CoA-transferase FEATURE !$1-221 #domain 3-oxoadipate CoA-transferase alpha chain !8homology #label BACA SUMMARY #length 231 #molecular-weight 24234 #checksum 6985 SEQUENCE /// ENTRY A44570 #type complete TITLE 3-oxoadipate CoA-transferase (EC 2.8.3.6) alpha chain - Acinetobacter calcoaceticus ORGANISM #formal_name Acinetobacter calcoaceticus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A44570 REFERENCE A44570 !$#authors Shanley, M.S.; Harrison, A.; Ornston, L.N. !$#submission submitted to GenBank, December 1991 !$#accession A44570 !'##status preliminary !'##molecule_type DNA !'##residues 1-228 ##label SHA !'##cross-references GB:M76991; NID:g915237; PID:g141759 GENETICS !$#gene catI CLASSIFICATION #superfamily 3-oxoadipate CoA-transferase alpha chain; !13-oxoadipate CoA-transferase alpha chain homology KEYWORDS CoA-transferase FEATURE !$1-221 #domain 3-oxoadipate CoA-transferase alpha chain !8homology #label BACA SUMMARY #length 228 #molecular-weight 24073 #checksum 83 SEQUENCE /// ENTRY B42985 #type complete TITLE 3-oxoadipate CoA-transferase (EC 2.8.3.6) beta chain [validated] - Pseudomonas putida ORGANISM #formal_name Pseudomonas putida DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-May-2000 ACCESSIONS B42985 REFERENCE A42985 !$#authors Parales, R.E.; Harwood, C.S. !$#journal J. Bacteriol. (1992) 174:4657-4666 !$#title Characterization of the genes encoding beta-ketoadipate: !1succinyl-coenzyme A transferase in Pseudomonas putida. !$#cross-references MUID:92325057; PMID:1624453 !$#accession B42985 !'##molecule_type DNA !'##residues 1-213 ##label PAR !'##cross-references GB:M88763; NID:g151426; PIDN:AAA25923.1; !1PID:g151428 !'##note sequence extracted from NCBI backbone (NCBIN:108150, !1NCBIP:108154) GENETICS !$#gene pacJ COMPLEX heterodimer of alpha (see PIR:A42985) and beta chains CLASSIFICATION #superfamily 3-oxoadipate CoA-transferase beta chain; !13-oxoadipate CoA-transferase beta chain homology KEYWORDS CoA-transferase; heterodimer FEATURE !$9-211 #domain 3-oxoadipate CoA-transferase beta chain !8homology #label BACB\ !$50 #active_site Glu #status predicted SUMMARY #length 213 #molecular-weight 22552 #checksum 804 SEQUENCE /// ENTRY B44570 #type complete TITLE 3-oxoadipate CoA-transferase (EC 2.8.3.6) beta chain - Acinetobacter calcoaceticus ORGANISM #formal_name Acinetobacter calcoaceticus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-May-2000 ACCESSIONS B44570 REFERENCE A44570 !$#authors Shanley, M.S.; Harrison, A.; Ornston, L.N. !$#submission submitted to GenBank, December 1991 !$#accession B44570 !'##status preliminary !'##molecule_type DNA !'##residues 1-217 ##label SHA !'##cross-references GB:M76991; NID:g915237; PID:g141760 GENETICS !$#gene catJ COMPLEX heterodimer of alpha (see PIR:A44570) and beta chains CLASSIFICATION #superfamily 3-oxoadipate CoA-transferase beta chain; !13-oxoadipate CoA-transferase beta chain homology KEYWORDS CoA-transferase; heterodimer FEATURE !$8-211 #domain 3-oxoadipate CoA-transferase beta chain !8homology #label BACB\ !$50 #active_site Glu #status predicted SUMMARY #length 217 #molecular-weight 23165 #checksum 1175 SEQUENCE /// ENTRY JN0489 #type complete TITLE butyrate-acetoacetate CoA-transferase (EC 2.8.3.9) beta chain - Clostridium acetobutylicum ALTERNATE_NAMES butyrate-acetoacetate CoA-transferase large chain ORGANISM #formal_name Clostridium acetobutylicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS JN0489; D37837; B60733; C49346; S33437 REFERENCE JN0487 !$#authors Petersen, D.J.; Cary, J.W.; Vanderleyden, J.; Bennett, G.N. !$#journal Gene (1993) 123:93-97 !$#title Sequence and arrangement of genes encoding enzymes of the !1acetone-production pathway of Clostridium acetobutylicum !1ATCC824. !$#cross-references MUID:93138439; PMID:8423010 !$#accession JN0489 !'##status preliminary !'##molecule_type DNA !'##residues 1-221 ##label PET !'##cross-references GB:M93363; NID:g2058393; PIDN:AAB53233.1; !1PID:g144706 !'##experimental_source ATCC 824 REFERENCE A37837 !$#authors Gerischer, U.; Duerre, P. !$#journal J. Bacteriol. (1990) 172:6907-6918 !$#title Cloning, sequencing, and molecular analysis of the !1acetoacetate decarboxylase gene region from Clostridium !1acetobutylicum. !$#cross-references MUID:91072241; PMID:2254264 !$#accession D37837 !'##status translation not shown !'##molecule_type DNA !'##residues 1-221 ##label GER !'##cross-references GB:M55392; GB:M34078; NID:g6466901; !1PIDN:AAA63762.1; PID:g144712 !'##experimental_source ATCC 824 REFERENCE A60733 !$#authors Cary, J.W.; Petersen, D.J.; Papoutsakis, E.T.; Bennett, G.N. !$#journal Appl. Environ. Microbiol. (1990) 56:1576-1583 !$#title Cloning and expression of Clostridium acetobutylicum ATCC !1824 acetoacetyl-coenzyme A:acetate/butyrate:coenzyme !1A-transferase in Escherichia coli. !$#cross-references MUID:90343312; PMID:2383002 !$#accession B60733 !'##molecule_type protein !'##residues 1-8 ##label CAR !'##experimental_source ATCC 824 REFERENCE A49346 !$#authors Fischer, R.J.; Helms, J.; Duerre, P. !$#journal J. Bacteriol. (1993) 175:6959-6969 !$#title Cloning, sequencing, and molecular analysis of the sol !1operon of Clostridium acetobutylicum, a chromosomal locus !1involved in solventogenesis. !$#cross-references MUID:94042861; PMID:8226639 !$#accession C49346 !'##status preliminary !'##molecule_type DNA !'##residues 1-221 ##label FIS !'##cross-references EMBL:X72831; NID:g298080; PIDN:CAA51346.1; !1PID:g298086 !'##experimental_source DSM 729 COMPLEX heterodimer of alpha (see PIR:B49346) and beta chains CLASSIFICATION #superfamily 3-oxoadipate CoA-transferase beta chain; !13-oxoadipate CoA-transferase beta chain homology KEYWORDS CoA-transferase; heterodimer FEATURE !$9-210 #domain 3-oxoadipate CoA-transferase beta chain !8homology #label BACB\ !$51 #active_site Glu #status predicted SUMMARY #length 221 #molecular-weight 23623 #checksum 4275 SEQUENCE /// ENTRY UVFUS #type complete TITLE cutinase (EC 3.1.-.-) precursor - fungus (Fusarium solani) ORGANISM #formal_name Fusarium solani f.sp. pisi DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 11-Jun-1999 ACCESSIONS A32836; A00731; B00731; A61421 REFERENCE A32836 !$#authors Soliday, C.L.; Dickman, M.B.; Kolattukudy, P.E. !$#journal J. Bacteriol. (1989) 171:1942-1951 !$#title Structure of the cutinase gene and detection of promoter !1activity in the 5'-flanking region by fungal transformation. !$#cross-references MUID:89197761; PMID:2703464 !$#accession A32836 !'##molecule_type DNA !'##residues 1-47,'A',49-93,'A',95-230 ##label SO1 !'##cross-references GB:M29759; NID:g168147; PIDN:AAA33335.1; !1PID:g168148 !'##note the authors translated the codon GCA for residue 94 as Arg REFERENCE A00731 !$#authors Soliday, C.L.; Flurkey, W.H.; Okita, T.W.; Kolattukudy, P.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:3939-3943 !$#title Cloning and structure determination of cDNA for cutinase, an !1enzyme involved in fungal penetration of plants. !$#accession A00731 !'##molecule_type mRNA !'##residues 1-230 ##label SO2 !'##cross-references GB:K02640; NID:g168145; PIDN:AAA33334.1; !1PID:g168146 !$#accession B00731 !'##molecule_type protein !'##residues 57-94;113-142;183-192 ##label SO3 REFERENCE A61421 !$#authors Soliday, C.L.; Kolattukudy, P.E. !$#journal Biochem. Biophys. Res. Commun. (1983) 114:1017-1022 !$#title Primary structure of the active site region of fungal !1cutinase, an enzyme involved in phytopathogenesis. !$#cross-references MUID:83308716; PMID:6412706 !$#accession A61421 !'##molecule_type protein !'##residues 113-142 ##label SO4 REFERENCE A44665 !$#authors Lin, T.S.; Kolattukudy, P.E. !$#journal Eur. J. Biochem. (1980) 106:341-351 !$#title Structural studies on cutinase, a glycoprotein containing !1novel amino acids and glucuronic acid amide at the N !1terminus. !$#cross-references MUID:80245930; PMID:7398618 !$#contents annotation; identification of glucuronylated amino end COMMENT This enzyme catalyzes the hydrolysis of cutin, a polyester !1that forms the structure of plant cuticle. COMMENT Southern blot results suggest that the genome contains two !1copies of the cutinase gene. This entry represents a gene !1induced in fungal spores after contact with a plant surface. GENETICS !$#introns 64/3 CLASSIFICATION #superfamily cutinase KEYWORDS blocked amino end; glycoprotein; hydrolase FEATURE !$1-31 #domain signal sequence #status predicted #label SIG\ !$32-230 #product cutinase #status predicted #label MAT\ !$32 #modified_site glucuronylated amino end (Gly) (in !8mature form) #status experimental\ !$125-187 #disulfide_bonds #status experimental\ !$136,204 #active_site Ser, His #status experimental SUMMARY #length 230 #molecular-weight 23982 #checksum 7892 SEQUENCE /// ENTRY S20448 #type complete TITLE cutinase (EC 3.1.-.-) - rice blast fungus ORGANISM #formal_name Magnaporthe grisea #common_name rice blast fungus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S20448 REFERENCE S20448 !$#authors Sweigard, J.A.; Chumley, F.G.; Valent, B. !$#journal Mol. Gen. Genet. (1992) 232:174-182 !$#title Cloning and analysis of CUT1, a cutinase gene from !1Magnaporthe grisea. !$#cross-references MUID:92212279; PMID:1557023 !$#accession S20448 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-228 ##label SWE !'##cross-references GB:X61500; NID:g2928; PIDN:CAA43717.1; PID:g1045205 GENETICS !$#gene CUT1 CLASSIFICATION #superfamily cutinase KEYWORDS hydrolase SUMMARY #length 228 #molecular-weight 24276 #checksum 223 SEQUENCE /// ENTRY S21427 #type complete TITLE cutinase - fungus (Ascochyta rabiei) ORGANISM #formal_name Ascochyta rabiei DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S21427 REFERENCE S21427 !$#authors Tenhaken, R.; Barz, W. !$#submission submitted to the EMBL Data Library, April 1992 !$#description Characterization and cloning of cutinase from Ascochyta !1rabiei. !$#accession S21427 !'##status preliminary !'##molecule_type DNA !'##residues 1-223 ##label TEN !'##cross-references EMBL:X65628; NID:g2472; PIDN:CAA46582.1; PID:g2473 GENETICS !$#introns 63/3 CLASSIFICATION #superfamily cutinase SUMMARY #length 223 #molecular-weight 23520 #checksum 1755 SEQUENCE /// ENTRY LIRTT #type complete TITLE triacylglycerol lipase (EC 3.1.1.3) precursor, lingual - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 11-Jun-1999 ACCESSIONS A23045 REFERENCE A23045 !$#authors Docherty, A.J.P.; Bodmer, M.W.; Angal, S.; Verger, R.; !1Riviere, C.; Lowe, P.A.; Lyons, A.; Emtage, J.S.; Harris, !1T.J.R. !$#journal Nucleic Acids Res. (1985) 13:1891-1903 !$#title Molecular cloning and nucleotide sequence of rat lingual !1lipase cDNA. !$#cross-references MUID:85215587; PMID:3839077 !$#accession A23045 !'##molecule_type mRNA !'##residues 1-395 ##label DOC !'##cross-references GB:X02309; NID:g56595; PIDN:CAA26179.1; PID:g56596 !'##experimental_source strain Sprague-Dawley !'##note the partial sequence of the mature protein from a different, !1unspecified strain differed from that shown in having 25-Met !1and 32-Val COMMENT This acid-stable lipase is secreted by the serous (von !1Ebner's) glands at the back of the tongue. CLASSIFICATION #superfamily triacylglycerol lipase, lingual KEYWORDS carboxylic ester hydrolase; glycoprotein; lipid digestion; !1saliva; serous glands; von Ebner's gland FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-395 #product triacylglycerol lipase, lingual #status !8predicted #label MPT\ !$33,68,98,184,270 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 395 #molecular-weight 44588 #checksum 7307 SEQUENCE /// ENTRY JC4017 #type complete TITLE triacylglycerol lipase (EC 3.1.1.3) PGE precursor - bovine ALTERNATE_NAMES pregastric esterase ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JC4017; S64678 REFERENCE JC4017 !$#authors Timmermans, M.Y.J.; Teuchy, H.; Kupers, L.P.M. !$#journal Gene (1994) 147:259-262 !$#title The cDNA sequence encoding bovine pregastric esterase. !$#cross-references MUID:95011625; PMID:7926811 !$#accession JC4017 !'##molecule_type mRNA !'##residues 1-397 ##label TIM !'##cross-references GB:L26319; NID:g600756; PIDN:AAA57037.1; !1PID:g600757 !'##experimental_source tongue REFERENCE S64678 !$#authors Timmermans, M.Y.J.; Reekmans, G.; Teuchy, H.J.H.; Kupers, !1L.P.M. !$#journal Biochem. J. (1996) 314:931-936 !$#title Inhibition studies on calf pregastric esterase: the enzyme !1has no functional thiol group. !$#cross-references MUID:96177869; PMID:8615791 !$#accession S64678 !'##molecule_type protein !'##residues 24-40;248-253 ##label TIW COMMENT Pregastric esterase is a major fat-digesting enzyme. GENETICS !$#gene pge CLASSIFICATION #superfamily triacylglycerol lipase, lingual KEYWORDS blocked amino end; carboxylic ester hydrolase; glycoprotein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-397 #product pregastric esterase #status predicted #label !8MAT\ !$33,270,326 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$171 #active_site Ser #status predicted SUMMARY #length 397 #molecular-weight 45231 #checksum 2511 SEQUENCE /// ENTRY JT0579 #type complete TITLE triacylglycerol lipase (EC 3.1.1.3) precursor - Pseudomonas sp. ALTERNATE_NAMES lipase ORGANISM #formal_name Pseudomonas sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS JT0579; PS0202; JQ1227; PQ0229 REFERENCE JT0579 !$#authors Iizumi, T.; Nakamura, K.; Shimada, Y.; Sugihara, A.; !1Tominaga, Y.; Fukase, T. !$#journal Agric. Biol. Chem. (1991) 55:2349-2357 !$#title Cloning, nucleotide sequencing, and expression in !1Escherichia coli of a lipase and its activator genes from !1Pseudomonas sp. KWI-56. !$#cross-references MUID:92118328; PMID:1368739 !$#accession JT0579 !'##molecule_type DNA !'##residues 1-364 ##label IIZ !'##cross-references GB:D10069; GB:D01216; NID:g216898; PIDN:BAA00960.1; !1PID:g216899 !$#accession PS0202 !'##molecule_type protein !'##residues 45-47 ##label II2 GENETICS !$#gene lip CLASSIFICATION #superfamily Pseudomonas triacylglycerol lipase KEYWORDS carboxylic ester hydrolase FEATURE !$1-44 #domain signal sequence #status predicted #label SIG\ !$45-364 #product triacylglycerol lipase #status predicted !8#label MAT SUMMARY #length 364 #molecular-weight 37511 #checksum 9013 SEQUENCE /// ENTRY A39133 #type complete TITLE triacylglycerol lipase (EC 3.1.1.3) precursor - Pseudomonas cepacia ORGANISM #formal_name Pseudomonas cepacia DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A39133 REFERENCE A39133 !$#authors Jorgensen, S.; Skov, K.W.; Diderichsen, B. !$#journal J. Bacteriol. (1991) 173:559-567 !$#title Cloning, sequence, and expression of a lipase gene from !1Pseudomonas cepacia: lipase production in heterologous hosts !1requires two Pseudomonas genes. !$#cross-references MUID:91100343; PMID:1987151 !$#accession A39133 !'##status preliminary !'##molecule_type DNA !'##residues 1-364 ##label JOR !'##cross-references GB:M58494 CLASSIFICATION #superfamily Pseudomonas triacylglycerol lipase KEYWORDS carboxylic ester hydrolase SUMMARY #length 364 #molecular-weight 37442 #checksum 8080 SEQUENCE /// ENTRY A48952 #type complete TITLE triacylglycerol lipase (EC 3.1.1.3) precursor - Pseudomonas glumae ORGANISM #formal_name Pseudomonas glumae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A48952; S36248; S37291 REFERENCE A48952 !$#authors Frenken, L.G.; Egmond, M.R.; Batenburg, A.M.; Bos, J.W.; !1Visser, C.; Verrips, C.T. !$#journal Appl. Environ. Microbiol. (1992) 58:3787-3791 !$#title Cloning of the Pseudomonas glumae lipase gene and !1determination of the active site residues. !$#cross-references MUID:93119130; PMID:1476423 !$#accession A48952 !'##status preliminary !'##molecule_type DNA !'##residues 1-358 ##label FRE !'##cross-references EMBL:X70354; NID:g49205; PIDN:CAA49812.1; !1PID:g49206 !'##experimental_source PG1 !'##note sequence extracted from NCBI backbone (NCBIN:121572, !1NCBIP:121573) REFERENCE S36248 !$#authors Frenken, L.G.J.; Bos, J.W.; Visser, C.; Mueller, W.; !1Tommassen, J.; Verrips, C.T. !$#journal Mol. Microbiol. (1993) 9:579-589 !$#title An accessory gene, lipB, required for the production of !1active Pseudomonas glumae lipase. !$#cross-references MUID:94018652; PMID:8412704 !$#accession S36248 !'##molecule_type DNA !'##residues 316-358 ##label FR2 !'##cross-references EMBL:X70354 GENETICS !$#gene lipA CLASSIFICATION #superfamily Pseudomonas triacylglycerol lipase KEYWORDS carboxylic ester hydrolase; extracellular protein SUMMARY #length 358 #molecular-weight 36928 #checksum 8431 SEQUENCE /// ENTRY S25768 #type complete TITLE triacylglycerol lipase (EC 3.1.1.3) precursor - Pseudomonas aeruginosa ALTERNATE_NAMES lipase A precursor ORGANISM #formal_name Pseudomonas aeruginosa DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 31-Dec-2000 ACCESSIONS S25768; S24160; S21751; B83289; JT0958 REFERENCE S25768 !$#authors Wohlfarth, S.; Hoesche, C.; Strunk, C.; Winkler, U.K. !$#journal J. Gen. Microbiol. (1992) 138:1325-1335 !$#title Molecular genetics of the extracellular lipase of !1Pseudomonas aeruginosa PAO1. !$#cross-references MUID:92381478; PMID:1512563 !$#accession S25768 !'##molecule_type DNA !'##residues 1-311 ##label WOH !'##cross-references EMBL:X63390; NID:g45340; PIDN:CAA44997.1; !1PID:g45341 REFERENCE S24160 !$#authors Chihara-Siomi, M.; Yoshikawa, K.; Oshima-Hirayama, N.; !1Yamamoto, K.; Sogabe, Y.; Nakatani, T.; Nishioka, T.; Oda, !1J. !$#journal Arch. Biochem. Biophys. (1992) 296:505-513 !$#title Purification, molecular cloning, and expression of lipase !1from Pseudomonas aeruginosa. !$#cross-references MUID:92337414; PMID:1632642 !$#accession S24160 !'##status preliminary !'##molecule_type DNA !'##residues 1-155,'I',157-201,'H',203,'V',205-311 ##label CHI !'##cross-references GB:D10048; NID:g2575868; PIDN:BAA23128.1; !1PID:g2575869 REFERENCE S21751 !$#authors Jaeger, K.E.; Adrian, F.J.; Meyer, H.E.; Hancock, R.E.W.; !1Winkler, U.K. !$#journal Biochim. Biophys. Acta (1992) 1120:315-321 !$#title Extracellular lipase from Pseudomonas aeruginosa is an !1amphiphilic protein. !$#cross-references MUID:92247813; PMID:1576157 !$#accession S21751 !'##status preliminary !'##molecule_type protein !'##residues 27-39,'X',41-53,'X',55-57 ##label JAE REFERENCE A82950 !$#authors Stover, C.K.; Pham, X.Q.; Erwin, A.L.; Mizoguchi, S.D.; !1Warrener, P.; Hickey, M.J.; Brinkman, F.S.L.; Hufnagle, !1W.O.; Kowalik, D.J.; Lagrou, M.; Garber, R.L.; Goltry, L.; !1Tolentino, E.; Westbrook-Wadman, S.; Yuan, Y.; Brody, L.L.; !1Coulter, S.N.; Folger, K.R.; Kas, A.; Larbig, K.; Lim, R.M.; !1Smith, K.A.; Spencer, D.H.; Wong, G.K.S.; Wu, Z.; Paulsen, !1I.T.; Reizer, J.; Saier, M.H.; Hancock, R.E.W.; Lory, S.; !1Olson, M.V. !$#journal Nature (2000) 406:959-964 !$#title Complete genome sequence of Pseudomonas aeruginosa PA01, an !1opportunistic pathogen. !$#cross-references MUID:20437337; PMID:10984043 !$#accession B83289 !'##status preliminary !'##molecule_type DNA !'##residues 1-311 ##label STO !'##cross-references GB:AE004712; GB:AE004091; NID:g9948940; !1PIDN:AAG06250.1; GSPDB:GN00131; PASP:PA2862 !'##experimental_source strain PAO1 GENETICS !$#gene lipA; lip; PA2862 CLASSIFICATION #superfamily Pseudomonas triacylglycerol lipase KEYWORDS carboxylic ester hydrolase FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-311 #product lipase #status predicted #label LIP SUMMARY #length 311 #molecular-weight 32723 #checksum 451 SEQUENCE /// ENTRY A40943 #type complete TITLE lactonizing lipase (EC 3.1.1.-) precursor - Pseudomonas sp. ALTERNATE_NAMES lipase P ORGANISM #formal_name Pseudomonas sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A40943; B40943 REFERENCE A40943 !$#authors Ihara, F.; Kageyama, Y.; Hirata, M.; Nihira, T.; Yamada, Y. !$#journal J. Biol. Chem. (1991) 266:18135-18140 !$#title Purification, characterization, and molecular cloning of !1lactonizing lipase from Pseudomonas species. !$#cross-references MUID:92011544; PMID:1917947 !$#accession A40943 !'##molecule_type DNA !'##residues 1-311 ##label IHA !'##cross-references GB:D10166; GB:D90398; NID:g216901; PIDN:BAA01035.1; !1PID:g216902 !$#accession B40943 !'##molecule_type protein !'##residues 27-45 ##label IH2 COMMENT This extracellular lipase catalyzes the synthesis of !1macrocyclic lactones in anhydrous organic solvents. CLASSIFICATION #superfamily Pseudomonas triacylglycerol lipase KEYWORDS carboxylic ester hydrolase FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-311 #product lactonizing lipase #status experimental !8#label MAT SUMMARY #length 311 #molecular-weight 32737 #checksum 580 SEQUENCE /// ENTRY S02005 #type complete TITLE triacylglycerol lipase (EC 3.1.1.3) - Pseudomonas fragi ORGANISM #formal_name Pseudomonas fragi DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S02005; A26383 REFERENCE S02005 !$#authors Aoyama, S.; Yoshida, N.; Inouye, S. !$#journal FEBS Lett. (1988) 242:36-40 !$#title Cloning, sequencing and expression of the lipase gene from !1Pseudomonas fragi IFO-12049 in E. coli. !$#cross-references MUID:89078617; PMID:3060375 !$#accession S02005 !'##molecule_type DNA !'##residues 1-277 ##label AOY !'##cross-references EMBL:X14033; NID:g45512; PIDN:CAA32193.1; !1PID:g45513 !'##experimental_source IFO-12049 REFERENCE A26383 !$#authors Kugimiya, W.; Otani, Y.; Hashimoto, Y.; Takagi, Y. !$#journal Biochem. Biophys. Res. Commun. (1986) 141:185-190 !$#title Molecular cloning and nucleotide sequence of the lipase gene !1from Pseudomonas fragi. !$#cross-references MUID:87100109; PMID:3800995 !$#accession A26383 !'##molecule_type DNA !'##residues 1-118,'CAWPLSRGGLAKRWLPP' ##label KUG !'##cross-references GB:M14604; NID:g151332; PIDN:AAA25879.1; !1PID:g151333 CLASSIFICATION #superfamily Pseudomonas triacylglycerol lipase KEYWORDS carboxylic ester hydrolase SUMMARY #length 277 #molecular-weight 29985 #checksum 2853 SEQUENCE /// ENTRY LIRTH #type complete TITLE hormone-sensitive lipase (EC 3.1.1.-) - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 27-Jan-1995 ACCESSIONS S03672; A41239 REFERENCE S03672 !$#authors Holm, C.; Kirchgessner, T.G.; Svenson, K.L.; Lusis, A.J.; !1Belfrage, P.; Schotz, M.C. !$#journal Nucleic Acids Res. (1988) 16:9879 !$#title Nucleotide sequence of rat adipose hormone sensitive lipase !1cDNA. !$#cross-references MUID:89041594; PMID:3186461 !$#accession S03672 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-757 ##label HO1 !'##cross-references EMBL:X51415 REFERENCE A41239 !$#authors Holm, C.; Kirchgessner, T.G.; Svenson, K.L.; Fredrikson, G.; !1Nilsson, S.; Miller, C.G.; Shively, J.E.; Heinzmann, C.; !1Sparkes, R.S.; Mohandas, T.; Lusis, A.J.; Belfrage, P.; !1Schotz, M.C. !$#journal Science (1988) 241:1503-1506 !$#title Hormone-sensitive lipase: sequence, expression, and !1chromosomal localization to 19 cent-q13.3. !$#cross-references MUID:88336885; PMID:3420405 !$#accession A41239 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-757 ##label HO2 !'##cross-references EMBL:X51415 COMMENT This enzyme is responsible for hormone-sensitive !1acylglycerol hydrolase and cholesteryl ester hydrolase !1activity in a variety of tissues. It is a key enzyme in !1fatty acid mobilization from adipose tissue triglycerides !1and probably is important in steroidogenesis. COMMENT This enzyme is rapidly activated by cAMP-dependent !1phosphorylation under the influence of catecholamines. !1Dephosphorylation and inactivation are controlled by !1insulin. CLASSIFICATION #superfamily hormone-sensitive lipase KEYWORDS carboxylic ester hydrolase; lipid degradation; !1phosphoprotein; steroid biosynthesis FEATURE !$563 #binding_site phosphate (Ser) (covalent) (by !8cAMP-dependent kinase) #status predicted SUMMARY #length 757 #molecular-weight 82820 #checksum 6167 SEQUENCE /// ENTRY LIPG #type complete TITLE triacylglycerol lipase (EC 3.1.1.3) - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 30-Nov-1980 #sequence_revision 22-May-1981 #text_change 31-Mar-2000 ACCESSIONS A90638; A91256; A90675; A91124; A00732 REFERENCE A90638 !$#authors De Caro, J.; Boudouard, M.; Bonicel, J.; Guidoni, A.; !1Desnuelle, P.; Rovery, M. !$#journal Biochim. Biophys. Acta (1981) 671:129-138 !$#title Porcine pancreatic lipase. Completion of the primary !1structure. !$#cross-references MUID:82113655; PMID:7326260 !$#accession A90638 !'##molecule_type protein !'##residues 308-449 ##label DEC !'##experimental_source pancreas REFERENCE A91256 !$#authors Bianchetta, J.D.; Bidaud, J.; Guidoni, A.A.; Bonicel, J.J.; !1Rovery, M. !$#journal Eur. J. Biochem. (1979) 97:395-405 !$#title Porcine pancreatic lipase. Sequence of the first 234 amino !1acids of the peptide chain. !$#cross-references MUID:79236335; PMID:380992 !$#contents carbohydrate-binding site !$#accession A91256 !'##molecule_type protein !'##residues 1-234 ##label BIA !'##experimental_source pancreas REFERENCE A90675 !$#authors Guidoni, A.; Bonicel, J.; Bianchetta, J.; Rovery, M. !$#journal Biochimie (1979) 61:841-845 !$#title Porcine pancreatic lipase. Sequence between the 235th and !1307th amino acids. !$#cross-references MUID:80088446; PMID:518929 !$#accession A90675 !'##molecule_type protein !'##residues 235-307 ##label GUI !'##experimental_source pancreas !'##note this sequence has since been revised at positions 302 and 305 REFERENCE A91124 !$#authors Benkouka, F.; Guidoni, A.A.; De Caro, J.D.; Bonicel, J.J.; !1Desnuelle, P.A.; Rovery, M. !$#journal Eur. J. Biochem. (1982) 128:331-341 !$#title Porcine pancreatic lipase. The disulfide bridges and the !1sulfhydryl groups. !$#cross-references MUID:83105095; PMID:7151781 !$#contents disulfide bonds !$#accession A91124 !'##molecule_type protein !'##residues 1-182,'E',184-449 ##label BEN !'##experimental_source pancreas REFERENCE A90634 !$#authors Guidoni, A.; Benkouka, F.; De Caro, J.; Rovery, M. !$#journal Biochim. Biophys. Acta (1981) 660:148-150 !$#title Characterization of the serine reacting with diethyl !1p-nitrophenyl phosphate in porcine pancreatic lipase. !$#cross-references MUID:82000578; PMID:6791692 !$#contents annotation; substrate-binding site COMMENT Ser-152 reacts with emulsified or micellar diethyl !1p-nitrophenyl phosphate and appears to be involved in the !1interface recognition site. CLASSIFICATION #superfamily triacylglycerol lipase KEYWORDS carboxylic ester hydrolase; glycoprotein; lipid digestion FEATURE !$4-10,237-261, !$285-296,299-304, !$433-449 #disulfide_bonds #status experimental\ !$90-101 #disulfide_bonds (or 90-103) #status experimental\ !$166 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 449 #molecular-weight 49926 #checksum 976 SEQUENCE /// ENTRY LIDG #type complete TITLE triacylglycerol lipase (EC 3.1.1.3) precursor, pancreatic - dog ALTERNATE_NAMES triacylglycerol acylhydrolase ORGANISM #formal_name Canis lupus familiaris #common_name dog DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 31-Mar-2000 ACCESSIONS B24392; A32615; B30034 REFERENCE A93751 !$#authors Kerfelec, B.; LaForge, K.S.; Puigserver, A.; Scheele, G. !$#journal Pancreas (1986) 1:430-437 !$#title Primary structures of canine pancreatic lipase and !1phospholipase A2 messenger RNAs. !$#cross-references MUID:87175472; PMID:3562437 !$#accession B24392 !'##molecule_type mRNA !'##residues 1-467 ##label KER !'##cross-references GB:M35302; NID:g164047; PIDN:AAA30885.1; !1PID:g164048 !'##note the authors translated the codon UGC for residue 21 as Lys REFERENCE A32615 !$#authors Mickel, F.S.; Weidenbach, F.; Swarovsky, B.; LaForge, K.S.; !1Scheele, G.A. !$#journal J. Biol. Chem. (1989) 264:12895-12901 !$#title Structure of the canine pancreatic lipase gene. !$#cross-references MUID:89327249; PMID:2502543 !$#accession A32615 !'##molecule_type DNA !'##residues 1-91,'I',93-97,'D',99-264,'D',266-467 ##label MIC GENETICS !$#introns 17/1; 68/3; 110/3; 155/3; 192/1; 232/1; 272/1; 311/3; 355/1; !1391/2; 447/2 CLASSIFICATION #superfamily triacylglycerol lipase KEYWORDS carboxylic ester hydrolase; lipid digestion; pancreas FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-467 #product triacylglycerol lipase, pancreatic #status !8predicted #label MPT\ !$171,194,281 #active_site Ser, Asp, His #status predicted SUMMARY #length 467 #molecular-weight 51468 #checksum 1773 SEQUENCE /// ENTRY JC1318 #type complete TITLE triacylglycerol lipase (EC 3.1.1.3) precursor, pancreatic - rabbit ALTERNATE_NAMES triglyceride lipase ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 31-Mar-2000 ACCESSIONS JC1318 REFERENCE JC1318 !$#authors Aleman-Gomez, J.A.; Colwell, N.S.; Sasser, T.; Kumar, V.B. !$#journal Biochem. Biophys. Res. Commun. (1992) 188:964-971 !$#title Molecular cloning and characterization of rabbit pancreatic !1triglyceride lipase. !$#cross-references MUID:93075235; PMID:1445366 !$#accession JC1318 !'##molecule_type mRNA !'##residues 1-465 ##label ALE !'##cross-references GB:M99365 CLASSIFICATION #superfamily triacylglycerol lipase KEYWORDS carboxylic ester hydrolase FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$170,194,281 #active_site Ser, Asp, His #status predicted SUMMARY #length 465 #molecular-weight 51163 #checksum 9084 SEQUENCE /// ENTRY A34671 #type complete TITLE triacylglycerol lipase (EC 3.1.1.3) precursor, pancreatic - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 31-Mar-2000 ACCESSIONS A34671 REFERENCE A34671 !$#authors Grusby, M.J.; Nabavi, N.; Wong, H.; Dick, R.F.; Bluestone, !1J.A.; Schotz, M.C.; Glimcher, L.H. !$#journal Cell (1990) 60:451-459 !$#title Cloning of an interleukin-4 inducible gene from cytotoxic T !1lymphocytes and its identification as a lipase. !$#cross-references MUID:90150272; PMID:2302735 !$#accession A34671 !'##status preliminary !'##molecule_type mRNA !'##residues 1-482 ##label GRU !'##cross-references GB:M30687 !'##note the authors translated the codon CGA for residue 362 as Gly CLASSIFICATION #superfamily triacylglycerol lipase KEYWORDS carboxylic ester hydrolase FEATURE !$1-30 #domain signal sequence #status predicted #label SIG\ !$184,208,295 #active_site Ser, Asp, His #status predicted SUMMARY #length 482 #molecular-weight 54097 #checksum 5583 SEQUENCE /// ENTRY A46696 #type complete TITLE triacylglycerol lipase (EC 3.1.1.3) precursor, pancreatic - rat ALTERNATE_NAMES glycosylated membrane-associated lipase GP-3 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 31-Mar-2000 ACCESSIONS A46696 REFERENCE A46696 !$#authors Wishart, M.J.; Andrews, P.C.; Nichols, R.; Blevins Jr., !1G.T.; Logsdon, C.D.; Williams, J.A. !$#journal J. Biol. Chem. (1993) 268:10303-10311 !$#title Identification and cloning of GP-3 from rat pancreatic !1acinar zymogen granules as a glycosylated !1membrane-associated lipase. !$#cross-references MUID:93252914; PMID:8486693 !$#accession A46696 !'##molecule_type mRNA; protein !'##residues 1-482 ##label WIS !'##cross-references GB:L09216; NID:g294555; PIDN:AAA41250.1; !1PID:g294556 !'##experimental_source pancreas !'##note sequence extracted from NCBI backbone (NCBIN:131274, !1NCBIP:131275) !'##note this publication is not cited in GenBank entry RATGLYLIPA, !1release 113.0 !'##note part of this sequence, including the amino end of the mature !1protein, was determined by protein sequencing CLASSIFICATION #superfamily triacylglycerol lipase KEYWORDS carboxylic ester hydrolase; glycoprotein FEATURE !$1-30 #domain signal sequence #status predicted #label SIG\ !$31-482 #product triacylglycerol lipase, pancreatic #status !8experimental #label MAT\ !$184,208,295 #active_site Ser, Asp, His #status predicted\ !$366 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 482 #molecular-weight 54005 #checksum 7239 SEQUENCE /// ENTRY A49488 #type complete TITLE triacylglycerol lipase (EC 3.1.1.3), pancreatic - guinea pig ORGANISM #formal_name Cavia porcellus #common_name guinea pig DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 31-Mar-2000 ACCESSIONS A49488 REFERENCE A49488 !$#authors Hjorth, A.; Carriere, F.; Cudrey, C.; Woldike, H.; Boel, E.; !1Lawson, D.M.; Ferrato, F.; Cambillau, C.; Dodson, G.G.; !1Thim, L.; Verger, R. !$#journal Biochemistry (1993) 32:4702-4707 !$#title A structural domain (the lid) found in pancreatic lipases is !1absent in the guinea pig (phospho)lipase. !$#cross-references MUID:93257433; PMID:8490016 !$#accession A49488 !'##status preliminary; translation not shown; not compared with !1conceptual translation !'##molecule_type mRNA; protein !'##residues 1-434 ##label HJO !'##experimental_source pancreas !'##note sequence extracted from NCBI backbone (NCBIP:132521) CLASSIFICATION #superfamily triacylglycerol lipase KEYWORDS carboxylic ester hydrolase FEATURE !$154,178,247 #active_site Ser, Asp, His #status predicted SUMMARY #length 434 #molecular-weight 47677 #checksum 4085 SEQUENCE /// ENTRY LIHUL #type complete TITLE lipoprotein lipase (EC 3.1.1.34) precursor - human ALTERNATE_NAMES LPL ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Jun-2000 ACCESSIONS A26082; S03710; S13552; PH0849; A42050; B42050; C42050; !1A39044; S10575; I37996; I55564; I70232; I55573 REFERENCE A26082 !$#authors Wion, K.L.; Kirchgessner, T.G.; Lusis, A.J.; Schotz, M.C.; !1Lawn, R.M. !$#journal Science (1987) 235:1638-1641 !$#title Human lipoprotein lipase complementary DNA sequence. !$#cross-references MUID:87149101; PMID:3823907 !$#accession A26082 !'##molecule_type mRNA !'##residues 1-475 ##label WIO !'##cross-references GB:M15856; NID:g187209; PIDN:AAB59536.1; !1PID:g307138 REFERENCE S03710 !$#authors Gotoda, T.; Senda, M.; Gamou, T.; Furuichi, Y.; Oka, K. !$#journal Nucleic Acids Res. (1989) 17:2351 !$#title Nucleotide sequence of human cDNA coding for a lipoprotein !1lipase (LPL) cloned from placental cDNA library. !$#cross-references MUID:89202044; PMID:2701938 !$#accession S03710 !'##molecule_type mRNA !'##residues 1-475 ##label GOT !'##cross-references EMBL:X14390; NID:g34404; PIDN:CAA32564.1; !1PID:g34405 REFERENCE S13552 !$#authors Takagi, A.; Ikeda, Y.; Yamamoto, A. !$#journal Nucleic Acids Res. (1990) 18:6436 !$#title DNA sequence of lipoprotein lipase cDNA cloned from human !1monocytic leukemia THP-1 cells. !$#cross-references MUID:91057142; PMID:2243796 !$#accession S13552 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-475 ##label TAK1 !'##cross-references EMBL:X54516; NID:g34382; PIDN:CAA38372.1; !1PID:g34383 REFERENCE PH0849 !$#authors Chuat, J.C.; Raisonnier, A.; Etienne, J.; Galibert, F. !$#journal Gene (1992) 110:257-261 !$#title The lipoprotein lipase-encoding human gene: sequence from !1intron-6 to intron-9 and presence in intron-7 of a !140-million-year-old Alu sequence. !$#cross-references MUID:92165069; PMID:1537564 !$#accession PH0849 !'##molecule_type DNA !'##residues 341-475 ##label CHU !'##cross-references GB:M76722; NID:g187215; PIDN:AAA59528.1; !1PID:g553523 REFERENCE A42050 !$#authors Ma, Y.H.; Bruin, T.; Tuzgol, S.; Wilson, B.I.; Roederer, G.; !1Liu, M.S.; Davignon, J.; Kastelein, J.J.; Brunzell, J.D.; !1Hayden, M.R. !$#journal J. Biol. Chem. (1992) 267:1918-1923 !$#title Two naturally occurring mutations at the first and second !1bases of codon aspartic acid 156 in the proposed catalytic !1triad of human lipoprotein lipase. In vivo evidence that !1aspartic acid 156 is essential for catalysis. !$#cross-references MUID:92112922; PMID:1730727 !$#accession A42050 !'##molecule_type DNA !'##residues 182,'G',184-186 ##label MA1 !'##cross-references GB:S76125; NID:g242985; PIDN:AAB20998.1; !1PID:g242986 !'##note sequence extracted from NCBI backbone (NCBIN:76125, !1NCBIP:76132) !$#accession B42050 !'##molecule_type DNA !'##residues 239-242,'S',244-247 ##label MA2 !'##cross-references GB:S76077; NID:g242987; PIDN:AAB20999.1; !1PID:g242988 !'##note sequence extracted from NCBI backbone (NCBIN:76077, !1NCBIP:76131) !$#accession C42050 !'##molecule_type DNA !'##residues 182,'N',184-189 ##label MA3 !'##cross-references GB:S76076; NID:g242989; PIDN:AAB21000.1; !1PID:g242990 !'##note sequence extracted from NCBI backbone (NCBIN:76076, !1NCBIP:76129) !'##note these mutations were identified in patients with LDL deficiency REFERENCE A39044 !$#authors Dichek, H.L.; Fojo, S.S.; Beg, O.U.; Skarlatos, S.I.; !1Brunzell, J.D.; Cutler Jr., G.B.; Brewer Jr., H.B. !$#journal J. Biol. Chem. (1991) 266:473-477 !$#title Identification of two separate allelic mutations in the !1lipoprotein lipase gene of a patient with the familial !1hyperchylomicronemia syndrome. !$#cross-references MUID:91093167; PMID:1702428 !$#accession A39044 !'##molecule_type mRNA !'##residues 219-223;268-272 ##label DIC !'##note normal sequence is shown; alleles with mutations of 221-Ile to !1Thr or of 270-Arg to His were inactive REFERENCE S10575 !$#authors Oka, K.; Tkalcevic, G.T.; Nakano, T.; Tucker, H.; !1Ishimura-Oka, K.; Brown, W.V. !$#journal Biochim. Biophys. Acta (1990) 1049:21-26 !$#title Structure and polymorphic map of human lipoprotein lipase !1gene. !$#cross-references MUID:90291024; PMID:1972631 !$#accession S10575 !'##molecule_type DNA !'##residues 1-5;26-34;79-88;139,'D', !1141-148;177-185;255-263;336-344;376-384;437-445;472-475 !1##label OKA !'##cross-references GB:X52978; GB:X53518; NID:g34386 !'##note this translation is not annotated in GenBank entry HSLIPASE, !1release 114.0 REFERENCE I37996 !$#authors Enerback, S.; Ohlsson, B.G.; Samuelsson, L.; Bjursell, G. !$#journal Mol. Cell. Biol. (1992) 12:4622-4633 !$#title Characterization of the human lipoprotein lipase (LPL) !1promoter: evidence of two cis-regulatory regions, LP-alpha !1and LP-beta, of importance for the differentiation-linked !1induction of the LPL gene during adipogenesis. !$#cross-references MUID:93024407; PMID:1406652 !$#accession I37996 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-5 ##label ENE !'##cross-references EMBL:X68111; NID:g34389; PIDN:CAA48230.1; !1PID:g4379028 REFERENCE I55564 !$#authors Gotoda, T.; Yamada, N.; Kawamura, M.; Kozaki, K.; Mori, N.; !1Ishibashi, S.; Shimano, H.; Takaku, F.; Yazaki, Y.; !1Furuichi, Y. !$#journal J. Clin. Invest. (1991) 88:1856-1864 !$#title Heterogeneous mutations in the human lipoprotein lipase gene !1in patients with familial lipoprotein lipase deficiency. !$#cross-references MUID:92091492; PMID:1752947 !$#accession I55564 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 228-230,'E',232-233 ##label GOT1 !'##cross-references GB:S71706; NID:g240930; PIDN:AAB20664.1; !1PID:g240931 !$#accession I70232 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 268-269,'H',271-273 ##label GOT2 !'##cross-references GB:S71710; NID:g240928; PIDN:AAB20663.1; !1PID:g240929 REFERENCE I55573 !$#authors Takagi, A.; Ikeda, Y.; Tsutsumi, Z.; Shoji, T.; Yamamoto, A. !$#journal J. Clin. Invest. (1992) 89:581-591 !$#title Molecular studies on primary lipoprotein lipase (LPL) !1deficiency. One base deletion (G916) in exon 5 of LPL gene !1causes no detectable LPL protein due to the absence of LPL !1mRNA transcript. !$#cross-references MUID:92147877; PMID:1737848 !$#accession I55573 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 246-247,'LSA' ##label TAK2 !'##cross-references GB:S81339; NID:g245360; PIDN:AAB21420.1; !1PID:g245361 !'##note mutant sequence from patients with primary lipoprotein lipase !1deficiency COMMENT The primary function of this lipase is the hydrolysis of !1triglycerides of circulating chylomicrons and very low !1density lipoproteins (VLDL). The enzyme functions in the !1presence of apolipoprotein C-II on the luminal surface of !1vascular endothelium, where it is anchored by a !1membrane-bound glycosaminoglycan chain. GENETICS !$#gene GDB:LPL; LIPD !'##cross-references GDB:120700; OMIM:238600 !$#map_position 8p22-8p22 !$#introns 380/2; 441/2 COMPLEX homodimer FUNCTION !$#description catalyzes the hydrolysis of triacylglycerol to !1diacylglycerol plus a fatty acid !$#pathway lipid degradation CLASSIFICATION #superfamily triacylglycerol lipase KEYWORDS carboxylic ester hydrolase; glycoprotein; lipid degradation; !1plasma FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-475 #product lipoprotein lipase #status predicted #label !8MPT\ !$152-169 #region lipid binding #status predicted\ !$54-67,243-266, !$291-310,302-305, !$445-465 #disulfide_bonds #status predicted\ !$70,386 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$159,183,268 #active_site Ser, Asp, His #status predicted SUMMARY #length 475 #molecular-weight 53162 #checksum 4551 SEQUENCE /// ENTRY A40570 #type complete TITLE lipoprotein lipase (EC 3.1.1.34) precursor - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 31-Mar-2000 ACCESSIONS A40570; JH0513; A60948; A29300; I55526 REFERENCE A40570 !$#authors Zechner, R.; Newman, T.C.; Steiner, E.; Breslow, J.L. !$#journal Genomics (1991) 11:62-76 !$#title The structure of the mouse lipoprotein lipase gene: a B1 !1repetitive element is inserted into the 3' untranslated !1region of the mRNA. !$#cross-references MUID:92112227; PMID:1765386 !$#accession A40570 !'##status preliminary !'##molecule_type DNA !'##residues 1-474 ##label ZEC !'##cross-references GB:M60846 REFERENCE JH0513 !$#authors Hua, X.; Enerbaeck, S.; Hudson, J.; Youkhana, K.; Gimble, !1J.M. !$#journal Gene (1991) 107:247-258 !$#title Cloning and characterization of the promoter of the murine !1lipoprotein lipase-encoding gene: structural and functional !1analysis. !$#cross-references MUID:92084117; PMID:1748295 !$#accession JH0513 !'##status translation not shown !'##molecule_type DNA !'##residues 1-29 ##label HUA !'##cross-references GB:M63335; NID:g198830; PIDN:AAC04464.1; !1PID:g2911254 REFERENCE A60948 !$#authors Semenkovich, C.F.; Chen, S.H.; Wims, M.; Luo, C.C.; Li, !1W.H.; Chan, L. !$#journal J. Lipid Res. (1989) 30:423-431 !$#title Lipoprotein lipase and hepatic lipase mRNA tissue specific !1expression, developmental regulation, and evolution. !$#cross-references MUID:89257126; PMID:2723548 !$#accession A60948 !'##status preliminary; nucleic acid sequence not shown; not compared !1with conceptual translation !'##molecule_type mRNA !'##residues 1-128,'Y',130-146,'N',148-474 ##label SEM REFERENCE A29300 !$#authors Kirchgessner, T.G.; Svenson, K.L.; Lusis, A.J.; Schotz, M.C. !$#journal J. Biol. Chem. (1987) 262:8463-8466 !$#title The sequence of cDNA encoding lipoprotein lipase. A member !1of a lipase gene family. !$#cross-references MUID:87250454; PMID:3597382 !$#accession A29300 !'##molecule_type mRNA !'##residues 9-146,'N',148-474 ##label KIR !'##cross-references GB:J03302; GB:J02740; NID:g198849; PIDN:AAA39440.1; !1PID:g387406 REFERENCE I55526 !$#authors Gimble, J.M.; Hua, X.; Youkhana, K.; Bass, H.W.; Medina, K.; !1Sullivan, M.; Greenberger, J.S.; Wang, C.S. !$#journal J. Cell. Biochem. (1992) 50:73-82 !$#title Apidogenesis in a myeloid supporting bone marrow stromal !1cell line. !$#cross-references MUID:93054974; PMID:1339460 !$#accession I55526 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-146,'N',148-184 ##label RES !'##cross-references GB:M65258; NID:g198863; PIDN:AAA39442.1; !1PID:g198864 COMMENT This enzyme is responsible for the hydrolysis of !1triglycerides into free fatty acids and glycerol. CLASSIFICATION #superfamily triacylglycerol lipase KEYWORDS carboxylic ester hydrolase; glycoprotein FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-474 #product lipoprotein lipase #status predicted #label !8MAT\ !$159,183,268 #active_site Ser, Asp, His #status predicted SUMMARY #length 474 #molecular-weight 53140 #checksum 2914 SEQUENCE /// ENTRY JH0790 #type complete TITLE lipoprotein lipase (EC 3.1.1.34) precursor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JH0790; A36127 REFERENCE JH0790 !$#authors Brault, D.; Noe, L.; Etienne, J.; Hamelin, J.; Raisonnier, !1A.; Souli, A.; Chuat, J.C.; Dugail, I.; Quignard-Boulange, !1A.; Lavau, M.; Galibert, F. !$#journal Gene (1992) 121:237-246 !$#title Sequence of rat lipoprotein lipase-encoding cDNA. !$#cross-references MUID:93077037; PMID:1339374 !$#accession JH0790 !'##molecule_type mRNA !'##residues 1-474 ##label BRA !'##cross-references GB:L03294; NID:g205214; PIDN:AAA41534.1; !1PID:g205215 !'##experimental_source testicular fat cell !'##note the authors translated the codon GCC for residue 384 as Ser, !1AAC for residue 411 as Ser, CGC for residue 416 as Ser, and !1GCT for residue 459 as Arg REFERENCE A36127 !$#authors Raynolds, M.V.; Awald, P.D.; Gordon, D.F.; !1Gutierrez-Hartmann, A.; Rule, D.C.; Wood, W.M.; Eckel, R.H. !$#journal Mol. Endocrinol. (1990) 4:1416-1422 !$#title Lipoprotein lipase gene expression in rat adipocytes is !1regulated by isoproterenol and insulin through different !1mechanisms. !$#cross-references MUID:91042645; PMID:2233752 !$#accession A36127 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 'V',337-474 ##label RAY CLASSIFICATION #superfamily triacylglycerol lipase KEYWORDS carboxylic ester hydrolase; glycoprotein; lipid metabolism; !1plasma FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-474 #product lipoprotein lipase #status predicted #label !8MAT\ !$159,183,268 #active_site Ser, Asp, His #status predicted SUMMARY #length 474 #molecular-weight 53082 #checksum 2034 SEQUENCE /// ENTRY A27053 #type complete TITLE lipoprotein lipase (EC 3.1.1.34) - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 31-Mar-2000 ACCESSIONS A27053; A34407; A26501 REFERENCE A27053 !$#authors Senda, M.; Oka, K.; Brown, W.V.; Qasba, P.K.; Furuichi, Y. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:4369-4373 !$#title Molecular cloning and sequence of a cDNA coding for bovine !1lipoprotein lipase. !$#cross-references MUID:87260809; PMID:2885834 !$#accession A27053 !'##molecule_type mRNA !'##residues 1-450 ##label SEN !'##cross-references GB:M16966; NID:g163304; PIDN:AAA30624.1; !1PID:g163305 REFERENCE A34407 !$#authors Yang, C.Y.; Gu, Z.W.; Yang, H.X.; Rohde, M.F.; Gotto Jr., !1A.M.; Pownall, H.J. !$#journal J. Biol. Chem. (1989) 264:16822-16827 !$#title Structure of bovine milk lipoprotein lipase. !$#cross-references MUID:89380314; PMID:2674142 !$#accession A34407 !'##molecule_type protein !'##residues 1-215,'F',217-450 ##label YAN REFERENCE A91178 !$#authors Bengtsson-Olivecrona, G.; Olivecrona, T.; Jornvall, H. !$#journal Eur. J. Biochem. (1986) 161:281-288 !$#title Lipoprotein lipases from cow, guinea-pig and man. Structural !1characterization and identification of protease-sensitive !1internal regions. !$#cross-references MUID:87054027; PMID:3536511 !$#accession A26501 !'##molecule_type protein !'##residues 1-28 ##label BEN CLASSIFICATION #superfamily triacylglycerol lipase KEYWORDS carboxylic ester hydrolase; glycoprotein FEATURE !$29-42,218-241, !$266-285,277-280, !$420-440 #disulfide_bonds #status experimental\ !$45,361 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$134,158,243 #active_site Ser, Asp, His #status predicted SUMMARY #length 450 #molecular-weight 50551 #checksum 9244 SEQUENCE /// ENTRY A27330 #type complete TITLE lipoprotein lipase (EC 3.1.1.34) precursor - guinea pig ORGANISM #formal_name Cavia porcellus #common_name guinea pig DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 31-Mar-2000 ACCESSIONS JS0398; A27330 REFERENCE JS0398 !$#authors Enerbaeck, S.; Bjursell, G. !$#journal Gene (1989) 84:391-397 !$#title Genomic organization of the region encoding guinea pig !1lipoprotein lipase; evidence for exon fusion and !1unconventional splicing. !$#cross-references MUID:90128283; PMID:2612912 !$#accession JS0398 !'##molecule_type DNA !'##residues 1-465 ##label EN2 !'##cross-references GB:M33381; NID:g191268; PIDN:AAA37039.1; !1PID:g553844 REFERENCE A27330 !$#authors Enerback, S.; Semb, H.; Bengtsson-Olivecrona, G.; Carlsson, !1P.; Hermansson, M.L.; Olivecrona, T.; Bjursell, G. !$#journal Gene (1987) 58:1-12 !$#title Molecular cloning and sequence analysis of cDNA encoding !1lipoprotein lipase of guinea pig. !$#cross-references MUID:88084436; PMID:3692172 !$#accession A27330 !'##molecule_type mRNA !'##residues 1-465 ##label ENE !'##cross-references GB:M15483; NID:g191285; PIDN:AAA37046.1; !1PID:g305339 GENETICS !$#introns 21/2; 73/3; 133/3; 171/1; 249/1; 330/1; 370/2; 431/2 CLASSIFICATION #superfamily triacylglycerol lipase KEYWORDS carboxylic ester hydrolase; glycoprotein; heparin binding FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-465 #product lipoprotein lipase #status experimental !8#label MPT\ !$309-317 #region heparin binding #status predicted\ !$60,376 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$149,173,258 #active_site Ser, Asp, His #status predicted\ !$149 #active_site Ser #status predicted SUMMARY #length 465 #molecular-weight 52781 #checksum 871 SEQUENCE /// ENTRY S04331 #type complete TITLE lipoprotein lipase (EC 3.1.1.34) precursor - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 28-Feb-1990 #sequence_revision 28-Feb-1990 #text_change 31-Mar-2000 ACCESSIONS S04331; A39093; S20598 REFERENCE S04331 !$#authors Cooper, D.A.; Stein, J.C.; Strieleman, P.J.; Bensadoun, A. !$#journal Biochim. Biophys. Acta (1989) 1008:92-101 !$#title Avian adipose lipoprotein lipase: cDNA sequence and !1reciprocal regulation of mRNA levels in adipose and heart. !$#cross-references MUID:89247453; PMID:2719965 !$#accession S04331 !'##molecule_type mRNA !'##residues 1-490 ##label COO !'##cross-references EMBL:X14670; NID:g63573; PIDN:CAA32800.1; !1PID:g63574 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing !'##note it is uncertain whether Met-1 or Met-7 is the initiator REFERENCE A39093 !$#authors Hoogewerf, A.J.; Bensadoun, A. !$#journal J. Biol. Chem. (1991) 266:1048-1057 !$#title Occurrence of sulfate in an asparagine-linked complex !1oligosaccharide of chicken adipose lipoprotein lipase. !$#cross-references MUID:91093211; PMID:1985932 !$#accession A39093 !'##molecule_type protein !'##residues 45-53,'X',55-66,'Q',68-69 ##label HOO !'##note sulfate was shown to be incorporated on a GlcNAc residue of a !1complex oligosaccharide at Asn-70; the other two N-linked !1glycosylation sites do not contain sulfate REFERENCE S20598 !$#authors Cooper, D.A.; Lu, S.C.; Viswanath, R.; Freiman, R.N.; !1Bensadoun, A. !$#journal Biochim. Biophys. Acta (1992) 1129:166-171 !$#title The structure and complete nucleotide sequence of the avian !1lipoprotein lipase gene. !$#cross-references MUID:92110377; PMID:1730055 !$#accession S20598 !'##status preliminary !'##molecule_type DNA !'##residues 1-376,'A',378-490 ##label CO2 !'##cross-references EMBL:X60547; NID:g62935; PIDN:CAA43037.1; !1PID:g62936 !'##note the authors translated the codon CCT for residue 46 as Phe, ACC !1for residue 75 as Tyr, and GCT for residue 377 as Pro GENETICS !$#introns 29/1; 83/3; 143/3; 181/1; 259/1; 340/1; 380/2; 441/2; 476/2 CLASSIFICATION #superfamily triacylglycerol lipase KEYWORDS carboxylic ester hydrolase; glycoprotein FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-490 #product lipoprotein lipase #status experimental !8#label MAT\ !$70,354,386 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$159,183,268 #active_site Ser, Asp, His #status predicted SUMMARY #length 490 #molecular-weight 55132 #checksum 7161 SEQUENCE /// ENTRY PSHU #type complete TITLE phospholipase A2 (EC 3.1.1.4) IB precursor [validated] - human ALTERNATE_NAMES pancreatic phospholipase A2; phosphatidylcholine 2-acylhydrolase ORGANISM #formal_name Homo sapiens #common_name man DATE 17-Mar-1987 #sequence_revision 31-Mar-1993 #text_change 08-Dec-2000 ACCESSIONS C25793; A25793; A00733; A21566 REFERENCE A25793 !$#authors Seilhamer, J.J.; Randall, T.L.; Yamanaka, M.; Johnson, L.K. !$#journal DNA (1986) 5:519-527 !$#title Pancreatic phospholipase A2: isolation of the human gene and !1cDNAs from porcine pancreas and human lung. !$#cross-references MUID:87132925; PMID:3028739 !$#accession C25793 !'##molecule_type DNA !'##residues 1-148 ##label SEI2 !'##cross-references GB:M22970 !$#accession A25793 !'##molecule_type mRNA !'##residues 1-148 ##label SEI !'##cross-references GB:M21055 !'##experimental_source lung REFERENCE A91114 !$#authors Grataroli, R.; Dijkman, R.; Dutilh, C.E.; Van der Ouderaa, !1F.; De Haas, G.H.; Figarella, C. !$#journal Eur. J. Biochem. (1982) 122:111-117 !$#title Studies on prophospholipase A2 and its enzyme from human !1pancreatic juice. Catalytic properties and sequence of the !1N-terminal region. !$#cross-references MUID:82138816; PMID:7060561 !$#accession A00733 !'##molecule_type protein !'##residues 16-22 ##label VER1 REFERENCE A90651 !$#authors Verheij, H.M.; Westerman, J.; Sternby, B.; De Haas, G.H. !$#journal Biochim. Biophys. Acta (1983) 747:93-99 !$#title The complete primary structure of phospholipase A2 from !1human pancreas. !$#cross-references MUID:83283533; PMID:6349696 !$#accession A21566 !'##molecule_type protein !'##residues 23-143,'YS',146-147 ##label VER2 GENETICS !$#gene GDB:PLA2G1B; PLA2A; PLA2; P !'##cross-references GDB:120715; OMIM:172410 !$#map_position 12q23-12qter !$#introns 12/1; 65/2; 108/1 FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; lipid degradation; !1lipid digestion; metalloprotein; pancreas; zymogen FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-22 #domain activation peptide #status experimental !8#label ACT\ !$23-148 #product phospholipase A2 IB #status experimental !8#label MAT\ !$33-99,49-146,51-67, !$66-127,73-120, !$83-113,106-118 #disulfide_bonds #status predicted\ !$50,52,54,71 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8predicted\ !$70,121 #active_site His, Asp #status predicted SUMMARY #length 148 #molecular-weight 16360 #checksum 6427 SEQUENCE /// ENTRY PSDG #type complete TITLE phospholipase A2 (EC 3.1.1.4) precursor - dog ALTERNATE_NAMES phosphatidylcholine 2-acylhydrolase ORGANISM #formal_name Canis lupus familiaris #common_name dog DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Jun-2000 ACCESSIONS S11316; A24392; JS0006 REFERENCE S11316 !$#authors Kerfelec, B.; LaForge, K.S.; Vasiloudes, P.; Puigserver, A.; !1Scheele, G.A. !$#journal Eur. J. Biochem. (1990) 190:299-304 !$#title Isolation and sequence of the canine pancreatic !1phospholipase A(2) gene. !$#cross-references MUID:90306027; PMID:2142076 !$#accession S11316 !'##molecule_type DNA !'##residues 1-146 ##label KE2 REFERENCE A93751 !$#authors Kerfelec, B.; LaForge, K.S.; Puigserver, A.; Scheele, G. !$#journal Pancreas (1986) 1:430-437 !$#title Primary structures of canine pancreatic lipase and !1phospholipase A2 messenger RNAs. !$#cross-references MUID:87175472; PMID:3562437 !$#accession A24392 !'##molecule_type mRNA !'##residues 1-146 ##label KER !'##cross-references GB:M35301; NID:g164041; PIDN:AAA30883.1; !1PID:g164042 REFERENCE A92008 !$#authors Ohara, O.; Tamaki, M.; Nakamura, E.; Tsuruta, Y.; Fujii, Y.; !1Shin, M.; Teraoka, H.; Okamoto, M. !$#journal J. Biochem. (1986) 99:733-739 !$#title Dog and rat pancreatic phospholipases A2: complete amino !1acid sequences deduced from complementary DNAs. !$#cross-references MUID:86223862; PMID:3754861 !$#accession JS0006 !'##molecule_type mRNA !'##residues 1-146 ##label OHA !'##cross-references GB:D00035; GB:N00035; NID:g217659; PIDN:BAA00023.1; !1PID:g217660 FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; lipid degradation; !1lipid digestion; metalloprotein; pancreas FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-22 #domain activation peptide #status predicted #label !8APT\ !$23-146 #product phospholipase A2 #status predicted #label !8MPT\ !$33-99,49-146,51-67, !$66-127,73-120, !$83-113,106-118 #disulfide_bonds #status predicted\ !$50,52,54,71 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8predicted\ !$70,121 #active_site His, Asp #status predicted SUMMARY #length 146 #molecular-weight 16235 #checksum 803 SEQUENCE /// ENTRY PSRT #type complete TITLE phospholipase A2 (EC 3.1.1.4) precursor - rat ALTERNATE_NAMES pancreatic phospholipase A2; phosphatidylcholine 2-acylhydrolase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 16-Jun-2000 ACCESSIONS A92008; S02147; A91987; A28617; A05322; JS0007 REFERENCE A92008 !$#authors Ohara, O.; Tamaki, M.; Nakamura, E.; Tsuruta, Y.; Fujii, Y.; !1Shin, M.; Teraoka, H.; Okamoto, M. !$#journal J. Biochem. (1986) 99:733-739 !$#title Dog and rat pancreatic phospholipases A2: complete amino !1acid sequences deduced from complementary DNAs. !$#cross-references MUID:86223862; PMID:3754861 !$#accession A92008 !'##molecule_type mRNA !'##residues 1-146 ##label OHA !'##cross-references GB:D00036; GB:N00036; NID:g220874; PIDN:BAA00024.1; !1PID:g220875 REFERENCE S02147 !$#authors Sakata, T.; Nakamura, E.; Tsuruta, Y.; Tamaki, M.; Teraoka, !1H.; Tojo, H.; Ono, T.; Okamoto, M. !$#journal Biochim. Biophys. Acta (1989) 1007:124-126 !$#title Presence of pancreatic-type phospholipase A(2) mRNA in rat !1gastric mucosa and lung. !$#cross-references MUID:89076874; PMID:2909239 !$#accession S02147 !'##molecule_type mRNA !'##residues 1-146 ##label SAK !'##cross-references EMBL:D00036; NID:g220874; PIDN:BAA00024.1; !1PID:g220875 REFERENCE A91987 !$#authors Ono, T.; Tojo, H.; Inoue, K.; Kagamiyama, H.; Yamano, T.; !1Okamoto, M. !$#journal J. Biochem. (1984) 96:785-792 !$#title Rat pancreatic phospholipase A2: purification, !1characterization, and N-terminal amino acid sequence. !$#cross-references MUID:85054750; PMID:6501264 !$#accession A91987 !'##molecule_type protein !'##residues 23-54 ##label ONO REFERENCE A28617 !$#authors Tojo, H.; Ono, T.; Kuramitsu, S.; Kagamiyama, H.; Okamoto, !1M. !$#journal J. Biol. Chem. (1988) 263:5724-5731 !$#title A phospholipase A-2 in the supernatant fraction of rat !1spleen. Its similarity to rat pancreatic phospholipase A-2. !$#cross-references MUID:88186889; PMID:3128547 !$#accession A28617 !'##molecule_type protein !'##residues 23-54 ##label TOJ !'##experimental_source spleen FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; lipid degradation; !1lipid digestion; metalloprotein; pancreas FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-22 #domain activation peptide #status predicted #label !8APT\ !$23-146 #product phospholipase A2 #status experimental #label !8MAT\ !$33-99,49-146,51-67, !$66-127,73-120, !$83-113,106-118 #disulfide_bonds #status predicted\ !$50,52,54,71 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8predicted\ !$70,121 #active_site His, Asp #status predicted SUMMARY #length 146 #molecular-weight 16424 #checksum 1851 SEQUENCE /// ENTRY PSPGA #type complete TITLE phospholipase A2 (EC 3.1.1.4) major precursor [validated] - pig ALTERNATE_NAMES pancreatic phospholipase A2; phosphatidylcholine 2-acylhydrolase ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 24-Apr-1984 #sequence_revision 30-Jun-1993 #text_change 20-Apr-2001 ACCESSIONS B25793; S30750; A60264; A00734 REFERENCE A25793 !$#authors Seilhamer, J.J.; Randall, T.L.; Yamanaka, M.; Johnson, L.K. !$#journal DNA (1986) 5:519-527 !$#title Pancreatic phospholipase A2: isolation of the human gene and !1cDNAs from porcine pancreas and human lung. !$#cross-references MUID:87132925; PMID:3028739 !$#accession B25793 !'##molecule_type mRNA !'##residues 1-146 ##label SEI !'##cross-references EMBL:M21055; NID:g164611; PIDN:AAA31101.1; !1PID:g164612 !'##experimental_source pancreas REFERENCE S30750 !$#authors de Geus, P.; van den Bergh, C.J.; Kuipers, O.; Verheij, !1H.M.; Hoekstra, W.P.M.; de Haas, G.H. !$#journal Nucleic Acids Res. (1987) 15:3743-3759 !$#title Expression of porcine pancreatic phospholipase A(2). !1Generation of active enzyme by sequence-specific cleavage of !1a hybrid protein from Escherichia coli. !$#cross-references MUID:87231066; PMID:3295782 !$#accession S30750 !'##molecule_type mRNA !'##residues 1-146 ##label DEG !'##cross-references EMBL:Y00146; NID:g2051; PIDN:CAA68341.1; PID:g2052 REFERENCE A60264 !$#authors Kuipers, O.P.; van den Bergh, C.J.; Verheij, H.M.; de Haas, !1G.H. !$#journal Adv. Exp. Med. Biol. (1990) 279:65-84 !$#title Probing the mechanism of pancreatic phospholipase A2 with !1the aid of recombinant DNA techniques. !$#cross-references MUID:91263889; PMID:2096701 !$#accession A60264 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-146 ##label KUI REFERENCE A90620 !$#authors Puijk, W.C.; Verheij, H.M.; de Haas, G.H. !$#journal Biochim. Biophys. Acta (1977) 492:254-259 !$#title The primary structure of phospholipase A-2 from porcine !1pancreas. A reinvestigation. !$#cross-references MUID:77222092; PMID:884127 !$#contents revision !$#accession A00734 !'##molecule_type protein !'##residues 16-146 ##label PUI REFERENCE A90579 !$#authors de Haas, G.H.; Slotboom, A.J.; Bonsen, P.P.M.; !1Nieuwenhuizen, W.; van Deenen, L.L.M.; Maroux, S.; Dlouha, !1V.; Desnuelle, P. !$#journal Biochim. Biophys. Acta (1970) 221:54-61 !$#title Studies on phospholipase A and its zymogen from porcine !1pancreas. II. The assignment of the position of the six !1disulfide bridges. !$#cross-references MUID:71014236; PMID:4919729 !$#contents annotation; disulfide bonds REFERENCE A50305 !$#authors Dijkstra, B.W.; Renetseder, R.; Kalk, K.H.; Hol, W.G.J.; !1Drenth, J. !$#submission submitted to the Brookhaven Protein Data Bank, June 1983 !$#cross-references PDB:1P2P !$#contents annotation; X-ray crystallography, 2.6 angstroms REFERENCE A92899 !$#authors Dijkstra, B.W.; Renetseder, R.; Kalk, K.H.; Hol, W.G.J.; !1Drenth, J. !$#journal J. Mol. Biol. (1983) 168:163-179 !$#title Structure of porcine pancreatic phospholipase A-2 at 2.6 !1angstrom resolution and comparison with bovine phospholipase !1A-2. !$#cross-references MUID:83268704; PMID:6876174 !$#contents annotation; X-ray crystallography, 2.6 angstroms; active and !1binding sites REFERENCE A60719 !$#authors van den Bergh, C.J.; Slotboom, A.J.; Verheij, H.M.; de Haas, !1G.H. !$#journal J. Cell. Biochem. (1989) 39:379-390 !$#title The role of Asp-49 and other conserved amino acids in !1phospholipases A2 and their importance for enzymatic !1activity. !$#cross-references MUID:89255682; PMID:2722967 !$#contents annotation REFERENCE A50680 !$#authors Finzel, B.C.; Ohlendorf, D.H.; Weber, P.C.; Salemme, F.R. !$#submission submitted to the Brookhaven Protein Data Bank, October 1991 !$#cross-references PDB:4P2P !$#contents annotation; X-ray crystallography, 2.4 angstroms, residues !123-146 REFERENCE A58515 !$#authors Finzel, B.C.; Ohlendorf, D.H.; Weber, P.C.; Salemme, F.R. !$#journal Acta Crystallogr. B (1991) 47:558-559 !$#title An independent crystallographic refinement of porcine !1phospholipase A2 at 2.4 angstroms resolution. !$#cross-references MUID:92029796; PMID:1930837 !$#contents annotation; X-ray crystallography, 2.4 angstroms FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; lipid degradation; !1lipid digestion; metalloprotein; pancreas; pyroglutamic acid FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-22 #domain activation peptide #status experimental !8#label APT\ !$23-146 #product phospholipase A2 major #status experimental !8#label MAT\ !$16 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$33-99,49-146,51-67, !$66-127,73-120, !$83-113,106-118 #disulfide_bonds #status experimental\ !$50,52,54,71 #binding_site calcium, high affinity (Tyr, Gly, Gly, !8Asp) #status experimental\ !$70,121 #active_site His, Asp #status experimental\ !$93,94,114 #binding_site calcium, low affinity (Glu, Ser, Glu) !8#status predicted SUMMARY #length 146 #molecular-weight 16279 #checksum 335 SEQUENCE /// ENTRY PSPGA2 #type complete TITLE phospholipase A2 (EC 3.1.1.4) minor - pig (tentative sequence) ALTERNATE_NAMES pancreatic phospholipase A2 minor isozyme; phosphatidylcholine 2-acylhydrolase ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 02-Jul-1998 ACCESSIONS A00735 REFERENCE A00735 !$#authors Puijk, W.C.; Verheij, H.M.; Wietzes, P.; de Haas, G.H. !$#journal Biochim. Biophys. Acta (1979) 580:411-415 !$#title The amino acid sequence of the phospholipase A-2 isoenzyme !1from porcine pancreas. !$#cross-references MUID:80088382; PMID:518908 !$#accession A00735 !'##molecule_type protein !'##residues 1-124 ##label PUI !'##experimental_source pancreas COMMENT This isozyme constitutes about 5% of the pancreatic !1phospholipase. COMMENT Phospholipase A2 occurs in virtually every mammalian tissue !1that has been examined. FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; lipid degradation; !1lipid digestion; metalloprotein; pancreas FEATURE !$11-77,27-124,29-45, !$44-105,51-98,61-91, !$84-96 #disulfide_bonds #status experimental\ !$28,30,32,49 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8experimental\ !$48,99 #active_site His, Asp #status experimental SUMMARY #length 124 #molecular-weight 13968 #checksum 930 SEQUENCE /// ENTRY PSBOA #type complete TITLE phospholipase A2 (EC 3.1.1.4) precursor [validated] - bovine ALTERNATE_NAMES pancreatic phospholipase A2; phosphatidylcholine 2-acylhydrolase ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Nov-1980 #sequence_revision 31-Mar-1993 #text_change 15-Sep-2000 ACCESSIONS A27508; A94661; A91252; A00736 REFERENCE A27508 !$#authors Tanaka, T.; Kimura, S.; Ota, Y. !$#journal Nucleic Acids Res. (1987) 15:3178 !$#title Sequence of a cDNA coding for bovine pancreatic !1phospholipase A2. !$#cross-references MUID:87174835; PMID:3562249 !$#accession A27508 !'##molecule_type mRNA !'##residues 1-145 ##label TAN !'##cross-references EMBL:Y00120; NID:g634; PIDN:CAA68303.1; PID:g635 REFERENCE A94661 !$#authors Dutilh, C.E.; Van Doren, P.J.; Verheul, F.E.A.M.; De Haas, !1G.H. !$#journal Eur. J. Biochem. (1975) 53:91-97 !$#title Isolation and properties of prophospholipase A2 from ox and !1sheep pancreas. !$#accession A94661 !'##molecule_type protein !'##residues 16-22 ##label DUT REFERENCE A91252 !$#authors Fleer, E.A.M.; Verheij, H.M.; de Haas, G.H. !$#journal Eur. J. Biochem. (1978) 82:261-269 !$#title The primary structure of bovine pancreatic phospholipase A2. !$#cross-references MUID:78084411; PMID:620674 !$#accession A91252 !'##molecule_type protein !'##residues 23-143,'N',145 ##label FLE REFERENCE A92853 !$#authors Dijkstra, B.W.; Drenth, J.; Kalk, K.H.; Vandermaelen, P.J. !$#journal J. Mol. Biol. (1978) 124:53-60 !$#title Three-dimensional structure and disulfide bond connections !1in bovine pancreatic phospholipase A2. !$#cross-references MUID:79050564; PMID:712836 !$#contents annotation; X-ray crystallography, 2.4 angstroms; disulfide !1bonds REFERENCE A93243 !$#authors Dijkstra, B.W.; Drenth, J.; Kalk, K.H. !$#journal Nature (1981) 289:604-606 !$#title Active site and catalytic mechanism of phospholipase A2. !$#cross-references MUID:81123082; PMID:7464926 !$#contents annotation; X-ray crystallography, 1.7 angstroms; active !1site; catalytic mechanism REFERENCE A50406 !$#authors Dijkstra, B.W.; van Nes, G.J.H.; Kalk, K.H.; Brandenburg, !1N.P.; Hol, W.G.J.; Drenth, J. !$#submission submitted to the Brookhaven Protein Data Bank, June 1981 !$#cross-references PDB:2BP2 !$#contents annotation; X-ray crystallography, 3.0 angstroms, residues !123-143,'N',145 !$#note pancreas, phospholipase A2 precursor REFERENCE A58516 !$#authors Dijkstra, B.W.; van Nes, G.J.H.; Kalk, K.H.; Brandenburg, !1N.P.; Hol, W.G.J.; Drenth, J. !$#journal Acta Crystallogr. (1982) B38:793-799 !$#title The structure of bovine pancreatic prophospholipase A2 at !13.0 angstroms resolution. !$#contents annotation; X-ray crystallography, 3.0 angstroms REFERENCE A51455 !$#authors Sundaralingam, M. !$#submission submitted to the Brookhaven Protein Data Bank, January 1992 !$#cross-references PDB:2BPP !$#contents annotation; X-ray crystallography, 1.8 angstroms, residues !123-143,'N',145 !$#note recombinant form expressed in Escherichia coli REFERENCE A58513 !$#authors Noel, J.P.; Bingman, C.A.; Deng, T.; Dupureur, C.M.; !1Hamilton, K.J.; Jiang, R.T.; Kwak, J.G.; Sekharudu, C.; !1Sundaralingam, M.; Tsai, M.D. !$#journal Biochemistry (1991) 30:11801-11811 !$#title Phospholipase A2 engineering. X-ray structural and !1functional evidence for the interaction of lysine-56 with !1substrates. !$#cross-references MUID:92089090; PMID:1751497 !$#contents annotation; X-ray crystallography, 1.8 angstroms FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; lipid degradation; !1lipid digestion; metalloprotein; pancreas; pyroglutamic acid FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-145 #product prophospholipase A2 #status experimental !8#label PRO\ !$16-22 #domain activation peptide #status experimental !8#label APT\ !$23-145 #product phospholipase A2 #status experimental #label !8MAT\ !$16 #modified_site pyrrolidone carboxylic acid (Gln) (in !8precursor form) #link PRO #status experimental\ !$33-99,49-145,51-67, !$66-127,73-120, !$83-113,106-118 #disulfide_bonds #status experimental\ !$50,52,54,71 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8experimental\ !$70,121 #active_site His, Asp #status experimental SUMMARY #length 145 #molecular-weight 16016 #checksum 8059 SEQUENCE /// ENTRY PSHOA #type complete TITLE phospholipase A2 (EC 3.1.1.4) precursor - horse (tentative sequence) ALTERNATE_NAMES pancreatic phospholipase A2; phosphatidylcholine 2-acylhydrolase ORGANISM #formal_name Equus caballus #common_name domestic horse DATE 24-Apr-1984 #sequence_revision 03-Aug-1984 #text_change 31-Mar-2000 ACCESSIONS A90615; A92198; A90651; A00737 REFERENCE A90615 !$#authors Evenberg, A.; Meyer, H.; Verheij, H.M.; de Haas, G.H. !$#journal Biochim. Biophys. Acta (1977) 491:265-274 !$#title Isolation and properties of prophospholipase A-2 and !1phospholipase A-2 from horse pancreas and horse pancreatic !1juice. !$#cross-references MUID:77134902; PMID:849461 !$#accession A90615 !'##molecule_type protein !'##residues 1-7 ##label EVE !'##note a second form, lacking residues 1 and 2, was also found REFERENCE A92198 !$#authors Evenberg, A.; Meyer, H.; Gaastra, W.; Verheij, H.M.; de !1Haas, G.H. !$#journal J. Biol. Chem. (1977) 252:1189-1196 !$#title Amino acid sequence of phospholipase A-2 from horse !1pancreas. !$#cross-references MUID:77118587; PMID:838712 !$#contents active site !$#accession A92198 !'##molecule_type protein !'##residues 8-131 ##label EV2 REFERENCE A90651 !$#authors Verheij, H.M.; Westerman, J.; Sternby, B.; De Haas, G.H. !$#journal Biochim. Biophys. Acta (1983) 747:93-99 !$#title The complete primary structure of phospholipase A2 from !1human pancreas. !$#cross-references MUID:83283533; PMID:6349696 !$#accession A90651 !'##molecule_type protein !'##residues 1-132 ##label VER COMMENT Phospholipase A2 occurs in virtually every mammalian tissue !1that has been examined. FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; lipid degradation; !1lipid digestion; metalloprotein; pancreas FEATURE !$1-7 #domain activation peptide #status experimental !8#label APT\ !$8-132 #product phospholipase A2 #status experimental #label !8MPT\ !$18-84,34-131,36-52, !$51-112,58-105, !$68-98,91-103 #disulfide_bonds #status predicted\ !$35,37,39,56 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8predicted\ !$55,106 #active_site His, Asp #status predicted SUMMARY #length 132 #molecular-weight 14694 #checksum 9251 SEQUENCE /// ENTRY S34049 #type complete TITLE phospholipase A2 (EC 3.1.1.4) precursor, gastric and pancreatic [validated] - guinea pig ALTERNATE_NAMES pancreatic phospholipase A2; phosphatidylcholine 2-acylhydrolase ORGANISM #formal_name Cavia porcellus #common_name guinea pig DATE 18-Aug-2000 #sequence_revision 18-Aug-2000 #text_change 18-Aug-2000 ACCESSIONS S34049; S34046; S34048; S34047 REFERENCE S34049 !$#authors Ying, Z.; Tojo, H.; Nonaka, Y.; Okamoto, M. !$#journal Eur. J. Biochem. (1993) 215:91-97 !$#title Cloning and expression of phospholipase A(2) from guinea pig !1gastric mucosa, its induction by carbachol and secretion in !1vivo. !$#cross-references MUID:93345504; PMID:8344290 !$#accession S34049 !'##molecule_type mRNA !'##residues 1-146 ##label YIN !'##cross-references GB:D00740; NID:g398128; PIDN:BAA00640.1; !1PID:g398129 REFERENCE S34046 !$#authors Tojo, H.; Ying, Z.; Okamoto, M. !$#journal Eur. J. Biochem. (1993) 215:81-90 !$#title Purification and characterization of guinea pig gastric !1phospholipase A(2) of the pancreatic type. !$#cross-references MUID:93345502; PMID:8344288 !$#accession S34046 !'##status preliminary !'##molecule_type protein !'##residues 23-63 ##label TOJ !'##experimental_source gastric mucosa !$#accession S34048 !'##status preliminary !'##molecule_type protein !'##residues 23-24,'X',26-32,'X',34 ##label TO2 !'##experimental_source pancreas COMMENT In this species phospholipase activity is high in gastric !1mucosa and jueic and low in the pancreas. The enzymes !1isolated from these sources appear to be identical. FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; gastric juice; lipid !1degradation; lipid digestion; metalloprotein; pancreas; !1stomach; zymogen FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-22 #domain activation peptide #status predicted #label !8ACT\ !$23-146 #product phospholipase A2 #status experimental #label !8MAT\ !$33-99,49-146,51-67, !$66-127,73-120, !$83-113,106-118 #disulfide_bonds #status predicted\ !$50,52,54,71 #binding_site calcium (Phe, Gly, Gly, Asp) #status !8predicted\ !$70,121 #active_site His, Asp #status predicted SUMMARY #length 146 #molecular-weight 16187 #checksum 9989 SEQUENCE /// ENTRY PSHUYF #type complete TITLE phospholipase A2 (EC 3.1.1.4) IIA precursor [validated] - human ALTERNATE_NAMES phosphatidylcholine 2-acylhydrolase; placental PLA2; platelet-secreted PLA2; synovial fluid phospholipase A2 ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 15-Sep-2000 ACCESSIONS A32862; B32862; A60266; A32847; A60263; A31350; PT0056; !1A32913; A60265; A61201; A61634 REFERENCE A32862 !$#authors Kramer, R.M.; Hession, C.; Johansen, B.; Hayes, G.; McGray, !1P.; Chow, E.P.; Tizard, R.; Pepinsky, R.B. !$#journal J. Biol. Chem. (1989) 264:5768-5775 !$#title Structure and properties of a human non-pancreatic !1phospholipase A-2. !$#cross-references MUID:89174633; PMID:2925633 !$#accession A32862 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-144 ##label KRA !$#accession B32862 !'##molecule_type protein !'##residues 21-39 ##label KR2 !'##note this protein was also detected in platelets REFERENCE A60266 !$#authors Kramer, R.M.; Johansen, B.; Hession, C.; Pepinsky, R.B. !$#journal Adv. Exp. Med. Biol. (1990) 275:35-53 !$#title Structure and properties of a secretable phospholipase A-2 !1from human platelets. !$#cross-references MUID:91050834; PMID:2239446 !$#accession A60266 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-144 ##label KR3 REFERENCE A32847 !$#authors Seilhamer, J.J.; Pruzanski, W.; Vadas, P.; Plant, S.; !1Miller, J.A.; Kloss, J.; Johnson, L.K. !$#journal J. Biol. Chem. (1989) 264:5335-5338 !$#title Cloning and recombinant expression of phospholipase A-2 !1present in rheumatoid arthritic synovial fluid. !$#cross-references MUID:89174566; PMID:2925608 !$#accession A32847 !'##molecule_type mRNA !'##residues 1-144 ##label SEI !'##cross-references GB:J04704; EMBL:M22430; NID:g190888; !1PIDN:AAA36550.1; PID:g190889 REFERENCE A60263 !$#authors Crowl, R.; Stoner, C.; Stoller, T.; Pan, Y.C.; Conroy, R. !$#journal Adv. Exp. Med. Biol. (1990) 279:173-184 !$#title Isolation and characterization of cDNA clones from human !1placenta coding for phospholipase A-2. !$#cross-references MUID:91263879; PMID:1710870 !$#accession A60263 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-144 ##label CRO REFERENCE A31350 !$#authors Lai, C.Y.; Wada, K. !$#journal Biochem. Biophys. Res. Commun. (1988) 157:488-493 !$#title Phospholipase A-2 from human synovial fluid: purification !1and structural homology to the placental enzyme. !$#cross-references MUID:89076274; PMID:3202859 !$#accession A31350 !'##molecule_type protein !'##residues 21-33 ##label LAI REFERENCE PT0056 !$#authors Hara, S.; Kudo, I.; Matsuta, K.; Miyamoto, T.; Inoue, K. !$#journal J. Biochem. (1988) 104:326-328 !$#title Amino acid composition and NH2-terminal amino acid sequence !1of human phospholipase A2 purified from rheumatoid synovial !1fluid. !$#cross-references MUID:89197814; PMID:3240982 !$#accession PT0056 !'##molecule_type protein !'##residues 21-46,'X',48-54 ##label HAR REFERENCE A32913 !$#authors Kanda, A.; Ono, T.; Yoshida, N.; Tojo, H.; Okamoto, M. !$#journal Biochem. Biophys. Res. Commun. (1989) 163:42-48 !$#title The primary structure of a membrane-associated phospholipase !1A-2 from human spleen. !$#cross-references MUID:89374261; PMID:2775276 !$#accession A32913 !'##molecule_type protein !'##residues 21-144 ##label KAN REFERENCE A60265 !$#authors Parks, T.P.; Lukas, S.; Hoffman, A.F. !$#journal Adv. Exp. Med. Biol. (1990) 275:55-81 !$#title Purification and characterization of a phospholipase A-2 !1from human osteoarthritic synovial fluid. !$#cross-references MUID:91050835; PMID:2146857 !$#accession A60265 !'##molecule_type protein !'##residues 21-45,'X' ##label PAR REFERENCE A61201 !$#authors Recklies, A.D.; White, C. !$#journal Arthritis Rheum. (1991) 34:1106-1115 !$#title Phospholipase A-2 is a major component of the !1salt-extractable pool of matrix proteins in adult human !1articular cartilage. !$#cross-references MUID:92029121; PMID:1930329 !$#accession A61201 !'##molecule_type protein !'##residues 21-40 ##label REC !'##experimental_source adult articular cartilage REFERENCE A61634 !$#authors Green, J.A.; Smith, G.M.; Buchta, R.; Lee, R.; Ho, K.Y.; !1Rajkovic, I.A.; Scott, K.F. !$#journal Inflammation (1991) 15:355-366 !$#title Circulating phospholipase A-2 activity associated with !1sepsis and septic shock is indistinguishable from that !1associated with rheumatoid arthritis. !$#cross-references MUID:92098137; PMID:1757123 !$#accession A61634 !'##molecule_type protein !'##residues 21-44 ##label GRE REFERENCE A51043 !$#authors Wery, J.P.; Schevitz, R.W.; Clawson, D.K.; Bobbitt, J.L.; !1Dow, E.R.; Gamboa, G.; Goodson Jr., T.; Hermann, R.B.; !1Kramer, R.M.; McClure, D.B.; Mihelich, E.D.; Putnam, J.E.; !1Sharp, J.D.; Stark, D.H.; Teater, C.; Warrick, M.W.; Jones, !1N.D. !$#submission submitted to the Brookhaven Protein Data Bank, May 1992 !$#cross-references PDB:1BBC !$#contents annotation; X-ray crystallography, 2.2 angstroms, residues !121-144 REFERENCE A58514 !$#authors Wery, J.P.; Schevitz, R.W.; Clawson, D.K.; Bobbitt, J.L.; !1Dow, E.R.; Gamboa, G.; Goodson Jr., T.; Hermann, R.B.; !1Kramer, R.M.; McClure, D.B.; Mihelich, E.D.; Putnam, J.E.; !1Sharp, J.D.; Stark, D.H.; Teater, C.; Warrick, M.W.; Jones, !1N.D. !$#journal Nature (1991) 352:79-82 !$#title Structure of recombinant human rheumatoid arthritic synovial !1fluid phospholipase A2 at 2.2 angstroms resolution. !$#cross-references MUID:91287826; PMID:2062381 !$#contents annotation; X-ray crystallography GENETICS !$#gene GDB:PLA2G2A; PLA2B; PLA2L !'##cross-references GDB:120296; OMIM:172411 !$#map_position 1p36.1-1p35 !$#introns 14/1; 62/2; 98/1 FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; extracellular protein; !1lipid degradation; lipid digestion; membrane protein; !1metalloprotein; platelet FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-144 #product phospholipase A2 IIA #status experimental !8#label MAT\ !$46-137,48-64, !$63-117,69-144, !$70-110,79-103, !$97-108 #disulfide_bonds #status experimental\ !$47,49,51,68 #binding_site calcium (His, Gly, Gly, Asp) #status !8predicted\ !$67,111 #active_site His, Asp #status predicted SUMMARY #length 144 #molecular-weight 16083 #checksum 4388 SEQUENCE /// ENTRY PSNJ3K #type complete TITLE phospholipase A2 (EC 3.1.1.4) III - monocled cobra ALTERNATE_NAMES phosphatidylcholine 2-acylhydrolase ORGANISM #formal_name Naja naja kaouthia, Naja naja siamensis #common_name monocled cobra DATE 31-Mar-1992 #sequence_revision 14-Feb-1997 #text_change 14-Feb-1997 ACCESSIONS B00739; A00739 REFERENCE A00739 !$#authors Joubert, F.J.; Taljaard, N. !$#journal Eur. J. Biochem. (1980) 112:493-499 !$#title Purification, some properties and amino-acid sequences of !1two phospholipases A (CM-II and CM-III) from Naja naja !1kaouthia venom. !$#cross-references MUID:81114211; PMID:7460933 !$#accession B00739 !'##molecule_type protein !'##residues 1-70,'SC',73-119 ##label JOU !'##note the sequences in Table 9 and Figure 4 disagree with the !1sequence in Figure 5; the sequence of Figure 5, which agrees !1with the alignment of related sequences, is shown FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; lipid degradation; !1metalloprotein; presynaptic neurotoxin; venom FEATURE !$4,67 #binding_site micellar substrate (Gln, Tyr) #status !8predicted\ !$11-71,26-118,28-44, !$43-99,50-92,60-85, !$78-90 #disulfide_bonds #status predicted\ !$27,29,31,48 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8predicted\ !$47,93 #active_site His, Asp #status predicted SUMMARY #length 119 #molecular-weight 13271 #checksum 7159 SEQUENCE /// ENTRY PSNJAF #type complete TITLE phospholipase A2 (EC 3.1.1.4) precursor [validated] - Chinese cobra ALTERNATE_NAMES phosphatidylcholine 2-acylhydrolase ORGANISM #formal_name Naja naja atra #common_name Chinese cobra DATE 29-Jun-1981 #sequence_revision 31-Jan-1997 #text_change 15-Sep-2000 ACCESSIONS JC2137; I51017; A00740; S38512 REFERENCE JC2137 !$#authors Pan, F.M.; Yeh, M.S.; Chang, W.C.; Hung, C.C.; Chiou, S.H. !$#journal Biochem. Biophys. Res. Commun. (1994) 199:969-976 !$#title Sequence analysis and expression of phospholipase A2 from !1Taiwan cobra. !$#cross-references MUID:94183285; PMID:7510963 !$#accession JC2137 !'##molecule_type mRNA !'##residues 1-146 ##label PAN1 !'##cross-references EMBL:X73225; NID:g395191; PIDN:CAA51694.1; !1PID:g395192 !'##experimental_source venom gland REFERENCE I51017 !$#authors Pan, F.M.; Chang, W.C.; Chiou, S.H. !$#journal Biochem. Mol. Biol. Int. (1994) 33:187-194 !$#title cDNA and protein sequences coding for the precursor of !1phospholipase A2 from Taiwan cobra, Naja naja atra. !$#cross-references MUID:94362505; PMID:7521702 !$#accession I51017 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-21,'S',23-75,'H',77-90,'S',92-146 ##label PAN2 !'##cross-references EMBL:X77755; NID:g456270; PIDN:CAA54802.1; !1PID:g558355 REFERENCE A00740 !$#authors Tsai, I.H.; Wu, S.H.; Lo, T.B. !$#journal Toxicon (1981) 19:141-152 !$#title Complete amino acid sequence of a phospholipase A-2 from the !1venom of Naja naja atra (Taiwan cobra). !$#cross-references MUID:81177953; PMID:7222082 !$#accession A00740 !'##molecule_type protein !'##residues 28-110,'CA',113-133,'D',135,'D',137-139,'N',141-146,'E' !1##label TSA REFERENCE S38512 !$#authors Chang, L.S.; Kuo, K.W.; Chang, C.C. !$#journal Biochim. Biophys. Acta (1993) 1202:216-220 !$#title Identification of functional involvement of tryptophan !1residues in phospholipase A(2) from Naja naja atra (Taiwan !1cobra) snake venom. !$#cross-references MUID:94002252; PMID:8399382 !$#accession S38512 !'##molecule_type protein !'##residues 44-54;84-92 ##label CHA !'##note sequence 1a in Table I has an extra Trp and an incorrect count !1as compared with sequences 3a, 5b, 4a, and 6b; it has been !1omitted !'##note Trp-45 is implicated in substrate binding REFERENCE A51344 !$#authors Scott, D.L.; Otwinowski, Z.; Sigler, P.B. !$#submission submitted to the Brookhaven Protein Data Bank, September !11992 !$#cross-references PDB:1POA !$#contents annotation; X-ray crystallography, 1.5 angstroms, residues !128-133,'D',135,'D',137-139,'N',141-145 REFERENCE A58470 !$#authors White, S.P.; Scott, D.L.; Otwinowski, Z.; Gelb, M.H.; !1Sigler, P.B. !$#journal Science (1990) 250:1560-1563 !$#title Crystal structure of cobra-venom phospholipase A2 in a !1complex with a transition-state analogue. !$#cross-references MUID:91111080; PMID:2274787 !$#contents annotation; X-ray crystallography, 2.0 angstroms COMMENT Like most acidic phospholipases, this protein is not !1neurotoxic. GENETICS !$#gene PLA2 FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; lipid degradation; !1metalloprotein; venom FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-146 #product phospholipase A2 #status experimental #label !8MAT\ !$31,94 #binding_site micellar substrate (Gln, Tyr) #status !8predicted\ !$38-98,53-145,55-71, !$70-126,77-119, !$87-112,105-117 #disulfide_bonds #status experimental\ !$54,56,58,75 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8predicted\ !$74 #active_site His #status experimental\ !$120 #active_site Asp #status predicted SUMMARY #length 146 #molecular-weight 16013 #checksum 1120 SEQUENCE /// ENTRY PSNJ2K #type complete TITLE phospholipase A2 (EC 3.1.1.4) II - monocled cobra ALTERNATE_NAMES phosphatidylcholine 2-acylhydrolase ORGANISM #formal_name Naja naja kaouthia, Naja naja siamensis #common_name monocled cobra DATE 01-Sep-1981 #sequence_revision 01-Sep-1981 #text_change 26-Feb-1999 ACCESSIONS A00739; A61011 REFERENCE A00739 !$#authors Joubert, F.J.; Taljaard, N. !$#journal Eur. J. Biochem. (1980) 112:493-499 !$#title Purification, some properties and amino-acid sequences of !1two phospholipases A (CM-II and CM-III) from Naja naja !1kaouthia venom. !$#cross-references MUID:81114211; PMID:7460933 !$#accession A00739 !'##molecule_type protein !'##residues 1-119 ##label JOU REFERENCE A61011 !$#authors Lo, C.H.; Chiou, S.H. !$#journal J. Chromatogr. (1990) 530:129-136 !$#title Simple fractionation of phospholipase A-2 analogues from !1snake venom by high-performance liquid chromatography. !$#cross-references MUID:91116028; PMID:2277102 !$#accession A61011 !'##molecule_type protein !'##residues 1-20 ##label LOA FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; lipid degradation; !1metalloprotein; presynaptic neurotoxin; venom FEATURE !$4,67 #binding_site micellar substrate (Gln, Tyr) #status !8predicted\ !$11-71,26-118,28-44, !$43-99,50-92,60-85, !$78-90 #disulfide_bonds #status predicted\ !$27,29,31,48 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8predicted\ !$47,93 #active_site His, Asp #status predicted SUMMARY #length 119 #molecular-weight 13455 #checksum 7067 SEQUENCE /// ENTRY PSRIA #type complete TITLE phospholipase A2 (EC 3.1.1.4) - ringhals ALTERNATE_NAMES phosphatidylcholine 2-acylhydrolase ORGANISM #formal_name Hemachatus haemachatus, Sepedon haemachatus #common_name ringhals DATE 29-Jul-1981 #sequence_revision 29-Jul-1981 #text_change 28-Feb-1997 ACCESSIONS A00738 REFERENCE A91228 !$#authors Joubert, F.J. !$#journal Eur. J. Biochem. (1975) 52:539-554 !$#title Hemachatus haemachatus (ringhals) venom. Purification, some !1properties and amino-acid sequence of phospholipase A !1(fraction DE-I). !$#cross-references MUID:77245910; PMID:1236145 !$#accession A00738 !'##molecule_type protein !'##residues 1-119 ##label JOU !'##note two forms of phospholipase A2 are found in ringhals venom; the !1sequence shown is designated fraction DE-I by the author REFERENCE A94312 !$#authors Yang, C.C.; King, K. !$#journal Toxicon (1980) 18:529-547 !$#title Chemical modification of the histidine residue in !1phospholipase A-2 from the Hemachatus haemachatus snake !1venom. !$#cross-references MUID:81177921; PMID:7222060 !$#contents annotation; active site !$#note enzymatic activity and toxicity are lost upon alkylation of !1His-47. Calcium ion markedly slows the inactivation FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; lipid degradation; !1metalloprotein; presynaptic neurotoxin; venom FEATURE !$4,67 #binding_site micellar substrate (Gln, Tyr) #status !8predicted\ !$11-71,26-118,28-44, !$43-99,50-92,60-85, !$78-90 #disulfide_bonds #status predicted\ !$27,29,31,48 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8predicted\ !$47 #active_site His #status experimental\ !$93 #active_site Asp #status predicted SUMMARY #length 119 #molecular-weight 13519 #checksum 7152 SEQUENCE /// ENTRY PSNJ1W #type complete TITLE phospholipase A2 (EC 3.1.1.4) I - forest cobra ALTERNATE_NAMES phosphatidylcholine 2-acylhydrolase ORGANISM #formal_name Naja melanoleuca #common_name forest cobra, black-lipped cobra DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 14-Feb-1997 ACCESSIONS A00741 REFERENCE A90601 !$#authors Joubert, F.J. !$#journal Biochim. Biophys. Acta (1975) 379:345-359 !$#title Naja melanoleuca (forest cobra) venom. The amino acid !1sequence of phospholipase A, fractions De-I and DE-II. !$#cross-references MUID:75128076; PMID:1122292 !$#accession A00741 !'##molecule_type protein !'##residues 1-118 ##label JOU !'##note see note for reference A00739 in PSNJ3K REFERENCE A90599 !$#authors Joubert, F.J.; van der Walt, S.J. !$#journal Biochim. Biophys. Acta (1975) 379:317-328 !$#title Naja melanoleuca (forest cobra) venom. Purification and some !1properties of phospholipases A. !$#cross-references MUID:75128074; PMID:1122290 !$#contents annotation; presence of disulfide bonds FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; lipid degradation; !1metalloprotein; presynaptic neurotoxin; venom FEATURE !$4,67 #binding_site micellar substrate (Gln, Tyr) #status !8predicted\ !$11-72,26-117,28-44, !$43-98,50-91,60-84, !$78-89 #disulfide_bonds #status predicted\ !$27,29,31,48 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8predicted\ !$47,92 #active_site His, Asp #status predicted SUMMARY #length 118 #molecular-weight 13473 #checksum 6679 SEQUENCE /// ENTRY PSNJ3W #type complete TITLE phospholipase A2 (EC 3.1.1.4) III - forest cobra ALTERNATE_NAMES phosphatidylcholine 2-acylhydrolase ORGANISM #formal_name Naja melanoleuca #common_name forest cobra, black-lipped cobra DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 14-Feb-1997 ACCESSIONS A90600; A00742 REFERENCE A90600 !$#authors Joubert, F.J. !$#journal Biochim. Biophys. Acta (1975) 379:329-344 !$#title Naja melanoleuca (forest cobra) venom. The amino acid !1sequence of phospholipase A, fraction DE-III. !$#cross-references MUID:75128075; PMID:1122291 !$#accession A90600 !'##molecule_type protein !'##residues 1-119 ##label JOU !'##note 104-Thr and 106-Asn were also found !'##note see note for reference A00739 in PSNJ3K FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; lipid degradation; !1metalloprotein; presynaptic neurotoxin; venom FEATURE !$4,67 #binding_site micellar substrate (Gln, Tyr) #status !8predicted\ !$11-72,26-118,28-44, !$43-99,50-92,60-85, !$79-90 #disulfide_bonds #status predicted\ !$27,29,31,48 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8predicted\ !$47,93 #active_site His, Asp #status predicted SUMMARY #length 119 #molecular-weight 13360 #checksum 7108 SEQUENCE /// ENTRY PSNJ2W #type complete TITLE phospholipase A2 (EC 3.1.1.4) II - forest cobra ALTERNATE_NAMES phosphatidylcholine 2-acylhydrolase ORGANISM #formal_name Naja melanoleuca #common_name forest cobra, black-lipped cobra DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 14-Feb-1997 ACCESSIONS A90601; A00742 REFERENCE A90601 !$#authors Joubert, F.J. !$#journal Biochim. Biophys. Acta (1975) 379:345-359 !$#title Naja melanoleuca (forest cobra) venom. The amino acid !1sequence of phospholipase A, fractions De-I and DE-II. !$#cross-references MUID:75128076; PMID:1122292 !$#accession A90601 !'##molecule_type protein !'##residues 1-119 ##label JOU !'##note 104-Pro and 106-Ile were also found !'##note see note for reference A00739 in PSNJ3K FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; lipid degradation; !1metalloprotein; presynaptic neurotoxin; venom FEATURE !$4,67 #binding_site micellar substrate (Gln, Tyr) #status !8predicted\ !$11-72,26-118,28-44, !$43-99,50-92,60-85, !$79-90 #disulfide_bonds #status predicted\ !$27,29,31,48 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8predicted\ !$47,93 #active_site His, Asp #status predicted SUMMARY #length 119 #molecular-weight 13427 #checksum 7888 SEQUENCE /// ENTRY PSNJ1M #type complete TITLE phospholipase A2 (EC 3.1.1.4) I - Mozambique cobra ALTERNATE_NAMES phosphatidylcholine 2-acylhydrolase ORGANISM #formal_name Naja mossambica mossambica #common_name Mozambique cobra DATE 30-Nov-1980 #sequence_revision 30-Nov-1980 #text_change 28-Feb-1997 ACCESSIONS A00743 REFERENCE A90623 !$#authors Joubert, F.J. !$#journal Biochim. Biophys. Acta (1977) 493:216-227 !$#title Naja mossambica mossambica venom. Purification, some !1properties and the amino acid sequences of three !1phospholipases A (CM-I, CM-II and CM-III). !$#cross-references MUID:77222126; PMID:880314 !$#accession A00743 !'##molecule_type protein !'##residues 1-118 ##label JOU FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; lipid degradation; !1metalloprotein; presynaptic neurotoxin; venom FEATURE !$4,66 #binding_site micellar substrate (Gln, Tyr) #status !8predicted\ !$11-70,26-117,28-44, !$43-98,50-91,59-84, !$77-89 #disulfide_bonds #status predicted\ !$27,29,31,48 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8predicted\ !$47,92 #active_site His, Asp #status predicted SUMMARY #length 118 #molecular-weight 13219 #checksum 6959 SEQUENCE /// ENTRY PSNJ2M #type complete TITLE phospholipase A2 (EC 3.1.1.4) II - Mozambique cobra ALTERNATE_NAMES phosphatidylcholine 2-acylhydrolase ORGANISM #formal_name Naja mossambica mossambica #common_name Mozambique cobra DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 28-Feb-1997 ACCESSIONS A90623; A00743 REFERENCE A90623 !$#authors Joubert, F.J. !$#journal Biochim. Biophys. Acta (1977) 493:216-227 !$#title Naja mossambica mossambica venom. Purification, some !1properties and the amino acid sequences of three !1phospholipases A (CM-I, CM-II and CM-III). !$#cross-references MUID:77222126; PMID:880314 !$#accession A90623 !'##molecule_type protein !'##residues 1-118 ##label JOU FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; lipid degradation; !1metalloprotein; presynaptic neurotoxin; venom FEATURE !$4,66 #binding_site micellar substrate (Gln, Tyr) #status !8predicted\ !$11-70,26-117,28-44, !$43-98,50-91,59-84, !$77-89 #disulfide_bonds #status predicted\ !$27,29,31,48 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8predicted\ !$47,92 #active_site His, Asp #status predicted SUMMARY #length 118 #molecular-weight 13234 #checksum 6237 SEQUENCE /// ENTRY PSNJ3M #type complete TITLE phospholipase A2 (EC 3.1.1.4) III - Mozambique cobra ALTERNATE_NAMES phosphatidylcholine 2-acylhydrolase ORGANISM #formal_name Naja mossambica mossambica #common_name Mozambique cobra DATE 30-Nov-1980 #sequence_revision 29-Jun-1981 #text_change 28-Feb-1997 ACCESSIONS A00744 REFERENCE A90623 !$#authors Joubert, F.J. !$#journal Biochim. Biophys. Acta (1977) 493:216-227 !$#title Naja mossambica mossambica venom. Purification, some !1properties and the amino acid sequences of three !1phospholipases A (CM-I, CM-II and CM-III). !$#cross-references MUID:77222126; PMID:880314 !$#accession A00744 !'##molecule_type protein !'##residues 1-118 ##label JOU FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; lipid degradation; !1metalloprotein; presynaptic neurotoxin; venom FEATURE !$4,66 #binding_site micellar substrate (Gln, Tyr) #status !8predicted\ !$11-70,26-117,28-44, !$43-98,50-91,59-84, !$77-89 #disulfide_bonds #status predicted\ !$27,29,31,48 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8predicted\ !$47,92 #active_site His, Asp #status predicted SUMMARY #length 118 #molecular-weight 13302 #checksum 7157 SEQUENCE /// ENTRY PSNJ3B #type complete TITLE phospholipase A2 (EC 3.1.1.4) III - cobra (Naja mossambica pallida) ALTERNATE_NAMES phosphatidylcholine 2-acylhydrolase ORGANISM #formal_name Naja mossambica pallida DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 28-Feb-1997 ACCESSIONS A94475; A00744 REFERENCE A94475 !$#authors Odidairo, T.K.; Tampitag, S.; Eaker, D. !$#citation unpublished results, cited by Joubert, F.J., Biochim. !1Biophys. Acta 493, 216-227, 1977 !$#accession A94475 !'##molecule_type protein !'##residues 1-118 ##label ODI FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; lipid degradation; !1metalloprotein; presynaptic neurotoxin; venom FEATURE !$4,66 #binding_site micellar substrate (Gln, Tyr) #status !8predicted\ !$11-70,26-117,28-44, !$43-98,50-91,59-84, !$77-89 #disulfide_bonds #status predicted\ !$27,29,31,48 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8predicted\ !$47,92 #active_site His, Asp #status predicted SUMMARY #length 118 #molecular-weight 13268 #checksum 7193 SEQUENCE /// ENTRY PSKF2U #type complete TITLE phospholipase A2 (EC 3.1.1.4) nontoxic isozyme precursor - many-banded krait ALTERNATE_NAMES phosphatidylcholine 2-acylhydrolase ORGANISM #formal_name Bungarus multicinctus #common_name many-banded krait DATE 06-Jul-1982 #sequence_revision 30-Jun-1991 #text_change 11-Jun-1999 ACCESSIONS S10981; A00745 REFERENCE S10981 !$#authors Danse, J.M. !$#journal Nucleic Acids Res. (1990) 18:4608 !$#title Nucleotide sequence encoding for non-toxic phospholipase-A2 !1from Bungarus multicinctus. !$#cross-references MUID:90356415; PMID:2388841 !$#accession S10981 !'##molecule_type mRNA !'##residues 1-145 ##label DAN !'##cross-references EMBL:X53406; NID:g62501; PIDN:CAA37482.1; !1PID:g62502 REFERENCE A00745 !$#authors Kondo, K.; Toda, H.; Narita, K. !$#journal J. Biochem. (1981) 89:37-47 !$#title Amino acid sequence of phospholipase A from Bungarus !1multicinctus venom. !$#cross-references MUID:81168081; PMID:7217037 !$#accession A00745 !'##molecule_type protein !'##residues 28-118 ##label KON FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; lipid degradation; !1metalloprotein; presynaptic neurotoxin; venom FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-145 #product phospholipase A2 nontoxic isozyme #status !8predicted #label MAT\ !$31,93 #binding_site micellar substrate (Gln, Tyr) #status !8predicted\ !$38-97,52-144,54-70, !$69-125,76-118, !$86-111,104-116 #disulfide_bonds #status predicted\ !$53,55,57,74 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8predicted\ !$73,119 #active_site His, Asp #status predicted SUMMARY #length 145 #molecular-weight 15593 #checksum 9033 SEQUENCE /// ENTRY PSKFT3 #type complete TITLE phospholipase A2 (EC 3.1.1.4) Vb-2 - banded krait ALTERNATE_NAMES phosphatidylcholine 2-acylhydrolase; toxin V-3 ORGANISM #formal_name Bungarus fasciatus #common_name banded krait DATE 31-Mar-1992 #sequence_revision 31-Jan-1997 #text_change 27-Feb-1997 ACCESSIONS B36487; B94313; A00759; A94313 REFERENCE A36487 !$#authors Liu, C.S.; Chen, J.M.; Chang, C.H.; Chen, S.W.; Tsai, I.H.; !1Lu, H.S.; Lo, T.B. !$#journal Toxicon (1990) 28:1457-1468 !$#title Revised amino acid sequences of the three major !1phospholipases A-2 from Bungarus fasciatus (banded krait) !1venom. !$#cross-references MUID:91213258; PMID:2089739 !$#accession B36487 !'##molecule_type protein !'##residues 1-118 ##label LIU REFERENCE A94313 !$#authors Lu, H.S.; Lo, T.B. !$#journal Toxicon (1981) 19:103-111 !$#title Complete amino acid sequences of two cardiotoxin-like !1analogues from Bungarus fasciatus (banded krait) snake !1venom. !$#cross-references MUID:81177948; PMID:6784277 !$#accession B94313 !'##molecule_type protein !'##residues 1-2,'Y',4-13,'T',15,'NIAGFTN',17,'Q',19,'L',21-30, !1'THDPDALEKN',31,'CY',34-36,'R',56-58,'IFNPLAAKCCGS',61,'NR', !164-66,'V',68-71,'A',73,'AFGI','K',87-93,'DCQT',98,'D',100, !1'YHKTA',106-107,'Y',110-112,'ET',115-118 ##label LUH FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; lipid degradation; !1metalloprotein; presynaptic neurotoxin; venom FEATURE !$4,66 #binding_site micellar substrate (Gln, Tyr) #status !8predicted\ !$11-70,25-117,27-43, !$42-98,49-91,59-84, !$77-89 #disulfide_bonds #status predicted\ !$26,28,30,47 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8predicted\ !$46,92 #active_site His, Asp #status predicted SUMMARY #length 118 #molecular-weight 13107 #checksum 4885 SEQUENCE /// ENTRY PSKFT2 #type complete TITLE phospholipase A2 (EC 3.1.1.4) Va - banded krait ALTERNATE_NAMES phosphatidylcholine 2-acylhydrolase; toxin V-2 ORGANISM #formal_name Bungarus fasciatus #common_name banded krait DATE 31-Mar-1992 #sequence_revision 31-Jan-1997 #text_change 27-Feb-1997 ACCESSIONS A36487; A94313; A00759 REFERENCE A36487 !$#authors Liu, C.S.; Chen, J.M.; Chang, C.H.; Chen, S.W.; Tsai, I.H.; !1Lu, H.S.; Lo, T.B. !$#journal Toxicon (1990) 28:1457-1468 !$#title Revised amino acid sequences of the three major !1phospholipases A-2 from Bungarus fasciatus (banded krait) !1venom. !$#cross-references MUID:91213258; PMID:2089739 !$#accession A36487 !'##molecule_type protein !'##residues 1-118 ##label LIU REFERENCE A94313 !$#authors Lu, H.S.; Lo, T.B. !$#journal Toxicon (1981) 19:103-111 !$#title Complete amino acid sequences of two cardiotoxin-like !1analogues from Bungarus fasciatus (banded krait) snake !1venom. !$#cross-references MUID:81177948; PMID:6784277 !$#accession A94313 !'##molecule_type protein !'##residues 1-2,'Y',4-9,'E',11-15,'NIAGFTN',17,'Q',19,'L',21-30,45-47, !1'PDALEKNG',49-50,'TGPLR',56-58,'IFNPLAAKCCGS',61,'NR',64-66, !1'V',68-71,'A',73,'AFGI','K',87-93,'DCQT',98,'D',100,'YHKTA', !1106-107,'Y',110-112,'ET',115-118 ##label LUH FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; lipid degradation; !1metalloprotein; presynaptic neurotoxin; venom FEATURE !$4,66 #binding_site micellar substrate (Gln, Tyr) #status !8predicted\ !$11-70,25-117,27-43, !$42-98,49-91,59-84, !$77-89 #disulfide_bonds #status predicted\ !$26,28,30,47 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8predicted\ !$46,92 #active_site His, Asp #status predicted SUMMARY #length 118 #molecular-weight 13098 #checksum 5317 SEQUENCE /// ENTRY PSKFT1 #type complete TITLE phospholipase A2 (EC 3.1.1.4) VI - banded krait ALTERNATE_NAMES phosphatidylcholine 2-acylhydrolase; toxin V-1 ORGANISM #formal_name Bungarus fasciatus #common_name banded krait DATE 22-May-1981 #sequence_revision 31-Jan-1997 #text_change 27-Feb-1997 ACCESSIONS C36487; A00759 REFERENCE A36487 !$#authors Liu, C.S.; Chen, J.M.; Chang, C.H.; Chen, S.W.; Tsai, I.H.; !1Lu, H.S.; Lo, T.B. !$#journal Toxicon (1990) 28:1457-1468 !$#title Revised amino acid sequences of the three major !1phospholipases A-2 from Bungarus fasciatus (banded krait) !1venom. !$#cross-references MUID:91213258; PMID:2089739 !$#accession C36487 !'##molecule_type protein !'##residues 1-118 ##label LIU REFERENCE A91756 !$#authors Lu, H.S.; Lo, T.B. !$#journal Int. J. Pept. Protein Res. (1978) 12:181-183 !$#title Complete amino acid sequence of a new type of cardiotoxin of !1Bungarus fasciatus venom. !$#cross-references MUID:79026543; PMID:700923 !$#accession A00759 !'##molecule_type protein !'##residues 1-15,'NIAGFTNWQALVK',22-30,'TH',40,'PDALEKNG',49-50, !1'TGPLR',56-58,'IYNLAAKCCGS',61,'NR',64-71,'A',73,'AFGI','K', !187-93,'DCQT',98,'D',100,'YHKTA',106-107,'Y',110-111,'DET', !1115-118 ##label LUH FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; lipid degradation; !1metalloprotein; presynaptic neurotoxin; venom FEATURE !$4,66 #binding_site micellar substrate (Gln, Tyr) #status !8predicted\ !$11-70,25-117,27-43, !$42-98,49-91,59-84, !$77-89 #disulfide_bonds #status predicted\ !$26,28,30,47 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8predicted\ !$46,92 #active_site His, Asp #status predicted SUMMARY #length 118 #molecular-weight 13052 #checksum 5132 SEQUENCE /// ENTRY PSOXA #type complete TITLE phospholipase A2 (EC 3.1.1.4) taipoxin alpha chain - Australian taipan ALTERNATE_NAMES phosphatidylcholine 2-acylhydrolase ORGANISM #formal_name Oxyuranus scutellatus scutellatus #common_name Australian taipan DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 28-Feb-1997 ACCESSIONS A00754 REFERENCE A00754 !$#authors Lind, P.; Eaker, D. !$#journal Eur. J. Biochem. (1982) 124:441-447 !$#title Amino-acid sequence of the alpha-subunit of taipoxin, an !1extremely potent presynaptic neurotoxin from the Australian !1snake Taipan (Oxyuranus s. scutellatus). !$#cross-references MUID:82261658; PMID:7049694 !$#accession A00754 !'##molecule_type protein !'##residues 1-119 ##label LIN FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; lipid degradation; !1metalloprotein; presynaptic neurotoxin; venom FEATURE !$4,68 #binding_site micellar substrate (Gln, Tyr) #status !8predicted\ !$11-72,27-118,29-45, !$44-99,51-92,61-85, !$79-90 #disulfide_bonds #status predicted\ !$28,30,32,49 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8predicted\ !$48,93 #active_site His, Asp #status predicted SUMMARY #length 119 #molecular-weight 13829 #checksum 2605 SEQUENCE /// ENTRY PSOXB #type complete TITLE phospholipase A2 homolog taipoxin beta chain - Australian taipan ORGANISM #formal_name Oxyuranus scutellatus scutellatus #common_name Australian taipan DATE 05-Apr-1983 #sequence_revision 05-Apr-1983 #text_change 24-Apr-1998 ACCESSIONS A00755 REFERENCE A00755 !$#authors Lind, P. !$#journal Eur. J. Biochem. (1982) 128:71-75 !$#title Amino-acid sequence of the beta1 isosubunit of taipoxin, an !1extremely potent presynaptic neurotoxin from the Australian !1snake Taipan (Oxyuranus s. scutellatus). !$#cross-references MUID:83079319; PMID:6756920 !$#accession A00755 !'##molecule_type protein !'##residues 1-118 ##label LIN !'##note the beta chain is neither toxic nor enzymatically active by !1itself; it does not bind calcium, a necessary cofactor for !1all pancreatic and venom phospholipases COMMENT Taipoxin, the most potent animal toxin known, contains three !1noncovalently bound chains (alpha, beta, and gamma), each !1related to phospholipase A2. This presynaptic neurotoxin is !1the main lethal component of the venom. CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; metalloprotein; venom FEATURE !$11-71,27-117,29-45, !$44-98,51-91,60-84, !$78-89 #disulfide_bonds #status predicted\ !$28,30,32,49 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8predicted SUMMARY #length 118 #molecular-weight 13236 #checksum 6104 SEQUENCE /// ENTRY PSNOA1 #type complete TITLE phospholipase A2 homolog notechis 1 - common tiger snake ORGANISM #formal_name Notechis scutatus scutatus #common_name common tiger snake, mainland tiger snake DATE 01-Sep-1981 #sequence_revision 08-Oct-1981 #text_change 24-Apr-1998 ACCESSIONS A00746 REFERENCE A00746 !$#authors Lind, P.; Eaker, D. !$#journal Eur. J. Biochem. (1980) 111:403-409 !$#title Complete amino-acid sequence of a non-neurotoxic, !1non-enzymatic phospholipase A-2 homolog from the venom of !1the Australian tiger snake Notechis scutatus scutatus. !$#cross-references MUID:81114152; PMID:7007039 !$#accession A00746 !'##molecule_type protein !'##residues 1-119 ##label LIN COMMENT This protein, which has no enzymatic or neurotoxic activity, !1is the major protein component of the venom of this species. CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; metalloprotein; venom FEATURE !$11-72,27-118,29-45, !$44-99,51-92,61-85, !$79-90 #disulfide_bonds #status predicted\ !$28,30,32,49 #binding_site calcium (Tyr, Ser, Gly, Asp) #status !8predicted SUMMARY #length 119 #molecular-weight 13323 #checksum 8356 SEQUENCE /// ENTRY PSSNK1 #type complete TITLE phospholipase A2 (EC 3.1.1.4) Pa 11 - mulga snake ALTERNATE_NAMES phosphatidylcholine 2-acylhydrolase ORGANISM #formal_name Pseudechis australis #common_name mulga snake DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 28-Feb-1997 ACCESSIONS A00747 REFERENCE A94319 !$#authors Nishida, S.; Terashima, M.; Tamiya, N. !$#journal Toxicon (1985) 23:87-104 !$#title Amino acid sequences of phospholipases A-2 from the venom of !1an Australian elapid snake (king brown snake, Pseudechis !1australis). !$#cross-references MUID:85193286; PMID:3887651 !$#accession A00747 !'##molecule_type protein !'##residues 1-118 ##label NIS COMMENT There are many protein components with phospholipase A2 !1activity in the mulga snake venom and some of them are !1myotoxic. FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; lipid degradation; !1metalloprotein; presynaptic neurotoxin; venom FEATURE !$4,67 #binding_site micellar substrate (Gln, Tyr) #status !8predicted\ !$11-71,27-117,29-45, !$44-98,51-91,60-84, !$78-89 #disulfide_bonds #status predicted\ !$28,30,32,49 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8predicted\ !$48,92 #active_site His, Asp #status predicted SUMMARY #length 118 #molecular-weight 12966 #checksum 7702 SEQUENCE /// ENTRY PSSNK3 #type complete TITLE phospholipase A2 (EC 3.1.1.4) Pa 13 - mulga snake ALTERNATE_NAMES phosphatidylcholine 2-acylhydrolase ORGANISM #formal_name Pseudechis australis #common_name mulga snake DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 28-Feb-1997 ACCESSIONS A00748 REFERENCE A94319 !$#authors Nishida, S.; Terashima, M.; Tamiya, N. !$#journal Toxicon (1985) 23:87-104 !$#title Amino acid sequences of phospholipases A-2 from the venom of !1an Australian elapid snake (king brown snake, Pseudechis !1australis). !$#cross-references MUID:85193286; PMID:3887651 !$#accession A00748 !'##molecule_type protein !'##residues 1-118 ##label NIS COMMENT There are many protein components with phospholipase A2 !1activity in the mulga snake venom and some of them are !1myotoxic. FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; lipid degradation; !1metalloprotein; presynaptic neurotoxin; venom FEATURE !$4,67 #binding_site micellar substrate (Gln, Tyr) #status !8predicted\ !$11-71,27-117,29-45, !$44-98,51-91,60-84, !$78-89 #disulfide_bonds #status predicted\ !$28,30,32,49 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8predicted\ !$48,92 #active_site His, Asp #status predicted SUMMARY #length 118 #molecular-weight 13213 #checksum 4674 SEQUENCE /// ENTRY PSNOAT #type complete TITLE phospholipase A2 (EC 3.1.1.4) notexin - common tiger snake ALTERNATE_NAMES phosphatidylcholine 2-acylhydrolase ORGANISM #formal_name Notechis scutatus scutatus #common_name common tiger snake, mainland tiger snake DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 14-Feb-1997 ACCESSIONS A00749; S06655; S19286 REFERENCE A92185 !$#authors Halpert, J.; Eaker, D. !$#journal J. Biol. Chem. (1975) 250:6990-6997 !$#title Amino acid sequence of a presynaptic neurotoxin from the !1venom of Notechis scutatus scutatus (Australian tiger !1snake). !$#cross-references MUID:76005594; PMID:1158892 !$#accession A00749 !'##molecule_type protein !'##residues 1-119 ##label HAL REFERENCE S06655 !$#authors Mollier, P.; Chwetzoff, S.; Bouet, F.; Harvey, A.L.; Menez, !1A. !$#journal Eur. J. Biochem. (1989) 185:263-270 !$#title Tryptophan 110, a residue involved in the toxic activity but !1not in the enzymatic activity of notexin. !$#cross-references MUID:90060109; PMID:2583182 !$#accession S06655 !'##molecule_type protein !'##residues 1-17,'X',19-24;96-112 ##label MOL !'##note chemical modification shows that Trp-110 is required for toxin !1activity, but that neither Trp-20 nor Trp-110 is required !1for enzyme activity REFERENCE S19286 !$#authors Yang, C.C.; Chang, L.S. !$#journal Biochem. J. (1991) 280:739-744 !$#title Dissociation of lethal toxicity and enzymic activity of !1notexin from Notechis scutatus scutatus !1(Australian-tiger-snake) venom by modification of tyrosine !1residues. !$#cross-references MUID:92109676; PMID:1764038 !$#accession S19286 !'##molecule_type protein !'##residues 3-17;64-79 ##label YAN !'##note chemical modification studies of four tyrosine residues REFERENCE A91426 !$#authors Halpert, J.; Eaker, D.; Karlsson, E. !$#journal FEBS Lett. (1976) 61:72-76 !$#title The role of phospholipase activity in the action of a !1presynaptic neurotoxin from the venom of Notechis scutatus !1scutatus (Australian tiger snake). !$#cross-references MUID:76092395; PMID:1245225 !$#contents annotation; active site !$#note both enzyme and and toxin activity are lost upon chemical !1modification of His-48 COMMENT Notexin inhibits acetylcholine release at the neuromuscular !1junction (presynaptic neurotoxin effect) and is directly !1toxic to skeletal muscle upon local application (dystrophic !1myotoxin effect). These toxin activities are distinct from !1phospholipase A enzyme activity. FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; lipid degradation; !1metalloprotein; myotoxin; presynaptic neurotoxin; venom FEATURE !$4,67 #binding_site micellar substrate (Gln, Tyr) #status !8predicted\ !$11-71,27-118,29-45, !$44-99,51-92,60-85, !$78-90 #disulfide_bonds #status predicted\ !$28,30,32,49 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8predicted\ !$48 #active_site His #status experimental\ !$93 #active_site Asp #status predicted SUMMARY #length 119 #molecular-weight 13593 #checksum 6138 SEQUENCE /// ENTRY PSNOAS #type complete TITLE phospholipase A2 (EC 3.1.1.4) notexin s - common tiger snake ALTERNATE_NAMES notechis N-s; phosphatidylcholine 2-acylhydrolase ORGANISM #formal_name Notechis scutatus scutatus #common_name common tiger snake, mainland tiger snake DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 28-Feb-1997 ACCESSIONS S08258 REFERENCE S08258 !$#authors Chwetzoff, S.; Mollier, P.; Bouet, F.; Rowan, E.G.; Harvey, !1A.L.; Menez, A. !$#journal FEBS Lett. (1990) 261:226-230 !$#title On the purification of notexin. Isolation of a single amino !1acid variant from the venom of Notechis scutatus scutatus. !$#cross-references MUID:90184450; PMID:2155818 !$#accession S08258 !'##molecule_type protein !'##residues 1-119 ##label CHW FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; homodimer; lipid !1degradation; metalloprotein; presynaptic neurotoxin; venom FEATURE !$4,67 #binding_site micellar substrate (Gln, Tyr) #status !8predicted\ !$11-71,27-118,29-45, !$44-99,51-92,60-85, !$78-90 #disulfide_bonds #status predicted\ !$28,30,32,49 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8predicted\ !$48,93 #active_site His, Asp #status predicted SUMMARY #length 119 #molecular-weight 13621 #checksum 6250 SEQUENCE /// ENTRY PSNOA5 #type complete TITLE phospholipase A2 (EC 3.1.1.4) notechis 5 - common tiger snake ALTERNATE_NAMES phosphatidylcholine 2-acylhydrolase ORGANISM #formal_name Notechis scutatus scutatus #common_name common tiger snake, mainland tiger snake DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 28-Feb-1997 ACCESSIONS A00750 REFERENCE A00750 !$#authors Halpert, J.; Eaker, D. !$#journal J. Biol. Chem. (1976) 251:7343-7347 !$#title Isolation and amino acid sequence of a neurotoxic !1phospholipase A from the venom of the Australian tiger snake !1Notechis scutatus scutatus. !$#cross-references MUID:77071450; PMID:1002692 !$#accession A00750 !'##molecule_type protein !'##residues 1-119 ##label HAL COMMENT Notechis 5 is less toxic than notexin but has a higher !1specific phospholipase activity. FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; lipid degradation; !1metalloprotein; presynaptic neurotoxin; venom FEATURE !$4,67 #binding_site micellar substrate (Gln, Tyr) #status !8predicted\ !$11-71,27-118,29-45, !$44-99,51-92,60-85, !$78-90 #disulfide_bonds #status predicted\ !$28,30,32,49 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8predicted\ !$48,93 #active_site His, Asp #status predicted SUMMARY #length 119 #molecular-weight 13676 #checksum 7513 SEQUENCE /// ENTRY PSEYA #type complete TITLE phospholipase A2 (EC 3.1.1.4) - beaked sea snake ALTERNATE_NAMES phosphatidylcholine 2-acylhydrolase ORGANISM #formal_name Enhydrina schistosa #common_name beaked sea snake, common sea snake DATE 29-Jun-1981 #sequence_revision 29-Jun-1981 #text_change 28-Feb-1997 ACCESSIONS A00751 REFERENCE A00751 !$#authors Lind, P.; Eaker, D. !$#journal Toxicon (1981) 19:11-24 !$#title Amino acid sequence of a lethal myotoxic phospholipase A-2 !1from the venom of the common sea snake (Enhydrina !1schistosa). !$#cross-references MUID:81177949; PMID:7222079 !$#accession A00751 !'##molecule_type protein !'##residues 1-119 ##label LIN !'##note 64-Leu was found in about 50% of the molecules !'##note 98-Lys was found in about 30% of the molecules FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; lipid degradation; !1metalloprotein; presynaptic neurotoxin; venom FEATURE !$4,67 #binding_site micellar substrate (Gln, Tyr) #status !8predicted\ !$11-71,27-118,29-45, !$44-99,51-92,60-85, !$78-90 #disulfide_bonds #status predicted\ !$28,30,32,49 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8predicted\ !$48,93 #active_site His, Asp #status predicted SUMMARY #length 119 #molecular-weight 13446 #checksum 6941 SEQUENCE /// ENTRY PSLT3E #type complete TITLE phospholipase A2 (EC 3.1.1.4) III - broad-banded blue sea krait ALTERNATE_NAMES phosphatidylcholine 2-acylhydrolase ORGANISM #formal_name Laticauda semifasciata #common_name broad-banded blue sea krait, erabu sea snake DATE 02-Apr-1982 #sequence_revision 13-Jun-1983 #text_change 28-Feb-1997 ACCESSIONS A00753 REFERENCE A90316 !$#authors Nishida, S.; Kim, H.S.; Tamiya, N. !$#journal Biochem. J. (1982) 207:589-594 !$#title Amino acid sequences of three phospholipases A I, III and IV !1from the venom of the sea snake Laticauda semifasciata. !$#cross-references MUID:83153048; PMID:7165712 !$#accession A00753 !'##molecule_type protein !'##residues 1-118 ##label NIS FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; lipid degradation; !1metalloprotein; presynaptic neurotoxin; venom FEATURE !$4,67 #binding_site micellar substrate (Gln, Tyr) #status !8predicted\ !$11-71,27-117,29-45, !$44-98,51-91,60-84, !$78-89 #disulfide_bonds #status predicted\ !$28,30,32,49 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8predicted\ !$48,92 #active_site His, Asp #status predicted SUMMARY #length 118 #molecular-weight 13243 #checksum 8924 SEQUENCE /// ENTRY PSLT4E #type complete TITLE phospholipase A2 (EC 3.1.1.4) IV - broad-banded blue sea krait ALTERNATE_NAMES phosphatidylcholine 2-acylhydrolase ORGANISM #formal_name Laticauda semifasciata #common_name broad-banded blue sea krait, erabu sea snake DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 28-Feb-1997 ACCESSIONS A90316; A00753 REFERENCE A90316 !$#authors Nishida, S.; Kim, H.S.; Tamiya, N. !$#journal Biochem. J. (1982) 207:589-594 !$#title Amino acid sequences of three phospholipases A I, III and IV !1from the venom of the sea snake Laticauda semifasciata. !$#cross-references MUID:83153048; PMID:7165712 !$#accession A90316 !'##molecule_type protein !'##residues 1-118 ##label NIS FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; lipid degradation; !1metalloprotein; presynaptic neurotoxin; venom FEATURE !$4,67 #binding_site micellar substrate (Gln, Tyr) #status !8predicted\ !$11-71,27-117,29-45, !$44-98,51-91,60-84, !$78-89 #disulfide_bonds #status predicted\ !$28,30,32,49 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8predicted\ !$48,92 #active_site His, Asp #status predicted SUMMARY #length 118 #molecular-weight 13241 #checksum 9810 SEQUENCE /// ENTRY PSLT1E #type complete TITLE phospholipase A2 (EC 3.1.1.4) I - broad-banded blue sea krait ALTERNATE_NAMES phosphatidylcholine 2-acylhydrolase ORGANISM #formal_name Laticauda semifasciata #common_name broad-banded blue sea krait, erabu sea snake DATE 02-Apr-1982 #sequence_revision 31-Dec-1989 #text_change 28-Feb-1997 ACCESSIONS A94325; A00752; A30821 REFERENCE A94325 !$#authors Takasaki, C.; Kuramochi, H.; Shimazu, T.; Tamiya, N. !$#journal Toxicon (1988) 26:747-749 !$#title Correction of amino acid sequence of phospholipase A-2 I !1from the venom of Laticauda semifasciata (erabu sea snake). !$#cross-references MUID:89044898; PMID:3188064 !$#accession A94325 !'##molecule_type protein !'##residues 1-118 ##label TAK REFERENCE A90316 !$#authors Nishida, S.; Kim, H.S.; Tamiya, N. !$#journal Biochem. J. (1982) 207:589-594 !$#title Amino acid sequences of three phospholipases A I, III and IV !1from the venom of the sea snake Laticauda semifasciata. !$#cross-references MUID:83153048; PMID:7165712 !$#contents annotation; specific activity !$#note Trp-64 is important to enzyme activity FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; lipid degradation; !1metalloprotein; presynaptic neurotoxin; venom FEATURE !$4,67 #binding_site micellar substrate (Gln, Tyr) #status !8predicted\ !$11-71,27-117,29-45, !$44-98,51-91,60-84, !$78-89 #disulfide_bonds #status predicted\ !$28,30,32,49 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8predicted\ !$48,92 #active_site His, Asp #status predicted SUMMARY #length 118 #molecular-weight 13131 #checksum 8391 SEQUENCE /// ENTRY PSOXG #type complete TITLE phospholipase A2 (EC 3.1.1.4) taipoxin gamma chain - Australian taipan (tentative sequence) ALTERNATE_NAMES phosphatidylcholine 2-acylhydrolase ORGANISM #formal_name Oxyuranus scutellatus scutellatus #common_name Australian taipan DATE 30-Nov-1980 #sequence_revision 30-Nov-1980 #text_change 31-Mar-2000 ACCESSIONS A00756 REFERENCE A00756 !$#authors Fohlman, J.; Lind, P.; Eaker, D. !$#journal FEBS Lett. (1977) 84:367-371 !$#title Taipoxin, an extremely potent presynaptic snake venom !1neurotoxin. Elucidation of the primary structure of the !1acidic carbohydrate-containing taipoxin-subunit, a !1prophospholipase homolog. !$#cross-references MUID:78084803; PMID:563806 !$#accession A00756 !'##molecule_type protein !'##residues 1-133 ##label FOH COMMENT Taipoxin, a presynaptic neurotoxin of the venom, contains !1three noncovalently bound chains (alpha, beta, and gamma), !1each related to phospholipase A2. FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; glycoprotein; lipid !1degradation; metalloprotein; toxin; venom FEATURE !$19-85,23-27,35-131, !$37-53,52-113, !$59-106,69-99,92-104 #disulfide_bonds #status predicted\ !$36,38,40,57 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8predicted\ !$56,107 #active_site His, Asp #status predicted\ !$78 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 133 #molecular-weight 14603 #checksum 9611 SEQUENCE /// ENTRY PSKFAU #type complete TITLE phospholipase A2 (EC 3.1.1.4) beta bungarotoxin chain A1 - many-banded krait (tentative sequence) ALTERNATE_NAMES phosphatidylcholine 2-acylhydrolase ORGANISM #formal_name Bungarus multicinctus #common_name many-banded krait DATE 30-Nov-1980 #sequence_revision 14-Nov-1983 #text_change 31-Mar-2000 ACCESSIONS B01220; A00757 REFERENCE A01220 !$#authors Kondo, K.; Toda, H.; Narita, K.; Lee, C.Y. !$#journal J. Biochem. (1982) 91:1519-1530 !$#title Amino acid sequence of beta-2-bungarotoxin from Bungarus !1multicinctus venom. The amino acid substitutions in the B !1chains. !$#cross-references MUID:82239269; PMID:7096304 !$#accession B01220 !'##molecule_type protein !'##residues 1-120 ##label KON1 REFERENCE A01218 !$#authors Kondo, K.; Narita, K.; Lee, C.Y. !$#journal J. Biochem. (1978) 83:101-115 !$#title Amino acid sequences of the two polypeptide chains in !1beta-1-bungarotoxin from the venom of Bungarus multicinctus. !$#cross-references MUID:78109400; PMID:624701 !$#accession A00757 !'##molecule_type protein !'##residues 1-84,'GTC',88-108,'E',110-120 ##label KON2 !'##note 89-Val occurs in 20% of the molecules REFERENCE A91948 !$#authors Kondo, K.; Toda, H.; Narita, K. !$#journal J. Biochem. (1978) 84:1301-1308 !$#title Characterization of phospholipase A activity of !1beta-1-bungarotoxin from Bungarus multicinctus venom. II. !1Identificationof the histidine residue of !1beta-1-bungarotoxin modified by p-bromophenacyl bromide. !$#cross-references MUID:79088714; PMID:730754 !$#contents annotation; characterization of phospholipase A2 activity REFERENCE A91250 !$#authors Abe, T.; Alema, S.; Miledi, R. !$#journal Eur. J. Biochem. (1977) 80:1-12 !$#title Isolation and characterization of presynaptically acting !1neurotoxins from the venom of Bungarus snakes. !$#cross-references MUID:78043174; PMID:303565 !$#contents annotation; characterization of presynaptic neurotoxins from !1venom of Bungarus snakes !$#note calcium is required for phospholipase A2 activity COMMENT Beta bungarotoxins are presynaptic neurotoxins found in the !1venom; they are dimers of dissimilar chains linked by one or !1more disulfide bonds. The A chains have phospholipase A2 !1activity and sequence homology with other venom and !1pancreatic phospholipases A2. The B chains show homology !1with the basic protease inhibitors. COMMENT The A1 chain is found in beta-1 and beta-2 bungarotoxins. !1The A2 chain is found in beta-3 and beta-4 bungarotoxins. FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; heterodimer; lipid !1degradation; metalloprotein; neurotoxin; venom FEATURE !$27-119,29-45, !$44-100,51-93,61-86, !$79-91 #disulfide_bonds #status predicted\ !$28,30,32,49 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8predicted\ !$48,94 #active_site His, Asp #status predicted SUMMARY #length 120 #molecular-weight 13489 #checksum 6832 SEQUENCE /// ENTRY PSKFA2 #type complete TITLE phospholipase A2 (EC 3.1.1.4) beta bungarotoxin chain A2 precursor - many-banded krait ALTERNATE_NAMES phosphatidylcholine 2-acylhydrolase ORGANISM #formal_name Bungarus multicinctus #common_name many-banded krait DATE 31-Dec-1990 #sequence_revision 30-Jun-1991 #text_change 11-Jun-1999 ACCESSIONS S10980; B00758; A00757 REFERENCE S10980 !$#authors Danse, J.M.; Toussaint, J.L.; Kempf, J. !$#journal Nucleic Acids Res. (1990) 18:4609 !$#title Nucleotide sequence encoding beta-bungarotoxin A2-chain from !1the venom glands of Bungarus multicinctus. !$#cross-references MUID:90356416; PMID:2388842 !$#accession S10980 !'##molecule_type mRNA !'##residues 1-145 ##label DAN !'##cross-references EMBL:X53407; NID:g62473; PIDN:CAA37483.1; !1PID:g62474 REFERENCE A00758 !$#authors Kondo, K.; Toda, H.; Narita, K.; Lee, C.Y. !$#journal J. Biochem. (1982) 91:1531-1548 !$#title Amino acid sequences of three beta-bungarotoxins (beta-3-, !1beta4-, and beta5-bungarotoxins) from Bungarus multicinctus !1venom. Amino acid substitutions in the A chains. !$#cross-references MUID:82239270; PMID:7096305 !$#accession B00758 !'##molecule_type protein !'##residues 26-90,'SQ',93-127,'Q',129,'E',131-145 ##label KON COMMENT Beta bungarotoxins are presynaptic neurotoxins found in the !1venom; they are dimers of dissimilar chains linked by one or !1more disulfide bonds. The A chains have phospholipase A2 !1activity and sequence homology with other venom and !1pancreatic phospholipases A2. The B chains show homology !1with the basic protease inhibitors. COMMENT The A1 chain is found in beta-1 and beta-2 bungarotoxins. !1The A2 chain is found in beta-3 and beta-4 bungarotoxins. FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; heterodimer; lipid !1degradation; metalloprotein; neurotoxin; venom FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-145 #product phospholipase A2 isoform A2 #status !8predicted #label MAT\ !$52-144,54-70, !$69-125,76-118, !$86-111,104-116 #disulfide_bonds #status predicted\ !$53,55,57,74 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8predicted\ !$73,119 #active_site His, Asp #status predicted SUMMARY #length 145 #molecular-weight 16296 #checksum 6538 SEQUENCE /// ENTRY PSKF3U #type complete TITLE phospholipase A2 (EC 3.1.1.4) beta bungarotoxin chain A3 - many-banded krait (tentative sequence) ALTERNATE_NAMES phosphatidylcholine 2-acylhydrolase ORGANISM #formal_name Bungarus multicinctus #common_name many-banded krait DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 31-Mar-2000 ACCESSIONS A00758 REFERENCE A00758 !$#authors Kondo, K.; Toda, H.; Narita, K.; Lee, C.Y. !$#journal J. Biochem. (1982) 91:1531-1548 !$#title Amino acid sequences of three beta-bungarotoxins (beta-3-, !1beta4-, and beta5-bungarotoxins) from Bungarus multicinctus !1venom. Amino acid substitutions in the A chains. !$#cross-references MUID:82239270; PMID:7096305 !$#accession A00758 !'##molecule_type protein !'##residues 1-120 ##label KON COMMENT Beta bungarotoxins are presynaptic neurotoxins of the venom; !1they are dimers of dissimilar chains linked by one or more !1disulfide bonds. The A chains have phospholipase A2 activity !1and sequence homology with other venom and pancreatic !1phospholipases A2. The B chains show homology with the basic !1protease inhibitors. COMMENT The A3 chain is found in beta-5 bungarotoxin. FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; heterodimer; lipid !1degradation; metalloprotein; neurotoxin; venom FEATURE !$27-119,29-45, !$44-100,51-93,61-86, !$79-91 #disulfide_bonds #status predicted\ !$28,30,32,49 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8predicted\ !$48,94 #active_site His, Asp #status predicted SUMMARY #length 120 #molecular-weight 13439 #checksum 6873 SEQUENCE /// ENTRY PSKFA4 #type complete TITLE phospholipase A2 (EC 3.1.1.4) isozyme A4 precursor - many-banded krait ALTERNATE_NAMES phosphatidylcholine 2-acylhydrolase ORGANISM #formal_name Bungarus multicinctus #common_name many-banded krait DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 11-Jun-1999 ACCESSIONS S10982 REFERENCE S10982 !$#authors Danse, J.M.; Garnier, J.M.; Kempf, J. !$#journal Nucleic Acids Res. (1990) 18:4610 !$#title cDNA deduced amino-acid sequence of a new phospholipase from !1Bungarus multicinctus. !$#cross-references MUID:90356417; PMID:2388843 !$#accession S10982 !'##molecule_type mRNA !'##residues 1-147 ##label DAN !'##cross-references EMBL:X53408; NID:g62505; PIDN:CAA37484.1; !1PID:g62506 FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; lipid degradation; !1metalloprotein; toxin; venom FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-147 #product phospholipase A2 isozyme A4 #status !8predicted #label MAT\ !$54-146,56-72, !$71-127,78-120, !$88-113,106-118 #disulfide_bonds #status predicted\ !$55,57,59,76 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8predicted\ !$75,121 #active_site His, Asp #status predicted SUMMARY #length 147 #molecular-weight 16177 #checksum 1505 SEQUENCE /// ENTRY PSBGA #type complete TITLE phospholipase A2 (EC 3.1.1.4) - Gaboon viper ALTERNATE_NAMES phosphatidylcholine 2-acylhydrolase ORGANISM #formal_name Bitis gabonica #common_name Gaboon viper DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 24-Apr-1998 ACCESSIONS A00760 REFERENCE A00760 !$#authors Botes, D.P.; Viljoen, C.C. !$#journal J. Biol. Chem. (1974) 249:3827-3835 !$#title Bitis gabonica venom. The amino acid sequence of !1phospholipase A. !$#cross-references MUID:74267200; PMID:4833747 !$#accession A00760 !'##molecule_type protein !'##residues 1-118 ##label BOT FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; lipid degradation; !1metalloprotein; toxin; venom FEATURE !$24-118,26-42,41-92, !$47-112,48-85,73-83 #disulfide_bonds #status predicted\ !$25,27,29,46 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8predicted\ !$45,86 #active_site His, Asp #status predicted SUMMARY #length 118 #molecular-weight 13376 #checksum 678 SEQUENCE /// ENTRY PSBG2H #type complete TITLE phospholipase A2 (EC 3.1.1.4) - rhinoceros viper ALTERNATE_NAMES phosphatidylcholine 2-acylhydrolase ORGANISM #formal_name Bitis nasicornis #common_name rhinoceros viper DATE 18-Apr-1984 #sequence_revision 18-Apr-1984 #text_change 24-Apr-1998 ACCESSIONS A00761 REFERENCE A00761 !$#authors Joubert, F.J.; Townshend, G.S.; Botes, D.P. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1983) 364:1717-1726 !$#title Purification, some properties of two phospholipases A-2 !1(CM-I and CM-II) and the amino-acid sequence of CM-II from !1Bitis nasicornis (horned adder) venom. !$#cross-references MUID:84133812; PMID:6667925 !$#accession A00761 !'##molecule_type protein !'##residues 1-119 ##label JOU !'##note two very similar relatively nontoxic phospholipases were !1isolated from the venom, CM-II (shown) and CM-I; the amino !1acid composition of CM-I differed from that of CM-II in !1having one more Thr and Ala and one fewer Ser and Lys FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; lipid degradation; !1metalloprotein; toxin; venom FEATURE !$24-119,26-42,41-93, !$47-113,48-86,73-84 #disulfide_bonds #status predicted\ !$25,27,29,46 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8predicted\ !$45,87 #active_site His, Asp #status predicted SUMMARY #length 119 #molecular-weight 13665 #checksum 2640 SEQUENCE /// ENTRY PSBGAC #type complete TITLE phospholipase A2 (EC 3.1.1.4) - horned viper ALTERNATE_NAMES caudoxin; phosphatidylcholine 2-acylhydrolase ORGANISM #formal_name Bitis caudalis #common_name horned viper DATE 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 24-Apr-1998 ACCESSIONS A00762 REFERENCE A00762 !$#authors Viljoen, C.C.; Botes, D.P.; Kruger, H. !$#journal Toxicon (1982) 20:715-737 !$#title Isolation and amino acid sequence of caudoxin, a presynaptic !1acting toxic phospholipase A-2 from the venom of the horned !1puff adder (Bitis caudalis). !$#cross-references MUID:83042262; PMID:7135414 !$#accession A00762 !'##molecule_type protein !'##residues 1-121 ##label VIL COMMENT This enzyme is a presynaptic neurotoxin. FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; lipid degradation; !1metalloprotein; presynaptic neurotoxin; venom FEATURE !$25-121,27-43,42-94, !$48-114,49-87,56-80, !$74-85 #disulfide_bonds #status predicted\ !$26,28,30,47 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8predicted\ !$46,88 #active_site His, Asp #status predicted SUMMARY #length 121 #molecular-weight 13363 #checksum 68 SEQUENCE /// ENTRY PSRSAE #type complete TITLE phospholipase A2 (EC 3.1.1.4) - eastern diamondback rattlesnake ALTERNATE_NAMES phosphatidylcholine 2-acylhydrolase ORGANISM #formal_name Crotalus adamanteus #common_name eastern diamondback rattlesnake DATE 30-Nov-1980 #sequence_revision 23-Oct-1981 #text_change 24-Apr-1998 ACCESSIONS A00763 REFERENCE A00763 !$#authors Heinrikson, R.L.; Krueger, E.T.; Keim, P.S. !$#journal J. Biol. Chem. (1977) 252:4913-4921 !$#title Amino acid sequence of phospholipase A-2-alpha from the !1venom of Crotalus adamanteus. !$#cross-references MUID:77207108; PMID:873920 !$#accession A00763 !'##molecule_type protein !'##residues 1-122 ##label HEI COMMENT The sequence of the alpha form is shown. COMMENT In contrast to the pancreatic enzymes, the molecules of !1venom phospholipases A2 are dimers of identical chains; the !1monomers appear to be inactive. COMMENT Two very similar active forms of the enzyme, called alpha !1and beta, were isolated from the venom of C. adamanteus. The !1sequence of the beta form differs in having 117-Glu. FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; dimer; lipid !1degradation; metalloprotein; toxin; venom FEATURE !$26-115,28-44,43-95, !$49-122,50-88,57-81, !$75-86 #disulfide_bonds #status predicted\ !$27,29,31,48 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8predicted\ !$47,89 #active_site His, Asp #status predicted SUMMARY #length 122 #molecular-weight 13679 #checksum 9969 SEQUENCE /// ENTRY PSRSAW #type complete TITLE phospholipase A2 (EC 3.1.1.4) [validated] - western diamondback rattlesnake ALTERNATE_NAMES phosphatidylcholine 2-acylhydrolase ORGANISM #formal_name Crotalus atrox #common_name western diamondback rattlesnake DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 15-Sep-2000 ACCESSIONS A00764 REFERENCE A92362 !$#authors Randolph, A.; Heinrikson, R.L. !$#journal J. Biol. Chem. (1982) 257:2155-2161 !$#title Crotalus atrox phospholipase A-2. Amino acid sequence and !1studies on the function of the NH-2-terminal region. !$#cross-references MUID:82142299; PMID:7061414 !$#accession A00764 !'##molecule_type protein !'##residues 1-122 ##label RAN REFERENCE A50318 !$#authors Brunie, S.; Sigler, P.B. !$#submission submitted to the Brookhaven Protein Data Bank, March 1986 !$#cross-references PDB:1PP2 !$#contents annotation; X-ray crystallography, 2.5 angstroms; residues !11-122 REFERENCE A92550 !$#authors Brunie, S.; Bolin, J.; Gewirth, D.; Sigler, P.B. !$#journal J. Biol. Chem. (1985) 260:9742-9749 !$#title The refined crystal structure of dimeric phospholipse A-2 at !12.5 angstrom. Access to a shielded catalytic center. !$#cross-references MUID:85261386; PMID:4019493 !$#contents annotation; X-ray crystallography, 2.5 angstroms; active !1sites; binding sites REFERENCE A92336 !$#authors Keith, C.; Feldman, D.S.; Deganello, S.; Glick, J.; Ward, !1K.B.; Jones, E.O.; Sigler, P.B. !$#journal J. Biol. Chem. (1981) 256:8602-8607 !$#title The 2.5-angstrom crystal structure of a dimeric !1phospholipase A-2 from the venom of Crotalus atrox. !$#cross-references MUID:81264275; PMID:7263673 !$#contents annotation; X-ray crystallography, 2.5 angstroms COMPLEX homodimer FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; homodimer; lipid !1degradation; metalloprotein; toxin; venom FEATURE !$4,64 #binding_site micellar substrate (Gln, Tyr) #status !8experimental\ !$26-115,28-44,43-95, !$49-122,50-88,57-81, !$75-86 #disulfide_bonds #status experimental\ !$27,29,31,48 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8predicted\ !$47,89 #active_site His, Asp #status experimental SUMMARY #length 122 #molecular-weight 13595 #checksum 8730 SEQUENCE /// ENTRY PSRSAT #type complete TITLE phospholipase A2 homolog crotoxin acidic subunit precursor - tropical rattlesnake ORGANISM #formal_name Crotalus durissus terrificus #common_name tropical rattlesnake, cascabel DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 11-Jun-1999 ACCESSIONS S01392; A23861; S11382; B23861; C23861 REFERENCE S01392 !$#authors Bouchier, C.; Ducancel, F.; Guignery-Frelat, G.; Bon, C.; !1Boulain, J.C.; Menez, A. !$#journal Nucleic Acids Res. (1988) 16:9050 !$#title Cloning and sequencing of cDNAs encoding the two subunits of !1crotoxin. !$#cross-references MUID:89016587; PMID:3174444 !$#accession S01392 !'##molecule_type mRNA !'##residues 1-138 ##label BOU !'##cross-references EMBL:X12606; NID:g62685; PIDN:CAA31126.1; !1PID:g62686 REFERENCE A90500 !$#authors Aird, S.D.; Kaiser, I.I.; Lewis, R.V.; Kruggel, W.G. !$#journal Biochemistry (1985) 24:7054-7058 !$#title Rattlesnake presynaptic neurotoxins: primary structure and !1evolutionary origin of the acidic subunit. !$#cross-references MUID:86104201; PMID:4084559 !$#accession A23861 !'##molecule_type protein !'##residues 39-73,'N',75-76;'XXXXXXXXXX',95-102,'G',104-118;125-138 !1##label AIR1 REFERENCE S11382 !$#authors Aird, S.D.; Yates III, J.R.; Martino, P.A.; Shabanowitz, J.; !1Hunt, D.F.; Kaiser, I.I. !$#journal Biochim. Biophys. Acta (1990) 1040:217-224 !$#title The amino acid sequence of the acidic subunit B-chain of !1crotoxin. !$#cross-references MUID:90381276; PMID:2400773 !$#accession S11382 !'##molecule_type protein !'##residues 'Z',85-118 ##label AIR2 COMMENT This subunit has no enzymatic or toxin activity. It helps !1target crotoxin basic subunit to neuromuscular junctions. COMPLEX heterodimer of acidic and basic subunits; mature acidic !1subunit has 3 chains, disulfide linked CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; heterodimer; metalloprotein; pyroglutamic acid; !1venom FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-38 #domain propeptide #status predicted #label PRO\ !$39-76,84-118, !$125-138 #product crotoxin acidic subunit #status experimental !8#label MAT\ !$39-76 #domain crotoxin acidic subunit chain A #status !8experimental #label CHA\ !$84-118 #domain crotoxin acidic subunit chain B #status !8experimental #label CHB\ !$125-138 #domain crotoxin acidic subunit chain C #status !8experimental #label CHC\ !$42-131,44-60, !$59-111,65-138, !$66-104,73-97,91-102 #disulfide_bonds #status predicted\ !$43,45,47,64 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8predicted\ !$84 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$125 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental SUMMARY #length 138 #molecular-weight 15273 #checksum 9814 SEQUENCE /// ENTRY I51380 #type complete TITLE phospholipase A2 homolog Mojave toxin acidic subunit precursor - Mojave rattlesnake ALTERNATE_NAMES Mtx-A ORGANISM #formal_name Crotalus scutulatus scutulatus #common_name Mojave rattlesnake DATE 13-Sep-1996 #sequence_revision 14-Feb-1997 #text_change 11-Jun-1999 ACCESSIONS I51380; A33006; A38106 REFERENCE I51380 !$#authors John, T.R.; Smith, L.A.; Kaiser, I.I. !$#journal Gene (1994) 139:229-234 !$#title Genomic sequences encoding the acidic and basic subunits of !1Mojave toxin: unusually high sequence identity of non-coding !1regions. !$#cross-references MUID:94156205; PMID:8112610 !$#accession I51380 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-138 ##label JOH !'##cross-references EMBL:U01026; NID:g451315; PIDN:AAC59673.1; !1PID:g451316 REFERENCE A33006 !$#authors Bieber, A.L.; Becker, R.R.; McParland, R.; Hunt, D.F.; !1Shabanowitz, J.; Yates III, J.R.; Martino, P.A.; Johnson, !1G.R. !$#submission submitted to the Protein Sequence Database, November 1989 !$#accession A33006 !'##molecule_type protein !'##residues 41-80;84-119;127-138 ##label BIE REFERENCE A38106 !$#authors Bieber, A.L.; Becker, R.R.; McParland, R.; Hunt, D.F.; !1Shabanowitz, J.; Yates III, J.R.; Johnson, G.R. !$#journal Toxicon (1989) 27:31 !$#title Studies of the sequence of Mojave toxin: the acidic subunit. !$#accession A38106 !'##molecule_type protein !'##residues 41-80;84-91,'Q',94-102,'G',104-116,'D',118;127-138 ##label !1BI2 COMMENT This subunit has no enzymatic or toxin activity. It helps !1target crotoxin basic subunit to neuromuscular junctions. GENETICS !$#introns 14/1; 58/2; 92/1 COMPLEX heterodimer of acidic and basic subunits; mature acidic !1subunit has 3 chains, disulfide linked CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; heterodimer; metalloprotein; pyroglutamic acid; !1venom FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-40 #domain propeptide #status predicted #label PRO\ !$41-80,84-119, !$127-138 #product phospholipase A2 homolog acidic subunit !8#status experimental #label MAT\ !$41-80 #domain phospholipase A2 homolog acidic subunit A !8chain #status experimental #label CHA\ !$84-119 #domain phospholipase A2 homolog acidic subunit B !8chain #status experimental #label CHB\ !$127-138 #domain phospholipase A2 homolog acidic subunit C1 !8chain #status experimental #label CHC1\ !$129-138 #domain phospholipase A2 homolog acidic subunit C2 !8chain #status experimental #label CHC2\ !$42-131,44-60, !$59-111,65-138, !$66-104,73-97,91-102 #disulfide_bonds #status predicted\ !$43,45,47,64 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8predicted\ !$84 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental SUMMARY #length 138 #molecular-weight 15211 #checksum 9257 SEQUENCE /// ENTRY PSTVIF #type complete TITLE phospholipase A2 (EC 3.1.1.4) I precursor - habu ALTERNATE_NAMES lecithinase A; phosphatidase; phosphatidolipase; phosphatidylcholine 2-acylhydrolase ORGANISM #formal_name Trimeresurus flavoviridis #common_name habu DATE 30-Sep-1987 #sequence_revision 30-Jun-1992 #text_change 16-Jun-2000 ACCESSIONS B48188; JX0137; A38828; A25187; JS0001 REFERENCE A48188 !$#authors Nakashima, K.; Ogawa, T.; Oda, N.; Hattori, M.; Sakaki, Y.; !1Kihara, H.; Ohno, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:5964-5968 !$#title Accelerated evolution of Trimeresurus flavoviridis venom !1gland phospholipase A2 isozymes. !$#cross-references MUID:93317604; PMID:8327468 !$#accession B48188 !'##molecule_type DNA !'##residues 1-138 ##label NAK !'##cross-references GB:D10724; GB:D01237; NID:g436250; PIDN:BAA01567.1; !1PID:g436251 !'##experimental_source liver REFERENCE JX0137 !$#authors Oda, N.; Ogawa, T.; Ohno, M.; Sasaki, H.; Sakaki, Y.; !1Kihara, H. !$#journal J. Biochem. (1990) 108:816-821 !$#title Cloning and sequence analysis of cDNA for Trimeresurus !1flavoviridis phospholipase A2, and consequent revision of !1the amino acid sequence. !$#cross-references MUID:91185340; PMID:1707052 !$#accession JX0137 !'##molecule_type mRNA !'##residues 1-138 ##label ODA !'##cross-references GB:D10070; GB:D01204; NID:g222960; PIDN:BAA00962.1; !1PID:g222961 !$#accession A38828 !'##molecule_type protein !'##residues 77-98 ##label OD2 REFERENCE A92006 !$#authors Tanaka, S.; Mohri, N.; Kihara, H.; Ohno, M. !$#journal J. Biochem. (1986) 99:281-289 !$#title Amino acid sequence of Trimeresurus flavoviridis !1phospholipase A2. !$#cross-references MUID:86168106; PMID:3514593 !$#accession A25187 !'##molecule_type protein !'##residues 17-84,'Q',87,'N',89-91,'G',93-94,'D',96-97,'D',98-138 !1##label TAN REFERENCE A94320 !$#authors Kini, R.M.; Kawabata, S.I.; Iwanaga, S. !$#journal Toxicon (1986) 24:1117-1129 !$#title Comparison of amino terminal region of three isoenzymes of !1phospholipases A2 (TFV PL-Ia, TFV PL-Ib, TFV PL-X) from !1Trimeresurus flavoviridis (Habu snake) venom and the !1complete amino acid sequence of the basic phospholipase, TFV !1PL-X. !$#cross-references MUID:87179112; PMID:3564060 !$#accession JS0001 !'##molecule_type protein !'##residues 17-32,'P',34-47 ##label KIN GENETICS !$#introns 14/1; 58/2; 92/1 FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; homodimer; lipid !1degradation; metalloprotein; venom FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-138 #product phospholipase A2 #status experimental #label !8MAT\ !$42-131,44-60, !$59-110,66-103, !$97-101 #disulfide_bonds #status predicted\ !$43,45,47,64 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8predicted\ !$63,104 #active_site His, Asp #status predicted SUMMARY #length 138 #molecular-weight 15535 #checksum 9967 SEQUENCE /// ENTRY PSTV #type complete TITLE phospholipase A2 (EC 3.1.1.4) 1 precursor - himehabu ALTERNATE_NAMES phosphatidylcholine 2-acylhydrolase ORGANISM #formal_name Trimeresurus okinavensis #common_name himehabu DATE 19-Feb-1984 #sequence_revision 14-Feb-1997 #text_change 11-Jun-1999 ACCESSIONS JC4874; A00765 REFERENCE JC4874 !$#authors Nobuhisa, I.; Nakashima, K.; Deshimaru, M.; Ogawa, T.; !1Shimohigashi, Y.; Fukumaki, Y.; Sakaki, Y.; Hattori, S.; !1Kihara, H.; Ohno, M. !$#journal Gene (1996) 172:267-272 !$#title Accelerated evolution of Trimeresurus okinavensis venom !1gland phospholipase A2 isozyme-encoding genes. !$#cross-references MUID:96269416; PMID:8682315 !$#contents venom gland !$#accession JC4874 !'##molecule_type mRNA !'##residues 1-139 ##label NOB !'##cross-references DDBJ:D49388; NID:g1469804; PIDN:BAA08383.1; !1PID:g1469805 REFERENCE A00765 !$#authors Joubert, F.J.; Haylett, T. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1981) 362:997-1006 !$#title Purification, some properties and amino acid sequence of a !1phospholipase A-2 (DE-I) from Trimeresurus okinavensis !1(Hime-habu) venom. !$#cross-references MUID:82005841; PMID:7275018 !$#accession A00765 !'##molecule_type protein !'##residues 17-82,'T',84-85,'E',87-89,'S',91-93,'ND',96-116,'N', !1118-119,'D',121-134,'SE',137-139 ##label JOU !'##note this acidic phospholipase is nontoxic FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; lipid degradation; !1metalloprotein; venom FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-139 #product phospholipase A2 1 #status experimental !8#label MAT\ !$20,80 #binding_site micellar substrate (Gln, Tyr) #status !8experimental\ !$42-132,44-60, !$59-111,65-139, !$66-104,73-97,91-102 #disulfide_bonds #status predicted\ !$43,45,47,64 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8predicted\ !$63,105 #active_site His, Asp #status predicted SUMMARY #length 139 #molecular-weight 15584 #checksum 850 SEQUENCE /// ENTRY PSVII #type complete TITLE phospholipase A2 inhibitor - western sand viper ORGANISM #formal_name Vipera ammodytes ammodytes #common_name western sand viper DATE 17-Mar-1987 #sequence_revision 07-Feb-1997 #text_change 24-Jul-1997 ACCESSIONS B29290; A00769 REFERENCE A94648 !$#authors Mancheva, I.; Kleinschmidt, T.; Aleksiev, B.; Braunitzer, G. !$#journal Biol. Chem. Hoppe-Seyler (1987) 368:343-350 !$#title The primary structure of phospholipase A-2 of vipoxin from !1the venom of the Bulgarian viper (Vipera ammodytes !1ammodytes, Serpentes). !$#cross-references MUID:87271131; PMID:3606821 !$#accession B29290 !'##molecule_type protein !'##residues 1-122 ##label MAN !'##note correction to sequence A00769 REFERENCE A00769 !$#authors Mancheva, I.; Kleinschmidt, T.; Aleksiev, B.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1984) 365:885-893 !$#title Sequence homology between phospholipase and its inhibitor in !1snake venom. The primary structure of the inhibitor of !1vipoxin from the venom of the Bulgarian viper (Vipera !1ammodytes ammodytes, serpentes). !$#cross-references MUID:85028863; PMID:6489936 !$#accession A00769 !'##molecule_type protein !'##residues 1-53,61-83,'VNDCNPK',84-122 ##label MA2 !'##note overlaps were not obtained for residues 35-36 and 53-54 COMMENT The source of this protein is vipoxin, a venom complex of a !1toxic basic protein having weak phospholipase A2 activity !1and a nontoxic acidic protein that functions as its !1inhibitor. Without the inhibitor the basic protein becomes !1unstable, losing enzymatic activity within 12-14 days. COMMENT This inhibitor is homologous with the viperid A2 !1phospholipases. CLASSIFICATION #superfamily phospholipase A2 KEYWORDS phospholipase A2 inhibitor; venom FEATURE !$47,89 #region defective catalytic pair\ !$26-115,28-44,43-95, !$49-122,50-88,57-81, !$75-86 #disulfide_bonds #status predicted SUMMARY #length 122 #molecular-weight 13738 #checksum 1276 SEQUENCE /// ENTRY PSABA #type complete TITLE phospholipase A2 (EC 3.1.1.4) - mamushi ALTERNATE_NAMES phosphatidylcholine 2-acylhydrolase ORGANISM #formal_name Agkistrodon blomhoffi #common_name mamushi DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 26-Feb-1999 ACCESSIONS A00766; S43474 REFERENCE A00766 !$#authors Forst, S.; Weiss, J.; Blackburn, P.; Frangione, B.; Goni, !1F.; Elsbach, P. !$#journal Biochemistry (1986) 25:4309-4314 !$#title Amino acid sequence of a basic Agkistrodon halys blomhoffii !1phospholipase A2. Possible role of NH-2-terminal lysines in !1action on phospholipids of Escherichia coli. !$#cross-references MUID:87000546; PMID:3530322 !$#accession A00766 !'##molecule_type protein !'##residues 1-122 ##label FOR !'##note the identification of 74-Val is tentative REFERENCE S43474 !$#authors Dua, R.; Cho, W. !$#journal Eur. J. Biochem. (1994) 221:481-490 !$#title Inhibition of human secretory class II phospholipase A(2) by !1heparin. !$#cross-references MUID:94222096; PMID:8168536 !$#accession S43474 !'##molecule_type protein !'##residues 1-19;50-56 ##label DUA COMPLEX homodimer FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; homodimer; lipid !1degradation; metalloprotein; toxin; venom FEATURE !$4,64 #binding_site micellar substrate (Gln, Tyr) #status !8predicted\ !$26-115,28-44,43-95, !$50-88,57-81,75-86 #disulfide_bonds #status predicted\ !$27,29,31,48 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8predicted\ !$47,89 #active_site His, Asp #status predicted\ !$49-122 #disulfide_bonds #status experimental SUMMARY #length 122 #molecular-weight 13982 #checksum 9941 SEQUENCE /// ENTRY PSTVXF #type complete TITLE phospholipase A2 (EC 3.1.1.4) X - habu ALTERNATE_NAMES phosphatidylcholine 2-acylhydrolase ORGANISM #formal_name Trimeresurus flavoviridis #common_name habu DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 24-Apr-1998 ACCESSIONS A25500 REFERENCE A94320 !$#authors Kini, R.M.; Kawabata, S.I.; Iwanaga, S. !$#journal Toxicon (1986) 24:1117-1129 !$#title Comparison of amino terminal region of three isoenzymes of !1phospholipases A2 (TFV PL-Ia, TFV PL-Ib, TFV PL-X) from !1Trimeresurus flavoviridis (Habu snake) venom and the !1complete amino acid sequence of the basic phospholipase, TFV !1PL-X. !$#cross-references MUID:87179112; PMID:3564060 !$#accession A25500 !'##molecule_type protein !'##residues 1-122 ##label KIN FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; homodimer; lipid !1degradation; metalloprotein; toxin; venom FEATURE !$26-122,28-44,43-95, !$49-115,50-88,57-81, !$75-86 #disulfide_bonds #status predicted\ !$27,29,31,48 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8predicted\ !$47,89 #active_site His, Asp #status predicted SUMMARY #length 122 #molecular-weight 13981 #checksum 772 SEQUENCE /// ENTRY PSRSBT #type complete TITLE phospholipase A2 (EC 3.1.1.4) crotoxin basic subunit 1 precursor - tropical rattlesnake ALTERNATE_NAMES CB1; crotoxin B, isoform beta; phosphatidylcholine 2-acylhydrolase ORGANISM #formal_name Crotalus durissus terrificus #common_name tropical rattlesnake, cascabel DATE 30-Jun-1988 #sequence_revision 30-Sep-1991 #text_change 11-Jun-1999 ACCESSIONS S02257; A90078; A94424; A49841; S45646; S46599; A26079; !1A28045; S46596 REFERENCE S01392 !$#authors Bouchier, C.; Ducancel, F.; Guignery-Frelat, G.; Bon, C.; !1Boulain, J.C.; Menez, A. !$#journal Nucleic Acids Res. (1988) 16:9050 !$#title Cloning and sequencing of cDNAs encoding the two subunits of !1crotoxin. !$#cross-references MUID:89016587; PMID:3174444 !$#accession S02257 !'##molecule_type mRNA !'##residues 1-138 ##label BOU !'##cross-references EMBL:X12603; NID:g62692; PIDN:CAA31123.1; !1PID:g62693 REFERENCE A90078 !$#authors Aird, S.D.; Kaiser, I.I.; Lewis, R.V.; Kruggel, W.G. !$#journal Arch. Biochem. Biophys. (1986) 249:296-300 !$#title A complete amino acid sequence for the basic subunit of !1crotoxin. !$#cross-references MUID:86321988; PMID:3753003 !$#accession A90078 !'##molecule_type protein !'##residues 17-80,'R',82-138 ##label AIR !'##note 49-Gln, 53-Arg, and 85-Arg were also found REFERENCE A94424 !$#authors Fraenkel-Conrat, H.; Jeng, T.W.; Hsiang, M. !$#book Natural Toxins, Eaker, D., and Wadstrom, T., eds., Pergamon !1Press, Oxford, 1980 !$#title Biological activities of crotoxin and amino acid sequence of !1crotoxin B. !$#accession A94424 !'##molecule_type protein !'##residues 17-48,'Q',50-76,'Y',77-80,'R',82-85,'K',87-114,'B',116-120, !1'B',122-138 ##label FRA REFERENCE A49841 !$#authors Landucci, E.C.T.; Condino-Neto, A.; Perez, A.C.; Hyslop, S.; !1Corrado, A.P.; Novello, J.C.; Marangoni, S.; Oliveira, B.; !1Antunes, E.; de Nucci, G. !$#journal Toxicon (1994) 32:217-226 !$#title Crotoxin induces aggregation of human washed platelets. !$#cross-references MUID:94205018; PMID:8153961 !$#accession A49841 !'##molecule_type protein !'##residues 17-36 ##label LAN REFERENCE S45646 !$#authors Faure, G.; Choumet, V.; Bouchier, C.; Camoin, L.; Guillaume, !1J.L.; Monegier, B.; Vuilhorgne, M.; Bon, C. !$#journal Eur. J. Biochem. (1994) 223:161-164 !$#title The origin of the diversity of crotoxin isoforms in the !1venom of Crotalus durissus terrificus. !$#cross-references MUID:94307256; PMID:8033889 !$#accession S45646 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 17-138 ##label FA2 !'##cross-references EMBL:X12603 !$#accession S46599 !'##molecule_type protein !'##residues 17-45 ##label FAU COMMENT Crotoxin is a beta-neurotoxin. COMPLEX heterodimer of acidic and basic subunits FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; heterodimer; lipid !1degradation; metalloprotein; myotoxin; presynaptic !1neurotoxin; venom FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-138 #product phospholipase A2 basic subunit 1 precursor !8#status experimental #label MAT\ !$20,80 #binding_site micellar substrate (Gln, Tyr) #status !8predicted\ !$42-131,44-60, !$59-111,65-138, !$66-104,73-97,91-102 #disulfide_bonds #status predicted\ !$43,45,47,64 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8predicted\ !$63,105 #active_site His, Asp #status predicted SUMMARY #length 138 #molecular-weight 15907 #checksum 1443 SEQUENCE /// ENTRY PSRSB2 #type complete TITLE phospholipase A2 (EC 3.1.1.4) crotoxin basic chain 2 precursor - tropical rattlesnake ALTERNATE_NAMES crotoxin B isoform alpha; phosphatidylcholine 2-acylhydrolase ORGANISM #formal_name Crotalus durissus terrificus #common_name tropical rattlesnake, cascabel DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 21-Jan-2000 ACCESSIONS S15068; B60265; S45647; S46598; S46597 REFERENCE S15068 !$#authors Bouchier, C.; Boulain, J.C.; Bon, C.; Menez, A. !$#journal Biochim. Biophys. Acta (1991) 1088:401-408 !$#title Analysis of cDNAs encoding the two subunits of crotoxin, a !1phospholipase A(2) neurotoxin from rattlesnake venom: the !1acidic non enzymatic subunit derives from a phospholipase A !1(2)-like precursor. !$#cross-references MUID:91198145; PMID:2015302 !$#accession S15068 !'##molecule_type mRNA !'##residues 1-138 ##label BOU !'##cross-references EMBL:X16100; NID:g62696; PIDN:CAA34227.1; !1PID:g62697 REFERENCE A60265 !$#authors Parks, T.P.; Lukas, S.; Hoffman, A.F. !$#journal Adv. Exp. Med. Biol. (1990) 275:55-81 !$#title Purification and characterization of a phospholipase A-2 !1from human osteoarthritic synovial fluid. !$#cross-references MUID:91050835; PMID:2146857 !$#accession B60265 !'##molecule_type protein !'##residues 17-41,'X' ##label PAR REFERENCE S45646 !$#authors Faure, G.; Choumet, V.; Bouchier, C.; Camoin, L.; Guillaume, !1J.L.; Monegier, B.; Vuilhorgne, M.; Bon, C. !$#journal Eur. J. Biochem. (1994) 223:161-164 !$#title The origin of the diversity of crotoxin isoforms in the !1venom of Crotalus durissus terrificus. !$#cross-references MUID:94307256; PMID:8033889 !$#accession S45647 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 17-138 ##label FAU !'##cross-references EMBL:X16100 !$#accession S46598 !'##molecule_type protein !'##residues 17-51 ##label FA2 COMMENT Crotoxin is a beta-neurotoxin. COMPLEX heterodimer of acidic and basic chains FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; heterodimer; lipid !1degradation; metalloprotein; myotoxin; presynaptic !1neurotoxin; venom FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-138 #product crotoxin basic chain 2 #status experimental !8#label MAT\ !$20,80 #binding_site micellar substrate (Gln, Tyr) #status !8predicted\ !$42-131,44-60, !$59-111,65-138, !$66-104,73-97,91-102 #disulfide_bonds #status predicted\ !$43,45,47,64 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8predicted\ !$63,105 #active_site His, Asp #status predicted SUMMARY #length 138 #molecular-weight 15968 #checksum 2186 SEQUENCE /// ENTRY I51381 #type complete TITLE phospholipase A2 (EC 3.1.1.4) Mojave toxin basic subunit precursor - Mojave rattlesnake ALTERNATE_NAMES Mtx-B; phosphatidylcholine 2-acylhydrolase ORGANISM #formal_name Crotalus scutulatus scutulatus #common_name Mojave rattlesnake DATE 13-Sep-1996 #sequence_revision 14-Feb-1997 #text_change 11-Jun-1999 ACCESSIONS I51381; A35951 REFERENCE I51380 !$#authors John, T.R.; Smith, L.A.; Kaiser, I.I. !$#journal Gene (1994) 139:229-234 !$#title Genomic sequences encoding the acidic and basic subunits of !1Mojave toxin: unusually high sequence identity of non-coding !1regions. !$#cross-references MUID:94156205; PMID:8112610 !$#accession I51381 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-138 ##label JOH !'##cross-references EMBL:U01027; NID:g451317; PIDN:AAC59674.1; !1PID:g451318 REFERENCE A35951 !$#authors Aird, S.D.; Kruggel, W.G.; Kaiser, I.I. !$#journal Toxicon (1990) 28:669-673 !$#title Amino acid sequence of the basic subunit of Mojave toxin !1from the venom of the Mojave rattlesnake (Crotalus s. !1scutulatus). !$#cross-references MUID:90385490; PMID:2402763 !$#accession A35951 !'##molecule_type protein !'##residues 17-138 ##label AIR GENETICS !$#introns 14/1; 58/2; 92/1 COMPLEX heterodimer of acidic and basic subunits FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; heterodimer; lipid !1degradation; metalloprotein; myotoxin; presynaptic !1neurotoxin; venom FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-138 #product phospholipase A2 basic chain #status !8experimental #label MAT\ !$20,80 #binding_site micellar substrate (Gln, Tyr) #status !8predicted\ !$42-131,44-60, !$59-111,65-138, !$66-104,73-97,91-102 #disulfide_bonds #status predicted\ !$43,45,47,64 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8predicted\ !$63,105 #active_site His, Asp #status predicted SUMMARY #length 138 #molecular-weight 15907 #checksum 1443 SEQUENCE /// ENTRY PSVIAA #type complete TITLE phospholipase A2 (EC 3.1.1.4) A precursor - western sand viper ALTERNATE_NAMES ammodytoxin A; phosphatidylcholine 2-acylhydrolase ORGANISM #formal_name Vipera ammodytes ammodytes #common_name western sand viper DATE 28-Feb-1986 #sequence_revision 12-Apr-1996 #text_change 28-Aug-1998 ACCESSIONS A39561; A00768 REFERENCE A39561 !$#authors Pungercar, J.; Kordis, D.; Strukelj, B.; Liang, N.S.; !1Gubensek, F. !$#journal Toxicon (1991) 29:269-273 !$#title Cloning and nucleotide sequence of a cDNA encoding !1ammodytoxin A, the most toxic phospholipase A-2 from the !1venom of long-nosed viper (Vipera ammodytes). !$#cross-references MUID:91263106; PMID:2048144 !$#accession A39561 !'##molecule_type mRNA !'##residues 1-138 ##label PUN !'##cross-references GB:X52241 REFERENCE A00768 !$#authors Ritonja, A.; Gubensek, F. !$#journal Biochim. Biophys. Acta (1985) 828:306-312 !$#title Ammodytoxin A, a highly lethal phospholipase A-2 from Vipera !1ammodytes ammodytes venom. !$#cross-references MUID:85175159; PMID:3986212 !$#accession A00768 !'##molecule_type protein !'##residues 17-138 ##label RIT COMMENT Ammodytoxin A is the most toxic presynaptically active !1phospholipase A2 isolated from this species. FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; lipid degradation; !1metalloprotein; presynaptic neurotoxin; venom FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-138 #product phospholipase A2 A #status experimental !8#label MAT\ !$42-138,44-60, !$59-111,66-104, !$73-97,91-102 #disulfide_bonds #status predicted\ !$43,45,47,64 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8predicted\ !$63,105 #active_site His, Asp #status predicted SUMMARY #length 138 #molecular-weight 15531 #checksum 9548 SEQUENCE /// ENTRY PSVIAC #type complete TITLE phospholipase A2 (EC 3.1.1.4) C precursor - western sand viper ALTERNATE_NAMES ammodytoxin C; phosphatidylcholine 2-acylhydrolase ORGANISM #formal_name Vipera ammodytes ammodytes #common_name western sand viper DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 11-Jun-1999 ACCESSIONS S04587; S06853 REFERENCE S04587 !$#authors Pungercar, J.; Kordis, D.; Jerala, R.; Trstenjak-Prebanda, !1M.; Dolinar, M.; Curin-Serbec, V.; Komel, R.; Gubensek, F. !$#journal Nucleic Acids Res. (1989) 17:4367 !$#title Amino acid sequence of ammodytoxin C as deduced from cDNA. !$#cross-references MUID:89296479; PMID:2740219 !$#accession S04587 !'##molecule_type mRNA !'##residues 1-138 ##label PUN !'##cross-references EMBL:X15138; NID:g64448; PIDN:CAA33238.1; !1PID:g64449 REFERENCE S06853 !$#authors Krizaj, I.; Turk, D.; Ritonja, A.; Gubensek, F. !$#journal Biochim. Biophys. Acta (1989) 999:198-202 !$#title Primary structure of ammodytoxin C further reveals the toxic !1site of ammodytoxin. !$#cross-references MUID:90089469; PMID:2597708 !$#accession S06853 !'##molecule_type protein !'##residues 17-138 ##label KRI FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; homodimer; lipid !1degradation; metalloprotein; toxin; venom FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-138 #product phospholipase A2 C #status experimental !8#label MAT\ !$42-131,44-60, !$59-111,65-138, !$66-104,73-97,91-102 #disulfide_bonds #status predicted\ !$43,45,47,64 #binding_site calcium (Tyr, Gly, Gly, Asp) #status !8predicted\ !$63,105 #active_site His, Asp #status predicted SUMMARY #length 138 #molecular-weight 15498 #checksum 9479 SEQUENCE /// ENTRY PSSNAM #type complete TITLE phospholipase A2 homolog, inactive [validated] - eastern cottonmouth ORGANISM #formal_name Agkistrodon piscivorus piscivorus #common_name eastern cottonmouth DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 15-Sep-2000 ACCESSIONS A00767; A60719 REFERENCE A00767 !$#authors Maraganore, J.M.; Heinrikson, R.L. !$#journal J. Biol. Chem. (1986) 261:4797-4804 !$#title The lysine-49 phospholipase A-2 from the venom of !1Agkistrodon piscivorus piscivorus. Relation of structure and !1function to other phospholipases A-2. !$#cross-references MUID:86168190; PMID:3082870 !$#accession A00767 !'##molecule_type protein !'##residues 1-121 ##label MAR REFERENCE A60719 !$#authors van den Bergh, C.J.; Slotboom, A.J.; Verheij, H.M.; de Haas, !1G.H. !$#journal J. Cell. Biochem. (1989) 39:379-390 !$#title The role of Asp-49 and other conserved amino acids in !1phospholipases A2 and their importance for enzymatic !1activity. !$#cross-references MUID:89255682; PMID:2722967 !$#accession A60719 !'##molecule_type protein !'##residues 1-8 ##label VAN !'##note the authors confirmed the identity of the purified protein by !1composition and peptide sequencing and showed that residual !1all activity belonged to a contaminating enzyme REFERENCE A51920 !$#authors Holland, D.R.; Clancy, L.L.; Muchmore, S.W.; Rydel, T.J.; !1Einspahr, H.M.; Finzel, B.C.; Heinrikson, R.L.; Watenpaugh, !1K.D. !$#submission submitted to the Brookhaven Protein Data Bank, October 1991 !$#cross-references PDB:1PPA !$#contents annotation; X-ray crystallography, 2.0 angstroms, residues !11-121 REFERENCE A39221 !$#authors Holland, D.R.; Clancy, L.L.; Muchmore, S.W.; Ryde, T.J.; !1Einspahr, H.M.; Finzel, B.C.; Heinrikson, R.L.; Watenpaugh, !1K.D. !$#journal J. Biol. Chem. (1990) 265:17649-17656 !$#title The crystal structure of a lysine 49 phospholipase A-2 from !1the venom of the cottonmouth snake at 2.0-angstrom !1resolution. !$#cross-references MUID:91009222; PMID:2120215 !$#contents annotation; X-ray crystallography, 2.0 angstroms COMMENT This homolog of phospholipase A2 lacks enzymatic activity !1because a Lys-48 replaces a conserved Asp in the calcium !1binding site. CLASSIFICATION #superfamily phospholipase A2 KEYWORDS venom FEATURE !$26-115,28-44,43-95, !$49-121,50-88,57-81, !$75-86 #disulfide_bonds #status experimental SUMMARY #length 121 #molecular-weight 13961 #checksum 9961 SEQUENCE /// ENTRY PC4024 #type fragment TITLE phospholipase A2 homolog bothropstoxin I precursor - jararacussu (fragment) ORGANISM #formal_name Bothrops jararacussu #common_name jararacussu DATE 26-Jun-1995 #sequence_revision 14-Feb-1997 #text_change 11-Jun-1999 ACCESSIONS PC4024; A53869 REFERENCE PC4024 !$#authors Ward, R.J.; Monesi, N.; Arni, R.K.; Larson, R.E.; !1Paco-Larson, M.L. !$#journal Gene (1995) 156:305-306 !$#title Sequence of a cDNA encoding bothropstoxin I, a myotoxin from !1the venom of Bothrops jararacussu. !$#cross-references MUID:95278763; PMID:7758974 !$#accession PC4024 !'##molecule_type mRNA !'##residues 1-121 ##label WAR !'##cross-references EMBL:X78599; NID:g509462; PIDN:CAA55334.1; !1PID:g987018 !'##experimental_source venom !'##note the authors do not provide either the complete nucleotide !1sequence or its translation REFERENCE A53869 !$#authors Cintra, A.C.; Marangoni, S.; Oliveira, B.; Giglio, J.R. !$#journal J. Protein Chem. (1993) 12:57-64 !$#title Bothropstoxin-I: amino acid sequence and function. !$#cross-references MUID:93151968; PMID:8427634 !$#accession A53869 !'##molecule_type protein !'##residues 1-20,'Y',22-57,'N',59-119,'P',121 ##label CIN !'##experimental_source venom !'##note sequence extracted from NCBI backbone (NCBIP:124611) COMMENT This protein has potent myotoxic activity, but has no !1detectable phospholipase A2 activity. FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid CLASSIFICATION #superfamily phospholipase A2 KEYWORDS myotoxin; venom FEATURE !$1-121 #product bothropstoxin I #status experimental #label !8MAT\ !$26-115,28-44,43-95, !$49-121,50-88,57-81, !$75-86 #disulfide_bonds #status predicted SUMMARY #length 121 #checksum 1342 SEQUENCE /// ENTRY JC4877 #type complete TITLE phospholipase A2 homolog 3 precursor - himehabu ORGANISM #formal_name Trimeresurus okinavensis #common_name himehabu DATE 15-Aug-1996 #sequence_revision 14-Feb-1997 #text_change 11-Jun-1999 ACCESSIONS JC4877 REFERENCE JC4874 !$#authors Nobuhisa, I.; Nakashima, K.; Deshimaru, M.; Ogawa, T.; !1Shimohigashi, Y.; Fukumaki, Y.; Sakaki, Y.; Hattori, S.; !1Kihara, H.; Ohno, M. !$#journal Gene (1996) 172:267-272 !$#title Accelerated evolution of Trimeresurus okinavensis venom !1gland phospholipase A2 isozyme-encoding genes. !$#cross-references MUID:96269416; PMID:8682315 !$#contents venom gland !$#accession JC4877 !'##molecule_type mRNA !'##residues 1-137 ##label NOB !'##cross-references DDBJ:D49389; NID:g1469806; PIDN:BAA08384.1; !1PID:g1469807 COMMENT This protein probably does not have phospholipase A2 !1activity. CLASSIFICATION #superfamily phospholipase A2 KEYWORDS venom FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-137 #product phospholipase A2 homolog 3 #status predicted !8#label MAT\ !$42-131,44-60, !$59-111,65-137, !$66-104,73-97,91-102 #disulfide_bonds #status predicted SUMMARY #length 137 #molecular-weight 15453 #checksum 6454 SEQUENCE /// ENTRY PSGHA5 #type complete TITLE phospholipase A2 (EC 3.1.1.4) - Gila monster ALTERNATE_NAMES phosphatidylcholine 2-acylhydrolase ORGANISM #formal_name Heloderma suspectum #common_name Gila monster DATE 30-Sep-1991 #sequence_revision 01-Dec-2000 #text_change 01-Dec-2000 ACCESSIONS S14764; S07090 REFERENCE S14764 !$#authors Vandermeers, A.; Vandermeers-Piret, M.C.; Vigneron, L.; !1Rathe, J.; Stievenart, M.; Christophe, J. !$#journal Eur. J. Biochem. (1991) 196:537-544 !$#title Differences in primary structure among five phospholipases A !1(2) from Heloderma suspectum. !$#cross-references MUID:91192022; PMID:2013276 !$#accession S14764 !'##status preliminary !'##molecule_type protein !'##residues 1-143 ##label VAN REFERENCE S07090 !$#authors Gomez, F.; Vandermeers, A.; Vandermeers-Piret, M.C.; Herzog, !1R.; Rathe, J.; Stievenart, M.; Winand, J.; Christophe, J. !$#journal Eur. J. Biochem. (1989) 186:23-33 !$#title Purification and characterization of five variants of !1phospholipase A(2) and complete primary structure of the !1main phospholipase A(2) variant in Heloderma suspectum (Gila !1monster) venom. !$#cross-references MUID:90092105; PMID:2480893 !$#accession S07090 !'##molecule_type protein !'##residues 1-142 ##label GOM FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; lipid degradation; !1metalloprotein; toxin; venom FEATURE !$11-33,32-72,39-65 #disulfide_bonds #status predicted\ !$20,22,24,37 #binding_site calcium (Tyr, Gln, Gly, Asp) #status !8predicted\ !$36,66 #active_site His, Asp #status predicted SUMMARY #length 143 #molecular-weight 16048 #checksum 2268 SEQUENCE /// ENTRY PSHBA #type fragment TITLE phospholipase A2 (EC 3.1.1.4) precursor [validated] - honeybee (fragment) ALTERNATE_NAMES phosphatidylcholine 2-acylhydrolase ORGANISM #formal_name Apis mellifera #common_name honeybee DATE 24-Apr-1984 #sequence_revision 30-Sep-1991 #text_change 15-Sep-2000 ACCESSIONS S05650; A00770 REFERENCE S05650 !$#authors Kuchler, K.; Gmachl, M.; Sippl, M.J.; Kreil, G. !$#journal Eur. J. Biochem. (1989) 184:249-254 !$#title Analysis of the cDNA for phospholipase A(2) from honeybee !1venom glands. The deduced amino acid sequence reveals !1homology to the corresponding vertebrate enzymes. !$#cross-references MUID:89377864; PMID:2776767 !$#accession S05650 !'##molecule_type mRNA !'##residues 1-162 ##label KUC !'##cross-references EMBL:X16709; NID:g5626; PIDN:CAA34681.1; PID:g5627 REFERENCE A91226 !$#authors Shipolini, R.A.; Callewaert, G.L.; Cottrell, R.C.; Vernon, !1C.A. !$#journal Eur. J. Biochem. (1974) 48:465-476 !$#title The amino-acid sequence and carbohydrate content of !1phospholipase A-2 from bee venom. !$#cross-references MUID:75093311; PMID:4448181 !$#accession A00770 !'##molecule_type protein !'##residues 29-66,'N',68-79,'N',81-83,86-89,'NNN',93,95-96,100-119,'N', !1121-162 ##label SHI REFERENCE A91227 !$#authors Shipolini, R.A.; Doonan, S.; Vernon, C.A. !$#journal Eur. J. Biochem. (1974) 48:477-483 !$#title The disulphide bridges of phospholipase A-2 from bee venom. !$#cross-references MUID:75093312; PMID:4614976 !$#contents annotation; disulfide bonds !$#note the presence of disulfide bonds between residues 37-58, !159-123, 65-141, and 89-133, as determined in this paper, was !1questioned (reference S05650) as being based on a sequence !1lacking Cys-91 and Cys-98 (from reference A00770) REFERENCE A51346 !$#authors Scott, D.L.; Otwinowski, Z.; Sigler, P.B. !$#submission submitted to the Brookhaven Protein Data Bank, September !11992 !$#cross-references PDB:1POC !$#contents annotation; X-ray crystallography, 2.0 angstroms, residues !129-162 REFERENCE A58471 !$#authors Scott, D.L.; Otwinowski, Z.; Gelb, M.H.; Sigler, P.B. !$#journal Science (1990) 250:1563-1566 !$#title Crystal structure of bee-venom phospholipase A2 in a complex !1with a transition-state analogue. !$#cross-references MUID:91111081; PMID:2274788 !$#contents annotation; X-ray crystallography, 2.0 angstroms; disulfide !1bonds FUNCTION !$#description catalyzes hydrolysis of 1, !12-diacyl-sn-glycero-3-phosphocholine to !11-acyl-sn-3-glycero-phosphocholine and fatty acid !$#note the reaction is strongly enhanced when the phospholipid is !1condensed into a micellar aggregate CLASSIFICATION #superfamily phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; glycoprotein; lipid !1degradation; metalloprotein; toxin; venom FEATURE !$1-13 #domain signal sequence (fragment) #status predicted !8#label SIG\ !$14-28 #domain propeptide #status predicted #label PRO\ !$29-162 #product phospholipase A2 #status experimental #label !8MAT\ !$36,38,40,63 #binding_site calcium (Trp, Gly, Gly, Asp) #status !8experimental\ !$37-59,58-98,65-91, !$89-123,133-141 #disulfide_bonds #status experimental\ !$41 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$62,92 #active_site His, Asp #status predicted SUMMARY #length 162 #checksum 1489 SEQUENCE /// ENTRY A39329 #type complete TITLE phospholipase A2 (EC 3.1.1.4), cytosolic - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 20-Apr-2000 ACCESSIONS A39329; A39898; A54198; S68898 REFERENCE A39329 !$#authors Sharp, J.D.; White, D.L.; Chiou, X.G.; Goodson, T.; Gamboa, !1G.C.; McClure, D.; Burgett, S.; Hoskins, J.; Skatrud, P.L.; !1Sportsman, J.R.; Becker, G.W.; Kang, L.H.; Roberts, E.F.; !1Kramer, R.M. !$#journal J. Biol. Chem. (1991) 266:14850-14853 !$#title Molecular cloning and expression of human Ca(2+)-sensitive !1cytosolic phospholipase A-2. !$#cross-references MUID:91331987; PMID:1869522 !$#accession A39329 !'##molecule_type mRNA !'##residues 1-749 ##label SHA !'##cross-references GB:M68874; NID:g190003; PIDN:AAA60105.1; !1PID:g190004 !'##note part of this sequence was confirmed by protein sequencing REFERENCE A39898 !$#authors Clark, J.D.; Lin, L.L.; Kriz, R.W.; Ramesha, C.S.; Sultzman, !1L.A.; Lin, A.Y.; Milona, N.; Knopf, J.L. !$#journal Cell (1991) 65:1043-1051 !$#title A novel arachidonic acid-selective cytosolic PLA-2 contains !1a Ca(2+)-dependent translocation domain with homology to PKC !1and GAP. !$#cross-references MUID:91256305; PMID:1904318 !$#accession A39898 !'##molecule_type mRNA !'##residues 1-749 ##label CLA !'##cross-references GB:M72393; NID:g190006; PIDN:AAB00789.1; !1PID:g190007 !'##note part of this sequence was confirmed by protein sequencing REFERENCE A54198 !$#authors Li, B.; Copp, L.; Castelhano, A.L.; Feng, R.; Stahl, M.; !1Yuan, Z.; Krantz, A. !$#journal Biochemistry (1994) 33:8594-8603 !$#title Inactivation of a cytosolic phospholipase A-2 by !1thiol-modifying reagents: cysteine residues as potential !1targets of phospholipase A-2. !$#cross-references MUID:94304876; PMID:8031794 !$#accession A54198 !'##molecule_type protein !'##residues 319-338,'X',340-345,'X',347-358 ##label LIA !'##note modification of preferred modification site Cys-324 abolished !1enzymatic activity REFERENCE S68897 !$#authors Gordon, R.D.; Leighton, I.A.; Campbell, D.G.; Cohen, P.; !1Creaney, A.; Wilton, D.C.; Masters, D.J.; Ritchie, G.A.F.; !1Mott, R.; Taylor, I.W.F.; Bundell, K.R.; Douglas, L.; !1Morten, J.; Needham, M. !$#journal Eur. J. Biochem. (1996) 238:690-697 !$#title Cloning and expression of cytosolic phospholipase A(2) (cPLA !1(2)) and a naturally occurring variant. Phosphorylation of !1Ser505 of recombinant cPLA(2) by p42 mitogen-activated !1protein kinase results in an increase in specific activity. !$#cross-references MUID:96300233; PMID:8706669 !$#accession S68898 !'##molecule_type protein !'##residues 497-507 ##label GOR COMMENT This cytosolic phospholipase A2 translocates to membrane !1vesicles in response to calcium and selectively cleaves !1arachidonic acid from vesicles. GENETICS !$#gene GDB:PLA2G4A; PLA2G4 !'##cross-references GDB:134687; OMIM:600522 !$#map_position 1q25-1q25 CLASSIFICATION #superfamily cytosolic phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; cytosol; inflammation; !1phosphoprotein FEATURE !$505 #binding_site phosphate (Ser) (covalent) #status !8experimental SUMMARY #length 749 #molecular-weight 85210 #checksum 5276 SEQUENCE /// ENTRY B39898 #type complete TITLE phospholipase A2 (EC 3.1.1.4), cytosolic - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B39898 REFERENCE A39898 !$#authors Clark, J.D.; Lin, L.L.; Kriz, R.W.; Ramesha, C.S.; Sultzman, !1L.A.; Lin, A.Y.; Milona, N.; Knopf, J.L. !$#journal Cell (1991) 65:1043-1051 !$#title A novel arachidonic acid-selective cytosolic PLA-2 contains !1a Ca(2+)-dependent translocation domain with homology to PKC !1and GAP. !$#cross-references MUID:91256305; PMID:1904318 !$#accession B39898 !'##molecule_type mRNA !'##residues 1-749 ##label CLA !'##cross-references GB:M72394 COMMENT This cytosolic phospholipase A2 translocates to membrane !1vesicles in response to calcium and selectively cleaves !1arachidonic acid from vesicles. CLASSIFICATION #superfamily cytosolic phospholipase A2 KEYWORDS calcium; carboxylic ester hydrolase; cytosol; inflammation SUMMARY #length 749 #molecular-weight 85337 #checksum 4092 SEQUENCE /// ENTRY I50699 #type complete TITLE cytosolic phospholipase A2 - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS I50699 REFERENCE A54908 !$#authors Nalefski, E.A.; Sultzman, L.A.; Martin, D.M.; Kriz, R.W.; !1Towler, P.S.; Knopf, J.L.; Clark, J.D. !$#journal J. Biol. Chem. (1994) 269:18239-18249 !$#title Delineation of two functionally distinct domains of !1cytosolic phospholipase A2, a regulatory Ca(2+)-dependent !1lipid-binding domain and a Ca(2+)-independent catalytic !1domain. !$#cross-references MUID:94299545; PMID:8027085 !$#accession I50699 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-748 ##label NAL !'##cross-references EMBL:U10329; NID:g508624; PIDN:AAA53228.1; !1PID:g508625 CLASSIFICATION #superfamily cytosolic phospholipase A2 KEYWORDS cytosol SUMMARY #length 748 #molecular-weight 84978 #checksum 9398 SEQUENCE /// ENTRY PSHUAM #type complete TITLE 14-3-3 protein zeta - human ALTERNATE_NAMES factor activating exoenzyme S (FAS); phospholipase A2, acyl-enzyme intermediate-forming [misidentification]; tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 04-Feb-2000 ACCESSIONS A38246; D61013; G01870 REFERENCE A38246 !$#authors Zupan, L.A.; Steffens, D.L.; Berry, C.A.; Landt, M.; Gross, !1R.W. !$#journal J. Biol. Chem. (1992) 267:8707-8710 !$#title Cloning and expression of a human 14-3-3 protein mediating !1phospholipolysis. Identification of an arachidonoyl-enzyme !1intermediate during catalysis. !$#cross-references MUID:92250445; PMID:1577711 !$#accession A38246 !'##molecule_type mRNA !'##residues 1-245 ##label ZUP !'##cross-references GB:M86400; NID:g189952; PIDN:AAA36446.1; !1PID:g189953 REFERENCE A61002 !$#authors Bauw, G.; Rasmussen, H.H.; Van Den Bulcke, M.; Van Damme, !1J.; Puype, M.; Gesser, B.; Celis, J.E.; Vandekerckhove, J. !$#journal Electrophoresis (1990) 11:528-536 !$#title Two-dimensional gel electrophoresis, protein electroblotting !1and microsequencing: a direct link between proteins and !1genes. !$#cross-references MUID:91031404; PMID:1699755 !$#accession D61013 !'##molecule_type protein !'##residues 140-150 ##label BAU REFERENCE G08674 !$#authors Seluja, G.A. !$#submission submitted to the EMBL Data Library, June 1995 !$#accession G01870 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-245 ##label SEL !'##cross-references EMBL:U28964; NID:g899458; PIDN:AAC52052.1; !1PID:g899459 COMMENT The identification of this protein as a phospholipase has !1been questioned. In known examples of phospholipase A2, !1cleavage of ester linkages leads to the release of free !1fatty acids. This intracellular protein was thought to form !1a stable arachidonoyl-enzyme intermediate which could, in !1principle, transfer arachidonic acid to acceptors other than !1water without the release of free arachidonic acid. GENETICS !$#gene GDB:YWHAZ !'##cross-references GDB:217085; OMIM:601288 !$#map_position 2p25.2-2p25.1 CLASSIFICATION #superfamily 14-3-3 protein KEYWORDS acetylated amino end; dimer; phosphoprotein FEATURE !$1 #modified_site acetylated amino end (Met) #status !8predicted\ !$184 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 245 #molecular-weight 27745 #checksum 2074 SEQUENCE /// ENTRY JC1122 #type complete TITLE 14-3-3 protein - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JC1122 REFERENCE JC1122 !$#authors Swanson, K.D.; Ganguly, R. !$#journal Gene (1992) 113:183-190 !$#title Characterization of a Drosophila melanogaster gene similar !1to the mammalian genes encoding the tyrosine/tryptophan !1hydroxylase activator and protein kinase C inhibitor !1proteins. !$#cross-references MUID:92241667; PMID:1349290 !$#accession JC1122 !'##molecule_type mRNA !'##residues 1-248 ##label SWA !'##cross-references GB:M77518; NID:g156782; PIDN:AAA28324.1; !1PID:g156783 GENETICS !$#gene D14-3-3 !'##cross-references FlyBase:FBgn0004907 CLASSIFICATION #superfamily 14-3-3 protein SUMMARY #length 248 #molecular-weight 28227 #checksum 9181 SEQUENCE /// ENTRY S30863 #type complete TITLE BMH1 protein - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES 14-3-3 protein homolog; protein YER177w ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-Nov-1999 ACCESSIONS S30863; S50680; S21151; S42684; S29896 REFERENCE S30812 !$#authors Mulligan, J.T.; Dietrich, F.S.; Hennessey, K.M.; Sehl, P.; !1Komp, C.; Wei, Y.; Taylor, P.; Nakahara, K.; Roberts, D.; !1Davis, R.W. !$#submission submitted to the EMBL Data Library, February 1993 !$#accession S30863 !'##molecule_type DNA !'##residues 1-267 ##label MUL !'##cross-references GB:U18922; EMBL:L11229; NID:g603405; !1PIDN:AAB64704.1; PID:g603418 REFERENCE S50680 !$#authors Dietrich, F.S. !$#submission submitted to the EMBL Data Library, December 1994 !$#description The sequence of S. cerevisiae cosmids 9163 and 9132. !$#accession S50680 !'##molecule_type DNA !'##residues 1-267 ##label DIE !'##cross-references EMBL:U18922; NID:g603405; PIDN:AAB64704.1; !1PID:g603418; GSPDB:GN00005; MIPS:YER177w REFERENCE S21151 !$#authors van Heusden, G.P.H.; Wenzel, T.J.; Lagendijk, E.L.; de !1Steensma, H.Y.; van den Berg, J.A. !$#journal FEBS Lett. (1992) 302:145-150 !$#title Characterization of the yeast BMH1 gene encoding a putative !1protein homologous to mammalian protein kinase II activators !1and protein kinase C inhibitors. !$#cross-references MUID:92339501; PMID:1378790 !$#accession S21151 !'##molecule_type DNA !'##residues 1-196,'R',198-262,'VKHQSKYSDKSKEKLLKKRKKKERGCNNL' ##label !1HEU !'##cross-references EMBL:X66206 REFERENCE S42684 !$#authors Wenzel, T.J.; Zuurmond, A.M.; Bergmans, A.; van den Berg, !1J.A.; Steensma, H.Y. !$#journal Yeast (1994) 10:297-308 !$#title Promoter analysis of the PDA1 gene encoding the E1-alpha !1subunit of the pyruvate dehydrogenase complex from !1Saccharomyces cerevisiae. !$#cross-references MUID:94287707; PMID:8017100 !$#accession S42684 !'##status translation not shown !'##molecule_type DNA !'##residues 98-196,'R',198-262,'VKHQSKYSDKSKEKLLKKRKKKERGCNNL' ##label !1WEN !'##cross-references EMBL:X71664; NID:g298058; PIDN:CAA50656.1; !1PID:g832919 GENETICS !$#gene SGD:BMH1; MIPS:YER177w !'##cross-references SGD:S0000979; MIPS:YER177w !$#map_position 5R CLASSIFICATION #superfamily 14-3-3 protein SUMMARY #length 267 #molecular-weight 30091 #checksum 711 SEQUENCE /// ENTRY S31975 #type complete TITLE 14-3-3 protein epsilon, renal - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS I48337; S31975 REFERENCE I48337 !$#authors McConnell, J.E.; Armstrong, J.F.; Hodges, P.E.; Bard, J.B. !$#journal Dev. Biol. (1995) 169:218-228 !$#title The mouse 14-3-3 epsilon isoform, a kinase regulator whose !1expression pattern is modulated in mesenchyme and neuronal !1differentiation. !$#cross-references MUID:95269876; PMID:7750640 !$#accession I48337 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-255 ##label RES !'##cross-references EMBL:Z19599; NID:g57965; PIDN:CAA79659.1; !1PID:g57966 CLASSIFICATION #superfamily 14-3-3 protein KEYWORDS kidney SUMMARY #length 255 #molecular-weight 29174 #checksum 6763 SEQUENCE /// ENTRY S38861 #type complete TITLE 14-3-3 protein homolog - pumpkin ALTERNATE_NAMES endonuclease, 32K ORGANISM #formal_name Cucurbita pepo #common_name pumpkin DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S38861 REFERENCE S38861 !$#authors Szopa, J. !$#submission submitted to the EMBL Data Library, November 1993 !$#accession S38861 !'##molecule_type mRNA !'##residues 1-275 ##label SZO !'##cross-references EMBL:X76086; NID:g429161; PIDN:CAA53700.1; !1PID:g429162 CLASSIFICATION #superfamily 14-3-3 protein KEYWORDS endonuclease SUMMARY #length 275 #molecular-weight 31106 #checksum 4629 SEQUENCE /// ENTRY A47237 #type complete TITLE 14-3-3 protein homolog GF14 - Arabidopsis thaliana ALTERNATE_NAMES G-box-binding factor GF14 ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A47237 REFERENCE A47237 !$#authors Lu, G.; DeLisle, A.J.; de Vetten, N.C.; Ferl, R.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:11490-11494 !$#title Brain proteins in plants: an Arabidopsis homolog to !1neurotransmitter pathway activators is part of a DNA binding !1complex. !$#cross-references MUID:93087554; PMID:1454838 !$#accession A47237 !'##status preliminary !'##molecule_type mRNA !'##residues 1-259 ##label LU1 !'##cross-references GB:M96855; NID:g553039; PIDN:AAA32798.1; !1PID:g553040 !'##note sequence extracted from NCBI backbone (NCBIN:119782, !1NCBIP:119783) CLASSIFICATION #superfamily 14-3-3 protein SUMMARY #length 259 #molecular-weight 29161 #checksum 3005 SEQUENCE /// ENTRY JQ1680 #type complete TITLE 14-3-3 protein homolog GF14-12 - maize ORGANISM #formal_name Zea mays #common_name maize DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JQ1680 REFERENCE JQ1680 !$#authors de Vetten, N.C.; Lu, G.; Ferl, R.J. !$#journal Plant Cell (1992) 4:1295-1307 !$#title A maize protein associated with the G-box binding complex !1has homology to brain regulatory proteins. !$#cross-references MUID:93076113; PMID:1446170 !$#accession JQ1680 !'##molecule_type mRNA !'##residues 1-248 ##label DEV !'##cross-references GB:M96856; NID:g168602; PIDN:AAA33505.1; !1PID:g168603 COMMENT Residues 75-Ile, 82-Ile, 89-Ile, and 96-Leu are involved in !1protein-protein interaction. CLASSIFICATION #superfamily 14-3-3 protein KEYWORDS phosphoprotein FEATURE !$52 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 248 #molecular-weight 28155 #checksum 8279 SEQUENCE /// ENTRY S30927 #type complete TITLE 14-3-3 protein homolog - rice ORGANISM #formal_name Oryza sativa #common_name rice DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S30927 REFERENCE S30927 !$#authors Kidou, S.; Umeda, M.; Kato, A.; Uchimiya, H. !$#journal Plant Mol. Biol. (1993) 21:191-194 !$#title Isolation and characterization of a rice cDNA similar to the !1bovine brain-specific 14-3-3 protein gene. !$#cross-references MUID:93144687; PMID:7678761 !$#accession S30927 !'##molecule_type mRNA !'##residues 1-260 ##label KID !'##cross-references EMBL:D16140; NID:g303858; PIDN:BAA03711.1; !1PID:g303859 !'##note the authors translated the codon AAC for residue 124 as Lys CLASSIFICATION #superfamily 14-3-3 protein SUMMARY #length 260 #molecular-weight 29129 #checksum 6356 SEQUENCE /// ENTRY S18911 #type complete TITLE 14-3-3 protein homolog - barley ALTERNATE_NAMES protein kinase regulator homolog ORGANISM #formal_name Hordeum vulgare #common_name barley DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S18911 REFERENCE S18911 !$#authors Brandt, J.; Thordal-Christensen, H.; Vad, K.; Gregersen, !1P.L.; Collinge, D.B. !$#submission submitted to the EMBL Data Library, December 1991 !$#description A pathogen-induced gene of barley encodes a protein showing !1high similarity to a protein kinase regulator. !$#accession S18911 !'##molecule_type mRNA !'##residues 1-261 ##label BRA !'##cross-references EMBL:X62388; NID:g22606; PIDN:CAA44259.1; !1PID:g22607 CLASSIFICATION #superfamily 14-3-3 protein SUMMARY #length 261 #molecular-weight 29265 #checksum 7739 SEQUENCE /// ENTRY PSECL2 #type complete TITLE lysophospholipase (EC 3.1.1.5) L2 - Escherichia coli (strain K-12) ALTERNATE_NAMES 2-lysophosphatidylcholine acylhydrolase; lecithinase B ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 10-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS B65187; A24131; S30715 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65187 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-340 ##label BLAT !'##cross-references GB:AE000458; GB:U00096; NID:g2367299; !1PIDN:AAC76828.1; PID:g2367303; UWGP:b3825 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A24131 !$#authors Kobayashi, T.; Kudo, I.; Karasawa, K.; Mizushima, H.; Inoue, !1K.; Nojima, S. !$#journal J. Biochem. (1985) 98:1017-1025 !$#title Nucleotide sequence of the pldB gene and characteristics of !1deduced amino acid sequence of lysophospholipase L2 in !1Escherichia coli. !$#cross-references MUID:86085747; PMID:3908445 !$#accession A24131 !'##molecule_type DNA !'##residues 1-314,'R',316-340 ##label KOB !'##cross-references GB:X03155; NID:g42426; PIDN:CAA26932.1; PID:g42427 !'##experimental_source strain KL16-99 REFERENCE S30660 !$#authors Daniels, D.L.; Plunkett III, G.; Burland, V.; Blattner, F.R. !$#journal Science (1992) 257:771-778 !$#title Analysis of the Escherichia coli genome: DNA sequence of the !1region from 84.5 to 86.5 minutes. !$#cross-references MUID:92358234; PMID:1379743 !$#accession S30715 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-163,'A',165-200,'XX',203-340 ##label DAN !'##cross-references EMBL:M87049; NID:g836656; PIDN:AAA67621.1; !1PID:g148224 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1992 COMMENT This enzyme is localized in the inner membrane. GENETICS !$#gene pldB !$#map_position 85 min CLASSIFICATION #superfamily lysophospholipase L2 KEYWORDS carboxylic ester hydrolase; lipid biosynthesis; membrane !1protein SUMMARY #length 340 #molecular-weight 38893 #checksum 4022 SEQUENCE /// ENTRY ACHU #type complete TITLE cholinesterase (EC 3.1.1.8) precursor [validated] - human ALTERNATE_NAMES acylcholine acylhydrolase; butyrylcholinesterase; choline esterase II; nonspecific cholinesterase; pseudocholinesterase ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1987 #sequence_revision 23-Feb-1996 #text_change 08-Dec-2000 ACCESSIONS A33769; A26613; A33887; A34668; A00772 REFERENCE A33769 !$#authors Arpagaus, M.; Kott, M.; Vatsis, K.P.; Bartels, C.F.; La Du, !1B.N.; Lockridge, O. !$#journal Biochemistry (1990) 29:124-131 !$#title Structure of the gene for human butyrylcholinesterase. !1Evidence for a single copy. !$#cross-references MUID:90212557; PMID:2322535 !$#accession A33769 !'##molecule_type DNA !'##residues 'MSVQSNLQAGAAAASCISPKYYMIFTPCKLCHLCCRESEIN',1-602 ##label !1ARP !'##cross-references GB:M32391; GB:J02879 !'##note two ATG codons found upstream of Met-1 do not lie in a !1favorable context for translation initiation REFERENCE A26613 !$#authors Prody, C.A.; Zevin-Sonkin, D.; Gnatt, A.; Goldberg, O.; !1Soreq, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:3555-3559 !$#title Isolation and characterization of full-length cDNA clones !1coding for cholinesterase from fetal human tissues. !$#cross-references MUID:87231856; PMID:3035536 !$#accession A26613 !'##molecule_type mRNA !'##residues 1-133,'D',135-602 ##label PRO REFERENCE A33887 !$#authors McTiernan, C.; Adkins, S.; Chatonnet, A.; Vaughan, T.A.; !1Bartels, C.F.; Kott, M.; Rosenberry, T.L.; La Du, B.N.; !1Lockridge, O. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:6682-6686 !$#title Brain cDNA clone for human cholinesterase. !$#cross-references MUID:88016155; PMID:3477799 !$#accession A33887 !'##molecule_type mRNA !'##residues 'MSVQSNLQAGAAAASCISPKYYMIFTPCKLYHLCCRESEIN',1-602 ##label !1MCT !'##note two ATG codons found upstream of Met-1 do not lie in a !1favorable context for translation initiation REFERENCE A34668 !$#authors Nogueira, C.P.; McGuire, M.C.; Graeser, C.; Bartels, C.F.; !1Arpagaus, M.; Van der Spek, A.F.L.; Lightstone, H.; !1Lockridge, O.; La Du, B.N. !$#journal Am. J. Hum. Genet. (1990) 46:934-942 !$#title Identification of a frameshift mutation responsible for the !1silent phenotype of human serum cholinesterase, Gly 117 !1(GGT--GGAG). !$#cross-references MUID:90252779; PMID:2339692 !$#accession A34668 !'##molecule_type DNA !'##residues 143-145,'VSNWNIIFTCL' ##label NOG !'##note frameshift mutant in codon for residue 145 (Gly) REFERENCE A00772 !$#authors Lockridge, O.; Bartels, C.F.; Vaughan, T.A.; Wong, C.K.; !1Norton, S.E.; Johnson, L.L. !$#journal J. Biol. Chem. (1987) 262:549-557 !$#title Complete amino acid sequence of human serum cholinesterase. !$#cross-references MUID:87109144; PMID:3542989 !$#accession A00772 !'##molecule_type protein !'##residues 29-602 ##label LOC !'##experimental_source plasma COMMENT Cholinesterase is present in most cells (except !1erythrocytes). GENETICS !$#gene GDB:BCHE; CHE1 !'##cross-references GDB:120558; OMIM:177400 !$#map_position 3q26.1-3q26.2 !$#introns 506/2; 562/1 FUNCTION !$#description hydrolyzes acylcholines to choline and a carboxylic acid !$#note this cholinesterase is highly reactive with organophosphate !1esters CLASSIFICATION #superfamily cholinesterase; cholinesterase homology KEYWORDS carboxylic ester hydrolase; glycoprotein; homotetramer FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-602 #product cholinesterase #status experimental #label !8MAT\ !$56-556 #domain cholinesterase homology #label CHE\ !$45,85,134,269,284, !$369,483,509,514 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$226 #active_site Ser #status experimental SUMMARY #length 602 #molecular-weight 68418 #checksum 9813 SEQUENCE /// ENTRY ACRYE #type complete TITLE acetylcholinesterase (EC 3.1.1.7) precursor, 11S form [validated] - Pacific electric ray ALTERNATE_NAMES acetylcholinesterase, asymmetric form ORGANISM #formal_name Torpedo californica #common_name Pacific electric ray DATE 17-Mar-1987 #sequence_revision 08-Nov-1996 #text_change 15-Sep-2000 ACCESSIONS A00773; A60820; A31962; B31962; A23902; B41117; S15677 REFERENCE A00773 !$#authors Schumacher, M.; Camp, S.; Maulet, Y.; Newton, M.; !1MacPhee-Quigley, K.; Taylor, S.S.; Friedmann, T.; Taylor, P. !$#journal Nature (1986) 319:407-409 !$#title Primary structure of Torpedo californica !1acetylcholinesterase deduced from its cDNA sequence. !$#cross-references MUID:86118676; PMID:3753747 !$#accession A00773 !'##molecule_type mRNA !'##residues 'NS',11-596 ##label SCH !'##cross-references GB:X03439; NID:g64389 !'##experimental_source electric organ !'##note parts of this sequence, including the amino and carboxyl ends !1of the mature protein, were determined by protein sequencing REFERENCE A60820 !$#authors Schumacher, M.; Camp, S.; Maulet, Y.; Newton, M.; !1MacPhee-Quigley, K.; Taylor, S.S.; Friedmann, T.; Taylor, P. !$#journal Fed. Proc. (1986) 45:2976-2981 !$#title Primary structure of acetylcholinesterase: implications for !1regulation and function. !$#cross-references MUID:87054662; PMID:3536598 !$#accession A60820 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 22-596 ##label SC2 REFERENCE A92701 !$#authors Schumacher, M.; Maulet, Y.; Camp, S.; Taylor, P. !$#journal J. Biol. Chem. (1988) 263:18979-18987 !$#title Multiple messenger RNA species give rise to the structural !1diversity in acetylcholinesterase. !$#cross-references MUID:89066695; PMID:3198606 !$#accession A31962 !'##molecule_type mRNA !'##residues 1-23 ##label SC3 !'##cross-references EMBL:X03439; NID:g64389 !'##experimental_source clones AChE-11 and AChE-18 !'##note revision to sequence A00773 !$#accession B31962 !'##molecule_type DNA; mRNA !'##residues 499-565 ##label SC4 !'##cross-references GB:X03439; NID:g64389 !'##experimental_source clone AChE-1 REFERENCE A23902 !$#authors MacPhee-Quigley, K.; Taylor, P.; Taylor, S. !$#journal J. Biol. Chem. (1985) 260:12185-12189 !$#title Primary structures of the catalytic subunits from two !1molecular forms of acetylcholinesterase. !$#cross-references MUID:86008285; PMID:3900071 !$#accession A23902 !'##molecule_type protein !'##residues 22,'B',24-45;214-237 ##label MAC !'##note active site Ser identification REFERENCE A41117 !$#authors Kreienkamp, H.J.; Weise, C.; Raba, R.; Aaviksaar, A.; Hucho, !1F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:6117-6121 !$#title Anionic subsites of the catalytic center of !1acetylcholinesterase from Torpedo and from cobra venom. !$#cross-references MUID:91296772; PMID:2068091 !$#accession B41117 !'##molecule_type protein !'##residues 100-108 ##label KRE !'##note substrate binding site REFERENCE PS0113 !$#authors Maulet, Y.; Camp, S.; Gibney, G.; Rachinsky, T.L.; Ekstroem, !1T.J.; Taylor, P. !$#journal Neuron (1990) 4:289-301 !$#title Single gene encodes glycophospholipid-anchored and !1asymmetric acetylcholinesterase forms: alternative coding !1exons contain inverted repeat sequences. !$#cross-references MUID:90166618; PMID:2306366 !$#accession S15677 !'##status preliminary !'##molecule_type DNA !'##residues 557-596 ##label MAU !'##cross-references EMBL:X56516 REFERENCE A43099 !$#authors MacPhee-Quigley, K.; Vedvick, T.S.; Taylor, P.; Taylor, S.S. !$#journal J. Biol. Chem. (1986) 261:13565-13570 !$#title Profile of the disulfide bonds in acetylcholinesterase. !$#cross-references MUID:87008586; PMID:3759980 !$#contents annotation; disulfide bonds REFERENCE A50061 !$#authors Sussman, J.L.; Harel, M.; Silman, I. !$#submission submitted to the Brookhaven Protein Data Bank, October 1991 !$#cross-references PDB:1ACE !$#contents annotation; X-ray crystallography, 2.8 angstroms, residues !126-481,511-555 of solubilized 5.6S form REFERENCE A43098 !$#authors Sussman, J.L.; Harel, M.; Frolow, F.; Oefner, C.; Goldman, !1A.; Toker, L.; Silman, I. !$#journal Science (1991) 253:872-879 !$#title Atomic structure of acetylcholinesterase from Torpedo !1californica: a prototypic acetylcholine-binding protein. !$#cross-references MUID:91343928; PMID:1678899 !$#contents annotation; X-ray crystallography, 2.8 angstroms, residues !126-481,511-555 of solubilized 5.6S form COMMENT Synapses usually contain this 11S (asymmetric) form of !1cholinesterase with a collagen-like part disulfide-bonded to !1the catalytic part. A different, 5.6S (globular or !1GPI-anchor) form of cholinesterase occurs on the outer !1surfaces of cell membranes, including those of erythrocytes. COMPLEX 11S form is disulfide linked homodimer; 18S form is !1homotetramer, a dimer of disulfide linked homodimers FUNCTION !$#description hydrolyzes acetylcholine to choline and acetate !$#pathway neurotransmitter degradation CLASSIFICATION #superfamily cholinesterase; cholinesterase homology KEYWORDS alternative splicing; carboxylic ester hydrolase; !1glycoprotein; membrane protein; muscle; nerve; !1neurotransmitter degradation; synapse FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-596 #product acetylcholinesterase, 11S form #status !8experimental #label MAT\ !$51-551 #domain cholinesterase homology #label CHE\ !$80,478,554 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$88-115,275-286, !$423-542 #disulfide_bonds #status experimental\ !$105 #binding_site substrate (Trp) #status experimental\ !$221 #active_site Ser #status experimental\ !$348,461 #active_site Glu, His #status predicted\ !$437 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$593 #disulfide_bonds interchain #status experimental SUMMARY #length 596 #molecular-weight 67818 #checksum 6045 SEQUENCE /// ENTRY A38868 #type complete TITLE acetylcholinesterase (EC 3.1.1.7) precursor - marbled electric ray ORGANISM #formal_name Torpedo marmorata #common_name marbled electric ray DATE 23-Apr-1993 #sequence_revision 15-Nov-1996 #text_change 11-Jun-1999 ACCESSIONS A38868; A29682; S15696; A25650 REFERENCE A38868 !$#authors Massoulie, J.; Bon, S. !$#submission submitted to the EMBL Data Library, June 1992 !$#accession A38868 !'##molecule_type mRNA !'##residues 1-599 ##label MAS !'##cross-references EMBL:X05497; NID:g64414; PIDN:CAA29047.1; !1PID:g64415 REFERENCE A29682 !$#authors Sikorav, J.L.; Krejci, E.; Massoulie, J. !$#journal EMBO J. (1987) 6:1865-1873 !$#title cDNA sequences of Torpedo marmorata acetylcholinesterase: !1primary structure of the precursor of a catalytic subunit; !1existence of multiple 5'-untranslated regions. !$#cross-references MUID:88004392; PMID:2820709 !$#accession A29682 !'##molecule_type mRNA !'##residues 1-40,'G',42-226,'G',228-272,'G',274-284,'E',286-420,'N', !1422-599 ##label SIK !'##cross-references EMBL:X05497 REFERENCE S01293 !$#authors Sikorav, J.L.; Duval, N.; Anselmet, A.; Bon, S.; Krejci, E.; !1Legay, C.; Osterlund, M.; Reimund, B.; Massoulie, J. !$#journal EMBO J. (1988) 7:2983-2993 !$#title Complex alternative splicing of acetylcholinesterase !1transcripts in Torpedo electric organ; primary structure of !1the precursor of the glycolipid-anchored dimeric form. !$#cross-references MUID:89030590; PMID:3181125 !$#accession S15696 !'##molecule_type mRNA !'##residues 526-599 ##label SI2 !'##cross-references EMBL:X13172; NID:g64416; PIDN:CAA31570.1; !1PID:g64417 !'##experimental_source clone pAChE2 REFERENCE A91370 !$#authors Bon, S.; Chang, J.Y.; Strosberg, A.D. !$#journal FEBS Lett. (1986) 209:206-212 !$#title Identical N-terminal peptide sequences of asymmetric forms !1and of low-salt-soluble and detergent-soluble amphiphilic !1dimers of Torpedo acetylcholinesterase. Comparison with !1bovine acetylcholinesterase. !$#cross-references MUID:87080761; PMID:3792544 !$#accession A25650 !'##molecule_type protein !'##residues 25-40,'G',42-47 ##label BON GENETICS !$#gene AChE FUNCTION !$#description hydrolyzes acetylcholine to choline and acetate !$#pathway neurotransmitter degradation CLASSIFICATION #superfamily cholinesterase; cholinesterase homology KEYWORDS alternative splicing; carboxylic ester hydrolase; !1glycoprotein; neurotransmitter degradation; synapse FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-599 #product acetylcholinesterase #status predicted !8#label MAT\ !$54-554 #domain cholinesterase homology #label CHE\ !$83,440,481,557 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$91-118,278-289, !$426-545 #disulfide_bonds #status predicted\ !$224,351,464 #active_site Ser, Glu, His #status predicted\ !$596 #disulfide_bonds interchain #status predicted SUMMARY #length 599 #molecular-weight 68510 #checksum 466 SEQUENCE /// ENTRY S25062 #type complete TITLE triacylglycerol lipase (EC 3.1.1.3) precursor - rabbit ALTERNATE_NAMES cholesterol esterase ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S25062; S29847 REFERENCE S25062 !$#authors Collwell, N.; Aleman-Gomez, J.; Kumar, V.B. !$#submission submitted to the EMBL Data Library, May 1992 !$#description Molecular cloning and expression of rabbit cholesterol !1esterase reveals evolutionary divergence at C-terminal end. !$#accession S25062 !'##molecule_type mRNA !'##residues 1-593 ##label COL1 !'##cross-references EMBL:X65944 REFERENCE S29847 !$#authors Colwell, N.S.; Aleman-Gomez, J.A.; Vijaya Kumar, B. !$#journal Biochim. Biophys. Acta (1993) 1172:175-180 !$#title Molecular cloning and expression of rabbit pancreatic !1cholesterol esterase. !$#cross-references MUID:93176805; PMID:8439557 !$#accession S29847 !'##molecule_type mRNA !'##residues 1-44,'AT',47-416,'M',418-457,'QY',460-485,'W',487-499, !1'GSARHWEPYTLENGSYLEINKKMSQDSTKSHLRNSFLQFWAGPTK',548-593 !1##label COL2 !'##cross-references EMBL:X65944 !'##note the difference near the carboxyl end is due to a frameshift !1error CLASSIFICATION #superfamily cholinesterase; cholinesterase homology KEYWORDS carboxylic ester hydrolase; glycoprotein FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-593 #product triacylglycerol lipase #status predicted !8#label MAT\ !$51-543 #domain cholinesterase homology #label CHE\ !$207 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$214,453 #active_site Ser, His #status predicted SUMMARY #length 593 #molecular-weight 64205 #checksum 5988 SEQUENCE /// ENTRY ACGUGC #type complete TITLE triacylglycerol lipase (EC 3.1.1.3) I precursor - yeast (Geotrichum candidum) ALTERNATE_NAMES lipase ORGANISM #formal_name Geotrichum candidum DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 31-Mar-2000 ACCESSIONS PN0492; JQ0022 REFERENCE PN0492 !$#authors Nagao, T.; Shimada, Y.; Sugihara, A.; Tominaga, Y. !$#journal J. Biochem. (1993) 113:776-780 !$#title Cloning and sequencing of two chromosomal lipase genes from !1Geotrichum candidum. !$#cross-references MUID:93380907; PMID:8370674 !$#accession PN0492 !'##molecule_type DNA !'##residues 1-563 ##label NAG !'##note the translation of residues 31-550 and the corresponding !1nucleotide sequence are not shown REFERENCE JQ0022 !$#authors Shimada, Y.; Sugihara, A.; Tominaga, Y.; Iizumi, T.; !1Tsunasawa, S. !$#journal J. Biochem. (1989) 106:383-388 !$#title cDNA molecular cloning of Geotrichum candidum lipase. !$#cross-references MUID:90110016; PMID:2481674 !$#accession JQ0022 !'##molecule_type mRNA !'##residues 1-563 ##label SHI !'##experimental_source strain ATCC 34614 !'##note sequences of several small peptides were also determined COMMENT The extracellular lipase produced by Geotrichum candidum !1hydrolyzes all ester bonds in triglyceride and displays a !1high affinity for triolein. GENETICS !$#gene lipI CLASSIFICATION #superfamily cholinesterase; cholinesterase homology KEYWORDS carboxylic ester hydrolase; glycoprotein; pyroglutamic acid FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-563 #product triacylglycerol lipase #status experimental !8#label MAT\ !$43-560 #domain cholinesterase homology #label CHE\ !$234-238 #region interfacial lipid recognition (GXSXG) motif\ !$20 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$80-124,295-307 #disulfide_bonds #status predicted\ !$236 #active_site Ser #status predicted\ !$302,383 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 563 #molecular-weight 61230 #checksum 9323 SEQUENCE /// ENTRY PN0493 #type complete TITLE triacylglycerol lipase (EC 3.1.1.3) II precursor - yeast (Geotrichum candidum) ORGANISM #formal_name Geotrichum candidum DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jun-2000 ACCESSIONS PN0493; A46760 REFERENCE PN0492 !$#authors Nagao, T.; Shimada, Y.; Sugihara, A.; Tominaga, Y. !$#journal J. Biochem. (1993) 113:776-780 !$#title Cloning and sequencing of two chromosomal lipase genes from !1Geotrichum candidum. !$#cross-references MUID:93380907; PMID:8370674 !$#accession PN0493 !'##molecule_type DNA !'##residues 1-563 ##label NAG !'##note the translation of residues 31-550 and the corresponding !1nucleotide sequence are not shown REFERENCE A46760 !$#authors Shimada, Y.; Sugihara, A.; Iizumi, T.; Tominaga, Y. !$#journal J. Biochem. (1990) 107:703-707 !$#title cDNA cloning and characterization of Geotrichum candidum !1lipase II. !$#cross-references MUID:90375435; PMID:2398037 !$#accession A46760 !'##molecule_type mRNA !'##residues 7-563 ##label SHI !'##cross-references GB:D00697; NID:g217926; PIDN:BAA00603.1; !1PID:g217927 COMMENT The extracellular lipase produced by Geotrichum candidum !1hydrolyzes all ester bonds in triglyceride and displays a !1high affinity for triolein. GENETICS !$#gene lipII CLASSIFICATION #superfamily cholinesterase; cholinesterase homology KEYWORDS carboxylic ester hydrolase; glycoprotein; pyroglutamic acid FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-563 #product triacylglycerol lipase II #status predicted !8#label MAT\ !$43-560 #domain cholinesterase homology #label CHE\ !$234-238 #region interfacial lipid recognition (GXSXG) motif\ !$20 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status predicted\ !$80-124,295-307 #disulfide_bonds #status predicted\ !$236 #active_site Ser #status predicted\ !$302,383 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 563 #molecular-weight 61617 #checksum 732 SEQUENCE /// ENTRY JC5408 #type complete TITLE carboxylesterase (EC 3.1.1.1) - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS JC5408 REFERENCE JC5408 !$#authors Schwer, H.; Langmann, T.; Daig, R.; Becker, A.; Aslanidis, !1C.; Schmitz, G. !$#journal Biochem. Biophys. Res. Commun. (1997) 233:117-120 !$#title Molecular cloning and characterization of a novel putative !1carboxylesterase, present in human intestine and liver. !$#cross-references MUID:97289502; PMID:9144407 !$#accession JC5408 !'##molecule_type mRNA !'##residues 1-559 ##label SCH !'##cross-references GB:Y09616; NID:g2058317; PIDN:CAA70831.1; !1PID:g2058318 !'##experimental_source intestine COMMENT This enzyme hydrolyzes many xenobiotics, such as carboxyl !1esters, thioesters and aromatic amides, and is involved in !1the detoxification of ester and amide prodrugs. GENETICS !$#gene GDB:CES2; iCE; CE2 !'##cross-references GDB:9959011 CLASSIFICATION #superfamily cholinesterase; cholinesterase homology KEYWORDS carboxylic ester hydrolase; glycoprotein FEATURE !$58-544 #domain cholinesterase homology #label CHE\ !$15-95,123-280, !$291-428 #disulfide_bonds #status predicted\ !$111,276 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$228,457 #active_site Ser, His #status predicted SUMMARY #length 559 #molecular-weight 61806 #checksum 4288 SEQUENCE /// ENTRY A41010 #type complete TITLE carboxylesterase (EC 3.1.1.1) precursor, monocyte/macrophage [validated] - human ALTERNATE_NAMES carboxylesterase, hepatic; monocyte/macrophage serine esterase ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 08-Dec-2000 ACCESSIONS A41010; JH0327; A47376; A49816; PS0280; I61085; A48809; !1I57004 REFERENCE A41010 !$#authors Munger, J.S.; Shi, G.P.; Mark, E.A.; Chin, D.T.; Gerard, C.; !1Chapman, H.A. !$#journal J. Biol. Chem. (1991) 266:18832-18838 !$#title A serine esterase released by human alveolar macrophages is !1closely related to liver microsomal carboxylesterases. !$#cross-references MUID:92011649; PMID:1918003 !$#accession A41010 !'##molecule_type mRNA !'##residues 1-567 ##label MUN !'##cross-references GB:M73499; NID:g179927; PIDN:AAA35649.1; !1PID:g179928 !'##note parts of this sequence, including the amino end of the mature !1protein, were confirmed by protein sequencing REFERENCE JH0327 !$#authors Long, R.M.; Calabrese, M.R.; Martin, B.M.; Pohl, L.R. !$#journal Life Sci. (1991) 48:PL43-PL49 !$#title Cloning and sequencing of a human liver carboxylesterase !1isoenzyme. !$#cross-references MUID:91148424; PMID:1997784 !$#accession JH0327 !'##molecule_type mRNA !'##residues 61-567 ##label LON !'##cross-references GB:M55509; NID:g179929; PIDN:AAA35650.1; !1PID:g179930 REFERENCE A47376 !$#authors Shibata, F.; Takagi, Y.; Kitajima, M.; Kuroda, T.; Omura, T. !$#journal Genomics (1993) 17:76-82 !$#title Molecular cloning and characterization of a human !1carboxylesterase gene. !$#cross-references MUID:94010913; PMID:8406473 !$#accession A47376 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type mRNA; DNA !'##residues 1-3,'PALV',8-11,'A',13-567 ##label SHI !'##cross-references GB:D21088; NID:g455476; PIDN:BAA04650.1; !1PID:g458470 !'##note sequence extracted from NCBI backbone (NCBIP:137630) and !1corrected to correspond with the published sequence in Fig. !14 REFERENCE A49816 !$#authors Zschunke, F.; Salmassi, A.; Kreipe, H.; Buck, F.; !1Parwaresch, M.R.; Radzun, H.J. !$#journal Blood (1991) 78:506-512 !$#title cDNA cloning and characterization of human monocyte/ !1macrophage serine esterase-1. !$#cross-references MUID:91300111; PMID:2070086 !$#accession A49816 !'##molecule_type mRNA !'##residues 'G',65-185,'G',187-361,363-567 ##label ZSC !'##cross-references GB:X52973; NID:g36421; PIDN:CAA37147.1; !1PID:g1335304 REFERENCE PS0280 !$#authors Riddles, P.W.; Richards, L.J.; Bowles, M.R.; Pond, S.M. !$#journal Gene (1991) 108:289-292 !$#title Cloning and analysis of a cDNA encoding a human liver !1carboxylesterase. !$#cross-references MUID:92084150; PMID:1748313 !$#accession PS0280 !'##molecule_type mRNA !'##residues 114,'H',116-280,'A',282-300,'IGNSYLWTYRETQREST',318-336, !1'R',338-382,'GSPI',387-388,'FA',391-416,'I',418-511,'K', !1513-562,'D',564-567 ##label RID !'##cross-references GB:M65261; NID:g187028; PIDN:AAA83932.1; !1PID:g187029 !'##experimental_source liver !'##note differences between this sequence and other reports appear to !1be due to frameshift errors REFERENCE A48809 !$#authors Kroetz, D.L.; McBride, O.W.; Gonzalez, F.J. !$#journal Biochemistry (1993) 32:11606-11617 !$#title Glycosylation-dependent activity of baculovirus-expressed !1human liver carboxylesterases: cDNA cloning and !1characterization of two highly similar enzyme forms. !$#cross-references MUID:94032283; PMID:8218228 !$#accession I61085 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-55,'G',57-361,363-535,'G',537-567 ##label KRO1 !'##cross-references GB:L07765; NID:g180949; PIDN:AAA35711.1; !1PID:g180950 !$#accession A48809 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-17,'A',18-55,'G',57-535,'G',537-567 ##label KRO2 !'##cross-references GB:L07764; NID:g180947; PIDN:AAA16036.1; !1PID:g180948 GENETICS !$#gene GDB:CES1; HMSE !'##cross-references GDB:128044; OMIM:114835 !$#map_position 16q13-16q22.1 CLASSIFICATION #superfamily cholinesterase; cholinesterase homology KEYWORDS carboxylic ester hydrolase; endoplasmic reticulum; liver FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-145 #domain propeptide #status predicted #label PRO\ !$50-553 #domain cholinesterase homology #label CHE\ !$146-567 #product carboxylesterase #status experimental #label !8MAT\ !$564-567 #region endoplasmic reticulum retention signal !8#status atypical\ !$221,468 #active_site Ser, His #status predicted SUMMARY #length 567 #molecular-weight 62521 #checksum 2783 SEQUENCE /// ENTRY S36787 #type complete TITLE carboxylesterase (EC 3.1.1.1) FE4 precursor - green peach aphid ORGANISM #formal_name Myzus persicae #common_name green peach aphid DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S36787 REFERENCE S36786 !$#authors Field, L.M.; Williamson, M.S.; Moores, G.D.; Devonshire, !1A.L. !$#journal Biochem. J. (1993) 294:569-574 !$#title Cloning and analysis of the esterase genes conferring !1insecticide resistance in the peach-potato aphid, Myzus !1persicae (Sulzer). !$#cross-references MUID:93384534; PMID:8373371 !$#accession S36787 !'##status preliminary !'##molecule_type mRNA !'##residues 1-564 ##label FIE !'##cross-references EMBL:X74555; NID:g397512; PIDN:CAA52649.1; !1PID:g397513 CLASSIFICATION #superfamily cholinesterase; cholinesterase homology KEYWORDS carboxylic ester hydrolase FEATURE !$52-552 #domain cholinesterase homology #label CHE SUMMARY #length 564 #molecular-weight 62757 #checksum 9304 SEQUENCE /// ENTRY S34607 #type complete TITLE carboxylesterase (EC 3.1.1.1) - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S34607 REFERENCE S34607 !$#authors Aida, K.; Moore, R.; Negishi, M. !$#journal Biochim. Biophys. Acta (1993) 1174:72-74 !$#title Cloning and nucleotide sequence of a novel, male-predominant !1carboxylesterase in mouse liver. !$#cross-references MUID:93326638; PMID:7916639 !$#accession S34607 !'##status preliminary !'##molecule_type mRNA !'##residues 1-554 ##label AID !'##cross-references GB:S64130; NID:g404388; PIDN:AAB27606.1; !1PID:g404389 CLASSIFICATION #superfamily cholinesterase; cholinesterase homology KEYWORDS carboxylic ester hydrolase FEATURE !$46-536 #domain cholinesterase homology #label CHE\ !$215,443 #active_site Ser, His #status predicted SUMMARY #length 554 #molecular-weight 61509 #checksum 1172 SEQUENCE /// ENTRY A34576 #type complete TITLE crystal protein precursor - slime mold (Dictyostelium discoideum) ORGANISM #formal_name Dictyostelium discoideum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A34576 REFERENCE A34576 !$#authors Bomblies, L.; Biegelmann, E.; Doering, V.; Gerisch, G.; !1Krafft-Czepa, H.; Noegel, A.A.; Schleicher, M.; Humbel, B.M. !$#journal J. Cell Biol. (1990) 110:669-679 !$#title Membrane-enclosed crystals in Dictyostelium discoideum !1cells, consisting of developmentally regulated proteins with !1sequence similarities to known esterases. !$#cross-references MUID:90171041; PMID:2307702 !$#accession A34576 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-550 ##label BOM !'##cross-references GB:X52464; NID:g7233; PIDN:CAA36702.1; PID:g7234 CLASSIFICATION #superfamily cholinesterase; cholinesterase homology FEATURE !$54-544 #domain cholinesterase homology #label CHE SUMMARY #length 550 #molecular-weight 61065 #checksum 3440 SEQUENCE /// ENTRY ESPSTP #type complete TITLE tropinesterase (EC 3.1.1.10) - Pseudomonas putida ALTERNATE_NAMES atropine acylhydrolase; atropinesterase ORGANISM #formal_name Pseudomonas putida DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 14-May-1999 ACCESSIONS A26563 REFERENCE A26563 !$#authors Hessing, J.G.M. !$#citation Ph.D. thesis, Univ. of Leiden, 1983 !$#description The primary structure of atropinesterase from Pseudomonas !1putida. !$#accession A26563 !'##molecule_type protein !'##residues 1-272 ##label HES !'##experimental_source biotype A, strain L COMMENT The tropinesterase molecule is a homodimer. COMMENT The strain used in this study was isolated from the soil !1between the roots of belladonna (Atropa belladonna). CLASSIFICATION #superfamily tropinesterase KEYWORDS alkaloid degradation; carboxylic ester hydrolase; dimer FEATURE !$110 #active_site Ser #status predicted SUMMARY #length 272 #molecular-weight 30263 #checksum 9506 SEQUENCE /// ENTRY ESPSSK #type complete TITLE 2,6-dioxo-6-phenylhexa-3-enoate hydrolase (EC 3.7.1.8) - Pseudomonas sp. ORGANISM #formal_name Pseudomonas sp. DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 11-Jun-1999 ACCESSIONS B32312; JU0086 REFERENCE A32312 !$#authors Kimbara, K.; Hashimoto, T.; Fukuda, M.; Koana, T.; Takagi, !1M.; Oishi, M.; Yano, K. !$#journal J. Bacteriol. (1989) 171:2740-2747 !$#title Cloning and sequencing of two tandem genes involved in !1degradation of 2,3-dihydroxybiphenyl to benzoic acid in the !1polychlorinated biphenyl-degrading soil bacterium !1Pseudomonas sp. strain KKS102. !$#cross-references MUID:89213965; PMID:2540155 !$#accession B32312 !'##molecule_type DNA !'##residues 1-277 ##label KIM !'##cross-references GB:M26433; NID:g151098; PIDN:AAA25751.1; !1PID:g151100 !'##experimental_source strain KKS102 REFERENCE JU0085 !$#authors Takagi, M. !$#submission submitted to JIPID, July 1989 !$#accession JU0086 !'##molecule_type DNA !'##residues 1-277 ##label TAK COMMENT This enzyme catalyzes the fourth, and final, step in the !1major degradative pathway for biphenyl and polychlorinated !1biphenyls (PCBs). GENETICS !$#gene bphD CLASSIFICATION #superfamily tropinesterase KEYWORDS aromatic hydrocarbon catabolism; hydrolase; PCB !1biodegradation SUMMARY #length 277 #molecular-weight 30253 #checksum 5765 SEQUENCE /// ENTRY C35124 #type complete TITLE 2,6-dioxo-6-phenylhexa-3-enoate hydrolase (EC 3.7.1.8) - Pseudomonas putida ORGANISM #formal_name Pseudomonas putida DATE 03-Aug-1990 #sequence_revision 06-Jan-1995 #text_change 11-Jun-1999 ACCESSIONS C35124 REFERENCE A35124 !$#authors Hayase, N.; Taira, K.; Furukawa, K. !$#journal J. Bacteriol. (1990) 172:1160-1164 !$#title Pseudomonas putida KF715 bphABCD operon encoding biphenyl !1and polychlorinated biphenyl degradation: cloning, analysis, !1and expression in soil bacteria. !$#cross-references MUID:90130279; PMID:2105297 !$#accession C35124 !'##molecule_type DNA !'##residues 1-286 ##label HAY !'##cross-references GB:M33813; NID:g151105; PIDN:AAA25757.1; !1PID:g151108 !'##experimental_source strain KF715 COMMENT This enzyme catalyzes the fourth, and final, step in the !1major degradative pathway for biphenyl and polychlorinated !1biphenyls (PCBs). GENETICS !$#gene bphD CLASSIFICATION #superfamily tropinesterase KEYWORDS aromatic hydrocarbon catabolism; hydrolase; PCB !1biodegradation FEATURE !$2-286 #product 2,6-dioxo-6-phenylhexa-3-enoate hydrolase !8#status predicted #label MAT SUMMARY #length 286 #molecular-weight 31951 #checksum 2931 SEQUENCE /// ENTRY E64762 #type complete TITLE probable 2,6-dioxo-6-phenylhexa-3-enoate hydrolase (EC 3.7.1.8) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS E64762 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64762 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-309 ##label BLAT !'##cross-references GB:AE000142; GB:U00096; NID:g1786542; !1PIDN:AAC73452.1; PID:g1786545; UWGP:b0349 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene mhpC CLASSIFICATION #superfamily tropinesterase KEYWORDS aromatic hydrocarbon catabolism; hydrolase; PCB !1biodegradation SUMMARY #length 309 #molecular-weight 34641 #checksum 8826 SEQUENCE /// ENTRY E64803 #type complete TITLE ybfF protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS E64803 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64803 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-254 ##label BLAT !'##cross-references GB:AE000172; GB:U00096; NID:g1786896; !1PIDN:AAC73780.1; PID:g1786902; UWGP:b0686 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ybfF CLASSIFICATION #superfamily tropinesterase SUMMARY #length 254 #molecular-weight 28437 #checksum 5548 SEQUENCE /// ENTRY E64053 #type complete TITLE hypothetical protein HI0193 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS E64053 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession E64053 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-287 ##label TIGR !'##cross-references GB:U32704; GB:L42023; NID:g1573143; !1PIDN:AAC21862.1; PID:g1573150; TIGR:HI0193 CLASSIFICATION #superfamily tropinesterase SUMMARY #length 287 #molecular-weight 32987 #checksum 6388 SEQUENCE /// ENTRY JC5419 #type complete TITLE 2-hydroxymuconate-semialdehyde hydrolase (EC 3.7.1.9) - Pseudomonas sp. ORGANISM #formal_name Pseudomonas sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JC5419 REFERENCE JC5419 !$#authors Shin, H.J.; Kim, S.J.; Kim, Y.C. !$#journal Biochem. Biophys. Res. Commun. (1997) 232:288-291 !$#title Sequence analysis of the phnD gene encoding 2-hydroxymuconic !1semialdehyde hydrolase in Pseudomonas sp. strain DJ77. !$#cross-references MUID:97242176; PMID:9125165 !$#accession JC5419 !'##molecule_type DNA !'##residues 1-286 ##label SHI !'##cross-references GB:U83881; NID:g1923244; PIDN:AAC45091.1; !1PID:g1923245 !'##experimental_source strain DJ77 !'##note the authors translated the initiation codon TTG for residue 1 !1as Met COMMENT This enzyme is involved in conversion of 2-hydroxymuconic !1semialdehyde to 2-hydrozypent-2,4-dienoate. GENETICS !$#gene phnD !$#start_codon GTT CLASSIFICATION #superfamily tropinesterase KEYWORDS hydrolase SUMMARY #length 286 #molecular-weight 31302 #checksum 4099 SEQUENCE /// ENTRY JC5087 #type complete TITLE tannase (EC 3.1.1.20) precursor - Aspergillus oryzae ALTERNATE_NAMES tannin acyl hydrolase ORGANISM #formal_name Aspergillus oryzae DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 21-Jul-2000 ACCESSIONS JC5087; PC4226 REFERENCE JC5087 !$#authors Hatamoto, O.; Watarai, T.; Kikuchi, M.; Mizusawa, K.; !1Sekine, H. !$#journal Gene (1996) 175:215-221 !$#title Cloning and sequencing of the gene encoding tannase and a !1structural study of the tannase subunit from Aspergillus !1oryzae. !$#cross-references MUID:97074675; PMID:8917102 !$#accession JC5087 !'##molecule_type DNA !'##residues 1-588 ##label HAT1 !'##cross-references DDBJ:D63338; NID:g1753190; PIDN:BAA09656.1; !1PID:g1753191 !$#accession PC4226 !'##molecule_type protein !'##residues 159-166;424-426;456-471 ##label HAT2 COMMENT This enzyme hydrolyzes the ester bonds of tannic acid to !1produce gallic acid and glucose. CLASSIFICATION #superfamily Aspergillus oryzae tannase KEYWORDS carboxylic ester hydrolase FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-588 #product tannase #status predicted #label MAT SUMMARY #length 588 #molecular-weight 64095 #checksum 979 SEQUENCE /// ENTRY S57530 #type complete TITLE carboxyl esterase - Acinetobacter calcoaceticus ORGANISM #formal_name Acinetobacter calcoaceticus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S57530 REFERENCE S57529 !$#authors Kok, R.G.; Bart, A.; Hellingwerf, K.J. !$#submission submitted to the EMBL Data Library, June 1995 !$#description Characterization of the estBR operon of Acinetobacter !1calcoaceticus BD413; a concept for the involvement of an !1esterase in oxidative stress response. !$#accession S57530 !'##status preliminary !'##molecule_type DNA !'##residues 1-321 ##label KOK !'##cross-references EMBL:X88895 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily carboxyl esterase SUMMARY #length 321 #molecular-weight 35697 #checksum 7733 SEQUENCE /// ENTRY XYEBET #type complete TITLE protein-glutamate methylesterase (EC 3.1.1.61) - Salmonella typhimurium ALTERNATE_NAMES chemotaxis-specific methylesterase ORGANISM #formal_name Salmonella typhimurium DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 13-Jun-1997 ACCESSIONS A00547; A26119 REFERENCE A00547 !$#authors Simms, S.A.; Keane, M.G.; Stock, J. !$#journal J. Biol. Chem. (1985) 260:10161-10168 !$#title Multiple forms of the CheB methylesterase in bacterial !1chemosensing. !$#cross-references MUID:85261436; PMID:2991277 !$#accession A00547 !'##molecule_type protein !'##residues 1-349 ##label SIM REFERENCE A26119 !$#authors Simms, S.A.; Cornman, E.W.; Mottonen, J.; Stock, J. !$#journal J. Biol. Chem. (1987) 262:29-31 !$#title Active site of the enzyme which demethylates receptors !1during bacterial chemotaxis. !$#cross-references MUID:87083462; PMID:3539934 !$#accession A26119 !'##molecule_type protein !'##residues 277-306 ##label SI2 COMMENT The proteolytic fragment 146-349 is 15 times more active !1than the native form. GENETICS !$#gene cheB !$#map_position 40 FUNCTION !$#description catalyzes the hydrolytic demethylation of gamma-glutamyl !1methyl ester in chemoreceptors at the cytoplasmic membrane !$#pathway chemotaxis !$#note this enzyme hydrolyzes the products of protein-glutamate !1O-methyltransferase (EC 2.1.1.80) CLASSIFICATION #superfamily protein-glutamate methylesterase; response !1regulator homology KEYWORDS carboxylic ester hydrolase; chemotaxis; phosphoprotein; !1sensory transduction FEATURE !$1-145 #domain amino-terminal modulation region #status !8predicted #label MOD\ !$6-118 #domain response regulator homology #label RRH\ !$146-349 #domain catalytic #status predicted #label CAT\ !$56 #binding_site phosphate (Asp) (covalent) #status !8predicted\ !$309 #active_site Cys #status predicted SUMMARY #length 349 #molecular-weight 37551 #checksum 3839 SEQUENCE /// ENTRY XYECEB #type complete TITLE protein-glutamate methylesterase (EC 3.1.1.61) - Escherichia coli (strain K-12) ALTERNATE_NAMES chemotaxis-specific methylesterase ORGANISM #formal_name Escherichia coli DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 01-Mar-2002 ACCESSIONS D25195; C64951 REFERENCE A91811 !$#authors Mutoh, N.; Simon, M.I. !$#journal J. Bacteriol. (1986) 165:161-166 !$#title Nucleotide sequence corresponding to five chemotaxis genes !1in Escherichia coli. !$#cross-references MUID:86085665; PMID:3510184 !$#accession D25195 !'##molecule_type DNA !'##residues 1-349 ##label MUT REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64951 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-349 ##label BLAT !'##cross-references GB:AE000282; GB:U00096; NID:g1788189; !1PIDN:AAC74953.1; PID:g1788192; UWGP:b1883 !'##experimental_source strain K-12, substrain MG1655 COMMENT This protein is a methylesterase specifically responsible !1for removing the methyl group from the gamma-glutamyl methyl !1ester residues in the methyl-accepting chemotaxis proteins !1(MCP). The MCP methylation state of the cell is crucial for !1sensory responses and adaptations. GENETICS !$#gene cheB !$#map_position 42 min FUNCTION !$#description catalyzes the hydrolytic demethylation of gamma-glutamyl !1methyl ester in chemoreceptors at the cytoplasmic membrane !$#pathway chemotaxis !$#note this enzyme hydrolyzes the products of protein-glutamate !1O-methyltransferase (EC 2.1.1.80) CLASSIFICATION #superfamily protein-glutamate methylesterase; response !1regulator homology KEYWORDS carboxylic ester hydrolase; chemotaxis; phosphoprotein; !1sensory transduction FEATURE !$1-145 #domain amino-terminal modulation region #status !8predicted #label MOD\ !$6-118 #domain response regulator homology #label RRH\ !$146-349 #domain catalytic #status predicted #label CAT\ !$56 #binding_site phosphate (Asp) (covalent) #status !8predicted\ !$309 #active_site Cys #status predicted SUMMARY #length 349 #molecular-weight 37467 #checksum 3199 SEQUENCE /// ENTRY A48511 #type complete TITLE protein-glutamate methylesterase (EC 3.1.1.61) cheB - Bacillus subtilis ALTERNATE_NAMES chemotactic methylesterase; MCP-glutamate methylesterase cheB ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A48511; F69598; S29596 REFERENCE A48511 !$#authors Kirsch, M.L.; Peters, P.D.; Hanlon, D.W.; Kirby, J.R.; !1Ordal, G.W. !$#journal J. Biol. Chem. (1993) 268:18610-18616 !$#title Chemotactic methylesterase promotes adaptation to high !1concentrations of attractant in Bacillus subtilis. !$#cross-references MUID:93366767; PMID:8395512 !$#accession A48511 !'##molecule_type DNA !'##residues 1-357 ##label KIR !'##cross-references EMBL:X67806; NID:g39840; PIDN:CAA48007.1; !1PID:g580836 !'##note authors translated the codon GAG for residue 85 as Gly, AAA for !1residue 118 as Leu, and CAG for residue 254 as Asn REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69598 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-357 ##label KUN !'##cross-references GB:Z99112; GB:AL009126; NID:g2633902; !1PIDN:CAB13515.1; PID:g2634014 !'##experimental_source strain 168 GENETICS !$#gene cheB !$#start_codon TTG CLASSIFICATION #superfamily protein-glutamate methylesterase; response !1regulator homology KEYWORDS carboxylic ester hydrolase; chemotaxis; phosphoprotein FEATURE !$4-116 #domain response regulator homology #label RRH\ !$54 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 357 #molecular-weight 38650 #checksum 702 SEQUENCE /// ENTRY S58646 #type complete TITLE protein-glutamate methylesterase (EC 3.1.1.61) cheB [similarity] - Halobacterium salinarum ALTERNATE_NAMES tactic signal adaptation protein cheB ORGANISM #formal_name Halobacterium salinarum DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 21-Jul-2000 ACCESSIONS S58646 REFERENCE S58645 !$#authors Rudolph, J.; Tolliday, N.; Schmitt, C.; Schuster, S.C.; !1Oesterhelt, D. !$#journal EMBO J. (1995) 14:4249-4257 !$#title Phosphorylation in halobacterial signal transduction. !$#cross-references MUID:96016197; PMID:7556066 !$#accession S58646 !'##status preliminary !'##molecule_type DNA !'##residues 1-347 ##label RUD !'##cross-references EMBL:X86407; NID:g994801; PIDN:CAA60162.1; !1PID:g994803 !'##note the source is designated as Halobacterium salinarium GENETICS !$#gene cheB FUNCTION TACT !$#description mediates the signal adaptation response [validated, !1MUID:96016197]; affects signal transfer from transducer !1proteins by protein methylation FUNCTION METE !$#description EC 3.1.1.61 CLASSIFICATION #superfamily protein-glutamate methylesterase; response !1regulator homology KEYWORDS carboxylic ester hydrolase; phosphoprotein FEATURE !$4-115 #domain response regulator homology #label RRH\ !$53 #binding_site phosphate (Asp) (covalent) #status !8predicted\ !$164,191,288 #active_site Ser, His, Asp #status predicted SUMMARY #length 347 #molecular-weight 36510 #checksum 1601 SEQUENCE /// ENTRY PSECA1 #type complete TITLE phospholipase A1 (EC 3.1.1.32) precursor - Escherichia coli (strain K-12) ALTERNATE_NAMES outer-membrane phospholipase A; phosphatidylcholine 1-acylhydrolase; phospholipase A, detergent-resistant ORGANISM #formal_name Escherichia coli DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 01-Mar-2002 ACCESSIONS A22133; S30711; A00771; S66447; F65186 REFERENCE A22133 !$#authors Homma, H.; Kobayashi, T.; Chiba, N.; Karasawa, K.; !1Mizushima, H.; Kudo, I.; Inoue, K.; Ikeda, H.; Sekiguchi, !1M.; Nojima, S. !$#journal J. Biochem. (1984) 96:1655-1664 !$#title The DNA sequence encoding pldA gene, the structural gene for !1detergent-resistant phospholipase A of E. coli. !$#cross-references MUID:85157492; PMID:6397464 !$#accession A22133 !'##molecule_type DNA !'##residues 1-289 ##label HOM !'##cross-references GB:X02143; GB:X00780; NID:g42423; PIDN:CAA26081.1; !1PID:g757840 !'##note this enzyme is tightly bound to the outer membrane of the cell REFERENCE S30660 !$#authors Daniels, D.L.; Plunkett III, G.; Burland, V.; Blattner, F.R. !$#journal Science (1992) 257:771-778 !$#title Analysis of the Escherichia coli genome: DNA sequence of the !1region from 84.5 to 86.5 minutes. !$#cross-references MUID:92358234; PMID:1379743 !$#accession S30711 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-13,'FA',16-289 ##label DAN !'##cross-references EMBL:M87049; NID:g836656; PIDN:AAA67617.1; !1PID:g148220 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1992 REFERENCE A00771 !$#authors de Geus, P.; Verheij, H.M.; Riegman, N.H.; Hoekstra, W.P.M.; !1de Haas, G.H. !$#journal EMBO J. (1984) 3:1799-1802 !$#title The pro- and mature forms of the E. coli K-12 outer membrane !1phospholipase A are identical. !$#cross-references MUID:85003590; PMID:6383820 !$#accession A00771 !'##molecule_type DNA !'##residues 'MTRQ',34-289 ##label DEG REFERENCE S66447 !$#authors Dekker, N.; Merck, K.; Tommassen, J.; Verheij, H.M. !$#journal Eur. J. Biochem. (1995) 232:214-219 !$#title In vitro folding of Escherichia coli outer-membrane !1phospholipase A. !$#cross-references MUID:96048049; PMID:7556153 !$#accession S66447 !'##status preliminary !'##molecule_type protein !'##residues 21-24 ##label DEK REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65186 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-289 ##label BLAT !'##cross-references GB:AE000458; GB:U00096; NID:g2367299; !1PIDN:AAC76824.1; PID:g2367300; UWGP:b3821 !'##experimental_source strain K-12, substrain MG1655 COMMENT This enzyme is tightly bound to the outer membrane of the !1cell. GENETICS !$#gene pldA !$#map_position 85 min CLASSIFICATION #superfamily bacterial phospholipase A1 KEYWORDS carboxylic ester hydrolase; membrane bound FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-289 #product phospholipase A1 #status predicted #label !8MPT SUMMARY #length 289 #molecular-weight 33163 #checksum 252 SEQUENCE /// ENTRY A40292 #type complete TITLE acyloxyacyl hydrolase (EC 3.1.1.-), neutrophil precursor [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 27-Mar-1992 #sequence_revision 27-Mar-1992 #text_change 08-Dec-2000 ACCESSIONS A40292 REFERENCE A40292 !$#authors Hagen, F.S.; Grant, F.J.; Kuijper, J.L.; Slaughter, C.A.; !1Moomaw, C.R.; Orth, K.; O'Hara, P.J.; Munford, R.S. !$#journal Biochemistry (1991) 30:8415-8423 !$#title Expression and characterization of recombinant human !1acyloxyacyl hydrolase, a leukocyte enzyme that deacylates !1bacterial lipopolysaccharides. !$#cross-references MUID:91355197; PMID:1883828 !$#accession A40292 !'##molecule_type mRNA !'##residues 1-575 ##label HAG !'##cross-references GB:M62840; NID:g178068; PIDN:AAA35506.1; !1PID:g178069 !'##note parts of this sequence, including the amino ends of the small !1and large chains, were determined by protein sequencing GENETICS !$#gene GDB:AOAH !'##cross-references GDB:134007; OMIM:102593 !$#map_position 7p14-7p12 COMPLEX heterodimer of disulfide-bonded chains derived from the same !1precursor FUNCTION !$#description hydrolyzes secondary acyl chains from bacterial !1lipopolysaccharide CLASSIFICATION #superfamily acyloxyacyl hydrolase; saposin repeat homology KEYWORDS carboxylic ester hydrolase; glycoprotein; leukocyte FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-34 #domain propeptide #status predicted #label PRO\ !$33-124 #domain saposin repeat homology #label SAP\ !$35-156 #domain small chain #status experimental #label SCH\ !$35-156,157-575 #product acyloxyacyl hydrolase #status experimental !8#label MAT\ !$157-575 #domain large chain #status experimental #label LCH\ !$261-265 #region lipase consensus motif (G-X-S-G)\ !$41-114,44-108,70-83 #disulfide_bonds #status predicted\ !$59,207,336,409,466 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 575 #molecular-weight 65104 #checksum 8740 SEQUENCE /// ENTRY C27058 #type complete TITLE carboxymethylenebutenolidase (EC 3.1.1.45) - Pseudomonas putida plasmid pAC27 ALTERNATE_NAMES dienelactone hydrolase ORGANISM #formal_name Pseudomonas putida DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 22-Oct-1999 ACCESSIONS C27058 REFERENCE A94163 !$#authors Frantz, B.; Chakrabarty, A.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:4460-4464 !$#title Organization and nucleotide sequence determination of a gene !1cluster involved in 3-chlorocatechol degradation. !$#cross-references MUID:87260828; PMID:3299368 !$#accession C27058 !'##molecule_type DNA !'##residues 1-236 ##label FRA !'##cross-references GB:M16964; NID:g141915; PIDN:AAA98284.1; !1PID:g141918 !'##note the authors translated the codon AAG for residue 154 as Asn and !1AGA for residue 224 as Thr GENETICS !$#gene clcD !$#genome plasmid CLASSIFICATION #superfamily carboxymethylenebutenolidase KEYWORDS carboxylic ester hydrolase SUMMARY #length 236 #molecular-weight 25555 #checksum 3106 SEQUENCE /// ENTRY C35255 #type complete TITLE carboxymethylenebutenolidase (EC 3.1.1.45) - Alcaligenes eutrophus ORGANISM #formal_name Alcaligenes eutrophus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C35255 REFERENCE A35255 !$#authors Perkins, E.J.; Gordon, M.P.; Caceres, O.; Lurquin, P.F. !$#journal J. Bacteriol. (1990) 172:2351-2359 !$#title Organization and sequence analysis of the 2,4-dichlorophenol !1hydroxylase and dichlorocatechol oxidative operons of !1plasmid pJP4. !$#cross-references MUID:90236889; PMID:2185214 !$#accession C35255 !'##status preliminary !'##molecule_type DNA !'##residues 1-234 ##label PER !'##cross-references GB:M35097; NID:g150766; PIDN:AAA98264.1; !1PID:g150769; GB:X07754 CLASSIFICATION #superfamily carboxymethylenebutenolidase KEYWORDS carboxylic ester hydrolase SUMMARY #length 234 #molecular-weight 25428 #checksum 204 SEQUENCE /// ENTRY ESECRM #type complete TITLE erythromycin esterase (EC 3.1.1.-) type II [validated] - Escherichia coli ORGANISM #formal_name Escherichia coli DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 26-May-2000 ACCESSIONS A24381 REFERENCE A24381 !$#authors Arthur, M.; Autissier, D.; Courvalin, P. !$#journal Nucleic Acids Res. (1986) 14:4987-4999 !$#title Analysis of the nucleotide sequence of the ereB gene !1encoding the erythromycin esterase type II. !$#cross-references MUID:86259072; PMID:3523438 !$#accession A24381 !'##molecule_type DNA !'##residues 1-419 ##label ART !'##cross-references GB:X03988; NID:g41355; PIDN:CAA27626.1; PID:g41357 COMMENT This enzyme confers resistance to erythromycin through !1inactivation by hydrolyzing the lactone ring of the !1antibiotic. GENETICS !$#gene ereB FUNCTION !$#description erythromycin esterase [validated, MUID:86259072] CLASSIFICATION #superfamily erythromycin esterase, type II KEYWORDS antibiotic resistance; carboxylic ester hydrolase SUMMARY #length 419 #molecular-weight 48172 #checksum 8565 SEQUENCE /// ENTRY ESDKTM #type complete TITLE oleoyl-[acyl-carrier-protein] hydrolase (EC 3.1.2.14) - mallard ALTERNATE_NAMES S-acyl fatty acid synthase thiolesterase ORGANISM #formal_name Anas platyrhynchos #common_name mallard DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 26-May-2000 ACCESSIONS A00775 REFERENCE A00775 !$#authors Poulose, A.J.; Rogers, L.; Cheesbrough, T.M.; Kolattukudy, !1P.E. !$#journal J. Biol. Chem. (1985) 260:15953-15958 !$#title Cloning and sequencing of the cDNA for S-acyl fatty acid !1synthase thioesterase from the uropygial gland of Mallard !1duck. !$#cross-references MUID:86059488; PMID:2415525 !$#accession A00775 !'##molecule_type mRNA !'##residues 1-251 ##label POU !'##cross-references GB:M12101; NID:g213098; PIDN:AAA49222.1; !1PID:g213099 COMMENT This protein, isolated from the uropygial gland, catalyzes !1the hydrolytic release of short-chain fatty acids from !1fatty-acid-acyl-carrier-protein, the product of the reaction !1catalyzed by fatty acid synthase. CLASSIFICATION #superfamily oleoyl-[acyl-carrier-protein] hydrolase; !1oleoyl-[acyl-carrier-protein] hydrolase homology KEYWORDS fatty acid biosynthesis; thiolester hydrolase FEATURE !$17-231 #domain oleoyl-[acyl-carrier-protein] hydrolase !8homology #label ACPH SUMMARY #length 251 #molecular-weight 28807 #checksum 2601 SEQUENCE /// ENTRY A26625 #type complete TITLE oleoyl-[acyl-carrier-protein] hydrolase (EC 3.1.2.14) - rat ALTERNATE_NAMES S-acyl fatty acid synthase thiolester hydrolase; thiolesterase II ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 26-May-2000 ACCESSIONS A26625; S02111; A26626; A29067; A32337 REFERENCE A26625 !$#authors Safford, R.; de Silva, J.; Lucas, C.; Windust, J.H.C.; !1Shedden, J.; James, C.M.; Sidebottom, C.M.; Slabas, A.R.; !1Tombs, M.P.; Hughes, S.G. !$#journal Biochemistry (1987) 26:1358-1364 !$#title Molecular cloning and sequence analysis of complementary DNA !1encoding rat mammary gland medium-chain S-acyl fatty acid !1synthetase thio ester hydrolase. !$#cross-references MUID:87185441; PMID:3105579 !$#accession A26625 !'##molecule_type mRNA !'##residues 1-263 ##label SAF !'##cross-references GB:M16200; NID:g205325; PIDN:AAA41578.1; !1PID:g205326 REFERENCE S02111 !$#authors Naggert, J.; Williams, B.; Cashman, D.P.; Smith, S. !$#journal Biochem. J. (1987) 243:597-601 !$#title Cloning and sequencing of the medium-chain S-acyl fatty acid !1synthetase thioester hydrolase cDNA from rat mammary gland. !$#cross-references MUID:87326291; PMID:3632637 !$#accession S02111 !'##molecule_type mRNA !'##residues 1-263 ##label NAG !'##cross-references EMBL:Y00311; NID:g57334; PIDN:CAA68411.1; !1PID:g57335 REFERENCE A26626 !$#authors Randhawa, Z.I.; Smith, S. !$#journal Biochemistry (1987) 26:1365-1373 !$#title Complete amino acid sequence of the medium-chain S-acyl !1fatty acid synthetase thio ester hydrolase from rat mammary !1gland. !$#cross-references MUID:87185442; PMID:3567174 !$#accession A26626 !'##molecule_type protein !'##residues 1-260 ##label RAN REFERENCE A29067 !$#authors Randhawa, Z.I.; Naggert, J.; Blacher, R.W.; Smith, S. !$#journal Eur. J. Biochem. (1987) 162:577-581 !$#title Amino acid sequence of the serine active-site region of the !1medium-chain S-acyl fatty acid synthetase thioester !1hydrolase from rat mammary gland. !$#cross-references MUID:87161827; PMID:3104035 !$#accession A29067 !'##molecule_type protein !'##residues 65-121 ##label RA2 CLASSIFICATION #superfamily oleoyl-[acyl-carrier-protein] hydrolase; !1oleoyl-[acyl-carrier-protein] hydrolase homology KEYWORDS fatty acid biosynthesis; thiolester hydrolase FEATURE !$28-242 #domain oleoyl-[acyl-carrier-protein] hydrolase !8homology #label ACPH SUMMARY #length 263 #molecular-weight 29471 #checksum 2346 SEQUENCE /// ENTRY S18532 #type complete TITLE hypothetical protein 5 (eryG 5' region) - Saccharopolyspora erythraea ORGANISM #formal_name Saccharopolyspora erythraea DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S18532; S16746 REFERENCE S18530 !$#authors Haydock, S.F.; Dowson, J.A.; Dhillon, N.; Roberts, G.A.; !1Cortes, J.; Leadlay, P.F. !$#journal Mol. Gen. Genet. (1991) 230:120-128 !$#title Cloning and sequence analysis of genes involved in !1erythromycin biosynthesis in Saccharopolyspora erythraea: !1sequence similarities between EryG and a family of !1S-adenosylmethionine-dependent methyltransferases. !$#cross-references MUID:92079886; PMID:1840640 !$#accession S18532 !'##status preliminary !'##molecule_type DNA !'##residues 1-247 ##label HAY !'##cross-references EMBL:X60379 REFERENCE S16744 !$#authors Haydock, S.F.; Dowson, J.A.; Dhillon, N.; Roberts, G.A.; !1Cortes, J.; Leadlay, P.F. !$#submission submitted to the EMBL Data Library, August 1991 !$#description Cloning and sequence analysis of genes involved in !1erythromycin biosynthesis in Saccharopolyspora erythraea: !1sequence similarities between eryG and a family of !1S-adenosylmethionine-dependent methyltransferases. !$#accession S16746 !'##status preliminary !'##molecule_type DNA !'##residues 1-35,'R',37-54,'R',56-247 ##label HAY2 !'##cross-references EMBL:X60379; NID:g48941; PIDN:CAA42928.1; !1PID:g48944 CLASSIFICATION #superfamily oleoyl-[acyl-carrier-protein] hydrolase; !1oleoyl-[acyl-carrier-protein] hydrolase homology FEATURE !$17-227 #domain oleoyl-[acyl-carrier-protein] hydrolase !8homology #label ACPH SUMMARY #length 247 #molecular-weight 26408 #checksum 1270 SEQUENCE /// ENTRY D47031 #type complete TITLE orf2 3' of bah - Streptomyces hygroscopicus ORGANISM #formal_name Streptomyces hygroscopicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS D47031 REFERENCE A47031 !$#authors Raibaud, A.; Zalacain, M.; Holt, T.G.; Tizard, R.; Thompson, !1C.J. !$#journal J. Bacteriol. (1991) 173:4454-4463 !$#title Nucleotide sequence analysis reveals linked N-acetyl !1hydrolase, thioesterase, transport, and regulatory genes !1encoded by the bialaphos biosynthetic gene cluster of !1Streptomyces hygroscopicus. !$#cross-references MUID:91294191; PMID:2066341 !$#accession D47031 !'##status preliminary !'##molecule_type DNA !'##residues 1-260 ##label RAI !'##note sequence extracted from NCBI backbone (NCBIN:41300, !1NCBIP:41306) CLASSIFICATION #superfamily oleoyl-[acyl-carrier-protein] hydrolase; !1oleoyl-[acyl-carrier-protein] hydrolase homology FEATURE !$26-240 #domain oleoyl-[acyl-carrier-protein] hydrolase !8homology #label ACPH SUMMARY #length 260 #molecular-weight 28147 #checksum 5319 SEQUENCE /// ENTRY C47031 #type complete TITLE orf1 3'of bah - Streptomyces hygroscopicus ORGANISM #formal_name Streptomyces hygroscopicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C47031 REFERENCE A47031 !$#authors Raibaud, A.; Zalacain, M.; Holt, T.G.; Tizard, R.; Thompson, !1C.J. !$#journal J. Bacteriol. (1991) 173:4454-4463 !$#title Nucleotide sequence analysis reveals linked N-acetyl !1hydrolase, thioesterase, transport, and regulatory genes !1encoded by the bialaphos biosynthetic gene cluster of !1Streptomyces hygroscopicus. !$#cross-references MUID:91294191; PMID:2066341 !$#accession C47031 !'##status preliminary !'##molecule_type DNA !'##residues 1-253 ##label RAI !'##cross-references GB:M64783; NID:g153172; PIDN:AAA79278.1; !1PID:g153174 !'##note sequence extracted from NCBI backbone (NCBIN:41300, !1NCBIP:41305) CLASSIFICATION #superfamily oleoyl-[acyl-carrier-protein] hydrolase; !1oleoyl-[acyl-carrier-protein] hydrolase homology FEATURE !$16-228 #domain oleoyl-[acyl-carrier-protein] hydrolase !8homology #label ACPH SUMMARY #length 253 #molecular-weight 27630 #checksum 7589 SEQUENCE /// ENTRY JQ0417 #type complete TITLE oleoyl-[acyl-carrier-protein] hydrolase (EC 3.1.2.14) homolog - Vibrio anguillarum ALTERNATE_NAMES hypothetical 28.1K protein; ORF6 protein; S-acyl fatty acid synthase thioesterase-like protein ORGANISM #formal_name Vibrio anguillarum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JQ0417; S26422 REFERENCE JQ0416 !$#authors Farrell, D.H.; Mikesell, P.; Actis, L.A.; Crosa, J.H. !$#journal Gene (1990) 86:45-51 !$#title A regulatory gene, angR, of the iron uptake system of Vibrio !1anguillarum: similarity with phage P22 cro and regulation by !1iron. !$#cross-references MUID:90185247; PMID:2311935 !$#accession JQ0417 !'##molecule_type DNA !'##residues 1-252 ##label FAR !'##cross-references GB:M34504; NID:g155150; PIDN:AAA79861.1; !1PID:g155153 REFERENCE S26421 !$#authors Tolmasky, M.E.; Actis, L.A.; Waldbeser, L.S.; Crosa, J.H. !$#submission submitted to the EMBL Data Library, April 1992 !$#description Genetic characterization of the regulatory protein AngR: !1presence of leucine zippers and evidence for a biosynthetic !1function. !$#accession S26422 !'##status preliminary !'##molecule_type DNA !'##residues 1-252 ##label TOL !'##cross-references EMBL:Z12000; NID:g48322; PIDN:CAA78045.1; !1PID:g48324 COMMENT This pathogenic bacterium is a causative agent of vibriosis, !1a widespread septicemic disease in marine fish. CLASSIFICATION #superfamily oleoyl-[acyl-carrier-protein] hydrolase; !1oleoyl-[acyl-carrier-protein] hydrolase homology KEYWORDS thiolester hydrolase FEATURE !$19-234 #domain oleoyl-[acyl-carrier-protein] hydrolase !8homology #label ACPH SUMMARY #length 252 #molecular-weight 28070 #checksum 2724 SEQUENCE /// ENTRY S57592 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) MRE11 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YM9959.06c; protein YMR224c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 12-Nov-1999 ACCESSIONS S57592; S55271; S27428 REFERENCE S57587 !$#authors Skelton, J.; Churcher, C.M. !$#submission submitted to the EMBL Data Library, June 1995 !$#accession S57592 !'##molecule_type DNA !'##residues 1-692 ##label SKE !'##cross-references EMBL:Z49939; NID:g887599; PIDN:CAA90195.1; !1PID:g887605; GSPDB:GN00013; MIPS:YMR224c !'##experimental_source strain AB972 REFERENCE S55265 !$#authors Johzuka, K.; Ogawa, H. !$#journal Genetics (1995) 139:1521-1532 !$#title Interaction of Mre11 and Rad50: two proteins required for !1DNA repair and meiosis-specific double-strand break !1formation in Saccharomyces cerevisiae. !$#cross-references MUID:95309669; PMID:7789757 !$#accession S55271 !'##molecule_type DNA !'##residues 1-643 ##label JOH !'##cross-references EMBL:D11463; NID:g1513064 !'##note the sequence in GenBank entry YSCMRE11, release 103, !1(PID:g1513065) has been revised and yields a full length !1translation GENETICS !$#gene SGD:MRE11; MIPS:YMR224c !'##cross-references SGD:S0004837; MIPS:YMR224c !$#map_position 13R CLASSIFICATION #superfamily probable phosphoesterase MRE11; phosphoesterase !1core homology KEYWORDS DNA recombination; DNA repair; hydrolase; meiosis FEATURE !$10-126 #domain phosphoesterase core homology #label PEC SUMMARY #length 692 #molecular-weight 77650 #checksum 4511 SEQUENCE /// ENTRY S58097 #type complete TITLE probable dna repair phosphoesterase (EC 3.1.-.-) rad32 - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES protein SPAC13C5.07 ORGANISM #formal_name Schizosaccharomyces pombe DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Dec-1999 ACCESSIONS S58097; S53875; T37620 REFERENCE S58093 !$#authors Devlin, K.; Churcher, C.M. !$#submission submitted to the EMBL Data Library, July 1995 !$#accession S58097 !'##molecule_type DNA !'##residues 1-649 ##label DEV !'##cross-references EMBL:Z50112; NID:g908889; PIDN:CAA90458.1; !1PID:g908896 !'##experimental_source strain 972h(-) REFERENCE S53875 !$#authors Tavassoli, M.; Shayeghi, M.; Nasim, A.; Watts, F.Z. !$#journal Nucleic Acids Res. (1995) 23:383-388 !$#title Cloning and characterisation of the Schizosaccharomyces !1pombe rad32 gene: a gene required for repair of double !1strand breaks and recombination. !$#cross-references MUID:95192046; PMID:7885834 !$#accession S53875 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-129,131-649 ##label TAV !'##cross-references EMBL:X82322; NID:g706836 !'##experimental_source strain 972h(-) !'##note translation of the GenBank sequence contains residue 130, has !1216-Val, and ends prematurely at residue 478 REFERENCE Z21731 !$#authors Devlin, K.; Churcher, C.M.; Barrell, B.G.; Rajandream, M.A.; !1Walsh, S.V. !$#submission submitted to the EMBL Data Library, July 1995 !$#accession T37620 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-649 ##label DE2 !'##cross-references EMBL:Z50112; PIDN:CAA90458.1; GSPDB:GN00066; !1SPDB:SPAC13C5.07 !'##experimental_source strain 972h-; cosmid c13C5 GENETICS !$#gene rad32; SPDB:SPAC13C5.07 !$#map_position 1 !$#introns 56/3; 225/2; 417/1; 478/2 CLASSIFICATION #superfamily probable phosphoesterase MRE11; phosphoesterase !1core homology KEYWORDS DNA recombination; DNA repair; hydrolase; meiosis FEATURE !$19-135 #domain phosphoesterase core homology #label PEC SUMMARY #length 649 #molecular-weight 73688 #checksum 8688 SEQUENCE /// ENTRY H64413 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) MJ0912 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 30-Oct-1998 #sequence_revision 30-Oct-1998 #text_change 21-Jul-2000 ACCESSIONS H64413 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession H64413 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-243 ##label BUL !'##cross-references GB:U67535; GB:L77117; NID:g2826348; !1PIDN:AAB98917.1; PID:g1499745; TIGR:MJ0912 COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#map_position FOR843690-844421 CLASSIFICATION #superfamily probable phosphoesterase MJ0912; !1phosphoesterase core homology KEYWORDS hydrolase FEATURE !$5-67 #domain phosphoesterase core homology #label PEC SUMMARY #length 243 #molecular-weight 27819 #checksum 6055 SEQUENCE /// ENTRY H71040 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) PH1616 [similarity] - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 30-Oct-1998 #sequence_revision 30-Oct-1998 #text_change 14-Dec-2001 ACCESSIONS H71040 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession H71040 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-233 ##label KAW !'##cross-references GB:AP000006; NID:g3236133; PIDN:BAA30728.1; !1PID:g3258045 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene PH1616 CLASSIFICATION #superfamily probable phosphoesterase MJ0912; !1phosphoesterase core homology KEYWORDS hydrolase FEATURE !$5-69 #domain phosphoesterase core homology #label PEC SUMMARY #length 233 #molecular-weight 26994 #checksum 2069 SEQUENCE /// ENTRY A75174 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) PAB1999 [similarity] - Pyrococcus abyssi (strain Orsay) ORGANISM #formal_name Pyrococcus abyssi DATE 20-Aug-1999 #sequence_revision 20-Aug-1999 #text_change 24-Aug-2001 ACCESSIONS A75174 REFERENCE A75001 !$#authors anonymous, Genoscope !$#submission submitted to the EMBL Data Library, July 1999 !$#description Pyrococcus abyssi genome sequence: insights into archaeal !1chromosome structure and evolution. !$#accession A75174 !'##molecule_type DNA !'##residues 1-233 ##label KAW !'##cross-references GB:AJ248284; GB:AL096836; NID:g5457730; !1PIDN:CAB49472.1; PID:g5457982 !'##experimental_source strain Orsay COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene PAB1999 CLASSIFICATION #superfamily probable phosphoesterase MJ0912; !1phosphoesterase core homology KEYWORDS hydrolase FEATURE !$5-69 #domain phosphoesterase core homology #label PEC SUMMARY #length 233 #molecular-weight 26930 #checksum 709 SEQUENCE /// ENTRY G71092 #type complete TITLE phosphoesterase-related protein PH1004 [similarity] - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 30-Oct-1998 #sequence_revision 30-Oct-1998 #text_change 11-Jan-2002 ACCESSIONS G71092 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession G71092 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-252 ##label KAW !'##cross-references GB:AP000004; NID:g3236131; PIDN:BAA30101.1; !1PID:g3257418 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank COMMENT Residues necessary for phosphoesterase activity are not !1conserved in this sequence. GENETICS !$#gene PH1004 CLASSIFICATION #superfamily probable phosphoesterase MJ0912; !1phosphoesterase core homology FEATURE !$3-74 #domain phosphoesterase core homology #label PEC SUMMARY #length 252 #molecular-weight 28640 #checksum 2514 SEQUENCE /// ENTRY A75073 #type complete TITLE phosphoesterase-related protein PAB1723 [similarity] - Pyrococcus abyssi (strain Orsay) ORGANISM #formal_name Pyrococcus abyssi DATE 20-Aug-1999 #sequence_revision 20-Aug-1999 #text_change 11-Jan-2002 ACCESSIONS A75073 REFERENCE A75001 !$#authors anonymous, Genoscope !$#submission submitted to the EMBL Data Library, July 1999 !$#description Pyrococcus abyssi genome sequence: insights into archaeal !1chromosome structure and evolution. !$#accession A75073 !'##status preliminary !'##molecule_type DNA !'##residues 1-252 ##label KAW !'##cross-references GB:AJ248286; GB:AL096836; NID:g5458366; !1PIDN:CAB49886.1; PID:g5458398 !'##experimental_source strain Orsay COMMENT Residues necessary for phosphoesterase activity are not !1conserved in this sequence. GENETICS !$#gene PAB1723 CLASSIFICATION #superfamily probable phosphoesterase MJ0912; !1phosphoesterase core homology FEATURE !$3-74 #domain phosphoesterase core homology #label PEC SUMMARY #length 252 #molecular-weight 28478 #checksum 2509 SEQUENCE /// ENTRY H84387 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) rad24c [similarity] - Halobacterium sp. NRC-1 ALTERNATE_NAMES DNA repair protein rad24c ORGANISM #formal_name Halobacterium sp. NRC-1 DATE 02-Feb-2001 #sequence_revision 02-Feb-2001 #text_change 24-Aug-2001 ACCESSIONS H84387 REFERENCE A84160 !$#authors Ng, W.V.; Kennedy, S.P.; Mahairas, G.G.; Berquist, B.; Pan, !1M.; Shukla, H.D.; Lasky, S.R.; Baliga, N.; Thorsson, V.; !1Sbrogna, J.; Swartzell, S.; Weir, D.; Hall, J.; Dahl, T.A.; !1Welti, R.; Goo, Y.A.; Leithauser, B.; Keller, K.; Cruz, R.; !1Danson, M.J.; Hough, D.W.; Maddocks, D.G.; Jablonski, P.E.; !1Krebs, M.P.; Angevine, C.M.; Dale, H.; Isenbarger, T.A.; !1Peck, R.F.; Pohlschrod, M.; Spudich, J.L.; Jung, K.H.; Alam, !1M.; Freitas, T.; Hou, S.; Daniels, C.J.; Dennis, P.P.; Omer, !1A.D.; Ebhardt, H.; Lowe, T.M.; Liang, P.; Riley, M.; Hood, !1L.; DasSarma, S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (2000) 97:12176-12181 !$#title Genome sequence of Halobacterium species NRC-1. !$#cross-references MUID:20504483; PMID:11016950 !$#accession H84387 !'##molecule_type DNA !'##residues 1-227 ##label STO !'##cross-references GB:AE004437; NID:g10581780; PIDN:AAG20468.1; !1GSPDB:GN00138 COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene rad24c CLASSIFICATION #superfamily probable phosphoesterase MJ0912; !1phosphoesterase core homology KEYWORDS hydrolase FEATURE !$2-62 #domain phosphoesterase core homology #label PEC SUMMARY #length 227 #molecular-weight 24814 #checksum 7990 SEQUENCE /// ENTRY E75287 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) DR2331 [similarity] - Deinococcus radiodurans (strain R1) ORGANISM #formal_name Deinococcus radiodurans DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 24-Aug-2001 ACCESSIONS E75287 REFERENCE A75250 !$#authors White, O.; Eisen, J.A.; Heidelberg, J.F.; Hickey, E.K.; !1Peterson, J.D.; Dodson, R.J.; Haft, D.H.; Gwinn, M.L.; !1Nelson, W.C.; Richardson, D.L.; Moffat, K.S.; Qin, H.; !1Jiang, L.; Pamphile, W.; Crosby, M.; Shen, M.; Vamathevan, !1J.J.; Lam, P.; McDonald, L.; Utterback, T.; Zalewski, C.; !1Makarova, K.S.; Aravind, L.; Daly, M.J.; Minton, K.W.; !1Fleischmann, R.D.; Ketchum, K.A.; Nelson, K.E.; Salzberg, !1S.; Smith, H.O.; Venter, J.C.; Fraser, C.M. !$#journal Science (1999) 286:1571-1577 !$#title Genome sequence of the radioresistant bacterium Deinococcus !1radiodurans R1. !$#cross-references MUID:20036896; PMID:10567266 !$#accession E75287 !'##molecule_type DNA !'##residues 1-253 ##label WHI !'##cross-references GB:AE002064; GB:AE000513; NID:g6460134; !1PIDN:AAF11877.1; PID:g6460142; TIGR:DR2331; GSPDB:GN00077 !'##experimental_source strain R1 COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene DR2331 !$#map_position 1 CLASSIFICATION #superfamily probable phosphoesterase MJ0912; !1phosphoesterase core homology KEYWORDS hydrolase FEATURE !$5-67 #domain phosphoesterase core homology #label PEC SUMMARY #length 253 #molecular-weight 28248 #checksum 9707 SEQUENCE /// ENTRY B95072 #type complete TITLE phosphoesterase-related protein SP0619 [similarity] - Streptococcus pneumoniae (strain TIGR4) ORGANISM #formal_name Streptococcus pneumoniae DATE 03-Aug-2001 #sequence_revision 03-Aug-2001 #text_change 02-Nov-2001 ACCESSIONS B95072 REFERENCE A95000 !$#authors Tettelin, H.; Nelson, K.E.; Paulsen, I.T.; Eisen, J.A.; !1Read, T.D.; Peterson, S.; Heidelberg, J.; DeBoy, R.T.; Haft, !1D.H.; Dodson, R.J.; Durkin, A.S.; Gwinn, M.; Kolonay, J.F.; !1Nelson, W.C.; Peterson, J.D.; Umayam, L.A.; White, O.; !1Salzberg, S.L.; Lewis, M.R.; Radune, D.; Holtzapple, E.; !1Khouri, H.; Wolf, A.M.; Utterback, T.R.; Hansen, C.L.; !1McDonald, L.A.; Feldblyum, T.V.; Angiuoli, S.; Dickinson, !1T.; Hickey, E.K.; Holt, I.E.; Loftus, B.J.; Yang, F.; Smith, !1H.O.; Venter, J.C.; Dougherty, B.A.; Morrison, D.A.; !1Hollingshead, S.K.; Fraser, C.M. !$#journal Science (2001) 293:498-506 !$#title Complete Genome Sequence of a virulent isolate of !1Streptococcus pneumoniae. !$#cross-references MUID:21357209; PMID:11463916 !$#accession B95072 !'##molecule_type DNA !'##residues 1-277 ##label KUR !'##cross-references GB:AE005672; PIDN:AAK74771.1; PID:g14972095; !1GSPDB:GN00164; TIGR:SP4SP0619 !'##experimental_source strain TIGR4 COMMENT Although this sequence has motifs characteristic of a !1variety of phosphoesterases, a critical active site residue !1is not conserved. GENETICS !$#gene SP0619 CLASSIFICATION #superfamily probable phosphoesterase MJ0912; !1phosphoesterase core homology FEATURE !$4-67 #domain phosphoesterase core homology #label PEC SUMMARY #length 277 #molecular-weight 31523 #checksum 2961 SEQUENCE /// ENTRY E75479 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) DR0761 [similarity] - Deinococcus radiodurans (strain R1) ORGANISM #formal_name Deinococcus radiodurans DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 09-Nov-2001 ACCESSIONS E75479 REFERENCE A75250 !$#authors White, O.; Eisen, J.A.; Heidelberg, J.F.; Hickey, E.K.; !1Peterson, J.D.; Dodson, R.J.; Haft, D.H.; Gwinn, M.L.; !1Nelson, W.C.; Richardson, D.L.; Moffat, K.S.; Qin, H.; !1Jiang, L.; Pamphile, W.; Crosby, M.; Shen, M.; Vamathevan, !1J.J.; Lam, P.; McDonald, L.; Utterback, T.; Zalewski, C.; !1Makarova, K.S.; Aravind, L.; Daly, M.J.; Minton, K.W.; !1Fleischmann, R.D.; Ketchum, K.A.; Nelson, K.E.; Salzberg, !1S.; Smith, H.O.; Venter, J.C.; Fraser, C.M. !$#journal Science (1999) 286:1571-1577 !$#title Genome sequence of the radioresistant bacterium Deinococcus !1radiodurans R1. !$#cross-references MUID:20036896; PMID:10567266 !$#accession E75479 !'##molecule_type DNA !'##residues 1-308 ##label WHI !'##cross-references GB:AE001931; GB:AE000513; NID:g6458461; !1PIDN:AAF10339.1; PID:g6458471; TIGR:DR0761; GSPDB:GN00077 !'##experimental_source strain R1 COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene DR0761 !$#map_position 1 CLASSIFICATION #superfamily probable phosphoesterase MJ0912; !1phosphoesterase core homology KEYWORDS hydrolase FEATURE !$34-97 #domain phosphoesterase core homology #label PEC SUMMARY #length 308 #molecular-weight 33938 #checksum 1296 SEQUENCE /// ENTRY H97939 #type complete TITLE phosphoesterase-related protein spr0544 [similarity] - Streptococcus pneumoniae (strain R6) ORGANISM #formal_name Streptococcus pneumoniae DATE 22-Oct-2001 #sequence_revision 22-Oct-2001 #text_change 09-Nov-2001 ACCESSIONS H97939 REFERENCE A97872 !$#authors Hoskins, J.A.; Alborn Jr., W.; Arnold, J.; Blaszczak, L.; !1Burgett, S.; DeHoff, B.S.; Estrem, S.; Fritz, L.; Fu, D.J.; !1Fuller, W.; Geringer, C.; Gilmour, R.; Glass, J.S.; Khoja, !1H.; Kraft, A.; LaGace, R.; LeBlanc, D.J.; Lee, L.N.; !1Lefkowitz, E.J.; Lu, J.; Matsushima, P.; McAhren, S.; !1McHenney, M.; McLeaster, K.; Mundy, C.; Nicas, T.I.; Norris, !1F.H.; O'Gara, M.; Peery, R.; Robertson, G.T.; Rockey, P.; !1Sun, P.M.; Winkler, M.E.; Yang, Y.; Young-Bellido, M.; Zhao, !1G.; Zook, C.; Baltz, R.H.; Jaskunas, S.R.; Rosteck Jr., !1P.R.; Skatrud, P.L.; Glass, J.I. !$#journal J. Bacteriol. (2001) 183:5709-5717 !$#title Genome of the Bacterium Streptococcus pneumoniae Strain R6. !$#cross-references MUID:21429245; PMID:11544234 !$#accession H97939 !'##molecule_type DNA !'##residues 1-277 ##label KUR !'##cross-references GB:AE007317; PIDN:AAK99348.1; PID:g15458120; !1GSPDB:GN00174 COMMENT Although this sequence has motifs characteristic of a !1variety of phosphoesterases, a critical active site residue !1is not conserved. GENETICS !$#gene spr0544 CLASSIFICATION #superfamily probable phosphoesterase MJ0912; !1phosphoesterase core homology FEATURE !$4-67 #domain phosphoesterase core homology #label PEC SUMMARY #length 277 #molecular-weight 31507 #checksum 2475 SEQUENCE /// ENTRY D95190 #type complete TITLE phosphoesterase-related protein SP1637 [similarity] - Streptococcus pneumoniae (strain TIGR4) ORGANISM #formal_name Streptococcus pneumoniae DATE 03-Aug-2001 #sequence_revision 03-Aug-2001 #text_change 02-Nov-2001 ACCESSIONS D95190 REFERENCE A95000 !$#authors Tettelin, H.; Nelson, K.E.; Paulsen, I.T.; Eisen, J.A.; !1Read, T.D.; Peterson, S.; Heidelberg, J.; DeBoy, R.T.; Haft, !1D.H.; Dodson, R.J.; Durkin, A.S.; Gwinn, M.; Kolonay, J.F.; !1Nelson, W.C.; Peterson, J.D.; Umayam, L.A.; White, O.; !1Salzberg, S.L.; Lewis, M.R.; Radune, D.; Holtzapple, E.; !1Khouri, H.; Wolf, A.M.; Utterback, T.R.; Hansen, C.L.; !1McDonald, L.A.; Feldblyum, T.V.; Angiuoli, S.; Dickinson, !1T.; Hickey, E.K.; Holt, I.E.; Loftus, B.J.; Yang, F.; Smith, !1H.O.; Venter, J.C.; Dougherty, B.A.; Morrison, D.A.; !1Hollingshead, S.K.; Fraser, C.M. !$#journal Science (2001) 293:498-506 !$#title Complete Genome Sequence of a virulent isolate of !1Streptococcus pneumoniae. !$#cross-references MUID:21357209; PMID:11463916 !$#accession D95190 !'##molecule_type DNA !'##residues 1-282 ##label KUR !'##cross-references GB:AE005672; PIDN:AAK75717.1; PID:g14973127; !1GSPDB:GN00164; TIGR:SP4SP1637 !'##experimental_source strain TIGR4 COMMENT Although this sequence has motifs characteristic of a !1variety of phosphoesterases, a critical active site residue !1is not conserved. GENETICS !$#gene SP1637 CLASSIFICATION #superfamily probable phosphoesterase MJ0912; !1phosphoesterase core homology FEATURE !$5-68 #domain phosphoesterase core homology #label PEC SUMMARY #length 282 #molecular-weight 32640 #checksum 3007 SEQUENCE /// ENTRY F98056 #type complete TITLE phosphoesterase-related protein spr1479 [similarity] - Streptococcus pneumoniae (strain R6) ORGANISM #formal_name Streptococcus pneumoniae DATE 22-Oct-2001 #sequence_revision 22-Oct-2001 #text_change 09-Nov-2001 ACCESSIONS F98056 REFERENCE A97872 !$#authors Hoskins, J.A.; Alborn Jr., W.; Arnold, J.; Blaszczak, L.; !1Burgett, S.; DeHoff, B.S.; Estrem, S.; Fritz, L.; Fu, D.J.; !1Fuller, W.; Geringer, C.; Gilmour, R.; Glass, J.S.; Khoja, !1H.; Kraft, A.; LaGace, R.; LeBlanc, D.J.; Lee, L.N.; !1Lefkowitz, E.J.; Lu, J.; Matsushima, P.; McAhren, S.; !1McHenney, M.; McLeaster, K.; Mundy, C.; Nicas, T.I.; Norris, !1F.H.; O'Gara, M.; Peery, R.; Robertson, G.T.; Rockey, P.; !1Sun, P.M.; Winkler, M.E.; Yang, Y.; Young-Bellido, M.; Zhao, !1G.; Zook, C.; Baltz, R.H.; Jaskunas, S.R.; Rosteck Jr., !1P.R.; Skatrud, P.L.; Glass, J.I. !$#journal J. Bacteriol. (2001) 183:5709-5717 !$#title Genome of the Bacterium Streptococcus pneumoniae Strain R6. !$#cross-references MUID:21429245; PMID:11544234 !$#accession F98056 !'##molecule_type DNA !'##residues 1-282 ##label KUR !'##cross-references GB:AE007317; PIDN:AAL00283.1; PID:g15459137; !1GSPDB:GN00174 COMMENT Although this sequence has motifs characteristic of a !1variety of phosphoesterases, a critical active site residue !1is not conserved. GENETICS !$#gene spr1479 CLASSIFICATION #superfamily probable phosphoesterase MJ0912; !1phosphoesterase core homology FEATURE !$5-68 #domain phosphoesterase core homology #label PEC SUMMARY #length 282 #molecular-weight 32640 #checksum 3094 SEQUENCE /// ENTRY H97638 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) AGR_C_4222 [similarity] - Agrobacterium tumefaciens (strain C58, Cereon) ORGANISM #formal_name Agrobacterium tumefaciens DATE 30-Sep-2001 #sequence_revision 30-Sep-2001 #text_change 18-Nov-2002 ACCESSIONS H97638 REFERENCE A97359 !$#authors Goodner, B.; Hinkle, G.; Gattung, S.; Miller, N.; Blanchard, !1M.; Qurollo, B.; Goldman, B.S.; Cao, Y.; Askenazi, M.; !1Halling, C.; Mullin, L.; Houmiel, K.; Gordon, J.; Vaudin, !1M.; Iartchouk, O.; Epp, A.; Liu, F.; Wollam, C.; Allinger, !1M.; Doughty, D.; Scott, C.; Lappas, C.; Markelz, B.; !1Flanagan, C.; Crowell, C.; Gurson, J.; Lomo, C.; Sear, C.; !1Strub, G.; Cielo, C.; Slater, S. !$#journal Science (2001) 294:2323-2328 !$#title Genome Sequence of the Plant Pathogen and Biotechnology !1Agent Agrobacterium tumefaciens C58. !$#cross-references MUID:21608551; PMID:11743194 !$#accession H97638 !'##molecule_type DNA !'##residues 1-247 ##label KUR !'##cross-references GB:AE007869; PIDN:AAK88065.1; PID:g15157489; !1GSPDB:GN00169 COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene AGR_C_4222 !$#map_position circular chromosome CLASSIFICATION #superfamily probable phosphoesterase MJ0912; !1phosphoesterase core homology KEYWORDS hydrolase FEATURE !$2-64 #domain phosphoesterase core homology #label PEC SUMMARY #length 247 #molecular-weight 27232 #checksum 3573 SEQUENCE /// ENTRY A69819 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) yhaO - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 03-Aug-2001 #sequence_revision 03-Aug-2001 #text_change 03-Aug-2001 ACCESSIONS A69819 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69819 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-408 ##label KUN !'##cross-references GB:Z99109; GB:AL009126; NID:g2633260; !1PIDN:CAB12831.1; PID:e1182993; PID:g2633327 !'##experimental_source strain 168 COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene yhaO CLASSIFICATION #superfamily Bacillus subtilis probable phosphoesterase !1yhaO; phosphoesterase core homology KEYWORDS hydrolase FEATURE !$6-98 #domain phosphoesterase core homology #label PEC SUMMARY #length 408 #molecular-weight 46810 #checksum 5913 SEQUENCE /// ENTRY C89971 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) SA1662 [imported] - Staphylococcus aureus (strain N315) ORGANISM #formal_name Staphylococcus aureus DATE 03-Aug-2001 #sequence_revision 03-Aug-2001 #text_change 22-Oct-2001 ACCESSIONS C89971 REFERENCE A89758 !$#authors Kuroda, M.; Ohta, T.; Uchiyama, I.; Baba, T.; Yuzawa, H.; !1Kobayashi, I.; Cui, L.; Oguchi, A.; Aoki, K.; Nagai, Y.; !1Lian, J.; Ito, T.; Kanamori, M.; Matsumaru, H.; Maruyama, !1A.; Murakami, H.; Hosoyama, A.; Mizutani-Ui, Y.; Kobayashi, !1N.; Sawano, T.; Inoue, R.; Kaito, C.; Sekimizu, K.; !1Hirakawa, H.; Kuhara, S.; Goto, S.; Yabuzaki, J.; Kanehisa, !1M.; Yamashita, A.; Oshima, K.; Furuya, K.; Yoshino, C.; !1Shiba, T.; Hattori, M.; Ogasawara, N.; Hayashi, H.; !1Hiramatsu, K. !$#journal Lancet (2001) 357:1225-1240 !$#title Whole genome sequencing of meticillin-resistant !1Stapylococcus aureus. !$#cross-references MUID:21311952; PMID:11418146 !$#accession C89971 !'##molecule_type DNA !'##residues 1-398 ##label KUR !'##cross-references GB:BA000018; NID:g13701637; PIDN:BAB42930.1; !1GSPDB:GN00149 !'##experimental_source strain N315 COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene SA1662 CLASSIFICATION #superfamily Bacillus subtilis probable phosphoesterase !1yhaO; phosphoesterase core homology KEYWORDS hydrolase FEATURE !$3-95 #domain phosphoesterase core homology #label PEC SUMMARY #length 398 #molecular-weight 46224 #checksum 6970 SEQUENCE /// ENTRY D64480 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) MJ1445 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 13-Sep-1996 #sequence_revision 13-Sep-1996 #text_change 11-Jun-1999 ACCESSIONS D64480 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession D64480 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-176 ##label BUL !'##cross-references GB:U67585; GB:L77117; NID:g1592088; !1PIDN:AAB99460.1; PID:g1500327; TIGR:MJ1445 GENETICS !$#map_position FOR1414333-1414863 CLASSIFICATION #superfamily probable phosphoesterase MJ1445; !1phosphoesterase core homology KEYWORDS hydrolase FEATURE !$5-86 #domain phosphoesterase core homology #label PEC SUMMARY #length 176 #molecular-weight 20713 #checksum 2574 SEQUENCE /// ENTRY S31011 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) - Mycobacterium phage L5 ALTERNATE_NAMES gene 66 protein ORGANISM #formal_name Mycobacterium phage L5 DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 11-Jun-1999 ACCESSIONS S31011 REFERENCE S30949 !$#authors Donnelly-Wu, M.K.; Jacobs Jr., W.R.; Hatfull, G.F. !$#journal Mol. Microbiol. (1993) 7:407-417 !$#title Superinfection immunity of mycobacteriophage L5: !1applications for genetic transformation of mycobacteria. !$#cross-references MUID:93211283; PMID:8459767 !$#accession S31011 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-207 ##label DON !'##cross-references EMBL:Z18946; NID:g15859; PIDN:CAA79442.1; !1PID:g15922 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1992 GENETICS !$#gene 66 CLASSIFICATION #superfamily probable phosphoesterase MJ1445; !1phosphoesterase core homology KEYWORDS hydrolase FEATURE !$3-84 #domain phosphoesterase core homology #label PEC SUMMARY #length 207 #molecular-weight 23581 #checksum 6982 SEQUENCE /// ENTRY E70444 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) aq_1666 - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 08-May-1998 #sequence_revision 15-May-1998 #text_change 11-Jun-1999 ACCESSIONS E70444 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession E70444 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-193 ##label AQF !'##cross-references GB:AE000750; NID:g2983999; PIDN:AAC07557.1; !1PID:g2984012; GB:AE000657 !'##experimental_source strain VF5 GENETICS !$#gene aq_1666 CLASSIFICATION #superfamily probable phosphoesterase MJ1445; !1phosphoesterase core homology KEYWORDS hydrolase FEATURE !$1-80 #domain phosphoesterase core homology #label PEC SUMMARY #length 193 #molecular-weight 23462 #checksum 2811 SEQUENCE /// ENTRY S76981 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) slr0306 - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 25-Apr-1997 #sequence_revision 25-Apr-1997 #text_change 02-Aug-2002 ACCESSIONS S76981 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76981 !'##status preliminary !'##molecule_type DNA !'##residues 1-506 ##label KAN !'##cross-references EMBL:D64005; GB:AB001339; NID:g1001779; !1PIDN:BAA10673.1; PID:d1011324; PID:g1001793 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. CLASSIFICATION #superfamily probable phosphoesterase MJ1445; !1phosphoesterase core homology KEYWORDS hydrolase SUMMARY #length 506 #molecular-weight 55300 #checksum 1059 SEQUENCE /// ENTRY A69809 #type complete TITLE probable multifunctional phosphoesterase (EC 3.1.-.-) yfkN - Bacillus subtilis CONTAINS probable 2',3'-cyclic-nucleotide 2'-phosphodiesterase (EC 3.1.4.16); probable 5'-nucleotidase (EC 3.1.3.5) ORGANISM #formal_name Bacillus subtilis DATE 05-Dec-1997 #sequence_revision 05-Dec-1997 #text_change 16-Jun-2000 ACCESSIONS A69809 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69809 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-1462 ##label KUN !'##cross-references GB:Z99108; GB:AL009126; NID:g2633055; !1PIDN:CAB12613.1; PID:g2633108 !'##experimental_source strain 168 GENETICS !$#gene yfkN CLASSIFICATION #superfamily probable multifunctional phosphoesterase yfkN; !12',3'-cyclic-nucleotide 2'-phosphodiesterase homology; !15'-nucleotidase homology; phosphoesterase core homology KEYWORDS phosphoric diester hydrolase; phosphoric monoester hydrolase FEATURE !$43-609 #domain 2',3'-cyclic-nucleotide 2'-phosphodiesterase !8homology #label CPDB\ !$46-143 #domain phosphoesterase core homology #label PEC1\ !$667-1155 #domain 5'-nucleotidase homology #label NT5\ !$670-742 #domain phosphoesterase core homology #label PEC2 SUMMARY #length 1462 #molecular-weight 159705 #checksum 521 SEQUENCE /// ENTRY E70755 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) Rv1277 [similarity] - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 03-Aug-2001 #sequence_revision 03-Aug-2001 #text_change 03-Aug-2001 ACCESSIONS E70755 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession E70755 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-417 ##label COL !'##cross-references GB:Z77137; GB:AL123456; NID:g3261593; !1PIDN:CAB00917.1; PID:e1299886; PID:g3261599 !'##experimental_source strain H37Rv COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene Rv1277 CLASSIFICATION #superfamily Mycobacterium tuberculosis probable !1phosphoesterase Rv1277; phosphoesterase core homology KEYWORDS hydrolase FEATURE !$20-122 #domain phosphoesterase core homology #label PEC SUMMARY #length 417 #molecular-weight 44790 #checksum 5848 SEQUENCE /// ENTRY A87049 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) ML1119 [similarity] - Mycobacterium leprae ORGANISM #formal_name Mycobacterium leprae DATE 03-Aug-2001 #sequence_revision 03-Aug-2001 #text_change 03-Aug-2001 ACCESSIONS A87049 REFERENCE A86909 !$#authors Cole, S.T.; Eiglmeier, K.; Parkhill, J.; James, K.D.; !1Thomson, N.R.; Wheeler, P.R.; Honore, N.; Ganier, T.; !1Churcher, C.; Harris, D.; Mungall, K.; Basham, D.; Brown, !1D.; Chillingworth, T.; Connor, R.; Davies, R.M.; Devlin, K.; !1Duthoy, S.; Feltwell, T.; Fraser, A.; Hamlin, N.; Holroyd, !1S.; Hornsby, T.; Jagels, K.; Lacroix, C.; Maclean, J.; !1Moule, S.; Murphy, L.; Oliver, K.; Quail, M.A.; Rajandream, !1M.A.; Rutherford, K.M.; Rutter, S.; Seeger, K.; Simon, S.; !1Simmonds, M.; Skelton, J.; Squares, R.; Squares, S.; !1Stevens, K.; Taylor, K.; Whitehead, S.; Woodward, J.R.; !1Barrell, B.G. !$#journal Nature (2001) 409:1007-1011 !$#title Massive gene decay in the leprosy bacillus. !$#cross-references MUID:21128732; PMID:11234002 !$#accession A87049 !'##molecule_type DNA !'##residues 1-383 ##label STO !'##cross-references GB:AL450380; NID:g13093102; PIDN:CAC31500.1; !1GSPDB:GN00147 COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene ML1119 CLASSIFICATION #superfamily Mycobacterium tuberculosis probable !1phosphoesterase Rv1277; phosphoesterase core homology KEYWORDS hydrolase FEATURE !$36-122 #domain phosphoesterase core homology #label PEC SUMMARY #length 383 #molecular-weight 41281 #checksum 1609 SEQUENCE /// ENTRY S73354 #type complete TITLE VPS29-like phosphoesterase-related protein MG207 homolog [similarity] - Mycoplasma pneumoniae (strain ATCC 29342) ALTERNATE_NAMES hypothetical protein C09_orf159 ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 24-Aug-2001 ACCESSIONS S73354 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73354 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-159 ##label HIM !'##cross-references EMBL:AE000004; GB:U00089; NID:g1673671; !1PIDN:AAB95676.1; PID:g1673676 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases; however, other members of the superfamily !1are missing a critical active site residue, suggesting that !1these proteins may have another function. GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily human vacuolar protein-sorting protein VPS29 !1homolog; phosphoesterase core homology SUMMARY #length 159 #molecular-weight 18339 #checksum 1290 SEQUENCE /// ENTRY H64222 #type complete TITLE VPS29-like phosphoesterase-related protein MG207 [similarity] - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 10-Sep-1999 #sequence_revision 02-Jun-2000 #text_change 24-Aug-2001 ACCESSIONS T09716; H64222 REFERENCE Z16818 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.L.; Nguyen, !1D.T.; Utterback, T.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Venter, J.C. !$#submission submitted to the EMBL Data Library, October 1998 !$#accession T09716 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-167 ##label FRA !'##cross-references EMBL:U39700; NID:g3844800; PID:g3844805 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession H64222 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 40-167 ##label TIGR !'##cross-references GB:U39698; GB:L43967; NID:g1045891; PID:g1045893; !1TIGR:MG207 !'##experimental_source strain G-37 !'##note this sequence is truncated at the amino end with respect to !1other members of this superfamily; it is missing the first !1of several sequence motifs and a critical active site !1residue found in a variety of phosphoesterases GENETICS !$#gene MG207 !$#genetic_code SGC3 CLASSIFICATION #superfamily human vacuolar protein-sorting protein VPS29 !1homolog; phosphoesterase core homology SUMMARY #length 167 #molecular-weight 19348 #checksum 3549 SEQUENCE /// ENTRY D69522 #type complete TITLE VPS29-like phosphoesterase-related protein AF2180 [similarity] - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 24-Aug-2001 ACCESSIONS D69522 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession D69522 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-175 ##label KLE !'##cross-references GB:AE000954; GB:AE000782; NID:g2689277; !1PIDN:AAB89070.1; PID:g2648343; TIGR:AF2180 COMMENT Although this sequence has motifs characteristic of a !1variety of phosphoesterases, a critical active site residue !1is not conserved. CLASSIFICATION #superfamily human vacuolar protein-sorting protein VPS29 !1homolog; phosphoesterase core homology SUMMARY #length 175 #molecular-weight 19731 #checksum 6794 SEQUENCE /// ENTRY D69986 #type complete TITLE VPS29-like phosphoesterase-related protein ysnB [similarity] - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 24-Aug-2001 ACCESSIONS D69986 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D69986 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-171 ##label KUN !'##cross-references GB:Z99118; GB:AL009126; NID:g2635200; !1PIDN:CAB14795.1; PID:g2635300 !'##experimental_source strain 168 COMMENT Although this sequence has motifs characteristic of a !1variety of phosphoesterases, a critical active site residue !1is not conserved. GENETICS !$#gene ysnB CLASSIFICATION #superfamily human vacuolar protein-sorting protein VPS29 !1homolog; phosphoesterase core homology SUMMARY #length 171 #molecular-weight 19155 #checksum 3461 SEQUENCE /// ENTRY E71262 #type complete TITLE VPS29-like phosphoesterase-related protein TP0937 [similarity] - syphilis spirochete ORGANISM #formal_name Treponema pallidum subsp. pallidum #common_name syphilis spirochete DATE 24-Jul-1998 #sequence_revision 24-Jul-1998 #text_change 02-Nov-2001 ACCESSIONS E71262 REFERENCE A71250 !$#authors Fraser, C.M.; Norris, S.J.; Weinstock, G.M.; White, O.; !1Sutton, G.G.; Dodson, R.; Gwinn, M.; Hickey, E.K.; Clayton, !1R.; Ketchum, K.A.; Sodergren, E.; Hardham, J.M.; McLeod, !1M.P.; Salzberg, S.; Peterson, J.; Khalak, H.; Richardson, !1D.; Howell, J.K.; Chidambaram, M.; Utterback, T.; McDonald, !1L.; Artiach, P.; Bowman, C.; Cotton, M.D.; Fujii, C.; !1Garland, S.; Hatch, B.; Horst, K.; Roberts, K.; Watthey, L.; !1Weidman, J.; Smith, H.O.; Venter, J.C. !$#journal Science (1998) 281:375-388 !$#title Complete genome sequence of Treponema pallidum, the syphilis !1spirochete. !$#cross-references MUID:98332770; PMID:9665876 !$#accession E71262 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-211 ##label COL !'##cross-references GB:AE001262; GB:AE000520; NID:g3323254; !1PIDN:AAC65894.1; PID:g3323258 !'##experimental_source strain Nichols COMMENT Although this sequence has motifs characteristic of a !1variety of phosphoesterases, a critical active site residue !1is not conserved. GENETICS !$#gene TP0937 CLASSIFICATION #superfamily human vacuolar protein-sorting protein VPS29 !1homolog; phosphoesterase core homology FEATURE !$28-95 #domain phosphoesterase core homology #label PEC SUMMARY #length 211 #molecular-weight 22799 #checksum 9103 SEQUENCE /// ENTRY H71029 #type complete TITLE VPS29-like phosphoesterase-related protein PH1530 [similarity] - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 11-Jan-2002 ACCESSIONS H71029 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession H71029 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-172 ##label KAW !'##cross-references GB:AP000006; NID:g3236133; PIDN:BAA30640.1; !1PID:g3257957 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1530 CLASSIFICATION #superfamily human vacuolar protein-sorting protein VPS29 !1homolog; phosphoesterase core homology FEATURE !$4-63 #domain phosphoesterase core homology #label PEC SUMMARY #length 172 #molecular-weight 18880 #checksum 5776 SEQUENCE /// ENTRY B70885 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) Rv2795c [similarity] - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 17-Jul-1998 #sequence_revision 17-Jul-1998 #text_change 02-Nov-2001 ACCESSIONS B70885 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession B70885 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-324 ##label COL !'##cross-references GB:AL008967; GB:AL123456; NID:g3261491; !1PIDN:CAA15590.1; PID:e1173925; PID:g2624317 !'##experimental_source strain H37Rv COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene Rv2795c CLASSIFICATION #superfamily Mycobacterium tuberculosis probable !1phosphoesterase Rv2795c; phosphoesterase core homology KEYWORDS hydrolase FEATURE !$16-81 #domain phosphoesterase core homology #label PEC SUMMARY #length 324 #molecular-weight 37600 #checksum 7525 SEQUENCE /// ENTRY F87102 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) ML1548 [similarity] - Mycobacterium leprae ORGANISM #formal_name Mycobacterium leprae DATE 20-Apr-2001 #sequence_revision 20-Apr-2001 #text_change 02-Nov-2001 ACCESSIONS F87102 REFERENCE A86909 !$#authors Cole, S.T.; Eiglmeier, K.; Parkhill, J.; James, K.D.; !1Thomson, N.R.; Wheeler, P.R.; Honore, N.; Ganier, T.; !1Churcher, C.; Harris, D.; Mungall, K.; Basham, D.; Brown, !1D.; Chillingworth, T.; Connor, R.; Davies, R.M.; Devlin, K.; !1Duthoy, S.; Feltwell, T.; Fraser, A.; Hamlin, N.; Holroyd, !1S.; Hornsby, T.; Jagels, K.; Lacroix, C.; Maclean, J.; !1Moule, S.; Murphy, L.; Oliver, K.; Quail, M.A.; Rajandream, !1M.A.; Rutherford, K.M.; Rutter, S.; Seeger, K.; Simon, S.; !1Simmonds, M.; Skelton, J.; Squares, R.; Squares, S.; !1Stevens, K.; Taylor, K.; Whitehead, S.; Woodward, J.R.; !1Barrell, B.G. !$#journal Nature (2001) 409:1007-1011 !$#title Massive gene decay in the leprosy bacillus. !$#cross-references MUID:21128732; PMID:11234002 !$#accession F87102 !'##molecule_type DNA !'##residues 1-321 ##label STO !'##cross-references GB:AL450380; NID:g13093367; PIDN:CAC30499.1; !1GSPDB:GN00147 COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene ML1548 CLASSIFICATION #superfamily Mycobacterium tuberculosis probable !1phosphoesterase Rv2795c; phosphoesterase core homology KEYWORDS hydrolase FEATURE !$13-78 #domain phosphoesterase core homology #label PEC SUMMARY #length 321 #molecular-weight 37459 #checksum 8617 SEQUENCE /// ENTRY T35171 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) SC5A7.22 [similarity] - Streptomyces coelicolor ORGANISM #formal_name Streptomyces coelicolor DATE 05-Nov-1999 #sequence_revision 05-Nov-1999 #text_change 02-Nov-2001 ACCESSIONS T35171 REFERENCE Z21570 !$#authors Seeger, K.J.; Harris, D.; Parkhill, J.; Barrell, B.G.; !1Rajandream, M.A. !$#submission submitted to the EMBL Data Library, July 1998 !$#accession T35171 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-295 ##label SEE !'##cross-references EMBL:AL031107; PIDN:CAA19951.1; GSPDB:GN00070; !1SCOEDB:SC5A7.22 !'##experimental_source strain A3(2) COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene SCOEDB:SC5A7.22 CLASSIFICATION #superfamily Mycobacterium tuberculosis probable !1phosphoesterase Rv2795c; phosphoesterase core homology KEYWORDS hydrolase FEATURE !$10-75 #domain phosphoesterase core homology #label PEC SUMMARY #length 295 #molecular-weight 33530 #checksum 301 SEQUENCE /// ENTRY E64304 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) MJ0037 - Methanococcus jannaschii ALTERNATE_NAMES hypothetical protein MJ0037 ORGANISM #formal_name Methanococcus jannaschii DATE 24-Jul-1998 #sequence_revision 24-Jul-1998 #text_change 11-Jun-1999 ACCESSIONS E64304 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession E64304 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-238 ##label BUL !'##cross-references GB:U67462; GB:L77117; NID:g1590835; !1PIDN:AAB98018.1; PID:g1498797; TIGR:MJ0037 COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#map_position FOR38073-38789 CLASSIFICATION #superfamily probable phosphoesterase MJ0037; !1phosphoesterase core homology KEYWORDS hydrolase FEATURE !$22-109 #domain phosphoesterase core homology #label PEC SUMMARY #length 238 #molecular-weight 27684 #checksum 220 SEQUENCE /// ENTRY G71001 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) PHLF004 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 21-Aug-1998 #sequence_revision 21-Aug-1998 #text_change 16-Jun-2000 ACCESSIONS G71001 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession G71001 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-228 ##label KAW !'##cross-references GB:AP000006; NID:g3236133; PIDN:BAA30415.1; !1PID:g3257732 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene PH1310 CLASSIFICATION #superfamily probable phosphoesterase MJ0037; !1phosphoesterase core homology KEYWORDS hydrolase FEATURE !$15-102 #domain phosphoesterase core homology #label PEC SUMMARY #length 228 #molecular-weight 25617 #checksum 9006 SEQUENCE /// ENTRY F75129 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) PAB0562 [similarity] - Pyrococcus abyssi (strain Orsay) ORGANISM #formal_name Pyrococcus abyssi DATE 03-Aug-2001 #sequence_revision 03-Aug-2001 #text_change 03-Aug-2001 ACCESSIONS F75129 REFERENCE A75001 !$#authors anonymous, Genoscope !$#submission submitted to the EMBL Data Library, July 1999 !$#description Pyrococcus abyssi genome sequence: insights into archaeal !1chromosome structure and evolution. !$#accession F75129 !'##molecule_type DNA !'##residues 1-229 ##label KAW !'##cross-references GB:AJ248285; GB:AL096836; NID:g5458067; !1PIDN:CAB49751.1; PID:g5458262 !'##experimental_source strain Orsay GENETICS !$#gene PAB0562 CLASSIFICATION #superfamily probable phosphoesterase MJ0037; !1phosphoesterase core homology KEYWORDS hydrolase FEATURE !$15-102 #domain phosphoesterase core homology #label PEC SUMMARY #length 229 #molecular-weight 25608 #checksum 2891 SEQUENCE /// ENTRY B69394 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) AF1155 - Archaeoglobus fulgidus ALTERNATE_NAMES MJ0037 homolog ORGANISM #formal_name Archaeoglobus fulgidus DATE 24-Jul-1998 #sequence_revision 24-Jul-1998 #text_change 11-Jun-1999 ACCESSIONS B69394 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession B69394 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-222 ##label KLE !'##cross-references GB:AE001024; GB:AE000782; NID:g2689347; !1PIDN:AAB90090.1; PID:g2649433; TIGR:AF1155 COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene AF1155 CLASSIFICATION #superfamily probable phosphoesterase MJ0037; !1phosphoesterase core homology KEYWORDS hydrolase FEATURE !$16-102 #domain phosphoesterase core homology #label PEC SUMMARY #length 222 #molecular-weight 24858 #checksum 7120 SEQUENCE /// ENTRY B71109 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) PHAE027 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 21-Aug-1998 #sequence_revision 21-Aug-1998 #text_change 16-Jun-2000 ACCESSIONS B71109 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession B71109 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-213 ##label KAW !'##cross-references GB:AP000003; NID:g3236130; PIDN:BAA29732.1; !1PID:g3257049 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene PH0641 CLASSIFICATION #superfamily probable phosphoesterase MJ0037; !1phosphoesterase core homology KEYWORDS hydrolase FEATURE !$17-96 #domain phosphoesterase core homology #label PEC SUMMARY #length 213 #molecular-weight 24539 #checksum 5332 SEQUENCE /// ENTRY D75051 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) PAB0926 [similarity] - Pyrococcus abyssi (strain Orsay) ALTERNATE_NAMES exonuclease sbcd related PAB0926 ORGANISM #formal_name Pyrococcus abyssi DATE 03-Aug-2001 #sequence_revision 03-Aug-2001 #text_change 03-Aug-2001 ACCESSIONS D75051 REFERENCE A75001 !$#authors anonymous, Genoscope !$#submission submitted to the EMBL Data Library, July 1999 !$#description Pyrococcus abyssi genome sequence: insights into archaeal !1chromosome structure and evolution. !$#accession D75051 !'##molecule_type DNA !'##residues 1-214 ##label KAW !'##cross-references GB:AJ248287; GB:AL096836; NID:g5458657; !1PIDN:CAB50305.1; PID:g5458818 !'##experimental_source strain Orsay GENETICS !$#gene PAB0926 CLASSIFICATION #superfamily probable phosphoesterase MJ0037; !1phosphoesterase core homology KEYWORDS hydrolase FEATURE !$19-98 #domain phosphoesterase core homology #label PEC SUMMARY #length 214 #molecular-weight 24420 #checksum 8281 SEQUENCE /// ENTRY H69398 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) AF1193 - Archaeoglobus fulgidus ALTERNATE_NAMES MJ0037 homolog ORGANISM #formal_name Archaeoglobus fulgidus DATE 24-Jul-1998 #sequence_revision 24-Jul-1998 #text_change 22-Mar-2002 ACCESSIONS H69398 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession H69398 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-193 ##label KLE !'##cross-references GB:AE001022; GB:AE000782; NID:g2689345; !1PIDN:AAB90052.1; PID:g2649393; TIGR:AF1193 COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. CLASSIFICATION #superfamily probable phosphoesterase MJ0037; !1phosphoesterase core homology KEYWORDS hydrolase FEATURE !$11-81 #domain phosphoesterase core homology #label PEC SUMMARY #length 193 #molecular-weight 21854 #checksum 9273 SEQUENCE /// ENTRY A69108 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) MTH1803 - Methanobacterium thermoautotrophicum (strain Delta H) ALTERNATE_NAMES MJ0037 homolog ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 24-Jul-1998 #sequence_revision 24-Jul-1998 #text_change 11-Jun-1999 ACCESSIONS A69108 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession A69108 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-247 ##label MTH !'##cross-references GB:AE000934; GB:AE000666; NID:g2622924; !1PIDN:AAB86269.1; PID:g2622935 !'##experimental_source strain Delta H COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene MTH1803 CLASSIFICATION #superfamily probable phosphoesterase MJ0037; !1phosphoesterase core homology KEYWORDS hydrolase FEATURE !$21-110 #domain phosphoesterase core homology #label PEC SUMMARY #length 247 #molecular-weight 28332 #checksum 2018 SEQUENCE /// ENTRY G84280 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) yhcR [similarity] - Halobacterium sp. NRC-1 ORGANISM #formal_name Halobacterium sp. NRC-1 DATE 03-Aug-2001 #sequence_revision 03-Aug-2001 #text_change 03-Aug-2001 ACCESSIONS G84280 REFERENCE A84160 !$#authors Ng, W.V.; Kennedy, S.P.; Mahairas, G.G.; Berquist, B.; Pan, !1M.; Shukla, H.D.; Lasky, S.R.; Baliga, N.; Thorsson, V.; !1Sbrogna, J.; Swartzell, S.; Weir, D.; Hall, J.; Dahl, T.A.; !1Welti, R.; Goo, Y.A.; Leithauser, B.; Keller, K.; Cruz, R.; !1Danson, M.J.; Hough, D.W.; Maddocks, D.G.; Jablonski, P.E.; !1Krebs, M.P.; Angevine, C.M.; Dale, H.; Isenbarger, T.A.; !1Peck, R.F.; Pohlschrod, M.; Spudich, J.L.; Jung, K.H.; Alam, !1M.; Freitas, T.; Hou, S.; Daniels, C.J.; Dennis, P.P.; Omer, !1A.D.; Ebhardt, H.; Lowe, T.M.; Liang, P.; Riley, M.; Hood, !1L.; DasSarma, S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (2000) 97:12176-12181 !$#title Genome sequence of Halobacterium species NRC-1. !$#cross-references MUID:20504483; PMID:11016950 !$#accession G84280 !'##molecule_type DNA !'##residues 1-247 ##label STO !'##cross-references GB:AE004437; NID:g10580779; PIDN:AAG19611.1; !1GSPDB:GN00138 GENETICS !$#gene yhcR CLASSIFICATION #superfamily probable phosphoesterase MJ0037; !1phosphoesterase core homology KEYWORDS hydrolase FEATURE !$21-106 #domain phosphoesterase core homology #label PEC SUMMARY #length 247 #molecular-weight 26178 #checksum 4813 SEQUENCE /// ENTRY C90246 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) SSO0952 [similarity] - Sulfolobus solfataricus ORGANISM #formal_name Sulfolobus solfataricus DATE 03-Aug-2001 #sequence_revision 03-Aug-2001 #text_change 03-Aug-2001 ACCESSIONS C90246 REFERENCE A99139 !$#authors She, Q.; Singh, R.K.; Confalonieri, F.; Zivanovic, Y.; !1Allard, G.; Awayez, M.J.; Chan-Weiher, C.C.Y.; Clausen, !1I.G.; Curtis, B.A.; De Moors, A.; Erauso, G.; Fletcher, C.; !1Gordon, P.M.K.; Heikamp-de Jong, I.; Jeffries, A.C.; Kozera, !1C.J.; Medina, N.; Peng, X.; Thi-Ngoc, H.P.; Redder, P.; !1Schenk, M.E.; Theriault, C.; Tolstrup, N.; Charlebois, R.L.; !1Doolittle, W.F.; Duguet, M.; Gaasterland, T.; Garrett, R.A.; !1Ragan, M.A.; Sensen, C.W.; Van der Oost, J. !$#submission submitted to GenBank, April 2001 !$#description Sulfolobus solfataricus complete genome. !$#accession C90246 !'##molecule_type DNA !'##residues 1-251 ##label KUR !'##cross-references GB:AE006641; NID:g13814132; PIDN:AAK41226.1; !1GSPDB:GN00155 GENETICS !$#gene SSO0952 CLASSIFICATION #superfamily probable phosphoesterase MJ0037; !1phosphoesterase core homology KEYWORDS hydrolase FEATURE !$23-112 #domain phosphoesterase core homology #label PEC SUMMARY #length 251 #molecular-weight 28831 #checksum 5442 SEQUENCE /// ENTRY E72572 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) APE1861 [similarity] - Aeropyrum pernix (strain K1) ORGANISM #formal_name Aeropyrum pernix DATE 03-Aug-2001 #sequence_revision 03-Aug-2001 #text_change 03-Aug-2001 ACCESSIONS E72572 REFERENCE A72450 !$#authors Kawarabayasi, Y.; Hino, Y.; Horikawa, H.; Yamazaki, S.; !1Haikawa, Y.; Jin-no, K.; Takahashi, M.; Sekine, M.; Baba, !1S.; Ankai, A.; Kosugi, H.; Hosoyama, A.; Fukui, S.; Nagai, !1Y.; Nishijima, K.; Nakazawa, H.; Takamiya, M.; Masuda, S.; !1Funahashi, T.; Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, !1N.; Oguchi, A.; Aoki, K.; Kubota, K.; Nakamura, Y.; Nomura, !1N.; Sako, Y.; Kikuchi, H. !$#journal DNA Res. (1999) 6:83-101 !$#title Complete genome sequence of an aerobic hyper-thermophilic !1Crenarchaeon, Aeropyrum pernix K1. !$#cross-references MUID:99310339; PMID:10382966 !$#accession E72572 !'##molecule_type DNA !'##residues 1-262 ##label KAW !'##cross-references DDBJ:AP000062; NID:g5105244; PIDN:BAA80866.1; !1PID:d1044652; PID:g5105553 !'##experimental_source strain K1 GENETICS !$#gene APE1861 CLASSIFICATION #superfamily probable phosphoesterase MJ0037; !1phosphoesterase core homology KEYWORDS hydrolase FEATURE !$36-126 #domain phosphoesterase core homology #label PEC SUMMARY #length 262 #molecular-weight 28612 #checksum 5766 SEQUENCE /// ENTRY D87502 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) CC2041 - Caulobacter crescentus ORGANISM #formal_name Caulobacter crescentus DATE 20-Apr-2001 #sequence_revision 20-Apr-2001 #text_change 02-Nov-2001 ACCESSIONS D87502 REFERENCE A87249 !$#authors Nierman, W.C.; Feldblyum, T.V.; Paulsen, I.T.; Nelson, K.E.; !1Eisen, J.; Heidelberg, J.F.; Alley, M.; Ohta, N.; Maddock, !1J.R.; Potocka, I.; Nelson, W.C.; Newton, A.; Stephens, C.; !1Phadke, N.D.; Ely, B.; Laub, M.T.; DeBoy, R.T.; Dodson, !1R.J.; Durkin, A.S.; Gwinn, M.L.; Haft, D.H.; Kolonay, J.F.; !1Smit, J.; Craven, M.; Khouri, H.; Shetty, J.; Berry, K.; !1Utterback, T.; Tran, K.; Wolf, A.; Vamathevan, J.; !1Ermolaeva, M.; White, O.; Salzberg, S.L.; Shapiro, L.; !1Venter, J.C.; Fraser, C.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (2001) 98:4136-4141 !$#title Complete Genome Sequence of Caulobacter crescentus. !$#cross-references MUID:21173698; PMID:11259647 !$#accession D87502 !'##molecule_type DNA !'##residues 1-235 ##label STO !'##cross-references GB:AE005673; NID:g13423518; PIDN:AAK24016.1; !1GSPDB:GN00148 COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene CC2041 CLASSIFICATION #superfamily probable phosphoesterase MJ0037; !1phosphoesterase core homology KEYWORDS hydrolase FEATURE !$35-123 #domain phosphoesterase core homology #label PEC SUMMARY #length 235 #molecular-weight 25339 #checksum 6383 SEQUENCE /// ENTRY C97419 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) AGR_C_876 [similarity] - Agrobacterium tumefaciens (strain C58, Cereon) ORGANISM #formal_name Agrobacterium tumefaciens DATE 30-Sep-2001 #sequence_revision 30-Sep-2001 #text_change 18-Nov-2002 ACCESSIONS C97419 REFERENCE A97359 !$#authors Goodner, B.; Hinkle, G.; Gattung, S.; Miller, N.; Blanchard, !1M.; Qurollo, B.; Goldman, B.S.; Cao, Y.; Askenazi, M.; !1Halling, C.; Mullin, L.; Houmiel, K.; Gordon, J.; Vaudin, !1M.; Iartchouk, O.; Epp, A.; Liu, F.; Wollam, C.; Allinger, !1M.; Doughty, D.; Scott, C.; Lappas, C.; Markelz, B.; !1Flanagan, C.; Crowell, C.; Gurson, J.; Lomo, C.; Sear, C.; !1Strub, G.; Cielo, C.; Slater, S. !$#journal Science (2001) 294:2323-2328 !$#title Genome Sequence of the Plant Pathogen and Biotechnology !1Agent Agrobacterium tumefaciens C58. !$#cross-references MUID:21608551; PMID:11743194 !$#accession C97419 !'##molecule_type DNA !'##residues 1-242 ##label KUR !'##cross-references GB:AE007869; PIDN:AAK86308.1; PID:g15155424; !1GSPDB:GN00169 COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene AGR_C_876 !$#map_position circular chromosome CLASSIFICATION #superfamily probable phosphoesterase MJ0037; !1phosphoesterase core homology KEYWORDS hydrolase FEATURE !$43-130 #domain phosphoesterase core homology #label PEC SUMMARY #length 242 #molecular-weight 26824 #checksum 6166 SEQUENCE /// ENTRY T15613 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) C25E10.12 [similarity] - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 20-Sep-1999 #sequence_revision 20-Sep-1999 #text_change 02-Nov-2001 ACCESSIONS T15613 REFERENCE Z18376 !$#authors Bradshaw, H. !$#submission submitted to the EMBL Data Library, February 1996 !$#description The sequence of C. elegans cosmid C25E10. !$#accession T15613 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-281 ##label BRA !'##cross-references EMBL:U50311; NID:g1226295; PID:g1226307; !1PIDN:AAA92317.1; CESP:C25E10.12 !'##experimental_source strain Bristol N2 COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene CESP:C25E10.12 !$#introns 36/2; 60/3; 94/1; 239/3 CLASSIFICATION #superfamily Caenorhabditis elegans probable phosphoesterase !1C25E10.12; phosphoesterase core homology KEYWORDS hydrolase FEATURE !$47-109 #domain phosphoesterase core homology #label PEC SUMMARY #length 281 #molecular-weight 31787 #checksum 6863 SEQUENCE /// ENTRY T24660 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) T07D4.2 [similarity] - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 02-Nov-2001 ACCESSIONS T24660 REFERENCE Z19919 !$#authors Smye, R. !$#submission submitted to the EMBL Data Library, July 1995 !$#accession T24660 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-342 ##label WIL !'##cross-references EMBL:Z50071; PIDN:CAA90405.1; GSPDB:GN00020; !1CESP:T07D4.2 !'##experimental_source clone T07D4 COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene CESP:T07D4.2 !$#map_position 2 !$#introns 55/3; 168/1; 197/3; 209/3; 248/1; 309/3 CLASSIFICATION #superfamily Caenorhabditis elegans probable phosphoesterase !1C25E10.12; phosphoesterase core homology KEYWORDS hydrolase FEATURE !$96-157 #domain phosphoesterase core homology #label PEC SUMMARY #length 342 #molecular-weight 38674 #checksum 14 SEQUENCE /// ENTRY A89124 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) K07C11.7 [similarity] - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 10-May-2001 #sequence_revision 10-May-2001 #text_change 02-Nov-2001 ACCESSIONS A89124 REFERENCE A75000 !$#authors anonymous, The C. elegans Sequencing Consortium. !$#journal Science (1998) 282:2012-2018 !$#title Genome sequence of the nematode C. elegans: a platform for !1investigating biology. !$#cross-references MUID:99069613; PMID:9851916 !$#note see websites genome.wustl.edu/gsc/C_elegans/ and !1www_sanger.ac.uk/Projects/C_elegans/ for a list of authors !$#note published errata appeared in Science 283, 35, 1999; Science !1283, 2103, 1999; and Science 285, 1493, 1999 !$#accession A89124 !'##molecule_type DNA !'##residues 1-271 ##label STO !'##cross-references GB:chr_V; PIDN:AAA96177.1; PID:g1255827; !1GSPDB:GN00023; CESP:K07C11.7 COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene K07C11.7 !$#map_position 5 CLASSIFICATION #superfamily Caenorhabditis elegans probable phosphoesterase !1C25E10.12; phosphoesterase core homology KEYWORDS hydrolase FEATURE !$68-128 #domain phosphoesterase core homology #label PEC SUMMARY #length 271 #molecular-weight 30917 #checksum 3202 SEQUENCE /// ENTRY D64650 #type complete TITLE probable membrane-bound phosphoesterase (EC 3.1.-.-) HP1044 - Helicobacter pylori (strain 26695) ALTERNATE_NAMES conserved hypothetical integral membrane protein HP1044 ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS D64650 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession D64650 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-370 ##label TOM !'##cross-references GB:AE000612; GB:AE000511; NID:g2314188; !1PIDN:AAD08089.1; PID:g2314191; TIGR:HP1044 COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. CLASSIFICATION #superfamily probable membrane-bound phosphoesterase HP1044; !1phosphoesterase core homology KEYWORDS hydrolase; transmembrane protein FEATURE !$146-217 #domain phosphoesterase core homology #label PEC SUMMARY #length 370 #molecular-weight 42456 #checksum 9569 SEQUENCE /// ENTRY B71937 #type complete TITLE probable membrane-bound phosphoesterase (EC 3.1.-.-) jhp0380 - Helicobacter pylori (strain J99) ORGANISM #formal_name Helicobacter pylori #variety strain J99 DATE 12-Feb-1999 #sequence_revision 12-Feb-1999 #text_change 24-Aug-2001 ACCESSIONS B71937 REFERENCE A71800 !$#authors Alm, R.A.; Ling, L.S.L.; Moir, D.T.; King, B.L.; Brown, !1E.D.; Doig, P.C.; Smith, D.R.; Noonan, B.; Guild, B.C.; !1deJonge, B.L.; Carmel, G.; Tummino, P.J.; Caruso, A.; !1Uria-Nickelsen, M.; Mills, D.M.; Ives, C.; Gibson, R.; !1Merberg, D.; Mills, S.D.; Jiang, Q.; Taylor, D.E.; Vovis, !1G.F.; Trust, T.J. !$#journal Nature (1999) 397:176-180 !$#title Genomic sequence comparison of two unrelated isolates of the !1human gastric pathogen Helicobacter pylori. !$#cross-references MUID:99120557; PMID:9923682 !$#accession B71937 !'##molecule_type DNA !'##residues 1-370 ##label ARN !'##cross-references GB:AE001473; GB:AE001439; NID:g4154910; !1PIDN:AAD05967.1; PID:g4154919 !'##experimental_source strain J99 COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene jhp0380 CLASSIFICATION #superfamily probable membrane-bound phosphoesterase HP1044; !1phosphoesterase core homology KEYWORDS hydrolase; transmembrane protein FEATURE !$146-217 #domain phosphoesterase core homology #label PEC SUMMARY #length 370 #molecular-weight 42169 #checksum 51 SEQUENCE /// ENTRY B69024 #type complete TITLE probable membrane-bound phosphoesterase (EC 3.1.-.-) MTH1179 - Methanobacterium thermoautotrophicum (strain Delta H) ALTERNATE_NAMES conserved hypothetical protein MTH1179 ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B69024 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession B69024 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-344 ##label MTH !'##cross-references GB:AE000886; GB:AE000666; NID:g2622276; !1PIDN:AAB85668.1; PID:g2622286 !'##experimental_source strain Delta H COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene MTH1179 CLASSIFICATION #superfamily probable membrane-bound phosphoesterase HP1044; !1phosphoesterase core homology KEYWORDS hydrolase; transmembrane protein FEATURE !$131-196 #domain phosphoesterase core homology #label PEC SUMMARY #length 344 #molecular-weight 38387 #checksum 4646 SEQUENCE /// ENTRY T25203 #type complete TITLE probable membrane-bound phosphoesterase (EC 3.1.-.-) T23G7.2 - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 24-Aug-2001 ACCESSIONS T25203 REFERENCE Z19995 !$#authors Barlow, K. !$#submission submitted to the EMBL Data Library, December 1995 !$#accession T25203 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-454 ##label WIL !'##cross-references EMBL:Z68319; PIDN:CAA92700.1; GSPDB:GN00020; !1CESP:T23G7.2 !'##experimental_source clone T23G7 COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene CESP:T23G7.2 !$#map_position 2 !$#introns 33/3; 55/3; 89/3; 120/3; 155/3; 185/2; 280/2; 320/2 CLASSIFICATION #superfamily probable membrane-bound phosphoesterase HP1044; !1phosphoesterase core homology KEYWORDS hydrolase; transmembrane protein FEATURE !$225-296 #domain phosphoesterase core homology #label PEC SUMMARY #length 454 #molecular-weight 52071 #checksum 416 SEQUENCE /// ENTRY T16303 #type complete TITLE probable membrane-bound phosphoesterase (EC 3.1.-.-) F40B5.2 [similarity] - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 20-Sep-1999 #sequence_revision 20-Sep-1999 #text_change 22-Oct-2001 ACCESSIONS T16303 REFERENCE Z18492 !$#authors Geisel, C. !$#submission submitted to the EMBL Data Library, March 1995 !$#description The sequence of C. elegans cosmid F40B5. !$#accession T16303 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-614 ##label GEI !'##cross-references EMBL:U23182; NID:g726441; PID:g726443; !1PIDN:AAA64337.1; CESP:F40B5.2 !'##experimental_source strain Bristol N2 COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene CESP:F40B5.2 !$#introns 13/3; 77/2; 104/2; 150/1; 198/2; 240/3; 281/1; 318/1; 340/3; !1442/2; 469/2; 521/3; 541/3; 565/3; 586/3 CLASSIFICATION #superfamily probable membrane-bound phosphoesterase !1F40B5.2; phosphoesterase core homology KEYWORDS hydrolase; transmembrane protein FEATURE !$19-35 #domain transmembrane #status predicted #label TM1\ !$133-149 #domain transmembrane #status predicted #label TM2\ !$155-188 #domain transmembrane #status predicted #label TM3\ !$208-224 #domain transmembrane #status predicted #label TM4\ !$250-321 #domain phosphoesterase core homology #label PEC SUMMARY #length 614 #molecular-weight 68990 #checksum 6801 SEQUENCE /// ENTRY D64740 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) yaeI - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS D64740 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64740 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-247 ##label BLAT !'##cross-references GB:AE000126; GB:U00096; NID:g1786358; !1PIDN:AAC73275.1; PID:g1786360; UWGP:b0164 !'##experimental_source strain K-12, substrain MG1655 COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene yaeI !$#map_position 3.97 CLASSIFICATION #superfamily probable phosphoesterase yaeI; phosphoesterase !1core homology KEYWORDS hydrolase FEATURE !$27-99 #domain phosphoesterase core homology #label PEC SUMMARY #length 247 #molecular-weight 27375 #checksum 3218 SEQUENCE /// ENTRY B69865 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) ykuE - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS B69865 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69865 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-287 ##label KUN !'##cross-references GB:Z99111; GB:AL009126; NID:g2633699; !1PIDN:CAB13278.1; PID:g2633776 !'##experimental_source strain 168 COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene ykuE CLASSIFICATION #superfamily probable phosphoesterase yaeI; phosphoesterase !1core homology KEYWORDS hydrolase FEATURE !$59-132 #domain phosphoesterase core homology #label PEC SUMMARY #length 287 #molecular-weight 31759 #checksum 1055 SEQUENCE /// ENTRY D69860 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) ykoQ - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS D69860 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D69860 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-270 ##label KUN !'##cross-references GB:Z99110; GB:Z99111; GB:AL009126; NID:g2633699; !1PIDN:CAB13210.1; PID:g2633708; NID:g2633472; PID:g2633691 !'##experimental_source strain 168 COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene ykoQ CLASSIFICATION #superfamily probable phosphoesterase yaeI; phosphoesterase !1core homology KEYWORDS hydrolase FEATURE !$47-118 #domain phosphoesterase core homology #label PEC SUMMARY #length 270 #molecular-weight 30876 #checksum 3988 SEQUENCE /// ENTRY F70390 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) aq_1054 - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS F70390 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession F70390 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-261 ##label AQF !'##cross-references GB:AE000720; NID:g2983529; PIDN:AAC07116.1; !1PID:g2983541; GB:AE000657 !'##experimental_source strain VF5 COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene aq_1054 CLASSIFICATION #superfamily probable phosphoesterase yaeI; phosphoesterase !1core homology KEYWORDS hydrolase FEATURE !$37-108 #domain phosphoesterase core homology #label PEC SUMMARY #length 261 #molecular-weight 29310 #checksum 5707 SEQUENCE /// ENTRY B69933 #type complete TITLE phosphoesterase-related protein ypbG [similarity] - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 11-Jan-2002 ACCESSIONS B69933 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69933 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-259 ##label KUN !'##cross-references GB:Z99115; GB:Z99116; GB:AL009126; NID:g2634723; !1PIDN:CAB14230.1; PID:g2634733; NID:g2634478; PID:g2634716 !'##experimental_source strain 168 COMMENT Although this sequence has motifs characteristic of a !1variety of phosphoesterases, a critical active site residue !1is not conserved. GENETICS !$#gene ypbG CLASSIFICATION #superfamily probable phosphoesterase yaeI; phosphoesterase !1core homology FEATURE !$48-114 #domain phosphoesterase core homology #label PEC SUMMARY #length 259 #molecular-weight 28560 #checksum 3614 SEQUENCE /// ENTRY B83852 #type complete TITLE phosphoesterase-related protein BH1618 [similarity] - Bacillus halodurans (strain C-125) ORGANISM #formal_name Bacillus halodurans DATE 01-Dec-2000 #sequence_revision 01-Dec-2000 #text_change 11-Jan-2002 ACCESSIONS B83852 REFERENCE A83650 !$#authors Takami, H.; Nakasone, K.; Takaki, Y.; Maeno, G.; Sasaki, R.; !1Masui, N.; Fuji, F.; Hirama, C.; Nakamura, Y.; Ogasawara, !1N.; Kuhara, S.; Horikoshi, K. !$#journal Nucleic Acids Res. (2000) 28:4317-4331 !$#title Complete genome sequence of the alkaliphilic bacterium !1Bacillus halodurans and genomic sequence comparison with !1Bacillus subtilis. !$#cross-references MUID:20512582; PMID:11058132 !$#accession B83852 !'##molecule_type DNA !'##residues 1-256 ##label STO !'##cross-references GB:AP001512; GB:BA000004; NID:g10174030; !1PIDN:BAB05337.1; GSPDB:GN00137 !'##experimental_source strain C-125 COMMENT Although this sequence has motifs characteristic of a !1variety of phosphoesterases, a critical active site residue !1is not conserved. GENETICS !$#gene BH1618 CLASSIFICATION #superfamily probable phosphoesterase yaeI; phosphoesterase !1core homology SUMMARY #length 256 #molecular-weight 28815 #checksum 3276 SEQUENCE /// ENTRY D70791 #type complete TITLE phosphoesterase-related protein Rv3683 [similarity] - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 03-Aug-2001 #sequence_revision 03-Aug-2001 #text_change 11-Jan-2002 ACCESSIONS D70791 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession D70791 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-319 ##label COL !'##cross-references GB:AL022121; GB:AL123456; NID:g3261559; !1PIDN:CAA18005.1; PID:g2960107 !'##experimental_source strain H37Rv COMMENT Although this sequence has motifs characteristic of a !1variety of phosphoesterases, a critical active site residue !1is not conserved. GENETICS !$#gene Rv3683 CLASSIFICATION #superfamily probable phosphoesterase yaeI; phosphoesterase !1core homology FEATURE !$52-119 #domain phosphoesterase core homology #label PEC SUMMARY #length 319 #molecular-weight 34394 #checksum 9420 SEQUENCE /// ENTRY A87198 #type complete TITLE phosphoesterase-related protein Rv3683 [similarity] - Mycobacterium leprae ORGANISM #formal_name Mycobacterium leprae DATE 20-Apr-2001 #sequence_revision 20-Apr-2001 #text_change 11-Jan-2002 ACCESSIONS A87198 REFERENCE A86909 !$#authors Cole, S.T.; Eiglmeier, K.; Parkhill, J.; James, K.D.; !1Thomson, N.R.; Wheeler, P.R.; Honore, N.; Ganier, T.; !1Churcher, C.; Harris, D.; Mungall, K.; Basham, D.; Brown, !1D.; Chillingworth, T.; Connor, R.; Davies, R.M.; Devlin, K.; !1Duthoy, S.; Feltwell, T.; Fraser, A.; Hamlin, N.; Holroyd, !1S.; Hornsby, T.; Jagels, K.; Lacroix, C.; Maclean, J.; !1Moule, S.; Murphy, L.; Oliver, K.; Quail, M.A.; Rajandream, !1M.A.; Rutherford, K.M.; Rutter, S.; Seeger, K.; Simon, S.; !1Simmonds, M.; Skelton, J.; Squares, R.; Squares, S.; !1Stevens, K.; Taylor, K.; Whitehead, S.; Woodward, J.R.; !1Barrell, B.G. !$#journal Nature (2001) 409:1007-1011 !$#title Massive gene decay in the leprosy bacillus. !$#cross-references MUID:21128732; PMID:11234002 !$#accession A87198 !'##molecule_type DNA !'##residues 1-330 ##label STO !'##cross-references GB:AL450380; NID:g13093934; PIDN:CAC31825.1; !1GSPDB:GN00147 COMMENT Although this sequence has motifs characteristic of a !1variety of phosphoesterases, a critical active site residue !1is not conserved. GENETICS !$#gene ML2309 CLASSIFICATION #superfamily probable phosphoesterase yaeI; phosphoesterase !1core homology FEATURE !$45-112 #domain phosphoesterase core homology #label PEC SUMMARY #length 330 #molecular-weight 36198 #checksum 6953 SEQUENCE /// ENTRY T36691 #type complete TITLE phosphoesterase-related protein SCH66.03 [similarity] - Streptomyces coelicolor ORGANISM #formal_name Streptomyces coelicolor DATE 03-Aug-2001 #sequence_revision 03-Aug-2001 #text_change 11-Jan-2002 ACCESSIONS T36691 REFERENCE Z21597 !$#authors Murphy, L.; Harris, D.; Bentley, S.D.; Parkhill, J.; !1Barrell, B.G.; Rajandream, M.A. !$#submission submitted to the EMBL Data Library, April 1999 !$#accession T36691 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-309 ##label MUR !'##cross-references EMBL:AL049731; PIDN:CAB41730.1; GSPDB:GN00070; !1SCOEDB:SCH66.03 !'##experimental_source strain A3(2) COMMENT Although this sequence has motifs characteristic of a !1variety of phosphoesterases, a critical active site residue !1is not conserved. GENETICS !$#gene SCOEDB:SCH66.03 CLASSIFICATION #superfamily probable phosphoesterase yaeI; phosphoesterase !1core homology FEATURE !$48-115 #domain phosphoesterase core homology #label PEC SUMMARY #length 309 #molecular-weight 33442 #checksum 4023 SEQUENCE /// ENTRY H75285 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) DR2345 [similarity] - Deinococcus radiodurans (strain R1) ORGANISM #formal_name Deinococcus radiodurans DATE 03-Aug-2001 #sequence_revision 03-Aug-2001 #text_change 03-Aug-2001 ACCESSIONS H75285 REFERENCE A75250 !$#authors White, O.; Eisen, J.A.; Heidelberg, J.F.; Hickey, E.K.; !1Peterson, J.D.; Dodson, R.J.; Haft, D.H.; Gwinn, M.L.; !1Nelson, W.C.; Richardson, D.L.; Moffat, K.S.; Qin, H.; !1Jiang, L.; Pamphile, W.; Crosby, M.; Shen, M.; Vamathevan, !1J.J.; Lam, P.; McDonald, L.; Utterback, T.; Zalewski, C.; !1Makarova, K.S.; Aravind, L.; Daly, M.J.; Minton, K.W.; !1Fleischmann, R.D.; Ketchum, K.A.; Nelson, K.E.; Salzberg, !1S.; Smith, H.O.; Venter, J.C.; Fraser, C.M. !$#journal Science (1999) 286:1571-1577 !$#title Genome sequence of the radioresistant bacterium Deinococcus !1radiodurans R1. !$#cross-references MUID:20036896; PMID:10567266 !$#accession H75285 !'##molecule_type DNA !'##residues 1-305 ##label WHI !'##cross-references GB:AE002065; GB:AE000513; NID:g6460149; !1PIDN:AAF11890.1; PID:g6460156; TIGR:DR2345; GSPDB:GN00077 !'##experimental_source strain R1 COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene DR2345 !$#map_position 1 CLASSIFICATION #superfamily probable phosphoesterase yaeI; phosphoesterase !1core homology KEYWORDS hydrolase FEATURE !$62-139 #domain phosphoesterase core homology #label PEC SUMMARY #length 305 #molecular-weight 32238 #checksum 2778 SEQUENCE /// ENTRY A71511 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) yaeI [similarity] - Chlamydia trachomatis (serotype D, strain UW3/Cx) ORGANISM #formal_name Chlamydia trachomatis DATE 03-Aug-2001 #sequence_revision 03-Aug-2001 #text_change 03-Aug-2001 ACCESSIONS A71511 REFERENCE A71570 !$#authors Stephens, R.S.; Kalman, S.; Lammel, C.J.; Fan, J.; Marathe, !1R.; Aravind, L.; Mitchell, W.P.; Olinger, L.; Tatusov, R.L.; !1Zhao, Q.; Koonin, E.V.; Davis, R.W. !$#journal Science (1998) 282:754-759 !$#title Genome sequence of an obligate intracellular pathogen of !1humans: Chlamydia trachomatis. !$#cross-references MUID:99000809; PMID:9784136 !$#accession A71511 !'##molecule_type DNA !'##residues 1-329 ##label ARN !'##cross-references GB:AE001320; GB:AE001273; NID:g3328891; !1PIDN:AAC68061.1; PID:g3328895 !'##experimental_source serotype D, strain UW-3/Cx COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene yaeI CLASSIFICATION #superfamily probable phosphoesterase yaeI; phosphoesterase !1core homology KEYWORDS hydrolase FEATURE !$53-125 #domain phosphoesterase core homology #label PEC SUMMARY #length 329 #molecular-weight 36954 #checksum 6258 SEQUENCE /// ENTRY B81669 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) TC0746 [similarity] - Chlamydia muridarum (strain Nigg) ORGANISM #formal_name Chlamydia muridarum, Chlamydia trachomatis MoPn DATE 03-Aug-2001 #sequence_revision 03-Aug-2001 #text_change 03-Aug-2001 ACCESSIONS B81669 REFERENCE A81500 !$#authors Read, T.D.; Brunham, R.C.; Shen, C.; Gill, S.R.; Heidelberg, !1J.F.; White, O.; Hickey, E.K.; Peterson, J.; Utterback, T.; !1Berry, K.; Bass, S.; Linher, K.; Weidman, J.; Khouri, H.; !1Craven, B.; Bowman, C.; Dodson, R.; Gwinn, M.; Nelson, W.; !1DeBoy, R.; Kolonay, J.; McClarty, G.; Salzberg, S.L.; Eisen, !1J.; Fraser, C.M. !$#journal Nucleic Acids Res. (2000) 28:1397-1406 !$#title Genome sequences of Chlamydia trachomatis MoPn and Chlamydia !1pneumoniae AR39. !$#cross-references MUID:20150255; PMID:10684935 !$#accession B81669 !'##molecule_type DNA !'##residues 1-329 ##label TET !'##cross-references GB:AE002343; GB:AE002160; NID:g7190772; !1PIDN:AAF39553.1; PID:g7190774; GSPDB:GN00121; TIGR:TC0746 !'##experimental_source strain Nigg (MoPn) COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene TC0746 CLASSIFICATION #superfamily probable phosphoesterase yaeI; phosphoesterase !1core homology KEYWORDS hydrolase FEATURE !$53-125 #domain phosphoesterase core homology #label PEC SUMMARY #length 329 #molecular-weight 37108 #checksum 7736 SEQUENCE /// ENTRY G72061 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) yaeI [similarity] - Chlamydophila pneumoniae (strain CWL029) ORGANISM #formal_name Chlamydophila pneumoniae, Chlamydia pneumoniae DATE 03-Aug-2001 #sequence_revision 03-Aug-2001 #text_change 03-Aug-2001 ACCESSIONS G72061 REFERENCE A72000 !$#authors Kalman, S.; Mitchell, W.; Marathe, R.; Lammel, C.; Fan, J.; !1Olinger, L.; Grimwood, J.; Davis, R.W.; Stephens, R.S. !$#journal Nature Genet. (1999) 21:385-389 !$#title Comparative genomes of Clamydia pneumoniae and C. !1trachomatis. !$#cross-references MUID:99206606; PMID:10192388 !$#accession G72061 !'##molecule_type DNA !'##residues 1-320 ##label ARN !'##cross-references GB:AE001642; GB:AE001363; NID:g4376865; !1PIDN:AAD18717.1; PID:g4376871 !'##experimental_source strain CWL029 COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene yaeI CLASSIFICATION #superfamily probable phosphoesterase yaeI; phosphoesterase !1core homology KEYWORDS hydrolase FEATURE !$46-118 #domain phosphoesterase core homology #label PEC SUMMARY #length 320 #molecular-weight 36412 #checksum 7210 SEQUENCE /// ENTRY G86562 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) yaeI [similarity] - Chlamydophila pneumoniae (strain J138) ORGANISM #formal_name Chlamydophila pneumoniae, Chlamydia pneumoniae DATE 03-Aug-2001 #sequence_revision 03-Aug-2001 #text_change 03-Aug-2001 ACCESSIONS G86562 REFERENCE A86491 !$#authors Shirai, M.; Hirakawa, H.; Kimoto, M.; Tabuchi, M.; Kishi, !1F.; Ouchi, K.; Shiba, T.; Ishii, K.; Hattori, M.; Kuhara, !1S.; Nakazawa, T. !$#journal Nucleic Acids Res. (2000) 28:2311-2314 !$#title Comparison of whole genome sequences of chlamydia pneumoniae !1J138. !$#cross-references MUID:20330349; PMID:10871362 !$#accession G86562 !'##molecule_type DNA !'##residues 1-320 ##label STO !'##cross-references GB:BA000008; NID:g8978950; PIDN:BAA98785.1; !1GSPDB:GN00142 !'##experimental_source strain J138 COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene yaeI CLASSIFICATION #superfamily probable phosphoesterase yaeI; phosphoesterase !1core homology KEYWORDS hydrolase FEATURE !$46-118 #domain phosphoesterase core homology #label PEC SUMMARY #length 320 #molecular-weight 36412 #checksum 7210 SEQUENCE /// ENTRY D86898 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) ywhB [similarity] - Lactococcus lactis subsp. lactis (strain IL1403) ORGANISM #formal_name Lactococcus lactis subsp. lactis DATE 03-Aug-2001 #sequence_revision 03-Aug-2001 #text_change 03-Aug-2001 ACCESSIONS D86898 REFERENCE A86625 !$#authors Bolotin, A.; Wincker, P.; Mauger, S.; Jaillon, O.; Malarme, !1K.; Weissenbach, J.; Ehrlich, S.D.; Sorokin, A. !$#journal Genome Res. (2001) 11:731-753 !$#title The complete genome sequence of the lactic acid bacterium !1Lactococcus lactis ssp. lactis IL1403. !$#cross-references MUID:21235186; PMID:11337471 !$#accession D86898 !'##molecule_type DNA !'##residues 1-257 ##label STO !'##cross-references GB:AE005176; PID:g12725252; PIDN:AAK06286.1; !1GSPDB:GN00146 !'##experimental_source strain IL1403 COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene ywhB CLASSIFICATION #superfamily probable phosphoesterase yaeI; phosphoesterase !1core homology KEYWORDS hydrolase FEATURE !$39-114 #domain phosphoesterase core homology #label PEC SUMMARY #length 257 #molecular-weight 29384 #checksum 3446 SEQUENCE /// ENTRY F71508 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) CT488 [similarity] - Chlamydia trachomatis (serotype D, strain UW3/Cx) ORGANISM #formal_name Chlamydia trachomatis DATE 03-Aug-2001 #sequence_revision 03-Aug-2001 #text_change 03-Aug-2001 ACCESSIONS F71508 REFERENCE A71570 !$#authors Stephens, R.S.; Kalman, S.; Lammel, C.J.; Fan, J.; Marathe, !1R.; Aravind, L.; Mitchell, W.P.; Olinger, L.; Tatusov, R.L.; !1Zhao, Q.; Koonin, E.V.; Davis, R.W. !$#journal Science (1998) 282:754-759 !$#title Genome sequence of an obligate intracellular pathogen of !1humans: Chlamydia trachomatis. !$#cross-references MUID:99000809; PMID:9784136 !$#accession F71508 !'##molecule_type DNA !'##residues 1-244 ##label ARN !'##cross-references GB:AE001322; GB:AE001273; NID:g3328916; !1PIDN:AAC68088.1; PID:g3328924 !'##experimental_source serotype D, strain UW-3/Cx COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene CT488 CLASSIFICATION #superfamily Chlamydia trachomatis probable phosphoesterase !1CT488; phosphoesterase core homology KEYWORDS hydrolase FEATURE !$2-85 #domain phosphoesterase core homology #label PEC SUMMARY #length 244 #molecular-weight 27694 #checksum 6469 SEQUENCE /// ENTRY E81667 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) TC0775 [similarity] - Chlamydia muridarum (strain Nigg) ORGANISM #formal_name Chlamydia muridarum, Chlamydia trachomatis MoPn DATE 03-Aug-2001 #sequence_revision 03-Aug-2001 #text_change 03-Aug-2001 ACCESSIONS E81667 REFERENCE A81500 !$#authors Read, T.D.; Brunham, R.C.; Shen, C.; Gill, S.R.; Heidelberg, !1J.F.; White, O.; Hickey, E.K.; Peterson, J.; Utterback, T.; !1Berry, K.; Bass, S.; Linher, K.; Weidman, J.; Khouri, H.; !1Craven, B.; Bowman, C.; Dodson, R.; Gwinn, M.; Nelson, W.; !1DeBoy, R.; Kolonay, J.; McClarty, G.; Salzberg, S.L.; Eisen, !1J.; Fraser, C.M. !$#journal Nucleic Acids Res. (2000) 28:1397-1406 !$#title Genome sequences of Chlamydia trachomatis MoPn and Chlamydia !1pneumoniae AR39. !$#cross-references MUID:20150255; PMID:10684935 !$#accession E81667 !'##molecule_type DNA !'##residues 1-247 ##label TET !'##cross-references GB:AE002345; GB:AE002160; NID:g7190791; !1PIDN:AAF39578.1; PID:g7190801; GSPDB:GN00121; TIGR:TC0775 !'##experimental_source strain Nigg (MoPn) COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene TC0775 CLASSIFICATION #superfamily Chlamydia trachomatis probable phosphoesterase !1CT488; phosphoesterase core homology KEYWORDS hydrolase FEATURE !$4-87 #domain phosphoesterase core homology #label PEC SUMMARY #length 247 #molecular-weight 28110 #checksum 7485 SEQUENCE /// ENTRY C86566 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) CPj0606 [similarity] - Chlamydophila pneumoniae (strain J138) ORGANISM #formal_name Chlamydophila pneumoniae, Chlamydia pneumoniae DATE 03-Aug-2001 #sequence_revision 03-Aug-2001 #text_change 03-Aug-2001 ACCESSIONS C86566 REFERENCE A86491 !$#authors Shirai, M.; Hirakawa, H.; Kimoto, M.; Tabuchi, M.; Kishi, !1F.; Ouchi, K.; Shiba, T.; Ishii, K.; Hattori, M.; Kuhara, !1S.; Nakazawa, T. !$#journal Nucleic Acids Res. (2000) 28:2311-2314 !$#title Comparison of whole genome sequences of chlamydia pneumoniae !1J138. !$#cross-references MUID:20330349; PMID:10871362 !$#accession C86566 !'##molecule_type DNA !'##residues 1-246 ##label STO !'##cross-references GB:BA000008; NID:g8978978; PIDN:BAA98813.1; !1GSPDB:GN00142 !'##experimental_source strain J138 COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene CPj0606 CLASSIFICATION #superfamily Chlamydia trachomatis probable phosphoesterase !1CT488; phosphoesterase core homology KEYWORDS hydrolase FEATURE !$2-85 #domain phosphoesterase core homology #label PEC SUMMARY #length 246 #molecular-weight 27619 #checksum 5760 SEQUENCE /// ENTRY H72057 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) CP0141 [similarity] - Chlamydophila pneumoniae (strains CWL029 and AR39) ALTERNATE_NAMES ct488 hypothetical protein ORGANISM #formal_name Chlamydophila pneumoniae, Chlamydia pneumoniae DATE 03-Aug-2001 #sequence_revision 03-Aug-2001 #text_change 03-Aug-2001 ACCESSIONS H72057; C81609 REFERENCE A72000 !$#authors Kalman, S.; Mitchell, W.; Marathe, R.; Lammel, C.; Fan, J.; !1Olinger, L.; Grimwood, J.; Davis, R.W.; Stephens, R.S. !$#journal Nature Genet. (1999) 21:385-389 !$#title Comparative genomes of Clamydia pneumoniae and C. !1trachomatis. !$#cross-references MUID:99206606; PMID:10192388 !$#accession H72057 !'##molecule_type DNA !'##residues 1-246 ##label ARN !'##cross-references GB:AE001645; GB:AE001363; NID:g4376896; !1PIDN:AAD18745.1; PID:g4376902 !'##experimental_source strain CWL029 REFERENCE A81500 !$#authors Read, T.D.; Brunham, R.C.; Shen, C.; Gill, S.R.; Heidelberg, !1J.F.; White, O.; Hickey, E.K.; Peterson, J.; Utterback, T.; !1Berry, K.; Bass, S.; Linher, K.; Weidman, J.; Khouri, H.; !1Craven, B.; Bowman, C.; Dodson, R.; Gwinn, M.; Nelson, W.; !1DeBoy, R.; Kolonay, J.; McClarty, G.; Salzberg, S.L.; Eisen, !1J.; Fraser, C.M. !$#journal Nucleic Acids Res. (2000) 28:1397-1406 !$#title Genome sequences of Chlamydia trachomatis MoPn and Chlamydia !1pneumoniae AR39. !$#cross-references MUID:20150255; PMID:10684935 !$#accession C81609 !'##molecule_type DNA !'##residues 1-246 ##label REA !'##cross-references GB:AE002175; GB:AE002161; NID:g7189069; !1PIDN:AAF38023.1; PID:g7189076; GSPDB:GN00122; TIGR:CP0141 !'##experimental_source strain AR39, HL cells COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene CPn0606; CP0141 CLASSIFICATION #superfamily Chlamydia trachomatis probable phosphoesterase !1CT488; phosphoesterase core homology KEYWORDS hydrolase FEATURE !$2-85 #domain phosphoesterase core homology #label PEC SUMMARY #length 246 #molecular-weight 27619 #checksum 5760 SEQUENCE /// ENTRY F75433 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) DR1119 [similarity] - Deinococcus radiodurans (strain R1) ORGANISM #formal_name Deinococcus radiodurans DATE 03-Aug-2001 #sequence_revision 03-Aug-2001 #text_change 03-Aug-2001 ACCESSIONS F75433 REFERENCE A75250 !$#authors White, O.; Eisen, J.A.; Heidelberg, J.F.; Hickey, E.K.; !1Peterson, J.D.; Dodson, R.J.; Haft, D.H.; Gwinn, M.L.; !1Nelson, W.C.; Richardson, D.L.; Moffat, K.S.; Qin, H.; !1Jiang, L.; Pamphile, W.; Crosby, M.; Shen, M.; Vamathevan, !1J.J.; Lam, P.; McDonald, L.; Utterback, T.; Zalewski, C.; !1Makarova, K.S.; Aravind, L.; Daly, M.J.; Minton, K.W.; !1Fleischmann, R.D.; Ketchum, K.A.; Nelson, K.E.; Salzberg, !1S.; Smith, H.O.; Venter, J.C.; Fraser, C.M. !$#journal Science (1999) 286:1571-1577 !$#title Genome sequence of the radioresistant bacterium Deinococcus !1radiodurans R1. !$#cross-references MUID:20036896; PMID:10567266 !$#accession F75433 !'##molecule_type DNA !'##residues 1-242 ##label WHI !'##cross-references GB:AE001962; GB:AE000513; NID:g6458855; !1PIDN:AAF10693.1; PID:g6458856; TIGR:DR1119; GSPDB:GN00077 !'##experimental_source strain R1 COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene DR1119 !$#map_position 1 CLASSIFICATION #superfamily Chlamydia trachomatis probable phosphoesterase !1CT488; phosphoesterase core homology KEYWORDS hydrolase FEATURE !$2-84 #domain phosphoesterase core homology #label PEC SUMMARY #length 242 #molecular-weight 26694 #checksum 2987 SEQUENCE /// ENTRY B64465 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) MJ1323 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B64465 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession B64465 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-366 ##label BUL !'##cross-references GB:U67572; GB:L77117; NID:g1591958; !1PIDN:AAB99332.1; PID:g1591963; TIGR:MJ1323 COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#map_position REV1274491-1273391 CLASSIFICATION #superfamily probable phosphoesterase MJ1323; !1phosphoesterase core homology KEYWORDS hydrolase FEATURE !$2-86 #domain phosphoesterase core homology #label PEC SUMMARY #length 366 #molecular-weight 43131 #checksum 2263 SEQUENCE /// ENTRY G69378 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) AF1031 - Archaeoglobus fulgidus ALTERNATE_NAMES DNA repair protein RAD32 homolog ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS G69378 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession G69378 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-443 ##label KLE !'##cross-references GB:AE001032; GB:AE000782; NID:g2689355; !1PIDN:AAB90212.1; PID:g2649563; TIGR:AF1031 COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. CLASSIFICATION #superfamily probable phosphoesterase MJ1323; !1phosphoesterase core homology KEYWORDS hydrolase FEATURE !$2-86 #domain phosphoesterase core homology #label PEC SUMMARY #length 443 #molecular-weight 51178 #checksum 9412 SEQUENCE /// ENTRY D71083 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) PHAR032 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 21-Aug-1998 #sequence_revision 21-Aug-1998 #text_change 16-Jun-2000 ACCESSIONS D71083 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession D71083 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-413 ##label KAW !'##cross-references GB:AP000004; NID:g3236131; PIDN:BAA30026.1; !1PID:g3257343 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene PH0930 CLASSIFICATION #superfamily probable phosphoesterase MJ1323; !1phosphoesterase core homology KEYWORDS hydrolase FEATURE !$2-86 #domain phosphoesterase core homology #label PEC SUMMARY #length 413 #molecular-weight 48042 #checksum 7427 SEQUENCE /// ENTRY E69171 #type complete TITLE phosphoesterase-related protein MTH541 [similarity] - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 05-Dec-1997 #sequence_revision 05-Dec-1997 #text_change 11-Jan-2002 ACCESSIONS E69171 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession E69171 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-587 ##label MTH !'##cross-references GB:AE000837; GB:AE000666; NID:g2621613; !1PIDN:AAB85047.1; PID:g2621616 !'##experimental_source strain Delta H COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases; however, the active site motif GNH[DE] is !1GSHD in this sequence. Except for a predicted amino-terminal !1extension of about 170 residues, this protein is homologous !1with MJ1323 and its relatives. GENETICS !$#gene MTH541 !$#start_codon GTG CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum !1phosphoesterase-related protein MTH541; phosphoesterase core !1homology FEATURE !$172-254 #domain phosphoesterase core homology #label PEC SUMMARY #length 587 #molecular-weight 65997 #checksum 1013 SEQUENCE /// ENTRY PAECA #type complete TITLE alkaline phosphatase (EC 3.1.3.1) precursor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 01-Sep-1981 #sequence_revision 15-Oct-1982 #text_change 01-Mar-2002 ACCESSIONS A00776; A16703; A26782; A24833; A35549; I59131; I79529; !1I79527; I79526; I79530; I54865; I55296; I54845; I69353; !1A35393; I41126; G64766; I54001 REFERENCE A00776 !$#authors Kikuchi, Y.; Yoda, K.; Yamasaki, M.; Tamura, G. !$#journal Nucleic Acids Res. (1981) 9:5671-5678 !$#title The nucleotide sequence of the promoter and the !1amino-terminal region of alkaline phosphatase structural !1gene (phoA) of Escherichia coli. !$#cross-references MUID:82081850; PMID:6273802 !$#accession A00776 !'##molecule_type DNA !'##residues 1-77 ##label KIK !'##cross-references GB:J01659; GB:V00315; NID:g147217; PIDN:AAA24359.1; !1PID:g551825 REFERENCE A16703 !$#authors Bradshaw, R.A.; Cancedda, F.; Ericsson, L.H.; Neumann, P.A.; !1Piccoli, S.P.; Schlesinger, M.J.; Shriefer, K.; Walsh, K.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:3473-3477 !$#title Amino acid sequence of Escherichia coli alkaline !1phosphatase. !$#cross-references MUID:81273081; PMID:7022451 !$#contents isozyme 3 !$#accession A16703 !'##molecule_type protein !'##residues 23-36,'N',38-56,'N',58-471 ##label BRA REFERENCE A26782 !$#authors Shuttleworth, H.; Taylor, J.; Minton, N. !$#journal Nucleic Acids Res. (1986) 14:8689 !$#title Sequence of the gene for alkaline phosphatase from !1Escherichia coli JM83. !$#cross-references MUID:87066741; PMID:3537962 !$#accession A26782 !'##molecule_type DNA !'##residues 1-50,'G',52-197,'E',199-471 ##label SHU !'##experimental_source strain JM83 REFERENCE A91552 !$#authors Chang, C.N.; Kuang, W.J.; Chen, E.Y. !$#journal Gene (1986) 44:121-125 !$#title Nucleotide sequence of the alkaline phosphatase gene of !1Escherichia coli. !$#cross-references MUID:87031576; PMID:3533724 !$#accession A24833 !'##molecule_type DNA !'##residues 1-197,'E',199-471 ##label CHA !'##cross-references GB:M13345; NID:g147224; PIDN:AAA83893.1; !1PID:g147225 !'##experimental_source strain K12, 294 REFERENCE A35549 !$#authors Chou, M.M.; Kendall, D.A. !$#journal J. Biol. Chem. (1990) 265:2873-2880 !$#title Polymeric sequences reveal a functional interrelationship !1between hydrophobicity and length of signal peptides. !$#cross-references MUID:90153918; PMID:2154463 !$#accession A35549 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type DNA !'##residues 1-21 ##label CHO REFERENCE I59131 !$#authors DuBose, R.F.; Dykhuizen, D.E.; Hartl, D.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:7036-7040 !$#title Genetic exchange among natural isolates of bacteria: !1Recombination within the phoA gene of Escherichia coli. !$#cross-references MUID:88320572; PMID:3045828 !$#accession I59131 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-2,'H',4-160,'S',162-197,'E',199-259,'N',261-266,'A', !1268-380,'D',382-471 ##label RES !'##cross-references GB:M29663; NID:g147228; PIDN:AAA24363.1; !1PID:g147229 !$#accession I79529 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-197,'E',199-380,'D',382-471 ##label RE6 !'##cross-references GB:M29669; NID:g147240; PIDN:AAA24369.1; !1PID:g147241 !'##experimental_source strain RM224H !$#accession I79527 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-197,'E',199-266,'A',268-380,'D',382-471 ##label RE7 !'##cross-references GB:M29667; NID:g147236; PIDN:AAA24367.1; !1PID:g147237 !'##experimental_source strain RM45E !$#accession I79526 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-197,'E',199-259,'N',261-266,'A',268-397,'V',399-471 !1##label RE8 !'##cross-references GB:M29666; NID:g147234; PIDN:AAA24366.1; !1PID:g147235 !'##experimental_source strain RM217T !$#accession I79530 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-35,'S',37-197,'E',199-290,'Q',292-359,'A',361-380,'D', !1382-471 ##label RE9 !'##cross-references GB:M29670; NID:g147242; PIDN:AAA24370.1; !1PID:g147243 !'##experimental_source strain RM202I REFERENCE I54865 !$#authors Michaelis, S.; Hunt, J.F.; Beckwith, J. !$#journal J. Bacteriol. (1986) 167:160-167 !$#title Effects of signal sequence mutations on the kinetics of !1alkaline phosphatase export to the periplasm in Escherichia !1coli. !$#cross-references MUID:86250586; PMID:3522543 !$#accession I54865 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-21 ##label RE2 !'##cross-references GB:M13763; NID:g147215; PIDN:AAA24358.1; !1PID:g147216 REFERENCE I55296 !$#authors Laforet, G.A.; Kaiser, E.T.; Kendall, D.A. !$#journal J. Biol. Chem. (1989) 264:14478-14485 !$#title Signal peptide subsegments are not always functionally !1interchangeable: M13 procoat hydrophobic core fails to !1transport alkaline phosphatase in Escherichia coli. !$#cross-references MUID:89340570; PMID:2668291 !$#accession I55296 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-23 ##label RE3 !'##cross-references GB:J05005; NID:g147226; PIDN:AAA24362.1; !1PID:g147227 REFERENCE I54845 !$#authors Inouye, H.; Barnes, W.; Beckwith, J. !$#journal J. Bacteriol. (1982) 149:434-439 !$#title Signal sequence of alkaline phosphatase of Escherichia coli. !$#cross-references MUID:82119946; PMID:7035431 !$#accession I54845 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 162-193 ##label RE4 !'##cross-references GB:J01660; NID:g147218; PIDN:AAA24360.1; !1PID:g147222 !$#accession I69353 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 385-399 ##label RE5 !'##cross-references GB:J01661; NID:g147219; PIDN:AAA24361.1; !1PID:g147223 REFERENCE A35393 !$#authors Agrawal, D.K.; Wanner, B.L. !$#journal J. Bacteriol. (1990) 172:3180-3190 !$#title A phoA structural gene mutation that conditionally affects !1formation of the enzyme bacterial alkaline phosphatase. !$#cross-references MUID:90264311; PMID:2345142 !$#accession A35393 !'##status preliminary !'##molecule_type DNA !'##residues 1-56,'Y',58-107 ##label AGR !'##cross-references GB:M33536 REFERENCE I41126 !$#authors Gray, G.L.; Baldridge, J.S.; McKeown, K.S.; Heyneker, H.L.; !1Chang, C.N. !$#journal Gene (1985) 39:247-254 !$#title Periplasmic production of correctly processed human growth !1hormone in Escherichia coli: natural and bacterial signal !1sequences are interchangeable. !$#cross-references MUID:86137393; PMID:3912261 !$#accession I41126 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-9,'V',11-21 ##label GRA !'##cross-references GB:M14399; NID:g145229; PIDN:AAA23431.1; !1PID:g145230 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64766 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 'MSRPRLIVALFLFFNVFVHGENKV',2-197,'E',199-471 ##label BLAT !'##cross-references GB:AE000145; GB:U00096; NID:g1786580; !1PIDN:AAC73486.1; PID:g1786582; UWGP:b0383 !'##experimental_source strain K-12, substrain MG1655 COMMENT This is a metalloenzyme containing zinc and magnesium. The !1active isozyme 3 is a dimer of identical chains. Isozyme 1, !1a dimer of identical chains, corresponds to residues 22-471; !1isozyme 2 is a dimer of heterogeneous chains, one of each of !1the subunits from isozymes 1 and 3. GENETICS !$#gene phoA !$#map_position 9 min !$#start_codon GTG CLASSIFICATION #superfamily alkaline phosphatase KEYWORDS magnesium; phosphoprotein; phosphoric monoester hydrolase; !1zinc FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-471 #product alkaline phosphatase, isozyme 1 chain !8#status experimental #label MAT1\ !$23-471 #product alkaline phosphatase, isozyme 3 chain !8#status experimental #label MAT3\ !$124 #active_site Ser (phosphoserine intermediate) #status !8experimental\ !$188 #binding_site substrate phosphate (Arg) #status !8experimental\ !$190-200,308-358 #disulfide_bonds #status experimental\ !$353,394,434 #binding_site zinc (His) #status experimental SUMMARY #length 471 #molecular-weight 49437 #checksum 3840 SEQUENCE /// ENTRY PAHUA #type complete TITLE alkaline phosphatase (EC 3.1.3.1) precursor, placental [validated] - human ALTERNATE_NAMES glycerophosphatase; orthophosphoric-monoester phosphohydrolase, Regan isozyme; phosphomonoesterase ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1987 #sequence_revision 28-Jul-1995 #text_change 08-Dec-2000 ACCESSIONS A31074; A27363; A24318; B24318; A25385; A94099; A94082; !1A28958; A90114; A24688 REFERENCE A31074 !$#authors Knoll, B.J.; Rothblum, K.N.; Longley, M. !$#journal J. Biol. Chem. (1988) 263:12020-12027 !$#title Nucleotide sequence of the human placental alkaline !1phosphatase gene. Evolution of the 5' flanking region by !1deletion/substitution. !$#cross-references MUID:88298886; PMID:3042787 !$#accession A31074 !'##molecule_type DNA !'##residues 1-535 ##label KNO !'##cross-references GB:J03931; GB:M19159; NID:g178475; PIDN:AAA51710.1; !1PID:g178476 REFERENCE A91586 !$#authors Knoll, B.J.; Rothblum, K.N.; Longley, M. !$#journal Gene (1987) 60:267-276 !$#title Two gene duplication events in the evolution of the human !1heat-stable alkaline phosphatases. !$#cross-references MUID:88167830; PMID:3443302 !$#accession A27363 !'##molecule_type mRNA !'##residues 1-76 ##label KN2 !'##cross-references GB:M19160 REFERENCE A94113 !$#authors Henthorn, P.S.; Knoll, B.J.; Raducha, M.; Rothblum, K.N.; !1Slaughter, C.; Weiss, M.; Lafferty, M.A.; Fischer, T.; !1Harris, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:5597-5601 !$#title Products of two common alleles at the locus for human !1placental alkaline phosphatase differ by seven amino acids. !$#cross-references MUID:86287303; PMID:3461452 !$#accession A24318 !'##molecule_type mRNA !'##residues 23-535 ##label HEN !'##cross-references GB:M14169 !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing !'##note this is polymorphism type 1; 67-Leu also found !$#accession B24318 !'##molecule_type mRNA !'##residues 1-24,'L',26-65,'V',67-262,'H',264-276,'R',278-284,'A', !1286-388,'C',390-393,'G',395-535 ##label HE2 !'##cross-references GB:M14170; NID:g178469; PIDN:AAA51709.1; !1PID:g178470 !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing !'##note this is polymorphism type 3; 89-Leu also found REFERENCE A25385 !$#authors Millan, J.L. !$#journal J. Biol. Chem. (1986) 261:3112-3115 !$#title Molecular cloning and sequence analysis of human placental !1alkaline phosphatase. !$#cross-references MUID:86140079; PMID:3512548 !$#accession A25385 !'##molecule_type mRNA !'##residues 1-230,'P',232-535 ##label MIL !'##cross-references GB:M13077; NID:g178471; PIDN:AAC97139.1; !1PID:g178474 REFERENCE A94099 !$#authors Ovitt, C.E.; Strauss, A.W.; Alpers, D.H.; Chou, J.Y.; Boime, !1I. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:3781-3785 !$#title Expression of different-sized placental alkaline phosphatase !1mRNAs in placenta and choriocarcinoma cells. !$#cross-references MUID:86233318; PMID:3459156 !$#accession A94099 !'##molecule_type mRNA !'##residues 382-435,'T',437-535 ##label OVI !'##note a soluble or serum form was also found that may arise by !1proteolytic cleavage REFERENCE A94082 !$#authors Kam, W.; Clauser, E.; Kim, Y.S.; Kan, Y.W.; Rutter, W.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:8715-8719 !$#title Cloning, sequencing, and chromosomal localization of human !1term placental alkaline phosphatase cDNA. !$#cross-references MUID:86094295; PMID:3001717 !$#accession A94082 !'##molecule_type mRNA !'##residues 6-24,'L',26-260,'GE',263-323,'H',325-395,'FI',398-400,'A', !1402-535 ##label KAM !'##cross-references GB:M12551; NID:g178463; PIDN:AAA51706.1; !1PID:g178464 REFERENCE A28958 !$#authors Micanovic, R.; Bailey, C.A.; Brink, L.; Gerber, L.; Pan, !1Y.C.E.; Hulmes, J.D.; Udenfriend, S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:1398-1402 !$#title Aspartic acid-484 of nascent placental alkaline phosphatase !1condenses with a phosphatidylinositol glycan to become the !1carboxyl terminus of the mature enzyme. !$#cross-references MUID:88144444; PMID:3422741 !$#accession A28958 !'##molecule_type protein !'##residues 485-535 ##label MIC REFERENCE A90114 !$#authors Ezra, E.; Blacher, R.; Udenfriend, S. !$#journal Biochem. Biophys. Res. Commun. (1983) 116:1076-1083 !$#title Purification and partial sequencing of human placental !1alkaline phosphatase. !$#cross-references MUID:84079906; PMID:6651840 !$#accession A90114 !'##molecule_type protein !'##residues 23-64 ##label EZR COMMENT This is the form of the enzyme predominantly expressed in !1the placenta after the fourteenth week. GENETICS !$#gene GDB:ALPP; ALP1 !'##cross-references GDB:119672; OMIM:171800 !$#map_position 2q37.1-2q37.1 !$#introns 26/1; 65/1; 103/3; 162/1; 219/3; 264/3; 289/1; 334/1; 398/1; !1437/1 !$#note this gene is very polymorphic COMPLEX homodimer FUNCTION !$#description catalyzes the hydrolysis of phosphate monoesters CLASSIFICATION #superfamily alkaline phosphatase KEYWORDS blocked carboxyl end; glycoprotein; homodimer; lipoprotein; !1membrane protein; metalloprotein; phosphatidylinositol !1linkage; phosphoprotein; phosphoric monoester hydrolase; !1placenta; zinc FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-506 #product alkaline phosphatase, placental #status !8experimental #label MAT\ !$507-535 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$114 #active_site Ser (phosphoserine intermediate) #status !8predicted\ !$144,271 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$188 #binding_site substrate phosphate (Arg) #status !8predicted\ !$342,382,454 #binding_site zinc (His) #status predicted\ !$506 #modified_site GPI-anchor ethanolamine amidated !8carboxyl end (Asp) (in mature form) #status !8experimental SUMMARY #length 535 #molecular-weight 57953 #checksum 8581 SEQUENCE /// ENTRY PAHUI #type complete TITLE alkaline phosphatase (EC 3.1.3.1) precursor, intestinal - human ALTERNATE_NAMES glycerophosphatase; phosphomonoesterase ORGANISM #formal_name Homo sapiens #common_name man DATE 16-Aug-1988 #sequence_revision 03-Aug-1995 #text_change 28-Jan-2000 ACCESSIONS A31073; S00697; A26582; A25885; C27363; A23531; C56889 REFERENCE A31073 !$#authors Henthorn, P.S.; Raducha, M.; Kadesch, T.; Weiss, M.J.; !1Harris, H. !$#journal J. Biol. Chem. (1988) 263:12011-12019 !$#title Sequence and characterization of the human intestinal !1alkaline phosphatase gene. !$#cross-references MUID:88298885; PMID:2841341 !$#accession A31073 !'##molecule_type DNA !'##residues 1-528 ##label HEN !'##cross-references GB:J03930; NID:g178441; PIDN:AAA98617.1; !1PID:g178442 REFERENCE S00697 !$#authors Millan, J.L. !$#journal Nucleic Acids Res. (1987) 15:10599 !$#title Promoter structure of the human intestinal alkaline !1phosphatase gene. !$#cross-references MUID:88096602; PMID:3697102 !$#accession S00697 !'##molecule_type DNA !'##residues 1-100 ##label MIL !'##cross-references EMBL:Y00512; NID:g28630; PIDN:CAA68564.1; !1PID:g296631 REFERENCE A26582 !$#authors Berger, J.; Garattini, E.; Hua, J.C.; Udenfriend, S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:695-698 !$#title Cloning and sequencing of human intestinal alkaline !1phosphatase cDNA. !$#cross-references MUID:87118235; PMID:3468508 !$#accession A26582 !'##molecule_type mRNA !'##residues 1-409,'T',411-528 ##label BER !'##cross-references GB:M15184; GB:M31008; NID:g178443; PIDN:AAA51704.1; !1PID:g178446 !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing REFERENCE A25885 !$#authors Henthorn, P.S.; Raducha, M.; Edwards, Y.H.; Weiss, M.J.; !1Slaughter, C.; Lafferty, M.A.; Harris, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:1234-1238 !$#title Nucleotide and amino acid sequences of human intestinal !1alkaline phosphatase: close homology to placental alkaline !1phosphatase. !$#cross-references MUID:87147248; PMID:3469665 !$#accession A25885 !'##molecule_type mRNA !'##residues 1-297,'L',299-346,'V',348-496,'L',498-528 ##label HE2 !'##cross-references GB:M15694; NID:g178431; PIDN:AAA51703.1; !1PID:g178432 REFERENCE A91586 !$#authors Knoll, B.J.; Rothblum, K.N.; Longley, M. !$#journal Gene (1987) 60:267-276 !$#title Two gene duplication events in the evolution of the human !1heat-stable alkaline phosphatases. !$#cross-references MUID:88167830; PMID:3443302 !$#accession C27363 !'##molecule_type mRNA !'##residues 1-73 ##label KNO !'##cross-references GB:M19161; NID:g178447; PIDN:AAA51705.1; !1PID:g553176 REFERENCE A94094 !$#authors Hua, J.C.; Berger, J.; Pan, Y.C.E.; Hulmes, J.D.; !1Udenfriend, S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:2368-2372 !$#title Partial sequencing of human adult, human fetal, and bovine !1intestinal alkaline phosphatases: comparison with the human !1placental and liver isozymes. !$#cross-references MUID:86205956; PMID:3458202 !$#accession A23531 !'##molecule_type protein !'##residues 20-49,'T',51-58 ##label HUA REFERENCE A56889 !$#authors Nishihara, Y.; Hayashi, Y.; Adachi, T.; Koyama, I.; !1Stigbrand, T.; Hirano, K. !$#journal Clin. Chem. (1992) 38:2539-2542 !$#title Chemical nature of intestinal-type alkaline phosphatase in !1human kidney. !$#cross-references MUID:93092315; PMID:1458595 !$#accession C56889 !'##molecule_type protein !'##residues 20-49 ##label NIS !'##experimental_source meconium; intestine; kidney !'##note sequence extracted from NCBI backbone (NCBIP:121052, !1NCBIP:121051, NCBIP:121050) !'##note identical sequences were determined for material from !1intestine, meconium, and (lacking the first residue) kidney COMMENT This form of the enzyme is predominantly expressed in the !1intestine. GENETICS !$#gene GDB:ALPI !'##cross-references GDB:119671; OMIM:171740 !$#map_position 2q37.1-2q37.1 !$#introns 23/1; 62/1; 100/3; 159/1; 216/3; 261/3; 286/1; 331/2; 395/1; !1434/1 COMPLEX homodimer FUNCTION !$#description catalyzes the hydrolysis of phosphate monoesters CLASSIFICATION #superfamily alkaline phosphatase KEYWORDS blocked carboxyl end; glycoprotein; homodimer; lipoprotein; !1membrane protein; metalloprotein; phosphatidylinositol !1linkage; phosphoprotein; phosphoric monoester hydrolase; !1zinc FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-503 #product alkaline phosphatase, intestinal #status !8predicted #label MAT\ !$504-528 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$111 #active_site Ser (phosphoserine intermediate) #status !8predicted\ !$141,268,429 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$185 #binding_site substrate phosphate (Arg) #status !8predicted\ !$339,379,451 #binding_site zinc (His) #status predicted\ !$503 #modified_site GPI-anchor ethanolamine amidated !8carboxyl end (Asp) (in mature form) #status predicted SUMMARY #length 528 #molecular-weight 56812 #checksum 1989 SEQUENCE /// ENTRY PAHUH #type complete TITLE alkaline phosphatase (EC 3.1.3.1) precursor, hepatic - human ALTERNATE_NAMES liver/bone/kidney-type alkaline phosphatase; tissue-nonspecific alkaline phosphatase ORGANISM #formal_name Homo sapiens #common_name man DATE 21-May-1988 #sequence_revision 28-Jul-1995 #text_change 11-Jun-1999 ACCESSIONS S03613; A25041; A25249; A56889 REFERENCE S03613 !$#authors Kishi, F.; Matsuura, S.; Kajii, T. !$#journal Nucleic Acids Res. (1989) 17:2129 !$#title Nucleotide sequence of the human liver-type alkaline !1phosphatase cDNA. !$#cross-references MUID:89183624; PMID:2928120 !$#accession S03613 !'##molecule_type mRNA !'##residues 1-524 ##label KIS !'##cross-references EMBL:X14174; NID:g28737; PIDN:CAA32376.1; !1PID:g28738 REFERENCE A25041 !$#authors Weiss, M.J.; Henthorn, P.S.; Lafferty, M.A.; Slaughter, C.; !1Raducha, M.; Harris, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:7182-7186 !$#title Isolation and characterization of a cDNA encoding a human !1liver/bone/kidney-type alkaline phosphatase. !$#cross-references MUID:87016911; PMID:3532105 !$#accession A25041 !'##molecule_type mRNA !'##residues 1-103,'N',105-234,'G',236-262,'Y',264-512,'V',514-524 !1##label WEI !'##cross-references GB:M14168 !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing REFERENCE A25249 !$#authors Garattini, E.; Hua, J.C.; Pan, Y.C.E.; Udenfriend, S. !$#journal Arch. Biochem. Biophys. (1986) 245:331-337 !$#title Human liver alkaline phosphatase, purification and partial !1sequencing: homology with the placental isozyme. !$#cross-references MUID:86157574; PMID:3954357 !$#accession A25249 !'##molecule_type protein !'##residues 18-28,'A',30-34,'X',36-39 ##label GAR REFERENCE A56889 !$#authors Nishihara, Y.; Hayashi, Y.; Adachi, T.; Koyama, I.; !1Stigbrand, T.; Hirano, K. !$#journal Clin. Chem. (1992) 38:2539-2542 !$#title Chemical nature of intestinal-type alkaline phosphatase in !1human kidney. !$#cross-references MUID:93092315; PMID:1458595 !$#accession A56889 !'##molecule_type protein !'##residues 18-32 ##label NIS !'##experimental_source liver; kidney !'##note sequence extracted from NCBI backbone (NCBIP:121054, !1NCBIP:121053) !'##note identical amino-terminal sequences were obtained from kidney !1and liver REFERENCE A44715 !$#authors Weiss, M.J.; Ray, K.; Henthorn, P.S.; Lamb, B.; Kadesch, T.; !1Harris, H. !$#journal J. Biol. Chem. (1988) 263:12002-12010 !$#title Structure of the human liver/bone/kidney alkaline !1phosphatase gene. !$#cross-references MUID:88298884; PMID:3165380 !$#contents annotation; introns; sequence corrections to A25041 COMMENT This form of the enzyme is expressed in a variety of tissues !1and is the predominantly expressed form in the placenta !1before the tenth week. GENETICS !$#gene GDB:ALPL !'##cross-references GDB:118730; OMIM:171760 !$#map_position 1p36.1-1p34 !$#introns 21/1; 61/1; 99/3; 158/1; 216/3; 264/3; 288/1; 333/1; 397/1; !1437/1 !$#note the first intron occurs before the initiator codon !$#note deficiency of this enzyme causes perinatal hypophosphatasia COMPLEX homodimer FUNCTION !$#description catalyzes the hydrolysis of phosphate monoesters !$#note in bone this enzyme functions in mineralization CLASSIFICATION #superfamily alkaline phosphatase KEYWORDS glycoprotein; homodimer; metalloprotein; phosphoprotein; !1phosphoric monoester hydrolase; zinc FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-524 #product alkaline phosphatase, hepatic #status !8predicted #label MAT\ !$110 #active_site Ser (phosphoserine intermediate) #status !8predicted\ !$140,230,271,430 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$184 #binding_site substrate phosphate (Arg) #status !8predicted\ !$303 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$341,381,454 #binding_site zinc (His) #status predicted SUMMARY #length 524 #molecular-weight 57292 #checksum 9058 SEQUENCE /// ENTRY S74570 #type complete TITLE alkaline phosphatase (EC 3.1.3.1) phoA - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES hypothetical protein sll0222 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S74570 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74570 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-326 ##label KAN !'##cross-references EMBL:D90900; GB:AB001339; NID:g1651768; !1PIDN:BAA16722.1; PID:g1651795 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene phoA FUNCTION !$#description catalyzes the hydrolysis of phosphate monoesters CLASSIFICATION #superfamily Synechocystis alkaline phosphatase phoA; !1phosphoesterase core homology KEYWORDS phosphoric monoester hydrolase FEATURE !$49-131 #domain phosphoesterase core homology #label PEC SUMMARY #length 326 #molecular-weight 36013 #checksum 6561 SEQUENCE /// ENTRY A42467 #type complete TITLE alkaline phosphatase (EC 3.1.3.1) phoA precursor - Lysobacter enzymogenes ORGANISM #formal_name Lysobacter enzymogenes DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A42467 REFERENCE A42467 !$#authors Au, S.; Roy, K.L.; von Tigerstrom, R.G. !$#journal J. Bacteriol. (1991) 173:4551-4557 !$#title Nucleotide sequence and characterization of the gene for !1secreted alkaline phosphatase from Lysobacter enzymogenes. !$#cross-references MUID:91310559; PMID:1856159 !$#accession A42467 !'##status preliminary !'##molecule_type DNA !'##residues 1-539 ##label AUA !'##cross-references EMBL:X56656; NID:g48800; PIDN:CAA39978.1; !1PID:g581292 !'##experimental_source ATCC 29487 GENETICS !$#gene phoA FUNCTION !$#description catalyzes the hydrolysis of phosphate monoesters CLASSIFICATION #superfamily Lysobacter alkaline phosphatase phoA; !1phosphoesterase core homology KEYWORDS phosphoric monoester hydrolase FEATURE !$152-221 #domain phosphoesterase core homology #label PEC SUMMARY #length 539 #molecular-weight 56489 #checksum 5196 SEQUENCE /// ENTRY PABYC #type complete TITLE acid phosphatase (EC 3.1.3.2) repressible, precursor - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES acid phosphatase PHO5; protein YBR0814; protein YBR093c ORGANISM #formal_name Saccharomyces cerevisiae DATE 19-Feb-1984 #sequence_revision 30-Sep-1991 #text_change 12-Nov-1999 ACCESSIONS S05795; A38792; S48260; S45961; A00777; A38793; S41855; !1B25241; A25367; A27774; S44675 REFERENCE S05794 !$#authors Bajwa, W.; Meyhack, B.; Rudolph, H.; Schweingruber, A.M.; !1Hinnen, A. !$#journal Nucleic Acids Res. (1984) 12:7721-7739 !$#title Structural analysis of the two tandemly repeated acid !1phosphatase genes in yeast. !$#cross-references MUID:85037940; PMID:6093051 !$#accession S05795 !'##molecule_type DNA !'##residues 1-467 ##label BAJ !'##cross-references EMBL:X01079; NID:g4162; PIDN:CAA25555.1; !1PID:g758282 !'##note the authors translated the codon TAC for residue 272 as Thr !$#accession A38792 !'##molecule_type protein !'##residues 18-45 ##label BAJ2 REFERENCE S48255 !$#authors Mannhaupt, G.; Stucka, R.; Ehnle, S.; Vetter, I.; Feldmann, !1H. !$#journal Yeast (1994) 10:1363-1381 !$#title Analysis of a 70 kb region on the right arm of yeast !1chromosome II. !$#cross-references MUID:95208357; PMID:7900426 !$#accession S48260 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-467 ##label MAN !'##cross-references EMBL:X78993; NID:g476045; PIDN:CAA55598.1; !1PID:g476051 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1994 REFERENCE S45927 !$#authors Feldmann, H.; Mannhaupt, G.; Schwarzlose, C.; Vetter, I. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S45961 !'##molecule_type DNA !'##residues 1-467 ##label FE2 !'##cross-references EMBL:Z35962; NID:g536364; PIDN:CAA85046.1; !1PID:g536365; GSPDB:GN00002; MIPS:YBR093c REFERENCE A00777 !$#authors Arima, K.; Oshima, T.; Kubota, I.; Nakamura, N.; Mizunaga, !1T.; Toh-e, A. !$#journal Nucleic Acids Res. (1983) 11:1657-1672 !$#title The nucleotide sequence of the yeast PHO5 gene: a putative !1precursor of repressible acid phosphatase contains a signal !1peptide. !$#cross-references MUID:83168913; PMID:6300772 !$#accession A00777 !'##molecule_type DNA !'##residues 1-35,'Y',37-129,'G',131-293,'Q',295-445,'V',447-461,'DT', !1464-465,'K',467 ##label ARI !'##cross-references EMBL:V01320; NID:g4158; PIDN:CAA24630.1; PID:g4159 !$#accession A38793 !'##molecule_type protein !'##residues 18-26,'X',28 ##label ARI2 REFERENCE S41855 !$#authors Meyhack, B.; Bajwa, W.; Rudolph, H.; Hinnen, A. !$#journal EMBO J. (1982) 1:675-680 !$#title Two yeast acid phosphatase structural genes are the result !1of a tandem duplication and show different degrees of !1homology in their promoter and coding sequences. !$#cross-references MUID:84236032; PMID:6329697 !$#accession S41855 !'##molecule_type DNA !'##residues 1-30,'T',32-51,'S',53-75 ##label MEY !'##cross-references EMBL:M24178; NID:g172156; PIDN:AAA34868.1; !1PID:g172157 REFERENCE A93074 !$#authors Tait-Kamradt, A.G.; Turner, K.J.; Kramer, R.A.; Elliott, !1Q.D.; Bostian, S.J.; Thill, G.P.; Rogers, D.T.; Bostian, !1K.A. !$#journal Mol. Cell. Biol. (1986) 6:1855-1865 !$#title Reciprocal regulation of the tandemly duplicated PHO5/PHO3 !1gene cluster within the acid phosphatase multigene family of !1Saccharomyces cerevisiae. !$#cross-references MUID:87064474; PMID:3537710 !$#accession B25241 !'##molecule_type DNA !'##residues 1-44 ##label TAI REFERENCE A25367 !$#authors Bergman, L.W. !$#journal Mol. Cell. Biol. (1986) 6:2298-2304 !$#title A DNA fragment containing the upstream activator sequence !1determines nucleosome positioning of the transcriptionally !1repressed PHO5 gene of Saccharomyces cerevisiae. !$#cross-references MUID:87064526; PMID:3023927 !$#accession A25367 !'##molecule_type DNA !'##residues 1-2,'Y',4-43,'T',45-51 ##label BER REFERENCE A27774 !$#authors Silve, S.; Monod, M.; Hinnen, A.; Haguenauer-Tsapis, R. !$#journal Mol. Cell. Biol. (1987) 7:3306-3314 !$#title The yeast acid phosphatase can enter the secretory pathway !1without its N-terminal signal sequence. !$#cross-references MUID:88038886; PMID:3313013 !$#accession A27774 !'##molecule_type DNA !'##residues 1-51,'S',53-60 ##label SIL !'##cross-references GB:M17306 GENETICS !$#gene SGD:PHO5; MIPS:YBR093c !'##cross-references SGD:S0000297; MIPS:YBR093c !$#map_position 2R !$#note YBR093c CLASSIFICATION #superfamily yeast acid phosphatase KEYWORDS glycoprotein; phosphohistidine; phosphoprotein; phosphoric !1monoester hydrolase FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-467 #product acid phosphatase, repressible #status !8experimental #label MAT\ !$75 #active_site His (phosphohistidine intermediate) !8#status predicted\ !$97,103,162,192,250, !$315,356,390,439, !$445,456,461 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$337 #active_site His #status predicted SUMMARY #length 467 #molecular-weight 52858 #checksum 455 SEQUENCE /// ENTRY PABYCC #type complete TITLE acid phosphatase (EC 3.1.3.2) precursor, constitutive - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES acid phosphatase PHO3; protein YBR0813; protein YBR092c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1991 #sequence_revision 09-Sep-1994 #text_change 05-Nov-1999 ACCESSIONS S48259; S45960; S05794; A25241; S44674 REFERENCE S48255 !$#authors Mannhaupt, G.; Stucka, R.; Ehnle, S.; Vetter, I.; Feldmann, !1H. !$#journal Yeast (1994) 10:1363-1381 !$#title Analysis of a 70 kb region on the right arm of yeast !1chromosome II. !$#cross-references MUID:95208357; PMID:7900426 !$#accession S48259 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-467 ##label MAN !'##cross-references EMBL:X78993; NID:g476045; PIDN:CAA55597.1; !1PID:g476050 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1994 REFERENCE S45927 !$#authors Feldmann, H.; Mannhaupt, G.; Schwarzlose, C.; Vetter, I. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S45960 !'##molecule_type DNA !'##residues 1-467 ##label FE2 !'##cross-references EMBL:Z35961; NID:g536362; PIDN:CAA85045.1; !1PID:g536363; GSPDB:GN00002; MIPS:YBR092c REFERENCE S05794 !$#authors Bajwa, W.; Meyhack, B.; Rudolph, H.; Schweingruber, A.M.; !1Hinnen, A. !$#journal Nucleic Acids Res. (1984) 12:7721-7739 !$#title Structural analysis of the two tandemly repeated acid !1phosphatase genes in yeast. !$#cross-references MUID:85037940; PMID:6093051 !$#accession S05794 !'##molecule_type DNA !'##residues 1-218,'MKT',222-467 ##label BAJ1 !'##cross-references EMBL:X01080; NID:g4148; PIDN:CAA25557.1; !1PID:g758281 !'##note the authors translated the codon AAT for residue 134 as Asp and !1TAC for residue 272 as Thr REFERENCE A93074 !$#authors Tait-Kamradt, A.G.; Turner, K.J.; Kramer, R.A.; Elliott, !1Q.D.; Bostian, S.J.; Thill, G.P.; Rogers, D.T.; Bostian, !1K.A. !$#journal Mol. Cell. Biol. (1986) 6:1855-1865 !$#title Reciprocal regulation of the tandemly duplicated PHO5/PHO3 !1gene cluster within the acid phosphatase multigene family of !1Saccharomyces cerevisiae. !$#cross-references MUID:87064474; PMID:3537710 !$#accession A25241 !'##molecule_type DNA !'##residues 1-44 ##label TAI GENETICS !$#gene SGD:PHO3; MIPS:YBR092c !'##cross-references SGD:S0000296; MIPS:YBR092c !$#map_position 2R CLASSIFICATION #superfamily yeast acid phosphatase KEYWORDS glycoprotein; phosphohistidine; phosphoprotein; phosphoric !1monoester hydrolase FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-467 #product acid phosphatase, constitutive #status !8predicted #label MAT\ !$75 #active_site His (phosphohistidine intermediate) !8#status predicted\ !$97,103,162,192,250, !$315,356,390,439, !$445,456,461 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$337 #active_site His #status predicted SUMMARY #length 467 #molecular-weight 52776 #checksum 2729 SEQUENCE /// ENTRY A25326 #type complete TITLE acid phosphatase (EC 3.1.3.2) precursor [similarity] - fission yeast (Schizosaccharomyces pombe) ORGANISM #formal_name Schizosaccharomyces pombe DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A25326; T50405 REFERENCE A25326 !$#authors Elliott, S.; Chang, C.; Schweingruber, M.E.; Schaller, J.; !1Rickli, E.E.; Carbon, J. !$#journal J. Biol. Chem. (1986) 261:2936-2941 !$#title Isolation and characterization of the structural gene for !1secreted acid phosphatase from Schizosaccharomyces pombe. !$#cross-references MUID:86140050; PMID:3005272 !$#accession A25326 !'##molecule_type DNA !'##residues 1-453 ##label ELL !'##cross-references GB:M11857; NID:g173422; PIDN:AAA35321.1; !1PID:g173423 REFERENCE Z25068 !$#authors Rieger, M.; McDougall, R.C.; Rajandream, M.A.; Barrell, B.G. !$#submission submitted to the EMBL Data Library, January 2000 !$#accession T50405 !'##molecule_type DNA !'##residues 1-453 ##label RIE !'##cross-references EMBL:AL137099; PIDN:CAB68657.1; GSPDB:GN00067; !1SPDB:SPBP4G3.02 !'##experimental_source strain 972h(-); clone p1 p4G3 GENETICS !$#gene pho1; SPDB:SPBP4G3.02 !$#map_position 2 CLASSIFICATION #superfamily yeast acid phosphatase KEYWORDS phosphohistidine; phosphoprotein; phosphoric monoester !1hydrolase FEATURE !$68 #active_site Arg #status predicted\ !$69 #active_site His (phosphohistidine intermediate) !8#status predicted SUMMARY #length 453 #molecular-weight 50557 #checksum 9744 SEQUENCE /// ENTRY JN0715 #type complete TITLE 3-phytase (EC 3.1.3.8) B precursor - Aspergillus ficuum ALTERNATE_NAMES pH 2.5-optimum acid phosphatase ORGANISM #formal_name Aspergillus ficuum DATE 14-Jul-1994 #sequence_revision 19-Oct-1995 #text_change 07-May-1999 ACCESSIONS JN0715; PN0594; PN0460 REFERENCE JN0715 !$#authors Ehrlich, K.C.; Montalbano, B.G.; Mullaney, E.J.; Dischinger !1Jr., H.C.; Ullah, A.H.J. !$#journal Biochem. Biophys. Res. Commun. (1993) 195:53-57 !$#title Identification and cloning of a second phytase gene (phyB) !1from Aspergillus niger (ficuum). !$#cross-references MUID:93371452; PMID:7916610 !$#accession JN0715 !'##molecule_type DNA !'##residues 1-479 ##label EHR !'##cross-references GB:L20567 !$#accession PN0594 !'##molecule_type protein !'##residues 20-101;133-146;376-399 ##label EH2 REFERENCE PN0460 !$#authors Ullah, A.H.J.; Dischinger Jr., H.C. !$#journal Biochem. Biophys. Res. Commun. (1993) 192:754-759 !$#title Identification of active-site residues in Aspergillus ficuum !1extracellular pH 2.5 optimum acid phosphatase. !$#cross-references MUID:93249452; PMID:8484781 !$#accession PN0460 !'##molecule_type protein !'##residues 65-66,68-93 ##label ULL COMMENT This enzyme, previously characterized as an acid phosphatase !1(EC 3.1.3.2), hydrolyzes phytic acid at pH 2.5. GENETICS !$#gene phyB !$#introns 261/1; 300/2; 335/2 CLASSIFICATION #superfamily yeast acid phosphatase KEYWORDS extracellular protein; glycoprotein; phosphohistidine; !1phosphoprotein; phosphoric monoester hydrolase FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-479 #product 3-phytase #status experimental #label MAT\ !$81,337 #active_site Arg, His #status predicted\ !$82 #active_site His (phosphohistidine intermediate) !8#status predicted\ !$106,191,227,250, !$315,340,425,442,458 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 479 #molecular-weight 52595 #checksum 4936 SEQUENCE /// ENTRY JN0890 #type complete TITLE acid phosphatase (EC 3.1.3.2) precursor - Aspergillus awamori ORGANISM #formal_name Aspergillus awamori DATE 14-Jul-1994 #sequence_revision 19-Oct-1995 #text_change 11-Jun-1999 ACCESSIONS JN0890 REFERENCE JN0889 !$#authors Piddington, C.S.; Houston, C.S.; Paloheimo, M.; Cantrell, !1M.; Miettinen-Oinonen, A.; Nevalainen, H.; Rambosek, J. !$#journal Gene (1993) 133:55-62 !$#title The cloning and sequencing of the genes encoding phytase !1(phy) and pH 2.5-optimum acid phosphatase (aph) from !1Aspergillus niger var. awamori. !$#cross-references MUID:94040796; PMID:8224894 !$#accession JN0890 !'##molecule_type DNA !'##residues 1-479 ##label PID !'##cross-references GB:L02420; NID:g166481; PIDN:AAA16897.1; !1PID:g166482 !'##experimental_source strain ALK0243 COMMENT The highly similar enzyme from A. ficuum has been shown to !1have 3-phytase (EC 3.1.3.8) activity at pH 2.5. GENETICS !$#gene aph !$#introns 261/1; 300/2; 335/2 CLASSIFICATION #superfamily yeast acid phosphatase KEYWORDS extracellular protein; glycoprotein; phosphohistidine; !1phosphoprotein; phosphoric monoester hydrolase FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-479 #product 3-phytase #status predicted #label MAT\ !$81,337 #active_site Arg, His #status predicted\ !$82 #active_site His (phosphohistidine intermediate) !8#status predicted\ !$106,191,227,250, !$315,340,425,442,458 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 479 #molecular-weight 52678 #checksum 4054 SEQUENCE /// ENTRY JN0889 #type complete TITLE 3-phytase (EC 3.1.3.8) A precursor - Aspergillus awamori ALTERNATE_NAMES myo-inositol hexakisphosphate phosphohydrolase; phyA protein ORGANISM #formal_name Aspergillus awamori DATE 14-Jul-1994 #sequence_revision 19-Oct-1995 #text_change 11-Jun-1999 ACCESSIONS JN0889 REFERENCE JN0889 !$#authors Piddington, C.S.; Houston, C.S.; Paloheimo, M.; Cantrell, !1M.; Miettinen-Oinonen, A.; Nevalainen, H.; Rambosek, J. !$#journal Gene (1993) 133:55-62 !$#title The cloning and sequencing of the genes encoding phytase !1(phy) and pH 2.5-optimum acid phosphatase (aph) from !1Aspergillus niger var. awamori. !$#cross-references MUID:94040796; PMID:8224894 !$#accession JN0889 !'##molecule_type DNA !'##residues 1-467 ##label PID !'##cross-references GB:L02421; NID:g166518; PIDN:AAA16898.1; !1PID:g166519 !'##experimental_source strain ALK0243 !'##note part of the sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing COMMENT This enzyme catalyzes the conversion of phytate to inositol !1and inorganic phosphate. GENETICS !$#gene phyA !$#introns 15/2 CLASSIFICATION #superfamily yeast acid phosphatase KEYWORDS extracellular protein; glycoprotein; phosphohistidine; !1phosphoprotein; phosphoric monoester hydrolase FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-467 #product 3-phytase A #status experimental #label MAT\ !$27,59,105,120,207, !$230,339,352,376,388 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$81,361 #active_site Arg, His #status predicted\ !$82 #active_site His (phosphohistidine intermediate) !8#status predicted SUMMARY #length 467 #molecular-weight 51074 #checksum 661 SEQUENCE /// ENTRY JN0656 #type complete TITLE 3-phytase (EC 3.1.3.8) A precursor - Aspergillus niger ALTERNATE_NAMES myo-inositol hexakisphosphate phosphohydrolase; phyA protein ORGANISM #formal_name Aspergillus niger DATE 03-Feb-1994 #sequence_revision 19-Oct-1995 #text_change 11-Jun-1999 ACCESSIONS JN0656; S28456 REFERENCE JN0656 !$#authors van Hartingsveldt, W.; van Zeijl, C.M.J.; Harteveld, G.M.; !1Gouka, R.J.; Suykerbuyk, M.E.G.; Luiten, R.G.M.; van !1Paridon, P.A.; Selten, G.C.M.; Veenstra, A.E.; van Gorcom, !1R.F.M.; van den Hondel, C.A.M.J.J. !$#journal Gene (1993) 127:87-94 !$#title Cloning, characterization and overexpression of the !1phytase-encoding gene (phyA) of Aspergillus niger. !$#cross-references MUID:93252284; PMID:8387447 !$#accession JN0656 !'##molecule_type DNA !'##residues 1-467 ##label VAN !'##cross-references GB:Z16414; NID:g2392; PIDN:CAA78904.1; PID:g2393 !'##experimental_source strain NRRL3135 !'##note parts of the sequence, including the amino end of the mature !1protein, were confirmed by protein sequencing COMMENT This enzyme catalyzes the hydrolysis of phytic acid into !1myo-inositol and inorganic phosphate. GENETICS !$#gene phyA !$#introns 15/2 CLASSIFICATION #superfamily yeast acid phosphatase KEYWORDS extracellular protein; glycoprotein; phosphohistidine; !1phosphoprotein; phosphoric monoester hydrolase FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-467 #product 3-phytase A #status experimental #label MAT\ !$27,59,105,120,207, !$230,339,352,376,388 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$81,361 #active_site Arg, His #status predicted\ !$82 #active_site His (phosphohistidine intermediate) !8#status predicted SUMMARY #length 467 #molecular-weight 51086 #checksum 1413 SEQUENCE /// ENTRY JN0482 #type complete TITLE 3-phytase (EC 3.1.3.8) A - Aspergillus ficuum ALTERNATE_NAMES myo-inositol hexakisphosphate phosphohydrolase; phyA protein ORGANISM #formal_name Aspergillus ficuum DATE 30-Sep-1993 #sequence_revision 19-Oct-1995 #text_change 07-May-1999 ACCESSIONS JN0482; PN0023 REFERENCE JN0482 !$#authors Ullah, A.H.J.; Dischinger Jr., H.C. !$#journal Biochem. Biophys. Res. Commun. (1993) 192:747-753 !$#title Aspergillus ficuum phytase: Complete primary structure !1elucidation by chemical sequencing. !$#cross-references MUID:93249451; PMID:8387289 !$#accession JN0482 !'##molecule_type protein !'##residues 1-441 ##label ULL !'##note authors state that the 9 Asn followed by Thr or Ser after an !1intervening residue are glycosylated; however, 10 Asn occur !1in this pattern REFERENCE PN0023 !$#authors Ullah, A.H.J.; Cummins, B.J.; Dischinger Jr., H.C. !$#journal Biochem. Biophys. Res. Commun. (1991) 178:45-53 !$#title Cyclohexanedione modification of arginine at the active site !1of Aspergillus ficuum phytase. !$#cross-references MUID:91298982; PMID:1648914 !$#accession PN0023 !'##molecule_type protein !'##residues 48-70 ##label UL2 COMMENT This enzyme catalyzes the hydrolysis of inorganic !1orthophosphate from phytate. CLASSIFICATION #superfamily yeast acid phosphatase KEYWORDS extracellular protein; glycoprotein; phosphohistidine; !1phosphoprotein; phosphoric monoester hydrolase FEATURE !$4,36,82,97,184,207, !$316,329,353,365 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$58,338 #active_site Arg, His #status predicted\ !$59 #active_site His (phosphohistidine intermediate) !8#status predicted SUMMARY #length 441 #molecular-weight 48524 #checksum 6058 SEQUENCE /// ENTRY S55288 #type complete TITLE phosphoglycolate phosphatase (EC 3.1.3.18) [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS S55288; D65133; S31740 REFERENCE S55287 !$#authors Lyngstadaas, A.; Lobner-Olesen, A.; Boye, E. !$#journal Mol. Gen. Genet. (1995) 247:546-554 !$#title Characterization of three genes in the dam-containing operon !1of Escherichia coli. !$#cross-references MUID:95327050; PMID:7603433 !$#accession S55288 !'##status preliminary !'##molecule_type DNA !'##residues 1-252 ##label LYN !'##cross-references EMBL:Z19601; NID:g41221; PIDN:CAA79664.1; !1PID:g41223 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65133 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-252 ##label BLAT !'##cross-references GB:AE000414; GB:U00096; NID:g1789783; !1PIDN:AAC76410.1; PID:g1789787; UWGP:b3385 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene gph FUNCTION !$#description EC 3.1.3.18 [validated, MUID:95327050] CLASSIFICATION #superfamily Alcaligenes eutrophus phosphoglycolate !1phosphatase KEYWORDS phosphoric monoester hydrolase SUMMARY #length 252 #molecular-weight 27389 #checksum 1703 SEQUENCE /// ENTRY G64154 #type complete TITLE hypothetical protein HI0565 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS G64154 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession G64154 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-224 ##label TIGR !'##cross-references GB:U32738; GB:L42023; NID:g1573548; !1PIDN:AAC22223.1; PID:g1573552; TIGR:HI0565 !'##note best homolog was a hypothetical protein from Escherichia coli CLASSIFICATION #superfamily Alcaligenes eutrophus phosphoglycolate !1phosphatase SUMMARY #length 224 #molecular-weight 24773 #checksum 6663 SEQUENCE /// ENTRY D70416 #type complete TITLE phosphoglycolate phosphatase - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS D70416 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession D70416 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-213 ##label AQF !'##cross-references GB:AE000735; NID:g2983749; PIDN:AAC07313.1; !1PID:g2983753; GB:AE000657 !'##experimental_source strain VF5 GENETICS !$#gene gph CLASSIFICATION #superfamily Alcaligenes eutrophus phosphoglycolate !1phosphatase SUMMARY #length 213 #molecular-weight 23895 #checksum 3402 SEQUENCE /// ENTRY G70044 #type complete TITLE histidine-containing protein P-Ser-HPr phosphatase (EC 3.1.3.-) [validated] - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS G70044 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G70044 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-216 ##label KUN !'##cross-references GB:Z99121; GB:AL009126; NID:g2635827; !1PIDN:CAB15502.1; PID:g2636010 !'##experimental_source strain 168 GENETICS !$#gene hprP; yvoE FUNCTION !$#description catalyzes the dephosphorylation of P-Ser-HPr !1(histidine-containing protein ptsH; PIR:WQBSPH) and !1P-Ser-crh (catabolite repression protein crh; PIR:D69607) !1[validated, MUID:98132676] !$#note requires Mg(2+) and is stimulated by inorganic phosphate; !1was also found to be stimulated by the presence of HPr !1kinase (PIR:E70044) CLASSIFICATION #superfamily Alcaligenes eutrophus phosphoglycolate !1phosphatase KEYWORDS phosphoric monoester hydrolase SUMMARY #length 216 #molecular-weight 24003 #checksum 4907 SEQUENCE /// ENTRY H71208 #type complete TITLE hypothetical protein PH1936 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H71208 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession H71208 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-217 ##label KAW !'##cross-references GB:AP000007; NID:g3236134; PIDN:BAA31063.1; !1PID:g3258380 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1936 CLASSIFICATION #superfamily Alcaligenes eutrophus phosphoglycolate !1phosphatase SUMMARY #length 217 #molecular-weight 25025 #checksum 1088 SEQUENCE /// ENTRY JH0610 #type complete TITLE acid phosphatase (EC 3.1.3.2) ACPP precursor [validated] - human ALTERNATE_NAMES acid phosphatase, prostatic; orthophosphoric monoester phosphohydrolase ORGANISM #formal_name Homo sapiens #common_name man DATE 17-Aug-1992 #sequence_revision 01-Dec-1995 #text_change 08-Dec-2000 ACCESSIONS JH0610; JS0693; A38608; S01331; A32419; S11147; S38863; !1S41251; S17042; S42730; I37175 REFERENCE JH0610 !$#authors Sharief, F.S.; Li, S.S.L. !$#journal Biochem. Biophys. Res. Commun. (1992) 184:1468-1476 !$#title Structure of human prostatic acid phosphatase gene. !$#cross-references MUID:92272747; PMID:1375464 !$#accession JH0610 !'##molecule_type DNA !'##residues 1-386 ##label SHA !'##cross-references GB:M97580; GB:M97581; GB:M97582; GB:M97583; !1GB:M97584; GB:M97585; GB:M97586; GB:M97587; GB:M97588 !$#accession JS0693 !'##molecule_type mRNA !'##residues 1-386 ##label SH3 !'##cross-references GB:M97589; NID:g189611; PIDN:AAA60021.1; !1PID:g189613 REFERENCE A38608 !$#authors Van Etten, R.L.; Davidson, R.; Stevis, P.E.; MacArthur, H.; !1Moore, D.L. !$#journal J. Biol. Chem. (1991) 266:2313-2319 !$#title Covalent structure, disulfide bonding, and identification of !1reactive surface and active site residues of human prostatic !1acid phosphatase. !$#cross-references MUID:91115848; PMID:1989985 !$#accession A38608 !'##molecule_type mRNA !'##residues 1-386 ##label VAN !'##cross-references GB:M34840; NID:g189620; PIDN:AAA69694.1; !1PID:g189621 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing; disulfide !1bonds were determined by mass spectrographic analysis REFERENCE S01331 !$#authors Vihko, P.; Virkkunen, P.; Henttu, P.; Roiko, K.; Solin, T.; !1Huhtala, M.L. !$#journal FEBS Lett. (1988) 236:275-281 !$#title Molecular cloning and sequence analysis of cDNA encoding !1human prostatic acid phosphatase. !$#cross-references MUID:88312981; PMID:2842184 !$#accession S01331 !'##molecule_type mRNA !'##residues 1-14,'A',16,'ASC',20,'CF',23,'C',25-65,'WIWPTHPA',74-211, !1'A',213-386 ##label VIH !'##cross-references EMBL:X52174; NID:g28321; PIDN:CAA36422.1; !1PID:g28322 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE A32419 !$#authors Sharief, F.S.; Lee, H.; Leuderman, M.M.; Lundwall, A.; !1Deaven, L.L.; Lee, C.; Li, S.S.L. !$#journal Biochem. Biophys. Res. Commun. (1989) 160:79-86 !$#title Human prostatic acid phosphatase: cDNA cloning, gene mapping !1and protein sequence homology with lysosomal acid !1phosphatase. !$#cross-references MUID:89228054; PMID:2712834 !$#accession A32419 !'##molecule_type mRNA !'##residues 1-14,'A',16,'ASC',20,'CF',23,'C',25-94,'D',96-115,'R', !1117-214,'S',216-293,'T',295-371,'V',373-386 ##label SH2 !'##cross-references GB:M24902; NID:g189618; PIDN:AAA60022.1; !1PID:g189619 !'##note the authors translated the codons GAC for residue 95 as Glu, !1CGT for residue 116 as Ala, TCT for residue 215 as Cys, and !1ACT for residue 294 as Ser REFERENCE S11147 !$#authors Tailor, P.G.; Govindan, M.V.; Patel, P.C. !$#journal Nucleic Acids Res. (1990) 18:4928 !$#title Nucleotide sequence of human prostatic acid phosphatase !1determined from a full-length cDNA clone. !$#cross-references MUID:90370491; PMID:2395659 !$#accession S11147 !'##status preliminary; translation not shown !'##molecule_type mRNA !'##residues 1-14,'AFASC',20,'CF',23,'C',25-45,'H',47-65,'RIWPTHPA', !174-138,'E',140-156,'R',158-382,'N',384-386 ##label TAI !'##cross-references EMBL:X53605; NID:g35683; PIDN:CAA37673.1; !1PID:g35684 REFERENCE S38863 !$#authors Banas, B.; Blaschke, D.; Fittler, F.; Hoerz, W. !$#submission submitted to the EMBL Data Library, April 1993 !$#description Characterization of the promoter of the human prostatic acid !1phosphatase gene. !$#accession S38863 !'##molecule_type DNA !'##residues 1-40 ##label BAN !'##cross-references EMBL:X71391; NID:g416530; PIDN:CAA50514.1; !1PID:g416531 REFERENCE S41251 !$#authors Virkkunen, P.H.; Hedberg, P.; Palvimo, J.J.; Birr, E.; !1Porvari, K.; Taavitsainen, P.; Ruokonen, M.; Jonne, O.A.; !1Vihko, P. !$#submission submitted to the EMBL Data Library, September 1993 !$#description Structural organization of human and rat prostate-specific !1acid phosphatase genes and their promoters: identification !1of putative androgen response elements in both promoters and !1alu sequence in the human gene promoter. !$#accession S41251 !'##molecule_type DNA !'##residues 1-40 ##label VIR !'##cross-references EMBL:X74961; NID:g439657; PIDN:CAA52913.1; !1PID:g439658 REFERENCE S17042 !$#authors Lee, H.; Chu, T.M.; Li, S.S.L.; Lee, C. !$#journal Biochem. J. (1991) 277:759-765 !$#title Homodimer and heterodimer subunits of human prostate acid !1phosphatase. !$#cross-references MUID:91336999; PMID:1908222 !$#accession S17042 !'##status preliminary !'##molecule_type protein !'##residues 33-49 ##label LEE REFERENCE S42730 !$#authors Banas, B.; Blaschke, D.; Fittler, F.; Hoerz, W. !$#journal Biochim. Biophys. Acta (1994) 1217:188-194 !$#title Analysis of the promoter of the human prostatic acid !1phosphatase gene. !$#cross-references MUID:94153995; PMID:8110833 !$#accession S42730 !'##status preliminary !'##molecule_type DNA !'##residues 1-40 ##label BA2 !'##cross-references GB:X71391; NID:g416530; PIDN:CAA50514.1; !1PID:g416531 REFERENCE I37175 !$#authors Sharief, F.S.; Li, S.S. !$#journal Biochem. Mol. Biol. Int. (1994) 33:561-565 !$#title Nucleotide sequence of human prostatic acid phosphatase ACPP !1gene. !$#cross-references MUID:95038536; PMID:7951074 !$#accession I37175 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-386 ##label RES !'##cross-references EMBL:U07097; NID:g515995; PIDN:AAB60640.1; !1PID:g515997 COMMENT This protein is synthesized under androgen regulation by !1epithelial cells of the prostate and secreted into seminal !1fluid. GENETICS !$#gene GDB:ACPP !'##cross-references GDB:119644; OMIM:171790 !$#map_position 3q21.3-3q25.2 !$#introns 40/3; 72/3; 101/3; 152/3; 185/3; 216/3; 260/3; 288/3; 323/2 FUNCTION !$#description catalyzes the hydrolysis of a wide range of phosphate esters CLASSIFICATION #superfamily mammalian acid phosphatase KEYWORDS glycoprotein; phosphohistidine; phosphoprotein; phosphoric !1monoester hydrolase FEATURE !$1-32 #domain signal sequence #status predicted #label SIG\ !$33-386 #product acid phosphatase ACPP #status experimental !8#label MAT\ !$43,86 #active_site Arg #status predicted\ !$44 #active_site His (phosphohistidine intermediate) !8#status predicted\ !$94,220,333 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$161-372,215-313, !$347-351 #disulfide_bonds #status experimental SUMMARY #length 386 #molecular-weight 44566 #checksum 2327 SEQUENCE /// ENTRY S06167 #type complete TITLE acid phosphatase (EC 3.1.3.2) ACP2 precursor [validated] - human ALTERNATE_NAMES acid phosphatase, lysosomal ORGANISM #formal_name Homo sapiens #common_name man DATE 04-Dec-1992 #sequence_revision 01-Dec-1995 #text_change 08-Dec-2000 ACCESSIONS S06167; S05525; S01155 REFERENCE S06167 !$#authors von Figura, K. !$#submission submitted to the EMBL Data Library, June 1989 !$#accession S06167 !'##molecule_type DNA !'##residues 1-423 ##label VON !'##cross-references EMBL:X15525; NID:g34239; PIDN:CAA33542.1; !1PID:g1199524 REFERENCE S05525 !$#authors Geier, C.; von Figura, K.; Pohlmann, R. !$#journal Eur. J. Biochem. (1989) 183:611-616 !$#title Structure of the human lysosomal acid phosphatase gene. !$#cross-references MUID:89377828; PMID:2776754 !$#accession S05525 !'##molecule_type DNA !'##residues 1-29 ##label GEI REFERENCE S01155 !$#authors Pohlmann, R.; Krentler, C.; Schmidt, B.; Schroeder, W.; !1Lorkowski, G.; Culley, J.; Mersmann, G.; Geier, C.; Waheed, !1A.; Gottschalk, S.; Grzeschik, K.H.; Hasilik, A.; von !1Figura, K. !$#journal EMBO J. (1988) 7:2343-2350 !$#title Human lysosomal acid phosphatase: cloning, expression and !1chromosomal assignment. !$#cross-references MUID:89052645; PMID:3191910 !$#accession S01155 !'##molecule_type mRNA !'##residues 1-423 ##label POH !'##cross-references EMBL:X12548; NID:g34262; PIDN:CAA31064.1; !1PID:g34263 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing GENETICS !$#gene GDB:ACP2 !'##cross-references GDB:118963; OMIM:171650 !$#map_position 11p11.2-11p11.11 !$#introns 38/3; 70/3; 99/3; 150/3; 183/3; 213/3; 258/1; 285/3; 321/2; !1380/1 FUNCTION !$#description catalyzes the hydrolysis of a wide range of phosphate esters CLASSIFICATION #superfamily mammalian acid phosphatase KEYWORDS glycoprotein; phosphohistidine; phosphoprotein; phosphoric !1monoester hydrolase FEATURE !$1-30 #domain signal sequence #status predicted #label SIG\ !$31-423 #product acid phosphatase ACP2 #status experimental !8#label MAT\ !$41 #active_site Arg #status predicted\ !$42 #active_site His (phosphohistidine intermediate) !8#status predicted\ !$92,133,167,177,191, !$267,322,331 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$159-370,212-310, !$345-349 #disulfide_bonds #status predicted SUMMARY #length 423 #molecular-weight 48344 #checksum 8204 SEQUENCE /// ENTRY PAOFCS #type complete TITLE acid phosphatase (EC 3.1.3.2) - Providencia stuartii ORGANISM #formal_name Providencia stuartii DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 03-Mar-2000 ACCESSIONS S19888 REFERENCE S19888 !$#authors Riccio, M.L.; Lombardi, G.; Chiesurin, A.; Satta, G. !$#submission submitted to the EMBL Data Library, February 1992 !$#accession S19888 !'##molecule_type DNA !'##residues 1-248 ##label RIC !'##cross-references EMBL:X64820; NID:g45861; PIDN:CAA46032.1; !1PID:g45862 GENETICS !$#gene phoN CLASSIFICATION #superfamily acid phosphatase; glucose-6-phosphatase !1catalytic domain homology KEYWORDS phosphoric monoester hydrolase FEATURE !$109-222 #domain glucose-6-phosphatase catalytic domain !8homology #label GPH SUMMARY #length 248 #molecular-weight 27043 #checksum 4950 SEQUENCE /// ENTRY S19187 #type complete TITLE acid phosphatase (EC 3.1.3.2) - Morganella morganii ORGANISM #formal_name Morganella morganii DATE 28-Jan-2000 #sequence_revision 28-Jan-2000 #text_change 03-Mar-2000 ACCESSIONS S19187 REFERENCE S19187 !$#authors Thaller, M.C.; Berlutti, F.; Schippa, S.; Rossolini, G.M. !$#submission submitted to the EMBL Data Library, February 1992 !$#description Sequencing the Morganella morgannii phoC gene coding for a !1periplasmic acid phosphatase: a new member of a conserved !1family of bacterial acid phosphatases. !$#accession S19187 !'##molecule_type DNA !'##residues 1-249 ##label THA !'##cross-references EMBL:X64444; NID:g44463; PIDN:CAA45774.1; !1PID:g44464 CLASSIFICATION #superfamily acid phosphatase; glucose-6-phosphatase !1catalytic domain homology KEYWORDS phosphoric monoester hydrolase FEATURE !$109-222 #domain glucose-6-phosphatase catalytic domain !8homology #label GPH SUMMARY #length 249 #molecular-weight 26998 #checksum 9811 SEQUENCE /// ENTRY A32044 #type complete TITLE acid phosphatase (EC 3.1.3.2) - Zymomonas mobilis ORGANISM #formal_name Zymomonas mobilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS A32044 REFERENCE A32044 !$#authors Pond, J.L.; Eddy, C.K.; Mackenzie, K.F.; Conway, T.; !1Borecky, D.J.; Ingram, L.O. !$#journal J. Bacteriol. (1989) 171:767-774 !$#title Cloning, sequencing, and characterization of the principal !1acid phosphatase, the phoC(+) product, from Zymomonas !1mobilis. !$#cross-references MUID:89123152; PMID:2914872 !$#accession A32044 !'##status preliminary !'##molecule_type DNA !'##residues 1-264 ##label PON !'##cross-references GB:M24141; NID:g155613; PIDN:AAA27700.1; !1PID:g155614 CLASSIFICATION #superfamily acid phosphatase; glucose-6-phosphatase !1catalytic domain homology KEYWORDS phosphoric monoester hydrolase FEATURE !$99-212 #domain glucose-6-phosphatase catalytic domain !8homology #label GPH SUMMARY #length 264 #molecular-weight 28989 #checksum 9361 SEQUENCE /// ENTRY A41330 #type complete TITLE acid phosphatase (EC 3.1.3.2) PhoN precursor - Salmonella typhimurium ALTERNATE_NAMES glycerophosphatase; nonspecific acid phosphatase; phosphomonoesterase ORGANISM #formal_name Salmonella typhimurium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS S20958; A41330; S14515; S18926 REFERENCE S20958 !$#authors Groisman, E.A.; Saier Jr., M.H.; Ochman, H. !$#journal EMBO J. (1992) 11:1309-1316 !$#title Horizontal transfer of a phosphatase gene as evidence for !1mosaic structure of the Salmonella genome. !$#cross-references MUID:92224869; PMID:1339343 !$#accession S20958 !'##molecule_type DNA !'##residues 1-250 ##label GRO !'##cross-references EMBL:X63599; NID:g47823; PIDN:CAA45144.1; !1PID:g47824 REFERENCE A41330 !$#authors Kasahara, M.; Nakata, A.; Shinagawa, H. !$#journal J. Bacteriol. (1991) 173:6760-6765 !$#title Molecular analysis of the Salmonella typhimurium phoN gene, !1which encodes nonspecific acid phosphatase. !$#cross-references MUID:92041557; PMID:1938882 !$#accession A41330 !'##molecule_type DNA !'##residues 1-228,'SVRS' ##label KAS !'##cross-references GB:X59036; NID:g48894; PIDN:CAA41760.1; PID:g48895 GENETICS !$#gene phoN !$#map_position 96 min !$#note regulated by the two-component regulatory system consisting !1of phoP and phoQ CLASSIFICATION #superfamily acid phosphatase; glucose-6-phosphatase !1catalytic domain homology KEYWORDS periplasmic space; phosphoric monoester hydrolase FEATURE !$108-221 #domain glucose-6-phosphatase catalytic domain !8homology #label GPH SUMMARY #length 250 #molecular-weight 28382 #checksum 6228 SEQUENCE /// ENTRY S15752 #type complete TITLE acid phosphatase (EC 3.1.3.2) ACP5 precursor - human ALTERNATE_NAMES purple acid phosphatase (PAP); tartrate-resistant acid phosphatase; uteroferrin ORGANISM #formal_name Homo sapiens #common_name man DATE 04-Dec-1992 #sequence_revision 01-Dec-1995 #text_change 03-Mar-2000 ACCESSIONS S15752; A31812; PN0621; S05251; A49133; A34638; B33781; !1A33781; B49133; C49133; S05255; S08027 REFERENCE S15752 !$#authors Lord, D.K.; Cross, N.C.P.; Bevilacqua, M.A.; Rider, S.H.; !1Gorman, P.A.; Groves, A.V.; Moss, D.W.; Sheer, D.; Cox, T.M. !$#journal Eur. J. Biochem. (1990) 189:287-293 !$#title Type 5 acid phosphatase. Sequence, expression and !1chromosomal localization of a differentiation-associated !1protein of the human macrophage. !$#cross-references MUID:90249371; PMID:2338077 !$#accession S15752 !'##molecule_type mRNA !'##residues 1-325 ##label LOR !'##cross-references EMBL:X14618; NID:g34733; PIDN:CAA32771.1; !1PID:g34734 !'##experimental_source placenta REFERENCE A31812 !$#authors Ketcham, C.M.; Roberts, R.M.; Simmen, R.C.M.; Nick, H.S. !$#journal J. Biol. Chem. (1989) 264:557-563 !$#title Molecular cloning of the type 5, iron-containing, !1tartrate-resistant acid phosphatase from human placenta. !$#cross-references MUID:89079710; PMID:2909539 !$#accession A31812 !'##molecule_type mRNA !'##residues 1-44,'GP',47-176,'LT',181-325 ##label KET !'##cross-references GB:J04430; GB:M19534; NID:g178005; PIDN:AAA76849.1; !1PID:g178006 !'##experimental_source placenta REFERENCE JN0787 !$#authors Cassady, A.I.; King, A.G.; Cross, N.C.P.; Hume, D.A. !$#journal Gene (1993) 130:201-207 !$#title Isolation and characterization of the genes encoding mouse !1and human type-5 acid phosphatase. !$#cross-references MUID:93366175; PMID:8359686 !$#accession PN0621 !'##molecule_type DNA !'##residues 1-245 ##label CAS !'##cross-references GB:X67123 REFERENCE S05251 !$#authors Hayman, A.R.; Warburton, M.J.; Pringle, J.A.S.; Coles, B.; !1Chambers, T.J. !$#journal Biochem. J. (1989) 261:601-609 !$#title Purification and characterization of a tartrate-resistant !1acid phosphatase from human osteoclastomas. !$#cross-references MUID:89374163; PMID:2775236 !$#accession S05251 !'##molecule_type protein !'##residues 22-46,'Q',48-49,'W',51-64;183-201,'A' ##label HAY !'##experimental_source osteclastoma REFERENCE A49133 !$#authors Janckila, A.J.; Latham, M.D.; Lam, K.W.; Chow, K.C.; Li, !1C.Y.; Yam, L.T. !$#journal Clin. Biochem. (1992) 25:437-443 !$#title Heterogeneity of hairy cell tartrate-resistant acid !1phosphatase. !$#cross-references MUID:93121546; PMID:1477968 !$#accession A49133 !'##molecule_type protein !'##residues 22-46,'G',48-49,'X',51-55;183-203 ##label JA4 !'##experimental_source spleen !'##note sequence modified after extraction from NCBI backbone REFERENCE A34638 !$#authors Stepan, J.J.; Lau, K.H.W.; Mohan, S.; Singer, F.R.; Baylink, !1D.J. !$#journal Biochem. Biophys. Res. Commun. (1990) 168:792-800 !$#title Purification and N-terminal amino acid sequence of the !1tartrate-resistant acid phosphatase from human !1osteoclastoma: evidence for a single structure. !$#cross-references MUID:90241255; PMID:2334436 !$#accession A34638 !'##molecule_type protein !'##residues 22-31 ##label STE !'##experimental_source osteoclastoma REFERENCE A33781 !$#authors Stepan, J.J.; Lau, K.H.W.; Mohan, S.; Kraenzlin, M.; !1Baylink, D.J. !$#journal Biochem. Biophys. Res. Commun. (1989) 165:1027-1034 !$#title Purification and N-terminal sequence of two !1tartrate-resistant acid phosphatases type-5 from the hairy !1cell leukemia spleen. !$#cross-references MUID:90121201; PMID:2610679 !$#accession B33781 !'##molecule_type protein !'##residues 22-33,'X',35-37 ##label ST3 !'##experimental_source hairy cell leukemia spleen COMMENT This enzyme contains a catalytically active binuclear iron !1complex at its active site, and also functions as a carrier !1of iron from the uterine endometrium to the fetus during !1pregnancy. GENETICS !$#gene GDB:ACP5; T5AP !'##cross-references GDB:118747; OMIM:171640 !$#map_position 19p13.3-19p13.2 !$#introns 87/3; 130/3 FUNCTION !$#description catalyzes the hydrolysis of a wide range of phosphate esters CLASSIFICATION #superfamily tartrate-resistant acid phosphatase; !1phosphoesterase core homology KEYWORDS blocked amino end; glycoprotein; iron; metalloprotein; !1phosphoric monoester hydrolase FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-182,183-325 #product acid phosphatase ACP5 #status predicted !8#label MAT\ !$22-182 #domain acid phosphatase ACP5 chain B #status !8predicted #label CHB\ !$27-112 #domain phosphoesterase core homology #label PEC\ !$183-325 #domain acid phosphatase ACP5 chain A #status !8predicted #label CHA\ !$33,71,74,242 #binding_site iron (Asp, Asp, Tyr, His) #status !8predicted\ !$71,110,205,240 #binding_site iron (Asp, Asn, His, His) #status !8predicted\ !$111,214 #active_site His #status predicted\ !$116,147 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$161-219 #disulfide_bonds #status predicted\ !$183 #modified_site blocked amino end (Thr) (in mature !8form) (partial) #status experimental\ !$238 #disulfide_bonds interchain (in dimeric form) #status !8predicted SUMMARY #length 325 #molecular-weight 36598 #checksum 5625 SEQUENCE /// ENTRY JN0787 #type complete TITLE acid phosphatase (EC 3.1.3.2) 5 precursor - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 24-Feb-1994 #sequence_revision 24-Feb-1994 #text_change 03-Mar-2000 ACCESSIONS JN0787; I55486; I55533 REFERENCE JN0787 !$#authors Cassady, A.I.; King, A.G.; Cross, N.C.P.; Hume, D.A. !$#journal Gene (1993) 130:201-207 !$#title Isolation and characterization of the genes encoding mouse !1and human type-5 acid phosphatase. !$#cross-references MUID:93366175; PMID:8359686 !$#accession JN0787 !'##molecule_type DNA !'##residues 1-327 ##label CAS !'##cross-references GB:M99054; NID:g553868; PIDN:AAA37245.1; !1PID:g191988 REFERENCE I55486 !$#authors Reddy, S.V.; Scarcez, T.; Windle, J.J.; Leach, R.J.; !1Hundley, J.E.; Chirgwin, J.M.; Roodman, G.D. !$#journal J. Bone Miner. Res. (1993) 8:1263-1270 !$#title Cloning and characterization of the 5'-flanking region of !1the mouse tartrate-resistant acid phosphatase (TRAP) gene. !$#cross-references MUID:94078828; PMID:8256664 !$#accession I55486 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-48 ##label RED !'##cross-references GB:M85212; NID:g202147; PIDN:AAA40479.1; !1PID:g554391 REFERENCE I55533 !$#authors Lacey, D.L.; Erdmann, J.M.; Tan, H.L. !$#journal J. Cell. Biochem. (1994) 54:365-371 !$#title Interleukin 4 increases type 5 acid phosphatase mRNA !1expression in murine bone marrow macrophages. !$#cross-references MUID:94259726; PMID:8200916 !$#accession I55533 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 'N',85-193 ##label LAC !'##cross-references GB:S70805; NID:g546967; PIDN:AAB30889.1; !1PID:g546968 GENETICS !$#gene T5AP; TRAP !$#introns 89/3; 132/3; 247/3 FUNCTION !$#description catalyzes the hydrolysis of a wide range of phosphate esters !$#note also functions as a carrier of iron from the uterine !1endometrium to the fetus during pregnancy !$#note this class of phosphatase has optimal activity at acid pH !1and is resistant to L(+)-tartrate inhibition CLASSIFICATION #superfamily tartrate-resistant acid phosphatase; !1phosphoesterase core homology KEYWORDS blocked amino end; disulfide bond; glycoprotein; iron; !1metalloprotein; phosphoric monoester hydrolase FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-184,185-327 #product acid phosphatase 5 #status predicted #label !8MAT\ !$22-184 #domain acid phosphatase 5 chain B #status predicted !8#label CHB\ !$29-114 #domain phosphoesterase core homology #label PEC\ !$85-89 #region endosomal/lysosomal sorting sequence\ !$185-327 #domain acid phosphatase 5 chain A #status predicted !8#label CHA\ !$35,73,76,244 #binding_site iron (Asp, Asp, Tyr, His) #status !8predicted\ !$73,112,207,242 #binding_site iron (Asp, Asn, His, His) #status !8predicted\ !$113,216 #active_site His #status predicted\ !$118,149 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$163-221 #disulfide_bonds #status predicted\ !$185 #modified_site blocked amino end (Thr) (in mature !8form) (partial) #status experimental\ !$240 #disulfide_bonds interchain (in dimeric form) #status !8predicted SUMMARY #length 327 #molecular-weight 36807 #checksum 837 SEQUENCE /// ENTRY A41720 #type complete TITLE acid phosphatase (EC 3.1.3.2) 5 precursor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A41720 REFERENCE A41720 !$#authors Ek-Rylander, B.; Bill, P.; Norgard, M.; Nilsson, S.; !1Andersson, G. !$#journal J. Biol. Chem. (1991) 266:24684-24689 !$#title Cloning, sequence, and developmental expression of a type 5, !1tartrate-resistant, acid phosphatase of rat bone. !$#cross-references MUID:92105136; PMID:1722212 !$#accession A41720 !'##status preliminary !'##molecule_type mRNA !'##residues 1-327 ##label EKA !'##cross-references GB:M76110; NID:g207543; PIDN:AAA42305.1; !1PID:g207544 CLASSIFICATION #superfamily tartrate-resistant acid phosphatase; !1phosphoesterase core homology KEYWORDS phosphoric monoester hydrolase FEATURE !$29-114 #domain phosphoesterase core homology #label PEC SUMMARY #length 327 #molecular-weight 36726 #checksum 1370 SEQUENCE /// ENTRY A46096 #type complete TITLE acid phosphatase (EC 3.1.3.2) 5 precursor - pig ALTERNATE_NAMES uteroferrin precursor ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A46096; A33318; A40928; B40928; A27035 REFERENCE A46096 !$#authors Ling, P.; Roberts, R.M. !$#journal J. Biol. Chem. (1993) 268:6896-6902 !$#title Uteroferrin and intracellular tartrate-resistant acid !1phosphatases are the products of the same gene. !$#cross-references MUID:93216620; PMID:8463220 !$#accession A46096 !'##status preliminary; translation not shown !'##molecule_type mRNA !'##residues 1-340 ##label LIN !'##cross-references GB:M98553; NID:g164696; PIDN:AAA31129.1; !1PID:g164697 REFERENCE A33318 !$#authors Simmen, R.C.M.; Srinivas, V.; Roberts, R.M. !$#journal DNA (1989) 8:543-554 !$#title cDNA sequence, gene organization, and progesterone induction !1of mRNA for uteroferrin, a porcine uterine iron transport !1protein. !$#cross-references MUID:90091741; PMID:2598770 !$#accession A33318 !'##status preliminary !'##molecule_type mRNA !'##residues 1-182,185-340 ##label SIM !'##cross-references GB:M30284; NID:g164719; PIDN:AAA31139.1; !1PID:g164720 !'##note the authors translated the codon CAG for residue 95 as Glu, and !1CTG for residue 163 as Lys REFERENCE A40928 !$#authors Simmen, R.C.M.; Baumbach, G.A.; Roberts, R.M. !$#journal Mol. Endocrinol. (1988) 2:253-262 !$#title Molecular cloning and temporal expression during pregnancy !1of the messenger ribonucleic acid encoding uteroferrin, a !1progesterone-induced uterine secretory protein. !$#cross-references MUID:88288243; PMID:2969454 !$#accession A40928 !'##molecule_type mRNA !'##residues 186-215;247-301 ##label SI2 !'##cross-references GB:M31214; GB:M31215 !$#accession B40928 !'##molecule_type mRNA !'##residues 292-297,'K',299,'G',301 ##label SI1 !'##cross-references GB:M31216 !'##note the authors translated the codon TTG for residue 6 as Phe REFERENCE A90131 !$#authors Hunt, D.F.; Yates III, J.R.; Shabanowitz, J.; Zhu, N.Z.; !1Zirino, T.; Averill, B.A.; Daurat-Larroque, S.T.; Shewale, !1J.G.; Roberts, R.M.; Brew, K. !$#journal Biochem. Biophys. Res. Commun. (1987) 144:1154-1160 !$#title Sequence homology in the metalloproteins; purple acid !1phosphatase from beef spleen and uteroferrin from porcine !1uterus. !$#cross-references MUID:87213307; PMID:3579955 !$#accession A27035 !'##molecule_type protein !'##residues 28-131,'KKILKRX',132-153,'PRX',161-182,185-245,'Q',247-256, !1264-336 ##label HUN CLASSIFICATION #superfamily tartrate-resistant acid phosphatase; !1phosphoesterase core homology KEYWORDS iron; phosphoric monoester hydrolase FEATURE !$35-120 #domain phosphoesterase core homology #label PEC SUMMARY #length 340 #molecular-weight 38011 #checksum 9834 SEQUENCE /// ENTRY B27035 #type complete TITLE acid phosphatase (EC 3.1.3.2) 5 - bovine ALTERNATE_NAMES purple acid phosphatase (PAP) ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B27035 REFERENCE A90131 !$#authors Hunt, D.F.; Yates III, J.R.; Shabanowitz, J.; Zhu, N.Z.; !1Zirino, T.; Averill, B.A.; Daurat-Larroque, S.T.; Shewale, !1J.G.; Roberts, R.M.; Brew, K. !$#journal Biochem. Biophys. Res. Commun. (1987) 144:1154-1160 !$#title Sequence homology in the metalloproteins; purple acid !1phosphatase from beef spleen and uteroferrin from porcine !1uterus. !$#cross-references MUID:87213307; PMID:3579955 !$#accession B27035 !'##molecule_type protein !'##residues 1-273 ##label HUN CLASSIFICATION #superfamily tartrate-resistant acid phosphatase; !1phosphoesterase core homology KEYWORDS iron; phosphoric monoester hydrolase FEATURE !$7-78 #domain phosphoesterase core homology #label PEC SUMMARY #length 273 #molecular-weight 30365 #checksum 4978 SEQUENCE /// ENTRY H86381 #type complete TITLE probable acid phosphatase (EC 3.1.3.2) F4F7.38 precursor [similarity] - Arabidopsis thaliana ALTERNATE_NAMES purple acid phosphatase ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 02-Mar-2001 #sequence_revision 02-Mar-2001 #text_change 02-Nov-2001 ACCESSIONS H86381 REFERENCE A86141 !$#authors Theologis, A.; Ecker, J.R.; Palm, C.J.; Federspiel, N.A.; !1Kaul, S.; White, O.; Alonso, J.; Altaf, H.; Araujo, R.; !1Bowman, C.L.; Brooks, S.Y.; Buehler, E.; Chan, A.; Chao, Q.; !1Chen, H.; Cheuk, R.F.; Chin, C.W.; Chung, M.K.; Conn, L.; !1Conway, A.B.; Conway, A.R.; Creasy, T.H.; Dewar, K.; Dunn, !1P.; Etgu, P.; Feldblyum, T.V.; Feng, J.; Fong, B.; Fujii, !1C.Y.; Gill, J.E.; Goldsmith, A.D.; Haas, B.; Hansen, N.F.; !1Hughes, B.; Huizar, L.; Hunter, J.L.; Jenkins, J.; !1Johnson-Hopson, C.; Khan, S.; Khaykin, E.; Kim, C.J.; Koo, !1H.L.; Kremenetskaia, I.; Kurtz, D.B.; Kwan, A.; Lam, B.; !1Langin-Hooper, S.; Lee, A.; Lee, J.M.; Lenz, C.A.; Li, J.H.; !1Li, Y.; Lin, X.; Liu, S.X.; Liu, Z.A.; Luros, J.S.; Maiti, !1R.; Marziali, A.; Militscher, J.; Miranda, M.; Nguyen, M.; !1Nierman, W.C.; Osborne, B.I.; Pai, G.; Peterson, J.; Pham, !1P.K.; Rizzo, M.; Rooney, T.; Rowley, D.; Sakano, H.; !1Salzberg, S.L.; Schwartz, J.R.; Shinn, P.; Southwick, A.M.; !1Sun, H.; Tallon, L.J.; Tambunga, G.; Toriumi, M.J.; Town, !1C.D.; Utterback, T.; van Aken, S.; Vaysberg, M.; Vysotskaia, !1V.S.; Walker, M.; Wu, D.; Yu, G.; Fraser, C.M.; Venter, !1J.C.; Davis, R.W. !$#journal Nature (2000) 408:816-820 !$#title Sequence and analysis of chromosome 1 of the plant !1Arabidopsis. !$#cross-references MUID:21016719; PMID:11130712 !$#accession H86381 !'##molecule_type DNA !'##residues 1-333 ##label STO !'##cross-references GB:AE005172; NID:g11067287; PIDN:AAG28815.1; !1GSPDB:GN00141 GENETICS !$#gene F4F7.38 !$#map_position 1 CLASSIFICATION #superfamily tartrate-resistant acid phosphatase; !1phosphoesterase core homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase FEATURE !$1-31 #domain signal sequence #status predicted #label SIG\ !$32-333 #product acid phosphatase #status predicted #label !8MAT\ !$47-120 #domain phosphoesterase core homology #label PEC\ !$53,80,83,249 #binding_site iron (Asp, Asp, Tyr, His) #status !8predicted\ !$80,118,212,247 #binding_site iron (Asp, Asn, His, His) #status !8predicted\ !$119,221 #active_site His #status predicted SUMMARY #length 333 #molecular-weight 37597 #checksum 4256 SEQUENCE /// ENTRY D86281 #type complete TITLE probable acid phosphatase (EC 3.1.3.2) F10B6.10 precursor [similarity] - Arabidopsis thaliana ALTERNATE_NAMES purple acid phosphatase ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 02-Mar-2001 #sequence_revision 02-Mar-2001 #text_change 02-Nov-2001 ACCESSIONS D86281 REFERENCE A86141 !$#authors Theologis, A.; Ecker, J.R.; Palm, C.J.; Federspiel, N.A.; !1Kaul, S.; White, O.; Alonso, J.; Altaf, H.; Araujo, R.; !1Bowman, C.L.; Brooks, S.Y.; Buehler, E.; Chan, A.; Chao, Q.; !1Chen, H.; Cheuk, R.F.; Chin, C.W.; Chung, M.K.; Conn, L.; !1Conway, A.B.; Conway, A.R.; Creasy, T.H.; Dewar, K.; Dunn, !1P.; Etgu, P.; Feldblyum, T.V.; Feng, J.; Fong, B.; Fujii, !1C.Y.; Gill, J.E.; Goldsmith, A.D.; Haas, B.; Hansen, N.F.; !1Hughes, B.; Huizar, L.; Hunter, J.L.; Jenkins, J.; !1Johnson-Hopson, C.; Khan, S.; Khaykin, E.; Kim, C.J.; Koo, !1H.L.; Kremenetskaia, I.; Kurtz, D.B.; Kwan, A.; Lam, B.; !1Langin-Hooper, S.; Lee, A.; Lee, J.M.; Lenz, C.A.; Li, J.H.; !1Li, Y.; Lin, X.; Liu, S.X.; Liu, Z.A.; Luros, J.S.; Maiti, !1R.; Marziali, A.; Militscher, J.; Miranda, M.; Nguyen, M.; !1Nierman, W.C.; Osborne, B.I.; Pai, G.; Peterson, J.; Pham, !1P.K.; Rizzo, M.; Rooney, T.; Rowley, D.; Sakano, H.; !1Salzberg, S.L.; Schwartz, J.R.; Shinn, P.; Southwick, A.M.; !1Sun, H.; Tallon, L.J.; Tambunga, G.; Toriumi, M.J.; Town, !1C.D.; Utterback, T.; van Aken, S.; Vaysberg, M.; Vysotskaia, !1V.S.; Walker, M.; Wu, D.; Yu, G.; Fraser, C.M.; Venter, !1J.C.; Davis, R.W. !$#journal Nature (2000) 408:816-820 !$#title Sequence and analysis of chromosome 1 of the plant !1Arabidopsis. !$#cross-references MUID:21016719; PMID:11130712 !$#accession D86281 !'##molecule_type DNA !'##residues 1-364 ##label STO !'##cross-references GB:AE005172; NID:g8778212; PIDN:AAF79221.1; !1GSPDB:GN00141 GENETICS !$#gene F10B6.10 !$#map_position 1 CLASSIFICATION #superfamily tartrate-resistant acid phosphatase; !1phosphoesterase core homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase FEATURE !$1-32 #domain signal sequence #status predicted #label SIG\ !$33-364 #product acid phosphatase #status predicted #label !8MAT\ !$75-152 #domain phosphoesterase core homology #label PEC\ !$81,114,117,281 #binding_site iron (Asp, Asp, Tyr, His) #status !8predicted\ !$114,150,244,279 #binding_site iron (Asp, Asn, His, His) #status !8predicted\ !$151,253 #active_site His #status predicted SUMMARY #length 364 #molecular-weight 41839 #checksum 825 SEQUENCE /// ENTRY D84430 #type complete TITLE probable acid phosphatase (EC 3.1.3.2) At2g01890 precursor [similarity] - Arabidopsis thaliana ALTERNATE_NAMES purple acid phosphatase ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 02-Feb-2001 #sequence_revision 02-Feb-2001 #text_change 02-Nov-2001 ACCESSIONS D84430 REFERENCE A84420 !$#authors Lin, X.; Kaul, S.; Rounsley, S.D.; Shea, T.P.; Benito, M.I.; !1Town, C.D.; Fujii, C.Y.; Mason, T.M.; Bowman, C.L.; !1Barnstead, M.E.; Feldblyum, T.V.; Buell, C.R.; Ketchum, !1K.A.; Lee, J.J.; Ronning, C.M.; Koo, H.; Moffat, K.S.; !1Cronin, L.A.; Shen, M.; VanAken, S.E.; Umayam, L.; Tallon, !1L.J.; Gill, J.E.; Adams, M.D.; Carrera, A.J.; Creasy, T.H.; !1Goodman, H.M.; Somerville, C.R.; Copenhaver, G.P.; Preuss, !1D.; Nierman, W.C.; White, O.; Eisen, J.A.; Salzberg, S.L.; !1Fraser, C.M.; Venter, J.C. !$#journal Nature (1999) 402:761-768 !$#title Sequence and analysis of chromosome 2 of the plant !1Arabidopsis thaliana. !$#cross-references MUID:20083487; PMID:10617197 !$#accession D84430 !'##molecule_type DNA !'##residues 1-351 ##label STO !'##cross-references GB:AE002093; NID:g4522012; PIDN:AAD21785.1; !1GSPDB:GN00139 GENETICS !$#gene At2g01890 !$#map_position 2 CLASSIFICATION #superfamily tartrate-resistant acid phosphatase; !1phosphoesterase core homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-351 #product acid phosphatase #status predicted #label !8MAT\ !$46-125 #domain phosphoesterase core homology #label PEC\ !$52,85,88,270 #binding_site iron (Asp, Asp, Tyr, His) #status !8predicted\ !$85,123,233,268 #binding_site iron (Asp, Asn, His, His) #status !8predicted\ !$124,242 #active_site His #status predicted SUMMARY #length 351 #molecular-weight 39998 #checksum 3926 SEQUENCE /// ENTRY C84430 #type complete TITLE probable acid phosphatase (EC 3.1.3.2) At2g01880 precursor [similarity] - Arabidopsis thaliana ALTERNATE_NAMES purple acid phosphatase ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 02-Feb-2001 #sequence_revision 02-Feb-2001 #text_change 02-Nov-2001 ACCESSIONS C84430 REFERENCE A84420 !$#authors Lin, X.; Kaul, S.; Rounsley, S.D.; Shea, T.P.; Benito, M.I.; !1Town, C.D.; Fujii, C.Y.; Mason, T.M.; Bowman, C.L.; !1Barnstead, M.E.; Feldblyum, T.V.; Buell, C.R.; Ketchum, !1K.A.; Lee, J.J.; Ronning, C.M.; Koo, H.; Moffat, K.S.; !1Cronin, L.A.; Shen, M.; VanAken, S.E.; Umayam, L.; Tallon, !1L.J.; Gill, J.E.; Adams, M.D.; Carrera, A.J.; Creasy, T.H.; !1Goodman, H.M.; Somerville, C.R.; Copenhaver, G.P.; Preuss, !1D.; Nierman, W.C.; White, O.; Eisen, J.A.; Salzberg, S.L.; !1Fraser, C.M.; Venter, J.C. !$#journal Nature (1999) 402:761-768 !$#title Sequence and analysis of chromosome 2 of the plant !1Arabidopsis thaliana. !$#cross-references MUID:20083487; PMID:10617197 !$#accession C84430 !'##molecule_type DNA !'##residues 1-304 ##label STO !'##cross-references GB:AE002093; NID:g4522007; PIDN:AAD21780.1; !1GSPDB:GN00139 GENETICS !$#gene At2g01880 !$#map_position 2 CLASSIFICATION #superfamily tartrate-resistant acid phosphatase; !1phosphoesterase core homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-304 #product acid phosphatase #status predicted #label !8MAT\ !$42-121 #domain phosphoesterase core homology #label PEC\ !$48,81,84,226 #binding_site iron (Asp, Asp, Tyr, His) #status !8predicted\ !$81,119,189,224 #binding_site iron (Asp, Asn, His, His) #status !8predicted\ !$120,198 #active_site His #status predicted SUMMARY #length 304 #molecular-weight 34541 #checksum 5986 SEQUENCE /// ENTRY S51031 #type complete TITLE acid phosphatase (EC 3.1.3.2) purple, precursor [validated] - kidney bean ALTERNATE_NAMES purple acid phosphatase (PAP) CONTAINS C10 protein; C9 protein ORGANISM #formal_name Phaseolus vulgaris #common_name kidney bean DATE 01-Aug-1995 #sequence_revision 18-Aug-2000 #text_change 24-Aug-2001 ACCESSIONS T51097; S51031; S51079; S51078 REFERENCE Z25295 !$#authors Vogel, A.; Schnittger, P.; Boerchers, T.; Krebs, B.; Spener, !1F. !$#submission submitted to the EMBL Data Library, August 1997 !$#description Cloning of the cDNA encoding purple acid phosphatase from !1red kidney bean. !$#accession T51097 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-459 ##label VOG !'##cross-references EMBL:AJ001270; NID:g2344870; PIDN:CAA04644.1; !1PID:g2344871 REFERENCE S51031 !$#authors Klabunde, T.; Stahl, B.; Suerbaum, H.; Hahner, S.; Karas, !1M.; Hillenkamp, F.; Krebs, B.; Witzel, H. !$#journal Eur. J. Biochem. (1994) 226:369-375 !$#title The amino acid sequence of the red kidney bean Fe(III)-Zn !1(II) purple acid phosphatase. Determination of the amino !1acid sequence by a combination of matrix-assisted laser !1desorption/ionization mass spectrometry and automated Edman !1sequencing. !$#cross-references MUID:95094794; PMID:8001554 !$#accession S51031 !'##molecule_type protein !'##residues 28-279,'HI',282-368,'D',370-459 ##label KLA1 !$#accession S51079 !'##molecule_type protein !'##residues 326-368,'D',370-399 ##label KLA2 !$#accession S51078 !'##molecule_type protein !'##residues 102-279,'HI',282-312 ##label KLA3 !'##note both the amino and carboxyl ends were subject to proteolytic !1processing REFERENCE A65943 !$#authors Klabunde, T.; Strater, N.; Krebs, B. !$#submission submitted to the Brookhaven Protein Data Bank, February 1995 !$#cross-references PDB:1KBP !$#contents annotation; X-ray crystallography, 2.9 angstroms, residues !136-368,'D',370-459 REFERENCE A67328 !$#authors Klabunde, T.; Strater, N.; Krebs, B. !$#submission submitted to the Brookhaven Protein Data Bank, October 1995 !$#cross-references PDB:3KBP !$#contents annotation; X-ray crystallography, 3.0 angstroms, residues !136-368,'D',370-459 REFERENCE A67350 !$#authors Klabunde, T.; Strater, N.; Krebs, B. !$#submission submitted to the Brookhaven Protein Data Bank, October 1995 !$#cross-references PDB:4KBP !$#contents annotation; X-ray crystallography, 2.7 angstroms, residues !136-368,'D',370-459 REFERENCE A56485 !$#authors Strater, N.; Klabunde, T.; Tucker, P.; Witzel, H.; Krebs, B. !$#journal Science (1995) 268:1489-1492 !$#title Crystal structure of a purple acid phosphatase containing a !1dinuclear Fe(III)-Zn(II) active site. !$#cross-references MUID:95288640; PMID:7770774 !$#contents annotation; X-ray crystallography, 2.9 angstroms REFERENCE A58726 !$#authors Klabunde, T.; Straeter, N.; Froelich, R.; Witzel, H.; Krebs, !1B. !$#journal J. Mol. Biol. (1996) 259:737-748 !$#title Mechanism of Fe(III)-Zn(II) purple acid phosphatase based on !1crystal structures. !$#cross-references MUID:96275658; PMID:8683579 !$#contents annotation; X-ray crystallography, 2.65 angstroms GENETICS !$#gene pap COMPLEX homodimer FUNCTION !$#description catalyzes the hydrolysis of phosphate monoesters CLASSIFICATION #superfamily kidney bean purple acid phosphatase; !1phosphoesterase core homology KEYWORDS glycoprotein; homodimer; iron; metalloprotein; phosphoric !1monoester hydrolase; zinc FEATURE !$1-27 #domain signal sequence and propeptide #status !8predicted #label PRO\ !$28-459 #product purple acid phosphatase #status experimental !8#label MAT\ !$156-230 #domain phosphoesterase core homology #label PEC\ !$108,136,170,238,423 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$162,191,194,352 #binding_site iron (Asp, Asp, Tyr, His) #status !8experimental\ !$191,228,313,350 #binding_site zinc (Asp, Asn, His, His) #status !8experimental\ !$229,322,323 #active_site His #status predicted\ !$285 #binding_site phosphate (Arg) #status predicted\ !$372 #disulfide_bonds interchain #status experimental SUMMARY #length 459 #molecular-weight 52856 #checksum 7093 SEQUENCE /// ENTRY A59200 #type complete TITLE acid phosphatase (EC 3.1.3.2) purple 1, precursor [validated] - sweet potato ALTERNATE_NAMES purple acid phosphatase (PAP) ORGANISM #formal_name Ipomoea batatas #common_name sweet potato DATE 24-Aug-2001 #sequence_revision 24-Aug-2001 #text_change 24-Aug-2001 ACCESSIONS A59200; C59200 REFERENCE Z25293 !$#authors Schenk, G.; Ge, Y.; Carrington, L.E.; Wynne, C.J.; Searle, !1I.R.; Carroll, B.J.; Hamilton, S.; de Jersey, J. !$#journal Arch. Biochem. Biophys. (1999) 370:183-189 !$#title Binuclear metal centers in plant purple acid phosphatases: !1Fe-Mn in sweet potato and Fe-Zn in soybean. !$#cross-references MUID:99441212; PMID:10510276 !$#accession A59200 !'##molecule_type mRNA !'##residues 1-473 ##label KUR !'##cross-references GB:AF200825; NID:g6635440; PIDN:AAF19821.1; !1PID:g6635441 !$#accession C59200 !'##molecule_type protein !'##residues 39-61 ##label KU2 COMMENT Metal content is iron and manganese, with small amounts of !1iron and copper. COMPLEX homodimer FUNCTION !$#description catalyzes the hydrolysis of phosphate monoesters [validated, !1MUID:99441212] !$#note active on a variety of activated and unactivated phosphate !1ester and anhydride substrates CLASSIFICATION #superfamily kidney bean purple acid phosphatase; !1phosphoesterase core homology KEYWORDS glycoprotein; homodimer; iron; manganese; metalloprotein; !1phosphoric monoester hydrolase FEATURE !$39-473 #product purple acid phosphatase #status experimental !8#label MAT\ !$166-240 #domain phosphoesterase core homology #label PEC\ !$118,180,311,433 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$172,201,204,362 #binding_site iron (Asp, Asp, Tyr, His) #status !8predicted\ !$201,238,323,360 #binding_site manganese (Asp, Asn, His, His) #status !8predicted\ !$239,333 #active_site His #status predicted\ !$382 #disulfide_bonds interchain #status predicted SUMMARY #length 473 #molecular-weight 53815 #checksum 594 SEQUENCE /// ENTRY T51095 #type complete TITLE acid phosphatase (EC 3.1.3.2) purple 2, precursor [similarity] - sweet potato ALTERNATE_NAMES purple acid phosphatase (PAP) ORGANISM #formal_name Ipomoea batatas #common_name sweet potato DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 14-Dec-2001 ACCESSIONS T51095; T51094 REFERENCE Z25293 !$#authors Schenk, G.; Ge, Y.; Carrington, L.E.; Wynne, C.J.; Searle, !1I.R.; Carroll, B.J.; Hamilton, S.; de Jersey, J. !$#journal Arch. Biochem. Biophys. (1999) 370:183-189 !$#title Binuclear metal centers in plant purple acid phosphatases: !1Fe-Mn in sweet potato and Fe-Zn in soybean. !$#cross-references MUID:99441212; PMID:10510276 !$#accession T51095 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-465 ##label SCH !'##cross-references EMBL:AF200826; PIDN:AAF19822.1 REFERENCE Z25292 !$#authors Durmus, A.; Eicken, C.; Spener, F.; Krebs, B. !$#journal Biochim. Biophys. Acta (1999) 1434:202-209 !$#title Cloning and comparative protein modeling of two purple acid !1phosphatase isozymes from sweet potatoes (Ipomoea batatas). !$#cross-references MUID:20028255; PMID:10556574 !$#accession T51094 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-99,'K',101-267,'S',269-361,'I',363-367,'N',369-372,'E', !1374-465 ##label DUR !'##cross-references EMBL:AJ006224; PIDN:CAA06921.1 !'##note designated spPAP1 in this report COMMENT Two other isoforms of sweet potato PAP have been shown to !1contain iron-zinc and iron-manganese binuclear metal !1centers, respectively. COMPLEX homodimer FUNCTION !$#description catalyzes the hydrolysis of phosphate monoesters CLASSIFICATION #superfamily kidney bean purple acid phosphatase; !1phosphoesterase core homology KEYWORDS glycoprotein; homodimer; iron; metalloprotein; phosphoric !1monoester hydrolase; zinc FEATURE !$1-24 #domain signal sequence #status predicted #label PRO\ !$158-232 #domain phosphoesterase core homology #label PEC\ !$110,138,172,303, !$400,425 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$164,193,196,354 #binding_site iron (Asp, Asp, Tyr, His) #status !8predicted\ !$193,230,315,352 #binding_site zinc or manganese (Asp, Asn, His, His) !8#status predicted\ !$231,325 #active_site His #status predicted\ !$374 #disulfide_bonds interchain #status predicted SUMMARY #length 465 #molecular-weight 53401 #checksum 5070 SEQUENCE /// ENTRY A59201 #type complete TITLE acid phosphatase (EC 3.1.3.2) purple 3 [validated] - sweet potato ALTERNATE_NAMES purple acid phosphatase (PAP) ORGANISM #formal_name Ipomoea batatas #common_name sweet potato DATE 24-Aug-2001 #sequence_revision 24-Aug-2001 #text_change 24-Aug-2001 ACCESSIONS A59201; B59201 REFERENCE Z25292 !$#authors Durmus, A.; Eicken, C.; Spener, F.; Krebs, B. !$#journal Biochim. Biophys. Acta (1999) 1434:202-209 !$#title Cloning and comparative protein modeling of two purple acid !1phosphatase isozymes from sweet potatoes (Ipomoea batatas). !$#cross-references MUID:20028255; PMID:10556574 !$#accession A59201 !'##molecule_type mRNA !'##residues 5-431 ##label KUR !'##cross-references GB:AJ006870; NID:g4210711; PIDN:CAA07280.1; !1PID:g4210712 !$#accession B59201 !'##molecule_type protein !'##residues 1-20 ##label KU2 !'##experimental_source root !'##note designated spPAP2 by these authors COMMENT Metal content is iron and zinc. COMPLEX homodimer FUNCTION !$#description catalyzes the hydrolysis of phosphate monoesters [validated, !1MUID:99441212] CLASSIFICATION #superfamily kidney bean purple acid phosphatase; !1phosphoesterase core homology KEYWORDS glycoprotein; homodimer; iron; metalloprotein; phosphoric !1monoester hydrolase; zinc FEATURE !$1-431 #product purple acid phosphatase #status experimental !8#label MAT\ !$124-198 #domain phosphoesterase core homology #label PEC\ !$58,76,138,269,344, !$391 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$130,159,162,320 #binding_site iron (Asp, Asp, Tyr, His) #status !8predicted\ !$159,196,281,318 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$197,291 #active_site His #status predicted\ !$340 #disulfide_bonds interchain #status predicted SUMMARY #length 431 #molecular-weight 49475 #checksum 7886 SEQUENCE /// ENTRY B59200 #type complete TITLE acid phosphatase (EC 3.1.3.2) purple, precursor [validated] - soybean ALTERNATE_NAMES purple acid phosphatase (PAP) ORGANISM #formal_name Glycine max #common_name soybean DATE 24-Aug-2001 #sequence_revision 24-Aug-2001 #text_change 24-Aug-2001 ACCESSIONS B59200 REFERENCE Z25293 !$#authors Schenk, G.; Ge, Y.; Carrington, L.E.; Wynne, C.J.; Searle, !1I.R.; Carroll, B.J.; Hamilton, S.; de Jersey, J. !$#journal Arch. Biochem. Biophys. (1999) 370:183-189 !$#title Binuclear metal centers in plant purple acid phosphatases: !1Fe-Mn in sweet potato and Fe-Zn in soybean. !$#cross-references MUID:99441212; PMID:10510276 !$#accession B59200 !'##molecule_type mRNA !'##residues 1-464 ##label KUR !'##cross-references GB:AF200824; NID:g6635438; PIDN:AAF19820.1; !1PID:g6635439 COMMENT Metal content is iron and zinc, with small amounts of !1manganese, copper, and magnesium. COMPLEX homodimer FUNCTION !$#description catalyzes the hydrolysis of phosphate monoesters [validated, !1MUID:99441212] !$#note active on a variety of activated and unactivated phosphate !1ester and anhydride substrates CLASSIFICATION #superfamily kidney bean purple acid phosphatase; !1phosphoesterase core homology KEYWORDS glycoprotein; homodimer; iron; metalloprotein; phosphoric !1monoester hydrolase; zinc FEATURE !$31-464 #product purple acid phosphatase #status experimental !8#label MAT\ !$156-230 #domain phosphoesterase core homology #label PEC\ !$108,136,170,301, !$398,423 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$162,191,194,352 #binding_site iron (Asp, Asp, Tyr, His) #status !8predicted\ !$191,228,313,350 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$229,323 #active_site His #status predicted\ !$372 #disulfide_bonds interchain #status predicted SUMMARY #length 464 #molecular-weight 53027 #checksum 8789 SEQUENCE /// ENTRY B84540 #type complete TITLE acid phosphatase (EC 3.1.3.2) purple At2g16430, precursor [similarity] - Arabidopsis thaliana ALTERNATE_NAMES purple acid phosphatase (PAP) ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 02-Feb-2001 #sequence_revision 02-Feb-2001 #text_change 14-Sep-2001 ACCESSIONS B84540 REFERENCE A84420 !$#authors Lin, X.; Kaul, S.; Rounsley, S.D.; Shea, T.P.; Benito, M.I.; !1Town, C.D.; Fujii, C.Y.; Mason, T.M.; Bowman, C.L.; !1Barnstead, M.E.; Feldblyum, T.V.; Buell, C.R.; Ketchum, !1K.A.; Lee, J.J.; Ronning, C.M.; Koo, H.; Moffat, K.S.; !1Cronin, L.A.; Shen, M.; VanAken, S.E.; Umayam, L.; Tallon, !1L.J.; Gill, J.E.; Adams, M.D.; Carrera, A.J.; Creasy, T.H.; !1Goodman, H.M.; Somerville, C.R.; Copenhaver, G.P.; Preuss, !1D.; Nierman, W.C.; White, O.; Eisen, J.A.; Salzberg, S.L.; !1Fraser, C.M.; Venter, J.C. !$#journal Nature (1999) 402:761-768 !$#title Sequence and analysis of chromosome 2 of the plant !1Arabidopsis thaliana. !$#cross-references MUID:20083487; PMID:10617197 !$#accession B84540 !'##molecule_type DNA !'##residues 1-468 ##label STO !'##cross-references GB:AE002093; NID:g4544387; PIDN:AAD22297.1; !1GSPDB:GN00139 GENETICS !$#gene At2g16430 !$#map_position 2 FUNCTION !$#description catalyzes the hydrolysis of phosphate monoesters CLASSIFICATION #superfamily kidney bean purple acid phosphatase; !1phosphoesterase core homology KEYWORDS glycoprotein; homodimer; iron; metalloprotein; phosphoric !1monoester hydrolase; zinc FEATURE !$161-235 #domain phosphoesterase core homology #label PEC\ !$95,113,175,184,306, !$428 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$167,196,199,357 #binding_site iron (Asp, Asp, Tyr, His) #status !8predicted\ !$196,233,318,355 #binding_site zinc or manganese (Asp, Asn, His, His) !8#status predicted\ !$234,328 #active_site His #status predicted\ !$377 #disulfide_bonds interchain #status predicted SUMMARY #length 468 #molecular-weight 54219 #checksum 535 SEQUENCE /// ENTRY T51096 #type complete TITLE acid phosphatase (EC 3.1.3.2) purple PAP32, precursor [similarity] - Anchusa officinalis ALTERNATE_NAMES purple acid phosphatase (PAP) ORGANISM #formal_name Anchusa officinalis DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 14-Sep-2001 ACCESSIONS T51096 REFERENCE Z25294 !$#authors Liang, H.; Su, W.; Sun, S. !$#submission submitted to the EMBL Data Library, February 1999 !$#description Purple acid phosphatase cDNA of Anchusa officinalis. !$#accession T51096 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-470 ##label LIA !'##cross-references EMBL:AF126255; PIDN:AAD20634.1 GENETICS !$#gene PAP32 FUNCTION !$#description catalyzes the hydrolysis of phosphate monoesters CLASSIFICATION #superfamily kidney bean purple acid phosphatase; !1phosphoesterase core homology KEYWORDS glycoprotein; homodimer; iron; metalloprotein; phosphoric !1monoester hydrolase; zinc FEATURE !$162-236 #domain phosphoesterase core homology #label PEC\ !$114,176,185,264, !$307,383,405,430 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$168,197,200,359 #binding_site iron (Asp, Asp, Tyr, His) #status !8predicted\ !$197,234,319,357 #binding_site zinc or manganese (Asp, Asn, His, His) !8#status predicted\ !$235,329 #active_site His #status predicted\ !$379 #disulfide_bonds interchain #status predicted SUMMARY #length 470 #molecular-weight 53838 #checksum 343 SEQUENCE /// ENTRY H84669 #type complete TITLE acid phosphatase (EC 3.1.3.2) purple At2g27190, precursor [similarity] - Arabidopsis thaliana ALTERNATE_NAMES purple acid phosphatase (PAP) ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 02-Feb-2001 #sequence_revision 02-Feb-2001 #text_change 14-Sep-2001 ACCESSIONS H84669 REFERENCE A84420 !$#authors Lin, X.; Kaul, S.; Rounsley, S.D.; Shea, T.P.; Benito, M.I.; !1Town, C.D.; Fujii, C.Y.; Mason, T.M.; Bowman, C.L.; !1Barnstead, M.E.; Feldblyum, T.V.; Buell, C.R.; Ketchum, !1K.A.; Lee, J.J.; Ronning, C.M.; Koo, H.; Moffat, K.S.; !1Cronin, L.A.; Shen, M.; VanAken, S.E.; Umayam, L.; Tallon, !1L.J.; Gill, J.E.; Adams, M.D.; Carrera, A.J.; Creasy, T.H.; !1Goodman, H.M.; Somerville, C.R.; Copenhaver, G.P.; Preuss, !1D.; Nierman, W.C.; White, O.; Eisen, J.A.; Salzberg, S.L.; !1Fraser, C.M.; Venter, J.C. !$#journal Nature (1999) 402:761-768 !$#title Sequence and analysis of chromosome 2 of the plant !1Arabidopsis thaliana. !$#cross-references MUID:20083487; PMID:10617197 !$#accession H84669 !'##molecule_type DNA !'##residues 1-469 ##label STO !'##cross-references GB:AE002093; NID:g4646219; PIDN:AAD26885.1; !1GSPDB:GN00139 GENETICS !$#gene At2g27190 !$#map_position 2 FUNCTION !$#description catalyzes the hydrolysis of phosphate monoesters CLASSIFICATION #superfamily kidney bean purple acid phosphatase; !1phosphoesterase core homology KEYWORDS glycoprotein; homodimer; iron; metalloprotein; phosphoric !1monoester hydrolase; zinc FEATURE !$162-236 #domain phosphoesterase core homology #label PEC\ !$114,176,307,429 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$168,197,200,358 #binding_site iron (Asp, Asp, Tyr, His) #status !8predicted\ !$197,234,319,356 #binding_site zinc or manganese (Asp, Asn, His, His) !8#status predicted\ !$235,329 #active_site His #status predicted\ !$378 #disulfide_bonds interchain #status predicted SUMMARY #length 469 #molecular-weight 54162 #checksum 7841 SEQUENCE /// ENTRY T04599 #type complete TITLE acid phosphatase (EC 3.1.3.2) purple F23E13.190, precursor [similarity] - Arabidopsis thaliana ALTERNATE_NAMES purple acid phosphatase (PAP) ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 23-Apr-1999 #sequence_revision 23-Apr-1999 #text_change 14-Sep-2001 ACCESSIONS T04599 REFERENCE Z15378 !$#authors Bevan, M.; Hilbert, H.; Braun, M.; Holzer, E.; Brandt, A.; !1Duesterhoeft, A.; Jesse, T.; Heijnen, L.; Vos, P.; Mewes, !1H.W.; Mayer, K.F.X.; Schueller, C. !$#submission submitted to the Protein Sequence Database, March 1998 !$#accession T04599 !'##molecule_type DNA !'##residues 1-466 ##label BEV !'##cross-references EMBL:AL022141 !'##experimental_source cultivar Columbia; BAC clone F23E13 GENETICS !$#gene F23E13.190 !$#map_position 4 !$#introns 53/3; 125/3; 163/1; 238/3; 285/1; 399/2 FUNCTION !$#description catalyzes the hydrolysis of phosphate monoesters CLASSIFICATION #superfamily kidney bean purple acid phosphatase; !1phosphoesterase core homology KEYWORDS glycoprotein; homodimer; iron; metalloprotein; phosphoric !1monoester hydrolase; zinc FEATURE !$158-231 #domain phosphoesterase core homology #label PEC\ !$164,192,195,353 #binding_site iron (Asp, Asp, Tyr, His) #status !8predicted\ !$172,367,424 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$192,229,314,351 #binding_site zinc or manganese (Asp, Asn, His, His) !8#status predicted\ !$230,324 #active_site His #status predicted SUMMARY #length 466 #molecular-weight 52969 #checksum 5577 SEQUENCE /// ENTRY F96605 #type complete TITLE acid phosphatase (EC 3.1.3.2) purple F13N6.16, precursor [similarity] - Arabidopsis thaliana ALTERNATE_NAMES purple acid phosphatase (PAP) ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 02-Mar-2001 #sequence_revision 02-Mar-2001 #text_change 14-Sep-2001 ACCESSIONS F96605 REFERENCE A86141 !$#authors Theologis, A.; Ecker, J.R.; Palm, C.J.; Federspiel, N.A.; !1Kaul, S.; White, O.; Alonso, J.; Altaf, H.; Araujo, R.; !1Bowman, C.L.; Brooks, S.Y.; Buehler, E.; Chan, A.; Chao, Q.; !1Chen, H.; Cheuk, R.F.; Chin, C.W.; Chung, M.K.; Conn, L.; !1Conway, A.B.; Conway, A.R.; Creasy, T.H.; Dewar, K.; Dunn, !1P.; Etgu, P.; Feldblyum, T.V.; Feng, J.; Fong, B.; Fujii, !1C.Y.; Gill, J.E.; Goldsmith, A.D.; Haas, B.; Hansen, N.F.; !1Hughes, B.; Huizar, L.; Hunter, J.L.; Jenkins, J.; !1Johnson-Hopson, C.; Khan, S.; Khaykin, E.; Kim, C.J.; Koo, !1H.L.; Kremenetskaia, I.; Kurtz, D.B.; Kwan, A.; Lam, B.; !1Langin-Hooper, S.; Lee, A.; Lee, J.M.; Lenz, C.A.; Li, J.H.; !1Li, Y.; Lin, X.; Liu, S.X.; Liu, Z.A.; Luros, J.S.; Maiti, !1R.; Marziali, A.; Militscher, J.; Miranda, M.; Nguyen, M.; !1Nierman, W.C.; Osborne, B.I.; Pai, G.; Peterson, J.; Pham, !1P.K.; Rizzo, M.; Rooney, T.; Rowley, D.; Sakano, H.; !1Salzberg, S.L.; Schwartz, J.R.; Shinn, P.; Southwick, A.M.; !1Sun, H.; Tallon, L.J.; Tambunga, G.; Toriumi, M.J.; Town, !1C.D.; Utterback, T.; van Aken, S.; Vaysberg, M.; Vysotskaia, !1V.S.; Walker, M.; Wu, D.; Yu, G.; Fraser, C.M.; Venter, !1J.C.; Davis, R.W. !$#journal Nature (2000) 408:816-820 !$#title Sequence and analysis of chromosome 1 of the plant !1Arabidopsis. !$#cross-references MUID:21016719; PMID:11130712 !$#accession F96605 !'##molecule_type DNA !'##residues 1-466 ##label STO !'##cross-references GB:AE005173; NID:g11024853; PIDN:AAG26938.1; !1GSPDB:GN00141 GENETICS !$#gene F13N6.16 !$#map_position 1 FUNCTION !$#description catalyzes the hydrolysis of phosphate monoesters CLASSIFICATION #superfamily kidney bean purple acid phosphatase; !1phosphoesterase core homology KEYWORDS glycoprotein; homodimer; iron; metalloprotein; phosphoric !1monoester hydrolase; zinc FEATURE !$158-231 #domain phosphoesterase core homology #label PEC\ !$88,172,367,424 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$164,192,195,353 #binding_site iron (Asp, Asp, Tyr, His) #status !8predicted\ !$192,229,314,351 #binding_site zinc or manganese (Asp, Asn, His, His) !8#status predicted\ !$230,324 #active_site His #status predicted SUMMARY #length 466 #molecular-weight 52830 #checksum 4939 SEQUENCE /// ENTRY T49031 #type complete TITLE acid phosphatase (EC 3.1.3.2) purple F3C22.180, precursor [similarity] - Arabidopsis thaliana ALTERNATE_NAMES purple acid phosphatase (PAP) ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 02-Jun-2000 #sequence_revision 02-Jun-2000 #text_change 14-Sep-2001 ACCESSIONS T49031 REFERENCE Z25013 !$#authors Purnelle, B.; Masuy, D.; Goffeau, A.; Boutry, M.; Mewes, !1H.W.; Rudd, S.; Lemcke, K.; Mayer, K.F.X.; Quetier, F.; !1Salanoubat, M. !$#submission submitted to the Protein Sequence Database, April 2000 !$#accession T49031 !'##molecule_type DNA !'##residues 1-427 ##label PUR !'##cross-references EMBL:AL353912; GSPDB:GN00061; ATSP:F3C22.180 !'##experimental_source cultivar Columbia; BAC clone F3C22 GENETICS !$#gene ATSP:F3C22.180 !$#map_position 3 !$#introns 46/3; 146/1; 227/2; 337/3; 367/2 FUNCTION !$#description catalyzes the hydrolysis of phosphate monoesters CLASSIFICATION #superfamily kidney bean purple acid phosphatase; !1phosphoesterase core homology KEYWORDS glycoprotein; iron; metalloprotein; phosphoric monoester !1hydrolase; zinc FEATURE !$141-209 #domain phosphoesterase core homology #label PEC\ !$85,392 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$147,174,177,332 #binding_site iron (Asp, Asp, Tyr, His) #status !8predicted\ !$174,207,291,330 #binding_site zinc or manganese (Asp, Asn, His, His) !8#status predicted\ !$208,301 #active_site His #status predicted SUMMARY #length 427 #molecular-weight 48461 #checksum 5991 SEQUENCE /// ENTRY T49035 #type complete TITLE acid phosphatase (EC 3.1.3.2) purple F3C22.220, precursor [similarity] - Arabidopsis thaliana ALTERNATE_NAMES purple acid phosphatase (PAP) ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 02-Jun-2000 #sequence_revision 02-Jun-2000 #text_change 14-Sep-2001 ACCESSIONS T49035 REFERENCE Z25013 !$#authors Purnelle, B.; Masuy, D.; Goffeau, A.; Boutry, M.; Mewes, !1H.W.; Rudd, S.; Lemcke, K.; Mayer, K.F.X.; Quetier, F.; !1Salanoubat, M. !$#submission submitted to the Protein Sequence Database, April 2000 !$#accession T49035 !'##molecule_type DNA !'##residues 1-426 ##label PUR !'##cross-references EMBL:AL353912; GSPDB:GN00061; ATSP:F3C22.220 !'##experimental_source cultivar Columbia; BAC clone F3C22 GENETICS !$#gene ATSP:F3C22.220 !$#map_position 3 !$#introns 49/3; 139/1; 270/3; 328/3; 358/2 FUNCTION !$#description catalyzes the hydrolysis of phosphate monoesters CLASSIFICATION #superfamily kidney bean purple acid phosphatase; !1phosphoesterase core homology KEYWORDS glycoprotein; iron; metalloprotein; phosphoric monoester !1hydrolase; zinc FEATURE !$134-202 #domain phosphoesterase core homology #label PEC\ !$108,395 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$140,167,170,323 #binding_site iron (Asp, Asp, Tyr, His) #status !8predicted\ !$167,200,284,321 #binding_site zinc or manganese (Asp, Asn, His, His) !8#status predicted\ !$201,294 #active_site His #status predicted SUMMARY #length 426 #molecular-weight 48551 #checksum 481 SEQUENCE /// ENTRY T49034 #type complete TITLE acid phosphatase (EC 3.1.3.2) purple F3C22.210, precursor [similarity] - Arabidopsis thaliana ALTERNATE_NAMES purple acid phosphatase (PAP) ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 02-Jun-2000 #sequence_revision 02-Jun-2000 #text_change 14-Sep-2001 ACCESSIONS T49034 REFERENCE Z25013 !$#authors Purnelle, B.; Masuy, D.; Goffeau, A.; Boutry, M.; Mewes, !1H.W.; Rudd, S.; Lemcke, K.; Mayer, K.F.X.; Quetier, F.; !1Salanoubat, M. !$#submission submitted to the Protein Sequence Database, April 2000 !$#accession T49034 !'##molecule_type DNA !'##residues 1-437 ##label PUR !'##cross-references EMBL:AL353912; GSPDB:GN00061; ATSP:F3C22.210 !'##experimental_source cultivar Columbia; BAC clone F3C22 GENETICS !$#gene ATSP:F3C22.210 !$#map_position 3 !$#introns 53/3; 151/1; 282/3; 340/3; 370/2 FUNCTION !$#description catalyzes the hydrolysis of phosphate monoesters CLASSIFICATION #superfamily kidney bean purple acid phosphatase; !1phosphoesterase core homology KEYWORDS glycoprotein; iron; metalloprotein; phosphoric monoester !1hydrolase; zinc FEATURE !$146-214 #domain phosphoesterase core homology #label PEC\ !$30 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$152,179,182,335 #binding_site iron (Asp, Asp, Tyr, His) #status !8predicted\ !$179,212,296,333 #binding_site zinc or manganese (Asp, Asn, His, His) !8#status predicted\ !$213,306 #active_site His #status predicted SUMMARY #length 437 #molecular-weight 50641 #checksum 7008 SEQUENCE /// ENTRY T05239 #type complete TITLE acid phosphatase (EC 3.1.3.2) purple F18A5.90, precursor [similarity] - Arabidopsis thaliana ALTERNATE_NAMES purple acid phosphatase (PAP) ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 23-Apr-1999 #sequence_revision 23-Apr-1999 #text_change 14-Sep-2001 ACCESSIONS T05239 REFERENCE Z15405 !$#authors Bevan, M.; Weber, N.; Grueninger, D.; Schmidheini, T.; !1Bancroft, I.; Mewes, H.W.; Mayer, K.F.X.; Schueller, C. !$#submission submitted to the Protein Sequence Database, February 1999 !$#accession T05239 !'##molecule_type DNA !'##residues 1-474 ##label BEV !'##cross-references EMBL:AL035528 !'##experimental_source cultivar Columbia; BAC clone F18A5 GENETICS !$#gene F18A5.90 !$#map_position 4 !$#introns 85/1; 149/1; 267/2; 350/1; 413/3 FUNCTION !$#description catalyzes the hydrolysis of phosphate monoesters CLASSIFICATION #superfamily kidney bean purple acid phosphatase; !1phosphoesterase core homology KEYWORDS glycoprotein; iron; metalloprotein; phosphoric monoester !1hydrolase; zinc FEATURE !$194-286 #domain phosphoesterase core homology #label PEC\ !$59,121,136,206,337, !$425,471 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$200,227,230,415 #binding_site iron (Asp, Asp, Tyr, His) #status !8predicted\ !$227,284,376,413 #binding_site zinc or manganese (Asp, Asn, His, His) !8#status predicted\ !$285,386 #active_site His #status predicted SUMMARY #length 474 #molecular-weight 53431 #checksum 432 SEQUENCE /// ENTRY T21089 #type complete TITLE acid phosphatase (EC 3.1.3.2) purple homolog F18E2.1, precursor [similarity] - Caenorhabditis elegans ALTERNATE_NAMES purple acid phosphatase (PAP) ORGANISM #formal_name Caenorhabditis elegans DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 14-Sep-2001 ACCESSIONS T21089 REFERENCE Z19372 !$#authors Lightning, J. !$#submission submitted to the EMBL Data Library, June 1996 !$#accession T21089 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-455 ##label WIL !'##cross-references EMBL:Z75537; PIDN:CAA99834.1; GSPDB:GN00023; !1CESP:F18E2.1 !'##experimental_source clone F18E2 GENETICS !$#gene CESP:F18E2.1 !$#map_position 5 !$#introns 48/1; 96/1; 178/3; 255/3; 292/3; 337/3; 424/2 CLASSIFICATION #superfamily kidney bean purple acid phosphatase; !1phosphoesterase core homology KEYWORDS glycoprotein; iron; metalloprotein; phosphoric monoester !1hydrolase; zinc FEATURE !$117-189 #domain phosphoesterase core homology #label PEC\ !$123,152,155,321 #binding_site iron (Asp, Asp, Tyr, His) #status !8predicted\ !$130,194,388 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$152,187,272,319 #binding_site zinc or manganese (Asp, Asn, His, His) !8#status predicted\ !$188 #active_site His #status predicted SUMMARY #length 455 #molecular-weight 51894 #checksum 2146 SEQUENCE /// ENTRY T21181 #type complete TITLE acid phosphatase (EC 3.1.3.2) purple homolog F21A3.2 precursor [similarity] - Caenorhabditis elegans ALTERNATE_NAMES purple acid phosphatase (PAP) ORGANISM #formal_name Caenorhabditis elegans DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 09-Nov-2001 ACCESSIONS T21181 REFERENCE Z19387 !$#authors McMurray, A. !$#submission submitted to the EMBL Data Library, November 1996 !$#accession T21181 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-424 ##label WIL !'##cross-references EMBL:Z81509; PIDN:CAB04153.1; GSPDB:GN00023; !1CESP:F21A3.2 !'##experimental_source clone F21A3 GENETICS !$#gene CESP:F21A3.2 !$#map_position 5 !$#introns 58/1; 119/1; 181/2; 229/1; 248/3; 314/3; 360/3 CLASSIFICATION #superfamily kidney bean purple acid phosphatase; !1phosphoesterase core homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; zinc FEATURE !$85-157 #domain phosphoesterase core homology #label PEC\ !$91,120,123,279 #binding_site iron (Asp, Asp, Tyr, His) #status !8predicted\ !$120,155,259,277 #binding_site zinc or manganese (Asp, Asn, Tyr, His) !8#status predicted\ !$156 #active_site His #status predicted SUMMARY #length 424 #molecular-weight 49674 #checksum 7635 SEQUENCE /// ENTRY T26388 #type complete TITLE acid phosphatase (EC 3.1.3.2) purple homolog Y105C5B.l precursor [similarity] - Caenorhabditis elegans ALTERNATE_NAMES purple acid phosphatase (PAP) ORGANISM #formal_name Caenorhabditis elegans DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 09-Nov-2001 ACCESSIONS T26388 REFERENCE Z20208 !$#authors McMurray, A. !$#submission submitted to the EMBL Data Library, September 1999 !$#accession T26388 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-475 ##label WIL !'##cross-references EMBL:AL110479; NID:e1542153; PIDN:CAB54360.1; !1CESP:Y105C5B.l !'##experimental_source clone Y105C5B GENETICS !$#gene CESP:Y105C5B.l !$#introns 46/1; 100/1; 158/1; 249/3; 416/3 CLASSIFICATION #superfamily kidney bean purple acid phosphatase; !1phosphoesterase core homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; zinc FEATURE !$183-256 #domain phosphoesterase core homology #label PEC\ !$189,219,222,380 #binding_site iron (Asp, Asp, Tyr, His) #status !8predicted\ !$219,254,331,378 #binding_site zinc or manganese (Asp, Asn, His, His) !8#status predicted\ !$255 #active_site His #status predicted SUMMARY #length 475 #molecular-weight 54486 #checksum 7870 SEQUENCE /// ENTRY T26378 #type complete TITLE acid phosphatase (EC 3.1.3.2) purple homolog Y105C5B.b [similarity] - Caenorhabditis elegans ALTERNATE_NAMES purple acid phosphatase (PAP) ORGANISM #formal_name Caenorhabditis elegans DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 09-Nov-2001 ACCESSIONS T26378 REFERENCE Z20208 !$#authors McMurray, A. !$#submission submitted to the EMBL Data Library, September 1999 !$#accession T26378 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-463 ##label WIL !'##cross-references EMBL:AL110479; NID:e1542153; PIDN:CAB54350.1; !1CESP:Y105C5B.b !'##experimental_source clone Y105C5B GENETICS !$#gene CESP:Y105C5B.b !$#introns 45/1; 99/1; 215/3; 383/3; 443/2 CLASSIFICATION #superfamily kidney bean purple acid phosphatase; !1phosphoesterase core homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; zinc FEATURE !$124-222 #domain phosphoesterase core homology #label PEC\ !$130,160,163,347 #binding_site iron (Asp, Asp, Tyr, His) #status !8predicted\ !$160,220,297,345 #binding_site zinc or manganese (Asp, Asn, His, His) !8#status predicted\ !$221 #active_site His #status predicted SUMMARY #length 463 #molecular-weight 52738 #checksum 793 SEQUENCE /// ENTRY T26381 #type complete TITLE purple acid phosphatase-related protein Y105C5B.e [similarity] - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 09-Nov-2001 ACCESSIONS T26381 REFERENCE Z20208 !$#authors McMurray, A. !$#submission submitted to the EMBL Data Library, September 1999 !$#accession T26381 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-348 ##label WIL !'##cross-references EMBL:AL110479; NID:e1542153; PIDN:CAB54353.1; !1CESP:Y105C5B.e !'##experimental_source clone Y105C5B COMMENT Residues essential for enzymatic activity are missing. GENETICS !$#gene CESP:Y105C5B.e !$#introns 11/1; 64/1; 155/3; 288/3 CLASSIFICATION #superfamily kidney bean purple acid phosphatase; !1phosphoesterase core homology SUMMARY #length 348 #molecular-weight 39809 #checksum 3079 SEQUENCE /// ENTRY JC2545 #type complete TITLE acid phosphatase (EC 3.1.3.2) - Aspergillus ficuum ALTERNATE_NAMES apases, orthophosphoric monoester phosphohydrolase ORGANISM #formal_name Aspergillus ficuum DATE 13-Jun-1995 #sequence_revision 14-Jul-1995 #text_change 07-May-1999 ACCESSIONS JC2545 REFERENCE JC2545 !$#authors Ullah, A.H.J.; Mullaney, E.M.; Dischinger Jr., H.C. !$#journal Biochem. Biophys. Res. Commun. (1994) 203:182-189 !$#title The complete primary structure elucidation of Aspergillus !1ficuum (niger), pH6.0, optimum acid phosphatase by Edman !1degradation. !$#cross-references MUID:94354800; PMID:8074654 !$#accession JC2545 !'##molecule_type protein !'##residues 1-583 ##label ULL COMMENT On the basis of the intense blue color, the authors believe !1that the metal binding sites are occupied by copper. FUNCTION !$#description catalyzes the hydrolysis of phosphate monoesters CLASSIFICATION #superfamily Aspergillus acid phosphatase; phosphoesterase !1core homology KEYWORDS copper; glycoprotein; metalloprotein; phosphoric monoester !1hydrolase FEATURE !$162-288 #domain phosphoesterase core homology #status !8atypical #label PEC\ !$88,139,220,273,311, !$318,330,386,407, !$490,501,537,556 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$168,197,200,479 #binding_site copper (Asp, Asp, Tyr, His) #status !8predicted\ !$197,286,442,477 #binding_site copper (Asp, Asn, His, His) #status !8predicted\ !$287 #active_site His #status predicted SUMMARY #length 583 #molecular-weight 64251 #checksum 3791 SEQUENCE /// ENTRY PAECS #type complete TITLE phosphoserine phosphatase (EC 3.1.3.3) - Escherichia coli (strain K-12) ALTERNATE_NAMES O-phosphoserine phosphohydrolase ORGANISM #formal_name Escherichia coli DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 01-Mar-2002 ACCESSIONS A24271; S56612; C65254 REFERENCE A24271 !$#authors Neuwald, A.F.; Stauffer, G.V. !$#journal Nucleic Acids Res. (1985) 13:7025-7039 !$#title DNA sequence and characterization of the Escherichia coli !1serB gene. !$#cross-references MUID:86041894; PMID:2997734 !$#accession A24271 !'##molecule_type DNA !'##residues 1-322 ##label NEU !'##cross-references GB:X03046; GB:M30784; NID:g432632; PIDN:CAA26852.1; !1PID:g42948 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56612 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-322 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97284.1; !1PID:g537228 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65254 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-322 ##label BLAT !'##cross-references GB:AE000509; GB:U00096; NID:g2367383; !1PIDN:AAC77341.1; PID:g1790849; UWGP:b4388 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene serB !$#map_position 100 min FUNCTION !$#description catalyzes the hydrolysis of O-phosphoserine to serine and !1ortho phosphate !$#pathway serine biosynthesis CLASSIFICATION #superfamily phosphoserine phosphatase KEYWORDS phosphoric monoester hydrolase; serine biosynthesis SUMMARY #length 322 #molecular-weight 35042 #checksum 8723 SEQUENCE /// ENTRY I64108 #type complete TITLE phosphoserine phosphatase (EC 3.1.3.3) - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES O-phosphoserine phosphohydrolase; serB protein ORGANISM #formal_name Haemophilus influenzae DATE 18-Aug-1995 #sequence_revision 04-Oct-1996 #text_change 28-Jul-2000 ACCESSIONS I64108 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession I64108 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-314 ##label TIGR !'##cross-references GB:U32784; GB:L42023; NID:g3212210; !1PIDN:AAC22693.1; PID:g1574066; TIGR:HI1033 !'##note named as homolog to a protein from Escherichia coli FUNCTION !$#description catalyzes the hydrolysis of O-phosphoserine to serine and !1orthophosphate !$#pathway serine biosynthesis CLASSIFICATION #superfamily phosphoserine phosphatase KEYWORDS phosphoric monoester hydrolase; serine biosynthesis SUMMARY #length 314 #molecular-weight 34720 #checksum 1728 SEQUENCE /// ENTRY A64499 #type complete TITLE phosphoserine phosphatase (EC 3.1.3.3) - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A64499 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession A64499 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-211 ##label BUL !'##cross-references GB:U67599; GB:L77117; NID:g2826435; !1PIDN:AAB99612.1; PID:g1592204; TIGR:MJ1594 GENETICS !$#map_position FOR1565667-1566302 CLASSIFICATION #superfamily phosphoserine phosphatase KEYWORDS phosphoric monoester hydrolase SUMMARY #length 211 #molecular-weight 23593 #checksum 649 SEQUENCE /// ENTRY D64601 #type complete TITLE phosphoserine phosphatase (EC 3.1.3.3) - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS D64601 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession D64601 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-207 ##label TOM !'##cross-references GB:AE000578; GB:AE000511; NID:g2313759; !1PIDN:AAD07711.1; PID:g2313770; TIGR:HP0652 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily phosphoserine phosphatase KEYWORDS phosphoric monoester hydrolase SUMMARY #length 207 #molecular-weight 22991 #checksum 5123 SEQUENCE /// ENTRY S53931 #type complete TITLE phosphoserine phosphatase (EC 3.1.3.3) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES phosphoserine phosphohydrolase; protein G7744; protein YGR208w ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S53931; S62100; S64530; S63857 REFERENCE S53922 !$#authors Guerreiro, P.; Barreiros, T.; Soares, H.; Cyrne, L.; Maia e !1Silva, A.; Rodrigues-Pousada, C. !$#submission submitted to the EMBL Data Library, April 1995 !$#description Sequencing of a 17.6 kb segment on the right arm of yeast !1chromosome VII reveals 12 open reading frames, including !1CCT, ADE3 and TR-I genes, homologous to the yeast YAL023 and !1EF1G genes, of the human. !$#accession S53931 !'##molecule_type DNA !'##residues 1-309 ##label GUE !'##cross-references EMBL:Z49133; NID:g790489; PIDN:CAA89001.1; !1PID:g790499 !'##experimental_source strain S288C REFERENCE S62100 !$#authors Song, J.M.; Cheung, E.; Rabinowitz, J.C. !$#submission submitted to the EMBL Data Library, September 1995 !$#description Identification and characterization of the Saccharomyces !1cerevisiae SER2 gene. !$#accession S62100 !'##molecule_type DNA !'##residues 1-309 ##label SON !'##cross-references EMBL:U36473; NID:g1015427; PIDN:AAA79062.1; !1PID:g1015428 !'##experimental_source strain GRF88 REFERENCE S64517 !$#authors Guerreiro, P.; Barreiros, T.; Cyrne, L.; Soares, H.; Maia e !1Silva, A.; Rodrigues-Pousada, C. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64530 !'##molecule_type DNA !'##residues 1-309 ##label GUW !'##cross-references EMBL:Z72993; NID:g1323372; PIDN:CAA97235.1; !1PID:g1323373; GSPDB:GN00007; MIPS:YGR208w !'##experimental_source strain S288C REFERENCE S63848 !$#authors Guerreiro, P.; Barreiros, T.; Soares, H.; Cyrne, L.; Maia e !1Silva, A.; Rodrigues-Pousada, C. !$#journal Yeast (1996) 12:273-280 !$#title Sequencing of a 17.6 kb segment on the right arm of yeast !1chromosome VII reveals 12 ORFs, including CCT, ADE3 and TR-I !1genes, homologues of the yeast PMT and EF1G genes, of the !1human and bacterial electron-transferring flavoproteins !1(beta-chain) and of the Escherichia coli phosphoserine !1phosphohydrolase, and five new ORFs. !$#cross-references MUID:97060019; PMID:8904340 !$#accession S63857 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-309 ##label GUF !'##cross-references EMBL:Z49133; NID:g790489; PIDN:CAA89001.1; !1PID:g790499 GENETICS !$#gene SGD:SER2; MIPS:YGR208w !'##cross-references SGD:S0003440; MIPS:YGR208w !$#map_position 7R CLASSIFICATION #superfamily phosphoserine phosphatase KEYWORDS phosphoric monoester hydrolase SUMMARY #length 309 #molecular-weight 34207 #checksum 5459 SEQUENCE /// ENTRY S11032 #type complete TITLE 5'-nucleotidase (EC 3.1.3.5) precursor [validated] - human ALTERNATE_NAMES 5'-ribonucleotide phosphohydrolase; CD73 antigen; ecto-5'-nucleotidase ORGANISM #formal_name Homo sapiens #common_name man DATE 21-Nov-1993 #sequence_revision 10-Nov-1995 #text_change 08-Dec-2000 ACCESSIONS S11032; A36248; B36248; C36248 REFERENCE S11032 !$#authors Misumi, Y.; Ogata, S.; Ohkubo, K.; Hirose, S.; Ikehara, Y. !$#journal Eur. J. Biochem. (1990) 191:563-569 !$#title Primary structure of human placental 5'-nucleotidase and !1identification of the glycolipid anchor in the mature form. !$#cross-references MUID:90361037; PMID:2129526 !$#accession S11032 !'##molecule_type mRNA !'##residues 1-574 ##label MIS !'##cross-references EMBL:X55740; NID:g23896; PIDN:CAA39271.1; !1PID:g23897 !'##experimental_source placenta !'##note parts of this sequence, including the amino and carboxyl ends !1of the mature protein, were determined by protein sequencing REFERENCE A36248 !$#authors Klemens, M.R.; Sherman, W.R.; Holmberg, N.J.; Ruedi, J.M.; !1Low, M.G.; Thompson, L.F. !$#journal Biochem. Biophys. Res. Commun. (1990) 172:1371-1377 !$#title Characterization of soluble vs membrane-bound human !1placental 5'-nucleotidase. !$#cross-references MUID:91058583; PMID:2173922 !$#accession A36248 !'##molecule_type protein !'##residues 'I',28-38,'ED' ##label KLE1 !'##experimental_source soluble form !$#accession B36248 !'##molecule_type protein !'##residues 'G',28-31,'IT',34-37,'MTE' ##label KLE2 !'##experimental_source phospholipase C sensitive, membrane-bound form !$#accession C36248 !'##molecule_type protein !'##residues 27-31,'I',33-40 ##label KLE3 !'##experimental_source phospholipase C insensitive, membrane-bound form !'##note authors suggest that this is a transmembrane anchored form GENETICS !$#gene GDB:NT5; CD73 !'##cross-references GDB:120243; OMIM:129190 !$#map_position 6q14-6q21 COMPLEX homodimer FUNCTION !$#description catalyzes hydrolysis of 5'-ribonucleotides to the !1corresponding ribonucleosides and phosphate CLASSIFICATION #superfamily 5'-nucleotidase; 5'-nucleotidase homology; !1phosphoesterase core homology KEYWORDS blocked carboxyl end; glycoprotein; homodimer; lipoprotein; !1membrane protein; metalloprotein; phosphatidylinositol !1linkage; phosphoprotein; phosphoric monoester hydrolase; !1zinc FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-549 #product 5'-nucleotidase #status experimental #label !8MAT\ !$27-528 #domain 5'-nucleotidase homology #label NT5\ !$30-119 #domain phosphoesterase core homology #label PEC\ !$550-574 #domain carboxyl-terminal propeptide #status !8predicted #label CPP\ !$36,38,85 #binding_site zinc (Asp, His, Asp) #status predicted\ !$53,311,333,403 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$85,117,220,243 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$118 #active_site His #status predicted\ !$549 #modified_site GPI-anchor ethanolamine amidated !8carboxyl end (Ser) (in mature form) #status !8experimental SUMMARY #length 574 #molecular-weight 63367 #checksum 8567 SEQUENCE /// ENTRY JX0269 #type complete TITLE 5'-nucleotidase (EC 3.1.3.5) precursor - bovine ALTERNATE_NAMES 5'-ribonucleotide phosphohydrolase; CD73 antigen; ecto-5'-nucleotidase ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jun-2000 ACCESSIONS JX0269; A54345; JQ1980; PQ0611 REFERENCE JX0269 !$#authors Suzuki, K.; Furukawa, Y.; Tamura, H.; Ejiri, N.; Suematsu, !1H.; Taguchi, R.; Nakamura, S.; Suzuki, Y.; Ikezawa, H. !$#journal J. Biochem. (1993) 113:607-613 !$#title Purification and cDNA cloning of bovine liver !15'-nucleotidase, a GPI-anchored protein, and its expression !1in COS cells. !$#cross-references MUID:93340109; PMID:8340354 !$#accession JX0269 !'##molecule_type mRNA !'##residues 1-574 ##label SUZ !'##cross-references GB:D14541; NID:g285641; PIDN:BAA03408.1; !1PID:g285642 !'##experimental_source liver !'##note parts of this sequence, including the amino end of the mature !1protein, were confirmed by protein sequencing REFERENCE A54345 !$#authors Taguchi, R.; Hamakawa, N.; Harada-Nishida, M.; Fukui, T.; !1Nojima, K.; Ikezawa, H. !$#journal Biochemistry (1994) 33:1017-1022 !$#title Microheterogeneity in glycosylphosphatidylinositol anchor !1structures of bovine liver 5'-nucleotidase. !$#cross-references MUID:94137709; PMID:8305428 !$#accession A54345 !'##molecule_type protein !'##residues 27-44;106-110, !1'DA';114-123;361-367;369-385;387-402;490-509;511-534;536-549 !1##label TAG !'##experimental_source liver !'##note experimental evidence for GPI-anchor attachment site COMPLEX homodimer FUNCTION !$#description catalyzes hydrolysis of 5'-nucleotides to the corresponding !1nucleosides and phosphate CLASSIFICATION #superfamily 5'-nucleotidase; 5'-nucleotidase homology; !1phosphoesterase core homology KEYWORDS blocked carboxyl end; glycoprotein; homodimer; lipoprotein; !1membrane protein; metalloprotein; phosphatidylinositol !1linkage; phosphoprotein; phosphoric monoester hydrolase; !1zinc FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-549 #product 5'-nucleotidase #status experimental #label !8MAT\ !$27-528 #domain 5'-nucleotidase homology #label NT5\ !$30-119 #domain phosphoesterase core homology #label PEC\ !$550-574 #domain carboxyl-terminal propeptide #status !8predicted #label CPP\ !$53,311,333 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$403 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$549 #modified_site GPI-anchor ethanolamine amidated !8carboxyl end (Ser) (in mature form) #status !8experimental SUMMARY #length 574 #molecular-weight 63085 #checksum 3038 SEQUENCE /// ENTRY JC2001 #type complete TITLE 5'-nucleotidase (EC 3.1.3.5) precursor - mouse ALTERNATE_NAMES 5'-ribonucleotide phosphohydrolase; CD73 antigen; ecto-5'-nucleotidase ORGANISM #formal_name Mus musculus #common_name house mouse DATE 19-May-1994 #sequence_revision 19-May-1994 #text_change 28-Jan-2000 ACCESSIONS JC2001 REFERENCE JC2001 !$#authors Resta, R.; Hooker, S.W.; Hansen, K.R.; Laurent, A.B.; Park, !1J.L.; Blackburn, M.R.; Knudsen, T.B.; Thompson, L.F. !$#journal Gene (1993) 133:171-177 !$#title Murine ecto-5'-nucleotidase (CD73): cDNA cloning and tissue !1distribution. !$#cross-references MUID:94040807; PMID:8224905 !$#accession JC2001 !'##molecule_type mRNA !'##residues 1-574 ##label RES COMPLEX homodimer FUNCTION !$#description catalyzes hydrolysis of 5'-nucleotides to the corresponding !1nucleosides and phosphate CLASSIFICATION #superfamily 5'-nucleotidase; 5'-nucleotidase homology; !1phosphoesterase core homology KEYWORDS blocked carboxyl end; glycoprotein; homodimer; lipoprotein; !1membrane protein; metalloprotein; phosphatidylinositol !1linkage; phosphoprotein; phosphoric monoester hydrolase; !1zinc FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-549 #product 5'-nucleotidase #status predicted #label !8MAT\ !$27-528 #domain 5'-nucleotidase homology #label NT5\ !$30-119 #domain phosphoesterase core homology #label PEC\ !$550-574 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$53,311,333,403 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$549 #modified_site GPI-anchor ethanolamine amidated !8carboxyl end (Ser) (in mature form) #status predicted SUMMARY #length 574 #molecular-weight 63309 #checksum 289 SEQUENCE /// ENTRY A35036 #type complete TITLE 5'-nucleotidase (EC 3.1.3.5) precursor - rat ALTERNATE_NAMES 5'-ribonucleotide phosphohydrolase; CD73 antigen; ecto-5'-nucleotidase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 20-Jul-1990 #sequence_revision 06-Nov-1992 #text_change 28-Jan-2000 ACCESSIONS A35036; A35613 REFERENCE A35036 !$#authors Misumi, Y.; Ogata, S.; Hirose, S.; Ikehara, Y. !$#journal J. Biol. Chem. (1990) 265:2178-2183 !$#title Primary structure of rat liver 5'-nucleotidase deduced from !1the cDNA. Presence of the COOH-terminal hydrophobic domain !1for possible post-translational modification by !1glycophospholipid. !$#cross-references MUID:90130472; PMID:2298743 !$#accession A35036 !'##molecule_type mRNA !'##residues 1-576 ##label MIS !'##cross-references GB:J05214; NID:g202550; PIDN:AAA40621.1; !1PID:g202551 !'##experimental_source liver !'##note parts of this sequence, including the amino end of the mature !1protein, were confirmed by protein sequencing; the authors !1translated the codon ATG for residue 34 as Leu REFERENCE A35613 !$#authors Ogata, S.; Hayashi, Y.; Misumi, Y.; Ikehara, Y. !$#journal Biochemistry (1990) 29:7923-7927 !$#title Membrane-anchoring domain of rat liver 5'-nucleotidase: !1identification of the COOH-terminal serine-523 covalently !1attached with a glycolipid. !$#cross-references MUID:91084455; PMID:2148114 !$#accession A35613 !'##molecule_type protein !'##residues 538-551 ##label OGA !'##experimental_source liver COMPLEX homodimer FUNCTION !$#description catalyzes hydrolysis of 5'-nucleotides to the corresponding !1nucleosides and phosphate CLASSIFICATION #superfamily 5'-nucleotidase; 5'-nucleotidase homology; !1phosphoesterase core homology KEYWORDS blocked carboxyl end; glycoprotein; homodimer; lipoprotein; !1membrane protein; metalloprotein; phosphatidylinositol !1linkage; phosphoprotein; phosphoric monoester hydrolase; !1zinc FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-551 #product 5'-nucleotidase #status experimental #label !8MAT\ !$29-530 #domain 5'-nucleotidase homology #label NT5\ !$32-121 #domain phosphoesterase core homology #label PEC\ !$552-576 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$55,313,335,349,405 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$551 #modified_site GPI-anchor ethanolamine amidated !8carboxyl end (Ser) (in mature form) #status !8experimental SUMMARY #length 576 #molecular-weight 63968 #checksum 6809 SEQUENCE /// ENTRY S19564 #type complete TITLE 5'-nucleotidase (EC 3.1.3.5) precursor - electric ray (Discopyge ommata) ALTERNATE_NAMES 5'-ribonucleotide phosphohydrolase; ecto-5'-nucleotidase ORGANISM #formal_name Discopyge ommata DATE 10-Mar-1994 #sequence_revision 10-Mar-1994 #text_change 21-Jan-2000 ACCESSIONS S19564; S39810; S17356 REFERENCE S19564 !$#authors Volknandt, W.; Vogel, M.; Pevsner, J.; Misumi, Y.; Ikehara, !1Y.; Zimmermann, H. !$#journal Eur. J. Biochem. (1991) 202:855-861 !$#title Nucleotidase from the electric ray electric lobe. Primary !1structure and relation to mammalian and procaryotic enzymes. !$#cross-references MUID:92111535; PMID:1765099 !$#accession S19564 !'##molecule_type mRNA !'##residues 1-577 ##label VOL1 !'##cross-references EMBL:X62278; NID:g62771; PIDN:CAA44168.1; !1PID:g62772 !$#accession S39810 !'##molecule_type protein !'##residues 30-47 ##label VOL2 FUNCTION !$#description catalyzes hydrolysis of 5'-nucleotides to the corresponding !1nucleosides and phosphate CLASSIFICATION #superfamily 5'-nucleotidase; 5'-nucleotidase homology; !1phosphoesterase core homology KEYWORDS glycoprotein; membrane protein; phosphoric monoester !1hydrolase; zinc FEATURE !$1-29 #domain signal sequence #status predicted #label SIG\ !$30-577 #product 5'-nucleotidase #status experimental #label !8MAT\ !$30-528 #domain 5'-nucleotidase homology #label NT5\ !$33-120 #domain phosphoesterase core homology #label PEC\ !$135,311,347,403 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 577 #molecular-weight 63613 #checksum 950 SEQUENCE /// ENTRY E71365 #type complete TITLE probable 5'-nucleotidase (EC 3.1.3.5) - syphilis spirochete ALTERNATE_NAMES 5'-ribonucleotide phosphohydrolase; ecto-5'-nucleotidase ORGANISM #formal_name Treponema pallidum subsp. pallidum #common_name syphilis spirochete DATE 30-Oct-1998 #sequence_revision 30-Oct-1998 #text_change 11-Jun-1999 ACCESSIONS E71365 REFERENCE A71250 !$#authors Fraser, C.M.; Norris, S.J.; Weinstock, G.M.; White, O.; !1Sutton, G.G.; Dodson, R.; Gwinn, M.; Hickey, E.K.; Clayton, !1R.; Ketchum, K.A.; Sodergren, E.; Hardham, J.M.; McLeod, !1M.P.; Salzberg, S.; Peterson, J.; Khalak, H.; Richardson, !1D.; Howell, J.K.; Chidambaram, M.; Utterback, T.; McDonald, !1L.; Artiach, P.; Bowman, C.; Cotton, M.D.; Fujii, C.; !1Garland, S.; Hatch, B.; Horst, K.; Roberts, K.; Watthey, L.; !1Weidman, J.; Smith, H.O.; Venter, J.C. !$#journal Science (1998) 281:375-388 !$#title Complete genome sequence of Treponema pallidum, the syphilis !1spirochete. !$#cross-references MUID:98332770; PMID:9665876 !$#accession E71365 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-593 ##label COL !'##cross-references GB:AE001195; GB:AE000520; NID:g3322366; !1PIDN:AAC26552.1; PID:g3322367 !'##experimental_source strain Nichols GENETICS !$#gene TP0104 FUNCTION !$#description catalyzes hydrolysis of 5'-ribonucleotides to the !1corresponding ribonucleosides and phosphate CLASSIFICATION #superfamily 5'-nucleotidase; 5'-nucleotidase homology; !1phosphoesterase core homology KEYWORDS phosphoric monoester hydrolase FEATURE !$32-560 #domain 5'-nucleotidase homology #label NT5\ !$35-125 #domain phosphoesterase core homology #label PEC\ !$124 #active_site His #status predicted SUMMARY #length 593 #molecular-weight 64870 #checksum 9033 SEQUENCE /// ENTRY E64054 #type complete TITLE probable 5'-nucleotidase (EC 3.1.3.5) precursor - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES 5'-ribonucleotide phosphohydrolase ORGANISM #formal_name Haemophilus influenzae DATE 18-Aug-1995 #sequence_revision 18-Aug-1995 #text_change 21-Jan-2000 ACCESSIONS E64054 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession E64054 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-603 ##label TIGR !'##cross-references GB:U32705; GB:L42023; NID:g1573156; !1PIDN:AAC21874.1; PID:g1573165; TIGR:HI0206 FUNCTION !$#description catalyzes hydrolysis of 5'-nucleotides to the corresponding !1nucleosides and phosphate CLASSIFICATION #superfamily 5'-nucleotidase; 5'-nucleotidase homology; !1phosphoesterase core homology KEYWORDS periplasmic space; phosphoric monoester hydrolase FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-603 #product probable 5'-nucleotidase #status predicted !8#label MAT\ !$35-563 #domain 5'-nucleotidase homology #label NT5\ !$38-128 #domain phosphoesterase core homology #label PEC SUMMARY #length 603 #molecular-weight 66245 #checksum 7046 SEQUENCE /// ENTRY YXECUG #type complete TITLE UDP-sugar diphosphatase (EC 3.6.1.45) precursor [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES UDP-sugar diphosphatase; UDPglucose hydrolase CONTAINS 5'-nucleotidase (EC 3.1.3.5) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 05-Dec-1997 #text_change 03-Jun-2002 ACCESSIONS G64778; A29276 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64778 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-550 ##label BLAT !'##cross-references GB:AE000154; GB:U00096; NID:g1786683; !1PIDN:AAC73582.1; PID:g1786687; UWGP:b0480 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A29276 !$#authors Burns, D.M.; Beacham, I.R. !$#journal Nucleic Acids Res. (1986) 14:4325-4342 !$#title Nucleotide sequence and transcriptional analysis of the E. !1coli ushA gene, encoding periplasmic UDP-sugar hydrolase !1(5'-nucleotidase): regulation of the ushA gene, and the !1signal sequence of its encoded protein product. !$#cross-references MUID:86232561; PMID:3012467 !$#accession A29276 !'##molecule_type DNA !'##residues 1-255,'T',257-550 ##label BUR !'##cross-references GB:X03895; NID:g43276; PIDN:CAA27532.1; PID:g757842 GENETICS !$#gene ushA !$#map_position 11 min FUNCTION FUN1 !$#description EC 3.6.1.45 [validated, MUID:86232561]; UDP-sugar hydrolase; !1catalyzes the degradation of external UDP-glucose to uridine !1monophosphate and glucose-1-phosphate !$#note cobalt required FUNCTION FUN2 !$#description EC 3.1.3.5 [validated, MUID:86232561]; 5'-nucleotidase !$#note two zinc ions are present in the active site [validated, !1MUID:99260739] CLASSIFICATION #superfamily 5'-nucleotidase; 5'-nucleotidase homology; !1phosphoesterase core homology KEYWORDS cobalt; multifunctional enzyme; periplasmic space; !1phosphoric monoester hydrolase FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-550 #product UDP-sugar hydrolase #status experimental !8#label MAT\ !$32-526 #domain 5'-nucleotidase homology #label NT5\ !$35-118 #domain phosphoesterase core homology #label PEC SUMMARY #length 550 #molecular-weight 60824 #checksum 3228 SEQUENCE /// ENTRY A85546 #type complete TITLE UDP-sugar diphosphatase (EC 3.6.1.45) precursor [similarity] - Escherichia coli (strain O157:H7, substrain EDL933) ALTERNATE_NAMES UDP-sugar diphosphatase; UDPglucose hydrolase CONTAINS 5'-nucleotidase (EC 3.1.3.5) ORGANISM #formal_name Escherichia coli DATE 16-Feb-2001 #sequence_revision 16-Feb-2001 #text_change 03-Jun-2002 ACCESSIONS A85546 REFERENCE A85480 !$#authors Perna, N.T.; Plunkett III, G.; Burland, V.; Mau, B.; !1Glasner, J.D.; Rose, D.J.; Mayhew, G.F.; Evans, P.S.; !1Gregor, J.; Kirkpatrick, H.A.; Posfai, G.; Hackett, J.; !1Klink, S.; Boutin, A.; Shao, Y.; Miller, L.; Grotbeck, E.J.; !1Davis, N.W.; Lim, A.; Dimalanta, E.; Potamousis, K.; !1Apodaca, J.; Anantharaman, T.S.; Lin, J.; Yen, G.; Schwartz, !1D.C.; Welch, R.A.; Blattner, F.R. !$#journal Nature (2001) 409:529-533 !$#title Genome sequence of enterohemorrhagic Escherichia coli !1O157:H7. !$#cross-references MUID:21074935; PMID:11206551 !$#accession A85546 !'##molecule_type DNA !'##residues 1-550 ##label STO !'##cross-references GB:AE005174; NID:g12513353; PIDN:AAG54829.1; !1GSPDB:GN00145; UWGP:Z0599 !'##experimental_source strain O157:H7, substrain EDL933 GENETICS !$#gene ushA CLASSIFICATION #superfamily 5'-nucleotidase; 5'-nucleotidase homology; !1phosphoesterase core homology KEYWORDS cobalt; multifunctional enzyme; periplasmic space; !1phosphoric monoester hydrolase FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-550 #product UDP-sugar hydrolase #status predicted #label !8MAT\ !$32-526 #domain 5'-nucleotidase homology #label NT5\ !$35-118 #domain phosphoesterase core homology #label PEC SUMMARY #length 550 #molecular-weight 60730 #checksum 2645 SEQUENCE /// ENTRY E90695 #type complete TITLE UDP-sugar diphosphatase (EC 3.6.1.45) precursor [similarity] - Escherichia coli (strain O157:H7, substrain RIMD 0509952) ALTERNATE_NAMES UDP-sugar diphosphatase; UDPglucose hydrolase CONTAINS 5'-nucleotidase (EC 3.1.3.5) ORGANISM #formal_name Escherichia coli DATE 18-Jul-2001 #sequence_revision 18-Jul-2001 #text_change 03-Jun-2002 ACCESSIONS E90695 REFERENCE A99629 !$#authors Hayashi, T.; Makino, K.; Ohnishi, M.; Kurokawa, K.; Ishii, !1K.; Yokoyama, K.; Han, C.G.; Ohtsubo, E.; Nakayama, K.; !1Murata, T.; Tanaka, M.; Tobe, T.; Iida, T.; Takami, H.; !1Honda, T.; Sasakawa, C.; Ogasawara, N.; Yasunaga, T.; !1Kuhara, S.; Shiba, T.; Hattori, M.; Shinagawa, H. !$#journal DNA Res. (2001) 8:11-22 !$#title Complete genome sequence of enterohemorrhagic Escherichia !1coli O157:H7 and genomic comparison with a laboratory strain !1K-12. !$#cross-references MUID:21156231; PMID:11258796 !$#accession E90695 !'##molecule_type DNA !'##residues 1-550 ##label HAY !'##cross-references GB:BA000007; PIDN:BAB33956.1; PID:g13359990; !1GSPDB:GN00154 !'##experimental_source strain O157:H7, substrain RIMD 0509952 GENETICS !$#gene ECs0533 CLASSIFICATION #superfamily 5'-nucleotidase; 5'-nucleotidase homology; !1phosphoesterase core homology KEYWORDS cobalt; multifunctional enzyme; periplasmic space; !1phosphoric monoester hydrolase FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-550 #product UDP-sugar hydrolase #status experimental !8#label MAT\ !$32-526 #domain 5'-nucleotidase homology #label NT5\ !$35-118 #domain phosphoesterase core homology #label PEC SUMMARY #length 550 #molecular-weight 60730 #checksum 2645 SEQUENCE /// ENTRY A26076 #type complete TITLE UDP-sugar diphosphatase (EC 3.6.1.45) precursor - Salmonella typhimurium ALTERNATE_NAMES UDPglucose hydrolase CONTAINS 5'-nucleotidase (EC 3.1.3.5) ORGANISM #formal_name Salmonella typhimurium DATE 05-Oct-1988 #sequence_revision 05-Oct-1988 #text_change 03-Jun-2002 ACCESSIONS A26076 REFERENCE A26076 !$#authors Burns, D.M.; Beacham, I.R. !$#journal J. Mol. Biol. (1986) 192:163-175 !$#title Identification and sequence analysis of a silent gene (ushA !1(0)) in Salmonella typhimurium. !$#cross-references MUID:87169716; PMID:3031310 !$#accession A26076 !'##molecule_type DNA !'##residues 1-550 ##label BUR !'##cross-references GB:X04651; NID:g47949; PIDN:CAA28348.1; PID:g47950 COMMENT This protein, though functional, is not detectably expressed !1in this organism, which expresses a biochemically and !1genetically distinct UPD-sugar hydrolase. GENETICS !$#gene ushA(0) CLASSIFICATION #superfamily 5'-nucleotidase; 5'-nucleotidase homology; !1phosphoesterase core homology KEYWORDS phosphoric monoester hydrolase FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-550 #product UDP-sugar hydrolase #status predicted #label !8MAT\ !$32-526 #domain 5'-nucleotidase homology #label NT5\ !$35-118 #domain phosphoesterase core homology #label PEC SUMMARY #length 550 #molecular-weight 60457 #checksum 3843 SEQUENCE /// ENTRY JC7221 #type complete TITLE UDP-sugar diphosphatase (EC 3.6.1.45) precursor [similarity] - Enterobacter aerogenes ALTERNATE_NAMES UDPglucose hydrolase CONTAINS 5'-nucleotidase (EC 3.1.3.5) ORGANISM #formal_name Enterobacter aerogenes DATE 09-Jun-2000 #sequence_revision 09-Jun-2000 #text_change 03-Jun-2002 ACCESSIONS JC7221 REFERENCE JC7221 !$#authors Lee, K.S.; Song, S.B.; Kim, K.E.; Kim, Y.H.; Kim, S.K.; Kho, !1B.H.; Ko, D.K.; Choi, Y.K.; Lee, Y.K.; Kim, C.K.; Kim, Y.C.; !1Lim, J.Y.; Kim, Y.; Min, K.H.; Wanner, B.L. !$#journal Biochem. Biophys. Res. Commun. (2000) 269:526-531 !$#title Cloning and characterization of the UDP-sugar hydrolase gene !1(ushA) of Enterobacter aerogenes IFO 12010. !$#accession JC7221 !'##molecule_type DNA !'##residues 1-550 ##label LEE !'##cross-references GB:AF068226 !'##experimental_source IFO 12010 COMMENT This enzyme is a component of the nucleotide-scavenging !1pathway, and an important factor affecting the host cell !1function following intracellular bacterial infection. It !1hydrolases UDP-sugar into uridine, sugar-1-phosphate and !1orthophosphate and releases inorganic phosphate from UDP !1(uridine 5'-diphosphate)-sugar. GENETICS !$#gene ushA CLASSIFICATION #superfamily 5'-nucleotidase; 5'-nucleotidase homology; !1phosphoesterase core homology KEYWORDS phosphoric monoester hydrolase FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-550 #product UDP-sugar hydrolase #status predicted #label !8MAT\ !$32-526 #domain 5'-nucleotidase homology #label NT5\ !$35-118 #domain phosphoesterase core homology #label PEC SUMMARY #length 550 #molecular-weight 60536 #checksum 4827 SEQUENCE /// ENTRY JX0153 #type complete TITLE 5'-nucleotidase (EC 3.1.3.5) precursor - Vibrio parahaemolyticus plasmid pNUT54 ALTERNATE_NAMES 5'-ribonucleotide phosphohydrolase; ecto-5'-nucleotidase ORGANISM #formal_name Vibrio parahaemolyticus DATE 19-Mar-1997 #sequence_revision 19-Mar-1997 #text_change 16-Jun-2000 ACCESSIONS JX0153 REFERENCE JX0153 !$#authors Tamao, Y.; Noguchi, K.; Sakai-Tomita, Y.; Hama, H.; !1Shimamoto, T.; Kanazawa, H.; Tsuda, M.; Tsuchiya, T. !$#journal J. Biochem. (1991) 109:24-29 !$#title Sequence analysis of nutA gene encoding membrane-bound !1Cl--dependent 5'-nucleotidase of Vibrio parahaemolyticus. !$#cross-references MUID:91201280; PMID:2016269 !$#accession JX0153 !'##molecule_type DNA !'##residues 1-560 ##label TAM !'##cross-references GB:X57711; NID:g48452; PIDN:CAA40882.1; PID:g48453; !1DDBJ:D00910; NID:g217190; PID:g217191 GENETICS !$#gene nutA !$#genome plasmid FUNCTION !$#description catalyzes dephosphorylation of extracellular nucleotides to !1the corresponding nucleosides !$#note nucleosides can cross the cell membrane !$#note requires chloride ion CLASSIFICATION #superfamily 5'-nucleotidase; 5'-nucleotidase homology; !1phosphoesterase core homology KEYWORDS blocked amino end; lipoprotein; membrane protein; phosphoric !1monoester hydrolase FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-560 #product 5'-nucleotidase #status predicted #label !8MAT\ !$36-529 #domain 5'-nucleotidase homology #label NT5\ !$39-122 #domain phosphoesterase core homology #label PEC SUMMARY #length 560 #molecular-weight 62146 #checksum 7811 SEQUENCE /// ENTRY E82108 #type complete TITLE 5'-nucleotidase (EC 3.1.3.5) precursor VC2174 [similarity] - Vibrio cholerae (strain N16961 serogroup O1) ALTERNATE_NAMES 5'-ribonucleotide phosphohydrolase; ecto-5'-nucleotidase ORGANISM #formal_name Vibrio cholerae DATE 18-Aug-2000 #sequence_revision 20-Aug-2000 #text_change 09-Nov-2001 ACCESSIONS E82108 REFERENCE A82035 !$#authors Heidelberg, J.F.; Eisen, J.A.; Nelson, W.C.; Clayton, R.A.; !1Gwinn, M.L.; Dodson, R.J.; Haft, D.H.; Hickey, E.K.; !1Peterson, J.D.; Umayam, L.A.; Gill, S.R.; Nelson, K.E.; !1Read, T.D.; Tettelin, H.; Richardson, D.; Ermolaeva, M.D.; !1Vamathevan, J.; Bass, S.; Qin, H.; Dragoi, I.; Sellers, P.; !1McDonald, L.; Utterback, T.; Fleishmann, R.D.; Nierman, !1W.C.; White, O.; Salzberg, S.L.; Smith, H.O.; Colwell, R.R.; !1Mekalanos, J.J.; Venter, J.C.; Fraser, C.M. !$#journal Nature (2000) 406:477-483 !$#title DNA Sequence of both chromosomes of the cholera pathogen !1Vibrio cholerae. !$#cross-references MUID:20406833; PMID:10952301 !$#accession E82108 !'##molecule_type DNA !'##residues 1-553 ##label HEI !'##cross-references GB:AE004289; GB:AE003852; NID:g9656725; !1PIDN:AAF95319.1; GSPDB:GN00126; TIGR:VC2174 !'##experimental_source serogroup O1; strain N16961; biotype El Tor GENETICS !$#gene VC2174 !$#map_position 1 CLASSIFICATION #superfamily 5'-nucleotidase; 5'-nucleotidase homology; !1phosphoesterase core homology KEYWORDS phosphoric monoester hydrolase FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-553 #product 5'-nucleotidase #status predicted #label !8MAT\ !$36-529 #domain 5'-nucleotidase homology #label NT5\ !$39-122 #domain phosphoesterase core homology #label PEC SUMMARY #length 553 #molecular-weight 60903 #checksum 696 SEQUENCE /// ENTRY D69359 #type complete TITLE probable 5'-nucleotidase (EC 3.1.3.5) precursor - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 05-Dec-1997 #sequence_revision 05-Dec-1997 #text_change 11-Jun-1999 ACCESSIONS D69359 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession D69359 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-584 ##label KLE !'##cross-references GB:AE001044; GB:AE000782; NID:g2689367; !1PIDN:AAB90365.1; PID:g2649728; TIGR:AF0876 CLASSIFICATION #superfamily 5'-nucleotidase; 5'-nucleotidase homology; !1phosphoesterase core homology KEYWORDS phosphoric monoester hydrolase FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-584 #product 5'-nucleotidase #status predicted #label !8MAT\ !$22-477 #domain 5'-nucleotidase homology #label NT5 SUMMARY #length 584 #molecular-weight 63933 #checksum 5611 SEQUENCE /// ENTRY G89760 #type complete TITLE probable 5'-nucleotidase (EC 3.1.3.5) SA0022 precursor [similarity] - Staphylococcus aureus (strain N315) ORGANISM #formal_name Staphylococcus aureus DATE 03-Aug-2001 #sequence_revision 03-Aug-2001 #text_change 22-Oct-2001 ACCESSIONS G89760 REFERENCE A89758 !$#authors Kuroda, M.; Ohta, T.; Uchiyama, I.; Baba, T.; Yuzawa, H.; !1Kobayashi, I.; Cui, L.; Oguchi, A.; Aoki, K.; Nagai, Y.; !1Lian, J.; Ito, T.; Kanamori, M.; Matsumaru, H.; Maruyama, !1A.; Murakami, H.; Hosoyama, A.; Mizutani-Ui, Y.; Kobayashi, !1N.; Sawano, T.; Inoue, R.; Kaito, C.; Sekimizu, K.; !1Hirakawa, H.; Kuhara, S.; Goto, S.; Yabuzaki, J.; Kanehisa, !1M.; Yamashita, A.; Oshima, K.; Furuya, K.; Yoshino, C.; !1Shiba, T.; Hattori, M.; Ogasawara, N.; Hayashi, H.; !1Hiramatsu, K. !$#journal Lancet (2001) 357:1225-1240 !$#title Whole genome sequencing of meticillin-resistant !1Stapylococcus aureus. !$#cross-references MUID:21311952; PMID:11418146 !$#accession G89760 !'##molecule_type DNA !'##residues 1-772 ##label KUR !'##cross-references GB:BA000018; PID:g13699940; PIDN:BAB41239.1; !1GSPDB:GN00149 !'##experimental_source strain N315 COMMENT May have UDP-sugar hydrolase (EC 3.6.1.45) activity. GENETICS !$#gene SA0022 CLASSIFICATION #superfamily Staphylococcus aureus probable 5'-nucleotidase !1SA0022; 5'-nucleotidase homology; phosphoesterase core !1homology KEYWORDS phosphoric monoester hydrolase FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-772 #product probable 5'-nucleotidase #status predicted !8#label MAT\ !$150-225 #domain phosphoesterase core homology #label PEC\ !$151-623 #domain 5'-nucleotidase homology #label NT5 SUMMARY #length 772 #molecular-weight 83498 #checksum 4094 SEQUENCE /// ENTRY A64726 #type complete TITLE bis(5'-nucleosyl)-tetraphosphatase (symmetrical) (EC 3.6.1.41) - Escherichia coli (strain K-12) ALTERNATE_NAMES diadenosine tetraphosphatase (symmetrical) ORGANISM #formal_name Escherichia coli DATE 12-Sep-1997 #sequence_revision 17-Sep-1997 #text_change 01-Mar-2002 ACCESSIONS A64726; A26221; S40570; Q00021 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64726 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-280 ##label BLAT !'##cross-references GB:AE000115; GB:U00096; NID:g1786230; !1PIDN:AAC73160.1; PID:g1786234; UWGP:b0049 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A26221 !$#authors Blanchin-Roland, S.; Blanquet, S.; Schmitter, J.M.; Fayat, !1G. !$#journal Mol. Gen. Genet. (1986) 205:515-522 !$#title The gene for Escherichia coli diadenosine tetraphosphatase !1is located immediately clockwise to folA and forms an operon !1with ksgA. !$#cross-references MUID:87172305; PMID:3031429 !$#accession A26221 !'##molecule_type DNA !'##residues 1-82,'L',84-274,'A',276-280 ##label BLA !'##cross-references GB:D10483; GB:J01597; GB:J01683; GB:J01706; !1GB:K01298; GB:K01990; GB:M10420; GB:M10611; GB:M12544; !1NID:g216434; PIDN:BAA01325.1; PID:g216474 REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40570 !'##molecule_type DNA !'##residues 1-82,'L',84-274,'A',276-280 ##label YUR !'##cross-references EMBL:D10483; NID:g216434; PIDN:BAA01325.1; !1PID:g216474 !'##note apaH gene product is adenosine-tetraphosphatase (EC 3.6.1.14) !1according to EMBL annotation GENETICS !$#gene apaH !$#map_position 1 min FUNCTION !$#pathway purine metabolism CLASSIFICATION #superfamily bis(5'-nucleosyl)-tetraphosphatase !1(symmetrical); phosphoesterase core homology KEYWORDS hydrolase FEATURE !$2-67 #domain phosphoesterase core homology #label PEC SUMMARY #length 280 #molecular-weight 31296 #checksum 4835 SEQUENCE /// ENTRY B42379 #type fragment TITLE bis(5'-nucleosyl)-tetraphosphatase (symmetrical) (EC 3.6.1.41) - Klebsiella pneumoniae (fragment) ALTERNATE_NAMES diadenosine tetraphosphatase (symmetrical) ORGANISM #formal_name Klebsiella pneumoniae DATE 16-Sep-1992 #sequence_revision 16-Sep-1992 #text_change 16-Jun-2000 ACCESSIONS B42379 REFERENCE A42379 !$#authors Azakami, H.; Sugino, H.; Murooka, Y. !$#journal J. Bacteriol. (1992) 174:2344-2351 !$#title Cloning and nucleotide sequence of a negative regulator gene !1for Klebsiella aerogenes arylsulfatase synthesis and !1identification of the gene as folA. !$#cross-references MUID:92202165; PMID:1551851 !$#accession B42379 !'##molecule_type DNA !'##residues 1-259 ##label AZA !'##cross-references GB:D10358; NID:g216718; PIDN:BAA01188.1; !1PID:g216720 !'##experimental_source strain W20 GENETICS !$#gene apaH FUNCTION !$#pathway purine metabolism CLASSIFICATION #superfamily bis(5'-nucleosyl)-tetraphosphatase !1(symmetrical); phosphoesterase core homology KEYWORDS hydrolase SUMMARY #length 259 #checksum 8353 SEQUENCE /// ENTRY B64077 #type complete TITLE bis(5'-nucleosyl)-tetraphosphatase (symmetrical) (EC 3.6.1.41) - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES diadenosine tetraphosphatase (symmetrical) ORGANISM #formal_name Haemophilus influenzae DATE 18-Aug-1995 #sequence_revision 18-Aug-1995 #text_change 11-Jun-1999 ACCESSIONS B64077 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession B64077 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-275 ##label TIGR !'##cross-references GB:U32737; GB:L42023; NID:g1573536; !1PIDN:AAC22209.1; PID:g1573537; TIGR:HI0551 !'##experimental_source strain Rd KW20 GENETICS !$#note TIGR:HI0551 FUNCTION !$#pathway purine metabolism CLASSIFICATION #superfamily bis(5'-nucleosyl)-tetraphosphatase !1(symmetrical); phosphoesterase core homology KEYWORDS hydrolase FEATURE !$2-67 #domain phosphoesterase core homology #label PEC SUMMARY #length 275 #molecular-weight 31908 #checksum 7950 SEQUENCE /// ENTRY PAPGF #type complete TITLE fructose-bisphosphatase (EC 3.1.3.11) - pig ALTERNATE_NAMES D-fructose-1,6-bisphosphate 1-phosphohydrolase; Fru-P2ase ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 05-Apr-1983 #sequence_revision 23-Aug-1997 #text_change 23-Sep-2002 ACCESSIONS S37696; A93937; A90070; A00778 REFERENCE S37696 !$#authors Williams, M.K.; Kantrowitz, E.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:3080-3082 !$#title Isolation and sequence analysis of the cDNA for pig kidney !1fructose 1,6-bisphosphatase. !$#cross-references MUID:92212971; PMID:1313579 !$#accession S37696 !'##molecule_type mRNA !'##residues 1-337 ##label WIL !'##cross-references EMBL:M86347; NID:g164456; PIDN:AAA31035.1; !1PID:g456571 REFERENCE A93937 !$#authors Marcus, F.; Edelstein, I.; Reardon, I.; Heinrikson, R.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:7161-7165 !$#title Complete amino acid sequence of pig kidney fructose-1, !16-bisphosphatase. !$#cross-references MUID:83117639; PMID:6296821 !$#accession A93937 !'##molecule_type protein !'##residues 1-19,'Q',21-95,'T',97-155,'E',157-198,'N',200-227,'E', !1229-335 ##label MAR !'##experimental_source kidney cortex REFERENCE A90070 !$#authors Macgregor, J.S.; Hannappel, E.; Xu, G.J.; Pontremoli, S.; !1Horecker, B.L. !$#journal Arch. Biochem. Biophys. (1982) 217:652-664 !$#title Conservation of primary structure at the !1proteinase-sensitive site of fructose 1,6-bisphosphatases. !$#cross-references MUID:83047209; PMID:6291465 !$#accession A90070 !'##molecule_type protein !'##residues 'A',2,'E',4-23;24,44-60 ##label MAC !'##experimental_source kidney REFERENCE A90014 !$#authors Benkovic, S.J.; deMaine, M.M. !$#journal Adv. Enzymol. (1982) 53:45-82 !$#title Advances in enzymology and related areas of molecular !1biology. !$#cross-references MUID:82132308; PMID:6277165 !$#contents annotation; binding of substrate and ligands, a review COMMENT The enzyme is necessary for, and specific to, !1gluconeogenesis. It catalyzes the hydrolysis of fructose-1, !16-bisphosphate to fructose-6-phosphate. COMMENT The enzyme is inhibited by AMP, which affects the turnover !1of bound substrate and not the affinity for substrate. COMMENT The molecule is a tetramer with four binding sites each for !1the substrate, for AMP, and for divalent metal cation (the !1greatest affinity is for zinc). COMMENT The molecule has a highly reactive cysteine residue (Cys-116 !1or Cys-128), which tends to form mixed disulfides (e.g., !1with homocystine) but is not essential for enzyme activity. CLASSIFICATION #superfamily fructose-bisphosphatase KEYWORDS acetylated amino end; gluconeogenesis; phosphoprotein; !1phosphoric monoester hydrolase; tetramer FEATURE !$1 #modified_site acetylated amino end (Thr) #status !8experimental\ !$141 #binding_site AMP, allosteric (Lys) #status !8predicted\ !$207 #binding_site phosphate (Ser) (covalent) #status !8experimental\ !$274 #active_site Lys #status predicted SUMMARY #length 337 #molecular-weight 36648 #checksum 2054 SEQUENCE /// ENTRY PASPY #type complete TITLE fructose-bisphosphatase (EC 3.1.3.11), cytosolic - spinach ORGANISM #formal_name Spinacia oleracea #common_name spinach DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 11-Jun-1999 ACCESSIONS S20852; S09335 REFERENCE S20852 !$#authors Hur, Y.; Unger, E.A.; Vasconcelos, A.C. !$#journal Plant Mol. Biol. (1992) 18:799-802 !$#title Isolation and characterization of a cDNA encoding cytosolic !1fructose-1,6-bisphosphatase from spinach. !$#cross-references MUID:92216057; PMID:1313712 !$#accession S20852 !'##molecule_type mRNA !'##residues 1-341 ##label HUR !'##cross-references EMBL:X61690; NID:g21244; PIDN:CAA43860.1; !1PID:g21245 REFERENCE S09335 !$#authors Ladror, U.S.; Latshaw, S.P.; Marcus, F. !$#journal Eur. J. Biochem. (1990) 189:89-94 !$#title Spinach cytosolic fructose-1,6-bisphosphatase. Purification, !1enzyme properties and structural comparisons. !$#cross-references MUID:90235866; PMID:2158892 !$#accession S09335 !'##molecule_type protein !'##residues 10-53;59-122,'F',124-130;191-341 ##label LAD FUNCTION !$#description catalyzes the hydrolysis of fructose-1,6,-bisphosphate to !1fructose 6-phosphate and orthophosphate !$#pathway gluconeogenesis CLASSIFICATION #superfamily fructose-bisphosphatase KEYWORDS gluconeogenesis; phosphoric monoester hydrolase FEATURE !$277 #active_site Lys #status predicted SUMMARY #length 341 #molecular-weight 37198 #checksum 9099 SEQUENCE /// ENTRY PAWTF #type complete TITLE fructose-bisphosphatase (EC 3.1.3.11) precursor, chloroplast - wheat ORGANISM #formal_name Triticum aestivum #common_name common wheat DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 11-Jun-1999 ACCESSIONS S14060; S01617 REFERENCE S14060 !$#authors Lloyd, J.C.; Raines, C.A.; John, U.P.; Dyer, T.A. !$#journal Mol. Gen. Genet. (1991) 225:209-216 !$#title The chloroplast FBPase gene of wheat: structure and !1expression of the promoter in photosynthetic and !1meristematic cells of transgenic tobacco plants. !$#cross-references MUID:91172118; PMID:1848650 !$#accession S14060 !'##molecule_type DNA !'##residues 1-409 ##label LLO !'##cross-references EMBL:X53957; NID:g21740; PIDN:CAA37908.1; !1PID:g21741 REFERENCE S01617 !$#authors Raines, C.A.; Lloyd, J.C.; Longstaff, M.; Bradley, D.; Dyer, !1T. !$#journal Nucleic Acids Res. (1988) 16:7931-7942 !$#title Chloroplast fructose-1,6-bisphosphatase: the product of a !1mosaic gene. !$#cross-references MUID:88335538; PMID:2843806 !$#accession S01617 !'##molecule_type mRNA !'##residues 1-409 ##label RAI !'##cross-references EMBL:X07780; NID:g21736; PIDN:CAA30612.1; !1PID:g21737 GENETICS !$#introns 142/3; 215/3; 384/3 CLASSIFICATION #superfamily fructose-bisphosphatase KEYWORDS Calvin cycle; chloroplast; gluconeogenesis; phosphoric !1monoester hydrolase FEATURE !$1-51 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$52-409 #product fructose-bisphosphatase #status predicted !8#label MAT SUMMARY #length 409 #molecular-weight 44218 #checksum 4302 SEQUENCE /// ENTRY PASPC #type complete TITLE fructose-bisphosphatase (EC 3.1.3.11), chloroplast - spinach ORGANISM #formal_name Spinacia oleracea #common_name spinach DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 13-Mar-1998 ACCESSIONS S09587; B37295; A28046; A31315 REFERENCE S09587 !$#authors Marcus, F.; Harrsch, P.B. !$#journal Arch. Biochem. Biophys. (1990) 279:151-157 !$#title Amino acid sequence of spinach chloroplast fructose-1, !16-bisphosphatase. !$#cross-references MUID:90247882; PMID:2159755 !$#accession S09587 !'##molecule_type protein !'##residues 1-358 ##label MAR REFERENCE A37295 !$#authors Harrsch, P.B.; Kim, Y.; Fox, J.L.; Marcus, F. !$#journal Biochem. Biophys. Res. Commun. (1985) 133:520-526 !$#title Amino acid sequence similarity between spinach chloroplast !1and mammalian gluconeogenic fructose-1,6-bisphosphatase. !$#cross-references MUID:86103320; PMID:3002349 !$#accession B37295 !'##status preliminary !'##molecule_type protein !'##residues 82-96;206-225;303-345 ##label HAR CLASSIFICATION #superfamily fructose-bisphosphatase KEYWORDS Calvin cycle; chloroplast; phosphoric monoester hydrolase SUMMARY #length 358 #molecular-weight 39143 #checksum 5859 SEQUENCE /// ENTRY PABY #type complete TITLE fructose-bisphosphatase (EC 3.1.3.11) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein L8039.18; protein YLR377c ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 12-Nov-1999 ACCESSIONS S01127; A28653; S51394; A24242; S05773 REFERENCE S01127 !$#authors Entian, K.D.; Vogel, R.F.; Rose, M.; Hofmann, L.; Mecke, D. !$#journal FEBS Lett. (1988) 236:195-200 !$#title Isolation and primary structure of the gene encoding !1fructose-1,6-bisphosphatase from Saccharomyces cerevisiae. !$#cross-references MUID:88296871; PMID:2841162 !$#accession S01127 !'##molecule_type DNA !'##residues 1-348 ##label ENT !'##cross-references EMBL:Y00754; NID:g3697; PIDN:CAA68723.1; PID:g3698 REFERENCE A28653 !$#authors Rogers, D.T.; Hiller, E.; Mitsock, L.; Orr, E. !$#journal J. Biol. Chem. (1988) 263:6051-6057 !$#title Characterization of the gene for fructose-1,6-bisphosphatase !1from Saccharomyces cerevisiae and Schizosaccharomyces pombe. !1Sequence, protein homology, and expression during growth on !1glucose. !$#cross-references MUID:88198137; PMID:2834361 !$#accession A28653 !'##molecule_type DNA !'##residues 1-348 ##label ROG !'##cross-references EMBL:J03207; NID:g171507; PIDN:AAA34603.1; !1PID:g171508 REFERENCE S51377 !$#authors Du, Z. !$#submission submitted to the EMBL Data Library, December 1994 !$#description The sequence of S. cerevisiae cosmid 8039. !$#accession S51394 !'##molecule_type DNA !'##residues 1-348 ##label DUZ !'##cross-references EMBL:U19103; NID:g609404; PIDN:AAB67579.1; !1PID:g609422; GSPDB:GN00012; MIPS:YLR377c REFERENCE A24242 !$#authors Marcus, F.; Gontero, B.; Harrsch, P.B.; Rittenhouse, J. !$#journal Biochem. Biophys. Res. Commun. (1986) 135:374-381 !$#title Amino acid sequence homology among fructose-1, !16-bisphosphatases. !$#cross-references MUID:86186761; PMID:3008716 !$#accession A24242 !'##molecule_type protein !'##residues 10-25;83-97;256-277,'D',279-280;289-306;327-346 ##label MAR REFERENCE S05773 !$#authors Rittenhouse, J.; Harrsch, P.B.; Kim, J.N.; Marcus, F. !$#journal J. Biol. Chem. (1986) 261:3939-3943 !$#title Amino acid sequence of the phosphorylation site of yeast !1(Saccharomyces cerevisiae) fructose-1,6-bisphosphatase. !$#cross-references MUID:86140201; PMID:3005313 !$#accession S05773 !'##molecule_type protein !'##residues 2-25 ##label RIT GENETICS !$#gene SGD:FBP1; MIPS:YLR377c !'##cross-references SGD:S0004369; MIPS:YLR377c !$#map_position 12R CLASSIFICATION #superfamily fructose-bisphosphatase KEYWORDS gluconeogenesis; homotetramer; phosphoprotein; phosphoric !1monoester hydrolase FEATURE !$2-348 #product fructose-bisphosphatase #status experimental !8#label MAT\ !$12 #binding_site phosphate (Ser) (covalent) #status !8experimental\ !$286 #active_site Lys #status predicted SUMMARY #length 348 #molecular-weight 38262 #checksum 1682 SEQUENCE /// ENTRY PAEC #type complete TITLE fructose-bisphosphatase (EC 3.1.3.11) - Escherichia coli (strain K-12) ALTERNATE_NAMES fructose-1,6-bisphosphatase ORGANISM #formal_name Escherichia coli DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 01-Mar-2002 ACCESSIONS S01383; B24242; S56458; C65235 REFERENCE S01383 !$#authors Hamilton, W.D.O.; Harrison, D.A.; Dyer, T.A. !$#journal Nucleic Acids Res. (1988) 16:8707 !$#title Sequence of the Escherichia coli fructose-1,6-bisphosphatase !1gene. !$#cross-references MUID:88335617; PMID:2843822 !$#accession S01383 !'##molecule_type DNA !'##residues 1-332 ##label HAM !'##cross-references EMBL:X12545; NID:g41415; PIDN:CAA31062.1; !1PID:g41416 REFERENCE A24242 !$#authors Marcus, F.; Gontero, B.; Harrsch, P.B.; Rittenhouse, J. !$#journal Biochem. Biophys. Res. Commun. (1986) 135:374-381 !$#title Amino acid sequence homology among fructose-1, !16-bisphosphatases. !$#cross-references MUID:86186761; PMID:3008716 !$#accession B24242 !'##molecule_type protein !'##residues 43-51,'Q',53-62;220-229;239-249;254-269;297-308 ##label MAR REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56458 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-332 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97129.1; !1PID:g537074 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65235 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-332 ##label BLAT !'##cross-references GB:AE000494; GB:U00096; NID:g1790670; !1PIDN:AAC77189.1; PID:g1790679; UWGP:b4232 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene fbp CLASSIFICATION #superfamily fructose-bisphosphatase KEYWORDS gluconeogenesis; phosphoric monoester hydrolase SUMMARY #length 332 #molecular-weight 36834 #checksum 9951 SEQUENCE /// ENTRY PAQXF #type complete TITLE fructose-bisphosphatase (EC 3.1.3.11) - Xanthobacter flavus CONTAINS sedoheptulose-bisphosphatase (EC 3.1.3.37) ORGANISM #formal_name Xanthobacter flavus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 31-Mar-2000 ACCESSIONS A45867; S13576 REFERENCE A45867 !$#authors Meijer, W.G.; Enequist, H.G.; Terpstra, P.; Dijkhuizen, L. !$#journal J. Gen. Microbiol. (1990) 136:2225-2230 !$#title Nucleotide sequences of the genes encoding !1fructosebisphosphatase and phosphoribulokinase from !1Xanthobacter flavus H4-14. !$#cross-references MUID:91178501; PMID:1964170 !$#accession A45867 !'##molecule_type DNA !'##residues 1-364 ##label ME2 !'##cross-references EMBL:X17252; NID:g48543; PIDN:CAA35118.1; !1PID:g48547 REFERENCE S13573 !$#authors Meijer, W.G.; Arnberg, A.C.; Enequist, H.G.; Terpstra, P.; !1Lidstrom, M.E.; Dijkhuizen, L. !$#journal Mol. Gen. Genet. (1991) 225:320-330 !$#title Identification and organization of carbon dioxide fixation !1genes in Xanthobacter flavus H4-14. !$#cross-references MUID:91172133; PMID:1900916 !$#accession S13576 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-364 ##label ME1 !'##cross-references EMBL:X17252; NID:g48543; PIDN:CAA35118.1; !1PID:g48547 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1989 GENETICS !$#gene cfxF CLASSIFICATION #superfamily fructose-bisphosphatase KEYWORDS Calvin cycle; phosphoric monoester hydrolase SUMMARY #length 364 #molecular-weight 38738 #checksum 1729 SEQUENCE /// ENTRY PARFAS #type complete TITLE fructose-bisphosphatase (EC 3.1.3.11) A - Rhodobacter sphaeroides ALTERNATE_NAMES hexosediphosphatase ORGANISM #formal_name Rhodobacter sphaeroides DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 11-Jun-1999 ACCESSIONS A40767 REFERENCE A40767 !$#authors Gibson, J.L.; Falcone, D.L.; Tabita, F.R. !$#journal J. Biol. Chem. (1991) 266:14646-14653 !$#title Nucleotide sequence, transcriptional analysis, and !1expression of genes encoded within the form I CO-2 fixation !1operon of Rhodobacter sphaeroides. !$#cross-references MUID:91317831; PMID:1907281 !$#accession A40767 !'##molecule_type DNA !'##residues 1-333 ##label GIB !'##cross-references GB:M64624; NID:g151920; PIDN:AAA26112.1; !1PID:g151921 COMMENT This protein is encoded within the form I !1ribulose-bisphosphate carboxylase operon, which predominates !1when carbon dioxide is limiting. GENETICS !$#gene fbpA !$#start_codon GUG CLASSIFICATION #superfamily fructose-bisphosphatase KEYWORDS Calvin cycle; gluconeogenesis; phosphoric monoester !1hydrolase SUMMARY #length 333 #molecular-weight 35996 #checksum 4723 SEQUENCE /// ENTRY A48251 #type complete TITLE glucose-6-phosphatase (EC 3.1.3.9) - human ORGANISM #formal_name Homo sapiens #common_name man DATE 28-Jan-2000 #sequence_revision 28-Jan-2000 #text_change 20-Apr-2000 ACCESSIONS A48251 REFERENCE A48251 !$#authors Lei, K.J.; Shelly, L.L.; Pan, C.J.; Sidbury, J.B.; Chou, !1J.Y. !$#journal Science (1993) 262:580-583 !$#title Mutations in the glucose-6-phosphatase gene that cause !1glycogen storage disease type 1a. !$#cross-references MUID:94024015; PMID:8211187 !$#accession A48251 !'##status preliminary !'##molecule_type mRNA !'##residues 1-357 ##label LEI !'##cross-references GB:U01120; NID:g452443; PIDN:AAA16222.1; !1PID:g452444 GENETICS !$#gene GDB:G6PC; G6PT; GSD1a !'##cross-references GDB:231927; OMIM:232200 !$#map_position 17q21-17q21 CLASSIFICATION #superfamily glucose-6-phosphatase; glucose-6-phosphatase !1catalytic domain homology KEYWORDS endoplasmic reticulum; gluconeogenesis; glycoprotein; !1membrane bound; nuclear membrane; phosphoric monoester !1hydrolase; transmembrane protein FEATURE !$52-191 #domain glucose-6-phosphatase catalytic domain !8homology #label GPH SUMMARY #length 357 #molecular-weight 40513 #checksum 5785 SEQUENCE /// ENTRY A48589 #type complete TITLE glucose-6-phosphatase (EC 3.1.3.9) - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 28-Jan-2000 #sequence_revision 28-Jan-2000 #text_change 03-Mar-2000 ACCESSIONS A48589 REFERENCE A48589 !$#authors Shelly, L.L.; Lei, K.J.; Pan, C.J.; Sakata, S.F.; Ruppert, !1S.; Schutz, G.; Chou, J.Y. !$#journal J. Biol. Chem. (1993) 268:21482-21485 !$#title Isolation of the gene for murine glucose-6-phosphatase, the !1enzyme deficient in glycogen storage disease type 1A. !$#cross-references MUID:94012716; PMID:8407995 !$#accession A48589 !'##status preliminary !'##molecule_type mRNA !'##residues 1-357 ##label SHE !'##cross-references GB:U00445; NID:g425406; PIDN:AAC52122.1; !1PID:g425407 CLASSIFICATION #superfamily glucose-6-phosphatase; glucose-6-phosphatase !1catalytic domain homology KEYWORDS endoplasmic reticulum; gluconeogenesis; glycoprotein; !1membrane bound; nuclear membrane; phosphoric monoester !1hydrolase; transmembrane protein FEATURE !$52-191 #domain glucose-6-phosphatase catalytic domain !8homology #label GPH SUMMARY #length 357 #molecular-weight 40480 #checksum 2647 SEQUENCE /// ENTRY JC2371 #type complete TITLE glucose-6-phosphatase (EC 3.1.3.9) catalytic chain - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 28-Jan-2000 #sequence_revision 28-Jan-2000 #text_change 03-Mar-2000 ACCESSIONS JC2371; JC2233; I55620 REFERENCE JC2233 !$#authors Lange, A.J.; Argaud, D.; El-Maghrabi, M.R.; Pan, W.; Maitra, !1S.R.; Pilkis, S.J. !$#journal Biochem. Biophys. Res. Commun. (1994) 201:302-309 !$#title Isolation of A cDNA for the catalytic subunit of rat liver !1glucose-6-phosphatase: regulation of gene expression in FAO !1hepatoma cells by insulin, dexamethasone and cAMP. !$#cross-references MUID:94256995; PMID:8198588 !$#accession JC2371 !'##molecule_type mRNA !'##residues 1-357 ##label LAN !'##cross-references EMBL:U07993; NID:g508225; PIDN:AAA19966.1; !1PID:g508226 !'##experimental_source liver !$#accession JC2233 !'##molecule_type mRNA !'##residues 1-357 ##label LA2 !'##cross-references EMBL:U07993; NID:g508225; PIDN:AAA19966.1; !1PID:g508226 !'##experimental_source liver REFERENCE I55620 !$#authors Haber, B.A.; Chin, S.; Chuang, E.; Buikhuisen, W.; Naji, A.; !1Taub, R. !$#journal J. Clin. Invest. (1995) 95:832-841 !$#title High levels of glucose-6-phosphatase gene and protein !1expression reflect an adaptive response in proliferating !1liver and diabetes. !$#cross-references MUID:95164719; PMID:7860767 !$#accession I55620 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 5-117,'G',119-357 ##label RES !'##cross-references GB:L37333; NID:g567863; PIDN:AAA74381.1; !1PID:g567864 COMMENT This enzyme catalyzes the terminal step in gluconeogenesis !1and is a key enzyme in the homeostatic regulation of blood !1glucose concentration. COMMENT This enzyme, a key enzyme in the homeostatic regulation of !1blood glucose concentration, catalyzes the terminal step in !1gluconeogenesis. GENETICS !$#gene G6Pase CLASSIFICATION #superfamily glucose-6-phosphatase; glucose-6-phosphatase !1catalytic domain homology KEYWORDS endoplasmic reticulum; gluconeogenesis; glycoprotein; !1membrane bound; nuclear membrane; phosphoric monoester !1hydrolase; transmembrane protein FEATURE !$52-191 #domain glucose-6-phosphatase catalytic domain !8homology #label GPH\ !$96,203,276 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 357 #molecular-weight 40597 #checksum 4637 SEQUENCE /// ENTRY C69621 #type complete TITLE fructose-bisphosphatase (EC 3.1.3.11) [validated] - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 05-Dec-1997 #sequence_revision 05-Dec-1997 #text_change 03-Jun-2002 ACCESSIONS C69621 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69621 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-671 ##label KUN !'##cross-references GB:Z99124; GB:AL009126; NID:g2636442; !1PIDN:CAB16056.1; PID:g2636566 !'##experimental_source strain 168 GENETICS !$#gene fbp; yydE FUNCTION !$#description catalyzes the hydrolysis of fructose-1,6-bisphosphate to !1fructose-6-phosphate and orthophosphate [validated, !1PMID:9696785] !$#pathway gluconeogenesis !$#note requires manganese ion for stability and phosphoenolpyruvate !1for activation CLASSIFICATION #superfamily Bacillus subtilis fructose-bisphosphatase; !1phosphoesterase core homology KEYWORDS carbohydrate metabolism; gluconeogenesis; metalloprotein; !1phosphoric monoester hydrolase SUMMARY #length 671 #molecular-weight 77978 #checksum 2936 SEQUENCE /// ENTRY E90055 #type complete TITLE fructose-bisphosphatase (EC 3.1.3.11) [similarity] - Staphylococcus aureus (strain N315) ORGANISM #formal_name Staphylococcus aureus DATE 10-May-2001 #sequence_revision 10-May-2001 #text_change 11-Jan-2002 ACCESSIONS E90055 REFERENCE A89758 !$#authors Kuroda, M.; Ohta, T.; Uchiyama, I.; Baba, T.; Yuzawa, H.; !1Kobayashi, I.; Cui, L.; Oguchi, A.; Aoki, K.; Nagai, Y.; !1Lian, J.; Ito, T.; Kanamori, M.; Matsumaru, H.; Maruyama, !1A.; Murakami, H.; Hosoyama, A.; Mizutani-Ui, Y.; Kobayashi, !1N.; Sawano, T.; Inoue, R.; Kaito, C.; Sekimizu, K.; !1Hirakawa, H.; Kuhara, S.; Goto, S.; Yabuzaki, J.; Kanehisa, !1M.; Yamashita, A.; Oshima, K.; Furuya, K.; Yoshino, C.; !1Shiba, T.; Hattori, M.; Ogasawara, N.; Hayashi, H.; !1Hiramatsu, K. !$#journal Lancet (2001) 357:1225-1240 !$#title Whole genome sequencing of meticillin-resistant !1Stapylococcus aureus. !$#cross-references MUID:21311952; PMID:11418146 !$#accession E90055 !'##molecule_type DNA !'##residues 1-654 ##label KUR !'##cross-references GB:BA000018; PID:g13702466; PIDN:BAB43607.1; !1GSPDB:GN00149 !'##experimental_source strain N315 GENETICS !$#gene fbp FUNCTION !$#description catalyzes the hydrolysis of fructose-1,6-bisphosphate to !1fructose-6-phosphate and orthophosphate !$#pathway gluconeogenesis CLASSIFICATION #superfamily Bacillus subtilis fructose-bisphosphatase; !1phosphoesterase core homology KEYWORDS carbohydrate metabolism; gluconeogenesis; metalloprotein; !1phosphoric monoester hydrolase SUMMARY #length 654 #molecular-weight 76174 #checksum 9197 SEQUENCE /// ENTRY AI1535 #type complete TITLE fructose-bisphosphatase (EC 3.1.3.11) [similarity] - Listeria innocua (strain Clip11262) ORGANISM #formal_name Listeria innocua DATE 27-Nov-2001 #sequence_revision 27-Nov-2001 #text_change 11-Jan-2002 ACCESSIONS AI1535 REFERENCE AB1077 !$#authors Glaser, P.; Frangeul, L.; Buchrieser, C.; Amend, A.; !1Baquero, F.; Berche, P.; Bloecker, H.; Brandt, P.; !1Chakraborty, T.; Charbit, A.; Chetouani, F.; Couve, E.; de !1Daruvar, A.; Dehoux, P.; Domann, E.; Dominguez-Bernal, G.; !1Duchaud, E.; Durand, L.; Dussurget, O.; Entian, K.D.; Fsihi, !1H.; Garcia-Del Portillo, F.; Garrido, P.; Gautier, L.; !1Goebel, W.; Gomez-Lopez, N.; Hain, T.; Hauf, J.; Jackson, !1D.; Jones, L.M.; Karst, U.; Kreft, J.; Kuhn, M.; Kunst, F.; !1Kurapkat, G.; Madueno, E.; Maitournam, A.; Mata Vicente, J.; !1Ng, E.; Nordsiek, G.; Novella, S.; de Pablos, B.; !1Perez-Diaz, J.C.; Remmel, B.; Rose, M.; Rusniok, C.; !1Schlueter, T.; Simoes, N.; Tierrez, A.; Vazquez-Boland, !1J.A.; Voss, H.; Wehland, J.; Cossart, P. !$#journal Science (2001) 294:849-852 !$#title Comparative genomics of Listeria species. !$#cross-references MUID:21537279; PMID:11679669 !$#accession AI1535 !'##molecule_type DNA !'##residues 1-653 ##label GLA !'##cross-references GB:AL592022; PIDN:CAC96057.1; PID:g16413276; !1GSPDB:GN00178 !'##experimental_source strain Clip11262 GENETICS !$#gene fbp FUNCTION !$#description catalyzes the hydrolysis of fructose-1,6-bisphosphate to !1fructose-6-phosphate and orthophosphate !$#pathway gluconeogenesis CLASSIFICATION #superfamily Bacillus subtilis fructose-bisphosphatase; !1phosphoesterase core homology KEYWORDS carbohydrate metabolism; gluconeogenesis; metalloprotein; !1phosphoric monoester hydrolase SUMMARY #length 653 #molecular-weight 76068 #checksum 5225 SEQUENCE /// ENTRY AF1178 #type complete TITLE fructose-bisphosphatase (EC 3.1.3.11) [similarity] - Listeria monocytogenes (strain EGD-e) ORGANISM #formal_name Listeria monocytogenes DATE 27-Nov-2001 #sequence_revision 27-Nov-2001 #text_change 11-Jan-2002 ACCESSIONS AF1178 REFERENCE AB1077 !$#authors Glaser, P.; Frangeul, L.; Buchrieser, C.; Amend, A.; !1Baquero, F.; Berche, P.; Bloecker, H.; Brandt, P.; !1Chakraborty, T.; Charbit, A.; Chetouani, F.; Couve, E.; de !1Daruvar, A.; Dehoux, P.; Domann, E.; Dominguez-Bernal, G.; !1Duchaud, E.; Durand, L.; Dussurget, O.; Entian, K.D.; Fsihi, !1H.; Garcia-Del Portillo, F.; Garrido, P.; Gautier, L.; !1Goebel, W.; Gomez-Lopez, N.; Hain, T.; Hauf, J.; Jackson, !1D.; Jones, L.M.; Karst, U.; Kreft, J.; Kuhn, M.; Kunst, F.; !1Kurapkat, G.; Madueno, E.; Maitournam, A.; Mata Vicente, J.; !1Ng, E.; Nordsiek, G.; Novella, S.; de Pablos, B.; !1Perez-Diaz, J.C.; Remmel, B.; Rose, M.; Rusniok, C.; !1Schlueter, T.; Simoes, N.; Tierrez, A.; Vazquez-Boland, !1J.A.; Voss, H.; Wehland, J.; Cossart, P. !$#journal Science (2001) 294:849-852 !$#title Comparative genomics of Listeria species. !$#cross-references MUID:21537279; PMID:11679669 !$#accession AF1178 !'##molecule_type DNA !'##residues 1-653 ##label GLA !'##cross-references GB:NC_003210; PIDN:CAC98908.1; PID:g16410219; !1GSPDB:GN00177 !'##experimental_source strain EGD-e GENETICS !$#gene fbp FUNCTION !$#description catalyzes the hydrolysis of fructose-1,6-bisphosphate to !1fructose-6-phosphate and orthophosphate !$#pathway gluconeogenesis CLASSIFICATION #superfamily Bacillus subtilis fructose-bisphosphatase; !1phosphoesterase core homology KEYWORDS carbohydrate metabolism; gluconeogenesis; metalloprotein; !1phosphoric monoester hydrolase SUMMARY #length 653 #molecular-weight 75644 #checksum 4735 SEQUENCE /// ENTRY A86657 #type complete TITLE fructose-bisphosphatase (EC 3.1.3.11) [similarity] - Lactococcus lactis subsp. lactis (strain IL1403) ORGANISM #formal_name Lactococcus lactis subsp. lactis DATE 23-Mar-2001 #sequence_revision 23-Mar-2001 #text_change 11-Jan-2002 ACCESSIONS A86657 REFERENCE A86625 !$#authors Bolotin, A.; Wincker, P.; Mauger, S.; Jaillon, O.; Malarme, !1K.; Weissenbach, J.; Ehrlich, S.D.; Sorokin, A. !$#journal Genome Res. (2001) 11:731-753 !$#title The complete genome sequence of the lactic acid bacterium !1Lactococcus lactis ssp. lactis IL1403. !$#cross-references MUID:21235186; PMID:11337471 !$#accession A86657 !'##molecule_type DNA !'##residues 1-640 ##label STO !'##cross-references GB:AE005176; PID:g12723117; PIDN:AAK04355.1; !1GSPDB:GN00146 !'##experimental_source strain IL1403 GENETICS !$#gene fbp FUNCTION !$#description catalyzes the hydrolysis of fructose-1,6-bisphosphate to !1fructose-6-phosphate and orthophosphate !$#pathway gluconeogenesis CLASSIFICATION #superfamily Bacillus subtilis fructose-bisphosphatase; !1phosphoesterase core homology KEYWORDS carbohydrate metabolism; gluconeogenesis; metalloprotein; !1phosphoric monoester hydrolase SUMMARY #length 640 #molecular-weight 73845 #checksum 6191 SEQUENCE /// ENTRY H97093 #type complete TITLE fructose-bisphosphatase (EC 3.1.3.11) [similarity] - Clostridium acetobutylicum ORGANISM #formal_name Clostridium acetobutylicum DATE 14-Sep-2001 #sequence_revision 14-Sep-2001 #text_change 11-Jan-2002 ACCESSIONS H97093 REFERENCE A96900 !$#authors Nolling, J.; Breton, G.; Omelchenko, M.V.; Markarova, K.S.; !1Zeng, Q.; Gibson, R.; Lee, H.M.; Dubois, J.; Qiu, D.; Hitti, !1J.; Wolf, Y.I.; Tatusov, R.L.; Sabathe, F.; Doucette-Stamm, !1L.; Soucaille, P.; Daly, M.J.; Bennett, G.N.; Koonin, E.V.; !1Smith, D.R. !$#journal J. Bacteriol. (2001) 183:4823-4838 !$#title Genome Sequence and Comparative Analysis of the !1Solvent-Producing Bacterium Clostridium acetobutylicum. !$#cross-references MUID:21359325; PMID:21359325 !$#accession H97093 !'##molecule_type DNA !'##residues 1-665 ##label KUR !'##cross-references GB:AE001437; PIDN:AAK79539.1; PID:g15024525; !1GSPDB:GN00168 !'##experimental_source Clostridium acetobutylicum ATCC824 GENETICS !$#gene CAC1572 FUNCTION !$#description catalyzes the hydrolysis of fructose-1,6-bisphosphate to !1fructose-6-phosphate and orthophosphate !$#pathway gluconeogenesis CLASSIFICATION #superfamily Bacillus subtilis fructose-bisphosphatase; !1phosphoesterase core homology KEYWORDS carbohydrate metabolism; gluconeogenesis; metalloprotein; !1phosphoric monoester hydrolase SUMMARY #length 665 #molecular-weight 77224 #checksum 204 SEQUENCE /// ENTRY Q1BP1L #type complete TITLE multiple specificity phosphoprotein phosphatase (EC 3.1.3.-) - phage lambda ORGANISM #formal_name phage lambda DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 11-Jun-1999 ACCESSIONS G43011; C43017; A04397 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession G43011 !'##molecule_type DNA !'##residues 1-221 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession C43017 !'##molecule_type DNA !'##residues 1-221 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96594.1; PID:g215160 COMMENT This enzyme is activated in vitro by Mn++ and !1dephosphorylates Ser, Thr, and Tyr phosphoproteins, as well !1as a bacterial histidyl phosphoprotein. GENETICS !$#map_position 89.12-90.48 CLASSIFICATION #superfamily phage lambda phosphoprotein phosphatase; !1phosphoesterase core homology KEYWORDS manganese; phosphoric monoester hydrolase FEATURE !$14-77 #domain phosphoesterase core homology #label PEC SUMMARY #length 221 #molecular-weight 25219 #checksum 637 SEQUENCE /// ENTRY B65054 #type complete TITLE probable multiple specificity phosphoprotein phosphatase (EC 3.1.3.-) b2734 - Escherichia coli (strain K-12) ALTERNATE_NAMES hypothetical protein b2734 ORGANISM #formal_name Escherichia coli DATE 12-Sep-1997 #sequence_revision 17-Sep-1997 #text_change 01-Mar-2002 ACCESSIONS B65054 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65054 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-218 ##label BLAT !'##cross-references GB:AE000357; GB:U00096; NID:g2367155; !1PIDN:AAC75776.1; PID:g1789090; UWGP:b2734 !'##experimental_source strain K-12, substrain MG1655 COMMENT The lambda phage enzyme is activated in vitro by Mn++ and !1dephosphorylates Ser, Thr, and Tyr phosphoproteins, as well !1as a bacterial histidyl phosphoprotein. CLASSIFICATION #superfamily phage lambda phosphoprotein phosphatase; !1phosphoesterase core homology KEYWORDS manganese; phosphoric monoester hydrolase FEATURE !$16-79 #domain phosphoesterase core homology #label PEC SUMMARY #length 218 #molecular-weight 25098 #checksum 609 SEQUENCE /// ENTRY F64945 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) 1, serine/threonine specific - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 12-Sep-1997 #sequence_revision 17-Sep-1997 #text_change 01-Mar-2002 ACCESSIONS F64945 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64945 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-219 ##label BLAT !'##cross-references GB:AE000278; GB:U00096; NID:g1788139; !1PIDN:AAC74908.1; PID:g1788143; UWGP:b1838 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ppha; prpA FUNCTION !$#description catayzes the removal of a phosphate group attached to a !1serine or a threonine residue; involved in signaling protein !1misfolding via CpxR and CpxA transducing system CLASSIFICATION #superfamily phage lambda phosphoprotein phosphatase; !1phosphoesterase core homology KEYWORDS iron; manganese; metalloprotein; phosphohistidine; !1phosphoprotein; phosphoric monoester hydrolase FEATURE !$19-82 #domain phosphoesterase core homology #label PEC\ !$25,27,54 #binding_site iron (Asp, His, Asp) #status predicted\ !$54,80 #binding_site manganese (Asp, Asn) #status predicted\ !$81 #active_site His (phosphohistidine intermediate) !8#status predicted SUMMARY #length 219 #molecular-weight 25405 #checksum 7070 SEQUENCE /// ENTRY PAHU2A #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) 2-alpha catalytic chain - human ALTERNATE_NAMES phosphoprotein phosphatase 2A-alpha catalytic chain; protein phosphatase 2 alpha isoform catalytic subunit ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Mar-2000 ACCESSIONS S01986; A37135; A32143 REFERENCE S01986 !$#authors Stone, S.R.; Mayer, R.; Wernet, W.; Maurer, F.; Hofsteenge, !1J.; Hemmings, B.A. !$#journal Nucleic Acids Res. (1988) 16:11365 !$#title The nucleotide sequence of the cDNA encoding the human lung !1protein phosphatase 2A-alpha catalytic subunit. !$#cross-references MUID:89083567; PMID:2849764 !$#accession S01986 !'##molecule_type mRNA !'##residues 1-309 ##label STO !'##cross-references EMBL:X12646; NID:g36119; PIDN:CAA31176.1; !1PID:g36120 REFERENCE A37135 !$#authors Khew-Goodall, Y.; Mayer, R.E.; Maurer, F.; Stone, S.R.; !1Hemmings, B.A. !$#journal Biochemistry (1991) 30:89-97 !$#title Structure and transcriptional regulation of protein !1phosphatase 2A catalytic subunit genes. !$#cross-references MUID:91105105; PMID:1846293 !$#accession A37135 !'##molecule_type DNA !'##residues 1-309 ##label KHE !'##cross-references GB:M60483; GB:J05297; NID:g190223; PIDN:AAA36466.1; !1PID:g190224 REFERENCE A94200 !$#authors Arino, J.; Woon, C.W.; Brautigan, D.L.; Miller Jr., T.B.; !1Johnson, G.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:4252-4256 !$#title Human liver phosphatase 2A: cDNA and amino acid sequence of !1two catalytic subunit isotypes. !$#cross-references MUID:88248000; PMID:2837763 !$#accession A32143 !'##molecule_type mRNA !'##residues 1-309 ##label ARI !'##cross-references GB:J03804; NID:g1707870; PIDN:AAB38019.1; !1PID:g1707871 !'##experimental_source liver; clone HL-14 !'##note the authors translated the codon CAT for residue 63 as Glu GENETICS !$#gene GDB:PPP2CA !'##cross-references GDB:126878; OMIM:176915 !$#map_position 5q23.2-5q31.2 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$23-282 #domain phosphoprotein phosphatase homology #label !8PPP\ !$51-119 #domain phosphoesterase core homology #label PEC\ !$57,59,85 #binding_site iron (Asp, His, Asp) #status predicted\ !$85,117,167,241 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$88,118,265 #active_site Asp, His, Tyr #status predicted\ !$89,214 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 309 #molecular-weight 35594 #checksum 6175 SEQUENCE /// ENTRY A27430 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) 2-alpha catalytic chain - pig ALTERNATE_NAMES phosphoprotein phosphatase 2A-alpha catalytic chain; protein phosphatase 2 alpha isoform catalytic subunit ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 19-Nov-1988 #sequence_revision 19-Nov-1988 #text_change 09-Nov-2001 ACCESSIONS A27430 REFERENCE A27430 !$#authors Stone, S.R.; Hofsteenge, J.; Hemmings, B.A. !$#journal Biochemistry (1987) 26:7215-7220 !$#title Molecular cloning of cDNAs encoding two isoforms of the !1catalytic subunit of protein phosphatase 2A. !$#cross-references MUID:88107662; PMID:2827745 !$#accession A27430 !'##molecule_type mRNA !'##residues 1-309 ##label STO !'##cross-references GB:M20192; NID:g164295; PIDN:AAA30981.1; !1PID:g164296 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$23-282 #domain phosphoprotein phosphatase homology #label !8PPP\ !$51-119 #domain phosphoesterase core homology #label PEC\ !$57,59,85 #binding_site iron (Asp, His, Asp) #status predicted\ !$85,117,167,241 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$88,118,265 #active_site Asp, His, Tyr #status predicted\ !$89,214 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 309 #molecular-weight 35594 #checksum 6175 SEQUENCE /// ENTRY S10371 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) 2A-alpha catalytic chain - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 04-Mar-2000 ACCESSIONS S10371; S32226 REFERENCE S10371 !$#authors de Paoli-Roach, A.A. !$#submission submitted to the EMBL Data Library, March 1990 !$#description Nucleotide sequence of a cDNA encoding the protein !1phosphatase 2A alpha catalytic subunit from bovine aorta !1smooth muscle. !$#accession S10371 !'##molecule_type mRNA !'##residues 1-309 ##label DEP !'##cross-references EMBL:X52554; NID:g628; PIDN:CAA36789.1; PID:g629 !'##experimental_source aortic smooth muscle REFERENCE S32226 !$#authors Chen, S.; Boynton, A. !$#submission submitted to the EMBL Data Library, March 1993 !$#description Nucleotide sequence of a bovine brain cDNA encoding the !1alpha isotype of protein phosphatase 2A catalytic subunit. !$#accession S32226 !'##status preliminary !'##molecule_type mRNA !'##residues 1-309 ##label CHE !'##cross-references EMBL:X72858; NID:g288410; PIDN:CAA51381.1; !1PID:g288411 !'##experimental_source brain CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$23-282 #domain phosphoprotein phosphatase homology #label !8PPP\ !$51-119 #domain phosphoesterase core homology #label PEC\ !$57,59,85 #binding_site iron (Asp, His, Asp) #status predicted\ !$85,117,167,241 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$88,118,265 #active_site Asp, His, Tyr #status predicted\ !$89,214 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 309 #molecular-weight 35594 #checksum 6175 SEQUENCE /// ENTRY PARBA1 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) 2A-alpha catalytic chain - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Mar-2000 ACCESSIONS S00104; S18812; A60240 REFERENCE S00104 !$#authors da Cruz e Silva, O.B.; Alemany, S.; Campbell, D.G.; Cohen, !1P.T.W. !$#journal FEBS Lett. (1987) 221:415-422 !$#title Isolation and sequence analysis of a cDNA clone encoding the !1entire catalytic subunit of a type-2A protein phosphatase. !$#cross-references MUID:87304854; PMID:3040474 !$#accession S00104 !'##molecule_type mRNA !'##residues 1-309 ##label DAC !'##cross-references EMBL:X06087; NID:g1682; PIDN:CAA29471.1; PID:g1683 !$#accession S18812 !'##molecule_type protein !'##residues 9-21;67-80;215-229,'X',231-238;277-298;304-308 ##label DAC2 REFERENCE A60240 !$#authors Stone, S.R.; Hofsteenge, J.; Hemmings, B.A. !$#journal Adv. Exp. Med. Biol. (1988) 231:559-566 !$#title Primary structure of protein phosphatase 2A as determined by !1molecular cloning: implications for a protein phosphatase !1gene family. !$#cross-references MUID:88323941; PMID:2843014 !$#accession A60240 !'##molecule_type protein !'##residues 2-19;26-37;48-62,'X',64-87;137-144;186-190,'X', !1192-199;215-224,'K',226-231,'K',233,'K',235;245-249,'V', !1251-265,'X',267-268,'X',270-294,'N',296-297 ##label STO CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$23-282 #domain phosphoprotein phosphatase homology #label !8PPP\ !$51-119 #domain phosphoesterase core homology #label PEC\ !$57,59,85 #binding_site iron (Asp, His, Asp) #status predicted\ !$85,117,167,241 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$88,118,265 #active_site Asp, His, Tyr #status predicted\ !$89,214 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 309 #molecular-weight 35594 #checksum 6175 SEQUENCE /// ENTRY PART2A #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) 2A-alpha catalytic chain - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Mar-2000 ACCESSIONS S06592; JS0060; PS0311; A36491 REFERENCE S06592 !$#authors Posas, F.; Arino, J. !$#journal Nucleic Acids Res. (1989) 17:8369 !$#title Nucleotide sequence of a rat heart cDNA encoding the isotype !1alpha of the catalytic subunit of protein phosphatase 2A. !$#cross-references MUID:90045961; PMID:2554255 !$#accession S06592 !'##molecule_type mRNA !'##residues 1-309 ##label POS !'##cross-references EMBL:X16043; NID:g56818; PIDN:CAA34166.1; !1PID:g56819 REFERENCE JS0060 !$#authors Kitagawa, Y.; Tahira, T.; Ikeda, I.; Kikuchi, K.; Tsuiki, !1S.; Sugimura, T.; Nagao, M. !$#journal Biochim. Biophys. Acta (1988) 951:123-129 !$#title Molecular cloning of cDNA for the catalytic subunit of rat !1liver type 2A protein phosphatase, and detection of high !1levels of expression of the gene in normal and cancer cells. !$#cross-references MUID:89051001; PMID:2461222 !$#accession JS0060 !'##molecule_type mRNA !'##residues 1-309 ##label KIT !'##cross-references GB:M33114; NID:g206286; PIDN:AAA41904.1; !1PID:g206287 !$#accession PS0311 !'##molecule_type protein !'##residues 284,'P',286-289,'L',291-293 ##label KI2 REFERENCE A36491 !$#authors Wadzinski, B.E.; Heasley, L.E.; Johnson, G.L. !$#journal J. Biol. Chem. (1990) 265:21504-21508 !$#title Multiplicity of protein serine-threonine phosphatases in !1PC12 pheochromocytoma and FTO-2B hepatoma cells. !$#cross-references MUID:91072341; PMID:2174876 !$#accession A36491 !'##status preliminary !'##molecule_type mRNA !'##residues 204-260 ##label WAD !'##cross-references GB:M58438; NID:g206300; PIDN:AAA41911.1; !1PID:g206301; GB:J05720 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$23-282 #domain phosphoprotein phosphatase homology #label !8PPP\ !$51-119 #domain phosphoesterase core homology #label PEC\ !$57,59,85 #binding_site iron (Asp, His, Asp) #status predicted\ !$85,117,167,241 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$88,118,265 #active_site Asp, His, Tyr #status predicted\ !$89,214 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 309 #molecular-weight 35608 #checksum 6125 SEQUENCE /// ENTRY S20348 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) 2A-alpha catalytic chain - clawed frog ORGANISM #formal_name Xenopus sp. #common_name clawed frog DATE 04-Dec-1992 #sequence_revision 04-Dec-1992 #text_change 04-Mar-2000 ACCESSIONS S20348 REFERENCE S20348 !$#authors Cormier, P.; Osborne, H.B.; Bassez, T.; Poulhe, R.; Belle, !1R.; Mulner-Lorillon, O. !$#journal FEBS Lett. (1991) 295:185-188 !$#title Protein phosphatase 2(A) from Xenopus oocytes. !1Characterization during meiotic cell division. !$#cross-references MUID:92111736; PMID:1662645 !$#accession S20348 !'##molecule_type mRNA !'##residues 1-309 ##label COR !'##cross-references EMBL:X62114 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$23-282 #domain phosphoprotein phosphatase homology #label !8PPP\ !$51-119 #domain phosphoesterase core homology #label PEC\ !$57,59,85 #binding_site iron (Asp, His, Asp) #status predicted\ !$85,117,167,241 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$88,118,265 #active_site Asp, His, Tyr #status predicted\ !$89,214 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 309 #molecular-weight 35551 #checksum 5638 SEQUENCE /// ENTRY PAHU2B #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) 2-beta catalytic chain - human ALTERNATE_NAMES protein phosphatase 2A-beta isoform catalytic subunit ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Mar-2000 ACCESSIONS B37135; S01985; B32143; S09378; A34060 REFERENCE A37135 !$#authors Khew-Goodall, Y.; Mayer, R.E.; Maurer, F.; Stone, S.R.; !1Hemmings, B.A. !$#journal Biochemistry (1991) 30:89-97 !$#title Structure and transcriptional regulation of protein !1phosphatase 2A catalytic subunit genes. !$#cross-references MUID:91105105; PMID:1846293 !$#accession B37135 !'##molecule_type DNA !'##residues 1-309 ##label KHE !'##cross-references GB:M60484; GB:J05297; NID:g190225; PIDN:AAA36467.1; !1PID:g190226 REFERENCE S01985 !$#authors Hemmings, B.A.; Wernet, W.; Mayer, R.; Maurer, F.; !1Hofsteenge, J.; Stone, S.R. !$#journal Nucleic Acids Res. (1988) 16:11366 !$#title The nucleotide sequence of the cDNA encoding the human lung !1protein phosphatase 2A-beta catalytic subunit. !$#cross-references MUID:89083568; PMID:2849765 !$#accession S01985 !'##molecule_type mRNA !'##residues 1-309 ##label HEM !'##cross-references EMBL:X12656; NID:g35580; PIDN:CAA31183.1; !1PID:g35581 REFERENCE A94200 !$#authors Arino, J.; Woon, C.W.; Brautigan, D.L.; Miller Jr., T.B.; !1Johnson, G.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:4252-4256 !$#title Human liver phosphatase 2A: cDNA and amino acid sequence of !1two catalytic subunit isotypes. !$#cross-references MUID:88248000; PMID:2837763 !$#accession B32143 !'##molecule_type mRNA !'##residues 2-18,'D',20-309 ##label AR2 !'##cross-references GB:J03805; NID:g178437; PIDN:AAB38020.1; !1PID:g178438 !'##experimental_source liver; clone HL-1 !'##note the authors translated the codon GAC for residue 18 as Glu REFERENCE S09378 !$#authors Virshup, D.M.; Kauffman, M.G.; Kelly, T.J. !$#journal EMBO J. (1989) 8:3891-3898 !$#title Activation of SV40 DNA replication in vitro by cellular !1protein phosphatase 2A. !$#cross-references MUID:90059993; PMID:2555176 !$#accession S09378 !'##molecule_type protein !'##residues 91-97;111-114;122-127;137-144;207-238 ##label VIR REFERENCE A34060 !$#authors Pallas, D.C.; Shahrik, L.K.; Martin, B.L.; Jaspers, S.; !1Miller, T.B.; Brautigan, D.L.; Roberts, T.M. !$#journal Cell (1990) 60:167-176 !$#title Polyoma small and middle T antigens and SV40 small t antigen !1form stable complexes with protein phosphatase 2A. !$#cross-references MUID:90106638; PMID:2153055 !$#accession A34060 !'##molecule_type protein !'##residues 75-89;215-234;'X',270-294;303-309 ##label PAL GENETICS !$#gene GDB:PPP2CB !'##cross-references GDB:126879; OMIM:176916 !$#map_position 8p12-8p11.2 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$23-282 #domain phosphoprotein phosphatase homology #label !8PPP\ !$51-119 #domain phosphoesterase core homology #label PEC\ !$57,59,85 #binding_site iron (Asp, His, Asp) #status predicted\ !$85,117,167,241 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$88,118,265 #active_site Asp, His, Tyr #status predicted\ !$89,214 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 309 #molecular-weight 35575 #checksum 6130 SEQUENCE /// ENTRY PARB2B #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) 2A-beta catalytic chain - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Mar-2000 ACCESSIONS S00220 REFERENCE S00220 !$#authors da Cruz e Silva, O.B.; Cohen, P.T.W. !$#journal FEBS Lett. (1987) 226:176-178 !$#title A second catalytic subunit of type-2A protein phosphatase !1from rabbit skeletal muscle. !$#cross-references MUID:88083628; PMID:2826253 !$#accession S00220 !'##molecule_type mRNA !'##residues 1-309 ##label DA1 !'##cross-references EMBL:Y00763; NID:g1684; PIDN:CAA68732.1; PID:g1685 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$23-282 #domain phosphoprotein phosphatase homology #label !8PPP\ !$51-119 #domain phosphoesterase core homology #label PEC\ !$57,59,85 #binding_site iron (Asp, His, Asp) #status predicted\ !$85,117,167,241 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$88,118,265 #active_site Asp, His, Tyr #status predicted\ !$89,214 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 309 #molecular-weight 35605 #checksum 6225 SEQUENCE /// ENTRY PART2B #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) 2A-beta catalytic chain - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Mar-2000 ACCESSIONS S08486; S06593; B36491; A31357 REFERENCE A31357 !$#authors Kitagawa, Y.; Sakai, R.; Tahira, T.; Tsuda, H.; Ito, N.; !1Sugimura, T.; Nagao, M. !$#journal Biochem. Biophys. Res. Commun. (1988) 157:821-827 !$#title Molecular cloning of rat phosphoprotein phosphatase 2A-beta !1cDNA and increased expressions of phosphatase 2A-alpha and !12A-beta in rat liver tumors. !$#cross-references MUID:89076322; PMID:2849437 !$#accession S08486 !'##molecule_type mRNA !'##residues 1-309 ##label KIT !'##cross-references EMBL:X14087; NID:g56895; PIDN:CAA32249.1; !1PID:g56896 REFERENCE S06593 !$#authors Posas, F.; Arino, J. !$#journal Nucleic Acids Res. (1989) 17:8370 !$#title Nucleotide sequence of a rat heart cDNA encoding the isotype !1beta of the catalytic subunit of protein phosphatase 2A. !$#cross-references MUID:90045962; PMID:2554256 !$#accession S06593 !'##molecule_type mRNA !'##residues 1-309 ##label POS !'##cross-references EMBL:X16044; NID:g56820; PIDN:CAA34167.1; !1PID:g56821 REFERENCE A36491 !$#authors Wadzinski, B.E.; Heasley, L.E.; Johnson, G.L. !$#journal J. Biol. Chem. (1990) 265:21504-21508 !$#title Multiplicity of protein serine-threonine phosphatases in !1PC12 pheochromocytoma and FTO-2B hepatoma cells. !$#cross-references MUID:91072341; PMID:2174876 !$#accession B36491 !'##status preliminary !'##molecule_type mRNA !'##residues 204-260 ##label WAD !'##cross-references GB:M58439; NID:g206304; PIDN:AAA41913.1; !1PID:g206305; GB:J05720 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$23-282 #domain phosphoprotein phosphatase homology #label !8PPP\ !$51-119 #domain phosphoesterase core homology #label PEC\ !$57,59,85 #binding_site iron (Asp, His, Asp) #status predicted\ !$85,117,167,241 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$88,118,265 #active_site Asp, His, Tyr #status predicted\ !$89,214 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 309 #molecular-weight 35575 #checksum 6130 SEQUENCE /// ENTRY JC4316 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) 2A-beta catalytic chain - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 29-Nov-1995 #sequence_revision 08-Feb-1996 #text_change 09-Nov-2001 ACCESSIONS JC4316 REFERENCE JC4316 !$#authors Van Hoof, C.; Ingels, F.; Cayla, X.; Stevens, I.; Merlevede, !1W.; Goris, J. !$#journal Biochem. Biophys. Res. Commun. (1995) 215:666-673 !$#title Molecular cloning and developmental regulation of expression !1of two isoforms of the catalytic subunit of protein !1phosphatase 2A from Xenopus laevis. !$#cross-references MUID:96011830; PMID:7488007 !$#accession JC4316 !'##molecule_type mRNA !'##residues 1-309 ##label VAN !'##cross-references EMBL:Z50852; NID:g1143702; PIDN:CAA90704.1; !1PID:g1143703 !'##experimental_source oocytes COMMENT This kinase is one of the major serine/threonine protein !1phosphatases. It controlles the cellular processes, such as !1cell division and cell transformation. GENETICS !$#gene xc4 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$23-282 #domain phosphoprotein phosphatase homology #label !8PPP\ !$51-119 #domain phosphoesterase core homology #label PEC\ !$57,59,85 #binding_site iron (Asp, His, Asp) #status predicted\ !$85,117,167,241 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$88,118,265 #active_site Asp, His, Tyr #status predicted\ !$89,214 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 309 #molecular-weight 35578 #checksum 6109 SEQUENCE /// ENTRY S12961 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) 2A-28D catalytic chain - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 09-Nov-2001 ACCESSIONS S12961 REFERENCE S12961 !$#authors Orgad, S.; Brewis, N.D.; Alphey, L.; Axton, J.M.; Dudai, Y.; !1Cohen, P.T.W. !$#journal FEBS Lett. (1990) 275:44-48 !$#title The structure of protein phosphatase 2A is as highly !1conserved as that of protein phosphatase 1. !$#cross-references MUID:91085575; PMID:2175718 !$#accession S12961 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-309 ##label ORG !'##cross-references GB:X55199; NID:g10915; PIDN:CAA38984.1; PID:g10916 GENETICS !$#gene FlyBase:Pp2A-28D !'##cross-references FlyBase:FBgn0004177 !$#map_position 2L 28D2-4 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$23-282 #domain phosphoprotein phosphatase homology #label !8PPP\ !$51-119 #domain phosphoesterase core homology #label PEC\ !$57,59,85 #binding_site iron (Asp, His, Asp) #status predicted\ !$85,117,167,241 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$88,118,265 #active_site Asp, His, Tyr #status predicted\ !$89,214 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 309 #molecular-weight 35469 #checksum 5162 SEQUENCE /// ENTRY T21975 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) 2A F38H4.9 [similarity] - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 09-Nov-2001 ACCESSIONS T21975 REFERENCE Z19496 !$#authors Lennard, N. !$#submission submitted to the EMBL Data Library, July 1996 !$#accession T21975 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-318 ##label WIL !'##cross-references EMBL:Z77660; PIDN:CAB01174.1; GSPDB:GN00022; !1CESP:F38H4.9 !'##experimental_source clone F38H4 GENETICS !$#gene CESP:F38H4.9 !$#map_position 4 !$#introns 43/3; 113/3; 134/3; 197/3; 255/3 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$32-291 #domain phosphoprotein phosphatase homology #label !8PPP\ !$60-128 #domain phosphoesterase core homology #label PEC\ !$66,68,94 #binding_site iron (Asp, His, Asp) #status predicted\ !$94,126,176,250 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$97,127,274 #active_site Asp, His, Tyr #status predicted\ !$98,223 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 318 #molecular-weight 36302 #checksum 6930 SEQUENCE /// ENTRY B96722 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) 2A catalytic chain F20P5.30 [similarity] - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 02-Mar-2001 #sequence_revision 02-Mar-2001 #text_change 09-Nov-2001 ACCESSIONS B96722 REFERENCE A86141 !$#authors Theologis, A.; Ecker, J.R.; Palm, C.J.; Federspiel, N.A.; !1Kaul, S.; White, O.; Alonso, J.; Altaf, H.; Araujo, R.; !1Bowman, C.L.; Brooks, S.Y.; Buehler, E.; Chan, A.; Chao, Q.; !1Chen, H.; Cheuk, R.F.; Chin, C.W.; Chung, M.K.; Conn, L.; !1Conway, A.B.; Conway, A.R.; Creasy, T.H.; Dewar, K.; Dunn, !1P.; Etgu, P.; Feldblyum, T.V.; Feng, J.; Fong, B.; Fujii, !1C.Y.; Gill, J.E.; Goldsmith, A.D.; Haas, B.; Hansen, N.F.; !1Hughes, B.; Huizar, L.; Hunter, J.L.; Jenkins, J.; !1Johnson-Hopson, C.; Khan, S.; Khaykin, E.; Kim, C.J.; Koo, !1H.L.; Kremenetskaia, I.; Kurtz, D.B.; Kwan, A.; Lam, B.; !1Langin-Hooper, S.; Lee, A.; Lee, J.M.; Lenz, C.A.; Li, J.H.; !1Li, Y.; Lin, X.; Liu, S.X.; Liu, Z.A.; Luros, J.S.; Maiti, !1R.; Marziali, A.; Militscher, J.; Miranda, M.; Nguyen, M.; !1Nierman, W.C.; Osborne, B.I.; Pai, G.; Peterson, J.; Pham, !1P.K.; Rizzo, M.; Rooney, T.; Rowley, D.; Sakano, H.; !1Salzberg, S.L.; Schwartz, J.R.; Shinn, P.; Southwick, A.M.; !1Sun, H.; Tallon, L.J.; Tambunga, G.; Toriumi, M.J.; Town, !1C.D.; Utterback, T.; van Aken, S.; Vaysberg, M.; Vysotskaia, !1V.S.; Walker, M.; Wu, D.; Yu, G.; Fraser, C.M.; Venter, !1J.C.; Davis, R.W. !$#journal Nature (2000) 408:816-820 !$#title Sequence and analysis of chromosome 1 of the plant !1Arabidopsis. !$#cross-references MUID:21016719; PMID:11130712 !$#accession B96722 !'##molecule_type DNA !'##residues 1-307 ##label STO !'##cross-references GB:AE005173; NID:g2194141; PIDN:AAB61116.1; !1GSPDB:GN00141 GENETICS !$#gene F20P5.30 !$#map_position 1 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$21-280 #domain phosphoprotein phosphatase homology #label !8PPP\ !$49-117 #domain phosphoesterase core homology #label PEC\ !$55,57,83 #binding_site iron (Asp, His, Asp) #status predicted\ !$83,115,165,239 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$86,116,263 #active_site Asp, His, Tyr #status predicted\ !$87,212 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 307 #molecular-weight 35041 #checksum 482 SEQUENCE /// ENTRY S52660 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) 2A-4 (version 1) - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 22-Nov-1996 #sequence_revision 22-Nov-1996 #text_change 09-Nov-2001 ACCESSIONS S52660 REFERENCE S52659 !$#authors Casamayor, A.; Perez-Callejon, E.; Pujol, G.; Arino, J.; !1Ferrer, A. !$#journal Plant Mol. Biol. (1994) 26:523-528 !$#title Molecular characterization of a fourth isoform of the !1catalytic subunit of protein phosphatase 2A from Arabidopsis !1thaliana. !$#cross-references MUID:95036028; PMID:7948902 !$#accession S52660 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-313 ##label CAS !'##cross-references EMBL:U08047; NID:g473258; PIDN:AAA64941.1; !1PID:g473259 GENETICS !$#gene PP2A-4 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$27-286 #domain phosphoprotein phosphatase homology #label !8PPP\ !$55-123 #domain phosphoesterase core homology #label PEC\ !$61,63,89 #binding_site iron (Asp, His, Asp) #status predicted\ !$89,121,171,245 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$92,122,269 #active_site Asp, His, Tyr #status predicted\ !$93,218 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 313 #molecular-weight 35767 #checksum 3396 SEQUENCE /// ENTRY S52659 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) 2A-3 - Arabidopsis thaliana ALTERNATE_NAMES hypothetical protein At2g42500 ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 14-Jul-1995 #sequence_revision 21-Jul-1995 #text_change 09-Nov-2001 ACCESSIONS S52659; F84854 REFERENCE S52659 !$#authors Casamayor, A.; Perez-Callejon, E.; Pujol, G.; Arino, J.; !1Ferrer, A. !$#journal Plant Mol. Biol. (1994) 26:523-528 !$#title Molecular characterization of a fourth isoform of the !1catalytic subunit of protein phosphatase 2A from Arabidopsis !1thaliana. !$#cross-references MUID:95036028; PMID:7948902 !$#accession S52659 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-313 ##label CAS !'##cross-references EMBL:M96841; NID:g466442; PIDN:AAA64742.1; !1PID:g466441 REFERENCE A84420 !$#authors Lin, X.; Kaul, S.; Rounsley, S.D.; Shea, T.P.; Benito, M.I.; !1Town, C.D.; Fujii, C.Y.; Mason, T.M.; Bowman, C.L.; !1Barnstead, M.E.; Feldblyum, T.V.; Buell, C.R.; Ketchum, !1K.A.; Lee, J.J.; Ronning, C.M.; Koo, H.; Moffat, K.S.; !1Cronin, L.A.; Shen, M.; VanAken, S.E.; Umayam, L.; Tallon, !1L.J.; Gill, J.E.; Adams, M.D.; Carrera, A.J.; Creasy, T.H.; !1Goodman, H.M.; Somerville, C.R.; Copenhaver, G.P.; Preuss, !1D.; Nierman, W.C.; White, O.; Eisen, J.A.; Salzberg, S.L.; !1Fraser, C.M.; Venter, J.C. !$#journal Nature (1999) 402:761-768 !$#title Sequence and analysis of chromosome 2 of the plant !1Arabidopsis thaliana. !$#cross-references MUID:20083487; PMID:10617197 !$#accession F84854 !'##molecule_type DNA !'##residues 1-313 ##label STO !'##cross-references GB:AE002093; NID:g4567320; PIDN:AAD23731.1; !1GSPDB:GN00139 GENETICS !$#gene PP2A-3; At2g42500 !$#map_position 2 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$27-286 #domain phosphoprotein phosphatase homology #label !8PPP\ !$55-123 #domain phosphoesterase core homology #label PEC\ !$61,63,89 #binding_site iron (Asp, His, Asp) #status predicted\ !$89,121,171,245 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$92,122,269 #active_site Asp, His, Tyr #status predicted\ !$93,218 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 313 #molecular-weight 35832 #checksum 3078 SEQUENCE /// ENTRY S35502 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) 2A - alfalfa ORGANISM #formal_name Medicago sativa #common_name alfalfa DATE 03-Feb-1994 #sequence_revision 03-Feb-1994 #text_change 09-Nov-2001 ACCESSIONS S35502; S35414 REFERENCE S35502 !$#authors Pirck, M.; Pay, A.; Heberle-Bors, E.; Hirt, H. !$#journal Mol. Gen. Genet. (1993) 240:126-131 !$#title Isolation and characterization of a phosphoprotein !1phosphatase type 2A gene from alfalfa. !$#cross-references MUID:93341450; PMID:8393512 !$#accession S35502 !'##molecule_type mRNA !'##residues 1-313 ##label PIR !'##cross-references EMBL:X70399; NID:g287810; PIDN:CAA49849.1; !1PID:g287811 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$27-286 #domain phosphoprotein phosphatase homology #label !8PPP\ !$55-123 #domain phosphoesterase core homology #label PEC\ !$61,63,89 #binding_site iron (Asp, His, Asp) #status predicted\ !$89,121,171,245 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$92,122,269 #active_site Asp, His, Tyr #status predicted\ !$93,218 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 313 #molecular-weight 35711 #checksum 2495 SEQUENCE /// ENTRY PARBA2 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) X catalytic chain - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Mar-2000 ACCESSIONS S36193; S11059; S02006 REFERENCE S36193 !$#authors Brewis, N.D.; Street, A.J.; Prescott, A.R.; Cohen, P.T.W. !$#journal EMBO J. (1993) 12:987-996 !$#title PPX, a novel protein serine/threonine phosphatase localized !1to centrosomes. !$#cross-references MUID:93209245; PMID:8384557 !$#accession S36193 !'##molecule_type mRNA !'##residues 1-307 ##label BRE !'##cross-references GB:S57412; NID:g298833; PIDN:AAB25913.1; !1PID:g298834 REFERENCE S11059 !$#authors Cohen, P.T.W.; Brewis, N.D.; Hughes, V.; Mann, D.J. !$#journal FEBS Lett. (1990) 268:355-359 !$#title Protein serine/threonine phosphatases; an expanding family. !$#cross-references MUID:90346193; PMID:2166691 !$#accession S11059 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-307 ##label COH REFERENCE S02006 !$#authors da Cruz e Silva, O.B.; da Cruz e Silva, E.F.; Cohen, P.T.W. !$#journal FEBS Lett. (1988) 242:106-110 !$#title Identification of a novel protein phosphatase catalytic !1subunit by cDNA cloning. !$#cross-references MUID:89078593; PMID:2849555 !$#accession S02006 !'##molecule_type mRNA !'##residues 105-307 ##label DA1 !'##cross-references GB:X14031; EMBL:Y00980; NID:g1691; PIDN:CAA32191.1; !1PID:g1692 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$20-279 #domain phosphoprotein phosphatase homology #label !8PPP\ !$48-116 #domain phosphoesterase core homology #label PEC\ !$54,56,82 #binding_site iron (Asp, His, Asp) #status predicted\ !$82,114,164,238 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$85,115,262 #active_site Asp, His, Tyr #status predicted\ !$86,211 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 307 #molecular-weight 35037 #checksum 7467 SEQUENCE /// ENTRY T27390 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) Y75B8A.30 - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 09-Nov-2001 ACCESSIONS T27390 REFERENCE Z20361 !$#authors Barlow, K. !$#submission submitted to the EMBL Data Library, November 1998 !$#accession T27390 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-333 ##label WIL !'##cross-references EMBL:AL033514; PIDN:CAA22090.1; CESP:Y75B8A.30 !'##experimental_source clone Y75B8A GENETICS !$#gene CESP:Y75B8A.30 !$#introns 34/2; 75/3; 117/3; 210/3; 291/2 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$45-305 #domain phosphoprotein phosphatase homology #label !8PPP\ !$73-141 #domain phosphoesterase core homology #label PEC\ !$79,81,107 #binding_site iron (Asp, His, Asp) #status predicted\ !$107,139,189,264 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$110,140,288 #active_site Asp, His, Tyr #status predicted\ !$111,237 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 333 #molecular-weight 37359 #checksum 5057 SEQUENCE /// ENTRY T40017 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) SPBC26H8.05c [similarity] - fission yeast (Schizosaccharomyces pombe) ORGANISM #formal_name Schizosaccharomyces pombe DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 09-Nov-2001 ACCESSIONS T40017 REFERENCE Z21899 !$#authors Wood, V.; Rajandream, M.A.; Barrell, B.G.; Devlin, K.; !1Churcher, C.M. !$#submission submitted to the EMBL Data Library, September 1998 !$#accession T40017 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-348 ##label WOO !'##cross-references EMBL:AL031743; PIDN:CAA21097.1; GSPDB:GN00067; !1SPDB:SPBC26H8.05c !'##experimental_source strain 972h-; cosmid c26H8 GENETICS !$#gene SPDB:SPBC26H8.05c !$#map_position 2 !$#introns 24/1; 175/3 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$19-320 #domain phosphoprotein phosphatase homology #label !8PPP\ !$47-115 #domain phosphoesterase core homology #label PEC\ !$53,55,81 #binding_site iron (Asp, His, Asp) #status predicted\ !$81,113,163,237 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$84,114,303 #active_site Asp, His, Tyr #status predicted\ !$85,210 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 348 #molecular-weight 39215 #checksum 6207 SEQUENCE /// ENTRY PABY3 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) PPH3 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein D4421; protein YD8554.08; protein YDR075w ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1993 #sequence_revision 10-Feb-1995 #text_change 16-Jun-2000 ACCESSIONS S44331; S48762; S55822; S49830; C41525; S67892; S17483 REFERENCE S44331 !$#authors Hoffmann, R.; Jung, S.; Ehrmann, M.; Hofer, H.W. !$#journal Yeast (1994) 10:567-578 !$#title The Saccharomyces cerevisiae gene PPH3 encodes a protein !1phosphatase with properties different from PPX, PP1 and !1PP2A. !$#cross-references MUID:95028155; PMID:7941742 !$#accession S44331 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-308 ##label HOF REFERENCE S48758 !$#authors Coster, F.; Jonniaux, J.L.; Goffeau, A. !$#submission submitted to the EMBL Data Library, October 1994 !$#accession S48762 !'##molecule_type DNA !'##residues 1-308 ##label COS !'##cross-references EMBL:X82086; NID:g558241; PIDN:CAA57602.1; !1PID:g558246 REFERENCE S55819 !$#authors Coster, F.; Jonniaux, J.L.; Goffeau, A. !$#journal Yeast (1995) 11:673-679 !$#title Analysis of a 32.8 kb segment of yeast chromosome IV reveals !121 open reading frames, including TPS2, PPH3, RAD55, SED1, !1PDC2, AFR1, SSS1, SLU7 and a tRNA for arginine. !$#cross-references MUID:96093910; PMID:7483840 !$#accession S55822 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-308 ##label COW !'##cross-references EMBL:X82086; NID:g558241; PIDN:CAA57602.1; !1PID:g558246 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1994 REFERENCE S49823 !$#authors Richards, C.; Harris, D.E. !$#submission submitted to the EMBL Data Library, November 1994 !$#accession S49830 !'##molecule_type DNA !'##residues 1-308 ##label RIC !'##cross-references EMBL:Z46796; NID:g577794; PIDN:CAA86797.1; !1PID:g577802 REFERENCE A41525 !$#authors Ronne, H.; Carlberg, M.; Hu, G.Z.; Nehlin, J.O. !$#journal Mol. Cell. Biol. (1991) 11:4876-4884 !$#title Protein phosphatase 2A in Saccharomyces cerevisiae: effects !1on cell growth and bud morphogenesis. !$#cross-references MUID:92017761; PMID:1656215 !$#accession C41525 !'##molecule_type DNA !'##residues 1-244,'I',246-308 ##label RON !'##cross-references GB:X58858; NID:g4211; PIDN:CAA41662.1; PID:g4213 REFERENCE S67889 !$#authors Foury, F.; Jonniaux, J.L.; Purnelle, B.; Coster, F.; !1Goffeau, A. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67892 !'##molecule_type DNA !'##residues 1-308 ##label FOU !'##cross-references EMBL:Z74371; NID:g1431538; PIDN:CAA98894.1; !1PID:g1431539; GSPDB:GN00004; MIPS:YDR075w !'##experimental_source strain S288C GENETICS !$#gene SGD:PPH3; MIPS:YDR075w !'##cross-references SGD:S0002482; MIPS:YDR075w !$#map_position 4R FUNCTION !$#description phosphoric monoester hydrolase CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$17-276 #domain phosphoprotein phosphatase homology #label !8PPP\ !$45-113 #domain phosphoesterase core homology #label PEC\ !$51,53,79 #binding_site iron (Asp, His, Asp) #status predicted\ !$79,111,161,235 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$82,112,259 #active_site Asp, His, Tyr #status predicted\ !$83,208 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 308 #molecular-weight 35264 #checksum 1003 SEQUENCE /// ENTRY PABY1 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) SIT4 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES PPH1 protein; protein D2693; protein YDL047w; suppressor protein SIT4 ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 21-Jul-2000 ACCESSIONS A31874; S67580 REFERENCE A31874 !$#authors Arndt, K.T.; Styles, C.A.; Fink, G.R. !$#journal Cell (1989) 56:527-537 !$#title A suppressor of a HIS4 transcriptional defect encodes a !1protein with homology to the catalytic subunit of protein !1phosphatases. !$#cross-references MUID:89136000; PMID:2537149 !$#accession A31874 !'##molecule_type DNA !'##residues 1-311 ##label ARN !'##cross-references EMBL:M24395; NID:g341163; PIDN:AAA56864.1; !1PID:g598433 REFERENCE S67560 !$#authors Paulin, L.; Saren, A.M.; Laamanen, P. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67580 !'##molecule_type DNA !'##residues 1-311 ##label PAU !'##cross-references EMBL:Z74095; NID:g1431037; PIDN:CAA98609.1; !1PID:g1431038; GSPDB:GN00004; MIPS:YDL047w !'##experimental_source strain S288C GENETICS !$#gene SGD:SIT4; PPH1; MIPS:YDL047w !'##cross-references SGD:S0002205; MIPS:YDL047w !$#map_position 4L CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$19-280 #domain phosphoprotein phosphatase homology #label !8PPP\ !$47-116 #domain phosphoesterase core homology #label PEC\ !$53,55,82 #binding_site iron (Asp, His, Asp) #status predicted\ !$82,114,164,238 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$85,115,263 #active_site Asp, His, Tyr #status predicted\ !$86,211 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 311 #molecular-weight 35537 #checksum 8002 SEQUENCE /// ENTRY A47727 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) SPCC1739.12 - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES cell shape control protein phosphatase ppe1; protein phosphatase esp1; serine-threonine phosphatase ORGANISM #formal_name Schizosaccharomyces pombe DATE 21-Jan-1994 #sequence_revision 18-Nov-1994 #text_change 09-Nov-2001 ACCESSIONS A47727; A47728; T41120; S33699 REFERENCE A47727 !$#authors Shimanuki, M.; Kinoshita, N.; Ohkura, H.; Yoshida, T.; Toda, !1T.; Yanagida, M. !$#journal Mol. Biol. Cell (1993) 4:303-313 !$#title Isolation and characterization of the fission yeast protein !1phosphatase gene ppe1+ involved in cell shape control and !1mitosis. !$#cross-references MUID:93250325; PMID:8387356 !$#accession A47727 !'##molecule_type DNA !'##residues 1-305 ##label SHI !'##cross-references GB:D13712; NID:g303942; PIDN:BAA02865.1; !1PID:g391946 !'##note sequence extracted from NCBI backbone (NCBIN:131118, !1NCBIP:131119) REFERENCE A47728 !$#authors Matsumoto, T.; Beach, D. !$#journal Mol. Biol. Cell (1993) 4:337-345 !$#title Interaction of the pim1/spi1 mitotic checkpoint with a !1protein phosphatase. !$#cross-references MUID:93250328; PMID:8387358 !$#accession A47728 !'##molecule_type DNA !'##residues 1-305 ##label MAT !'##cross-references EMBL:Z18925; NID:g312019; PIDN:CAA79358.1; !1PID:g312020 !'##note sequence extracted from NCBI backbone (NCBIN:131120, !1NCBIP:131121) REFERENCE Z21969 !$#authors Lyne, M.; Rajandream, M.A.; Barrell, B.G.; Murphy, L.; !1Harris, D. !$#submission submitted to the EMBL Data Library, September 1998 !$#accession T41120 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-305 ##label LYN !'##cross-references EMBL:AL031540; PIDN:CAA20786.1; GSPDB:GN00068; !1SPDB:SPCC1739.12 !'##experimental_source strain 972h-; cosmid c1739 GENETICS !$#gene SPCC1739.12 !$#map_position 3 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$17-277 #domain phosphoprotein phosphatase homology #label !8PPP\ !$45-113 #domain phosphoesterase core homology #label PEC\ !$51,53,79 #binding_site iron (Asp, His, Asp) #status predicted\ !$79,111,161,235 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$82,112,260 #active_site Asp, His, Tyr #status predicted\ !$83,208 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 305 #molecular-weight 35259 #checksum 9585 SEQUENCE /// ENTRY T51050 #type complete TITLE probable phosphoprotein phosphatase (EC 3.1.3.16) B12F1.20 [similarity] - Neurospora crassa ALTERNATE_NAMES cell shape control protein phosphatase ppe1; protein B12F1.20 ORGANISM #formal_name Neurospora crassa DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 09-Nov-2001 ACCESSIONS T51050 REFERENCE Z25286 !$#authors Schulte, U.; Aign, V.; Hoheisel, J.; Brandt, P.; Fartmann, !1B.; Holland, R.; Nyakatura, G.; Mewes, H.W.; Mannhaupt, G. !$#submission submitted to the Protein Sequence Database, July 2000 !$#accession T51050 !'##molecule_type DNA !'##residues 1-334 ##label SCH !'##cross-references EMBL:AL390091; GSPDB:GN00116; NCSP:B12F1.20 !'##experimental_source BAC clone B12F1; strain OR74A GENETICS !$#gene NCSP:B12F1.20 !$#map_position 6 !$#introns 50/1; 85/1; 128/2; 271/3 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$31-305 #domain phosphoprotein phosphatase homology #label !8PPP\ !$59-141 #domain phosphoesterase core homology #label PEC\ !$65,67,107 #binding_site iron (Asp, His, Asp) #status predicted\ !$107,139,189,263 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$110,140,288 #active_site Asp, His, Tyr #status predicted\ !$111,236 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 334 #molecular-weight 37296 #checksum 3906 SEQUENCE /// ENTRY PABY21 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) PPH21 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES phosphoprotein phosphatase 2A-beta.1 catalytic chain; protein D2180; protein YDL134c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 21-Jul-2000 ACCESSIONS A41525; S12500; S67680; S17480 REFERENCE A41525 !$#authors Ronne, H.; Carlberg, M.; Hu, G.Z.; Nehlin, J.O. !$#journal Mol. Cell. Biol. (1991) 11:4876-4884 !$#title Protein phosphatase 2A in Saccharomyces cerevisiae: effects !1on cell growth and bud morphogenesis. !$#cross-references MUID:92017761; PMID:1656215 !$#accession A41525 !'##molecule_type DNA !'##residues 1-369 ##label RON !'##cross-references GB:X58856; NID:g4202; PIDN:CAA41656.1; PID:g4203 REFERENCE S12500 !$#authors Sneddon, A.A.; Cohen, P.T.W.; Stark, M.J.R. !$#journal EMBO J. (1990) 9:4339-4346 !$#title Saccharomyces cerevisiae protein phosphatase 2A performs an !1essential cellular function and is encoded by two genes. !$#cross-references MUID:91092257; PMID:2176150 !$#accession S12500 !'##molecule_type DNA !'##residues 1-369 ##label SNE !'##cross-references EMBL:X56261; NID:g4200; PIDN:CAA39702.1; PID:g4201 !'##experimental_source strain LL20 REFERENCE S67677 !$#authors Saluz, H.P.; Woelfl, S.; Hanemann, V. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67680 !'##molecule_type DNA !'##residues 1-369 ##label SAL !'##cross-references EMBL:Z74182; NID:g1431204; PIDN:CAA98707.1; !1PID:g1431205; GSPDB:GN00004; MIPS:YDL134c !'##experimental_source strain S288C GENETICS !$#gene SGD:PPH21; MIPS:YDL134c !'##cross-references SGD:S0002292; MIPS:YDL134c !$#map_position 4L CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$83-342 #domain phosphoprotein phosphatase homology #label !8PPP\ !$114-182 #domain phosphoesterase core homology #label PEC\ !$117,119,145 #binding_site iron (Asp, His, Asp) #status predicted\ !$145,177,227,301 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$148,178,325 #active_site Asp, His, Tyr #status predicted\ !$149,274 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 369 #molecular-weight 41938 #checksum 6708 SEQUENCE /// ENTRY PABY22 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) PPH22 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES phosphoprotein phosphatase 2A-beta.2 catalytic chain; protein D1271; protein YDL188c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 21-Jul-2000 ACCESSIONS B41525; S12501; S14773; S58730; S67743; S17481 REFERENCE A41525 !$#authors Ronne, H.; Carlberg, M.; Hu, G.Z.; Nehlin, J.O. !$#journal Mol. Cell. Biol. (1991) 11:4876-4884 !$#title Protein phosphatase 2A in Saccharomyces cerevisiae: effects !1on cell growth and bud morphogenesis. !$#cross-references MUID:92017761; PMID:1656215 !$#accession B41525 !'##molecule_type DNA !'##residues 1-377 ##label RON !'##cross-references GB:X58857; NID:g4204; PIDN:CAA41659.1; PID:g4208 REFERENCE S12500 !$#authors Sneddon, A.A.; Cohen, P.T.W.; Stark, M.J.R. !$#journal EMBO J. (1990) 9:4339-4346 !$#title Saccharomyces cerevisiae protein phosphatase 2A performs an !1essential cellular function and is encoded by two genes. !$#cross-references MUID:91092257; PMID:2176150 !$#accession S12501 !'##molecule_type DNA !'##residues 1-377 ##label SNE !'##cross-references EMBL:X56262; NID:g4209; PIDN:CAA39703.1; PID:g4210 !'##experimental_source strain LL20 REFERENCE S14773 !$#authors Sutton, A.; Immanuel, D.; Arndt, K.T. !$#journal Mol. Cell. Biol. (1991) 11:2133-2148 !$#title The SIT4 protein phosphatase functions in late G(1) for !1progression into S phase. !$#cross-references MUID:91172202; PMID:1848673 !$#accession S14773 !'##molecule_type DNA !'##residues 1-377 ##label SUT !'##cross-references EMBL:M60317; NID:g1435187; PIDN:AAB04032.1; !1PID:g172610 REFERENCE S58730 !$#authors Verhasselt, P.; Voet, M.; Volckaert, G. !$#journal Yeast (1995) 11:961-966 !$#title New open reading frames, one of which is similar to the nifV !1gene of Azotobacter vinelandii, found on a 12.5 kbp fragment !1of chromosome IV of Saccharomyces cerevisiae. !$#cross-references MUID:96021607; PMID:8533471 !$#accession S58730 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-377 ##label VER !'##cross-references EMBL:X83276; NID:g1004294; PIDN:CAA58259.1; !1PID:g1004307 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1994 REFERENCE S67735 !$#authors Volckaert, G.; Verhasselt, P.; Voet, M. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67743 !'##molecule_type DNA !'##residues 1-377 ##label VOL !'##cross-references EMBL:Z74236; NID:g1431305; PIDN:CAA98765.1; !1PID:g1431306; GSPDB:GN00004; MIPS:YDL188c !'##experimental_source strain S288C GENETICS !$#gene SGD:PPH22; MIPS:YDL188c !'##cross-references SGD:S0002347; MIPS:YDL188c !$#map_position 4L CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$91-350 #domain phosphoprotein phosphatase homology #label !8PPP\ !$122-190 #domain phosphoesterase core homology #label PEC\ !$125,127,153 #binding_site iron (Asp, His, Asp) #status predicted\ !$153,185,235,309 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$156,186,333 #active_site Asp, His, Tyr #status predicted\ !$157,282 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 377 #molecular-weight 43047 #checksum 5210 SEQUENCE /// ENTRY T27049 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) Y49E10.3 [similarity] - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 09-Nov-2001 ACCESSIONS T27049 REFERENCE Z20303 !$#authors Barlow, K. !$#submission submitted to the EMBL Data Library, August 1997 !$#accession T27049 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-321 ##label WIL !'##cross-references EMBL:Z98866; PIDN:CAB11559.1; GSPDB:GN00021; !1CESP:Y49E10.3 !'##experimental_source clone Y49E10 GENETICS !$#gene CESP:Y49E10.3 !$#map_position 3 !$#introns 19/2; 60/3; 276/2 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$30-290 #domain phosphoprotein phosphatase homology #label !8PPP\ !$58-126 #domain phosphoesterase core homology #label PEC\ !$64,66,92 #binding_site iron (Asp, His, Asp) #status predicted\ !$92,124,174,249 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$95,125,273 #active_site Asp, His, Tyr #status predicted\ !$96,222 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 321 #molecular-weight 36306 #checksum 8851 SEQUENCE /// ENTRY H96539 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) F14I3.5 [similarity] - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 02-Mar-2001 #sequence_revision 02-Mar-2001 #text_change 09-Nov-2001 ACCESSIONS H96539 REFERENCE A86141 !$#authors Theologis, A.; Ecker, J.R.; Palm, C.J.; Federspiel, N.A.; !1Kaul, S.; White, O.; Alonso, J.; Altaf, H.; Araujo, R.; !1Bowman, C.L.; Brooks, S.Y.; Buehler, E.; Chan, A.; Chao, Q.; !1Chen, H.; Cheuk, R.F.; Chin, C.W.; Chung, M.K.; Conn, L.; !1Conway, A.B.; Conway, A.R.; Creasy, T.H.; Dewar, K.; Dunn, !1P.; Etgu, P.; Feldblyum, T.V.; Feng, J.; Fong, B.; Fujii, !1C.Y.; Gill, J.E.; Goldsmith, A.D.; Haas, B.; Hansen, N.F.; !1Hughes, B.; Huizar, L.; Hunter, J.L.; Jenkins, J.; !1Johnson-Hopson, C.; Khan, S.; Khaykin, E.; Kim, C.J.; Koo, !1H.L.; Kremenetskaia, I.; Kurtz, D.B.; Kwan, A.; Lam, B.; !1Langin-Hooper, S.; Lee, A.; Lee, J.M.; Lenz, C.A.; Li, J.H.; !1Li, Y.; Lin, X.; Liu, S.X.; Liu, Z.A.; Luros, J.S.; Maiti, !1R.; Marziali, A.; Militscher, J.; Miranda, M.; Nguyen, M.; !1Nierman, W.C.; Osborne, B.I.; Pai, G.; Peterson, J.; Pham, !1P.K.; Rizzo, M.; Rooney, T.; Rowley, D.; Sakano, H.; !1Salzberg, S.L.; Schwartz, J.R.; Shinn, P.; Southwick, A.M.; !1Sun, H.; Tallon, L.J.; Tambunga, G.; Toriumi, M.J.; Town, !1C.D.; Utterback, T.; van Aken, S.; Vaysberg, M.; Vysotskaia, !1V.S.; Walker, M.; Wu, D.; Yu, G.; Fraser, C.M.; Venter, !1J.C.; Davis, R.W. !$#journal Nature (2000) 408:816-820 !$#title Sequence and analysis of chromosome 1 of the plant !1Arabidopsis. !$#cross-references MUID:21016719; PMID:11130712 !$#accession H96539 !'##molecule_type DNA !'##residues 1-303 ##label STO !'##cross-references GB:AE005173; NID:g5734785; PIDN:AAD50050.1; !1GSPDB:GN00141 GENETICS !$#gene F14I3.5 !$#map_position 1 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$16-276 #domain phosphoprotein phosphatase homology #label !8PPP\ !$44-112 #domain phosphoesterase core homology #label PEC\ !$50,52,78 #binding_site iron (Asp, His, Asp) #status predicted\ !$78,110,160,234 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$81,111,259 #active_site Asp, His, Tyr #status predicted\ !$82,207 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 303 #molecular-weight 34819 #checksum 3576 SEQUENCE /// ENTRY T19701 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) C34C12.3 - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 09-Nov-2001 ACCESSIONS T19701 REFERENCE Z19166 !$#authors Kershaw, J. !$#submission submitted to the EMBL Data Library, December 1994 !$#accession T19701 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-382 ##label WIL !'##cross-references EMBL:Z46996; PIDN:CAA87100.1; GSPDB:GN00021; !1CESP:C34C12.3 !'##experimental_source clone C34C12 GENETICS !$#gene CESP:C34C12.3 !$#map_position 3 !$#introns 77/2; 107/2; 145/1; 179/2; 221/3; 265/3; 292/3; 336/1 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$96-356 #domain phosphoprotein phosphatase homology #label !8PPP\ !$124-192 #domain phosphoesterase core homology #label PEC\ !$130,132,158 #binding_site iron (Asp, His, Asp) #status predicted\ !$158,190,240,315 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$161,191,339 #active_site Asp, His, Tyr #status predicted\ !$162,288 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 382 #molecular-weight 43269 #checksum 2176 SEQUENCE /// ENTRY A46240 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) 1-alpha catalytic chain, splice form 2 [validated] - human ALTERNATE_NAMES protein phosphatase PPP1CA; protein phosphatase type 1 catalytic subunit (PP-1 alpha 2) CONTAINS phosphoprotein phosphatase 1-alpha catalytic chain, splice form 1 ORGANISM #formal_name Homo sapiens #common_name man DATE 02-May-1994 #sequence_revision 18-Nov-1994 #text_change 09-Nov-2001 ACCESSIONS A46240; A32729; JN0723; S29985 REFERENCE A46240 !$#authors Durfee, T.; Becherer, K.; Chen, P.L.; Yeh, S.H.; Yang, Y.; !1Kilburn, A.E.; Lee, W.H.; Elledge, S.J. !$#journal Genes Dev. (1993) 7:555-569 !$#title The retinoblastoma protein associates with the protein !1phosphatase type 1 catalytic subunit. !$#cross-references MUID:93209540; PMID:8384581 !$#accession A46240 !'##molecule_type mRNA !'##residues 1-341 ##label DUR !'##cross-references GB:S57501; NID:g298963; PIDN:AAB26015.1; !1PID:g298964 !'##note sequence extracted from NCBI backbone (NCBIN:128433, !1NCBIP:128434) REFERENCE A32729 !$#authors Barker, H.M.; Jones, T.A.; da Cruz e Silva, E.F.; Spurr, !1N.K.; Sheer, D.; Cohen, P.T.W. !$#journal Genomics (1990) 7:159-166 !$#title Localization of the gene encoding a type I protein !1phosphatase catalytic subunit to human chromosome band !111q13. !$#cross-references MUID:90269804; PMID:2161401 !$#accession A32729 !'##molecule_type mRNA !'##residues 34-341 ##label BAR !'##cross-references GB:J04759; NID:g190280; PIDN:AAA36475.1; !1PID:g190281 REFERENCE JN0723 !$#authors Song, Q.; Khanna, K.K.; Lu, H.; Lavin, M.F. !$#journal Gene (1993) 129:291-295 !$#title Cloning and characterization of a human protein phosphatase !11-encoding cDNA. !$#cross-references MUID:93314976; PMID:8392016 !$#accession JN0723 !'##molecule_type mRNA !'##residues 1-18,30-341 ##label SON !'##cross-references EMBL:X70848; NID:g287796; PIDN:CAA50197.1; !1PID:g35451 !'##note the authors translated the codon TTC for residue 320 as Leu COMMENT This enzyme plays a key role in cell cycle control and !1regulates glycogen metabolism and muscle contraction. GENETICS !$#gene GDB:PPP1CA; PPP1A !'##cross-references GDB:120310; OMIM:176875 !$#map_position 11q13-11q13 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS alternative splicing; iron; metalloprotein; phosphoric !1monoester hydrolase; serine/threonine-specific phosphatase; !1zinc FEATURE !$41-300 #domain phosphoprotein phosphatase homology #label !8PPP\ !$69-137 #domain phosphoesterase core homology #label PEC\ !$75,77,103 #binding_site iron (Asp, His, Asp) #status predicted\ !$103,135,184,259 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$106,136,283 #active_site Asp, His, Tyr #status predicted\ !$107,232 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 341 #molecular-weight 38631 #checksum 9126 SEQUENCE /// ENTRY JX0157 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) 1-alpha catalytic chain [validated] - rat ALTERNATE_NAMES protein phosphatase 1, catalytic subunit ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 21-Nov-1993 #sequence_revision 16-Feb-1996 #text_change 09-Nov-2001 ACCESSIONS JX0157; D36491; I56953; I56556; S68721 REFERENCE JX0157 !$#authors Kitamura, K.; Mizuno, Y.; Sasaki, A.; Yasui, A.; Tsuiki, S.; !1Kikuchi, K. !$#journal J. Biochem. (1991) 109:307-310 !$#title Molecular cloning and sequence analysis of cDNA for the !1catalytic subunit 1 alpha of rat kidney type 1 protein !1phosphatase, and detection of the gene expression at high !1levels in hepatoma cells and regenerating livers as compared !1to rat livers. !$#cross-references MUID:91324314; PMID:1650776 !$#accession JX0157 !'##molecule_type mRNA !'##residues 1-330 ##label KIT !'##cross-references GB:D00859; NID:g220866; PIDN:BAA00732.1; !1PID:g220867 REFERENCE A36491 !$#authors Wadzinski, B.E.; Heasley, L.E.; Johnson, G.L. !$#journal J. Biol. Chem. (1990) 265:21504-21508 !$#title Multiplicity of protein serine-threonine phosphatases in !1PC12 pheochromocytoma and FTO-2B hepatoma cells. !$#cross-references MUID:91072341; PMID:2174876 !$#accession D36491 !'##molecule_type mRNA !'##residues 210-229,'D',231-232,'S',234-236,'NR',239-267 ##label WAD !'##cross-references GB:M58434; NID:g206288; PIDN:AAA41905.1; !1PID:g206289; GB:J05720 REFERENCE I56953 !$#authors Sasaki, K.; Shima, H.; Kitagawa, Y.; Irino, S.; Sugimura, !1T.; Nagao, M. !$#journal Jpn. J. Cancer Res. (1990) 81:1272-1280 !$#title Identification of members of the protein phosphatase 1 gene !1family in the rat and enhanced expression of protein !1phosphatase 1a gene in rat hepatocellular carcinomas. !$#cross-references MUID:91115668; PMID:2177460 !$#accession I56953 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-330 ##label SAS !'##cross-references GB:D90163; NID:g3236121; PIDN:BAA14194.1; !1PID:g220865 REFERENCE I56556 !$#authors da Cruz e Silva, E.F.; Fox, C.A.; Ouimet, C.C.; Gustafson, !1E.; Watson, S.J.; Greengard, P. !$#journal J. Neurosci. (1995) 15:3375-3389 !$#title Differential expression of protein phosphatase 1 isoforms in !1mammalian brain. !$#cross-references MUID:95271296; PMID:7751917 !$#accession I56556 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-330 ##label CRU !'##cross-references GB:S78215; NID:g999338; PIDN:AAB34333.1; !1PID:g999339 REFERENCE S68721 !$#authors Moorhead, G.; MacKintosh, C.; Morrice, N.; Cohen, P. !$#journal FEBS Lett. (1995) 362:101-105 !$#title Purification of the hepatic glycogen-associated form of !1protein phosphatase-1 by microcystin-Sepharose affinity !1chromatography. !$#cross-references MUID:95237359; PMID:7720853 !$#accession S68721 !'##molecule_type protein !'##residues 306-317 ##label MOO !'##experimental_source liver CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS glycogen metabolism; heterodimer; iron; metalloprotein; !1phosphoric monoester hydrolase; serine/threonine-specific !1phosphatase; zinc FEATURE !$30-289 #domain phosphoprotein phosphatase homology #label !8PPP\ !$58-126 #domain phosphoesterase core homology #label PEC\ !$64,66,92 #binding_site iron (Asp, His, Asp) #status predicted\ !$92,124,173,248 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$95,125,272 #active_site Asp, His, Tyr #status predicted\ !$96,221 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 330 #molecular-weight 37512 #checksum 2456 SEQUENCE /// ENTRY PARB11 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) 1-alpha catalytic chain [validated] - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 15-Sep-2000 ACCESSIONS S04335; S09417; S09352; A60239; S00607 REFERENCE S04335 !$#authors Cohen, P.T.W.; Schelling, D.L.; da Cruz e Silva, O.B.; !1Barker, H.M.; Cohen, P. !$#journal Biochim. Biophys. Acta (1989) 1008:125-128 !$#title The major type-1 protein phosphatase catalytic subunits are !1the same gene products in rabbit skeletal muscle and rabbit !1liver. !$#cross-references MUID:89247442; PMID:2541784 !$#accession S04335 !'##molecule_type mRNA !'##residues 1-330 ##label COH !'##cross-references EMBL:X14832; NID:g1678; PIDN:CAA32941.1; PID:g1679 REFERENCE S09417 !$#authors Bai, G.; Zhang, Z.; Amin, J.; Deans-Zirattu, S.A.; Lee, !1E.Y.C. !$#journal FASEB J. (1988) 2:3010-3016 !$#title Molecular cloning of a cDNA for the catalytic subunit of !1rabbit muscle phosphorylase phosphatase. !$#cross-references MUID:89031735; PMID:2846396 !$#accession S09417 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-330 ##label BAI REFERENCE S00174 !$#authors Berndt, N.; Campbell, D.G.; Caudwell, F.B.; Cohen, P.; da !1Cruz e Silva, E.F.; da Cruz e Silva, O.B.; Cohen, P.T.W. !$#journal FEBS Lett. (1987) 223:340-346 !$#title Isolation and sequence analysis of a cDNA clone encoding a !1type-1 protein phosphatase catalytic subunit: homology with !1protein phosphatase 2A. !$#cross-references MUID:88030078; PMID:2822491 !$#accession S09352 !'##molecule_type protein !'##residues 44-60;61-69,'T',71-74;75-84,'A',86-96;151-168;169-195,'X', !1197,'T',199-201,'X',203-205;212-225;226-229,'D',231-232,'S', !1234-235;247-260 ##label BER REFERENCE A65601 !$#authors Goldberg, J.; Nairn, A.C.; Kuriyan, J. !$#submission submitted to the Brookhaven Protein Data Bank, December 1995 !$#cross-references PDB:1FJM !$#contents annotation; X-ray crystallography, 2.1 angstroms, residues !17-300 REFERENCE A58724 !$#authors Goldberg, J.; Huang, H.B.; Kwon, Y.G.; Greengard, P.; Nairn, !1A.C.; Kuriyan, J. !$#journal Nature (1995) 376:745-753 !$#title Three-dimensional structure of the catalytic subunit of !1protein serine/threonine phosphatase-1. !$#cross-references MUID:95379968; PMID:7651533 !$#contents annotation; X-ray crystallography, 2.1 angstroms !$#note the crystal structure was determined for a fully active !1enzyme with manganese 1 in what is thought to be the iron !1binding site and manganese 2 in what is thought to be the !1the zinc binding site FUNCTION !$#description catalyzes hydrolysis of peptidyl-phosphoserine or !1-phosphothreonine to release phosphate CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS alternative splicing; iron; manganese; phosphoric monoester !1hydrolase; serine/threonine-specific phosphatase; zinc FEATURE !$30-289 #domain phosphoprotein phosphatase homology #label !8PPP\ !$58-126 #domain phosphoesterase core homology #label PEC\ !$64,66,92 #binding_site manganese 1 (Asp, His, Asp) #status !8experimental\ !$92,124,173,248 #binding_site manganese 2 (Asp, Asn, His, His) !8#status experimental\ !$95,125,272 #active_site Asp, His, Tyr #status predicted\ !$96,221 #binding_site substrate phosphate (Arg) #status !8experimental SUMMARY #length 330 #molecular-weight 37512 #checksum 2456 SEQUENCE /// ENTRY T16476 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) 1-alpha F56C9.1 [similarity] - Caenorhabditis elegans ALTERNATE_NAMES protein phosphatase 1, catalytic subunit ORGANISM #formal_name Caenorhabditis elegans DATE 20-Sep-1999 #sequence_revision 20-Sep-1999 #text_change 09-Nov-2001 ACCESSIONS T16476 REFERENCE S46729 !$#authors Du, Z. !$#submission submitted to the EMBL Data Library, May 1994 !$#description The sequence of C. elegans cosmid F56C9. !$#accession T16476 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-333 ##label DUZ !'##cross-references EMBL:U00063; NID:g488186; PID:g488187; !1PIDN:AAB08710.1; CESP:F56C9.1 !'##experimental_source strain Bristol N2 GENETICS !$#gene CESP:F56C9.1 !$#introns 18/1; 62/1; 139/1; 210/3; 248/3; 293/3 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS glycogen metabolism; heterodimer; iron; metalloprotein; !1phosphoric monoester hydrolase; serine/threonine-specific !1phosphatase; zinc FEATURE !$29-288 #domain phosphoprotein phosphatase homology #label !8PPP\ !$57-125 #domain phosphoesterase core homology #label PEC\ !$63,65,91 #binding_site iron (Asp, His, Asp) #status predicted\ !$91,123,172,247 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$94,124,271 #active_site Asp, His, Tyr #status predicted\ !$95,220 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 333 #molecular-weight 37791 #checksum 4095 SEQUENCE /// ENTRY S41052 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) 1-beta [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 19-May-1994 #sequence_revision 10-Nov-1995 #text_change 09-Nov-2001 ACCESSIONS S41052; I38126 REFERENCE S41052 !$#authors Barker, H.M.; Brewis, N.D.; Street, A.J.; Spurr, N.K.; !1Cohen, P.T.W. !$#journal Biochim. Biophys. Acta (1994) 1220:212-218 !$#title Three genes for protein phosphatase 1 map to different human !1chromosomes: sequence, expression and gene localisation of !1protein serine/threonine phosphatase 1 beta (PPP1CB). !$#cross-references MUID:94146118; PMID:8312365 !$#accession S41052 !'##status preliminary !'##molecule_type mRNA !'##residues 1-327 ##label BAR !'##cross-references GB:X80910; NID:g531475; PIDN:CAA56870.1; !1PID:g531476 REFERENCE I38126 !$#authors Prochazka, M.; Mochizuki, H.; Baier, L.J.; Cohen, P.T.; !1Bogardus, C. !$#journal Diabetologia (1995) 38:461-466 !$#title Molecular and linkage analysis of type-1 protein phosphatase !1catalytic beta-subunit gene: lack of evidence for its major !1role in insulin resistance in Pima Indians. !$#cross-references MUID:95317505; PMID:7796987 !$#accession I38126 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-327 ##label RES !'##cross-references EMBL:U11005; NID:g506770; PIDN:AAA85093.1; !1PID:g506772 GENETICS !$#gene GDB:PPP1CB !'##cross-references GDB:136793; OMIM:600590 !$#map_position 2p23-2p23 !$#introns 18/1; 62/1; 139/1; 174/1; 198/1; 248/3; 293/3 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$29-288 #domain phosphoprotein phosphatase homology #label !8PPP\ !$57-125 #domain phosphoesterase core homology #label PEC\ !$63,65,91 #binding_site iron (Asp, His, Asp) #status predicted\ !$91,123,172,247 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$94,124,271 #active_site Asp, His, Tyr #status predicted\ !$95,220 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 327 #molecular-weight 37186 #checksum 2607 SEQUENCE /// ENTRY S13829 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) 1-beta catalytic chain [validated] - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 09-Nov-2001 ACCESSIONS S13829; S27045 REFERENCE S13827 !$#authors Dombradi, V.; Axton, J.M.; Brewis, N.D.; da Cruz e Silva, !1E.F.; Alphey, L.; Cohen, P.T.W. !$#journal Eur. J. Biochem. (1990) 194:739-745 !$#title Drosophila contains three genes that encode distinct !1isoforms of protein phosphatase 1. !$#cross-references MUID:91099353; PMID:2176604 !$#accession S13829 !'##molecule_type mRNA !'##residues 1-327 ##label DOM !'##cross-references EMBL:X61639; NID:g1680; PIDN:CAA43820.1; PID:g1681 REFERENCE S27045 !$#authors Dent, P.; MacDougall, L.K.; MacKintosh, C.; Campbell, D.G.; !1Cohen, P. !$#journal Eur. J. Biochem. (1992) 210:1037-1044 !$#title A myofibrillar protein phosphatase from rabbit skeletal !1muscle contains the beta isoform of protein phosphatase-1 !1complexed to a regulatory subunit which greatly enhances the !1dephosphorylation of myosin. !$#cross-references MUID:93130883; PMID:1336456 !$#accession S27045 !'##molecule_type protein !'##residues 26-35;60-73;147-149;168-186;'X',222-232;246-259;304-319 !1##label DEN CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$29-288 #domain phosphoprotein phosphatase homology #label !8PPP\ !$57-125 #domain phosphoesterase core homology #label PEC\ !$63,65,91 #binding_site iron (Asp, His, Asp) #status predicted\ !$91,123,172,247 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$94,124,271 #active_site Asp, His, Tyr #status predicted\ !$95,220 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 327 #molecular-weight 37186 #checksum 2607 SEQUENCE /// ENTRY D32550 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) 1-beta catalytic chain [similarity] - mouse ALTERNATE_NAMES chromosome disjoining protein dis2m2 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 12-Oct-1989 #sequence_revision 28-Aug-1992 #text_change 09-Nov-2001 ACCESSIONS D32550 REFERENCE A32550 !$#authors Ohkura, H.; Kinoshita, N.; Miyatani, S.; Toda, T.; Yanagida, !1M. !$#journal Cell (1989) 57:997-1007 !$#title The fission yeast dis2(+) gene required for chromosome !1disjoining encodes one of two putative type 1 protein !1phosphatases. !$#cross-references MUID:89288305; PMID:2544298 !$#accession D32550 !'##status preliminary !'##molecule_type DNA !'##residues 1-327 ##label OHK !'##cross-references GB:M27073; NID:g471977; PIDN:AAA37527.1; !1PID:g471978 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$29-288 #domain phosphoprotein phosphatase homology #label !8PPP\ !$57-125 #domain phosphoesterase core homology #label PEC\ !$63,65,91 #binding_site iron (Asp, His, Asp) #status predicted\ !$91,123,172,247 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$94,124,271 #active_site Asp, His, Tyr #status predicted\ !$95,220 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 327 #molecular-weight 37186 #checksum 2607 SEQUENCE /// ENTRY T21553 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) 1-beta F29F11.6 [similarity] - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 09-Nov-2001 ACCESSIONS T21553 REFERENCE Z19440 !$#authors Gardner, A. !$#submission submitted to the EMBL Data Library, June 1996 !$#accession T21553 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-329 ##label WIL !'##cross-references EMBL:Z73974; PIDN:CAA98273.1; GSPDB:GN00023; !1CESP:F29F11.6 !'##experimental_source clone F29F11 GENETICS !$#gene CESP:F29F11.6 !$#map_position 5 !$#introns 19/1; 63/1; 140/1; 294/3 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$30-289 #domain phosphoprotein phosphatase homology #label !8PPP\ !$58-126 #domain phosphoesterase core homology #label PEC\ !$64,66,92 #binding_site iron (Asp, His, Asp) #status predicted\ !$92,124,173,248 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$95,125,272 #active_site Asp, His, Tyr #status predicted\ !$96,221 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 329 #molecular-weight 37204 #checksum 8445 SEQUENCE /// ENTRY S35699 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) 1-gamma catalytic chain, splice form 1 [validated] - human ALTERNATE_NAMES protein phosphatase-1 ORGANISM #formal_name Homo sapiens #common_name man DATE 03-Mar-1994 #sequence_revision 10-Nov-1995 #text_change 09-Nov-2001 ACCESSIONS S35699; I57016; S66644 REFERENCE S35699 !$#authors Barker, H.M.; Craig, S.P.; Spurr, N.K.; Cohen, P.T.W. !$#journal Biochim. Biophys. Acta (1993) 1178:228-233 !$#title Sequence of human protein serine/threonine phosphatase 1 !1gamma and localization of the gene (PPP1CC) encoding it to !1chromosome bands 12q24.1-q24.2. !$#cross-references MUID:93349989; PMID:8394140 !$#accession S35699 !'##molecule_type mRNA !'##residues 1-323 ##label BAR !'##cross-references EMBL:X74008; NID:g402777; PIDN:CAA52169.1; !1PID:g402778 REFERENCE I57016 !$#authors Norman, S.A.; Mott, D.M. !$#journal Mamm. Genome (1994) 5:41-45 !$#title Molecular cloning and chromosomal localization of a human !1skeletal muscle PP-1 gamma 1 cDNA. !$#cross-references MUID:94154385; PMID:8111128 !$#accession I57016 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 5-323 ##label RES !'##cross-references GB:L07395; NID:g190218; PIDN:AAA19823.1; !1PID:g484316 REFERENCE S66644 !$#authors MacKintosh, R.W.; Dalby, K.N.; Campbell, D.G.; Cohen, !1P.T.W.; Cohen, P.; MacKintosh, C. !$#journal FEBS Lett. (1995) 371:236-240 !$#title The cyanobacterial toxin microcystin binds covalently to !1cysteine-273 on protein phosphatase 1. !$#cross-references MUID:96013140; PMID:7556599 !$#accession S66644 !'##molecule_type protein !'##residues 191-201;'XX',264-281 ##label MAC GENETICS !$#gene GDB:PPP1CC !'##cross-references GDB:135661; OMIM:176914 !$#map_position 12q24.1-12q24.2 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS alternative splicing; iron; metalloprotein; phosphoric !1monoester hydrolase; serine/threonine-specific phosphatase; !1zinc FEATURE !$30-289 #domain phosphoprotein phosphatase homology #label !8PPP\ !$58-126 #domain phosphoesterase core homology #label PEC\ !$64,66,92 #binding_site iron (Asp, His, Asp) #status predicted\ !$92,124,173,248 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$95,125,272 #active_site Asp, His, Tyr #status predicted\ !$96,221 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 323 #molecular-weight 36983 #checksum 281 SEQUENCE /// ENTRY S35700 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) 1-gamma catalytic chain, splice form 2 - human ALTERNATE_NAMES phosphoprotein phosphatase-1 ORGANISM #formal_name Homo sapiens #common_name man DATE 03-Mar-1994 #sequence_revision 10-Nov-1995 #text_change 09-Nov-2001 ACCESSIONS S35700 REFERENCE S35699 !$#authors Barker, H.M.; Craig, S.P.; Spurr, N.K.; Cohen, P.T.W. !$#journal Biochim. Biophys. Acta (1993) 1178:228-233 !$#title Sequence of human protein serine/threonine phosphatase 1 !1gamma and localization of the gene (PPP1CC) encoding it to !1chromosome bands 12q24.1-q24.2. !$#cross-references MUID:93349989; PMID:8394140 !$#accession S35700 !'##status preliminary !'##molecule_type mRNA !'##residues 1-337 ##label BAR !'##cross-references EMBL:X74008; NID:g402777 GENETICS !$#gene GDB:PPP1CC !'##cross-references GDB:135661; OMIM:176914 !$#map_position 12q24.1-12q24.2 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS alternative splicing; iron; metalloprotein; phosphoric !1monoester hydrolase; serine/threonine-specific phosphatase; !1zinc FEATURE !$30-289 #domain phosphoprotein phosphatase homology #label !8PPP\ !$58-126 #domain phosphoesterase core homology #label PEC\ !$64,66,92 #binding_site iron (Asp, His, Asp) #status predicted\ !$92,124,173,248 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$95,125,272 #active_site Asp, His, Tyr #status predicted\ !$96,221 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 337 #molecular-weight 38518 #checksum 1636 SEQUENCE /// ENTRY I76573 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) 1-gamma catalytic chain - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 02-Aug-1996 #sequence_revision 02-Aug-1996 #text_change 09-Nov-2001 ACCESSIONS I76573 REFERENCE I56953 !$#authors Sasaki, K.; Shima, H.; Kitagawa, Y.; Irino, S.; Sugimura, !1T.; Nagao, M. !$#journal Jpn. J. Cancer Res. (1990) 81:1272-1280 !$#title Identification of members of the protein phosphatase 1 gene !1family in the rat and enhanced expression of protein !1phosphatase 1a gene in rat hepatocellular carcinomas. !$#cross-references MUID:91115668; PMID:2177460 !$#accession I76573 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-337 ##label RES !'##cross-references GB:D90166; NID:g3236123; PIDN:BAA14197.1; !1PID:g220873 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$30-289 #domain phosphoprotein phosphatase homology #label !8PPP\ !$58-126 #domain phosphoesterase core homology #label PEC\ !$64,66,92 #binding_site iron (Asp, His, Asp) #status predicted\ !$92,124,173,248 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$95,125,272 #active_site Asp, His, Tyr #status predicted\ !$96,221 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 337 #molecular-weight 38538 #checksum 1552 SEQUENCE /// ENTRY C32550 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) 1-gamma catalytic chain - mouse ALTERNATE_NAMES chromosome disjoining protein dis2m1 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 12-Oct-1989 #sequence_revision 12-Oct-1989 #text_change 09-Nov-2001 ACCESSIONS C32550 REFERENCE A32550 !$#authors Ohkura, H.; Kinoshita, N.; Miyatani, S.; Toda, T.; Yanagida, !1M. !$#journal Cell (1989) 57:997-1007 !$#title The fission yeast dis2(+) gene required for chromosome !1disjoining encodes one of two putative type 1 protein !1phosphatases. !$#cross-references MUID:89288305; PMID:2544298 !$#accession C32550 !'##status preliminary !'##molecule_type mRNA !'##residues 1-337 ##label OHK !'##cross-references GB:M27071; NID:g471975; PIDN:AAA37526.1; !1PID:g471976 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$30-289 #domain phosphoprotein phosphatase homology #label !8PPP\ !$58-126 #domain phosphoesterase core homology #label PEC\ !$64,66,92 #binding_site iron (Asp, His, Asp) #status predicted\ !$92,124,173,248 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$95,125,272 #active_site Asp, His, Tyr #status predicted\ !$96,221 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 337 #molecular-weight 38504 #checksum 1810 SEQUENCE /// ENTRY PAFF1A #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) 1-alpha-2 catalytic chain - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES phosphoprotein phosphatase isoform 87B catalytic chain ORGANISM #formal_name Drosophila melanogaster DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Mar-2000 ACCESSIONS S12960; S05524 REFERENCE S12960 !$#authors Dombradi, V.; Axton, J.M.; Barker, H.M.; Cohen, P.T.W. !$#journal FEBS Lett. (1990) 275:39-43 !$#title Protein phosphatase 1 activity in Drosophila mutants with !1abnormalities in mitosis and chromosome condensation. !$#cross-references MUID:91085574; PMID:2175717 !$#accession S12960 !'##molecule_type DNA !'##residues 1-302 ##label DOM !'##cross-references GB:X55198; GB:S47852; NID:g8361; PIDN:CAA38983.1; !1PID:g8362 REFERENCE S05524 !$#authors Dombradi, V.; Axton, J.M.; Glover, D.M.; Cohen, P.T.W. !$#journal Eur. J. Biochem. (1989) 183:603-610 !$#title Cloning and chromosomal localization of Drosophila cDNA !1encoding the catalytic subunit of protein phosphatase !11-alpha. High conservation between mammalian and insect !1sequences. !$#cross-references MUID:89377827; PMID:2550221 !$#accession S05524 !'##molecule_type mRNA !'##residues 1-302 ##label DOM2 !'##cross-references EMBL:X15583; NID:g8363; PIDN:CAA33609.1; PID:g8364 GENETICS !$#gene FlyBase:Pp1-87B !'##cross-references FlyBase:FBgn0004103 !$#map_position 3R 87B6-12 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$28-287 #domain phosphoprotein phosphatase homology #label !8PPP\ !$56-124 #domain phosphoesterase core homology #label PEC\ !$62,64,90 #binding_site iron (Asp, His, Asp) #status predicted\ !$90,122,171,246 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$93,123,270 #active_site Asp, His, Tyr #status predicted\ !$94,219 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 302 #molecular-weight 34541 #checksum 3059 SEQUENCE /// ENTRY S13827 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) 1-alpha-1 catalytic chain - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES phosphoprotein phosphatase isoform 96A catalytic chain ORGANISM #formal_name Drosophila melanogaster DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 21-Jun-2002 ACCESSIONS S13827 REFERENCE S13827 !$#authors Dombradi, V.; Axton, J.M.; Brewis, N.D.; da Cruz e Silva, !1E.F.; Alphey, L.; Cohen, P.T.W. !$#journal Eur. J. Biochem. (1990) 194:739-745 !$#title Drosophila contains three genes that encode distinct !1isoforms of protein phosphatase 1. !$#cross-references MUID:91099353; PMID:2176604 !$#accession S13827 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-327 ##label DOM !'##cross-references GB:X56438; NID:g8365; PIDN:CAA39820.1; PID:g8366 GENETICS !$#gene FlyBase:Pp1-alpha-96A !'##cross-references FlyBase:FBgn0003134 !$#map_position 3 96A2-5 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$28-287 #domain phosphoprotein phosphatase homology #label !8PPP\ !$56-124 #domain phosphoesterase core homology #label PEC\ !$62,64,90 #binding_site iron (Asp, His, Asp) #status predicted\ !$90,122,171,246 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$93,123,270 #active_site Asp, His, Tyr #status predicted\ !$94,219 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 327 #molecular-weight 37370 #checksum 996 SEQUENCE /// ENTRY PAFFY #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) Y - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Mar-2000 ACCESSIONS S03963; S11061 REFERENCE S03963 !$#authors Dombradi, V.; Axton, J.M.; Glover, D.M.; Cohen, P.T.W. !$#journal FEBS Lett. (1989) 247:391-395 !$#title Molecular cloning and chromosomal localization of a novel !1Drosophila protein phosphatase. !$#cross-references MUID:89232161; PMID:2541022 !$#accession S03963 !'##molecule_type mRNA !'##residues 1-314 ##label DOM !'##cross-references EMBL:Y07510; NID:g8371; PIDN:CAA68808.1; PID:g8372 REFERENCE S11059 !$#authors Cohen, P.T.W.; Brewis, N.D.; Hughes, V.; Mann, D.J. !$#journal FEBS Lett. (1990) 268:355-359 !$#title Protein serine/threonine phosphatases; an expanding family. !$#cross-references MUID:90346193; PMID:2166691 !$#accession S11061 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-314 ##label COH GENETICS !$#gene FlyBase:PpY-55A !'##cross-references FlyBase:FBgn0003140 !$#map_position 2R 55A1-3 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$26-285 #domain phosphoprotein phosphatase homology #label !8PPP\ !$54-122 #domain phosphoesterase core homology #label PEC\ !$60,62,88 #binding_site iron (Asp, His, Asp) #status predicted\ !$88,120,169,244 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$91,121,268 #active_site Asp, His, Tyr #status predicted\ !$92,217 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 314 #molecular-weight 36022 #checksum 1802 SEQUENCE /// ENTRY T27138 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) 1 ZK938.1 [similarity] - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 22-Oct-2001 ACCESSIONS T27138; T28116 REFERENCE Z20317 !$#authors Kershaw, J. !$#submission submitted to the EMBL Data Library, May 1997 !$#accession T27138 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-327 ##label WIL !'##cross-references EMBL:Z95623; PIDN:CAB09135.1; GSPDB:GN00020; !1CESP:ZK938.1 !'##experimental_source clone Y53C12C REFERENCE Z20471 !$#authors Lloyd, C. !$#submission submitted to the EMBL Data Library, June 1995 !$#accession T28116 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-327 ##label WI2 !'##cross-references EMBL:Z49913; PIDN:CAA90149.1; GSPDB:GN00020; !1CESP:ZK938.1 !'##experimental_source clone ZK938 GENETICS !$#gene CESP:ZK938.1 !$#map_position 2 !$#introns 14/1; 56/3; 149/3; 239/3; 245/3 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$26-285 #domain phosphoprotein phosphatase homology #label !8PPP\ !$54-122 #domain phosphoesterase core homology #label PEC\ !$60,62,88 #binding_site iron (Asp, His, Asp) #status predicted\ !$88,120,169,244 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$91,121,268 #active_site Asp, His, Tyr #status predicted\ !$92,217 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 327 #molecular-weight 36879 #checksum 4926 SEQUENCE /// ENTRY T22522 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) 1 F52H3.6 [similarity] - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 22-Oct-2001 ACCESSIONS T22522 REFERENCE Z19575 !$#authors Gardner, A. !$#submission submitted to the EMBL Data Library, October 1995 !$#accession T22522 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-329 ##label WIL !'##cross-references EMBL:Z66512; PIDN:CAA91326.1; GSPDB:GN00020; !1CESP:F52H3.6 !'##experimental_source clone F52H3 GENETICS !$#gene CESP:F52H3.6 !$#map_position 2 !$#introns 14/1; 56/3; 149/3; 245/3 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$26-285 #domain phosphoprotein phosphatase homology #label !8PPP\ !$54-122 #domain phosphoesterase core homology #label PEC\ !$60,62,88 #binding_site iron (Asp, His, Asp) #status predicted\ !$88,120,169,244 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$91,121,268 #active_site Asp, His, Tyr #status predicted\ !$92,217 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 329 #molecular-weight 37220 #checksum 2524 SEQUENCE /// ENTRY T29191 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) 1 T03F1.5 [similarity] - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 22-Oct-2001 ACCESSIONS T29191 REFERENCE Z20586 !$#authors Du, Z.; Le, T.T. !$#submission submitted to the EMBL Data Library, February 1997 !$#description The sequence of C. elegans cosmid T03F1. !$#accession T29191 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-305 ##label DUZ !'##cross-references EMBL:U88169; PIDN:AAB42233.1; GSPDB:GN00019; !1CESP:T03F1.5 !'##experimental_source strain Bristol N2; clone T03F1 GENETICS !$#gene CESP:T03F1.5 !$#map_position 1 !$#introns 152/3; 283/3 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$28-288 #domain phosphoprotein phosphatase homology #label !8PPP\ !$56-124 #domain phosphoesterase core homology #label PEC\ !$62,64,90 #binding_site iron (Asp, His, Asp) #status predicted\ !$90,122,172,247 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$93,123,271 #active_site Asp, His, Tyr #status predicted\ !$94,220 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 305 #molecular-weight 34583 #checksum 7209 SEQUENCE /// ENTRY T34462 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) 1 W09C3.6 [similarity] - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 29-Oct-1999 #sequence_revision 29-Oct-1999 #text_change 22-Oct-2001 ACCESSIONS T34462; T42014 REFERENCE Z21529 !$#authors Wamsley, P.; Kramer, J. !$#submission submitted to the EMBL Data Library, February 1997 !$#description The sequence of C. elegans cosmid W09C3. !$#accession T34462 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-305 ##label WAM !'##cross-references EMBL:U88178; PIDN:AAC24414.1; GSPDB:GN00019; !1CESP:W09C3.6 !'##experimental_source strain Bristol N2; clone W09C3 REFERENCE Z22025 !$#authors Zeke, T.; Gergely, P.; Dombradi, V. !$#submission submitted to the EMBL Data Library, July 1996 !$#description The catalytic subunits of Ser/Thr protein phosphatases from !1Caenorhabditis elegans: A biochemical and molecular !1biological survey. !$#accession T42014 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 66-89 ##label ZEK !'##cross-references EMBL:Z77740; PIDN:CAB01299.1 !'##experimental_source strain Bristol; clone C-1 GENETICS !$#gene CESP:W09C3.6 !$#map_position 1 !$#introns 152/3; 283/3 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$28-288 #domain phosphoprotein phosphatase homology #label !8PPP\ !$56-124 #domain phosphoesterase core homology #label PEC\ !$62,64,90 #binding_site iron (Asp, His, Asp) #status predicted\ !$90,122,172,247 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$93,123,271 #active_site Asp, His, Tyr #status predicted\ !$94,220 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 305 #molecular-weight 34596 #checksum 7995 SEQUENCE /// ENTRY T31766 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) 1 C09H5.7 [similarity] - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 29-Oct-1999 #sequence_revision 29-Oct-1999 #text_change 02-Nov-2001 ACCESSIONS T31766 REFERENCE Z21081 !$#authors Le, T.T.; Waterston, R. !$#submission submitted to the EMBL Data Library, July 1997 !$#description The sequence of C. elegans cosmid C09H5. !$#accession T31766 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-348 ##label LET !'##cross-references EMBL:AF016433; PIDN:AAB65386.1; GSPDB:GN00023; !1CESP:C09H5.7 !'##experimental_source strain Bristol N2; clone C09H5 GENETICS !$#gene CESP:C09H5.7 !$#map_position 5 !$#introns 334/3 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$54-329 #domain phosphoprotein phosphatase homology #label !8PPP\ !$82-165 #domain phosphoesterase core homology #label PEC\ !$88,90,131 #binding_site iron (Asp, His, Asp) #status predicted\ !$131,163,213,288 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$134,164,312 #active_site Asp, His, Tyr #status predicted\ !$135,261 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 348 #molecular-weight 39655 #checksum 5468 SEQUENCE /// ENTRY C96665 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) 1 F22C12.20 [similarity] - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 02-Mar-2001 #sequence_revision 02-Mar-2001 #text_change 09-Nov-2001 ACCESSIONS C96665 REFERENCE A86141 !$#authors Theologis, A.; Ecker, J.R.; Palm, C.J.; Federspiel, N.A.; !1Kaul, S.; White, O.; Alonso, J.; Altaf, H.; Araujo, R.; !1Bowman, C.L.; Brooks, S.Y.; Buehler, E.; Chan, A.; Chao, Q.; !1Chen, H.; Cheuk, R.F.; Chin, C.W.; Chung, M.K.; Conn, L.; !1Conway, A.B.; Conway, A.R.; Creasy, T.H.; Dewar, K.; Dunn, !1P.; Etgu, P.; Feldblyum, T.V.; Feng, J.; Fong, B.; Fujii, !1C.Y.; Gill, J.E.; Goldsmith, A.D.; Haas, B.; Hansen, N.F.; !1Hughes, B.; Huizar, L.; Hunter, J.L.; Jenkins, J.; !1Johnson-Hopson, C.; Khan, S.; Khaykin, E.; Kim, C.J.; Koo, !1H.L.; Kremenetskaia, I.; Kurtz, D.B.; Kwan, A.; Lam, B.; !1Langin-Hooper, S.; Lee, A.; Lee, J.M.; Lenz, C.A.; Li, J.H.; !1Li, Y.; Lin, X.; Liu, S.X.; Liu, Z.A.; Luros, J.S.; Maiti, !1R.; Marziali, A.; Militscher, J.; Miranda, M.; Nguyen, M.; !1Nierman, W.C.; Osborne, B.I.; Pai, G.; Peterson, J.; Pham, !1P.K.; Rizzo, M.; Rooney, T.; Rowley, D.; Sakano, H.; !1Salzberg, S.L.; Schwartz, J.R.; Shinn, P.; Southwick, A.M.; !1Sun, H.; Tallon, L.J.; Tambunga, G.; Toriumi, M.J.; Town, !1C.D.; Utterback, T.; van Aken, S.; Vaysberg, M.; Vysotskaia, !1V.S.; Walker, M.; Wu, D.; Yu, G.; Fraser, C.M.; Venter, !1J.C.; Davis, R.W. !$#journal Nature (2000) 408:816-820 !$#title Sequence and analysis of chromosome 1 of the plant !1Arabidopsis. !$#cross-references MUID:21016719; PMID:11130712 !$#accession C96665 !'##molecule_type DNA !'##residues 1-340 ##label STO !'##cross-references GB:AE005173; NID:g6692101; PIDN:AAF24566.1; !1GSPDB:GN00141 GENETICS !$#gene F22C12.20 !$#map_position 1 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$27-296 #domain phosphoprotein phosphatase homology #label !8PPP\ !$55-123 #domain phosphoesterase core homology #label PEC\ !$61,63,89 #binding_site iron (Asp, His, Asp) #status predicted\ !$89,121,170,245 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$92,122,279 #active_site Asp, His, Tyr #status predicted\ !$93,218 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 340 #molecular-weight 38543 #checksum 1053 SEQUENCE /// ENTRY S31087 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) 1 (clone TOPP3) [similarity] - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 13-Jan-1995 #sequence_revision 13-Jan-1995 #text_change 09-Nov-2001 ACCESSIONS S31087 REFERENCE S31085 !$#authors Smith, R.D.; Walker, J.C. !$#journal Plant Mol. Biol. (1993) 21:307-316 !$#title Expression of multiple type 1 phosphoprotein phosphatases in !1Arabidopsis thaliana. !$#cross-references MUID:93144705; PMID:7678768 !$#accession S31087 !'##molecule_type mRNA !'##residues 1-322 ##label SMI !'##cross-references EMBL:M93410; NID:g166798; PIDN:AAA32838.1; !1PID:g166799 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$27-286 #domain phosphoprotein phosphatase homology #label !8PPP\ !$55-123 #domain phosphoesterase core homology #label PEC\ !$61,63,89 #binding_site iron (Asp, His, Asp) #status predicted\ !$89,121,170,245 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$92,122,269 #active_site Asp, His, Tyr #status predicted\ !$93,218 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 322 #molecular-weight 36215 #checksum 4004 SEQUENCE /// ENTRY S46282 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) 1 [similarity] - alfalfa ORGANISM #formal_name Medicago sativa #common_name alfalfa DATE 19-Mar-1997 #sequence_revision 19-Mar-1997 #text_change 09-Nov-2001 ACCESSIONS S46282 REFERENCE S46282 !$#authors Pay, A.; Pirck, M.; Boegre, L.; Hirt, H.; Heberle-Bors, E. !$#journal Mol. Gen. Genet. (1994) 244:176-182 !$#title Isolation and characterization of phosphoprotein phosphatase !11 from alfalfa. !$#cross-references MUID:94329070; PMID:7519721 !$#accession S46282 !'##status preliminary !'##molecule_type mRNA !'##residues 1-321 ##label PAY CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$27-286 #domain phosphoprotein phosphatase homology #label !8PPP\ !$55-123 #domain phosphoesterase core homology #label PEC\ !$61,63,89 #binding_site iron (Asp, His, Asp) #status predicted\ !$89,121,170,245 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$92,122,269 #active_site Asp, His, Tyr #status predicted\ !$93,218 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 321 #molecular-weight 36248 #checksum 1630 SEQUENCE /// ENTRY A99987 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) 1 catalytic chain [similarity] - Guillardia theta nucleomorph ALTERNATE_NAMES protein phosphatase 1, catalytic subunit ORGANISM #formal_name nucleomorph Guillardia theta #note a nucleomorph is the vestigial nucleus of a eukaryotic endosymbiont DATE 10-May-2001 #sequence_revision 10-May-2001 #text_change 09-Nov-2001 ACCESSIONS A99987 REFERENCE A99082 !$#authors Douglas, S.; Zauner, S.; Fraunholz, M.; Beaton, M.; Penny, !1S.; Deng, L.T.; Wu, X.; Reith, M.; Cavalier-Smith, T.; !1Maier, U.G. !$#journal Nature (2001) 410:1091-1096 !$#title The highly reduced genome of an enslaved algal nucleus. !$#cross-references MUID:11323671; PMID:11323671 !$#accession A99987 !'##molecule_type DNA !'##residues 1-304 ##label DOU !'##cross-references GB:AF165818; NID:g13794453; PIDN:AAK39828.1; !1GSPDB:GN00150 GENETICS !$#gene PP1 !$#map_position 1 !$#genome nucleomorph CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS glycogen metabolism; iron; metalloprotein; nucleomorph; !1phosphoric monoester hydrolase; serine/threonine-specific !1phosphatase; zinc FEATURE !$26-285 #domain phosphoprotein phosphatase homology #label !8PPP\ !$54-122 #domain phosphoesterase core homology #label PEC\ !$60,62,88 #binding_site iron (Asp, His, Asp) #status predicted\ !$88,120,169,244 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$91,121,268 #active_site Asp, His, Tyr #status predicted\ !$92,217 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 304 #molecular-weight 35425 #checksum 3930 SEQUENCE /// ENTRY T21322 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) 1 F25B3.4 [similarity] - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 09-Nov-2001 ACCESSIONS T21322 REFERENCE Z19406 !$#authors Gardner, A. !$#submission submitted to the EMBL Data Library, April 1996 !$#accession T21322 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-291 ##label WIL !'##cross-references EMBL:Z70752; PIDN:CAA94756.1; GSPDB:GN00023; !1CESP:F25B3.4 !'##experimental_source clone F25B3 GENETICS !$#gene CESP:F25B3.4 !$#map_position 5 !$#introns 20/2; 157/3; 273/3 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$7-268 #domain phosphoprotein phosphatase homology #label !8PPP\ !$35-103 #domain phosphoesterase core homology #label PEC\ !$41,43,69 #binding_site iron (Asp, His, Asp) #status predicted\ !$69,101,151,227 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$72,102,251 #active_site Asp, His, Tyr #status predicted\ !$73,200 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 291 #molecular-weight 33700 #checksum 3900 SEQUENCE /// ENTRY T25993 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) 1 ZK354.9 [similarity] - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 09-Nov-2001 ACCESSIONS T25993 REFERENCE Z20120 !$#authors Johnson, D.; Wamsley, P.; Bradshaw, H. !$#submission submitted to the EMBL Data Library, February 1997 !$#description The sequence of C. elegans cosmid ZK354. !$#accession T25993 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-310 ##label JOH !'##cross-references EMBL:U88172; PIDN:AAB42261.1; GSPDB:GN00022; !1CESP:ZK354.9 !'##experimental_source strain Bristol N2; clone ZK354 GENETICS !$#gene CESP:ZK354.9 !$#map_position 4 !$#introns 27/2 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$15-291 #domain phosphoprotein phosphatase homology #label !8PPP\ !$42-110 #domain phosphoesterase core homology #label PEC\ !$48,50,76 #binding_site iron (Asp, His, Asp) #status predicted\ !$76,108,158,250 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$79,109,274 #active_site Asp, His, Tyr #status predicted\ !$80,223 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 310 #molecular-weight 35864 #checksum 5118 SEQUENCE /// ENTRY E69477 #type complete TITLE probable phosphoprotein phosphatase (EC 3.1.3.16) - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 05-Dec-1997 #sequence_revision 05-Dec-1997 #text_change 03-Mar-2000 ACCESSIONS E69477 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession E69477 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-268 ##label KLE !'##cross-references GB:AE000977; GB:AE000782; NID:g2689300; !1PIDN:AAB89430.1; PID:g2648726; TIGR:AF1822 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$1-258 #domain phosphoprotein phosphatase homology #label !8PPP\ !$32,34,56 #binding_site iron (Asp, His, Asp) #status predicted\ !$56,86,137,212 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$59,87,236 #active_site Asp, His, Tyr #status predicted\ !$60,185 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 268 #molecular-weight 30695 #checksum 1858 SEQUENCE /// ENTRY T31469 #type complete TITLE probable phosphoprotein phosphatase (EC 3.1.3.16) R08A2.2 [similarity] - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 29-Oct-1999 #sequence_revision 29-Oct-1999 #text_change 22-Oct-2001 ACCESSIONS T31469 REFERENCE Z21037 !$#authors Williams, L. !$#submission submitted to the EMBL Data Library, October 1999 !$#accession T31469 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-386 ##label WIL !'##cross-references EMBL:Z98853; PIDN:CAB57902.1; CESP:R08A2.2 !'##experimental_source clone R08A2 GENETICS !$#gene CESP:R08A2.2 !$#introns 47/3; 159/3; 306/3; 353/1 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$36-314 #domain phosphoprotein phosphatase homology #label !8PPP\ !$64-132 #domain phosphoesterase core homology #label PEC\ !$70,72,98 #binding_site iron (Asp, His, Asp) #status predicted\ !$98,130,179,273 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$101,131,297 #active_site Asp, His, Tyr #status predicted\ !$102,246 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 386 #molecular-weight 43942 #checksum 2193 SEQUENCE /// ENTRY T27607 #type complete TITLE phosphoprotein phosphatase-related protein ZC477.2 [similarity] - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 11-Jan-2002 ACCESSIONS T27607 REFERENCE Z20392 !$#authors Du, Z. !$#submission submitted to the EMBL Data Library, November 1995 !$#description The sequence of C. elegans cosmid ZC477. !$#accession T27607 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-352 ##label DUZ !'##cross-references EMBL:U40802; PIDN:AAA81508.1; CESP:ZC477.2 GENETICS !$#gene CESP:ZC477.2 !$#introns 27/3; 101/2; 126/3; 151/3; 205/3; 238/2; 276/3; 303/3 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology FEATURE !$30-315 #domain phosphoprotein phosphatase homology #label !8PPP\ !$58-141 #domain phosphoesterase core homology #label PEC SUMMARY #length 352 #molecular-weight 40102 #checksum 8082 SEQUENCE /// ENTRY T19423 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) C24H11.2 [similarity] - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 09-Nov-2001 ACCESSIONS T19423 REFERENCE Z19123 !$#authors Lloyd, C. !$#submission submitted to the EMBL Data Library, November 1996 !$#accession T19423 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-384 ##label WIL !'##cross-references EMBL:Z81475; PIDN:CAB03908.1; GSPDB:GN00021; !1CESP:C24H11.2 !'##experimental_source clone C24H11 GENETICS !$#gene CESP:C24H11.2 !$#map_position 3 !$#introns 18/3; 62/3; 132/3; 187/2; 259/3; 311/3 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$81-351 #domain phosphoprotein phosphatase homology #label !8PPP\ !$113-181 #domain phosphoesterase core homology #label PEC\ !$119,121,147 #binding_site iron (Asp, His, Asp) #status predicted\ !$147,179,233,310 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$150,180,334 #active_site Asp, His, Tyr #status predicted\ !$151,283 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 384 #molecular-weight 43266 #checksum 281 SEQUENCE /// ENTRY T19427 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) C24H11.1 [similarity] - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 09-Nov-2001 ACCESSIONS T19427 REFERENCE Z19123 !$#authors Lloyd, C. !$#submission submitted to the EMBL Data Library, November 1996 !$#accession T19427 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-384 ##label WIL !'##cross-references EMBL:Z81475; PIDN:CAB03912.1; GSPDB:GN00021; !1CESP:C24H11.1 !'##experimental_source clone C24H11 GENETICS !$#gene CESP:C24H11.1 !$#map_position 3 !$#introns 18/3; 62/3; 132/3; 187/2; 259/3; 311/3 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$81-351 #domain phosphoprotein phosphatase homology #label !8PPP\ !$113-181 #domain phosphoesterase core homology #label PEC\ !$119,121,147 #binding_site iron (Asp, His, Asp) #status predicted\ !$147,179,233,310 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$150,180,334 #active_site Asp, His, Tyr #status predicted\ !$151,283 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 384 #molecular-weight 43256 #checksum 299 SEQUENCE /// ENTRY T32935 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) W03D8.2 [similarity] - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 29-Oct-1999 #sequence_revision 29-Oct-1999 #text_change 09-Nov-2001 ACCESSIONS T32935 REFERENCE Z21249 !$#authors Jones, K.; Graves, T.; Ozersky, P. !$#submission submitted to the EMBL Data Library, January 1998 !$#description The sequence of C. elegans cosmid W03D8. !$#accession T32935 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-364 ##label JON !'##cross-references EMBL:AF043702; PIDN:AAB97589.1; GSPDB:GN00019; !1CESP:W03D8.2 !'##experimental_source strain Bristol N2; clone W03D8 GENETICS !$#gene CESP:W03D8.2 !$#map_position 1 !$#introns 6/3; 210/3; 276/3 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$47-315 #domain phosphoprotein phosphatase homology #label !8PPP\ !$76-144 #domain phosphoesterase core homology #label PEC\ !$82,84,110 #binding_site iron (Asp, His, Asp) #status predicted\ !$110,142,195,271 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$113,143,299 #active_site Asp, His, Tyr #status predicted\ !$114,244 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 364 #molecular-weight 41570 #checksum 8899 SEQUENCE /// ENTRY T29290 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) C34D4.2 [similarity] - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 09-Nov-2001 ACCESSIONS T29290 REFERENCE Z20600 !$#authors Du, Z.; Le, T.T. !$#submission submitted to the EMBL Data Library, May 1996 !$#description The sequence of C. elegans cosmid C34D4. !$#accession T29290 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-345 ##label DUZ !'##cross-references EMBL:U58755; PIDN:AAB00704.1; GSPDB:GN00022; !1CESP:C34D4.2 !'##experimental_source strain Bristol N2; clone C34D4 GENETICS !$#gene CESP:C34D4.2 !$#map_position 4 !$#introns 18/3; 68/3; 319/3 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$44-319 #domain phosphoprotein phosphatase homology #label !8PPP\ !$72-140 #domain phosphoesterase core homology #label PEC\ !$78,80,106 #binding_site iron (Asp, His, Asp) #status predicted\ !$106,138,187,278 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$109,139,302 #active_site Asp, His, Tyr #status predicted\ !$110,251 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 345 #molecular-weight 39282 #checksum 2279 SEQUENCE /// ENTRY T21288 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) F23B12.1 [similarity] - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 09-Nov-2001 ACCESSIONS T21288 REFERENCE Z19402 !$#authors Wild, A. !$#submission submitted to the EMBL Data Library, July 1996 !$#accession T21288 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-401 ##label WIL !'##cross-references EMBL:Z77659; PIDN:CAB01164.1; GSPDB:GN00023; !1CESP:F23B12.1 !'##experimental_source clone F23B12 GENETICS !$#gene CESP:F23B12.1 !$#map_position 5 !$#introns 71/3; 121/3; 153/2; 251/2; 377/2 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$97-356 #domain phosphoprotein phosphatase homology #label !8PPP\ !$125-193 #domain phosphoesterase core homology #label PEC\ !$131,133,159 #binding_site iron (Asp, His, Asp) #status predicted\ !$159,191,240,315 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$162,192,339 #active_site Asp, His, Tyr #status predicted\ !$163,288 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 401 #molecular-weight 46264 #checksum 2568 SEQUENCE /// ENTRY T27314 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) Y69E1A.4 [similarity] - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 09-Nov-2001 ACCESSIONS T27314 REFERENCE Z20342 !$#authors Lennard, N. !$#submission submitted to the EMBL Data Library, November 1998 !$#accession T27314 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-375 ##label WIL !'##cross-references EMBL:AL034365; PIDN:CAA22262.1; CESP:Y69E1A.4 !'##experimental_source clone Y69E1A GENETICS !$#gene CESP:Y69E1A.4 !$#introns 98/3; 203/2; 271/3 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$36-349 #domain phosphoprotein phosphatase homology #label !8PPP\ !$64-186 #domain phosphoesterase core homology #label PEC\ !$70,72,152 #binding_site iron (Asp, His, Asp) #status predicted\ !$152,184,233,308 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$155,233,315 #active_site Asp, His, Tyr #status predicted\ !$156,281 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 375 #molecular-weight 43031 #checksum 8824 SEQUENCE /// ENTRY T25259 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) T25B9.2 [similarity] - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 09-Nov-2001 ACCESSIONS T25259 REFERENCE Z20006 !$#authors Matthews, P. !$#submission submitted to the EMBL Data Library, March 1996 !$#accession T25259 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-366 ##label WIL !'##cross-references EMBL:Z70311; PIDN:CAA94374.1; GSPDB:GN00022; !1CESP:T25B9.2 !'##experimental_source clone T25B9 GENETICS !$#gene CESP:T25B9.2 !$#map_position 4 !$#introns 66/3; 171/2; 239/3; 333/1 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$4-317 #domain phosphoprotein phosphatase homology #label !8PPP\ !$32-154 #domain phosphoesterase core homology #label PEC\ !$38,40,120 #binding_site iron (Asp, His, Asp) #status predicted\ !$120,152,201,276 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$123,201,283 #active_site Asp, His, Tyr #status predicted\ !$124,249 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 366 #molecular-weight 41900 #checksum 3028 SEQUENCE /// ENTRY T26790 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) Y40H4A.2 [similarity] - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 09-Nov-2001 ACCESSIONS T26790 REFERENCE Z20267 !$#authors McMurray, A. !$#submission submitted to the EMBL Data Library, December 1998 !$#accession T26790 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-324 ##label WIL !'##cross-references EMBL:AL034391; PIDN:CAA22302.1; CESP:Y40H4A.2 !'##experimental_source clone Y40H4A GENETICS !$#gene CESP:Y40H4A.2 !$#introns 99/2; 212/3; 228/3; 269/3; 307/3 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$48-308 #domain phosphoprotein phosphatase homology #label !8PPP\ !$79-147 #domain phosphoesterase core homology #label PEC\ !$85,87,113 #binding_site iron (Asp, His, Asp) #status predicted\ !$113,145,197,264 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$116,146,292 #active_site Asp, His, Tyr #status predicted\ !$117,237 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 324 #molecular-weight 36736 #checksum 4454 SEQUENCE /// ENTRY T22434 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) F49E11.7 [similarity] - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 09-Nov-2001 ACCESSIONS T22434 REFERENCE Z19564 !$#authors Baynes, C. !$#submission submitted to the EMBL Data Library, March 1996 !$#accession T22434 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-384 ##label WIL !'##cross-references EMBL:Z70308; PIDN:CAA94346.1; GSPDB:GN00022; !1CESP:F49E11.7 !'##experimental_source clone F49E11 GENETICS !$#gene CESP:F49E11.7 !$#map_position 4 !$#introns 28/3; 98/2; 123/3; 204/3; 237/2; 275/3; 303/3 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$31-315 #domain phosphoprotein phosphatase homology #label !8PPP\ !$59-138 #domain phosphoesterase core homology #label PEC\ !$65,67,104 #binding_site iron (Asp, His, Asp) #status predicted\ !$104,136,189,274 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$107,137,298 #active_site Asp, His, Tyr #status predicted\ !$108,247 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 384 #molecular-weight 43315 #checksum 6379 SEQUENCE /// ENTRY T22930 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) F58G1.3 [similarity] - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 09-Nov-2001 ACCESSIONS T22930 REFERENCE Z19639 !$#authors Smye, R. !$#submission submitted to the EMBL Data Library, November 1996 !$#accession T22930 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-341 ##label WIL !'##cross-references EMBL:Z81556; PIDN:CAB04521.1; GSPDB:GN00020; !1CESP:F58G1.3 !'##experimental_source clone F58G1 GENETICS !$#gene CESP:F58G1.3 !$#map_position 2 !$#introns 15/1; 46/1; 228/1; 296/3 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$59-295 #domain phosphoprotein phosphatase homology #label !8PPP\ !$87-155 #domain phosphoesterase core homology #label PEC\ !$93,95,121 #binding_site iron (Asp, His, Asp) #status predicted\ !$121,153,202,254 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$124,154,278 #active_site Asp, His, Tyr #status predicted\ !$125,227 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 341 #molecular-weight 38524 #checksum 5541 SEQUENCE /// ENTRY T18972 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) C06A1.3 [similarity] - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 09-Nov-2001 ACCESSIONS T18972 REFERENCE Z19054 !$#authors McMurray, A. !$#submission submitted to the EMBL Data Library, June 1995 !$#accession T18972 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-364 ##label WIL !'##cross-references EMBL:Z49886; PIDN:CAA90052.1; GSPDB:GN00020; !1CESP:C06A1.3 !'##experimental_source clone C06A1 GENETICS !$#gene CESP:C06A1.3 !$#map_position 2 !$#introns 15/1; 46/1; 251/1; 319/3 CLASSIFICATION #superfamily phosphoprotein phosphatase; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$59-318 #domain phosphoprotein phosphatase homology #label !8PPP\ !$87-155 #domain phosphoesterase core homology #label PEC\ !$93,95,121 #binding_site iron (Asp, His, Asp) #status predicted\ !$121,153,202,277 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$124,154,301 #active_site Asp, His, Tyr #status predicted\ !$125,250 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 364 #molecular-weight 41207 #checksum 9476 SEQUENCE /// ENTRY S52570 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) 5 [validated] - human ALTERNATE_NAMES serine/threonine phosphatase PP5 ORGANISM #formal_name Homo sapiens #common_name man DATE 03-Aug-2001 #sequence_revision 03-Aug-2001 #text_change 03-Aug-2001 ACCESSIONS S52570; PC4136 REFERENCE S52570 !$#authors Chen, M.X.; McPartlin, A.E.; Brown, L.; Chen, Y.H.; Barker, !1H.M.; Cohen, P.T.W. !$#journal EMBO J. (1994) 13:4278-4290 !$#title A novel human protein serine/threonine phosphatase, which !1possesses four tetratricopeptide repeat motifs and localizes !1to the nucleus. !$#cross-references MUID:95009929; PMID:7925273 !$#accession S52570 !'##molecule_type mRNA !'##residues 7-498 ##label CH2 !'##cross-references EMBL:S73586; EMBL:X89416 !'##experimental_source teratocarcinoma cell line NTERA-2 REFERENCE PC4136 !$#authors Xu, X.L.; Lagercrantz, J.; Zickert, P.; !1Bajalica-Lagercrantz, S.; Zetterberg, A. !$#journal Biochem. Biophys. Res. Commun. (1996) 218:514-517 !$#title Chromosomal localization and 5' sequence of the human !1protein serine/threonine phosphatase 5' gene. !$#cross-references MUID:96144708; PMID:8561788 !$#accession PC4136 !'##molecule_type mRNA !'##residues 1-37 ##label XUX !'##cross-references EMBL:X92121; NID:g1177477; PIDN:CAA63089.1; !1PID:e205526; PID:g1177478 !'##experimental_source fetal brain COMMENT mRNA encoding this protein was detected in all human tissues !1tested and was located predominantly in the nucleus. GENETICS !$#gene GDB:PPP5C; PPP5; PP5 !'##cross-references GDB:136857 !$#map_position 19q13.3-19q13.3 FUNCTION !$#description catalyzes the hydrolytic dephosphorylation of !1protein-phosphoserine [validated, MUID:95009929] !$#note may play a role in the regulation of RNA synthesis and !1mitosis CLASSIFICATION #superfamily human phosphoprotein phosphatase 5; !1phosphoesterase core homology; phosphoprotein phosphatase !1homology; tetratricopeptide repeat homology KEYWORDS iron; metalloprotein; nucleus; phosphoric monoester !1hydrolase; zinc FEATURE !$28-61 #domain tetratricopeptide repeat homology #label TT1\ !$62-95 #domain tetratricopeptide repeat homology #label TT2\ !$96-129 #domain tetratricopeptide repeat homology #label TT3\ !$204-467 #domain phosphoprotein phosphatase homology #label !8PPP\ !$236-305 #domain phosphoesterase core homology #label PEC\ !$242,244,271 #binding_site iron (Asp, His, Asp) #status predicted\ !$271,303,352,426 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$274,304,450 #active_site Asp, His, Tyr #status predicted\ !$275,399 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 498 #molecular-weight 56820 #checksum 5353 SEQUENCE /// ENTRY A55346 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) PPT - rat ALTERNATE_NAMES serine/threonine phosphatase PP5 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 03-Aug-2001 #sequence_revision 03-Aug-2001 #text_change 03-Aug-2001 ACCESSIONS A55346 REFERENCE A55346 !$#authors Becker, W.; Kentrup, H.; Klumpp, S.; Schultz, J.E.; Joost, !1H.G. !$#journal J. Biol. Chem. (1994) 269:22586-22592 !$#title Molecular cloning of a protein serine/threonine phosphatase !1containing a putative regulatory tetratricopeptide repeat !1domain. !$#cross-references MUID:94357899; PMID:8077208 !$#accession A55346 !'##molecule_type mRNA !'##residues 1-499 ##label BEC !'##cross-references GB:X77237 !'##note authors translated the codon AAG for residue 53 as Gln, and GTA !1for residue 496 as Leu CLASSIFICATION #superfamily human phosphoprotein phosphatase 5; !1phosphoesterase core homology; phosphoprotein phosphatase !1homology; tetratricopeptide repeat homology KEYWORDS iron; metalloprotein; nucleus; phosphoric monoester !1hydrolase; zinc FEATURE !$28-61 #domain tetratricopeptide repeat homology #label TT1\ !$62-95 #domain tetratricopeptide repeat homology #label TT2\ !$96-129 #domain tetratricopeptide repeat homology #label TT3\ !$204-468 #domain phosphoprotein phosphatase homology #label !8PPP\ !$236-305 #domain phosphoesterase core homology #label PEC\ !$242,244,271 #binding_site iron (Asp, His, Asp) #status predicted\ !$271,303,352,427 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$274,304,451 #active_site Asp, His, Tyr #status predicted\ !$275,400 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 499 #molecular-weight 56902 #checksum 8503 SEQUENCE /// ENTRY T45058 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) Y39B6B.ff [similarity] - Caenorhabditis elegans ALTERNATE_NAMES serine/threonine phosphatase PP5 homolog ORGANISM #formal_name Caenorhabditis elegans DATE 03-Aug-2001 #sequence_revision 03-Aug-2001 #text_change 03-Aug-2001 ACCESSIONS T45058 REFERENCE S43531 !$#authors Wilson, R.; Ainscough, R.; Anderson, K.; Baynes, C.; Berks, !1M.; Bonfield, J.; Burton, J.; Connell, M.; Copsey, T.; !1Cooper, J.; Coulson, A.; Craxton, M.; Dear, S.; Du, Z.; !1Durbin, R.; Favello, A.; Fraser, A.; Fulton, L.; Gardner, !1A.; Green, P.; Hawkins, T.; Hillier, L.; Jier, M.; Johnston, !1L.; Jones, M.; Kershaw, J.; Kirsten, J.; Laisster, N.; !1Latreille, P.; Lightning, J.; Lloyd, C.; Mortimore, B.; !1O'Callaghan, M.; Parsons, J.; Percy, C.; Rifken, L.; Roopra, !1A.; Saunders, D.; Shownkeen, R.; Sims, M.; Smaldon, N.; !1Smith, A.; Smith, M.; Sonnhammer, E.; Staden, R.; Sulston, !1J.; Thierry-Mieg, J.; Thomas, K.; Vaudin, M.; Vaughan, K.; !1Waterston, R.; Watson, A.; Weinstock, L.; Wilkinson-Sproat, !1J.; Wohldman, P. !$#journal Nature (1994) 368:32-38 !$#title 2.2 Mb of contiguous nucleotide sequence from chromosome III !1of C. elegans. !$#cross-references MUID:94150718; PMID:7906398 !$#accession T45058 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-526 ##label WIL !'##cross-references EMBL:AL132896; NID:g6434440; PIDN:CAB60937.1; !1PID:g6434472 !'##experimental_source clone Y39B6B GENETICS !$#map_position 3 !$#introns 42/1; 124/3; 184/3; 265/3; 348/3; 385/2; 415/2; 499/3 !$#note Y39B6B.ff CLASSIFICATION #superfamily human phosphoprotein phosphatase 5; !1phosphoesterase core homology; phosphoprotein phosphatase !1homology; tetratricopeptide repeat homology KEYWORDS iron; metalloprotein; nucleus; phosphoric monoester !1hydrolase; zinc FEATURE !$29-61 #domain tetratricopeptide repeat homology #label TT1\ !$62-95 #domain tetratricopeptide repeat homology #label TT2\ !$96-129 #domain tetratricopeptide repeat homology #label TT3\ !$203-497 #domain phosphoprotein phosphatase homology #label !8PPP\ !$235-304 #domain phosphoesterase core homology #label PEC\ !$241,243,270 #binding_site iron (Asp, His, Asp) #status predicted\ !$270,302,351,456 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$273,303,480 #active_site Asp, His, Tyr #status predicted\ !$274,429 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 526 #molecular-weight 59935 #checksum 4698 SEQUENCE /// ENTRY T46576 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) ppt-1 [similarity] - Neurospora crassa ALTERNATE_NAMES serine/threonine phosphatase PP5 homolog ORGANISM #formal_name Neurospora crassa DATE 03-Aug-2001 #sequence_revision 03-Aug-2001 #text_change 03-Aug-2001 ACCESSIONS T46576 REFERENCE Z23089 !$#authors Yatzkan, E.; Yarden, O. !$#submission submitted to the EMBL Data Library, February 1997 !$#description Ppt-1, a N. crassa novel-type phosphatase. !$#accession T46576 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-479 ##label YAT !'##cross-references EMBL:U89985; PIDN:AAB65138.1 GENETICS !$#gene ppt-1 !$#map_position V CLASSIFICATION #superfamily human phosphoprotein phosphatase 5; !1phosphoesterase core homology; phosphoprotein phosphatase !1homology; tetratricopeptide repeat homology KEYWORDS iron; metalloprotein; nucleus; phosphoric monoester !1hydrolase; zinc FEATURE !$8-41 #domain tetratricopeptide repeat homology #label TT1\ !$42-75 #domain tetratricopeptide repeat homology #label TT2\ !$76-109 #domain tetratricopeptide repeat homology #label TT3\ !$183-448 #domain phosphoprotein phosphatase homology #label !8PPP\ !$215-284 #domain phosphoesterase core homology #label PEC\ !$221,223,250 #binding_site iron (Asp, His, Asp) #status predicted\ !$250,282,331,408 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$253,283,432 #active_site Asp, His, Tyr #status predicted\ !$254,381 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 479 #molecular-weight 54666 #checksum 9200 SEQUENCE /// ENTRY T40391 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) SPBC3F6.01c [similarity] - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES serine/threonine phosphatase PP5 homolog ORGANISM #formal_name Schizosaccharomyces pombe DATE 03-Aug-2001 #sequence_revision 03-Aug-2001 #text_change 03-Aug-2001 ACCESSIONS T40391 REFERENCE Z21925 !$#authors Lyne, M.; Rajandream, M.A.; Barrell, B.G.; Churcher, C.M. !$#submission submitted to the EMBL Data Library, February 1998 !$#accession T40391 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-473 ##label LYN !'##cross-references EMBL:AL022019; PIDN:CAA17690.2; GSPDB:GN00067; !1SPDB:SPBC3F6.01c !'##experimental_source strain 972h-; cosmid c3F6 GENETICS !$#gene SPDB:SPBC3F6.01c !$#map_position 2 CLASSIFICATION #superfamily human phosphoprotein phosphatase 5; !1phosphoesterase core homology; phosphoprotein phosphatase !1homology; tetratricopeptide repeat homology KEYWORDS iron; metalloprotein; nucleus; phosphoric monoester !1hydrolase; zinc FEATURE !$5-38 #domain tetratricopeptide repeat homology #label TT1\ !$39-72 #domain tetratricopeptide repeat homology #label TT2\ !$73-106 #domain tetratricopeptide repeat homology #label TT3\ !$179-444 #domain phosphoprotein phosphatase homology #label !8PPP\ !$211-280 #domain phosphoesterase core homology #label PEC\ !$217,219,246 #binding_site iron (Asp, His, Asp) #status predicted\ !$246,278,327,404 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$249,279,428 #active_site Asp, His, Tyr #status predicted\ !$250,377 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 473 #molecular-weight 53290 #checksum 8941 SEQUENCE /// ENTRY S52571 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) PPT1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein G6347; protein YGR123c; serine/threonine phosphatase PP5 homolog; serine/threonine phosphatase PPT1 ORGANISM #formal_name Saccharomyces cerevisiae DATE 03-Aug-2001 #sequence_revision 03-Aug-2001 #text_change 03-Aug-2001 ACCESSIONS S52571; S55981; S64432; S64697 REFERENCE S52570 !$#authors Chen, M.X.; McPartlin, A.E.; Brown, L.; Chen, Y.H.; Barker, !1H.M.; Cohen, P.T.W. !$#journal EMBO J. (1994) 13:4278-4290 !$#title A novel human protein serine/threonine phosphatase, which !1possesses four tetratricopeptide repeat motifs and localizes !1to the nucleus. !$#cross-references MUID:95009929; PMID:7925273 !$#accession S52571 !'##molecule_type mRNA !'##residues 1-513 ##label CHE REFERENCE S55976 !$#authors van Dyck, L.; Goffeau, A. !$#submission submitted to the EMBL Data Library, December 1994 !$#description Genes for an asn synthase, a GLFG-motif nucleoporin and a !1putative homeobox-domain protein are identified on a 18.3 kb !1segment of the yeast chromosome VII also carrying MEP1, !1PPT1, tree new ORFs, remnants of Ty and three tRNA genes. !$#accession S55981 !'##molecule_type DNA !'##residues 1-513 ##label VAN !'##cross-references EMBL:X83099; NID:g642340; PID:g642346 REFERENCE S64428 !$#authors Van Dyck, L.; Skala, J.; de Wergifosse, P.; Purnelle, B.; !1Talla, E.; Nawrocki, A.; Del Bino, S.; Goffeau, A. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64432 !'##molecule_type DNA !'##residues 1-513 ##label VAW !'##cross-references EMBL:Z72908; NID:g1323200; PID:e243462; !1PID:g1323201; MIPS:YGR123c !'##experimental_source strain S288C REFERENCE S64697 !$#authors Chen, M.X.; McPartlin, A.E.; Brown, L.; Chen, Y.H.; Barker, !1H.M.; Cohen, P.T.W. !$#submission submitted to the EMBL Data Library, July 1995 !$#description A novel human protein serine/threonine phosphatase, which !1possesses four tetratricopeptide repeat motifs and localizes !1to the nucleus. !$#accession S64697 !'##molecule_type DNA !'##residues 1-380,'HHLE',389,'AP',392-393,'NFYGRTHKKPTGWVL',409,'SVV' !1##label CHW !'##cross-references EMBL:X89417; NID:g897805; PID:g897806 GENETICS !$#gene SGD:PPT1 !'##cross-references SGD:S0003355; MIPS:YGR123c !$#map_position 7R CLASSIFICATION #superfamily human phosphoprotein phosphatase 5; !1phosphoesterase core homology; phosphoprotein phosphatase !1homology; tetratricopeptide repeat homology KEYWORDS iron; metalloprotein; nucleus; phosphoric monoester !1hydrolase; zinc FEATURE !$12-45 #domain tetratricopeptide repeat homology #label TT1\ !$46-79 #domain tetratricopeptide repeat homology #label TT2\ !$80-113 #domain tetratricopeptide repeat homology #label TT3\ !$209-475 #domain phosphoprotein phosphatase homology #label !8PPP\ !$243-312 #domain phosphoesterase core homology #label PEC\ !$249,251,278 #binding_site iron (Asp, His, Asp) #status predicted\ !$278,310,359,434 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$281,311,458 #active_site Asp, His, Tyr #status predicted\ !$282,407 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 513 #molecular-weight 57994 #checksum 7788 SEQUENCE /// ENTRY PABY12 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) PPZ1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YM9571.02c; protein YML016c ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1992 #sequence_revision 17-Nov-1995 #text_change 03-Mar-2000 ACCESSIONS S55103; S31265; S35673; S16812; S11060 REFERENCE S55102 !$#authors Gentles, S.; Bowman, S. !$#submission submitted to the EMBL Data Library, June 1995 !$#accession S55103 !'##molecule_type DNA !'##residues 1-692 ##label GEN !'##cross-references EMBL:Z49810; NID:g854472; PIDN:CAA89936.1; !1PID:g854474; GSPDB:GN00013; MIPS:YML016c !'##experimental_source strain AB972 REFERENCE S31265 !$#authors Posas, F.; Casamayor, A.; Morral, N.; Arino, J. !$#journal J. Biol. Chem. (1992) 267:11734-11740 !$#title Molecular cloning and analysis of a yeast protein !1phosphatase with an unusual amino-terminal region. !$#cross-references MUID:92291038; PMID:1318299 !$#accession S31265 !'##molecule_type DNA !'##residues 1-339,'G',341-692 ##label POS !'##cross-references EMBL:M86242; NID:g172232; PIDN:AAA34898.1; !1PID:g172233 REFERENCE S35673 !$#authors Hughes, V.; Mueller, A.; Stark, M.J.R.; Cohen, P.T.W. !$#journal Eur. J. Biochem. (1993) 216:269-279 !$#title Both isoforms of protein phosphatase Z are essential for the !1maintenance of cell size and integrity in Saccharomyces !1cerevisiae in response to osmotic stress. !$#cross-references MUID:93373936; PMID:8396031 !$#accession S35673 !'##molecule_type DNA !'##residues 1-692 ##label HUG !'##cross-references EMBL:X74135; NID:g403319; PIDN:CAA52232.1; !1PID:g403320 REFERENCE S16812 !$#authors da Cruz e Silva, E.F.; Hughes, V.; McDonald, P.; Stark, !1M.J.R.; Cohen, P.T.W. !$#journal Biochim. Biophys. Acta (1991) 1089:269-272 !$#title Protein phosphatase 2B(w) and protein phosphatase Z are !1Saccharomyces cerevisiae enzymes. !$#cross-references MUID:91274364; PMID:1647215 !$#accession S16812 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 389-610 ##label CRU REFERENCE S11059 !$#authors Cohen, P.T.W.; Brewis, N.D.; Hughes, V.; Mann, D.J. !$#journal FEBS Lett. (1990) 268:355-359 !$#title Protein serine/threonine phosphatases; an expanding family. !$#cross-references MUID:90346193; PMID:2166691 !$#accession S11060 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 345-439,'A',441-648,'K',650-692 ##label COH !'##note sequence revised in reference S16812 !'##note species identification revised in reference S16812 GENETICS !$#gene SGD:PPZ1; MIPS:YML016c !'##cross-references SGD:S0004478; MIPS:YML016c !$#map_position 13L CLASSIFICATION #superfamily phosphoprotein phosphatase PPZ1; !1phosphoesterase core homology; phosphoprotein phosphatase !1homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; transmembrane !1protein; zinc FEATURE !$385-644 #domain phosphoprotein phosphatase homology #label !8PPP\ !$413-481 #domain phosphoesterase core homology #label PEC\ !$511-527 #domain transmembrane #status predicted #label TMM\ !$419,421,447 #binding_site iron (Asp, His, Asp) #status predicted\ !$447,479,528,603 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$450,480,627 #active_site Asp, His, Tyr #status predicted\ !$451,576 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 692 #molecular-weight 77490 #checksum 8846 SEQUENCE /// ENTRY T15581 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) C23G10.1 [similarity] - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 20-Sep-1999 #sequence_revision 20-Sep-1999 #text_change 22-Oct-2001 ACCESSIONS T15581 REFERENCE Z18372 !$#authors Latreille, P. !$#submission submitted to the EMBL Data Library, November 1995 !$#description The sequence of C. elegans cosmid C23G10. !$#accession T15581 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-455 ##label LAT !'##cross-references EMBL:U39851; NID:g1055062; PID:g1055072; !1PIDN:AAA81073.1; CESP:C23G10.1 GENETICS !$#gene CESP:C23G10.1 !$#introns 114/3; 138/1; 167/1; 207/3; 285/3; 323/2; 399/3 CLASSIFICATION #superfamily Caenorhabditis elegans phosphoprotein !1phosphatase C23G10.1; phosphoesterase core homology; !1phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$157-424 #domain phosphoprotein phosphatase homology #label !8PPP\ !$185-255 #domain phosphoesterase core homology #label PEC\ !$191,193,221 #binding_site iron (Asp, His, Asp) #status predicted\ !$221,253,305,379 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$224,254,407 #active_site Asp, His, Tyr #status predicted\ !$225,352 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 455 #molecular-weight 51837 #checksum 656 SEQUENCE /// ENTRY S39533 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) PPQ1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein P2247; protein phosphatase Q; protein YPL179w; SAL6 protein ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S39533; S50229; S65191 REFERENCE S39533 !$#authors Chen, M.X.; Chen, Y.H.; Cohen, P.T.W. !$#journal Eur. J. Biochem. (1993) 218:689-699 !$#title PPQ, a novel protein phosphatase containing a Ser + Asn-rich !1amino-terminal domain, is involved in the regulation of !1protein synthesis. !$#cross-references MUID:94094864; PMID:8269960 !$#accession S39533 !'##molecule_type DNA !'##residues 1-549 ##label CHE !'##cross-references EMBL:X75485; NID:g435536; PIDN:CAA53214.1; !1PID:g435537 REFERENCE S50229 !$#authors Vincent, A.; Newnam, G.; Liebman, S.W. !$#journal Genetics (1994) 138:597-607 !$#title The yeast translational allosuppressor, SAL6: a new member !1of the PP1-like phosphatase family with a long serine-rich !1N-terminal extension. !$#cross-references MUID:95154688; PMID:7851758 !$#accession S50229 !'##molecule_type DNA !'##residues 1-549 ##label VIN !'##cross-references EMBL:U00795; NID:g397974; PIDN:AAC48924.1; !1PID:g397975 REFERENCE S65183 !$#authors Benes, V.; Rechmann, S.; Nentwich, U.; Voss, H.; Ansorge, W. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S65191 !'##molecule_type DNA !'##residues 1-549 ##label BEN !'##cross-references EMBL:Z73535; NID:g1370376; PIDN:CAA97886.1; !1PID:g1370377; GSPDB:GN00016; MIPS:YPL179w !'##experimental_source strain S288C (AB972) GENETICS !$#gene SGD:PPQ1; SAL6; MIPS:YPL179w !'##cross-references SGD:S0006100; MIPS:YPL179w !$#map_position 16L CLASSIFICATION #superfamily phosphoprotein phosphatase PPQ1; !1phosphoesterase core homology; phosphoprotein phosphatase !1homology KEYWORDS phosphoric monoester hydrolase FEATURE !$267-526 #domain phosphoprotein phosphatase homology #label !8PPP\ !$295-363 #domain phosphoesterase core homology #label PEC SUMMARY #length 549 #molecular-weight 61420 #checksum 9729 SEQUENCE /// ENTRY T32635 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) F42G8.8 [similarity] - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 29-Oct-1999 #sequence_revision 29-Oct-1999 #text_change 02-Nov-2001 ACCESSIONS T32635 REFERENCE Z21203 !$#authors Gattung, S.; Holmes, A. !$#submission submitted to the EMBL Data Library, December 1997 !$#description The sequence of C. elegans cosmid F42G8. !$#accession T32635 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-487 ##label GAT !'##cross-references EMBL:AF038618; PIDN:AAB92072.1; GSPDB:GN00022; !1CESP:F42G8.8 !'##experimental_source strain Bristol N2; clone F42G8 COMMENT This sequence shares a domain (approximately residues !1378-487) with mammalian selenium-binding proteins. GENETICS !$#gene CESP:F42G8.8 !$#map_position 4 !$#introns 27/3; 97/2; 122/3; 203/3; 236/2; 274/3; 302/3; 377/1 CLASSIFICATION #superfamily Caenorhabditis elegans phosphoprotein !1phosphatase F42G8.8; phosphoesterase core homology; !1phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; zinc FEATURE !$30-314 #domain phosphoprotein phosphatase homology #label !8PPP\ !$58-137 #domain phosphoesterase core homology #label PEC\ !$64,66,103 #binding_site iron (Asp, His, Asp) #status predicted\ !$103,135,188,273 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$106,136,297 #active_site Asp, His, Tyr #status predicted\ !$107,246 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 487 #molecular-weight 54922 #checksum 7991 SEQUENCE /// ENTRY S35067 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) 3-alpha catalytic chain [similarity] - human ALTERNATE_NAMES calcineurin alpha chain A; calcineurin catalytic chain; protein phosphatase 2B catalytic chain ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Dec-1993 #sequence_revision 10-Nov-1995 #text_change 19-May-2000 ACCESSIONS S35067; B42232; T48685 REFERENCE S35067 !$#authors Muramatsu, T.; Kincaid, R.L. !$#journal Biochim. Biophys. Acta (1993) 1178:117-120 !$#title Molecular cloning of a full-length cDNA encoding the !1catalytic subunit of human calmodulin-dependent protein !1phosphatase (calcineurin A-alpha). !$#cross-references MUID:93320118; PMID:8392375 !$#accession S35067 !'##molecule_type mRNA !'##residues 1-521 ##label MUR !'##cross-references GB:L14778; NID:g306476; PIDN:AAA02631.1; !1PID:g306477 REFERENCE A42232 !$#authors Kincaid, R.L.; Giri, P.R.; Higuchi, S.; Tamura, J.; Dixon, !1S.C.; Marietta, C.A.; Amorese, D.A.; Martin, B.M. !$#journal J. Biol. Chem. (1990) 265:11312-11319 !$#title Cloning and characterization of molecular isoforms of the !1catalytic subunit of calcineurin using nonisotopic methods. !$#cross-references MUID:90293081; PMID:2162844 !$#accession B42232 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 269-521 ##label KIN !'##cross-references GB:J05480; NID:g179807; PIDN:AAA35634.1; !1PID:g179808 REFERENCE Z24534 !$#authors Ansorge, W.; Wirkner, U.; Mewes, H.W.; Weil, B.; Wiemann, S. !$#submission submitted to the Protein Sequence Database, April 2000 !$#accession T48685 !'##molecule_type mRNA !'##residues 1-521 ##label AAA !'##cross-references EMBL:AL353950 !'##experimental_source adult amygdala; clone DKFZp761L0516 GENETICS !$#gene GDB:PPP3CA; CALN; CNA1; CCN1; CALNA; PPP2B !'##cross-references GDB:118761; OMIM:114105 !$#map_position 4q21-4q244pter-4qter !$#note DKFZp761L0516.1 COMPLEX heterodimer with calcineurin regulatory chain FUNCTION !$#description catalyzes hydrolysis of peptidyl-phosphoserine or !1-phosphothreonine to release phosphate CLASSIFICATION #superfamily calcineurin catalytic chain; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS heterodimer; iron; metalloprotein; phosphoprotein; !1phosphoric monoester hydrolase; serine/threonine-specific !1phosphatase; zinc FEATURE !$56-328 #domain phosphoprotein phosphatase homology #label !8PPP\ !$84-152 #domain phosphoesterase core homology #label PEC\ !$90,92,118 #binding_site iron (Asp, His, Asp) #status predicted\ !$118,150,199,281 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$121,151,311 #active_site Asp, His, Tyr #status predicted\ !$122,254 #binding_site substrate phosphate (Arg) #status !8predicted\ !$411 #binding_site phosphate (Ser) (covalent) (by !8calmodulin-dependent kinase II) #status predicted SUMMARY #length 521 #molecular-weight 58687 #checksum 450 SEQUENCE /// ENTRY A56968 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) 3-alpha catalytic chain [validated] - bovine ALTERNATE_NAMES calcineurin catalytic chain; calcineurin chain A; protein phosphatase 2B catalytic chain ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 25-Aug-1995 #sequence_revision 25-Aug-1995 #text_change 15-Sep-2000 ACCESSIONS A56968; A60256; A33551 REFERENCE A56968 !$#authors Su, K.H.; Su, M. !$#citation unpublished results, cited by Griffith, J.P.; Kim, J.L.; !1Kim, E.E.; Sintchak, M.D.; Thomson, J.A.; Fitzgibbon, M.J.; !1Fleming, M.A.; Caron, P.R.; Hsiao, K.; Navia, M.A. Cell, 82, !1507-522, 1995 !$#accession A56968 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-521 ##label SUA REFERENCE A60256 !$#authors Kincaid, R.L.; Martin, B.M. !$#journal Adv. Exp. Med. Biol. (1989) 255:347-358 !$#title Characterization of the calmodulin-binding domain of !1calcineurin deduced from a complementary DNA clone. !$#cross-references MUID:90144199; PMID:2559598 !$#accession A60256 !'##molecule_type protein !'##residues 244,'N',246-251,'P',253;'XX',309-318;409-419;425-437, !1'X';442-458;467-474;488-500,'R' ##label KIN REFERENCE A33551 !$#authors Martensen, T.M.; Martin, B.M.; Kincaid, R.L. !$#journal Biochemistry (1989) 28:9243-9247 !$#title Identification of the site on calcineurin phosphorylated by !1Ca(2+)/CaM-dependent kinase II: modification of the !1CaM-binding domain. !$#cross-references MUID:90122785; PMID:2558715 !$#accession A33551 !'##molecule_type protein !'##residues 291-299;407-410,'X',412-414 ##label MAR !'##note the residue designated 'X' was determined to be phosphoserine REFERENCE A42232 !$#authors Kincaid, R.L.; Giri, P.R.; Higuchi, S.; Tamura, J.; Dixon, !1S.C.; Marietta, C.A.; Amorese, D.A.; Martin, B.M. !$#journal J. Biol. Chem. (1990) 265:11312-11319 !$#title Cloning and characterization of molecular isoforms of the !1catalytic subunit of calcineurin using nonisotopic methods. !$#cross-references MUID:90293081; PMID:2162844 !$#contents annotation; sequence of peptides compared with human and !1mouse REFERENCE A66708 !$#authors Griffith, J.P.; Kim, J.L.; Kim, E.E.; Sintchak, M.D.; !1Thomson, J.A.; Fitzgibbon, M.J.; Fleming, M.A.; Caron, P.R.; !1Hsiao, K.; Navia, M.A. !$#submission submitted to the Brookhaven Protein Data Bank, August 1996 !$#cross-references PDB:1TCO !$#contents annotation; X-ray crystallography, 2.5 angstroms, residues !121-372 REFERENCE A56967 !$#authors Griffith, J.P.; Kim, J.L.; Kim, E.E.; Sintchak, M.D.; !1Thomson, J.A.; Fitzgibbon, M.J.; Fleming, M.A.; Caron, P.R.; !1Hsiao, K.; Navia, M.A. !$#journal Cell (1995) 82:507-522 !$#title X-ray structure of calcineurin inhibited by the !1immunophilin-immunosuppressant FKBP12-FK506 complex. !$#cross-references MUID:95360994; PMID:7543369 !$#contents annotation; X-ray crystallography, 2.5 angstroms COMPLEX heterodimer with calcineurin regulatory chain (see !1PIR:S34127) FUNCTION !$#description catalyzes hydrolysis of peptidyl-phosphoserine or !1-phosphothreonine to release phosphate CLASSIFICATION #superfamily calcineurin catalytic chain; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS heterodimer; iron; metalloprotein; phosphoprotein; !1phosphoric monoester hydrolase; serine/threonine-specific !1phosphatase; zinc FEATURE !$56-328 #domain phosphoprotein phosphatase homology #label !8PPP\ !$84-152 #domain phosphoesterase core homology #label PEC\ !$90,92,118 #binding_site iron (Asp, His, Asp) #status !8experimental\ !$118,150,199,281 #binding_site zinc (Asp, Asn, His, His) #status !8experimental\ !$121,151,311 #active_site Asp, His, Tyr #status predicted\ !$122,254 #binding_site substrate phosphate (Arg) #status !8experimental\ !$411 #binding_site phosphate (Ser) (covalent) (by !8calmodulin-dependent kinase II) #status experimental SUMMARY #length 521 #molecular-weight 58671 #checksum 9540 SEQUENCE /// ENTRY A36222 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) 3-beta catalytic chain, splice form 1 - human ALTERNATE_NAMES calcineurin catalytic chain; calcineurin chain A alpha; calcineurin chain A type 1; protein phosphatase 2B, catalytic subunit ORGANISM #formal_name Homo sapiens #common_name man DATE 04-Oct-1991 #sequence_revision 13-Jan-1993 #text_change 03-Mar-2000 ACCESSIONS A36222 REFERENCE A36222 !$#authors Guerini, D.; Klee, C.B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:9183-9187 !$#title Cloning of human calcineurin A: evidence for two isozymes !1and identification of a polyproline structural domain. !$#cross-references MUID:90083232; PMID:2556704 !$#accession A36222 !'##molecule_type mRNA !'##residues 1-514 ##label GUE !'##cross-references GB:M29550; NID:g180706; PIDN:AAA35705.1; !1PID:g180707 GENETICS !$#gene GDB:PPP3CB !'##cross-references GDB:131362; OMIM:114106 !$#map_position 10q21-10q22 COMPLEX heterodimer with calcineurin regulatory chain FUNCTION !$#description catalyzes hydrolysis of peptidyl-phosphoserine or !1-phosphothreonine to release phosphate CLASSIFICATION #superfamily calcineurin catalytic chain; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS alternative splicing; heterodimer; iron; metalloprotein; !1phosphoprotein; phosphoric monoester hydrolase; serine/ !1threonine-specific phosphatase; zinc FEATURE !$65-355 #domain phosphoprotein phosphatase homology #label !8PPP\ !$99,101,127 #binding_site iron (Asp, His, Asp) #status predicted\ !$127,177,226,308 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$130,178,338 #active_site Asp, His, Tyr #status predicted\ !$131,281 #binding_site substrate phosphate (Arg) #status !8predicted\ !$438 #binding_site phosphate (Ser) (covalent) (by !8calmodulin-dependent kinase II) #status predicted SUMMARY #length 514 #molecular-weight 58013 #checksum 5980 SEQUENCE /// ENTRY B36222 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) 3-beta catalytic chain, splice form 2 - human ALTERNATE_NAMES calcineurin catalytic chain; calcineurin chain A beta; calcineurin chain A type 2; protein phosphatase 2B isoform beta CONTAINS phosphoprotein phosphatase 3-beta catalytic chain, splice form 3 ORGANISM #formal_name Homo sapiens #common_name man DATE 04-Oct-1991 #sequence_revision 13-Jan-1993 #text_change 03-Mar-2000 ACCESSIONS B36222; S14272 REFERENCE A36222 !$#authors Guerini, D.; Klee, C.B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:9183-9187 !$#title Cloning of human calcineurin A: evidence for two isozymes !1and identification of a polyproline structural domain. !$#cross-references MUID:90083232; PMID:2556704 !$#accession B36222 !'##molecule_type mRNA !'##residues 1-524 ##label GUE !'##cross-references GB:M29551; NID:g180708; PIDN:AAA35706.1; !1PID:g180709 REFERENCE S14272 !$#authors McPartlin, A.E.; Barker, H.M.; Cohen, P.T.W. !$#journal Biochim. Biophys. Acta (1991) 1088:308-310 !$#title Identification of a third alternatively spliced cDNA !1encoding the catalytic subunit of protein phosphatase !12Bbeta. !$#cross-references MUID:91159485; PMID:1848109 !$#accession S14272 !'##molecule_type mRNA !'##residues 1-395,'V',396-456,467-524 ##label MCP GENETICS !$#gene GDB:PPP3CB !'##cross-references GDB:131362; OMIM:114106 !$#map_position 10q21-10q22 COMPLEX heterodimer with calcineurin regulatory chain FUNCTION !$#description catalyzes hydrolysis of peptidyl-phosphoserine or !1-phosphothreonine to release phosphate CLASSIFICATION #superfamily calcineurin catalytic chain; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS alternative splicing; heterodimer; iron; metalloprotein; !1phosphoprotein; phosphoric monoester hydrolase; serine/ !1threonine-specific phosphatase; zinc FEATURE !$1-524 #product protein phosphatase 3-beta catalytic chain !8splice form 2 #status predicted #label SF2\ !$1-456,467-524 #product protein phosphatase 3-beta catalytic chain !8splice form 3 #status predicted #label SF3\ !$65-337 #domain phosphoprotein phosphatase homology #label !8PPP\ !$93-161 #domain phosphoesterase core homology #label PEC\ !$99,101,127 #binding_site iron (Asp, His, Asp) #status predicted\ !$127,159,208,290 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$130,160,320 #active_site Asp, His, Tyr #status predicted\ !$131,263 #binding_site substrate phosphate (Arg) #status !8predicted\ !$420 #binding_site phosphate (Ser) (covalent) (by !8calmodulin-dependent kinase II) #status predicted SUMMARY #length 524 #molecular-weight 59024 #checksum 6481 SEQUENCE /// ENTRY JC1283 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) 3-gamma catalytic chain - human ALTERNATE_NAMES calcineurin catalytic chain; calcineurin chain A; protein phosphatase 2B catalytic chain ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 03-Mar-2000 ACCESSIONS JC1283 REFERENCE JC1283 !$#authors Muramatsu, T.; Kincaid, R.L. !$#journal Biochem. Biophys. Res. Commun. (1992) 188:265-271 !$#title Molecular cloning and chromosomal mapping of the human gene !1for the testis-specific catalytic subunit of !1calmodulin-dependent protein phosphatase (calcineurin A). !$#cross-references MUID:93038669; PMID:1339277 !$#accession JC1283 !'##molecule_type mRNA !'##residues 1-502 ##label MUR !'##cross-references GB:S46622; NID:g258000; PIDN:AAB23769.1; !1PID:g258001 !'##experimental_source testis GENETICS !$#gene GDB:PPP3CC !'##cross-references GDB:136027; OMIM:114107 !$#map_position 8pter-8qter COMPLEX heterodimer with calcineurin regulatory chain FUNCTION !$#description catalyzes hydrolysis of peptidyl-phosphoserine or !1-phosphothreonine to release phosphate !$#note this isoform is testis specific and is associated with sperm !1flagellar motility CLASSIFICATION #superfamily calcineurin catalytic chain; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS heterodimer; iron; metalloprotein; phosphoprotein; !1phosphoric monoester hydrolase; serine/threonine-specific !1phosphatase; testis; zinc FEATURE !$52-324 #domain phosphoprotein phosphatase homology #label !8PPP\ !$80-148 #domain phosphoesterase core homology #label PEC\ !$86,88,114 #binding_site iron (Asp, His, Asp) #status predicted\ !$114,146,195,277 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$117,147,307 #active_site Asp, His, Tyr #status predicted\ !$118,250 #binding_site substrate phosphate (Arg) #status !8predicted\ !$405 #binding_site phosphate (Ser) (covalent) (by !8calmodulin-dependent kinase II) #status predicted SUMMARY #length 502 #molecular-weight 57125 #checksum 8748 SEQUENCE /// ENTRY JC7241 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16), calcineurin catalytic chain [similarity] - scallop (Patinopecten yessoensis) ALTERNATE_NAMES Ca2+/calmodulin-dependent phosphoprotein phosphatase catalytic subunit ORGANISM #formal_name Patinopecten yessoensis #common_name Yesso scallop DATE 09-Jun-2000 #sequence_revision 09-Jun-2000 #text_change 09-Nov-2001 ACCESSIONS JC7241; PC7069 REFERENCE JC7241 !$#authors Uryu, M.; Nakatomi, A.; Watanabe, M.; Hatsuse, R.; Yazawa, !1M. !$#journal J. Biochem. (2000) 127:739-746 !$#title Molecular cloning of cDNA encoding two subunits of !1calcineurin from scallop testis: Demonstration of !1stage-specific expression during maturation of the testis. !$#accession JC7241 !'##molecule_type mRNA !'##residues 1-486 ##label URY !'##cross-references DDBJ:AB041523 !'##experimental_source testis !$#accession PC7069 !'##molecule_type protein !'##residues !143-62;72-92;133-153;165-185;210-230;239-249;289-309;319-339; !1356-373;405-424;441-456 ##label UR2 COMMENT This testis-specific isoform functions during the maturation !1process. It is involved in spermiogenesis and the regulation !1of flagellar motility. GENETICS !$#gene cna FUNCTION !$#description catalyzes hydrolysis of peptidyl-phosphoserine or !1-phosphothreonine to release phosphate CLASSIFICATION #superfamily calcineurin catalytic chain; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS calmodulin binding; flagellar rotation; iron; !1metalloprotein; phosphoprotein; phosphoric monoester !1hydrolase; serine/threonine-specific phosphatase; testis; !1zinc FEATURE !$52-324 #domain phosphoprotein phosphatase homology #label !8PPP\ !$80-148 #domain phosphoesterase core homology #label PEC\ !$86,88,114 #binding_site iron (Asp, His, Asp) #status predicted\ !$114,146,195,277 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$117,147,307 #active_site Asp, His, Tyr #status predicted\ !$118,250 #binding_site substrate phosphate (Arg) #status !8predicted\ !$411 #binding_site phosphate (Thr) (covalent) (by !8calmodulin-dependent kinase II) #status predicted SUMMARY #length 486 #molecular-weight 55006 #checksum 7863 SEQUENCE /// ENTRY S70551 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16), calcineurin catalytic chain CnnA14D, splice form II [similarity] - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 19-Mar-1998 #sequence_revision 17-Apr-1998 #text_change 09-Nov-2001 ACCESSIONS S70551 REFERENCE S70551 !$#authors Hong, C.S.; Ganetzky, B. !$#journal Genetics (1996) 142:879-892 !$#title Molecular characterization of neurally expressing genes in !1the para sodium channel gene cluster of Drosophila. !$#cross-references MUID:97002547; PMID:8849894 !$#accession S70551 !'##status preliminary; nucleic acid sequence not shown; not compared !1with conceptual translation !'##molecule_type mRNA !'##residues 1-569 ##label HON FUNCTION !$#description catalyzes hydrolysis of peptidyl-phosphoserine or !1-phosphothreonine to release phosphate CLASSIFICATION #superfamily calcineurin catalytic chain; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoprotein; phosphoric monoester !1hydrolase; serine/threonine-specific phosphatase; zinc FEATURE !$121-393 #domain phosphoprotein phosphatase homology #label !8PPP\ !$149-217 #domain phosphoesterase core homology #label PEC\ !$155,157,183 #binding_site iron (Asp, His, Asp) #status predicted\ !$183,215,264,346 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$186,216,376 #active_site Asp, His, Tyr #status predicted\ !$187,319 #binding_site substrate phosphate (Arg) #status !8predicted\ !$478 #binding_site phosphate (Ser) (covalent) (by !8calmodulin-dependent kinase II) #status predicted SUMMARY #length 569 #molecular-weight 63044 #checksum 1168 SEQUENCE /// ENTRY S70554 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16), calcineurin catalytic chain CnnA14D, splice form I [similarity] - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 19-Mar-1998 #sequence_revision 17-Apr-1998 #text_change 09-Nov-2001 ACCESSIONS S70554 REFERENCE S70551 !$#authors Hong, C.S.; Ganetzky, B. !$#journal Genetics (1996) 142:879-892 !$#title Molecular characterization of neurally expressing genes in !1the para sodium channel gene cluster of Drosophila. !$#cross-references MUID:97002547; PMID:8849894 !$#accession S70554 !'##status preliminary; nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-578 ##label HON !'##cross-references EMBL:U30493; NID:g1335782; PIDN:AAC47079.1; !1PID:g1335783 FUNCTION !$#description catalyzes hydrolysis of peptidyl-phosphoserine or !1-phosphothreonine to release phosphate CLASSIFICATION #superfamily calcineurin catalytic chain; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoprotein; phosphoric monoester !1hydrolase; serine/threonine-specific phosphatase; zinc FEATURE !$130-402 #domain phosphoprotein phosphatase homology #label !8PPP\ !$158-226 #domain phosphoesterase core homology #label PEC\ !$164,166,192 #binding_site iron (Asp, His, Asp) #status predicted\ !$192,224,273,355 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$195,225,385 #active_site Asp, His, Tyr #status predicted\ !$196,328 #binding_site substrate phosphate (Arg) #status !8predicted\ !$487 #binding_site phosphate (Ser) (covalent) (by !8calmodulin-dependent kinase II) #status predicted SUMMARY #length 578 #molecular-weight 63955 #checksum 7543 SEQUENCE /// ENTRY T18864 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16), calcineurin catalytic chain C02F4.2 [similarity] - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 09-Nov-2001 ACCESSIONS T18864 REFERENCE Z19034 !$#authors Cummings, P. !$#submission submitted to the EMBL Data Library, October 1996 !$#accession T18864 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-535 ##label WIL !'##cross-references EMBL:Z81032; PIDN:CAB02719.1; GSPDB:GN00022; !1CESP:C02F4.2 !'##experimental_source clone C02F4 GENETICS !$#gene CESP:C02F4.2 !$#map_position 4 !$#introns 14/1; 44/1; 77/3; 239/3; 286/2; 312/2; 344/1; 386/1; 412/1; !1440/2; 473/1 FUNCTION !$#description catalyzes hydrolysis of peptidyl-phosphoserine or !1-phosphothreonine to release phosphate CLASSIFICATION #superfamily calcineurin catalytic chain; phosphoesterase !1core homology; phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoprotein; phosphoric monoester !1hydrolase; serine/threonine-specific phosphatase; zinc FEATURE !$81-353 #domain phosphoprotein phosphatase homology #label !8PPP\ !$109-177 #domain phosphoesterase core homology #label PEC\ !$115,117,143 #binding_site iron (Asp, His, Asp) #status predicted\ !$143,175,224,306 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$146,176,336 #active_site Asp, His, Tyr #status predicted\ !$147,279 #binding_site substrate phosphate (Arg) #status !8predicted\ !$437 #binding_site phosphate (Ser) (covalent) (by !8calmodulin-dependent kinase II) #status predicted SUMMARY #length 535 #molecular-weight 60665 #checksum 7308 SEQUENCE /// ENTRY T38946 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) SPAC57A7.08 - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES serine-threonine protein phosphatase pp-z ORGANISM #formal_name Schizosaccharomyces pombe DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 09-Nov-2001 ACCESSIONS T38946 REFERENCE Z21819 !$#authors Skelton, J.; Churcher, C.M.; Barrell, B.G.; Rajandream, !1M.A.; Wood, V. !$#submission submitted to the EMBL Data Library, May 1997 !$#accession T38946 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-515 ##label SKE !'##cross-references EMBL:Z95396; PIDN:CAB08766.1; GSPDB:GN00066; !1SPDB:SPAC57A7.08 !'##experimental_source strain 972h-; cosmid c57A7 GENETICS !$#gene SPDB:SPAC57A7.08 !$#map_position 1 CLASSIFICATION #superfamily Schizosaccharomyces pombe phosphoprotein !1phosphatase SPAC57A7.08; phosphoesterase core homology; !1phosphoprotein phosphatase homology KEYWORDS iron; metalloprotein; phosphoric monoester hydrolase; !1serine/threonine-specific phosphatase; transmembrane !1protein; zinc FEATURE !$214-473 #domain phosphoprotein phosphatase homology #label !8PPP\ !$242-310 #domain phosphoesterase core homology #label PEC\ !$340-356 #domain transmembrane #status predicted #label TMM\ !$248,250,276 #binding_site iron (Asp, His, Asp) #status predicted\ !$276,308,357,432 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$279,309,456 #active_site Asp, His, Tyr #status predicted\ !$280,405 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 515 #molecular-weight 57131 #checksum 4622 SEQUENCE /// ENTRY A42287 #type complete TITLE phosphoprotein phosphatase (EC 3.1.3.16) rdgC - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES retinal degeneration protein C ORGANISM #formal_name Drosophila melanogaster DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 03-Mar-2000 ACCESSIONS A42287; S27811 REFERENCE A42287 !$#authors Steele, F.R.; Washburn, T.; Rieger, R.; O'Tousa, J.E. !$#journal Cell (1992) 69:669-676 !$#title Drosophila retinal degeneration C (rdgC) encodes a novel !1serine/threonine protein phosphatase. !$#cross-references MUID:92266398; PMID:1316807 !$#accession A42287 !'##molecule_type DNA !'##residues 1-661 ##label STE !'##cross-references EMBL:M89628; NID:g158237; PIDN:AAB00734.1; !1PID:g158238 !'##note sequence extracted from NCBI backbone (NCBIN:103017, !1NCBIN:103023, NCBIN:103028, NCBIN:103032, NCBIN:103036, !1NCBIN:103041, NCBIN:103048, NCBIN:103053, NCBIN:103063, !1NCBIN:103071, NCBIN:103095, NCBIN:103104, NCBIP:103001) GENETICS !$#gene rdgC !'##cross-references FlyBase:FBgn0004366 !$#introns 5/1; 47/3; 74/3; 116/3; 172/3; 240/3; 290/3; 312/3; 374/3; !1510/3; 544/1 FUNCTION !$#description catalyzes the hydrolytic dephosphorylation of !1protein-phosphoserine and protein-posphothreonine !$#note prevents light-induced retinal degeneration CLASSIFICATION #superfamily phosphoprotein phosphatase rdgC; calmodulin !1repeat homology; phosphoesterase core homology; !1phosphoprotein phosphatase homology KEYWORDS calcium binding; EF hand; iron; metalloprotein; nucleus; !1phosphoric monoester hydrolase; serine/threonine-specific !1phosphatase; vision; zinc FEATURE !$120-401 #domain phosphoprotein phosphatase homology #label !8PPP\ !$152-221 #domain phosphoesterase core homology #label PEC\ !$526-558 #domain calmodulin repeat homology #label EF1\ !$566-598 #domain calmodulin repeat homology #label EF2\ !$158,160,187 #binding_site iron (Asp, His, Asp) #status predicted\ !$187,219,271,360 #binding_site zinc (Asp, Asn, His, His) #status !8predicted\ !$190,220,384 #active_site Asp, His, Tyr #status predicted\ !$191,333 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 661 #molecular-weight 75510 #checksum 6411 SEQUENCE /// ENTRY PAECGA #type complete TITLE phosphatidylglycerophosphatase (EC 3.1.3.27) A - Escherichia coli ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 11-Jun-1999 ACCESSIONS A30192 REFERENCE A30192 !$#authors Icho, T. !$#journal J. Bacteriol. (1988) 170:5110-5116 !$#title Membrane-bound phosphatases in Escherichia coli: sequence of !1the pgpA gene. !$#cross-references MUID:89033892; PMID:2846510 !$#accession A30192 !'##molecule_type DNA !'##residues 1-168 ##label ICH !'##cross-references GB:M23546; NID:g340942; PIDN:AAA24325.1; !1PID:g387599 COMMENT This inner membrane enzyme, one of the three phospholipid !1phosphatases, specifically hydrolyzes !1phosphatidylglycerophosphate. GENETICS !$#gene pgpA !$#map_position 18 min CLASSIFICATION #superfamily phosphatidylglycerophosphatase A KEYWORDS phosphoric monoester hydrolase SUMMARY #length 168 #molecular-weight 19001 #checksum 4925 SEQUENCE /// ENTRY PAECGB #type complete TITLE phosphatidylglycerophosphatase (EC 3.1.3.27) B - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 01-Mar-2002 ACCESSIONS A30193; A64876 REFERENCE A30193 !$#authors Icho, T. !$#journal J. Bacteriol. (1988) 170:5117-5124 !$#title Membrane-bound phosphatases in Escherichia coli: sequence of !1the pgpB gene and dual subcellular localization of the pgpB !1product. !$#cross-references MUID:89033893; PMID:2846511 !$#accession A30193 !'##molecule_type DNA !'##residues 1-254 ##label ICH !'##cross-references GB:M23628; NID:g340982; PIDN:AAB36618.1; !1PID:g450384 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64876 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-254 ##label BLAT !'##cross-references GB:AE000226; GB:U00096; NID:g2367115; !1PIDN:AAC74360.1; PID:g1787534; UWGP:b1278 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene pgpB FUNCTION !$#description hydrolyzes phosphatidylglycerophosphate, phosphatidic acid, !1and lysophosphatidic acid !$#note the pattern of activities varies according to subcellular !1location CLASSIFICATION #superfamily phosphatidylglycerophosphatase B; !1glucose-6-phosphatase catalytic domain homology KEYWORDS phospholipid biosynthesis; phosphoric monoester hydrolase; !1transmembrane protein FEATURE !$8-24 #domain transmembrane #status predicted #label TM1\ !$52-68 #domain transmembrane #status predicted #label TM2\ !$72-88 #domain transmembrane #status predicted #label TM3\ !$73-222 #domain glucose-6-phosphatase catalytic domain !8homology #label GPH\ !$187-203 #domain transmembrane #status predicted #label TM4\ !$212-228 #domain transmembrane #status predicted #label TM5 SUMMARY #length 254 #molecular-weight 29021 #checksum 5769 SEQUENCE /// ENTRY I64054 #type complete TITLE phosphatidylglycerophosphatase B homolog - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 28-Jan-2000 #sequence_revision 28-Jan-2000 #text_change 03-Mar-2000 ACCESSIONS I64054 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession I64054 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-241 ##label TIGR !'##cross-references GB:U32706; GB:L42023; NID:g1573170; !1PIDN:AAC21879.1; PID:g1573171; TIGR:HI0211 CLASSIFICATION #superfamily phosphatidylglycerophosphatase B; !1glucose-6-phosphatase catalytic domain homology FEATURE !$70-224 #domain glucose-6-phosphatase catalytic domain !8homology #label GPH SUMMARY #length 241 #molecular-weight 27490 #checksum 5005 SEQUENCE /// ENTRY S67800 #type complete TITLE aryl phosphatase (EC 3.1.3.-) PHO13 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES 4-nitrophenylphosphatase (EC 3.1.3.41); protein D0786; protein YDL236w ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S67800; JQ0358 REFERENCE S67798 !$#authors Alt-Moerbe, J.; Schneider, C.; Moro, M. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67800 !'##molecule_type DNA !'##residues 1-312 ##label ALT !'##cross-references EMBL:Z74284; NID:g1431399; PIDN:CAA98816.1; !1PID:g1431400; GSPDB:GN00004; MIPS:YDL236w !'##experimental_source strain S288C REFERENCE JQ0358 !$#authors Kaneko, Y.; Toh-e, A.; Banno, I.; Oshima, Y. !$#journal Mol. Gen. Genet. (1989) 220:133-139 !$#title Molecular characterization of a specific !1p-nitrophenylphosphatase gene, PHO13, and its mapping by !1chromosome fragmentation in Saccharomyces cerevisiae. !$#cross-references MUID:90114099; PMID:2558283 !$#accession JQ0358 !'##molecule_type DNA !'##residues 1-49,'D',51-95,'P',97-283,'T',285-305,'A',307-312 ##label !1KAN !'##cross-references GB:X51611; NID:g4142; PIDN:CAB56540.1; PID:g5924022 COMMENT The activity of this enzyme is enhanced by Mg2+ ion but !1inhibited by Ca2+, Zn2+ and Be2+ ions. GENETICS !$#gene SGD:PHO13; MIPS:YDL236w !'##cross-references SGD:S0002395; MIPS:YDL236w !$#map_position 4L CLASSIFICATION #superfamily aryl phosphatase PHO13 KEYWORDS glycoprotein; phosphoric monoester hydrolase FEATURE !$64,65 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 312 #molecular-weight 34624 #checksum 7061 SEQUENCE /// ENTRY A38148 #type complete TITLE protein-tyrosine-phosphatase (EC 3.1.3.48), low molecular weight, splice form f [validated] - human ALTERNATE_NAMES acid phosphatase A; acid phosphatase ACP1; acid phosphatase B-f; HCPTP-A; phosphotyrosyl protein phosphatase A; soluble acid phosphatase ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1993 #sequence_revision 01-Dec-1995 #text_change 08-Dec-2000 ACCESSIONS A38148; A39491; S23142; S23143; A40663; PN0630; I39392 REFERENCE A38148 !$#authors Wo, Y.Y.P.; McCormack, A.L.; Shabanowitz, J.; Hunt, D.F.; !1Davis, J.P.; Mitchell, G.L.; Van Etten, R.L. !$#journal J. Biol. Chem. (1992) 267:10856-10865 !$#title Sequencing, cloning, and expression of human red cell-type !1acid phosphatase, a cytoplasmic phosphotyrosyl protein !1phosphatase. !$#cross-references MUID:92268143; PMID:1587862 !$#accession A38148 !'##molecule_type mRNA !'##residues 1-158 ##label WOY !'##cross-references GB:M83653; NID:g179635; PIDN:AAB59354.1; !1PID:g179636 !'##experimental_source red cells; allele B !'##note sequence extracted from NCBI backbone (NCBIP:103842) REFERENCE A39491 !$#authors Dissing, J.; Johnsen, A.H.; Sensabaugh, G.F. !$#journal J. Biol. Chem. (1991) 266:20619-20625 !$#title Human red cell acid phosphatase (ACP1). The amino acid !1sequence of the two isozymes Bf and Bs encoded by the ACP1*B !1allele. !$#cross-references MUID:92041911; PMID:1939112 !$#accession A39491 !'##molecule_type protein !'##residues 2-158 ##label DIS !'##experimental_source allele B REFERENCE S23142 !$#authors Dissing, J.; Johnsen, A.H. !$#journal Biochim. Biophys. Acta (1992) 1121:261-268 !$#title Human red cell acid phosphatase (ACP1): the primary !1structure of the two pairs of isozymes encoded by the ACP1 A !1and ACP1 C alleles. !$#cross-references MUID:92329495; PMID:1627603 !$#accession S23142 !'##molecule_type protein !'##residues 2-105,'R',107-158 ##label DI2 !'##experimental_source allele A !$#accession S23143 !'##molecule_type protein !'##residues 2-158 ##label DI3 !'##experimental_source allele C REFERENCE A40663 !$#authors Shekels, L.L.; Smith, A.J.; Van Etten, R.L.; Bernlohr, D.A. !$#journal Protein Sci. (1992) 1:710-721 !$#title Identification of the adipocyte acid phosphatase as a !1PAO-sensitive tyrosyl phosphatase. !$#cross-references MUID:93284125; PMID:1304913 !$#accession A40663 !'##molecule_type mRNA !'##residues 'PARREAAR',21-105,'R',107-158 ##label SHE !'##cross-references GB:S62884; NID:g386133; PIDN:AAB27085.1; !1PID:g386134 !'##experimental_source adipocytes; allele A !'##note sequence extracted from NCBI backbone (NCBIN:134183, !1NCBIP:134185) REFERENCE PN0630 !$#authors Lazaruk, K.D.A.; Dissing, J.; Sensabaugh, G.F. !$#journal Biochem. Biophys. Res. Commun. (1993) 196:440-446 !$#title Exon structure at the human ACP1 locus supports alternative !1splicing model for f and s isozyme generation. !$#cross-references MUID:94030032; PMID:8216326 !$#accession PN0630 !'##molecule_type DNA !'##residues 40-77 ##label LAZ REFERENCE I39392 !$#authors Sensabaugh, G.F.; Lazaruk, K.A. !$#journal Hum. Mol. Genet. (1993) 2:1079 !$#title A TaqI site identifies the *A allele at the ACP1 locus. !$#cross-references MUID:93372822; PMID:8364553 !$#accession I39392 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 99-155,'XX',158 ##label SEN !'##cross-references GB:L06508; NID:g178004; PIDN:AAB59628.1; !1PID:g505334 GENETICS !$#gene GDB:ACP1 !'##cross-references GDB:118962; OMIM:171500 !$#map_position 2p25-2p25 !$#introns 133/3 FUNCTION !$#description catalyzes hydrolysis of peptidyl-phosphotyrosine to !1peptidyl-tyrosine and phosphate CLASSIFICATION #superfamily protein-tyrosine-phosphatase, low molecular !1weight KEYWORDS acetylated amino end; alternative splicing; phosphoprotein; !1phosphoric monoester hydrolase; polymorphism; !1tyrosine-specific phosphatase FEATURE !$2-158 #product protein-tyrosine-phosphatase, low molecular !8weight, splice form f #status experimental #label !8MAT\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental\ !$13 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$19 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 158 #molecular-weight 18042 #checksum 5808 SEQUENCE /// ENTRY B38148 #type complete TITLE protein-tyrosine-phosphatase (EC 3.1.3.48), low molecular weight, splice form s [validated] - human ALTERNATE_NAMES acid phosphatase ACP1; acid phosphatase B-s; HCPTP-B; phosphotyrosyl protein phosphatase B; soluble acid phosphatase ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1993 #sequence_revision 01-Dec-1995 #text_change 08-Dec-2000 ACCESSIONS B38148; C38148; B39491; A38967; B38967; PN0631; B40663 REFERENCE A38148 !$#authors Wo, Y.Y.P.; McCormack, A.L.; Shabanowitz, J.; Hunt, D.F.; !1Davis, J.P.; Mitchell, G.L.; Van Etten, R.L. !$#journal J. Biol. Chem. (1992) 267:10856-10865 !$#title Sequencing, cloning, and expression of human red cell-type !1acid phosphatase, a cytoplasmic phosphotyrosyl protein !1phosphatase. !$#cross-references MUID:92268143; PMID:1587862 !$#accession B38148 !'##molecule_type mRNA !'##residues 3-157 ##label WO2 !'##cross-references GB:M83654; NID:g179660; PIDN:AAB59355.1; !1PID:g179661 !'##experimental_source red cells; allele B !'##note sequence modified after extraction from NCBI backbone !$#accession C38148 !'##molecule_type protein !'##residues 1-8,'X',10-12,'X',14-15,'X',17-20,'X',22-28,'X',30-34,'X', !136-40,'X',42-67,'X',69-76,'X',78-87,'XX',90-115,'X',117-124, !1'XXX',128-157 ##label WOA !'##experimental_source allele B REFERENCE A39491 !$#authors Dissing, J.; Johnsen, A.H.; Sensabaugh, G.F. !$#journal J. Biol. Chem. (1991) 266:20619-20625 !$#title Human red cell acid phosphatase (ACP1). The amino acid !1sequence of the two isozymes Bf and Bs encoded by the ACP1*B !1allele. !$#cross-references MUID:92041911; PMID:1939112 !$#accession B39491 !'##molecule_type protein !'##residues 1-157 ##label DIS !'##experimental_source allele B REFERENCE S23142 !$#authors Dissing, J.; Johnsen, A.H. !$#journal Biochim. Biophys. Acta (1992) 1121:261-268 !$#title Human red cell acid phosphatase (ACP1): the primary !1structure of the two pairs of isozymes encoded by the ACP1 A !1and ACP1 C alleles. !$#cross-references MUID:92329495; PMID:1627603 !$#accession A38967 !'##molecule_type protein !'##residues 1-104,'R',106-157 ##label DI2 !'##experimental_source allele A !$#accession B38967 !'##molecule_type protein !'##residues 1-157 ##label DI3 !'##experimental_source allele C REFERENCE PN0630 !$#authors Lazaruk, K.D.A.; Dissing, J.; Sensabaugh, G.F. !$#journal Biochem. Biophys. Res. Commun. (1993) 196:440-446 !$#title Exon structure at the human ACP1 locus supports alternative !1splicing model for f and s isozyme generation. !$#cross-references MUID:94030032; PMID:8216326 !$#accession PN0631 !'##molecule_type DNA !'##residues 39-76 ##label LAZ REFERENCE A40663 !$#authors Shekels, L.L.; Smith, A.J.; Van Etten, R.L.; Bernlohr, D.A. !$#journal Protein Sci. (1992) 1:710-721 !$#title Identification of the adipocyte acid phosphatase as a !1PAO-sensitive tyrosyl phosphatase. !$#cross-references MUID:93284125; PMID:1304913 !$#accession B40663 !'##molecule_type mRNA !'##residues 'PRRGR',6-104,'R',106-157 ##label SHE !'##cross-references GB:S62885; NID:g386135; PIDN:AAB27086.1; !1PID:g386136 !'##experimental_source adipocytes; allele A !'##note sequence extracted from NCBI backbone (NCBIN:134184, !1NCBIP:134186) GENETICS !$#gene GDB:ACP1 !'##cross-references GDB:118962; OMIM:171500 !$#map_position 2p25-2p25 CLASSIFICATION #superfamily protein-tyrosine-phosphatase, low molecular !1weight KEYWORDS acetylated amino end; alternative splicing; phosphoprotein; !1phosphoric monoester hydrolase; polymorphism; !1tyrosine-specific phosphatase FEATURE !$1-157 #product protein-tyrosine-phosphatase, low molecular !8weight, splice form s #status experimental #label !8MAT\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$12 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$18 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 157 #molecular-weight 17846 #checksum 3102 SEQUENCE /// ENTRY A42082 #type complete TITLE protein-tyrosine-phosphatase (EC 3.1.3.48), low molecular weight - bovine ALTERNATE_NAMES acid phosphatase; acid phosphomonoesterase ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A42082; A31423 REFERENCE A42082 !$#authors Wo, Y.Y.; Zhou, M.M.; Stevis, P.; Davis, J.P.; Zhang, Z.Y.; !1Van Etten, R.L. !$#journal Biochemistry (1992) 31:1712-1721 !$#title Cloning, expression, and catalytic mechanism of the low !1molecular weight phosphotyrosyl protein phosphatase from !1bovine heart. !$#cross-references MUID:92144586; PMID:1339287 !$#accession A42082 !'##molecule_type mRNA !'##residues 1-158 ##label WO1 !'##cross-references GB:M83656; NID:g163595; PIDN:AAC37328.1; !1PID:g163596 !'##experimental_source heart !'##note sequence extracted from NCBI backbone (NCBIN:81040, !1NCBIP:81041) REFERENCE A31423 !$#authors Camici, G.; Manao, G.; Cappugi, G.; Modesti, A.; Stefani, !1M.; Ramponi, G. !$#journal J. Biol. Chem. (1989) 264:2560-2567 !$#title The complete amino acid sequence of the low molecular weight !1cytosolic acid phosphatase. !$#cross-references MUID:89123343; PMID:2644264 !$#accession A31423 !'##molecule_type protein !'##residues 2-56,'N',58-158 ##label CAM !'##experimental_source liver REFERENCE A57845 !$#authors Davis, J.P.; Zhou, M.M.; Van Etten, R.L. !$#journal J. Biol. Chem. (1994) 269:8734-8740 !$#title Kinetic and site-directed mutagenesis studies of the !1cysteine residues of bovine low molecular weight !1phosphotyrosyl protein phosphatase. !$#cross-references MUID:94179276; PMID:8132604 !$#contents annotation; site-directed mutagenesis of active site !1residues REFERENCE A57844 !$#authors Zhang, Z.; Harms, E.; Van Etten, R.L. !$#journal J. Biol. Chem. (1994) 269:25947-25950 !$#title Asp-129 of low molecular weight protein tyrosine phosphatase !1is involved in leaving group protonation. !$#cross-references MUID:95014410; PMID:7929301 !$#contents annotation; site-directed mutagenesis of active site !1residues CLASSIFICATION #superfamily protein-tyrosine-phosphatase, low molecular !1weight KEYWORDS acetylated amino end; phosphoprotein; phosphoric monoester !1hydrolase; tyrosine-specific phosphatase FEATURE !$2-158 #product acid phosphatase #status experimental #label !8MAT\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental\ !$13 #active_site Cys (phosphocysteine intermediate) !8#status experimental\ !$19 #binding_site substrate phosphate (Arg) #status !8experimental SUMMARY #length 158 #molecular-weight 18054 #checksum 8582 SEQUENCE /// ENTRY A55446 #type complete TITLE protein-tyrosine-phosphatase (EC 3.1.3.48), low molecular weight - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES protein-tyrosine-phosphatase stp1 ORGANISM #formal_name Schizosaccharomyces pombe DATE 10-Feb-1995 #sequence_revision 08-Mar-1996 #text_change 01-Dec-2000 ACCESSIONS A55446; T39199; T37494 REFERENCE A55446 !$#authors Mondesert, O.; Moreno, S.; Russell, P. !$#journal J. Biol. Chem. (1994) 269:27996-27999 !$#title Low molecular weight protein-tyrosine phosphatases are !1highly conserved between fission yeast and man. !$#cross-references MUID:95050572; PMID:7961734 !$#accession A55446 !'##molecule_type mRNA !'##residues 1-156 ##label MON !'##cross-references GB:L33929; NID:g602991; PIDN:AAA61930.1; !1PID:g602992 REFERENCE Z21835 !$#authors Wood, V.; Rajandream, M.A.; Barrell, B.G.; Ramsperger, U.; !1Pohl, T. !$#submission submitted to the EMBL Data Library, September 1999 !$#accession T39199 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-58 ##label WOO !'##cross-references EMBL:AL110469; PIDN:CAB54149.1; GSPDB:GN00066; !1SPDB:SPAC926.01c !'##experimental_source strain 972h-; cosmid c926 REFERENCE Z21718 !$#authors Bothe, G.; Pohl, T.; McDougall, R.C.; Rajandream, M.A.; !1Barrell, B.G. !$#submission submitted to the EMBL Data Library, November 1999 !$#accession T37494 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 58-156 ##label BOT !'##cross-references EMBL:AL132769; PIDN:CAB59888.1; GSPDB:GN00066; !1SPDB:SPAC1071.12c !'##experimental_source strain 972h-; cosmid c1071 GENETICS !$#gene stp1; SPDB:SPAC926.01c; SPDB:SPAC1071.12c !$#map_position 1 CLASSIFICATION #superfamily protein-tyrosine-phosphatase, low molecular !1weight KEYWORDS phosphoprotein; phosphoric monoester hydrolase; !1tyrosine-specific phosphatase FEATURE !$11 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$17 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 156 #molecular-weight 17391 #checksum 9023 SEQUENCE /// ENTRY A57390 #type complete TITLE protein-tyrosine-phosphatase (EC 3.1.3.48), low molecular weight - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YP9499.28c; protein YPR073c; protein-tyrosine-phosphatase LTP1 ORGANISM #formal_name Saccharomyces cerevisiae DATE 08-Dec-1995 #sequence_revision 08-Mar-1996 #text_change 21-Jul-2000 ACCESSIONS A57390; S48543; S54094; S69061 REFERENCE A57390 !$#authors Ostanin, K.; Pokalsky, C.; Wang, S.; Van Etten, R.L. !$#journal J. Biol. Chem. (1995) 270:18491-18499 !$#title Cloning and characterization of a Saccharomyces cerevisiae !1gene encoding the low molecular weight protein-tyrosine !1phosphatase. !$#cross-references MUID:95355477; PMID:7629177 !$#accession A57390 !'##molecule_type DNA !'##residues 1-161 ##label OST !'##cross-references GB:U11057; NID:g507919; PIDN:AAA99546.1; !1PID:g507920 REFERENCE S48543 !$#authors Ostanin, K.; Van Etten, R.L. !$#submission submitted to the EMBL Data Library, June 1994 !$#description Cloning of the low molecular weight protein tyrosine !1phosphatase from yeast Saccharomyces cerevisiae. !$#accession S48543 !'##molecule_type mRNA !'##residues 1-161 ##label OS2 !'##cross-references EMBL:U11057; NID:g507919; PIDN:AAA99546.1; !1PID:g507920 REFERENCE S54059 !$#authors Badcock, K.; Churcher, C.M. !$#submission submitted to the EMBL Data Library, May 1995 !$#accession S54094 !'##molecule_type DNA !'##residues 1-161 ##label BAD !'##cross-references EMBL:Z49219; NID:g805025; PIDN:CAA89190.1; !1PID:g805053; GSPDB:GN00016; MIPS:YPR073c !'##experimental_source strain AB972 REFERENCE S69057 !$#authors Couch, J. !$#submission submitted to the EMBL Data Library, March 1996 !$#description The sequence of S. cerevisiae cosmid 9513. !$#accession S69061 !'##molecule_type DNA !'##residues 1-161 ##label COU !'##cross-references EMBL:U51033; NID:g1230676; PIDN:AAB68124.1; !1PID:g1230681; GSPDB:GN00016; MIPS:YPR073c GENETICS !$#gene SGD:LTP1; MIPS:YPR073c !'##cross-references SGD:S0006277; MIPS:YPR073c !$#map_position 16R CLASSIFICATION #superfamily protein-tyrosine-phosphatase, low molecular !1weight KEYWORDS phosphoprotein; phosphoric monoester hydrolase; !1tyrosine-specific phosphatase FEATURE !$14 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$20 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 161 #molecular-weight 18675 #checksum 5516 SEQUENCE /// ENTRY S49360 #type complete TITLE protein-tyrosine-phosphatase (EC 3.1.3.48) homolog ywlE, low molecular weight - Bacillus subtilis ALTERNATE_NAMES ipc-31d protein ORGANISM #formal_name Bacillus subtilis DATE 16-Feb-1995 #sequence_revision 08-Mar-1996 #text_change 16-Jun-2000 ACCESSIONS I40479; B70062; S49360 REFERENCE I40473 !$#authors Martinussen, J.; Glaser, P.; Andersen, P.S.; Saxild, H.H. !$#journal J. Bacteriol. (1995) 177:271-274 !$#title Two genes encoding uracil phosphoribosyltransferase are !1present in Bacillus subtilis. !$#cross-references MUID:95095982; PMID:7798145 !$#accession I40479 !'##status nucleic acid sequence not shown; translation not shown; !1translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-150 ##label MAR !'##cross-references EMBL:Z38002; NID:g556877; PIDN:CAA86107.1; !1PID:g556883 !'##note sequence unidentified by authors or in GB/EMBL/DDBJ REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B70062 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-150 ##label KUN !'##cross-references GB:Z99122; GB:AL009126; NID:g2636029; !1PIDN:CAB15710.1; PID:g2636218 !'##experimental_source strain 168 GENETICS !$#gene ywlE; ipc-31d CLASSIFICATION #superfamily protein-tyrosine-phosphatase, low molecular !1weight KEYWORDS phosphoprotein; phosphoric monoester hydrolase; !1tyrosine-specific phosphatase FEATURE !$7 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$13 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 150 #molecular-weight 16785 #checksum 860 SEQUENCE /// ENTRY S52140 #type complete TITLE protein-tyrosine-phosphatase (EC 3.1.3.48), low molecular weight - Erwinia amylovora ALTERNATE_NAMES acid phosphatase amsI ORGANISM #formal_name Erwinia amylovora DATE 15-Jul-1995 #sequence_revision 08-Mar-1996 #text_change 11-Jun-1999 ACCESSIONS S61893; S52140 REFERENCE S61891 !$#authors Bugert, P.; Geider, K. !$#journal Mol. Microbiol. (1995) 15:917-933 !$#title Molecular analysis of the ams operon required for !1exopolysaccharide synthesis of Erwinia amylovora. !$#cross-references MUID:95319333; PMID:7596293 !$#accession S61893 !'##molecule_type DNA !'##residues 1-144 ##label BU2 !'##cross-references EMBL:X77921; NID:g600426; PIDN:CAA54881.1; !1PID:g600429 GENETICS !$#gene amsI CLASSIFICATION #superfamily protein-tyrosine-phosphatase, low molecular !1weight KEYWORDS phosphoprotein; phosphoric monoester hydrolase; !1tyrosine-specific phosphatase FEATURE !$9 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$15 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 144 #molecular-weight 15772 #checksum 3352 SEQUENCE /// ENTRY D41903 #type complete TITLE arsenate reductase (EC 1.-.-.-) - Staphylococcus aureus plasmid pI258 ORGANISM #formal_name Staphylococcus aureus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 11-Jun-1999 ACCESSIONS D41903 REFERENCE A41903 !$#authors Ji, G.; Silver, S. !$#journal J. Bacteriol. (1992) 174:3684-3694 !$#title Regulation and expression of the arsenic resistance operon !1from Staphylococcus aureus plasmid pI258. !$#cross-references MUID:92276351; PMID:1534328 !$#accession D41903 !'##molecule_type DNA !'##residues 1-131 ##label JI1 !'##cross-references GB:M86824; NID:g150725; PIDN:AAA25638.1; !1PID:g150729 !'##note sequence extracted from NCBI backbone (NCBIN:104669, !1NCBIP:104673) GENETICS !$#gene arsC !$#genome plasmid FUNCTION !$#description catalyzes the reduction of arsenate [As(V)] to arsenite [As !1(III)] CLASSIFICATION #superfamily protein-tyrosine-phosphatase, low molecular !1weight KEYWORDS oxidoreductase; toxic oxyanion resistance SUMMARY #length 131 #molecular-weight 14813 #checksum 8938 SEQUENCE /// ENTRY C41902 #type complete TITLE arsenate reductase (EC 1.-.-.-) - Staphylococcus xylosus plasmid pSX267 ORGANISM #formal_name Staphylococcus xylosus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 31-Mar-1996 ACCESSIONS C41902 REFERENCE A41902 !$#authors Rosenstein, R.; Peschel, A.; Wieland, B.; Gotz, F. !$#journal J. Bacteriol. (1992) 174:3676-3683 !$#title Expression and regulation of the antimonite, arsenite, and !1arsenate resistance operon of Staphylococcus xylosus plasmid !1pSX267. !$#cross-references MUID:92276350; PMID:1534327 !$#accession C41902 !'##molecule_type DNA !'##residues 1-131 ##label ROS !'##cross-references GB:M80565 !'##note sequence extracted from NCBI backbone (NCBIN:104639, !1NCBIP:104646) GENETICS !$#gene arsC !$#genome plasmid FUNCTION !$#description catalyzes the reduction of arsenate [As(V)] to arsenite [As !1(III)] CLASSIFICATION #superfamily protein-tyrosine-phosphatase, low molecular !1weight KEYWORDS oxidoreductase; toxic oxyanion resistance SUMMARY #length 131 #molecular-weight 14922 #checksum 8858 SEQUENCE /// ENTRY A38874 #type complete TITLE protein-tyrosine-phosphatase (EC 3.1.3.48) cdc25C - human ALTERNATE_NAMES cdc25C protein ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1993 #sequence_revision 25-Apr-1997 #text_change 11-Jun-1999 ACCESSIONS I59168; A38874 REFERENCE I59168 !$#authors Sadhu, K.; Reed, B.I.; Richardson, H.; Russell, P. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:5139-5143 !$#title Human homolog of fission yeast cdc25 mitotic inducer is !1predominantly expressed in G-2. !$#cross-references MUID:90311358; PMID:2195549 !$#accession I59168 !'##molecule_type mRNA !'##residues 1-473 ##label RUS !'##cross-references GB:M34065; NID:g180175; PIDN:AAA35666.1; !1PID:g180176 GENETICS !$#gene GDB:CDC25C; CDC25 !'##cross-references GDB:129559; OMIM:157680 !$#map_position 5q31-5q31 FUNCTION !$#description catalyzes hydrolysis of peptidyl-phosphotyrosine to !1peptidyl-tyrosine and phosphate !$#pathway initiation of mitosis !$#note cdc25 activates the cdc2 protein kinase by dephosphorylating !1it CLASSIFICATION #superfamily human protein-tyrosine-phosphatase cdc25C; !1cdc25-type protein-tyrosine-phosphatase homology KEYWORDS cell cycle control; mitosis; phosphoprotein; phosphoric !1monoester hydrolase; tyrosine-specific phosphatase FEATURE !$259-452 #domain cdc25-type protein-tyrosine-phosphatase !8homology #label PTP\ !$377 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$383 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 473 #molecular-weight 53311 #checksum 641 SEQUENCE /// ENTRY A42679 #type complete TITLE protein-tyrosine-phosphatase (EC 3.1.3.48) cdc25-1 - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 30-Sep-1993 #sequence_revision 25-Apr-1997 #text_change 11-Jun-1999 ACCESSIONS A42679; I51406 REFERENCE A42679 !$#authors Kumagai, A.; Dunphy, W.G. !$#journal Cell (1992) 70:139-151 !$#title Regulation of the cdc25 protein during the cell cycle in !1Xenopus extracts. !$#cross-references MUID:92323543; PMID:1623517 !$#accession A42679 !'##molecule_type mRNA !'##residues 1-550 ##label KUM !'##cross-references GB:M94262; NID:g214024; PIDN:AAA49671.1; !1PID:g214025 REFERENCE I51405 !$#authors Izumi, T.; Walker, D.H.; Maller, J.L. !$#journal Mol. Biol. Cell (1992) 3:927-939 !$#title Periodic changes in phosphorylation of the Xenopus cdc25 !1phosphatase regulate its activity. !$#cross-references MUID:93004945; PMID:1392080 !$#accession I51406 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-550 ##label IZU !'##cross-references GB:M96858; NID:g214030; PIDN:AAA49674.1; !1PID:g214031 COMMENT This protein is activated by extensive phosphorylation on !1Ser and Thr residues in its amino-terminal region. GENETICS !$#gene cdc25B FUNCTION !$#description catalyzes hydrolysis of peptidyl-phosphotyrosine to !1peptidyl-tyrosine and phosphate !$#pathway initiation of mitosis !$#note cdc25 activates the cdc2 protein kinase by dephosphorylating !1it CLASSIFICATION #superfamily human protein-tyrosine-phosphatase cdc25C; !1cdc25-type protein-tyrosine-phosphatase homology KEYWORDS cell cycle control; mitosis; phosphoprotein; phosphoric !1monoester hydrolase; tyrosine-specific phosphatase FEATURE !$339-532 #domain cdc25-type protein-tyrosine-phosphatase !8homology #label PTP\ !$457 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$463 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 550 #molecular-weight 62182 #checksum 1823 SEQUENCE /// ENTRY A41648 #type complete TITLE protein-tyrosine-phosphatase (EC 3.1.3.48) cdc25A - human ALTERNATE_NAMES cell division cycle protein cdc25A ORGANISM #formal_name Homo sapiens #common_name man DATE 28-May-1992 #sequence_revision 25-Apr-1997 #text_change 11-Jun-1999 ACCESSIONS A41648 REFERENCE A41648 !$#authors Galaktionov, K.; Beach, D. !$#journal Cell (1991) 67:1181-1194 !$#title Specific activation of cdc25 tyrosine phosphatases by B-type !1cyclins: evidence for multiple roles of mitotic cyclins. !$#cross-references MUID:92103683; PMID:1836978 !$#accession A41648 !'##molecule_type mRNA !'##residues 1-523 ##label GAL !'##cross-references GB:M81933; NID:g180170; PIDN:AAA58415.1; !1PID:g180171 COMMENT This protein can be activated by association with cyclin B. GENETICS !$#gene GDB:CDC25A !'##cross-references GDB:133773; OMIM:116947 !$#map_position 3p21.3-3p21.2 FUNCTION !$#description catalyzes the hydrolysis of peptidyl-phosphotyrosine to !1release phosphate !$#pathway initiation of mitosis !$#note cdc25 activates the cdc2 protein kinase by dephosphorylating !1it CLASSIFICATION #superfamily human protein-tyrosine-phosphatase cdc25A; !1cdc25-type protein-tyrosine-phosphatase homology KEYWORDS cell cycle control; mitosis; phosphoprotein; phosphoric !1monoester hydrolase; tyrosine-specific phosphatase FEATURE !$312-505 #domain cdc25-type protein-tyrosine-phosphatase !8homology #label PTP\ !$430 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$436 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 523 #molecular-weight 58796 #checksum 5612 SEQUENCE /// ENTRY B41648 #type complete TITLE protein-tyrosine-phosphatase (EC 3.1.3.48) cdc25B - human ALTERNATE_NAMES cdc25B tyrosine phoshphatase; cdc25Hu2 protein ORGANISM #formal_name Homo sapiens #common_name man DATE 28-May-1992 #sequence_revision 25-Apr-1997 #text_change 11-Jun-1999 ACCESSIONS B41648; A45579 REFERENCE A41648 !$#authors Galaktionov, K.; Beach, D. !$#journal Cell (1991) 67:1181-1194 !$#title Specific activation of cdc25 tyrosine phosphatases by B-type !1cyclins: evidence for multiple roles of mitotic cyclins. !$#cross-references MUID:92103683; PMID:1836978 !$#accession B41648 !'##molecule_type mRNA !'##residues 1-566 ##label GAL !'##cross-references GB:M81934; NID:g180172; PIDN:AAA58416.1; !1PID:g180173 REFERENCE A45579 !$#authors Nagata, A.; Igarashi, M.; Jinno, S.; Suto, K.; Okayama, H. !$#journal New Biol. (1991) 3:959-968 !$#title An additional homolog of the fission yeast cdc25+ gene !1occurs in humans and is highly expressed in some cancer !1cells. !$#cross-references MUID:92118716; PMID:1662986 !$#accession A45579 !'##molecule_type mRNA !'##residues 1-560,'D',562-566 ##label NAG !'##cross-references GB:S78187; NID:g243485; PIDN:AAB21139.1; !1PID:g243486 !'##note sequence extracted from NCBI backbone (NCBIN:78187, !1NCBIP:78188) COMMENT This protein is highly expressed in some cancer cells. GENETICS !$#gene GDB:CDC25B !'##cross-references GDB:133774; OMIM:116949 !$#map_position 20p13-20p13 FUNCTION !$#description catalyzes hydrolysis of peptidyl-phosphotyrosine to !1peptidyl-tyrosine and phosphate !$#pathway initiation of mitosis !$#note cdc25 activates the cdc2 protein kinase by dephosphorylating !1it CLASSIFICATION #superfamily human protein-tyrosine-phosphatase cdc25A; !1cdc25-type protein-tyrosine-phosphatase homology KEYWORDS cell cycle control; mitosis; phosphoprotein; phosphoric !1monoester hydrolase; tyrosine-specific phosphatase FEATURE !$357-548 #domain cdc25-type protein-tyrosine-phosphatase !8homology #label PTP\ !$473 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$479 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 566 #molecular-weight 63442 #checksum 4395 SEQUENCE /// ENTRY A32290 #type complete TITLE protein-tyrosine-phosphatase (EC 3.1.3.48) cdc25 homolog string - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 05-Oct-1989 #sequence_revision 25-Apr-1997 #text_change 11-Jun-1999 ACCESSIONS A32290; S12008 REFERENCE A32290 !$#authors Edgar, B.A.; O'Farrell, P.H. !$#journal Cell (1989) 57:177-187 !$#title Genetic control of cell division patterns in the Drosophila !1embryo. !$#cross-references MUID:89195217; PMID:2702688 !$#accession A32290 !'##molecule_type mRNA !'##residues 1-479 ##label EDG !'##cross-references GB:M24909; NID:g158507; PIDN:AAA28916.1; !1PID:g158508 REFERENCE S12008 !$#authors Jimenez, J.; Alphey, L.; Nurse, P.; Glover, D.M. !$#journal EMBO J. (1990) 9:3565-3571 !$#title Complementation of fission yeast cdc2(ts) and cdc25(ts) !1mutants identifies two cell cycle genes from Drosophila: a !1cdc2 homologue and string. !$#cross-references MUID:91006056; PMID:2120044 !$#accession S12008 !'##molecule_type mRNA !'##residues 1-227,'A',229-479 ##label JIM !'##cross-references EMBL:X57495; NID:g7706; PIDN:CAA40732.1; PID:g7707 GENETICS !$#gene FlyBase:stg !'##cross-references FlyBase:FBgn0003525 FUNCTION !$#description catalyzes hydrolysis of peptidyl-phosphotyrosine to !1peptidyl-tyrosine and phosphate !$#pathway initiation of mitosis !$#note cdc25 activates the cdc2 protein kinase by dephosphorylating !1it CLASSIFICATION #superfamily protein-tyrosine-phosphatase string; cdc25-type !1protein-tyrosine-phosphatase homology KEYWORDS cell cycle control; mitosis; phosphoprotein; phosphoric !1monoester hydrolase; tyrosine-specific phosphatase FEATURE !$252-456 #domain cdc25-type protein-tyrosine-phosphatase !8homology #label PTP\ !$379 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$385 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 479 #molecular-weight 54124 #checksum 5721 SEQUENCE /// ENTRY A41910 #type complete TITLE protein-tyrosine-phosphatase (EC 3.1.3.48) cdc25 homolog twine - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 04-Mar-1993 #sequence_revision 25-Apr-1997 #text_change 11-Jun-1999 ACCESSIONS A41910; S26692 REFERENCE A41910 !$#authors Alphey, L.; Jimenez, J.; White-Cooper, H.; Dawson, I.; !1Nurse, P.; Glover, D.M. !$#journal Cell (1992) 69:977-988 !$#title twine, a cdc25 homolog that functions in the male and female !1germline of Drosophila. !$#cross-references MUID:92298395; PMID:1606618 !$#accession A41910 !'##molecule_type mRNA !'##residues 1-426 ##label ALP !'##cross-references GB:M94158; NID:g157055; PIDN:AAA28413.1; !1PID:g157056 !'##note sequence extracted from NCBI backbone (NCBIN:106834, !1NCBIP:106835) REFERENCE S26692 !$#authors Courtot, C.; Fankhauser, C.; Simanis, V.; Lehner, C.F. !$#journal Development (1992) 116:405-416 !$#title The Drosophila cdc25 homolog twine is required for meiosis. !$#cross-references MUID:93161947; PMID:1286615 !$#accession S26692 !'##molecule_type mRNA !'##residues 32-47,'M',49-426 ##label COU !'##cross-references EMBL:X69018; NID:g8755; PIDN:CAA48783.1; PID:g8756 GENETICS !$#gene twe !'##cross-references FlyBase:FBgn0002673 FUNCTION !$#description catalyzes hydrolysis of peptidyl-phosphotyrosine to !1peptidyl-tyrosine and phosphate !$#pathway meiosis; spermatogenesis; mitosis in embryo !$#note cdc25 activates the cdc2 protein kinase by dephosphorylating !1it CLASSIFICATION #superfamily protein-tyrosine-phosphatase string; cdc25-type !1protein-tyrosine-phosphatase homology KEYWORDS cell cycle control; meiosis; mitosis; phosphoprotein; !1phosphoric monoester hydrolase; spermatogenesis; !1tyrosine-specific phosphatase FEATURE !$201-395 #domain cdc25-type protein-tyrosine-phosphatase !8homology #label PTP\ !$318 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$324 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 426 #molecular-weight 48320 #checksum 3445 SEQUENCE /// ENTRY S15799 #type complete TITLE protein-tyrosine-phosphatase (EC 3.1.3.48) cdc25 homolog - Caenorhabditis elegans ALTERNATE_NAMES protein ZK637.11 ORGANISM #formal_name Caenorhabditis elegans DATE 06-Jan-1995 #sequence_revision 25-Apr-1997 #text_change 20-Mar-1998 ACCESSIONS S15799 REFERENCE S15786 !$#authors Craxton, M.; Ainscough, R.; Coulson, A.; Dear, S.; Du, Z.; !1Durbin, R.; Green, P.; Halloran, N.; Hawkins, T.; Hillier, !1L.; Kozono, Y.; Lee, C.; Lutterbach, B.; Metzstein, M.; Qiu, !1Q.; Shownkeen, R.; Staden, R.; Sulston, J.; Thierry-Mieg, !1J.; Thomas, K.; Waterston, R.; Wilson, R. !$#submission submitted to the EMBL Data Library, May 1991 !$#accession S15799 !'##molecule_type DNA !'##residues 1-316 ##label CRA !'##cross-references EMBL:Z11115; NID:g6953; PID:g6964 GENETICS !$#introns 34/2; 157/3 FUNCTION !$#description catalyzes hydrolysis of peptidyl-phosphotyrosine to !1peptidyl-tyrosine and phosphate !$#pathway initiation of mitosis !$#note cdc25 activates the cdc2 protein kinase by dephosphorylating !1it CLASSIFICATION #superfamily Caenorhabditis protein-tyrosine-phosphatase !1cdc25 homolog; cdc25-type protein-tyrosine-phosphatase !1homology KEYWORDS phosphoprotein; phosphoric monoester hydrolase; !1tyrosine-specific phosphatase FEATURE !$77-274 #domain cdc25-type protein-tyrosine-phosphatase !8homology #label PTP\ !$189 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$195 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 316 #molecular-weight 36469 #checksum 2633 SEQUENCE /// ENTRY S24395 #type complete TITLE protein-tyrosine-phosphatase (EC 3.1.3.48) cdc25 homolog nimT - Emericella nidulans ORGANISM #formal_name Emericella nidulans, Aspergillus nidulans DATE 31-Dec-1993 #sequence_revision 25-Apr-1997 #text_change 11-Jun-1999 ACCESSIONS S24395; S19834 REFERENCE S22694 !$#authors O'Connell, M.J.; Osmani, A.H.; Morris, N.R.; Osmani, S.A. !$#journal EMBO J. (1992) 11:2139-2149 !$#title An extra copy of nimE(cyclinB) elevates pre-MPF levels and !1partially suppresses mutation of nimT(cdc25) in Aspergillus !1nidulans. !$#cross-references MUID:92289679; PMID:1534750 !$#accession S24395 !'##molecule_type mRNA !'##residues 1-556 ##label OCO !'##cross-references EMBL:X64601; NID:g2707; PIDN:CAA45885.1; PID:g2708 GENETICS !$#gene nimT !$#map_position 2 FUNCTION !$#description catalyzes hydrolysis of peptidyl-phosphotyrosine to !1peptidyl-tyrosine and phosphate !$#pathway initiation of mitosis !$#note cdc25 activates the cdc2 protein kinase by dephosphorylating !1it CLASSIFICATION #superfamily protein-tyrosine-phosphatase nimT; cdc25-type !1protein-tyrosine-phosphatase homology KEYWORDS cell cycle control; mitosis; phosphoprotein; phosphoric !1monoester hydrolase; tyrosine-specific phosphatase FEATURE !$300-498 #domain cdc25-type protein-tyrosine-phosphatase !8homology #label PTP\ !$421 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$427 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 556 #molecular-weight 61586 #checksum 2169 SEQUENCE /// ENTRY S62407 #type complete TITLE protein-tyrosine-phosphatase (EC 3.1.3.48) cdc25 - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES cell division control protein cdc25; M-phase inducer phosphatase; mitosis initiation protein; mitotic inducer cdc25m; protein SPAC24H6.05 ORGANISM #formal_name Schizosaccharomyces pombe DATE 16-May-1996 #sequence_revision 25-Apr-1997 #text_change 10-Dec-1999 ACCESSIONS S62407; A25301; T38361 REFERENCE S62402 !$#authors Skelton, J.; Churcher, C.M. !$#submission submitted to the EMBL Data Library, September 1995 !$#accession S62407 !'##molecule_type DNA !'##residues 1-596 ##label SKE !'##cross-references EMBL:Z54142; NID:g984697; PIDN:CAA90849.1; !1PID:g984702 REFERENCE A25301 !$#authors Russell, P.; Nurse, P. !$#journal Cell (1986) 45:145-153 !$#title cdc25+ functions as an inducer in the mitotic control of !1fission yeast. !$#cross-references MUID:86161690; PMID:3955656 !$#accession A25301 !'##molecule_type DNA !'##residues 1-353,'V',355-542,'R',544-570,'WPKCVSF',578,'RR' ##label !1RUS !'##cross-references GB:M13158; NID:g173360; PIDN:AAA35294.1; !1PID:g173361 REFERENCE Z21788 !$#authors Skelton, J.; Churcher, C.M.; Barrell, B.G.; Rajandream, !1M.A.; Walsh, S.V.; Wood, V. !$#submission submitted to the EMBL Data Library, September 1995 !$#accession T38361 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-596 ##label SK2 !'##cross-references EMBL:Z54142; PIDN:CAA90849.1; GSPDB:GN00066; !1SPDB:SPAC24H6.05 !'##experimental_source strain 972h-; cosmid c24H6 GENETICS !$#gene cdc25; SPDB:SPAC24H6.05 !$#map_position 1L FUNCTION !$#description catalyzes hydrolysis of peptidyl-phosphotyrosine to !1peptidyl-tyrosine and phosphate !$#pathway initiation of mitosis !$#note cdc25 activates the cdc2 protein kinase by dephosphorylating !1it; required for initiation of mitosis in this species CLASSIFICATION #superfamily protein-tyrosine-phosphatase nimT; cdc25-type !1protein-tyrosine-phosphatase homology KEYWORDS cell cycle control; mitosis; phosphoprotein; phosphoric !1monoester hydrolase; tyrosine-specific phosphatase FEATURE !$366-557 #domain cdc25-type protein-tyrosine-phosphatase !8homology #label PTP\ !$480 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$486 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 596 #molecular-weight 66565 #checksum 4056 SEQUENCE /// ENTRY A32386 #type complete TITLE protein-tyrosine-phosphatase (EC 3.1.3.48) cdc25 homolog MIH1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES mitotic inducer MIH1; protein YM9532.01c; protein YM9973.10c; protein YMR036c ORGANISM #formal_name Saccharomyces cerevisiae DATE 08-Sep-1989 #sequence_revision 25-Apr-1997 #text_change 21-Jul-2000 ACCESSIONS A32386; S52885; S53953; S05801 REFERENCE A32386 !$#authors Russell, P.; Moreno, S.; Reed, S.I. !$#journal Cell (1989) 57:295-303 !$#title Conservation of mitotic controls in fission and budding !1yeasts. !$#cross-references MUID:89195240; PMID:2649252 !$#accession A32386 !'##molecule_type DNA !'##residues 1-474 ##label RUS !'##cross-references GB:J04846; NID:g340551; PIDN:AAA57223.1; !1PID:g602325 REFERENCE S52885 !$#authors Odell, C.; Bowman, S. !$#submission submitted to the EMBL Data Library, February 1995 !$#accession S52885 !'##molecule_type DNA !'##residues 1-232 ##label ODE !'##cross-references EMBL:Z48502; NID:g695715; PIDN:CAA88402.1; !1PID:g695716; GSPDB:GN00013; MIPS:YMR036c REFERENCE S53944 !$#authors Bowman, S. !$#submission submitted to the EMBL Data Library, May 1995 !$#accession S53953 !'##molecule_type DNA !'##residues 223-237,'ND',240,'FPRISPET',249-364,'FDN',367-473, !1'ILSKSSMSSNSNLSTSHMLLMDGLDTPSYFSFEDERGNHQQVSG', !1'DEEQDGDFTFVGSDREDLPRPARRSLFPSLETEDKK' ##label BOW !'##cross-references EMBL:Z49213; NID:g798952; PIDN:CAA89152.1; !1PID:g798962; GSPDB:GN00013; MIPS:YMR036c !'##experimental_source strain AB972 GENETICS !$#gene SGD:MIH1; MIPS:YMR036c !'##cross-references SGD:S0004639; MIPS:YMR036c !$#map_position 13R FUNCTION !$#description catalyzes hydrolysis of peptidyl-phosphotyrosine to !1peptidyl-tyrosine and phosphate !$#pathway initiation of mitosis !$#note cdc25 activates the cdc2 protein kinase by dephosphorylating !1it CLASSIFICATION #superfamily protein-tyrosine-phosphatase MIH1; cdc25-type !1protein-tyrosine-phosphatase homology KEYWORDS cell cycle control; mitosis; phosphoprotein; phosphoric !1monoester hydrolase; tyrosine-specific phosphatase FEATURE !$196-396 #domain cdc25-type protein-tyrosine-phosphatase !8homology #status atypical #label PTP\ !$320 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$326 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 474 #molecular-weight 54376 #checksum 9965 SEQUENCE /// ENTRY A40449 #type complete TITLE protein-tyrosine-phosphatase (EC 3.1.3.48), nonreceptor type pyp1 - fission yeast (Schizosaccharomyces pombe) ORGANISM #formal_name Schizosaccharomyces pombe DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Dec-1999 ACCESSIONS A40449; T38410 REFERENCE A40449 !$#authors Ottilie, S.; Chernoff, J.; Hannig, G.; Hoffman, C.S.; !1Erikson, R.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:3455-3459 !$#title A fission-yeast gene encoding a protein with features of !1protein-tyrosine-phosphatases. !$#cross-references MUID:91195370; PMID:1849659 !$#accession A40449 !'##status preliminary !'##molecule_type DNA !'##residues 1-550 ##label OTT !'##cross-references GB:M63257; NID:g173441; PIDN:AAA35328.1; !1PID:g173442 REFERENCE Z21792 !$#authors Brown, D.; Churcher, C.M.; Barrell, B.G.; Rajandream, M.A.; !1Walsh, S.V. !$#submission submitted to the EMBL Data Library, April 1996 !$#accession T38410 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-550 ##label BRO !'##cross-references EMBL:Z73100; PIDN:CAA97367.1; GSPDB:GN00066; !1SPDB:SPAC26F1.10c !'##experimental_source strain 972h-; cosmid c26F1 GENETICS !$#gene SPAC26F1.10c !$#map_position 1 CLASSIFICATION #superfamily Schizosaccharomyces !1protein-tyrosine-phosphatase, nonreceptor type pyp1; !1protein-tyrosine-phosphatase homology KEYWORDS phosphoprotein; phosphoric monoester hydrolase; !1tyrosine-specific phosphatase FEATURE !$295-528 #domain protein-tyrosine-phosphatase homology #label !8PTP\ !$470 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$476 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 550 #molecular-weight 61587 #checksum 2007 SEQUENCE /// ENTRY S28391 #type complete TITLE protein-tyrosine-phosphatase (EC 3.1.3.48), nonreceptor type pyp2 - fission yeast (Schizosaccharomyces pombe) ORGANISM #formal_name Schizosaccharomyces pombe DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Dec-1999 ACCESSIONS S28391; A45030; T37961 REFERENCE S28391 !$#authors Millar, J.B.A.; Russell, P.; Dixon, J.E.; Guan, K.L. !$#journal EMBO J. (1992) 11:4943-4952 !$#title Negative regulation of mitosis by two functionally !1overlapping PTPases in fission yeast. !$#cross-references MUID:93099869; PMID:1464319 !$#accession S28391 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-711 ##label MIL !'##cross-references GB:S51320; NID:g261946; PIDN:AAB24544.1; !1PID:g261947 REFERENCE A45030 !$#authors Ottilie, S.; Chernoff, J.; Hannig, G.; Hoffman, C.S.; !1Erikson, R.L. !$#journal Mol. Cell. Biol. (1992) 12:5571-5580 !$#title The fission yeast genes pyp1+ and pyp2+ encode protein !1tyrosine phosphatases that negatively regulate mitosis. !$#cross-references MUID:93078758; PMID:1448087 !$#accession A45030 !'##status preliminary !'##molecule_type DNA !'##residues 1-711 ##label OTT !'##note sequence extracted from NCBI backbone (NCBIP:119076) REFERENCE Z21757 !$#authors Devlin, K.; Churcher, C.M.; Wood, V.; Barrell, B.G.; !1Rajandream, M.A. !$#submission submitted to the EMBL Data Library, September 1997 !$#accession T37961 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-711 ##label DEV !'##cross-references EMBL:Z99531; PIDN:CAB16711.1; GSPDB:GN00066; !1SPDB:SPAC19D5.01 !'##experimental_source strain 972h-; cosmid c19D5 GENETICS !$#gene pyp2 !$#map_position 1 CLASSIFICATION #superfamily Schizosaccharomyces !1protein-tyrosine-phosphatase, nonreceptor type pyp2; !1protein-tyrosine-phosphatase homology KEYWORDS phosphoprotein; phosphoric monoester hydrolase; !1tyrosine-specific phosphatase FEATURE !$458-687 #domain protein-tyrosine-phosphatase homology #label !8PTP\ !$630 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$636 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 711 #molecular-weight 79356 #checksum 1656 SEQUENCE /// ENTRY S28392 #type complete TITLE protein-tyrosine-phosphatase (EC 3.1.3.48), nonreceptor type pyp3 - fission yeast (Schizosaccharomyces pombe) ORGANISM #formal_name Schizosaccharomyces pombe DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Dec-1999 ACCESSIONS S28392; T37537 REFERENCE S28392 !$#authors Millar, J.B.A.; Lenaers, G.; Russell, P. !$#journal EMBO J. (1992) 11:4933-4941 !$#title Pyp3 PTPase acts as a mitotic inducer in fission yeast. !$#cross-references MUID:93099868; PMID:1464318 !$#accession S28392 !'##molecule_type DNA !'##residues 1-303 ##label MIL !'##cross-references EMBL:X69994; NID:g5017; PIDN:CAA49609.1; PID:g5018 REFERENCE Z21721 !$#authors Murphy, L.; Harris, D.; Barrell, B.G.; Rajandream, M.A.; !1Walsh, S.V. !$#submission submitted to the EMBL Data Library, August 1997 !$#accession T37537 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-303 ##label MUR !'##cross-references EMBL:Z98595; PIDN:CAB11188.1; GSPDB:GN00066; !1SPDB:SPAC11E3.09 !'##experimental_source strain 972h-; cosmid c11E3 GENETICS !$#gene pyp3 !$#map_position 1 !$#introns 96/3 CLASSIFICATION #superfamily Schizosaccharomyces !1protein-tyrosine-phosphatase, nonreceptor type pyp3; !1protein-tyrosine-phosphatase homology KEYWORDS phosphoprotein; phosphoric monoester hydrolase; !1tyrosine-specific phosphatase FEATURE !$49-281 #domain protein-tyrosine-phosphatase homology #label !8PTP\ !$227 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$233 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 303 #molecular-weight 34583 #checksum 5144 SEQUENCE /// ENTRY TPHUN1 #type complete TITLE protein-tyrosine-phosphatase (EC 3.1.3.48), nonreceptor type 1 [validated] - human ALTERNATE_NAMES phosphotyrosine phosphatase 1B, long form; protein-tyrosine phosphatase 1B, placental membrane (PTP1B); PTPN1 CONTAINS protein-tyrosine-phosphatase, nonreceptor type 1, membrane-bound form; protein-tyrosine-phosphatase, nonreceptor type 1, soluble form ORGANISM #formal_name Homo sapiens #common_name man DATE 07-Apr-1994 #sequence_revision 07-Apr-1994 #text_change 15-Sep-2000 ACCESSIONS A35992; I59169; I79576; S15849; A33897; A37275 REFERENCE A35992 !$#authors Chernoff, J.; Schievella, A.R.; Jost, C.A.; Erikson, R.L.; !1Neel, B.G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:2735-2739 !$#title Cloning of a cDNA for a major human !1protein-tyrosine-phosphatase. !$#cross-references MUID:90207272; PMID:2157211 !$#accession A35992 !'##molecule_type mRNA !'##residues 1-435 ##label CHE !'##cross-references GB:M31724; NID:g190741; PIDN:AAA60223.1; !1PID:g190742 REFERENCE I59169 !$#authors Brown-Shimer, S.; Johnson, K.A.; Lawrence, J.B.; Johnson, !1C.; Bruskin, A.; Green, N.R.; Hill, D.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:5148-5152 !$#title Molecular cloning and chromosome mapping of the human gene !1encoding protein phosphotyrosyl phosphatase 1B. !$#cross-references MUID:90311360; PMID:2164224 !$#accession I59169 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA; mRNA !'##residues 1-435 ##label BRO1 !'##cross-references GB:M33689; NID:g190271; PIDN:AAA60157.1; !1PID:g190272 !$#accession I79576 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 165-435 ##label BRO2 !'##cross-references GB:M33684; NID:g190277; PIDN:AAA60158.1; !1PID:g190279 REFERENCE S15849 !$#authors Pallen, C.J.; Lai, D.S.Y.; Chia, H.P.; Boulet, I.; Tong, !1P.H. !$#journal Biochem. J. (1991) 276:315-323 !$#title Purification and characterization of a higher-molecular-mass !1form of protein phosphotyrosine phosphatase (PTP 1B) from !1placental membranes. !$#cross-references MUID:91264781; PMID:1646596 !$#accession S15849 !'##molecule_type protein !'##residues 'X',8-21;80-92,'C',94-99;'GR',123-130 ##label BIO REFERENCE A33897 !$#authors Charbonneau, H.; Tonks, N.K.; Kumar, S.; Diltz, C.D.; !1Harrylock, M.; Cool, D.E.; Krebs, E.G.; Fischer, E.H.; !1Walsh, K.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:5252-5256 !$#title Human placenta protein-tyrosine-phosphatase: amino acid !1sequence and relationship to a family of receptor-like !1proteins. !$#cross-references MUID:89315775; PMID:2546149 !$#accession A33897 !'##molecule_type protein !'##residues 1-321 ##label CHA REFERENCE A52879 !$#authors Barford, D.; Flint, A.J.; Tonks, N.K. !$#submission submitted to the Brookhaven Protein Data Bank, September !11994 !$#cross-references PDB:2HNP !$#contents annotation; X-ray crystallography, 2.8 angstroms, residues !15-282 REFERENCE A38904 !$#authors Barford, D.; Flint, A.J.; Tonks, N.K. !$#journal Science (1994) 263:1397-1404 !$#title Crystal structure of human protein tyrosine phosphatase 1B. !$#cross-references MUID:94174273; PMID:8128219 !$#contents annotation; X-ray crystallography, 2.8 angstroms REFERENCE A49919 !$#authors Flint, A.J.; Gebbink, M.F.G.B.; Franza Jr., B.R.; Hill, !1D.E.; Tonks, N.K. !$#journal EMBO J. (1993) 12:1937-1946 !$#title Multi-site phosphorylation of the protein tyrosine !1phosphatase, PTP1B: identification of cell cycle regulated !1and phorbol ester stimulated sites of phosphorylation. !$#cross-references MUID:93259136; PMID:8491187 !$#contents annotation; phosphorylation sites GENETICS !$#gene GDB:PTPN1; PTP1B !'##cross-references GDB:126728; OMIM:176885 !$#map_position 20q13.1-20q13.2 !$#introns 164/3; 234/3; 288/3; 363/2; 428/3 FUNCTION !$#description catalyzes hydrolysis of peptidyl-phosphotyrosine to release !1phosphate CLASSIFICATION #superfamily protein-tyrosine-phosphatase, nonreceptor type !11; protein-tyrosine-phosphatase homology KEYWORDS acetylated amino end; phosphoprotein; phosphoric monoester !1hydrolase; tyrosine-specific phosphatase FEATURE !$1-435 #product protein-tyrosine-phosphatase, nonreceptor !8type 1, membrane-bound form #status predicted #label !8MAT\ !$1-321 #product protein-tyrosine-phosphatase, nonreceptor !8type 1, soluble form #status experimental #label SOL\ !$40-266 #domain protein-tyrosine-phosphatase homology #label !8PTP\ !$405-425 #domain transmembrane #status predicted #label TRM\ !$1 #modified_site acetylated amino end (Met) #status !8experimental\ !$215 #active_site Cys (phosphocysteine intermediate) !8#status experimental\ !$221 #binding_site substrate phosphate (Arg) #status !8experimental\ !$352 #binding_site phosphate (Ser) (covalent) (by !8unidentified kinase) #status experimental\ !$378 #binding_site phosphate (Ser) (covalent) (by protein !8kinase C) #status experimental\ !$386 #binding_site phosphate (Ser) (covalent) (by cdc2 !8kinase) #status experimental SUMMARY #length 435 #molecular-weight 49966 #checksum 4319 SEQUENCE /// ENTRY JN0317 #type complete TITLE protein-tyrosine-phosphatase (EC 3.1.3.48), nonreceptor type 1 - mouse ALTERNATE_NAMES protein-tyrosine-phosphatase HA2; protein-tyrosine-phosphatase PTPTY20 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 23-Mar-2001 ACCESSIONS JN0317; S40288; C61180; A57503 REFERENCE JN0317 !$#authors Miyasaka, H.; Li, S.S.L. !$#journal Biochem. Biophys. Res. Commun. (1992) 185:818-825 !$#title The cDNA cloning, nucleotide sequence and expression of an !1intracellular protein tyrosine phosphatase from mouse !1testis. !$#cross-references MUID:92328784; PMID:1378268 !$#accession JN0317 !'##molecule_type mRNA !'##residues 1-432 ##label MIY !'##experimental_source testis REFERENCE S40280 !$#authors Hendriks, W.; Brugman, C.; Zeeuwen, P.; Schepens, J.; !1Wieringa, B. !$#submission submitted to the EMBL Data Library, June 1993 !$#description Assessment of the expression levels of murine !1protein-tyrosine phosphatases, including three novel ones, !1in brain by a semi-quantitative method. !$#accession S40288 !'##molecule_type mRNA !'##residues 102-213 ##label HEN !'##cross-references EMBL:Z23057; NID:g438151; PIDN:CAA80592.1; !1PID:g438152 REFERENCE A61180 !$#authors Yi, T.; Cleveland, J.L.; Ihle, J.N. !$#journal Blood (1991) 78:2222-2228 !$#title Identification of novel protein tyrosine phosphatases of !1hematopoietic cells by polymerase chain reaction !1amplification. !$#cross-references MUID:92032882; PMID:1932742 !$#accession C61180 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 102-103,'I',105,'S',107-213 ##label YIA REFERENCE A57503 !$#authors Liao, K.; Lane, M.D. !$#journal J. Biol. Chem. (1995) 270:12123-12132 !$#title The blockade of preadipocyte differentiation by !1protein-tyrosine phosphatase HA2 is reversed by vanadate. !$#cross-references MUID:95263562; PMID:7744861 !$#accession A57503 !'##status preliminary !'##molecule_type mRNA !'##residues 1-47,'D',49-172,'P',174-265,'HV',268-432 ##label LIA !'##cross-references GB:L40595; NID:g755042; PIDN:AAA64615.1; !1PID:g755043 CLASSIFICATION #superfamily protein-tyrosine-phosphatase, nonreceptor type !11; protein-tyrosine-phosphatase homology KEYWORDS phosphoprotein; phosphoric monoester hydrolase; !1tyrosine-specific phosphatase FEATURE !$40-266 #domain protein-tyrosine-phosphatase homology #label !8PTP\ !$215 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$221 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 432 #molecular-weight 49641 #checksum 7229 SEQUENCE /// ENTRY A34845 #type complete TITLE protein-tyrosine-phosphatase (EC 3.1.3.48), nonreceptor type 1B - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A34845; S23126 REFERENCE A34845 !$#authors Guan, K.; Haun, R.S.; Watson, S.J.; Geahlen, R.L.; Dixon, !1J.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:1501-1505 !$#title Cloning and expression of a protein-tyrosine-phosphatase. !$#cross-references MUID:90160354; PMID:2154749 !$#accession A34845 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-432 ##label GUA !'##cross-references GB:M33962; NID:g206496; PIDN:AAC79516.1; !1PID:g206497 REFERENCE S23126 !$#authors Hashimoto, N.; Zhang, W.R.; Goldstein, B.J. !$#journal Biochem. J. (1992) 284:569-576 !$#title Insulin receptor and epidermal growth factor receptor !1dephosphorylation by three major rat liver protein-tyrosine !1phosphatases expressed in a recombinant bacterial system. !$#cross-references MUID:92287069; PMID:1599438 !$#accession S23126 !'##status preliminary !'##molecule_type mRNA !'##residues 35-283 ##label HAS CLASSIFICATION #superfamily protein-tyrosine-phosphatase, nonreceptor type !11; protein-tyrosine-phosphatase homology KEYWORDS phosphoprotein; phosphoric monoester hydrolase; !1tyrosine-specific phosphatase FEATURE !$40-266 #domain protein-tyrosine-phosphatase homology #label !8PTP\ !$215 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$221 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 432 #molecular-weight 49674 #checksum 4136 SEQUENCE /// ENTRY A33899 #type complete TITLE protein-tyrosine-phosphatase (EC 3.1.3.48), nonreceptor type 2 - human ALTERNATE_NAMES protein-tyrosine-phosphatase, T-cell specific ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1990 #sequence_revision 02-May-1994 #text_change 07-May-1999 ACCESSIONS A33899; C60345; A45742 REFERENCE A33899 !$#authors Cool, D.E.; Tonks, N.K.; Charbonneau, H.; Walsh, K.A.; !1Fischer, E.H.; Krebs, E.G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:5257-5261 !$#title cDNA isolated from a human T-cell library encodes a member !1of the protein-tyrosine-phosphatase family. !$#cross-references MUID:89315776; PMID:2546150 !$#accession A33899 !'##molecule_type mRNA !'##residues 1-415 ##label COO !'##cross-references GB:M25393 REFERENCE A60345 !$#authors Champion-Arnaud, P.; Gesnel, M.C.; Foulkes, N.; Ronsin, C.; !1Sassone-Corsi, P.; Breathnach, R. !$#journal Oncogene (1991) 6:1203-1209 !$#title Activation of transcription via AP-1 or CREB regulatory !1sites is blocked by protein tyrosine phosphatases. !$#cross-references MUID:91319401; PMID:1650442 !$#accession C60345 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 348-415 ##label CHA REFERENCE A45742 !$#authors Johnson, C.V.; Cool, D.E.; Glaccum, M.B.; Green, N.; !1Fischer, E.H.; Bruskin, A.; Hill, D.E.; Lawrence, J.B. !$#journal Genomics (1993) 16:619-629 !$#title Isolation and mapping of human T-cell protein tyrosine !1phosphatase sequences: localization of genes and pseudogenes !1discriminated using fluorescence hybridization with genomic !1versus cDNA probes. !$#cross-references MUID:93315152; PMID:8325634 !$#accession A45742 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type DNA !'##residues 115-125;160-170;230-241;413-415 ##label JOH COMMENT This protein and protein-tyrosine-phosphatase 11A are !1produced from the same gene by alternative splicing. GENETICS !$#gene GDB:PTPN2; PTPT !'##cross-references GDB:128098; OMIM:176887 !$#map_position 18p11.22-18p11.21 !$#introns 120/3; 165/3; 235/3; 347/2 !$#note list of introns may be incomplete CLASSIFICATION #superfamily protein-tyrosine-phosphatase, nonreceptor type !11; protein-tyrosine-phosphatase homology KEYWORDS alternative splicing; phosphoprotein; phosphoric monoester !1hydrolase; tyrosine-specific phosphatase FEATURE !$42-264 #domain protein-tyrosine-phosphatase homology #label !8PTP\ !$216 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$222 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 415 #molecular-weight 48473 #checksum 809 SEQUENCE /// ENTRY A60345 #type complete TITLE protein-tyrosine-phosphatase (EC 3.1.3.48) 11A - human ORGANISM #formal_name Homo sapiens #common_name man DATE 20-Feb-1993 #sequence_revision 02-May-1994 #text_change 24-Apr-1998 ACCESSIONS A60345; B60345 REFERENCE A60345 !$#authors Champion-Arnaud, P.; Gesnel, M.C.; Foulkes, N.; Ronsin, C.; !1Sassone-Corsi, P.; Breathnach, R. !$#journal Oncogene (1991) 6:1203-1209 !$#title Activation of transcription via AP-1 or CREB regulatory !1sites is blocked by protein tyrosine phosphatases. !$#cross-references MUID:91319401; PMID:1650442 !$#accession A60345 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-387 ##label CHA !$#accession B60345 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 348-387 ##label CH2 GENETICS !$#gene GDB:PTPN2; PTPT !'##cross-references GDB:128098; OMIM:176887 !$#map_position 18p11.22-18p11.21 !$#introns 347/2; 381/2 CLASSIFICATION #superfamily protein-tyrosine-phosphatase, nonreceptor type !11; protein-tyrosine-phosphatase homology KEYWORDS alternative splicing; phosphoprotein; phosphoric monoester !1hydrolase; tyrosine-specific phosphatase FEATURE !$42-264 #domain protein-tyrosine-phosphatase homology #label !8PTP\ !$216 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$222 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 387 #molecular-weight 45244 #checksum 2281 SEQUENCE /// ENTRY A38191 #type complete TITLE protein-tyrosine-phosphatase (EC 3.1.3.48) 11A - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 17-Feb-1994 #sequence_revision 02-May-1994 #text_change 11-Jun-1999 ACCESSIONS A38191 REFERENCE A38191 !$#authors Mosinger Jr., B.; Tillmann, U.; Westphal, H.; Tremblay, M.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:499-503 !$#title Cloning and characterization of a mouse cDNA encoding a !1cytoplasmic protein-tyrosine-phosphatase. !$#cross-references MUID:92115688; PMID:1731319 !$#accession A38191 !'##molecule_type mRNA !'##residues 1-382 ##label MOS !'##cross-references GB:M81477; NID:g192683; PIDN:AAA37446.1; !1PID:g192684 !'##note sequence extracted from NCBI backbone (NCBIN:75809, !1NCBIP:75812) COMMENT This transcript was found in a variety of embryonic and !1adult tissues. A shorter transcript was expressed only in !1testes. CLASSIFICATION #superfamily protein-tyrosine-phosphatase, nonreceptor type !11; protein-tyrosine-phosphatase homology KEYWORDS alternative splicing; phosphoprotein; phosphoric monoester !1hydrolase; tyrosine-specific phosphatase FEATURE !$42-264 #domain protein-tyrosine-phosphatase homology #label !8PTP\ !$216 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$222 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 382 #molecular-weight 44572 #checksum 8844 SEQUENCE /// ENTRY S14294 #type complete TITLE protein-tyrosine-phosphatase (EC 3.1.3.48) 11A - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S14294; S21831 REFERENCE S14294 !$#authors Swarup, G.; Kamatkar, S.; Radha, V.; Rema, V. !$#journal FEBS Lett. (1991) 280:65-69 !$#title Molecular cloning and expression of a protein-tyrosine !1phosphatase showing homology with transcription factors Fos !1and Jun. !$#cross-references MUID:91184422; PMID:1849097 !$#accession S14294 !'##status preliminary !'##molecule_type mRNA !'##residues 1-363 ##label SWA !'##cross-references GB:X58828; NID:g56995; PIDN:CAA41633.1; PID:g56996 REFERENCE S21831 !$#authors Swarup, G.; Kamatkar, S.; Radha, V.; Rema, V. !$#submission submitted to the EMBL Data Library, April 1991 !$#accession S21831 !'##status preliminary !'##molecule_type mRNA !'##residues 1-363 ##label SWA2 !'##cross-references EMBL:X58828; NID:g56995; PIDN:CAA41633.1; !1PID:g56996 CLASSIFICATION #superfamily protein-tyrosine-phosphatase, nonreceptor type !11; protein-tyrosine-phosphatase homology KEYWORDS alternative splicing; DNA binding; phosphoprotein; !1phosphoric monoester hydrolase; tyrosine-specific !1phosphatase FEATURE !$42-264 #domain protein-tyrosine-phosphatase homology #label !8PTP\ !$216 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$222 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 363 #molecular-weight 42235 #checksum 3486 SEQUENCE /// ENTRY A41109 #type complete TITLE protein-tyrosine-phosphatase (EC 3.1.3.48) PTPN3, nonreceptor type 3 [validated] - human ALTERNATE_NAMES PTPH1 ORGANISM #formal_name Homo sapiens #common_name man DATE 27-Mar-1992 #sequence_revision 02-May-1994 #text_change 21-Jun-2002 ACCESSIONS A41109; I55698 REFERENCE A41109 !$#authors Yang, Q.; Tonks, N.K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:5949-5953 !$#title Isolation of a cDNA clone encoding a human protein-tyrosine !1phosphatase with homology to the cytoskeletal-associated !1proteins band 4.1, ezrin, and talin. !$#cross-references MUID:91296738; PMID:1648725 !$#accession A41109 !'##molecule_type mRNA !'##residues 1-913 ##label YAN !'##cross-references GB:M64572; NID:g179912; PIDN:AAA35647.1; !1PID:g179913 REFERENCE I55698 !$#authors Ikuta, S.; Itoh, F.; Hinoda, Y.; Toyota, M.; Makiguchi, Y.; !1Imai, K.; Yachi, A. !$#journal J. Gastroenterol. (1994) 29:727-732 !$#title Expression of cytoskeletal-associated protein tyrosine !1phosphatase PTPH1 mRNA in human hepatocellular carcinoma. !$#cross-references MUID:95179278; PMID:7874267 !$#accession I55698 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 899-913 ##label RES !'##cross-references GB:S76309; NID:g913165; PIDN:AAB33583.1; !1PID:g913166 GENETICS !$#gene GDB:PTPN3 !'##cross-references GDB:131386; OMIM:176877 !$#map_position 9q31-9q31 CLASSIFICATION #superfamily protein-tyrosine-phosphatase, nonreceptor type !13; GLGF domain homology; protein 4.1 membrane-binding domain !1homology; protein-tyrosine-phosphatase homology KEYWORDS phosphoprotein; phosphoric monoester hydrolase; !1tyrosine-specific phosphatase FEATURE !$31-308 #domain protein 4.1 membrane-binding domain homology !8#label B41\ !$516-590 #domain GLGF domain homology #label GLG\ !$670-890 #domain protein-tyrosine-phosphatase homology #label !8PTP\ !$842 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$848 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 913 #molecular-weight 104029 #checksum 2796 SEQUENCE /// ENTRY A41105 #type complete TITLE protein-tyrosine-phosphatase (EC 3.1.3.48) PTPN4, nonreceptor type 4 [validated] - human ALTERNATE_NAMES PTPase MEG ORGANISM #formal_name Homo sapiens #common_name man DATE 20-Mar-1992 #sequence_revision 02-May-1994 #text_change 21-Jun-2002 ACCESSIONS A41105 REFERENCE A41105 !$#authors Gu, M.; York, J.D.; Warshawsky, I.; Majerus, P.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:5867-5871 !$#title Identification, cloning, and expression of a cytosolic !1megakaryocyte protein-tyrosine-phosphatase with sequence !1homology to cytoskeletal protein 4.1. !$#cross-references MUID:91288564; PMID:1648233 !$#accession A41105 !'##molecule_type mRNA !'##residues 1-926 ##label GUA !'##cross-references GB:M68941; NID:g190747; PIDN:AAA36530.1; !1PID:g190748 !'##experimental_source megakaryocytes, cell line MEG-10 GENETICS !$#gene GDB:PTPN4 !'##cross-references GDB:131387; OMIM:176878 !$#map_position 9q31-9q31 CLASSIFICATION #superfamily protein-tyrosine-phosphatase, nonreceptor type !13; GLGF domain homology; protein 4.1 membrane-binding domain !1homology; protein-tyrosine-phosphatase homology KEYWORDS phosphoprotein; phosphoric monoester hydrolase; !1tyrosine-specific phosphatase FEATURE !$31-308 #domain protein 4.1 membrane-binding domain homology !8#label B41\ !$523-597 #domain GLGF domain homology #label GLG\ !$679-900 #domain protein-tyrosine-phosphatase homology #label !8PTP\ !$852 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$858 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 926 #molecular-weight 105910 #checksum 4136 SEQUENCE /// ENTRY A41147 #type complete TITLE protein-tyrosine-phosphatase (EC 3.1.3.48), nonreceptor type 5 - rat ALTERNATE_NAMES protein-tyrosine-phosphatase STEP ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Apr-1992 #sequence_revision 02-May-1994 #text_change 11-Jun-1999 ACCESSIONS A41147 REFERENCE A41147 !$#authors Lombroso, P.J.; Murdoch, G.; Lerner, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:7242-7246 !$#title Molecular characterization of a protein-tyrosine-phosphatase !1enriched in striatum. !$#cross-references MUID:91334442; PMID:1714595 !$#accession A41147 !'##molecule_type mRNA !'##residues 1-369 ##label LOM !'##cross-references GB:S49400; GB:M65159; NID:g298203; PIDN:AAB19491.1; !1PID:g233699 !'##note Met-1, Met-25, or Met-41 may be the initiator; if Met-41 is the !1initiator, Gly-42 is a potential site for amino-terminal !1myristoylation COMMENT This protein is found primarily in nervous system tissues. CLASSIFICATION #superfamily protein-tyrosine-phosphatase, nonreceptor type !15; protein-tyrosine-phosphatase homology KEYWORDS brain; phosphoprotein; phosphoric monoester hydrolase; !1tyrosine-specific phosphatase FEATURE !$126-348 #domain protein-tyrosine-phosphatase homology #label !8PTP\ !$300 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$306 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 369 #molecular-weight 42366 #checksum 7338 SEQUENCE /// ENTRY JH0692 #type complete TITLE protein-tyrosine-phosphatase (EC 3.1.3.48), nonreceptor type 7 - human ALTERNATE_NAMES BPTP-4; HePTPase; LC-PTP ORGANISM #formal_name Homo sapiens #common_name man DATE 02-May-1994 #sequence_revision 02-May-1994 #text_change 16-Jun-2000 ACCESSIONS JH0692; A46541; D44929; A46752 REFERENCE JH0692 !$#authors Adachi, M.; Sekiya, M.; Isobe, M.; Kumura, Y.; Ogita, Z.; !1Hinoda, Y.; Imai, K.; Yachi, A. !$#journal Biochem. Biophys. Res. Commun. (1992) 186:1607-1615 !$#title Molecular cloning and chromosomal mapping of a human !1protein-tyrosine phosphatase LC-PTP. !$#cross-references MUID:92378634; PMID:1510684 !$#accession JH0692 !'##molecule_type mRNA !'##residues 1-360 ##label ADA !'##cross-references DDBJ:D11327; NID:g219901; PIDN:BAA01946.1; !1PID:g219902 !'##experimental_source T-cell PEER cDNA library REFERENCE A46541 !$#authors Zanke, B.; Suzuki, H.; Kishihara, K.; Mizzen, L.; Minden, !1M.; Pawson, A.; Mak, T.W. !$#journal Eur. J. Immunol. (1992) 22:235-239 !$#title Cloning and expression of an inducible lymphoid-specific, !1protein tyrosine phosphatase (HePTPase). !$#cross-references MUID:92111631; PMID:1530918 !$#accession A46541 !'##molecule_type mRNA !'##residues 22-234,'HV',237-336,'A',338-360 ##label ZAN !'##cross-references GB:M64322; NID:g187227; PIDN:AAA59531.1; !1PID:g187228 !'##experimental_source PWM-stimulated peripheral T lymphocytes !'##note sequence extracted from NCBI backbone (NCBIN:79322, !1NCBIP:79323) REFERENCE A44929 !$#authors Adachi, M.; Sekiya, M.; Arimura, Y.; Takekawa, M.; Itoh, F.; !1Hinoda, Y.; Imai, K.; Yachi, A. !$#journal Cancer Res. (1992) 52:737-740 !$#title Protein-tyrosine phosphatase expression in pre-B cell !1NALM-6. !$#cross-references MUID:92119637; PMID:1370651 !$#accession D44929 !'##molecule_type mRNA !'##residues 'Q',207-292 ##label AD3 !'##cross-references GB:S78090; NID:g243549; PIDN:AAB21149.1; !1PID:g243550 !'##experimental_source pre-B cell NALM-6 !'##note the authors translated the codon CTG for residue 245 as Arg, !1CTG for residue 246 as Ser, CGC for residue 247 as Val, CTA !1for residue 248 as Lys, and GTG for residue 249 as His; the !1sequence shown follows the authors' translation !'##note sequence extracted from NCBI backbone (NCBIP:78091) REFERENCE A46752 !$#authors Adachi, M.; Sekiya, M.; Arimura, Y.; Takekawa, M.; Itoh, F.; !1Hinoda, Y.; Imai, K.; Yachi, A. !$#submission submitted to GenBank, May 1992 !$#accession A46752 !'##molecule_type mRNA !'##residues 'Q',207-244,'LLRLV',250-291 ##label AD2 !'##cross-references GB:S78090 !'##note sequence extracted from NCBI backbone (NCBIN:78090) COMMENT This enzyme is expressed only in hematopoietic cells and may !1play a role in the regulation of T and B lympocyte !1development and signal transduction. GENETICS !$#gene GDB:PTPN7 !'##cross-references GDB:135507; OMIM:176889 !$#map_position 1q32.1-1q32.1 CLASSIFICATION #superfamily protein-tyrosine-phosphatase, nonreceptor type !15; protein-tyrosine-phosphatase homology KEYWORDS phosphoprotein; phosphoric monoester hydrolase; !1tyrosine-specific phosphatase FEATURE !$119-339 #domain protein-tyrosine-phosphatase homology #label !8PTP\ !$291 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$297 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 360 #molecular-weight 40573 #checksum 9548 SEQUENCE /// ENTRY S20825 #type complete TITLE protein-tyrosine-phosphatase (EC 3.1.3.48) PTPN6, nonreceptor type 6 [validated] - human ALTERNATE_NAMES hematopoietic cell phosphatase HCP; protein-tyrosine-phosphatase 1C; protein-tyrosine-phosphatase SHP-1; PTP1C; PTPTY42; SHPTP-1; tyrosine phosphatase hSH-PTP1 ORGANISM #formal_name Homo sapiens #common_name man DATE 19-May-1994 #sequence_revision 08-Feb-1996 #text_change 21-Jun-2002 ACCESSIONS B42031; A38189; S20825; S17234; S20837 REFERENCE A42031 !$#authors Yi, T.L.; Cleveland, J.L.; Ihle, J.N. !$#journal Mol. Cell. Biol. (1992) 12:836-846 !$#title Protein tyrosine phosphatase containing SH2 domains: !1characterization, preferential expression in hematopoietic !1cells, and localization to human chromosome 12p12-p13. !$#cross-references MUID:92123209; PMID:1732748 !$#accession B42031 !'##molecule_type mRNA !'##residues 1-595 ##label YI1 !'##cross-references GB:M74093 !'##experimental_source T-lymphoid cell line !'##note sequence extracted from GenBank REFERENCE A38189 !$#authors Plutzky, J.; Neel, B.G.; Rosenberg, R.D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:1123-1127 !$#title Isolation of a src homology 2-containing tyrosine !1phosphatase. !$#cross-references MUID:92141214; PMID:1736296 !$#accession A38189 !'##molecule_type mRNA !'##residues 1-85,'V',87-595 ##label PLU !'##cross-references GB:M77273; NID:g338079; PIDN:AAA36610.1; !1PID:g338080 !'##note sequence extracted from NCBI backbone (NCBIN:79619, !1NCBIP:79620) REFERENCE S20825 !$#authors Shen, S.H.; Bastien, L.; Posner, B.I.; Chretien, P. !$#journal Nature (1991) 353:868 !$#title Corrigendum: A protein-tyrosine phosphatase with sequence !1similarity to the SH2 domain of the protein-tyrosine !1kinases. !$#accession S20825 !'##molecule_type mRNA !'##residues 1,'LSRG',4-595 ##label SHE !'##cross-references EMBL:X62055; NID:g35781; PIDN:CAA43982.1; !1PID:g35782 REFERENCE S17234 !$#authors Shen, S.H.; Bastien, L.; Posner, B.I.; Chretien, P. !$#journal Nature (1991) 352:736-739 !$#title A protein-tyrosine phosphatase with sequence similarity to !1the SH2 domain of the protein-tyrosine kinases. !$#cross-references MUID:91343005; PMID:1652101 !$#accession S17234 !'##molecule_type mRNA !'##residues 1,'LSRG',4-589,'VPSRGSERCCPQVAMPQP' ##label SH2 !'##experimental_source breast carcinoma cells !'##note sequence revised in reference S20805 GENETICS !$#gene GDB:PTPN6 !'##cross-references GDB:131389; OMIM:176883 !$#map_position 12p13-12p13 CLASSIFICATION #superfamily protein-tyrosine-phosphatase, nonreceptor type !16; protein-tyrosine-phosphatase homology; SH2 homology KEYWORDS phosphoprotein; phosphoric monoester hydrolase; !1tyrosine-specific phosphatase FEATURE !$4-98 #domain SH2 homology #label SH2A\ !$110-211 #domain SH2 homology #label SH2B\ !$265-521 #domain phosphatase catalytic domain #status !8predicted #label PHP\ !$270-504 #domain protein-tyrosine-phosphatase homology #label !8PTP\ !$453 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$459 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 595 #molecular-weight 67561 #checksum 4607 SEQUENCE /// ENTRY A53593 #type complete TITLE protein-tyrosine-phosphatase (EC 3.1.3.48), nonreceptor type 11 - rat ALTERNATE_NAMES PTPase L1 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A53593; S29281 REFERENCE A53593 !$#authors Mei, L.; Doherty, C.A.; Huganir, R.L. !$#journal J. Biol. Chem. (1994) 269:12254-12262 !$#title RNA splicing regulates the activity of a SH2 !1domain-containing protein tyrosine phosphatase. !$#cross-references MUID:94216346; PMID:7512964 !$#accession A53593 !'##status preliminary !'##molecule_type mRNA !'##residues 1-597 ##label MEI !'##cross-references GB:U05963; NID:g458332; PIDN:AAA19133.1; !1PID:g458333 REFERENCE S29281 !$#authors Hiraga, A.; Munakata, H.; Hata, K.; Suzuki, Y.; Tsuiki, S. !$#journal Eur. J. Biochem. (1992) 209:195-206 !$#title Purification and characterization of a rat liver !1protein-tyrosine phosphatase with sequence similarity to !1src-homology region 2. !$#cross-references MUID:93011127; PMID:1382983 !$#accession S29281 !'##molecule_type protein !'##residues 24-31;36-54;56-89;100-103,'X',105-108;'X', !1113-120;132-155;179-198;214-233;245-258;281-314;315, !1380-402;'VG',412-419,'X',421-426,'X',428-429,'X', !1431-433;497-531,'X',533-535 ##label HIR CLASSIFICATION #superfamily protein-tyrosine-phosphatase, nonreceptor type !16; protein-tyrosine-phosphatase homology; SH2 homology KEYWORDS alternative splicing; phosphoprotein; phosphoric monoester !1hydrolase; tyrosine-specific phosphatase FEATURE !$6-100 #domain SH2 homology #label SH2A\ !$112-214 #domain SH2 homology #label SH2B\ !$273-514 #domain protein-tyrosine-phosphatase homology #label !8PTP\ !$463 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$469 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 597 #molecular-weight 68382 #checksum 9262 SEQUENCE /// ENTRY A44390 #type complete TITLE protein-tyrosine-phosphatase (EC 3.1.3.48), nonreceptor type 6 - mouse ALTERNATE_NAMES hematopoietic cell phosphatase (HCP); protein-tyrosine-phosphatase 1C (PTP1C); protein-tyrosine-phosphatase SHP-1 (SHPTP-1); PTPTY42 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 03-May-1994 #sequence_revision 19-May-1994 #text_change 11-Jun-1999 ACCESSIONS A44390; A42031; F61180; I65741; I52816; I65740; A45143; !1B45143 REFERENCE A44390 !$#authors Matthews, R.J.; Bowne, D.B.; Flores, E.; Thomas, M.L. !$#journal Mol. Cell. Biol. (1992) 12:2396-2405 !$#title Characterization of hematopoietic intracellular protein !1tyrosine phosphatases: description of a phosphatase !1containing an SH2 domain and another enriched in proline-, !1glutamic acid-, serine-, and threonine-rich sequences. !$#cross-references MUID:92236615; PMID:1373816 !$#accession A44390 !'##molecule_type mRNA !'##residues 1-595 ##label MAT !'##cross-references GB:M90389; NID:g200550; PIDN:AAA40007.1; !1PID:g200551 REFERENCE A42031 !$#authors Yi, T.L.; Cleveland, J.L.; Ihle, J.N. !$#journal Mol. Cell. Biol. (1992) 12:836-846 !$#title Protein tyrosine phosphatase containing SH2 domains: !1characterization, preferential expression in hematopoietic !1cells, and localization to human chromosome 12p12-p13. !$#cross-references MUID:92123209; PMID:1732748 !$#accession A42031 !'##molecule_type mRNA !'##residues 1-595 ##label YI1 !'##cross-references GB:M68902; NID:g193807 !'##note sequence extracted from NCBI backbone (NCBIN:76845, !1NCBIP:76846) REFERENCE A61180 !$#authors Yi, T.; Cleveland, J.L.; Ihle, J.N. !$#journal Blood (1991) 78:2222-2228 !$#title Identification of novel protein tyrosine phosphatases of !1hematopoietic cells by polymerase chain reaction !1amplification. !$#cross-references MUID:92032882; PMID:1932742 !$#accession F61180 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 342-451 ##label YIA REFERENCE I52816 !$#authors Shultz, L.D.; Schweitzer, P.A.; Rajan, T.V.; Yi, T.; Ihle, !1J.N.; Matthews, R.J.; Thomas, M.L.; Beier, D.R. !$#journal Cell (1993) 73:1445-1454 !$#title Mutations at the murine motheaten locus are within the !1hematopoietic cell protein-tyrosine phosphatase (Hcph) gene. !$#cross-references MUID:93313972; PMID:8324828 !$#accession I65741 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 334-353,359-382 ##label SHU1 !'##cross-references GB:S63803; NID:g388449 !'##note deletion mutation !$#accession I52816 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 350-358,'EGQSPNFLTPTFSSLVLVQYHTQ',359-366 ##label SHU2 !'##cross-references GB:S63763; NID:g388447 !'##note insertion mutation !$#accession I65740 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 34-76,'VPRPHIWRAGGVTAAGQGRALD' ##label SHU3 !'##cross-references GB:S63764; NID:g388450 !'##note frameshift mutation REFERENCE A45143 !$#authors Yeung, Y.G.; Berg, K.L.; Pixley, F.J.; Angeletti, R.H.; !1Stanley, E.R. !$#journal J. Biol. Chem. (1992) 267:23447-23450 !$#title Protein tyrosine phosphatase-1C is rapidly phosphorylated in !1tyrosine in macrophages in response to colony stimulating !1factor-1. !$#cross-references MUID:93054686; PMID:1385421 !$#accession A45143 !'##status preliminary !'##molecule_type protein !'##residues 137-139,'X',141-143,'X',145-151 ##label YEU !'##experimental_source BAC1.2F5 macrophage !'##note sequence extracted from NCBI backbone (NCBIP:118519) !$#accession B45143 !'##status preliminary !'##molecule_type protein !'##residues 54-56,'X',58,'X',60-61,'X',63-68 ##label YE2 !'##experimental_source BAC1.2F5 macrophage !'##note sequence extracted from NCBI backbone (NCBIP:118518) COMMENT This protein is found primarily in hematopoietic tissues. GENETICS !$#gene me/HCPH; motheaten FUNCTION !$#description catalyzes hydrolysis of peptidyl-phosphotyrosine to release !1phosphate CLASSIFICATION #superfamily protein-tyrosine-phosphatase, nonreceptor type !16; protein-tyrosine-phosphatase homology; SH2 homology KEYWORDS phosphoprotein; phosphoric monoester hydrolase; !1tyrosine-specific phosphatase FEATURE !$4-98 #domain SH2 homology #label SH2A\ !$110-211 #domain SH2 homology #label SH2B\ !$265-521 #domain phosphatase catalytic domain #status !8predicted #label PHP\ !$270-504 #domain protein-tyrosine-phosphatase homology #label !8PTP\ !$453 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$459 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 595 #molecular-weight 67559 #checksum 6889 SEQUENCE /// ENTRY JN0805 #type complete TITLE protein-tyrosine-phosphatase (EC 3.1.3.48) PTPN11, nonreceptor type 11 [validated] - human ALTERNATE_NAMES BPTP-3; protein-tyrosine-phosphatase SHP-2; PTP1D; PTP2C; SH-PTP2; SH-PTP3 ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Mar-1994 #sequence_revision 19-May-1994 #text_change 21-Jun-2002 ACCESSIONS JN0805; A46210; A47386; A47244; S27398; C44929; S31767 REFERENCE JN0805 !$#authors Bastien, L.; Ramachandran, C.; Liu, S.; Adam, M. !$#journal Biochem. Biophys. Res. Commun. (1993) 196:124-133 !$#title Cloning, expression and mutational analysis of SH-PTP2, !1human protein-tyrosine phosphatase. !$#cross-references MUID:94029983; PMID:8216283 !$#accession JN0805 !'##molecule_type mRNA !'##residues 1-593 ##label BAS !'##cross-references GB:L07527; NID:g292406; PIDN:AAA17022.1; !1PID:g292407 REFERENCE A46210 !$#authors Vogel, W.; Lammers, R.; Huang, J.; Ullrich, A. !$#journal Science (1993) 259:1611-1614 !$#title Activation of a phosphotyrosine phosphatase by tyrosine !1phosphorylation. !$#cross-references MUID:93206095; PMID:7681217 !$#accession A46210 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-593 ##label VOG !'##cross-references EMBL:X70766; NID:g35783; PIDN:CAA50045.1; !1PID:g35784 !'##experimental_source SK-BR-3 mammary carcinoma cells !'##note sequence extracted from NCBI backbone (NCBIP:127775) REFERENCE A47386 !$#authors Ahmad, S.; Banville, D.; Zhao, Z.; Fischer, E.H.; Shen, S.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:2197-2201 !$#title A widely expressed human protein-tyrosine phosphatase !1containing src homology 2 domains. !$#cross-references MUID:93211929; PMID:7681589 !$#accession A47386 !'##molecule_type mRNA !'##residues 1-593 ##label AHM !'##experimental_source umbilical cord !'##note sequence extracted from NCBI backbone (NCBIN:128129, !1NCBIP:128131) REFERENCE A47244 !$#authors Freeman Jr., R.M.; Plutzky, J.; Neel, B.G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:11239-11243 !$#title Identification of a human src homology 2-containing !1protein-tyrosine-phosphatase: a putative homolog of !1Drosophila corkscrew. !$#cross-references MUID:93087502; PMID:1280823 !$#accession A47244 !'##molecule_type mRNA !'##residues 1-593 ##label FRE !'##cross-references GB:L03535; NID:g338081; PIDN:AAA36611.1; !1PID:g338082 !'##note sequence extracted from NCBI backbone (NCBIN:119760, !1NCBIP:119761) REFERENCE S27398 !$#authors Adachi, M.; Sekiya, M.; Miyachi, T.; Matsuno, K.; Hinoda, !1Y.; Imai, K.; Yachi, A. !$#journal FEBS Lett. (1992) 314:335-339 !$#title Molecular cloning of a novel protein-tyrosine phosphatase !1SH-PTP3 with sequence similarity to the src-homology region !12. !$#cross-references MUID:93106179; PMID:1281790 !$#accession S27398 !'##molecule_type mRNA !'##residues 1-534,'R',536-547,'P',549-593 ##label AD2 !'##cross-references DDBJ:D13540; NID:g220071; PIDN:BAA02740.2; !1PID:g4519425 REFERENCE A44929 !$#authors Adachi, M.; Sekiya, M.; Arimura, Y.; Takekawa, M.; Itoh, F.; !1Hinoda, Y.; Imai, K.; Yachi, A. !$#journal Cancer Res. (1992) 52:737-740 !$#title Protein-tyrosine phosphatase expression in pre-B cell !1NALM-6. !$#cross-references MUID:92119637; PMID:1370651 !$#accession C44929 !'##molecule_type mRNA !'##residues 'Q',370-460 ##label ADA !'##cross-references GB:S78088; NID:g243547; PIDN:AAB21148.1; !1PID:g243548 !'##experimental_source pre-B cell NALM-6 !'##note sequence extracted from NCBI backbone (NCBIN:78088, !1NCBIP:78089) !'##note the authors did not report the entire codon for residue 92 COMMENT This ubiquitous enzyme plays a critical role in regulating !1physiological cellular processes and catalyzes !1dephosphorylation of phosphotyrosyl residues. GENETICS !$#gene GDB:PTPN11 !'##cross-references GDB:137093; OMIM:176876 !$#map_position 12q24.1-12q24.1 CLASSIFICATION #superfamily protein-tyrosine-phosphatase, nonreceptor type !16; protein-tyrosine-phosphatase homology; SH2 homology KEYWORDS phosphoprotein; phosphoric monoester hydrolase; !1tyrosine-specific phosphatase FEATURE !$6-100 #domain SH2 homology #label SH2A\ !$112-214 #domain SH2 homology #label SH2B\ !$273-510 #domain protein-tyrosine-phosphatase homology #label !8PTP\ !$459 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$465 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 593 #molecular-weight 68010 #checksum 853 SEQUENCE /// ENTRY A55651 #type complete TITLE protein-tyrosine-phosphatase (EC 3.1.3.48), nonreceptor type 11 - African clawed frog ALTERNATE_NAMES SH-PTP2 ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A55651 REFERENCE A55651 !$#authors Tang, T.L.; Freeman Jr., R.M.; O'Reilly, A.M.; Neel, B.G.; !1Sokol, S.Y. !$#journal Cell (1995) 80:473-483 !$#title The SH2-containing protein-tyrosine phosphatase SH-PTP2 is !1required upstream of MAP kinase for early Xenopus !1development. !$#cross-references MUID:95163101; PMID:7859288 !$#accession A55651 !'##status preliminary !'##molecule_type mRNA !'##residues 1-595 ##label TAN !'##cross-references GB:U15287; NID:g601781; PIDN:AAA65731.1; !1PID:g601782 CLASSIFICATION #superfamily protein-tyrosine-phosphatase, nonreceptor type !16; protein-tyrosine-phosphatase homology; SH2 homology KEYWORDS phosphoprotein; phosphoric monoester hydrolase; !1tyrosine-specific phosphatase FEATURE !$6-100 #domain SH2 homology #label SH2A\ !$112-214 #domain SH2 homology #label SH2B\ !$273-510 #domain protein-tyrosine-phosphatase homology #label !8PTP\ !$459 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$465 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 595 #molecular-weight 68249 #checksum 4037 SEQUENCE /// ENTRY B44390 #type complete TITLE protein-tyrosine-phosphatase (EC 3.1.3.48) PEP, nonreceptor type 8 - mouse ALTERNATE_NAMES protein-tyrosine-phosphatase PEP ORGANISM #formal_name Mus musculus #common_name house mouse DATE 03-May-1994 #sequence_revision 26-May-1994 #text_change 11-Jun-1999 ACCESSIONS B44390; S71952; S27876 REFERENCE A44390 !$#authors Matthews, R.J.; Bowne, D.B.; Flores, E.; Thomas, M.L. !$#journal Mol. Cell. Biol. (1992) 12:2396-2405 !$#title Characterization of hematopoietic intracellular protein !1tyrosine phosphatases: description of a phosphatase !1containing an SH2 domain and another enriched in proline-, !1glutamic acid-, serine-, and threonine-rich sequences. !$#cross-references MUID:92236615; PMID:1373816 !$#accession B44390 !'##molecule_type mRNA !'##residues 1-802 ##label MAT !'##cross-references GB:M90388; NID:g200522; PIDN:AAA39994.1; !1PID:g200523 REFERENCE S71952 !$#authors Cloutier, J.F.; Veillette, A. !$#journal EMBO J. (1996) 15:4909-4918 !$#title Association of inhibitory tyrosine protein kinase p50(csk) !1with protein tyrosine phosphatase PEP in T cells and other !1hemopoietic cells. !$#cross-references MUID:97045099; PMID:8890164 !$#accession S71952 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type mRNA !'##residues 495-789 ##label CLO COMMENT This protein is found primarily in hematopoietic tissues. GENETICS !$#gene 70zpep COMPLEX physically associates with inhibitory tyrosine protein !1kinase Csk; interaction is mediated by the Csk SH3 domain !1and by two proline-rich motifs present in the C-terminal !1region of PEP FUNCTION !$#description probably an effector and/or regulator of tyrosine protein !1kinase csk in T-cells and other hematopoietic cells; !1dephosphorylation of O-phosphotyrosine in phosphoproteins CLASSIFICATION #superfamily protein-tyrosine-phosphatase, nonreceptor type !18; protein-tyrosine-phosphatase homology KEYWORDS phosphoprotein; phosphoric monoester hydrolase; !1tyrosine-specific phosphatase FEATURE !$54-278 #domain protein-tyrosine-phosphatase homology #label !8PTP\ !$497-802 #region glutamic acid/proline/serine/threonine-rich\ !$613-621 #region proline-rich\ !$688-695 #region proline-rich\ !$227 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$233 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 802 #molecular-weight 89713 #checksum 9030 SEQUENCE /// ENTRY A42690 #type complete TITLE protein-tyrosine-phosphatase (EC 3.1.3.48), nonreceptor type 9 - human ALTERNATE_NAMES PTPase MEG2 ORGANISM #formal_name Homo sapiens #common_name man DATE 03-May-1994 #sequence_revision 26-May-1994 #text_change 11-Jun-1999 ACCESSIONS A42690 REFERENCE A42690 !$#authors Gu, M.; Warshawsky, I.; Majerus, P.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:2980-2984 !$#title Cloning and expression of a cytosolic megakaryocyte !1protein-tyrosine-phosphatase with sequence homology to !1retinaldehyde-binding protein and yeast SEC14p. !$#cross-references MUID:92212952; PMID:1557404 !$#accession A42690 !'##molecule_type mRNA !'##residues 1-593 ##label GUA !'##cross-references GB:M83738; NID:g190745; PIDN:AAA60226.1; !1PID:g190746 GENETICS !$#gene GDB:PTPN9 !'##cross-references GDB:132399 !$#map_position 1q32.1-1q32.1 CLASSIFICATION #superfamily protein-tyrosine-phosphatase, nonreceptor type !19; cellular retinaldehyde-binding protein homology; !1protein-tyrosine-phosphatase homology KEYWORDS phosphoprotein; phosphoric monoester hydrolase; !1tyrosine-specific phosphatase FEATURE !$48-237 #domain cellular retinaldehyde-binding protein !8homology #label CRB\ !$327-563 #domain protein-tyrosine-phosphatase homology #label !8PTP\ !$515 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$521 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 593 #molecular-weight 68020 #checksum 2459 SEQUENCE /// ENTRY JC1368 #type complete TITLE protein-tyrosine-phosphatase (EC 3.1.3.48) PTPN12, nonreceptor type 12 [validated] - human ALTERNATE_NAMES PTP-PEST; PTPG1 ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1993 #sequence_revision 01-Mar-1996 #text_change 21-Jun-2002 ACCESSIONS JC1368; A47506; A45496; S41746 REFERENCE JC1368 !$#authors Takekawa, M.; Itoh, F.; Hinoda, Y.; Arimura, Y.; Toyota, M.; !1Sekiya, M.; Adachi, M.; Imai, K.; Yachi, A. !$#journal Biochem. Biophys. Res. Commun. (1992) 189:1223-1230 !$#title Cloning and characterization of a human cDNA encoding a !1novel putative cytoplasmic protein-tyrosine-phosphatase. !$#cross-references MUID:93112015; PMID:1472029 !$#accession JC1368 !'##molecule_type mRNA !'##residues 1-780 ##label TAK !'##cross-references DDBJ:D13380; NID:g220033; PIDN:BAA02648.1; !1PID:g220034 !'##note the authors translated the codon AGT for residue 636 as Ala REFERENCE A47506 !$#authors Yang, Q.; Co, D.; Sommercorn, J.; Tonks, N.K. !$#journal J. Biol. Chem. (1993) 268:17650 !$#cross-references MUID:93352561; PMID:8349645 !$#contents erratum !$#accession A47506 !'##molecule_type mRNA !'##residues 1-120,'I',122-321,'I',323-780 ##label YAN !'##cross-references EMBL:M93425; NID:g292408; PIDN:AAA36529.1; !1PID:g292409 REFERENCE A45496 !$#authors Yang, Q.; Co, D.; Sommercorn, J.; Tonks, N.K. !$#journal J. Biol. Chem. (1993) 268:6622-6628 !$#title Cloning and expression of PTP-PEST. A novel, human, !1nontransmembrane protein tyrosine phosphatase. !$#cross-references MUID:93203262; PMID:8454633 !$#accession A45496 !'##molecule_type mRNA !'##residues 1-120,'I',122-321,'I',323-494,518-525,'FLLMRKDM' ##label !1YA2 !'##note sequence extracted from NCBI backbone (NCBIN:127945, !1NCBIP:127946) !'##note sequence has been revised in reference A47506 REFERENCE S41746 !$#authors Takekawa, M.; Itoh, F.; Hinoda, Y.; Adachi, M.; Ariyama, T.; !1Inazawa, J.; Imai, K.; Yachi, A. !$#journal FEBS Lett. (1994) 339:222-228 !$#title Chromosomal localization of the protein tyrosine phosphatase !1G1 gene and characterization of the aberrant transcripts in !1human colon cancer cells. !$#cross-references MUID:94156037; PMID:7509295 !$#accession S41746 !'##molecule_type mRNA !'##residues 59-127,'YY',130-134,'TE' ##label TA2 !'##note sequence shown is wild type COMMENT PEST sequences in this widely expressed protein suggest that !1it is rapidly degraded. The sequence also contains a number !1of potential phosphorylation sites. GENETICS !$#gene GDB:PTPN12 !'##cross-references GDB:136846; OMIM:600079 !$#map_position 7q11.23-7q11.23 CLASSIFICATION #superfamily protein-tyrosine-phosphatase, nonreceptor type !112; protein-tyrosine-phosphatase homology KEYWORDS phosphoprotein; phosphoric monoester hydrolase; !1tyrosine-specific phosphatase FEATURE !$58-282 #domain protein-tyrosine-phosphatase homology #label !8PTP\ !$231 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$237 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 780 #molecular-weight 88092 #checksum 9950 SEQUENCE /// ENTRY S48748 #type complete TITLE protein-tyrosine-phosphatase (EC 3.1.3.48), probable nonreceptor type 12 splice form - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S48748 REFERENCE S48748 !$#authors Moriyama, T.; Kawanishi, S.; Inoue, T.; Imai, E.; Kaneko, !1T.; Xia, C.; Takenaka, M.; Noguchi, T.; Kamada, T.; Ueda, N. !$#journal FEBS Lett. (1994) 353:305-308 !$#title cDNA cloning of a cytosolic protein tyrosine phosphatase !1(RKPTP) from rat kidney. !$#cross-references MUID:95046282; PMID:7957881 !$#accession S48748 !'##molecule_type mRNA !'##residues 1-382 ##label MOR !'##cross-references GB:D38072; NID:g567262; PIDN:BAA07266.1; !1PID:g699627 CLASSIFICATION #superfamily protein-tyrosine-phosphatase, nonreceptor type !112; protein-tyrosine-phosphatase homology KEYWORDS phosphoprotein; phosphoric monoester hydrolase; !1tyrosine-specific phosphatase FEATURE !$58-282 #domain protein-tyrosine-phosphatase homology #label !8PTP\ !$231 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$237 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 382 #molecular-weight 44438 #checksum 3306 SEQUENCE /// ENTRY JH0609 #type complete TITLE protein-tyrosine-phosphatase (EC 3.1.3.48) P19 - mouse ALTERNATE_NAMES protein-tyrosine-phosphatase PTPTY43 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JH0609; PS0365; PS0369; PS0366; G61180 REFERENCE JH0609 !$#authors den Hertog, J.; Pals, C.E.G.M.; Jonk, L.J.C.; Kruijer, W. !$#journal Biochem. Biophys. Res. Commun. (1992) 184:1241-1249 !$#title Differential expression of a novel murine non-receptor !1protein tyrosine phosphatase during differentiation of P19 !1embryonal carcinoma cells. !$#cross-references MUID:92272714; PMID:1590786 !$#accession JH0609 !'##molecule_type mRNA !'##residues 1-773 ##label DEN !'##cross-references GB:X63440; GB:S36169; NID:g416181; PIDN:CAA45037.1; !1PID:g416182 !'##experimental_source embryonic carcinoma cell, P19 cell !$#accession PS0365 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 88-91,'G',93-110,'G',112-118,'S',120,'T',122 ##label DE2 !'##experimental_source embryonic carcinoma cell, P19 cell, clone PTP33 !$#accession PS0369 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 88-91,'G',93-109,'LG',112-120,'T',122 ##label DE3 !'##experimental_source embryonic carcinoma cell, P19 cell, clone PTP59 !$#accession PS0366 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 88-91,'KY',94-109,'LA',112-118,'S',120-122 ##label DE4 !'##experimental_source embryonic carcinoma cell, P19 cell, clone PTP42 REFERENCE A61180 !$#authors Yi, T.; Cleveland, J.L.; Ihle, J.N. !$#journal Blood (1991) 78:2222-2228 !$#title Identification of novel protein tyrosine phosphatases of !1hematopoietic cells by polymerase chain reaction !1amplification. !$#cross-references MUID:92032882; PMID:1932742 !$#accession G61180 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 124-127,'I',129-229 ##label YIA COMMENT This protein is a located in the cytoplasm. CLASSIFICATION #superfamily protein-tyrosine-phosphatase, nonreceptor type !112; protein-tyrosine-phosphatase homology KEYWORDS phosphoprotein; phosphoric monoester hydrolase; !1tyrosine-specific phosphatase FEATURE !$55-299 #domain phosphatase catalytic domain #status !8predicted #label PCD\ !$58-282 #domain protein-tyrosine-phosphatase homology #label !8PTP\ !$231 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$237 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 773 #molecular-weight 86608 #checksum 3345 SEQUENCE /// ENTRY A54971 #type complete TITLE protein-tyrosine-phosphatase (EC 3.1.3.48) PTPN13, nonreceptor type 13, splice form 1 [validated] - human ALTERNATE_NAMES Fas-associated phosphatase FAP-1; protein-tyrosine-phosphatase hPTP1E; protein-tyrosine-phosphatase PTPL1 ORGANISM #formal_name Homo sapiens #common_name man DATE 11-Nov-1994 #sequence_revision 08-Feb-1996 #text_change 21-Jun-2002 ACCESSIONS A54971; A55114; I59595; I53483; S46955 REFERENCE A54971 !$#authors Banville, D.; Ahmad, S.; Stocco, R.; Shen, S.H. !$#journal J. Biol. Chem. (1994) 269:22320-22327 !$#title A novel protein-tyrosine phosphatase with homology to both !1the cytoskeletal proteins of the band 4.1 family and !1junction-associated guanylate kinases. !$#cross-references MUID:94350988; PMID:8071359 !$#accession A54971 !'##molecule_type mRNA !'##residues 1-2490 ##label BAN !'##cross-references GB:U12128 !'##note sequence shown follows authors' translation at positions 62-63 REFERENCE A55114 !$#authors Saras, J.; Claesson-Welsh, L.; Heldin, C.H.; Gonez, L.J. !$#journal J. Biol. Chem. (1994) 269:24082-24089 !$#title Cloning and characterization of PTPL1, a protein tyrosine !1phosphatase with similarities to cytoskeletal-associated !1proteins. !$#cross-references MUID:95014139; PMID:7929060 !$#accession A55114 !'##molecule_type mRNA !'##residues 1-61,'GS',64-839,'D',841-1055,1075-1133,'FH',1136-1210,'I', !11212-1383,1389-1542,'A',1544-1801,'A',1803-2299,'QM', !12302-2490 ##label SAR !'##cross-references GB:X80289; NID:g515030; PIDN:CAA56563.1; !1PID:g515031 REFERENCE I59595 !$#authors Sato, T.; Irie, S.; Kitada, S.; Reed, J.C. !$#journal Science (1995) 268:411-415 !$#title FAP-1: a protein tyrosine phosphatase that associates with !1Fas. !$#cross-references MUID:95232528; PMID:7536343 !$#accession I59595 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1279-1888 ##label RES !'##cross-references GB:L34583; NID:g806291; PIDN:AAC41755.1; !1PID:g806292 REFERENCE I53483 !$#authors Maekawa, K.; Imagawa, N.; Nagamatsu, M.; Harada, S. !$#journal FEBS Lett. (1994) 337:200-206 !$#title Molecular cloning of a novel protein-tyrosine phosphatase !1containing a membrane-binding domain and GLGF repeats. !$#cross-references MUID:94116679; PMID:8287977 !$#accession I53483 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-61,'GS',64-839,'D',841-1210,'I',1212-1383,1389-2299,'QM', !12302-2490 ##label RE2 !'##cross-references GB:D21209; NID:g452189; PIDN:BAA04750.1; !1PID:g452190 GENETICS !$#gene GDB:PTPN13 !'##cross-references GDB:306348; OMIM:600267 !$#map_position 4q21.3-4q21.3 CLASSIFICATION #superfamily protein-tyrosine-phosphatase, nonreceptor type !113; GLGF domain homology; protein 4.1 membrane-binding !1domain homology; protein-tyrosine-phosphatase homology KEYWORDS alternative splicing; phosphoprotein; phosphoric monoester !1hydrolase; tyrosine-specific phosphatase FEATURE !$574-868 #domain protein 4.1 membrane-binding domain homology !8#label B41\ !$1099-1175 #domain GLGF domain homology #label GLG1\ !$1373-1454 #domain GLGF domain homology #label GLG2\ !$1511-1590 #domain GLGF domain homology #label GLG3\ !$1799-1870 #domain GLGF domain homology #label GLG4\ !$1893-1967 #domain GLGF domain homology #label GLG5\ !$2242-2461 #domain protein-tyrosine-phosphatase homology #label !8PTP1\ !$2413 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$2419 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 2490 #molecular-weight 277568 #checksum 9288 SEQUENCE /// ENTRY JC4155 #type complete TITLE protein-tyrosine-phosphatase (EC 3.1.3.48), nonreceptor type 14 - human ALTERNATE_NAMES PEZ protein; protein-tyrosine-phosphatase/ezrin-like protein ORGANISM #formal_name Homo sapiens #common_name man DATE 27-Aug-1995 #sequence_revision 23-Feb-1996 #text_change 21-Jul-2000 ACCESSIONS JC4155 REFERENCE JC4155 !$#authors Smith, A.L.; Mitchell, P.J.; Shipley, J.; Gusterson, B.A.; !1Rogers, M.V.; Crompton, M.R. !$#journal Biochem. Biophys. Res. Commun. (1995) 209:959-965 !$#title PEZ:a novel human cDNA encoding protein tyrosine !1phosphatase-and ezrin-like domains. !$#cross-references MUID:95251727; PMID:7733990 !$#accession JC4155 !'##molecule_type mRNA !'##residues 1-1187 ##label SMI !'##cross-references EMBL:X82676; NID:g3929753; PIDN:CAA57993.1; !1PID:g809029 !'##experimental_source breast GENETICS !$#gene GDB:PTPN14 !'##cross-references GDB:454485 !$#map_position 1q32.2-1q32.2 CLASSIFICATION #superfamily protein-tyrosine-phosphatase, nonreceptor type !114; protein 4.1 membrane-binding domain homology; !1protein-tyrosine-phosphatase homology KEYWORDS phosphoprotein; phosphoric monoester hydrolase; !1tyrosine-specific phosphatase FEATURE !$23-302 #domain protein 4.1 membrane-binding domain homology !8#label B41\ !$566-575 #region proline-rich\ !$709-716 #region acidic\ !$933-1169 #domain protein-tyrosine-phosphatase homology #label !8PTP2\ !$1121 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$1127 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 1187 #molecular-weight 135238 #checksum 5184 SEQUENCE /// ENTRY JC2366 #type complete TITLE protein-tyrosine-phosphatase (EC 3.1.3.48), nonreceptor type 14 - mouse ALTERNATE_NAMES PEZ protein; protein-tyrosine-phosphatase PTP36; protein-tyrosine-phosphatase/ezrin-like protein ORGANISM #formal_name Mus musculus #common_name house mouse DATE 24-Feb-1995 #sequence_revision 23-Feb-1996 #text_change 21-Jul-2000 ACCESSIONS JC2366 REFERENCE JC2366 !$#authors Sawada, M.; Ogata, M.; Fujino, Y.; Hamaoka, T. !$#journal Biochem. Biophys. Res. Commun. (1994) 203:479-484 !$#title cDNA cloning of a novel protein tyrosine phosphatase with !1homology to cytoskeletal protein 4.1 and its expression in !1T-lineage cells. !$#cross-references MUID:94354845; PMID:8074693 !$#accession JC2366 !'##molecule_type mRNA !'##residues 1-1189 ##label SAW !'##cross-references GB:D31842; NID:g507330; PIDN:BAA06628.1; !1PID:g507331 !'##experimental_source thymus CLASSIFICATION #superfamily protein-tyrosine-phosphatase, nonreceptor type !114; protein 4.1 membrane-binding domain homology; !1protein-tyrosine-phosphatase homology KEYWORDS phosphoprotein; phosphoric monoester hydrolase; !1tyrosine-specific phosphatase FEATURE !$23-302 #domain protein 4.1 membrane-binding domain homology !8#label B41\ !$566-575 #region proline-rich\ !$712-718 #region acidic\ !$935-1171 #domain protein-tyrosine-phosphatase homology #label !8PTP2\ !$1123 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$1129 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 1189 #molecular-weight 135030 #checksum 3322 SEQUENCE /// ENTRY A44267 #type complete TITLE protein-tyrosine-phosphatase (EC 3.1.3.48), nonreceptor type 1 - slime mold (Dictyostelium discoideum) ORGANISM #formal_name Dictyostelium discoideum DATE 30-Apr-1993 #sequence_revision 08-Mar-1996 #text_change 24-Apr-1998 ACCESSIONS A44267 REFERENCE A44267 !$#authors Howard, P.K.; Sefton, B.M.; Firtel, R.A. !$#journal Cell (1992) 71:637-647 !$#title Analysis of a spatially regulated phosphotyrosine !1phosphatase identifies tyrosine phosphorylation as a key !1regulatory pathway in Dictyostelium. !$#cross-references MUID:93046662; PMID:1423620 !$#accession A44267 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type mRNA; DNA !'##residues 1-521 ##label HOW !'##note sequence extracted from NCBI backbone (NCBIP:117713) CLASSIFICATION #superfamily Dictyostelium protein-tyrosine-phosphatase, !1nonreceptor type 1; protein-tyrosine-phosphatase homology KEYWORDS phosphoprotein; phosphoric monoester hydrolase; !1tyrosine-specific phosphatase FEATURE !$121-459 #domain protein-tyrosine-phosphatase homology #status !8atypical #label PTP\ !$310 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$316 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 521 #molecular-weight 59383 #checksum 9734 SEQUENCE /// ENTRY A48711 #type complete TITLE protein-tyrosine-phosphatase (EC 3.1.3.48), nonreceptor type 2 - slime mold (Dictyostelium discoideum) ALTERNATE_NAMES protein-tyrosine-phosphatase DdPTPa; PTP2 ORGANISM #formal_name Dictyostelium discoideum DATE 02-Jun-1995 #sequence_revision 08-Mar-1996 #text_change 11-Jun-1999 ACCESSIONS A48711; A53774 REFERENCE A48711 !$#authors Ramalingam, R.; Shaw, D.R.; Ennis, H.L. !$#journal J. Biol. Chem. (1993) 268:22680-22685 !$#title Cloning and functional expression of a Dictyostelium !1discoideum protein tyrosine phosphatase. !$#cross-references MUID:94043028; PMID:8226777 !$#accession A48711 !'##molecule_type mRNA !'##residues 1-377 ##label RAM !'##cross-references GB:L15420; NID:g290036; PIDN:AAA33242.1; !1PID:g290037 REFERENCE A53774 !$#authors Howard, P.K.; Gamper, M.; Hunter, T.; Firtel, R.A. !$#journal Mol. Cell. Biol. (1994) 14:5154-5164 !$#title Regulation by protein-tyrosine phosphatase PTP2 is distinct !1from that by PTP1 during Dictyostelium growth and !1development. !$#cross-references MUID:94309635; PMID:7518559 !$#accession A53774 !'##status nucleic acid sequence not shown !'##molecule_type mRNA; DNA !'##residues 1-377 ##label HOW !'##cross-references GB:L15420; NID:g290036; PIDN:AAA33242.1; !1PID:g290037 !'##note the translation of the nucleotide sequence is not complete in !1this paper CLASSIFICATION #superfamily Dictyostelium protein-tyrosine-phosphatase, !1nonreceptor type 2; protein-tyrosine-phosphatase homology KEYWORDS phosphoprotein; phosphoric monoester hydrolase; !1tyrosine-specific phosphatase FEATURE !$114-336 #domain protein-tyrosine-phosphatase homology #status !8atypical #label PTP\ !$281 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$287 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 377 #molecular-weight 43488 #checksum 2996 SEQUENCE /// ENTRY A39862 #type complete TITLE protein-tyrosine-phosphatase (EC 3.1.3.48), nonreceptor type 1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein D0815; protein YDL230w ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Dec-1991 #sequence_revision 08-Mar-1996 #text_change 21-Jul-2000 ACCESSIONS A39862; S67793 REFERENCE A39862 !$#authors Guan, K.; Deschenes, R.J.; Qiu, H.; Dixon, J.E. !$#journal J. Biol. Chem. (1991) 266:12964-12970 !$#title Cloning and expression of a yeast protein tyrosine !1phosphatase. !$#cross-references MUID:91302312; PMID:1649172 !$#accession A39862 !'##molecule_type DNA !'##residues 1-335 ##label GUA !'##cross-references GB:M64062; NID:g172295; PIDN:AAA34923.1; !1PID:g172296 REFERENCE S67778 !$#authors Rasmussen, S.W. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67793 !'##molecule_type DNA !'##residues 1-335 ##label RAS !'##cross-references EMBL:Z74278; NID:g1431387; PIDN:CAA98809.1; !1PID:g1431388; GSPDB:GN00004; MIPS:YDL230w !'##experimental_source strain S288C GENETICS !$#gene SGD:PTP1; MIPS:YDL230w !'##cross-references SGD:S0002389; MIPS:YDL230w !$#map_position 4L CLASSIFICATION #superfamily Saccharomyces protein-tyrosine-phosphatase, !1nonreceptor type 1; protein-tyrosine-phosphatase homology KEYWORDS phosphoprotein; phosphoric monoester hydrolase; !1tyrosine-specific phosphatase FEATURE !$52-303 #domain protein-tyrosine-phosphatase homology #label !8PTP\ !$252 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$258 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 335 #molecular-weight 38868 #checksum 7553 SEQUENCE /// ENTRY S29090 #type complete TITLE dual specificity phosphoprotein phosphatase (EC 3.1.3.-) 1 - human ALTERNATE_NAMES protein-tyrosine-phosphatase CL100; protein-tyrosine-phosphatase, nonreceptor type 10 ORGANISM #formal_name Homo sapiens #common_name man DATE 25-Feb-1994 #sequence_revision 02-May-1994 #text_change 11-Jun-1999 ACCESSIONS S29090; A53052 REFERENCE S29090 !$#authors Keyse, S.M.; Emslie, E.A. !$#journal Nature (1992) 359:644-647 !$#title Oxidative stress and heat shock induce a human gene encoding !1a protein-tyrosine phosphatase. !$#cross-references MUID:93024952; PMID:1406996 !$#accession S29090 !'##molecule_type mRNA !'##residues 1-367 ##label KEY !'##cross-references EMBL:X68277; NID:g29980; PIDN:CAA48338.1; !1PID:g29981 REFERENCE A53052 !$#authors Kwak, S.P.; Hakes, D.J.; Martell, K.J.; Dixon, J.E. !$#journal J. Biol. Chem. (1994) 269:3596-3604 !$#title Isolation and characterization of a human dual specificity !1protein-tyrosine phosphatase gene. !$#cross-references MUID:94148864; PMID:8106404 !$#accession A53052 !'##molecule_type DNA !'##residues 1-367 ##label KWA !'##experimental_source leukocyte !'##note sequence extracted from NCBI backbone (NCBIN:143800, !1NCBIN:143802, NCBIN:143804, NCBIN:143806, NCBIP:143807) GENETICS !$#gene GDB:DUSP1; PTPN10 !'##cross-references GDB:136197; OMIM:600714 !$#map_position 5q34-5q34 CLASSIFICATION #superfamily dual specificity phosphoprotein phosphatase 1; !1VH1-type dual specificity phosphoprotein phosphatase !1homology KEYWORDS heat shock; phosphoprotein; phosphoric monoester hydrolase; !1stress-induced protein FEATURE !$181-312 #domain VH1-type dual specificity phosphoprotein !8phosphatase homology #label VH1\ !$258 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$264 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 367 #molecular-weight 39297 #checksum 5401 SEQUENCE /// ENTRY A57126 #type complete TITLE dual specificity phosphoprotein phosphatase (EC 3.1.3.-) 2 - human ALTERNATE_NAMES mitogen-induced nuclear tyrosine phosphatase; phosphatase of activated cells PAC-1 ORGANISM #formal_name Homo sapiens #common_name man DATE 03-Nov-1995 #sequence_revision 02-Jul-1996 #text_change 11-Jun-1999 ACCESSIONS A57126 REFERENCE A57126 !$#authors Rohan, P.J.; Davis, P.; Moskaluk, C.A.; Kearns, M.; !1Krutzsch, H.; Siebenlist, U.; Kelly, K. !$#journal Science (1993) 259:1763-1766 !$#title PAC-1: a mitogen-induced nuclear protein tyrosine !1phosphatase. !$#cross-references MUID:93206122; PMID:7681221 !$#accession A57126 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-314 ##label ROH !'##cross-references GB:L11329; NID:g559539; PIDN:AAA50779.1; !1PID:g292376 GENETICS !$#gene GDB:DUSP2 !'##cross-references GDB:139200 !$#map_position 2q11-2q11 FUNCTION !$#description catalyzes the hydrolysis of peptidyl-phosphoserine, !1-phosphothreonine, and -phosphotyrosine to release phosphate CLASSIFICATION #superfamily dual specificity phosphoprotein phosphatase 1; !1VH1-type dual specificity phosphoprotein phosphatase !1homology KEYWORDS nucleus; phosphoprotein; phosphoric monoester hydrolase FEATURE !$140-160 #region nuclear location signal\ !$180-311 #domain VH1-type dual specificity phosphoprotein !8phosphatase homology #label VH1\ !$257 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$263 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 314 #molecular-weight 34399 #checksum 9557 SEQUENCE /// ENTRY S24411 #type complete TITLE dual specificity phosphoprotein phosphatase (EC 3.1.3.-) 1 - mouse ALTERNATE_NAMES 3CH134 protein; protein-tyrosine-phosphatase erp, nonreceptor type 10 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 19-Feb-1994 #sequence_revision 02-May-1994 #text_change 11-Jun-1999 ACCESSIONS A54681; S24411 REFERENCE A54681 !$#authors Noguchi, T.; Metz, R.; Chen, L.; Mattei, M.G.; Carrasco, D.; !1Bravo, R. !$#journal Mol. Cell. Biol. (1993) 13:5195-5205 !$#title Structure, mapping, and expression of erp, a growth !1factor-inducible gene encoding a nontransmembrane protein !1tyrosine phosphatase, and effect of ERP on cell growth. !$#cross-references MUID:93360956; PMID:8355678 !$#accession A54681 !'##molecule_type DNA !'##residues 1-367 ##label NOG !'##cross-references GB:S64851; NID:g409976; PIDN:AAB27882.1; !1PID:g409977 REFERENCE S24411 !$#authors Charles, C.H.; Abler, A.S.; Lau, L.F. !$#journal Oncogene (1992) 7:187-190 !$#title cDNA sequence of a growth factor-inducible immediate early !1gene and characterization of its encoded protein. !$#cross-references MUID:92158357; PMID:1741163 !$#accession S24411 !'##molecule_type mRNA !'##residues 1-367 ##label CHA !'##cross-references EMBL:X61940; NID:g49735; PIDN:CAA43944.1; !1PID:g49736 GENETICS !$#gene erp !$#introns 123/1; 172/1; 245/1 CLASSIFICATION #superfamily dual specificity phosphoprotein phosphatase 1; !1VH1-type dual specificity phosphoprotein phosphatase !1homology KEYWORDS immediate-early protein; phosphoprotein; phosphoric !1monoester hydrolase FEATURE !$181-312 #domain VH1-type dual specificity phosphoprotein !8phosphatase homology #label VH1\ !$258 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$264 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 367 #molecular-weight 39369 #checksum 5871 SEQUENCE /// ENTRY I38890 #type complete TITLE dual specificity phosphoprotein phosphatase (EC 3.1.3.-) 5 - human ALTERNATE_NAMES dual specificity phosphatase B23; dual-specificity phosphatase hVH-3; VH-1-like protein tyrosine phosphatase ORGANISM #formal_name Homo sapiens #common_name man DATE 16-Feb-1996 #sequence_revision 01-Mar-1996 #text_change 11-Jun-1999 ACCESSIONS I38890; A55313 REFERENCE A55432 !$#authors Kwak, S.P.; Dixon, J.E. !$#journal J. Biol. Chem. (1995) 270:1156-1160 !$#title Multiple dual specificity protein tyrosine phosphatases are !1expressed and regulated differentially in liver cell lines. !$#cross-references MUID:95138103; PMID:7836374 !$#accession I38890 !'##molecule_type mRNA !'##residues 1-384 ##label RES !'##cross-references EMBL:U16996; NID:g642012; PIDN:AAB06261.1; !1PID:g642013 !'##experimental_source placenta REFERENCE A55313 !$#authors Ishibashi, T.; Bottaro, D.P.; Michieli, P.; Kelley, C.A.; !1Aaronson, S.A. !$#journal J. Biol. Chem. (1994) 269:29897-29902 !$#title A novel dual specificity phosphatase induced by serum !1stimulation and heat shock. !$#cross-references MUID:95050849; PMID:7961985 !$#accession A55313 !'##molecule_type mRNA !'##residues 1-8,'GHV',12-70,'R',72-104,'F',107-362, !1'RCLPTQQSQSSAEALWQRPNPAKTGMEESAQPQEQL' ##label ISH !'##cross-references GB:U15932; NID:g606971; PIDN:AAA64693.1; !1PID:g606972 !'##experimental_source mammary epithelial cells GENETICS !$#gene GDB:DUSP5 !'##cross-references GDB:385447 !$#map_position 10q25-10q25 CLASSIFICATION #superfamily dual specificity phosphoprotein phosphatase 1; !1VH1-type dual specificity phosphoprotein phosphatase !1homology KEYWORDS phosphoprotein; phosphoric monoester hydrolase FEATURE !$186-317 #domain VH1-type dual specificity phosphoprotein !8phosphatase homology #label VH1\ !$263 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$269 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 384 #molecular-weight 42107 #checksum 691 SEQUENCE /// ENTRY A47196 #type complete TITLE dual specificity phosphoprotein phosphatase (EC 3.1.3.-) DUSP3 [validated] - human ALTERNATE_NAMES protein-tyrosine-phosphatase VHR; VH1-related dual-specificity phosphatase ORGANISM #formal_name Homo sapiens #common_name man DATE 21-Sep-1993 #sequence_revision 01-Mar-1996 #text_change 15-Sep-2000 ACCESSIONS A47196; A58760 REFERENCE A47196 !$#authors Ishibashi, T.; Bottaro, D.P.; Chan, A.; Miki, T.; Aaronson, !1S.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:12170-12174 !$#title Expression cloning of a human dual-specificity phosphatase. !$#cross-references MUID:93101689; PMID:1281549 !$#accession A47196 !'##molecule_type mRNA !'##residues 1-185 ##label ISH !'##cross-references GB:L05147; NID:g181839; PIDN:AAA35777.1; !1PID:g181840 !'##experimental_source fibroblasts !'##note sequence extracted from NCBI backbone (NCBIN:120790, !1NCBIP:120791) REFERENCE A58760 !$#authors Denu, J.M.; Zhou, G.; Wu, L.; Zhao, R.; Yuvaniyama, J.; !1Saper, M.A.; Dixon, J.E. !$#journal J. Biol. Chem. (1995) 270:3796-3803 !$#title The purification and characterization of a human !1dual-specific protein tyrosine phosphatase. !$#cross-references MUID:95181338; PMID:7876121 !$#accession A58760 !'##molecule_type protein !'##residues 2-7 ##label DEN REFERENCE A66852 !$#authors Yuvaniyama, J.; Denu, J.M.; Dixon, J.E.; Saper, M.A. !$#submission submitted to the Brookhaven Protein Data Bank, February 1996 !$#cross-references PDB:1VHR !$#contents annotation; X-ray crystallography, 2.1 angstroms, residues !18-185 REFERENCE A55447 !$#authors Zhou, G.; Denu, J.M.; Wu, L.; Dixon, J.E. !$#journal J. Biol. Chem. (1994) 269:28084-28090 !$#title The catalytic role of Cys(124) in the dual specificity !1phosphatase VHR. !$#cross-references MUID:95050584; PMID:7961745 !$#contents annotation; active site GENETICS !$#gene GDB:DUSP3; VHR !'##cross-references GDB:342110; OMIM:600183 !$#map_position 17q21-17q21 FUNCTION !$#description catalyzes hydrolysis of peptidyl-phosphoserine, !1-phosphothreonine and -phosphotyrosine to release phosphate CLASSIFICATION #superfamily dual specificity phosphoprotein phosphatase !1DUSP3; VH1-type dual specificity phosphoprotein phosphatase !1homology KEYWORDS phosphoprotein; phosphoric monoester hydrolase FEATURE !$2-185 #product dual specificity phosphatase 3 #status !8predicted #label MAT\ !$37-177 #domain VH1-type dual specificity phosphoprotein !8phosphatase homology #label VH1\ !$124 #active_site Cys (phosphocysteine intermediate) !8#status experimental\ !$130 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 185 #molecular-weight 20478 #checksum 3219 SEQUENCE /// ENTRY QQVZH1 #type complete TITLE dual specificity phosphoprotein phosphatase (EC 3.1.3.-) VH1 - vaccinia virus (strain Ankara and WR) ALTERNATE_NAMES H1 protein; H1L protein ORGANISM #formal_name vaccinia virus DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 18-Feb-2000 ACCESSIONS A24481; T37367 REFERENCE A93022 !$#authors Rosel, J.L.; Earl, P.L.; Weir, J.P.; Moss, B. !$#journal J. Virol. (1986) 60:436-449 !$#title Conserved TAAATG sequence at the transcriptional and !1translational initiation sites of vaccinia virus late genes !1deduced by structural and functional analysis of the HindIII !1H genome fragment. !$#cross-references MUID:87036903; PMID:3021979 !$#accession A24481 !'##molecule_type DNA !'##residues 1-171 ##label ROS !'##cross-references GB:M13209; NID:g335739; PIDN:AAB59836.1; !1PID:g335742 REFERENCE Z20877 !$#authors Antoine, G.; Scheiflinger, F.; Falkner, F.G.; Dorner, F. !$#submission submitted to the EMBL Data Library, March 1997 !$#description The complete genomic sequence of the Modified Vaccinia !1Ankara (MVA) strain. !$#accession T37367 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-171 ##label ANT !'##cross-references EMBL:U94848; PIDN:AAB96446.1 !'##experimental_source strain Ankara GENETICS !$#note MVA091L FUNCTION !$#description catalyzes hydrolysis of peptidyl-phosphoserine, !1-phosphothreonine and -phosphotyrosine to release phosphate CLASSIFICATION #superfamily dual specificity phosphoprotein phosphatase !1DUSP3; VH1-type dual specificity phosphoprotein phosphatase !1homology KEYWORDS late protein; phosphoprotein; phosphoric monoester hydrolase FEATURE !$34-169 #domain VH1-type dual specificity phosphoprotein !8phosphatase homology #label VH1\ !$110 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$116 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 171 #molecular-weight 19698 #checksum 1340 SEQUENCE /// ENTRY A42514 #type complete TITLE dual specificity phosphoprotein phosphatase (EC 3.1.3.-) VH1 - vaccinia virus (strain Copenhagen) ALTERNATE_NAMES H1L protein ORGANISM #formal_name vaccinia virus #note host Homo sapiens (man) DATE 28-Aug-1998 #sequence_revision 28-Aug-1998 #text_change 11-Jun-1999 ACCESSIONS A42514; A47452 REFERENCE A33172 !$#authors Johnson, G.P. !$#submission submitted to GenBank, June 1990 !$#accession A42514 !'##molecule_type DNA !'##residues 1-171 ##label JOH !'##cross-references GB:M35027; NID:g335317; PIDN:AAA48088.1; !1PID:g335436 !'##experimental_source strain Copenhagen REFERENCE A47452 !$#authors Hakes, D.J.; Martell, K.J.; Zhao, W.G.; Massung, R.F.; !1Esposito, J.J.; Dixon, J.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:4017-4021 !$#title A protein phosphatase related to the vaccinia virus VH1 is !1encoded in the genomes of several orthopoxviruses and a !1baculovirus. !$#cross-references MUID:93248221; PMID:8387208 !$#contents annotation FUNCTION !$#description catalyzes hydrolysis of peptidyl-phosphoserine, !1-phosphothreonine and -phosphotyrosine to release phosphate CLASSIFICATION #superfamily dual specificity phosphoprotein phosphatase !1DUSP3; VH1-type dual specificity phosphoprotein phosphatase !1homology KEYWORDS late protein; phosphoprotein; phosphoric monoester hydrolase FEATURE !$34-169 #domain VH1-type dual specificity phosphoprotein !8phosphatase homology #label VH1\ !$110 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$116 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 171 #molecular-weight 19672 #checksum 1473 SEQUENCE /// ENTRY I36845 #type complete TITLE dual specificity phosphoprotein phosphatase (EC 3.1.3.-) VH1 - variola virus ALTERNATE_NAMES I1L protein; vaccinia virus H1L protein homolog ORGANISM #formal_name variola virus DATE 28-Aug-1998 #sequence_revision 28-Aug-1998 #text_change 23-Mar-2001 ACCESSIONS I36845; S33098 REFERENCE A36859 !$#authors Blinov, V.M. !$#submission submitted to GenBank, November 1992 !$#accession I36845 !'##molecule_type DNA !'##residues 1-171 ##label BLI !'##cross-references GB:X69198; NID:g456758; PIDN:CAA49025.1; !1PID:g297264 !'##experimental_source strain India-1967 REFERENCE S33069 !$#authors Shchelkunov, S.N.; Blinov, V.M.; Totmenin, A.V.; !1Marennikova, S.S.; Kolykhalov, A.A.; Frolov, I.V.; !1Chizhikov, V.E.; Gytorov, V.V.; Gashikov, P.V.; Belanov, !1E.F.; Belavin, P.A.; Resenchuk, S.M.; Andzhaparidze, O.G.; !1Sandakhchiev, L.S. !$#journal Virus Res. (1993) 27:25-35 !$#title Nucleotide sequence analysis of variola virus HindIII M, L, !1I genome fragments. !$#cross-references MUID:93190624; PMID:8383392 !$#accession S33098 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-171 ##label SHC !'##cross-references EMBL:X67119; NID:g62330; PIDN:CAA47583.1; !1PID:g62360 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1992 FUNCTION !$#description catalyzes hydrolysis of peptidyl-phosphoserine, !1-phosphothreonine and -phosphotyrosine to release phosphate CLASSIFICATION #superfamily dual specificity phosphoprotein phosphatase !1DUSP3; VH1-type dual specificity phosphoprotein phosphatase !1homology KEYWORDS late protein; phosphoprotein; phosphoric monoester hydrolase FEATURE !$34-169 #domain VH1-type dual specificity phosphoprotein !8phosphatase homology #label VH1\ !$110 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$116 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 171 #molecular-weight 19746 #checksum 3377 SEQUENCE /// ENTRY B47452 #type complete TITLE dual specificity phosphoprotein phosphatase (EC 3.1.3.-) VH1 - raccoonpox virus ORGANISM #formal_name raccoonpox virus DATE 28-Aug-1998 #sequence_revision 28-Aug-1998 #text_change 28-Aug-1998 ACCESSIONS B47452 REFERENCE A47452 !$#authors Hakes, D.J.; Martell, K.J.; Zhao, W.G.; Massung, R.F.; !1Esposito, J.J.; Dixon, J.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:4017-4021 !$#title A protein phosphatase related to the vaccinia virus VH1 is !1encoded in the genomes of several orthopoxviruses and a !1baculovirus. !$#cross-references MUID:93248221; PMID:8387208 !$#accession B47452 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-171 ##label HAK !'##cross-references GB:L13165; NID:g310337 !'##note sequence extracted from NCBI backbone (NCBIP:130800) FUNCTION !$#description catalyzes hydrolysis of peptidyl-phosphoserine, !1-phosphothreonine and -phosphotyrosine to release phosphate CLASSIFICATION #superfamily dual specificity phosphoprotein phosphatase !1DUSP3; VH1-type dual specificity phosphoprotein phosphatase !1homology KEYWORDS late protein; phosphoprotein; phosphoric monoester hydrolase FEATURE !$34-169 #domain VH1-type dual specificity phosphoprotein !8phosphatase homology #label VH1\ !$110 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$116 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 171 #molecular-weight 19741 #checksum 669 SEQUENCE /// ENTRY A49436 #type complete TITLE dual specificity phosphoprotein phosphatase (EC 3.1.3.-) CDKN3 - human ALTERNATE_NAMES CDK2-associated dual specificity phosphatase; cyclin-dependent kinase inhibitor 3; cyclin-dependent kinase interactor 1 (Cdi1); KAP ORGANISM #formal_name Homo sapiens #common_name man DATE 07-Apr-1994 #sequence_revision 12-Jul-1996 #text_change 21-Jul-2000 ACCESSIONS A49436; A53133 REFERENCE A49436 !$#authors Gyuris, J.; Golemis, E.; Chertkov, H.; Brent, R. !$#journal Cell (1993) 75:791-803 !$#title Cdi1, a human G1 and S phase protein phosphatase that !1associates with Cdk2. !$#cross-references MUID:94061995; PMID:8242750 !$#accession A49436 !'##molecule_type mRNA !'##residues 1-212 ##label GYU !'##cross-references GB:S67331; GB:U02681; NID:g2934877; !1PIDN:AAC04932.1; PID:g2934878 !'##experimental_source HeLa cells !'##note sequence extracted from NCBI backbone (NCBIN:139833, !1NCBIP:139834) REFERENCE A53133 !$#authors Hannon, G.J.; Casso, D.; Beach, D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1994) 91:1731-1735 !$#title KAP: a dual specificity phosphatase that interacts with !1cyclin-dependent kinases. !$#cross-references MUID:94173903; PMID:8127873 !$#accession A53133 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1,'K',3-212 ##label RES !'##cross-references GB:L27711; NID:g808006; PIDN:AAA66496.1; !1PID:g443669 GENETICS !$#gene GDB:CDKN3; KAP1 !'##cross-references GDB:330748; OMIM:123832 !$#map_position 14q22-14q22 FUNCTION !$#description catalyzes hydrolysis of peptidyl-phosphoserine, !1-phosphothreonine and -phosphotyrosine to release phosphate CLASSIFICATION #superfamily dual specificity phosphoprotein phosphatase !1DUSP3; VH1-type dual specificity phosphoprotein phosphatase !1homology KEYWORDS cell cycle control; phosphoprotein; phosphoric monoester !1hydrolase FEATURE !$75-196 #domain VH1-type dual specificity phosphoprotein !8phosphatase homology #label VH1\ !$140 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$146 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 212 #molecular-weight 23806 #checksum 2511 SEQUENCE /// ENTRY S48459 #type complete TITLE probable dual specificity phosphoprotein phosphatase (EC 3.1.3.-) YIL113w - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein-tyrosine-phosphatase ORGANISM #formal_name Saccharomyces cerevisiae DATE 02-Dec-1994 #sequence_revision 12-Apr-1996 #text_change 19-Apr-2002 ACCESSIONS S48459 REFERENCE S48455 !$#authors Bowman, S.; Churcher, C. !$#submission submitted to the EMBL Data Library, September 1994 !$#accession S48459 !'##molecule_type DNA !'##residues 1-209 ##label BOW !'##cross-references GB:Z47047; EMBL:Z38125; NID:g603997; PID:g763233; !1GSPDB:GN00009; MIPS:YIL113w GENETICS !$#gene MIPS:YIL113w !'##cross-references SGD:S0001375 !$#map_position 9L FUNCTION !$#description catalyzes hydrolysis of peptidyl-phosphoserine, !1-phosphothreonine and -phosphotyrosine to release phosphate CLASSIFICATION #superfamily dual specificity phosphoprotein phosphatase !1DUSP3; VH1-type dual specificity phosphoprotein phosphatase !1homology KEYWORDS phosphoprotein; phosphoric monoester hydrolase FEATURE !$68-194 #domain VH1-type dual specificity phosphoprotein !8phosphatase homology #label VH1\ !$140 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$146 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 209 #molecular-weight 23885 #checksum 9828 SEQUENCE /// ENTRY A40781 #type complete TITLE dual specificity phosphoprotein phosphatase (EC 3.1.3.-) BVP - Autographa californica nuclear polyhedrosis virus ALTERNATE_NAMES ORF1 protein ORGANISM #formal_name Autographa californica nuclear polyhedrosis virus, AcMNPV DATE 28-Feb-1992 #sequence_revision 19-Apr-1996 #text_change 24-Nov-1999 ACCESSIONS A40781; C38477; A72850; A45431 REFERENCE A40781 !$#authors Possee, R.D.; Sun, T.P.; Howard, S.C.; Ayres, M.D.; !1Hill-Perkins, M.; Gearing, K.L. !$#journal Virology (1991) 185:229-241 !$#title Nucleotide sequence of the Autographa californica nuclear !1polyhedrosis 9.4 kbp EcoRI-I and -R (polyhedrin gene) !1region. !$#cross-references MUID:92024079; PMID:1926775 !$#accession A40781 !'##molecule_type DNA !'##residues 1-168 ##label POS !'##cross-references GB:M75679 !'##experimental_source strain C6 REFERENCE A38477 !$#authors Tilakaratne, N.; Hardin, S.E.; Weaver, R.F. !$#journal J. Gen. Virol. (1991) 72:285-291 !$#title Nucleotide sequence and transcript mapping of the HindIII F !1region of the Autographa californica nuclear polyhedrosis !1virus genome. !$#cross-references MUID:91132123; PMID:1993873 !$#accession C38477 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-48,'I',50-166,'F' ##label TIL !'##experimental_source strain L1 REFERENCE A45431 !$#authors Sheng, Z.; Charbonneau, H. !$#journal J. Biol. Chem. (1993) 268:4728-4733 !$#title The baculovirus Autographa californica encodes a protein !1tyrosine phosphatase. !$#cross-references MUID:93186773; PMID:8444848 !$#contents annotation; tyrosine and serine phosphatase activity REFERENCE A72850 !$#authors Ayres, M.D.; Howard, S.C.; Kuzio, J.; Lopez-Ferber, M.; !1Possee, R.D. !$#journal Virology (1994) 202:586-605 !$#title The complete DNA sequence of Autographa californica nuclear !1polyhedrosis virus. !$#cross-references MUID:94303173; PMID:8030224 !$#accession A72850 !'##status preliminary !'##molecule_type DNA !'##residues 1-168 ##label AYR !'##cross-references GB:L22858; NID:g510708; PIDN:AAA66631.1; !1PID:g559070 GENETICS !$#gene Ac-ptp FUNCTION !$#description catalyzes hydrolysis of peptidyl-phosphoserine, !1-phosphothreonine and -phosphotyrosine to release phosphate CLASSIFICATION #superfamily dual specificity phosphoprotein phosphatase !1DUSP3; VH1-type dual specificity phosphoprotein phosphatase !1homology KEYWORDS phosphoprotein; phosphoric monoester hydrolase FEATURE !$47-168 #domain VH1-type dual specificity phosphoprotein !8phosphatase homology #label VH1\ !$119 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$125 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 168 #molecular-weight 19288 #checksum 5052 SEQUENCE /// ENTRY S31304 #type complete TITLE protein-tyrosine-phosphatase (EC 3.1.3.48) YVH1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YIR026c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 12-Nov-1999 ACCESSIONS S31304; S48488; S28650 REFERENCE S31304 !$#authors Guan, K.; Hakes, D.J.; Wang, Y.; Park, H.D.; Cooper, T.G.; !1Dixon, J.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:12175-12179 !$#title A yeast protein phosphatase related to the vaccinia virus !1VH1 phosphatase is induced by nitrogen starvation. !$#cross-references MUID:93101690; PMID:1334559 !$#accession S31304 !'##molecule_type DNA !'##residues 1-364 ##label GUA !'##cross-references EMBL:L04673; NID:g172167; PIDN:AAA34874.1; !1PID:g172168 REFERENCE S48478 !$#authors Rowley, K. !$#submission submitted to the EMBL Data Library, October 1994 !$#accession S48488 !'##molecule_type DNA !'##residues 1-364 ##label ROW !'##cross-references GB:Z47047; EMBL:Z38061; NID:g603997; PID:g763371; !1GSPDB:GN00009; MIPS:YIR026c REFERENCE S28649 !$#authors Buckholz, R.G.; Cooper, T.G. !$#journal Yeast (1991) 7:913-923 !$#title The allantoinase (DAL1) gene of Saccharomyces cerevisiae. !$#cross-references MUID:92206070; PMID:1803816 !$#accession S28650 !'##molecule_type DNA !'##residues 1-67,69-197,'AI' ##label BUC !'##cross-references EMBL:M69294 GENETICS !$#gene SGD:YVH1; MIPS:YIR026c !'##cross-references SGD:S0001465; MIPS:YIR026c !$#map_position 9R CLASSIFICATION #superfamily Saccharomyces protein-tyrosine-phosphatase !1YVH1; VH1-type dual specificity phosphoprotein phosphatase !1homology KEYWORDS phosphoric monoester hydrolase; tyrosine-specific !1phosphatase FEATURE !$19-171 #domain VH1-type dual specificity phosphoprotein !8phosphatase homology #label VH1 SUMMARY #length 364 #molecular-weight 41185 #checksum 3844 SEQUENCE /// ENTRY S58725 #type complete TITLE dual specificity phosphatase (EC 3.1.3.-) MSG5 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein N2480; protein YNL053w; protein YNL1629 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S58725; S40029; S05831; S62981 REFERENCE S58711 !$#authors Bergez, P.; Doignon, F.; Crouzet, M. !$#journal Yeast (1995) 11:967-974 !$#title The sequence of a 44 420 bp fragment located on the left arm !1of chromosome XIV from Saccharomyces cerevisiae. !$#cross-references MUID:96021608; PMID:8533472 !$#accession S58725 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-489 ##label BER !'##cross-references EMBL:U12141; NID:g1314216; PIDN:AAA99659.1; !1PID:g994834 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1994 REFERENCE S40029 !$#authors Doi, K.; Gartner, A.; Ammerer, G.; Errede, B.; Shinkawa, H.; !1Sugimoto, K.; Matsumoto, K. !$#journal EMBO J. (1994) 13:61-70 !$#title MSG5, a novel protein phosphatase promotes adaptation to !1pheromone response in S. cerevisiae. !$#cross-references MUID:94139675; PMID:8306972 !$#accession S40029 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type DNA !'##residues 1-346,'DE',349-489 ##label DOI !'##cross-references GB:D17548; NID:g459242; PIDN:BAA04485.1; !1PID:g459243 REFERENCE S05831 !$#authors Seraphin, B.; Simon, M.; Faye, G. !$#journal Curr. Genet. (1985) 9:435-439 !$#title Primary structure of a gene for subunit V of the cytochrome !1c oxidase from Saccharomyces cerevisiae. !$#cross-references MUID:88223509; PMID:2836092 !$#accession S05831 !'##molecule_type DNA !'##residues 415-489 ##label SER !'##cross-references EMBL:X02561; NID:g3568; PIDN:CAA26402.1; PID:g3569 REFERENCE S62975 !$#authors Bergez, P.; Doignon, F.; Crouzet, M. !$#submission submitted to the Protein Sequence Database, April 1996 !$#accession S62981 !'##molecule_type DNA !'##residues 1-489 ##label BEW !'##cross-references EMBL:Z71329; NID:g1301916; PIDN:CAA95922.1; !1PID:g1301917; GSPDB:GN00014; MIPS:YNL1629 !'##experimental_source strain S288C GENETICS !$#gene SGD:MSG5; MIPS:YNL1629 !'##cross-references SGD:S0004998; MIPS:YNL053w !$#map_position 14L FUNCTION !$#description allows recovery from pheromone stimulation by !1dephosphorylating the MAP kinase FUS3, which is part of the !1mating factor signal transduction pathway CLASSIFICATION #superfamily dual specificity phosphoprotein phosphatase !1MSG5; VH1-type dual specificity phosphoprotein phosphatase !1homology KEYWORDS phosphoprotein; phosphoric monoester hydrolase FEATURE !$242-373 #domain VH1-type dual specificity phosphoprotein !8phosphatase homology #label VH1\ !$319 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$325 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 489 #molecular-weight 54217 #checksum 2656 SEQUENCE /// ENTRY S43743 #type complete TITLE probable dual specificity phosphoprotein phosphatase (EC 3.1.3.-) - yeast (Candida albicans) ALTERNATE_NAMES protein-tyrosine-phosphatase ORGANISM #formal_name Candida albicans DATE 03-May-1994 #sequence_revision 12-Apr-1996 #text_change 05-Jun-1998 ACCESSIONS S43743 REFERENCE S43743 !$#authors Dignard, D. !$#submission submitted to the EMBL Data Library, August 1992 !$#accession S43743 !'##molecule_type DNA !'##residues 1-597 ##label DIG !'##cross-references EMBL:L01038; NID:g349178; PID:g349179 COMMENT This enzyme interferes with the S.cerevisiae pheromone !1response pathway. CLASSIFICATION #superfamily Candida probable dual specificity !1phosphoprotein phosphatase; VH1-type dual specificity !1phosphoprotein phosphatase homology KEYWORDS phosphoprotein; phosphoric monoester hydrolase FEATURE !$437-577 #domain VH1-type dual specificity phosphoprotein !8phosphatase homology #label VH1\ !$516 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$522 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 597 #molecular-weight 65637 #checksum 2918 SEQUENCE /// ENTRY S44538 #type complete TITLE probable protein-tyrosine-phosphatase (EC 3.1.3.48) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein YBR2013; hypothetical protein YBR276c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-Nov-1999 ACCESSIONS S44538; S46158; S39132 REFERENCE S44537 !$#authors Holmstrom, K.; Brandt, T.; Kallesoe, T. !$#journal Yeast (1994) 10(Suppl.A):S47-S62 !$#title The sequence of a 32420 bp segment located on the right arm !1of chromosome II from Saccharomyces cerevisiae. !$#cross-references MUID:94378722; PMID:8091861 !$#accession S44538 !'##status translation not shown !'##molecule_type DNA !'##residues 1-807 ##label HOL !'##cross-references EMBL:X76053; NID:g600025; PIDN:CAA53639.1; !1PID:g429121 REFERENCE S46157 !$#authors Brandt, T.; Christiansen, C.; Holmstroem, K.; Kallesoe, T. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S46158 !'##molecule_type DNA !'##residues 1-807 ##label BRA !'##cross-references EMBL:Z36145; NID:g536716; PIDN:CAA85239.1; !1PID:g536717; GSPDB:GN00002; MIPS:YBR276c GENETICS !$#gene SGD:PPS1; MIPS:YBR276c !'##cross-references SGD:S0000480; MIPS:YBR276c !$#map_position 2R CLASSIFICATION #superfamily Saccharomyces protein-tyrosine-phosphatase !1YBR2013; VH1-type dual specificity phosphoprotein !1phosphatase homology KEYWORDS phosphoric monoester hydrolase; transmembrane protein; !1tyrosine-specific phosphatase FEATURE !$228-247 #domain transmembrane #status predicted #label TM1\ !$450-466 #domain transmembrane #status predicted #label TM2\ !$485-501 #domain transmembrane #status predicted #label TM3\ !$593-781 #domain VH1-type dual specificity phosphoprotein !8phosphatase homology #status atypical #label VH1\ !$606-622 #domain transmembrane #status predicted #label TM4\ !$721-737 #domain transmembrane #status predicted #label TM5\ !$725 #active_site Cys #status predicted SUMMARY #length 807 #molecular-weight 91684 #checksum 5879 SEQUENCE /// ENTRY A46635 #type complete TITLE dual specificity phosphoprotein phosphatase (EC 3.1.3.-) IphP precursor - Nostoc commune ORGANISM #formal_name Nostoc commune DATE 21-Sep-1993 #sequence_revision 08-Mar-1996 #text_change 11-Jun-1999 ACCESSIONS A46635 REFERENCE A46635 !$#authors Potts, M.; Sun, H.; Mockaitis, K.; Kennelly, P.J.; Reed, D.; !1Tonks, N.K. !$#journal J. Biol. Chem. (1993) 268:7632-7635 !$#title A protein-tyrosine/serine phosphatase encoded by the genome !1of the cyanobacterium Nostoc commune UTEX 584. !$#cross-references MUID:93216721; PMID:7681825 !$#accession A46635 !'##molecule_type DNA !'##residues 1-294 ##label POT !'##cross-references GB:L11392; NID:g293976; PIDN:AAA25511.1; !1PID:g293977 !'##experimental_source strain UTEX 584 !'##note sequence extracted from NCBI backbone (NCBIN:128982, !1NCBIP:128983); part of this sequence, including the amino !1end of the mature protein isolated from transformed E. coli, !1was confirmed by protein sequencing CLASSIFICATION #superfamily Nostoc dual specificity phosphoprotein !1phosphatase IphP KEYWORDS phosphoprotein; phosphoric monoester hydrolase FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-294 #product dual specificity phosphatase IphP #status !8predicted #label MAT\ !$182 #active_site Cys (phosphocysteine intermediate) !8#status predicted\ !$188 #binding_site substrate phosphate (Arg) #status !8predicted SUMMARY #length 294 #molecular-weight 31005 #checksum 1934 SEQUENCE /// ENTRY NCBPT5 #type complete TITLE phosphodiesterase I (EC 3.1.4.1) - phage T5 ALTERNATE_NAMES 5'-exonuclease ORGANISM #formal_name phage T5 #note host Escherichia coli DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 11-Jun-1999 ACCESSIONS A23610 REFERENCE A23610 !$#authors Kaliman, A.V.; Krutilina, A.I.; Kryukov, V.M.; Bayev, A.A. !$#journal FEBS Lett. (1986) 195:61-64 !$#title Cloning and DNA sequence of the 5'-exonuclease gene of !1bacteriophage T5. !$#cross-references MUID:86108899; PMID:3002857 !$#accession A23610 !'##molecule_type DNA !'##residues 1-291 ##label KAL !'##cross-references GB:X03402; NID:g15413; PIDN:CAA27136.1; PID:g15414 GENETICS !$#gene D15 CLASSIFICATION #superfamily phage T5 phosphodiesterase I KEYWORDS exonuclease; phosphoric diester hydrolase SUMMARY #length 291 #molecular-weight 33448 #checksum 6968 SEQUENCE /// ENTRY A39825 #type complete TITLE sphingomyelin phosphodiesterase (EC 3.1.4.12), acidic, splice form 1 precursor [validated] - human ALTERNATE_NAMES acid sphingomyelinase ORGANISM #formal_name Homo sapiens #common_name man DATE 20-Mar-1992 #sequence_revision 07-Jul-1995 #text_change 22-Mar-2002 ACCESSIONS S27009; S36357; A39825; JX0276; S06957; I55567; A42801; !1B42801; C42801; D42801 REFERENCE S27009 !$#authors Newrzella, D.; Stoffel, W. !$#journal Biol. Chem. Hoppe-Seyler (1992) 373:1233-1238 !$#title Molecular cloning of the acid sphingomyelinase of the mouse !1and the organization and complete nucleotide sequence of the !1gene. !$#cross-references MUID:93183402; PMID:1292508 !$#accession S27009 !'##molecule_type DNA !'##residues 1-629 ##label NEW !'##cross-references EMBL:X63600; NID:g556808 REFERENCE S36357 !$#authors Hofmann, K. !$#submission submitted to the EMBL Data Library, December 1991 !$#accession S36357 !'##molecule_type DNA !'##residues 1-321,'T',323-629 ##label HOF !'##cross-references EMBL:X63600; NID:g556808; PIDN:CAA45145.1; !1PID:g556809 REFERENCE A39825 !$#authors Schuchman, E.H.; Suchi, M.; Takahashi, T.; Sandhoff, K.; !1Desnick, R.J. !$#journal J. Biol. Chem. (1991) 266:8531-8539 !$#title Human acid sphingomyelinase. Isolation, nucleotide sequence, !1and expression of the full-length and alternatively spliced !1cDNAs. !$#cross-references MUID:91217097; PMID:1840600 !$#accession A39825 !'##molecule_type mRNA !'##residues 1-629 ##label SCH !'##cross-references GB:M59916; NID:g179094; PIDN:AAA58377.1; !1PID:g179095 !'##note polymorphisms were demonstrated at positions 322 and 506 REFERENCE JX0276 !$#authors Ida, H.; Rennert, O.M.; Eto, Y.; Chan, W.Y. !$#journal J. Biochem. (1993) 114:15-20 !$#title Cloning of a human acid sphingomyelinase cDNA with a new !1mutation that renders the enzyme inactive. !$#cross-references MUID:94012573; PMID:8407868 !$#accession JX0276 !'##molecule_type mRNA !'##residues 1-35,38-156,'R',158-321,'T',323-505,'G',507-629 ##label IDA !'##cross-references EMBL:X59960; NID:g402620; PIDN:CAA42584.1; !1PID:g402621 !'##note the authors translated the codon CTC for residue 85 as Thr and !1ACC for residue 86 as Leu !'##note this form has no catalytic activity; correction of position 157 !1to Cys restores activity REFERENCE S06957 !$#authors Quintern, L.E.; Schuchman, E.H.; Levran, O.; Suchi, M.; !1Ferlinz, K.; Reinke, H.; Sandhoff, K.; Desnick, R.J. !$#journal EMBO J. (1989) 8:2469-2473 !$#title Isolation of cDNA clones encoding human acid !1sphingomyelinase: occurrence of alternatively processed !1transcripts. !$#cross-references MUID:90060003; PMID:2555181 !$#accession S06957 !'##molecule_type mRNA !'##residues 128-629 ##label QUI !'##cross-references EMBL:X52678; NID:g28879; PIDN:CAA36901.1; !1PID:g28880 !'##note parts of this sequence were confirmed by peptide sequencing REFERENCE I55567 !$#authors Levran, O.; Desnick, R.J.; Schuchman, E.H. !$#journal J. Clin. Invest. (1991) 88:806-810 !$#title Niemann-Pick type B disease. Identification of a single !1codon deletion in the acid sphingomyelinase gene and !1genotype/phenotype correlations in type A and B patients. !$#cross-references MUID:91358737; PMID:1885770 !$#accession I55567 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 119-120,'H',122 ##label LEV !'##cross-references GB:S55766; NID:g234719; PIDN:AAB19680.1; !1PID:g234720 REFERENCE A42801 !$#authors Takahashi, T.; Suchi, M.; Desnick, R.J.; Takada, G.; !1Schuchman, E.H. !$#journal J. Biol. Chem. (1992) 267:12552-12558 !$#title Identification and expression of five mutations in the human !1acid sphingomyelinase gene causing types A and B !1Niemann-Pick disease. Molecular evidence for genetic !1heterogeneity in the neuronopathic and non-neuronopathic !1forms. !$#cross-references MUID:92316934; PMID:1618760 !$#contents annotation; characterization of mutations !$#note substitution of Ile for 382-Met or Ser for 383-Asn result in !1complete inactivation and lead to severe (type A) !1Niemann-Pick disease; substitution of Arg for 282-Gly result !1in partial inactivation and lead to milder (type B) disease COMMENT Two isoforms, neutral and acidic, have been identified. The !1acidic isoform is located in lysosomes, whereas the neutral !1isoform is membrane-bound. COMMENT For the inactive splice form 2, see PIR:S06958. GENETICS !$#gene GDB:SMPD1 !'##cross-references GDB:128144; OMIM:257200 !$#map_position 11p15.4-11p15.4 !$#introns 104/3; 362/2; 419/3; 445/2; 494/1 !$#note a defect in this gene may result in Niemann-Pick disease COMPLEX monomer FUNCTION !$#description catalyzes the hydrolysis of sphingomylin to form !1phosphorylcholine and ceramide CLASSIFICATION #superfamily acid sphingomyelinase; phosphoesterase core !1homology; saposin repeat homology KEYWORDS acetylated amino end; alternative splicing; glycoprotein; !1lysosome; metalloprotein; phosphoric diester hydrolase FEATURE !$1-48 #domain signal sequence #status predicted #label SIG\ !$49-629 #product sphingomyelin phosphodiesterase #status !8predicted #label MAT\ !$81-175 #domain saposin repeat homology #label SAP\ !$200-320 #domain phosphoesterase core homology #label PEC\ !$49 #modified_site acetylated amino end (Asp) (in mature !8form) #status predicted\ !$86,175,335,395,503, !$520 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$89-165,92-157, !$120-131 #disulfide_bonds #status predicted\ !$251,319,439 #active_site Asp, His, Tyr #status predicted SUMMARY #length 629 #molecular-weight 69862 #checksum 1603 SEQUENCE /// ENTRY S27393 #type complete TITLE sphingomyelin phosphodiesterase (EC 3.1.4.12), acidic, splice form 1 precursor - mouse ALTERNATE_NAMES acid sphingomyelinase ORGANISM #formal_name Mus musculus #common_name house mouse DATE 22-Nov-1993 #sequence_revision 30-Jan-1998 #text_change 11-Jun-1999 ACCESSIONS A58720; S27393; S27392 REFERENCE A58720 !$#authors Hofmann, K. !$#submission submitted to GenBank, April 1994 !$#accession A58720 !'##molecule_type mRNA !'##residues 1-627 ##label HOF !'##cross-references EMBL:Z14252; NID:g475956; PIDN:CAA78619.1; !1PID:g475957 REFERENCE S27009 !$#authors Newrzella, D.; Stoffel, W. !$#journal Biol. Chem. Hoppe-Seyler (1992) 373:1233-1238 !$#title Molecular cloning of the acid sphingomyelinase of the mouse !1and the organization and complete nucleotide sequence of the !1gene. !$#cross-references MUID:93183402; PMID:1292508 !$#accession S27393 !'##status preliminary !'##molecule_type DNA !'##residues 1-223,'SG',226-383,'P',385-627 ##label NE1 !'##cross-references EMBL:Z14132; NID:g475954 !$#accession S27392 !'##status preliminary !'##molecule_type mRNA !'##residues 1-223,'SG',226-383,'P',385-627 ##label NE2 !'##cross-references EMBL:Z14252; NID:g475956 COMMENT Sphingomyelin phosphodiesterase catalyzes the cleavage of !1sphingomylin to form phosphorylcholine and ceramide. Two !1isoforms have been identified: neutral and acidic isoforms. !1The acidic isoform is located in lysosomes, whereas the !1neutral isoform is membrane-bound. CLASSIFICATION #superfamily acid sphingomyelinase; phosphoesterase core !1homology; saposin repeat homology KEYWORDS alternative splicing; glycoprotein; lysosome; phosphoric !1diester hydrolase FEATURE !$1-44 #domain signal sequence #status predicted #label SIG\ !$45-627 #product sphingomyelin phosphodiesterase #status !8predicted #label MAT\ !$79-173 #domain saposin repeat homology #label SAP\ !$198-318 #domain phosphoesterase core homology #label PEC\ !$84,173,333,393,518, !$611 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 627 #molecular-weight 69926 #checksum 713 SEQUENCE /// ENTRY S62358 #type complete TITLE inositol 1,4,5-trisphosphate-binding protein, 130K - rat ALTERNATE_NAMES phospholipase C delta 1 homolog ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S62358; S69328 REFERENCE S62358 !$#authors Kanematsu, T.; Misumi, Y.; Watanabe, Y.; Ozaki, S.; Koga, !1T.; Iwanaga, S.; Ikehara, Y.; Hirata, M. !$#journal Biochem. J. (1996) 313:319-325 !$#title A new inositol 1,4,5-trisphosphate binding protein similar !1to phospholipase c-delta(1). !$#cross-references MUID:96132642; PMID:8546702 !$#accession S62358 !'##molecule_type mRNA !'##residues 1-1096 ##label KAN1 !'##cross-references EMBL:D45920; NID:g1183843; PIDN:BAA08351.1; !1PID:g1183844 !$#accession S69328 !'##molecule_type protein !'##residues 172-191;228-242;1024-1034 ##label KAN2 CLASSIFICATION #superfamily human phosphoinositide-specific phospholipase !1C; 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase !1domain X homology; 1-phosphatidylinositol-4,5-bisphosphate !1phosphodiesterase domain Y homology FEATURE !$401-543 #domain 1-phosphatidylinositol-4,5-bisphosphate !8phosphodiesterase domain X homology #label PIPX\ !$585-705 #domain 1-phosphatidylinositol-4,5-bisphosphate !8phosphodiesterase domain Y homology #label PIPY SUMMARY #length 1096 #molecular-weight 122771 #checksum 6862 SEQUENCE /// ENTRY I54390 #type complete TITLE phosphoinositide-specific phospholipase C (EC 3.1.4.-) epsilon - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS I54390 REFERENCE I54390 !$#authors Kohno, T.; Otsuka, T.; Takano, H.; Yamamoto, T.; Hamaguchi, !1M.; Terada, M.; Yokota, J. !$#journal Hum. Mol. Genet. (1995) 4:667-674 !$#title Identification of a novel phospholipase C family gene at !1chromosome 2q33 that is homozygously deleted in human small !1cell lung carcinoma. !$#cross-references MUID:95359973; PMID:7633416 !$#accession I54390 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-997 ##label RES !'##cross-references GB:D42108; NID:g780121; PIDN:BAA07688.1; !1PID:g780122 GENETICS !$#gene GDB:PLCE; PLC-L !'##cross-references GDB:699207; OMIM:600597 !$#map_position 2q33-2q33 CLASSIFICATION #superfamily human phosphoinositide-specific phospholipase !1C; 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase !1domain X homology; 1-phosphatidylinositol-4,5-bisphosphate !1phosphodiesterase domain Y homology KEYWORDS phosphoric diester hydrolase FEATURE !$302-444 #domain 1-phosphatidylinositol-4,5-bisphosphate !8phosphodiesterase domain X homology #label PIPX\ !$486-606 #domain 1-phosphatidylinositol-4,5-bisphosphate !8phosphodiesterase domain Y homology #label PIPY SUMMARY #length 997 #molecular-weight 112954 #checksum 3881 SEQUENCE /// ENTRY A55943 #type complete TITLE 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase (EC 3.1.4.11) delta-1 [validated] - human ALTERNATE_NAMES phosphoinositidase C; phospholipase C-delta-1; triphosphoinositide phosphodiesterase ORGANISM #formal_name Homo sapiens #common_name man DATE 02-Jun-2000 #sequence_revision 02-Jun-2000 #text_change 02-Jun-2000 ACCESSIONS A55943 REFERENCE A55943 !$#authors Cheng, H.F.; Jiang, M.J.; Chen, C.L.; Liu, S.M.; Wong, L.P.; !1Lomasney, J.W.; King, K. !$#journal J. Biol. Chem. (1995) 270:5495-5505 !$#title Cloning and identification of amino acid residues of human !1phospholipase Cdelta1 essential for catalysis. !$#cross-references MUID:95197554; PMID:7890667 !$#accession A55943 !'##molecule_type mRNA !'##residues 1-756 ##label CHE !'##cross-references GB:U09117; NID:g483919; PIDN:AAA73567.1; !1PID:g483920 !'##experimental_source aortic smooth muscle COMMENT The products of hydrolysis, diacylglycerol and !1D-myo-inositol 1,4,5-triphosphate, are important second !1messengers in receptor-coupled signal transduction. GENETICS !$#gene GDB:PLCD1 !'##cross-references GDB:6075994 CLASSIFICATION #superfamily 1-phosphatidylinositol-4,5-bisphosphate !1phosphodiesterase delta-1; 1-phosphatidylinositol-4, !15-bisphosphate phosphodiesterase domain X homology; !11-phosphatidylinositol-4,5-bisphosphate phosphodiesterase !1domain Y homology; calmodulin repeat homology; pleckstrin !1repeat homology; protein kinase C C2 region homology KEYWORDS duplication; EF hand; lipid degradation; phosphoric diester !1hydrolase; signal transduction FEATURE !$19-128 #domain pleckstrin repeat homology #label PLK\ !$140-172 #domain calmodulin repeat homology #label EF1\ !$176-208 #domain calmodulin repeat homology #label EF2\ !$298-440 #domain 1-phosphatidylinositol-4,5-bisphosphate !8phosphodiesterase domain X homology #label PIPX\ !$491-612 #domain 1-phosphatidylinositol-4,5-bisphosphate !8phosphodiesterase domain Y homology #label PIPY\ !$614-724 #domain protein kinase C C2 region homology #label !8KC2 SUMMARY #length 756 #molecular-weight 85762 #checksum 6735 SEQUENCE /// ENTRY B28821 #type complete TITLE 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase (EC 3.1.4.11) delta-1 - rat ALTERNATE_NAMES phosphoinositidase C; phospholipase C-delta-1; triphosphoinositide phosphodiesterase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 02-Jun-2000 ACCESSIONS B28821; I55942 REFERENCE A90899 !$#authors Suh, P.G.; Ryu, S.H.; Moon, K.H.; Suh, H.W.; Rhee, S.G. !$#journal Cell (1988) 54:161-169 !$#title Cloning and sequence of multiple forms of phospholipase C. !$#cross-references MUID:88270495; PMID:3390863 !$#accession B28821 !'##molecule_type mRNA !'##residues 1-756 ##label SUH !'##cross-references GB:M20637; GB:J03136; NID:g206219; PIDN:AAA41886.1; !1PID:g206220 !'##experimental_source brain REFERENCE I55942 !$#authors Yagisawa, H.; Tanase, H.; Nojima, H. !$#journal J. Hypertens. (1991) 9:997-1004 !$#title Phospholipase C-delta gene of the spontaneously hypertensive !1rat harbors point mutations causing amino acid substitutions !1in a catalytic domain. !$#cross-references MUID:92098966; PMID:1684614 !$#accession I55942 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-411,'M',413-422,'S',424-462,'D',464-626,'A',628,'K', !1630-667,'A',669-756 ##label YAG !'##cross-references GB:S74591; NID:g241276 !'##note this translation is not annotated in GenBank entry S74591, !1release 113.0 !'##note spontaneously hypertensive mutant COMMENT The products of hydrolysis, diacylglycerol and !1D-myo-inositol 1,4,5-triphosphate, are important second !1messengers in receptor-coupled signal transduction. CLASSIFICATION #superfamily 1-phosphatidylinositol-4,5-bisphosphate !1phosphodiesterase delta-1; 1-phosphatidylinositol-4, !15-bisphosphate phosphodiesterase domain X homology; !11-phosphatidylinositol-4,5-bisphosphate phosphodiesterase !1domain Y homology; calmodulin repeat homology; pleckstrin !1repeat homology; protein kinase C C2 region homology KEYWORDS duplication; EF hand; lipid degradation; phosphoric diester !1hydrolase; signal transduction FEATURE !$19-128 #domain pleckstrin repeat homology #label PLK\ !$140-172 #domain calmodulin repeat homology #label EF1\ !$176-208 #domain calmodulin repeat homology #label EF2\ !$298-440 #domain 1-phosphatidylinositol-4,5-bisphosphate !8phosphodiesterase domain X homology #label PIPX\ !$491-612 #domain 1-phosphatidylinositol-4,5-bisphosphate !8phosphodiesterase domain Y homology #label PIPY\ !$614-724 #domain protein kinase C C2 region homology #label !8KC2 SUMMARY #length 756 #molecular-weight 85961 #checksum 6831 SEQUENCE /// ENTRY PC4183 #type fragment TITLE 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase (EC 3.1.4.11) delta-1 - Chinese hamster (fragment) ALTERNATE_NAMES phosphoinositidase C; phospholipase C-delta-1; triphosphoinositide phosphodiesterase ORGANISM #formal_name Cricetulus griseus #common_name Chinese hamster DATE 02-Jun-2000 #sequence_revision 02-Jun-2000 #text_change 02-Jun-2000 ACCESSIONS PC4183 REFERENCE PC4183 !$#authors Leonis, M.A.; Silbert, D.F. !$#journal Biochem. Biophys. Res. Commun. (1996) 224:382-390 !$#title Genomic organization of the hamster phospholipase C-delta1 !1gene: Differential loss of separate alleles of the !1phospholipase C-delta1 gene in two fibroblast mutants !1lacking phospholipase C-delta1. !$#cross-references MUID:96295498; PMID:8702399 !$#contents fibroblast !$#accession PC4183 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-745 ##label LEO !'##cross-references GB:U50564 COMMENT The products of hydrolysis, diacylglycerol and !1D-myo-inositol 1,4,5-triphosphate, are important second !1messengers in receptor-coupled signal transduction. GENETICS !$#gene PLCdelta1 !$#introns 56/1; 132/2; 175/3; 253/1; 320/2; 368/3; 418/3; 471/3; 525/ !11; 564/1; 623/3; 668/1; 718/1 CLASSIFICATION #superfamily 1-phosphatidylinositol-4,5-bisphosphate !1phosphodiesterase delta-1; 1-phosphatidylinositol-4, !15-bisphosphate phosphodiesterase domain X homology; !11-phosphatidylinositol-4,5-bisphosphate phosphodiesterase !1domain Y homology; calmodulin repeat homology; pleckstrin !1repeat homology; protein kinase C C2 region homology KEYWORDS duplication; EF hand; lipid degradation; phosphoric diester !1hydrolase; signal transduction FEATURE !$8-117 #domain pleckstrin repeat homology #label PLK\ !$129-161 #domain calmodulin repeat homology #label EF1\ !$165-197 #domain calmodulin repeat homology #label EF2\ !$287-429 #domain 1-phosphatidylinositol-4,5-bisphosphate !8phosphodiesterase domain X homology #label PIPX\ !$480-601 #domain 1-phosphatidylinositol-4,5-bisphosphate !8phosphodiesterase domain Y homology #label PIPY\ !$603-713 #domain protein kinase C C2 region homology #label !8KC2 SUMMARY #length 745 #checksum 8835 SEQUENCE /// ENTRY S14113 #type complete TITLE 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase (EC 3.1.4.11) delta-2 - bovine ALTERNATE_NAMES phosphoinositidase C; phospholipase C-delta-2; triphosphoinositide phosphodiesterase ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 02-Jun-2000 ACCESSIONS S14113; S04944 REFERENCE S14113 !$#authors Meldrum, E.; Kriz, R.W.; Totty, N.; Parker, P.J. !$#journal Eur. J. Biochem. (1991) 196:159-165 !$#title A second gene product of the inositol-phospholipid-specific !1phospholipase C-delta subclass. !$#cross-references MUID:91160548; PMID:1848183 !$#accession S14113 !'##status preliminary !'##molecule_type mRNA !'##residues 1-764 ##label MEL !'##experimental_source brain REFERENCE S04944 !$#authors Meldrum, E.; Katan, M.; Parker, P. !$#journal Eur. J. Biochem. (1989) 182:673-677 !$#title A novel inositol-phospholipid-specific phospholipase C. !1Rapid purification and characterization. !$#cross-references MUID:89325315; PMID:2753038 !$#accession S04944 !'##status preliminary !'##molecule_type protein !'##residues 528-541,'X',543-553;659-669 ##label ME2 !'##experimental_source brain COMMENT The products of hydrolysis, diacylglycerol and !1D-myo-inositol 1,4,5-triphosphate, are important second !1messengers in receptor-coupled signal transduction. CLASSIFICATION #superfamily 1-phosphatidylinositol-4,5-bisphosphate !1phosphodiesterase delta-1; 1-phosphatidylinositol-4, !15-bisphosphate phosphodiesterase domain X homology; !11-phosphatidylinositol-4,5-bisphosphate phosphodiesterase !1domain Y homology; calmodulin repeat homology; pleckstrin !1repeat homology; protein kinase C C2 region homology KEYWORDS duplication; EF hand; lipid degradation; phosphoric diester !1hydrolase; signal transduction FEATURE !$15-122 #domain pleckstrin repeat homology #label PLK\ !$134-166 #domain calmodulin repeat homology #label EF1\ !$170-202 #domain calmodulin repeat homology #label EF2\ !$292-435 #domain 1-phosphatidylinositol-4,5-bisphosphate !8phosphodiesterase domain X homology #label PIPX\ !$489-609 #domain 1-phosphatidylinositol-4,5-bisphosphate !8phosphodiesterase domain Y homology #label PIPY\ !$611-725 #domain protein kinase C C2 region homology #label !8KC2 SUMMARY #length 764 #molecular-weight 87681 #checksum 1361 SEQUENCE /// ENTRY A44165 #type complete TITLE 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase (EC 3.1.4.11) - slime mold (Dictyostelium discoideum) ALTERNATE_NAMES phosphoinositide-specific phospholipase C ORGANISM #formal_name Dictyostelium discoideum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS A44165 REFERENCE A44165 !$#authors Drayer, A.L.; van Haastert, P.J. !$#journal J. Biol. Chem. (1992) 267:18387-18392 !$#title Molecular cloning and expression of a !1phosphoinositide-specific phospholipase C of Dictyostelium !1discoideum. !$#cross-references MUID:92406741; PMID:1326523 !$#accession A44165 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-801 ##label DRA !'##cross-references GB:M95783; NID:g167846; PIDN:AAA33235.1; !1PID:g167847 !'##note sequence extracted from NCBI backbone (NCBIP:113302) CLASSIFICATION #superfamily 1-phosphatidylinositol-4,5-bisphosphate !1phosphodiesterase delta-1; 1-phosphatidylinositol-4, !15-bisphosphate phosphodiesterase domain X homology; !11-phosphatidylinositol-4,5-bisphosphate phosphodiesterase !1domain Y homology; calmodulin repeat homology; pleckstrin !1repeat homology; protein kinase C C2 region homology KEYWORDS EF hand; phosphoprotein; phosphoric diester hydrolase FEATURE !$324-465 #domain 1-phosphatidylinositol-4,5-bisphosphate !8phosphodiesterase domain X homology #label PIPX\ !$538-656 #domain 1-phosphatidylinositol-4,5-bisphosphate !8phosphodiesterase domain Y homology #label PIPY\ !$658-769 #domain protein kinase C C2 region homology #label !8KC2 SUMMARY #length 801 #molecular-weight 91279 #checksum 3693 SEQUENCE /// ENTRY T29357 #type complete TITLE 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase (EC 3.1.4.11) delta - Caenorhabditis elegans ALTERNATE_NAMES inositol-phospholipid-specific phospholipase C ORGANISM #formal_name Caenorhabditis elegans DATE 02-Jun-2000 #sequence_revision 02-Jun-2000 #text_change 02-Jun-2000 ACCESSIONS T29357 REFERENCE Z20612 !$#authors Murray, J.; Le, T.T. !$#submission submitted to the EMBL Data Library, May 1996 !$#description The sequence of C. elegans cosmid R05G6. !$#accession T29357 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-751 ##label MUR !'##cross-references EMBL:U58746; PIDN:AAB00624.1; GSPDB:GN00022; !1CESP:R05G6.8 !'##experimental_source strain Bristol N2; clone R05G6 GENETICS !$#gene CESP:R05G6.8 !$#map_position 4 !$#introns 39/2; 132/3; 261/3; 362/1; 394/3; 516/1; 697/3 CLASSIFICATION #superfamily 1-phosphatidylinositol-4,5-bisphosphate !1phosphodiesterase delta-1; 1-phosphatidylinositol-4, !15-bisphosphate phosphodiesterase domain X homology; !11-phosphatidylinositol-4,5-bisphosphate phosphodiesterase !1domain Y homology; calmodulin repeat homology; pleckstrin !1repeat homology; protein kinase C C2 region homology KEYWORDS duplication; EF hand; phosphoric diester hydrolase FEATURE !$25-144 #domain pleckstrin repeat homology #label PLK\ !$156-188 #domain calmodulin repeat homology #label EF1\ !$192-226 #domain calmodulin repeat homology #label EF2\ !$318-460 #domain 1-phosphatidylinositol-4,5-bisphosphate !8phosphodiesterase domain X homology #label PIPX\ !$493-611 #domain 1-phosphatidylinositol-4,5-bisphosphate !8phosphodiesterase domain Y homology #label PIPY\ !$612-716 #domain protein kinase C C2 region homology #label !8KC2 SUMMARY #length 751 #molecular-weight 85868 #checksum 4447 SEQUENCE /// ENTRY S54098 #type complete TITLE 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase (EC 3.1.4.11) - Arabidopsis thaliana ALTERNATE_NAMES protein T21L8.40 ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 10-Sep-1999 #sequence_revision 26-May-2000 #text_change 26-May-2000 ACCESSIONS T12984; S54098 REFERENCE Z17586 !$#authors Choisne, N.; Robert, C.; Brottier, P.; Wincker, P.; !1Cattolico, L.; Artiguenave, F.; Saurin, W.; Weissenbach, J.; !1Mewes, H.W.; Mayer, K.F.X.; Lemcke, K.; Schueller, C.; !1Quetier, F.; Salanoubat, M. !$#submission submitted to the Protein Sequence Database, July 1999 !$#accession T12984 !'##molecule_type DNA !'##residues 1-531 ##label CHO !'##cross-references EMBL:AL096860; GSPDB:GN00061; ATSP:T21L8.40 !'##experimental_source cultivar Columbia; BAC clone T21L8 REFERENCE S54098 !$#authors Kopka, J.; Willmitzer, L.; Mueller-Roeber, B. !$#submission submitted to the EMBL Data Library, March 1995 !$#accession S54098 !'##molecule_type mRNA !'##residues 1-81,'K',83-357,'D',359-531 ##label KOP !'##cross-references EMBL:X85973; NID:g769742; PIDN:CAA59962.1; !1PID:g769743 GENETICS !$#gene Plc2; ATSP:T21L8.40 !$#map_position 3 !$#introns 102/3; 166/2; 211/3; 317/2; 356/3; 406/3; 434/3 CLASSIFICATION #superfamily Arabidopsis thaliana 1-phosphatidylinositol-4, !15-bisphosphate phosphodiesterase; 1-phosphatidylinositol-4, !15-bisphosphate phosphodiesterase domain X homology; !11-phosphatidylinositol-4,5-bisphosphate phosphodiesterase !1domain Y homology KEYWORDS phosphoric diester hydrolase FEATURE !$107-247 #domain 1-phosphatidylinositol-4,5-bisphosphate !8phosphodiesterase domain X homology #label PPX SUMMARY #length 531 #molecular-weight 61076 #checksum 2125 SEQUENCE /// ENTRY S71170 #type complete TITLE phosphoinositide-specific phospholipase C (EC 3.1.4.-) - Arabidopsis thaliana ALTERNATE_NAMES phosphodiesterase ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S71170 REFERENCE S71170 !$#authors Fukunaga, M.; Hamase, A.; Sohnaka, M.; Inoue, H.; Tsuruta, !1Y.; Nakao, M. !$#submission submitted to the EMBL Data Library, June 1995 !$#description Genetic characterization of borrelia burgdorferi sensu lato !1from Japanese ticks, ixodes tanuki, ixodes turdus, and !1ixodes columnae. !$#accession S71170 !'##molecule_type mRNA !'##residues 1-581 ##label FUK !'##cross-references EMBL:D50804; NID:g857373; PIDN:BAA09432.1; !1PID:g857374 CLASSIFICATION #superfamily Arabidopsis thaliana 1-phosphatidylinositol-4, !15-bisphosphate phosphodiesterase; 1-phosphatidylinositol-4, !15-bisphosphate phosphodiesterase domain X homology; !11-phosphatidylinositol-4,5-bisphosphate phosphodiesterase !1domain Y homology KEYWORDS phosphoric diester hydrolase FEATURE !$105-248 #domain 1-phosphatidylinositol-4,5-bisphosphate !8phosphodiesterase domain X homology #label PIPX SUMMARY #length 581 #molecular-weight 66122 #checksum 5599 SEQUENCE /// ENTRY A53970 #type complete TITLE 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase (EC 3.1.4.11) gamma-D - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 17-Mar-2000 ACCESSIONS A53970 REFERENCE A53970 !$#authors Emori, Y.; Sugaya, R.; Akimaru, H.; Higashijima, S.; !1Shishido, E.; Saigo, K.; Homma, Y. !$#journal J. Biol. Chem. (1994) 269:19474-19479 !$#title Drosophila phospholipase C-gamma expressed predominantly in !1blastoderm cells at cellularization and in endodermal cells !1during later embryonic stages. !$#cross-references MUID:94308233; PMID:8034716 !$#accession A53970 !'##status preliminary !'##molecule_type DNA !'##residues 1-1236 ##label EMO !'##cross-references GB:D29806 GENETICS !$#gene plc-gammad !'##cross-references FlyBase:FBgn0003416 CLASSIFICATION #superfamily 1-phosphatidylinositol-4,5-bisphosphate !1phosphodiesterase II; 1-phosphatidylinositol-4, !15-bisphosphate phosphodiesterase domain X homology; !11-phosphatidylinositol-4,5-bisphosphate phosphodiesterase !1domain Y homology; SH2 homology; SH3 homology KEYWORDS phosphoric diester hydrolase FEATURE !$326-468 #domain 1-phosphatidylinositol-4,5-bisphosphate !8phosphodiesterase domain X homology #label PIPX\ !$589-688 #domain SH2 homology #label SH2B\ !$701-789 #domain SH2 homology #label SH2\ !$831-879 #domain SH3 homology #label SH3\ !$979-1095 #domain 1-phosphatidylinositol-4,5-bisphosphate !8phosphodiesterase domain Y homology #label PIPY SUMMARY #length 1236 #molecular-weight 141998 #checksum 6683 SEQUENCE /// ENTRY A47257 #type complete TITLE 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase (EC 3.1.4.11) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES phosphoinositide-specific phospholipase C; protein P0357; protein YPL268w; triphosphoinositide phosphodiesterase ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A47257; A48142; A54699; S65301; S65322; S42142 REFERENCE A47257 !$#authors Yoko-o, T.; Matsui, Y.; Yagisawa, H.; Nojima, H.; Uno, I.; !1Toh-e, A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:1804-1808 !$#title The putative phosphoinositide-specific phospholipase C gene, !1PLC1, of the yeast Saccharomyces cerevisiae is important for !1cell growth. !$#cross-references MUID:93189586; PMID:8383328 !$#accession A47257 !'##molecule_type DNA !'##residues 1-869 ##label YOK !'##cross-references EMBL:D12738; NID:g287611; PIDN:BAA02230.1; !1PID:g287612 !'##note sequence extracted from NCBI backbone (NCBIN:126918, !1NCBIP:126919) REFERENCE A48142 !$#authors Payne, W.E.; Fitzgerald-Hayes, M. !$#journal Mol. Cell. Biol. (1993) 13:4351-4364 !$#title A mutation in PLC1, a candidate phosphoinositide-specific !1phospholipase C gene from Saccharomyces cerevisiae, causes !1aberrant mitotic chromosome segregation. !$#cross-references MUID:93309469; PMID:8391635 !$#accession A48142 !'##molecule_type DNA !'##residues 1-869 ##label PAY !'##cross-references EMBL:S63468; NID:g386552; PIDN:AAB27349.1; !1PID:g386553 !'##note sequence extracted from NCBI backbone (NCBIN:134649, !1NCBIP:134654) !'##note the authors did not translate the codon for residue 370 REFERENCE A54699 !$#authors Flick, J.S.; Thorner, J. !$#journal Mol. Cell. Biol. (1993) 13:5861-5876 !$#title Genetic and biochemical characterization of a !1phosphatidylinositol-specific phospholipase C in !1Saccharomyces cerevisiae. !$#cross-references MUID:93361018; PMID:8395015 !$#accession A54699 !'##molecule_type DNA !'##residues 1-158,'M',160-180,'T',182-580,'V',582-869 ##label FL2 !'##cross-references EMBL:L13036; NID:g295640; PIDN:AAA99927.1; !1PID:g295642 REFERENCE S65292 !$#authors Duesterhoeft, A.; Floeth, M.; Fritz, M.; Hilbert, H.; !1Moestl, D. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S65301 !'##molecule_type DNA !'##residues 1-869 ##label DUE !'##cross-references EMBL:Z73624; NID:g1370552; PIDN:CAA98004.1; !1PID:g1370553; GSPDB:GN00016; MIPS:YPL268w !'##experimental_source strain S288C (AB972) REFERENCE S64967 !$#authors Delius, H.; Hebling, U. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S65322 !'##molecule_type DNA !'##residues 1-869 ##label DEL !'##cross-references EMBL:Z73624; NID:g1370552; PIDN:CAA98004.1; !1PID:g1370553; GSPDB:GN00016; MIPS:YPL268w !'##experimental_source strain S288C (AB972) GENETICS !$#gene SGD:PLC1; MIPS:YPL268w !'##cross-references SGD:S0006189; MIPS:YPL268w !$#map_position 16L FUNCTION !$#description phosphoric diester hydrolase; signal transduction CLASSIFICATION #superfamily yeast 1-phosphatidylinositol-4,5-bisphosphate !1phosphodiesterase; 1-phosphatidylinositol-4,5-bisphosphate !1phosphodiesterase domain X homology; !11-phosphatidylinositol-4,5-bisphosphate phosphodiesterase !1domain Y homology KEYWORDS calcium binding; EF hand; phosphoric diester hydrolase; !1signal transduction FEATURE !$382-520 #domain 1-phosphatidylinositol-4,5-bisphosphate !8phosphodiesterase domain X homology #label PIPX\ !$586-713 #domain 1-phosphatidylinositol-4,5-bisphosphate !8phosphodiesterase domain Y homology #label PIPY SUMMARY #length 869 #molecular-weight 100547 #checksum 7069 SEQUENCE /// ENTRY S66672 #type complete TITLE phosphatidylinositol-specific phospholipase C - northern European squid ORGANISM #formal_name Loligo forbesi #common_name northern European squid DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Dec-2002 ACCESSIONS S66672; S74310; S41169 REFERENCE S66672 !$#authors Carne, A.; McGregor, R.A.; Bhatia, J.; Sivaprasadarao, A.; !1Keen, J.N.; Davies, A.; Findlay, J.B.C. !$#journal FEBS Lett. (1995) 372:243-248 !$#title A beta-subclass phosphatidylinositol-specific phospholipase !1C from squid (Loligo forbesi) photoreceptors exhibiting a !1truncated C-terminus. !$#cross-references MUID:96000215; PMID:7556677 !$#accession S66672 !'##molecule_type mRNA !'##residues 1-875 ##label CAR !'##cross-references EMBL:X76968; NID:g439518; PIDN:CAA54275.1; !1PID:g439519 !'##note the authors translated the codon AAA for residue 86 as Asp and !1AAT for residue 126 as His !$#accession S74310 !'##molecule_type protein !'##residues 90-102;278-297;756-770 ##label CAN CLASSIFICATION #superfamily Phosphatidylinositol-specific Phospholipase C; !11-phosphatidylinositol-4,5-bisphosphate phosphodiesterase !1domain X homology; 1-phosphatidylinositol-4,5-bisphosphate !1phosphodiesterase domain Y homology FEATURE !$325-471 #domain 1-phosphatidylinositol-4,5-bisphosphate !8phosphodiesterase domain X homology #label PIPX\ !$513-633 #domain 1-phosphatidylinositol-4,5-bisphosphate !8phosphodiesterase domain Y homology #label PIPY SUMMARY #length 875 #molecular-weight 98179 #checksum 9968 SEQUENCE /// ENTRY A53766 #type complete TITLE phosphoinositide-specific phospholipase C - brine shrimp ORGANISM #formal_name Artemia sp. #common_name brine shrimp DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A53766 REFERENCE A53766 !$#authors Su, X.; Chen, F.; Hokin, L.E. !$#journal J. Biol. Chem. (1994) 269:12925-12931 !$#title Cloning and expression of a novel, highly truncated !1phosphoinositide-specific phospholipase C cDNA from embryos !1of the brine shrimp, Artemia. !$#cross-references MUID:94230375; PMID:8175710 !$#accession A53766 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-489 ##label SUA !'##cross-references GB:U07936 CLASSIFICATION #superfamily brine shrimp phosphoinositide-specific !1phospholipase C; 1-phosphatidylinositol-4,5-bisphosphate !1phosphodiesterase domain Y homology FEATURE !$114-234 #domain 1-phosphatidylinositol-4,5-bisphosphate !8phosphodiesterase domain Y homology #label PIPY SUMMARY #length 489 #molecular-weight 56088 #checksum 4816 SEQUENCE /// ENTRY A53430 #type complete TITLE 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase (EC 3.1.4.11) beta-1b - rat ALTERNATE_NAMES phospholipase C beta-1b ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A53430 REFERENCE A53430 !$#authors Bahk, Y.Y.; Lee, Y.H.; Lee, T.G.; Seo, J.; Ryu, S.H.; Suh, !1P.G. !$#journal J. Biol. Chem. (1994) 269:8240-8245 !$#title Two forms of phospholipase C-beta1 generated by alternative !1splicing. !$#cross-references MUID:94179201; PMID:7510682 !$#accession A53430 !'##status preliminary; nucleic acid sequence not shown; not compared !1with conceptual translation !'##molecule_type mRNA !'##residues 1-1173 ##label BAH !'##cross-references GB:L14323 CLASSIFICATION #superfamily 1-phosphatidylinositol-4,5-bisphosphate !1phosphodiesterase I; 1-phosphatidylinositol-4,5-bisphosphate !1phosphodiesterase domain X homology; !11-phosphatidylinositol-4,5-bisphosphate phosphodiesterase !1domain Y homology KEYWORDS alternative splicing; phosphoric diester hydrolase FEATURE !$318-467 #domain 1-phosphatidylinositol-4,5-bisphosphate !8phosphodiesterase domain X homology #label PIPX\ !$539-659 #domain 1-phosphatidylinositol-4,5-bisphosphate !8phosphodiesterase domain Y homology #label PIPY SUMMARY #length 1173 #molecular-weight 133127 #checksum 5839 SEQUENCE /// ENTRY A31225 #type complete TITLE phospholipase C (EC 3.1.4.3) - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A31225 REFERENCE A31225 !$#authors Bloomquist, B.T.; Shortridge, R.D.; Schneuwly, S.; Perdew, !1M.; Montell, C.; Steller, H.; Rubin, G.; Pak, W.L. !$#journal Cell (1988) 54:723-733 !$#title Isolation of a putative phospholipase C gene of Drosophila, !1norpA, and its role in phototransduction. !$#cross-references MUID:88311074; PMID:2457447 !$#accession A31225 !'##molecule_type mRNA !'##residues 1-1095 ##label BLO !'##note the authors translated the codons TAC and CAG for residues 582 !1and 585 as Glu; TTG, GCG, and GGC for residues 583, 592, and !1593 as Ser; AAG for residue 584 as Ala; AGC for residue 586 !1as Met; TCC for residue 587 as Asn; ATC for residue 588 as !1Tyr; GAC for residue 589 as Leu; GAA for residue 590 as Lys; !1TCG for residue 591 as Gln; ATG for residue 594 as Ile; and !1AAC for residue 595 as Asp GENETICS !$#gene FlyBase:norpA !'##cross-references FlyBase:FBgn0004625 CLASSIFICATION #superfamily 1-phosphatidylinositol-4,5-bisphosphate !1phosphodiesterase I; 1-phosphatidylinositol-4,5-bisphosphate !1phosphodiesterase domain X homology; !11-phosphatidylinositol-4,5-bisphosphate phosphodiesterase !1domain Y homology KEYWORDS phosphoric diester hydrolase FEATURE !$321-469 #domain 1-phosphatidylinositol-4,5-bisphosphate !8phosphodiesterase domain X homology #label PIPX\ !$549-669 #domain 1-phosphatidylinositol-4,5-bisphosphate !8phosphodiesterase domain Y homology #label PIPY SUMMARY #length 1095 #molecular-weight 124821 #checksum 1950 SEQUENCE /// ENTRY A48047 #type complete TITLE phospholipase C (EC 3.1.4.-) beta-4 - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 02-Jun-2000 ACCESSIONS A48047; JN0691 REFERENCE A48047 !$#authors Lee, C.W.; Park, D.J.; Lee, K.H.; Kim, C.G.; Rhee, S.G. !$#journal J. Biol. Chem. (1993) 268:21318-21327 !$#title Purification, molecular cloning, and sequencing of !1phospholipase C-beta 4. !$#cross-references MUID:94012687; PMID:8407970 !$#accession A48047 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-1176 ##label LEE !'##cross-references GB:L15556; NID:g404071 !'##experimental_source brain !'##note sequence extracted from NCBI backbone (NCBIP:138517) !'##note this translation is not annotated in GenBank entry RATBETA4AA, !1release 113.0 REFERENCE JN0691 !$#authors Kim, M.J.; Bahk, Y.Y.; Min, D.S.; Lee, S.J.; Ryu, S.H.; Suh, !1P.G. !$#journal Biochem. Biophys. Res. Commun. (1993) 194:706-712 !$#title Cloning of cDNA encoding rat phospholipase C-beta4, a new !1member of the phospholipase C. !$#cross-references MUID:93343926; PMID:7688223 !$#accession JN0691 !'##molecule_type mRNA !'##residues 1-254,'M',256-307,'A',309-416,'E',418-469,'K',471-504, !1506-545,'DE',548-734,'L',736-741,'H',743-764,'M',766-776, !1'N',778-828,'F',830-843,'Y',845-916,'T',918-1013,'A', !11015-1023,'Q',1025-1043,'M',1045-1176 ##label KIM !'##cross-references GB:L18962 !'##experimental_source brain !'##note the authors translated the codon AAC for residue 140 as Lys, !1CAG for residue 1023 as Glu, and ATG for residue 1043 as Leu COMMENT This enzyme belongs a member of the phosphoinositide !1specific phospholipase C, which catalyzes the hydrolysis of !1phosphatidylinositol 4,5-bisphosphate and produces the !1intracellular second messenger molecules, inositol 1,4, !15-triphosphate and diacylglycerol in response to the binding !1of various ligands to the receptors in signal transduction !1pathway. CLASSIFICATION #superfamily 1-phosphatidylinositol-4,5-bisphosphate !1phosphodiesterase I; 1-phosphatidylinositol-4,5-bisphosphate !1phosphodiesterase domain X homology; !11-phosphatidylinositol-4,5-bisphosphate phosphodiesterase !1domain Y homology KEYWORDS phosphoric diester hydrolase FEATURE !$315-463 #domain 1-phosphatidylinositol-4,5-bisphosphate !8phosphodiesterase domain X homology #label PIPX\ !$565-685 #domain 1-phosphatidylinositol-4,5-bisphosphate !8phosphodiesterase domain Y homology #label PIPY SUMMARY #length 1176 #molecular-weight 134533 #checksum 726 SEQUENCE /// ENTRY B40879 #type complete TITLE phospholipase C (EC 3.1.4.3), neuronal, long splice form - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B40879 REFERENCE A40879 !$#authors Shortridge, R.D.; Yoon, J.; Lending, C.R.; Bloomquist, B.T.; !1Perdew, M.H.; Pak, W.L. !$#journal J. Biol. Chem. (1991) 266:12474-12480 !$#title A Drosophila phospholipase C gene that is expressed in the !1central nervous system. !$#cross-references MUID:91286274; PMID:2061323 !$#accession B40879 !'##status preliminary !'##molecule_type mRNA !'##residues 1-1312 ##label SHO !'##cross-references GB:M60453; NID:g158132; PIDN:AAA28820.1; !1PID:g158133 GENETICS !$#gene FlyBase:Plc21C !'##cross-references FlyBase:FBgn0004611 CLASSIFICATION #superfamily fruit fly neuronal phospholipase C; !11-phosphatidylinositol-4,5-bisphosphate phosphodiesterase !1domain X homology; 1-phosphatidylinositol-4,5-bisphosphate !1phosphodiesterase domain Y homology KEYWORDS alternative splicing; phosphoric diester hydrolase FEATURE !$320-466 #domain 1-phosphatidylinositol-4,5-bisphosphate !8phosphodiesterase domain X homology #label PIPX\ !$598-718 #domain 1-phosphatidylinositol-4,5-bisphosphate !8phosphodiesterase domain Y homology #label PIPY SUMMARY #length 1312 #molecular-weight 145730 #checksum 3088 SEQUENCE /// ENTRY ESECPC #type complete TITLE 2',3'-cyclic-nucleotide 2'-phosphodiesterase (EC 3.1.4.16) precursor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 10-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS H65232; S56438; A26398; PS0149 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65232 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-647 ##label BLAT !'##cross-references GB:AE000492; GB:U00096; NID:g1790649; !1PIDN:AAC77170.1; PID:g1790658; UWGP:b4213 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56438 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-647 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97109.1; !1PID:g537054 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A26398 !$#authors Liu, J.; Burns, D.M.; Beacham, I.R. !$#journal J. Bacteriol. (1986) 165:1002-1010 !$#title Isolation and sequence analysis of the gene (cpdB) encoding !1periplasmic 2',3'-cyclic phosphodiesterase. !$#cross-references MUID:86139859; PMID:3005231 !$#accession A26398 !'##molecule_type DNA !'##residues 1-315,'G',317-527,'ASRLIRTPCSWLPPITI',546,'LT',549,'QIC', !1553-647 ##label LIU !'##cross-references EMBL:M13464; NID:g145583; PIDN:AAA23597.1; !1PID:g145584 COMMENT This bifunctional enzyme catalyzes two consecutive reactions !1converting 2',3'-cyclic-nucleotide to 3'-nucleotide and then !13'-nucleotide to nucleic acid and phosphate. Two kinetically !1distinguishable active sites for two corresponding !1substrates can be identified. GENETICS !$#gene cpdB !$#map_position 96 min CLASSIFICATION #superfamily 2',3'-cyclic-nucleotide 2'-phosphodiesterase; !12',3'-cyclic-nucleotide 2'-phosphodiesterase homology; !1phosphoesterase core homology KEYWORDS multifunctional enzyme; periplasmic space; phosphoric !1diester hydrolase FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-647 #product 2',3'-cyclic-nucleotide 2'-phosphodiesterase !8#status predicted #label MAT\ !$22-595 #domain 2',3'-cyclic-nucleotide 2'-phosphodiesterase !8homology #label CPDB\ !$25-118 #domain phosphoesterase core homology #label PEC SUMMARY #length 647 #molecular-weight 70832 #checksum 6512 SEQUENCE /// ENTRY G86118 #type complete TITLE 2',3'-cyclic-nucleotide 2'-phosphodiesterase (EC 3.1.4.16) cpdB [similarity] - Escherichia coli (strain O157:H7, substrain EDL933) ORGANISM #formal_name Escherichia coli DATE 03-Aug-2001 #sequence_revision 03-Aug-2001 #text_change 14-Sep-2001 ACCESSIONS G86118 REFERENCE A85480 !$#authors Perna, N.T.; Plunkett III, G.; Burland, V.; Mau, B.; !1Glasner, J.D.; Rose, D.J.; Mayhew, G.F.; Evans, P.S.; !1Gregor, J.; Kirkpatrick, H.A.; Posfai, G.; Hackett, J.; !1Klink, S.; Boutin, A.; Shao, Y.; Miller, L.; Grotbeck, E.J.; !1Davis, N.W.; Lim, A.; Dimalanta, E.; Potamousis, K.; !1Apodaca, J.; Anantharaman, T.S.; Lin, J.; Yen, G.; Schwartz, !1D.C.; Welch, R.A.; Blattner, F.R. !$#journal Nature (2001) 409:529-533 !$#title Genome sequence of enterohemorrhagic Escherichia coli !1O157:H7. !$#cross-references MUID:21074935; PMID:11206551 !$#accession G86118 !'##molecule_type DNA !'##residues 1-647 ##label STO !'##cross-references GB:AE005174; NID:g12519209; PIDN:AAG59411.1; !1GSPDB:GN00145; UWGP:Z5824 !'##experimental_source strain O157:H7, substrain EDL933 GENETICS !$#gene cpdB CLASSIFICATION #superfamily 2',3'-cyclic-nucleotide 2'-phosphodiesterase; !12',3'-cyclic-nucleotide 2'-phosphodiesterase homology; !1phosphoesterase core homology KEYWORDS phosphoric diester hydrolase FEATURE !$22-595 #domain 2',3'-cyclic-nucleotide 2'-phosphodiesterase !8homology #label CPDB\ !$25-118 #domain phosphoesterase core homology #label PEC SUMMARY #length 647 #molecular-weight 70905 #checksum 6638 SEQUENCE /// ENTRY G91277 #type complete TITLE 2',3'-cyclic-nucleotide 2'-phosphodiesterase (EC 3.1.4.16) cpdB [similarity] - Escherichia coli (strain O157:H7, substrain RIMD 0509952) ORGANISM #formal_name Escherichia coli DATE 18-Jul-2001 #sequence_revision 18-Jul-2001 #text_change 24-Aug-2001 ACCESSIONS G91277 REFERENCE A99629 !$#authors Hayashi, T.; Makino, K.; Ohnishi, M.; Kurokawa, K.; Ishii, !1K.; Yokoyama, K.; Han, C.G.; Ohtsubo, E.; Nakayama, K.; !1Murata, T.; Tanaka, M.; Tobe, T.; Iida, T.; Takami, H.; !1Honda, T.; Sasakawa, C.; Ogasawara, N.; Yasunaga, T.; !1Kuhara, S.; Shiba, T.; Hattori, M.; Shinagawa, H. !$#journal DNA Res. (2001) 8:11-22 !$#title Complete genome sequence of enterohemorrhagic Escherichia !1coli O157:H7 and genomic comparison with a laboratory strain !1K-12. !$#cross-references MUID:21156231; PMID:11258796 !$#accession G91277 !'##molecule_type DNA !'##residues 1-647 ##label HAY !'##cross-references GB:BA000007; PIDN:BAB38614.1; PID:g13364668; !1GSPDB:GN00154 !'##experimental_source strain O157:H7, substrain RIMD 0509952 GENETICS !$#gene cpdB; ECs5191 CLASSIFICATION #superfamily 2',3'-cyclic-nucleotide 2'-phosphodiesterase; !12',3'-cyclic-nucleotide 2'-phosphodiesterase homology; !1phosphoesterase core homology KEYWORDS phosphoric diester hydrolase FEATURE !$22-595 #domain 2',3'-cyclic-nucleotide 2'-phosphodiesterase !8homology #label CPDB\ !$25-118 #domain phosphoesterase core homology #label PEC SUMMARY #length 647 #molecular-weight 70905 #checksum 6638 SEQUENCE /// ENTRY S52695 #type complete TITLE 2',3'-cyclic-nucleotide 2'-phosphodiesterase (EC 3.1.4.16) precursor - Yersinia enterocolitica ORGANISM #formal_name Yersinia enterocolitica DATE 19-May-1995 #sequence_revision 01-Sep-1995 #text_change 21-Jan-2000 ACCESSIONS S52695 REFERENCE S52695 !$#authors Truelzsch, K.S. !$#submission submitted to the EMBL Data Library, March 1995 !$#accession S52695 !'##molecule_type DNA !'##residues 1-652 ##label TRU !'##cross-references EMBL:X85742; NID:g747912; PIDN:CAA59745.1; !1PID:g747913 COMMENT In E. coli the enzyme is bifunctional, catalyzing two !1consecutive reactions converting 2',3'-cyclic-nucleotide to !13'-nucleotide and then 3'-nucleotide to nucleic acid and !1phosphate. Two kinetically distinguishable active sites for !1two corresponding substrates can be identified. GENETICS !$#gene cpdB CLASSIFICATION #superfamily 2',3'-cyclic-nucleotide 2'-phosphodiesterase; !12',3'-cyclic-nucleotide 2'-phosphodiesterase homology; !1phosphoesterase core homology KEYWORDS multifunctional enzyme; periplasmic space; phosphoric !1diester hydrolase FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-652 #product 2',3'-cyclic-nucleotide 2'-phosphodiesterase !8#status predicted #label MAT\ !$27-600 #domain 2',3'-cyclic-nucleotide 2'-phosphodiesterase !8homology #label CPDB\ !$30-123 #domain phosphoesterase core homology #label PEC SUMMARY #length 652 #molecular-weight 71491 #checksum 6368 SEQUENCE /// ENTRY A64079 #type complete TITLE 2',3'-cyclic-nucleotide 2'-phosphodiesterase (EC 3.1.4.16) precursor - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 18-Aug-1995 #sequence_revision 18-Aug-1995 #text_change 21-Jan-2000 ACCESSIONS A64079 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession A64079 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-657 ##label TIGR !'##cross-references GB:U32740; GB:L42023; NID:g1573572; !1PIDN:AAC22242.1; PID:g1573573; TIGR:HI0583 COMMENT In E. coli the enzyme is bifunctional, catalyzing two !1consecutive reactions converting 2',3'-cyclic-nucleotide to !13'-nucleotide and then 3'-nucleotide to nucleic acid and !1phosphate. Two kinetically distinguishable active sites for !1two corresponding substrates can be identified. CLASSIFICATION #superfamily 2',3'-cyclic-nucleotide 2'-phosphodiesterase; !12',3'-cyclic-nucleotide 2'-phosphodiesterase homology; !1phosphoesterase core homology KEYWORDS multifunctional enzyme; periplasmic space; phosphoric !1diester hydrolase FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-657 #product 2',3'-cyclic-nucleotide 2'-phosphodiesterase !8#status predicted #label MAT\ !$32-605 #domain 2',3'-cyclic-nucleotide 2'-phosphodiesterase !8homology #label CPDB\ !$35-128 #domain phosphoesterase core homology #label PEC SUMMARY #length 657 #molecular-weight 72763 #checksum 9806 SEQUENCE /// ENTRY H82059 #type complete TITLE 2',3'-cyclic-nucleotide 2'-phosphodiesterase (EC 3.1.4.16) VC2562 [similarity] - Vibrio cholerae (strain N16961 serogroup O1) ORGANISM #formal_name Vibrio cholerae DATE 03-Aug-2001 #sequence_revision 03-Aug-2001 #text_change 03-Aug-2001 ACCESSIONS H82059 REFERENCE A82035 !$#authors Heidelberg, J.F.; Eisen, J.A.; Nelson, W.C.; Clayton, R.A.; !1Gwinn, M.L.; Dodson, R.J.; Haft, D.H.; Hickey, E.K.; !1Peterson, J.D.; Umayam, L.A.; Gill, S.R.; Nelson, K.E.; !1Read, T.D.; Tettelin, H.; Richardson, D.; Ermolaeva, M.D.; !1Vamathevan, J.; Bass, S.; Qin, H.; Dragoi, I.; Sellers, P.; !1McDonald, L.; Utterback, T.; Fleishmann, R.D.; Nierman, !1W.C.; White, O.; Salzberg, S.L.; Smith, H.O.; Colwell, R.R.; !1Mekalanos, J.J.; Venter, J.C.; Fraser, C.M. !$#journal Nature (2000) 406:477-483 !$#title DNA Sequence of both chromosomes of the cholera pathogen !1Vibrio cholerae. !$#cross-references MUID:20406833; PMID:10952301 !$#accession H82059 !'##molecule_type DNA !'##residues 1-681 ##label HEI !'##cross-references GB:AE004325; GB:AE003852; NID:g9657147; !1PIDN:AAF95703.1; GSPDB:GN00126; TIGR:VC2562 !'##experimental_source serogroup O1; strain N16961; biotype El Tor GENETICS !$#gene VC2562 !$#map_position 1 CLASSIFICATION #superfamily 2',3'-cyclic-nucleotide 2'-phosphodiesterase; !12',3'-cyclic-nucleotide 2'-phosphodiesterase homology; !1phosphoesterase core homology KEYWORDS phosphoric diester hydrolase FEATURE !$56-629 #domain 2',3'-cyclic-nucleotide 2'-phosphodiesterase !8homology #label CPDB\ !$59-152 #domain phosphoesterase core homology #label PEC SUMMARY #length 681 #molecular-weight 75031 #checksum 9194 SEQUENCE /// ENTRY B75360 #type complete TITLE 2',3'-cyclic-nucleotide 2'-phosphodiesterase (EC 3.1.4.16) DR1736 [similarity] - Deinococcus radiodurans (strain R1) ORGANISM #formal_name Deinococcus radiodurans DATE 03-Aug-2001 #sequence_revision 03-Aug-2001 #text_change 03-Aug-2001 ACCESSIONS B75360 REFERENCE A75250 !$#authors White, O.; Eisen, J.A.; Heidelberg, J.F.; Hickey, E.K.; !1Peterson, J.D.; Dodson, R.J.; Haft, D.H.; Gwinn, M.L.; !1Nelson, W.C.; Richardson, D.L.; Moffat, K.S.; Qin, H.; !1Jiang, L.; Pamphile, W.; Crosby, M.; Shen, M.; Vamathevan, !1J.J.; Lam, P.; McDonald, L.; Utterback, T.; Zalewski, C.; !1Makarova, K.S.; Aravind, L.; Daly, M.J.; Minton, K.W.; !1Fleischmann, R.D.; Ketchum, K.A.; Nelson, K.E.; Salzberg, !1S.; Smith, H.O.; Venter, J.C.; Fraser, C.M. !$#journal Science (1999) 286:1571-1577 !$#title Genome sequence of the radioresistant bacterium Deinococcus !1radiodurans R1. !$#cross-references MUID:20036896; PMID:10567266 !$#accession B75360 !'##molecule_type DNA !'##residues 1-678 ##label WHI !'##cross-references GB:AE002015; GB:AE000513; NID:g6459504; !1PIDN:AAF11292.1; PID:g6459508; TIGR:DR1736; GSPDB:GN00077 !'##experimental_source strain R1 GENETICS !$#gene DR1736 !$#map_position 1 CLASSIFICATION #superfamily 2',3'-cyclic-nucleotide 2'-phosphodiesterase; !12',3'-cyclic-nucleotide 2'-phosphodiesterase homology; !1phosphoesterase core homology KEYWORDS phosphoric diester hydrolase FEATURE !$64-637 #domain 2',3'-cyclic-nucleotide 2'-phosphodiesterase !8homology #label CN2\ !$67-161 #domain phosphoesterase core homology #label PEC SUMMARY #length 678 #molecular-weight 73271 #checksum 6664 SEQUENCE /// ENTRY H64532 #type complete TITLE 2',3'-cyclic-nucleotide 2'-phosphodiesterase (EC 3.1.4.16) precursor - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 09-Aug-1997 #sequence_revision 09-Aug-1997 #text_change 11-Jun-1999 ACCESSIONS H64532 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession H64532 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-581 ##label TOM !'##cross-references GB:AE000532; GB:AE000511; NID:g2313184; !1PIDN:AAD07174.1; PID:g2313187; TIGR:HP0104 COMMENT In E. coli the enzyme is bifunctional, catalyzing two !1consecutive reactions converting 2',3'-cyclic-nucleotide to !13'-nucleotide and then 3'-nucleotide to nucleic acid and !1phosphate. Two kinetically distinguishable active sites for !1two corresponding substrates can be identified. GENETICS !$#gene HP0104 CLASSIFICATION #superfamily 2',3'-cyclic-nucleotide 2'-phosphodiesterase; !12',3'-cyclic-nucleotide 2'-phosphodiesterase homology; !1phosphoesterase core homology KEYWORDS multifunctional enzyme; periplasmic space; phosphoric !1diester hydrolase FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-581 #product 2',3'-cyclic-nucleotide 2'-phosphodiesterase !8#status predicted #label MAT\ !$21-537 #domain 2',3'-cyclic-nucleotide 2'-phosphodiesterase !8homology #label CPDB SUMMARY #length 581 #molecular-weight 65798 #checksum 848 SEQUENCE /// ENTRY B71973 #type complete TITLE 2',3'-cyclic-nucleotide 2'-phosphodiesterase (EC 3.1.4.16) cpdB [similarity] - Helicobacter pylori (strain J99) ORGANISM #formal_name Helicobacter pylori #variety strain J99 DATE 03-Aug-2001 #sequence_revision 03-Aug-2001 #text_change 03-Aug-2001 ACCESSIONS B71973 REFERENCE A71800 !$#authors Alm, R.A.; Ling, L.S.L.; Moir, D.T.; King, B.L.; Brown, !1E.D.; Doig, P.C.; Smith, D.R.; Noonan, B.; Guild, B.C.; !1deJonge, B.L.; Carmel, G.; Tummino, P.J.; Caruso, A.; !1Uria-Nickelsen, M.; Mills, D.M.; Ives, C.; Gibson, R.; !1Merberg, D.; Mills, S.D.; Jiang, Q.; Taylor, D.E.; Vovis, !1G.F.; Trust, T.J. !$#journal Nature (1999) 397:176-180 !$#title Genomic sequence comparison of two unrelated isolates of the !1human gastric pathogen Helicobacter pylori. !$#cross-references MUID:99120557; PMID:9923682 !$#accession B71973 !'##molecule_type DNA !'##residues 1-581 ##label ARN !'##cross-references GB:AE001449; GB:AE001439; NID:g4154604; !1PIDN:AAD05687.1; PID:g4154615 !'##experimental_source strain J99 GENETICS !$#gene cpdB CLASSIFICATION #superfamily 2',3'-cyclic-nucleotide 2'-phosphodiesterase; !12',3'-cyclic-nucleotide 2'-phosphodiesterase homology; !1phosphoesterase core homology KEYWORDS phosphoric diester hydrolase FEATURE !$21-537 #domain 2',3'-cyclic-nucleotide 2'-phosphodiesterase !8homology #label CPDB\ !$24-111 #domain phosphoesterase core homology #label PEC SUMMARY #length 581 #molecular-weight 65582 #checksum 866 SEQUENCE /// ENTRY T35760 #type complete TITLE 2',3'-cyclic-nucleotide 2'-phosphodiesterase (EC 3.1.4.16) SC7H2.29 [similarity] - Streptomyces coelicolor ORGANISM #formal_name Streptomyces coelicolor DATE 03-Aug-2001 #sequence_revision 03-Aug-2001 #text_change 03-Aug-2001 ACCESSIONS T35760 REFERENCE Z21588 !$#authors Saunders, D.C.; Harris, D.; Bentley, S.D.; Parkhill, J.; !1Barrell, B.G.; Rajandream, M.A. !$#submission submitted to the EMBL Data Library, August 1999 !$#accession T35760 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-602 ##label SAU !'##cross-references EMBL:AL109732; PIDN:CAB52071.1; GSPDB:GN00070; !1SCOEDB:SC7H2.29 !'##experimental_source strain A3(2) GENETICS !$#gene SCOEDB:SC7H2.29 CLASSIFICATION #superfamily 2',3'-cyclic-nucleotide 2'-phosphodiesterase; !12',3'-cyclic-nucleotide 2'-phosphodiesterase homology; !1phosphoesterase core homology KEYWORDS phosphoric diester hydrolase FEATURE !$46-594 #domain 2',3'-cyclic-nucleotide 2'-phosphodiesterase !8homology #label CPDB\ !$49-152 #domain phosphoesterase core homology #label PEC SUMMARY #length 602 #molecular-weight 65030 #checksum 906 SEQUENCE /// ENTRY E89775 #type complete TITLE 2',3'-cyclic-nucleotide 2'-phosphodiesterase (EC 3.1.4.16) SA0140 [similarity] - Staphylococcus aureus (strain N315) ORGANISM #formal_name Staphylococcus aureus DATE 03-Aug-2001 #sequence_revision 03-Aug-2001 #text_change 22-Oct-2001 ACCESSIONS E89775 REFERENCE A89758 !$#authors Kuroda, M.; Ohta, T.; Uchiyama, I.; Baba, T.; Yuzawa, H.; !1Kobayashi, I.; Cui, L.; Oguchi, A.; Aoki, K.; Nagai, Y.; !1Lian, J.; Ito, T.; Kanamori, M.; Matsumaru, H.; Maruyama, !1A.; Murakami, H.; Hosoyama, A.; Mizutani-Ui, Y.; Kobayashi, !1N.; Sawano, T.; Inoue, R.; Kaito, C.; Sekimizu, K.; !1Hirakawa, H.; Kuhara, S.; Goto, S.; Yabuzaki, J.; Kanehisa, !1M.; Yamashita, A.; Oshima, K.; Furuya, K.; Yoshino, C.; !1Shiba, T.; Hattori, M.; Ogasawara, N.; Hayashi, H.; !1Hiramatsu, K. !$#journal Lancet (2001) 357:1225-1240 !$#title Whole genome sequencing of meticillin-resistant !1Stapylococcus aureus. !$#cross-references MUID:21311952; PMID:11418146 !$#accession E89775 !'##molecule_type DNA !'##residues 1-511 ##label KUR !'##cross-references GB:BA000018; NID:g13700061; PIDN:BAB41360.1; !1GSPDB:GN00149 !'##experimental_source strain N315 GENETICS !$#gene SA0140 CLASSIFICATION #superfamily 2',3'-cyclic-nucleotide 2'-phosphodiesterase; !12',3'-cyclic-nucleotide 2'-phosphodiesterase homology; !1phosphoesterase core homology KEYWORDS phosphoric diester hydrolase FEATURE !$2-501 #domain 2',3'-cyclic-nucleotide 2'-phosphodiesterase !8homology #label CPDB\ !$5-95 #domain phosphoesterase core homology #label PEC SUMMARY #length 511 #molecular-weight 57941 #checksum 7563 SEQUENCE /// ENTRY G86662 #type complete TITLE 2',3'-cyclic-nucleotide 2'-phosphodiesterase (EC 3.1.4.16) ycjM [similarity] - Lactococcus lactis subsp. lactis (strain IL1403) ORGANISM #formal_name Lactococcus lactis subsp. lactis DATE 03-Aug-2001 #sequence_revision 03-Aug-2001 #text_change 03-Aug-2001 ACCESSIONS G86662 REFERENCE A86625 !$#authors Bolotin, A.; Wincker, P.; Mauger, S.; Jaillon, O.; Malarme, !1K.; Weissenbach, J.; Ehrlich, S.D.; Sorokin, A. !$#journal Genome Res. (2001) 11:731-753 !$#title The complete genome sequence of the lactic acid bacterium !1Lactococcus lactis ssp. lactis IL1403. !$#cross-references MUID:21235186; PMID:11337471 !$#accession G86662 !'##molecule_type DNA !'##residues 1-519 ##label STO !'##cross-references GB:AE005176; NID:g12723167; PIDN:AAK04401.1; !1GSPDB:GN00146 !'##experimental_source strain IL1403 GENETICS !$#gene ycjM CLASSIFICATION #superfamily 2',3'-cyclic-nucleotide 2'-phosphodiesterase; !12',3'-cyclic-nucleotide 2'-phosphodiesterase homology; !1phosphoesterase core homology KEYWORDS phosphoric diester hydrolase FEATURE !$1-517 #domain 2',3'-cyclic-nucleotide 2'-phosphodiesterase !8homology #label CPDB\ !$4-99 #domain phosphoesterase core homology #label PEC SUMMARY #length 520 #molecular-weight 58527 #checksum 4233 SEQUENCE /// ENTRY JC6129 #type complete TITLE 3',5'-cyclic-nucleotide phosphodiesterase (EC 3.1.4.17) 1B, calmodulin-dependent, 63K splice form - human ALTERNATE_NAMES 63K calmodulin-stimulated phosphodiesterase, brain; CAM-PDE1B1 ORGANISM #formal_name Homo sapiens #common_name man DATE 20-Aug-1999 #sequence_revision 20-Aug-1999 #text_change 21-Jul-2000 ACCESSIONS JC6129; G02260 REFERENCE JC6129 !$#authors Jiang, X.; Li, J.; Paskind, M.; Epstein, P.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1996) 93:11236-11241 !$#title Inhibition of calmodulin-dependent phosphodiesterase induces !1apoptosis in human leukemic cells. !$#cross-references MUID:97008163; PMID:8855339 !$#accession JC6129 !'##molecule_type mRNA !'##residues 1-536 ##label JIA !'##cross-references GB:U56976; NID:g1621591; PIDN:AAC50769.1; !1PID:g1621592 !'##experimental_source lymphoblastoid B-cell REFERENCE H00937 !$#authors Houslay, M.D.; Erdogan, S.; Rena, G.; Sullivan, M. !$#submission submitted to the EMBL Data Library, November 1995 !$#accession G02260 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 201-203,'W',205-358,'S',360-384 ##label HOU !'##cross-references EMBL:U40584; NID:g1110534; PID:g1110535 COMMENT This enzyme is a useful target for inducing the death of !1leaukemic cells, and the inhibition of this enzyme induces !1apoptosis of lymphoblastoid and leukemic cells. GENETICS !$#gene GDB:PDE1B; PDES1B !'##cross-references GDB:120264; OMIM:171891 !$#map_position 16p13.11 CLASSIFICATION #superfamily 3',5'-cyclic-nucleotide phosphodiesterase 1B, !1calmodulin-dependent; 3',5'-cyclic-nucleotide !1phosphodiesterase homology KEYWORDS alternative splicing; calmodulin binding; cGMP binding; !1phosphoric diester hydrolase FEATURE !$222-439 #domain 3',5'-cyclic-nucleotide phosphodiesterase !8homology #label CNPD SUMMARY #length 536 #molecular-weight 61379 #checksum 2700 SEQUENCE /// ENTRY A44162 #type complete TITLE 3',5'-cyclic-nucleotide phosphodiesterase (EC 3.1.4.17) 1B, calmodulin-dependent, 63K splice form - bovine ALTERNATE_NAMES 63K calmodulin-stimulated phosphodiesterase, brain; CAM-PDE1B1 ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 20-Aug-1999 #sequence_revision 20-Aug-1999 #text_change 05-Nov-1999 ACCESSIONS A44162; B40283 REFERENCE A44162 !$#authors Bentley, J.K.; Kadlecek, A.; Sherbert, C.H.; Seger, D.; !1Sonnenburg, W.K.; Charbonneau, H.; Novack, J.P.; Beavo, J.A. !$#journal J. Biol. Chem. (1992) 267:18676-18682 !$#title Molecular cloning of cDNA encoding a "63"-kDa !1calmodulin-stimulated phosphodiesterase from bovine brain. !$#cross-references MUID:92406781; PMID:1326531 !$#accession A44162 !'##molecule_type mRNA !'##residues 1-534 ##label BEN !'##cross-references GB:M94867; NID:g162782; PIDN:AAA74558.1; !1PID:g162783 !'##experimental_source brain !'##note sequence extracted from NCBI backbone (NCBIP:113352) REFERENCE A40283 !$#authors Novack, J.P.; Charbonneau, H.; Bentley, J.K.; Walsh, K.A.; !1Beavo, J.A. !$#journal Biochemistry (1991) 30:7940-7947 !$#title Sequence comparison of the 63-, 61-, and 59-kDa !1calmodulin-dependent cyclic nucleotide phosphodiesterases. !$#cross-references MUID:91329366; PMID:1651112 !$#accession B40283 !'##molecule_type protein !'##residues 29-45,'IP',48,'R',50-52,'IS',55-85;196-215;277,'D',279,'T', !1281-287,'T',289-292;345-356,358-396 ##label NOV !'##experimental_source brain COMMENT This enzyme is a useful target for inducing the death of !1leukemic cells, and the inhibition of this enzyme induces !1apoptosis of lymphoblastoid and leukemic cells. CLASSIFICATION #superfamily 3',5'-cyclic-nucleotide phosphodiesterase 1B, !1calmodulin-dependent; 3',5'-cyclic-nucleotide !1phosphodiesterase homology KEYWORDS alternative splicing; calmodulin binding; cGMP binding; !1phosphoric diester hydrolase FEATURE !$220-437 #domain 3',5'-cyclic-nucleotide phosphodiesterase !8homology #label CNPD SUMMARY #length 534 #molecular-weight 61006 #checksum 3098 SEQUENCE /// ENTRY A46378 #type complete TITLE 3',5'-cyclic-nucleotide phosphodiesterase (EC 3.1.4.17) 1B, calmodulin-dependent, 63K splice form - mouse ALTERNATE_NAMES 63K calmodulin-stimulated phosphodiesterase, brain; CAM-PDE1B1 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 20-Aug-1999 #sequence_revision 20-Aug-1999 #text_change 21-Jan-2000 ACCESSIONS A46378; B44161 REFERENCE A46378 !$#authors Polli, J.W.; Kincaid, R.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:11079-11083 !$#title Molecular cloning of DNA encoding a calmodulin-dependent !1phosphodiesterase enriched in striatum. !$#cross-references MUID:93066388; PMID:1332068 !$#accession A46378 !'##molecule_type mRNA; protein !'##residues 1-535 ##label POL !'##cross-references GB:L01695; NID:g200269; PIDN:AAA39902.1; !1PID:g200270 !'##experimental_source brain !'##note sequence extracted from NCBI backbone (NCBIN:118901, !1NCBIP:118903) REFERENCE A44161 !$#authors Repaske, D.R.; Swinnen, J.V.; Jin, S.L.; Van Wyk, J.J.; !1Conti, M. !$#journal J. Biol. Chem. (1992) 267:18683-18688 !$#title A polymerase chain reaction strategy to identify and clone !1cyclic nucleotide phosphodiesterase cDNAs. Molecular cloning !1of the cDNA encoding the 63-kDa calmodulin-dependent !1phosphodiesterase. !$#cross-references MUID:92406782; PMID:1326532 !$#accession B44161 !'##molecule_type mRNA !'##residues 221-223,'R',225-336 ##label REP !'##cross-references GB:M94538; NID:g192368; PIDN:AAA37367.1; !1PID:g192369 !'##note sequence extracted from NCBI backbone (NCBIP:113365) CLASSIFICATION #superfamily 3',5'-cyclic-nucleotide phosphodiesterase 1B, !1calmodulin-dependent; 3',5'-cyclic-nucleotide !1phosphodiesterase homology KEYWORDS alternative splicing; calmodulin binding; cGMP binding; !1phosphoric diester hydrolase FEATURE !$221-438 #domain 3',5'-cyclic-nucleotide phosphodiesterase !8homology #label CNP SUMMARY #length 535 #molecular-weight 61225 #checksum 2774 SEQUENCE /// ENTRY A44161 #type complete TITLE 3',5'-cyclic-nucleotide phosphodiesterase (EC 3.1.4.17) 1B, calmodulin-dependent, 63K splice form - rat ALTERNATE_NAMES 63K calmodulin-stimulated phosphodiesterase, brain; CAM-PDE1B1 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 20-Aug-1999 #sequence_revision 20-Aug-1999 #text_change 05-Nov-1999 ACCESSIONS A44161 REFERENCE A44161 !$#authors Repaske, D.R.; Swinnen, J.V.; Jin, S.L.; Van Wyk, J.J.; !1Conti, M. !$#journal J. Biol. Chem. (1992) 267:18683-18688 !$#title A polymerase chain reaction strategy to identify and clone !1cyclic nucleotide phosphodiesterase cDNAs. Molecular cloning !1of the cDNA encoding the 63-kDa calmodulin-dependent !1phosphodiesterase. !$#cross-references MUID:92406782; PMID:1326532 !$#accession A44161 !'##molecule_type mRNA !'##residues 1-535 ##label REP !'##cross-references GB:M94537; NID:g203268; PIDN:AAA16530.1; !1PID:g203269 !'##experimental_source brain !'##note sequence extracted from NCBI backbone (NCBIP:113357) COMMENT This enzyme is a useful target for inducing the death of !1leukemic cells, and the inhibition of this enzyme induces !1apoptosis of lymphoblastoid and leukemic cells. CLASSIFICATION #superfamily 3',5'-cyclic-nucleotide phosphodiesterase 1B, !1calmodulin-dependent; 3',5'-cyclic-nucleotide !1phosphodiesterase homology KEYWORDS alternative splicing; calmodulin binding; cGMP binding; !1phosphoric diester hydrolase FEATURE !$221-438 #domain 3',5'-cyclic-nucleotide phosphodiesterase !8homology #label CNPD SUMMARY #length 535 #molecular-weight 61259 #checksum 4991 SEQUENCE /// ENTRY A45334 #type complete TITLE 3',5'-cyclic-nucleotide phosphodiesterase (EC 3.1.4.17) 1A, calmodulin-dependent, 61K brain form - bovine ALTERNATE_NAMES 61K cyclic-nucleotide phosphodiesterase, brain ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 20-Aug-1999 #sequence_revision 20-Aug-1999 #text_change 05-Nov-1999 ACCESSIONS A45334; A40282; A26650; A54958 REFERENCE A45334 !$#authors Sonnenburg, W.K.; Seger, D.; Beavo, J.A. !$#journal J. Biol. Chem. (1993) 268:645-652 !$#title Molecular cloning of a cDNA encoding the "61-kDa" !1calmodulin-stimulated cyclic nucleotide phosphodiesterase. !1Tissue-specific expression of structurally related isoforms. !$#cross-references MUID:93107074; PMID:7678006 !$#accession A45334 !'##molecule_type mRNA !'##residues 1-530 ##label SON !'##cross-references GB:M90358; NID:g162878; PIDN:AAA74560.1; !1PID:g162879 !'##experimental_source brain !'##note sequence extracted from NCBI backbone (NCBIP:121478) REFERENCE A40282 !$#authors Charbonneau, H.; Kumar, S.; Novack, J.P.; Blumenthal, D.K.; !1Griffin, P.R.; Shabanowitz, J.; Hunt, D.F.; Beavo, J.A.; !1Walsh, K.A. !$#journal Biochemistry (1991) 30:7931-7940 !$#title Evidence for domain organization within the 61-kDa !1calmodulin-dependent cyclic nucleotide phosphodiesterase !1from bovine brain. !$#cross-references MUID:91329365; PMID:1651111 !$#accession A40282 !'##molecule_type protein !'##residues 2-530 ##label CHA !'##experimental_source brain REFERENCE A26650 !$#authors Charbonneau, H.; Beier, N.; Walsh, K.A.; Beavo, J.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:9308-9312 !$#title Identification of a conserved domain among cyclic nucleotide !1phosphodiesterases from diverse species. !$#cross-references MUID:87092242; PMID:3025833 !$#accession A26650 !'##molecule_type protein !'##residues 194-211,'X',213-236,'G',238-273,'X',275-320,'W',322-374, !1'XKL',378-427 ##label CH2 !'##experimental_source brain REFERENCE A54958 !$#authors Florio, V.A.; Sonnenburg, W.K.; Johnson, R.; Kwak, K.S.; !1Jensen, G.S.; Walsh, K.A.; Beavo, J.A. !$#journal Biochemistry (1994) 33:8948-8954 !$#title Phosphorylation of the 61-kDa calmodulin-stimulated cyclic !1nucleotide phosphodiesterase at serine 120 reduces its !1affinity for calmodulin. !$#cross-references MUID:94318639; PMID:8043581 !$#accession A54958 !'##status preliminary !'##molecule_type protein !'##residues 105-109;116-125;138-142;156-160;453,'X',455-460;503-505, !1'X',507-512 ##label FLO COMPLEX homodimer CLASSIFICATION #superfamily 3',5'-cyclic-nucleotide phosphodiesterase 1B, !1calmodulin-dependent; 3',5'-cyclic-nucleotide !1phosphodiesterase homology KEYWORDS acetylated amino end; alternative splicing; calmodulin !1binding; homodimer; phosphoprotein; phosphoric diester !1hydrolase FEATURE !$2-530 #product 3',5'-cyclic-nucleotide phosphodiesterase !81A, calmodulin-dependent, 61K brain form #status !8experimental #label MAT\ !$24-42 #region calmodulin binding\ !$218-435 #domain 3',5'-cyclic-nucleotide phosphodiesterase !8homology #label CNPD\ !$2 #modified_site acetylated amino end (Gly) (in mature !8form) #status experimental\ !$120,138 #binding_site phosphate (Ser) (covalent) (by protein !8kinase A) #status experimental SUMMARY #length 530 #molecular-weight 60843 #checksum 1453 SEQUENCE /// ENTRY A40981 #type complete TITLE 3',5'-cyclic-nucleotide phosphodiesterase (EC 3.1.4.17), cGMP-stimulated - bovine ALTERNATE_NAMES cGMP-dependent phosphodiesterase ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 26-Aug-1999 #sequence_revision 26-Aug-1999 #text_change 05-Nov-1999 ACCESSIONS A40981; B36112; A36112; B26650; A60179; C26650 REFERENCE A40981 !$#authors Sonnenburg, W.K.; Mullaney, P.J.; Beavo, J.A. !$#journal J. Biol. Chem. (1991) 266:17655-17661 !$#title Molecular cloning of a cyclic GMP-stimulated cyclic !1nucleotide phosphodiesterase cDNA. Identification and !1distribution of isozyme variants. !$#cross-references MUID:91373395; PMID:1654333 !$#accession A40981 !'##molecule_type mRNA !'##residues 1-921 ##label SON !'##cross-references GB:M73512; NID:g162829; PIDN:AAA74559.1; !1PID:g162830 REFERENCE A36112 !$#authors Le Trong, H.; Beier, N.; Sonnenburg, W.K.; Stroop, S.D.; !1Walsh, K.A.; Beavo, J.A.; Charbonneau, H. !$#journal Biochemistry (1990) 29:10280-10288 !$#title Amino acid sequence of the cyclic GMP stimulated cyclic !1nucleotide phosphodiesterase from bovine heart. !$#cross-references MUID:91104948; PMID:2176866 !$#accession B36112 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 592-921 ##label LET !$#accession A36112 !'##molecule_type protein !'##residues 1-203,'D',205-477,'Q',479-921 ##label LET2 REFERENCE A26650 !$#authors Charbonneau, H.; Beier, N.; Walsh, K.A.; Beavo, J.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:9308-9312 !$#title Identification of a conserved domain among cyclic nucleotide !1phosphodiesterases from diverse species. !$#cross-references MUID:87092242; PMID:3025833 !$#accession B26650 !'##molecule_type protein !'##residues 613-632,'L',634-794;808-868 ##label CHA !'##experimental_source heart REFERENCE A60179 !$#authors Tanaka, T.; Hockman, S.; Moos Jr., M.; Taira, M.; Meacci, !1E.; Murashima, S.; Manganiello, V.C. !$#journal Second Messengers Phosphoproteins (1991) 13:87-98 !$#title Comparison of putative cGMP-binding regions in bovine brain !1and cardiac cGMP-stimulated phosphodiesterases. !$#cross-references MUID:92065414; PMID:1659635 !$#accession A60179 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 311-803,'DV',806-921 ##label TAN !'##note part of this sequence was confirmed by protein sequencing COMMENT This protein is not glycosylated. CLASSIFICATION #superfamily 3',5'-cyclic-nucleotide phosphodiesterase, !1cGMP-stimulated; 3',5'-cyclic-nucleotide phosphodiesterase !1homology KEYWORDS acetylated amino end; alternative splicing; cAMP binding; !1cGMP binding; homodimer; phosphoric diester hydrolase FEATURE !$635-857 #domain 3',5'-cyclic-nucleotide phosphodiesterase !8homology #label CNPD\ !$1 #modified_site acetylated amino end (Met) #status !8experimental SUMMARY #length 921 #molecular-weight 103227 #checksum 5128 SEQUENCE /// ENTRY JC2486 #type complete TITLE 3',5'-cyclic-nucleotide phosphodiesterase (EC 3.1.4.17), cGMP-stimulated - rat ALTERNATE_NAMES cGMP-dependent phosphodiesterase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 26-Aug-1999 #sequence_revision 26-Aug-1999 #text_change 05-Nov-1999 ACCESSIONS JC2486 REFERENCE JC2486 !$#authors Yang, Q.; Paskind, M.; Bolger, G.; Thompson, W.J.; Repaske, !1D.R.; Cutler, L.S.; Epstein, P.M. !$#journal Biochem. Biophys. Res. Commun. (1994) 205:1850-1858 !$#title A novel cyclic GMP stimulated phosphodiesterase from rat !1brain. !$#cross-references MUID:95110334; PMID:7811274 !$#accession JC2486 !'##molecule_type mRNA !'##residues 1-928 ##label YAN !'##cross-references GB:U21101; NID:g706929; PIDN:AAA63683.1; !1PID:g706930 !'##experimental_source brain CLASSIFICATION #superfamily 3',5'-cyclic-nucleotide phosphodiesterase, !1cGMP-stimulated; 3',5'-cyclic-nucleotide phosphodiesterase !1homology KEYWORDS alternative splicing; cAMP binding; cGMP binding; homodimer; !1phosphoprotein; phosphoric diester hydrolase FEATURE !$643-865 #domain 3',5'-cyclic-nucleotide phosphodiesterase !8homology #label CNPD\ !$109 #binding_site phosphate (Ser) (covalent) (by protein !8kinase A) #status predicted SUMMARY #length 928 #molecular-weight 104663 #checksum 7548 SEQUENCE /// ENTRY ESBYPC #type complete TITLE 3',5'-cyclic-nucleotide phosphodiesterase (EC 3.1.4.17), low-affinity - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein G0574; protein NRB369; protein YGL248w ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1991 #sequence_revision 12-Apr-1996 #text_change 16-Jun-2000 ACCESSIONS S61613; S05879; S64274 REFERENCE S61598 !$#authors Coissac, E.; Maillier, E.; Robineau, S.; Netter, P. !$#submission submitted to the EMBL Data Library, December 1995 !$#accession S61613 !'##molecule_type DNA !'##residues 1-369 ##label COI !'##cross-references EMBL:X94357; NID:g1150575; PIDN:CAA64139.1; !1PID:g1150591 REFERENCE S05879 !$#authors Nikawa, J.; Sass, P.; Wigler, M. !$#journal Mol. Cell. Biol. (1987) 7:3629-3636 !$#title Cloning and characterization of the low-affinity cyclic AMP !1phosphodiesterase gene of Saccharomyces cerevisiae. !$#cross-references MUID:88065501; PMID:2824992 !$#accession S05879 !'##molecule_type DNA !'##residues 1-93,'F',95-369 ##label NIK !'##cross-references EMBL:M17781; NID:g172228; PIDN:AAA34896.1; !1PID:g172229 !'##experimental_source strain PS1-2 REFERENCE S64271 !$#authors Coissac, E.; Maillier, E.; Netter, P. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64274 !'##molecule_type DNA !'##residues 1-369 ##label COW !'##cross-references EMBL:Z72770; NID:g1322920; PIDN:CAA96968.1; !1PID:g1322921; GSPDB:GN00007; MIPS:YGL248w !'##experimental_source strain S288C GENETICS !$#gene SGD:PDE1; MIPS:YGL248w !'##cross-references SGD:S0003217; MIPS:YGL248w !$#map_position 7L CLASSIFICATION #superfamily 3',5'-cyclic-nucleotide phosphodiesterase KEYWORDS phosphoric diester hydrolase SUMMARY #length 369 #molecular-weight 42016 #checksum 8831 SEQUENCE /// ENTRY S24462 #type complete TITLE probable 3',5'-cyclic-nucleotide phosphodiesterase (EC 3.1.4.17) R08D7.6 - Caenorhabditis elegans ALTERNATE_NAMES hypothetical protein R08D7.6 ORGANISM #formal_name Caenorhabditis elegans DATE 26-Aug-1999 #sequence_revision 26-Aug-1999 #text_change 26-Aug-1999 ACCESSIONS S41041; S24462 REFERENCE S41036 !$#authors Ainscough, R.; Hawkins, T. !$#submission submitted to the EMBL Data Library, May 1992 !$#accession S41041 !'##molecule_type DNA !'##residues 1-841 ##label AIN !'##cross-references EMBL:Z12017 REFERENCE S24457 !$#authors Sulston, J.; Du, Z.; Thomas, K.; Wilson, R.; Hillier, L.; !1Staden, R.; Halloran, N.; Green, P.; Thierry-Mieg, J.; Qiu, !1L.; Dear, S.; Coulson, A.; Craxton, M.; Durbin, R.; Berks, !1M.; Metzstein, M.; Hawkins, T.; Ainscough, R.; Waterston, R. !$#journal Nature (1992) 356:37-41 !$#title The C. elegans genome sequencing project: a beginning. !$#cross-references MUID:92168156; PMID:1538779 !$#contents annotation GENETICS !$#introns 31/1; 97/3; 179/2; 260/1; 296/3; 324/3; 622/2; 701/3; 775/3 CLASSIFICATION #superfamily Caenorhabditis probable 3',5'-cyclic-nucleotide !1phosphodiesterase R08D7.6; 3',5'-cyclic-nucleotide !1phosphodiesterase homology KEYWORDS phosphoric diester hydrolase FEATURE !$403-627 #domain 3',5'-cyclic-nucleotide phosphodiesterase !8homology #label CNPD SUMMARY #length 841 #molecular-weight 95724 #checksum 7831 SEQUENCE /// ENTRY F65090 #type complete TITLE 3',5'-cyclic-nucleotide phosphodiesterase (EC 3.1.4.17) cpdA - Escherichia coli (strain K-12) ALTERNATE_NAMES icc protein ORGANISM #formal_name Escherichia coli DATE 12-Sep-1997 #sequence_revision 17-Sep-1997 #text_change 01-Mar-2002 ACCESSIONS F65090; A58723 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65090 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-275 ##label BLAT !'##cross-references GB:AE000385; GB:U00096; NID:g1789405; !1PIDN:AAC76068.1; PID:g1789410; UWGP:b3032 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A58723 !$#authors Imamura, R.; Yamanaka, K.; Ogura, T.; Hiraga, S.; Fujita, !1N.; Ishihama, A.; Niki, H. !$#journal J. Biol. Chem. (1996) 271:25423-25429 !$#title Identification of the cpdA gene encoding cyclic 3', !15'-adenosine monophosphate phosphodiesterase in Escherichia !1coli. !$#cross-references MUID:96411758; PMID:8810311 !$#accession A58723 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-275 ##label IMA !'##cross-references GB:D16557; NID:g453393; PIDN:BAA03989.1; !1PID:g453396 !'##experimental_source strain K-12 !'##note part of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing GENETICS !$#gene cpdA; icc !$#map_position 68.4 min FUNCTION !$#description catalyzes the hydrolysis of 3',5'-cyclic-nucleoside !1monophosphate to nucleoside 5'-phosphate !$#note appears to act only on cAMP; affects lacZ expression by !1decreasing concentration of cAMP, a positive regulator for !1transcription of the lacZ gene CLASSIFICATION #superfamily 3',5'-cyclic-nucleotide phosphodiesterase cpdA; !13',5'-cyclic-nucleotide phosphodiesterase cpdA homology; !1phosphoesterase core homology KEYWORDS iron; metalloprotein; phosphoric diester hydrolase FEATURE !$16-205 #domain 3',5'-cyclic-nucleotide phosphodiesterase !8cpdA homology #label CPDA\ !$16-96 #domain phosphoesterase core homology #label PEC SUMMARY #length 275 #molecular-weight 30938 #checksum 3690 SEQUENCE /// ENTRY H91118 #type complete TITLE 3',5'-cyclic-nucleotide phosphodiesterase (EC 3.1.4.17) cpdA - Escherichia coli (strain O157:H7, substrain RIMD 0509952) ALTERNATE_NAMES icc protein; regulator of lacZ ORGANISM #formal_name Escherichia coli DATE 18-Jul-2001 #sequence_revision 18-Jul-2001 #text_change 24-Aug-2001 ACCESSIONS H91118 REFERENCE A99629 !$#authors Hayashi, T.; Makino, K.; Ohnishi, M.; Kurokawa, K.; Ishii, !1K.; Yokoyama, K.; Han, C.G.; Ohtsubo, E.; Nakayama, K.; !1Murata, T.; Tanaka, M.; Tobe, T.; Iida, T.; Takami, H.; !1Honda, T.; Sasakawa, C.; Ogasawara, N.; Yasunaga, T.; !1Kuhara, S.; Shiba, T.; Hattori, M.; Shinagawa, H. !$#journal DNA Res. (2001) 8:11-22 !$#title Complete genome sequence of enterohemorrhagic Escherichia !1coli O157:H7 and genomic comparison with a laboratory strain !1K-12. !$#cross-references MUID:21156231; PMID:11258796 !$#accession H91118 !'##molecule_type DNA !'##residues 1-275 ##label HAY !'##cross-references GB:BA000007; PIDN:BAB37343.1; PID:g13363393; !1GSPDB:GN00154 !'##experimental_source strain O157:H7, substrain RIMD 0509952 GENETICS !$#gene ECs3920 FUNCTION !$#description catalyzes the hydrolysis of 3',5'-cyclic-nucleoside !1monophosphate to nucleoside 5'-phosphate !$#note appears to act only on cAMP; affects lacZ expression by !1decreasing concentration of cAMP, a positive regulator for !1transcription of the lacZ gene CLASSIFICATION #superfamily 3',5'-cyclic-nucleotide phosphodiesterase cpdA; !13',5'-cyclic-nucleotide phosphodiesterase cpdA homology; !1phosphoesterase core homology KEYWORDS iron; metalloprotein; phosphoric diester hydrolase FEATURE !$16-205 #domain 3',5'-cyclic-nucleotide phosphodiesterase !8cpdA homology #label CPDA\ !$16-96 #domain phosphoesterase core homology #label PEC SUMMARY #length 275 #molecular-weight 30938 #checksum 3690 SEQUENCE /// ENTRY G85963 #type complete TITLE 3',5'-cyclic-nucleotide phosphodiesterase (EC 3.1.4.17) cpdA - Escherichia coli (strain O157:H7, substrain EDL933) ALTERNATE_NAMES icc protein; regulator of lacZ ORGANISM #formal_name Escherichia coli DATE 16-Feb-2001 #sequence_revision 16-Feb-2001 #text_change 14-Sep-2001 ACCESSIONS G85963 REFERENCE A85480 !$#authors Perna, N.T.; Plunkett III, G.; Burland, V.; Mau, B.; !1Glasner, J.D.; Rose, D.J.; Mayhew, G.F.; Evans, P.S.; !1Gregor, J.; Kirkpatrick, H.A.; Posfai, G.; Hackett, J.; !1Klink, S.; Boutin, A.; Shao, Y.; Miller, L.; Grotbeck, E.J.; !1Davis, N.W.; Lim, A.; Dimalanta, E.; Potamousis, K.; !1Apodaca, J.; Anantharaman, T.S.; Lin, J.; Yen, G.; Schwartz, !1D.C.; Welch, R.A.; Blattner, F.R. !$#journal Nature (2001) 409:529-533 !$#title Genome sequence of enterohemorrhagic Escherichia coli !1O157:H7. !$#cross-references MUID:21074935; PMID:11206551 !$#accession G85963 !'##molecule_type DNA !'##residues 1-275 ##label STO !'##cross-references GB:AE005174; NID:g12517610; PIDN:AAG58171.1; !1GSPDB:GN00145; UWGP:Z4389 !'##experimental_source strain O157:H7, substrain EDL933 GENETICS !$#gene icc FUNCTION !$#description catalyzes the hydrolysis of 3',5'-cyclic-nucleoside !1monophosphate to nucleoside 5'-phosphate !$#note appears to act only on cAMP; affects lacZ expression by !1decreasing concentration of cAMP, a positive regulator for !1transcription of the lacZ gene CLASSIFICATION #superfamily 3',5'-cyclic-nucleotide phosphodiesterase cpdA; !13',5'-cyclic-nucleotide phosphodiesterase cpdA homology; !1phosphoesterase core homology KEYWORDS iron; metalloprotein; phosphoric diester hydrolase FEATURE !$16-205 #domain 3',5'-cyclic-nucleotide phosphodiesterase !8cpdA homology #label CPDA\ !$16-96 #domain phosphoesterase core homology #label PEC SUMMARY #length 275 #molecular-weight 30938 #checksum 3690 SEQUENCE /// ENTRY AG0889 #type complete TITLE 3',5'-cyclic-nucleotide phosphodiesterase (EC 3.1.4.17) cpdA-type STY3361 [similarity] - Salmonella enterica subsp. enterica serovar Typhi (strain CT18) ALTERNATE_NAMES icc protein ORGANISM #formal_name Salmonella enterica subsp. enterica serovar Typhi #note this species has also been called Salmonella typhi DATE 09-Nov-2001 #sequence_revision 09-Nov-2001 #text_change 18-Nov-2002 ACCESSIONS AG0889 REFERENCE AB0502 !$#authors Parkhill, J.; Dougan, G.; James, K.D.; Thomson, N.R.; !1Pickard, D.; Wain, J.; Churcher, C.; Mungall, K.L.; Bentley, !1S.D.; Holden, M.T.G.; Sebaihia, M.; Baker, S.; Basham, D.; !1Brooks, K.; Chillingworth, T.; Connerton, P.; Cronin, A.; !1Davis, P.; Davies, R.M.; Dowd, L.; White, N.; Farrar, J.; !1Feltwell, T.; Hamlin, N.; Haque, A.; Hien, T.T.; Holroyd, !1S.; Jagels, K.; Krogh, A.; Larsen, T.S.; Leather, S.; Moule, !1S.; O'Gaora, P.; Parry, C.; Quail, M.; Rutherford, K.; !1Simmonds, M.; Skelton, J.; Stevens, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (2001) 413:848-852 !$#title Complete genome sequence of a multiple drug resistant !1Salmonella enterica serovar Typhi CT18. !$#cross-references MUID:21534947; PMID:11677608 !$#accession AG0889 !'##molecule_type DNA !'##residues 1-275 ##label PAR !'##cross-references GB:AL513382; PIDN:CAD03015.1; PID:g16504260; !1GSPDB:GN00176 GENETICS !$#gene STY3361 FUNCTION !$#description catalyzes the hydrolysis of 3',5'-cyclic-nucleoside !1monophosphate to nucleoside 5'-phosphate CLASSIFICATION #superfamily 3',5'-cyclic-nucleotide phosphodiesterase cpdA; !13',5'-cyclic-nucleotide phosphodiesterase cpdA homology; !1phosphoesterase core homology KEYWORDS iron; metalloprotein; phosphoric diester hydrolase FEATURE !$16-205 #domain 3',5'-cyclic-nucleotide phosphodiesterase !8cpdA homology #label CPDA\ !$16-96 #domain phosphoesterase core homology #label PEC SUMMARY #length 275 #molecular-weight 30993 #checksum 6671 SEQUENCE /// ENTRY AE0082 #type complete TITLE 3',5'-cyclic-nucleotide phosphodiesterase (EC 3.1.4.17) cpdA-type [similarity] - Yersinia pestis (strain CO92) ALTERNATE_NAMES icc protein ORGANISM #formal_name Yersinia pestis DATE 02-Nov-2001 #sequence_revision 02-Nov-2001 #text_change 11-Jan-2002 ACCESSIONS AE0082 REFERENCE AB0001 !$#authors Parkhill, J.; Wren, B.W.; Thomson, N.R.; Titball, R.W.; !1Holden, M.T.G.; Prentice, M.B.; Sebaihia, M.; James, K.D.; !1Churcher, C.; Mungall, K.L.; Baker, S.; Basham, D.; Bentley, !1S.D.; Brooks, K.; Cerdeno-Tarraga, A.M.; Chillingworth, T.; !1Cronin, A.; Davies, R.M.; Davis, P.; Dougan, G.; Feltwell, !1T.; Hamlin, N.; Holroyd, S.; Jagels, K.; Leather, S.; !1Karlyshev, A.V.; Moule, S.; Oyston, P.C.F.; Quail, M.; !1Rutherford, K.; Simmonds, M.; Skelton, J.; Stevens, K.; !1Whitehead, S.; Barrell, B.G. !$#journal Nature (2001) 413:523-527 !$#title Genome sequence of Yersinia pestis, the causative agent of !1plague. !$#cross-references MUID:21470413; PMID:11586360 !$#accession AE0082 !'##molecule_type DNA !'##residues 1-275 ##label KUR !'##cross-references GB:AL590842; PIDN:CAC89520.1; PID:g15978756; !1GSPDB:GN00175 GENETICS !$#gene icc FUNCTION !$#description catalyzes the hydrolysis of 3',5'-cyclic-nucleoside !1monophosphate to nucleoside 5'-phosphate CLASSIFICATION #superfamily 3',5'-cyclic-nucleotide phosphodiesterase cpdA; !13',5'-cyclic-nucleotide phosphodiesterase cpdA homology; !1phosphoesterase core homology KEYWORDS iron; metalloprotein; phosphoric diester hydrolase FEATURE !$16-205 #domain 3',5'-cyclic-nucleotide phosphodiesterase !8cpdA homology #label CPDA\ !$16-96 #domain phosphoesterase core homology #label PEC SUMMARY #length 275 #molecular-weight 30932 #checksum 4472 SEQUENCE /// ENTRY E64065 #type complete TITLE 3',5'-cyclic-nucleotide phosphodiesterase (EC 3.1.4.17) cpdA homolog - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES hypothetical protein HI0399; icc protein ORGANISM #formal_name Haemophilus influenzae DATE 18-Aug-1995 #sequence_revision 18-Aug-1995 #text_change 11-Jun-1999 ACCESSIONS E64065 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession E64065 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-274 ##label TIGR !'##cross-references GB:U32723; GB:L42023; NID:g1573363; !1PIDN:AAC22058.1; PID:g1573370; TIGR:HI0399 FUNCTION !$#description catalyzes the hydrolysis of 3',5'-cyclic-nucleoside !1monophosphate to nucleoside 5'-phosphate CLASSIFICATION #superfamily 3',5'-cyclic-nucleotide phosphodiesterase cpdA; !13',5'-cyclic-nucleotide phosphodiesterase cpdA homology; !1phosphoesterase core homology KEYWORDS iron; metalloprotein; phosphoric diester hydrolase FEATURE !$15-204 #domain 3',5'-cyclic-nucleotide phosphodiesterase !8cpdA homology #label CPDA\ !$15-95 #domain phosphoesterase core homology #label PEC SUMMARY #length 274 #molecular-weight 31556 #checksum 6128 SEQUENCE /// ENTRY G82076 #type complete TITLE 3',5'-cyclic-nucleotide phosphodiesterase (EC 3.1.4.17) cpdA-type VC2433 [similarity] - Vibrio cholerae (strain N16961 serogroup O1) ALTERNATE_NAMES icc protein ORGANISM #formal_name Vibrio cholerae DATE 18-Aug-2000 #sequence_revision 20-Aug-2000 #text_change 02-Nov-2001 ACCESSIONS G82076 REFERENCE A82035 !$#authors Heidelberg, J.F.; Eisen, J.A.; Nelson, W.C.; Clayton, R.A.; !1Gwinn, M.L.; Dodson, R.J.; Haft, D.H.; Hickey, E.K.; !1Peterson, J.D.; Umayam, L.A.; Gill, S.R.; Nelson, K.E.; !1Read, T.D.; Tettelin, H.; Richardson, D.; Ermolaeva, M.D.; !1Vamathevan, J.; Bass, S.; Qin, H.; Dragoi, I.; Sellers, P.; !1McDonald, L.; Utterback, T.; Fleishmann, R.D.; Nierman, !1W.C.; White, O.; Salzberg, S.L.; Smith, H.O.; Colwell, R.R.; !1Mekalanos, J.J.; Venter, J.C.; Fraser, C.M. !$#journal Nature (2000) 406:477-483 !$#title DNA Sequence of both chromosomes of the cholera pathogen !1Vibrio cholerae. !$#cross-references MUID:20406833; PMID:10952301 !$#accession G82076 !'##molecule_type DNA !'##residues 1-272 ##label HEI !'##cross-references GB:AE004313; GB:AE003852; NID:g9657007; !1PIDN:AAF95576.1; GSPDB:GN00126; TIGR:VC2433 !'##experimental_source serogroup O1; strain N16961; biotype El Tor GENETICS !$#gene VC2433 !$#map_position 1 CLASSIFICATION #superfamily 3',5'-cyclic-nucleotide phosphodiesterase cpdA; !13',5'-cyclic-nucleotide phosphodiesterase cpdA homology; !1phosphoesterase core homology KEYWORDS iron; metalloprotein; phosphoric diester hydrolase FEATURE !$13-202 #domain 3',5'-cyclic-nucleotide phosphodiesterase !8cpdA homology #label CPDA\ !$13-93 #domain phosphoesterase core homology #label PEC SUMMARY #length 272 #molecular-weight 30462 #checksum 1142 SEQUENCE /// ENTRY F70536 #type complete TITLE 3',5'-cyclic-nucleotide phosphodiesterase (EC 3.1.4.17) cpdA homolog - Mycobacterium tuberculosis (strain H37RV) ALTERNATE_NAMES hypothetical protein Rv0805 ORGANISM #formal_name Mycobacterium tuberculosis DATE 30-Oct-1998 #sequence_revision 30-Oct-1998 #text_change 16-Jun-2000 ACCESSIONS F70536 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession F70536 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-318 ##label COL !'##cross-references GB:Z95618; GB:AL123456; NID:g3261788; !1PIDN:CAB09106.1; PID:g2117277 !'##experimental_source strain H37Rv GENETICS !$#gene Rv0805 FUNCTION !$#description catalyzes the hydrolysis of 3',5'-cyclic-nucleoside !1monophosphate to nucleoside 5'-phosphate CLASSIFICATION #superfamily 3',5'-cyclic-nucleotide phosphodiesterase cpdA; !13',5'-cyclic-nucleotide phosphodiesterase cpdA homology; !1phosphoesterase core homology KEYWORDS iron; metalloprotein; phosphoric diester hydrolase FEATURE !$15-209 #domain 3',5'-cyclic-nucleotide phosphodiesterase !8cpdA homology #label CPDA\ !$15-99 #domain phosphoesterase core homology #label PEC SUMMARY #length 318 #molecular-weight 34233 #checksum 8211 SEQUENCE /// ENTRY E87185 #type complete TITLE 3',5'-cyclic-nucleotide phosphodiesterase (EC 3.1.4.17) cpdA homolog ML2210 - Mycobacterium leprae ORGANISM #formal_name Mycobacterium leprae DATE 03-Aug-2001 #sequence_revision 03-Aug-2001 #text_change 03-Aug-2001 ACCESSIONS E87185 REFERENCE A86909 !$#authors Cole, S.T.; Eiglmeier, K.; Parkhill, J.; James, K.D.; !1Thomson, N.R.; Wheeler, P.R.; Honore, N.; Ganier, T.; !1Churcher, C.; Harris, D.; Mungall, K.; Basham, D.; Brown, !1D.; Chillingworth, T.; Connor, R.; Davies, R.M.; Devlin, K.; !1Duthoy, S.; Feltwell, T.; Fraser, A.; Hamlin, N.; Holroyd, !1S.; Hornsby, T.; Jagels, K.; Lacroix, C.; Maclean, J.; !1Moule, S.; Murphy, L.; Oliver, K.; Quail, M.A.; Rajandream, !1M.A.; Rutherford, K.M.; Rutter, S.; Seeger, K.; Simon, S.; !1Simmonds, M.; Skelton, J.; Squares, R.; Squares, S.; !1Stevens, K.; Taylor, K.; Whitehead, S.; Woodward, J.R.; !1Barrell, B.G. !$#journal Nature (2001) 409:1007-1011 !$#title Massive gene decay in the leprosy bacillus. !$#cross-references MUID:21128732; PMID:11234002 !$#accession E87185 !'##molecule_type DNA !'##residues 1-317 ##label STO !'##cross-references GB:AL450380; NID:g13093741; PIDN:CAC31165.1; !1GSPDB:GN00147 GENETICS !$#gene ML2210 CLASSIFICATION #superfamily 3',5'-cyclic-nucleotide phosphodiesterase cpdA; !13',5'-cyclic-nucleotide phosphodiesterase cpdA homology; !1phosphoesterase core homology KEYWORDS iron; metalloprotein; phosphoric diester hydrolase FEATURE !$15-208 #domain 3',5'-cyclic-nucleotide phosphodiesterase !8cpdA homology #label CPDA\ !$15-98 #domain phosphoesterase core homology #label PEC SUMMARY #length 317 #molecular-weight 34198 #checksum 8946 SEQUENCE /// ENTRY S52234 #type complete TITLE 3',5'-cyclic-nucleotide phosphodiesterase (EC 3.1.4.17) cpdA homolog - Coxiella burnetii plasmids ALTERNATE_NAMES hypothetical protein 248; icc protein homolog ORGANISM #formal_name Coxiella burnetii DATE 30-Oct-1998 #sequence_revision 30-Oct-1998 #text_change 11-Jun-1999 ACCESSIONS S52234; S38222 REFERENCE S52227 !$#authors Willems, H.; Thiele, D.; Valkova, D. !$#submission submitted to the EMBL Data Library, March 1995 !$#accession S52234 !'##molecule_type DNA !'##residues 1-248 ##label WIL !'##cross-references EMBL:X85964; NID:g757760; PIDN:CAA59947.1; !1PID:g757768 !'##experimental_source strain Q1182, plasmid QpDV REFERENCE S38215 !$#authors Thiele, D.; Willems, H.; Haas, M.; Krauss, H. !$#submission submitted to the EMBL Data Library, October 1993 !$#accession S38222 !'##molecule_type DNA !'##residues 1-75,'V',77-128,'D',130-142,'D',144-235,'F',237-248 ##label !1THI !'##cross-references EMBL:X75356; NID:g407370; PIDN:CAA53110.1; !1PID:g407378 !'##experimental_source isolate Nine Mile phase I, plasmid QpH1 GENETICS !$#genome plasmid FUNCTION !$#description catalyzes the hydrolysis of 3',5'-cyclic-nucleoside !1monophosphate to nucleoside 5'-phosphate CLASSIFICATION #superfamily 3',5'-cyclic-nucleotide phosphodiesterase cpdA; !13',5'-cyclic-nucleotide phosphodiesterase cpdA homology; !1phosphoesterase core homology KEYWORDS iron; metalloprotein; phosphoric diester hydrolase FEATURE !$7-193 #domain 3',5'-cyclic-nucleotide phosphodiesterase !8cpdA homology #label CPDA\ !$7-84 #domain phosphoesterase core homology #label PEC SUMMARY #length 248 #molecular-weight 28898 #checksum 228 SEQUENCE /// ENTRY A70360 #type complete TITLE 3',5'-cyclic-nucleotide phosphodiesterase (EC 3.1.4.17) cpdA homolog - Aquifex aeolicus ALTERNATE_NAMES hypothetical protein aq_684 ORGANISM #formal_name Aquifex aeolicus DATE 08-May-1998 #sequence_revision 15-May-1998 #text_change 11-Jun-1999 ACCESSIONS A70360 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession A70360 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-249 ##label AQF !'##cross-references GB:AE000702; NID:g2983276; PIDN:AAC06876.1; !1PID:g2983283; GB:AE000657 !'##experimental_source strain VF5 GENETICS !$#gene aq_684 FUNCTION !$#description catalyzes the hydrolysis of 3',5'-cyclic-nucleoside !1monophosphate to nucleoside 5'-phosphate CLASSIFICATION #superfamily 3',5'-cyclic-nucleotide phosphodiesterase cpdA; !13',5'-cyclic-nucleotide phosphodiesterase cpdA homology; !1phosphoesterase core homology KEYWORDS iron; metalloprotein; phosphoric diester hydrolase FEATURE !$2-181 #domain 3',5'-cyclic-nucleotide phosphodiesterase !8cpdA homology #label CPDA\ !$2-74 #domain phosphoesterase core homology #label PEC SUMMARY #length 249 #molecular-weight 29000 #checksum 1556 SEQUENCE /// ENTRY C69097 #type complete TITLE 3',5'-cyclic-nucleotide phosphodiesterase (EC 3.1.4.17) cpdA homolog - Methanobacterium thermoautotrophicum (strain Delta H) ALTERNATE_NAMES icc protein homolog ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 05-Dec-1997 #sequence_revision 05-Dec-1997 #text_change 11-Jun-1999 ACCESSIONS C69097 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession C69097 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-262 ##label MTH !'##cross-references GB:AE000928; GB:AE000666; NID:g2622835; !1PIDN:AAB86192.1; PID:g2622852 !'##experimental_source strain Delta H GENETICS !$#gene MTH1722 FUNCTION !$#description catalyzes the hydrolysis of 3',5'-cyclic-nucleoside !1monophosphate to nucleoside 5'-phosphate CLASSIFICATION #superfamily 3',5'-cyclic-nucleotide phosphodiesterase cpdA; !13',5'-cyclic-nucleotide phosphodiesterase cpdA homology; !1phosphoesterase core homology KEYWORDS iron; metalloprotein; phosphoric diester hydrolase FEATURE !$4-185 #domain 3',5'-cyclic-nucleotide phosphodiesterase !8cpdA homology #label CPDA\ !$4-77 #domain phosphoesterase core homology #label PEC SUMMARY #length 262 #molecular-weight 29964 #checksum 7423 SEQUENCE /// ENTRY F69104 #type complete TITLE 3',5'-cyclic-nucleotide phosphodiesterase (EC 3.1.4.17) cpdA homolog MTH178 - Methanobacterium thermoautotrophicum (strain Delta H) ALTERNATE_NAMES Icc related protein ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 30-Oct-1998 #sequence_revision 30-Oct-1998 #text_change 11-Jun-1999 ACCESSIONS F69104 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession F69104 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-196 ##label MTH !'##cross-references GB:AE000805; GB:AE000666; NID:g2621213; !1PIDN:AAB84684.1; PID:g2621221 !'##experimental_source strain Delta H GENETICS !$#gene MTH178 FUNCTION !$#description catalyzes the hydrolysis of 3',5'-cyclic-nucleoside !1monophosphate to nucleoside 5'-phosphate CLASSIFICATION #superfamily 3',5'-cyclic-nucleotide phosphodiesterase cpdA; !13',5'-cyclic-nucleotide phosphodiesterase cpdA homology; !1phosphoesterase core homology KEYWORDS iron; metalloprotein; phosphoric diester hydrolase FEATURE !$3-183 #domain 3',5'-cyclic-nucleotide phosphodiesterase !8cpdA homology #label CPDA\ !$3-74 #domain phosphoesterase core homology #label PEC SUMMARY #length 196 #molecular-weight 21927 #checksum 9143 SEQUENCE /// ENTRY G71475 #type complete TITLE probable 3',5'-cyclic-nucleotide phosphodiesterase (EC 3.1.4.17) cpdA-type [similarity] - Chlamydia trachomatis (serotype D, strain UW3/Cx) ALTERNATE_NAMES icc protein ORGANISM #formal_name Chlamydia trachomatis DATE 13-Sep-1998 #sequence_revision 13-Sep-1998 #text_change 02-Nov-2001 ACCESSIONS G71475 REFERENCE A71570 !$#authors Stephens, R.S.; Kalman, S.; Lammel, C.J.; Fan, J.; Marathe, !1R.; Aravind, L.; Mitchell, W.P.; Olinger, L.; Tatusov, R.L.; !1Zhao, Q.; Koonin, E.V.; Davis, R.W. !$#journal Science (1998) 282:754-759 !$#title Genome sequence of an obligate intracellular pathogen of !1humans: Chlamydia trachomatis. !$#cross-references MUID:99000809; PMID:9784136 !$#accession G71475 !'##molecule_type DNA !'##residues 1-290 ##label ARN !'##cross-references GB:AE001347; GB:AE001273; NID:g3329210; !1PIDN:AAC68349.1; PID:g3329215 !'##experimental_source serotype D, strain UW-3/Cx GENETICS !$#gene icc CLASSIFICATION #superfamily 3',5'-cyclic-nucleotide phosphodiesterase cpdA; !13',5'-cyclic-nucleotide phosphodiesterase cpdA homology; !1phosphoesterase core homology KEYWORDS iron; metalloprotein; phosphoric diester hydrolase FEATURE !$10-226 #domain 3',5'-cyclic-nucleotide phosphodiesterase !8cpdA homology #label CPD\ !$10-107 #domain phosphoesterase core homology #label PEC SUMMARY #length 290 #molecular-weight 32716 #checksum 4159 SEQUENCE /// ENTRY D81738 #type complete TITLE probable 3',5'-cyclic-nucleotide phosphodiesterase (EC 3.1.4.17) cpdA-type TC0135 [similarity] - Chlamydia muridarum (strain Nigg) ALTERNATE_NAMES icc-related protein ORGANISM #formal_name Chlamydia muridarum, Chlamydia trachomatis MoPn DATE 31-Mar-2000 #sequence_revision 31-Mar-2000 #text_change 02-Nov-2001 ACCESSIONS D81738 REFERENCE A81500 !$#authors Read, T.D.; Brunham, R.C.; Shen, C.; Gill, S.R.; Heidelberg, !1J.F.; White, O.; Hickey, E.K.; Peterson, J.; Utterback, T.; !1Berry, K.; Bass, S.; Linher, K.; Weidman, J.; Khouri, H.; !1Craven, B.; Bowman, C.; Dodson, R.; Gwinn, M.; Nelson, W.; !1DeBoy, R.; Kolonay, J.; McClarty, G.; Salzberg, S.L.; Eisen, !1J.; Fraser, C.M. !$#journal Nucleic Acids Res. (2000) 28:1397-1406 !$#title Genome sequences of Chlamydia trachomatis MoPn and Chlamydia !1pneumoniae AR39. !$#cross-references MUID:20150255; PMID:10684935 !$#accession D81738 !'##molecule_type DNA !'##residues 1-290 ##label TET !'##cross-references GB:AE002280; GB:AE002160; NID:g7190162; !1PIDN:AAF39013.1; PID:g7190171; GSPDB:GN00121; TIGR:TC0135 !'##experimental_source strain Nigg (MoPn) GENETICS !$#gene TC0135 CLASSIFICATION #superfamily 3',5'-cyclic-nucleotide phosphodiesterase cpdA; !13',5'-cyclic-nucleotide phosphodiesterase cpdA homology; !1phosphoesterase core homology KEYWORDS iron; metalloprotein; phosphoric diester hydrolase FEATURE !$10-226 #domain 3',5'-cyclic-nucleotide phosphodiesterase !8cpdA homology #label CPD\ !$10-107 #domain phosphoesterase core homology #label PEC SUMMARY #length 290 #molecular-weight 32689 #checksum 4373 SEQUENCE /// ENTRY D72021 #type complete TITLE probable 3',5'-cyclic-nucleotide phosphodiesterase (EC 3.1.4.17) cpdA-type [similarity] - Chlamydophila pneumoniae (strains CWL029 and AR39) ALTERNATE_NAMES icc protein ORGANISM #formal_name Chlamydophila pneumoniae, Chlamydia pneumoniae DATE 23-Apr-1999 #sequence_revision 23-Apr-1999 #text_change 02-Nov-2001 ACCESSIONS D72021; H81516 REFERENCE A72000 !$#authors Kalman, S.; Mitchell, W.; Marathe, R.; Lammel, C.; Fan, J.; !1Olinger, L.; Grimwood, J.; Davis, R.W.; Stephens, R.S. !$#journal Nature Genet. (1999) 21:385-389 !$#title Comparative genomes of Clamydia pneumoniae and C. !1trachomatis. !$#cross-references MUID:99206606; PMID:10192388 !$#accession D72021 !'##molecule_type DNA !'##residues 1-295 ##label ARN !'##cross-references GB:AE001670; GB:AE001363; NID:g4377212; !1PIDN:AAD19035.1; PID:g4377217 !'##experimental_source strain CWL029 REFERENCE A81500 !$#authors Read, T.D.; Brunham, R.C.; Shen, C.; Gill, S.R.; Heidelberg, !1J.F.; White, O.; Hickey, E.K.; Peterson, J.; Utterback, T.; !1Berry, K.; Bass, S.; Linher, K.; Weidman, J.; Khouri, H.; !1Craven, B.; Bowman, C.; Dodson, R.; Gwinn, M.; Nelson, W.; !1DeBoy, R.; Kolonay, J.; McClarty, G.; Salzberg, S.L.; Eisen, !1J.; Fraser, C.M. !$#journal Nucleic Acids Res. (2000) 28:1397-1406 !$#title Genome sequences of Chlamydia trachomatis MoPn and Chlamydia !1pneumoniae AR39. !$#cross-references MUID:20150255; PMID:10684935 !$#accession H81516 !'##molecule_type DNA !'##residues 1-295 ##label REA !'##cross-references GB:AE002256; GB:AE002161; NID:g7189893; !1PIDN:AAF38749.1; PID:g7189882; GSPDB:GN00122; TIGR:CP0969 !'##experimental_source strain AR39, HL cells GENETICS !$#gene CPn0897; CP0969 CLASSIFICATION #superfamily 3',5'-cyclic-nucleotide phosphodiesterase cpdA; !13',5'-cyclic-nucleotide phosphodiesterase cpdA homology; !1phosphoesterase core homology KEYWORDS iron; metalloprotein; phosphoric diester hydrolase FEATURE !$10-226 #domain 3',5'-cyclic-nucleotide phosphodiesterase !8cpdA homology #label CPDA\ !$10-107 #domain phosphoesterase core homology #label PEC SUMMARY #length 295 #molecular-weight 33643 #checksum 5225 SEQUENCE /// ENTRY G86602 #type complete TITLE probable 3',5'-cyclic-nucleotide phosphodiesterase (EC 3.1.4.17) cpdA-type CPj0897 [similarity] - Chlamydophila pneumoniae (strain J138) ALTERNATE_NAMES icc protein ORGANISM #formal_name Chlamydophila pneumoniae, Chlamydia pneumoniae DATE 02-Mar-2001 #sequence_revision 02-Mar-2001 #text_change 02-Nov-2001 ACCESSIONS G86602 REFERENCE A86491 !$#authors Shirai, M.; Hirakawa, H.; Kimoto, M.; Tabuchi, M.; Kishi, !1F.; Ouchi, K.; Shiba, T.; Ishii, K.; Hattori, M.; Kuhara, !1S.; Nakazawa, T. !$#journal Nucleic Acids Res. (2000) 28:2311-2314 !$#title Comparison of whole genome sequences of chlamydia pneumoniae !1J138. !$#cross-references MUID:20330349; PMID:10871362 !$#accession G86602 !'##molecule_type DNA !'##residues 1-295 ##label STO !'##cross-references GB:BA000008; NID:g8979271; PIDN:BAA99105.1; !1GSPDB:GN00142 !'##experimental_source strain J138 GENETICS !$#gene CPj0897 CLASSIFICATION #superfamily 3',5'-cyclic-nucleotide phosphodiesterase cpdA; !13',5'-cyclic-nucleotide phosphodiesterase cpdA homology; !1phosphoesterase core homology KEYWORDS iron; metalloprotein; phosphoric diester hydrolase FEATURE !$10-226 #domain 3',5'-cyclic-nucleotide phosphodiesterase !8cpdA homology #label CPD\ !$10-107 #domain phosphoesterase core homology #label PEC SUMMARY #length 295 #molecular-weight 33643 #checksum 5225 SEQUENCE /// ENTRY G83023 #type complete TITLE 3',5'-cyclic-nucleotide phosphodiesterase (EC 3.1.4.17) cpdA-type PA4969 [similarity] - Pseudomonas aeruginosa (strain PAO1) ALTERNATE_NAMES icc protein ORGANISM #formal_name Pseudomonas aeruginosa DATE 15-Sep-2000 #sequence_revision 15-Sep-2000 #text_change 24-Aug-2001 ACCESSIONS G83023 REFERENCE A82950 !$#authors Stover, C.K.; Pham, X.Q.; Erwin, A.L.; Mizoguchi, S.D.; !1Warrener, P.; Hickey, M.J.; Brinkman, F.S.L.; Hufnagle, !1W.O.; Kowalik, D.J.; Lagrou, M.; Garber, R.L.; Goltry, L.; !1Tolentino, E.; Westbrook-Wadman, S.; Yuan, Y.; Brody, L.L.; !1Coulter, S.N.; Folger, K.R.; Kas, A.; Larbig, K.; Lim, R.M.; !1Smith, K.A.; Spencer, D.H.; Wong, G.K.S.; Wu, Z.; Paulsen, !1I.T.; Reizer, J.; Saier, M.H.; Hancock, R.E.W.; Lory, S.; !1Olson, M.V. !$#journal Nature (2000) 406:959-964 !$#title Complete genome sequence of Pseudomonas aeruginosa PA01, an !1opportunistic pathogen. !$#cross-references MUID:20437337; PMID:10984043 !$#accession G83023 !'##molecule_type DNA !'##residues 1-272 ##label STO !'##cross-references GB:AE004910; GB:AE004091; NID:g9951251; !1PIDN:AAG08354.1; GSPDB:GN00131; PASP:PA4969 !'##experimental_source strain PAO1 GENETICS !$#gene PA4969 CLASSIFICATION #superfamily 3',5'-cyclic-nucleotide phosphodiesterase cpdA; !13',5'-cyclic-nucleotide phosphodiesterase cpdA homology; !1phosphoesterase core homology KEYWORDS iron; metalloprotein; phosphoric diester hydrolase FEATURE !$15-202 #domain 3',5'-cyclic-nucleotide phosphodiesterase !8cpdA homology #label CPDA\ !$15-95 #domain phosphoesterase core homology #label PEC SUMMARY #length 272 #molecular-weight 30516 #checksum 8896 SEQUENCE /// ENTRY T35867 #type complete TITLE probable 3',5'-cyclic-nucleotide phosphodiesterase (EC 3.1.4.17) cpdA-type SC9B1.22c [similarity] - Streptomyces coelicolor ALTERNATE_NAMES icc protein ORGANISM #formal_name Streptomyces coelicolor DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 24-Aug-2001 ACCESSIONS T35867 REFERENCE Z21591 !$#authors Saunders, D.C.; Harris, D.; Bentley, S.D.; Parkhill, J.; !1Barrell, B.G.; Rajandream, M.A. !$#submission submitted to the EMBL Data Library, April 1999 !$#accession T35867 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-273 ##label SAU !'##cross-references EMBL:AL049727; PIDN:CAB41568.1; GSPDB:GN00070; !1SCOEDB:SC9B1.22c !'##experimental_source strain A3(2) GENETICS !$#gene SCOEDB:SC9B1.22c CLASSIFICATION #superfamily 3',5'-cyclic-nucleotide phosphodiesterase cpdA; !13',5'-cyclic-nucleotide phosphodiesterase cpdA homology; !1phosphoesterase core homology KEYWORDS iron; metalloprotein; phosphoric diester hydrolase FEATURE !$25-214 #domain 3',5'-cyclic-nucleotide phosphodiesterase !8cpdA homology #label CPD SUMMARY #length 273 #molecular-weight 29377 #checksum 7528 SEQUENCE /// ENTRY C97631 #type complete TITLE probable 3',5'-cyclic-nucleotide phosphodiesterase (EC 3.1.4.17) cpdA-type AGR_C_4113 [similarity] - Agrobacterium tumefaciens (strain C58, Cereon) ORGANISM #formal_name Agrobacterium tumefaciens DATE 30-Sep-2001 #sequence_revision 30-Sep-2001 #text_change 18-Nov-2002 ACCESSIONS C97631 REFERENCE A97359 !$#authors Goodner, B.; Hinkle, G.; Gattung, S.; Miller, N.; Blanchard, !1M.; Qurollo, B.; Goldman, B.S.; Cao, Y.; Askenazi, M.; !1Halling, C.; Mullin, L.; Houmiel, K.; Gordon, J.; Vaudin, !1M.; Iartchouk, O.; Epp, A.; Liu, F.; Wollam, C.; Allinger, !1M.; Doughty, D.; Scott, C.; Lappas, C.; Markelz, B.; !1Flanagan, C.; Crowell, C.; Gurson, J.; Lomo, C.; Sear, C.; !1Strub, G.; Cielo, C.; Slater, S. !$#journal Science (2001) 294:2323-2328 !$#title Genome Sequence of the Plant Pathogen and Biotechnology !1Agent Agrobacterium tumefaciens C58. !$#cross-references MUID:21608551; PMID:11743194 !$#accession C97631 !'##molecule_type DNA !'##residues 1-316 ##label KUR !'##cross-references GB:AE007869; PIDN:AAK88004.1; PID:g15157419; !1GSPDB:GN00169 GENETICS !$#gene AGR_C_4113 !$#map_position circular chromosome CLASSIFICATION #superfamily 3',5'-cyclic-nucleotide phosphodiesterase cpdA; !13',5'-cyclic-nucleotide phosphodiesterase cpdA homology; !1phosphoesterase core homology KEYWORDS iron; metalloprotein; phosphoric diester hydrolase FEATURE !$3-229 #domain 3',5'-cyclic-nucleotide phosphodiesterase !8cpdA homology #label CPDA\ !$3-101 #domain phosphoesterase core homology #label PEC SUMMARY #length 316 #molecular-weight 34703 #checksum 9616 SEQUENCE /// ENTRY B87393 #type complete TITLE probable 3',5'-cyclic-nucleotide phosphodiesterase (EC 3.1.4.17) cpdA-type CC1158 [similarity] - Caulobacter crescentus ORGANISM #formal_name Caulobacter crescentus DATE 20-Apr-2001 #sequence_revision 20-Apr-2001 #text_change 02-Nov-2001 ACCESSIONS B87393 REFERENCE A87249 !$#authors Nierman, W.C.; Feldblyum, T.V.; Paulsen, I.T.; Nelson, K.E.; !1Eisen, J.; Heidelberg, J.F.; Alley, M.; Ohta, N.; Maddock, !1J.R.; Potocka, I.; Nelson, W.C.; Newton, A.; Stephens, C.; !1Phadke, N.D.; Ely, B.; Laub, M.T.; DeBoy, R.T.; Dodson, !1R.J.; Durkin, A.S.; Gwinn, M.L.; Haft, D.H.; Kolonay, J.F.; !1Smit, J.; Craven, M.; Khouri, H.; Shetty, J.; Berry, K.; !1Utterback, T.; Tran, K.; Wolf, A.; Vamathevan, J.; !1Ermolaeva, M.; White, O.; Salzberg, S.L.; Shapiro, L.; !1Venter, J.C.; Fraser, C.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (2001) 98:4136-4141 !$#title Complete Genome Sequence of Caulobacter crescentus. !$#cross-references MUID:21173698; PMID:11259647 !$#accession B87393 !'##molecule_type DNA !'##residues 1-305 ##label STO !'##cross-references GB:AE005673; NID:g13422478; PIDN:AAK23142.1; !1GSPDB:GN00148 GENETICS !$#gene CC1158 CLASSIFICATION #superfamily 3',5'-cyclic-nucleotide phosphodiesterase cpdA; !13',5'-cyclic-nucleotide phosphodiesterase cpdA homology; !1phosphoesterase core homology KEYWORDS iron; metalloprotein; phosphoric diester hydrolase FEATURE !$5-223 #domain 3',5'-cyclic-nucleotide phosphodiesterase !8cpdA homology #label CPDA\ !$5-103 #domain phosphoesterase core homology #label PEC SUMMARY #length 305 #molecular-weight 32474 #checksum 7665 SEQUENCE /// ENTRY B87690 #type complete TITLE probable 3',5'-cyclic-nucleotide phosphodiesterase (EC 3.1.4.17) cpdA-type CC3556 [similarity] - Caulobacter crescentus ORGANISM #formal_name Caulobacter crescentus DATE 20-Apr-2001 #sequence_revision 20-Apr-2001 #text_change 02-Nov-2001 ACCESSIONS B87690 REFERENCE A87249 !$#authors Nierman, W.C.; Feldblyum, T.V.; Paulsen, I.T.; Nelson, K.E.; !1Eisen, J.; Heidelberg, J.F.; Alley, M.; Ohta, N.; Maddock, !1J.R.; Potocka, I.; Nelson, W.C.; Newton, A.; Stephens, C.; !1Phadke, N.D.; Ely, B.; Laub, M.T.; DeBoy, R.T.; Dodson, !1R.J.; Durkin, A.S.; Gwinn, M.L.; Haft, D.H.; Kolonay, J.F.; !1Smit, J.; Craven, M.; Khouri, H.; Shetty, J.; Berry, K.; !1Utterback, T.; Tran, K.; Wolf, A.; Vamathevan, J.; !1Ermolaeva, M.; White, O.; Salzberg, S.L.; Shapiro, L.; !1Venter, J.C.; Fraser, C.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (2001) 98:4136-4141 !$#title Complete Genome Sequence of Caulobacter crescentus. !$#cross-references MUID:21173698; PMID:11259647 !$#accession B87690 !'##molecule_type DNA !'##residues 1-262 ##label STO !'##cross-references GB:AE005673; NID:g13425294; PIDN:AAK25518.1; !1GSPDB:GN00148 GENETICS !$#gene CC3556 CLASSIFICATION #superfamily 3',5'-cyclic-nucleotide phosphodiesterase cpdA; !13',5'-cyclic-nucleotide phosphodiesterase cpdA homology; !1phosphoesterase core homology KEYWORDS iron; metalloprotein; phosphoric diester hydrolase FEATURE !$1-224 #domain 3',5'-cyclic-nucleotide phosphodiesterase !8cpdA homology #label CPDA\ !$1-74 #domain phosphoesterase core homology #label PEC SUMMARY #length 262 #molecular-weight 28121 #checksum 790 SEQUENCE /// ENTRY G69553 #type complete TITLE 3',5'-cyclic-nucleotide phosphodiesterase (EC 3.1.4.17) cpdA homolog - Archaeoglobus fulgidus ALTERNATE_NAMES icc protein homolog; lacZ expression regulatory protein homolog ORGANISM #formal_name Archaeoglobus fulgidus DATE 30-Oct-1998 #sequence_revision 30-Oct-1998 #text_change 11-Jun-1999 ACCESSIONS G69553 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession G69553 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-372 ##label KLE !'##cross-references GB:AE001107; GB:AE000782; NID:g2689430; !1PIDN:AAB91233.1; PID:g2650659; TIGR:AF2430 FUNCTION !$#description catalyzes the hydrolysis of 3',5'-cyclic-nucleoside !1monophosphate to nucleoside 5'-phosphate CLASSIFICATION #superfamily Archaeoglobus fulgidus 3',5'-cyclic-nucleotide !1phosphodiesterase cpdA homolog; 3',5'-cyclic-nucleotide !1phosphodiesterase cpdA homology; phosphoesterase core !1homology KEYWORDS iron; metalloprotein; phosphoric diester hydrolase FEATURE !$2-177 #domain 3',5'-cyclic-nucleotide phosphodiesterase !8cpdA homology #label CPDA\ !$2-72 #domain phosphoesterase core homology #label PEC SUMMARY #length 372 #molecular-weight 42562 #checksum 4854 SEQUENCE /// ENTRY JW0106 #type complete TITLE 3',5'-cyclic-GMP phosphodiesterase (EC 3.1.4.35) 5A - human ALTERNATE_NAMES PDE5A1 ORGANISM #formal_name Homo sapiens #common_name man DATE 26-Aug-1999 #sequence_revision 26-Aug-1999 #text_change 16-Jun-2000 ACCESSIONS JW0106 REFERENCE JW0106 !$#authors Stacey, P.; Rulten, S.; Dapling, A.; Phillips, S.C. !$#journal Biochem. Biophys. Res. Commun. (1998) 247:249-254 !$#title Molecular cloning and expression of human cGMP-binding !1cGMP-specific phosphodiesterase (PDE5). !$#cross-references MUID:98308101; PMID:9642111 !$#accession JW0106 !'##molecule_type mRNA !'##residues 1-875 ##label STA !'##cross-references GB:AJ004865; NID:g3355605; PIDN:CAA06170.1; !1PID:g3355606 GENETICS !$#gene GDB:PDE5A !'##cross-references GDB:9032947 CLASSIFICATION #superfamily 3',5'-cyclic-GMP phosphodiesterase 5A; 3', !15'-cyclic-nucleotide phosphodiesterase homology KEYWORDS alternative splicing; cGMP binding; phosphoprotein; !1phosphoric diester hydrolase FEATURE !$612-835 #domain 3',5'-cyclic-nucleotide phosphodiesterase !8homology #label CNPD\ !$102 #binding_site phosphate (Ser) (covalent) (by !8cGMP-dependent kinase) #status predicted SUMMARY #length 875 #molecular-weight 100012 #checksum 6188 SEQUENCE /// ENTRY A48719 #type complete TITLE 3',5'-cyclic-GMP phosphodiesterase (EC 3.1.4.35) 5A - bovine ALTERNATE_NAMES PDE5A1 ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 26-Aug-1999 #sequence_revision 26-Aug-1999 #text_change 26-Aug-1999 ACCESSIONS A48719; A35807 REFERENCE A48719 !$#authors McAllister-Lucas, L.M.; Sonnenburg, W.K.; Kadlecek, A.; !1Seger, D.; Le Trong, H.; Colbran, J.L.; Thomas, M.K.; Walsh, !1K.A.; Francis, S.H.; Corbin, J.D.; Beavo, J.A. !$#journal J. Biol. Chem. (1993) 268:22863-22873 !$#title The structure of a bovine lung cGMP-binding, cGMP-specific !1phosphodiesterase deduced from a cDNA clone. !$#cross-references MUID:94043054; PMID:8226796 !$#accession A48719 !'##molecule_type mRNA !'##residues 1-875 ##label MCA !'##cross-references GB:L16545 !'##experimental_source lung REFERENCE A35807 !$#authors Thomas, M.K.; Francis, S.H.; Corbin, J.D. !$#journal J. Biol. Chem. (1990) 265:14971-14978 !$#title Substrate- and kinase-directed regulation of phosphorylation !1of a cGMP-binding phosphodiesterase by cGMP. !$#cross-references MUID:90368672; PMID:2168396 !$#accession A35807 !'##molecule_type protein !'##residues 90-101 ##label THO CLASSIFICATION #superfamily 3',5'-cyclic-GMP phosphodiesterase 5A; 3', !15'-cyclic-nucleotide phosphodiesterase homology KEYWORDS alternative splicing; cGMP binding; phosphoprotein; !1phosphoric diester hydrolase FEATURE !$602-825 #domain 3',5'-cyclic-nucleotide phosphodiesterase !8homology #label CNPD\ !$92 #binding_site phosphate (Ser) (covalent) (by !8cGMP-dependent kinase) #status predicted SUMMARY #length 875 #molecular-weight 99638 #checksum 1210 SEQUENCE /// ENTRY S06418 #type complete TITLE 3',5'-cyclic-GMP phosphodiesterase (EC 3.1.4.35) alpha chain - bovine ALTERNATE_NAMES cGMP phosphodiesterase alpha chain ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 21-Jan-2000 ACCESSIONS S06418; S27007; S00161; A34611; S08516 REFERENCE S06418 !$#authors Ovchinnikov, Y.A.; Gubanov, V.V.; Khramtsov, N.V.; Akhmedov, !1N.B.; Ishchenko, K.A.; Zagranichnyi, V.E.; Vasilevskaya, !1I.A.; Rakitina, T.V.; Atabekova, N.V.; Barinov, A.A.; !1Muradov, K.G.; Shuvaeva, T.M.; Bystrov, N.S.; Severtsova, !1I.V.; Lipkin, V.M. !$#journal Dokl. Biochem. (1987) 296:303-307 !$#title Cyclic GMP phosphodiesterase from bovine retina. Amino acid !1sequence of the alpha-subunit and nucleotide sequence of the !1corresponding cDNA. !$#accession S06418 !'##molecule_type mRNA !'##residues 1-859 ##label OV1 !'##cross-references EMBL:X12756; NID:g616; PIDN:CAA31243.1; PID:g617 !$#accession S27007 !'##molecule_type protein !'##residues !12-11;22-27;32-40;95-98;112-115;180-193;248-267;275-282; !1297-306;312-330;361-372;382-388;395-406;416-424;441-453; !1456-459;473-477;516-520;526-534;552-554;556-562;583-589; !1605-612;621-636;641-645;654-661;663-667;703-712;734-736; !1751-760;766-771;787-798;811-819 ##label OVC !'##note this paper is a translation of the Russian paper published in !1Dokl. Akad. Nauk SSSR (1987) 296: 487-491 REFERENCE S00161 !$#authors Ovchinnikov, Y.A.; Gubanov, V.V.; Khramtsov, N.V.; Ischenko, !1K.A.; Zagranichny, V.E.; Muradov, K.G.; Shuvaeva, T.M.; !1Lipkin, V.M. !$#journal FEBS Lett. (1987) 223:169-173 !$#title Cyclic GMP phosphodiesterase from bovine retina. Amino acid !1sequence of the alpha-subunit and nucleotide sequence of the !1corresponding cDNA. !$#cross-references MUID:88030033; PMID:2822478 !$#accession S00161 !'##molecule_type mRNA !'##residues 1-859 ##label OV2 !'##cross-references EMBL:M27541; NID:g162826; PIDN:AAA30441.1; !1PID:g162828 !'##note part of this sequence was confirmed by protein sequencing !'##note 381-Val was also found REFERENCE A34611 !$#authors Pittler, S.J.; Baehr, W.; Wasmuth, J.J.; McConnell, D.G.; !1Champagne, M.S.; vanTuinen, P.; Ledbetter, D.; Davis, R.L. !$#journal Genomics (1990) 6:272-283 !$#title Molecular characterization of human and bovine rod !1photoreceptor cGMP phosphodiesterase alpha-subunit and !1chromosomal localization of the human gene. !$#cross-references MUID:90169986; PMID:2155175 !$#accession A34611 !'##molecule_type mRNA !'##residues 1-193,'V',195-423,'T',425-674,'F',676-859 ##label PIT !'##cross-references GB:M26043; NID:g162833; PIDN:AAA30443.1; !1PID:g162834 COMMENT This protein is involved in the transduction and !1amplification of the visual signal. CLASSIFICATION #superfamily 3',5'-cyclic-GMP phosphodiesterase alpha chain; !13',5'-cyclic-nucleotide phosphodiesterase homology KEYWORDS acetylated amino end; cGMP; heterotrimer; phosphoric diester !1hydrolase; retina FEATURE !$2-859 #product 3',5'-cyclic-GMP phosphodiesterase alpha !8chain #status experimental #label MAT\ !$558-791 #domain 3',5'-cyclic-nucleotide phosphodiesterase !8homology #label CNP\ !$2 #modified_site acetylated amino end (Gly) (in mature !8form) #status experimental SUMMARY #length 859 #molecular-weight 99238 #checksum 9125 SEQUENCE /// ENTRY A47451 #type complete TITLE 3',5'-cyclic-GMP phosphodiesterase (EC 3.1.4.35) beta chain - dog ORGANISM #formal_name Canis lupus familiaris #common_name dog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jan-2000 ACCESSIONS A47451; S34290 REFERENCE A47451 !$#authors Suber, M.L.; Pittler, S.J.; Qin, N.; Wright, G.C.; Holcombe, !1V.; Lee, R.H.; Craft, C.M.; Lolley, R.N.; Baehr, W.; !1Hurwitz, R.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:3968-3972 !$#title Irish setter dogs affected with rod/cone dysplasia contain a !1nonsense mutation in the rod cGMP phosphodiesterase !1beta-subunit gene. !$#cross-references MUID:93248211; PMID:8387203 !$#accession A47451 !'##status preliminary !'##molecule_type mRNA !'##residues 1-856 ##label SUB !'##cross-references GB:Z23014; NID:g312327 !'##experimental_source Irish setter, retina !'##note sequence inconsistent with the nucleotide translation !'##note sequence extracted from NCBI backbone (NCBIN:130782, !1NCBIP:130783) REFERENCE S34290 !$#authors Clements, P.J. !$#submission submitted to the EMBL Data Library, June 1993 !$#accession S34290 !'##status preliminary !'##molecule_type mRNA !'##residues 1-184,'D',186-856 ##label CLE !'##cross-references EMBL:Z23014; NID:g312327; PIDN:CAA80557.1; !1PID:g312328 CLASSIFICATION #superfamily 3',5'-cyclic-GMP phosphodiesterase alpha chain; !13',5'-cyclic-nucleotide phosphodiesterase homology KEYWORDS cGMP binding; phosphoric diester hydrolase FEATURE !$556-789 #domain 3',5'-cyclic-nucleotide phosphodiesterase !8homology #label CNP SUMMARY #length 856 #molecular-weight 98475 #checksum 1717 SEQUENCE /// ENTRY ESMSGM #type complete TITLE 3',5'-cyclic-GMP phosphodiesterase (EC 3.1.4.35) gamma chain - mouse ALTERNATE_NAMES cGMP-PDE gamma chain ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 11-Jun-1999 ACCESSIONS S00612 REFERENCE S00612 !$#authors Tuteja, N.; Farber, D.B. !$#journal FEBS Lett. (1988) 232:182-186 !$#title Gamma-subunit of mouse retinal cyclic-GMP phosphodiesterase: !1cDNA and corresponding amino acid sequence. !$#cross-references MUID:88211857; PMID:2835267 !$#accession S00612 !'##molecule_type mRNA !'##residues 1-87 ##label TUT !'##cross-references EMBL:Y00746; NID:g50404; PIDN:CAA68714.1; !1PID:g50405 CLASSIFICATION #superfamily 3',5'-cyclic-GMP phosphodiesterase gamma chain KEYWORDS cGMP; phosphoric diester hydrolase SUMMARY #length 87 #molecular-weight 9637 #checksum 869 SEQUENCE /// ENTRY JH0142 #type complete TITLE 3',5'-cyclic-GMP phosphodiesterase (EC 3.1.4.35) gamma chain - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 24-Sep-1999 ACCESSIONS JH0142; S23744 REFERENCE JH0142 !$#authors Tuteja, N.; Danciger, M.; Klisak, I.; Tuteja, R.; Inana, G.; !1Mohandas, T.; Sparkes, R.S.; Farber, D.B. !$#journal Gene (1990) 88:227-232 !$#title Isolation and characterization of cDNA encoding the !1gamma-subunit of cGMP phosphodiesterase in human retina. !$#cross-references MUID:90269611; PMID:2161380 !$#accession JH0142 !'##molecule_type mRNA !'##residues 1-87 ##label TUT !'##cross-references GB:U00482; NID:g409401; PIDN:AAA03653.1; !1PID:g409403 !'##experimental_source retina !'##note the authors translated the codon GGC for residue 85 as Gln REFERENCE S23744 !$#authors Piriyev, N.I.; Purishko, V.A.; Khramtsov, N.V.; Lipkin, V.M. !$#journal Dokl. Akad. Nauk SSSR (1990) 315:229-231 !$#title Organization of the gene of the gamma-subunit of human !1photoreceptor cyclic GMP phosphodiesterase. !$#cross-references MUID:91266687; PMID:1965799 !$#accession S23744 !'##status preliminary !'##molecule_type DNA !'##residues 1-87 ##label PIR !'##cross-references EMBL:X62025; NID:g36107; PIDN:CAA43975.1; !1PID:g36108 COMMENT The gamma chain inhibits alpha- and beta-catalytic chain of !1this enzyme. GENETICS !$#gene GDB:PDE6G; PDEG !'##cross-references GDB:128660; OMIM:180073 !$#map_position 17q21.1-17q21.1 CLASSIFICATION #superfamily 3',5'-cyclic-GMP phosphodiesterase gamma chain KEYWORDS cGMP binding; phosphoric diester hydrolase SUMMARY #length 87 #molecular-weight 9643 #checksum 655 SEQUENCE /// ENTRY JC1517 #type complete TITLE 2',3'-cyclic-nucleotide 3'-phosphodiesterase (EC 3.1.4.37) long splice form - human ALTERNATE_NAMES 2',3'-cyclic nucleotide-3'-phosphohydrolase; CNPase; cyclic-CMP phosphodiesterase; nucleoside-2', 3'-cyclic-phosphate 2'-nucleotidohydrolase CONTAINS 2',3'-cyclic-nucleotide 3'-phosphodiesterase (EC 3.1.4.37) short splice form ORGANISM #formal_name Homo sapiens #common_name man DATE 14-Jul-1994 #sequence_revision 14-Jul-1994 #text_change 19-Jan-2001 ACCESSIONS JC1517; JC1518; A48934; A27703; PC4368 REFERENCE JC1517 !$#authors Monoh, K.; Kurihara, T.; Takahashi, Y.; Ichikawa, T.; !1Kumanishi, T.; Hayashi, S.; Minoshima, S.; Shimizu, N. !$#journal Gene (1993) 129:297-301 !$#title Structure, expression and chromosomal localization of the !1gene encoding human 2',3'-cyclic-nucleotide !13'-phosphodiesterase. !$#cross-references MUID:93314977; PMID:8392017 !$#accession JC1517 !'##molecule_type DNA !'##residues 1-421 ##label MON !'##cross-references DDBJ:D13144; DDBJ:D13145; DDBJ:D13146; NID:g219398; !1PIDN:BAA39694.1; PID:g219400 !'##note long form (isoform 1) !$#accession JC1518 !'##molecule_type DNA !'##residues 21-421 ##label MO2 !'##cross-references DDBJ:D13144; DDBJ:D13145; DDBJ:D13146; NID:g219398; !1PIDN:BAA02435.1; PID:g219401 !'##note short form (isoform 2) REFERENCE A48934 !$#authors Thompson, R.J. !$#journal Biochem. Soc. Trans. (1992) 20:621-626 !$#title 2',3'-cyclic nucleotide-3'-phosphohydrolase and signal !1transduction in central nervous system myelin. !$#cross-references MUID:93050745; PMID:1385234 !$#accession A48934 !'##molecule_type DNA !'##residues 1-194,'Y',196-343,'Y',345-421 ##label THO !'##cross-references GB:S46849; NID:g258813; PIDN:AAB23928.1; !1PID:g258814 !'##note this sequence is inconsistent with the nucleotide translation !'##note sequence extracted from NCBI backbone (NCBIN:116965, !1NCBIN:116968, NCBIN:116970, NCBIN:116972, NCBIP:116974) REFERENCE A27703 !$#authors Kurihara, T.; Takahashi, Y.; Nishiyama, A.; Kumanishi, T. !$#journal Biochem. Biophys. Res. Commun. (1988) 152:837-842 !$#title cDNA cloning and amino acid sequence of human brain 2', !13'-cyclic-nucleotide 3'-phosphodiesterase. !$#cross-references MUID:88209067; PMID:2835044 !$#accession A27703 !'##molecule_type mRNA !'##residues 21-421 ##label KUR !'##cross-references GB:M19650; NID:g180686; PIDN:AAA35704.1; !1PID:g180687 REFERENCE PC4368 !$#authors Stricker, R.; Kalbacher, H.; Reiser, G. !$#journal Biochem. Biophys. Res. Commun. (1997) 237:266-270 !$#title The epitope recognized by a monoclonal antibody in the !1myelin-associated protein CNP (2',3'-cyclic nucleotide !13'-phosphodiesterase). !$#cross-references MUID:97415786; PMID:9268698 !$#accession PC4368 !'##molecule_type protein !'##residues 21-58 ##label STR COMMENT This enzyme is a marker enzyme for oligodendroglia and !1myelin in the central nervous system. It hydrolyzes 2', !13'-cyclic nucleotide to produce the 2'-derivatives. GENETICS !$#gene GDB:CNP !'##cross-references GDB:128029; OMIM:123830 !$#map_position 17q21-17q21 !$#introns 1/3; 226/1; 272/3 CLASSIFICATION #superfamily 2',3'-cyclic-nucleotide 3'-phosphodiesterase KEYWORDS alternative initiators; alternative splicing; myelin; !1nucleotide binding; P-loop; phosphoric diester hydrolase FEATURE !$1-421 #product 2',3'-cyclic-nucleotide 3'-phosphodiesterase !8long splice form #status predicted #label MAT1\ !$21-421 #product 2',3'-cyclic-nucleotide 3'-phosphodiesterase !8short splice form #status predicted #label MAT2\ !$57-64 #region nucleotide-binding motif A (P-loop) SUMMARY #length 421 #molecular-weight 47578 #checksum 8052 SEQUENCE /// ENTRY ESBOP3 #type complete TITLE 2',3'-cyclic-nucleotide 3'-phosphodiesterase (EC 3.1.4.37) - bovine ALTERNATE_NAMES CNPase; cyclic-CMP phosphodiesterase; nucleoside-2', 3'-cyclic-phosphate 2'-nucleotidohydrolase ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 11-Jun-1999 ACCESSIONS A26861; A27038; A29136; A43792 REFERENCE A26861 !$#authors Vogel, U.S.; Thompson, R.J. !$#journal Nucleic Acids Res. (1987) 15:7204 !$#title Nucleotide sequence of bovine retina 2',3'-cyclic nucleotide !13'-phosphohydrolase. !$#cross-references MUID:88015580; PMID:2821502 !$#accession A26861 !'##molecule_type mRNA !'##residues 1-400 ##label VOG !'##cross-references GB:Y00405; NID:g261; PIDN:CAA68466.1; PID:g262 !'##experimental_source retina REFERENCE A27038 !$#authors Vogel, U.S.; Thompson, R.J. !$#journal FEBS Lett. (1987) 218:261-265 !$#title Molecular cloning of the myelin specific enzyme 2', !13'-cyclic-nucleotide 3'-phosphohydrolase. !$#cross-references MUID:87247281; PMID:3036592 !$#accession A27038 !'##molecule_type mRNA !'##residues 1-400 ##label VO2 !'##cross-references GB:M27606; NID:g162880; PIDN:AAA30457.1; !1PID:g162881 !'##experimental_source brain REFERENCE A29136 !$#authors Kurihara, T.; Fowler, A.V.; Takahashi, Y. !$#journal J. Biol. Chem. (1987) 262:3256-3261 !$#title cDNA cloning and amino acid sequence of bovine brain 2', !13'-cyclic-nucleotide 3'-phosphodiesterase. !$#cross-references MUID:87137604; PMID:3029107 !$#accession A29136 !'##molecule_type mRNA !'##residues 1-317,'A',319-400 ##label KUR !'##cross-references GB:J02659; NID:g162876; PIDN:AAA30456.1; !1PID:g162877 !'##note this sequence has been corrected in reference A43792 REFERENCE A43792 !$#authors Kurihara, T.; Fowler, A.V.; Takahashi, Y. !$#journal J. Biol. Chem. (1987) 262:16754 !$#title cDNA cloning and amino acid sequence of bovine brain 2', !13'-cyclic-nucleotide 3'-phosphodiesterase (correction). !$#accession A43792 !'##molecule_type mRNA !'##residues 316-320 ##label KU2 !'##cross-references GB:J02659 !'##note this reference is a correction to reference A29136 CLASSIFICATION #superfamily 2',3'-cyclic-nucleotide 3'-phosphodiesterase KEYWORDS phosphoric diester hydrolase SUMMARY #length 400 #molecular-weight 44875 #checksum 8090 SEQUENCE /// ENTRY ESMS32 #type complete TITLE 2',3'-cyclic-nucleotide 3'-phosphodiesterase (EC 3.1.4.37) 2, brain - mouse ALTERNATE_NAMES CNPase; cyclic-CMP phosphodiesterase; nucleoside-2', 3'-cyclic-phosphate 2'-nucleotidohydrolase CONTAINS 2',3'-cyclic-nucleotide 3'-phosphodiesterase 1 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 11-Jun-1999 ACCESSIONS A35708; A33788; A60056 REFERENCE A35708 !$#authors Kurihara, T.; Monoh, K.; Sakimura, K.; Takahashi, Y. !$#journal Biochem. Biophys. Res. Commun. (1990) 170:1074-1081 !$#title Alternative splicing of mouse brain 2',3'-cyclic-nucleotide !13'-phosphodiesterase mRNA. !$#cross-references MUID:90358801; PMID:2167669 !$#accession A35708 !'##molecule_type mRNA !'##residues 1-420 ##label KUR !'##cross-references GB:M31810 !'##note the authors translated the codon TGG for residue 191 as Gly REFERENCE A33788 !$#authors Monoh, K.; Kurihara, T.; Sakimura, K.; Takahashi, Y. !$#journal Biochem. Biophys. Res. Commun. (1989) 165:1213-1220 !$#title Structure of mouse 2',3'-cyclic-nucleotide !13'-phosphodiesterase gene. !$#cross-references MUID:90121227; PMID:2558653 !$#accession A33788 !'##molecule_type mRNA !'##residues 21-420 ##label MON !'##cross-references GB:M31810; NID:g192648; PIDN:AAA37429.1; !1PID:g309178 !'##note the authors translated the codon TGG for residue 191 as Gly REFERENCE A60056 !$#authors Kurihara, T.; Takahashi, Y.; Fujita, N.; Sato, S.; Miyatake, !1T. !$#journal Brain Res. Mol. Brain Res. (1989) 5:247-250 !$#title Developmental expression of 2',3'-cyclic-nucleotide !13'-phosphodiesterase mRNA in brains of normal and quaking !1mice. !$#cross-references MUID:89260946; PMID:2542718 !$#accession A60056 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 82-227 ##label KU2 COMMENT This protein is the third most abundant protein in myelin, !1after proteolipid protein and myelin basic protein. CLASSIFICATION #superfamily 2',3'-cyclic-nucleotide 3'-phosphodiesterase KEYWORDS alternative splicing; brain; myelin; phosphoric diester !1hydrolase FEATURE !$1-420 #product 2',3'-cyclic-nucleotide 3'-phosphodiesterase !82 #status predicted #label ALT2\ !$21-420 #product 2',3'-cyclic-nucleotide 3'-phosphodiesterase !81 #status predicted #label ALT1 SUMMARY #length 420 #molecular-weight 47123 #checksum 3625 SEQUENCE /// ENTRY KJHUAA #type complete TITLE cerebroside-sulfatase (EC 3.1.6.8) precursor - human ALTERNATE_NAMES arylsulfatase (EC 3.1.6.1) [misidentification]; arylsulfatase A (ASA) ORGANISM #formal_name Homo sapiens #common_name man DATE 21-Nov-1993 #sequence_revision 27-Oct-1995 #text_change 04-Feb-2000 ACCESSIONS S11031; G02857; A32207; S23932 REFERENCE S11031 !$#authors Kreysing, J.; von Figura, K.; Gieselmann, V. !$#journal Eur. J. Biochem. (1990) 191:627-631 !$#title Structure of the arylsulfatase A gene. !$#cross-references MUID:90361046; PMID:1975241 !$#accession S11031 !'##molecule_type DNA !'##residues 1-507 ##label KRE !'##cross-references EMBL:X52150; NID:g28859; PIDN:CAA36398.1; !1PID:g28860 REFERENCE H01749 !$#authors Adams, M.D.; Kerlavage, A.R.; Fuldner, R.A.; Phillips, C.A.; !1Venter, J.C. !$#submission submitted to the EMBL Data Library, June 1996 !$#accession G02857 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 'MS',1-507 ##label ADA !'##cross-references EMBL:U62317; NID:g1399959; PID:g13 !'##note an incorrect initiation codon was used REFERENCE A32207 !$#authors Stein, C.; Gieselmann, V.; Kreysing, J.; Schmidt, B.; !1Pohlmann, R.; Waheed, A.; Meyer, H.E.; O'Brien, J.S.; von !1Figura, K. !$#journal J. Biol. Chem. (1989) 264:1252-1259 !$#title Cloning and expression of human arylsulfatase A. !$#cross-references MUID:89093115; PMID:2562955 !$#accession A32207 !'##molecule_type mRNA !'##residues 1-358,'RPPAAGHRQEPSAVSLLLPVLPRRGPWGFCCADWKVQGSLLHP',402-507 !1##label STE !'##cross-references GB:X52151; GB:J04442; GB:J04593 !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing REFERENCE S23932 !$#authors Fujii, T.; Kobayashi, T.; Honke, K.; Gasa, S.; Ishikawa, M.; !1Shimizu, T.; Makita, A. !$#journal Biochim. Biophys. Acta (1992) 1122:93-98 !$#title Proteolytic processing of human lysosomal arylsulfatase A. !$#cross-references MUID:92338230; PMID:1352993 !$#accession S23932 !'##molecule_type protein !'##residues 20-29,31-33;434-479 ##label FUJ !'##experimental_source placenta REFERENCE A57113 !$#authors Schmidt, B.; Selmer, T.; Ingendoh, A.; von Figura, K. !$#journal Cell (1995) 82:271-278 !$#title A novel amino acid modification in sulfatases that is !1defective in multiple sulfatase deficiency. !$#cross-references MUID:95354208; PMID:7628016 !$#contents annotation; identification of 3-oxoalanine, !12-amino-3-oxopropanoic acid GENETICS !$#gene GDB:ARSA !'##cross-references GDB:119007; OMIM:250100 !$#map_position 22q13.31-22qter !$#introns 73/2; 153/3; 226/3; 283/2; 325/1; 367/3; 402/1 !$#note defects in this gene can cause metachromatic leukodystrophy FUNCTION !$#description hydrolyzes cerebroside 3-sulfate to release sulfate; can !1also hydrolyze galactose-3-sulfate, ascorbate 2-sulfate, and !1many phenol sulfates CLASSIFICATION #superfamily animal sulfatase KEYWORDS glycoprotein; lysosomal storage disease; lysosome; sulfuric !1ester hydrolase FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-507 #product cerebroside-sulfatase #status predicted !8#label MAT\ !$20-444,445-507 #product cerebroside-sulfatase component b #status !8predicted #label MCB\ !$20-444,448-507 #product cerebroside-sulfatase component c #status !8predicted #label MCC\ !$20-444,449-507 #product cerebroside-sulfatase minor component c !8#status predicted #label MCD\ !$69 #modified_site 3-oxoalanine (Cys) #status !8experimental\ !$158 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$184,350 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 507 #molecular-weight 53588 #checksum 6235 SEQUENCE /// ENTRY KJHUG6 #type complete TITLE N-acetylgalactosamine-6-sulfatase (EC 3.1.6.4) precursor [validated] - human ALTERNATE_NAMES chondroitinase; chondroitinsulfatase; galactose-6-sulfate sulfatase; N-acetylgalactosamine-6-sulfate 6-sulfohydrolase ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1992 #sequence_revision 27-Oct-1995 #text_change 08-Dec-2000 ACCESSIONS JQ1299; PQ0242; I37406 REFERENCE JQ1299 !$#authors Tomatsu, S.; Fukuda, S.; Masue, M.; Sukegawa, K.; Fukao, T.; !1Yamagishi, A.; Hori, T.; Iwata, H.; Ogawa, T.; Nakashima, !1Y.; Hanyu, Y.; Hashimoto, T.; Titani, K.; Oyama, R.; Suzuki, !1M.; Yagi, K.; Hayashi, Y.; Orii, T. !$#journal Biochem. Biophys. Res. Commun. (1991) 181:677-683 !$#title Morquio disease: isolation, characterization and expression !1of full-length cDNA for human !1N-acetylgalactosamine-6-sulfate sulfatase. !$#cross-references MUID:92095973; PMID:1755850 !$#accession JQ1299 !'##molecule_type mRNA !'##residues 1-522 ##label TOM !'##experimental_source placenta !$#accession PQ0242 !'##molecule_type protein !'##residues 27-42,'X',44-54;175-183,'X', !1185-192;201-218;243-265;311-324,'XX',327-336;377-404,'X', !1405-407,'X',409-417,'C',419-431,'E',433-436;518-522 ##label !1TOM1 REFERENCE I37406 !$#authors Morris, C.P.; Guo, X.H.; Apostolou, S.; Hopwood, J.J.; !1Scott, H.S. !$#journal Genomics (1994) 22:652-654 !$#title Morquio A syndrome: cloning, sequence, and structure of the !1human N-acetylgalactosamine 6-sulfatase (GALNS) gene. !$#cross-references MUID:95095267; PMID:8001980 !$#accession I37406 !'##status preliminary; translation not shown !'##molecule_type DNA !'##residues 1-522 ##label RES !'##cross-references EMBL:U06088; NID:g507365; PIDN:AAC51350.1; !1PID:g618426 !'##note nucleotide sequence not complete GENETICS !$#gene GDB:GALNS !'##cross-references GDB:129085; OMIM:253000 !$#map_position 16q24-16q24 !$#introns 40/3; 82/1; 107/1; 141/2; 189/2; 211/3; 253/2; 300/1; 334/3; !1380/2; 414/3; 455/2; 494/3 !$#note defects in this gene can cause mucopolysaccharidosis type IV !1A, Morquio disease FUNCTION !$#description hydrolyzes N-acetylgalactosamine-6-sulfate units in !1chondroitin sulfate and galactose-6-sulfate units in keratan !1sulfate to release sulfate CLASSIFICATION #superfamily animal sulfatase KEYWORDS glycoprotein; sulfuric ester hydrolase FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-522 #product N-acetylgalactosamine-6-sulfatase #status !8experimental #label MAT\ !$79 #modified_site 3-oxoalanine (Cys) #status predicted\ !$204,423 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 522 #molecular-weight 58026 #checksum 3633 SEQUENCE /// ENTRY KJHUAC #type complete TITLE steryl-sulfatase (EC 3.1.6.2) precursor - human ALTERNATE_NAMES arylsulfatase C; steroid sulfatase (STS); steryl-sulfate sulfohydrolase; sterylsulfatase ORGANISM #formal_name Homo sapiens #common_name man DATE 21-May-1990 #sequence_revision 27-Oct-1995 #text_change 11-May-2000 ACCESSIONS A32641; A57116; A25961; S05415; S05423; I52800; I65619 REFERENCE A32641 !$#authors Stein, C.; Hille, A.; Seidel, J.; Rijnbout, S.; Waheed, A.; !1Schmidt, B.; Geuze, H.; von Figura, K. !$#journal J. Biol. Chem. (1989) 264:13865-13872 !$#title Cloning and expression of human steroid-sulfatase. Membrane !1topology, glycosylation, and subcellular distribution in !1BHK-21 cells. !$#cross-references MUID:89340479; PMID:2668275 !$#accession A32641 !'##molecule_type mRNA !'##residues 1-583 ##label STE !'##cross-references GB:J04964; NID:g338564; PIDN:AAA60597.1; !1PID:g338565 !'##experimental_source BHK-21 cells !'##note parts of this sequence were determined by protein sequencing REFERENCE A57116 !$#authors Yen, P.H. !$#citation unpublished results 1988, cited by GenBank !$#accession A57116 !'##molecule_type mRNA !'##residues 1-22,'E',24-583 ##label YEN1 !'##cross-references GB:M16505; NID:g338513; PIDN:AAA60596.1; !1PID:g338514 REFERENCE A25961 !$#authors Yen, P.H.; Allen, E.; Marsh, B.; Mohandas, T.; Wang, N.; !1Taggart, R.T.; Shapiro, L.J. !$#journal Cell (1987) 49:443-454 !$#title Cloning and expression of steroid sulfatase cDNA and the !1frequent occurrence of deletions in STS deficiency: !1implications for X-Y interchange. !$#cross-references MUID:87187642; PMID:3032454 !$#accession A25961 !'##molecule_type mRNA !'##residues 1-22,'E',24-456, !1'LRTTHPSGRPFSSPPTSTPWFQRIALPHTCASVSGVMSPITTHLYSLIFP', !1'KIPERETH' ##label YEN2 !'##cross-references GB:M16505; NID:g338513 !'##note this sequence revised in A57116 !'##note part of this sequence, including the amino end of the mature !1protein, was determined by protein sequencing REFERENCE S05414 !$#authors Kawano, J.I.; Kotani, T.; Ohtaki, S.; Minamino, N.; Matsuo, !1H.; Oinuma, T.; Aikawa, E. !$#journal Biochim. Biophys. Acta (1989) 997:199-205 !$#title Characterization of rat and human steroid sulfatases. !$#cross-references MUID:89352671; PMID:2765556 !$#accession S05415 !'##molecule_type protein !'##residues 22-43,'X',45-46 ##label KAW REFERENCE S05423 !$#authors Dibbelt, L.; Otto, J.; Kuss, E. !$#journal Biol. Chem. Hoppe-Seyler (1989) 370:847-848 !$#title The N-terminal amino-acid sequence of human placental !1sterylsulfatase. !$#cross-references MUID:90074181; PMID:2590467 !$#accession S05423 !'##molecule_type protein !'##residues 22-35 ##label DIB REFERENCE I52800 !$#authors Yen, P.H.; Marsh, B.; Allen, E.; Tsai, S.P.; Ellison, J.; !1Connolly, L.; Neiswanger, K.; Shapiro, L.J. !$#journal Cell (1988) 55:1123-1135 !$#title The human X-linked steroid sulfatase gene and a Y-encoded !1pseudogene: evidence for an inversion of the Y chromosome !1during primate evolution. !$#cross-references MUID:89077541; PMID:3203382 !$#accession I52800 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 134-274 ##label YEN3 !'##cross-references GB:M23945; NID:g338604; PIDN:AAA60598.1; !1PID:g338607 !$#accession I65619 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 461-583 ##label YEN4 !'##cross-references GB:M23556; NID:g338605; PIDN:AAA60599.1; !1PID:g338608 GENETICS !$#gene GDB:STS !'##cross-references GDB:120393; OMIM:308100 !$#map_position Xp22.32-Xp22.32 !$#note defects in this gene can cause X-linked ichthyosis FUNCTION !$#description hydrolyzes 3beta-hydroxysteroid sulfates to release sulfate CLASSIFICATION #superfamily animal sulfatase KEYWORDS endoplasmic reticulum; glycoprotein; lysosome; microsome; !1sulfuric ester hydrolase; transmembrane protein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-583 #product steryl-sulfatase #status predicted #label !8MAT\ !$185-211 #domain transmembrane #status predicted #label TM1\ !$213-237 #domain transmembrane #status predicted #label TM2\ !$47,259 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$75 #modified_site 3-oxoalanine (Cys) #status predicted\ !$333,459 #binding_site carbohydrate (Asn) (covalent) #status !8absent SUMMARY #length 583 #molecular-weight 65492 #checksum 7062 SEQUENCE /// ENTRY KJHUAB #type complete TITLE N-acetylgalactosamine-4-sulfatase (EC 3.1.6.12) precursor [validated] - human ALTERNATE_NAMES arylsulfatase B (ASB); chondroitinase; chondroitinsulfatase; G4S; N-acetyl-D-galactosamine-4-sulfate 4-sulfohydrolase ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1993 #sequence_revision 27-Oct-1995 #text_change 08-Dec-2000 ACCESSIONS S35990; S33307; A35078; A45659; A42449; B42449; C42449; !1I54217; A56865 REFERENCE S35990 !$#authors Peters, C.W.B. !$#submission submitted to the EMBL Data Library, March 1993 !$#accession S35990 !'##molecule_type DNA !'##residues 1-533 ##label PET !'##cross-references EMBL:X72735; NID:g289009; PIDN:CAA51272.1; !1PID:g825628 REFERENCE S33307 !$#authors Modaressi, S.; Rupp, K.; von Figura, K.; Peters, C. !$#journal Biol. Chem. Hoppe-Seyler (1993) 374:327-335 !$#title Structure of the human arylsulfatase B gene. !$#cross-references MUID:93332648; PMID:7687847 !$#accession S33307 !'##molecule_type DNA !'##residues 1-104 ##label MOD !'##cross-references EMBL:X72735; EMBL:X72736; EMBL:X72737; EMBL:X72738; !1EMBL:X72739; EMBL:X72740; EMBL:X72741; EMBL:X72742 !'##note the enzyme is referred to as EC 3.1.6.9 REFERENCE A35078 !$#authors Peters, C.; Schmidt, B.; Rommerskirch, W.; Rupp, K.; !1Zuehlsdorf, M.; Vingron, M.; Meyer, H.E.; Pohlmann, R.; von !1Figura, K. !$#journal J. Biol. Chem. (1990) 265:3374-3381 !$#title Phylogenetic conservation of arylsulfatases. cDNA cloning !1and expression of human arylsulfatase B. !$#cross-references MUID:90153994; PMID:2303452 !$#accession A35078 !'##molecule_type mRNA !'##residues 1-357,'V',359-533 ##label PE2 !'##cross-references GB:J05225; NID:g179076; PIDN:AAA51784.1; !1PID:g179077 !'##note parts of this sequence were determined by protein sequencing !'##note the enzyme is referred to as EC 3.1.6.1 REFERENCE A45659 !$#authors Litjens, T.; Morris, C.P.; Gibson, G.J.; Beckmann, K.R.; !1Hopwood, J.J. !$#journal Biochem. Int. (1991) 24:209-215 !$#title Human N-acetylgalactosamine-4-sulphatase: protein maturation !1and isolation of genomic clones. !$#cross-references MUID:92028992; PMID:1930244 !$#accession A45659 !'##molecule_type DNA; protein !'##residues 1-104 ##label LIT !'##cross-references GB:S57777; NID:g236697; PIDN:AAB19988.1; !1PID:g236698 !'##note sequence extracted from NCBI backbone (NCBIN:57777, !1NCBIP:57778) !'##note the enzyme is referred to as EC 3.1.6.1 !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing !'##note a form is described with a proteolytic cleavage somewhere !1between residue 450 and residue 469, the amino terminal of !1the cleaved chain REFERENCE A42449 !$#authors Jin, W.D.; Jackson, C.E.; Desnick, R.J.; Schuchman, E.H. !$#journal Am. J. Hum. Genet. (1992) 50:795-800 !$#title Mucopolysaccharidosis type VI: identification of three !1mutations in the arylsulfatase B gene of patients with the !1severe and mild phenotypes provides molecular evidence for !1genetic heterogeneity. !$#cross-references MUID:92197625; PMID:1550123 !$#accession A42449 !'##molecule_type mRNA !'##residues 115-116,'R',118 ##label JIN !'##cross-references GB:S90729; NID:g247486; PIDN:AAB21831.1; !1PID:g247487 !'##note sequence extracted from NCBI backbone (NCBIN:90729, !1NCBIP:90731) !$#accession B42449 !'##molecule_type mRNA !'##residues 234-235,'P',237-238 ##label JI2 !'##cross-references GB:S90736; NID:g247488; PIDN:AAB21832.1; !1PID:g247489 !'##note sequence extracted from NCBI backbone (NCBIN:90736, !1NCBIP:90739) !$#accession C42449 !'##molecule_type mRNA !'##residues 403-404,'Y',406-407 ##label JI3 !'##cross-references GB:S90743; NID:g247490; PIDN:AAB21833.1; !1PID:g247491 !'##note sequence extracted from NCBI backbone (NCBIN:90743, !1NCBIP:90747) !'##note the enzyme is referred to as EC 3.1.6.1 !'##note these mutations give rise to mucopolysaccharidosis type VI, !1Maroteaux-Lamy disease REFERENCE A57113 !$#authors Schmidt, B.; Selmer, T.; Ingendoh, A.; von Figura, K. !$#journal Cell (1995) 82:271-278 !$#title A novel amino acid modification in sulfatases that is !1defective in multiple sulfatase deficiency. !$#cross-references MUID:95354208; PMID:7628016 !$#contents annotation; identification of 3-oxoalanine, !12-amino-3-oxopropanoic acid REFERENCE I54217 !$#authors Schuchman, E.H.; Jackson, C.E.; Desnick, R.J. !$#journal Genomics (1990) 6:149-158 !$#title Human arylsulfatase B: MOPAC cloning, nucleotide sequence of !1a full-length cDNA, and regions of amino acid identity with !1arylsulfatases A and C. !$#cross-references MUID:90152677; PMID:1968043 !$#accession I54217 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-357,'V',359-375,'M',377-533 ##label RES !'##cross-references GB:M32373; NID:g179029; PIDN:AAA51779.1; !1PID:g179030 REFERENCE A56865 !$#authors Kobayashi, T.; Honke, K.; Jin, T.; Gasa, S.; Miyazaki, T.; !1Makita, A. !$#journal Biochim. Biophys. Acta (1992) 1159:243-247 !$#title Components and proteolytic processing sites of arylsulfatase !1B from human placenta. !$#cross-references MUID:93003385; PMID:1390929 !$#accession A56865 !'##molecule_type protein !'##residues 41-55;424-425,'X',427-454;466-483 ##label KOB !'##experimental_source placenta !'##note sequence modified after extraction from NCBI backbone !'##note the fragments shown are the amino ends of the alpha, gamma, and !1beta chains of the mature (processed) protein COMMENT This enzyme is frequently misidentified as EC 3.1.6.1. GENETICS !$#gene GDB:ARSB !'##cross-references GDB:119008; OMIM:253200 !$#map_position 5q11-5q13 !$#introns 104/3; 167/1; 230/3; 300/1; 381/2; 405/1; 446/1 !$#note defects in this gene can cause mucopolysaccharidosis type !1VI, Maroteaux-Lamy disease FUNCTION !$#description hydrolyzes N-acetylgalactosamine-4-sulfate units in !1chondroitin sulfate and dermatan sulfate to release sulfate CLASSIFICATION #superfamily animal sulfatase KEYWORDS glycoprotein; lysosomal storage disease; lysosome; sulfuric !1ester hydrolase FEATURE !$1-40 #domain signal sequence #status predicted #label SIG\ !$41-423 #product alpha chain #status predicted #label AMAT\ !$424-465 #product gamma chain #status predicted #label GMAT\ !$466-533 #product beta chain #status experimental #label BMAT\ !$91 #modified_site 3-oxoalanine (Cys) #status !8experimental\ !$188,279,366,458 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$291 #binding_site carbohydrate (Asn) (covalent) #status !8absent\ !$426 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 533 #molecular-weight 59719 #checksum 9452 SEQUENCE /// ENTRY A44475 #type complete TITLE N-acetylgalactosamine-4-sulfatase (EC 3.1.6.12) precursor - cat ALTERNATE_NAMES arylsulfatase B (ARSB); chondroitinase; chondroitinsulfatase; G4S; N-acetyl-D-galactosamine-4-sulfate 4-sulfohydrolase ORGANISM #formal_name Felis silvestris catus #common_name domestic cat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A44475 REFERENCE A44475 !$#authors Jackson, C.E.; Yuhki, N.; Desnick, R.J.; Haskins, M.E.; !1O'Brien, S.J.; Schuchman, E.H. !$#journal Genomics (1992) 14:403-411 !$#title Feline arylsulfatase B (ARSB): isolation and expression of !1the cDNA, comparison with human ARSB, and gene localization !1to feline chromosome A1. !$#cross-references MUID:93052342; PMID:1427856 !$#accession A44475 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-535 ##label JAC !'##cross-references GB:S48472; NID:g258855; PIDN:AAB23941.1; !1PID:g258856 !'##experimental_source liver !'##note sequence extracted from NCBI backbone (NCBIP:117976) COMMENT This enzyme is frequently misidentified as EC 3.1.6.1. FUNCTION !$#description hydrolyzes N-acetylgalactosamine-4-sulfate units in !1chondroitin sulfate and dermatan sulfate to release sulfate CLASSIFICATION #superfamily animal sulfatase KEYWORDS glycoprotein; lysosomal storage disease; lysosome; sulfuric !1ester hydrolase FEATURE !$1-42 #domain signal sequence #status predicted #label SIG\ !$43-425 #product alpha chain #status predicted #label AMAT\ !$426-467 #product gamma chain #status predicted #label GMAT\ !$468-535 #product beta chain #status predicted #label BMAT\ !$93 #modified_site 3-oxoalanine (Cys) #status predicted\ !$190,281,428,460 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 535 #molecular-weight 59753 #checksum 9874 SEQUENCE /// ENTRY KJHUID #type complete TITLE iduronate-2-sulfatase (EC 3.1.6.13) precursor - human ALTERNATE_NAMES chondroitinsulfatase; L-iduronate 2-sulfate 2-sulfohydrolase ORGANISM #formal_name Homo sapiens #common_name man DATE 28-Mar-1991 #sequence_revision 27-Oct-1995 #text_change 24-Sep-1999 ACCESSIONS A47535; A36483 REFERENCE A47535 !$#authors Wilson, P.J.; Meaney, C.A.; Hopwood, J.J.; Morris, C.P. !$#journal Genomics (1993) 17:773-775 !$#title Sequence of the human iduronate 2-sulfatase (IDS) gene. !$#cross-references MUID:94063929; PMID:8244397 !$#accession A47535 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-550 ##label WI2 !'##cross-references GB:L13329; NID:g405203; PIDN:AAA16877.1; !1PID:g405205 REFERENCE A36483 !$#authors Wilson, P.J.; Morris, C.P.; Anson, D.S.; Occhiodoro, T.; !1Bielicki, J.; Clements, P.R.; Hopwood, J.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:8531-8535 !$#title Hunter syndrome: isolation of an iduronate-2-sulfatase cDNA !1clone and analysis of patient DNA. !$#cross-references MUID:91046030; PMID:2122463 !$#accession A36483 !'##molecule_type mRNA !'##residues 1-550 ##label WIL !'##cross-references GB:M58342; GB:M38371; NID:g184561; PIDN:AAA63197.1; !1PID:g184562 !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing !'##note a form is described with a proteolytic cleavage releasing !1residue 456 as the amino terminal of the cleaved chain GENETICS !$#gene GDB:IDS; SIDS !'##cross-references GDB:120521; OMIM:309900 !$#map_position Xq28-Xq28 !$#introns 35/1; 80/3; 140/1; 169/3; 236/3; 293/3; 336/1; 394/1 !$#note defects in this gene can cause mucopolysaccharidosis type !1II, Hunter disease FUNCTION !$#description hydrolyzes iduronate-2-sulfate units in dermatan sulfate and !1heparan sulfate to release sulfate CLASSIFICATION #superfamily animal sulfatase KEYWORDS glycoprotein; Hunter disease; lysosomal storage disease; !1lysosome; sulfuric ester hydrolase FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-33 #domain propeptide #status predicted #label PRO\ !$34-550 #product iduronate-2-sulfatase #status predicted !8#label MAT\ !$31,115,144,246,280, !$325,513,537 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$84 #modified_site 3-oxoalanine (Cys) #status predicted SUMMARY #length 550 #molecular-weight 61872 #checksum 5247 SEQUENCE /// ENTRY KJHUGU #type complete TITLE N-acetylglucosamine-6-sulfatase (EC 3.1.6.14) precursor - human ALTERNATE_NAMES chondroitinsulfatase; N-acetyl-D-glucosamine-6-sulfate 6-sulfohydrolase ORGANISM #formal_name Homo sapiens #common_name man DATE 22-Nov-1993 #sequence_revision 27-Oct-1995 #text_change 24-Sep-1999 ACCESSIONS S27164; A31672 REFERENCE S27164 !$#authors Robertson, D.A.; Freeman, C.; Morris, C.P.; Hopwood, J.J. !$#journal Biochem. J. (1992) 288:539-544 !$#title A cDNA clone for human glucosamine-6-sulphatase reveals !1differences between arylsulphatases and non-arylsulphatases. !$#cross-references MUID:93098807; PMID:1463457 !$#accession S27164 !'##molecule_type mRNA !'##residues 1-552 ##label ROB !'##cross-references GB:Z12173; EMBL:M23657; NID:g31866; !1PIDN:CAA78164.1; PID:g31867 !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing !'##note a form is described with a proteolytic cleavage releasing !1residue 222 as the amino terminal of the cleaved chain REFERENCE A31672 !$#authors Robertson, D.A.; Freeman, C.; Nelson, P.V.; Morris, C.P.; !1Hopwood, J.J. !$#journal Biochem. Biophys. Res. Commun. (1988) 157:218-224 !$#title Human glucosamine-6-sulfatase cDNA reveals homology with !1steroid sulfatase. !$#cross-references MUID:89061714; PMID:3196333 !$#accession A31672 !'##molecule_type mRNA !'##residues 178-552 ##label RO2 !'##cross-references GB:Z12173; EMBL:M23657; NID:g31866 GENETICS !$#gene GDB:GNS !'##cross-references GDB:120006; OMIM:252940 !$#map_position 12q14-12q14 !$#note defects in this gene can cause mucopolysaccharidosis type !1III D, Sanfilippo D disease FUNCTION !$#description hydrolyzes N-acetyl-D-glucosamine 6-sulfate units in heparan !1sulfate and keratan sulfate to release sulfate CLASSIFICATION #superfamily animal sulfatase KEYWORDS glycoprotein; lysosomal storage disease; lysosome; !1Sanfilippo disease; sulfuric ester hydrolase FEATURE !$1-43 #domain signal sequence #status predicted #label SIG\ !$44-552 #product N-acetylglucosamine-6-sulfatase #status !8predicted #label MAT\ !$91 #modified_site 3-oxoalanine (Cys) #status predicted\ !$111,117,183,198, !$210,279,317,362, !$387,405,449,480 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$422 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 552 #molecular-weight 62082 #checksum 2417 SEQUENCE /// ENTRY KJKM #type complete TITLE arylsulfatase (EC 3.1.6.1) precursor - Chlamydomonas reinhardtii ALTERNATE_NAMES sulfatase ORGANISM #formal_name Chlamydomonas reinhardtii DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 24-Sep-1999 ACCESSIONS JQ0310 REFERENCE JQ0310 !$#authors de Hostos, E.L.; Schilling, J.; Grossman, A.R. !$#journal Mol. Gen. Genet. (1989) 218:229-239 !$#title Structure and expression of the gene encoding the !1periplasmic arylsulfatase of Chlamydomonas reinhardtii. !$#cross-references MUID:89384447; PMID:2476654 !$#accession JQ0310 !'##molecule_type mRNA !'##residues 1-646 ##label DEH !'##cross-references GB:X16180; NID:g18118; PIDN:CAA34302.1; PID:g18119; !1GB:X52304; NID:g18173; PIDN:CAA36545.1; PID:g18174 !'##experimental_source strain cw15mt+ !'##note part of this sequence, including the amino end of the mature !1protein, was determined by protein sequencing COMMENT This enzyme is commonly produced by soil microorganisms and !1plays an important role in the mineralization of sulfate. CLASSIFICATION #superfamily plant sulfatase KEYWORDS glycoprotein; sulfuric ester hydrolase FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-646 #product arylsulfatase #status predicted #label MAT\ !$42,443,527 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$73 #modified_site 3-oxoalanine (Cys) #status predicted SUMMARY #length 646 #molecular-weight 70543 #checksum 7703 SEQUENCE /// ENTRY SHECGD #type complete TITLE guanosine-3',5'-bis(diphosphate) 3'-diphosphatase (EC 3.1.7.2) - Escherichia coli (strain K-12) ALTERNATE_NAMES (ppGpp)ase ORGANISM #formal_name Escherichia coli DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 03-Jun-2002 ACCESSIONS B30374; D65166; JV0042; Q00796 REFERENCE A30374 !$#authors Sarubbi, E.; Rudd, K.E.; Xiao, H.; Ikehara, K.; Kalman, M.; !1Cashel, M. !$#journal J. Biol. Chem. (1989) 264:15074-15082 !$#title Characterization of the spoT gene of Escherichia coli. !$#cross-references MUID:89359321; PMID:2549050 !$#accession B30374 !'##molecule_type DNA !'##residues 1-702 ##label SAR !'##cross-references GB:M24503; GB:J04976; NID:g147863; PIDN:AAB00160.1; !1PID:g551840 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65166 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-702 ##label BLAT !'##cross-references GB:AE000442; GB:U00096; NID:g2367253; !1PIDN:AAC76674.1; PID:g1790082; UWGP:b3650 !'##experimental_source strain K-12, substrain MG1655 COMMENT This enzyme is responsible for the control of cellular !1degradation of guanosine-3',5'-bis(diphosphate). GENETICS !$#gene spoT !$#map_position 82 min !$#start_codon TTG CLASSIFICATION #superfamily guanosine 3',5'-bis(diphosphate) !13'-pyrophosphatase KEYWORDS diphosphoric monoester hydrolase SUMMARY #length 702 #molecular-weight 79342 #checksum 8904 SEQUENCE /// ENTRY KIECG #type complete TITLE GTP diphosphokinase (EC 2.7.6.5) - Escherichia coli (strain K-12) ALTERNATE_NAMES guanosine 3',5'-polyphosphate synthase; stringent factor ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 17-Oct-1997 #text_change 03-Jun-2002 ACCESSIONS D65060; A31996 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65060 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-744 ##label BLAT !'##cross-references GB:AE000362; GB:U00096; NID:g1789143; !1PIDN:AAC75826.1; PID:g1789147; UWGP:b2784 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A31996 !$#authors Metzger, S.; Dror, I.B.; Aizenman, E.; Schreiber, G.; Toone, !1M.; Friesen, J.D.; Cashel, M.; Glaser, G. !$#journal J. Biol. Chem. (1988) 263:15699-15704 !$#title The nucleotide sequence and characterization of the relA !1gene of Escherichia coli. !$#cross-references MUID:89008481; PMID:2844820 !$#accession A31996 !'##molecule_type DNA !'##residues 1-306,'K',308-744 ##label MET !'##cross-references GB:J04039; NID:g416195; PIDN:AAA03237.1; !1PID:g147562 COMMENT This enzyme catalyzes the formation of guanosine !15'-triphosphate 3'-diphosphate (pppGpp), which is then !1hydrolyzed to ppGpp under stringent response to amino acid !1starvation. This is the firt step in ppGpp metabolism. GENETICS !$#gene relA !$#map_position 60 min CLASSIFICATION #superfamily guanosine 3',5'-bis(diphosphate) !13'-pyrophosphatase KEYWORDS diphosphotransferase SUMMARY #length 744 #molecular-weight 83875 #checksum 6057 SEQUENCE /// ENTRY E69844 #type complete TITLE GTP pyrophosphokinase homolog yjbM - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS E69844 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69844 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-211 ##label KUN !'##cross-references GB:Z99110; GB:AL009126; NID:g2633472; !1PIDN:CAB13017.1; PID:g2633514 !'##experimental_source strain 168 GENETICS !$#gene yjbM CLASSIFICATION #superfamily GTP pyrophosphokinase related protein SUMMARY #length 211 #molecular-weight 24704 #checksum 9834 SEQUENCE /// ENTRY S39662 #type complete TITLE GTP-pyrophosphokinase homolog ywaC - Bacillus subtilis ALTERNATE_NAMES protein ipa-7d ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S39662; C70050 REFERENCE S39655 !$#authors Glaser, P.; Kunst, F.; Arnaud, M.; Coudart, M.P.; Gonzales, !1W.; Hullo, M.F.; Ionescu, M.; Lubochinsky, B.; Marcelino, !1L.; Moszer, I.; Presecan, E.; Santana, M.; Schneider, E.; !1Schweizer, J.; Vertes, A.; Rapoport, G.; Danchin, A. !$#journal Mol. Microbiol. (1993) 10:371-384 !$#title Bacillus subtilis genome project: cloning and sequencing of !1the 97 kb region from 325 degrees to 333 degrees. !$#cross-references MUID:95020537; PMID:7934828 !$#accession S39662 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-210 ##label GLA !'##cross-references EMBL:X73124; NID:g413923; PIDN:CAA51563.1; !1PID:g413931 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1993 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C70050 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-210 ##label KUN !'##cross-references GB:Z99123; GB:AL009126; NID:g2636240; !1PIDN:CAB15874.1; PID:g2636383 !'##experimental_source strain 168 GENETICS !$#gene ywaC CLASSIFICATION #superfamily GTP pyrophosphokinase related protein SUMMARY #length 210 #molecular-weight 24599 #checksum 4296 SEQUENCE /// ENTRY JS0349 #type complete TITLE exonuclease (EC 3.1.-.-) sbcD - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 01-Mar-2002 ACCESSIONS JS0349; F64768; S06603 REFERENCE JS0349 !$#authors Naom, I.S.; Morton, S.J.; Leach, D.R.F.; Lloyd, R.G. !$#journal Nucleic Acids Res. (1989) 17:8033-8045 !$#title Molecular organization of sbcC, a gene that affects genetic !1recombination and the viability of DNA palindromes in !1Escherichia coli K-12. !$#cross-references MUID:90045931; PMID:2530497 !$#accession JS0349 !'##molecule_type DNA !'##residues 1-400 ##label NAO !'##cross-references GB:X15981; NID:g42912; PIDN:CAA34103.1; PID:g42913 !'##experimental_source strain K12 !'##note the codon for the carboxyl end of this sequence overlaps with !1the start codon of the sbcC gene by 1 base pair REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64768 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-400 ##label BLAT !'##cross-references GB:AE000146; GB:U00096; NID:g1786596; !1PIDN:AAC73501.1; PID:g1786598; UWGP:b0398 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene sbcD !$#map_position 9 min CLASSIFICATION #superfamily exonuclease sbcD; phosphoesterase core homology KEYWORDS exonuclease; hydrolase FEATURE !$2-85 #domain phosphoesterase core homology #label PEC SUMMARY #length 400 #molecular-weight 44713 #checksum 598 SEQUENCE /// ENTRY D70203 #type complete TITLE exonuclease (EC 3.1.-.-) sbcD homolog - Lyme disease spirochete ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 13-Feb-1998 #sequence_revision 13-Feb-1998 #text_change 11-Jun-1999 ACCESSIONS D70203 REFERENCE A70100 !$#authors Fraser, C.M.; Casjens, S.; Huang, W.M.; Sutton, G.G.; !1Clayton, R.; Lathigra, R.; White, O.; Ketchum, K.A.; Dodson, !1R.; Hickey, E.K.; Gwinn, M.; Dougherty, B.; Tomb, J.F.; !1Fleischmann, R.D.; Richardson, D.; Peterson, J.; Kerlavage, !1A.R.; Quackenbush, J.; Salzberg, S.; Hanson, M.; Vugt, R.V.; !1Palmer, N.; Adams, M.D.; Gocayne, J.; Weidman, J.; !1Utterback, T.; Watthey, L.; McDonald, L.; Artiach, P.; !1Bowman, C.; Garland, S.; Fujii, C.; Cotton, M.D.; Horst, K.; !1Roberts, K.; Hatch, B.; Smith, H.O.; Venter, J.C. !$#journal Nature (1997) 390:580-586 !$#title Genomic sequence of a Lyme disease spirochaete, Borrelia !1burgdorferi. !$#cross-references MUID:98065943; PMID:9403685 !$#accession D70203 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-413 ##label KLE !'##cross-references GB:AE001181; GB:AE000783; NID:g2688772; !1PIDN:AAC67182.1; PID:g2688778; TIGR:BB0829 !'##experimental_source strain B31 CLASSIFICATION #superfamily exonuclease sbcD; phosphoesterase core homology KEYWORDS exonuclease; hydrolase FEATURE !$5-89 #domain phosphoesterase core homology #label PEC SUMMARY #length 413 #molecular-weight 48240 #checksum 4442 SEQUENCE /// ENTRY E70462 #type complete TITLE ATP-dependent dsDNA exonuclease (EC 3.1.-.-) - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 08-May-1998 #sequence_revision 15-May-1998 #text_change 11-Jun-1999 ACCESSIONS E70462 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession E70462 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-379 ##label AQF !'##cross-references GB:AE000761; NID:g2984149; PIDN:AAC07689.1; !1PID:g2984155; GB:AE000657 !'##experimental_source strain VF5 GENETICS !$#gene sbcD CLASSIFICATION #superfamily exonuclease sbcD; phosphoesterase core homology KEYWORDS exonuclease; hydrolase FEATURE !$2-85 #domain phosphoesterase core homology #label PEC SUMMARY #length 379 #molecular-weight 43589 #checksum 8793 SEQUENCE /// ENTRY H75336 #type complete TITLE probable exonuclease (EC 3.1.-.-) sbcD-type DR1921 [similarity] - Deinococcus radiodurans (strain R1) ORGANISM #formal_name Deinococcus radiodurans DATE 03-Aug-2001 #sequence_revision 03-Aug-2001 #text_change 03-Aug-2001 ACCESSIONS H75336 REFERENCE A75250 !$#authors White, O.; Eisen, J.A.; Heidelberg, J.F.; Hickey, E.K.; !1Peterson, J.D.; Dodson, R.J.; Haft, D.H.; Gwinn, M.L.; !1Nelson, W.C.; Richardson, D.L.; Moffat, K.S.; Qin, H.; !1Jiang, L.; Pamphile, W.; Crosby, M.; Shen, M.; Vamathevan, !1J.J.; Lam, P.; McDonald, L.; Utterback, T.; Zalewski, C.; !1Makarova, K.S.; Aravind, L.; Daly, M.J.; Minton, K.W.; !1Fleischmann, R.D.; Ketchum, K.A.; Nelson, K.E.; Salzberg, !1S.; Smith, H.O.; Venter, J.C.; Fraser, C.M. !$#journal Science (1999) 286:1571-1577 !$#title Genome sequence of the radioresistant bacterium Deinococcus !1radiodurans R1. !$#cross-references MUID:20036896; PMID:10567266 !$#accession H75336 !'##molecule_type DNA !'##residues 1-416 ##label WHI !'##cross-references GB:AE002032; GB:AE000513; NID:g6459715; !1PIDN:AAF11473.1; PID:g6459705; TIGR:DR1921; GSPDB:GN00077 !'##experimental_source strain R1 GENETICS !$#gene DR1921 !$#map_position 1 CLASSIFICATION #superfamily exonuclease sbcD; phosphoesterase core homology KEYWORDS exonuclease; hydrolase FEATURE !$25-108 #domain phosphoesterase core homology #label PEC SUMMARY #length 416 #molecular-weight 44968 #checksum 3669 SEQUENCE /// ENTRY B86790 #type complete TITLE probable exonuclease (EC 3.1.-.-) sbcD-type [similarity] - Lactococcus lactis subsp. lactis (strain IL1403) ORGANISM #formal_name Lactococcus lactis subsp. lactis DATE 03-Aug-2001 #sequence_revision 03-Aug-2001 #text_change 03-Aug-2001 ACCESSIONS B86790 REFERENCE A86625 !$#authors Bolotin, A.; Wincker, P.; Mauger, S.; Jaillon, O.; Malarme, !1K.; Weissenbach, J.; Ehrlich, S.D.; Sorokin, A. !$#journal Genome Res. (2001) 11:731-753 !$#title The complete genome sequence of the lactic acid bacterium !1Lactococcus lactis ssp. lactis IL1403. !$#cross-references MUID:21235186; PMID:11337471 !$#accession B86790 !'##molecule_type DNA !'##residues 1-390 ##label STO !'##cross-references GB:AE005176; NID:g12724302; PIDN:AAK05420.1; !1GSPDB:GN00146 !'##experimental_source strain IL1403 GENETICS !$#gene sbcD CLASSIFICATION #superfamily exonuclease sbcD; phosphoesterase core homology KEYWORDS exonuclease; hydrolase FEATURE !$2-86 #domain phosphoesterase core homology #label PEC SUMMARY #length 390 #molecular-weight 44901 #checksum 2769 SEQUENCE /// ENTRY F82450 #type complete TITLE probable exonuclease (EC 3.1.-.-) sbcD-type VCA0520 [similarity] - Vibrio cholerae (strain N16961 serogroup O1) ORGANISM #formal_name Vibrio cholerae DATE 03-Aug-2001 #sequence_revision 03-Aug-2001 #text_change 03-Aug-2001 ACCESSIONS F82450 REFERENCE A82035 !$#authors Heidelberg, J.F.; Eisen, J.A.; Nelson, W.C.; Clayton, R.A.; !1Gwinn, M.L.; Dodson, R.J.; Haft, D.H.; Hickey, E.K.; !1Peterson, J.D.; Umayam, L.A.; Gill, S.R.; Nelson, K.E.; !1Read, T.D.; Tettelin, H.; Richardson, D.; Ermolaeva, M.D.; !1Vamathevan, J.; Bass, S.; Qin, H.; Dragoi, I.; Sellers, P.; !1McDonald, L.; Utterback, T.; Fleishmann, R.D.; Nierman, !1W.C.; White, O.; Salzberg, S.L.; Smith, H.O.; Colwell, R.R.; !1Mekalanos, J.J.; Venter, J.C.; Fraser, C.M. !$#journal Nature (2000) 406:477-483 !$#title DNA Sequence of both chromosomes of the cholera pathogen !1Vibrio cholerae. !$#cross-references MUID:20406833; PMID:10952301 !$#accession F82450 !'##molecule_type DNA !'##residues 1-379 ##label HEI !'##cross-references GB:AE004382; GB:AE003853; NID:g9657917; !1PIDN:AAF96423.1; GSPDB:GN00127; TIGR:VCA0520 !'##experimental_source serogroup O1; strain N16961; biotype El Tor GENETICS !$#gene VCA0520 !$#map_position 2 CLASSIFICATION #superfamily exonuclease sbcD; phosphoesterase core homology KEYWORDS exonuclease; hydrolase FEATURE !$2-86 #domain phosphoesterase core homology #label PEC SUMMARY #length 379 #molecular-weight 42623 #checksum 7438 SEQUENCE /// ENTRY C71302 #type complete TITLE probable exonuclease (EC 3.1.-.-) sbcD-type TP0626 [similarity] - syphilis spirochete ORGANISM #formal_name Treponema pallidum subsp. pallidum #common_name syphilis spirochete DATE 03-Aug-2001 #sequence_revision 03-Aug-2001 #text_change 03-Aug-2001 ACCESSIONS C71302 REFERENCE A71250 !$#authors Fraser, C.M.; Norris, S.J.; Weinstock, G.M.; White, O.; !1Sutton, G.G.; Dodson, R.; Gwinn, M.; Hickey, E.K.; Clayton, !1R.; Ketchum, K.A.; Sodergren, E.; Hardham, J.M.; McLeod, !1M.P.; Salzberg, S.; Peterson, J.; Khalak, H.; Richardson, !1D.; Howell, J.K.; Chidambaram, M.; Utterback, T.; McDonald, !1L.; Artiach, P.; Bowman, C.; Cotton, M.D.; Fujii, C.; !1Garland, S.; Hatch, B.; Horst, K.; Roberts, K.; Watthey, L.; !1Weidman, J.; Smith, H.O.; Venter, J.C. !$#journal Science (1998) 281:375-388 !$#title Complete genome sequence of Treponema pallidum, the syphilis !1spirochete. !$#cross-references MUID:98332770; PMID:9665876 !$#accession C71302 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-391 ##label COL !'##cross-references GB:AE001237; GB:AE000520; NID:g3322916; !1PIDN:AAC65598.1; PID:g3322921 !'##experimental_source strain Nichols GENETICS !$#gene TP0626 CLASSIFICATION #superfamily exonuclease sbcD; phosphoesterase core homology KEYWORDS exonuclease; hydrolase FEATURE !$2-87 #domain phosphoesterase core homology #label PEC SUMMARY #length 391 #molecular-weight 44297 #checksum 4520 SEQUENCE /// ENTRY T03466 #type complete TITLE probable exonuclease (EC 3.1.-.-) sbcD-type [similarity] - Rhodobacter capsulatus ORGANISM #formal_name Rhodobacter capsulatus DATE 03-Aug-2001 #sequence_revision 03-Aug-2001 #text_change 03-Aug-2001 ACCESSIONS T03466 REFERENCE Z14955 !$#authors Vlcek, C.; Paces, V.; Maltsev, N.; Paces, J.; Haselkorn, R.; !1Fonstein, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1997) 94:9384-9388 !$#title Sequence of a 189-kb segment of the chromosome of !1Rhodobacter capsulatus SB1003. !$#cross-references MUID:97404404; PMID:9256491 !$#accession T03466 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-405 ##label VLC !'##cross-references EMBL:AF010496; NID:g3128256; PIDN:AAC16119.1; !1PID:g3128267 GENETICS !$#map_position 1 CLASSIFICATION #superfamily exonuclease sbcD; phosphoesterase core homology KEYWORDS exonuclease; hydrolase FEATURE !$2-87 #domain phosphoesterase core homology #label PEC SUMMARY #length 405 #molecular-weight 42908 #checksum 6671 SEQUENCE /// ENTRY C72230 #type complete TITLE probable exonuclease (EC 3.1.-.-) sbcD-type TM1635 [similarity] - Thermotoga maritima (strain MSB8) ORGANISM #formal_name Thermotoga maritima DATE 03-Aug-2001 #sequence_revision 03-Aug-2001 #text_change 03-Aug-2001 ACCESSIONS C72230 REFERENCE A72200 !$#authors Nelson, K.E.; Clayton, R.A.; Gill, S.R.; Gwinn, M.L.; !1Dodson, R.J.; Haft, D.H.; Hickey, E.K.; Peterson, J.D.; !1Nelson, W.C.; Ketchum, K.A.; McDonald, L.; Utterback, T.R.; !1Malek, J.A.; Linher, K.D.; Garrett, M.M.; Stewart, A.M.; !1Cotton, M.D.; Pratt, M.S.; Phillips, C.A.; Richardson, D.; !1Heidelberg, J.; Sutton, G.G.; Fleischmann, R.D.; White, O.; !1Salzberg, S.L.; Smith, H.O.; Venter, J.C.; Fraser, C.M. !$#journal Nature (1999) 399:323-329 !$#title Evidence for lateral gene transfer between Archaea and !1Bacteria from genome sequence of Thermotoga maritima. !$#cross-references MUID:99287316; PMID:10360571 !$#accession C72230 !'##molecule_type DNA !'##residues 1-385 ##label ARN !'##cross-references GB:AE001806; GB:AE000512; NID:g4982196; !1PIDN:AAD36702.1; PID:g4982208; TIGR:TM1635 !'##experimental_source strain MSB8 GENETICS !$#gene TM1635 CLASSIFICATION #superfamily exonuclease sbcD; phosphoesterase core homology KEYWORDS exonuclease; hydrolase FEATURE !$8-95 #domain phosphoesterase core homology #label PEC SUMMARY #length 385 #molecular-weight 44686 #checksum 3238 SEQUENCE /// ENTRY B89910 #type complete TITLE probable exonuclease (EC 3.1.-.-) sbcD-type SA1180 [similarity] - Staphylococcus aureus (strain N315) ORGANISM #formal_name Staphylococcus aureus DATE 03-Aug-2001 #sequence_revision 03-Aug-2001 #text_change 22-Oct-2001 ACCESSIONS B89910 REFERENCE A89758 !$#authors Kuroda, M.; Ohta, T.; Uchiyama, I.; Baba, T.; Yuzawa, H.; !1Kobayashi, I.; Cui, L.; Oguchi, A.; Aoki, K.; Nagai, Y.; !1Lian, J.; Ito, T.; Kanamori, M.; Matsumaru, H.; Maruyama, !1A.; Murakami, H.; Hosoyama, A.; Mizutani-Ui, Y.; Kobayashi, !1N.; Sawano, T.; Inoue, R.; Kaito, C.; Sekimizu, K.; !1Hirakawa, H.; Kuhara, S.; Goto, S.; Yabuzaki, J.; Kanehisa, !1M.; Yamashita, A.; Oshima, K.; Furuya, K.; Yoshino, C.; !1Shiba, T.; Hattori, M.; Ogasawara, N.; Hayashi, H.; !1Hiramatsu, K. !$#journal Lancet (2001) 357:1225-1240 !$#title Whole genome sequencing of meticillin-resistant !1Stapylococcus aureus. !$#cross-references MUID:21311952; PMID:11418146 !$#accession B89910 !'##molecule_type DNA !'##residues 1-373 ##label KUR !'##cross-references GB:BA000018; NID:g13701143; PIDN:BAB42438.1; !1GSPDB:GN00149 !'##experimental_source strain N315 GENETICS !$#gene SA1180 CLASSIFICATION #superfamily exonuclease sbcD; phosphoesterase core homology KEYWORDS exonuclease; hydrolase FEATURE !$2-86 #domain phosphoesterase core homology #label PEC SUMMARY #length 373 #molecular-weight 42967 #checksum 8389 SEQUENCE /// ENTRY B83110 #type complete TITLE probable exonuclease (EC 3.1.-.-) sbcD-type PA4281 [similarity] - Pseudomonas aeruginosa (strain PAO1) ORGANISM #formal_name Pseudomonas aeruginosa DATE 15-Sep-2000 #sequence_revision 15-Sep-2000 #text_change 24-Aug-2001 ACCESSIONS B83110 REFERENCE A82950 !$#authors Stover, C.K.; Pham, X.Q.; Erwin, A.L.; Mizoguchi, S.D.; !1Warrener, P.; Hickey, M.J.; Brinkman, F.S.L.; Hufnagle, !1W.O.; Kowalik, D.J.; Lagrou, M.; Garber, R.L.; Goltry, L.; !1Tolentino, E.; Westbrook-Wadman, S.; Yuan, Y.; Brody, L.L.; !1Coulter, S.N.; Folger, K.R.; Kas, A.; Larbig, K.; Lim, R.M.; !1Smith, K.A.; Spencer, D.H.; Wong, G.K.S.; Wu, Z.; Paulsen, !1I.T.; Reizer, J.; Saier, M.H.; Hancock, R.E.W.; Lory, S.; !1Olson, M.V. !$#journal Nature (2000) 406:959-964 !$#title Complete genome sequence of Pseudomonas aeruginosa PA01, an !1opportunistic pathogen. !$#cross-references MUID:20437337; PMID:10984043 !$#accession B83110 !'##molecule_type DNA !'##residues 1-409 ##label STO !'##cross-references GB:AE004844; GB:AE004091; NID:g9950500; !1PIDN:AAG07669.1; GSPDB:GN00131; PASP:PA4281 !'##experimental_source strain PAO1 GENETICS !$#gene sbcD; PA4281 CLASSIFICATION #superfamily exonuclease sbcD; phosphoesterase core homology KEYWORDS exonuclease; hydrolase FEATURE !$2-87 #domain phosphoesterase core homology #label PEC SUMMARY #length 409 #molecular-weight 45433 #checksum 7128 SEQUENCE /// ENTRY S76329 #type complete TITLE probable exonuclease (EC 3.1.-.-) sbcD-type s11021 [similarity] - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 25-Apr-1997 #sequence_revision 25-Apr-1997 #text_change 24-Aug-2001 ACCESSIONS S76329 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76329 !'##molecule_type DNA !'##residues 1-416 ##label KAN !'##cross-references EMBL:D64000; GB:AB001339; NID:g1001484; !1PIDN:BAA10181.1; PID:d1010832; PID:g1001554 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. CLASSIFICATION #superfamily exonuclease sbcD; phosphoesterase core homology KEYWORDS exonuclease; hydrolase FEATURE !$3-95 #domain phosphoesterase core homology #label PEC SUMMARY #length 416 #molecular-weight 45939 #checksum 4655 SEQUENCE /// ENTRY C39432 #type complete TITLE exonuclease (EC 3.1.-.-) sbcD - Bacillus subtilis ALTERNATE_NAMES hypothetical protein (AddB 3' region) ORGANISM #formal_name Bacillus subtilis DATE 21-Feb-1992 #sequence_revision 21-Feb-1992 #text_change 16-Jun-2000 ACCESSIONS C39432; H69703 REFERENCE A39432 !$#authors Kooistra, J.; Venema, G. !$#journal J. Bacteriol. (1991) 173:3644-3655 !$#title Cloning, sequencing, and expression of Bacillus subtilis !1genes involved in ATP-dependent nuclease synthesis. !$#cross-references MUID:91267926; PMID:1646786 !$#accession C39432 !'##molecule_type DNA !'##residues 1-253 ##label KOO !'##cross-references GB:M63489; NID:g142438; PIDN:AAA22202.1; !1PID:g142441 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69703 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-253 ##label KUN !'##cross-references GB:Z99109; GB:AL009126; NID:g2633260; !1PIDN:CAB12904.1; PID:g2633400 !'##experimental_source strain 168 GENETICS !$#gene sbcD CLASSIFICATION #superfamily Bacillus subtilis exonuclease sbcD; !1phosphoesterase core homology KEYWORDS exonuclease; hydrolase; metalloprotein FEATURE !$2-86 #domain phosphoesterase core homology #label PEC SUMMARY #length 253 #molecular-weight 28157 #checksum 6620 SEQUENCE /// ENTRY NCECX1 #type complete TITLE exodeoxyribonuclease I (EC 3.1.11.1) - Escherichia coli (strain K-12) ALTERNATE_NAMES exonuclease I ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS B64966; A26123 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64966 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-475 ##label BLAT !'##cross-references GB:AE000292; GB:U00096; NID:g1788310; !1PIDN:AAC75072.1; PID:g1788321; UWGP:b2011 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A26123 !$#authors Phillips, G.J.; Kushner, S.R. !$#journal J. Biol. Chem. (1987) 262:455-459 !$#title Determination of the nucleotide sequence for the exonuclease !1I structural gene (sbcB) of Escherichia coli K12. !$#cross-references MUID:87083489; PMID:3539937 !$#accession A26123 !'##molecule_type DNA !'##residues 1-209,219-224,'H',226-342,'E',344-474,'A' ##label PHI !'##cross-references GB:J02641; NID:g511668; PIDN:AAA19938.1; !1PID:g147788 !'##experimental_source K12 !'##note the authors translated the codon CAA for residue 342 as Glu and !1TTG for residue 440 as Phe GENETICS !$#gene sbcB; xonA; cpeA !$#map_position 44 min FUNCTION !$#description catalyzes the degradation of single-stranded DNA in a 3' to !15' direction releasing 5'-phosphomononucleotides !$#note the E. coli enzyme also catalyzes the hydrolysis of !1glucosylated DNA CLASSIFICATION #superfamily exodeoxyribonuclease I KEYWORDS DNA repair; exonuclease; hydrolase SUMMARY #length 475 #molecular-weight 54500 #checksum 7886 SEQUENCE /// ENTRY NCECX3 #type complete TITLE exodeoxyribonuclease III (EC 3.1.11.2) - Escherichia coli (strain K-12) ALTERNATE_NAMES E. coli exonuclease III ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS E64934; A31839; S03102 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64934 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-268 ##label BLAT !'##cross-references GB:AE000270; GB:U00096; NID:g1788045; !1PIDN:AAC74819.1; PID:g1788046; UWGP:b1749 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A31839 !$#authors Saporito, S.M.; Smith-White, B.J.; Cunningham, R.P. !$#journal J. Bacteriol. (1988) 170:4542-4547 !$#title Nucleotide sequence of the xth gene of Escherichia coli !1K-12. !$#cross-references MUID:89008066; PMID:3049539 !$#accession A31839 !'##molecule_type DNA !'##residues 1-48,'NV',51-268 ##label SAP !'##cross-references GB:M22592; NID:g148276; PIDN:AAA24767.1; !1PID:g148277 !'##experimental_source strain K12 REFERENCE S03102 !$#authors Wurst, H.; Hoheisel, J.D.; Pohl, F.M. !$#submission submitted to the EMBL Data Library, September 1988 !$#accession S03102 !'##molecule_type DNA !'##residues 1-87,'HG',90-268 ##label WUR !'##cross-references EMBL:X13002 COMMENT This enzyme is the major apurinic-apyrimidinic (AP) !1endonuclease of E. coli. GENETICS !$#gene xthA; xth !$#map_position 38 min FUNCTION !$#description removes the damaged DNA at cytosines and guanines by !1cleaving on the 3' side of the AP site by a beta-elimination !1reaction CLASSIFICATION #superfamily exodeoxyribonuclease III KEYWORDS DNA repair; hydrolase SUMMARY #length 268 #molecular-weight 30969 #checksum 5256 SEQUENCE /// ENTRY NCECX5 #type complete TITLE exodeoxyribonuclease V (EC 3.1.11.5) 135K chain - Escherichia coli (strain K-12) ALTERNATE_NAMES exonuclease 135K polypeptide; recBC DNase 135K polypeptide ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 01-Mar-2002 ACCESSIONS A25532; E65064 REFERENCE A25532 !$#authors Finch, P.W.; Storey, A.; Chapman, K.E.; Brown, K.; Hickson, !1I.D.; Emmerson, P.T. !$#journal Nucleic Acids Res. (1986) 14:8573-8582 !$#title Complete nucleotide sequence of the Escherichia coli recB !1gene. !$#cross-references MUID:87066729; PMID:3537960 !$#accession A25532 !'##molecule_type DNA !'##residues 1-1180 ##label FIN !'##cross-references GB:X04581; NID:g42680; PIDN:CAA28250.1; PID:g42682 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65064 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-1180 ##label BLAT !'##cross-references GB:AE000365; GB:U00096; NID:g2367163; !1PIDN:AAC75859.1; PID:g1789183; UWGP:b2820 !'##experimental_source strain K-12, substrain MG1655 COMMENT This enzyme is required for efficient DNA repair; it !1catalyzes the unwinding of double-stranded DNA and the !1cleavage of single-stranded DNA and it stimulates local !1genetic recombination. All of these activities require !1concomitant hydrolysis of ATP. GENETICS !$#gene recB !$#map_position 61 min CLASSIFICATION #superfamily exodeoxyribonuclease V 135K chain KEYWORDS ATP; DNA repair; hydrolase; nucleotide binding; P-loop FEATURE !$23-30 #region nucleotide-binding motif A (P-loop) SUMMARY #length 1180 #molecular-weight 133958 #checksum 1854 SEQUENCE /// ENTRY NCECXV #type complete TITLE exodeoxyribonuclease V (EC 3.1.11.5) 125K chain - Escherichia coli (strain K-12) ALTERNATE_NAMES E. coli exonuclease V 125K polypeptide; recBC DNase 125K polypeptide ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 01-Mar-2002 ACCESSIONS A24137; G65064 REFERENCE A93625 !$#authors Finch, P.W.; Wilson, R.E.; Brown, K.; Hickson, I.D.; !1Tomkinson, A.E.; Emmerson, P.T. !$#journal Nucleic Acids Res. (1986) 14:4437-4451 !$#title Complete nucleotide sequence of the Escherichia coli recC !1gene and of the thyA-recC intergenic region. !$#cross-references MUID:86232583; PMID:3520484 !$#accession A24137 !'##molecule_type DNA !'##residues 1-1122 ##label FIN !'##cross-references GB:X03966; NID:g42684; PIDN:CAA27604.1; PID:g42689 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65064 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-1122 ##label BLAT !'##cross-references GB:AE000366; GB:U00096; NID:g1789185; !1PIDN:AAC75861.1; PID:g1789186; UWGP:b2822 !'##experimental_source strain K-12, substrain MG1655 COMMENT This is one of the polypeptide chains of exonuclease V, !1which can catalyze a wide range of reactions; its activity !1includes that of the DNA dependent ATPase and several other !1ATP-dependent activities such as exonuclease, endonuclease, !1and helicase. Mutation of this gene leads to reduction of !1genetic recombination and increased sensitivity to UV !1radiation. GENETICS !$#gene recC !$#map_position 61 min CLASSIFICATION #superfamily exodeoxyribonuclease V 125K chain KEYWORDS ATP; DNA repair; hydrolase SUMMARY #length 1122 #molecular-weight 128846 #checksum 9249 SEQUENCE /// ENTRY NCECXF #type complete TITLE exodeoxyribonuclease V (EC 3.1.11.5) 67K chain - Escherichia coli (strain K-12) ALTERNATE_NAMES exonuclease V alpha chain; recBC DNase alpha chain ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS D65064; A25533; C25532 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65064 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-608 ##label BLAT !'##cross-references GB:AE000365; GB:U00096; NID:g2367163; !1PIDN:AAC75858.1; PID:g1789182; UWGP:b2819 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A25533 !$#authors Finch, P.W.; Storey, A.; Brown, K.; Hickson, I.D.; Emmerson, !1P.T. !$#journal Nucleic Acids Res. (1986) 14:8583-8594 !$#title Complete nucleotide sequence of recD, the structural gene !1for the alpha-subunit of exonuclease V of Escherichia coli. !$#cross-references MUID:87066730; PMID:3537961 !$#accession A25533 !'##molecule_type DNA !'##residues 1-246,'HR',249-305,'V',307-389,'L',391-608 ##label FIN !'##cross-references GB:X04582; NID:g42690; PIDN:CAA28253.1; PID:g42691 REFERENCE A25532 !$#authors Finch, P.W.; Storey, A.; Chapman, K.E.; Brown, K.; Hickson, !1I.D.; Emmerson, P.T. !$#journal Nucleic Acids Res. (1986) 14:8573-8582 !$#title Complete nucleotide sequence of the Escherichia coli recB !1gene. !$#cross-references MUID:87066729; PMID:3537960 !$#accession C25532 !'##molecule_type DNA !'##residues 1-31 ##label FI2 !'##cross-references GB:X04581 GENETICS !$#gene recD !$#map_position 61 min FUNCTION !$#description one of the components of E. coli exonuclease V, which is !1required for efficient DNA repair; catalyzes the unwinding !1of double-stranded DNA and the cleavage of single-stranded !1DNA and it stimulates local genetic recombination; all of !1these activities require concomitant hydrolysis of ATP CLASSIFICATION #superfamily exodeoxyribonuclease V 67K chain KEYWORDS ATP; DNA repair; hydrolase; nucleotide binding; P-loop FEATURE !$171-178 #region nucleotide-binding motif A (P-loop) SUMMARY #length 608 #molecular-weight 66902 #checksum 5073 SEQUENCE /// ENTRY NCEC7 #type complete TITLE exodeoxyribonuclease VII (EC 3.1.11.6) large chain - Escherichia coli (strain K-12) ALTERNATE_NAMES exonuclease VII large chain ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 12-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS D65027; A25940 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65027 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-456 ##label BLAT !'##cross-references GB:AE000337; GB:U00096; NID:g1788850; !1PIDN:AAC75562.1; PID:g1788856; UWGP:b2509 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A25940 !$#authors Chase, J.W.; Rabin, B.A.; Murphy, J.B.; Stone, K.L.; !1Williams, K.R. !$#journal J. Biol. Chem. (1986) 261:14929-14935 !$#title Escherichia coli exonuclease VII: cloning and sequencing of !1the gene encoding the large subunit (xseA). !$#cross-references MUID:87033720; PMID:3021756 !$#accession A25940 !'##molecule_type DNA !'##residues 1-66,'S',68-456 ##label CHA !'##cross-references GB:J02599; NID:g148273; PIDN:AAA24766.1; !1PID:g148275 !'##note part of the sequence was confirmed by protein sequencing GENETICS !$#gene xseA !$#map_position 54 min CLASSIFICATION #superfamily exodeoxyribonuclease VII KEYWORDS hydrolase; single-stranded DNA degradation SUMMARY #length 456 #molecular-weight 51832 #checksum 6618 SEQUENCE /// ENTRY NCECX8 #type complete TITLE exodeoxyribonuclease VIII (EC 3.1.11.-) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 30-Sep-1997 #text_change 01-Mar-2002 ACCESSIONS A64885; PS0030; S38952; I55007; T09175 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64885 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-866 ##label BLAT !'##cross-references GB:AE000232; GB:U00096; NID:g1787600; !1PIDN:AAC74432.1; PID:g1787612; UWGP:b1350 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A91895 !$#authors Chu, C.C.; Templin, A.; Clark, A.J. !$#journal J. Bacteriol. (1989) 171:2101-2109 !$#title Suppression of a frameshift mutation in the recE gene of !1Escherichia coli K-12 occurs by gene fusion. !$#cross-references MUID:89197781; PMID:2649487 !$#accession PS0030 !'##molecule_type DNA !'##residues 1-365,'G',367-661 ##label CHU !'##cross-references GB:M24905; NID:g147534; PIDN:AAA03212.1; !1PID:g147536 !'##experimental_source strain K12 REFERENCE S38951 !$#authors Mahajan, S.K.; Chu, C.C.; Willis, D.K.; Templin, A.; Clark, !1A.J. !$#journal Genetics (1990) 125:261-273 !$#title Physical analysis of spontaneous and mutagen-induced mutants !1of Escherichia coli K-12 expressing DNA exonuclease VIII !1activity. !$#cross-references MUID:90337272; PMID:2199308 !$#accession S38952 !'##molecule_type DNA !'##residues 295-346 ##label MAH REFERENCE I55007 !$#authors Clark, A.J.; Sharma, V.; Brenowitz, S.; Chu, C.C.; Sandler, !1S.J.; Satin, L.; Templin, A.; Berger, I.; Cohen, A. !$#journal J. Bacteriol. (1993) 175:7673-7682 !$#title Genetic and molecular analysis of the C-Terminal region of !1the recE gene from the Rac prophage of E. coli K-12. !$#cross-references MUID:94064562; PMID:8244937 !$#accession I55007 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 660-690,'TA',693-866 ##label RES !'##cross-references GB:L23927; NID:g397679; PIDN:AAA16178.1; !1PID:g397680 REFERENCE Z16603 !$#authors Aiba, H.; Baba, T.; Fujita, K.; Hayashi, K.; Inada, T.; !1Isono, K.; Itoh, T.; Kasai, H.; Kashimoto, K.; Kimura, S.; !1Kitakawa, M.; Kitagawa, M.; Makino, K.; Miki, T.; Mizobuchi, !1K.; Mori, H.; Mori, T.; Motomura, K.; Nakade, S.; Nakamura, !1Y.; Nashimoto, H.; Nishio, Y.; Oshima, T.; Saito, N.; !1Sampei, G.; Seki, Y.; Sivasundaram, S.; Tagami, H.; Takeda, !1J.; Takemoto, K.; Takeuchi, Y.; Wada, C.; Yamamoto, Y.; !1Horiuchi, T. !$#journal DNA Res. (1996) 3:363-377 !$#title A 570-kb DNA sequence of the Escherichia coli K-12 genome !1corresponding to the 28.0-40.1 min region on the linkage !1map. !$#cross-references MUID:97251357; PMID:9097039 !$#accession T09175 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-866 ##label AIB !'##cross-references EMBL:D90774; NID:g1742217; PIDN:BAA14952.1; !1PID:g1742219 GENETICS !$#gene recE !$#map_position 30 min FUNCTION !$#description ATP-independent exonuclease; catalyzes the cleavage of !1double-stranded DNA; involved in recombination CLASSIFICATION #superfamily exodeoxyribonuclease VIII KEYWORDS exonuclease; hydrolase FEATURE !$2-866 #product exodeoxyribonuclease VIII #status predicted !8#label MAT SUMMARY #length 866 #molecular-weight 96367 #checksum 4597 SEQUENCE /// ENTRY NDBPT7 #type complete TITLE exodeoxyribonuclease (EC 3.1.11.-) - phage T7 ORGANISM #formal_name phage T7 DATE 13-Jun-1983 #sequence_revision 26-Jul-1996 #text_change 11-Jun-1999 ACCESSIONS S42316; A00780; S43608 REFERENCE S42315 !$#authors Dunn, J.J. !$#submission submitted to the EMBL Data Library, October 1993 !$#accession S42316 !'##molecule_type DNA !'##residues 1-300 ##label DUN !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24418.1; !1PID:g431192 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession A00780 !'##molecule_type DNA !'##residues 'MSRDLVTIPRDVWNDIQGYIDSLERENDSLKNQLMEADEYVAELEEKLNGT',4-300 !1##label DUF !'##note due to a frameshift error genes 5.9 and 6 were concatenated !1into a single reading frame REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S43608 !'##molecule_type DNA !'##residues 'MSRDLVTIPRDVWNDIQGYIDSLERENDSLKNQLMEADEYVAELEEKLNGT',4-300 !1##label DUW !'##cross-references EMBL:V01146 !'##note due to a frameshift error genes 5.9 and 6 were concatenated !1into a single reading frame !'##note the authors did not translate the codon for residue 1 GENETICS !$#gene 6 !$#map_position 43.74-46.08 FUNCTION !$#description 5' to 3' exonuclease specific for double-stranded DNA; !1probably removes DNA-linked RNA primers !$#note essential for phage DNA replication; required for host DNA !1degradation and phage genetic recombination CLASSIFICATION #superfamily phage T7 exodeoxyribonuclease KEYWORDS exonuclease; hydrolase SUMMARY #length 300 #molecular-weight 34502 #checksum 7095 SEQUENCE /// ENTRY S07503 #type complete TITLE exodeoxyribonuclease (EC 3.1.11.-) - phage T3 ORGANISM #formal_name phage T3 DATE 30-Sep-1991 #sequence_revision 26-Jul-1996 #text_change 11-Jun-1999 ACCESSIONS S07503 REFERENCE S07500 !$#authors Beck, P.J.; Gonzalez, S.; Ward, C.L.; Molineux, I.J. !$#journal J. Mol. Biol. (1989) 210:687-701 !$#title Sequence of bacteriophage T3 DNA from gene 2.5 through gene !19. !$#cross-references MUID:90133923; PMID:2614843 !$#accession S07503 !'##molecule_type DNA !'##residues 1-302 ##label BEC !'##cross-references EMBL:X17255; NID:g15682; PIDN:CAA35147.1; !1PID:g15709 GENETICS !$#gene 6 FUNCTION !$#description 5' to 3' exonuclease specific for double-stranded DNA; !1probably removes DNA-linked RNA primers !$#note essential for phage DNA replication; required for host DNA !1degradation and phage genetic recombination CLASSIFICATION #superfamily phage T7 exodeoxyribonuclease KEYWORDS exonuclease; hydrolase SUMMARY #length 302 #molecular-weight 34627 #checksum 1113 SEQUENCE /// ENTRY NDBE61 #type complete TITLE exonuclease (EC 3.1.11.-) - human herpesvirus 1 (strain 17) ALTERNATE_NAMES gene UL12 protein (deoxyribonuclease) ORGANISM #formal_name human herpesvirus 1 #note host Homo sapiens (man) DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 16-Jun-2000 ACCESSIONS A00781; C30083 REFERENCE A93620 !$#authors McGeoch, D.J.; Dolan, A.; Frame, M.C. !$#journal Nucleic Acids Res. (1986) 14:3435-3448 !$#title DNA sequence of the region in the genome of herpes simplex !1virus type 1 containing the exonuclease gene and !1neighbouring genes. !$#cross-references MUID:86205244; PMID:3010237 !$#accession A00781 !'##molecule_type DNA !'##residues 1-626 ##label MCG !'##cross-references GB:X03839; NID:g59841; PIDN:CAA27453.1; PID:g59844 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession C30083 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-626 ##label MC2 !'##cross-references GB:X14112; NID:g1944536; PIDN:CAA32325.1; !1PID:g59513; GB:D00317 GENETICS !$#gene UL12 !$#map_position 0.16-0.20 CLASSIFICATION #superfamily herpesvirus exonuclease KEYWORDS exonuclease; hydrolase SUMMARY #length 626 #molecular-weight 67507 #checksum 8052 SEQUENCE /// ENTRY NDBE48 #type complete TITLE exonuclease (EC 3.1.11.-) - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 11-Jun-1999 ACCESSIONS D27344 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession D27344 !'##molecule_type DNA !'##residues 1-551 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27931.1; !1PID:g60037 GENETICS !$#gene 48 CLASSIFICATION #superfamily herpesvirus exonuclease KEYWORDS exonuclease; hydrolase SUMMARY #length 551 #molecular-weight 61270 #checksum 7851 SEQUENCE /// ENTRY NDBEE3 #type complete TITLE exonuclease (EC 3.1.11.-) - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 11-Jun-1999 ACCESSIONS E36800 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession E36800 !'##molecule_type DNA !'##residues 1-508 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02485.1; !1PID:g330841 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 50 CLASSIFICATION #superfamily herpesvirus exonuclease KEYWORDS hydrolase SUMMARY #length 508 #molecular-weight 56067 #checksum 2484 SEQUENCE /// ENTRY QQBE37 #type complete TITLE alkaline exonuclease (EC 3.1.11.-) - human herpesvirus 4 (strain B95-8) ALTERNATE_NAMES BGLF5 protein ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 23-Mar-2001 ACCESSIONS A03779; B93065; S33032 REFERENCE A38059 !$#authors Farrell, P.J.; Barrell, B.G. !$#submission submitted to the EMBL Data Library, June 1984 !$#description DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#accession A03779 !'##molecule_type DNA !'##residues 1-470 ##label FAR !'##cross-references EMBL:V01555; NID:g59074; PIDN:CAA24827.1; !1PID:g1334891 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession B93065 !'##molecule_type DNA !'##residues 1-470 ##label BAN !'##cross-references EMBL:V01555; NID:g59074; PIDN:CAA24827.1; !1PID:g1334891 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region CLASSIFICATION #superfamily human cytomegalovirus alkaline exonuclease KEYWORDS exonuclease; hydrolase SUMMARY #length 470 #molecular-weight 52666 #checksum 2145 SEQUENCE /// ENTRY QQBEJ6 #type complete TITLE alkaline exonuclease (EC 3.1.11.-) - human cytomegalovirus (strain AD169) ALTERNATE_NAMES UL98 protein ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 #note host Homo sapiens (man) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 11-Jun-1999 ACCESSIONS S09863 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09863 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-584 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35334.1; !1PID:g1780877 !'##note possible protein-coding frames are given !'##note the DNA sequence was submitted to EMBL, December 1989, in !1computer-readable form CLASSIFICATION #superfamily human cytomegalovirus alkaline exonuclease KEYWORDS exonuclease; hydrolase SUMMARY #length 584 #molecular-weight 65271 #checksum 7907 SEQUENCE /// ENTRY QQBEHS #type complete TITLE alkaline exonuclease (EC 3.1.11.-) - human herpesvirus 6 (strain Uganda-1102) ORGANISM #formal_name human herpesvirus 6 DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 11-Jun-1999 ACCESSIONS F36769 REFERENCE A33560 !$#authors Lawrence, G.L.; Chee, M.; Craxton, M.A.; Gompels, U.A.; !1Honess, R.W.; Barrell, B.G. !$#journal J. Virol. (1990) 64:287-299 !$#title Human herpesvirus 6 is closely related to human !1cytomegalovirus. !$#cross-references MUID:90080132; PMID:2152817 !$#accession F36769 !'##molecule_type DNA !'##residues 1-488 ##label LAW !'##cross-references GB:M68963; GB:M28243; NID:g325494; PIDN:AAA65578.1; !1PID:g325510 CLASSIFICATION #superfamily human cytomegalovirus alkaline exonuclease KEYWORDS exonuclease; hydrolase SUMMARY #length 488 #molecular-weight 56644 #checksum 9017 SEQUENCE /// ENTRY QQBEN4 #type complete TITLE alkaline exonuclease (EC 3.1.11.-) - saimiriine herpesvirus 1 (strain 11) ORGANISM #formal_name saimiriine herpesvirus 1 #note host Saimiri sciureus (common squirrel monkey) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 11-Jun-1999 ACCESSIONS H36809 REFERENCE A36806 !$#authors Albrecht, J. !$#submission submitted to the EMBL Data Library, January 1992 !$#description Primary structure of the herpesvirus saimiri genome. !$#accession H36809 !'##molecule_type DNA !'##residues 1-483 ##label ALB !'##cross-references GB:X64346; NID:g60320; PIDN:CAA45660.1; PID:g60358 REFERENCE A37309 !$#authors Albrecht, J.C.; Nicholas, J.; Biller, D.; Cameron, K.R.; !1Biesinger, B.; Newman, C.; Wittmann, S.; Craxton, M.A.; !1Coleman, H.; Fleckenstein, B.; Honess, R.W. !$#journal J. Virol. (1992) 66:5047-5058 !$#title Primary structure of the herpesvirus saimiri genome. !$#cross-references MUID:92333688; PMID:1321287 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 37 CLASSIFICATION #superfamily human cytomegalovirus alkaline exonuclease KEYWORDS exonuclease; hydrolase SUMMARY #length 483 #molecular-weight 55554 #checksum 6775 SEQUENCE /// ENTRY S55632 #type complete TITLE deoxyribonuclease 37 - equine herpesvirus 2 ORGANISM #formal_name equine herpesvirus 2 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S55632 REFERENCE S55594 !$#authors Telford, E.A.R.; Watson, M.S.; Aird, H.C.; Perry, J.; !1Davison, A.J. !$#journal J. Mol. Biol. (1995) 249:520-528 !$#title The DNA sequence of equine herpesvirus 2. !$#cross-references MUID:95302501; PMID:7783207 !$#accession S55632 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-509 ##label TEL !'##cross-references GB:U20824; NID:g695172; PIDN:AAC13825.1; !1PID:g695210 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1February 1995 CLASSIFICATION #superfamily human cytomegalovirus alkaline exonuclease SUMMARY #length 509 #molecular-weight 57577 #checksum 9848 SEQUENCE /// ENTRY NRECD #type complete TITLE ribonuclease III (EC 3.1.26.3) rnd - Escherichia coli (strain K-12) ALTERNATE_NAMES ribonuclease D ORGANISM #formal_name Escherichia coli DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 01-Mar-2002 ACCESSIONS S01223; A30431; S41590; D64941; S42849; D21915 REFERENCE S01223 !$#authors Zhang, J.; Deutscher, M.P. !$#journal Nucleic Acids Res. (1988) 16:6265-6278 !$#title Escherichia coli RNase D: sequencing of the rnd structural !1gene and purification of the overexpressed protein. !$#cross-references MUID:88289400; PMID:3041371 !$#accession S01223 !'##molecule_type DNA !'##residues 1-375 ##label ZHA !'##cross-references EMBL:X07055; NID:g42770; PIDN:CAA30098.1; !1PID:g581215 !$#accession A30431 !'##molecule_type protein !'##residues 1-6 ##label ZH2 REFERENCE S41588 !$#authors Fulda, M.; Heinz, E.; Wolter, F.P. !$#journal Mol. Gen. Genet. (1994) 242:241-249 !$#title The fadD gene of Escherichia coli K12 is located close to !1rnd at 39.6 min of the chromosomal map and is a new member !1of the AMP-binding protein family. !$#cross-references MUID:94150456; PMID:8107670 !$#accession S41590 !'##molecule_type DNA !'##residues 1-38 ##label FUL !'##cross-references GB:X70994; NID:g433478; PIDN:CAA50322.1; !1PID:g581071 !'##experimental_source strain K12 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64941 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-375 ##label BLAT !'##cross-references GB:AE000274; GB:U00096; NID:g1788089; !1PIDN:AAC74874.1; PID:g1788105; UWGP:b1804 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S42848 !$#authors Fulda, M. !$#submission submitted to the EMBL Data Library, February 1993 !$#accession S42849 !'##status preliminary !'##molecule_type DNA !'##residues 'L',2-38 ##label FU2 !'##cross-references EMBL:X70994 GENETICS !$#gene rnd !$#map_position 40 min !$#start_codon TTG CLASSIFICATION #superfamily ribonuclease D KEYWORDS exonuclease; hydrolase FEATURE !$1-375 #product ribonuclease D #status experimental #label !8MAT SUMMARY #length 375 #molecular-weight 42734 #checksum 5288 SEQUENCE /// ENTRY NDHU1 #type complete TITLE deoxyribonuclease I (EC 3.1.21.1) precursor [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 08-Dec-2000 ACCESSIONS A38417; PL0036; PS0144 REFERENCE A38417 !$#authors Shak, S.; Capon, D.J.; Hellmiss, R.; Marsters, S.A.; Baker, !1C.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:9188-9192 !$#title Recombinant human DNase I reduces the viscosity of cystic !1fibrosis sputum. !$#cross-references MUID:91067672; PMID:2251263 !$#accession A38417 !'##molecule_type mRNA !'##residues 1-282 ##label SHA !'##cross-references GB:M55983; NID:g181623; PIDN:AAA63170.1; !1PID:g181624 REFERENCE PL0036 !$#authors Rosenstreich, D.L.; Tu, J.H.; Kinkade, P.R.; Maurer-Fogy, !1I.; Kahn, J.; Barton, R.W.; Farina, P.R. !$#journal J. Exp. Med. (1988) 168:1767-1779 !$#title A human urine-derived interleukin 1 inhibitor. Homology with !1deoxyribonuclease I. !$#cross-references MUID:89035996; PMID:3263467 !$#accession PL0036 !'##molecule_type protein !'##residues 23-25,'X',27-30,'X',32-39,'X',41-43,'X',45,73-95 ##label !1ROS REFERENCE PS0144 !$#authors Yasuda, T.; Awazu, S.; Sato, W.; Iida, R.; Tanaka, Y.; !1Kishi, K. !$#journal J. Biochem. (1990) 108:393-398 !$#title Human genetically polymorphic deoxyribonuclease: !1purification, characterization, and multiplicity of urine !1deoxyribonuclease I. !$#cross-references MUID:91115785; PMID:2277032 !$#accession PS0144 !'##molecule_type protein !'##residues 23-39,'X',41-49 ##label YAS GENETICS !$#gene GDB:DNASE1; DNL1 !'##cross-references GDB:132846; OMIM:125505 !$#map_position 16p13.3-16p13.3 CLASSIFICATION #superfamily deoxyribonuclease I KEYWORDS glycoprotein; hydrolase FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-282 #product deoxyribonuclease I #status experimental !8#label MAT\ !$40,128 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$156 #active_site His #status predicted SUMMARY #length 282 #molecular-weight 31433 #checksum 940 SEQUENCE /// ENTRY NDBOA #type complete TITLE deoxyribonuclease I (EC 3.1.21.1) precursor - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 24-Apr-1984 #sequence_revision 05-Dec-1998 #text_change 16-Jun-2000 ACCESSIONS JC6532; A92123; A92124; A92148; A26325; A00782; S19525 REFERENCE JC6532 !$#authors Chen, C.Y.; Lu, S.C.; Liao, T.H. !$#journal Gene (1998) 206:181-184 !$#title Cloning, sequencing and expression of a cDNA encoding bovine !1pancreatic deoxyribonuclease I in Escherichia coli: !1Purification and characterization of the recombinant enzyme. !$#cross-references MUID:98137790; PMID:9469931 !$#accession JC6532 !'##molecule_type mRNA !'##residues 1-282 ##label CHE !'##cross-references GB:AJ001538; NID:g2546887; PIDN:CAA04819.1; !1PID:g2546888 REFERENCE A92123 !$#authors Liao, T.H.; Salnikow, J.; Moore, S.; Stein, W.H. !$#journal J. Biol. Chem. (1973) 248:1489-1495 !$#title Bovine pancreatic deoxyribonuclease A. Isolation of cyanogen !1bromide peptides: complete covalent structure of the !1polypeptide chain. !$#cross-references MUID:73097126; PMID:4734471 !$#accession A92123 !'##molecule_type protein !'##residues 23-49,53-59,'EQ',62-248,'GP',251-282 ##label LI1 !'##experimental_source deoxyribonuclease A !'##note this sequence revised in reference A38938 !'##note disulfide bonds link residues 123-126 and 195-231; the former !1bond can be reduced without loss of enzymatic activity REFERENCE A38938 !$#authors Liao, T.H.; Salnikow, J.; Moore, S.; Stein, W.H. !$#journal J. Biol. Chem. (1992) 267:7957 !$#cross-references MUID:92218466; PMID:1348510 !$#contents annotation; revisions REFERENCE A92124 !$#authors Salnikow, J.; Murphy, D. !$#journal J. Biol. Chem. (1973) 248:1499-1501 !$#title Bovine pancreatic deoxyribonucleases A and C. A proline for !1histidine substitution in deoxyribonuclease C. !$#cross-references MUID:73149229; PMID:4735137 !$#accession A92124 !'##molecule_type protein !'##residues 23-49,53-59,'EQ',62-142,'P',144-248,'GP',251-282 ##label !1SAL !'##experimental_source deoxyribonuclease C REFERENCE A92148 !$#authors Liao, T.H. !$#journal J. Biol. Chem. (1974) 249:2354-2356 !$#title Bovine pancreatic deoxyribonuclese D. !$#cross-references MUID:74143471; PMID:4856650 !$#accession A92148 !'##molecule_type protein !'##residues 23-49,53-59,'EQ',62-142,'P',144-248,'GP',251-282 ##label !1LI2 !'##experimental_source deoxyribonuclease D !'##note the C and D forms differ from the A and B forms in having !1143-Pro; the only differences between the A and B forms and !1between the C and D forms are in the compositions of the !1carbohydrate moieties bound to Asn-40 REFERENCE A26325 !$#authors Paudel, H.K.; Liao, T.H. !$#journal J. Biol. Chem. (1986) 261:16012-16017 !$#title Comparison of the three primary structures of !1deoxyribonuclease isolated from bovine, ovine, and porcine !1pancreas. Derivation of the amino acid sequence of ovine !1DNase and revision of the previously published amino acid !1sequence of bovine DNase. !$#cross-references MUID:87057261; PMID:3782105 !$#accession A26325 !'##molecule_type protein !'##residues 39,'X',41-58 ##label PAU REFERENCE A92054 !$#authors Price, P.A.; Moore, S.; Stein, W.H. !$#journal J. Biol. Chem. (1969) 244:924-928 !$#title Alkylation of a histidine residue at the active site of !1bovine pancreatic deoxyribonuclease. !$#cross-references MUID:69184134; PMID:4976790 !$#contents annotation !$#note in the presence of divalent cations, His-156 is alkylated by !1iodoacetate with concomitant loss of enzymatic activity REFERENCE A92094 !$#authors Hugli, T.E.; Stein, W.H. !$#journal J. Biol. Chem. (1971) 246:7191-7200 !$#title Involvement of a tyrosine residue in the activity of bovine !1pancreatic deoxyribonuclease A. !$#cross-references MUID:72064723; PMID:5166750 !$#contents annotation !$#note nitration of Tyr-87 by tetranitromethane destroys a calcium !1binding site and inactivates the enzyme REFERENCE S19525 !$#authors Lahm, A.; Suck, D. !$#journal J. Mol. Biol. (1991) 221:645-667 !$#title DNase I-induced DNA conformation. 2 A structure of a DNase !1I-octamer complex. !$#contents annotation; X-ray crystallography, 2.0 angstroms FUNCTION !$#description catalyzes the hydrolysis of DNA to 5'-phosphodinucleotides !1and 5'-phosphooligonucleotides CLASSIFICATION #superfamily deoxyribonuclease I KEYWORDS glycoprotein; hydrolase; nucleic acid degradation FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-282 #product deoxyribonuclease I #status experimental !8#label MAT\ !$40 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$123-126,195-231 #disulfide_bonds #status experimental SUMMARY #length 282 #molecular-weight 31345 #checksum 5874 SEQUENCE /// ENTRY B26325 #type complete TITLE deoxyribonuclease I (EC 3.1.21.1) - sheep ORGANISM #formal_name Ovis orientalis aries, Ovis ammon aries #common_name domestic sheep DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B26325 REFERENCE A26325 !$#authors Paudel, H.K.; Liao, T.H. !$#journal J. Biol. Chem. (1986) 261:16012-16017 !$#title Comparison of the three primary structures of !1deoxyribonuclease isolated from bovine, ovine, and porcine !1pancreas. Derivation of the amino acid sequence of ovine !1DNase and revision of the previously published amino acid !1sequence of bovine DNase. !$#cross-references MUID:87057261; PMID:3782105 !$#accession B26325 !'##molecule_type protein !'##residues 1-260 ##label PAU CLASSIFICATION #superfamily deoxyribonuclease I KEYWORDS hydrolase SUMMARY #length 260 #molecular-weight 28939 #checksum 8619 SEQUENCE /// ENTRY A26324 #type complete TITLE deoxyribonuclease I (EC 3.1.21.1) - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A26324 REFERENCE A26324 !$#authors Paudel, H.K.; Liao, T.H. !$#journal J. Biol. Chem. (1986) 261:16006-16011 !$#title Purification, characterization, and the complete amino acid !1sequence of porcine pancreatic deoxyribonuclease. !$#cross-references MUID:87057260; PMID:3782104 !$#accession A26324 !'##molecule_type protein !'##residues 1-262 ##label PAU CLASSIFICATION #superfamily deoxyribonuclease I KEYWORDS hydrolase SUMMARY #length 262 #molecular-weight 29447 #checksum 2437 SEQUENCE /// ENTRY JC2526 #type complete TITLE deoxyribonuclease I (EC 3.1.21.1) - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JC2526 REFERENCE JC2526 !$#authors Peitsch, M.C.; Irmler, M.; French, L.E.; Tschopp, J. !$#journal Biochem. Biophys. Res. Commun. (1995) 207:62-68 !$#title Genomic organisation and expression of mouse !1deoxyribonuclease I. !$#cross-references MUID:95160718; PMID:7857306 !$#accession JC2526 !'##molecule_type mRNA !'##residues 1-284 ##label PEI !'##cross-references EMBL:U00478; NID:g437052; PIDN:AAA03710.1; !1PID:g437053 CLASSIFICATION #superfamily deoxyribonuclease I KEYWORDS actin binding; calcium binding; hydrolase SUMMARY #length 284 #molecular-weight 32154 #checksum 3375 SEQUENCE /// ENTRY S13676 #type complete TITLE deoxyribonuclease I (EC 3.1.21.1) - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S13676 REFERENCE S13676 !$#authors Polzar, B.; Mannherz, H.G. !$#journal Nucleic Acids Res. (1990) 18:7151 !$#title Nucleotide sequence of a full length cDNA clone encoding the !1deoxyribonuclease I from the rat parotid gland. !$#cross-references MUID:91088312; PMID:2263485 !$#accession S13676 !'##molecule_type mRNA !'##residues 1-284 ##label POL !'##cross-references EMBL:X56060 CLASSIFICATION #superfamily deoxyribonuclease I KEYWORDS hydrolase SUMMARY #length 284 #molecular-weight 32064 #checksum 4033 SEQUENCE /// ENTRY NDEC4 #type complete TITLE deoxyribonuclease IV (phage-T4-induced) (EC 3.1.21.2) - Escherichia coli (strain K-12) ALTERNATE_NAMES endodeoxyribonuclease IV; Escherichia coli endonuclease IV ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS F64984; A30194 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64984 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-285 ##label BLAT !'##cross-references GB:AE000305; GB:U00096; NID:g1788479; !1PIDN:AAC75220.1; PID:g1788483; UWGP:b2159 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A30194 !$#authors Saporito, S.M.; Cunningham, R.P. !$#journal J. Bacteriol. (1988) 170:5141-5145 !$#title Nucleotide sequence of the nfo gene of Escherichia coli !1K-12. !$#cross-references MUID:89033896; PMID:2460435 !$#accession A30194 !'##molecule_type DNA !'##residues 1-9,'R',11-285 ##label SAP !'##cross-references GB:M22591; NID:g146953; PIDN:AAA24216.1; !1PID:g146954 !'##experimental_source strain K12 COMMENT This enzyme cleaves phosphodiester bonds at apurinic or !1apyrimidinic sites (AP sites) to produce new 5' ends that !1are base-free deoxyribose 5-phosphate residues. It !1preferentially attacks modified AP sites created by !1bleomycin and neocarzinostatin. GENETICS !$#gene nfo CLASSIFICATION #superfamily deoxyribonuclease IV (phage T4-induced) KEYWORDS endonuclease; hydrolase SUMMARY #length 285 #molecular-weight 31479 #checksum 5167 SEQUENCE /// ENTRY JC5235 #type complete TITLE DNA-(apurinic or apyrimidinic site) lyase (EC 4.2.99.18) - Caenorhabditis elegans ALTERNATE_NAMES apurinic/apyrinidinic endonuclease ORGANISM #formal_name Caenorhabditis elegans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 29-Oct-1999 ACCESSIONS JC5235; T24553 REFERENCE JC5235 !$#authors Masson, J.Y.; Tremblay, S.; Ramotar, D. !$#journal Gene (1996) 179:291-293 !$#title The Caenorhabditis elegans gene CeAPN1 encodes a homolog of !1Escherichia coli and yeast apurinic/apyrimidinic !1endonuclease. !$#cross-references MUID:97128321; PMID:8972914 !$#accession JC5235 !'##status preliminary !'##molecule_type mRNA !'##residues 1-278 ##label MAS !'##cross-references GB:U40707; NID:g1289372; PIDN:AAB39924.1; !1PID:g1335852 REFERENCE Z19907 !$#authors Thomas, K. !$#submission submitted to the EMBL Data Library, January 1995 !$#accession T24553 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-278 ##label WIL !'##cross-references EMBL:Z47812; PIDN:CAA87789.1; GSPDB:GN00020; !1CESP:T05H10.2 !'##experimental_source clone T05H10 COMMENT This enzyme is involved in the repair of damaged DNA, and !1preventing genetic in stability. GENETICS !$#gene CeAPN1 !$#map_position 2 !$#introns 141/1 CLASSIFICATION #superfamily deoxyribonuclease IV (phage T4-induced) KEYWORDS carbon-oxygen lyase SUMMARY #length 278 #molecular-weight 31397 #checksum 9794 SEQUENCE /// ENTRY S29871 #type complete TITLE DNA-(apurinic or apyrimidinic site) lyase (EC 4.2.99.18) [validated] - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES apurinic/apyrimidinic endonuclease / 3'-repair diesterase; deoxyribonuclease (apurinic or apyrimidinic); protein YKL114c; protein YKL513 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 26-May-2000 ACCESSIONS S29871; S37942; S29364; A35790 REFERENCE S22267 !$#authors Jacquier, A.; Legrain, P.; Dujon, B. !$#journal Yeast (1992) 8:121-132 !$#title Sequence of a 10.7 kb segment of yeast chromosome XI !1identifies the APN1 and the BAF1 loci and reveals one tRNA !1gene and several new open reading frames including homologs !1to RAD2 and kinases. !$#cross-references MUID:92221689; PMID:1561835 !$#accession S29871 !'##molecule_type DNA !'##residues 1-367 ##label JAC !'##cross-references GB:S93804; NID:g248391; PIDN:AAB22003.1; !1PID:g1680184 !'##experimental_source strain S288C REFERENCE S37938 !$#authors Jacquier, A.; Legrain, P.; Colleaux, L.; Richard, G.F.; !1Thierry, A.; Dujon, B. !$#submission submitted to the Protein Sequence Database, March 1994 !$#accession S37942 !'##molecule_type DNA !'##residues 1-367 ##label JA2 !'##cross-references EMBL:Z28114; NID:g486191; PIDN:CAA81954.1; !1PID:g486192; GSPDB:GN00011; MIPS:YKL114c !'##experimental_source strain S288C REFERENCE S29364 !$#authors Johnson, A.W.; Demple, B. !$#journal J. Biol. Chem. (1988) 263:18009-18016 !$#title Yeast DNA diesterase for 3'-fragments of deoxyribose: !1purification and physical properties of a repair enzyme for !1oxidative DNA damage. !$#cross-references MUID:89053965; PMID:3056935 !$#accession S29364 !'##molecule_type protein !'##residues 2-16 ##label JOH REFERENCE A35790 !$#authors Popoff, S.C.; Spira, A.I.; Johnson, A.W.; Demple, B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:4193-4197 !$#title Yeast structural gene (APN1) for the major apurinic !1endonuclease: homology to Escherichia coli endonuclease IV. !$#cross-references MUID:90272680; PMID:1693433 !$#accession A35790 !'##molecule_type DNA !'##residues 1-238,'S',240-367 ##label POP !'##cross-references EMBL:M33667; NID:g171067; PIDN:AAA34429.1; !1PID:g171068 GENETICS !$#gene SGD:APN1; MIPS:YKL114c !'##cross-references SGD:S0001597; MIPS:YKL114c !$#map_position 11L FUNCTION !$#description EC 4.2.99.18 [validated, MUID:90272680]; repairs DNA damage !1generated by oxygen radicals CLASSIFICATION #superfamily deoxyribonuclease IV (phage T4-induced) KEYWORDS carbon-oxygen lyase; metalloprotein; nucleus FEATURE !$2-367 #product DNA-(apurinic or apyrimidinic site) lyase !8#status experimental #label MAT SUMMARY #length 367 #molecular-weight 41439 #checksum 20 SEQUENCE /// ENTRY E69954 #type complete TITLE endonuclease IV homolog yqfS - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69954 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69954 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-297 ##label KUN !'##cross-references GB:Z99116; GB:AL009126; NID:g2634723; !1PIDN:CAB14443.1; PID:g2634946 !'##experimental_source strain 168 GENETICS !$#gene yqfS CLASSIFICATION #superfamily deoxyribonuclease IV (phage T4-induced) SUMMARY #length 297 #molecular-weight 33068 #checksum 6045 SEQUENCE /// ENTRY I64225 #type complete TITLE endonuclease IV homolog - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 07-Dec-1999 ACCESSIONS I64225 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession I64225 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-291 ##label TIGR !'##cross-references GB:U39701; GB:L43967; NID:g1045915; PID:g1045924; !1TIGR:MG235 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily deoxyribonuclease IV (phage T4-induced) SUMMARY #length 291 #molecular-weight 32391 #checksum 2353 SEQUENCE /// ENTRY NDECKR #type complete TITLE type I site-specific deoxyribonuclease (EC 3.1.21.3) EcoK chain R - Escherichia coli (strain K-12) ALTERNATE_NAMES type I restriction enzyme EcoK R chain; type I restriction-modification system EcoK R chain ORGANISM #formal_name Escherichia coli DATE 31-Mar-1990 #sequence_revision 26-Sep-1997 #text_change 01-Mar-2002 ACCESSIONS S56576; H65249; S18776; A30375; Q00648 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56576 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1188 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97247.1; !1PID:g537192 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65249 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1188 ##label BLAT !'##cross-references GB:AE000505; GB:U00096; NID:g2367375; !1PIDN:AAC77306.1; PID:g1790809; UWGP:b4350 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A40368 !$#authors Waite-Rees, P.A.; Keating, C.J.; Moran, L.S.; Slatko, B.E.; !1Hornstra, L.J.; Benner, J.S. !$#journal J. Bacteriol. (1991) 173:5207-5219 !$#title Characterization and expression of the Escherichia coli Mrr !1restriction system. !$#cross-references MUID:91317743; PMID:1650347 !$#accession S18776 !'##status translation not shown !'##molecule_type DNA !'##residues 1-27 ##label WAI !'##cross-references EMBL:X54198 REFERENCE A30375 !$#authors Loenen, W.A.M.; Daniel, A.S.; Braymer, H.D.; Murray, N.E. !$#journal J. Mol. Biol. (1987) 198:159-170 !$#title Organization and sequence of the hsd genes of Escherichia !1coli K-12. !$#cross-references MUID:88118919; PMID:3323532 !$#accession A30375 !'##molecule_type DNA !'##residues 1-628, !1'ECGKNRSHRHPGATYCADFRRAGLPLYLPYRGYRRFSDRPGSAYSDHHPQRAGGGLSLQ !1RRAGRAHQPA',698-1083,'MKISPPG' ##label LOE !'##cross-references GB:X06545; NID:g41751; PIDN:CAA29791.1; PID:g41752 COMMENT This is one of three components (S, R, and M chains) of type !1I site-specific deoxyribonuclease, a multifunctional enzyme !1complex that requires ATP, S-adenosylmethionine, and Mg ion !1as cofactors; it is the site-specificity determinant for the !1catalytic activities of the enzyme. GENETICS !$#gene hsdR !$#map_position 99 min CLASSIFICATION #superfamily type I site-specific deoxyribonuclease EcoK !1chain R KEYWORDS ATP; DNA binding; hydrolase; nucleotide binding; P-loop; !1restriction modification system FEATURE !$489-496 #region nucleotide-binding motif A (P-loop)\ !$588-593 #region nucleotide-binding motif B\ !$592-595 #region DEAH motif SUMMARY #length 1188 #molecular-weight 136100 #checksum 1864 SEQUENCE /// ENTRY NDECKS #type complete TITLE type I site-specific deoxyribonuclease (EC 3.1.21.3) EcoK chain S [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES type I restriction enzyme EcoK chain S; type I restriction-modification system EcoK chain S ORGANISM #formal_name Escherichia coli DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 01-Mar-2002 ACCESSIONS A30369; S56574; S54706; F65249; Q00649 REFERENCE A30369 !$#authors Gough, J.A.; Murray, N.E. !$#journal J. Mol. Biol. (1983) 166:1-19 !$#title Sequence diversity among related genes for recognition of !1specific targets in DNA molecules. !$#cross-references MUID:83216118; PMID:6304321 !$#accession A30369 !'##molecule_type DNA !'##residues 1-464 ##label GOU !'##cross-references GB:V00288; GB:J01632; NID:g41745; PIDN:CAA23554.1; !1PID:g41746 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56574 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-464 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97245.1; !1PID:g537190 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE S54706 !$#authors Chen, A.; Powell, L.M.; Dryden, D.T.F.; Murray, N.E.; Brown, !1T. !$#journal Nucleic Acids Res. (1995) 23:1177-1183 !$#title Tyrosine 27 of the specificity polypeptide of EcoKI can be !1UV crosslinked to a bromodeoxyuridine-substituted DNA target !1sequence. !$#cross-references MUID:95258326; PMID:7739896 !$#accession S54706 !'##status preliminary !'##molecule_type protein !'##residues 2-35 ##label CHE REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65249 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-464 ##label BLAT !'##cross-references GB:AE000505; GB:U00096; NID:g2367375; !1PIDN:AAC77304.1; PID:g1790807; UWGP:b4348 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene hsdS !$#map_position 99 min COMPLEX heterotrimer; S chain (PIR:NDECKS), R chain (PIR:NDECKR), !1and M chain (PIR:XYECHM) FUNCTION !$#description EC 3.1.21.3 [validated, MUID:95258326]; type I site-specific !1deoxyribonuclease, a multifunctional enzyme complex that !1requires ATP, S-adenosylmethionine, and Mg ion as cofactors; !1the site-specificity determinant for the catalytic !1activities of the enzyme CLASSIFICATION #superfamily type I site-specific deoxyribonuclease EcoK !1chain S KEYWORDS ATP; DNA binding; hydrolase; restriction modification system SUMMARY #length 464 #molecular-weight 51395 #checksum 3101 SEQUENCE /// ENTRY NDECAS #type complete TITLE type I site-specific deoxyribonuclease (EC 3.1.21.3) EcoA chain S - Escherichia coli ALTERNATE_NAMES deoxyribonuclease, EcoA, S chain (ATP- and S-adenosyl-L-methionine-dependent); type 1 restriction-modification system, EcoA, S chain; type I restriction enzyme, EcoA, S chain ORGANISM #formal_name Escherichia coli DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 30-Jun-1993 ACCESSIONS A32343 REFERENCE A32343 !$#authors Cowan, G.M.; Gann, A.A.F.; Murray, N.E. !$#journal Cell (1989) 56:103-109 !$#title Conservation of complex DNA recognition domains between !1families of restriction enzymes. !$#cross-references MUID:89089749; PMID:2642743 !$#accession A32343 !'##molecule_type DNA !'##residues 1-589 ##label COW COMMENT This S chain, one of three components (S, R, and M chains) !1of type I site-specific deoxyribonuclease, confers sequence !1specificity to it. The amino-terminal 150 residues are !1sufficient to confer specificity for the target sequence, !1GAG. CLASSIFICATION #superfamily type I site-specific deoxyribonuclease EcoA !1chain S KEYWORDS DNA binding; hydrolase; restriction modification system SUMMARY #length 589 #molecular-weight 66692 #checksum 871 SEQUENCE /// ENTRY NDECES #type complete TITLE type I site-specific deoxyribonuclease (EC 3.1.21.3) EcoE chain S - Escherichia coli ALTERNATE_NAMES deoxyribonuclease, EcoE, S chain (ATP- and S-adenosyl-L-methionine-dependent); type 1 restriction-modification system, EcoE, S chain; type I restriction enzyme, EcoE, S chain ORGANISM #formal_name Escherichia coli DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 11-Jun-1999 ACCESSIONS B32343 REFERENCE A32343 !$#authors Cowan, G.M.; Gann, A.A.F.; Murray, N.E. !$#journal Cell (1989) 56:103-109 !$#title Conservation of complex DNA recognition domains between !1families of restriction enzymes. !$#cross-references MUID:89089749; PMID:2642743 !$#accession B32343 !'##molecule_type DNA !'##residues 1-594 ##label COW !'##cross-references GB:J03162; NID:g146399; PIDN:AAA23986.1; !1PID:g146400 COMMENT This S chain, one of three components (S, R, and M chains) !1of type I site-specific deoxyribonuclease, confers sequence !1specificity to it. The amino-terminal 150 residues are !1sufficient to confer specificity for the target sequence, !1GAG. CLASSIFICATION #superfamily type I site-specific deoxyribonuclease EcoA !1chain S KEYWORDS DNA binding; hydrolase; restriction modification system SUMMARY #length 594 #molecular-weight 66343 #checksum 8137 SEQUENCE /// ENTRY S06097 #type complete TITLE type I site-specific deoxyribonuclease (EC 3.1.21.3) CfrA chain S - Citrobacter freundii ALTERNATE_NAMES restriction endonuclease CfrA, polypeptide S ORGANISM #formal_name Citrobacter freundii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S06097 REFERENCE S06097 !$#authors Kannan, P.; Cowan, G.M.; Daniel, A.S.; Gann, A.A.F.; Murray, !1N.E. !$#journal J. Mol. Biol. (1989) 209:335-344 !$#title Conservation of organization in the specificity polypeptides !1of two families of type I restriction enzymes. !$#cross-references MUID:90064497; PMID:2585490 !$#accession S06097 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-578 ##label KAN !'##cross-references GB:X17591; NID:g40466; PIDN:CAA35604.1; PID:g40467 GENETICS !$#gene hsdS CLASSIFICATION #superfamily type I site-specific deoxyribonuclease EcoA !1chain S KEYWORDS hydrolase SUMMARY #length 578 #molecular-weight 65074 #checksum 9706 SEQUENCE /// ENTRY NDOFS #type complete TITLE type II site-specific deoxyribonuclease (EC 3.1.21.4) PstI - Providencia stuartii ALTERNATE_NAMES endonuclease PstI; type II restriction enzyme PstI ORGANISM #formal_name Providencia stuartii DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 11-Jun-1999 ACCESSIONS A00783 REFERENCE A92485 !$#authors Walder, R.Y.; Walder, J.A.; Donelson, J.E. !$#journal J. Biol. Chem. (1984) 259:8015-8026 !$#title The organization and complete nucleotide sequence of the !1PstI restriction-modification system. !$#cross-references MUID:84239756; PMID:6330092 !$#accession A00783 !'##molecule_type DNA !'##residues 1-326 ##label WAL !'##cross-references GB:K02081; NID:g150922; PIDN:AAA25673.1; !1PID:g150924 !'##experimental_source strain 164 !'##note the authors translated the codon AAA for residue 218 as Gly COMMENT This is one of the type II restriction enzymes, which !1require only magnesium ions, have separate modification !1methylases, recognize specific short, double-stranded !1nucleotides, and cleave within, or at a short specific !1distance from, the recognition sites. The recognition !1sequence for PstI is 5'-CTGCAG. COMMENT Providencia, a genus of enterobacteriacean rods, is !1sometimes included in the genus Proteus. CLASSIFICATION #superfamily type II site-specific deoxyribonuclease PstI KEYWORDS endonuclease; hydrolase; magnesium SUMMARY #length 326 #molecular-weight 37413 #checksum 9009 SEQUENCE /// ENTRY NDPS7A #type complete TITLE type II site-specific deoxyribonuclease (EC 3.1.21.4) PaeR7I - Pseudomonas aeruginosa plasmid pMG7 ALTERNATE_NAMES restriction endonuclease PaeR7I ORGANISM #formal_name Pseudomonas aeruginosa DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 11-Jun-1999 ACCESSIONS S07935 REFERENCE S07366 !$#authors Theriault, G.; Roy, P.H.; Howard, K.A.; Benner, J.S.; !1Brooks, J.E.; Waters, A.F.; Gingeras, T.R. !$#journal Nucleic Acids Res. (1985) 13:8441-8461 !$#title Nucleotide sequence of the PaeR7 restriction/modification !1system and partial characterization of its protein products. !$#cross-references MUID:86093653; PMID:3001639 !$#accession S07935 !'##molecule_type DNA !'##residues 1-246 ##label THE !'##cross-references EMBL:X03274; NID:g45385; PIDN:CAA27026.1; !1PID:g45387 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing GENETICS !$#gene paeR7IR !$#genome plasmid CLASSIFICATION #superfamily type II site-specific deoxyribonuclease PaeR7I KEYWORDS endonuclease; homodimer; hydrolase FEATURE !$2-246 #product type II site-specific deoxyribonuclease !8PaeR7I #status experimental #label MAT SUMMARY #length 246 #molecular-weight 27279 #checksum 4667 SEQUENCE /// ENTRY NDECR5 #type complete TITLE type II site-specific deoxyribonuclease (EC 3.1.21.4) EcoRV - Escherichia coli ALTERNATE_NAMES endonuclease EcoRV; type II restriction enzyme EcoRV ORGANISM #formal_name Escherichia coli DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 11-Jun-1999 ACCESSIONS A00784; I77184 REFERENCE A93516 !$#authors Bougueleret, L.; Schwarzstein, M.; Tsugita, A.; Zabeau, M. !$#journal Nucleic Acids Res. (1984) 12:3659-3676 !$#title Characterization of the genes coding for the Eco RV !1restriction and modification system of Escherichia coli. !$#cross-references MUID:84221388; PMID:6328432 !$#accession A00784 !'##molecule_type DNA !'##residues 1-245 ##label BOU !'##cross-references GB:X00530; GB:K02335; NID:g41324; PIDN:CAA25208.1; !1PID:g41325 !'##note the authors translated the codon GAT for residue 90 as Asn REFERENCE I57396 !$#authors Kraev, A.S.; Kravets, A.N.; Chernov, B.K.; Skryabin, K.G.; !1Baev, A.A. !$#journal Mol. Biol. (1985) 19:236-242 !$#title The EcoRV restriction-modification system: Genes, enzymes, !1synthetic substrates. !$#accession I77184 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-245 ##label RES !'##cross-references GB:M19941; NID:g147784; PIDN:AAA24615.1; !1PID:g147786 FUNCTION !$#description this is one of the type II restriction enzymes, which !1require only magnesium ions, have separate modification !1methylases, recognize specific short, double-stranded !1nucleotides, and cleave within, or at a short specific !1distance from, the recognition sites; the recognition !1sequence for EcoRV is 5'-GATATC, and the blunt-ended !1cleavage site is between the T and the A in the center of !1the recognition sequence CLASSIFICATION #superfamily type II site-specific deoxyribonuclease EcoRV KEYWORDS endonuclease; hydrolase; magnesium SUMMARY #length 245 #molecular-weight 28650 #checksum 9145 SEQUENCE /// ENTRY NDBSR1 #type complete TITLE type II site-specific deoxyribonuclease (EC 3.1.21.4) BsuRI - Bacillus subtilis (strain R) ALTERNATE_NAMES endonuclease BsuRI; type II restriction enzyme BsuRI ORGANISM #formal_name Bacillus subtilis DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 11-Jun-1999 ACCESSIONS A23488 REFERENCE A93587 !$#authors Kiss, A.; Posfai, G.; Keller, C.C.; Venetianer, P.; Roberts, !1R.J. !$#journal Nucleic Acids Res. (1985) 13:6403-6421 !$#title Nucleotide sequence of the BsuRI restriction-modification !1system. !$#cross-references MUID:86041846; PMID:2997708 !$#accession A23488 !'##molecule_type DNA !'##residues 1-576 ##label KIS !'##cross-references GB:X02988; NID:g40245; PIDN:CAA26730.1; PID:g40246 COMMENT The recognition sequence for this enzyme is 5'-GGCC and it !1cleaves between the C and G. COMMENT This enzyme in this strain is not found in strain 168. CLASSIFICATION #superfamily type II site-specific deoxyribonuclease BsuR1 KEYWORDS endonuclease; hydrolase; magnesium SUMMARY #length 576 #molecular-weight 66304 #checksum 2700 SEQUENCE /// ENTRY S38901 #type complete TITLE type II site-specific deoxyribonuclease (EC 3.1.21.4) munI - Mycoplasma sp. ORGANISM #formal_name Mycoplasma sp. DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 07-Dec-1999 ACCESSIONS S38901 REFERENCE S38899 !$#authors Siksnys, V.; Zareckaja, N.; Vaisvila, R.; Timinskas, A.; !1Stakenas, P.; Butkus, V.; Janulaitis, A. !$#submission submitted to the EMBL Data Library, November 1993 !$#description CAATTG-specific restriction-modification MunI genes from !1Mycoplasma: homologies between R. MunI and R. EcoRI. !$#accession S38901 !'##molecule_type DNA !'##residues 1-202 ##label SIK !'##cross-references EMBL:X76192; NID:g431927; PIDN:CAA53788.1; !1PID:g431930 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily Mycoplasma type II site-specific !1deoxyribonuclease munI KEYWORDS endonuclease; hydrolase SUMMARY #length 202 #molecular-weight 23389 #checksum 6504 SEQUENCE /// ENTRY S14133 #type complete TITLE DNA endonuclease (EC 3.1.-.-) I-CeuI - Chlamydomonas eugametos chloroplast ALTERNATE_NAMES 23S rRNA intron 1 protein ORGANISM #formal_name chloroplast Chlamydomonas eugametos DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 11-Jun-1999 ACCESSIONS S14133; S15138 REFERENCE S14133 !$#authors Gauthier, A.; Turmel, M.; Lemieux, C. !$#journal Curr. Genet. (1991) 19:43-47 !$#title A group I intron in the chloroplast large subunit rRNA gene !1of Chlamydomonas eugametos encodes a double-strand !1endonuclease that cleaves the homing site of this intron. !$#cross-references MUID:91243206; PMID:2036685 !$#accession S14133 !'##molecule_type DNA !'##residues 1-218 ##label GAU !'##cross-references EMBL:Z17234; NID:g11360; PIDN:CAA78934.1; !1PID:g11361 REFERENCE S15138 !$#authors Turmel, M.; Boulanger, J.; Schnare, M.N.; Gray, M.W.; !1Lemieux, C. !$#journal J. Mol. Biol. (1991) 218:293-311 !$#title Six group I introns and three internal transcribed spacers !1in the chloroplast large subunit ribosomal RNA gene of the !1green alga Chlamydomonas eugametos. !$#cross-references MUID:91186395; PMID:1849178 !$#accession S15138 !'##molecule_type DNA !'##residues 1-218 ##label TUR !'##cross-references EMBL:Z17234; NID:g11360; PIDN:CAA78934.1; !1PID:g11361 GENETICS !$#genome chloroplast CLASSIFICATION #superfamily DNA endonuclease I-CeuI KEYWORDS chloroplast; endonuclease; hydrolase SUMMARY #length 218 #molecular-weight 24891 #checksum 4123 SEQUENCE /// ENTRY NEBP37 #type complete TITLE endodeoxyribonuclease I (EC 3.1.21.-) - phage T7 ORGANISM #formal_name phage T7 DATE 01-Sep-1981 #sequence_revision 24-Sep-1981 #text_change 11-Jun-1999 ACCESSIONS B94615; C92866; S42301; A00785 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession B94615 !'##molecule_type DNA !'##residues 1-149 ##label DU1 REFERENCE A92866 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1981) 148:303-330 !$#title Nucleotide sequence from the genetic left end of !1bacteriophage T7 DNA to the beginning of gene 4. !$#cross-references MUID:82078034; PMID:7310871 !$#accession C92866 !'##molecule_type DNA !'##residues 1-149 ##label DU2 !'##cross-references GB:V01127; NID:g15498; PIDN:CAA24345.1; PID:g15517 REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42301 !'##molecule_type DNA !'##residues 1-149 ##label DUN !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24402.1; !1PID:g15581 !'##note the authors did not translate the codon for residue 1 COMMENT Endodeoxyribonuclease I, which is expressed in the late !1stage, is necessary for T7 genetic recombination and the !1breakdown of host DNA. In the early stage of infection, T7 !1DNA replicates as a linear monomer. In the late stage, the !1T7 DNA replicates via linear concatemers several genomes in !1length. The gene 3 product has also been implicated in the !1maturation of these concatemers. GENETICS !$#gene 3 !$#map_position 25.64-26.76 CLASSIFICATION #superfamily phage T7 exodeoxyribonuclease I KEYWORDS hydrolase SUMMARY #length 149 #molecular-weight 17172 #checksum 1563 SEQUENCE /// ENTRY NEBPT4 #type complete TITLE endonuclease V [validated] - phage T4 ALTERNATE_NAMES AP-endonuclease; DenV protein; deoxyribonuclease (pyrimidine dimer) (EC 3.1.25.1) [misnomer]; PD-glycosylase; pyrimidine dimer DNA-glycosylase CONTAINS deoxyribodipyrimidine endonucleosidase (EC 3.2.2.17); DNA- (apurinic or apyrimidinic site) lyase (EC 4.2.99.18) ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 15-Sep-2000 ACCESSIONS A93540; A93004; S48016; A55702; A42850; A00786 REFERENCE A93540 !$#authors Valerie, K.; Henderson, E.E.; DeRiel, J.K. !$#journal Nucleic Acids Res. (1984) 12:8085-8096 !$#title Identification, physical map location and sequence of the !1denV gene from bacteriophage T4. !$#cross-references MUID:85062800; PMID:6095188 !$#accession A93540 !'##molecule_type DNA !'##residues 1-138 ##label VAL !'##cross-references GB:X04567; NID:g15260; PIDN:CAA28215.1; PID:g15268 REFERENCE A93004 !$#authors Radany, E.H.; Naumovski, L.; Love, J.D.; Gutekunst, K.A.; !1Hall, D.H.; Friedberg, E.C. !$#journal J. Virol. (1984) 52:846-856 !$#title Physical mapping and complete nucleotide sequence of the !1denV gene of bacteriophage T4. !$#cross-references MUID:85033951; PMID:6092716 !$#accession A93004 !'##molecule_type DNA !'##residues 1-138 ##label RAD REFERENCE S48006 !$#authors Repoila, F.; Tetart, F.; Bouet, J.Y.; Krisch, H.M. !$#journal EMBO J. (1994) 13:4181-4192 !$#title Genomic polymorphism in the T-even bacteriophages. !$#cross-references MUID:94357192; PMID:8076614 !$#accession S48016 !'##molecule_type DNA !'##residues 1-138 ##label REP REFERENCE A55702 !$#authors Manuel, R.C.; Latham, K.A.; Dodson, M.L.; Lloyd, R.S. !$#journal J. Biol. Chem. (1995) 270:2652-2661 !$#title Involvement of glutamic acid 23 in the catalytic mechanism !1of T4 endonuclease V. !$#cross-references MUID:95155330; PMID:7852333 !$#accession A55702 !'##molecule_type protein !'##residues 2-26 ##label MAN REFERENCE A42850 !$#authors Hori, N.; Iwai, S.; Inoue, H.; Ohtsuka, E. !$#journal J. Biol. Chem. (1992) 267:15591-15594 !$#title Photoaffinity labeling of T4 endonuclease V with a substrate !1containing a phenyldiazirine derivative. !$#cross-references MUID:92348416; PMID:1639800 !$#accession A42850 !'##molecule_type protein !'##residues 87-91;122-129;131-133 ##label HOR !'##note the cited accession number, K02201, is not in GenBank release !1103.1 REFERENCE A52708 !$#authors Vassylyev, D.G.; Ariyoshi, M.; Matsumoto, O.; Katayanagi, !1K.; Ohtsuka, E.; Morikawa, K. !$#submission submitted to the Brookhaven Protein Data Bank, August 1994 !$#cross-references PDB:2END !$#contents annotation; X-ray crystallography, 1.45 angstroms, residues !12-138 REFERENCE A58665 !$#authors Morikawa, K.; Matsumoto, O.; Tsujimoto, M.; Katayanagi, K.; !1Ariyoshi, M.; Doi, T.; Ikehara, M.; Inaoka, T.; Ohtsuka, E. !$#journal Science (1992) 256:523-526 !$#title X-ray structure of T4 endonuclease V: an excision repair !1enzyme specific for a pyrimidine dimer. !$#cross-references MUID:92237690; PMID:1575827 !$#contents annotation; X-ray crystallography, 1.6 angstroms GENETICS !$#gene denV FUNCTION DGL !$#description as deoxyribodipyrimidine endonucleosidase (EC 3.2.2.17), !1catalyzes cleavage of the 5'-pyrimidine N-glycosidic bond to !1deoxy-D-ribose at a cyclobutadipyrimidine (cross-linked !1pyrimidine dimer) in DNA FUNCTION APE !$#description as DNA-(apurinic or apyrimidinic site) lyase (EC 4.2.99.18), !1catalyzes beta-elimination cleavage of an apyrimidinic !1phosphodiester to produce 3'-terminal 1-oxo-4, !15-dihydroxy-2-pentene and 5'-terminal cyclobutadipyrimidine !1deoxyribose 5'-phosphate DNA !$#note the overall reaction, endonucleolytic cleavage of !1cross-linked pyrimidine dimers to make a 5'-phosphate !1product, has been described as a deoxyribonuclease !1(pyrimidine dimer) (EC 3.1.25.1) activity CLASSIFICATION #superfamily phage T4 endonuclease V KEYWORDS carbon-oxygen lyase; endonuclease; glycosidase; hydrolase FEATURE !$2-138 #product endonuclease V #status experimental #label !8MAT\ !$2 #active_site Thr (covalent substrate-binding !8amino-terminal) (in mature form) #status !8experimental\ !$23 #active_site Glu #status experimental SUMMARY #length 138 #molecular-weight 16078 #checksum 2338 SEQUENCE /// ENTRY XYECMB #type complete TITLE 5-methylcytosine-specific restriction enzyme B (EC 3.1.21.-) - Escherichia coli (strain K-12) CONTAINS McrB 33K protein ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 03-Nov-1995 #text_change 01-Mar-2002 ACCESSIONS A36708; JS0120; S56572; D65249; JN0253 REFERENCE A36708 !$#authors Dila, D.; Sutherland, E.; Moran, L.; Slatko, B.; Raleigh, !1E.A. !$#journal J. Bacteriol. (1990) 172:4888-4900 !$#title Genetic and sequence organization of the mcrBC locus of !1Escherichia coli K-12. !$#cross-references MUID:90368539; PMID:2203735 !$#accession A36708 !'##status preliminary !'##molecule_type DNA !'##residues 1-465 ##label DIL !'##cross-references GB:M58752; GB:M34235; NID:g146795; PIDN:AAA24145.1; !1PID:g146796 REFERENCE A91894 !$#authors Ross, T.K.; Achberger, E.C.; Braymer, H.D. !$#journal J. Bacteriol. (1989) 171:1974-1981 !$#title Nucleotide sequence of the McrB region of Escherichia coli !1K-12 and evidence for two independent translational !1initiation sites at the mcrB locus. !$#cross-references MUID:89197765; PMID:2649480 !$#accession JS0120 !'##molecule_type DNA !'##residues 7-191,'SDTQTINHQKKYYPPGAARRWKNLCCT',219-229,'RTKYGSV', !1239-250,'IVRMASASVKTHI',266-465 ##label ROS !'##cross-references GB:M24927; NID:g146789; PIDN:AAA24142.1; !1PID:g146790 !'##experimental_source strain K12 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56572 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-465 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97243.1; !1PID:g537188 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65249 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-465 ##label BLAT !'##cross-references GB:AE000505; GB:U00096; NID:g2367375; !1PIDN:AAC77302.1; PID:g1790805; UWGP:b4346 !'##experimental_source strain K-12, substrain MG1655 REFERENCE JN0253 !$#authors Zheng, L.; Wang, X.; Braymer, H.D. !$#journal Gene (1992) 112:97-100 !$#title Purification and N-terminal amino acid sequences of two !1polypeptides encoded by the mcrB gene from Escherichia coli !1K-12. !$#cross-references MUID:92201708; PMID:1312983 !$#accession JN0253 !'##molecule_type protein !'##residues 7-16;169-181 ##label ZHE !'##experimental_source strain K12 !'##note the first 16 residues are the amino-terminal end of McrB 51K !1protein and the following 171 residues are the !1amino-terminal end of McrB 33K protein GENETICS !$#gene mcrB !$#map_position 99 min !$#note another, less active, molecular species (residues 168-465) !1of this enzyme is also found; it is an independently !1translated (using a different initiation codon) product from !1the same gene FUNCTION !$#description a restriction enzyme attacks foreign DNA containing !15-methylcytosine; it recognizes the consensus sequence of !1GmC CLASSIFICATION #superfamily 5-methylcytosine-specific restriction enzyme B KEYWORDS DNA binding; hydrolase FEATURE !$1-465 #product 5-methylcytosine-specific restriction enzyme !8B #status predicted #label MC5\ !$168-465 #product 33K 5-methylcytosine-specific restriction !8enzyme B #status predicted #label MC3 SUMMARY #length 465 #molecular-weight 53920 #checksum 4805 SEQUENCE /// ENTRY NDECP4 #type complete TITLE type II site-specific deoxyribonuclease (EC 3.1.21.4) EcoRI - Escherichia coli plasmids ALTERNATE_NAMES endonuclease EcoRI ORGANISM #formal_name Escherichia coli DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 28-May-1999 ACCESSIONS B92308; A00787 REFERENCE A92308 !$#authors Newman, A.K.; Rubin, R.A.; Kim, S.H.; Modrich, P. !$#journal J. Biol. Chem. (1981) 256:2131-2139 !$#title DNA sequences of structural genes for Eco RI DNA restriction !1and modification enzymes. !$#cross-references MUID:81117318; PMID:6257701 !$#accession B92308 !'##molecule_type DNA !'##residues 1-276 ##label NEW !'##cross-references GB:J01675; NID:g152446; PIDN:AAA26371.1; !1PID:g152447 !'##experimental_source strain C600, plasmid pMB4 REFERENCE A92309 !$#authors Rubin, R.A.; Modrich, P.; Vanaman, T.C. !$#journal J. Biol. Chem. (1981) 256:2140-2142 !$#title Partial NH-2- and COOH-terminal sequence analyses of ECO RI !1DNA restriction and modification enzymes. !$#cross-references MUID:81117319; PMID:6257702 !$#contents annotation !$#note the amino and carboxyl ends of the sequence were confirmed !1by amino acid analysis REFERENCE A92310 !$#authors Greene, P.J.; Gupta, M.; Boyer, H.W.; Brown, W.E.; !1Rosenberg, J.M. !$#journal J. Biol. Chem. (1981) 256:2143-2153 !$#title Sequence analysis of the DNA encoding the Eco RI !1endonuclease and methylase. !$#cross-references MUID:81117320; PMID:6257703 !$#accession A00787 !'##molecule_type DNA !'##residues 1-276 ##label GRE !'##cross-references GB:J01675; NID:g152446; PIDN:AAA26371.1; !1PID:g152447 !'##experimental_source plasmid pMB1 GENETICS !$#genome plasmid FUNCTION !$#description EcoRI restriction endodeoxyribonuclease recognizes the !1double-stranded hexanucleotide GAATTC and causes !1double-strand cleavage within the sequence CLASSIFICATION #superfamily type II site-specific deoxyribonuclease EcoRI KEYWORDS endonuclease; hydrolase; magnesium; restriction modification !1system SUMMARY #length 276 #molecular-weight 30928 #checksum 3821 SEQUENCE /// ENTRY NDHIH2 #type complete TITLE type II site-specific deoxyribonuclease (EC 3.1.21.4) HhaII - Haemophilus haemolyticus ALTERNATE_NAMES endonuclease HhaII ORGANISM #formal_name Haemophilus haemolyticus DATE 20-Sep-1984 #sequence_revision 20-Sep-1984 #text_change 30-Sep-1993 ACCESSIONS A00788 REFERENCE A91503 !$#authors Schoner, B.; Kelly, S.; Smith, H.O. !$#journal Gene (1983) 24:227-236 !$#title The nucleotide sequence of the HhaII restriction and !1modification genes from Haemophilus haemolyticus. !$#cross-references MUID:84059084; PMID:6315538 !$#accession A00788 !'##molecule_type DNA !'##residues 1-227 ##label SCH COMMENT The HhaII restriction endodeoxyribonuclease recognizes the !1double-stranded pentanucleotide GANTC. However, the precise !1cleavage site has not been determined. COMMENT H. haemolyticus is a minute, gram-negative, rod-shaped !1parasitic bacterium found in mucus membrane of the upper !1respiratory tract of man. CLASSIFICATION #superfamily type II site-specific deoxyribonuclease HhaII KEYWORDS hydrolase SUMMARY #length 227 #molecular-weight 25910 #checksum 7469 SEQUENCE /// ENTRY NDKE2M #type complete TITLE type II site-specific deoxyribonuclease (EC 3.1.21.4) MspI - Moraxella sp. ALTERNATE_NAMES restriction endonuclease MspI ORGANISM #formal_name Moraxella sp. DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 11-Jun-1999 ACCESSIONS S04187 REFERENCE S04187 !$#authors Lin, P.M.; Lee, C.H.; Roberts, R.J. !$#journal Nucleic Acids Res. (1989) 17:3001-3011 !$#title Cloning and characterization of the genes encoding the MspI !1restriction modification system. !$#cross-references MUID:89263712; PMID:2471145 !$#accession S04187 !'##molecule_type DNA !'##residues 1-262 ##label LIN !'##cross-references EMBL:X14191; NID:g44538; PIDN:CAA32394.1; !1PID:g44540 CLASSIFICATION #superfamily type II site-specific deoxyribonuclease MspI KEYWORDS endonuclease; homodimer; hydrolase; restriction modification !1system SUMMARY #length 262 #molecular-weight 29829 #checksum 1120 SEQUENCE /// ENTRY NCSAF #type complete TITLE micrococcal nuclease (EC 3.1.31.1) precursor - Staphylococcus aureus ALTERNATE_NAMES staphylococcal nuclease CONTAINS micrococcal nuclease A; micrococcal nuclease B ORGANISM #formal_name Staphylococcus aureus DATE 29-Jul-1981 #sequence_revision 19-Feb-1984 #text_change 11-Jun-1999 ACCESSIONS A00790; A05340; A05341 REFERENCE A00790 !$#authors Shortle, D. !$#journal Gene (1983) 22:181-189 !$#title A genetic system for analysis of staphylococcal nuclease. !$#cross-references MUID:83263136; PMID:6307819 !$#accession A00790 !'##molecule_type DNA !'##residues 1-231 ##label SHO !'##cross-references GB:V01281; GB:J01785; GB:M10924; NID:g46623; !1PIDN:CAA24594.1; PID:g673492 !'##experimental_source strain Foggi REFERENCE A05340 !$#authors Davis, A.; Moore, I.B.; Parker, D.S.; Taniuchi, H. !$#journal J. Biol. Chem. (1977) 252:6544-6551 !$#title Nuclease B. A possible precursor of nuclease A, an !1extracellular nuclease of Staphylococcus aureus. !$#cross-references MUID:77249610; PMID:893427 !$#accession A05340 !'##molecule_type protein !'##residues 64-82 ##label DAV !'##experimental_source strain Foggi !'##note 68-Asp and 71-Asp were also found REFERENCE A05341 !$#authors Cone, J.L.; Cusumano, C.L.; Taniuchi, H.; Anfinsen, C.B. !$#journal J. Biol. Chem. (1971) 246:3103-3110 !$#title Staphylcoccal nuclease (Foggi strain). !$#cross-references MUID:71185678; PMID:4324890 !$#accession A05341 !'##molecule_type protein !'##residues 83-231 ##label CON !'##experimental_source strain Foggi REFERENCE A05342 !$#authors Bohnert, J.L.; Taniuchi, H. !$#journal J. Biol. Chem. (1972) 247:4557-4560 !$#title The examination of the presence of amide groups in glutamic !1acid and aspartic acid residues of straphylococcal nuclease !1(Foggi strain). !$#cross-references MUID:72234381; PMID:4339720 !$#contents annotation; amide assignments for residues 83-231; strain !1Foggi REFERENCE A05343 !$#authors Cotton, F.A.; Hazen Jr., E.C.; Legg, M.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1979) 76:2551-2555 !$#title Staphylococcal nuclease: proposed mechanism of action based !1on structure of enzyme-thymidine 3',5'-bisphosphate-calcium !1ion complex at 1.5-angstrom resolution. !$#cross-references MUID:79223828; PMID:288045 !$#contents annotation; X-ray crystallography, 1.5 angstroms; proposed !1catalytic mechanism COMMENT Nuclease B is a membrane-bound precursor of nuclease A found !1in exponentially growing cells. COMMENT Staphylococcal nuclease is a calcium-dependent, !1extracellular enzyme that catalyzes the hydrolysis of both !1DNA and RNA at the 5' position of the phosphodiester bond. GENETICS !$#gene nuc CLASSIFICATION #superfamily micrococcal nuclease KEYWORDS hydrolase FEATURE !$1-63 #domain signal sequence #status predicted #label SIG\ !$64-231 #product micrococcal nuclease B #status experimental !8#label MATB\ !$83-231 #product micrococcal nuclease A #status experimental !8#label MATA\ !$117,125,169 #active_site Arg, Glu, Arg #status experimental SUMMARY #length 231 #molecular-weight 25471 #checksum 4576 SEQUENCE /// ENTRY NCEBPX #type complete TITLE micrococcal nuclease (EC 3.1.31.1) precursor - Shigella flexneri plasmid pSa ORGANISM #formal_name Shigella flexneri DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 11-Jun-1999 ACCESSIONS S20541 REFERENCE S20540 !$#authors Close, S.M.; Kado, C.I. !$#journal Mol. Microbiol. (1992) 6:521-527 !$#title A gene near the plasmid pSa origin of replication encodes a !1nuclease. !$#cross-references MUID:92219997; PMID:1560781 !$#accession S20541 !'##molecule_type DNA !'##residues 1-174 ##label CLO !'##cross-references GB:U30471; EMBL:M81325; NID:g976151; !1PIDN:AAA75246.1; PID:g976155 GENETICS !$#gene nuc !$#genome plasmid CLASSIFICATION #superfamily micrococcal nuclease KEYWORDS hydrolase FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-174 #product micrococcal nuclease #status predicted !8#label MAT SUMMARY #length 174 #molecular-weight 19689 #checksum 4627 SEQUENCE /// ENTRY CDECP3 #type complete TITLE cloacin DF13 protein - Escherichia coli plasmid CloDF13 ALTERNATE_NAMES protein A CONTAINS ribonuclease (EC 3.1.-.-) activity ORGANISM #formal_name Escherichia coli DATE 18-Aug-1982 #sequence_revision 19-Feb-1984 #text_change 11-Jun-1999 ACCESSIONS A00791; C28585 REFERENCE A00791 !$#authors van den Elzen, P.J.M.; Walters, H.H.B.; Veltkamp, E.; !1Nijkamp, H.J.J. !$#journal Nucleic Acids Res. (1983) 11:2465-2477 !$#title Molecular structure and function of the bacteriocin gene and !1bacteriocin protein of plasmid Clo DF13. !$#cross-references MUID:83220797; PMID:6344017 !$#accession A00791 !'##molecule_type DNA !'##residues 1-561 ##label VAN REFERENCE A93765 !$#authors Nijkamp, H.J.J.; de Lang, R.; Stuitje, A.R.; van den Elzen, !1P.J.M.; Veltkamp, E.; van Putten, A.J. !$#journal Plasmid (1986) 16:135-160 !$#title The complete nucleotide sequence of the bacteriocinogenic !1plasmid CloDF13. !$#cross-references MUID:86314306; PMID:3749334 !$#accession C28585 !'##molecule_type DNA !'##residues 1-111,'P',113-561 ##label NIJ !'##cross-references GB:X04466; GB:J01558; GB:J01559; GB:J01560; !1GB:J01561; GB:J01562; GB:K02267; GB:K02333; GB:M16195; !1GB:M17497; GB:M23861; GB:M38599; GB:V00377; GB:X00141; !1GB:X00223; GB:X01287; NID:g42320; PIDN:CAA28147.1; !1PID:g42323 !'##experimental_source strain K12 P678-54 !'##note the authors translated the codon GAA for residue 330 as Asp COMMENT This protein can be divided into four domains according to !1function: the first 150-180 residues are probably involved !1in the translocation of the protein across the cell !1membrane; the central region (residues 200-420) is !1responsible for the receptor binding activity; the !1carboxyl-terminal domain (the last 200 residues) has !1ribonuclease activity. The last 30 residues are also !1responsible for binding of immunity protein. GENETICS !$#genome plasmid CLASSIFICATION #superfamily cloacin DF13 protein KEYWORDS bacteriocin; hydrolase SUMMARY #length 561 #molecular-weight 59294 #checksum 8557 SEQUENCE /// ENTRY NRECE3 #type complete TITLE colicin E3 (EC 3.1.21.-) chain A - Escherichia coli plasmid ColE3(-CA38) ORGANISM #formal_name Escherichia coli DATE 30-Nov-1980 #sequence_revision 01-Mar-1996 #text_change 11-Jun-1999 ACCESSIONS S07269; C00789; A93470; A91307; A91947; A00792 REFERENCE S07269 !$#authors Masaki, H.; Ohta, T. !$#journal J. Mol. Biol. (1985) 182:217-227 !$#title Colicin E3 and its immunity genes. !$#cross-references MUID:85210906; PMID:3889348 !$#accession S07269 !'##status preliminary !'##molecule_type DNA !'##residues 1-551 ##label MAS !'##cross-references EMBL:X02397; NID:g41132; PIDN:CAA26241.1; !1PID:g41133 REFERENCE A00789 !$#authors Lau, P.C.K.; Rowsome, R.W.; Zuker, M.; Visentin, L.P. !$#journal Nucleic Acids Res. (1984) 12:8733-8745 !$#title Comparative nucleotide sequences encoding the immunity !1proteins and the carboxyl-terminal peptides of colicins E2 !1and E3. !$#cross-references MUID:85062845; PMID:6095211 !$#accession C00789 !'##status preliminary !'##molecule_type DNA !'##residues 370-551 ##label LAU !'##cross-references GB:X01162; NID:g41802; PIDN:CAA25607.1; PID:g41803 REFERENCE A93470 !$#authors Mock, M.; Miyada, C.G.; Gunsalus, R.P. !$#journal Nucleic Acids Res. (1983) 11:3547-3557 !$#title Nucleotide sequence for the catalytic domain of colicin E3 !1and its immunity protein. Evidence for a third gene !1overlapping colicin. !$#cross-references MUID:83220760; PMID:6344012 !$#accession A93470 !'##molecule_type DNA !'##residues 428-551 ##label MOC REFERENCE A91307 !$#authors Masaki, H.; Ohta, T. !$#journal FEBS Lett. (1982) 149:129-132 !$#title A plasmid region encoding the active fragment and the !1inhibitor protein of colicin E3-CA38. !$#cross-references MUID:83105715; PMID:6295812 !$#accession A91307 !'##molecule_type DNA !'##residues 445-551 ##label MA2 REFERENCE A91947 !$#authors Suzuki, K.; Imahori, K. !$#journal J. Biochem. (1978) 84:1031-1039 !$#title Amino acid sequence of an active fragment (T2A) of colicin !1E3. !$#cross-references MUID:79088682; PMID:730747 !$#accession A91947 !'##molecule_type protein !'##residues 455-489,'D',491-551 ##label SUZ GENETICS !$#gene ceaC !$#genome plasmid COMPLEX heterodimer of chain A and chain B FUNCTION !$#description colicin E3 is a plasmid-specified antibiotic; chain A !1inactivates ribosomes by hydrolyzing 16S RNA in 30S !1ribosomes at a specific site; chain B inhibits this !1activity; both chains are essential for bactericidal !1activity; residues 455-551 above have all of the !1ribosome-inactivating activity of chain A CLASSIFICATION #superfamily cloacin DF13 protein KEYWORDS bacteriocin; endonuclease; hydrolase; toxin SUMMARY #length 551 #molecular-weight 57963 #checksum 4183 SEQUENCE /// ENTRY S49176 #type fragment TITLE colicin E4 (EC 3.1.21.-) - Escherichia coli (fragment) ORGANISM #formal_name Escherichia coli DATE 16-Feb-1995 #sequence_revision 22-Nov-1996 #text_change 11-Jun-1999 ACCESSIONS S49176 REFERENCE S49176 !$#authors Lau, P.C.K.; Parsons, M. !$#submission submitted to the EMBL Data Library, December 1991 !$#description Nucleotide sequence encoding the immunity and lysis proteins !1and the carboxyl terminl peptides of colicins E4 and E7. !$#accession S49176 !'##status preliminary !'##molecule_type DNA !'##residues 1-177 ##label LAU !'##cross-references EMBL:X63621; NID:g510380; PIDN:CAA45167.1; !1PID:g510381 CLASSIFICATION #superfamily cloacin DF13 protein KEYWORDS bacteriocin; endonuclease; hydrolase; toxin SUMMARY #length 177 #checksum 749 SEQUENCE /// ENTRY S22453 #type complete TITLE colicin E7 (EC 3.1.21.-) - Escherichia coli plasmid ColE7-K317 ORGANISM #formal_name Escherichia coli DATE 04-Dec-1992 #sequence_revision 24-Apr-1998 #text_change 11-Jun-1999 ACCESSIONS S22453; S49179 REFERENCE S22453 !$#authors Soong, B.W.; Lu, F.M.; Chak, K.F. !$#journal Mol. Gen. Genet. (1992) 233:177-183 !$#title Characterization of the cea gene of the ColE7 plasmid. !$#cross-references MUID:92293113; PMID:1603061 !$#accession S22453 !'##molecule_type DNA !'##residues 1-576 ##label SOO !'##cross-references EMBL:M62409; NID:g144374; PIDN:AAA98054.1; !1PID:g144375 !'##note the authors translated the codon GAA for residue 366 as Phe REFERENCE S49176 !$#authors Lau, P.C.K.; Parsons, M. !$#submission submitted to the EMBL Data Library, December 1991 !$#description Nucleotide sequence encoding the immunity and lysis proteins !1and the carboxyl terminl peptides of colicins E4 and E7. !$#accession S49179 !'##molecule_type DNA !'##residues 371-576 ##label LAU !'##cross-references EMBL:X63620; NID:g510384; PIDN:CAA45164.1; !1PID:g510385 GENETICS !$#gene cea !$#genome plasmid ColE7-K317 CLASSIFICATION #superfamily cloacin DF13 protein KEYWORDS bacteriocin; endonuclease; hydrolase; toxin SUMMARY #length 576 #molecular-weight 61349 #checksum 7865 SEQUENCE /// ENTRY NDECE2 #type complete TITLE colicin E2 (EC 3.1.21.-) - Escherichia coli plasmid ColE2-P9 ALTERNATE_NAMES colicin E2 activity protein ORGANISM #formal_name Escherichia coli DATE 17-Mar-1987 #sequence_revision 09-May-1997 #text_change 11-Jun-1999 ACCESSIONS I40687; A00789 REFERENCE I40687 !$#authors Cole, S.T.; Saint-Joanis, B.; Pugsley, A.P. !$#journal Mol. Gen. Genet. (1985) 198:465-472 !$#title Molecular characterisation of the colicin E2 operon and !1identification of its products. !$#cross-references MUID:85239907; PMID:3892228 !$#accession I40687 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-581 ##label RES !'##cross-references GB:M29885; NID:g144366; PIDN:AAA23068.1; !1PID:g144367 !'##experimental_source plasmid ColE2 REFERENCE A00789 !$#authors Lau, P.C.K.; Rowsome, R.W.; Zuker, M.; Visentin, L.P. !$#journal Nucleic Acids Res. (1984) 12:8733-8745 !$#title Comparative nucleotide sequences encoding the immunity !1proteins and the carboxyl-terminal peptides of colicins E2 !1and E3. !$#cross-references MUID:85062845; PMID:6095211 !$#accession A00789 !'##molecule_type DNA !'##residues 377-428,'RS',432-472,'R',474-503,'L',505-581 ##label LAU !'##cross-references GB:X01163; NID:g41800; PIDN:CAA25609.1; PID:g809683 !'##experimental_source plasmid ColE2 COMMENT This plasmid-coded bactericidal protein is an endonuclease !1active on both single- and double-stranded DNA but with !1undefined specificity. GENETICS !$#gene ceaB; col !$#genome plasmid CLASSIFICATION #superfamily cloacin DF13 protein KEYWORDS bacteriocin; endonuclease; hydrolase; toxin SUMMARY #length 581 #molecular-weight 61629 #checksum 3872 SEQUENCE /// ENTRY NDECE8 #type fragment TITLE colicin E8 (EC 3.1.21.-) - Escherichia coli plasmid ColE8-J (fragment) ALTERNATE_NAMES colicin E8 complex, protein A ORGANISM #formal_name Escherichia coli DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 11-Jun-1999 ACCESSIONS A28184; S01080 REFERENCE A91874 !$#authors Toba, M.; Masaki, H.; Ohta, T. !$#journal J. Bacteriol. (1988) 170:3237-3242 !$#title Colicin E8, a DNase which indicates an evolutionary !1relationship between colicins E2 and E3. !$#cross-references MUID:88257046; PMID:3290201 !$#accession A28184 !'##molecule_type DNA !'##residues 1-205 ##label TOB !'##cross-references GB:M21404; NID:g144380; PIDN:AAA23073.1; !1PID:g144381 REFERENCE S01080 !$#authors Uchimura, T.; Lau, P.C.K. !$#journal Mol. Gen. Genet. (1987) 209:489-493 !$#title Nucleotide sequences from the colicin E8 operon: homology !1with plasmid ColE2-P9. !$#cross-references MUID:88121677; PMID:3323826 !$#accession S01080 !'##molecule_type DNA !'##residues 1-205 ##label UCH !'##cross-references EMBL:X06119; NID:g41136; PIDN:CAA29491.1; !1PID:g809672 !'##note the authors translated the codon AAA for residue 75 as Ala GENETICS !$#gene col !$#genome plasmid CLASSIFICATION #superfamily cloacin DF13 protein KEYWORDS bacteriocin; endonuclease; hydrolase; toxin SUMMARY #length 205 #checksum 4496 SEQUENCE /// ENTRY PQ0032 #type fragment TITLE colicin E9 (EC 3.1.21.-) - Escherichia coli plasmid ColE9-J (fragment) ORGANISM #formal_name Escherichia coli DATE 07-Sep-1990 #sequence_revision 22-Nov-1996 #text_change 11-Jun-1999 ACCESSIONS PQ0032; S03087 REFERENCE JQ0326 !$#authors Lau, P.C.K.; Condie, J.A. !$#journal Mol. Gen. Genet. (1989) 217:269-277 !$#title Nucleotide sequences from the colicin E5, E6 and E9 operons: !1presence of a degenerate transposon-like structure in the !1ColE9-J plasmid. !$#cross-references MUID:89364708; PMID:2549375 !$#accession PQ0032 !'##molecule_type DNA !'##residues 1-205 ##label LAU !'##cross-references GB:X15858; NID:g40548; PIDN:CAA33862.1; PID:g809666 !'##experimental_source strain W3110 REFERENCE S03087 !$#authors Eaton, T.; James, R. !$#journal Nucleic Acids Res. (1989) 17:1761 !$#title Complete nucleotide sequence of the colicin E9 (cei) gene. !$#cross-references MUID:89160332; PMID:2646600 !$#accession S03087 !'##status translation not shown !'##molecule_type DNA !'##residues 123-124,'GRLYGR',132-133,'R',135-201,'L',203-205 ##label !1EAT !'##cross-references EMBL:X12591 !'##note Colicin E9 has desoxyribonuclease activity GENETICS !$#gene colE9; cei !$#genome plasmid CLASSIFICATION #superfamily cloacin DF13 protein KEYWORDS bacteriocin; endonuclease; hydrolase; toxin SUMMARY #length 205 #checksum 8271 SEQUENCE /// ENTRY PQ0030 #type fragment TITLE colicin E6 (EC 3.1.21.-) - Escherichia coli plasmid ColE6-CT14 (fragment) ORGANISM #formal_name Escherichia coli DATE 07-Sep-1990 #sequence_revision 22-Nov-1996 #text_change 11-Jun-1999 ACCESSIONS PQ0030; A43716 REFERENCE JQ0326 !$#authors Lau, P.C.K.; Condie, J.A. !$#journal Mol. Gen. Genet. (1989) 217:269-277 !$#title Nucleotide sequences from the colicin E5, E6 and E9 operons: !1presence of a degenerate transposon-like structure in the !1ColE9-J plasmid. !$#cross-references MUID:89364708; PMID:2549375 !$#accession PQ0030 !'##molecule_type DNA !'##residues 1-175 ##label LAU !'##cross-references GB:X15856; NID:g40544; PIDN:CAA33855.1; PID:g809665 !'##experimental_source strain WA802 REFERENCE A43716 !$#authors Akutsu, A.; Masaki, H.; Ohta, T. !$#journal J. Bacteriol. (1989) 171:6430-6436 !$#title Molecular structure and immunity specificity of colicin E6, !1an evolutionary intermediate between E-group colicins and !1cloacin DF13. !$#cross-references MUID:90078082; PMID:2687234 !$#accession A43716 !'##status preliminary !'##molecule_type DNA !'##residues 45-175 ##label AKU !'##cross-references GB:J01574; GB:J01575; GB:M14038; GB:X02397 GENETICS !$#gene colEb !$#genome plasmid CLASSIFICATION #superfamily cloacin DF13 protein KEYWORDS bacteriocin; endonuclease; hydrolase; toxin FEATURE !$121,137 #active_site Arg, His #status predicted SUMMARY #length 175 #checksum 1953 SEQUENCE /// ENTRY S66583 #type complete TITLE crossover junction endoribonuclease (EC 3.1.22.4) rusA - phage 82 ALTERNATE_NAMES Holliday junction resolvase; Holliday junction-specific endonuclease rusA; RUS endonuclease ORGANISM #formal_name phage 82 DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 03-Jun-2002 ACCESSIONS S66583 REFERENCE S66579 !$#authors Mahdi, A.A.; Sharples, G.J.; Mandal, T.N.; Lloyd, R.G. !$#journal J. Mol. Biol. (1996) 257:561-573 !$#title Holliday junction resolvases encoded by homologous rusA !1genes in Escherichia coli K-12 and phage 82. !$#cross-references MUID:96196428; PMID:8648624 !$#accession S66583 !'##molecule_type DNA !'##residues 1-120 ##label MAH !'##cross-references EMBL:X92588; NID:g1051111; PIDN:CAA63330.1; !1PID:g1051116 GENETICS !$#gene rusA !$#start_codon GTG CLASSIFICATION #superfamily phage 82 crossover junction !1endodeoxyribonuclease rusA KEYWORDS DNA recombination; DNA repair; endonuclease; hydrolase SUMMARY #length 120 #molecular-weight 13885 #checksum 4381 SEQUENCE /// ENTRY S66590 #type complete TITLE crossover junction endoribonuclease (EC 3.1.22.4) - Escherichia coli (strain K-12) cryptic lambdoid prophage DLP12 ALTERNATE_NAMES Holliday junction resolvase; Holliday junction-specific endonuclease rusA; RUS endonuclease ORGANISM #formal_name Escherichia coli DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 03-Jun-2002 ACCESSIONS S66590; S52058; D64787 REFERENCE S66579 !$#authors Mahdi, A.A.; Sharples, G.J.; Mandal, T.N.; Lloyd, R.G. !$#journal J. Mol. Biol. (1996) 257:561-573 !$#title Holliday junction resolvases encoded by homologous rusA !1genes in Escherichia coli K-12 and phage 82. !$#cross-references MUID:96196428; PMID:8648624 !$#accession S66590 !'##molecule_type DNA !'##residues 1-120 ##label MAH !'##cross-references EMBL:X92587; NID:g1051136; PIDN:CAA63321.1; !1PID:g1051141 REFERENCE S52058 !$#authors Sharples, G.J.; Chan, S.N.; Mahdi, A.A.; Whitby, M.C.; !1Lloyd, R.G. !$#journal EMBO J. (1994) 13:6133-6142 !$#title Processing of intermediates in recombination and DNA repair: !1identification of a new endonuclease that specifically !1cleaves Holliday junctions. !$#cross-references MUID:95112824; PMID:7813450 !$#accession S52058 !'##molecule_type protein !'##residues 1-9 ##label SHA REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64787 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-120 ##label BLAT !'##cross-references GB:AE000160; GB:U00096; NID:g1786751; !1PIDN:AAC73651.1; PID:g1786762; UWGP:b0550 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene rusA !$#map_position 12 min !$#genome prophage !$#start_codon GTG CLASSIFICATION #superfamily phage 82 crossover junction !1endodeoxyribonuclease rusA KEYWORDS DNA recombination; DNA repair; endonuclease; hydrolase SUMMARY #length 120 #molecular-weight 13846 #checksum 3907 SEQUENCE /// ENTRY NREC3 #type complete TITLE ribonuclease III (EC 3.1.26.3) rnc - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Sep-1987 #sequence_revision 24-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS F65034; A26023; A24022 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65034 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-226 ##label BLAT !'##cross-references GB:AE000343; GB:U00096; NID:g2367139; !1PIDN:AAC75620.1; PID:g1788920; UWGP:b2567 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A26023 !$#authors Nashimoto, H.; Uchida, H. !$#journal Mol. Gen. Genet. (1985) 201:25-29 !$#title DNA sequencing of the Escherichia coli ribonuclease III gene !1and its mutations. !$#cross-references MUID:86039802; PMID:3903434 !$#accession A26023 !'##molecule_type DNA !'##residues 1-226 ##label NAS !'##cross-references GB:D64044; NID:g987635; PIDN:BAA10914.1; !1PID:g987642 !'##note 44-Asp and 211-Val were also found REFERENCE A24022 !$#authors March, P.E.; Ahnn, J.; Inouye, M. !$#journal Nucleic Acids Res. (1985) 13:4677-4685 !$#title The DNA sequence of the gene (rnc) encoding ribonuclease III !1of Escherichia coli. !$#cross-references MUID:85269601; PMID:3895158 !$#accession A24022 !'##molecule_type DNA !'##residues 1-167,'P',195,'AAADLSGSPGTWSKRTIRNLLSTARSV',196-226 ##label !1MAR !'##cross-references GB:X02673; NID:g42765; PIDN:CAA26504.1; PID:g42766 GENETICS !$#gene rnc CLASSIFICATION #superfamily ribonuclease III; double-stranded RNA-binding !1repeat homology KEYWORDS hydrolase; RNA processing FEATURE !$152-226 #domain double-stranded RNA-binding repeat homology !8#label DSR SUMMARY #length 226 #molecular-weight 25550 #checksum 1782 SEQUENCE /// ENTRY NRECH #type complete TITLE ribonuclease H (EC 3.1.26.4) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 18-Apr-1984 #sequence_revision 18-Apr-1984 #text_change 01-Mar-2002 ACCESSIONS A92401; A93979; S13170; B24257; I54847; H64745; A00793 REFERENCE A92401 !$#authors Kanaya, S.; Crouch, R.J. !$#journal J. Biol. Chem. (1983) 258:1276-1281 !$#title DNA sequence of the gene coding for Escherichia coli !1ribonuclease H. !$#cross-references MUID:83108846; PMID:6296074 !$#accession A92401 !'##molecule_type DNA !'##residues 1-155 ##label KAN !'##cross-references GB:K00552; GB:J01676; GB:V00337; NID:g147676; !1PID:g147677 REFERENCE A93979 !$#authors Maki, H.; Horiuchi, T.; Sekiguchi, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:7137-7141 !$#title Structure and expression of the dnaQ mutator and the RNas H !1genes of Escherichia coli: overlap of the promoter regions. !$#cross-references MUID:84070781; PMID:6316347 !$#accession A93979 !'##molecule_type DNA !'##residues 1-155 ##label MAK !'##cross-references GB:K00985; GB:M30201; NID:g147678; PIDN:AAA24565.1; !1PID:g147680 REFERENCE S13170 !$#authors Kanaya, S.; Kimura, S.; Katsuda, C.; Ikehara, M. !$#journal Biochem. J. (1990) 271:59-66 !$#title Role of cysteine residues in ribonuclease H from Escherichia !1coli. !$#cross-references MUID:91024947; PMID:2171503 !$#accession S13170 !'##molecule_type DNA !'##residues 1-155 ##label KA2 REFERENCE A24257 !$#authors Cox, E.C.; Horner, D.L. !$#journal J. Mol. Biol. (1986) 190:113-117 !$#title DNA sequence and coding properties of mutD(dnaQ) a dominant !1Escherichia coli mutator gene. !$#cross-references MUID:87060973; PMID:3023634 !$#accession B24257 !'##molecule_type DNA !'##residues 1-155 ##label COX !'##cross-references GB:X04027; NID:g42061; PIDN:CAA27660.1; PID:g42062 REFERENCE I54847 !$#authors Kanaya, S.; Crouch, R.J. !$#journal J. Bacteriol. (1983) 154:1021-1026 !$#title Low levels of RNase H activity in Escherichia coli FB2 rnh !1result from a single-base change in the structural gene of !1RNase H. !$#cross-references MUID:83185998; PMID:6302075 !$#accession I54847 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-155 ##label RES !'##cross-references EMBL:V00337; NID:g42776; PIDN:CAA23620.1; !1PID:g42777 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64745 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-155 ##label BLAT !'##cross-references GB:AE000130; GB:U00096; NID:g1786402; !1PIDN:AAC73319.1; PID:g1786408; UWGP:b0214 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene rnhA; rnh !$#map_position 5 min FUNCTION !$#description an endonulease that degrades the RNA of RNA-DNA hybrids !1specifically CLASSIFICATION #superfamily ribonuclease H KEYWORDS hydrolase SUMMARY #length 155 #molecular-weight 17597 #checksum 7235 SEQUENCE /// ENTRY QQECBE #type complete TITLE ribonuclease H (EC 3.1.26.4) II - Escherichia coli (strain K-12) ALTERNATE_NAMES ribonuclease HII; RNase HII ORGANISM #formal_name Escherichia coli DATE 31-Dec-1988 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS G64742; B28390; A36485 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64742 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-198 ##label BLAT !'##cross-references GB:AE000127; GB:U00096; NID:g1786370; !1PIDN:AAC73294.1; PID:g1786380; UWGP:b0183 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A91855 !$#authors Tomasiewicz, H.G.; McHenry, C.S. !$#journal J. Bacteriol. (1987) 169:5735-5744 !$#title Sequence analysis of the Escherichia coli dnaE gene. !$#cross-references MUID:88058791; PMID:3316192 !$#accession B28390 !'##molecule_type DNA !'##residues 1-195,'TCVLILVSRLSKPESEDV' ##label TOM !'##cross-references GB:D83536; NID:g4902908; PIDN:BAA77858.1; !1PID:g4902924 REFERENCE A36485 !$#authors Itaya, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:8587-8591 !$#title Isolation and characterization of a second RNase H (RNase !1HII) of Escherichia coli K-12 encoded by the rnhB gene. !$#cross-references MUID:91046040; PMID:2172991 !$#accession A36485 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-195,'TCVLILVSRLSKPESEDV' ##label ITA GENETICS !$#gene rnhB !$#map_position 4 min FUNCTION !$#description an endonulease that degrades the RNA of RNA-DNA hybrids !1specifically CLASSIFICATION #superfamily ribonuclease HII KEYWORDS hydrolase SUMMARY #length 198 #molecular-weight 21526 #checksum 866 SEQUENCE /// ENTRY NRECP #type complete TITLE ribonuclease P (EC 3.1.26.5) protein component - Escherichia coli (strain K-12) ALTERNATE_NAMES protein C5 ORGANISM #formal_name Escherichia coli DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 01-Mar-2002 ACCESSIONS A00794; D21915; A65173 REFERENCE A00794 !$#authors Hansen, F.G.; Hansen, E.B.; Atlung, T. !$#journal Gene (1985) 38:85-93 !$#title Physical mapping and nucleotide sequence of the rnpA gene !1that encodes the protein component of ribonuclease P in !1Escherichia coli. !$#cross-references MUID:86056995; PMID:2415431 !$#contents pBR322 !$#accession A00794 !'##molecule_type DNA !'##residues 1-119 ##label HAN !'##cross-references GB:M11056; NID:g147681; PIDN:AAA24567.1; !1PID:g147683 REFERENCE A21915 !$#authors Hansen, F.G.; Hansen, E.B.; Atlung, T. !$#journal EMBO J. (1982) 1:1043-1048 !$#title The nucleotide sequence of the dnaA gene promoter and of the !1adjacent rpmH gene, coding for the ribosomal protein L34, of !1Escherichia coli. !$#cross-references MUID:84236082; PMID:6329723 !$#accession D21915 !'##molecule_type DNA !'##residues 1-69 ##label HA2 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65173 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-119 ##label BLAT !'##cross-references GB:AE000447; GB:U00096; NID:g2367266; !1PIDN:AAC76727.1; PID:g1790139; UWGP:b3704 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene rnpA !$#map_position 83 min !$#start_codon GTG COMPLEX ribonuclease P consists of the M1 RNA moiety and the protein !1component; both are necessary for full enzymatic activity; !1however, it is the RNA that carries the catalytic site FUNCTION !$#description ribonuclease P generates mature tRNA molecules by cleaving !1their 5 ends; it can cleave also the 4.5S RNA CLASSIFICATION #superfamily ribonuclease P, protein component KEYWORDS endonuclease; hydrolase; tRNA processing SUMMARY #length 119 #molecular-weight 13789 #checksum 3979 SEQUENCE /// ENTRY JQ0731 #type complete TITLE ribonuclease P (EC 3.1.26.5) protein component - Proteus mirabilis ORGANISM #formal_name Proteus mirabilis DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 11-Jun-1999 ACCESSIONS JQ0731 REFERENCE JQ0729 !$#authors Skovgaard, O. !$#journal Gene (1990) 93:27-34 !$#title Nucleotide sequence of a Proteus mirabilis DNA fragment !1homologous to the 60K-rnpA-rpmH-dnaA-dnaN-recF-gyrB region !1of Escherichia coli. !$#cross-references MUID:91033012; PMID:2172087 !$#accession JQ0731 !'##molecule_type DNA !'##residues 1-119 ##label SKO !'##cross-references GB:M58352; GB:M31295; NID:g150873; PIDN:AAA83956.1; !1PID:g150876 !'##experimental_source strain LM1509 COMMENT Ribonuclease P consists of the M1 RNA moiety and the protein !1component. Both are necessary for full enzymatic activity. !1However, it is the RNA that carries the catalytic site. COMMENT Ribonuclease P generates mature tRNA molecules by cleaving !1their 5' ends. It can also cleave the 4.5S RNA. GENETICS !$#gene rnpA !$#start_codon GTG CLASSIFICATION #superfamily ribonuclease P, protein component KEYWORDS endonuclease; hydrolase; tRNA processing SUMMARY #length 119 #molecular-weight 14059 #checksum 4484 SEQUENCE /// ENTRY JC1155 #type complete TITLE ribonuclease P (EC 3.1.26.5) protein component - Buchnera aphidicola ORGANISM #formal_name Buchnera aphidicola DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 11-Jun-1999 ACCESSIONS JC1155 REFERENCE JC1154 !$#authors Lai, C.Y.; Baumann, P. !$#journal Gene (1992) 113:175-181 !$#title Genetic analysis of an aphid endosymbiont DNA fragment !1homologous to the rnpA-rpmH-dnaA-dnaN-gyrB region of !1eubacteria. !$#cross-references MUID:92241666; PMID:1572539 !$#accession JC1155 !'##molecule_type DNA !'##residues 1-114 ##label LAI !'##cross-references GB:M80817; NID:g144144; PIDN:AAA73147.1; !1PID:g144147 COMMENT Ribonuclease P consists of the M1 RNA moiety and the protein !1component. Both are necessary for full enzymatic activity. !1However, it is the RNA that carries the catalytic site. COMMENT Ribonuclease P generates mature tRNA molecules by cleaving !1their 5' ends. It can also cleave the 4.5S RNA. GENETICS !$#gene rnpA !$#start_codon GTG CLASSIFICATION #superfamily ribonuclease P, protein component KEYWORDS endonuclease; hydrolase; tRNA processing SUMMARY #length 114 #molecular-weight 13784 #checksum 6596 SEQUENCE /// ENTRY S27311 #type complete TITLE ribonuclease E (EC 3.1.4.-) - Escherichia coli (strain K-12) ALTERNATE_NAMES cell shape-determining protein; message stability-altering protein; RNase E ORGANISM #formal_name Escherichia coli DATE 30-Sep-1993 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS A64852; S45572; S27311; A23747; JG0009; A40661; S13127; !1S25116 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64852 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1061 ##label BLAT !'##cross-references GB:AE000209; GB:U00096; NID:g1787322; !1PIDN:AAC74168.1; PID:g1787325; UWGP:b1084 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S45572 !$#authors Casaregola, S.; Jacq, A.; Laoudj, D.; Mcgurk, G.; Margarson, !1S.; Tempete, M.; Norris, V.; Holland, I.B. !$#journal J. Mol. Biol. (1994) 238:867 !$#title Cloning and analysis of the entire Escherichia coli ams !1gene. !$#cross-references MUID:94238701; PMID:8182758 !$#accession S45572 !'##molecule_type DNA !'##residues 1001-1061 ##label CAS REFERENCE S27311 !$#authors Casaregola, S.; Jacq, A.; Laoudj, D.; McGurk, G.; Margarson, !1S.; Tempete, M.; Norris, V.; Holland, I.B. !$#journal J. Mol. Biol. (1992) 228:30-40 !$#title Cloning and analysis of the entire Escherichia coli ams !1gene. ams is identical to hmp1 and encodes a 114 kDa protein !1that migrates as a 180 kDa protein. !$#cross-references MUID:93078265; PMID:1447789 !$#accession S27311 !'##molecule_type DNA !'##residues 1-486,'V',488-563,'R',565-783,'K',785-904,'R',906-1000, !11060-1061,'ITTLPANDARSSTGICSGATASQ' ##label CA2 !'##cross-references EMBL:X67470; NID:g49115; PIDN:CAA47818.1; !1PID:g49116 !'##experimental_source strain MC4100 REFERENCE A23747 !$#authors Claverie-Martin, F.; Diaz-Torres, M.R.; Yancey, S.D.; !1Kushner, S.R. !$#journal J. Biol. Chem. (1991) 266:2843-2851 !$#title Analysis of the altered mRNA stability (ams) gene from !1Escherichia coli. Nucleotide sequence, transcriptional !1analysis, and homology of its product to MRP3, a !1mitochondrial ribosomal protein from Neurospora crassa. !$#cross-references MUID:91131576; PMID:1704367 !$#accession A23747 !'##status preliminary !'##molecule_type DNA !'##residues 1-389,'H',391-486,'V',488-795,'SF',798,1009,'LASS', !11014-1015,'RKWSASSSLS' ##label CLA !'##cross-references GB:M36288; GB:M62747; NID:g145271; PIDN:AAA23443.1; !1PID:g145273 !'##experimental_source strain K-12 !'##note this sequence has been proven to be erroneous in Ref:S27311 REFERENCE JG0009 !$#authors Chauhan, A.K.; Miczak, A.; Taraseviciene, L.; Apirion, D. !$#journal Nucleic Acids Res. (1991) 19:125-129 !$#title Sequencing and expression of the rne gene of Escherichia !1coli. !$#cross-references MUID:91187608; PMID:2011493 !$#accession JG0009 !'##status preliminary !'##molecule_type DNA !'##residues 1-258,'N',260-529,'QPLPCR','MC',719,'LR',722-726,'LPRLL' !1##label CHA !'##cross-references EMBL:X54309 !'##experimental_source strain K-12 !'##note this sequence has been proven to be erroneous in Ref:S27311 REFERENCE A40661 !$#authors McDowall, K.J.; Hernandez, R.G.; Lin-Chao, S.; Cohen, S.N. !$#journal J. Bacteriol. (1993) 175:4245-4249 !$#title The ams-1 and rne-3071 temperature-sensitive mutations in !1the ams gene are in close proximity to each other and cause !1substitutions within a domain that resembles a product of !1the Escherichia coli mre locus. !$#cross-references MUID:93308106; PMID:8320240 !$#accession A40661 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-486,'V',488-489 ##label MCD !'##note sequence extracted from NCBI backbone (NCBIP:134520) GENETICS !$#gene rne; ams; hmp1 !$#map_position 24 min FUNCTION !$#description cleaves RNA endonucleolytically in AU-rich single-strand !1regions; RNA-binding activity; interacts with polynucleotide !1phosphorylase and other proteins implicated in processing !1and degradation of RNA !$#note autoregulation CLASSIFICATION #superfamily ribonuclease E KEYWORDS endonuclease; P-loop; phosphoric diester hydrolase; RNA !1binding; transmembrane protein FEATURE !$113-131 #domain transmembrane #status predicted #label TMM\ !$169-176 #region nucleotide-binding motif A (P-loop) #status !8atypical\ !$524-568 #region proline-rich\ !$743-778 #region proline-rich SUMMARY #length 1061 #molecular-weight 118196 #checksum 5236 SEQUENCE /// ENTRY E64066 #type complete TITLE ribonuclease E (EC 3.1.4.-) - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 18-Aug-1995 #sequence_revision 05-Jan-1996 #text_change 31-Mar-2000 ACCESSIONS E64066 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession E64066 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-951 ##label TIGR !'##cross-references GB:U32724; GB:L42023; NID:g1573378; !1PIDN:AAC22072.1; PID:g1573386; TIGR:HI0413 GENETICS !$#start_codon GTG FUNCTION !$#description cleaves RNA endonucleolytically in AU-rich single-strand !1regions; RNA-binding activity; interacts with polynucleotide !1phosphorylase and other proteins implicated in processing !1and degradation of RNA !$#note autoregulation CLASSIFICATION #superfamily ribonuclease E KEYWORDS endonuclease; P-loop; phosphoric diester hydrolase; RNA !1binding; transmembrane protein FEATURE !$129-147 #domain transmembrane #status predicted #label TMM\ !$185-192 #region nucleotide-binding motif A (P-loop) #status !8atypical SUMMARY #length 951 #molecular-weight 108712 #checksum 9833 SEQUENCE /// ENTRY NRBSN #type complete TITLE ribonuclease (EC 3.1.27.-) precursor - Bacillus amyloliquefaciens ALTERNATE_NAMES barnase; G specific endonuclease ORGANISM #formal_name Bacillus amyloliquefaciens DATE 24-Apr-1984 #sequence_revision 26-Jan-1996 #text_change 20-Apr-2001 ACCESSIONS A24038; A32060; S01372; A00795 REFERENCE A24038 !$#authors Paddon, C.J.; Hartley, R.W. !$#journal Gene (1985) 40:231-239 !$#title Cloning, sequencing and transcription of an inactivated copy !1of Bacillus amyloliquefaciens extracellular ribonuclease !1(barnase). !$#cross-references MUID:86165864; PMID:3007290 !$#accession A24038 !'##molecule_type DNA !'##residues 'MMKMEGIAL',2-149 ##label PAD !'##note the initiation site has been revised in A32060 REFERENCE A32060 !$#authors Paddon, C.J.; Vasantha, N.; Hartley, R.W. !$#journal J. Bacteriol. (1989) 171:1185-1187 !$#title Translation and processing of Bacillus amyloliquefaciens !1extracellular RNase. !$#cross-references MUID:89123119; PMID:2914867 !$#accession A32060 !'##molecule_type DNA !'##residues 1-45 ##label PA2 !'##note the authors translated the codon TGT for residue 11 as Lys; !1site-directed mutagenesis studies of this protein expressed !1in Bacillus subtilis suggest that translation begins with !1fMet for codon UUG at position 1 !'##note cleavage at 35-36 produces a form referred to as probarnase II REFERENCE S01372 !$#authors Hartley, R.W. !$#journal J. Mol. Biol. (1988) 202:913-915 !$#title Barnase and barstar. Expression of its cloned inhibitor !1permits expression of a cloned ribonuclease. !$#cross-references MUID:89012012; PMID:3050134 !$#accession S01372 !'##molecule_type DNA !'##residues 40-149 ##label HAR !'##cross-references EMBL:X12871; NID:g39309; PIDN:CAA31365.1; !1PID:g39310 REFERENCE A00795 !$#authors Hartley, R.W.; Barker, E.A. !$#journal Nature New Biol. (1972) 235:15-16 !$#title Amino-acid sequence of extracellular ribonuclease (Barnase) !1of Bacillus amyloliquefaciens. !$#cross-references MUID:72164019; PMID:4553460 !$#accession A00795 !'##molecule_type protein !'##residues 40-60,'ND',63-149 ##label HA2 REFERENCE A44743 !$#authors Baudet, S.; Janin, J. !$#journal J. Mol. Biol. (1991) 219:123-132 !$#title Crystal structure of a barnase-d(GpC) complex at 1.9 !1angstrom resolution. !$#cross-references MUID:91218173; PMID:2023257 !$#contents annotation; X-ray crystallography, 1.9 angstroms !$#note recombinant form cloned and expressed in Escherichia coli; !1modeled with sequence of A00795 GENETICS !$#start_codon UUG CLASSIFICATION #superfamily ribonuclease Sa KEYWORDS hydrolase FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-35 #domain propeptide I #status predicted #label PRO1\ !$36-39 #domain propeptide II #status predicted #label PRO2\ !$40-149 #product ribonuclease #status experimental #label !8MAT\ !$112,141 #active_site Glu, His #status predicted\ !$122,126 #binding_site substrate (Arg) #status predicted SUMMARY #length 149 #molecular-weight 16599 #checksum 500 SEQUENCE /// ENTRY NRBSI #type complete TITLE ribonuclease (EC 3.1.-.-) - Bacillus "intermedius" ORGANISM #formal_name Bacillus "intermedius" DATE 30-Nov-1980 #sequence_revision 30-Nov-1980 #text_change 04-Dec-1994 ACCESSIONS A00796 REFERENCE A00796 !$#authors Aphanasenko, G.A.; Dudkin, S.M.; Kaminir, L.B.; !1Leshchinskaya, I.B.; Severin, E.S. !$#journal FEBS Lett. (1979) 97:77-80 !$#title Primary structure of ribonuclease from Bacillus intermedius !17P. !$#cross-references MUID:79107452; PMID:761620 !$#accession A00796 !'##molecule_type protein !'##residues 1-109 ##label APH !'##experimental_source strain 7P COMMENT This enzyme is a puryloribonuclease. CLASSIFICATION #superfamily ribonuclease Sa KEYWORDS hydrolase SUMMARY #length 109 #molecular-weight 12212 #checksum 2828 SEQUENCE /// ENTRY NRSMTE #type complete TITLE ribonuclease Sa (EC 3.1.27.-) - Saccharopolyspora erythraea ALTERNATE_NAMES guanyloribonuclease; ribonuclease St ORGANISM #formal_name Saccharopolyspora erythraea DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 06-Dec-1996 ACCESSIONS A91429; A00797 REFERENCE A91429 !$#authors Yoshida, N.; Sasaki, A.; Rashid, M.A.; Otsuka, H. !$#journal FEBS Lett. (1976) 64:122-125 !$#title The amino acid sequence of ribonuclease St. !$#cross-references MUID:76188019; PMID:1269746 !$#accession A91429 !'##molecule_type protein !'##residues 1-25,'G',26-101 ##label YOS REFERENCE A94589 !$#authors Yoshida, N.; Sasaki, A.; Rashid, M.A.; Otsuka, H. !$#submission submitted to the Atlas, June 1977 !$#contents annotation; revision !$#note a Gly following residue 25 has been deleted from the !1published sequence CLASSIFICATION #superfamily ribonuclease Sa KEYWORDS extracellular protein; hydrolase FEATURE !$4-54 #disulfide_bonds #status experimental SUMMARY #length 101 #molecular-weight 11354 #checksum 9588 SEQUENCE /// ENTRY NRSM #type complete TITLE ribonuclease Sa (EC 3.1.27.-) - Streptomyces aureofaciens ALTERNATE_NAMES guanyloribonuclease ORGANISM #formal_name Streptomyces aureofaciens DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 20-Apr-2001 ACCESSIONS A25655; S08339; S03792 REFERENCE A25655 !$#authors Shlyapnikov, S.V.; Both, V.; Kulikov, V.A.; Dementiev, A.A.; !1Sevcik, J.; Zelinka, J. !$#journal FEBS Lett. (1986) 209:335-339 !$#title Amino acid sequence determination of guanyl-specific !1ribonuclease Sa from Streptomyces aureofaciens. !$#cross-references MUID:87080784; PMID:3098582 !$#accession A25655 !'##molecule_type protein !'##residues 1-96 ##label SHL1 REFERENCE S08339 !$#authors Shlyapnikov, S.V.; Both, V.; Kulikov, V.A.; Dementiev, A.A.; !1Zelinka, J. !$#journal Sov. J. Bioorg. Chem. (1987) 13:391-402 !$#title Extracellular guanyl-specific ribonuclease Sa from !1actinomycete Streptomyces aureofaciens. Primary structure !1and homology with ribonucleases of bacteria and fungi. !$#accession S08339 !'##molecule_type protein !'##residues 1-96 ##label SHL2 !'##note this paper is a translation of the Russian paper published in !1Bioorg. Khim. (1987) 13: 760-772 REFERENCE A44669 !$#authors Sevcik, J.; Dodson, E.J.; Dodson, G.G. !$#journal Acta Crystallogr. B (1991) 47:240 !$#title Determination and restrained least-squares refinement of the !1crystal structures of ribonuclease Sa and its complex with !13'-guanylic acid at 1.8 angstroms resolution. !$#cross-references MUID:92000408; PMID:1654932 !$#contents annotation; X-ray crystallography, 1.8 angstroms CLASSIFICATION #superfamily ribonuclease Sa KEYWORDS extracellular protein; hydrolase FEATURE !$7-72 #disulfide_bonds #status predicted SUMMARY #length 96 #molecular-weight 10577 #checksum 264 SEQUENCE /// ENTRY JC1287 #type complete TITLE ribonuclease Sa (EC 3.1.27.-) precursor - Streptomyces aureofaciens (strain CCM3239) ALTERNATE_NAMES guanyloribonuclease; ribonuclease Sa3 ORGANISM #formal_name Streptomyces aureofaciens DATE 30-Sep-1993 #sequence_revision 02-Dec-1994 #text_change 06-Dec-1996 ACCESSIONS JC1287 REFERENCE JC1287 !$#authors Homerova, D.; Hollaenderova, Z.; Kormanec, J.; Sevcik, J. !$#journal Gene (1992) 119:147-148 !$#title Cloning and sequencing of the gene encoding a ribonuclease !1from Streptomyces aureofaciens CCM3239. !$#cross-references MUID:93012968; PMID:1398084 !$#accession JC1287 !'##molecule_type DNA !'##residues 1-141 ##label HOM !'##cross-references GB:M82920 !'##experimental_source strain CCM3239 CLASSIFICATION #superfamily ribonuclease Sa KEYWORDS extracellular protein; hydrolase FEATURE !$1-28 #domain (or 1-34) signal sequence #status predicted !8#label SIG\ !$29-141 #product (or 35-141) ribonuclease #status predicted !8#label MAT SUMMARY #length 141 #molecular-weight 14819 #checksum 1055 SEQUENCE /// ENTRY NRAST1 #type complete TITLE ribonuclease T1 (EC 3.1.27.3) precursor - Aspergillus oryzae ALTERNATE_NAMES guanyloribonuclease ORGANISM #formal_name Aspergillus oryzae DATE 24-Apr-1984 #sequence_revision 06-Dec-1996 #text_change 16-Jun-2000 ACCESSIONS JC4325; A24129; S02030; A00798 REFERENCE JC4325 !$#authors Fujii, T.; Yamaoka, H.; Gomi, K.; Kitamoto, K.; Kumagai, C. !$#journal Biosci. Biotechnol. Biochem. (1995) 59:1869-1874 !$#title Cloning and nucleotide sequence of the ribonuclease T1 gene !1(rntA) from Aspergillus oryzae and its expression in !1Saccharomyces cerevisiae and Aspergillus oryzae. !$#cross-references MUID:96068932; PMID:8534978 !$#accession JC4325 !'##molecule_type mRNA !'##residues 1-130 ##label FUJ !'##cross-references DDBJ:D28341; NID:g460685; PIDN:BAA05707.1; !1PID:g541652 !'##experimental_source RIB40 REFERENCE A24129 !$#authors Takahashi, K. !$#journal J. Biochem. (1985) 98:815-817 !$#title A revision and confirmation of the amino acid sequence of !1ribonuclease T1. !$#cross-references MUID:86111687; PMID:3936843 !$#accession A24129 !'##molecule_type protein !'##residues 27-130 ##label TAK !'##note revision of NRAST1 (residues 97-99) REFERENCE S02030 !$#authors Hoffmann, E.; Rueterjans, H. !$#journal Eur. J. Biochem. (1988) 177:539-560 !$#title Two-dimensional (1)H-NMR investigation of ribonuclease T(1). !1Resonance assignments, secondary and low-resolution tertiary !1structures of ribonuclease T(1). !$#cross-references MUID:89064808; PMID:3143569 !$#accession S02030 !'##molecule_type protein !'##residues 27-50,'K',52-130 ##label HOF REFERENCE A91927 !$#authors Takahashi, K. !$#journal J. Biochem. (1971) 70:945-960 !$#title The structure and function of ribonuclease T-1. XVII. !1Isolation and amino acid sequences of papain and subtilisin !1peptides from ribonuclease T-1 - the complete covalent !1structure of ribonuclease T-1. !$#cross-references MUID:72150415; PMID:5144355 !$#contents disulfide bonds !$#accession A00798 !'##molecule_type protein !'##residues 27-96,'PGS',100-130 ##label TA2 !'##note this is the final paper in a series REFERENCE A92032 !$#authors Takahashi, K.; Stein, W.H.; Moore, S. !$#journal J. Biol. Chem. (1967) 242:4682-4690 !$#title The identification of a glutamic acid residue as part of the !1active site of ribonuclease T-1. !$#cross-references MUID:68054788; PMID:6061414 !$#contents annotation; active site REFERENCE A91926 !$#authors Takahashi, K. !$#journal J. Biochem. (1971) 69:331-338 !$#title The structure and function of ribonuclese T-1. XII. Further !1studies on rose bengal-catalyzed photooxidation of !1ribonuclease T-1- identification of a critical histidine !1residue. !$#cross-references MUID:71155511; PMID:5550972 !$#contents annotation; active site GENETICS !$#gene rntA FUNCTION !$#description cleaves single-stranded RNA specifically after guanosineand !1releases oligonucleotides with guanosine at the 3'-phosphate !1termini CLASSIFICATION #superfamily ribonuclease T1 KEYWORDS endonuclease; hydrolase FEATURE !$1-5 #domain signal sequence #status predicted #label SIG\ !$6-26 #domain propeptide #status predicted #label PRS\ !$27-130 #product ribonuclease T1 #status predicted #label !8MAT\ !$28-36,32-129 #disulfide_bonds #status experimental\ !$64,66,84,103,118 #active_site Tyr, His, Glu, Arg, His #status !8experimental SUMMARY #length 130 #molecular-weight 13960 #checksum 3101 SEQUENCE /// ENTRY NRASTC #type complete TITLE ribonuclease T1 (EC 3.1.27.3) - Aspergillus clavatus ALTERNATE_NAMES guanyloribonuclease; ribonuclease C2 ORGANISM #formal_name Aspergillus clavatus DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 31-Dec-1993 ACCESSIONS A00799 REFERENCE A00799 !$#authors Bezborodova, S.I.; Khodova, O.M.; Stepanov, V.M. !$#journal FEBS Lett. (1983) 159:256-258 !$#title The complete amino acid sequence of ribonuclease C-2 from !1Aspergillus clavatus. !$#accession A00799 !'##molecule_type protein !'##residues 1-104 ##label BEZ CLASSIFICATION #superfamily ribonuclease T1 KEYWORDS endonuclease; hydrolase FEATURE !$2-10,6-103 #disulfide_bonds #status predicted\ !$38,40,58,77,92 #active_site Tyr, His, Glu, Arg, His #status !8predicted SUMMARY #length 104 #molecular-weight 11087 #checksum 4146 SEQUENCE /// ENTRY NRASTP #type complete TITLE ribonuclease T1 (EC 3.1.27.3) - Aspergillus phoenicis ALTERNATE_NAMES guanyloribonuclease; ribonuclease Ms ORGANISM #formal_name Aspergillus phoenicis DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 31-Dec-1996 ACCESSIONS A00800 REFERENCE A00800 !$#authors Watanabe, H.; Ohgi, K.; Irie, M. !$#journal J. Biochem. (1982) 91:1495-1509 !$#title Primary structure of a minor ribonuclease from Aspergillus !1saitoi. !$#cross-references MUID:82239267; PMID:7096302 !$#accession A00800 !'##molecule_type protein !'##residues 1-106 ##label WAT !'##note the source was designated as Aspergillus saitoi CLASSIFICATION #superfamily ribonuclease T1 KEYWORDS endonuclease; extracellular protein; hydrolase FEATURE !$3-11,7-103 #disulfide_bonds #status experimental\ !$37,39,57,76,91 #active_site Tyr, His, Glu, Arg, His #status !8predicted SUMMARY #length 106 #molecular-weight 11374 #checksum 7839 SEQUENCE /// ENTRY NRPLTB #type complete TITLE ribonuclease T1 (EC 3.1.27.3) - Penicillium brevicompactum ALTERNATE_NAMES guanyloribonuclease ORGANISM #formal_name Penicillium brevicompactum DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 06-Dec-1996 ACCESSIONS A23350 REFERENCE A23350 !$#authors Shlyapnikov, S.V.; Yakovlev, G.I.; Kulikov, V.A. !$#journal Dokl. Akad. Nauk SSSR (1985) 281:226-229 !$#title Analysis of the structures of guanyl-specific ribonucleases !1of fungi: determination of the amino acid sequence and !1prediction of the secondary structure of ribonuclease from !1Penicillium brevicompactum. !$#cross-references MUID:85203410; PMID:3922722 !$#accession A23350 !'##molecule_type protein !'##residues 1-102 ##label SHL CLASSIFICATION #superfamily ribonuclease T1 KEYWORDS endonuclease; extracellular protein; hydrolase FEATURE !$2-10,6-101 #disulfide_bonds #status predicted\ !$36,38,56,75,90 #active_site Tyr, His, Glu, Arg, His #status !8predicted SUMMARY #length 102 #molecular-weight 10803 #checksum 5839 SEQUENCE /// ENTRY NRNCT1 #type complete TITLE ribonuclease T1 (EC 3.1.27.3) - Neurospora crassa ALTERNATE_NAMES ribonuclease N1 ORGANISM #formal_name Neurospora crassa DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 06-Dec-1996 ACCESSIONS JT0301 REFERENCE JT0301 !$#authors Takahashi, K. !$#journal J. Biochem. (1988) 104:375-382 !$#title The amino acid sequence of ribonuclease N1, a !1guanine-specific ribonuclease from the fungus Neurospora !1crassa. !$#cross-references MUID:89197823; PMID:2977130 !$#accession JT0301 !'##molecule_type protein !'##residues 1-104 ##label TAK CLASSIFICATION #superfamily ribonuclease T1 KEYWORDS endonuclease; extracellular protein; hydrolase FEATURE !$2-10,6-103 #disulfide_bonds #status experimental\ !$38,40,58,77,92 #active_site Tyr, His, Glu, Arg, His #status !8predicted SUMMARY #length 104 #molecular-weight 11178 #checksum 2803 SEQUENCE /// ENTRY NRUSU2 #type complete TITLE riblonuclease U2 (EC 3.1.27.4) [validated] - smut fungus (Ustilago sphaerogena) ALTERNATE_NAMES ribonuclease U2 isoform A; ribonuclease U2 isoform B ORGANISM #formal_name Ustilago sphaerogena DATE 24-Apr-1984 #sequence_revision 17-Sep-1997 #text_change 03-Jun-2002 ACCESSIONS PC4081; A26071; A00801 REFERENCE PC4081 !$#authors Kanaya, S.; Uchida, T. !$#journal J. Biochem. (1995) 118:681-682 !$#title Revised sequence of ribonuclease U2 in the substrate-binding !1region. !$#cross-references MUID:96157700; PMID:8576077 !$#accession PC4081 !'##molecule_type protein !'##residues 38-65 ##label KAN REFERENCE A26071 !$#authors Kanaya, S.; Uchida, T. !$#journal Biochem. J. (1986) 240:163-170 !$#title Comparison of primary structures of ribonuclease U2 !1isoforms. !$#cross-references MUID:87156566; PMID:3827836 !$#accession A26071 !'##molecule_type protein !'##residues 1-48,'DQ',51-114 ##label KA2 REFERENCE A90280 !$#authors Sato, S.; Uchida, T. !$#journal Biochem. J. (1975) 145:353-360 !$#title The amino acid sequence of ribonuclease U-2 from Ustilago !1sphaerogena. !$#cross-references MUID:75224613; PMID:1156364 !$#accession A00801 !'##molecule_type protein !'##residues 1,'N',3-4,'E',6-31,'RP',34,'G',37-48,'DQ',51-56,'P',58,'S', !160-114 ##label SAT REFERENCE A91936 !$#authors Sato, S.; Uchida, T. !$#journal J. Biochem. (1975) 77:1171-1176 !$#title The disulfide bridges of ribonuclease U-2 from Ustilago !1sphaerogena. !$#cross-references MUID:76189971; PMID:1225902 !$#contents annotation; disulfide bonds REFERENCE A94440 !$#authors Uchida, T.; Sato, S. !$#book Ribosomes and RNA Metabolism, Zelinka, J., and Balan, J., !1eds., pp.453-472, Publ. House Slovak Acad. Sci., Bratislava, !11973 !$#contents annotation; active site REFERENCE A66564 !$#authors Noguchi, S.; Satow, Y.; Uchida, T.; Sasaki, C.; Matsuzaki, !1T. !$#submission submitted to the Brookhaven Protein Data Bank, May 1995 !$#cross-references PDB:1RTU !$#contents annotation; X-ray crystallography, 1.8 angstroms COMMENT This enzyme, a purine-specific ribonuclease, exists in two !1isoforms, U2-A and U2-B. The U2-A is the major component !1named simply U2. COMMENT This fungus is a basidiomycete. COMMENT Isoform B, a less active form, results from the isopeptide !1isomerization of the Asn-32 to Gly-33 bond through a !1probable cyclic imide intermediate. CLASSIFICATION #superfamily ribonuclease T1 KEYWORDS endonuclease; extracellular protein; hydrolase FEATURE !$1-54,9-113,55-96 #disulfide_bonds #status experimental\ !$39,41,85,101 #active_site Tyr, His, Arg, His #status predicted\ !$62 #active_site Glu #status experimental SUMMARY #length 114 #molecular-weight 12387 #checksum 1903 SEQUENCE /// ENTRY NRASSG #type complete TITLE ribonuclease alpha-sarcin (EC 3.1.-.-) precursor - Aspergillus giganteus ORGANISM #formal_name Aspergillus giganteus DATE 18-Apr-1984 #sequence_revision 30-Sep-1991 #text_change 16-Jun-2000 ACCESSIONS JU0138; S12582; A00802; S21866 REFERENCE JU0138 !$#authors Wnendt, S.; Felske-Zech, H.; Henze, P.P.C.; Ulbrich, N.; !1Stahl, U. !$#journal Gene (1993) 124:239-244 !$#title Characterization of the gene encoding alpha-sarcin, a !1ribosome-inactivating protein secreted by aspergillus !1giganteus. !$#cross-references MUID:93185929; PMID:8444347 !$#accession JU0138 !'##molecule_type DNA !'##residues 1-177 ##label WNE !'##cross-references EMBL:X60770; NID:g2310; PIDN:CAA43180.1; PID:g2311 REFERENCE S12582 !$#authors Oka, T.; Natori, Y.; Tanaka, S.; Tsurugi, K.; Endo, Y. !$#journal Nucleic Acids Res. (1990) 18:1897 !$#title Complete nucleotide sequence of cDNA for the cytotoxin alpha !1sarcin. !$#cross-references MUID:90245591; PMID:2336369 !$#accession S12582 !'##molecule_type mRNA !'##residues 1-177 ##label OKA !'##cross-references GB:D13704; GB:D00516; NID:g217810; PIDN:BAA02863.1; !1PID:g217811 REFERENCE A00802 !$#authors Sacco, G.; Drickamer, K.; Wool, I.G. !$#journal J. Biol. Chem. (1983) 258:5811-5818 !$#title The primary structure of the cytotoxin alpha-sarcin. !$#cross-references MUID:83213554; PMID:6343394 !$#accession A00802 !'##molecule_type protein !'##residues 28-177 ##label SAC COMMENT Alpha-sarcin is specific for purines in both single- and !1double-stranded RNA. Its toxic action on eukaryotic cells is !1the result of cleavage of a single phosphodiester bond in !1the rRNA of the 60S subunit of ribosomes. GENETICS !$#gene sar !$#introns 29/3 CLASSIFICATION #superfamily ribonuclease T1 KEYWORDS endonuclease; extracellular protein; hydrolase; toxin FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-177 #product ribonuclease alpha-sarcin #status !8experimental #label MAT\ !$33-175,103-159 #disulfide_bonds #status predicted\ !$75,77,123,148,164 #active_site Tyr, His, Glu, Arg, His #status !8predicted SUMMARY #length 177 #molecular-weight 19724 #checksum 9773 SEQUENCE /// ENTRY NRASMR #type complete TITLE ribonuclease mitogillin (EC 3.1.-.-) precursor - Aspergillus restrictus ALTERNATE_NAMES restrictocin ORGANISM #formal_name Aspergillus restrictus DATE 17-Mar-1987 #sequence_revision 26-Jan-1996 #text_change 18-Jun-1999 ACCESSIONS S22294; A00803; S74185 REFERENCE S22294 !$#authors Lamy, B.; Davies, J. !$#journal Nucleic Acids Res. (1991) 19:1001-1006 !$#title Isolation and nucleotide sequence of the Aspergillus !1restrictus gene coding for the ribonucleolytic toxin !1restrictocin and its expression in Aspergillus nidulans: the !1leader sequence protects producing strains from suicide. !$#cross-references MUID:91212176; PMID:2020539 !$#accession S22294 !'##status preliminary !'##molecule_type DNA !'##residues 1-176 ##label LAM !'##cross-references EMBL:X56176; NID:g2475; PIDN:CAA39637.1; PID:g2476 REFERENCE A00803 !$#authors Fernandez-Luna, J.L.; Lopez-Otin, C.; Soriano, F.; Mendez, !1E. !$#journal Biochemistry (1985) 24:861-867 !$#title Complete amino acid sequence of the Aspergillus cytotoxin !1mitogillin. !$#cross-references MUID:85199836; PMID:3994994 !$#accession A00803 !'##molecule_type protein !'##residues 28-51,'N',53-141,'N',143-176 ##label FER REFERENCE S74185 !$#authors Rathore, D.; Nayak, S.K.; Batra, J.K. !$#journal FEBS Lett. (1996) 392:259-262 !$#title Expression of ribonucleolytic toxin restrictocin in !1Escherichia coli: purification and characterization. !$#cross-references MUID:96371022; PMID:8774857 !$#accession S74185 !'##molecule_type protein !'##residues 28-47 ##label RAT !'##experimental_source ATCC strain 34475 COMMENT This purine-specific ribonuclease cleaves 28S RNA in !1eukaryotic ribosomes, inhibits protein synthesis, and shows !1antitumor activity. GENETICS !$#introns 28/3 CLASSIFICATION #superfamily ribonuclease T1 KEYWORDS cytotoxin; endonuclease; hydrolase FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-176 #product ribonuclease mitogillin #status experimental !8#label MAT\ !$32-174,102-158 #disulfide_bonds #status experimental\ !$74,76,122,147,163 #active_site Tyr, His, Glu, Arg, His #status !8predicted SUMMARY #length 176 #molecular-weight 19595 #checksum 7616 SEQUENCE /// ENTRY A46497 #type complete TITLE major allergen I - Aspergillus fumigatus ALTERNATE_NAMES 18K IgE binding protein; allergen I/a; IgE-binding ribotoxin; ribonuclease mitogillin (EC 3.1.-.-) I; ribonucleotoxin-related protein ORGANISM #formal_name Aspergillus fumigatus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A46497; S16479; PH0101; A46524 REFERENCE A46497 !$#authors Arruda, L.K.; Mann, B.J.; Chapman, M.D. !$#journal J. Immunol. (1992) 149:3354-3359 !$#title Selective expression of a major allergen and cytotoxin, Asp !1f I, in Aspergillus fumigatus. Implications for the !1immunopathogenesis of Aspergillus-related diseases. !$#cross-references MUID:93056501; PMID:1431110 !$#accession A46497 !'##status preliminary !'##molecule_type DNA !'##residues 1-176 ##label ARR !'##cross-references GB:M83781; NID:g166485; PIDN:AAB07779.1; !1PID:g166486 !'##note sequence extracted from NCBI backbone (NCBIP:117477) REFERENCE S16479 !$#authors Lamy, B.; Moutaouakil, M.; Latge, J.P.; Davies, J. !$#journal Mol. Microbiol. (1991) 5:1811-1815 !$#title Secretion of a potential virulence factor, a fungal !1ribonucleotoxin, during human aspergillosis infections. !$#cross-references MUID:92048500; PMID:1943712 !$#accession S16479 !'##status preliminary !'##molecule_type DNA !'##residues 1-51,'S',53-176 ##label LAM REFERENCE PH0101 !$#authors Arruda, L.K.; Platts-Mills, T.A.E.; Fox, J.W.; Chapman, M.D. !$#journal J. Exp. Med. (1990) 172:1529-1532 !$#title Aspergillus fumigatus allergen I, a major IgE-binding !1protein, is a member of the mitogillin family of cytotoxins. !$#cross-references MUID:91037819; PMID:2230656 !$#accession PH0101 !'##molecule_type protein !'##residues 28-43,'X',45,'XXG',49-58,'T',60-65,'XXXX',70-76,'X',78-79, !1'D',81-85,'F',87;114-134;148-155 ##label AR2 REFERENCE A46524 !$#authors Moser, M.; Crameri, R.; Menz, G.; Schneider, T.; Dudler, T.; !1Virchow, C.; Gmachl, M.; Blaser, K.; Suter, M. !$#journal J. Immunol. (1992) 149:454-460 !$#title Cloning and expression of recombinant Aspergillus fumigatus !1allergen I/a (rAsp f I/a) with IgE binding and type I skin !1test activity. !$#cross-references MUID:92325473; PMID:1624793 !$#accession A46524 !'##molecule_type mRNA !'##residues 28-51,'S',53-176 ##label MOS !'##cross-references GB:S39330; NID:g250901; PIDN:AAB22442.1; !1PID:g250902 !'##experimental_source strain AF 102, ATCC 42202 !'##note sequence extracted from NCBI backbone (NCBIN:108064, !1NCBIP:108065) COMMENT This purine-specific ribonuclease cleaves 28S RNA in !1eukaryotic ribosomes, inhibits protein synthesis, is !1allergenic, and shows antitumor activity. GENETICS !$#gene aspf1 CLASSIFICATION #superfamily ribonuclease T1 KEYWORDS cytotoxin; endonuclease; hydrolase FEATURE !$32-174,102-158 #disulfide_bonds #status predicted\ !$74,76,122,147,163 #active_site Tyr, His, Glu, Arg, His #status !8predicted SUMMARY #length 176 #molecular-weight 19622 #checksum 7356 SEQUENCE /// ENTRY NRHU1 #type complete TITLE pancreatic ribonuclease (EC 3.1.27.5) precursor [validated] - human ALTERNATE_NAMES ribonuclease A; ribonuclease HK-2A; ribonuclease, secretory CONTAINS pancreatic ribonuclease, pancreatic form; pancreatic ribonuclease, secreted form ORGANISM #formal_name Homo sapiens #common_name man DATE 19-Nov-1988 #sequence_revision 03-Oct-1995 #text_change 08-Dec-2000 ACCESSIONS S45003; S22809; S47636; A27235; S02657; PW0011; S11307; !1S11308; S39772; S39773; S18179 REFERENCE S45003 !$#authors Lukasheva, V.; Kochetov, A.; Filipenko, M.L.; Mertvetsov, !1N.; Rivkin, M.I. !$#submission submitted to the EMBL Data Library, May 1994 !$#description Cloning and sequencing of human pancreatic ribonuclease !1gene. !$#accession S45003 !'##molecule_type DNA !'##residues 1-150,'T',152 ##label LU2 !'##cross-references EMBL:X79235; NID:g488412; PIDN:CAA55817.1; !1PID:g488413 !'##experimental_source placenta REFERENCE S22808 !$#authors Haugg, M.; Schein, C.H. !$#journal Nucleic Acids Res. (1992) 20:612 !$#title The DNA sequences of the human and hamster secretory !1ribonucleases determined with the polymerase chain reaction !1(PCR). !$#cross-references MUID:92158677; PMID:1741299 !$#accession S22809 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 23-149 ##label HAU !'##cross-references EMBL:X62946; NID:g35280; PIDN:CAA44718.1; !1PID:g35281 REFERENCE S47636 !$#authors Seno, M.; Futami, J.; Kosaka, M.; Seno, S.; Yamada, H. !$#journal Biochim. Biophys. Acta (1994) 1218:466-468 !$#title Nucleotide sequence encoding human pancreatic ribonuclease. !$#cross-references MUID:94325363; PMID:8049276 !$#accession S47636 !'##molecule_type mRNA !'##residues 1,'A',3-156 ##label SEN !'##cross-references EMBL:D26129; NID:g532677; PIDN:BAA05124.1; !1PID:g641937 !'##experimental_source pancreas REFERENCE A27235 !$#authors Beintema, J.J.; Wietzes, P.; Weickmann, J.L.; Glitz, D.G. !$#journal Anal. Biochem. (1984) 136:48-64 !$#title The amino acid sequence of human pancreatic ribonuclease. !$#cross-references MUID:84176533; PMID:6201087 !$#accession A27235 !'##molecule_type protein !'##residues 29-155 ##label BE2 REFERENCE S02657 !$#authors Beintema, J.J.; Blank, A.; Schieven, G.L.; Dekker, C.A.; !1Sorrentino, S.; Libonati, M. !$#journal Biochem. J. (1988) 255:501-505 !$#title Differences in glycosylation pattern of human secretory !1ribonucleases. !$#cross-references MUID:89076210; PMID:3202829 !$#accession S02657 !'##molecule_type protein !'##residues 29-156 ##label BEI REFERENCE PW0011 !$#authors Sakakibara, R.; Hashida, K.; Tominaga, N.; Sakai, K.; !1Ishiguro, M.; Imamura, S.; Ohmatsu, F.; Sato, E. !$#journal Chem. Pharm. Bull. (1991) 39:146-149 !$#title A putative mouse oocyte maturation inhibitory protein from !1urine of pregnant women: N-terminal sequence homology with !1human nonsecretory ribonuclease. !$#cross-references MUID:91266339; PMID:2049798 !$#accession PW0011 !'##molecule_type protein !'##residues 29-43 ##label SAK REFERENCE S11306 !$#authors Mizuta, K.; Awazu, S.; Yasuda, T.; Kishi, K. !$#journal Arch. Biochem. Biophys. (1990) 281:144-151 !$#title Purification and characterization of three ribonucleases !1from human kidney: comparison with urine ribonucleases. !$#cross-references MUID:90343354; PMID:2383019 !$#accession S11307 !'##molecule_type protein !'##residues 29-43,'X',45-48 ##label MIZ !'##note this form was designated ribonuclease HK-2A !$#accession S11308 !'##molecule_type protein !'##residues 29-47 ##label MI2 !'##note this form was designated ribonuclease HK-2B REFERENCE S39772 !$#authors Yasuda, T.; Nadano, D.; Takeshita, H.; Kishi, K. !$#journal Biochem. J. (1993) 296:617-625 !$#title Two distinct secretory ribonucleases from human cerebrum: !1purification, characterization and relationships to other !1ribonucleases. !$#cross-references MUID:94107224; PMID:8280059 !$#accession S39772 !'##molecule_type protein !'##residues 29-36,'E',38,'E',40-48 ##label YAS !'##note this form was designated ribonuclease HB-1 !$#accession S39773 !'##molecule_type protein !'##residues 29-36,'E',38,'E',40-49 ##label YA2 !'##note this form was designated ribonuclease HB-2 GENETICS !$#gene GDB:RNASE1; RNS1 !'##cross-references GDB:125275; OMIM:180440 !$#map_position 14 !$#introns #status absent FUNCTION !$#description ribonuclease endonucleolytically hydrolyzes RNA to produce !13'-phosphomono- and -oligonucleotides at pyrimidine residues !$#pathway ribonucleic acid digestion !$#note this enzyme can also destabilize or unwind the DNA helix by !1complexing with single-stranded DNA; this complex arises by !1an extended multisite cation-anion interaction between the !1lysine and arginine residues of the enzyme and the phosphate !1groups of the nucleotides CLASSIFICATION #superfamily pancreatic ribonuclease KEYWORDS glycoprotein; hydrolase; nucleic acid digestion; pancreas FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-156 #product pancreatic ribonuclease, secreted form !8#status experimental #label MAT1\ !$29-155 #product pancreatic ribonuclease, pancreatic form !8#status experimental #label MAT2\ !$40,69,147 #active_site His, Lys, His #status predicted\ !$54-112,68-123, !$86-138,93-100 #disulfide_bonds #status predicted\ !$62,104,116 #binding_site carbohydrate (Asn) (covalent) #link !8MAT1 #status experimental\ !$62 #binding_site carbohydrate (Asn) (covalent) (partial) !8#link MAT2 #status experimental SUMMARY #length 156 #molecular-weight 17630 #checksum 6145 SEQUENCE /// ENTRY NRBO #type complete TITLE pancreatic ribonuclease (EC 3.1.27.5) precursor [validated] - bovine ALTERNATE_NAMES ribonuclease 1; ribonuclease A ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 24-Apr-1984 #sequence_revision 05-Aug-1994 #text_change 15-Sep-2000 ACCESSIONS S00897; I45998; A32471; A00804; A92018; A61293; S53757; !1S05528 REFERENCE S00897 !$#authors Carsana, A.; Confalone, E.; Palmieri, M.; Libonati, M.; !1Furia, A. !$#journal Nucleic Acids Res. (1988) 16:5491-5502 !$#title Structure of the bovine pancreatic ribonuclease gene: the !1unique intervening sequence in the 5' untranslated region !1contains a promoter-like element. !$#cross-references MUID:88262557; PMID:2838818 !$#accession S00897 !'##molecule_type DNA !'##residues 1-150 ##label CAR !'##cross-references EMBL:X07283; NID:g671; PIDN:CAA30263.1; PID:g672 REFERENCE I45998 !$#authors Vasantha, N.; Filpula, D. !$#journal Gene (1989) 76:53-60 !$#title Expression of bovine pancreatic ribonuclease A coded by a !1synthetic gene in Bacillus subtilis. !$#cross-references MUID:89306659; PMID:2501158 !$#accession I45998 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 'M',27-150 ##label VAS !'##cross-references EMBL:X15802; NID:g93; PIDN:CAA33801.1; PID:g94 !'##note recombinant gene expressed in E. coli REFERENCE A32471 !$#authors Robertson, A.D.; Purisima, E.O.; Eastman, M.A.; Scheraga, !1H.A. !$#journal Biochemistry (1989) 28:5930-5938 !$#title Proton NMR assignments and regular backbone structure of !1bovine pancreatic ribonuclease a in aqueous solution. !$#cross-references MUID:89375325; PMID:2775743 !$#accession A32471 !'##molecule_type protein !'##residues 27-150 ##label ROB REFERENCE A92016 !$#authors Smyth, D.G.; Stein, W.H.; Moore, S. !$#journal J. Biol. Chem. (1963) 238:227-234 !$#title The sequence of amino acid residues in bovine pancreatic !1ribonuclease: revisions and confirmations. !$#accession A00804 !'##molecule_type protein !'##residues 27-150 ##label SMY !'##note disulfide bonds were determined REFERENCE A92018 !$#authors Plummer Jr., T.H.; Hirs, C.H.W. !$#journal J. Biol. Chem. (1964) 239:2530-2538 !$#title On the structure of bovine pancreatic ribonuclease B. !1Isolation of a glycopeptide. !$#accession A92018 !'##molecule_type protein !'##residues 27-150 ##label PLU REFERENCE A61293 !$#authors Kumagai, H.; Yoshihara, K.; Umemoto, M.; Igarashi, K.; !1Hirose, S.; Ohgi, K.; Irie, M. !$#journal J. Biochem. (1983) 93:865-874 !$#title Studies on salivary gland ribonucleases. III. Purification !1and properties of three ribonucleases from bovine parotid !1gland. !$#cross-references MUID:83265672; PMID:6874668 !$#accession A61293 !'##molecule_type protein !'##residues 27-40,'XX',43,'X',45-46 ##label KUM REFERENCE S53757 !$#authors Yang, H.J.; Tsou, C.L. !$#journal Biochem. J. (1995) 305:379-384 !$#title Inactivation during denaturation of ribonuclease A by !1guanidinium chloride is accompanied by unfolding at the !1active site. !$#cross-references MUID:95134214; PMID:7832749 !$#accession S53757 !'##molecule_type protein !'##residues 27-53;60-63;69-73 ##label YAN REFERENCE A51385 !$#authors Birdsall, D.L.; McPherson, A. !$#submission submitted to the Brookhaven Protein Data Bank, August 1992 !$#cross-references PDB:1RTB !$#contents annotation; X-ray crystallography, 2.5 angstroms, residues !127-150 REFERENCE A44321 !$#authors Birdsall, D.L.; McPherson, A. !$#journal J. Biol. Chem. (1992) 267:22230-22236 !$#title Crystal structure disposition of thymidylic acid tetramer in !1complex with ribonuclease A. !$#cross-references MUID:93054504; PMID:1429575 !$#contents annotation; X-ray crystallography, 2.5 angstroms REFERENCE A50330 !$#authors Williams, R.L.; Greene, S.M.; McPherson, A. !$#submission submitted to the Brookhaven Protein Data Bank, September !11987 !$#cross-references PDB:1RBB !$#contents annotation; X-ray crystallography, 2.5 angstroms, residues !127-150 REFERENCE A50927 !$#authors Wlodawer, A. !$#submission submitted to the Brookhaven Protein Data Bank, April 1985 !$#cross-references PDB:5RSA !$#contents annotation; X-ray and neutron crystallography, 2.0 !1angstroms, residues 27-150 REFERENCE A92350 !$#authors Wlodawer, A.; Bott, R.; Sjolin, L. !$#journal J. Biol. Chem. (1982) 257:1325-1332 !$#title The refined crystal structure of ribonuclease A at 2.0 !1angstrom resolution. !$#cross-references MUID:82120062; PMID:6276380 !$#contents annotation; X-ray crystallography, 2.0 angstroms REFERENCE A50626 !$#authors Howlin, B.; Moss, D.S.; Harris, G.W.; Palmer, R.A. !$#submission submitted to the Brookhaven Protein Data Bank, October 1991 !$#cross-references PDB:3RN3 !$#contents annotation; X-ray crystallography, 1.45 angstroms, residues !127-150 REFERENCE A92949 !$#authors Carlisle, C.H.; Palmer, R.A.; Mazumdar, S.K.; Gorinsky, !1B.A.; Yeates, D.G.R. !$#journal J. Mol. Biol. (1974) 85:1-18 !$#title The structure of ribonuclease at 2.5 angstrom resolution. !$#cross-references MUID:74253324; PMID:4835726 !$#contents annotation; X-ray crystallography, 2.5 angstroms REFERENCE A92059 !$#authors Wyckoff, H.W.; Tsernoglou, D.; Hanson, A.W.; Knox, J.R.; !1Lee, B.; Richards, F.M. !$#journal J. Biol. Chem. (1970) 245:305-328 !$#title The three-dimensional structure of ribonuclease-S. !1Interpretation of an electron density map at a nominal !1resolution of 2 A. !$#cross-references MUID:70092235; PMID:5460889 !$#contents annotation; X-ray crystallography, 2.0 angstroms REFERENCE A52045 !$#authors Santoro, J.; Gonzalez, C.; Bruix, M.; Neira, J.L.; Nieto, !1J.L.; Herranz, J.; Rico, M. !$#submission submitted to the Brookhaven Protein Data Bank, November 1992 !$#cross-references PDB:2AAS !$#contents annotation; conformation by (1)H-NMR, residues 27-150 REFERENCE S05528 !$#authors Rico, M.; Bruix, M.; Santoro, J.; Gonzalez, C.; Neira, J.L.; !1Nieto, J.L.; Herranz, J. !$#journal Eur. J. Biochem. (1989) 183:623-638 !$#title Sequential (1)H-NMR assignment and solution structure of !1bovine pancreatic ribonuclease A. !$#cross-references MUID:89377830; PMID:2776756 !$#contents annotation; confirmation by (1)H-NMR REFERENCE A92946 !$#authors Shall, S.; Barnard, E.A. !$#journal J. Mol. Biol. (1969) 41:237-251 !$#title Heavy atom-labelled derivatives of bovine pancreatic !1ribonuclease. I. Specific reactions of ribonuclease with !1N-acetylhomocysteine thiolactone and silver ion. !$#cross-references MUID:69260123; PMID:5801478 !$#contents annotation; active site REFERENCE A92020 !$#authors Heinrikson, R.L.; Stein, W.H.; Crestfield, A.M.; Moore, S. !$#journal J. Biol. Chem. (1965) 240:2921-2934 !$#title The reactivities of the histidine residues at the active !1site of ribonuclease toward halo acids of different !1structures. !$#contents annotation; active site FUNCTION !$#description ribonuclease endonucleolytically hydrolyzes RNA to produce !13'-phosphomono- and -oligonucleotides at pyrimidine residues !$#pathway ribonucleic acid digestion !$#note this enzyme can also destabilize or unwind the DNA helix by !1complexing with single-stranded DNA; this complex arises by !1an extended multisite cation-anion interaction between the !1lysine and arginine residues of the enzyme and the phosphate !1groups of the nucleotides CLASSIFICATION #superfamily pancreatic ribonuclease KEYWORDS glycoprotein; hydrolase; nucleic acid digestion; pancreas FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-150 #product pancreatic ribonuclease #status experimental !8#label MAT\ !$38,67,145 #active_site His, Lys, His #status experimental\ !$52-110,66-121, !$84-136,91-98 #disulfide_bonds #status experimental\ !$60 #binding_site carbohydrate (Asn) (covalent) (partial) !8#status experimental SUMMARY #length 150 #molecular-weight 16461 #checksum 6084 SEQUENCE /// ENTRY NRBOB #type complete TITLE pancreatic ribonuclease (EC 3.1.27.5) - American bison (tentative sequence) ALTERNATE_NAMES RNase 1; RNase A ORGANISM #formal_name Bison bison #common_name American bison DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 08-Dec-1994 ACCESSIONS A91771; A90270; A94696; A00804 REFERENCE A91771 !$#authors Muskiet, F.A.J.; Welling, G.W.; Beintema, J.J. !$#journal Int. J. Pept. Protein Res. (1976) 8:345-348 !$#cross-references MUID:76259396; PMID:955781 !$#accession A91771 !'##molecule_type protein !'##residues 1-124 ##label MUS !'##note comparison of peptide compositions and partial sequence !1determination revealed no differences from the bovine !1sequence REFERENCE A90270 !$#authors Stewart, G.R.; Stevenson, K.J. !$#journal Biochem. J. (1973) 135:427-441 !$#title The isolation and partial characterization of ribonuclease A !1from Bison bison. !$#cross-references MUID:74081066; PMID:4772270 !$#accession A90270 !'##molecule_type protein !'##residues 1-60,62-124 ##label STE !'##note peptide compositions were compared with the bovine sequence REFERENCE A94696 !$#authors Barnard, E.A.; Cohen, M.S.; Gold, M.H.; Kim, J.K. !$#journal Nature (1972) 240:395-398 !$#title Evolution of ribonuclease in relation to polypeptide folding !1mechanisms. !$#cross-references MUID:73045781; PMID:4564316 !$#accession A94696 !'##molecule_type protein !'##residues 1-15,'E',17,'E',19-20,'XTA',24-30 ##label BAR CLASSIFICATION #superfamily pancreatic ribonuclease KEYWORDS glycoprotein; hydrolase; nucleic acid digestion; pancreas FEATURE !$12,41,119 #active_site His, Lys, His #status predicted\ !$26-84,40-95,58-110, !$65-72 #disulfide_bonds #status predicted\ !$34 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 124 #molecular-weight 13690 #checksum 7894 SEQUENCE /// ENTRY NRWB #type complete TITLE pancreatic ribonuclease (EC 3.1.27.5) - domestic water buffalo ALTERNATE_NAMES RNase 1; RNase A ORGANISM #formal_name Bubalus arnee bubalis #common_name domestic water buffalo DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 01-Dec-1995 ACCESSIONS A00805; S08548 REFERENCE A00805 !$#authors Sidik, A.; Martena, B.; Beintema, J.J. !$#journal Biochem. Genet. (1979) 17:1151-1158 !$#title Amino acid sequence differences in pancreatic ribonucleases !1from water buffalo breeds from Indonesia and Italy. !$#cross-references MUID:80153329; PMID:540006 !$#accession A00805 !'##molecule_type protein !'##residues 1-124 ##label SID !'##experimental_source Italian river breed and Indonesian swamp breed !'##note the sequence from the Italian river breed is shown !'##note the sequence from Indonesian swamp breed differs from that !1shown in having 34-Ser, 61-Lys, and 120-Phe. In this breed, !1most of the molecules do not bind carbohydrate, but there is !1evidence of a polymorphic form that does REFERENCE S07141 !$#authors Beintema, J.J. !$#journal Biochim. Biophys. Acta (1980) 621:89-103 !$#title Primary structures of pancreatic ribonucleases from Bovidae. !1Impala, Thomson's gazelle, nilgai and water buffalo. !$#cross-references MUID:80109825; PMID:7353035 !$#accession S08548 !'##status preliminary !'##molecule_type protein !'##residues 1-124 ##label BEI CLASSIFICATION #superfamily pancreatic ribonuclease KEYWORDS glycoprotein; hydrolase; nucleic acid digestion; pancreas FEATURE !$12,41,119 #active_site His, Lys, His #status predicted\ !$26-84,40-95,58-110, !$65-72 #disulfide_bonds #status predicted\ !$34 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 124 #molecular-weight 13699 #checksum 8765 SEQUENCE /// ENTRY NRANE #type complete TITLE pancreatic ribonuclease (EC 3.1.27.5) - eland ALTERNATE_NAMES RNase 1; RNase A ORGANISM #formal_name Tragelaphus oryx, Taurotragus oryx #common_name eland DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 31-Dec-1993 ACCESSIONS A00806 REFERENCE A00806 !$#authors Russchen, F.; de Vrieze, G.; Gaastra, W.; Beintema, J.J. !$#journal Biochim. Biophys. Acta (1976) 427:719-726 !$#title Studies on the covalent structure of eland pancreatic !1ribonuclease. !$#cross-references MUID:76184786; PMID:1268225 !$#accession A00806 !'##molecule_type protein !'##residues 1-124 ##label RUS CLASSIFICATION #superfamily pancreatic ribonuclease KEYWORDS hydrolase; nucleic acid digestion; pancreas FEATURE !$12,41,119 #active_site His, Lys, His #status predicted\ !$26-84,40-95,58-110, !$65-72 #disulfide_bonds #status predicted SUMMARY #length 124 #molecular-weight 13742 #checksum 798 SEQUENCE /// ENTRY NRANT #type complete TITLE pancreatic ribonuclease (EC 3.1.27.5) - korrigum sassaby ALTERNATE_NAMES RNase 1; RNase A ORGANISM #formal_name Damaliscus lunatus korrigum #common_name korrigum sassaby, korrigum topi DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 31-Dec-1993 ACCESSIONS A00807 REFERENCE A00807 !$#authors Kuper, H.; Beintema, J.J. !$#journal Biochim. Biophys. Acta (1976) 446:337-344 !$#title The amino acid sequence of topi pancreatic ribonuclease. !$#cross-references MUID:77045543; PMID:990282 !$#accession A00807 !'##molecule_type protein !'##residues 1-124 ##label KUP CLASSIFICATION #superfamily pancreatic ribonuclease KEYWORDS glycoprotein; hydrolase; nucleic acid digestion; pancreas FEATURE !$12,41,119 #active_site His, Lys, His #status predicted\ !$26-84,40-95,58-110, !$65-72 #disulfide_bonds #status predicted\ !$34 #binding_site carbohydrate (Asn) (covalent) (partial) !8#status experimental SUMMARY #length 124 #molecular-weight 13709 #checksum 9608 SEQUENCE /// ENTRY NRGN #type complete TITLE pancreatic ribonuclease (EC 3.1.27.5) - brindled gnu ALTERNATE_NAMES RNase 1; RNase A ORGANISM #formal_name Connochaetes taurinus #common_name brindled gnu, white-bearded gnu, blue wildebeest DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 04-Oct-1996 ACCESSIONS A00808 REFERENCE A00808 !$#authors Groen, G.; Welling, G.W.; Beintema, J.J. !$#journal FEBS Lett. (1975) 60:300-304 !$#title The amino acid sequence of gnu pancreatic ribonuclease. !$#cross-references MUID:76210818; PMID:1227969 !$#accession A00808 !'##molecule_type protein !'##residues 1-124 ##label GRO CLASSIFICATION #superfamily pancreatic ribonuclease KEYWORDS glycoprotein; hydrolase; nucleic acid digestion; pancreas FEATURE !$12,41,119 #active_site His, Lys, His #status predicted\ !$26-84,40-95,58-110, !$65-72 #disulfide_bonds #status predicted\ !$34 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 124 #molecular-weight 13686 #checksum 7369 SEQUENCE /// ENTRY NRSH #type complete TITLE pancreatic ribonuclease (EC 3.1.27.5) - sheep ALTERNATE_NAMES RNase 1; RNase A ORGANISM #formal_name Ovis orientalis aries, Ovis ammon aries #common_name domestic sheep DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 04-Oct-1996 ACCESSIONS A91406; A92145; A00809 REFERENCE A91406 !$#authors Welling, G.W.; Scheffer, A.J.; Beintema, J.J. !$#journal FEBS Lett. (1974) 41:58-61 !$#title The primary structure of goat and sheep pancreatic !1ribonucleases. !$#cross-references MUID:74309062; PMID:4855010 !$#accession A91406 !'##molecule_type protein !'##residues 1-124 ##label WEL REFERENCE A92145 !$#authors Kobayashi, R.; Hirs, C.H.W. !$#journal J. Biol. Chem. (1973) 248:7833-7837 !$#title The amino acid sequence of ovine pancreatic ribonuclese A. !$#cross-references MUID:74025520; PMID:4356260 !$#accession A92145 !'##molecule_type protein !'##residues 1-48,'Q',50-102,'Q',104-124 ##label KOB CLASSIFICATION #superfamily pancreatic ribonuclease KEYWORDS glycoprotein; hydrolase; nucleic acid digestion; pancreas FEATURE !$12,41,119 #active_site His, Lys, His #status predicted\ !$26-84,40-95,58-110, !$65-72 #disulfide_bonds #status predicted\ !$34 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 124 #molecular-weight 13707 #checksum 8041 SEQUENCE /// ENTRY NRGT #type complete TITLE pancreatic ribonuclease (EC 3.1.27.5) - goat ALTERNATE_NAMES RNase 1; RNase A ORGANISM #formal_name Capra aegagrus hircus #common_name domestic goat DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 04-Oct-1996 ACCESSIONS A00810 REFERENCE A91406 !$#authors Welling, G.W.; Scheffer, A.J.; Beintema, J.J. !$#journal FEBS Lett. (1974) 41:58-61 !$#title The primary structure of goat and sheep pancreatic !1ribonucleases. !$#cross-references MUID:74309062; PMID:4855010 !$#accession A00810 !'##molecule_type protein !'##residues 1-124 ##label WEL CLASSIFICATION #superfamily pancreatic ribonuclease KEYWORDS glycoprotein; hydrolase; nucleic acid digestion; pancreas FEATURE !$12,41,119 #active_site His, Lys, His #status predicted\ !$26-84,40-95,58-110, !$65-72 #disulfide_bonds #status predicted\ !$34 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 124 #molecular-weight 13709 #checksum 9450 SEQUENCE /// ENTRY NRGF #type complete TITLE pancreatic ribonuclease (EC 3.1.27.5) - giraffe (tentative sequence) ALTERNATE_NAMES RNase 1; RNase A ORGANISM #formal_name Giraffa camelopardalis #common_name giraffe DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 31-Mar-2000 ACCESSIONS A94452; A91405; A00811 REFERENCE A94452 !$#authors Gaastra, W. !$#citation Ph.D. thesis, University of Groningen, Groningen, The !1Netherlands, 1975 !$#accession A94452 !'##molecule_type protein !'##residues 1-124 ##label GAA REFERENCE A91405 !$#authors Gaastra, W.; Groen, G.; Welling, G.W.; Beintema, J.J. !$#journal FEBS Lett. (1974) 41:227-232 !$#title The primary structure of giraffe pancreatic ribonuclease. !$#cross-references MUID:74309061; PMID:4855009 !$#accession A91405 !'##molecule_type protein !'##residues 1-124 ##label GA2 CLASSIFICATION #superfamily pancreatic ribonuclease KEYWORDS glycoprotein; hydrolase; nucleic acid digestion; pancreas FEATURE !$12,41,119 #active_site His, Lys, His #status predicted\ !$26-84,40-95,58-110, !$65-72 #disulfide_bonds #status predicted\ !$34 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 124 #molecular-weight 13703 #checksum 8489 SEQUENCE /// ENTRY NRDER #type complete TITLE pancreatic ribonuclease (EC 3.1.27.5) - red deer (tentative sequence) ALTERNATE_NAMES RNase 1; RNase A ORGANISM #formal_name Cervus elaphus #common_name red deer DATE 24-Apr-1984 #sequence_revision 31-Dec-1991 #text_change 03-Feb-1994 ACCESSIONS B90613; A00812 REFERENCE A91207 !$#authors Zwiers, H.; Scheffer, A.J.; Beintema, J.J. !$#journal Eur. J. Biochem. (1973) 36:569-574 !$#title Amino-acid sequences of red-deer and roe-deer pancreatic !1ribonucleases. !$#cross-references MUID:73253236; PMID:4738402 !$#contents annotation !$#note the sequence has been revised in reference A90613 REFERENCE A90613 !$#authors Oosterhuis, S.; Welling, G.W.; Gaastra, W.; Beintema, J.J. !$#journal Biochim. Biophys. Acta (1977) 490:523-529 !$#title Reinvestigation of the primary structures of red deer and !1roe deer pancreatic ribonuclease and proline sites in !1mammalian ribonucleases. !$#cross-references MUID:77112628; PMID:836889 !$#accession B90613 !'##molecule_type protein !'##residues 1-124 ##label OOS !'##note the authors reinvestigated the sequences of residues 1-25 CLASSIFICATION #superfamily pancreatic ribonuclease KEYWORDS hydrolase; nucleic acid digestion; pancreas FEATURE !$12,41,119 #active_site His, Lys, His #status predicted\ !$26-84,40-95,58-110, !$65-72 #disulfide_bonds #status predicted SUMMARY #length 124 #molecular-weight 13725 #checksum 7429 SEQUENCE /// ENTRY NRDEO #type complete TITLE pancreatic ribonuclease (EC 3.1.27.5) - roe deer (tentative sequence) ALTERNATE_NAMES RNase 1; RNase A ORGANISM #formal_name Capreolus capreolus #common_name roe deer DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 03-Feb-1994 ACCESSIONS A90613; A00812 REFERENCE A91207 !$#authors Zwiers, H.; Scheffer, A.J.; Beintema, J.J. !$#journal Eur. J. Biochem. (1973) 36:569-574 !$#title Amino-acid sequences of red-deer and roe-deer pancreatic !1ribonucleases. !$#cross-references MUID:73253236; PMID:4738402 !$#contents annotation !$#note the sequence has been revised in reference A90613 REFERENCE A90613 !$#authors Oosterhuis, S.; Welling, G.W.; Gaastra, W.; Beintema, J.J. !$#journal Biochim. Biophys. Acta (1977) 490:523-529 !$#title Reinvestigation of the primary structures of red deer and !1roe deer pancreatic ribonuclease and proline sites in !1mammalian ribonucleases. !$#cross-references MUID:77112628; PMID:836889 !$#accession A90613 !'##molecule_type protein !'##residues 1-124 ##label OOS !'##note the authors reinvestigated the sequences of residues 1-25 and !199 CLASSIFICATION #superfamily pancreatic ribonuclease KEYWORDS glycoprotein; hydrolase; nucleic acid digestion; pancreas FEATURE !$12,41,119 #active_site His, Lys, His #status predicted\ !$26-84,40-95,58-110, !$65-72 #disulfide_bonds #status predicted\ !$34 #binding_site carbohydrate (Asn) (covalent) (partial) !8#status experimental SUMMARY #length 124 #molecular-weight 13813 #checksum 7899 SEQUENCE /// ENTRY NRDEF #type complete TITLE pancreatic ribonuclease (EC 3.1.27.5) - fallow deer (tentative sequence) ALTERNATE_NAMES RNase 1; RNase A ORGANISM #formal_name Dama dama #common_name fallow deer DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 31-Dec-1993 ACCESSIONS A91418; A00812 REFERENCE A91418 !$#authors Leijenaar-van den Berg, G.; Beintema, J.J. !$#journal FEBS Lett. (1975) 56:101-107 !$#title The amino acid sequences of reindeer, moose and fallow deer !1pancreatic ribonucleases. !$#cross-references MUID:76003215; PMID:1157925 !$#accession A91418 !'##molecule_type protein !'##residues 1-124 ##label LEI CLASSIFICATION #superfamily pancreatic ribonuclease KEYWORDS hydrolase; nucleic acid digestion; pancreas FEATURE !$12,41,119 #active_site His, Lys, His #status predicted\ !$26-84,40-95,58-110, !$65-72 #disulfide_bonds #status predicted SUMMARY #length 124 #molecular-weight 13807 #checksum 6927 SEQUENCE /// ENTRY NRDEN #type complete TITLE pancreatic ribonuclease (EC 3.1.27.5) - reindeer (tentative sequence) ALTERNATE_NAMES RNase 1; RNase A ORGANISM #formal_name Rangifer tarandus #common_name reindeer DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 31-Dec-1993 ACCESSIONS B91418; A00812 REFERENCE A91418 !$#authors Leijenaar-van den Berg, G.; Beintema, J.J. !$#journal FEBS Lett. (1975) 56:101-107 !$#title The amino acid sequences of reindeer, moose and fallow deer !1pancreatic ribonucleases. !$#cross-references MUID:76003215; PMID:1157925 !$#accession B91418 !'##molecule_type protein !'##residues 1-124 ##label LEI CLASSIFICATION #superfamily pancreatic ribonuclease KEYWORDS hydrolase; nucleic acid digestion; pancreas FEATURE !$12,41,119 #active_site His, Lys, His #status predicted\ !$26-84,40-95,58-110, !$65-72 #disulfide_bonds #status predicted SUMMARY #length 124 #molecular-weight 13759 #checksum 7693 SEQUENCE /// ENTRY NREKN #type complete TITLE pancreatic ribonuclease (EC 3.1.27.5) - European moose (tentative sequence) ALTERNATE_NAMES RNase 1; RNase A ORGANISM #formal_name Alces alces alces #common_name European moose, elk DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 31-Dec-1993 ACCESSIONS C91418; A00812 REFERENCE A91418 !$#authors Leijenaar-van den Berg, G.; Beintema, J.J. !$#journal FEBS Lett. (1975) 56:101-107 !$#title The amino acid sequences of reindeer, moose and fallow deer !1pancreatic ribonucleases. !$#cross-references MUID:76003215; PMID:1157925 !$#accession C91418 !'##molecule_type protein !'##residues 1-124 ##label LEI CLASSIFICATION #superfamily pancreatic ribonuclease KEYWORDS glycoprotein; hydrolase; nucleic acid digestion; pancreas FEATURE !$12,41,119 #active_site His, Lys, His #status predicted\ !$26-84,40-95,58-110, !$65-72 #disulfide_bonds #status predicted\ !$34 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 124 #molecular-weight 13774 #checksum 7510 SEQUENCE /// ENTRY NRPRH #type complete TITLE pancreatic ribonuclease (EC 3.1.27.5) - pronghorn (tentative sequence) ALTERNATE_NAMES RNase 1; RNase A ORGANISM #formal_name Antilocapra americana #common_name pronghorn DATE 28-Feb-1981 #sequence_revision 28-Feb-1981 #text_change 31-Mar-2000 ACCESSIONS A00813 REFERENCE A00813 !$#authors Beintema, J.J.; Gaastra, W.; Munniksma, J. !$#journal J. Mol. Evol. (1979) 13:305-316 !$#title Primary structure of pronghorn pancreatic ribonuclease: !1close relationship between giraffe and pronghorn. !$#cross-references MUID:80075014; PMID:513141 !$#accession A00813 !'##molecule_type protein !'##residues 1-124 ##label BEI CLASSIFICATION #superfamily pancreatic ribonuclease KEYWORDS glycoprotein; hydrolase; nucleic acid digestion; pancreas FEATURE !$12,41,119 #active_site His, Lys, His #status predicted\ !$26-84,40-95,58-110, !$65-72 #disulfide_bonds #status predicted\ !$34 #binding_site carbohydrate (Asn) (covalent) (partial) !8#status experimental SUMMARY #length 124 #molecular-weight 13711 #checksum 8768 SEQUENCE /// ENTRY NRBOS #type complete TITLE seminal ribonuclease (EC 3.1.27.5) precursor - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 24-Apr-1984 #sequence_revision 30-Jun-1991 #text_change 18-Jun-1999 ACCESSIONS S08392; S00131; A45654; A23094 REFERENCE S08392 !$#authors Preuss, K.D.; Wagner, S.; Freudenstein, J.; Scheit, K.H. !$#journal Nucleic Acids Res. (1990) 18:1057 !$#title Cloning of cDNA encoding the complete precursor for bovine !1seminal ribonuclease. !$#cross-references MUID:90192098; PMID:2315023 !$#accession S08392 !'##molecule_type mRNA !'##residues 1-150 ##label PRE !'##cross-references EMBL:X51337; NID:g748; PIDN:CAA35716.1; PID:g749 REFERENCE S00131 !$#authors Suzuki, H.; Parente, A.; Farina, B.; Greco, L.; la Montagna, !1R.; Leone, E. !$#journal Biol. Chem. Hoppe-Seyler (1987) 368:1305-1312 !$#title Complete amino-acid sequence of bovine seminal ribonuclease, !1a dimeric protein from seminal plasma. !$#cross-references MUID:88106995; PMID:3426801 !$#accession S00131 !'##molecule_type protein !'##residues 27-150 ##label SUZ !'##note this is the final paper in a series REFERENCE A45654 !$#authors Ramakrishna, T.; Vijayarangam, D.; Sitaram, N.; Pandit, !1M.W.; Bhargava, P.M. !$#journal Biochem. Int. (1992) 26:125-133 !$#title Apparent specificity of bovine seminal ribonucleases can !1depend on the conditions used for the isolation of !1substrate. !$#cross-references MUID:92313367; PMID:1377468 !$#accession A45654 !'##molecule_type protein !'##residues 27-42,'X',44-47 ##label RAM !'##experimental_source seminal plasma !'##note sequence extracted from NCBI backbone (NCBIP:107298) REFERENCE A23094 !$#authors Palmieri, M.; Carsana, A.; Furia, A.; Libonati, M. !$#journal Eur. J. Biochem. (1985) 152:275-277 !$#title Sequence analysis of a cloned cDNA coding for bovine seminal !1ribonuclease. !$#cross-references MUID:86030265; PMID:3840434 !$#accession A23094 !'##molecule_type mRNA !'##residues 73-150 ##label PAL !'##cross-references GB:X03029; NID:g752; PIDN:CAA26832.1; PID:g753 REFERENCE A30432 !$#authors Krietsch, W.K.G.; Simm, F.C.; Hertenberger, B.; Kuntz, !1G.W.K.; Wachter, E. !$#journal Anal. Biochem. (1983) 128:213-216 !$#title Isolation of bovine seminal ribonuclease by affinity !1chromatography. !$#cross-references MUID:83202042; PMID:6846794 !$#contents annotation; amidation state of residue 43 REFERENCE A30433 !$#authors di Donato, A.; d'Alessio, G. !$#journal Biochem. Biophys. Res. Commun. (1973) 55:919-928 !$#title Interchain disulfide bridges in ribonuclease BS-1. !$#cross-references MUID:74049879; PMID:4761089 !$#contents annotation; interchain disulfide bonds REFERENCE A30434 !$#authors di Donato, A.; d'Alessio, G. !$#journal Biochim. Biophys. Acta (1979) 579:303-313 !$#title Intrachain disulfide bridges of bovine seminal ribonuclease. !$#cross-references MUID:80130655; PMID:534646 !$#contents annotation; intrachain disulfide bonds REFERENCE A30435 !$#authors Capasso, S.; Giordano, F.; Mattia, C.A.; Mazzarella, L.; !1Zagari, A. !$#journal Biopolymers (1983) 22:327-332 !$#title Refinement of the structure of bovine seminal ribonuclease. !$#cross-references MUID:84179398; PMID:6673761 !$#contents annotation; X-ray crystallography, 2.5 angstroms COMMENT This enzyme hydrolyzes both single- and double-stranded RNA. CLASSIFICATION #superfamily pancreatic ribonuclease KEYWORDS homodimer; hydrolase FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-150 #product seminal ribonuclease #status experimental !8#label MAT\ !$38,67,145 #active_site His, Lys, His #status predicted\ !$52-110,66-121, !$84-136,91-98 #disulfide_bonds #status experimental\ !$57,58 #disulfide_bonds interchain #status experimental SUMMARY #length 150 #molecular-weight 16377 #checksum 5779 SEQUENCE /// ENTRY NRCM #type complete TITLE pancreatic ribonuclease (EC 3.1.27.5) - Arabian camel (tentative sequence) ALTERNATE_NAMES RNase 1; RNase A ORGANISM #formal_name Camelus dromedarius #common_name Arabian camel DATE 24-Apr-1984 #sequence_revision 17-Mar-1987 #text_change 31-Dec-1993 ACCESSIONS A00815; A90283 REFERENCE A91340 !$#authors Beintema, J.J. !$#journal FEBS Lett. (1985) 185:115-120 !$#title Mammalian ribonucleases. The absence of a glycosylated !1Asn-Pro-Thr sequence in horse ribonuclease and the presence !1of tryptophan at position 39 in horse and dromedary !1ribonuclease. !$#cross-references MUID:85204378; PMID:3922790 !$#accession A00815 !'##molecule_type protein !'##residues 1-124 ##label BEI REFERENCE A90283 !$#authors Welling, G.W.; Groen, G.; Beintema, J.J. !$#journal Biochem. J. (1975) 147:505-511 !$#title The amino acid sequence of dromedary pancreatic !1ribonuclease. !$#cross-references MUID:76039472; PMID:1167157 !$#accession A90283 !'##molecule_type protein !'##residues 1-36,'N',38,'X',40-77,'S',79-102,'Q',104-124 ##label WEL !'##note this sequence has been revised in reference A91340 CLASSIFICATION #superfamily pancreatic ribonuclease KEYWORDS hydrolase; nucleic acid digestion; pancreas FEATURE !$12,41,119 #active_site His, Lys, His #status predicted\ !$26-84,40-95,58-110, !$65-72 #disulfide_bonds #status predicted SUMMARY #length 124 #molecular-weight 13938 #checksum 6201 SEQUENCE /// ENTRY NRCMM #type complete TITLE pancreatic ribonuclease (EC 3.1.27.5), minor form - Arabian camel (tentative sequence) ALTERNATE_NAMES RNase 1; RNase A ORGANISM #formal_name Camelus dromedarius #common_name Arabian camel DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 31-Dec-1993 ACCESSIONS A90229; A00815 REFERENCE A90229 !$#authors Welling, G.W.; Mulder, H.; Beintema, J.J. !$#journal Biochem. Genet. (1976) 14:309-317 !$#title Allelic polymorphism in Arabian camel ribonuclease and the !1amino acid sequence of Bactrian camel ribonuclease. !$#cross-references MUID:76277807; PMID:962846 !$#accession A90229 !'##molecule_type protein !'##residues 1-124 ##label WEL CLASSIFICATION #superfamily pancreatic ribonuclease KEYWORDS hydrolase; nucleic acid digestion; pancreas FEATURE !$12,41,119 #active_site His, Lys, His #status predicted\ !$26-84,40-95,58-110, !$65-72 #disulfide_bonds #status predicted SUMMARY #length 124 #molecular-weight 13938 #checksum 6477 SEQUENCE /// ENTRY NRCMB #type complete TITLE pancreatic ribonuclease (EC 3.1.27.5) - Bactrian camel (tentative sequence) ALTERNATE_NAMES RNase 1; RNase A ORGANISM #formal_name Camelus bactrianus #common_name Bactrian camel DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 31-Dec-1993 ACCESSIONS B90229; A00815 REFERENCE A90229 !$#authors Welling, G.W.; Mulder, H.; Beintema, J.J. !$#journal Biochem. Genet. (1976) 14:309-317 !$#title Allelic polymorphism in Arabian camel ribonuclease and the !1amino acid sequence of Bactrian camel ribonuclease. !$#cross-references MUID:76277807; PMID:962846 !$#accession B90229 !'##molecule_type protein !'##residues 1-124 ##label WEL CLASSIFICATION #superfamily pancreatic ribonuclease KEYWORDS hydrolase; nucleic acid digestion; pancreas FEATURE !$12,41,119 #active_site His, Lys, His #status predicted\ !$26-84,40-95,58-110, !$65-72 #disulfide_bonds #status predicted SUMMARY #length 124 #molecular-weight 13938 #checksum 6477 SEQUENCE /// ENTRY NRPG #type complete TITLE pancreatic ribonuclease (EC 3.1.27.5) - pig ALTERNATE_NAMES RNase 1; RNase A ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 03-Jun-1994 ACCESSIONS A92071; A91391; A00816 REFERENCE A92071 !$#authors Jackson, R.L.; Hirs, C.H.W. !$#journal J. Biol. Chem. (1970) 245:637-653 !$#title The primary structure of porcine pancreatic ribonuclease. !1II. The amino acid sequence of the reduced S-aminoethylated !1protein. !$#cross-references MUID:70104197; PMID:5460946 !$#accession A92071 !'##molecule_type protein !'##residues 1,'Q',3-124 ##label JAC REFERENCE A91391 !$#authors Wierenga, R.K.; Huizinga, J.D.; Gaastra, W.; Welling, G.W.; !1Beintema, J.J. !$#journal FEBS Lett. (1973) 31:181-185 !$#title Affinity chromatography of porcine pancreatic ribonuclease !1and reinvestigation of the N-terminal amino acid sequence. !$#accession A91391 !'##molecule_type protein !'##residues 1-124 ##label WIE REFERENCE A92072 !$#authors Phelan, J.J.; Hirs, C.H.W. !$#journal J. Biol. Chem. (1970) 245:654-661 !$#title The primary structure of porcine pancreatic ribonuclease. !1III. The disulfide bonds. !$#cross-references MUID:70104198; PMID:4904878 !$#contents annotation; disulfide bonds CLASSIFICATION #superfamily pancreatic ribonuclease KEYWORDS glycoprotein; hydrolase; nucleic acid digestion; pancreas FEATURE !$12,41,119 #active_site His, Lys, His #status predicted\ !$21,34,76 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$26-84,40-95,58-110, !$65-72 #disulfide_bonds #status experimental SUMMARY #length 124 #molecular-weight 13804 #checksum 8298 SEQUENCE /// ENTRY NRHP #type complete TITLE pancreatic ribonuclease (EC 3.1.27.5) - hippopotamus (tentative sequence) ALTERNATE_NAMES RNase 1; RNase A ORGANISM #formal_name Hippopotamus amphibius #common_name hippopotamus DATE 31-Dec-1980 #sequence_revision 31-Dec-1980 #text_change 31-Mar-2000 ACCESSIONS A00817 REFERENCE A91099 !$#authors Havinga, J.; Beintema, J.J. !$#journal Eur. J. Biochem. (1980) 110:131-142 !$#title Pancreatic ribonucleases of mammals with ruminant-like !1digestion. Amino-acid sequences of hippopotamus and sloth !1ribonucleases. !$#cross-references MUID:81066627; PMID:7439154 !$#accession A00817 !'##molecule_type protein !'##residues 1-124 ##label HAV !'##note 37-Lys is found in about half of the molecules; this form of !1the enzyme does not bind carbohydrate CLASSIFICATION #superfamily pancreatic ribonuclease KEYWORDS glycoprotein; hydrolase; nucleic acid digestion; pancreas FEATURE !$12,41,119 #active_site His, Lys, His #status predicted\ !$26-84,40-95,58-110, !$65-72 #disulfide_bonds #status predicted\ !$34 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 124 #molecular-weight 14025 #checksum 7852 SEQUENCE /// ENTRY NRWHK #type complete TITLE pancreatic ribonuclease (EC 3.1.27.5) - minke whale ALTERNATE_NAMES RNase 1; RNase A ORGANISM #formal_name Balaenoptera acutorostrata #common_name minke whale, lesser rorqual DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 03-Jun-1994 ACCESSIONS A00818 REFERENCE A00818 !$#authors Emmens, M.; Welling, G.W.; Beintema, J.J. !$#journal Biochem. J. (1976) 157:317-323 !$#title The amino acid sequence of pike whale (lesser rorqual) !1pancreatic ribonuclease. !$#cross-references MUID:76277855; PMID:962870 !$#accession A00818 !'##molecule_type protein !'##residues 1-124 ##label EMM CLASSIFICATION #superfamily pancreatic ribonuclease KEYWORDS glycoprotein; hydrolase; nucleic acid digestion; pancreas FEATURE !$12,41,119 #active_site His, Lys, His #status predicted\ !$26-84,40-95,58-110, !$65-72 #disulfide_bonds #status predicted\ !$76 #binding_site carbohydrate (Asn) (covalent) (partial) !8#status experimental SUMMARY #length 124 #molecular-weight 14125 #checksum 8010 SEQUENCE /// ENTRY NRHO #type complete TITLE pancreatic ribonuclease (EC 3.1.27.5) - horse ALTERNATE_NAMES RNase 1; RNase A ORGANISM #formal_name Equus caballus #common_name domestic horse DATE 24-Apr-1984 #sequence_revision 17-Mar-1987 #text_change 31-Dec-1993 ACCESSIONS A91340; A00819 REFERENCE A91340 !$#authors Beintema, J.J. !$#journal FEBS Lett. (1985) 185:115-120 !$#title Mammalian ribonucleases. The absence of a glycosylated !1Asn-Pro-Thr sequence in horse ribonuclease and the presence !1of tryptophan at position 39 in horse and dromedary !1ribonuclease. !$#cross-references MUID:85204378; PMID:3922790 !$#accession A91340 !'##molecule_type protein !'##residues 1-128 ##label BEI REFERENCE A91222 !$#authors Scheffer, A.J.; Beintema, J.J. !$#journal Eur. J. Biochem. (1974) 46:221-233 !$#title Horse pancreatic ribonuclease. !$#cross-references MUID:74302367; PMID:4852291 !$#contents annotation; tentative sequence !$#note this sequence has been revised CLASSIFICATION #superfamily pancreatic ribonuclease KEYWORDS glycoprotein; hydrolase; nucleic acid digestion; pancreas FEATURE !$12,41,119 #active_site His, Lys, His #status predicted\ !$26-84,40-95,58-110, !$65-72 #disulfide_bonds #status predicted\ !$34,62 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 128 #molecular-weight 14374 #checksum 2587 SEQUENCE /// ENTRY NRKS #type complete TITLE pancreatic ribonuclease (EC 3.1.27.5) - casiragua ORGANISM #formal_name Proechimys guairae #common_name casiragua DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 30-Sep-1993 ACCESSIONS A00821 REFERENCE A90644 !$#authors Beintema, J.J.; Knol, G.; Martena, B. !$#journal Biochim. Biophys. Acta (1982) 705:102-110 !$#title The primary structures of pancreatic ribonucleases from !1African porcupine and casiragua, two hystricomorph rodent !1species. !$#cross-references MUID:83000399; PMID:7115727 !$#accession A00821 !'##molecule_type protein !'##residues 1-128 ##label BEI !'##note residues 67-78 were positioned primarily by homology with other !1ribonucleases CLASSIFICATION #superfamily pancreatic ribonuclease KEYWORDS glycoprotein; hydrolase; nucleic acid digestion; pancreas FEATURE !$12,41,119 #active_site His, Lys, His #status predicted\ !$26-84,40-95,58-110, !$65-72 #disulfide_bonds #status predicted\ !$34 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 128 #molecular-weight 14244 #checksum 1261 SEQUENCE /// ENTRY NRCB #type complete TITLE pancreatic ribonuclease (EC 3.1.27.5) - Chinchilla brevicaudata (tentative sequence) ALTERNATE_NAMES RNase 1; RNase A ORGANISM #formal_name Chinchilla brevicaudata, Chinchilla lanigera brevicaudata DATE 24-Apr-1984 #sequence_revision 30-Sep-1988 #text_change 31-Mar-2000 ACCESSIONS A00820 REFERENCE A90612 !$#authors van den Berg, A.; van den Hende-Timmer, L.; Beintema, J.J. !$#journal Biochim. Biophys. Acta (1976) 453:400-409 !$#title Isolation, properties and primary structure of coypu and !1chinchilla pancreatic ribonuclease. !$#cross-references MUID:77065676; PMID:999896 !$#accession A00820 !'##molecule_type protein !'##residues 1-124 ##label VAN !'##note a second component of chinchilla ribonuclease has 32-Asp CLASSIFICATION #superfamily pancreatic ribonuclease KEYWORDS glycoprotein; hydrolase; nucleic acid digestion; pancreas FEATURE !$12,41,119 #active_site His, Lys, His #status predicted\ !$26-84,40-95,58-110, !$65-72 #disulfide_bonds #status predicted\ !$34 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 124 #molecular-weight 13886 #checksum 8853 SEQUENCE /// ENTRY NRCU #type complete TITLE pancreatic ribonuclease (EC 3.1.27.5) - nutria (tentative sequence) ALTERNATE_NAMES RNase 1; RNase A ORGANISM #formal_name Myocastor coypus #common_name nutria, coypu DATE 24-Apr-1984 #sequence_revision 30-Sep-1988 #text_change 31-Mar-2000 ACCESSIONS A00822 REFERENCE A90612 !$#authors van den Berg, A.; van den Hende-Timmer, L.; Beintema, J.J. !$#journal Biochim. Biophys. Acta (1976) 453:400-409 !$#title Isolation, properties and primary structure of coypu and !1chinchilla pancreatic ribonuclease. !$#cross-references MUID:77065676; PMID:999896 !$#accession A00822 !'##molecule_type protein !'##residues 1-128 ##label VAN CLASSIFICATION #superfamily pancreatic ribonuclease KEYWORDS glycoprotein; hydrolase; nucleic acid digestion; pancreas FEATURE !$12,41,119 #active_site His, Lys, His #status predicted\ !$26-84,40-95,58-110, !$65-72 #disulfide_bonds #status predicted\ !$34 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 128 #molecular-weight 14267 #checksum 3470 SEQUENCE /// ENTRY NRGPA #type complete TITLE pancreatic ribonuclease (EC 3.1.27.5) A - guinea pig (tentative sequence) ALTERNATE_NAMES RNase IA ORGANISM #formal_name Cavia porcellus #common_name guinea pig DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 31-Mar-2000 ACCESSIONS A00825 REFERENCE A91247 !$#authors van den Berg, A.; van den Hende-Timmer, L.; Hofsteenge, J.; !1Gaastra, W.; Beintema, J.J. !$#journal Eur. J. Biochem. (1977) 75:91-100 !$#title Guinea pig pancreatic ribonucleases. Isolation, properties, !1primary structure and glycosidation. !$#cross-references MUID:77185023; PMID:862624 !$#accession A00825 !'##molecule_type protein !'##residues 1-124 ##label VAN CLASSIFICATION #superfamily pancreatic ribonuclease KEYWORDS glycoprotein; hydrolase; nucleic acid digestion; pancreas FEATURE !$12,41,119 #active_site His, Lys, His #status predicted\ !$26-84,40-95,58-110, !$65-72 #disulfide_bonds #status predicted\ !$62,94 #binding_site carbohydrate (Asn) (covalent) #status !8absent SUMMARY #length 124 #molecular-weight 13844 #checksum 7927 SEQUENCE /// ENTRY NRPQ #type complete TITLE pancreatic ribonuclease (EC 3.1.27.5) - crested porcupine ORGANISM #formal_name Hystrix cristata #common_name crested porcupine DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 30-Sep-1993 ACCESSIONS A00823 REFERENCE A90644 !$#authors Beintema, J.J.; Knol, G.; Martena, B. !$#journal Biochim. Biophys. Acta (1982) 705:102-110 !$#title The primary structures of pancreatic ribonucleases from !1African porcupine and casiragua, two hystricomorph rodent !1species. !$#cross-references MUID:83000399; PMID:7115727 !$#accession A00823 !'##molecule_type protein !'##residues 1-128 ##label BEI !'##note residues 67-78 were positioned primarily by homology with other !1ribonucleases !'##note 98-Arg was also found CLASSIFICATION #superfamily pancreatic ribonuclease KEYWORDS glycoprotein; hydrolase; nucleic acid digestion; pancreas FEATURE !$12,41,119 #active_site His, Lys, His #status predicted\ !$26-84,40-95,58-110, !$65-72 #disulfide_bonds #status predicted\ !$34 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 128 #molecular-weight 14273 #checksum 3892 SEQUENCE /// ENTRY NRYY #type complete TITLE pancreatic ribonuclease (EC 3.1.27.5) - capybara ALTERNATE_NAMES RNase 1; RNase A ORGANISM #formal_name Hydrochaeris hydrochaeris #common_name capybara, carpincho DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 29-Oct-1999 ACCESSIONS A00824 REFERENCE A92957 !$#authors Beintema, J.J.; Neuteboom, B. !$#journal J. Mol. Evol. (1983) 19:145-152 !$#title Origin of the duplicated ribonuclease gene in guinea-pig: !1comparison of the amino acid sequences with those of two !1close relatives: capybara and cuis ribonuclease. !$#cross-references MUID:87036770; PMID:6571219 !$#accession A00824 !'##molecule_type protein !'##residues 1-128 ##label BEI CLASSIFICATION #superfamily pancreatic ribonuclease KEYWORDS hydrolase; nucleic acid digestion; pancreas FEATURE !$12,41,119 #active_site His, Lys, His #status predicted\ !$26-84,40-95,58-110, !$65-72 #disulfide_bonds #status predicted SUMMARY #length 128 #molecular-weight 14345 #checksum 3487 SEQUENCE /// ENTRY NRGPB #type complete TITLE pancreatic ribonuclease (EC 3.1.27.5) B - guinea pig (tentative sequence) ALTERNATE_NAMES RNase IB ORGANISM #formal_name Cavia porcellus #common_name guinea pig DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 31-Mar-2000 ACCESSIONS A00826 REFERENCE A91247 !$#authors van den Berg, A.; van den Hende-Timmer, L.; Hofsteenge, J.; !1Gaastra, W.; Beintema, J.J. !$#journal Eur. J. Biochem. (1977) 75:91-100 !$#title Guinea pig pancreatic ribonucleases. Isolation, properties, !1primary structure and glycosidation. !$#cross-references MUID:77185023; PMID:862624 !$#accession A00826 !'##molecule_type protein !'##residues 1-128 ##label VAN !'##note 64-Pro was also found CLASSIFICATION #superfamily pancreatic ribonuclease KEYWORDS glycoprotein; hydrolase; nucleic acid digestion; pancreas FEATURE !$12,41,119 #active_site His, Lys, His #status predicted\ !$21,34 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$26-84,40-95,58-110, !$65-72 #disulfide_bonds #status predicted SUMMARY #length 128 #molecular-weight 14406 #checksum 3518 SEQUENCE /// ENTRY NRUI #type complete TITLE pancreatic ribonuclease (EC 3.1.27.5) - cuis ALTERNATE_NAMES RNase 1; RNase A ORGANISM #formal_name Galea musteloides #common_name cuis DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 04-Oct-1996 ACCESSIONS A00827 REFERENCE A92957 !$#authors Beintema, J.J.; Neuteboom, B. !$#journal J. Mol. Evol. (1983) 19:145-152 !$#title Origin of the duplicated ribonuclease gene in guinea-pig: !1comparison of the amino acid sequences with those of two !1close relatives: capybara and cuis ribonuclease. !$#cross-references MUID:87036770; PMID:6571219 !$#accession A00827 !'##molecule_type protein !'##residues 1-124 ##label BEI !'##note about one-third of the molecules lacked Ala-1 COMMENT The cuis is a rodent belonging to the same subfamily as the !1guinea pig. CLASSIFICATION #superfamily pancreatic ribonuclease KEYWORDS glycoprotein; hydrolase; nucleic acid digestion; pancreas FEATURE !$12,41,119 #active_site His, Lys, His #status predicted\ !$26-84,40-95,58-110, !$65-72 #disulfide_bonds #status predicted\ !$94 #binding_site carbohydrate (Asn) (covalent) #status !8absent SUMMARY #length 124 #molecular-weight 13870 #checksum 469 SEQUENCE /// ENTRY NROZ #type complete TITLE pancreatic ribonuclease (EC 3.1.27.5) - muskrat (tentative sequence) ALTERNATE_NAMES RNase 1; RNase A ORGANISM #formal_name Ondatra zibethicus #common_name muskrat DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 31-Mar-2000 ACCESSIONS A00828 REFERENCE A00828 !$#authors van Dijk, H.; Sloots, B.; van den Berg, A.; Gaastra, W.; !1Beintema, J.J. !$#journal Int. J. Pept. Protein Res. (1976) 8:305-316 !$#title The primary structure of muskrat pancreatic ribonuclease. !$#cross-references MUID:76212474; PMID:1279085 !$#accession A00828 !'##molecule_type protein !'##residues 1-124 ##label VAN !'##note the placement of residues 32-33 and 75-76 is tentative CLASSIFICATION #superfamily pancreatic ribonuclease KEYWORDS glycoprotein; hydrolase; nucleic acid digestion; pancreas FEATURE !$12,41,119 #active_site His, Lys, His #status predicted\ !$26-84,40-95,58-110, !$65-72 #disulfide_bonds #status predicted\ !$62 #binding_site carbohydrate (Asn) (covalent) #status !8absent SUMMARY #length 124 #molecular-weight 13879 #checksum 9997 SEQUENCE /// ENTRY NRHY #type complete TITLE pancreatic ribonuclease (EC 3.1.27.5) - golden hamster (tentative sequence) ALTERNATE_NAMES RNase 1; RNase A ORGANISM #formal_name Mesocricetus auratus #common_name golden hamster DATE 30-Nov-1980 #sequence_revision 30-Nov-1980 #text_change 31-Mar-2000 ACCESSIONS A00829 REFERENCE A00829 !$#authors Jekel, P.A.; Sips, H.J.; Lenstra, J.A.; Beintema, J.J. !$#journal Biochimie (1979) 61:827-839 !$#title The amino acid sequence of hamster pancreatic ribonuclease. !$#cross-references MUID:80088445; PMID:518928 !$#accession A00829 !'##molecule_type protein !'##residues 1-124 ##label JEK CLASSIFICATION #superfamily pancreatic ribonuclease KEYWORDS glycoprotein; hydrolase; nucleic acid digestion; pancreas FEATURE !$12,41,119 #active_site His, Lys, His #status predicted\ !$26-84,40-95,58-110, !$65-72 #disulfide_bonds #status predicted\ !$34 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 124 #molecular-weight 13867 #checksum 7939 SEQUENCE /// ENTRY NRMS #type complete TITLE pancreatic ribonuclease (EC 3.1.27.5) precursor - mouse ALTERNATE_NAMES RNase 1; RNase A ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Nov-1980 #sequence_revision 13-Mar-1997 #text_change 18-Jun-1999 ACCESSIONS A34090; S22598; A00830 REFERENCE A34090 !$#authors Schueller, C.; Nijssen, H.M.J.; Kok, R.; Beintema, J.J. !$#journal Mol. Biol. Evol. (1990) 7:29-44 !$#title Evolution of nucleic acids coding for ribonucleases: the !1mRNA sequence of mouse pancreatic ribonuclease. !$#cross-references MUID:90136034; PMID:2299980 !$#accession A34090 !'##status preliminary !'##molecule_type mRNA !'##residues 1-149 ##label SCH !'##cross-references GB:M27814; NID:g200762; PIDN:AAA40060.1; !1PID:g200763 REFERENCE S22598 !$#authors Samuelson, L.C.; Wiebauer, K.; Howard, G.; Schmid, R.M.; !1Koeplin, D.; Meisler, M.H. !$#journal Nucleic Acids Res. (1991) 19:6935-6941 !$#title Isolation of the murine ribonuclease gene Rib-1: structure !1and tissue specific expression in pancreas and parotid !1gland. !$#cross-references MUID:92107684; PMID:1840677 !$#accession S22598 !'##status preliminary !'##molecule_type DNA !'##residues 1-149 ##label SAM !'##cross-references EMBL:X60103; NID:g53981; PIDN:CAA42697.1; !1PID:g53982 REFERENCE A00830 !$#authors Lenstra, J.A.; Beintema, J.J. !$#journal Eur. J. Biochem. (1979) 98:399-408 !$#title The amino acid sequence of mouse pancreatic ribonuclease. !$#cross-references MUID:80024269; PMID:556267 !$#accession A00830 !'##molecule_type protein !'##residues 26-149 ##label LEN CLASSIFICATION #superfamily pancreatic ribonuclease KEYWORDS glycoprotein; hydrolase; nucleic acid digestion; pancreas FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-149 #product pancreatic ribonuclease #status experimental !8#label MAT\ !$37,66,144 #active_site His, Lys, His #status predicted\ !$51-109,65-120, !$83-135,90-97 #disulfide_bonds #status predicted\ !$62,87 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 149 #molecular-weight 16820 #checksum 2040 SEQUENCE /// ENTRY NRRT #type complete TITLE pancreatic ribonuclease (EC 3.1.27.5) precursor - rat ALTERNATE_NAMES RNase 1; RNase A ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 03-Jun-1994 ACCESSIONS A92356; A90585; A91313; A00831 REFERENCE A92356 !$#authors MacDonald, R.J.; Stary, S.J.; Swift, G.H. !$#journal J. Biol. Chem. (1982) 257:14582-14585 !$#title Rat pancreatic ribonuclease messenger RNA. The nucleotide !1sequence of the entire mRNA and the derived amino acid !1sequence of the pre-enzyme. !$#cross-references MUID:83082740; PMID:7174650 !$#accession A92356 !'##molecule_type mRNA !'##residues 1-152 ##label MAC REFERENCE A90585 !$#authors Beintema, J.J.; Gruber, M. !$#journal Biochim. Biophys. Acta (1973) 310:161-173 !$#title Rat pancreatic ribonuclease. II. Amino acid sequence. !$#cross-references MUID:73194545; PMID:4710592 !$#accession A90585 !'##molecule_type protein !'##residues 26-97,'D',99-123,'T',125,'N',127-128,'N',130,'E',132-152 !1##label BEI REFERENCE A91313 !$#authors Beintema, J.J. !$#journal FEBS Lett. (1983) 159:191-195 !$#title Rat pancreatic ribonuclease: agreement between the corrected !1amino acid sequence and the sequence derived from its !1messenger RNA. !$#cross-references MUID:83262417; PMID:6873294 !$#accession A91313 !'##molecule_type protein !'##residues 26-152 ##label BE2 CLASSIFICATION #superfamily pancreatic ribonuclease KEYWORDS hydrolase; nucleic acid digestion; pancreas FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-152 #product pancreatic ribonuclease #status experimental !8#label MAT\ !$40,69,147 #active_site His, Lys, His #status predicted\ !$54-112,68-123, !$86-138,93-100 #disulfide_bonds #status predicted SUMMARY #length 152 #molecular-weight 16823 #checksum 1644 SEQUENCE /// ENTRY NROW2 #type complete TITLE pancreatic ribonuclease (EC 3.1.27.5) - Hoffmann's two-fingered sloth (tentative sequence) ALTERNATE_NAMES RNase 1; RNase A ORGANISM #formal_name Choloepus hoffmanni #common_name Hoffmann's two-fingered sloth DATE 31-Dec-1980 #sequence_revision 31-Dec-1980 #text_change 31-Mar-2000 ACCESSIONS A00832 REFERENCE A91099 !$#authors Havinga, J.; Beintema, J.J. !$#journal Eur. J. Biochem. (1980) 110:131-142 !$#title Pancreatic ribonucleases of mammals with ruminant-like !1digestion. Amino-acid sequences of hippopotamus and sloth !1ribonucleases. !$#cross-references MUID:81066627; PMID:7439154 !$#accession A00832 !'##molecule_type protein !'##residues 1-128 ##label HAV CLASSIFICATION #superfamily pancreatic ribonuclease KEYWORDS glycoprotein; hydrolase; nucleic acid digestion; pancreas FEATURE !$12,41,119 #active_site His, Lys, His #status predicted\ !$26-84,40-95,58-110, !$65-72 #disulfide_bonds #status predicted\ !$34 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 128 #molecular-weight 14492 #checksum 3420 SEQUENCE /// ENTRY NRKGR #type complete TITLE pancreatic ribonuclease (EC 3.1.27.5) - red kangaroo ALTERNATE_NAMES RNase 1; RNase A ORGANISM #formal_name Macropus rufus, Megaleia rufa #common_name red kangaroo DATE 30-Nov-1980 #sequence_revision 30-Nov-1980 #text_change 04-Oct-1996 ACCESSIONS A00833 REFERENCE A00833 !$#authors Gaastra, W.; Welling, G.W.; Beintema, J.J. !$#journal Eur. J. Biochem. (1978) 86:209-217 !$#title The amino-acid sequence of kangaroo pancreatic ribonuclease. !$#cross-references MUID:78190621; PMID:658039 !$#accession A00833 !'##molecule_type protein !'##residues 1-122 ##label GAA CLASSIFICATION #superfamily pancreatic ribonuclease KEYWORDS glycoprotein; hydrolase; nucleic acid digestion; pancreas FEATURE !$11,40,117 #active_site His, Lys, His #status predicted\ !$25-83,39-94,57-109, !$64-71 #disulfide_bonds #status predicted\ !$61 #binding_site carbohydrate (Asn) (covalent) #status !8absent SUMMARY #length 122 #molecular-weight 13831 #checksum 7436 SEQUENCE /// ENTRY NRBOK2 #type complete TITLE pancreatic-type ribonuclease (EC 3.1.27.5) K2, nonsecretory - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 09-Jun-1994 ACCESSIONS JX0047 REFERENCE JX0047 !$#authors Irie, M.; Nitta, R.; Ohgi, K.; Niwata, Y.; Watanabe, H.; !1Iwama, M.; Beintema, J.J.; Sanda, A.; Takizawa, Y. !$#journal J. Biochem. (1988) 104:289-296 !$#title Primary structure of a non-secretory ribonuclease from !1bovine kidney. !$#cross-references MUID:89034023; PMID:3182769 !$#accession JX0047 !'##molecule_type protein !'##residues 1-127 ##label IRI COMMENT Ribonuclease K2 is a nonsecretory ribonuclease specific for !1the 3' ends of pyrimidine nucleotides. CLASSIFICATION #superfamily pancreatic ribonuclease KEYWORDS glycoprotein; hydrolase; kidney; nucleic acid degradation FEATURE !$15,38,117 #active_site His, Lys, His #status predicted\ !$23-81,37-91,55-106, !$62-69 #disulfide_bonds #status predicted\ !$32,77 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 127 #molecular-weight 14770 #checksum 8262 SEQUENCE /// ENTRY NRST #type complete TITLE pancreatic ribonuclease (EC 3.1.27.5) - snapping turtle ORGANISM #formal_name Chelydra serpentina #common_name snapping turtle DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 04-Oct-1996 ACCESSIONS A91155; B94696; A00834 REFERENCE A91155 !$#authors Beintema, J.J.; Broos, J.; Meulenberg, J.; Schuller, C. !$#journal Eur. J. Biochem. (1985) 153:305-312 !$#title The amino acid sequence of snapping turtle (Chelydra !1serpentina) ribonuclease. !$#cross-references MUID:86081767; PMID:4076178 !$#accession A91155 !'##molecule_type protein !'##residues 1-119 ##label BEI !'##note peptides were positioned in part by homology REFERENCE A94696 !$#authors Barnard, E.A.; Cohen, M.S.; Gold, M.H.; Kim, J.K. !$#journal Nature (1972) 240:395-398 !$#title Evolution of ribonuclease in relation to polypeptide folding !1mechanisms. !$#cross-references MUID:73045781; PMID:4564316 !$#accession B94696 !'##molecule_type protein !'##residues 1-30 ##label BAR CLASSIFICATION #superfamily pancreatic ribonuclease KEYWORDS glycoprotein; hydrolase; nucleic acid digestion; pancreas FEATURE !$11,41,114 #active_site His, Lys, His #status predicted\ !$26-81,40-92,58-107 #disulfide_bonds #status predicted\ !$73 #binding_site carbohydrate (Asn) (covalent) #status !8absent SUMMARY #length 119 #molecular-weight 12915 #checksum 5867 SEQUENCE /// ENTRY JX0120 #type complete TITLE ribonuclease-related sialic acid-binding lectin - Japanese frog ORGANISM #formal_name Rana japonica #common_name Japanese frog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JX0120 REFERENCE JX0120 !$#authors Kamiya, Y.; Oyama, F.; Oyama, R.; Sakakibara, F.; Nitta, K.; !1Kawauchi, H.; Takayanagi, Y.; Titani, K. !$#journal J. Biochem. (1990) 108:139-143 !$#title Amino acid sequence of a lectin from Japanese frog (Rana !1japonica) eggs. !$#cross-references MUID:91035319; PMID:2229005 !$#accession JX0120 !'##molecule_type protein !'##residues 1-111 ##label KAM !'##experimental_source egg CLASSIFICATION #superfamily pancreatic ribonuclease KEYWORDS lectin; pyroglutamic acid FEATURE !$1 #modified_site pyrrolidone carboxylic acid (Gln) !8#status experimental\ !$19-72,34-82,52-97, !$94-111 #disulfide_bonds #status experimental SUMMARY #length 111 #molecular-weight 12326 #checksum 9205 SEQUENCE /// ENTRY NRHUAG #type complete TITLE angiogenin precursor [validated] - human ALTERNATE_NAMES angiogenesis factor CONTAINS ribonuclease (EC 3.1.27.-) ORGANISM #formal_name Homo sapiens #common_name man DATE 13-Aug-1986 #sequence_revision 13-Aug-1986 #text_change 15-Sep-2000 ACCESSIONS A90498; A90497; A00835 REFERENCE A90498 !$#authors Kurachi, K.; Davie, E.W.; Strydom, D.J.; Riordan, J.F.; !1Vallee, B.L. !$#journal Biochemistry (1985) 24:5494-5499 !$#title Sequence of the cDNA and gene for angiogenin, a human !1angiogenesis factor. !$#cross-references MUID:86077688; PMID:2866795 !$#accession A90498 !'##molecule_type mRNA !'##residues 1-147 ##label KUR !'##cross-references GB:M11567; NID:g178249; PIDN:AAA51678.1; !1PID:g178250 !'##experimental_source colon adenocarcinoma cell line HT-29 !'##note the authors do not known whether Met-1 or Met-3 is the !1initiator REFERENCE A90497 !$#authors Strydom, D.J.; Fett, J.W.; Lobb, R.R.; Alderman, E.M.; !1Bethune, J.L.; Riordan, J.F.; Vallee, B.L. !$#journal Biochemistry (1985) 24:5486-5494 !$#title Amino acid sequence of human tumor derived angiogenin. !$#cross-references MUID:86077687; PMID:2866794 !$#accession A90497 !'##molecule_type protein !'##residues 25-147 ##label STR !'##experimental_source colon adenocarcinoma cell line HT-29 !'##note disulfide bonds were determined REFERENCE A30634 !$#authors Saxena, S.K.; Rybak, S.M.; Davey Jr., R.T.; Youle, R.J.; !1Ackerman, E.J. !$#journal J. Biol. Chem. (1992) 267:21982-21986 !$#title Angiogenin is a cytotoxic, tRNA-specific ribonuclease in the !1RNase A superfamily. !$#cross-references MUID:93016165; PMID:1400510 !$#contents annotation; enzyme activity REFERENCE A68734 !$#authors Acharya, K.R.; Allen, S.; Shapiro, R.; Riordan, J.F.; !1Vallee, B.L. !$#submission submitted to the Brookhaven Protein Data Bank, January 1994 !$#cross-references PDB:1ANG !$#contents annotation; X-ray crystallography, 2.4 angstroms, residues !125-147 REFERENCE A54934 !$#authors Acharya, K.R.; Shapiro, R.; Allen, S.C.; Riordan, J.F.; !1Vallee, B.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1994) 91:2915-2919 !$#title Crystal structure of human angiogenin reveals the structural !1basis for its functional divergence from ribonuclease. !$#cross-references MUID:94211772; PMID:8159679 !$#contents annotation; X-ray crystallography, 2.4 angstroms GENETICS !$#gene GDB:ANG; RNASE5 !'##cross-references GDB:119679; OMIM:105850 !$#map_position 14q11.1-14q11.2 FUNCTION !$#description hydrolyzes tRNA; induces vascularization of normal and !1malignant tissues CLASSIFICATION #superfamily pancreatic ribonuclease KEYWORDS angiogenesis; hydrolase; nucleic acid degradation; !1pyroglutamic acid FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-147 #product angiogenin #status experimental #label MAT\ !$25 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$37,64,138 #active_site His, Lys, His #status predicted\ !$50-105,63-116, !$81-131 #disulfide_bonds #status experimental SUMMARY #length 147 #molecular-weight 16550 #checksum 7959 SEQUENCE /// ENTRY A35932 #type complete TITLE angiogenin precursor - mouse ALTERNATE_NAMES angiogenesis factor CONTAINS ribonuclease (EC 3.1.27.-) ORGANISM #formal_name Mus musculus #common_name house mouse DATE 09-Nov-1990 #sequence_revision 09-Nov-1990 #text_change 18-Jun-1999 ACCESSIONS A35932 REFERENCE A35932 !$#authors Bond, M.D.; Vallee, B.L. !$#journal Biochem. Biophys. Res. Commun. (1990) 171:988-995 !$#title Isolation and sequencing of mouse angiogenin DNA. !$#cross-references MUID:91025023; PMID:2222458 !$#accession A35932 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-145 ##label BON !'##cross-references GB:U22516; NID:g726325; PIDN:AAA91366.1; !1PID:g726326 GENETICS !$#introns #status absent FUNCTION !$#description hydrolyzes tRNA; induces vascularization of normal and !1malignant tissues CLASSIFICATION #superfamily pancreatic ribonuclease KEYWORDS angiogenesis; hydrolase; nucleic acid degradation; !1pyroglutamic acid FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-145 #product angiogenin #status predicted #label MAT\ !$25 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status predicted\ !$37,64,137 #active_site His, Lys, His #status predicted\ !$50-104,63-115, !$81-130 #disulfide_bonds #status predicted SUMMARY #length 145 #molecular-weight 16228 #checksum 1411 SEQUENCE /// ENTRY B43825 #type complete TITLE angiogenin - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S29833; B43825 REFERENCE S29833 !$#authors Bond, M.D.; Strydom, D.J.; Vallee, B.L. !$#journal Biochim. Biophys. Acta (1993) 1162:177-186 !$#title Characterization and sequencing of rabbit, pig and mouse !1angiogenins: discernment of functionally important residues !1and regions. !$#cross-references MUID:93192291; PMID:8448182 !$#accession S29833 !'##status preliminary !'##molecule_type protein !'##residues 1-125 ##label BON !'##note submitted to the Protein Sequence Database, December 1992 CLASSIFICATION #superfamily pancreatic ribonuclease KEYWORDS pyroglutamic acid FEATURE !$1 #modified_site pyrrolidone carboxylic acid (Gln) !8#status experimental SUMMARY #length 125 #molecular-weight 14361 #checksum 8657 SEQUENCE /// ENTRY A43825 #type complete TITLE angiogenin - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S29834; A43825 REFERENCE S29833 !$#authors Bond, M.D.; Strydom, D.J.; Vallee, B.L. !$#journal Biochim. Biophys. Acta (1993) 1162:177-186 !$#title Characterization and sequencing of rabbit, pig and mouse !1angiogenins: discernment of functionally important residues !1and regions. !$#cross-references MUID:93192291; PMID:8448182 !$#accession S29834 !'##status preliminary !'##molecule_type protein !'##residues 1-123 ##label BON !'##note this sequence was submitted to the Protein Sequence Database, !1December 1992 CLASSIFICATION #superfamily pancreatic ribonuclease SUMMARY #length 123 #molecular-weight 14058 #checksum 2920 SEQUENCE /// ENTRY A32474 #type complete TITLE angiogenin [validated] - bovine ALTERNATE_NAMES angiogenesis factor CONTAINS ribonuclease (EC 3.1.27.-) ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 25-Sep-1989 #sequence_revision 25-Sep-1989 #text_change 15-Sep-2000 ACCESSIONS A32474; S02001; A30044; S48212 REFERENCE A32474 !$#authors Bond, M.D.; Strydom, D.J. !$#journal Biochemistry (1989) 28:6110-6113 !$#title Amino acid sequence of bovine angiogenin. !$#cross-references MUID:89375344; PMID:2775757 !$#accession A32474 !'##molecule_type protein !'##residues 1-125 ##label BON !'##experimental_source plasma REFERENCE S02001 !$#authors Maes, P.; Damart, D.; Rommens, C.; Montreuil, J.; Spik, G.; !1Tartar, A. !$#journal FEBS Lett. (1988) 241:41-45 !$#title The complete amino acid sequence of bovine milk angiogenin. !$#cross-references MUID:89065101; PMID:3197838 !$#accession S02001 !'##molecule_type protein !'##residues 1-125 ##label MAE !'##experimental_source milk REFERENCE A65065 !$#authors Acharya, K.R.; Shapiro, R.; Riordan, J.F.; Vallee, B.L. !$#submission submitted to the Brookhaven Protein Data Bank, January 1995 !$#cross-references PDB:1AGI !$#contents annotation; X-ray crystallography, 1.5 angstroms, residues !11-125 REFERENCE A58315 !$#authors Acharya, K.R.; Shapiro, R.; Riordan, J.F.; Vallee, B.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1995) 92:2949-2953 !$#title Crystal structure of bovine angiogenin at 1.5 Angstroms !1resolution. !$#cross-references MUID:95224057; PMID:7708754 !$#contents annotation; X-ray crystallography, 1.5 angstroms REFERENCE A65709 !$#authors Lequin, O.; Albaret, C.; Bontems, F.; Spik, G.; Lallemand, !1J.Y. !$#submission submitted to the Brookhaven Protein Data Bank, April 1996 !$#cross-references PDB:1GIO !$#contents annotation; conformation by (1)H-NMR, residues 1-125 REFERENCE A58821 !$#authors Lequin, O.; Albaret, C.; Bontems, F.; Spik, G.; Lallemand, !1J.Y. !$#journal Biochemistry (1996) 35:8870-8880 !$#title Solution structure of bovine angiogenin by (1)H nuclear !1magnetic resonance spectroscopy. !$#cross-references MUID:96280645; PMID:8688423 !$#contents annotation; conformation by (1)H-NMR REFERENCE S48212 !$#authors Reisdorf, C.; Abergel, D.; Bontems, F.; Lallemand, J.Y.; !1Decottignies, J.P.; Spik, G. !$#journal Eur. J. Biochem. (1994) 224:811-822 !$#title Proton resonance assignments and secondary structure of !1bovine angiogenin. !$#cross-references MUID:95010071; PMID:7925406 !$#contents annotation; conformation by (1)H-NMR FUNCTION !$#description hydrolyzes tRNA; induces vascularization of normal and !1malignant tissues CLASSIFICATION #superfamily pancreatic ribonuclease KEYWORDS angiogenesis; hydrolase; nucleic acid degradation FEATURE !$60-68 #region receptor binding #status predicted\ !$14,41,115 #active_site His, Lys, His #status predicted\ !$27-82,40-93,58-108 #disulfide_bonds #status experimental SUMMARY #length 125 #molecular-weight 14593 #checksum 6368 SEQUENCE /// ENTRY JQ0777 #type complete TITLE Enterobacter ribonuclease (EC 3.1.27.6) I precursor - Escherichia coli (strain K-12) ALTERNATE_NAMES ribonuclease I ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS JQ0777; A64795 REFERENCE JQ0777 !$#authors Meador III, J.; Kennell, D. !$#journal Gene (1990) 95:1-7 !$#title Cloning and sequencing the gene encoding Escherichia coli !1ribonuclease I: exact physical mapping using the genome !1library. !$#cross-references MUID:91071590; PMID:2253883 !$#accession JQ0777 !'##status preliminary !'##molecule_type DNA !'##residues 1-268 ##label MEA !'##cross-references GB:M55687; GB:M37486; NID:g147652; PIDN:AAA24548.1; !1PID:g147653 !'##experimental_source K12 strain W3110 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64795 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-268 ##label BLAT !'##cross-references GB:AE000166; GB:U00096; NID:g1786819; !1PIDN:AAC73712.1; PID:g1786828; UWGP:b0611 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene rna; rnsA !$#map_position 14 min CLASSIFICATION #superfamily Enterobacter ribonuclease KEYWORDS endonuclease; hydrolase FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-268 #product Enterobacter ribonuclease #status predicted !8#label MAT SUMMARY #length 268 #molecular-weight 29617 #checksum 1962 SEQUENCE /// ENTRY LNNTSA #type complete TITLE ribonuclease (EC 3.1.27.-) S2 precursor - Persian tobacco ALTERNATE_NAMES stylar glycoprotein 2 ORGANISM #formal_name Nicotiana alata #common_name Persian tobacco DATE 13-Aug-1986 #sequence_revision 13-Aug-1986 #text_change 18-Jun-1999 ACCESSIONS S57782; A03368 REFERENCE S57782 !$#authors Matton, D.P.; Mau, S.L.; Okamoto, S.; Clarke, A.E.; !1Newbigin, E. !$#journal Plant Mol. Biol. (1995) 28:847-858 !$#title The S-locus of Nicotiana alata: genomic organization and !1sequence analysis of two S-RNase alleles. !$#cross-references MUID:95367646; PMID:7640357 !$#accession S57782 !'##status preliminary !'##molecule_type DNA !'##residues 1-214 ##label MATT !'##cross-references EMBL:U08860; NID:g482812; PIDN:AAB40027.1; !1PID:g482813 REFERENCE A28819 !$#authors Anderson, M.A.; Cornish, E.C.; Mau, S.L.; Williams, E.G.; !1Hoggart, R.; Atkinson, A.; Bonig, I.; Grego, B.; Simpson, !1R.; Roche, P.J.; Haley, J.D.; Penschow, J.D.; Niall, H.D.; !1Tregear, G.W.; Coghlan, J.P.; Crawford, R.J.; Clarke, A.E. !$#journal Nature (1986) 321:38-44 !$#title Cloning of cDNA for a stylar glycoprotein associated with !1expression of self-incompatibility in Nicotiana alata. !$#accession A03368 !'##molecule_type mRNA !'##residues 1-214 ##label AND !'##cross-references EMBL:X03803; NID:g19670; PIDN:CAA27428.1; !1PID:g19671 REFERENCE A57401 !$#authors Oxley, D.; Bacic, A. !$#journal Glycobiology (1995) 5:517-523 !$#title Microheterogeneity of N-glycosylation on a stylar !1self-incompatibility glycoprotein of Nicotiana alata. !$#cross-references MUID:96089544; PMID:8563138 !$#contents annotation; glycosylation sites characterized by mass !1spectrometry !$#note sequence supported by peptide compositions GENETICS !$#gene S-2 !$#introns 77/3 FUNCTION !$#description hydrolyzes internal phosphodiester bonds of RNA to produce !13'-phosphomononucleotides !$#note involved in self-incompatibility of flowering plants CLASSIFICATION #superfamily Enterobacter ribonuclease KEYWORDS angiosperm reproduction; glycoprotein; hydrolase FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-214 #product ribonuclease S2 #status experimental #label !8MAT\ !$49,59,160 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$53,109,113 #active_site His, Glu, His #status predicted\ !$67-116,175-204 #disulfide_bonds #status predicted\ !$172 #binding_site carbohydrate (Asn) (covalent) #status !8absent SUMMARY #length 214 #molecular-weight 24875 #checksum 1120 SEQUENCE /// ENTRY LNNTS6 #type complete TITLE ribonuclease (EC 3.1.27.-) S6 precursor - Persian tobacco ALTERNATE_NAMES stylar glycoprotein 6 ORGANISM #formal_name Nicotiana alata #common_name Persian tobacco DATE 04-Dec-1992 #sequence_revision 01-Dec-1995 #text_change 20-Apr-2001 ACCESSIONS JQ1079; PQ0196; S39943; S57783; S58930 REFERENCE JQ1078 !$#authors Anderson, M.A.; McFadden, G.I.; Bernatzky, R.; Atkinson, A.; !1Orpin, T.; Dedman, H.; Tregear, G.; Fernley, R.; Clarke, !1A.E. !$#journal Plant Cell (1989) 1:483-491 !$#title Sequence variability of three alleles of the !1self-incompatibility gene of Nicotiana alata. !$#cross-references MUID:92404716; PMID:2535547 !$#accession JQ1079 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-215 ##label AND REFERENCE PQ0192 !$#authors Mau, S.L.; Williams, E.G.; Atkinson, A.; Anderson, M.A.; !1Cornish, E.C.; Grego, B.; Simpson, R.J.; Kheyr-Pour, A.; !1Clarke, A.E. !$#journal Planta (1986) 169:184-191 !$#title Style proteins of a wild tomato (Lycopersicon peruvianum) !1associated with expression of self-incompatibility. !$#accession PQ0196 !'##molecule_type protein !'##residues 23-37 ##label MAU !'##experimental_source style REFERENCE S39930 !$#authors Sassa, H.; Hirano, H.; Ikehashi, H. !$#journal Mol. Gen. Genet. (1993) 241:17-25 !$#title Identification and characterization of stylar glycoproteins !1associated with self-incompatibility genes of Japanese pear, !1Pyrus serotina Rehd. !$#cross-references MUID:94049676; PMID:8232200 !$#accession S39943 !'##status preliminary !'##molecule_type protein !'##residues 23-36 ##label SAS REFERENCE S57782 !$#authors Matton, D.P.; Mau, S.L.; Okamoto, S.; Clarke, A.E.; !1Newbigin, E. !$#journal Plant Mol. Biol. (1995) 28:847-858 !$#title The S-locus of Nicotiana alata: genomic organization and !1sequence analysis of two S-RNase alleles. !$#cross-references MUID:95367646; PMID:7640357 !$#accession S57783 !'##molecule_type DNA !'##residues 1-182,'E',184-215 ##label MAT1 !'##cross-references EMBL:U08861; NID:g482814; PIDN:AAB40028.1; !1PID:g482815 !'##note the authors translated the codon ACA for residue 206 as Pro REFERENCE S58930 !$#authors Matton, D.P.; Mau, S.; Okamoto, S.; Haring, V.; Anderson, !1M.A.; Clarke, A.E.; Newbigin, E. !$#submission submitted to the EMBL Data Library, April 1994 !$#description The S-locus of Nicotiana alata: genomic organization and !1sequence analysis of two S-RNase alleles. !$#accession S58930 !'##molecule_type DNA !'##residues 1-35,'T',37-182,'E',184-215 ##label MAT2 !'##cross-references EMBL:U08861; NID:g482814; PIDN:AAB40028.1; !1PID:g482815 GENETICS !$#gene S-6 !$#introns 77/3 FUNCTION !$#description hydrolyzes internal phosphodiester bonds of RNA to produce !13'-phosphomononucleotides !$#note involved in self-incompatibility of flowering plants CLASSIFICATION #superfamily Enterobacter ribonuclease KEYWORDS angiosperm reproduction; glycoprotein; hydrolase FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-215 #product ribonuclease S6 #status predicted #label !8MAT\ !$49,59,160 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$53,109,113 #active_site His, Glu, His #status predicted\ !$67-116,175-204 #disulfide_bonds #status predicted SUMMARY #length 215 #molecular-weight 24778 #checksum 7103 SEQUENCE /// ENTRY S28611 #type complete TITLE ribonuclease X2 (EC 3.1.-.-) precursor - Petunia inflata ORGANISM #formal_name Petunia inflata DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S28611; S28958 REFERENCE S28611 !$#authors Lee, H.S.; Singh, A.; Kao, T.H. !$#journal Plant Mol. Biol. (1992) 20:1131-1141 !$#title RNase X2, a pistil-specific ribonuclease from Petunia !1inflata, shares sequence similarity with solanaceous S !1proteins. !$#cross-references MUID:93099263; PMID:1463846 !$#accession S28611 !'##molecule_type DNA !'##residues 1-215 ##label LEE !'##cross-references EMBL:M93418 !$#accession S28958 !'##molecule_type protein !'##residues 23-55 ##label LE2 GENETICS !$#gene rnx2 !$#introns 80/3 CLASSIFICATION #superfamily Enterobacter ribonuclease KEYWORDS hydrolase FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-215 #product ribonuclease X2 #status experimental #label !8MAT SUMMARY #length 215 #molecular-weight 24730 #checksum 9468 SEQUENCE /// ENTRY S22516 #type complete TITLE S-allele-associated glycoprotein Sx precursor - garden petunia ALTERNATE_NAMES style glycoprotein S1 ORGANISM #formal_name Petunia x hybrida #common_name garden petunia DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 20-Apr-2001 ACCESSIONS S22516; S18610; PH0109 REFERENCE S22516 !$#authors Ai, Y.; Tsai, D.S.; Kao, T. !$#journal Plant Mol. Biol. (1992) 19:523-528 !$#title Cloning and sequencing of cDNAs encoding two S proteins of a !1self-compatible cultivar of Petunia hybrida. !$#cross-references MUID:92322988; PMID:1344883 !$#accession S22516 !'##molecule_type mRNA !'##residues 1-220 ##label AIY !'##cross-references EMBL:M81685; NID:g169247; PIDN:AAA33729.1; !1PID:g169248 REFERENCE S18610 !$#authors Ai, Y.; Kron, E.; Kao, T. !$#journal Mol. Gen. Genet. (1991) 230:353-358 !$#title S-alleles are retained and expressed in a self-compatible !1cultivar of Petunia hybrida. !$#cross-references MUID:92114864; PMID:1766433 !$#accession S18610 !'##molecule_type protein !'##residues 23-44 ##label AIA REFERENCE PH0109 !$#authors Broothaerts, W.J.; van Laere, A.; Witters, R.; Preaux, G.; !1Decock, B.; van Damme, J.; Vendrig, J.C. !$#journal Plant Mol. Biol. (1990) 14:93-102 !$#title Purification and N-terminal sequencing of style !1glycoproteins associated with self-incompatibility in !1Petunia hybrida. !$#cross-references MUID:91322492; PMID:2101314 !$#accession PH0109 !'##status preliminary !'##molecule_type protein !'##residues 23-37,'X',39-42 ##label BRO FUNCTION !$#description this protein is linked to self-incompatibility in flowering !1plants CLASSIFICATION #superfamily Enterobacter ribonuclease KEYWORDS angiosperm reproduction; glycoprotein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-220 #product S-allele-associated protein Sx #status !8experimental #label MAT\ !$52 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 220 #molecular-weight 25845 #checksum 1699 SEQUENCE /// ENTRY S20989 #type complete TITLE S1 protein - Petunia inflata ORGANISM #formal_name Petunia inflata DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S20989 REFERENCE S20989 !$#authors Coleman, C.E.; Kao, T. !$#journal Plant Mol. Biol. (1992) 18:725-737 !$#title The flanking regions of two Petunia inflata S alleles are !1heterogeneous and contain repetitive sequences. !$#cross-references MUID:92216048; PMID:1558946 !$#accession S20989 !'##status preliminary !'##molecule_type DNA !'##residues 1-222 ##label COL !'##cross-references EMBL:M67990; NID:g169241; PIDN:AAA33726.1; !1PID:g169242 GENETICS !$#introns 79/3 CLASSIFICATION #superfamily Enterobacter ribonuclease KEYWORDS glycoprotein SUMMARY #length 222 #molecular-weight 26206 #checksum 741 SEQUENCE /// ENTRY JX0295 #type complete TITLE ribonuclease (EC 3.1.27.-), nonspecific - Japanese oyster ORGANISM #formal_name Crassostrea gigas #common_name Japanese oyster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JX0295 REFERENCE JX0295 !$#authors Watanabe, H.; Narumi, H.; Inaba, T.; Ohgi, K.; Irie, M. !$#journal J. Biochem. (1993) 114:800-807 !$#title Purification, some properties, and primary structure of a !1base non-specific ribonuclease from oyster (Crussdstrea !1grigus). !$#cross-references MUID:94186499; PMID:8138535 !$#note the source is designated as Crussdstrea grigus !$#accession JX0295 !'##molecule_type protein !'##residues 1-213 ##label WAT CLASSIFICATION #superfamily Enterobacter ribonuclease KEYWORDS endonuclease; glycoprotein; hydrolase FEATURE !$35,88,89,93 #active_site His, His, Glu, His #status predicted\ !$52,121,142 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 213 #molecular-weight 24360 #checksum 7203 SEQUENCE /// ENTRY JH0367 #type complete TITLE ribonuclease (EC 3.1.27.-) Rh precursor - Rhizopus niveus ALTERNATE_NAMES base nonspecific ribonuclease ORGANISM #formal_name Rhizopus niveus DATE 05-Mar-1993 #sequence_revision 31-Jan-1997 #text_change 16-Jun-2000 ACCESSIONS JH0367; A41449; B41449 REFERENCE JH0367 !$#authors Ohgi, K.; Horiuchi, H.; Watanabe, H.; Takagi, M.; Yano, K.; !1Irie, M. !$#journal J. Biochem. (1991) 109:776-785 !$#title Expression of RNase Rh from Rhizopus niveus in yeast and !1characterization of the secreted proteins. !$#cross-references MUID:92011465; PMID:1655721 !$#accession JH0367 !'##molecule_type DNA !'##residues 1-238 ##label OHG !'##cross-references DDBJ:D12476; DDBJ:D01125; NID:g220997; !1PIDN:BAA02042.1; PID:g286264 REFERENCE A41449 !$#authors Horiuchi, H.; Yanai, K.; Takagi, M.; Yano, K.; Wakabayashi, !1E.; Sanda, A.; Mine, S.; Ohgi, K.; Irie, M. !$#journal J. Biochem. (1988) 103:408-418 !$#title Primary structure of a base non-specific ribonuclease from !1Rhizopus niveus. !$#cross-references MUID:88273061; PMID:3391995 !$#accession A41449 !'##molecule_type DNA !'##residues 1-81,'SLY',85-238 ##label HOR !'##cross-references GB:D00238; NID:g218044; PIDN:BAA00167.1; !1PID:g218045 !'##note the authors translated the codon TCA for residue 82 as Asn, CTC !1for residue 83 as Arg, and TAT for residue 84 as Ala !$#accession B41449 !'##molecule_type protein !'##residues 17-238 ##label HO2 REFERENCE S62310 !$#authors Kurihara, H.; Nonaka, T.; Mitsui, Y.; Ohgi, K.; Irie, M.; !1Nakamura, K.T. !$#journal J. Mol. Biol. (1996) 255:310-320 !$#title The crystal structure of ribonuclease Rh from Rhizopus !1niveus at 2.0 A resolution. !$#cross-references MUID:96150305; PMID:8551522 !$#contents annotation; X-ray crystallography, 2.0 angstroms GENETICS !$#introns 21/1; 116/2; 151/3; 167/2 FUNCTION !$#description hydrolyzes internal phosphodiester bonds of RNA to produce !13'-phosphomononucleotides CLASSIFICATION #superfamily Enterobacter ribonuclease KEYWORDS hydrolase FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-238 #product ribonuclease Rh #status experimental #label !8MAT\ !$19-36,26-69,35-136, !$79-128,198-229 #disulfide_bonds #status experimental\ !$62,121,125 #active_site His, Glu, His #status predicted\ !$65,120,124 #binding_site substrate (Trp, His, Lys) #status !8predicted SUMMARY #length 238 #molecular-weight 25635 #checksum 6286 SEQUENCE /// ENTRY JX0127 #type complete TITLE ribonuclease M (EC 3.1.27.-) - Aspergillus phoenicis ORGANISM #formal_name Aspergillus phoenicis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JX0127 REFERENCE JX0127 !$#authors Watanabe, H.; Naitoh, A.; Suyama, Y.; Inokuchi, N.; Shimada, !1H.; Koyama, T.; Ohgi, K.; Irie, M. !$#journal J. Biochem. (1990) 108:303-310 !$#title Primary structure of a base non-specific and adenylic acid !1preferential ribonuclease from Aspergillus saitoi. !$#cross-references MUID:91035364; PMID:2229029 !$#accession JX0127 !'##molecule_type protein !'##residues 1-238 ##label WAT FUNCTION !$#description ribonuclease M is a base nonspecific and adenylate !1preferential ribonuclease from Aspergillus saitoi CLASSIFICATION #superfamily Enterobacter ribonuclease KEYWORDS glycoprotein; hydrolase FEATURE !$74 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 238 #molecular-weight 26606 #checksum 9062 SEQUENCE /// ENTRY JU0205 #type complete TITLE ribonuclease T2 (EC 3.1.27.1) precursor - Aspergillus oryzae ORGANISM #formal_name Aspergillus oryzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JU0205; S01668 REFERENCE JU0205 !$#authors Ozeki, K.; Kitamoto, K.; Gomi, K.; Kumagai, C.; Tamura, G.; !1Hara, S. !$#journal Curr. Genet. (1991) 19:367-373 !$#title Cloning and nucleotide sequence of the genomic ribonuclease !1T2 gene (rntB) from Aspergillus oryzae. !$#cross-references MUID:92005789; PMID:1913876 !$#accession JU0205 !'##molecule_type DNA !'##residues 1-276 ##label OZE !'##cross-references GB:X61086; NID:g2467; PIDN:CAA43400.1; PID:g2468 !'##experimental_source strain RIB40 REFERENCE S01668 !$#authors Kawata, Y.; Sakiyama, F.; Tamaoki, H. !$#journal Eur. J. Biochem. (1988) 176:683-697 !$#title Amino-acid sequence of ribonuclease T2 from Aspergillus !1oryzae. !$#cross-references MUID:89005122; PMID:3169020 !$#accession S01668 !'##molecule_type protein !'##residues 18-256 ##label KAW GENETICS !$#gene rntB !$#introns 73/2; 133/1; 171/3; 237/1 CLASSIFICATION #superfamily Enterobacter ribonuclease KEYWORDS hydrolase FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-256 #product ribonuclease T2 #status experimental #label !8MAT SUMMARY #length 276 #molecular-weight 30742 #checksum 5318 SEQUENCE /// ENTRY JC1373 #type complete TITLE ribonuclease (EC 3.1.-.-) LE2 - shiitake mushroom ORGANISM #formal_name Lentinula edodes #common_name shiitake mushroom DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JC1373; PS0416 REFERENCE JC1373 !$#authors Kobayashi-Shimada, H.; Inokuchi, N.; Koyama, T.; Watanabe, !1H.; Iwama, M.; Ohgi, K.; Irie, M. !$#journal Biosci. Biotechnol. Biochem. (1992) 56:2003-2010 !$#title Primary structure of a base non-specific and adenylic acid !1preferential ribonuclease from the fruit bodies of Lentinus !1edodes. !$#cross-references MUID:93129853; PMID:1369096 !$#accession JC1373 !'##molecule_type protein !'##residues 1-239 ##label KOB !'##experimental_source fruiting bodies REFERENCE PS0416 !$#authors Simada, H.; Inokuchi, N.; Okuwaki, H.; Koyama, T.; Irie, M. !$#journal Agric. Biol. Chem. (1991) 55:1167-1169 !$#title Purification and characterization of a base non-specific and !1adenylic acid preferring ribonuclease from the fruit bodies !1of Lentinus edodes. !$#cross-references MUID:91254740; PMID:1368676 !$#accession PS0416 !'##molecule_type protein !'##residues 1-41 ##label SIM CLASSIFICATION #superfamily Enterobacter ribonuclease KEYWORDS hydrolase SUMMARY #length 239 #molecular-weight 25877 #checksum 9692 SEQUENCE /// ENTRY JX0197 #type complete TITLE ribonuclease TRV (EC 3.1.27.-) - fungus (Trichoderma viride) ORGANISM #formal_name Trichoderma viride DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JX0197 REFERENCE JX0197 !$#authors Inada, Y.; Watanabe, H.; Ohgi, K.; Irie, M. !$#journal J. Biochem. (1991) 110:896-904 !$#title Isolation, characterization, and primary structure of a base !1non-specific and adenylic acid preferential ribonuclease !1with higher specific activity from Trichoderma viride. !$#cross-references MUID:92176163; PMID:1794979 !$#accession JX0197 !'##molecule_type protein !'##residues 1-234 ##label INA CLASSIFICATION #superfamily Enterobacter ribonuclease KEYWORDS glycoprotein; hydrolase FEATURE !$15 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 234 #molecular-weight 25901 #checksum 6320 SEQUENCE /// ENTRY JX0262 #type complete TITLE ribonuclease (EC 3.1.27.-) Phy-b - slime mold (Physarum polycephalum) CONTAINS ribonuclease Phy-b ORGANISM #formal_name Physarum polycephalum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JX0262 REFERENCE JX0262 !$#authors Inokuchi, N.; Koyama, T.; Sawada, F.; Irie, M. !$#journal J. Biochem. (1993) 113:425-432 !$#title Purification, some properties, and primary structure of base !1non-specific ribonucleases from Physarum polycephalum. !$#cross-references MUID:93293791; PMID:8514732 !$#accession JX0262 !'##molecule_type protein !'##residues 1-180 ##label INO CLASSIFICATION #superfamily Enterobacter ribonuclease KEYWORDS glycoprotein; hydrolase FEATURE !$2-180 #product ribonuclease Phy-b #status experimental !8#label MAT\ !$15 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 180 #molecular-weight 19723 #checksum 836 SEQUENCE /// ENTRY A47118 #type complete TITLE periplasmic ribonuclease (EC 3.1.-.-) - Aeromonas hydrophila ORGANISM #formal_name Aeromonas hydrophila DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A47118; S23227 REFERENCE A47118 !$#authors Favre, D.; Ngai, P.K.; Timmis, K.N. !$#journal J. Bacteriol. (1993) 175:3710-3722 !$#title Relatedness of a periplasmic, broad-specificity RNase from !1Aeromonas hydrophila to RNase I of Escherichia coli and to a !1family of eukaryotic RNases. !$#cross-references MUID:93285983; PMID:7685334 !$#accession A47118 !'##status preliminary !'##molecule_type DNA !'##residues 1-215 ##label FAV !'##cross-references GB:X67054; NID:g38839; PIDN:CAA47438.1; PID:g38840 CLASSIFICATION #superfamily Enterobacter ribonuclease KEYWORDS hydrolase SUMMARY #length 215 #molecular-weight 24410 #checksum 1654 SEQUENCE /// ENTRY C64009 #type complete TITLE ribonuclease homolog HI0526 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C64009 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession C64009 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-272 ##label TIGR !'##cross-references GB:U32735; GB:L42023; NID:g1573509; !1PIDN:AAC22192.1; PID:g1573510; TIGR:HI0526 CLASSIFICATION #superfamily Enterobacter ribonuclease SUMMARY #length 272 #molecular-weight 31482 #checksum 849 SEQUENCE /// ENTRY QQECPE #type complete TITLE tRNA nucleotidyltransferase (EC 2.7.7.56) - Escherichia coli (strain K-12) ALTERNATE_NAMES phosphate-dependent exoribonuclease; ribonuclease PH; RNase PH ORGANISM #formal_name Escherichia coli DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 01-Mar-2002 ACCESSIONS A04470; E65165 REFERENCE A30400 !$#authors Poulsen, P.; Bonekamp, F.; Jensen, K.F. !$#journal EMBO J. (1984) 3:1783-1790 !$#title Structure of the Escherichia coli pyrE operon and control of !1pyrE expression by a UTP modulated intercistronic !1attentuation. !$#cross-references MUID:85003588; PMID:6207018 !$#accession A04470 !'##molecule_type DNA !'##residues 1-238 ##label POU !'##cross-references GB:X00781; GB:X01713; NID:g499180; PIDN:CAA25357.1; !1PID:g499181 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65165 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-122,'GG',125-223,'ESNPL' ##label BLAT !'##cross-references GB:AE000441; GB:U00096; NID:g1790063; !1PIDN:AAC76667.1; PID:g1790074; UWGP:b3643 !'##experimental_source strain K-12, substrain MG1655 !'##note this strain is known to contain a frameshift mutation at the !1carboxyl end REFERENCE A45741 !$#authors Burland, V.; Plunkett III, G.; Daniels, D.L.; Blattner, F.R. !$#journal Genomics (1993) 16:551-561 !$#title DNA sequence and analysis of 136 kilobases of the !1Escherichia coli genome: organizational symmetry around the !1origin of replication. !$#cross-references MUID:93315143; PMID:7686882 !$#contents annotation; coding regions REFERENCE A43128 !$#authors Kelly, K.O.; Deutscher, M.P. !$#journal J. Biol. Chem. (1992) 267:17153-17158 !$#title Characterization of Escherichia coli RNase PH. !$#cross-references MUID:92381029; PMID:1512253 !$#contents annotation; enzyme activity GENETICS !$#gene rph !$#map_position 82 min !$#note this gene and the pyrE gene constitute an operon FUNCTION !$#description catalyzes the reversible phosphorolyis of ribonucleotides !1following -CCA at the 3'-terminus of tRNA producing !1ribonucleoside diphosphates CLASSIFICATION #superfamily tRNA nucleotidyltransferase KEYWORDS nucleotidyltransferase; tRNA processing FEATURE !$1-238 #product tRNA nucleotidyltransferase #status !8predicted #label MAT SUMMARY #length 238 #molecular-weight 25495 #checksum 1025 SEQUENCE /// ENTRY A64059 #type complete TITLE tRNA nucleotidyltransferase (EC 2.7.7.56) - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES phosphate-dependent exoribonuclease; ribonuclease PH ORGANISM #formal_name Haemophilus influenzae DATE 18-Aug-1995 #sequence_revision 18-Aug-1995 #text_change 18-Jun-1999 ACCESSIONS A64059 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession A64059 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-238 ##label TIGR !'##cross-references GB:U32713; GB:L42023; NID:g1573231; !1PIDN:AAC21939.1; PID:g1573239; TIGR:HI0273 FUNCTION !$#description catalyzes the reversible phosphorolyis of ribonucleotides !1following -CCA at the 3'-terminus of tRNA producing !1ribonucleoside diphosphates CLASSIFICATION #superfamily tRNA nucleotidyltransferase KEYWORDS nucleotidyltransferase; tRNA processing SUMMARY #length 238 #molecular-weight 25789 #checksum 1973 SEQUENCE /// ENTRY S72788 #type complete TITLE tRNA nucleotidyltransferase (EC 2.7.7.56) - Mycobacterium leprae ALTERNATE_NAMES B1549_C1_182 protein; phosphate-dependent exoribonuclease; ribonuclease PH ORGANISM #formal_name Mycobacterium leprae DATE 19-Mar-1997 #sequence_revision 25-Apr-1997 #text_change 23-Mar-2001 ACCESSIONS S72788 REFERENCE S72582 !$#authors Smith, D.R.; Robison, K. !$#submission submitted to the EMBL Data Library, November 1993 !$#description Mycobacterium leprae cosmid B1549. !$#accession S72788 !'##status preliminary !'##molecule_type DNA !'##residues 1-259 ##label SMI !'##cross-references EMBL:U00014; NID:g466903; PIDN:AAA50880.1; !1PID:g466905 GENETICS !$#gene rnpH !$#start_codon GTG FUNCTION !$#description catalyzes the reversible phosphorolyis of ribonucleotides !1following -CCA at the 3'-terminus of tRNA producing !1ribonucleoside diphosphates CLASSIFICATION #superfamily tRNA nucleotidyltransferase KEYWORDS nucleotidyltransferase; tRNA processing SUMMARY #length 259 #molecular-weight 27365 #checksum 7993 SEQUENCE /// ENTRY A44914 #type complete TITLE tRNA nucleotidyltransferase (EC 2.7.7.56) - Bacillus subtilis ALTERNATE_NAMES phosphate-dependent exoribonuclease; ribonuclease PH ORGANISM #formal_name Bacillus subtilis DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jun-2000 ACCESSIONS A44914; D69694 REFERENCE A44914 !$#authors Craven, M.G.; Henner, D.J.; Alessi, D.; Schauer, A.T.; Ost, !1K.A.; Deutscher, M.P.; Friedman, D.I. !$#journal J. Bacteriol. (1992) 174:4727-4735 !$#title Identification of the rph (RNase PH) gene of Bacillus !1subtilis: evidence for suppression of cold-sensitive !1mutations in Escherichia coli. !$#cross-references MUID:92325065; PMID:1624460 !$#accession A44914 !'##molecule_type DNA !'##residues 1-245 ##label CRA !'##cross-references GB:M85163; NID:g143443; PIDN:AAA22705.1; !1PID:g143444 !'##note sequence extracted from NCBI backbone (NCBIP:108178) REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D69694 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-6,'Q',8-71,'Q',73-245 ##label KUN !'##cross-references GB:Z99118; GB:AL009126; NID:g2635200; !1PIDN:CAB14797.1; PID:g2635302 !'##experimental_source strain 168 GENETICS !$#gene rph FUNCTION !$#description catalyzes the reversible phosphorolyis of ribonucleotides !1following -CCA at the 3'-terminus of tRNA producing !1ribonucleoside diphosphates CLASSIFICATION #superfamily tRNA nucleotidyltransferase KEYWORDS nucleotidyltransferase; tRNA processing SUMMARY #length 245 #molecular-weight 26539 #checksum 7992 SEQUENCE /// ENTRY NCBYN1 #type complete TITLE nuclease NUC1 (EC 3.1.30.-) precursor, mitochondrial - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein HRE329; protein J0310; protein YJL208c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 21-Jul-2000 ACCESSIONS S05888; S50777; S46621; S56995; S56998; S45165 REFERENCE S05885 !$#authors Vincent, R.D.; Hofmann, T.J.; Zassenhaus, H.P. !$#journal Nucleic Acids Res. (1988) 16:3297-3312 !$#title Sequence and expression of NUC1, the gene encoding the !1mitochondrial nuclease in Saccharomyces cerevisiae. !$#cross-references MUID:88233924; PMID:2836792 !$#accession S05888 !'##molecule_type DNA !'##residues 1-329 ##label VIN !'##cross-references EMBL:X06670; NID:g4062; PIDN:CAA29870.1; PID:g4066 REFERENCE S50701 !$#authors Vandenbol, M.; Durand, P.; Bolle, P.A.; Dion, C.; !1Portetelle, D.; Hilger, F. !$#journal Yeast (1994) 10:1657-1662 !$#title Sequence analysis of a 40.2 kb DNA fragment located near the !1left telomere of yeast chromosome X. !$#cross-references MUID:95242842; PMID:7725802 !$#accession S50777 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-329 ##label VAW !'##cross-references EMBL:Z34098; NID:g496934; PIDN:CAA84003.1; !1PID:g496954 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1994 REFERENCE S46621 !$#authors Purnelle, B.; Coster, F.; Goffeau, A. !$#journal Yeast (1994) 10:1235-1249 !$#title The sequence of a 36 kb segment on the left arm of yeast !1chromosome X identifies 24 open reading frames including !1NUC1, PRP21 (SPP91), CDC6, CRY2, the gene for S24, a !1homologue to the aconitase gene ACO1 and two homologues to !1chromosome III genes. !$#cross-references MUID:95274326; PMID:7754713 !$#accession S46621 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-329 ##label PUR !'##cross-references EMBL:X77688; NID:g1183992; PIDN:CAA54748.1; !1PID:g547582 REFERENCE S56977 !$#authors Purnelle, B.; Coster, F.; Goffeau, A. !$#submission submitted to the Protein Sequence Database, September 1995 !$#accession S56995 !'##molecule_type DNA !'##residues 1-329 ##label PUW !'##cross-references EMBL:Z49483; NID:g1015588; PIDN:CAA89505.1; !1PID:g1015589; GSPDB:GN00010; MIPS:YJL208c REFERENCE S56835 !$#authors Vandenbol, M.; Durand, P.; Portetelle, D.; Hilger, F. !$#submission submitted to the Protein Sequence Database, September 1995 !$#accession S56998 !'##molecule_type DNA !'##residues 1-329 ##label VAN !'##cross-references EMBL:Z49483; NID:g1015588; PIDN:CAA89505.1; !1PID:g1015589; GSPDB:GN00010; MIPS:YJL208c GENETICS !$#gene SGD:NUC1; MIPS:YJL208c !'##cross-references SGD:S0003744; MIPS:YJL208c !$#map_position 10L !$#genome nuclear COMPLEX homodimer FUNCTION !$#description nuclease !$#note the protein has both RNAse and DNAse activity CLASSIFICATION #superfamily nuclease NUC1 KEYWORDS homodimer; hydrolase; membrane protein; mitochondrion FEATURE !$138 #active_site His #status predicted SUMMARY #length 329 #molecular-weight 37209 #checksum 8505 SEQUENCE /// ENTRY ALHUS #type complete TITLE alpha-amylase (EC 3.2.1.1) precursor, salivary - human ALTERNATE_NAMES 1,4-alpha-D-glucan glucanohydrolase; alpha-amylase 1 ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1987 #sequence_revision 28-Dec-1987 #text_change 18-Jun-1999 ACCESSIONS A91543; A54640; I39446; A91570; A00836; A25851; A29493 REFERENCE A91543 !$#authors Nishide, T.; Nakamura, Y.; Emi, M.; Yamamoto, T.; Ogawa, M.; !1Mori, T.; Matsubara, K. !$#journal Gene (1986) 41:299-304 !$#title Primary structure of human salivary alpha-amylase gene. !$#cross-references MUID:86221711; PMID:2423416 !$#accession A91543 !'##molecule_type DNA !'##residues 1-511 ##label NIS !'##cross-references GB:K02214; GB:M18786; NID:g178583; PIDN:AAA52279.1; !1PID:g178585 !'##genetics AM1A !'##note the authors translated the codon CAA for residue 317 as Gly REFERENCE A54640 !$#authors Handy, D.E.; Larsen, S.H.; Karn, R.C.; Hodes, M.E. !$#journal Mol. Biol. Med. (1987) 4:145-155 !$#title Identification of a human salivary amylase gene. Partial !1sequence of genomic DNA suggests a mode of regulation !1different from that of mouse, Amy. !$#cross-references MUID:87314429; PMID:2442579 !$#accession A54640 !'##molecule_type DNA !'##residues 1-142,'A',144-284,'T',286-293;450-511 ##label HAN !'##cross-references GB:M17883; NID:g178589 !'##genetics AM1A REFERENCE I39446 !$#authors Gumucio, D.L.; Wiebauer, K.; Caldwell, R.M.; Samuelson, !1L.C.; Meisler, M.H. !$#journal Mol. Cell. Biol. (1988) 8:1197-1205 !$#title Concerted evolution of human amylase genes. !$#cross-references MUID:88216594; PMID:2452973 !$#accession I39446 !'##molecule_type DNA !'##residues 1-56 ##label RES !'##cross-references GB:M18671; NID:g178554; PIDN:AAA58368.1; !1PID:g463065 !'##genetics AM1C REFERENCE A91570 !$#authors Nakamura, Y.; Ogawa, M.; Nishide, T.; Emi, M.; Kosaki, G.; !1Himeno, S.; Matsubara, K. !$#journal Gene (1986) 50:371-372 !$#title Corrected sequences of cDNAs for human salivary and !1pancreatic alpha-amylases. !$#accession A91570 !'##molecule_type mRNA !'##residues 1-511 ##label NAK REFERENCE A91511 !$#authors Nakamura, Y.; Ogawa, M.; Nishide, T.; Emi, M.; Kosaki, G.; !1Himeno, S.; Matsubara, K. !$#journal Gene (1984) 28:263-270 !$#title Sequences of cDNAs for human salivary and pancreatic !1alpha-amylases. !$#cross-references MUID:84237580; PMID:6610603 !$#contents annotation; mRNA sequence !$#note this sequence differs considerably from that shown; it !1contained several errors; the corrected sequence is given in !1reference A91570 GENETICS AM1A !$#gene GDB:AMY1A; AMY1 !'##cross-references GDB:120544; OMIM:104700 !$#map_position 1p21-1p21 !$#introns 56/3; 105/2; 171/3; 248/3; 293/2; 334/2; 367/3; 407/2; 449/2 !$#note recently duplicated genes AMY1A, AMY1B, and AMY1C had no !1differences over a region of 950 base pairs sequenced (see !1reference I39446) GENETICS AM1B !$#gene GDB:AMY1B; AMY1 !'##cross-references GDB:120545; OMIM:104701 !$#map_position 1p21-1p21 GENETICS AM1C !$#gene GDB:AMY1C; AMY1 !'##cross-references GDB:120546; OMIM:104702 !$#map_position 1p21-1p21 FUNCTION !$#description catalyzes the hydrolysis of internal 1,4-alpha-D-glucosidic !1bonds !$#pathway carbohydrate digestion; glycogen/starch degradation CLASSIFICATION #superfamily mammalian alpha-amylase; alpha-amylase core !1homology KEYWORDS carbohydrate digestion; glycoprotein; glycosidase; !1hydrolase; polysaccharide degradation; pyroglutamic acid; !1salivary gland FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-511 #product alpha-amylase, salivary #status predicted !8#label MAT\ !$180-318 #domain alpha-amylase core homology #label AMY\ !$16 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status predicted\ !$43-101,85-130, !$156-175,393-399, !$465-477 #disulfide_bonds #status predicted\ !$115,182,216 #binding_site calcium (Asn, Asp, His) #status !8predicted\ !$212,248,315 #active_site Asp, Glu, Asp #status predicted\ !$427 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 511 #molecular-weight 57796 #checksum 5683 SEQUENCE /// ENTRY ALHUP #type complete TITLE alpha-amylase (EC 3.2.1.1) 2A precursor, pancreatic - human ALTERNATE_NAMES 1,4-alpha-D-glucan glucanohydrolase; alpha-amylase 2 ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1987 #sequence_revision 31-Dec-1988 #text_change 18-Jun-1999 ACCESSIONS A29614; B91570; A28293; I39447; I39448; A00837; B29493 REFERENCE A29614 !$#authors Horii, A.; Emi, M.; Tomita, N.; Nishide, T.; Ogawa, M.; !1Mori, T.; Matsubara, K. !$#journal Gene (1987) 60:57-64 !$#title Primary structure of human pancreatic alpha-amylase gene: !1its comparison with human salivary alpha-amylase gene. !$#cross-references MUID:88152502; PMID:2450054 !$#accession A29614 !'##molecule_type DNA !'##residues 1-511 ##label HOR !'##cross-references GB:M18785; GB:K02213; NID:g178565; PIDN:AAA52280.1; !1PID:g178567 !'##note the authors translated the codon GAA for residue 42 as Gly, GAG !1for residue 44 as Gly, AAA for residue 337 as Asn, and AAC !1for residue 430 as Asp REFERENCE A91570 !$#authors Nakamura, Y.; Ogawa, M.; Nishide, T.; Emi, M.; Kosaki, G.; !1Himeno, S.; Matsubara, K. !$#journal Gene (1986) 50:371-372 !$#title Corrected sequences of cDNAs for human salivary and !1pancreatic alpha-amylases. !$#accession B91570 !'##molecule_type mRNA !'##residues 1-511 ##label NAK !'##note the authors translated the codon GAG for residue 186 as Gln, !1AAA for residue 337 as Asn, and AAC for residue 430 as Asp REFERENCE A91511 !$#authors Nakamura, Y.; Ogawa, M.; Nishide, T.; Emi, M.; Kosaki, G.; !1Himeno, S.; Matsubara, K. !$#journal Gene (1984) 28:263-270 !$#title Sequences of cDNAs for human salivary and pancreatic !1alpha-amylases. !$#cross-references MUID:84237580; PMID:6610603 !$#contents annotation !$#note this sequence contained several errors; the corrected !1sequence is given in reference A91570 REFERENCE A93684 !$#authors Groot, P.C.; Bleeker, M.J.; Pronk, J.C.; Arwert, F.; Mager, !1W.H.; Planta, R.J.; Eriksson, A.W.; Frants, R.R. !$#journal Nucleic Acids Res. (1988) 16:4724 !$#title Human pancreatic amylase is encoded by two different genes. !$#cross-references MUID:88247775; PMID:3260028 !$#accession A28293 !'##status translation not shown !'##molecule_type DNA !'##residues 1-56 ##label GRO !'##cross-references GB:X07056; NID:g28681; PIDN:CAA30099.1; PID:g28682 REFERENCE I39446 !$#authors Gumucio, D.L.; Wiebauer, K.; Caldwell, R.M.; Samuelson, !1L.C.; Meisler, M.H. !$#journal Mol. Cell. Biol. (1988) 8:1197-1205 !$#title Concerted evolution of human amylase genes. !$#cross-references MUID:88216594; PMID:2452973 !$#accession I39447 !'##molecule_type DNA !'##residues 1-56 ##label RES !'##cross-references GB:M18669; NID:g178568; PIDN:AAA51723.1; !1PID:g560765 REFERENCE I39448 !$#authors Wise, R.J.; Karn, R.C.; Larsen, S.H.; Hodes, M.E.; Gardell, !1S.J.; Rutter, W.J. !$#journal Mol. Biol. Med. (1984) 2:307-322 !$#title A complementary DNA sequence that predicts a human !1pancreatic amylase primary structure consistent with the !1electrophoretic mobility of the common isozyme, Amy2 A. !$#cross-references MUID:86091475; PMID:6336237 !$#accession I39448 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-511 ##label RE2 !'##cross-references GB:M28443; NID:g529396; PIDN:AAA51724.1; !1PID:g529397 GENETICS !$#gene GDB:AMY2A; AMY2 !'##cross-references GDB:120547; OMIM:104650 !$#map_position 1p21-1p21 !$#introns 56/3; 105/3; 171/3; 248/3; 293/2; 334/2; 367/3; 407/2; 449/2 FUNCTION !$#description catalyzes the hydrolysis of internal 1,4-alpha-D-glucosidic !1bonds !$#pathway carbohydrate digestion; glycogen/starch degradation CLASSIFICATION #superfamily mammalian alpha-amylase; alpha-amylase core !1homology KEYWORDS carbohydrate digestion; glycoprotein; glycosidase; !1hydrolase; pancreas; polysaccharide degradation; !1pyroglutamic acid FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-511 #product alpha-amylase, pancreatic #status predicted !8#label MAT\ !$180-318 #domain alpha-amylase core homology #label AMY\ !$16 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status predicted\ !$43-101,85-130, !$156-175,393-399, !$465-477 #disulfide_bonds #status predicted\ !$216,248,315 #active_site His, Glu, Asp #status predicted\ !$427 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 511 #molecular-weight 57707 #checksum 5308 SEQUENCE /// ENTRY ALHU2B #type complete TITLE alpha-amylase (EC 3.2.1.1) 2B precursor, pancreatic - human ALTERNATE_NAMES 1,4-alpha-D-glucan glucanohydrolase; alpha-amylase 3; carcinoid alpha-amylase ORGANISM #formal_name Homo sapiens #common_name man DATE 07-Jun-1990 #sequence_revision 11-Aug-1995 #text_change 16-Jun-2000 ACCESSIONS JS0165; B28293; S40490; I39449 REFERENCE JS0165 !$#authors Tomita, N.; Horii, A.; Doi, S.; Yokouchi, H.; Shiosaki, K.; !1Higashiyama, M.; Matsuura, N.; Ogawa, M.; Mori, T.; !1Matsubara, K. !$#journal Gene (1989) 76:11-18 !$#title A novel type of human alpha-amylase produced in lung !1carcinoid tumor. !$#cross-references MUID:89306646; PMID:2701942 !$#accession JS0165 !'##molecule_type mRNA !'##residues 1-511 ##label TOM !'##cross-references GB:D90097; NID:g219471; PIDN:BAA14130.1; !1PID:g780137 REFERENCE A93684 !$#authors Groot, P.C.; Bleeker, M.J.; Pronk, J.C.; Arwert, F.; Mager, !1W.H.; Planta, R.J.; Eriksson, A.W.; Frants, R.R. !$#journal Nucleic Acids Res. (1988) 16:4724 !$#title Human pancreatic amylase is encoded by two different genes. !$#cross-references MUID:88247775; PMID:3260028 !$#accession B28293 !'##status translation not shown !'##molecule_type DNA !'##residues 1-56 ##label GRO !'##cross-references GB:X07057; NID:g28683; PIDN:CAA30100.1; PID:g28684 REFERENCE S40490 !$#authors Omichi, K.; Hase, S. !$#journal Biochim. Biophys. Acta (1993) 1203:224-229 !$#title Identification of the characteristic amino-acid sequence for !1human alpha-amylase encoded by the AMY2B gene. !$#cross-references MUID:94092712; PMID:8268204 !$#accession S40490 !'##molecule_type protein !'##residues 177-191 ##label OMI !'##experimental_source urine REFERENCE I39446 !$#authors Gumucio, D.L.; Wiebauer, K.; Caldwell, R.M.; Samuelson, !1L.C.; Meisler, M.H. !$#journal Mol. Cell. Biol. (1988) 8:1197-1205 !$#title Concerted evolution of human amylase genes. !$#cross-references MUID:88216594; PMID:2452973 !$#accession I39449 !'##molecule_type DNA !'##residues 1-56 ##label RES !'##cross-references GB:M18670; NID:g178570; PIDN:AAA51725.1; !1PID:g463066 GENETICS !$#gene GDB:AMY2B; AMY2 !'##cross-references GDB:120548; OMIM:104660 !$#map_position 1p21-1p21 !$#introns 56/3 !$#note the list of introns is incomplete FUNCTION !$#description catalyzes the hydrolysis of internal 1,4-alpha-D-glucosidic !1bonds !$#pathway carbohydrate digestion; glycogen/starch degradation CLASSIFICATION #superfamily mammalian alpha-amylase; alpha-amylase core !1homology KEYWORDS carbohydrate digestion; glycoprotein; glycosidase; !1hydrolase; polysaccharide degradation; pyroglutamic acid FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-511 #product alpha-amylase 2B #status predicted #label !8MAT\ !$180-318 #domain alpha-amylase core homology #label AMY\ !$16 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status predicted\ !$43-101,85-130, !$156-175,393-399, !$465-477 #disulfide_bonds #status predicted\ !$216,248,315 #active_site His, Glu, Asp #status predicted\ !$427 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 511 #molecular-weight 57709 #checksum 5174 SEQUENCE /// ENTRY ALMSS #type complete TITLE alpha-amylase (EC 3.2.1.1) precursor, salivary and hepatic - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Nov-1980 #sequence_revision 29-Jul-1981 #text_change 18-Jun-1999 ACCESSIONS A90798; A93245; I49487; A00838 REFERENCE A90798 !$#authors Hagenbuchle, O.; Bovey, R.; Young, R.A. !$#journal Cell (1980) 21:179-187 !$#title Tissue-specific expression of mouse alpha-amylase genes: !1nucleotide sequence of isoenzyme mRNAs from pancreas and !1salivary gland. !$#cross-references MUID:81001853; PMID:6157477 !$#accession A90798 !'##molecule_type mRNA !'##residues 1-511 ##label HA1 !'##cross-references GB:V00717; NID:g49926; PIDN:CAA24097.1; PID:g49927 !'##experimental_source salivary REFERENCE A93245 !$#authors Hagenbuchle, O.; Tosi, M.; Schibler, U.; Bovey, R.; !1Wellauer, P.K.; Young, R.A. !$#journal Nature (1981) 289:643-646 !$#title Mouse liver and salivary gland alpha-amylase mRNAs differ !1only in 5' non-translated sequences. !$#cross-references MUID:81123091; PMID:6162108 !$#accession A93245 !'##molecule_type mRNA !'##residues 1-511 ##label HA2 !'##cross-references GB:J00356; NID:g191906; PIDN:AAA37221.1; !1PID:g309103 !'##experimental_source hepatic !'##note hepatic and salivary alpha-amylases are coded by the same gene; !1however, their mRNAs have different 5' untranslated !1sequences REFERENCE A91288 !$#authors Karn, R.C.; Petersen, T.E.; Hjorth, J.P.; Nieles, J.T.; !1Roepstorff, P. !$#journal FEBS Lett. (1981) 126:292-296 !$#title Characterization of the amino termini of mouse salivary and !1pancreatic amylases. !$#contents annotation; beginning of mature enzyme REFERENCE I49487 !$#authors Young, R.A.; Hagenbuechle, O.; Schibler, U. !$#journal Cell (1981) 23:451-458 !$#title a single mouse alpha-amylase gene specifies two different !1tissue-specific mrnas. !$#cross-references MUID:81135845; PMID:6162570 !$#accession I49487 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-94 ##label RES !'##cross-references GB:J00353; NID:g191899; PIDN:AAA37219.1; !1PID:g191903 GENETICS !$#gene Amy-1 !$#map_position 3 !$#introns 56/3 FUNCTION !$#description catalyzes the hydrolysis of internal 1,4-alpha-D-glucosidic !1bonds !$#pathway carbohydrate digestion; glycogen/starch degradation CLASSIFICATION #superfamily mammalian alpha-amylase; alpha-amylase core !1homology KEYWORDS carbohydrate digestion; glycosidase; hydrolase; liver; !1polysaccharide degradation; pyroglutamic acid; salivary !1gland FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-508 #product alpha-amylase #status experimental #label !8MPT\ !$180-318 #domain alpha-amylase core homology #label AMY\ !$16 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$43-101,85-130, !$156-175,393-399, !$465-477 #disulfide_bonds #status predicted\ !$216,248,315 #active_site His, Glu, Asp #status predicted SUMMARY #length 511 #molecular-weight 57623 #checksum 9277 SEQUENCE /// ENTRY ALMSP #type complete TITLE alpha-amylase (EC 3.2.1.1) A2 precursor, pancreatic - mouse ALTERNATE_NAMES 1,4-alpha-D-glucan glucanohydrolase ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Nov-1980 #sequence_revision 29-Jul-1981 #text_change 18-Jun-1999 ACCESSIONS B90798; A00839 REFERENCE A90798 !$#authors Hagenbuchle, O.; Bovey, R.; Young, R.A. !$#journal Cell (1980) 21:179-187 !$#title Tissue-specific expression of mouse alpha-amylase genes: !1nucleotide sequence of isoenzyme mRNAs from pancreas and !1salivary gland. !$#cross-references MUID:81001853; PMID:6157477 !$#accession B90798 !'##molecule_type mRNA !'##residues 1-508 ##label HAG !'##cross-references GB:V00718; NID:g49928; PIDN:CAA24098.1; PID:g49929 REFERENCE A91288 !$#authors Karn, R.C.; Petersen, T.E.; Hjorth, J.P.; Nieles, J.T.; !1Roepstorff, P. !$#journal FEBS Lett. (1981) 126:292-296 !$#title Characterization of the amino termini of mouse salivary and !1pancreatic amylases. !$#contents annotation; beginning of the mature enzyme GENETICS !$#gene Amy-2 !$#map_position 3 FUNCTION !$#description catalyzes the hydrolysis of internal 1,4-alpha-D-glucosidic !1bonds !$#pathway carbohydrate digestion; glycogen/starch degradation CLASSIFICATION #superfamily mammalian alpha-amylase; alpha-amylase core !1homology KEYWORDS carbohydrate digestion; glycosidase; hydrolase; pancreas; !1polysaccharide degradation; pyroglutamic acid FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-508 #product alpha-amylase #status experimental #label !8MPT\ !$177-315 #domain alpha-amylase core homology #label AMY\ !$16 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$43-101,85-130, !$156-172,390-396, !$462-474 #disulfide_bonds #status predicted\ !$213,245,312 #active_site His, Glu, Asp #status predicted SUMMARY #length 508 #molecular-weight 57417 #checksum 470 SEQUENCE /// ENTRY ALMSP1 #type complete TITLE alpha-amylase (EC 3.2.1.1) A1 precursor, pancreatic - mouse ALTERNATE_NAMES 1,4-alpha-D-glucan glucanohydrolase ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 18-Jun-1999 ACCESSIONS A90995; I48247; A91626; I48244; I49491; B22784 REFERENCE A90995 !$#authors Tosi, M.; Bovey, R.; Astolfi, S.; Bodary, S.; Meisler, M.; !1Wellauer, P.K. !$#journal EMBO J. (1984) 3:2809-2816 !$#title Multiple non-allelic genes encoding pancreatic alpha-amylase !1of mouse are expressed in a strain-specific fashion. !$#cross-references MUID:85126875; PMID:6098446 !$#accession A90995 !'##molecule_type mRNA !'##residues 1-508 ##label TOS !'##cross-references GB:X02577; NID:g49955; PIDN:CAA26414.1; PID:g49956 !'##experimental_source strain CE/J !$#accession I48247 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-232 ##label RE2 !'##cross-references EMBL:X02579; NID:g49959; PIDN:CAA26417.1; !1PID:g49960 REFERENCE A91626 !$#authors Strahler, J.R.; Meisler, M. !$#journal Genetics (1982) 101:91-102 !$#title Two distinct pancreatic amylase genes are active in YBR !1mice. !$#cross-references MUID:83004912; PMID:6180955 !$#accession A91626 !'##molecule_type protein !'##residues 407-458 ##label STR !'##experimental_source strain YBR REFERENCE A91288 !$#authors Karn, R.C.; Petersen, T.E.; Hjorth, J.P.; Nieles, J.T.; !1Roepstorff, P. !$#journal FEBS Lett. (1981) 126:292-296 !$#title Characterization of the amino termini of mouse salivary and !1pancreatic amylases. !$#contents annotation; beginning of the mature enzyme REFERENCE I48244 !$#authors Bodary, S.; Grossi, G.; Hagenbuchle, O.; Wellauer, P.K. !$#journal J. Mol. Biol. (1985) 182:1-10 !$#title Members of the Amy-2 alpha-amylase gene family of mouse !1strain CE/J contain duplicated 5' termini. !$#cross-references MUID:85210888; PMID:2987507 !$#accession I48244 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-94 ##label RES !'##cross-references EMBL:X02343; NID:g49949; PIDN:CAA26202.1; !1PID:g49950 REFERENCE I49489 !$#authors Gumucio, D.L.; Wiebauer, K.; Dranginis, A.; Samuelson, L.C.; !1Treisman, L.O.; Caldwell, R.M.; Antonucci, T.K.; Meisler, !1M.H. !$#journal J. Biol. Chem. (1985) 260:13483-13489 !$#title Evolution of the amylase multigene family: YBR/Ki mice !1express a pancreatic amylase gene which is silent in other !1strains. !$#cross-references MUID:86033801; PMID:2414282 !$#accession I49491 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 388-470 ##label RE3 !'##cross-references GB:M11895; NID:g191912; PIDN:AAA37224.1; !1PID:g191913 GENETICS !$#gene Amy-2 !$#map_position 3 !$#introns 56/3 !$#note list of introns may be incomplete FUNCTION !$#description catalyzes the hydrolysis of internal 1,4-alpha-D-glucosidic !1bonds !$#pathway carbohydrate digestion; glycogen/starch degradation CLASSIFICATION #superfamily mammalian alpha-amylase; alpha-amylase core !1homology KEYWORDS carbohydrate digestion; glycosidase; hydrolase; pancreas; !1polysaccharide degradation; pyroglutamic acid FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-508 #product alpha-amylase #status experimental #label !8MPT\ !$177-315 #domain alpha-amylase core homology #label AMY\ !$16 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$43-101,85-130, !$156-172,390-396, !$462-474 #disulfide_bonds #status predicted\ !$213,245,312 #active_site His, Glu, Asp #status predicted SUMMARY #length 508 #molecular-weight 57479 #checksum 1903 SEQUENCE /// ENTRY ALMSPC #type complete TITLE alpha-amylase (EC 3.2.1.1) B(C) precursor, pancreatic - mouse ALTERNATE_NAMES 1,4-alpha-D-glucan glucanohydrolase ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 18-Jun-1999 ACCESSIONS B90995; C22784 REFERENCE A90995 !$#authors Tosi, M.; Bovey, R.; Astolfi, S.; Bodary, S.; Meisler, M.; !1Wellauer, P.K. !$#journal EMBO J. (1984) 3:2809-2816 !$#title Multiple non-allelic genes encoding pancreatic alpha-amylase !1of mouse are expressed in a strain-specific fashion. !$#cross-references MUID:85126875; PMID:6098446 !$#accession B90995 !'##molecule_type mRNA !'##residues 1-508 ##label TOS !'##cross-references GB:X02578; NID:g49957; PIDN:CAA26415.1; PID:g49958 !'##experimental_source strain CE/J REFERENCE A91288 !$#authors Karn, R.C.; Petersen, T.E.; Hjorth, J.P.; Nieles, J.T.; !1Roepstorff, P. !$#journal FEBS Lett. (1981) 126:292-296 !$#title Characterization of the amino termini of mouse salivary and !1pancreatic amylases. !$#contents annotation; beginning of the mature enzyme GENETICS !$#gene Amy-2 !$#map_position 3 FUNCTION !$#description catalyzes the hydrolysis of internal 1,4-alpha-D-glucosidic !1bonds !$#pathway carbohydrate digestion; glycogen/starch degradation CLASSIFICATION #superfamily mammalian alpha-amylase; alpha-amylase core !1homology KEYWORDS carbohydrate digestion; glycosidase; hydrolase; pancreas; !1polysaccharide degradation; pyroglutamic acid FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-508 #product alpha-amylase #status experimental #label !8MPT\ !$177-315 #domain alpha-amylase core homology #label AMY\ !$16 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$43-101,85-130, !$156-172,390-396, !$462-474 #disulfide_bonds #status predicted\ !$213,245,312 #active_site His, Glu, Asp #status predicted SUMMARY #length 508 #molecular-weight 57421 #checksum 1699 SEQUENCE /// ENTRY ALMSPA #type complete TITLE alpha-amylase (EC 3.2.1.1) B(A) precursor, pancreatic - mouse ALTERNATE_NAMES 1,4-alpha-D-glucan glucanohydrolase; pancreatic amylase (Amy-2.1y) ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 18-Jun-1999 ACCESSIONS C90995; I49490; A22784 REFERENCE A90995 !$#authors Tosi, M.; Bovey, R.; Astolfi, S.; Bodary, S.; Meisler, M.; !1Wellauer, P.K. !$#journal EMBO J. (1984) 3:2809-2816 !$#title Multiple non-allelic genes encoding pancreatic alpha-amylase !1of mouse are expressed in a strain-specific fashion. !$#cross-references MUID:85126875; PMID:6098446 !$#accession C90995 !'##molecule_type mRNA !'##residues 1-508 ##label TOS !'##cross-references GB:X02576; NID:g49953; PIDN:CAA26413.1; PID:g49954 !'##experimental_source strain CE/J REFERENCE A91288 !$#authors Karn, R.C.; Petersen, T.E.; Hjorth, J.P.; Nieles, J.T.; !1Roepstorff, P. !$#journal FEBS Lett. (1981) 126:292-296 !$#title Characterization of the amino termini of mouse salivary and !1pancreatic amylases. !$#contents annotation; beginning of the mature enzyme REFERENCE I49490 !$#authors Osborn, L.; Rosenberg, M.P.; Keller, S.A.; Meisler, M.H. !$#journal Mol. Cell. Biol. (1987) 7:326-334 !$#title Tissue-specific and insulin-dependent expression of a !1pancreatic amylase gene in transgenic mice. !$#cross-references MUID:87172721; PMID:2436036 !$#accession I49490 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-94 ##label RES !'##cross-references GB:M16540; NID:g191910; PIDN:AAA37223.1; !1PID:g191911 GENETICS !$#gene Amy-2 !$#map_position 3 !$#introns 56/3 !$#note list of introns may be incomplete FUNCTION !$#description catalyzes the hydrolysis of internal 1,4-alpha-D-glucosidic !1bonds !$#pathway carbohydrate digestion; glycogen/starch degradation CLASSIFICATION #superfamily mammalian alpha-amylase; alpha-amylase core !1homology KEYWORDS carbohydrate digestion; glycosidase; hydrolase; pancreas; !1polysaccharide degradation; pyroglutamic acid FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-508 #product alpha-amylase #status predicted #label MPT\ !$177-315 #domain alpha-amylase core homology #label AMY\ !$16 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$43-101,85-130, !$156-172,390-396, !$462-474 #disulfide_bonds #status predicted\ !$213,245,312 #active_site His, Glu, Asp #status predicted SUMMARY #length 508 #molecular-weight 57393 #checksum 626 SEQUENCE /// ENTRY ALRTP #type fragment TITLE alpha-amylase (EC 3.2.1.1) precursor, pancreatic - rat (fragment) ALTERNATE_NAMES 1,4-alpha-D-glucan glucanohydrolase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Nov-1980 #sequence_revision 30-Nov-1980 #text_change 18-Jun-1999 ACCESSIONS A00840; I52679 REFERENCE A00840 !$#authors MacDonald, R.J.; Crerar, M.M.; Swain, W.F.; Pictet, R.L.; !1Thomas, G.; Rutter, W.J. !$#journal Nature (1980) 287:117-122 !$#title Structure of a family of rat amylase genes. !$#cross-references MUID:81052269; PMID:6159531 !$#accession A00840 !'##molecule_type mRNA !'##residues 1-503 ##label MAC !'##cross-references GB:J00703; NID:g202865; PIDN:AAA40725.1; !1PID:g202866 !'##note the amino end of the mature protein is blocked REFERENCE I52679 !$#authors MacDonald, R.J.; Crerar, M.M.; Swain, W.F.; Pictet, R.L.; !1Rutter, W.J. !$#journal Cancer (1981) 47:1497-1504 !$#title Pancreas-specific genes: Structure and expression. !$#cross-references MUID:82001788; PMID:6168351 !$#accession I52679 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-503 ##label RES !'##cross-references GB:M24962; NID:g202891; PIDN:AAA40731.1; !1PID:g202892 FUNCTION !$#description catalyzes the hydrolysis of internal 1,4-alpha-D-glucosidic !1bonds !$#pathway carbohydrate digestion; glycogen/starch degradation CLASSIFICATION #superfamily mammalian alpha-amylase; alpha-amylase core !1homology KEYWORDS blocked amino end; carbohydrate digestion; glycosidase; !1hydrolase; pancreas; polysaccharide degradation FEATURE !$1-10 #domain signal sequence (fragment) #status predicted !8#label SIG\ !$11-503 #product alpha-amylase, pancreatic #status predicted !8#label MPT\ !$172-310 #domain alpha-amylase core homology #label AMY\ !$38-96,80-125, !$151-167,385-391, !$457-469 #disulfide_bonds #status predicted\ !$208,240,307 #active_site His, Glu, Asp #status predicted SUMMARY #length 503 #checksum 3926 SEQUENCE /// ENTRY ALPGP #type complete TITLE alpha-amylase (EC 3.2.1.1), pancreatic - pig ALTERNATE_NAMES 1,4-alpha-D-glucan glucanohydrolase ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 02-Apr-1982 #sequence_revision 30-Sep-1987 #text_change 06-Dec-1996 ACCESSIONS A25412 REFERENCE A90659 !$#authors Pasero, L.; Mazzei-Pierron, Y.; Abadie, B.; Chicheportiche, !1Y.; Marchis-Mouren, G. !$#journal Biochim. Biophys. Acta (1986) 869:147-157 !$#title Complete amino acid sequence and location of the five !1disulfide bridges in porcine pancreatic alpha-amylase. !$#cross-references MUID:86104352; PMID:3484639 !$#contents isozyme I !$#accession A25412 !'##molecule_type protein !'##residues 1-496 ##label PAS REFERENCE A90010 !$#authors Payan, F.; Haser, R.; Pierrot, M.; Frey, M.; Astier, J.P.; !1Abadie, B.; Duee, E.; Buisson, G. !$#journal Acta Crystallogr. (1980) B36:416-421 !$#title The three-dimensional structure of alpha-amylase from !1porcine pancreat 5 angstrom resolution - the active-site !1location. !$#contents annotation; X-ray crystallography, 5 angstroms COMMENT The structure is composed of an amino-terminal beta-barrel !1and carboxyl-terminal beta-sheets. The beta-barrel encloses !1one chloride ion, which activates the enzyme. The molecule !1also binds calcium ion, which is essential for its enzymatic !1activity. COMMENT The two forms of this enzyme, I and II, show very similar !1activities, molecular masses, and compositions and differ !1only in their isoelectric points. FUNCTION !$#pathway carbohydrate digestion; glycogen/starch degradation CLASSIFICATION #superfamily mammalian alpha-amylase; alpha-amylase core !1homology KEYWORDS calcium; carbohydrate digestion; chloride; glycosidase; !1hydrolase; pancreas; polysaccharide degradation; !1pyroglutamic acid FEATURE !$165-303 #domain alpha-amylase core homology #label AMY\ !$1 #modified_site pyrrolidone carboxylic acid (Gln) !8#status experimental\ !$28-86,70-115, !$141-160,378-384, !$450-462 #disulfide_bonds #status experimental\ !$201,233,300 #active_site His, Glu, Asp #status predicted SUMMARY #length 496 #molecular-weight 55475 #checksum 6466 SEQUENCE /// ENTRY A25529 #type complete TITLE alpha-amylase (EC 3.2.1.1) precursor - fruit fly (Drosophila melanogaster) (strain Oregon-R and others) ALTERNATE_NAMES 1,4-alpha-D-glucan glucanohydrolase ORGANISM #formal_name Drosophila melanogaster #variety strain Oregon-R; strain TN-329; strain TN22; strain TN329; strain AO168 DATE 30-Jun-1988 #sequence_revision 08-Nov-1996 #text_change 18-Jun-1999 ACCESSIONS A25529; JT0375; S58950; S58955; S58963 REFERENCE A25529 !$#authors Boer, P.H.; Hickey, D.A. !$#journal Nucleic Acids Res. (1986) 14:8399-8411 !$#title The alpha-amylase gene in Drosophila melanogaster: !1nucleotide sequence, gene structure and expression motifs. !$#cross-references MUID:87066719; PMID:3024105 !$#accession A25529 !'##molecule_type DNA; mRNA !'##residues 1-494 ##label BOE !'##cross-references GB:X04569; NID:g7580; PIDN:CAA28238.1; PID:g790427 !'##experimental_source wild-type Oregon-R strain, proximal gene !'##genetics AMYP !'##note wild-type strain Canton-S differs in having 144-His and 181-Asn !'##note the transcriptionally active distal gene differs at least in !1having 11-Ser !'##note amino end is known to be blocked REFERENCE JT0375 !$#authors Okuyama, E.; Yamazaki, T. !$#journal Proc. Jpn. Acad. (1988) 64B:274-277 !$#title Nucleotide sequences of the duplicated amylase structural !1genes in Drosophila melanogaster; one active and one null !1strain. !$#accession JT0375 !'##molecule_type DNA !'##residues 1-475,'Y',477-494 ##label OKU !'##cross-references EMBL:X84405; NID:g666993; PIDN:CAA59126.1; !1PID:g666994 !'##experimental_source strain TN-329, distal gene !'##genetics AMYD !'##note translation of sequence of proximal gene of strain TN-329 is !1said to be identical with that of Oregon-R REFERENCE S58950 !$#authors Inomata, N.; Shibata, H.; Okuyama, E.; Yamazaki, T. !$#journal Genetics (1995) 141:237-244 !$#title Evolutionary relationships and sequence variation of !1alpha-amylase variants encoded by duplicated genes in the !1Amy locus of Drosophila melanogaster. !$#cross-references MUID:96042908; PMID:8536971 !$#accession S58950 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-494 ##label INO !'##cross-references EMBL:L22716; NID:g348087; PIDN:AAA92226.1; !1PID:g348088 !'##experimental_source strain TN22, proximal gene !'##genetics AMYP !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1993 !$#accession S58955 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-494 ##label INF !'##cross-references EMBL:L22721; NID:g348097; PIDN:AAA92231.1; !1PID:g348098 !'##experimental_source strain TN329, proximal gene !'##genetics AMYP !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1993 !$#accession S58963 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-494 ##label INZ !'##cross-references EMBL:L22731; NID:g348734; PIDN:AAA92234.1; !1PID:g348735 !'##experimental_source strain AO168, proximal gene !'##genetics AMYP !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1993 COMMENT Two highly polymorphic loci encode essentially identical !1products. GENETICS AMYP !$#gene FlyBase:Amy-p !'##cross-references FlyBase:FBgn0000079 GENETICS AMYD !$#gene FlyBase:Amy-d; Amy1 !'##cross-references FlyBase:FBgn0000078 FUNCTION !$#description catalyzes hydrolysis of internal 1,4-alpha-D-glucosidic !1bonds !$#pathway carbohydrate digestion; glycogen/starch degradation CLASSIFICATION #superfamily mammalian alpha-amylase; alpha-amylase core !1homology KEYWORDS carbohydrate digestion; glycoprotein; glycosidase; !1hydrolase; polysaccharide degradation; pyroglutamic acid FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-494 #product alpha-amylase #status predicted #label MAT\ !$172-309 #domain alpha-amylase core homology #label AMY\ !$19 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status predicted\ !$46-102,153-167, !$376-382,448-460 #disulfide_bonds #status predicted\ !$208,241,306 #active_site His, Glu, Asp #status predicted\ !$410,435 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 494 #molecular-weight 53745 #checksum 7150 SEQUENCE /// ENTRY ALBS #type complete TITLE alpha-amylase (EC 3.2.1.1) amyE M-type precursor - Bacillus subtilis ALTERNATE_NAMES 1,4-alpha-D-glucan glucanohydrolase ORGANISM #formal_name Bacillus subtilis DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 21-Jul-2000 ACCESSIONS A00842; F69585; A92260; B92260; A26263 REFERENCE A00842 !$#authors Yang, M.; Galizzi, A.; Henner, D. !$#journal Nucleic Acids Res. (1983) 11:237-249 !$#title Nucleotide sequence of the amylase gene from Bacillus !1subtilis. !$#cross-references MUID:83143299; PMID:6186986 !$#accession A00842 !'##molecule_type DNA !'##residues 1-660 ##label YAN !'##cross-references GB:J01547; EMBL:V00101; NID:g39793; !1PIDN:CAA23437.1; PID:g39794 !'##experimental_source strain 168 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69585 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-660 ##label KUN !'##cross-references GB:Z99105; GB:AL009126; NID:g2632457; !1PIDN:CAB12098.1; PID:g2632590 !'##experimental_source strain 168 REFERENCE A92260 !$#authors Mantsala, P.; Zalkin, H. !$#journal J. Biol. Chem. (1979) 254:8540-8547 !$#title Membrane-bound and soluble extracellular alpha-amylase from !1Bacillus subtilis. !$#cross-references MUID:79239474; PMID:112102 !$#accession A92260 !'##molecule_type protein !'##residues 42-48 ##label MAN1 !'##experimental_source strain YY88; membrane-bound enzyme !$#accession B92260 !'##molecule_type protein !'##residues 42-48 ##label MAN2 !'##experimental_source strain YY88; soluble, extracellular enzyme GENETICS !$#gene amyE FUNCTION !$#description catalyzes the hydrolysis of internal 1,4-alpha-D-glucosidic !1bonds !$#pathway glycogen/starch degradation !$#note this form of the enzyme produces glucose and maltose, and !1does hydrolyze maltotriose CLASSIFICATION #superfamily alpha-amylase, subtilis type; alpha-amylase !1core homology KEYWORDS carbohydrate digestion; extracellular protein; glycosidase; !1hydrolase; membrane-associated protein; polysaccharide !1degradation FEATURE !$1-31 #domain signal sequence #status predicted #label SIG\ !$32-41 #domain propeptide #status predicted #label PRO\ !$42-660 #product alpha-amylase #status predicted #label MAT\ !$185-313 #domain alpha-amylase core homology #label AMY\ !$142,187,221 #binding_site calcium (Asn, Asp, His) #status !8predicted\ !$217,249,310 #active_site Asp, Glu, Asp #status predicted SUMMARY #length 660 #molecular-weight 72799 #checksum 4426 SEQUENCE /// ENTRY ALBSNA #type complete TITLE alpha-amylase (EC 3.2.1.1) amyE precursor - Bacillus subtilis (strain NA64) ALTERNATE_NAMES 1,4-alpha-D-glucan glucanohydrolase ORGANISM #formal_name Bacillus subtilis DATE 19-Feb-1984 #sequence_revision 02-Jul-1998 #text_change 18-Jun-1999 ACCESSIONS A91793; I40359 REFERENCE A91793 !$#authors Yamazaki, H.; Ohmura, K.; Nakayama, A.; Takeichi, Y.; !1Otozai, K.; Yamasaki, M.; Tamura, G.; Yamane, K. !$#journal J. Bacteriol. (1983) 156:327-337 !$#title alpha-Amylase genes (amyR2 and amyE(+)) from an !1alpha-amylase-hyperproducing Bacillus subtilis strain: !1molecular cloning and nucleotide sequences. !$#cross-references MUID:84008046; PMID:6413492 !$#accession A91793 !'##molecule_type DNA !'##residues 1-592 ##label YAM !'##cross-references GB:K00563; NID:g142502; PIDN:AAA22234.1; !1PID:g142503 !'##experimental_source strain NA64 !'##note the authors translated the codon AAT for residue 180 as Asp REFERENCE I40359 !$#authors Ohmura, K.; Yamazaki, H.; Takeichi, Y.; Nakayama, A.; !1Otozai, K.; Yamane, K.; Yamasaki, M.; Tamura, G. !$#journal Biochem. Biophys. Res. Commun. (1983) 112:678-683 !$#title Nucleotide sequence of the promoter and NH2-terminal signal !1peptide region of Bacillus subtilis alpha-amylase gene !1cloned in pUB110. !$#cross-references MUID:83204125; PMID:6189486 !$#accession I40359 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-66 ##label OHM !'##cross-references EMBL:V00100; NID:g39791; PIDN:CAA23436.1; !1PID:g39792 !'##experimental_source strain NA64 COMMENT This form of the enzyme in this strain is not found in !1strain 168. See PIR:ALBS. GENETICS !$#gene amyE FUNCTION !$#description catalyzes the hydrolysis of internal 1,4-alpha-D-glucosidic !1bonds !$#pathway glycogen/starch degradation !$#note the hydrolysis products of this form of the enzyme are not !1reported CLASSIFICATION #superfamily alpha-amylase, subtilis type; alpha-amylase !1core homology KEYWORDS carbohydrate digestion; extracellular protein; glycosidase; !1hydrolase; polysaccharide degradation FEATURE !$1-31 #domain signal sequence #status predicted #label SIG\ !$32-41 #domain propeptide #status predicted #label PRO\ !$42-592 #product alpha-amylase #status predicted #label MAT\ !$185-313 #domain alpha-amylase core homology #label AMY\ !$142,187,221 #binding_site calcium (Asn, Asp, His) #status !8predicted\ !$217,249,310 #active_site Asp, Glu, Asp #status predicted SUMMARY #length 592 #molecular-weight 65912 #checksum 4616 SEQUENCE /// ENTRY ALBSN7 #type complete TITLE alpha-amylase (EC 3.2.1.1) amyE N-type precursor - Bacillus subtilis ALTERNATE_NAMES 1,4-alpha-D-glucan glucanohydrolase ORGANISM #formal_name Bacillus subtilis DATE 30-Sep-1987 #sequence_revision 02-Jul-1998 #text_change 18-Jun-1999 ACCESSIONS S02098; I39771; A91983; A22134 REFERENCE S02098 !$#authors Emori, M.; Maruo, B. !$#journal Nucleic Acids Res. (1988) 16:7178 !$#title Complete nucleotide sequence of an alpha-amylase gene from !1Bacillus subtilis 2633, an alpha-amylase extrahyperproducing !1strain. !$#cross-references MUID:88303338; PMID:2457205 !$#accession S02098 !'##molecule_type DNA !'##residues 1-477 ##label EMO1 !'##cross-references EMBL:X07796; NID:g39789; PIDN:CAA30643.1; !1PID:g39790 !'##experimental_source strain 2633 REFERENCE I39771 !$#authors Emori, M.; Tojo, T.; Maruo, B. !$#journal Agric. Biol. Chem. (1988) 52:399-406 !$#title Molecular cloning and expression of an alpha-amylase gene !1from an alpha-amylase extrahyper producing Bacullis !1subtilis. !$#accession I39771 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-43 ##label EMO2 !'##cross-references GB:M35517; NID:g142494; PIDN:AAA22230.1; !1PID:g142495 !'##experimental_source strain 2633 REFERENCE A91983 !$#authors Yamane, K.; Hirata, Y.I.; Furusato, T.; Yamazaki, H.; !1Nakayama, A. !$#journal J. Biochem. (1984) 96:1849-1858 !$#title Changes in the properties and molecular weights of Bacillus !1subtilis M-type and N-type alpha-amylases resulting from a !1spontaneous deletion. !$#cross-references MUID:85157515; PMID:6099357 !$#accession A91983 !'##molecule_type DNA !'##residues 1-145,'F',147-283,'K',285-389,'P',391-469,'M',471-477 !1##label YAM !'##cross-references GB:X02150; NID:g39795; PIDN:CAA26086.1; PID:g39796 !'##experimental_source strain N7, derived from strain 6160 !'##note the authors translated the codon TAC for residue 100 as Thr, !1GAG for residue 223 as Gln, AAG for residue 284 as Asn, and !1ATG for residue 470 as Ile COMMENT This form of the enzyme in these strains is not found in !1strain 168. See PIR:ALBS. See also PIR:A36709. GENETICS !$#gene amyE FUNCTION !$#description catalyzes the hydrolysis of internal 1,4-alpha-D-glucosidic !1bonds !$#pathway glycogen/starch degradation !$#note this form of the enzyme produces maltose and maltotriose, !1and does not hydrolyze maltotriose CLASSIFICATION #superfamily alpha-amylase, subtilis type; alpha-amylase !1core homology KEYWORDS carbohydrate digestion; extracellular protein; glycosidase; !1hydrolase; polysaccharide degradation FEATURE !$1-31 #domain signal sequence #status predicted #label SIG\ !$32-41 #domain propeptide #status predicted #label PRO\ !$42-477 #product alpha-amylase #status predicted #label MAT\ !$185-313 #domain alpha-amylase core homology #label AMY\ !$142,187,221 #binding_site calcium (Asn, Asp, His) #status !8predicted\ !$217,249,310 #active_site Asp, Glu, Asp #status predicted SUMMARY #length 477 #molecular-weight 52773 #checksum 7040 SEQUENCE /// ENTRY A36709 #type complete TITLE alpha-amylase (EC 3.2.1.1) amyE N-type precursor - Bacillus subtilis (strain natto IAM1212) ALTERNATE_NAMES 1,4-alpha-D-glucan glucanohydrolase ORGANISM #formal_name Bacillus subtilis DATE 19-Feb-1984 #sequence_revision 02-Jul-1998 #text_change 18-Jun-1999 ACCESSIONS A36709 REFERENCE A36709 !$#authors Emori, M.; Takagi, M.; Maruo, B.; Yano, K. !$#journal J. Bacteriol. (1990) 172:4901-4908 !$#title Molecular cloning, nucleotide sequencing, and expression of !1the Bacillus subtilis (natto) IAM1212 alpha-amylase gene, !1which encodes an alpha-amylase structurally similar to but !1enzymatically distinct from that of Bacillus subtilis 2633. !$#cross-references MUID:90368540; PMID:2118504 !$#accession A36709 !'##molecule_type DNA !'##residues 1-477 ##label EMO !'##cross-references GB:M79444; NID:g142434; PIDN:AAA22194.1; !1PID:g142435 !'##experimental_source strain natto IAM1212 COMMENT This form of the enzyme in this strain is not found in !1strain 168. See PIR:ALBS and PIR:ALBSN7. GENETICS !$#gene amyE FUNCTION !$#description catalyzes the hydrolysis of internal 1,4-alpha-D-glucosidic !1bonds !$#pathway glycogen/starch degradation !$#note in this strain this form of the enzyme produces glucose and !1maltose, and does hydrolyze maltotriose CLASSIFICATION #superfamily alpha-amylase, subtilis type; alpha-amylase !1core homology KEYWORDS carbohydrate digestion; extracellular protein; glycosidase; !1hydrolase; polysaccharide degradation FEATURE !$1-31 #domain signal sequence #status predicted #label SIG\ !$32-41 #domain propeptide #status predicted #label PRO\ !$42-477 #product alpha-amylase #status predicted #label MAT\ !$185-313 #domain alpha-amylase core homology #label AMY\ !$142,187,221 #binding_site calcium (Asn, Asp, His) #status !8predicted\ !$217,249,310 #active_site Asp, Glu, Asp #status predicted SUMMARY #length 477 #molecular-weight 52911 #checksum 8082 SEQUENCE /// ENTRY ALBSN #type complete TITLE alpha-amylase (EC 3.2.1.1) precursor - Bacillus amyloliquefaciens ALTERNATE_NAMES 1,4-alpha-D-glucan glucanohydrolase ORGANISM #formal_name Bacillus amyloliquefaciens DATE 30-Nov-1980 #sequence_revision 30-Jun-1987 #text_change 18-Jun-1999 ACCESSIONS A92389; A90307; I39756; I39763; A00843 REFERENCE A92389 !$#authors Takkinen, K.; Pettersson, R.F.; Kalkkinen, N.; Palva, I.; !1Soderlund, H.; Kaariainen, L. !$#journal J. Biol. Chem. (1983) 258:1007-1013 !$#title Amino acid sequence of alpha-amylase from Bacillus !1amyloliquefaciens deduced from the nucleotide sequence of !1the cloned gene. !$#cross-references MUID:83108808; PMID:6185474 !$#contents pUB110 !$#accession A92389 !'##molecule_type DNA !'##residues 1-514 ##label TAK !'##cross-references GB:J01542; GB:J01543; GB:M12033; GB:M12034; !1NID:g142428; PIDN:AAA22191.1; PID:g142429 REFERENCE A90307 !$#authors Chung, H.S.; Friedberg, F. !$#journal Biochem. J. (1980) 185:387-395 !$#title Sequence of the N-terminal half of Bacillus !1amyloliquefaciens alpha-amylase. !$#cross-references MUID:80241725; PMID:6156671 !$#accession A90307 !'##molecule_type protein !'##residues 32-53,'I',55-63,'L',65-78,'D',80-83,'S',85-222 ##label CHU REFERENCE I39756 !$#authors Palva, I.; Pettersson, R.F.; Kalkkinen, N.; Lehtovaara, P.; !1Sarvas, M.; Soderlund, H.; Takkinen, K.; Kaariainen, L. !$#journal Gene (1981) 15:43-51 !$#title Nucleotide sequence of the promoter and NH2-terminal signal !1peptide region of the alpha-amylase gene from Bacillus !1amyloliquefaciens. !$#cross-references MUID:82051296; PMID:6170539 !$#accession I39756 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-96 ##label RES !'##cross-references EMBL:V00092; NID:g39297; PIDN:CAA23430.1; !1PID:g39298 REFERENCE I39763 !$#authors Ruohonen, L.; Hackman, P.; Lehtovaara, P.; Knowles, J.K.C.; !1Karaenen, S. !$#journal Gene (1987) 59:161-170 !$#title Efficient secretion of Bacillus amyloliquefaciens !1alpha-amylase cells by its own signal peptide from !1Saccharomyces cerevisiae host. !$#cross-references MUID:88137952; PMID:2830166 !$#accession I39763 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-39 ##label RE2 !'##cross-references GB:M18424; NID:g142430; PIDN:AAA22192.1; !1PID:g142431 FUNCTION !$#description catalyzes the hydrolysis of internal 1,4-alpha-D-glucosidic !1bonds !$#pathway glycogen/starch degradation CLASSIFICATION #superfamily alpha-amylase, amyloliquefaciens type; !1alpha-amylase core homology KEYWORDS extracellular protein; glycosidase; hydrolase; !1polysaccharide degradation FEATURE !$1-31 #domain signal sequence #status predicted #label SIG\ !$32-514 #product alpha-amylase #status predicted #label MPT\ !$229-362 #domain alpha-amylase core homology #label AMY\ !$133,231,266 #binding_site calcium (Asn, Asp, His) #status !8predicted\ !$262,292,359 #active_site Asp, Glu, Asp #status predicted SUMMARY #length 514 #molecular-weight 58403 #checksum 2384 SEQUENCE /// ENTRY ALBSL #type complete TITLE alpha-amylase (EC 3.2.1.1) precursor [validated] - Bacillus licheniformis ALTERNATE_NAMES 1,4-alpha-D-glucan glucanohydrolase ORGANISM #formal_name Bacillus licheniformis DATE 30-Jun-1987 #sequence_revision 24-Apr-1998 #text_change 15-Sep-2000 ACCESSIONS A91997; B24549; A91796; A21663; I39774; I39772; A26151; !1S53788; A00844 REFERENCE A91997 !$#authors Yuuki, T.; Nomura, T.; Tezuka, H.; Tsuboi, A.; Yamagata, H.; !1Tsukagoshi, N.; Udaka, S. !$#journal J. Biochem. (1985) 98:1147-1156 !$#title Complete nucleotide sequence of a gene coding for heat- and !1pH-stable alpha-amylase of Bacillus licheniformis: !1comparison of the amino acid sequences of three bacterial !1liquefying alpha-amylases deduced from the DNA sequences. !$#cross-references MUID:86111694; PMID:2418011 !$#accession A91997 !'##molecule_type DNA !'##residues 1-162,'R',164-512 ##label YUU !'##cross-references GB:X03236; NID:g39551; PIDN:CAA26981.1; PID:g39552 !'##experimental_source ATCC 27811 REFERENCE A91817 !$#authors Gray, G.L.; Mainzer, S.E.; Rey, M.W.; Lamsa, M.H.; Kindle, !1K.L.; Carmona, C.; Requadt, C. !$#journal J. Bacteriol. (1986) 166:635-643 !$#title Structural genes encoding the thermophilic alpha-amylases of !1Bacillus stearothermophilus and Bacillus licheniformis. !$#cross-references MUID:86195857; PMID:3009417 !$#accession B24549 !'##molecule_type DNA !'##residues 1-338,'G',340-348,'S',350-512 ##label GRA !'##cross-references GB:M13256; NID:g142510; PIDN:AAA22240.1; !1PID:g142511 !'##experimental_source NCIB 8061 REFERENCE A91796 !$#authors Stephens, M.A.; Ortlepp, S.A.; Ollington, J.F.; McConnell, !1D.J. !$#journal J. Bacteriol. (1984) 158:369-372 !$#title Nucleotide sequence of the 5' region of the Bacillus !1licheniformis alpha-amylase gene: comparison with the !1Bacillus amyloliquefaciens gene. !$#cross-references MUID:84185455; PMID:6609154 !$#accession A91796 !'##molecule_type DNA !'##residues 1-104 ##label STE !'##cross-references GB:K01984; NID:g142432; PIDN:AAA22193.1; !1PID:g142433 REFERENCE A21663 !$#authors Sibakov, M.; Palva, I. !$#journal Eur. J. Biochem. (1984) 145:567-572 !$#title Isolation and the 5'-end nucleotide sequence of Bacillus !1licheniformis alpha-amylase gene. !$#cross-references MUID:85076654; PMID:6334606 !$#accession A21663 !'##molecule_type DNA !'##residues 1-3,'H',5-12,'P',14-47,'R',49-61,'V',63,'D',65-67,'VA', !170-71,'S',73-80,'D',82-104,118-121 ##label SIB !'##experimental_source chromosomal DNA of ATCC 14580 !'##note the authors translated the codon CGT for residue 48 as Gly and !1GAC for residue 64 as His REFERENCE I39773 !$#authors Laoide, B.M.; Chambliss, G.H.; McConnell, D.J. !$#journal J. Bacteriol. (1989) 171:2435-2442 !$#title Bacillus licheniformis alpha-amylase gene, amyL, is subject !1to promoter-independent catabolite repression in Bacillus !1subtilis. !$#cross-references MUID:89213924; PMID:2540150 !$#accession I39774 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-29 ##label LAO !'##cross-references GB:M26412; NID:g341477; PIDN:AAA22237.1; !1PID:g516590 REFERENCE I39772 !$#authors Jorgensen, P.L.; Hansen, C.K.; Poulsen, G.B.; Diderichsen, !1B. !$#journal Gene (1990) 96:37-41 !$#title In vivo genetic engineering: homologous recombination as a !1tool for plasmid construction. !$#cross-references MUID:91092499; PMID:2265757 !$#accession I39772 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-32,'I' ##label JOR !'##cross-references GB:M62637; NID:g142498; PIDN:AAA22232.1; !1PID:g142499 REFERENCE A26151 !$#authors Kuhn, H.; Fietzek, P.P.; Lampen, J.O. !$#journal J. Bacteriol. (1982) 149:372-373 !$#title N-terminal amino acid sequence of Bacillus licheniformis !1alpha-amylase: comparison with Bacillus amyloliquefaciens !1and Bacillus subtilis enzymes. !$#cross-references MUID:82098050; PMID:6172418 !$#accession A26151 !'##molecule_type protein !'##residues 30-37,'E',39-41,'X',43-47 ##label KUH REFERENCE S53788 !$#authors Machius, M.; Wiegand, G.; Huber, R. !$#journal J. Mol. Biol. (1995) 246:545-559 !$#title Crystal structure of calcium-depleted Bacillus licheniformis !1alpha-amylase at 2.2 A resolution. !$#cross-references MUID:95182462; PMID:7877175 !$#accession S53788 !'##molecule_type protein !'##residues 'D',220-227 ##label MAC !'##note sequence represents amino end of an internal fragment created !1by a single enzymatic cleavage by a protease trace !1contaminant during purification REFERENCE A65206 !$#authors Machius, M.; Wiegand, G.; Huber, R. !$#submission submitted to the Brookhaven Protein Data Bank, July 1995 !$#cross-references PDB:1BPL !$#contents annotation; X-ray crystallography, 2.2 angstroms, residues !132-210;222-511 !$#note these structural studies suggest 163 is Leu rather than Arg REFERENCE A66860 !$#authors Song, H.K.; Hwang, K.Y.; Chang, C.; Suh, S.W. !$#submission submitted to the Brookhaven Protein Data Bank, October 1996 !$#cross-references PDB:1VJS !$#contents annotation; X-ray crystallography, 1.7 angstroms, residues !132-210;222-511 GENETICS !$#gene amyL FUNCTION !$#description catalyzes the hydrolysis of internal 1,4-alpha-D-glucosidic !1bonds !$#pathway glycogen/starch degradation CLASSIFICATION #superfamily alpha-amylase, amyloliquefaciens type; !1alpha-amylase core homology KEYWORDS extracellular protein; glycosidase; heat-stable protein; !1hydrolase; polysaccharide degradation FEATURE !$1-29 #domain signal sequence #status predicted #label SIG\ !$30-512 #product alpha-amylase #status experimental #label !8MAT\ !$227-360 #domain alpha-amylase core homology #label AMY\ !$133,229,264 #binding_site calcium (Asn, Asp, His) #status !8experimental\ !$260,290,357 #active_site Asp, Glu, Asp #status experimental SUMMARY #length 512 #molecular-weight 58506 #checksum 6609 SEQUENCE /// ENTRY A27705 #type complete TITLE alpha-amylase (EC 3.2.1.1) precursor - Bacillus sp. ALTERNATE_NAMES 1,4-alpha-D-glucan glucanohydrolase; G6-amylase ORGANISM #formal_name Bacillus sp. DATE 31-Mar-1989 #sequence_revision 18-Aug-1995 #text_change 18-Jun-1999 ACCESSIONS A27705 REFERENCE A27705 !$#authors Tsukamoto, A.; Kimura, K.; Ishii, Y.; Takano, T.; Yamane, K. !$#journal Biochem. Biophys. Res. Commun. (1988) 151:25-31 !$#title Nucleotide sequence of the maltohexaose-producing amylase !1gene from an alkalophilic Bacillus sp. 707 and structural !1similarity to liquefying type alpha-amylases. !$#cross-references MUID:88162814; PMID:3258152 !$#accession A27705 !'##molecule_type DNA !'##residues 1-518 ##label TSU !'##cross-references GB:M18862; NID:g142496; PIDN:AAA22231.1; !1PID:g142497 !'##experimental_source chromosomal DNA of strain 707 !'##note amino end of mature protein also determined COMMENT This is the smallest of five starch-hydrolyzing enzymes from !1this organism. FUNCTION !$#description catalyzes the hydrolysis of internal 1,4-alpha-D-glucosidic !1bonds !$#pathway glycogen/starch degradation CLASSIFICATION #superfamily alpha-amylase, amyloliquefaciens type; !1alpha-amylase core homology KEYWORDS extracellular protein; glycosidase; hydrolase; !1polysaccharide degradation FEATURE !$1-33 #domain signal sequence #status predicted #label SIG\ !$34-518 #product alpha-amylase #status experimental #label !8MAT\ !$236-369 #domain alpha-amylase core homology #label AMY\ !$139,238,273 #binding_site calcium (Asn, Asp, His) #status !8predicted\ !$269,299,366 #active_site Asp, Glu, Asp #status predicted SUMMARY #length 518 #molecular-weight 59008 #checksum 7204 SEQUENCE /// ENTRY A54541 #type complete TITLE alpha-amylase (EC 3.2.1.1) precursor - Bacillus stearothermophilus (strain DN1792) ALTERNATE_NAMES 1,4-alpha-D-glucan glucanohydrolase ORGANISM #formal_name Bacillus stearothermophilus DATE 28-Oct-1994 #sequence_revision 18-Aug-1995 #text_change 13-Jun-1997 ACCESSIONS A54541 REFERENCE A54541 !$#authors Jorgensen, P.L.; Poulsen, G.B.; Diderichsen, B. !$#journal FEMS Microbiol. Lett. (1991) 77:271-276 !$#title Cloning of a chromosomal alpha-amylase gene from Bacillus !1stearothermophilus. !$#accession A54541 !'##molecule_type DNA !'##residues 1-549 ##label JOR !'##cross-references GB:X59476 !'##experimental_source chromosomal DNA of strain DN1792 COMMENT Alpha-amylase genes have been found on plasmids and in !1multiple copies on the chromosome in various strains of this !1organism. GENETICS !$#start_codon GTG FUNCTION !$#description catalyzes the hydrolysis of internal 1,4-alpha-D-glucosidic !1bonds !$#pathway glycogen/starch degradation CLASSIFICATION #superfamily alpha-amylase, amyloliquefaciens type; !1alpha-amylase core homology KEYWORDS extracellular protein; glycosidase; heat-stable protein; !1hydrolase; polysaccharide degradation FEATURE !$1-34 #domain signal sequence #status predicted #label SIG\ !$35-549 #product alpha-amylase #status predicted #label MAT\ !$235-368 #domain alpha-amylase core homology #label AMY\ !$139,237,272 #binding_site calcium (Asp, Asp, His) #status !8predicted\ !$268,298,365 #active_site Asp, Glu, Asp #status predicted SUMMARY #length 549 #molecular-weight 62598 #checksum 5758 SEQUENCE /// ENTRY A24549 #type complete TITLE alpha-amylase (EC 3.2.1.1) precursor - Bacillus stearothermophilus (strain NZ-3) ALTERNATE_NAMES 1,4-alpha-D-glucan glucanohydrolase ORGANISM #formal_name Bacillus stearothermophilus DATE 30-Jun-1988 #sequence_revision 18-Aug-1995 #text_change 18-Jun-1999 ACCESSIONS A24549; I39501; I39770 REFERENCE A91817 !$#authors Gray, G.L.; Mainzer, S.E.; Rey, M.W.; Lamsa, M.H.; Kindle, !1K.L.; Carmona, C.; Requadt, C. !$#journal J. Bacteriol. (1986) 166:635-643 !$#title Structural genes encoding the thermophilic alpha-amylases of !1Bacillus stearothermophilus and Bacillus licheniformis. !$#cross-references MUID:86195857; PMID:3009417 !$#accession A24549 !'##molecule_type DNA !'##residues 1-549 ##label GRA !'##cross-references GB:M13255; NID:g142512; PIDN:AAA22241.1; !1PID:g142513 !'##experimental_source genomic DNA of strain NZ-3 REFERENCE I39501 !$#authors Satoh, H.; Nishida, H.; Isono, K. !$#journal J. Bacteriol. (1988) 170:1034-1040 !$#title Evidence for movement of the alpha-amylase gene into two !1phylogenetically distant Bacillus stearothermophilus !1strains. !$#cross-references MUID:88139156; PMID:3257753 !$#accession I39501 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 536-549 ##label RES !'##cross-references GB:M29577; NID:g142476; PIDN:AAA22225.1; !1PID:g142478 !'##experimental_source strain DY-5 !$#accession I39770 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 536-549 ##label RE2 !'##cross-references GB:M29578; NID:g142484; PIDN:AAA22228.1; !1PID:g142486 !'##experimental_source strain 799 COMMENT Alpha-amylase genes have been found on plasmids and in !1multiple copies on the chromosome in various strains of this !1organism. GENETICS !$#start_codon GTG FUNCTION !$#description catalyzes the hydrolysis of internal 1,4-alpha-D-glucosidic !1bonds !$#pathway glycogen/starch degradation CLASSIFICATION #superfamily alpha-amylase, amyloliquefaciens type; !1alpha-amylase core homology KEYWORDS extracellular protein; glycosidase; heat-stable protein; !1hydrolase; polysaccharide degradation FEATURE !$1-34 #domain signal sequence #status predicted #label SIG\ !$35-549 #product alpha-amylase #status predicted #label MAT\ !$235-368 #domain alpha-amylase core homology #label AMY\ !$139,237,272 #binding_site calcium (Asp, Asp, His) #status !8predicted\ !$268,298,365 #active_site Asp, Glu, Asp #status predicted SUMMARY #length 549 #molecular-weight 62643 #checksum 6769 SEQUENCE /// ENTRY A24436 #type complete TITLE alpha-amylase (EC 3.2.1.1) precursor - Bacillus stearothermophilus plasmid pAT5 ALTERNATE_NAMES 1,4-alpha-D-glucan glucanohydrolase ORGANISM #formal_name Bacillus stearothermophilus DATE 05-Jun-1987 #sequence_revision 18-Aug-1995 #text_change 18-Jun-1999 ACCESSIONS A24436; I39777 REFERENCE A24436 !$#authors Nakajima, R.; Imanaka, T.; Aiba, S. !$#journal J. Bacteriol. (1985) 163:401-406 !$#cross-references MUID:85234394; PMID:3924897 !$#accession A24436 !'##molecule_type DNA !'##residues 1-549 ##label NAK !'##cross-references GB:M11450 !'##experimental_source plasmid pAT5 !'##note amino end of the mature protein also determined REFERENCE I39772 !$#authors Jorgensen, P.L.; Hansen, C.K.; Poulsen, G.B.; Diderichsen, !1B. !$#journal Gene (1990) 96:37-41 !$#title In vivo genetic engineering: homologous recombination as a !1tool for plasmid construction. !$#cross-references MUID:91092499; PMID:2265757 !$#accession I39777 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-45 ##label RES !'##cross-references GB:M62638; NID:g142514; PIDN:AAA22242.1; !1PID:g142515 COMMENT Alpha-amylase genes have been found on plasmids and in !1multiple copies on the chromosome in various strains of this !1organism. GENETICS !$#gene amyS !$#genome plasmid !$#start_codon GTG FUNCTION !$#description catalyzes the hydrolysis of internal 1,4-alpha-D-glucosidic !1bonds !$#pathway glycogen/starch degradation CLASSIFICATION #superfamily alpha-amylase, amyloliquefaciens type; !1alpha-amylase core homology KEYWORDS extracellular protein; glycosidase; heat-stable protein; !1hydrolase; polysaccharide degradation FEATURE !$1-34 #domain signal sequence #status predicted #label SIG\ !$35-549 #product alpha-amylase #status experimental #label !8MAT\ !$235-368 #domain alpha-amylase core homology #label AMY\ !$139,237,272 #binding_site calcium (Asp, Asp, His) #status !8predicted\ !$268,298,365 #active_site Asp, Glu, Asp #status predicted SUMMARY #length 549 #molecular-weight 62670 #checksum 5048 SEQUENCE /// ENTRY ALBSF #type complete TITLE alpha-amylase (EC 3.2.1.1) precursor - Bacillus stearothermophilus (strain DY-5) plasmid pHI300 ALTERNATE_NAMES 1,4-alpha-D-glucan glucanohydrolase ORGANISM #formal_name Bacillus stearothermophilus DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 16-Feb-1997 ACCESSIONS A91999; B91999; A91804; A00845 REFERENCE A91999 !$#authors Ihara, H.; Sasaki, T.; Tsuboi, A.; Yamagata, H.; Tsukagoshi, !1N.; Udaka, S. !$#journal J. Biochem. (1985) 98:95-103 !$#title Complete nucleotide sequence of a thermophilic alpha-amylase !1gene: homology between prokaryotic and eukaryotic !1alpha-amylases at the active sites. !$#cross-references MUID:86008166; PMID:3876333 !$#accession A91999 !'##molecule_type DNA !'##residues 1-548 ##label IH1 !'##cross-references GB:X02769 !'##experimental_source plasmid pHI300 from strain DY-5 !$#accession B91999 !'##molecule_type protein !'##residues 35-48 ##label IH2 !'##experimental_source strain DY-5 REFERENCE A91804 !$#authors Tsukagoshi, N.; Iritani, S.; Sasaki, T.; Takemura, T.; !1Ihara, H.; Idota, Y.; Yamagata, H.; Udaka, S. !$#journal J. Bacteriol. (1985) 164:1182-1187 !$#title Efficient synthesis and secretion of a thermophilic !1alpha-amylase by protein-producing Bacillus brevis 47 !1carrying the Bacillus stearothermophilus amylase gene. !$#cross-references MUID:86059211; PMID:2999073 !$#contents pBAM101 !$#accession A91804 !'##molecule_type DNA !'##residues 1-29,'Q',31-75,'W',77-122 ##label TSU COMMENT Alpha-amylase genes have been found on plasmids and in !1multiple copies on the chromosome in various strains of this !1organism. GENETICS !$#genome plasmid !$#start_codon GTG FUNCTION !$#description catalyzes the hydrolysis of internal 1,4-alpha-D-glucosidic !1bonds !$#pathway glycogen/starch degradation CLASSIFICATION #superfamily alpha-amylase, amyloliquefaciens type; !1alpha-amylase core homology KEYWORDS extracellular protein; glycosidase; heat-stable protein; !1hydrolase; polysaccharide degradation FEATURE !$1-34 #domain signal sequence #status predicted #label SIG\ !$35-548 #product alpha-amylase #status experimental #label !8MAT\ !$235-368 #domain alpha-amylase core homology #label AMY\ !$139,237,272 #binding_site calcium (Asp, Asp, His) #status !8predicted\ !$268,298,365 #active_site Asp, Glu, Asp #status predicted SUMMARY #length 548 #molecular-weight 62585 #checksum 3079 SEQUENCE /// ENTRY A45738 #type complete TITLE alpha-amylase (EC 3.2.1.1), cytosolic - Escherichia coli (strain K-12) ALTERNATE_NAMES 1,4-alpha-D-glucan glucanohydrolase ORGANISM #formal_name Escherichia coli DATE 07-Apr-1994 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS D64956; A45738 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64956 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-495 ##label BLAT !'##cross-references GB:AE000285; GB:U00096; NID:g1788229; !1PIDN:AAC74994.1; PID:g1788236; UWGP:b1927 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A45738 !$#authors Raha, M.; Kawagishi, I.; Mueller, V.; Kihara, M.; Macnab, !1R.M. !$#journal J. Bacteriol. (1992) 174:6644-6652 !$#title Escherichia coli produces a cytoplasmic alpha-amylase, amyA. !$#cross-references MUID:93015717; PMID:1400215 !$#accession A45738 !'##molecule_type DNA !'##residues 1-18,'SS',21-108,'V',110-148,'E',150-233,'I',235-495 !1##label RAH !'##cross-references GB:L01642; NID:g146021; PIDN:AAA23810.1; !1PID:g146023 GENETICS !$#gene amyA FUNCTION !$#description catalyzes the hydrolysis of internal 1,4-alpha-D-glucosidic !1bonds !$#pathway glycogen/starch degradation CLASSIFICATION #superfamily alpha-amylase, amyloliquefaciens type; !1alpha-amylase core homology KEYWORDS cytosol; glycosidase; hydrolase; polysaccharide degradation FEATURE !$202-335 #domain alpha-amylase core homology #label AMY\ !$104,204,239 #binding_site calcium (Asn, Asn, His) #status !8predicted\ !$235,265,332 #active_site Asp, Glu, Asp #status predicted SUMMARY #length 495 #molecular-weight 56639 #checksum 9372 SEQUENCE /// ENTRY B45738 #type complete TITLE alpha-amylase (EC 3.2.1.1), cytosolic - Salmonella typhimurium ALTERNATE_NAMES 1,4-alpha-D-glucan glucanohydrolase ORGANISM #formal_name Salmonella typhimurium DATE 07-Apr-1994 #sequence_revision 18-Aug-1995 #text_change 18-Jun-1999 ACCESSIONS B45738 REFERENCE A45738 !$#authors Raha, M.; Kawagishi, I.; Mueller, V.; Kihara, M.; Macnab, !1R.M. !$#journal J. Bacteriol. (1992) 174:6644-6652 !$#title Escherichia coli produces a cytoplasmic alpha-amylase, amyA. !$#cross-references MUID:93015717; PMID:1400215 !$#accession B45738 !'##molecule_type DNA !'##residues 1-494 ##label RAH !'##cross-references GB:L01643; NID:g154043; PIDN:AAA27110.1; !1PID:g154045 GENETICS !$#gene amyA FUNCTION !$#description catalyzes the hydrolysis of internal 1,4-alpha-D-glucosidic !1bonds !$#pathway glycogen/starch degradation CLASSIFICATION #superfamily alpha-amylase, amyloliquefaciens type; !1alpha-amylase core homology KEYWORDS cytosol; glycosidase; hydrolase; polysaccharide degradation FEATURE !$202-335 #domain alpha-amylase core homology #label AMY\ !$239,265,332 #active_site His, Glu, Asp #status predicted SUMMARY #length 494 #molecular-weight 56496 #checksum 9082 SEQUENCE /// ENTRY ALBSK #type complete TITLE alpha-amylase (EC 3.2.1.1) precursor - Bacillus circulans ALTERNATE_NAMES 1,4-alpha-D-glucan glucanohydrolase ORGANISM #formal_name Bacillus circulans DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 18-Jun-1999 ACCESSIONS A29083 REFERENCE A29083 !$#authors Nishizawa, M.; Ozawa, F.; Hishinuma, F. !$#journal DNA (1987) 6:255-265 !$#title Molecular cloning of an amylase gene of Bacillus circulans. !$#cross-references MUID:87246076; PMID:3109866 !$#accession A29083 !'##molecule_type DNA !'##residues 1-528 ##label NIS !'##cross-references GB:M16657; NID:g142492; PIDN:AAA22229.1; !1PID:g142493 FUNCTION !$#description catalyzes the hydrolysis of internal 1,4-alpha-D-glucosidic !1bonds !$#pathway glycogen/starch degradation CLASSIFICATION #superfamily cyclomaltodextrin glucanotransferase; !1alpha-amylase core homology KEYWORDS extracellular protein; glycosidase; hydrolase; !1polysaccharide degradation FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-528 #product alpha-amylase #status predicted #label MAT\ !$226-360 #domain alpha-amylase core homology #label AMY\ !$55,57,60,61,80,82 #binding_site calcium (Asp, Asn, Asn, Asn, Gly, Asp) !8#status predicted\ !$71-79 #disulfide_bonds #status predicted\ !$168,219,228,262 #binding_site calcium (Asn, Ile, Asp, His) #status !8predicted\ !$258,286,357 #active_site Asp, Glu, Asp #status predicted SUMMARY #length 528 #molecular-weight 57940 #checksum 3743 SEQUENCE /// ENTRY ALBSGR #type complete TITLE cyclomaltodextrin glucanotransferase (EC 2.4.1.19) precursor - Bacillus macerans ALTERNATE_NAMES cyclodextrin glucanotransferase ORGANISM #formal_name Bacillus macerans DATE 31-Dec-1989 #sequence_revision 30-Sep-1993 #text_change 19-Jul-2002 ACCESSIONS S31281; A29847; B29847 REFERENCE S31281 !$#authors Fujiwara, S.; Kakihara, H.; Woo, K.B.; Lejeune, A.; !1Kanemoto, M.; Sakaguchi, K.; Imanaka, T. !$#journal Appl. Environ. Microbiol. (1992) 58:4016-4025 !$#title Cyclization characteristics of cyclodextrin !1glucanotransferase are conferred by the NH(2)-terminal !1region of the enzyme. !$#cross-references MUID:93119155; PMID:1476442 !$#accession S31281 !'##molecule_type DNA !'##residues 1-714 ##label FUJ !'##cross-references EMBL:X59045; NID:g39624; PIDN:CAA41773.1; !1PID:g39625 REFERENCE A29847 !$#authors Takano, T.; Fukuda, M.; Monma, M.; Kobayashi, S.; Kainuma, !1K.; Yamane, K. !$#journal J. Bacteriol. (1986) 166:1118-1122 !$#title Molecular cloning, DNA nucleotide sequencing, and expression !1in Bacillus subtilis cells of the Bacillus macerans !1cyclodextrin glucanotransferase gene. !$#cross-references MUID:86223774; PMID:3011735 !$#accession A29847 !'##molecule_type DNA !'##residues 1-151,'LTLITSRSDRLRPQPHVSGRAGT',175-182,'AL',185-259,'QY', !1262-642,'T',644-714 ##label TAK1 !'##cross-references EMBL:M12777; NID:g142653; PIDN:AAA22298.1; !1PID:g142654 !'##note the authors translated the codon CAA for residue 105 as His !$#accession B29847 !'##molecule_type protein !'##residues 28-29 ##label TAK2 GENETICS !$#gene cgtM FUNCTION !$#description catalyzes the breaking and reformation of 1, !14-alpha-D-glucopyranosyl bonds in long chain polymers to !1form cyclic chains, typically with 6 to 8 subunits !$#note can also catalyze the disproportionation transfer of 6 to 8 !11,4-alpha-D-glucopyranosyl subunits between two long chain !1polymers CLASSIFICATION #superfamily cyclomaltodextrin glucanotransferase; !1alpha-amylase core homology KEYWORDS calcium; duplication; extracellular protein; !1glycosyltransferase; hexosyltransferase; homodimer FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-714 #product cyclomaltodextrin glucanotransferase #status !8experimental #label MAT\ !$28-165 #domain A1 #label DA1\ !$166-229 #domain B #label DOB\ !$224-359 #domain alpha-amylase core homology #label AMY\ !$230-434 #domain A2 #label DA2\ !$435-523 #domain C #label DOC\ !$524-610 #domain D #label DOD\ !$611-714 #domain E #label DOE\ !$54,56,59,60,78,80 #binding_site calcium (Asp, Asp, Asn, Asn, Gly, Asp) !8#status predicted\ !$166,217,226,260 #binding_site calcium (Asn, Ile, Asp, His) #status !8predicted\ !$256,285,356 #active_site Asp, Glu, Asp #status predicted SUMMARY #length 714 #molecular-weight 76960 #checksum 4487 SEQUENCE /// ENTRY ALBSMX #type complete TITLE cyclomaltodextrin glucanotransferase (EC 2.4.1.19) precursor - Bacillus licheniformis ALTERNATE_NAMES cyclodextrin glucosyltransferase ORGANISM #formal_name Bacillus licheniformis DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 18-Jun-1999 ACCESSIONS S15920; S06711 REFERENCE S15920 !$#authors Hill, D.E.; Aldape, R.; Rozzell, J.D. !$#journal Nucleic Acids Res. (1990) 18:199 !$#title Nucleotide sequence of a cyclodextrin glucosyltransferase !1gene, cgtA, from Bacillus licheniformis. !$#cross-references MUID:90174931; PMID:2137908 !$#accession S15920 !'##status translation not shown !'##molecule_type DNA !'##residues 1-718 ##label HIL !'##cross-references EMBL:X15752; NID:g39565; PIDN:CAA33763.1; !1PID:g39566 GENETICS !$#gene cgtA FUNCTION !$#description catalyzes the breaking and reformation of 1, !14-alpha-D-glucopyranosyl bonds in long chain polymers to !1form cyclic chains, typically with 6 to 8 subunits !$#note can also catalyze the disproportionation transfer of 6 to 8 !11,4-alpha-D-glucopyranosyl subunits between two long chain !1polymers CLASSIFICATION #superfamily cyclomaltodextrin glucanotransferase; !1alpha-amylase core homology KEYWORDS calcium; duplication; extracellular protein; !1glycosyltransferase; hexosyltransferase; monomer FEATURE !$1-34 #domain signal sequence #status predicted #label SIG\ !$35-718 #product cyclomaltodextrin glucanotransferase #status !8predicted #label MAT\ !$35-172 #domain A1 #label DA1\ !$173-236 #domain B #label DOB\ !$231-365 #domain alpha-amylase core homology #label AMY\ !$237-440 #domain A2 #label DA2\ !$441-528 #domain C #label DOC\ !$529-614 #domain D #label DOD\ !$615-718 #domain E #label DOE\ !$61,63,66,67,85,87 #binding_site calcium (Asp, Asn, Asn, Asn, Gly, Asp) !8#status predicted\ !$77-84 #disulfide_bonds #status predicted\ !$173,224,233,267 #binding_site calcium (Asn, Ile, Asp, His) #status !8predicted\ !$263,291,362 #active_site Asp, Glu, Asp #status predicted SUMMARY #length 718 #molecular-weight 78002 #checksum 5244 SEQUENCE /// ENTRY ALBSG6 #type complete TITLE cyclomaltodextrin glucanotransferase (EC 2.4.1.19) precursor - Bacillus sp. (strain 6.6.3) ALTERNATE_NAMES beta-cyclodextrin glucanotransferase ORGANISM #formal_name Bacillus sp. DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 18-Jun-1999 ACCESSIONS S21532 REFERENCE S21532 !$#authors Akhmetzjanov, A.A. !$#submission submitted to the EMBL Data Library, May 1992 !$#accession S21532 !'##molecule_type DNA !'##residues 1-718 ##label AKH !'##cross-references EMBL:X66106; NID:g39838; PIDN:CAA46901.1; !1PID:g39839 GENETICS !$#gene cgt FUNCTION !$#description catalyzes the breaking and reformation of 1, !14-alpha-D-glucopyranosyl bonds in long chain polymers to !1form cyclic chains, typically with 6 to 8 subunits !$#note can also catalyze the disproportionation transfer of 6 to 8 !11,4-alpha-D-glucopyranosyl subunits between two long chain !1polymers CLASSIFICATION #superfamily cyclomaltodextrin glucanotransferase; !1alpha-amylase core homology KEYWORDS calcium; duplication; extracellular protein; !1glycosyltransferase; hexosyltransferase; monomer FEATURE !$1-34 #domain signal sequence #status predicted #label SIG\ !$35-718 #product cyclomaltodextrin glucanotransferase #status !8predicted #label MAT\ !$35-172 #domain A1 #label DA1\ !$173-236 #domain B #label DOB\ !$231-365 #domain alpha-amylase core homology #label AMY\ !$237-440 #domain A2 #label DA2\ !$441-528 #domain C #label DOC\ !$529-614 #domain D #label DOD\ !$615-718 #domain E #label DOE\ !$61,63,66,67,85,87 #binding_site calcium (Asp, Asn, Asn, Asn, Gly, Asp) !8#status predicted\ !$77-84 #disulfide_bonds #status predicted\ !$173,224,233,267 #binding_site calcium (Asn, Ile, Asp, His) #status !8predicted\ !$263,291,362 #active_site Asp, Glu, Asp #status predicted SUMMARY #length 718 #molecular-weight 78014 #checksum 5729 SEQUENCE /// ENTRY ALBSGC #type complete TITLE cyclomaltodextrin glucanotransferase (EC 2.4.1.19) precursor [validated] - Bacillus circulans (strain 8) ALTERNATE_NAMES beta-cyclodextrin glycosyltransferase; cyclodextrin synthase ORGANISM #formal_name Bacillus circulans #variety strain 8 DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 15-Sep-2000 ACCESSIONS S23674; S23772 REFERENCE S23674 !$#authors Nitschke, L.; Heeger, K.; Bender, H.; Schulz, G.E. !$#journal Appl. Microbiol. Biotechnol. (1990) 33:542-546 !$#title Molecular cloning, nucleotide sequence and expression in !1Escherichia coli of the beta-cyclodextrin !1glycosyltransferase gene from Bacillus circulans strain no. !18. !$#cross-references MUID:91103970; PMID:1368573 !$#accession S23674 !'##molecule_type DNA !'##residues 1-718 ##label NIT !'##cross-references EMBL:X68326; NID:g39419; PIDN:CAA48401.1; !1PID:g39420 REFERENCE S23772 !$#authors Schiltz, E.; Hofmann, B. !$#submission submitted to the Protein Sequence Database, September 1992 !$#accession S23772 !'##molecule_type protein !'##residues 35-49;'X',167-173,'X',175-180 ##label SCH REFERENCE A51664 !$#authors Klein, C.; Schulz, G.E. !$#submission submitted to the Brookhaven Protein Data Bank, June 1992 !$#cross-references PDB:1CGT !$#contents annotation; X-ray crystallography, 2.0 angstroms, residues !135-718 REFERENCE S14381 !$#authors Klein, C.; Schulz, G.E. !$#journal J. Mol. Biol. (1991) 217:737-750 !$#title Structure of cyclodextrin glycosyltransferase refined at 2.0 !1A resolution. !$#cross-references MUID:91171298; PMID:1826034 !$#contents annotation; X-ray crystallography, 2.0 angstroms FUNCTION !$#description catalyzes the breaking and reformation of 1, !14-alpha-D-glucopyranosyl bonds in long chain polymers to !1form cyclic chains, typically with 6 to 8 subunits !$#note can also catalyze the disproportionation transfer of 6 to 8 !11,4-alpha-D-glucopyranosyl subunits between two long chain !1polymers CLASSIFICATION #superfamily cyclomaltodextrin glucanotransferase; !1alpha-amylase core homology KEYWORDS calcium; duplication; extracellular protein; !1glycosyltransferase; hexosyltransferase; monomer FEATURE !$1-34 #domain signal sequence #status predicted #label SIG\ !$35-718 #product cyclomaltodextrin glucanotransferase #status !8experimental #label MAT\ !$35-172 #domain A1 #label DA1\ !$173-236 #domain B #label DOB\ !$231-365 #domain alpha-amylase core homology #label AMY\ !$237-440 #domain A2 #label DA2\ !$441-528 #domain C #label DOC\ !$529-614 #domain D #label DOD\ !$615-718 #domain E #label DOE\ !$61,63,66,67,85,87 #binding_site calcium (Asp, Asn, Asn, Asn, Gly, Asp) !8#status experimental\ !$77-84 #disulfide_bonds #status experimental\ !$173,224,233,267 #binding_site calcium (Asn, Ile, Asp, His) #status !8experimental\ !$263,291,362 #active_site Asp, Glu, Asp #status experimental SUMMARY #length 718 #molecular-weight 78046 #checksum 8869 SEQUENCE /// ENTRY ALBSG1 #type complete TITLE cyclomaltodextrin glucanotransferase (EC 2.4.1.19) precursor - Bacillus sp. (strain 1011) ORGANISM #formal_name Bacillus sp. DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 18-Jun-1999 ACCESSIONS A26678; B26678 REFERENCE A26678 !$#authors Kimura, K.; Kataoka, S.; Ishii, Y.; Takano, T.; Yamane, K. !$#journal J. Bacteriol. (1987) 169:4399-4402 !$#title Nucleotide sequence of the beta-cyclodextrin !1glucanotransferase gene of alkalophilic Bacillus sp. strain !11011 and similarity of its amino acid sequence to those of !1alpha-amylases. !$#cross-references MUID:87308036; PMID:2957361 !$#accession A26678 !'##molecule_type DNA !'##residues 1-713 ##label KIM !'##cross-references EMBL:M17366; NID:g142675; PIDN:AAA22308.1; !1PID:g142676 !$#accession B26678 !'##molecule_type protein !'##residues 28-30 ##label KI2 FUNCTION !$#description catalyzes the breaking and reformation of 1, !14-alpha-D-glucopyranosyl bonds in long chain polymers to !1form cyclic chains, typically with 6 to 8 subunits !$#note can also catalyze the disproportionation transfer of 6 to 8 !11,4-alpha-D-glucopyranosyl subunits between two long chain !1polymers CLASSIFICATION #superfamily cyclomaltodextrin glucanotransferase; !1alpha-amylase core homology KEYWORDS calcium; duplication; extracellular protein; !1glycosyltransferase; hexosyltransferase; monomer FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-713 #product cyclomaltodextrin glucanotransferase #status !8experimental #label MAT\ !$28-165 #domain A1 #label DA1\ !$166-229 #domain B #label DOB\ !$224-358 #domain alpha-amylase core homology #label AMY\ !$230-433 #domain A2 #label DA2\ !$434-522 #domain C #label DOC\ !$523-609 #domain D #label DOD\ !$610-713 #domain E #label DOE\ !$54,56,59,60,78,80 #binding_site calcium (Asp, Asn, Asn, Asn, Gly, Asp) !8#status predicted\ !$70-77 #disulfide_bonds #status predicted\ !$166,217,226,260 #binding_site calcium (Asn, Ile, Asp, His) #status !8predicted\ !$256,284,355 #active_site Asp, Glu, Asp #status predicted SUMMARY #length 713 #molecular-weight 78340 #checksum 2085 SEQUENCE /// ENTRY ALBSG3 #type complete TITLE cyclomaltodextrin glucanotransferase (EC 2.4.1.19) precursor - Bacillus sp. (strain no. 38-2) ORGANISM #formal_name Bacillus sp. DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jun-2000 ACCESSIONS S24193; S24235; S28785; S26398 REFERENCE S24193 !$#authors Kaneko, T.; Hamamoto, T.; Horikoshi, K. !$#journal J. Gen. Microbiol. (1988) 134:97-105 !$#title Molecular cloning and nucleotide sequence of the !1cyclomaltodextrin glucanotransferase gene from the !1alkalophilic Bacillus sp. strain no. 38-2. !$#cross-references MUID:89036108; PMID:2972812 !$#accession S24193 !'##molecule_type DNA !'##residues 1-712 ##label KAN !'##cross-references EMBL:M19880; NID:g142677; PIDN:AAA22309.1; !1PID:g142678 !$#accession S24235 !'##molecule_type protein !'##residues 28-44 ##label KA2 REFERENCE S28785 !$#authors Hamamoto, T.; Kaneko, T.; Horikoshi, K. !$#journal Agric. Biol. Chem. (1987) 51:2019-2022 !$#title Nucleotide sequence of the cyclomaltodextrin !1glucanotransferase (CGTase) gene from alkalophilic Bacillus !1sp. strain No. 38-2. !$#accession S28785 !'##molecule_type DNA !'##residues 1-581,'SW',590,'HL' ##label HAM !'##cross-references EMBL:D00129; NID:g216247; PIDN:BAA00077.1; !1PID:g216248 FUNCTION !$#description catalyzes the breaking and reformation of 1, !14-alpha-D-glucopyranosyl bonds in long chain polymers to !1form cyclic chains, typically with 6 to 8 subunits !$#note can also catalyze the disproportionation transfer of 6 to 8 !11,4-alpha-D-glucopyranosyl subunits between two long chain !1polymers CLASSIFICATION #superfamily cyclomaltodextrin glucanotransferase; !1alpha-amylase core homology KEYWORDS calcium; duplication; extracellular protein; !1glycosyltransferase; hexosyltransferase; monomer FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-712 #product cyclomaltodextrin glucanotransferase #status !8experimental #label MAT\ !$28-165 #domain A1 #label DA1\ !$166-229 #domain B #label DOB\ !$224-358 #domain alpha-amylase core homology #label AMY\ !$230-433 #domain A2 #label DA2\ !$434-522 #domain C #label DOC\ !$523-608 #domain D #label DOD\ !$609-712 #domain E #label DOE\ !$54,56,59,60,78,80 #binding_site calcium (Asp, Asn, Asn, Asn, Gly, Asp) !8#status predicted\ !$70-77 #disulfide_bonds #status predicted\ !$166,217,226,260 #binding_site calcium (Asn, Ile, Asp, His) #status !8predicted\ !$256,284,355 #active_site Asp, Glu, Asp #status predicted SUMMARY #length 712 #molecular-weight 78249 #checksum 1182 SEQUENCE /// ENTRY ALBSG7 #type complete TITLE cyclomaltodextrin glucanotransferase (EC 2.4.1.19) precursor - Bacillus sp. (strain 17-1) ORGANISM #formal_name Bacillus sp. DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 18-Jun-1999 ACCESSIONS A37208; B37208 REFERENCE A37208 !$#authors Kaneko, T.; Song, K.B.; Hamamoto, T.; Kudo, T.; Horikoshi, !1K. !$#journal J. Gen. Microbiol. (1989) 135:3447-3457 !$#title Construction of a chimeric series of Bacillus !1cyclomaltodextrin glucanotransferases and analysis of the !1thermal stabilities and pH optima of the enzymes. !$#cross-references MUID:90257592; PMID:2534600 !$#accession A37208 !'##molecule_type DNA !'##residues 1-713 ##label KAN !'##cross-references GB:M28053; NID:g142679; PIDN:AAA22310.1; !1PID:g142680 !$#accession B37208 !'##molecule_type protein !'##residues 28-44 ##label KA2 FUNCTION !$#description catalyzes the breaking and reformation of 1, !14-alpha-D-glucopyranosyl bonds in long chain polymers to !1form cyclic chains, typically with 6 to 8 subunits !$#note can also catalyze the disproportionation transfer of 6 to 8 !11,4-alpha-D-glucopyranosyl subunits between two long chain !1polymers CLASSIFICATION #superfamily cyclomaltodextrin glucanotransferase; !1alpha-amylase core homology KEYWORDS calcium; duplication; extracellular protein; !1glycosyltransferase; hexosyltransferase; monomer FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-713 #product cyclomaltodextrin glucanotransferase #status !8experimental #label MAT\ !$28-165 #domain A1 #label DA1\ !$166-229 #domain B #label DOB\ !$224-358 #domain alpha-amylase core homology #label AMY\ !$230-433 #domain A2 #label DA2\ !$434-522 #domain C #label DOC\ !$523-609 #domain D #label DOD\ !$610-713 #domain E #label DOE\ !$54,56,59,60,78,80 #binding_site calcium (Asp, Asn, Asn, Asn, Gly, Asp) !8#status predicted\ !$70-77 #disulfide_bonds #status predicted\ !$166,217,226,260 #binding_site calcium (Asn, Ile, Asp, His) #status !8predicted\ !$256,284,355 #active_site Asp, Glu, Asp #status predicted SUMMARY #length 713 #molecular-weight 77389 #checksum 1777 SEQUENCE /// ENTRY ALBSX1 #type complete TITLE cyclomaltodextrin glucanotransferase (EC 2.4.1.19) precursor - Bacillus sp. (strain 1-1) ALTERNATE_NAMES cyclodextrin glycosyltransferase ORGANISM #formal_name Bacillus sp. DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 24-Apr-1998 ACCESSIONS S26399; S26593 REFERENCE S26399 !$#authors Schmid, G.; Englbrecht, A.; Schmid, D. !$#book Proceedings of the Fourth International Symposium on !1Cyclodextrins, Huber, O., and Szejtli, J., eds., pp.71-76, !1Kluwer Academic Publishers, Dordrecht and Boston, 1988 !$#title Cloning and nucleotide sequence of a cyclodextrin !1glycosyltransferase gene from the alkalophilic Bacillus 1-1. !$#accession S26399 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-703 ##label SCH !$#accession S26593 !'##molecule_type protein !'##residues 30-52 ##label SC2 FUNCTION !$#description catalyzes the breaking and reformation of 1, !14-alpha-D-glucopyranosyl bonds in long chain polymers to !1form cyclic chains, typically with 6 to 8 subunits !$#note can also catalyze the disproportionation transfer of 6 to 8 !11,4-alpha-D-glucopyranosyl subunits between two long chain !1polymers CLASSIFICATION #superfamily cyclomaltodextrin glucanotransferase; !1alpha-amylase core homology KEYWORDS calcium; duplication; extracellular protein; !1glycosyltransferase; hexosyltransferase; monomer FEATURE !$1-29 #domain signal sequence #status predicted #label SIG\ !$30-703 #product cyclomaltodextrin glucanotransferase #status !8experimental #label MAT\ !$30-160 #domain A1 #label DA1\ !$161-224 #domain B #label DOB\ !$219-353 #domain alpha-amylase core homology #label AMY\ !$225-428 #domain A2 #label DA2\ !$429-516 #domain C #label DOC\ !$517-600 #domain D #label DOD\ !$601-703 #domain E #label DOE\ !$52,54,57,58,76,78 #binding_site calcium (Asp, Asn, Asn, Asn, Gly, Asp) !8#status predicted\ !$68-75 #disulfide_bonds #status predicted\ !$161,212,221,255 #binding_site calcium (Asn, Ile, Asp, His) #status !8predicted\ !$251,279,350 #active_site Asp, Glu, Asp #status predicted SUMMARY #length 703 #molecular-weight 78662 #checksum 2696 SEQUENCE /// ENTRY ALBSXF #type complete TITLE cyclomaltodextrin glucanotransferase (EC 2.4.1.19) precursor [validated] - Bacillus stearothermophilus ALTERNATE_NAMES beta-cyclodextrin glycosyltransferase; cyclodextrin glucanotransferase ORGANISM #formal_name Bacillus stearothermophilus DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 19-Jan-2001 ACCESSIONS S26588; S26590; S31284; S31283; S31282 REFERENCE S26588 !$#authors Sugimoto, T.; Kubota, M.; Sakai, S. !$#citation patent application, UK, GB2169902, July, 1986 !$#description Polypeptide possessing cyclomaltodextrin glucanotransferase !1activity. !$#accession S26588 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-711 ##label SUG1 !$#accession S26590 !'##molecule_type protein !'##residues 32-41 ##label SUG2 !'##experimental_source strain FERM-P No. 2225 REFERENCE S31281 !$#authors Fujiwara, S.; Kakihara, H.; Woo, K.B.; Lejeune, A.; !1Kanemoto, M.; Sakaguchi, K.; Imanaka, T. !$#journal Appl. Environ. Microbiol. (1992) 58:4016-4025 !$#title Cyclization characteristics of cyclodextrin !1glucanotransferase are conferred by the NH(2)-terminal !1region of the enzyme. !$#cross-references MUID:93119155; PMID:1476442 !$#accession S31284 !'##molecule_type DNA !'##residues 1-459,'A',461-711 ##label FUJ !'##cross-references EMBL:X59042; NID:g39832; PIDN:CAA41770.1; !1PID:g39833 !'##experimental_source strain NO2 !'##genetics CGT1 !$#accession S31283 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-459,'A',461-711 ##label FU2 !'##cross-references EMBL:X59043; NID:g39836; PIDN:CAA41771.1; !1PID:g39837 !'##experimental_source strain NO2 !'##genetics CGT5 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1991 !$#accession S31282 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-459,'A',461-711 ##label FU3 !'##cross-references EMBL:X59044; NID:g39834; PIDN:CAA41772.1; !1PID:g39835 !'##experimental_source strain NO2 !'##genetics C232 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1991 GENETICS CGT1 !$#gene cgt1 GENETICS CGT5 !$#gene cgt5 GENETICS C232 !$#gene cgt232 FUNCTION !$#description catalyzes the breaking and reformation of 1, !14-alpha-D-glucopyranosyl bonds in long chain polymers to !1form cyclic chains, typically with 6 to 8 subunits !$#note can also catalyze the disproportionation transfer of 6 to 8 !11,4-alpha-D-glucopyranosyl subunits between two long chain !1polymers CLASSIFICATION #superfamily cyclomaltodextrin glucanotransferase; !1alpha-amylase core homology KEYWORDS calcium; duplication; extracellular protein; !1glycosyltransferase; hexosyltransferase; monomer FEATURE !$1-31 #domain signal sequence #status predicted #label SIG\ !$32-711 #product cyclomaltodextrin glucanotransferase #status !8experimental #label MAT\ !$32-165 #domain A1 #label DA1\ !$166-229 #domain B #label DOB\ !$224-358 #domain alpha-amylase core homology #label AMY\ !$230-433 #domain A2 #label DA2\ !$434-522 #domain C #label DOC\ !$523-606 #domain D #label DOD\ !$607-711 #domain E #label DOE\ !$55,57,60,61,79,81 #binding_site calcium (Asp, Asn, Asn, Asn, Gly, Asp) !8#status predicted\ !$71-78 #disulfide_bonds #status predicted\ !$166,217,226,260 #binding_site calcium (Asn, Ile, Asp, His) #status !8predicted\ !$256,284,355 #active_site Asp, Glu, Asp #status predicted SUMMARY #length 711 #molecular-weight 79008 #checksum 4933 SEQUENCE /// ENTRY ALBSXR #type complete TITLE cyclomaltodextrin glucanotransferase (EC 2.4.1.19) precursor [validated] - Bacillus macerans ALTERNATE_NAMES beta-cyclodextrin glycosyltransferase ORGANISM #formal_name Bacillus macerans DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 19-Jan-2001 ACCESSIONS S26589; S26591 REFERENCE S26588 !$#authors Sugimoto, T.; Kubota, M.; Sakai, S. !$#citation patent application, UK, GB2169902, July, 1986 !$#description Polypeptide possessing cyclomaltodextrin glucanotransferase !1activity. !$#accession S26589 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-713 ##label SUG1 !$#accession S26591 !'##molecule_type protein !'##residues 28-37 ##label SUG2 FUNCTION !$#description catalyzes the breaking and reformation of 1, !14-alpha-D-glucopyranosyl bonds in long chain polymers to !1form cyclic chains, typically with 6 to 8 subunits !$#note can also catalyze the disproportionation transfer of 6 to 8 !11,4-alpha-D-glucopyranosyl subunits between two long chain !1polymers CLASSIFICATION #superfamily cyclomaltodextrin glucanotransferase; !1alpha-amylase core homology KEYWORDS calcium; duplication; extracellular protein; !1glycosyltransferase; hexosyltransferase; monomer FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-713 #product cyclomaltodextrin glucanotransferase #status !8experimental #label MAT\ !$28-165 #domain A1 #label DA1\ !$166-229 #domain B #label DOB\ !$224-359 #domain alpha-amylase core homology #label AMY\ !$230-434 #domain A2 #label DA2\ !$435-522 #domain C #label DOC\ !$523-609 #domain D #label DOD\ !$610-713 #domain E #label DOE\ !$54,56,59,60,78,80 #binding_site calcium (Asp, Asn, Asn, Asn, Gly, Asp) !8#status predicted\ !$166,217,226,260 #binding_site calcium (Asn, Ile, Asp, His) #status !8predicted\ !$256,285,356 #active_site Asp, Glu, Asp #status predicted SUMMARY #length 713 #molecular-weight 76857 #checksum 2150 SEQUENCE /// ENTRY S28784 #type complete TITLE alpha-amylase (EC 3.2.1.1) precursor - Bacillus stearothermophilus ORGANISM #formal_name Bacillus stearothermophilus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S28784; S29256 REFERENCE S28784 !$#authors Diderichsen, B.; Christiansen, L. !$#journal FEMS Microbiol. Lett. (1988) 56:53-60 !$#title Cloning of a maltogenic alpha-amylase from Bacillus !1stearothermophilus. !$#accession S28784 !'##molecule_type DNA !'##residues 1-717 ##label DID !'##cross-references EMBL:M36539; NID:g142500; PIDN:AAA22233.1; !1PID:g142501 !$#accession S29256 !'##molecule_type protein !'##residues 34,'XX',37,'X',41-45 ##label DI2 GENETICS !$#gene amyM FUNCTION !$#description catalyzes the hydrolysis of internal 1,4-alpha-D-glucosidic !1bonds !$#pathway glycogen/starch degradation CLASSIFICATION #superfamily cyclomaltodextrin glucanotransferase; !1alpha-amylase core homology KEYWORDS glycosidase; hydrolase; polysaccharide degradation FEATURE !$1-33 #domain signal sequence #status predicted #label SIG\ !$34-717 #product alpha-amylase #status experimental #label !8MAT\ !$229-362 #domain alpha-amylase core homology #label AMY SUMMARY #length 717 #molecular-weight 78723 #checksum 5976 SEQUENCE /// ENTRY ALKBG #type complete TITLE cyclomaltodextrin glucanotransferase (EC 2.4.1.19) precursor - Klebsiella pneumoniae ORGANISM #formal_name Klebsiella pneumoniae DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 18-Jun-1999 ACCESSIONS A29023; B29023 REFERENCE A29023 !$#authors Binder, F.; Huber, O.; Bock, A. !$#journal Gene (1986) 47:269-277 !$#title Cyclodextrin-glycosyltransferase from Klebsiella pneumoniae !1M5a1: cloning, nucleotide sequence and expression. !$#cross-references MUID:87163498; PMID:2951300 !$#accession A29023 !'##molecule_type DNA !'##residues 1-655 ##label BIN !'##cross-references EMBL:M15264; NID:g149178; PIDN:AAA25059.1; !1PID:g149179 !'##note the authors translated the codon CAG for residue 233 as Asn !$#accession B29023 !'##molecule_type protein !'##residues 31-33 ##label BI2 GENETICS !$#gene cgt FUNCTION !$#description catalyzes the breaking and reformation of 1, !14-alpha-D-glucopyranosyl bonds in long chain polymers to !1form cyclic chains, typically with 6 to 8 subunits !$#note can also catalyze the disproportionation transfer of 6 to 8 !11,4-alpha-D-glucopyranosyl subunits between two long chain !1polymers CLASSIFICATION #superfamily cyclomaltodextrin glucanotransferase; !1alpha-amylase core homology KEYWORDS calcium; duplication; extracellular protein; !1glycosyltransferase; hexosyltransferase; monomer FEATURE !$1-30 #domain signal sequence #status predicted #label SIG\ !$31-655 #product cyclomaltodextrin glucanotransferase #status !8experimental #label MAT\ !$33-163 #domain A1 #label DA1\ !$164-226 #domain B #label DOB\ !$221-366 #domain alpha-amylase core homology #label AMY\ !$227-416 #domain A2 #label DA2\ !$417-555 #domain C and D #label DOCD\ !$556-655 #domain E #label DOE\ !$55,57,60,61,79,81 #binding_site calcium (Asp, Asp, Asn, Asn, Gly, Asp) !8#status predicted\ !$164,214,223,257 #binding_site calcium (Asn, Lys, Asp, His) #status !8predicted\ !$253,287,363 #active_site Asp, Glu, Asp #status predicted SUMMARY #length 655 #molecular-weight 73024 #checksum 174 SEQUENCE /// ENTRY A69784 #type complete TITLE macrolide glycosyltransferase homolog ydhE - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A69784 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69784 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-381 ##label KUN !'##cross-references GB:Z99107; GB:AL009126; NID:g2632866; !1PIDN:CAB12391.1; PID:g2632885 !'##experimental_source strain 168 GENETICS !$#gene ydhE CLASSIFICATION #superfamily glycosyltransferase SUMMARY #length 381 #molecular-weight 43025 #checksum 2852 SEQUENCE /// ENTRY C69851 #type complete TITLE macrolide glycosyltransferase homolog yjiC - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS C69851 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69851 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-392 ##label KUN !'##cross-references GB:Z99110; GB:AL009126; NID:g2633472; !1PIDN:CAB13079.1; PID:g2633576 !'##experimental_source strain 168 GENETICS !$#gene yjiC CLASSIFICATION #superfamily glycosyltransferase SUMMARY #length 392 #molecular-weight 43987 #checksum 5091 SEQUENCE /// ENTRY S33184 #type complete TITLE glycosyltransferase (EC 2.4.1.-) - Streptomyces antibioticus ORGANISM #formal_name Streptomyces antibioticus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S33184 REFERENCE S33182 !$#authors Hernandez, C.; Olano, C.; Mendez, C.; Salas, J.A. !$#submission submitted to the EMBL Data Library, April 1993 !$#description Characterization of a Streptomyces antibioticus gene cluster !1encoding a glycosyltransferase involved in oleandomycin !1inactivation. !$#accession S33184 !'##molecule_type DNA !'##residues 1-430 ##label HER !'##cross-references EMBL:Z22577; NID:g404284; PIDN:CAA80301.1; !1PID:g581564 !'##experimental_source ATCC 11891 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily glycosyltransferase KEYWORDS glycosyltransferase; hexosyltransferase SUMMARY #length 430 #molecular-weight 47136 #checksum 1093 SEQUENCE /// ENTRY S74500 #type complete TITLE zeaxanthin glucosyl transferase crtX - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES hypothetical protein slr1125 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S74500 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74500 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-419 ##label KAN !'##cross-references EMBL:D90899; GB:AB001339; NID:g1651650; !1PIDN:BAA16652.1; PID:g1651724 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene crtX CLASSIFICATION #superfamily glycosyltransferase SUMMARY #length 419 #molecular-weight 45330 #checksum 4941 SEQUENCE /// ENTRY ALAS1 #type complete TITLE alpha-amylase (EC 3.2.1.1) 1 precursor [validated] - Aspergillus oryzae ALTERNATE_NAMES alpha-amylase isozyme II; glycogenase; Taka-amylase A ORGANISM #formal_name Aspergillus oryzae DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 15-Sep-2000 ACCESSIONS S04548; A33214; JS0240; A91930; A93767; A10627 REFERENCE S04548 !$#authors Wirsel, S.; Lachmund, A.; Wildhardt, G.; Ruttkowski, E. !$#journal Mol. Microbiol. (1989) 3:3-14 !$#title Three alpha-amylase genes of Aspergillus oryzae exhibit !1identical intron-exon organization. !$#cross-references MUID:89237897; PMID:2785629 !$#accession S04548 !'##molecule_type DNA !'##residues 1-499 ##label WIR !'##cross-references EMBL:X12725; NID:g2430; PIDN:CAA31218.1; !1PID:g295921 !'##genetics AMY1 !$#accession A33214 !'##molecule_type mRNA !'##residues 1-499 ##label WI2 !'##cross-references GB:X12725; NID:g2430; PIDN:CAA31218.1; PID:g295921 REFERENCE JS0240 !$#authors Genes, M.J.; Dove, M.J.; Seligy, V.L. !$#journal Gene (1989) 79:107-117 !$#title Aspergillus oryzae has two nearly identical Taka-amylase !1genes, each containing eight introns. !$#cross-references MUID:89378767; PMID:2789162 !$#accession JS0240 !'##molecule_type DNA !'##residues 1-499 ##label GEN !'##genetics AMY2 !'##note the authors refer to this as isozyme II REFERENCE A91930 !$#authors Isemura, S.; Ikenaka, T. !$#journal J. Biochem. (1973) 74:1-10 !$#cross-references MUID:74001521; PMID:4733850 !$#accession A91930 !'##molecule_type protein !'##residues 206-225 ##label ISE REFERENCE A93767 !$#authors Narita, K. !$#journal Proc. Jpn. Acad. (1975) 51:285-290 !$#accession A93767 !'##molecule_type protein !'##residues 434-443,446-447,'Q',449-458,'GTTV',459-464,467-468,'B',470, !1'B',472-499 ##label NAR REFERENCE A37454 !$#authors Matsuura, Y.; Kusunoki, M.; Harada, W.; Kakudo, M. !$#journal J. Biochem. (1984) 95:697-702 !$#title Structure and possible catalytic residues of Taka-amylase A. !$#cross-references MUID:84212370; PMID:6609921 !$#contents annotation; X-ray crystallography, 3.0 angstroms REFERENCE A51548 !$#authors Swift, H.J.; Brady, L.; Derewenda, Z.S.; Dodson, E.J.; !1Turkenburg, J.P.; Wilkinson, A.J. !$#submission submitted to the Brookhaven Protein Data Bank, August 1992 !$#cross-references PDB:6TAA !$#contents annotation; X-ray crystallography, 2.1 angstroms, residues !122-497 COMMENT One atom of calcium per molecule is essential for activity. GENETICS AMY1 !$#gene amy1 !$#introns 56/3; 69/3; 108/2; 144/3; 221/1; 275/2; 324/2; 404/3 GENETICS AMY2 !$#gene amy2; AmyII !$#introns 56/3; 69/3; 108/2; 144/3; 221/1; 275/2; 324/2; 404/3 FUNCTION !$#description catalyzes the hydrolysis of internal 1,4-alpha-D-glucosidic !1bonds !$#pathway glycogen/starch degradation CLASSIFICATION #superfamily Aspergillus alpha-amylase; alpha-amylase core !1homology KEYWORDS calcium; carbohydrate digestion; glycoprotein; glycosidase; !1hydrolase; polysaccharide degradation FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-499 #product alpha-amylase 1 #status experimental #label !8MAT\ !$194-321 #domain alpha-amylase core homology #label AMY\ !$51-59,171-185, !$261-304,461-496 #disulfide_bonds #status experimental\ !$142,183,196,231 #binding_site calcium (Asn, Glu, Asp, His) #status !8predicted\ !$218 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$227,251,318 #active_site Asp, Glu, Asp #status predicted SUMMARY #length 499 #molecular-weight 54810 #checksum 7889 SEQUENCE /// ENTRY ALAS3 #type complete TITLE alpha-amylase (EC 3.2.1.1) 3 precursor - Aspergillus oryzae ALTERNATE_NAMES alpha-amylase isozyme I; glycogenase; Taka-amylase A ORGANISM #formal_name Aspergillus oryzae DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 18-Jun-1999 ACCESSIONS S04549; A33215; A44713 REFERENCE S04548 !$#authors Wirsel, S.; Lachmund, A.; Wildhardt, G.; Ruttkowski, E. !$#journal Mol. Microbiol. (1989) 3:3-14 !$#title Three alpha-amylase genes of Aspergillus oryzae exhibit !1identical intron-exon organization. !$#cross-references MUID:89237897; PMID:2785629 !$#accession S04549 !'##molecule_type DNA !'##residues 1-499 ##label WIR !'##cross-references EMBL:X12727; NID:g2454; PIDN:CAA31220.1; !1PID:g295922 !$#accession A33215 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-499 ##label WI2 !'##cross-references GB:X12727; NID:g2454; PIDN:CAA31220.1; PID:g295922 REFERENCE JS0240 !$#authors Genes, M.J.; Dove, M.J.; Seligy, V.L. !$#journal Gene (1989) 79:107-117 !$#title Aspergillus oryzae has two nearly identical Taka-amylase !1genes, each containing eight introns. !$#cross-references MUID:89378767; PMID:2789162 !$#accession A44713 !'##molecule_type DNA !'##residues 1-499 ##label GEN !'##note the authors refer to this as isozyme I REFERENCE A37454 !$#authors Matsuura, Y.; Kusunoki, M.; Harada, W.; Kakudo, M. !$#journal J. Biochem. (1984) 95:697-702 !$#title Structure and possible catalytic residues of Taka-amylase A. !$#cross-references MUID:84212370; PMID:6609921 !$#contents annotation; X-ray crystallography, 3.0 angstroms COMMENT One atom of calcium per molecule is essential for activity. GENETICS !$#gene amy3; AmyI !$#introns 56/3; 69/3; 108/2; 144/3; 221/1; 275/2; 324/2; 404/3 FUNCTION !$#description catalyzes the hydrolysis of internal 1,4-alpha-D-glucosidic !1bonds !$#pathway glycogen/starch degradation CLASSIFICATION #superfamily Aspergillus alpha-amylase; alpha-amylase core !1homology KEYWORDS calcium; carbohydrate digestion; glycoprotein; glycosidase; !1hydrolase; metalloprotein; polysaccharide degradation FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-499 #product alpha-amylase 3 #status experimental #label !8MAT\ !$194-321 #domain alpha-amylase core homology #label AMY\ !$51-59,171-185, !$261-304,461-496 #disulfide_bonds #status experimental\ !$142,183,196,231 #binding_site calcium (Asn, Glu, Asp, His) #status !8predicted\ !$218 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$231,251,318 #active_site His, Glu, Asp #status experimental SUMMARY #length 499 #molecular-weight 54804 #checksum 7951 SEQUENCE /// ENTRY A35282 #type complete TITLE alpha-amylase (EC 3.2.1.1) - Aspergillus niger ORGANISM #formal_name Aspergillus niger DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A35282 REFERENCE A35282 !$#authors Boel, E.; Brady, L.; Brzozowski, A.M.; Derewenda, Z.; !1Dodson, G.G.; Jensen, V.J.; Petersen, S.B.; Swift, H.; Thim, !1L.; Woldike, H.F. !$#journal Biochemistry (1990) 29:6244-6249 !$#title Calcium binding in alpha-amylases: an X-ray diffraction !1study at 2.1-angstrom resolution of two enzymes from !1Aspergillus. !$#cross-references MUID:91002514; PMID:2207069 !$#accession A35282 !'##status preliminary; nucleic acid sequence not shown; not compared !1with conceptual translation !'##molecule_type mRNA !'##residues 1-484 ##label BOE FUNCTION !$#description catalyzes the hydrolysis of internal 1,4-alpha-D-glucosidic !1bonds !$#pathway glycogen/starch degradation CLASSIFICATION #superfamily Aspergillus alpha-amylase; alpha-amylase core !1homology KEYWORDS glycoprotein; glycosidase; hydrolase; polysaccharide !1degradation FEATURE !$173-300 #domain alpha-amylase core homology #label AMY SUMMARY #length 484 #molecular-weight 53050 #checksum 7789 SEQUENCE /// ENTRY ALBYAF #type complete TITLE alpha-amylase (EC 3.2.1.1) precursor - yeast (Saccharomycopsis fibuligera) ORGANISM #formal_name Saccharomycopsis fibuligera DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 18-Jun-1999 ACCESSIONS S00064 REFERENCE S00064 !$#authors Itoh, T.; Yamashita, I.; Fukui, S. !$#journal FEBS Lett. (1987) 219:339-342 !$#title Nucleotide sequence of the alpha-amylase gene (ALP1) in the !1yeast Saccharomycopsis fibuligera. !$#cross-references MUID:87276512; PMID:3497057 !$#accession S00064 !'##molecule_type DNA !'##residues 1-494 ##label ITO !'##cross-references EMBL:X05791; NID:g4847; PIDN:CAA29233.1; PID:g4848 !'##note the sequence from Fig. 3 is inconsistent with that from Fig. 1 !1in having 368-Thr GENETICS !$#gene ALP1 FUNCTION !$#description catalyzes the hydrolysis of internal 1,4-alpha-D-glucosidic !1bonds !$#pathway glycogen/starch degradation CLASSIFICATION #superfamily Aspergillus alpha-amylase; alpha-amylase core !1homology KEYWORDS calcium; extracellular protein; glycoprotein; glycosidase; !1hydrolase; metalloprotein; polysaccharide degradation FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-494 #product alpha-amylase #status predicted #label MAT\ !$200-327 #domain alpha-amylase core homology #label AMY\ !$57-65,177-191, !$267-310,462-493 #disulfide_bonds #status predicted\ !$148,189,202,237 #binding_site calcium (Asn, Gln, Asp, His) #status !8predicted\ !$224 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$233,257,324 #active_site Asp, Glu, Asp #status predicted SUMMARY #length 494 #molecular-weight 54386 #checksum 6120 SEQUENCE /// ENTRY JC4510 #type complete TITLE pullulanase (EC 3.2.1.41) precursor - yeast (Lipomyces kononenkoae) ALTERNATE_NAMES LKA1 protein; raw starch-degrading amylase CONTAINS alpha-dextrin endo-1,6-alpha-glucosidase (EC 3.2.1.41) ORGANISM #formal_name Lipomyces kononenkoae DATE 07-Feb-1996 #sequence_revision 23-Aug-1996 #text_change 03-Jun-2002 ACCESSIONS JC4510; PC4116 REFERENCE JC4510 !$#authors Steyn, A.J.C.; Marmur, J.; Pretorius, I.S. !$#journal Gene (1995) 166:65-71 !$#title Cloning, sequence analysis and expression in yeasts of a !1cDNA containing a Lipomyces kononenkoae !1alpha-amylase-encoding gene. !$#cross-references MUID:96105202; PMID:8529895 !$#accession JC4510 !'##molecule_type mRNA !'##residues 1-624 ##label STE !'##cross-references GB:U30376; NID:g1173536; PIDN:AAC49622.1; !1PID:g1173537 !'##experimental_source strain IGC4052B !$#accession PC4116 !'##molecule_type protein !'##residues 29-44 ##label ST2 !'##experimental_source IGC4052B GENETICS !$#gene LKA1 FUNCTION !$#description hydrolyzes raw starch, degrading both alpha-1,4 and alpha-1, !16 linkages !$#pathway glycogen/starch degradation CLASSIFICATION #superfamily Lipomyces alpha-amylase; alpha-amylase core !1homology; glucoamylase starch-binding domain homology KEYWORDS extracellular protein; glycoprotein; glycosidase; hydrolase; !1polysaccharide degradation FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-624 #product alpha-amylase #status predicted #label MAT\ !$48-141 #domain glucoamylase starch-binding domain homology !8#label SBD\ !$320-447 #domain alpha-amylase core homology #label AMY\ !$177-185,297-311, !$387-430,587-622 #disulfide_bonds #status predicted\ !$304,344 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$357,377,444 #active_site His, Glu, Asp #status predicted SUMMARY #length 624 #molecular-weight 68876 #checksum 7457 SEQUENCE /// ENTRY A37008 #type complete TITLE neopullulanase (EC 3.2.1.135) - Bacillus stearothermophilus ORGANISM #formal_name Bacillus stearothermophilus DATE 31-Jan-1992 #sequence_revision 18-Aug-1995 #text_change 18-Jun-1999 ACCESSIONS A37008 REFERENCE A37008 !$#authors Kuriki, T.; Imanaka, T. !$#journal J. Gen. Microbiol. (1989) 135:1521-1528 !$#title Nucleotide sequence of the neopullulanase gene from Bacillus !1stearothermophilus. !$#cross-references MUID:90132572; PMID:2482332 !$#accession A37008 !'##molecule_type DNA !'##residues 1-588 ##label KUR !'##cross-references GB:M28138; NID:g341834; PIDN:AAA22622.1; !1PID:g541633 !'##experimental_source strain TRS40 !'##note amino end of mature protein is Met-Arg-Lys-Glu-Ala GENETICS !$#gene nplT FUNCTION !$#description hydrolysis of alpha-(1->4)-glucosidic linkages of pullulan !1to produce panose (6-alpha-D-glucosylmaltose) !$#pathway pullulan degradation CLASSIFICATION #superfamily neopullulanase; alpha-amylase core homology KEYWORDS extracellular protein; glycosidase; heat-stable protein; !1hydrolase; monomer; polysaccharide degradation FEATURE !$1-588 #product neopullulanase #status experimental #label !8MAT\ !$295-427 #domain alpha-amylase core homology #label AMY\ !$332,357,424 #active_site Glu, Glu, Asp #status predicted SUMMARY #length 588 #molecular-weight 69145 #checksum 2092 SEQUENCE /// ENTRY JS0673 #type complete TITLE neopullulanase (EC 3.2.1.135) - Bacillus sp. ORGANISM #formal_name Bacillus sp. DATE 30-Jun-1992 #sequence_revision 18-Aug-1995 #text_change 16-Jun-2000 ACCESSIONS JS0673 REFERENCE JS0673 !$#authors Igarashi, K.; Ara, K.; Saeki, K.; Ozaki, K.; Kawai, S.; Ito, !1S. !$#journal Biosci. Biotechnol. Biochem. (1992) 56:514-516 !$#title Nucleotide sequence of the gene that encodes a !1neopullulanase from an alkalophilic Bacillus. !$#cross-references MUID:92330017; PMID:1368334 !$#accession JS0673 !'##molecule_type DNA !'##residues 1-583 ##label IGA !'##cross-references GB:D13255; DDBJ:D01187; NID:g216291; !1PIDN:BAA02521.1; PID:g216292 !'##experimental_source strain KSM-1876 COMMENT This enzyme is not heat stable. FUNCTION !$#description hydrolysis of alpha-(1->4)-glucosidic linkages of pullulan !1to produce panose (6-alpha-D-glucosylmaltose) !$#pathway pullulan degradation CLASSIFICATION #superfamily neopullulanase; alpha-amylase core homology KEYWORDS glycosidase; hydrolase; monomer; polysaccharide degradation FEATURE !$294-426 #domain alpha-amylase core homology #label AMY\ !$331,356,423 #active_site Glu, Glu, Asp #status predicted SUMMARY #length 583 #molecular-weight 68608 #checksum 5393 SEQUENCE /// ENTRY S34731 #type complete TITLE amylase (EC 3.2.1.-), maltogenic - Bacillus acidopullulyticus ORGANISM #formal_name Bacillus acidopullulyticus DATE 20-Feb-1995 #sequence_revision 18-Aug-1995 #text_change 18-Jun-1999 ACCESSIONS S34731 REFERENCE S34731 !$#authors Kelly, A.P.; Diderichsen, B.; Jorgensen, S.T.; Mcconnell, !1D.J. !$#submission submitted to the EMBL Data Library, April 1993 !$#description Molecular genetics analysis of a maltogenic amylase gene of !1Bacillus acidopullulyticus. !$#accession S34731 !'##molecule_type DNA !'##residues 1-586 ##label KEL !'##cross-references EMBL:Z22520; NID:g396082; PIDN:CAA80246.1; !1PID:g396083 CLASSIFICATION #superfamily neopullulanase; alpha-amylase core homology KEYWORDS glycosidase; hydrolase FEATURE !$295-427 #domain alpha-amylase core homology #label AMY\ !$332,357,424 #active_site Glu, Glu, Asp #status predicted SUMMARY #length 586 #molecular-weight 68520 #checksum 6578 SEQUENCE /// ENTRY S48130 #type complete TITLE cyclomaltodextrinase (EC 3.2.1.54) - Bacillus sphaericus ORGANISM #formal_name Bacillus sphaericus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S48130 REFERENCE S48130 !$#authors Oguma, T.; Matsuyama, A.; Kikuchi, M.; Nakano, E. !$#journal Appl. Microbiol. Biotechnol. (1993) 39:197-203 !$#title Cloning and sequence analysis of the cyclomaltodextrinase !1gene from Bacillus sphaericus and expression in Escherichia !1coli cells. !$#cross-references MUID:93312539; PMID:7763728 !$#accession S48130 !'##molecule_type DNA !'##residues 1-591 ##label OGU !'##cross-references EMBL:X62576; NID:g393402; PIDN:CAA44454.1; !1PID:g393403 CLASSIFICATION #superfamily neopullulanase; alpha-amylase core homology KEYWORDS glycosidase; hydrolase FEATURE !$294-426 #domain alpha-amylase core homology #label AMY SUMMARY #length 591 #molecular-weight 67898 #checksum 8447 SEQUENCE /// ENTRY JC1486 #type complete TITLE neopullulanase (EC 3.2.1.135) - Thermoactinomyces vulgaris ALTERNATE_NAMES alpha-amylase II ORGANISM #formal_name Thermoactinomyces vulgaris DATE 31-Dec-1993 #sequence_revision 18-Aug-1995 #text_change 16-Jun-2000 ACCESSIONS JC1486 REFERENCE JC1486 !$#authors Tonozuka, T.; Ohtsuka, M.; Mogi, S.; Sakai, H.; Ohta, T.; !1Sakano, Y. !$#journal Biosci. Biotechnol. Biochem. (1993) 57:395-401 !$#title A neopullulanase-type alpha-amylase gene from !1Thermoactinomyces vulgaris R-47. !$#cross-references MUID:93222535; PMID:7763540 !$#accession JC1486 !'##molecule_type DNA !'##residues 1-585 ##label TON !'##cross-references GB:D13178; NID:g391625; PIDN:BAA02473.1; !1PID:g398125 FUNCTION !$#description hydrolysis of alpha-(1->4)-glucosidic linkages of pullulan !1to produce panose (6-alpha-D-glucosylmaltose) !$#pathway pullulan degradation !$#note also has alpha-amylase activity CLASSIFICATION #superfamily neopullulanase; alpha-amylase core homology KEYWORDS glycosidase; hydrolase; polysaccharide degradation FEATURE !$293-424 #domain alpha-amylase core homology #label AMY\ !$329,354,421 #active_site Glu, Glu, Asp #status predicted SUMMARY #length 585 #molecular-weight 67467 #checksum 4196 SEQUENCE /// ENTRY A42950 #type complete TITLE cyclomaltodextrinase (EC 3.2.1.54) - Thermoanaerobacter thermohydrosulfuricus ALTERNATE_NAMES cyclodextrin-degrading enzyme; cyclodextrinase ORGANISM #formal_name Thermoanaerobacter thermohydrosulfuricus DATE 17-Feb-1994 #sequence_revision 18-Aug-1995 #text_change 18-Jun-1999 ACCESSIONS A42950 REFERENCE A42950 !$#authors Podkovyrov, S.M.; Zeikus, J.G. !$#journal J. Bacteriol. (1992) 174:5400-5405 !$#title Structure of the gene encoding cyclomaltodextrinase from !1Clostridium thermohydrosulfuricum 39E and characterization !1of the enzyme purified from Escherichia coli. !$#cross-references MUID:92355516; PMID:1644767 !$#accession A42950 !'##molecule_type DNA !'##residues 1-574 ##label POD !'##cross-references GB:M88602; NID:g144750; PIDN:AAA23219.1; !1PID:g144751 !'##experimental_source Clostridium thermohydrosulfuricum 39E !'##note sequence extracted from NCBI backbone (NCBIP:110537) !'##note amino end of mature protein is Met-Ile-Lys-Gly-Ala FUNCTION !$#description hydrolyzes cyclomaltodextrin to linear maltodextrins; also !1hydrolyzed linear maltodextrin CLASSIFICATION #superfamily neopullulanase; alpha-amylase core homology KEYWORDS glycosidase; heat-stable protein; hydrolase; monomer FEATURE !$1-574 #product neopullulanase #status experimental #label !8MAT\ !$292-424 #domain alpha-amylase core homology #label AMY\ !$329,354,421 #active_site Glu, Glu, Asp #status predicted SUMMARY #length 574 #molecular-weight 68025 #checksum 3953 SEQUENCE /// ENTRY A47102 #type complete TITLE system b(0,+) amino acid transporter-involved protein - human ALTERNATE_NAMES rBAT ORGANISM #formal_name Homo sapiens #common_name man DATE 03-May-1994 #sequence_revision 25-Aug-1995 #text_change 18-Jun-1999 ACCESSIONS A47102; I39384 REFERENCE A47102 !$#authors Bertran, J.; Werner, A.; Chillaron, J.; Nunes, V.; Biber, !1J.; Testar, X.; Zorzano, A.; Estivill, X.; Murer, H.; !1Palacin, M. !$#journal J. Biol. Chem. (1993) 268:14842-14849 !$#title Expression cloning of a human renal cDNA that induces high !1affinity transport of L-cystine shared with dibasic amino !1acids in Xenopus oocytes. !$#cross-references MUID:93315457; PMID:7686906 !$#accession A47102 !'##molecule_type mRNA !'##residues 1-685 ##label BER !'##cross-references GB:L11696; NID:g349705; PIDN:AAA81778.1; !1PID:g349706 !'##experimental_source kidney cortex REFERENCE I39384 !$#authors Lee, W.S.; Wells, R.G.; Sabbag, R.V.; Mohandas, T.K.; !1Hediger, M.A. !$#journal J. Clin. Invest. (1993) 91:1959-1963 !$#title Cloning and chromosomal localization of a human kidney cDNA !1involved in cystine, dibasic, and neutral amino acid !1transport. !$#cross-references MUID:93253036; PMID:8486766 !$#accession I39384 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-617,'I',619-685 ##label RES !'##cross-references GB:M95548; NID:g306441; PIDN:AAA35500.1; !1PID:g306442 GENETICS !$#gene GDB:SLC3A1 !'##cross-references GDB:202968; OMIM:104614 !$#map_position 2p21-2p21 FUNCTION !$#description may be a subunit, or an activator, of the system b(0,+) !1transporter !$#pathway membrane transport of cystine and dibasic and neutral amino !1acids CLASSIFICATION #superfamily system b(0,+) amino acid transporter-involved !1protein; alpha-amylase core homology KEYWORDS amino acid transport; glycoprotein; transmembrane protein FEATURE !$1-88 #domain intracellular #status predicted #label INT\ !$89-110 #domain transmembrane #status predicted #label TMM\ !$111-685 #domain extracellular #status predicted #label EXT\ !$282-452 #domain alpha-amylase core homology #label AMY\ !$214,261,332,495, !$513,575 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 685 #molecular-weight 78851 #checksum 7485 SEQUENCE /// ENTRY A45264 #type complete TITLE system b(0,+) amino acid transporter-involved protein - rabbit ALTERNATE_NAMES rBAT ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 25-Mar-1993 #sequence_revision 25-Aug-1995 #text_change 18-Jun-1999 ACCESSIONS A45264; A45048 REFERENCE A45264 !$#authors Bertran, J.; Werner, A.; Moore, M.L.; Stange, G.; Markovich, !1D.; Biber, J.; Testar, X.; Zorzano, A.; Palacin, M.; Murer, !1H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:5601-5605 !$#title Expression cloning of a cDNA from rabbit kidney cortex that !1induces a single transport system for cystine and dibasic !1and neutral amino acids. !$#cross-references MUID:92302290; PMID:1376925 !$#accession A45264 !'##molecule_type mRNA !'##residues 1-677 ##label BER !'##cross-references GB:M90096; NID:g165687; PIDN:AAA31460.1; !1PID:g165688 !'##experimental_source kidney cortex; clone rBAT-1 !'##note sequence extracted from NCBI backbone (NCBIN:107129, !1NCBIP:107130) REFERENCE A45048 !$#authors Markovich, D.; Stange, G.; Bertran, J.; Palacin, M.; Werner, !1A.; Biber, J.; Murer, H. !$#journal J. Biol. Chem. (1993) 268:1362-1367 !$#title Two mRNA transcripts (rBAT-1 and rBAT-2) are involved in !1system b0,(+)-related amino acid transport. !$#cross-references MUID:93123258; PMID:8419338 !$#accession A45048 !'##molecule_type mRNA !'##residues 1-40,'K',42-212,'A',214-677 ##label MAR !'##cross-references GB:L04504; NID:g165479; PIDN:AAA31391.1; !1PID:g165480 !'##experimental_source kidney cortex; clone rBAT-2 !'##note sequence extracted from NCBI backbone (NCBIP:122108) FUNCTION !$#description membrane transport of cystine, dibasic and neutral amino !1acids !$#pathway amino acid transport !$#note may be a subunit, or an activator, of the system b(0,+) !1transporter CLASSIFICATION #superfamily system b(0,+) amino acid transporter-involved !1protein; alpha-amylase core homology KEYWORDS amino acid transport; glycoprotein; transmembrane protein FEATURE !$1-80 #domain intracellular #status predicted #label INT\ !$81-102 #domain transmembrane #status predicted #label TMM\ !$103-677 #domain extracellular #status predicted #label EXT\ !$274-444 #domain alpha-amylase core homology #label AMY\ !$206,253,324,487, !$505,515,567 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 677 #molecular-weight 77835 #checksum 7197 SEQUENCE /// ENTRY A41785 #type complete TITLE system b(0,+) amino acid transporter-involved protein - rat ALTERNATE_NAMES membrane protein D2; rBAT ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 04-Mar-1993 #sequence_revision 25-Aug-1995 #text_change 18-Jun-1999 ACCESSIONS A41785; A45263 REFERENCE A41785 !$#authors Tate, S.S.; Yan, N.; Udenfriend, S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:1-5 !$#title Expression cloning of a Na(+)-independent neutral amino acid !1transporter from rat kidney. !$#cross-references MUID:92107996; PMID:1729674 !$#accession A41785 !'##molecule_type mRNA !'##residues 1-683 ##label TAT !'##cross-references GB:M77345; NID:g205238; PIDN:AAA41544.1; !1PID:g205239 !'##experimental_source kidney !'##note sequence extracted from NCBI backbone (NCBIN:74682, !1NCBIP:74683) REFERENCE A45263 !$#authors Wells, R.G.; Hediger, M.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:5596-5600 !$#title Cloning of a rat kidney cDNA that stimulates dibasic and !1neutral amino acid transport and has sequence similarity to !1glucosidases. !$#cross-references MUID:92302289; PMID:1376924 !$#accession A45263 !'##molecule_type mRNA !'##residues 1-683 ##label WEL !'##cross-references GB:M80804; NID:g207084; PIDN:AAA73144.1; !1PID:g207085 FUNCTION !$#description may be a subunit, or an activator, of the system b(0,+) !1transporter !$#pathway membrane transport of cystine and dibasic and neutral amino !1acids CLASSIFICATION #superfamily system b(0,+) amino acid transporter-involved !1protein; alpha-amylase core homology KEYWORDS amino acid transport; glycoprotein; transmembrane protein FEATURE !$1-85 #domain intracellular #status predicted #label INT\ !$86-107 #domain transmembrane #status predicted #label TMM\ !$108-683 #domain extracellular #status predicted #label EXT\ !$279-449 #domain alpha-amylase core homology #label AMY\ !$211,238,258,329, !$510,520,574 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 683 #molecular-weight 78506 #checksum 4674 SEQUENCE /// ENTRY ALWT3 #type complete TITLE alpha-amylase (EC 3.2.1.1) 3 precursor - wheat ORGANISM #formal_name Triticum aestivum #common_name common wheat DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 31-Dec-1996 ACCESSIONS S06357 REFERENCE S06357 !$#authors Baulcombe, D.C.; Huttly, A.K.; Martienssen, R.A.; Barker, !1R.F.; Jarvis, M.G. !$#journal Mol. Gen. Genet. (1987) 209:33-40 !$#title A novel wheat alpha-amylase gene (alpha-Amy3). !$#accession S06357 !'##molecule_type DNA !'##residues 1-413 ##label BAU GENETICS !$#gene Amy3 !$#map_position 5A !$#introns 30/3; 327/3 FUNCTION !$#description catalyzes the hydrolysis of internal 1,4-alpha-D-glucosidic !1bonds !$#pathway glycogen/starch degradation CLASSIFICATION #superfamily wheat alpha-amylase; alpha-amylase core !1homology KEYWORDS calcium binding; glycosidase; hydrolase; monomer; !1polysaccharide degradation FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-413 #product alpha-amylase 3 #status predicted #label !8MAT\ !$170-299 #domain alpha-amylase core homology #label AMY\ !$193-208 #domain calcium binding #status predicted #label CAB\ !$203,228,296 #active_site Asp, Glu, Asp #status predicted SUMMARY #length 413 #molecular-weight 45370 #checksum 4883 SEQUENCE /// ENTRY ALBH #type complete TITLE alpha-amylase (EC 3.2.1.1) precursor - barley ORGANISM #formal_name Hordeum vulgare #common_name barley DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 18-Jun-1999 ACCESSIONS A00846; S65602 REFERENCE A00846 !$#authors Rogers, J.C.; Milliman, C. !$#journal J. Biol. Chem. (1983) 258:8169-8174 !$#title Isolation and sequence analysis of a barley alpha-amylase !1cDNA clone. !$#cross-references MUID:83238423; PMID:6190808 !$#accession A00846 !'##molecule_type mRNA !'##residues 1-438 ##label ROG !'##cross-references GB:J01236; NID:g166986; PIDN:AAA32929.1; !1PID:g166987 !'##experimental_source cv. Himalaya REFERENCE S65602 !$#authors Juge, N.; Rodenburg, K.W.; Guo, X.J.; Chaix, J.C.; Svensson, !1B. !$#journal FEBS Lett. (1995) 363:299-303 !$#title Isozyme hybrids within the protruding third loop domain of !1the barley alpha-amylase (beta/alpha)(8)-barrel. Implication !1for BASI sensitivity and substrate affinity. !$#cross-references MUID:95255567; PMID:7737421 !$#accession S65602 !'##molecule_type protein !'##residues 25-29 ##label JUG COMMENT Production of this enzyme in barley is hormonally regulated. !1Germinating barley embryos produce gibberellic acid, which !1stimulates cells covering the endosperm to produce !1alpha-amylase. FUNCTION !$#description catalyzes the hydrolysis of internal 1,4-alpha-D-glucosidic !1bonds !$#pathway glycogen/starch degradation CLASSIFICATION #superfamily wheat alpha-amylase; alpha-amylase core !1homology KEYWORDS calcium binding; glycosidase; hydrolase; monomer; !1polysaccharide degradation FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-438 #product alpha-amylase #status predicted #label MAT\ !$171-318 #domain alpha-amylase core homology #label AMY\ !$204,229,315 #active_site Asp, Glu, Asp #status experimental SUMMARY #length 438 #molecular-weight 47796 #checksum 9025 SEQUENCE /// ENTRY ALBHB #type complete TITLE alpha-amylase (EC 3.2.1.1) B precursor 6-4 - barley ALTERNATE_NAMES 1,4-alpha-D-glucan glucanohydrolase; alpha-amylase 2 ORGANISM #formal_name Hordeum vulgare #common_name barley DATE 30-Jun-1987 #sequence_revision 01-Sep-1995 #text_change 18-Jun-1999 ACCESSIONS A31960; A00847; JE0405; A26267; A24457; A30759 REFERENCE A92700 !$#authors Khursheed, B.; Rogers, J.C. !$#journal J. Biol. Chem. (1988) 263:18953-18960 !$#title Barley alpha-amylase genes. Quantitative comparison of !1steady-state mRNA levels from individual members of the two !1different families expressed in aleurone cells. !$#cross-references MUID:89066691; PMID:3264283 !$#accession A31960 !'##molecule_type DNA !'##residues 1-427 ##label KHU !'##cross-references GB:J04202 !'##experimental_source cv. Himalaya; gene Amy6-4 REFERENCE A00847 !$#authors Rogers, J.C. !$#journal J. Biol. Chem. (1985) 260:3731-3738 !$#title Two barley alpha-amylase gene families are regulated !1differently in aleurone cells. !$#cross-references MUID:85131184; PMID:3871776 !$#accession A00847 !'##molecule_type mRNA !'##residues 1-133,'D',135-194,'HRL',198-424,'Q',426-427 ##label ROG !'##experimental_source seed REFERENCE JE0405 !$#authors Rahmatullah, R.J.; Huang, J.K.; Clark, K.L.; Reeck, G.R.; !1Chandra, G.R.; Muthukrishnan, S. !$#journal Plant Mol. Biol. (1989) 12:119-121 !$#title Nucleotide and predicted amino acid sequences of two !1different genes for high-pI alpha-amylases from barley. !$#accession JE0405 !'##molecule_type DNA !'##residues 1-133,'D',135-424,'Q',426-427 ##label RAH !'##cross-references EMBL:X15226; NID:g18894; PIDN:CAA33298.1; !1PID:g295804 !'##experimental_source gene Amy152 REFERENCE A26267 !$#authors Chandler, P.M.; Zwar, J.A.; Jacobsen, J.V.; Higgins, T.J.V.; !1Inglis, A.S. !$#journal Plant Mol. Biol. (1984) 3:407-418 !$#title The effects of gibberellic acid and abscisic acid on !1alpha-amylase mRNA levels in barley aleurone layers studies !1using an alpha amylase cDNA clone. !$#accession A26267 !'##molecule_type mRNA !'##residues 1-133,'V',135-184,'A',186-366,'GA' ##label CHA !'##experimental_source cv. Himalaya !'##note the authors translated the codon GTC for residue 134 as Gly REFERENCE A24457 !$#authors Svensson, B.; Mundy, J.; Gibson, R.M.; Svendsen, I. !$#journal Carlsberg Res. Commun. (1985) 50:15-22 !$#title Partial amino acid sequences of alpha-amylase isozymes from !1barley malt. !$#accession A24457 !'##molecule_type protein !'##residues 25-59,'X',61-67,'HX',70-85,'X',87-92,'E', !194;146-165;228-251;297-303,'X',305-324,'X',326-337,'X', !1339-342,'X',344-347 ##label SVE COMMENT The mRNA of this isozyme (B) is present at very low levels !1in unstimulated aleurone cells of the seed but increases at !1least 100-fold after stimulation by gibberellic acid, which !1is produced by the embryo during germination. GENETICS !$#gene Amy2-2 !$#map_position 6 !$#introns 29/3; 344/3 !$#note multigene family on chromosome 6 encodes type B !1alpha-amylases; type A alpha-amylase genes are on chromosome !11 FUNCTION !$#description catalyzes the hydrolysis of internal 1,4-alpha-D-glucosidic !1bonds !$#pathway glycogen/starch degradation CLASSIFICATION #superfamily wheat alpha-amylase; alpha-amylase core !1homology KEYWORDS aleurone cell; blocked amino end; calcium binding; !1germination; glycosidase; hydrolase; monomer; polysaccharide !1degradation; seed FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-427 #product alpha-amylase #status experimental #label !8MAT\ !$170-316 #domain alpha-amylase core homology #label AMY\ !$25 #modified_site blocked amino end (Gln) (in mature !8form) (probably pyrrolidone carboxylic acid) #status !8experimental\ !$203,228,313 #active_site Asp, Glu, Asp #status predicted SUMMARY #length 427 #molecular-weight 47355 #checksum 1107 SEQUENCE /// ENTRY JE0406 #type complete TITLE alpha-amylase (EC 3.2.1.1) B precursor (gene Amy56 and others) - barley ALTERNATE_NAMES 1,4-alpha-D-glucan glucanohydrolase ORGANISM #formal_name Hordeum vulgare #common_name barley DATE 17-Apr-1993 #sequence_revision 21-Jan-1997 #text_change 18-Jun-1999 ACCESSIONS JE0406; B30759; S06275; B31960; B21826 REFERENCE JE0405 !$#authors Rahmatullah, R.J.; Huang, J.K.; Clark, K.L.; Reeck, G.R.; !1Chandra, G.R.; Muthukrishnan, S. !$#journal Plant Mol. Biol. (1989) 12:119-121 !$#title Nucleotide and predicted amino acid sequences of two !1different genes for high-pI alpha-amylases from barley. !$#accession JE0406 !'##molecule_type DNA !'##residues 1-429 ##label RAH !'##cross-references EMBL:X15227; NID:g18899; PIDN:CAA33299.1; !1PID:g295805 !'##experimental_source gene Amy56 for alpha-amylase !'##genetics A56 REFERENCE A94535 !$#authors Rogers, J.C. !$#submission submitted to GenBank, September 1988 !$#accession B30759 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-104,'G',106-154,'A',156-160,'PD',163,'G',167-196,'V', !1198-342,'T',344-392,'D',394-429 ##label ROG !'##cross-references GB:J04202; NID:g166984; PIDN:AAA98615.1; !1PID:g166985 !'##experimental_source cv. Himalaya gene Amy46 for alpha-amylase B !'##genetics A46 REFERENCE S06275 !$#authors Knox, C.A.P.; Sonthayanon, B.; Chandra, G.R.; Muthukrishnan, !1S. !$#journal Plant Mol. Biol. (1987) 9:3-17 !$#title Structure and organization of two divergent alpha-amylase !1genes from barley. !$#accession S06275 !'##molecule_type DNA !'##residues 1-11,'LI',14-32,'S',34-57,'I',59-79,'Y',81-139,'R',141-160, !1'PA',163-164,'R',166-196,'V',198-315,'N',317-319,'K', !1321-370,'D',372-392,'D',394-429 ##label KNO !'##cross-references EMBL:M17125; NID:g166978; PIDN:AAA32926.1; !1PID:g166979 !'##experimental_source cv. Sundance gene for alpha-amylase 1 precursor !1(clone p141.117) !'##genetics AA1 !'##note the authors translated the codon TCG for residue 33 as Trp REFERENCE A92700 !$#authors Khursheed, B.; Rogers, J.C. !$#journal J. Biol. Chem. (1988) 263:18953-18960 !$#title Barley alpha-amylase genes. Quantitative comparison of !1steady-state mRNA levels from individual members of the two !1different families expressed in aleurone cells. !$#cross-references MUID:89066691; PMID:3264283 !$#accession B31960 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-51 ##label KHU !'##experimental_source strain Himalaya gene Amy46 for alpha-amylase B !1precursor REFERENCE A92837 !$#authors Huang, J.K.; Swegle, M.; Dandekar, A.M.; Muthukrishnan, S. !$#journal J. Mol. Appl. Genet. (1984) 2:579-588 !$#cross-references MUID:85159405; PMID:6335720 !$#accession B21826 !'##molecule_type mRNA !'##residues 379-389,'T',391-392,'D',394-429 ##label HUA !'##cross-references GB:K02636; NID:g166992; PIDN:AAA32932.1; !1PID:g166993 !'##experimental_source cv. Himalaya aleurone cell mRNA (clone 96 for !1alpha-amylase B) GENETICS A56 !$#gene Amy56 !$#introns 29/3; 346/3 GENETICS A46 !$#gene Amy46 GENETICS AA1 !$#gene Amy1 !$#map_position 6 !$#introns 29/3; 346/3 FUNCTION !$#description catalyzes the hydrolysis of internal 1,4-alpha-D-glucosidic !1bonds !$#pathway glycogen/starch degradation CLASSIFICATION #superfamily wheat alpha-amylase; alpha-amylase core !1homology KEYWORDS aleurone cell; germination; glycosidase; hydrolase; !1polysaccharide degradation; seed FEATURE !$172-318 #domain alpha-amylase core homology #label AMY\ !$205,230,315 #active_site Asp, Glu, Asp #status predicted SUMMARY #length 429 #molecular-weight 47937 #checksum 865 SEQUENCE /// ENTRY ALRZOC #type complete TITLE alpha-amylase (EC 3.2.1.1) precursor (clone OSamy-c) - rice ORGANISM #formal_name Oryza sativa #common_name rice DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 21-Jan-2000 ACCESSIONS S19142; PS0158 REFERENCE S19142 !$#authors Kim, J.K.; Wu, R. !$#journal Plant Mol. Biol. (1992) 18:399-402 !$#title Nucleotide sequence of a high-pI rice (Oryza sativa) !1-amylase gene. !$#cross-references MUID:92119260; PMID:1731997 !$#accession S19142 !'##molecule_type DNA !'##residues 1-383 ##label KIM !'##cross-references EMBL:X52240; NID:g20170; PIDN:CAA36485.1; !1PID:g20171 !'##experimental_source cv. IR26 REFERENCE JT0945 !$#authors Huang, N.; Koizumi, N.; Reinl, S.; Rodriguez, R.L. !$#journal Nucleic Acids Res. (1990) 18:7007-7014 !$#title Structural organization and differential expression of rice !1alpha-amylase genes. !$#cross-references MUID:91088278; PMID:2263460 !$#accession PS0158 !'##molecule_type DNA !'##residues 1-50 ##label HUA !'##cross-references GB:M59350; GB:M36983; NID:g169766; PIDN:AAA33893.1; !1PID:g169767 GENETICS !$#introns 31/3; 75/3; 313/3 FUNCTION !$#description catalyzes the hydrolysis of internal 1,4-alpha-D-glucosidic !1bonds !$#pathway glycogen/starch degradation CLASSIFICATION #superfamily wheat alpha-amylase; alpha-amylase core !1homology KEYWORDS glycosidase; hydrolase; polysaccharide degradation FEATURE !$1-31 #domain signal sequence #status predicted #label SIG\ !$32-383 #product alpha-amylase #status predicted #label MAT\ !$150-289 #domain alpha-amylase core homology #label AMY SUMMARY #length 383 #molecular-weight 43254 #checksum 482 SEQUENCE /// ENTRY ALDYAT #type complete TITLE amylase A (EC 3.2.1.-) - Dictyoglomus thermophilum ORGANISM #formal_name Dictyoglomus thermophilum DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 18-Jun-1999 ACCESSIONS S00628; A34969 REFERENCE S00628 !$#authors Fukusumi, S.; Kamizono, A.; Horinouchi, S.; Beppu, T. !$#journal Eur. J. Biochem. (1988) 174:15-21 !$#title Cloning and nucleotide sequence of a heat-stable amylase !1gene from an anaerobic thermophile, Dictyoglomus !1thermophilum. !$#cross-references MUID:88225097; PMID:2453362 !$#accession S00628 !'##molecule_type DNA !'##residues 1-686 ##label FUK !'##cross-references EMBL:X07896; NID:g2688; PIDN:CAA30735.1; PID:g2689 !$#accession A34969 !'##molecule_type protein !'##residues 2-13 ##label FUK2 GENETICS !$#gene amyA CLASSIFICATION #superfamily Dictyoglomus thermophilum amylase A KEYWORDS glycosidase; hydrolase FEATURE !$2-686 #product amylase A #status experimental #label MAT SUMMARY #length 686 #molecular-weight 81191 #checksum 6463 SEQUENCE /// ENTRY A60473 #type complete TITLE beta-amylase (EC 3.2.1.2) 2 [validated] - soybean ALTERNATE_NAMES 1,4-alpha-D-glucan maltohydrolase ORGANISM #formal_name Glycine max #common_name soybean DATE 20-Feb-1993 #sequence_revision 25-Oct-1996 #text_change 15-Sep-2000 ACCESSIONS A29291; A60473; A24416; S33849 REFERENCE A94637 !$#authors Morita, Y. !$#submission submitted to the Protein Sequence Database, October 1987 !$#accession A29291 !'##molecule_type mRNA !'##residues 1-496 ##label MON REFERENCE A60473 !$#authors Nomura, K.; Mikami, B.; Morita, Y. !$#journal J. Biochem. (1987) 102:341-349 !$#title Partial amino acid sequences around sulfhydryl groups of !1soybean beta-amylase. !$#cross-references MUID:88032954; PMID:2444583 !$#accession A60473 !'##molecule_type protein !'##residues 78-85;94-111;208-210;287-290;343-345;449-453 ##label NOM REFERENCE A24416 !$#authors Mikami, B.; Nomura, K.; Morita, Y. !$#journal J. Biochem. (1986) 100:513-516 !$#title N-terminal sequence of soybean beta-amylase. !$#cross-references MUID:87057111; PMID:2430952 !$#accession A24416 !'##molecule_type protein !'##residues 2-8,'G',10 ##label MIK REFERENCE S33849 !$#authors Totsuka, A.; Fukazawa, C. !$#journal Eur. J. Biochem. (1993) 214:787-794 !$#title Expression and mutation of soybean beta-amylase in !1Escherichia coli. !$#cross-references MUID:93307295; PMID:8319688 !$#accession S33849 !'##status preliminary !'##molecule_type mRNA !'##residues 1-496 ##label TOT !'##cross-references EMBL:X71419; NID:g296446; PIDN:CAA50551.1; !1PID:g296447 REFERENCE A51063 !$#authors Mikami, B.; Hehre, E.J.; Sato, M.; Katsube, Y.; Hirose, M.; !1Morita, Y.; Sacchettini, J.C. !$#submission submitted to the Brookhaven Protein Data Bank, February 1993 !$#cross-references PDB:1BTC !$#contents annotation; X-ray crystallography, 2.0 angstroms, with !1inhibitor alpha-cyclodextrin, residues 6-496 REFERENCE A52292 !$#authors Mikami, B.; Degano, M.; Hehre, E.J.; Sacchettini, J.C. !$#submission submitted to the Brookhaven Protein Data Bank, January 1994 !$#cross-references PDB:1BYA !$#contents annotation; X-ray crystallography, 2.2 angstroms, residues !16-495 REFERENCE A54208 !$#authors Mikami, B.; Degano, M.; Hehre, E.J.; Sacchettini, J.C. !$#journal Biochemistry (1994) 33:7779-7787 !$#title Crystal structures of soybean beta-amylase reacted with !1beta-maltose and maltal: active site components and their !1apparent roles in catalysis. !$#cross-references MUID:94281209; PMID:8011643 !$#contents annotation; X-ray crystallography, 1.9-2.2 angstroms, !1catalytically active (unliganded) and complexed with !1beta-maltose or maltal !$#note the carboxylate of Glu-381 is implicated as the general base !1in the catalytic mechanism; there are no histidine imidazole !1groups close enough to the reaction center to be !1catalytically active; Asp-102 is involved in binding !1substrate REFERENCE A53087 !$#authors Mikami, B.; Hehre, E.J.; Sato, M.; Katsube, Y.; Hirose, M.; !1Morita, Y.; Sacchettini, J.C. !$#journal Biochemistry (1993) 32:6836-6845 !$#title The 2.0-angstrom resolution structure of soybean !1beta-amylase complexed with alpha-cyclodextrin. !$#cross-references MUID:93326569; PMID:8334116 !$#contents annotation; X-ray crystallography, 2.0 angstroms, with !1inhibitor alpha-cyclodextrin REFERENCE A43088 !$#authors Nitta, Y.; Isoda, Y.; Toda, H.; Sakiyama, F. !$#journal J. Biochem. (1989) 105:573-576 !$#title Identification of glutamic acid 186 affinity-labeled by 2, !13-epoxypropyl alpha-D-glucopyranoside in soybean !1beta-amylase. !$#cross-references MUID:89340383; PMID:2474529 !$#contents annotation; active site affinity labeling REFERENCE A43091 !$#authors Totsuka, A.; Nong, V.H.; Kadokawa, H.; Kim, C.S.; Itoh, Y.; !1Fukazawa, C. !$#journal Eur. J. Biochem. (1994) 221:649-654 !$#title Residues essential for catalytic activity of soybean !1beta-amylase. !$#cross-references MUID:94229061; PMID:8174545 !$#contents annotation; active site by mutagenesis FUNCTION !$#description hydrolyzes 1,4-glycosidic linkages of starch, removing !1maltose units successively from the non-reducing end CLASSIFICATION #superfamily beta-amylase KEYWORDS acetylated amino end; glycosidase; hydrolase; monomer; !1polysaccharide degradation FEATURE !$2-496 #product beta-amylase #status experimental #label !8MAT\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental\ !$187 #active_site Glu #status experimental\ !$381 #active_site Glu #status predicted SUMMARY #length 496 #molecular-weight 56142 #checksum 8340 SEQUENCE /// ENTRY JQ2248 #type complete TITLE beta-amylase (EC 3.2.1.2) - rye ALTERNATE_NAMES 1,4-alpha-D-glucan maltohydrolase ORGANISM #formal_name Secale cereale #common_name rye DATE 03-May-1994 #sequence_revision 25-Oct-1996 #text_change 28-May-1999 ACCESSIONS JQ2248 REFERENCE JQ2248 !$#authors Sadowski, J.; Rorat, T.; Cooke, R.; Delseny, M. !$#journal Plant Physiol. (1993) 102:315-316 !$#title Nucleotide sequence of a cDNA clone encoding ubiquitous !1beta-amylase in rye (Secale cereale L.). !$#cross-references MUID:94151427; PMID:8108499 !$#accession JQ2248 !'##molecule_type mRNA !'##residues 1-503 ##label SAD !'##cross-references GB:Z11772; NID:g393449; PIDN:CAA77817.1; !1PID:g393450 FUNCTION !$#description hydrolyzes 1,4-glycosidic linkages of starch, removing !1maltose units successively from the non-reducing end CLASSIFICATION #superfamily beta-amylase KEYWORDS glycoprotein; glycosidase; hydrolase; monomer; !1polysaccharide degradation FEATURE !$2-503 #product beta-amylase #status predicted #label MAT\ !$184,378 #active_site Glu #status predicted\ !$249,338 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 503 #molecular-weight 56759 #checksum 6299 SEQUENCE /// ENTRY S37075 #type complete TITLE beta-amylase (EC 3.2.1.2) - maize ALTERNATE_NAMES 1,4-alpha-D-glucan maltohydrolase ORGANISM #formal_name Zea mays #common_name maize DATE 09-Dec-1993 #sequence_revision 25-Oct-1996 #text_change 18-Jun-1999 ACCESSIONS S37075 REFERENCE S37075 !$#authors Wang, S.; Lue, W.; Chen, J. !$#submission submitted to the EMBL Data Library, September 1993 !$#description Sequence of a beta-amylase cDNA from Zea mays. !$#accession S37075 !'##molecule_type mRNA !'##residues 1-488 ##label WAN !'##cross-references EMBL:Z25871; NID:g397958; PIDN:CAA81091.1; !1PID:g397959 FUNCTION !$#description hydrolyzes 1,4-glycosidic linkages of starch, removing !1maltose units successively from the non-reducing end CLASSIFICATION #superfamily beta-amylase KEYWORDS glycosidase; hydrolase; monomer; polysaccharide degradation FEATURE !$2-488 #product beta-amylase #status predicted #label MAT\ !$184,378 #active_site Glu #status predicted SUMMARY #length 488 #molecular-weight 55180 #checksum 3129 SEQUENCE /// ENTRY S00222 #type complete TITLE beta-amylase (EC 3.2.1.2) - barley ALTERNATE_NAMES 1,4-alpha-D-glucan maltohydrolase ORGANISM #formal_name Hordeum vulgare #common_name barley DATE 30-Jun-1989 #sequence_revision 25-Oct-1996 #text_change 16-Jun-2000 ACCESSIONS S00222; JX0299; PC2019 REFERENCE S00222 !$#authors Kreis, M.; Williamson, M.; Buxton, B.; Pywell, J.; Hejgaard, !1J.; Svendsen, I. !$#journal Eur. J. Biochem. (1987) 169:517-525 !$#title Primary structure and differential expression of !1beta-amylase in normal and mutant barleys. !$#cross-references MUID:88082785; PMID:2446870 !$#accession S00222 !'##molecule_type mRNA !'##residues 1-535 ##label KRE !'##cross-references EMBL:X52321; NID:g18917; PIDN:CAA36556.1; !1PID:g18918 !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing REFERENCE JX0299 !$#authors Yoshigi, N.; Okada, Y.; Sahara, H.; Koshino, S. !$#journal J. Biochem. (1994) 115:47-51 !$#title PCR cloning and sequencing of the beta-amylase cDNA from !1barley. !$#cross-references MUID:94245663; PMID:8188635 !$#accession JX0299 !'##molecule_type mRNA !'##residues 1-232,'A',234-346,'S',348-526,'M',528-535 ##label YOS !'##cross-references GB:D21349; NID:g415599; PIDN:BAA04815.1; !1PID:g464145 !$#accession PC2019 !'##molecule_type protein !'##residues 129-141;152-162;384-394;440-457 ##label YO2 GENETICS !$#map_position 4 FUNCTION !$#description hydrolyzes 1,4-glycosidic linkages of starch, removing !1maltose units successively from the non-reducing end CLASSIFICATION #superfamily beta-amylase KEYWORDS glycosidase; hydrolase; monomer; polysaccharide degradation; !1seed; tandem repeat FEATURE !$2-535 #product beta-amylase #status predicted #label MAT\ !$488-531 #region 11-residue repeats\ !$184,378 #active_site Glu #status predicted SUMMARY #length 535 #molecular-weight 59647 #checksum 1249 SEQUENCE /// ENTRY S36094 #type complete TITLE beta-amylase (EC 3.2.1.2) - Arabidopsis thaliana ALTERNATE_NAMES 1,4-alpha-D-glucan maltohydrolase ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress #variety columbia DATE 31-Dec-1993 #sequence_revision 26-Feb-1999 #text_change 16-Jun-2000 ACCESSIONS B71416; S36094; S37630 REFERENCE A71400 !$#authors Bevan, M.; Bancroft, I.; Bent, E.; Love, K.; Goodman, H.; !1Dean, C.; Bergkamp, R.; Dirkse, W.; Van Staveren, M.; !1Stiekema, W.; Drost, L.; Ridley, P.; Hudson, S.A.; Patel, !1K.; Murphy, G.; Piffanelli, P.; Wedler, H.; Wedler, E.; !1Wambutt, R.; Weitzenegger, T.; Pohl, T.M.; Terryn, N.; !1Gielen, J.; Villarroel, R.; De Clerck, R.; Van Montagu, M.; !1Lecharny, A.; Auborg, S.; Gy, I.; Kreis, M.; Lao, N.; !1Kavanagh, T.; Hempel, S.; Kotter, P.; Entian, K.D.; Rieger, !1M.; Schaeffer, M.; Funk, B.; Mueller-Auer, S.; Silvey, M.; !1James, R.; Montfort, A.; Pons, A.; Puigdomenech, P.; Douka, !1A.; Voukelatou, E.; Milioni, D.; Hatzopoulos, P.; Piravandi, !1E.; Obermaier, B.; Hilbert, H.; Duesterhoft, A.; Moores, T.; !1Jones, J.D.G.; Eneva, T.; Palme, K.; Benes, V.; Rechman, S.; !1Ansorge, W.; Cooke, R.; Berger, C.; Delseny, M.; Voet, M.; !1Volckaert, G.; Mewes, H.W.; Klosterman, S.; Schueller, C.; !1Chalwatzis, N. !$#journal Nature (1998) 391:485-488 !$#title Analysis of 1.9 Mb of contiguous sequence from chromosome 4 !1of Arabidopsis thaliana. !$#cross-references MUID:98121113; PMID:9461215 !$#accession B71416 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-499 ##label BEV !'##cross-references GB:Z97338; NID:g2244870; PIDN:CAB10300.1; !1PID:g2244879 REFERENCE S36094 !$#authors Monroe, J.D.; Salminen, M.D.; Preiss, J. !$#journal Plant Physiol. (1991) 97:1599-1601 !$#title Nucleotide sequence of a cDNA clone encoding a beta-amylase !1from Arabidopsis thaliana. !$#accession S36094 !'##molecule_type mRNA !'##residues 1-155,157-499 ##label MON !'##cross-references EMBL:M73467; NID:g166601; PIDN:AAA32737.1; !1PID:g166602 !$#accession S37630 !'##molecule_type protein !'##residues 228-241;265-272;458-464;467-488 ##label MO2 GENETICS !$#map_position 4COP9-4G3845 FUNCTION !$#description hydrolyzes 1,4-glycosidic linkages of starch, removing !1maltose units successively from the non-reducing end CLASSIFICATION #superfamily beta-amylase KEYWORDS glycosidase; hydrolase; monomer; polysaccharide degradation FEATURE !$2-499 #product beta-amylase #status predicted #label MAT\ !$190,384 #active_site Glu #status predicted SUMMARY #length 499 #molecular-weight 56161 #checksum 2969 SEQUENCE /// ENTRY JC1447 #type complete TITLE beta-amylase (EC 3.2.1.2) - sweet potato ALTERNATE_NAMES 1,4-alpha-D-glucan maltohydrolase ORGANISM #formal_name Ipomoea batatas #common_name sweet potato DATE 30-Sep-1993 #sequence_revision 25-Oct-1996 #text_change 18-Jun-1999 ACCESSIONS JC1447; JX0183; S35667; A29292; JQ0913; JU0045 REFERENCE JC1447 !$#authors Yoshida, N.; Hayashi, K.; Nakamura, K. !$#journal Gene (1992) 120:255-259 !$#title A nuclear gene encoding beta-amylase of sweet potato. !$#cross-references MUID:93013042; PMID:1383095 !$#accession JC1447 !'##molecule_type DNA !'##residues 1-237,'T',239-396,'I',398-499 ##label YOS !'##cross-references DDBJ:D12882; NID:g217935; PIDN:BAA02286.1; !1PID:g217936 !'##note the authors translated the codon GGC for residue 102 as Ala, !1ACC for residue 238 as Ala, ATA for residue 397 as Met, AAC !1for residue 400 as Lys, and GTC for residue 401 as Leu REFERENCE JX0183 !$#authors Yoshida, N.; Nakamura, K. !$#journal J. Biochem. (1991) 110:196-201 !$#title Molecular cloning and expression in Escherichia coli of cDNA !1encoding the subunit of sweet potato beta-amylase. !$#cross-references MUID:92105047; PMID:1837016 !$#accession JX0183 !'##molecule_type mRNA !'##residues 1-256,'LQDGYGQV',265-399,'KL',402-499 ##label YO2 !'##cross-references DDBJ:D01022; NID:g217939; PIDN:BAA00828.1; !1PID:g217940 !'##experimental_source var. Kokei No.14, tuberous root !'##note the authors translated the codon GGC for residue 102 as Ala REFERENCE S35667 !$#authors Toda, H.; Nitta, Y.; Asanami, S.; Kim, J.P.; Sakiyama, F. !$#journal Eur. J. Biochem. (1993) 216:25-38 !$#title Sweet potato beta-amylase. Primary structure and !1identification of the active-site glutamyl residue. !$#cross-references MUID:93373933; PMID:8103452 !$#accession S35667 !'##molecule_type protein !'##residues 2-499 ##label TOD !'##experimental_source commercially available tubers from Korea GENETICS !$#gene AmyB; beta-Amy !$#introns 21/3; 154/3; 209/3; 298/3; 368/3; 448/3 COMPLEX homotetramer; this beta-amylase is unusual in not being !1monomeric FUNCTION !$#description hydrolyzes 1,4-glycosidic linkages of starch, removing !1maltose units successively from the non-reducing end CLASSIFICATION #superfamily beta-amylase KEYWORDS glycosidase; homotetramer; hydrolase; polysaccharide !1degradation FEATURE !$2-499 #product beta-amylase #status experimental #label !8MAT\ !$188 #active_site Glu #status experimental\ !$383 #active_site Glu #status predicted SUMMARY #length 499 #molecular-weight 56079 #checksum 5246 SEQUENCE /// ENTRY A48961 #type complete TITLE beta-amylase - Bacillus cereus ORGANISM #formal_name Bacillus cereus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A48961 REFERENCE A48961 !$#authors Nanmori, T.; Nagai, M.; Shimizu, Y.; Shinke, R.; Mikami, B. !$#journal Appl. Environ. Microbiol. (1993) 59:623-627 !$#title Cloning of the beta-amylase gene from Bacillus cereus and !1characteristics of the primary structure of the enzyme. !$#cross-references MUID:93167830; PMID:8434930 !$#accession A48961 !'##status preliminary !'##molecule_type DNA; protein !'##residues 1-544 ##label NAN !'##cross-references GB:S54911; NID:g265587; PID:g265588 !'##experimental_source BQ10-S1 (SpoII) !'##note sequence inconsistent with the nucleotide translation !'##note sequence extracted from NCBI backbone (NCBIN:125103, !1NCBIP:125104) CLASSIFICATION #superfamily beta-amylase SUMMARY #length 544 #molecular-weight 61277 #checksum 9055 SEQUENCE /// ENTRY A31389 #type complete TITLE beta-amylase (EC 3.2.1.2) precursor, thermophilic - Thermoanaerobacterium thermosulfurigenes ORGANISM #formal_name Thermoanaerobacterium thermosulfurigenes DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A31389 REFERENCE A31389 !$#authors Kitamoto, N.; Yamagata, H.; Kato, T.; Tsukagoshi, N.; Udaka, !1S. !$#journal J. Bacteriol. (1988) 170:5848-5854 !$#title Cloning and sequencing of the gene encoding thermophilic !1beta-amylase of Clostridium thermosulfurogenes. !$#cross-references MUID:89053915; PMID:2461360 !$#accession A31389 !'##molecule_type DNA !'##residues 1-551 ##label KIT !'##cross-references GB:M22471; NID:g144724; PIDN:AAA23204.1; !1PID:g144725 CLASSIFICATION #superfamily beta-amylase KEYWORDS glycosidase; hydrolase; polysaccharide degradation FEATURE !$1-32 #domain signal sequence #status predicted #label SIG\ !$33-551 #product beta-amylase, thermophilic #status predicted !8#label MAT SUMMARY #length 551 #molecular-weight 60547 #checksum 2249 SEQUENCE /// ENTRY S03745 #type complete TITLE beta-amylase (EC 3.2.1.2) precursor - Bacillus circulans ORGANISM #formal_name Bacillus circulans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S03745 REFERENCE S03745 !$#authors Siggens, K.W. !$#journal Mol. Microbiol. (1987) 1:86-91 !$#title Molecular cloning and characterization of the beta-amylase !1gene from Bacillus circulans. !$#cross-references MUID:88260890; PMID:2455212 !$#accession S03745 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-575 ##label SIG1 !'##cross-references GB:Y00523; NID:g39407; PIDN:CAA68578.1; PID:g39408 FUNCTION !$#description catalyzes the hydrolysis of 1,4-glycosidic linkages of !1starch, removing maltose units successively from the !1non-reducing end (beta-amylase activity) CLASSIFICATION #superfamily beta-amylase KEYWORDS glycosidase; hydrolase; polysaccharide degradation FEATURE !$1-36 #domain signal sequence #status predicted #label SIG\ !$37-575 #product beta-amylase #status predicted #label MAT SUMMARY #length 575 #molecular-weight 62899 #checksum 1955 SEQUENCE /// ENTRY ALASGR #type complete TITLE glucan 1,4-alpha-glucosidase (EC 3.2.1.3) precursor - Aspergillus niger ALTERNATE_NAMES 1,4-alpha-D-glucan glucohydrolase; glucoamylase ORGANISM #formal_name Aspergillus niger DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 28-May-1999 ACCESSIONS A90986; A91161; A05287; A22149; A25402 REFERENCE A90986 !$#authors Boel, E.; Hansen, M.T.; Hjort, I.; Hoegh, I.; Fiil, N.P. !$#journal EMBO J. (1984) 3:1581-1585 !$#title Two different types of intervening sequences in the !1glucoamylase gene from Aspergillus niger. !$#cross-references MUID:84261458; PMID:6204865 !$#accession A90986 !'##molecule_type DNA !'##residues 1-640 ##label BOE !'##cross-references GB:X00712; GB:K02466; NID:g2342; PIDN:CAA25303.1; !1PID:g2343 !'##note the authors translated the codon GAT for residue 317 as Asn REFERENCE A91161 !$#authors Svensson, B.; Larsen, K.; Gunnarsson, A. !$#journal Eur. J. Biochem. (1986) 154:497-502 !$#title Characterization of a glucoamylase G2 from Aspergillus !1niger. !$#cross-references MUID:86136085; PMID:3081341 !$#contents comparison of forms G1 and G2 !$#accession A91161 !'##molecule_type protein !'##residues 25-640 ##label SVE COMMENT The large molecular form G1 is shown. COMMENT Smaller molecular forms of the enzyme, G2, arise by !1proteolytic cleavage(s) of the carboxyl end of the large !1form, G1. Only G1 adsorbs and digests raw starch, but both !1forms are equally active towards soluble poly- and !1oligosaccharides. GENETICS !$#introns 72/1; 167/3; 200/1; 412/3 CLASSIFICATION #superfamily Aspergillus glucan 1,4-alpha-glucosidase; !1glucan 1,4-alpha-glucosidase homology KEYWORDS alternative splicing; extracellular protein; glycoprotein; !1glycosidase; hydrolase; polysaccharide degradation FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$23-447 #domain glucan 1,4-alpha-glucosidase homology #label !8GAG\ !$25-640 #product glucan 1,4-alpha-glucosidase G1 #status !8experimental #label GG1\ !$25-538 #product glucan 1,4-alpha-glucosidase G2, long form !8#status experimental #label GG3\ !$25-536 #product glucan 1,4-alpha-glucosidase G2, short form !8#status experimental #label GG2\ !$195,419 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$465,467,468,477, !$483,484,492,508, !$510,513,515,522, !$525,527,529,530,532 #binding_site carbohydrate (Ser) (covalent) #status !8experimental\ !$476,486,488,496, !$499,500,501,502, !$504,506,512,514, !$517,518,520,524, !$526,528,531,534,535 #binding_site carbohydrate (Thr) (covalent) #status !8experimental SUMMARY #length 640 #molecular-weight 68308 #checksum 9634 SEQUENCE /// ENTRY ALBYG #type complete TITLE glucan 1,4-alpha-glucosidase (EC 3.2.1.3) precursor - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES 1,4-alpha-D-glucan glucohydrolase; glucoamylase ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 05-Sep-1997 ACCESSIONS A21896; A23470 REFERENCE A21896 !$#authors Yamashita, I.; Suzuki, K.; Fukui, S. !$#journal J. Bacteriol. (1985) 161:567-573 !$#title Nucleotide sequence of the extracellular glucoamylase gene !1STA1 in the yeast Saccharomyces diastaticus. !$#cross-references MUID:85104778; PMID:3918017 !$#note S. diastaticus !$#accession A21896 !'##molecule_type DNA !'##residues 1-778 ##label YA1 !'##experimental_source strain 5106-9A; ATCC 60709 REFERENCE A23470 !$#authors Yamashita, I.; Suzuki, K.; Sakuzo, F. !$#journal Agric. Biol. Chem. (1986) 50:475-482 !$#title Proteolytic processing of glucoamylase in the yeast !1Saccharomyces cerevisiae. !$#contents signal sequence cleavage site !$#accession A23470 !'##molecule_type protein !'##residues 1-65 ##label YA2 GENETICS !$#gene STA1 CLASSIFICATION #superfamily yeast glucan 1,4-alpha-glucosidase STA1; glucan !11,4-alpha-glucosidase homology KEYWORDS extracellular protein; glycoprotein; glycosidase; hydrolase; !1polysaccharide degradation FEATURE !$1-32 #domain signal sequence #status experimental #label !8SIG\ !$33-778 #product glucan 1,4-alpha-glucosidase #status !8predicted #label MPT\ !$345-778 #domain glucan 1,4-alpha-glucosidase homology #label !8GAG\ !$46,319,333,425,434, !$445,524,557,656, !$661,731,752 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$635 #active_site Asp #status predicted SUMMARY #length 778 #molecular-weight 83730 #checksum 4212 SEQUENCE /// ENTRY JU0474 #type complete TITLE glucan 1,4-alpha-glucosidase (EC 3.2.1.3) STA2 - yeast (Saccharomyces diastaticus) ALTERNATE_NAMES glucoamylase II ORGANISM #formal_name Saccharomyces diastaticus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JU0474; S35895 REFERENCE JU0474 !$#authors Lambrechts, M.G.; Pretorius, I.S.; Sollitti, P.; Marmur, J. !$#journal Gene (1991) 100:95-103 !$#title Primary structure and regulation of a glucoamylase-encoding !1gene (STA2) in Saccharomyces diastaticus. !$#cross-references MUID:91276266; PMID:2055484 !$#accession JU0474 !'##molecule_type DNA !'##residues 1-767 ##label LAM !'##cross-references GB:M60650; NID:g172733; PIDN:AAA35107.1; !1PID:g172734 !'##note the authors translated the codon CCG for residue 337 as Ala, !1CCG for residue 364 as Ala, CCG for residue 404 as Ala, and !1CCG for residue 619 as Ala REFERENCE S35895 !$#authors Kim, K.; Bajszar, G.; Lee, S.Y.; Knudsen, F.; Mattoon, J.R. !$#submission submitted to the EMBL Data Library, May 1992 !$#description Cloning of a new allelic variant of a Saccharomyces !1diastaticus glucoamylase gene and its introduction into !1industrial yeasts. !$#accession S35895 !'##molecule_type DNA !'##residues 1-163,'A',164-622,'D',624-767 ##label KIM !'##cross-references EMBL:M90490; NID:g172735; PIDN:AAA20560.1; !1PID:g172736 GENETICS !$#gene STA2; DEX1 CLASSIFICATION #superfamily yeast glucan 1,4-alpha-glucosidase STA1; glucan !11,4-alpha-glucosidase homology KEYWORDS glycosidase; hydrolase; polysaccharide degradation FEATURE !$334-767 #domain glucan 1,4-alpha-glucosidase homology #label !8GAG SUMMARY #length 767 #molecular-weight 82514 #checksum 1091 SEQUENCE /// ENTRY S48474 #type complete TITLE glucan 1,4-alpha-glucosidase (EC 3.2.1.3) SGA1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES glucoamylase; protein YIL099w ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 12-Nov-1999 ACCESSIONS S48474; C26877; S27284 REFERENCE S48455 !$#authors Bowman, S.; Churcher, C. !$#submission submitted to the EMBL Data Library, September 1994 !$#accession S48474 !'##molecule_type DNA !'##residues 1-549 ##label BOW !'##cross-references GB:Z47047; EMBL:Z38125; NID:g603997; PID:g763247; !1GSPDB:GN00009; MIPS:YIL099w REFERENCE A91831 !$#authors Yamashita, I.; Nakamura, M.; Fukui, S. !$#journal J. Bacteriol. (1987) 169:2142-2149 !$#title Gene fusion is a possible mechanism underlying the evolution !1of STA1. !$#cross-references MUID:87194600; PMID:3106330 !$#accession C26877 !'##molecule_type DNA !'##residues 1-503,507,'W',513-514,'TG',516 ##label YAM !'##cross-references EMBL:M16166; NID:g172592; PIDN:AAA35042.1; !1PID:g172593 REFERENCE S27281 !$#authors Pardo, J.M.; Ianez, E.; Zalacain, M.; Claros, M.G.; Jimenez, !1A. !$#journal FEBS Lett. (1988) 239:179-184 !$#title Similar short elements in the 5' regions of the STA2 and SGA !1genes from Saccharomyces cerevisiae. !$#cross-references MUID:89031230; PMID:3141213 !$#accession S27284 !'##molecule_type DNA !'##residues 1-183,'H',185-190 ##label PAR !'##cross-references EMBL:X13858; NID:g4461; PIDN:CAA32071.1; PID:g4463 GENETICS !$#gene SGD:SGA1; MIPS:YIL099w !'##cross-references SGD:S0001361; MIPS:YIL099w !$#map_position 9L FUNCTION !$#description hydrolysis of terminal 1,4-linked alpha-D-glucose residues !1succesively from non-reducing ends of the chains with !1release of beta-D-glucose CLASSIFICATION #superfamily yeast glucan 1,4-alpha-glucosidase SGA1; glucan !11,4-alpha-glucosidase homology KEYWORDS glycosidase; hydrolase; polysaccharide degradation; yeast !1vacuole FEATURE !$77-536 #domain glucan 1,4-alpha-glucosidase homology #label !8GAG SUMMARY #length 549 #molecular-weight 61462 #checksum 9214 SEQUENCE /// ENTRY A54549 #type complete TITLE glucan 1,4-alpha-glucosidase (EC 3.2.1.3) - yeast (Saccharomycopsis fibuligera) ALTERNATE_NAMES 1,4-alpha-D-glucan glucohydrolase; glucoamylase ORGANISM #formal_name Saccharomycopsis fibuligera DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A54549; S14596 REFERENCE A54549 !$#authors Hostinova, E.; Balanova, J.; Gasperik, J. !$#journal FEMS Microbiol. Lett. (1991) 67:103-108 !$#title The nucleotide sequence of the glucoamylase gene GLA1 from !1Saccharomycopsis fibuligera KZ. !$#cross-references MUID:92137640; PMID:1840532 !$#accession A54549 !'##status preliminary !'##molecule_type DNA !'##residues 1-519 ##label HOS !'##experimental_source KZ !'##note sequence inconsistent with nucleotide translation !'##note sequence extracted from NCBI backbone (NCBIN:78827, !1NCBIP:78828) REFERENCE S14596 !$#authors Hostinova, E.; Gasperik, J. !$#submission submitted to the EMBL Data Library, March 1991 !$#description Nucleotide and deduced amino acid sequence of the !1glucoamylase gene from Saccharomycopsis fibuligera KZ. !$#accession S14596 !'##status preliminary !'##molecule_type DNA !'##residues 1-271,'T',273-519 ##label HO2 !'##cross-references EMBL:X58117 GENETICS !$#gene GLA1 CLASSIFICATION #superfamily yeast glucan 1,4-alpha-glucosidase SGA1; glucan !11,4-alpha-glucosidase homology KEYWORDS glycosidase; hydrolase; polysaccharide degradation FEATURE !$41-506 #domain glucan 1,4-alpha-glucosidase homology #label !8GAG SUMMARY #length 519 #molecular-weight 57654 #checksum 6609 SEQUENCE /// ENTRY S48478 #type complete TITLE glucan 1,4-alpha-glucosidase (EC 3.2.1.3) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES extracellular glucoamylase; mucin-like protein MUC1; protein YIR019c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 12-Nov-1999 ACCESSIONS S48478; A26877; B26877; S27281; JC6123 REFERENCE S48478 !$#authors Rowley, K. !$#submission submitted to the EMBL Data Library, October 1994 !$#accession S48478 !'##molecule_type DNA !'##residues 1-1367 ##label ROW !'##cross-references GB:Z47047; EMBL:Z38061; NID:g603997; PID:g763364; !1GSPDB:GN00009; MIPS:YIR019c REFERENCE A91831 !$#authors Yamashita, I.; Nakamura, M.; Fukui, S. !$#journal J. Bacteriol. (1987) 169:2142-2149 !$#title Gene fusion is a possible mechanism underlying the evolution !1of STA1. !$#cross-references MUID:87194600; PMID:3106330 !$#accession A26877 !'##molecule_type DNA !'##residues 1-242 ##label YAM !'##cross-references EMBL:M16164; NID:g172522; PIDN:AAA35014.1; !1PID:g172525 !$#accession B26877 !'##molecule_type DNA !'##residues 762-1331 ##label YA2 !'##cross-references EMBL:M16165; NID:g172523; PIDN:AAA35015.1; !1PID:g172526 REFERENCE S27281 !$#authors Pardo, J.M.; Ianez, E.; Zalacain, M.; Claros, M.G.; Jimenez, !1A. !$#journal FEBS Lett. (1988) 239:179-184 !$#title Similar short elements in the 5' regions of the STA2 and SGA !1genes from Saccharomyces cerevisiae. !$#cross-references MUID:89031230; PMID:3141213 !$#accession S27281 !'##molecule_type DNA !'##residues 1-31 ##label PAR !'##cross-references EMBL:X13857; NID:g4551; PIDN:CAA32069.1; PID:g4552 REFERENCE JC6123 !$#authors Lambrechts, M.G.; Bauer, F.F.; Marmur, J.; Pretorius, I.S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1996) 93:8419-8424 !$#title Muc1, a mucin-like protein that is regulated by Mss10, is !1critical for pseudohyphal differentiation in yeast. !$#cross-references MUID:96323237; PMID:8710886 !$#accession JC6123 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-1367 ##label LAM !'##cross-references GB:U30626; NID:g1304386; PIDN:AAC49609.1; !1PID:g1304387 GENETICS !$#gene SGD:MUC1; STA2; MAL5; DEX2; SGD:S0001458 !'##cross-references MIPS:YIR019c; SGD:S0001458 !$#map_position 9R CLASSIFICATION #superfamily yeast glucan 1,4-alpha-glucosidase homolog; !1glucan 1,4-alpha-glucosidase homology KEYWORDS glycosidase; hydrolase; polysaccharide degradation; !1transmembrane protein FEATURE !$5-21 #domain transmembrane #status predicted #label TM1\ !$1350-1366 #domain transmembrane #status predicted #label TM2 SUMMARY #length 1367 #molecular-weight 136109 #checksum 3688 SEQUENCE /// ENTRY JP0001 #type complete TITLE glucan 1,4-alpha-glucosidase (EC 3.2.1.3) precursor - Rhizopus oryzae ALTERNATE_NAMES 1,4-alpha-D-glucan glucohydrolase; glucoamylase ORGANISM #formal_name Rhizopus oryzae DATE 28-Dec-1987 #sequence_revision 23-Aug-1996 #text_change 16-Jun-2000 ACCESSIONS JP0001 REFERENCE A90022 !$#authors Ashikari, T.; Nakamura, N.; Tanaka, Y.; Kiuchi, N.; Shibano, !1Y.; Tanaka, T.; Amachi, T.; Yoshizumi, H. !$#journal Agric. Biol. Chem. (1986) 50:957-964 !$#title Rhizopus raw-starch-degrading glucoamylase: its cloning and !1expression in yeast. !$#accession JP0001 !'##molecule_type DNA !'##residues 1-604 ##label ASH !'##cross-references GB:D00049; PIDN:BAA00033.1; PID:g218035 !'##experimental_source strain SAM0034 !'##note there are two errors in the published sequence (personal !1communication): GCT (1101-1103) should be GGT and TAA !1(1894-1896) should be TTA; the deduced amino acid sequence !1corresponds completely to the known amino acid sequence of !111 peptides from glucoamylase, including the amino-terminal !1tetrapeptide sequence of glucoamylase 1 REFERENCE A90023 !$#authors Tanaka, Y.; Ashikari, T.; Nakamura, N.; Kiuchi, N.; Shibano, !1Y.; Amachi, T.; Yoshizumi, H. !$#journal Agric. Biol. Chem. (1980) 50:965-969 !$#title Comparison of amino acid sequences of three glucoamylases !1and their structure-function relationships. !$#contents annotation; homology; predicted secondary structure COMMENT Rhizopus glucoamylase exists in multiple forms, Gluc 1, Gluc !12, and Gluc 3, all of which hydrolyze gelatinized starch at !1similar rates, but only the largest one (Gluc 1) is able to !1adsorb and degrade raw starch. GENETICS !$#introns 51/3; 110/3; 129/1; 436/3 CLASSIFICATION #superfamily Rhizopus glucan 1,4-alpha-glucosidase; glucan !11,4-alpha-glucosidase homology; glucoamylase starch-binding !1domain homology KEYWORDS glycosidase; hydrolase; polysaccharide degradation FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-604 #product glucan 1,4-alpha-glucosidase (Gluc 1) !8#status predicted #label GL1\ !$34-138 #domain glucoamylase starch-binding domain homology !8#label SBD\ !$116-604 #product (or 110-604) glucan 1,4-alpha-glucosidase !8(Gluc 3) #status predicted #label GL3\ !$159-604 #product glucan 1,4-alpha-glucosidase (Gluc 2) !8#status predicted #label GL2\ !$166-592 #domain glucan 1,4-alpha-glucosidase homology #label !8GAG SUMMARY #length 604 #molecular-weight 65079 #checksum 2664 SEQUENCE /// ENTRY JN0102 #type complete TITLE glucan 1,4-alpha-glucosidase (EC 3.2.1.3) GAM1 precursor - yeast (Schwanniomyces occidentalis) ALTERNATE_NAMES acid maltase; glucoamylase ORGANISM #formal_name Schwanniomyces occidentalis DATE 10-Mar-1994 #sequence_revision 05-Apr-1995 #text_change 18-Jun-1999 ACCESSIONS JN0102 REFERENCE JN0102 !$#authors Dohmen, R.J.; Strasser, A.W.M.; Dahlems, U.M.; Hollenberg, !1C.P. !$#journal Gene (1990) 95:111-121 !$#title Cloning of the Schwanniomyces occidentalis glucoamylase gene !1(GAM1) and its expression in Saccharomyces cerevisiae. !$#cross-references MUID:91071592; PMID:1979298 !$#accession JN0102 !'##molecule_type mRNA !'##residues 1-958 ##label DOH !'##cross-references GB:M60207; GB:M34666; NID:g169845; PIDN:AAA33923.1; !1PID:g169846 GENETICS !$#gene GAM1 CLASSIFICATION #superfamily Schwanniomyces glucan 1,4-alpha-glucosidase !1GAM1; sucrase/isomaltase homology KEYWORDS glycoprotein; glycosidase; hydrolase; polysaccharide !1degradation FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-958 #product glucan 1,4-alpha-glucosidase #status !8predicted #label MAT\ !$156-876 #domain sucrase/isomaltase homology #label SIM\ !$61,78,197,403,416, !$513,580,602,813,907 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$470 #active_site Asp #status predicted SUMMARY #length 958 #molecular-weight 106507 #checksum 9563 SEQUENCE /// ENTRY JQ0868 #type complete TITLE glucan 1,4-alpha-glucosidase (EC 3.2.1.3) precursor - Clostridium sp. ALTERNATE_NAMES glucoamylase ORGANISM #formal_name Clostridium sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S24140; JQ0868 REFERENCE S24140 !$#authors Ohnishi, H.; Kitamura, H.; Minowa, T.; Sakai, H.; Ohta, T. !$#journal Eur. J. Biochem. (1992) 207:413-418 !$#title Molecular cloning of a glucoamylase gene from a thermophilic !1Clostridium and kinetics of the cloned enzyme. !$#cross-references MUID:92339427; PMID:1633799 !$#accession S24140 !'##status preliminary !'##molecule_type DNA !'##residues 1-702 ##label OHN !'##cross-references GB:D12818; GB:D00823; NID:g216416; PIDN:BAA02251.1; !1PID:g216417 !'##experimental_source strain G0005 GENETICS !$#gene cga CLASSIFICATION #superfamily Clostridium glucan 1,4-alpha-glucosidase KEYWORDS glycosidase; hydrolase; polysaccharide degradation FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-702 #product glucan 1,4-alpha-glucosidase #status !8predicted #label MAT\ !$455 #active_site Glu #status predicted SUMMARY #length 702 #molecular-weight 78658 #checksum 7891 SEQUENCE /// ENTRY CZCLAM #type complete TITLE cellulase (EC 3.2.1.4) A precursor - Clostridium thermocellum ALTERNATE_NAMES endo-1,4-beta-glucanase A precursor ORGANISM #formal_name Clostridium thermocellum DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 18-Jun-1999 ACCESSIONS A23100; B23100 REFERENCE A23100 !$#authors Beguin, P.; Cornet, P.; Aubert, J.P. !$#journal J. Bacteriol. (1985) 162:102-105 !$#title Sequence of a cellulase gene of the thermophilic bacterium !1Clostridium thermocellum. !$#cross-references MUID:85157393; PMID:3980433 !$#accession A23100 !'##molecule_type DNA !'##residues 1-477 ##label BEG !'##cross-references GB:K03088; NID:g144752; PIDN:AAA83521.1; !1PID:g144753 !$#accession B23100 !'##molecule_type protein !'##residues 33-48 ##label BEG2 GENETICS !$#gene celA FUNCTION !$#description catalyzes the hydrolysis of 1,4-beta-D-glucosidic bonds in !1beta-D-glucans such as cellulose and lichenin; can hydrolyze !1such linkages in beta-D-glucans that also contain 1, !13-linkages !$#pathway cellulose degradation CLASSIFICATION #superfamily cellulase A; Clostridium cellulase repeat !1homology KEYWORDS duplication; extracellular protein; glycosidase; hydrolase; !1polysaccharide degradation FEATURE !$1-32 #domain signal sequence #status predicted #label SIG\ !$33-477 #product cellulase A #status predicted #label MPT\ !$417-440 #domain Clostridium cellulase repeat homology #label !8CCR1\ !$449-472 #domain Clostridium cellulase repeat homology #label !8CCR2 SUMMARY #length 477 #molecular-weight 52593 #checksum 1793 SEQUENCE /// ENTRY JH0158 #type complete TITLE cellulase (EC 3.2.1.4) precursor - Xanthomonas campestris pv. campestris ALTERNATE_NAMES endo-1,4-beta-glucanase; extracellular endoglucanase ORGANISM #formal_name Xanthomonas campestris pv. campestris DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 24-Sep-1999 ACCESSIONS JH0158 REFERENCE JH0158 !$#authors Gough, C.L.; Dow, J.M.; Keen, J.; Henrissat, B.; Daniels, !1M.J. !$#journal Gene (1990) 89:53-59 !$#title Nucleotide sequence of the engXCA gene encoding the major !1endoglucanase of Xanthomonas campestris pv. campestris. !$#cross-references MUID:90323605; PMID:2373365 !$#accession JH0158 !'##molecule_type DNA !'##residues 1-493 ##label GOU !'##cross-references GB:M32700; NID:g155397; PIDN:AAA27612.1; !1PID:g155398 COMMENT Encloglucanase plays a minor role in the early stages of !1pathogenicity of Xanthomonas campestris on turnip and !1radish. GENETICS !$#gene engXCA FUNCTION !$#description hydrolysis of 1,4-beta-D-glucosidic linkages in !1beta-D-glucans such as cellulose and lichenin; can hydrolyze !1such linkages in beta-D-glucans that also contain 1, !13-linkages !$#pathway cellulose degradation CLASSIFICATION #superfamily Xanthomonas campestris cellulase KEYWORDS glycosidase; hydrolase; polysaccharide degradation FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-474 #product cellulase #status predicted #label MAT\ !$375-399 #region proline/threonine-rich SUMMARY #length 493 #molecular-weight 53865 #checksum 4018 SEQUENCE /// ENTRY CZCLBM #type complete TITLE cellulase (EC 3.2.1.4) B precursor - Clostridium thermocellum ALTERNATE_NAMES endo-1,4-beta-glucanase B precursor ORGANISM #formal_name Clostridium thermocellum DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 18-Jun-1999 ACCESSIONS A23512 REFERENCE A23512 !$#authors Grepinet, O.; Beguin, P. !$#journal Nucleic Acids Res. (1986) 14:1791-1799 !$#title Sequence of the cellulase gene of Clostridium thermocellum !1coding for endoglucanase B. !$#cross-references MUID:86148508; PMID:3453102 !$#accession A23512 !'##molecule_type DNA !'##residues 1-563 ##label GRE !'##cross-references GB:X03592; NID:g40668; PIDN:CAA27266.1; PID:g40669 COMMENT This secretory enzyme is part of a highly active and !1thermostable cellulase complex that is involved in !1extracellular cellulose degradation. GENETICS !$#gene celB FUNCTION !$#description catalyzes the hydrolysis of 1,4-beta-D-glucosidic bonds in !1beta-D-glucans such as cellulose and lichenin; can hydrolyze !1such linkages in beta-D-glucans that also contain 1, !13-linkages !$#pathway cellulose degradation CLASSIFICATION #superfamily cellulase B; Clostridium cellulase repeat !1homology KEYWORDS duplication; extracellular protein; glycosidase; hydrolase; !1polysaccharide degradation FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-563 #product cellulase B #status predicted #label MAT\ !$502-525 #domain Clostridium cellulase repeat homology #label !8CCR1\ !$534-557 #domain Clostridium cellulase repeat homology #label !8CCR2 SUMMARY #length 563 #molecular-weight 63929 #checksum 849 SEQUENCE /// ENTRY CZCLDM #type complete TITLE cellulase (EC 3.2.1.4) D precursor [validated] - Clostridium thermocellum ALTERNATE_NAMES CelD; endo-1,4-beta-glucanase D; endoglucanase ORGANISM #formal_name Clostridium thermocellum DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 15-Sep-2000 ACCESSIONS A25535; S55546 REFERENCE A25535 !$#authors Joliff, G.; Beguin, P.; Aubert, J.P. !$#journal Nucleic Acids Res. (1986) 14:8605-8613 !$#title Nucleotide sequence of the cellulase gene celD encoding !1endoglucanase D of Clostridium thermocellum. !$#cross-references MUID:87066732; PMID:3024110 !$#accession A25535 !'##molecule_type DNA !'##residues 1-649 ##label JOL !'##cross-references EMBL:X04584; NID:g40671; PIDN:CAA28255.1; !1PID:g40672 REFERENCE S55546 !$#authors Chitarra, V.; Souchon, H.; Spinelli, S.; Juy, M.; Beguin, !1P.; Alzari, P.M. !$#journal J. Mol. Biol. (1995) 248:225-232 !$#title Multiple crystal forms of endoglucanase CelD: signal peptide !1residues modulate lattice formation. !$#cross-references MUID:95257384; PMID:7739036 !$#accession S55546 !'##molecule_type protein !'##residues 28-31;35-47 ##label CHI REFERENCE A65281 !$#authors Alzari, P.M.; Lascombe, M.B. !$#submission submitted to the Brookhaven Protein Data Bank, January 1995 !$#cross-references PDB:1CLC !$#contents annotation; X-ray crystallography, 1.9 angstroms, residues !135-575 !$#note this form was expressed in Escherichia coli REFERENCE A58611 !$#authors Juy, M.; Amit, A.G.; Alzari, P.M.; Poljak, R.J.; Claeyssens, !1M.; Beguin, P.; Aubert, J.P. !$#journal Nature (1992) 357:89-91 !$#title Three-dimensional structure of a thermostable bacterial !1cellulase. !$#contents annotation; X-ray crystallography, 1.9 angstroms COMMENT This secretory enzyme is part of a highly active and !1thermostable cellulase complex that is involved in !1extracellular cellulose degradation. GENETICS !$#gene celD FUNCTION !$#description catalyzes the hydrolysis of 1,4-beta-D-glucosidic bonds in !1beta-D-glucans such as cellulose and lichenin; can hydrolyze !1such linkages in beta-D-glucans that also contain 1, !13-linkages !$#pathway cellulose degradation CLASSIFICATION #superfamily cellulase D; Clostridium cellulase repeat !1homology KEYWORDS duplication; extracellular protein; glycosidase; hydrolase; !1polysaccharide degradation FEATURE !$1-41 #domain signal sequence #status predicted #label SIG\ !$42-649 #product cellulase D #status predicted #label MAT\ !$585-608 #domain Clostridium cellulase repeat homology #label !8CCR1\ !$621-644 #domain Clostridium cellulase repeat homology #label !8CCR2 SUMMARY #length 649 #molecular-weight 72415 #checksum 389 SEQUENCE /// ENTRY CZCLEM #type complete TITLE cellulase (EC 3.2.1.4) E precursor - Clostridium thermocellum ALTERNATE_NAMES endo-1,4-beta-glucanase E; endoglucanase E ORGANISM #formal_name Clostridium thermocellum DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 18-Jun-1999 ACCESSIONS JT0347 REFERENCE JT0347 !$#authors Hall, J.; Hazlewood, G.P.; Barker, P.J.; Gilbert, H.J. !$#journal Gene (1988) 69:29-38 !$#title Conserved reiterated domains in Clostridium thermocellum !1endoglucanases are not essential for catalytic activity. !$#cross-references MUID:89137992; PMID:3066698 !$#accession JT0347 !'##molecule_type DNA !'##residues 1-814 ##label HAL !'##cross-references GB:M22759; NID:g144768; PIDN:AAA23224.1; !1PID:g144770 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing COMMENT This secretory enzyme is part of a highly active and !1thermostable cellulase complex that is involved in !1extracellular cellulose degradation. GENETICS !$#gene celE !$#start_codon GTG FUNCTION !$#description catalyzes the hydrolysis of 1,4-beta-D-glucosidic bonds in !1beta-D-glucans such as cellulose and lichenin; can hydrolyze !1such linkages in beta-D-glucans that also contain 1, !13-linkages !$#pathway cellulose degradation CLASSIFICATION #superfamily cellulase CCA; Clostridium cellulase repeat !1homology KEYWORDS duplication; extracellular protein; glycosidase; hydrolase; !1polysaccharide degradation FEATURE !$1-34 #domain signal sequence #status predicted #label SIG\ !$35-814 #product cellulase E #status predicted #label MAT\ !$415-438 #domain Clostridium cellulase repeat homology #label !8CCR1\ !$451-474 #domain Clostridium cellulase repeat homology #label !8CCR2 SUMMARY #length 814 #molecular-weight 90244 #checksum 3788 SEQUENCE /// ENTRY CZCLCA #type complete TITLE cellulase (EC 3.2.1.4) CCA precursor - Clostridium sp. ALTERNATE_NAMES endo-1,4-beta-glucanase; endoglucanase-A ORGANISM #formal_name Clostridium sp. DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 06-Dec-1996 ACCESSIONS JH0082 REFERENCE JH0082 !$#authors Faure, E.; Belaich, A.; Bagnara, C.; Gaudin, C.; Belaich, !1J.P. !$#journal Gene (1989) 84:39-46 !$#title Sequence analysis of the Clostridium cellulolyticum !1endoglucanase-A-encoding gene, celCCA. !$#cross-references MUID:90108715; PMID:2558058 !$#accession JH0082 !'##molecule_type DNA !'##residues 1-475 ##label FAU !'##experimental_source ATCC 35319 !'##note a strong homology is found between the C-terminal duplicated !1region of this protein and regions in four endoglucanases !1and one xylanase from Clostridium thermocellum GENETICS !$#gene celCCA FUNCTION !$#description catalyzes the hydrolysis of 1,4-beta-D-glucosidic bonds in !1beta-D-glucans such as cellulose and lichenin; can hydrolyze !1such linkages in beta-D-glucans that also contain 1, !13-linkages !$#pathway cellulose degradation CLASSIFICATION #superfamily cellulase CCA; Clostridium cellulase repeat !1homology KEYWORDS duplication; extracellular protein; glycosidase; hydrolase; !1polysaccharide degradation FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$26-475 #product cellulase #status predicted #label MAT\ !$415-438 #domain Clostridium cellulase repeat homology #label !8CCR1\ !$446-469 #domain Clostridium cellulase repeat homology #label !8CCR SUMMARY #length 475 #molecular-weight 53624 #checksum 5839 SEQUENCE /// ENTRY S28372 #type complete TITLE cellulase (EC 3.2.1.4) III precursor - fungus (Trichoderma reesei) ALTERNATE_NAMES endo-1,4-beta-glucanase; endoglucanase III ORGANISM #formal_name Trichoderma reesei DATE 11-Sep-1998 #sequence_revision 11-Sep-1998 #text_change 18-Jun-1999 ACCESSIONS S28372; S78516; S78517; S02626 REFERENCE S28372 !$#authors Saloheimo, M.; Lehtovaara, P.; Penttilae, M.; Teeri, T.T.; !1Stahlberg, J.; Johansson, G.; Pettersson, G.; Claeyssens, !1M.; Tomme, P.; Knowles, J.K.C. !$#journal Gene (1988) 63:11-21 !$#title EGIII, a new endoglucanase from Trichoderma reesei: the !1characterization of both gene and enzyme. !$#cross-references MUID:88255850; PMID:3384334 !$#accession S28372 !'##molecule_type DNA !'##residues 1-418 ##label SAL1 !'##cross-references EMBL:M19373; NID:g170548; PIDN:AAA34213.1; !1PID:g170549 !$#accession S78516 !'##molecule_type mRNA !'##residues 1-418 ##label SAL2 !'##cross-references GB:M19373; NID:g170548; PIDN:AAA34213.1; !1PID:g170549 !$#accession S78517 !'##molecule_type protein !'##residues 22-23,'X',25-46,'XX',49-58 ##label SAL3 REFERENCE S02625 !$#authors Stahlberg, J.; Johansson, G.; Pettersson, G. !$#journal Eur. J. Biochem. (1988) 173:179-183 !$#title A binding-site-deficient, catalytically active, core protein !1of endoglucanase III from the culture filtrate of !1Trichoderma reesei. !$#cross-references MUID:88185316; PMID:3356188 !$#accession S02626 !'##molecule_type protein !'##residues 'XXXX',87-88,'V',90,'X',92-93,'Y',95-99 ##label STA !'##experimental_source culture filtrate GENETICS !$#gene egl3 !$#introns 110/2 FUNCTION !$#description hydrolysis of 1,4-beta-D-glucosidic linkages in !1beta-D-glucans such as cellulose and lichenin; can hydrolyze !1such linkages in beta-D-glucans that also contain 1, !13-linkages !$#pathway cellulose degradation CLASSIFICATION #superfamily Trichoderma cellulase III; fungal !1cellulose-binding domain homology KEYWORDS blocked amino end; glycoprotein; glycosidase; hydrolase; !1polysaccharide degradation; pyroglutamic acid FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-418 #product cellulase #status experimental #label MAT1\ !$26-57 #domain fungal cellulose-binding domain homology !8#label FCB\ !$83-418 #product cellulase core #status experimental #label !8MAT2\ !$22 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$124 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 418 #molecular-weight 44227 #checksum 4626 SEQUENCE /// ENTRY S68153 #type complete TITLE cellulase (EC 3.2.1.4) 3D precursor - Penicillium janthinellum ALTERNATE_NAMES 3D endoglucanase 2; endo-1,4-beta-glucanase ORGANISM #formal_name Penicillium janthinellum DATE 11-Sep-1998 #sequence_revision 11-Sep-1998 #text_change 18-Jun-1999 ACCESSIONS S68153; S57950 REFERENCE S68153 !$#authors Mernitz, G.; Koch, A.; Henrissat, B.; Schulz, G. !$#journal Curr. Genet. (1996) 29:490-495 !$#title Endoglucanase II (EGII) of Penicillium janthinellum: cDNA !1sequence, heterologous expression and promotor analysis. !$#cross-references MUID:96207475; PMID:8625430 !$#accession S68153 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type mRNA !'##residues 1-410 ##label MER !'##cross-references EMBL:X89564; NID:g984165; PIDN:CAA61740.1; !1PID:g984166 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1995 FUNCTION !$#description hydrolysis of 1,4-beta-D-glucosidic linkages in !1beta-D-glucans such as cellulose and lichenin; can hydrolyze !1such linkages in beta-D-glucans that also contain 1, !13-linkages !$#pathway cellulose degradation CLASSIFICATION #superfamily Trichoderma cellulase III; fungal !1cellulose-binding domain homology KEYWORDS glycosidase; hydrolase; polysaccharide degradation FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-410 #product cellulase #status predicted #label MAT\ !$26-57 #domain fungal cellulose-binding domain homology !8#label FCB SUMMARY #length 410 #molecular-weight 43914 #checksum 8684 SEQUENCE /// ENTRY JC5461 #type complete TITLE cellulase (EC 3.2.1.4) precursor - imperfect fungus (Humicola grisea) ALTERNATE_NAMES endo-1,4-beta-glucanase; endoglucanase ORGANISM #formal_name Humicola grisea var. thermoidea DATE 11-Sep-1998 #sequence_revision 11-Sep-1998 #text_change 16-Jun-2000 ACCESSIONS JC5461 REFERENCE JC5461 !$#authors Takashima, S.; Nakamura, A.; Masaki, H.; Uozumi, T. !$#journal Biosci. Biotechnol. Biochem. (1997) 61:245-250 !$#title Cloning, sequencing, and expression of a thermostable !1cellulase gene of Humicola grisea. !$#cross-references MUID:97212020; PMID:9058960 !$#accession JC5461 !'##molecule_type DNA !'##residues 1-388 ##label TAK !'##cross-references DDBJ:D84470; NID:g1304101; PIDN:BAA12676.1; !1PID:g1304102 !'##experimental_source strain IFO9854 GENETICS !$#gene egl2 !$#introns 120/3; 369/1 FUNCTION !$#description hydrolysis of 1,4-beta-D-glucosidic linkages in !1beta-D-glucans such as cellulose and lichenin; can hydrolyze !1such linkages in beta-D-glucans that also contain 1, !13-linkages !$#pathway cellulose degradation CLASSIFICATION #superfamily Trichoderma cellulase III; fungal !1cellulose-binding domain homology KEYWORDS glycosidase; hydrolase; polysaccharide degradation FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-388 #product cellulase #status predicted #label MAT\ !$21-52 #domain fungal cellulose-binding domain homology !8#label FCB SUMMARY #length 388 #molecular-weight 42606 #checksum 4069 SEQUENCE /// ENTRY S43920 #type complete TITLE cellulase (EC 3.2.1.4) precursor - imperfect fungus (Humicola insolens) ALTERNATE_NAMES endo-1,4-beta-glucanase; endoglucanase ORGANISM #formal_name Humicola insolens DATE 11-Sep-1998 #sequence_revision 11-Sep-1998 #text_change 18-Jun-1999 ACCESSIONS S43920 REFERENCE S43919 !$#authors Dalboge, H.; Heldt-Hansen, H.P. !$#journal Mol. Gen. Genet. (1994) 243:253-260 !$#title A novel method for efficient expression cloning of fungal !1enzyme genes. !$#cross-references MUID:94247364; PMID:8190078 !$#accession S43920 !'##molecule_type mRNA !'##residues 1-388 ##label DAL !'##cross-references EMBL:X76046; NID:g505194; PIDN:CAA53631.1; !1PID:g505195 GENETICS !$#gene CMC3 FUNCTION !$#description hydrolysis of 1,4-beta-D-glucosidic linkages in !1beta-D-glucans such as cellulose and lichenin; can hydrolyze !1such linkages in beta-D-glucans that also contain 1, !13-linkages !$#pathway cellulose degradation CLASSIFICATION #superfamily Trichoderma cellulase III; fungal !1cellulose-binding domain homology KEYWORDS glycosidase; hydrolase; polysaccharide degradation FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-388 #product cellulase #status predicted #label MAT\ !$21-52 #domain fungal cellulose-binding domain homology !8#label FCB SUMMARY #length 388 #molecular-weight 42563 #checksum 4303 SEQUENCE /// ENTRY JS0589 #type complete TITLE endo-1,4-beta-xylanase (EC 3.2.1.8) A precursor - Streptomyces lividans ALTERNATE_NAMES xylanase A ORGANISM #formal_name Streptomyces lividans DATE 10-Mar-1994 #sequence_revision 22-Nov-1996 #text_change 26-Feb-1999 ACCESSIONS JS0589; PS0238 REFERENCE JS0589 !$#authors Shareck, F.; Roy, C.; Yaguchi, M.; Morosoli, R.; Kluepfel, !1D. !$#journal Gene (1991) 107:75-82 !$#title Sequences of three genes specifying xylanases in !1Streptomyees lividans. !$#cross-references MUID:92077439; PMID:1743521 !$#accession JS0589 !'##molecule_type DNA !'##residues 1-477 ##label SHA !'##cross-references GB:M64551 !$#accession PS0238 !'##molecule_type protein !'##residues 42-92 ##label SH2 GENETICS !$#gene xlnA FUNCTION !$#description catalyzes the hydrolysis of 1,4-beta-xylosidic bonds in !1xylans !$#pathway xylan degradation CLASSIFICATION #superfamily Streptomyces endo-1,4-beta-xylanase A; !1Streptomyces endo-1,4-beta-xylanase A homology KEYWORDS extracellular protein; glycosidase; hydrolase; !1polysaccharide degradation FEATURE !$1-41 #domain signal sequence #status predicted #label SIG\ !$42-477 #product endo-1,4-beta-xylanase A #status !8experimental #label MAT\ !$74-341 #domain Streptomyces endo-1,4-beta-xylanase A !8homology #label SXY\ !$169,277 #active_site Glu #status predicted SUMMARY #length 477 #molecular-weight 51215 #checksum 4489 SEQUENCE /// ENTRY S13391 #type complete TITLE endo-1,4-beta-xylanase (EC 3.2.1.8) B - Pseudomonas fluorescens subsp. cellulosa ALTERNATE_NAMES xylanase B ORGANISM #formal_name Pseudomonas fluorescens subsp. cellulosa DATE 17-Apr-1993 #sequence_revision 11-Apr-1997 #text_change 18-Jun-1999 ACCESSIONS S13391 REFERENCE S13391 !$#authors Kellett, L.E.; Poole, D.M.; Ferreira, L.M.A.; Durrant, A.J.; !1Hazlewood, G.P.; Gilbert, H.J. !$#journal Biochem. J. (1990) 272:369-376 !$#title Xylanase B and an arabinofuranosidase from Pseudomonas !1fluorescens subsp. cellulosa contain identical !1cellulose-binding domains and are encoded by adjacent genes. !$#cross-references MUID:91097447; PMID:2125205 !$#accession S13391 !'##molecule_type DNA !'##residues 1-592 ##label KEL !'##cross-references EMBL:X54523; NID:g45523; PIDN:CAA38389.1; !1PID:g45524 GENETICS !$#gene xynB FUNCTION !$#description catalyzes the hydrolysis of 1,4-beta-xylosidic linkages in !1xylans !$#pathway xylan degradation CLASSIFICATION #superfamily Pseudomonas endo-1,4-beta-xylanase B; bacterial !1cellulose-binding domain homology; Streptomyces endo-1, !14-beta-xylanase A homology KEYWORDS glycosidase; hydrolase; polysaccharide degradation FEATURE !$38-134 #domain bacterial cellulose-binding domain homology !8#label BCB\ !$337-592 #domain Streptomyces endo-1,4-beta-xylanase A !8homology #label SXY\ !$39-133 #disulfide_bonds #status predicted\ !$431,530 #active_site Glu #status predicted SUMMARY #length 592 #molecular-weight 63410 #checksum 9500 SEQUENCE /// ENTRY S06047 #type complete TITLE endo-1,4-beta-xylanase (EC 3.2.1.8) A precursor - Pseudomonas fluorescens subsp. cellulosa ORGANISM #formal_name Pseudomonas fluorescens subsp. cellulosa DATE 01-Dec-1989 #sequence_revision 11-Apr-1997 #text_change 18-Jun-1999 ACCESSIONS S06047 REFERENCE S06047 !$#authors Hall, J.; Hazlewood, G.P.; Huskisson, N.S.; Durrant, A.J.; !1Gilbert, H.J. !$#journal Mol. Microbiol. (1989) 3:1211-1219 !$#title Conserved serine-rich sequences in xylanase and cellulase !1from Pseudomonas fluorescens subspecies cellulosa: internal !1signal sequence and unusual protein processing. !$#cross-references MUID:90014181; PMID:2507868 !$#accession S06047 !'##molecule_type DNA !'##residues 1-611 ##label HAL !'##cross-references EMBL:X15429; NID:g45519; PIDN:CAA33469.1; !1PID:g45520 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing GENETICS !$#gene xynA FUNCTION !$#description catalyzes the hydrolysis of 1,4-beta-xylosidic linkages in !1xylans !$#pathway xylan degradation CLASSIFICATION #superfamily Pseudomonas endo-1,4-beta-xylanase A; bacterial !1cellulose-binding domain homology; glycosidase GWGW domain !1homology; Streptomyces endo-1,4-beta-xylanase A homology KEYWORDS glycosidase; hydrolase; polysaccharide degradation FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-611 #product endo-1,4-beta-xylanase #status predicted !8#label MAT\ !$30-126 #domain bacterial cellulose-binding domain homology !8#label BCB\ !$183-220 #domain glycosidase GWGW domain homology #label GWG\ !$296-608 #domain Streptomyces endo-1,4-beta-xylanase A !8homology #label SXY\ !$31-125 #disulfide_bonds #status predicted SUMMARY #length 611 #molecular-weight 64830 #checksum 6487 SEQUENCE /// ENTRY S61311 #type complete TITLE endo-1,4-beta-xylanase (EC 3.2.1.8) A - Thermotoga maritima (strain MSB8) ALTERNATE_NAMES xylanase A ORGANISM #formal_name Thermotoga maritima DATE 27-Apr-1996 #sequence_revision 11-Apr-1997 #text_change 21-Jul-2000 ACCESSIONS S61311; A72422 REFERENCE S61311 !$#authors Winterhalter, C.; Heinrich, P.; Candussio, A.; Wich, G.; !1Liebl, W. !$#journal Mol. Microbiol. (1995) 15:431-444 !$#title Identification of a novel cellulose-binding domain within !1the multidomain 120 kDa xylanase XynA of the !1hyperthermophilic bacterium Thermotoga maritima. !$#cross-references MUID:95302955; PMID:7783614 !$#accession S61311 !'##molecule_type DNA !'##residues 1-1059 ##label WIN !'##cross-references EMBL:Z46264; NID:g559959; PIDN:CAA86406.1; !1PID:g559960 !'##experimental_source strain MSB8 (DSM 3109) REFERENCE A72200 !$#authors Nelson, K.E.; Clayton, R.A.; Gill, S.R.; Gwinn, M.L.; !1Dodson, R.J.; Haft, D.H.; Hickey, E.K.; Peterson, J.D.; !1Nelson, W.C.; Ketchum, K.A.; McDonald, L.; Utterback, T.R.; !1Malek, J.A.; Linher, K.D.; Garrett, M.M.; Stewart, A.M.; !1Cotton, M.D.; Pratt, M.S.; Phillips, C.A.; Richardson, D.; !1Heidelberg, J.; Sutton, G.G.; Fleischmann, R.D.; White, O.; !1Salzberg, S.L.; Smith, H.O.; Venter, J.C.; Fraser, C.M. !$#journal Nature (1999) 399:323-329 !$#title Evidence for lateral gene transfer between Archaea and !1Bacteria from genome sequence of Thermotoga maritima. !$#cross-references MUID:99287316; PMID:10360571 !$#accession A72422 !'##molecule_type DNA !'##residues 1-1059 ##label ARN !'##cross-references GB:AE001693; GB:AE000512; NID:g4980547; !1PIDN:AAD35155.1; PID:g4980548; TIGR:TM0061 !'##experimental_source strain MSB8 GENETICS !$#gene xynA FUNCTION !$#description catalyzes the hydrolysis of 1,4-beta-xylosidic bonds in !1xylans !$#pathway xylan degradation CLASSIFICATION #superfamily Thermotoga endo-1,4-beta-xylanase A; !1Streptomyces endo-1,4-beta-xylanase A homology; Thermotoga !1xylanase A amino-terminal repeat homology; Thermotoga !1xylanase A cellulose-binding repeat homology KEYWORDS duplication; glycosidase; hydrolase; polysaccharide !1degradation FEATURE !$50-195 #domain Thermotoga xylanase A amino-terminal repeat !8homology #label TXA1\ !$204-349 #domain Thermotoga xylanase A amino-terminal repeat !8homology #label TXA2\ !$397-693 #domain Streptomyces endo-1,4-beta-xylanase A !8homology #label SXY\ !$700-868 #domain Thermotoga xylanase A cellulose-binding !8repeat homology #label TXC1\ !$871-1058 #domain Thermotoga xylanase A cellulose-binding !8repeat homology #label TXC2 SUMMARY #length 1059 #molecular-weight 119642 #checksum 8243 SEQUENCE /// ENTRY A48490 #type complete TITLE endo-1,4-beta-xylanase (EC 3.2.1.8) A precursor - Thermoanaerobacterium saccharolyticum (strain B6A-RI) ORGANISM #formal_name Thermoanaerobacterium saccharolyticum DATE 03-May-1994 #sequence_revision 11-Apr-1997 #text_change 16-Jul-1999 ACCESSIONS A48490 REFERENCE A48490 !$#authors Lee, Y.E.; Lowe, S.E.; Henrissat, B.; Zeikus, J.G. !$#journal J. Bacteriol. (1993) 175:5890-5898 !$#title Characterization of the active site and thermostability !1regions of endoxylanase from Thermoanaerobacterium !1saccharolyticum B6A-RI. !$#cross-references MUID:93388520; PMID:8376336 !$#accession A48490 !'##molecule_type DNA !'##residues 1-1231 ##label LEE !'##cross-references GB:M97882; NID:g533366; PIDN:AAA21812.1; !1PID:g533367 !'##experimental_source strain B6A-RI !'##note mutation experiments support roles for Asp-537, Glu-600, and !1Asp-602; His-572 can be replaced by Asn with some loss of !1activity, but Asn could conceivably function similarly; the !1roles of Glu-495, Asn-539, and His-572 are supported by !1X-ray reference A55905 on another molecule with this same !1domain GENETICS !$#gene xynA FUNCTION !$#description catalyzes the hydrolysis of 1,4-beta-xylosidic linkages in !1xylans !$#pathway xylan degradation CLASSIFICATION #superfamily Thermoanaerobacterium endo-1,4-beta-xylanase A; !1S-layer repeat homology; Streptomyces endo-1,4-beta-xylanase !1A homology; Thermotoga xylanase A amino-terminal repeat !1homology; Thermotoga xylanase A cellulose-binding repeat !1homology KEYWORDS duplication; glycosidase; heat-stable protein; hydrolase; !1polysaccharide degradation FEATURE !$1-33 #domain signal sequence #status predicted #label SIG\ !$34-1231 #product endo-1,4-beta-xylanase A #status predicted !8#label MAT\ !$39-186 #domain Thermotoga xylanase A amino-terminal repeat !8homology #label TXA1\ !$196-340 #domain Thermotoga xylanase A amino-terminal repeat !8homology #label TXA2\ !$386-676 #domain Streptomyces endo-1,4-beta-xylanase A !8homology #label SXY\ !$683-854 #domain Thermotoga xylanase A cellulose-binding !8repeat homology #label TXC1\ !$858-1043 #domain Thermotoga xylanase A cellulose-binding !8repeat homology #label TXC2\ !$1056-1109 #domain S-layer repeat homology #label SLR1\ !$1115-1168 #domain S-layer repeat homology #label SLR2\ !$1179-1231 #domain S-layer repeat homology #status atypical !8#label SLR3\ !$495,572,600,602 #active_site Glu, His, Glu, Asp #status predicted\ !$537,539 #binding_site substrate (Asp, Asn) #status predicted SUMMARY #length 1231 #molecular-weight 136355 #checksum 9395 SEQUENCE /// ENTRY S41797 #type complete TITLE cellulose 1,4-beta-cellobiosidase (EC 3.2.1.91) precursor - Clostridium thermocellum ALTERNATE_NAMES xylanase X ORGANISM #formal_name Clostridium thermocellum DATE 20-May-1994 #sequence_revision 11-Apr-1997 #text_change 16-Jul-1999 ACCESSIONS S41797 REFERENCE S41797 !$#authors Pack, M.Y.; Jung, K.H. !$#submission submitted to the EMBL Data Library, February 1993 !$#description Nucleotide sequence of exo-beta-1,4-glucanase gene of !1Clostridium thermocellum. !$#accession S41797 !'##molecule_type DNA !'##residues 1-1087 ##label PAC !'##cross-references EMBL:M67438; NID:g144775; PIDN:AAA23227.1; !1PID:g144776 GENETICS !$#gene xynX FUNCTION !$#description catalyzes the hydrolysis of 1,4-beta-D-glucosidic bonds in !1cellulose to release the disaccharide cellobiose CLASSIFICATION #superfamily Thermoanaerobacterium endo-1,4-beta-xylanase A; !1S-layer repeat homology; Streptomyces endo-1,4-beta-xylanase !1A homology; Thermotoga xylanase A amino-terminal repeat !1homology; Thermotoga xylanase A cellulose-binding repeat !1homology KEYWORDS duplication; glycosidase; hydrolase; polysaccharide !1degradation FEATURE !$1-30 #domain signal sequence #status predicted #label SIG\ !$31-1087 #product cellulose 1,4-beta-cellobiosidase #status !8predicted #label MAT\ !$38-185 #domain Thermotoga xylanase A amino-terminal repeat !8homology #label TXA\ !$238-528 #domain Streptomyces endo-1,4-beta-xylanase A !8homology #label SXY\ !$535-706 #domain Thermotoga xylanase A cellulose-binding !8repeat homology #label TXC1\ !$710-895 #domain Thermotoga xylanase A cellulose-binding !8repeat homology #label TXC2\ !$908-961 #domain S-layer repeat homology #label SLR1\ !$967-1020 #domain S-layer repeat homology #label SLR2\ !$1031-1086 #domain S-layer repeat homology #label SLR3\ !$347,424,452,454 #active_site Glu, His, Glu, Asp #status predicted\ !$389,391 #binding_site substrate (Asp, Asn) #status predicted SUMMARY #length 1087 #molecular-weight 120357 #checksum 9657 SEQUENCE /// ENTRY I39760 #type complete TITLE endo-1,4-beta-xylanase (EC 3.2.1.8) - Bacillus stearothermophilus ORGANISM #formal_name Bacillus stearothermophilus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS I39760 REFERENCE I39759 !$#authors Baba, T.; Shinke, R.; Nanmori, T. !$#journal Appl. Environ. Microbiol. (1994) 60:2252-2258 !$#title Identification and characterization of clustered genes for !1thermostable xylan-degrading enzymes, beta-xylosidase and !1xylanase, of Bacillus stearothermophilus 21. !$#cross-references MUID:94354640; PMID:8074507 !$#accession I39760 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-330 ##label RES !'##cross-references GB:D28121; NID:g456581; PIDN:BAA05668.1; !1PID:g499714 FUNCTION !$#description catalyzes the hydrolysis of 1,4-beta-xylosidic linkages in !1xylans !$#pathway xylan degradation CLASSIFICATION #superfamily Bacillus endo-beta-1,4-xylanase; Streptomyces !1endo-1,4-beta-xylanase A homology KEYWORDS glycosidase; hydrolase; polysaccharide degradation FEATURE !$33-330 #domain Streptomyces endo-1,4-beta-xylanase A !8homology #label SXY SUMMARY #length 330 #molecular-weight 38473 #checksum 5304 SEQUENCE /// ENTRY S59634 #type complete TITLE endo-1,4-beta-xylanase (EC 3.2.1.8) F precursor - Pseudomonas fluorescens ORGANISM #formal_name Pseudomonas fluorescens DATE 15-Feb-1996 #sequence_revision 11-Apr-1997 #text_change 18-Jun-1999 ACCESSIONS S59634; S52749 REFERENCE S59631 !$#authors Millward-Sadler, S.J.; Davidson, K.; Hazlewood, G.P.; Black, !1G.W.; Gilbert, H.J.; Clarke, J.H. !$#journal Biochem. J. (1995) 312:39-48 !$#title Novel cellulose-binding domains, NodB homologues and !1conserved modular architecture in xylanases from the aerobic !1soil bacteria Pseudomonas fluorescens subsp. cellulosa and !1Cellvibrio mixtus. !$#cross-references MUID:96077124; PMID:7492333 !$#accession S59634 !'##molecule_type DNA !'##residues 1-606 ##label MIL !'##cross-references EMBL:Z48928; NID:g758226; PIDN:CAA88764.1; !1PID:g758227 GENETICS !$#gene xynF FUNCTION !$#description catalyzes the hydrolysis of 1,4-beta-xylosidic linkages in !1xylans !$#pathway xylan degradation CLASSIFICATION #superfamily Pseudomonas endo-1,4-beta-xylanase F; !1Streptomyces endo-1,4-beta-xylanase A homology KEYWORDS glycosidase; hydrolase; polysaccharide degradation FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-606 #product endo-1,4-beta-xylanase F #status predicted !8#label MAT\ !$284-597 #domain Streptomyces endo-1,4-beta-xylanase A !8homology #label SXY\ !$385,497 #active_site Glu #status predicted SUMMARY #length 606 #molecular-weight 64841 #checksum 6457 SEQUENCE /// ENTRY S59632 #type complete TITLE endo-1,4-beta-xylanase (EC 3.2.1.8) B precursor - Cellvibrio mixtus ORGANISM #formal_name Cellvibrio mixtus DATE 15-Feb-1996 #sequence_revision 11-Apr-1997 #text_change 18-Jun-1999 ACCESSIONS S59632; S52742 REFERENCE S59631 !$#authors Millward-Sadler, S.J.; Davidson, K.; Hazlewood, G.P.; Black, !1G.W.; Gilbert, H.J.; Clarke, J.H. !$#journal Biochem. J. (1995) 312:39-48 !$#title Novel cellulose-binding domains, NodB homologues and !1conserved modular architecture in xylanases from the aerobic !1soil bacteria Pseudomonas fluorescens subsp. cellulosa and !1Cellvibrio mixtus. !$#cross-references MUID:96077124; PMID:7492333 !$#accession S59632 !'##molecule_type DNA !'##residues 1-621 ##label MIL !'##cross-references EMBL:Z48926; NID:g757808; PIDN:CAA88762.1; !1PID:g757809 GENETICS !$#gene xynB FUNCTION !$#description catalyzes the hydrolysis of 1,4-beta-xylosidic linkages in !1xylans !$#pathway xylan degradation CLASSIFICATION #superfamily Pseudomonas endo-1,4-beta-xylanase F; !1Streptomyces endo-1,4-beta-xylanase A homology KEYWORDS glycosidase; hydrolase; polysaccharide degradation FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-621 #product endo-1,4-beta-xylanase B #status predicted !8#label MAT\ !$302-615 #domain Streptomyces endo-1,4-beta-xylanase A !8homology #label SXY\ !$403,516 #active_site Glu #status predicted SUMMARY #length 621 #molecular-weight 64929 #checksum 1375 SEQUENCE /// ENTRY A31842 #type complete TITLE endo-1,4-beta-xylanase (EC 3.2.1.8) Z precursor - Clostridium thermocellum ALTERNATE_NAMES xylanase Z ORGANISM #formal_name Clostridium thermocellum DATE 31-Mar-1990 #sequence_revision 11-Apr-1997 #text_change 18-Jun-1999 ACCESSIONS A31842 REFERENCE A31842 !$#authors Grepinet, O.; Chebrou, M.C.; Beguin, P. !$#journal J. Bacteriol. (1988) 170:4582-4588 !$#title Nucleotide sequence and deletion analysis of the xylanase !1gene (xynZ) of Clostridium thermocellum. !$#cross-references MUID:89008072; PMID:3139632 !$#accession A31842 !'##molecule_type DNA !'##residues 1-837 ##label GRE !'##cross-references GB:M22624; NID:g144931; PIDN:AAA23286.1; !1PID:g144932 GENETICS !$#gene xynZ FUNCTION !$#description catalyzes the hydrolysis of 1,4-beta-xylosidic linkages in !1xylans !$#pathway xylan degradation CLASSIFICATION #superfamily Clostridium endo-1,4-beta-xylanase Z; !1Clostridium cellulase repeat homology; Clostridium xylanase !1A repeat homology; Streptomyces endo-1,4-beta-xylanase A !1homology KEYWORDS duplication; extracellular protein; glycosidase; heat-stable !1protein; hydrolase; polysaccharide degradation FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-837 #product endo-1,4-beta-xylanase #status predicted !8#label MAT\ !$326-419 #domain Clostridium xylanase A repeat homology #label !8CXA\ !$430-453 #domain Clostridium cellulase repeat homology #label !8CCR1\ !$464-487 #domain Clostridium cellulase repeat homology #label !8CCR2\ !$548-834 #domain Streptomyces endo-1,4-beta-xylanase A !8homology #label SXY\ !$645,754 #active_site Glu #status predicted SUMMARY #length 837 #molecular-weight 92262 #checksum 316 SEQUENCE /// ENTRY WWBSXP #type complete TITLE endo-1,4-beta-xylanase (EC 3.2.1.8) A precursor - Bacillus pumilus ALTERNATE_NAMES xylanase A ORGANISM #formal_name Bacillus pumilus DATE 20-Sep-1984 #sequence_revision 20-Sep-1984 #text_change 06-Dec-1996 ACCESSIONS A00848 REFERENCE A00848 !$#authors Fukusaki, E.; Panbangred, W.; Shinmyo, A.; Okada, H. !$#journal FEBS Lett. (1984) 171:197-201 !$#title The complete nucleotide sequence of the xylanase gene (xynA) !1of Bacillus pumilus. !$#accession A00848 !'##molecule_type DNA !'##residues 1-228 ##label FUK GENETICS !$#gene xynA FUNCTION !$#description catalyzes the hydrolysis of 1,4-beta-xylosidic bonds in !1xylans !$#pathway xylan degradation CLASSIFICATION #superfamily endo-1,4-beta-xylanase; endo-1,4-beta-xylanase !1homology KEYWORDS extracellular protein; glycosidase; hydrolase; !1polysaccharide degradation FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-228 #product endo-1,4-beta-xylanase A #status predicted !8#label MAT\ !$40-222 #domain endo-1,4-beta-xylanase homology #label XYL\ !$120,209 #active_site Glu #status predicted SUMMARY #length 228 #molecular-weight 25521 #checksum 3801 SEQUENCE /// ENTRY S12745 #type complete TITLE endo-1,4-beta-xylanase (EC 3.2.1.8) B precursor - Clostridium acetobutylicum ALTERNATE_NAMES xylanase B ORGANISM #formal_name Clostridium acetobutylicum DATE 30-Sep-1993 #sequence_revision 22-Nov-1996 #text_change 18-Jun-1999 ACCESSIONS S12745 REFERENCE S12745 !$#authors Zappe, H.; Jones, W.A.; Woods, D.R. !$#journal Nucleic Acids Res. (1990) 18:2179 !$#title Nucleotide sequence of a Clostridium acetobutylicum P262 !1xylanase gene (xynB). !$#cross-references MUID:90245673; PMID:2336398 !$#accession S12745 !'##molecule_type DNA !'##residues 1-261 ##label ZAP !'##cross-references EMBL:M31726; NID:g144933; PIDN:AAA23287.1; !1PID:g144934 !'##experimental_source strain P262 GENETICS !$#gene xynB FUNCTION !$#description catalyzes the hydrolysis of 1,4-beta-xylosidic bonds in !1xylans !$#pathway xylan degradation CLASSIFICATION #superfamily endo-1,4-beta-xylanase; endo-1,4-beta-xylanase !1homology KEYWORDS extracellular protein; glycosidase; hydrolase; !1polysaccharide degradation FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-261 #product endo-1,4-beta-xylanase B #status predicted !8#label MAT\ !$72-255 #domain endo-1,4-beta-xylanase homology #label XYL\ !$152,242 #active_site Glu #status predicted SUMMARY #length 261 #molecular-weight 29032 #checksum 6764 SEQUENCE /// ENTRY I40569 #type complete TITLE endo-1,4-beta-xylanase (EC 3.2.1.8) A precursor - Bacillus subtilis ALTERNATE_NAMES xylanase A ORGANISM #formal_name Bacillus subtilis DATE 12-Aug-1996 #sequence_revision 02-Jul-1998 #text_change 21-Jul-2000 ACCESSIONS I40569; S39157; S39158; A53635; F69735; S51711 REFERENCE I40370 !$#authors Wolf, M.; Geczi, A.; Simon, O.; Borriss, R. !$#journal Microbiology (1995) 141:281-290 !$#title Genes encoding xylan and beta-glucan hydrolysing enzymes in !1Bacillus subtilis: characterization, mapping and !1construction of strains deficient in lichenase, cellulase !1and xylanase. !$#cross-references MUID:95219081; PMID:7704256 !$#accession I40569 !'##status nucleic acid sequence not shown; translation not shown; !1translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-22,'P',24-213 ##label WOL !'##cross-references EMBL:Z34519; NID:g2995396; PIDN:CAA84276.1; !1PID:g607050 !'##experimental_source strain 168 REFERENCE S39157 !$#authors Paice, M.G.; Bourbonnais, R.; Desrochers, M.; Jurasek, L.; !1Yaguchi, M. !$#journal Arch. Microbiol. (1986) 144:201-206 !$#title A xylanase gene from Bacillus subtilis: nucleotide sequence !1and comparison with B. pumilus gene. !$#accession S39157 !'##molecule_type DNA !'##residues 1-213 ##label PAI1 !'##cross-references EMBL:M36648; NID:g143842; PIDN:AAA22897.1; !1PID:g143843 !'##experimental_source strain PAP115 !$#accession S39158 !'##molecule_type protein !'##residues 29-58;60-73;75-76 ##label PAI2 !'##experimental_source strain PAP115 REFERENCE A53635 !$#authors Miao, S.; Ziser, L.; Aebersold, R.; Withers, S.G. !$#journal Biochemistry (1994) 33:7027-7032 !$#title Identification of glutamic acid 78 as the active site !1nucleophile in Bacillus subtilis xylanase using electrospray !1tandem mass spectrometry. !$#cross-references MUID:94271752; PMID:7911679 !$#accession A53635 !'##status preliminary !'##molecule_type protein !'##residues 97-107 ##label MIA REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69735 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-213 ##label KUN !'##cross-references GB:Z99114; GB:AL009126; NID:g2634230; !1PIDN:CAB13776.1; PID:g2634277 !'##experimental_source strain 168 GENETICS !$#gene xynA !$#map_position 175 degrees FUNCTION !$#description catalyzes the hydrolysis of 1,4-beta-xylosidic bonds in !1xylans !$#pathway xylan degradation CLASSIFICATION #superfamily endo-1,4-beta-xylanase; endo-1,4-beta-xylanase !1homology KEYWORDS extracellular protein; glycosidase; hydrolase; !1polysaccharide degradation FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-213 #product endo-1,4-beta-xylanase A #status !8experimental #label MAT\ !$31-213 #domain endo-1,4-beta-xylanase homology #label XYL\ !$106 #active_site Glu #status experimental\ !$200 #active_site Glu #status predicted SUMMARY #length 213 #molecular-weight 23345 #checksum 2430 SEQUENCE /// ENTRY S01734 #type complete TITLE endo-1,4-beta-xylanase (EC 3.2.1.8) A precursor [validated] - Bacillus circulans ALTERNATE_NAMES xylanase A ORGANISM #formal_name Bacillus circulans DATE 07-Jun-1990 #sequence_revision 22-Nov-1996 #text_change 15-Sep-2000 ACCESSIONS S01734 REFERENCE S01734 !$#authors Yang, R.C.A.; MacKenzie, C.R.; Narang, S.A. !$#journal Nucleic Acids Res. (1988) 16:7187 !$#title Nucleotide sequence of a Bacillus circulans xylanase gene. !$#cross-references MUID:88303346; PMID:3405767 !$#accession S01734 !'##status translation not shown !'##molecule_type DNA !'##residues 1-213 ##label YAN !'##cross-references EMBL:X07723; NID:g39462; PIDN:CAA30553.1; !1PID:g39463 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE A53181 !$#authors Wakarchuk, W.W.; Campbell, R.L.; Sung, W.L.; Davoodi, J.; !1Yaguchi, M. !$#journal Protein Sci. (1994) 3:467-475 !$#title Mutational and crystallographic analyses of the active site !1residues of the Bacillus circulans xylanase. !$#cross-references MUID:94290322; PMID:8019418 !$#contents annotation; X-ray crystallography, 1.49 angstroms, residues !129-213 REFERENCE A52866 !$#authors Campbell, R.L. !$#submission submitted to the Brookhaven Protein Data Bank, June 1994 !$#cross-references PDB:1XNB !$#contents annotation; X-ray crystallography, 1.49 angstroms, residues !129-213 GENETICS !$#gene xlnA FUNCTION !$#description catalyzes the hydrolysis of 1,4-beta-xylosidic bonds in !1xylans !$#pathway xylan degradation CLASSIFICATION #superfamily endo-1,4-beta-xylanase; endo-1,4-beta-xylanase !1homology KEYWORDS extracellular protein; glycosidase; hydrolase; !1polysaccharide degradation FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-213 #product endo-1,4-beta-xylanase A #status !8experimental #label MAT\ !$31-213 #domain endo-1,4-beta-xylanase homology #label XYL\ !$97,108,140 #binding_site substrate (Tyr, Tyr, Arg) #status !8experimental\ !$106,200 #active_site Glu #status experimental SUMMARY #length 213 #molecular-weight 23359 #checksum 2434 SEQUENCE /// ENTRY S48126 #type complete TITLE endo-1,4-beta-xylanase (EC 3.2.1.8) S precursor - Bacillus sp. (strain YA-14) ALTERNATE_NAMES xylanase S ORGANISM #formal_name Bacillus sp. #variety strain YA-14 DATE 14-Jul-1995 #sequence_revision 22-Nov-1996 #text_change 18-Jun-1999 ACCESSIONS S48126 REFERENCE S48126 !$#authors Ju-Hyun, Y.; Park, Y.S.; Yum, D.Y.; Kim, J.M.; Kong, I.S.; !1Bai, D.H. !$#journal J. Microbiol. Biotechnol. (1993) 3:139-145 !$#title Nucleotide sequence and analysis of a xylanase gene (xynS) !1from alkali-tolerant Bacillus sp. YA-14 and comparison with !1other xylanases. !$#accession S48126 !'##molecule_type DNA !'##residues 1-213 ##label JUH !'##cross-references EMBL:X59058; NID:g458800; PIDN:CAA41783.1; !1PID:g458801 !'##experimental_source strain YA-14 GENETICS !$#gene xynS FUNCTION !$#description catalyzes the hydrolysis of 1,4-beta-xylosidic bonds in !1xylans !$#pathway xylan degradation CLASSIFICATION #superfamily endo-1,4-beta-xylanase; endo-1,4-beta-xylanase !1homology KEYWORDS extracellular protein; glycosidase; hydrolase; !1polysaccharide degradation FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-213 #product endo-1,4-beta-xylanase S #status predicted !8#label MAT\ !$31-213 #domain endo-1,4-beta-xylanase homology #label XYL\ !$106,200 #active_site Glu #status predicted SUMMARY #length 213 #molecular-weight 23341 #checksum 2452 SEQUENCE /// ENTRY JS0591 #type complete TITLE endo-1,4-beta-xylanase (EC 3.2.1.8) C precursor - Streptomyces lividans ALTERNATE_NAMES xylanase C ORGANISM #formal_name Streptomyces lividans DATE 14-Jul-1994 #sequence_revision 22-Nov-1996 #text_change 18-Jun-1999 ACCESSIONS JS0591; PS0240 REFERENCE JS0589 !$#authors Shareck, F.; Roy, C.; Yaguchi, M.; Morosoli, R.; Kluepfel, !1D. !$#journal Gene (1991) 107:75-82 !$#title Sequences of three genes specifying xylanases in !1Streptomyees lividans. !$#cross-references MUID:92077439; PMID:1743521 !$#accession JS0591 !'##molecule_type DNA !'##residues 1-240 ##label SHA !'##cross-references GB:M64553; NID:g153530; PIDN:AAA26836.1; !1PID:g153531 !$#accession PS0240 !'##molecule_type protein !'##residues 50-80 ##label SH2 GENETICS !$#gene xlnC FUNCTION !$#description catalyzes the hydrolysis of 1,4-beta-xylosidic bonds in !1xylans !$#pathway xylan degradation CLASSIFICATION #superfamily endo-1,4-beta-xylanase; endo-1,4-beta-xylanase !1homology KEYWORDS extracellular protein; glycosidase; hydrolase; !1polysaccharide degradation FEATURE !$1-49 #domain signal sequence #status predicted #label SIG\ !$50-240 #product endo-1,4-beta-xylanase C #status !8experimental #label MAT\ !$62-239 #domain endo-1,4-beta-xylanase homology #label XYL\ !$134,226 #active_site Glu #status predicted SUMMARY #length 240 #molecular-weight 25673 #checksum 9152 SEQUENCE /// ENTRY S47512 #type complete TITLE endo-1,4-beta-xylanase (EC 3.2.1.8) precursor - Streptomyces sp. ALTERNATE_NAMES xylanase ORGANISM #formal_name Streptomyces sp. DATE 13-Jan-1995 #sequence_revision 22-Nov-1996 #text_change 18-Jun-1999 ACCESSIONS S47512 REFERENCE S47512 !$#authors Mazy-Servais, C.; Moreau, A.; Gerard, C.; Dusart, J. !$#submission submitted to the EMBL Data Library, August 1994 !$#description Cloning and sequencing of a xylanase-encoding gene from !1Streptomyces sp. EC3. !$#accession S47512 !'##molecule_type DNA !'##residues 1-240 ##label MAZ !'##cross-references EMBL:X81045; NID:g531767; PIDN:CAA56935.1; !1PID:g531768 !'##experimental_source strain EC3 FUNCTION !$#description catalyzes the hydrolysis of 1,4-beta-xylosidic bonds in !1xylans !$#pathway xylan degradation CLASSIFICATION #superfamily endo-1,4-beta-xylanase; endo-1,4-beta-xylanase !1homology KEYWORDS extracellular protein; glycosidase; hydrolase; !1polysaccharide degradation FEATURE !$1-47 #domain signal sequence #status predicted #label SIG\ !$48-240 #product endo-1,4-beta-xylanase #status predicted !8#label MAT\ !$62-239 #domain endo-1,4-beta-xylanase homology #label XYL\ !$135,226 #active_site Glu #status predicted SUMMARY #length 240 #molecular-weight 25949 #checksum 1139 SEQUENCE /// ENTRY S57477 #type complete TITLE endo-1,4-beta-xylanase (EC 3.2.1.8) 1 precursor - Emericella nidulans ALTERNATE_NAMES xylanase 1 ORGANISM #formal_name Emericella nidulans, Aspergillus nidulans DATE 10-Oct-1995 #sequence_revision 22-Nov-1996 #text_change 23-Mar-2001 ACCESSIONS S57477 REFERENCE S57469 !$#authors Perez-Gonzalez, J.A. !$#submission submitted to the EMBL Data Library, June 1995 !$#description Expression in Saccharomyces cerevisiae of two xylanase !1encoding genes from Aspergillus nidulans. !$#accession S57477 !'##molecule_type DNA !'##residues 1-225 ##label PER !'##cross-references EMBL:Z49892; NID:g870832; PIDN:CAA90073.1; !1PID:g870833 GENETICS !$#introns 93/2 FUNCTION !$#description catalyzes the hydrolysis of 1,4-beta-xylosidic bonds in !1xylans !$#pathway xylan degradation CLASSIFICATION #superfamily endo-1,4-beta-xylanase; endo-1,4-beta-xylanase !1homology KEYWORDS glycosidase; hydrolase; polysaccharide degradation FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-225 #product endo-1,4-beta-xylanase 1 #status predicted !8#label MAT\ !$48-225 #domain endo-1,4-beta-xylanase homology #label XYL\ !$121,212 #active_site Glu #status predicted SUMMARY #length 225 #molecular-weight 24070 #checksum 1842 SEQUENCE /// ENTRY S57469 #type complete TITLE endo-1,4-beta-xylanase (EC 3.2.1.8) 2 precursor - Emericella nidulans ALTERNATE_NAMES xylanase 2 ORGANISM #formal_name Emericella nidulans, Aspergillus nidulans DATE 10-Oct-1995 #sequence_revision 22-Nov-1996 #text_change 08-May-1998 ACCESSIONS S57469 REFERENCE S57469 !$#authors Perez-Gonzalez, J.A. !$#submission submitted to the EMBL Data Library, June 1995 !$#description Expression in Saccharomyces cerevisiae of two xylanase !1encoding genes from Aspergillus nidulans. !$#accession S57469 !'##molecule_type DNA !'##residues 1-221 ##label PER !'##cross-references EMBL:Z49893; NID:g870834; PID:g870835 GENETICS !$#introns 89/3 FUNCTION !$#description catalyzes the hydrolysis of 1,4-beta-xylosidic bonds in !1xylans !$#pathway xylan degradation CLASSIFICATION #superfamily endo-1,4-beta-xylanase; endo-1,4-beta-xylanase !1homology KEYWORDS glycosidase; hydrolase; polysaccharide degradation FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$19-221 #product endo-1,4-beta-xylanase 1 #status predicted !8#label MAT\ !$44-221 #domain endo-1,4-beta-xylanase homology #label XYL\ !$117,208 #active_site Glu #status predicted SUMMARY #length 221 #molecular-weight 23517 #checksum 8081 SEQUENCE /// ENTRY A44597 #type complete TITLE endo-1,4-beta-xylanase (EC 3.2.1.8) A - bracket fungus (Schizophyllum commune) ALTERNATE_NAMES xylanase A ORGANISM #formal_name Schizophyllum commune DATE 27-Jun-1994 #sequence_revision 22-Nov-1996 #text_change 06-Dec-1996 ACCESSIONS A44597; S41411; A05147; S38973 REFERENCE A44593 !$#authors Yaguchi, M. !$#submission submitted to the Protein Sequence Database, March 1994 !$#accession A44597 !'##molecule_type protein !'##residues 1-197 ##label YAG !'##experimental_source strain Delmar ATCC 38548 REFERENCE S41411 !$#authors Bray, M.R.; Clarke, A.J. !$#journal Eur. J. Biochem. (1994) 219:821-827 !$#title Identification of a glutamate residue at the active site of !1xylanase A from Schizophyllum commune. !$#cross-references MUID:94155888; PMID:7906649 !$#accession S41411 !'##status preliminary !'##molecule_type protein !'##residues 83-123 ##label BRA REFERENCE A05147 !$#authors Paice, M.G.; Jurasek, L.; Carpenter, M.R.; Smillie, L.B. !$#journal Appl. Environ. Microbiol. (1978) 36:802-808 !$#cross-references MUID:79102289; PMID:32833 !$#accession A05147 !'##molecule_type protein !'##residues 1-27 ##label PAI REFERENCE S38973 !$#authors Oku, T.; Roy, C.; Watson, D.C.; Wakarchuk, W.; Campbell, R.; !1Yaguchi, M.; Jurasek, L.; Paice, M.G. !$#journal FEBS Lett. (1993) 334:296-300 !$#title Amino acid sequence and thermostability of xylanase A from !1Schizophyllum commune. !$#cross-references MUID:94063044; PMID:8243636 !$#accession S38973 !'##molecule_type protein !'##residues 1-197 ##label OKU !'##experimental_source ATCC 38548 FUNCTION !$#description catalyzes the hydrolysis of 1,4-beta-xylosidic bonds in !1xylans !$#pathway xylan degradation CLASSIFICATION #superfamily endo-1,4-beta-xylanase; endo-1,4-beta-xylanase !1homology KEYWORDS extracellular protein; glycosidase; hydrolase; !1polysaccharide degradation FEATURE !$12-197 #domain endo-1,4-beta-xylanase homology #label XYL\ !$87,184 #active_site Glu #status predicted\ !$111-160 #disulfide_bonds #status experimental SUMMARY #length 197 #molecular-weight 20978 #checksum 9655 SEQUENCE /// ENTRY A44593 #type complete TITLE endo-1,4-beta-xylanase (EC 3.2.1.8) [validated] - fungus (Trichoderma harzianum) (strain E58) ALTERNATE_NAMES xylanase ORGANISM #formal_name Trichoderma harzianum DATE 27-Jun-1994 #sequence_revision 22-Nov-1996 #text_change 15-Sep-2000 ACCESSIONS A44593 REFERENCE A44593 !$#authors Yaguchi, M. !$#submission submitted to the Protein Sequence Database, March 1994 !$#accession A44593 !'##molecule_type protein !'##residues 1-190 ##label YAG !'##experimental_source strain E58 REFERENCE A52868 !$#authors Campbell, R.L.; Rose, D.R. !$#submission submitted to the Brookhaven Protein Data Bank, June 1994 !$#cross-references PDB:1XND !$#contents annotation; X-ray crystallography, 1.8 angstroms, residues !11-46,'A'48-190 FUNCTION !$#description catalyzes the hydrolysis of 1,4-beta-xylosidic bonds in !1xylans !$#pathway xylan degradation CLASSIFICATION #superfamily endo-1,4-beta-xylanase; endo-1,4-beta-xylanase !1homology KEYWORDS glycosidase; hydrolase; polysaccharide degradation FEATURE !$12-190 #domain endo-1,4-beta-xylanase homology #label XYL\ !$86,177 #active_site Glu #status experimental SUMMARY #length 190 #molecular-weight 20689 #checksum 2192 SEQUENCE /// ENTRY A44595 #type complete TITLE endo-1,4-beta-xylanase (EC 3.2.1.8) IIB (proteinase-sensitive) - fungus (Trichoderma viride) ALTERNATE_NAMES xylanase IIB ORGANISM #formal_name Trichoderma viride DATE 27-Jun-1994 #sequence_revision 22-Nov-1996 #text_change 13-Mar-1998 ACCESSIONS A44595 REFERENCE A44593 !$#authors Yaguchi, M. !$#submission submitted to the Protein Sequence Database, March 1994 !$#accession A44595 !'##status preliminary !'##molecule_type protein !'##residues 1-190 ##label YAG FUNCTION !$#description catalyzes the hydrolysis of 1,4-beta-xylosidic bonds in !1xylans !$#pathway xylan degradation CLASSIFICATION #superfamily endo-1,4-beta-xylanase; endo-1,4-beta-xylanase !1homology KEYWORDS glycosidase; hydrolase; polysaccharide degradation FEATURE !$12-190 #domain endo-1,4-beta-xylanase homology #label XYL\ !$86,177 #active_site Glu #status predicted\ !$126-127 #cleavage_site Pro-Ser (unidentified proteinase) !8#status predicted\ !$129-130 #cleavage_site Glu-Gly (unidentified proteinase) !8#status predicted SUMMARY #length 190 #molecular-weight 20756 #checksum 2711 SEQUENCE /// ENTRY A44594 #type complete TITLE endo-1,4-beta-xylanase (EC 3.2.1.8) IIA - fungus (Trichoderma viride) ALTERNATE_NAMES xylanase IIA ORGANISM #formal_name Trichoderma viride DATE 27-Jun-1994 #sequence_revision 22-Nov-1996 #text_change 07-Nov-1997 ACCESSIONS A44594 REFERENCE A44593 !$#authors Yaguchi, M. !$#submission submitted to the Protein Sequence Database, March 1994 !$#accession A44594 !'##molecule_type protein !'##residues 1-190 ##label YAG FUNCTION !$#description catalyzes the hydrolysis of 1,4-beta-xylosidic bonds in !1xylans !$#pathway xylan degradation CLASSIFICATION #superfamily endo-1,4-beta-xylanase; endo-1,4-beta-xylanase !1homology KEYWORDS glycosidase; hydrolase; polysaccharide degradation FEATURE !$12-190 #domain endo-1,4-beta-xylanase homology #label XYL\ !$77,88 #binding_site substrate (Tyr) #status predicted\ !$86,177 #active_site Glu #status predicted SUMMARY #length 190 #molecular-weight 20773 #checksum 3109 SEQUENCE /// ENTRY S48229 #type complete TITLE endo-1,4-beta-xylanase (EC 3.2.1.8) 1A precursor - Aspergillus awamori ALTERNATE_NAMES xylanase 1A ORGANISM #formal_name Aspergillus awamori DATE 15-Jul-1995 #sequence_revision 22-Nov-1996 #text_change 18-Jun-1999 ACCESSIONS S48229; S43015 REFERENCE S48229 !$#authors Hessing, J.G.M.; van Rotterdam, C.; Verbakel, J.M.A.; Roza, !1M.; Maat, J.; van Gorcom, R.F.M.; van den Hondel, C.A.M.J.J. !$#journal Curr. Genet. (1994) 26:228-232 !$#title Isolation and characterization of a 1,4-beta-endoxylanase !1gene of A. awamori. !$#cross-references MUID:95163119; PMID:7859305 !$#accession S48229 !'##molecule_type DNA !'##residues 1-211 ##label HES !'##cross-references EMBL:X78115; NID:g460340; PIDN:CAA55005.1; !1PID:g460341 !'##experimental_source ATCC11358 GENETICS !$#gene ex1A !$#introns 77/2 FUNCTION !$#description catalyzes the hydrolysis of 1,4-beta-xylosidic bonds in !1xylans !$#pathway xylan degradation CLASSIFICATION #superfamily endo-1,4-beta-xylanase; endo-1,4-beta-xylanase !1homology KEYWORDS glycosidase; hydrolase; polysaccharide degradation FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-211 #product endo-1,4-beta-xylanase 1A #status predicted !8#label MAT\ !$30-210 #domain endo-1,4-beta-xylanase homology #label XYL\ !$106,197 #active_site Glu #status predicted SUMMARY #length 211 #molecular-weight 22627 #checksum 4375 SEQUENCE /// ENTRY JC1198 #type complete TITLE endo-1,4-beta-xylanase (EC 3.2.1.8) C precursor - Aspergillus niger ALTERNATE_NAMES xylanase C ORGANISM #formal_name Aspergillus niger DATE 05-Mar-1993 #sequence_revision 22-Nov-1996 #text_change 26-Feb-1999 ACCESSIONS JC1198; PS0436 REFERENCE JC1198 !$#authors Ito, K.; Iwashita, K.; Iwano, K. !$#journal Biosci. Biotechnol. Biochem. (1992) 56:1338-1340 !$#title Cloning and sequencing of the xynC gene encoding acid !1xylanase of Aspergillus kawachii. !$#cross-references MUID:93005082; PMID:1368843 !$#accession JC1198 !'##molecule_type DNA !'##residues 1-211 ##label ITO !$#accession PS0436 !'##molecule_type protein !'##residues 28-34 ##label ITO1 !'##note the source is designated as Aspergillus kawachii GENETICS !$#gene xynC !$#introns 77/2 FUNCTION !$#description catalyzes the hydrolysis of 1,4-beta-xylosidic bonds in !1xylans !$#pathway xylan degradation CLASSIFICATION #superfamily endo-1,4-beta-xylanase; endo-1,4-beta-xylanase !1homology KEYWORDS glycosidase; hydrolase; polysaccharide degradation FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-211 #product endo-1,4-beta-xylanase C #status !8experimental #label MAT\ !$30-210 #domain endo-1,4-beta-xylanase homology #label XYL\ !$106,197 #active_site Glu #status predicted SUMMARY #length 211 #molecular-weight 22560 #checksum 4107 SEQUENCE /// ENTRY S48865 #type complete TITLE endo-1,4-beta-xylanase (EC 3.2.1.8) 2 precursor - rumen fungus (Neocallimastix frontalis) ALTERNATE_NAMES xylanase 2 ORGANISM #formal_name Neocallimastix frontalis DATE 13-Jan-1995 #sequence_revision 22-Nov-1996 #text_change 18-Jun-1999 ACCESSIONS S48865 REFERENCE S48865 !$#authors Durand, R.; Fevre, M. !$#submission submitted to the EMBL Data Library, November 1994 !$#description The XYN2 gene of the anaerobic fungus Neocallimastix !1frontalis. !$#accession S48865 !'##molecule_type mRNA !'##residues 1-266 ##label DUR !'##cross-references EMBL:X82439; NID:g565625; PIDN:CAA57820.1; !1PID:g565626 GENETICS !$#gene XYN2 FUNCTION !$#description catalyzes the hydrolysis of 1,4-beta-xylosidic bonds in !1xylans !$#pathway xylan degradation CLASSIFICATION #superfamily endo-1,4-beta-xylanase; endo-1,4-beta-xylanase !1homology KEYWORDS glycosidase; hydrolase; polysaccharide degradation FEATURE !$1-54 #domain signal sequence #status predicted #label SIG\ !$55-266 #product endo-1,4-beta-xylanase 2 #status predicted !8#label MAT\ !$67-256 #domain endo-1,4-beta-xylanase homology #label XYL\ !$150,243 #active_site Glu #status predicted SUMMARY #length 266 #molecular-weight 29689 #checksum 230 SEQUENCE /// ENTRY S59633 #type complete TITLE endo-1,4-beta-xylanase (EC 3.2.1.8) E precursor - Pseudomonas fluorescens ALTERNATE_NAMES xylanase E ORGANISM #formal_name Pseudomonas fluorescens DATE 15-Feb-1996 #sequence_revision 22-Nov-1996 #text_change 18-Jun-1999 ACCESSIONS S59633; S52748 REFERENCE S59631 !$#authors Millward-Sadler, S.J.; Davidson, K.; Hazlewood, G.P.; Black, !1G.W.; Gilbert, H.J.; Clarke, J.H. !$#journal Biochem. J. (1995) 312:39-48 !$#title Novel cellulose-binding domains, NodB homologues and !1conserved modular architecture in xylanases from the aerobic !1soil bacteria Pseudomonas fluorescens subsp. cellulosa and !1Cellvibrio mixtus. !$#cross-references MUID:96077124; PMID:7492333 !$#accession S59633 !'##molecule_type DNA !'##residues 1-661 ##label MIL !'##cross-references EMBL:Z48927; NID:g758224; PIDN:CAA88763.1; !1PID:g758225 GENETICS !$#gene xynE FUNCTION !$#description catalyzes the hydrolysis of 1,4-beta-xylosidic bonds in !1xylans !$#pathway xylan degradation CLASSIFICATION #superfamily Pseudomonas endo-1,4-beta-xylanase E; endo-1, !14-beta-xylanase homology; glycosidase GWGW domain homology; !1nodB homology KEYWORDS extracellular protein; glycosidase; hydrolase; !1polysaccharide degradation FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-661 #product endo-1,4-beta-xylanase E #status predicted !8#label MAT\ !$40-226 #domain endo-1,4-beta-xylanase homology #label XYL\ !$403-549 #domain nodB homology #label NODB\ !$616-653 #domain glycosidase GWGW domain homology #label GWG\ !$116,213 #active_site Glu #status predicted SUMMARY #length 661 #molecular-weight 69193 #checksum 809 SEQUENCE /// ENTRY S59631 #type complete TITLE endo-1,4-beta-xylanase (EC 3.2.1.8) A precursor - Cellvibrio mixtus ALTERNATE_NAMES xylanase A ORGANISM #formal_name Cellvibrio mixtus DATE 19-Mar-1997 #sequence_revision 11-Apr-1997 #text_change 18-Jun-1999 ACCESSIONS S59631; S52741 REFERENCE S59631 !$#authors Millward-Sadler, S.J.; Davidson, K.; Hazlewood, G.P.; Black, !1G.W.; Gilbert, H.J.; Clarke, J.H. !$#journal Biochem. J. (1995) 312:39-48 !$#title Novel cellulose-binding domains, NodB homologues and !1conserved modular architecture in xylanases from the aerobic !1soil bacteria Pseudomonas fluorescens subsp. cellulosa and !1Cellvibrio mixtus. !$#cross-references MUID:96077124; PMID:7492333 !$#accession S59631 !'##molecule_type DNA !'##residues 1-656 ##label MIL !'##cross-references EMBL:Z48925; NID:g757806; PIDN:CAA88761.1; !1PID:g757807 GENETICS !$#gene xynA FUNCTION !$#description catalyzes the hydrolysis of 1,4-beta-xylosidic bonds in !1xylans !$#pathway xylan degradation CLASSIFICATION #superfamily Pseudomonas endo-1,4-beta-xylanase E; endo-1, !14-beta-xylanase homology; glycosidase GWGW domain homology; !1nodB homology KEYWORDS extracellular protein; glycosidase; hydrolase; !1polysaccharide degradation FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-656 #product endo-1,4-beta-xylanase A #status predicted !8#label MAT\ !$40-225 #domain endo-1,4-beta-xylanase homology #label XYL\ !$398-544 #domain nodB homology #label NODB\ !$611-648 #domain glycosidase GWGW domain homology #label GWG\ !$115,212 #active_site Glu #status predicted SUMMARY #length 656 #molecular-weight 68668 #checksum 320 SEQUENCE /// ENTRY I40712 #type complete TITLE endo-1,4-beta-xylanase (EC 3.2.1.8) D precursor - Cellulomonas fimi ALTERNATE_NAMES xylanase D ORGANISM #formal_name Cellulomonas fimi DATE 16-Aug-1996 #sequence_revision 22-Nov-1996 #text_change 18-Jun-1999 ACCESSIONS I40712 REFERENCE I40712 !$#authors Millward-Sadler, S.J.; Poole, D.M.; Henrissat, B.; !1Hazlewood, G.P.; Clarke, J.H.; Gilbert, H.J. !$#journal Mol. Microbiol. (1994) 11:375-382 !$#title Evidence for a general role for high-affinity non-catalytic !1cellulose binding domains in microbial plant cell wall !1hydrolases. !$#cross-references MUID:94224155; PMID:8170399 !$#accession I40712 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-644 ##label RES !'##cross-references EMBL:X76729; NID:g558176; PIDN:CAA54145.1; !1PID:g558177 GENETICS !$#gene xynD FUNCTION !$#description catalyzes the hydrolysis of 1,4-beta-xylosidic bonds in !1xylans !$#pathway xylan degradation CLASSIFICATION #superfamily Cellulomonas endo-1,4-beta-xylanase D; endo-1, !14-beta-xylanase homology; nodB homology KEYWORDS extracellular protein; glycosidase; hydrolase; !1polysaccharide degradation FEATURE !$1-35 #domain signal sequence #status predicted #label SIG\ !$36-644 #product endo-1,4-beta-xylanase D #status predicted !8#label MAT\ !$54-229 #domain endo-1,4-beta-xylanase homology #label XYL\ !$361-508 #domain nodB homology #label NODB\ !$126,216 #active_site Glu #status predicted SUMMARY #length 644 #molecular-weight 66581 #checksum 711 SEQUENCE /// ENTRY JS0590 #type complete TITLE endo-1,4-beta-xylanase (EC 3.2.1.8) B precursor - Streptomyces lividans ALTERNATE_NAMES xylanase B ORGANISM #formal_name Streptomyces lividans DATE 10-Mar-1994 #sequence_revision 22-Nov-1996 #text_change 26-Feb-1999 ACCESSIONS JS0590; PS0239 REFERENCE JS0589 !$#authors Shareck, F.; Roy, C.; Yaguchi, M.; Morosoli, R.; Kluepfel, !1D. !$#journal Gene (1991) 107:75-82 !$#title Sequences of three genes specifying xylanases in !1Streptomyees lividans. !$#cross-references MUID:92077439; PMID:1743521 !$#accession JS0590 !'##molecule_type DNA !'##residues 1-333 ##label SHA !'##cross-references GB:M64552 !$#accession PS0239 !'##molecule_type protein !'##residues 41-71 ##label SH2 GENETICS !$#gene xlnB FUNCTION !$#description catalyzes the hydrolysis of 1,4-beta-xylosidic bonds in !1xylans !$#pathway xylan degradation CLASSIFICATION #superfamily Clostridium endo-1,4-beta-xylanase B; endo-1, !14-beta-xylanase homology KEYWORDS extracellular protein; glycosidase; hydrolase; !1polysaccharide degradation FEATURE !$1-40 #domain signal sequence #status predicted #label SIG\ !$41-333 #product endo-1,4-beta-xylanase B #status !8experimental #label MAT\ !$54-230 #domain endo-1,4-beta-xylanase homology #label XYL\ !$127,217 #active_site Glu #status predicted SUMMARY #length 333 #molecular-weight 35581 #checksum 8647 SEQUENCE /// ENTRY S51779 #type complete TITLE endo-1,4-beta-xylanase (EC 3.2.1.8) Y precursor - Bacillus sp. (strain YA-335) ALTERNATE_NAMES xylanase Y ORGANISM #formal_name Bacillus sp. #variety strain YA-335 DATE 15-Jul-1995 #sequence_revision 22-Nov-1996 #text_change 16-Jun-2000 ACCESSIONS S51779; S48127 REFERENCE S51779 !$#authors Hyun Ju, Y. !$#submission submitted to the EMBL Data Library, December 1990 !$#accession S51779 !'##molecule_type DNA !'##residues 1-354 ##label HYU !'##cross-references EMBL:X59059; NID:g487722; PIDN:CAA41784.1; !1PID:g1334251 !'##experimental_source strain YA-335 REFERENCE S48126 !$#authors Ju-Hyun, Y.; Park, Y.S.; Yum, D.Y.; Kim, J.M.; Kong, I.S.; !1Bai, D.H. !$#journal J. Microbiol. Biotechnol. (1993) 3:139-145 !$#title Nucleotide sequence and analysis of a xylanase gene (xynS) !1from alkali-tolerant Bacillus sp. YA-14 and comparison with !1other xylanases. !$#accession S48127 !'##molecule_type DNA !'##residues 1-17,19-229 ##label JUH !'##cross-references EMBL:X59059 !'##experimental_source strain YA-335 !'##note the authors translated the initiation codon TTG for residue 1 !1as Leu GENETICS !$#gene xynY !$#start_codon TTG FUNCTION !$#description catalyzes the hydrolysis of 1,4-beta-xylosidic bonds in !1xylans !$#pathway xylan degradation CLASSIFICATION #superfamily Clostridium endo-1,4-beta-xylanase B; endo-1, !14-beta-xylanase homology KEYWORDS extracellular protein; glycosidase; hydrolase; !1polysaccharide degradation FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-354 #product endo-1,4-beta-xylanase Y #status predicted !8#label MAT\ !$39-223 #domain endo-1,4-beta-xylanase homology #label XYL\ !$120,210 #active_site Glu #status predicted SUMMARY #length 354 #molecular-weight 38935 #checksum 5405 SEQUENCE /// ENTRY JQ1935 #type complete TITLE endo-1,4-beta-xylanase (EC 3.2.1.8) A precursor - Clostridium stercorarium ALTERNATE_NAMES xylanase A ORGANISM #formal_name Clostridium stercorarium DATE 30-Sep-1993 #sequence_revision 22-Nov-1996 #text_change 26-Feb-1999 ACCESSIONS JQ1935; PQ0531 REFERENCE JQ1935 !$#authors Sakka, K.; Kojima, Y.; Kondo, T.; Karita, S.I.; Ohmiya, K.; !1Shimada, K. !$#journal Biosci. Biotechnol. Biochem. (1993) 57:273-277 !$#title Nucleotide sequence of the Clostridium stercorarium xynA !1gene encoding xylanase A: identification of catalytic and !1cellulose binding domains. !$#cross-references MUID:93214115; PMID:7763496 !$#accession JQ1935 !'##molecule_type DNA !'##residues 1-511 ##label SAK !$#accession PQ0531 !'##molecule_type protein !'##residues 31-40 ##label SA2 !'##note the authors translated the codon AAC for residue 415 as GLy FUNCTION !$#description catalyzes the hydrolysis of 1,4-beta-xylosidic bonds in !1xylans !$#pathway xylan degradation CLASSIFICATION #superfamily Clostridium endo-1,4-beta-xylanase A; !1Clostridium xylanase A repeat homology; endo-1, !14-beta-xylanase homology KEYWORDS extracellular protein; glycosidase; hydrolase; !1polysaccharide degradation FEATURE !$1-30 #domain signal sequence #status predicted #label SIG\ !$31-511 #product endo-1,4-beta-xylanase A #status predicted !8#label MAT\ !$44-228 #domain endo-1,4-beta-xylanase homology #label XYL\ !$236-244 #region linker\ !$277-368 #domain Clostridium xylanase A repeat homology #label !8CXA1\ !$413-506 #domain Clostridium xylanase A repeat homology #label !8CXA2\ !$124,215 #active_site Glu #status predicted SUMMARY #length 511 #molecular-weight 56576 #checksum 320 SEQUENCE /// ENTRY S20907 #type complete TITLE endo-1,4-beta-xylanase (EC 3.2.1.8) precursor, bifunctional - Ruminococcus flavefaciens CONTAINS endo-1,4-beta-xylanase (EC 3.2.1.8) ORGANISM #formal_name Ruminococcus flavefaciens DATE 22-Nov-1993 #sequence_revision 22-Nov-1996 #text_change 18-Jun-1999 ACCESSIONS S20907; S18043 REFERENCE S20907 !$#authors Zhang, J.X.; Flint, H.J. !$#journal Mol. Microbiol. (1992) 6:1013-1023 !$#title A bifunctional xylanase encoded by the xynA gene of the !1rumen cellulolytic bacterium Ruminococcus flavefaciens 17 !1comprises two dissimilar domains linked by an asparagine/ !1glutamine-rich sequence. !$#cross-references MUID:92261318; PMID:1584021 !$#accession S20907 !'##molecule_type DNA !'##residues 1-954 ##label ZHA !'##cross-references EMBL:Z11127; NID:g46161; PIDN:CAA77476.1; !1PID:g581505 !'##experimental_source strain 17 GENETICS !$#gene xynA !$#start_codon TTG FUNCTION !$#description catalyzes the hydrolysis of 1,4-beta-xylosidic bonds in !1xylans !$#pathway xylan degradation CLASSIFICATION #superfamily Ruminococcus bifunctional endo-1, !14-beta-xylanase; endo-1,4-beta-xylanase homology; !1Streptomyces endo-1,4-beta-xylanase A homology KEYWORDS extracellular protein; glycosidase; hydrolase; !1multifunctional enzyme; polysaccharide degradation; tandem !1repeat FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-954 #product bifunctional endo-1,4-beta-xylanase #status !8predicted #label MAT\ !$28-248 #domain catalytic domain A #status predicted #label !8CDA\ !$40-236 #domain endo-1,4-beta-xylanase homology #label XYL\ !$249-622 #domain linker region B #status predicted #label LRB\ !$623-954 #domain catalytic domain C #status predicted #label !8CDC\ !$655-953 #domain Streptomyces endo-1,4-beta-xylanase A !8homology #label SXY\ !$122,223 #active_site Glu #status predicted SUMMARY #length 954 #molecular-weight 111362 #checksum 2784 SEQUENCE /// ENTRY S18750 #type complete TITLE chitinase (EC 3.2.1.14) precursor - western balsam poplar x cottonwood ORGANISM #formal_name Populus trichocarpa x Populus deltoides #common_name western balsam poplar x cottonwood DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S18750; S17755 REFERENCE S18750 !$#authors Davis, J.M. !$#submission submitted to the EMBL Data Library, May 1991 !$#accession S18750 !'##molecule_type DNA !'##residues 1-336 ##label DAV !'##cross-references EMBL:X59995 REFERENCE S17755 !$#authors Davis, J.M.; Clarke, H.R.G.; Bradshaw Jr., H.D.; Gordon, !1M.P. !$#journal Plant Mol. Biol. (1991) 17:631-639 !$#title Populus chitinase genes: structure, organization, and !1similarity of translated sequences to herbaceous plant !1chitinases. !$#cross-references MUID:92003678; PMID:1912489 !$#accession S17755 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-103 ##label DAV2 !'##cross-references EMBL:X59995 GENETICS !$#introns 153/1; 203/2 CLASSIFICATION #superfamily lectin-related plant chitinase; hevein !1chitin-binding domain homology; plant chitinase homology KEYWORDS endoplasmic reticulum; glycosidase; hydrolase; !1polysaccharide degradation FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-336 #product chitinase #status predicted #label MAT\ !$22-63 #domain hevein chitin-binding domain homology #label !8HCB\ !$63-82 #region spacer\ !$83-336 #domain catalytic #status predicted #label CAT\ !$88-326 #domain plant chitinase homology #label PCH SUMMARY #length 336 #molecular-weight 35984 #checksum 7563 SEQUENCE /// ENTRY S37344 #type complete TITLE chitinase (EC 3.2.1.14) chi9 precursor - tomato ORGANISM #formal_name Lycopersicon esculentum #common_name tomato DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S37344; S38838; S25637 REFERENCE S37341 !$#authors Danhash, N.; Wagemakers, C.A.M.; van Kan, J.A.L.; de Wit, !1P.J.G.M. !$#journal Plant Mol. Biol. (1993) 22:1017-1029 !$#title Molecular characterization of four chitinase cDNAs obtained !1from Cladosporium fulvum-infected tomato. !$#cross-references MUID:94003061; PMID:8400122 !$#accession S37344 !'##molecule_type mRNA !'##residues 1-322 ##label DAN1 !'##cross-references EMBL:Z15140; NID:g19190; PIDN:CAA78845.1; !1PID:g19191 !$#accession S38838 !'##molecule_type protein !'##residues 23-42;202-216;224-236;247-258 ##label DAN2 CLASSIFICATION #superfamily lectin-related plant chitinase; hevein !1chitin-binding domain homology; plant chitinase homology KEYWORDS glycosidase; hydrolase; polysaccharide degradation FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-322 #product chitinase chi9 #status experimental #label !8MAT\ !$23-65 #domain hevein chitin-binding domain homology #label !8HCB\ !$75-314 #domain plant chitinase homology #label PCH SUMMARY #length 322 #molecular-weight 34345 #checksum 8968 SEQUENCE /// ENTRY S05426 #type complete TITLE chitinase (EC 3.2.1.14) precursor - potato ORGANISM #formal_name Solanum tuberosum #common_name potato DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S05426; S00877 REFERENCE S05426 !$#authors Gaynor, J.J.; Unkenholz, K.M. !$#journal Nucleic Acids Res. (1989) 17:5855-5856 !$#title Sequence analysis of a genomic clone encoding an !1endochitinase from Solanum tuberosum. !$#cross-references MUID:89345190; PMID:2762165 !$#accession S05426 !'##status translation not shown !'##molecule_type DNA !'##residues 1-328 ##label GAY1 !'##cross-references EMBL:X15494; NID:g21426; PIDN:CAA33517.1; !1PID:g21427 REFERENCE S00877 !$#authors Gaynor, J.J. !$#journal Nucleic Acids Res. (1988) 16:5210 !$#title Primary structure of an endochitinase mRNA from Solanum !1tuberosum. !$#cross-references MUID:88262525; PMID:3387233 !$#accession S00877 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-328 ##label GAY2 !'##cross-references EMBL:X07130; NID:g21422; PIDN:CAA30142.1; !1PID:g21423 CLASSIFICATION #superfamily lectin-related plant chitinase; hevein !1chitin-binding domain homology; plant chitinase homology KEYWORDS glycosidase; hydrolase; polysaccharide degradation FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-328 #product chitinase #status predicted #label MAT\ !$27-69 #domain hevein chitin-binding domain homology #label !8HCB\ !$82-320 #domain plant chitinase homology #label PCH SUMMARY #length 328 #molecular-weight 35406 #checksum 6817 SEQUENCE /// ENTRY JQ0965 #type complete TITLE chitinase (EC 3.2.1.14) precursor - kidney bean ORGANISM #formal_name Phaseolus vulgaris #common_name kidney bean DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 15-Oct-1999 ACCESSIONS JQ0965; A25898; A24215; T11784 REFERENCE JQ0965 !$#authors Broglie, K.E.; Biddle, P.; Cressman, R.; Broglie, R. !$#journal Plant Cell (1989) 1:599-607 !$#title Functional analysis of DNA sequences responsible for !1ethylene regulation of a bean chitinase gene in transgenic !1tobacco. !$#cross-references MUID:92393399; PMID:2535512 !$#accession JQ0965 !'##molecule_type DNA !'##residues 1-327 ##label BRO !'##cross-references GB:S43926; NID:g255451; PIDN:AAB23263.1; !1PID:g255452 REFERENCE A25898 !$#authors Broglie, K.E.; Gaynor, J.J.; Broglie, R.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:6820-6824 !$#title Ethylene-regulated gene expression: molecular cloning of the !1genes encoding an endochitinase from Phaseolus vulgaris. !$#cross-references MUID:86313667; PMID:2428042 !$#accession A25898 !'##status preliminary !'##molecule_type mRNA !'##residues 1-7,'M',9-10,'W',12-20,'L',21-58,'PG',61-86,'M',88-166,'T', !1168-318,'L',320-327 ##label BR2 !'##cross-references GB:M13968; NID:g169330; PIDN:AAA33756.1; !1PID:g169331 REFERENCE A24215 !$#authors Lucas, J.; Henschen, A.; Lottspeich, F.; Voegeli, U.; !1Boller, T. !$#journal FEBS Lett. (1985) 193:208-210 !$#title Amino-terminal sequence of ethylene-induced bean leaf !1chitinase reveals similarities to sugar-binding domains of !1wheat germ agglutinin. !$#accession A24215 !'##molecule_type protein !'##residues 27-52,'S',54,'E',56 ##label LUC REFERENCE Z17344 !$#authors Hedrick, S.A.; Bell, J.N.; Boller, T.; Lamb, C.J. !$#journal Plant Physiol. (1988) 86:182-186 !$#title Chitinase cDNA cloning and mRNA induction by fungal !1elicitor, wounding, and infection. !$#accession T11784 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 27-38,'L',40-50 ##label HED !'##cross-references EMBL:M19052; NID:g169332; PID:g169333 GENETICS !$#gene CH5B FUNCTION !$#description catalyzes the hydrolysis of chitin, a beta-1,4-linked !1homopolymer of N-acetyl-D-glucosamine CLASSIFICATION #superfamily lectin-related plant chitinase; hevein !1chitin-binding domain homology; plant chitinase homology KEYWORDS glycosidase; hydrolase; polysaccharide degradation FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-301 #product chitinase #status predicted #label MAT\ !$27-68 #domain hevein chitin-binding domain homology #label !8HCB\ !$78-315 #domain plant chitinase homology #label PCH SUMMARY #length 327 #molecular-weight 35290 #checksum 8662 SEQUENCE /// ENTRY A44039 #type complete TITLE chitinase (EC 3.2.1.14) I, acidic - Japanese yam ORGANISM #formal_name Dioscorea japonica #common_name Japanese yam DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A44039; S22506; A40173 REFERENCE A44039 !$#authors Araki, T.; Funatsu, J.; Kuramoto, M.; Konno, H.; Torikata, !1T. !$#journal J. Biol. Chem. (1992) 267:19944-19947 !$#title The complete amino acid sequence of yam (Dioscorea japonica) !1chitinase. A newly identified acidic class I chitinase. !$#cross-references MUID:93015853; PMID:1400311 !$#accession A44039 !'##status preliminary !'##molecule_type protein !'##residues 1-250 ##label ARA !'##experimental_source aerial tubers !'##note sequence extracted from NCBI backbone (NCBIP:115626) REFERENCE S22506 !$#authors Araki, T.; Funatsu, J.; Kuramoto, M.; Torikata, T. !$#journal Plant Mol. Biol. (1992) 19:351-354 !$#title Amino acid sequence of the N-terminal domain of yam !1(Dioscorea japonica) aerial tuber acidic chitinase. Evidence !1for the presence of a wheat germ agglutinin domain in !1matured acidic chitinase from unstressed tuber. !$#cross-references MUID:92322966; PMID:1623187 !$#accession S22506 !'##molecule_type protein !'##residues 1-53 ##label AR2 CLASSIFICATION #superfamily lectin-related plant chitinase; hevein !1chitin-binding domain homology; plant chitinase homology KEYWORDS glycosidase; hydrolase; polysaccharide degradation FEATURE !$1-37 #domain hevein chitin-binding domain homology #label !8HCB\ !$48-250 #domain plant chitinase homology #label PCH SUMMARY #length 250 #molecular-weight 27909 #checksum 7787 SEQUENCE /// ENTRY JN0858 #type complete TITLE chitinase (EC 3.2.1.14) A precursor - Streptomyces lividans CONTAINS chitinase A1; chitinase A2; chitinase A3 ORGANISM #formal_name Streptomyces lividans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS JN0858; PN0650 REFERENCE JN0858 !$#authors Miyashita, K.; Fujii, T. !$#journal Biosci. Biotechnol. Biochem. (1993) 57:1691-1698 !$#title Nucleotide sequence and analysis of a gene (chiA) for a !1chitinase from Streptomyces lividans 66. !$#cross-references MUID:94080029; PMID:7764265 !$#accession JN0858 !'##molecule_type DNA !'##residues 1-571 ##label MIY !'##cross-references GB:D13775; NID:g471166; PIDN:BAA02918.1; !1PID:g705392 !$#accession PN0650 !'##molecule_type protein !'##residues 37-46;171-188;488-501 ##label MI2 GENETICS !$#gene chiA !$#start_codon GTG CLASSIFICATION #superfamily Streptomyces chitinase chiA KEYWORDS glycosidase; hydrolase; polysaccharide degradation FEATURE !$1-36 #domain signal sequence #status predicted #label SIG\ !$37-571 #product chitinase A1 #status predicted #label CA1\ !$37-487 #product chitinase A2 #status experimental #label !8CA2\ !$171-488 #product chitinase A3 #status experimental #label CA3 SUMMARY #length 571 #molecular-weight 58110 #checksum 590 SEQUENCE /// ENTRY S32039 #type complete TITLE chitinase (EC 3.2.1.14) 1 - Streptomyces olivaceoviridis ORGANISM #formal_name Streptomyces olivaceoviridis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S33848; S32039 REFERENCE S33848 !$#authors Blaak, H.; Schnellmann, J.; Walter, S.; Henrissat, B.; !1Schrempf, H. !$#journal Eur. J. Biochem. (1993) 214:659-669 !$#title Characteristics of an exochitinase from Streptomyces !1olivaceoviridis, its corresponding gene, putative protein !1domains and relationship to other chitinases. !$#cross-references MUID:93307280; PMID:8319677 !$#accession S33848 !'##status preliminary !'##molecule_type DNA !'##residues 1-597 ##label BLA !'##cross-references EMBL:X71080; NID:g49258; PIDN:CAA50398.1; !1PID:g581715 !'##experimental_source ATCC 11238 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily Streptomyces chitinase chiA KEYWORDS glycosidase; hydrolase; polysaccharide degradation SUMMARY #length 597 #molecular-weight 62314 #checksum 3428 SEQUENCE /// ENTRY S31195 #type complete TITLE polygalacturonase (EC 3.2.1.15) - avocado ORGANISM #formal_name Persea americana #common_name avocado DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S31195; S28072 REFERENCE S31195 !$#authors Dopico, B.; Lowe, A.L.; Wilson, I.D.; Merodio, C.; Grierson, !1D. !$#journal Plant Mol. Biol. (1993) 21:437-449 !$#title Cloning and characterization of avocado fruit mRNAs and !1their expression during ripening and low-temperature !1storage. !$#cross-references MUID:93184201; PMID:8095163 !$#accession S31195 !'##molecule_type mRNA !'##residues 1-462 ##label DOP !'##cross-references EMBL:X66426 REFERENCE S28072 !$#authors Dopico, B. !$#submission submitted to the EMBL Data Library, May 1992 !$#accession S28072 !'##molecule_type mRNA !'##residues 1-181,'S',183-462 ##label DO2 !'##cross-references EMBL:X66426; NID:g22630; PIDN:CAA47055.1; !1PID:g22631 CLASSIFICATION #superfamily polygalacturonase KEYWORDS glycosidase; hydrolase; polysaccharide degradation SUMMARY #length 462 #molecular-weight 50316 #checksum 9230 SEQUENCE /// ENTRY LZHU #type complete TITLE lysozyme (EC 3.2.1.17) c precursor [validated] - human ALTERNATE_NAMES muramidase ORGANISM #formal_name Homo sapiens #common_name man DATE 24-Apr-1984 #sequence_revision 08-Feb-1996 #text_change 15-Sep-2000 ACCESSIONS S04938; A31240; JS0063; I52223; JC1075; A93399; A91379; !1A91632; A91378; S32375; S65415; A00849 REFERENCE S04938 !$#authors Peters, C.W.B.; Kruse, U.; Pollwein, R.; Grzeschik, K.H.; !1Sippel, A.E. !$#journal Eur. J. Biochem. (1989) 182:507-516 !$#title The human lysozyme gene. Sequence organization and !1chromosomal localization. !$#cross-references MUID:89325294; PMID:2546758 !$#accession S04938 !'##molecule_type DNA !'##residues 1-148 ##label PET !'##cross-references EMBL:X14008; NID:g34433 !'##note the translation in GenBank entry HSLYSOZY, release 103.0, !1(PID:e74526; PID:g1335210) fails to include the first 18 !1residues of the authors' translation REFERENCE A31240 !$#authors Chung, L.P.; Keshav, S.; Gordon, S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:6227-6231 !$#title Cloning the human lysozyme cDNA: inverted Alu repeat in the !1mRNA and in situ hybridization for macrophages and Paneth !1cells. !$#cross-references MUID:88320415; PMID:3413092 !$#accession A31240 !'##molecule_type mRNA !'##residues 1-148 ##label CHU !'##cross-references GB:J03801; NID:g187243; PIDN:AAA59535.1; !1PID:g307140 REFERENCE JS0063 !$#authors Castanon, M.J.; Spevak, W.; Adolf, G.R.; !1Chlebowicz-Sledziewska, E.; Sledziewski, A. !$#journal Gene (1988) 66:223-234 !$#title Cloning of human lysozyme gene and expression in the yeast !1Saccharomyces cerevisiae. !$#cross-references MUID:89006264; PMID:2971592 !$#accession JS0063 !'##molecule_type mRNA !'##residues 1-148 ##label CAS !'##cross-references GB:M21119; NID:g187245 !'##note the sequence in GenBank entry HUMLSZA, release 103.0, !1(PID:g307141) has the codon ATG for 41-Met rather than the !1published ATC REFERENCE I52223 !$#authors Yoshimura, K.; Toibana, A.; Nakahama, K. !$#journal Biochem. Biophys. Res. Commun. (1988) 150:794-801 !$#title Human lysozyme: sequencing of a cDNA, and expression and !1secretion by Saccharomyces cerevisiae. !$#cross-references MUID:88134189; PMID:2829884 !$#accession I52223 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-148 ##label RES !'##cross-references GB:M19045; NID:g187247; PIDN:AAA59536.1; !1PID:g307142 REFERENCE JC1075 !$#authors Huang, B.R.; Zhao, C.; Lei, X.H.; Cai, L.W. !$#journal Chinese Biochem. J. (1993) 9:269-273 !$#title The cloning, sequencing and analysis of Chinese human !1lysozyme gene cDNA amplified with RT-PCR from human !1placental total RNA. !$#accession JC1075 !'##molecule_type mRNA !'##residues 1-9,'A',11-70,'S',72-110,'A',112-119,'S',121-123,'V', !1125-127,'A',129-135,'D',137-148 ##label HUA !'##experimental_source placenta REFERENCE A93399 !$#authors Canfield, R.E.; Kammerman, S.; Sobel, H.H.; Morgan, F.J. !$#journal Nature New Biol. (1971) 232:16-17 !$#title Primary structure of lysozymes from man and goose. !$#cross-references MUID:71276655; PMID:5284421 !$#accession A93399 !'##molecule_type protein !'##residues 19-117,119-148 ##label CAN !'##experimental_source urine REFERENCE A91379 !$#authors Thomsen, J.; Lund, E.H.; Kristiansen, K.; Brunfeldt, K.; !1Malmquist, J. !$#journal FEBS Lett. (1972) 22:34-36 !$#title A Val-Val sequence found in a human monocytic leukemia !1lysozyme. !$#accession A91379 !'##molecule_type protein !'##residues 19-148 ##label THO !'##experimental_source urine !'##note the lysozymes isolated from human milk and from the urine of !1patients with chronic leukemia are identical REFERENCE A91632 !$#authors Jolles, J.; Jolles, P. !$#journal Helv. Chim. Acta (1971) 54:2668-2675 !$#title Human milk lysozyme: unpublished data concerning the !1establishment of the complete primary structure; comparison !1with lysozymes of various origins. !$#cross-references MUID:72131416; PMID:5168859 !$#accession A91632 !'##molecule_type protein !'##residues 19-117,119-148 ##label JOL !'##experimental_source milk REFERENCE A91378 !$#authors Jolles, J.; Jolles, P. !$#journal FEBS Lett. (1972) 22:31-33 !$#title Comparison between human and bird lysozymes: note concerning !1the previously observed deletion. !$#accession A91378 !'##molecule_type protein !'##residues 19-148 ##label JO2 !'##experimental_source milk REFERENCE S32375 !$#authors Pepys, M.B.; Hawkins, P.N.; Booth, D.R.; Vigushin, D.M.; !1Tennent, G.A.; Soutar, A.K.; Totty, N.; Nguyen, O.; Blake, !1C.C.F.; Terry, C.J.; Feest, T.G.; Zalin, A.M.; Hsuan, J.J. !$#journal Nature (1993) 362:553-557 !$#title Human lysozyme gene mutations cause hereditary systemic !1amyloidosis. !$#cross-references MUID:93218745; PMID:8464497 !$#accession S32375 !'##molecule_type protein !'##residues 19-73,'T',75-148 ##label PEP !'##experimental_source amyloid fibrils, hereditary non-neuropathic !1systemic amyloidosis (Ostertag-type) patient REFERENCE S65409 !$#authors Frohm, M.; Gunne, H.; Bergman, A.C.; Agerberth, B.; Bergman, !1T.; Boman, A.; Liden, S.; Joernvall, H.; Boman, H.G. !$#journal Eur. J. Biochem. (1996) 237:86-92 !$#title Biochemical and antibacterial analysis of human wound and !1blister fluid. !$#cross-references MUID:96203912; PMID:8620898 !$#accession S65415 !'##status preliminary !'##molecule_type protein !'##residues 19-38 ##label FRO REFERENCE A50263 !$#authors Artymiuk, P.J.; Blake, C.C.F. !$#submission submitted to the Brookhaven Protein Data Bank, October 1984 !$#cross-references PDB:1LZ1 !$#contents annotation; X-ray crystallography, 1.5 angstroms, residues !119-148 REFERENCE A92873 !$#authors Artymiuk, P.J.; Blake, C.C.F. !$#journal J. Mol. Biol. (1981) 152:737-762 !$#title Refinement of human lysozyme at 1.5 angstrom resolution !1analysis of non-bonded and hydrogen-bond interactions. !$#cross-references MUID:82145543; PMID:7334520 !$#contents annotation; X-ray crystallography, 1.5 angstroms REFERENCE A94420 !$#authors Banyard, S.H.; Blake, C.C.F.; Swan, I.D.A. !$#book Lysozyme, Osserman, E.F., Canfield, R.E., and Beychok, S., !1eds., pp.71-79, Academic Press, New York and London, 1974 !$#contents annotation; X-ray crystallography, 2.5 angstroms GENETICS !$#gene GDB:LYZ !'##cross-references GDB:120160; OMIM:153450 !$#map_position 12pter-12qter !$#introns 46/1; 101/1; 127/2 FUNCTION !$#description catalyzes hydrolysis of the beta-1,4-glycosidic bond between !1N-acetylmuramic acid and N-acetylglucosamine in !1peptidoglycan and other complex polysaccharides CLASSIFICATION #superfamily lysozyme c KEYWORDS bacteriolytic enzyme; glycosidase; hydrolase; polysaccharide !1degradation FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-148 #product lysozyme #status experimental #label MAT\ !$24-146,48-134, !$83-99,95-113 #disulfide_bonds #status experimental\ !$53,71 #active_site Glu, Asp #status predicted\ !$120 #binding_site substrate (Asp) #status predicted SUMMARY #length 148 #molecular-weight 16537 #checksum 5362 SEQUENCE /// ENTRY LZBA #type complete TITLE lysozyme (EC 3.2.1.17) c - baboon (tentative sequence) ORGANISM #formal_name Papio sp. #common_name baboon DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 31-Mar-2000 ACCESSIONS A00850 REFERENCE A00850 !$#authors Hermann, J.; Jolles, J.; Buss, D.H.; Jolles, P. !$#journal J. Mol. Biol. (1973) 79:587-595 !$#title Amino acid sequence of lysozyme from baboon milk. !$#cross-references MUID:74043811; PMID:4202218 !$#accession A00850 !'##molecule_type protein !'##residues 1-130 ##label HER !'##experimental_source milk FUNCTION !$#description catalyzes hydrolysis of the beta-1,4-glycosidic bond between !1N-acetylmuramic acid and N-acetylglucosamine in !1peptidoglycan and other complex polysaccharides CLASSIFICATION #superfamily lysozyme c KEYWORDS bacteriolytic enzyme; glycosidase; hydrolase FEATURE !$6-128,30-116,65-81, !$77-95 #disulfide_bonds #status predicted\ !$35,53 #active_site Glu, Asp #status predicted\ !$102 #binding_site substrate (Asp) #status predicted SUMMARY #length 130 #molecular-weight 14573 #checksum 3852 SEQUENCE /// ENTRY LZBO #type complete TITLE lysozyme (EC 3.2.1.17) c 2 precursor - bovine ALTERNATE_NAMES stomach lysozyme ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 17-Mar-1987 #sequence_revision 05-May-1995 #text_change 18-Jun-1999 ACCESSIONS C34277; B34277; D34277; E34277; A49315; A00851 REFERENCE A34277 !$#authors Irwin, D.M.; Wilson, A.C. !$#journal J. Biol. Chem. (1989) 264:11387-11393 !$#title Multiple cDNA sequences and the evolution of bovine stomach !1lysozyme. !$#cross-references MUID:89291894; PMID:2738070 !$#accession C34277 !'##molecule_type mRNA !'##residues 1-147 ##label IRW !'##cross-references GB:M26243; NID:g163316; PIDN:AAA30629.1; !1PID:g163317; GB:J04831; GB:M27182 !'##experimental_source abomasum !'##note the authors translated the codon CAA for residue 17 as Lys !'##note this sequence was designated isoform 2b !$#accession B34277 !'##molecule_type mRNA !'##residues 'T',4-147 ##label IR2 !'##cross-references GB:M26241; NID:g163314; PIDN:AAA30628.1; !1PID:g163315; GB:J04831; GB:M27181 !'##experimental_source abomasum !'##note the authors translated the codon CAA for residue 17 as Lys !'##note this sequence was designated isoform 2a !$#accession D34277 !'##molecule_type mRNA !'##residues 16,'K',18-147 ##label IR3 !'##cross-references GB:M26244; NID:g163318; PIDN:AAA30630.1; !1PID:g163319; GB:J04831; GB:M27183 !'##experimental_source abomasum !'##note this sequence was designated isoform 2c !$#accession E34277 !'##molecule_type mRNA !'##residues 44,'S',46-147 ##label IR4 !'##cross-references GB:M26240; NID:g163320; PIDN:AAA30631.1; !1PID:g163321; GB:J04831; GB:M27184 !'##experimental_source abomasum !'##note this sequence was designated isoform 2d REFERENCE A49315 !$#authors Takeuchi, K.; Irwin, D.M.; Gallup, M.; Shinbrot, E.; Kai, !1H.; Stewart, C.B.; Basbaum, C. !$#journal J. Biol. Chem. (1993) 268:27440-27446 !$#title Multiple cDNA sequences of bovine tracheal lysozyme. !$#cross-references MUID:94086565; PMID:8262986 !$#accession A49315 !'##molecule_type mRNA !'##residues 19-147 ##label TAK !'##experimental_source tracheal epithelium !'##note sequence extracted from NCBI backbone (NCBIN:140986, !1NCBIP:140988) REFERENCE A00851 !$#authors Jolles, P.; Schoentgen, F.; Jolles, J.; Dobson, D.E.; !1Prager, E.M.; Wilson, A.C. !$#journal J. Biol. Chem. (1984) 259:11617-11625 !$#title Stomach lysozymes of ruminants. II. Amino acid sequence of !1cow lysozyme 2 and immunological comparisons with other !1lysozymes. !$#cross-references MUID:84289624; PMID:6470012 !$#accession A00851 !'##molecule_type protein !'##residues 19-115,'K',117-147 ##label JOL COMMENT Lysozymes c are capable of both hydrolysis and !1transglycosylation; they show also a slight esterase !1activity. COMMENT Lysozymes c act rapidly on both peptide-substituted and !1unsubstituted peptidoglycan and, slowly, on chitin !1oligosaccharides. COMMENT The bovine lysozyme c is synthesized almost exclusively in !1the digestive tract, mainly the stomach (the lysozyme from !1other tissue is of a different type, similar to lysozyme g). COMMENT The ruminant gastric lysozymes, which digest symbiotic !1bacteria coming with cud from the rumen, are much more !1resistant to inactivation by pepsin than are other !1lysozymes. GENETICS !$#note the presence of four distinct mRNA sequences from a single !1specimen in reference A34277 suggests the presence of !1several genes or of at least two polymorphic genes for !1lysozyme 2 FUNCTION !$#description catalyzes hydrolysis of the beta-1,4-glycosidic bond between !1N-acetylmuramic acid and N-acetylglucosamine in !1peptidoglycan and other complex polysaccharides CLASSIFICATION #superfamily lysozyme c KEYWORDS bacteriolytic enzyme; glycosidase; hydrolase; rumen; stomach FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-147 #product lysozyme c 2 #status experimental #label !8MAT\ !$24-145,48-133, !$83-99,95-113 #disulfide_bonds #status predicted\ !$53,71 #active_site Glu, Asp #status predicted\ !$120 #binding_site substrate (Glu) #status predicted SUMMARY #length 147 #molecular-weight 16303 #checksum 3420 SEQUENCE /// ENTRY LZRT #type complete TITLE lysozyme (EC 3.2.1.17) 1 precursor - rat ALTERNATE_NAMES muramidese ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Nov-1980 #sequence_revision 05-Dec-1997 #text_change 07-May-1999 ACCESSIONS A40729; A00852; A60814 REFERENCE A40729 !$#authors Yeh, T.C.; Wilson, A.C.; Irwin, D.M. !$#journal Mol. Phylogenet. Evol. (1993) 2:65-75 !$#title Evolution of rodent lysozymes: isolation and sequence of the !1rat lysozyme genes. !$#cross-references MUID:94362956; PMID:8081549 !$#accession A40729 !'##status preliminary !'##molecule_type DNA !'##residues 1-148 ##label YEH !'##cross-references GB:L12459 REFERENCE A00852 !$#authors White, T.J.; Mross, G.A.; Osserman, E.F.; Wilson, A.C. !$#journal Biochemistry (1977) 16:1430-1436 !$#title Primary structure of rat lysozyme. !$#cross-references MUID:77134767; PMID:851497 !$#accession A00852 !'##molecule_type protein !'##residues 19,'T',21-63,'D',65-148 ##label WHI REFERENCE A60814 !$#authors Singh, G.; Katyal, S.L.; Brown, W.E.; Collins, D.L.; Mason, !1R.J. !$#journal Am. Rev. Respir. Dis. (1988) 138:1261-1267 !$#title Pulmonary lysozyme-a secretory protein of type II !1pneumocytes in the the rat. !$#cross-references MUID:89075395; PMID:3202483 !$#accession A60814 !'##molecule_type protein !'##residues 19,'T',21-23,'X',25-35,'X',37-38 ##label SIN GENETICS !$#introns 46/1; 101/1; 127/2 FUNCTION !$#description catalyzes hydrolysis of the beta-1,4-glycosidic bond between !1N-acetylmuramic acid and N-acetylglucosamine in !1peptidoglycan and other complex polysaccharides CLASSIFICATION #superfamily lysozyme c KEYWORDS bacteriolytic enzyme; glycosidase; hydrolase; polysaccharide !1degradation FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-148 #product lysozyme 1 #status experimental #label MAT\ !$24-146,48-134, !$83-99,95-113 #disulfide_bonds #status predicted\ !$53,71 #active_site Glu, Asp #status predicted\ !$120 #binding_site substrate (Asp) #status predicted SUMMARY #length 148 #molecular-weight 16730 #checksum 6328 SEQUENCE /// ENTRY LZCH #type complete TITLE lysozyme (EC 3.2.1.17) c precursor [validated] - chicken ALTERNATE_NAMES 1,4-beta-N-acetylmuramidase c; peptidoglycan N-acetylmuramoylhydrolase c ORGANISM #formal_name Gallus gallus #common_name chicken DATE 31-May-1979 #sequence_revision 31-May-1979 #text_change 15-Sep-2000 ACCESSIONS A93859; B93859; A41423; A92209; A92017; S23310; S65910; !1A00853; S51218 REFERENCE A93859 !$#authors Jung, A.; Sippel, A.E.; Grez, M.; Schutz, G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1980) 77:5759-5763 !$#title Exons encode functional and structural units of chicken !1lysozyme. !$#cross-references MUID:81077254; PMID:6934509 !$#accession A93859 !'##molecule_type DNA !'##residues 1-147 ##label JU1 !'##cross-references GB:J00885; NID:g212274; PIDN:AAA48943.1; !1PID:g212276 !$#accession B93859 !'##molecule_type mRNA !'##residues 1-48,'V',50-123,'S',125-147 ##label JU2 !'##cross-references GB:V00428; NID:g63580; PIDN:CAA23711.1; PID:g63581 !'##note these differences may have arisen during construction of the !1cDNA plasmid REFERENCE A41423 !$#authors Kumagai, I.; Kojima, S.; Tamaki, E.; Miura, K. !$#journal J. Biochem. (1987) 102:733-740 !$#title Conversion of trp 62 of hen egg-white lysozyme to tyr by !1site-directed mutagenesis. !$#cross-references MUID:88139224; PMID:3325501 !$#accession A41423 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-147 ##label KUM !'##experimental_source hen oviduct !'##note a site-directed mutant with Trp-80 replaced by Tyr showed !1enhanced bacteriolytic activity REFERENCE A92209 !$#authors Palmiter, R.D.; Gagnon, J.; Ericsson, L.H.; Walsh, K.A. !$#journal J. Biol. Chem. (1977) 252:6386-6393 !$#title Precursor of egg white lysozyme. Amino acid sequence of an !1NH-2-terminal extension. !$#cross-references MUID:77249586; PMID:893412 !$#accession A92209 !'##molecule_type protein !'##residues 1-20 ##label PAL REFERENCE A92017 !$#authors Canfield, R. !$#journal J. Biol. Chem. (1963) 238:2698-2707 !$#title The amino acid sequence of egg white lysozyme. !$#accession A92017 !'##molecule_type protein !'##residues 19-120,'D',122-147 ##label CAN REFERENCE S23188 !$#authors Tsugita, A.; Takamoto, K.; Kamo, M.; Iwadate, H. !$#journal Eur. J. Biochem. (1992) 206:691-696 !$#title C-terminal sequencing of protein. A novel partial acid !1hydrolysis and analysis by mass spectrometry. !$#cross-references MUID:92298996; PMID:1606956 !$#accession S23310 !'##molecule_type protein !'##residues 19-45;121-147 ##label TSU REFERENCE A92019 !$#authors Canfield, R.; Liu, A.K. !$#journal J. Biol. Chem. (1965) 240:1997-2002 !$#title The disulfide bonds of egg white lysozyme (muramidase). !$#contents annotation; disulfide bonds REFERENCE A90570 !$#authors Jauregui-Adell, J.; Jolles, J.; Jolles, P. !$#journal Biochim. Biophys. Acta (1965) 107:97-111 !$#title The disulfide bridges of hen's egg-white lysozyme. !$#cross-references MUID:66076966; PMID:5857373 !$#contents annotation; disulfide bonds REFERENCE A94444 !$#authors Imoto, T.; Johnson, L.N.; North, A.C.T.; Phillips, D.C.; !1Rupley, J.A. !$#book The Enzymes, 3rd ed., vol.7, Boyer, P.D., ed., pp.665-868, !1Academic Press, New York and London, 1972 !$#title Vertebrate lysozymes. !$#contents annotation; X-ray crystallography, 2.0 angstroms; review REFERENCE A50763 !$#authors Diamond, R.; Phillips, D.C.; Blake, C.C.F.; North, A.C.T. !$#submission submitted to the Brookhaven Protein Data Bank, February 1975 !$#cross-references PDB:6LYZ !$#contents annotation; X-ray crystallography, 1.8 angstroms, residues !119-147 REFERENCE A58453 !$#authors Diamond, R. !$#journal J. Mol. Biol. (1974) 82:371-391 !$#title Real-space refinement of the structure of hen egg-white !1lysozyme. !$#cross-references MUID:74127120; PMID:4856347 !$#contents annotation; X-ray crystallography, 2.0 angstroms REFERENCE A50266 !$#authors Hodsdon, J.M.; Brown, G.M.; Sieker, L.C.; Jensen, L.H. !$#submission submitted to the Brookhaven Protein Data Bank, April 1985 !$#cross-references PDB:1LZT !$#contents annotation; X-ray crystallography, triclinic habit, 1.97 !1angstroms, residues 19-147 REFERENCE A58454 !$#authors Kurachi, K.; Sieker, L.C.; Jensen, L.H. !$#journal J. Mol. Biol. (1976) 101:11-24 !$#title Structures of triclinic mono- and di-N-acetylglucosamine: !1lysozyme complexes - a crystallographic study. !$#cross-references MUID:76146540; PMID:1255720 !$#contents annotation; X-ray crystallography, triclinic habit, 1.97 !1angstroms, residues 19-147 REFERENCE A50949 !$#authors Kodandapani, R.; Suresh, C.G.; Vijayan, M. !$#submission submitted to the Brookhaven Protein Data Bank, July 1990 !$#cross-references PDB:4LYM !$#contents annotation; X-ray crystallography, 2.1 angstroms, residues !119-147 REFERENCE A37878 !$#authors Kodandapani, R.; Suresh, C.G.; Vijayan, M. !$#journal J. Biol. Chem. (1990) 265:16126-16131 !$#title Crystal structure of low humidity tetragonal lysozyme at !12.1-angstrom resolution. Variability in hydration shell and !1its structural consequences. !$#cross-references MUID:90375467; PMID:2398048 !$#contents annotation; X-ray crystallography, 2.1 angstroms, residues !119-147 REFERENCE A51239 !$#authors Smith, L.J.; Sutcliffe, M.J.; Redfield, C.; Dobson, C.M. !$#submission submitted to the Brookhaven Protein Data Bank, August 1992 !$#cross-references PDB:1HWA !$#contents annotation; conformation by (1)H-NMR, residues 19-147 REFERENCE A58443 !$#authors Smith, L.J.; Sutcliffe, M.J.; Redfield, C.; Dobson, C.M. !$#journal J. Mol. Biol. (1993) 229:930-944 !$#title Structure of hen lysozyme in solution. !$#cross-references MUID:93188024; PMID:8445657 !$#contents annotation; conformation by (1)H-NMR, residues 19-147 REFERENCE A30625 !$#authors Redfield, C.; Dobson, C.M. !$#journal Biochemistry (1988) 27:122-136 !$#title Sequential (1)H NMR assignments and secondary structure of !1hen egg white lysozyme in solution. !$#cross-references MUID:88163558; PMID:3349024 !$#contents annotation; conformation by (1)H-NMR, residues 19-147 REFERENCE S65910 !$#authors Fukamizo, T.; Hatta, T.; Goto, S. !$#journal Eur. J. Biochem. (1995) 231:56-64 !$#title Hen-egg-white lysozyme modified with histamine. State of the !1imidazolylethyl group covalently attached to the binding !1site and its effect on the sugar-binding ability. !$#cross-references MUID:95354703; PMID:7628485 !$#accession S65910 !'##molecule_type protein !'##residues 116-118,'X',120-130 ##label FUK COMMENT Lysozyme c has been found in the egg white and !1polymorphonuclear leukocytes. COMMENT Lysozymes are primarily bacteriolytic; those in tissues and !1body fluids are associated with the monocyte-macrophage !1system and enhance the activity of immunoagents. GENETICS !$#introns 46/1; 100/1; 126/1 FUNCTION !$#description catalyzes hydrolysis of the beta-1,4-glycosidic bond between !1N-acetylmuramic acid and N-acetylglucosamine in !1peptidoglycan and other complex polysaccharides !$#note this protein has hydrolytic and transglycosylation !1activities, and slight esterase activity; it acts rapidly on !1both peptide-substituted and unsubstituted peptidoglycan !1and, slowly, on chitin oligosaccharides CLASSIFICATION #superfamily lysozyme c KEYWORDS bacteriolytic enzyme; egg white; glycosidase; hydrolase; !1leukocyte; polysaccharide degradation FEATURE !$1-18 #domain signal sequence #status experimental #label !8SIG\ !$19-147 #product lysozyme c #status experimental #label MAT\ !$24-145,48-133, !$82-98,94-112 #disulfide_bonds #status experimental\ !$53,70 #active_site Glu, Asp #status experimental\ !$119 #binding_site substrate (Asp) #status experimental SUMMARY #length 147 #molecular-weight 16238 #checksum 2808 SEQUENCE /// ENTRY LZQJEC #type complete TITLE lysozyme (EC 3.2.1.17) c - California quail ALTERNATE_NAMES 1,4-beta-N-acetylmuramidase; peptidoglycan N-acetylmuramoylhydrolase ORGANISM #formal_name Lophortyx californica #common_name California quail DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 21-Jan-1997 ACCESSIONS A00854 REFERENCE A00854 !$#authors Ibrahimi, I.M.; Prager, E.M.; White, T.J.; Wilson, A.C. !$#journal Biochemistry (1979) 18:2736-2744 !$#title Amino acid sequence of California quail lysozyme. Effect of !1evolutionary substitutions on the antigenic structure of !1lysozyme. !$#cross-references MUID:80000412; PMID:89864 !$#accession A00854 !'##molecule_type protein !'##residues 1-129 ##label IBR !'##note lysozyme c from Lophortyx gambeli (Gambel's quail) shows !1identical composition and immunological cross-reactivity and !1has the same amino-terminal residue (Lys-1) FUNCTION !$#description catalyzes hydrolysis of the beta-1,4-glycosidic bond between !1N-acetylmuramic acid and N-acetylglucosamine in !1peptidoglycan and other complex polysaccharides CLASSIFICATION #superfamily lysozyme c KEYWORDS bacteriolytic enzyme; egg white; glycosidase; hydrolase FEATURE !$6-127,30-115,64-80, !$76-94 #disulfide_bonds #status predicted\ !$35,52 #active_site Glu, Asp #status predicted\ !$101 #binding_site substrate (Asp) #status predicted SUMMARY #length 129 #molecular-weight 14308 #checksum 3029 SEQUENCE /// ENTRY LZQJEB #type complete TITLE lysozyme (EC 3.2.1.17) c [validated] - common bobwhite ALTERNATE_NAMES 1,4-beta-N-acetylmuramidase; peptidoglycan N-acetylmuramoylhydrolase ORGANISM #formal_name Colinus virginianus #common_name common bobwhite DATE 28-Feb-1986 #sequence_revision 06-Feb-1998 #text_change 15-Sep-2000 ACCESSIONS A00855 REFERENCE A00855 !$#authors Prager, E.M.; Arnheim, N.; Mross, G.A.; Wilson, A.C. !$#journal J. Biol. Chem. (1972) 247:2905-2916 !$#title Amino acid sequence studies on bobwhite quail egg white !1lysozyme. !$#cross-references MUID:72181385; PMID:4112539 !$#accession A00855 !'##molecule_type protein !'##residues 1-129 ##label PRA !'##note the authors assumed the residue at position 103 to be Asp, !1based on the previous version of the chicken sequence; !1however, the chicken nucleotide sequence predicts 103-Asn REFERENCE A65429 !$#authors Jeffrey, P.D.; Sheriff, S. !$#submission submitted to the Brookhaven Protein Data Bank, January 1996 !$#cross-references PDB:1DKJ !$#contents annotation; X-ray crystallography, 2.0 angstroms, residues !11-129 REFERENCE A65430 !$#authors Jeffrey, P.D.; Sheriff, S. !$#submission submitted to the Brookhaven Protein Data Bank, January 1996 !$#cross-references PDB:1DKK !$#contents annotation; X-ray crystallography, 1.9 angstroms, residues !11-129 FUNCTION !$#description catalyzes hydrolysis of the beta-1,4-glycosidic bond between !1N-acetylmuramic acid and N-acetylglucosamine in !1peptidoglycan and other complex polysaccharides CLASSIFICATION #superfamily lysozyme c KEYWORDS bacteriolytic enzyme; egg white; glycosidase; hydrolase FEATURE !$6-127,30-115,64-80, !$76-94 #disulfide_bonds #status experimental\ !$35,52 #active_site Glu, Asp #status predicted\ !$101 #binding_site substrate (Asp) #status predicted SUMMARY #length 129 #molecular-weight 14271 #checksum 3015 SEQUENCE /// ENTRY LZQJE #type complete TITLE lysozyme (EC 3.2.1.17) c precursor [validated] - Japanese quail ALTERNATE_NAMES 1,4-beta-N-acetylmuramidase c; peptidoglycan N-acetylmuramoylhydrolase c; prelysozyme c ORGANISM #formal_name Coturnix coturnix japonica #common_name Japanese quail DATE 28-Feb-1986 #sequence_revision 21-Jan-1997 #text_change 15-Sep-2000 ACCESSIONS A91922; A92574; A00856 REFERENCE A91922 !$#authors Kaneda, M.; Kato, I.; Tominaga, N.; Titani, K.; Narita, K. !$#journal J. Biochem. (1969) 66:747-749 !$#title The amino acid sequence of quail lysozyme. !$#cross-references MUID:70059129; PMID:5358633 !$#accession A91922 !'##molecule_type protein !'##residues 19-44,'B',46-54,'B',56,'B',58,'Z',60-61,'B',63,'B',65,'B', !167-69,'B',71-74,'Z',76,'B',78-82,'BB',85-91,'B',93-94,'B', !196-104,'B',106-110,'B',112-147 ##label KA2 !'##experimental_source egg white REFERENCE A92574 !$#authors Weisman, L.S.; Krummel, B.M.; Wilson, A.C. !$#journal J. Biol. Chem. (1986) 261:2309-2313 !$#title Evolutionary shift in the site of cleavage of prelysozyme. !$#cross-references MUID:86111933; PMID:3511061 !$#accession A92574 !'##molecule_type protein !'##residues 1-18 ##label WEI REFERENCE A52075 !$#authors Houdusse, A.; Bentley, G.A.; Poljak, R.J.; Souchon, H.; !1Zhang, Z. !$#submission submitted to the Brookhaven Protein Data Bank, June 1993 !$#cross-references PDB:2IHL !$#contents annotation; X-ray crystallography, 1.4 angstroms, residue !119-147; sequence supported FUNCTION !$#description catalyzes hydrolysis of the beta-1,4-glycosidic bond between !1N-acetylmuramic acid and N-acetylglucosamine in !1peptidoglycan and other complex polysaccharides CLASSIFICATION #superfamily lysozyme c KEYWORDS bacteriolytic enzyme; egg white; glycosidase; hydrolase; !1polysaccharide degradation FEATURE !$1-18 #domain signal sequence #status experimental #label !8SIG\ !$19-147 #product lysozyme c #status experimental #label MAT\ !$24-145,48-133, !$82-98,94-112 #disulfide_bonds #status experimental\ !$53,70 #active_site Glu, Asp #status predicted\ !$119 #binding_site substrate (Asp) #status predicted SUMMARY #length 147 #molecular-weight 16278 #checksum 3108 SEQUENCE /// ENTRY LZFER #type complete TITLE lysozyme (EC 3.2.1.17) c precursor [validated] - ring-necked pheasant (tentative sequence) ALTERNATE_NAMES 1,4-beta-N-acetylmuramidase c; peptidoglycan N-acetylmuramoylhydrolase c; prelysozyme c ORGANISM #formal_name Phasianus colchicus #common_name ring-necked pheasant DATE 30-Nov-1980 #sequence_revision 28-May-1986 #text_change 15-Sep-2000 ACCESSIONS B92574; A90429; A00857 REFERENCE A92574 !$#authors Weisman, L.S.; Krummel, B.M.; Wilson, A.C. !$#journal J. Biol. Chem. (1986) 261:2309-2313 !$#title Evolutionary shift in the site of cleavage of prelysozyme. !$#cross-references MUID:86111933; PMID:3511061 !$#accession B92574 !'##molecule_type protein !'##residues 1-18 ##label WEI REFERENCE A90429 !$#authors Jolles, J.; Ibrahimi, I.M.; Prager, E.M.; Schoentgen, F.; !1Jolles, P.; Wilson, A.C. !$#journal Biochemistry (1979) 18:2744-2752 !$#title Amino acid sequence of pheasant lysozyme. Evolutionary !1change affecting processing of prelysozyme. !$#cross-references MUID:80000413; PMID:476049 !$#accession A90429 !'##molecule_type protein !'##residues 18-147 ##label JOL !'##experimental_source egg white !'##note peptides were positioned by homology with chicken lysozyme REFERENCE A51196 !$#authors Alzari, P.M.; Lescar, J. !$#submission submitted to the Brookhaven Protein Data Bank, May 1993 !$#cross-references PDB:1GHL !$#contents annotation; X-ray crystallography, 2.1 angstroms, residues !118-120,'N',122-147 COMMENT By the evolutionary shift in the site of proteolytic !1cleavage of prelysozyme, 18-Gly became the amino-terminal !1residue of the mature protein instead of being the !1carboxyl-terminal residue of the signal sequence as in other !1birds. FUNCTION !$#description catalyzes hydrolysis of the beta-1,4-glycosidic bond between !1N-acetylmuramic acid and N-acetylglucosamine in !1peptidoglycan and other complex polysaccharides CLASSIFICATION #superfamily lysozyme c KEYWORDS bacteriolytic enzyme; egg white; glycosidase; hydrolase; !1polysaccharide degradation FEATURE !$1-17 #domain signal sequence #status experimental #label !8SIG\ !$18-147 #product lysozyme c #status experimental #label MAT\ !$24-145,48-133, !$82-98,94-112 #disulfide_bonds #status experimental\ !$53,70 #active_site Glu, Asp #status predicted\ !$119 #binding_site substrate (Asp) #status predicted SUMMARY #length 147 #molecular-weight 16166 #checksum 3124 SEQUENCE /// ENTRY LZTK #type complete TITLE lysozyme (EC 3.2.1.17) c precursor [validated] - turkey ALTERNATE_NAMES 1,4-beta-N-acetylmuramidase c precursor; peptidoglycan N-acetylmuramoylhydrolase c precursor; prelysozyme c ORGANISM #formal_name Meleagris gallopavo #common_name common turkey DATE 24-Apr-1984 #sequence_revision 21-Jan-1997 #text_change 15-Sep-2000 ACCESSIONS C92574; A92056; A00858 REFERENCE A92574 !$#authors Weisman, L.S.; Krummel, B.M.; Wilson, A.C. !$#journal J. Biol. Chem. (1986) 261:2309-2313 !$#title Evolutionary shift in the site of cleavage of prelysozyme. !$#cross-references MUID:86111933; PMID:3511061 !$#accession C92574 !'##molecule_type protein !'##residues 1-18 ##label WEI REFERENCE A92056 !$#authors LaRue, J.N.; Speck Jr., J.C. !$#journal J. Biol. Chem. (1970) 245:1985-1991 !$#title Turkey egg white lysozyme. Preparation of the crystalline !1enzyme and investigation of the amino acid sequence. !$#cross-references MUID:70166699; PMID:5440837 !$#accession A92056 !'##molecule_type protein !'##residues 19-35,'BB',38-52,'Z',54-63,'B',65,'B',67-69,'B',71-74,'Z', !176,'B',78-82,'BB',85-91,'B',93-94,'B',96-104,'B',106-110, !1'B',112-120,'B',122-123,'B',125-136,'B',138-147 ##label LAR !'##experimental_source egg white, broad-breasted bronze and Beltsville !1white breeds REFERENCE A50264 !$#authors Bott, R.; Sarma, R. !$#submission submitted to the Brookhaven Protein Data Bank, September !11981 !$#cross-references PDB:1LZ2 !$#contents annotation; X-ray crystallography, 2.8 angstroms, residues !119-147 REFERENCE A92847 !$#authors Sarma, R.; Bott, R. !$#journal J. Mol. Biol. (1977) 113:555-565 !$#cross-references MUID:77230499; PMID:886621 !$#contents annotation; X-ray crystallography, 2.8 angstroms, and !1disulfide bonds !$#note some side chains are identified in the electron density map REFERENCE A51001 !$#authors Harata, K. !$#submission submitted to the Brookhaven Protein Data Bank, June 1993 !$#cross-references PDB:135L !$#contents annotation; X-ray crystallography, 1.30 angstroms, residues !119-147 REFERENCE A58439 !$#authors Bartik, K.; Dobson, C.M.; Redfield, C. !$#journal Eur. J. Biochem. (1993) 215:255-266 !$#title (1)H-NMR analysis of turkey egg-white lysozyme and !1comparison with hen egg-white lysozyme. !$#cross-references MUID:93345511; PMID:8344294 !$#contents annotation; sequence confirmed, and conformation determined !1by (1)H-NMR, residues 19-147 REFERENCE A58440 !$#authors Bartik, K.; Redfield, C.; Dobson, C.M. !$#journal Biophys. J. (1994) 66:1180-1184 !$#title Measurement of the individual pKa values of acidic residues !1of hen and turkey lysozymes by two-dimensional (1)H NMR. !$#cross-references MUID:94312639; PMID:8038389 !$#contents annotation; active site residues determined by (1)H-NMR FUNCTION !$#description catalyzes hydrolysis of the beta-1,4-glycosidic bond between !1N-acetylmuramic acid and N-acetylglucosamine in !1peptidoglycan and other complex polysaccharides CLASSIFICATION #superfamily lysozyme c KEYWORDS bacteriolytic enzyme; egg white; glycosidase; hydrolase; !1polysaccharide degradation FEATURE !$1-18 #domain signal sequence #status experimental #label !8SIG\ !$19-147 #product lysozyme c #status experimental #label MPT\ !$24-145,48-133, !$82-98,94-112 #disulfide_bonds #status experimental\ !$53,70 #active_site Glu, Asp #status experimental SUMMARY #length 147 #molecular-weight 16134 #checksum 2810 SEQUENCE /// ENTRY LZUH #type complete TITLE lysozyme (EC 3.2.1.17) c [validated] - helmeted guineafowl ALTERNATE_NAMES 1,4-beta-N-acetylmuramidase; peptidoglycan N-acetylmuramoylhydrolase ORGANISM #formal_name Numida meleagris #common_name helmeted guineafowl DATE 24-Apr-1984 #sequence_revision 21-Jan-1997 #text_change 15-Sep-2000 ACCESSIONS A00859 REFERENCE A00859 !$#authors Jolles, J.; van Leemputten, E.; Mouton, A.; Jolles, P. !$#journal Biochim. Biophys. Acta (1972) 257:497-510 !$#title Amino acid sequence of guinea-hen egg-white lysozyme. !$#cross-references MUID:72170113; PMID:5063251 !$#accession A00859 !'##molecule_type protein !'##residues 1-102,'B',104-129 ##label JO2 !'##experimental_source egg white !'##note the authors assumed the residue at position 103 to be Asp, !1based on the previous version of the chicken sequence; !1however, the chicken nucleotide sequence predicts 103-Asn REFERENCE A51228 !$#authors Alzari, P.M.; Lescar, J. !$#submission submitted to the Brookhaven Protein Data Bank, May 1993 !$#cross-references PDB:1HHL !$#contents annotation; X-ray crystallography, 1.9 angstroms, residues !11-129 FUNCTION !$#description catalyzes hydrolysis of the beta-1,4-glycosidic bond between !1N-acetylmuramic acid and N-acetylglucosamine in !1peptidoglycan and other complex polysaccharides CLASSIFICATION #superfamily lysozyme c KEYWORDS bacteriolytic enzyme; egg white; glycosidase; hydrolase; !1polysaccharide degradation FEATURE !$6-127,30-115,64-80, !$76-94 #disulfide_bonds #status experimental\ !$35,52 #active_site Glu, Asp #status predicted\ !$101 #binding_site substrate (Asp) #status predicted SUMMARY #length 129 #molecular-weight 14310 #checksum 1392 SEQUENCE /// ENTRY LZDK #type complete TITLE lysozyme (EC 3.2.1.17) c precursor - duck ALTERNATE_NAMES 1,4-beta-N-acetylmuramidase c precursor; peptidoglycan N-acetylmuramoylhydrolase c precursor; prelysozyme c ORGANISM #formal_name Anas platyrhynchos #common_name domestic duck DATE 24-Apr-1984 #sequence_revision 28-May-1986 #text_change 07-May-1999 ACCESSIONS D92574; A91967; B91967; C91967; A91189; A00860 REFERENCE A92574 !$#authors Weisman, L.S.; Krummel, B.M.; Wilson, A.C. !$#journal J. Biol. Chem. (1986) 261:2309-2313 !$#title Evolutionary shift in the site of cleavage of prelysozyme. !$#cross-references MUID:86111933; PMID:3511061 !$#accession D92574 !'##molecule_type protein !'##residues 1-18 ##label WEI !'##experimental_source Pekin breed REFERENCE A91967 !$#authors Kondo, K.; Fujio, H.; Amano, T. !$#journal J. Biochem. (1982) 91:571-587 !$#title Chemical and immunological properties and amino acid !1sequences of three lysozymes from Peking-duck egg white. !$#cross-references MUID:82167337; PMID:7068576 !$#contents DL-1; DL-2; DL-3 !$#accession A91967 !'##molecule_type protein !'##residues 19-54,'S',56-88,'G',90-147 ##label KO1 !'##experimental_source Pekin breed !$#accession B91967 !'##molecule_type protein !'##residues 19-147 ##label KO2 !$#accession C91967 !'##molecule_type protein !'##residues 19-96,'R',98-147 ##label KO3 !'##note 43-Ile was also found REFERENCE A91189 !$#authors Hermann, J.; Jolles, J.; Jolles, P. !$#journal Eur. J. Biochem. (1971) 24:12-17 !$#title Multiple forms of duck-egg-white lysozyme. Primary structure !1of two duck lysozymes. !$#cross-references MUID:72095897; PMID:5138644 !$#contents lysozyme II !$#accession A91189 !'##molecule_type protein !'##residues 19-54,'S',56-74,'E',76-88,'G',90-147 ##label HER REFERENCE A90056 !$#authors Hermann, J.; Jolles, J.; Jolles, P. !$#journal Arch. Biochem. Biophys. (1973) 158:355-358 !$#title The disulfide bridges of duck egg-white lysozyme II. !$#cross-references MUID:73248843; PMID:4580844 !$#contents annotation; lysozyme II, disulfide bonds REFERENCE A92011 !$#authors Prager, E.M.; Wilson, A.C. !$#journal J. Biol. Chem. (1971) 246:523-530 !$#cross-references MUID:71104910; PMID:5542021 !$#contents annotation; lysozymes A, B, and C, electrophoresis, !1immunology, and amino acid composition; Pekin breed !$#note as only one lysozyme, or any combination of two lysozymes, !1but never all three, occurred in one egg, the existence of !1three alleles at one locus has been suggested COMMENT The sequence of the DL-2 variant of lysozyme c from Pekin !1breed is shown. COMMENT The amino acid compositions of DL-1, DL-2, and DL-3 are !1identical with those of lysozymes A, B, and C, respectively. !1DL-1 and DL-2 are electrophoretically and immunologically !1indistinguishable from lysozymes A and B, respectively. FUNCTION !$#description catalyzes hydrolysis of the beta-1,4-glycosidic bond between !1N-acetylmuramic acid and N-acetylglucosamine in !1peptidoglycan and other complex polysaccharides CLASSIFICATION #superfamily lysozyme c KEYWORDS bacteriolytic enzyme; egg white; glycosidase; hydrolase FEATURE !$1-18 #domain signal sequence #status experimental #label !8SIG\ !$19-147 #product lysozyme c #status experimental #label MAT\ !$24-145,48-133, !$82-98,94-112 #disulfide_bonds #status experimental\ !$53,70 #active_site Glu, Asp #status predicted\ !$119 #binding_site substrate (Asp) #status predicted SUMMARY #length 147 #molecular-weight 16363 #checksum 4441 SEQUENCE /// ENTRY LZDK3 #type complete TITLE lysozyme (EC 3.2.1.17) c III - duck ALTERNATE_NAMES 1,4-beta-N-acetylmuramidase; peptidoglycan N-acetylmuramoylhydrolase ORGANISM #formal_name Anas platyrhynchos #common_name domestic duck DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 21-Jan-1997 ACCESSIONS A00861 REFERENCE A91189 !$#authors Hermann, J.; Jolles, J.; Jolles, P. !$#journal Eur. J. Biochem. (1971) 24:12-17 !$#title Multiple forms of duck-egg-white lysozyme. Primary structure !1of two duck lysozymes. !$#cross-references MUID:72095897; PMID:5138644 !$#accession A00861 !'##molecule_type protein !'##residues 1-129 ##label HER !'##experimental_source Kaki breed !'##note 37-Gly was found in 30% of the molecules FUNCTION !$#description catalyzes hydrolysis of the beta-1,4-glycosidic bond between !1N-acetylmuramic acid and N-acetylglucosamine in !1peptidoglycan and other complex polysaccharides CLASSIFICATION #superfamily lysozyme c KEYWORDS bacteriolytic enzyme; egg white; glycosidase; hydrolase FEATURE !$6-127,30-115,64-80, !$76-94 #disulfide_bonds #status predicted\ !$35,52 #active_site Glu, Asp #status predicted\ !$101 #binding_site substrate (Asp) #status predicted SUMMARY #length 129 #molecular-weight 14507 #checksum 1984 SEQUENCE /// ENTRY LZOVE #type complete TITLE lysozyme (EC 3.2.1.17) c - plain chachalaca ALTERNATE_NAMES 1,4-beta-N-acetylmuramidase; peptidoglycan N-acetylmuramoylhydrolase ORGANISM #formal_name Ortalis vetula #common_name plain chachalaca DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 21-Jan-1997 ACCESSIONS A00862 REFERENCE A00862 !$#authors Jolles, J.; Schoentgen, F.; Jolles, P.; Prager, E.M.; !1Wilson, A.C. !$#journal J. Mol. Evol. (1976) 8:59-78 !$#title Amino acid sequence and immunological properties of !1chachalaca egg white lysozyme. !$#cross-references MUID:76240636; PMID:940173 !$#accession A00862 !'##molecule_type protein !'##residues 1-129 ##label JOL FUNCTION !$#description catalyzes hydrolysis of the beta-1,4-glycosidic bond between !1N-acetylmuramic acid and N-acetylglucosamine in !1peptidoglycan and other complex polysaccharides CLASSIFICATION #superfamily lysozyme c KEYWORDS bacteriolytic enzyme; egg white; glycosidase; hydrolase FEATURE !$6-127,30-115,64-80, !$76-94 #disulfide_bonds #status predicted\ !$35,52 #active_site Glu, Asp #status predicted\ !$101 #binding_site substrate (Asp) #status predicted SUMMARY #length 129 #molecular-weight 14509 #checksum 2803 SEQUENCE /// ENTRY LZPY #type complete TITLE lysozyme (EC 3.2.1.17) c - pigeon ALTERNATE_NAMES 1,4-beta-N-acetylmuramidase c; peptidoglycan N-acetylmuramoylhydrolase c ORGANISM #formal_name Columba livia #common_name domestic pigeon DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 21-Jan-1997 ACCESSIONS A00863 REFERENCE A00863 !$#authors Rodriguez, R.; Menendez-Arias, L.; Gonzalez de Buitrago, G.; !1Gavilanes, J.G. !$#journal Biochem. Int. (1985) 11:841-843 !$#title Amino acid sequence of pigeon egg-white lysozyme. !$#cross-references MUID:86130671; PMID:4091856 !$#accession A00863 !'##molecule_type protein !'##residues 1-127 ##label ROD FUNCTION !$#description catalyzes hydrolysis of the beta-1,4-glycosidic bond between !1N-acetylmuramic acid and N-acetylglucosamine in !1peptidoglycan and other complex polysaccharides CLASSIFICATION #superfamily lysozyme c KEYWORDS bacteriolytic enzyme; egg white; glycosidase; hydrolase FEATURE !$6-127,30-115,64-80, !$76-94 #disulfide_bonds #status predicted\ !$35,52 #active_site Glu, Asp #status predicted\ !$101 #binding_site substrate (Glu) #status predicted SUMMARY #length 127 #molecular-weight 14452 #checksum 8919 SEQUENCE /// ENTRY LZWK #type fragment TITLE lysozyme (EC 3.2.1.17) c precursor - cecropia moth (fragment) ALTERNATE_NAMES 1,4-beta-N-acetylmuramidase c; peptidoglycan N-acetylmuramoylhydrolase c ORGANISM #formal_name Hyalophora cecropia #common_name cecropia moth DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 21-Jan-1997 ACCESSIONS A24649 REFERENCE A24649 !$#authors Engstrom, A.; Xanthopoulos, K.G.; Boman, H.G.; Bennich, H. !$#journal EMBO J. (1985) 4:2119-2122 !$#title Amino acid and cDNA sequences of lysozyme from Hyalophora !1cecropia. !$#accession A24649 !'##molecule_type mRNA !'##residues 1-132 ##label ENG !'##experimental_source pupae !'##note 27-Leu and 78-Thr were also found FUNCTION !$#description catalyzes hydrolysis of the beta-1,4-glycosidic bond between !1N-acetylmuramic acid and N-acetylglucosamine in !1peptidoglycan and other complex polysaccharides CLASSIFICATION #superfamily lysozyme c KEYWORDS bacteriolytic enzyme; glycosidase; hydrolase FEATURE !$1-12 #domain signal sequence (fragment) #status predicted !8#label SIG\ !$13-132 #product lysozyme c #status predicted #label MPT\ !$18-132,39-122, !$74-88,84-102 #disulfide_bonds #status predicted\ !$44,62 #active_site Glu, Asp #status predicted SUMMARY #length 132 #checksum 2669 SEQUENCE /// ENTRY A40796 #type complete TITLE lysozyme (EC 3.2.1.17) - tobacco hornworm ORGANISM #formal_name Manduca sexta #common_name tobacco hornworm DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A40796 REFERENCE A40796 !$#authors Rosenthal, G.A.; Dahlman, D.L. !$#journal J. Biol. Chem. (1991) 266:15684-15687 !$#title Studies of L-canavanine incorporation into insectan !1lysozyme. !$#cross-references MUID:91340702; PMID:1874726 !$#accession A40796 !'##molecule_type protein !'##residues 1-120 ##label ROS CLASSIFICATION #superfamily lysozyme c KEYWORDS bacteriolytic enzyme; glycosidase; hydrolase; polysaccharide !1degradation SUMMARY #length 120 #molecular-weight 13984 #checksum 5656 SEQUENCE /// ENTRY JC4233 #type complete TITLE lysozyme (EC 3.2.1.17) precursor - silkworm ORGANISM #formal_name Bombyx mori #common_name silkworm DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JC4233; PC4067 REFERENCE JC4233 !$#authors Lee, W.J.; Brey, P.T. !$#journal Gene (1995) 161:199-203 !$#title Isolation and characterization of the lysozyme-encoding gene !1from the silkworm Bombyx mori. !$#cross-references MUID:95394356; PMID:7665079 !$#accession JC4233 !'##molecule_type mRNA !'##residues 1-137 ##label LEE !'##cross-references GB:L37416; NID:g567098; PIDN:AAB40947.1; !1PID:g567099 !$#accession PC4067 !'##molecule_type protein !'##residues 19-24;40-45 ##label LE2 COMMENT This enzyme catalyzes the hydrolysis of the beta-1, !14-glycosidic linkage between N-acetyl muramic acid and !1N-acetylglucosamine of peptidoglycan. It is up-regulated in !1fat body, hemocytes and cuticular epidermal tissue following !1the injection of Gram positive bacteria. COMMENT This protein has eight structural important cysteine !1residues. GENETICS !$#gene lys CLASSIFICATION #superfamily lysozyme c KEYWORDS bacteriolytic enzyme; glycosidase; hydrolase; polysaccharide !1degradation FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-137 #product lysozyme #status predicted #label MAT\ !$50,67 #active_site Glu, Asp #status predicted SUMMARY #length 137 #molecular-weight 15668 #checksum 1173 SEQUENCE /// ENTRY LAHU #type complete TITLE alpha-lactalbumin precursor [validated] - human ALTERNATE_NAMES lactose synthase (EC 2.4.1.22) protein B ORGANISM #formal_name Homo sapiens #common_name man DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 15-Sep-2000 ACCESSIONS A27880; A93427; A91196; A00864 REFERENCE A27880 !$#authors Hall, L.; Emery, D.C.; Davies, M.S.; Parker, D.; Craig, R.K. !$#journal Biochem. J. (1987) 242:735-742 !$#title Organization and sequence of the human alpha-lactalbumin !1gene. !$#cross-references MUID:87241386; PMID:2954544 !$#accession A27880 !'##molecule_type DNA !'##residues 1-142 ##label HAL1 !'##cross-references GB:X05153; NID:g34212; PIDN:CAA28799.1; PID:g296662 REFERENCE A93427 !$#authors Hall, L.; Craig, R.K.; Edbrooke, M.R.; Campbell, P.N. !$#journal Nucleic Acids Res. (1982) 10:3503-3515 !$#title Comparison of the nucleotide sequence of cloned human and !1guinea-pig pre-alpha-lactalbumin cDNA with that of chick !1pre-lysozyme cDNA suggests evolution from a common ancestral !1gene. !$#cross-references MUID:82247223; PMID:6285305 !$#accession A93427 !'##molecule_type mRNA !'##residues 1-142 ##label HAL2 !'##cross-references GB:J00270; NID:g186830; PIDN:AAA60345.1; !1PID:g307104 REFERENCE A91196 !$#authors Findlay, J.B.C.; Brew, K. !$#journal Eur. J. Biochem. (1972) 27:65-86 !$#title The complete amino-acid sequence of human alpha-lactalbumin. !$#cross-references MUID:72250267; PMID:5049057 !$#accession A91196 !'##molecule_type protein !'##residues 20-63,'DQ',66-100,'N',102,'N',104-105,'NN',108-120,'N', !1122-142 ##label FIN REFERENCE A43134 !$#authors Giuffrida, M.G.; Cavaletto, M.; Giunta, C.; Neuteboom, B.; !1Cantisani, A.; Napolitano, L.; Calderone, V.; !1Godovac-Zimmermann, J.; Conti, A. !$#journal J. Protein Chem. (1997) 16:747-753 !$#title The unusual amino acid triplet Asn-Ile-Cys is a !1glycosylation consensus site in human alpha-lactalbumin. !$#cross-references MUID:98032627; PMID:9365923 !$#contents annotation; sequence confirmation; mass spectrographic !1detection of glycosylation REFERENCE A67004 !$#authors Ren, J.; Stuart, D.I.; Acharya, K.R. !$#submission submitted to the Brookhaven Protein Data Bank, September !11994 !$#cross-references PDB:1HML !$#contents annotation; X-ray crystallography, 1.7 angstroms, residues !120-142 REFERENCE A58676 !$#authors Acharya, K.R.; Ren, J.; Stuart, D.I.; Phillips, D.C.; Fenna, !1R.E. !$#journal J. Mol. Biol. (1991) 221:571-581 !$#title Crystal structure of human alpha-lactalbumin at 1.7 !1Angstroms resolution. !$#cross-references MUID:92015247; PMID:1920433 !$#contents annotation; X-ray crystallography, 1.7 angstroms GENETICS !$#gene GDB:LALBA !'##cross-references GDB:120134; OMIM:149750 !$#map_position 12q13-12q13 !$#introns 45/1; 98/1; 123/2 FUNCTION !$#description as a regulatory subunit of lactose synthase, !1alpha-lactalbumin changes the substrate specificity of !1galactosyltransferase in the mammary gland, making glucose !1an acceptor rather than N-acetylglucosaminylpeptide !$#pathway lactose biosynthesis CLASSIFICATION #superfamily lysozyme c KEYWORDS calcium; glycoprotein; glycosyltransferase; !1hexosyltransferase; lactose biosynthesis; mammary gland; !1milk FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-142 #product alpha-lactalbumin #status experimental !8#label MAT\ !$25-139,47-130, !$80-96,92-110 #disulfide_bonds #status experimental\ !$64 #binding_site carbohydrate (Asn) (covalent) #status !8absent\ !$90 #binding_site carbohydrate (Asn) (covalent) (partial) !8#status atypical\ !$98,101,103,106,107 #binding_site calcium (Lys, Asp, Asp, Asp, Asp) !8#status experimental SUMMARY #length 142 #molecular-weight 16225 #checksum 7328 SEQUENCE /// ENTRY LACM #type complete TITLE alpha-lactalbumin - Arabian camel ALTERNATE_NAMES lactose synthase (EC 2.4.1.22) protein B ORGANISM #formal_name Camelus dromedarius #common_name Arabian camel DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 21-Nov-1997 ACCESSIONS A00865 REFERENCE A00865 !$#authors Beg, O.U.; von Bahr-Lindstrom, H.; Zaidi, Z.H.; Jornvall, H. !$#journal Eur. J. Biochem. (1985) 147:233-239 !$#title The primary structure of alpha-lactalbumin from camel milk. !$#cross-references MUID:85127035; PMID:3971980 !$#accession A00865 !'##molecule_type protein !'##residues 1-123 ##label BEG COMMENT Alpha-lactalbumin is synthesized only in the mammary gland. COMMENT As a regulatory subunit of lactose synthase, !1alpha-lactalbumin changes substrate specificity of !1galactosyltransferase in the mammary gland, making glucose a !1good acceptor substrate for this enzyme. In other tissues, !1galactosyltransferase transfers galactose onto the !1N-acetylglucosamine of the oligosaccharide chains in !1glycoproteins. CLASSIFICATION #superfamily lysozyme c KEYWORDS calcium; glycoprotein; glycosyltransferase; !1hexosyltransferase; lactose biosynthesis; mammary gland; !1milk FEATURE !$6-120,28-111,61-77, !$73-91 #disulfide_bonds #status predicted SUMMARY #length 123 #molecular-weight 14430 #checksum 1751 SEQUENCE /// ENTRY LAHO #type complete TITLE alpha-lactalbumin - horse ALTERNATE_NAMES lactose synthase (EC 2.4.1.22) protein B ORGANISM #formal_name Equus caballus #common_name domestic horse DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 21-Nov-1997 ACCESSIONS A29147 REFERENCE A29147 !$#authors Kaminogawa, S.; McKenzie, H.A.; Shaw, D.C. !$#journal Biochem. Int. (1984) 9:539-546 !$#title The amino acid sequence of equine alpha-lactalbumin. !$#cross-references MUID:85121939; PMID:6525193 !$#accession A29147 !'##molecule_type protein !'##residues 1-123 ##label KAM CLASSIFICATION #superfamily lysozyme c KEYWORDS calcium; glycosyltransferase; hexosyltransferase; lactose !1biosynthesis; mammary gland; milk FEATURE !$6-120,28-111,61-77, !$73-91 #disulfide_bonds #status predicted SUMMARY #length 123 #molecular-weight 14224 #checksum 3641 SEQUENCE /// ENTRY LAPG #type complete TITLE alpha-lactalbumin precursor - pig ALTERNATE_NAMES lactose synthase (EC 2.4.1.22) B component ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 31-Mar-1992 #sequence_revision 31-Jan-1997 #text_change 18-Jun-1999 ACCESSIONS JH0264; S10617 REFERENCE JH0264 !$#authors Das Gupta, N.A.; Alexander, L.J.; Beattie, C.W. !$#journal Gene (1992) 110:265-266 !$#title The sequence of a porcine cDNA encoding alpha-lactoalbumin. !$#cross-references MUID:92165071; PMID:1537566 !$#accession JH0264 !'##molecule_type mRNA !'##residues 1-141 ##label DAS !'##cross-references GB:M80520; NID:g164526; PIDN:AAA31060.1; !1PID:g164527 REFERENCE S10617 !$#authors Godovac-Zimmermann, J.; Conti, A.; Napolitano, L. !$#journal Biol. Chem. Hoppe-Seyler (1990) 371:649-653 !$#title The complete primary structure of alpha-lactalbumin isolated !1from pig (Sus scrofa) milk. !$#cross-references MUID:91025636; PMID:2222864 !$#accession S10617 !'##molecule_type protein !'##residues 20-61,'SN',64-67,'F',69-106,'D',108-140,'L' ##label GOD COMMENT In the presence of this protein, the N-acetyllactosamine !1synthase (EC 2.4.1.90) functions as lactose synthase (EC !12.4.1.22). CLASSIFICATION #superfamily lysozyme c KEYWORDS calcium; glycosyltransferase; hexosyltransferase; lactose !1biosynthesis; mammary gland; milk FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-141 #product alpha-lactalbumin #status predicted #label !8ALP\ !$97-106 #domain calcium binding #status predicted #label CAB\ !$25-138,47-129, !$80-95,91-109 #disulfide_bonds #status predicted SUMMARY #length 141 #molecular-weight 16174 #checksum 5735 SEQUENCE /// ENTRY LABO #type complete TITLE alpha-lactalbumin precursor [validated] - bovine ALTERNATE_NAMES lactose synthase (EC 2.4.1.22) protein B ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 24-Apr-1984 #sequence_revision 06-Feb-1995 #text_change 15-Sep-2000 ACCESSIONS A27360; A34188; S02332; I45994; B25251; A90577; S62671; !1A00866 REFERENCE A27360 !$#authors Hurley, W.L.; Schuler, L.A. !$#journal Gene (1987) 61:119-122 !$#title Molecular cloning and nucleotide sequence of a bovine !1alpha-lactalbumin cDNA. !$#cross-references MUID:88167838; PMID:3443304 !$#accession A27360 !'##molecule_type mRNA !'##residues 1-142 ##label HUR !'##cross-references GB:M18780; NID:g163282; PIDN:AAA30615.1; !1PID:g163283 REFERENCE A34188 !$#authors Wang, M.; Scott, W.A.; Rao, K.R.; Udey, J.; Conner, G.E.; !1Brew, K. !$#journal J. Biol. Chem. (1989) 264:21116-21121 !$#title Recombinant bovine alpha-lactalbumin obtained by limited !1proteolysis of a fusion protein expressed at high levels in !1Escherichia coli. !$#cross-references MUID:90078209; PMID:2687274 !$#accession A34188 !'##molecule_type mRNA !'##residues 1-142 ##label WAN !'##cross-references GB:J05147; NID:g162643; PIDN:AAA30367.1; !1PID:g162644 REFERENCE S02332 !$#authors Vilotte, J.L.; Soulier, S.; Mercier, J.C.; Gaye, P.; !1Hue-Delahaie, D.; Furet, J.P. !$#journal Biochimie (1987) 69:609-620 !$#title Complete nucleotide sequence of bovine alpha-lactalbumin !1gene: comparison with its rat counterpart. !$#cross-references MUID:88078102; PMID:3120795 !$#accession S02332 !'##molecule_type DNA !'##residues 1-48,'A',50-142 ##label VIL !'##cross-references EMBL:X06366; NID:g497; PIDN:CAA29664.1; PID:g295774 !'##note the authors translated the codon GCG for residue 49 as Thr REFERENCE I45994 !$#authors Viaene, A.; Volckaert, G.; Joniau, M.; De Baetselier, A.; !1Van Cauwelaert, F. !$#journal Eur. J. Biochem. (1991) 202:471-477 !$#title Efficient expression of bovine alpha-lactalbumin in !1Saccharomyces cerevisiae. !$#cross-references MUID:92104168; PMID:1840525 !$#accession I45994 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 20-48,'A',50-142 ##label VIA !'##cross-references EMBL:X63317; NID:g67; PIDN:CAA44927.1; PID:g68 REFERENCE A92476 !$#authors Shewale, J.G.; Sinha, S.K.; Brew, K. !$#journal J. Biol. Chem. (1984) 259:4947-4956 !$#title Evolution of alpha-lactalbumins. The complete amino acid !1sequence of the alpha-lactalbumin from a marsupial (Macropus !1rufogriseus) and corrections to regions of sequence in !1bovine and goat alpha-lactalbumins. !$#cross-references MUID:84185596; PMID:6715332 !$#accession B25251 !'##molecule_type protein !'##residues 20-57,'E',59-81,'N',83-84,'D',86-142 ##label SHE REFERENCE A92066 !$#authors Brew, K.; Castellino, F.J.; Vanaman, T.C.; Hill, R.L. !$#journal J. Biol. Chem. (1970) 245:4570-4582 !$#title The complete amino acid sequence of bovine !1alpha-lactalbumin. !$#cross-references MUID:71103833; PMID:5532231 !$#contents annotation !$#note this sequence has been revised in reference A92476 REFERENCE A90577 !$#authors Bell, K.; Hopper, K.E.; McKenzie, H.A.; Murphy, W.H.; Shaw, !1D.C. !$#journal Biochim. Biophys. Acta (1970) 214:437-444 !$#title A comparison of bovine alpha-lactalbumin A and B of !1Droughtmaster. !$#cross-references MUID:71159904; PMID:5534301 !$#contents allelic variants, tentative sequences !$#accession A90577 !'##molecule_type protein !'##residues 20-57,'E',59-81,'N',83-84,'D',86-142 ##label BEL !'##experimental_source Droughtmaster breed !'##note the sequence from variant B appears to be identical with that !1shown; that from variant A appears to differ only in having !129-Gln REFERENCE S62671 !$#authors Matsumura, Y.; Chanyongvorakul, Y.; Kumazawa, Y.; Ohtsuka, !1T.; Mori, T. !$#journal Biochim. Biophys. Acta (1996) 1292:69-76 !$#title Enhanced susceptibility to transglutaminase reaction of !1alpha-lactalbumin in the molten globule state. !$#cross-references MUID:96139329; PMID:8547351 !$#accession S62671 !'##status preliminary !'##molecule_type protein !'##residues 74-78 ##label MAS REFERENCE A92067 !$#authors Vanaman, T.C.; Brew, K.; Hill, R.L. !$#journal J. Biol. Chem. (1970) 245:4583-4590 !$#title The disulfide bonds of bovine alpha-lactalbumin. !$#cross-references MUID:71103834; PMID:5532232 !$#contents annotation; disulfide bonds REFERENCE A90219 !$#authors Hiraoka, Y.; Segawa, T.; Kuwajima, K.; Sugai, S.; Murai, N. !$#journal Biochem. Biophys. Res. Commun. (1980) 95:1098-1104 !$#title alpha-Lactalbumin: a calcium metalloprotein. !$#cross-references MUID:81021144; PMID:6774718 !$#contents annotation; calcium binding REFERENCE A92335 !$#authors Kronman, M.J.; Sinha, S.K.; Brew, K. !$#journal J. Biol. Chem. (1981) 256:8582-8587 !$#title Characteristics of the binding of Ca(2+) and other divalent !1metal ions to bovine alpha-lactalbumin. !$#cross-references MUID:81264272; PMID:7263672 !$#contents annotation; calcium binding REFERENCE A67606 !$#authors Pike, A.C.W.; Brew, K.; Acharya, K.R. !$#submission submitted to the Brookhaven Protein Data Bank, June 1996 !$#cross-references PDB:1HFZ !$#contents annotation; X-ray crystallography, 2.3 angstroms, engineered !1sequence, residues 'M',20-108,'M',110-141 COMMENT Calcium is bound at two sites, one strong, and one weak. GENETICS !$#gene alfaLA !$#introns 45/1; 98/1; 123/2 FUNCTION !$#description as a regulatory subunit of lactose synthase, !1alpha-lactalbumin changes the substrate specificity of !1galactosyltransferase in the mammary gland, making glucose !1an acceptor rather than N-acetylglucosaminylpeptide !$#pathway lactose biosynthesis CLASSIFICATION #superfamily lysozyme c KEYWORDS calcium; glycosyltransferase; hexosyltransferase; lactose !1biosynthesis; mammary gland; milk FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-142 #product alpha-lactalbumin #status predicted #label !8MAT\ !$25-139,47-130, !$80-96,92-110 #disulfide_bonds #status experimental\ !$44,130,131,132,133, !$135 #binding_site calcium (Glu, Cys, Ser, Glu, Lys, Asp) !8#status predicted\ !$64 #binding_site carbohydrate (Asn) (covalent) #status !8absent\ !$98,101,103,106,107 #binding_site calcium (Lys, Asp, Asp, Asp, Asp) !8#status predicted SUMMARY #length 142 #molecular-weight 16246 #checksum 747 SEQUENCE /// ENTRY LABOZ #type complete TITLE alpha-lactalbumin - bovine (tentative sequence) ALTERNATE_NAMES lactose synthase (EC 2.4.1.22) protein B ORGANISM #formal_name Bos primigenius indicus #common_name zebu cattle DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 21-Nov-1997 ACCESSIONS A92772; A00866 REFERENCE A92772 !$#authors Gordon, W.G.; Aschaffenburg, R.; Sen, A.; Ghosh, S.K. !$#journal J. Dairy Sci. (1968) 51:947 !$#contents variant A, amino acid composition !$#accession A92772 !'##molecule_type protein !'##residues 1-123 ##label GOR COMMENT Alpha-lactalbumin is synthesized only in the mammary gland. COMMENT As a regulatory subunit of lactose synthase, !1alpha-lactalbumin changes the substrate specificity of !1galactosyltransferase in the mammary gland, making glucose a !1good acceptor substrate for this enzyme. In other tissues, !1galactosyltransferase transfers galactose onto the !1N-acetylglucosamine of the oligosaccharide chains in !1glycoproteins. CLASSIFICATION #superfamily lysozyme c KEYWORDS calcium; glycoprotein; glycosyltransferase; !1hexosyltransferase; lactose biosynthesis; mammary gland; !1milk FEATURE !$6-120,28-111,61-77, !$73-91 #disulfide_bonds #status predicted\ !$25,112,113,116 #binding_site calcium (Glu, Ser, Glu, Asp) #status !8predicted\ !$45 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 123 #molecular-weight 14159 #checksum 3727 SEQUENCE /// ENTRY LAGT #type complete TITLE alpha-lactalbumin precursor [validated] - goat ALTERNATE_NAMES lactose synthase (EC 2.4.1.22) protein B ORGANISM #formal_name Capra aegagrus hircus #common_name domestic goat DATE 28-May-1986 #sequence_revision 23-Aug-1997 #text_change 15-Sep-2000 ACCESSIONS JU0455; A25848; A00867 REFERENCE JU0455 !$#authors Vilotte, J.L.; Soulier, S.; Printz, C.; Mercier, J.C. !$#journal Gene (1991) 98:271-276 !$#title Sequence of the goat alpha-lactalbumin-encoding gene: !1comparison with the bovine gene and evidence of related !1sequences in the goat genome. !$#cross-references MUID:91200677; PMID:2016067 !$#accession JU0455 !'##molecule_type DNA !'##residues 1-142 ##label VIL !'##cross-references GB:M63868; NID:g164106 !'##note this ORF is not translated in GenBank entry GOTALAL REFERENCE A25848 !$#authors Kumagai, I.; Tamaki, E.; Kakinuma, S.; Miura, K. !$#journal J. Biochem. (1987) 101:511-517 !$#title Molecular cloning and sequencing of cDNA encoding goat pre !1alpha-lactalbumin. !$#cross-references MUID:87222269; PMID:2884215 !$#accession A25848 !'##molecule_type mRNA !'##residues 1-142 ##label KUM !'##cross-references GB:X05149; NID:g979; PIDN:CAA28797.1; PID:g980 REFERENCE A92476 !$#authors Shewale, J.G.; Sinha, S.K.; Brew, K. !$#journal J. Biol. Chem. (1984) 259:4947-4956 !$#title Evolution of alpha-lactalbumins. The complete amino acid !1sequence of the alpha-lactalbumin from a marsupial (Macropus !1rufogriseus) and corrections to regions of sequence in !1bovine and goat alpha-lactalbumins. !$#cross-references MUID:84185596; PMID:6715332 !$#accession A00867 !'##molecule_type protein !'##residues 20-84,'D',86-142 ##label SHE REFERENCE A90065 !$#authors MacGillivray, R.T.A.; Brew, K.; Barnes, K. !$#journal Arch. Biochem. Biophys. (1979) 197:404-414 !$#title The amino acid sequence of goat alpha-lactalbumin. !$#cross-references MUID:80063770; PMID:507821 !$#contents annotation !$#note this sequence has been revised in reference A92476 REFERENCE A67605 !$#authors Pike, A.C.W.; Brew, K.; Acharya, K.R. !$#submission submitted to the Brookhaven Protein Data Bank, June 1996 !$#cross-references PDB:1HFY !$#contents annotation; X-ray crystallography, 2.3 angstroms, residues !120-139 GENETICS !$#gene alpha-LA !$#introns 45/1; 98/1; 123/2 FUNCTION !$#description as a regulatory subunit of lactose synthase, !1alpha-lactalbumin changes the substrate specificity of !1galactosyltransferase in the mammary gland, making glucose !1an acceptor rather than N-acetylglucosaminylpeptide !$#pathway lactose biosynthesis CLASSIFICATION #superfamily lysozyme c KEYWORDS calcium; glycosyltransferase; hexosyltransferase; lactose !1biosynthesis; mammary gland; milk FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-142 #product alpha-lactalbumin #status experimental !8#label MAT\ !$25-139,47-130, !$80-96,92-110 #disulfide_bonds #status experimental\ !$64 #binding_site carbohydrate (Asn) (covalent) #status !8absent\ !$98,101,103,106,107 #binding_site calcium (Lys, Asp, Asp, Asp, Asp) !8#status predicted SUMMARY #length 142 #molecular-weight 16254 #checksum 9161 SEQUENCE /// ENTRY LAGP #type complete TITLE alpha-lactalbumin precursor [validated] - guinea pig CONTAINS lactose synthase (EC 2.4.1.22) protein B ORGANISM #formal_name Cavia porcellus #common_name guinea pig DATE 13-Jun-1983 #sequence_revision 21-Nov-1997 #text_change 15-Sep-2000 ACCESSIONS S01144; B93427; A91194; A00868 REFERENCE S01144 !$#authors Laird, J.E.; Jack, L.; Hall, L.; Boulton, A.P.; Parker, D.; !1Craig, R.K. !$#journal Biochem. J. (1988) 254:85-94 !$#title Structure and expression of the guinea-pig alpha-lactalbumin !1gene. !$#cross-references MUID:89025693; PMID:2845947 !$#accession S01144 !'##molecule_type DNA !'##residues 1-142 ##label LAI !'##cross-references EMBL:Y00726; NID:g49426; PIDN:CAA68710.1; !1PID:g49427 REFERENCE A93427 !$#authors Hall, L.; Craig, R.K.; Edbrooke, M.R.; Campbell, P.N. !$#journal Nucleic Acids Res. (1982) 10:3503-3515 !$#title Comparison of the nucleotide sequence of cloned human and !1guinea-pig pre-alpha-lactalbumin cDNA with that of chick !1pre-lysozyme cDNA suggests evolution from a common ancestral !1gene. !$#cross-references MUID:82247223; PMID:6285305 !$#accession B93427 !'##molecule_type mRNA !'##residues 1-142,'RAPDVSANPALPIHPEPLFPHATPVYLFLPLNMICL' ##label HAL !'##cross-references GB:J00051; NID:g191281 !'##note the codon given for 81-Glu (GAC) is inconsistent with the !1authors' translation !'##note GenBank entry GPILACTAL, PID:g305338, shows codon TTC rather !1than the published TTG for 124-Leu !'##note the authors found 5 plasmids terminating at position 143 and !1one that did not; in vitro translation did not yield a !1larger than expected product REFERENCE A91194 !$#authors Brew, K. !$#journal Eur. J. Biochem. (1972) 27:341-353 !$#title The complete amino-acid sequence of guinea-pig !1alpha-lactalbumin. !$#cross-references MUID:72255347; PMID:5065784 !$#accession A91194 !'##molecule_type protein !'##residues 20-64,'N',66-75,'N',77-89,'D',91-100,'N',102,'N',104-105, !1'NN',108-120,'N',122-142 ##label BRE REFERENCE A67604 !$#authors Pike, A.C.W.; Brew, K.; Acharya, K.R. !$#submission submitted to the Brookhaven Protein Data Bank, June 1996 !$#cross-references PDB:1HFX !$#contents annotation; X-ray crystallography, 1.9 angstroms, residues !120-142 GENETICS !$#introns 45/1; 98/1; 123/2 FUNCTION !$#description as a regulatory subunit of lactose synthase, !1alpha-lactalbumin changes the substrate specificity of !1galactosyltransferase in the mammary gland, making glucose !1an acceptor rather than N-acetylglucosaminylpeptide !$#pathway lactose biosynthesis CLASSIFICATION #superfamily lysozyme c KEYWORDS calcium; glycosyltransferase; hexosyltransferase; lactose !1biosynthesis; mammary gland; milk FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-142 #product alpha-lactalbumin #status experimental !8#label MAT\ !$25-139,47-130, !$80-96,92-110 #disulfide_bonds #status experimental\ !$98,101,103,106,107 #binding_site calcium (Lys, Asp, Asp, Asp, Asp) !8#status predicted SUMMARY #length 142 #molecular-weight 16300 #checksum 8688 SEQUENCE /// ENTRY LART #type complete TITLE alpha-lactalbumin precursor - rat ALTERNATE_NAMES lactose synthase (EC 2.4.1.22) protein B ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 17-Dec-1982 #sequence_revision 25-Feb-1985 #text_change 16-Jun-2000 ACCESSIONS A93327; A93885; A00870; A00869 REFERENCE A93327 !$#authors Qasba, P.K.; Safaya, S.K. !$#journal Nature (1984) 308:377-380 !$#title Similarity of the nucleotide sequences of rat !1alpha-lactalbumin and chicken lysozyme genes. !$#cross-references MUID:84168126; PMID:6709045 !$#accession A93327 !'##molecule_type DNA !'##residues 1-159 ##label QAS !'##cross-references GB:X00461; NID:g56547; PIDN:CAA25150.1; PID:g297550 REFERENCE A93885 !$#authors Dandekar, A.M.; Qasba, P.K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:4853-4857 !$#title Rat alpha-lactalbumin has a 17-residue-long COOH-terminal !1hydrophobic extension as judged by sequence analysis of the !1cDNA clones. !$#cross-references MUID:82060152; PMID:6272279 !$#accession A93885 !'##molecule_type mRNA !'##residues 44-159 ##label DAN !'##cross-references GB:V01251; GB:J00702; NID:g56545; PIDN:CAA24564.1; !1PID:g1334301 REFERENCE A00870 !$#authors Prasad, R.V.; Butkowski, R.J.; Hamilton, J.W.; Ebner, K.E. !$#journal Biochemistry (1982) 21:1479-1482 !$#title Amino acid sequence of rat alpha-lactalbumin: a unique !1alpha-lactalbumin. !$#cross-references MUID:82206628; PMID:7044414 !$#accession A00870 !'##molecule_type protein !'##residues 20-37,'E',39,'V',41-42,'P',44-56,'TE',59,'S',61-62,'D', !164-77,'D',79-81,'ENQ',85,'V',87-120,'N',122-123,'L',125-152, !1'DG',155-159 ##label PRA GENETICS !$#introns 45/1; 98/1; 123/2 FUNCTION !$#description as a regulatory subunit of lactose synthase, !1alpha-lactalbumin changes the substrate specificity of !1galactosyltransferase in the mammary gland, making glucose !1an acceptor rather than N-acetylglucosaminylpeptide !$#pathway lactose biosynthesis CLASSIFICATION #superfamily lysozyme c KEYWORDS calcium; glycoprotein; glycosyltransferase; !1hexosyltransferase; lactose biosynthesis; mammary gland; !1milk FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-159 #product alpha-lactalbumin #status experimental !8#label MAT\ !$25-139,47-130, !$80-96,92-110 #disulfide_bonds #status predicted\ !$64 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 159 #molecular-weight 17850 #checksum 6317 SEQUENCE /// ENTRY LARB #type complete TITLE alpha-lactalbumin - rabbit ALTERNATE_NAMES lactose synthase (EC 2.4.1.22) protein B ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 30-Nov-1980 #sequence_revision 30-Nov-1980 #text_change 21-Nov-1997 ACCESSIONS A00871 REFERENCE A00871 !$#authors Hopp, T.P.; Woods, K.R. !$#journal Biochemistry (1979) 18:5182-5191 !$#title Primary structure of rabbit alpha-lactalbumin. !$#cross-references MUID:80043012; PMID:497176 !$#accession A00871 !'##molecule_type protein !'##residues 1-122 ##label HOP CLASSIFICATION #superfamily lysozyme c KEYWORDS calcium; glycoprotein; glycosyltransferase; !1hexosyltransferase; lactose biosynthesis; mammary gland; !1milk FEATURE !$6-120,28-111,61-77, !$73-91 #disulfide_bonds #status predicted\ !$45 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 122 #molecular-weight 14060 #checksum 2381 SEQUENCE /// ENTRY LAKGAW #type complete TITLE alpha-lactalbumin - red-necked wallaby ALTERNATE_NAMES lactose synthase (EC 2.4.1.22) protein B ORGANISM #formal_name Macropus rufogriseus #common_name red-necked wallaby DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 21-Nov-1997 ACCESSIONS A25251 REFERENCE A92476 !$#authors Shewale, J.G.; Sinha, S.K.; Brew, K. !$#journal J. Biol. Chem. (1984) 259:4947-4956 !$#title Evolution of alpha-lactalbumins. The complete amino acid !1sequence of the alpha-lactalbumin from a marsupial (Macropus !1rufogriseus) and corrections to regions of sequence in !1bovine and goat alpha-lactalbumins. !$#cross-references MUID:84185596; PMID:6715332 !$#accession A25251 !'##molecule_type protein !'##residues 1-121 ##label SHE CLASSIFICATION #superfamily lysozyme c KEYWORDS calcium; glycoprotein; glycosyltransferase; !1hexosyltransferase; lactose biosynthesis; mammary gland; !1milk FEATURE !$6-121,28-112,61-77, !$73-91 #disulfide_bonds #status predicted\ !$44 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 121 #molecular-weight 13784 #checksum 267 SEQUENCE /// ENTRY LZGSG #type complete TITLE lysozyme (EC 3.2.1.17) g [validated] - goose ALTERNATE_NAMES 1,4-beta-N-acetylmuramidase; peptidoglycan N-acetylmuramoylhydrolase ORGANISM #formal_name Anser anser #common_name domestic goose DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 15-Sep-2000 ACCESSIONS A00873 REFERENCE A90650 !$#authors Simpson, R.J.; Morgan, F.J. !$#journal Biochim. Biophys. Acta (1983) 744:349-351 !$#title Complete amino acid sequence of Embden goose (Anser anser) !1egg-white lysozyme. !$#accession A00873 !'##molecule_type protein !'##residues 1-185 ##label SIM !'##experimental_source Embden breed REFERENCE A52899 !$#authors Weaver, L.H.; Gruetter, M.G.; Matthews, B.W. !$#submission submitted to the Brookhaven Protein Data Bank, May 1994 !$#cross-references PDB:153L !$#contents annotation; X-ray crystallography, 1.60 angstroms, residues !11-185 REFERENCE A93306 !$#authors Grutter, M.G.; Weaver, L.H.; Matthews, B.W. !$#journal Nature (1983) 303:828-831 !$#title Goose lysozyme structure: an evolutionary link between hen !1and bacteriophage lysozymes? !$#cross-references MUID:83244971; PMID:6866082 !$#contents annotation; X-ray crystallography, 2.1 angstroms; active !1site; disulfide bonds FUNCTION !$#description catalyzes hydrolysis of the beta-1,4-glycosidic bond between !1N-acetylmuramic acid and N-acetylglucosamine in !1peptidoglycan and other complex polysaccharides !$#note shows a preference for N-acetylmuramic acid residues !1substituted with peptide; acts only as a glycanohydrolase CLASSIFICATION #superfamily lysozyme g KEYWORDS bacteriolytic enzyme; egg white; glycosidase; hydrolase; !1polysaccharide degradation FEATURE !$4-60,18-29 #disulfide_bonds #status experimental\ !$73,86 #active_site Glu, Asp #status predicted SUMMARY #length 185 #molecular-weight 20373 #checksum 5420 SEQUENCE /// ENTRY LZWSG #type complete TITLE lysozyme (EC 3.2.1.17) g [validated] - black swan ALTERNATE_NAMES 1,4-beta-N-acetylmuramidase; peptidoglycan N-acetylmuramoylhydrolase ORGANISM #formal_name Cygnus atratus #common_name black swan DATE 30-Nov-1980 #sequence_revision 30-Nov-1980 #text_change 20-Oct-2000 ACCESSIONS A00872; B34047 REFERENCE A00872 !$#authors Simpson, R.J.; Begg, G.S.; Dorow, D.S.; Morgan, F.J. !$#journal Biochemistry (1980) 19:1814-1819 !$#title Complete amino acid sequence of the goose-type lysozyme from !1the egg white of the black swan. !$#cross-references MUID:80198318; PMID:7378374 !$#accession A00872 !'##molecule_type protein !'##residues 1-185 ##label SIM REFERENCE A90157 !$#authors Jahnen, W.; Ward, L.D.; Reid, G.E.; Moritz, R.L.; Simpson, !1R.J. !$#journal Biochem. Biophys. Res. Commun. (1990) 166:139-145 !$#title Internal amino acid sequencing of proteins by in situ !1cyanogen bromide cleavage in polyacrylamide gels. !$#cross-references MUID:90147691; PMID:2302197 !$#accession B34047 !'##molecule_type protein !'##residues 'X',47-59,'X',61-68;95-99,'X',101-106,'X',108,'X',110-111 !1##label JA2 FUNCTION !$#description catalyzes hydrolysis of the beta-1,4-glycosidic bond between !1N-acetylmuramic acid and N-acetylglucosamine in !1peptidoglycan and other complex polysaccharides CLASSIFICATION #superfamily lysozyme g KEYWORDS bacteriolytic enzyme; egg white; glycosidase; hydrolase; !1polysaccharide degradation FEATURE !$4-60,18-29 #disulfide_bonds #status predicted\ !$73,86 #active_site Glu, Asp #status predicted SUMMARY #length 185 #molecular-weight 20400 #checksum 5363 SEQUENCE /// ENTRY LZOSG #type complete TITLE lysozyme (EC 3.2.1.17) g [validated] - ostrich ALTERNATE_NAMES 1,4-beta-N-acetylmuramidase; peptidoglycan N-acetylmuramoylhydrolase ORGANISM #formal_name Struthio camelus #common_name ostrich DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 20-Oct-2000 ACCESSIONS A00874; A61350 REFERENCE A00874 !$#authors Schoentgen, F.; Jolles, J.; Jolles, P. !$#journal Eur. J. Biochem. (1982) 123:489-497 !$#title Complete amino acid sequence of ostrich (Struthio camelus) !1egg-white lysozyme, a goose-type lysozyme. !$#cross-references MUID:82186721; PMID:7075596 !$#accession A00874 !'##molecule_type protein !'##residues 1-185 ##label SCH REFERENCE A61350 !$#authors Jolles, J.; Perin, J.P.; Jolles, P. !$#journal Mol. Cell. Biochem. (1977) 17:39-44 !$#title The ostrich (Struthio camelus) egg-white lysozyme. !$#cross-references MUID:78010132; PMID:904618 !$#accession A61350 !'##molecule_type protein !'##residues 1-32,'X',34 ##label JOL COMMENT This g (goose) type lysozyme differs from c (chicken) type !1lysozymes in its larger molecular weight, its sequence, and !1its insensitivity to inhibition by N-acetylglucosamine. FUNCTION !$#description catalyzes hydrolysis of the beta-1,4-glycosidic bond between !1N-acetylmuramic acid and N-acetylglucosamine in !1peptidoglycan and other complex polysaccharides CLASSIFICATION #superfamily lysozyme g KEYWORDS bacteriolytic enzyme; egg white; glycosidase; hydrolase FEATURE !$4-60,18-29 #disulfide_bonds #status predicted\ !$73,86 #active_site Glu, Asp #status predicted SUMMARY #length 185 #molecular-weight 20563 #checksum 5266 SEQUENCE /// ENTRY A59351 #type complete TITLE lysozyme (EC 3.2.1.17) g [validated] - double-wattled cassowary ALTERNATE_NAMES 1,4-beta-N-acetylmuramidase; peptidoglycan N-acetylmuramoylhydrolase ORGANISM #formal_name Casuarius casuarius #common_name double-wattled cassowary, Australian cassowary DATE 20-Oct-2000 #sequence_revision 20-Oct-2000 #text_change 20-Oct-2000 ACCESSIONS A59351 REFERENCE A59351 !$#authors Thammasirirak, S.; Torikata, T.; Takami, K.; Murata, K.; !1Araki, T. !$#submission submitted to the Protein Sequence Database, October 2000 !$#description Complete amino acid sequence of Cassowary (Casuarius !1casuarius) goose type lysozyme. !$#accession A59351 !'##status preliminary !'##molecule_type protein !'##residues 1-185 ##label THA FUNCTION !$#description catalyzes hydrolysis of the beta-1,4-glycosidic bond between !1N-acetylmuramic acid and N-acetylglucosamine in !1peptidoglycan and other complex polysaccharides CLASSIFICATION #superfamily lysozyme g KEYWORDS bacteriolytic enzyme; egg white; glycosidase; hydrolase; !1polysaccharide degradation; pyroglutamic acid FEATURE !$1 #modified_site pyrrolidone carboxylic acid (Gln) !8#status experimental\ !$4-60,18-29 #disulfide_bonds #status predicted\ !$73,86 #active_site Glu, Asp #status predicted SUMMARY #length 185 #molecular-weight 20426 #checksum 6860 SEQUENCE /// ENTRY G5BPT4 #type complete TITLE lysozyme (EC 3.2.1.17), tail-associated - phage T4 ALTERNATE_NAMES gene 5 protein; gene 50.2 protein ORGANISM #formal_name phage T4 DATE 30-Sep-1991 #sequence_revision 31-Mar-1993 #text_change 18-Jun-1999 ACCESSIONS S25240; PS0060; JF0061; S10108 REFERENCE S25239 !$#authors Mosig, G.; Lin, G.W.; Franklin, J.; Fan, W.H. !$#journal New Biol. (1989) 1:171-179 !$#title Functional relationships and structural determinants of two !1bacteriophage T4 lysozymes: a soluble (gene e) and a !1baseplate-associated (gene 5) protein. !$#cross-references MUID:91190815; PMID:2488704 !$#accession S25240 !'##molecule_type DNA !'##residues 1-575 ##label MOS !'##cross-references GB:X15728; NID:g15224; PIDN:CAA33749.1; PID:g15227 REFERENCE S04608 !$#authors Koch, T.; Lamm, N.; Rueger, W. !$#journal Nucleic Acids Res. (1989) 17:4392 !$#title Sequencing, cloning and overexpression of genes of !1bacteriophage T4 between map positions 74.325 and 77.184. !$#cross-references MUID:89296504; PMID:2740234 !$#accession PS0060 !'##status translation not shown !'##molecule_type DNA !'##residues 1-64 ##label KOC !'##cross-references EMBL:X14845 GENETICS !$#gene 5 !$#map_position 77.0-78.6 FUNCTION !$#description catalyzes hydrolysis of the beta-1,4-glycosidic bond between !1N-acetylmuramic acid and N-acetylglucosamine in !1peptidoglycan and other complex polysaccharides CLASSIFICATION #superfamily phage T4 gene 5 protein; phage T4 lysozyme !1homology KEYWORDS glycosidase; host cell lysis; hydrolase; late protein FEATURE !$184-323 #domain phage T4 lysozyme homology #label T4L\ !$184,193 #active_site Glu, Asp #status predicted SUMMARY #length 575 #molecular-weight 63116 #checksum 3948 SEQUENCE /// ENTRY LZBPT4 #type complete TITLE lysozyme (EC 3.2.1.17) [validated] - phage T4 ALTERNATE_NAMES endolysin; muramidase ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 15-Sep-2000 ACCESSIONS A92896; A92061; A00875 REFERENCE A92896 !$#authors Owen, J.E.; Schultz, D.W.; Taylor, A.; Smith, G.R. !$#journal J. Mol. Biol. (1983) 165:229-248 !$#title Nucleotide sequence of the lysozyme gene of bacteriophage !1T4. Analysis of mutations involving repeated sequences. !$#cross-references MUID:83189145; PMID:6302287 !$#accession A92896 !'##molecule_type DNA !'##residues 1-164 ##label OWE REFERENCE A92061 !$#authors Inouye, M.; Imada, M.; Tsugita, A. !$#journal J. Biol. Chem. (1970) 245:3479-3484 !$#title The amino acid sequence of T4 phage lysozyme. IV. Dilute !1acid hydrolysis and the order of tryptic peptides. !$#cross-references MUID:71007898; PMID:5470817 !$#accession A92061 !'##molecule_type protein !'##residues 1-164 ##label INO REFERENCE A50487 !$#authors Weaver, L.H.; Matthews, B.W. !$#submission submitted to the Brookhaven Protein Data Bank, August 1986 !$#cross-references PDB:2LZM !$#contents annotation; X-ray crystallography, 1.7 angstroms, residues !11-164 REFERENCE A58441 !$#authors Weaver, L.H.; Matthews, B.W. !$#journal J. Mol. Biol. (1987) 193:189-199 !$#title Structure of bacteriophage T4 lysozyme refined at 1.7 !1angstroms resolution. !$#cross-references MUID:87226186; PMID:3586019 !$#contents annotation; X-ray crystallography, 1.7 angstroms, residues !11-164 REFERENCE A90204 !$#authors Remington, S.J.; Ten Eyck, L.F.; Matthews, B.W. !$#journal Biochem. Biophys. Res. Commun. (1977) 75:265-270 !$#title Atomic coordinates for T4 phage lysozyme. !$#cross-references MUID:77157239; PMID:322662 !$#contents annotation; X-ray crystallography, 2.4 angstroms REFERENCE A93791 !$#authors Matthews, B.W.; Remington, S.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1974) 71:4178-4182 !$#title The three dimensional structure of the lysozyme from !1bacteriophge T4. !$#cross-references MUID:75046782; PMID:4530293 !$#contents annotation; X-ray crystallography, 2.5 angstroms FUNCTION !$#description catalyzes hydrolysis of the beta-1,4-glycosidic bond between !1N-acetylmuramic acid and N-acetylglucosamine in !1peptidoglycan and other complex polysaccharides !$#note assists in releasing phage particles by breaking down cell !1wall peptidoglycan CLASSIFICATION #superfamily phage T4 lysozyme; phage T4 lysozyme homology KEYWORDS glycosidase; host cell lysis; hydrolase; late protein; !1polysaccharide degradation FEATURE !$11-145 #domain phage T4 lysozyme homology #label T4L\ !$11,20 #active_site Glu, Asp #status predicted SUMMARY #length 164 #molecular-weight 18635 #checksum 8797 SEQUENCE /// ENTRY WMBPP9 #type complete TITLE lysozyme (EC 3.2.1.17) - phage phi-29 ALTERNATE_NAMES morphogenesis protein 2 ORGANISM #formal_name phage phi-29 #note host Bacillus amyloliquefaciens; Bacillus subtilis DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 18-Jun-1999 ACCESSIONS B24721; A33078 REFERENCE A24721 !$#authors Garvey, K.J.; Saedi, M.S.; Ito, J. !$#journal Nucleic Acids Res. (1986) 14:10001-10008 !$#title Nucleotide sequence of Bacillus phage phi-29 genes 14 and !115: homology of gene 15 with other phage lysozymes. !$#cross-references MUID:87117505; PMID:3027653 !$#accession B24721 !'##molecule_type DNA !'##residues 1-258 ##label GAR !'##cross-references GB:X04962; NID:g15676; PIDN:CAA28632.1; PID:g15679 REFERENCE A25816 !$#authors Vlcek, C.; Paces, V. !$#journal Gene (1986) 46:215-225 !$#title Nucleotide sequence of the late region of Bacillus phage !1phi-29 completes the 19285-bp sequence of phi-29 genome. !1Comparison with the homologous sequence of phage PZA. !$#cross-references MUID:87106857; PMID:3803926 !$#accession A33078 !'##molecule_type DNA !'##residues 1-258 ##label VLC !'##cross-references GB:M14782; NID:g215323; PIDN:AAA32288.1; !1PID:g215333 GENETICS !$#gene 15 FUNCTION !$#description catalyzes hydrolysis of the beta-1,4-glycosidic bond between !1N-acetylmuramic acid and N-acetylglucosamine in !1peptidoglycan and other complex polysaccharides CLASSIFICATION #superfamily phage T4 lysozyme; phage T4 lysozyme homology KEYWORDS glycosidase; host cell lysis; hydrolase; late protein FEATURE !$15-134 #domain phage T4 lysozyme homology #label T4L SUMMARY #length 258 #molecular-weight 28054 #checksum 5010 SEQUENCE /// ENTRY WMBP15 #type complete TITLE lysozyme (EC 3.2.1.17) - phage PZA ORGANISM #formal_name phage PZA #note host Bacillus subtilis DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 18-Jun-1999 ACCESSIONS A26215; J24831 REFERENCE A91550 !$#authors Paces, V.; Vlcek, C.; Urbanek, P. !$#journal Gene (1986) 44:107-114 !$#title Nucleotide sequence of the late region of Bacillus subtilis !1phage PZA, a close relative of phi-29. !$#cross-references MUID:87031573; PMID:3095188 !$#accession A26215 !'##molecule_type DNA !'##residues 1-258 ##label PAC !'##cross-references GB:M11813; GB:M13904; GB:M13905; NID:g216046; !1PIDN:AAA88492.1; PID:g216064 GENETICS !$#gene 15 FUNCTION !$#description catalyzes hydrolysis of the beta-1,4-glycosidic bond between !1N-acetylmuramic acid and N-acetylglucosamine in !1peptidoglycan and other complex polysaccharides CLASSIFICATION #superfamily phage T4 lysozyme; phage T4 lysozyme homology KEYWORDS glycosidase; host cell lysis; hydrolase; late protein FEATURE !$15-134 #domain phage T4 lysozyme homology #label T4L SUMMARY #length 258 #molecular-weight 28052 #checksum 5326 SEQUENCE /// ENTRY LZBP22 #type complete TITLE lysozyme (EC 3.2.1.17) - phage P22 ALTERNATE_NAMES gene 19 protein ORGANISM #formal_name phage P22 DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 18-Jun-1999 ACCESSIONS S22904; S23051 REFERENCE S22903 !$#authors Rennell, D.; Poteete, A.R. !$#journal Virology (1985) 143:280-289 !$#title Phage P22 lysis genes: nucleotide sequences and functional !1relationships with T4 and lambda genes. !$#cross-references MUID:86045883; PMID:2998005 !$#accession S22904 !'##molecule_type DNA !'##residues 1-146 ##label REN !'##cross-references EMBL:M10997; NID:g215262; PIDN:AAA32266.1; !1PID:g215264 !$#accession S23051 !'##molecule_type protein !'##residues 2-34 ##label RE2 GENETICS !$#gene 19 FUNCTION !$#description catalyzes hydrolysis of the beta-1,4-glycosidic bond between !1N-acetylmuramic acid and N-acetylglucosamine in !1peptidoglycan and other complex polysaccharides CLASSIFICATION #superfamily phage T4 lysozyme; phage T4 lysozyme homology KEYWORDS glycosidase; host cell lysis; hydrolase; late protein FEATURE !$2-146 #product lysozyme #status experimental #label MAT\ !$16-136 #domain phage T4 lysozyme homology #label T4L\ !$16,25 #active_site Glu, Asp #status predicted SUMMARY #length 146 #molecular-weight 16138 #checksum 4060 SEQUENCE /// ENTRY WMBPP2 #type complete TITLE lysozyme (EC 3.2.1.17) - phage PA2 ORGANISM #formal_name phage PA2 #note host Escherichia coli DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 18-Jun-1999 ACCESSIONS C25647 REFERENCE A25647 !$#authors Blasband, A.J.; Marcotte Jr., W.R.; Schnaitman, C.A. !$#journal J. Biol. Chem. (1986) 261:12723-12732 !$#title Structure of the lc and nmpC outer membrane porin protein !1genes of lambdoid bacteriophage. !$#cross-references MUID:86304457; PMID:3017988 !$#accession C25647 !'##molecule_type DNA !'##residues 1-165 ##label BLA !'##cross-references GB:J02580; NID:g215366; PIDN:AAA32300.1; !1PID:g215368 FUNCTION !$#description catalyzes hydrolysis of the beta-1,4-glycosidic bond between !1N-acetylmuramic acid and N-acetylglucosamine in !1peptidoglycan and other complex polysaccharides CLASSIFICATION #superfamily phage T4 lysozyme; phage T4 lysozyme homology KEYWORDS glycosidase; host cell lysis; hydrolase; late protein FEATURE !$35-152 #domain phage T4 lysozyme homology #label T4L\ !$35,44 #active_site Glu, Asp #status predicted SUMMARY #length 165 #molecular-weight 17998 #checksum 5761 SEQUENCE /// ENTRY LZBP21 #type complete TITLE lysozyme (EC 3.2.1.17) - phage 21 ALTERNATE_NAMES gene R protein ORGANISM #formal_name phage 21 DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 18-Jun-1999 ACCESSIONS S22906 REFERENCE S22905 !$#authors Bonovich, M.T.; Young, R. !$#journal J. Bacteriol. (1991) 173:2897-2905 !$#title Dual start motif in two lambdoid S genes unrelated to lambda !1S. !$#cross-references MUID:91210180; PMID:2019562 !$#accession S22906 !'##molecule_type DNA !'##residues 1-165 ##label BON !'##cross-references EMBL:M65239; NID:g215466; PIDN:AAA32350.1; !1PID:g215468 GENETICS !$#gene R FUNCTION !$#description catalyzes hydrolysis of the beta-1,4-glycosidic bond between !1N-acetylmuramic acid and N-acetylglucosamine in !1peptidoglycan and other complex polysaccharides CLASSIFICATION #superfamily phage T4 lysozyme; phage T4 lysozyme homology KEYWORDS glycosidase; host cell lysis; hydrolase; late protein FEATURE !$35-152 #domain phage T4 lysozyme homology #label T4L\ !$35,44 #active_site Glu, Asp #status predicted SUMMARY #length 165 #molecular-weight 17996 #checksum 4027 SEQUENCE /// ENTRY MUKAD #type complete TITLE lysozyme (EC 3.2.1.17) - fungus (Chalara sp.) ALTERNATE_NAMES lysozyme Ch; N,O-diacetylmuramidase ORGANISM #formal_name Chalara sp. DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 09-Apr-1998 ACCESSIONS A00876 REFERENCE A92178 !$#authors Felch, J.W.; Inagami, T.; Hash, J.H. !$#journal J. Biol. Chem. (1975) 250:3713-3720 !$#title The N,O-diacetylmuramidase of Chalaropsis species. V. The !1complete amino acid sequence. !$#cross-references MUID:75151523; PMID:1168638 !$#accession A00876 !'##molecule_type protein !'##residues 1-211 ##label FEL !'##note this is the final paper in a series REFERENCE A92236 !$#authors Fouche, P.B.; Hash, J.H. !$#journal J. Biol. Chem. (1978) 253:6787-6793 !$#title The N,O-diacetylmuramidase of Chalaropsis species. !1Identification of aspartyl and glutamyl residues in the !1active site. !$#cross-references MUID:79005662; PMID:567645 !$#contents annotation; active site COMMENT This extracellular enzyme has both lysozyme !1(acetylmuramidase) and diacetylmuramidase activities. FUNCTION !$#description catalyzes hydrolysis of the beta-1,4-glycosidic bond between !1N-acetylmuramic acid and N-acetylglucosamine in !1peptidoglycan and other complex polysaccharides CLASSIFICATION #superfamily Chalara lysozyme; Chalara lysozyme homology KEYWORDS extracellular protein; glycosidase; hydrolase FEATURE !$6-170 #domain Chalara lysozyme homology #label CHL\ !$6,33 #active_site Asp, Glu #status experimental\ !$108-147 #disulfide_bonds #status experimental SUMMARY #length 211 #molecular-weight 22413 #checksum 1762 SEQUENCE /// ENTRY MUSMM1 #type complete TITLE lysozyme (EC 3.2.1.17) M1 precursor - Streptomyces globisporus ALTERNATE_NAMES N-acetylmuramidase ORGANISM #formal_name Streptomyces globisporus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 18-Jun-1999 ACCESSIONS JQ0529 REFERENCE JQ0529 !$#authors Lichenstein, H.S.; Hastings, A.E.; Langley, K.E.; Mendiaz, !1E.A.; Rohde, M.F.; Elmore, R.; Zukowski, M.M. !$#journal Gene (1990) 88:81-86 !$#title Cloning and nucleotide sequence of the N-acetylmuramidase !1M1-encoding gene from Streptomyces globisporus. !$#cross-references MUID:90255972; PMID:2341041 !$#accession JQ0529 !'##molecule_type DNA !'##residues 1-294 ##label LIC !'##cross-references GB:M30645; NID:g153139; PIDN:AAA26687.1; !1PID:g153140 !'##experimental_source strain ATCC 21553 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing COMMENT This extracellular enzyme has both lysozyme !1(acetylmuramidase) and diacetylmuramidase activities. GENETICS !$#gene acm FUNCTION !$#description catalyzes hydrolysis of the beta-1,4-glycosidic bond between !1N-acetylmuramic acid and N-acetylglucosamine in !1peptidoglycan and other complex polysaccharides CLASSIFICATION #superfamily Chalara lysozyme; Chalara lysozyme homology KEYWORDS extracellular protein; glycosidase; hydrolase FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-77 #domain propeptide #status predicted #label PRO\ !$78-294 #product lysozyme M1 #status experimental #label MAT\ !$86-247 #domain Chalara lysozyme homology #label CHL\ !$86,113 #active_site Asp, Glu #status predicted\ !$185-224 #disulfide_bonds #status experimental SUMMARY #length 294 #molecular-weight 31168 #checksum 8317 SEQUENCE /// ENTRY MUBPM1 #type complete TITLE lysozyme (EC 3.2.1.17) - Lactobacillus delbrueckii subsp. bulgaricus phage mv1 ALTERNATE_NAMES endolysin; muramidase ORGANISM #formal_name Lactobacillus delbrueckii subsp. bulgaricus phage mv1 #note host Lactobacillus delbrueckii subsp. bulgaricus DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 09-Apr-1998 ACCESSIONS JQ0789 REFERENCE JQ0789 !$#authors Boizet, B.; Lahbib-Mansais, Y.; Dupont, L.; Ritzenthaler, !1P.; Mata, M. !$#journal Gene (1990) 94:61-67 !$#title Cloning, expression and sequence analysis of an !1endolysin-encoding gene of Lactobacillus bulgaricus !1bacteriophage mv1. !$#cross-references MUID:91033066; PMID:2227453 !$#accession JQ0789 !'##molecule_type DNA !'##residues 1-195 ##label BOI !'##cross-references GB:M35235 COMMENT This enzyme helps to release the mature phage particles from !1the cell wall by breaking down the peptidoglycan. GENETICS !$#gene lysA FUNCTION !$#description catalyzes hydrolysis of the beta-1,4-glycosidic bond between !1N-acetylmuramic acid and N-acetylglucosamine in !1peptidoglycan and other complex polysaccharides CLASSIFICATION #superfamily Chalara lysozyme; Chalara lysozyme homology KEYWORDS glycosidase; hydrolase FEATURE !$8-167 #domain Chalara lysozyme homology #label CHL\ !$8,34 #active_site Asp, Glu #status predicted SUMMARY #length 195 #molecular-weight 21119 #checksum 8327 SEQUENCE /// ENTRY LYBPD1 #type complete TITLE lytic enzyme (EC 3.-.-.-) - phage PRD1 ALTERNATE_NAMES protein P15 ORGANISM #formal_name phage PRD1 #note host Salmonella typhimurium; Escherichia coli DATE 31-Dec-1990 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS S03568; C27328 REFERENCE S03568 !$#authors Pakula, T.M.; Savilahti, H.; Bamford, D.H. !$#journal Eur. J. Biochem. (1989) 180:149-152 !$#title Comparison of the amino acid sequence of the lytic enzyme !1from broad-host-range bacteriophage PRD1 with sequences of !1other cell-wall-peptidoglycan lytic enzymes. !$#cross-references MUID:89210844; PMID:2651121 !$#accession S03568 !'##molecule_type DNA !'##residues 1-149 ##label PAK !'##cross-references GB:X14980; NID:g15802; PIDN:CAA33104.1; PID:g15803 REFERENCE A27328 !$#authors Savilahti, H.; Bamford, D.H. !$#journal Gene (1987) 57:121-130 !$#title The complete nucleotide sequence of the left very early !1region of Escherichia coli bacteriophage PRD1 coding for the !1terminal protein and the DNA polymerase. !$#cross-references MUID:88112855; PMID:3322943 !$#accession C27328 !'##molecule_type DNA !'##residues 1-98 ##label SAV !'##cross-references GB:M22161; NID:g215750; PIDN:AAA32451.1; !1PID:g553022 GENETICS !$#gene XV CLASSIFICATION #superfamily phage PRD1 lytic enzyme KEYWORDS host cell lysis; hydrolase SUMMARY #length 149 #molecular-weight 17269 #checksum 9764 SEQUENCE /// ENTRY QQECW1 #type complete TITLE soluble lytic transglycosylase (EC 3.2.1.-) precursor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 05-Apr-1983 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS S56616; G65254; A41332; A93698; A93867; A04435 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56616 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-654 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97288.1; !1PID:g537232 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65254 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-654 ##label BLAT !'##cross-references GB:AE000509; GB:U00096; NID:g2367383; !1PIDN:AAC77345.1; PID:g1790853; UWGP:b4392 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A41332 !$#authors Engel, H.; Kazemier, B.; Keck, W. !$#journal J. Bacteriol. (1991) 173:6773-6782 !$#title Murein-metabolizing enzymes from Escherichia coli: sequence !1analysis and controlled overexpression of the slt gene, !1which encodes the soluble lytic transglycosylase. !$#cross-references MUID:92041559; PMID:1938883 !$#accession A41332 !'##molecule_type DNA !'##residues 'M',11-591,'L',593-654 ##label ENG !'##cross-references GB:M69185; NID:g147835; PIDN:AAA24634.1; !1PID:g147836 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE A93698 !$#authors Singleton, C.K.; Roeder, W.D.; Bogosian, G.; Somerville, !1R.L.; Weith, H.L. !$#journal Nucleic Acids Res. (1980) 8:1551-1560 !$#title DNA sequence of the Escherichia coli trpR gene and !1prediction of the amino acid sequence of Trp repressor. !$#cross-references MUID:81053831; PMID:7001368 !$#accession A93698 !'##molecule_type DNA !'##residues 558-591,'L',593-648 ##label SIN !'##cross-references GB:J01715 REFERENCE A93867 !$#authors Gunsalus, R.P.; Yanofsky, C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1980) 77:7117-7121 !$#title Nucleotide sequence and expression of Escherichia coli trpR, !1the structural gene for the trp aporepressor. !$#cross-references MUID:81175101; PMID:7012834 !$#accession A93867 !'##molecule_type DNA !'##residues 649-654 ##label GUN !'##cross-references GB:J01715 GENETICS !$#gene slt !$#map_position 100 min !$#start_codon GTG CLASSIFICATION #superfamily soluble lytic transglycosylase KEYWORDS cell wall synthesis; glycosidase; hydrolase FEATURE !$1-36 #domain signal sequence #status predicted #label SIG\ !$37-654 #product soluble lytic transglycosylase #status !8experimental #label MAT SUMMARY #length 654 #molecular-weight 74407 #checksum 2375 SEQUENCE /// ENTRY HNNZS #type complete TITLE hemagglutinin-neuraminidase (EC 3.2.1.-) - Sendai virus ORGANISM #formal_name Sendai virus DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 18-Jun-1999 ACCESSIONS A00877 REFERENCE A00877 !$#authors Blumberg, B.; Giorgi, C.; Roux, L.; Raju, R.; Dowling, P.; !1Chollet, A.; Kolakofsky, D. !$#journal Cell (1985) 41:269-278 !$#title Sequence determination of the Sendai virus HN gene and its !1comparison to the influenza virus glycoproteins. !$#cross-references MUID:85201677; PMID:2986845 !$#accession A00877 !'##molecule_type genomic RNA !'##residues 1-576 ##label BLU !'##cross-references GB:M12397; NID:g334933; PIDN:AAA47810.1; !1PID:g334934 GENETICS !$#gene HN CLASSIFICATION #superfamily paramyxovirus hemagglutinin-neuraminidase KEYWORDS glycoprotein; glycosidase; hemagglutinin; hydrolase; !1transmembrane protein FEATURE !$36-60 #domain transmembrane #status predicted #label TRM\ !$77,448,499,504,511 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 576 #molecular-weight 63515 #checksum 3229 SEQUENCE /// ENTRY HNNZSZ #type complete TITLE hemagglutinin-neuraminidase (EC 3.2.1.-) - Sendai virus (strain Z) ORGANISM #formal_name Sendai virus DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 18-Jun-1999 ACCESSIONS A00878 REFERENCE A00878 !$#authors Shioda, T.; Iwasaki, K.; Shibuta, H. !$#journal Nucleic Acids Res. (1986) 14:1545-1563 !$#title Determination of the complete nucleotide sequence of the !1Sendai virus genome RNA and the predicted amino acid !1sequences of the F, HN and L proteins. !$#cross-references MUID:86148492; PMID:3005975 !$#accession A00878 !'##molecule_type genomic RNA !'##residues 1-575 ##label SHI !'##cross-references GB:X03614; NID:g60898; PIDN:CAA27274.1; PID:g60902 GENETICS !$#gene HN CLASSIFICATION #superfamily paramyxovirus hemagglutinin-neuraminidase KEYWORDS glycoprotein; glycosidase; hemagglutinin; hydrolase; !1transmembrane protein FEATURE !$36-60 #domain transmembrane #status predicted #label TRM\ !$77,448,499,504,511 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 575 #molecular-weight 63409 #checksum 1806 SEQUENCE /// ENTRY HNNZSH #type complete TITLE hemagglutinin-neuraminidase (EC 3.2.1.-) - Sendai virus (strain HVJ) ORGANISM #formal_name Sendai virus DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 18-Jun-1999 ACCESSIONS A24004 REFERENCE A24004 !$#authors Miura, N.; Nakatani, Y.; Ishiura, M.; Uchida, T.; Okada, Y. !$#journal FEBS Lett. (1985) 188:112-116 !$#title Molecular cloning of a full-length cDNA encoding the !1hemagglutinin-neuraminidase glycoprotein of Sendai virus. !$#cross-references MUID:85258120; PMID:2991016 !$#accession A24004 !'##molecule_type genomic RNA !'##residues 1-575 ##label MIU !'##cross-references GB:X02808; NID:g61002; PIDN:CAA26576.1; PID:g61003 !'##note the authors translated the codon TAT for residue 389 as Thr GENETICS !$#gene HN CLASSIFICATION #superfamily paramyxovirus hemagglutinin-neuraminidase KEYWORDS glycoprotein; glycosidase; hemagglutinin; hydrolase; !1transmembrane protein FEATURE !$36-60 #domain transmembrane #status predicted #label TRM\ !$77,448,499,504,511 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 575 #molecular-weight 63433 #checksum 2471 SEQUENCE /// ENTRY HNNZ39 #type complete TITLE hemagglutinin-neuraminidase (EC 3.2.1.-) - Sendai virus (strain C39) ORGANISM #formal_name Sendai virus DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 15-Oct-1996 ACCESSIONS A34682 REFERENCE A34682 !$#authors Gorman, W.L.; Gill, D.S.; Scroggs, R.A.; Portner, A. !$#journal Virology (1990) 175:211-221 !$#title The hemagglutinin-neuraminidase glycoproteins of human !1parainfluenza virus type 1 and Sendai virus have high !1structure-function similarity with limited antigenic !1cross-reactivity. !$#cross-references MUID:90177217; PMID:1689918 !$#accession A34682 !'##molecule_type mRNA !'##residues 1-575 ##label GOR !'##experimental_source ATCC VR-94 GENETICS !$#gene HN CLASSIFICATION #superfamily paramyxovirus hemagglutinin-neuraminidase KEYWORDS glycoprotein; glycosidase; hemagglutinin; hydrolase; !1transmembrane protein FEATURE !$35-56 #domain transmembrane #status predicted #label TMN\ !$8,19,77,173,277, !$361,499,504,511,551 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 575 #molecular-weight 63937 #checksum 6688 SEQUENCE /// ENTRY HNNZB3 #type complete TITLE hemagglutinin-neuraminidase (EC 3.2.1.-) - parainfluenza virus type 3 ORGANISM #formal_name parainfluenza virus type 3 DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 18-Jun-1999 ACCESSIONS B27218 REFERENCE A93659 !$#authors Suzu, S.; Sakai, Y.; Shioda, T.; Shibuta, H. !$#journal Nucleic Acids Res. (1987) 15:2945-2958 !$#title Nucleotide sequence of the bovine parainfluenza 3 virus !1genome: the genes of the F and HN glycoproteins. !$#cross-references MUID:87174819; PMID:3031615 !$#accession B27218 !'##molecule_type genomic RNA !'##residues 1-572 ##label SUZ !'##cross-references EMBL:Y00114; NID:g60891; PIDN:CAA68298.1; !1PID:g60897 GENETICS !$#gene HN CLASSIFICATION #superfamily paramyxovirus hemagglutinin-neuraminidase KEYWORDS glycoprotein; glycosidase; hemagglutinin; hydrolase; !1transmembrane protein FEATURE !$40-56 #domain transmembrane #status predicted #label TMN\ !$8,163,485,570 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 572 #molecular-weight 64590 #checksum 3227 SEQUENCE /// ENTRY HNNZP3 #type complete TITLE hemagglutinin-neuraminidase (EC 3.2.1.-) - parainfluenza virus type 3 (strain 47885) ORGANISM #formal_name parainfluenza virus type 3 #note host Homo sapiens (man) DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 01-Dec-2000 ACCESSIONS A27765; A46451 REFERENCE A27765 !$#authors Elango, N.; Coligan, J.E.; Jambou, R.C.; Venkatesan, S. !$#journal J. Virol. (1986) 57:481-489 !$#title Human parainfluenza type 3 virus hemagglutinin-neuraminidase !1glycoprotein: nucleotide sequence of mRNA and limited amino !1acid sequence of the purified protein. !$#cross-references MUID:86115395; PMID:3003381 !$#accession A27765 !'##molecule_type mRNA !'##residues 1-572 ##label ELA !'##cross-references GB:M17641; NID:g332704; PIDN:AAA46846.1; !1PID:g332705 REFERENCE A46451 !$#authors Storey, D.G.; Cote, M.J.; Dimock, K.; Kang, C.Y. !$#journal Intervirology (1987) 27:69-80 !$#title Nucleotide sequence of the coding and flanking regions of !1the human parainfluenza virus 3 hemagglutinin - !1neuraminidase gene: comparison with other paramyxoviruses. !$#cross-references MUID:88032139; PMID:2822598 !$#accession A46451 !'##status preliminary !'##molecule_type mRNA !'##residues 1-488,'G',490-511,'A',513-572 ##label STO !'##cross-references GB:M20402; NID:g332720; PIDN:AAA46856.1; !1PID:g332721 GENETICS !$#gene HN CLASSIFICATION #superfamily paramyxovirus hemagglutinin-neuraminidase KEYWORDS glycoprotein; glycosidase; hemagglutinin; hydrolase; !1transmembrane protein FEATURE !$32-53 #domain transmembrane #status predicted #label TRM\ !$308,351,485,523 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 572 #molecular-weight 64247 #checksum 2479 SEQUENCE /// ENTRY HNNZ73 #type complete TITLE hemagglutinin-neuraminidase (EC 3.2.1.-) - parainfluenza virus type 3 (strain Wash/1511/73) ORGANISM #formal_name parainfluenza virus type 3 #note host Homo sapiens (man) DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 18-Jun-1999 ACCESSIONS A29970 REFERENCE A94369 !$#authors van Wyke Coelingh, K.L.; Winter, C.C.; Murphy, B.R. !$#journal Virology (1988) 162:137-143 !$#title Nucleotide and deduced amino acid sequence of !1hemagglutinin-neuraminidase genes of human type 3 !1parainfluenza viruses isolated from 1957 to 1983. !$#cross-references MUID:88101361; PMID:2827373 !$#accession A29970 !'##molecule_type genomic RNA !'##residues 1-572 ##label VAN !'##cross-references GB:M18759; NID:g332700; PIDN:AAA46844.1; !1PID:g332701 GENETICS !$#gene HN CLASSIFICATION #superfamily paramyxovirus hemagglutinin-neuraminidase KEYWORDS glycoprotein; glycosidase; hemagglutinin; hydrolase; !1transmembrane protein FEATURE !$32-53 #domain transmembrane #status predicted #label TMN\ !$308,351,485,523 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 572 #molecular-weight 64315 #checksum 2905 SEQUENCE /// ENTRY HNNZ74 #type complete TITLE hemagglutinin-neuraminidase (EC 3.2.1.-) - parainfluenza virus type 3 (strain Aus/124854/74) ORGANISM #formal_name parainfluenza virus type 3 #note host Homo sapiens (man) DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 18-Jun-1999 ACCESSIONS B29970 REFERENCE A94369 !$#authors van Wyke Coelingh, K.L.; Winter, C.C.; Murphy, B.R. !$#journal Virology (1988) 162:137-143 !$#title Nucleotide and deduced amino acid sequence of !1hemagglutinin-neuraminidase genes of human type 3 !1parainfluenza viruses isolated from 1957 to 1983. !$#cross-references MUID:88101361; PMID:2827373 !$#accession B29970 !'##molecule_type genomic RNA !'##residues 1-572 ##label VAN !'##cross-references GB:M18760; NID:g332706; PIDN:AAA46847.1; !1PID:g332707 GENETICS !$#gene HN CLASSIFICATION #superfamily paramyxovirus hemagglutinin-neuraminidase KEYWORDS glycoprotein; glycosidase; hemagglutinin; hydrolase; !1transmembrane protein FEATURE !$32-53 #domain transmembrane #status predicted #label TMN\ !$308,351,485,523 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 572 #molecular-weight 64233 #checksum 885 SEQUENCE /// ENTRY HNNZ79 #type complete TITLE hemagglutinin-neuraminidase (EC 3.2.1.-) - parainfluenza virus type 3 (strain Wash/641/79) ORGANISM #formal_name parainfluenza virus type 3 #note host Homo sapiens (man) DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 18-Jun-1999 ACCESSIONS C29970 REFERENCE A94369 !$#authors van Wyke Coelingh, K.L.; Winter, C.C.; Murphy, B.R. !$#journal Virology (1988) 162:137-143 !$#title Nucleotide and deduced amino acid sequence of !1hemagglutinin-neuraminidase genes of human type 3 !1parainfluenza viruses isolated from 1957 to 1983. !$#cross-references MUID:88101361; PMID:2827373 !$#accession C29970 !'##molecule_type genomic RNA !'##residues 1-572 ##label VAN !'##cross-references GB:M18761; NID:g332708; PIDN:AAA46848.1; !1PID:g332709 GENETICS !$#gene HN CLASSIFICATION #superfamily paramyxovirus hemagglutinin-neuraminidase KEYWORDS glycoprotein; glycosidase; hemagglutinin; hydrolase; !1transmembrane protein FEATURE !$32-53 #domain transmembrane #status predicted #label TMN\ !$308,351,485,523 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 572 #molecular-weight 64335 #checksum 2804 SEQUENCE /// ENTRY HNNZ80 #type complete TITLE hemagglutinin-neuraminidase (EC 3.2.1.-) - parainfluenza virus type 3 (strain Tex/545/80) ORGANISM #formal_name parainfluenza virus type 3 #note host Homo sapiens (man) DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 18-Jun-1999 ACCESSIONS D29970 REFERENCE A94369 !$#authors van Wyke Coelingh, K.L.; Winter, C.C.; Murphy, B.R. !$#journal Virology (1988) 162:137-143 !$#title Nucleotide and deduced amino acid sequence of !1hemagglutinin-neuraminidase genes of human type 3 !1parainfluenza viruses isolated from 1957 to 1983. !$#cross-references MUID:88101361; PMID:2827373 !$#accession D29970 !'##molecule_type genomic RNA !'##residues 1-572 ##label VAN !'##cross-references GB:M18762; NID:g332710; PIDN:AAA46849.1; !1PID:g332711 GENETICS !$#gene HN CLASSIFICATION #superfamily paramyxovirus hemagglutinin-neuraminidase KEYWORDS glycoprotein; glycosidase; hemagglutinin; hydrolase; !1transmembrane protein FEATURE !$32-53 #domain transmembrane #status predicted #label TMN\ !$308,351,389,485,523 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 572 #molecular-weight 64259 #checksum 2930 SEQUENCE /// ENTRY HNNZ82 #type complete TITLE hemagglutinin-neuraminidase (EC 3.2.1.-) - parainfluenza virus type 3 (strain Tex/9305/82) ORGANISM #formal_name parainfluenza virus type 3 #note host Homo sapiens (man) DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 18-Jun-1999 ACCESSIONS E29970 REFERENCE A94369 !$#authors van Wyke Coelingh, K.L.; Winter, C.C.; Murphy, B.R. !$#journal Virology (1988) 162:137-143 !$#title Nucleotide and deduced amino acid sequence of !1hemagglutinin-neuraminidase genes of human type 3 !1parainfluenza viruses isolated from 1957 to 1983. !$#cross-references MUID:88101361; PMID:2827373 !$#accession E29970 !'##molecule_type genomic RNA !'##residues 1-572 ##label VAN !'##cross-references GB:M18763; NID:g332712; PIDN:AAA46850.1; !1PID:g332713 GENETICS !$#gene HN CLASSIFICATION #superfamily paramyxovirus hemagglutinin-neuraminidase KEYWORDS glycoprotein; glycosidase; hemagglutinin; hydrolase; !1transmembrane protein FEATURE !$32-53 #domain transmembrane #status predicted #label TMN\ !$308,351,485,523 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 572 #molecular-weight 64394 #checksum 2922 SEQUENCE /// ENTRY HNNZ83 #type complete TITLE hemagglutinin-neuraminidase (EC 3.2.1.-) - parainfluenza virus type 3 (strain Tex/12677/83) ORGANISM #formal_name parainfluenza virus type 3 #note host Homo sapiens (man) DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 18-Jun-1999 ACCESSIONS F29970 REFERENCE A94369 !$#authors van Wyke Coelingh, K.L.; Winter, C.C.; Murphy, B.R. !$#journal Virology (1988) 162:137-143 !$#title Nucleotide and deduced amino acid sequence of !1hemagglutinin-neuraminidase genes of human type 3 !1parainfluenza viruses isolated from 1957 to 1983. !$#cross-references MUID:88101361; PMID:2827373 !$#accession F29970 !'##molecule_type genomic RNA !'##residues 1-572 ##label VAN !'##cross-references GB:M18764; NID:g332714; PIDN:AAA46851.1; !1PID:g332715 GENETICS !$#gene HN CLASSIFICATION #superfamily paramyxovirus hemagglutinin-neuraminidase KEYWORDS glycoprotein; glycosidase; hemagglutinin; hydrolase; !1transmembrane protein FEATURE !$32-53 #domain transmembrane #status predicted #label TMN\ !$308,351,389,485,523 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 572 #molecular-weight 64330 #checksum 1869 SEQUENCE /// ENTRY HNNZ4A #type complete TITLE hemagglutinin-neuraminidase (EC 3.2.1.-) - parainfluenza virus type 4A (strain Toshiba) ORGANISM #formal_name parainfluenza virus type 4A DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 18-Jun-1999 ACCESSIONS A34683 REFERENCE A34683 !$#authors Bando, H.; Kondo, K.; Kawano, M.; Komada, H.; Tsurudome, M.; !1Nishio, M.; Ito, Y. !$#journal Virology (1990) 175:307-312 !$#title Molecular cloning and sequence analysis of human !1parainfluenza type 4A virus HN gene: its irregularities on !1structure and activities. !$#cross-references MUID:90177230; PMID:2155512 !$#accession A34683 !'##molecule_type mRNA !'##residues 1-573 ##label BAN !'##cross-references GB:M34033; NID:g332577; PIDN:AAA46799.1; !1PID:g332578 GENETICS !$#gene HN CLASSIFICATION #superfamily paramyxovirus hemagglutinin-neuraminidase KEYWORDS glycoprotein; glycosidase; hemagglutinin; hydrolase; !1transmembrane protein FEATURE !$28-46 #domain transmembrane #status predicted #label TMN\ !$126,258,330,339, !$347,433,502,509,530 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 573 #molecular-weight 65544 #checksum 6125 SEQUENCE /// ENTRY HNNZSV #type complete TITLE hemagglutinin-neuraminidase (EC 3.2.1.-) - simian paramyxovirus SV5 ORGANISM #formal_name simian paramyxovirus SV5 DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 18-Jun-1999 ACCESSIONS A00879; JQ1304; A21878 REFERENCE A93008 !$#authors Hiebert, S.W.; Paterson, R.G.; Lamb, R.A. !$#journal J. Virol. (1985) 54:1-6 !$#title Hemagglutinin-neuraminidase protein of the paramyxovirus !1simian virus 5: nucleotide sequence of the mRNA predicts an !1N-terminal membrane anchor. !$#cross-references MUID:85135055; PMID:3973974 !$#accession A00879 !'##molecule_type mRNA !'##residues 1-565 ##label HIE !'##cross-references GB:K02870; NID:g335110; PIDN:AAA47878.1; !1PID:g335111 REFERENCE JQ1304 !$#authors Baty, D.U.; Southern, J.A.; Randall, R.E. !$#journal J. Gen. Virol. (1991) 72:3103-3107 !$#title Sequence comparison between the haemagglutinin-neuraminidase !1genes of simian, canine and human isolates of simian virus !15. !$#cross-references MUID:92113554; PMID:1765772 !$#accession JQ1304 !'##molecule_type mRNA !'##residues 1-565 ##label BAT !'##cross-references GB:S76876; NID:g243331; PIDN:AAB21114.1; !1PID:g243332 !'##experimental_source isolate W3 GENETICS !$#gene HN CLASSIFICATION #superfamily paramyxovirus hemagglutinin-neuraminidase KEYWORDS glycoprotein; glycosidase; hemagglutinin; hydrolase; !1transmembrane protein FEATURE !$18-36 #domain transmembrane #status predicted #label TRM\ !$110,139,267,471, !$497,504 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 565 #molecular-weight 62204 #checksum 9196 SEQUENCE /// ENTRY HNNZC1 #type complete TITLE hemagglutinin-neuraminidase (EC 3.2.1.-) - simian paramyxovirus SV5 (isolate canine/CPI-) ORGANISM #formal_name simian paramyxovirus SV5 DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 15-Oct-1996 ACCESSIONS JQ1305 REFERENCE JQ1304 !$#authors Baty, D.U.; Southern, J.A.; Randall, R.E. !$#journal J. Gen. Virol. (1991) 72:3103-3107 !$#title Sequence comparison between the haemagglutinin-neuraminidase !1genes of simian, canine and human isolates of simian virus !15. !$#cross-references MUID:92113554; PMID:1765772 !$#accession JQ1305 !'##molecule_type mRNA !'##residues 1-565 ##label BAT GENETICS !$#gene HN CLASSIFICATION #superfamily paramyxovirus hemagglutinin-neuraminidase KEYWORDS glycoprotein; glycosidase; hemagglutinin; hydrolase; !1transmembrane protein FEATURE !$18-36 #domain transmembrane #status predicted #label TM1\ !$535-551 #domain transmembrane #status predicted #label TM2\ !$110,139,267,471, !$497,504 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 565 #molecular-weight 62278 #checksum 7973 SEQUENCE /// ENTRY HNNZC2 #type complete TITLE hemagglutinin-neuraminidase (EC 3.2.1.-) - simian paramyxovirus SV5 (isolate canine/CPI+) ORGANISM #formal_name simian paramyxovirus SV5 DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 15-Oct-1996 ACCESSIONS JQ1306 REFERENCE JQ1304 !$#authors Baty, D.U.; Southern, J.A.; Randall, R.E. !$#journal J. Gen. Virol. (1991) 72:3103-3107 !$#title Sequence comparison between the haemagglutinin-neuraminidase !1genes of simian, canine and human isolates of simian virus !15. !$#cross-references MUID:92113554; PMID:1765772 !$#accession JQ1306 !'##molecule_type mRNA !'##residues 1-565 ##label BAT GENETICS !$#gene HN CLASSIFICATION #superfamily paramyxovirus hemagglutinin-neuraminidase KEYWORDS glycoprotein; glycosidase; hemagglutinin; hydrolase; !1transmembrane protein FEATURE !$18-36 #domain transmembrane #status predicted #label TM1\ !$535-551 #domain transmembrane #status predicted #label TM2\ !$110,139,267,471, !$497,504 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 565 #molecular-weight 62306 #checksum 8015 SEQUENCE /// ENTRY HNNZC3 #type complete TITLE hemagglutinin-neuraminidase (EC 3.2.1.-) - simian paramyxovirus SV5 (isolate human/LN) ORGANISM #formal_name simian paramyxovirus SV5 DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 15-Oct-1996 ACCESSIONS JQ1307 REFERENCE JQ1304 !$#authors Baty, D.U.; Southern, J.A.; Randall, R.E. !$#journal J. Gen. Virol. (1991) 72:3103-3107 !$#title Sequence comparison between the haemagglutinin-neuraminidase !1genes of simian, canine and human isolates of simian virus !15. !$#cross-references MUID:92113554; PMID:1765772 !$#accession JQ1307 !'##molecule_type mRNA !'##residues 1-565 ##label BAT GENETICS !$#gene HN CLASSIFICATION #superfamily paramyxovirus hemagglutinin-neuraminidase KEYWORDS glycoprotein; glycosidase; hemagglutinin; hydrolase; !1transmembrane protein FEATURE !$18-36 #domain transmembrane #status predicted #label TM1\ !$535-551 #domain transmembrane #status predicted #label TM2\ !$110,139,267,471, !$497,504 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 565 #molecular-weight 62137 #checksum 9442 SEQUENCE /// ENTRY HNNZ41 #type complete TITLE hemagglutinin-neuraminidase (EC 3.2.1.-) - simian paramyxovirus SV41 (strain Toshiba/Chanock) ORGANISM #formal_name simian paramyxovirus SV41 DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 18-Jun-1999 ACCESSIONS A36419 REFERENCE A36419 !$#authors Tsurudome, M.; Bando, H.; Nishio, M.; Iwamoto, Y.; Kawano, !1M.; Kondo, K.; Komada, H.; Ito, Y. !$#journal Virology (1990) 179:738-748 !$#title Antigenic and structural properties of a paramyxovirus !1simian virus 41 (SV41) reveal a close relationship with !1human parainfluenza type 2 virus. !$#cross-references MUID:91049440; PMID:2173260 !$#accession A36419 !'##molecule_type genomic RNA !'##residues 1-568 ##label TSU !'##cross-references GB:M62733; NID:g334026; PIDN:AAA47451.1; !1PID:g334027 GENETICS !$#gene HN CLASSIFICATION #superfamily paramyxovirus hemagglutinin-neuraminidase KEYWORDS glycoprotein; glycosidase; hemagglutinin; hydrolase; !1transmembrane protein FEATURE !$19-37 #domain transmembrane #status predicted #label TMN\ !$44,111,268,280,382, !$500,513 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 568 #molecular-weight 61733 #checksum 2312 SEQUENCE /// ENTRY HNNZP2 #type complete TITLE hemagglutinin-neuraminidase (EC 3.2.1.-) - parainfluenza virus type 2 (strain Toshiba) ORGANISM #formal_name parainfluenza virus type 2 DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 18-Jun-1999 ACCESSIONS A33777; S16663 REFERENCE A33777 !$#authors Kawano, M.; Bando, H.; Yuasa, T.; Kondo, K.; Tsurudome, M.; !1Komada, H.; Nishio, M.; Ito, Y. !$#journal Virology (1990) 174:308-313 !$#title Sequence determination of the hemagglutinin-neuraminidase !1(HN) gene of human parainfluenza type 2 virus and the !1construction of a phylogenetic tree for HN proteins of all !1the paramyxoviruses that are infectious to humans. !$#cross-references MUID:90101390; PMID:2152995 !$#accession A33777 !'##molecule_type genomic RNA; mRNA !'##residues 1-571 ##label KAW1 !'##cross-references GB:X57559; NID:g61985; PIDN:CAA40787.1; PID:g61990 REFERENCE S16659 !$#authors Kawano, M.; Okamoto, K.; Bando, H.; Kondo, K.; Tsurudome, !1M.; Komada, H.; Nishio, M.; Ito, Y. !$#journal Nucleic Acids Res. (1991) 19:2739-2746 !$#title Characterizations of the human parainfluenza type 2 virus !1gene encoding the L protein and the intergenic sequences. !$#cross-references MUID:91252221; PMID:1645865 !$#accession S16663 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type genomic RNA !'##residues 1-571 ##label KAW2 !'##cross-references EMBL:X57559; NID:g61985; PIDN:CAA40787.1; !1PID:g61990 !'##experimental_source strain Toshiba !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1March 1991 GENETICS !$#gene HN CLASSIFICATION #superfamily paramyxovirus hemagglutinin-neuraminidase KEYWORDS glycoprotein; glycosidase; hemagglutinin; hydrolase; !1transmembrane protein FEATURE !$23-40 #domain transmembrane #status predicted #label TMN\ !$6,115,142,272,284, !$335,341,386,454, !$498,501,504,517,522 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 571 #molecular-weight 63262 #checksum 9280 SEQUENCE /// ENTRY HNNZT2 #type complete TITLE hemagglutinin-neuraminidase (EC 3.2.1.-) - parainfluenza virus type 2 ORGANISM #formal_name parainfluenza virus type 2 DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jun-2000 ACCESSIONS A34767 REFERENCE A34767 !$#authors Precious, B.; Southern, J.A.; Randall, R.E. !$#journal J. Gen. Virol. (1990) 71:1163-1168 !$#title Sequence analysis of the HN gene of parainfluenza virus type !12. !$#cross-references MUID:90264848; PMID:2161050 !$#accession A34767 !'##molecule_type mRNA !'##residues 1-571 ##label PRE !'##cross-references GB:D00865; NID:g222240; PIDN:BAA00739.1; !1PID:g222241 GENETICS !$#gene HN CLASSIFICATION #superfamily paramyxovirus hemagglutinin-neuraminidase KEYWORDS glycoprotein; glycosidase; hemagglutinin; hydrolase; !1transmembrane protein FEATURE !$23-40 #domain transmembrane #status predicted #label TMN\ !$6,115,142,272,284, !$335,386,454,498, !$501,504,517,522 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 571 #molecular-weight 63315 #checksum 9738 SEQUENCE /// ENTRY HNNZMP #type complete TITLE hemagglutinin-neuraminidase (EC 3.2.1.-) - mumps virus (strain RW) ORGANISM #formal_name mumps virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 18-Jun-1999 ACCESSIONS A28917 REFERENCE A28917 !$#authors Waxham, M.N.; Aronowski, J.; Server, A.C.; Wolinsky, J.S.; !1Smith, J.A.; Goodman, H.M. !$#journal Virology (1988) 164:318-325 !$#title Sequence determination of the mumps virus HN gene. !$#cross-references MUID:88219518; PMID:3369084 !$#accession A28917 !'##molecule_type genomic RNA !'##residues 1-582 ##label WAX !'##cross-references GB:M19933; NID:g332275; PIDN:AAA46609.1; !1PID:g332276 GENETICS !$#gene HN CLASSIFICATION #superfamily paramyxovirus hemagglutinin-neuraminidase KEYWORDS glycoprotein; glycosidase; hemagglutinin; hydrolase; !1transmembrane protein FEATURE !$35-53 #domain transmembrane #status predicted #label TMN\ !$12,127,284,329,400, !$448,507,514 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 582 #molecular-weight 64045 #checksum 9507 SEQUENCE /// ENTRY HNNZMM #type complete TITLE hemagglutinin-neuraminidase (EC 3.2.1.-) - mumps virus (strain Miyahara) ORGANISM #formal_name mumps virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 18-Jun-1999 ACCESSIONS A34054; S04878 REFERENCE A34054 !$#authors Takeuchi, K.; Tanabayashi, K.; Hishiyama, M.; Yamada, A.; !1Sugiura, A. !$#journal Nucleic Acids Res. (1989) 17:5840 !$#title Cloning and sequencing of the haemagglutinin-neuraminidase !1gene of mumps virus (Miyahara strain). !$#cross-references MUID:89345175; PMID:2762157 !$#accession A34054 !'##molecule_type mRNA !'##residues 1-582 ##label TAK !'##cross-references GB:X15284; NID:g60584; PIDN:CAA33358.1; PID:g60585 GENETICS !$#gene HN CLASSIFICATION #superfamily paramyxovirus hemagglutinin-neuraminidase KEYWORDS glycoprotein; glycosidase; hemagglutinin; hydrolase; !1transmembrane protein FEATURE !$35-53 #domain transmembrane #status predicted #label TMN\ !$12,127,284,329,400, !$448,464,507,514 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 582 #molecular-weight 64044 #checksum 8851 SEQUENCE /// ENTRY HNNZSB #type complete TITLE hemagglutinin-neuraminidase (EC 3.2.1.-) - mumps virus (strain SBL-1) ORGANISM #formal_name mumps virus DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jun-2000 ACCESSIONS A42758; PQ0103 REFERENCE A42758 !$#authors Koevamees, J.; Norrby, E.; Elango, N. !$#journal Virus Res. (1989) 12:87-96 !$#title Complete nucleotide sequence of the !1hemagglutinin-neuraminidase (HN) mRNA of mumps virus and !1comparison of paramyxovirus HN proteins. !$#cross-references MUID:89243817; PMID:2718627 !$#accession A42758 !'##molecule_type mRNA !'##residues 1-582 ##label KOE !'##cross-references GB:M55065 REFERENCE JQ0596 !$#authors Elliott, G.D.; Yeo, R.P.; Afzal, M.A.; Simpson, E.J.B.; !1Curran, J.A.; Rima, B.K. !$#journal J. Gen. Virol. (1990) 71:1555-1560 !$#title Strain-variable editing during transcription of the P gene !1of mumps virus may lead to the generation of non-structural !1proteins NS1(V) and NS2. !$#cross-references MUID:90324941; PMID:2165137 !$#accession PQ0103 !'##molecule_type genomic RNA !'##residues 1-153 ##label ELL !'##cross-references GB:D00663; NID:g222149; PIDN:BAA00563.1; !1PID:g2160356 !'##experimental_source strain SBL1 GENETICS !$#gene HN CLASSIFICATION #superfamily paramyxovirus hemagglutinin-neuraminidase KEYWORDS glycoprotein; glycosidase; hemagglutinin; hydrolase; !1transmembrane protein FEATURE !$1-34 #domain intracellular #status predicted #label INT\ !$35-51 #domain transmembrane #status predicted #label TM1\ !$52-582 #domain extracellular #status predicted #label EXT\ !$127,284,329,400, !$448,464,507 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 582 #molecular-weight 63944 #checksum 9884 SEQUENCE /// ENTRY HNNZNC #type complete TITLE hemagglutinin-neuraminidase (EC 3.2.1.-) (version 2) - Newcastle disease virus ORGANISM #formal_name Newcastle disease virus DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 18-Jun-1999 ACCESSIONS A26355 REFERENCE A26355 !$#authors Jorgensen, E.D.; Collins, P.L.; Lomedico, P.T. !$#journal Virology (1987) 156:12-24 !$#title Cloning and nucleotide sequence of Newcastle disease virus !1hemagglutinin-neuraminidase mRNA: identification of a !1putative sialic acid binding site. !$#cross-references MUID:87122141; PMID:3027962 !$#accession A26355 !'##molecule_type mRNA !'##residues 1-577 ##label JOR !'##cross-references GB:M16573; NID:g332355; PIDN:AAA46668.1; !1PID:g332356 GENETICS !$#gene HN CLASSIFICATION #superfamily paramyxovirus hemagglutinin-neuraminidase KEYWORDS glycoprotein; glycosidase; hemagglutinin; hydrolase; !1transmembrane protein FEATURE !$27-50 #domain transmembrane #status predicted #label TMN\ !$119,341,433,481,538 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 577 #molecular-weight 63241 #checksum 8538 SEQUENCE /// ENTRY HNNZU1 #type complete TITLE hemagglutinin-neuraminidase (EC 3.2.1.-) - Newcastle disease virus (strain Ulster) ORGANISM #formal_name Newcastle disease virus DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jun-2000 ACCESSIONS B29823 REFERENCE A92799 !$#authors Millar, N.S.; Chambers, P.; Emmerson, P.T. !$#journal J. Gen. Virol. (1988) 69:613-620 !$#title Nucleotide sequence of the fusion and !1haemagglutinin-neuraminidase glycoprotein genes of Newcastle !1disease virus, strain Ulster: molecular basis for variations !1in pathogenicity between strains. !$#cross-references MUID:88171450; PMID:3351479 !$#accession B29823 !'##molecule_type mRNA !'##residues 1-616 ##label MIL !'##cross-references GB:D00243; NID:g222174; PIDN:BAA00174.1; !1PID:g222176 GENETICS !$#gene HN CLASSIFICATION #superfamily paramyxovirus hemagglutinin-neuraminidase KEYWORDS glycoprotein; glycosidase; hemagglutinin; hydrolase; !1transmembrane protein FEATURE !$27-54 #domain transmembrane #status predicted #label TMN\ !$119,341,433,481, !$538,600 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 616 #molecular-weight 67589 #checksum 6762 SEQUENCE /// ENTRY A46328 #type complete TITLE hemagglutinin-neuraminidase (EC 3.2.1.-) - Newcastle disease virus (strain D26.76) ORGANISM #formal_name Newcastle disease virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 18-Jun-1999 ACCESSIONS A46328 REFERENCE A46328 !$#authors Sakaguchi, T.; Toyoda, T.; Gotoh, B.; Inocencio, N.M.; Kuma, !1K.; Miyata, T.; Nagai, Y. !$#journal Virology (1989) 169:260-272 !$#title Newcastle disease virus evolution. I. Multiple lineages !1defined by sequence variability of the !1hemagglutinin-neuraminidase gene. !$#cross-references MUID:89204897; PMID:2705297 !$#accession A46328 !'##molecule_type mRNA !'##residues 1-616 ##label SAK !'##cross-references GB:M24705; NID:g332329; PIDN:AAA46655.1; !1PID:g332330 GENETICS !$#gene HN CLASSIFICATION #superfamily paramyxovirus hemagglutinin-neuraminidase KEYWORDS glycoprotein; glycosidase; hemagglutinin; hydrolase; !1transmembrane protein FEATURE !$27-48 #domain transmembrane #status predicted #label TMN\ !$119,341,433,481, !$538,600 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 616 #molecular-weight 67660 #checksum 7957 SEQUENCE /// ENTRY B46328 #type complete TITLE hemagglutinin-neuraminidase (EC 3.2.1.-) - Newcastle disease virus (strain QUE/66) ORGANISM #formal_name Newcastle disease virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 18-Jun-1999 ACCESSIONS B46328 REFERENCE A46328 !$#authors Sakaguchi, T.; Toyoda, T.; Gotoh, B.; Inocencio, N.M.; Kuma, !1K.; Miyata, T.; Nagai, Y. !$#journal Virology (1989) 169:260-272 !$#title Newcastle disease virus evolution. I. Multiple lineages !1defined by sequence variability of the !1hemagglutinin-neuraminidase gene. !$#cross-references MUID:89204897; PMID:2705297 !$#accession B46328 !'##molecule_type mRNA !'##residues 1-616 ##label SAK !'##cross-references GB:M24706; NID:g332331; PIDN:AAA46656.1; !1PID:g332332 GENETICS !$#gene HN CLASSIFICATION #superfamily paramyxovirus hemagglutinin-neuraminidase KEYWORDS glycoprotein; glycosidase; hemagglutinin; hydrolase; !1transmembrane protein FEATURE !$27-48 #domain transmembrane #status predicted #label TMN\ !$119,341,433,481, !$538,600 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 616 #molecular-weight 67591 #checksum 7173 SEQUENCE /// ENTRY C46328 #type complete TITLE hemagglutinin-neuraminidase (EC 3.2.1.-) - Newcastle disease virus (strain ULS/67) ORGANISM #formal_name Newcastle disease virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 15-Oct-1996 ACCESSIONS C46328 REFERENCE A46328 !$#authors Sakaguchi, T.; Toyoda, T.; Gotoh, B.; Inocencio, N.M.; Kuma, !1K.; Miyata, T.; Nagai, Y. !$#journal Virology (1989) 169:260-272 !$#title Newcastle disease virus evolution. I. Multiple lineages !1defined by sequence variability of the !1hemagglutinin-neuraminidase gene. !$#cross-references MUID:89204897; PMID:2705297 !$#accession C46328 !'##molecule_type mRNA !'##residues 1-616 ##label SAK !'##cross-references GB:M24707 GENETICS !$#gene HN CLASSIFICATION #superfamily paramyxovirus hemagglutinin-neuraminidase KEYWORDS glycoprotein; glycosidase; hemagglutinin; hydrolase; !1transmembrane protein FEATURE !$27-48 #domain transmembrane #status predicted #label TMN\ !$119,341,433,481, !$538,600 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 616 #molecular-weight 67656 #checksum 6880 SEQUENCE /// ENTRY HNNZQD #type complete TITLE hemagglutinin-neuraminidase (EC 3.2.1.-) precursor - Newcastle disease virus (strain Queensland avirulent) ORGANISM #formal_name Newcastle disease virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 18-Jun-1999 ACCESSIONS A31110 REFERENCE A92665 !$#authors Gorman, J.J.; Nestorowicz, A.; Mitchell, S.J.; Corino, G.L.; !1Selleck, P.W. !$#journal J. Biol. Chem. (1988) 263:12522-12531 !$#title Characterization of the sites of proteolytic activation of !1Newcastle disease virus membrane glycoprotein precursors. !$#cross-references MUID:88315049; PMID:3045120 !$#accession A31110 !'##molecule_type genomic RNA !'##residues 1-616 ##label GOR !'##cross-references GB:J03911; NID:g332327; PIDN:AAA46654.1; !1PID:g332328 GENETICS !$#gene HN CLASSIFICATION #superfamily paramyxovirus hemagglutinin-neuraminidase KEYWORDS glycoprotein; glycosidase; hemagglutinin; hydrolase; !1transmembrane protein FEATURE !$1-574 #product hemagglutinin-neuraminidase #status !8predicted #label HNS\ !$27-54 #domain transmembrane #status predicted #label TMN\ !$119,341,433,481, !$538,600 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 616 #molecular-weight 67656 #checksum 8832 SEQUENCE /// ENTRY HNNZAV #type complete TITLE hemagglutinin-neuraminidase (EC 3.2.1.-) - Newcastle disease virus (strain Australia-Victoria) ORGANISM #formal_name Newcastle disease virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 15-Oct-1996 ACCESSIONS B31110; S07424 REFERENCE A92665 !$#authors Gorman, J.J.; Nestorowicz, A.; Mitchell, S.J.; Corino, G.L.; !1Selleck, P.W. !$#journal J. Biol. Chem. (1988) 263:12522-12531 !$#title Characterization of the sites of proteolytic activation of !1Newcastle disease virus membrane glycoprotein precursors. !$#cross-references MUID:88315049; PMID:3045120 !$#accession B31110 !'##molecule_type genomic RNA !'##residues 1-570 ##label GOR !'##experimental_source strain Australia-Victoria virulent REFERENCE S07424 !$#authors McGinnes, L.W.; Wilde, A.; Morrison, T.G. !$#journal Virus Res. (1987) 7:187-202 !$#title Nucleotide sequence of the gene encoding the Newcastle !1disease virus hemagglutinin-neuraminidase protein and !1comparisons of paramyxovirus hemagglutinin-neuraminidase !1protein sequences. !$#cross-references MUID:87266149; PMID:3037818 !$#accession S07424 !'##molecule_type mRNA !'##residues 1-570 ##label MCG !'##cross-references EMBL:M22110 !'##experimental_source strain A-V GENETICS !$#gene HN CLASSIFICATION #superfamily paramyxovirus hemagglutinin-neuraminidase KEYWORDS glycoprotein; glycosidase; hemagglutinin; hydrolase; !1transmembrane protein FEATURE !$27-48 #domain transmembrane #status predicted #label TMM\ !$119,340,432,480, !$507,537 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 570 #molecular-weight 62284 #checksum 2977 SEQUENCE /// ENTRY D46328 #type complete TITLE hemagglutinin-neuraminidase (EC 3.2.1.-) - Newcastle disease virus (strain B1/47) ORGANISM #formal_name Newcastle disease virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 15-Oct-1996 ACCESSIONS D46328 REFERENCE A46328 !$#authors Sakaguchi, T.; Toyoda, T.; Gotoh, B.; Inocencio, N.M.; Kuma, !1K.; Miyata, T.; Nagai, Y. !$#journal Virology (1989) 169:260-272 !$#title Newcastle disease virus evolution. I. Multiple lineages !1defined by sequence variability of the !1hemagglutinin-neuraminidase gene. !$#cross-references MUID:89204897; PMID:2705297 !$#accession D46328 !'##molecule_type mRNA !'##residues 1-577 ##label SAK !'##cross-references GB:M24708 GENETICS !$#gene HN CLASSIFICATION #superfamily paramyxovirus hemagglutinin-neuraminidase KEYWORDS glycoprotein; glycosidase; hemagglutinin; hydrolase; !1transmembrane protein FEATURE !$27-48 #domain transmembrane #status predicted #label TMN\ !$119,341,433,481,538 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 577 #molecular-weight 63215 #checksum 8741 SEQUENCE /// ENTRY E46328 #type complete TITLE hemagglutinin-neuraminidase (EC 3.2.1.-) - Newcastle disease virus (strain LAS/46) ORGANISM #formal_name Newcastle disease virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 15-Oct-1996 ACCESSIONS E46328 REFERENCE A46328 !$#authors Sakaguchi, T.; Toyoda, T.; Gotoh, B.; Inocencio, N.M.; Kuma, !1K.; Miyata, T.; Nagai, Y. !$#journal Virology (1989) 169:260-272 !$#title Newcastle disease virus evolution. I. Multiple lineages !1defined by sequence variability of the !1hemagglutinin-neuraminidase gene. !$#cross-references MUID:89204897; PMID:2705297 !$#accession E46328 !'##molecule_type mRNA !'##residues 1-577 ##label SAK !'##cross-references GB:M24709 GENETICS !$#gene HN CLASSIFICATION #superfamily paramyxovirus hemagglutinin-neuraminidase KEYWORDS glycoprotein; glycosidase; hemagglutinin; hydrolase; !1transmembrane protein FEATURE !$27-48 #domain transmembrane #status predicted #label TMN\ !$119,341,433,481,538 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 577 #molecular-weight 63209 #checksum 9504 SEQUENCE /// ENTRY F46328 #type complete TITLE hemagglutinin-neuraminidase (EC 3.2.1.-) (version 1) - Newcastle disease virus ORGANISM #formal_name Newcastle disease virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 18-Jun-1999 ACCESSIONS F46328; A27005 REFERENCE A46328 !$#authors Sakaguchi, T.; Toyoda, T.; Gotoh, B.; Inocencio, N.M.; Kuma, !1K.; Miyata, T.; Nagai, Y. !$#journal Virology (1989) 169:260-272 !$#title Newcastle disease virus evolution. I. Multiple lineages !1defined by sequence variability of the !1hemagglutinin-neuraminidase gene. !$#cross-references MUID:89204897; PMID:2705297 !$#accession F46328 !'##molecule_type mRNA !'##residues 1-577 ##label SAK !'##cross-references GB:M24710; NID:g332339; PIDN:AAA46660.1; !1PID:g332340 !'##experimental_source strain BEA/45 REFERENCE A27005 !$#authors Millar, N.S.; Chambers, P.; Emmerson, P.T. !$#journal J. Gen. Virol. (1986) 67:1917-1927 !$#title Nucleotide sequence analysis of the !1haemagglutinin-neuraminidase gene of Newcastle disease !1virus. !$#cross-references MUID:86306666; PMID:3018130 !$#accession A27005 !'##molecule_type mRNA !'##residues 1-577 ##label MIL !'##cross-references GB:X04355; GB:X03634; NID:g60935; PIDN:CAA27880.1; !1PID:g60936 GENETICS !$#gene HN CLASSIFICATION #superfamily paramyxovirus hemagglutinin-neuraminidase KEYWORDS glycoprotein; glycosidase; hemagglutinin; hydrolase; !1transmembrane protein FEATURE !$27-48 #domain transmembrane #status predicted #label TMN\ !$119,341,433,481,538 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 577 #molecular-weight 63142 #checksum 9885 SEQUENCE /// ENTRY G46328 #type complete TITLE hemagglutinin-neuraminidase (EC 3.2.1.-) - Newcastle disease virus ORGANISM #formal_name Newcastle disease virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 15-Oct-1996 ACCESSIONS G46328; A29201 REFERENCE A46328 !$#authors Sakaguchi, T.; Toyoda, T.; Gotoh, B.; Inocencio, N.M.; Kuma, !1K.; Miyata, T.; Nagai, Y. !$#journal Virology (1989) 169:260-272 !$#title Newcastle disease virus evolution. I. Multiple lineages !1defined by sequence variability of the !1hemagglutinin-neuraminidase gene. !$#cross-references MUID:89204897; PMID:2705297 !$#accession G46328 !'##molecule_type mRNA !'##residues 1-577 ##label SAK !'##cross-references GB:M24711 !'##experimental_source strain TEX/48 REFERENCE A94379 !$#authors Schaper, U.M.; Fuller, F.J.; Ward, M.D.W.; Mehrotra, Y.; !1Stone, H.O.; Stripp, B.R.; De Buysscher, E.V. !$#journal Virology (1988) 165:291-295 !$#title Nucleotide sequence of the envelope protein genes of a !1highly virulent, neurotropic strain of Newcastle disease !1virus. !$#cross-references MUID:88265873; PMID:3388773 !$#accession A29201 !'##molecule_type mRNA !'##residues 1-577 ##label SCH !'##experimental_source strain Texas G.B. GENETICS !$#gene HN CLASSIFICATION #superfamily paramyxovirus hemagglutinin-neuraminidase KEYWORDS glycoprotein; glycosidase; hemagglutinin; hydrolase; !1transmembrane protein FEATURE !$27-48 #domain transmembrane #status predicted #label TMN\ !$119,341,433,481,538 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 577 #molecular-weight 63251 #checksum 9752 SEQUENCE /// ENTRY H46328 #type complete TITLE hemagglutinin-neuraminidase (EC 3.2.1.-) - Newcastle disease virus (strain AUS/32) ORGANISM #formal_name Newcastle disease virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 15-Oct-1996 ACCESSIONS H46328 REFERENCE A46328 !$#authors Sakaguchi, T.; Toyoda, T.; Gotoh, B.; Inocencio, N.M.; Kuma, !1K.; Miyata, T.; Nagai, Y. !$#journal Virology (1989) 169:260-272 !$#title Newcastle disease virus evolution. I. Multiple lineages !1defined by sequence variability of the !1hemagglutinin-neuraminidase gene. !$#cross-references MUID:89204897; PMID:2705297 !$#accession H46328 !'##molecule_type mRNA !'##residues 1-571 ##label SAK !'##cross-references GB:M24712 GENETICS !$#gene HN CLASSIFICATION #superfamily paramyxovirus hemagglutinin-neuraminidase KEYWORDS glycoprotein; glycosidase; hemagglutinin; hydrolase; !1transmembrane protein FEATURE !$27-48 #domain transmembrane #status predicted #label TMN\ !$119,341,433,481, !$508,538 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 571 #molecular-weight 62487 #checksum 4360 SEQUENCE /// ENTRY I46328 #type complete TITLE hemagglutinin-neuraminidase (EC 3.2.1.-) - Newcastle disease virus (strain MIY/51) ORGANISM #formal_name Newcastle disease virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 15-Oct-1996 ACCESSIONS I46328 REFERENCE A46328 !$#authors Sakaguchi, T.; Toyoda, T.; Gotoh, B.; Inocencio, N.M.; Kuma, !1K.; Miyata, T.; Nagai, Y. !$#journal Virology (1989) 169:260-272 !$#title Newcastle disease virus evolution. I. Multiple lineages !1defined by sequence variability of the !1hemagglutinin-neuraminidase gene. !$#cross-references MUID:89204897; PMID:2705297 !$#accession I46328 !'##molecule_type mRNA !'##residues 1-571 ##label SAK !'##cross-references GB:M24713 GENETICS !$#gene HN CLASSIFICATION #superfamily paramyxovirus hemagglutinin-neuraminidase KEYWORDS glycoprotein; glycosidase; hemagglutinin; hydrolase; !1transmembrane protein FEATURE !$27-48 #domain transmembrane #status predicted #label TMN\ !$119,341,433,481, !$508,538 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 571 #molecular-weight 62536 #checksum 4419 SEQUENCE /// ENTRY A36829 #type complete TITLE hemagglutinin-neuraminidase (EC 3.2.1.-) - Newcastle disease virus (strain HER/33) ORGANISM #formal_name Newcastle disease virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 15-Oct-1996 ACCESSIONS A36829 REFERENCE A46328 !$#authors Sakaguchi, T.; Toyoda, T.; Gotoh, B.; Inocencio, N.M.; Kuma, !1K.; Miyata, T.; Nagai, Y. !$#journal Virology (1989) 169:260-272 !$#title Newcastle disease virus evolution. I. Multiple lineages !1defined by sequence variability of the !1hemagglutinin-neuraminidase gene. !$#cross-references MUID:89204897; PMID:2705297 !$#accession A36829 !'##molecule_type mRNA !'##residues 1-571 ##label SAK !'##cross-references GB:M24714 GENETICS !$#gene HN CLASSIFICATION #superfamily paramyxovirus hemagglutinin-neuraminidase KEYWORDS glycoprotein; glycosidase; hemagglutinin; hydrolase; !1transmembrane protein FEATURE !$27-48 #domain transmembrane #status predicted #label TMN\ !$119,341,433,481, !$508,538 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 571 #molecular-weight 62609 #checksum 6655 SEQUENCE /// ENTRY B36829 #type complete TITLE hemagglutinin-neuraminidase (EC 3.2.1.-) - Newcastle disease virus ORGANISM #formal_name Newcastle disease virus DATE 31-Dec-1993 #sequence_revision 22-Oct-1999 #text_change 22-Oct-1999 ACCESSIONS S07126; B36829 REFERENCE S07126 !$#authors Wemers, C.D.; de Henau, S.; Neyt, C.; Espion, D.; Letellier, !1C.; Meulemans, G.; Burny, A. !$#journal Arch. Virol. (1987) 97:101-113 !$#title The hemagglutinin-neuraminidase (HN) gene of Newcastle !1disease virus strain Italien (ndv Italien): comparison with !1HNs of other strains and expression by a vaccinia !1recombinant. !$#cross-references MUID:88076411; PMID:3318761 !$#accession S07126 !'##molecule_type mRNA !'##residues 1-571 ##label WEM !'##cross-references EMBL:M18640; NID:g332361; PIDN:AAA46671.1; !1PID:g332362 !'##experimental_source strain Italien REFERENCE A46328 !$#authors Sakaguchi, T.; Toyoda, T.; Gotoh, B.; Inocencio, N.M.; Kuma, !1K.; Miyata, T.; Nagai, Y. !$#journal Virology (1989) 169:260-272 !$#title Newcastle disease virus evolution. I. Multiple lineages !1defined by sequence variability of the !1hemagglutinin-neuraminidase gene. !$#cross-references MUID:89204897; PMID:2705297 !$#accession B36829 !'##molecule_type mRNA !'##residues 1-2,'LP',5-52,'S',54-215,'A',217-399,'AD',402-571 ##label !1SAK !'##cross-references GB:M24715 !'##experimental_source strain ITA/45 GENETICS !$#gene HN CLASSIFICATION #superfamily paramyxovirus hemagglutinin-neuraminidase KEYWORDS glycoprotein; glycosidase; hemagglutinin; hydrolase; !1transmembrane protein FEATURE !$27-48 #domain transmembrane #status predicted #label TMM\ !$119,341,433,481, !$508,538 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 571 #molecular-weight 62604 #checksum 5509 SEQUENCE /// ENTRY C36829 #type complete TITLE hemagglutinin-neuraminidase (EC 3.2.1.-) - Newcastle disease virus (strain CHI/85) ORGANISM #formal_name Newcastle disease virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 18-Jun-1999 ACCESSIONS C36829 REFERENCE A46328 !$#authors Sakaguchi, T.; Toyoda, T.; Gotoh, B.; Inocencio, N.M.; Kuma, !1K.; Miyata, T.; Nagai, Y. !$#journal Virology (1989) 169:260-272 !$#title Newcastle disease virus evolution. I. Multiple lineages !1defined by sequence variability of the !1hemagglutinin-neuraminidase gene. !$#cross-references MUID:89204897; PMID:2705297 !$#accession C36829 !'##molecule_type mRNA !'##residues 1-571 ##label SAK !'##cross-references GB:M24716; NID:g332351; PIDN:AAA46666.1; !1PID:g332352 GENETICS !$#gene HN CLASSIFICATION #superfamily paramyxovirus hemagglutinin-neuraminidase KEYWORDS glycoprotein; glycosidase; hemagglutinin; hydrolase; !1transmembrane protein FEATURE !$27-48 #domain transmembrane #status predicted #label TMN\ !$119,341,433,481,508 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 571 #molecular-weight 62901 #checksum 5259 SEQUENCE /// ENTRY D36829 #type complete TITLE hemagglutinin-neuraminidase (EC 3.2.1.-) - Newcastle disease virus (strain IBA/85) ORGANISM #formal_name Newcastle disease virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 18-Jun-1999 ACCESSIONS D36829 REFERENCE A46328 !$#authors Sakaguchi, T.; Toyoda, T.; Gotoh, B.; Inocencio, N.M.; Kuma, !1K.; Miyata, T.; Nagai, Y. !$#journal Virology (1989) 169:260-272 !$#title Newcastle disease virus evolution. I. Multiple lineages !1defined by sequence variability of the !1hemagglutinin-neuraminidase gene. !$#cross-references MUID:89204897; PMID:2705297 !$#accession D36829 !'##molecule_type mRNA !'##residues 1-571 ##label SAK !'##cross-references GB:M24717; NID:g332353; PIDN:AAA46667.1; !1PID:g332354 GENETICS !$#gene HN CLASSIFICATION #superfamily paramyxovirus hemagglutinin-neuraminidase KEYWORDS glycoprotein; glycosidase; hemagglutinin; hydrolase; !1transmembrane protein FEATURE !$27-48 #domain transmembrane #status predicted #label TMN\ !$119,341,481,508 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 571 #molecular-weight 62995 #checksum 6031 SEQUENCE /// ENTRY NMCLSS #type complete TITLE exo-alpha-sialidase (EC 3.2.1.18) precursor - Clostridium septicum ALTERNATE_NAMES neuraminidase ORGANISM #formal_name Clostridium septicum DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 18-Jun-1999 ACCESSIONS S15994 REFERENCE S15994 !$#authors Rothe, B.; Rothe, B.; Roggentin, P.; Schauer, R. !$#journal Mol. Gen. Genet. (1991) 226:190-197 !$#title The sialidase gene from Clostridium septicum: cloning, !1sequencing, expression in Escherichia coli and !1identification of conserved sequences in sialidases and !1other proteins. !$#cross-references MUID:91238693; PMID:2034213 !$#accession S15994 !'##molecule_type DNA !'##residues 1-1014 ##label MOL !'##cross-references EMBL:X63266; NID:g40662; PIDN:CAA44916.1; !1PID:g40663 CLASSIFICATION #superfamily Clostridium exo-alpha-sialidase KEYWORDS glycosidase; hydrolase FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-1014 #product exo-alpha-sialidase #status predicted #label !8MAT SUMMARY #length 1014 #molecular-weight 110652 #checksum 9621 SEQUENCE /// ENTRY NMEBST #type complete TITLE exo-alpha-sialidase (EC 3.2.1.18) - Salmonella typhimurium ALTERNATE_NAMES neuraminidase ORGANISM #formal_name Salmonella typhimurium DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 05-Jan-1996 ACCESSIONS S20976; S23020; S23980; A33133 REFERENCE S20976 !$#authors Hoyer, L.L.; Hamilton, A.C.; Steenbergen, S.M.; Vimr, E.R. !$#journal Mol. Microbiol. (1992) 6:873-884 !$#title Cloning, sequencing and distribution of the Salmonella !1typhimurium LT2 sialidase gene, nanH, provides evidence for !1interspecies gene transfer. !$#cross-references MUID:92292952; PMID:1602967 !$#accession S20976 !'##molecule_type DNA !'##residues 1-376 ##label HOY !'##cross-references EMBL:M55342 !$#accession S23020 !'##molecule_type protein !'##residues 2-40 ##label HO2 REFERENCE S23980 !$#authors Warner, T.G.; Harris, R.; McDowell, R.; Vimr, E.R. !$#journal Biochem. J. (1992) 285:957-964 !$#title Photolabelling of Salmonella typhimurium LT2 sialidase. !1Identification of a peptide with a predicted structural !1similarity to the active sites of influenza-virus !1sialidases. !$#cross-references MUID:92359969; PMID:1295492 !$#accession S23980 !'##status preliminary !'##molecule_type protein !'##residues 270-299,301-357 ##label WAR GENETICS !$#gene nanH CLASSIFICATION #superfamily Salmonella typhimurium exo-alpha-sialidase KEYWORDS glycosidase; hydrolase FEATURE !$2-376 #product exo-alpha-sialidase #status experimental !8#label MAT SUMMARY #length 376 #molecular-weight 41309 #checksum 8699 SEQUENCE /// ENTRY NMIV #type complete TITLE exo-alpha-sialidase (EC 3.2.1.18) - influenza A virus (strain A/PR/8/34) ALTERNATE_NAMES neuraminidase ORGANISM #formal_name influenza A virus DATE 01-Sep-1981 #sequence_revision 01-Sep-1981 #text_change 18-Jun-1999 ACCESSIONS A00880 REFERENCE A00880 !$#authors Fields, S.; Winter, G.; Brownlee, G.G. !$#journal Nature (1981) 290:213-217 !$#title Structure of the neuraminidase gene in human influenza virus !1A/PR/8/34. !$#cross-references MUID:81148841; PMID:7010182 !$#accession A00880 !'##molecule_type genomic RNA !'##residues 1-454 ##label FIE !'##cross-references GB:J02146; NID:g324507; PIDN:AAA43412.1; !1PID:g324508 !'##note this enzyme exists as a tetramer in the viral membrane; the !1amino-terminal hydrophobic region, i.e., residues 7-35, may !1be the membrane attachment site COMMENT This enzyme catalyzes the cleavage of the terminal sialic !1acid (N-acetylneuraminic acid) from carbohydrate chains in !1glycoproteins. Its function may be to prevent !1self-aggregation by removing the carbohydrate residues from !1the viral envelope. GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily influenza virus exo-alpha-sialidase KEYWORDS glycoprotein; glycosidase; hydrolase; transmembrane protein FEATURE !$7-23 #domain transmembrane #status predicted #label TMN\ !$24-75 #region hypervariable stalk\ !$76-454 #region head of exo-alpha-sialidase\ !$44,58,73,131,220 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 454 #molecular-weight 50143 #checksum 5745 SEQUENCE /// ENTRY NMIVU7 #type complete TITLE exo-alpha-sialidase (EC 3.2.1.18) - influenza A virus (strain USSR/90/77) ALTERNATE_NAMES neuraminidase ORGANISM #formal_name influenza A virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 18-Jun-1999 ACCESSIONS A00881 REFERENCE A00881 !$#authors Concannon, P.; Kwolek, C.J.; Salser, W.A. !$#journal J. Virol. (1984) 50:654-656 !$#title Nucleotide sequence of the influenza virus A/USSR/90/77 !1neuraminidase gene. !$#cross-references MUID:84165099; PMID:6708174 !$#accession A00881 !'##molecule_type genomic RNA !'##residues 1-470 ##label CON !'##cross-references GB:K02018; NID:g324577; PIDN:AAA43449.1; !1PID:g324578 !'##note this enzyme exists as a tetramer in the viral membrane; the !1amino-terminal hydrophobic region, i.e., residues 7-35, may !1be the membrane attachment site COMMENT This enzyme catalyzes the cleavage of the terminal sialic !1acid (N-acetylneuraminic acid) from carbohydrate chains in !1glycoproteins. Its function may be to prevent !1self-aggregation by removing the carbohydrate residues from !1the viral envelope. GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily influenza virus exo-alpha-sialidase KEYWORDS glycoprotein; glycosidase; hydrolase; transmembrane protein FEATURE !$7-23 #domain transmembrane #status predicted #label TMA\ !$24-90 #region hypervariable stalk\ !$91-470 #region head of exo-alpha-sialidase\ !$44,58,63,68,88,146, !$235,365,455 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 470 #molecular-weight 51936 #checksum 3936 SEQUENCE /// ENTRY NMIVAK #type complete TITLE exo-alpha-sialidase (EC 3.2.1.18) - influenza A virus (strain A/Kiev/59/79 [H1N1]) ALTERNATE_NAMES neuraminidase ORGANISM #formal_name influenza A virus #note host Homo sapiens (man) DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 18-Jun-1999 ACCESSIONS JN0397 REFERENCE JN0397 !$#authors Beklemishev, A.B.; Blinov, V.M.; Vassilenko, S.K.; Golovin, !1S.Y.; Karginov, V.A.; Mamayev, L.V.; Netesov, S.V.; Petrov, !1N.A.; Safronov, P.F. !$#journal Bioorg. Khim. (1985) 11:1423-1426 !$#title Nucleotide sequence of a full-length DNA copy of the !1influenza virus A/Kiev/59/79 (H1N1) neuraminidase gene. !$#cross-references MUID:86077083; PMID:4074401 !$#accession JN0397 !'##molecule_type genomic RNA !'##residues 1-470 ##label BEK !'##cross-references GB:M38335; NID:g324549; PIDN:AAA43435.1; !1PID:g324550 !'##note the authors translated the codon AGU for residue 247 as Thr !'##note this enzyme exists as a tetramer in the viral membrane; the !1amino-terminal hydrophobic region, i.e., residues 7-35, may !1be the membrane attachment site COMMENT This enzyme catalyzes the cleavage of the terminal sialic !1acid (N-acetylneuraminic acid) from carbohydrate chains in !1glycoproteins. Its function may be to prevent !1self-aggregation by removing the carbohydrate residues from !1the viral envelope. GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily influenza virus exo-alpha-sialidase KEYWORDS glycoprotein; glycosidase; hydrolase; transmembrane protein FEATURE !$7-23 #domain transmembrane #status predicted #label TM1\ !$24-90 #region hypervariable stalk\ !$91-470 #region head of exo-alpha-sialidase\ !$44,58,63,68,88,146, !$235,285,365,455 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 470 #molecular-weight 51907 #checksum 4820 SEQUENCE /// ENTRY NMIVXL #type complete TITLE exo-alpha-sialidase (EC 3.2.1.18) - influenza A virus (strain X/Leningrad/54/1 [H1N1]) ALTERNATE_NAMES neuraminidase ORGANISM #formal_name influenza A virus DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 09-Sep-1994 ACCESSIONS JN0396 REFERENCE JN0396 !$#authors Beklemishev, A.B.; Blinov, V.M.; Vassilenko, S.K.; Golovin, !1S.Y.; Karginov, V.A.; Mamayev, L.V.; Mikriukov, N.N.; !1Netesov, S.V.; Petrenko, V.A.; Petrov, N.A.; Frolov, I.V. !$#journal Bioorg. Khim. (1985) 11:628-635 !$#title Synthesis, cloning and sequencing of a full-length DNA copy !1of the influenza virus (H1N1 subtype) neuraminidase gene. !$#cross-references MUID:85307105; PMID:4038348 !$#accession JN0396 !'##molecule_type genomic RNA !'##residues 1-470 ##label BEK !'##cross-references GB:M38309 !'##note this enzyme exists as a tetramer in the viral membrane; the !1amino-terminal hydrophobic region, i.e., residues 7-35, may !1be the membrane attachment site COMMENT This enzyme catalyzes the cleavage of the terminal sialic !1acid (N-acetylneuraminic acid) from carbohydrate chains in !1glycoproteins. Its function may be to prevent !1self-aggregation by removing the carbohydrate residues from !1the viral envelope. GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily influenza virus exo-alpha-sialidase KEYWORDS glycoprotein; glycosidase; hydrolase; transmembrane protein FEATURE !$7-23 #domain transmembrane #status predicted #label TM1\ !$24-90 #region hypervariable stalk\ !$91-470 #region head of exo-alpha-sialidase\ !$44,58,63,68,88,146, !$235,365,455 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 470 #molecular-weight 51893 #checksum 4224 SEQUENCE /// ENTRY NMIV3 #type complete TITLE exo-alpha-sialidase (EC 3.2.1.18) - influenza A virus (strain A/WSN/33 [H1N1]) ALTERNATE_NAMES neuraminidase ORGANISM #formal_name influenza A virus DATE 05-Apr-1983 #sequence_revision 05-Apr-1983 #text_change 09-Sep-1994 ACCESSIONS A00882 REFERENCE A00882 !$#authors Hiti, A.L.; Nayak, D.P. !$#journal J. Virol. (1982) 41:730-734 !$#title Complete nucleotide sequence of the neuraminidase gene of !1human influenza virus A/WSN/33. !$#cross-references MUID:82192605; PMID:7077751 !$#accession A00882 !'##molecule_type genomic RNA !'##residues 1-453 ##label HIT !'##cross-references GB:J02177 !'##note this enzyme exists as a tetramer in the viral membrane; the !1amino-terminal hydrophobic region, i.e., residues 7-35, may !1be the membrane attachment site COMMENT This enzyme catalyzes the cleavage of the terminal sialic !1acid (N-acetylneuraminic acid) from carbohydrate chains in !1glycoproteins. Its function may be to prevent !1self-aggregation by removing the carbohydrate residues from !1the viral envelope. GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily influenza virus exo-alpha-sialidase KEYWORDS glycoprotein; glycosidase; hydrolase; transmembrane protein FEATURE !$7-23 #domain transmembrane #status predicted #label TMA\ !$24-74 #region hypervariable stalk\ !$75-453 #region head of exo-alpha-sialidase\ !$44,72,219,382 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 453 #molecular-weight 49623 #checksum 8948 SEQUENCE /// ENTRY NMIVEK #type complete TITLE exo-alpha-sialidase (EC 3.2.1.18) - influenza A virus (strain A/Ken/1/81[N8]) ALTERNATE_NAMES neuraminidase ORGANISM #formal_name influenza A virus DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 18-Jun-1999 ACCESSIONS B25615 REFERENCE A94349 !$#authors Dale, B.; Brown, R.; Miller, J.; White, R.T.; Air, G.M.; !1Cordell, B. !$#journal Virology (1986) 155:460-468 !$#title Nucleotide and deduced amino acid sequence of the influenza !1neuraminidase genes of two equine serotypes. !$#cross-references MUID:87071664; PMID:3788060 !$#accession B25615 !'##molecule_type mRNA !'##residues 1-470 ##label DAL !'##cross-references GB:M14917; NID:g324251; PIDN:AAA43245.1; !1PID:g324252 !'##note this enzyme exists as a tetramer in the viral membrane; the !1amino-terminal hydrophobic region, i.e., residues 7-35, may !1be the membrane attachment site COMMENT This enzyme catalyzes the cleavage of the terminal sialic !1acid (N-acetylneuraminic acid) from carbohydrate chains in !1glycoproteins. Its function may be to prevent !1self-aggregation by removing the carbohydrate residues from !1the viral envelope. GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily influenza virus exo-alpha-sialidase KEYWORDS glycoprotein; glycosidase; hydrolase; transmembrane protein FEATURE !$17-33 #domain transmembrane #status predicted #label TMM\ !$34-88 #region hypervariable stalk\ !$89-470 #region head of exo-alpha-sialidase\ !$39,46,54,84,144, !$293,398 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 470 #molecular-weight 52171 #checksum 8223 SEQUENCE /// ENTRY NMIVAA #type complete TITLE exo-alpha-sialidase (EC 3.2.1.18) - influenza A virus (strain A/shearwater/Australia/1/72 [H6N5]) ALTERNATE_NAMES neuraminidase ORGANISM #formal_name influenza A virus #note host Puffinus pacificus chlorohynchus (shearwater) DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 18-Jun-1999 ACCESSIONS A30123 REFERENCE A30123 !$#authors Harley, V.R.; Ward, C.W.; Hudson, P.J. !$#journal Virology (1989) 169:239-243 !$#title Molecular cloning and analysis of the N5 neuraminidase !1subtype from an avian influenza virus. !$#cross-references MUID:89163262; PMID:2922926 !$#accession A30123 !'##molecule_type genomic RNA !'##residues 1-468 ##label HAR !'##cross-references GB:M24740; NID:g537509; PIDN:AAA43672.1; !1PID:g537510 GENETICS !$#map_position segment 6 COMPLEX homotetramer FUNCTION !$#description catalyzes the cleavage of terminal sialic acid !1(N-acetylneuraminic acid) residues from carbohydrate chains !1of glycoproteins !$#note may prevent self-aggregation by removing carbohydrate !1residues from the viral envelope that are added by host !1enzymes CLASSIFICATION #superfamily influenza virus exo-alpha-sialidase KEYWORDS glycoprotein; glycosidase; homotetramer; hydrolase; !1transmembrane protein FEATURE !$18-34 #domain transmembrane #status predicted #label TMA\ !$35-82 #region hypervariable stalk\ !$83-468 #domain catalytic #status predicted #label CAT\ !$46,52,65,78,138,395 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 468 #molecular-weight 51589 #checksum 7525 SEQUENCE /// ENTRY NMIV9 #type complete TITLE exo-alpha-sialidase (EC 3.2.1.18) - influenza A virus (strain A/tern/Australia/G70C/75) ALTERNATE_NAMES neuraminidase ORGANISM #formal_name influenza A virus DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 18-Jun-1999 ACCESSIONS A00884 REFERENCE A00884 !$#authors Air, G.M.; Ritchie, L.R.; Laver, W.G.; Colman, P.M. !$#journal Virology (1985) 145:117-122 !$#title Gene and protein sequence of an influenza neuraminidase with !1hemagglutinin activity. !$#cross-references MUID:85246214; PMID:4013081 !$#accession A00884 !'##molecule_type genomic RNA !'##residues 1-470 ##label AIR !'##cross-references GB:M11445; NID:g324415; PIDN:AAA43353.1; !1PID:g324416 !'##note this enzyme exists as a tetramer in the viral membrane; the !1amino-terminal hydrophobic region, i.e., residues 7-35, may !1be the membrane attachment site COMMENT This enzyme catalyzes the cleavage of the terminal sialic !1acid (N-acetylneuraminic acid) from carbohydrate chains in !1glycoproteins. Its function may be to prevent !1self-aggregation by removing the carbohydrate residues from !1the viral envelope. GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily influenza virus exo-alpha-sialidase KEYWORDS glycoprotein; glycosidase; hydrolase; transmembrane protein FEATURE !$8-24 #domain transmembrane #status predicted #label TMA\ !$25-91 #region hypervariable stalk\ !$92-470 #region head of exo-alpha-sialidase\ !$63,66,87,147 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 470 #molecular-weight 52468 #checksum 7461 SEQUENCE /// ENTRY NMIVW8 #type complete TITLE exo-alpha-sialidase (EC 3.2.1.18) - influenza A virus (strain A/whale/Maine/1/84 [H13N9]) ALTERNATE_NAMES neuraminidase ORGANISM #formal_name influenza A virus DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 18-Jun-1999 ACCESSIONS A27145 REFERENCE A27145 !$#authors Air, G.M.; Webster, R.G.; Colman, P.M.; Laver, W.G. !$#journal Virology (1987) 160:346-354 !$#title Distribution of sequence differences in influenza N9 !1neuraminidase of tern and whale viruses and crystallization !1of the whale neuraminidase complexed with antibodies. !$#cross-references MUID:88019185; PMID:3660585 !$#accession A27145 !'##molecule_type mRNA !'##residues 1-470 ##label AIR !'##cross-references GB:M17812; NID:g324884; PIDN:AAA43575.1; !1PID:g324885 !'##note this enzyme exists as a tetramer in the viral membrane; the !1amino-terminal hydrophobic region, i.e., residues 7-35, may !1be the membrane attachment site COMMENT This enzyme catalyzes the cleavage of the terminal sialic !1acid (N-acetylneuraminic acid) from carbohydrate chains in !1glycoproteins. Its function may be to prevent !1self-aggregation by removing the carbohydrate residues from !1the viral envelope. GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily influenza virus exo-alpha-sialidase KEYWORDS glycoprotein; glycosidase; hydrolase; transmembrane protein FEATURE !$15-31 #domain transmembrane #status predicted #label TMA\ !$32-89 #region hypervariable stalk\ !$90-470 #region head of exo-alpha-sialidase\ !$42,52,63,66,87,147, !$202 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 470 #molecular-weight 52393 #checksum 9159 SEQUENCE /// ENTRY NMIVEA #type complete TITLE exo-alpha-sialidase (EC 3.2.1.18) - influenza A virus (strain A/Cor/16/74[N7]) ALTERNATE_NAMES neuraminidase ORGANISM #formal_name influenza A virus DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 18-Jun-1999 ACCESSIONS A25615 REFERENCE A94349 !$#authors Dale, B.; Brown, R.; Miller, J.; White, R.T.; Air, G.M.; !1Cordell, B. !$#journal Virology (1986) 155:460-468 !$#title Nucleotide and deduced amino acid sequence of the influenza !1neuraminidase genes of two equine serotypes. !$#cross-references MUID:87071664; PMID:3788060 !$#accession A25615 !'##molecule_type mRNA !'##residues 1-469 ##label DAL !'##cross-references GB:M14916; NID:g323979; PIDN:AAA43093.1; !1PID:g323980 !'##note this enzyme exists as a tetramer in the viral membrane; the !1amino-terminal hydrophobic region, i.e., residues 7-35, may !1be the membrane attachment site COMMENT This enzyme catalyzes the cleavage of the terminal sialic !1acid (N-acetylneuraminic acid) from carbohydrate chains in !1glycoproteins. Its function may be to prevent !1self-aggregation by removing the carbohydrate residues from !1the viral envelope. GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily influenza virus exo-alpha-sialidase KEYWORDS glycoprotein; glycosidase; hydrolase; transmembrane protein FEATURE !$8-24 #domain transmembrane #status predicted #label TMM\ !$25-88 #region hypervariable stalk\ !$89-469 #region head of exo-alpha-sialidase\ !$28,32,46,55,66,85, !$143,198,232,399 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 469 #molecular-weight 52014 #checksum 1327 SEQUENCE /// ENTRY NMIV2 #type complete TITLE exo-alpha-sialidase (EC 3.2.1.18) - influenza A virus (strain A/NT/60/68) ALTERNATE_NAMES neuraminidase ORGANISM #formal_name influenza A virus DATE 05-Apr-1983 #sequence_revision 05-Apr-1983 #text_change 18-Jun-1999 ACCESSIONS A00885 REFERENCE A00885 !$#authors Bentley, D.R.; Brownlee, G.G. !$#journal Nucleic Acids Res. (1982) 10:5033-5042 !$#title Sequence of the N2 neuraminidase from influenza virus A/NT/ !160/68. !$#cross-references MUID:83038653; PMID:6752886 !$#accession A00885 !'##molecule_type genomic RNA !'##residues 1-469 ##label BEN !'##cross-references GB:J02136; NID:g324487; PIDN:AAA43399.1; !1PID:g324488 !'##note this enzyme exists as a tetramer in the viral membrane; the !1amino-terminal hydrophobic region, i.e., residues 7-35, may !1be the membrane attachment site COMMENT This enzyme catalyzes the cleavage of the terminal sialic !1acid (N-acetylneuraminic acid) from carbohydrate chains in !1glycoproteins. Its function may be to prevent !1self-aggregation by removing the carbohydrate residues from !1the viral envelope. GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily influenza virus exo-alpha-sialidase KEYWORDS glycoprotein; glycosidase; hydrolase; transmembrane protein FEATURE !$7-23 #domain transmembrane #status predicted #label TMA\ !$24-90 #region hypervariable stalk\ !$91-469 #region head of exo-alpha-sialidase\ !$61,69,70,86,146, !$200,234,402 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 469 #molecular-weight 52142 #checksum 5848 SEQUENCE /// ENTRY NMIV72 #type fragment TITLE exo-alpha-sialidase (EC 3.2.1.18) - influenza A virus (strain A/Memphis/102/72 [H3N2]) (fragment) ALTERNATE_NAMES neuraminidase ORGANISM #formal_name influenza A virus DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 18-Jun-1999 ACCESSIONS A00887 REFERENCE A90462 !$#authors Blok, J.; Air, G.M. !$#journal Biochemistry (1982) 21:4001-4007 !$#title Variation in the membrane-insertion and "stalk" sequences in !1eight subtypes of influenza type A virus neuraminidase. !$#cross-references MUID:83023028; PMID:6896994 !$#accession A00887 !'##molecule_type genomic RNA !'##residues 1-91 ##label BLO !'##cross-references GB:V01091; GB:J02130; NID:g60762; PIDN:CAA24275.1; !1PID:g60763 !'##note this enzyme exists as a tetramer in the viral membrane; the !1amino-terminal hydrophobic region, i.e., residues 7-35, may !1be the membrane attachment site COMMENT This enzyme catalyzes the cleavage of the terminal sialic !1acid (N-acetylneuraminic acid) from carbohydrate chains in !1glycoproteins. Its function may be to prevent !1self-aggregation by removing the carbohydrate residues from !1the viral envelope. GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily influenza virus exo-alpha-sialidase KEYWORDS glycoprotein; glycosidase; hydrolase; transmembrane protein FEATURE !$7-23 #domain transmembrane #status predicted #label TMA\ !$24-90 #region hypervariable stalk\ !$91 #region head of exo-alpha-sialidase (fragment)\ !$61,70,86 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 91 #checksum 3266 SEQUENCE /// ENTRY NMIVN5 #type fragment TITLE exo-alpha-sialidase (EC 3.2.1.18) - influenza A virus (strain A/shearwater/Australia/72 [H6N5]) (fragment) ALTERNATE_NAMES neuraminidase ORGANISM #formal_name influenza A virus DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 18-Jun-1999 ACCESSIONS A00890 REFERENCE A90462 !$#authors Blok, J.; Air, G.M. !$#journal Biochemistry (1982) 21:4001-4007 !$#title Variation in the membrane-insertion and "stalk" sequences in !1eight subtypes of influenza type A virus neuraminidase. !$#cross-references MUID:83023028; PMID:6896994 !$#accession A00890 !'##molecule_type genomic RNA !'##residues 1-107 ##label BLO !'##cross-references GB:J02159; NID:g324511; PIDN:AAA43414.1; !1PID:g324512 !'##note this enzyme exists as a tetramer in the viral membrane; the !1amino-terminal hydrophobic region, i.e., residues 7-35, may !1be the membrane attachment site COMMENT This enzyme catalyzes the cleavage of the terminal sialic !1acid (N-acetylneuraminic acid) from carbohydrate chains in !1glycoproteins. Its function may be to prevent !1self-aggregation by removing the carbohydrate residues from !1the viral envelope. GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily influenza virus exo-alpha-sialidase KEYWORDS glycoprotein; glycosidase; hydrolase; transmembrane protein FEATURE !$7-23 #domain transmembrane #status predicted #label TMA\ !$24-82 #region hypervariable stalk\ !$83-107 #region head of exo-alpha-sialidase (fragment)\ !$46,52,65,78 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 107 #checksum 3625 SEQUENCE /// ENTRY NMIV78 #type fragment TITLE exo-alpha-sialidase (EC 3.2.1.18) - influenza A virus (strain A/black duck/Australia/702/78) (fragment) ALTERNATE_NAMES neuraminidase ORGANISM #formal_name influenza A virus DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 21-Jul-2000 ACCESSIONS A00893 REFERENCE A90462 !$#authors Blok, J.; Air, G.M. !$#journal Biochemistry (1982) 21:4001-4007 !$#title Variation in the membrane-insertion and "stalk" sequences in !1eight subtypes of influenza type A virus neuraminidase. !$#cross-references MUID:83023028; PMID:6896994 !$#accession A00893 !'##molecule_type genomic RNA !'##residues 1-102 ##label BLO !'##cross-references GB:J02101; NID:g60772; PIDN:CAA24280.1; PID:g60773 !'##note this enzyme exists as a tetramer in the viral membrane; the !1amino-terminal hydrophobic region, i.e., residues 7-35, may !1be the membrane attachment site COMMENT This enzyme catalyzes the cleavage of the terminal sialic !1acid (N-acetylneuraminic acid) from carbohydrate chains in !1glycoproteins. Its function may be to prevent !1self-aggregation by removing the carbohydrate residues from !1the viral envelope. GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily influenza virus exo-alpha-sialidase KEYWORDS glycoprotein; glycosidase; hydrolase; transmembrane protein FEATURE !$12-33 #domain transmembrane #status predicted #label TMA\ !$34-88 #region hypervariable stalk\ !$89-102 #region head of exo-alpha-sialidase (fragment)\ !$46,54,84 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 102 #checksum 3342 SEQUENCE /// ENTRY NMIVN2 #type complete TITLE exo-alpha-sialidase (EC 3.2.1.18) - influenza A virus (strain A/Victoria/3/75 [N2]) ALTERNATE_NAMES neuraminidase ORGANISM #formal_name influenza A virus DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 09-Sep-1994 ACCESSIONS A92889; A00894; A94330 REFERENCE A92889 !$#authors Van Rompuy, L.; Min Jou, W.; Huylebroeck, D.; Fiers, W. !$#journal J. Mol. Biol. (1982) 161:1-11 !$#title Complete nucleotide sequence of human influenza !1neuraminidase gene of subtype N2 (A/Victoria/3/75). !$#cross-references MUID:83111935; PMID:6185683 !$#accession A92889 !'##molecule_type genomic RNA !'##residues 1-469 ##label VAN !'##cross-references GB:J02173 COMMENT This enzyme catalyzes the cleavage of the terminal sialic !1acid (N-acetylneuraminic acid) from carbohydrate chains in !1glycoproteins. Its function may be to prevent !1self-aggregation by removing the carbohydrate residues from !1the viral envelope. GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily influenza virus exo-alpha-sialidase KEYWORDS glycoprotein; glycosidase; hydrolase; transmembrane protein FEATURE !$17-33 #domain transmembrane #status predicted #label TMA\ !$34-90 #region hypervariable stalk\ !$91-469 #region head of exo-alpha-sialidase\ !$61,70,86,146,200, !$234,402 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 469 #molecular-weight 52174 #checksum 8173 SEQUENCE /// ENTRY NMIVH3 #type complete TITLE exo-alpha-sialidase (EC 3.2.1.18) - influenza A virus (strain A/Udorn/72 [H3N2]) ALTERNATE_NAMES neuraminidase ORGANISM #formal_name influenza A virus DATE 14-Nov-1983 #sequence_revision 12-May-1994 #text_change 18-Jun-1999 ACCESSIONS A94330; A00894 REFERENCE A94330 !$#authors Markoff, L.; Lai, C.J. !$#journal Virology (1982) 119:288-297 !$#title Sequence of the influenza A/Udorn/72 (H3N2) virus !1neuraminidase gene as determined from cloned full-length !1DNA. !$#cross-references MUID:82201024; PMID:7080447 !$#accession A94330 !'##molecule_type genomic RNA !'##residues 1-469 ##label MAR !'##cross-references GB:J02168; NID:g324523; PIDN:AAA43419.1; !1PID:g324524 !'##note this enzyme exists as a tetramer in the viral membrane; the !1amino-terminal hydrophobic region, i.e., residues 7-35, may !1be the membrane attachment site COMMENT This enzyme catalyzes the cleavage of the terminal sialic !1acid (N-acetylneuraminic acid) from carbohydrate chains in !1glycoproteins. Its function may be to prevent !1self-aggregation by removing the carbohydrate residues from !1the viral envelope. GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily influenza virus exo-alpha-sialidase KEYWORDS glycoprotein; glycosidase; hydrolase; transmembrane protein FEATURE !$17-33 #domain transmembrane #status predicted #label TMA\ !$34-90 #region hypervariable stalk\ !$91-469 #region head of exo-alpha-sialidase\ !$61,70,86,146,200, !$234,402 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 469 #molecular-weight 52146 #checksum 7524 SEQUENCE /// ENTRY NMIV27 #type complete TITLE exo-alpha-sialidase (EC 3.2.1.18) - influenza A virus (strain A/RI/5-/57 [H2N2]) ALTERNATE_NAMES neuraminidase ORGANISM #formal_name influenza A virus DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 18-Jun-1999 ACCESSIONS A00895 REFERENCE A00895 !$#authors Elleman, T.C.; Azad, A.A.; Ward, C.W. !$#journal Nucleic Acids Res. (1982) 10:7005-7015 !$#title Neuraminidase gene from the early Asian strain of human !1influenza virus, A/RI/5-/57 (H2N2). !$#cross-references MUID:83090456; PMID:6294624 !$#accession A00895 !'##molecule_type genomic RNA !'##residues 1-469 ##label ELL !'##cross-references GB:J02156; NID:g324509; PIDN:AAA43413.1; !1PID:g324510 !'##note this enzyme exists as a tetramer in the viral membrane; the !1amino-terminal hydrophobic region, i.e., residues 7-35, may !1be the membrane attachment site COMMENT This enzyme catalyzes the cleavage of the terminal sialic !1acid (N-acetylneuraminic acid) from carbohydrate chains in !1glycoproteins. Its function may be to prevent !1self-aggregation by removing the carbohydrate residues from !1the viral envelope. GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily influenza virus exo-alpha-sialidase KEYWORDS glycoprotein; glycosidase; hydrolase; transmembrane protein FEATURE !$13-29 #domain transmembrane #status predicted #label TMA\ !$30-90 #region hypervariable stalk\ !$91-469 #region head of exo-alpha-sialidase\ !$61,69,70,86,146, !$200,234,402 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 469 #molecular-weight 52005 #checksum 5380 SEQUENCE /// ENTRY NMIV4 #type complete TITLE exo-alpha-sialidase (EC 3.2.1.18) - influenza B virus (strain B/Lee/40) ALTERNATE_NAMES neuraminidase ORGANISM #formal_name influenza B virus DATE 05-Apr-1983 #sequence_revision 05-Apr-1983 #text_change 18-Jun-1999 ACCESSIONS A00886 REFERENCE A00886 !$#authors Shaw, M.W.; Lamb, R.A.; Erickson, B.W.; Briedis, D.J.; !1Choppin, P.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:6817-6821 !$#title Complete nucleotide sequence of the neuraminidase gene of !1influenza B virus. !$#cross-references MUID:83091050; PMID:6294654 !$#accession A00886 !'##molecule_type genomic RNA !'##residues 1-466 ##label SHA !'##cross-references GB:J02095; NID:g325235; PIDN:AAA43749.1; !1PID:g325237 !'##note this enzyme exists as a tetramer in the viral membrane; the !1amino-terminal hydrophobic region, i.e., residues 7-35, may !1be the membrane attachment site COMMENT This enzyme catalyzes the cleavage of the terminal sialic !1acid (N-acetylneuraminic acid) from carbohydrate chains in !1glycoproteins. Its function may be to prevent !1self-aggregation by removing the carbohydrate residues from !1the viral envelope. GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily influenza virus exo-alpha-sialidase KEYWORDS glycoprotein; glycosidase; hydrolase; transmembrane protein FEATURE !$8-24 #domain transmembrane #status predicted #label TMA\ !$25-69 #region hypervariable stalk\ !$70-466 #region head of exo-alpha-sialidase\ !$56,64,144,284 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 466 #molecular-weight 51441 #checksum 4319 SEQUENCE /// ENTRY NMIVB1 #type complete TITLE exo-alpha-sialidase (EC 3.2.1.18) - influenza B virus (strain B/Beijing/1/87) ALTERNATE_NAMES neuraminidase ORGANISM #formal_name influenza B virus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 18-Jun-1999 ACCESSIONS B38520; C38520 REFERENCE A38520 !$#authors Burmeister, W.P.; Daniels, R.S.; Dayan, S.; Gagnon, J.; !1Cusack, S.; Ruigrok, R.W.H. !$#journal Virology (1991) 180:266-272 !$#title Sequence and crystallization of influenza virus B/Beijing/1/ !187 neuraminidase. !$#cross-references MUID:91082418; PMID:1984652 !$#accession B38520 !'##molecule_type mRNA !'##residues 1-465 ##label BUR1 !'##cross-references GB:M54967; NID:g325211; PIDN:AAA43733.1; !1PID:g325213 !$#accession C38520 !'##molecule_type protein !'##residues 69-85;87-100;102-103 ##label BUR2 GENETICS !$#map_position segment 6 COMPLEX homotetramer in the viral membrane FUNCTION !$#description catalyzes hydrolytic cleavage of the terminal sialic acid, !1N-acetylneuraminic acid, from carbohydrate chains of !1glycoproteins !$#note by removing carbohydrate residues from the viral envelope !1this activity may prevent viral self-aggregation CLASSIFICATION #superfamily influenza virus exo-alpha-sialidase KEYWORDS glycoprotein; glycosidase; homotetramer; hydrolase; !1transmembrane protein FEATURE !$8-24 #domain transmembrane #status predicted #label TMA\ !$25-69 #region variable stalk\ !$70-465 #region exo-alpha-sialidase head\ !$55,63,143,283 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 465 #molecular-weight 51487 #checksum 9018 SEQUENCE /// ENTRY A46347 #type complete TITLE exo-alpha-sialidase (EC 3.2.1.18) - influenza B virus (strain B/Memphis/3/89) ALTERNATE_NAMES neuraminidase ORGANISM #formal_name influenza B virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 18-Jun-1999 ACCESSIONS A46347 REFERENCE A46347 !$#authors Air, G.M.; Laver, W.G.; Luo, M.; Stray, S.J.; Legrone, G.; !1Webster, R.G. !$#journal Virology (1990) 177:578-587 !$#title Antigenic, sequence, and crystal variation in influenza B !1neuraminidase. !$#cross-references MUID:90320130; PMID:1695410 !$#accession A46347 !'##molecule_type genomic RNA !'##residues 1-465 ##label AIR !'##cross-references GB:M30635; NID:g325220; PIDN:AAA43739.1; !1PID:g325222 !'##note this enzyme exists as a tetramer in the viral membrane; the !1amino-terminal hydrophobic region, i.e., residues 7-35, may !1be the membrane attachment site COMMENT This enzyme catalyzes the cleavage of the terminal sialic !1acid (N-acetylneuraminic acid) from carbohydrate chains in !1glycoproteins. Its function may be to prevent !1self-aggregation by removing the carbohydrate residues from !1the viral envelope. GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily influenza virus exo-alpha-sialidase KEYWORDS glycoprotein; glycosidase; hydrolase; transmembrane protein FEATURE !$8-24 #domain transmembrane #status predicted #label TMA\ !$25-69 #region hypervariable stalk\ !$70-465 #region head of exo-alpha-sialidase\ !$55,63,143,283 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 465 #molecular-weight 51391 #checksum 9045 SEQUENCE /// ENTRY C46347 #type complete TITLE exo-alpha-sialidase (EC 3.2.1.18) - influenza B virus ALTERNATE_NAMES neuraminidase ORGANISM #formal_name influenza B virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 18-Jun-1999 ACCESSIONS C46347; B46347 REFERENCE A46347 !$#authors Air, G.M.; Laver, W.G.; Luo, M.; Stray, S.J.; Legrone, G.; !1Webster, R.G. !$#journal Virology (1990) 177:578-587 !$#title Antigenic, sequence, and crystal variation in influenza B !1neuraminidase. !$#cross-references MUID:90320130; PMID:1695410 !$#accession C46347 !'##molecule_type genomic RNA !'##residues 1-465 ##label AIR !'##cross-references GB:M30632; NID:g325208; PIDN:AAA43731.1; !1PID:g325210 !'##experimental_source strain B/Leningrad/179/86 !$#accession B46347 !'##molecule_type genomic RNA !'##residues 1-465 ##label AI2 !'##cross-references GB:M30634; NID:g325217; PIDN:AAA43737.1; !1PID:g325219 !'##experimental_source strain B/Memphis/6/86 COMMENT This enzyme exists as a tetramer in the viral membrane; the !1amino-terminal hydrophobic region may be the membrane !1attachment site. COMMENT This enzyme catalyzes the cleavage of the terminal sialic !1acid (N-acetylneuraminic acid) from carbohydrate chains in !1glycoproteins. Its function may be to prevent !1self-aggregation by removing the carbohydrate residues from !1the viral envelope. GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily influenza virus exo-alpha-sialidase KEYWORDS glycoprotein; glycosidase; hydrolase; transmembrane protein FEATURE !$8-24 #domain transmembrane #status predicted #label TMA\ !$25-69 #region hypervariable stalk\ !$70-465 #region head of exo-alpha-sialidase\ !$55,63,143,283,294 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 465 #molecular-weight 51381 #checksum 9129 SEQUENCE /// ENTRY D46347 #type complete TITLE exo-alpha-sialidase (EC 3.2.1.18) - influenza B virus (strain B/Victoria/3/85) ALTERNATE_NAMES neuraminidase ORGANISM #formal_name influenza B virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 18-Jun-1999 ACCESSIONS D46347 REFERENCE A46347 !$#authors Air, G.M.; Laver, W.G.; Luo, M.; Stray, S.J.; Legrone, G.; !1Webster, R.G. !$#journal Virology (1990) 177:578-587 !$#title Antigenic, sequence, and crystal variation in influenza B !1neuraminidase. !$#cross-references MUID:90320130; PMID:1695410 !$#accession D46347 !'##molecule_type genomic RNA !'##residues 1-465 ##label AIR !'##cross-references GB:M30639; NID:g325232; PIDN:AAA43747.1; !1PID:g325234 !'##note this enzyme exists as a tetramer in the viral membrane; the !1amino-terminal hydrophobic region, i.e., residues 7-35, may !1be the membrane attachment site COMMENT This enzyme catalyzes the cleavage of the terminal sialic !1acid (N-acetylneuraminic acid) from carbohydrate chains in !1glycoproteins. Its function may be to prevent !1self-aggregation by removing the carbohydrate residues from !1the viral envelope. GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily influenza virus exo-alpha-sialidase KEYWORDS glycoprotein; glycosidase; hydrolase; transmembrane protein FEATURE !$8-24 #domain transmembrane #status predicted #label TMA\ !$25-69 #region hypervariable stalk\ !$70-465 #region head of exo-alpha-sialidase\ !$55,63,143,283,294 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 465 #molecular-weight 51454 #checksum 437 SEQUENCE /// ENTRY E46347 #type complete TITLE exo-alpha-sialidase (EC 3.2.1.18) - influenza B virus (strain B/USSR/100/83) ALTERNATE_NAMES neuraminidase ORGANISM #formal_name influenza B virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 18-Jun-1999 ACCESSIONS E46347 REFERENCE A46347 !$#authors Air, G.M.; Laver, W.G.; Luo, M.; Stray, S.J.; Legrone, G.; !1Webster, R.G. !$#journal Virology (1990) 177:578-587 !$#title Antigenic, sequence, and crystal variation in influenza B !1neuraminidase. !$#cross-references MUID:90320130; PMID:1695410 !$#accession E46347 !'##molecule_type genomic RNA !'##residues 1-466 ##label AIR !'##cross-references GB:M30638; NID:g325229; PIDN:AAA43745.1; !1PID:g325231 !'##note this enzyme exists as a tetramer in the viral membrane; the !1amino-terminal hydrophobic region, i.e., residues 7-35, may !1be the membrane attachment site COMMENT This enzyme catalyzes the cleavage of the terminal sialic !1acid (N-acetylneuraminic acid) from carbohydrate chains in !1glycoproteins. Its function may be to prevent !1self-aggregation by removing the carbohydrate residues from !1the viral envelope. GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily influenza virus exo-alpha-sialidase KEYWORDS glycoprotein; glycosidase; hydrolase; transmembrane protein FEATURE !$8-24 #domain transmembrane #status predicted #label TMA\ !$25-69 #region hypervariable stalk\ !$70-466 #region head of exo-alpha-sialidase\ !$56,64,144,284 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 466 #molecular-weight 51513 #checksum 1296 SEQUENCE /// ENTRY F46347 #type complete TITLE exo-alpha-sialidase (EC 3.2.1.18) - influenza B virus (strain B/Oregon/5/80) ALTERNATE_NAMES neuraminidase ORGANISM #formal_name influenza B virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 18-Jun-1999 ACCESSIONS F46347 REFERENCE A46347 !$#authors Air, G.M.; Laver, W.G.; Luo, M.; Stray, S.J.; Legrone, G.; !1Webster, R.G. !$#journal Virology (1990) 177:578-587 !$#title Antigenic, sequence, and crystal variation in influenza B !1neuraminidase. !$#cross-references MUID:90320130; PMID:1695410 !$#accession F46347 !'##molecule_type genomic RNA !'##residues 1-466 ##label AIR !'##cross-references GB:M30636; NID:g325223; PIDN:AAA43741.1; !1PID:g325225 !'##note this enzyme exists as a tetramer in the viral membrane; the !1amino-terminal hydrophobic region, i.e., residues 7-35, may !1be the membrane attachment site COMMENT This enzyme catalyzes the cleavage of the terminal sialic !1acid (N-acetylneuraminic acid) from carbohydrate chains in !1glycoproteins. Its function may be to prevent !1self-aggregation by removing the carbohydrate residues from !1the viral envelope. GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily influenza virus exo-alpha-sialidase KEYWORDS glycoprotein; glycosidase; hydrolase; transmembrane protein FEATURE !$8-24 #domain transmembrane #status predicted #label TMA\ !$25-69 #region hypervariable stalk\ !$70-466 #region head of exo-alpha-sialidase\ !$56,64,144,284 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 466 #molecular-weight 51461 #checksum 1511 SEQUENCE /// ENTRY G46347 #type complete TITLE exo-alpha-sialidase (EC 3.2.1.18) - influenza B virus (strain B/Singapore/222/79) ALTERNATE_NAMES neuraminidase ORGANISM #formal_name influenza B virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 18-Jun-1999 ACCESSIONS G46347 REFERENCE A46347 !$#authors Air, G.M.; Laver, W.G.; Luo, M.; Stray, S.J.; Legrone, G.; !1Webster, R.G. !$#journal Virology (1990) 177:578-587 !$#title Antigenic, sequence, and crystal variation in influenza B !1neuraminidase. !$#cross-references MUID:90320130; PMID:1695410 !$#accession G46347 !'##molecule_type genomic RNA !'##residues 1-466 ##label AIR !'##cross-references GB:M30637; NID:g325226; PIDN:AAA43743.1; !1PID:g325228 !'##note this enzyme exists as a tetramer in the viral membrane; the !1amino-terminal hydrophobic region, i.e., residues 7-35, may !1be the membrane attachment site COMMENT This enzyme catalyzes the cleavage of the terminal sialic !1acid (N-acetylneuraminic acid) from carbohydrate chains in !1glycoproteins. Its function may be to prevent !1self-aggregation by removing the carbohydrate residues from !1the viral envelope. GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily influenza virus exo-alpha-sialidase KEYWORDS glycoprotein; glycosidase; hydrolase; transmembrane protein FEATURE !$8-24 #domain transmembrane #status predicted #label TMA\ !$25-69 #region hypervariable stalk\ !$70-466 #region head of exo-alpha-sialidase\ !$56,64,144,284 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 466 #molecular-weight 51500 #checksum 2539 SEQUENCE /// ENTRY H46347 #type complete TITLE exo-alpha-sialidase (EC 3.2.1.18) - influenza B virus (strain B/Hong Kong/8/73) ALTERNATE_NAMES neuraminidase ORGANISM #formal_name influenza B virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 18-Jun-1999 ACCESSIONS H46347 REFERENCE A46347 !$#authors Air, G.M.; Laver, W.G.; Luo, M.; Stray, S.J.; Legrone, G.; !1Webster, R.G. !$#journal Virology (1990) 177:578-587 !$#title Antigenic, sequence, and crystal variation in influenza B !1neuraminidase. !$#cross-references MUID:90320130; PMID:1695410 !$#accession H46347 !'##molecule_type genomic RNA !'##residues 1-466 ##label AIR !'##cross-references GB:M30631; NID:g325205; PIDN:AAA43729.1; !1PID:g325207 !'##note this enzyme exists as a tetramer in the viral membrane; the !1amino-terminal hydrophobic region, i.e., residues 7-35, may !1be the membrane attachment site COMMENT This enzyme catalyzes the cleavage of the terminal sialic !1acid (N-acetylneuraminic acid) from carbohydrate chains in !1glycoproteins. Its function may be to prevent !1self-aggregation by removing the carbohydrate residues from !1the viral envelope. GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily influenza virus exo-alpha-sialidase KEYWORDS glycoprotein; glycosidase; hydrolase; transmembrane protein FEATURE !$8-24 #domain transmembrane #status predicted #label TMA\ !$25-69 #region hypervariable stalk\ !$70-466 #region head of exo-alpha-sialidase\ !$56,64,144,284 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 466 #molecular-weight 51506 #checksum 3982 SEQUENCE /// ENTRY I46347 #type complete TITLE exo-alpha-sialidase (EC 3.2.1.18) - influenza B virus (strain B/Maryland/59) ALTERNATE_NAMES neuraminidase ORGANISM #formal_name influenza B virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 18-Jun-1999 ACCESSIONS I46347 REFERENCE A46347 !$#authors Air, G.M.; Laver, W.G.; Luo, M.; Stray, S.J.; Legrone, G.; !1Webster, R.G. !$#journal Virology (1990) 177:578-587 !$#title Antigenic, sequence, and crystal variation in influenza B !1neuraminidase. !$#cross-references MUID:90320130; PMID:1695410 !$#accession I46347 !'##molecule_type genomic RNA !'##residues 1-466 ##label AIR !'##cross-references GB:M30633; NID:g325214; PIDN:AAA43735.1; !1PID:g325216 !'##note this enzyme exists as a tetramer in the viral membrane; the !1amino-terminal hydrophobic region, i.e., residues 7-35, may !1be the membrane attachment site COMMENT This enzyme catalyzes the cleavage of the terminal sialic !1acid (N-acetylneuraminic acid) from carbohydrate chains in !1glycoproteins. Its function may be to prevent !1self-aggregation by removing the carbohydrate residues from !1the viral envelope. GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily influenza virus exo-alpha-sialidase KEYWORDS glycoprotein; glycosidase; hydrolase; transmembrane protein FEATURE !$8-24 #domain transmembrane #status predicted #label TMA\ !$25-69 #region hypervariable stalk\ !$70-466 #region head of exo-alpha-sialidase\ !$56,64,144,284 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 466 #molecular-weight 51501 #checksum 3317 SEQUENCE /// ENTRY ALBY #type complete TITLE alpha-glucosidase (EC 3.2.1.20) MAL62 [similarity] - yeast (Saccharomyces cerevisiae) (strain carlsbergensis JM1947) ALTERNATE_NAMES alpha-glucosidase MAL6S; maltase ORGANISM #formal_name Saccharomyces cerevisiae #variety strain carlsbergensis JM1947 DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 20-Oct-2000 ACCESSIONS S05847 REFERENCE S05847 !$#authors Hong, S.H.; Marmur, J. !$#journal Gene (1986) 41:75-84 !$#title Primary structure of the maltase gene of the MAL6 locus of !1Saccharomyces carlsbergensis. !$#cross-references MUID:86193582; PMID:3516795 !$#accession S05847 !'##molecule_type DNA !'##residues 1-584 ##label HON !'##cross-references EMBL:M12601; NID:g171886; PIDN:AAA34757.1; !1PID:g171888 !'##experimental_source strain carlsbergensis JM1947 !'##note the source is designated as Saccharomyces carlsbergensis GENETICS !$#gene MAL62; MAL6S !$#map_position 8 CLASSIFICATION #superfamily alpha-glucosidase; alpha-amylase core homology KEYWORDS glycosidase; hydrolase FEATURE !$181-352 #domain alpha-amylase core homology #label AMY SUMMARY #length 584 #molecular-weight 68183 #checksum 6034 SEQUENCE /// ENTRY A32609 #type complete TITLE alpha-glucosidase (EC 3.2.1.20) precursor, lysosomal - human ALTERNATE_NAMES acid alpha-glucosidase; acid maltase; maltase-glucoamylase ORGANISM #formal_name Homo sapiens #common_name man DATE 21-May-1990 #sequence_revision 05-Apr-1995 #text_change 18-Jun-1999 ACCESSIONS A40577; A32609; A35698; S00831; S18847; I52309; S63526 REFERENCE A40577 !$#authors Martiniuk, F.; Bodkin, M.; Tzall, S.; Hirschhorn, R. !$#journal DNA Cell Biol. (1991) 10:283-292 !$#title Isolation and partial characterization of the structural !1gene for human acid alpha glucosidase. !$#cross-references MUID:91229698; PMID:1674202 !$#accession A40577 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-952 ##label MAR !'##note order of exons in Figure 2 is incorrect REFERENCE A32609 !$#authors Martiniuk, F.; Mehler, M.; Tzall, S.; Meredith, G.; !1Hirschhorn, R. !$#journal DNA Cell Biol. (1990) 9:85-94 !$#title Sequence of the cDNA and 5'-flanking region for human acid !1alpha-glucosidase, detection of an intron in the 5' !1untranslated leader sequence, definition of 18-bp !1polymorphisms, and differences with previous cDNA and amino !1acid sequences. !$#cross-references MUID:90262651; PMID:2111708 !$#accession A32609 !'##molecule_type mRNA !'##residues 1-952 ##label MA2 !'##cross-references GB:M34424; NID:g182907; PIDN:AAA52506.1; !1PID:g182908 REFERENCE A35698 !$#authors Martiniuk, F.; Bodkin, M.; Tzall, S.; Hirschhorn, R. !$#journal Am. J. Hum. Genet. (1990) 47:440-445 !$#title Identification of the base-pair substitution responsible for !1a human acid alpha glucosidase allele with lower "affinity" !1for glycogen (GAA 2) and transient gene expression in !1deficient cells. !$#cross-references MUID:90365036; PMID:2203258 !$#contents partial sequence of GAA 2 allelic form !$#accession A35698 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-90,'N',92-129 ##label MA3 REFERENCE S00831 !$#authors Hoefsloot, L.H.; Hoogeveen-Westerveld, M.; Kroos, M.A.; van !1Beeumen, J.; Reuser, A.J.J.; Oostra, B.A. !$#journal EMBO J. (1988) 7:1697-1704 !$#title Primary structure and processing of lysosomal !1alpha-glucosidase; homology with the intestinal !1sucrase-isomaltase complex. !$#cross-references MUID:89005058; PMID:3049072 !$#accession S00831 !'##molecule_type mRNA !'##residues 1-126,'VLL',130-198,'R',200-222,'H',224-371,'L',373-401, !1'R',403-412,'TSRSTRMASGLPGH',428-575,'A',577-803, !1'VGDAAGPPGHHQRPPPGWVHHPPA',828-952 ##label HOE !'##cross-references EMBL:Y00839 !$#accession S18847 !'##molecule_type protein !'##residues 70-89;123-126,'VLL', !1130-145;204-215;230-249;332-345;349-370;394-401,'R', !1403-409;480-513;520-545;703-719;726-731;795-803 ##label HO2 REFERENCE I52309 !$#authors Lin, C.Y.; Shieh, J.J. !$#journal Biochem. Biophys. Res. Commun. (1995) 208:886-893 !$#title Identification of a de novo point mutation resulting in !1infantile form of Pompe's disease. !$#cross-references MUID:95209708; PMID:7695647 !$#accession I52309 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 631-644,'H',646-680 ##label RES !'##cross-references GB:S76893; NID:g912786; PIDN:AAB33842.1; !1PID:g912787 !'##note homozygous mutation of Asp-645 to His causes an infantile form !1of Pompe's disease REFERENCE S63526 !$#authors Fuller, M.; van der Ploeg, A.; Reuser, A.J.J.; Anson, D.S.; !1Hopwood, J.J. !$#journal Eur. J. Biochem. (1995) 234:903-909 !$#title Isolation and characterisation of a recombinant, precursor !1form of lysosomal acid alpha-glucosidase. !$#cross-references MUID:96163476; PMID:8575451 !$#accession S63526 !'##molecule_type protein !'##residues 68-74,'X',76-79,'X',81 ##label FUL COMMENT In common with other lysosomal enzymes, posttranslational !1processing includes glycosylation, phosphorylation of !1mannose residues with subsequent targeting to the lysosomes, !1and proteolytic processing at both amino and carboxyl ends. GENETICS !$#gene GDB:GAA !'##cross-references GDB:119965; OMIM:232300 !$#map_position 17q23-17q23 !$#introns 182/3; 231/2; 286/3; 319/1; 359/1; 398/3; 442/3; 479/3; 517/ !13; 546/1; 585/2; 630/1; 680/3; 730/2; 777/3; 827/3; 882/3; !1933/3 !$#note GAA 1, GAA 2, and GAA 4 are common alleles in the normal !1population FUNCTION !$#description also has EC 3.1.2.3 activity; hydrolyzes alpha 1,4 and alpha !11,6 glycosidic links in glycogen, maltase, and isomaltose !$#note deficiency causes glycogen storage disease type II (Pompe's !1disease) CLASSIFICATION #superfamily lysosomal alpha-glucosidase; sucrase/isomaltase !1homology; trefoil homology KEYWORDS glycoprotein; glycosidase; hydrolase; lysosomal storage !1disease; lysosome; phosphoprotein FEATURE !$82-130 #domain trefoil homology #label TRF\ !$208-867 #domain sucrase/isomaltase homology #label SIM\ !$69-70 #cleavage_site Gln-Ala (unidentified proteinase) !8#status experimental\ !$82-109,92-108, !$103-127 #disulfide_bonds #status predicted\ !$122-123 #cleavage_site Met-Gly (unidentified proteinase) !8#status experimental\ !$140,233 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$203-204 #cleavage_site Arg-Ala (unidentified proteinase) !8#status experimental\ !$390,470,492,652, !$882,925 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$518 #active_site Asp #status predicted SUMMARY #length 952 #molecular-weight 105337 #checksum 3050 SEQUENCE /// ENTRY GLHQ #type complete TITLE beta-glucosidase (EC 3.2.1.21) precursor - yeast (Pichia anomala) ALTERNATE_NAMES beta-D-glucoside glucohydrolase; cellobiase; gentiobiase ORGANISM #formal_name Pichia anomala, Candida pelliculosa DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 28-May-1999 ACCESSIONS B23783 REFERENCE A93583 !$#authors Kohchi, C.; Toh-e, A. !$#journal Nucleic Acids Res. (1985) 13:6273-6282 !$#title Nucleotide sequence of Candida pelliculosa beta-glucosidase !1gene. !$#cross-references MUID:86016087; PMID:2995925 !$#accession B23783 !'##molecule_type DNA !'##residues 1-825 ##label KOH !'##cross-references GB:X02903; NID:g2632; PIDN:CAA26662.1; PID:g2634 !'##experimental_source var. acetaetherius !'##note the authors translated the codon TGT for residue 320 as Gly, !1TAT for residue 356 as Thr, GAA for residue 375 as Gln, AAT !1for residue 418 as Asp, and GAG for residue 487 as Gly COMMENT This enzyme is secreted into the periplasmic space, which !1suggests the presence of a signal sequence. CLASSIFICATION #superfamily beta-glucosidase KEYWORDS glycoprotein; glycosidase; hydrolase; polysaccharide !1degradation FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-825 #product beta-glucosidase #status predicted #label !8MAT\ !$21,34,74,97,230, !$271,328,335,537, !$550,578,667,690, !$718,733,761 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 825 #molecular-weight 89560 #checksum 8818 SEQUENCE /// ENTRY GLVK #type complete TITLE beta-glucosidase (EC 3.2.1.21) precursor - yeast (Kluyveromyces marxianus var. marxianus) ALTERNATE_NAMES beta-D-glucoside glucohydrolase; cellobiase; gentiobiase ORGANISM #formal_name Kluyveromyces marxianus var. marxianus, Candida kefyr DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 28-May-1999 ACCESSIONS A29148 REFERENCE A29148 !$#authors Raynal, A.; Gerbaud, C.; Francingues, M.C.; Guerineau, M. !$#journal Curr. Genet. (1987) 12:175-184 !$#title Sequence and transcription of the beta-glucosidase gene of !1Kluyveromyces fragilis cloned in Saccharomyces cerevisiae. !$#cross-references MUID:88210533; PMID:2835179 !$#accession A29148 !'##molecule_type DNA !'##residues 1-845 ##label RAY !'##cross-references GB:X05918; NID:g2804; PIDN:CAA29353.1; PID:g2805 CLASSIFICATION #superfamily beta-glucosidase KEYWORDS glycoprotein; glycosidase; hydrolase; polysaccharide !1degradation FEATURE !$66,304,438,621 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 845 #molecular-weight 93916 #checksum 8034 SEQUENCE /// ENTRY GLAG #type complete TITLE beta-glucosidase (EC 3.2.1.21) - Agrobacterium sp. ALTERNATE_NAMES amygdalase; cellobiase; gentiobiase ORGANISM #formal_name Agrobacterium sp. DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 25-Oct-1996 ACCESSIONS A28673; A45768 REFERENCE A28673 !$#authors Wakarchuk, W.W.; Greenberg, N.M.; Kilburn, D.G.; Miller Jr., !1R.C.; Warren, R.A.J. !$#journal J. Bacteriol. (1988) 170:301-307 !$#title Structure and transcription analysis of the gene encoding a !1cellobiase from Agrobacterium sp. strain ATCC 21400. !$#cross-references MUID:88086886; PMID:2826395 !$#accession A28673 !'##molecule_type DNA !'##residues 1-459 ##label WAK !'##experimental_source ATCC 21400 REFERENCE A45768 !$#authors Withers, S.G.; Warren, R.A.J.; Street, I.P.; Rupitz, K.; !1Kempton, J.B.; Aebersold, R. !$#journal J. Am. Chem. Soc. (1990) 112:5887-5889 !$#title Unequivocal demonstration of the involvement of a glutamate !1residue as a nucleophile in the mechanism of a "retaining" !1glycosidase. !$#accession A45768 !'##status preliminary !'##molecule_type protein !'##residues 356-362 ##label WIT GENETICS !$#gene abg FUNCTION !$#description one of the enzymes required for efficient degradation of !1cellulose to glucose; with affinity and high specificity for !1cellulose, it catalyzes the hydrolysis of terminal, !1nonreducing 1,4-linked beta-D-glucose residues CLASSIFICATION #superfamily Agrobacterium beta-glucosidase KEYWORDS glycosidase; hydrolase; polysaccharide degradation SUMMARY #length 459 #molecular-weight 51171 #checksum 6830 SEQUENCE /// ENTRY GLJY14 #type fragment TITLE beta-glucosidase (EC 3.2.1.21) precursor (clone TRE104) - white clover (fragment) ALTERNATE_NAMES linamarase ORGANISM #formal_name Trifolium repens #common_name white clover DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 18-Jun-1999 ACCESSIONS S16580; S20208 REFERENCE S16580 !$#authors Oxtoby, E.; Dunn, M.A.; Pancoro, A.; Hughes, M.A. !$#journal Plant Mol. Biol. (1991) 17:209-219 !$#title Nucleotide and derived amino acid sequence of the cyanogenic !1beta-glucosidase (linamarase) from white clover (Trifolium !1repens L.). !$#cross-references MUID:91322517; PMID:1907511 !$#accession S16580 !'##molecule_type mRNA !'##residues 1-425 ##label OXT !'##cross-references EMBL:X56733; NID:g21952; PIDN:CAA40057.1; !1PID:g21953 !$#accession S20208 !'##molecule_type protein !'##residues 12-25;125-147 ##label OX2 CLASSIFICATION #superfamily Agrobacterium beta-glucosidase KEYWORDS cyanogenesis; glycoprotein; glycosidase; hydrolase FEATURE !$1-11 #domain signal sequence (fragment) #status predicted !8#label SIG\ !$12-425 #product beta-glucosidase #status experimental #label !8MAT\ !$26,220,362,412 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 425 #checksum 8092 SEQUENCE /// ENTRY GLJY31 #type complete TITLE beta-glucosidase (EC 3.2.1.21) precursor (clone TRE361) - white clover ORGANISM #formal_name Trifolium repens #common_name white clover DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 18-Jun-1999 ACCESSIONS S16581 REFERENCE S16580 !$#authors Oxtoby, E.; Dunn, M.A.; Pancoro, A.; Hughes, M.A. !$#journal Plant Mol. Biol. (1991) 17:209-219 !$#title Nucleotide and derived amino acid sequence of the cyanogenic !1beta-glucosidase (linamarase) from white clover (Trifolium !1repens L.). !$#cross-references MUID:91322517; PMID:1907511 !$#accession S16581 !'##molecule_type mRNA !'##residues 1-493 ##label PLA !'##cross-references EMBL:X56734; NID:g21954; PIDN:CAA40058.1; !1PID:g21955 CLASSIFICATION #superfamily Agrobacterium beta-glucosidase KEYWORDS glycoprotein; glycosidase; hydrolase FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-493 #product beta-glucosidase #status predicted #label !8MAT\ !$34,335,371,412 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 493 #molecular-weight 55960 #checksum 9891 SEQUENCE /// ENTRY GLSOPL #type complete TITLE 6-phospho-beta-galactosidase (EC 3.2.1.85) - Lactococcus lactis ORGANISM #formal_name Lactococcus lactis DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 18-Jun-1999 ACCESSIONS A37168; B37168; C23696; A29896; S25781 REFERENCE A37168 !$#authors de Vos, W.M.; Gasson, M.J. !$#journal J. Gen. Microbiol. (1989) 135:1833-1846 !$#title Structure and expression of the Lactococcus lactis gene for !1phospho-beta-galactosidase (lacG) in Escherichia coli and L. !1lactis. !$#cross-references MUID:90132588; PMID:2515252 !$#accession A37168 !'##molecule_type DNA !'##residues 1-468 ##label DEV !'##cross-references GB:M28357 !$#accession B37168 !'##molecule_type protein !'##residues 1-10 ##label DE3 REFERENCE A23696 !$#authors de Vos, W.M.; Boerrigter, I.; van Rooyen, R.J.; Reiche, B.; !1Hengstenberg, W. !$#journal J. Biol. Chem. (1990) 265:22554-22560 !$#title Characterization of the lactose-specific enzymes of the !1phosphotransferase system in Lactococcus lactis. !$#cross-references MUID:91093107; PMID:2125052 !$#accession C23696 !'##molecule_type DNA !'##residues 1-468 ##label DE2 !'##cross-references GB:M60447; GB:J05748; NID:g149404; PIDN:AAA25183.1; !1PID:g149412 REFERENCE A29896 !$#authors Boizet, B.; Villeval, D.; Slos, P.; Novel, M.; Novel, G.; !1Mercenier, A. !$#journal Gene (1988) 62:249-261 !$#title Isolation and structural analysis of the !1phospho-beta-galactosidase gene from Streptococcus lactis !1Z268. !$#cross-references MUID:88212181; PMID:3130294 !$#accession A29896 !'##molecule_type DNA !'##residues 'MLFLKGLTL',1-468 ##label BOI !'##cross-references GB:M19454; NID:g153754; PIDN:AAA26949.1; !1PID:g153755 !'##experimental_source strain Z268 !'##note the source is designated as Lactococcus lactis plasmid pUCL13 REFERENCE JC1259 !$#authors Huang, D.C.; Novel, M.; Huang, X.F.; Novel, G. !$#journal Gene (1992) 118:39-46 !$#title Nonidentity between plasmid and chromosomal copies of !1ISS1-like sequences in Lactococcus lactis subsp. lactis !1CNRZ270 and their possible role in chromosomal integration !1of plasmid genes. !$#cross-references MUID:92380489; PMID:1339371 !$#accession S25781 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 192-468 ##label HUA !'##cross-references EMBL:X60456; NID:g44053; PIDN:CAA42986.1; !1PID:g44054 !'##note this sequence was submitted to the EMBL Data Library, July 1991 GENETICS !$#gene lacG FUNCTION !$#description hydrolyzes lactose 6-phosphate to glucose and galactose !16-phosphate. CLASSIFICATION #superfamily Agrobacterium beta-glucosidase KEYWORDS glycosidase; hydrolase; phosphotransferase system SUMMARY #length 468 #molecular-weight 54072 #checksum 3426 SEQUENCE /// ENTRY A27233 #type complete TITLE beta-galactosidase (EC 3.2.1.23) - Staphylococcus aureus ALTERNATE_NAMES lactase ORGANISM #formal_name Staphylococcus aureus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A27233 REFERENCE A27233 !$#authors Breidt Jr., F.; Stewart, G.C. !$#journal Appl. Environ. Microbiol. (1987) 53:969-973 !$#title Nucleotide and deduced amino acid sequences of the !1Staphylococcus aureus phospho-beta-galactosidase gene. !$#cross-references MUID:87269583; PMID:3111370 !$#accession A27233 !'##molecule_type DNA !'##residues 1-470 ##label BRE !'##cross-references GB:J03479; GB:M17729; NID:g153036; PIDN:AAA26650.1; !1PID:g153039 CLASSIFICATION #superfamily Agrobacterium beta-glucosidase KEYWORDS glycosidase; hydrolase SUMMARY #length 470 #molecular-weight 54550 #checksum 8873 SEQUENCE /// ENTRY A29897 #type complete TITLE 6-phospho-beta-galactosidase (EC 3.2.1.85) - Lactobacillus casei ORGANISM #formal_name Lactobacillus casei DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A29897 REFERENCE A29897 !$#authors Porter, E.V.; Chassy, B.M. !$#journal Gene (1988) 62:263-276 !$#title Nucleotide sequence of the beta-D-phosphogalactoside !1galactohydrolase gene of Lactobacillus casei: comparison to !1analogous pbg genes of other Gram-positive organisms. !$#cross-references MUID:88212182; PMID:3130295 !$#accession A29897 !'##molecule_type DNA !'##residues 1-474 ##label POR !'##cross-references GB:M20151; NID:g149583; PIDN:AAD15134.1; !1PID:g149584 CLASSIFICATION #superfamily Agrobacterium beta-glucosidase KEYWORDS glycosidase; hydrolase SUMMARY #length 474 #molecular-weight 53982 #checksum 64 SEQUENCE /// ENTRY GBHUA #type complete TITLE alpha-galactosidase (EC 3.2.1.22) A precursor - human ALTERNATE_NAMES alpha-D-galactoside galactohydrolase; melibiase ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1987 #sequence_revision 27-Oct-1995 #text_change 18-Jun-1999 ACCESSIONS S04081; A29608; A30214; S14879; A00896; B00896; I37140 REFERENCE S04081 !$#authors Kornreich, R.; Desnick, R.J.; Bishop, D.F. !$#journal Nucleic Acids Res. (1989) 17:3301-3302 !$#title Nucleotide sequence of the human alpha-galactosidase A gene. !$#cross-references MUID:89263745; PMID:2542896 !$#accession S04081 !'##status translation not shown !'##molecule_type DNA !'##residues 1-429 ##label KOR !'##cross-references EMBL:X14448; NID:g31755; PIDN:CAA32617.1; !1PID:g31756 REFERENCE A29608 !$#authors Quinn, M.; Hantzopoulos, P.; Fidanza, V.; Calhoun, D.H. !$#journal Gene (1987) 58:177-188 !$#title A genomic clone containing the promoter for the gene !1encoding the human lysosomal enzyme, alpha-galactosidase A. !$#cross-references MUID:88112869; PMID:2892762 !$#accession A29608 !'##molecule_type DNA !'##residues 1-64 ##label QUI !'##cross-references GB:M18242; NID:g182944; PIDN:AAA52514.1; !1PID:g553299 REFERENCE A30214 !$#authors Bishop, D.F.; Kornreich, R.; Desnick, R.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:3903-3907 !$#title Structural organization of the human alpha-galactosidase A !1gene: further evidence for the absence of a 3' untranslated !1region. !$#cross-references MUID:88234528; PMID:2836863 !$#accession A30214 !'##molecule_type DNA !'##residues 1-64 ##label BIS !'##cross-references EMBL:M20317; EMBL:J03249 REFERENCE S14879 !$#authors Koide, T.; Ishiura, M.; Iwai, K.; Inoue, M.; Kaneda, Y.; !1Okada, Y.; Uchida, T. !$#journal FEBS Lett. (1990) 259:353-356 !$#title A case of Fabry's disease in a patient with no !1alpha-galactosidase A activity caused by a single amino acid !1substitution of Pro-40 by Ser. !$#cross-references MUID:90092580; PMID:2152885 !$#accession S14879 !'##molecule_type mRNA !'##residues 1,'K',3-39,'S',41-429 ##label KOI !'##cross-references EMBL:X16889 !'##experimental_source Fabry's disease patient REFERENCE A00896 !$#authors Bishop, D.F.; Calhoun, D.H.; Bernstein, H.S.; Hantzopoulos, !1P.; Quinn, M.; Desnick, R.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:4859-4863 !$#title Human alpha-galactosidase A: nucleotide sequence of a cDNA !1clone encoding the mature enzyme. !$#cross-references MUID:86259694; PMID:3014515 !$#accession A00896 !'##molecule_type mRNA !'##residues 27-429 ##label BI2 !'##cross-references GB:M13571; NID:g178245; PIDN:AAA51676.1; !1PID:g178246 !'##experimental_source lung !$#accession B00896 !'##molecule_type protein !'##residues 32-55,'S',57-58,'R',60-65,'S',67-68;228-232,'N',234-237, !1'A';298-326;'L',334-339,'GSK',343-346;393-401 ##label BI3 REFERENCE I37140 !$#authors Tsuji, S.; Martin, B.M.; Kaslow, D.C.; Migeon, B.R.; !1Choudary, P.V.; Stubbleflied, B.K.; Mayor, J.A.; Murray, !1G.J.; Barranger, J.A.; Ginns, E.I. !$#journal Eur. J. Biochem. (1987) 165:275-280 !$#title Signal sequence and DNA-mediated expression of human !1lysosomal alpha-galactosidase A. !$#cross-references MUID:87246603; PMID:3036505 !$#accession I37140 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-429 ##label RES !'##cross-references EMBL:X05790; NID:g28535; PIDN:CAA29232.1; !1PID:g757912 GENETICS !$#gene GDB:GLA !'##cross-references GDB:119272; OMIM:301500 !$#map_position Xq21.3-Xq22 !$#introns 65/2; 123/3; 183/1; 213/3; 267/3; 333/3 CLASSIFICATION #superfamily alpha-galactosidase KEYWORDS Fabry disease; glycolipid metabolism; glycoprotein; !1glycosidase; hydrolase; lysosome FEATURE !$1-31 #domain signal sequence #status predicted #label SIG\ !$32-429 #product alpha-galactosidase A #status predicted !8#label MAT\ !$139,192,215,408 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 429 #molecular-weight 48766 #checksum 7217 SEQUENCE /// ENTRY GBBYAG #type complete TITLE alpha-galactosidase (EC 3.2.1.22) MEL1 precursor - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES alpha-D-galactoside galactohydrolase; melibiase ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 18-Jun-1999 ACCESSIONS A00897; A91527; A93595 REFERENCE A91527 !$#authors Sumner-Smith, M.; Bozzato, R.P.; Skipper, N.; Davies, R.W.; !1Hopper, J.E. !$#journal Gene (1985) 36:333-340 !$#title Analysis of the inducible MEL1 gene of Saccharomyces !1carlsbergensis and its secreted product, alpha-galactosidase !1(melibiase). !$#cross-references MUID:86083175; PMID:3000884 !$#note S. carlsbergensis !$#accession A00897 !'##molecule_type DNA !'##residues 1-471 ##label SUM1 !'##cross-references EMBL:M10604; NID:g171925; PIDN:AAA34770.1; !1PID:g171926 !$#accession A91527 !'##molecule_type protein !'##residues 19-28 ##label SUM2 REFERENCE A93595 !$#authors Liljestrom, P.L. !$#journal Nucleic Acids Res. (1985) 13:7257-7268 !$#title The nucleotide sequence of the yeast MEL1 gene. !$#cross-references MUID:86041913; PMID:2997745 !$#note S. uvarum !$#accession A93595 !'##molecule_type DNA !'##residues 1-471 ##label LIL !'##cross-references GB:X03102; NID:g3919; PIDN:CAA26888.1; PID:g3920 !'##experimental_source ATCC 9080 COMMENT The expression of the MEL1 gene is induced by galactose and !1melibiose and repressed by glucose. GENETICS !$#gene MEL1 !$#map_position 2L CLASSIFICATION #superfamily alpha-galactosidase KEYWORDS glycoprotein; glycosidase; homodimer; hydrolase FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-471 #product alpha-galactosidase #status experimental !8#label MAT\ !$105,175,270,370, !$403,413,422,435,454 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 471 #molecular-weight 52101 #checksum 9295 SEQUENCE /// ENTRY GBECAG #type complete TITLE alpha-galactosidase (EC 3.2.1.22), melibiose-specific - Escherichia coli (strain K-12) ALTERNATE_NAMES alpha-D-galactoside galactohydrolase; melibiase ORGANISM #formal_name Escherichia coli DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 01-Mar-2002 ACCESSIONS A26571; S56348; F65221; I52201 REFERENCE A26571 !$#authors Liljestroem, P.L.; Liljestroem, P. !$#journal Nucleic Acids Res. (1987) 15:2213-2220 !$#title Nucleotide sequence of the melA gene, coding for !1alpha-galactosidase in Escherichia coli K-12. !$#cross-references MUID:87174747; PMID:3031590 !$#accession A26571 !'##molecule_type DNA !'##residues 1-451 ##label LIL !'##cross-references GB:X04894; NID:g41990; PIDN:CAA28581.1; PID:g41991 !'##experimental_source strain K12 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56348 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-451 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97019.1; !1PID:g536964 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65221 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-451 ##label BLAT !'##cross-references GB:AE000484; GB:U00096; NID:g2367352; !1PIDN:AAC77080.1; PID:g1790560; UWGP:b4119 !'##experimental_source strain K-12, substrain MG1655 REFERENCE I52201 !$#authors Shimamoto, T.; Yazyu, H.; Futai, M.; Tsuchiya, T. !$#journal Biochem. Biophys. Res. Commun. (1984) 121:41-46 !$#title Nucleotide sequence of the promoter region of the melibiose !1operon of Escherichia coli. !$#cross-references MUID:84231376; PMID:6329200 !$#accession I52201 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 'MGMLNLKPEVFCRFACHDEVIQASQEIC',1-52 ##label RES !'##cross-references GB:K01490; NID:g146805; PIDN:AAA24149.1; !1PID:g551819 GENETICS !$#gene melA !$#map_position 93 min FUNCTION !$#description catalyzes the hydrolysis of melibiose to glucose and !1galactose CLASSIFICATION #superfamily melibiose-specific alpha-galactosidase KEYWORDS glycoprotein; glycosidase; hydrolase SUMMARY #length 451 #molecular-weight 50657 #checksum 4499 SEQUENCE /// ENTRY A43717 #type complete TITLE alpha-galactosidase (EC 3.2.1.22), raffinose-specific - Escherichia coli plasmid D1021 ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A43717; B35160 REFERENCE A43717 !$#authors Aslanidis, C.; Schmid, K.; Schmitt, R. !$#journal J. Bacteriol. (1989) 171:6753-6763 !$#title Nucleotide sequences and operon structure of plasmid-borne !1genes mediating uptake and utilization of raffinose in !1Escherichia coli. !$#cross-references MUID:90078124; PMID:2556373 !$#accession A43717 !'##status preliminary !'##molecule_type DNA !'##residues 1-708 ##label ASL !'##cross-references GB:M27273; NID:g147504; PIDN:AAA24497.1; !1PID:g147505 REFERENCE A35160 !$#authors Aslanidis, C.; Schmitt, R. !$#journal J. Bacteriol. (1990) 172:2178-2180 !$#title Regulatory elements of the raffinose operon: nucleotide !1sequences of operator and repressor genes. !$#cross-references MUID:90202743; PMID:2180920 !$#accession B35160 !'##status preliminary !'##molecule_type DNA !'##residues 1-6 ##label AS2 !'##cross-references GB:M29849; NID:g147508; PIDN:AAA24501.1; !1PID:g551828 GENETICS !$#gene rafA !$#genome plasmid COMPLEX homotetramer FUNCTION !$#description catalyzes the hydrolysis of raffinose to galactose and !1sucrose CLASSIFICATION #superfamily raffinose-specific alpha-galactosidase KEYWORDS glycoprotein; glycosidase; hydrolase SUMMARY #length 708 #molecular-weight 81188 #checksum 4796 SEQUENCE /// ENTRY GBEC #type complete TITLE beta-galactosidase (EC 3.2.1.23) lacZ [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES beta-D-galactosidase; lactase ORGANISM #formal_name Escherichia coli DATE 24-Apr-1984 #sequence_revision 23-Sep-1997 #text_change 01-Mar-2002 ACCESSIONS A90981; A92233; A93224; S06878; I41218; H64761; I40987; !1A00898; S14637; S14639 REFERENCE A90981 !$#authors Kalnins, A.; Otto, K.; Ruther, U.; Muller-Hill, B. !$#journal EMBO J. (1983) 2:593-597 !$#title Sequence of the lacZ gene of Escherichia coli. !$#cross-references MUID:84028567; PMID:6313347 !$#accession A90981 !'##molecule_type DNA !'##residues 2-1024 ##label KAL !'##cross-references GB:V00296; NID:g41901; PIDN:CAA23573.1; !1PID:g1197203 !'##note translation of initiator Met is not shown REFERENCE A92233 !$#authors Fowler, A.V.; Zabin, I. !$#journal J. Biol. Chem. (1978) 253:5521-5525 !$#title Amino acid sequence of beta-galactosidase. XI. Peptide !1ordering procedures and the complete sequence. !$#cross-references MUID:78218239; PMID:97298 !$#accession A92233 !'##molecule_type protein !'##residues 2-1024 ##label FOW !'##note this is the final paper in a series REFERENCE A93224 !$#authors Calos, M.P.; Miller, J.H. !$#journal Nature (1980) 285:38-41 !$#title Molecular consequences of deletion formation mediated by the !1transposon Tn9. !$#cross-references MUID:80188189; PMID:6246435 !$#accession A93224 !'##molecule_type DNA !'##residues 356-476 ##label CAL REFERENCE S06878 !$#authors Ruteshouser, E.C.; Richardson, J.P. !$#journal J. Mol. Biol. (1989) 208:23-43 !$#title Identification and characterization of transcription !1termination sites in the Escherichia coli lacZ gene. !$#cross-references MUID:89362462; PMID:2475637 !$#accession S06878 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-147 ##label RUT !'##cross-references EMBL:X16313; NID:g41903; PIDN:CAA34380.1; !1PID:g41904 REFERENCE I41218 !$#authors Mikryukov, N.N.; Petrov, N.A.; Karginov, V.A.; Vassilenko, !1S.K. !$#journal Bioorg. Khim. (1980) 6:1735-1736 !$#title Nucleotide sequence of a lambda-plac 5-1 DNA region coding !1for a COOH-terminal part of Escherichia coli !1beta-galactosidase. !$#accession I41218 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 967-971,'R',973-1022,'E',1024 ##label MIK !'##cross-references GB:M38327; NID:g146061; PIDN:AAA23835.1; !1PID:g146062 REFERENCE A65162 !$#authors Jacobson, R.H.; Zhang, X.; Dubose, R.F.; Matthews, B.W. !$#submission submitted to the Brookhaven Protein Data Bank, July 1994 !$#cross-references PDB:1BGL !$#contents annotation; X-ray crystallography, 2.50 angstroms, residues !14-1024 REFERENCE A58594 !$#authors Jacobson, R.H.; Zhang, X.J.; DuBose, R.F.; Matthews, B.W. !$#journal Nature (1994) 369:761-766 !$#title Three-dimensional structure of beta-galactosidase from E. !1coli. !$#cross-references MUID:94277211; PMID:8008071 !$#contents annotation; X-ray crystallography, 2.50 angstroms REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64761 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1024 ##label BLAT !'##cross-references GB:AE000141; GB:U00096; NID:g1786532; !1PIDN:AAC73447.1; PID:g1786539; UWGP:b0344 !'##experimental_source strain K-12, substrain MG1655 REFERENCE I40987 !$#authors Prentki, P. !$#journal Gene (1992) 122:231-232 !$#title Nucleotide sequence of the classical lacZ deletion delta !1M15. !$#cross-references MUID:93083990; PMID:1339377 !$#accession I40987 !'##molecule_type DNA !'##residues 1-11,43-50 ##label RES !'##cross-references EMBL:X58252; NID:g40882; PIDN:CAA41206.1; !1PID:g40883 GENETICS !$#gene lacZ !$#map_position 8 min COMPLEX homotetramer FUNCTION !$#description catalyzes hydrolysis of lactose into galactose and glucose CLASSIFICATION #superfamily beta-galactosidase KEYWORDS glycosidase; homotetramer; hydrolase; magnesium FEATURE !$2-1024 #product beta-galactosidase #status experimental !8#label MAT\ !$2-50 #region alpha complementation\ !$51-218 #domain 1, jelly-roll beta-barrel #status predicted !8#label DM1\ !$219-334 #domain 2, fibronectin type-III fold #status !8predicted #label DM2\ !$335-627 #domain 3, distorted TIM barrel #status predicted !8#label DM3\ !$628-737 #domain 4, fibronectin type-III fold #status !8predicted #label DM4\ !$738-1024 #domain 5, anti-parallel beta-sandwich #status !8predicted #label DM5\ !$417,419,462 #binding_site magnesium (Glu, His, Glu) #status !8experimental\ !$462,504,538 #active_site Glu, Tyr, Glu #status predicted SUMMARY #length 1024 #molecular-weight 116482 #checksum 1464 SEQUENCE /// ENTRY GBECE #type complete TITLE beta-galactosidase (EC 3.2.1.23) alpha chain - Escherichia coli (strain K-12) ALTERNATE_NAMES beta-D-galactoside galactohydrolase; lactase; phospho-beta-D-galactosidase alpha-subunit ORGANISM #formal_name Escherichia coli DATE 30-Sep-1987 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS A65096; A25751; S09206 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65096 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1042 ##label BLAT !'##cross-references GB:AE000389; GB:U00096; NID:g1789451; !1PIDN:AAC76111.1; PID:g1789457; UWGP:b3076 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A93056 !$#authors Stokes, H.W.; Betts, P.W.; Hall, B.G. !$#journal Mol. Biol. Evol. (1985) 2:469-477 !$#title Sequence of the ebgA gene of Escherichia coli: comparison !1with the lacZ gene. !$#cross-references MUID:88216133; PMID:3939707 !$#accession A25751 !'##molecule_type DNA !'##residues 80-476,'R',478-651,'S',653-660,'P',662-674,'CRSWTPAKRS', !1685-724,'KCASV',730-779,'M',780-974,'G',1034,'SIT',1038, !1'CLASAPTPGAARCWTPGASGSVTSATALRCCRFLAEKLPRKAWRRMSSAQGSFPRICTR !1RIS' ##label STO !'##cross-references GB:X03228; GB:M13700; GB:M13796; NID:g41311; !1PIDN:CAA26978.1; PID:g41313 REFERENCE A92390 !$#authors Fowler, A.V.; Smith, P.J. !$#journal J. Biol. Chem. (1983) 258:10204-10207 !$#title The active site regions of lacZ and ebg beta-galactosidases !1are homologous. !$#cross-references MUID:83290932; PMID:6411710 !$#contents annotation; active site regions REFERENCE S09205 !$#authors Hall, B.G.; Betts, P.W.; Wootton, J.C. !$#journal Genetics (1989) 123:635-648 !$#title DNA sequence analysis of artificially evolved ebg enzyme and !1ebg repressor genes. !$#cross-references MUID:90128218; PMID:2515108 !$#accession S09206 !'##molecule_type DNA !'##residues 13-476,'R',478-651,'S',653-660,'P',662-779,'M',780-1037, !1'T',1039-1042 ##label HAL !'##cross-references EMBL:X52031; NID:g41307; PIDN:CAA36274.1; !1PID:g41309 COMMENT The wild-type enzyme is an ineffective lactase. Two classes !1of point mutations dramatically improve activity of the !1enzyme. GENETICS !$#gene ebgA !$#map_position 68 min COMPLEX homohexamer CLASSIFICATION #superfamily beta-galactosidase KEYWORDS glycosidase; hexamer; hydrolase; magnesium FEATURE !$413,415,461 #binding_site magnesium (Glu, His, Glu) #status !8predicted\ !$461,502,524 #active_site Glu, Tyr, Glu #status predicted SUMMARY #length 1042 #molecular-weight 119064 #checksum 5085 SEQUENCE /// ENTRY JC1266 #type complete TITLE beta-galactosidase (EC 3.2.1.23) - yeast (Kluyveromyces marxianus var. lactis) ORGANISM #formal_name Kluyveromyces marxianus var. lactis, Candida sphaerica DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 18-Aug-2000 ACCESSIONS JC1266; A05063; A29357 REFERENCE JC1266 !$#authors Poch, O.; L'Hote, H.; Dallery, V.; Debeaux, F.; Fleer, R.; !1Sodoyer, R. !$#journal Gene (1992) 118:55-63 !$#title Sequence of the Kluyveromyces lactis beta-galactosidase: !1comparison with prokaryotic enzymes and secondary structure !1analysis. !$#cross-references MUID:92380492; PMID:1511885 !$#accession JC1266 !'##molecule_type DNA !'##residues 1-1025 ##label POC !'##cross-references GB:M84410; NID:g173304; PIDN:AAA35265.1; !1PID:g173305 REFERENCE A05063 !$#authors Breunig, K.D.; Dahlems, U.; Das, S.; Hollenberg, C.P. !$#journal Nucleic Acids Res. (1984) 12:2327-2341 !$#title Analysis of a eukaryotic beta-galactosidase gene: the !1N-terminal end of the yeast Kluyveromyces lactis protein !1shows homology to the Escherichia coli lacZ gene product. !$#cross-references MUID:84169536; PMID:6324114 !$#accession A05063 !'##molecule_type DNA !'##residues 1-119 ##label BRE !'##cross-references GB:X00430; GB:M15311; NID:g2859; PIDN:CAA25128.1; !1PID:g2860 REFERENCE A29357 !$#authors Leonardo, J.M.; Bhairi, S.M.; Dickson, R.C. !$#journal Mol. Cell. Biol. (1987) 7:4369-4376 !$#title Identification of upstream activator sequences that regulate !1induction of the beta-galactosidase gene in Kluyveromyces !1lactis. !$#cross-references MUID:88142828; PMID:3125422 !$#accession A29357 !'##molecule_type DNA !'##residues 1-116,'L',118 ##label LEO !'##cross-references GB:M18108; NID:g173276; PIDN:AAA35257.1; !1PID:g173277 GENETICS !$#gene LAC4 CLASSIFICATION #superfamily beta-galactosidase KEYWORDS glycosidase; hydrolase FEATURE !$414,416,482 #binding_site magnesium (Glu, His, Glu) #status !8predicted\ !$482,523,551 #active_site Glu, Tyr, Glu #status predicted SUMMARY #length 1025 #molecular-weight 117618 #checksum 670 SEQUENCE /// ENTRY B69649 #type complete TITLE beta-galactosidase lacA - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS B69649 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69649 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-687 ##label KUN !'##cross-references GB:Z99121; GB:AL009126; NID:g2635827; !1PIDN:CAB15418.1; PID:g2635926 !'##experimental_source strain 168 GENETICS !$#gene lacA CLASSIFICATION #superfamily Bacillus beta-galactosidase SUMMARY #length 687 #molecular-weight 79260 #checksum 1562 SEQUENCE /// ENTRY A29836 #type complete TITLE beta-galactosidase (EC 3.2.1.23) I - Bacillus stearothermophilus ORGANISM #formal_name Bacillus stearothermophilus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A29836 REFERENCE A29836 !$#authors Hirata, H.; Fukazawa, T.; Negoro, S.; Okada, H. !$#journal J. Bacteriol. (1986) 166:722-727 !$#title Structure of a beta-galactosidase gene of Bacillus !1stearothermophilus. !$#cross-references MUID:86223784; PMID:3086288 !$#accession A29836 !'##molecule_type DNA !'##residues 1-672 ##label HIR !'##cross-references GB:M13466; NID:g142577; PIDN:AAA22262.1; !1PID:g142578 CLASSIFICATION #superfamily Bacillus beta-galactosidase KEYWORDS glycosidase; hydrolase SUMMARY #length 672 #molecular-weight 78052 #checksum 3397 SEQUENCE /// ENTRY A69798 #type complete TITLE beta-galactosidase homolog yesZ - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A69798 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69798 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-663 ##label KUN !'##cross-references GB:Z99107; GB:AL009126; NID:g2632866; !1PIDN:CAB12527.1; PID:g2633021 !'##experimental_source strain 168 GENETICS !$#gene yesZ CLASSIFICATION #superfamily Bacillus beta-galactosidase SUMMARY #length 663 #molecular-weight 74098 #checksum 4133 SEQUENCE /// ENTRY T44793 #type complete TITLE beta-galactosidase (EC 3.2.1.23) [validated] - Haloferax alicantei ORGANISM #formal_name Haloferax alicantei DATE 18-Feb-2000 #sequence_revision 18-Feb-2000 #text_change 18-Feb-2000 ACCESSIONS T44793 REFERENCE Z22843 !$#authors Holmes, M.L.; Dyall-Smith, M.L. !$#submission submitted to the EMBL Data Library, May 1999 !$#accession T44793 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-665 ##label HOL !'##cross-references EMBL:U70664; PIDN:AAB40123.1 !'##experimental_source strain SB1 GENETICS !$#gene bgaH COMPLEX homodimer [validated, MUID:97201076] FUNCTION !$#description EC 3.2.1.23 [validated, MUID:97201076] !$#note cleaves several different beta-galactoside substrates such !1as ONP-Gal, X-Gal and lactulose, but not lactose, and also !1has beta-D-fucosidase activity CLASSIFICATION #superfamily Bacillus beta-galactosidase KEYWORDS glycosidase; homodimer; hydrolase SUMMARY #length 665 #molecular-weight 74674 #checksum 9242 SEQUENCE /// ENTRY IFBY #type complete TITLE beta-fructofuranosidase (EC 3.2.1.26) 2 precursor - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES beta-D-fructofuranoside fructohydrolase; invertase; protein YIL162w; saccharase ORGANISM #formal_name Saccharomyces cerevisiae DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 21-Jul-2000 ACCESSIONS A00899; S50365; S24557; S05871; S05870; S59658; A27748; !1A45656 REFERENCE A00899 !$#authors Taussig, R.; Carlson, M. !$#journal Nucleic Acids Res. (1983) 11:1943-1954 !$#title Nucleotide sequence of the yeast SUC2 gene for invertase. !$#cross-references MUID:83168934; PMID:6300785 !$#accession A00899 !'##molecule_type DNA !'##residues 1-532 ##label TAU !'##cross-references EMBL:V01311; NID:g3833; PIDN:CAA24618.1; PID:g3834 REFERENCE S50349 !$#authors Lye, G.; Bowman, S.; Churcher, C. !$#submission submitted to the EMBL Data Library, December 1994 !$#accession S50365 !'##molecule_type DNA !'##residues 1-532 ##label LYE !'##cross-references GB:Z47047; EMBL:Z46921; NID:g603997; PID:g604013; !1GSPDB:GN00009; MIPS:YIL162w REFERENCE S24557 !$#authors Carlson, M.; Taussig, R.; Kustu, S.; Botstein, D. !$#journal Mol. Cell. Biol. (1983) 3:439-447 !$#title The secreted form of invertase in Saccharomyces cerevisiae !1is synthesized from mRNA encoding a signal sequence. !$#cross-references MUID:83192078; PMID:6341817 !$#accession S24557 !'##molecule_type DNA !'##residues 1-54 ##label TAU2 !'##cross-references EMBL:V01311 REFERENCE S05871 !$#authors Sarokin, L.; Carlson, M. !$#journal Mol. Cell. Biol. (1984) 4:2750-2757 !$#title Upstream region required for regulated expression of the !1glucose-repressible SUC2 gene of Saccharomyces cerevisiae. !$#cross-references MUID:85137467; PMID:6396505 !$#accession S05871 !'##molecule_type DNA !'##residues 1-25 ##label SAR !'##cross-references EMBL:K03294 REFERENCE S05870 !$#authors Kaiser, C.A.; Botstein, D. !$#journal Mol. Cell. Biol. (1986) 6:2382-2391 !$#title Secretion-defective mutations in the signal sequence for !1Saccharomyces cerevisiae invertase. !$#cross-references MUID:87064535; PMID:3537718 !$#accession S05870 !'##molecule_type DNA !'##residues 1-21 ##label KAI !'##cross-references EMBL:M13627; NID:g172781; PIDN:AAA35129.1; !1PID:g172782 REFERENCE S59658 !$#authors Xu, L. !$#submission submitted to the EMBL Data Library, January 1995 !$#accession S59658 !'##molecule_type DNA !'##residues 1-50,'P',52-66 ##label XUL !'##cross-references EMBL:U19781 REFERENCE A27748 !$#authors Reddy, V.A.; Johnson, R.S.; Biemann, K.; Williams, R.S.; !1Ziegler, F.D.; Trimble, R.B.; Maley, F. !$#journal J. Biol. Chem. (1988) 263:6978-6985 !$#title Characterization of the glycosylation sites in yeast !1external invertase. I. N-linked oligosaccharide content of !1the individual sequons. !$#cross-references MUID:88213364; PMID:3284881 !$#accession A27748 !'##molecule_type protein !'##residues 20-408,'P',410-532 ##label RED REFERENCE A45656 !$#authors Takegawa, K.; Yoshikawa, M.; Mishima, T.; Nakoshi, M.; !1Iwahara, S. !$#journal Biochem. Int. (1991) 25:585-592 !$#title Determination of glycosylation sites using a protein !1sequencer and deglycosylation of native yeast invertase by !1endo-beta-N-acetylglucosaminidase. !$#cross-references MUID:92215257; PMID:1805802 !$#accession A45656 !'##status preliminary !'##molecule_type protein !'##residues !120-30;60-68;96-102;111-116;118-124;163-169;266-270;271-278; !1350-363;367-372;'S',380-389;396-401,'SV',404-408 ##label TAK !'##note sequence extracted from NCBI backbone (NCBIP:93131, !1NCBIP:93145, NCBIP:93147, NCBIP:93150, NCBIP:93152, !1NCBIP:93154, NCBIP:93156, NCBIP:93157, NCBIP:93159, !1NCBIP:93161, NCBIP:93163, NCBIP:93165) COMMENT The secreted form of this protein is glycosylated. The !1intracellular form is not glycosylated. GENETICS !$#gene SGD:SUC2; MIPS:YIL162w !'##cross-references SGD:S0001424; MIPS:YIL162w !$#map_position 9L CLASSIFICATION #superfamily beta-fructofuranosidase KEYWORDS alternative initiators; glycoprotein; glycosidase; hydrolase FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-532 #product beta-fructofuranosidase 2, secreted form !8#status predicted #label MAT1\ !$21-532 #product beta-fructofuranosidase 2, cytosolic #status !8predicted #label MAT2\ !$23,64,97,111,118, !$165,266,275,356, !$369,384,398,512 #binding_site carbohydrate (Asn) (covalent) #link !8MAT1 #status predicted SUMMARY #length 532 #molecular-weight 60639 #checksum 184 SEQUENCE /// ENTRY S31330 #type complete TITLE inulinase (EC 3.2.1.7) - yeast (Kluyveromyces marxianus) ORGANISM #formal_name Kluyveromyces marxianus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S31330 REFERENCE S31330 !$#authors Bergkamp, R.J.M.; Mooren, A.T.A. !$#submission submitted to the EMBL Data Library, September 1992 !$#accession S31330 !'##molecule_type DNA !'##residues 1-556 ##label BER !'##cross-references EMBL:X68479; NID:g2911; PIDN:CAA48500.1; PID:g2912 CLASSIFICATION #superfamily beta-fructofuranosidase KEYWORDS glycosidase; hydrolase; polysaccharide degradation SUMMARY #length 556 #molecular-weight 62294 #checksum 5966 SEQUENCE /// ENTRY S17502 #type complete TITLE inulinase (EC 3.2.1.7) - yeast (Kluyveromyces marxianus var. marxianus) ORGANISM #formal_name Kluyveromyces marxianus var. marxianus, Candida kefyr DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S17502 REFERENCE S17502 !$#authors Laloux, O.; Cassart, J.P.; Delcour, J.; van Beeumen, J.; !1Vandenhaute, J. !$#journal FEBS Lett. (1991) 289:64-68 !$#title Cloning and sequencing of the inulinase gene of !1Kluyveromyces marxianus var. marxianus ATCC 12424. !$#cross-references MUID:91372407; PMID:1840529 !$#accession S17502 !'##molecule_type DNA !'##residues 1-555 ##label LAL !'##cross-references GB:X57202; NID:g1498231; PIDN:CAA40488.1; PID:g2910 CLASSIFICATION #superfamily beta-fructofuranosidase KEYWORDS glycosidase; hydrolase; polysaccharide degradation SUMMARY #length 555 #molecular-weight 62213 #checksum 2167 SEQUENCE /// ENTRY C43717 #type complete TITLE beta-fructofuranosidase (EC 3.2.1.26) - Escherichia coli plasmid D1021 ALTERNATE_NAMES invertase; sucrose hydrolase ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C43717 REFERENCE A43717 !$#authors Aslanidis, C.; Schmid, K.; Schmitt, R. !$#journal J. Bacteriol. (1989) 171:6753-6763 !$#title Nucleotide sequences and operon structure of plasmid-borne !1genes mediating uptake and utilization of raffinose in !1Escherichia coli. !$#cross-references MUID:90078124; PMID:2556373 !$#accession C43717 !'##molecule_type DNA !'##residues 1-476 ##label ASL !'##cross-references GB:M27273; NID:g147504; PIDN:AAA24499.1; !1PID:g147507 GENETICS !$#gene rafD !$#genome plasmid CLASSIFICATION #superfamily beta-fructofuranosidase KEYWORDS glycosidase; hydrolase SUMMARY #length 476 #molecular-weight 54327 #checksum 3002 SEQUENCE /// ENTRY S31157 #type complete TITLE beta-fructofuranosidase (EC 3.2.1.26) precursor - currant tomato ALTERNATE_NAMES vacuolar invertase ORGANISM #formal_name Lycopersicon pimpinellifolium #common_name currant tomato DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S31157; S31158; S28513; S28514 REFERENCE S31155 !$#authors Elliott, K.J.; Butler, W.O.; Dickinson, C.D.; Konno, Y.; !1Vedvick, T.S.; Fitzmaurice, L.; Mirkov, T.E. !$#journal Plant Mol. Biol. (1993) 21:515-524 !$#title Isolation and characterization of fruit vacuolar invertase !1genes from two tomato species and temporal differences in !1mRNA levels during fruit ripening. !$#cross-references MUID:93184207; PMID:8095164 !$#accession S31157 !'##molecule_type DNA !'##residues 1-636 ##label ELL !'##cross-references EMBL:Z12028; NID:g22722; PIDN:CAA78063.1; !1PID:g22723 !$#accession S31158 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type mRNA !'##residues 1-636 ##label EL2 !'##cross-references EMBL:Z12026; NID:g22718; PIDN:CAA78061.1; !1PID:g22719 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1May 1992 GENETICS !$#introns 118/1; 121/1; 407/3; 461/3; 541/2; 570/3 CLASSIFICATION #superfamily beta-fructofuranosidase KEYWORDS glycosidase; hydrolase SUMMARY #length 636 #molecular-weight 70096 #checksum 2796 SEQUENCE /// ENTRY S31155 #type complete TITLE beta-fructofuranosidase (EC 3.2.1.26) precursor - tomato ALTERNATE_NAMES beta-fructosidase; vacuolar invertase ORGANISM #formal_name Lycopersicon esculentum #common_name tomato DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S31155; S31156; S34561; S41449; S28511; S30563 REFERENCE S31155 !$#authors Elliott, K.J.; Butler, W.O.; Dickinson, C.D.; Konno, Y.; !1Vedvick, T.S.; Fitzmaurice, L.; Mirkov, T.E. !$#journal Plant Mol. Biol. (1993) 21:515-524 !$#title Isolation and characterization of fruit vacuolar invertase !1genes from two tomato species and temporal differences in !1mRNA levels during fruit ripening. !$#cross-references MUID:93184207; PMID:8095164 !$#accession S31155 !'##molecule_type DNA !'##residues 1-636 ##label ELL !'##cross-references EMBL:Z12027; NID:g22720; PIDN:CAA78062.1; !1PID:g22721 !'##experimental_source cv. UC82B !$#accession S31156 !'##molecule_type mRNA !'##residues 1-636 ##label EL2 !'##cross-references EMBL:Z12025; NID:g22716; PIDN:CAA78060.1; !1PID:g22717 !$#accession S34561 !'##molecule_type protein !'##residues 93-114;116-124;191-207;253-274;295-307 ##label EL3 REFERENCE S41449 !$#authors Davies, K.M.; Grierson, D. !$#submission submitted to the EMBL Data Library, January 1994 !$#accession S41449 !'##molecule_type mRNA !'##residues 474-636 ##label DAV !'##cross-references EMBL:X77264; NID:g452399; PIDN:CAA54480.1; !1PID:g452400 GENETICS !$#introns 118/1; 121/1; 407/3; 461/3; 541/2; 570/3 CLASSIFICATION #superfamily beta-fructofuranosidase KEYWORDS glycosidase; hydrolase FEATURE !$1-92 #domain signal sequence #status predicted #label SIG\ !$93-636 #product beta-fructofuranosidase #status predicted !8#label MAT SUMMARY #length 636 #molecular-weight 70096 #checksum 2796 SEQUENCE /// ENTRY GBECGC #type complete TITLE beta-glucuronidase (EC 3.2.1.31) uidA - Escherichia coli (strain K-12) ALTERNATE_NAMES beta-D-glucuronoside glucuronosohydrolase; gusA protein ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS C64918; I53717; A26487; S43555 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64918 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-603 ##label BLAT !'##cross-references GB:AE000257; GB:U00096; NID:g1787898; !1PIDN:AAC74689.1; PID:g1787903; UWGP:b1617 !'##experimental_source strain K-12, substrain MG1655 REFERENCE I53717 !$#authors Schlaman, H.R.; Risseeuw, E.; Franke-van Dijk, M.E.; !1Hooykaas, P.J. !$#journal Gene (1994) 138:259-260 !$#title Nucleotide sequence corrections of the uidA open reading !1frame encoding beta-glucuronidase. !$#cross-references MUID:94171050; PMID:8125312 !$#accession I53717 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-603 ##label RES !'##cross-references GB:S69414; NID:g545893; PIDN:AAB30197.1; !1PID:g545894 REFERENCE A26487 !$#authors Jefferson, R.A.; Burgess, S.M.; Hirsh, D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:8447-8451 !$#title Beta-glucuronidase from Escherichia coli as a gene-fusion !1marker. !$#cross-references MUID:87041472; PMID:3534890 !$#accession A26487 !'##molecule_type DNA !'##residues 1-419,'VHGNIS',427-603 ##label JEF !'##cross-references GB:M14641; NID:g868017; PIDN:AAA68923.1; !1PID:g868020 REFERENCE S43555 !$#authors Punt, P. !$#submission submitted to the EMBL Data Library, April 1994 !$#accession S43555 !'##status preliminary !'##molecule_type DNA !'##residues 1,'V',3-603 ##label PUN !'##cross-references EMBL:Z32701; NID:g475168; PID:g475169 COMMENT This acid hydrolase catalyzes the cleavage of a wide variety !1of beta-glucuronides. Substrates for this enzyme are !1generally water-soluble. GENETICS !$#gene uidA !$#map_position 36 min FUNCTION !$#description catalyzes hydrolysis of beta-D-glucuronoside to !1D-glucuronate and alcohol; hydrolyzes O-glycosyl compounds !$#pathway strach and glucose metabolism CLASSIFICATION #superfamily beta-glucuronidase KEYWORDS glycosidase; hydrolase SUMMARY #length 603 #molecular-weight 68447 #checksum 9170 SEQUENCE /// ENTRY HUBPHA #type complete TITLE hyalurononglucosaminidase (EC 3.2.1.35) - Streptococcus pyogenes phage H4489A ALTERNATE_NAMES hyaluronidase ORGANISM #formal_name Streptococcus pyogenes phage H4489A #note host Streptococcus pyogenes DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 03-Jun-2002 ACCESSIONS A30566 REFERENCE A30566 !$#authors Hynes, W.L.; Ferretti, J.J. !$#journal Infect. Immun. (1989) 57:533-539 !$#title Sequence analysis and expression in Escherichia coli of the !1hyaluronidase gene of Streptococcus pyogenes bacteriophage !1H4489A. !$#cross-references MUID:89108597; PMID:2643574 !$#accession A30566 !'##molecule_type DNA !'##residues 1-371 ##label HYN !'##cross-references GB:M19348; NID:g215052; PIDN:AAA98101.1; !1PID:g215053 GENETICS !$#gene hylP CLASSIFICATION #superfamily phage hyaluronoglucosaminidase KEYWORDS glycosidase; hydrolase SUMMARY #length 371 #molecular-weight 39518 #checksum 4239 SEQUENCE /// ENTRY I39759 #type complete TITLE xylan 1,4-beta-xylosidase (EC 3.2.1.37) - Bacillus stearothermophilus ORGANISM #formal_name Bacillus stearothermophilus DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Dec-1999 ACCESSIONS I39759 REFERENCE I39759 !$#authors Baba, T.; Shinke, R.; Nanmori, T. !$#journal Appl. Environ. Microbiol. (1994) 60:2252-2258 !$#title Identification and characterization of clustered genes for !1thermostable xylan-degrading enzymes, beta-xylosidase and !1xylanase, of Bacillus stearothermophilus 21. !$#cross-references MUID:94354640; PMID:8074507 !$#accession I39759 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-705 ##label RES !'##cross-references GB:D28121; NID:g456581; PIDN:BAA05667.1; !1PID:g499713 CLASSIFICATION #superfamily Bacillus stearothermophilus xylan 1, !14-beta-xylosidase KEYWORDS glycosidase; hydrolase; polysaccharide degradation SUMMARY #length 705 #molecular-weight 79834 #checksum 4656 SEQUENCE /// ENTRY EUHUGC #type complete TITLE glucosylceramidase (EC 3.2.1.45) precursor - human ALTERNATE_NAMES acid beta-glucosidase; beta-glucocerebrosidase; D-glucosyl-N-acylsphingosine glucohydrolase; glucocerebrosidase ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1987 #sequence_revision 21-Feb-1997 #text_change 01-Dec-2000 ACCESSIONS A94068; A27306; A92582; A25130; I59112; I53691; I65972; !1T08828; A00900; A25180; A61340 REFERENCE A94068 !$#authors Sorge, J.; West, C.; Westwood, B.; Beutler, E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:7289-7293 !$#title Molecular cloning and nucleotide sequence of human !1glucocerebrosidase cDNA. !$#cross-references MUID:86042651; PMID:3864160 !$#accession A94068 !'##molecule_type mRNA !'##residues 21-179,181-536 ##label SOR REFERENCE A27306 !$#authors Sorge, J.A.; West, C.; Kuhl, W.; Treger, L.; Beutler, E. !$#journal Am. J. Hum. Genet. (1987) 41:1016-1024 !$#title The human glucocerebrosidase gene has two functional ATG !1initiator codons. !$#cross-references MUID:88074307; PMID:3687939 !$#accession A27306 !'##molecule_type mRNA !'##residues 1-45 ##label SO2 !'##cross-references GB:M20248; NID:g183016; PIDN:AAA35874.1; !1PID:g183017 !'##note the use of two different initiator codons was demonstrated in a !1rabbit reticulocyte translation system REFERENCE A92582 !$#authors Tsuji, S.; Choudary, P.V.; Martin, B.M.; Winfield, S.; !1Barranger, J.A.; Ginns, E.I. !$#journal J. Biol. Chem. (1986) 261:50-53 !$#title Nucleotide sequence of cDNA containing the complete coding !1sequence for human lysosomal glucocerebrosidase. !$#cross-references MUID:86085859; PMID:3001061 !$#accession A92582 !'##molecule_type mRNA !'##residues 21-297,'L',299-508,'L',510-533,'R',535-536 ##label TSU !'##cross-references GB:K02920; NID:g183021; PIDN:AAA35877.1; !1PID:g183022 !'##experimental_source hepatoma !'##note 298-Phe was confirmed by sequencing the mature protein REFERENCE A25130 !$#authors Dinur, T.; Osiecki, K.M.; Legler, G.; Gatt, S.; Desnick, !1R.J.; Grabowski, G.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:1660-1664 !$#title Human acid beta-glucosidase: isolation and amino acid !1sequence of a peptide containing the catalytic site. !$#cross-references MUID:86149363; PMID:3456607 !$#accession A25130 !'##molecule_type protein !'##residues 469,'I',471-520 ##label DIN !'##experimental_source placenta REFERENCE I59112 !$#authors Tsuji, S.; Martin, B.M.; Barranger, J.A.; Stubblefield, !1B.K.; LaMarca, M.E.; Ginns, E.I. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:2349-2352 !$#title Genetic heterogeneity in type 1 Gaucher disease: Multiple !1genotypes in Ashkenazic and non-Ashkenazic individuals. !$#cross-references MUID:88176943; PMID:3353383 !$#accession I59112 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 409-462 ##label RES !'##cross-references GB:M20282; NID:g183019; PIDN:AAA35876.1; !1PID:g553300 REFERENCE I53691 !$#authors Imai, K.; Nakamura, M.; Yamada, M.; Asano, A.; Yokoyama, S.; !1Tsuji, S.; Ginns, E.I. !$#journal Gene (1993) 136:365-368 !$#title A novel transcript from a pseudogene for human !1glucocerebrosidase in non-Gaucher disease cells. !$#cross-references MUID:94124033; PMID:8294033 !$#accession I53691 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-508,'L',510-533,'R',535-536 ##label RE2 !'##cross-references GB:D13286; NID:g496368; PIDN:BAA02545.1; !1PID:g496369 REFERENCE I52980 !$#authors Reiner, O.; Wigderson, M.; Horowitz, M. !$#journal DNA (1988) 7:107-116 !$#title Structural analysis of the human glucocerebrosidase genes. !$#cross-references MUID:88195776; PMID:3359914 !$#accession I65972 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-508,'L',510-536 ##label RE3 !'##cross-references GB:M19285; NID:g183027; PIDN:AAA35880.1; !1PID:g183028 REFERENCE A61340 !$#authors Ginns, E.; Choudary, P.V.; Martin, B.M.; Winfield, S.; !1Stubblefield, B.; Major, J.; Merkle-Lehman, D.; Murray, !1G.J.; Bowers, L.A.; Barranger, J.A. !$#journal Biochem. Biophys. Res. Commun. (1984) 123:574-580 !$#title Isolation of cDNA clones for human beta-glucocerebrosidase !1using the lambda-gt11 expression system. !$#cross-references MUID:85022513; PMID:6091633 !$#contents annotation REFERENCE Z16482 !$#authors Winfield, S.L.; Tayebi, N.; Martin, B.M.; Ginns, E.I.; !1Sidransky, E. !$#journal Genome Res. (1997) 7:1020-1026 !$#title Identification of three additional genes contiguous to the !1glucocerebrosidase locus on chromosome 1q21: Implications !1for Gaucher Disease. !$#cross-references MUID:97474796; PMID:9331372 !$#accession T08828 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-508,'L',510-533,'R',535-536 ##label WIN !'##cross-references EMBL:AF023268; NID:g2564910; PIDN:AAC51820.1; !1PID:g2564914 GENETICS !$#gene GDB:GBA !'##cross-references GDB:119262; OMIM:230800 !$#map_position 1q21-1q21 !$#introns 9/3; 39/1; 103/1; 152/1; 196/3; 254/2; 333/3; 408/3; 463/2; !1502/2 FUNCTION !$#description catalyzes the hydrolysis of glucocerbroside !1(glucosylceramide) into glucose and ceramide CLASSIFICATION #superfamily glucosylceramidase KEYWORDS alternative initiators; Gaucher disease; glycoprotein; !1glycosidase; hydrolase; lysosomal storage disease; lysosome; !1membrane bound; sphingolipid metabolism FEATURE !$1-39 #domain (or 21-39) signal sequence #status predicted !8#label SIG\ !$40-536 #product glucosylceramidase #status predicted #label !8MPT\ !$58,98,185,309,501 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 536 #molecular-weight 59681 #checksum 3306 SEQUENCE /// ENTRY A32931 #type complete TITLE glucosylceramidase (EC 3.2.1.45) precursor - mouse ALTERNATE_NAMES acid beta-glucosidase; beta-glucocerebrosidase; D-glucosyl-N-acylsphingosine glucohydrolase ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A32931; I49683 REFERENCE A32931 !$#authors O'Neill, R.R.; Tokoro, T.; Kozak, C.A.; Brady, R.O. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:5049-5053 !$#title Comparison of the chromosomal localization of murine and !1human glucocerebrosidase genes and of the deduced amino acid !1sequences. !$#cross-references MUID:89296941; PMID:2740343 !$#accession A32931 !'##molecule_type DNA !'##residues 1-515 ##label ONE !'##cross-references GB:M24119; NID:g193449; PIDN:AAA37671.1; !1PID:g309247 REFERENCE I49683 !$#authors Carstea, E.D.; Murray, G.J.; O'Neill, R.R. !$#journal Biochem. Biophys. Res. Commun. (1992) 184:1477-1483 !$#title Molecular and functional characterization of the murine !1glucocerebrosidase gene. !$#cross-references MUID:92272748; PMID:1317175 !$#accession I49683 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-18 ##label RES !'##cross-references GB:M89949; NID:g193437; PIDN:AAA37665.1; !1PID:g193438 COMMENT This is a lysosomal enzyme which hydrolyses glucocerbroside !1(glucosylceramide) into glucose and ceramide. COMMENT All 11 residues in humam sequence known to be involved in !1mutations leading to Gaucher disease are conserved in the !1mouse sequence. GENETICS !$#gene Gba CLASSIFICATION #superfamily glucosylceramidase KEYWORDS Gaucher disease; glycoprotein; glycosidase; hydrolase; !1lysosomal storage disease; lysosome; membrane bound; !1sphingolipid metabolism FEATURE !$38,78,165,289,480 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 515 #molecular-weight 57621 #checksum 1439 SEQUENCE /// ENTRY UUHU #type complete TITLE sucrose alpha-glucosidase (EC 3.2.1.48) / oligo-1, 6-glucosidase (EC 3.2.1.10) [validated] - human ALTERNATE_NAMES limit dextrinase; small intestinal sucrase/isomaltase (SI) ORGANISM #formal_name Homo sapiens #common_name man DATE 19-Nov-1988 #sequence_revision 24-May-1996 #text_change 08-Dec-2000 ACCESSIONS S36082; A27326; S24329; A61136 REFERENCE S36082 !$#authors Lacasa, M. !$#submission submitted to the EMBL Data Library, December 1991 !$#accession S36082 !'##molecule_type mRNA !'##residues 1-1827 ##label LAC !'##cross-references EMBL:X63597; NID:g36644; PIDN:CAA45140.1; !1PID:g36645 REFERENCE A27326 !$#authors Green, F.; Edwards, Y.; Hauri, H.P.; Povey, S.; Ho, M.W.; !1Pinto, M.; Swallow, D. !$#journal Gene (1987) 57:101-110 !$#title Isolation of a cDNA probe for a human jejunal brush-border !1hydrolase, sucrase-isomaltase, and assignment of the gene !1locus to chromosome 3. !$#cross-references MUID:88112852; PMID:2962903 !$#accession A27326 !'##molecule_type mRNA !'##residues 1-661,'X',663-678 ##label GRE !'##cross-references GB:M22616 REFERENCE S24329 !$#authors Chantret, I.; Lacasa, M.; Chevalier, G.; Ruf, J.; Islam, I.; !1Mantei, N.; Edwards, Y.; Swallow, D.; Rousset, M. !$#journal Biochem. J. (1992) 285:915-923 !$#title Sequence of the complete cDNA and the 5' structure of the !1human sucrase-isomaltase gene. Possible homology with yeast !1glucoamylase. !$#cross-references MUID:92359963; PMID:1353958 !$#accession S24329 !'##molecule_type mRNA !'##residues 1-661,'F',663-931 ##label CHA !'##cross-references EMBL:X63597 REFERENCE A61136 !$#authors Gorvel, J.P.; Ferrero, A.; Chambraud, L.; Rigal, A.; !1Bonicel, J.; Maroux, S. !$#journal Gastroenterology (1991) 101:618-625 !$#title Expression of sucrase-isomaltase and dipeptidylpeptidase IV !1in human small intestine and colon. !$#cross-references MUID:91317403; PMID:1677636 !$#accession A61136 !'##molecule_type protein !'##residues 2-14,'F',16-20;1008-1015,'E',1017-1021,'TX',1024 ##label !1GOR GENETICS !$#gene GDB:SI !'##cross-references GDB:120377; OMIM:222900 !$#map_position 3q25.2-3q26.2 COMPLEX the two product chains remain associated after cleavage FUNCTION ISM !$#description oligo-1,6-glucosidase catalyzes the hydrolysis of 1, !16-alpha-D-glucosidic bonds in isomaltose and dextrins !$#pathway carbohydrate digestion FUNCTION SUC !$#description sucrose alpha-glucosidase catalyzes the hydrolysis of the 1, !12-alpha-D-glucosidic bond in sucrose and the 1, !14-alpha-D-glucosidic bonds in maltose !$#pathway carbohydrate digestion CLASSIFICATION #superfamily sucrase/isomaltase; sucrase/isomaltase !1homology; trefoil homology KEYWORDS carbohydrate digestion; duplication; glycoprotein; !1glycosidase; hydrolase; membrane protein FEATURE !$2-1007 #product oligo-1,6-glucosidase (isomaltase chain) !8#status experimental #label MAT1\ !$13-32 #domain membrane associated #status predicted #label !8TMM\ !$42-60 #region serine/threonine-rich\ !$63-109 #domain trefoil homology #label TRF1\ !$189-840 #domain sucrase/isomaltase homology #label SIM\ !$931-977 #domain trefoil homology #label TRF2\ !$1008-1827 #product sucrose alpha-glucosidase (sucrase chain) !8#status experimental #label MAT2\ !$1062-1734 #domain sucrase/isomaltase homology #label SIM2\ !$12 #binding_site carbohydrate (Ser) (covalent) #status !8absent\ !$99,437,455,823,855, !$904,926,1235,1303, !$1340,1354,1403, !$1535,1572,1675, !$1748,1763,1815 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$1007-1008 #cleavage_site Arg-Ile (trypsin) #status predicted SUMMARY #length 1827 #molecular-weight 209402 #checksum 3975 SEQUENCE /// ENTRY A23945 #type complete TITLE sucrose alpha-glucosidase (EC 3.2.1.48) / oligo-1, 6-glucosidase (EC 3.2.1.10) - rabbit ALTERNATE_NAMES small intestinal sucrase/isomaltase (SI) ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 03-Mar-1994 #sequence_revision 03-Mar-1994 #text_change 24-May-1996 ACCESSIONS A23945; B25987; A29163 REFERENCE A23945 !$#authors Hunziker, W.; Spiess, M.; Semenza, G.; Lodish, H.F. !$#journal Cell (1986) 46:227-234 !$#title The sucrase-isomaltase complex: primary structure, !1membrane-orientation, and evolution of a stalked, intrinsic !1brush border protein. !$#cross-references MUID:86245068; PMID:3755079 !$#accession A23945 !'##molecule_type mRNA !'##residues 1-1827 ##label HUN REFERENCE A25987 !$#authors Sjoestroem, H.; Noren, O.; Christiansen, L.A.; Wacker, H.; !1Spiess, M.; Bigler-Meier, B.; Rickli, E.E.; Semenza, G. !$#journal FEBS Lett. (1982) 148:321-325 !$#title N-terminal sequences of pig intestinal sucrase-isomaltase !1and pro-sucrase-isomaltase. Implications for the !1biosynthesis and membrane insertion of !1pro-sucrase-isomaltase. !$#cross-references MUID:83105704; PMID:7152027 !$#accession B25987 !'##molecule_type protein !'##residues 2-32,'XXX',36-38;1008,'N',1010-1014,'E' ##label SJ2 REFERENCE A29163 !$#authors Frank, G.; Brunner, J.; Jauser, H.; Wacker, H.; Semenza, G.; !1Zuber, H. !$#journal FEBS Lett. (1978) 96:183-188 !$#title The hydrophobic anchor of small-intestinal !1sucrase-isomaltase. N-terminal sequence of the isomaltase !1subunit. !$#cross-references MUID:79086207; PMID:729784 !$#accession A29163 !'##molecule_type protein !'##residues 2,'VNA',6-32,'XXX',36-38 ##label FRA COMMENT Carbohydrate analysis of the mature enzyme complex indicates !1both N- and O-linked glycosylation. COMPLEX the two product chains remain associated after cleavage FUNCTION ISM !$#description oligo-1,6-glucosidase catalyzes the hydrolysis of 1, !16-alpha-D-glucosidic bonds in isomaltose and dextrins !$#pathway carbohydrate digestion FUNCTION SUC !$#description sucrose alpha-glucosidase catalyzes the hydrolysis of the 1, !12-alpha-D-glucosidic bond in sucrose and the 1, !14-alpha-D-glucosidic bonds in maltose !$#pathway carbohydrate digestion CLASSIFICATION #superfamily sucrase/isomaltase; sucrase/isomaltase !1homology; trefoil homology KEYWORDS carbohydrate digestion; duplication; glycoprotein; !1glycosidase; hydrolase; membrane protein FEATURE !$2-1007 #product oligo-1,6-glucosidase (isomaltase chain) !8#status experimental #label ISO\ !$13-32 #domain membrane associated #status predicted #label !8TMM\ !$43-65 #region serine/threonine-rich\ !$63-109 #domain trefoil homology #label TRF1\ !$189-840 #domain sucrase/isomaltase homology #label SIM\ !$931-977 #domain trefoil homology #label TRF2\ !$1008-1827 #product sucrose alpha-glucosidase (sucrase chain) !8#status experimental #label SUC\ !$1062-1734 #domain sucrase/isomaltase homology #label SIM2\ !$12 #binding_site carbohydrate (Thr) (covalent) #status !8experimental\ !$99,455,859,896,904, !$1235,1303,1325, !$1340,1354,1368, !$1403,1535,1572, !$1748,1763,1799 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$1007-1008 #cleavage_site Arg-Ile (trypsin) #status predicted SUMMARY #length 1827 #molecular-weight 210254 #checksum 2690 SEQUENCE /// ENTRY G02270 #type complete TITLE alpha-N-acetylglucosaminidase (EC 3.2.1.50) - human ORGANISM #formal_name Homo sapiens #common_name man DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Dec-1999 ACCESSIONS G02270 REFERENCE H00952 !$#authors Weber, B.; Scott, H.; Hopwood, J.J. !$#submission submitted to the EMBL Data Library, November 1995 !$#accession G02270 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-743 ##label WEB !'##cross-references EMBL:U40846; NID:g1197839; PID:g1197840 GENETICS !$#gene GDB:NAGLU !'##cross-references GDB:636533 !$#map_position 17q21 !$#note deficient in Sanfilippo B syndrome CLASSIFICATION #superfamily human alpha-N-acetylglucosaminidase KEYWORDS glycosidase; hydrolase SUMMARY #length 743 #molecular-weight 82166 #checksum 993 SEQUENCE /// ENTRY HWHUFA #type complete TITLE alpha-L-fucosidase (EC 3.2.1.51) 1 precursor, tissue - human ALTERNATE_NAMES alpha-L-fucosidase I; alpha-L-fucoside fucohydrolase ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1987 #sequence_revision 30-Jun-1991 #text_change 21-Jul-2000 ACCESSIONS A33427; A00901; A61016; I54348; I37394; I84457 REFERENCE A33427 !$#authors Occhiodoro, T.; Beckmann, K.R.; Morris, C.P.; Hopwood, J.J. !$#journal Biochem. Biophys. Res. Commun. (1989) 164:439-445 !$#title Human alpha-L-fucosidase: complete coding sequence from cDNA !1clones. !$#cross-references MUID:90026416; PMID:2803312 !$#accession A33427 !'##molecule_type mRNA !'##residues 1-461 ##label OCC !'##cross-references GB:M29877; NID:g178408; PIDN:AAA35519.1; !1PID:g178409 REFERENCE A00901 !$#authors Fukushima, H.; de Wet, J.R.; O'Brien, J.S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:1262-1265 !$#title Molecular cloning of a cDNA for human alpha-L-fucosidase. !$#cross-references MUID:85140268; PMID:2983333 !$#accession A00901 !'##molecule_type mRNA !'##residues 73-263,'C',265-419 ##label FS1 !'##cross-references GB:M10355 !'##note the authors translated the codon GAA for residue 319 as Leu REFERENCE A61016 !$#authors Fukushima, H.; Nishimoto, J.; Okada, S. !$#journal J. Inherit. Metab. Dis. (1990) 13:761-765 !$#title Sequencing and expression of a full-length cDNA for human !1alpha-L-fucosidase. !$#cross-references MUID:91061435; PMID:2174090 !$#accession A61016 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-68,'T',70-87 ##label FS2 REFERENCE I54348 !$#authors Seo, H.C.; Willems, P.J.; Kretz, K.A.; Martin, B.M.; !1O'Brien, J.S. !$#journal Hum. Mol. Genet. (1993) 2:423-429 !$#title Fucosidosis: four new mutations and a new polymorphism. !$#cross-references MUID:93278392; PMID:8504303 !$#accession I54348 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-263,'C',265-461 ##label RES !'##cross-references GB:M80815; NID:g182786; PIDN:AAA52481.1; !1PID:g182788 REFERENCE I37394 !$#authors de Wet, J.R.; Fukushima, H.; Dewji, N.N.; Wilcox, E.; !1O'Brien, J.S.; Helinski, D.R. !$#journal DNA (1984) 3:437-447 !$#title Chromogenic immunodetection of human serum albumin and !1alpha-L-fucosidase clones in a human hepatoma cDNA !1expression library. !$#cross-references MUID:85076174; PMID:6096099 !$#accession I37394 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 357-393 ##label RE2 !'##cross-references EMBL:X01390; NID:g31475; PIDN:CAA25646.1; !1PID:g1335066 !$#accession I84457 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 70,'FL',73-263,'C',265-421,'P' ##label RE3 !'##cross-references GB:M10157; NID:g182778; PID:g182779 COMMENT The fucosidases hydrolyze alpha-L-fucose from glycolipids !1and oligosaccharides. GENETICS !$#gene GDB:FUCA1 !'##cross-references GDB:119237; OMIM:230000 !$#map_position 1p35-1p34 !$#introns 125/2; 170/2; 216/2; 251/3; 318/3; 382/2; 415/3 CLASSIFICATION #superfamily alpha-L-fucosidase KEYWORDS fucosidosis; glycoprotein; glycosidase; homotetramer; !1hydrolase; lysosome FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-461 #product alpha-L-fucosidase #status predicted #label !8MAT\ !$236,246,263,377 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 461 #molecular-weight 53160 #checksum 7511 SEQUENCE /// ENTRY A30364 #type complete TITLE alpha-L-fucosidase (EC 3.2.1.51) homolog precursor - slime mold (Dictyostelium discoideum) ORGANISM #formal_name Dictyostelium discoideum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A30364; B30364 REFERENCE A30364 !$#authors Mueller-Taubenberger, A.; Westphal, M.; Noegel, A.; Gerisch, !1G. !$#journal FEBS Lett. (1989) 246:185-192 !$#title A developmentally regulated gene product from Dictyostelium !1discoideum shows high homology to human alpha-L-fucosidase. !$#cross-references MUID:89211397; PMID:2540036 !$#accession A30364 !'##molecule_type DNA !'##residues 1-461 ##label MUE !'##cross-references GB:Y07497; NID:g7170; PIDN:CAA68800.1; PID:g7171 !$#accession B30364 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-461 ##label MU2 !'##cross-references EMBL:Y07497; NID:g7170; PIDN:CAA68800.1; PID:g7171 GENETICS !$#introns 36/3; 177/1; 215/1 CLASSIFICATION #superfamily alpha-L-fucosidase KEYWORDS glycoprotein; glycosidase; hydrolase FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-461 #product probable alpha-L-fucosidase #status !8predicted #label MAT\ !$90,244,308,370,380, !$408 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 461 #molecular-weight 52647 #checksum 7174 SEQUENCE /// ENTRY AOHUBA #type complete TITLE beta-N-acetylhexosaminidase (EC 3.2.1.52) alpha chain precursor [validated] - human ALTERNATE_NAMES beta-hexosaminidase alpha chain; N-acetyl-beta-D-glucosaminide N-acetylglucosaminohydrolase; N-acetyl-beta-glucosaminidase ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 08-Dec-2000 ACCESSIONS A23561; A26727; A34204; I51862; A23842; A28139; A35748; !1S04492; I64828 REFERENCE A23561 !$#authors Myerowitz, R.; Piekarz, R.; Neufeld, E.F.; Shows, T.B.; !1Suzuki, K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:7830-7834 !$#title Human beta-hexosaminidase alpha chain: coding sequence and !1homology with the beta chain. !$#cross-references MUID:86067997; PMID:2933746 !$#accession A23561 !'##molecule_type mRNA !'##residues 1-529 ##label MYE !'##cross-references GB:M16424; GB:J02704; GB:M11572; NID:g179456; !1PIDN:AAB00965.1; PID:g179458 REFERENCE A26727 !$#authors Proia, R.L.; Soravia, E. !$#journal J. Biol. Chem. (1987) 262:5677-5681 !$#title Organization of the gene encoding the human !1beta-hexosaminidase alpha-chain. !$#cross-references MUID:87194761; PMID:2952641 !$#accession A26727 !'##molecule_type DNA !'##residues 1-93 ##label PRO !'##cross-references GB:J02704 REFERENCE A34204 !$#authors Tanaka, A.; Ohno, K.; Sandhoff, K.; Maire, I.; Kolodny, !1E.H.; Brown, A.; Suzuki, K. !$#journal Am. J. Hum. Genet. (1990) 46:329-339 !$#title GM2-gangliosidosis B1 variant: analysis of !1beta-hexosaminidase alpha gene abnormalities in seven !1patients. !$#cross-references MUID:90144743; PMID:2137287 !$#accession A34204 !'##molecule_type DNA !'##residues 151-195 ##label TAN REFERENCE I51862 !$#authors Triggs-Raine, B.L.; Akerman, B.R.; Clarke, J.T.; Gravel, !1R.A. !$#journal Am. J. Hum. Genet. (1991) 49:1041-1054 !$#title Sequence of DNA flanking the exons of the HEXA gene, and !1identification of mutations in Tay-Sachs disease. !$#cross-references MUID:92026083; PMID:1833974 !$#accession I51862 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-529 ##label RES !'##cross-references GB:S62076; NID:g237703; PIDN:AAD13932.1; !1PID:g4261632 REFERENCE A23842 !$#authors Korneluk, R.G.; Mahuran, D.J.; Neote, K.; Klavins, M.H.; !1O'Dowd, B.F.; Tropak, M.; Willard, H.F.; Anderson, M.J.; !1Lowden, J.A.; Gravel, R.A. !$#journal J. Biol. Chem. (1986) 261:8407-8413 !$#title Isolation of cDNA clones coding for the alpha-subunit of !1human beta-hexosaminidase. !$#cross-references MUID:86250742; PMID:3013851 !$#accession A23842 !'##molecule_type mRNA !'##residues 40-529 ##label KOR !'##cross-references GB:M13520; NID:g179459; PIDN:AAA51827.1; !1PID:g179460 REFERENCE A92713 !$#authors Mahuran, D.J.; Neote, K.; Klavins, M.H.; Leung, A.; Gravel, !1R.A. !$#journal J. Biol. Chem. (1988) 263:4612-4618 !$#title Proteolytic processing of pro-alpha and pro-beta precursors !1from human beta-hexosaminidase. Generation of the mature !1alpha and beta-a beta-b subunits. !$#cross-references MUID:88169570; PMID:2965147 !$#accession A28139 !'##molecule_type protein !'##residues 'X',90-99 ##label MAH REFERENCE A35748 !$#authors Mahuran, D.J. !$#journal J. Biol. Chem. (1990) 265:6794-6799 !$#title Characterization of human placental beta-hexosaminidase I-2. !1Proteolytic processing intermediates of hexosaminidase A. !$#cross-references MUID:90216707; PMID:2139028 !$#accession A35748 !'##molecule_type protein !'##residues 23-24,'X',26-29,'X',31,'X';'XXX',90-96 ##label MA2 REFERENCE S04492 !$#authors Hubbes, M.; Callahan, J.; Gravel, R.; Mahuran, D. !$#journal FEBS Lett. (1989) 249:316-320 !$#title The amino-terminal sequences in the pro-alpha and -beta !1polypeptides of human lysosomal beta-hexosaminidase A and B !1are retained in the mature isozymes. !$#cross-references MUID:89290003; PMID:2525487 !$#accession S04492 !'##molecule_type protein !'##residues 1-129 ##label HUB REFERENCE I51882 !$#authors Boles, D.J.; Proia, R.L. !$#journal Am. J. Hum. Genet. (1995) 56:716-724 !$#title The molecular basis of HEXA mRNA deficiency caused by the !1most common Tay-Sachs disease mutation. !$#cross-references MUID:95193801; PMID:7887427 !$#accession I64828 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 419-443 ##label RE2 !'##cross-references GB:S76982; NID:g912780; PIDN:AAD14242.1; !1PID:g4261942 COMMENT beta-Hexosaminidase exists predominantly as an A and a B !1isozyme. The A isozyme consists of a processed form of the !1alpha chain and a processed form for the beta chain, while !1the B isozyme is a homodimer of processed forms of the beta !1chain. Some minor isozymes contain less processed forms of !1the alpha or beta chains. COMMENT beta-Hexosaminidase A is responsible for the degradation of !1GM2 gangliosides in the brain and other tissues. Lack of !1this enzyme leads to Tay-Sachs disease. GENETICS !$#gene GDB:HEXA !'##cross-references GDB:120040; OMIM:272800 !$#map_position 15q23-15q24 !$#introns 85/1; 116/1; 138/1; 153/3; 190/3; 224/3; 269/1; 329/2; 358/ !12; 382/3; 444/1; 474/2; 509/2 CLASSIFICATION #superfamily beta-hexosaminidase KEYWORDS disulfide bond; glycoprotein; glycosidase; GM2 !1gangliosidosis; hydrolase; lysosome; Tay-Sachs disease FEATURE !$1-22 #domain signal sequence #status experimental #label !8SIG\ !$23-74 #product beta-N-acetylhexosaminidase chain alpha-p !8#status experimental #label CAP\ !$91-529 #product (or 92-529) beta-N-acetylhexosaminidase !8chain alpha #status experimental #label MAT\ !$115 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$157,295 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 529 #molecular-weight 60688 #checksum 5845 SEQUENCE /// ENTRY LXBS #type complete TITLE licheninase (EC 3.2.1.73) precursor - Bacillus subtilis ALTERNATE_NAMES 1,3-1,4-beta-D-glucan 4-gluconohydrolase; beta-glucanase; lichenase CONTAINS licheninase E-1; licheninase E-2 ORGANISM #formal_name Bacillus subtilis DATE 30-Jun-1988 #sequence_revision 13-Mar-1998 #text_change 16-Jun-2000 ACCESSIONS I40370; B69594; A22914; A90026; A90027; JU0110 REFERENCE I40370 !$#authors Wolf, M.; Geczi, A.; Simon, O.; Borriss, R. !$#journal Microbiology (1995) 141:281-290 !$#title Genes encoding xylan and beta-glucan hydrolysing enzymes in !1Bacillus subtilis: characterization, mapping and !1construction of strains deficient in lichenase, cellulase !1and xylanase. !$#cross-references MUID:95219081; PMID:7704256 !$#accession I40370 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-242 ##label RES !'##cross-references EMBL:Z46862; NID:g599673; PIDN:CAA86922.1; !1PID:g599674 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69594 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-242 ##label KUN !'##cross-references GB:Z99124; GB:AL009126; NID:g2636442; !1PIDN:CAB15943.1; PID:g2636453 !'##experimental_source strain 168 REFERENCE A93526 !$#authors Murphy, N.; McConnell, D.J.; Cantwell, B.A. !$#journal Nucleic Acids Res. (1984) 12:5355-5367 !$#title The DNA sequence of the gene and genetic control sites for !1the excreted B. subtilis enzyme beta-glucanase. !$#cross-references MUID:84272222; PMID:6087283 !$#accession A22914 !'##molecule_type DNA !'##residues 1-203,'L',205-242 ##label MUR !'##cross-references EMBL:X00754; NID:g39818; PIDN:CAA25328.1; !1PID:g685236 !'##experimental_source strain C120 !'##note the authors translated the codon CAA for residue 29 as Lys and !1CCA for residue 82 as Leu REFERENCE A90026 !$#authors Tezuka, H.; Yuuki, T.; Yabuuchi, S. !$#journal Agric. Biol. Chem. (1989) 53:2335-2339 !$#title Construction of a beta-glucanase hyperproducing Bacillus !1subtilis using the cloned beta-glucanase gene and a !1multi-copy plasmid. !$#accession A90026 !'##molecule_type DNA !'##residues 1-23,'S',25-82,'S',84-242 ##label TEZ !'##cross-references DDBJ:D00518; NID:g216243; PIDN:BAA00405.1; !1PID:g216244 !'##experimental_source strain Y-25, clone pLE100 REFERENCE A90027 !$#authors Yuuki, T.; Tezuka, H.; Yabuuchi, S. !$#journal Agric. Biol. Chem. (1989) 53:2341-2346 !$#title Purification and some properties of two enzymes from a !1beta-glucanase hyperproducing strain, Bacillus subtilis !1HL-25. !$#contents annotation !$#note source was hyperproducing strain HL-25 with gene from strain !1Y-25 !$#note the amino ends of the mature forms of E-1 and E-2 are !1pyroglutamic acid and glutamine, respectively GENETICS !$#gene bglS FUNCTION !$#description catalyzes the hydrolysis of 1,4-beta-D-glucosidic bonds in !1lichenin and other 1,3- and 1,4-beta-linked polysaccharides CLASSIFICATION #superfamily licheninase KEYWORDS extracellular protein; glycosidase; hydrolase; !1polysaccharide degradation; pyroglutamic acid FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-242 #product licheninase #status predicted #label MAT\ !$29 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) (partial) #status experimental SUMMARY #length 242 #molecular-weight 27268 #checksum 4439 SEQUENCE /// ENTRY A29091 #type complete TITLE licheninase (EC 3.2.1.73) beta - Bacillus amyloliquefaciens ALTERNATE_NAMES 1,3-1,4-beta-D-glucan 4-glucanohydrolase; beta-glucanase; lichenase ORGANISM #formal_name Bacillus amyloliquefaciens DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A29091 REFERENCE A91564 !$#authors Hofemeister, J.; Kurtz, A.; Borriss, R.; Knowles, J. !$#journal Gene (1986) 49:177-187 !$#title The beta-glucanase gene from Bacillus amyloliquefaciens !1shows extensive homology with that of Bacillus subtilis. !$#cross-references MUID:87192007; PMID:3106158 !$#accession A29091 !'##molecule_type DNA !'##residues 1-239 ##label HOF !'##cross-references GB:M15674; NID:g143009; PIDN:AAA87323.1; !1PID:g143010 !'##experimental_source strain BE20/78 GENETICS !$#gene bglA CLASSIFICATION #superfamily licheninase KEYWORDS glycosidase; hydrolase; polysaccharide degradation SUMMARY #length 239 #molecular-weight 26928 #checksum 1611 SEQUENCE /// ENTRY S15388 #type complete TITLE licheninase (EC 3.2.1.73) - Bacillus licheniformis ALTERNATE_NAMES endo-beta-1,3-1,4-D-glucanase; lichenase ORGANISM #formal_name Bacillus licheniformis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S15388 REFERENCE S15388 !$#authors Lloberas, J.; Perez-Pons, J.A.; Querol, E. !$#journal Eur. J. Biochem. (1991) 197:337-343 !$#title Molecular cloning, expression and nucleotide sequence of the !1endo-beta-1,3-1,4-D-glucanase gene from Bacillus !1licheniformis. Predictive structural analyses of the encoded !1polypeptide. !$#cross-references MUID:91224124; PMID:2026156 !$#accession S15388 !'##status preliminary !'##molecule_type DNA !'##residues 1-243 ##label LLO !'##cross-references EMBL:X57279; NID:g39558; PIDN:CAA40547.1; !1PID:g39559 CLASSIFICATION #superfamily licheninase KEYWORDS glycosidase; hydrolase; polysaccharide degradation SUMMARY #length 243 #molecular-weight 27435 #checksum 9335 SEQUENCE /// ENTRY S19012 #type complete TITLE licheninase (EC 3.2.1.73) precursor - Bacillus polymyxa ALTERNATE_NAMES endo-beta-1,3-1,4-glucanase; lichenase ORGANISM #formal_name Bacillus polymyxa DATE 22-Nov-1993 #sequence_revision 10-Nov-1995 #text_change 18-Jun-1999 ACCESSIONS S19012 REFERENCE S19011 !$#authors Gosalbes, M.J.; Perez-Gonzalez, J.A.; Gonzalez, R.; Navarro, !1A. !$#journal J. Bacteriol. (1991) 173:7705-7710 !$#title Two beta-glycanase genes are clustered in Bacillus polymyxa: !1molecular cloning, expression, and sequence analysis of !1genes encoding a xylanase and an endo-beta-(1,3)-(1, !14)-glucanase. !$#cross-references MUID:92041687; PMID:1938968 !$#accession S19012 !'##status preliminary !'##molecule_type DNA !'##residues 1-238 ##label GOS !'##cross-references EMBL:X57094; NID:g48815; PIDN:CAA40379.1; !1PID:g48817 FUNCTION !$#description catalyzes the hydrolysis of 1,4-beta-D-glucosidic bonds in !1lichenin and other 1,3- and 1,4-beta-linked polysaccharides CLASSIFICATION #superfamily licheninase KEYWORDS glycosidase; hydrolase; polysaccharide degradation FEATURE !$1-26 #domain signal sequence #status predicted #label PRO\ !$27-237 #product licheninase #status predicted #label MAT\ !$56-85 #disulfide_bonds #status predicted\ !$129 #active_site Glu #status predicted SUMMARY #length 238 #molecular-weight 26919 #checksum 5765 SEQUENCE /// ENTRY S11927 #type complete TITLE licheninase (EC 3.2.1.73) precursor [validated] - Bacillus macerans ALTERNATE_NAMES endo-beta-1,3-1,4-glucanase; lichenase ORGANISM #formal_name Bacillus macerans DATE 13-Jan-1995 #sequence_revision 13-Jan-1995 #text_change 15-Sep-2000 ACCESSIONS S11927 REFERENCE S11927 !$#authors Borriss, R.; Buettner, K.; Maentsaelae, P. !$#journal Mol. Gen. Genet. (1990) 222:278-283 !$#title Structure of the beta-1,3-1,4-glucanase gene of Bacillus !1macerans: homologies to other beta-glucanases. !$#cross-references MUID:91109712; PMID:2274030 !$#accession S11927 !'##status preliminary !'##molecule_type DNA !'##residues 1-237 ##label BOR !'##cross-references EMBL:X55959; NID:g296715; PIDN:CAA39426.1; !1PID:g296716 REFERENCE A67074 !$#authors Hahn, M.; Heinemann, U. !$#submission submitted to the Brookhaven Protein Data Bank, December 1994 !$#cross-references PDB:1MAC !$#contents annotation; X-ray crystallography, 2.3 angstroms, residues !126-37,'P',39-237 !$#note recombinant form with residues 26-41 from Bacillus !1amyloliquefaciens expressed in Escherichia coli REFERENCE A47562 !$#authors Keitel, T.; Simon, O.; Borriss, R.; Heinemann, U. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:5287-5291 !$#title Molecular and active-site structure of a Bacillus 1,3-1, !14-beta-glucanase. !$#cross-references MUID:93281743; PMID:8099449 !$#contents annotation; X-ray crystallography, 2.3 angstroms !$#note recombinant form with residues 26-41 from Bacillus !1amyloliquefaciens expressed in Escherichia coli FUNCTION !$#description catalyzes the hydrolysis of 1,4-beta-D-glucosidic bonds in !1lichenin and other 1,3- and 1,4-beta-linked polysaccharides CLASSIFICATION #superfamily licheninase KEYWORDS glycosidase; hydrolase; polysaccharide degradation FEATURE !$1-25 #domain signal sequence #status predicted #label PRO\ !$26-237 #product licheninase #status experimental #label MAT\ !$55-84 #disulfide_bonds #status experimental\ !$128 #active_site Glu #status predicted SUMMARY #length 237 #molecular-weight 26589 #checksum 1681 SEQUENCE /// ENTRY S23498 #type complete TITLE licheninase (EC 3.2.1.73) licB precursor - Clostridium thermocellum ALTERNATE_NAMES beta-1,3-1,4-glucanase licB; lichenase licB ORGANISM #formal_name Clostridium thermocellum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S23498; S22137 REFERENCE S23498 !$#authors Schimming, S.; Schwarz, W.H.; Staudenbauer, W.L. !$#journal Eur. J. Biochem. (1992) 204:13-19 !$#title Structure of the Clostridium thermocellum gene licB and the !1encoded beta-1,3-1,4-glucanase. A catalytic region !1homologous to Bacillus lichenases joined to the reiterated !1domain of clostridial cellulases. !$#cross-references MUID:92155194; PMID:1740123 !$#accession S23498 !'##molecule_type DNA !'##residues 1-334 ##label SCH !'##cross-references EMBL:X63355; NID:g40697; PIDN:CAA44959.1; !1PID:g40698 GENETICS !$#gene licB CLASSIFICATION #superfamily licheninase licB; Clostridium cellulase repeat !1homology KEYWORDS glycosidase; hydrolase; polysaccharide degradation FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-334 #product licheninase #status predicted #label MAT\ !$273-296 #domain Clostridium cellulase repeat homology #label !8CCR1\ !$308-331 #domain Clostridium cellulase repeat homology #label !8CCR2 SUMMARY #length 334 #molecular-weight 37896 #checksum 1214 SEQUENCE /// ENTRY S53645 #type complete TITLE L-iduronidase (EC 3.2.1.76) precursor - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S53645; S53644 REFERENCE S53645 !$#authors Scott, H.S.; Guo, X.H.; Hopwood, J.J.; Morris, C.P. !$#journal Genomics (1992) 13:1311-1313 !$#title Structure and sequence of the human alpha-L-iduronidase !1gene. !$#cross-references MUID:92372031; PMID:1505961 !$#accession S53645 !'##status preliminary; translation not shown !'##molecule_type DNA !'##residues 1-653 ##label SCO !'##cross-references EMBL:M95739 REFERENCE S53644 !$#authors Scott, H.S.; Anson, D.S.; Orsborn, A.M.; Nelson, P.V.; !1Clements, P.R.; Morris, C.P.; Hopwood, J.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:9695-9699 !$#title Human alpha-L-iduronidase: cDNA isolation and expression. !$#cross-references MUID:92052158; PMID:1946389 !$#accession S53644 !'##status preliminary !'##molecule_type mRNA !'##residues 1-621,'A',623-653 ##label SC2 !'##cross-references EMBL:M74715; NID:g184558; PIDN:AAA81589.1; !1PID:g184559 GENETICS !$#gene GDB:IDUA !'##cross-references GDB:119327; OMIM:252800 !$#map_position 4p16.3-4p16.3 !$#introns 53/2; 100/2; 129/1; 165/1; 197/1; 264/3; 324/3; 397/1; 468/ !11; 508/3; 550/3; 576/2; 610/1 CLASSIFICATION #superfamily L-iduronidase KEYWORDS glycosidase; hydrolase; polysaccharide degradation SUMMARY #length 653 #molecular-weight 72690 #checksum 4519 SEQUENCE /// ENTRY A42420 #type complete TITLE L-iduronidase (EC 3.2.1.76) - dog ORGANISM #formal_name Canis lupus familiaris #common_name dog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A42420 REFERENCE A42420 !$#authors Stoltzfus, L.J.; Sosa-Pineda, B.; Moskowitz, S.M.; Menon, !1K.P.; Dlott, B.; Hooper, L.; Teplow, D.B.; Shull, R.M.; !1Neufeld, E.F. !$#journal J. Biol. Chem. (1992) 267:6570-6575 !$#title Cloning and characterization of cDNA encoding canine !1alpha-L-iduronidase. mRNA deficiency in !1mucopolysaccharidosis I dog. !$#cross-references MUID:92202199; PMID:1551868 !$#accession A42420 !'##status preliminary !'##molecule_type mRNA !'##residues 1-655 ##label STO !'##cross-references GB:M81893; NID:g163963; PIDN:AAA51455.1; !1PID:g163964 !'##experimental_source testis !'##note sequence extracted from NCBI backbone (NCBIP:89830) CLASSIFICATION #superfamily L-iduronidase KEYWORDS glycosidase; hydrolase; polysaccharide degradation SUMMARY #length 655 #molecular-weight 72938 #checksum 4797 SEQUENCE /// ENTRY A55683 #type complete TITLE L-iduronidase (EC 3.2.1.76) precursor - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A55683 REFERENCE A55683 !$#authors Clarke, L.A.; Nasir, J.; Zhang, H.; McDonald, H.; !1Applegarth, D.A.; Hayden, M.R.; Toone, J. !$#journal Genomics (1994) 24:311-316 !$#title Murine alpha-L-iduronidase: cDNA isolation and expression. !$#cross-references MUID:95213022; PMID:7698753 !$#accession A55683 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-634 ##label CLA !'##cross-references GB:L34111; NID:g623169; PIDN:AAC42044.1; !1PID:g623170 CLASSIFICATION #superfamily L-iduronidase KEYWORDS glycosidase; hydrolase; polysaccharide degradation SUMMARY #length 634 #molecular-weight 71180 #checksum 2249 SEQUENCE /// ENTRY EUSMAG #type complete TITLE agarase (EC 3.2.1.81) precursor - Streptomyces coelicolor ORGANISM #formal_name Streptomyces coelicolor DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 10-Dec-1999 ACCESSIONS S07322; A38804; T42037 REFERENCE S07322 !$#authors Buttner, M.J.; Fearnley, I.M.; Bibb, M.J. !$#journal Mol. Gen. Genet. (1987) 209:101-109 !$#title The agarase gene (dagA) of Streptomyces coelicolor A3(2): !1nucleotide sequence and transcriptional analysis. !$#accession S07322 !'##molecule_type DNA !'##residues 1-309 ##label BUT !'##cross-references EMBL:X05811; NID:g46837; PIDN:CAA29257.1; !1PID:g581613 !$#accession A38804 !'##molecule_type protein !'##residues 31-49,'X',51-61 ##label BUT2 !$#accession T42037 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-309 ##label BU2 !'##cross-references EMBL:X05811; PIDN:CAA29257.1 GENETICS !$#gene dagA !$#start_codon GTG FUNCTION !$#description catalyzes the hydrolysis of 1,3-beta-D-galactosidic bonds in !1agarose to release predominantly tetrasaccharide product CLASSIFICATION #superfamily agarase KEYWORDS extracellular protein; glycosidase; hydrolase; !1polysaccharide degradation FEATURE !$1-30 #domain signal sequence #status predicted #label SIG\ !$31-309 #product agarase #status experimental #label MAT SUMMARY #length 309 #molecular-weight 35164 #checksum 6673 SEQUENCE /// ENTRY EUTQI #type complete TITLE cellulose 1,4-beta-cellobiosidase (EC 3.2.1.91) I precursor - fungus (Trichoderma reesei) ALTERNATE_NAMES exo-cellobiohydrolase I ORGANISM #formal_name Trichoderma reesei DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 16-Jul-1999 ACCESSIONS A00902 REFERENCE A00902 !$#authors Shoemaker, S.; Schweickart, V.; Ladner, M.; Gelfand, D.; !1Kwok, S.; Myambo, K.; Innis, M. !$#journal Bio/Technology (1983) 1:691-696 !$#title Molecular cloning of exo-cellobiohydrolase I derived from !1Trichoderma reesei strain L27. !$#accession A00902 !'##molecule_type DNA !'##residues 1-513 ##label SHO !'##experimental_source strain L27 COMMENT This is the most abundantly produced cellulase in this !1filamentous fungus; it cleaves cellobiosyl units from the !1nonreducing ends of the cellulose polymer chains. GENETICS !$#gene CBH1 !$#introns 154/2; 386/3 FUNCTION !$#description catalyzes the hydrolysis of 1,4-beta-D-glucosidic bonds in !1cellulose to release the disaccharide cellobiose CLASSIFICATION #superfamily cellulose 1,4-beta-cellobiosidase I; fungal !1cellulose-binding domain homology KEYWORDS glycosidase; hydrolase; polysaccharide degradation FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-513 #product cellulose 1,4-beta-cellobiosidase I #status !8predicted #label MAT\ !$482-513 #domain fungal cellulose-binding domain homology !8#label FCB SUMMARY #length 513 #molecular-weight 54073 #checksum 5287 SEQUENCE /// ENTRY B48939 #type complete TITLE cellulose 1,4-beta-cellobiosidase (EC 3.2.1.91) 1-2 precursor - basidiomycete (Phanerochaete chrysosporium) ALTERNATE_NAMES exo-cellobiohydrolase cbh1-2 CONTAINS cellulose 1,4-beta-cellobiosidase 1 ORGANISM #formal_name Phanerochaete chrysosporium DATE 28-Aug-1998 #sequence_revision 28-Aug-1998 #text_change 18-Jun-1999 ACCESSIONS B48939; S20739; S20740 REFERENCE A48939 !$#authors Covert, S.F.; Vanden Wymelenberg, A.; Cullen, D. !$#journal Appl. Environ. Microbiol. (1992) 58:2168-2175 !$#title Structure, organization, and transcription of a !1cellobiohydrolase gene cluster from Phanerochaete !1chrysosporium. !$#cross-references MUID:92344372; PMID:1637155 !$#accession B48939 !'##molecule_type DNA !'##residues 1-504 ##label COV !'##cross-references EMBL:X54411; NID:g3130; PIDN:CAA38275.1; PID:g3132 !'##note sequence extracted from NCBI backbone (NCBIP:109552) REFERENCE S20739 !$#authors Covert, S.F.; Cullen, D. !$#submission submitted to the EMBL Data Library, August 1990 !$#description Molecular cloning and characterization of two closely linked !1cellulase genes from Phanerochaete chrysosporium. !$#accession S20739 !'##molecule_type DNA !'##residues 1-450 ##label CO2 !'##cross-references EMBL:X54411 GENETICS !$#introns 2/1; 202/3 FUNCTION !$#description catalyzes the hydrolysis of 1,4-beta-D-glucosidic bonds in !1cellulose to release the disaccharide cellobiose CLASSIFICATION #superfamily cellulose 1,4-beta-cellobiosidase I; fungal !1cellulose-binding domain homology KEYWORDS glycosidase; hydrolase; polysaccharide degradation FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-450 #product cellulose 1,4-beta-cellobiosidase 1 #status !8predicted #label ALT\ !$472-504 #domain fungal cellulose-binding domain homology !8#label FCB SUMMARY #length 504 #molecular-weight 51946 #checksum 2976 SEQUENCE /// ENTRY JU0150 #type complete TITLE cellulose 1,4-beta-cellobiosidase (EC 3.2.1.91) I - Penicillium janthinellum ALTERNATE_NAMES exo-cellobiohydrolase ORGANISM #formal_name Penicillium janthinellum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS JU0150; S21508 REFERENCE JU0150 !$#authors Christoph, A.K.; Weigel, T.O.; Schulz, G. !$#journal Gene (1993) 124:57-65 !$#title Cloning, sequencing, and heterologous expression of a !1cellulase-encoding cDNA (cbh1) from Penicillium !1janthinellum. !$#cross-references MUID:93178976; PMID:8440481 !$#accession JU0150 !'##molecule_type mRNA !'##residues 1-537 ##label CHR !'##cross-references EMBL:X59054; NID:g3177; PIDN:CAA41780.1; PID:g3178 !'##note the authors translated the codon ATG for residue 172 as Asn GENETICS !$#gene cbh1 CLASSIFICATION #superfamily cellulose 1,4-beta-cellobiosidase I; fungal !1cellulose-binding domain homology KEYWORDS glycosidase; hydrolase; polysaccharide degradation FEATURE !$506-537 #domain fungal cellulose-binding domain homology !8#label FCB SUMMARY #length 537 #molecular-weight 56842 #checksum 9925 SEQUENCE /// ENTRY S38794 #type complete TITLE cellulose 1,4-beta-cellobiosidase (EC 3.2.1.91) - imperfect fungus (Humicola grisea) ALTERNATE_NAMES beta-glucancellobiohydrolase; exoglucanase ORGANISM #formal_name Humicola grisea var. thermoidea DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S38794; S08240; A45869 REFERENCE S38794 !$#authors Radford, A. !$#submission submitted to the EMBL Data Library, June 1991 !$#accession S38794 !'##molecule_type DNA !'##residues 1-525 ##label RAD !'##cross-references EMBL:X17258; NID:g2760; PIDN:CAA35159.1; PID:g2761 !'##note this is a revision to the sequence from reference S08240 REFERENCE S08240 !$#authors de Oliviera Azevedo, M.; Radford, A. !$#journal Nucleic Acids Res. (1990) 18:668 !$#title Sequence of cbh-1 gene of Humicola grisea var. thermoidea. !$#cross-references MUID:90175006; PMID:2308855 !$#accession S08240 !'##molecule_type DNA !'##residues 1-299,'H',301-525 ##label DEO !'##cross-references EMBL:X17258 !'##note the authors translated the codon CAG for residue 87 as His !'##note this sequence has been revised in reference S38794 REFERENCE A45869 !$#authors Azevedo, M.; de, O.; Felipe, M.S.S.; Astolfi-Filho, S.; !1Radford, A. !$#journal J. Gen. Microbiol. (1990) 136:2569-2576 !$#title Cloning, sequencing and homologies of the cbh-1 !1(exoglucanase) gene of Humicola grisea var. thermoidea. !$#cross-references MUID:91178527; PMID:2127803 !$#accession A45869 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-20,'R',22-34,'K',36-86,'H',88-141,'V',143-157,'Y', !1159-237,'QQH',241-244,'I',246-299,'H',301-525 ##label AZE !'##cross-references GB:M64588; GB:X17258 !'##note this sequence has been revised. See entry S08240 GENETICS !$#gene cbh-1 !$#introns 138/1 CLASSIFICATION #superfamily cellulose 1,4-beta-cellobiosidase I; fungal !1cellulose-binding domain homology KEYWORDS glycosidase; hydrolase; polysaccharide degradation FEATURE !$494-525 #domain fungal cellulose-binding domain homology !8#label FCB SUMMARY #length 525 #molecular-weight 55693 #checksum 6069 SEQUENCE /// ENTRY A26160 #type complete TITLE cellulose 1,4-beta-cellobiosidase (EC 3.2.1.91) II precursor - fungus (Trichoderma reesei) ALTERNATE_NAMES exo-cellobiohydrolase II ORGANISM #formal_name Trichoderma reesei DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A26160; A26472 REFERENCE A26160 !$#authors Chen, C.M.; Gritzali, M.; Stafford, D.W. !$#journal Bio/Technology (1987) 5:274-278 !$#title Nucleotide sequence and deduced primary structure of !1cellobiohydrolase II from Trichoderma reesei. !$#accession A26160 !'##status preliminary !'##molecule_type DNA !'##residues 1-471 ##label CHE REFERENCE A26472 !$#authors Teeri, T.T.; Lehtovaara, P.; Kauppinen, S.; Salovuori, I.; !1Knowles, J. !$#journal Gene (1987) 51:43-52 !$#title Homologous domains in Trichoderma reesei cellulolytic !1enzymes: gene sequence and expression of cellobiohydrolase !1II. !$#cross-references MUID:87248061; PMID:3596237 !$#accession A26472 !'##molecule_type DNA !'##residues 1-471 ##label TEE !'##cross-references GB:M16190; NID:g170540; PIDN:AAA34210.1; !1PID:g170541 GENETICS !$#introns 31/2; 160/2; 243/1 CLASSIFICATION #superfamily cellulose 1,4-beta-cellobiosidase II; fungal !1cellulose-binding domain homology KEYWORDS glycosidase; hydrolase; polysaccharide degradation FEATURE !$31-62 #domain fungal cellulose-binding domain homology !8#label FCB SUMMARY #length 471 #molecular-weight 49653 #checksum 6834 SEQUENCE /// ENTRY A38979 #type complete TITLE cellulose 1,4-beta-cellobiosidase (EC 3.2.1.91) II - fungus (Trichoderma viride) ORGANISM #formal_name Trichoderma viride DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A38979 REFERENCE A38979 !$#authors Wang, J.R.; Zhang, M.F.; Huang, T. !$#journal Acta Genet. Sin. (1995) 22:74-80 !$#title The primary structure of cellobiohydrase gene (CBH II) from !1Trichaderma viride. !$#accession A38979 !'##molecule_type DNA !'##residues 1-471 ##label WAN GENETICS !$#gene cbhII !$#introns 31/2; 160/2; 243/1 CLASSIFICATION #superfamily cellulose 1,4-beta-cellobiosidase II; fungal !1cellulose-binding domain homology KEYWORDS glycosidase; hydrolase; polysaccharide degradation FEATURE !$31-62 #domain fungal cellulose-binding domain homology !8#label FCB SUMMARY #length 471 #molecular-weight 49653 #checksum 6834 SEQUENCE /// ENTRY S70602 #type complete TITLE cellulose 1,4-beta-cellobiosidase (EC 3.2.1.91) II precursor - cultivated mushroom ALTERNATE_NAMES cellulase ORGANISM #formal_name Agaricus bisporus #common_name cultivated mushroom DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S70602 REFERENCE S70602 !$#authors Yaguee, E.; Chow, C.M.; Challen, M.P.; Thurston, C.F. !$#journal Curr. Genet. (1996) 30:56-61 !$#title Correlation of exons with functional domains and folding !1regions in a cellulase from Agaricus bisporus. !$#cross-references MUID:96269930; PMID:8662210 !$#accession S70602 !'##status preliminary !'##molecule_type DNA !'##residues 1-438 ##label YAG !'##cross-references EMBL:Z34007; NID:g1494969; PIDN:CAA83971.1; !1PID:g1494970 GENETICS !$#introns 34/1; 56/2; 96/3; 202/1; 325/3; 410/2 CLASSIFICATION #superfamily cellulose 1,4-beta-cellobiosidase II; fungal !1cellulose-binding domain homology KEYWORDS glycosidase; hydrolase; polysaccharide degradation FEATURE !$25-56 #domain fungal cellulose-binding domain homology !8#label FCB SUMMARY #length 438 #molecular-weight 46209 #checksum 9508 SEQUENCE /// ENTRY A24994 #type complete TITLE cellulose 1,4-beta-cellobiosidase (EC 3.2.1.91) A precursor [validated] - Cellulomonas fimi ALTERNATE_NAMES exo-cellobiohydrolase A ORGANISM #formal_name Cellulomonas fimi DATE 15-Dec-1988 #sequence_revision 22-Nov-1996 #text_change 15-Sep-2000 ACCESSIONS A24994 REFERENCE A24994 !$#authors O'Neill, G.; Goh, S.H.; Warren, R.A.J.; Kilburn, D.G.; !1Miller Jr., R.C. !$#journal Gene (1986) 44:325-330 !$#title Structure of the gene encoding the exoglucanase of !1Cellulomonas fimi. !$#cross-references MUID:87055250; PMID:3096818 !$#accession A24994 !'##molecule_type DNA !'##residues 1-484 ##label ONE !'##cross-references GB:M15824; NID:g144424; PIDN:AAA56791.1; !1PID:g144425 !'##note the amino-terminal sequence of the mature protein (residues !142-71) has been determined (M.L. Langsford, unpublished !1data) REFERENCE A67217 !$#authors White, A.; Withers, S.G.; Gilkes, N.R.; Rose, D.R. !$#submission submitted to the Brookhaven Protein Data Bank, July 1994 !$#cross-references PDB:2EXO !$#contents annotation; X-ray crystallography, 1.8 angstroms, residues !142-173,'G',175,'RR'178-353 REFERENCE A55905 !$#authors White, A.; Withers, S.G.; Gilkes, N.R.; Rose, D.R. !$#journal Biochemistry (1994) 33:12546-12552 !$#title Crystal structure of the catalytic domain of the beta-1, !14-glycanase Cex from Cellulomonas fimi. !$#cross-references MUID:95001978; PMID:7918478 !$#contents annotation; X-ray crystallography, 1.8 angstroms, residues !142-173,'G',175,'RR'178-353 GENETICS !$#gene cex FUNCTION !$#description hydrolyses 1,4-beta-D-glucosidic linkages in cellulose and, !1releasing cellobiose from the non-reducing ends of the !1chains CLASSIFICATION #superfamily Cellulomonas cellulose 1,4-beta-cellobiosidase !1A; bacterial cellulose-binding domain homology; Streptomyces !1endo-1,4-beta-xylanase A homology KEYWORDS extracellular protein; glycoprotein; glycosidase; hydrolase; !1polysaccharide degradation; tandem repeat FEATURE !$1-41 #domain signal sequence #status predicted #label SIG\ !$42-484 #product cellulose 1,4-beta-cellobiosidase #status !8experimental #label MAT\ !$73-353 #domain Streptomyces endo-1,4-beta-xylanase A !8homology #label SXY\ !$357-377 #region 7-residue repeats (P-T-P-T-P-T-[S/T])\ !$381-482 #domain bacterial cellulose-binding domain homology !8#label BCB\ !$137,398,403,447,461 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$168,274 #active_site Glu #status experimental\ !$208-240,302-308 #disulfide_bonds #status experimental\ !$382-481 #disulfide_bonds #status predicted SUMMARY #length 484 #molecular-weight 51291 #checksum 9660 SEQUENCE /// ENTRY JC5861 #type complete TITLE endo-1,4-beta-xylanase (EC 3.2.1.8) - imperfect fungus (Humicola grisea) ORGANISM #formal_name Humicola grisea DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS JC5861 REFERENCE JC5861 !$#authors Iikura, H.; Takashima, S.; Nakamura, A.; Masaki, H.; Uozumi, !1T. !$#journal Biosci. Biotechnol. Biochem. (1997) 61:1593-1595 !$#title Cloning of a gene encoding a putative xylanase with a !1cellulose-binding domain from Humicola grisea. !$#cross-references MUID:97480951; PMID:9339567 !$#accession JC5861 !'##molecule_type DNA !'##residues 1-429 ##label IIK !'##cross-references DDBJ:AB001030; NID:g1842141; PIDN:BAA19220.1; !1PID:g1842142 COMMENT This enzyme hydrolyze cellulosic substrates as well as !1xylan. GENETICS !$#gene xyn1 !$#introns 112/3; 188/2 CLASSIFICATION #superfamily Humicola endo-1,4-beta-xylanase; fungal !1cellulose-binding domain homology; Streptomyces endo-1, !14-beta-xylanase A homology KEYWORDS glycosidase; hydrolase FEATURE !$53-337 #domain Streptomyces endo-1,4-beta-xylanase A !8homology #label SXY\ !$344-393 #region hinge\ !$394-429 #domain cellulose-binding #status predicted #label !8CBD\ !$398-429 #domain fungal cellulose-binding domain homology !8#label FCB SUMMARY #length 429 #molecular-weight 47017 #checksum 8594 SEQUENCE /// ENTRY RBSMHP #type complete TITLE mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase (EC 3.2.1.96) H precursor - Streptomyces plicatus ALTERNATE_NAMES di-N-acetylchitobiosyl beta-N-acetylglucosaminidase H; endo-beta-N-acetylglucosaminidase H ORGANISM #formal_name Streptomyces plicatus DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 18-Jun-1999 ACCESSIONS A00903 REFERENCE A00903 !$#authors Robbins, P.W.; Trimble, R.B.; Wirth, D.F.; Hering, C.; !1Maley, F.; Maley, G.F.; Das, R.; Gibson, B.W.; Royal, N.; !1Biemann, K. !$#journal J. Biol. Chem. (1984) 259:7577-7583 !$#title Primary structure of the Streptomyces enzyme !1endo-beta-N-acetylglucosaminidase H. !$#cross-references MUID:84239689; PMID:6429133 !$#accession A00903 !'##molecule_type DNA !'##residues 1-313 ##label ROB !'##cross-references GB:K02182; NID:g153246; PIDN:AAA26738.1; !1PID:g153247 CLASSIFICATION #superfamily mannosyl-glycoprotein !1endo-beta-N-acetylglucosaminidase H KEYWORDS glycosidase; hydrolase FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-313 #product mannosyl-glycoprotein !8endo-beta-N-acetylglucosaminidase H #status predicted !8#label MPT SUMMARY #length 313 #molecular-weight 33052 #checksum 1889 SEQUENCE /// ENTRY DGECM1 #type complete TITLE 3-methyladenine-DNA glycosylase (EC 3.2.2.-) I - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 01-Mar-2002 ACCESSIONS A24604; S47770; I58249; G65153 REFERENCE A24604 !$#authors Sakumi, K.; Nakabeppu, Y.; Yamamoto, Y.; Kawabata, S.; !1Iwanaga, S.; Sekiguchi, M. !$#journal J. Biol. Chem. (1986) 261:15761-15766 !$#title Purification and structure of 3-methyladenine-DNA !1glycosylase I of Escherichia coli. !$#cross-references MUID:87057218; PMID:3536912 !$#accession A24604 !'##molecule_type DNA !'##residues 1-187 ##label SAK !'##cross-references GB:J02606; NID:g147919; PIDN:AAA24658.1; !1PID:g147920 !'##experimental_source K12 REFERENCE S47666 !$#authors Plunkett, G. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S47770 !'##molecule_type DNA !'##residues 1-187 ##label PLU !'##cross-references EMBL:U00039; NID:g466582; PIDN:AAB18526.1; !1PID:g466687 REFERENCE I58249 !$#authors Steinum, A.L.; Seeberg, E. !$#journal Nucleic Acids Res. (1986) 14:3763-3772 !$#title Nucleotide sequence of the tag gene from Escherichia coli. !$#cross-references MUID:86232617; PMID:3520491 !$#accession I58249 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-187 ##label RES !'##cross-references EMBL:X03845; NID:g43029; PIDN:CAA27472.1; !1PID:g43030 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65153 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-187 ##label BLAT !'##cross-references GB:AE000432; GB:U00096; NID:g2367241; !1PIDN:AAC76573.1; PID:g1789971; UWGP:b3549 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene tag; tagI !$#map_position 72 min FUNCTION !$#description one of the two enzymes that catalyze the hydrolysis of the !1deoxyribose N-glycosidic bond to excise 3-methyladenine; its !1activity is controlled by product inhibition; the other !1enzyme, 3-methyladenine-DNA glycosylase II, excises other !1alkylated nucleoside bases from damaged DNA polymers; its !1activity is inducible by alkylating agents and is not !1inhibited by reaction products CLASSIFICATION #superfamily 3-methyladenine DNA glycosylase I KEYWORDS DNA repair; glycosidase; hydrolase SUMMARY #length 187 #molecular-weight 21100 #checksum 6779 SEQUENCE /// ENTRY DGECMA #type complete TITLE DNA-3-methyladenine glycosidase II (EC 3.2.2.21) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 01-Mar-2002 ACCESSIONS A00904; C64973 REFERENCE A00904 !$#authors Nakabeppu, Y.; Miyata, T.; Kondo, H.; Iwanaga, S.; !1Sekiguchi, M. !$#journal J. Biol. Chem. (1984) 259:13730-13736 !$#title Structure and expression of the alkA gene of Escherichia !1coli involved in adaptive response to alkylating agents. !$#cross-references MUID:85054800; PMID:6094528 !$#accession A00904 !'##molecule_type DNA !'##residues 1-282 ##label NAK !'##cross-references GB:K02498; NID:g145225; PIDN:AAA23430.1; !1PID:g145226 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64973 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-282 ##label BLAT !'##cross-references GB:AE000297; GB:U00096; NID:g1788382; !1PIDN:AAC75129.1; PID:g1788383; UWGP:b2068 !'##experimental_source strain K-12, substrain MG1655 COMMENT This enzyme, which is induced when E. coli cells are exposed !1to DNA alkylating agents, catalyzes the hydrolysis of the !1deoxyribose N-glycosidic bond to excise 3-methyladenine and !1other alkylated nucleoside bases from the damaged DNA !1polymer formed by alkylation lesions. GENETICS !$#gene alkA !$#map_position 43 min CLASSIFICATION #superfamily 3-methyladenine DNA glycosylase II KEYWORDS DNA repair; glycosidase; hydrolase SUMMARY #length 282 #molecular-weight 31393 #checksum 3682 SEQUENCE /// ENTRY S11489 #type complete TITLE DNA-formamidopyrimidine glycosylase (EC 3.2.2.23) - Bacillus firmus ORGANISM #formal_name Bacillus firmus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S11489 REFERENCE S11489 !$#authors Ivey, D.M. !$#journal Nucleic Acids Res. (1990) 18:5882 !$#title Nucleotide sequence of a gene from alkaliphilic Bacillus !1firmus RAB that is homologous to the fpg gene of Escherichia !1coli. !$#cross-references MUID:91016932; PMID:2216780 !$#accession S11489 !'##status preliminary !'##molecule_type DNA !'##residues 1-274 ##label IVE !'##cross-references EMBL:X53930; NID:g39474; PIDN:CAA37877.1; !1PID:g39475 CLASSIFICATION #superfamily formamidopyrimidine-DNA glycosidase KEYWORDS glycosidase; hydrolase SUMMARY #length 274 #molecular-weight 31114 #checksum 7297 SEQUENCE /// ENTRY S75925 #type complete TITLE DNA-formamidopyrimidine glycosylase (EC 3.2.2.23) - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S75925; C34301 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75925 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-287 ##label KAN !'##cross-references EMBL:D90913; GB:AB001339; NID:g1653348; !1PIDN:BAA18384.1; PID:g1653470 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 REFERENCE A34301 !$#authors Chitnis, P.R.; Reilly, P.A.; Miedel, M.C.; Nelson, N. !$#journal J. Biol. Chem. (1989) 264:18374-18380 !$#title Structure and targeted mutagenesis of the gene encoding !18-kDa subunit of photosystem I from the cyanobacterium !1Synechocystis sp. PCC 6803. !$#cross-references MUID:90036928; PMID:2509456 !$#accession C34301 !'##molecule_type DNA !'##residues 84-128,'AI',131-168 ##label CHI !'##cross-references GB:J05079; NID:g154482; PIDN:AAA88630.1; !1PID:g1196953 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily formamidopyrimidine-DNA glycosidase KEYWORDS glycosidase; hydrolase SUMMARY #length 287 #molecular-weight 32061 #checksum 8630 SEQUENCE /// ENTRY DGECFP #type complete TITLE DNA-formamidopyrimidine glycosylase (EC 3.2.2.23) - Escherichia coli (strain K-12) ALTERNATE_NAMES 2-6-diamino-4-hydroxy-5N-methyl-formamidopyrimidine; Fapy-DNA glycosylase ORGANISM #formal_name Escherichia coli DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 03-Jun-2002 ACCESSIONS A30254; PS0429; S47856; A35462; E65164; S27563 REFERENCE A30254 !$#authors Boiteux, S.; O'Connor, T.R.; Laval, J. !$#journal EMBO J. (1987) 6:3177-3183 !$#title Formamidopyrimidine-DNA glycosylase of Escherichia coli: !1cloning and sequencing of the fpg structural gene and !1overproduction of the protein. !$#cross-references MUID:88082692; PMID:3319582 !$#accession A30254 !'##molecule_type DNA !'##residues 1-269 ##label BOI !'##cross-references GB:X06036; NID:g41480; PIDN:CAA29431.1; PID:g41481 REFERENCE JU0467 !$#authors Clementz, T.; Raetz, C.R.H. !$#journal J. Biol. Chem. (1991) 266:9687-9696 !$#title A gene coding for 3-deoxy-D-manno-octulosonic-acid !1transferase in Escherichia coli. !$#cross-references MUID:91236744; PMID:2033061 !$#accession PS0429 !'##molecule_type DNA !'##residues 181-269 ##label CLE !'##cross-references GB:M60670; NID:g146555; PIDN:AAA24045.1; !1PID:g146558; EMBL:M86305; NID:g146540; PID:g146545 !'##experimental_source strain K12 REFERENCE S47666 !$#authors Plunkett, G. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S47856 !'##molecule_type DNA !'##residues 1-269 ##label PLU !'##cross-references EMBL:U00039; NID:g466582; PIDN:AAB18612.1; !1PID:g466773 REFERENCE A35462 !$#authors Boiteux, S.; O'Connor, T.R.; Lederer, F.; Gouyette, A.; !1Laval, J. !$#journal J. Biol. Chem. (1990) 265:3916-3922 !$#title Homogeneous Escherichia coli FPG protein. A DNA glycosylase !1which excises imidazole ring-opened purines and nicks DNA at !1apurinic/apyrimidinic sites. !$#cross-references MUID:90154076; PMID:1689309 !$#accession A35462 !'##status preliminary !'##molecule_type DNA !'##residues 1-24 ##label BO2 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65164 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-269 ##label BLAT !'##cross-references GB:AE000441; GB:U00096; NID:g1790063; !1PIDN:AAC76659.1; PID:g1790066; UWGP:b3635 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene mutM; fpg !$#map_position 82 min FUNCTION !$#description catalyzes the removal of formamidopyrimidine, the !1ring-opened form of N7-methylguanine, and may play a !1significant role in processes leading to recovery from !1mutagenesis and/or cell death by alkylating agents CLASSIFICATION #superfamily formamidopyrimidine-DNA glycosidase KEYWORDS DNA repair; glycosidase; hydrolase SUMMARY #length 269 #molecular-weight 30290 #checksum 3070 SEQUENCE /// ENTRY DGECU #type complete TITLE uracil-DNA glycosylase (EC 3.2.2.-) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 01-Mar-2002 ACCESSIONS A28175; C65036 REFERENCE A28175 !$#authors Varshney, U.; Hutcheon, T.; van de Sande, J.H. !$#journal J. Biol. Chem. (1988) 263:7776-7784 !$#title Sequence analysis, expression, and conservation of !1Escherichia coli uracil DNA glycosylase and its gene (ung). !$#cross-references MUID:88227981; PMID:2836397 !$#accession A28175 !'##molecule_type DNA !'##residues 1-229 ##label VAR !'##cross-references GB:D64044; NID:g987635; PIDN:BAA10923.1; !1PID:g987651 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65036 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-229 ##label BLAT !'##cross-references GB:AE000344; GB:U00096; NID:g1788927; !1PIDN:AAC75633.1; PID:g1788934; UWGP:b2580 !'##experimental_source strain K-12, substrain MG1655 COMMENT This enzyme catalyzes the hydrolysis of the deoxyribose !1N-glycosidic bond to excise uracil residues from damaged DNA !1and initiate DNA repair; its activity is controlled by !1product inhibition. GENETICS !$#gene ung !$#map_position 56 min CLASSIFICATION #superfamily uracil-DNA glycosylase KEYWORDS DNA repair; glycosidase; hydrolase SUMMARY #length 229 #molecular-weight 25693 #checksum 6877 SEQUENCE /// ENTRY A60472 #type complete TITLE uracil-DNA glycosylase (EC 3.2.2.-) precursor [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 08-Dec-2000 ACCESSIONS S05964; A60472 REFERENCE S05964 !$#authors Olsen, L.C.; Aasland, R.; Wittwer, C.U.; Krokan, H.E.; !1Helland, D.E. !$#journal EMBO J. (1989) 8:3121-3125 !$#title Molecular cloning of human uracil-DNA glycosylase, a highly !1conserved DNA repair enzyme. !$#cross-references MUID:90059899; PMID:2555154 !$#accession S05964 !'##molecule_type mRNA !'##residues 1-304 ##label OLS !'##cross-references EMBL:X15653; NID:g37598; PIDN:CAA33679.1; !1PID:g37599 REFERENCE A60472 !$#authors Wittwer, C.U.; Bauw, G.; Krokan, H.E. !$#journal Biochemistry (1989) 28:780-784 !$#title Purification and determination of the NH-2-terminal amino !1acid sequence of uracil-DNA glycosylase from human placenta. !$#cross-references MUID:89229080; PMID:2713345 !$#accession A60472 !'##molecule_type protein !'##residues 78-93,'X',95-104 ##label WIT GENETICS !$#gene GDB:UNG; DGU; UDG !'##cross-references GDB:119844; OMIM:191525 !$#map_position 12pter-12qter CLASSIFICATION #superfamily uracil-DNA glycosylase KEYWORDS DNA repair; glycosidase; hydrolase; mitochondrion FEATURE !$1-77 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$78-304 #product uracil-DNA glycosylase #status experimental !8#label MAT SUMMARY #length 304 #molecular-weight 33924 #checksum 3337 SEQUENCE /// ENTRY A31425 #type complete TITLE uracil-DNA glycosylase (EC 3.2.2.-) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YML021c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A31425; S49756; A30790 REFERENCE A31425 !$#authors Percival, K.J.; Klein, M.B.; Burgers, P.M.J. !$#journal J. Biol. Chem. (1989) 264:2593-2598 !$#title Molecular cloning and primary structure of the !1uracil-DNA-glycosylase gene from Saccharomyces cerevisiae. !$#cross-references MUID:89123348; PMID:2644266 !$#accession A31425 !'##molecule_type DNA !'##residues 1-359 ##label PER !'##cross-references EMBL:J04470; NID:g173139; PIDN:AAA35195.1; !1PID:g173140 REFERENCE S49741 !$#authors Badcock, K.; Churcher, C. !$#submission submitted to the EMBL Data Library, November 1994 !$#accession S49756 !'##molecule_type DNA !'##residues 1-359 ##label BAD !'##cross-references EMBL:Z46659; NID:g575680; PIDN:CAA86634.1; !1PID:g575698; GSPDB:GN00013; MIPS:YML021c GENETICS !$#gene SGD:UNG1; MIPS:YML021c !'##cross-references SGD:S0004483; MIPS:YML021c !$#map_position 13L CLASSIFICATION #superfamily uracil-DNA glycosylase KEYWORDS glycosidase; hydrolase; mitochondrion; nucleus SUMMARY #length 359 #molecular-weight 40471 #checksum 3962 SEQUENCE /// ENTRY DGBEHG #type complete TITLE uracil-DNA glycosylase (EC 3.2.2.-) - human herpesvirus 2 (strain HG52) ORGANISM #formal_name human herpesvirus 2 #note host Homo sapiens (man) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jun-2000 ACCESSIONS JQ1495 REFERENCE JQ1494 !$#authors McGeoch, D.J.; Cunningham, C.; McIntyre, G.; Dolan, A. !$#journal J. Gen. Virol. (1991) 72:3057-3075 !$#title Comparative sequence analysis of the long repeat regions and !1adjoining parts of the long unique regions in the genomes of !1herpes simplex viruses types 1 and 2. !$#cross-references MUID:92113549; PMID:1662697 !$#accession JQ1495 !'##molecule_type DNA !'##residues 1-255 ##label MCG !'##cross-references GB:D10470; DDBJ:D01127; NID:g221791; !1PIDN:BAA01265.1; PID:g221793 GENETICS !$#gene UL2 CLASSIFICATION #superfamily uracil-DNA glycosylase KEYWORDS glycosidase; hydrolase SUMMARY #length 255 #molecular-weight 28479 #checksum 3915 SEQUENCE /// ENTRY DGBEH2 #type complete TITLE uracil-DNA glycosylase (EC 3.2.2.-) - human herpesvirus 2 (strain 333) ORGANISM #formal_name human herpesvirus 2 DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 04-Mar-1994 ACCESSIONS A31885 REFERENCE A31885 !$#authors Worrad, D.M.; Caradonna, S. !$#journal J. Virol. (1988) 62:4774-4777 !$#title Identification of the coding sequence for herpes simplex !1virus uracil-DNA glycosylase. !$#cross-references MUID:89037371; PMID:2846888 !$#accession A31885 !'##molecule_type DNA !'##residues 1-294 ##label WOR GENETICS !$#gene UL2 CLASSIFICATION #superfamily uracil-DNA glycosylase KEYWORDS glycosidase; hydrolase SUMMARY #length 294 #molecular-weight 32495 #checksum 2455 SEQUENCE /// ENTRY DGBEX2 #type complete TITLE uracil-DNA glycosylase (EC 3.2.2.-) - human herpesvirus 1 (strain 17) ORGANISM #formal_name human herpesvirus 1 DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jun-2000 ACCESSIONS B28133 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession B28133 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-334 ##label MCG !'##cross-references GB:X14112; NID:g1944536; PIDN:CAA32338.1; !1PID:g59503; GB:D00317 GENETICS !$#gene UL2 CLASSIFICATION #superfamily uracil-DNA glycosylase KEYWORDS glycosidase; hydrolase SUMMARY #length 334 #molecular-weight 36328 #checksum 8080 SEQUENCE /// ENTRY DGBEL5 #type complete TITLE uracil-DNA glycosylase (EC 3.2.2.-) - human cytomegalovirus (strain AD169) ALTERNATE_NAMES UL114 protein ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 #note host Homo sapiens (man) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 18-Jun-1999 ACCESSIONS S09881 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09881 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-250 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35316.1; !1PID:g1780896 !'##note possible protein-coding frames are given !'##note the DNA sequence was submitted to EMBL, December 1989, in !1computer-readable form CLASSIFICATION #superfamily uracil-DNA glycosylase KEYWORDS glycosidase; hydrolase SUMMARY #length 250 #molecular-weight 28353 #checksum 6234 SEQUENCE /// ENTRY DGBE59 #type complete TITLE uracil-DNA glycosylase (EC 3.2.2.-) - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 18-Jun-1999 ACCESSIONS G27215 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession G27215 !'##molecule_type DNA !'##residues 1-305 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27942.1; !1PID:g60048 GENETICS !$#gene 59 CLASSIFICATION #superfamily uracil-DNA glycosylase KEYWORDS glycosidase; hydrolase SUMMARY #length 305 #molecular-weight 34376 #checksum 4226 SEQUENCE /// ENTRY DGBEF3 #type complete TITLE uracil-DNA glycosylase (EC 3.2.2.-) - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS G36801 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession G36801 !'##molecule_type DNA !'##residues 1-312 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02496.1; !1PID:g330852 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 61 CLASSIFICATION #superfamily uracil-DNA glycosylase KEYWORDS glycosidase; hydrolase SUMMARY #length 312 #molecular-weight 34777 #checksum 8200 SEQUENCE /// ENTRY DGBEN8 #type complete TITLE uracil-DNA glucosidase (EC 3.2.2.-) - saimiriine herpesvirus 1 (strain 11) ORGANISM #formal_name saimiriine herpesvirus 1 #note host Saimiri sciureus (common squirrel monkey) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 18-Jun-1999 ACCESSIONS H36810 REFERENCE A36806 !$#authors Albrecht, J. !$#submission submitted to the EMBL Data Library, January 1992 !$#description Primary structure of the herpesvirus saimiri genome. !$#accession H36810 !'##molecule_type DNA !'##residues 1-252 ##label ALB !'##cross-references GB:X64346; NID:g60320; PIDN:CAA45669.1; PID:g60367 REFERENCE A37309 !$#authors Albrecht, J.C.; Nicholas, J.; Biller, D.; Cameron, K.R.; !1Biesinger, B.; Newman, C.; Wittmann, S.; Craxton, M.A.; !1Coleman, H.; Fleckenstein, B.; Honess, R.W. !$#journal J. Virol. (1992) 66:5047-5058 !$#title Primary structure of the herpesvirus saimiri genome. !$#cross-references MUID:92333688; PMID:1321287 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 46 CLASSIFICATION #superfamily uracil-DNA glycosylase KEYWORDS glycosidase; hydrolase SUMMARY #length 252 #molecular-weight 28864 #checksum 226 SEQUENCE /// ENTRY A43629 #type complete TITLE adenosylhomocysteinase (EC 3.3.1.1) - human ALTERNATE_NAMES S-adenosyl-L-homocysteine hydrolase ORGANISM #formal_name Homo sapiens #common_name man DATE 11-Feb-1993 #sequence_revision 04-Oct-1996 #text_change 07-May-1999 ACCESSIONS A43629; A60446; A57486; S65894 REFERENCE A43629 !$#authors Coulter-Karis, D.E.; Hershfield, M.S. !$#journal Ann. Hum. Genet. (1989) 53:169-175 !$#title Sequence of full length cDNA for human !1S-adenosylhomocysteine hydrolase. !$#cross-references MUID:90087640; PMID:2596825 !$#accession A43629 !'##molecule_type mRNA !'##residues 1-432 ##label COU !'##cross-references GB:M61831 REFERENCE A60446 !$#authors Arredondo-Vega, F.X.; Charlton, J.A.; Edwards, Y.H.; !1Hopkinson, D.A.; Whitehouse, D.B. !$#journal Ann. Hum. Genet. (1989) 53:157-167 !$#title Isozyme and DNA analysis of human S-adenosyl-L-homocysteine !1hydrolase (AHCY). !$#cross-references MUID:90087639; PMID:2574561 !$#accession A60446 !'##molecule_type mRNA !'##residues 122-432 ##label ARR !'##note the authors translated the codon CTT for residue 162 as Glu, !1TAC for residue 295 as Thr, and CTG for residue 296 as Glu REFERENCE A57486 !$#authors Yuan, C.S.; Borchardt, R.T. !$#journal J. Biol. Chem. (1995) 270:16140-16146 !$#title Photoaffinity labeling of human placental !1S-adenosylhomocysteine hydrolase with [2-(3)H] !18-azido-adenosine. !$#cross-references MUID:95332317; PMID:7608178 !$#accession A57486 !'##status preliminary !'##molecule_type protein !'##residues 175-178,'X',180,'X',182-184,'X',186;319-326,'X' ##label YUA REFERENCE S65894 !$#authors Gupta, R.A.; Yuan, C.S.; Ault-Riche, D.B.; Borchardt, R.T. !$#journal Arch. Biochem. Biophys. (1995) 319:365-371 !$#title Limited proteolysis of S-adenosylhomocysteine hydrolase: !1implications for the three-dimensional structure. !$#cross-references MUID:95305573; PMID:7786017 !$#accession S65894 !'##status preliminary !'##molecule_type protein !'##residues 2-6;104-108;198-202 ##label GUP GENETICS !$#gene GDB:AHCY !'##cross-references GDB:118983; OMIM:180960 !$#map_position 20cen-20q13.1 FUNCTION !$#description catalyzes the reversible hydrolysis of !1S-adenosyl-L-homocysteine to adenosine and homocysteine CLASSIFICATION #superfamily adenosylhomocysteinase KEYWORDS homotetramer; NAD; thioether hydrolase FEATURE !$214-243 #region beta-alpha-beta NAD nucleotide-binding fold\ !$79,113 #active_site Cys #status predicted SUMMARY #length 432 #molecular-weight 47716 #checksum 5183 SEQUENCE /// ENTRY A26583 #type complete TITLE adenosylhomocysteinase (EC 3.3.1.1) - rat ALTERNATE_NAMES S-adenosyl-L-homocysteine hydrolase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 19-Nov-1988 #sequence_revision 04-Oct-1996 #text_change 18-Jun-1999 ACCESSIONS A26583; A26191; B26191; S69333 REFERENCE A26583 !$#authors Ogawa, H.; Gomi, T.; Mueckler, M.M.; Fujioka, M.; Backlund !1Jr., P.S.; Aksamit, R.R.; Unson, C.G.; Cantoni, G.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:719-723 !$#title Amino acid sequence of S-adenosyl-L-homocysteine hydrolase !1from rat liver as derived from the cDNA sequence. !$#cross-references MUID:87118240; PMID:3027698 !$#accession A26583 !'##molecule_type mRNA !'##residues 1-432 ##label OGA !'##cross-references GB:M15185; NID:g202803; PIDN:AAA40705.1; !1PID:g202804 REFERENCE A92560 !$#authors Gomi, T.; Ogawa, H.; Fujioka, M. !$#journal J. Biol. Chem. (1986) 261:13422-13425 !$#title S-Adenosylhomocysteinase from rat liver. Amino acid !1sequences of the peptides containing active site cysteine !1residues modified by treatment with !15'-p-fluorosulfonylbenzoyladenosine. !$#cross-references MUID:87008564; PMID:3759971 !$#accession A26191 !'##molecule_type protein !'##residues 76-94 ##label GOM !$#accession B26191 !'##molecule_type protein !'##residues 104-121 ##label GO2 !'##note in a manner saturably inhibited by adenosine (a product) or !1adenine (a competitive inhibitor), FSBA inactivates !1adenosylhomocysteinase by causing the formation of a !1disulfide bond between Cys-79 and Cys-113, suggesting a role !1for these residues at the active site; however, neither !1residue appears to be completely conserved among !1adenosylhomocysteinases REFERENCE S69333 !$#authors Merta, A.; Aksamit, R.R.; Kasir, J.; Cantoni, G.L. !$#journal Eur. J. Biochem. (1995) 229:575-582 !$#title The gene and pseudogenes of rat S-adenosyl-L-homocysteine !1hydrolase. !$#cross-references MUID:95262723; PMID:7744082 !$#accession S69333 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-432 ##label MER !'##cross-references EMBL:U14937; NID:g1223843; PIDN:AAA92043.1; !1PID:g1185363 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1September 1994 GENETICS !$#introns 10/1; 73/3; 99/1; 149/1; 186/3; 256/1; 285/2; 324/3; 389/3 FUNCTION !$#description catalyzes the reversible hydrolysis of !1S-adenosyl-L-homocysteine to adenosine and homocysteine CLASSIFICATION #superfamily adenosylhomocysteinase KEYWORDS homotetramer; NAD; thioether hydrolase FEATURE !$214-243 #region beta-alpha-beta NAD nucleotide-binding fold\ !$79,113 #active_site Cys #status predicted SUMMARY #length 432 #molecular-weight 47538 #checksum 3428 SEQUENCE /// ENTRY JC2480 #type complete TITLE adenosylhomocysteinase (EC 3.3.1.1) - African clawed frog ALTERNATE_NAMES S-adenosyl-L-homocysteine hydrolase ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 29-Mar-1995 #sequence_revision 04-Oct-1996 #text_change 28-May-1999 ACCESSIONS JC2480 REFERENCE JC2480 !$#authors Seery, L.T.; McCabe, B.D.; Schoenberg, D.R.; Whitehead, A.S. !$#journal Biochem. Biophys. Res. Commun. (1994) 205:1539-1546 !$#title S-Adenosyl-L-homocysteine hydrolase from Xenopus !1laevis:Identification, developmental expression and !1evolution. !$#cross-references MUID:95110290; PMID:7811234 !$#accession JC2480 !'##molecule_type mRNA !'##residues 1-433 ##label SEE !'##cross-references GB:L35559; NID:g558507; PIDN:AAA65963.1; !1PID:g558508 !'##experimental_source liver FUNCTION !$#description catalyzes the reversible hydrolysis of !1S-adenosyl-L-homocysteine to adenosine and homocysteine CLASSIFICATION #superfamily adenosylhomocysteinase KEYWORDS NAD; thioether hydrolase FEATURE !$215-244 #region beta-alpha-beta NAD nucleotide-binding fold\ !$79,113 #active_site Cys #status predicted SUMMARY #length 433 #molecular-weight 47747 #checksum 9778 SEQUENCE /// ENTRY A45569 #type complete TITLE adenosylhomocysteinase (EC 3.3.1.1) - Leishmania donovani ALTERNATE_NAMES S-adenosyl-L-homocysteine hydrolase ORGANISM #formal_name Leishmania donovani DATE 03-Feb-1994 #sequence_revision 04-Oct-1996 #text_change 15-Oct-1996 ACCESSIONS A45569 REFERENCE A45569 !$#authors Henderson, D.M.; Hanson, S.; Allen, T.; Wilson, K.; !1Coulter-Karis, D.E.; Greenberg, M.L.; Hershfield, M.S.; !1Ullman, B. !$#journal Mol. Biochem. Parasitol. (1992) 53:169-183 !$#title Cloning of the gene encoding Leishmania donovani !1S-adenosylhomocysteine hydrolase, a potential target for !1antiparasitic chemotherapy. !$#cross-references MUID:92365726; PMID:1501636 !$#accession A45569 !'##molecule_type DNA !'##residues 1-437 ##label HEN !'##note this sequence is inconsistent with the nucleotide translation !'##note sequence extracted from NCBI backbone (NCBIN:111168, !1NCBIP:111170) FUNCTION !$#description catalyzes the reversible hydrolysis of !1S-adenosyl-L-homocysteine to adenosine and homocysteine CLASSIFICATION #superfamily adenosylhomocysteinase KEYWORDS NAD; thioether hydrolase FEATURE !$213-242 #region beta-alpha-beta NAD nucleotide-binding fold\ !$76,110 #active_site Cys #status predicted SUMMARY #length 437 #molecular-weight 47782 #checksum 9678 SEQUENCE /// ENTRY A27655 #type complete TITLE adenosylhomocysteinase (EC 3.3.1.1) - slime mold (Dictyostelium discoideum) ALTERNATE_NAMES S-adenosyl-L-homocysteine hydrolase ORGANISM #formal_name Dictyostelium discoideum DATE 31-Mar-1989 #sequence_revision 04-Oct-1996 #text_change 18-Jun-1999 ACCESSIONS A27655; S06394 REFERENCE A27655 !$#authors Kasir, J.; Aksamit, R.R.; Backlund Jr., P.S.; Cantoni, G.L. !$#journal Biochem. Biophys. Res. Commun. (1988) 153:359-364 !$#title Amino acid sequence of S-adenosyl-L-homocysteine hydrolase !1from Dictyostelium discoideum as deduced from the cDNA !1sequence. !$#cross-references MUID:88240426; PMID:3288206 !$#accession A27655 !'##molecule_type mRNA !'##residues 1-430 ##label KAS !'##cross-references GB:M19937; NID:g167663; PIDN:AAA33165.1; !1PID:g167664 REFERENCE S06394 !$#authors Guitton, M.C.; Part, D.; Veron, M. !$#journal Biochimie (1988) 70:835-840 !$#title Cloning of a cDNA for the S-adenosyl-L-homocysteine !1hydrolase from Dictyostelium discoideum. !$#cross-references MUID:89000991; PMID:3139100 !$#accession S06394 !'##molecule_type mRNA !'##residues 'VVTKSSPWKPPLHYQT',270-311,'G',313-323,'S',325-359,'SVTK', !1365-382,'F',384-430 ##label GUI !'##cross-references EMBL:X12523; NID:g7204; PIDN:CAA31040.1; PID:g7205 !'##note this sequence differs at the amino end by an apparant frame !1shift; comparison to orthologs suggests that this report is !1in error FUNCTION !$#description catalyzes the reversible hydrolysis of !1S-adenosyl-L-homocysteine to adenosine and homocysteine CLASSIFICATION #superfamily adenosylhomocysteinase KEYWORDS NAD; thioether hydrolase FEATURE !$213-242 #region beta-alpha-beta NAD nucleotide-binding fold\ !$78,112 #active_site Cys #status predicted SUMMARY #length 430 #molecular-weight 47083 #checksum 1873 SEQUENCE /// ENTRY A46035 #type complete TITLE adenosylhomocysteinase (EC 3.3.1.1) - Rhodobacter capsulatus ALTERNATE_NAMES S-adenosyl-L-homocysteine hydrolase ORGANISM #formal_name Rhodobacter capsulatus DATE 04-Mar-1994 #sequence_revision 04-Oct-1996 #text_change 18-Jun-1999 ACCESSIONS A46035; A36863 REFERENCE A46035 !$#authors Sganga, M.W.; Aksamit, R.R.; Cantoni, G.L.; Bauer, C.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:6328-6332 !$#title Mutational and nucleotide sequence analysis of !1S-adenosyl-L-homocysteine hydrolase from Rhodobacter !1capsulatus. !$#cross-references MUID:92335291; PMID:1631127 !$#accession A46035 !'##molecule_type DNA !'##residues 1-462 ##label SGA !'##note sequence extracted from NCBI backbone (NCBIN:108691, !1NCBIP:108696) REFERENCE A36863 !$#authors Buggy, J.J.; Sganga, M.W.; Bauer, C.E. !$#journal J. Bacteriol. (1994) 176:61-69 !$#title Nucleotide sequence and characterization of the Rhodobacter !1capsulatus hvrB gene: HvrB is an activator of !1S-adenosyl-L-homocysteine hydrolase expression and is a !1member of the LysR family. !$#cross-references MUID:94110241; PMID:8282711 !$#accession A36863 !'##molecule_type DNA !'##residues 1-13 ##label BUG !'##cross-references GB:L23836; NID:g577613; PIDN:AAA53540.1; !1PID:g577614 GENETICS !$#gene ahcY FUNCTION !$#description catalyzes the reversible hydrolysis of !1S-adenosyl-L-homocysteine to adenosine and homocysteine CLASSIFICATION #superfamily adenosylhomocysteinase KEYWORDS NAD; thioether hydrolase FEATURE !$247-276 #region beta-alpha-beta NAD nucleotide-binding fold SUMMARY #length 462 #molecular-weight 50465 #checksum 9660 SEQUENCE /// ENTRY A54040 #type complete TITLE adenosylhomocysteinase (EC 3.3.1.1) - malaria parasite (Plasmodium falciparum) ALTERNATE_NAMES S-adenosyl-L-homocysteine hydrolase ORGANISM #formal_name Plasmodium falciparum DATE 02-Aug-1994 #sequence_revision 04-Oct-1996 #text_change 09-Jun-2000 ACCESSIONS A54040 REFERENCE A54040 !$#authors Creedon, K.A.; Rathod, P.K.; Wellems, T.E. !$#journal J. Biol. Chem. (1994) 269:16364-16370 !$#title Plasmodium falciparum S-adenosylhomocysteine hydrolase. cDNA !1identification, predicted protein sequence, and expression !1in Escherichia coli. !$#cross-references MUID:94266832; PMID:8206944 !$#accession A54040 !'##molecule_type mRNA !'##residues 1-479 ##label CRE !'##cross-references GB:U07365; NID:g537431; PIDN:AAA21391.1; !1PID:g460639 FUNCTION !$#description catalyzes the reversible hydrolysis of !1S-adenosyl-L-homocysteine to adenosine and homocysteine CLASSIFICATION #superfamily adenosylhomocysteinase KEYWORDS NAD; thioether hydrolase FEATURE !$258-287 #region beta-alpha-beta NAD nucleotide-binding fold SUMMARY #length 479 #molecular-weight 53893 #checksum 4808 SEQUENCE /// ENTRY S01302 #type complete TITLE adenosylhomocysteinase (EC 3.3.1.1) - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S01302 REFERENCE S01302 !$#authors DeLorenzi, M.; Ali, N.; Saari, G.; Henry, C.; Wilcox, M.; !1Bienz, M. !$#journal EMBO J. (1988) 7:3223-3231 !$#title Evidence that the Abdominal-B r element function is !1conferred by a trans-regulatory homeoprotein. !$#cross-references MUID:89030618; PMID:2903049 !$#accession S01302 !'##molecule_type DNA !'##residues 1-527 ##label DEL !'##cross-references EMBL:X13168; NID:g7675; PIDN:CAA31566.1; PID:g7676 GENETICS !$#gene FlyBase:Abd-B !'##cross-references FlyBase:FBgn0000015 !$#introns 17/3; 41/1; 263/2; 369/3; 451/1 CLASSIFICATION #superfamily adenosylhomocysteinase KEYWORDS NAD; thioether hydrolase FEATURE !$275-304 #region beta-alpha-beta NAD nucleotide-binding fold\ !$140,174 #active_site Cys #status predicted SUMMARY #length 527 #molecular-weight 58120 #checksum 752 SEQUENCE /// ENTRY C64473 #type complete TITLE adenosylhomocysteinase (EC 3.3.1.1) - Methanococcus jannaschii ALTERNATE_NAMES S-adenosyl-L-homocysteine hydrolase ORGANISM #formal_name Methanococcus jannaschii DATE 13-Sep-1996 #sequence_revision 04-Oct-1996 #text_change 21-Jul-2000 ACCESSIONS C64473 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession C64473 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-415 ##label BUL !'##cross-references GB:U67578; GB:L77117; NID:g2826403; !1PIDN:AAB99397.1; PID:g1592034; TIGR:MJ1388 GENETICS !$#map_position FOR1335810-1337057 FUNCTION !$#description catalyzes the reversible hydrolysis of !1S-adenosyl-L-homocysteine to adenosine and homocysteine CLASSIFICATION #superfamily adenosylhomocysteinase KEYWORDS NAD; thioether hydrolase FEATURE !$206-235 #region beta-alpha-beta NAD nucleotide-binding fold\ !$74 #active_site Cys #status predicted SUMMARY #length 415 #molecular-weight 46607 #checksum 7241 SEQUENCE /// ENTRY DABPT3 #type complete TITLE adenosylmethionine hydrolase (EC 3.3.1.2) - phage T3 ALTERNATE_NAMES S-adenosyl-L-methionine hydrolase ORGANISM #formal_name phage T3 #note host Escherichia coli DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 18-Jun-1999 ACCESSIONS A26441 REFERENCE A26441 !$#authors Hughes, J.A.; Brown, L.R.; Ferro, A.J. !$#journal Nucleic Acids Res. (1987) 15:717-729 !$#title Nucleotide sequence and analysis of the coliphage T3 !1S-adenosylmethionine hydrolase gene and its surrounding !1ribonuclease III processing sites. !$#cross-references MUID:87146388; PMID:3547328 !$#accession A26441 !'##molecule_type DNA !'##residues 1-152 ##label HUG !'##cross-references EMBL:X04791; NID:g15558; PIDN:CAA28477.1; !1PID:g15559 COMMENT This enzyme hydrolyzes adenosylmethionine to homoserine and !15'-methylthioadenosine. CLASSIFICATION #superfamily phage T3 adenosylmethionine hydrolase KEYWORDS thioether hydrolase SUMMARY #length 152 #molecular-weight 17035 #checksum 981 SEQUENCE /// ENTRY YXECIC #type complete TITLE isochorismatase (EC 3.3.2.1) - Escherichia coli (strain K-12) ALTERNATE_NAMES 2,3 dihydro-2,3 dihydroxybenzoate synthase ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 01-Mar-2002 ACCESSIONS C91904; B91903; A64793; A32046; B32047 REFERENCE A91904 !$#authors Liu, J.; Duncan, K.; Walsh, C.T. !$#journal J. Bacteriol. (1989) 171:791-798 !$#title Nucleotide sequence of a cluster of Escherichia coli !1enterobactin biosynthesis genes: identification of entA and !1purification of its product 2,3-dihydro-2, !13-dihydroxybenzoate dehydrogenase. !$#cross-references MUID:89123155; PMID:2521622 !$#accession C91904 !'##molecule_type DNA !'##residues 1-285 ##label LIU !'##cross-references GB:M24148; NID:g304949; PIDN:AAA16102.1; !1PID:g450381 REFERENCE A91903 !$#authors Nahlik, M.S.; Brickman, T.J.; Ozenberger, B.A.; McIntosh, !1M.A. !$#journal J. Bacteriol. (1989) 171:784-790 !$#title Nucleotide sequence and transcriptional organization of the !1Escherichia coli enterobactin biosynthesis cistrons entB and !1entA. !$#cross-references MUID:89123154; PMID:2521621 !$#accession B91903 !'##molecule_type DNA !'##residues 1-285 ##label NAH !'##cross-references GB:M24143; NID:g341118; PIDN:AAA76835.1; !1PID:g522182 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64793 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-285 ##label BLAT !'##cross-references GB:AE000165; GB:U00096; NID:g1786808; !1PIDN:AAC73696.1; PID:g1786811; UWGP:b0595 !'##experimental_source strain K-12, substrain MG1655 COMMENT This enzyme catalyzes the hydrolysis of isochorismate to 2, !13-dihydro-2,3-dihydroxybenzoate and pyruvate. This reaction !1is part of the biosynthesis pathway for enterobactin, which !1is an iron-chelating compound involved in transporting iron !1from the bacterial environment into the cell cytoplasm. GENETICS !$#gene entB !$#map_position 14 min CLASSIFICATION #superfamily isochorismatase KEYWORDS enterobactin biosynthesis; ether hydrolase SUMMARY #length 285 #molecular-weight 32554 #checksum 9478 SEQUENCE /// ENTRY A29939 #type complete TITLE epoxide hydrolase (EC 3.3.2.3) 1, microsomal - human ALTERNATE_NAMES microsomal xenobiotic epoxide hydrolase ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 24-Sep-1999 ACCESSIONS A29939; S03114; A26856; I52380; S45275; I54369 REFERENCE A29939 !$#authors Skoda, R.C.; Demierre, A.; McBride, O.W.; Gonzalez, F.J.; !1Meyer, U.A. !$#journal J. Biol. Chem. (1988) 263:1549-1554 !$#title Human microsomal xenobiotic epoxide hydrolase. Complementary !1DNA sequence, complementary DNA-directed expression in COS-1 !1cells, and chromosomal localization. !$#cross-references MUID:88087301; PMID:2891713 !$#accession A29939 !'##molecule_type mRNA !'##residues 1-455 ##label SKO !'##cross-references GB:J03518; NID:g340389; PIDN:AAA61305.1; !1PID:g340390 REFERENCE S03114 !$#authors Wilson, N.M.; Omiecinski, C.J. !$#submission submitted to the EMBL Data Library, June 1988 !$#accession S03114 !'##molecule_type mRNA !'##residues 1-455 ##label WIL !'##cross-references EMBL:X07936; NID:g34542; PIDN:CAA30759.1; !1PID:g34543 REFERENCE A26856 !$#authors Jackson, M.R.; Craft, J.A.; Burchell, B. !$#journal Nucleic Acids Res. (1987) 15:7188 !$#title Nucleotide and deduced amino acid sequence of human liver !1microsomal epoxide hydrolase. !$#cross-references MUID:88015564; PMID:3502697 !$#accession A26856 !'##molecule_type mRNA !'##residues 1-147,'N',149-347,'S',349-405,'F',407-419,'V',421-455 !1##label JAC !'##cross-references GB:Y00424; NID:g34537; PIDN:CAA68486.1; PID:g34538 !'##note the authors translated the codon TTC for residue 406 as Leu REFERENCE I52380 !$#authors Craft, J.A.; Jackson, M.R.; Burchell, B. !$#journal Biochem. Soc. Trans. (1987) 15:708-709 !$#title Partial nucleotide sequence of a cloned cDNA for human liver !1microsomal epoxide hydrolase. !$#accession I52380 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 9-111,'K',113-147,'N',149-242,'L',244-327 ##label CRA !'##cross-references GB:M36374; NID:g187511; PIDN:AAA59580.1; !1PID:g187512 REFERENCE S45275 !$#authors Papadopoulos, D.; Joernvall, H.; Rydstroem, J.; DePierre, !1J.W. !$#journal Biochim. Biophys. Acta (1994) 1206:253-262 !$#title Purification and initial characterization of microsomal !1epoxide hydrolase from the human adrenal gland. !$#cross-references MUID:94271826; PMID:8003529 !$#accession S45275 !'##molecule_type protein !'##residues 1,'X',3-7 ##label PAP !'##experimental_source adrenal gland of kidney REFERENCE I54369 !$#authors Hassett, C.; Aicher, L.; Sidhu, J.S.; Omiecinski, C.J. !$#journal Hum. Mol. Genet. (1994) 3:421-428 !$#title Human microsomal epoxide hydrolase: genetic polymorphism and !1functional expression in vitro of amino acid variants. !$#cross-references MUID:94282033; PMID:7516776 !$#accession I54369 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-395,'I',397-455 ##label RES !'##cross-references GB:L25878; NID:g450268; PIDN:AAA52389.1; !1PID:g450269 GENETICS !$#gene GDB:EPHX1 !'##cross-references GDB:119876; OMIM:132810 !$#map_position 1p11-1qter CLASSIFICATION #superfamily epoxide hydrolase KEYWORDS aromatic hydrocarbon catabolism; detoxification; endoplasmic !1reticulum; ether hydrolase; transmembrane protein SUMMARY #length 455 #molecular-weight 52948 #checksum 1615 SEQUENCE /// ENTRY YXRBH #type complete TITLE epoxide hydrolase (EC 3.3.2.3) - rabbit ALTERNATE_NAMES microsomal epoxide hydrolase ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 04-Dec-1986 #sequence_revision 11-Apr-1997 #text_change 18-Jun-1999 ACCESSIONS S04342; A00905 REFERENCE S04342 !$#authors Hassett, C.; Turnblom, S.M.; DeAngeles, A.; Omiecinski, C.J. !$#journal Arch. Biochem. Biophys. (1989) 271:380-389 !$#title Rabbit microsomal epoxide hydrolase: isolation and !1characterization of the xenobiotic metabolizing enzyme cDNA. !$#cross-references MUID:89271920; PMID:2729997 !$#accession S04342 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-455 ##label HAS !'##cross-references GB:M21496; NID:g165481; PIDN:AAA31392.1; !1PID:g165482 REFERENCE A00905 !$#authors Heinemann, F.S.; Ozols, J. !$#journal J. Biol. Chem. (1984) 259:797-804 !$#title The covalent structure of hepatic microsomal epoxide !1hydrolase. II. The complete amino acid sequence. !$#cross-references MUID:84111558; PMID:6693396 !$#accession A00905 !'##molecule_type protein !'##residues 1-67,71-112,'L',114-200,'N',202,'V',204-211,'RISSY', !1213-247,'DL',250-302,'Q',304-365,'W',367,'RTHY',372-454 !1##label HEI !'##experimental_source New Zealand white breed !'##note the enzyme was purified from the phenobarbital-stimulated liver COMMENT This enzyme acts on epoxides (alkene oxides, oxiranes) and !1arene oxides. It was found in essentially all tissues of !1rats and mice. CLASSIFICATION #superfamily epoxide hydrolase KEYWORDS aromatic hydrocarbon catabolism; detoxification; endoplasmic !1reticulum; ether hydrolase; transmembrane protein SUMMARY #length 455 #molecular-weight 52511 #checksum 7597 SEQUENCE /// ENTRY A26081 #type complete TITLE epoxide hydrolase (EC 3.3.2.3) - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A26732; A26081 REFERENCE A26732 !$#authors Falany, C.N.; McQuiddy, P.; Kasper, C.B. !$#journal J. Biol. Chem. (1987) 262:5924-5930 !$#title Structure and organization of the microsomal xenobiotic !1epoxide hydrolase gene. !$#cross-references MUID:87194796; PMID:3032949 !$#accession A26732 !'##molecule_type DNA !'##residues 1-455 ##label FAL REFERENCE A26081 !$#authors Porter, T.D.; Beck, T.W.; Kasper, C.B. !$#journal Arch. Biochem. Biophys. (1986) 248:121-129 !$#title Complementary DNA and amino acid sequence of rat liver !1microsomal, xenobiotic epoxide hydrolase. !$#cross-references MUID:86267750; PMID:3755318 !$#accession A26081 !'##molecule_type mRNA !'##residues 1-455 ##label POR !'##cross-references GB:M26125; NID:g207688; PIDN:AAA42350.1; !1PID:g207689 CLASSIFICATION #superfamily epoxide hydrolase KEYWORDS ether hydrolase; transmembrane protein SUMMARY #length 455 #molecular-weight 52581 #checksum 1675 SEQUENCE /// ENTRY JC4686 #type complete TITLE juvenile-hormone epoxide hydrolase (EC 3.3.2.-) - tobacco hornworm ORGANISM #formal_name Manduca sexta #common_name tobacco hornworm DATE 16-Aug-1996 #sequence_revision 23-Aug-1996 #text_change 18-Jun-1999 ACCESSIONS JC4686 REFERENCE JC4686 !$#authors Wojtasek, H.; Prestwich, G.D. !$#journal Biochem. Biophys. Res. Commun. (1996) 220:323-329 !$#title An insect juvenile hormone-specific epoxide hydrolase is !1related to vertebrate microsomal epoxide hydrolases. !$#cross-references MUID:96184652; PMID:8645304 !$#accession JC4686 !'##molecule_type mRNA !'##residues 1-462 ##label WOJ !'##cross-references GB:U46682; NID:g1276939; PIDN:AAC47018.1; !1PID:g1276940 !'##note parts of this sequence were determined by protein sequencing FUNCTION !$#description catalyzes hydration of juvenile hormone, an epoxide, to a !1glycol !$#pathway catabolism of juvenile hormone !$#note modulates metamorphosis by inactivating juvenile hormone CLASSIFICATION #superfamily epoxide hydrolase KEYWORDS aromatic hydrocarbon catabolism; ether hydrolase FEATURE !$154 #binding_site substrate (Trp) #status predicted\ !$227,350,401,428 #active_site Asp, Asp, Glu, His #status predicted SUMMARY #length 462 #molecular-weight 52611 #checksum 2463 SEQUENCE /// ENTRY S65947 #type complete TITLE leukotriene-A4 hydrolase (EC 3.3.2.6) long isoform - human ALTERNATE_NAMES LTA4 hydrolase ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S65947; A33886; A27415; S70627; S70650; A61165; A61447; !1S15136 REFERENCE S65947 !$#authors Mancini, J.A.; Evans, J.F. !$#journal Eur. J. Biochem. (1995) 231:65-71 !$#title Cloning and characterization of the human leukotriene A(4) !1hydrolase gene. !$#cross-references MUID:95354704; PMID:7628486 !$#accession S65947 !'##molecule_type DNA !'##residues 1-611 ##label MAN !'##cross-references EMBL:U27292 REFERENCE A33886 !$#authors Funk, C.D.; Radmark, O.; Fu, J.Y.; Matsumoto, T.; Joernvall, !1H.; Shimizu, T.; Samuelsson, B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:6677-6681 !$#title Molecular cloning and amino acid sequence of leukotriene A-4 !1hydrolase. !$#cross-references MUID:88016154; PMID:2821541 !$#accession A33886 !'##molecule_type mRNA !'##residues 1-611 ##label FUN !'##cross-references GB:J02959; NID:g187174; PIDN:AAA36177.1; !1PID:g307131 !'##note parts of this sequence, including the amino end of the mature !1protein, were confirmed by peptide sequencing REFERENCE A27415 !$#authors Minami, M.; Ohno, S.; Kawasaki, H.; Radmark, O.; Samuelsson, !1B.; Joernvall, H.; Shimizu, T.; Seyama, Y.; Suzuki, K. !$#journal J. Biol. Chem. (1987) 262:13873-13876 !$#title Molecular cloning of a cDNA coding for human leukotriene A-4 !1hydrolase. Complete primary structure of an enzyme involved !1in eicosanoid synthesis. !$#cross-references MUID:88007621; PMID:3654641 !$#accession A27415 !'##molecule_type mRNA !'##residues 1-611 ##label MIN !'##cross-references GB:J03459; NID:g187172; PIDN:AAA36176.1; !1PID:g307130 REFERENCE S70627 !$#authors Jendraschak, E.; Kaminski, W.E.; Kiefl, R.; von Schacky, C. !$#journal Biochem. J. (1996) 314:733-737 !$#title The human leukotriene A(4) hydrolase gene is expressed in !1two alternatively spliced mRNA forms. !$#cross-references MUID:96177841; PMID:8615763 !$#accession S70627 !'##molecule_type mRNA !'##residues 511-611 ##label JEN !$#accession S70650 !'##molecule_type DNA !'##residues 511-537 ##label JEW !'##cross-references EMBL:U43410 REFERENCE A61165 !$#authors Odlander, B.; Haeggstroem, J.; Bergman, T.; Radmark, O.; !1Wetterholm, A.; Claesson, H.E. !$#journal Adv. Prostaglandin Thromboxane Leukotriene Res. (1990) !121:133-136 !$#title Leukotriene A-4 hydrolase in the B-lymphocytic cell line !1RAJI. !$#accession A61165 !'##molecule_type protein !'##residues 2-7,'X',9-16,'X',18-22 ##label ODL REFERENCE A61447 !$#authors Radmark, O.; Shimizu, T.; Joernvall, H.; Samuelsson, B. !$#journal J. Biol. Chem. (1984) 259:12339-12345 !$#title Leukotriene A-4 hydrolase in human leukocytes. Purification !1and properties. !$#cross-references MUID:85030308; PMID:6490615 !$#accession A61447 !'##molecule_type protein !'##residues 2-7,'X',9-16 ##label RAD REFERENCE S15136 !$#authors Odlander, B.; Claesson, H.E.; Bergman, T.; Radmark, O.; !1Joernvall, H.; Haeggstroem, J.Z. !$#journal Arch. Biochem. Biophys. (1991) 287:167-174 !$#title Leukotriene A(4) hydrolase in the human B-lymphocytic cell !1line Raji: indications of catalytically divergent forms of !1the enzyme. !$#cross-references MUID:91378377; PMID:1897988 !$#accession S15136 !'##status preliminary !'##molecule_type protein !'##residues 2-7,'X',9-16,'X',18-22 ##label OD2 GENETICS !$#gene GDB:LTA4H !'##cross-references GDB:128992; OMIM:151570 !$#map_position 12q22-12q22 !$#introns 53/3; 97/2; 137/3; 160/3; 195/3; 213/2; 237/3; 284/3; 292/3; !1316/2; 353/3; 402/1; 436/3; 460/2; 478/3; 510/3; 538/2; 573/ !12 FUNCTION !$#description catalyzes the hydrolysis of leukotriene A4 to leukotriene B4 CLASSIFICATION #superfamily leukotriene-A4 hydrolase KEYWORDS alternative splicing; ether hydrolase; zinc FEATURE !$296,300,319 #binding_site zinc (His, His, Glu) #status predicted SUMMARY #length 611 #molecular-weight 69285 #checksum 5606 SEQUENCE /// ENTRY S20444 #type complete TITLE leukotriene-A4 hydrolase (EC 3.3.2.6) - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S20444 REFERENCE S20444 !$#authors Makita, N.; Funk, C.D.; Imai, E.; Hoover, R.L.; Badr, K.F. !$#journal FEBS Lett. (1992) 299:273-277 !$#title Molecular cloning and functional expression of rat !1leukotriene A(4) hydrolase using the polymerase chain !1reaction. !$#cross-references MUID:92183952; PMID:1544505 !$#accession S20444 !'##molecule_type mRNA !'##residues 1-610 ##label MAK !'##cross-references GB:S87522; NID:g247155; PIDN:AAB21778.1; !1PID:g247156 CLASSIFICATION #superfamily leukotriene-A4 hydrolase KEYWORDS ether hydrolase SUMMARY #length 610 #molecular-weight 69175 #checksum 9336 SEQUENCE /// ENTRY JN0066 #type complete TITLE leukotriene-A4 hydrolase (EC 3.3.2.6) - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JN0066; PS0227 REFERENCE JN0066 !$#authors Medina, J.F.; Radmark, O.; Funk, C.D.; Haeggstroem, J.Z. !$#journal Biochem. Biophys. Res. Commun. (1991) 176:1516-1524 !$#title Molecular cloning and expression of mouse leukotriene A4 !1hydrolase cDNA. !$#cross-references MUID:91248250; PMID:1710117 !$#accession JN0066 !'##molecule_type mRNA !'##residues 1-611 ##label MED !'##cross-references GB:M63848; NID:g198883; PIDN:AAB59675.1; !1PID:g198884 !$#accession PS0227 !'##molecule_type mRNA !'##residues 70-592,'K',594-611 ##label ME2 COMMENT This enzyme catalyzes the hydrolysis of leukotriene A4 to !1leukotriene B4. CLASSIFICATION #superfamily leukotriene-A4 hydrolase KEYWORDS ether hydrolase; zinc FEATURE !$296,300,319 #binding_site zinc (His, His, Glu) #status predicted SUMMARY #length 611 #molecular-weight 69048 #checksum 3944 SEQUENCE /// ENTRY JC4237 #type complete TITLE leukotriene-A4 hydrolase (EC 3.3.2.6) - guinea pig ORGANISM #formal_name Cavia porcellus #common_name guinea pig DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS JC4237; PC4068; S01018; A61637 REFERENCE JC4237 !$#authors Minami, M.; Mutoh, H.; Ohishi, N.; Honda, Z.; Bito, H.; !1Shimizu, T. !$#journal Gene (1995) 161:249-251 !$#title Amino-acid sequence and tissue distribution of guinea-pig !1leukotriene A4 hydrolase. !$#cross-references MUID:95394365; PMID:7665088 !$#accession JC4237 !'##molecule_type mRNA !'##residues 1-611 ##label MIN !'##cross-references DDBJ:D16669; NID:g391692; PIDN:BAA04077.1; !1PID:g1255596 !'##experimental_source lung !$#accession PC4068 !'##molecule_type protein !'##residues !12-20;84-91;113-126;196-204;231-240;289-300;338-352;366-375; !1387-406;410-414;419-434;483-491;574-580 ##label MI2 REFERENCE S01018 !$#authors Haeggstroem, J.; Bergman, T.; Joernvall, H.; Radmark, O. !$#journal Eur. J. Biochem. (1988) 174:717-724 !$#title Guinea-pig liver leukotriene A4 hydrolase: purification, !1characterization and structural properties. !$#cross-references MUID:88271346; PMID:3391178 !$#accession S01018 !'##molecule_type protein !'##residues 2-21 ##label HAE !'##experimental_source liver REFERENCE A61637 !$#authors Bito, H.; Ohishi, N.; Miki, I.; Minami, M.; Tanabe, T.; !1Shimizu, T.; Seyama, Y. !$#journal J. Biochem. (1989) 105:261-264 !$#title Leukotriene A-4 hydrolase from guinea pig lung: the presence !1of two catalytically active forms. !$#cross-references MUID:89255172; PMID:2722767 !$#accession A61637 !'##molecule_type protein !'##residues 2-7,'X',9-16,'X',18-21 ##label BIT !'##experimental_source lung COMMENT This enzyme is a cytosolic enzyme which converts leukotriene !1A4 intothe chemotactic compound leukotriene B4. This enzyme !1also possesses other cellular roles that are distinct from !1leukotriene B4 synthesis. CLASSIFICATION #superfamily leukotriene-A4 hydrolase KEYWORDS ether hydrolase; zinc FEATURE !$296,300,319 #binding_site zinc (His, His, Glu) #status predicted\ !$297 #active_site Glu #status predicted SUMMARY #length 611 #molecular-weight 68970 #checksum 2072 SEQUENCE /// ENTRY APBPML #type complete TITLE endopeptidase (EC 3.4.-.-) - phage lambda ORGANISM #formal_name phage lambda DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 18-Jun-1999 ACCESSIONS A94614; C92891; JN0749; A00906 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession A94614 !'##molecule_type DNA !'##residues 1-153 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession C92891 !'##molecule_type DNA !'##residues 1-153 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96599.1; PID:g215165 REFERENCE JN0749 !$#authors Hanych, B.; Kedzierska, S.; Walderich, B.; Uznanski, B.; !1Taylor, A. !$#journal Gene (1993) 129:1-8 !$#title Expression of the Rz gene and the overlapping Rz1 reading !1frame present at the right end of the bacteriophage lambda !1genome. !$#cross-references MUID:93328108; PMID:8335247 !$#accession JN0749 !'##molecule_type DNA !'##residues 1-153 ##label HAN COMMENT Gene Rz is necessary for host cell lysis. It is believed to !1code for an endopeptidase that cleaves the amino-carboxyl !1cross-link between the diaminopimelic acid and D-alanine !1residues in the murein component of the bacterial cell wall. GENETICS !$#gene Rz !$#map_position 94.77-95.72 CLASSIFICATION #superfamily phage PA2 endopeptidase KEYWORDS host cell lysis; hydrolase SUMMARY #length 153 #molecular-weight 17229 #checksum 8129 SEQUENCE /// ENTRY APBP21 #type complete TITLE endopeptidase (EC 3.4.-.-) - phage 21 ALTERNATE_NAMES gene Rz protein; lysis protein Rz ORGANISM #formal_name phage 21 DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 18-Jun-1999 ACCESSIONS S22907 REFERENCE S22905 !$#authors Bonovich, M.T.; Young, R. !$#journal J. Bacteriol. (1991) 173:2897-2905 !$#title Dual start motif in two lambdoid S genes unrelated to lambda !1S. !$#cross-references MUID:91210180; PMID:2019562 !$#accession S22907 !'##molecule_type DNA !'##residues 1-153 ##label BON !'##cross-references EMBL:M65239; NID:g215466; PIDN:AAA32351.1; !1PID:g215469 GENETICS !$#gene Rz CLASSIFICATION #superfamily phage PA2 endopeptidase KEYWORDS host cell lysis; hydrolase SUMMARY #length 153 #molecular-weight 17325 #checksum 191 SEQUENCE /// ENTRY APBPP2 #type fragment TITLE endopeptidase (EC 3.4.-.-) - phage PA2 (fragment) ALTERNATE_NAMES lysis protein ORGANISM #formal_name phage PA2 #note host Escherichia coli DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 18-Jun-1999 ACCESSIONS B25647 REFERENCE A25647 !$#authors Blasband, A.J.; Marcotte Jr., W.R.; Schnaitman, C.A. !$#journal J. Biol. Chem. (1986) 261:12723-12732 !$#title Structure of the lc and nmpC outer membrane porin protein !1genes of lambdoid bacteriophage. !$#cross-references MUID:86304457; PMID:3017988 !$#accession B25647 !'##molecule_type DNA !'##residues 1-64 ##label BLA !'##cross-references GB:J02580; NID:g215366; PIDN:AAA32299.1; !1PID:g553011 GENETICS !$#gene Rz !$#start_codon GTG CLASSIFICATION #superfamily phage PA2 endopeptidase KEYWORDS host cell lysis; hydrolase SUMMARY #length 64 #checksum 5930 SEQUENCE /// ENTRY APBP22 #type complete TITLE probable endopeptidase (EC 3.4.-.-) - phage P22 ALTERNATE_NAMES lysis protein ORGANISM #formal_name phage P22 #note host Salmonella typhimurium DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 18-Jun-1999 ACCESSIONS A33080 REFERENCE A33080 !$#authors Casjens, S.; Eppler, K.; Parr, R.; Poteete, A.R. !$#journal Virology (1989) 171:588-598 !$#title Nucleotide sequence of the bacteriophage P22 gene 19 to 3 !1region: identification of a new gene required for lysis. !$#cross-references MUID:89348017; PMID:2763468 !$#accession A33080 !'##molecule_type DNA !'##residues 1-145 ##label CAS !'##cross-references GB:J04356; NID:g215265; PIDN:AAA88341.1; !1PID:g215267 GENETICS !$#gene 15 CLASSIFICATION #superfamily phage PA2 endopeptidase KEYWORDS host cell lysis; hydrolase SUMMARY #length 145 #molecular-weight 16218 #checksum 8506 SEQUENCE /// ENTRY ESECGD #type complete TITLE glycerophosphodiester phosphodiesterase (EC 3.1.4.46) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 01-Mar-2002 ACCESSIONS JV0024; S15946; S47668; S04865; D65141; S14530 REFERENCE JV0024 !$#authors Kasahara, M.; Makino, K.; Amemura, M.; Nakata, A. !$#journal Nucleic Acids Res. (1989) 17:2854 !$#title Nucleotide sequence of the ugpQ gene encoding !1glycerophosphoryl diester phosphodiesterase of Escherichia !1coli K-12. !$#cross-references MUID:89240042; PMID:2541415 !$#accession JV0024 !'##molecule_type DNA !'##residues 1-247 ##label KAS !'##cross-references GB:X14437; NID:g43250; PIDN:CAA32609.1; PID:g43251 !'##experimental_source strain K12 REFERENCE S15945 !$#authors Tommassen, J.; Eiglmeier, K.; Cole, S.T.; Overduin, P.; !1Larson, T.J.; Boos, W. !$#journal Mol. Gen. Genet. (1991) 226:321-327 !$#title Characterization of two genes, glpQ and ugpQ, encoding !1glycerophosphoryl diester phosphodiesterases of Escherichia !1coli. !$#cross-references MUID:91238712; PMID:1851953 !$#accession S15946 !'##molecule_type DNA !'##residues 1-247 ##label TOM !'##cross-references EMBL:X56908; NID:g43252; PIDN:CAA40224.1; !1PID:g43253 REFERENCE S47666 !$#authors Plunkett, G. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S47668 !'##molecule_type DNA !'##residues 1-247 ##label PLU !'##cross-references EMBL:U00039; NID:g466582; PIDN:AAB18424.1; !1PID:g466585 REFERENCE S03780 !$#authors Overduin, P.; Boos, W.; Tommassen, J. !$#journal Mol. Microbiol. (1988) 2:767-775 !$#title Nucleotide sequence of the ugp genes of Escherichia coli !1K-12: homology to the maltose system. !$#cross-references MUID:89096498; PMID:3062310 !$#accession S04865 !'##status translation not shown !'##molecule_type DNA !'##residues 1-50 ##label OVE !'##cross-references EMBL:X13141; NID:g43243; PIDN:CAA31535.1; !1PID:g581245 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65141 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-247 ##label BLAT !'##cross-references GB:AE000421; GB:U00096; NID:g1789854; !1PIDN:AAC76474.1; PID:g1789858; UWGP:b3449 !'##experimental_source strain K-12, substrain MG1655 COMMENT This enzyme catalyzes the hydrolysis of glycerophosphoryl !1diesters, i.e., deacylated phospholipids, to !1sn-glycerol-3-phosphate and the corresponding alcohols only !1during the phosphate-regulon-dependent high affinity !1transport process of the diesters. However, it is not !1essential for translocation of glycerophosphoryl diesters or !1sn-glycerol-3-phosphate. GENETICS !$#gene ugpQ !$#map_position 76 min CLASSIFICATION #superfamily glycerophosphodiester phosphodiesterase KEYWORDS glycerol metabolism; phosphoric diester hydrolase SUMMARY #length 247 #molecular-weight 27409 #checksum 9484 SEQUENCE /// ENTRY APBOL #type complete TITLE leucyl aminopeptidase (EC 3.4.11.1), renal - bovine ALTERNATE_NAMES cytosol aminopeptidase; leucine aminopeptidase ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Aug-1980 #sequence_revision 19-May-1995 #text_change 09-Dec-2002 ACCESSIONS A54338; A00907 REFERENCE A54338 !$#authors Wallner, B.P.; Hession, C.; Tizard, R.; Frey, A.Z.; Zuliani, !1A.; Mura, C.; Jahngen-Hodge, J.; Taylor, A. !$#journal Biochemistry (1993) 32:9296-9301 !$#title Isolation of bovine kidney leucine aminopeptidase cDNA: !1comparison with the lens enzyme and tissue-specific !1expression of two mRNAs. !$#cross-references MUID:93378980; PMID:8369298 !$#accession A54338 !'##molecule_type mRNA !'##residues 1-513 ##label WAL !'##cross-references GB:S65367; NID:g410688; PIDN:AAB28170.1; !1PID:g410689 !'##experimental_source kidney !'##note sequence extracted from NCBI backbone (NCBIN:137416, !1NCBIP:137417) REFERENCE A92380 !$#authors Cuypers, H.T.; van Loon-Klaassen, L.A.H.; Vree Egberts, !1W.T.M.; de Jong, W.W.; Bloemendal, H. !$#journal J. Biol. Chem. (1982) 257:7077-7085 !$#title The primary structure of leucine aminopeptidase from bovine !1eye lens. !$#cross-references MUID:82213853; PMID:7085616 !$#accession A00907 !'##molecule_type protein !'##residues 27-70,'P',72-407,'M',410-499,508-513 ##label CUY !'##experimental_source eye lens REFERENCE A92381 !$#authors Cuypers, H.T.; van Loon-Klaassen, L.A.H.; Vree Egberts, !1W.T.M.; de Jong, W.W.; Bloemendal, H. !$#journal J. Biol. Chem. (1982) 257:7086-7091 !$#title Sulfhydryl content of bovine eye lens leucine !1aminopeptidase. Determination of the reactivity of the !1sulfhydryl groups of the zinc metalloenzyme, of the enzyme !1activated by Mg(2+), Mn(2+), and Co(2+), and of the !1metal-free apoenzyme. !$#cross-references MUID:82213854; PMID:7085617 !$#contents annotation !$#note no disulfide bonds are present COMMENT This protein is a hexamer of identical chains. CLASSIFICATION #superfamily Leucyl aminopeptidase KEYWORDS aminopeptidase SUMMARY #length 513 #molecular-weight 55575 #checksum 259 SEQUENCE /// ENTRY APECA #type complete TITLE leucyl aminopeptidase (EC 3.4.11.1) A - Escherichia coli (strain K-12) ALTERNATE_NAMES aminopeptidase I; cytosol aminopeptidase A ORGANISM #formal_name Escherichia coli DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 09-Dec-2002 ACCESSIONS S04462; A33212; S56486; S58667; G65238 REFERENCE S04462 !$#authors Stirling, C.J.; Colloms, S.D.; Collins, J.F.; Szatmari, G.; !1Sherratt, D.J. !$#journal EMBO J. (1989) 8:1623-1627 !$#title xerB, an Escherichia coli gene required for plasmid ColE1 !1site-specific recombination, is identical to pepA, encoding !1aminopeptidase A, a protein with substantial similarity to !1bovine lens leucine aminopeptidase. !$#cross-references MUID:89356633; PMID:2670557 !$#accession S04462 !'##molecule_type DNA !'##residues 1-503 ##label STI !'##cross-references EMBL:X15130; NID:g43308; PIDN:CAA33225.1; !1PID:g43309 !$#accession A33212 !'##molecule_type protein !'##residues 1-20 ##label ST2 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56486 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-503 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97157.1; !1PID:g537102 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE S58667 !$#authors Charlier, D.; Hassanzadeh Gh, G.; Kholti, A.; Gigot, D.; !1Pierard, A.; Glansdorff, N. !$#journal J. Mol. Biol. (1995) 250:392-406 !$#title carP, Involved in pyrimidine regulation of the Escherichia !1coli carbamoylphosphate synthetase operon encodes a !1sequence-specific DNA-binding protein identical to XerB and !1PepA, also required for resolution of ColEI multimers. !$#cross-references MUID:95341674; PMID:7616564 !$#accession S58667 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-503 ##label CHA !'##cross-references GB:X86443; NID:g1054724; PIDN:CAA60164.1; !1PID:g1054725 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65238 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-503 ##label BLAT !'##cross-references GB:AE000496; GB:U00096; NID:g2367366; !1PIDN:AAC77217.1; PID:g1790710; UWGP:b4260 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene pepA; xerB !$#map_position 96.5 min FUNCTION !$#description release of N-terminal amino acid, preferably linked to Leu CLASSIFICATION #superfamily Leucyl aminopeptidase KEYWORDS aminopeptidase FEATURE !$1-503 #product cytosol aminopeptidase A #status !8experimental #label MAT SUMMARY #length 503 #molecular-weight 54879 #checksum 7897 SEQUENCE /// ENTRY C64137 #type complete TITLE leucyl aminopeptidase (EC 3.4.11.1) A - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Dec-2002 ACCESSIONS C64137 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession C64137 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-491 ##label TIGR !'##cross-references GB:U32843; GB:L42023; NID:g1574554; !1PIDN:AAC23351.1; PID:g1574559; TIGR:HI1705 CLASSIFICATION #superfamily Leucyl aminopeptidase KEYWORDS aminopeptidase SUMMARY #length 491 #molecular-weight 53529 #checksum 9493 SEQUENCE /// ENTRY S22399 #type complete TITLE leucyl aminopeptidase (EC 3.4.11.1) - Arabidopsis thaliana ALTERNATE_NAMES leucine aminopeptidase ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Dec-2002 ACCESSIONS S22399; G84633 REFERENCE S22399 !$#authors Bartling, D.; Weiler, E.W. !$#journal Eur. J. Biochem. (1992) 205:425-431 !$#title Leucine aminopeptidase from Arabidopsis thaliana. Molecular !1evidence for a phylogenetically conserved enzyme of protein !1turnover in higher plants. !$#cross-references MUID:92209533; PMID:1555602 !$#accession S22399 !'##molecule_type mRNA !'##residues 1-520 ##label BAR !'##cross-references EMBL:X63444; NID:g16393; PIDN:CAA45040.1; !1PID:g16394 REFERENCE A84420 !$#authors Lin, X.; Kaul, S.; Rounsley, S.D.; Shea, T.P.; Benito, M.I.; !1Town, C.D.; Fujii, C.Y.; Mason, T.M.; Bowman, C.L.; !1Barnstead, M.E.; Feldblyum, T.V.; Buell, C.R.; Ketchum, !1K.A.; Lee, J.J.; Ronning, C.M.; Koo, H.; Moffat, K.S.; !1Cronin, L.A.; Shen, M.; VanAken, S.E.; Umayam, L.; Tallon, !1L.J.; Gill, J.E.; Adams, M.D.; Carrera, A.J.; Creasy, T.H.; !1Goodman, H.M.; Somerville, C.R.; Copenhaver, G.P.; Preuss, !1D.; Nierman, W.C.; White, O.; Eisen, J.A.; Salzberg, S.L.; !1Fraser, C.M.; Venter, J.C. !$#journal Nature (1999) 402:761-768 !$#title Sequence and analysis of chromosome 2 of the plant !1Arabidopsis thaliana. !$#cross-references MUID:20083487; PMID:10617197 !$#accession G84633 !'##status preliminary !'##molecule_type DNA !'##residues 1-520 ##label STO !'##cross-references GB:AE002093; NID:g4115380; PIDN:AAD03381.1; !1GSPDB:GN00139 GENETICS !$#gene At2g24200 !$#map_position 2 CLASSIFICATION #superfamily Leucyl aminopeptidase KEYWORDS aminopeptidase SUMMARY #length 520 #molecular-weight 54509 #checksum 9268 SEQUENCE /// ENTRY A48788 #type complete TITLE leucyl aminopeptidase (EC 3.4.11.1) DR57 - tomato ORGANISM #formal_name Lycopersicon esculentum #common_name tomato DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Dec-2002 ACCESSIONS A48788 REFERENCE A48788 !$#authors Pautot, V.; Holzer, F.M.; Reisch, B.; Walling, L.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:9906-9910 !$#title Leucine aminopeptidase: an inducible component of the !1defense response in Lycopersicon esculentum (tomato). !$#cross-references MUID:94052201; PMID:8234334 !$#accession A48788 !'##status preliminary; nucleic acid sequence not shown; not compared !1with conceptual translation !'##molecule_type mRNA !'##residues 1-469 ##label PAU !'##cross-references PIDN:AAB28717.1; PID:g440604 !'##experimental_source Peto 238R, leaves !'##note sequence extracted from NCBI backbone (NCBIP:139497) CLASSIFICATION #superfamily Leucyl aminopeptidase KEYWORDS aminopeptidase SUMMARY #length 469 #molecular-weight 49198 #checksum 1895 SEQUENCE /// ENTRY S41376 #type complete TITLE leucyl aminopeptidase (EC 3.4.11.1) - potato ALTERNATE_NAMES wound-induced protein (clone 17) ORGANISM #formal_name Solanum tuberosum #common_name potato DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Dec-2002 ACCESSIONS S41376; PQ0470; S24769 REFERENCE S41376 !$#authors Herbers, K.; Prat, S.; Willmitzer, L. !$#submission submitted to the EMBL Data Library, December 1993 !$#description Functional analysis of a leucine aminopeptidase from Solanum !1tuberosum L. !$#accession S41376 !'##status preliminary !'##molecule_type mRNA !'##residues 1-573 ##label HER !'##cross-references EMBL:X77015; NID:g443978; PIDN:CAA54314.1; !1PID:g443979 REFERENCE JQ1692 !$#authors Hildmann, T.; Ebneth, M.; Pena-Cortes, H.; Sanchez-Serrano, !1J.J.; Willmitzer, L.; Prat, S. !$#journal Plant Cell (1992) 4:1157-1170 !$#title General roles of abscisic and jasmonic acids in gene !1activation as a result of mechanical wounding. !$#cross-references MUID:93005746; PMID:1392612 !$#accession PQ0470 !'##molecule_type mRNA !'##residues 20-573 ##label HIL !'##cross-references EMBL:X67845; NID:g21486; PIDN:CAA48038.1; !1PID:g21487 !'##experimental_source strain desiree CLASSIFICATION #superfamily Leucyl aminopeptidase KEYWORDS aminopeptidase SUMMARY #length 573 #molecular-weight 60122 #checksum 8915 SEQUENCE /// ENTRY DPECN #type complete TITLE membrane alanyl aminopeptidase (EC 3.4.11.2) - Escherichia coli (strain K-12) ALTERNATE_NAMES alpha-aminoacylpeptide hydrolase; aminopeptidase N; microsomal aminopeptidase ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 26-Sep-1997 #text_change 01-Mar-2002 ACCESSIONS C64833; A27164; A91561; A91163; B91163; I57748; A25058; !1A29045 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64833 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-870 ##label BLAT !'##cross-references GB:AE000195; GB:U00096; NID:g1787156; !1PIDN:AAC74018.1; PID:g1787163; UWGP:b0932 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A27164 !$#authors Foglino, M.; Gharbi, S.; Lazdunski, A. !$#journal Gene (1986) 49:303-309 !$#title Nucleotide sequence of the pepN gene encoding aminopeptidase !1N of Escherichia coli. !$#cross-references MUID:87192020; PMID:2436977 !$#accession A27164 !'##molecule_type DNA !'##residues 1-870 ##label FOG !'##cross-references GB:M15676; NID:g147143; PIDN:AAA24318.1; !1PID:g147144 REFERENCE A91561 !$#authors McCaman, M.T.; Gabe, J.D. !$#journal Gene (1986) 48:145-153 !$#title The nucleotide sequence of the pepN gene and its !1over-expression in Escherichia coli. !$#cross-references MUID:87163509; PMID:3549459 !$#accession A91561 !'##molecule_type DNA !'##residues 1-642,'R',644-870 ##label MCC REFERENCE A91163 !$#authors Bally, M.; Foglino, M.; Bruschi, M.; Murgier, M.; Lazdunski, !1A. !$#journal Eur. J. Biochem. (1986) 155:565-569 !$#title Nucleotide sequence of the promoter and amino-terminal !1encoding region of the Escherichia coli pepN gene. !$#cross-references MUID:86164315; PMID:2869947 !$#accession A91163 !'##molecule_type DNA !'##residues 1-176 ##label BA1 !'##cross-references GB:X03709; NID:g42354; PIDN:CAA27336.1; PID:g42356 !$#accession B91163 !'##molecule_type protein !'##residues 1-21 ##label BA2 REFERENCE I57748 !$#authors McCaman, M.T.; Gabe, J.D. !$#journal Mol. Gen. Genet. (1986) 204:148-152 !$#title Sequence of the promoter and 5' coding region of pepN, and !1the amino-terminus of peptidase N from Escherichia coli !1K-12. !$#cross-references MUID:86310300; PMID:3018440 !$#accession I57748 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-75,'D',77-242 ##label RES !'##cross-references EMBL:X04020; NID:g42352; PIDN:CAA27647.1; !1PID:g42353 COMMENT This enzyme is active in the cytoplasm and is probably bound !1to the inner surface of the cytoplasmic membrane. COMMENT This enzyme hydrolyzes L-amino acid beta-naphthylamides. GENETICS !$#gene pepN !$#map_position 21 min FUNCTION !$#description releases N-terminal amino acid residues from polypeptides !1and proteins !$#note requires zinc for proteolytic activity CLASSIFICATION #superfamily microsomal aminopeptidase KEYWORDS aminopeptidase; membrane protein; metalloproteinase; zinc FEATURE !$297,301,320 #binding_site zinc, catalytic (His, His, Glu) #status !8predicted\ !$381 #active_site Tyr #status predicted SUMMARY #length 870 #molecular-weight 98918 #checksum 257 SEQUENCE /// ENTRY DPECP #type complete TITLE X-Pro aminopeptidase (EC 3.4.11.9) II - Escherichia coli (strain K-12) ALTERNATE_NAMES aminoacylproline aminopeptidase; aminopeptidase P; proline aminopeptidase II ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 01-Mar-2002 ACCESSIONS JX0067; B47020; D65075; JQ0843 REFERENCE JX0067 !$#authors Yoshimoto, T.; Tone, H.; Honda, T.; Osatomi, K.; Kobayashi, !1R.; Tsuru, D. !$#journal J. Biochem. (1989) 105:412-416 !$#title Sequencing and high expression of aminopeptidase P gene from !1Escherichia coli HB101. !$#cross-references MUID:89278065; PMID:2659585 !$#accession JX0067 !'##molecule_type DNA !'##residues 1-441 ##label YOS !'##cross-references GB:D00398; NID:g216528; PIDN:BAA00299.1; !1PID:g216529 !'##experimental_source strain HB101 REFERENCE A47020 !$#authors Nakahigashi, K.; Miyamoto, K.; Nishimura, K.; Inokuchi, H. !$#journal J. Bacteriol. (1992) 174:7352-7359 !$#title Isolation and characterization of a light-sensitive mutant !1of Escherichia coli K-12 with a mutation in a gene that is !1required for the biosynthesis of ubiquinone. !$#cross-references MUID:93054351; PMID:1339425 !$#accession B47020 !'##molecule_type DNA !'##residues 1-441 ##label NAK !'##cross-references GB:D90281; NID:g216625; PIDN:BAA14325.1; !1PID:g216627 !'##experimental_source strain K12 CA274 !'##note sequence extracted from NCBI backbone (NCBIN:118090, !1NCBIP:118092) REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65075 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-441 ##label BLAT !'##cross-references GB:AE000374; GB:U00096; NID:g1789270; !1PIDN:AAC75946.1; PID:g1789275; UWGP:b2908 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene pepP !$#map_position 63 min CLASSIFICATION #superfamily aminopeptidase P KEYWORDS aminopeptidase; zinc SUMMARY #length 441 #molecular-weight 49815 #checksum 7631 SEQUENCE /// ENTRY JN0491 #type complete TITLE X-Pro aminopeptidase (EC 3.4.11.9) - Streptomyces lividans ALTERNATE_NAMES aminopeptidase P; PepP ORGANISM #formal_name Streptomyces lividans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Feb-2002 ACCESSIONS JN0491; PN0466 REFERENCE JN0491 !$#authors Butler, M.J.; Bergeron, A.; Soostmeyer, G.; Zimny, T.; !1Malek, L.T. !$#journal Gene (1993) 123:115-119 !$#title Cloning and characterisation of an aminopeptidase P-encoding !1gene from Streptomyces lividans. !$#cross-references MUID:93138419; PMID:8422994 !$#accession JN0491 !'##molecule_type DNA !'##residues 1-491 ##label BUT !'##cross-references GB:M91546; NID:g295165; PIDN:AAA26703.1; !1PID:g295167 !$#accession PN0466 !'##molecule_type protein !'##residues 2-16 ##label BU1 COMMENT This enzyme hydrolyses aminoacyl Prolyl bonds binds when !1proline is in the penultimate position from the amino !1terminus of a polypeptide. GENETICS !$#gene pepP CLASSIFICATION #superfamily aminopeptidase P KEYWORDS aminopeptidase SUMMARY #length 491 #molecular-weight 54048 #checksum 1781 SEQUENCE /// ENTRY KZEC #type complete TITLE alkaline phosphatase isozyme conversion protein (EC 3.4.11.-) precursor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 01-Mar-2002 ACCESSIONS A28382; E65056 REFERENCE A28382 !$#authors Ishino, Y.; Shinagawa, H.; Makino, K.; Amemura, M.; Nakata, !1A. !$#journal J. Bacteriol. (1987) 169:5429-5433 !$#title Nucleotide sequence of the iap gene, responsible for !1alkaline phosphatase isozyme conversion in Escherichia coli, !1and identification of the gene product. !$#cross-references MUID:88058748; PMID:3316184 !$#accession A28382 !'##molecule_type DNA !'##residues 1-345 ##label ISH !'##cross-references GB:M18270; NID:g146429; PIDN:AAA24005.1; !1PID:g146430 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65056 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-345 ##label BLAT !'##cross-references GB:AE000359; GB:U00096; NID:g1789110; !1PIDN:AAC75795.1; PID:g1789111; UWGP:b2753 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene iap !$#map_position 59 min FUNCTION !$#description this protein, presumably an aminopeptidase, mediates the !1conversion of E. coli alkaline phosphatase from isozyme 1 to !1isozymes 2 and 3 by proteolitically removing the two !1amino-terminal arginine residues one by one CLASSIFICATION #superfamily alkaline phosphatase isozyme conversion protein KEYWORDS aminopeptidase FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-345 #product alkaline phosphatase isozyme conversion !8protein #status predicted #label MAT SUMMARY #length 345 #molecular-weight 37920 #checksum 1871 SEQUENCE /// ENTRY DPECM #type complete TITLE methionyl aminopeptidase (EC 3.4.11.18) [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES metallooligopeptidase; methionine aminopeptidase; peptidase M ORGANISM #formal_name Escherichia coli DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 01-Mar-2002 ACCESSIONS A27761; S45233; H64740 REFERENCE A27761 !$#authors Ben-Bassat, A.; Bauer, K.; Chang, S.Y.; Myambo, K.; Boosman, !1A.; Chang, S. !$#journal J. Bacteriol. (1987) 169:751-757 !$#title Processing of the initiation methionine from proteins: !1properties of the Escherichia coli methionine aminopeptidase !1and its gene structure. !$#cross-references MUID:87109068; PMID:3027045 !$#accession A27761 !'##molecule_type DNA !'##residues 1-264 ##label BEN !'##cross-references GB:M15106; NID:g146726; PIDN:AAA24112.1; !1PID:g146727 !'##note comparative analyses indicate that residues adjacent to initial !1methionines of substrates significantly influence the !1hydrolysis REFERENCE S45181 !$#authors Fujita, N. !$#submission submitted to the EMBL Data Library, January 1994 !$#accession S45233 !'##molecule_type DNA !'##residues 1-264 ##label FUJ !'##cross-references EMBL:D26562; NID:g473770; PIDN:BAA05612.1; !1PID:g473823 !'##experimental_source strain K-12, substrain W3110 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64740 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-264 ##label BLAT !'##cross-references GB:AE000126; GB:U00096; NID:g1786358; !1PIDN:AAC73279.1; PID:g1786364; UWGP:b0168 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A51847 !$#authors Roderick, S.L.; Matthews, B.W. !$#submission submitted to the Brookhaven Protein Data Bank, December 1992 !$#cross-references PDB:1MAT !$#contents annotation; X-ray crystallography, 2.4 angstroms, residues !12-264 REFERENCE A49470 !$#authors Roderick, S.L.; Matthews, B.W. !$#journal Biochemistry (1993) 32:3907-3912 !$#title Structure of the cobalt-dependent methionine aminopeptidase !1from Escherichia coli: a new type of proteolytic enzyme. !$#cross-references MUID:93229487; PMID:8471602 !$#contents annotation; X-ray crystallography, 2.4 angstroms GENETICS !$#gene map !$#map_position 4 min COMPLEX monomer FUNCTION !$#description catalyzes hydrolysis of amino-terminal methionine from !1proteins CLASSIFICATION #superfamily Escherichia coli methionyl aminopeptidase KEYWORDS aminopeptidase; cobalt; metalloprotein; monomer; protein !1biosynthesis FEATURE !$97,108,235 #binding_site cobalt 2 (Asp, Asp, Glu) #status !8experimental\ !$108,171,204,235 #binding_site cobalt 1 (Asp, His, Glu, Glu) #status !8experimental SUMMARY #length 264 #molecular-weight 29331 #checksum 1511 SEQUENCE /// ENTRY C69585 #type complete TITLE aminopeptidase ampS - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS C69585 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69585 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-410 ##label KUN !'##cross-references GB:Z99111; GB:AL009126; NID:g2633699; !1PIDN:CAB13318.1; PID:g2633816 !'##experimental_source strain 168 GENETICS !$#gene ampS CLASSIFICATION #superfamily Bacillus aminopeptidase SUMMARY #length 410 #molecular-weight 45798 #checksum 3087 SEQUENCE /// ENTRY JN0087 #type complete TITLE leucyl aminopeptidase (EC 3.4.11.1) T - Thermus aquaticus ORGANISM #formal_name Thermus aquaticus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Feb-2002 ACCESSIONS JN0087; JC5864 REFERENCE JN0087 !$#authors Motoshima, H.; Azuma, N.; Kaminogawa, S.; Ono, M.; Minagawa, !1E.; Matsuzawa, H.; Ohta, T.; Yamauchi, K. !$#journal Agric. Biol. Chem. (1990) 54:2385-2392 !$#title Molecular cloning and nucleotide sequence of the !1aminopeptidase T gene of Thermus aquaticus YT-1 and its !1high-level expression in Escherichia coli. !$#cross-references MUID:91136783; PMID:1368580 !$#accession JN0087 !'##molecule_type DNA !'##residues 1-408 ##label MOT !'##cross-references GB:D87664; NID:g1526546; PIDN:BAA13426.1; !1PID:g1526548 !'##experimental_source strain YT-1 REFERENCE JC5862 !$#authors Motoshima, H.; Minagawa, E.; Tsukasaki, F.; Kaminogawa, S. !$#journal Biosci. Biotechnol. Biochem. (1997) 61:1710-1717 !$#title Cloning of genes of the aminopeptidase T family from Thermus !1thermophilus HB8 and Bacillus stearothermophilus NCIB8924: !1Apparent similarity to the leucyl aminopeptidase family. !$#cross-references MUID:98028210; PMID:9362117 !$#accession JC5864 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-408 ##label MO2 !'##cross-references DDBJ:D87664; NID:g1526546; PIDN:BAA13426.1; !1PID:g1526548 !'##experimental_source strain YT1 !'##note the authors translated the initiation codon GTG for residue 1 !1as Met COMMENT This enzyme is a highly thermostable, metallo-dependent !1(Co2+, Mg2+) dimeric protein with a broad substrate !1specificity. GENETICS !$#gene AP-T !$#start_codon GTG CLASSIFICATION #superfamily Bacillus aminopeptidase KEYWORDS aminopeptidase FEATURE !$305-312 #region leucyl aminopeptidase signature SUMMARY #length 408 #molecular-weight 44820 #checksum 3242 SEQUENCE /// ENTRY DPHUM2 #type complete TITLE methionyl aminopeptidase (EC 3.4.11.18) 2 - human ALTERNATE_NAMES p67; translation initiation factor eIF-2-associated protein ORGANISM #formal_name Homo sapiens #common_name man DATE 14-Jul-1995 #sequence_revision 23-Aug-1996 #text_change 01-Feb-2002 ACCESSIONS S52112 REFERENCE S52112 !$#authors Li, X.; Chang, Y.H. !$#journal Biochim. Biophys. Acta (1995) 1260:333-336 !$#title Molecular cloning of a human complementary DNA encoding an !1initiation factor 2-associated protein (p(67)). !$#cross-references MUID:95178556; PMID:7873610 !$#accession S52112 !'##molecule_type mRNA !'##residues 1-478 ##label LIX !'##cross-references GB:U13261; NID:g687242; PIDN:AAC63402.1; !1PID:g687243 GENETICS !$#gene GDB:P67EIF2 !'##cross-references GDB:512821 FUNCTION !$#description catalyzes hydrolysis of amino-terminal methionine from !1proteins CLASSIFICATION #superfamily human methionyl aminopeptidase KEYWORDS aminopeptidase; cobalt; metalloprotein; protein biosynthesis FEATURE !$251,262,459 #binding_site cobalt 2 (Asp, Asp, Glu) #status !8predicted\ !$262,331,364,459 #binding_site cobalt 1 (Asp, His, Glu, Glu) #status !8predicted SUMMARY #length 478 #molecular-weight 52891 #checksum 4484 SEQUENCE /// ENTRY AIBSAF #type fragment TITLE thermophilic aminopeptidase (EC 3.4.11.12) I alpha chain - Bacillus stearothermophilus (fragment) ORGANISM #formal_name Bacillus stearothermophilus DATE 30-Nov-1980 #sequence_revision 23-Oct-1981 #text_change 01-Feb-2002 ACCESSIONS A00908 REFERENCE A00908 !$#authors Stoll, E.; Ericsson, L.H.; Zuber, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1973) 70:3781-3784 !$#title The function of two subunits of thermophilic aminopeptidase !1I. !$#cross-references MUID:74087636; PMID:4521203 !$#accession A00908 !'##molecule_type protein !'##residues 1-30 ##label STO !'##experimental_source NCIB 8924 COMMENT The active enzyme is composed of 12 chains of two different !1but homologous types, alpha and beta, which can combine in !1various ratios. CLASSIFICATION #superfamily thermophilic aminopeptidase I alpha chain KEYWORDS aminopeptidase SUMMARY #length 30 #checksum 4936 SEQUENCE /// ENTRY S29848 #type complete TITLE membrane dipeptidase (EC 3.4.13.19) precursor - human ALTERNATE_NAMES dehydropeptidase-I; renal dipeptidase ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jan-2000 ACCESSIONS S29848; JS0756; A35467; JS0757; S08193; PX0021 REFERENCE S29848 !$#authors Satoh, S.; Kusunoki, C.; Konta, Y.; Niwa, M.; Kohsaka, M. !$#journal Biochim. Biophys. Acta (1993) 1172:181-183 !$#title Cloning and structural analysis of genomic DNA for human !1renal dipeptidase. !$#cross-references MUID:93176806; PMID:8439558 !$#accession S29848 !'##molecule_type DNA !'##residues 1-411 ##label SAT !'##cross-references DDBJ:D13136; NID:g219597; DDBJ:D13137; NID:g219598; !1PIDN:BAA02430.1; PID:g219600 !'##note the authors translated the codon TCC for residue 9 as Pro REFERENCE JS0756 !$#authors Satoh, S.; Kusunoki, C.; Konta, Y.; Niwa, M.; Kohsaka, M. !$#submission submitted to JIPID, September 1992 !$#accession JS0756 !'##status translation not shown !'##molecule_type DNA !'##residues 1-411 ##label SA2 !'##cross-references DDBJ:D13128; NID:g219589 REFERENCE A35467 !$#authors Adachi, H.; Tawaragi, Y.; Inuzuka, C.; Kubota, I.; !1Tsujimoto, M.; Nishihara, T.; Nakazato, H. !$#journal J. Biol. Chem. (1990) 265:3992-3995 !$#title Primary structure of human microsomal dipeptidase deduced !1from molecular cloning. !$#cross-references MUID:90154088; PMID:2303490 !$#accession A35467 !'##molecule_type mRNA !'##residues 1-8,'P',10-101,'R',103-124,'R',126-411 ##label ADA !'##cross-references GB:J05257; NID:g598188; PIDN:AAB59410.1; !1PID:g598189 REFERENCE JS0757 !$#authors Satoh, S.; Ohtuka, K.; Kusunoki, C.; Konta, Y.; Keida, Y.; !1Niwa, M.; Kohsaka, M. !$#submission submitted to JIPID, September 1992 !$#accession JS0757 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-8,'P',10-144,'P',146-174,'S',176-411 ##label SA3 !'##cross-references DDBJ:D13138; NID:g219584; PIDN:BAA02431.1; !1PID:g219585 REFERENCE S08193 !$#authors Hooper, N.M.; Keen, J.N.; Turner, A.J. !$#journal Biochem. J. (1990) 265:429-433 !$#title Characterization of the !1glycosyl-phosphatidylinositol-anchored human renal !1dipeptidase reveals that it is more extensively glycosylated !1than the pig enzyme. !$#cross-references MUID:90147607; PMID:2137335 !$#accession S08193 !'##molecule_type protein !'##residues 17-35,'X',37-39 ##label HOO !'##experimental_source kidney REFERENCE PX0021 !$#authors Adachi, H.; Kubota, I.; Okamura, N.; Iwata, H.; Tsujimoto, !1M.; Nakazato, H.; Nishihara, T.; Noguchi, T. !$#journal J. Biochem. (1989) 105:957-961 !$#title Purification and characterization of human microsomal !1dipeptidase. !$#cross-references MUID:89359222; PMID:2768222 !$#accession PX0021 !'##molecule_type protein !'##residues 17-35,'G' ##label AD2 !'##experimental_source kidney REFERENCE A58391 !$#authors Adachi, H.; Katayama, T.; Nakazato, H.; Tsujimoto, M. !$#journal Biochim. Biophys. Acta (1993) 1163:42-48 !$#title Importance of Glu-125 in the catalytic activity of human !1renal dipeptidase. !$#cross-references MUID:93237320; PMID:8097406 !$#contents annotation; active site by labeling and mutagenesis GENETICS !$#gene GDB:DPEP1 !'##cross-references GDB:128059; OMIM:179780 !$#map_position 16q24-16q24 !$#introns 35/2; 79/3; 124/1; 174/2; 197/3; 256/3; 285/1; 310/2; 355/3 COMPLEX homodimer, disulfide linked FUNCTION !$#description hydrolyzes a broad range of dipeptides; hydolyzes !1leukotriene D4 to leukotriene E4 and glycine !$#note has been implicated in the renal metabolism of glutathione !1conjugates CLASSIFICATION #superfamily membrane dipeptidase KEYWORDS blocked carboxyl end; dipeptide hydrolase; glycoprotein; !1homodimer; kidney; lipoprotein; membrane protein; !1phosphatidylinositol linkage; phosphoprotein; zinc FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-384 #product membrane dipeptidase #status predicted !8#label MAT\ !$385-411 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$57,279,332,358 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$141 #active_site Glu #status predicted\ !$235,286,289 #binding_site zinc (His) #status predicted\ !$384 #modified_site GPI-anchor ethanolamine amidated !8carboxyl end (Ser) (in mature form) #status predicted SUMMARY #length 411 #molecular-weight 45663 #checksum 3494 SEQUENCE /// ENTRY JS0759 #type complete TITLE membrane dipeptidase (EC 3.4.13.19) precursor - pig ALTERNATE_NAMES renal dipeptidase ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jan-2000 ACCESSIONS JS0759; PS0394; S13059; S08194 REFERENCE JS0759 !$#authors Satoh, S.; Koyama, S.; Ohtuka, K.; Keida, Y.; Niwa, M.; !1Kohsaka, M. !$#submission submitted to JIPID, September 1992 !$#accession JS0759 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-409 ##label SAT !'##cross-references DDBJ:D13142; NID:g217704; PIDN:BAA02433.1; !1PID:g217705 !'##experimental_source kidney !$#accession PS0394 !'##status translation not shown !'##molecule_type mRNA !'##residues 75-129,'Q',131-312,'L',314-409 ##label SA2 !'##cross-references DDBJ:D13143; NID:g217703 !'##experimental_source kidney REFERENCE S13059 !$#authors Rached, E.; Hooper, N.M.; James, P.; Semenza, G.; Turner, !1A.J.; Mantei, N. !$#journal Biochem. J. (1990) 271:755-760 !$#title cDNA cloning and expression in Xenopus laevis oocytes of pig !1renal dipeptidase, a glycosyl-phosphatidylinositol-anchored !1ectoenzyme. !$#cross-references MUID:91058511; PMID:2173907 !$#accession S13059 !'##molecule_type mRNA !'##residues 1-409 ##label RAC !'##cross-references EMBL:X53730; NID:g2101; PIDN:CAA37762.1; PID:g2102 !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing !'##note the authors refer to the old number EC 3.4.13.11 REFERENCE S08193 !$#authors Hooper, N.M.; Keen, J.N.; Turner, A.J. !$#journal Biochem. J. (1990) 265:429-433 !$#title Characterization of the !1glycosyl-phosphatidylinositol-anchored human renal !1dipeptidase reveals that it is more extensively glycosylated !1than the pig enzyme. !$#cross-references MUID:90147607; PMID:2137335 !$#accession S08194 !'##molecule_type protein !'##residues 17-39 ##label HOO COMPLEX homodimer, disulfide linked FUNCTION !$#description hydrolyzes a broad range of dipeptides; hydolyzes !1leukotriene D4 to leukotriene E4 and glycine !$#note has been implicated in the renal metabolism of glutathione !1conjugates CLASSIFICATION #superfamily membrane dipeptidase KEYWORDS blocked carboxyl end; dipeptide hydrolase; glycoprotein; !1homodimer; kidney; lipoprotein; membrane protein; !1phosphatidylinositol linkage; phosphoprotein; zinc FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-384 #product membrane dipeptidase #status predicted !8#label MAT\ !$385-409 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$57 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$235,286,289 #binding_site zinc (His) #status predicted\ !$279 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$384 #modified_site GPI-anchor ethanolamine amidated !8carboxyl end (Ser) (in mature form) #status predicted SUMMARY #length 409 #molecular-weight 44699 #checksum 306 SEQUENCE /// ENTRY S18442 #type complete TITLE membrane dipeptidase (EC 3.4.13.19) precursor - rabbit ALTERNATE_NAMES renal dipeptidase ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jan-2000 ACCESSIONS S18442; S37681 REFERENCE S18442 !$#authors Igarashi, P.; Karniski, L.P. !$#journal Biochem. J. (1991) 280:71-78 !$#title Cloning of cDNAs encoding a rabbit renal brush border !1membrane protein immunologically related to band 3. Sequence !1similarity with microsomal dipeptidase. !$#cross-references MUID:92074997; PMID:1741759 !$#accession S18442 !'##molecule_type mRNA !'##residues 1-410 ##label IGA1 !'##cross-references EMBL:X61503; NID:g1423; PIDN:CAA43720.1; PID:g1424 !$#accession S37681 !'##molecule_type protein !'##residues 18-27;29-35;37-40 ##label IGA2 COMPLEX homodimer, disulfide linked FUNCTION !$#description hydrolyzes a broad range of dipeptides; hydolyzes !1leukotriene D4 to leukotriene E4 and glycine !$#note has been implicated in the renal metabolism of glutathione !1conjugates CLASSIFICATION #superfamily membrane dipeptidase KEYWORDS blocked carboxyl end; dipeptide hydrolase; glycoprotein; !1homodimer; kidney; lipoprotein; membrane protein; !1phosphatidylinositol linkage; phosphoprotein; zinc FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-384 #product membrane dipeptidase #status predicted !8#label MAT\ !$385-410 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$57 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$235,286 #binding_site zinc (His) #status predicted\ !$384 #modified_site GPI-anchor ethanolamine amidated !8carboxyl end (Ser) (in mature form) #status predicted SUMMARY #length 410 #molecular-weight 45304 #checksum 3676 SEQUENCE /// ENTRY S33757 #type complete TITLE membrane dipeptidase (EC 3.4.13.19) precursor - mouse ALTERNATE_NAMES renal dipeptidase ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jan-2000 ACCESSIONS S33757; S34781; JS0758 REFERENCE S33757 !$#authors Satoh, S.; Keida, Y.; Konta, Y.; Maeda, M.; Matsumoto, Y.; !1Niwa, M.; Kohsaka, M. !$#journal Biochim. Biophys. Acta (1993) 1163:234-242 !$#title Purification and molecular cloning of mouse renal !1dipeptidase. !$#cross-references MUID:93283418; PMID:8507661 !$#accession S33757 !'##molecule_type mRNA !'##residues 1-410 ##label SAT1 !'##cross-references EMBL:D13139; NID:g220397; PIDN:BAA02432.1; !1PID:g220398 !$#accession S34781 !'##molecule_type protein !'##residues 17-36;73-80;198-212;222-232 ##label SAT2 REFERENCE JS0758 !$#authors Satoh, S.; Keida, Y.; Konta, Y.; Maeda, M.; Niwa, M.; !1Kohsaka, M. !$#submission submitted to JIPID, September 1992 !$#accession JS0758 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-203,'T',205-410 ##label SAT3 !'##cross-references DDBJ:D13139; NID:g220397; PIDN:BAA02432.1; !1PID:g220398 COMPLEX homodimer, disulfide linked FUNCTION !$#description hydrolyzes a broad range of dipeptides; hydolyzes !1leukotriene D4 to leukotriene E4 and glycine !$#note has been implicated in the renal metabolism of glutathione !1conjugates CLASSIFICATION #superfamily membrane dipeptidase KEYWORDS blocked carboxyl end; dipeptide hydrolase; glycoprotein; !1homodimer; kidney; lipoprotein; membrane protein; !1phosphatidylinositol linkage; phosphoprotein; zinc FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-384 #product membrane dipeptidase #status predicted !8#label MAT\ !$385-410 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$121,258,332 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$235,286,289 #binding_site zinc (His) #status predicted\ !$384 #modified_site GPI-anchor ethanolamine amidated !8carboxyl end (Ser) (in mature form) #status predicted SUMMARY #length 410 #molecular-weight 45695 #checksum 2879 SEQUENCE /// ENTRY S27204 #type complete TITLE membrane dipeptidase (EC 3.4.13.19) precursor - rat ALTERNATE_NAMES renal dipeptidase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jan-2000 ACCESSIONS S27204 REFERENCE S27204 !$#authors Adachi, H.; Ishida, N.; Tsujimoto, M. !$#journal Biochim. Biophys. Acta (1992) 1132:311-314 !$#title Primary structure of rat renal dipeptidase and expression of !1its mRNA in rat tissues and COS-1 cells. !$#cross-references MUID:93041934; PMID:1420313 !$#accession S27204 !'##molecule_type mRNA !'##residues 1-410 ##label ADA !'##cross-references EMBL:M94056; NID:g203969; PIDN:AAA41093.1; !1PID:g203970 COMPLEX homodimer, disulfide linked FUNCTION !$#description hydrolyzes a broad range of dipeptides; hydolyzes !1leukotriene D4 to leukotriene E4 and glycine !$#note has been implicated in the renal metabolism of glutathione !1conjugates CLASSIFICATION #superfamily membrane dipeptidase KEYWORDS blocked carboxyl end; dipeptide hydrolase; glycoprotein; !1homodimer; kidney; lipoprotein; membrane protein; !1phosphatidylinositol linkage; phosphoprotein; zinc FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-384 #product membrane dipeptidase #status predicted !8#label MAT\ !$385-410 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$57,121,332 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$235,286,289 #binding_site zinc (His) #status predicted\ !$384 #modified_site GPI-anchor ethanolamine amidated !8carboxyl end (Ser) (in mature form) #status predicted SUMMARY #length 410 #molecular-weight 45506 #checksum 2511 SEQUENCE /// ENTRY JC4222 #type complete TITLE membrane dipeptidase (EC 3.4.13.19) homolog - Acinetobacter calcoaceticus ORGANISM #formal_name Acinetobacter calcoaceticus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JC4222 REFERENCE JC4222 !$#authors Adachi, H.; Tsujimoto, M. !$#journal J. Biochem. (1995) 118:555-561 !$#title Cloning and expression of dipeptidase from Acinetobacter !1calcoaceticus ATCC 23055. !$#cross-references MUID:96115926; PMID:8690717 !$#accession JC4222 !'##molecule_type DNA !'##residues 1-350 ##label ADA !'##cross-references DDBJ:D50330; NID:g1088398; PIDN:BAA08867.1; !1PID:g1088400 !'##experimental_source ATCC 23055 COMMENT This enzyme is a zinc-containing ectoenzyme. GENETICS !$#gene acdp FUNCTION !$#description hydrolyzes a broad range of dipeptides !$#note cannot hydrolyze the unsaturated dipeptide !1N-glycyl-dehydrophenylalanine CLASSIFICATION #superfamily membrane dipeptidase KEYWORDS dipeptide hydrolase; glycoprotein FEATURE !$132,226 #active_site Glu, His #status predicted SUMMARY #length 350 #molecular-weight 39395 #checksum 2267 SEQUENCE /// ENTRY CDHU26 #type complete TITLE dipeptidyl-peptidase IV (EC 3.4.14.5) - human ALTERNATE_NAMES cell surface glycoprotein CD26; thymocyte-activating molecule (THAM) ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1993 #sequence_revision 23-Aug-1996 #text_change 18-Jun-1999 ACCESSIONS S24313; B42408; A42408; B61136; S59510; I56154; S59857; !1S15520 REFERENCE S24313 !$#authors Misumi, Y.; Hayashi, Y.; Arakawa, F.; Ikehara, Y. !$#journal Biochim. Biophys. Acta (1992) 1131:333-336 !$#title Molecular cloning and sequence analysis of human dipeptidyl !1peptidase IV, a serine proteinase on the cell surface. !$#cross-references MUID:92329551; PMID:1352704 !$#accession S24313 !'##molecule_type mRNA !'##residues 1-6,'I',8-766 ##label MIS !'##cross-references EMBL:X60708; NID:g35335; PIDN:CAA43118.1; !1PID:g35336 REFERENCE A42408 !$#authors Darmoul, D.; Lacasa, M.; Baricault, L.; Marguet, D.; Sapin, !1C.; Trotot, P.; Barbat, A.; Trugnan, G. !$#journal J. Biol. Chem. (1992) 267:4824-4833 !$#title Dipeptidyl peptidase IV (CD 26) gene expression in !1enterocyte-like colon cancer cell lines HT-29 and Caco-2. !1Cloning of the complete human coding sequence and changes of !1dipeptidyl peptidase IV mRNA levels during cell !1differentiation. !$#cross-references MUID:92165847; PMID:1347043 !$#accession B42408 !'##molecule_type mRNA !'##residues 1-5,'R',7-436,'S',438-556,'I',558-662,'E',664-766 ##label !1DAR1 !'##cross-references GB:M80536; NID:g181569; PIDN:AAA52308.1; !1PID:g181570 !'##experimental_source intestine !'##note this sequence corresponds with the author's translation !$#accession A42408 !'##molecule_type mRNA !'##residues 1-5,'R',7-436,'S',438-556,'I',558-662,'E',664-711,'G', !1713-766 ##label DAR2 !'##cross-references GB:M80536; NID:g181569 !'##note sequence extracted from NCBI backbone (NCBIN:83986, !1NCBIP:83988); this sequence is inconsistent with the !1nucleotide translation REFERENCE A61136 !$#authors Gorvel, J.P.; Ferrero, A.; Chambraud, L.; Rigal, A.; !1Bonicel, J.; Maroux, S. !$#journal Gastroenterology (1991) 101:618-625 !$#title Expression of sucrase-isomaltase and dipeptidylpeptidase IV !1in human small intestine and colon. !$#cross-references MUID:91317403; PMID:1677636 !$#accession B61136 !'##molecule_type protein !'##residues 1-15,'X',17-22 ##label GOR REFERENCE S59510 !$#authors Boehm, S.K.; Gum Jr., J.R.; Erickson, R.H.; Hicks, J.W.; !1Kim, Y.S. !$#journal Biochem. J. (1995) 311:835-843 !$#title Human dipeptidyl peptidase IV gene promoter: tissue-specific !1regulation from a TATA-less GC-rich sequence characteristic !1of a housekeeping gene promoter. !$#cross-references MUID:96067599; PMID:7487939 !$#accession S59510 !'##molecule_type DNA !'##residues 1-31 ##label BOE !'##cross-references GB:S79876; NID:g1195574; PIDN:AAB35614.1; !1PID:g1195575 REFERENCE I56154 !$#authors Tanaka, T.; Camerini, D.; Seed, B.; Torimoto, Y.; Dang, !1N.H.; Kameoka, J.; Dahlberg, H.N.; Schlossman, S.F.; !1Morimoto, C. !$#journal J. Immunol. (1992) 149:481-486 !$#title Cloning and functional expression of the T cell activation !1antigen CD26. !$#cross-references MUID:92325476; PMID:1352530 !$#accession I56154 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-436,'S',438-766 ##label TAN !'##cross-references GB:M74777; NID:g180082; PIDN:AAA51943.1; !1PID:g180083 REFERENCE S59857 !$#authors Abbott, C.A.; Baker, E.; Sutherland, G.R.; McCaughan, G.W. !$#journal Immunogenetics (1994) 40:331-338 !$#title Genomic organization, exact localization, and tissue !1expression of the human CD26 (dipeptidyl peptidase IV) gene. !$#cross-references MUID:95012454; PMID:7927537 !$#accession S59857 !'##molecule_type DNA !'##residues 1-436,'S',438-766 ##label ABB !'##cross-references EMBL:U13734 GENETICS !$#gene GDB:DPP4 !'##cross-references GDB:125239; OMIM:102720 !$#map_position 2q24.3-2q24.3 !$#introns 2/3; 32/1; 65/1; 95/3; 122/3; 140/2; 164/3; 205/1; 258/3; !1296/2; 341/3; 356/3; 392/3; 415/2; 433/2; 474/1; 490/1; 523/ !11; 546/2; 611/2; 629/3; 663/1; 684/3; 709/1; 733/3 CLASSIFICATION #superfamily dipeptidyl-peptidase IV KEYWORDS dipeptidylpeptide hydrolase; glycoprotein; homodimer; !1proteinase; transmembrane protein FEATURE !$1-6 #domain intracellular #status predicted #label INT\ !$7-28 #domain transmembrane #status predicted #label TMN\ !$29-766 #domain extracellular #status predicted #label EXT\ !$85,92,150,219,229, !$281,321,520,685 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$630,708,740 #active_site Ser, Asp, His #status predicted SUMMARY #length 766 #molecular-weight 88304 #checksum 2597 SEQUENCE /// ENTRY S23752 #type complete TITLE dipeptidyl-peptidase IV (EC 3.4.14.5) alpha chain - mouse ALTERNATE_NAMES CD26 alpha subunit; THAM alpha subunit ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S23752; A46465; A56030 REFERENCE S23752 !$#authors Marguet, D.; Bernard, A.M.; Vivier, I.; Darmoul, D.; Naquet, !1P.; Pierres, M. !$#journal J. Biol. Chem. (1992) 267:2200-2208 !$#title cDNA cloning for mouse thymocyte-activating molecule. A !1multifunctional ecto-dipeptidyl peptidase IV (CD26) included !1in a subgroup of serine proteases. !$#cross-references MUID:92129288; PMID:1370813 !$#accession S23752 !'##status preliminary !'##molecule_type mRNA !'##residues 1-760 ##label MAR !'##cross-references EMBL:X58384 REFERENCE A46465 !$#authors Vivier, I.; Marguet, D.; Naquet, P.; Bonicel, J.; Black, D.; !1Li, C.X.; Bernard, A.M.; Gorvel, J.P.; Pierres, M. !$#journal J. Immunol. (1991) 147:447-454 !$#title Evidence that thymocyte-activating molecule is mouse CD26 !1(dipeptidyl peptidase IV). !$#cross-references MUID:91302787; PMID:1712807 !$#accession A46465 !'##status preliminary !'##molecule_type protein !'##residues 1-20 ##label VIV !'##experimental_source M14.T thymoma cells, Swiss nu/nu !'##note sequence extracted from NCBI backbone (NCBIP:42236) REFERENCE A56030 !$#authors Bernard, A.M.; Mattei, M.G.; Pierres, M.; Marguet, D. !$#journal Biochemistry (1994) 33:15204-15214 !$#title Structure of the mouse dipeptidyl peptidase IV (CD26) gene. !$#cross-references MUID:95092780; PMID:7999781 !$#accession A56030 !'##status preliminary !'##molecule_type DNA !'##residues 746-760 ##label BER !'##cross-references GB:U12620 GENETICS !$#gene CD26 CLASSIFICATION #superfamily dipeptidyl-peptidase IV KEYWORDS dipeptidylpeptide hydrolase; glycoprotein; transmembrane !1protein FEATURE !$213,223,315,514,679 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$624,702,734 #active_site Ser, Asp, His #status predicted SUMMARY #length 760 #molecular-weight 87464 #checksum 8783 SEQUENCE /// ENTRY A39914 #type complete TITLE dipeptidyl-peptidase IV (EC 3.4.14.5), membrane-bound form precursor - rat ALTERNATE_NAMES GP110; membrane glycoprotein 110K; OX-61 CONTAINS dipeptidyl-peptidase IV, soluble form ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A39914; A33315; B33315; A60730; A42203; S38949; A31781 REFERENCE A39914 !$#authors Hong, W.; Doyle, D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:7962-7966 !$#title cDNA cloning for a bile canaliculus domain-specific membrane !1glycoprotein of rat hepatocytes. !$#cross-references MUID:88068516; PMID:3479775 !$#accession A39914 !'##molecule_type mRNA !'##residues 1-792 ##label HON !'##cross-references GB:J02997; NID:g204463; PIDN:AAA41272.1; !1PID:g204464 REFERENCE A33315 !$#authors Ogata, S.; Misumi, Y.; Ikehara, Y. !$#journal J. Biol. Chem. (1989) 264:3596-3601 !$#title Primary structure of rat liver dipeptidyl peptidase IV !1deduced from its cDNA and identification of the !1NH-2-terminal signal sequence as the membrane-anchoring !1domain. !$#cross-references MUID:89123496; PMID:2563382 !$#accession A33315 !'##molecule_type mRNA !'##residues 1-37,'A',39-182,'I',184-331,'T',333-351,'C',353-393,'V', !1395-561,'L',563-623,'R',625-766,'R' ##label OGA !'##cross-references GB:J04591; NID:g203973; PIDN:AAA41096.1; !1PID:g203974 !'##note the authors translated the codon GCG for residue 38 as Arg, ACC !1for residue 332 as Asn, TGC for residue 352 as Val, CAG for !1residue 384 as Glu, and CAA for residue 607 as Glu !$#accession B33315 !'##molecule_type protein !'##residues !11-20;35-54;427-443;505-509;511-520;530-538;593-600;602-608; !1618-627 ##label HO2 REFERENCE A60730 !$#authors McCaughan, G.W.; Wickson, J.E.; Creswick, P.F.; Gorrell, !1M.D. !$#journal Hepatology (1990) 11:534-544 !$#title Identification of the bile canalicular cell surface molecule !1GP110 as the ectopeptidase dipeptidyl peptidase IV: an !1analysis by tissue distribution, purification and N-terminal !1amino acid sequence. !$#cross-references MUID:90228896; PMID:1970322 !$#accession A60730 !'##molecule_type protein !'##residues 28-47,'XX',50-53,55-58 ##label MCC REFERENCE A42203 !$#authors Ogata, S.; Misumi, Y.; Tsuji, E.; Takami, N.; Oda, K.; !1Ikehara, Y. !$#journal Biochemistry (1992) 31:2582-2587 !$#title Identification of the active site residues in dipeptidyl !1peptidase IV by affinity labeling and site-directed !1mutagenesis. !$#cross-references MUID:92190188; PMID:1347701 !$#accession A42203 !'##molecule_type protein !'##residues 'R',625-630,'X',632-648 ##label OG2 REFERENCE S38949 !$#authors Iwaki-Egawa, S.; Watanabe, Y.; Fujimoto, Y. !$#journal Biol. Chem. Hoppe-Seyler (1993) 374:973-975 !$#title N-terminal amino acid sequence of the 60-kDa protein of rat !1kidney dipeptidyl peptidase IV. !$#cross-references MUID:94128239; PMID:7905271 !$#accession S38949 !'##status preliminary !'##molecule_type protein !'##residues 281-302 ##label IWA REFERENCE A31781 !$#authors Hong, W.; Doyle, D. !$#journal J. Biol. Chem. (1988) 263:16892-16898 !$#title Membrane orientation of rat gp110 as studied by in vitro !1translation. !$#cross-references MUID:89034185; PMID:3182821 !$#accession A31781 !'##molecule_type mRNA !'##residues 1-40 ##label HO3 COMMENT This protein is localized to the bile canaliculus, which is !1the apical domain of the hepatocyte. CLASSIFICATION #superfamily dipeptidyl-peptidase IV KEYWORDS dipeptidylpeptide hydrolase; glycoprotein; homodimer; liver; !1serine proteinase; transmembrane protein FEATURE !$1-792 #product dipeptidyl-peptidase, membrane-bound form !8#status experimental #label MATM\ !$1-28 #domain signal sequence #link MATS #status !8experimental #label SIG\ !$1-6 #domain intracellular #status predicted #label INT\ !$7-28 #domain transmembrane #status predicted #label TMN\ !$29-792 #domain extracellular #status predicted #label EXT\ !$29-34 #domain propeptide #link MATS #status experimental !8#label PRO\ !$35-792 #product dipeptidyl-peptidase, soluble form #status !8experimental #label MATS\ !$83,90,148,217,227, !$319,521,686 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$631 #active_site Ser #status experimental\ !$709,741 #active_site Asp, His #status predicted SUMMARY #length 792 #molecular-weight 90926 #checksum 3787 SEQUENCE /// ENTRY A30107 #type complete TITLE dipeptidyl aminopeptidase B (EC 3.4.14.-) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YHR028c ORGANISM #formal_name Saccharomyces cerevisiae DATE 07-Jun-1990 #sequence_revision 30-May-1997 #text_change 23-Mar-2001 ACCESSIONS S46780; A30107 REFERENCE S46773 !$#authors Du, Z. !$#submission submitted to the EMBL Data Library, June 1994 !$#description The sequence of S. cerevisiae cosmid 8082. !$#accession S46780 !'##molecule_type DNA !'##residues 1-818 ##label DUZ !'##cross-references EMBL:U10399; NID:g500689; PIDN:AAB68879.1; !1PID:g500698; GSPDB:GN00008; MIPS:YHR028c REFERENCE A30107 !$#authors Roberts, C.J.; Pohlig, G.; Rothman, J.H.; Stevens, T.H. !$#journal J. Cell Biol. (1989) 108:1363-1373 !$#title Structure, biosynthesis, and localization of dipeptidyl !1aminopeptidase B, an integral membrane glycoprotein of the !1yeast vacuole. !$#cross-references MUID:89174971; PMID:2647766 !$#accession A30107 !'##molecule_type DNA !'##residues 1-82,'H',84-124,'N',126-181,'LRRLET',189-199,'N',201-365, !1'DFKRGKERKF',376-571,'T',573-807,'QSVLSM',814, !1'NLTNELTIYSSSHRDIHKTFSYLHTMYI' ##label ROB !'##cross-references EMBL:X15484 !'##note the authors translated the codon ACC for residue 572 as Asn GENETICS !$#gene SGD:DAP2; STE13; MIPS:YHR028c !'##cross-references SGD:S0001070; MIPS:YHR028c !$#map_position 8R CLASSIFICATION #superfamily dipeptidyl-peptidase IV KEYWORDS dipeptidylpeptide hydrolase; glycoprotein; transmembrane !1protein; yeast vacuole FEATURE !$30-45 #domain transmembrane #status predicted #label TMM\ !$63,79,110,139,392, !$421 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 818 #molecular-weight 93404 #checksum 2391 SEQUENCE /// ENTRY A31759 #type complete TITLE peptidyl-dipeptidase A (EC 3.4.15.1) precursor, renal and pulmonary splice form - human ALTERNATE_NAMES angiotensin I-converting enzyme (ACE); CD143; dipeptidyl carboxypeptidase I; peptidyl-dipeptidase I, pulmonary ORGANISM #formal_name Homo sapiens #common_name man DATE 07-Jun-1990 #sequence_revision 02-Jul-1998 #text_change 18-Jun-1999 ACCESSIONS A31759; PQ0004 REFERENCE A31759 !$#authors Soubrier, F.; Alhenc-Gelas, F.; Hubert, C.; Allegrini, J.; !1John, M.; Tregear, G.; Corvol, P. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:9386-9390 !$#title Two putative active centers in human angiotensin !1I-converting enzyme revealed by molecular cloning. !$#cross-references MUID:89071703; PMID:2849100 !$#accession A31759 !'##molecule_type mRNA !'##residues 1-1306 ##label SOU !'##cross-references GB:J04144; NID:g178285; PIDN:AAA51684.1; !1PID:g178286 !'##experimental_source kidney !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing REFERENCE PQ0004 !$#authors Takeuchi, K.; Shimizu, T.; Ohishi, N.; Seyama, Y.; Takaku, !1F.; Yotsumoto, H. !$#journal J. Biochem. (1989) 106:442-445 !$#title Purification of human lung angiotensin-converting enzyme by !1high-performance liquid chromatography: properties and !1N-terminal amino acid sequence. !$#cross-references MUID:90110025; PMID:2558109 !$#accession PQ0004 !'##molecule_type protein !'##residues 'XX',32-34,'E',36-37,'X',39-41,'R',43-46 ##label TAK !'##experimental_source lung COMMENT This splice form is found in many tissues, in particular !1kidney and lung vascular endothelium. For the testicular !1splice form, see PIR:S05238. GENETICS !$#gene GDB:DCP1; ACE !'##cross-references GDB:119840; OMIM:106180 !$#map_position 17q23-17q23 FUNCTION !$#description catalyzes the hydrolysis of dipeptides from the carboxyl end !1of polypeptides !$#note plays a role in the control of blood pressure by catalyzing !1the conversion of angiotensin I to the more vasoactive !1angiotensin II CLASSIFICATION #superfamily mammalian peptidyl-dipeptidase A KEYWORDS alternative splicing; blood pressure control; glycoprotein; !1kidney; lung; metalloproteinase; peptidyldipeptide !1hydrolase; transmembrane protein; zinc FEATURE !$1-29 #domain signal sequence #status predicted #label SIG\ !$30-1306 #product peptidyl dipeptidase I #status predicted !8#label MAT\ !$1260-1276 #domain transmembrane #status predicted #label TRM\ !$38,54,74,111,146, !$160,318,445,509, !$523,677,695,714, !$760,942,1191,1225 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$390,394 #binding_site zinc (His) #status predicted\ !$988,992,1008 #binding_site zinc, catalytic (His, His, Glu) #status !8predicted\ !$989 #active_site Glu #status predicted SUMMARY #length 1306 #molecular-weight 149714 #checksum 4577 SEQUENCE /// ENTRY S05238 #type complete TITLE peptidyl-dipeptidase A (EC 3.4.15.1) precursor, testicular splice form - human ALTERNATE_NAMES angiotensin I-converting enzyme (ACE); CD143; dipeptidyl carboxypeptidase I; peptidyl-dipeptidase I ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1991 #sequence_revision 02-Jul-1998 #text_change 18-Jun-1999 ACCESSIONS S05238; A33979 REFERENCE S05238 !$#authors Lattion, A.L.; Soubrier, F.; Allegrini, J.; Hubert, C.; !1Corvol, P.; Alhenc-Gelas, F. !$#journal FEBS Lett. (1989) 252:99-104 !$#title The testicular transcript of the angiotensin I-converting !1enzyme encodes for the ancestral, non-duplicated form of the !1enzyme. !$#cross-references MUID:89338720; PMID:2547653 !$#accession S05238 !'##molecule_type mRNA !'##residues 1-732 ##label LAT !'##cross-references EMBL:X16295; NID:g28264; PIDN:CAA34362.1; !1PID:g28265 REFERENCE A33979 !$#authors Ehlers, M.R.W.; Fox, E.A.; Strydom, D.J.; Riordan, J.F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:7741-7745 !$#title Molecular cloning of human testicular angiotensin-converting !1enzyme: the testis isozyme is identical to the C-terminal !1half of endothelial angiotensin-converting enzyme. !$#cross-references MUID:90046671; PMID:2554286 !$#accession A33979 !'##molecule_type mRNA !'##residues 1-732 ##label EHL !'##cross-references GB:M26657; NID:g338666; PIDN:AAA60611.1; !1PID:g338667 !'##experimental_source clones R1.2 and T8B !'##note neither the complete nucleic acid sequence nor the complete !1translation are shown COMMENT For the renal and pulmonary splice form, see PIR:A31759. GENETICS !$#gene GDB:DCP1; ACE !'##cross-references GDB:119840; OMIM:106180 !$#map_position 17q23-17q23 FUNCTION !$#description catalyzes the hydrolysis of dipeptides from the carboxyl end !1of polypeptides CLASSIFICATION #superfamily mammalian peptidyl-dipeptidase A KEYWORDS alternative splicing; glycoprotein; metalloproteinase; !1peptidyldipeptide hydrolase; sperm; testis; transmembrane !1protein; zinc FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-732 #product peptidyl dipeptidase I #status predicted !8#label MAT\ !$686-702 #domain transmembrane #status predicted #label TRM\ !$103,121,140,186, !$368,617,651 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$414,418,434 #binding_site zinc, catalytic (His, His, Glu) #status !8predicted\ !$415 #active_site Glu #status predicted SUMMARY #length 732 #molecular-weight 83330 #checksum 2091 SEQUENCE /// ENTRY A34171 #type complete TITLE peptidyl-dipeptidase A (EC 3.4.15.1) precursor - mouse ALTERNATE_NAMES ACE; angiotensin-converting enzyme; carboxycathepsin; dipeptidyl carboxypeptidase I; kininase II; peptidase P; peptidyl-dipeptidase I ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A34171; A29220; A61477 REFERENCE A34171 !$#authors Bernstein, K.E.; Martin, B.M.; Edwards, A.S.; Bernstein, !1E.A. !$#journal J. Biol. Chem. (1989) 264:11945-11951 !$#title Mouse angiotensin-converting enzyme is a protein composed of !1two homologous domains. !$#cross-references MUID:89308599; PMID:2545691 !$#accession A34171 !'##molecule_type mRNA !'##residues 1-1312 ##label BER !'##cross-references GB:J04947 REFERENCE A29220 !$#authors Bernstein, K.E.; Martin, B.M.; Bernstein, E.A.; Linton, J.; !1Striker, L.; Striker, G. !$#journal J. Biol. Chem. (1988) 263:11021-11024 !$#title The isolation of angiotensin-converting enzyme cDNA. !$#cross-references MUID:88298730; PMID:2841312 !$#accession A29220 !'##molecule_type mRNA !'##residues 1-332 ##label BE2 !'##cross-references GB:J03940; NID:g191583; PIDN:AAA37146.1; !1PID:g191584 REFERENCE A61477 !$#authors Bernstein, K.E.; Martin, B.M.; Striker, L.; Striker, G. !$#journal Kidney Int. (1988) 33:652-655 !$#title Partial protein sequence of mouse and bovine kidney !1angiotensin converting enzyme. !$#cross-references MUID:88215372; PMID:2835538 !$#accession A61477 !'##status preliminary !'##molecule_type protein !'##residues 35-54 ##label BE3 !'##experimental_source kidney CLASSIFICATION #superfamily mammalian peptidyl-dipeptidase A KEYWORDS alternative splicing; blood pressure control; membrane !1protein; peptidyldipeptide hydrolase; zinc FEATURE !$1-34 #domain signal sequence #status predicted #label SIG\ !$35-1312 #product peptidyl dipeptidase I #status predicted !8#label MAT SUMMARY #length 1312 #molecular-weight 150947 #checksum 9686 SEQUENCE /// ENTRY A35655 #type complete TITLE peptidyl-dipeptidase A (EC 3.4.15.1), testis - mouse ALTERNATE_NAMES peptidyl-dipeptidase I, testis ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A35655 REFERENCE A35655 !$#authors Howard, T.E.; Shai, S.Y.; Langford, K.G.; Martin, B.M.; !1Bernstein, K.E. !$#journal Mol. Cell. Biol. (1990) 10:4294-4302 !$#title Transcription of testicular angiotensin-converting enzyme !1(ACE) is initiated within the 12th intron of the somatic ACE !1gene. !$#cross-references MUID:90318396; PMID:2164636 !$#accession A35655 !'##status preliminary !'##molecule_type mRNA !'##residues 1-732 ##label HOW !'##cross-references GB:M55333; NID:g191589; PIDN:AAA37149.1; !1PID:g191590 CLASSIFICATION #superfamily mammalian peptidyl-dipeptidase A KEYWORDS alternative splicing; peptidyldipeptide hydrolase; !1transmembrane protein; zinc SUMMARY #length 732 #molecular-weight 84047 #checksum 9135 SEQUENCE /// ENTRY JC2038 #type complete TITLE peptidyl-dipeptidase A (EC 3.4.15.1) - rat ALTERNATE_NAMES angiotensin converting enzyme; kininase II ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JC2038 REFERENCE JC2038 !$#authors Koike, G.; Krieger, J.E.; Jacob, H.J.; Mukoyama, M.; Pratt, !1R.E.; Dzau, V.J. !$#journal Biochem. Biophys. Res. Commun. (1994) 198:380-386 !$#title Angiotensin converting enzyme and genetic hypertension: !1Cloning of rat cDNAs and characterization of the enzyme. !$#cross-references MUID:94121658; PMID:8292044 !$#accession JC2038 !'##molecule_type mRNA !'##residues 1-1313 ##label KOI !'##cross-references GB:U03734; NID:g437289; PIDN:AAA82111.1; !1PID:g437290 !'##note the authors translated the codon ACC for residue 159 as Tyr COMMENT This enzyme is a zinc-containg dicarboxy peptidase that !1cleaves angiotensin I to form the vasoconstrictor !1angiotensin II and degrades the vasodilt bradykinin. COMMENT This enzyme plays a critical role in blood pressure !1homeostasis and is the target of an important class of !1anti-hypertensive agents. CLASSIFICATION #superfamily mammalian peptidyl-dipeptidase A KEYWORDS alternative splicing; peptidyldipeptide hydrolase; !1transmembrane protein; zinc FEATURE !$393-400,990-998 #region catalytic #status predicted\ !$1264-1284 #domain transmembrane #status predicted #label TMM SUMMARY #length 1313 #molecular-weight 150879 #checksum 8607 SEQUENCE /// ENTRY A34402 #type complete TITLE peptidyl-dipeptidase A (EC 3.4.15.1) precursor, testicular - rabbit ALTERNATE_NAMES angiotensin I-converting enzyme; dipeptidyl carboxypeptidase I; peptidyl-dipeptidase I, testicular; peptidyldipeptide hydrolase ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A34402; A60724; A36232; C18700 REFERENCE A34402 !$#authors Kumar, R.S.; Kusari, J.; Roy, S.N.; Soffer, R.L.; Sen, G.C. !$#journal J. Biol. Chem. (1989) 264:16754-16758 !$#title Structure of testicular angiotensin-converting enzyme. A !1segmental mosaic isozyme. !$#cross-references MUID:89380303; PMID:2550457 !$#accession A34402 !'##molecule_type mRNA !'##residues 1-737 ##label KUM !'##cross-references GB:J05041; NID:g164744; PIDN:AAA31153.1; !1PID:g164745 REFERENCE A60724 !$#authors Sen, G.C.; Thekkumkara, T.J.; Kumar, R.S. !$#journal J. Cardiovasc. Pharmacol. (1990) 16(Suppl.4):S14-S18 !$#title Angiotensin-coverting enzyme: structural relationship of the !1testicular and the pulmonary forms. !$#cross-references MUID:91155372; PMID:1705622 !$#accession A60724 !'##status translation not shown !'##molecule_type mRNA !'##residues 73-173 ##label SEN !'##note identical sequences were obtained for mRNAs from lung and !1testes REFERENCE A36232 !$#authors Chen, Y.N.P.; Riordan, J.F. !$#journal Biochemistry (1990) 29:10493-10498 !$#title Identification of essential tyrosine and lysine residues in !1angiotensin converting enzyme: evidence for a single active !1site. !$#cross-references MUID:91104959; PMID:2176870 !$#accession A36232 !'##molecule_type protein !'##residues 154-160;236-242 ##label CHE REFERENCE A90107 !$#authors Iwata, K.; Lai, C.Y.; El-Dorry, H.A.; Soffer, R.L. !$#journal Biochem. Biophys. Res. Commun. (1982) 107:1097-1103 !$#title The NH2-and COOH-terminal sequences of the !1angiotensin-converting enzyme isozymes from rabbit lung and !1testis. !$#cross-references MUID:83048249; PMID:6291514 !$#accession C18700 !'##molecule_type protein !'##residues 33-35,'SN',38-39,'SS';'FAEL',737 ##label IWA !'##note several of the amino acids in reported are tentative COMMENT The pulmonary and testicular isoforms of this enzyme differ !1substantially in both human and rat. The identity of regions !1from this testicular isoform to domains in the pulmonary !1isoform suggests that the two isoforms arise by alternative !1splicing of one gene. CLASSIFICATION #superfamily mammalian peptidyl-dipeptidase A KEYWORDS alternative splicing; peptidyldipeptide hydrolase; testis; !1transmembrane protein; zinc SUMMARY #length 737 #molecular-weight 83923 #checksum 9979 SEQUENCE /// ENTRY S35484 #type complete TITLE peptidyl-dipeptidase A (EC 3.4.15.1) precursor, pulmonary splice form - rabbit ALTERNATE_NAMES angiotensin-converting enzyme; dipeptidyl carboxypeptidase I; kininase II; peptidyl-dipeptidase I, pulmonary; peptidyldipeptide hydrolase ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S35484; A23455; A18700; A38655; A49726; S17509 REFERENCE S35484 !$#authors Thekkumkara, T.J.; Livingston III, W.; Kumar, R.S.; Sen, !1G.C. !$#journal Nucleic Acids Res. (1992) 20:683-687 !$#title Use of alternative polyadenylation sites for tissue-specific !1transcription of two angiotensin-converting enzyme mRNAs. !$#cross-references MUID:92178960; PMID:1311831 !$#accession S35484 !'##molecule_type mRNA !'##residues 1-1309 ##label THE !'##cross-references EMBL:X62551 REFERENCE A23455 !$#authors Iwata, K.; Blacher, R.; Soffer, R.L.; Lai, C.Y. !$#journal Arch. Biochem. Biophys. (1983) 227:188-201 !$#cross-references MUID:84051289; PMID:6314908 !$#accession A23455 !'##molecule_type protein !'##residues 34-47,'N',49-55 ##label IWA !'##experimental_source lung REFERENCE A90107 !$#authors Iwata, K.; Lai, C.Y.; El-Dorry, H.A.; Soffer, R.L. !$#journal Biochem. Biophys. Res. Commun. (1982) 107:1097-1103 !$#title The NH2-and COOH-terminal sequences of the !1angiotensin-converting enzyme isozymes from rabbit lung and !1testis. !$#cross-references MUID:83048249; PMID:6291514 !$#accession A18700 !'##molecule_type protein !'##residues 34-44;754-755,'L',757 ##label IW2 REFERENCE A38655 !$#authors Kumar, R.S.; Thekkumkara, T.J.; Sen, G.C. !$#journal J. Biol. Chem. (1991) 266:3854-3862 !$#title The mRNAs encoding the two angiotensin-converting isozymes !1are transcribed from the same gene by a tissue-specific !1choice of alternative transcription initiation sites. !$#cross-references MUID:91139683; PMID:1847388 !$#accession A38655 !'##molecule_type DNA !'##residues 1-88 ##label KUM !'##cross-references GB:M58579 REFERENCE A49726 !$#authors Ramchandran, R.; Sen, G.C.; Misono, K.; Sen, I. !$#journal J. Biol. Chem. (1994) 269:2125-2130 !$#title Regulated cleavage-secretion of the membrane-bound !1angiotensin-converting enzyme. !$#cross-references MUID:94124568; PMID:8294466 !$#accession A49726 !'##status preliminary !'##molecule_type protein !'##residues 1236-1258 ##label RAM !'##experimental_source testis REFERENCE S17509 !$#authors Kirley, T.L. !$#journal Biochem. J. (1991) 278:375-380 !$#title The Mg(2+)-ATPase of rabbit skeletal-muscle transverse !1tubule is a highly glycosylated multiple-subunit enzyme. !$#cross-references MUID:91378880; PMID:1654880 !$#accession S17509 !'##status preliminary !'##molecule_type protein !'##residues 34-55 ##label KIR COMMENT This enzyme converts angiotensin I to angiotensin II in !1presence of divalent cations and chloride ions. The major !1site of this reaction is vascular endothelium, primarily in !1the lung; however, the enzyme has been found also in renal !1tubules and intestinal mucosa. CLASSIFICATION #superfamily mammalian peptidyl-dipeptidase A KEYWORDS alternative splicing; blood pressure control; chloride; !1glycoprotein; intestine; kidney; lung; peptidyldipeptide !1hydrolase; transmembrane protein; zinc FEATURE !$1-33 #domain signal sequence #status predicted #label SIG\ !$34-1309 #product peptidyl-dipeptidase A, pulmonary #status !8experimental #label MAT\ !$59,79,150,322,448, !$512,680,698,717, !$945,1194 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1309 #molecular-weight 149659 #checksum 2123 SEQUENCE /// ENTRY CPBYY #type complete TITLE carboxypeptidase C (EC 3.4.16.5) precursor [validated] - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES carboxypeptidase Y; protein YMR297w ORGANISM #formal_name Saccharomyces cerevisiae DATE 15-Oct-1982 #sequence_revision 31-Mar-1993 #text_change 15-Sep-2000 ACCESSIONS A26597; S47458; A90763; A94609; A00909 REFERENCE A26597 !$#authors Valls, L.A.; Hunter, C.P.; Rothman, J.H.; Stevens, T.H. !$#journal Cell (1987) 48:887-897 !$#title Protein sorting in yeast: the localization determinant of !1yeast vacuolar carboxypeptidase Y resides in the propeptide. !$#cross-references MUID:87131100; PMID:3028649 !$#accession A26597 !'##molecule_type DNA !'##residues 1-532 ##label VAL !'##cross-references EMBL:M15482; NID:g172238; PIDN:AAA34902.1; !1PID:g172239 REFERENCE S47445 !$#authors Barrell, B.G. !$#submission submitted to the EMBL Data Library, August 1994 !$#accession S47458 !'##molecule_type DNA !'##residues 1-532 ##label BAR !'##cross-references EMBL:X80836; NID:g1289327; PIDN:CAA56806.1; !1PID:g530354; GSPDB:GN00013; MIPS:YMR297w REFERENCE A90763 !$#authors Svendsen, I.; Martin, B.M.; Viswanatha, T.; Johansen, J.T. !$#journal Carlsberg Res. Commun. (1982) 47:15-27 !$#title Amino acid sequence of carboxypeptidase Y. II. Peptides from !1enzymatic cleavages. !$#accession A90763 !'##molecule_type protein !'##residues 112-223,'X',225;228-239,'X',241-259,'HG',262-267,'X', !1269-388,'E',390-451,'N',453,'T',455-478,'C',480-528,'D', !1530-532 ##label SVE !'##note this sequence has been revised in reference A94609 REFERENCE A94609 !$#authors Svendsen, I. !$#submission submitted to the Atlas, October 1982 !$#contents disulfide bond !$#accession A94609 !'##molecule_type protein !'##residues 224-227 ##label SV2 !'##note this is a revision to the sequence in reference A90763 REFERENCE A90762 !$#authors Martin, B.M.; Svendsen, I.; Viswanatha, T.; Johansen, J.T. !$#journal Carlsberg Res. Commun. (1982) 47:1-13 !$#title Amino acid sequence of carboxypeptidase Y. Peptides from !1cleavage with cyanogen bromide. !$#contents annotation; experimental details REFERENCE A52472 !$#authors Endrizzi, J.A.; Remington, S.J. !$#submission submitted to the Brookhaven Protein Data Bank, March 1994 !$#cross-references PDB:1YSC !$#contents annotation; X-ray crystallography at 2.8 angstroms; !1disulfide bonds GENETICS !$#gene SGD:PRC1; LBC1; MIPS:YMR297w !'##cross-references SGD:S0004912; MIPS:YMR297w !$#map_position 13R CLASSIFICATION #superfamily serine carboxypeptidase KEYWORDS glycoprotein; hydrolase; serine carboxypeptidase; yeast !1vacuole; zymogen FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-111 #domain propeptide #status predicted #label PRO\ !$112-532 #product carboxypeptidase C #status experimental !8#label MAT\ !$124,198,279 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$167-409,304-318, !$328-351,335-344, !$373-379 #disulfide_bonds #status experimental\ !$257 #active_site Ser #status experimental\ !$449,508 #active_site Asp, His #status predicted SUMMARY #length 532 #molecular-weight 59802 #checksum 8191 SEQUENCE /// ENTRY JC1380 #type complete TITLE carboxypeptidase C (EC 3.4.16.5) precursor - yeast (Candida albicans) ALTERNATE_NAMES carboxypeptidase Y ORGANISM #formal_name Candida albicans DATE 24-Nov-1999 #sequence_revision 24-Nov-1999 #text_change 24-Nov-1999 ACCESSIONS JC1380 REFERENCE JC1380 !$#authors Mukhtar, M.; Logan, D.A.; Kaeufer, N.F. !$#journal Gene (1992) 121:173-177 !$#title The carboxypeptidase Y-encoding gene from Candida albicans !1and its transcription during yeast-to-hyphae conversion. !$#cross-references MUID:93051356; PMID:1427093 !$#accession JC1380 !'##molecule_type DNA !'##residues 1-542 ##label MUK !'##cross-references GB:M95182; NID:g170828; PIDN:AAA34326.1; !1PID:g170829 !'##note the authors translated the codon GAT for residue 42 as Asn, AAA !1for residue 373 as Tyr, AAA for residue 460 as Tyr, and ACA !1for residue 509 as Leu GENETICS !$#gene CPY1 CLASSIFICATION #superfamily serine carboxypeptidase KEYWORDS glycoprotein; hydrolase; serine carboxypeptidase; zymogen FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-127 #domain propeptide #status predicted #label PRO\ !$128-542 #product carboxypeptidase C #status predicted #label !8MAT\ !$213,291 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$269,461,518 #active_site Ser, Asp, His #status predicted\ !$316-330,347-356 #disulfide_bonds #status predicted SUMMARY #length 542 #molecular-weight 61096 #checksum 8878 SEQUENCE /// ENTRY S61713 #type complete TITLE carboxypeptidase C (EC 3.4.16.5) precursor - yeast (Pichia pastoris) ALTERNATE_NAMES carboxypeptidase Y ORGANISM #formal_name Pichia pastoris DATE 24-Nov-1999 #sequence_revision 24-Nov-1999 #text_change 16-Jun-2000 ACCESSIONS S61713 REFERENCE S61713 !$#authors Ohi, H.; Ohtani, W.; Okazaki, N.; Furuhata, N.; Ohmura, T. !$#journal Yeast (1996) 12:31-40 !$#title Cloning and characterization of the Pichia pastoris PRC1 !1gene encoding carboxypeptidase Y. !$#cross-references MUID:96381245; PMID:8789258 !$#accession S61713 !'##molecule_type DNA !'##residues 1-523 ##label OHI !'##cross-references EMBL:X87987; NID:g1171615; PIDN:CAA61240.1; !1PID:g1171616 CLASSIFICATION #superfamily serine carboxypeptidase KEYWORDS glycoprotein; hydrolase; serine carboxypeptidase; zymogen FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-106 #domain propeptide #status predicted #label PRO\ !$107-522 #product carboxypeptidase C #status predicted #label !8MAT\ !$193,271,484,487 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$249,441,498 #active_site Ser, Asp, His #status predicted\ !$296-310,327-336 #disulfide_bonds #status predicted SUMMARY #length 523 #molecular-weight 59447 #checksum 8470 SEQUENCE /// ENTRY S46008 #type complete TITLE probable carboxypeptidase C (EC 3.4.16.5) YBR139w - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein YBR1015; hypothetical protein YBR139w ORGANISM #formal_name Saccharomyces cerevisiae DATE 26-Aug-1994 #sequence_revision 05-Jan-1996 #text_change 19-Apr-2002 ACCESSIONS S46008; S46581 REFERENCE S45995 !$#authors Becam, A.M.; Herbert, C.J.; Nasr, F.; Slonimski, P.P.; !1Zagulski, M. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S46008 !'##molecule_type DNA !'##residues 1-508 ##label BEC !'##cross-references EMBL:Z36008; NID:g536435; PIDN:CAA85097.1; !1PID:g536436; GSPDB:GN00002; MIPS:YBR139w !'##experimental_source strain S288C REFERENCE S46569 !$#authors Becam, A.M.; Cullin, C.; Grzybowska, E.; Lacroute, F.; Nasr, !1F.; Ozier-Kalogeropoulos, O.; Palucha, A.; Slonimski, P.P.; !1Zagulski, M.; Herbert, C.J. !$#journal Yeast (1994) 10(Suppl.A):S1-S11 !$#title The sequence of 29.7kb from the right arm of chromosome II !1reveals 13 complete open reading frames, of which ten !1correspond to new genes. !$#cross-references MUID:94378717; PMID:8091856 !$#accession S46581 !'##molecule_type DNA !'##residues 1-508 ##label BE2 !'##cross-references EMBL:X75891; NID:g496856; PIDN:CAA53497.1; !1PID:g496869 !'##experimental_source strain S288C GENETICS !'##cross-references SGD:S0000343 !$#map_position 2R !$#note MIPS:YBR139w CLASSIFICATION #superfamily serine carboxypeptidase KEYWORDS hydrolase; serine carboxypeptidase; transmembrane protein FEATURE !$6-22 #domain transmembrane #status predicted #label TMM\ !$219,415,474 #active_site Ser, Asp, His #status predicted SUMMARY #length 508 #molecular-weight 57638 #checksum 3955 SEQUENCE /// ENTRY S22530 #type complete TITLE carboxypeptidase C (EC 3.4.16.5) precursor - rice ALTERNATE_NAMES carboxypeptidase III ORGANISM #formal_name Oryza sativa #common_name rice DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 24-Nov-1999 ACCESSIONS S22530 REFERENCE S22530 !$#authors Washio, K.; Ishikawa, K. !$#journal Plant Mol. Biol. (1992) 19:631-640 !$#title Structure and expression during the germination of rice !1seeds of the gene for a carboxypeptidase. !$#cross-references MUID:92329723; PMID:1627776 !$#accession S22530 !'##molecule_type DNA !'##residues 1-500 ##label WAS !'##cross-references EMBL:S40458 GENETICS !$#introns 100/2; 156/3; 196/3; 244/3; 295/1; 324/3; 411/1; 455/3 CLASSIFICATION #superfamily serine carboxypeptidase KEYWORDS glycoprotein; hydrolase; serine carboxypeptidase; zymogen FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-73 #domain propeptide #status predicted #label PRO\ !$74-484 #product carboxypeptidase C #status predicted #label !8MAT\ !$485-499 #domain carboxyl-terminal propeptide #status !8predicted #label CPRO\ !$144 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$216,404,461 #active_site Ser, Asp, His #status predicted SUMMARY #length 500 #molecular-weight 55446 #checksum 6021 SEQUENCE /// ENTRY A29412 #type complete TITLE carboxypeptidase C (EC 3.4.16.5) precursor - wheat ALTERNATE_NAMES carboxypeptidase Y homolog ORGANISM #formal_name Triticum aestivum #common_name common wheat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 24-Nov-1999 ACCESSIONS A29412 REFERENCE A29412 !$#authors Baulcombe, D.C.; Barker, R.F.; Jarvis, M.G. !$#journal J. Biol. Chem. (1987) 262:13726-13735 !$#title A gibberellin responsive wheat gene has homology to yeast !1carboxypeptidase Y. !$#cross-references MUID:88007602; PMID:2820978 !$#accession A29412 !'##molecule_type mRNA !'##residues 1-499 ##label BAU GENETICS !$#introns 100/2; 156/3; 196/3; 244/3; 295/1; 324/3; 411/1; 455/3 CLASSIFICATION #superfamily serine carboxypeptidase KEYWORDS glycoprotein; hydrolase; serine carboxypeptidase; zymogen FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-73 #domain propeptide #status predicted #label PRO\ !$74-484 #product carboxypeptidase C #status predicted #label !8MAT\ !$485-499 #domain carboxyl-terminal propeptide #status !8predicted #label CPRO\ !$144 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$216,404,461 #active_site Ser, Asp, His #status predicted SUMMARY #length 499 #molecular-weight 55220 #checksum 9250 SEQUENCE /// ENTRY A35275 #type complete TITLE carboxypeptidase C (EC 3.4.16.5) - barley ALTERNATE_NAMES carboxypeptidase III ORGANISM #formal_name Hordeum vulgare #common_name barley DATE 24-Nov-1999 #sequence_revision 24-Nov-1999 #text_change 24-Nov-1999 ACCESSIONS A35275 REFERENCE A35275 !$#authors Sorensen, S.B.; Svendsen, I.; Breddam, K. !$#journal Carlsberg Res. Commun. (1989) 54:193-202 !$#title Primary structure of carboxypeptidase III from malted !1barley. !$#cross-references MUID:90315015; PMID:2639682 !$#accession A35275 !'##molecule_type protein !'##residues 1-411 ##label SOR !'##note 185-Val was also found CLASSIFICATION #superfamily serine carboxypeptidase KEYWORDS blocked amino end; glycoprotein; hydrolase; serine !1carboxypeptidase FEATURE !$1 #modified_site blocked amino end (Leu) (probably !8acetylated) #status experimental\ !$71 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$143,331,388 #active_site Ser, Asp, His #status predicted SUMMARY #length 411 #molecular-weight 46216 #checksum 634 SEQUENCE /// ENTRY T03607 #type complete TITLE probable carboxypeptidase C (EC 3.4.16.5) cbp31 - rice ALTERNATE_NAMES serine-type carboxypeptidase homolog ORGANISM #formal_name Oryza sativa #common_name rice DATE 24-Nov-1999 #sequence_revision 24-Nov-1999 #text_change 21-Jul-2000 ACCESSIONS T03607 REFERENCE Z14975 !$#authors Washio, K.; Ishikawa, K. !$#journal Plant Physiol. (1994) 105:1275-1280 !$#title Organ-specific and hormone-dependent expression of genes for !1serine carboxypeptidases during development and folloing !1germination of rice grains. !$#cross-references MUID:95062718; PMID:7972496 !$#accession T03607 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-429 ##label WAS !'##cross-references EMBL:D17587; NID:g409581; PIDN:BAA04511.1; !1PID:g409582 !'##experimental_source cv. Yukihikari GENETICS !$#gene cbp31 CLASSIFICATION #superfamily serine carboxypeptidase KEYWORDS glycoprotein; hydrolase; serine carboxypeptidase FEATURE !$76,414,417 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$148,336,393 #active_site Ser, Asp, His #status predicted SUMMARY #length 429 #molecular-weight 47745 #checksum 9090 SEQUENCE /// ENTRY CPBHS #type complete TITLE carboxypeptidase C (EC 3.4.16.5) precursor - barley ALTERNATE_NAMES serine-type carboxypeptidase I ORGANISM #formal_name Hordeum vulgare #common_name barley DATE 30-Jun-1988 #sequence_revision 24-Nov-1999 #text_change 16-Jun-2000 ACCESSIONS T05367; A29226; A25858; B25858 REFERENCE Z15412 !$#authors Rocher, A.; Lok, F.; Cameron-Mills, V.; von Wettstein, D. !$#submission submitted to the EMBL Data Library, November 1996 !$#description The gene family of serine carboxypeptidases in barley. !$#accession T05367 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-499 ##label ROC !'##cross-references EMBL:Y09603; PIDN:CAA70816.1 !'##experimental_source cv. Himalaya, aleurone REFERENCE A29226 !$#authors Doan, N.P.; Fincher, G.B. !$#journal J. Biol. Chem. (1988) 263:11106-11110 !$#title The A- and B-chains of carboxypeptidase I from germinated !1barley originate from a single precursor polypeptide. !$#cross-references MUID:88298749; PMID:3403516 !$#accession A29226 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 88-499 ##label DOA !'##cross-references GB:J03897; NID:g167011; PIDN:AAA32940.1; !1PID:g167012 REFERENCE A90769 !$#authors Sorensen, S.B.; Breddam, K.; Svendsen, I. !$#journal Carlsberg Res. Commun. (1986) 51:475-485 !$#title Primary structure of carboxypeptidase I from malted barley. !$#accession A25858 !'##molecule_type protein !'##residues 31-101,'P',103-296;352-424,'X',426-499 ##label SOR GENETICS !$#gene Cxp1 COMPLEX homodimer of two mature products, each containing an A and a !1B chain CLASSIFICATION #superfamily serine carboxypeptidase KEYWORDS disulfide bond; glycoprotein; homodimer; hydrolase; serine !1carboxypeptidase; zymogen FEATURE !$1-30 #domain signal sequence #status predicted #label SIG\ !$31-296,352-499 #product carboxypeptidase C #status experimental !8#label MAT\ !$31-296 #domain chain A #status experimental #label CHA\ !$297-351 #domain connecting peptide #status predicted #label !8CNP\ !$352-499 #domain chain B #status experimental #label CHB\ !$148,262,407 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$188,423,476 #active_site Ser, Asp, His #status predicted SUMMARY #length 499 #molecular-weight 54096 #checksum 3632 SEQUENCE /// ENTRY S43516 #type complete TITLE carboxypeptidase C (EC 3.4.16.5) precursor - rice ALTERNATE_NAMES serine-type carboxypeptidase I ORGANISM #formal_name Oryza sativa #common_name rice DATE 24-Nov-1999 #sequence_revision 24-Nov-1999 #text_change 16-Jun-2000 ACCESSIONS S43516 REFERENCE S43516 !$#authors Washio, K.; Ishikawa, K. !$#journal Biochim. Biophys. Acta (1994) 1199:311-314 !$#title Cloning and sequencing of the gene for type I !1carboxypeptidase in rice. !$#cross-references MUID:94213891; PMID:8161571 !$#accession S43516 !'##molecule_type DNA !'##residues 1-510 ##label WAS !'##cross-references EMBL:D17586; NID:g409579; PIDN:BAA04510.1; !1PID:g409580 !'##note the authors translated the codon AGT for residue 430 as Arg GENETICS !$#introns 60/2; 109/1; 134/3; 175/3; 210/1; 222/3; 256/3; 283/3; 367/ !13; 389/3; 430/2; 468/2; 483/3 CLASSIFICATION #superfamily serine carboxypeptidase KEYWORDS disulfide bond; glycoprotein; hydrolase; serine !1carboxypeptidase FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$154,268,418 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$194,434,487 #active_site Ser, Asp, His #status predicted SUMMARY #length 510 #molecular-weight 55709 #checksum 5704 SEQUENCE /// ENTRY S51516 #type complete TITLE serine-type carboxypeptidase (EC 3.4.16.-) Z precursor - Absidia zychae ORGANISM #formal_name Absidia zychae DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 16-Jun-2000 ACCESSIONS S51516; S78013; S78014 REFERENCE S51516 !$#authors Lee, B.R.; Takeuchi, M.; Kobayashi, Y. !$#journal Curr. Genet. (1995) 27:159-165 !$#title Molecular cloning and sequence analysis of the scpZ gene !1encoding the serine carboxypeptidase of Absidia zychae. !$#cross-references MUID:95308538; PMID:7788719 !$#accession S51516 !'##molecule_type DNA !'##residues 1-460 ##label LEE !'##cross-references EMBL:D16519; NID:g556466; PIDN:BAA03966.1; !1PID:g995456 !'##experimental_source strain NRIC 1199 !$#accession S78013 !'##molecule_type protein !'##residues 52-62;90-99;367-381 ##label LEB !$#accession S78014 !'##molecule_type mRNA !'##residues 18-460 ##label LES GENETICS !$#gene spcZ !$#introns 64/3; 95/1; 107/2; 138/3; 234/2; 246/1; 270/1; 343/3; 353/2; !1384/3; 437/3 CLASSIFICATION #superfamily serine carboxypeptidase KEYWORDS glycoprotein; hydrolase; serine carboxypeptidase FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-51 #domain propeptide #status predicted #label PRE\ !$52-460 #product serine-type carboxypeptidase #status !8experimental #label MAT\ !$40,46,119 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$186 #active_site Ser #status predicted SUMMARY #length 460 #molecular-weight 50825 #checksum 7106 SEQUENCE /// ENTRY S57907 #type complete TITLE carboxypeptidase D (EC 3.4.16.6) precursor - Aspergillus niger ALTERNATE_NAMES serine-type carboxypeptidase II ORGANISM #formal_name Aspergillus niger DATE 24-Nov-1999 #sequence_revision 24-Nov-1999 #text_change 24-Nov-1999 ACCESSIONS S57907; S78071; S47152 REFERENCE S57907 !$#authors van den Hombergh, J.P.T.W.; Jarai, G.; Buxton, F.P.; Visser, !1J. !$#journal Gene (1994) 151:73-79 !$#title Cloning, characterization and expression of pepF, a gene !1encoding a serine carboxypeptidase from Aspergillus niger. !$#cross-references MUID:95129895; PMID:7828908 !$#accession S57907 !'##molecule_type DNA !'##residues 1-530 ##label VAN !'##cross-references EMBL:X79541 !'##note the authors translated the codon TAC for residue 68 as Thr REFERENCE S78071 !$#authors Svendsen, I.; Dal Degan, F. !$#submission submitted to the Protein Sequence Database, November 1997 !$#description The amino acid sequence of carboxypeptidases I and II from !1Aspergillus niger. !$#accession S78071 !'##molecule_type protein !'##residues 53-94,'L',96-113,'I',115-129,'FLQENG',136-279,'TL',282-322, !1'D',324,'A',326-335,'G',337-342,'L',344-353,'L',355-359, !1'GATIYFDR',367,'DV',370-384,'M',386-401,'F',403-473,'V', !1475-530 ##label ISV GENETICS !$#gene pepF !$#introns 67/1; 161/3; 237/2 CLASSIFICATION #superfamily serine carboxypeptidase KEYWORDS glycoprotein; hydrolase; serine carboxypeptidase; zymogen FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-52 #domain propeptide #status predicted #label PRO\ !$53-530 #product carboxypeptidase D #status experimental !8#label MAT\ !$63,94,155,228,271, !$309,377,435,443 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$124-383,285-315, !$331-341 #disulfide_bonds #status experimental\ !$211,427,506 #active_site Ser, Asp, His #status predicted SUMMARY #length 530 #molecular-weight 59052 #checksum 7356 SEQUENCE /// ENTRY S57294 #type complete TITLE carboxypeptidase D (EC 3.4.16.6) - Penicillium janthinellum ALTERNATE_NAMES penicillopeptidase S3 ORGANISM #formal_name Penicillium janthinellum DATE 24-Nov-1999 #sequence_revision 24-Nov-1999 #text_change 24-Nov-1999 ACCESSIONS S57294; S57293 REFERENCE S57294 !$#authors Svendsen, I.; Day, E.S. !$#journal FEBS Lett. (1995) 371:1-3 !$#title The primary structure of carboxypeptidase S3 from !1Penicillium janthinellum IBT 3991. !$#cross-references MUID:95394135; PMID:7664873 !$#accession S57294 !'##molecule_type protein !'##residues 1-481 ##label SVE !'##experimental_source strain IBI 3991 REFERENCE S57293 !$#authors Svendsen, I. !$#submission submitted to the Protein Sequence Database, September 1995 !$#accession S57293 !'##molecule_type protein !'##residues 1-481 ##label SVW !'##experimental_source strain IBI 3991 CLASSIFICATION #superfamily serine carboxypeptidase KEYWORDS glycoprotein; hydrolase; serine carboxypeptidase FEATURE !$1-481 #product carboxypeptidase D #status experimental !8#label MAT\ !$41,218,256,326,384, !$392 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$71-332,191-289, !$232-279 #disulfide_bonds #status experimental\ !$158,378,456 #active_site Ser, Asp, His #status predicted SUMMARY #length 481 #molecular-weight 54591 #checksum 8697 SEQUENCE /// ENTRY T05701 #type complete TITLE carboxypeptidase D (EC 3.4.16.6) precursor - barley ALTERNATE_NAMES serine-type carboxypeptidase II ORGANISM #formal_name Hordeum vulgare #common_name barley DATE 24-Nov-1999 #sequence_revision 24-Nov-1999 #text_change 16-Jun-2000 ACCESSIONS T05701; A29640; B29640 REFERENCE Z15412 !$#authors Rocher, A.; Lok, F.; Cameron-Mills, V.; von Wettstein, D. !$#submission submitted to the EMBL Data Library, November 1996 !$#description The gene family of serine carboxypeptidases in barley. !$#accession T05701 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-476 ##label ROC !'##cross-references EMBL:Y09602; PIDN:CAA70815.1 !'##experimental_source cv. Igri, leaf REFERENCE A90770 !$#authors Sorensen, S.B.; Svendsen, I.; Breddam, K. !$#journal Carlsberg Res. Commun. (1987) 52:285-295 !$#title Primary structure of carboxypeptidase II from malted barley. !$#accession A29640 !'##molecule_type protein !'##residues 35-180,'R',182-294 ##label SOR !$#accession B29640 !'##molecule_type protein !'##residues 314-350,'TN',353-472 ##label SO2 !'##note 351-Ala and 352-Thr were also found and Thr-352 was !1glycosylated GENETICS !$#gene Cxp2 !$#introns 130/1; 310/3; 386/2; 422/3 COMPLEX homodimer of two mature products, each containing an A and a !1B chain CLASSIFICATION #superfamily serine carboxypeptidase KEYWORDS blocked amino end; disulfide bond; glycoprotein; homodimer; !1hydrolase; serine carboxypeptidase; zymogen FEATURE !$1-34 #domain signal sequence #status predicted #label SIG\ !$35-294,314-472 #product carboxypeptidase D #status experimental !8#label MAT\ !$35-294 #domain chain A #status experimental #label CHA\ !$295-313 #domain connecting peptide #status predicted #label !8CNP\ !$314-472 #domain chain B #status experimental #label CHB\ !$473-476 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$148,159,291,341, !$347,472 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$190,390,443 #active_site Ser, Asp, His #status predicted\ !$314 #modified_site blocked amino end (Thr) (in mature !8form) (probably acetylated) #status experimental SUMMARY #length 476 #molecular-weight 52582 #checksum 6285 SEQUENCE /// ENTRY A29639 #type complete TITLE carboxypeptidase D (EC 3.4.16.6) - wheat ALTERNATE_NAMES serine-type carboxypeptidase II ORGANISM #formal_name Triticum aestivum #common_name common wheat DATE 24-Nov-1999 #sequence_revision 24-Nov-1999 #text_change 24-Nov-1999 ACCESSIONS A29639; C29639; B29639 REFERENCE A90771 !$#authors Breddam, K.; Sorensen, S.B.; Svendsen, I. !$#journal Carlsberg Res. Commun. (1987) 52:297-311 !$#title Primary structure and enzymatic properties of !1carboxypeptidase II from wheat bran. !$#accession A29639 !'##molecule_type protein !'##residues 1-263 ##label BRE !'##note A chain !$#accession C29639 !'##molecule_type protein !'##residues 4-263 ##label BR2 !'##note A' chain !$#accession B29639 !'##molecule_type protein !'##residues 264-423 ##label BR3 !'##note B chain COMPLEX homodimer of two mature products, each of which is cleaved !1to contain an A-type and a B chain CLASSIFICATION #superfamily serine carboxypeptidase KEYWORDS disulfide bond; glycoprotein; homodimer; hydrolase; serine !1carboxypeptidase FEATURE !$1-263,264-423 #product carboxypeptidase D #status experimental !8#label MAT\ !$1-263 #domain A chain #status experimental #label CHA\ !$4-263 #domain A' chain #status experimental #label CHA1\ !$264-423 #domain B chain #status experimental #label CHB\ !$116,127,259,291, !$297,421 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$158,340,392 #active_site Ser, Asp, His #status predicted SUMMARY #length 423 #molecular-weight 47111 #checksum 3322 SEQUENCE /// ENTRY S78072 #type complete TITLE serine-type carboxypeptidase (EC 3.4.16.-) I - Aspergillus niger ORGANISM #formal_name Aspergillus niger DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Dec-1999 ACCESSIONS S78072 REFERENCE S78071 !$#authors Svendsen, I.; Dal Degan, F. !$#submission submitted to the Protein Sequence Database, November 1997 !$#description The amino acid sequence of carboxypeptidases I and II from !1Aspergillus niger. !$#accession S78072 !'##molecule_type protein !'##residues 1-471 ##label ISV CLASSIFICATION #superfamily serine carboxypeptidase KEYWORDS glycoprotein; hydrolase; serine carboxypeptidase FEATURE !$1-471 #product serine-type carboxypeptidase I #status !8experimental #label MAT\ !$6,14,40,100,215, !$304,350,366,374 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$69-322,229-257, !$273-283 #disulfide_bonds #status experimental\ !$156,360,439 #active_site Ser, Asp, His #status experimental SUMMARY #length 471 #molecular-weight 52540 #checksum 7717 SEQUENCE /// ENTRY CPBOA #type complete TITLE carboxypeptidase A (EC 3.4.17.1) precursor [validated] - bovine ALTERNATE_NAMES procarboxypeptidase A activation peptide ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 24-Apr-1984 #sequence_revision 30-Jun-1992 #text_change 05-May-2000 ACCESSIONS JN0126; JT0440; A31406; S00059; A38834; A00910; A90355 REFERENCE JN0126 !$#authors Le Hueerou, I.; Guilloteau, P.; Toullec, R.; Puigserver, A.; !1Wicker, C. !$#journal Biochem. Biophys. Res. Commun. (1991) 175:110-116 !$#title Cloning and nucleotide sequence of a bovine pancreatic !1preprocarboxypeptidase A cDNA. !$#cross-references MUID:91151335; PMID:1998496 !$#accession JN0126 !'##molecule_type mRNA !'##residues 1-419 ##label LEH !'##cross-references GB:M61851; NID:g162788; PIDN:AAA30426.1; !1PID:g162789 REFERENCE JT0440 !$#authors Foglizzo, E.; Bonicel, J.; Kerfelec, B.; Granon, S.; Chapus, !1C. !$#journal Biochim. Biophys. Acta (1988) 954:183-188 !$#title Primary structure of the activation peptide from bovine !1pancreatic procarboxypeptidase A. !$#cross-references MUID:88209583; PMID:3365436 !$#accession JT0440 !'##molecule_type protein !'##residues 17-110 ##label FOG REFERENCE A31406 !$#authors Wade, R.D.; Hass, G.M.; Kumar, S.; Walsh, K.A.; Neurath, H. !$#journal Biochimie (1988) 70:1137-1142 !$#title The amino acid sequence of the activation peptide of bovine !1pro-carboxypeptidase A. !$#cross-references MUID:89150306; PMID:3147705 !$#accession A31406 !'##molecule_type protein !'##residues 17-110 ##label WAD REFERENCE S00059 !$#authors Chapus, C.; Kerfelec, B.; Foglizzo, E.; Bonicel, J. !$#journal Eur. J. Biochem. (1987) 166:379-385 !$#title Further studies on the activation of bovine pancreatic !1procarboxypeptidase A by trypsin. !$#cross-references MUID:87275921; PMID:3609014 !$#accession S00059 !'##molecule_type protein !'##residues 17-69 ##label CHA REFERENCE A38834 !$#authors Bradshaw, R.A.; Ericsson, L.H.; Walsh, K.A.; Neurath, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1969) 63:1389-1394 !$#title The amino acid sequence of bovine carboxypeptidase A. !$#cross-references MUID:70050818; PMID:5260942 !$#accession A38834 !'##molecule_type protein !'##residues 111-137,'Q',139-140,'E',142-417 ##label BRA REFERENCE A90360 !$#authors Bradshaw, R.A.; Walsh, K.A.; Neurath, H. !$#journal Biochemistry (1971) 10:961-972 !$#title Amino acid sequence of bovine carboxypeptidase A. Isolation !1and characterization of selected peptic and nagarse peptides !1and the complete sequence of fragment F1. !$#cross-references MUID:71155185; PMID:4927805 !$#accession A00910 !'##molecule_type protein !'##residues 214-411 ##label BR2 !'##note this is the final paper in a series REFERENCE A90355 !$#authors Petra, P.H.; Hermodson, M.A.; Walsh, K.A.; Neurath, H. !$#journal Biochemistry (1971) 10:4023-4025 !$#title Characterization of bovine carboxypeptidase A(Allan). !$#cross-references MUID:72138789; PMID:5143102 !$#accession A90355 !'##molecule_type protein !'##residues 111-142 ##label PET REFERENCE A90556 !$#authors Petra, P.H.; Bradshaw, R.A.; Walsh, K.A.; Neurath, H. !$#journal Biochemistry (1969) 8:2762-2768 !$#title Identification of the amino acid replacements characterizing !1the allotropic forms of bovine carboxypeptidase A. !$#cross-references MUID:69283620; PMID:5817619 !$#contents annotation; allelic variant !$#note an allelic variant having 179-Val, 228-Glu, and 305-Leu !1occurs with nearly equal frequency REFERENCE A50963 !$#authors Lipscomb, W.N.; Rees, D.C. !$#submission submitted to the Brookhaven Protein Data Bank, March 1982 !$#cross-references PDB:4CPA !$#contents annotation; X-ray crystallography, 2.5 angstroms, residues !1111-137,'Q',139-140,'E',142-198,'N',200-202,'N',204-223,'N', !1225-231,'E',233-294,'N',296-337,'A',339-414,'V',416-417 REFERENCE A92902 !$#authors Rees, D.C.; Lewis, M.; Lipscomb, W.N. !$#journal J. Mol. Biol. (1983) 168:367-387 !$#title Refined crystal structure of carboxypeptidase A at 1.54 !1angstrom resolution. !$#cross-references MUID:83294519; PMID:6887246 !$#contents annotation; X-ray crystallography, 1.54 angstroms CLASSIFICATION #superfamily carboxypeptidase KEYWORDS hydrolase; metallo-carboxypeptidase; metalloprotein; protein !1digestion; zinc FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-110 #domain activation peptide #status experimental !8#label ACP\ !$111-419 #product carboxypeptidase A #status experimental !8#label MAT\ !$179,182,306 #binding_site zinc (His, Glu, His) #status !8experimental\ !$248-271 #disulfide_bonds #status experimental\ !$358,380 #active_site Tyr, Glu #status experimental SUMMARY #length 419 #molecular-weight 47082 #checksum 9714 SEQUENCE /// ENTRY S29127 #type complete TITLE carboxypeptidase A (EC 3.4.17.1) CPA1 precursor - human ALTERNATE_NAMES pancreatic carboxypeptidase A1 ORGANISM #formal_name Homo sapiens #common_name man DATE 25-Feb-1994 #sequence_revision 19-Jan-1996 #text_change 18-Jun-1999 ACCESSIONS S29127; A34205; S08253; S02810; S71394; S02811 REFERENCE S29127 !$#authors Catasus, L.; Villegas, V.; Pascual, R.; Aviles, F.X.; !1Wicker-Planquart, C.; Puigserver, A. !$#journal Biochem. J. (1992) 287:299-303 !$#title cDNA cloning and sequence analysis of human pancreatic !1procarboxypeptidase A1. !$#cross-references MUID:93038569; PMID:1417781 !$#accession S29127 !'##molecule_type mRNA !'##residues 1-419 ##label CAT !'##cross-references EMBL:X67318; NID:g35329; PIDN:CAA47732.1; !1PID:g35330 REFERENCE A34205 !$#authors Stewart, E.A.; Craik, C.S.; Hake, L.; Bowcock, A.M. !$#journal Am. J. Hum. Genet. (1990) 46:795-800 !$#title Human carboxypeptidase A identifies a BglII RFLP and maps to !17q31-qter. !$#cross-references MUID:90196012; PMID:1969228 !$#accession A34205 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 330-396 ##label STE !'##note the authors translated the codon CTG for residue 391 as Val REFERENCE S08253 !$#authors Moulard, M.; Michon, T.; Kerfelec, B.; Chapus, C. !$#journal FEBS Lett. (1990) 261:179-183 !$#title Further studies on the human pancreatic binary complexes !1involving procarboxypeptidase A. !$#cross-references MUID:90169111; PMID:2307232 !$#accession S08253 !'##molecule_type protein !'##residues 17-43;'XXX',114-135 ##label MOU REFERENCE S02809 !$#authors Pascual, R.; Burgos, F.J.; Salva, M.; Soriano, F.; Mendez, !1E.; Aviles, F.X. !$#journal Eur. J. Biochem. (1989) 179:609-616 !$#title Purification and properties of five different forms of human !1procarboxypeptidases. !$#cross-references MUID:89153096; PMID:2920728 !$#accession S02810 !'##molecule_type protein !'##residues 17-42 ##label PAS REFERENCE S71394 !$#authors Laethem, R.M.; Blumenkopf, T.A.; Cory, M.; Elwell, L.; !1Moxham, C.P.; Ray, P.H.; Walton, L.M.; Smith, G.K. !$#journal Arch. Biochem. Biophys. (1996) 332:8-18 !$#title Expression and characterization of human pancreatic !1preprocarboxypeptidase A1 and preprocarboxypeptidase A2. !$#cross-references MUID:96400327; PMID:8806703 !$#accession S71394 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-419 ##label LAE GENETICS !$#gene GDB:CPA1; CPA !'##cross-references GDB:120597; OMIM:114850 !$#map_position 7q32-7qter CLASSIFICATION #superfamily carboxypeptidase KEYWORDS hydrolase; metallo-carboxypeptidase; metalloprotein; protein !1digestion; zinc FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-110 #domain activation peptide #status predicted #label !8ACP\ !$111-419 #product carboxypeptidase A isozyme 1 #status !8predicted #label MAT\ !$179,182,306 #binding_site zinc (His, Glu, His) #status predicted\ !$248-271 #disulfide_bonds #status predicted\ !$358,380 #active_site Tyr, Glu #status predicted SUMMARY #length 419 #molecular-weight 47140 #checksum 6056 SEQUENCE /// ENTRY CPRTA #type complete TITLE carboxypeptidase A (EC 3.4.17.1) precursor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 24-Sep-1999 ACCESSIONS A00911; B32129 REFERENCE A00911 !$#authors Quinto, C.; Quiroga, M.; Swain, W.F.; Nikovits Jr., W.C.; !1Standring, D.N.; Pictet, R.L.; Valenzuela, P.; Rutter, W.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:31-35 !$#title Rat preprocarboxypeptidase A: cDNA sequence and preliminary !1characterization of the gene. !$#cross-references MUID:82105986; PMID:6275388 !$#accession A00911 !'##molecule_type mRNA !'##residues 1-419 ##label QUI !'##cross-references GB:J00713; NID:g203364; PIDN:AAA40893.1; !1PID:g203365 REFERENCE A92693 !$#authors Clauser, E.; Gardell, S.J.; Craik, C.S.; MacDonald, R.J.; !1Rutter, W.J. !$#journal J. Biol. Chem. (1988) 263:17837-17845 !$#title Structural characterization of the rat carboxypeptidase A1 !1and B genes. Comparative analysis of the rat !1carboxypeptidase gene family. !$#cross-references MUID:89034324; PMID:3182872 !$#accession B32129 !'##molecule_type DNA !'##residues 1-260,'F',262,'M',264-346,'K',348-419 ##label CLA GENETICS !$#gene CPA1 !$#introns 22/2; 49/3; 127/3; 161/3; 196/2; 232/3; 263/2; 329/3; 358/1 !$#note the authors translated the codon GTC for residue 196 as Ile CLASSIFICATION #superfamily carboxypeptidase KEYWORDS hydrolase; metallo-carboxypeptidase; metalloprotein; protein !1digestion; zinc FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-110 #domain activation peptide #status predicted #label !8PRO\ !$111-419 #product carboxypeptidase A #status predicted #label !8MAT\ !$179,182,306 #binding_site zinc (His, Glu, His) #status predicted\ !$248-271 #disulfide_bonds #status predicted\ !$358,380 #active_site Tyr, Glu #status predicted SUMMARY #length 419 #molecular-weight 47147 #checksum 6710 SEQUENCE /// ENTRY A42332 #type complete TITLE carboxypeptidase B (EC 3.4.17.2) precursor, pancreatic - human ALTERNATE_NAMES carboxypeptidase B isozyme 1 ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1993 #sequence_revision 19-Jan-1996 #text_change 18-Jun-1999 ACCESSIONS A42332; S08254; S02813; S02812 REFERENCE A42332 !$#authors Yamamoto, K.K.; Pousette, A.; Chow, P.; Wilson, H.; el !1Shami, S.; French, C.K. !$#journal J. Biol. Chem. (1992) 267:2575-2581 !$#title Isolation of a cDNA encoding a human serum marker for acute !1pancreatitis. Identification of pancreas-specific protein as !1pancreatic procarboxypeptidase B. !$#cross-references MUID:92129345; PMID:1370825 !$#accession A42332 !'##molecule_type mRNA !'##residues 1-416 ##label YAM !'##cross-references GB:M81057; NID:g809194; PIDN:AAA66973.1; !1PID:g189625 !'##experimental_source pancreas !'##note sequence extracted from NCBI backbone (NCBIN:78573, !1NCBIP:78574) REFERENCE S08253 !$#authors Moulard, M.; Michon, T.; Kerfelec, B.; Chapus, C. !$#journal FEBS Lett. (1990) 261:179-183 !$#title Further studies on the human pancreatic binary complexes !1involving procarboxypeptidase A. !$#cross-references MUID:90169111; PMID:2307232 !$#accession S08254 !'##molecule_type protein !'##residues 16-40 ##label MOU !'##experimental_source pancreas REFERENCE S02809 !$#authors Pascual, R.; Burgos, F.J.; Salva, M.; Soriano, F.; Mendez, !1E.; Aviles, F.X. !$#journal Eur. J. Biochem. (1989) 179:609-616 !$#title Purification and properties of five different forms of human !1procarboxypeptidases. !$#cross-references MUID:89153096; PMID:2920728 !$#accession S02813 !'##molecule_type protein !'##residues 16-36,'X',38-43 ##label PAS !'##experimental_source pancreas !$#accession S02812 !'##molecule_type protein !'##residues 16-36,'Q',38-43 ##label PA2 !'##experimental_source pancreas GENETICS !$#gene GDB:CPB1 !'##cross-references GDB:132160; OMIM:114852 !$#map_position 3q21.3-3q25 CLASSIFICATION #superfamily carboxypeptidase KEYWORDS hydrolase; metallo-carboxypeptidase; metalloprotein; protein !1digestion; zinc FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-110 #domain activation peptide #status predicted #label !8ACP\ !$111-415 #product carboxypeptidase B, pancreatic #status !8predicted #label MAT\ !$173-186,258-272 #disulfide_bonds #status predicted\ !$176,179,303 #binding_site zinc (His, Glu, His) #status predicted\ !$355,377 #active_site Tyr, Glu #status predicted SUMMARY #length 416 #molecular-weight 47264 #checksum 2935 SEQUENCE /// ENTRY CPBOB #type complete TITLE carboxypeptidase B (EC 3.4.17.2) - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 02-Aug-1994 ACCESSIONS A93797; A92150; A00912 REFERENCE A93797 !$#authors Titani, K.; Ericsson, L.H.; Walsh, K.A.; Neurath, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1975) 72:1666-1670 !$#title Amino-acid sequence of bovine carboxypeptidase B. !$#cross-references MUID:75217824; PMID:1057162 !$#accession A93797 !'##molecule_type protein !'##residues 1-306 ##label TIT REFERENCE A92150 !$#authors Schmidt, J.J.; Hirs, C.H.W. !$#journal J. Biol. Chem. (1974) 249:3756-3764 !$#title Primary structure of bovine carboxypeptidase B. Inferences !1from the locations of the half-cystines and identification !1of the active site arginine. !$#cross-references MUID:74260705; PMID:4833744 !$#accession A92150 !'##molecule_type protein !'##residues 31-93;131-181;263-265;292-306 ##label SCH REFERENCE A92839 !$#authors Schmid, M.F.; Herriott, J.R. !$#journal J. Mol. Biol. (1976) 103:175-190 !$#title Structure of carboxypeptidase B at 2.8 angstrom resolution. !$#cross-references MUID:76265065; PMID:957425 !$#contents annotation; X-ray crystallography, 2.8 angstroms, and !1disulfide bonds REFERENCE A92051 !$#authors Plummer Jr., T.H. !$#journal J. Biol. Chem. (1969) 244:5246-5253 !$#title Isolation and sequence of peptides at the active center of !1bovine carboxypeptidase B. !$#cross-references MUID:70007159; PMID:5344132 !$#contents annotation; active site REFERENCE A92119 !$#authors Kimmel, M.T.; Plummer Jr., T.H. !$#journal J. Biol. Chem. (1972) 247:7864-7869 !$#title Identification of a glutamic acid at the active center of !1bovine carboxypeptidase B. !$#cross-references MUID:73061487; PMID:4565668 !$#contents annotation; active site CLASSIFICATION #superfamily carboxypeptidase KEYWORDS hydrolase; metallo-carboxypeptidase; metalloprotein; protein !1digestion; zinc FEATURE !$63-76,135-158, !$149-163 #disulfide_bonds #status experimental\ !$66,69,194 #binding_site zinc (His, Glu, His) #status !8experimental\ !$246,268 #active_site Tyr, Glu #status experimental SUMMARY #length 306 #molecular-weight 34612 #checksum 2173 SEQUENCE /// ENTRY A34487 #type complete TITLE carboxypeptidase A (EC 3.4.17.1) precursor - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A34487 REFERENCE A34487 !$#authors Reynolds, D.S.; Stevens, R.L.; Gurley, D.S.; Lane, W.S.; !1Austen, K.F.; Serafin, W.E. !$#journal J. Biol. Chem. (1989) 264:20094-20099 !$#title Isolation and molecular cloning of mast cell !1carboxypeptidase A. A novel member of the carboxypeptidase !1gene family. !$#cross-references MUID:90062123; PMID:2584208 !$#accession A34487 !'##status preliminary !'##molecule_type mRNA !'##residues 1-417 ##label REY !'##cross-references GB:J05118; NID:g192372; PIDN:AAA37369.1; !1PID:g309135 CLASSIFICATION #superfamily carboxypeptidase KEYWORDS hydrolase; metallo-carboxypeptidase FEATURE !$356,378 #active_site Tyr, Glu #status predicted SUMMARY #length 417 #molecular-weight 48790 #checksum 8106 SEQUENCE /// ENTRY CPCYB #type complete TITLE carboxypeptidase B (EC 3.4.17.2) - broad-fingered crayfish ORGANISM #formal_name Astacus astacus, Astacus fluviatilis #common_name broad-fingered crayfish DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 06-Dec-1996 ACCESSIONS A05141; A14178 REFERENCE A90482 !$#authors Titani, K.; Ericsson, L.H.; Kumar, S.; Jakob, F.; Neurath, !1H.; Zwilling, R. !$#journal Biochemistry (1984) 23:1245-1250 !$#title Amino acid sequence of crayfish (Astacus fluviatilis) !1carboxypeptidase B. !$#accession A05141 !'##molecule_type protein !'##residues 1-303 ##label TIT CLASSIFICATION #superfamily carboxypeptidase KEYWORDS hydrolase; metallo-carboxypeptidase; metalloprotein; protein !1digestion; zinc FEATURE !$241,264 #active_site Tyr, Glu #status predicted SUMMARY #length 303 #molecular-weight 33918 #checksum 3249 SEQUENCE /// ENTRY CPSMMU #type complete TITLE muramoylpentapeptide carboxypeptidase (EC 3.4.17.8) precursor - Streptomyces albus ALTERNATE_NAMES metallo-DD-peptidase ORGANISM #formal_name Streptomyces albus DATE 20-Sep-1984 #sequence_revision 27-Jun-1994 #text_change 18-Jun-1999 ACCESSIONS A60997; A00913 REFERENCE A60997 !$#authors Duez, C.; Lakaye, B.; Houba, S.; Dusart, J.; Ghuysen, J.M. !$#journal FEMS Microbiol. Lett. (1990) 71:215-220 !$#title Cloning, nucleotide sequence and amplified expression of the !1gene encoding the extracellular metallo (Zn) DD-peptidase of !1Streptomyces albus G. !$#accession A60997 !'##molecule_type DNA !'##residues 1-255 ##label DUE !'##cross-references GB:X55794; NID:g288966; PIDN:CAA39319.1; !1PID:g288967 REFERENCE A91127 !$#authors Joris, B.; Van Beeumen, J.; Casagrande, F.; Gerday, C.; !1Frere, J.M.; Ghuysen, J. !$#journal Eur. J. Biochem. (1983) 130:53-69 !$#title The complete amino acid sequence of the Zn(2+)-containing !1D-alanyl-D-alanine-cleaving carboxypeptidase of Streptomyces !1albus G. !$#cross-references MUID:83131648; PMID:6825689 !$#note S. albus G !$#accession A00913 !'##molecule_type protein !'##residues 'N',44-109,111-255 ##label JOR REFERENCE A93288 !$#authors Dideberg, O.; Charlier, P.; Dive, G.; Joris, B.; Frere, !1J.M.; Ghuysen, J.M. !$#journal Nature (1982) 299:469-470 !$#title Structure of a Zn(2+)-containing D-alanyl-Dalanine-cleaving !1carboxypeptidase at 2.5 angstrom resolution. !$#cross-references MUID:83012968; PMID:7121588 !$#contents annotation; X-ray crystallography, 2.5 angstroms COMMENT This enzyme catalyzes carboxypeptidation and !1transpeptidation reactions involved in bacterial cell wall !1metabolism. It also has a weak beta-lactamase activity, !1hydrolyzing penicillin into penicilloate at a very low rate. CLASSIFICATION #superfamily muramoyl-pentapeptide carboxypeptidase KEYWORDS hydrolase; metallo-carboxypeptidase; zinc FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-42 #domain propeptide #status predicted #label PRO\ !$43-255 #product muramoylpentapeptide carboxypeptidase !8#status experimental #label MAT\ !$45-123,136-184, !$212-253 #disulfide_bonds #status experimental\ !$180 #binding_site substrate (Arg) #status predicted\ !$196,237,239 #binding_site zinc (His) #status experimental\ !$234 #active_site His #status predicted SUMMARY #length 255 #molecular-weight 26190 #checksum 2335 SEQUENCE /// ENTRY YXPSF2 #type complete TITLE carboxypeptidase G2 (EC 3.4.17.-) precursor - Pseudomonas sp. ALTERNATE_NAMES folate hydrolase G2; pteroylmonoglutamic acid hydrolase G2 ORGANISM #formal_name Pseudomonas sp. DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 18-Jun-1999 ACCESSIONS A24955 REFERENCE A24955 !$#authors Minton, N.P.; Atkinson, T.; Bruton, C.J.; Sherwood, R.F. !$#journal Gene (1984) 31:31-38 !$#title The complete nucleotide sequence of the Pseudomonas gene !1coding for carboxypeptidase G2. !$#cross-references MUID:85128455; PMID:6396165 !$#accession A24955 !'##molecule_type DNA !'##residues 1-415 ##label MIN !'##cross-references GB:M12599; GB:M12151; NID:g695388; PIDN:AAA62842.1; !1PID:g151184 !'##experimental_source strain RS-16 !'##note part of the mature protein was sequenced CLASSIFICATION #superfamily folate hydrolase G KEYWORDS dimer; hydrolase; metallo-carboxypeptidase; zinc FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-415 #product folate hydrolase G2 #status predicted #label !8MPT SUMMARY #length 415 #molecular-weight 43932 #checksum 3500 SEQUENCE /// ENTRY JC4655 #type complete TITLE acylaminoacyl-peptidase (EC 3.4.19.1) - human ALTERNATE_NAMES acidpeptide hydrolase; acylamino acid releasing enzyme; lung DNF15S2 protein ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS JC4655; A42257; A30145; A53799 REFERENCE JC4655 !$#authors Mitta, M.; Ohnogi, H.; Mizutani, S.; Sakiyama, F.; Kato, I.; !1Tsunasawa, S. !$#journal DNA Res. (1996) 3:31-35 !$#title The nucleotide sequence of human acylamino acid-releasing !1enzyme. !$#cross-references MUID:96281126; PMID:8724851 !$#accession JC4655 !'##molecule_type mRNA !'##residues 1-732 ##label MIT !'##cross-references DDBJ:D38441; NID:g556513; PIDN:BAA07476.1; !1PID:g556514 !'##experimental_source liver REFERENCE A42257 !$#authors Scaloni, A.; Jones, W.M.; Barra, D.; Pospischil, M.; Sassa, !1S.; Popowicz, A.; Manning, L.R.; Schneewind, O.; Manning, !1J.M. !$#journal J. Biol. Chem. (1992) 267:3811-3818 !$#title Acylpeptide hydrolase: inhibitors and some active site !1residues of the human enzyme. !$#cross-references MUID:92156118; PMID:1740429 !$#accession A42257 !'##molecule_type protein !'##residues 4-18;45-53;90-95;119-126;130-136,'A',138-149;173-193,'T', !1195-199,'A',201-219;270-273;280-306;314-337;340-360,'XX', !1363-366;376-385;412-416,'X',418-420,'N',422-427;435-457, !1459-461,'D',463-471,'Q',473-475,'V',477-497;519-527;539-574, !1'M',576-591,'L',593;656-657,'K',659-664;677-681;699-717 !1##label SCA !'##experimental_source lung REFERENCE A30145 !$#authors Naylor, S.L.; Marshall, A.; Hensel, C.; Martinez, P.F.; !1Holley, B.; Sakaguchi, A.Y. !$#journal Genomics (1989) 4:355-361 !$#title The DNF15S2 locus at 3p21 is transcribed in normal lung and !1small cell lung cancer. !$#cross-references MUID:89233127; PMID:2565880 !$#accession A30145 !'##molecule_type mRNA !'##residues 102-112,'D',114-136,'A',138-167,'K',169-196, !1'QTKPSRGISLCFMKTGRNMVSKSIPVSACWMSRVETSLCLRGSLRMCPLDRHFGPLEML !1VWCLWAGGMSL',197,'V',271-383,'T',385-451, !1'WRRPSPFPTSTGASGCYSHPQSKRMCSMLALTLKQSCCSLAALQIRPKCPWWSCPT', !1509,'A',511-581,'X',583-604,'RACLRTRDHNASMLGSTDILTGAWW', !1'RL',617-618,637-659,'SSGEDTTVTDVGQEDAVCLSRHEYTSSRPECA', !1697-716,'A',718 ##label NA2 !'##cross-references GB:J03068; NID:g181629; PIDN:AAA35769.1; !1PID:g181630 !'##experimental_source lung REFERENCE A53799 !$#authors Scaloni, A.; Barra, D.; Jones, W.M.; Manning, J.M. !$#journal J. Biol. Chem. (1994) 269:15076-15084 !$#title Human acylpeptide hydrolase. Studies on its thiol groups and !1mechanism of action. !$#cross-references MUID:94253066; PMID:8195144 !$#accession A53799 !'##molecule_type protein !'##residues 19-33;63-65 ##label SC2 GENETICS !$#gene GDB:APEH; AARE; D3S48E; DNF15S2 !'##cross-references GDB:127917; OMIM:102645 !$#map_position 3p21.3-3p21.2 FUNCTION !$#description hydrolyzes amino-terminal acetylated peptides into peptides !1having free amino-termini and N-acetylamino acids CLASSIFICATION #superfamily acylaminoacyl-peptidase KEYWORDS acetylated amino end; blocked amino end; homotetramer; !1hydrolase; liver; omega peptidase; serine proteinase FEATURE !$1 #modified_site acetylated amino end (Met) #status !8predicted\ !$587 #active_site Ser #status experimental\ !$675,707 #active_site Asp, His #status predicted SUMMARY #length 732 #molecular-weight 81292 #checksum 467 SEQUENCE /// ENTRY JU0132 #type complete TITLE acylaminoacyl-peptidase (EC 3.4.19.1) [validated] - pig ALTERNATE_NAMES acyl-peptide hydrolase; acylamino-acid-releasing enzyme ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 21-Jul-2000 ACCESSIONS JU0132 REFERENCE JU0132 !$#authors Mitta, M.; Asada, K.; Uchimura, Y.; Kimizuka, F.; Kato, I.; !1Sakiyama, F.; Tsunasawa, S. !$#journal J. Biochem. (1989) 106:548-551 !$#title The primary structure of porcine liver acylamino !1acid-releasing enzyme deduced from cDNA sequences. !$#cross-references MUID:90110044; PMID:2691504 !$#accession JU0132 !'##molecule_type mRNA !'##residues 1-732 ##label MIT GENETICS !$#introns 4/3; 49/1; 91/2; 122/3; 148/1; 202/3; 248/3; 279/2; 293/1; !1333/3; 354/1; 386/3; 404/1; 433/3; 480/1; 508/1; 535/1; 564/ !13; 628/2; 662/3; 698/2 FUNCTION !$#description EC 3.4.19.1 [validated, MUID:90110044] CLASSIFICATION #superfamily acylaminoacyl-peptidase KEYWORDS acetylated amino end; homotetramer; hydrolase; omega !1peptidase FEATURE !$1 #modified_site acetylated amino end (Met) #status !8experimental\ !$587,675,707 #active_site Ser, Asp, His #status predicted SUMMARY #length 732 #molecular-weight 81257 #checksum 1473 SEQUENCE /// ENTRY S07624 #type complete TITLE acylaminoacyl-peptidase (EC 3.4.19.1) - rat ALTERNATE_NAMES acyl-peptide hydrolase; acylamino-acid-releasing enzyme ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 18-Jun-1999 ACCESSIONS A33706; S07624 REFERENCE A33706 !$#authors Kobayashi, K.; Lin, L.W.; Yeadon, J.E.; Klickstein, L.B.; !1Smith, J.A. !$#journal J. Biol. Chem. (1989) 264:8892-8899 !$#title Cloning and sequence analysis of a rat liver cDNA encoding !1acyl-peptide hydrolase. !$#cross-references MUID:89255359; PMID:2722805 !$#accession A33706 !'##molecule_type mRNA !'##residues 1-732 ##label KOB !'##cross-references GB:J04733; NID:g202931; PIDN:AAA88506.1; !1PID:g202932 !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing REFERENCE S07624 !$#authors Lin, L.W.; Lee, F.J.S.; Smith, J.A. !$#journal Nucleic Acids Res. (1989) 17:4397-4400 !$#title Structural organization of the rat acyl-peptide hydrolase !1gene. !$#cross-references MUID:89296508; PMID:2578023 !$#accession S07624 !'##status translation not shown !'##molecule_type DNA !'##residues 1-732 ##label LIN !'##cross-references EMBL:X14915 GENETICS !$#introns 4/3; 49/1; 91/2; 122/3; 148/1; 202/3; 248/3; 279/2; 293/1; !1333/3; 354/1; 386/3; 404/1; 433/3; 480/1; 508/1; 535/1; 564/ !13; 628/2; 662/3; 698/2 CLASSIFICATION #superfamily acylaminoacyl-peptidase KEYWORDS blocked amino end; homotetramer; hydrolase; omega peptidase FEATURE !$1 #modified_site blocked amino end (Met) (probably !8acetylated) #status experimental\ !$118,291,443 #modified_site lysine derivative (Lys) #status !8experimental\ !$587,675,707 #active_site Ser, Asp, His #status predicted SUMMARY #length 732 #molecular-weight 81383 #checksum 9837 SEQUENCE /// ENTRY PRSASK #type complete TITLE glutamyl endopeptidase (EC 3.4.21.19) precursor - Staphylococcus aureus ALTERNATE_NAMES staphylococcal serine proteinase ORGANISM #formal_name Staphylococcus aureus DATE 04-Dec-1986 #sequence_revision 30-Jun-1991 #text_change 18-Jun-1999 ACCESSIONS A26812; A00966 REFERENCE A26812 !$#authors Carmona, C.; Gray, G.L. !$#journal Nucleic Acids Res. (1987) 15:6757 !$#title Nucleotide sequence of the serine protease gene of !1Staphylococcus aureus, strain V8. !$#cross-references MUID:87316953; PMID:3306605 !$#accession A26812 !'##molecule_type DNA !'##residues 1-336 ##label CAR !'##cross-references EMBL:Y00356; NID:g46686; PIDN:CAA68434.1; !1PID:g46687 !'##experimental_source strain V8 REFERENCE A23824 !$#authors Drapeau, G.R. !$#journal Can. J. Biochem. (1978) 56:534-544 !$#title The primary structure of staphylococcal protease. !$#cross-references MUID:78212487; PMID:96922 !$#accession A00966 !'##molecule_type protein !'##residues 69-108;110-124;126-144,'D',146-192,'T',194-228,'N',230-258, !1'Q',260,'D',262-267,'NE',270,'N',271-280,'NN';336 ##label !1DRA !'##experimental_source strain V8 COMMENT This extracellular proteolytic enzyme preferentially cleaves !1the peptide bonds on the carboxyl-terminal side of either !1aspartate or glutamate. COMMENT This enzyme may be distantly related to the trypsin-type !1serine proteinases, although there is little sequence !1similarity except in the vicinity of the known and predicted !1active site residues. CLASSIFICATION #superfamily staphylococcal serine proteinase KEYWORDS hydrolase; serine proteinase FEATURE !$69-336 #product staphylococcal serine proteinase #status !8experimental #label ACT\ !$119,161 #active_site His, Asp #status predicted\ !$237 #active_site Ser #status experimental SUMMARY #length 336 #molecular-weight 36326 #checksum 1208 SEQUENCE /// ENTRY PRSAEA #type complete TITLE epidermolytic toxin A precursor - Staphylococcus aureus ALTERNATE_NAMES exfoliative toxin A ORGANISM #formal_name Staphylococcus aureus DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 18-Jun-1999 ACCESSIONS A26680; C26680; A26679; S11541; A46569 REFERENCE A26680 !$#authors Lee, C.Y.; Schmidt, J.J.; Johnson-Winegar, A.D.; Spero, L.; !1Iandolo, J.J. !$#journal J. Bacteriol. (1987) 169:3904-3909 !$#title Sequence determination and comparison of the exfoliative !1toxin A and toxin B genes from Staphylococcus aureus. !$#cross-references MUID:87307959; PMID:3040666 !$#accession A26680 !'##molecule_type DNA !'##residues 1-280 ##label LEE !'##cross-references GB:M17347; NID:g153005; PIDN:AAA26625.1; !1PID:g153006 !'##experimental_source strain UT0002 !$#accession C26680 !'##molecule_type protein !'##residues 39-82;209-248 ##label LEE2 !'##note the carboxyl-terminal residue of the mature protein is Lys REFERENCE A26679 !$#authors O'Toole, P.W.; Foster, T.J. !$#journal J. Bacteriol. (1987) 169:3910-3915 !$#title Nucleotide sequence of the epidermolytic toxin A gene of !1Staphylococcus aureus. !$#cross-references MUID:87307960; PMID:3040667 !$#accession A26679 !'##molecule_type DNA !'##residues 1-280 ##label OTO !'##cross-references GB:M17357; NID:g153007; PIDN:AAA26626.1; !1PID:g153008 !'##experimental_source strain TC16 REFERENCE S11541 !$#authors Bailey, C.J.; Smith, T.P. !$#journal Biochem. J. (1990) 269:535-537 !$#title The reactive serine residue of epidermolytic toxin A. !$#cross-references MUID:90351379; PMID:2117445 !$#accession S11541 !'##status preliminary !'##molecule_type protein !'##residues 224-240 ##label BAI REFERENCE A46569 !$#authors Sakurai, S.; Suzuki, H.; Kondo, I. !$#journal J. Gen. Microbiol. (1988) 134:711-717 !$#title DNA sequencing of the eta gene coding for staphylococcal !1exfoliative toxin serotype A. !$#cross-references MUID:89036121; PMID:3183619 !$#accession A46569 !'##status preliminary !'##molecule_type DNA !'##residues 1-2,'I',4-249,'R',251-254,'I',256-280 ##label SAK !'##cross-references GB:M20371 !'##experimental_source strain ZM !'##note the authors translated the codon ATT for residue 3 as Asn, CAA !1for residue 32 as Glu, GAA for residue 212 as Asp, GAG for !1residue 214 as Asp, AGG for residue 250 as Ser, and ATT for !1residue 255 as Leu GENETICS !$#gene eta CLASSIFICATION #superfamily staphylococcal serine proteinase KEYWORDS scalded skin syndrome; toxin FEATURE !$1-38 #domain signal sequence #status predicted #label SIG\ !$39-280 #product epidermolytic toxin A #status predicted !8#label MAT SUMMARY #length 280 #molecular-weight 31077 #checksum 305 SEQUENCE /// ENTRY PRSAEB #type complete TITLE epidermolytic toxin B precursor - Staphylococcus aureus plasmid pRW001 ALTERNATE_NAMES exfoliative toxin B ORGANISM #formal_name Staphylococcus aureus DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 18-Jun-1999 ACCESSIONS B26680; D26680 REFERENCE A26680 !$#authors Lee, C.Y.; Schmidt, J.J.; Johnson-Winegar, A.D.; Spero, L.; !1Iandolo, J.J. !$#journal J. Bacteriol. (1987) 169:3904-3909 !$#title Sequence determination and comparison of the exfoliative !1toxin A and toxin B genes from Staphylococcus aureus. !$#cross-references MUID:87307959; PMID:3040666 !$#accession B26680 !'##molecule_type DNA !'##residues 1-277 ##label LEE !'##cross-references GB:M17348; NID:g153011; PIDN:AAA26628.1; !1PID:g153012 !'##experimental_source strain UT0002 !$#accession D26680 !'##molecule_type protein !'##residues 32-71;203-250 ##label LEE2 GENETICS !$#gene etb !$#genome plasmid CLASSIFICATION #superfamily staphylococcal serine proteinase KEYWORDS scalded skin syndrome; toxin FEATURE !$1-31 #domain signal sequence #status predicted #label SIG\ !$32-277 #product epidermolytic toxin B #status predicted !8#label MAT SUMMARY #length 277 #molecular-weight 30765 #checksum 5589 SEQUENCE /// ENTRY A37942 #type complete TITLE prolyl oligopeptidase (EC 3.4.21.26) - pig ALTERNATE_NAMES prolyl endopeptidase ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A37942 REFERENCE A37942 !$#authors Rennex, D.; Hemmings, B.A.; Hofsteenge, J.; Stone, S.R. !$#journal Biochemistry (1991) 30:2195-2203 !$#title cDNA cloning of porcine brain prolyl endopeptidase and !1identification of the active-site seryl residue. !$#cross-references MUID:91152034; PMID:1900195 !$#accession A37942 !'##status preliminary !'##molecule_type mRNA !'##residues 1-710 ##label REN !'##cross-references GB:M64227; GB:J05311; NID:g164620; PIDN:AAA31110.1; !1PID:g164621 CLASSIFICATION #superfamily prolyl oligopeptidase KEYWORDS hydrolase; serine proteinase FEATURE !$554 #active_site Ser #status experimental SUMMARY #length 710 #molecular-weight 80769 #checksum 9650 SEQUENCE /// ENTRY JN0585 #type complete TITLE prolyl oligopeptidase (EC 3.4.21.26) - Aeromonas hydrophila (strain JM83) ALTERNATE_NAMES prolyl endopeptidase ORGANISM #formal_name Aeromonas hydrophila DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS JN0585; PN0498 REFERENCE JN0585 !$#authors Kanatani, A.; Yoshimoto, T.; Kitazono, A.; Kokubo, T.; !1Tsuru, D. !$#journal J. Biochem. (1993) 113:790-796 !$#title Prolyl endopeptidase from Aeromonas hydrophila: Cloning, !1sequencing, and expression of the enzyme gene, and !1characterization of the expressed enzyme. !$#cross-references MUID:93380910; PMID:8370677 !$#accession JN0585 !'##molecule_type DNA !'##residues 1-689 ##label KAN !'##cross-references DDBJ:D14005; NID:g216200; PIDN:BAA03105.1; !1PID:g216201 !$#accession PN0498 !'##molecule_type protein !'##residues !118-51;62-71;149-157;190-215;218-223;297-316;461-467;511-526; !1565-578;581-587;593-608;639-653 ##label KA2 CLASSIFICATION #superfamily prolyl oligopeptidase KEYWORDS hydrolase; serine proteinase FEATURE !$2-689 #product prolyl oligopeptidase #status predicted !8#label POP\ !$512,537,656 #active_site Asp, Ser, His #status predicted SUMMARY #length 689 #molecular-weight 76384 #checksum 7164 SEQUENCE /// ENTRY E64946 #type complete TITLE oligopeptidase B (EC 3.4.21.83) - Escherichia coli (strain K-12) ALTERNATE_NAMES proteinase II ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS E64946; JQ1151; PQ0214 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64946 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-686 ##label BLAT !'##cross-references GB:AE000278; GB:U00096; NID:g1788139; !1PIDN:AAC74915.1; PID:g1788150; UWGP:b1845 !'##experimental_source strain K-12, substrain MG1655 REFERENCE JQ1151 !$#authors Kanatani, A.; Masuda, T.; Shimoda, T.; Misoka, F.; Lin, !1X.S.; Yoshimoto, T.; Tsuru, D. !$#journal J. Biochem. (1991) 110:315-320 !$#title Protease II from Escherichia coli: sequencing and expression !1of the enzyme gene and characterization of the expressed !1enzyme. !$#cross-references MUID:92121142; PMID:1769955 !$#accession JQ1151 !'##molecule_type DNA !'##residues 1-681,'LRLRTKYFPDNVSVLNAAPGSCCPGY' ##label KAN1 !'##cross-references GB:D10976; GB:D01148; NID:g216623; PIDN:BAA01750.1; !1PID:g216624 !$#accession PQ0214 !'##molecule_type protein !'##residues !11-30;52-81;133-171;259-279;301-311;318-344;383-387;394-423; !1530-554;566-581;593-620;649-654;668-681 ##label KAN2 !'##experimental_source strain HB101 GENETICS !$#gene ptrB; tlp FUNCTION !$#description hydrolyzes peptide bonds of the carboxyl group of lysyl and !1argininyl residues !$#note catalytic activity seems to be provided by a charge relay !1system similar to that of the trypsin family of serine !1proteinases CLASSIFICATION #superfamily prolyl oligopeptidase KEYWORDS hydrolase; serine proteinase FEATURE !$204,617,652 #active_site His, Asp, His #status predicted\ !$532 #active_site Ser #status experimental SUMMARY #length 686 #molecular-weight 79490 #checksum 7193 SEQUENCE /// ENTRY PRSMAG #type complete TITLE streptogrisin A (EC 3.4.21.80) precursor - Streptomyces griseus ORGANISM #formal_name Streptomyces griseus DATE 24-Apr-1984 #sequence_revision 12-May-1994 #text_change 16-Aug-2002 ACCESSIONS A26974; A00963 REFERENCE A91842 !$#authors Henderson, G.; Krygsman, P.; Liu, C.J.; Davey, C.C.; Malek, !1L.T. !$#journal J. Bacteriol. (1987) 169:3778-3784 !$#title Characterization and structure of genes for proteases A and !1B from Streptomyces griseus. !$#cross-references MUID:87279934; PMID:3112129 !$#accession A26974 !'##molecule_type DNA !'##residues 1-297 ##label HEN !'##cross-references GB:M17103; NID:g153466; PIDN:AAA26818.1; !1PID:g153467 REFERENCE A00963 !$#authors Johnson, P.; Smillie, L.B. !$#journal FEBS Lett. (1974) 47:1-6 !$#title The amino acid sequence and predicted structure of !1Streptomyces griseus protease A. !$#cross-references MUID:75039088; PMID:4214713 !$#accession A00963 !'##molecule_type protein !'##residues 117-151,'S',152-183,'N',185-248,'Q',250-297 ##label JOH REFERENCE A37555 !$#authors Brayer, G.D.; Delbaere, L.T.J.; James, M.N.G. !$#journal J. Mol. Biol. (1978) 124:261-283 !$#title Molecular structure of crystalline Streptomyces griseus !1protease A at 2.8 angstroms resolution. !$#cross-references MUID:79050558; PMID:101674 !$#contents annotation; X-ray crystallography, 2.8 angstroms !$#note this is the second paper in a series GENETICS !$#gene sprA CLASSIFICATION #superfamily streptogrisin A KEYWORDS hydrolase; serine proteinase FEATURE !$1-38 #domain signal sequence #status predicted #label SIG\ !$39-116 #domain propeptide #status predicted #label PRO\ !$117-297 #product proteinase A #status experimental #label !8MAT\ !$130-150,247-274 #disulfide_bonds #status experimental\ !$149,171,253 #active_site His, Asp, Ser #status experimental SUMMARY #length 297 #molecular-weight 29663 #checksum 6181 SEQUENCE /// ENTRY PRSMBG #type complete TITLE streptogrisin B (EC 3.4.21.81) precursor - Streptomyces griseus ORGANISM #formal_name Streptomyces griseus DATE 24-Apr-1984 #sequence_revision 12-May-1994 #text_change 16-Aug-2002 ACCESSIONS B26974; A00964 REFERENCE A91842 !$#authors Henderson, G.; Krygsman, P.; Liu, C.J.; Davey, C.C.; Malek, !1L.T. !$#journal J. Bacteriol. (1987) 169:3778-3784 !$#title Characterization and structure of genes for proteases A and !1B from Streptomyces griseus. !$#cross-references MUID:87279934; PMID:3112129 !$#accession B26974 !'##molecule_type DNA !'##residues 1-299 ##label HEN !'##cross-references GB:M17104; NID:g153468; PIDN:AAA26819.1; !1PID:g153469 REFERENCE A00964 !$#authors Jurasek, L.; Carpenter, M.R.; Smillie, L.B.; Gertler, A.; !1Levy, S.; Ericsson, L.H. !$#journal Biochem. Biophys. Res. Commun. (1974) 61:1095-1100 !$#title Amino acid sequence of Streptomyces griseus protease B, a !1major component of pronase. !$#cross-references MUID:75127477; PMID:4218101 !$#accession A00964 !'##molecule_type protein !'##residues 115-153,'GT',156,'W',158-203,'B',205-292,'V',294-295,'A', !1297-299 ##label JUR !'##experimental_source strain K-1 !'##note disulfide bonds were determined REFERENCE A37556 !$#authors Delbaere, L.T.J.; Hutcheon, W.L.B.; James, M.N.G.; Thiessen, !1W.E. !$#journal Nature (1975) 257:758-763 !$#title Tertiary structural differences between microbial serine !1proteases and pancreatic serine enzymes. !$#cross-references MUID:76051298; PMID:1186854 !$#contents annotation; X-ray crystallography, 2.8 angstroms !$#note on the basis of the crystallographic analysis, Trp-43 and !1Val-126 were added to the sequence REFERENCE A37557 !$#authors Delbaere, L.T.J.; Brayer, G.D.; James, M.N.G. !$#journal Can. J. Biochem. (1979) 57:135-144 !$#title The 2.8-angstrom resolution structure of Streptomyces !1griseus protease b and its homology with alpha-chymotrypsin !1and Streptomyces griseus protease a. !$#cross-references MUID:79210651; PMID:110426 !$#contents annotation; X-ray crystallography, 2.8 angstroms !$#note on the basis of the crystallographic analysis, an alanine !1previously reported to precede Asn-44 was removed, as it was !1thought to be a degradation product of Trp-43 REFERENCE A37558 !$#authors Gertler, A. !$#journal FEBS Lett. (1974) 43:81-85 !$#title Inhibition of Streptomyces griseus protease B by peptide !1chloromethyl ketones: partial mapping of the binding site !1and identification of the reactive residue. !$#cross-references MUID:74302902; PMID:4212092 !$#contents annotation; active site His REFERENCE A37559 !$#authors Wahlby, S.; Engstrom, L. !$#journal Biochim. Biophys. Acta (1968) 151:402-408 !$#title Studies on Streptomyces griseus protease: II. The amino acid !1sequence around the reactive serine residue of DFP-sensitive !1components with esterase activity. !$#cross-references MUID:68124983; PMID:5636372 !$#contents annotation; active site Ser GENETICS !$#gene sprB CLASSIFICATION #superfamily streptogrisin A KEYWORDS hydrolase; serine proteinase FEATURE !$1-38 #domain signal sequence #status predicted #label SIG\ !$39-114 #domain propeptide #status predicted #label PRO\ !$115-299 #product proteinase B #status experimental #label !8MAT\ !$128-148,249-276 #disulfide_bonds #status experimental\ !$147,255 #active_site His, Ser #status experimental\ !$177 #active_site Asp #status predicted SUMMARY #length 299 #molecular-weight 30554 #checksum 2048 SEQUENCE /// ENTRY S37460 #type complete TITLE glutamyl endopeptidase II (EC 3.4.21.82) precursor [validated] - Streptomyces griseus ORGANISM #formal_name Streptomyces griseus DATE 19-May-2000 #sequence_revision 19-May-2000 #text_change 19-May-2000 ACCESSIONS S37460; S18322; S60516 REFERENCE S37460 !$#authors Suzuki, Y.; Yabuta, M.; Ohsuye, K. !$#submission submitted to the EMBL Data Library, August 1993 !$#accession S37460 !'##molecule_type DNA !'##residues 1-355 ##label SUZ !'##cross-references EMBL:X74868; NID:g404331; PIDN:CAA52860.1; !1PID:g404332 REFERENCE S18322 !$#authors Svendsen, I.; Jensen, M.R.; Breddam, K. !$#journal FEBS Lett. (1991) 292:165-167 !$#title The primary structure of the glutamic acid-specific protease !1of Streptomyces griseus. !$#cross-references MUID:92070480; PMID:1959600 !$#accession S18322 !'##molecule_type protein !'##residues 169-299,'G',301-344,'K',346-355,'L' ##label SVE !$#accession S60516 !'##molecule_type DNA !'##residues 211-289 ##label SVW CLASSIFICATION #superfamily streptogrisin A KEYWORDS hydrolase; serine proteinase FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-168 #domain propeptide #status predicted #label PRO\ !$169-355 #product glutamyl endopeptidase II #status !8experimental #label MAT\ !$182-202,305-331 #disulfide_bonds #status predicted\ !$201,230,311 #active_site His, Asp, Ser #status predicted SUMMARY #length 355 #molecular-weight 35380 #checksum 8591 SEQUENCE /// ENTRY S33321 #type complete TITLE glutamyl endopeptidase II (EC 3.4.21.82) precursor [similarity] - Streptomyces fradiae ORGANISM #formal_name Streptomyces fradiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S33321 REFERENCE S33321 !$#authors Kitadokoro, K.; Nakamura, E.; Tamaki, M.; Horii, T.; !1Okamoto, H.; Shin, M.; Sato, T.; Fujiwara, T.; Tsuzuki, H.; !1Yoshida, N.; Teraoka, H. !$#journal Biochim. Biophys. Acta (1993) 1163:149-157 !$#title Purification, characterization and molecular cloning of an !1acidic amino acid-specific proteinase from Streptomyces !1fradiae ATCC 14544. !$#cross-references MUID:93257481; PMID:8490047 !$#accession S33321 !'##status preliminary !'##molecule_type DNA !'##residues 1-357 ##label KIT !'##cross-references EMBL:D12470; NID:g217009; PIDN:BAA02038.1; !1PID:g217010 CLASSIFICATION #superfamily streptogrisin A KEYWORDS hydrolase; serine proteinase FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-170 #domain propeptide #status predicted #label PRO\ !$171-357 #product glutamyl endopeptidase II #status predicted !8#label MAT\ !$184-204,307-333 #disulfide_bonds #status predicted\ !$203,232,313 #active_site His, Asp, Ser #status predicted SUMMARY #length 357 #molecular-weight 35848 #checksum 1811 SEQUENCE /// ENTRY TRYXB4 #type complete TITLE alpha-lytic proteinase (EC 3.4.21.12) precursor - Lysobacter enzymogenes ORGANISM #formal_name Lysobacter enzymogenes DATE 24-Apr-1984 #sequence_revision 31-Mar-1992 #text_change 19-May-2000 ACCESSIONS A31772; A00965; JT0346 REFERENCE A31772 !$#authors Epstein, D.M.; Wensink, P.C. !$#journal J. Biol. Chem. (1988) 263:16586-16590 !$#title The alpha-lytic protease gene of Lysobacter enzymogenes. The !1nucleotide sequence predicts a large prepro-peptide with !1homology to pro-peptides of other chymotrypsin-like enzymes. !$#cross-references MUID:89034140; PMID:3053694 !$#accession A31772 !'##molecule_type DNA !'##residues 1-396 ##label EPS !'##cross-references GB:J04052 REFERENCE A00965 !$#authors Olson, M.O.J.; Nagabhushan, N.; Dzwiniel, M.; Smillie, L.B.; !1Whitaker, D.R. !$#journal Nature (1970) 228:438-442 !$#title Primary structure of alpha-lytic protease: a bacterial !1homologue of the pancreatic serine proteases. !$#cross-references MUID:71039222; PMID:5482494 !$#accession A00965 !'##molecule_type protein !'##residues 199-396 ##label OLS !'##experimental_source ATCC 29487 REFERENCE JT0346 !$#authors Silen, J.L.; McGrath, C.N.; Smith, K.R.; Agard, D.A. !$#journal Gene (1988) 69:237-244 !$#title Molecular analysis of the gene encoding alpha-lytic !1protease: evidence for a preproenzyme. !$#cross-references MUID:89172068; PMID:3234766 !$#accession JT0346 !'##molecule_type DNA !'##residues 1-25;138-396 ##label SIL !'##experimental_source ATCC 29487 !'##note this sequence differs from that shown between residues 26 and !1137 due to a frameshift error REFERENCE A37560 !$#authors Brayer, G.D.; Delbaere, L.T.J.; James, M.N.G. !$#journal J. Mol. Biol. (1979) 131:743-775 !$#title Molecular structure of the alpha-lytic protease from !1Myxobacter 495 at 2.8 angstroms resolution. !$#cross-references MUID:80074995; PMID:117110 !$#contents annotation; X-ray crystallography, 2.8 angstroms CLASSIFICATION #superfamily streptogrisin A KEYWORDS hydrolase; serine proteinase FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-198 #domain propeptide #status predicted #label PRO\ !$199-396 #product alpha-lytic proteinase #status experimental !8#label MAT\ !$215-235,299-309, !$335-368 #disulfide_bonds #status experimental\ !$234,261,341 #active_site His, Asp, Ser #status experimental SUMMARY #length 396 #molecular-weight 40521 #checksum 4675 SEQUENCE /// ENTRY A25852 #type complete TITLE trypsin (EC 3.4.21.4) I precursor [validated] - human ALTERNATE_NAMES trypsin, cationic; trypsinogen I ORGANISM #formal_name Homo sapiens #common_name man DATE 03-Mar-1994 #sequence_revision 03-Mar-1994 #text_change 08-Dec-2000 ACCESSIONS A25852; B61066; A43988 REFERENCE A91544 !$#authors Emi, M.; Nakamura, Y.; Ogawa, M.; Yamamoto, T.; Nishide, T.; !1Mori, T.; Matsubara, K. !$#journal Gene (1986) 41:305-310 !$#title Cloning, characterization and nucleotide sequences of two !1cDNAs encoding human pancreatic trypsinogens. !$#cross-references MUID:86221712; PMID:3011602 !$#accession A25852 !'##molecule_type mRNA !'##residues 1-247 ##label EMI !'##cross-references GB:M22612; NID:g521215; PIDN:AAA61231.1; !1PID:g521216 REFERENCE A61066 !$#authors Kimland, M.; Russick, C.; Marks, W.H.; Borgstroem, A. !$#journal Clin. Chim. Acta (1989) 184:31-46 !$#title Immunoreactive anionic and cationic trypsin in human serum. !$#cross-references MUID:90091010; PMID:2598466 !$#accession B61066 !'##molecule_type protein !'##residues 16-43 ##label KIM REFERENCE A43988 !$#authors Koivunen, E.; Huhtala, M.L.; Stenman, U.H. !$#journal J. Biol. Chem. (1989) 264:14095-14099 !$#title Human ovarian tumor-associated trypsin. Its purification and !1characterization from mucinous cyst fluid and identification !1as an activator of pro-urokinase. !$#cross-references MUID:89340515; PMID:2503510 !$#accession A43988 !'##molecule_type protein !'##residues 16-54 ##label KOI !'##experimental_source mucinous ovarian tumor cyst fluid GENETICS !$#gene GDB:PRSS1; TRY1 !'##cross-references GDB:119620; OMIM:276000 !$#map_position 7q35-7q35 !$#note The human genome contains at least ten trypsin genes or !1pseudogenes, at least two of which are transcribed in adult !1pancreas CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS hydrolase; pancreas; phosphoprotein; protein digestion; !1serine proteinase; zymogen FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-246 #product trypsinogen I #status experimental #label !8ZYM\ !$16-23 #domain activation peptide #status experimental !8#label APT\ !$24-246 #product trypsin I #status predicted #label ENZ\ !$24-239 #domain trypsin homology #label TRY\ !$30-160,48-64, !$139-206,171-185, !$196-220 #disulfide_bonds #status predicted\ !$63,107,200 #active_site His, Asp, Ser #status predicted\ !$75,77,80,85 #binding_site calcium (Glu, Asn, Val, Glu) #status !8predicted SUMMARY #length 247 #molecular-weight 26558 #checksum 6731 SEQUENCE /// ENTRY B25852 #type complete TITLE trypsin (EC 3.4.21.4) II precursor [validated] - human ALTERNATE_NAMES trypsin 2; trypsin, anionic; trypsinogen II ORGANISM #formal_name Homo sapiens #common_name man DATE 03-Mar-1994 #sequence_revision 03-Mar-1994 #text_change 08-Dec-2000 ACCESSIONS B25852; A61066; B43988 REFERENCE A91544 !$#authors Emi, M.; Nakamura, Y.; Ogawa, M.; Yamamoto, T.; Nishide, T.; !1Mori, T.; Matsubara, K. !$#journal Gene (1986) 41:305-310 !$#title Cloning, characterization and nucleotide sequences of two !1cDNAs encoding human pancreatic trypsinogens. !$#cross-references MUID:86221712; PMID:3011602 !$#accession B25852 !'##molecule_type mRNA !'##residues 1-247 ##label EMI !'##cross-references GB:M27602; NID:g521217; PIDN:AAA61232.1; !1PID:g521218 REFERENCE A61066 !$#authors Kimland, M.; Russick, C.; Marks, W.H.; Borgstroem, A. !$#journal Clin. Chim. Acta (1989) 184:31-46 !$#title Immunoreactive anionic and cationic trypsin in human serum. !$#cross-references MUID:90091010; PMID:2598466 !$#accession A61066 !'##molecule_type protein !'##residues 16-39,'X',41-42,'XXXX',47-49 ##label KIM REFERENCE A43988 !$#authors Koivunen, E.; Huhtala, M.L.; Stenman, U.H. !$#journal J. Biol. Chem. (1989) 264:14095-14099 !$#title Human ovarian tumor-associated trypsin. Its purification and !1characterization from mucinous cyst fluid and identification !1as an activator of pro-urokinase. !$#cross-references MUID:89340515; PMID:2503510 !$#accession B43988 !'##molecule_type protein !'##residues 16-49 ##label KOI !'##experimental_source mucinous ovarian tumor cyst fluid GENETICS !$#gene GDB:PRSS2; TRY2 !'##cross-references GDB:335289; OMIM:601564 !$#map_position 7q35-7q35 !$#note the human genome contains at least ten trypsin genes or !1pseudogenes, at least two of which are transcribed in adult !1pancreas CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS hydrolase; pancreas; protein digestion; serine proteinase; !1zymogen FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-246 #product trypsinogen II #status experimental #label !8ZYM\ !$16-23 #domain activation peptide #status experimental !8#label APT\ !$24-246 #product trypsin II #status predicted #label ENZ\ !$24-239 #domain trypsin homology #label TRY\ !$30-160,48-64, !$171-185,196-220 #disulfide_bonds #status predicted\ !$63,107,200 #active_site His, Asp, Ser #status predicted\ !$75,77,80,85 #binding_site calcium (Glu, Asn, Val, Glu) #status !8predicted SUMMARY #length 247 #molecular-weight 26488 #checksum 7483 SEQUENCE /// ENTRY TRRT1 #type complete TITLE trypsin (EC 3.4.21.4) I precursor - rat ALTERNATE_NAMES trypsinogen I ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 24-Sep-1999 ACCESSIONS B22657; A00948 REFERENCE A22657 !$#authors Craik, C.S.; Choo, Q.L.; Swift, G.H.; Quinto, C.; MacDonald, !1R.J.; Rutter, W.J. !$#journal J. Biol. Chem. (1984) 259:14255-14264 !$#title Structure of two related rat pancreatic trypsin genes. !$#cross-references MUID:85054880; PMID:6094547 !$#accession B22657 !'##molecule_type DNA !'##residues 1-246 ##label CRA !'##cross-references GB:J00778; NID:g206507; PIDN:AAA98518.1; !1PID:g206508 !'##note the authors translated the codon ATC for residue 6 as Leu and !1GAC for residue 170 as Asn REFERENCE A00948 !$#authors MacDonald, R.J.; Stary, S.J.; Swift, G.H. !$#journal J. Biol. Chem. (1982) 257:9724-9732 !$#title Two similar but nonallelic rat pancreatic trypsinogens. !1Nucleotide sequences of the cloned cDNAs. !$#cross-references MUID:82265624; PMID:6896710 !$#accession A00948 !'##molecule_type mRNA !'##residues 1-246 ##label MAC !'##cross-references GB:J00778; NID:g206507; PIDN:AAA98518.1; !1PID:g206508 GENETICS !$#introns 14/1; 67/2; 152/1; 197/3 CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS hydrolase; pancreas; protein digestion; serine proteinase; !1zymogen FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-23 #domain activation peptide #status predicted #label !8APT\ !$24-246 #product trypsin I #status predicted #label ENZ\ !$24-239 #domain trypsin homology #label TRY\ !$30-160,48-64, !$132-233,139-206, !$171-185 #disulfide_bonds #status predicted\ !$63,107,200 #active_site His, Asp, Ser #status predicted\ !$75,77,80,85 #binding_site calcium (Glu, Asn, Val, Glu) #status !8predicted SUMMARY #length 246 #molecular-weight 25959 #checksum 6732 SEQUENCE /// ENTRY TRRT2 #type complete TITLE trypsin (EC 3.4.21.4) II precursor - rat ALTERNATE_NAMES trypsinogen II ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 05-Apr-1983 #sequence_revision 30-Sep-1987 #text_change 18-Jul-1997 ACCESSIONS A22657; A00949 REFERENCE A22657 !$#authors Craik, C.S.; Choo, Q.L.; Swift, G.H.; Quinto, C.; MacDonald, !1R.J.; Rutter, W.J. !$#journal J. Biol. Chem. (1984) 259:14255-14264 !$#title Structure of two related rat pancreatic trypsin genes. !$#cross-references MUID:85054880; PMID:6094547 !$#accession A22657 !'##molecule_type DNA !'##residues 1-246 ##label CRA REFERENCE A00948 !$#authors MacDonald, R.J.; Stary, S.J.; Swift, G.H. !$#journal J. Biol. Chem. (1982) 257:9724-9732 !$#title Two similar but nonallelic rat pancreatic trypsinogens. !1Nucleotide sequences of the cloned cDNAs. !$#cross-references MUID:82265624; PMID:6896710 !$#accession A00949 !'##molecule_type mRNA !'##residues 9-246 ##label MAC COMMENT The trypsin II mRNA is present in much lower quantities than !1the trypsin I mRNA. GENETICS !$#introns 14/1; 67/2 CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS hydrolase; pancreas; protein digestion; serine proteinase; !1zymogen FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-23 #domain activation peptide #status predicted #label !8APT\ !$24-246 #product trypsin II #status predicted #label ENZ\ !$24-239 #domain trypsin homology #label TRY\ !$30-160,48-64, !$132-233,139-206, !$171-185 #disulfide_bonds #status predicted\ !$63,107,200 #active_site His, Asp, Ser #status predicted\ !$75,77,80,85 #binding_site calcium (Glu, Asn, Val, Glu) #status !8predicted SUMMARY #length 246 #molecular-weight 26243 #checksum 3816 SEQUENCE /// ENTRY TRBOTR #type complete TITLE trypsin (EC 3.4.21.4) precursor - bovine CONTAINS trypsinogen ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 24-Apr-1984 #sequence_revision 28-Feb-1986 #text_change 18-Jul-1997 ACCESSIONS A90164; A00946; S08774 REFERENCE A90164 !$#authors Mikes, O.; Holeysovsky, V.; Tomasek, V.; Sorm, F. !$#journal Biochem. Biophys. Res. Commun. (1966) 24:346-352 !$#title Covalent structure of bovine trypsinogen. The position of !1the remaining amides. !$#cross-references MUID:67168848; PMID:5967094 !$#accession A90164 !'##molecule_type protein !'##residues 1-57,'Q',59-67,'Q',69-150,'N',152-176,'N',178-229 ##label !1MIK REFERENCE A93755 !$#authors Hartley, B.S. !$#journal Philos. Trans. R. Soc. Lond. (1970) B257:77-87 !$#contents annotation; revisions REFERENCE A00950 !$#authors Titani, K.; Ericsson, L.H.; Neurath, H.; Walsh, K.A. !$#journal Biochemistry (1975) 14:1358-1366 !$#title Amino acid sequence of dogfish trypsin. !$#cross-references MUID:75146445; PMID:1092332 !$#contents annotation; revisions !$#note the sequence agrees with that shown REFERENCE A92954 !$#authors Bode, W.; Schwager, P. !$#journal J. Mol. Biol. (1975) 98:693-717 !$#title The refined crystal structure of bovine beta-trypsin at 1.8 !1angstrom resolution. !$#cross-references MUID:76072097; PMID:512 !$#contents annotation; X-ray crystallography; binding sites for !1calcium, substrate, and inhibitors COMMENT Trypsinogen is synthesized in the acinar cells of the !1pancreas. COMMENT Autocatalytic cleavage after Lys-6 leads to beta-trypsin by !1releasing a terminal hexapeptide. Subsequent cleavage after !1Lys-131 leads to alpha-trypsin. Further cleavage after !1Lys-176 yields pseudotrypsin. A cleavage may also occur !1after Arg-105. CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS hydrolase; pancreas; protein digestion; serine proteinase; !1zymogen FEATURE !$1-229 #product trypsinogen #status experimental #label ZYM\ !$1-6 #domain activation peptide #status experimental !8#label APT\ !$7-222 #domain trypsin homology #label TRY\ !$7-131,132-229 #product alpha-trypsin #status experimental #label !8MPT\ !$6-7 #cleavage_site Lys-Ile (enteropeptidase) #status !8experimental\ !$13-143,31-47, !$115-216,122-189, !$154-168,179-203 #disulfide_bonds #status experimental\ !$46,90,183 #active_site His, Asp, Ser #status experimental\ !$58,60,63,68 #binding_site calcium (Glu, Asn, Val, Glu) #status !8experimental\ !$131-132 #cleavage_site Lys-Ser (autolytic) #status !8experimental SUMMARY #length 229 #molecular-weight 23993 #checksum 2248 SEQUENCE /// ENTRY TRPGTR #type complete TITLE trypsin (EC 3.4.21.4) precursor - pig (tentative sequence) CONTAINS trypsinogen ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 31-Mar-2000 ACCESSIONS A90641; A90368; A00947 REFERENCE A90641 !$#authors Charles, M.; Rovery, M.; Guidoni, A.; Desnuelle, P. !$#journal Biochim. Biophys. Acta (1963) 69:115-129 !$#title Su le trypsinogene et la trypsine de porc. !$#accession A90641 !'##molecule_type protein !'##residues 1-10 ##label CHA REFERENCE A90368 !$#authors Hermodson, M.A.; Ericsson, L.H.; Neurath, H.; Walsh, K.A. !$#journal Biochemistry (1973) 12:3146-3153 !$#title Determination of the amino acid sequence of porcine trypsin !1by sequenator analysis. !$#cross-references MUID:73258692; PMID:4738933 !$#accession A90368 !'##molecule_type protein !'##residues 9-231 ##label HER !'##note at position 20, Ile and Val occur alternatively CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS hydrolase; pancreas; polymorphism; protein digestion; serine !1proteinase; zymogen FEATURE !$1-231 #product trypsinogen #status experimental #label ZYM\ !$1-8 #domain activation peptide #status experimental !8#label APT\ !$9-231 #product trypsin #status experimental #label MAT\ !$9-224 #domain trypsin homology #label TRY\ !$15-145,33-49, !$117-218,124-191, !$156-170,181-205 #disulfide_bonds #status predicted\ !$48,92,185 #active_site His, Asp, Ser #status predicted\ !$60,62,65,70 #binding_site calcium (Glu, Asn, Val, Glu) #status !8predicted SUMMARY #length 231 #molecular-weight 24409 #checksum 4251 SEQUENCE /// ENTRY TRDGC #type complete TITLE trypsin (EC 3.4.21.4) precursor, cationic - dog ALTERNATE_NAMES cationic trypsinogen ORGANISM #formal_name Canis lupus familiaris #common_name dog DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 18-Jun-1999 ACCESSIONS B26273 REFERENCE A26273 !$#authors Pinsky, S.D.; LaForge, K.S.; Scheele, G. !$#journal Mol. Cell. Biol. (1985) 5:2669-2676 !$#title Differential regulation of trypsinogen mRNA translation: !1full-length mRNA sequences encoding two oppositely charged !1trypsinogen isoenzymes in the dog pancreas. !$#cross-references MUID:86284628; PMID:3841794 !$#accession B26273 !'##molecule_type mRNA !'##residues 1-246 ##label PIN !'##cross-references GB:M11590; NID:g164096; PIDN:AAA30900.1; !1PID:g164097 CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS hydrolase; pancreas; protein digestion; serine proteinase; !1zymogen FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-23 #domain activation peptide #status predicted #label !8APT\ !$24-246 #product trypsin, cationic #status predicted #label !8ENZ\ !$24-239 #domain trypsin homology #label TRY\ !$30-160,48-64, !$132-233,139-206, !$171-185 #disulfide_bonds #status predicted\ !$63,107,200 #active_site His, Asp, Ser #status predicted\ !$75,77,80,85 #binding_site calcium (Glu, Asn, Val, Glu) #status !8predicted SUMMARY #length 246 #molecular-weight 26170 #checksum 7929 SEQUENCE /// ENTRY TRDG #type complete TITLE trypsin (EC 3.4.21.4) precursor, anionic - dog ALTERNATE_NAMES cationic trypsinogen ORGANISM #formal_name Canis lupus familiaris #common_name dog DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 18-Jun-1999 ACCESSIONS A26273 REFERENCE A26273 !$#authors Pinsky, S.D.; LaForge, K.S.; Scheele, G. !$#journal Mol. Cell. Biol. (1985) 5:2669-2676 !$#title Differential regulation of trypsinogen mRNA translation: !1full-length mRNA sequences encoding two oppositely charged !1trypsinogen isoenzymes in the dog pancreas. !$#cross-references MUID:86284628; PMID:3841794 !$#accession A26273 !'##molecule_type mRNA !'##residues 1-247 ##label PIN !'##cross-references GB:M11589; NID:g164094; PIDN:AAA30899.1; !1PID:g164095 CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS hydrolase; pancreas; protein digestion; serine proteinase; !1zymogen FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-23 #domain activation peptide #status predicted #label !8APT\ !$24-247 #product trypsin, anionic #status predicted #label !8ENZ\ !$24-239 #domain trypsin homology #label TRY\ !$30-160,48-64, !$132-233,139-206, !$171-185 #disulfide_bonds #status predicted\ !$63,107,200 #active_site His, Asp, Ser #status predicted\ !$75,77,80,85 #binding_site calcium (Glu, Asn, Val, Glu) #status !8predicted SUMMARY #length 247 #molecular-weight 26423 #checksum 8431 SEQUENCE /// ENTRY TRDFS #type complete TITLE trypsin (EC 3.4.21.4) precursor - spiny dogfish ALTERNATE_NAMES trypsinogen ORGANISM #formal_name Squalus acanthias #common_name spiny dogfish DATE 31-May-1979 #sequence_revision 31-May-1979 #text_change 21-Jan-1997 ACCESSIONS A00950; B27719 REFERENCE A00950 !$#authors Titani, K.; Ericsson, L.H.; Neurath, H.; Walsh, K.A. !$#journal Biochemistry (1975) 14:1358-1366 !$#title Amino acid sequence of dogfish trypsin. !$#cross-references MUID:75146445; PMID:1092332 !$#accession A00950 !'##molecule_type protein !'##residues 8-229 ##label TIT !'##note 119-Pro was also found REFERENCE A27719 !$#authors Hermodson, M.A.; Tye, R.W.; Reeck, G.R.; Neurath, H.; Walsh, !1K.A. !$#journal FEBS Lett. (1971) 14:222-224 !$#title Comparison of the amino terminal sequences of bovine, !1dogfish, and lungfish trypsinogens. !$#accession B27719 !'##molecule_type protein !'##residues 1-21 ##label HER CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS hydrolase; pancreas; polymorphism; protein digestion; serine !1proteinase; zymogen FEATURE !$1-7 #domain activation peptide #status experimental !8#label APT\ !$8-229 #product trypsin #status predicted #label MAT\ !$8-222 #domain trypsin homology #label TRY\ !$14-143,32-48, !$116-216,123-189, !$154-168,179-203 #disulfide_bonds #status predicted\ !$47,91,183 #active_site His, Asp, Ser #status predicted\ !$59,61,64,69 #binding_site calcium (Glu, Asp, Ala, Glu) #status !8predicted SUMMARY #length 229 #molecular-weight 24591 #checksum 7194 SEQUENCE /// ENTRY A32121 #type complete TITLE snake venom factor V activator (EC 3.4.21.95) alpha [validated] - Russell's viper ALTERNATE_NAMES factor V-activating proteinase alpha; proteinase RVV-V alpha ORGANISM #formal_name Vipera russellii siamensis DATE 19-May-2000 #sequence_revision 19-May-2000 #text_change 18-Jul-2001 ACCESSIONS A32121 REFERENCE A94684 !$#authors Tokunaga, F.; Nagasawa, K.; Tamura, S.; Miyata, T.; Iwanaga, !1S.; Kisiel, W. !$#journal J. Biol. Chem. (1988) 263:17471-17481 !$#title The factor V-activating enzyme (RVV-V) from Russell's viper !1venom. Identification of isoproteins RVV-V-alpha, -V-beta, !1and -V-gamma and their complete amino acid sequences. !$#cross-references MUID:89034273; PMID:3053712 !$#accession A32121 !'##molecule_type protein !'##residues 1-236 ##label TOK COMMENT This enzyme can fully activate human factor V by a single !1cleavage. CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS glycoprotein; hydrolase; serine proteinase FEATURE !$1-222 #domain trypsin homology #label TRY\ !$7-141,28-44,76-234, !$120-188,152-167, !$178-203 #disulfide_bonds #status predicted\ !$43,88,182 #active_site His, Asp, Ser #status predicted\ !$229 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 236 #molecular-weight 26182 #checksum 9897 SEQUENCE /// ENTRY B32121 #type complete TITLE snake venom factor V activator (EC 3.4.21.95) gamma [validated] - Russell's viper ALTERNATE_NAMES factor V-activating proteinase gamma; proteinase RVV-V beta ORGANISM #formal_name Vipera russellii siamensis DATE 19-May-2000 #sequence_revision 19-May-2000 #text_change 18-Jul-2001 ACCESSIONS B32121 REFERENCE A94684 !$#authors Tokunaga, F.; Nagasawa, K.; Tamura, S.; Miyata, T.; Iwanaga, !1S.; Kisiel, W. !$#journal J. Biol. Chem. (1988) 263:17471-17481 !$#title The factor V-activating enzyme (RVV-V) from Russell's viper !1venom. Identification of isoproteins RVV-V-alpha, -V-beta, !1and -V-gamma and their complete amino acid sequences. !$#cross-references MUID:89034273; PMID:3053712 !$#accession B32121 !'##molecule_type protein !'##residues 1-236 ##label TOK COMMENT This enzyme can fully activate human factor V by a single !1cleavage. CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS glycoprotein; hydrolase; serine proteinase FEATURE !$1-222 #domain trypsin homology #label TRY\ !$7-141,28-44,76-234, !$120-188,152-167, !$178-203 #disulfide_bonds #status predicted\ !$43,88,182 #active_site His, Asp, Ser #status predicted\ !$229 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 236 #molecular-weight 26167 #checksum 9216 SEQUENCE /// ENTRY JC4803 #type complete TITLE venombin A (EC 3.4.21.74) precursor [validated] - Korean viper ALTERNATE_NAMES alpha-fibrinogenase; calobin; thrombin-like enzyme ORGANISM #formal_name Agkistrodon caliginosus #common_name Korean viper DATE 19-May-2000 #sequence_revision 19-May-2000 #text_change 19-May-2000 ACCESSIONS JC4803 REFERENCE JC4803 !$#authors Hahn, B.S.; Yang, K.Y.; Park, E.M.; Chang, I.M.; Kim, Y.S. !$#journal J. Biochem. (1996) 119:835-843 !$#title Purification and molecular cloning of calobin, a !1thrombin-like enzyme from Agkistrodon caliginosus (Korean !1viper). !$#cross-references MUID:96389987; PMID:8797081 !$#accession JC4803 !'##molecule_type mRNA !'##residues 1-262 ##label HAH !'##cross-references GB:U32937; NID:g1389588; PIDN:AAC59906.1; !1PID:g1389589 !'##experimental_source venom !'##note part of this sequence, including the amino end of the mature !1protein, was determined by protein sequencing COMMENT This is a thrombin-like enzyme acting on fibrinogen to form !1fibrin and exhibiting arginine esterase activity. COMPLEX monomer CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS glycoprotein; hydrolase; serine proteinase; venom; zymogen FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-24 #domain activation peptide #status predicted #label !8ACP\ !$25-262 #product venombin A #status predicted #label MAT\ !$25-248 #domain trypsin homology #label TRY\ !$31-165,52-68, !$100-260,144-214, !$176-193,204-229 #disulfide_bonds #status predicted\ !$67,112,208 #active_site His, Asp, Ser #status predicted\ !$105 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 262 #molecular-weight 28908 #checksum 7577 SEQUENCE /// ENTRY JC2479 #type complete TITLE venombin B (EC 3.4.21.-) precursor [validated] - Chinese habu ALTERNATE_NAMES beta-fibrinogenase; fibrinogenolytic proteinase ORGANISM #formal_name Trimeresurus mucrosquamatus #common_name Chinese habu DATE 19-May-2000 #sequence_revision 19-May-2000 #text_change 19-May-2000 ACCESSIONS JC2479; A38940 REFERENCE JC2479 !$#authors Hung, C.C.; Huang, K.F.; Chiou, S.H. !$#journal Biochem. Biophys. Res. Commun. (1994) 205:1707-1715 !$#title Characterization of one novel venom protease with !1beta-fibrinogenase activity from the Taiwan habu !1(Trimeresurus mucrosquamatus): Purification and cDNA !1sequence analysis. !$#cross-references MUID:95110313; PMID:7811255 !$#accession JC2479 !'##molecule_type mRNA !'##residues 1-257 ##label HUN !'##cross-references GB:X83221; NID:g602595; PIDN:CAA58221.1; !1PID:g602596 !'##experimental_source venom !'##note part of this sequence, including the amino end of the mature !1protein, was determined by protein sequencing COMPLEX monomer CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS hydrolase; serine proteinase; venom; zymogen FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-24 #domain activation peptide #status predicted #label !8ACP\ !$25-257 #product venombin B #status predicted #label MAT\ !$25-243 #domain trypsin homology #label TRY\ !$31-162,49-65, !$97-255,141-209, !$173-188,199-224 #disulfide_bonds #status predicted\ !$64,109,203 #active_site His, Asp, Ser #status predicted SUMMARY #length 257 #molecular-weight 28099 #checksum 8201 SEQUENCE /// ENTRY A28169 #type complete TITLE venombin A (EC 3.4.21.74) precursor - barba amarilla ALTERNATE_NAMES alpha-fibrinogenase; B. atrox coagulant enzyme; batroxobin ORGANISM #formal_name Bothrops atrox #common_name barba amarilla, fer-de-lance DATE 19-May-2000 #sequence_revision 19-May-2000 #text_change 19-May-2000 ACCESSIONS A28169; A29135; S02110 REFERENCE A28169 !$#authors Itoh, N.; Tanaka, N.; Funakoshi, I.; Kawasaki, T.; Mihashi, !1S.; Yamashina, I. !$#journal J. Biol. Chem. (1988) 263:7628-7631 !$#title Organization of the gene for batroxobin, a thrombin-like !1snake venom enzyme. Homology with the trypsin/kallikrein !1gene family. !$#cross-references MUID:88227959; PMID:3163691 !$#accession A28169 !'##molecule_type DNA !'##residues 1-255 ##label ITO !'##cross-references GB:J02684; NID:g211023; PIDN:AAA48552.1; !1PID:g211024 REFERENCE A29135 !$#authors Itoh, N.; Tanaka, N.; Mihashi, S.; Yamashina, I. !$#journal J. Biol. Chem. (1987) 262:3132-3135 !$#title Molecular cloning and sequence analysis of cDNA for !1batroxobin, a thrombin-like snake venom enzyme. !$#cross-references MUID:87137585; PMID:3546302 !$#accession A29135 !'##molecule_type mRNA !'##residues 1-255 ##label IT2 !'##cross-references GB:J02684; NID:g211023; PIDN:AAA48552.1; !1PID:g211024 REFERENCE S02110 !$#authors Itoh, N.; Tanaka, N.; Funakoshi, I.; Kawasaki, T.; Mihashi, !1S.; Yamashina, I. !$#journal Nucleic Acids Res. (1988) 16:10377-10378 !$#title The complete nucleotide sequence of the gene for batroxobin, !1a thrombin-like snake venom enzyme. !$#cross-references MUID:89057491; PMID:3194214 !$#accession S02110 !'##molecule_type DNA !'##residues 1-255 ##label IT3 !'##cross-references EMBL:X12747; NID:g62463; PIDN:CAA31240.1; !1PID:g62464 GENETICS !$#introns 18/1; 68/2; 155/1; 199/3 CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS glycoprotein; hydrolase; serine proteinase; venom; zymogen FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-24 #domain activation peptide #status predicted #label !8ACP\ !$25-255 #product venombin A #status predicted #label MAT\ !$25-242 #domain trypsin homology #label TRY\ !$31-163,50-66, !$98-254,142-208, !$174-187,198-223 #disulfide_bonds #status predicted\ !$65,110,202 #active_site His, Asp, Ser #status predicted\ !$170,249 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 255 #molecular-weight 28188 #checksum 341 SEQUENCE /// ENTRY S36783 #type complete TITLE venombin A (EC 3.4.21.74) 2 precursor - Malayan pit viper ALTERNATE_NAMES alpha-fibrinogenase; ancrod ORGANISM #formal_name Calloselasma rhodostoma #common_name Malayan pit viper DATE 19-May-2000 #sequence_revision 19-May-2000 #text_change 19-May-2000 ACCESSIONS S36783 REFERENCE S36783 !$#authors Au, L.C.; Lin, S.B.; Chou, J.S.; Teh, G.W.; Chang, K.J.; !1Shih, C.M. !$#journal Biochem. J. (1993) 294:387-390 !$#title Molecular cloning and sequence analysis of the cDNA for !1ancrod, a thrombin-like enzyme from the venom of !1Calloselasma rhodostoma. !$#cross-references MUID:93384507; PMID:8373353 !$#accession S36783 !'##molecule_type mRNA !'##residues 1-258 ##label AUL !'##cross-references GB:L07308; NID:g403077; PIDN:AAA49195.1; !1PID:g403078 !'##note the sequence from Fig. 4 is inconsistent with that from Fig. 3 !1in having 63-Thr and 180-Glu CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS glycoprotein; hydrolase; serine proteinase; venom; zymogen FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-24 #domain activation peptide #status predicted #label !8ACP\ !$25-258 #product venombin A #status predicted #label MAT\ !$25-246 #domain trypsin homology #label TRY\ !$31-165,52-68, !$102-256,144-212, !$176-191,202-227 #disulfide_bonds #status predicted\ !$67,112,206 #active_site His, Asp, Ser #status predicted\ !$123,172,253 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 258 #molecular-weight 29145 #checksum 6692 SEQUENCE /// ENTRY JG0169 #type complete TITLE venombin A (EC 3.4.21.74) [validated] - sharp-nosed viper ALTERNATE_NAMES acutin; alpha-fibrinogenase ORGANISM #formal_name Agkistrodon acutus #common_name sharp-nosed viper DATE 19-May-2000 #sequence_revision 19-May-2000 #text_change 19-May-2000 ACCESSIONS JG0169 REFERENCE JG0169 !$#authors Pan, H.; Du, X.; Yang, G.; Zhou, Y.; Wu, X. !$#journal Biochem. Biophys. Res. Commun. (1999) 255:412-415 !$#title cDNA cloning and expression of acutin, a thrombin-like !1enzyme from Agkistrodon acutus. !$#cross-references MUID:99160877; PMID:10049722 !$#accession JG0169 !'##molecule_type DNA !'##residues 'M',1-233 ##label PAN !'##cross-references GB:AF089847; NID:g4378028; PIDN:AAD19350.1; !1PID:g4378029 !'##experimental_source venom !'##note part of this sequence, including the amino end of the mature !1protein, was determined by protein sequencing COMMENT This is a thrombin-like enzyme acting on fibrinogen to form !1fibrin and exhibiting arginine esterase activity. CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS glycoprotein; hydrolase; serine proteinase; venom FEATURE !$1-233 #product venombin A #status experimental #label MAT\ !$1-219 #domain trypsin homology #label TRY\ !$7-139,26-42,74-231, !$118-185,150-164, !$175-200 #disulfide_bonds #status predicted\ !$20,160 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$41,86,179 #active_site His, Asp, Ser #status predicted SUMMARY #length 233 #molecular-weight 25276 #checksum 5717 SEQUENCE /// ENTRY A54361 #type complete TITLE venombin A (EC 3.4.21.74) [validated] - jararaca ALTERNATE_NAMES alpha-fibrinogenase; bothrombin ORGANISM #formal_name Bothrops jararaca #common_name jararaca DATE 19-May-2000 #sequence_revision 19-May-2000 #text_change 19-May-2000 ACCESSIONS A54361 REFERENCE A54361 !$#authors Nishida, S.; Fujimura, Y.; Miura, S.; Ozaki, Y.; Usami, Y.; !1Suzuki, M.; Titani, K.; Yoshida, E.; Sugimoto, M.; Yoshioka, !1A.; Fukui, H. !$#journal Biochemistry (1994) 33:1843-1849 !$#title Purification and characterization of bothrombin, a !1fibrinogen-clotting serine protease from the venom of !1Bothrops jararaca. !$#cross-references MUID:94153945; PMID:8110787 !$#accession A54361 !'##molecule_type protein !'##residues 1-232 ##label NIS !'##experimental_source venom !'##note sequence extracted from NCBI backbone (NCBIP:143879) COMMENT This is a thrombin-like enzyme acting on fibrinogen to form !1fibrin and exhibiting arginine esterase activity. COMPLEX monomer CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS glycoprotein; hydrolase; serine proteinase; venom FEATURE !$1-232 #product venombin A #status experimental #label MAT\ !$1-218 #domain trypsin homology #label TRY\ !$7-139,26-42,74-230, !$118-184,150-163, !$174-199 #disulfide_bonds #status predicted\ !$41,86,178 #active_site His, Asp, Ser #status predicted\ !$98,146,225 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 232 #molecular-weight 25584 #checksum 6922 SEQUENCE /// ENTRY S20407 #type complete TITLE venombin A (EC 3.4.21.74) 1 [validated] - Malayan pit viper ALTERNATE_NAMES alpha-fibrinogenase; ancrod ORGANISM #formal_name Calloselasma rhodostoma #common_name Malayan pit viper DATE 19-May-2000 #sequence_revision 19-May-2000 #text_change 19-May-2000 ACCESSIONS S20407 REFERENCE S20407 !$#authors Burkhart, W.; Smith, G.F.H.; Su, J.L.; Parikh, I.; LeVine !1III, H. !$#journal FEBS Lett. (1992) 297:297-301 !$#title Amino acid sequence determination of Ancrod, the !1thrombin-like alpha-fibrinogenase from the venom of !1Akistrodon rhodostoma. !$#cross-references MUID:92183814; PMID:1544412 !$#accession S20407 !'##molecule_type protein !'##residues 1-234 ##label BUR !'##experimental_source venom !'##note the source is given as Akistrodon rhodostoma COMMENT The sequence from Fig. 3 is inconsistent with that from Fig. !12 in having 58-His and 217-Asp. COMMENT This is a thrombin-like enzyme acting on fibrinogen to form !1fibrin and exhibiting arginine esterase activity. CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS glycoprotein; hydrolase; serine proteinase; venom FEATURE !$1-234 #product venombin A #status experimental #label MAT\ !$1-222 #domain trypsin homology #label TRY\ !$7-141,28-44,78-232, !$120-188,152-167, !$178-203 #disulfide_bonds #status predicted\ !$23,79,99,148,229 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$43,88,182 #active_site His, Asp, Ser #status predicted SUMMARY #length 234 #molecular-weight 26570 #checksum 5874 SEQUENCE /// ENTRY S35689 #type complete TITLE venombin A (EC 3.4.21.74) [validated] - bushmaster ALTERNATE_NAMES alpha-fibrinogenase; gyroxin analog ORGANISM #formal_name Lachesis muta muta #common_name bushmaster DATE 19-May-2000 #sequence_revision 19-May-2000 #text_change 19-May-2000 ACCESSIONS S35689; A32415 REFERENCE S35689 !$#authors Magalhaes, A.; da Fonseca, B.C.B.; Diniz, C.R.; Gilroy, J.; !1Richardson, M. !$#journal FEBS Lett. (1993) 329:116-120 !$#title The complete amino acid sequence of a thrombin-like enzyme/ !1gyroxin analogue from venom of the bushmaster snake !1(Lachesis muta muta). !$#cross-references MUID:93359030; PMID:8354384 !$#accession S35689 !'##molecule_type protein !'##residues 1-228 ##label MAG !'##experimental_source venom REFERENCE A32415 !$#authors da Silva, N.J.; Aird, S.D.; Seebart, C.; Kaiser, I.I. !$#journal Toxicon (1989) 27:763-771 !$#title A gyroxin analog from the venom of the bushmaster (Lachesis !1muta muta). !$#cross-references MUID:89388830; PMID:2781576 !$#accession A32415 !'##molecule_type protein !'##residues 1-25 ##label DAS !'##experimental_source venom COMMENT This is a thrombin-like enzyme acting on fibrinogen to form !1fibrin and exhibiting arginine esterase activity. CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS glycoprotein; hydrolase; serine proteinase; venom FEATURE !$1-228 #product venombin A #status experimental #label MAT\ !$1-217 #domain trypsin homology #label TRY\ !$7-138,28-44,78-227, !$117-183,149-162, !$173-198 #disulfide_bonds #status predicted\ !$43,88,177 #active_site His, Asp, Ser #status predicted\ !$45,81,145,224 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 228 #molecular-weight 25629 #checksum 5927 SEQUENCE /// ENTRY S65621 #type complete TITLE venombin AB (EC 3.4.21.55) [validated] - cantil ALTERNATE_NAMES alpha/beta-fibrinogenase; thrombin-like proteinase bilineobin ORGANISM #formal_name Agkistrodon bilineatus #common_name cantil DATE 19-May-2000 #sequence_revision 19-May-2000 #text_change 19-May-2000 ACCESSIONS S65621; A45368 REFERENCE S65621 !$#authors Nikai, T.; Ohara, A.; Komori, Y.; Fox, J.W.; Sugihara, H. !$#journal Arch. Biochem. Biophys. (1995) 318:89-96 !$#title Primary structure of a coagulant enzyme, bilineobin, from !1Agkistrodon bilineatus venom. !$#cross-references MUID:95243661; PMID:7726578 !$#accession S65621 !'##molecule_type protein !'##residues 1-235 ##label NIK !'##experimental_source venom REFERENCE A45368 !$#authors Komori, Y.; Nikai, T.; Ohara, A.; Yagihashi, S.; Sugihara, !1H. !$#journal Toxicon (1993) 31:257-270 !$#title Effect of bilineobin, a thrombin-like proteinase from the !1venom of common cantil (Agkistrodon bilineatus). !$#cross-references MUID:93227264; PMID:8470131 !$#accession A45368 !'##molecule_type protein !'##residues 'V',2-6,'X',8-22,'X',24 ##label KOM !'##experimental_source venom !'##note sequence extracted from NCBI backbone (NCBIP:129510) COMMENT This is a thrombin-like enzyme acting on fibrinogen to form !1fibrin and exhibiting arginine esterase activity. CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS glycoprotein; hydrolase; serine proteinase; venom FEATURE !$1-235 #product venombin A #status experimental #label MAT\ !$1-222 #domain trypsin homology #label TRY\ !$7-141,28-44,78-234, !$120-188,152-167, !$178-203 #disulfide_bonds #status experimental\ !$43,88,182 #active_site His, Asp, Ser #status predicted\ !$45,57,81,132,148, !$229 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 235 #molecular-weight 26478 #checksum 9520 SEQUENCE /// ENTRY A41456 #type complete TITLE venombin A (EC 3.4.21.74) [validated] - habu ALTERNATE_NAMES alpha-fibrinogenase; flavoxobin ORGANISM #formal_name Trimeresurus flavoviridis #common_name habu DATE 19-May-2000 #sequence_revision 19-May-2000 #text_change 19-May-2000 ACCESSIONS A41456 REFERENCE A41456 !$#authors Shieh, T.C.; Kawabata, S.; Kihara, H.; Ohno, M.; Iwanaga, S. !$#journal J. Biochem. (1988) 103:596-605 !$#title Amino acid sequence of a coagulant enzyme, flavoxobin, from !1Trimeresurus flavoviridis venom. !$#cross-references MUID:89008159; PMID:3170503 !$#accession A41456 !'##molecule_type protein !'##residues 1-236 ##label SHI !'##experimental_source venom CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS hydrolase; serine proteinase; venom FEATURE !$1-236 #product venombin A #status experimental #label MAT\ !$1-222 #domain trypsin homology #label TRY\ !$7-141,28-44,76-234, !$120-188,152-167, !$178-203 #disulfide_bonds #status predicted\ !$43,88,182 #active_site His, Asp, Ser #status predicted SUMMARY #length 236 #molecular-weight 25741 #checksum 5450 SEQUENCE /// ENTRY TRCY1 #type complete TITLE trypsin (EC 3.4.21.4) I - broad-fingered crayfish ORGANISM #formal_name Astacus astacus, Astacus fluviatilis #common_name broad-fingered crayfish DATE 18-Apr-1984 #sequence_revision 18-Apr-1984 #text_change 18-Jul-1997 ACCESSIONS A00951 REFERENCE A00951 !$#authors Titani, K.; Sasagawa, T.; Woodbury, R.G.; Ericsson, L.H.; !1Dorsam, H.; Kraemer, M.; Neurath, H.; Zwilling, R. !$#journal Biochemistry (1983) 22:1459-1465 !$#title Amino acid sequence of crayfish Astacus fluviatilis trypsin !1I-f. !$#cross-references MUID:83178967; PMID:6838862 !$#accession A00951 !'##molecule_type protein !'##residues 1-237 ##label TIT COMMENT Trypsin I is one of five forms of the enzyme known to be !1present in crayfish. This protein is more acidic than !1mammalian trypsin. CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS hydrolase; protein digestion; serine proteinase FEATURE !$1-232 #domain trypsin homology #label TRY\ !$30-46,159-174, !$185-213 #disulfide_bonds #status predicted\ !$45,96,189 #active_site His, Asp, Ser #status predicted SUMMARY #length 237 #molecular-weight 25021 #checksum 7759 SEQUENCE /// ENTRY TRFF #type complete TITLE trypsin-like proteinase (EC 3.4.21.-) precursor - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 21-Jun-2002 ACCESSIONS A23493 REFERENCE A23493 !$#authors Davis, C.A.; Riddell, D.C.; Higgins, M.J.; Holden, J.J.A.; !1White, B.N. !$#journal Nucleic Acids Res. (1985) 13:6605-6619 !$#title A gene family in Drosophila melanogaster coding for !1trypsin-like enzymes. !$#cross-references MUID:86041859; PMID:2414727 !$#accession A23493 !'##molecule_type DNA !'##residues 1-256 ##label DAV !'##cross-references GB:X02989; NID:g8741; PIDN:CAA26732.1; PID:g8742 COMMENT This enzyme is synthesized in the midgut of both larvae and !1adults, primarily in the ventriculus and gastric caeca. GENETICS !$#gene FlyBase:alpha-Try !'##cross-references FlyBase:FBgn0003863 CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS hydrolase; insect midgut; protein digestion; serine !1proteinase FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-30 #domain propeptide #status predicted #label PRO\ !$31-256 #product trypsin-like proteinase #status predicted !8#label TRL\ !$31-249 #domain trypsin homology #label TRY\ !$71,116,210 #active_site His, Asp, Ser #status predicted SUMMARY #length 256 #molecular-weight 26041 #checksum 6757 SEQUENCE /// ENTRY TRWV3Y #type complete TITLE trypsin-like proteinase (EC 3.4.21.-) 3A1 precursor - yellow fever mosquito ORGANISM #formal_name Aedes aegypti #common_name yellow fever mosquito DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 18-Jun-1999 ACCESSIONS S19890 REFERENCE S19890 !$#authors Kalhok, S.; Tabak, L.M.; Prosser, D.E.; Downe, A.E.R.; !1White, B.N. !$#submission submitted to the EMBL Data Library, February 1992 !$#description Isolation, sequencing and characterization of 2 cDNA clones !1coding for trypsin-like enzymes in the midgut of Aedes !1aegypi. !$#accession S19890 !'##molecule_type mRNA !'##residues 1-254 ##label KAL !'##cross-references EMBL:X64362; NID:g5561; PIDN:CAA45714.1; PID:g5562 CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS hydrolase; insect midgut; protein digestion; serine !1proteinase FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-27 #domain propeptide #status predicted #label PRO\ !$28-254 #product trypsin-like proteinase 3A1 #status !8predicted #label MAT\ !$28-248 #domain trypsin homology #label TRY\ !$53-69,178-194, !$205-229 #disulfide_bonds #status predicted\ !$68,113,209 #active_site His, Asp, Ser #status predicted SUMMARY #length 254 #molecular-weight 26939 #checksum 4392 SEQUENCE /// ENTRY TRWV5Y #type fragment TITLE trypsin-like proteinase (EC 3.4.21.-) 5G1 precursor - yellow fever mosquito (fragment) ORGANISM #formal_name Aedes aegypti #common_name yellow fever mosquito DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 18-Jun-1999 ACCESSIONS S19891 REFERENCE S19890 !$#authors Kalhok, S.; Tabak, L.M.; Prosser, D.E.; Downe, A.E.R.; !1White, B.N. !$#submission submitted to the EMBL Data Library, February 1992 !$#description Isolation, sequencing and characterization of 2 cDNA clones !1coding for trypsin-like enzymes in the midgut of Aedes !1aegypi. !$#accession S19891 !'##molecule_type mRNA !'##residues 1-238 ##label KAL !'##cross-references EMBL:X64363; NID:g5563; PIDN:CAA45715.1; PID:g5564 CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS hydrolase; insect midgut; protein digestion; serine !1proteinase FEATURE !$1-11 #domain signal sequence and propeptide (fragment) !8#status predicted #label SIG\ !$12-238 #product trypsin-like proteinase 5G1 #status !8predicted #label MAT\ !$12-232 #domain trypsin homology #label TRY\ !$38-54,162-178, !$189-213 #disulfide_bonds #status predicted\ !$53,97,193 #active_site His, Asp, Ser #status predicted SUMMARY #length 238 #checksum 56 SEQUENCE /// ENTRY KQHU #type complete TITLE tissue kallikrein (EC 3.4.21.35) precursor [validated] - human ALTERNATE_NAMES kininogenin; pancreatic kallikrein; salivary kallikrein; urinary kallikrein ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 08-Dec-2000 ACCESSIONS A24696; A28678; A23587; S05642; JX0040; A04628; A60248; !1JK0218; A60251; A60250; S33773; S55240; S55241; A27256; !1A60247; JT0010; S03367 REFERENCE A24696 !$#authors Fukushima, D.; Kitamura, N.; Nakanishi, S. !$#journal Biochemistry (1985) 24:8037-8043 !$#title Nucleotide sequence of cloned cDNA for human pancreatic !1kallikrein. !$#cross-references MUID:86131629; PMID:3004571 !$#accession A24696 !'##molecule_type mRNA !'##residues 1-262 ##label FUK !'##cross-references GB:M25629; NID:g186652; PIDN:AAA36136.1; !1PID:g186653 REFERENCE A28678 !$#authors Evans, B.A.; Yun, Z.X.; Close, J.A.; Tregear, G.W.; !1Kitamura, N.; Nakanishi, S.; Callen, D.F.; Baker, E.; !1Hyland, V.J.; Sutherland, G.R.; Richards, R.I. !$#journal Biochemistry (1988) 27:3124-3129 !$#title Structure and chromosomal localization of the human renal !1kallikrein gene. !$#cross-references MUID:88269498; PMID:2898948 !$#accession A28678 !'##molecule_type DNA !'##residues 1-185,'K',187-262 ##label EVA !'##cross-references GB:M33105; GB:M33106; GB:M33107; GB:M33108; !1GB:M33109; NID:g186649; PIDN:AAA59455.1; PID:g186651 REFERENCE A23587 !$#authors Baker, A.R.; Shine, J. !$#journal DNA (1985) 4:445-450 !$#title Human kidney kallikrein: cDNA cloning and sequence analysis. !$#cross-references MUID:86135264; PMID:3853975 !$#accession A23587 !'##molecule_type mRNA !'##residues 17-262 ##label BAK REFERENCE S05642 !$#authors Angermann, A.; Bergmann, C.; Appelhans, H. !$#journal Biochem. J. (1989) 262:787-793 !$#title Cloning and expression of human salivary-gland kallikrein in !1Escherichia coli. !$#cross-references MUID:90073574; PMID:2686621 !$#accession S05642 !'##molecule_type mRNA !'##residues 1-144,'E',146-185,'K',187-262 ##label ANG !'##cross-references EMBL:X13561; NID:g34026; PIDN:CAA31912.1; !1PID:g34027 !'##note the authors translated the codon GGT for residue 226 as Glu REFERENCE JX0040 !$#authors Takahashi, S.; Irie, A.; Miyake, Y. !$#journal J. Biochem. (1988) 104:22-29 !$#title Primary structure of human urinary prokallikrein. !$#cross-references MUID:89123217; PMID:3065335 !$#accession JX0040 !'##molecule_type protein !'##residues 18-262 ##label TAK REFERENCE A04628 !$#authors Lottspeich, F.; Geiger, R.; Henschen, A.; Kutzbach, C. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1979) 360:1947-1950 !$#title N-terminal amino acid sequence of human urinary kallikrein !1homology with other serine proteases. !$#cross-references MUID:80114126; PMID:393608 !$#accession A04628 !'##molecule_type protein !'##residues 25-55 ##label LOT !'##experimental_source urine REFERENCE A60248 !$#authors Kellermann, J.; Lottspeich, F.; Geiger, R.; Deutzmann, R. !$#journal Adv. Exp. Med. Biol. (1989) 247A:519-525 !$#title Human urinary kallikrein: amino acid sequence and !1carbohydrate attachment sites. !$#cross-references MUID:90102100; PMID:2603817 !$#accession A60248 !'##molecule_type protein !'##residues 25-262 ##label KEL REFERENCE JK0218 !$#authors Lu, H.S.; Lin, F.K.; Chao, L.; Chao, J. !$#journal Int. J. Pept. Protein Res. (1989) 33:237-249 !$#title Human urinary kallikrein: complete amino acid sequence and !1sites of glycosylation. !$#cross-references MUID:89326688; PMID:2666327 !$#accession JK0218 !'##molecule_type protein !'##residues 25-185,'K',187-262 ##label LUH REFERENCE A60251 !$#authors Terashima, H.; Atomi, Y.; Ohnishi, N.; Kuroda, A.; Morioka, !1Y.; Ikekita, M.; Aoki, K.; Kamada, M.; Kizuki, K.; Moriya, !1H. !$#journal Adv. Exp. Med. Biol. (1989) 247B:177-182 !$#title Characterization of human pancreatic kallikrein. !$#cross-references MUID:90119035; PMID:2610057 !$#accession A60251 !'##molecule_type protein !'##residues 25-30,'X',32-37 ##label TER REFERENCE A60250 !$#authors Matsuda, Y.; Fujimoto, Y.; Watanabe, Y.; Obara, T.; Akihama, !1S. !$#journal Adv. Exp. Med. Biol. (1989) 247B:169-175 !$#title Human salivary kallikrein and submaxillary glands !1kallikreins. !$#cross-references MUID:90119034; PMID:2610056 !$#accession A60250 !'##molecule_type protein !'##residues 25-30,'X',32-33,'X',35-43,'X',45,'X' ##label MTS !'##experimental_source saliva REFERENCE S33772 !$#authors Lin, F.K.; Lin, C.H.; Chou, C.C.; Chen, K.; Lu, H.S.; !1Bacheller, W.; Herrera, C.; Jones, T.; Chao, J.; Chao, L. !$#journal Biochim. Biophys. Acta (1993) 1173:325-328 !$#title Molecular cloning and sequence analysis of the monkey and !1human tissue kallikrein genes. !$#cross-references MUID:93305727; PMID:7916636 !$#accession S33773 !'##status preliminary !'##molecule_type DNA !'##residues 1-185,'K',187-262 ##label LIN !'##cross-references GB:L10038 REFERENCE S55240 !$#authors Chen, L.M.; Richards, G.P.; Chao, L.; Chao, J. !$#journal Biochem. J. (1995) 307:481-486 !$#title Molecular cloning, purification and in situ localization of !1human colon kallikrein. !$#cross-references MUID:95251612; PMID:7733886 !$#accession S55240 !'##status preliminary !'##molecule_type mRNA !'##residues 1-48 ##label CHE !'##cross-references GB:S77952; NID:g999010; PIDN:AAB34120.1; !1PID:g999011 !$#accession S55241 !'##status preliminary !'##molecule_type protein !'##residues 25-34 ##label CH2 COMMENT Tissue kallikreins cleave Met-Lys and Arg-Ser bonds in !1kininogen to release lysyl-bradykinin (kallidin). COMMENT The substitution of Lys for Glu in references A28678, !1S05642, and JK0218 may represent a common polymorphism. GENETICS !$#gene GDB:KLK1 !'##cross-references GDB:120118; OMIM:147910 !$#map_position 19q13.3-19q13.4 !$#introns 16/1; 69/2; 166/1; 211/3 CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS glycoprotein; hydrolase; pancreas; serine proteinase; !1zymogen FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-24 #domain activation peptide #status experimental !8#label ACT\ !$25-262 #product tissue kallikrein #status experimental !8#label MAT\ !$25-254 #domain trypsin homology #label TRY\ !$65,120,214 #active_site His, Asp, Ser #status predicted\ !$93,104,167 #binding_site carbohydrate (Ser) (covalent) #status !8experimental\ !$102,108,165 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 262 #molecular-weight 28889 #checksum 6909 SEQUENCE /// ENTRY KQPG #type complete TITLE tissue kallikrein (EC 3.4.21.35), pancreatic - pig (tentative sequence) ALTERNATE_NAMES glandular kallikrein; kininogenin ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 24-Apr-1984 #sequence_revision 31-Dec-1993 #text_change 31-Mar-2000 ACCESSIONS A00938; A92895 REFERENCE A90015 !$#authors Tschesche, H.; Mair, G.; Godec, G.; Fiedler, F.; Ehret, W.; !1Hirschauer, C.; Lemon, M.; Fritz, H.; Schmidt-Kastner, G.; !1Kutzbach, C. !$#journal Adv. Exp. Med. Biol. (1979) 120:245-260 !$#title The primary structure of porcine glandular kallikreins. !$#accession A00938 !'##molecule_type protein !'##residues 1-49,'GWL',53-134,'D',136-156,'H',158,'B',160-224,'B', !1226-232 ##label TSC !'##note the residue identified as 225-Asx is bound to carbohydrate; !1therefore, we have shown it as Asn REFERENCE A92895 !$#authors Bode, W.; Chen, Z.; Bartels, K.; Kutzbach, C.; !1Schmidt-Kastner, G.; Bartunik, H. !$#journal J. Mol. Biol. (1983) 164:237-282 !$#title Refined 2 angstrom X-ray crystal structure of porcine !1pancreatic kallikrein A, a specific trypsin-like serine !1proteinase. Crystallization, structure determination, !1crystallographic refinement, structure and its comparison !1with bovine trypsin. !$#cross-references MUID:83189107; PMID:6551452 !$#contents X-ray crystallography, 2 angstroms !$#accession A92895 !'##molecule_type protein !'##residues 1-224,'B',226-232 ##label BOD COMMENT The protein consists of two chains, A and B, held together !1by disulfide bonds. COMMENT Tissue kallikreins cleave Met-Lys and Arg-Ser bonds in !1kininogen to release lysyl-bradykinin (kallidin). CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS glycoprotein; hydrolase; pancreas; serine proteinase FEATURE !$1-224 #domain trypsin homology #label TRY\ !$1-80 #product tissue kallikrein chain A #status !8experimental #label MPTA\ !$79-82 #region autolysis loop\ !$81-232 #product tissue kallikrein chain B #status !8experimental #label MPTB\ !$7-144,26-42, !$121-190,155-169, !$180-205 #disulfide_bonds #status experimental\ !$41,89,184 #active_site His, Asp, Ser #status experimental\ !$78 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$225 #binding_site carbohydrate (Asn) (covalent) (partial) !8#status experimental SUMMARY #length 232 #molecular-weight 25589 #checksum 2761 SEQUENCE /// ENTRY KQMSM #type fragment TITLE tissue kallikrein (EC 3.4.21.35), submandibular - mouse (fragment) ALTERNATE_NAMES glandular kallikrein; kininogenin ORGANISM #formal_name Mus musculus #common_name house mouse DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 16-Jun-2000 ACCESSIONS A00939 REFERENCE A00939 !$#authors Richards, R.I.; Catanzaro, D.F.; Mason, A.J.; Morris, B.J.; !1Baxter, J.D.; Shine, J. !$#journal J. Biol. Chem. (1982) 257:2758-2761 !$#title Mouse glandular kallikrein genes. Nucleotide sequence of !1cloned cDNA coding for a member of the kallikrein arginyl !1esteropeptidase group of serine proteases. !$#cross-references MUID:82142394; PMID:6174512 !$#accession A00939 !'##molecule_type mRNA !'##residues 1-149 ##label RIC !'##cross-references GB:V00828; GB:J00389; NID:g52773; PIDN:CAA24211.1; !1PID:g1334112 !'##experimental_source Quakenbush inbred strain COMMENT Tissue kallikreins cleave Met-Lys and Arg-Ser bonds in !1kininogen to release lysyl-bradykinin (kallidin). GENETICS !$#map_position 7 CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS hydrolase; saliva; serine proteinase; submandibular gland FEATURE !$1-141 #domain trypsin homology (fragment) #label TRY\ !$8,101 #active_site Asp, Ser #status predicted\ !$40-107,72-86,97-122 #disulfide_bonds #status predicted SUMMARY #length 149 #checksum 8420 SEQUENCE /// ENTRY EGMSB #type complete TITLE tissue kallikrein (EC 3.4.21.35) mGK-26 precursor - mouse ALTERNATE_NAMES epidermal growth factor-binding protein type B 2; prorenin-converting enzyme 2 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 18-Jun-1999 ACCESSIONS A00940; S19310 REFERENCE A00940 !$#authors Lundgren, S.; Ronne, H.; Rask, L.; Peterson, P.A. !$#journal J. Biol. Chem. (1984) 259:7780-7784 !$#title Sequence of an epidermal growth factor-binding protein. !$#cross-references MUID:84239721; PMID:6330081 !$#accession A00940 !'##molecule_type mRNA !'##residues 1-261 ##label LUN !'##cross-references GB:K01831; NID:g192995; PIDN:AAA37540.1; !1PID:g309211 REFERENCE S19310 !$#authors Kim, W.S.; Nakayama, K.; Murakami, K. !$#journal FEBS Lett. (1991) 293:142-144 !$#title The presence of two types of prorenin converting enzymes in !1the mouse submandibular gland. !$#cross-references MUID:92070545; PMID:1959648 !$#accession S19310 !'##molecule_type mRNA !'##residues 1-261 ##label KIM !'##cross-references GB:X63327; NID:g53773; PIDN:CAA44931.1; PID:g53774 CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS hydrolase; serine proteinase FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-24 #domain activation peptide #status predicted #label !8ACT\ !$25-261 #product tissue kallikrein mGK-26 #status predicted !8#label MAT\ !$25-253 #domain trypsin homology #label TRY\ !$31-173,50-66, !$152-219,184-198, !$209-234 #disulfide_bonds #status predicted\ !$65,120,213 #active_site His, Asp, Ser #status predicted SUMMARY #length 261 #molecular-weight 28463 #checksum 8469 SEQUENCE /// ENTRY KQMS1 #type complete TITLE tissue kallikrein (EC 3.4.21.35) mGK-1 precursor, submandibular - mouse ALTERNATE_NAMES glandular kallikrein; kininogenin ORGANISM #formal_name Mus musculus #common_name house mouse DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 24-Sep-1999 ACCESSIONS A00941 REFERENCE A00941 !$#authors Mason, A.J.; Evans, B.A.; Cox, D.R.; Shine, J.; Richards, !1R.I. !$#journal Nature (1983) 303:300-307 !$#title Structure of mouse kallikrein gene family suggests a role in !1specific processing of biologically active peptides. !$#cross-references MUID:83219214; PMID:6602295 !$#accession A00941 !'##molecule_type DNA !'##residues 1-261 ##label MAS !'##cross-references GB:V00829; NID:g52775; PIDN:CAA24213.1; PID:g52776 !'##experimental_source Quakenbush inbred strain COMMENT mGK-1 belongs to a family of 25 to 30 homologous kallikrein !1genes. COMMENT Tissue kallikreins cleave Met-Lys and Arg-Ser bonds in !1kininogen to release lysyl-bradykinin (kallidin). GENETICS !$#gene mGK-1 !$#map_position 7 !$#introns 16/1; 69/2; 165/1; 210/3 CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS glycoprotein; hydrolase; saliva; serine proteinase; !1submandibular gland; zymogen FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-24 #domain activation peptide #status predicted #label !8APT\ !$25-261 #product tissue kallikrein, submandibular #status !8predicted #label MPT\ !$25-253 #domain trypsin homology #label TRY\ !$31-173,50-66, !$152-219,184-198, !$209-234 #disulfide_bonds #status predicted\ !$65,120,213 #active_site His, Asp, Ser #status predicted\ !$102 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 261 #molecular-weight 29021 #checksum 8365 SEQUENCE /// ENTRY NGMSG #type complete TITLE 7S nerve growth factor gamma chain (EC 3.4.21.-) precursor - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 18-Dec-1981 #sequence_revision 17-May-1985 #text_change 18-Jun-1999 ACCESSIONS A91005; A90949; A93510; A92341; A00942; A21093; A22705 REFERENCE A91005 !$#authors Evans, B.A.; Richards, R.I. !$#journal EMBO J. (1985) 4:133-138 !$#title Genes for the alpha and gamma subunits of mouse nerve growth !1factor are contiguous. !$#cross-references MUID:85257431; PMID:3848399 !$#accession A91005 !'##molecule_type DNA !'##residues 1-261 ##label EVA REFERENCE A90949 !$#authors Ullrich, A.; Gray, A.; Wood, W.I.; Hayflick, J.; Seeburg, !1P.H. !$#journal DNA (1984) 3:387-392 !$#title Isolation of a cDNA clone coding for the gamma-subunit of !1mouse nerve growth factor using a high-stringency selection !1procedure. !$#cross-references MUID:85076169; PMID:6548955 !$#accession A90949 !'##molecule_type mRNA !'##residues 1-261 ##label ULL !'##cross-references GB:X01389; NID:g53373; PIDN:CAA25645.1; PID:g53374 REFERENCE A93510 !$#authors Howles, P.N.; Dickinson, D.P.; DiCaprio, L.L.; !1Woodworth-Gutai, M.; Gross, K.W. !$#journal Nucleic Acids Res. (1984) 12:2791-2805 !$#title Use of a cDNA recombinant for the gamma-subunit of mouse !1nerve growth factor to localize members of this multigene !1family near the TAM-1 locus on chromosome 7. !$#cross-references MUID:84169573; PMID:6200835 !$#accession A93510 !'##molecule_type mRNA !'##residues 127-202,'E',204-261 ##label HOW !'##cross-references GB:X00472; NID:g54260; PIDN:CAA25154.1; PID:g54261 !'##experimental_source inbred strain DBA/2J REFERENCE A92341 !$#authors Thomas, K.A.; Baglan, N.C.; Bradshaw, R.A. !$#journal J. Biol. Chem. (1981) 256:9156-9166 !$#title The amino acid sequence of the gamma-subunit of mouse !1submaxillary gland 7 S nerve growth factor. !$#cross-references MUID:81264363; PMID:7263706 !$#accession A92341 !'##molecule_type protein !'##residues 25-107,112-261 ##label THO !'##experimental_source outbred strain Swiss Webster COMMENT 7S nerve growth factor is composed of two alpha chains, a !1beta dimer composed of identical chains, and two gamma !1chains. The gamma chain is an arginine-specific proteinase. COMMENT The active form of the gamma chain occurs naturally as !1combinations of either two or three segments held together !1by disulfide bonds: B1 + A or B1 + C + B2. GENETICS !$#map_position 7 !$#introns 16/1; 69/2; 165/1; 210/3 CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS glycoprotein; growth factor; hydrolase; serine proteinase; !1submandibular gland FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$25-253 #domain trypsin homology #label TRY\ !$25-107 #domain segment B1 #label GB1\ !$25-107,112-261 #product nerve growth factor gamma chain (active !8form) #status experimental #label MAT\ !$112-261 #domain segment A #label GAA\ !$112-164 #domain segment C #label GCC\ !$165-261 #domain segment B2 #label GB2\ !$31-173,50-66, !$152-219,184-198, !$209-234 #disulfide_bonds #status predicted\ !$65,120,213 #active_site His, Asp, Ser #status predicted\ !$102 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 261 #molecular-weight 28998 #checksum 4983 SEQUENCE /// ENTRY TRMSM5 #type complete TITLE tissue kallikrein (EC 3.4.21.35) mGK-5, submandibular precursor - mouse ALTERNATE_NAMES glandular kallikrein ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 18-Jun-1999 ACCESSIONS S06305; I70019 REFERENCE S06305 !$#authors Drinkwater, C.C.; Richards, R.I. !$#journal Nucleic Acids Res. (1987) 15:10052 !$#title Sequence of the mouse glandular kallikrein gene, mGK-5. !$#cross-references MUID:88096499; PMID:3502721 !$#accession S06305 !'##molecule_type DNA !'##residues 1-261 ##label DRI !'##cross-references EMBL:Y00500; NID:g51071; PIDN:CAA68553.1; !1PID:g297525 REFERENCE I55260 !$#authors Evans, B.A.; Drinkwater, C.C.; Richards, R.I. !$#journal J. Biol. Chem. (1987) 262:8027-8034 !$#title Mouse glandular kallikrein genes: Structure and partial !1sequence analysis of the kallikrein gene locus. !$#cross-references MUID:87250386; PMID:3036794 !$#accession I70019 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 70-122 ##label RES !'##cross-references GB:M18604; NID:g198514; PIDN:AAD15284.1; !1PID:g198524 GENETICS !$#introns 16/1; 69/2; 165/1; 210/3 CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS glycoprotein; hydrolase; serine proteinase; submandibular !1gland FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-24 #domain propeptide #status predicted #label PRO\ !$25-261 #product tissue kallikrein mGK-5, submanibular !8#status predicted #label MAT\ !$25-253 #domain trypsin homology #label TRY\ !$31-173,50-66, !$152-219,184-198, !$209-234 #disulfide_bonds #status predicted\ !$65,120,213 #active_site His, Asp, Ser #status predicted\ !$102 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 261 #molecular-weight 28748 #checksum 3274 SEQUENCE /// ENTRY NGMSA #type complete TITLE 7S nerve growth factor alpha chain precursor - mouse ALTERNATE_NAMES NGF ORGANISM #formal_name Mus musculus #common_name house mouse DATE 28-May-1986 #sequence_revision 30-Sep-1987 #text_change 18-Jun-1999 ACCESSIONS B91005; A90491; B90491; A90481; A00943; B22705 REFERENCE A91005 !$#authors Evans, B.A.; Richards, R.I. !$#journal EMBO J. (1985) 4:133-138 !$#title Genes for the alpha and gamma subunits of mouse nerve growth !1factor are contiguous. !$#cross-references MUID:85257431; PMID:3848399 !$#accession B91005 !'##molecule_type DNA !'##residues 1-256 ##label EVA REFERENCE A90491 !$#authors Isackson, P.J.; Ullrich, A.; Bradshaw, R.A. !$#journal Biochemistry (1984) 23:5997-6002 !$#title Mouse 7S nerve growth factor: complete sequence of a cDNA !1coding for the alpha-subunit precursor and its relationship !1to serine proteases. !$#cross-references MUID:85122662; PMID:6395888 !$#accession A90491 !'##molecule_type mRNA !'##residues 1-256 ##label ISA !'##experimental_source clone 3F2 !$#accession B90491 !'##molecule_type mRNA !'##residues 1-183,'K',185-256 ##label IS2 !'##cross-references GB:M11434; NID:g200049; PIDN:AAA39819.1; !1PID:g200050 !'##experimental_source clone 2AF !'##note clones 2A4 and 3F2 probably represent different alleles !'##note the amino end of the mature protein is blocked; however, it is !1not clear if this occurs in the 7S complex or has been !1experimentally introduced REFERENCE A90481 !$#authors Ronne, H.; Anundi, H.; Rask, L.; Peterson, P.A. !$#journal Biochemistry (1984) 23:1229-1234 !$#title 7S nerve growth factor alpha and gamma subunits are closely !1related proteins. !$#cross-references MUID:84179095; PMID:6712944 !$#accession A90481 !'##molecule_type protein !'##residues 18-43,'L',45-47;113-139,'C',141;162-178 ##label RON COMMENT Although residues 1-17 and 18-24 are, by homology, the !1signal sequence and activation peptide, respectively, the !1presence of Gln-24 prevents cleavage of the activation !1peptide, which remains attached at the amino end of the !1mature alpha chain. COMMENT The role of the alpha chain in NGF function remains obscure. !1Although homologous to the glandular kallikrein family, this !1protein has no demonstrable enzymatic activity. This may be !1due to several critical changes in its sequence, relative to !1those of the related proteases. GENETICS !$#introns 16/1; 64/2; 160/1; 205/3 CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS growth factor; submandibular gland FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-256 #product nerve growth factor alpha chain #status !8experimental #label NFA\ !$21-248 #domain trypsin homology #label TRY SUMMARY #length 256 #molecular-weight 28548 #checksum 7275 SEQUENCE /// ENTRY KQRTP #type complete TITLE tissue kallikrein (EC 3.4.21.35) precursor - rat ALTERNATE_NAMES glandular kallikrein; kininogenin; true tissue kallikrein ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 05-Apr-1983 #sequence_revision 05-Apr-1983 #text_change 16-Jun-2000 ACCESSIONS A00944; A41429; A25137; JX0073; A23863; A33359 REFERENCE A00944 !$#authors Swift, G.H.; Dagorn, J.C.; Ashley, P.L.; Cummings, S.W.; !1MacDonald, R.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:7263-7267 !$#title Rat pancreatic kallikrein mRNA: nucleotide sequence and !1amino acid sequence of the encoded preproenzyme. !$#cross-references MUID:83117659; PMID:6961406 !$#accession A00944 !'##molecule_type mRNA !'##residues 1-265 ##label SWI !'##experimental_source pancreatic REFERENCE A41429 !$#authors Kato, H.; Nakanishi, E.; Enjyoji, K.; Hayashi, I.; Oh-Ishi, !1S.; Iwanaga, S. !$#journal J. Biochem. (1987) 102:1389-1404 !$#title Characterization of serine proteinases isolated from rat !1submaxillary gland: with special reference to the !1degradation of rat kininogens by these enzymes. !$#cross-references MUID:88198057; PMID:3482210 !$#accession A41429 !'##status preliminary !'##molecule_type protein !'##residues 29-53,'X',55-87 ##label KAT REFERENCE A25137 !$#authors Gerald, W.L.; Chao, J.; Chao, L. !$#journal Biochim. Biophys. Acta (1986) 866:1-14 !$#title Immunological identification of rat tissue kallikrein cDNA !1and characterization of the kallikrein gene family. !$#cross-references MUID:86131678; PMID:3004582 !$#accession A25137 !'##molecule_type mRNA !'##residues 115-265 ##label GER REFERENCE JX0073 !$#authors Inoue, H.; Fukui, K.; Miyake, Y. !$#journal J. Biochem. (1989) 105:834-840 !$#title Identification and structure of the rat true tissue !1kallikrein gene expressed in the kidney. !$#cross-references MUID:89327211; PMID:2753879 !$#accession JX0073 !'##molecule_type DNA !'##residues 1-265 ##label INO !'##cross-references GB:D00448; NID:g220792; PIDN:BAA00346.1; !1PID:g220794 !'##experimental_source kidney REFERENCE A23863 !$#authors Ashley, P.L.; MacDonald, R.J. !$#journal Biochemistry (1985) 24:4512-4520 !$#title Kallikrein-related mRNAs of the rat submaxillary gland: !1nucleotide sequences of four distinct types including tonin. !$#cross-references MUID:86051477; PMID:2998455 !$#accession A23863 !'##status preliminary !'##molecule_type mRNA !'##residues 1-265 ##label ASH !'##cross-references GB:M11563; NID:g205029; PIDN:AAA41464.1; !1PID:g205030 !'##experimental_source submaxillary gland REFERENCE A33359 !$#authors Wines, D.R.; Brady, J.M.; Pritchett, D.B.; Roberts, J.L.; !1MacDonald, R.J. !$#journal J. Biol. Chem. (1989) 264:7653-7662 !$#title Organization and expression of the rat kallikrein gene !1family. !$#cross-references MUID:89214217; PMID:2708383 !$#accession A33359 !'##status preliminary !'##molecule_type DNA !'##residues 5-265 ##label WIN !'##cross-references GB:M23874; GB:J04701; GB:M23875; GB:M23876; !1NID:g205007; PIDN:AAA41462.1; PID:g205009 COMMENT The kallikreins liberate lysyl-bradykinin, a vasoactive !1decapeptide, from kininogens. COMMENT The protein presumably assumes the two-chain form by !1cleavage between residues 115-116. COMMENT Tissue kallikreins cleave Met-Lys and Arg-Ser bonds in !1kininogen to release lysyl-bradykinin (kallidin). GENETICS !$#introns 20/1; 73/2; 169/1; 214/3 CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS hydrolase; pancreas; serine proteinase; zymogen FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-28 #domain activation peptide #status predicted #label !8APT\ !$29-265 #product tissue kallikrein, pancreatic #status !8predicted #label MPT\ !$29-257 #domain trypsin homology #label TRY\ !$35-177,54-70, !$156-223,188-202, !$213-238 #disulfide_bonds #status predicted\ !$69,124,217 #active_site His, Asp, Ser #status predicted SUMMARY #length 265 #molecular-weight 29280 #checksum 7064 SEQUENCE /// ENTRY KQRTTN #type complete TITLE tonin (EC 3.4.21.-) precursor - rat ALTERNATE_NAMES esterase 1 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 25-Feb-1985 #sequence_revision 02-Dec-1994 #text_change 18-Jun-1999 ACCESSIONS B33359; A32340; C23863; A93323; A94635; A34050; A30971; !1A00945 REFERENCE A33359 !$#authors Wines, D.R.; Brady, J.M.; Pritchett, D.B.; Roberts, J.L.; !1MacDonald, R.J. !$#journal J. Biol. Chem. (1989) 264:7653-7662 !$#title Organization and expression of the rat kallikrein gene !1family. !$#cross-references MUID:89214217; PMID:2708383 !$#accession B33359 !'##molecule_type DNA !'##residues 1-259 ##label WIN !'##cross-references GB:M23877; GB:J04702; GB:M23878; NID:g207411; !1PIDN:AAA42259.1; PID:g207413; GB:M23879 REFERENCE A32340 !$#authors Shai, S.Y.; Woodley-Miller, C.; Chao, J.; Chao, L. !$#journal Biochemistry (1989) 28:5334-5343 !$#title Characterization of genes encoding rat tonin and a !1kallikrein-like serine protease. !$#cross-references MUID:89375248; PMID:2550051 !$#accession A32340 !'##molecule_type DNA !'##residues 1-259 ##label SHA !'##cross-references GB:M26533; NID:g206775; PIDN:AAA42081.1; !1PID:g206776; GB:J02860 REFERENCE A23863 !$#authors Ashley, P.L.; MacDonald, R.J. !$#journal Biochemistry (1985) 24:4512-4520 !$#title Kallikrein-related mRNAs of the rat submaxillary gland: !1nucleotide sequences of four distinct types including tonin. !$#cross-references MUID:86051477; PMID:2998455 !$#accession C23863 !'##molecule_type mRNA !'##residues 1-259 ##label ASH !'##cross-references GB:M11565; NID:g205033; PIDN:AAA41466.1; !1PID:g205034 REFERENCE A93323 !$#authors Lazure, C.; Leduc, R.; Seidah, N.G.; Thibault, G.; Genest, !1J.; Chretien, M. !$#journal Nature (1984) 307:555-558 !$#title Amino acid sequence of rat submaxillary tonin reveals !1similarities to serine proteases. !$#cross-references MUID:84117504; PMID:6320014 !$#accession A93323 !'##molecule_type protein !'##residues 25-259 ##label LA1 REFERENCE A94635 !$#authors Lazure, C. !$#submission submitted to the Protein Sequence Database, March 1985 !$#contents carbohydrate-binding site; revisions !$#accession A94635 !'##molecule_type protein !'##residues 104-119 ##label LA2 REFERENCE A34050 !$#authors Kamada, M.; Furuhata, N.; Yamaguchi, T.; Ikekita, M.; !1Kizuki, K.; Moriya, H. !$#journal Biochem. Biophys. Res. Commun. (1990) 166:231-237 !$#title Observation of tissue prokallikrein activation by some !1serine proteases, arginine esterases in rat submandibular !1gland. !$#cross-references MUID:90147705; PMID:2302205 !$#accession A34050 !'##molecule_type protein !'##residues 25-30,'X',32-34 ##label KAM REFERENCE A30971 !$#authors Lazure, C.; Leduc, R.; Seidah, N.G.; Thibault, G.; Genest, !1J.; Chretien, M. !$#journal Biochem. Cell Biol. (1987) 65:321-337 !$#title The complete amino acid sequence of rat submaxillary gland !1tonin does contain the aspartic acid at the active site: !1confirmation by protein sequence analyses. !$#cross-references MUID:87271223; PMID:3038148 !$#accession A30971 !'##molecule_type protein !'##residues 25-259 ##label LAZ COMMENT This protein is found in submaxillary gland. It has both !1trypsin- and chymotrypsin-like activities, being able to !1release angiotensin II from angiotensin I or !1angiotensinogen. GENETICS !$#introns 16/1; 67/2; 163/1; 208/3 CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS glycoprotein; hydrolase; serine proteinase FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-24 #domain propeptide #status predicted #label PRO\ !$25-259 #product tonin #status experimental #label MAT\ !$25-251 #domain trypsin homology #label TRY\ !$31-171,48-64, !$150-217,182-196, !$207-232 #disulfide_bonds #status predicted\ !$63,118,211 #active_site His, Asp, Ser #status predicted\ !$106,189 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 259 #molecular-weight 28248 #checksum 3760 SEQUENCE /// ENTRY A32297 #type complete TITLE semenogelase (EC 3.4.21.77) precursor [validated] - human ALTERNATE_NAMES gamma-seminoprotein; P-30 antigen; prostate-specific antigen; prostate-specific serine proteinase; prostatic antigen; prostatic proantigen; seminin ORGANISM #formal_name Homo sapiens #common_name man DATE 19-May-2000 #sequence_revision 19-May-2000 #text_change 08-Dec-2000 ACCESSIONS A32297; A32423; S03604; S05468; S05467; A32546; S02239; !1A26757; C31567; A31567; B31567; S00232; A23937; G01551; !1I52712; S41212 REFERENCE A32297 !$#authors Riegman, P.H.J.; Vlietstra, R.J.; van der Korput, J.A.G.M.; !1Romijn, J.C.; Trapman, J. !$#journal Biochem. Biophys. Res. Commun. (1989) 159:95-102 !$#title Characterization of the prostate-specific antigen gene: a !1novel human kallikrein-like gene. !$#cross-references MUID:89165891; PMID:2466464 !$#accession A32297 !'##status preliminary !'##molecule_type DNA !'##residues 1-261 ##label RIE !'##cross-references GB:M24543 REFERENCE A32423 !$#authors Lundwall, A. !$#journal Biochem. Biophys. Res. Commun. (1989) 161:1151-1159 !$#title Characterization of the gene for prostate-specific antigen, !1a human glandular kallikrein. !$#cross-references MUID:89302090; PMID:2472789 !$#accession A32423 !'##status preliminary !'##molecule_type DNA !'##residues 1-261 ##label LUN !'##cross-references GB:M27274; NID:g190552; PIDN:AAA60192.1; !1PID:g190553 REFERENCE S03604 !$#authors Digby, M.; Zhang, X.Y.; Richards, R.I. !$#journal Nucleic Acids Res. (1989) 17:2137 !$#title Human prostate specific antigen (PSA) gene: structure and !1linkage to the kallikrein-like gene, hGK-1. !$#cross-references MUID:89183632; PMID:2467258 !$#accession S03604 !'##molecule_type DNA !'##residues 1-261 ##label DIG !'##cross-references EMBL:X13940 REFERENCE S05468 !$#authors Klobeck, H.G.; Combriato, G.; Schulz, P.; Arbusow, V.; !1Fittler, F. !$#submission submitted to the EMBL Data Library, May 1989 !$#accession S05468 !'##molecule_type DNA !'##residues 1-261 ##label KL1 !'##cross-references EMBL:X14810; NID:g35732; PIDN:CAA32915.1; !1PID:g296671 REFERENCE S05467 !$#authors Klobeck, H.G.; Combriato, G.; Schulz, P.; Arbusow, V.; !1Fittler, F. !$#journal Nucleic Acids Res. (1989) 17:3981 !$#title Genomic sequence of human prostate specific antigen (PSA). !$#cross-references MUID:89282407; PMID:2471958 !$#accession S05467 !'##molecule_type DNA !'##residues 1-29 ##label KL2 !'##cross-references EMBL:X14810 REFERENCE A32546 !$#authors Henttu, P.; Vihko, P. !$#journal Biochem. Biophys. Res. Commun. (1989) 160:903-910 !$#title cDNA coding for the entire human prostate specific antigen !1shows high homologies to the human tissue kallikrein genes. !$#cross-references MUID:89246551; PMID:2470373 !$#accession A32546 !'##molecule_type mRNA !'##residues 1-72,'T',74-85,'I',87-174,'P',176-183,'Q',185-259,'D',261 !1##label HEN !'##cross-references GB:M26663 REFERENCE S02239 !$#authors Schulz, P.; Stucka, R.; Feldmann, H.; Combriato, G.; !1Klobeck, H.G.; Fittler, F. !$#journal Nucleic Acids Res. (1988) 16:6226 !$#title Sequence of a cDNA clone encompassing the complete mature !1human prostate specific antigen (PSA) and an unspliced !1leader sequence. !$#cross-references MUID:88289366; PMID:2456523 !$#accession S02239 !'##molecule_type mRNA !'##residues 17-63,'T',65-135,'M',137-261 ##label SCH !'##cross-references EMBL:X07730 REFERENCE A26757 !$#authors Lundwall, A.; Lilja, H. !$#journal FEBS Lett. (1987) 214:317-322 !$#title Molecular cloning of human prostate specific antigen cDNA. !$#cross-references MUID:87190978; PMID:2436946 !$#accession A26757 !'##molecule_type mRNA !'##residues 5-261 ##label LU2 REFERENCE A90144 !$#authors Riegman, P.H.J.; Klaassen, P.; van der Korput, J.A.G.M.; !1Romijn, J.C.; Trapman, J. !$#journal Biochem. Biophys. Res. Commun. (1988) 155:181-188 !$#title Molecular cloning and characterization of novel prostate !1antigen cDNA's. !$#cross-references MUID:88326297; PMID:2458104 !$#accession C31567 !'##molecule_type mRNA !'##residues 5-261 ##label RI2 !'##cross-references GB:M21895; NID:g189523; PIDN:AAA59995.1; !1PID:g189524 !'##note the authors translated the codon GGC for residue 28 as Arg and !1TGG for residue 29 as Leu !$#accession A31567 !'##molecule_type mRNA !'##residues 5-210,'WVILITELTMPA',223,'PMVLHGSLV',233,'WRGGV' ##label !1RI3 !'##cross-references GB:M21896; NID:g189525; PIDN:AAA59996.1; !1PID:g189526 !'##note the authors translated the codon GGC for residue 28 as Arg and !1TGG for residue 29 as Leu !$#accession B31567 !'##molecule_type mRNA !'##residues 5-164,'CTPGPDGAAGSPDAWV' ##label RI4 !'##cross-references GB:M21897; NID:g189529; PIDN:AAA59997.1; !1PID:g189530 !'##note the authors translated the codon GGC for residue 28 as Arg, TGG !1for residue 29 as Leu, and CCT for residue 167 as Ala REFERENCE S00232 !$#authors Schaller, J.; Akiyama, K.; Tsuda, R.; Hara, M.; Marti, T.; !1Rickli, E.E. !$#journal Eur. J. Biochem. (1987) 170:111-120 !$#title Isolation, characterization and amino-acid sequence of !1gamma-seminoprotein, a glycoprotein from human seminal !1plasma. !$#cross-references MUID:88082806; PMID:3691515 !$#accession S00232 !'##molecule_type protein !'##residues 25-261 ##label SC2 REFERENCE A23937 !$#authors Watt, K.W.K.; Lee, P.J.; M'Timkulu, T.; Chan, W.P.; Loor, R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:3166-3170 !$#title Human prostate-specific antigen: structural and functional !1similarity with serine proteases. !$#cross-references MUID:86205857; PMID:2422647 !$#accession A23937 !'##molecule_type protein !'##residues 25-93,'T',95-164,'HL',166,'YDQM',169-174,'Q',176-261 !1##label WAT REFERENCE G07735 !$#authors Moreno, J.M. !$#submission submitted to the EMBL Data Library, November 1994 !$#accession G01551 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-261 ##label MOR !'##cross-references EMBL:U17040; NID:g595945; PIDN:AAA56764.1; !1PID:g595946 REFERENCE I52712 !$#authors Monne, M.; Croce, C.M.; Yu, H.; Diamandis, E.P. !$#journal Cancer Res. (1994) 54:6344-6347 !$#title Molecular characterization of prostate-specific antigen !1messenger RNA expressed in breast tumors. !$#cross-references MUID:95079406; PMID:7527295 !$#accession I52712 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 'PQAYHLHPESCVT',1-176 ##label RES !'##cross-references GB:S75755; NID:g861469; PIDN:AAD14185.1; !1PID:g4261885 REFERENCE S41212 !$#authors Christensson, A.; Lilja, H. !$#journal Eur. J. Biochem. (1994) 220:45-53 !$#title Complex formation between protein C inhibitor and !1prostate-specific antigen in vitro and in human semen. !$#cross-references MUID:94164172; PMID:7509746 !$#accession S41212 !'##molecule_type protein !'##residues 25-30,'X',32-49 ##label CHR COMMENT This enzyme preferentially cleaves after tyrosine residues. GENETICS !$#gene GDB:APS; PSA !'##cross-references GDB:119695; OMIM:176820 !$#map_position 19q13.3-19q13.3 !$#introns 16/1; 69/2; 165/1; 210/3 CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS glycoprotein; hydrolase; prostate; serine proteinase FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-24 #domain propeptide #status predicted #label PRO\ !$25-261 #product semenogelase #status experimental #label !8MAT\ !$25-253 #domain trypsin homology #label TRY\ !$65,120,213 #active_site His, Asp, Ser #status predicted SUMMARY #length 261 #molecular-weight 28741 #checksum 1256 SEQUENCE /// ENTRY S35711 #type complete TITLE semenogelase (EC 3.4.21.77) precursor - rhesus macaque ALTERNATE_NAMES gamma-seminoprotein; P-30 antigen; prostate-specific antigen; prostate-specific serine proteinase; prostatic antigen; prostatic proantigen; seminin ORGANISM #formal_name Macaca mulatta #common_name rhesus macaque DATE 19-May-2000 #sequence_revision 19-May-2000 #text_change 19-May-2000 ACCESSIONS S35711; S34239 REFERENCE S35711 !$#authors Gauthier, E.R.; Chapdelaine, P.; Tremblay, R.R.; Dube, J.Y. !$#journal Biochim. Biophys. Acta (1993) 1174:207-210 !$#title Characterization of rhesus monkey prostate specific antigen !1cDNA. !$#cross-references MUID:93363642; PMID:7689340 !$#accession S35711 !'##molecule_type mRNA !'##residues 1-261 ##label GAU !'##cross-references EMBL:X73560; NID:g311843; PIDN:CAA51957.1; !1PID:g311844 COMMENT This enzyme preferentially cleaves after tyrosine residues. CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS glycoprotein; hydrolase; prostate; serine proteinase FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-24 #domain propeptide #status predicted #label PRO\ !$25-261 #product semenogelase #status predicted #label MAT\ !$25-253 #domain trypsin homology #label TRY\ !$65,120,213 #active_site His, Asp, Ser #status predicted SUMMARY #length 261 #molecular-weight 28816 #checksum 3070 SEQUENCE /// ENTRY ELRT1 #type complete TITLE pancreatic elastase (EC 3.4.21.36) I precursor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 18-Jun-1999 ACCESSIONS A00960; A20534 REFERENCE A00960 !$#authors MacDonald, R.J.; Swift, G.H.; Quinto, C.; Swain, W.; Pictet, !1R.L.; Nikovits, W.; Rutter, W.J. !$#journal Biochemistry (1982) 21:1453-1463 !$#title Primary structure of two distinct rat pancreatic !1preproelastases determined by sequence analysis of the !1complete cloned messenger ribonucleic acid sequences. !$#cross-references MUID:82182967; PMID:6918221 !$#accession A00960 !'##molecule_type mRNA !'##residues 1-266 ##label MAC !'##cross-references GB:V01234; NID:g56088; PIDN:CAA24544.1; PID:g56089 REFERENCE A20534 !$#authors Largman, C. !$#journal Biochemistry (1983) 22:3763-3770 !$#title Isolation and characterization of rat pancreatic elastase. !$#cross-references MUID:84000385; PMID:6555050 !$#accession A20534 !'##molecule_type protein !'##residues 17-37,'X',39-45 ##label LAR CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS hydrolase; pancreas; serine proteinase; zymogen FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-26 #domain activation peptide #status predicted #label !8APT\ !$27-266 #product elastase I #status predicted #label MPT\ !$27-259 #domain trypsin homology #label TRY\ !$71,119,214 #active_site His, Asp, Ser #status predicted SUMMARY #length 266 #molecular-weight 28976 #checksum 6741 SEQUENCE /// ENTRY ELPG #type complete TITLE pancreatic elastase (EC 3.4.21.36) I precursor - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 24-Apr-1984 #sequence_revision 30-Sep-1990 #text_change 16-Jun-2000 ACCESSIONS JS0013; A26777; A10061; A00959 REFERENCE A92005 !$#authors Shirasu, Y.; Yoshida, H.; Mikayama, T.; Matsuki, S.; Tanaka, !1J.I.; Ikenaga, H. !$#journal J. Biochem. (1986) 99:1707-1712 !$#title Isolation and expression in Escherichia coli of a cDNA clone !1encoding porcine pancreatic elastase. !$#cross-references MUID:86304235; PMID:3528137 !$#accession JS0013 !'##molecule_type mRNA !'##residues 1-266 ##label SHI !'##cross-references GB:X04036; GB:D00070; GB:N00070; NID:g1941; !1PIDN:CAA27670.1; PID:g1942 REFERENCE A26777 !$#authors Tani, T.; Kawashima, I.; Furukawa, H.; Ohmine, T.; !1Takiguchi, Y. !$#journal J. Biochem. (1987) 101:591-599 !$#title Characterization of a silent gene for human pancreatic !1elastase I: structure of the 5'-flanking region. !$#cross-references MUID:87250343; PMID:3648024 !$#accession A26777 !'##molecule_type mRNA !'##residues 1-125,'G',127-183,'L',185-266 ##label TAN !'##cross-references GB:D00160; NID:g217683; PIDN:BAA00118.1; !1PID:g217684 !'##note the authors translated the codon GGG for residue 58 as Gln, GGC !1for residue 126 as Ala, and CTG for residue 184 as Cys REFERENCE A90267 !$#authors Shotton, D.M.; Hartley, B.S. !$#journal Biochem. J. (1973) 131:643-675 !$#title Evidence for the amino acid sequence of porcine pancreatic !1elastase. !$#cross-references MUID:73229121; PMID:4578945 !$#accession A10061 !'##molecule_type protein !'##residues 27-91,'N',93-203,'N',205-266 ##label SHO REFERENCE A93160 !$#authors Shotton, D.M.; Hartley, B.S. !$#journal Nature (1970) 225:811-816 !$#title Three-dimensional structure of tosyl-elastase. !$#cross-references MUID:70114044; PMID:5415110 !$#contents annotation; X-ray crystallography, 3.5 angstroms; active !1site CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS hydrolase; pancreas; serine proteinase; zymogen FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-26 #domain activation peptide #status predicted #label !8APT\ !$27-266 #product elastase I #status experimental #label MAT\ !$27-259 #domain trypsin homology #label TRY\ !$56-72,153-220, !$184-200,210-240 #disulfide_bonds #status experimental\ !$71,119,214 #active_site His, Asp, Ser #status experimental SUMMARY #length 266 #molecular-weight 28821 #checksum 2748 SEQUENCE /// ENTRY ELRT2 #type complete TITLE pancreatic elastase II (EC 3.4.21.71) precursor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 24-Sep-1999 ACCESSIONS A00961 REFERENCE A00960 !$#authors MacDonald, R.J.; Swift, G.H.; Quinto, C.; Swain, W.; Pictet, !1R.L.; Nikovits, W.; Rutter, W.J. !$#journal Biochemistry (1982) 21:1453-1463 !$#title Primary structure of two distinct rat pancreatic !1preproelastases determined by sequence analysis of the !1complete cloned messenger ribonucleic acid sequences. !$#cross-references MUID:82182967; PMID:6918221 !$#accession A00961 !'##molecule_type mRNA !'##residues 1-271 ##label MAC !'##cross-references GB:L00124; GB:J00731; NID:g204019; PIDN:AAA98780.1; !1PID:g204021 CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS hydrolase; pancreas; serine proteinase; zymogen FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-30 #domain activation peptide #status predicted #label !8APT\ !$31-271 #product elastase II #status predicted #label MPT\ !$31-264 #domain trypsin homology #label TRY\ !$75,123,218 #active_site His, Asp, Ser #status predicted SUMMARY #length 271 #molecular-weight 28884 #checksum 9693 SEQUENCE /// ENTRY CPBOA3 #type complete TITLE procarboxypeptidase A complex component III - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 18-Jul-1997 ACCESSIONS A25065 REFERENCE A25065 !$#authors Venot, N.; Sciaky, M.; Puigserver, A.; Desnuelle, P.; !1Laurent, G. !$#journal Eur. J. Biochem. (1986) 157:91-99 !$#title Amino acid sequence and disulfide bridges of subunit III, a !1defective endopeptidase present in the bovine pancreatic 6 S !1procarboxypeptidase A complex. !$#cross-references MUID:86220198; PMID:3519215 !$#accession A25065 !'##molecule_type protein !'##residues 1-240 ##label VEN COMMENT This protein is found in the pancreatic juice of ruminants, !1where it constitutes 5-6% of the total proteins, in a !1noncovalent association with the zymogens of !1carboxypeptidase A (EC 3.4.17.1) and chymotrypsin C (EC !13.4.21.2). It is inactive towards the usual substrates of !1serine proteinases and apparently represents a defective !1elastase. Its likely function is to protect the !1procarboxypeptidase against denaturation in the acidic !1environment of the ruminant duodenum. CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS pancreas FEATURE !$1-233 #domain trypsin homology #label TRY\ !$28-44,87-90, !$127-193,158-174, !$183-214 #disulfide_bonds #status experimental\ !$43,93,187 #active_site His, Asp, Ser #status predicted SUMMARY #length 240 #molecular-weight 25863 #checksum 5009 SEQUENCE /// ENTRY KYRTB #type complete TITLE chymotrypsin (EC 3.4.21.1) B precursor - rat ALTERNATE_NAMES chymotrypsinogen B ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 18-Jun-1999 ACCESSIONS A22658 REFERENCE A22658 !$#authors Bell, G.I.; Quinto, C.; Quiroga, M.; Valenzuela, P.; Craik, !1C.S.; Rutter, W.J. !$#journal J. Biol. Chem. (1984) 259:14265-14270 !$#title Isolation and sequence of a rat chymotrypsin B gene. !$#cross-references MUID:85054881; PMID:6209274 !$#accession A22658 !'##molecule_type DNA !'##residues 1-263 ##label BEL !'##cross-references GB:K02298; NID:g203653; PIDN:AAA98732.1; !1PID:g203654 GENETICS !$#introns 18/1; 52/3; 79/2; 105/3; 166/1; 210/3 CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS hydrolase; pancreas; protein digestion; serine proteinase FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-33 #domain propeptide #status predicted #label PRO\ !$34-263 #product chymotrypsin B #status predicted #label MAT\ !$34-256 #domain trypsin homology #label TRY\ !$75,120,213 #active_site His, Asp, Ser #status predicted SUMMARY #length 263 #molecular-weight 27849 #checksum 4310 SEQUENCE /// ENTRY KYBOB #type complete TITLE chymotrypsin (EC 3.4.21.1) B precursor - bovine ALTERNATE_NAMES chymotrypsinogen B ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 08-Oct-1981 #sequence_revision 08-Oct-1981 #text_change 18-Jul-1997 ACCESSIONS A00953 REFERENCE A00953 !$#authors Smillie, L.B.; Furka, A.; Nagabhushan, N.; Stevenson, K.J.; !1Parkes, C.O. !$#journal Nature (1968) 218:343-346 !$#title Structure of chymotrypsinogen B compared with !1chymotrypsinogen A and trypsinogen. !$#cross-references MUID:68238908; PMID:5649671 !$#accession A00953 !'##molecule_type protein !'##residues 1-245 ##label SMI COMMENT Chymotrypsinogen B is synthesized, along with !1chymotrypsinogen A, in the acinar cells of pancreas. COMMENT The first activation cleavage, leading to pi-chymotrypsin B, !1occurs in the same position (after Arg-15) as in !1chymotrypsinogen A. CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS hydrolase; pancreas; protein digestion; serine proteinase; !1zymogen FEATURE !$1-15 #domain propeptide #status experimental #label PRO\ !$16-245 #product chymotrypsin B #status experimental #label !8MAT\ !$16-238 #domain trypsin homology #label TRY\ !$1-122,42-58, !$136-201,168-182, !$191-220 #disulfide_bonds #status experimental\ !$57,102,195 #active_site His, Asp, Ser #status experimental SUMMARY #length 245 #molecular-weight 25755 #checksum 9874 SEQUENCE /// ENTRY KYBOA #type complete TITLE chymotrypsin (EC 3.4.21.1) A precursor - bovine ALTERNATE_NAMES chymotrypsinogen A ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 07-May-1999 ACCESSIONS A90235; A93158; S29650; A00952 REFERENCE A90235 !$#authors Brown, J.R.; Hartley, B.S. !$#journal Biochem. J. (1966) 101:214-228 !$#title Location of disulphide bridges by diagonal paper !1electrophoresis. The disulphide bridges of bovine !1chymotrypsinogen A. !$#cross-references MUID:67181721; PMID:5971783 !$#accession A90235 !'##molecule_type protein !'##residues 1-101,'N',103-245 ##label BRO REFERENCE A93158 !$#authors Blow, D.M.; Birktoft, J.J.; Hartley, B.S. !$#journal Nature (1969) 221:337-340 !$#title Role of a buried acid group in the mechanism of action of !1chymotrypsin. !$#cross-references MUID:69106266; PMID:5764436 !$#contents annotation; revision to residue 102 REFERENCE A90572 !$#authors Meloun, B.; Kluh, I.; Kostka, V.; Moravek, L.; Prusik, Z.; !1Vanacek, J.; Keil, B.; Sorm, F. !$#journal Biochim. Biophys. Acta (1966) 130:543-546 !$#title Covalent structure of bovine chymotrypsinogen A. !$#cross-references MUID:67183948; PMID:5972866 !$#accession A93158 !'##molecule_type protein !'##residues 1-101,'N',103-245 ##label MEL !'##note disulfide bonds were determined REFERENCE S29650 !$#authors Cutruzzola, F.; Ascenzi, P.; Barra, D.; Bolognesi, M.; !1Menegatti, E.; Sarti, P.; Schnebli, H.P.; Tomova, S.; !1Amiconi, G. !$#journal Biochim. Biophys. Acta (1993) 1161:201-208 !$#title Selective oxidation of Met-192 in bovine alpha-chymotrypsin. !1Effect on catalytic and inhibitor binding properties. !$#cross-references MUID:93160238; PMID:8431470 !$#accession S29650 !'##molecule_type protein !'##residues 1-12;16-27;149-160;181-200 ##label CUT REFERENCE A90236 !$#authors Smillie, L.B.; Hartley, B.S. !$#journal Biochem. J. (1966) 101:232-241 !$#title Histidine sequences in the active centres of some 'serine' !1proteinases. !$#cross-references MUID:67181723; PMID:5971785 !$#contents annotation; active site REFERENCE A93754 !$#authors Birktoft, J.J.; Blow, D.M.; Henderson, R.; Steitz, T.A. !$#journal Philos. Trans. R. Soc. Lond. (1970) B257:67-76 !$#title The structure of alpha-chymotrypsin. !$#contents annotation; X-ray crystallography COMMENT Chymotrypsinogens are synthesized in the acinar cells of !1pancreas. COMMENT Tryptic cleavage after Arg-15 results in a fully active !1enzyme (pi-chymotrypsin); subsequent chymotryptic cleavage !1after Leu-13 liberates the dipeptide Ser-14 and Arg-15 and !1thus leads to delta-chymotrypsin; further chymotryptic !1cleavage liberates the dipeptide Thr-147 and Asn-148 and !1thus leads to alpha-chymotrypsin; upon slow activation, !1chymotrypsin excises the dipeptide Thr-147 and Asn-148 !1directly from chymotrypsinogen, which leads to the degraded !1form neochymotrypsin. CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS hydrolase; pancreas; protein digestion; serine proteinase; !1zymogen FEATURE !$1-245 #product chymotrypsinogen #status experimental #label !8ZYM\ !$1-13,16-146,149-245 #product alpha-chymotrypsin #status experimental !8#label MPT\ !$16-238 #domain trypsin homology #label TRY\ !$1-122,42-58, !$136-201,168-182, !$191-220 #disulfide_bonds #status experimental\ !$57,102,195 #active_site His, Asp, Ser #status experimental SUMMARY #length 245 #molecular-weight 25666 #checksum 2697 SEQUENCE /// ENTRY KYVH2O #type complete TITLE chymotrypsin (EC 3.4.21.1) II - oriental hornet ORGANISM #formal_name Vespa orientalis #common_name oriental hornet DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 18-Jul-1997 ACCESSIONS A00954 REFERENCE A90109 !$#authors Jany, K.D.; Bekelar, K.; Pfleiderer, G.; Ishay, J. !$#journal Biochem. Biophys. Res. Commun. (1983) 110:1-7 !$#title Amino acid sequence of an insect chymotrypsin from the !1larvae of the hornet, Vespa orientalis. !$#cross-references MUID:83178101; PMID:6340663 !$#accession A00954 !'##molecule_type protein !'##residues 1-216 ##label JAN REFERENCE A90635 !$#authors Jany, K.D.; Bekelar, K.; Ishay, J. !$#journal Biochim. Biophys. Acta (1981) 668:197-200 !$#title The amino acid sequences around the reactive serine and !1histidine residues of the chymotrypsin-like protease from !1the hornet, Vespa orientalis. !$#cross-references MUID:81208311; PMID:6786354 !$#contents annotation; active site CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS hydrolase; protein digestion; serine proteinase FEATURE !$1-211 #domain trypsin homology #label TRY\ !$25-40,146-159, !$169-193 #disulfide_bonds #status experimental\ !$39,173 #active_site His, Ser #status experimental\ !$82 #active_site Asp #status predicted SUMMARY #length 216 #molecular-weight 23471 #checksum 2059 SEQUENCE /// ENTRY KYVH2C #type complete TITLE chymotrypsin (EC 3.4.21.1) II - European hornet ORGANISM #formal_name Vespa crabro #common_name European hornet DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 18-Jul-1997 ACCESSIONS A00955 REFERENCE A00955 !$#authors Jany, K.D.; Haug, H. !$#journal FEBS Lett. (1983) 158:98-102 !$#title Amino acid sequence of the chymotryptic protease II from the !1larvae of the nornet, Vespa crabro. !$#accession A00955 !'##molecule_type protein !'##residues 1-218 ##label JAN !'##note an additional Arg was found at the carboxyl end of some of the !1molecules CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS hydrolase; protein digestion; serine proteinase FEATURE !$1-213 #domain trypsin homology #label TRY\ !$25-40,148-161, !$171-195 #disulfide_bonds #status predicted\ !$39,175 #active_site His, Ser #status experimental\ !$84 #active_site Asp #status predicted SUMMARY #length 218 #molecular-weight 23677 #checksum 9812 SEQUENCE /// ENTRY S49129 #type complete TITLE chymotrypsin (EC 3.4.21.1) 1 precursor - African malaria mosquito ALTERNATE_NAMES chymotrypsin-like proteinase ANCHYM1 ORGANISM #formal_name Anopheles gambiae #common_name African malaria mosquito DATE 19-May-2000 #sequence_revision 19-May-2000 #text_change 19-May-2000 ACCESSIONS S49129; S44185 REFERENCE S35412 !$#authors Mueller, H. !$#submission submitted to the EMBL Data Library, November 1992 !$#description Cloning of blood meal induced serine protease genes of the !1mosquito Anopheles gambiae. !$#accession S49129 !'##molecule_type mRNA !'##residues 1-259 ##label MUE !'##cross-references EMBL:Z18887; NID:g509414; PIDN:CAA79325.1; !1PID:g509415 !'##experimental_source strain Suakoko REFERENCE S44184 !$#authors Mueller, H.M.; Catteruccia, F.; Crisanti, A. !$#submission submitted to the EMBL Data Library, April 1994 !$#description An Anopheles gambiae locus containing the sequences of two !1closely related chymotrypsin-like proteases induced in the !1gut following blood meal. !$#accession S44185 !'##molecule_type DNA !'##residues 1-259 ##label MU2 !'##cross-references EMBL:Z32645; NID:g474026; PIDN:CAA83568.1; !1PID:g474028 !'##experimental_source strain Suakoko GENETICS !$#introns 78/2; 209/3 CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS hydrolase; protein digestion; serine proteinase FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-32 #domain activation peptide #status predicted #label !8PRO\ !$33-259 #product chymotrypsin 1 #status predicted #label MAT\ !$33-250 #domain trypsin homology #label TRY\ !$59-75,182-198, !$208-232 #disulfide_bonds #status experimental\ !$74,119,212 #active_site His, Asp, Ser #status predicted SUMMARY #length 259 #molecular-weight 27717 #checksum 196 SEQUENCE /// ENTRY S44184 #type complete TITLE chymotrypsin (EC 3.4.21.1) 2 precursor - African malaria mosquito ALTERNATE_NAMES chymotrypsin-like proteinase ANCHYM2 ORGANISM #formal_name Anopheles gambiae #common_name African malaria mosquito DATE 19-May-2000 #sequence_revision 19-May-2000 #text_change 19-May-2000 ACCESSIONS S44184; S49130 REFERENCE S44184 !$#authors Mueller, H.M.; Catteruccia, F.; Crisanti, A. !$#submission submitted to the EMBL Data Library, April 1994 !$#description An Anopheles gambiae locus containing the sequences of two !1closely related chymotrypsin-like proteases induced in the !1gut following blood meal. !$#accession S44184 !'##molecule_type DNA !'##residues 1-258 ##label MUE !'##cross-references EMBL:Z32645; NID:g474026; PIDN:CAA83567.1; !1PID:g474027 REFERENCE S35412 !$#authors Mueller, H. !$#submission submitted to the EMBL Data Library, November 1992 !$#description Cloning of blood meal induced serine protease genes of the !1mosquito Anopheles gambiae. !$#accession S49130 !'##molecule_type DNA !'##residues 1-165,'R',167-193,'FPD',197-258 ##label MU2 !'##cross-references EMBL:Z18888; NID:g509416; PIDN:CAA79326.1; !1PID:g509417 GENETICS !$#introns 78/2; 209/3 CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS hydrolase; protein digestion; serine proteinase FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-32 #domain activation peptide #status predicted #label !8PRO\ !$33-258 #product chymotrypsin 2 #status predicted #label MAT\ !$33-250 #domain trypsin homology #label TRY\ !$59-75,182-198, !$208-232 #disulfide_bonds #status experimental\ !$74,119,212 #active_site His, Asp, Ser #status predicted SUMMARY #length 258 #molecular-weight 27919 #checksum 536 SEQUENCE /// ENTRY KCUF #type complete TITLE brachyurin (EC 3.4.21.32) [validated] - Atlantic sand fiddler crab ALTERNATE_NAMES collagenolytic proteinase U ORGANISM #formal_name Uca pugilator #common_name Atlantic sand fiddler crab DATE 30-Nov-1980 #sequence_revision 30-Nov-1980 #text_change 15-Sep-2000 ACCESSIONS A00958 REFERENCE A00958 !$#authors Grant, G.A.; Henderson, K.O.; Eisen, A.Z.; Bradshaw, R.A. !$#journal Biochemistry (1980) 19:4653-4659 !$#title Amino acid sequence of a collagenolytic protease from the !1hepatopancreas of the fiddler crab, Uca pugilator. !$#cross-references MUID:81040004; PMID:6252953 !$#accession A00958 !'##molecule_type protein !'##residues 1-226 ##label GRA !'##experimental_source tissue hepatopancreas REFERENCE A73134 !$#authors Perona, J.J.; Fletterick, R.J. !$#submission submitted to the Brookhaven Protein Data Bank, November 1997 !$#cross-references PDB:1AZZ !$#contents annotation; X-ray crystallography, 2.3 angstroms, residues !11-90,'I',92-146,'SN',149-174,'N',176-184,'N',186-226 REFERENCE A59231 !$#authors Perona, J.J.; Tsu, C.A.; Craik, C.S.; Fletterick, R.J. !$#journal Biochemistry (1997) 36:5381-5392 !$#title Crystal structure of an ecotin-collagenase complex suggests !1a model for recognition and cleavage of the collagen triple !1helix. !$#cross-references MUID:97299771; PMID:9154920 !$#contents annotation; X-ray crystallography, 2.5 angstroms COMPLEX homodimer FUNCTION !$#description serine proteinase with a broad specificity, capable of !1degrading the native triple helix of collagen CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS homodimer; hydrolase; protein degradation; protein !1digestion; serine proteinase FEATURE !$1-218 #domain trypsin homology #label TRY\ !$26-42,151-164, !$174-200 #disulfide_bonds #status experimental\ !$41,87,178 #active_site His, Asp, Ser #status predicted SUMMARY #length 226 #molecular-weight 23499 #checksum 4229 SEQUENCE /// ENTRY KYHUCM #type complete TITLE chymase (EC 3.4.21.39) precursor [validated] - human ALTERNATE_NAMES chymase I; mast cell proteinase I ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 08-Dec-2000 ACCESSIONS A40967; B40967; A39861; S15906; S33247; S56063; A23686; !1A60772 REFERENCE A40967 !$#authors Urata, H.; Kinoshita, A.; Perez, D.M.; Misono, K.S.; Bumpus, !1F.M.; Graham, R.M.; Husain, A. !$#journal J. Biol. Chem. (1991) 266:17173-17179 !$#title Cloning of the gene and cDNA for human heart chymase. !$#cross-references MUID:91373329; PMID:1894611 !$#accession A40967 !'##molecule_type mRNA !'##residues 1-247 ##label URA !'##cross-references GB:M69136; NID:g180539; PIDN:AAA52019.1; !1PID:g180540 !'##experimental_source ventricular myocardium !$#accession B40967 !'##molecule_type DNA !'##residues 1-247 ##label UR2 !'##cross-references GB:M69137; NID:g180543; PIDN:AAA52021.1; !1PID:g180544 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE A39861 !$#authors Caughey, G.H.; Zerweck, E.H.; Vanderslice, P. !$#journal J. Biol. Chem. (1991) 266:12956-12963 !$#title Structure, chromosomal assignment, and deduced amino acid !1sequence of a human gene for mast cell chymase. !$#cross-references MUID:91302311; PMID:2071582 !$#accession A39861 !'##molecule_type DNA !'##residues 1-247 ##label CAU !'##cross-references GB:M64269; NID:g180541; PIDN:AAA52020.1; !1PID:g180542 !'##note these authors suggest that mast cells are the source of heart !1chymase REFERENCE S15906 !$#authors Jenne, D.E.; Tschopp, J. !$#journal Biochem. J. (1991) 276:567-568 !$#title Angiotensin II-forming heart chymase is a mast-cell-specific !1enzyme. !$#cross-references MUID:91264818; PMID:2049082 !$#accession S15906 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 26-60 ##label JEN !'##cross-references EMBL:X59072; NID:g29949; PIDN:CAA41796.1; !1PID:g29950 REFERENCE S33247 !$#authors Sukenaga, Y.; Kido, H.; Neki, A.; Enomoto, M.; Ishida, K.; !1Takagi, K.; Katunuma, N. !$#journal FEBS Lett. (1993) 323:119-122 !$#title Purification and molecular cloning of chymase from human !1tonsils. !$#cross-references MUID:93265916; PMID:8495723 !$#accession S33247 !'##molecule_type mRNA !'##residues 22-27,'S',29-247 ##label SUK !'##cross-references GB:S61334; NID:g409010; PIDN:AAB26828.1; !1PID:g409011 !$#accession S56063 !'##molecule_type protein !'##residues 22-27,'S',29-42 ##label SU2 !'##experimental_source tonsil REFERENCE A23686 !$#authors Urata, H.; Kinoshita, A.; Misono, K.S.; Bumpus, F.M.; !1Husain, A. !$#journal J. Biol. Chem. (1990) 265:22348-22357 !$#title Identification of a highly specific chymase as the major !1angiotensin II-forming enzyme in the human heart. !$#cross-references MUID:91093078; PMID:2266130 !$#accession A23686 !'##molecule_type protein !'##residues 22-30,32-39,'Q',41-45;136-141,'I',143 ##label UR3 REFERENCE A60772 !$#authors Schechter, N.M.; Irani, A.M.A.; Sprows, J.L.; Abernethy, J.; !1Wintroub, B.; Schwartz, L.B. !$#journal J. Immunol. (1990) 145:2652-2661 !$#title Identification of a cathepsin G-like proteinase in the MC-TC !1type of human mast cell. !$#cross-references MUID:91010743; PMID:2212656 !$#accession A60772 !'##molecule_type protein !'##residues 22-27,'S',29-56 ##label SCH COMMENT Functions of this chymotrypsin-like serine proteinase after !1mast cell degranulation include degradation of extracellular !1matrix and modification of vasoactive peptides. In heart, !1much of the cleavage of angiotensin I to angiotensin II is !1accomplished by this enzyme rather than by angiotensin !1converting enzyme. GENETICS !$#gene GDB:CMA1 !'##cross-references GDB:127603; OMIM:118940 !$#map_position 14q11.2-14q11.2 !$#introns 20/1; 70/2; 115/3; 200/3 CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS glycoprotein; hydrolase; serine proteinase FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-21 #domain propeptide #status predicted #label PRO\ !$22-247 #product chymase #status experimental #label MAT\ !$22-240 #domain trypsin homology #label TRY\ !$66,110,203 #active_site His, Asp, Ser #status predicted\ !$80 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$103 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 247 #molecular-weight 27325 #checksum 8053 SEQUENCE /// ENTRY A35842 #type complete TITLE chymase (EC 3.4.21.39) precursor - dog ALTERNATE_NAMES mast cell protease I; skeletal muscle (SK) protease ORGANISM #formal_name Canis lupus familiaris #common_name dog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A35842; PT0062 REFERENCE A35842 !$#authors Caughey, G.H.; Raymond, W.W.; Vanderslice, P. !$#journal Biochemistry (1990) 29:5166-5171 !$#title Dog mast cell chymase: molecular cloning and !1characterization. !$#cross-references MUID:90335214; PMID:2378872 !$#accession A35842 !'##molecule_type mRNA !'##residues 1-249 ##label CAU !'##cross-references GB:J02904; NID:g163919; PIDN:AAA30835.1; !1PID:g163920 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE PT0062 !$#authors Caughey, G.H.; Viro, N.F.; Lazarus, S.C.; Nadel, J.A. !$#journal Biochim. Biophys. Acta (1988) 952:142-149 !$#title Purification and characterization of dog mastocytoma !1chymase: identification of an octapeptide conserved in !1chymotryptic leukocyte proteinases. !$#cross-references MUID:88107816; PMID:3122835 !$#accession PT0062 !'##molecule_type protein !'##residues 22-28,'R',30-37,'Q',39-44,'T',46 ##label CA2 CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS glycoprotein; hydrolase; serine proteinase; skeletal muscle FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-249 #product chymase #status predicted #label MAT\ !$22-240 #domain trypsin homology #label TRY\ !$66,110,203 #active_site His, Asp, Ser #status predicted\ !$121,155 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 249 #molecular-weight 27811 #checksum 9005 SEQUENCE /// ENTRY A46504 #type complete TITLE chymase (EC 3.4.21.39) precursor - mouse ALTERNATE_NAMES mast cell proteinase I ORGANISM #formal_name Mus musculus #common_name house mouse DATE 18-Jun-1993 #sequence_revision 27-Jun-1994 #text_change 18-Jun-1999 ACCESSIONS A46504; S26041; A30105; S35607 REFERENCE A46504 !$#authors Ghildyal, N.; McNeil, H.P.; Stechschulte, S.; Austen, K.F.; !1Silberstein, D.; Gurish, M.F.; Somerville, L.L.; Stevens, !1R.L. !$#journal J. Immunol. (1992) 149:2123-2129 !$#title IL-10 induces transcription of the gene for mouse mast cell !1protease-1, a serine protease preferentially expressed in !1mucosal mast cells of Trichinella spiralis-infected mice. !$#cross-references MUID:92388686; PMID:1517575 !$#accession A46504 !'##molecule_type DNA !'##residues 1-246 ##label GHI !'##cross-references GB:S44609; NID:g255141; PIDN:AAB23194.1; !1PID:g255142 !'##experimental_source rIL-10 treated bone marrow !'##note sequence extracted from NCBI backbone (NCBIP:113144) REFERENCE S26041 !$#authors Huang, R.; Blom, T.; Hellman, L. !$#journal Eur. J. Immunol. (1991) 21:1611-1621 !$#title Cloning and structural analysis of MMCP-1, MMCP-4 and !1MMCP-5, three mouse mast cell-specific serine proteases. !$#cross-references MUID:91285010; PMID:2060576 !$#accession S26041 !'##molecule_type DNA !'##residues 1-246 ##label HUA !'##cross-references EMBL:X68803; NID:g53154; PIDN:CAA48703.1; !1PID:g53155 !'##experimental_source strain Balb/c REFERENCE A30105 !$#authors Trong, H.L.; Newlands, G.F.J.; Miller, H.R.P.; Charbonneau, !1H.; Neurath, H.; Woodbury, R.G. !$#journal Biochemistry (1989) 28:391-395 !$#title Amino acid sequence of a mouse mucosal mast cell protease. !$#cross-references MUID:89207558; PMID:2706264 !$#accession A30105 !'##molecule_type protein !'##residues 21-246 ##label TRO REFERENCE S35607 !$#authors Newlands, G.F.J.; Knox, D.P.; Pirie-Shepherd, S.R.; Miller, !1H.R.P. !$#journal Biochem. J. (1993) 294:127-135 !$#title Biochemical and immunological characterization of multiple !1glycoforms of mouse mast cell protease 1: comparison with an !1isolated murine serosal mast cell protease (MMCP-4). !$#cross-references MUID:93371351; PMID:8363563 !$#accession S35607 !'##status preliminary !'##molecule_type protein !'##residues 21-49 ##label NEW GENETICS !$#gene MMCP-1 !$#introns 20/1; 70/2; 115/3; 200/3 CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS glycoprotein; hydrolase; mast cell; serine proteinase FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-20 #domain propeptide #status predicted #label PRO\ !$21-246 #product chymase #status experimental #label MAT\ !$21-239 #domain trypsin homology #label TRY\ !$50-66,143-208, !$174-187 #disulfide_bonds #status predicted\ !$65,109,202 #active_site His, Asp, Ser #status predicted\ !$102 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 246 #molecular-weight 27013 #checksum 4873 SEQUENCE /// ENTRY PRRTG #type complete TITLE mast cell proteinase II (EC 3.4.21.-) precursor - rat ALTERNATE_NAMES group-specific proteinase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Nov-1980 #sequence_revision 19-Oct-1995 #text_change 18-Jun-1999 ACCESSIONS A29548; A00957 REFERENCE A92636 !$#authors Benfey, P.N.; Yin, F.H.; Leder, P. !$#journal J. Biol. Chem. (1987) 262:5377-5384 !$#title Cloning of the mast cell protease, RMCP II. Evidence for !1cell-specific expression and a multi-gene family. !$#cross-references MUID:87165980; PMID:3549719 !$#accession A29548 !'##molecule_type DNA; mRNA !'##residues 1-247 ##label BEN !'##cross-references GB:J02712; NID:g205335; PIDN:AAA66284.1; !1PID:g205336 REFERENCE A00957 !$#authors Woodbury, R.G.; Katunuma, N.; Kobayashi, K.; Titani, K.; !1Neurath, H. !$#journal Biochemistry (1978) 17:811-819 !$#title Covalent structure of a group-specific protease from rat !1small intestine. !$#cross-references MUID:78124137; PMID:629933 !$#accession A00957 !'##molecule_type protein !'##residues 21-237,'T',239-244 ##label WOO !'##experimental_source small intestine COMMENT This enzyme has chymotrypsin-like specificity toward small !1substrates. It is found in all mast cells, although at !1higher concentrations it occurs specifically in the atypical !1mast cells of the gut and lung. GENETICS !$#introns 19/1; 69/2; 124/3; 199/3 CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS hydrolase; mast cell; serine proteinase FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-247 #product mast cell proteinase II #status predicted !8#label MAT\ !$21-239 #domain trypsin homology #label TRY\ !$50-66,143-208, !$174-187 #disulfide_bonds #status predicted\ !$65,109,202 #active_site His, Asp, Ser #status predicted SUMMARY #length 247 #molecular-weight 27101 #checksum 7370 SEQUENCE /// ENTRY A31372 #type complete TITLE granzyme A (EC 3.4.21.78) precursor [validated] - human ALTERNATE_NAMES cytotoxic T-lymphocyte proteinase; cytotoxic T-lymphocyte tryptase; cytotoxic T-lymphocyte-associated serine esterase 3; granzyme 1; Hanukah factor ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1990 #sequence_revision 07-Jul-1995 #text_change 08-Dec-2000 ACCESSIONS A31372; A30525; A30526; A28943 REFERENCE A31372 !$#authors Gershenfeld, H.K.; Hershberger, R.J.; Shows, T.B.; Weissman, !1I.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:1184-1188 !$#title Cloning and chromosomal assignment of a human cDNA encoding !1a T cell- and natural killer cell-specific trypsin-like !1serine protease. !$#cross-references MUID:88125000; PMID:3257574 !$#accession A31372 !'##molecule_type mRNA !'##residues 1-262 ##label GER !'##cross-references GB:M18737; NID:g184022; PIDN:AAA52647.1; !1PID:g306845 REFERENCE A92823 !$#authors Hameed, A.; Lowrey, D.M.; Lichtenheld, M.; Podack, E.R. !$#journal J. Immunol. (1988) 141:3142-3147 !$#title Characterization of three serine esterases isolated from !1human IL-2 activated killer cells. !$#cross-references MUID:89009866; PMID:3262682 !$#accession A30525 !'##molecule_type protein !'##residues 29-40 ##label HAM REFERENCE A92824 !$#authors Kraehenbuehl, O.; Rey, C.; Jenne, D.; Lanzavecchia, A.; !1Groscurth, P.; Carrel, S.; Tschopp, J. !$#journal J. Immunol. (1988) 141:3471-3477 !$#title Characterization of granzymes A and B isolated from granules !1of cloned human cytotoxic T lymphocytes. !$#cross-references MUID:89035468; PMID:3263427 !$#accession A30526 !'##molecule_type protein !'##residues 29-39 ##label KRA REFERENCE A28943 !$#authors Poe, M.; Bennett, C.D.; Biddison, W.E.; Blake, J.T.; Norton, !1G.P.; Rodkey, J.A.; Sigal, N.H.; Turner, R.V.; Wu, J.K.; !1Zweerink, H.J. !$#journal J. Biol. Chem. (1988) 263:13215-13222 !$#title Human cytotoxic lymphocyte tryptase. Its purification from !1granules and the characterization of inhibitor and substrate !1specificity. !$#cross-references MUID:88330824; PMID:3047119 !$#accession A28943 !'##molecule_type protein !'##residues 29-38,'RX',41-46,'R',48-49,'X',51,'X',53 ##label POE !'##experimental_source CTL line Q31 !'##note details from reference A39027 (see entry A61021) suggest this !1protein is granzyme A rather than a related protein GENETICS !$#gene GDB:GZMA; CTLA3; HFSP !'##cross-references GDB:120601; OMIM:140050 !$#map_position 5q11-5q12 CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS glycoprotein; hydrolase; serine proteinase; T-cell FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-28 #domain propeptide #status predicted #label APT\ !$29-261 #product granzyme A #status experimental #label MPT\ !$29-254 #domain trypsin homology #label TRY\ !$54-70,148-218, !$179-197 #disulfide_bonds #status predicted\ !$69,114,212 #active_site His, Asp, Ser #status predicted\ !$170 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 262 #molecular-weight 28968 #checksum 685 SEQUENCE /// ENTRY A61021 #type complete TITLE granzyme B (EC 3.4.21.79) precursor [validated] - human ALTERNATE_NAMES CTL proteinase 1; cytotoxic T-lymphocyte proteinase 1; cytotoxic T-lymphocyte-associated serine esterase 1; granzyme 2; T-cell serine esterase ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1993 #sequence_revision 07-Jul-1995 #text_change 08-Dec-2000 ACCESSIONS A61021; JH0094; A32168; I56092; I71986; A31405; A28659; !1B30525; B30526; A39027 REFERENCE A61021 !$#authors Dahl, C.A.; Bach, F.H.; Chan, W.; Huebner, K.; Russo, G.; !1Croce, C.M.; Herfurth, T.; Cairns, J.S. !$#journal Hum. Genet. (1990) 84:465-470 !$#title Isolation of a cDNA clone encoding a novel form of granzyme !1B from human NK cells and mapping to chromosome 14. !$#cross-references MUID:90215752; PMID:2323780 !$#accession A61021 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-57 ##label DAH !'##note some mRNA transcripts contain an extended 5' region with an !1alternative initiator represented here as Met-1; although !1translation from Met-1 has been demonstrated in vitro, the !1majority of transcripts initiate translation at Met-35 REFERENCE JH0094 !$#authors Haddad, P.; Clement, M.V.; Bernard, O.; Larsen, C.J.; Degos, !1L.; Sasportes, M.; Mathieu-Mahul, D. !$#journal Gene (1990) 87:265-271 !$#title Structural organization of the hCTLA-1 gene encoding human !1granzyme B. !$#cross-references MUID:90236319; PMID:2332171 !$#accession JH0094 !'##molecule_type DNA !'##residues 35-127,'A',129-281 ##label HAD !'##cross-references GB:M28879; NID:g181185; PIDN:AAA75490.1; !1PID:g181186 REFERENCE A32168 !$#authors Klein, J.L.; Shows, T.B.; Dupont, B.; Trapani, J.A. !$#journal Genomics (1989) 5:110-117 !$#title Genomic organization and chromosomal assignment for a serine !1protease gene (CSPB) expressed by human cytotoxic !1lymphocytes. !$#cross-references MUID:89357968; PMID:2788607 !$#accession A32168 !'##molecule_type DNA !'##residues 34-245,'C',247-281 ##label KLE !'##cross-references GB:J03072 !'##note the authors translated the codon GTC for residue 106 as Gly, !1CAG for residue 121 as Ser, and TGT for residue 246 as Val REFERENCE I56092 !$#authors Caputo, A.; Sauer, D.E.; Rowe, P.B. !$#journal J. Immunol. (1990) 145:737-744 !$#title Nucleotide sequence and genomic organization of a human T !1lymphocyte serine protease gene. !$#cross-references MUID:90308320; PMID:2365998 !$#accession I56092 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 35-281 ##label CAP !'##cross-references GB:M38193; NID:g825611; PIDN:AAA67124.1; !1PID:g306682 REFERENCE I55992 !$#authors Schmid, J.; Weissmann, C. !$#journal J. Immunol. (1987) 139:250-256 !$#title Induction of mRNA for a serine protease and a !1beta-thromboglobulin-like protein in mitogen-stimulated !1human leukocytes. !$#cross-references MUID:87224164; PMID:2953813 !$#accession I71986 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 35-281 ##label RE2 !'##cross-references GB:M17016; NID:g338295; PIDN:AAA36627.1; !1PID:g338296 REFERENCE A31405 !$#authors Trapani, J.A.; Klein, J.L.; White, P.C.; Dupont, B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:6924-6928 !$#title Molecular cloning of an inducible serine esterase gene from !1human cytotoxic lymphocytes. !$#cross-references MUID:88320548; PMID:3261871 !$#accession A31405 !'##molecule_type mRNA !'##residues 35-105,'G',107-281 ##label TRA !'##cross-references GB:J04071; NID:g181136; PIDN:AAA52118.1; !1PID:g181137 REFERENCE A28659 !$#authors Caputo, A.; Fahey, D.; Lloyd, C.; Vozab, R.; McCairns, E.; !1Rowe, P.B. !$#journal J. Biol. Chem. (1988) 263:6363-6369 !$#title Structure and differential mechanisms of regulation of !1expression of a serine esterase gene in activated human T !1lymphocytes. !$#cross-references MUID:88198184; PMID:3258865 !$#accession A28659 !'##molecule_type mRNA !'##residues 35-88,'R',90-127,'A',129-281 ##label CA2 !'##cross-references GB:J03189; NID:g338010; PIDN:AAA36603.1; !1PID:g338011 REFERENCE A92823 !$#authors Hameed, A.; Lowrey, D.M.; Lichtenheld, M.; Podack, E.R. !$#journal J. Immunol. (1988) 141:3142-3147 !$#title Characterization of three serine esterases isolated from !1human IL-2 activated killer cells. !$#cross-references MUID:89009866; PMID:3262682 !$#accession B30525 !'##molecule_type protein !'##residues 55-74 ##label HAM REFERENCE A92824 !$#authors Kraehenbuehl, O.; Rey, C.; Jenne, D.; Lanzavecchia, A.; !1Groscurth, P.; Carrel, S.; Tschopp, J. !$#journal J. Immunol. (1988) 141:3471-3477 !$#title Characterization of granzymes A and B isolated from granules !1of cloned human cytotoxic T lymphocytes. !$#cross-references MUID:89035468; PMID:3263427 !$#accession B30526 !'##molecule_type protein !'##residues 55-66 ##label KRA REFERENCE A39027 !$#authors Poe, M.; Blake, J.T.; Boulton, D.A.; Gammon, M.; Sigal, !1N.H.; Wu, J.K.; Zweerink, H.J. !$#journal J. Biol. Chem. (1991) 266:98-103 !$#title Human cytotoxic lymphocyte granzyme B. Its purification from !1granules and the characterization of substrate and inhibitor !1specificity. !$#cross-references MUID:91093203; PMID:1985927 !$#accession A39027 !'##molecule_type protein !'##residues 55-72 ##label POE !'##experimental_source CTL line Q31 COMMENT This enzyme is probably necessary for target cell lysis in !1cell-mediated immune responses. GENETICS !$#gene GDB:GZMB; CTLA1; CSPB; CCPI; CGL-1; CSP-B !'##cross-references GDB:120744; OMIM:123910 !$#map_position 14q11.2-14q11.2 !$#introns 53/1; 102/2; 147/3; 234/3 !$#note the list of introns may be incomplete CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS alternative initiators; glycoprotein; hydrolase; serine !1proteinase; T-cell FEATURE !$1-52 #domain (or 35-52) signal sequence #status predicted !8#label SIG\ !$53-54 #domain activation peptide #status predicted #label !8ACP\ !$55-281 #product cytotoxic T-lymphocyte proteinase 1 #status !8experimental #label MAT\ !$55-274 #domain trypsin homology #label TRY\ !$83-99,176-243, !$207-222 #disulfide_bonds #status predicted\ !$98,142,237 #active_site His, Asp, Ser #status predicted\ !$105,138 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 281 #molecular-weight 31392 #checksum 3766 SEQUENCE /// ENTRY PRMSCL #type complete TITLE granzyme B (EC 3.4.21.79) precursor - mouse ALTERNATE_NAMES CTLA-1 protein; cytotoxic cell proteinase 1 (CPPI); cytotoxic T-cell-specific proteinase 1 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 19-May-2000 ACCESSIONS A94288; A93382; A28952; B26944; I48937; A00956 REFERENCE A94288 !$#authors Lobe, C.G.; Finlay, B.B.; Paranchych, W.; Paetkau, V.H.; !1Bleackley, R.C. !$#journal Science (1986) 232:858-861 !$#title Novel serine proteases encoded by two cytotoxic T !1lymphocyte-specific genes. !$#cross-references MUID:86208120; PMID:3518058 !$#accession A94288 !'##molecule_type mRNA !'##residues 1-247 ##label LOB !'##cross-references GB:M12302; NID:g192452; PIDN:AAA37383.1; !1PID:g309154 REFERENCE A93382 !$#authors Brunet, J.F.; Dosseto, M.; Denizot, F.; Mattei, M.G.; Clark, !1W.R.; Haqqi, T.M.; Ferrier, P.; Nabholz, M.; !1Schmitt-Verhulst, A.M.; Luciani, M.F.; Golstein, P. !$#journal Nature (1986) 322:268-271 !$#title The inducible cytotoxic T-lymphocyte-associated gene !1transcript CTLA-1 sequence and gene localization to mouse !1chromosome 14. !$#cross-references MUID:86284960; PMID:3090449 !$#contents chromosome mapping !$#accession A93382 !'##molecule_type mRNA !'##residues 1-247 ##label BRU !'##cross-references EMBL:X04072; NID:g50586; PIDN:CAA27715.1; !1PID:g50587 REFERENCE A90536 !$#authors Lobe, C.G.; Upton, C.; Duggan, B.; Ehrman, N.; Letellier, !1M.; Bell, J.; McFadden, G.; Bleackley, R.C. !$#journal Biochemistry (1988) 27:6941-6946 !$#title Organization of two genes encoding cytotoxic T !1lymphocyte-specific serine proteases CCPI and CCPII. !$#cross-references MUID:89062424; PMID:3264185 !$#accession A28952 !'##molecule_type DNA !'##residues 1-247 ##label LO2 !'##cross-references GB:M22526; NID:g2226432; PIDN:AAB61756.1; !1PID:g201027 REFERENCE A90894 !$#authors Masson, D.; Tschopp, J. !$#journal Cell (1987) 49:679-685 !$#title A family of serine esterases in lytic granules of cytolytic !1T lymphocytes. !$#cross-references MUID:87215932; PMID:3555842 !$#accession B26944 !'##molecule_type protein !'##residues 21-40 ##label MAS REFERENCE I48934 !$#authors Ko, M.S.; Wang, X.; Horton, J.H.; Hagen, M.D.; Takahashi, !1N.; Maezaki, Y.; Nadeau, J.H. !$#journal Mamm. Genome (1994) 5:349-355 !$#title Genetic mapping of 40 cDNA clones on the mouse genome by !1PCR. !$#cross-references MUID:94319082; PMID:8043949 !$#accession I48937 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 227-247 ##label RES !'##cross-references EMBL:U05707; NID:g497035; PIDN:AAB60470.1; !1PID:g497036 COMMENT This enzyme is probably necessary for target cell lysis in !1cell-mediated immune responses. GENETICS !$#gene CTLA-1 !$#map_position 14 !$#introns 19/1; 68/2; 113/3; 200/3 CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS hydrolase; serine proteinase; T-cell FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-20 #domain propeptide #status predicted #label APT\ !$21-247 #product cytotoxic T-lymphocyte proteinase 1 #status !8predicted #label MPT\ !$21-240 #domain trypsin homology #label TRY\ !$49-65,142-209, !$173-188 #disulfide_bonds #status predicted\ !$64,108,203 #active_site His, Asp, Ser #status predicted SUMMARY #length 247 #molecular-weight 27470 #checksum 92 SEQUENCE /// ENTRY PRMSC2 #type complete TITLE granzyme C (EC 3.4.21.-) precursor - mouse ALTERNATE_NAMES CPPII; cytotoxic T-cell-specific proteinase 2; cytotoxic T-lymphocyte proteinase 2 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Jun-1989 #sequence_revision 14-Jul-1994 #text_change 18-Jun-1999 ACCESSIONS B28952; S03004; I49702; C26944 REFERENCE A90536 !$#authors Lobe, C.G.; Upton, C.; Duggan, B.; Ehrman, N.; Letellier, !1M.; Bell, J.; McFadden, G.; Bleackley, R.C. !$#journal Biochemistry (1988) 27:6941-6946 !$#title Organization of two genes encoding cytotoxic T !1lymphocyte-specific serine proteases CCPI and CCPII. !$#cross-references MUID:89062424; PMID:3264185 !$#accession B28952 !'##molecule_type DNA !'##residues 1-248 ##label LOB !'##cross-references GB:M22527; NID:g201028; PIDN:AAA85454.1; !1PID:g201029 REFERENCE S01006 !$#authors Bleackley, R.C.; Duggan, B.; Ehrman, N.; Lobe, C.G. !$#journal FEBS Lett. (1988) 234:153-159 !$#title Isolation of two cDNA sequences which encode cytotoxic cell !1proteases. !$#cross-references MUID:88271600; PMID:3292281 !$#accession S03004 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-248 ##label BLE !'##cross-references EMBL:X12822; NID:g50056; PIDN:CAA31309.1; !1PID:g50057 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1988 REFERENCE I49702 !$#authors Jenne, D.E.; Rey, C.; Masson, D.; Stanley, K.K.; Herz, J.; !1Plaetinck, G.; Tschopp, J. !$#journal J. Immunol. (1988) 140:318-323 !$#title cDNA cloning of granzyme C, a granule-associated serine !1protease of cytolytic T lymphocytes. !$#cross-references MUID:88088827; PMID:3257230 !$#accession I49702 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-68,'R',70-248 ##label JEN !'##cross-references GB:M18459; NID:g193621; PIDN:AAA37734.1; !1PID:g309274 REFERENCE A90894 !$#authors Masson, D.; Tschopp, J. !$#journal Cell (1987) 49:679-685 !$#title A family of serine esterases in lytic granules of cytolytic !1T lymphocytes. !$#cross-references MUID:87215932; PMID:3555842 !$#accession C26944 !'##molecule_type protein !'##residues 21-40 ##label MAS GENETICS !$#introns 19/1; 69/2; 114/3; 201/3 CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS hydrolase; serine proteinase; T-cell FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-20 #domain propeptide #status predicted #label APT\ !$21-248 #product granzyme C #status predicted #label MPT\ !$21-241 #domain trypsin homology #label TRY\ !$50-66,143-210, !$174-189 #disulfide_bonds #status predicted\ !$65,109,204 #active_site His, Asp, Ser #status predicted SUMMARY #length 248 #molecular-weight 27310 #checksum 6683 SEQUENCE /// ENTRY S01007 #type complete TITLE granzyme F (EC 3.4.21.-) precursor - mouse ALTERNATE_NAMES CTL proteinase 4; cytotoxic cell proteinase 4 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 03-Mar-1994 #sequence_revision 03-Mar-1994 #text_change 23-Mar-2001 ACCESSIONS S24940; A46473; S01007; S06178; C36172; A60419; F26944 REFERENCE S24939 !$#authors Prendergast, J.A.; Pinkoski, M.; Wolfenden, A.; Bleackley, !1R.C. !$#submission submitted to the EMBL Data Library, November 1990 !$#description Intron/exon organisation of the cytotoxic cell proteinase !1genes, CCP3, CCP4 and CCP5. !$#accession S24940 !'##molecule_type DNA !'##residues 1-248 ##label PRE !'##cross-references EMBL:X56989; NID:g50326; PIDN:CAA40307.1; !1PID:g50327 REFERENCE A46473 !$#authors Jenne, D.E.; Zimmer, M.; Garcia-Sanz, J.A.; Tschopp, J.; !1Lichter, P. !$#journal J. Immunol. (1991) 147:1045-1052 !$#title Genomic organization and subchromosomal in situ localization !1of the murine granzyme F, a serine protease expressed in !1CD8+ T cells. !$#cross-references MUID:91318146; PMID:1861068 !$#accession A46473 !'##molecule_type DNA !'##residues 1-248 ##label JE2 !'##cross-references GB:M96930; NID:g193639; PIDN:AAA37741.1; !1PID:g193640 !'##experimental_source cosmid clone gGRAF-1, spleen !'##note sequence extracted from NCBI backbone (NCBIN:45141, !1NCBIP:45142) REFERENCE S01006 !$#authors Bleackley, R.C.; Duggan, B.; Ehrman, N.; Lobe, C.G. !$#journal FEBS Lett. (1988) 234:153-159 !$#title Isolation of two cDNA sequences which encode cytotoxic cell !1proteases. !$#cross-references MUID:88271600; PMID:3292281 !$#accession S01007 !'##molecule_type mRNA !'##residues 1-248 ##label BLE !'##cross-references EMBL:X12823; NID:g50206; PIDN:CAA31310.1; !1PID:g50207 REFERENCE S06176 !$#authors Kwon, B.S.; Kestler, D.; Lee, E.; Wakulchik, M.; Young, !1J.D.E. !$#journal J. Exp. Med. (1988) 168:1839-1854 !$#title Isolation and sequence analysis of serine protease cDNAs !1from mouse cytolytic T lymphocytes. !$#cross-references MUID:89036001; PMID:3053963 !$#accession S06178 !'##molecule_type mRNA !'##residues 1-248 ##label KWO !'##cross-references EMBL:X14094; NID:g53030; PIDN:CAA32256.1; !1PID:g53031 REFERENCE A36172 !$#authors Jenne, D.; Rey, C.; Haefliger, J.A.; Qiao, B.Y.; Groscurth, !1P.; Tschopp, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:4814-4818 !$#title Identification and sequencing of cDNA clones encoding the !1granule-associated serine proteases granzymes D, E, and F of !1cytolytic T lymphocytes. !$#cross-references MUID:88263037; PMID:3260382 !$#accession C36172 !'##molecule_type mRNA !'##residues 1-248 ##label JEN !'##cross-references GB:J03257; NID:g193629; PIDN:AAA37738.1; !1PID:g193630 REFERENCE A60419 !$#authors Jiang, S.; Hasselkus-Light, C.S.; Ojcius, D.M.; Young, !1J.D.E. !$#journal Protein Expr. Purif. (1990) 1:77-80 !$#title Purification of a membrane-associated serine esterase from !1murine cytotoxic T lymphocytes by a single reverse-phase !1column. !$#cross-references MUID:93044519; PMID:2152187 !$#accession A60419 !'##molecule_type protein !'##residues 21-45 ##label JIA REFERENCE A90894 !$#authors Masson, D.; Tschopp, J. !$#journal Cell (1987) 49:679-685 !$#title A family of serine esterases in lytic granules of cytolytic !1T lymphocytes. !$#cross-references MUID:87215932; PMID:3555842 !$#accession F26944 !'##molecule_type protein !'##residues 21-40 ##label MAS COMMENT The family of granzymes probably participates in !1cell-mediated cytotoxicity. COMMENT This enzyme is stored in cytoplasmic granules in its fully !1processed, mature form. COMMENT Up to half of the molecular weight of this enzyme is !1carbohydrate. GENETICS !$#map_position 14 !$#introns 19/1; 69/2; 114/3; 201/3 CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS cytolysis; extracellular protein; glycoprotein; hydrolase; !1serine proteinase; T-cell FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-20 #domain propeptide #status predicted #label PRO\ !$21-248 #product granzyme F #status experimental #label MAT\ !$21-241 #domain trypsin homology #label TRY\ !$65,109,204 #active_site His, Asp, Ser #status predicted\ !$106,154,223 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 248 #molecular-weight 27642 #checksum 959 SEQUENCE /// ENTRY DBHU #type fragment TITLE complement factor D (EC 3.4.21.46) precursor [validated] - human (fragment) ALTERNATE_NAMES adipsin; C3 convertase activator ORGANISM #formal_name Homo sapiens #common_name man DATE 28-Aug-1985 #sequence_revision 31-Dec-1992 #text_change 08-Dec-2000 ACCESSIONS A40197; A00936; A60571; S66645 REFERENCE A40197 !$#authors White, R.T.; Damm, D.; Hancock, N.; Rosen, B.S.; Lowell, !1B.B.; Usher, P.; Flier, J.S.; Spiegelman, B.M. !$#journal J. Biol. Chem. (1992) 267:9210-9213 !$#title Human adipsin is identical to complement factor D and is !1expressed at high levels in adipose tissue. !$#cross-references MUID:92250520; PMID:1374388 !$#accession A40197 !'##molecule_type mRNA !'##residues 1-246 ##label WHI !'##cross-references GB:M84526 REFERENCE A00936 !$#authors Niemann, M.A.; Bhown, A.S.; Bennett, J.C.; Volanakis, J.E. !$#journal Biochemistry (1984) 23:2482-2486 !$#title Amino acid sequence of human D of the alternative complement !1pathway. !$#cross-references MUID:85000441; PMID:6383466 !$#accession A00936 !'##molecule_type protein !'##residues 19-44,'G',46-51,'Q',53-75,'TH',78,'P',80-83,'XXXITIE', !190-172,86-91,185-235,'T',237-242,'H',244-245 ##label NIE !'##note a few residues were assigned from the previously published !1sequence of Reid et al., Methods Enzymol. 80, 3728, 1981 REFERENCE A60571 !$#authors Miyata, T.; Oda, O.; Inagi, R.; Sugiyama, S.; Miyama, A.; !1Maeda, K.; Nakashima, I.; Yamanaka, N. !$#journal Mol. Immunol. (1990) 27:637-644 !$#title Molecular and functional identification and purification of !1complement component factor D from urine of patients with !1chronic renal failure. !$#cross-references MUID:90370044; PMID:2395435 !$#accession A60571 !'##molecule_type protein !'##residues 19-20,'XX',23-27,'XX',30-31,'XX',34,'X',36-40 ##label MIY REFERENCE S66645 !$#authors Balke, N.; Holtkamp, U.; Hoerl, W.H.; Tschesche, H. !$#journal FEBS Lett. (1995) 371:300-302 !$#title Inhibition of degranulation of human polymorphonuclear !1leukocytes by complement factor D. !$#cross-references MUID:96013156; PMID:7556615 !$#accession S66645 !'##status preliminary !'##molecule_type protein !'##residues 19-44,'C',46-48 ##label BAL COMMENT Factor D cleaves factor B when the latter is complexed with !1factor C3b, activating the C3bBb complex, which then becomes !1the C3 convertase of the alternate pathway. GENETICS !$#gene GDB:DF !'##cross-references GDB:132645; OMIM:134350 !$#map_position Xpter-Xqter CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS complement alternate pathway; hydrolase; plasma; serine !1proteinase FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-246 #product complement factor D (fragment) #status !8experimental #label MAT\ !$19-241 #domain trypsin homology #label TRY\ !$44-60,141-207, !$172-188,197-222 #disulfide_bonds #status predicted\ !$59,105,201 #active_site His, Asp, Ser #status predicted SUMMARY #length 246 #checksum 7612 SEQUENCE /// ENTRY WMMS28 #type complete TITLE complement factor D (EC 3.4.21.46) precursor - mouse ALTERNATE_NAMES adipocyte 28K proteinase; adipsin; C3 convertase activator; complement factor D homolog ORGANISM #formal_name Mus musculus #common_name house mouse DATE 13-Aug-1986 #sequence_revision 13-Aug-1986 #text_change 19-May-2000 ACCESSIONS C25952; A00937; A26105 REFERENCE A92553 !$#authors Phillips, M.; Djian, P.; Green, H. !$#journal J. Biol. Chem. (1986) 261:10821-10827 !$#title The nucleotide sequence of three genes participating in the !1adipose differentiation of 3T3 cells. !$#cross-references MUID:86278164; PMID:3015943 !$#accession C25952 !'##molecule_type DNA !'##residues 1-259 ##label PHI !'##cross-references GB:M13386; NID:g192033; PIDN:AAA37262.1; !1PID:g387105 REFERENCE A00937 !$#authors Cook, K.S.; Groves, D.L.; Min, H.Y.; Spiegelman, B.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:6480-6484 !$#title A developmentally regulated mRNA from 3T3 adipocytes encodes !1a novel serine protease homologue. !$#cross-references MUID:86016726; PMID:3901003 !$#accession A00937 !'##molecule_type mRNA !'##residues 1-259 ##label COO !'##cross-references GB:M11768; NID:g202166; PIDN:AAA40486.1; !1PID:g202167 !'##experimental_source strain Swiss White !'##note only one Ala is present in place of Ala-19 and Ala-20 in !1another equally abundant form; this heterogeneity presumably !1arises by alternative splicing of the 28K gene REFERENCE A26105 !$#authors Min, H.Y.; Spiegelman, B.M. !$#journal Nucleic Acids Res. (1986) 14:8879-8892 !$#title Adipsin, the adipocyte serine protease: gene structure and !1control of expression by tumor necrosis factor. !$#cross-references MUID:87066764; PMID:3024123 !$#accession A26105 !'##molecule_type mRNA !'##residues 1-259 ##label MIN !'##cross-references GB:X04673; NID:g49883; PIDN:CAA28378.1; PID:g581866 COMMENT Human complement factor D is synthesized primarily in cells !1of the macrophage/monocyte lineage and serves as the !1catalyst for the rate-limiting first step in the alternative !1pathway of complement activation. However, expression of the !1murine homolog is specific to adipose tissue. GENETICS !$#gene 28K !$#introns 19/1; 71/2; 120/3; 206/3 CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS adipose tissue; alternative splicing; hydrolase; serine !1proteinase FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-25 #domain propeptide #status predicted #label PRO\ !$26-259 #product adipsin #status predicted #label MAT\ !$26-249 #domain trypsin homology #label TRY\ !$51-67,149-215, !$180-196,205-230 #disulfide_bonds #status predicted\ !$66,115,209 #active_site His, Asp, Ser #status predicted SUMMARY #length 259 #molecular-weight 28057 #checksum 7139 SEQUENCE /// ENTRY I55608 #type complete TITLE complement factor D (EC 3.4.21.46) precursor - rat ALTERNATE_NAMES adipsin; C3 convertase activator; endogenous vascular elastase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 19-May-2000 #sequence_revision 19-May-2000 #text_change 19-May-2000 ACCESSIONS I55608; S19275 REFERENCE I55608 !$#authors Zhu, L.; Wigle, D.; Hinek, A.; Kobayashi, J.; Ye, C.; Zuker, !1M.; Dodo, H.; Keeley, F.W.; Rabinovitch, M. !$#journal J. Clin. Invest. (1994) 94:1163-1171 !$#title The endogenous vascular elastase that governs development !1and progression of monocrotaline-induced pulmonary !1hypertension in rats is a novel enzyme related to the serine !1proteinase adipsin [see comments]. !$#cross-references MUID:94365184; PMID:8083356 !$#accession I55608 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-263 ##label RES !'##cross-references GB:S73894; NID:g693721; PIDN:AAB31922.1; !1PID:g693722 !'##experimental_source pulmonary artery REFERENCE S19275 !$#authors Baker, B.C.; Campbell, C.J.; Grinham, C.J.; Turcatti, G. !$#journal Biochem. J. (1991) 279:775-779 !$#title Purification and partial characterization of rat factor D. !$#cross-references MUID:92061993; PMID:1953671 !$#accession S19275 !'##molecule_type protein !'##residues 26-50,'X',52-55 ##label BAK COMMENT Unlike its human and mouse counterparts, this molecule is !1N-glycosylated. COMPLEX monomer CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS complement alternate pathway; glycoprotein; hydrolase; !1plasma; serine proteinase FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-25 #domain propeptide #status predicted #label PRO\ !$26-263 #product adipsin #status predicted #label MAT\ !$26-249 #domain trypsin homology #label TRY\ !$46,124,256,260 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$51-67,149-215, !$180-196,205-230 #disulfide_bonds #status predicted\ !$66,115,209 #active_site His, Asp, Ser #status predicted SUMMARY #length 263 #molecular-weight 28442 #checksum 9058 SEQUENCE /// ENTRY TRHUAZ #type complete TITLE azurocidin precursor [validated] - human ALTERNATE_NAMES cationic antimicrobial protein CAP37; heparin-binding protein; neutrophil-derived chemotactic factor CAP37 ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1992 #sequence_revision 30-Sep-1993 #text_change 08-Dec-2000 ACCESSIONS A46268; A46455; S16450; S18520; S12881; S15445; S14738; !1B33913; A60708; B43600; A49211; A61502; B43981; PH0081; !1A33070 REFERENCE A46268 !$#authors Zimmer, M.; Medcalf, R.L.; Fink, T.M.; Mattmann, C.; !1Lichter, P.; Jenne, D.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:8215-8219 !$#title Three human elastase-like genes coordinately expressed in !1the myelomonocyte lineage are organized as a single genetic !1locus on 19pter. !$#cross-references MUID:92390417; PMID:1518849 !$#accession A46268 !'##molecule_type DNA !'##residues 1-251 ##label ZIM !'##cross-references GB:M96326; NID:g179301; PIDN:AAB59353.1; !1PID:g179302 !'##note sequence extracted from NCBI backbone (NCBIN:112883, !1NCBIN:112891, NCBIN:112893, NCBIN:112895, NCBIN:112897, !1NCBIP:112907) REFERENCE A46455 !$#authors Morgan, J.G.; Sukiennicki, T.; Pereira, H.A.; Spitznagel, !1J.K.; Guerra, M.E.; Larrick, J.W. !$#journal J. Immunol. (1991) 147:3210-3214 !$#title Cloning of the cDNA for the serine protease homolog CAP37/ !1azurocidin, a microbicidal and chemotactic protein from !1human granulocytes. !$#cross-references MUID:92013155; PMID:1919011 !$#accession A46455 !'##molecule_type mRNA !'##residues 1-251 ##label MOR !'##cross-references GB:M96326; NID:g179301; PIDN:AAB59353.1; !1PID:g179302 !'##note sequence extracted from NCBI backbone (NCBIN:60386, !1NCBIP:60395) REFERENCE S16450 !$#authors Almeida, R.P.; Melchior, M.; Campanelli, D.; Nathan, C.; !1Gabay, J.E. !$#journal Biochem. Biophys. Res. Commun. (1991) 177:688-695 !$#title Complementary DNA sequence of human neutrophil azurocidin, !1an antibiotic with extensive homology to serine proteases. !$#cross-references MUID:91264832; PMID:2049091 !$#accession S16450 !'##molecule_type mRNA !'##residues 3-251 ##label ALM !'##cross-references EMBL:X58794; NID:g28976; PIDN:CAA41601.1; !1PID:g28977 !$#accession S18520 !'##molecule_type protein !'##residues 47-51,'S',53-59,'T',61-62,'V',64-87 ##label AL2 REFERENCE S12881 !$#authors Pohl, J.; Pereira, H.A.; Martin, N.M.; Spitznagel, J.K. !$#journal FEBS Lett. (1990) 272:200-204 !$#title Amino acid sequence of CAP37, a human neutrophil !1granule-derived antibacterial and monocyte-specific !1chemotactic glycoprotein structurally similar to neutrophil !1elastase. !$#cross-references MUID:91032128; PMID:2226832 !$#accession S12881 !'##molecule_type protein !'##residues 27-248 ##label POH REFERENCE S15393 !$#authors Flodgaard, H.; Ostergaard, E.; Bayne, S.; Svendsen, A.; !1Thomsen, J.; Engels, M.; Wollmer, A. !$#journal Eur. J. Biochem. (1991) 197:535-547 !$#title Covalent structure of two novel neutrophile !1leucocyte-derived proteins of porcine and human origin. !1Neutrophile elastase homologues with strong monocyte and !1fibroblast chemotactic activities. !$#cross-references MUID:91224149; PMID:2026172 !$#accession S15445 !'##molecule_type protein !'##residues 27-129,'N',131-247 ##label FLO !'##note the sequence from Fig. 7 is inconsistent with that from Fig. 6 !1in having 190-Ile REFERENCE S14736 !$#authors Green, B.G.; Weston, H.; Ashe, B.M.; Doherty, J.; Finke, P.; !1Hagmann, W.; Lark, M.; Mao, J.; Maycock, A.; Moore, V.; !1Mumford, R.; Shah, S.; Walakovits, L.; Knight, W.B. !$#journal Arch. Biochem. Biophys. (1991) 286:284-292 !$#title PMN elastases: a comparison of the specificity of human !1isozymes and the enzyme from other species toward substrates !1and inhibitors. !$#cross-references MUID:91378304; PMID:1897955 !$#accession S14738 !'##molecule_type protein !'##residues 27-47 ##label GRE REFERENCE A33913 !$#authors Gabay, J.E.; Scott, R.W.; Campanelli, D.; Griffith, J.; !1Wilde, C.; Marra, M.N.; Seeger, M.; Nathan, C.F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:5610-5614 !$#title Antibiotic proteins of human polymorphonuclear leukocytes. !$#cross-references MUID:89315847; PMID:2501794 !$#accession B33913 !'##molecule_type protein !'##residues 27-46 ##label GAB REFERENCE A60708 !$#authors Pereira, H.A.; Shafer, W.M.; Pohl, J.; Martin, L.E.; !1Spitznagel, J.K. !$#journal J. Clin. Invest. (1990) 85:1468-1476 !$#title CAP37, a human neutrophil-derived chemotactic factor with !1monocyte specific activity. !$#cross-references MUID:90237224; PMID:2332502 !$#accession A60708 !'##molecule_type protein !'##residues 27-68 ##label PER REFERENCE A43600 !$#authors Wasiluk, K.R.; Skubitz, K.M.; Gray, B.H. !$#journal Infect. Immun. (1991) 59:4193-4200 !$#title Comparison of granule proteins from human polymorphonuclear !1leukocytes which are bactericidal toward Pseudomonas !1aeruginosa. !$#cross-references MUID:92040097; PMID:1937776 !$#accession B43600 !'##molecule_type protein !'##residues 27-48 ##label WAS REFERENCE A49211 !$#authors Miyasaki, K.T.; Bodeau, A.L. !$#journal Infect. Immun. (1992) 60:4973-4975 !$#title Human neutrophil azurocidin synergizes with leukocyte !1elastase and cathepsin G in the killing of Capnocytophaga !1sputigena. !$#cross-references MUID:93014226; PMID:1399008 !$#accession A49211 !'##molecule_type protein !'##residues 27-46 ##label MIY !'##note sequence extracted from NCBI backbone (NCBIP:116551) REFERENCE A61502 !$#authors Shellard, J.E.; Leitch, H.A.; Logan, P.M.; McMaster, W.R.; !1Levy, J.G. !$#journal Exp. Hematol. (1991) 19:136-142 !$#title Purification of an in vitro inhibitor of normal myelopoiesis !1using a monoclonal antibody directed to a common antigen of !1myelogenous leukemia (CAMAL). !$#cross-references MUID:91122218; PMID:1991495 !$#accession A61502 !'##molecule_type protein !'##residues 27-48 ##label SHE REFERENCE A43981 !$#authors Wilde, C.G.; Snable, J.L.; Griffith, J.E.; Scott, R.W. !$#journal J. Biol. Chem. (1990) 265:2038-2041 !$#title Characterization of two azurophil granule proteases with !1active-site homology to neutrophil elastase. !$#cross-references MUID:90130450; PMID:2404977 !$#accession B43981 !'##molecule_type protein !'##residues 27-35,'H',37-46;194-217 ##label WIL REFERENCE PH0081 !$#authors Pereira, H.A.; Spitznagel, J.K.; Pohl, J.; Wilson, D.E.; !1Morgan, J.; Palings, I.; Larrick, J.W. !$#journal Life Sci. (1990) 46:189-196 !$#title CAP 37, a 37 kD human neutrophil granule cationic protein !1shares homology with inflammatory proteinases. !$#cross-references MUID:90157837; PMID:2406527 !$#accession PH0081 !'##molecule_type protein !'##residues 27-67 ##label PE2 !'##experimental_source polymorphonuclear leukocyte COMMENT This protein is homologous to serine proteinases but lacks !1proteolytic activity. It is released from leukocyte granules !1and is chemotactic for monocytes during inflammation. It !1shows antimicrobial activity against a number of !1gram-negative bacteria. GENETICS !$#gene GDB:AZU1 !'##cross-references GDB:135033; OMIM:162815 !$#map_position 19p13.3-19p13.3 !$#introns 20/1; 72/2; 150/3; 198/3 CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS glycoprotein; inflammation FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-26 #domain amino-terminal propeptide #status predicted !8#label PRO\ !$27-248 #product azurocidin #status experimental #label MAT\ !$27-239 #domain trypsin homology #label TRY\ !$67,115,201 #region defective catalytic triad\ !$249-251 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$52-68 #disulfide_bonds #status experimental\ !$126,140,171 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$149-207,180-186, !$197-222 #disulfide_bonds #status predicted SUMMARY #length 251 #molecular-weight 26885 #checksum 5964 SEQUENCE /// ENTRY TRPGAZ #type complete TITLE azurocidin - pig ALTERNATE_NAMES heparin-binding protein ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 18-Jul-1997 ACCESSIONS S15393 REFERENCE S15393 !$#authors Flodgaard, H.; Ostergaard, E.; Bayne, S.; Svendsen, A.; !1Thomsen, J.; Engels, M.; Wollmer, A. !$#journal Eur. J. Biochem. (1991) 197:535-547 !$#title Covalent structure of two novel neutrophile !1leucocyte-derived proteins of porcine and human origin. !1Neutrophile elastase homologues with strong monocyte and !1fibroblast chemotactic activities. !$#cross-references MUID:91224149; PMID:2026172 !$#accession S15393 !'##molecule_type protein !'##residues 1-219 ##label FLO REFERENCE A37448 !$#authors Sorensen, H.H.; Thomsen, J.; Bayne, S.; Hojrup, P.; !1Roepstorff, P. !$#journal Biomed. Environ. Mass Spectrom. (1990) 19:713-720 !$#title Strategies for determination of disulphide bridges in !1proteins using plasma desorption mass spectrometry. !$#cross-references MUID:91167744; PMID:2076469 !$#contents annotation; disulfide bonds CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS glycoprotein FEATURE !$1-211 #domain trypsin homology #label TRY\ !$41,88,173 #region defective catalytic triad\ !$26-42,122-179, !$152-158 #disulfide_bonds #status experimental\ !$113,144 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 219 #molecular-weight 24301 #checksum 3315 SEQUENCE /// ENTRY ELHUL #type complete TITLE leukocyte elastase (EC 3.4.21.37) precursor [validated] - human ALTERNATE_NAMES inflammatory serine proteinase; medullasin; neutrophil elastase ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 08-Dec-2000 ACCESSIONS A31976; S04954; S06241; A27064; S00631; A28370; A34570; !1A05293; A25907; S14736 REFERENCE A31976 !$#authors Takahashi, H.; Nukiwa, T.; Yoshimura, K.; Quick, C.D.; !1States, D.J.; Holmes, M.D.; Whang-Peng, J.; Knutsen, T.; !1Crystal, R.G. !$#journal J. Biol. Chem. (1988) 263:14739-14747 !$#title Structure of the human neutrophil elastase gene. !$#cross-references MUID:89008342; PMID:2902087 !$#accession A31976 !'##molecule_type DNA !'##residues 1-267 ##label TAK !'##cross-references GB:M20203; GB:J04032; NID:g189147; PIDN:AAA36359.1; !1PID:g386981 REFERENCE S04954 !$#authors Farley, D.; Travis, J.; Salvesen, G. !$#journal Biol. Chem. Hoppe-Seyler (1989) 370:737-744 !$#title The human neutrophil elastase gene. Analysis of the !1nucleotide sequence reveals three distinct classes of !1repetitive DNA. !$#cross-references MUID:89374820; PMID:2775493 !$#accession S04954 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-267 ##label FAR REFERENCE S06241 !$#authors Nakamura, H.; Okano, K.; Aoki, Y.; Shimizu, H.; Naruto, M. !$#journal Nucleic Acids Res. (1987) 15:9601-9602 !$#title Nucleotide sequence of human bone marrow serine protease !1(medullasin) gene. !$#cross-references MUID:88067782; PMID:3479752 !$#accession S06241 !'##status preliminary; translation not shown !'##molecule_type DNA !'##residues 1-267 ##label NAK !'##cross-references EMBL:Y00477; NID:g34529; PIDN:CAA68537.1; !1PID:g296665 REFERENCE A27064 !$#authors Okano, K.; Aoki, Y.; Sakurai, T.; Kajitani, M.; Kanai, S.; !1Shimazu, T.; Shimizu, H.; Naruto, M. !$#journal J. Biochem. (1987) 102:13-16 !$#title Molecular cloning of complementary DNA for human medullasin: !1an inflammatory serine protease in bone marrow cells. !$#cross-references MUID:88032918; PMID:2822677 !$#accession A27064 !'##molecule_type mRNA !'##residues 30-267 ##label OKA !'##cross-references EMBL:X05875; NID:g34532; PIDN:CAA29300.1; !1PID:g1335212 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE S00631 !$#authors Farley, D.; Salvesen, G.; Travis, J. !$#journal Biol. Chem. Hoppe-Seyler (1988) 369(Suppl.):3-7 !$#title Molecular cloning of human neutrophil elastase. !$#cross-references MUID:89076526; PMID:2462434 !$#accession S00631 !'##molecule_type mRNA !'##residues 123-267 ##label FA2 !'##cross-references GB:M27783; NID:g182055; PIDN:AAA35792.1; !1PID:g182056 !'##note the authors translated the codon TTC for residue 218 as Pro REFERENCE A28370 !$#authors Takahashi, H.; Nukiwa, T.; Basset, P.; Crystal, R.G. !$#journal J. Biol. Chem. (1988) 263:2543-2547 !$#title Myelomonocytic cell lineage expression of the neutrophil !1elastase gene. !$#cross-references MUID:88115408; PMID:3422232 !$#accession A28370 !'##molecule_type mRNA !'##residues 75-267 ##label TA2 !'##cross-references GB:J03545; NID:g182050; PIDN:AAA52378.1; !1PID:g182051 REFERENCE A34570 !$#authors Okano, K.; Aoki, Y.; Shimizu, H.; Naruto, M. !$#journal Biochem. Biophys. Res. Commun. (1990) 167:1326-1332 !$#title Functional expression of human leukocyte elastase (HLE)/ !1medullasin in eukaryotic cells. !$#cross-references MUID:90211319; PMID:2322278 !$#accession A34570 !'##molecule_type mRNA !'##residues 1-267 ##label OK2 !'##cross-references GB:M34379; NID:g187116; PIDN:AAA36173.1; !1PID:g307123 REFERENCE A94428 !$#authors Travis, J.; Giles, P.J.; Porcelli, L.; Reilly, C.F.; Baugh, !1R.; Powers, J. !$#book Protein Degradation in Health and Disease, Ciba Foundation !1Symposium 75, 51-68, 1980 !$#accession A05293 !'##molecule_type protein !'##residues 30-66,'G',68-73,'D',75,78-82,'E',84-89,'T',91-94,'PT', !197-100,'L',102-103 ##label TRA !'##experimental_source neutrophil granulocytes REFERENCE A25907 !$#authors Sinha, S.; Watorek, W.; Karr, S.; Giles, J.; Bode, W.; !1Travis, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:2228-2232 !$#title Primary structure of human neutrophil elastase. !$#cross-references MUID:87175647; PMID:3550808 !$#accession A25907 !'##molecule_type protein !'##residues 30-247 ##label SIN !'##note the sequence from Fig. 1 is inconsistent with that from Fig. 2 !1in having 107-Asp REFERENCE S14736 !$#authors Green, B.G.; Weston, H.; Ashe, B.M.; Doherty, J.; Finke, P.; !1Hagmann, W.; Lark, M.; Mao, J.; Maycock, A.; Moore, V.; !1Mumford, R.; Shah, S.; Walakovits, L.; Knight, W.B. !$#journal Arch. Biochem. Biophys. (1991) 286:284-292 !$#title PMN elastases: a comparison of the specificity of human !1isozymes and the enzyme from other species toward substrates !1and inhibitors. !$#cross-references MUID:91378304; PMID:1897955 !$#accession S14736 !'##molecule_type protein !'##residues 30-50 ##label GRE COMMENT This is a lysosomal proteinase found in the azurophil !1granules of neutrophils. COMMENT This elastase cleaves preferentially bonds after Ala and !1Val. It is believed to be one of the major agents !1responsible for tissue destruction in emphysema and !1rheumatoid arthritis. GENETICS !$#gene GDB:ELA2 !'##cross-references GDB:118792; OMIM:130130 !$#map_position 19p13.3-19p13.3 !$#introns 23/1; 75/2; 122/3; 199/3 CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS emphysema; glycoprotein; hydrolase; leukocyte; lysosome; !1rheumatoid arthritis; serine proteinase FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-29 #domain propeptide #status predicted #label PRO\ !$30-247 #product leukocyte elastase #status experimental !8#label MAT\ !$30-242 #domain trypsin homology #label TRY\ !$248-267 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$55-71,151-208, !$181-187,198-223 #disulfide_bonds #status experimental\ !$70,117,202 #active_site His, Asp, Ser #status predicted\ !$88 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$124,173 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 267 #molecular-weight 28518 #checksum 2080 SEQUENCE /// ENTRY PRHU3 #type complete TITLE proteinase 3 (EC 3.4.21.-) precursor [validated] - human ALTERNATE_NAMES AGP7; C-ANCA antigen; neutrophil proteinase 4; p29; Wegener's granulomatosis autoantigen CONTAINS myeloblastin ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 20-Apr-2001 ACCESSIONS A45080; B46268; A43983; JH0331; A33751; S11091; A61176; !1A60148; A43982; A43981; C33913; A60481; S10605; PL0230; !1A33059; S14406; S29674 REFERENCE A45080 !$#authors Sturrock, A.B.; Franklin, K.F.; Rao, G.; Marshall, B.C.; !1Rebentisch, M.B.; Lemons, R.S.; Hoidal, J.R. !$#journal J. Biol. Chem. (1992) 267:21193-21199 !$#title Structure, chromosomal assignment, and expression of the !1gene for proteinase-3. The Wegener's granulomatosis !1autoantigen. !$#cross-references MUID:93016043; PMID:1400430 !$#accession A45080 !'##molecule_type DNA !'##residues 1-254,'P' ##label STU !'##cross-references GB:M97911 !'##note sequence extracted from NCBI backbone (NCBIP:116205) REFERENCE A46268 !$#authors Zimmer, M.; Medcalf, R.L.; Fink, T.M.; Mattmann, C.; !1Lichter, P.; Jenne, D.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:8215-8219 !$#title Three human elastase-like genes coordinately expressed in !1the myelomonocyte lineage are organized as a single genetic !1locus on 19pter. !$#cross-references MUID:92390417; PMID:1518849 !$#accession B46268 !'##molecule_type DNA !'##residues 1-118,'V',120-134,'AT',137-256 ##label ZIM !'##note sequence extracted from NCBI backbone (NCBIN:112898, !1NCBIN:112900, NCBIN:112902, NCBIN:112904, NCBIN:112906, !1NCBIP:112908) REFERENCE A43983 !$#authors Labbaye, C.; Musette, P.; Cayre, Y.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:9253-9256 !$#title Wegener autoantigen and myeloblastin are encoded by a single !1mRNA. !$#cross-references MUID:92021028; PMID:1681549 !$#accession A43983 !'##molecule_type mRNA !'##residues 1-69,'P',71-256 ##label LA2 !'##cross-references GB:M75154; NID:g187398; PIDN:AAA59558.1; !1PID:g187399 REFERENCE JH0331 !$#authors Campanelli, D.; Melchior, M.; Fu, Y.; Nakata, M.; Shuman, !1H.; Nathan, C.; Gabay, J.E. !$#journal J. Exp. Med. (1990) 172:1709-1715 !$#title Cloning of cDNA for proteinase 3: a serine protease, !1antibiotic, and autoantigen from human neutrophils. !$#cross-references MUID:91079774; PMID:2258701 !$#accession JH0331 !'##molecule_type mRNA !'##residues 'R',3-118,'V',120-134,'AT',137-254,'P' ##label CAM !'##cross-references GB:X55668; NID:g35687; PIDN:CAA39203.1; !1PID:g1335280 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE A33751 !$#authors Bories, D.; Raynal, M.C.; Solomon, D.H.; Darzynkiewicz, Z.; !1Cayre, Y.E. !$#journal Cell (1989) 59:959-968 !$#title Down-regulation of a serine protease, myeloblastin, causes !1growth arrest and differentiation of promyelocytic leukemia !1cells. !$#cross-references MUID:90090622; PMID:2598267 !$#accession A33751 !'##molecule_type mRNA !'##residues 42-256 ##label BOR !'##cross-references GB:M29142; NID:g188983; PIDN:AAA36342.1; !1PID:g188984 !'##note the authors translated the codon GGG for residue 49 as Glu, GGC !1for residue 52 as Glu, GGA for residue 57 as Glu, and GGC !1for residue 58 as Glu REFERENCE S11091 !$#authors Jenne, D.E.; Tschopp, J.; Luedemann, J.; Utecht, B.; Gross, !1W.L. !$#journal Nature (1990) 346:520 !$#title Wegener's autoantigen decoded. !$#cross-references MUID:90332035; PMID:2377228 !$#accession S11091 !'##molecule_type mRNA !'##residues 20-56 ##label JEN REFERENCE A61176 !$#authors Musette, P.; Labbaye, C.; Dorner, M.H.; Cayre, Y.E.; !1Casanova, J.L.; Kourilsky, P. !$#journal Blood (1991) 77:1398-1399 !$#title Wegener's autoantigen and leukemia. !$#cross-references MUID:91159650; PMID:2001463 !$#accession A61176 !'##molecule_type mRNA !'##residues 1-42 ##label MUS !'##cross-references EMBL:X56606; NID:g35189; PIDN:CAA39943.1; !1PID:g35190 REFERENCE A60148 !$#authors Goldschmeding, R.; Dolman, K.M.; Van Den Ende, M.E.; Van Der !1Meer-Gerritsen, C.H.; Sonnenberg, A.; Von Dem Borne, !1A.E.G.K. !$#journal APMIS Suppl. (1990) 19:26-27 !$#title The relation of 29 kD C-ANCA antigen to proteinase 3. !$#cross-references MUID:91136884; PMID:2285532 !$#accession A60148 !'##molecule_type protein !'##residues 28-48 ##label GOL REFERENCE A43982 !$#authors Rao, N.V.; Wehner, N.G.; Marshall, B.C.; Gray, W.R.; Gray, !1B.H.; Hoidal, J.R. !$#journal J. Biol. Chem. (1991) 266:9540-9548 !$#title Characterization of proteinase-3 (PR-3), a neutrophil serine !1proteinase. Structural and functional properties. !$#cross-references MUID:91236723; PMID:2033050 !$#accession A43982 !'##molecule_type protein !'##residues 28-61,'X',63,'D',65-67;228-244 ##label RAO REFERENCE A43981 !$#authors Wilde, C.G.; Snable, J.L.; Griffith, J.E.; Scott, R.W. !$#journal J. Biol. Chem. (1990) 265:2038-2041 !$#title Characterization of two azurophil granule proteases with !1active-site homology to neutrophil elastase. !$#cross-references MUID:90130450; PMID:2404977 !$#accession A43981 !'##molecule_type protein !'##residues 28-45,'E',47;196-208,'X',210-215,'X',217-219 ##label WIL REFERENCE A33913 !$#authors Gabay, J.E.; Scott, R.W.; Campanelli, D.; Griffith, J.; !1Wilde, C.; Marra, M.N.; Seeger, M.; Nathan, C.F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:5610-5614 !$#title Antibiotic proteins of human polymorphonuclear leukocytes. !$#cross-references MUID:89315847; PMID:2501794 !$#accession C33913 !'##molecule_type protein !'##residues 28-45,'E',47 ##label GAB REFERENCE A60481 !$#authors Niles, J.L.; McCluskey, R.T.; Ahmad, M.F.; Arnaout, M.A. !$#journal Blood (1989) 74:1888-1893 !$#title Wegener's granulomatosis autoantigen is a novel neutrophil !1serine proteinase. !$#cross-references MUID:90028708; PMID:2679910 !$#accession A60481 !'##molecule_type protein !'##residues 28-38,'X',40-47 ##label NI2 REFERENCE S10605 !$#authors Ohlsson, K.; Linder, C.; Rosengren, M. !$#journal Biol. Chem. Hoppe-Seyler (1990) 371:549-555 !$#title Monoclonal antibodies specific for neutrophil proteinase 4. !1Production and use for isolation of the enzyme. !$#cross-references MUID:91025622; PMID:2121162 !$#accession S10605 !'##molecule_type protein !'##residues 28-52 ##label OHL REFERENCE PL0230 !$#authors Luedemann, J.; Utecht, B.; Gross, W.L. !$#journal J. Exp. Med. (1990) 171:357-362 !$#title Anti-neutrophil cytoplasm antibodies in Wegener's !1granulomatosis recognize an elastinolytic enzyme. !$#cross-references MUID:90111630; PMID:1688612 !$#accession PL0230 !'##molecule_type protein !'##residues 28-37,'I',39-40,'I',41-43 ##label LUE COMMENT This polymorphonuclear leukocyte serine protease from !1azurophilic granules degrades a variety of extracellular !1matrix proteins in vitro. GENETICS !$#gene GDB:PRTN3 !'##cross-references GDB:126876; OMIM:177020 !$#map_position 19p13.3-19p13.3 !$#introns 21/1; 76/2; 123/3; 200/3 CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS glycoprotein; hydrolase; polymorphonuclear leukocyte; serine !1proteinase FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-27 #domain propeptide #status predicted #label PRO\ !$28-256 #product proteinase 3 #status experimental #label !8MAT\ !$28-243 #domain trypsin homology #label TRY\ !$56-72,152-209, !$182-188,199-224 #disulfide_bonds #status predicted\ !$71,118,203 #active_site His, Asp, Ser #status predicted\ !$129,174 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 256 #molecular-weight 27837 #checksum 4014 SEQUENCE /// ENTRY TRSMG #type complete TITLE trypsin (EC 3.4.21.4) precursor - Streptomyces griseus ORGANISM #formal_name Streptomyces griseus DATE 24-Apr-1984 #sequence_revision 12-May-1994 #text_change 07-May-1999 ACCESSIONS JQ1302; A00962 REFERENCE JQ1302 !$#authors Kim, J.C.; Cha, S.H.; Jeong, S.T.; Oh, S.K.; Byun, S.M. !$#journal Biochem. Biophys. Res. Commun. (1991) 181:707-713 !$#title Molecular cloning and nucleotide sequence of Streptomyces !1griseus trypsin gene. !$#cross-references MUID:92095977; PMID:1755852 !$#accession JQ1302 !'##molecule_type DNA !'##residues 1-259 ##label KIM !'##cross-references GB:M64471 !'##experimental_source strain ATCC10137 REFERENCE A00962 !$#authors Olafson, R.W.; Jurasek, L.; Carpenter, M.R.; Smillie, L.B. !$#journal Biochemistry (1975) 14:1168-1177 !$#title Amino acid sequence of Streptomyces griseus trypsin. !1Cyanogen bromide fragments and complete sequence. !$#cross-references MUID:75127940; PMID:804314 !$#accession A00962 !'##molecule_type protein !'##residues 37-95,98-259 ##label OLA REFERENCE A44574 !$#authors Read, R.J.; James, M.N.G. !$#journal J. Mol. Biol. (1988) 200:523 !$#title Refined crystal structure of Streptomyces griseus trypsin at !11.7 angstroms resolution. !$#cross-references MUID:88286735; PMID:3135412 !$#contents annotation; X-ray crystallography, 1.7 angstroms !$#note residues 96-97 modeled as Gly-Ala GENETICS !$#gene sprT CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS hydrolase; serine proteinase FEATURE !$1-32 #domain signal sequence #status predicted #label SIG\ !$33-36 #domain propeptide #status predicted #label PRO\ !$37-258 #product trypsin #status experimental #label MAT\ !$37-252 #domain trypsin homology #label TRY\ !$58-74,177-192, !$204-233 #disulfide_bonds #status experimental\ !$73,118,208 #active_site His, Asp, Ser #status experimental SUMMARY #length 259 #molecular-weight 26776 #checksum 4929 SEQUENCE /// ENTRY A57014 #type complete TITLE prostasin (EC 3.4.21.-) precursor - human ORGANISM #formal_name Homo sapiens #common_name man DATE 24-May-1996 #sequence_revision 24-May-1996 #text_change 03-Feb-2003 ACCESSIONS A57014; A54866 REFERENCE A57014 !$#authors Yu, J.X.; Chao, L.; Chao, J. !$#journal J. Biol. Chem. (1995) 270:13483-13489 !$#title Molecular cloning, tissue-specific expression, and cellular !1localization of human prostasin mRNA. !$#cross-references MUID:95286644; PMID:7768952 !$#accession A57014 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-343 ##label RES !'##cross-references GB:L41351; NID:g862304; PIDN:AAC41759.1; !1PID:g862305 !'##experimental_source prostate !'##note parts of this sequence were determined by protein sequencing REFERENCE A54866 !$#authors Yu, J.X.; Chao, L.; Chao, J. !$#journal J. Biol. Chem. (1994) 269:18843-18848 !$#title Prostasin is a novel human serine proteinase from seminal !1fluid. Purification, tissue distribution, and localization !1in prostate gland. !$#cross-references MUID:94308140; PMID:8034638 !$#accession A54866 !'##molecule_type protein !'##residues 45-64 ##label YUA GENETICS !$#gene GDB:PRSS8 !'##cross-references GDB:676446; OMIM:600823 !$#map_position 16p11.2-16p11.2 CLASSIFICATION #superfamily trypsin; trypsin homology KEYWORDS glycoprotein; hydrolase; serine proteinase; transmembrane !1protein FEATURE !$1-32 #domain signal sequence #status predicted #label SIG\ !$33-44,45-343 #product prostasin #status predicted #label MAT\ !$33-44 #domain prostasin light chain #status predicted !8#label CHL\ !$45-343 #domain prostasin heavy chain #status predicted !8#label CHH\ !$45-281 #domain trypsin homology #label TRY\ !$323-341 #domain transmembrane #status predicted #label TMM1\ !$37-154,70-86, !$168-244,201-223, !$234-262 #disulfide_bonds #status predicted\ !$85,134,238 #active_site His, Asp, Ser #status predicted\ !$159 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 343 #molecular-weight 36431 #checksum 5606 SEQUENCE /// ENTRY HPHU1 #type complete TITLE haptoglobin precursor, allele 1 [validated] - human CONTAINS haptoglobin alpha chain; haptoglobin beta chain ORGANISM #formal_name Homo sapiens #common_name man DATE 19-Feb-1984 #sequence_revision 30-Sep-1987 #text_change 08-Dec-2000 ACCESSIONS A93521; A91321; A94703; A91004; A00917; A22704; A22864; !1A25739 REFERENCE A93521 !$#authors Brune, J.L.; Yang, F.; Barnett, D.R.; Bowman, B.H. !$#journal Nucleic Acids Res. (1984) 12:4531-4538 !$#title Evolution of haptoglobin: comparison of complementary DNA !1encoding Hpalpha(1S) and Hpalpha(2FS). !$#cross-references MUID:84247319; PMID:6330675 !$#accession A93521 !'##molecule_type mRNA !'##residues 1-347 ##label BRU !'##cross-references EMBL:X60037 REFERENCE A91321 !$#authors van der Straten, A.; Herzog, A.; Cabezon, T.; Bollen, A. !$#journal FEBS Lett. (1984) 168:103-107 !$#title Characterization of human haptoglobin cDNAs coding for !1alpha-2FS-beta and alpha-1S-beta variants. !$#cross-references MUID:84158941; PMID:6546723 !$#accession A91321 !'##molecule_type mRNA !'##residues 1-347 ##label VAN !'##cross-references EMBL:K01763; NID:g184316; PIDN:AAA52684.1; !1PID:g306880 REFERENCE A94703 !$#authors Kurosky, A.; Barnett, D.R.; Lee, T.H.; Touchstone, B.; Hay, !1R.E.; Arnott, M.S.; Bowman, B.H.; Fitch, W.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1980) 77:3388-3392 !$#title Covalent structure of human haptoglobin: a serine protease !1homolog. !$#cross-references MUID:81013890; PMID:6997877 !$#contents variant alpha-1S (slow); disulfide bonds !$#accession A94703 !'##molecule_type protein !'##residues 19-101;103-307,'N',309-320,'CS',323-337,'N',339-347 ##label !1KUR REFERENCE A91004 !$#authors Bensi, G.; Raugei, G.; Klefenz, H.; Cortese, R. !$#journal EMBO J. (1985) 4:119-126 !$#title Structure and expression of the human haptoglobin locus. !$#cross-references MUID:85257429; PMID:4018023 !$#contents variant alpha-1F (fast) !$#accession A91004 !'##molecule_type DNA !'##residues 3-69,'DK',72-347 ##label BEN !'##cross-references GB:X01793 REFERENCE A90931 !$#authors Kurosky, A.; Kim, H.H.; Touchstone, B. !$#journal Comp. Biochem. Physiol. B (1976) 55:453-459 !$#title Comparative sequence analysis of the N-terminal region of !1rat, rabbit, and dog haptoglobin beta-chains. !$#cross-references MUID:77025019; PMID:975782 !$#contents annotation; carbohydrate bound to beta chain REFERENCE A90747 !$#authors Malchy, B.; Dixon, G.H. !$#journal Can. J. Biochem. (1973) 51:249-264 !$#title Studies on the interchain disulfides of human haptoglobins. !$#cross-references MUID:73166302; PMID:4573324 !$#contents annotation; disulfide bonds in alpha chain COMMENT The sequence of the 1S variant is shown. There is a separate !1entry for haptoglobin allele 2 (see PIR:HPHU2). COMMENT The mature haptoglobin molecule is a dimer of heterodimers, !1the two chains of which, alpha and beta, arise from the same !1precursor molecule. COMMENT Each haptoglobin beta chain can bind an alpha-beta !1heterodimer of hemoglobin so that haptoglobin complexes with !1hemoglobin in a one-to-one ratio. COMMENT The haptoglobin-hemoglobin complex exceeds the kidney !1threshold for excretion, and thus haptoglobin prevents loss !1of iron and protects the kidneys from damage by hemoglobin. COMMENT The haptoglobin-hemoglobin complex is degraded in the liver !1(where haptoglobin is also synthesized). The parenchymal !1cells of the liver have a receptor that recognizes the !1conformational change in haptoglobin that results from its !1binding to hemoglobin. GENETICS !$#gene GDB:HP !'##cross-references GDB:119314; OMIM:140100 !$#map_position 16q22.2-16q22.2 !$#introns 2/2; 30/1; 64/1; 89/1 CLASSIFICATION #superfamily haptoglobin; complement factor H repeat !1homology; trypsin homology KEYWORDS acute phase; glycoprotein; hemoglobin binding; !1heterotetramer; iron transport; liver; plasma FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-101 #product haptoglobin alpha chain #status experimental !8#label ACH\ !$33-86 #domain complement factor H repeat homology #label !8FH2\ !$103-347 #product haptoglobin beta chain #status experimental !8#label BCH\ !$103-340 #domain trypsin homology #label TRY\ !$33 #disulfide_bonds interchain #status experimental\ !$52-86,90-207, !$250-281,292-322 #disulfide_bonds #status experimental\ !$125,148,152,182 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 347 #molecular-weight 38452 #checksum 1676 SEQUENCE /// ENTRY HPHUR #type complete TITLE haptoglobin-related protein precursor - human ORGANISM #formal_name Homo sapiens #common_name man DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 18-Jun-1999 ACCESSIONS A00919; A30360; I61855; I60126 REFERENCE A92532 !$#authors Maeda, N. !$#journal J. Biol. Chem. (1985) 260:6698-6709 !$#title Nucleotide sequence of the haptoglobin and !1haptoglobin-related gene pair. The haptoglobin-related gene !1contains a retrovirus-like element. !$#cross-references MUID:85207676; PMID:2987228 !$#accession A00919 !'##molecule_type DNA !'##residues 1-348 ##label MAE !'##cross-references GB:M10935 REFERENCE A30360 !$#authors Kuhajda, F.P.; Katumuluwa, A.I.; Pasternack, G.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:1188-1192 !$#title Expression of haptoglobin-related protein and its potential !1role as a tumor antigen. !$#cross-references MUID:89145208; PMID:2465547 !$#accession A30360 !'##molecule_type protein !'##residues 68-73,'E',75;92-99,'Q',101-103 ##label KUH !'##note the amino-terminal end of the mature alpha chain was found to !1be blocked REFERENCE I36941 !$#authors Erickson, L.M.; Kim, H.S.; Maeda, N. !$#journal Genomics (1992) 14:948-958 !$#title Junctions between genes in the haptoglobin gene cluster of !1primates. !$#cross-references MUID:93122805; PMID:1478675 !$#accession I61855 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-348 ##label RES !'##cross-references GB:M69197; NID:g292156; PIDN:AAA88079.1; !1PID:g292158 REFERENCE I60126 !$#authors Maeda, N.; McEvoy, S.M.; Harris, H.F.; Huisman, T.H.; !1Smithies, O. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:7395-7399 !$#title Polymorphisms in the human haptoglobin gene cluster: !1chromosomes with multiple haptoglobin-related (Hpr) genes. !$#cross-references MUID:87016954; PMID:2876426 !$#accession I60126 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 258-338,'H',340-348 ##label RE2 !'##cross-references GB:M13908; NID:g184320; PIDN:AAA52686.1; !1PID:g184321 !'##experimental_source an individual (C.G.) with multiple !1haptoglobin-related genes COMMENT This protein is expressed during pregnancy and in some !1breast carcinomas. It apparently functions like haptoglobin !1(see PIR:HPHU1). GENETICS !$#gene GDB:HPR !'##cross-references GDB:119316; OMIM:140210 !$#map_position 16q22.1-16q22.1 !$#introns 2/3; 31/1; 65/1; 90/1 !$#note humans are polymorphic in the number of Hpr genes CLASSIFICATION #superfamily haptoglobin; complement factor H repeat !1homology; trypsin homology KEYWORDS acute phase; blocked amino end; glycoprotein; hemoglobin !1binding; heterotetramer; iron transport; plasma FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-102 #product haptoglobin-related protein alpha chain !8#status predicted #label ALP\ !$34-87 #domain complement factor H repeat homology #label !8FH2\ !$104-348 #product haptoglobin-related protein beta chain !8#status predicted #label BET\ !$104-341 #domain trypsin homology #label TRY\ !$20 #modified_site blocked amino end (Leu) (in mature !8form) #status experimental\ !$53-87,91-208, !$251-282,293-323 #disulfide_bonds #status predicted\ !$126,149,153 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 348 #molecular-weight 39007 #checksum 3004 SEQUENCE /// ENTRY HPHU2 #type complete TITLE haptoglobin precursor, allele 2 [validated] - human ALTERNATE_NAMES haptoglobin-2 ORGANISM #formal_name Homo sapiens #common_name man DATE 19-Feb-1984 #sequence_revision 27-Nov-1985 #text_change 08-Dec-2000 ACCESSIONS A92532; B25739; A93973; A93485; I61854; A00918 REFERENCE A92532 !$#authors Maeda, N. !$#journal J. Biol. Chem. (1985) 260:6698-6709 !$#title Nucleotide sequence of the haptoglobin and !1haptoglobin-related gene pair. The haptoglobin-related gene !1contains a retrovirus-like element. !$#cross-references MUID:85207676; PMID:2987228 !$#accession A92532 !'##molecule_type DNA !'##residues 1-406 ##label MAE !'##cross-references GB:M10935; NID:g184327; PIDN:AAA88080.1; !1PID:g386783 REFERENCE A91321 !$#authors van der Straten, A.; Herzog, A.; Cabezon, T.; Bollen, A. !$#journal FEBS Lett. (1984) 168:103-107 !$#title Characterization of human haptoglobin cDNAs coding for !1alpha-2FS-beta and alpha-1S-beta variants. !$#cross-references MUID:84158941; PMID:6546723 !$#accession B25739 !'##molecule_type mRNA !'##residues 1-406 ##label VAN !'##cross-references EMBL:K01763 REFERENCE A93973 !$#authors Yang, F.; Brune, J.L.; Baldwin, W.D.; Barnett, D.R.; Bowman, !1B.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:5875-5879 !$#title Identification and characterization of human haptoglobin !1cDNA. !$#cross-references MUID:83300066; PMID:6310599 !$#accession A93973 !'##molecule_type mRNA !'##residues 1-69,'N',71-406 ##label YAN !'##cross-references EMBL:K00422; NID:g184322; PIDN:AAA52687.1; !1PID:g306882 REFERENCE A93485 !$#authors Raugei, G.; Bensi, G.; Colantuoni, V.; Romano, V.; Santoro, !1C.; Costanzo, F.; Cortese, R. !$#journal Nucleic Acids Res. (1983) 11:5811-5819 !$#title Sequence of human haptoglobin cDNA: evidence that the alpha !1and beta subunits are coded by the same mRNA. !$#cross-references MUID:83299252; PMID:6310515 !$#accession A93485 !'##molecule_type mRNA !'##residues 3-366,'N',368-406 ##label RAU !'##cross-references GB:M12387 REFERENCE A94703 !$#authors Kurosky, A.; Barnett, D.R.; Lee, T.H.; Touchstone, B.; Hay, !1R.E.; Arnott, M.S.; Bowman, B.H.; Fitch, W.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1980) 77:3388-3392 !$#title Covalent structure of human haptoglobin: a serine protease !1homolog. !$#cross-references MUID:81013890; PMID:6997877 !$#contents annotation; revisions to the alpha-2 chain deduced from !1comparisons with the alpha-1 chain REFERENCE A90747 !$#authors Malchy, B.; Dixon, G.H. !$#journal Can. J. Biochem. (1973) 51:249-264 !$#title Studies on the interchain disulfides of human haptoglobins. !$#cross-references MUID:73166302; PMID:4573324 !$#contents annotation; disulfide bonds REFERENCE I36941 !$#authors Erickson, L.M.; Kim, H.S.; Maeda, N. !$#journal Genomics (1992) 14:948-958 !$#title Junctions between genes in the haptoglobin gene cluster of !1primates. !$#cross-references MUID:93122805; PMID:1478675 !$#accession I61854 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-406 ##label RES !'##cross-references GB:M69197; NID:g292156; PIDN:AAA88078.1; !1PID:g292157 COMMENT This haptoglobin with a partial duplication in the alpha !1chain region is a common allelic variant (see PIR:HPHU1). GENETICS !$#gene GDB:HP !'##cross-references GDB:119314; OMIM:140100 !$#map_position 16q22.2-16q22.2 !$#introns 2/2; 30/1; 64/1; 89/1; 123/1; 148/1 CLASSIFICATION #superfamily haptoglobin; complement factor H repeat !1homology; trypsin homology KEYWORDS acute phase; duplication; glycoprotein; hemoglobin binding; !1heterotetramer; iron transport; liver; plasma FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-160 #product haptoglobin allele 2 alpha chain #status !8experimental #label ACH\ !$33-86 #domain complement factor H repeat homology #status !8atypical #label FH1\ !$92-145 #domain complement factor H repeat homology #status !8atypical #label FH2\ !$162-406 #product haptoglobin beta chain #status predicted !8#label BCH\ !$162-399 #domain trypsin homology #label TRY\ !$33,92 #disulfide_bonds interchain #status experimental\ !$52-86,111-145 #disulfide_bonds #status experimental\ !$184,207,211,241 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$309-340,351-381 #disulfide_bonds #status predicted SUMMARY #length 406 #molecular-weight 45205 #checksum 7252 SEQUENCE /// ENTRY HPMS #type complete TITLE haptoglobin precursor - mouse CONTAINS haptoglobin alpha chain; haptoglobin beta chain ORGANISM #formal_name Mus musculus #common_name house mouse DATE 23-Mar-1995 #sequence_revision 31-May-1996 #text_change 18-Jun-1999 ACCESSIONS A48918 REFERENCE A48918 !$#authors Yang, F.; Linehan, L.A.; Friedrichs, W.E.; Lalley, P.A.; !1Sakaguchi, A.Y.; Bowman, B.H. !$#journal Genomics (1993) 18:374-380 !$#title Characterization of the mouse haptoglobin gene. !$#cross-references MUID:94117006; PMID:8288241 !$#accession A48918 !'##molecule_type mRNA !'##residues 1-347 ##label YAN !'##cross-references GB:S67972; NID:g461137; PIDN:AAB29697.1; !1PID:g461138 !'##note sequence extracted from NCBI backbone (NCBIN:142156, !1NCBIP:142157); sequence inconsistent with nucleotide !1translation COMMENT The mature haptoglobin molecule is a dimer of heterodimers, !1the two chains of which, alpha and beta, arise from the same !1precursor molecule. COMMENT Haptoglobin is a plasma glycoprotein; haptoglobin forms a !1complex with hemoglobin released from erythrocytes by !1hemolysis and delivers it to the liver for degradation. GENETICS !$#gene Hp !$#map_position 8 CLASSIFICATION #superfamily haptoglobin; complement factor H repeat !1homology; trypsin homology KEYWORDS acute phase; glycoprotein; hemoglobin binding; !1heterotetramer; iron transport; liver; plasma FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-101 #product haptoglobin alpha chain #status predicted !8#label ACH\ !$33-86 #domain complement factor H repeat homology #label !8FH2\ !$103-347 #product haptoglobin beta chain #status predicted !8#label BCH\ !$103-340 #domain trypsin homology #label TRY\ !$33 #disulfide_bonds interchain #status predicted\ !$52-86,90-207, !$250-281,292-322 #disulfide_bonds #status predicted\ !$148,182,256,264 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 347 #molecular-weight 38845 #checksum 1902 SEQUENCE /// ENTRY HPRT #type complete TITLE haptoglobin precursor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1987 #sequence_revision 01-Dec-1995 #text_change 11-May-2000 ACCESSIONS A34784; A92487; A92429; A90931; A20881; A22505 REFERENCE A34784 !$#authors Marinkovic, S.; Baumann, H. !$#journal Mol. Cell. Biol. (1990) 10:1573-1583 !$#title Structure, hormonal regulation, and identification of the !1interleukin-6- and dexamethasone-responsive element of the !1rat haptoglobin gene. !$#cross-references MUID:90205837; PMID:2320005 !$#accession A34784 !'##molecule_type DNA !'##residues 1-347 ##label MAR !'##cross-references GB:M34230; GB:M34231; GB:M34232; NID:g204653; !1PIDN:AAA41348.1; PID:g204655 !'##note the authors translated the codon CTA for residue 220 as Gly, !1TGT for residue 221 as Tyr, CGG for residue 223 as Ser, TTG !1for residue 224 as Gly, GGG for residue 225 as Trp, and GCG !1for residue 226 as Gly REFERENCE A92487 !$#authors Goldstein, L.A.; Heath, E.C. !$#journal J. Biol. Chem. (1984) 259:9212-9217 !$#title Nucleotide sequence of rat haptoglobin cDNA. !1Characterization of the alpha-beta-subunit junction region !1of prohaptoglobin. !$#cross-references MUID:84264555; PMID:6204979 !$#accession A92487 !'##molecule_type mRNA !'##residues 76-219,'GY',222,'SGWG',227-331,'R',333-347 ##label GOL !'##cross-references GB:K01933; NID:g204656; PIDN:AAA41349.1; !1PID:g204657 REFERENCE A92429 !$#authors Hanley, J.M.; Haugen, T.H.; Heath, E.C. !$#journal J. Biol. Chem. (1983) 258:7858-7869 !$#title Biosynthesis and processing of rat haptoglobin. !$#cross-references MUID:83238370; PMID:6863267 !$#accession A92429 !'##molecule_type protein !'##residues 19-24,'D',26-43,103-127 ##label HAN !'##note the amino terminal of the mature chain was determined REFERENCE A90931 !$#authors Kurosky, A.; Kim, H.H.; Touchstone, B. !$#journal Comp. Biochem. Physiol. B (1976) 55:453-459 !$#title Comparative sequence analysis of the N-terminal region of !1rat, rabbit, and dog haptoglobin beta-chains. !$#cross-references MUID:77025019; PMID:975782 !$#accession A90931 !'##molecule_type protein !'##residues 103-142 ##label KUR !'##note the amino terminal of the mature chain was determined COMMENT The mature haptoglobin molecule is a dimer of heterodimers, !1the two chains of which, alpha and beta, arise from the same !1precursor molecule. COMMENT Haptoglobin is a plasma glycoprotein; haptoglobin forms a !1complex with hemoglobin released from erythrocytes by !1hemolysis and delivers it to the liver for degradation. CLASSIFICATION #superfamily haptoglobin; complement factor H repeat !1homology; trypsin homology KEYWORDS acute phase; glycoprotein; hemoglobin binding; !1heterotetramer; iron; liver; plasma FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-102 #product haptoglobin alpha chain #status predicted !8#label ACH\ !$33-86 #domain complement factor H repeat homology #label !8FH2\ !$103-347 #product haptoglobin beta chain #status predicted !8#label BCH\ !$103-340 #domain trypsin homology #label TRY\ !$90-207,250-281, !$292-322 #disulfide_bonds #status predicted\ !$148,152 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 347 #molecular-weight 38555 #checksum 7140 SEQUENCE /// ENTRY HPDG #type fragments TITLE haptoglobin precursor - dog (fragments) ORGANISM #formal_name Canis lupus familiaris #common_name dog DATE 09-Oct-1992 #sequence_revision 31-May-1996 #text_change 11-May-2000 ACCESSIONS JX0223; JX0224; B26503 REFERENCE JX0223 !$#authors Kumazaki, T.; Urushibara, N.; Ishii, S. !$#journal J. Biochem. (1992) 112:11-19 !$#title Amino acid sequence and disulfide-bridge location of canine !1haptoglobin. !$#cross-references MUID:93054403; PMID:1429498 !$#accession JX0223 !'##molecule_type protein !'##residues 1-83 ##label KU2 !'##experimental_source plasma !'##note Arg-84 was found at the end of some alpha chains; we have !1inserted it by homology with other haptoglobin precursor !1sequences !$#accession JX0224 !'##molecule_type protein !'##residues 85-329 ##label KU3 !'##experimental_source plasma REFERENCE A90931 !$#authors Kurosky, A.; Kim, H.H.; Touchstone, B. !$#journal Comp. Biochem. Physiol. B (1976) 55:453-459 !$#title Comparative sequence analysis of the N-terminal region of !1rat, rabbit, and dog haptoglobin beta-chains. !$#cross-references MUID:77025019; PMID:975782 !$#accession B26503 !'##molecule_type protein !'##residues 85-124 ##label KUR COMMENT The mature haptoglobin molecule is a dimer of heterodimers, !1the two chains of which, alpha and beta, arise from the same !1precursor molecule. COMMENT Haptoglobin is a plasma glycoprotein; haptoglobin forms a !1complex with hemoglobin released from erythrocytes by !1hemolysis and delivers it to the liver for degradation. CLASSIFICATION #superfamily haptoglobin; complement factor H repeat !1homology; trypsin homology KEYWORDS acute phase; glycoprotein; hemoglobin binding; !1heterotetramer; iron transport; liver; plasma FEATURE !$1-83 #product haptoglobin alpha chain #status experimental !8#label ALP\ !$15-68 #domain complement factor H repeat homology #label !8FH2\ !$85-329 #product haptoglobin beta chain #status experimental !8#label BET\ !$85-322 #domain trypsin homology #label TRY\ !$9,107,214 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$34-68,72-189, !$232-263,274-304 #disulfide_bonds #status experimental SUMMARY #length 329 #checksum 9614 SEQUENCE /// ENTRY HPRB #type fragments TITLE haptoglobin precursor - rabbit (fragments) CONTAINS haptoglobin alpha chain; haptoglobin beta chain ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 31-Mar-1988 #sequence_revision 31-May-1996 #text_change 11-May-2000 ACCESSIONS A19376; A26503 REFERENCE A19376 !$#authors Chow, V.; Murray, R.K.; Dixon, J.D.; Kurosky, A. !$#journal FEBS Lett. (1983) 153:275-279 !$#title Biosynthesis of rabbit haptoglobin: chemical evidence for a !1single chain precursor. !$#cross-references MUID:84005090; PMID:6413248 !$#accession A19376 !'##molecule_type protein !'##residues 1-33 ##label CH2 REFERENCE A90931 !$#authors Kurosky, A.; Kim, H.H.; Touchstone, B. !$#journal Comp. Biochem. Physiol. B (1976) 55:453-459 !$#title Comparative sequence analysis of the N-terminal region of !1rat, rabbit, and dog haptoglobin beta-chains. !$#cross-references MUID:77025019; PMID:975782 !$#accession A26503 !'##molecule_type protein !'##residues 34-73 ##label KUR COMMENT The mature haptoglobin molecule is a dimer of heterodimers, !1the two chains of which, alpha and beta, arise from the same !1precursor molecule. COMMENT Haptoglobin is a plasma glycoprotein; haptoglobin forms a !1complex with hemoglobin released from erythrocytes by !1hemolysis and delivers it to the liver for degradation. CLASSIFICATION #superfamily haptoglobin; complement factor H repeat !1homology; trypsin homology KEYWORDS acute phase; glycoprotein; hemoglobin binding; !1heterotetramer; iron transport; liver; plasma FEATURE !$1-18 #domain signal sequence #status experimental #label !8SIG\ !$19-33 #product haptoglobin alpha chain (fragment) #status !8experimental #label ACH\ !$34-73 #product haptoglobin beta chain (fragment) #status !8experimental #label BCH\ !$34-73 #domain trypsin homology (fragment) #label TRY SUMMARY #length 73 #checksum 5174 SEQUENCE /// ENTRY HPBO #type fragments TITLE haptoglobin precursor - bovine (fragments) ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 28-Feb-1992 #sequence_revision 31-May-1996 #text_change 31-Oct-1997 ACCESSIONS A40430; B40430 REFERENCE A40430 !$#authors Morimatsu, M.; Syuto, B.; Shimada, N.; Fujinaga, T.; !1Yamamoto, S.; Saito, M.; Naiki, M. !$#journal J. Biol. Chem. (1991) 266:11833-11837 !$#title Isolation and characterization of bovine haptoglobin from !1acute phase sera. !$#cross-references MUID:91268055; PMID:1904872 !$#accession A40430 !'##molecule_type protein !'##residues 1-25 ##label MOR !$#accession B40430 !'##molecule_type protein !'##residues 26-45 ##label MO2 COMMENT The mature haptoglobin molecule is a dimer of heterodimers, !1the two chains of which, alpha and beta, arise from the same !1precursor molecule. COMMENT Haptoglobin is a plasma glycoprotein; haptoglobin forms a !1complex with hemoglobin released from erythrocytes by !1hemolysis and delivers it to the liver for degradation. CLASSIFICATION #superfamily haptoglobin; complement factor H repeat !1homology; trypsin homology KEYWORDS acute phase; glycoprotein; hemoglobin binding; !1heterotetramer; iron transport; liver; plasma FEATURE !$1-25 #product haptoglobin alpha chain (fragment) #status !8experimental #label ALP\ !$26-45 #product haptoglobin beta chain (fragment) #status !8experimental #label BET SUMMARY #length 45 #checksum 8525 SEQUENCE /// ENTRY A56318 #type complete TITLE enteropeptidase (EC 3.4.21.9) precursor - human ALTERNATE_NAMES enterokinase ORGANISM #formal_name Homo sapiens #common_name man DATE 19-May-1995 #sequence_revision 09-Aug-1996 #text_change 18-Jun-1999 ACCESSIONS A56318; B43090 REFERENCE A56318 !$#authors Kitamoto, Y.; Veile, R.A.; Donis-Keller, H.; Sadler, J.E. !$#journal Biochemistry (1995) 34:4562-4568 !$#title cDNA sequence and chromosomal localization of human !1enterokinase, the proteolytic activator of trypsinogen. !$#cross-references MUID:95234679; PMID:7718557 !$#accession A56318 !'##molecule_type mRNA !'##residues 1-1019 ##label KIT !'##cross-references GB:U09860; NID:g746412; PIDN:AAC50138.1; !1PID:g746413 REFERENCE A43090 !$#authors Kitamoto, Y.; Yuan, X.; Wu, Q.; McCourt, D.W.; Sadler, J.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1994) 91:7588-7592 !$#title Enterokinase, the initiator of intestinal digestion, is a !1mosaic protease composed of a distinctive assortment of !1domains. !$#cross-references MUID:94329561; PMID:8052624 !$#accession B43090 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 749-1019 ##label KI2 !'##cross-references GB:U09860 COMMENT The mechanism of association with the membrane of the !1intestinal brush border is unknown. The sequence is !1compatible with type II membrane attachment using a !1signal-anchor sequence (as annotated below) or with !1amino-terminal myristoylation of the heavy chain. GENETICS !$#gene GDB:PRSS7 !'##cross-references GDB:384083; OMIM:226200 !$#map_position 21q21-21q21 COMPLEX Mature enteropeptidase is variously reported to contain two !1(heavy and light) or three (mini, heavy, and light) chains !1derived from a single precursor form; heavy and light chains !1are linked by a disulfide bond. Possibly, conversion from !1membrane-bound to soluble forms involves further processing. !1See the pig or bovine entries (PIR:A53663, PIR:A43090) for !1an alternative version of products. FUNCTION !$#description cleaves activation peptide from trypsinogen to produce !1active trypsin !$#pathway intestinal digestive hydrolase cascade CLASSIFICATION #superfamily enteropeptidase; C1r/C1s repeat homology; LDL !1receptor ligand-binding repeat homology; MAM homology; !1scavenger receptor cysteine-rich domain homology; trypsin !1homology KEYWORDS glycoprotein; hydrolase; serine proteinase; transmembrane !1protein; zymogen FEATURE !$1-784 #product enteropeptidase heavy chain #status !8predicted #label HCH\ !$22-38 #domain transmembrane #status predicted #label TMM\ !$184-221 #domain LDL receptor ligand-binding repeat homology !8#label LDL1\ !$342-504 #domain MAM homology #label MAM\ !$526-631 #domain C1r/C1s repeat homology #label C1R\ !$643-677 #domain LDL receptor ligand-binding repeat homology !8#label LDL2\ !$678-783 #domain scavenger receptor cysteine-rich domain !8homology #status atypical #label SRCR\ !$785-1019 #product enteropeptidase light chain #status !8predicted #label LCH\ !$785-1014 #domain trypsin homology #label TRY\ !$116,147,179,328, !$335,388,440,470, !$503,534,630,682, !$706,725,848,887, !$909,949 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$772-896,810-826, !$910-977,941-956, !$967-995 #disulfide_bonds #status predicted\ !$825,876,971 #active_site His, Asp, Ser #status predicted SUMMARY #length 1019 #molecular-weight 112923 #checksum 7518 SEQUENCE /// ENTRY A53663 #type complete TITLE enteropeptidase (EC 3.4.21.9) precursor - pig ALTERNATE_NAMES enterokinase ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 07-Oct-1994 #sequence_revision 09-Aug-1996 #text_change 18-Jun-1999 ACCESSIONS A53663 REFERENCE A53663 !$#authors Matsushima, M.; Ichinose, M.; Yahagi, N.; Kakei, N.; !1Tsukada, S.; Miki, K.; Kurokawa, K.; Tashiro, K.; Shiokawa, !1K.; Shinomiya, K.; Umeyama, H.; Inoue, H.; Takahashi, T.; !1Takahashi, K. !$#journal J. Biol. Chem. (1994) 269:19976-19982 !$#title Structural characterization of porcine enteropeptidase. !$#cross-references MUID:94327548; PMID:8051081 !$#accession A53663 !'##molecule_type mRNA !'##residues 1-1034 ##label MAT !'##cross-references GB:D30799; NID:g505122; PIDN:BAA06459.1; !1PID:g505123 !'##note parts of this sequence, including the amino ends of three !1chains isolated from the mature protein, were determined by !1protein sequencing COMMENT The mechanism of association with the membrane of the !1intestinal brush border is unknown. The sequence is !1compatible with type II membrane attachment using a !1signal-anchor sequence (as annotated below) or with !1amino-terminal myristoylation of the heavy chain. COMPLEX Mature enteropeptidase is variously reported to contain two !1(heavy and light) or three (mini, heavy, and light) chains !1derived from a single precursor form; heavy and light chains !1are linked by a disulfide bond. Possibly, conversion from !1membrane-bound to soluble forms involves further processing. !1See the human entry (PIR:A56318) for an alternative version !1of products. FUNCTION !$#description cleaves activation peptide from trypsinogen to produce !1active trypsin !$#pathway intestinal digestive hydrolase cascade CLASSIFICATION #superfamily enteropeptidase; C1r/C1s repeat homology; LDL !1receptor ligand-binding repeat homology; MAM homology; !1scavenger receptor cysteine-rich domain homology; trypsin !1homology KEYWORDS glycoprotein; hydrolase; serine proteinase; transmembrane !1protein; zymogen FEATURE !$22-38 #domain transmembrane #status predicted #label TMM\ !$52-117 #product enteropeptidase mini chain #status predicted !8#label MCH\ !$118-799 #product enteropeptidase heavy chain #status !8predicted #label HCH\ !$199-236 #domain LDL receptor ligand-binding repeat homology !8#label LDL1\ !$357-519 #domain MAM homology #label MAM\ !$541-646 #domain C1r/C1s repeat homology #label C1R\ !$658-692 #domain LDL receptor ligand-binding repeat homology !8#label LDL2\ !$693-798 #domain scavenger receptor cysteine-rich domain !8homology #status atypical #label SRCR\ !$800-1034 #product enteropeptidase light chain #status !8predicted #label LCH\ !$800-1029 #domain trypsin homology #label TRY\ !$116,147,170,194, !$283,343,350,403, !$455,485,518,549, !$645,697,701,721, !$740,761,804,863, !$902,964 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$787-911,825-841, !$925-992,956-971, !$982-1010 #disulfide_bonds #status predicted\ !$840,891,986 #active_site His, Asp, Ser #status predicted SUMMARY #length 1034 #molecular-weight 114793 #checksum 9505 SEQUENCE /// ENTRY A43090 #type complete TITLE enteropeptidase (EC 3.4.21.9) precursor - bovine ALTERNATE_NAMES enterokinase ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A43090; A48874; A61436 REFERENCE A43090 !$#authors Kitamoto, Y.; Yuan, X.; Wu, Q.; McCourt, D.W.; Sadler, J.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1994) 91:7588-7592 !$#title Enterokinase, the initiator of intestinal digestion, is a !1mosaic protease composed of a distinctive assortment of !1domains. !$#cross-references MUID:94329561; PMID:8052624 !$#accession A43090 !'##status nucleic acid sequence not shown; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-1035 ##label KIT !'##cross-references GB:U09859; NID:g746410; PIDN:AAB40026.1; !1PID:g746411 !'##experimental_source small intestine REFERENCE A48874 !$#authors LaVallie, E.R.; Rehemtulla, A.; Racie, L.A.; DiBlasio, E.A.; !1Ferenz, C.; Grant, K.L.; Light, A.; McCoy, J.M. !$#journal J. Biol. Chem. (1993) 268:23311-23317 !$#title Cloning and functional expression of a cDNA encoding the !1catalytic subunit of bovine enterokinase. !$#cross-references MUID:94043122; PMID:8226855 !$#accession A48874 !'##molecule_type mRNA !'##residues 801-1035 ##label LAV !'##cross-references GB:L19663; NID:g416131; PIDN:AAA16035.1; !1PID:g416132 !'##note parts of this sequence, including the amino end of the mature !1protein, were confirmed by protein sequencing REFERENCE A61436 !$#authors Light, A.; Janska, H. !$#journal J. Protein Chem. (1991) 10:475-480 !$#title The amino-terminal sequence of the catalytic subunit of !1bovine enterokinase. !$#cross-references MUID:92189715; PMID:1799406 !$#accession A61436 !'##molecule_type protein !'##residues 801-807,'Y',809-827 ##label LIG COMMENT The mechanism of association with the membrane of the !1intestinal brush border is unknown. The sequence is !1compatible with amino-terminal myristoylation of the heavy !1chain or with type II membrane attachment using a !1signal-anchor sequence. COMMENT Conversion from membrane-bound to soluble forms may involve !1further processing. See the human entry (PIR:A56318) for an !1alternative version of products. COMPLEX mature enteropeptidase is variously reported to contain two !1(heavy and light) or three (mini, heavy, and light) chains !1derived from a single precursor form; heavy and light chains !1are disulfide linked FUNCTION !$#description cleaves propeptide from trypsinogen to produce active !1trypsin !$#pathway intestinal digestive hydrolase cascade CLASSIFICATION #superfamily enteropeptidase; C1r/C1s repeat homology; LDL !1receptor ligand-binding repeat homology; MAM homology; !1scavenger receptor cysteine-rich domain homology; trypsin !1homology KEYWORDS glycoprotein; hydrolase; intestine; serine proteinase; !1transmembrane protein; zymogen FEATURE !$22-38 #domain transmembrane #status predicted #label TMM\ !$52-117 #product enteropeptidase mini chain #status predicted !8#label MCH\ !$118-800 #product enteropeptidase heavy chain #status !8predicted #label HCH\ !$199-236 #domain LDL receptor ligand-binding repeat homology !8#label LDL1\ !$358-520 #domain MAM homology #label MAM\ !$542-647 #domain C1r/C1s repeat homology #label C1R\ !$659-693 #domain LDL receptor ligand-binding repeat homology !8#label LDL2\ !$694-799 #domain scavenger receptor cysteine-rich domain !8homology #status atypical #label SRCR\ !$801-1035 #product enteropeptidase light chain #status !8predicted #label LCH\ !$801-1030 #domain trypsin homology #label TRY\ !$116,147,170,194, !$233,263,264,404, !$456,486,519,550, !$646,698,722,741, !$762,864,903,965 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$788-912,826-842, !$926-993,957-972, !$983-1011 #disulfide_bonds #status predicted\ !$841,892,987 #active_site His, Asp, Ser #status predicted SUMMARY #length 1035 #molecular-weight 114886 #checksum 4578 SEQUENCE /// ENTRY S00845 #type complete TITLE hepsin (EC 3.4.21.-) - human ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 18-Jun-1999 ACCESSIONS S00845 REFERENCE S00845 !$#authors Leytus, S.P.; Loeb, K.R.; Hagen, F.S.; Kurachi, K.; Davie, !1E.W. !$#journal Biochemistry (1988) 27:1067-1074 !$#title A novel trypsin-like serine protease (hepsin) with a !1putative transmembrane domain expressed by human liver and !1hepatoma cells. !$#cross-references MUID:88209431; PMID:2835076 !$#accession S00845 !'##molecule_type mRNA !'##residues 1-417 ##label LEY !'##cross-references EMBL:X07732; NID:g32063; PIDN:CAA30558.1; !1PID:g32064 GENETICS !$#gene GDB:HPN; TMPRSS1; hepsin !'##cross-references GDB:135685; OMIM:142440 !$#map_position 19q11-19q13.2 CLASSIFICATION #superfamily hepsin; trypsin homology KEYWORDS hydrolase; liver; serine proteinase; transmembrane protein FEATURE !$23-45 #domain transmembrane #status predicted #label TMN\ !$163-400 #domain trypsin homology #label TRY\ !$188-204,291-359, !$322-338,349-381 #disulfide_bonds #status predicted\ !$203,257,353 #active_site His, Asp, Ser #status predicted SUMMARY #length 417 #molecular-weight 45011 #checksum 5762 SEQUENCE /// ENTRY S33777 #type complete TITLE hepsin (EC 3.4.21.-) - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 06-Jan-1995 #sequence_revision 06-Jan-1995 #text_change 18-Jun-1999 ACCESSIONS S33777; S32013 REFERENCE S33777 !$#authors Farley, D.; Reymond, F.; Nick, H. !$#journal Biochim. Biophys. Acta (1993) 1173:350-352 !$#title Cloning and sequence analysis of rat hepsin, a cell surface !1serine proteinase. !$#cross-references MUID:93305733; PMID:8318546 !$#accession S33777 !'##status preliminary !'##molecule_type mRNA !'##residues 1-416 ##label FAR !'##cross-references EMBL:X70900; NID:g57928; PIDN:CAA50256.1; !1PID:g57929 CLASSIFICATION #superfamily hepsin; trypsin homology KEYWORDS hydrolase; liver; serine proteinase; transmembrane protein FEATURE !$22-44 #domain transmembrane #status predicted #label TMN\ !$162-399 #domain trypsin homology #label TRY\ !$187-203,290-358, !$321-337,348-380 #disulfide_bonds #status predicted\ !$202,256,352 #active_site His, Asp, Ser #status predicted SUMMARY #length 416 #molecular-weight 44926 #checksum 5191 SEQUENCE /// ENTRY A47547 #type complete TITLE serine proteinease stubble-stubbloid (EC 3.4.21.-) - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A47547 REFERENCE A47547 !$#authors Appel, L.F.; Prout, M.; Abu-Shumays, R.; Hammonds, A.; !1Garbe, J.C.; Fristrom, D.; Fristrom, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:4937-4941 !$#title The Drosophila Stubble-stubbloid gene encodes an apparent !1transmembrane serine protease required for epithelial !1morphogenesis. !$#cross-references MUID:93281671; PMID:7685111 !$#accession A47547 !'##status preliminary !'##molecule_type mRNA !'##residues 1-786 ##label APP !'##cross-references GB:L11451; NID:g158511; PIDN:AAA28918.1; !1PID:g158512 GENETICS !$#gene Sb-sbd !'##cross-references FlyBase:FBgn0003319 CLASSIFICATION #superfamily serine proteinease stubble-stubbloid; trypsin !1homology KEYWORDS hydrolase; serine proteinase; transmembrane protein FEATURE !$61-77 #domain transmembrane #status predicted #label TMN\ !$543-781 #domain trypsin homology #label TRY SUMMARY #length 786 #molecular-weight 85010 #checksum 7042 SEQUENCE /// ENTRY S11674 #type complete TITLE acrosin (EC 3.4.21.10) precursor - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S11674; S23499; S12063; A61022; S03330 REFERENCE S11674 !$#authors Keime, S.; Adham, I.M.; Engel, W. !$#journal Eur. J. Biochem. (1990) 190:195-200 !$#title Nucleotide sequence and exon-intron organization of the !1human proacrosin gene. !$#cross-references MUID:90306003; PMID:2114285 !$#accession S11674 !'##molecule_type DNA !'##residues 1-421 ##label KEI !'##cross-references EMBL:X54017; NID:g35582; PIDN:CAA37964.1; !1PID:g1216165 !'##note the authors translated the codon AGG for residue 64 as Thr and !1CTG for residue 268 as Arg REFERENCE S23499 !$#authors Vazquez-Levin, M.H.; Reventos, J.; Gordon, J.W. !$#journal Eur. J. Biochem. (1992) 207:23-26 !$#title Molecular cloning, sequencing and restriction mapping of the !1genomic sequence encoding human proacrosin. !$#cross-references MUID:92331659; PMID:1628652 !$#accession S23499 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-421 ##label VAZ !'##cross-references EMBL:M77378 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1992 REFERENCE S12063 !$#authors Keime, S. !$#submission submitted to the EMBL Data Library, December 1989 !$#accession S12063 !'##molecule_type DNA !'##residues 1-225,'R',227-421 ##label KEI2 !'##cross-references EMBL:X54017 REFERENCE A61022 !$#authors Adham, I.M.; Klemm, U.; Maier, W.M.; Engel, W. !$#journal Hum. Genet. (1990) 84:125-128 !$#title Molecular cloning of human preproacrosin cDNA. !$#cross-references MUID:90128988; PMID:2298447 !$#accession A61022 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-63,'T',65-225,'V',227-267,'R',269-421 ##label ADH REFERENCE S03330 !$#authors Baba, T.; Watanabe, K.; Kashiwabara, S.I.; Arai, Y. !$#journal FEBS Lett. (1989) 244:296-300 !$#title Primary structure of human proacrosin deduced from its cDNA !1sequence. !$#cross-references MUID:89153568; PMID:2493394 !$#accession S03330 !'##molecule_type mRNA !'##residues 1-63,'T',65-119,'V',121-165,'L',167-267,'R',269-344,'R', !1346-421 ##label BAB !'##cross-references EMBL:Y00970; NID:g28325; PIDN:CAA68784.1; !1PID:g28326 GENETICS !$#gene GDB:ACR !'##cross-references GDB:119645; OMIM:102480 !$#map_position 22q13-22qter !$#introns 26/2; 94/2; 189/2; 237/3 CLASSIFICATION #superfamily acrosin; trypsin homology KEYWORDS glycoprotein; hydrolase; serine proteinase; sperm FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-421 #product acrosin #status predicted #label MAT\ !$20-42 #product acrosin light chain #status predicted #label !8LCH\ !$43-421 #product acrosin heavy chain #status predicted #label !8HCH\ !$43-285 #domain trypsin homology #label TRY\ !$302-379 #region proline-rich\ !$22,210 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$25-154 #disulfide_bonds #status predicted\ !$29-162 #disulfide_bonds #status predicted\ !$73-89 #disulfide_bonds #status predicted\ !$88,142,240 #active_site His, Asp, Ser #status predicted\ !$177-246 #disulfide_bonds #status predicted\ !$209-225 #disulfide_bonds #status predicted\ !$236-266 #disulfide_bonds #status predicted SUMMARY #length 421 #molecular-weight 45799 #checksum 9188 SEQUENCE /// ENTRY A34170 #type complete TITLE acrosin (EC 3.4.21.10) precursor - pig ALTERNATE_NAMES 53K fucose-binding protein ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A34170; S08994; S02428; S04940; S16657; S02780; S10695; !1S12968 REFERENCE A34170 !$#authors Baba, T.; Kashiwabara, S.; Watanabe, K.; Itoh, H.; !1Michikawa, Y.; Kimura, K.; Takada, M.; Fukamizu, A.; Arai, !1Y. !$#journal J. Biol. Chem. (1989) 264:11920-11927 !$#title Activation and maturation mechanisms of boar acrosin zymogen !1based on the deduced primary structure. !$#cross-references MUID:89308595; PMID:2745422 !$#accession A34170 !'##status preliminary !'##molecule_type mRNA !'##residues 1-415 ##label BAB !'##cross-references GB:J04950; NID:g164702; PIDN:AAA31131.1; !1PID:g164703 REFERENCE S08994 !$#authors Cechova, D.; Toepfer-Petersen, E.; Zucker, A.; Jonakova, V. !$#journal Biol. Chem. Hoppe-Seyler (1990) 371:317-323 !$#title Is sperminogen a modified proacrosin? Isolation, !1purification, and partial characterization of !1low-molecular-mass boar proacrosin. !$#cross-references MUID:90253655; PMID:2111146 !$#accession S08994 !'##molecule_type protein !'##residues 'X',18,'X',20-25,'X',27-32,'X',34-38,'X',40-50 ##label CEC REFERENCE S02428 !$#authors Toepfer-Petersen, E.; Henschen, A. !$#journal FEBS Lett. (1987) 226:38-42 !$#title Acrosin shows zona and fucose binding, novel properties for !1a serine proteinase. !$#cross-references MUID:88083633; PMID:3480243 !$#accession S02428 !'##molecule_type protein !'##residues 17-32;40-55 ##label TOE REFERENCE S04940 !$#authors Adham, I.M.; Klemm, U.; Maier, W.M.; Hoyer-Fender, S.; !1Tsaousidou, S.; Engel, W. !$#journal Eur. J. Biochem. (1989) 182:563-568 !$#title Molecular cloning of preproacrosin and analysis of its !1expression pattern in spermatogenesis. !$#cross-references MUID:89325301; PMID:2502391 !$#accession S04940 !'##molecule_type mRNA !'##residues 1-7,9-210,'Q',212-216,'VT',219-346,'A',348-388,390-393, !1'GN',396,'LVE',399-409,'RRTARLLI' ##label ADH !'##cross-references EMBL:X14844 !'##note the authors translated the codon CCT for residue 240 as Ala, !1GCC for residue 264 as Gly, and ACC for residue 298 as Ser REFERENCE S16657 !$#authors Adham, I.M. !$#submission submitted to the EMBL Data Library, March 1989 !$#accession S16657 !'##molecule_type mRNA !'##residues 1-7,9-210,'Q',212-216,'VT',219-346,'A',348-388,390-398, !1'KELL' ##label AD2 !'##cross-references EMBL:X14844; NID:g1867; PIDN:CAA32948.1; PID:g1868 !'##note the difference at the carboxyl end is due to a frameshift error REFERENCE S02780 !$#authors Baba, T.; Michikawa, Y.; Kawakura, K.; Arai, Y. !$#journal FEBS Lett. (1989) 244:132-136 !$#title Activation of boar proacrosin is effected by processing at !1both N- and C-terminal portions of the zymogen molecule. !$#cross-references MUID:89171246; PMID:2494060 !$#accession S02780 !'##molecule_type protein !'##residues 17-69 ##label BA2 REFERENCE S10695 !$#authors Toepfer-Petersen, E.; Steinberger, M.; von Eschenbach, C.E.; !1Zucker, A. !$#journal FEBS Lett. (1990) 265:51-54 !$#title Zona pellucida-binding of boar sperm acrosin is associated !1with the N-terminal peptide of the acrosin B-chain (heavy !1chain). !$#cross-references MUID:90306316; PMID:2365054 !$#accession S10695 !'##molecule_type protein !'##residues 40-62 ##label TO2 REFERENCE S12968 !$#authors Toepfer-Petersen, E.; Calvete, J.; Schaefer, W.; Henschen, !1A. !$#journal FEBS Lett. (1990) 275:139-142 !$#title Complete localization of the disulfide bridges and !1glycosylation sites in boar sperm acrosin. !$#cross-references MUID:91085546; PMID:2261983 !$#accession S12968 !'##molecule_type protein !'##residues !117-29;34-66;68-91;94-121;123-166;171-184;190-207;209-216; !1219-228;231-245;248-381;383-415 ##label TO3 CLASSIFICATION #superfamily acrosin; trypsin homology KEYWORDS glycoprotein; hydrolase; serine proteinase; sperm FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-415 #product acrosin #status experimental #label MAT\ !$17-39 #product acrosin light (A) chain #status experimental !8#label LCH\ !$40-415 #product acrosin heavy (B) chain #status experimental !8#label HCH\ !$40-283 #domain trypsin homology #label TRY\ !$300-374 #region proline-rich\ !$19,208 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$22-152,26-160, !$71-87,175-244, !$207-223,234-264 #disulfide_bonds #status experimental\ !$86,140,238 #active_site His, Asp, Ser #status predicted SUMMARY #length 415 #molecular-weight 45387 #checksum 6203 SEQUENCE /// ENTRY KFHU1 #type complete TITLE coagulation factor XIa (EC 3.4.21.27) precursor [validated] - human ALTERNATE_NAMES antihemophilic factor C; plasma thromboplastin antecedent ORGANISM #formal_name Homo sapiens #common_name man DATE 13-Aug-1986 #sequence_revision 26-May-1994 #text_change 08-Dec-2000 ACCESSIONS A27431; A00920; A37940 REFERENCE A27431 !$#authors Asakai, R.; Davie, E.W.; Chung, D.W. !$#journal Biochemistry (1987) 26:7221-7228 !$#title Organization of the gene for human factor XI. !$#cross-references MUID:88107663; PMID:2827746 !$#accession A27431 !'##molecule_type DNA !'##residues 1-625 ##label ASA !'##cross-references GB:M18295 !'##note the sequence shown follows the authors' translation REFERENCE A00920 !$#authors Fujikawa, K.; Chung, D.W.; Hendrickson, L.E.; Davie, E.W. !$#journal Biochemistry (1986) 25:2417-2424 !$#title Amino acid sequence of human factor XI, a blood coagulation !1factor with four tandem repeats that are highly homologous !1with plasma prekallikrein. !$#cross-references MUID:86243360; PMID:3636155 !$#accession A00920 !'##molecule_type mRNA !'##residues 1-625 ##label FUJ !'##cross-references GB:M13142; NID:g182832; PIDN:AAA52487.1; !1PID:g182833 REFERENCE A37940 !$#authors McMullen, B.A.; Fujikawa, K.; Davie, E.W. !$#journal Biochemistry (1991) 30:2056-2060 !$#title Location of the disulfide bonds in human coagulation factor !1XI: the presence of tandem apple domains. !$#cross-references MUID:91152017; PMID:1998667 !$#accession A37940 !'##molecule_type protein !'##residues 28-33;35-49,'X',51-55,'X',57-63;70-75,'X',77-79;107-109, !1'X',111-112;132-139;'X',141-154;163-164,'X',166-168;192,'X', !1194;198-199,'X';223-228;229,'X',231-235,'X',237-248;253-254, !1'X',256-258;280-282,'X',284;285-297;313-316,'X', !1318-319;320-326;'X',328-330;'X',347-349;373,'X',375;377-379, !1'X',381-383;414-415,'X',417-431,'X',433-437;486-499,'X', !1501-507;535-548;559,'X',561-564 ##label MCM COMMENT The proenzyme consists of two identical chains linked by one !1or more disulfide bonds. It is activated by factor XIIa (or !1XII), which cleaves each chain into a light chain, which !1contains the active site, and a heavy chain, which !1associates with high molecular weight (HMW) kininogen. GENETICS !$#gene GDB:F11 !'##cross-references GDB:119891; OMIM:264900 !$#map_position 4q35-4q35 !$#introns 19/1; 73/2; 109/1; 162/2; 199/1; 252/2; 289/1; 343/2; 379/1; !1435/2; 494/1; 526/1; 572/3 FUNCTION !$#description catalyzes the proteolytic activation of coagulation factor !1IX !$#pathway blood coagulation intrinsic pathway CLASSIFICATION #superfamily coagulation factor XI; trypsin homology KEYWORDS blood coagulation; duplication; glycoprotein; hemophilia C; !1homodimer; hydrolase; plasma; serine proteinase FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-387 #product coagulation factor XIa heavy chain #status !8experimental #label HCH\ !$19-108 #domain apple repeat #label AP1\ !$109-198 #domain apple repeat #label AP2\ !$199-288 #domain apple repeat #label AP3\ !$290-379 #domain apple repeat #label AP4\ !$388-625 #product coagulation factor XIa light chain #status !8experimental #label LCH\ !$388-618 #domain trypsin homology #label TRY\ !$20-103,514-581, !$571-599 #disulfide_bonds #status predicted\ !$29 #disulfide_bonds interchain #status experimental\ !$46-76,50-56, !$110-193,136-165, !$140-146,200-283, !$226-255,230-236, !$291-374,317-346, !$321-327,380-500, !$416-432,545-560 #disulfide_bonds #status experimental\ !$90,126,353,450 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$339 #disulfide_bonds interchain #status predicted\ !$387-388 #cleavage_site Arg-Ile (coagulation factor XIIa) !8#status experimental\ !$431,480,575 #active_site His, Asp, Ser #status predicted\ !$491 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 625 #molecular-weight 70109 #checksum 9314 SEQUENCE /// ENTRY KQHUP #type complete TITLE plasma kallikrein (EC 3.4.21.34) precursor - human ALTERNATE_NAMES kininogenin; plasma prekallikrein ORGANISM #formal_name Homo sapiens #common_name man DATE 13-Aug-1986 #sequence_revision 13-Aug-1986 #text_change 18-Jun-1999 ACCESSIONS A00921; A37939 REFERENCE A00921 !$#authors Chung, D.W.; Fujikawa, K.; McMullen, B.A.; Davie, E.W. !$#journal Biochemistry (1986) 25:2410-2417 !$#title Human plasma prekallikrein, a zymogen to a serine protease !1that contains four tandem repeats. !$#cross-references MUID:86243359; PMID:3521732 !$#accession A00921 !'##molecule_type mRNA !'##residues 1-638 ##label CHU !'##cross-references GB:M13143; NID:g190262; PIDN:AAA60153.1; !1PID:g190263 REFERENCE A37939 !$#authors McMullen, B.A.; Fujikawa, K.; Davie, E.W. !$#journal Biochemistry (1991) 30:2050-2056 !$#title Location of the disulfide bonds in human plasma !1prekallikrein: the presence of four novel apple domains in !1the amino-terminal portion of the molecule. !$#cross-references MUID:91152016; PMID:1998666 !$#accession A37939 !'##molecule_type protein !'##residues 20-27;40-46,'X',48,'H';50,'X',52-70,'H';75-76,'X', !178-80;103-113;131-140;141-143;'S',144-146;147-159;187-193, !1'X',195-198;199-200,'X',202,'H';219-228;229-230,'X', !1232-248;254-255,'X',257-259;260-283,'X',285;287-291,'X', !1293-295;314-317,'X',319-320;321-324;'X',329-333;334-339,'X', !1341-346,'X',348-350;351,'XNT',355;380-382,'X', !1384-386;417-418,'X',420-434,'X',436-446;489-502,'X', !1504-506;510-525;538-551;562,'X',564-567;573,'X', !1575-576;578-583,'X',585;592-604 ##label MCM COMMENT This protein, synthesized in the liver, circulates as a !1noncovalent complex with high molecular weight (HMW) !1kininogen. COMMENT The zymogen is activated by factor XIIa, which cleaves the !1molecule into a light chain, which contains the active site, !1and a heavy chain, which associates with HMW kininogen. !1These chains are linked by one or more disulfide bonds. COMMENT The enzyme cleaves Lys-Arg and Arg-Ser bonds. It activates, !1in a reciprocal reaction, factor XII after its binding to a !1negatively charged surface. It also releases bradykinin from !1HMW kininogen and may also play a role in the !1renin-angiotensin system by converting prorenin into renin. GENETICS !$#gene GDB:KLK3 !'##cross-references GDB:127575; OMIM:229000 !$#map_position 4q35-4q35 CLASSIFICATION #superfamily coagulation factor XI; trypsin homology KEYWORDS blood coagulation; duplication; fibrinolysis; glycoprotein; !1hydrolase; inflammation; liver; plasma; serine proteinase FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-638 #product plasma kallikrein #status predicted #label !8MAT\ !$20-390 #domain plasma kallikrein heavy chain #status !8predicted #label HCH\ !$20-109 #domain apple repeat #label AP1\ !$110-199 #domain apple repeat #label AP2\ !$200-289 #domain apple repeat #label AP3\ !$291-380 #domain apple repeat #label AP4\ !$391-638 #domain plasma kallikrein light chain #status !8predicted #label LCH\ !$391-621 #domain trypsin homology #label TRY\ !$21-104,47-77,51-57, !$111-194,137-166, !$141-147,201-284, !$227-256,231-237, !$292-375,322-328, !$383-503,419-435, !$517-584,548-563, !$574-602 #disulfide_bonds #status experimental\ !$127,308,396,453,494 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$318-347,340-345 #disulfide_bonds #status predicted\ !$390-391 #cleavage_site Arg-Ile (coagulation factor XIIa) !8#status predicted\ !$434,483,578 #active_site His, Asp, Ser #status predicted SUMMARY #length 638 #molecular-weight 71369 #checksum 585 SEQUENCE /// ENTRY KQRTPL #type complete TITLE plasma kallikrein (EC 3.4.21.34) precursor - rat ALTERNATE_NAMES Fletcher factor; kininogenin; serum kallikrein ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS A39180; A33320; S06851; I53041; S06852 REFERENCE A39180 !$#authors Beaubien, G.; Rosinski-Chupin, I.; Mattei, M.G.; Mbikay, M.; !1Chretien, M.; Seidah, N.G. !$#journal Biochemistry (1991) 30:1628-1635 !$#title Gene structure and chromosomal localization of plasma !1kallikrein. !$#cross-references MUID:91129236; PMID:1993180 !$#accession A39180 !'##molecule_type DNA !'##residues 1-638 ##label BEA !'##cross-references GB:J05315 !'##note the authors translated the codon GAG for residue 81 as Gln REFERENCE A33320 !$#authors Seidah, N.G.; Ladenheim, R.; Mbikay, M.; Hamelin, J.; !1Lutfalla, G.; Rougeon, F.; Lazure, C.; Chretien, M. !$#journal DNA (1989) 8:563-574 !$#title The cDNA structure of rat plasma kallikrein. !$#cross-references MUID:90091743; PMID:2598771 !$#accession A33320 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-638 ##label SEI !'##cross-references GB:M30282; NID:g205010; PIDN:AAA41463.1; !1PID:g205011 !'##note part of this sequence, including the amino ends of both the !1heavy and light chains, was confirmed by protein sequencing REFERENCE S06851 !$#authors Paquin, J.; Benjannet, S.; Sawyer, N.; Lazure, C.; Chretien, !1M.; Seidah, N.G. !$#journal Biochim. Biophys. Acta (1989) 999:103-110 !$#title Rat plasma kallikrein: purification, NH(2)-terminal !1sequencing and development of a specific radioimmunoassay. !$#cross-references MUID:90089457; PMID:2597701 !$#accession S06851 !'##molecule_type protein !'##residues 20-45;391-413 ##label PAQ REFERENCE I53041 !$#authors Seidah, N.G.; Ladenheim, R.; Mbikay, M.; Hamelin, J.; !1Lutfalla, G.; Rougeon, R.; Lazure, C.; Chretien, M. !$#journal DNA Cell Biol. (1989) 8:563-574 !$#title The cDNA structure of rat plasma kallikrein. !$#accession I53041 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-638 ##label RES !'##cross-references GB:M58590; NID:g206721; PIDN:AAA42069.1; !1PID:g206722 COMMENT This protein, synthesized in the liver, circulates as a !1noncovalent complex with high molecular weight (HMW) !1kininogen. COMMENT The zymogen is activated by factor XIIa, which cleaves the !1molecule into a light chain, which contains the active site, !1and a heavy chain, which associates with HMW kininogen. !1These chains are linked by one or more disulfide bonds. GENETICS !$#gene PK CLASSIFICATION #superfamily coagulation factor XI; trypsin homology KEYWORDS blood coagulation; duplication; fibrinolysis; glycoprotein; !1hydrolase; inflammation; liver; plasma; serine proteinase; !1zymogen FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-390 #product plasma kallikrein heavy chain #status !8experimental #label MAT1\ !$20-109 #domain apple repeat #label AP1\ !$110-199 #domain apple repeat #label AP2\ !$200-289 #domain apple repeat #label AP3\ !$291-380 #domain apple repeat #label AP4\ !$391-638 #product plasma kallikrein light chain #status !8experimental #label MAT2\ !$391-621 #domain trypsin homology #label TRY\ !$21-104,47-77,51-57, !$111-194,137-166, !$141-147,201-284, !$227-256,231-237, !$292-375,318-347, !$322-328,340-345, !$383-503,419-435, !$517-584,548-563, !$574-602 #disulfide_bonds #status predicted\ !$127,215,308,453, !$459,494 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$396 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$434,483,578 #active_site His, Asp, Ser #status predicted SUMMARY #length 638 #molecular-weight 71273 #checksum 227 SEQUENCE /// ENTRY KQMSPL #type complete TITLE plasma kallikrein (EC 3.4.21.34) precursor - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS A36557 REFERENCE A36557 !$#authors Seidah, N.G.; Sawyer, N.; Hamelin, J.; Mion, P.; Beaubien, !1G.; Brachpapa, L.; Rochemont, J.; Mbikay, M.; Chretien, M. !$#journal DNA Cell Biol. (1990) 9:737-748 !$#title Mouse plasma kallikrein: cDNA structure, enzyme !1characterization, and comparison of protein and mRNA levels !1among species. !$#cross-references MUID:91090844; PMID:2264928 !$#accession A36557 !'##molecule_type mRNA !'##residues 1-638 ##label SEI !'##cross-references GB:M58588; NID:g200358; PIDN:AAA63393.1; !1PID:g200359 !'##note part of this sequence, including the amino ends of both the !1heavy and light chains, was confirmed by protein sequencing COMMENT This protein, synthesized in the liver, circulates as a !1noncovalent complex with high molecular weight (HMW) !1kininogen. COMMENT The zymogen is activated by factor XIIa, which cleaves the !1molecule into a light chain, which contains the active site, !1and a heavy chain, which associates with HMW kininogen. !1These chains are linked by one or more disulfide bonds. CLASSIFICATION #superfamily coagulation factor XI; trypsin homology KEYWORDS blood coagulation; duplication; fibrinolysis; glycoprotein; !1hydrolase; inflammation; liver; plasma; serine proteinase; !1zymogen FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-390 #product plasma kallikrein heavy chain #status !8experimental #label HCH\ !$20-109 #domain apple repeat #label AP1\ !$110-199 #domain apple repeat #label AP2\ !$200-289 #domain apple repeat #label AP3\ !$291-380 #domain apple repeat #label AP4\ !$391-638 #product plasma kallikrein light chain #status !8experimental #label LCH\ !$391-621 #domain trypsin homology #label TRY\ !$21-104,47-77,51-57, !$111-194,137-166, !$141-147,201-284, !$227-256,231-237, !$292-375,318-347, !$322-328,340-345, !$383-503,419-435, !$517-584,548-563, !$574-602 #disulfide_bonds #status predicted\ !$127,215,308,396,494 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$434,483,578 #active_site His, Asp, Ser #status predicted SUMMARY #length 638 #molecular-weight 71368 #checksum 3126 SEQUENCE /// ENTRY EXHU #type complete TITLE coagulation factor Xa (EC 3.4.21.6) precursor [validated] - human ALTERNATE_NAMES Stuart factor ORGANISM #formal_name Homo sapiens #common_name man DATE 15-Nov-1984 #sequence_revision 02-May-1994 #text_change 08-Dec-2000 ACCESSIONS A24478; JQ0917; A42485; A25853; A22208; A21284; A20362; !1S39415; I54051; A00924 REFERENCE A24478 !$#authors Leytus, S.P.; Foster, D.C.; Kurachi, K.; Davie, E.W. !$#journal Biochemistry (1986) 25:5098-5102 !$#title Gene for human Factor X: a blood coagulation factor whose !1gene organization is essentially identical with that of !1Factor IX and protein C. !$#cross-references MUID:87026600; PMID:3768336 !$#accession A24478 !'##molecule_type DNA !'##residues 1-488 ##label LEY !'##cross-references GB:L29433; GB:M14327; NID:g459809; PIDN:AAA52764.1; !1PID:g182831 REFERENCE JQ0917 !$#authors Messier, T.L.; Pittman, D.D.; Long, G.L.; Kaufman, R.J.; !1Church, W.R. !$#journal Gene (1991) 99:291-294 !$#title Cloning and expression in COS-1 cells of a full-length cDNA !1encoding human coagulation factor X. !$#cross-references MUID:91216473; PMID:1902434 !$#accession JQ0917 !'##molecule_type mRNA !'##residues 1-488 ##label MES !'##cross-references GB:M57285; NID:g182389; PIDN:AAA52421.1; !1PID:g182390 REFERENCE A42485 !$#authors Miao, C.H.; Leytus, S.P.; Chung, D.W.; Davie, E.W. !$#journal J. Biol. Chem. (1992) 267:7395-7401 !$#title Liver-specific expression of the gene coding for human !1factor X, a blood coagulation factor. !$#cross-references MUID:92218390; PMID:1313796 !$#accession A42485 !'##molecule_type DNA !'##residues 1-15 ##label MIA !'##experimental_source liver !'##note sequence extracted from NCBI backbone (NCBIN:93780, !1NCBIP:93787) REFERENCE A25853 !$#authors Kaul, R.K.; Hildebrand, B.; Roberts, S.; Jagadeeswaran, P. !$#journal Gene (1986) 41:311-314 !$#title Isolation and characterization of human blood-coagulation !1factor X cDNA. !$#cross-references MUID:86221713; PMID:3011603 !$#accession A25853 !'##molecule_type mRNA !'##residues 19-284,'E',289-488 ##label KAU !'##cross-references GB:M22613; NID:g180335; PIDN:AAA51984.1; !1PID:g180336 REFERENCE A22208 !$#authors Fung, M.R.; Hay, C.W.; MacGillivray, R.T.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:3591-3595 !$#title Characterization of an almost full-length cDNA coding for !1human blood coagulation factor X. !$#cross-references MUID:85216545; PMID:2582420 !$#accession A22208 !'##molecule_type mRNA !'##residues 13-441,'S',443-488 ##label FUN !'##cross-references GB:K03194; NID:g182840; PIDN:AAA52490.1; !1PID:g182841 REFERENCE A21284 !$#authors Leytus, S.P.; Chung, D.W.; Kisiel, W.; Kurachi, K.; Davie, !1E.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:3699-3702 !$#title Characterization of a cDNA coding for human factor X. !$#cross-references MUID:84222026; PMID:6587384 !$#accession A21284 !'##molecule_type mRNA !'##residues 13-284,'E',289-488 ##label LE2 !'##cross-references GB:K01886 REFERENCE A20362 !$#authors McMullen, B.A.; Fujikawa, K.; Kisiel, W.; Sasagawa, T.; !1Howald, W.N.; Kwa, E.Y.; Weinstein, B. !$#journal Biochemistry (1983) 22:2875-2884 !$#title Complete amino acid sequence of the light chain of human !1blood coagulation factor X: evidence for identification of !1residue 63 as beta-hydroxyaspartic acid. !$#cross-references MUID:83257207; PMID:6871167 !$#accession A20362 !'##molecule_type protein !'##residues 41-179 ##label MCM REFERENCE S39414 !$#authors Inoue, K.; Morita, T. !$#journal Eur. J. Biochem. (1993) 218:153-163 !$#title Identification of O-linked oligosaccharide chains in the !1activation peptides of blood coagulation factor X. The role !1of the carbohydrate moieties in the activation of factor X. !$#cross-references MUID:94062825; PMID:8243461 !$#accession S39415 !'##molecule_type protein !'##residues 183-234 ##label INO !'##note glycosylation sites !'##note identification and characterization of beta-hydroxyaspartic !1acid REFERENCE I54051 !$#authors Jagadeeswaran, P.; Reddy, S.V.; Rao, K.J.; Hamsabhushanam, !1K.; Lyman, G. !$#journal Gene (1989) 84:517-519 !$#title Cloning and characterization of the 5' end (exon 1) of the !1gene encoding human factor X. !$#cross-references MUID:90128299; PMID:2612918 !$#accession I54051 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-23 ##label RES !'##cross-references GB:M33297; NID:g183860; PIDN:AAA52636.1; !1PID:g553330 REFERENCE A49458 !$#authors Padmanabhan, K.; Padmanabhan, K.P.; Tulinsky, A.; Park, !1C.H.; Bode, W.; Huber, R.; Blankenship, D.T.; Cardin, A.D.; !1Kisiel, W. !$#journal J. Mol. Biol. (1993) 232:947-966 !$#title Structure of human des(1-45) factor Xa at 2.2 angstroms !1resolution. !$#cross-references MUID:93360277; PMID:8355279 !$#contents annotation; X-ray crystallography, 2.2 angstroms COMMENT The two chains held together by one disulfide bond are !1formed from a single-chain precursor by excision of residues !1180-182. COMMENT The activation peptide is cleaved by factor IXa (in the !1intrinsic pathway) or by factor VIIa (in the extrinsic !1pathway). GENETICS !$#gene GDB:F10 !'##cross-references GDB:119890; OMIM:227600 !$#map_position 13q34-13q34 !$#introns 24/1; 77/3; 86/1; 124/1; 150/3; 249/3; 289/1 !$#note deficiency of this factor causes Stuart disease FUNCTION !$#description catalyzes the proteolytic activation of prothrombin to !1thrombin in the presence of calcium, phospholipid, and !1factor Va !$#pathway blood coagulation CLASSIFICATION #superfamily coagulation factor X; EGF homology; Gla domain !1homology; trypsin homology KEYWORDS beta-hydroxyaspartic acid; blood coagulation; calcium !1binding; carboxyglutamic acid; glycoprotein; hydrolase; !1plasma; serine proteinase; vitamin K FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-40 #domain propeptide #status predicted #label PRO\ !$25-84 #domain Gla domain homology #label GLA\ !$41-179 #product coagulation factor X light chain #status !8experimental #label LCH\ !$90-121 #domain EGF homology #label EG1\ !$129-164 #domain EGF homology #label EG2\ !$183-488 #product coagulation factor X heavy chain #status !8experimental #label HCH\ !$183-234 #domain activation peptide #status experimental !8#label APT\ !$235-488 #product coagulation factor Xa heavy chain #status !8experimental #label ACT\ !$235-462 #domain trypsin homology #label TRY\ !$46,47,54,56,59,60, !$65,66,69,72,79 #modified_site gamma-carboxyglutamic acid (Glu) !8#status experimental\ !$57-62 #disulfide_bonds #status predicted\ !$90-101,95-110, !$112-121,129-140, !$136-149,151-164, !$172-342,241-246, !$261-277,390-404, !$415-443 #disulfide_bonds #status experimental\ !$103 #modified_site erythro-beta-hydroxyaspartic acid !8(Asp) #status experimental\ !$199,211 #binding_site carbohydrate (Thr) (covalent) #status !8experimental\ !$221,231 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$234-235 #cleavage_site Arg-Ile (coagulation factor IXa, !8coagulation factor VIIa) #status experimental\ !$276,322,419 #active_site His, Asp, Ser #status experimental SUMMARY #length 488 #molecular-weight 54731 #checksum 2459 SEQUENCE /// ENTRY EXBO #type complete TITLE coagulation factor Xa (EC 3.4.21.6) precursor - bovine ALTERNATE_NAMES Stuart factor ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 24-Apr-1984 #sequence_revision 17-Mar-1987 #text_change 16-Jul-1999 ACCESSIONS A22867; A14997; A12030; A34412; S39414; A00925 REFERENCE A22867 !$#authors Fung, M.R.; Campbell, R.M.; MacGillivray, T.A. !$#journal Nucleic Acids Res. (1984) 12:4481-4492 !$#title Blood coagulation factor X mRNA encodes a single polypeptide !1chain containing a prepro leader sequence. !$#cross-references MUID:84247315; PMID:6330671 !$#accession A22867 !'##molecule_type mRNA !'##residues 1-487 ##label FUN !'##cross-references GB:X00673; NID:g192; PIDN:CAA25286.1; PID:g193 REFERENCE A14997 !$#authors Enfield, D.L.; Ericsson, L.H.; Fujikawa, K.; Walsh, K.A.; !1Neurath, H.; Titani, K. !$#journal Biochemistry (1980) 19:659-667 !$#title Amino acid sequence of the light chain of bovine factor X-1 !1(Stuart factor). !$#cross-references MUID:80130563; PMID:6766735 !$#accession A14997 !'##molecule_type protein !'##residues 41-102,'N',104-180 ##label ENF REFERENCE A20274 !$#authors McMullen, B.A.; Fujikawa, K.; Kisiel, W. !$#journal Biochem. Biophys. Res. Commun. (1983) 115:8-14 !$#title The occurrence of beta-hydroxyaspartic acid in the vitamin !1K-dependent blood coagulation zymogens. !$#cross-references MUID:83308813; PMID:6688526 !$#contents annotation; revision to residue 103 REFERENCE A12030 !$#authors Titani, K.; Fujikawa, K.; Enfield, D.L.; Ericsson, L.H.; !1Walsh, K.A.; Neurath, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1975) 72:3082-3086 !$#title Bovine factor X-1 (Stuart factor): amino-acid sequence of !1heavy chain. !$#cross-references MUID:76053069; PMID:1059093 !$#accession A12030 !'##molecule_type protein !'##residues 183-292,294-295,'GDE',299-334,336-348,'AE',351-354,356-441, !1'GKFG',446-492 ##label TIT !'##note carbohydrate binding sites and disulfide bonds were determined REFERENCE A34412 !$#authors Persson, E.; Selander, M.; Linse, S.; Drakenberg, T.; !1Oehlin, A.K.; Stenflo, J. !$#journal J. Biol. Chem. (1989) 264:16897-16904 !$#title Calcium binding to the isolated beta-hydroxyaspartic !1acid-containing epidermal growth factor-like domain of !1bovine factor X. !$#cross-references MUID:89380326; PMID:2789221 !$#accession A34412 !'##molecule_type protein !'##residues 85-126 ##label PER !'##note beta-hydroxyaspartic acid site REFERENCE S39414 !$#authors Inoue, K.; Morita, T. !$#journal Eur. J. Biochem. (1993) 218:153-163 !$#title Identification of O-linked oligosaccharide chains in the !1activation peptides of blood coagulation factor X. The role !1of the carbohydrate moieties in the activation of factor X. !$#cross-references MUID:94062825; PMID:8243461 !$#accession S39414 !'##molecule_type protein !'##residues 183-196;199-209;216-233 ##label INO !'##note carbohydrate binding sites REFERENCE A12453 !$#authors Titani, K.; Hermodson, M.A.; Fujikawa, K.; Ericsson, L.H.; !1Walsh, K.A.; Neurath, H.; Davie, E.W. !$#journal Biochemistry (1972) 11:4899-4903 !$#title Bovine factor X-1a (activated Stuart factor). Evidence of !1homology with mammalian serine proteases. !$#cross-references MUID:73053314; PMID:4264286 !$#contents annotation; active site REFERENCE A13504 !$#authors Fujikawa, K.; Titani, K.; Davie, E.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1975) 72:3359-3363 !$#title Activation of bovine factor X (Stuart factor): conversion of !1factor Xaalpha to factor Xabeta. !$#cross-references MUID:76053121; PMID:1059122 !$#contents annotation; activation REFERENCE A38024 !$#authors Sugo, T.; Bjork, I.; Holmgren, A.; Stenflo, J. !$#journal J. Biol. Chem. (1984) 259:5705-5710 !$#title Calcium-binding properties of bovine factor X lacking the !1gamma-carboxyglutamic acid-containing region. !$#cross-references MUID:84185716; PMID:6546930 !$#contents annotation; calcium binding REFERENCE A38025 !$#authors Morita, T.; Jackson, C.M. !$#journal J. Biol. Chem. (1986) 261:4008-4014 !$#cross-references MUID:86140210; PMID:3949800 !$#contents annotation; sulfate binding COMMENT Factor Xa converts prothrombin to thrombin during blood !1clotting. COMMENT The two chains are formed from a single-chain precursor by !1the excision of two arginine residues and are held together !1by one or more disulfide bonds. COMMENT The activation peptide is cleaved by factor IXa (in the !1intrinsic pathway), or by factor VIIa (in the extrinsic !1pathway). Also residues 476-492 may be removed but this is !1not necessary for activation. COMMENT Calcium binds to the gamma-carboxyglutamic acid (Gla) !1residues and, with stronger affinity, to another site, !1beyond the Gla domain. COMMENT The gamma-carboxyglutamic acid residues arise by a !1posttranslational, vitamin K-dependent, enzymatic !1carboxylation of glutamic acid residues. GENETICS !$#gene F10 !$#map_position 13q34 FUNCTION !$#description catalyzes the proteolytic activation of prothrombin to !1thrombin in the presence of calcium, phospholipid, and !1factor Va !$#pathway blood coagulation CLASSIFICATION #superfamily coagulation factor X; EGF homology; Gla domain !1homology; trypsin homology KEYWORDS beta-hydroxyaspartic acid; blood coagulation; calcium !1binding; carboxyglutamic acid; glycoprotein; hydrolase; !1plasma; serine proteinase; sulfoprotein FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-40 #domain propeptide #status predicted #label PRO\ !$25-84 #domain Gla domain homology #label GLA\ !$41-180 #product coagulation factor X light chain #status !8experimental #label LCH\ !$90-121 #domain EGF homology #label EG1\ !$129-164 #domain EGF homology #label EG2\ !$183-492 #product coagulation factor X heavy chain #status !8experimental #label HCH\ !$183-233 #domain activation peptide #status experimental !8#label APT\ !$234-492 #product coagulation factor Xa heavy chain #status !8experimental #label AHC\ !$234-461 #domain trypsin homology #label TRY\ !$46,47,54,56,59,60, !$65,66,69,72,75,79 #modified_site gamma-carboxyglutamic acid (Glu) !8#status experimental\ !$57-62,90-101, !$95-110,112-121, !$129-140,136-149, !$151-164,172-341 #disulfide_bonds #status predicted\ !$103 #modified_site erythro-beta-hydroxyaspartic acid !8(Asp) #status experimental\ !$200 #binding_site sulfate (Tyr) (covalent) (partial) !8#status experimental\ !$208,485 #binding_site carbohydrate (Thr) (covalent) #status !8experimental\ !$218 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$233-234 #cleavage_site Arg-Ile (coagulation factor IXa, !8coagulation factor VIIa) #status experimental\ !$240-245,260-276, !$389-403,414-442 #disulfide_bonds #status experimental\ !$275,321,418 #active_site His, Asp, Ser #status predicted SUMMARY #length 492 #molecular-weight 54510 #checksum 2818 SEQUENCE /// ENTRY EXRT #type complete TITLE coagulation factor Xa (EC 3.4.21.6) precursor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Jan-1995 #sequence_revision 07-Feb-1997 #text_change 08-Dec-2000 ACCESSIONS S49075; JC4670; PS0191; PS0190; I62745 REFERENCE A58498 !$#authors Stanton, C.; Ross, P.; Hutson, S.; Wallin, R. !$#journal Thromb. Res. (1995) 80:63-73 !$#title Evidence for competition between vitamin K-dependent !1clotting factors for intracellular processing by the vitamin !1K-dependent gamma-carboxylase. !$#cross-references MUID:96093366; PMID:8578539 !$#accession S49075 !'##molecule_type mRNA !'##residues 1-482 ##label STA1 !'##cross-references EMBL:X79807; NID:g506600; PIDN:CAA56202.1; !1PID:g506601 !'##note submitted to the EMBL Data Library, June 1994 !'##note neither the complete nucleic acid sequence nor the complete !1translation are shown REFERENCE JC4670 !$#authors Stanton, C.; Ross, R.P.; Hutson, S.; Wallin, R. !$#journal Gene (1996) 169:269-273 !$#title Processing and expression of rat and human clotting !1factor-X-encoding cDNAs. !$#cross-references MUID:96194815; PMID:8647460 !$#accession JC4670 !'##molecule_type mRNA !'##residues 1-482 ##label STA2 !'##cross-references EMBL:X79807; NID:g506600; PIDN:CAA56202.1; !1PID:g506601 !'##experimental_source Cos-1 cell REFERENCE PS0190 !$#authors Enjyoji, K.; Miyazaki, K.; Kato, H. !$#journal J. Biochem. (1991) 109:890-898 !$#title Characterization of rat factors X and Xa: demonstration of !1factor Xa in rat plasma. !$#cross-references MUID:92041742; PMID:1718949 !$#accession PS0191 !'##molecule_type protein !'##residues 41-58,'X',60-65 ##label ENJ1 !$#accession PS0190 !'##molecule_type protein !'##residues 183-186,'X',188-207 ##label ENJ2 REFERENCE I46196 !$#authors Murakawa, M.; Okamura, T.; Kamura, T.; Kuroiwa, M.; Harada, !1M.; Niho, Y. !$#journal Eur. J. Haematol. (1994) 52:162-168 !$#title Analysis of the partial nucleotide sequences and deduced !1primary structures of the protease domains of mammalian !1blood coagulation factors VII and X. !$#cross-references MUID:94222160; PMID:8168596 !$#accession I62745 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 295-383,'G',385-455 ##label MUR !'##cross-references GB:D21215; NID:g415309; PIDN:BAA04756.1; !1PID:g455396 FUNCTION !$#description catalyzes the proteolytic activation of prothrombin to !1thrombin in the presence of calcium, phospholipid, and !1factor Va !$#pathway blood coagulation CLASSIFICATION #superfamily coagulation factor X; EGF homology; Gla domain !1homology; trypsin homology KEYWORDS beta-hydroxyaspartic acid; blood coagulation; calcium !1binding; carboxyglutamic acid; glycoprotein; hydrolase; !1plasma; serine proteinase FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-40 #domain propeptide #status predicted #label PRO\ !$25-84 #domain Gla domain homology #label GLA\ !$41-179 #product coagulation factor X light chain #status !8predicted #label LCH\ !$90-121 #domain EGF homology #label EG1\ !$129-164 #domain EGF homology #label EG2\ !$183-482 #product coagulation factor X heavy chain #status !8predicted #label HCH\ !$183-231 #domain activation peptide #status predicted #label !8APT\ !$232-482 #product coagulation factor Xa heavy chain #status !8predicted #label ACT\ !$232-460 #domain trypsin homology #label TRY\ !$46,47,54,56,59,60, !$65,66,69,72,79 #modified_site gamma-carboxyglutamic acid (Glu) !8#status predicted\ !$57-62,90-101, !$95-110,112-121, !$129-140,136-149, !$151-164,172-340, !$238-243,259-275, !$388-402,413-441 #disulfide_bonds #status predicted\ !$103 #modified_site erythro-beta-hydroxyaspartic acid !8(Asp) #status predicted\ !$187 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$208 #binding_site carbohydrate (Thr) (covalent) #status !8predicted\ !$218 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$231-232 #cleavage_site Arg-Ile (coagulation factor IXa, !8coagulation factor VIIa) #status predicted\ !$274,320,417 #active_site His, Asp, Ser #status predicted SUMMARY #length 482 #molecular-weight 54265 #checksum 158 SEQUENCE /// ENTRY EXCH #type complete TITLE coagulation factor Xa (EC 3.4.21.6) precursor - chicken ALTERNATE_NAMES virus-activating proteinase ORGANISM #formal_name Gallus gallus #common_name chicken DATE 12-Feb-1993 #sequence_revision 07-Feb-1997 #text_change 16-Jul-1999 ACCESSIONS S15838; S20380; S20381 REFERENCE S15838 !$#authors Suzuki, H.; Harada, A.; Hayashi, Y.; Wada, K.; Asaka, J.; !1Gotoh, B.; Ogasawara, T.; Nagai, Y. !$#journal FEBS Lett. (1991) 283:281-285 !$#title Primary structure of the virus activating protease from !1chick embryo. Its identity with the blood clotting factor !1Xa. !$#cross-references MUID:91257322; PMID:2044767 !$#accession S15838 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-475 ##label SUZ !'##cross-references DDBJ:D00844; NID:g222869; PIDN:BAA00724.1; !1PID:g222870 REFERENCE S20380 !$#authors Gotoh, B.; Yamauchi, F.; Ogasawara, T.; Nagai, Y. !$#journal FEBS Lett. (1992) 296:274-278 !$#title Isolation of factor Xa from chick embryo as the amniotic !1endoprotease responsible for paramyxovirus activation. !$#cross-references MUID:92164779; PMID:1537403 !$#accession S20380 !'##molecule_type protein !'##residues 41-55 ##label GO2 !$#accession S20381 !'##molecule_type protein !'##residues 241-246,'X',248-251,'X',253-261 ##label GOT FUNCTION !$#description catalyzes the proteolytic activation of prothrombin to !1thrombin in the presence of calcium, phospholipid, and !1factor Va !$#pathway blood coagulation CLASSIFICATION #superfamily coagulation factor X; EGF homology; Gla domain !1homology; trypsin homology KEYWORDS beta-hydroxyaspartic acid; blood coagulation; calcium !1binding; carboxyglutamic acid; glycoprotein; hydrolase; !1plasma; serine proteinase FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-40 #domain propeptide #status predicted #label PRO\ !$25-84 #domain Gla domain homology #label GLA\ !$41-185 #product coagulation factor X light chain #status !8experimental #label LCH\ !$90-121 #domain EGF homology #label EG1\ !$129-167 #domain EGF homology #label EG2\ !$186-475 #product coagulation factor X heavy chain #status !8predicted #label HCH\ !$186-240 #domain activation peptide #status predicted #label !8APT\ !$241-475 #product coagulation factor Xa heavy chain #status !8experimental #label AHC\ !$241-468 #domain trypsin homology #label TRY\ !$46,47,54,56,59,60, !$65,66,69,72,75,79 #modified_site gamma-carboxyglutamic acid (Glu) !8#status predicted\ !$57-62,90-101, !$95-110,112-121, !$129-140,136-152, !$154-167,175-348, !$247-252,267-283, !$396-410,421-449 #disulfide_bonds #status predicted\ !$103 #modified_site erythro-beta-hydroxyaspartic acid !8(Asp) #status predicted\ !$196,207,228,285 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$282,328,425 #active_site His, Asp, Ser #status predicted SUMMARY #length 475 #molecular-weight 53142 #checksum 7282 SEQUENCE /// ENTRY KFHU #type complete TITLE coagulation factor IXa (EC 3.4.21.22) precursor [validated] - human ALTERNATE_NAMES antihemophilic factor B; Christmas factor ORGANISM #formal_name Homo sapiens #common_name man DATE 17-Dec-1982 #sequence_revision 30-Jun-1987 #text_change 15-Sep-2000 ACCESSIONS A00922; A37570; A30511; A32989; A22673; A21337; A37546; !1A30623; A60486; A20274; S02527; S12058; S12377; I59612; !1I59529; A54255 REFERENCE A00922 !$#authors Yoshitake, S.; Schach, B.G.; Foster, D.C.; Davie, E.W.; !1Kurachi, K. !$#journal Biochemistry (1985) 24:3736-3750 !$#title Nucleotide sequence of the gene for human factor IX !1(antihemophilic factor B). !$#cross-references MUID:86000558; PMID:2994716 !$#accession A00922 !'##molecule_type DNA !'##residues 1-461 ##label YOS !'##cross-references GB:K02402; NID:g182612; PIDN:AAB59620.1; !1PID:g182613 REFERENCE A37570 !$#authors Anson, D.S.; Choo, K.H.; Rees, D.J.G.; Giannelli, F.; Gould, !1K.; Huddleston, J.A.; Brownlee, G.G. !$#journal EMBO J. (1984) 3:1053-1060 !$#title The gene structure of human anti-haemophilic factor IX. !$#cross-references MUID:84236100; PMID:6329734 !$#accession A37570 !'##molecule_type DNA !'##residues 1-461 ##label ANS !'##cross-references GB:K02048 REFERENCE A30511 !$#authors Reitsma, P.H.; Bertina, R.M.; Ploos van Amstel, J.K.; !1Riemens, A.; Briet, E. !$#journal Blood (1988) 72:1074-1076 !$#title The putative factor IX gene promoter in hemophilia B Leyden. !$#cross-references MUID:88327116; PMID:3416069 !$#accession A30511 !'##molecule_type DNA !'##residues 8-24 ##label REI !'##cross-references EMBL:X55008; NID:g311288; PIDN:CAB38245.2; !1PID:g4469253 REFERENCE A32989 !$#authors Koeberl, D.D.; Bottema, C.D.K.; Buerstedde, J.M.; Sommer, !1S.S. !$#journal Am. J. Hum. Genet. (1989) 45:448-457 !$#title Functionally important regions of the factor IX gene have a !1low rate of polymorphism and a high rate of mutation in the !1dinucleotide CpG. !$#cross-references MUID:89371752; PMID:2773937 !$#accession A32989 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 30-92 ##label KOE REFERENCE A22673 !$#authors McGraw, R.A.; Davis, L.M.; Noyes, C.M.; Lundblad, R.L.; !1Roberts, H.R.; Graham, J.B.; Stafford, D.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:2847-2851 !$#title Evidence for a prevalent dimorphism in the activation !1peptide of human coagulation factor IX. !$#cross-references MUID:85190593; PMID:3857619 !$#accession A22673 !'##molecule_type mRNA !'##residues 1-193,'T',195-461 ##label MCG !'##cross-references GB:M11309; NID:g180552; PIDN:AAA52023.1; !1PID:g180553 !'##note the authors translated the codon ACA for residue 29 as Tyr REFERENCE A21337 !$#authors Jaye, M.; de la Salle, H.; Schamber, F.; Balland, A.; Kohli, !1V.; Findeli, A.; Tolstoshev, P.; Lecocq, J.P. !$#journal Nucleic Acids Res. (1983) 11:2325-2335 !$#title Isolation of a human anti-haemophilic factor IX cDNA clone !1using a unique 52-base synthetic oligonucleotide probe !1deduced from the amino acid sequence of bovine factor IX. !$#cross-references MUID:83220788; PMID:6687940 !$#accession A21337 !'##molecule_type mRNA !'##residues 1-193,'T',195-461 ##label JAY !'##cross-references GB:J00137; NID:g182610; PIDN:AAA52763.1; !1PID:g182611 REFERENCE A37546 !$#authors Jagadeeswaran, P.; Lavelle, D.E.; Kaul, R.; Mohandas, T.; !1Warren, S.T. !$#journal Somat. Cell Mol. Genet. (1984) 10:465-473 !$#title Isolation and characterization of human factor IX cDNA: !1identification of Taq I polymorphism and regional !1assignment. !$#cross-references MUID:84300526; PMID:6089357 !$#accession A37546 !'##molecule_type mRNA !'##residues 38-193,'T',195-326 ##label JAG !'##cross-references GB:M35672 REFERENCE A30623 !$#authors Kurachi, K.; Davie, E.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:6461-6464 !$#title Isolation and characterization of a cDNA coding for human !1factor IX. !$#cross-references MUID:83065193; PMID:6959130 !$#accession A30623 !'##molecule_type mRNA !'##residues 1-12,'S',14-73,'P',75-82,'K',84-203,'P',205-216,'G', !1218-298,'A',299-356,'A',358-461 ##label KUR !'##cross-references GB:J00136; NID:g182608; PIDN:AAA98726.1; !1PID:g182609 !'##experimental_source liver REFERENCE A60486 !$#authors Tharakan, J.; Strickland, D.; Burgess, W.; Drohan, W.N.; !1Clark, D.B. !$#journal Vox Sang. (1990) 58:21-29 !$#title Development of an immunoaffinity process for factor IX !1purification. !$#cross-references MUID:90194857; PMID:2316207 !$#accession A60486 !'##molecule_type protein !'##residues 47-52,'XX',55-60,'X',62,'XX',65 ##label THA REFERENCE A20274 !$#authors McMullen, B.A.; Fujikawa, K.; Kisiel, W. !$#journal Biochem. Biophys. Res. Commun. (1983) 115:8-14 !$#title The occurrence of beta-hydroxyaspartic acid in the vitamin !1K-dependent blood coagulation zymogens. !$#cross-references MUID:83308813; PMID:6688526 !$#accession A20274 !'##molecule_type protein !'##residues 105-109,'X',111-115 ##label MCM REFERENCE S02527 !$#authors Balland, A.; Faure, T.; Carvallo, D.; Cordier, P.; Ulrich, !1P.; Fournet, B.; de la Salle, H.; Lecocq, J.P. !$#journal Eur. J. Biochem. (1988) 172:565-572 !$#title Characterisation of two differently processed forms of human !1recombinant factor IX synthesised in CHO cells transformed !1with a polycistronic vector. !$#cross-references MUID:88166735; PMID:3280312 !$#accession S02527 !'##molecule_type protein !'##residues 29-63 ##label BAL !'##note processed forms expressed in recombinant system REFERENCE S12058 !$#authors Jallat, S.; Perraud, F.; Dalemans, W.; Balland, A.; !1Dieterle, A.; Faure, T.; Meulien, P.; Pavirani, A. !$#journal EMBO J. (1990) 9:3295-3301 !$#title Characterization of recombinant human Factor IX expressed in !1transgenic mice and in derived transimmortalized hepatic !1cell lines. !$#cross-references MUID:91006024; PMID:2209546 !$#accession S12058 !'##molecule_type mRNA; protein !'##residues 1-68 ##label JAL !'##note processed forms expressed in recombinant system REFERENCE S12377 !$#authors Handford, P.A.; Baron, M.; Mayhew, M.; Willis, A.; Beesley, !1T.; Brownlee, G.G.; Campbell, I.D. !$#journal EMBO J. (1990) 9:475-480 !$#title The first EGF-like domain from human factor IX contains a !1high-affinity calcium binding site. !$#cross-references MUID:90151623; PMID:2406129 !$#accession S12377 !'##molecule_type protein !'##residues 92-130 ##label HAN !'##note NMR detection of calcium binding by domain expressed in !1recombinant system REFERENCE I59612 !$#authors de la Salle, C.; Charmantier, J.L.; Baas, M.J.; Schwartz, !1A.; Wiesel, M.L.; Grunebaum, L.; Cazenave, J.P. !$#journal Thromb. Haemost. (1993) 70:370-371 !$#title A deletion located in the 3' non translated part of the !1factor IX gene responsible for mild haemophilia B. !$#cross-references MUID:94054330; PMID:8236150 !$#accession I59612 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 444-461 ##label RES !'##cross-references GB:S66752; NID:g439773; PIDN:AAB28588.1; !1PID:g439774 REFERENCE I59529 !$#authors Stoflet, E.S.; Koeberl, D.D.; Sarkar, G.; Sommer, S.S. !$#journal Science (1988) 239:491-494 !$#title Genomic amplification with transcript sequencing. !$#cross-references MUID:88127096; PMID:3340835 !$#accession I59529 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 290-359 ##label RE2 !'##cross-references GB:M19063; NID:g182622; PIDN:AAA52456.1; !1PID:g182623 REFERENCE A54255 !$#authors Agarwala, K.L.; Kawabata, S.; Takao, T.; Murata, H.; !1Shimonishi, Y.; Nishimura, H.; Iwanaga, S. !$#journal Biochemistry (1994) 33:5167-5171 !$#title Activation peptide of human factor IX has oligosaccharides !1O-glycosidically linked to threonine residues at 159 and !1169. !$#cross-references MUID:94227047; PMID:8172892 !$#accession A54255 !'##molecule_type protein !'##residues 'D',204,'X',206-211;212,'D',214,'X',216-221,'D' ##label AGA !'##note the residues designated 'X' were determined to be threonine !1bound to carbohydrate REFERENCE A18483 !$#authors Di Scipio, R.G.; Kurachi, K.; Davie, E.W. !$#journal J. Clin. Invest. (1978) 61:1528-1538 !$#title Activation of human factor IX (Christmas factor). !$#cross-references MUID:78194509; PMID:659613 !$#contents annotation; activation; active site; carbohydrate binding REFERENCE A37569 !$#authors McGraw, R.A.; Davis, L.M.; Noyes, C.M.; Graham, J.B.; !1Roberts, H.R.; Stafford, D.W. !$#journal Am. Soc. Hematol. Abstr. (1984) 64(Suppl.1):262a !$#contents annotation !$#note 194-Thr was also found REFERENCE A37543 !$#authors Morita, T.; Isaacs, B.S.; Esmon, C.T.; Johnson, A.E. !$#journal J. Biol. Chem. (1984) 259:5698-5704 !$#title Derivatives of blood coagulation factor IX contain a high !1affinity Ca2+-binding site that lacks gamma-carboxyglutamic !1acid. !$#cross-references MUID:84185715; PMID:6425296 !$#contents annotation; calcium binding REFERENCE A37544 !$#authors Morita, T.; Isaacs, B.S.; Esmon, C.T.; Johnson, A.E. !$#journal J. Biol. Chem. (1985) 260:2583 !$#contents annotation; calcium binding, correction REFERENCE A37545 !$#authors Bentley, A.K.; Rees, D.J.G.; Rizza, C.; Brownlee, G.G. !$#journal Cell (1986) 45:343-348 !$#title Defective propeptide processing of blood clotting factor IX !1caused by mutation of arginine to glutamine at position -4. !$#cross-references MUID:86189947; PMID:3009023 !$#contents annotation; signal sequence cleavage site REFERENCE A30622 !$#authors Suehiro, K.; Kawabata, S.I.; Miyata, T.; Takeya, H.; !1Takamatsu, J.; Ogata, K.; Kamiya, T.; Saito, H.; Niho, Y.; !1Iwanaga, S. !$#journal J. Biol. Chem. (1989) 264:21257-21265 !$#title Blood clotting factor IX B(M) Nagoya: substitution of !1arginine 180 by tryptophan and its activation by !1alpha-chymotrypsin and rat mast cell chymase. !$#cross-references MUID:90078229; PMID:2592373 !$#contents annotation; sequence of mutant B(M) Nagoya !$#note carboxylation, glycosylation, and cleavage sites REFERENCE A51252 !$#authors Baron, M.; Norman, D.G.; Harvey, T.S.; Hanford, P.A.; !1Mayhew, M.; Tse, A.G.D.; Brownlee, G.G.; Campbell, I.D.C. !$#submission submitted to the Brookhaven Protein Data Bank, November 1991 !$#cross-references PDB:1IXA !$#contents annotation; conformation by (1)H-NMR, residues 92-130 !$#note recombinant form expressed in yeast COMMENT Factor IX is activated by factor XIa, which excises the !1activation peptide producing a molecule of two chains held !1together by one or more disulfide bonds. COMMENT The gamma-carboxyglutamic acid residues arise by !1posttranslational, vitamin K-dependent carboxylation of !1glutamic acid residues. COMMENT Calcium binds to the gamma-carboxyglutamic acid (Gla) !1residues and, with stronger affinity, to another site, !1beyond the Gla domain. GENETICS !$#gene GDB:F9 !'##cross-references GDB:119900; OMIM:306900 !$#map_position Xq27.1-Xq27.2 !$#introns 30/1; 84/2; 93/1; 131/1; 174/1; 241/3; 280/1 FUNCTION !$#description catalyzes the proteolytic activation of coagulation factor X !1in the presence of calcium, phospholipid, and factor VIIIa !$#pathway blood coagulation intrinsic pathway CLASSIFICATION #superfamily coagulation factor X; EGF homology; Gla domain !1homology; trypsin homology KEYWORDS beta-hydroxyaspartic acid; blood coagulation; calcium !1binding; carboxyglutamic acid; glycoprotein; hemophilia B; !1hydrolase; phosphoprotein; plasma; serine proteinase; !1vitamin K FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-46 #domain propeptide #status experimental #label PPT\ !$31-91 #domain Gla domain homology #label GLA\ !$47-191 #product coagulation factor IXa light chain #status !8experimental #label ALC\ !$97-128 #domain EGF homology #label EG1\ !$134-170 #domain EGF homology #label EG2\ !$192-226 #domain activation peptide #status experimental !8#label ACT\ !$227-461 #product coagulation factor IXa heavy chain #status !8experimental #label AHC\ !$227-454 #domain trypsin homology #label TRY\ !$53,54,61,63,66,67, !$72,73,76,79,82,86 #modified_site gamma-carboxyglutamic acid (Glu) !8#status experimental\ !$64-69,97-108, !$102-117,119-128, !$134-145,141-155, !$157-170,178-335, !$252-268,382-396, !$407-435 #disulfide_bonds #status experimental\ !$99 #binding_site carbohydrate (Ser) (covalent) #status !8experimental\ !$110 #modified_site erythro-beta-hydroxyaspartic acid !8(Asp) #status experimental\ !$191-192 #cleavage_site Arg-Ala (coagulation factor XIa) !8#status experimental\ !$203,213 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$205,215 #binding_site carbohydrate (Thr) (covalent) #status !8experimental\ !$226-227 #cleavage_site Arg-Val (coagulation factor XIa) !8#status experimental\ !$267,315 #active_site His, Asp #status predicted\ !$411 #active_site Ser #status experimental SUMMARY #length 461 #molecular-weight 51748 #checksum 9506 SEQUENCE /// ENTRY A30351 #type complete TITLE coagulation factor IXa (EC 3.4.21.22) precursor - dog ORGANISM #formal_name Canis lupus familiaris #common_name dog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A30351; I46201 REFERENCE A30351 !$#authors Evans, J.P.; Watzke, H.H.; Ware, J.L.; Stafford, D.W.; High, !1K.A. !$#journal Blood (1989) 74:207-212 !$#title Molecular cloning of a cDNA encoding canine factor IX. !$#cross-references MUID:89323338; PMID:2752110 !$#accession A30351 !'##status preliminary !'##molecule_type mRNA !'##residues 1-452 ##label EVA !'##cross-references GB:M21757; NID:g972719; PIDN:AAA75006.1; !1PID:g163948 REFERENCE I46201 !$#authors Axelrod, J.H.; Read, M.S.; Brinkhous, K.M.; Verma, I.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:5173-5177 !$#title Phenotypic correction of factor IX deficiency in skin !1fibroblasts of hemophilic dogs. !$#cross-references MUID:90311364; PMID:2367529 !$#accession I46201 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-452 ##label AXE !'##cross-references GB:M33826; NID:g163949; PIDN:AAA30844.1; !1PID:g163950 CLASSIFICATION #superfamily coagulation factor X; EGF homology; Gla domain !1homology; trypsin homology KEYWORDS beta-hydroxyaspartic acid; blood coagulation; calcium !1binding; carboxyglutamic acid; glycoprotein; hydrolase; !1serine proteinase FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-40 #domain propeptide #status predicted #label PRO\ !$24-84 #domain Gla domain homology #label GLA\ !$41-452 #product coagulation factor IX #status predicted !8#label MAT\ !$90-121 #domain EGF homology #label EG1\ !$127-163 #domain EGF homology #label EG2\ !$218-445 #domain trypsin homology #label TRY\ !$46,47,54,56,59,60, !$65,66,69,72,75,79 #modified_site gamma-carboxyglutamic acid (Glu) !8#status predicted\ !$57-62,90-101, !$95-110,112-121, !$127-138,134-148, !$150-163,171-326, !$243-259,373-387, !$398-426 #disulfide_bonds #status predicted\ !$258,306,402 #active_site His, Asp, Ser #status predicted SUMMARY #length 452 #molecular-weight 50827 #checksum 6835 SEQUENCE /// ENTRY KFBO #type complete TITLE coagulation factor IXa (EC 3.4.21.22) precursor - bovine ALTERNATE_NAMES Christmas factor ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Nov-1980 #sequence_revision 03-Aug-1984 #text_change 16-Jul-1999 ACCESSIONS A14757; B20274; I45891; A00923 REFERENCE A14757 !$#authors Katayama, K.; Ericsson, L.H.; Enfield, D.L.; Walsh, K.A.; !1Neurath, H.; Davie, E.W.; Titani, K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1979) 76:4990-4994 !$#title Comparison of amino acid sequence of bovine coagulation !1factor IX (Christmas factor) with that of other vitamin !1K-dependent plasma proteins. !$#cross-references MUID:80056619; PMID:291916 !$#accession A14757 !'##molecule_type protein !'##residues 1-63,'T',65-416 ##label KAT REFERENCE A20274 !$#authors McMullen, B.A.; Fujikawa, K.; Kisiel, W. !$#journal Biochem. Biophys. Res. Commun. (1983) 115:8-14 !$#title The occurrence of beta-hydroxyaspartic acid in the vitamin !1K-dependent blood coagulation zymogens. !$#cross-references MUID:83308813; PMID:6688526 !$#accession B20274 !'##molecule_type protein !'##residues 59-63,'X',65-69 ##label MCM REFERENCE I45891 !$#authors Choo, K.H.; Gould, K.G.; Rees, D.J.G.; Brownlee, G.G. !$#journal Nature (1982) 299:178-180 !$#title Molecular cloning of the gene for human anti-haemophilic !1factor IX. !$#cross-references MUID:82272386; PMID:6287289 !$#accession I45891 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 52-139 ##label CHO !'##cross-references GB:J00007; NID:g163053; PIDN:AAA30520.1; !1PID:g163054 REFERENCE A44556 !$#authors Hase, S.; Kawabata, S.; Nishimura, H.; Takeya, H.; Sueyoshi, !1T.; Miyata, T.; Iwanaga, S.; Takao, T.; Shimonishi, Y.; !1Ikenaka, T. !$#journal J. Biochem. (1988) 104:867-868 !$#title A new trisaccharide sugar chain linked to a serine residue !1in bovine blood coagulation factors VII and IX. !$#cross-references MUID:89213999; PMID:3149637 !$#contents annotation !$#note structure and location of a carbohydrate covalently bound to !1Ser COMMENT Factor IX is activated by factor XIa, which excises the !1activation peptide producing a molecule of two chains held !1together by one or more disulfide bonds. COMMENT The gamma-carboxyglutamic acid residues arise by !1posttranslational, vitamin K-dependent carboxylation of !1glutamic acid residues. COMMENT Calcium binds to the gamma-carboxyglutamic acid (Gla) !1residues and, with stronger affinity, to another site, !1beyond the Gla domain. FUNCTION !$#description catalyzes the proteolytic activation of coagulation factor X !1in the presence of calcium, phospholipid, and factor VIIIa !$#pathway blood coagulation intrinsic pathway CLASSIFICATION #superfamily coagulation factor X; EGF homology; Gla domain !1homology; trypsin homology KEYWORDS beta-hydroxyaspartic acid; blood coagulation; calcium !1binding; carboxyglutamic acid; glycoprotein; hydrolase; !1plasma; serine proteinase FEATURE !$1-146 #product coagulation factor IXa light chain #status !8experimental #label ALC\ !$1-45 #domain Gla domain homology (fragment) #label GLA\ !$51-82 #domain EGF homology #label EG1\ !$88-124 #domain EGF homology #label EG2\ !$147-181 #domain activation peptide #status experimental !8#label APT\ !$182-416 #product coagulation factor IXa heavy chain #status !8experimental #label AHC\ !$182-409 #domain trypsin homology #label TRY\ !$7,8,15,17,20,21,26, !$27,30,33,36,40 #modified_site gamma-carboxyglutamic acid (Glu) !8#status experimental\ !$18-23,51-62,56-71, !$73-82,88-99,95-109, !$111-124,132-290, !$207-223,337-351, !$362-390 #disulfide_bonds #status predicted\ !$53 #binding_site carbohydrate (Ser) (covalent) #status !8experimental\ !$64 #modified_site erythro-beta-hydroxyaspartic acid !8(Asp) #status experimental\ !$158,168,173,261 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$222,270,366 #active_site His, Asp, Ser #status predicted SUMMARY #length 416 #molecular-weight 46785 #checksum 2007 SEQUENCE /// ENTRY KFHU7 #type complete TITLE coagulation factor VIIa (EC 3.4.21.21) precursor [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 19-May-1989 #sequence_revision 19-May-1994 #text_change 08-Dec-2000 ACCESSIONS A28322; A23819; A31186; B31186; S63524 REFERENCE A28322 !$#authors O'Hara, P.J.; Grant, F.J.; Haldeman, B.A.; Gray, C.L.; !1Insley, M.Y.; Hagen, F.S.; Murray, M.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:5158-5162 !$#title Nucleotide sequence of the gene coding for human factor VII, !1a vitamin K-dependent protein participating in blood !1coagulation. !$#cross-references MUID:87260948; PMID:3037537 !$#accession A28322 !'##molecule_type DNA !'##residues 1-466 ##label OHA !'##cross-references GB:J02933; NID:g180333; PIDN:AAA51983.1; !1PID:g180334 REFERENCE A23819 !$#authors Hagen, F.S.; Gray, C.L.; O'Hara, P.; Grant, F.J.; Saari, !1G.C.; Woodbury, R.G.; Hart, C.E.; Insley, M.; Kisiel, W.; !1Kurachi, K.; Davie, E.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:2412-2416 !$#title Characterization of a cDNA coding for human factor VII. !$#cross-references MUID:86205965; PMID:3486420 !$#accession A23819 !'##molecule_type mRNA !'##residues 1-466 ##label HAG !'##cross-references GB:M13232; NID:g182799; PIDN:AAA88040.1; !1PID:g182801 REFERENCE A90539 !$#authors Thim, L.; Bjoern, S.; Christensen, M.; Nicolaisen, E.M.; !1Lund-Hansen, T.; Pedersen, A.H.; Hedner, U. !$#journal Biochemistry (1988) 27:7785-7793 !$#title Amino acid sequence and posttranslational modifications of !1human factor VII-a from plasma and transfected baby hamster !1kidney cells. !$#cross-references MUID:89088153; PMID:3264725 !$#accession A31186 !'##molecule_type protein !'##residues 61-212 ##label THI !$#accession B31186 !'##molecule_type protein !'##residues 213-466 ##label TH2 REFERENCE A40529 !$#authors Bjoern, S.; Foster, D.C.; Thim, L.; Wiberg, F.C.; !1Christensen, M.; Komiyama, Y.; Pedersen, A.H.; Kisiel, W. !$#journal J. Biol. Chem. (1991) 266:11051-11057 !$#title Human plasma and recombinant factor VII. Characterization of !1O-glycosylations at serine residues 52 and 60 and effects of !1site-directed mutagenesis of serine 52 to alanine. !$#cross-references MUID:91250411; PMID:1904059 !$#contents annotation; carbohydrate binding sites REFERENCE S63524 !$#authors Persson, E.; Petersen, L.C. !$#journal Eur. J. Biochem. (1995) 234:293-300 !$#title Structurally and functionally distinct Ca(2+) binding sites !1in the gamma-carboxyglutamic acid-containing domain of !1factor VIIa. !$#cross-references MUID:96096752; PMID:8529655 !$#accession S63524 !'##molecule_type protein !'##residues 61-65;99-103;105-109;213-217;308-312 ##label PER GENETICS !$#gene GDB:F7 !'##cross-references GDB:119897; OMIM:227500 !$#map_position 13q34-13q34 !$#introns 22/1; 44/1; 97/3; 106/1; 144/1; 191/1; 227/3; 269/1 FUNCTION !$#description catalyzes the proteolytic activation of coagulation factor X !1in the presence of calcium and tissue factor, coagulation !1factor III; capable of catalyzing the proteolytic activation !1of coagulation factor IX in the presence of calcium and !1tissue factor !$#pathway blood coagulation extrinsic pathway CLASSIFICATION #superfamily coagulation factor X; EGF homology; Gla domain !1homology; trypsin homology KEYWORDS beta-hydroxyaspartic acid; blood coagulation; calcium !1binding; carboxyglutamic acid; glycoprotein; hydrolase; !1plasma; serine proteinase; vitamin K FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-60 #domain propeptide #status predicted #label PRO\ !$45-104 #domain Gla domain homology #label GLA\ !$61-212 #product coagulation factor VIIa light chain #status !8experimental #label MA1\ !$110-141 #domain EGF homology #label EG1\ !$151-187 #domain EGF homology #label EG2\ !$213-466 #product coagulation factor VIIa heavy chain #status !8experimental #label MA2\ !$213-447 #domain trypsin homology #label TRY\ !$66,67,74,76,79,80, !$85,86,89,95 #modified_site gamma-carboxyglutamic acid (Glu) !8#status experimental\ !$77-82,110-121, !$115-130,132-141, !$151-162,158-172, !$174-187,195-322, !$219-224,238-254, !$370-389,400-428 #disulfide_bonds #status predicted\ !$112,120 #binding_site carbohydrate (Ser) (covalent) #status !8experimental\ !$123 #modified_site erythro-beta-hydroxyaspartic acid !8(Asp) #status absent\ !$205,382 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$212-213 #cleavage_site Arg-Ile (coagulation factor XIIa) !8#status experimental\ !$253,302,404 #active_site His, Asp, Ser #status predicted\ !$350-351 #cleavage_site Arg-Gly (coagulation factor Xa) !8#status predicted SUMMARY #length 466 #molecular-weight 51593 #checksum 4382 SEQUENCE /// ENTRY KFBO7 #type complete TITLE coagulation factor VIIa (EC 3.4.21.21) - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 21-May-1990 #sequence_revision 23-Mar-1995 #text_change 16-Jul-1999 ACCESSIONS A31979; C20274 REFERENCE A31979 !$#authors Takeya, H.; Kawabata, S.; Nakagawa, K.; Yamamichi, Y.; !1Miyata, T.; Iwanaga, S. !$#journal J. Biol. Chem. (1988) 263:14868-14877 !$#title Bovine factor VII. Its purification and complete amino acid !1sequence. !$#cross-references MUID:89008362; PMID:3049594 !$#accession A31979 !'##molecule_type protein !'##residues 1-407 ##label TAK REFERENCE A20274 !$#authors McMullen, B.A.; Fujikawa, K.; Kisiel, W. !$#journal Biochem. Biophys. Res. Commun. (1983) 115:8-14 !$#title The occurrence of beta-hydroxyaspartic acid in the vitamin !1K-dependent blood coagulation zymogens. !$#cross-references MUID:83308813; PMID:6688526 !$#accession C20274 !'##molecule_type protein !'##residues 58-62,'X',64-68 ##label MCM !'##note the residue designated 'X' was determined to be hydroxyaspartic !1acid REFERENCE A44556 !$#authors Hase, S.; Kawabata, S.; Nishimura, H.; Takeya, H.; Sueyoshi, !1T.; Miyata, T.; Iwanaga, S.; Takao, T.; Shimonishi, Y.; !1Ikenaka, T. !$#journal J. Biochem. (1988) 104:867-868 !$#title A new trisaccharide sugar chain linked to a serine residue !1in bovine blood coagulation factors VII and IX. !$#cross-references MUID:89213999; PMID:3149637 !$#contents annotation !$#note structure and location of covalently bound carbohydrate FUNCTION !$#description catalyzes the proteolytic activation of coagulation factor X !1in the presence of calcium and tissue factor, coagulation !1factor 3; capable of catalyzing the proteolytic activation !1of coagulation factor IX in the presence of calcium and !1tissue factor !$#pathway blood coagulation extrinsic pathway CLASSIFICATION #superfamily coagulation factor X; EGF homology; Gla domain !1homology; trypsin homology KEYWORDS beta-hydroxyaspartic acid; blood coagulation; calcium !1binding; carboxyglutamic acid; glycoprotein; hydrolase; !1plasma; serine proteinase FEATURE !$1-152 #product coagulation factor VIIa light chain #status !8experimental #label MA1\ !$1-44 #domain Gla domain homology (fragment) #label GLA\ !$50-81 #domain EGF homology #label EG1\ !$91-127 #domain EGF homology #label EG2\ !$153-407 #product coagulation factor VIIa heavy chain #status !8experimental #label MA2\ !$153-387 #domain trypsin homology #label TRY\ !$6,7,14,16,19,20,25, !$26,29,34,35 #modified_site gamma-carboxyglutamic acid (Glu) !8#status experimental\ !$17-22,50-61,55-70, !$72-81,91-102, !$98-112,114-127, !$135-262,159-164, !$178-194,310-329, !$340-368 #disulfide_bonds #status predicted\ !$52 #binding_site carbohydrate (Ser) (covalent) #status !8experimental\ !$63 #modified_site erythro-beta-hydroxyaspartic acid !8(Asp) (partial) #status experimental\ !$145,203 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$152-153 #cleavage_site Arg-Ile (coagulation factor XIIa) !8#status experimental\ !$193,242,344 #active_site His, Asp, Ser #status predicted\ !$290-291 #cleavage_site Arg-Gly (coagulation factor Xa) !8#status experimental SUMMARY #length 407 #molecular-weight 44431 #checksum 8791 SEQUENCE /// ENTRY KXHUZ #type complete TITLE plasma protein Z precursor [validated] - human ALTERNATE_NAMES vitamin K-dependent glycoprotein Z ORGANISM #formal_name Homo sapiens #common_name man DATE 18-Jan-1991 #sequence_revision 05-Jan-1996 #text_change 08-Dec-2000 ACCESSIONS A36244; A35893; B35893 REFERENCE A36244 !$#authors Ichinose, A.; Takeya, H.; Espling, E.; Iwanaga, S.; Kisiel, !1W.; Davie, E.W. !$#journal Biochem. Biophys. Res. Commun. (1990) 172:1139-1144 !$#title Amino acid sequence of human protein Z, a vitamin !1K-dependent plasma glycoprotein. !$#cross-references MUID:91058548; PMID:2244898 !$#accession A36244 !'##molecule_type mRNA !'##residues 1-422 ##label ICH !'##cross-references GB:M55671; NID:g190465; PIDN:AAA36501.1; !1PID:g190466 !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing REFERENCE A35893 !$#authors Sejima, H.; Hayashi, T.; Deyashiki, Y.; Nishioka, J.; !1Suzuki, K. !$#journal Biochem. Biophys. Res. Commun. (1990) 171:661-668 !$#title Primary structure of vitamin K-dependent human protein Z. !$#cross-references MUID:90386637; PMID:2403355 !$#accession A35893 !'##molecule_type protein !'##residues 63-68,'XX',71-72,'X',74-76,'X',78,'XX',81,'XX',84,'X', !186-87,'XX',90,'XX',93-94,'X',96,'XX',99-100,'XX',103 ##label !1SEJ !$#accession B35893 !'##molecule_type mRNA !'##residues 103-422 ##label SE2 !'##cross-references GB:M59303; NID:g190461; PIDN:AAA36499.1; !1PID:g190462 GENETICS !$#gene GDB:PROZ !'##cross-references GDB:9957440; OMIM:176895 !$#map_position 13q34-13q34 CLASSIFICATION #superfamily coagulation factor X; EGF homology; Gla domain !1homology; trypsin homology KEYWORDS beta-hydroxyaspartic acid; calcium binding; carboxyglutamic !1acid; glycoprotein; vitamin K FEATURE !$1-10 #domain signal sequence #status predicted #label SIG\ !$11-62 #domain propeptide #status predicted #label PRO\ !$47-107 #domain Gla domain homology #label GLA\ !$63-422 #product protein Z #status experimental #label MAT\ !$113-144 #domain EGF homology #label EG1\ !$151-187 #domain EGF homology #label EG2\ !$199-417 #domain trypsin homology #label TRY\ !$69,70,73,77,79,82, !$83,88,89,92,95,97, !$102 #modified_site gamma-carboxyglutamic acid (Glu) !8#status experimental\ !$115 #binding_site carbohydrate (Ser) (covalent) #status !8experimental\ !$121,247,255,328,354 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$126 #modified_site erythro-beta-hydroxyaspartic acid !8(Asp) #status predicted\ !$134,337 #binding_site carbohydrate (Thr) (covalent) #status !8predicted\ !$225-241,349-363 #disulfide_bonds #status predicted\ !$258 #binding_site carbohydrate (Ser) (covalent) #status !8predicted SUMMARY #length 422 #molecular-weight 47053 #checksum 5502 SEQUENCE /// ENTRY KXBOZ #type complete TITLE plasma protein Z - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 16-Jul-1999 ACCESSIONS A22171; A00926 REFERENCE A22171 !$#authors Hoejrup, P.; Jensen, M.S.; Petersen, T.E. !$#journal FEBS Lett. (1985) 184:333-338 !$#title Amino acid sequence of bovine protein Z: a vitamin !1K-dependent serine protease homolog. !$#cross-references MUID:85204370; PMID:3888670 !$#accession A22171 !'##molecule_type protein !'##residues 1-396 ##label HOE COMMENT Protein Z is a single-chain plasma glycoprotein of unknown !1function. Although homologous with the vitamin K-dependent !1clotting factors, it has lost two of the essential catalytic !1residues and has no enzymatic activity. CLASSIFICATION #superfamily coagulation factor X; EGF homology; Gla domain !1homology; trypsin homology KEYWORDS beta-hydroxyaspartic acid; calcium binding; carboxyglutamic !1acid; glycoprotein; plasma FEATURE !$1-46 #domain calcium binding #status predicted #label CAB\ !$1-45 #domain Gla domain homology (fragment) #label GLA\ !$51-82 #domain EGF homology #label EG1\ !$89-125 #domain EGF homology #label EG2\ !$143-352 #domain trypsin homology #label TRY\ !$7,8,11,15,17,20,21, !$26,27,30,33,36,40 #modified_site gamma-carboxyglutamic acid (Glu) !8#status experimental\ !$59,191,289 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$64 #modified_site erythro-beta-hydroxyaspartic acid !8(Asp) #status predicted\ !$388 #binding_site carbohydrate (Thr) (covalent) #status !8experimental SUMMARY #length 396 #molecular-weight 43112 #checksum 2084 SEQUENCE /// ENTRY KXHU #type complete TITLE protein C (activated) (EC 3.4.21.69) precursor - human ALTERNATE_NAMES autoprothrombin IIA; plasma protein C ORGANISM #formal_name Homo sapiens #common_name man DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 16-Jul-1999 ACCESSIONS A22331; A25426; A21781; A23789; A00927 REFERENCE A22331 !$#authors Foster, D.C.; Yoshitake, S.; Davie, E.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:4673-4677 !$#title The nucleotide sequence of the gene for human protein C. !$#cross-references MUID:85270390; PMID:2991887 !$#accession A22331 !'##molecule_type DNA !'##residues 1-461 ##label FOS1 !'##cross-references GB:M11228; NID:g190333; PIDN:AAA60166.1; !1PID:g190334 REFERENCE A25426 !$#authors Plutzky, J.; Hoskins, J.A.; Long, G.L.; Crabtree, G.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:546-550 !$#title Evolution and organization of the human protein C gene. !$#cross-references MUID:86120978; PMID:3511471 !$#accession A25426 !'##molecule_type DNA !'##residues 1-445,'L',446-461 ##label PLU !'##cross-references GB:M12712; NID:g190330; PIDN:AAA60165.1; !1PID:g190332 REFERENCE A21781 !$#authors Foster, D.; Davie, E.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:4766-4770 !$#title Characterization of a cDNA coding for human protein C. !$#cross-references MUID:84272714; PMID:6589623 !$#accession A21781 !'##molecule_type mRNA !'##residues 'Q',107-461 ##label FOS2 !'##cross-references GB:K02059; NID:g190322; PIDN:AAA60164.1; !1PID:g190323 REFERENCE A23789 !$#authors Beckmann, R.J.; Schmidt, R.J.; Santerre, R.F.; Plutzky, J.; !1Crabtree, G.R.; Long, G.L. !$#journal Nucleic Acids Res. (1985) 13:5233-5247 !$#title The structure and evolution of a 461 amino acid human !1protein C precursor and its messenger RNA, based upon the !1DNA sequence of cloned human liver cDNAs. !$#cross-references MUID:85269639; PMID:2991859 !$#accession A23789 !'##molecule_type mRNA !'##residues 1-461 ##label BEC !'##cross-references GB:X02750; NID:g35689; PIDN:CAA26528.1; PID:g763120 REFERENCE A44605 !$#authors Miletich, J.P.; Broze Jr., G.J. !$#journal J. Biol. Chem. (1990) 265:11397-11404 !$#title Beta protein C is not glycosylated at asparagine 329. The !1rate of translation may influence the frequency of usage at !1asparagine-X-cysteine sites. !$#cross-references MUID:90293094; PMID:1694179 !$#contents annotation; carbohydrate binding sites; activation peptide !$#note the alpha form of protein C is glycosylated at Asn-329, and !1the beta form is not REFERENCE A44606 !$#authors Harris, R.J.; Ling, V.T.; Spellman, M.W. !$#journal J. Biol. Chem. (1992) 267:5102-5107 !$#title O-linked fucose is present in the first epidermal growth !1factor domain of factor XII but not protein C. !$#cross-references MUID:92184750; PMID:1544894 !$#contents annotation; beta-hydroxyaspartic acid COMMENT Protein C is the zymogen of the vitamin K-dependent serine !1proteinase that inactivates coagulation factors Va and VIIIa !1in the presence of calcium ions and phospholipid membrane; !1the inactivation of factor Va is strongly enhanced by !1complexing with protein S. Protein C also facilitates !1fibrinolysis by neutralizing an inhibitor of plasminogen !1activator. COMMENT Protein C is synthesized in the liver as a single chain !1precursor, which is cleaved into a light chain and a heavy !1chain held together by a disulfide bond. The enzyme is !1activated by thrombin, which cleaves a dodecapeptide from !1the amino end of the heavy chain; this reaction, which !1occurs at the surface of endothelial cells, is strongly !1promoted by thrombomodulin. GENETICS !$#gene GDB:PROC !'##cross-references GDB:120317; OMIM:176860 !$#map_position 2q13-2q21 !$#introns 24/1; 79/3; 88/1; 134/1; 179/1; 226/3; 266/1 CLASSIFICATION #superfamily coagulation factor X; EGF homology; Gla domain !1homology; trypsin homology KEYWORDS anticoagulant; beta-hydroxyaspartic acid; blood coagulation; !1calcium binding; carboxyglutamic acid; glycoprotein; !1hydrolase; liver; plasma; serine proteinase; vitamin K FEATURE !$1-32 #domain signal sequence #status predicted #label SIG\ !$27-86 #domain Gla domain homology #label GLA\ !$33-42 #domain propeptide #status predicted #label PRO\ !$43-197 #product protein C light chain #status predicted !8#label LCH\ !$92-131 #domain EGF homology #label EG1\ !$140-175 #domain EGF homology #label EG2\ !$200-461 #product protein C heavy chain #status predicted !8#label HCH\ !$200-211 #domain activation peptide #status experimental !8#label APT\ !$212-445 #domain trypsin homology #label TRY\ !$48,49,56,58,61,62, !$67,68,71 #modified_site gamma-carboxyglutamic acid (Glu) !8#status experimental\ !$59-64,92-105, !$101-120,122-131, !$140-151,147-160, !$162-175,183-319, !$238-254,373-387, !$398-426 #disulfide_bonds #status predicted\ !$106-111 #disulfide_bonds #status predicted\ !$110 #binding_site carbohydrate (Thr) (covalent) #status !8absent\ !$113 #modified_site erythro-beta-hydroxyaspartic acid !8(Asp) #status experimental\ !$139,290,355 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$211-212 #cleavage_site Arg-Leu (thrombin) #status !8experimental\ !$253,299,402 #active_site His, Asp, Ser #status predicted\ !$371 #binding_site carbohydrate (Asn) (covalent) (partial) !8#status atypical SUMMARY #length 461 #molecular-weight 52071 #checksum 3806 SEQUENCE /// ENTRY KXBO #type fragment TITLE protein C (activated) (EC 3.4.21.69) precursor - bovine (fragment) ALTERNATE_NAMES autoprothrombin IIA; plasma protein C ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Nov-1980 #sequence_revision 17-Mar-1987 #text_change 16-Jul-1999 ACCESSIONS A26250; A18385; A18386; A00928 REFERENCE A26250 !$#authors Long, G.L.; Balagaje, R.M.; MacGillivray, R.T.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:5653-5656 !$#title Cloning and sequence of liver cDNA coding for bovine protein !1C. !$#cross-references MUID:85014826; PMID:6091100 !$#accession A26250 !'##molecule_type mRNA !'##residues 1-456 ##label LON REFERENCE A18385 !$#authors Fernlund, P.; Stenflo, J. !$#journal J. Biol. Chem. (1982) 257:12170-12179 !$#title Amino acid sequence of the light chain of bovine protein C. !$#cross-references MUID:83007325; PMID:6896876 !$#accession A18385 !'##molecule_type protein !'##residues 40-194 ##label FER !'##note 82-Lys was also found REFERENCE A19316 !$#authors Drakenberg, T.; Fernlund, P.; Roepstorff, P.; Stenflo, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:1802-1806 !$#title beta-Hydroxyaspartic acid in vitamin K-dependent protein C. !$#cross-references MUID:83169769; PMID:6572939 !$#contents annotation; revision to residue 110 REFERENCE A18386 !$#authors Stenflo, J.; Fernlund, P. !$#journal J. Biol. Chem. (1982) 257:12180-12190 !$#title Amino acid sequence of the heavy chain of bovine protein C. !$#cross-references MUID:83007326; PMID:6896877 !$#accession A18386 !'##molecule_type protein !'##residues 197-454,'PV' ##label STE REFERENCE A37541 !$#authors Esmon, N.L.; DeBault, L.E.; Esmon, C.T. !$#journal J. Biol. Chem. (1983) 258:5548-5553 !$#title Proteolytic formation and properties of !1gamma-carboxyglutamic acid-domainless protein C. !$#cross-references MUID:83213513; PMID:6304092 !$#contents annotation; activation; calcium binding REFERENCE A37542 !$#authors Johnson, A.E.; Esmon, N.L.; Laue, T.M.; Esmon, C.T. !$#journal J. Biol. Chem. (1983) 258:5554-5560 !$#title Structural changes required for activation of protein C are !1induced by Ca2+ binding to a high affinity site that does !1not contain gamma-carboxyglutamic acid. !$#cross-references MUID:83213514; PMID:6406503 !$#contents annotation; activation; calcium binding COMMENT Protein C is the zymogen of the vitamin K-dependent serine !1proteinase that regulates blood coagulation by inactivating !1Factors Va and VIIIa in the presence of calcium ions and !1phospholipids. COMMENT Protein C is synthesized in the liver as a single chain !1precursor, which is cleaved into a light chain and a heavy !1chain held together by a disulfide bond. The enzyme is !1activated by thrombin, which cleaves a tetradecapeptide from !1the amino end of the heavy chain; this reaction, which !1occurs at the surface of endothelial cells, is strongly !1promoted by thrombomodulin. COMMENT Calcium binds to the gamma-carboxyglutamic acid (Gla) !1residues and, with stronger affinity, to another site, !1beyond the Gla domain. The Gla-independent binding site is !1necessary for the recognition of the thrombin-thrombomodulin !1complex. COMMENT The gamma-carboxyglutamic acid residues arise by a !1posttranslational, vitamin K-dependent, enzymatic !1carboxylation of glutamic acid residues. CLASSIFICATION #superfamily coagulation factor X; EGF homology; Gla domain !1homology; trypsin homology KEYWORDS anticoagulant; beta-hydroxyaspartic acid; blood coagulation; !1calcium binding; carboxyglutamic acid; glycoprotein; !1hydrolase; liver; plasma; serine proteinase FEATURE !$1-29 #domain signal sequence (fragment) #status predicted !8#label SIG\ !$24-83 #domain Gla domain homology #label GLA\ !$30-39 #domain propeptide #status predicted #label PRO\ !$40-194 #product protein C light chain #status experimental !8#label LCH\ !$98-128 #domain EGF homology #label EG1\ !$137-172 #domain EGF homology #label EG2\ !$197-456 #product protein C heavy chain #status experimental !8#label HCH\ !$197-210 #domain activation peptide #status experimental !8#label APT\ !$211-440 #domain trypsin homology #label TRY\ !$45,46,53,55,58,59, !$62,64,65,68,74 #modified_site gamma-carboxyglutamic acid (Glu) !8#status experimental\ !$110 #modified_site erythro-beta-hydroxyaspartic acid !8(Asp) #status experimental\ !$119-128,137-148, !$144-157,159-172, !$180-318,237-253, !$368-382,393-421 #disulfide_bonds #status predicted\ !$136,289,350 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$252,298,397 #active_site His, Asp, Ser #status predicted\ !$366 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 456 #checksum 4124 SEQUENCE /// ENTRY S18994 #type complete TITLE protein C (activated) (EC 3.4.21.69) precursor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 29-Oct-1999 ACCESSIONS S18994; S24312 REFERENCE S18994 !$#authors Okafuji, T.; Maekawa, K.; Nawa, K.; Marumoto, Y. !$#submission submitted to the EMBL Data Library, February 1992 !$#description The cDNA cloninig and mRNA expression of rat protein C. !$#accession S18994 !'##status preliminary !'##molecule_type mRNA !'##residues 1-461 ##label OKA !'##cross-references EMBL:X64336; NID:g56962; PIDN:CAA45617.1; !1PID:g56963 REFERENCE S24312 !$#authors Okafuji, T.; Maekawa, K.; Nawa, K.; Marumoto, Y. !$#journal Biochim. Biophys. Acta (1992) 1131:329-332 !$#title The cDNA cloning and mRNA expression of rat protein C. !$#cross-references MUID:92329550; PMID:1627650 !$#accession S24312 !'##status preliminary !'##molecule_type mRNA !'##residues 1-461 ##label OKA2 !'##cross-references EMBL:X64336; NID:g56962; PIDN:CAA45617.1; !1PID:g56963 CLASSIFICATION #superfamily coagulation factor X; EGF homology; Gla domain !1homology; trypsin homology KEYWORDS beta-hydroxyaspartic acid; glycoprotein; hydrolase; serine !1proteinase FEATURE !$1-32 #domain signal sequence #status predicted #label SIG\ !$27-85 #domain Gla domain homology #label GLA\ !$33-42 #domain propeptide #status predicted #label PRO\ !$43-461 #product protein C #status predicted #label PRC\ !$91-130 #domain EGF homology #label EG1\ !$139-174 #domain EGF homology #label EG2\ !$213-445 #domain trypsin homology #label TRY\ !$47,48,55,57,60,61, !$66,67,70,76 #modified_site gamma-carboxyglutamic acid (Glu) !8#status predicted\ !$112 #modified_site erythro-beta-hydroxyaspartic acid !8(Asp) #status predicted\ !$121-130,139-150, !$146-159,161-174, !$182-320,239-255, !$373-387,398-426 #disulfide_bonds #status predicted\ !$215,291,355 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$254,300,402 #active_site His, Asp, Ser #status predicted SUMMARY #length 461 #molecular-weight 51912 #checksum 4055 SEQUENCE /// ENTRY JX0210 #type complete TITLE protein C (activated) (EC 3.4.21.69) precursor - mouse ALTERNATE_NAMES vitamin K-dependent serine proteinase ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS JX0210 REFERENCE JX0210 !$#authors Tada, N.; Sato, M.; Tsujimura, A.; Iwase, R.; !1Hashimoto-Gotoh, T. !$#journal J. Biochem. (1992) 111:491-495 !$#title Isolation and characterization of a mouse protein C cDNA. !$#cross-references MUID:92316897; PMID:1618739 !$#accession JX0210 !'##molecule_type mRNA !'##residues 1-461 ##label TAD !'##cross-references GB:D10445; NID:g220385; PIDN:BAA01235.1; !1PID:g220386 !'##experimental_source liver COMMENT Protein C is the zymogen of the vitamin K-dependent serine !1proteinase that regulates blood coagulation by inactivating !1Factors Va and VIIIa in the presence of calcium ions and !1phospholipids. CLASSIFICATION #superfamily coagulation factor X; EGF homology; Gla domain !1homology; trypsin homology KEYWORDS beta-hydroxyaspartic acid; blood coagulation; calcium !1binding; carboxyglutamic acid; glycoprotein; hydrolase; !1serine proteinase; zymogen FEATURE !$1-33 #domain signal sequence #status predicted #label SIG\ !$27-85 #domain Gla domain homology #label GLA\ !$34-41 #domain propeptide #status predicted #label PRO\ !$42-196,199-461 #product protein C #status predicted #label PRC\ !$42-196 #domain light chain #status predicted #label PCL\ !$91-130 #domain EGF homology #label EG1\ !$139-174 #domain EGF homology #label EG2\ !$199-461 #domain heavy chain #status predicted #label PCH\ !$199-211 #domain activation peptide #status predicted #label !8ACT\ !$212-461 #product vitamin K-dependent serine proteinase !8#status predicted #label VIT\ !$212-445 #domain trypsin homology #label TRY\ !$47,48,55,57,60,61, !$66,67,70,76 #modified_site gamma-carboxyglutamic acid (Glu) !8#status predicted\ !$112 #modified_site erythro-beta-hydroxyaspartic acid !8(Asp) #status predicted\ !$121-130,139-150, !$146-159,161-174, !$182-319,238-254, !$373-387,398-426 #disulfide_bonds #status predicted\ !$214,290,355 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$253,299,402 #active_site His, Asp, Ser #status predicted SUMMARY #length 461 #molecular-weight 51945 #checksum 2123 SEQUENCE /// ENTRY UKHU #type complete TITLE u-plasminogen activator (EC 3.4.21.73) precursor [validated] - human ALTERNATE_NAMES cellular plasminogen activator; urokinase; urokinase-type plasminogen activator (uPA) CONTAINS urokinase-type plasminogen activator chain A; urokinase-type plasminogen activator chain A1; urokinase-type plasminogen activator chain B; urokinase-type plasminogen activator, single chain form ORGANISM #formal_name Homo sapiens #common_name man DATE 17-Dec-1982 #sequence_revision 04-Dec-1986 #text_change 15-Sep-2000 ACCESSIONS A00931; I52209; JT0102; A37561; I38102; S65783; A37562; !1A37563; A37564; A35689; A36697 REFERENCE A00931 !$#authors Riccio, A.; Grimaldi, G.; Verde, P.; Sebastio, G.; Boast, !1S.; Blasi, F. !$#journal Nucleic Acids Res. (1985) 13:2759-2771 !$#title The human urokinase-plasminogen activator gene and its !1promoter. !$#cross-references MUID:85215647; PMID:2987867 !$#accession A00931 !'##molecule_type DNA !'##residues 1-431 ##label RIC !'##cross-references GB:X02419; NID:g37601; PIDN:CAA26268.1; !1PID:g1834524 !'##note the authors translated the codon ATG for residue 214 as Ile REFERENCE I52209 !$#authors Nagamine, Y.; Pearson, D.; Grattan, M. !$#journal Biochem. Biophys. Res. Commun. (1985) 132:563-569 !$#title Exon-intron boundary sliding in the generation of two mRNAs !1coding for porcine urokinase-like plasminogen activator. !$#cross-references MUID:86050639; PMID:3933505 !$#accession I52209 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 145-161 ##label NAG1 !'##cross-references GB:K03027; NID:g340174; PIDN:AAA61257.1; !1PID:g340175 REFERENCE JT0102 !$#authors Nagai, M.; Hiramatsu, R.; Kaneda, T.; Hayasuke, N.; Arimura, !1H.; Nishida, M.; Suyama, T. !$#journal Gene (1985) 36:183-188 !$#title Molecular cloning of cDNA coding for human preprourokinase. !$#cross-references MUID:86056954; PMID:2415429 !$#accession JT0102 !'##molecule_type mRNA !'##residues 1-213,'I',215-431 ##label NAG2 !'##cross-references GB:K03226; NID:g340155; PIDN:AAC97138.1; !1PID:g340158; GB:D00244; NID:g220138; PID:g220139 REFERENCE A37561 !$#authors Verde, P.; Stoppelli, M.P.; Galeffi, P.; Di Nocera, P.; !1Blasi, F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:4727-4731 !$#title Identification and primary sequence of an unspliced human !1urokinase poly(A)+ RNA. !$#cross-references MUID:84272706; PMID:6589620 !$#accession A37561 !'##molecule_type mRNA !'##residues 66-431 ##label VER !'##cross-references GB:D00244; NID:g220138 REFERENCE I38102 !$#authors Jacobs, P.; Cravador, A.; Loriau, R.; Brockly, F.; Colau, !1B.; Chuchana, P.; van Elsen, A.; Herzog, A.; Bollen, A. !$#journal DNA (1985) 4:139-146 !$#title Molecular cloning, sequencing, and expression in Escherichia !1coli of human preprourokinase cDNA. !$#cross-references MUID:85203359; PMID:3888571 !$#accession I38102 !'##status preliminary !'##molecule_type mRNA !'##residues 1-150,'W',152-213,'I',215-385,'C',387-429,'V',431 ##label !1JAC !'##cross-references EMBL:X02760; NID:g35297; PIDN:CAA26535.1; !1PID:g35298 REFERENCE S65783 !$#authors Yoshimoto, M.; Ushiyama, Y.; Sakai, M.; Tamaki, S.; Hara, !1H.; Takahashi, K.; Sawasaki, Y.; Hanada, K. !$#journal Biochim. Biophys. Acta (1996) 1293:83-89 !$#title Characterization of single chain urokinase-type plasminogen !1activator with a novel amino-acid substitution in the !1kringle structure. !$#cross-references MUID:96186279; PMID:8652631 !$#accession S65783 !'##status preliminary !'##molecule_type mRNA !'##residues 21-140,'L',142-213,'I',215-431 ##label YOS !'##cross-references EMBL:D11143; NID:g1311467; PIDN:BAA01919.1; !1PID:g1199928 REFERENCE A37562 !$#authors Gunzler, W.A.; Steffens, G.J.; Otting, F.; Kim, S.M.A.; !1Frankus, E.; Flohe, L. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1982) 363:1155-1165 !$#title The primary structure of high molecular mass urokinase from !1human urine. !$#cross-references MUID:83055084; PMID:6754569 !$#accession A37562 !'##molecule_type protein !'##residues 21-177 ##label GUN REFERENCE A37563 !$#authors Schaller, J.; Nick, H.; Rickli, E.E.; Gillessen, D.; !1Lergier, W.; Studer, R.O. !$#journal Eur. J. Biochem. (1982) 125:251-257 !$#title Human low-molecular-weight urinary urokinase. Partial !1characterization and preliminary sequence data of the two !1polypeptide chains. !$#cross-references MUID:83003608; PMID:6749491 !$#accession A37563 !'##molecule_type protein !'##residues 156-176;179-193,'T',195,'T',197-224 ##label SCH REFERENCE A37564 !$#authors Steffens, G.J.; Gunzler, W.A.; Otting, F.; Frankus, E.; !1Flohe, L. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1982) 363:1043-1058 !$#title The complete amino acid sequence of low molecular mass !1urokinase from human urine. !$#cross-references MUID:83055099; PMID:6754572 !$#accession A37564 !'##molecule_type protein !'##residues 158-410 ##label STE REFERENCE A35689 !$#authors Kentzer, E.J.; Buko, A.; Menon, G.; Sarin, V.K. !$#journal Biochem. Biophys. Res. Commun. (1990) 171:401-406 !$#title Carbohydrate composition and presence of a fucose-protein !1linkage in recombinant human pro-urokinase. !$#cross-references MUID:90365737; PMID:2393398 !$#accession A35689 !'##molecule_type protein !'##residues 21-30,'X',32,'X',34-38,'X',40-43 ##label KEN !'##note identification of a fucose and attempt to determine its !1attachment site REFERENCE A36697 !$#authors Rabbani, S.A.; Desjardins, J.; Bell, A.W.; Banville, D.; !1Mazar, A.; Henkin, J.; Goltzman, D. !$#journal Biochem. Biophys. Res. Commun. (1990) 173:1058-1064 !$#title An amino-terminal fragment of urokinase isolated from a !1prostate cancer cell line (PC-3) is mitogenic for !1osteoblast-like cells. !$#cross-references MUID:91097529; PMID:2125213 !$#accession A36697 !'##molecule_type protein !'##residues 21-34 ##label RAB REFERENCE A51255 !$#authors Li, X.; Bokman, A.M.; Llinas, M.; Smith, R.A.G.; Dobson, !1C.M. !$#submission submitted to the Brookhaven Protein Data Bank, July 1993 !$#cross-references PDB:1KDU !$#contents annotation; conformation and disulfide bond assignments by !1(1)H-NMR, residues 69-153 REFERENCE A44375 !$#authors Li, X.; Smith, R.A.G.; Dobson, C.M. !$#journal Biochemistry (1992) 31:9562-9571 !$#title Sequential (1)H NMR assignments and secondary structure of !1the kringle domain from urokinase. !$#cross-references MUID:93003110; PMID:1327118 !$#contents annotation; conformation and disulfide bond assignments by !1(1)H-NMR REFERENCE A66822 !$#authors Hansen, A.P.; Petros, A.M.; Meadows, R.P.; Nettesheim, D.G.; !1Mazar, A.P.; Olejniczak, E.T.; Xu, R.X.; Pederson, T.M.; !1Henkin, J.; Fesik, S.W. !$#submission submitted to the Brookhaven Protein Data Bank, January 1994 !$#cross-references PDB:1URK !$#contents annotation; conformation and disulfide bond assignments by !1(1)H-NMR, residues 26-155 REFERENCE A66058 !$#authors Spraggon, G.S.; Phillips, C.; Nowak, U.K.; Ponting, C.P.; !1Saunders, D.; Dobson, C.M.; Stuart, D.I.; Jones, E.Y. !$#submission submitted to the Brookhaven Protein Data Bank, July 1995 !$#cross-references PDB:1LMW !$#contents annotation; X-ray crystallography, 2.5 angstroms, residues !1168-175;179-426 COMMENT This enzyme is found in urine in a high molecular mass form, !1consisting of A and B chains, and a low molecular mass form, !1consisting of A1 and B chains. COMMENT Urokinase-type plasminogen activator proteolytically !1activates plasminogen, and the inactive single-chain form is !1proteolytically activated by plasmin (see PIR:PLHU). GENETICS !$#gene GDB:PLAU !'##cross-references GDB:119497; OMIM:191840 !$#map_position 10q24-10q24 !$#introns 19/3; 29/1; 65/1; 123/2; 154/1; 227/2; 277/1; 324/1; 373/3 FUNCTION !$#description proteolytically activates plasminogen !$#pathway fibrinolysis CLASSIFICATION #superfamily urokinase-type plasminogen activator; EGF !1homology; kringle homology; trypsin homology KEYWORDS fibrinolysis; glycoprotein; heterodimer; hydrolase; kringle; !1serine proteinase; urine FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-431 #product urokinase-type plasminogen activator, single !8chain form #status predicted #label MAT\ !$21-177 #product urokinase-type plasminogen activator chain A !8#status experimental #label MPA\ !$31-62 #domain EGF homology #label EGF\ !$70-151 #domain kringle homology #label KRG\ !$156-177 #product urokinase-type plasminogen activator chain !8A1 #status experimental #label MP1\ !$179-431 #product urokinase-type plasminogen activator chain B !8#status experimental #label MPB\ !$179-419 #domain trypsin homology #label TRY\ !$31-39,33-51,53-62, !$70-151,91-133, !$122-146,168-299, !$209-225,217-288, !$313-382,345-361, !$372-400 #disulfide_bonds #status experimental\ !$38 #binding_site carbohydrate (Thr) (covalent) #status !8predicted\ !$178-179 #cleavage_site Lys-Ile (plasmin) #status !8experimental\ !$224,275,376 #active_site His, Asp, Ser #status experimental\ !$322 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 431 #molecular-weight 48525 #checksum 4866 SEQUENCE /// ENTRY UKBAY #type complete TITLE u-plasminogen activator (EC 3.4.21.73) precursor - yellow baboon ORGANISM #formal_name Papio cynocephalus, Papio hamadryas cynocephalus #common_name yellow baboon DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 18-Jun-1999 ACCESSIONS S14687; S08651 REFERENCE S14687 !$#authors Au, Y.P.T.; Wang, T.W.; Clowes, A.W. !$#journal Nucleic Acids Res. (1990) 18:3411 !$#title Nucleotide and deduced amino acid sequences of baboon !1urokinase-type plasminogen activator. !$#cross-references MUID:90287734; PMID:2113276 !$#accession S14687 !'##molecule_type mRNA !'##residues 1-433 ##label AUY !'##cross-references EMBL:X51935; NID:g38130; PIDN:CAA36200.1; !1PID:g38131 CLASSIFICATION #superfamily urokinase-type plasminogen activator; EGF !1homology; kringle homology; trypsin homology KEYWORDS glycoprotein; heterodimer; hydrolase; kringle; serine !1proteinase FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-176 #product plasminogen activator chain A #status !8predicted #label ACH\ !$30-61 #domain EGF homology #label EGF\ !$69-150 #domain kringle homology #label KRG\ !$178-433 #product plasminogen activator chain B #status !8predicted #label BCH\ !$178-421 #domain trypsin homology #label TRY\ !$167-298,208-224, !$216-287,315-384, !$347-363,374-402 #disulfide_bonds #status predicted\ !$223,274,378 #active_site His, Asp, Ser #status predicted\ !$324 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 433 #molecular-weight 48595 #checksum 2056 SEQUENCE /// ENTRY UKPG #type complete TITLE u-plasminogen activator (EC 3.4.21.73) precursor - pig ALTERNATE_NAMES uPA ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 04-Dec-1986 #sequence_revision 17-Mar-1987 #text_change 07-Aug-1998 ACCESSIONS A00932 REFERENCE A00932 !$#authors Nagamine, Y.; Pearson, D.; Altus, M.S.; Reich, E. !$#journal Nucleic Acids Res. (1984) 12:9525-9541 !$#title cDNA and gene nucleotide sequence of porcine plasminogen !1activator. !$#cross-references MUID:85087954; PMID:6096832 !$#accession A00932 !'##molecule_type DNA !'##residues 1-240,'H',242-442 ##label NAG1 !'##experimental_source kidney cell line LLC-PK1 REFERENCE A37566 !$#authors Nagamine, Y. !$#submission submitted to the Protein Sequence Database, December 1986 !$#contents annotation; correction to residue 241 GENETICS !$#introns 19/3; 31/1; 67/1; 125/2; 165/1; 238/2; 288/1; 335/1; 384/3 CLASSIFICATION #superfamily urokinase-type plasminogen activator; EGF !1homology; kringle homology; trypsin homology KEYWORDS glycoprotein; heterodimer; hydrolase; kringle; serine !1proteinase FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-188 #product urokinase-type plasminogen activator chain A !8#status predicted #label ACH\ !$33-64 #domain EGF homology #label EGF\ !$72-153 #domain kringle homology #label KRG\ !$190-442 #product urokinase-type plasminogen activator chain B !8#status predicted #label BCH\ !$190-430 #domain trypsin homology #label TRY\ !$152 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$179-310,220-236, !$228-299,324-393, !$356-372,383-411 #disulfide_bonds #status predicted\ !$235,286,387 #active_site His, Asp, Ser #status predicted SUMMARY #length 442 #molecular-weight 49116 #checksum 6339 SEQUENCE /// ENTRY JN0560 #type complete TITLE u-plasminogen activator (EC 3.4.21.73) precursor - bovine ALTERNATE_NAMES uPA ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS JN0560 REFERENCE JN0560 !$#authors Kraetzschmar, J.; Haendler, B.; Kojima, S.; Rifkin, D.B.; !1Schleuning, W.D. !$#journal Gene (1993) 125:177-183 !$#title Bovine urokinase-type plasminogen activator and its !1receptor: cloning and induction by retinoic acid. !$#cross-references MUID:93216119; PMID:8385052 !$#accession JN0560 !'##molecule_type mRNA !'##residues 1-433 ##label KRA !'##cross-references GB:L03546; NID:g163800; PIDN:AAA51419.1; !1PID:g163801 CLASSIFICATION #superfamily urokinase-type plasminogen activator; EGF !1homology; kringle homology; trypsin homology KEYWORDS glycoprotein; heterodimer; hydrolase; kringle; serine !1proteinase FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-179 #product plasminogen activator chain A #status !8predicted #label MA1\ !$21-179 #product urokinase-type plasminogen activator chain A !8#status predicted #label ACH\ !$33-64 #domain EGF homology #label EGF\ !$72-153 #domain kringle homology #label KRG\ !$181-433 #product plasminogen activator chain B #status !8predicted #label MA2\ !$181-421 #domain trypsin homology #label TRY\ !$170-301,211-227, !$219-290,315-384, !$347-363,374-402 #disulfide_bonds #status predicted\ !$226,277,378 #active_site His, Asp, Ser #status predicted SUMMARY #length 433 #molecular-weight 48730 #checksum 409 SEQUENCE /// ENTRY UKMS #type complete TITLE u-plasminogen activator (EC 3.4.21.73) precursor - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 18-Jun-1999 ACCESSIONS A29420; A24615 REFERENCE A29420 !$#authors Degen, S.J.F.; Heckel, J.L.; Reich, E.; Degen, J.L. !$#journal Biochemistry (1987) 26:8270-8279 !$#title The murine urokinase-type plasminogen activator gene. !$#cross-references MUID:88163489; PMID:2831940 !$#accession A29420 !'##molecule_type DNA !'##residues 1-433 ##label DEG !'##cross-references GB:M17922; NID:g202296; PIDN:AAA40539.1; !1PID:g202297 REFERENCE A24615 !$#authors Belin, D.; Vassalli, J.D.; Combepine, C.; Godeau, F.; !1Nagamine, Y.; Reich, E.; Kocher, H.P.; Duvoisin, R.M. !$#journal Eur. J. Biochem. (1985) 148:225-232 !$#title Cloning, nucleotide sequencing and expression of cDNAs !1encoding mouse urokinase-type plasminogen activator. !$#cross-references MUID:85179474; PMID:2985383 !$#accession A24615 !'##molecule_type mRNA !'##residues 1-433 ##label BEL !'##cross-references GB:X02389; NID:g55127; PIDN:CAA26231.1; PID:g55128 GENETICS !$#introns 19/3; 30/1; 66/1; 124/2; 155/1; 229/2; 279/1; 326/1; 375/3 CLASSIFICATION #superfamily urokinase-type plasminogen activator; EGF !1homology; kringle homology; trypsin homology KEYWORDS glycoprotein; heterodimer; hydrolase; kringle; serine !1proteinase FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-178 #product urokinase-type plasminogen activator chain A !8#status predicted #label ACH\ !$32-63 #domain EGF homology #label EGF\ !$71-152 #domain kringle homology #label KRG\ !$180-433 #product urokinase-type plasminogen activator chain B !8#status predicted #label BCH\ !$180-421 #domain trypsin homology #label TRY\ !$169-301,211-227, !$219-290,315-384, !$347-363,374-402 #disulfide_bonds #status predicted\ !$226,277,378 #active_site His, Asp, Ser #status predicted SUMMARY #length 433 #molecular-weight 48268 #checksum 7594 SEQUENCE /// ENTRY S18932 #type complete TITLE u-plasminogen activator (EC 3.4.21.73) precursor - rat ALTERNATE_NAMES plasminogen activator, urokinase-type; urinary plasminogen activator ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 18-Oct-1989 #sequence_revision 10-Feb-1995 #text_change 18-Jun-1999 ACCESSIONS S24604; I60186; I53472; S18932 REFERENCE S24604 !$#authors Rabbani, S.A. !$#submission submitted to the EMBL Data Library, April 1992 !$#accession S24604 !'##molecule_type mRNA !'##residues 1-15,'H',17-23,'G',25-331,'N',333-432 ##label RAB !'##cross-references EMBL:X65651; NID:g57456; PIDN:CAA46601.1; !1PID:g57457 !'##experimental_source tissue kidney REFERENCE I60186 !$#authors Henderson, B.R.; Tansey, W.P.; Phillips, S.M.; Ramshaw, !1I.A.; Kefford, R.F. !$#journal Cancer Res. (1992) 52:2489-2496 !$#title Transcriptional and posttranscriptional activation of !1urokinase plasminogen activator gene expression in !1metastatic tumor cells. !$#cross-references MUID:92233409; PMID:1568219 !$#accession I60186 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-432 ##label RES !'##cross-references EMBL:X63434; NID:g57465; PIDN:CAA45028.1; !1PID:g57466 !'##experimental_source strain Fischer 344; tissue mammary REFERENCE I53472 !$#authors Ragno, P.; Cassano, S.; Degen, J.; Kessler, C.; Blasi, F.; !1Rossi, G. !$#journal FEBS Lett. (1992) 306:193-198 !$#title The receptor for the plasminogen activator of urokinase type !1is up-regulated in transformed rat thyroid cells. !$#cross-references MUID:92339549; PMID:1321734 !$#accession I53472 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 31-62 ##label RE2 !'##cross-references EMBL:X66907; NID:g396200; PIDN:CAA47356.1; !1PID:g938279 GENETICS !$#gene uPA CLASSIFICATION #superfamily urokinase-type plasminogen activator; EGF !1homology; kringle homology; trypsin homology KEYWORDS glycoprotein; heterodimer; hydrolase; kringle; serine !1proteinase FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-177 #product urokinase-type plasminogen activator chain A !8#status predicted #label ACH\ !$31-62 #domain EGF homology #label EGF\ !$70-151 #domain kringle homology #label KRG\ !$179-432 #product urokinase-type plasminogen activator chain B !8#status predicted #label BCH\ !$179-420 #domain trypsin homology #label TRY\ !$168-300,210-226, !$218-289,314-383, !$346-362,373-401 #disulfide_bonds #status predicted\ !$225,276,377 #active_site His, Asp, Ser #status predicted SUMMARY #length 432 #molecular-weight 47957 #checksum 5403 SEQUENCE /// ENTRY A35005 #type complete TITLE u-plasminogen activator (EC 3.4.21.73) precursor - chicken ALTERNATE_NAMES uPA ORGANISM #formal_name Gallus gallus #common_name chicken DATE 20-Jul-1990 #sequence_revision 20-Jul-1990 #text_change 16-Jul-1999 ACCESSIONS A35005 REFERENCE A35005 !$#authors Leslie, N.D.; Kessler, C.A.; Bell, S.M.; Degen, J.L. !$#journal J. Biol. Chem. (1990) 265:1339-1344 !$#title The chicken urokinase-type plasminogen activator gene. !$#cross-references MUID:90110185; PMID:2295632 !$#accession A35005 !'##status preliminary !'##molecule_type mRNA !'##residues 1-434 ##label LES !'##cross-references GB:J05187; NID:g212858; PIDN:AAA49131.1; !1PID:g212859 CLASSIFICATION #superfamily urokinase-type plasminogen activator; EGF !1homology; kringle homology; trypsin homology KEYWORDS glycoprotein; heterodimer; hydrolase; kringle; serine !1proteinase FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-171 #product urokinase-type plasminogen activator chain A !8#status predicted #label ACH\ !$40-71 #domain EGF homology #label EGF\ !$79-158 #domain kringle homology #label KRG\ !$173-428 #product urokinase-type plasminogen activator chain B !8#status predicted #label BCH\ !$173-416 #domain trypsin homology #label TRY\ !$162-296,202-218, !$210-285,310-379, !$342-358,369-397 #disulfide_bonds #status predicted\ !$217,272,373 #active_site His, Asp, Ser #status predicted SUMMARY #length 434 #molecular-weight 49400 #checksum 1323 SEQUENCE /// ENTRY UKHUT #type complete TITLE t-plasminogen activator (EC 3.4.21.68) precursor [validated] - human ALTERNATE_NAMES t-PA; tissue plasminogen activator ORGANISM #formal_name Homo sapiens #common_name man DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 08-Dec-2000 ACCESSIONS A94004; A23529; JT0562; A93293; S02125; A91343; A93951; !1A91322; A54645; I60110; I55232; A00933; A23993; A26270; !1A60902 REFERENCE A94004 !$#authors Ny, T.; Elgh, F.; Lund, B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:5355-5359 !$#title The structure of the human tissue-type plasminogen activator !1gene: correlation of intron and exon structures to !1functional and structural domains. !$#cross-references MUID:84298137; PMID:6089198 !$#accession A94004 !'##molecule_type DNA !'##residues 1-562 ##label NYT !'##cross-references GB:L00141 !'##note the codon given for residue 93 (ACC) is inconsistent with the !1authors' translation REFERENCE A23529 !$#authors Friezner Degen, S.J.; Rajput, B.; Reich, E. !$#journal J. Biol. Chem. (1986) 261:6972-6985 !$#title The human tissue plasminogen activator gene. !$#cross-references MUID:86196143; PMID:3009482 !$#accession A23529 !'##molecule_type DNA !'##residues 1-562 ##label DEG !'##cross-references GB:K03021; NID:g339817; PIDN:AAA98809.1; !1PID:g339818 REFERENCE JT0562 !$#authors Itagaki, Y.; Yasuda, H.; Morinaga, T.; Mitsuda, S.; !1Higashio, K. !$#journal Agric. Biol. Chem. (1991) 55:1225-1232 !$#title Purification and characterization of tissue plasminogen !1activator secreted by human embryonic lung diploid !1fibroblasts, IMR-90 cells. !$#cross-references MUID:91291340; PMID:1368681 !$#accession JT0562 !'##molecule_type mRNA !'##residues 31-562 ##label ITA !'##cross-references DDBJ:D01096; NID:g220128; PIDN:BAA00881.1; !1PID:g441174 !'##experimental_source embryonic lung fibroblast IMR-90 cells !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE A93293 !$#authors Pennica, D.; Holmes, W.E.; Kohr, W.J.; Harkins, R.N.; Vehar, !1G.A.; Ward, C.A.; Bennett, W.F.; Yelverton, E.; Seeburg, !1P.H.; Heyneker, H.L.; Goeddel, D.V.; Collen, D. !$#journal Nature (1983) 301:214-221 !$#title Cloning and expression of human tissue-type plasminogen !1activator cDNA in Escherichia coli. !$#cross-references MUID:83115262; PMID:6337343 !$#accession A93293 !'##molecule_type mRNA !'##residues 1-562 ##label PEN !'##cross-references GB:L00141 !'##experimental_source melanoma cells REFERENCE S02125 !$#authors Sasaki, H.; Saito, Y.; Hayashi, M.; Otsuka, K.; Niwa, M. !$#journal Nucleic Acids Res. (1988) 16:5695 !$#title Nucleotide sequence of the tissue-type plasminogen activator !1cDNA from human fetal lung cells. !$#cross-references MUID:88262579; PMID:3133640 !$#accession S02125 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-562 ##label SAS !'##cross-references EMBL:X07393; NID:g37243; PIDN:CAA30302.1; !1PID:g37244 !'##experimental_source fetal lung cells REFERENCE A91343 !$#authors Kagitani, H.; Tagawa, M.; Hatanaka, K.; Ikari, T.; Saito, !1A.; Bando, H.; Okada, K.; Matsuo, O. !$#journal FEBS Lett. (1985) 189:145-149 !$#title Expression in Escherichia coli of finger-domain lacking !1tissue-type plasminogen activator with high fibrin affinity. !$#cross-references MUID:85285620; PMID:3896853 !$#accession A91343 !'##molecule_type mRNA !'##residues 1-38,'G',86-433,'E',435-562 ##label KAG !'##experimental_source Detroit 562 cells; ATCC 138 REFERENCE A93951 !$#authors Edlund, T.; Ny, T.; Ranby, M.; Heden, L.O.; Palm, G.; !1Holmgren, E.; Josephson, S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:349-352 !$#title Isolation of cDNA sequences coding for a part of human !1tissue plasminogen activator. !$#cross-references MUID:83169656; PMID:6572897 !$#accession A93951 !'##molecule_type mRNA !'##residues 251-358 ##label EDL !'##experimental_source melanoma cells REFERENCE A90488 !$#authors Pohl, G.; Kallstrom, M.; Bergsdorf, N.; Wallen, P.; !1Jornvall, H. !$#journal Biochemistry (1984) 23:3701-3707 !$#title Tissue plasminogen activator: peptide analyses confirm an !1indirectly derived amino acid sequnce, identify the active !1site serine residue, establish glycosylation sites, and !1localize variant differences. !$#cross-references MUID:85000468; PMID:6433976 !$#contents annotation; melanoma cells, partial sequence of residues !136-562, active and binding sites, heterogeneity REFERENCE A91322 !$#authors Pohl, G.; Kaplan, L.; Einarsson, M.; Wallen, P.; Jornvall, !1H. !$#journal FEBS Lett. (1984) 168:29-32 !$#title Differences between uterine and melanoma forms of tissue !1plasminogen activator. !$#cross-references MUID:84158956; PMID:6538514 !$#accession A91322 !'##molecule_type protein !'##residues 33-45;311-320 ##label POH !'##experimental_source uterus !'##note in the uterus, cleavage of the activation peptide may also !1occur after 38-Gln REFERENCE A37567 !$#authors van Zonneveld, A.J.; Veerman, H.; Pannekoek, H. !$#journal J. Biol. Chem. (1986) 261:14214-14218 !$#cross-references MUID:87033611; PMID:3021732 !$#contents annotation; fibrin binding site REFERENCE A37568 !$#authors Verheijen, J.H.; Caspers, M.P.M.; Chang, G.T.G.; de Munk, !1G.A.W.; Pouwels, P.H.; Enger-Valk, B.E. !$#journal EMBO J. (1986) 5:3525-3530 !$#title Involvement of finger domain and kringle 2 domain of !1tissue-type plasminogen activator in fibrin binding and !1stimulation of activity by fibrin. !$#cross-references MUID:87161761; PMID:3030730 !$#contents annotation; fibrin binding site REFERENCE A60902 !$#authors Dodd, I.; Nunn, B.; Robinson, J.H. !$#journal Thromb. Haemost. (1988) 59:523-528 !$#title Isolation, identification and pharmacokinetic properties of !1human tissue-type plasminogen activator species: possible !1localisation of a clearance recognition site. !$#cross-references MUID:89044681; PMID:3142086 !$#contents annotation; novel forms of expressed recombinant t-PA REFERENCE A54645 !$#authors Harris, T.J.R.; Patel, T.; Marston, F.A.O.; Little, S.; !1Emtage, J.S.; Opdenakker, G.; Volckaert, G.; Rombauts, W.; !1Billiau, A.; De Somer, P. !$#journal Mol. Biol. Med. (1986) 3:279-292 !$#title Cloning of cDNA coding for human tissue-type plasminogen !1activator and its expression in Escherichia coli. !$#cross-references MUID:86284200; PMID:3090401 !$#accession A54645 !'##molecule_type mRNA !'##residues 1-562 ##label HAR !'##cross-references GB:M15518; NID:g190031; PIDN:AAA60111.1; !1PID:g190032 !'##note parts of this sequence were confirmed by peptide sequencing REFERENCE I60110 !$#authors Reddy, V.B.; Garramone, A.J.; Sasak, H.; Wei, C. !$#journal DNA (1987) 6:461-472 !$#title Expression of human uterine tissue-type plasminogen !1activator in mouse cells using BPV vectors. !$#cross-references MUID:88054470; PMID:2824147 !$#accession I60110 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-562 ##label RES !'##cross-references GB:M18182; NID:g340176; PIDN:AAA36800.1; !1PID:g340177 REFERENCE I55232 !$#authors Fisher, R.; Waller, E.K.; Grossi, G.; Thompson, D.; Tizard, !1R.; Schleuning, W.D. !$#journal J. Biol. Chem. (1985) 260:11223-11230 !$#title Isolation and characterization of the human tissue-type !1plasminogen activator structural gene including its 5' !1flanking region. !$#cross-references MUID:85289338; PMID:3161893 !$#accession I55232 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-36 ##label RE2 !'##cross-references GB:M11890; NID:g339837; PIDN:AAA61213.1; !1PID:g339839 COMMENT Cleavage by plasmin or trypsin produces two chains held !1together by a single disulfide bond. COMMENT t-PA converts plasminogen to plasmin by hydrolyzing a single !1Arg-Val bond. It is active in tissue remodeling and !1destruction, particularly in fibrinolysis, and in cell !1migration. COMMENT t-PA binds chain A of fibrin by kringle 2 and the !1fibronectin type I repeat. GENETICS !$#gene GDB:PLAT !'##cross-references GDB:119496; OMIM:173370 !$#map_position 8p12-8p12 !$#introns 24/3; 39/1; 85/1; 122/1; 180/2; 211/1; 268/2; 297/1; 362/2; !1408/1; 455/3; 510/3 CLASSIFICATION #superfamily tissue plasminogen activator; EGF homology; !1fibronectin type I repeat homology; kringle homology; !1trypsin homology KEYWORDS fibrinolysis; glycoprotein; hydrolase; kringle; plasma; !1serine proteinase FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-32 #domain propeptide #status predicted #label PRO\ !$33-562 #product t-plasminogen activator #status experimental !8#label MAT\ !$33-310 #product t-plasminogen activator chain A #status !8experimental #label ACH\ !$41-78 #domain fibronectin type I repeat homology #label !81F1\ !$86-119 #domain EGF homology #label EGF\ !$127-208 #domain kringle homology #label KR1\ !$215-296 #domain kringle homology #label KR2\ !$311-562 #product t-plasminogen activator chain B #status !8experimental #label BCH\ !$311-556 #domain trypsin homology #label TRY\ !$41-71,69-78,86-97, !$91-108,110-119, !$127-208,148-190, !$179-203,215-296, !$236-278,267-291, !$299-430,342-358, !$350-419,444-519, !$476-492,509-537 #disulfide_bonds #status predicted\ !$152,483 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$219 #binding_site carbohydrate (Asn) (covalent) (partial) !8#status experimental\ !$310-311 #cleavage_site Arg-Ile (plasmin, trypsin) #status !8experimental\ !$357,406 #active_site His, Asp #status predicted\ !$513 #active_site Ser #status experimental SUMMARY #length 562 #molecular-weight 62916 #checksum 7542 SEQUENCE /// ENTRY A35029 #type complete TITLE t-plasminogen activator (EC 3.4.21.68) precursor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A35029; A31597 REFERENCE A35029 !$#authors Feng, P.; Ohlsson, M.; Ny, T. !$#journal J. Biol. Chem. (1990) 265:2022-2027 !$#title The structure of the TATA-less rat tissue-type plasminogen !1activator gene. Species-specific sequence divergences in the !1promoter predict differences in regulation of gene !1expression. !$#cross-references MUID:90130448; PMID:2105315 !$#accession A35029 !'##status preliminary !'##molecule_type DNA !'##residues 1-559 ##label FEN !'##cross-references GB:M31197; NID:g207429; PIDN:AAA42261.1; !1PID:g207431; GB:J05226 REFERENCE A31597 !$#authors Ny, T.; Leonardsson, G.; Hsueh, A.J.W. !$#journal DNA (1988) 7:671-677 !$#title Cloning and characterization of a cDNA for rat tissue-type !1plasminogen activator. !$#cross-references MUID:89170114; PMID:3148445 !$#accession A31597 !'##molecule_type mRNA !'##residues 1-379,'K',381-559 ##label NYT !'##cross-references GB:M23697; NID:g530159; PIDN:AAA41812.1; !1PID:g530160 CLASSIFICATION #superfamily tissue plasminogen activator; EGF homology; !1fibronectin type I repeat homology; kringle homology; !1trypsin homology KEYWORDS fibrinolysis; glycoprotein; hydrolase; kringle; serine !1proteinase FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-29 #domain propeptide #status predicted #label PRO\ !$30-559 #product t-plasminogen activator #status predicted !8#label MAT\ !$30-308 #product t-plasminogen activator chain A #status !8predicted #label ACH\ !$38-75 #domain fibronectin type I repeat homology #label !81F1\ !$83-116 #domain EGF homology #label EGF\ !$124-205 #domain kringle homology #label KR1\ !$213-294 #domain kringle homology #label KR2\ !$309-559 #product t-plasminogen activator chain B #status !8predicted #label BCH\ !$309-553 #domain trypsin homology #label TRY\ !$38-68,66-75,83-94, !$88-105,107-116, !$124-205,145-187, !$176-200,213-294, !$234-276,265-289, !$297-428,340-356, !$348-417,442-516, !$474-490,506-534 #disulfide_bonds #status predicted\ !$149,481 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$308-309 #cleavage_site Arg-Ile (plasmin, trypsin) #status !8predicted\ !$355,404,510 #active_site His, Asp, Ser #status predicted SUMMARY #length 559 #molecular-weight 62903 #checksum 8573 SEQUENCE /// ENTRY A29941 #type complete TITLE t-plasminogen activator (EC 3.4.21.68) precursor - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A29941; S48205; S48207; S48206 REFERENCE A29941 !$#authors Rickles, R.J.; Darrow, A.L.; Strickland, S. !$#journal J. Biol. Chem. (1988) 263:1563-1569 !$#title Molecular cloning of complementary DNA to mouse tissue !1plasminogen activator mRNA and its expression during F9 !1teratocarcinoma cell differentiation. !$#cross-references MUID:88087303; PMID:2826484 !$#accession A29941 !'##molecule_type mRNA !'##residues 1-559 ##label RIC !'##cross-references GB:J03520; NID:g202109; PIDN:AAA40470.1; !1PID:g202110 REFERENCE S48202 !$#authors Lijnen, H.R.; van Hoef, B.; Beelen, V.; Collen, D. !$#journal Eur. J. Biochem. (1994) 224:863-871 !$#title Characterization of the murine plasma fibrinolytic system. !$#cross-references MUID:95010076; PMID:7523120 !$#accession S48205 !'##molecule_type protein !'##residues 33-37,'X',39-40 ##label LIJ !$#accession S48207 !'##molecule_type protein !'##residues 309-316 ##label LI2 !$#accession S48206 !'##molecule_type protein !'##residues 33-37,'X',39-40 ##label LIW CLASSIFICATION #superfamily tissue plasminogen activator; EGF homology; !1fibronectin type I repeat homology; kringle homology; !1trypsin homology KEYWORDS fibrinolysis; glycoprotein; hydrolase; kringle; serine !1proteinase FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-29 #domain propeptide #status predicted #label PRO\ !$30-559 #product t-plasminogen activator #status predicted !8#label MAT\ !$30-308 #product t-plasminogen activator chain A #status !8predicted #label ACH\ !$38-75 #domain fibronectin type I repeat homology #label !81F1\ !$83-116 #domain EGF homology #label EGF\ !$124-205 #domain kringle homology #label KR1\ !$213-294 #domain kringle homology #label KR2\ !$309-559 #product t-plasminogen activator chain B #status !8predicted #label BCH\ !$309-553 #domain trypsin homology #label TRY\ !$38-68,66-75,83-94, !$88-105,107-116, !$124-205,145-187, !$176-200,213-294, !$234-276,265-289, !$297-428,340-356, !$348-417,442-516, !$474-490,506-534 #disulfide_bonds #status predicted\ !$149,481 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$308-309 #cleavage_site Arg-Ile (plasmin, trypsin) #status !8predicted\ !$355,404,510 #active_site His, Asp, Ser #status predicted SUMMARY #length 559 #molecular-weight 63110 #checksum 9461 SEQUENCE /// ENTRY A34369 #type complete TITLE t-plasminogen activator (EC 3.4.21.68) precursor - false vampire bat (Megaderma lyra) ORGANISM #formal_name Megaderma lyra DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A34369 REFERENCE A34369 !$#authors Gardell, S.J.; Duong, L.T.; Diehl, R.E.; York, J.D.; Hare, !1T.R.; Register, R.B.; Jacobs, J.W.; Dixon, R.A.F.; Friedman, !1P.A. !$#journal J. Biol. Chem. (1989) 264:17947-17952 !$#title Isolation, characterization, and cDNA cloning of a vampire !1bat salivary plasminogen activator. !$#cross-references MUID:90036867; PMID:2509450 !$#accession A34369 !'##status preliminary !'##molecule_type mRNA !'##residues 1-477 ##label GAR !'##cross-references GB:J05082; NID:g166080; PIDN:AAA31596.1; !1PID:g166081 CLASSIFICATION #superfamily tissue plasminogen activator; EGF homology; !1fibronectin type I repeat homology; kringle homology; !1trypsin homology KEYWORDS fibrinolysis; glycoprotein; hydrolase; kringle; serine !1proteinase FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-36 #domain propeptide #status predicted #label PRO\ !$37-477 #product plasminogen activator #status predicted !8#label PLA\ !$42-79 #domain fibronectin type I repeat homology #label !81FA\ !$87-120 #domain EGF homology #label EGF\ !$128-209 #domain kringle homology #label KRG\ !$226-471 #domain trypsin homology #label TRY\ !$42-72,70-79,87-98, !$92-109,111-120, !$128-209,149-191, !$180-204,214-345, !$257-273,265-334, !$359-434,391-407, !$424-452 #disulfide_bonds #status predicted\ !$272,321,428 #active_site His, Asp, Ser #status predicted SUMMARY #length 477 #molecular-weight 53732 #checksum 648 SEQUENCE /// ENTRY KFHU12 #type complete TITLE coagulation factor XIIa (EC 3.4.21.38) precursor [validated] - human ALTERNATE_NAMES Hageman factor (activated) ORGANISM #formal_name Homo sapiens #common_name man DATE 27-Nov-1985 #sequence_revision 30-Jun-1991 #text_change 08-Dec-2000 ACCESSIONS A29411; A26814; A00930; A25191; A22248; A21037 REFERENCE A29411 !$#authors Cool, D.E.; MacGillivray, R.T.A. !$#journal J. Biol. Chem. (1987) 262:13662-13673 !$#title Characterization of the human blood coagulation factor XII !1gene. Intron/exon gene organization and analysis of the !15'-flanking region. !$#cross-references MUID:88007593; PMID:2888762 !$#accession A29411 !'##molecule_type DNA !'##residues 1-615 ##label COO !'##cross-references GB:M17466; GB:J02807; NID:g180355; PIDN:AAB59490.1; !1PID:g180357 REFERENCE A26814 !$#authors Tripodi, M.; Citarella, F.; Guida, S.; Galeffi, P.; Fantoni, !1A.; Cortese, R. !$#journal Nucleic Acids Res. (1986) 14:3146 !$#title cDNA sequence coding for human coagulation factor XII !1(Hageman). !$#cross-references MUID:86176794; PMID:3754331 !$#accession A26814 !'##molecule_type mRNA !'##residues 4-615 ##label TRI !'##cross-references GB:M31315; NID:g182291; PIDN:AAA70225.1; !1PID:g182292 REFERENCE A00930 !$#authors Cool, D.E.; Edgell, C.J.S.; Louie, G.V.; Zoller, M.J.; !1Brayer, G.D.; MacGillivray, R.T.A. !$#journal J. Biol. Chem. (1985) 260:13666-13676 !$#title Characterization of human blood coagulation factor XII cDNA. !1Prediction of the primary structure of factor XII and the !1tertiary structure of beta-factor XIIa. !$#cross-references MUID:86033830; PMID:3877053 !$#accession A00930 !'##molecule_type mRNA !'##residues 14-332,'S',334-615 ##label CO2 !'##cross-references GB:M11723; NID:g180358; PIDN:AAA51986.1; !1PID:g180359 REFERENCE A25191 !$#authors Que, B.G.; Davie, E.W. !$#journal Biochemistry (1986) 25:1525-1528 !$#title Characterization of a cDNA coding for human factor XII !1(Hageman factor). !$#cross-references MUID:86216049; PMID:3011063 !$#accession A25191 !'##molecule_type mRNA !'##residues 146-378,'G',380-615 ##label QUE !'##cross-references GB:M13147; NID:g180360; PIDN:AAA70224.1; !1PID:g180361 REFERENCE A22248 !$#authors McMullen, B.A.; Fujikawa, K. !$#journal J. Biol. Chem. (1985) 260:5328-5341 !$#title Amino acid sequence of the heavy chain of human alpha-factor !1XIIa (activated Hageman factor). !$#cross-references MUID:85182674; PMID:3886654 !$#accession A22248 !'##molecule_type protein !'##residues 20-379 ##label MCM REFERENCE A21037 !$#authors Fujikawa, K.; McMullen, B.A. !$#journal J. Biol. Chem. (1983) 258:10924-10933 !$#title Amino acid sequence of human beta-factor XIIa. !$#cross-references MUID:83291041; PMID:6604055 !$#accession A21037 !'##molecule_type protein !'##residues 354-362;373-615 ##label FUJ REFERENCE A44606 !$#authors Harris, R.J.; Ling, V.T.; Spellman, M.W. !$#journal J. Biol. Chem. (1992) 267:5102-5107 !$#title O-linked fucose is present in the first epidermal growth !1factor domain of factor XII but not protein C. !$#cross-references MUID:92184750; PMID:1544894 !$#contents annotation; carbohydrate binding site GENETICS !$#gene GDB:F12 !'##cross-references GDB:119892; OMIM:234000 !$#map_position 5q34-5qter !$#introns 19/3; 39/1; 72/2; 96/1; 133/1; 177/1; 212/1; 267/2; 340/1; !1417/2; 463/1; 511/1; 560/3 COMPLEX factor XII, prekallikrein, and HMW kininogen form a complex !1bound to anionic surfaces FUNCTION !$#description factor XIIa catalyzes the proteolytic activation of !1plasminogen, plasma prekallikrein, and coagulation factors !1VII and IX; factor XII can catalyze the proteolytic !1activation of prekallikrein !$#pathway blood coagulation; fibrinolysis CLASSIFICATION #superfamily coagulation factor XII; EGF homology; !1fibronectin type I repeat homology; fibronectin type II !1repeat homology; kringle homology; trypsin homology KEYWORDS blood coagulation; fibrinolysis; glycoprotein; hydrolase; !1kringle; plasma; serine proteinase FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-372,373-615 #product coagulation factor XIIa, alpha form #status !8experimental #label A12\ !$47-88 #domain fibronectin type II repeat homology #label !8FB2\ !$98-130 #domain EGF homology #label EG1\ !$135-170 #domain fibronectin type I repeat homology #label !81F1\ !$178-209 #domain EGF homology #label EG2\ !$217-295 #domain kringle homology #label KRG\ !$298-356 #region proline-rich\ !$354-362,373-615 #product coagulation factor XIIa, beta form #status !8experimental #label B12\ !$373-609 #domain trypsin homology #label TRY\ !$98-110,104-119, !$121-130,135-163, !$161-170,178-189, !$183-198,200-209, !$217-295,238-277, !$266-290,359-486, !$397-413,405-475, !$436-439,500-569, !$532-548,559-590 #disulfide_bonds #status predicted\ !$109 #binding_site carbohydrate (Thr) (covalent) #status !8experimental\ !$249,433 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$299,305,328,329,337 #binding_site carbohydrate (Thr) (covalent) #status !8predicted\ !$308 #binding_site carbohydrate (Ser) (covalent) #status !8predicted\ !$412,461,563 #active_site His, Asp, Ser #status predicted SUMMARY #length 615 #molecular-weight 67818 #checksum 7287 SEQUENCE /// ENTRY A46688 #type complete TITLE hepatocyte growth factor activator (EC 3.4.21.-) precursor [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 21-Sep-1993 #sequence_revision 25-Aug-1995 #text_change 08-Dec-2000 ACCESSIONS A46688 REFERENCE A46688 !$#authors Miyazawa, K.; Shimomura, T.; Kitamura, A.; Kondo, J.; !1Morimoto, Y.; Kitamura, N. !$#journal J. Biol. Chem. (1993) 268:10024-10028 !$#title Molecular cloning and sequence analysis of the cDNA for a !1human serine protease reponsible for activation of !1hepatocyte growth factor. Structural similarity of the !1protease precursor to blood coagulation factor XII. !$#cross-references MUID:93252878; PMID:7683665 !$#accession A46688 !'##molecule_type mRNA !'##residues 1-655 ##label MIY !'##cross-references DDBJ:D14012; NID:g219680; PIDN:BAA03113.1; !1PID:g219681 !'##experimental_source liver (mRNA); serum (protein) !'##note sequence extracted from NCBI backbone (NCBIN:131227, !1NCBIP:131228) !'##note parts of the sequence, including the amino ends of the heavy !1and light chains, confirmed by protein sequencing GENETICS !$#gene GDB:HGFAC; HGFA; HGFAP !'##cross-references GDB:9954514 !$#map_position 4p16-4p16 FUNCTION !$#description activates hepatocyte growth factor by specific proteolytic !1cleavage !$#pathway tissue repair and regeneration CLASSIFICATION #superfamily coagulation factor XII; EGF homology; !1fibronectin type I repeat homology; fibronectin type II !1repeat homology; kringle homology; trypsin homology KEYWORDS glycoprotein; hydrolase; kringle; liver; plasma; serine !1proteinase FEATURE !$1-34 #domain signal sequence #status predicted #label SIG\ !$108-148 #domain fibronectin type II repeat homology #label !81F2\ !$164-197 #domain EGF homology #label EG1\ !$202-237 #domain fibronectin type I repeat homology #label !81F1\ !$245-278 #domain EGF homology #label EG2\ !$286-367 #domain kringle homology #label KRG\ !$373-407 #product hepatocyte growth factor activator light !8chain #status experimental #label LCH\ !$408-655 #product hepatocyte growth factor activator heavy !8chain #status experimental #label HCH\ !$408-641 #domain trypsin homology #label TRY\ !$40,48,290,468,492, !$546 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$164-175,169-186, !$188-197,202-230, !$228-237,245-256, !$250-267,269-278, !$286-367,307-349, !$338-362,394-521, !$432-448,440-510, !$535-604,567-583, !$594-622 #disulfide_bonds #status predicted\ !$447,497,598 #active_site His, Asp, Ser #status predicted SUMMARY #length 655 #molecular-weight 70681 #checksum 645 SEQUENCE /// ENTRY JC4795 #type complete TITLE plasma hyaluronan-binding protein precursor - human ALTERNATE_NAMES hepatocyte growth factor activator-like protein; PHBP CONTAINS serine proteinase (EC 3.4.21.-) ORGANISM #formal_name Homo sapiens #common_name man DATE 15-Oct-1995 #sequence_revision 16-Aug-1996 #text_change 19-Jul-2002 ACCESSIONS JC4795 REFERENCE JC4795 !$#authors Choi-Miura, N.H.; Tobe, T.; Sumiya, J.; Nakano, Y.; Sano, !1Y.; Mazda, T.; Tomita, M. !$#journal J. Biochem. (1996) 119:1157-1165 !$#title Purification and characterization of a novel !1hyaluronan-binding protein (PHBP) from human plasma: It has !1three EGF, a kringle and a serine protease domain, similar !1to hepatocyte growth factor activator. !$#cross-references MUID:96425001; PMID:8827452 !$#accession JC4795 !'##molecule_type mRNA !'##residues 1-560 ##label CHO !'##cross-references GB:S83182; NID:g1836158; PIDN:AAB46909.1; !1PID:g1836159 !'##experimental_source plasma !'##note parts of this sequence, including the amino ends of the mature !1chains, were determined by protein sequencing GENETICS !$#gene GDB:HABP2; HABP; PHBP; HGFAL !'##cross-references GDB:4573962 COMPLEX a disulfide-bonded heterodimer of chains produced from the !1same precursor; the catalytic chain is degraded to a 17K !1chain lacking the active site serine residue CLASSIFICATION #superfamily plasma hyaluronan-binding protein; EGF !1homology; kringle homology; trypsin homology KEYWORDS chondroitin sulfate proteoglycan; glycoprotein; hyaluronic !1acid; hydrolase; kringle; plasma; serine proteinase FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-313 #product plasma hyaluronan-binding protein, 50K chain !8#status predicted #label 50K\ !$77-108 #domain EGF homology #label EG1\ !$115-147 #domain EGF homology #label EG2\ !$154-187 #domain EGF homology #label EG3\ !$194-276 #domain kringle homology #label KRI\ !$314-550 #domain trypsin homology #label TRY\ !$314-516 #product plasma hyaluronan-binding protein, catalytic !8chain #status predicted #label CAT\ !$54,207 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$77-88,82-97,99-108, !$115-125,120-136, !$138-147,154-165, !$159-176,178-187, !$194-276,215-257, !$246-271,301-435, !$347-363,355-424, !$447-515,477-493, !$505-533 #disulfide_bonds #status predicted\ !$362,405,509 #active_site His, Asp, Ser #status predicted SUMMARY #length 560 #molecular-weight 62671 #checksum 4714 SEQUENCE /// ENTRY TBHU #type complete TITLE thrombin (EC 3.4.21.5) precursor [validated] - human ALTERNATE_NAMES coagulation factor II CONTAINS prothrombin ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Nov-1980 #sequence_revision 22-Jul-1994 #text_change 08-Dec-2000 ACCESSIONS A29351; A00914; B00914; A37549; A37550; I51952 REFERENCE A29351 !$#authors Degen, S.J.F.; Davie, E.W. !$#journal Biochemistry (1987) 26:6165-6177 !$#title Nucleotide sequence of the gene for human prothrombin. !$#cross-references MUID:88077877; PMID:2825773 !$#accession A29351 !'##molecule_type DNA !'##residues 1-622 ##label DEG !'##cross-references GB:M17262; GB:M33691; NID:g558069; PIDN:AAC63054.1; !1PID:g339641 REFERENCE A00914 !$#authors Degen, S.J.F.; MacGillivray, R.T.A.; Davie, E.W. !$#journal Biochemistry (1983) 22:2087-2097 !$#title Characterization of the complementary deoxyribonucleic acid !1and gene coding for human prothrombin. !$#cross-references MUID:83231469; PMID:6305407 !$#accession A00914 !'##molecule_type mRNA !'##residues 8-163,'N',165-622 ##label DE2 !'##cross-references GB:V00595; GB:J00307; NID:g37128; PIDN:CAA23842.1; !1PID:g1335344 !$#accession B00914 !'##molecule_type DNA !'##residues 188-311 ##label DE3 REFERENCE A37549 !$#authors Walz, D.A.; Hewett-Emmett, D.; Seegers, W.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1977) 74:1969-1972 !$#cross-references MUID:77193964; PMID:266717 !$#accession A37549 !'##molecule_type protein !'##residues 44-118,'N',120,'S',122-163,'I',165-175,'A',177-182,'T', !1184-193,'MV',196-308,'EE',309-314 ##label WAL REFERENCE A37550 !$#authors Butkowski, R.J.; Elion, J.; Downing, M.R.; Mann, K.G. !$#journal J. Biol. Chem. (1977) 252:4942-4957 !$#title Primary structure of human prethrombin 2 and alpha-thrombin. !$#cross-references MUID:77207112; PMID:873923 !$#accession A37550 !'##molecule_type protein !'##residues 315-334,'N',336-348,'N',350-368,'N',370-397,'N',399-413, !1'N',415-484,'N',486-493,'G',495-503,'Y',505-508,'S',510,'V', !1512-513,'D',515-528,'AL',531,'Q',533-622 ##label BUT REFERENCE A37551 !$#authors Rabiet, M.J.; Blashill, A.; Furie, B.; Furie, B.C. !$#journal J. Biol. Chem. (1986) 261:13210-13215 !$#cross-references MUID:87008532; PMID:3759958 !$#contents annotation; activation cleavages REFERENCE I51952 !$#authors MacGillivray, R.T.; Irwin, D.M.; Guinto, E.R.; Stone, J.C. !$#journal Ann. N. Y. Acad. Sci. (1986) 485:73-79 !$#title Recombinant genetic approaches to functional mapping of !1thrombin. !$#cross-references MUID:87182874; PMID:3471151 !$#accession I51952 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-2,'RI',5-100 ##label RES !'##cross-references GB:M33031; NID:g190723; PIDN:AAA60220.1; !1PID:g190724 COMMENT Thrombin, which cleaves bonds after Arg and Lys, converts !1fibrinogen to fibrin and activates factors V, VIII, XIII, !1and, in complex with thrombomodulin, protein C. COMMENT Prothrombin is activated on the surface of a phospholipid !1membrane that binds the amino end of prothrombin and factors !1Va and Xa in calcium-dependent interactions. The activation !1peptide(s) can be removed either by factor Xa or thrombin; !1the cleavage into light and heavy chains is by factor Xa. It !1is not known whether one or two smaller activation peptides, !1with additional cleavage after 314-Arg, are released in !1natural blood clotting. COMMENT The cleavage after Arg-198, observed in vitro, does not !1occur in plasma. COMMENT The gamma-carboxyglutamyl residues bind calcium ions, result !1from the carboxylation of glutamyl residues by microsomal !1vitamin K-dependent carboxylase, and are necessary for !1calcium-dependent interaction with the negatively charged !1phospholipid membrane surface. COMMENT The prothrombin precursor is synthesized in the liver. GENETICS !$#gene GDB:F2 !'##cross-references GDB:119894; OMIM:176930 !$#map_position 11p11-11q12 !$#introns 27/1; 80/3; 89/1; 106/1; 141/2; 187/1; 292/1; 335/1; 377/2; !1433/2; 491/2; 552/1; 575/3 CLASSIFICATION #superfamily thrombin; Gla domain homology; kringle !1homology; trypsin homology KEYWORDS acute phase; blood coagulation; calcium binding; !1carboxyglutamic acid; duplication; glycoprotein; hydrolase; !1kringle; liver; plasma; serine proteinase FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-43 #domain propeptide #status predicted #label PRO\ !$28-87 #domain Gla domain homology #label GLA\ !$44-622 #product prothrombin #status experimental #label MAT\ !$44-327 #domain activation peptide #status experimental !8#label APT\ !$108-186 #domain kringle homology #label KR1\ !$213-291 #domain kringle homology #label KR2\ !$328-363 #product thrombin light chain #status experimental !8#label LCH\ !$364-622 #product thrombin heavy chain #status experimental !8#label HCH\ !$364-613 #domain trypsin homology #label TRY\ !$49,50,57,59,62,63, !$68,69,72,75 #modified_site gamma-carboxyglutamic acid (Glu) !8#status experimental\ !$60-65,90-103, !$108-186,129-169, !$157-181,213-291, !$234-274,262-286 #disulfide_bonds #status predicted\ !$121,143 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$336-482,536-550, !$564-594 #disulfide_bonds #status predicted\ !$391-407 #disulfide_bonds #status experimental\ !$406,462 #active_site His, Asp #status predicted\ !$416 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$568 #active_site Ser #status experimental SUMMARY #length 622 #molecular-weight 70036 #checksum 3003 SEQUENCE /// ENTRY TBBO #type complete TITLE thrombin (EC 3.4.21.5) precursor - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 24-Apr-1984 #sequence_revision 14-Jul-1994 #text_change 18-Jun-1999 ACCESSIONS S02537; A00915; A37552; I46045; S67518 REFERENCE S02537 !$#authors Irwin, D.M.; Robertson, K.A.; MacGillivray, R.T.A. !$#journal J. Mol. Biol. (1988) 200:31-45 !$#title Structure and evolution of the bovine prothrombin gene. !$#cross-references MUID:88245190; PMID:3379642 !$#accession S02537 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-625 ##label IRW REFERENCE A00915 !$#authors MacGillivray, R.T.A.; Davie, E.W. !$#journal Biochemistry (1984) 23:1626-1634 !$#title Characterization of bovine prothrombin mRNA and its !1translation product. !$#cross-references MUID:84203525; PMID:6326805 !$#accession A00915 !'##molecule_type mRNA !'##residues 1-230,'H',232-625 ##label MAC !'##note 600-Asn was also found REFERENCE A37552 !$#authors Magnusson, S.; Sottrup-Jensen, L.; Petersen, T.E.; Claeys, !1H. !$#book Boerhaave Symposium on Prothrombin and Related Coagulation !1Factors, Hemker, H.C., and Veltkamp, J.J., eds., pp.25-46, !1Leiden Univ. Press, Leiden, 1975 !$#accession A37552 !'##molecule_type protein !'##residues 44-287,'N',289-352,'E',354,'Q',356-548,'ND',551-599,'N', !1601-625 ##label MAG !'##note the evidence for 231-Ser is strong !'##note disulfide bonds and carbohydrate binding sites were determined REFERENCE A37553 !$#authors Park, C.H.; Tulinsky, A. !$#journal Biochemistry (1986) 25:3977-3982 !$#title Three-dimensional structure of the kringle sequence: !1structure of prothrombin fragment 1. !$#cross-references MUID:86296631; PMID:3741841 !$#contents annotation; residues 44-317, X-ray crystallography, 2.8 !1angstroms REFERENCE A37554 !$#authors Irwin, D.M.; Ahern, K.G.; Pearson, G.D.; MacGillivray, !1R.T.A. !$#journal Biochemistry (1985) 24:6854-6861 !$#title Characterization of the bovine prothrombin gene. !$#cross-references MUID:86077733; PMID:3000440 !$#contents annotation; gene structure REFERENCE I46045 !$#authors MacGillivray, R.T.; Degen, S.J.; Chandra, T.; Woo, S.L.; !1Davie, E.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1980) 77:5153-5157 !$#title Cloning and analysis of a cDNA coding for bovine !1prothrombin. !$#cross-references MUID:81054926; PMID:6254059 !$#accession I46045 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 466-599,'N',601-625 ##label MA2 !'##cross-references EMBL:V00135; NID:g772; PIDN:CAA23451.1; PID:g808945 REFERENCE S67518 !$#authors Pejler, G.; Karlstroem, A.R.; Berg, L. !$#journal Eur. J. Biochem. (1995) 227:102-107 !$#title Identification of the proteolytic thrombin fragments formed !1after cleavage with rat mast cell protease 1. !$#cross-references MUID:95154277; PMID:7851376 !$#accession S67518 !'##status preliminary !'##molecule_type protein !'##residues 318-325;333-338,'X',340;367-374;481-484,'X',486-488;515-522 !1##label PEJ COMMENT Thrombin, which cleaves bonds after Arg and Lys, converts !1fibrinogen to fibrin and activates factors V, VII, VIII, !1XIII, and, in complex with thrombomodulin, protein C. COMMENT Prothrombin is activated on the surface of a phospholipid !1membrane that binds the amino end of prothrombin and factors !1Va and Xa in calcium-dependent interactions; factor Xa !1removes the activation peptide and cleaves the remaining !1part into light and heavy chains. The activation process !1starts slowly because factor V itself has to be activated by !1the initial, small amounts of thrombin. COMMENT Thrombin can cleave the amino-terminal activation peptide 1 !1from prothrombin, prior to its activation by factor Xa. COMMENT The gamma-carboxyglutamyl residues bind calcium ions, result !1from the carboxylation of glutamyl residues by microsomal !1vitamin K-dependent carboxylase, and are necessary for !1calcium-dependent interaction with the negatively charged !1phospholipid membrane surface. COMMENT The prothrombin precursor is synthesized in the liver. CLASSIFICATION #superfamily thrombin; Gla domain homology; kringle !1homology; trypsin homology KEYWORDS blood coagulation; calcium binding; carboxyglutamic acid; !1duplication; glycoprotein; hydrolase; kringle; liver; !1plasma; serine proteinase FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-43 #domain propeptide #status predicted #label PRO\ !$28-88 #domain Gla domain homology #label GLA\ !$44-625 #product prothrombin #status experimental #label MPT\ !$44-199 #domain activation peptide 1 #status experimental !8#label FR1\ !$109-187 #domain kringle homology #label KR1\ !$200-317 #domain activation peptide 2 #status experimental !8#label FR2\ !$214-292 #domain kringle homology #label KR2\ !$318-366 #product thrombin light chain #status experimental !8#label LCH\ !$367-625 #product thrombin heavy chain #status experimental !8#label HCH\ !$367-616 #domain trypsin homology #label TRY\ !$50,51,58,60,63,64, !$69,70,73,76 #modified_site gamma-carboxyglutamic acid (Glu) !8#status experimental\ !$61-66,91-104, !$109-187,130-170, !$158-182,214-292, !$235-275,263-287, !$339-485,394-410, !$539-553,567-597 #disulfide_bonds #status experimental\ !$120,144,419 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$409,465,571 #active_site His, Asp, Ser #status experimental SUMMARY #length 625 #molecular-weight 70505 #checksum 7248 SEQUENCE /// ENTRY PLHU #type complete TITLE plasmin (EC 3.4.21.7) precursor [validated] - human ALTERNATE_NAMES plasminogen precursor [misnomer] CONTAINS angiostatin; microplasmin; plasminogen ORGANISM #formal_name Homo sapiens #common_name man DATE 24-Apr-1984 #sequence_revision 02-Dec-1994 #text_change 15-Sep-2000 ACCESSIONS A35229; I52242; A26646; I62738; I84609; S03735; A00929; !1A04627; A04625; A04626; A39940 REFERENCE A35229 !$#authors Petersen, T.E.; Martzen, M.R.; Ichinose, A.; Davie, E.W. !$#journal J. Biol. Chem. (1990) 265:6104-6111 !$#title Characterization of the gene for human plasminogen, a key !1proenzyme in the fibrinolytic system. !$#cross-references MUID:90202879; PMID:2318848 !$#accession A35229 !'##molecule_type DNA !'##residues 1-810 ##label PET !'##cross-references GB:J05286; GB:M34276; NID:g190064; PIDN:AAA60113.1; !1PID:g387026 !'##experimental_source leukocyte; lung fibroblast REFERENCE I52242 !$#authors Malgaretti, N.; Bruno, L.; Pontoglio, M.; Candiani, G.; !1Meroni, G.; Ottolenghi, S.; Taramelli, R. !$#journal Biochem. Biophys. Res. Commun. (1990) 173:1013-1018 !$#title Definition of the transcription initiation site of human !1plasminogen gene in liver and non hepatic cell lines. !$#cross-references MUID:91097523; PMID:2268308 !$#accession I52242 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-16 ##label MAL1 !'##cross-references GB:M62890; NID:g190092; PIDN:AAA36454.1; !1PID:g553613 REFERENCE A26646 !$#authors Forsgren, M.; Raden, B.; Israelsson, M.; Larsson, K.; Heden, !1L.O. !$#journal FEBS Lett. (1987) 213:254-260 !$#title Molecular cloning and characterization of a full-length cDNA !1clone for human plasminogen. !$#cross-references MUID:87162490; PMID:3030813 !$#accession A26646 !'##molecule_type mRNA !'##residues 1-471,'D',473-810 ##label FOR !'##cross-references GB:X05199; NID:g35530; PIDN:CAA28831.1; PID:g35531 !'##experimental_source liver REFERENCE I45961 !$#authors Malinowski, D.P.; Sadler, J.E.; Davie, E.W. !$#journal Biochemistry (1984) 23:4243-4250 !$#title Characterization of a complementary deoxyribonucleic acid !1coding for human and bovine plasminogen. !$#cross-references MUID:85023311; PMID:6148961 !$#accession I62738 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 292-471,'D',473-810 ##label MAL2 !'##cross-references GB:K02922; NID:g190112; PIDN:AAA60124.1; !1PID:g387031 !$#accession I84609 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 367-419 ##label MAL3 !'##cross-references GB:K02921; NID:g190110; PIDN:AAA60123.1; !1PID:g190111 REFERENCE S03735 !$#authors Brunisholz, R.A.; Lerch, P.G.; Schaller, J.; Rickli, E.E.; !1Lergier, W.; Manneberg, M.; Gillessen, D. !$#journal Eur. J. Biochem. (1981) 114:465-470 !$#title Comparison of the primary structure of the N-terminal CNBr !1fragments of human, bovine and porcine plasminogen. !$#cross-references MUID:81212097; PMID:7238497 !$#accession S03735 !'##molecule_type protein !'##residues 20-71,'E',73-76 ##label BRU REFERENCE A00929 !$#authors Sottrup-Jensen, L.; Petersen, T.E.; Magnusson, S. !$#submission submitted to the Atlas, July 1977 !$#accession A00929 !'##molecule_type protein !'##residues 20-71,'E',73-85,87-106,'D',108-360,'E',362-810 ##label SOT REFERENCE A04627 !$#authors Wiman, B. !$#journal Eur. J. Biochem. (1977) 76:129-137 !$#title Primary structure of the B-chain of human plasmin. !$#cross-references MUID:77225245; PMID:142009 !$#accession A04627 !'##molecule_type protein !'##residues 581-810 ##label WI1 REFERENCE A04625 !$#authors Wiman, B.; Wallen, P. !$#journal Eur. J. Biochem. (1975) 50:489-494 !$#title Structural relationship between "glutamic acid" and "lysine" !1forms of human plasminogen and their interaction with the !1NH-2-terminal activation peptide as studied by affinity !1chromatography. !$#cross-references MUID:75093329; PMID:122932 !$#accession A04625 !'##molecule_type protein !'##residues 20-50,'Q',51-71,'E',73-85,87-100 ##label WI2 REFERENCE A04626 !$#authors Wiman, B.; Wallen, P. !$#journal Eur. J. Biochem. (1975) 58:539-547 !$#title Amino-acid sequence of the cyanogen-bromide fragment from !1human plasminogen that forms the linkage between the plasmin !1chains. !$#cross-references MUID:76043692; PMID:126863 !$#accession A04626 !'##molecule_type protein !'##residues 483-507,'E',509-604 ##label WI3 REFERENCE A92125 !$#authors Robbins, K.C.; Bernabe, P.; Arzadon, L.; Summaria, L. !$#journal J. Biol. Chem. (1973) 248:1631-1633 !$#title The primary structure of human plasminogen. II. The !1histidine loop of human plasmin: light (B) chain active !1center histidine sequence. !$#cross-references MUID:73149248; PMID:4694729 !$#contents annotation; active site REFERENCE A92048 !$#authors Groskopf, W.R.; Summaria, L.; Robbins, K.C. !$#journal J. Biol. Chem. (1969) 244:3590-3597 !$#title Studies on the active center of human plasmin. Partial amino !1acid sequence of a peptide containing the active center !1serine residue. !$#cross-references MUID:69234739; PMID:4240117 !$#contents annotation; active site REFERENCE A92382 !$#authors Trexler, M.; Vali, Z.; Patthy, L. !$#journal J. Biol. Chem. (1982) 257:7401-7406 !$#title Structure of the omega-aminocarboxylic acid-binding sites of !1human plasminogen. Arginine 70 and aspartic acid 56 are !1essential for binding of ligand by kringle 4. !$#cross-references MUID:82213905; PMID:6919539 !$#contents annotation; omega-aminocarboxylic acid binding sites REFERENCE A92458 !$#authors Vali, Z.; Patthy, L. !$#journal J. Biol. Chem. (1984) 259:13690-13694 !$#title The fibrin-binding site of human plasminogen. Arginines 32 !1and 34 are essential for fibrin affinity of the kringle 1 !1domain. !$#cross-references MUID:85054794; PMID:6094526 !$#contents annotation; fibrin binding site; omega-aminocarboxylic acid !1binding site REFERENCE A58811 !$#authors Cao, Y.; Ji, R.W.; Davidson, D.; Schaller, J.; Marti, D.; !1Soehndel, S.; McCance, S.G.; O'Reilly, M.S.; Llinas, M.; !1Folkman, J. !$#journal J. Biol. Chem. (1996) 271:29461-29467 !$#title Kringle domains of human angiostatin. Characterization of !1the anti-proliferative activity on endothelial cells. !$#cross-references MUID:97067211; PMID:8910613 !$#contents annotation REFERENCE A58812 !$#authors Lijnen, H.R.; Ugwu, F.; Bini, A.; Collen, D. !$#journal Biochemistry (1998) 37:4699-4702 !$#title Generation of an angiostatin-like fragment from plasminogen !1by stromelysin-1 (MMP-3). !$#cross-references MUID:9548733; PMID:9548733 !$#contents annotation REFERENCE A51341 !$#authors Tulinsky, A.; Mulichak, A.M. !$#submission submitted to the Brookhaven Protein Data Bank, July 1991 !$#cross-references PDB:1PK4 !$#contents annotation; X-ray crystallography, 1.9 angstroms, residues !1376-454 REFERENCE A51488 !$#authors Tulinsky, A.; Wu, T.P. !$#submission submitted to the Brookhaven Protein Data Bank, July 1991 !$#cross-references PDB:2PK4 !$#contents annotation; X-ray crystallography, 2.25 angstroms, residues !1375-454 REFERENCE A51911 !$#authors Wu, T.P.; Tulinsky, A. !$#submission submitted to the Brookhaven Protein Data Bank, August 1993 !$#cross-references PDB:1PKR !$#contents annotation; X-ray crystallography, 2.48 angstroms, residues !1102-181 REFERENCE A52408 !$#authors Padmanabhan, K.; Tulinsky, A. !$#submission submitted to the Brookhaven Protein Data Bank, April 1994 !$#cross-references PDB:1PMK !$#contents annotation; X-ray crystallography, 2.25 angstroms, residues !1377-454 REFERENCE A65244 !$#authors Tulinsky, A.; Mathews, I.I. !$#submission submitted to the Brookhaven Protein Data Bank, December 1995 !$#cross-references PDB:1CEA !$#contents annotation; X-ray crystallography, 2.1 angstroms, residues !1102-181 REFERENCE A65245 !$#authors Tulinsky, A.; Mathews, I.I. !$#submission submitted to the Brookhaven Protein Data Bank, December 1995 !$#cross-references PDB:1CEB !$#contents annotation; X-ray crystallography, 2.1 angstroms, residues !1102-181 REFERENCE A58819 !$#authors Mulichak, A.M.; Tulinsky, A.; Ravichandran, K.G. !$#journal Biochemistry (1991) 30:10576-10588 !$#title Crystal and molecular structure of human plasminogen kringle !14 refined at 1.9 Angstroms resolution. !$#cross-references MUID:92031502; PMID:1657148 !$#contents annotation REFERENCE A58818 !$#authors Wu, T.P.; Padmanabhan, K.; Tulinsky, A.; Mulichak, A.M. !$#journal Biochemistry (1991) 30:10589-10594 !$#title The refined structure of the epsilon-aminocaproic acid !1complex of human plasminogen kringle 4. !$#cross-references MUID:92031503; PMID:1657149 !$#contents annotation REFERENCE A39483 !$#authors de Vos, A.M.; Ultsch, M.H.; Kelley, R.F.; Padmanabhan, K.; !1Tulinsky, A.; Westbrook, M.L.; Kossiakoff, A.A. !$#journal Biochemistry (1992) 31:270-279 !$#title Crystal structure of the kringle 2 domain of tissue !1plasminogen activator at 2.4-angstrom resolution. !$#cross-references MUID:92118803; PMID:1310033 !$#contents annotation; X-ray crystallography, 2.4 angstroms REFERENCE A65980 !$#authors Stec, B.; Teeter, M.M.; Whitlow, M.; Yamano, A. !$#submission submitted to the Brookhaven Protein Data Bank, June 1995 !$#cross-references PDB:1KRN !$#contents annotation; X-ray crystallography, 1.67 angstroms, residues !1376-454 REFERENCE A65803 !$#authors Rejante, M.; Llinas, M. !$#submission submitted to the Brookhaven Protein Data Bank, August 1996 !$#cross-references PDB:1HPJ !$#contents annotation; conformation by (1)H-NMR, residues 103-181 REFERENCE A65804 !$#authors Rejante, M.; Llinas, M. !$#submission submitted to the Brookhaven Protein Data Bank, August 1996 !$#cross-references PDB:1HPK !$#contents annotation; conformation by (1)H-NMR, residues 103-181 REFERENCE S43645 !$#authors Rejante, M.R.; Llinas, M. !$#journal Eur. J. Biochem. (1994) 221:927-937 !$#title (1)H-NMR assignments and secondary structure of human !1plasminogen kringle 1. !$#cross-references MUID:94237157; PMID:8181475 !$#contents annotation; conformation by (1)H-NMR, residues 96-184 REFERENCE A58817 !$#authors Rejante, M.R.; Llinas, M. !$#journal Eur. J. Biochem. (1994) 221:939-949 !$#title Solution structure of the epsilon-aminohexanoic acid complex !1of human plasminogen kringle 1. !$#cross-references MUID:94237158; PMID:8181476 !$#contents annotation; conformation by (1)H-NMR COMMENT Plasminogen is synthesized by the kidney and is present in !1plasma and many other extracellular fluids. COMMENT Plasminogen is converted to plasmin by plasminogen !1activators (see PIR:UKHU and PIR:UKHUT). Both plasmin and !1the activator are then bound to fibrin (see PIR:FGHUA, !1PIR:FGHUB, PIR:FGHUG, and PIR:FGHUGB). COMMENT Plasmin is inactivated by alpha-2-antiplasmin (see !1PIR:ITHUA2) immediately after dissociation from the clot. In !1the presence of the inhibitor, the activation involves only !1cleavage after Arg-580, resulting in two chains connected by !1two disulfide bonds. Without the inhibitor, the activation !1also involves removal of the activation peptide. COMMENT Microplasmin is formed by autolytic cleavage of plasmin !1under artificial conditions at pH 11. COMMENT Stromelysin 1 (see PIR:KCHUS1) acts on plasminogen to !1produce angiostatin. Together with endostatin (see !1PIR:A53019), angiostatin acts to inhibit angiogenesis, and !1so may be useful in treating solid tumors. GENETICS !$#gene GDB:PLG !'##cross-references GDB:119498; OMIM:173350 !$#map_position 6q26-6q27 !$#introns 17/1; 62/2; 98/1; 136/2; 183/1; 223/2; 263/1; 317/2; 366/1; !1419/2; 480/1; 529/3; 561/1; 601/2; 626/2; 673/2; 709/1; 757/ !13 FUNCTION !$#description dissolves the fibrin of blood clots; acts as a proteolytic !1factor in a variety of processes including embryonic !1development, tissue remodeling and tumor invasion; in !1ovulation it weakens the walls of the graafian follicle; !1also activates the urokinase-type plasminogen activator !$#pathway fibrinolysis CLASSIFICATION #superfamily plasmin; kringle homology; plasminogen-related !1protein precursor homology; trypsin homology KEYWORDS angiogenesis inhibitor; blood; duplication; fibrinolysis; !1glycoprotein; hydrolase; kidney; kringle; plasma; !1polymorphism; serine proteinase; zymogen FEATURE !$1-96 #domain plasminogen-related protein precursor !8homology #label PLPH\ !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-810 #product plasminogen #status experimental #label PRO\ !$20-96 #domain activation peptide #status experimental !8#label APT\ !$79-466 #product angiostatin #status experimental #label AST\ !$97-580,581-810 #product plasmin #status experimental #label MAT\ !$97-580 #domain plasmin chain A #status experimental #label !8CHA\ !$103-181 #domain kringle homology #label KR1\ !$185-262 #domain kringle homology #label KR2\ !$275-352 #domain kringle homology #label KR3\ !$377-454 #domain kringle homology #label KR4\ !$481-560 #domain kringle homology #label KR5\ !$550-580,581-810 #product microplasmin #status experimental #label !8MMT\ !$550-580 #domain microplasmin chain A #status experimental !8#label MPA\ !$581-810 #domain chain B #status experimental #label CHB\ !$581-803 #domain trypsin homology #label TRY\ !$49-73,53-61, !$124-164,152-176, !$188-316,206-245, !$234-257,296-335, !$324-347,377-454, !$398-437,426-449, !$481-560,502-543, !$531-555,567-685, !$577-585,607-623, !$729-745 #disulfide_bonds #status experimental\ !$78-79 #cleavage_site Glu-Asn (stromelysin 1) #status !8experimental\ !$103-181,185-262, !$275-352,699-766, !$756-784 #disulfide_bonds #status predicted\ !$134,136 #binding_site fibrin (Arg) #status experimental\ !$136 #binding_site omega-aminocarboxylic acids (Arg) !8#status experimental\ !$158,172 #binding_site omega-aminocarboxylic acids (Asp, Arg) !8#status predicted\ !$308 #binding_site carbohydrate (Asn) (covalent) (partial) !8#status experimental\ !$365 #binding_site carbohydrate (Thr) (covalent) #status !8experimental\ !$432,445 #binding_site omega-aminocarboxylic acids (Asp, Arg) !8#status experimental\ !$466-467 #cleavage_site Pro-Val (stromelysin 1) #status !8experimental\ !$555-560 #disulfide_bonds #link MMT #status experimental\ !$580-581 #cleavage_site Arg-Val (plasminogen activator) !8#status experimental\ !$622,760 #active_site His, Ser #status experimental\ !$665 #active_site Asp #status predicted SUMMARY #length 810 #molecular-weight 90567 #checksum 8970 SEQUENCE /// ENTRY PLPG #type fragment TITLE plasmin (EC 3.4.21.7) precursor - pig (fragment) ALTERNATE_NAMES plasminogen CONTAINS miniplasminogen ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 07-Sep-1990 #sequence_revision 01-Nov-1996 #text_change 18-Jul-1997 ACCESSIONS S03733; S03737; A25834 REFERENCE S03733 !$#authors Schaller, J.; Marti, T.; Roesselet, S.J.; Kaempfer, U.; !1Rickli, E.E. !$#journal Fibrinolysis (1987) 1:91-102 !$#title Amino acid sequence of the heavy chain of porcine plasmin. !1Comparison of the carbohydrate attachment sites with the !1human and bovine species. !$#accession S03733 !'##molecule_type protein !'##residues 1-560 ##label SCH REFERENCE S03735 !$#authors Brunisholz, R.A.; Lerch, P.G.; Schaller, J.; Rickli, E.E.; !1Lergier, W.; Manneberg, M.; Gillessen, D. !$#journal Eur. J. Biochem. (1981) 114:465-470 !$#title Comparison of the primary structure of the N-terminal CNBr !1fragments of human, bovine and porcine plasminogen. !$#cross-references MUID:81212097; PMID:7238497 !$#accession S03737 !'##molecule_type protein !'##residues 1-57 ##label BRU REFERENCE A25834 !$#authors Marti, T.; Schaller, J.; Rickli, E.E. !$#journal Eur. J. Biochem. (1985) 149:279-285 !$#title Determination of the complete amino-acid sequence of porcine !1miniplasminogen. !$#cross-references MUID:85203907; PMID:3846533 !$#accession A25834 !'##molecule_type protein !'##residues 450-790 ##label MAR FUNCTION !$#description dissolves the fibrin of blood clots; acts as a proteolytic !1factor in a variety of processes including embryonic !1development, tissue remodeling and tumor invasion; in !1ovulation it weakens the walls of the graafian follicle; !1also activates the urokinase-type plasminogen activator !$#pathway fibrinolysis CLASSIFICATION #superfamily plasmin; kringle homology; plasminogen-related !1protein precursor homology; trypsin homology KEYWORDS fibrinolysis; glycoprotein; hydrolase; kidney; kringle; !1plasma; serine proteinase FEATURE !$1-790 #product plasminogen #status predicted #label PRO\ !$1-77 #domain plasminogen-related protein precursor !8homology (fragment) #label PLPH\ !$1-77 #domain activation peptide #status predicted #label !8APT\ !$78-560 #product plasmin chain A #status predicted #label !8ACH\ !$84-162 #domain kringle homology #label KR1\ !$166-243 #domain kringle homology #label KR2\ !$256-333 #domain kringle homology #label KR3\ !$358-435 #domain kringle homology #label KR4\ !$450-790 #product miniplasminogen #status experimental #label !8MIN\ !$461-540 #domain kringle homology #label KR5\ !$561-790 #product plasmin chain B #status experimental #label !8BCH\ !$561-783 #domain trypsin homology #label TRY\ !$30-54,34-42,84-162, !$105-145,133-157, !$166-243,169-297, !$187-226,215-238, !$256-333,277-316, !$305-328,358-435, !$379-418,407-430, !$461-540,482-523, !$511-535,547-665, !$557-565,587-603, !$679-746,709-725, !$736-764 #disulfide_bonds #status predicted\ !$602,645,740 #active_site His, Asp, Ser #status predicted SUMMARY #length 790 #checksum 3770 SEQUENCE /// ENTRY PLMS #type complete TITLE plasmin (EC 3.4.21.7) precursor - mouse CONTAINS angiostatin; plasminogen ORGANISM #formal_name Mus musculus #common_name house mouse DATE 20-Sep-1991 #sequence_revision 01-Nov-1996 #text_change 18-Jun-1999 ACCESSIONS A38514; S48202; S48203 REFERENCE A38514 !$#authors Degen, S.J.F.; Bell, S.M.; Schaefer, L.A.; Elliott, R.W. !$#journal Genomics (1990) 8:49-61 !$#title Characterization of the cDNA coding for mouse plasminogen !1and localization of the gene to mouse chromosome 17. !$#cross-references MUID:91184812; PMID:2081600 !$#accession A38514 !'##molecule_type mRNA !'##residues 1-812 ##label DEG !'##cross-references GB:J04766; NID:g200402; PIDN:AAA50168.1; !1PID:g200403 REFERENCE S48202 !$#authors Lijnen, H.R.; van Hoef, B.; Beelen, V.; Collen, D. !$#journal Eur. J. Biochem. (1994) 224:863-871 !$#title Characterization of the murine plasma fibrinolytic system. !$#cross-references MUID:95010076; PMID:7523120 !$#accession S48202 !'##molecule_type protein !'##residues 20-25 ##label LIJ !$#accession S48203 !'##molecule_type protein !'##residues 22-27 ##label LI2 COMMENT Plasminogen is synthesized by the kidney and is present in !1plasma and many other extracellular fluids. COMMENT Plasminogen is converted into plasmin by plasminogen !1activators, both plasminogen and its activator being bound !1to fibrin. Plasmin is inactivated by alpha-2-antiplasmin !1(see PIR:S47217) immediately after dissociation from the !1clot. In the presence of the inhibitor, the activation !1involves only cleavage after Arg-581, resulting in two !1chains connected by two disulfide bonds. Without the !1inhibitor, the activation involves also removal of the !1activation peptide. COMMENT Stromelysin 1 (see PIR:KCMSS1) acts on plasminogen to !1produce angiostatin. Together with endostatin (see !1PIR:A56101, PIR:B56101), angiostatin acts to inhibit !1angiogenesis, and so may be useful in treating solid tumors. FUNCTION !$#description dissolves the fibrin of blood clots; acts as a proteolytic !1factor in a variety of processes including embryonic !1development, tissue remodeling and tumor invasion; in !1ovulation it weakens the walls of the graafian follicle; !1also activates the urokinase-type plasminogen activator !$#pathway fibrinolysis CLASSIFICATION #superfamily plasmin; kringle homology; plasminogen-related !1protein precursor homology; trypsin homology KEYWORDS angiogenesis inhibitor; blood; duplication; fibrinolysis; !1glycoprotein; hydrolase; kidney; kringle; plasma; serine !1proteinase; zymogen FEATURE !$1-96 #domain plasminogen-related protein precursor !8homology #label PLPH\ !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-812 #product plasminogen #status predicted #label PRO\ !$20-96 #domain activation peptide #status predicted #label !8APT\ !$79-466 #product angiostatin #status predicted #label AST\ !$97-581,582-812 #product plasmin #status predicted #label MAT\ !$97-581 #domain chain A #status predicted #label ACH\ !$103-181 #domain kringle homology #label KR1\ !$185-262 #domain kringle homology #label KR2\ !$275-352 #domain kringle homology #label KR3\ !$377-454 #domain kringle homology #label KR4\ !$481-560 #domain kringle homology #label KR5\ !$582-812 #domain chain B #status predicted #label BCH\ !$582-805 #domain trypsin homology #label TRY\ !$49-73,53-61, !$103-181,124-164, !$152-176,185-262, !$188-316,206-245, !$234-257,275-352, !$296-335,324-347, !$377-454,398-437, !$426-449,481-560, !$502-543,531-555, !$568-687,578-586, !$609-625,701-768, !$731-747,758-786 #disulfide_bonds #status predicted\ !$78-79 #cleavage_site Glu-Asn (stromelysin 1) #status !8predicted\ !$136,308 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$466-467 #cleavage_site Thr-Val (stromelysin 1) #status !8predicted\ !$581-582 #cleavage_site Arg-Val (plasminogen activator) !8#status experimental\ !$624,667,762 #active_site His, Asp, Ser #status predicted SUMMARY #length 812 #molecular-weight 90846 #checksum 237 SEQUENCE /// ENTRY PLBO #type complete TITLE plasmin (EC 3.4.21.7) precursor - bovine ALTERNATE_NAMES plasminogen ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Sep-1987 #sequence_revision 28-Apr-1995 #text_change 18-Jun-1999 ACCESSIONS S45046; A25835; I45961; S03736 REFERENCE S45046 !$#authors Berglund, L.; Andersen, M.D.; Petersen, T.E. !$#submission submitted to the EMBL Data Library, May 1994 !$#description Cloning and characterizatin of the bovine plasminogen cDNA. !$#accession S45046 !'##molecule_type mRNA !'##residues 1-812 ##label BER !'##cross-references EMBL:X79402; NID:g494962; PIDN:CAA55939.1; !1PID:g494963 !'##experimental_source liver !'##note it is uncertain whether Met-1 or Met-8 is the initiator REFERENCE A25835 !$#authors Schaller, J.; Moser, P.W.; Dannegger-Muller, G.A.K.; !1Rosselet, S.J.; Kampfer, U.; Rickli, E.E. !$#journal Eur. J. Biochem. (1985) 149:267-278 !$#title Complete amino acid sequence of bovine plasminogen. !1Comparison with human plasminogen. !$#cross-references MUID:85203906; PMID:3846532 !$#accession A25835 !'##molecule_type protein !'##residues 27-334,'D',336-515,'H',517-554,'L',556-812 ##label SCH REFERENCE I45961 !$#authors Malinowski, D.P.; Sadler, J.E.; Davie, E.W. !$#journal Biochemistry (1984) 23:4243-4250 !$#title Characterization of a complementary deoxyribonucleic acid !1coding for human and bovine plasminogen. !$#cross-references MUID:85023311; PMID:6148961 !$#accession I45961 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 706-743,'R',745-812 ##label MAL !'##cross-references GB:K02935; NID:g163551; PIDN:AAA30714.1; !1PID:g163552 REFERENCE S03735 !$#authors Brunisholz, R.A.; Lerch, P.G.; Schaller, J.; Rickli, E.E.; !1Lergier, W.; Manneberg, M.; Gillessen, D. !$#journal Eur. J. Biochem. (1981) 114:465-470 !$#title Comparison of the primary structure of the N-terminal CNBr !1fragments of human, bovine and porcine plasminogen. !$#cross-references MUID:81212097; PMID:7238497 !$#accession S03736 !'##molecule_type protein !'##residues 27-83 ##label BRU FUNCTION !$#description dissolves the fibrin of blood clots; acts as a proteolytic !1factor in a variety of processes including embryonic !1development, tissue remodeling and tumor invasion; in !1ovulation it weakens the walls of the graafian follicle; !1also activates the urokinase-type plasminogen activator !$#pathway fibrinolysis CLASSIFICATION #superfamily plasmin; kringle homology; plasminogen-related !1protein precursor homology; trypsin homology KEYWORDS duplication; fibrinolysis; glycoprotein; hydrolase; kidney; !1kringle; plasma; serine proteinase; zymogen FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$8-103 #domain plasminogen-related protein precursor !8homology #label PLPH\ !$27-812 #product plasminogen #status experimental #label PRO\ !$27-103 #domain activation peptide #status experimental !8#label APT\ !$104-583,584-812 #product plasmin #status experimental #label MAT\ !$104-583 #domain plasmin chain A #status experimental #label !8ACH\ !$110-188 #domain kringle homology #label KR1\ !$192-269 #domain kringle homology #label KR2\ !$282-359 #domain kringle homology #label KR3\ !$384-461 #domain kringle homology #label KR4\ !$485-564 #domain kringle homology #label KR5\ !$584-812 #domain plasmin chain B #status experimental #label !8BCH\ !$584-805 #domain trypsin homology #label TRY\ !$56-80,60-68, !$110-188,131-171, !$159-183,192-269, !$195-323,213-252, !$241-264,282-359, !$303-342,331-354, !$384-461,405-444, !$433-456,485-564, !$506-547,535-559, !$570-687,580-588, !$609-625,701-768, !$731-747,758-786 #disulfide_bonds #status predicted\ !$315 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$365 #binding_site carbohydrate (Ser) (covalent) #status !8experimental\ !$624,667,762 #active_site His, Asp, Ser #status predicted SUMMARY #length 812 #molecular-weight 91215 #checksum 321 SEQUENCE /// ENTRY JH0579 #type complete TITLE hepatocyte growth factor precursor [validated] - human ALTERNATE_NAMES hepapoietin A; scatter factor ORGANISM #formal_name Homo sapiens #common_name man DATE 17-Aug-1992 #sequence_revision 17-Aug-1992 #text_change 08-Dec-2000 ACCESSIONS JH0579; JU0333; A41140; B36677; A36677; A33512; A39006; !1PH0114; A37796; S06794; I59214; S15443; I52253 REFERENCE JH0579 !$#authors Seki, T.; Hagiya, M.; Shimonishi, M.; Nakamura, T.; Shimizu, !1S. !$#journal Gene (1991) 102:213-219 !$#title Organization of the human hepatocyte growth factor-encoding !1gene. !$#cross-references MUID:91340155; PMID:1831432 !$#accession JH0579 !'##molecule_type DNA !'##residues 1-728 ##label SEK !'##cross-references DDBJ:D90318 !'##note the authors translated the codon GAA for residue 662 as Gly REFERENCE JU0333 !$#authors Seki, T.; Hagiya, M.; Shimonishi, M.; Nakamura, T.; Shimizu, !1S. !$#submission submitted to JIPID, March 1991 !$#description Organization of the human hepatocyte growth factor-encoding !1gene. !$#accession JU0333 !'##molecule_type DNA !'##residues 1-481,'RT',484-728 ##label SE2 REFERENCE A41140 !$#authors Weidner, K.M.; Arakaki, N.; Hartmann, G.; Vandekerckhove, !1J.; Weingart, S.; Rieder, H.; Fonatsch, C.; Tsubouchi, H.; !1Hishida, T.; Daikuhara, Y.; Birchmeier, W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:7001-7005 !$#title Evidence for the identity of human scatter factor and human !1hepatocyte growth factor. !$#cross-references MUID:91334393; PMID:1831266 !$#accession A41140 !'##molecule_type mRNA !'##residues 1-728 ##label WEI !'##cross-references GB:M73239; NID:g337935; PIDN:AAA64239.1; !1PID:g337936 REFERENCE A36677 !$#authors Seki, T.; Ihara, I.; Sugimura, A.; Shimonishi, M.; !1Nishizawa, T.; Asami, O.; Hagiya, M.; Nakamura, T.; Shimizu, !1S. !$#journal Biochem. Biophys. Res. Commun. (1990) 172:321-327 !$#title Isolation and expression of cDNA for different forms of !1hepatocyte growth factor from human leukocyte. !$#cross-references MUID:91025062; PMID:2145836 !$#accession B36677 !'##molecule_type mRNA !'##residues 1-728 ##label SE3 !'##cross-references GB:M60718; NID:g184031; PIDN:AAA52648.1; !1PID:g184032 !$#accession A36677 !'##molecule_type mRNA !'##residues 1-161,167-728 ##label SE4 !'##cross-references EMBL:X16323 !'##experimental_source leukocyte REFERENCE A33512 !$#authors Miyazawa, K.; Tsubouchi, H.; Naka, D.; Takahashi, K.; !1Okigaki, M.; Arakaki, N.; Nakayama, H.; Hirono, S.; !1Sakiyama, O.; Takahashi, K.; Gohda, E.; Daikuhara, Y.; !1Kitamura, N. !$#journal Biochem. Biophys. Res. Commun. (1989) 163:967-973 !$#title Molecular cloning and sequence analysis of cDNA for human !1hepatocyte growth factor. !$#cross-references MUID:89392017; PMID:2528952 !$#accession A33512 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-728 ##label MIY !'##cross-references GB:M29145; NID:g184041; PIDN:AAA52650.1; !1PID:g306846 REFERENCE A39006 !$#authors Rubin, J.S.; Chan, A.M.L.; Bottaro, D.P.; Burgess, W.H.; !1Taylor, W.G.; Cech, A.C.; Hirschfield, D.W.; Wong, J.; Miki, !1T.; Finch, P.W.; Aaronson, S.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:415-419 !$#title A broad-spectrum human lung fibroblast-derived mitogen is a !1variant of hepatocyte growth factor. !$#cross-references MUID:91110540; PMID:1824873 !$#accession A39006 !'##molecule_type mRNA !'##residues 1-161,167-728 ##label RUB !'##cross-references GB:M55379 !'##experimental_source embryonic lung REFERENCE PH0114 !$#authors Yoshiyama, Y.; Arakaki, N.; Naka, D.; Takahashi, K.; Hirono, !1S.; Kondo, J.; Nakayama, H.; Gohda, E.; Kitamura, N.; !1Tsubouchi, H.; Ishii, T.; Hishida, T.; Daikuhara, Y. !$#journal Biochem. Biophys. Res. Commun. (1991) 175:660-667 !$#title Identification of the N-terminal residue of the heavy chain !1of both native and recombinant human hepatocyte growth !1factor. !$#cross-references MUID:91207365; PMID:1826837 !$#accession PH0114 !'##molecule_type protein !'##residues 32-43;53-58 ##label YOS !'##experimental_source plasma REFERENCE A37796 !$#authors Weidner, K.M.; Behrens, J.; Vandekerckhove, J.; Birchmeier, !1W. !$#journal J. Cell Biol. (1990) 111:2097-2108 !$#title Scatter factor: molecular characteristics and effect on the !1invasiveness of epithelial cells. !$#cross-references MUID:91035621; PMID:2146276 !$#accession A37796 !'##molecule_type protein !'##residues 86-91;329-344;356-363,'XX',366-370;425-434;442-447,'X', !1449-450;543-546,'X',548-553;563-565,'X',567-574 ##label WE2 REFERENCE S06794 !$#authors Nakamura, T.; Nishizawa, T.; Hagiya, M.; Seki, T.; !1Shimonishi, M.; Sugimura, A.; Tashiro, K.; Shimizu, S. !$#journal Nature (1989) 342:440-443 !$#title Molecular cloning and expression of human hepatocyte growth !1factor. !$#cross-references MUID:90066676; PMID:2531289 !$#accession S06794 !'##molecule_type mRNA !'##residues 1-31,'HK',34-77,'N',79-292,'V',294-299,'M',301-316,'A', !1318-335,'K',337-386,'N',388-415,'N',417-504,'V',506-508,'I', !1510-557,'E',559-560,'R',562-594,'N',596-728 ##label NAK !'##cross-references EMBL:X16323; NID:g32081; PIDN:CAA34387.1; !1PID:g32082 !'##experimental_source liver !'##note the authors translated the codon CAG for residue 727 as Glu !'##note part of this sequence, including the amino end of both the !1alpha and beta chains, was confirmed by protein sequencing REFERENCE I59214 !$#authors Hartmann, G.; Naldini, L.; Weidner, K.M.; Sachs, M.; Vigna, !1E.; Comoglio, P.M.; Birchmeier, W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:11574-11578 !$#title A functional domain in the heavy chain of scatter factor/ !1hepatocyte growth factor binds the c-Met receptor and !1induces cell dissociation but not mitogenesis. !$#cross-references MUID:93087571; PMID:1280830 !$#accession I59214 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-288,'ET' ##label HAR !'##cross-references GB:L02931; NID:g184033; PIDN:AAA52649.1; !1PID:g184034 REFERENCE S15443 !$#authors Miyazawa, K.; Kitamura, A.; Naka, D.; Kitamura, N. !$#journal Eur. J. Biochem. (1991) 197:15-22 !$#title An alternatively processed mRNA generated from human !1hepatocyte growth factor gene. !$#cross-references MUID:91200041; PMID:1826653 !$#accession S15443 !'##status preliminary !'##molecule_type mRNA !'##residues 1-288,'ET' ##label MIY2 !'##cross-references EMBL:X57574; NID:g32083; PIDN:CAA40802.1; !1PID:g32084 REFERENCE I52253 !$#authors Shima, N.; Nagao, M.; Ogaki, F.; Tsuda, E.; Murakami, A.; !1Higashio, K. !$#journal Biochem. Biophys. Res. Commun. (1991) 180:1151-1158 !$#title Tumor cytotoxic factor/hepatocyte growth factor from human !1fibroblasts: cloning of its cDNA, purification and !1characterization of recombinant protein. !$#cross-references MUID:92062058; PMID:1835383 !$#accession I52253 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 161-166 ##label SHI !'##cross-references GB:S62561; NID:g237996; PIDN:AAB20169.1; !1PID:g237997 GENETICS !$#gene GDB:HGF !'##cross-references GDB:127524; OMIM:142409 !$#map_position 7q21.1-7q21.1 !$#introns 30/1; 85/2; 123/1; 161/2; 209/1; 249/2; 289/1; 347/2; 390/1; !1424/2; 469/1; 482/1; 514/2; 539/2; 586/2; 622/1; 670/3 COMPLEX disulfide-bonded heterodimer of chains derived from the same !1precursor FUNCTION !$#description stimulates mitosis of hepatocytes and other cells !$#note does not have proteinase activity CLASSIFICATION #superfamily hepatocyte growth factor; kringle homology; !1trypsin homology KEYWORDS alternative splicing; glycoprotein; growth factor; !1heterodimer; kringle; pyroglutamic acid FEATURE !$1-31 #domain signal sequence #status predicted #label SIG\ !$32-494,495-728 #product hepatocyte growth factor #status !8experimental #label MAT\ !$32-494 #domain alpha chain #status experimental #label ACH\ !$128-206 #domain kringle homology #label KR1\ !$211-288 #domain kringle homology #label KR2\ !$305-383 #domain kringle homology #label KR3\ !$391-469 #domain kringle homology #label KR4\ !$495-728 #domain beta chain #status experimental #label BCH\ !$495-716 #domain trypsin homology #label TRY\ !$32 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$294,402,566,653 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$487-604 #disulfide_bonds #status predicted SUMMARY #length 728 #molecular-weight 83133 #checksum 4163 SEQUENCE /// ENTRY A35644 #type complete TITLE hepatocyte growth factor precursor - rat ALTERNATE_NAMES hepapoietin A; scatter factor ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 28-Sep-1990 #sequence_revision 18-Nov-1992 #text_change 21-Jul-2000 ACCESSIONS A35644; S13211 REFERENCE A35644 !$#authors Tashiro, K.; Hagiya, M.; Nishizawa, T.; Seki, T.; !1Shimonishi, M.; Shimizu, S.; Nakamura, T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:3200-3204 !$#title Deduced primary structure of rat hepatocyte growth factor !1and expression of the mRNA in rat tissues. !$#cross-references MUID:90222197; PMID:2139229 !$#accession A35644 !'##status preliminary !'##molecule_type mRNA !'##residues 1-728 ##label TAS !'##cross-references GB:D90102; GB:M32987; NID:g220766; PIDN:BAA14133.1; !1PID:g220767 !'##note the authors translated the codon GAG for residue 70 as Gln, GAC !1for residue 417 as Asn, and TAT for residue 547 as Trp REFERENCE S13211 !$#authors Okajima, A.; Miyazawa, K.; Kitamura, N. !$#journal Eur. J. Biochem. (1990) 193:375-381 !$#title Primary structure of rat hepatocyte growth factor and !1induction of its mRNA during liver regeneration following !1hepatic injury. !$#cross-references MUID:91031482; PMID:2146117 !$#accession S13211 !'##status preliminary !'##molecule_type mRNA !'##residues 1-728 ##label OKA !'##cross-references EMBL:X54400; NID:g56353; PIDN:CAA38266.1; !1PID:g4539554 COMPLEX disulfide-bonded heterodimer of chains derived from the same !1precursor FUNCTION !$#description stimulates mitosis of hepatocytes and other cells !$#note does not have proteinase activity CLASSIFICATION #superfamily hepatocyte growth factor; kringle homology; !1trypsin homology KEYWORDS alternative splicing; glycoprotein; growth factor; !1heterodimer; kringle; pyroglutamic acid FEATURE !$1-32 #domain signal sequence #status predicted #label SIG\ !$56-495 #product hepatocyte growth factor #status predicted !8#label MAT\ !$56-495 #domain hepatocyte growth factor alpha chain #status !8predicted #label ACH\ !$129-207 #domain kringle homology #label KR1\ !$212-289 #domain kringle homology #label KR2\ !$306-384 #domain kringle homology #label KR3\ !$392-470 #domain kringle homology #label KR4\ !$496-728 #domain hepatocyte growth factor beta chain #status !8predicted #label BCH\ !$496-719 #domain trypsin homology #label TRY\ !$33 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status predicted\ !$295,403,569,656 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$488-607 #disulfide_bonds #status predicted SUMMARY #length 728 #molecular-weight 82905 #checksum 4630 SEQUENCE /// ENTRY A60185 #type complete TITLE hepatocyte growth factor precursor - mouse ALTERNATE_NAMES hepapoietin A; scatter factor ORGANISM #formal_name Mus musculus #common_name house mouse DATE 03-Mar-1993 #sequence_revision 26-May-1994 #text_change 16-Jun-2000 ACCESSIONS JC2117; PC2064; A60185; S43416; S45521; S17173; S10966; !1I48758; JU0231 REFERENCE JC2117 !$#authors Sasaki, M.; Nishio, M.; Sasaki, T.; Enami, J. !$#journal Biochem. Biophys. Res. Commun. (1994) 199:772-779 !$#title Identification of mouse mammary fibroblast-derived mammary !1growth factor as hepatocyte growth factor. !$#cross-references MUID:94183257; PMID:8135822 !$#accession JC2117 !'##molecule_type mRNA !'##residues 1-728 ##label SAS2 !'##cross-references GB:D10212; NID:g220435; PIDN:BAA01064.1; !1PID:g220436 !'##experimental_source fibroblast, COS-1 cell !'##note submitted to JIPID, May 1993 !$#accession PC2064 !'##molecule_type protein !'##residues 496-504 ##label SA2 REFERENCE A60185 !$#authors Rosen, E.M.; Meromsky, L.; Setter, E.; Vinter, D.W.; !1Goldberg, I.D. !$#journal Proc. Soc. Exp. Biol. Med. (1990) 195:34-43 !$#title Purified scatter factor stimulates epithelial and vascular !1endothelial cell migration (43115). !$#cross-references MUID:90377927; PMID:2144630 !$#accession A60185 !'##molecule_type protein !'##residues 'X',184-188,'KX',191-192,'X',194,'XX',197;357-364,'XX', !1367;375-377,'E',379,'E',381-383;653-666 ##label ROS REFERENCE S43416 !$#authors Liu, Y.; Michalopoulos, G.K.; Zarnegar, R. !$#journal Biochim. Biophys. Acta (1993) 1216:299-303 !$#title Molecular cloning and characterization of cDNA encoding !1mouse hepatocyte growth factor. !$#cross-references MUID:94060105; PMID:8241272 !$#accession S43416 !'##status preliminary !'##molecule_type mRNA !'##residues 1-728 ##label LIU !'##cross-references EMBL:X72307 REFERENCE S45521 !$#authors Liu, Y. !$#submission submitted to the EMBL Data Library, May 1993 !$#accession S45521 !'##status preliminary !'##molecule_type mRNA !'##residues 1-563,'H',565-728 ##label LI2 !'##cross-references EMBL:X72307 REFERENCE S17173 !$#authors Coffer, A.; Fellows, J.; Young, S.; Pappin, D.; Rahman, D. !$#journal Biochem. J. (1991) 278:35-41 !$#title Purification and characterization of biologically active !1scatter factor from ras-transformed NIH 3T3 conditioned !1medium. !$#cross-references MUID:91354223; PMID:1831975 !$#accession S17173 !'##molecule_type protein !'##residues 496-517,'T',519 ##label COF REFERENCE S10966 !$#authors Gherardi, E.; Stoker, M. !$#journal Nature (1990) 346:228 !$#title Hepatocytes and scatter factor. !$#cross-references MUID:90326152; PMID:2142751 !$#accession S10966 !'##status preliminary !'##molecule_type protein !'##residues 496-507,'X',509-512,'L',514-516,'X',518-519 ##label NAT REFERENCE I48758 !$#authors Plaschke-Schlutter, A.; Behrens, J.; Gherardi, E.; !1Birchmeier, W. !$#journal J. Biol. Chem. (1995) 270:830-836 !$#title Characterization of the scatter factor/hepatocyte growth !1factor gene promoter. Positive and negative regulatory !1elements direct gene expression to mesenchymal cells. !$#cross-references MUID:95122532; PMID:7822318 !$#accession I48758 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-30 ##label RES !'##cross-references EMBL:X81630; NID:g673451; PIDN:CAA57286.1; !1PID:g673452 COMPLEX disulfide-bonded heterodimer of chains derived from the same !1precursor FUNCTION !$#description stimulates mitosis of hepatocytes and other cells !$#note does not have proteinase activity CLASSIFICATION #superfamily hepatocyte growth factor; kringle homology; !1trypsin homology KEYWORDS alternative splicing; glycoprotein; growth factor; !1heterodimer; kringle; pyroglutamic acid FEATURE !$1-32 #domain signal sequence #status predicted #label SIG\ !$56-495,496-728 #product hepatocyte growth factor #status predicted !8#label MAT\ !$56-495 #domain hepatocyte growth factor alpha chain #status !8predicted #label ACH\ !$129-207 #domain kringle homology #label KR1\ !$212-289 #domain kringle homology #label KR2\ !$306-384 #domain kringle homology #label KR3\ !$392-470 #domain kringle homology #label KR4\ !$496-728 #domain hepatocyte growth factor beta chain #status !8predicted #label BCH\ !$496-719 #domain trypsin homology #label TRY\ !$33 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status predicted\ !$295,403,569,656 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$488-607 #disulfide_bonds #status predicted SUMMARY #length 728 #molecular-weight 82944 #checksum 4034 SEQUENCE /// ENTRY I51283 #type complete TITLE hepatocyte growth factor precursor - clawed frog ALTERNATE_NAMES hepapoietin A; scatter factor ORGANISM #formal_name Xenopus sp. #common_name clawed frog DATE 13-Sep-1996 #sequence_revision 13-Sep-1996 #text_change 18-Jun-1999 ACCESSIONS I51283 REFERENCE I51283 !$#authors Nakamura, H.; Tashiro, K.; Nakamura, T.; Shiokawa, K. !$#journal Mech. Dev. (1995) 49:123-131 !$#title Molecular cloning of Xenopus HGF cDNA and its expression !1studies in Xenopus early embryogenesis. !$#cross-references MUID:95267690; PMID:7748783 !$#accession I51283 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-710 ##label NAK !'##cross-references GB:S77422; NID:g998932; PIDN:AAB34354.1; !1PID:g998933 !'##note the authors' translation for residue 458 (Thr) is inconsistent !1with the nucleotide sequence COMPLEX disulfide-bonded heterodimer of chains derived from the same !1precursor FUNCTION !$#description stimulates mitosis of hepatocytes and other cells !$#note does not have proteinase activity CLASSIFICATION #superfamily hepatocyte growth factor; kringle homology; !1trypsin homology KEYWORDS duplication; glycoprotein; growth factor; heterodimer; !1kringle FEATURE !$42-477,478-709 #product hepatocyte growth factor #status predicted !8#label MAT\ !$42-477 #domain hepatocyte growth factor alpha chain #status !8predicted #label ACH\ !$115-193 #domain kringle homology #label KR1\ !$198-275 #domain kringle homology #label KR2\ !$289-367 #domain kringle homology #label KR3\ !$375-453 #domain kringle homology #label KR4\ !$478-709 #domain hepatocyte growth factor beta chain #status !8predicted #label BCH\ !$478-700 #domain trypsin homology #label TRY\ !$52,128,281,322,379, !$550,637,666 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$470-588 #disulfide_bonds #status predicted SUMMARY #length 710 #molecular-weight 81487 #checksum 5196 SEQUENCE /// ENTRY A47136 #type complete TITLE macrophage-stimulating protein 1 precursor - human ORGANISM #formal_name Homo sapiens #common_name man DATE 03-May-1994 #sequence_revision 14-Nov-1997 #text_change 18-Jun-1999 ACCESSIONS A40331; B40331; A47136; A61395 REFERENCE A40331 !$#authors Han, S.; Stuart, L.A.; Degen, S.J.F. !$#journal Biochemistry (1991) 30:9768-9780 !$#title Characterization of the DNF15S2 locus on human chromosome 3: !1identification of a gene coding for four kringle domains !1with homology to hepatocyte growth factor. !$#cross-references MUID:92002016; PMID:1655021 !$#accession A40331 !'##molecule_type DNA !'##residues 1-711 ##label HA1 !'##cross-references GB:M74179 !$#accession B40331 !'##molecule_type mRNA !'##residues 1-711 ##label HA2 !'##cross-references GB:M74178; NID:g183976; PIDN:AAA50165.1; !1PID:g183977 REFERENCE A47136 !$#authors Yoshimura, T.; Yuhki, N.; Wang, M.H.; Skeel, A.; Leonard, !1E.J. !$#journal J. Biol. Chem. (1993) 268:15461-15468 !$#title Cloning, sequencing, and expression of human macrophage !1stimulating protein (MSP, MST1) confirms MSP as a member of !1the family of kringle proteins and locates the MSP gene on !1chromosome 3. !$#cross-references MUID:93340141; PMID:8393443 !$#accession A47136 !'##molecule_type mRNA !'##residues 1-12,'C',14-622,'F',624-711 ##label YOS !'##cross-references GB:L11924; NID:g398037; PIDN:AAA59872.1; !1PID:g398038 !'##note authors translated the codon TTT for residue 623 as Leu; parts !1of this sequence were determined by protein sequencing REFERENCE A61395 !$#authors Skeel, A.; Yoshimura, T.; Showalter, S.D.; Tanaka, S.; !1Appella, E.; Leonard, E.J. !$#journal J. Exp. Med. (1991) 173:1227-1234 !$#title Macrophage stimulating protein: purification, partial amino !1acid sequence, and cellular activity. !$#cross-references MUID:91217635; PMID:1827141 !$#accession A61395 !'##molecule_type protein !'##residues 230-247;288-291,'E',293-295,'X',297-301,'X',303,'E',305, !1'EX',308-310;326-331,'X',333-341;484-501;530-536,'X', !1538-546,'X',548-549,'SL';574-592,'E',594-596;602-611 ##label !1SKE !'##experimental_source plasma GENETICS !$#gene GDB:MST1; D3F15S2; DNF15S2; HGFL !'##cross-references GDB:128833; OMIM:142408 !$#map_position 3p21-3p21.3 COMPLEX disulfide-bonded heterodimer of chains derived from the same !1precursor CLASSIFICATION #superfamily hepatocyte growth factor; kringle homology; !1trypsin homology KEYWORDS duplication; glycoprotein; growth factor; kringle; plasma FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-483,484-711 #product macrophage-stimulating protein 1 #status !8predicted #label MAT\ !$19-483 #domain alpha chain #status predicted #label ACH\ !$110-186 #domain kringle homology #label KR1\ !$191-268 #domain kringle homology #label KR2\ !$283-361 #domain kringle homology #label KR3\ !$370-448 #domain kringle homology #label KR4\ !$484-711 #domain beta chain #status predicted #label BCH\ !$484-704 #domain trypsin homology #label TRY\ !$56-78,60-66, !$110-186,131-169, !$157-181,191-268, !$212-251,240-263, !$283-361,304-343, !$332-355,370-448, !$391-431,419-443, !$507-523,602-667, !$632-646,657-685 #disulfide_bonds #status predicted\ !$72,296,615 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 711 #molecular-weight 80379 #checksum 5521 SEQUENCE /// ENTRY A40332 #type complete TITLE macrophage-stimulating protein 1 precursor - mouse ALTERNATE_NAMES hepatocyte growth factor-like protein ORGANISM #formal_name Mus musculus #common_name house mouse DATE 17-Jul-1992 #sequence_revision 17-Jul-1992 #text_change 18-Jun-1999 ACCESSIONS A40332; B40332 REFERENCE A40332 !$#authors Degen, S.J.F.; Stuart, L.A.; Han, S.; Jamison, C.S. !$#journal Biochemistry (1991) 30:9781-9791 !$#title Characterization of the mouse cDNA and gene coding for a !1hepatocyte growth factor-like protein: expression during !1development. !$#cross-references MUID:92002017; PMID:1832957 !$#accession A40332 !'##molecule_type DNA !'##residues 1-716 ##label DEG !'##cross-references GB:M74180; NID:g193831; PIDN:AAA50166.1; !1PID:g193832 !$#accession B40332 !'##molecule_type mRNA !'##residues 1-18,'P',20-716 ##label DEG2 !'##cross-references GB:M74181; NID:g193833; PIDN:AAA50167.1; !1PID:g193834 GENETICS !$#introns 18/1; 67/2; 105/1; 143/2; 189/1; 229/2; 269/1; 334/2; 378/1; !1412/2; 458/1; 470/1; 506/2; 532/2; 581/2; 617/1; 663/3 COMPLEX disulfide-bonded heterodimer of chains derived from the same !1precursor CLASSIFICATION #superfamily hepatocyte growth factor; kringle homology; !1trypsin homology KEYWORDS duplication; glycoprotein; growth factor; kringle FEATURE !$1-31 #domain signal sequence #status predicted #label SIG\ !$19-488,489-716 #product macrophage-stimulating protein 1 #status !8experimental #label MAT\ !$19-483 #domain alpha chain #status experimental #label ACH\ !$110-186 #domain kringle homology #label KR1\ !$191-268 #domain kringle homology #label KR2\ !$292-370 #domain kringle homology #label KR3\ !$379-457 #domain kringle homology #label KR4\ !$484-711 #domain beta chain #status experimental #label BCH\ !$489-709 #domain trypsin homology #label TRY\ !$72,173,305,620 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 716 #molecular-weight 80619 #checksum 7627 SEQUENCE /// ENTRY JC5061 #type complete TITLE macrophage-stimulating protein 1 precursor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Jan-1997 #sequence_revision 31-Jan-1997 #text_change 16-Jun-2000 ACCESSIONS JC5061 REFERENCE JC5061 !$#authors Ohshiro, K.; Iwama, A.; Matsuno, K.; Ezaki, T.; Sakamoto, !1O.; Hamaguchi, I.; Takasu, N.; Suda, T. !$#journal Biochem. Biophys. Res. Commun. (1996) 227:273-280 !$#title Molecular cloning of rat macrophage-stimulating protein and !1its involvement in the male reproductive system. !$#cross-references MUID:97011126; PMID:8858136 !$#accession JC5061 !'##molecule_type mRNA !'##residues 1-716 ##label OHS !'##cross-references EMBL:X95096; NID:g1669718; PIDN:CAA64473.1; !1PID:g1669719 COMPLEX disulfide-bonded heterodimer of chains derived from the same !1precursor CLASSIFICATION #superfamily hepatocyte growth factor; kringle homology; !1trypsin homology KEYWORDS duplication; glycoprotein; growth factor; kringle FEATURE !$1-31 #domain signal sequence #status predicted #label SIG\ !$32-488,489-716 #product macrophage-stimulating protein 1 #status !8predicted #label MAT\ !$32-488 #domain macrophage-stimulating protein 1 alpha chain !8#status predicted #label ACH\ !$110-186 #domain kringle homology #label KRI1\ !$191-268 #domain kringle homology #label KRI2\ !$292-370 #domain kringle homology #label KRI3\ !$379-457 #domain kringle homology #label KRI4\ !$489-716 #domain macrophage-stimulating protein 1 beta chain !8#status predicted #label BCH\ !$489-709 #domain trypsin homology #label TRY\ !$72,305,620 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 716 #molecular-weight 80733 #checksum 9217 SEQUENCE /// ENTRY S00657 #type complete TITLE apoprotein(a) (EC 3.4.21.-) precursor [validated] - human ALTERNATE_NAMES apolipoprotein(a); lipoprotein(a) chain apo(a) ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 08-Dec-2000 ACCESSIONS S00657; A28017; A47277; I60906; A47233; I52415; I65286 REFERENCE S00657 !$#authors McLean, J.W.; Tomlinson, J.E.; Kuang, W.J.; Eaton, D.L.; !1Chen, E.Y.; Fless, G.M.; Scanu, A.M.; Lawn, R.M. !$#journal Nature (1987) 330:132-137 !$#title cDNA sequence of human apolipoprotein(a) is homologous to !1plasminogen. !$#cross-references MUID:88039109; PMID:3670400 !$#accession S00657 !'##molecule_type mRNA !'##residues 1-4548 ##label MCL !'##cross-references GB:X06290; EMBL:X06696; NID:g28619; !1PIDN:CAA29618.1; PID:g28620 REFERENCE A28017 !$#authors Eaton, D.L.; Fless, G.M.; Kohr, W.J.; McLean, J.W.; Xu, !1Q.T.; Miller, C.G.; Lawn, R.M.; Scanu, A.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:3224-3228 !$#title Partial amino acid sequence of apolipoprotein(a) shows that !1it is homologous to plasminogen. !$#cross-references MUID:87204109; PMID:3472206 !$#accession A28017 !'##molecule_type protein !'##residues 20-21,'P',23-34;177-179,'N',181-186,'T',188-196,'DKG', !1200;292-314,'W',316-318;4201-4202,'X',4204-4207,'LL', !14210-4212,'P',4214-4218,'X',4220-4232;4323-4334, !1'LTP';4382-4386,'X',4388-4393,'PX',4396-4401 ##label EAT REFERENCE A47277 !$#authors Wade, D.P.; Clarke, J.G.; Lindahl, G.E.; Liu, A.C.; Zysow, !1B.R.; Meer, K.; Schwartz, K.; Lawn, R.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:1369-1373 !$#title 5' control regions of the apolipoprotein(a) gene and members !1of the related plasminogen gene family. !$#cross-references MUID:93165698; PMID:7679504 !$#accession A47277 !'##status preliminary; translation not shown; translated from GB/EMBL/ !1DDBJ !'##molecule_type DNA !'##residues 1-16 ##label RES !'##cross-references GB:L07899; NID:g967973; PID:g967974 REFERENCE A47233 !$#authors Malgaretti, N.; Acquati, F.; Magnaghi, P.; Bruno, L.; !1Pontoglio, M.; Rocchi, M.; Saccone, S.; Della Valle, G.; !1D'Urso, M.; LePaslier, D.; Ottolenghi, S.; Taramelli, R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:11584-11588 !$#title Characterization by yeast artificial chromosome cloning of !1the linked apolipoprotein(a) and plasminogen genes and !1identification of the apolipoprotein(a) 5' flanking region. !$#cross-references MUID:93087573; PMID:1454851 !$#accession I60906 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-16 ##label RE2 !'##cross-references GB:M90078; NID:g178786; PIDN:AAA35547.1; !1PID:g553188 !'##note apo(a) gene 1 (nomenclature of reference I52415) !$#accession A47233 !'##status preliminary; translation not shown; translated from GB/EMBL/ !1DDBJ !'##molecule_type DNA !'##residues 1-16 ##label RE5 !'##cross-references GB:M90079; NID:g178784; PIDN:AAA35546.1; !1PID:g553187 REFERENCE I52415 !$#authors Ichinose, A. !$#journal Biochemistry (1992) 31:3113-3118 !$#title Multiple members of the plasminogen-apolipoprotein(a) gene !1family associated with thrombosis. !$#cross-references MUID:92207924; PMID:1554698 !$#accession I52415 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-16 ##label RE3 !'##cross-references GB:M86877; NID:g178780; PIDN:AAB49909.1; !1PID:g553185 !'##note apo(a) gene 1 (nomenclature of reference I52415) !$#accession I65286 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-16 ##label RE4 !'##cross-references GB:M86878; NID:g178782; PIDN:AAA51749.1; !1PID:g553186 GENETICS !$#gene GDB:LPA !'##cross-references GDB:120699; OMIM:152200 !$#map_position 6q26-6q27 !$#note several genes closely linked on chromosome 6 are identical !1in the first coding exon; the products of any one expressed !1locus are highly variable in human populations because of !1variable numbers of kringle repeats CLASSIFICATION #superfamily apolipoprotein(a); kringle homology; trypsin !1homology KEYWORDS hydrolase; kringle; lipid binding; lipoprotein; serine !1proteinase FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-4548 #product apolipoprotein(a) #status experimental !8#label MAT\ !$28-105 #domain kringle homology #label KR1\ !$142-219 #domain kringle homology #label KR2\ !$256-333 #domain kringle homology #label KR3\ !$370-447 #domain kringle homology #label KR4\ !$484-561 #domain kringle homology #label KR5\ !$598-675 #domain kringle homology #label KR6\ !$712-789 #domain kringle homology #label KR7\ !$826-903 #domain kringle homology #label KR8\ !$940-1017 #domain kringle homology #label KR9\ !$1054-1131 #domain kringle homology #label KR10\ !$1168-1245 #domain kringle homology #label KR11\ !$1282-1359 #domain kringle homology #label KR12\ !$1396-1473 #domain kringle homology #label KR13\ !$1510-1587 #domain kringle homology #label KR14\ !$1624-1701 #domain kringle homology #label KR15\ !$1738-1815 #domain kringle homology #label KR16\ !$1852-1929 #domain kringle homology #label KR17\ !$1966-2043 #domain kringle homology #label KR18\ !$2080-2157 #domain kringle homology #label KR19\ !$2194-2271 #domain kringle homology #label KR20\ !$2308-2385 #domain kringle homology #label KR21\ !$2422-2499 #domain kringle homology #label KR22\ !$2536-2613 #domain kringle homology #label KR23\ !$2650-2727 #domain kringle homology #label KR24\ !$2764-2841 #domain kringle homology #label KR25\ !$2878-2955 #domain kringle homology #label KR26\ !$2992-3069 #domain kringle homology #label KR27\ !$3106-3183 #domain kringle homology #label KR28\ !$3220-3297 #domain kringle homology #label KR29\ !$3334-3411 #domain kringle homology #label KR30\ !$3448-3525 #domain kringle homology #label KR31\ !$3562-3639 #domain kringle homology #label KR32\ !$3676-3753 #domain kringle homology #label KR33\ !$3782-3859 #domain kringle homology #label KR34\ !$3896-3973 #domain kringle homology #label KR35\ !$4010-4087 #domain kringle homology #label KR36\ !$4124-4201 #domain kringle homology #label KR37\ !$4228-4307 #domain kringle homology #label KR38\ !$4328-4541 #domain trypsin homology #label TRY SUMMARY #length 4548 #molecular-weight 501316 #checksum 1998 SEQUENCE /// ENTRY C2HU #type complete TITLE complement C2 precursor [validated] - human CONTAINS classical-complement-pathway C3/C5 convertase (EC 3.4.21.43) C2a subunit; classical-complement-pathway C3/C5 convertase (EC 3.4.21.43) C2b subunit ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 23-Mar-2001 ACCESSIONS A25971; JS0281; A25290; A05289; A37539; A37540; A26506; !1B26506; I56179; I54419 REFERENCE A25971 !$#authors Wu, L.; Morley, B.J.; Campbell, R.D. !$#journal Cell (1987) 48:331-342 !$#title Cell-specific expression of the human complement protein !1factor B gene: evidence for the role of two distinct !15'-flanking elements. !$#cross-references MUID:87102880; PMID:3643061 !$#accession A25971 !'##molecule_type DNA !'##residues 694-752 ##label WUL !'##cross-references GB:M15082; NID:g187699; PIDN:AAA59624.1; !1PID:g467309 REFERENCE JS0281 !$#authors Horiuchi, T.; Macon, K.J.; Kidd, V.J.; Volanakis, J.E. !$#journal J. Immunol. (1989) 142:2105-2111 !$#title cDNA cloning and expression of human complement component !1C2. !$#cross-references MUID:89156483; PMID:2493504 !$#accession JS0281 !'##molecule_type mRNA !'##residues 1-532,'F',534-752 ##label HOR !'##cross-references GB:M26301 REFERENCE A25290 !$#authors Bentley, D.R. !$#journal Biochem. J. (1986) 239:339-345 !$#title Primary structure of human complement component C2. !$#cross-references MUID:87127920; PMID:2949737 !$#accession A25290 !'##molecule_type mRNA !'##residues 1-752 ##label BEN !'##cross-references GB:X04481; NID:g34627; PIDN:CAA28169.1; PID:g34628 REFERENCE A05289 !$#authors Bentley, D.R.; Porter, R.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:1212-1215 !$#title Isolation of cDNA clones for human complement component C2. !$#cross-references MUID:84144868; PMID:6199794 !$#accession A05289 !'##molecule_type mRNA !'##residues 588-717 ##label BE2 !'##cross-references GB:K01236 REFERENCE A37539 !$#authors Gagnon, J. !$#journal Philos. Trans. R. Soc. Lond. B Biol. Sci. (1984) 306:301-309 !$#title Structure and activation of complement components C2 and !1factor B. !$#cross-references MUID:85038851; PMID:6149575 !$#accession A37539 !'##molecule_type protein !'##residues 137-149,'AG',150-171;454-466;574-717 ##label GAG !'##note two glycosylation sites were determined REFERENCE A37540 !$#authors Parkes, C.; Gagnon, J.; Kerr, M.A. !$#journal Biochem. J. (1983) 213:201-209 !$#title The reaction of iodine and thiol-blocking reagents with !1human complement components C2 and factor B. Purification !1and N-terminal amino acid sequence of a peptide from C2a !1containing a free thiol group. !$#cross-references MUID:83308518; PMID:6555044 !$#accession A37540 !'##molecule_type protein !'##residues 244-267,'G',269 ##label PAR REFERENCE A26506 !$#authors Kerr, M.A.; Gagnon, J. !$#journal Biochem. J. (1982) 205:59-67 !$#title The purification and properties of the second component of !1guinea-pig complement. !$#cross-references MUID:83022289; PMID:6922702 !$#accession A26506 !'##molecule_type protein !'##residues 244-248,'SX',251,'XK',254-256 ##label KER !$#accession B26506 !'##molecule_type protein !'##residues 21-23,'X',25-28,'XLX',32-33,'S',35-38,'X',40,'X',42-44,'X', !146 ##label KE2 REFERENCE I56179 !$#authors Ishii, Y.; Zhu, Z.B.; Macon, K.J.; Volanakis, J.E. !$#journal J. Immunol. (1993) 151:170-174 !$#title Structure of the human C2 gene. !$#cross-references MUID:93315833; PMID:8326124 !$#accession I56179 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-532,'F',534-752 ##label RES !'##cross-references GB:L09708; NID:g179663; PIDN:AAB97607.1; !1PID:g298124 REFERENCE I54419 !$#authors Bentley, D.R.; Campbell, R.D.; Cross, S.J. !$#journal Immunogenetics (1985) 22:377-390 !$#title DNA polymorphism of the C2 locus. !$#cross-references MUID:86032058; PMID:2997031 !$#accession I54419 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 21-46 ##label RE2 !'##cross-references GB:M15549; NID:g187764; PIDN:AAA59649.1; !1PID:g187765 GENETICS !$#gene GDB:C2 !'##cross-references GDB:119731; OMIM:217000 !$#map_position 6p21.3-6p21.3 !$#introns 16/1; 86/1; 148/1; 206/1; 239/1; 283/3; 330/1; 377/1; 407/1; !1454/1; 485/3; 523/1; 578/2; 604/1; 634/3; 677/1; 693/3 COMPLEX The proenzyme forms a complex with C4a and is activated by !1cleavage into C2a, containing the active site, and C2b, !1which binds C4a. FUNCTION !$#description cleaves complement C3 and complement C5 alpha chains !$#pathway complement classical pathway CLASSIFICATION #superfamily complement C2; complement factor H repeat !1homology; trypsin homology; von Willebrand factor type A !1repeat homology KEYWORDS complement classical pathway; duplication; glycoprotein; !1hydrolase; plasma; serine proteinase FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-243 #product complement C2b subunit #status experimental !8#label C2B\ !$24-84 #domain complement factor H repeat homology #label !8FH1\ !$89-144 #domain complement factor H repeat homology #label !8FH2\ !$151-204 #domain complement factor H repeat homology #label !8FH3\ !$244-752 #product complement C2a subunit #status experimental !8#label C2A\ !$252-442 #domain von Willebrand factor type A repeat homology !8#label VFA\ !$471-739 #domain trypsin homology #status atypical #label TRY\ !$24-64,51-84,89-131, !$117-144,151-191, !$177-204,463-581, !$492-508,584-600, !$638-665,675-705 #disulfide_bonds #status predicted\ !$29,112,290,333,467, !$471 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$243-244 #cleavage_site Arg-Lys (complement subcomponent C1s) !8#status experimental\ !$507,561,679 #active_site His, Asp, Ser #status predicted\ !$621,651 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 752 #molecular-weight 83233 #checksum 767 SEQUENCE /// ENTRY C2MS #type complete TITLE classical-complement-pathway C3/C5 convertase (EC 3.4.21.43) C2 component precursor - mouse ALTERNATE_NAMES C3 convertase; C5 convertase; complement C2 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 19-May-2000 ACCESSIONS A38876; B36593; I54429 REFERENCE A38875 !$#authors Ishikawa, N.; Nonaka, M.; Wetsel, R.A.; Colten, H.R. !$#submission submitted to GenBank, January 1991 !$#accession A38876 !'##molecule_type DNA !'##residues 1-760 ##label IS2 !'##cross-references GB:M57891; GB:J05661; NID:g192436; PIDN:AAA63294.1; !1PID:g192437 REFERENCE A36593 !$#authors Ishikawa, N.; Nonaka, M.; Wetsel, R.A.; Colten, H.R. !$#journal J. Biol. Chem. (1990) 265:19040-19046 !$#title Murine complement C2 and factor B genomic and cDNA cloning !1reveals different mechanisms for multiple transcripts of C2 !1and B. !$#cross-references MUID:91035430; PMID:2229060 !$#accession B36593 !'##molecule_type mRNA !'##residues 1-760 ##label ISH !'##cross-references EMBL:M57891; NID:g192436; PIDN:AAA63294.1; !1PID:g192437 REFERENCE I54429 !$#authors Falus, A.; Wakeland, E.K.; McConnell, T.J.; Gitlin, J.; !1Whitehead, A.S.; Colten, H.R. !$#journal Immunogenetics (1987) 25:290-298 !$#title DNA polymorphism of MHC III genes in inbred and wild mouse !1strains. !$#cross-references MUID:87192938; PMID:2883115 !$#accession I54429 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 660-677,'R',679,681-723,'G',725 ##label RES !'##cross-references GB:M16271; NID:g199289; PIDN:AAA39562.1; !1PID:g199290 GENETICS !$#introns 16/1; 91/1; 153/1; 212/1; 245/3; 290/3; 337/1; 384/1; 414/1; !1461/1; 492/3; 532/1; 587/2; 613/1; 643/3; 687/1; 703/3 COMPLEX The proenzyme forms a complex with C4a and is activated by !1cleavage into C2a, containing the active site, and C2b, !1which binds C4a. FUNCTION !$#description cleaves complement C3 and complement C5 alpha chains !$#pathway complement classical pathway CLASSIFICATION #superfamily complement C2; complement factor H repeat !1homology; trypsin homology; von Willebrand factor type A !1repeat homology KEYWORDS alternative splicing; complement classical pathway; !1duplication; glycoprotein; hydrolase; plasma; serine !1proteinase FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-250 #product complement C2b fragment #status predicted !8#label C2B\ !$22-89 #domain complement factor H repeat homology #label !8FH1\ !$94-149 #domain complement factor H repeat homology #label !8FH2\ !$156-210 #domain complement factor H repeat homology #label !8FH3\ !$251-760 #product complement C2a fragment long form #status !8predicted #label C2A\ !$251-605,613-760 #product complement C2a fragment short form #status !8predicted #label C2S\ !$259-449 #domain von Willebrand factor type A repeat homology !8#label VFA\ !$478-747 #domain trypsin homology #status atypical #label TRY\ !$22-62,49-89,94-136, !$122-149,156-197, !$182-210,470-590, !$499-515,593-609, !$647-674,685-715 #disulfide_bonds #status predicted\ !$27,117,297,340,474, !$478,663 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$514,570,689 #active_site His, Asp, Ser #status predicted SUMMARY #length 760 #molecular-weight 84726 #checksum 6021 SEQUENCE /// ENTRY BBHU #type complete TITLE complement factor B precursor [validated] - human ALTERNATE_NAMES C3 convertase; C3 proactivator; glycine-rich beta-glycoprotein; heat-labile complement factor; proenzyme factor B; properdin factor B CONTAINS alternative-complement-pathway C3/C5 convertase (EC 3.4.21.47) Bb fragment ORGANISM #formal_name Homo sapiens #common_name man DATE 19-Feb-1984 #sequence_revision 05-Aug-1994 #text_change 08-Dec-2000 ACCESSIONS S34075; A44622; A00934; A19188; A19947; B19947; B25971; !1S14339; A44628; I54409; I57824; B19447 REFERENCE S34075 !$#authors Mejia, J.E.; Jahn, I.; de la Salle, H.; Hauptmann, G. !$#submission submitted to the EMBL Data Library, March 1993 !$#accession S34075 !'##molecule_type mRNA !'##residues 1-764 ##label MEJ !'##cross-references EMBL:X72875; NID:g297568; PIDN:CAA51389.1; !1PID:g297569 REFERENCE A44622 !$#authors Woods, D.E.; Markham, A.F.; Ricker, A.T.; Goldberger, G.; !1Colten, H.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:5661-5665 !$#title Isolation of cDNA clones for the human complement protein !1factor B, a class III major histocompatibility complex gene !1product. !$#cross-references MUID:83039428; PMID:6957884 !$#accession A44622 !'##molecule_type mRNA !'##residues 467-546;550-595;752-764 ##label WOO !'##cross-references GB:J00185; GB:J00186 !'##note the authors translated the codon TAC at 519 as Thr; the nucleic !1acid translation differs from the sequence shown in having !1537-Thr, and 764-His REFERENCE A20751 !$#authors Mole, J.E.; Anderson, J.K.; Davison, E.A.; Woods, D.E. !$#journal J. Biol. Chem. (1984) 259:3407-3412 !$#title Complete primary structure for the zymogen of human !1complement factor B. !$#cross-references MUID:84161997; PMID:6546754 !$#accession A00934 !'##molecule_type protein; mRNA !'##residues 26-764 ##label MOL !'##cross-references GB:K01566 !'##note nucleic acid translation differs from the sequence shown in !1having 300-Leu, 328-Val, 356-Glu, and 357-Glu !'##note 736-Ser was also found !'##note glycosylation sites were determined REFERENCE A19188 !$#authors Christie, D.L.; Gagnon, J. !$#journal Biochem. J. (1983) 209:61-70 !$#title Amino acid sequence of the Bb fragment from complement !1factor B. Sequence of the major cyanogen bromide-cleavage !1peptide (CB-II) and completion of the sequence of the Bb !1fragment. !$#cross-references MUID:83204002; PMID:6342610 !$#contents the final paper in a series documenting the sequence, !1glycosylation site, and active site !$#accession A19188 !'##molecule_type protein !'##residues 260-296,'T',298-764 ##label CHR REFERENCE A19947 !$#authors Campbell, R.D.; Porter, R.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:4464-4468 !$#title Molecular cloning and characterization of the gene coding !1for human complement protein factor B. !$#cross-references MUID:83273641; PMID:6308626 !$#accession A19947 !'##molecule_type DNA !'##residues 346-764 ##label CAM !'##cross-references GB:J00125 !$#accession B19947 !'##molecule_type mRNA !'##residues 339-509 ##label CA1 !'##cross-references GB:J00126; NID:g187723; PIDN:AAA36226.1; !1PID:g553536 REFERENCE A25971 !$#authors Wu, L.; Morley, B.J.; Campbell, R.D. !$#journal Cell (1987) 48:331-342 !$#title Cell-specific expression of the human complement protein !1factor B gene: evidence for the role of two distinct !15'-flanking elements. !$#cross-references MUID:87102880; PMID:3643061 !$#accession B25971 !'##molecule_type DNA !'##residues 1-99 ##label WUL !'##cross-references GB:M15082; NID:g187699; PIDN:AAA59625.1; !1PID:g553534 REFERENCE S14339 !$#authors Niemann, M.A.; Bhown, A.S.; Miller, E.J. !$#journal Biochem. J. (1991) 274:473-480 !$#title The principal site of glycation of human complement Factor !1B. !$#cross-references MUID:91174758; PMID:2006911 !$#accession S14339 !'##molecule_type protein !'##residues 270-329 ##label NIE !'##note binding site for carbohydrate to lysine under artificial !1conditions REFERENCE A44628 !$#authors Morley, B.J.; Campbell, R.D. !$#journal EMBO J. (1984) 3:153-157 !$#title Internal homologies of the Ba fragment from human complement !1component factor B, a class III MHC antigen. !$#cross-references MUID:84158524; PMID:6323161 !$#accession A44628 !'##status preliminary !'##molecule_type mRNA !'##residues 16-225,'F',227-259 ##label MOR REFERENCE I54409 !$#authors Schwaeble, W.; Luttig, B.; Sokolowski, T.; Estaller, C.; !1Weiss, E.H.; Meyer zum Buschenfelde, K.H.; Whaley, K.; !1Dippold, W. !$#journal Immunobiology (1993) 188:221-232 !$#title Human complement factor B: functional properties of a !1recombinant zymogen of the alternative activation pathway !1convertase. !$#cross-references MUID:94041399; PMID:8225386 !$#accession I54409 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-764 ##label RES !'##cross-references GB:S67310; NID:g452937; PIDN:AAD13989.1; !1PID:g4261689 REFERENCE I57824 !$#authors Horiuchi, T.; Kim, S.; Matsumoto, M.; Watanabe, I.; Fujita, !1S.; Volanakis, J.E. !$#journal Mol. Immunol. (1993) 30:1587-1592 !$#title Human complement factor B: cDNA cloning, nucleotide !1sequencing, phenotypic conversion by site-directed !1mutagenesis and expression. !$#cross-references MUID:94067177; PMID:8247029 !$#accession I57824 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-31,'Q',33-764 ##label RE2 !'##cross-references GB:L15702; NID:g291921; PIDN:AAA16820.1; !1PID:g291922 COMMENT 292-Cys has a free sulfhydryl. GENETICS !$#gene GDB:BF !'##cross-references GDB:119726; OMIM:138470 !$#map_position 6p21.3-6p21.3 !$#introns 21/3; 99/3; 346/1; 390/1; 424/1; 470/1; 502/3; 542/1; 593/2; !1619/1; 652/3; 697/1; 713/3 !$#note the list of introns may be incomplete !$#note gene is located in the major histocompatibility complex, !1class III region COMPLEX complement factor B initially forms an inactive complex with !1complement factor C3b, becoming susceptible to cleavage by !1factor D into Ba and Bb fragments; Bb remains associated !1with complement factor C3b forming active C3/C5 convertase; !1Ba is released FUNCTION !$#description Bb is a serine proteinase; C3/C5 convertase cleaves !1complement C3 alpha chain to release C3a and form C3b; it !1also cleaves C5 alpha chain to release C5a and form C5b; Ba !1is nonfunctional !$#pathway complement alternate pathway CLASSIFICATION #superfamily complement C2; complement factor H repeat !1homology; trypsin homology; von Willebrand factor type A !1repeat homology KEYWORDS acute phase; complement alternate pathway; duplication; !1glycoprotein; hydrolase; plasma; serine proteinase FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-764 #product complement factor B #status experimental !8#label MAT\ !$26-259 #product complement factor Ba fragment #status !8experimental #label BAF\ !$37-98 #domain complement factor H repeat homology #label !8FH1\ !$103-158 #domain complement factor H repeat homology #label !8FH2\ !$165-218 #domain complement factor H repeat homology #label !8FH3\ !$260-764 #product C3/C5 convertase Bb fragment #status !8experimental #label BBF\ !$268-458 #domain von Willebrand factor type A repeat homology !8#label VFA\ !$482-752 #domain trypsin homology #status atypical #label TRY\ !$37-76,62-98, !$103-145,131-158, !$165-205,191-218, !$478-596,511-527, !$599-615,656-682, !$695-725 #disulfide_bonds #status predicted\ !$122,142,285,378 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$259-260 #cleavage_site Arg-Lys (complement factor D) #status !8experimental\ !$526,576,699 #active_site His, Asp, Ser #status experimental SUMMARY #length 764 #molecular-weight 85532 #checksum 5595 SEQUENCE /// ENTRY BBMS #type complete TITLE complement factor B precursor - mouse CONTAINS alternative-complement-pathway C3/C5 convertase (EC 3.4.21.47), Bb fragment ORGANISM #formal_name Mus musculus #common_name house mouse DATE 04-Dec-1986 #sequence_revision 30-Sep-1993 #text_change 19-May-2000 ACCESSIONS A38875; A36593; A00935 REFERENCE A38875 !$#authors Ishikawa, N.; Nonaka, M.; Wetsel, R.A.; Colten, H.R. !$#submission submitted to GenBank, January 1991 !$#accession A38875 !'##molecule_type DNA !'##residues 1-761 ##label IS2 !'##cross-references GB:M57890; GB:J05660; NID:g192413; PIDN:AAA63293.1; !1PID:g192414 REFERENCE A36593 !$#authors Ishikawa, N.; Nonaka, M.; Wetsel, R.A.; Colten, H.R. !$#journal J. Biol. Chem. (1990) 265:19040-19046 !$#title Murine complement C2 and factor B genomic and cDNA cloning !1reveals different mechanisms for multiple transcripts of C2 !1and B. !$#cross-references MUID:91035430; PMID:2229060 !$#accession A36593 !'##molecule_type mRNA !'##residues 1-761 ##label ISH !'##cross-references GB:M57890; NID:g192413; PIDN:AAA63293.1; !1PID:g192414; GB:J05660 REFERENCE A23194 !$#authors Sackstein, R.; Colten, H.R.; Woods, D.E. !$#journal J. Biol. Chem. (1983) 258:14693-14697 !$#title Phylogenetic conservation of a class III major !1histocompatibility complex antigen, factor B: isolation and !1nucleotide sequencing of mouse factor B cDNA clones. !$#cross-references MUID:84061931; PMID:6689022 !$#accession A00935 !'##molecule_type mRNA !'##residues 285-729,'P',731-744,'E',746-761 ##label SAC !'##cross-references GB:K01496; NID:g199252; PIDN:AAA39549.1; !1PID:g387437 COMMENT The Bb fragment, cleaved from this protein by complement !1factor D, associates with complement factor C3b to form !1alternative-complement-pathway C3/C5 convertase. GENETICS !$#introns 19/1; 97/1; 159/1; 217/1; 251/1; 296/3; 343/1; 387/1; 421/1; !1467/1; 499/3; 539/1; 590/2; 616/1; 649/3; 694/1; 710/3 CLASSIFICATION #superfamily complement C2; complement factor H repeat !1homology; trypsin homology; von Willebrand factor type A !1repeat homology KEYWORDS complement alternate pathway; duplication; glycoprotein; !1hydrolase; plasma; serine proteinase FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-256 #product Ba fragment #status predicted #label BAF\ !$34-95 #domain complement factor H repeat homology #label !8FH1\ !$100-155 #domain complement factor H repeat homology #label !8FH2\ !$162-215 #domain complement factor H repeat homology #label !8FH3\ !$257-761 #product Bb fragment #status predicted #label BBF\ !$265-455 #domain von Willebrand factor type A repeat homology !8#label VFA\ !$479-749 #domain trypsin homology #status atypical #label TRY\ !$34-73,59-95, !$100-142,128-155, !$162-202,188-215 #disulfide_bonds #status predicted\ !$119,139,282,375 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$475-593,508-524, !$596-612,653-679, !$692-722 #disulfide_bonds #status predicted\ !$523,573,696 #active_site His, Asp, Ser #status predicted SUMMARY #length 761 #molecular-weight 85004 #checksum 9540 SEQUENCE /// ENTRY C1HURB #type complete TITLE complement subcomponent C 1RBAR.GIF (EC 3.4.21.41) precursor [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 15-Nov-1984 #sequence_revision 30-Jun-1991 #text_change 03-Jun-2002 ACCESSIONS A24170; A29768; A29769; S02422; A00916; A37820; S68830 REFERENCE A24170 !$#authors Leytus, S.P.; Kurachi, K.; Sakariassen, K.S.; Davie, E.W. !$#journal Biochemistry (1986) 25:4855-4863 !$#title Nucleotide sequence of the cDNA coding for human complement !1C1r. !$#cross-references MUID:87026566; PMID:3021205 !$#accession A24170 !'##molecule_type mRNA !'##residues 1-705 ##label LEY !'##cross-references GB:M14058; NID:g179643; PIDN:AAA51851.1; !1PID:g179644 REFERENCE A29768 !$#authors Journet, A.; Tosi, M. !$#journal Biochem. J. (1986) 240:783-787 !$#title Cloning and sequencing of full-length cDNA encoding the !1precursor of human complement component C1r. !$#cross-references MUID:87156625; PMID:3030286 !$#accession A29768 !'##molecule_type mRNA !'##residues 1-151,'L',153-705 ##label JOU !'##cross-references GB:X04701; NID:g29538; PIDN:CAA28407.1; PID:g29539 REFERENCE A29769 !$#authors Arlaud, G.J.; Willis, A.C.; Gagnon, J. !$#journal Biochem. J. (1987) 241:711-720 !$#title Complete amino acid sequence of the A chain of human !1complement-classical-pathway enzyme C1r. !$#cross-references MUID:87241248; PMID:3036070 !$#accession A29769 !'##molecule_type protein !'##residues 18-166,'X',168-463 ##label ARL !'##note 152-Leu was also found REFERENCE S02422 !$#authors Arlaud, G.J.; van Dorsselaer, A.; Bell, A.; Mancini, M.; !1Aude, C.; Gagnon, J. !$#journal FEBS Lett. (1987) 222:129-134 !$#title Identification of erythro-beta-hydroxyasparagine in the !1EGF-like domain of human C1r. !$#cross-references MUID:88005128; PMID:2820791 !$#accession S02422 !'##molecule_type protein !'##residues 152-186 ##label AR3 !'##note 152-Leu was also found REFERENCE A00916 !$#authors Arlaud, G.J.; Gagnon, J. !$#journal Biochemistry (1983) 22:1758-1764 !$#title Complete amino acid sequence of the catalytic chain of human !1complement subcomponent C1r. !$#cross-references MUID:83204782; PMID:6303394 !$#accession A00916 !'##molecule_type protein !'##residues 464-705 ##label AR2 REFERENCE A37820 !$#authors Thielens, N.M.; Aude, C.A.; Lacroix, M.B.; Gagnon, J.; !1Arlaud, G.J. !$#journal J. Biol. Chem. (1990) 265:14469-14475 !$#title Ca(2+) binding properties and Ca(2+)-dependent interactions !1of the isolated NH-2-terminal alpha fragments of human !1complement proteases C1r and C1s. !$#cross-references MUID:90354439; PMID:2387866 !$#accession A37820 !'##molecule_type protein !'##residues 18-26;'L',153-160;'XX',252-255 ##label THI REFERENCE S68830 !$#authors Pelloux, S.; Thielens, N.M.; Hudry-Clergeon, G.; Petillot, !1Y.; Filhol, O.; Arlaud, G.J. !$#journal FEBS Lett. (1996) 386:15-20 !$#title Identification of a cryptic protein kinase CK2 !1phosphorylation site in human complement protease C1r, and !1its use to probe intramolecular interaction. !$#cross-references MUID:96221263; PMID:8635594 !$#accession S68830 !'##molecule_type protein !'##residues 133-137;187-211;610-613 ##label PEL !'##experimental_source plasma COMMENT C1r is a dimer of identical chains, each of which is !1activated by cleavage into two chains, A and B, connected by !1disulfide bonds. Autocatalysis releases fragments alpha and !1beta from the A chain, while fragment gamma remains !1disulfide-bonded to the B chain to form C1r II. COMMENT This protein is a serine protease that combines with C1q and !1C1s to form C1, the first component of the classical pathway !1of the complement system. C1r activates C1s so that it can, !1in turn, activate C2 and C4. GENETICS !$#gene GDB:C1R !'##cross-references GDB:119729; OMIM:216950 !$#map_position 12p13-12p13 CLASSIFICATION #superfamily complement subcomponent C1r; C1r/C1s repeat !1homology; complement factor H repeat homology; EGF homology; !1trypsin homology KEYWORDS acute phase; beta-hydroxyasparagine; calcium binding; !1complement pathway; duplication; glycoprotein; homodimer; !1hydrolase; phosphoprotein; plasma; serine proteinase FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$17-138 #domain C1r/C1s repeat homology #label C1R1\ !$18-463 #product complement C1r chain A #status experimental !8#label ACH\ !$146-189 #domain EGF homology #label EGF\ !$193-302 #domain C1r/C1s repeat homology #label C1R2\ !$297-463 #product C1r gamma fragment #status experimental !8#label GFR\ !$309-371 #domain complement factor H repeat homology #label !8FH1\ !$376-447 #domain complement factor H repeat homology #label !8FH2\ !$464-705 #product complement C1r chain B #status experimental !8#label BCH\ !$464-697 #domain trypsin homology #label TRY\ !$71-89,146-165, !$161-174,176-189, !$193-220,250-268, !$309-358,338-371, !$376-429,406-447, !$451-577,620-639, !$650-680 #disulfide_bonds #status predicted\ !$125,221,514,581 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$167 #modified_site erythro-beta-hydroxyasparagine (Asn) !8#status experimental\ !$206 #binding_site phosphate (Ser) (covalent) (by casein !8kinase II) #status experimental\ !$463-464 #cleavage_site Arg-Ile (autolytic) #status !8experimental\ !$502,557,654 #active_site His, Asp, Ser #status predicted SUMMARY #length 705 #molecular-weight 80173 #checksum 7028 SEQUENCE /// ENTRY C1HUS #type complete TITLE complement subcomponent C 1SBAR.GIF (EC 3.4.21.42) precursor [validated] - human ALTERNATE_NAMES C1 esterase precursor ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Jun-2002 ACCESSIONS A40496; A27381; S00224; S26732; S05634; A05140; A25396; !1A38407; B37820 REFERENCE A40496 !$#authors Kusumoto, H.; Hirosawa, S.; Salier, J.P.; Hagen, F.S.; !1Kurachi, K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:7307-7311 !$#title Human genes for complement components C1r and C1s in a close !1tail-to-tail arrangement. !$#cross-references MUID:89017187; PMID:2459702 !$#accession A40496 !'##molecule_type mRNA !'##residues 1-688 ##label KUS !'##cross-references GB:J04080; NID:g179645; PIDN:AAA51852.1; !1PID:g179646 REFERENCE A27381 !$#authors Tosi, M.; Duponchel, C.; Meo, T.; Julier, C. !$#journal Biochemistry (1987) 26:8516-8524 !$#title Complete cDNA sequence of human complement C1s and close !1physical linkage of the homologous genes C1s and C1r. !$#cross-references MUID:88163522; PMID:2831944 !$#accession A27381 !'##molecule_type mRNA !'##residues 1-688 ##label TOS !'##cross-references GB:M18767; NID:g179647; PIDN:AAA51853.1; !1PID:g179648 REFERENCE S00224 !$#authors Mackinnon, C.M.; Carter, P.E.; Smyth, S.J.; Dunbar, B.; !1Fothergill, J.E. !$#journal Eur. J. Biochem. (1987) 169:547-553 !$#title Molecular cloning of cDNA for human complement component !1C1s. The complete amino acid sequence. !$#cross-references MUID:88082788; PMID:3500856 !$#accession S00224 !'##molecule_type mRNA !'##residues 1-688 ##label MAC !'##cross-references EMBL:X06596; NID:g29542; PIDN:CAA29817.1; !1PID:g763110 !$#accession S26732 !'##molecule_type protein !'##residues 16-38;68-116;170-236;246-262;265-280;282-284;287-308, !1315-363;384-394;421-435;438-688 ##label MA2 REFERENCE S05634 !$#authors Tosi, M.; Duponchel, C.; Meo, T.; Couture-Tosi, E. !$#journal J. Mol. Biol. (1989) 208:709-714 !$#title Complement genes C1r and C1s feature an intronless serine !1protease domain closely related to haptoglobin. !$#cross-references MUID:90040704; PMID:2553984 !$#accession S05634 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 356-513,'G',514-688 ##label TO2 REFERENCE A05140 !$#authors Carter, P.E.; Dunbar, B.; Fothergill, J.E. !$#journal Biochem. J. (1983) 215:565-571 !$#title The serine proteinase chain of human complement component !1C1s. Cyanogen bromide cleavage and N-terminal sequences of !1the fragments. !$#cross-references MUID:84104122; PMID:6362661 !$#accession A05140 !'##molecule_type protein !'##residues 438-483,'X',485-500;503-534;542-558;561-572,'A', !1574-601;617-623;626-644;647-652,'X',654-656 ##label CAR REFERENCE A25396 !$#authors Spycher, S.E.; Nick, H.; Rickli, E.E. !$#journal Eur. J. Biochem. (1986) 156:49-57 !$#title Human complement component C1s. Partial sequence !1determination of the heavy chain and identification of the !1peptide bond cleaved during activation. !$#cross-references MUID:86164350; PMID:3007145 !$#accession A25396 !'##molecule_type protein !'##residues 16-61;168-219;287-293,'K',295-334;384-445 ##label SPY REFERENCE A38407 !$#authors Hess, D.; Schaller, J.; Rickli, E.E. !$#journal Biochemistry (1991) 30:2827-2833 !$#title Identification of the disulfide bonds of human complement !1C1s. !$#cross-references MUID:91175725; PMID:2007122 !$#accession A38407 !'##molecule_type protein !'##residues 131-134,'X',136-146,'X',148-150;155,'X',157-162;166-170, !1'X',172-174,'X',176-180;189-201,'X', !1203-205;227-234;247-251;288-293,'X',295-297;319-322;338-340, !1'X',342-345;352-358,'X',360-364;385,'X',387-402,'X', !1404-408;416-424,'X',426-431;547-556;592-597;617,'X',619-627, !1'X',629-635;655-660 ##label HES REFERENCE A37820 !$#authors Thielens, N.M.; Aude, C.A.; Lacroix, M.B.; Gagnon, J.; !1Arlaud, G.J. !$#journal J. Biol. Chem. (1990) 265:14469-14475 !$#title Ca(2+) binding properties and Ca(2+)-dependent interactions !1of the isolated NH-2-terminal alpha fragments of human !1complement proteases C1r and C1s. !$#cross-references MUID:90354439; PMID:2387866 !$#accession B37820 !'##molecule_type protein !'##residues 16-25;'X',203-207 ##label THI REFERENCE A32672 !$#authors Thielens, N.M.; Van Dorsselaer, A.; Gagnon, J.; Arlaud, G.J. !$#journal Biochemistry (1990) 29:3570-3578 !$#title Chemical and functional characterization of a fragment of !1C1s containing the epidermal growth factor homology region. !$#cross-references MUID:90283368; PMID:2141278 !$#contents annotation; erythro-beta-hydroxyasparagine site, content !$#note about half of the A chains contain !1erythro-beta-hydroxyasparagine COMMENT This protein is a serine proteinase that combines with C1q !1and C1r to form C1, the first component of the classical !1pathway of the complement system. C1r activates C1s, which !1then activates C2 and C4. COMMENT C1s is a dimer of identical chains, each of which is !1activated by cleavage into two chains, A and B, connected by !1disulfide bonds. GENETICS !$#gene GDB:C1S !'##cross-references GDB:119730; OMIM:120580 !$#map_position 12p13-12p13 !$#introns 291/1; 329/3; 356/1; 399/1; 424/1 !$#note the list of introns may be incomplete CLASSIFICATION #superfamily complement subcomponent C1r; C1r/C1s repeat !1homology; complement factor H repeat homology; EGF homology; !1trypsin homology KEYWORDS acute phase; beta-hydroxyasparagine; calcium binding; !1complement pathway; duplication; glycoprotein; homodimer; !1hydrolase; plasma; serine proteinase FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$11-127 #domain C1r/C1s repeat homology #label C1R1\ !$16-688 #product complement subcomponent C1s #status !8experimental #label MAT\ !$16-437 #product complement subcomponent C1s chain A (heavy !8chain) #status experimental #label ACH\ !$135-171 #domain EGF homology #label EGF\ !$175-287 #domain C1r/C1s repeat homology #label C1R2\ !$294-354 #domain complement factor H repeat homology #label !8FH1\ !$359-421 #domain complement factor H repeat homology #label !8FH2\ !$438-688 #product complement subcomponent C1s chain B (light !8chain) #status experimental #label BCH\ !$438-675 #domain trypsin homology #label TRY\ !$65-83,135-147, !$143-156,158-171, !$175-202,234-251, !$294-341,321-354, !$359-403,386-421, !$425-549,595-618, !$628-659 #disulfide_bonds #status experimental\ !$149 #modified_site erythro-beta-hydroxyasparagine (Asn) !8(partial) #status experimental\ !$174,406 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$437-438 #cleavage_site Arg-Ile (complement subcomponent C1r) !8#status experimental\ !$475,529,632 #active_site His, Asp, Ser #status predicted SUMMARY #length 688 #molecular-weight 76684 #checksum 5721 SEQUENCE /// ENTRY S05008 #type complete TITLE complement subcomponent C 1SBAR.GIF (EC 3.4.21.42) precursor [similarity] - golden hamster ORGANISM #formal_name Mesocricetus auratus #common_name golden hamster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S05008 REFERENCE S05008 !$#authors Kinoshita, H.; Sakiyama, H.; Tokunaga, K.; Imajoh-Ohmi, S.; !1Hamada, Y.; Isono, K.; Sakiyama, S. !$#journal FEBS Lett. (1989) 250:411-415 !$#title Complete primary structure of a calcium-dependent serine !1proteinase capable of degrading extracellular matrix !1proteins. !$#cross-references MUID:89325606; PMID:2753140 !$#accession S05008 !'##molecule_type mRNA !'##residues 1-695 ##label KIN !'##cross-references EMBL:X16160; NID:g49621; PIDN:CAA34286.1; !1PID:g49622 !'##note part of this sequence, including the amino ends of both the !1heavy and light chains, was confirmed by protein sequencing CLASSIFICATION #superfamily complement subcomponent C1r; C1r/C1s repeat !1homology; complement factor H repeat homology; EGF homology; !1trypsin homology KEYWORDS beta-hydroxyasparagine; calcium binding; duplication; !1glycoprotein; hydrolase; serine proteinase FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$17-133 #domain C1r/C1s repeat homology #label C1R1\ !$22-444 #product serine proteinase heavy chain #status !8experimental #label HCH\ !$141-177 #domain EGF homology #label EGF\ !$181-293 #domain C1r/C1s repeat homology #label C1R2\ !$300-360 #domain complement factor H repeat homology #label !8FH1\ !$365-428 #domain complement factor H repeat homology #label !8FH2\ !$445-682 #domain trypsin homology #label TRY\ !$446-695 #product serine proteinase light chain #status !8experimental #label LCH\ !$71-89,141-153, !$149-162,164-177, !$181-208,240-257, !$300-347,327-360, !$365-410,392-428, !$432-556,602-625, !$634-666 #disulfide_bonds #status predicted\ !$155 #modified_site erythro-beta-hydroxyasparagine (Asn) !8#status predicted\ !$180,413 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$482,536,638 #active_site His, Asp, Ser #status predicted SUMMARY #length 695 #molecular-weight 77492 #checksum 3079 SEQUENCE /// ENTRY I54763 #type complete TITLE Ra-reactive factor (EC 3.4.21.-) 1 precursor - human ALTERNATE_NAMES mannose binding protein-associated serine proteinase 1 (MASP-1) ORGANISM #formal_name Homo sapiens #common_name man DATE 19-May-2000 #sequence_revision 19-May-2000 #text_change 16-Jun-2000 ACCESSIONS I54763; JN0883 REFERENCE I54763 !$#authors Sato, T.; Endo, Y.; Matsushita, M.; Fujita, T. !$#journal Int. Immunol. (1994) 6:665-669 !$#title Molecular characterization of a novel serine protease !1involved in activation of the complement system by !1mannose-binding protein. !$#cross-references MUID:94289349; PMID:8018603 !$#accession I54763 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-699 ##label SAT !'##cross-references GB:D28593; NID:g790963; PIDN:BAA05928.1; !1PID:g471128 REFERENCE JN0883 !$#authors Takada, F.; Takayama, Y.; Hatsuse, H.; Kawakami, M. !$#journal Biochem. Biophys. Res. Commun. (1993) 196:1003-1009 !$#title A new member of the C1s family of complement proteins found !1in a bactericidal factor, Ra-reactive factor, in human !1serum. !$#cross-references MUID:94059062; PMID:8240317 !$#accession JN0883 !'##molecule_type mRNA !'##residues 1-234,'E',236-284,'G',286-498,'K',500-542,'K',544-642,'S', !1644-699 ##label TAK !'##cross-references DDBJ:D17525; NID:g439712; PIDN:BAA04477.1; !1PID:g439713 !'##experimental_source liver COMMENT This is a serum bactericidal factor that activates !1complement C4 and C2 components after binding to Ra and R2 !1polysaccharides. GENETICS !$#gene GDB:MASP1; GDB:CRARF; CRARF1; PRSS5; MASP !'##cross-references GDB:361104; GDB:330954; OMIM:600521 !$#map_position 3q27-3q28 CLASSIFICATION #superfamily complement subcomponent C1r; C1r/C1s repeat !1homology; complement factor H repeat homology; EGF homology; !1trypsin homology KEYWORDS beta-hydroxyasparagine; complement pathway; duplication; !1glycoprotein; hydrolase; liver; serine proteinase FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-448,449-699 #product Ra-reactive factor #status predicted #label !8MAT\ !$19-135 #domain C1r/C1s repeat homology #label C1R1\ !$143-181 #domain EGF homology #label EGF\ !$185-294 #domain C1r/C1s repeat homology #label C1R2\ !$301-362 #domain complement factor H repeat homology #label !8FH1\ !$367-432 #domain complement factor H repeat homology #label !8FH2\ !$449-691 #domain trypsin homology #label TRY\ !$49,178,407 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$73-91,143-157, !$153-166,168-181, !$185-212,242-260, !$301-349,329-362, !$367-414,397-432, !$436-572,614-631, !$642-672 #disulfide_bonds #status predicted\ !$159 #modified_site erythro-beta-hydroxyasparagine (Asn) !8#status predicted\ !$448-449 #cleavage_site Arg-Ile (autolytic) #status predicted\ !$490,552,646 #active_site His, Asp, Ser #status predicted SUMMARY #length 699 #molecular-weight 79187 #checksum 357 SEQUENCE /// ENTRY A59271 #type complete TITLE Ra-reactive factor (EC 3.4.21.-) 2 precursor - human ALTERNATE_NAMES mannose binding protein-associated serine proteinase 2 (MASP-2) ORGANISM #formal_name Homo sapiens #common_name man DATE 19-May-2000 #sequence_revision 19-May-2000 #text_change 16-Jun-2000 ACCESSIONS A59271 REFERENCE A59271 !$#authors Thiel, S.; Vorup-Jensen, T.; Stover, C.M.; Schwaeble, W.J.; !1Laursen, S.B.; Poulsen, K.; Willis, A.C.; Eggleton, P.; !1Hansen, S.; Holmskov, U.; Reid, K.B.M.; Jensenius, J.C. !$#journal Nature (1997) 386:506-510 !$#title A second serine protease associated with mannan-binding !1lectin that activates complement. !$#cross-references MUID:97242412; PMID:9087411 !$#accession A59271 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type mRNA !'##residues 1-686 ##label JEN !'##cross-references GB:Y09926; NID:g4007626; PIDN:CAA71059.1; !1PID:g4007627 !'##experimental_source tissue liver !'##note submitted to GenBank, December 1996 !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing GENETICS !$#gene GDB:MASP2 !'##cross-references GDB:6071500 !$#map_position 1p36.2-1p36.3 CLASSIFICATION #superfamily complement subcomponent C1r; C1r/C1s repeat !1homology; complement factor H repeat homology; EGF homology; !1trypsin homology KEYWORDS beta-hydroxyasparagine; complement pathway; duplication; !1hydrolase; serine proteinase FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-444,445-686 #product Ra-reactive factor 2 #status predicted !8#label MAT\ !$19-134 #domain C1r/C1s repeat homology #label C1R1\ !$142-180 #domain EGF homology #label EGF\ !$184-293 #domain C1r/C1s repeat homology #label C1R2\ !$300-361 #domain complement factor H repeat homology #label !8FH1\ !$366-430 #domain complement factor H repeat homology #label !8FH2\ !$445-679 #domain trypsin homology #label TRY\ !$72-90,142-156, !$152-165,167-180, !$184-211,241-259, !$300-348,328-361, !$366-412,396-430, !$434-552,598-618, !$629-660 #disulfide_bonds #status predicted\ !$158 #modified_site erythro-beta-hydroxyasparagine (Asn) !8#status predicted\ !$444-445 #cleavage_site Arg-Ile (autolytic) #status predicted\ !$483,532,633 #active_site His, Asp, Ser #status predicted SUMMARY #length 686 #molecular-weight 75685 #checksum 2072 SEQUENCE /// ENTRY A24702 #type complete TITLE serine proteinase snake (EC 3.4.21.-) precursor - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A24702; S47868 REFERENCE A24702 !$#authors DeLotto, R.; Spierer, P. !$#journal Nature (1986) 323:688-692 !$#title A gene required for the specification of dorsal-ventral !1pattern in Drosophila appears to encode a serine protease. !$#accession A24702 !'##molecule_type DNA !'##residues 1-430 ##label DEL REFERENCE S47868 !$#authors Smith, C.; Giordano, H.; DeLotto, R. !$#journal Genetics (1994) 136:1355-1365 !$#title Mutational analysis of the Drosophila snake protease: an !1essential role for domains within the proenzyme polypeptide !1chain. !$#cross-references MUID:94283901; PMID:8013912 !$#accession S47868 !'##status preliminary; translation not shown !'##molecule_type mRNA !'##residues 1-430 ##label SMI !'##cross-references EMBL:X04513; NID:g8631; PIDN:CAA28197.1; PID:g8632 GENETICS !$#gene snake !'##cross-references FlyBase:FBgn0003450 !$#note a maternal effect gene CLASSIFICATION #superfamily serine proteinase snake; trypsin homology KEYWORDS hydrolase; serine proteinase FEATURE !$184-422 #domain trypsin homology #label TRY\ !$233,280,376 #active_site His, Asp, Ser #status predicted SUMMARY #length 430 #molecular-weight 47782 #checksum 2723 SEQUENCE /// ENTRY A30100 #type complete TITLE serine proteinase easter (EC 3.4.21.-) precursor - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A30100; A32727 REFERENCE A30100 !$#authors Chasan, R.; Anderson, K.V. !$#journal Cell (1989) 56:391-400 !$#title The role of Easter, an apparent serine protease, in !1organizing the dorsal-ventral pattern of the Drosophila !1embryo. !$#cross-references MUID:89119561; PMID:2492450 !$#accession A30100 !'##molecule_type mRNA !'##residues 1-392 ##label CHA !'##cross-references GB:J03154; NID:g157313; PIDN:AAA28496.1; !1PID:g157314 REFERENCE A32727 !$#authors Jin, Y.; Anderson, K.V. !$#journal Cell (1990) 60:873-881 !$#title Dominant and recessive alleles of the Drosophila easter gene !1are point mutations at conserved sites in the serine !1protease catalytic domain. !$#cross-references MUID:90182675; PMID:2107028 !$#accession A32727 !'##status preliminary; nucleic acid sequence not shown; not compared !1with conceptual translation !'##molecule_type DNA !'##residues 128-392 ##label JIN GENETICS !$#gene FlyBase:ea !'##cross-references FlyBase:FBgn0000533 CLASSIFICATION #superfamily serine proteinase easter; trypsin homology KEYWORDS hydrolase; serine proteinase FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-392 #domain easter protein #status predicted #label MAT\ !$128-386 #domain trypsin homology #label TRY\ !$173,240,338 #active_site His, Asp, Ser #status predicted SUMMARY #length 392 #molecular-weight 43065 #checksum 8517 SEQUENCE /// ENTRY A23689 #type complete TITLE limulus clotting enzyme (EC 3.4.21.86) precursor - horseshoe crab (Tachypleus tridentatus) ORGANISM #formal_name Tachypleus tridentatus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-May-2000 ACCESSIONS A23689 REFERENCE A23689 !$#authors Muta, T.; Hashimoto, R.; Miyata, T.; Nishimura, H.; Toh, Y.; !1Iwanaga, S. !$#journal J. Biol. Chem. (1990) 265:22426-22433 !$#title Proclotting enzyme from horseshoe crab hemocytes. cDNA !1cloning, disulfide locations, and subcellular localization. !$#cross-references MUID:91093088; PMID:2266134 !$#accession A23689 !'##status preliminary !'##molecule_type mRNA !'##residues 1-375 ##label MUT !'##cross-references GB:M58366; NID:g161657; PIDN:AAA30094.1; !1PID:g161658 CLASSIFICATION #superfamily serine proteinase easter; trypsin homology KEYWORDS hydrolase; serine proteinase FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$128-370 #domain trypsin homology #label TRY\ !$172,228,326 #active_site His, Asp, Ser #status predicted SUMMARY #length 375 #molecular-weight 41591 #checksum 1665 SEQUENCE /// ENTRY A48050 #type complete TITLE coagulation factor B (EC 3.4.21.-) precursor - horseshoe crab (Tachypleus tridentatus) ORGANISM #formal_name Tachypleus tridentatus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A48050 REFERENCE A48050 !$#authors Muta, T.; Oda, T.; Iwanaga, S. !$#journal J. Biol. Chem. (1993) 268:21384-21388 !$#title Horseshoe crab coagulation factor B. A unique serine !1protease zymogen activated by cleavage of an Ile-Ile bond. !$#cross-references MUID:94012695; PMID:8407978 !$#accession A48050 !'##status preliminary !'##molecule_type mRNA; protein !'##residues 1-400 ##label MUT !'##cross-references GB:D14701; NID:g452529; PIDN:BAA03528.1; !1PID:g452530 !'##experimental_source hemocyte lysate !'##note sequence extracted from NCBI backbone (NCBIN:138529, !1NCBIP:138530) CLASSIFICATION #superfamily serine proteinase easter; trypsin homology KEYWORDS hydrolase; serine proteinase FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$148-387 #domain trypsin homology #label TRY SUMMARY #length 400 #molecular-weight 43048 #checksum 9841 SEQUENCE /// ENTRY BZSO #type complete TITLE streptokinase (EC 3.4.-.-) - Streptococcus sp. ORGANISM #formal_name Streptococcus sp. DATE 05-Apr-1983 #sequence_revision 05-Apr-1983 #text_change 23-Aug-1996 ACCESSIONS A00967 REFERENCE A00967 !$#authors Jackson, K.W.; Tang, J. !$#journal Biochemistry (1982) 21:6620-6625 !$#title Complete amino acid sequence of streptokinase and its !1homology with serine proteases. !$#cross-references MUID:83127125; PMID:6760891 !$#accession A00967 !'##molecule_type protein !'##residues 1-415 ##label JAC !'##note 169-Asp and 181-Asp were also found !'##note this protein is not a protease, but it activates plasminogen by !1complexing with it CLASSIFICATION #superfamily streptokinase KEYWORDS hydrolase SUMMARY #length 415 #molecular-weight 47399 #checksum 7303 SEQUENCE /// ENTRY A22801 #type complete TITLE streptokinase precursor - Streptococcus "equisimilis" ORGANISM #formal_name Streptococcus "equisimilis" DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 24-Sep-1999 ACCESSIONS A22801 REFERENCE A22801 !$#authors Malke, H.; Roe, B.; Ferretti, J.J. !$#journal Gene (1985) 34:357-362 !$#title Nucleotide sequence of the streptokinase gene from !1Streptococcus equisimilis H46A. !$#cross-references MUID:85232082; PMID:2989113 !$#accession A22801 !'##molecule_type DNA !'##residues 1-440 ##label MAL !'##cross-references GB:X72832; NID:g407876; PIDN:CAA51351.1; !1PID:g407879 !'##experimental_source strain H46A GENETICS !$#gene skc CLASSIFICATION #superfamily streptokinase SUMMARY #length 440 #molecular-weight 50140 #checksum 4045 SEQUENCE /// ENTRY A29358 #type complete TITLE cerevisin (EC 3.4.21.48) precursor - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YEL060c; yeast proteinase B ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A29358; S50529; A42641; S20135 REFERENCE A29358 !$#authors Moehle, C.M.; Tizard, R.; Lemmon, S.K.; Smart, J.; Jones, !1E.W. !$#journal Mol. Cell. Biol. (1987) 7:4390-4399 !$#title Protease B of the lysosomelike vacuole of the yeast !1Saccharomyces cerevisiae is homologous to the subtilisin !1family of serine proteases. !$#cross-references MUID:88142830; PMID:3325823 !$#accession A29358 !'##molecule_type DNA !'##residues 1-635 ##label MOE !'##cross-references EMBL:M18097; NID:g172236; PIDN:AAA34901.1; !1PID:g172237 REFERENCE S50513 !$#authors Dietrich, F.S. !$#submission submitted to the EMBL Data Library, December 1994 !$#description The sequence of S. cerevisiae cosmids 9669, 8334, 8199, and !1lambda clone 1160. !$#accession S50529 !'##molecule_type DNA !'##residues 1-635 ##label DIE !'##cross-references EMBL:U18795; NID:g603241; PIDN:AAB65027.1; !1PID:g603258; GSPDB:GN00005; MIPS:YEL060c REFERENCE A42641 !$#authors Hoyt, M.A.; He, L.; Loo, K.K.; Saunders, W.S. !$#journal J. Cell Biol. (1992) 118:109-120 !$#title Two Saccharomyces cerevisiae kinesin-related gene products !1required for mitotic spindle assembly. !$#cross-references MUID:92317149; PMID:1618897 !$#accession A42641 !'##molecule_type DNA !'##residues 605-621,'K',623-635 ##label HOY !'##cross-references EMBL:Z11859; NID:g3541; PIDN:CAA77886.1; PID:g3543 !'##note sequence extracted from NCBI backbone (NCBIN:107723, !1NCBIP:107724) GENETICS !$#gene SGD:PRB1; MIPS:YEL060c !'##cross-references SGD:S0000786; MIPS:YEL060c !$#map_position 5L CLASSIFICATION #superfamily cerevisin; subtilisin homology KEYWORDS hydrolase; serine proteinase; yeast vacuole FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-635 #product cerevisin proprotein #status predicted !8#label MAT\ !$316-533 #domain subtilisin homology #label SBT\ !$325,357,519 #active_site Asp, His, Ser #status predicted SUMMARY #length 635 #molecular-weight 69621 #checksum 3187 SEQUENCE /// ENTRY SUBSCL #type complete TITLE subtilisin (EC 3.4.21.62) Carlsberg precursor - Bacillus licheniformis ORGANISM #formal_name Bacillus licheniformis DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 21-Jul-2000 ACCESSIONS A24111; A00968 REFERENCE A24111 !$#authors Jacobs, M.; Eliasson, M.; Uhlen, M.; Flock, J.I. !$#journal Nucleic Acids Res. (1985) 13:8913-8926 !$#title Cloning, sequencing and expression of subtilisin Carlsberg !1from Bacillus licheniformis. !$#cross-references MUID:86093688; PMID:3001653 !$#accession A24111 !'##molecule_type DNA !'##residues 1-379 ##label JAC !'##cross-references GB:X03341; NID:g487721; PIDN:CAB56500.1; !1PID:g5921206 !'##experimental_source strain NCIB6816 REFERENCE A00968 !$#authors Smith, E.L.; DeLange, R.J.; Evans, W.H.; Landon, M.; !1Markland, F.S. !$#journal J. Biol. Chem. (1968) 243:2184-2191 !$#title Subtilisin Carlsberg. V. The complete sequence; comparison !1with subtilisin BPN'; evolutionary relationships. !$#cross-references MUID:68234702; PMID:4967581 !$#accession A00968 !'##molecule_type protein !'##residues 106-206,'S',208-232,'A',234-261,'N',263-264,'S',266-315, !1'N',317-379 ##label SMI COMMENT Secretion of subtilisin is associated with the onset of !1sporulation, and many mutations blocking sporulation at !1early stages affect expression levels of subtilisin. !1However, subtilisin is not necessary for normal sporulation. CLASSIFICATION #superfamily subtilisin; subtilisin homology KEYWORDS extracellular protein; hydrolase; serine proteinase FEATURE !$1-29 #domain signal sequence #status predicted #label SIG\ !$30-105 #domain propeptide #status predicted #label APT\ !$106-379 #product subtilisin Carlsberg #status experimental !8#label MPT\ !$128-339 #domain subtilisin homology #label SBT\ !$137,168,325 #active_site Asp, His, Ser #status predicted SUMMARY #length 379 #molecular-weight 38908 #checksum 8579 SEQUENCE /// ENTRY SUBSD #type complete TITLE subtilisin (EC 3.4.21.62) DY - Bacillus subtilis (strain DY) ALTERNATE_NAMES alkaline serine proteinase ORGANISM #formal_name Bacillus subtilis #variety strain DY DATE 20-Sep-1984 #sequence_revision 20-Sep-1984 #text_change 02-Jul-1998 ACCESSIONS A00969; S02492 REFERENCE A00969 !$#authors Nedkov, P.; Oberthur, W.; Braunitzer, G. !$#journal Biol. Chem. Hoppe-Seyler (1985) 366:421-430 !$#title Determination of the complete amino-acid sequence of !1subtilisin DY and its comparison with the primary structures !1of the subtilisins BPN', Carlsberg and amylosacchariticus. !$#cross-references MUID:85279896; PMID:3927935 !$#accession A00969 !'##molecule_type protein !'##residues 1-274 ##label NED !'##experimental_source strain DY REFERENCE S02492 !$#authors Lilova, A.; Kleinschmidt, T.; Nedkov, P. !$#journal Biol. Chem. Hoppe-Seyler (1987) 368:1479-1487 !$#title Reductive alkylation of lysine residues in subtilisin DY. !$#cross-references MUID:88134577; PMID:3124865 !$#accession S02492 !'##molecule_type protein !'##residues !11-2;12-17;22-24;27-29;43-45;93-95;123;135-137;140-142; !1169-171;183-187;221;236-238;246,'D',248-250;264-266;274 !1##label LIL COMMENT Secretion of subtilisin is associated with the onset of !1sporulation, and many mutations blocking sporulation at !1early stages affect expression levels of subtilisin. !1However, subtilisin is not necessary for normal sporulation. CLASSIFICATION #superfamily subtilisin; subtilisin homology KEYWORDS extracellular protein; hydrolase; serine proteinase FEATURE !$23-234 #domain subtilisin homology #label SBT\ !$32,63,220 #active_site Asp, His, Ser #status predicted SUMMARY #length 274 #molecular-weight 27435 #checksum 2856 SEQUENCE /// ENTRY SUBSN #type complete TITLE subtilisin (EC 3.4.21.62) BPN' precursor - Bacillus amyloliquefaciens ALTERNATE_NAMES subtilisin Novo ORGANISM #formal_name Bacillus amyloliquefaciens DATE 24-Apr-1984 #sequence_revision 28-Aug-1985 #text_change 21-Jul-2000 ACCESSIONS B25415; A93495; T44584; A92033; A00970 REFERENCE A25415 !$#authors Vasantha, N.; Thompson, L.D.; Rhodes, C.; Banner, C.; Nagle, !1J.; Filpula, D. !$#journal J. Bacteriol. (1984) 159:811-819 !$#title Genes for alkaline protease and neutral protease from !1Bacillus amyloliquefaciens contain a large open reading !1frame between the regions coding for signal sequence and !1mature protein. !$#cross-references MUID:85006739; PMID:6090391 !$#accession B25415 !'##molecule_type DNA !'##residues 1-382 ##label VAS !'##cross-references GB:K02496; NID:g142525; PIDN:AAB05345.1; !1PID:g142526 !'##experimental_source ATCC 23844 REFERENCE A93495 !$#authors Wells, J.A.; Ferrari, E.; Henner, D.J.; Estell, D.A.; Chen, !1E.Y. !$#journal Nucleic Acids Res. (1983) 11:7911-7925 !$#title Cloning, sequencing, and secretion of Bacillus !1amyloliquefaciens subtilisin in Bacillus subtilis. !$#cross-references MUID:84069812; PMID:6316278 !$#accession A93495 !'##molecule_type DNA !'##residues 1-382 ##label WEL !$#accession T44584 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 'M',8-382 ##label WE2 !'##cross-references EMBL:X00165; NID:g39337; PIDN:CAA24990.1; !1PID:g773560 REFERENCE A92033 !$#authors Markland, F.S.; Smith, E.L. !$#journal J. Biol. Chem. (1967) 242:5198-5211 !$#title Subtilisin BPN'. VII. Isolation of cyanogen bromide peptides !1and the complete amino acid sequence. !$#cross-references MUID:68086682; PMID:6065094 !$#accession A92033 !'##molecule_type protein !'##residues 108-162,'PN',165-167,'D',169-194,'SA',197-204,'DA',207-264, !1'ST',267-357,'Q',359-382 ##label MAR REFERENCE A94443 !$#authors Kraut, J. !$#book The Enzymes, 3rd ed., vol.3, Boyer, P.D., ed., pp.547-560, !1Academic Press, New York, 1971 !$#title Subtilisin: X-ray structure. !$#contents annotation; X-ray crystallography, 2.5 angstroms; active !1site COMMENT Secretion of subtilisin is associated with the onset of !1sporulation, and many mutations blocking sporulation at !1early stages affect expression levels of subtilisin. !1However, subtilisin is not necessary for normal sporulation. GENETICS !$#start_codon GTG CLASSIFICATION #superfamily subtilisin; subtilisin homology KEYWORDS hydrolase; serine proteinase FEATURE !$1-32 #domain signal sequence #status predicted #label SIG\ !$33-107 #domain activation peptide #status predicted #label !8APT\ !$108-382 #product subtilisin BPN' #status experimental #label !8MPT\ !$130-342 #domain subtilisin homology #label SBT\ !$139,171,328 #active_site Asp, His, Ser #status experimental SUMMARY #length 382 #molecular-weight 39181 #checksum 9387 SEQUENCE /// ENTRY SUBSS #type complete TITLE subtilisin (EC 3.4.21.62) amylosacchariticus precursor - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 24-Apr-1984 #sequence_revision 24-Feb-1995 #text_change 16-Jun-2000 ACCESSIONS A41448; A00971; S68013 REFERENCE A41448 !$#authors Yoshimoto, T.; Oyama, H.; Honda, T.; Tone, H.; Takeshita, !1T.; Kamiyama, T.; Tsuru, D. !$#journal J. Biochem. (1988) 103:1060-1065 !$#title Cloning and expression of subtilisin amylosacchariticus !1gene. !$#cross-references MUID:89008194; PMID:3139650 !$#accession A41448 !'##molecule_type DNA !'##residues 1-381 ##label YOS !'##cross-references GB:D00264; NID:g216328; PIDN:BAA00186.1; !1PID:g912425 !'##experimental_source var. amylosacchariticus REFERENCE A00971 !$#authors Kurihara, M.; Markland, F.S.; Smith, E.L. !$#journal J. Biol. Chem. (1972) 247:5619-5631 !$#title Subtilisin amylosacchariticus. III. Isolation and sequence !1of the chymotryptic peptides and the complete amino acid !1sequence. !$#cross-references MUID:72266688; PMID:5055784 !$#accession A00971 !'##molecule_type protein !'##residues !1107;112-114;148-152;155-157;164-170;173-174;178-181;200-205; !1210-212;219-225;237-268;271-280;292-302;305-323;328-332; !1339-362;367-373;380-381 ##label KUR !'##experimental_source var. amylosacchariticus REFERENCE S68012 !$#authors Kamal, M.; Hoeoeg, J.O.; Kaiser, R.; Shafqat, J.; Razzaki, !1T.; Zaidi, Z.H.; Joernvall, H. !$#journal FEBS Lett. (1995) 374:363-366 !$#title Isolation, characterization and structure of subtilisin from !1a thermostable Bacillus subtilis isolate. !$#cross-references MUID:96069945; PMID:7589571 !$#accession S68013 !'##status preliminary !'##molecule_type protein !'##residues 107-235,'T',237-245,293-381 ##label KAM COMMENT Secretion of subtilisin is associated with the onset of !1sporulation, and many mutations blocking sporulation at !1early stages affect expression levels of subtilisin. !1However, subtilisin is not necessary for normal sporulation. GENETICS !$#start_codon GTG CLASSIFICATION #superfamily subtilisin; subtilisin homology KEYWORDS extracellular protein; hydrolase; serine proteinase FEATURE !$107-381 #product subtilisin #status predicted #label MAT\ !$129-341 #domain subtilisin homology #label SBT\ !$138,170,327 #active_site Asp, His, Ser #status predicted SUMMARY #length 381 #molecular-weight 39467 #checksum 7982 SEQUENCE /// ENTRY SUBSI #type complete TITLE subtilisin (EC 3.4.21.62) E precursor - Bacillus subtilis ALTERNATE_NAMES alkaline proteinase; bacillopeptidase E; extracellular alkaline serine proteinase aprE ORGANISM #formal_name Bacillus subtilis DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 16-Jun-2000 ACCESSIONS A00972; A26116; I39970; I39778; I39779; S68012; H69586 REFERENCE A00972 !$#authors Stahl, M.L.; Ferrari, E. !$#journal J. Bacteriol. (1984) 158:411-418 !$#title Replacement of the Bacillus subtilis subtilisin structural !1gene with an in vitro-derived deletion mutation. !$#cross-references MUID:84212198; PMID:6427178 !$#accession A00972 !'##molecule_type DNA !'##residues 1-381 ##label STA !'##cross-references GB:K01988; NID:g143519; PIDN:AAA22742.1; !1PID:g143520 !'##experimental_source strain I168 REFERENCE A26116 !$#authors Wong, S.L.; Price, C.W.; Goldfarb, D.S.; Doi, R.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:1184-1188 !$#title The subtilisin E gene of Bacillus subtilis is transcribed !1from a sigma37 promoter in vivo. !$#cross-references MUID:84144862; PMID:6322190 !$#accession A26116 !'##molecule_type DNA !'##residues 1-155 ##label WON !'##cross-references GB:K01443; NID:g143665; PIDN:AAA22814.1; !1PID:g143666 REFERENCE I39969 !$#authors Ikemura, H.; Takagi, H.; Inouye, M. !$#journal J. Biol. Chem. (1987) 262:7859-7864 !$#title Requirement of pro-sequence for the production of active !1subtilisin E in Escherichia coli. !$#cross-references MUID:87222417; PMID:3108260 !$#accession I39970 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-156 ##label IKE !'##cross-references GB:M16639; NID:g143521; PIDN:AAA22744.1; !1PID:g143523 REFERENCE I39778 !$#authors Henner, D.J.; Ferrari, E.; Perego, M.; Hoch, J.A. !$#journal J. Bacteriol. (1988) 170:296-300 !$#title Location of the targets of the hpr-97, sacU32(Hy), and !1sacQ36(Hy) mutations in upstream regions of the subtilisin !1promoter. !$#cross-references MUID:88086885; PMID:2447063 !$#accession I39778 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-8 ##label HEN !'##cross-references GB:M19125; NID:g142527; PIDN:AAA22245.1; !1PID:g142528 REFERENCE I39779 !$#authors Park, S. !$#journal J. Bacteriol. (1989) 171:2657-2665 !$#title Bacillus subtilis subtilisin gene (aprE) is expressed from a !1sigma-A (sigma-43) promoter in vitro and in vivo. !$#cross-references MUID:89213955; PMID:2496113 !$#accession I39779 !'##molecule_type DNA !'##residues 1-13 ##label PAR !'##cross-references GB:M31060; NID:g142529; PIDN:AAA22246.1; !1PID:g142530 !'##experimental_source strain W168, substrain PY79 REFERENCE S68012 !$#authors Kamal, M.; Hoeoeg, J.O.; Kaiser, R.; Shafqat, J.; Razzaki, !1T.; Zaidi, Z.H.; Joernvall, H. !$#journal FEBS Lett. (1995) 374:363-366 !$#title Isolation, characterization and structure of subtilisin from !1a thermostable Bacillus subtilis isolate. !$#cross-references MUID:96069945; PMID:7589571 !$#accession S68012 !'##status preliminary !'##molecule_type DNA !'##residues 113-323 ##label KAM REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69586 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-26,'V',28-381 ##label KUN !'##cross-references GB:Z99109; GB:AL009126; NID:g2633260; !1PIDN:CAB12870.1; PID:g2633366 !'##experimental_source strain 168 COMMENT Secretion of subtilisin is associated with the onset of !1sporulation, and many mutations blocking sporulation at !1early stages affect expression levels of subtilisin. !1However, subtilisin is not necessary for normal sporulation. GENETICS !$#gene aprE !$#map_position 690-771 !$#start_codon GTG FUNCTION !$#description catalyzes the hydrolyis of peptide bonds !$#pathway protein digestion !$#note this enzyme has broad specificity and will hydrolyze peptide !1amides; it prefers cleaving on the carboxyl side of large !1uncharged residues CLASSIFICATION #superfamily subtilisin; subtilisin homology KEYWORDS extracellular protein; hydrolase; protein digestion; serine !1proteinase FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-106 #domain activation peptide #status predicted #label !8APT\ !$107-381 #product subtilisin E #status predicted #label MPT\ !$129-341 #domain subtilisin homology #label SBT\ !$138,170,327 #active_site Asp, His, Ser #status predicted SUMMARY #length 381 #molecular-weight 39495 #checksum 8030 SEQUENCE /// ENTRY SUMYTV #type complete TITLE thermitase (EC 3.4.21.66) - Thermoactinomyces vulgaris ORGANISM #formal_name Thermoactinomyces vulgaris DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 15-Nov-1996 ACCESSIONS A00973 REFERENCE A00973 !$#authors Meloun, B.; Baudys, M.; Kostka, V.; Hausdorf, G.; Frommel, !1C.; Hohne, W.E. !$#journal FEBS Lett. (1985) 183:195-200 !$#title Complete primary structure of thermitase from !1Thermoactinomyces vulgaris and its structural features !1related to the subtilisin-type proteinases. !$#accession A00973 !'##molecule_type protein !'##residues 1-279 ##label MEL COMMENT This protein is enzymatically similar to a proteinase from !1Streptomyces sp. CLASSIFICATION #superfamily subtilisin; subtilisin homology KEYWORDS hydrolase; serine proteinase FEATURE !$29-239 #domain subtilisin homology #label SBT\ !$38,71,225 #active_site Asp, His, Ser #status predicted SUMMARY #length 279 #molecular-weight 28366 #checksum 466 SEQUENCE /// ENTRY S23407 #type complete TITLE subtilisin (EC 3.4.21.62) 1 precursor - Bacillus sp. (strain TA39) ORGANISM #formal_name Bacillus sp. DATE 04-Dec-1992 #sequence_revision 04-Dec-1992 #text_change 18-Jun-1999 ACCESSIONS S23407 REFERENCE S23407 !$#authors Narinx, E.; Davail, S.; Feller, G.; Gerday, C. !$#journal Biochim. Biophys. Acta (1992) 1131:111-113 !$#title Nucleotide and derived amino acid sequence of the subtilisin !1from the antarctic psychrotroph Bacillus TA39. !$#cross-references MUID:92256481; PMID:1581352 !$#accession S23407 !'##molecule_type DNA !'##residues 1-420 ##label NAR !'##cross-references EMBL:X62369; NID:g40200; PIDN:CAA44227.1; !1PID:g40201 GENETICS !$#gene sub1 CLASSIFICATION #superfamily subtilisin; subtilisin homology KEYWORDS extracellular protein; hydrolase; serine proteinase FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-111 #domain propeptide #status predicted #label PRO\ !$112-420 #product microbial serine proteinase #status !8predicted #label MAT\ !$136-374 #domain subtilisin homology #label SBT\ !$145,185,360 #active_site Asp, His, Ser #status predicted SUMMARY #length 420 #molecular-weight 44086 #checksum 3806 SEQUENCE /// ENTRY S25835 #type complete TITLE subtilisin (EC 3.4.21.62) precursor - Bacillus sp. (strain TA41) ORGANISM #formal_name Bacillus sp. DATE 22-Nov-1993 #sequence_revision 20-Feb-1995 #text_change 18-Jun-1999 ACCESSIONS S25835 REFERENCE S25835 !$#authors Davail, S.; Feller, G.; Narinx, E.; Gerday, C. !$#journal Gene (1992) 119:143-144 !$#title Sequence of the subtilisin-encoding gene from an antarctic !1psychrotroph Bacillus TA41. !$#cross-references MUID:93012966; PMID:1398082 !$#accession S25835 !'##molecule_type DNA !'##residues 1-419 ##label DAV !'##cross-references EMBL:X63533; NID:g40198; PIDN:CAA45096.1; !1PID:g40199 CLASSIFICATION #superfamily subtilisin; subtilisin homology KEYWORDS extracellular protein; hydrolase; serine proteinase FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-110 #domain propeptide #status predicted #label PRO\ !$111-419 #product microbial serine proteinase #status !8predicted #label MAT\ !$135-373 #domain subtilisin homology #label SBT\ !$144,184,359 #active_site Asp, His, Ser #status predicted SUMMARY #length 419 #molecular-weight 43346 #checksum 837 SEQUENCE /// ENTRY SUTIKA #type complete TITLE endopeptidase K (EC 3.4.21.64) precursor - imperfect fungus (Tritirachium album) ALTERNATE_NAMES proteinase K; Tritirachium alkaline proteinase ORGANISM #formal_name Tritirachium album DATE 30-Sep-1987 #sequence_revision 08-Feb-1996 #text_change 18-Jun-1999 ACCESSIONS S02142; A30465; A24541; A23188 REFERENCE S02142 !$#authors Gunkel, F.A.; Gassen, H.G. !$#journal Eur. J. Biochem. (1989) 179:185-194 !$#title Proteinase K from Tritirachium album Limber. !1Characterization of the chromosomal gene and expression of !1the cDNA in Escherichia coli. !$#cross-references MUID:89137080; PMID:2645134 !$#accession S02142 !'##molecule_type DNA !'##residues 1-384 ##label GUN !'##cross-references EMBL:X14689; NID:g5158; PIDN:CAA32820.1; !1PID:g295946 !$#accession A30465 !'##molecule_type mRNA !'##residues 1-384 ##label GUN2 !'##cross-references EMBL:X14688; NID:g5164; PIDN:CAA32819.1; PID:g5165 REFERENCE A24541 !$#authors Jany, K.D.; Lederer, G.; Mayer, B. !$#journal FEBS Lett. (1986) 199:139-144 !$#title Amino acid sequence of proteinase K from the mold !1Tritirachium album limber. Proteinase K - a !1subtilisin-related enzyme with disulfide bonds. !$#accession A24541 !'##molecule_type protein !'##residues 106-184,'G',185-311,'DL','S',317-376,378-384 ##label JAN REFERENCE A23188 !$#authors Jany, K.D.; Lederer, G.; Mayer, B. !$#journal Biol. Chem. Hoppe-Seyler (1986) 367:87 !$#title Proteinase K - a new subclass of the subtilisins. The amino !1acid sequence of the enzyme. !$#accession A23188 !'##molecule_type protein !'##residues 106-184,'G',185-311,'DS',314,317-373,'F',375-376,378-384 !1##label JA2 COMMENT proteinase K hydrolyzes keratin at aromatic and hydrophobic !1residues. GENETICS !$#introns 92/3 CLASSIFICATION #superfamily subtilisin; subtilisin homology KEYWORDS hydrolase; serine proteinase FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-105 #domain activation peptide #status predicted #label !8APT\ !$106-384 #product endopeptidase K #status predicted #label !8MAT\ !$135-343 #domain subtilisin homology #label SBT\ !$139-228,283-354 #disulfide_bonds #status experimental\ !$144,174,329 #active_site Asp, His, Ser #status predicted SUMMARY #length 384 #molecular-weight 40300 #checksum 6001 SEQUENCE /// ENTRY S22387 #type complete TITLE cuticle-degrading proteinase (EC 3.4.21.-) precursor - imperfect fungus (Metarhizium anisopliae) ORGANISM #formal_name Metarhizium anisopliae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S22387; S45442 REFERENCE S22387 !$#authors Leger, R.J.S.; Frank, D.C.; Roberts, D.W.; Staples, R.C. !$#journal Eur. J. Biochem. (1992) 204:991-1001 !$#title Molecular cloning and regulatory analysis of the !1cuticle-degrading-protease structural gene from the !1entomopathogenic fungus Metarhizium anisopliae. !$#cross-references MUID:92201213; PMID:1551399 !$#accession S22387 !'##molecule_type mRNA !'##residues 1-388 ##label LEG1 !'##cross-references EMBL:M73795; NID:g168342; PIDN:AAA33417.1; !1PID:g168343 !'##note the authors translated the codon GGT for residue 118 as Glu !$#accession S45442 !'##molecule_type protein !'##residues 108-115 ##label LEG2 CLASSIFICATION #superfamily subtilisin; subtilisin homology KEYWORDS glycoprotein; hydrolase; serine proteinase FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-107 #domain propeptide #status predicted #label PRO\ !$108-388 #product cuticle-degrading proteinase #status !8experimental #label MAT\ !$139-348 #domain subtilisin homology #label SBT\ !$143-233,288-360 #disulfide_bonds #status predicted\ !$148,179,334 #active_site Asp, His, Ser #status predicted\ !$278 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 388 #molecular-weight 40331 #checksum 3637 SEQUENCE /// ENTRY JC2142 #type complete TITLE alkaline proteinase (EC 3.4.21.-) precursor - fungus (Fusarium sp.) (strain S-19-5) ORGANISM #formal_name Fusarium sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JC2142; PC2082 REFERENCE JC2142 !$#authors Morita, S.; Kuriyama, M.; Maejima, K.; Kitano, K. !$#journal Biosci. Biotechnol. Biochem. (1994) 58:621-626 !$#title Cloning and nucleotide sequence of the alkaline protease !1gene from Fusarium sp. S-19-5 and expression in !1Saccharomyces cerevisiae. !$#cross-references MUID:94264394; PMID:7764853 !$#accession JC2142 !'##molecule_type mRNA !'##residues 1-379 ##label MOR !$#accession PC2082 !'##molecule_type protein !'##residues 100-111;301-310 ##label MO2 !'##note the authors translated the codon TGC for residue 74 as Ser GENETICS !$#gene Alp !$#introns 86/3; 148/3; 318/3 CLASSIFICATION #superfamily subtilisin; subtilisin homology KEYWORDS glycoprotein; hydrolase; serine proteinase FEATURE !$1-14 #domain signal sequence #status predicted #label SIG\ !$15-99 #domain propeptide #status predicted #label PRO\ !$100-379 #product alkaline proteinase #status predicted #label !8MAT\ !$131-339 #domain subtilisin homology #label SBT\ !$140,170,325 #active_site Asp, His, Ser #status predicted\ !$200,269,377 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 379 #molecular-weight 39402 #checksum 3767 SEQUENCE /// ENTRY S45493 #type complete TITLE serine proteinase (EC 3.4.21.-) isp6 - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES sexual differentiation subtilase-type proteinase ORGANISM #formal_name Schizosaccharomyces pombe DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S45493; T38773 REFERENCE S45492 !$#authors Sato, S.; Suzuki, H.; Widyastuti, U.; Hotta, Y.; Tabata, S. !$#journal Curr. Genet. (1994) 26:31-37 !$#title Identification and characterization of genes induced during !1sexual differentiation in Schizosaccharomyces pombe. !$#cross-references MUID:95042833; PMID:7954893 !$#accession S45493 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type mRNA !'##residues 1-467 ##label SAT !'##cross-references GB:D14063; NID:g218555; PIDN:BAA03149.1; !1PID:g218556 REFERENCE Z21751 !$#authors Skelton, J.; Churcher, C.M.; Barrell, B.G.; Rajandream, !1M.A.; Wood, V. !$#submission submitted to the EMBL Data Library, August 1997 !$#accession T38773 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-467 ##label SKE !'##cross-references EMBL:Z98762; PIDN:CAB11474.1; GSPDB:GN00066; !1SPDB:SPAC4A8.04 !'##experimental_source strain 972h-; cosmid c4A8 GENETICS !$#gene isp6; SPAC4A8.04 !$#map_position 1 CLASSIFICATION #superfamily subtilisin; subtilisin homology KEYWORDS hydrolase; serine proteinase FEATURE !$212-423 #domain subtilisin homology #label SBT\ !$221,253,409 #active_site Asp, His, Ser #status predicted SUMMARY #length 467 #molecular-weight 49366 #checksum 416 SEQUENCE /// ENTRY JU0332 #type complete TITLE alkaline proteinase (EC 3.4.21.-) precursor - fungus (Acremonium chrysogenum) ALTERNATE_NAMES serine proteinase ORGANISM #formal_name Acremonium chrysogenum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS JU0332; PN0129 REFERENCE JU0332 !$#authors Isogai, T.; Fukagawa, M.; Kojo, H.; Kohsaka, M.; Aoki, H.; !1Imanaka, H. !$#journal Agric. Biol. Chem. (1991) 55:471-477 !$#title Cloning and nucleotide sequences of the complementary and !1genomic DNAs for the alkaline protease from Acremonium !1chrysogenum. !$#cross-references MUID:91299283; PMID:1368696 !$#accession JU0332 !'##molecule_type DNA !'##residues 1-402 ##label ISO !'##cross-references GB:D00923; NID:g217795; PIDN:BAA00765.1; !1PID:g217796 !'##experimental_source ATCC 11550 !'##note cDNA is also sequenced REFERENCE PN0129 !$#authors Vasilyeva, L.I.; Rudenskaya, G.N.; Krestyanova, I.N.; !1Khodova, O.M.; Bartoshevich, Y.E.; Stepanov, V.M. !$#journal Biokhimiia (1985) 50:355-361 !$#title Acremonium chrysogenum proteinase I; serine proteinase of a !1new type. !$#accession PN0129 !'##molecule_type protein !'##residues 121-128,'P',129-135,'QN',138-140,'A',142-146,'XG' ##label !1VAS !'##note article in Russian with English abstract GENETICS !$#gene Alp !$#introns 96/3; 255/1 CLASSIFICATION #superfamily subtilisin; subtilisin homology KEYWORDS hydrolase; serine proteinase FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-117 #domain propeptide #status predicted #label PRO\ !$118-402 #product alkaline proteinase #status predicted #label !8MAT\ !$151-361 #domain subtilisin homology #label SBT\ !$160,191,347 #active_site Asp, His, Ser #status predicted SUMMARY #length 402 #molecular-weight 42099 #checksum 7166 SEQUENCE /// ENTRY S32905 #type complete TITLE serine proteinase (EC 3.4.21.-) prb1 precursor - fungus (Trichoderma harzianum) ALTERNATE_NAMES basic proteinase ORGANISM #formal_name Trichoderma harzianum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S32905; S34787 REFERENCE S32905 !$#authors Geremia, R.A.; Goldman, G.H.; Jacobs, D.; Ardiles, W.; Vila, !1S.B.; van Montagu, M.; Herrera-Estrella, A. !$#journal Mol. Microbiol. (1993) 8:603-613 !$#title Molecular characterization of the proteinase-encoding gene, !1prb1, related to mycoparasitism by Trichoderma harzianum. !$#cross-references MUID:93316857; PMID:8326868 !$#accession S32905 !'##molecule_type DNA !'##residues 1-409 ##label GER1 !'##cross-references EMBL:M87518; NID:g170544; PIDN:AAA34211.1; !1PID:g170545 !$#accession S34787 !'##molecule_type protein !'##residues 121-130;157-159,'X',161-171;'X',317-327,'X',329-330;391-404 !1##label GER2 GENETICS !$#gene prb1 !$#introns 100/3; 210/3 CLASSIFICATION #superfamily subtilisin; subtilisin homology KEYWORDS hydrolase; serine proteinase FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-120 #domain propeptide #status predicted #label PRO\ !$121-409 #product serine proteinase #status experimental !8#label MAT\ !$152-367 #domain subtilisin homology #label SBT\ !$161,192,353 #active_site Asp, His, Ser #status predicted SUMMARY #length 409 #molecular-weight 42271 #checksum 1062 SEQUENCE /// ENTRY SUASO #type complete TITLE oryzin (EC 3.4.21.63) precursor - Aspergillus oryzae ALTERNATE_NAMES Aspergillus alkaline proteinase; Aspergillus proteinase B ORGANISM #formal_name Aspergillus oryzae DATE 30-Jun-1989 #sequence_revision 12-Apr-1996 #text_change 16-Jun-2000 ACCESSIONS JU0278; JQ0355; JQ1345; JT0237; A37538; A38852 REFERENCE JU0278 !$#authors Murakami, K.; Ishida, Y.; Masaki, A.; Tatsumi, H.; Murakami, !1S.; Nakano, E.; Motai, H.; Kawabe, H.; Arimura, H. !$#journal Agric. Biol. Chem. (1991) 55:2807-2811 !$#title Isolation and characterization of the alkaline protease gene !1of Aspergillus oryzae. !$#cross-references MUID:92134740; PMID:1368748 !$#accession JU0278 !'##molecule_type DNA !'##residues 1-403 ##label MUR !'##cross-references GB:D10062; NID:g217802; PIDN:BAA00951.1; !1PID:g217803 REFERENCE JQ0355 !$#authors Tatsumi, H.; Ogawa, Y.; Murakami, S.; Ishida, Y.; Murakami, !1K.; Masaki, A.; Kawabe, H.; Arimura, H.; Nakano, E.; Motai, !1H. !$#journal Mol. Gen. Genet. (1989) 219:33-38 !$#title A full length cDNA clone for the alkaline protease from !1Aspergillus oryzae: structural analysis and expression in !1Saccharomyces cerevisiae. !$#cross-references MUID:90136525; PMID:2693947 !$#accession JQ0355 !'##molecule_type mRNA !'##residues 1-403 ##label TAT !'##cross-references GB:X17561; NID:g2427; PIDN:CAA35594.1; PID:g2428 !'##experimental_source ATCC 20386 !'##note residues 1-10 were confirmed by amino acid sequencing REFERENCE JQ1345 !$#authors Cheevadhanarak, S.; Renno, D.V.; Saunders, G.; Holt, G. !$#journal Gene (1991) 108:151-155 !$#title Cloning and selective overexpression of an alkaline !1protease-encoding gene from Aspergillus oryzae. !$#cross-references MUID:92104499; PMID:1840548 !$#accession JQ1345 !'##molecule_type DNA !'##residues 1-403 ##label CHE !'##cross-references GB:S75278; NID:g241857; PIDN:AAB20819.1; !1PID:g241858 !'##experimental_source strain U212 REFERENCE JT0237 !$#authors Tatsumi, H.; Ohsawa, M.; Tsuji, R.F.; Murakami, S.; Nakano, !1E.; Motai, H.; Masaki, A.; Ishida, Y.; Murakami, K.; Kawabe, !1H.; Arimura, H. !$#journal Agric. Biol. Chem. (1988) 52:1887-1888 !$#title Cloning and sequencing of the alkaline protease cDNA from !1Aspergillus oryzae. !$#accession JT0237 !'##molecule_type mRNA !'##residues 122-228,'L',230-403 ##label TA1 !'##note this sequence has been revised in reference A38852 !$#accession A37538 !'##molecule_type protein !'##residues 122-137;263-274;305-332;360-373 ##label TA2 REFERENCE A38852 !$#authors Tatsumi, H.; Ohsawa, M.; Tsuji, R.F.; Murakami, S.; Nakano, !1E.; Motai, H.; Masaki, A.; Ishida, Y.; Murakami, K.; Kawabe, !1H.; Arimura, H. !$#submission submitted to JIPID, September 1992 !$#accession A38852 !'##molecule_type mRNA !'##residues 'V',123-137, !1'AFNDAVENAFEQAIQKSNNRASFSNFGKVVDVFAPGQDILLYLAALENLDGPAA', !1192-228,'L',230-403 ##label TA3 GENETICS !$#gene alpA !$#introns 108/3; 257/1; 286/3 CLASSIFICATION #superfamily subtilisin; subtilisin homology KEYWORDS glycoprotein; hydrolase; serine proteinase FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$122-403 #product oryzin #status experimental #label MAT\ !$153-363 #domain subtilisin homology #label SBT\ !$162,193,349 #active_site Asp, His, Ser #status predicted\ !$253 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 403 #molecular-weight 42571 #checksum 9060 SEQUENCE /// ENTRY S22184 #type complete TITLE oryzin (EC 3.4.21.63) precursor - Aspergillus fumigatus ALTERNATE_NAMES Aspergillus alkaline proteinase; Aspergillus proteinase B; serine proteinase alp ORGANISM #formal_name Aspergillus fumigatus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-May-2000 ACCESSIONS S22184 REFERENCE S22184 !$#authors Monod, M. !$#submission submitted to the EMBL Data Library, January 1992 !$#description Cloning and characterization of the alkanline protease gene !1(alp) from Aspergillus fumigatus. !$#accession S22184 !'##status preliminary !'##molecule_type DNA !'##residues 1-403 ##label MON !'##cross-references EMBL:Z11580; NID:g2294; PIDN:CAA77666.1; PID:g2295 GENETICS !$#gene alp !$#introns 108/3; 257/1; 286/3 CLASSIFICATION #superfamily subtilisin; subtilisin homology KEYWORDS hydrolase; serine proteinase FEATURE !$153-363 #domain subtilisin homology #label SBT\ !$162,193,349 #active_site Asp, His, Ser #status predicted SUMMARY #length 403 #molecular-weight 42245 #checksum 3376 SEQUENCE /// ENTRY A26955 #type complete TITLE alkaline serine proteinase (EC 3.4.21.-) precursor - yeast (Yarrowia lipolytica) ALTERNATE_NAMES alkaline extracellular proteinase ORGANISM #formal_name Yarrowia lipolytica, Candida lipolytica DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 24-Sep-1999 ACCESSIONS A26955; A31563 REFERENCE A26955 !$#authors Davidow, L.S.; O'Donnell, M.M.; Kaczmarek, F.S.; Pereira, !1D.A.; DeZeeuw, J.R.; Franke, A.E. !$#journal J. Bacteriol. (1987) 169:4621-4629 !$#title Cloning and sequencing of the alkaline extracellular !1protease gene of Yarrowia lipolytica. !$#cross-references MUID:88007405; PMID:2443483 !$#accession A26955 !'##molecule_type DNA !'##residues 1-454 ##label DAV !'##cross-references GB:M17741; NID:g173242; PIDN:AAA35242.1; !1PID:g173244 REFERENCE A31563 !$#authors Matoba, S.; Fukayama, J.; Wing, R.A.; Ogrydziak, D.M. !$#journal Mol. Cell. Biol. (1988) 8:4904-4916 !$#title Intracellular precursors and secretion of alkaline !1extracellular protease of Yarrowia lipolytica. !$#cross-references MUID:89096864; PMID:3211132 !$#accession A31563 !'##molecule_type DNA !'##residues 1-200 ##label MAT CLASSIFICATION #superfamily subtilisin; subtilisin homology KEYWORDS extracellular protein; hydrolase; serine proteinase FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-157 #domain propeptide #status predicted #label PRO\ !$158-454 #product serine proteinase #status predicted #label !8MA2\ !$191-411 #domain subtilisin homology #label SBT\ !$200,231,397 #active_site Asp, His, Ser #status predicted SUMMARY #length 454 #molecular-weight 46906 #checksum 2836 SEQUENCE /// ENTRY S61986 #type complete TITLE subtilisin-like proteinase (EC 3.4.21.-) YSP3 precursor - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein O2517; protein UNC478; protein YOR003w; subtilisin-like proteinase III ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S61986; S66868; S72135 REFERENCE S61981 !$#authors Sterky, F.; Uhlen, M. !$#submission submitted to the EMBL Data Library, December 1995 !$#accession S61986 !'##molecule_type DNA !'##residues 1-478 ##label STE !'##cross-references EMBL:U43491; NID:g1150992; PIDN:AAC49482.1; !1PID:g1150998 REFERENCE S66682 !$#authors Pettersson, B.; Sterky, F.; Uhlen, M. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S66868 !'##molecule_type DNA !'##residues 1-478 ##label PET !'##cross-references EMBL:Z74911; NID:g1420091; PIDN:CAA99191.1; !1PID:g1420092; GSPDB:GN00015; MIPS:YOR003w !'##experimental_source strain S288C REFERENCE S72130 !$#authors Sterky, F.; Holmberg, A.; Pettersson, B.; Uhlen, M. !$#journal Yeast (1996) 12:1091-1095 !$#title The sequence of a 30 kb fragment on the left arm of !1chromosome XV from Saccharomyces cerevisiae reveals 15 open !1reading frames, five of which correspond to previously !1identified genes. !$#cross-references MUID:97051599; PMID:8896276 !$#accession S72135 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-478 ##label STW !'##cross-references EMBL:U43491; NID:g1150992; PIDN:AAC49482.1; !1PID:g1150998 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1995 GENETICS !$#gene SGD:YSP3; MIPS:YOR003w !'##cross-references SGD:S0005529; MIPS:YOR003w !$#map_position 15R CLASSIFICATION #superfamily subtilisin; subtilisin homology KEYWORDS hydrolase; serine proteinase FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-478 #product subtilisin-like proteinase YSP3 #status !8predicted #label MAT\ !$204-421 #domain subtilisin homology #label SBT\ !$213,245,407 #active_site Asp, His, Ser #status predicted SUMMARY #length 478 #molecular-weight 52089 #checksum 1502 SEQUENCE /// ENTRY S19458 #type complete TITLE hypothetical protein YCR045c - yeast (Saccharomyces cerevisiae) ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S19458; S19759 REFERENCE S19396 !$#authors Bolotin-Fukuhara, M.; Buhler, J.M.; Daignan-Fornier, B.; !1Doira, C.; Francingues-Gaillard, M.C.; Iborra, F.; Jacquet, !1M.; Pallier, C.; Raynal, A.; Soustelle, C. !$#submission submitted to the Protein Sequence Database, March 1992 !$#accession S19458 !'##molecule_type DNA !'##residues 1-491 ##label BOL !'##cross-references EMBL:X59720; NID:g1907116; PIDN:CAA42293.1; !1PID:g1907187; GSPDB:GN00003; MIPS:YCR045c REFERENCE S19412 !$#authors Grivell, L.A.; de Haan, M.; Maat, M.J. !$#submission submitted to the Protein Sequence Database, March 1992 !$#accession S19759 !'##molecule_type DNA !'##residues 1-491 ##label GRI !'##cross-references EMBL:X59720; NID:g1907116; PIDN:CAA42293.1; !1PID:g1907187; GSPDB:GN00003; MIPS:YCR045c GENETICS !$#gene MIPS:YCR045c !'##cross-references SGD:S0000641 !$#map_position 3R CLASSIFICATION #superfamily subtilisin; subtilisin homology FEATURE !$165-379 #domain subtilisin homology #label SBT\ !$174,205,365 #active_site Asp, His, Ser #status predicted SUMMARY #length 491 #molecular-weight 55068 #checksum 6305 SEQUENCE /// ENTRY JU0146 #type complete TITLE serine proteinase (EC 3.4.21.-) precursor - Aspergillus niger ORGANISM #formal_name Aspergillus niger DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JU0146 REFERENCE JU0146 !$#authors Frederick, G.D.; Rombouts, P.; Buxton, F.P. !$#journal Gene (1993) 125:57-64 !$#title Cloning and characterisation of pepC, a gene encoding a !1serine protease from Aspergillus niger. !$#cross-references MUID:93194078; PMID:8449413 !$#accession JU0146 !'##molecule_type DNA !'##residues 1-533 ##label FRE !'##cross-references GB:M96758; NID:g289171; PIDN:AAA32702.1; !1PID:g289172 GENETICS !$#gene pepC !$#introns 123/3 CLASSIFICATION #superfamily subtilisin; subtilisin homology KEYWORDS hydrolase; serine proteinase FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-533 #product serine proteinase #status predicted #label !8MAT\ !$172-393 #domain subtilisin homology #label SBT\ !$181,213,379 #active_site Asp, His, Ser #status predicted SUMMARY #length 533 #molecular-weight 56948 #checksum 9249 SEQUENCE /// ENTRY JS0173 #type complete TITLE alkaline proteinase (EC 3.4.21.-) A precursor - Vibrio alginolyticus ALTERNATE_NAMES alkaline serine exoproteinase A ORGANISM #formal_name Vibrio alginolyticus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JS0173 REFERENCE JS0173 !$#authors Deane, S.M.; Robb, F.T.; Robb, S.M.; Woods, D.R. !$#journal Gene (1989) 76:281-288 !$#title Nucleotide sequence of the Vibrio alginolyticus !1calcium-dependent, detergent-resistant alkaline serine !1exoprotease A. !$#cross-references MUID:89326126; PMID:2546861 !$#accession JS0173 !'##molecule_type DNA !'##residues 1-534 ##label DEA !'##cross-references GB:M25499; NID:g155250; PIDN:AAA27550.1; !1PID:g155251 COMMENT This protein is a calcium-dependent and sodium dodecyl !1sulfate-resistant proteinase. CLASSIFICATION #superfamily subtilisin; subtilisin homology KEYWORDS calcium; hydrolase; serine proteinase FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-534 #product alkaline serine proteinase A #status !8predicted #label MAT\ !$171-378 #domain subtilisin homology #label SBT\ !$271-273,297-299 #region S1 specificity crevice #status predicted\ !$180,213,363 #active_site Asp, His, Ser #status predicted SUMMARY #length 534 #molecular-weight 55930 #checksum 5905 SEQUENCE /// ENTRY A35742 #type complete TITLE aqualysin (EC 3.4.21.-) I precursor - Thermus aquaticus ORGANISM #formal_name Thermus aquaticus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A35742; S00620; S00324 REFERENCE A35742 !$#authors Terada, I.; Kwon, S.T.; Miyata, Y.; Matsuzawa, H.; Ohta, T. !$#journal J. Biol. Chem. (1990) 265:6576-6581 !$#title Unique precursor structure of an extracellular protease, !1aqualysin I, with NH-2- and COOH-terminal pro-sequences and !1its processing in Escherichia coli. !$#cross-references MUID:90216674; PMID:2182621 !$#accession A35742 !'##molecule_type DNA !'##residues 1-513 ##label TER !'##cross-references GB:J90108; GB:D90108; GB:J05414; NID:g217171; !1PIDN:BAA14135.1; PID:g217172 !'##note the authors translated the codon CTG for residue 470 as Val, !1and GGT for residue 473 as Ala REFERENCE S00620 !$#authors Kwon, S.T.; Terada, I.; Matsuzawa, H.; Ohta, T. !$#journal Eur. J. Biochem. (1988) 173:491-497 !$#title Nucleotide sequence of the gene for aqualysin I (a !1thermophilic alkaline serine protease) of Thermus aquaticus !1YT-1 and characteristics of the deduced primary structure of !1the enzyme. !$#cross-references MUID:88225062; PMID:3286255 !$#accession S00620 !'##molecule_type DNA !'##residues 75-442 ##label KWO !'##cross-references EMBL:X07734; NID:g48069; PIDN:CAA30559.1; !1PID:g602091 !'##note part of this sequence, including the amino and carboxyl ends of !1the mature protein, was confirmed by protein sequencing REFERENCE S00324 !$#authors Matsuzawa, H.; Tokugawa, K.; Hamaoki, M.; Mizoguchi, M.; !1Taguchi, H.; Terada, I.; Kwon, S.T.; Ohta, T. !$#journal Eur. J. Biochem. (1988) 171:441-447 !$#title Purification and characterization of aqualysin I (a !1thermophilic alkaline serine protease) produced by Thermus !1aquaticus YT-1. !$#cross-references MUID:88151937; PMID:3162211 !$#accession S00324 !'##molecule_type protein !'##residues 128-170 ##label MATS CLASSIFICATION #superfamily subtilisin; subtilisin homology KEYWORDS extracellular protein; hydrolase; serine proteinase FEATURE !$1-14 #domain signal sequence #status predicted #label SIG\ !$15-127 #domain propeptide #status predicted #label PRO\ !$128-408 #product aqualysin I #status experimental #label MAT\ !$157-364 #domain subtilisin homology #label SBT\ !$255-257,281-283 #region S1 specificity crevice #status predicted\ !$409-513 #domain carboxyl-terminal propeptide #status !8predicted #label CPR\ !$166,197,349 #active_site Asp, His, Ser #status predicted SUMMARY #length 513 #molecular-weight 53913 #checksum 2790 SEQUENCE /// ENTRY S52769 #type complete TITLE subtilisin-like proteinase ag12 (EC 3.4.21.-) - alder ORGANISM #formal_name Alnus glutinosa #common_name alder DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-May-2000 ACCESSIONS S52769 REFERENCE S52769 !$#authors Ribeiro, A.; Akkermans, A.D.L.; van Kammen, A.; Bisseling, !1T.; Pawlowski, K. !$#submission submitted to the EMBL Data Library, March 1995 !$#description A nodule-specific gene encoding a subtilisin-like protease !1is involved in early stages of actinorhizal nodule !1development. !$#accession S52769 !'##molecule_type mRNA !'##residues 1-761 ##label RIB !'##cross-references EMBL:X85975; NID:g757521; PIDN:CAA59964.1; !1PID:g757522 GENETICS !$#gene ag12 CLASSIFICATION #superfamily subtilisin-like proteinase ag12; subtilisin !1homology KEYWORDS hydrolase; serine proteinase FEATURE !$136-551 #domain subtilisin homology #status atypical #label !8SBT SUMMARY #length 761 #molecular-weight 81725 #checksum 7432 SEQUENCE /// ENTRY A55800 #type complete TITLE cucumisin (EC 3.4.21.25) precursor - muskmelon ORGANISM #formal_name Cucumis melo #common_name muskmelon DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A55800 REFERENCE A55800 !$#authors Yamagata, H.; Masuzawa, T.; Nagaoka, Y.; Ohnishi, T.; !1Iwasaki, T. !$#journal J. Biol. Chem. (1994) 269:32725-32731 !$#title Cucumisin, a serine protease from melon fruits, shares !1structural homology with subtilisin and is generated from a !1large precursor. !$#cross-references MUID:95105149; PMID:7806492 !$#accession A55800 !'##molecule_type mRNA !'##residues 'LIAKSTT',1-731 ##label YAM !'##cross-references EMBL:D32206 !'##note it is uncertain whether Met-1 is the initiator or whether !1translation is initiated 5' to the sequenced region CLASSIFICATION #superfamily subtilisin-like proteinase ag12; subtilisin !1homology KEYWORDS hydrolase; serine proteinase FEATURE !$1-110 #domain signal sequence and amino-terminal propeptide !8(fragment) #status predicted #label PRO\ !$111-615 #product cucumisin #status predicted #label MAT\ !$131-539 #domain subtilisin homology #status atypical #label !8SBT\ !$616-731 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$615-616 #cleavage_site Thr-Gly (autolytic) #status predicted SUMMARY #length 731 #molecular-weight 78819 #checksum 748 SEQUENCE /// ENTRY C41335 #type complete TITLE microbial serine proteinase (EC 3.4.21.-), intracellular - Bacillus polymyxa ORGANISM #formal_name Bacillus polymyxa DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS C41335 REFERENCE A41335 !$#authors Takekawa, S.; Uozumi, N.; Tsukagoshi, N.; Udaka, S. !$#journal J. Bacteriol. (1991) 173:6820-6825 !$#title Proteases involved in generation of beta- and alpha-amylases !1from a large amylase precursor in Bacillus polymyxa. !$#cross-references MUID:92041565; PMID:1834632 !$#accession C41335 !'##status preliminary !'##molecule_type DNA !'##residues 1-326 ##label TAK !'##cross-references GB:D00862; NID:g216285; PIDN:BAA00735.1; !1PID:g216286 CLASSIFICATION #superfamily Bacillus intracellular serine proteinase; !1subtilisin homology KEYWORDS hydrolase; serine proteinase FEATURE !$40-258 #domain subtilisin homology #label SBT\ !$49,86,244 #active_site Asp, His, Ser #status predicted SUMMARY #length 326 #molecular-weight 35173 #checksum 8812 SEQUENCE /// ENTRY S27501 #type complete TITLE alkaline proteinase (EC 3.4.21.-), intracellular - Bacillus sp. (strain 221) ORGANISM #formal_name Bacillus sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S27501 REFERENCE S27501 !$#authors Kato, C.; Nakano, Y.; Yamamoto, M.; Horikoshi, K. !$#submission submitted to the EMBL Data Library, March 1992 !$#description Cloning and nucleotide sequence of the intracellular !1alkaline protease gene of alkaliphilic Bacillus sp. strain !1221. !$#accession S27501 !'##molecule_type DNA !'##residues 1-321 ##label KAT !'##cross-references EMBL:D10730; NID:g216233; PIDN:BAA01573.1; !1PID:g216234 CLASSIFICATION #superfamily Bacillus intracellular serine proteinase; !1subtilisin homology KEYWORDS hydrolase; serine proteinase FEATURE !$40-264 #domain subtilisin homology #label SBT\ !$49,86,250 #active_site Asp, His, Ser #status predicted SUMMARY #length 321 #molecular-weight 33747 #checksum 877 SEQUENCE /// ENTRY SUBSMP #type complete TITLE serine proteinase (EC 3.4.21.-) epr precursor - Bacillus subtilis ALTERNATE_NAMES minor extracellular serine proteinase epr ORGANISM #formal_name Bacillus subtilis DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jun-2000 ACCESSIONS S11504; S20207; A31386; S39670; C69620 REFERENCE S11504 !$#authors Brueckner, R.; Shoseyov, O.; Doi, R.H. !$#journal Mol. Gen. Genet. (1990) 221:486-490 !$#title Multiple active forms of a novel serine protease from !1Bacillus subtilis. !$#cross-references MUID:90340301; PMID:2116590 !$#accession S11504 !'##molecule_type DNA !'##residues 1-645 ##label BRU !'##cross-references EMBL:X53307; NID:g39899; PIDN:CAA37392.1; !1PID:g39900 !$#accession S20207 !'##molecule_type protein !'##residues 'XXX',107-113 ##label BR2 REFERENCE A31386 !$#authors Sloma, A.; Ally, A.; Ally, D.; Pero, J. !$#journal J. Bacteriol. (1988) 170:5557-5563 !$#title Gene encoding a minor extracellular protease in Bacillus !1subtilis. !$#cross-references MUID:89053875; PMID:3142851 !$#accession A31386 !'##molecule_type DNA !'##residues 1-645 ##label SLO !'##cross-references GB:M22407; NID:g142893; PIDN:AAA22423.1; !1PID:g142894 REFERENCE S39655 !$#authors Glaser, P.; Kunst, F.; Arnaud, M.; Coudart, M.P.; Gonzales, !1W.; Hullo, M.F.; Ionescu, M.; Lubochinsky, B.; Marcelino, !1L.; Moszer, I.; Presecan, E.; Santana, M.; Schneider, E.; !1Schweizer, J.; Vertes, A.; Rapoport, G.; Danchin, A. !$#journal Mol. Microbiol. (1993) 10:371-384 !$#title Bacillus subtilis genome project: cloning and sequencing of !1the 97 kb region from 325 degrees to 333 degrees. !$#cross-references MUID:95020537; PMID:7934828 !$#accession S39670 !'##molecule_type DNA !'##residues 1-645 ##label GLA !'##cross-references EMBL:X73124; NID:g413923; PIDN:CAA51571.1; !1PID:g413939 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69620 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-645 ##label KUN !'##cross-references GB:Z99123; GB:AL009126; NID:g2636240; !1PIDN:CAB15866.1; PID:g2636375 !'##experimental_source strain 168 GENETICS !$#gene epr CLASSIFICATION #superfamily serine proteinase epr; subtilisin homology KEYWORDS extracellular protein; hydrolase; serine proteinase FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-103 #domain propeptide #status predicted #label PRO\ !$104-645 #product serine proteinase epr #status experimental !8#label MAT\ !$133-340 #domain subtilisin homology #label SBT\ !$142,172,326 #active_site Asp, His, Ser #status predicted SUMMARY #length 645 #molecular-weight 69695 #checksum 3384 SEQUENCE /// ENTRY SUSEMM #type complete TITLE serine proteinase (EC 3.4.21.-) precursor - Serratia marcescens (strain RH1) ORGANISM #formal_name Serratia marcescens DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 18-Jun-1999 ACCESSIONS S19882 REFERENCE S19882 !$#authors Lee, S.; Kim, J.; Kho, Y.; Rho, H. !$#submission submitted to the EMBL Data Library, February 1992 !$#description Cloning and nucleotide sequence of the alkaline protease !1gene from Serratia marcescens RH1. !$#accession S19882 !'##molecule_type DNA !'##residues 1-1045 ##label LEE !'##cross-references EMBL:X59719; NID:g47260; PIDN:CAA42236.1; !1PID:g47261 CLASSIFICATION #superfamily Serratia serine proteinase; subtilisin homology KEYWORDS hydrolase; serine proteinase FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-407 #product serine proteinase #status predicted #label !8MAT\ !$67-354 #domain subtilisin homology #label SBT\ !$408-1045 #domain carboxyl-terminal propeptide #status !8predicted #label PRO\ !$76,112,341 #active_site Asp, His, Ser #status predicted SUMMARY #length 1045 #molecular-weight 112728 #checksum 6005 SEQUENCE /// ENTRY A36734 #type complete TITLE bacillopeptidase F (EC 3.4.21.-) precursor bpr [validated] - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 19-May-2000 #sequence_revision 19-May-2000 #text_change 16-Jun-2000 ACCESSIONS A36734; A35131; A35750; B35750; S08223; JN0335; I39849; !1B69596; JU0084 REFERENCE A36734 !$#authors Sloma, A.; Rufo Jr., G.A.; Rudolph, C.F.; Sullivan, B.J.; !1Theriault, K.A.; Pero, J. !$#journal J. Bacteriol. (1990) 172:5520-5521 !$#cross-references MUID:90368623; PMID:2118514 !$#contents erratum !$#accession A36734 !'##molecule_type DNA !'##residues 1-1433 ##label SLO !'##cross-references GB:M29035; NID:g143307; PIDN:AAA62679.1; !1PID:g143308 REFERENCE A35131 !$#authors Sloma, A.; Rufo Jr., G.A.; Rudolph, C.F.; Sullivan, B.J.; !1Theriault, K.A.; Pero, J. !$#journal J. Bacteriol. (1990) 172:1470-1477 !$#title Bacillopeptidase F of Bacillus subtilis: purification of the !1protein and cloning of the gene. !$#cross-references MUID:90170864; PMID:2106512 !$#accession A35131 !'##molecule_type DNA !'##residues 1-365,'S',367-682,'EIMP',893,'Q',895-896 ##label SL2 !'##cross-references GB:M29035 !'##note the authors translated the codon GAA for residue 545 as Leu REFERENCE A35750 !$#authors Wu, X.C.; Nathoo, S.; Pang, A.S.H.; Carne, T.; Wong, S.L. !$#journal J. Biol. Chem. (1990) 265:6845-6850 !$#title Cloning, genetic organization, and characterization of a !1structural gene encoding bacillopeptidase F from Bacillus !1subtilis. !$#cross-references MUID:90216713; PMID:2108961 !$#accession A35750 !'##molecule_type DNA !'##residues 1-392,'V',394-828,'NIRTRLYSLKFCRSRHKSV' ##label WUA !'##cross-references GB:J05400; NID:g142607; PIDN:AAA83362.1; !1PID:g142609 !'##note this sequence has been corrected !$#accession B35750 !'##molecule_type DNA !'##residues 876-935,'CG' ##label WU2 !'##cross-references GB:J05400; NID:g142607; PIDN:AAA83363.1; !1PID:g1119197 !'##note this sequence has been corrected REFERENCE S08223 !$#authors Masuda, E.S.; Anaguchi, H.; Sato, T.; Takeuchi, M.; !1Kobayashi, Y. !$#journal Nucleic Acids Res. (1990) 18:657 !$#title Nucleotide sequence of the sporulation gene spoIIGA from !1Bacillus subtilis. !$#cross-references MUID:90174995; PMID:2106671 !$#accession S08223 !'##molecule_type DNA !'##residues 1410-1433 ##label MAS !'##cross-references EMBL:X17344; NID:g40165; PIDN:CAA35224.1; !1PID:g809661 REFERENCE JN0335 !$#authors Kato, T.; Yamagata, Y.; Arai, T.; Ichishima, E. !$#journal Biosci. Biotechnol. Biochem. (1992) 56:1166-1168 !$#title Purification of a new extracellular 90-kDa serine proteinase !1with isoelectric point of 3.9 from Bacillus subtilis (natto) !1and elucidation of its distinct mode of action. !$#cross-references MUID:93005071; PMID:1368833 !$#accession JN0335 !'##molecule_type protein !'##residues 195-218,'A' ##label KAT !'##note source of this material was Bacillus subtilis (natto) REFERENCE I39846 !$#authors Beall, B.; Lowe, M.; Lutkenhaus, J. !$#journal J. Bacteriol. (1988) 170:4855-4864 !$#title Cloning and characterization of Bacillus subtilis homologs !1of Escherichia coli cell division genes ftsZ and ftsA. !$#cross-references MUID:89008108; PMID:3139638 !$#accession I39849 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-211 ##label RES !'##cross-references GB:M22630; NID:g142938; PIDN:AAA22458.1; !1PID:g551705 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69596 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1433 ##label KUN !'##cross-references GB:Z99111; GB:Z99112; GB:AL009126; NID:g2633902; !1PIDN:CAB13404.1; PID:g2633903; NID:g2633699; PID:g2633901 !'##experimental_source strain 168 GENETICS !$#gene bpr; bpf !$#map_position 135 (degrees) CLASSIFICATION #superfamily bacillopeptidase F; subtilisin homology KEYWORDS extracellular protein; hydrolase; serine proteinase FEATURE !$1-30 #domain signal sequence #status predicted #label SIG\ !$31-194 #domain propeptide #status predicted #label PRO\ !$195-1433 #product bacillopeptidase F #status experimental !8#label MAT\ !$218-466 #domain subtilisin homology #label SBT\ !$227,274,452 #active_site Asp, His, Ser #status predicted SUMMARY #length 1433 #molecular-weight 154577 #checksum 3073 SEQUENCE /// ENTRY B44858 #type complete TITLE lactocepin (EC 3.4.21.96) precursor [validated] - Lactobacillus paracasei (strain NCDO 151) ALTERNATE_NAMES cell-envelope-associated proteinase prtP; serine proteinase Lp151 ORGANISM #formal_name Lactobacillus paracasei DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-May-2000 ACCESSIONS B44858; C44858; A44850 REFERENCE A44858 !$#authors Holck, A.; Naes, H. !$#journal J. Gen. Microbiol. (1992) 138:1353-1364 !$#title Cloning, sequencing and expression of the gene encoding the !1cell-envelope-associated proteinase from Lactobacillus !1paracasei subsp. paracasei NCDO 151. !$#cross-references MUID:92381481; PMID:1512565 !$#accession B44858 !'##molecule_type DNA !'##residues 1-1902 ##label HOL1 !'##cross-references GB:M83946; NID:g149580; PIDN:AAA25248.1; !1PID:g149582 !'##note sequence extracted from NCBI backbone (NCBIN:112261, !1NCBIP:112263) !'##note the source is designated as Lactobacillus paracasei subsp. !1paracasei !$#accession C44858 !'##molecule_type protein !'##residues 'X',189-196 ##label HOL2 REFERENCE A44850 !$#authors Naes, H.; Nissen-Meyer, J. !$#journal J. Gen. Microbiol. (1992) 138:313-318 !$#title Purification and N-terminal amino acid sequence !1determination of the cell-wall-bound proteinase from !1Lactobacillus paracasei subsp. paracasei. !$#cross-references MUID:92226694; PMID:1564442 !$#accession A44850 !'##status preliminary !'##molecule_type protein !'##residues 189-196 ##label NAE !'##cross-references PIDN:AAB22052.1; PID:g248666 !'##experimental_source strain NCDO 151 !'##note sequence extracted from NCBI backbone (NCBIP:94706) GENETICS !$#gene prtP CLASSIFICATION #superfamily lactocepin; subtilisin homology KEYWORDS hydrolase; serine proteinase; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$23-187 #domain propeptide #status predicted #label PRO\ !$188-1902 #product serine proteinase, cell-envelope-associated !8#status experimental #label MAT\ !$208-634 #domain subtilisin homology #status atypical #label !8SBT SUMMARY #length 1902 #molecular-weight 200252 #checksum 208 SEQUENCE /// ENTRY SWQPA1 #type complete TITLE serotype-specific antigen (EC 3.4.21.-) precursor - Pasteurella haemolytica (strain A1) ALTERNATE_NAMES Ssa1 ORGANISM #formal_name Pasteurella haemolytica DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 18-Jun-1999 ACCESSIONS A43608 REFERENCE A43608 !$#authors Lo, R.Y.C.; Strathdee, C.A.; Shewen, P.E.; Cooney, B.J. !$#journal Infect. Immun. (1991) 59:3398-3406 !$#title Molecular studies of Ssa1, a serotype-specific antigen of !1Pasteurella haemolytica A1. !$#cross-references MUID:91372942; PMID:1840576 !$#accession A43608 !'##molecule_type DNA !'##residues 1-932 ##label LOA !'##cross-references GB:M62363; NID:g150517; PIDN:AAA25549.1; !1PID:g150518 COMMENT This plasmid-encoded protein is found in the outer membrane. CLASSIFICATION #superfamily Pasteurella haemolytica A1 serotype-specific !1antigen; subtilisin homology KEYWORDS hydrolase; membrane protein; serine proteinase FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-932 #product serotype-specific antigen #status predicted !8#label MAT\ !$49-365 #domain subtilisin homology #label SBT\ !$58,116,351 #active_site Asp, His, Ser #status predicted SUMMARY #length 932 #molecular-weight 103590 #checksum 6690 SEQUENCE /// ENTRY A35066 #type complete TITLE streptococcal C5a peptidase (EC 3.4.21.-) precursor - Streptococcus pyogenes ORGANISM #formal_name Streptococcus pyogenes DATE 13-Nov-1998 #sequence_revision 13-Nov-1998 #text_change 18-Jun-1999 ACCESSIONS A35066; S52539 REFERENCE A35066 !$#authors Chen, C.C.; Cleary, P.P. !$#journal J. Biol. Chem. (1990) 265:3161-3167 !$#title Complete nucleotide sequence of the streptococcal C5a !1peptidase gene of Streptococcus pyogenes. !$#cross-references MUID:90153964; PMID:2406246 !$#accession A35066 !'##molecule_type DNA !'##residues 1-1167 ##label CHE !'##cross-references GB:J05229; NID:g153776; PIDN:AAA26960.1; !1PID:g552009 !'##note the amino end of the mature protein was determined by protein !1sequencing REFERENCE S52535 !$#authors Katerov, V.; Schalen, C.; Totolian, A.A. !$#journal Mol. Gen. Genet. (1994) 245:78-85 !$#title Sequencing of genes within the vir regulon of Streptococcus !1pyogenes type M15 - an opacity factor-positive serotype with !1low opacity factor expression. !$#cross-references MUID:95147851; PMID:7845360 !$#accession S52539 !'##status preliminary !'##molecule_type DNA !'##residues 1-75,'V',77-78,'K',80-83,'PS' ##label KAT !'##cross-references GB:S75411; NID:g914107; PIDN:AAB33264.1; !1PID:g914112 !'##note in Genbank entry S75411, release 106.0, the initiation codon !1TTG for residue 1 is translated as Leu GENETICS !$#gene scpA !$#start_codon TTG FUNCTION !$#description specifically cleaves a Lys-Asp peptide bond near the !1carboxyl end of human C5a anaphylatoxin, destroying its !1chemoattractant activity CLASSIFICATION #superfamily streptococcal C5a peptidase; subtilisin !1homology KEYWORDS cell wall; hydrolase; serine proteinase; tandem repeat; !1transmembrane protein FEATURE !$1-31 #domain signal sequence #status predicted #label SIG\ !$32-1167 #product streptococcal C5a peptidase #status !8predicted #label MAT\ !$121-526 #domain subtilisin homology #status atypical #label !8SBT\ !$1029-1139 #domain cell wall spanning #status predicted #label !8CWS\ !$1034-1101 #region glycine/proline-rich 17-residue repeats\ !$1040-1157 #domain transmembrane #status predicted #label TMM\ !$130,193,512 #active_site Asp, His, Ser #status predicted SUMMARY #length 1167 #molecular-weight 128263 #checksum 1473 SEQUENCE /// ENTRY PRAISB #type complete TITLE serine proteinase, calcium-dependent (EC 3.4.21.-) - Anabaena variabilis ORGANISM #formal_name Anabaena variabilis DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jul-1999 ACCESSIONS S13335; A38816 REFERENCE S13335 !$#authors Maldener, I.; Lockau, W.; Cai, Y.; Wolk, C.P. !$#journal Mol. Gen. Genet. (1991) 225:113-120 !$#title Calcium-dependent protease of the cyanobacterium Anabaena: !1molecular cloning and expression of the gene in Escherichia !1coli, sequencing and site-directed mutagenesis. !$#cross-references MUID:91155923; PMID:1900347 !$#accession S13335 !'##molecule_type DNA !'##residues 1-477 ##label MAL !'##cross-references EMBL:X56955 !$#accession A38816 !'##molecule_type protein !'##residues 192-205;258-262 ##label MA2 GENETICS !$#gene prcA CLASSIFICATION #superfamily serine proteinase, calcium-dependent; !1subtilisin homology KEYWORDS calcium; hydrolase; serine proteinase FEATURE !$224-446 #domain subtilisin homology #label SBT\ !$231-243 #domain calcium binding #status predicted #label CAL SUMMARY #length 477 #molecular-weight 51960 #checksum 4207 SEQUENCE /// ENTRY S68421 #type complete TITLE endopeptidase Clp (EC 3.4.21.92) chain P [similarity] - human ALTERNATE_NAMES proteinase CLPP ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 08-Dec-2000 ACCESSIONS S68421; S61216 REFERENCE S68421 !$#authors Bross, P.; Andresen, B.S.; Knudsen, I.; Kruse, T.A.; !1Gregersen, N. !$#journal FEBS Lett. (1995) 377:249-252 !$#title Human ClpP protease: cDNA sequence, tissue-specific !1expression and chromosomal assignment of the gene. !$#cross-references MUID:96128239; PMID:8543061 !$#accession S68421 !'##molecule_type mRNA !'##residues 1-277 ##label BRO !'##cross-references EMBL:Z50853; NID:g963047; PIDN:CAA90705.1; !1PID:g963048 GENETICS !$#gene GDB:CLPP !'##cross-references GDB:9954598; OMIM:601119 !$#map_position 19pter-19qter !$#genome nuclear FUNCTION !$#description ATP-driven cleavage of proteins to small peptides !$#note magnesium required CLASSIFICATION #superfamily endopeptidase Clp chain P KEYWORDS ATP; hydrolase; mitochondrion; protein degradation; serine !1proteinase FEATURE !$153,178 #active_site Ser, His #status predicted SUMMARY #length 277 #molecular-weight 30180 #checksum 5957 SEQUENCE /// ENTRY B36575 #type complete TITLE endopeptidase Clp (EC 3.4.21.92) chain P [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES heat shock protein F21.5 ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS B36575; E64773 REFERENCE A36575 !$#authors Maurizi, M.R.; Clark, W.P.; Katayama, Y.; Rudikoff, S.; !1Pumphrey, J.; Bowers, B.; Gottesman, S. !$#journal J. Biol. Chem. (1990) 265:12536-12545 !$#title Sequence and structure of Clp P, the proteolytic component !1of the ATP-dependent Clp protease of Escherichia coli. !$#cross-references MUID:90324245; PMID:2197275 !$#accession B36575 !'##status preliminary !'##molecule_type DNA !'##residues 1-207 ##label MAU !'##cross-references GB:J05534; NID:g145554; PIDN:AAA23588.1; !1PID:g145556 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64773 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-207 ##label BLAT !'##cross-references GB:AE000150; GB:U00096; NID:g1786639; !1PIDN:AAC73540.1; PID:g1786641; UWGP:b0437 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene clpP; lopP COMPLEX heterodimer; proteolytic chain (clpP) and an ATP-binding !1regulatory chain; regulatory chain isoforms are clpA and !1clpX FUNCTION !$#description ATP-driven cleavage of proteins to small peptides !$#note clpP is the proteolytic component of clp proteinase !$#note magnesium required CLASSIFICATION #superfamily endopeptidase Clp chain P KEYWORDS ATP; heat shock; heterodimer; hydrolase; serine proteinase FEATURE !$111,136 #active_site Ser, His #status predicted SUMMARY #length 207 #molecular-weight 23186 #checksum 6038 SEQUENCE /// ENTRY D64088 #type complete TITLE endopeptidase Clp (EC 3.4.21.92) chain P [similarity] - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 08-Dec-2000 ACCESSIONS D64088 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession D64088 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-193 ##label TIGR !'##cross-references GB:U32754; GB:L42023; NID:g1573711; !1PIDN:AAC22371.1; PID:g1573716; TIGR:HI0714 GENETICS !$#gene clpP FUNCTION !$#description ATP-driven cleavage of proteins to small peptides !$#note magnesium required CLASSIFICATION #superfamily endopeptidase Clp chain P KEYWORDS ATP; hydrolase; serine proteinase FEATURE !$98,123 #active_site Ser, His #status predicted SUMMARY #length 193 #molecular-weight 21372 #checksum 17 SEQUENCE /// ENTRY S12408 #type complete TITLE endopeptidase Clp (EC 3.4.21.92) chain P [similarity] - wheat chloroplast ORGANISM #formal_name chloroplast Triticum aestivum #common_name common wheat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 08-Dec-2000 ACCESSIONS S12408 REFERENCE S12407 !$#authors Gray, J.C.; Hird, S.M.; Dyer, T.A. !$#journal Plant Mol. Biol. (1990) 15:947-950 !$#title Nucleotide sequence of a wheat chloroplast gene encoding the !1proteolytic subunit of an ATP-dependent protease. !$#cross-references MUID:91355920; PMID:2103485 !$#accession S12408 !'##molecule_type DNA !'##residues 1-216 ##label GRA !'##cross-references EMBL:X54484; NID:g12334; PIDN:CAA38354.1; !1PID:g12336 !'##experimental_source cv. Mardler !'##note the authors translated the codon ACG for residue 44 as Arg GENETICS !$#gene clpP !$#genome chloroplast FUNCTION !$#description ATP-driven cleavage of proteins to small peptides !$#note magnesium required CLASSIFICATION #superfamily endopeptidase Clp chain P KEYWORDS ATP; chloroplast; hydrolase; serine proteinase FEATURE !$101,126 #active_site Ser, His #status predicted SUMMARY #length 216 #molecular-weight 24881 #checksum 8981 SEQUENCE /// ENTRY JQ0251 #type complete TITLE endopeptidase Clp (EC 3.4.21.92) chain P [similarity] - rice chloroplast ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 08-Dec-2000 ACCESSIONS JQ0251; S05131 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0251 !'##molecule_type DNA !'##residues 1-216 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05131 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-216 ##label HIR !'##cross-references GB:X15901; NID:g11957; PIDN:CAA33972.1; PID:g12012 !'##experimental_source cv. Nihonbare !'##note this sequence was submitted to EMBL, July 1989 GENETICS !$#genome chloroplast FUNCTION !$#description ATP-driven cleavage of proteins to small peptides !$#note magnesium required CLASSIFICATION #superfamily endopeptidase Clp chain P KEYWORDS ATP; chloroplast; hydrolase; serine proteinase FEATURE !$101,126 #active_site Ser, His #status predicted SUMMARY #length 216 #molecular-weight 24714 #checksum 9653 SEQUENCE /// ENTRY S50763 #type complete TITLE endopeptidase Clp (EC 3.4.21.92) chain P [similarity] - shore pine chloroplast ALTERNATE_NAMES ATP-dependent proteinase proteolytic chain ORGANISM #formal_name chloroplast Pinus contorta #common_name shore pine DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 08-Dec-2000 ACCESSIONS S50763 REFERENCE S50763 !$#authors Clarke, A.K.; Gustafsson, P.; Lidholm, J.A. !$#journal Plant Mol. Biol. (1994) 26:851-862 !$#title Identification and expression of the chloroplast clpP gene !1in the conifer Pinus contorta. !$#cross-references MUID:95093026; PMID:7999999 !$#accession S50763 !'##molecule_type DNA !'##residues 1-205 ##label CLA !'##cross-references EMBL:L28807; NID:g457147; PIDN:AAA68094.1; !1PID:g457148 !'##experimental_source tissue needles !'##note the authors translated the codon TAT for residue 81 as Phe and !1CGT for residue 82 as Asp GENETICS !$#gene clpP !$#genome chloroplast FUNCTION !$#description ATP-driven cleavage of proteins to small peptides !$#note magnesium required CLASSIFICATION #superfamily endopeptidase Clp chain P KEYWORDS ATP; chloroplast; hydrolase; serine proteinase FEATURE !$101,126 #active_site Ser, His #status predicted SUMMARY #length 205 #molecular-weight 22922 #checksum 2480 SEQUENCE /// ENTRY S58576 #type complete TITLE endopeptidase Clp (EC 3.4.21.92) chain P [similarity] - maize chloroplast ORGANISM #formal_name chloroplast Zea mays #common_name maize DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 08-Dec-2000 ACCESSIONS S58576; S19126; S16733 REFERENCE S58531 !$#authors Maier, R.M.; Neckermann, K.; Igloi, G.L.; Koessel, H. !$#journal J. Mol. Biol. (1995) 251:614-628 !$#title Complete sequence of the maize chloroplast genome: gene !1content, hotspots of divergence and fine tuning of genetic !1information by transcript editing. !$#cross-references MUID:95395841; PMID:7666415 !$#accession S58576 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-216 ##label MAI !'##cross-references EMBL:X86563; NID:g902200; PIDN:CAA60310.1; !1PID:g902246 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1995 REFERENCE S19126 !$#authors Wegloehner, W.; Subramanian, A.R. !$#journal Plant Mol. Biol. (1992) 18:415-418 !$#title Nucleotide sequence of a region of maize chloroplast DNA !1containing the 3' end of clpP, exon 1 of rps12 and rpl20 and !1their cotranscription. !$#cross-references MUID:92119264; PMID:1732000 !$#accession S19126 !'##molecule_type DNA !'##residues 186-216 ##label WEG !'##cross-references EMBL:X60548; NID:g12413; PIDN:CAA43038.1; !1PID:g12414 GENETICS !$#gene clpP !$#genome chloroplast FUNCTION !$#description ATP-driven cleavage of proteins to small peptides !$#note magnesium required CLASSIFICATION #superfamily endopeptidase Clp chain P KEYWORDS ATP; chloroplast; hydrolase; serine proteinase FEATURE !$101,126 #active_site Ser, His #status predicted SUMMARY #length 216 #molecular-weight 24758 #checksum 7519 SEQUENCE /// ENTRY A05056 #type complete TITLE endopeptidase Clp (EC 3.4.21.92) chain P [similarity] - liverwort (Marchantia polymorpha) chloroplast ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 08-Dec-2000 ACCESSIONS S01545; A05056 REFERENCE S01529 !$#authors Fukuzawa, H.; Kohchi, T.; Sano, T.; Shirai, H.; Umesono, K.; !1Inokuchi, H.; Ozeki, H.; Ohyama, K. !$#journal J. Mol. Biol. (1988) 203:333-351 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. III. Gene organization of the large !1single copy region from rbcL to trnI(CAU). !$#cross-references MUID:89068687; PMID:3199436 !$#accession S01545 !'##molecule_type DNA !'##residues 1-203 ##label FUK !'##cross-references EMBL:X04465; NID:g11640; PIDN:CAA28109.1; !1PID:g456519 REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features GENETICS !$#genome chloroplast !$#introns 24/2; 121/3 FUNCTION !$#description ATP-driven cleavage of proteins to small peptides !$#note magnesium required CLASSIFICATION #superfamily endopeptidase Clp chain P KEYWORDS ATP; chloroplast; hydrolase; serine proteinase FEATURE !$101,126 #active_site Ser, His #status predicted SUMMARY #length 203 #molecular-weight 22685 #checksum 7886 SEQUENCE /// ENTRY SUECCA #type complete TITLE endopeptidase Clp (EC 3.4.21.-) ATP-binding chain clpA [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES ATP-dependent Clp proteinase regulatory chain A; ATP-dependent proteinase ATP-binding protein CONTAINS adenosinetriphosphatase (EC 3.6.1.3) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS B64827; A35365; PS0229; A31985; F35905 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64827 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-758 ##label BLAT !'##cross-references GB:AE000190; GB:U00096; NID:g1787106; !1PIDN:AAC73969.1; PID:g1787109; UWGP:b0882 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A35365 !$#authors Gottesman, S.; Clark, W.P.; Maurizi, M.R. !$#journal J. Biol. Chem. (1990) 265:7886-7893 !$#title The ATP-dependent Clp protease of Escherichia coli. Sequence !1of clpA and identification of a Clp-specific substrate. !$#cross-references MUID:90243657; PMID:2186030 !$#accession A35365 !'##molecule_type DNA !'##residues 1-366,'G',368-410,'V',412-532,'V',534-758 ##label GOT !'##cross-references GB:M31045; NID:g145548; PIDN:AAA23583.1; !1PID:g145549 !'##experimental_source strain K-12 REFERENCE PS0228 !$#authors Cummings, H.S.; Sands, J.F.; Foreman, P.C.; Fraser, J.; !1Hershey, J.W.B. !$#journal J. Biol. Chem. (1991) 266:16491-16498 !$#title Structure and expression of the infA operon encoding !1translational initiation factor IF1. Transcriptional control !1by growth rate. !$#cross-references MUID:91358434; PMID:1909328 !$#accession PS0229 !'##molecule_type DNA !'##residues 511-758 ##label CUM REFERENCE A31985 !$#authors Katayama, Y.; Gottesman, S.; Pumphrey, J.; Rudikoff, S.; !1Clark, W.P.; Maurizi, M.R. !$#journal J. Biol. Chem. (1988) 263:15226-15236 !$#title The two-component, ATP-dependent Clp protease of Escherichia !1coli. Purification, cloning, and mutational analysis of the !1ATP-binding component. !$#cross-references MUID:89008411; PMID:3049606 !$#accession A31985 !'##molecule_type protein !'##residues 1-28 ##label KAT !'##experimental_source strain SG1110 GENETICS !$#gene clpA; lopD !$#map_position 19 min COMPLEX heterodimer; proteolytic chain (clpP) and an ATP-binding !1regulatory chain; regulatory chain isoforms are clpA and !1clpX FUNCTION !$#description allows clpP to hydrolyze polypeptides and proteins, probably !1by a chaperone-like activity that makes protein substrates !1more accessible to the clpP active site; independently has !1ATPase activity; ATP hydrolysis is required for Clp !1hydrolysis of proteins but not of smaller polypeptides CLASSIFICATION #superfamily endopeptidase Clp ATP-binding chain KEYWORDS ATP; heat shock; heterodimer; hydrolase; molecular !1chaperone; nucleotide binding; P-loop; serine proteinase FEATURE !$214-221 #region nucleotide-binding motif A (P-loop)\ !$281-285 #region nucleotide-binding motif B\ !$495-502 #region nucleotide-binding motif A (P-loop)\ !$560-564 #region nucleotide-binding motif B\ !$220 #binding_site ATP (Lys) #status predicted\ !$501 #binding_site ATP (Lys) #status predicted SUMMARY #length 758 #molecular-weight 84206 #checksum 9906 SEQUENCE /// ENTRY SURFCA #type complete TITLE endopeptidase Clp (EC 3.4.21.-) ATP-binding chain A [similarity] - Rhodopseudomonas blastica ALTERNATE_NAMES ATP-dependent Clp proteinase regulatory chain A CONTAINS adenosinetriphosphatase (EC 3.6.1.3) ORGANISM #formal_name Rhodopseudomonas blastica DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 19-Jan-2001 ACCESSIONS S04667 REFERENCE S04666 !$#authors Tybulewicz, V.L.J.; Falk, G.; Walker, J.E. !$#journal J. Mol. Biol. (1984) 179:185-214 !$#title Rhodopseudomonas blastica atp operon. Nucleotide sequence !1and transcription. !$#cross-references MUID:85058188; PMID:6209404 !$#accession S04667 !'##molecule_type DNA !'##residues 1-793 ##label TYB FUNCTION !$#description allows clpP to hydrolyze polypeptides and proteins, probably !1by a chaperone-like activity that makes protein substrates !1more accessible to the clpP active site; independently has !1ATPase activity; ATP hydrolysis is required for Clp !1hydrolysis of proteins but not of smaller polypeptides CLASSIFICATION #superfamily endopeptidase Clp ATP-binding chain KEYWORDS ATP; hydrolase; molecular chaperone; nucleotide binding; !1P-loop; serine proteinase FEATURE !$244-251 #region nucleotide-binding motif A (P-loop)\ !$311-315 #region nucleotide-binding motif B\ !$525-532 #region nucleotide-binding motif A (P-loop)\ !$590-594 #region nucleotide-binding motif B\ !$250 #binding_site ATP (Lys) #status predicted\ !$531 #binding_site ATP (Lys) #status predicted SUMMARY #length 793 #molecular-weight 86890 #checksum 4832 SEQUENCE /// ENTRY A35905 #type complete TITLE endopeptidase Clp (EC 3.4.21.-) ATP-binding chain cd4A, chloroplast [similarity] - tomato ALTERNATE_NAMES ATP-dependent Clp proteinase regulatory chain A; CD4A protein CONTAINS adenosinetriphosphatase (EC 3.6.1.3) ORGANISM #formal_name Lycopersicon esculentum #common_name tomato DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 19-Jan-2001 ACCESSIONS A35905 REFERENCE A35905 !$#authors Gottesman, S.; Squires, C.; Pichersky, E.; Carrington, M.; !1Hobbs, M.; Mattick, J.S.; Dalrymple, B.; Kuramitsu, H.; !1Shiroza, T.; Foster, T.; Clark, W.P.; Ross, B.; Squires, !1C.L.; Maurizi, M.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:3513-3517 !$#title Conservation of the regulatory subunit for the Clp !1ATP-dependent protease in prokaryotes and eukaryotes. !$#cross-references MUID:90239044; PMID:2185473 !$#accession A35905 !'##molecule_type DNA !'##residues 1-926 ##label GOT !'##cross-references GB:M32603; NID:g170432; PIDN:AAA34160.1; !1PID:g170433 GENETICS !$#gene cd4A !$#map_position 3 FUNCTION !$#description allows clpP to hydrolyze polypeptides and proteins, probably !1by a chaperone-like activity that makes protein substrates !1more accessible to the clpP active site; independently has !1ATPase activity; ATP hydrolysis is required for Clp !1hydrolysis of proteins but not of smaller polypeptides CLASSIFICATION #superfamily endopeptidase Clp ATP-binding chain KEYWORDS ATP; chloroplast; hydrolase; molecular chaperone; nucleotide !1binding; P-loop; serine proteinase FEATURE !$302-309 #region nucleotide-binding motif A (P-loop)\ !$367-371 #region nucleotide-binding motif B\ !$646-653 #region nucleotide-binding motif A (P-loop)\ !$711-715 #region nucleotide-binding motif B\ !$308 #binding_site ATP (Lys) #status predicted\ !$652 #binding_site ATP (Lys) #status predicted SUMMARY #length 926 #molecular-weight 102556 #checksum 9330 SEQUENCE /// ENTRY B35905 #type complete TITLE endopeptidase Clp (EC 3.4.21.-) ATP-binding chain cd4B, chloroplast [similarity] - tomato ALTERNATE_NAMES ATP-dependent Clp proteinase regulatory chain B; CD4B protein CONTAINS adenosinetriphosphatase (EC 3.6.1.3) ORGANISM #formal_name Lycopersicon esculentum #common_name tomato DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 19-Jan-2001 ACCESSIONS B35905 REFERENCE A35905 !$#authors Gottesman, S.; Squires, C.; Pichersky, E.; Carrington, M.; !1Hobbs, M.; Mattick, J.S.; Dalrymple, B.; Kuramitsu, H.; !1Shiroza, T.; Foster, T.; Clark, W.P.; Ross, B.; Squires, !1C.L.; Maurizi, M.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:3513-3517 !$#title Conservation of the regulatory subunit for the Clp !1ATP-dependent protease in prokaryotes and eukaryotes. !$#cross-references MUID:90239044; PMID:2185473 !$#accession B35905 !'##molecule_type DNA !'##residues 1-923 ##label GOT !'##cross-references GB:M32604; NID:g170434; PIDN:AAA34161.1; !1PID:g170435 GENETICS !$#gene cd4B !$#map_position 12 FUNCTION !$#description allows clpP to hydrolyze polypeptides and proteins, probably !1by a chaperone-like activity that makes protein substrates !1more accessible to the clpP active site; independently has !1ATPase activity; ATP hydrolysis is required for Clp !1hydrolysis of proteins but not of smaller polypeptides CLASSIFICATION #superfamily endopeptidase Clp ATP-binding chain KEYWORDS ATP; chloroplast; hydrolase; molecular chaperone; nucleotide !1binding; P-loop; serine proteinase FEATURE !$300-307 #region nucleotide-binding motif A (P-loop)\ !$367-371 #region nucleotide-binding motif B\ !$643-650 #region nucleotide-binding motif A (P-loop)\ !$711-715 #region nucleotide-binding motif B\ !$306 #binding_site ATP (Lys) #status predicted\ !$649 #binding_site ATP (Lys) #status predicted SUMMARY #length 923 #molecular-weight 102240 #checksum 3666 SEQUENCE /// ENTRY S31164 #type complete TITLE endopeptidase Clp (EC 3.4.21.-) ATP-binding chain, chloroplast [similarity] - garden pea ALTERNATE_NAMES ATP-dependent Clp proteinase regulatory chain CONTAINS adenosinetriphosphatase (EC 3.6.1.3) ORGANISM #formal_name Pisum sativum #common_name garden pea DATE 30-Apr-1999 #sequence_revision 30-Apr-1999 #text_change 19-Jan-2001 ACCESSIONS S31164 REFERENCE S31164 !$#authors Moore, T.; Keegstra, K. !$#journal Plant Mol. Biol. (1993) 21:525-537 !$#title Characterization of a cDNA clone encoding a !1chloroplast-targeted Clp homologue. !$#cross-references MUID:93184208; PMID:8443344 !$#accession S31164 !'##molecule_type mRNA !'##residues 1-922 ##label MOO !'##cross-references EMBL:L09547; NID:g169127; PIDN:AAA33680.1; !1PID:g169128 FUNCTION !$#description allows clpP to hydrolyze polypeptides and proteins, probably !1by a chaperone-like activity that makes protein substrates !1more accessible to the clpP active site; independently has !1ATPase activity; ATP hydrolysis is required for Clp !1hydrolysis of proteins but not of smaller polypeptides CLASSIFICATION #superfamily endopeptidase Clp ATP-binding chain KEYWORDS ATP; chloroplast; hydrolase; molecular chaperone; nucleotide !1binding; P-loop; serine proteinase FEATURE !$300-307 #region nucleotide-binding motif A (P-loop)\ !$367-372 #region nucleotide-binding motif B\ !$643-650 #region nucleotide-binding motif A (P-loop)\ !$711-716 #region nucleotide-binding motif B\ !$306 #binding_site ATP (Lys) #status predicted\ !$649 #binding_site ATP (Lys) #status predicted SUMMARY #length 922 #molecular-weight 102710 #checksum 3878 SEQUENCE /// ENTRY S76330 #type complete TITLE endopeptidase Clp (EC 3.4.21.-) ATP-binding chain C [similarity] - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES ATP-dependent Clp proteinase regulatory chain CONTAINS adenosinetriphosphatase (EC 3.6.1.3) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 30-Apr-1999 #sequence_revision 30-Apr-1999 #text_change 19-Jan-2001 ACCESSIONS S76330 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76330 !'##status preliminary !'##molecule_type DNA !'##residues 1-821 ##label KAN !'##cross-references EMBL:D64000; GB:AB001339; NID:g1001484; !1PIDN:BAA10182.1; PID:g1001555 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 FUNCTION !$#description allows clpP to hydrolyze polypeptides and proteins, probably !1by a chaperone-like activity that makes protein substrates !1more accessible to the clpP active site; independently has !1ATPase activity; ATP hydrolysis is required for Clp !1hydrolysis of proteins but not of smaller polypeptides CLASSIFICATION #superfamily endopeptidase Clp ATP-binding chain KEYWORDS ATP; hydrolase; molecular chaperone; nucleotide binding; !1P-loop; serine proteinase FEATURE !$208-215 #region nucleotide-binding motif A (P-loop)\ !$275-280 #region nucleotide-binding motif B\ !$545-552 #region nucleotide-binding motif A (P-loop)\ !$613-618 #region nucleotide-binding motif B\ !$214 #binding_site ATP (Lys) #status predicted\ !$551 #binding_site ATP (Lys) #status predicted SUMMARY #length 821 #molecular-weight 91174 #checksum 8226 SEQUENCE /// ENTRY S71553 #type complete TITLE endopeptidase Clp (EC 3.4.21.-) ATP-binding chain clpC [similarity] - Synechococcus sp. (strain PCC 7942) ALTERNATE_NAMES ATP-dependent Clp proteinase regulatory chain CONTAINS adenosinetriphosphatase (EC 3.6.1.3) ORGANISM #formal_name Synechococcus sp. #variety PCC 7942 DATE 30-Apr-1999 #sequence_revision 30-Apr-1999 #text_change 19-Jan-2001 ACCESSIONS S71553 REFERENCE S71553 !$#authors Clarke, A.K.; Eriksson, M.J. !$#journal Plant Mol. Biol. (1996) 31:721-730 !$#title The cyanobacterium Synechococcus sp. PCC 7942 possesses a !1close homologue to the chloroplast ClpC protein of higher !1plants. !$#cross-references MUID:96400027; PMID:8806403 !$#accession S71553 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-839 ##label CLA !'##cross-references EMBL:U16134; NID:g755162; PIDN:AAB67745.1; !1PID:g755163 GENETICS !$#gene clpC FUNCTION !$#description allows clpP to hydrolyze polypeptides and proteins, probably !1by a chaperone-like activity that makes protein substrates !1more accessible to the clpP active site; independently has !1ATPase activity; ATP hydrolysis is required for Clp !1hydrolysis of proteins but not of smaller polypeptides CLASSIFICATION #superfamily endopeptidase Clp ATP-binding chain KEYWORDS ATP; hydrolase; molecular chaperone; nucleotide binding; !1P-loop; serine proteinase FEATURE !$222-229 #region nucleotide-binding motif A (P-loop)\ !$289-294 #region nucleotide-binding motif B\ !$562-569 #region nucleotide-binding motif A (P-loop)\ !$630-635 #region nucleotide-binding motif B\ !$228 #binding_site ATP (Lys) #status predicted\ !$568 #binding_site ATP (Lys) #status predicted SUMMARY #length 839 #molecular-weight 92883 #checksum 4823 SEQUENCE /// ENTRY S73253 #type complete TITLE endopeptidase Clp (EC 3.4.21.-) ATP-binding chain clpC [similarity] - red alga (Porphyra purpurea) chloroplast ALTERNATE_NAMES ATP-dependent Clp proteinase regulatory chain CONTAINS adenosinetriphosphatase (EC 3.6.1.3) ORGANISM #formal_name chloroplast Porphyra purpurea DATE 30-Apr-1999 #sequence_revision 30-Apr-1999 #text_change 19-Jan-2001 ACCESSIONS S73253 REFERENCE S73108 !$#authors Reith, M.; Munholland, J. !$#journal Plant Mol. Biol. Rep. (1995) 13:333-335 !$#title Complete nucleotide sequence of the Porphyra purpurea !1chloroplast genome. !$#accession S73253 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-821 ##label REI !'##cross-references EMBL:U38804; NID:g1276652; PIDN:AAC08218.1; !1PID:g1276798 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1995 GENETICS !$#gene clpC !$#genome chloroplast FUNCTION !$#description allows clpP to hydrolyze polypeptides and proteins, probably !1by a chaperone-like activity that makes protein substrates !1more accessible to the clpP active site; independently has !1ATPase activity; ATP hydrolysis is required for Clp !1hydrolysis of proteins but not of smaller polypeptides CLASSIFICATION #superfamily endopeptidase Clp ATP-binding chain KEYWORDS ATP; chloroplast; hydrolase; molecular chaperone; nucleotide !1binding; P-loop; serine proteinase FEATURE !$210-217 #region nucleotide-binding motif A (P-loop)\ !$277-282 #region nucleotide-binding motif B\ !$549-556 #region nucleotide-binding motif A (P-loop)\ !$617-622 #region nucleotide-binding motif B\ !$216 #binding_site ATP (Lys) #status predicted\ !$555 #binding_site ATP (Lys) #status predicted SUMMARY #length 821 #molecular-weight 91060 #checksum 7778 SEQUENCE /// ENTRY S78246 #type complete TITLE endopeptidase Clp (EC 3.4.21.-) ATP-binding chain clpC [similarity] - Odontella sinensis chloroplast ALTERNATE_NAMES ATP-dependent Clp proteinase regulatory chain; caseinolytic Clp proteinase homolog CONTAINS adenosinetriphosphatase (EC 3.6.1.3) ORGANISM #formal_name chloroplast Odontella sinensis DATE 30-Apr-1999 #sequence_revision 30-Apr-1999 #text_change 19-Jan-2001 ACCESSIONS S78246 REFERENCE S78238 !$#authors Kowallik, K.V.; Stoebe, B.; Schaffran, I.; Kroth-Pancic, P.; !1Freier, U. !$#journal Plant Mol. Biol. Rep. (1995) 13:336-342 !$#title The Chloroplast Genome of a chlorophyll a+c- containing !1Alga, Odontella sinensis. !$#accession S78246 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-885 ##label KOW !'##cross-references EMBL:Z67753; NID:g1185127; PIDN:CAA91619.1; !1PID:g1185136 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1995 GENETICS !$#gene clpC !$#genome chloroplast FUNCTION !$#description allows clpP to hydrolyze polypeptides and proteins, probably !1by a chaperone-like activity that makes protein substrates !1more accessible to the clpP active site; independently has !1ATPase activity; ATP hydrolysis is required for Clp !1hydrolysis of proteins but not of smaller polypeptides CLASSIFICATION #superfamily endopeptidase Clp ATP-binding chain KEYWORDS ATP; chloroplast; hydrolase; molecular chaperone; nucleotide !1binding; P-loop; serine proteinase FEATURE !$218-225 #region nucleotide-binding motif A (P-loop)\ !$285-290 #region nucleotide-binding motif B\ !$560-567 #region nucleotide-binding motif A (P-loop)\ !$628-633 #region nucleotide-binding motif B\ !$224 #binding_site ATP (Lys) #status predicted\ !$566 #binding_site ATP (Lys) #status predicted SUMMARY #length 885 #molecular-weight 99917 #checksum 1724 SEQUENCE /// ENTRY E70954 #type complete TITLE endopeptidase Clp (EC 3.4.21.-) ATP-binding chain clpC [similarity] - Mycobacterium tuberculosis (strain H37RV) ALTERNATE_NAMES ATP-dependent Clp proteinase regulatory chain CONTAINS adenosinetriphosphatase (EC 3.6.1.3) ORGANISM #formal_name Mycobacterium tuberculosis DATE 30-Apr-1999 #sequence_revision 30-Apr-1999 #text_change 19-Jan-2001 ACCESSIONS E70954 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession E70954 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-848 ##label COL !'##cross-references GB:Z95557; GB:AL123456; NID:g3242276; !1PIDN:CAB08932.1; PID:g2113980 !'##experimental_source strain H37Rv GENETICS !$#gene clpC FUNCTION !$#description allows clpP to hydrolyze polypeptides and proteins, probably !1by a chaperone-like activity that makes protein substrates !1more accessible to the clpP active site; independently has !1ATPase activity; ATP hydrolysis is required for Clp !1hydrolysis of proteins but not of smaller polypeptides CLASSIFICATION #superfamily endopeptidase Clp ATP-binding chain KEYWORDS ATP; hydrolase; molecular chaperone; nucleotide binding; !1P-loop; serine proteinase FEATURE !$216-223 #region nucleotide-binding motif A (P-loop)\ !$283-288 #region nucleotide-binding motif B\ !$553-560 #region nucleotide-binding motif A (P-loop)\ !$621-626 #region nucleotide-binding motif B\ !$222 #binding_site ATP (Lys) #status predicted\ !$559 #binding_site ATP (Lys) #status predicted SUMMARY #length 848 #molecular-weight 93552 #checksum 9782 SEQUENCE /// ENTRY I40508 #type complete TITLE endopeptidase Clp (EC 3.4.21.-) ATP-binding chain clpC [similarity] - Bacillus subtilis ALTERNATE_NAMES adenosine triphosphatase clpC; ATP-dependent Clp proteinase regulatory chain; class III stress response-related ATPase clpC; clpA/clpB protein homolog CONTAINS adenosinetriphosphatase (EC 3.6.1.3) ORGANISM #formal_name Bacillus subtilis DATE 30-Apr-1999 #sequence_revision 30-Apr-1999 #text_change 19-Jan-2001 ACCESSIONS I40508; S66115; I40385; H69600 REFERENCE I40507 !$#authors Msadek, T.; Kunst, F.; Rapoport, G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1994) 91:5788-5792 !$#title MecB of Bacillus subtilis, a member of the ClpC ATPase !1family, is a pleiotropic regulator controlling competence !1gene expression and growth at high temperature. !$#cross-references MUID:94286523; PMID:8016066 !$#accession I40508 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-810 ##label RES !'##cross-references EMBL:U02604; NID:g442358; PIDN:AAA19233.1; !1PID:g442360 REFERENCE S65967 !$#authors Ogasawara, N.; Nakai, S.; Yoshikawa, H. !$#journal DNA Res. (1994) 1:1-14 !$#title Systematic sequencing of the 180 kilobase region of the !1Bacillus subtilis chromosome containing the replication !1origin. !$#cross-references MUID:96051385; PMID:7584024 !$#accession S66115 !'##status preliminary !'##molecule_type DNA !'##residues 1-810 ##label OGA !'##cross-references EMBL:D26185; NID:g467326; PIDN:BAA05320.1; !1PID:g467474 REFERENCE I40385 !$#authors Kruger, E.; Volker, U.; Hecker, M. !$#journal J. Bacteriol. (1994) 176:3360-3367 !$#title Stress induction of clpC in Bacillus subtilis and its !1involvement in stress tolerance. !$#cross-references MUID:94253006; PMID:8195092 !$#accession I40385 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 211-387 ##label RE2 !'##cross-references EMBL:X75930; NID:g512561; PIDN:CAA53534.1; !1PID:g512562 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69600 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-810 ##label KUN !'##cross-references GB:Z99104; GB:AL009126; NID:g2632267; !1PIDN:CAB11862.1; PID:g2632353 !'##experimental_source strain 168 GENETICS !$#gene clpC; mecB FUNCTION !$#description allows clpP to hydrolyze polypeptides and proteins, probably !1by a chaperone-like activity that makes protein substrates !1more accessible to the clpP active site; independently has !1ATPase activity; ATP hydrolysis is required for Clp !1hydrolysis of proteins but not of smaller polypeptides CLASSIFICATION #superfamily endopeptidase Clp ATP-binding chain KEYWORDS ATP; hydrolase; molecular chaperone; nucleotide binding; !1P-loop; serine proteinase FEATURE !$208-215 #region nucleotide-binding motif A (P-loop)\ !$275-280 #region nucleotide-binding motif B\ !$545-552 #region nucleotide-binding motif A (P-loop)\ !$613-618 #region nucleotide-binding motif B\ !$214 #binding_site ATP (Lys) #status predicted\ !$551 #binding_site ATP (Lys) #status predicted SUMMARY #length 810 #molecular-weight 90118 #checksum 6006 SEQUENCE /// ENTRY B70412 #type complete TITLE endopeptidase Clp (EC 3.4.21.-) ATP-binding chain clpC [similarity] - Aquifex aeolicus ALTERNATE_NAMES ATP-dependent Clp proteinase regulatory chain CONTAINS adenosinetriphosphatase (EC 3.6.1.3) ORGANISM #formal_name Aquifex aeolicus DATE 30-Apr-1999 #sequence_revision 30-Apr-1999 #text_change 19-Jan-2001 ACCESSIONS B70412 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession B70412 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-810 ##label AQF !'##cross-references GB:AE000733; NID:g2983720; PIDN:AAC07290.1; !1PID:g2983728; GB:AE000657 !'##experimental_source strain VF5 GENETICS !$#gene clpC FUNCTION !$#description allows clpP to hydrolyze polypeptides and proteins, probably !1by a chaperone-like activity that makes protein substrates !1more accessible to the clpP active site; independently has !1ATPase activity; ATP hydrolysis is required for Clp !1hydrolysis of proteins but not of smaller polypeptides CLASSIFICATION #superfamily endopeptidase Clp ATP-binding chain KEYWORDS ATP; hydrolase; molecular chaperone; nucleotide binding; !1P-loop; serine proteinase FEATURE !$201-208 #region nucleotide-binding motif A (P-loop)\ !$268-273 #region nucleotide-binding motif B\ !$538-545 #region nucleotide-binding motif A (P-loop)\ !$606-611 #region nucleotide-binding motif B\ !$207 #binding_site ATP (Lys) #status predicted\ !$544 #binding_site ATP (Lys) #status predicted SUMMARY #length 810 #molecular-weight 92355 #checksum 5010 SEQUENCE /// ENTRY C71533 #type complete TITLE endopeptidase Clp (EC 3.4.21.-) ATP-binding chain clpC [similarity] - Chlamydia trachomatis (serotype D, strain UW3/Cx) ALTERNATE_NAMES ATP-dependent Clp proteinase regulatory chain CONTAINS adenosinetriphosphatase (EC 3.6.1.3) ORGANISM #formal_name Chlamydia trachomatis DATE 30-Apr-1999 #sequence_revision 30-Apr-1999 #text_change 19-Jan-2001 ACCESSIONS C71533 REFERENCE A71570 !$#authors Stephens, R.S.; Kalman, S.; Lammel, C.J.; Fan, J.; Marathe, !1R.; Aravind, L.; Mitchell, W.P.; Olinger, L.; Tatusov, R.L.; !1Zhao, Q.; Koonin, E.V.; Davis, R.W. !$#journal Science (1998) 282:754-759 !$#title Genome sequence of an obligate intracellular pathogen of !1humans: Chlamydia trachomatis. !$#cross-references MUID:99000809; PMID:9784136 !$#accession C71533 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-854 ##label ARN !'##cross-references GB:AE001301; GB:AE001273; NID:g3328697; !1PIDN:AAC67879.1; PID:g3328700 !'##experimental_source serotype D, strain UW-3/Cx GENETICS !$#gene clpC FUNCTION !$#description allows clpP to hydrolyze polypeptides and proteins, probably !1by a chaperone-like activity that makes protein substrates !1more accessible to the clpP active site; independently has !1ATPase activity; ATP hydrolysis is required for Clp !1hydrolysis of proteins but not of smaller polypeptides CLASSIFICATION #superfamily endopeptidase Clp ATP-binding chain KEYWORDS ATP; hydrolase; molecular chaperone; nucleotide binding; !1P-loop; serine proteinase FEATURE !$234-241 #region nucleotide-binding motif A (P-loop)\ !$301-306 #region nucleotide-binding motif B\ !$571-578 #region nucleotide-binding motif A (P-loop)\ !$639-644 #region nucleotide-binding motif B\ !$240 #binding_site ATP (Lys) #status predicted\ !$577 #binding_site ATP (Lys) #status predicted SUMMARY #length 854 #molecular-weight 95145 #checksum 2669 SEQUENCE /// ENTRY G72079 #type complete TITLE endopeptidase Clp (EC 3.4.21.-) ATP-binding chain clpC [similarity] - Chlamydophila pneumoniae (strain CWL029) ALTERNATE_NAMES ATP-dependent Clp proteinase regulatory chain CONTAINS adenosinetriphosphatase (EC 3.6.1.3) ORGANISM #formal_name Chlamydophila pneumoniae, Chlamydia pneumoniae DATE 30-Apr-1999 #sequence_revision 30-Apr-1999 #text_change 19-Jan-2001 ACCESSIONS G72079 REFERENCE A72000 !$#authors Kalman, S.; Mitchell, W.; Marathe, R.; Lammel, C.; Fan, J.; !1Olinger, L.; Grimwood, J.; Davis, R.W.; Stephens, R.S. !$#journal Nature Genet. (1999) 21:385-389 !$#title Comparative genomes of Clamydia pneumoniae and C. !1trachomatis. !$#cross-references MUID:99206606; PMID:10192388 !$#accession G72079 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-845 ##label ARN !'##cross-references GB:AE001626; GB:AE001363; NID:g4376708; !1PIDN:AAD18581.1; PID:g4376719 !'##experimental_source strain CWL029 GENETICS !$#gene clpC FUNCTION !$#description allows clpP to hydrolyze polypeptides and proteins, probably !1by a chaperone-like activity that makes protein substrates !1more accessible to the clpP active site; independently has !1ATPase activity; ATP hydrolysis is required for Clp !1hydrolysis of proteins but not of smaller polypeptides CLASSIFICATION #superfamily endopeptidase Clp ATP-binding chain KEYWORDS ATP; hydrolase; molecular chaperone; nucleotide binding; !1P-loop; serine proteinase FEATURE !$232-239 #region nucleotide-binding motif A (P-loop)\ !$299-304 #region nucleotide-binding motif B\ !$569-576 #region nucleotide-binding motif A (P-loop)\ !$637-642 #region nucleotide-binding motif B\ !$238 #binding_site ATP (Lys) #status predicted\ !$575 #binding_site ATP (Lys) #status predicted SUMMARY #length 845 #molecular-weight 95008 #checksum 5271 SEQUENCE /// ENTRY D35905 #type complete TITLE endopeptidase Clp (EC 3.4.21.-) ATP-binding chain clpB [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES ATP-dependent Clp proteinase regulatory chain B CONTAINS adenosinetriphosphatase (EC 3.6.1.3) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1993 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS C65037; D35905; A04440; S18736; JN0279; JN0280 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65037 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-857 ##label BLAT !'##cross-references GB:AE000345; GB:U00096; NID:g1788939; !1PIDN:AAC75641.1; PID:g1788943; UWGP:b2592 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A35905 !$#authors Gottesman, S.; Squires, C.; Pichersky, E.; Carrington, M.; !1Hobbs, M.; Mattick, J.S.; Dalrymple, B.; Kuramitsu, H.; !1Shiroza, T.; Foster, T.; Clark, W.P.; Ross, B.; Squires, !1C.L.; Maurizi, M.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:3513-3517 !$#title Conservation of the regulatory subunit for the Clp !1ATP-dependent protease in prokaryotes and eukaryotes. !$#cross-references MUID:90239044; PMID:2185473 !$#accession D35905 !'##molecule_type DNA !'##residues 1-95,'NV',98-121,'V',123-857 ##label GOT !'##cross-references GB:M29364; NID:g147363; PIDN:AAA24422.1; !1PID:g147365 REFERENCE A04440 !$#authors Shen, W.F.; Squires, C.; Squires, C.L. !$#journal Nucleic Acids Res. (1982) 10:3303-3313 !$#title Nucleotide sequence of the rrnG ribosomal RNA promoter !1region of Escherichia coli. !$#cross-references MUID:82247208; PMID:6285294 !$#accession A04440 !'##molecule_type DNA !'##residues 753-857 ##label SHE !'##cross-references GB:J01699 REFERENCE S18736 !$#authors Kitagawa, M.; Wada, C.; Yoshioka, S.; Yura, T. !$#journal J. Bacteriol. (1991) 173:4247-4253 !$#title Expression of ClpB, an analog of the ATP-dependent protease !1regulatory subunit in Escherichia coli, is controlled by a !1heat shock sigma factor (sigma(32)). !$#cross-references MUID:91294165; PMID:1906060 !$#accession S18736 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-593 ##label KIT !'##cross-references EMBL:X57620 !'##note this sequence was submitted to the EMBL Data Library, February !11991 REFERENCE JN0279 !$#authors Pontis, E.; Sun, X.Y.; Joernvall, H.; Krook, M.; Reichard, !1P. !$#journal Biochem. Biophys. Res. Commun. (1991) 180:1222-1226 !$#title ClpB proteins copurify with the anaerobic Escherichia coli !1reductase. !$#cross-references MUID:92062147; PMID:1953774 !$#accession JN0279 !'##molecule_type protein !'##residues 1-14;355-364;452-460 ##label PON1 !$#accession JN0280 !'##molecule_type protein !'##residues 'M',150-157;355-364;452-461 ##label PON2 !'##note two chains, alpha and beta3, are encoded by the clpB gene !'##note residues 1-14, 355-364, and 452-460 are from alpha protein, !1while residues 149-157 (with 149 determined as Met) and !1452-461 are from beta3 protein !'##note the amino-terminal residue of the beta3 protein, demonstrated !1to be a methionine, is encoded by a GTG codon and is !1translated as 149-Val in the longer alpha protein !'##note 456-Asp was also found in the beta3 chain GENETICS CLB !$#gene clpB !$#map_position 56 min GENETICS CL3 !$#gene clpB(3) !$#map_position 56 min !$#start_codon GTG FUNCTION !$#description allows clpP to hydrolyze polypeptides and proteins, probably !1by a chaperone-like activity that makes protein substrates !1more accessible to the clpP active site; independently has !1ATPase activity; ATP hydrolysis is required for Clp !1hydrolysis of proteins but not of smaller polypeptides CLASSIFICATION #superfamily endopeptidase Clp ATP-binding chain KEYWORDS ATP; hydrolase; molecular chaperone; nucleotide binding; !1P-loop; serine proteinase FEATURE !$1-593 #product clpB alpha chain #status experimental #label !8MATA\ !$'M',150-593 #product clpB beta-3 chain #status experimental !8#label MTB3\ !$206-213 #region nucleotide-binding motif A (P-loop)\ !$274-278 #region nucleotide-binding motif B\ !$605-612 #region nucleotide-binding motif A (P-loop)\ !$673-677 #region nucleotide-binding motif B\ !$212 #binding_site ATP (Lys) #status predicted\ !$611 #binding_site ATP (Lys) #status predicted SUMMARY #length 857 #molecular-weight 95584 #checksum 3256 SEQUENCE /// ENTRY F64098 #type complete TITLE endopeptidase Clp (EC 3.4.21.-) ATP-binding chain [similarity] - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES ATP-dependent Clp proteinase regulatory chain CONTAINS adenosinetriphosphatase (EC 3.6.1.3) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS F64098 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession F64098 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-856 ##label TIGR !'##cross-references GB:U32767; GB:L42023; NID:g1573868; !1PIDN:AAC22518.1; PID:g1573874; TIGR:HI0859 FUNCTION !$#description allows clpP to hydrolyze polypeptides and proteins, probably !1by a chaperone-like activity that makes protein substrates !1more accessible to the clpP active site; independently has !1ATPase activity; ATP hydrolysis is required for Clp !1hydrolysis of proteins but not of smaller polypeptides CLASSIFICATION #superfamily endopeptidase Clp ATP-binding chain KEYWORDS ATP; hydrolase; molecular chaperone; nucleotide binding; !1P-loop; serine proteinase FEATURE !$206-213 #region nucleotide-binding motif A (P-loop)\ !$274-278 #region nucleotide-binding motif B\ !$605-612 #region nucleotide-binding motif A (P-loop)\ !$673-677 #region nucleotide-binding motif B\ !$212 #binding_site ATP (Lys) #status predicted\ !$611 #binding_site ATP (Lys) #status predicted SUMMARY #length 856 #molecular-weight 95836 #checksum 1380 SEQUENCE /// ENTRY C35905 #type complete TITLE endopeptidase Clp (EC 3.4.21.-) ATP-binding chain clpB [similarity] - Dichelobacter nodosus ALTERNATE_NAMES ATP-dependent Clp proteinase regulatory chain B CONTAINS adenosinetriphosphatase (EC 3.6.1.3) ORGANISM #formal_name Dichelobacter nodosus DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 19-Jan-2001 ACCESSIONS C35905; S18723; S15253; S15254; S15257 REFERENCE A35905 !$#authors Gottesman, S.; Squires, C.; Pichersky, E.; Carrington, M.; !1Hobbs, M.; Mattick, J.S.; Dalrymple, B.; Kuramitsu, H.; !1Shiroza, T.; Foster, T.; Clark, W.P.; Ross, B.; Squires, !1C.L.; Maurizi, M.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:3513-3517 !$#title Conservation of the regulatory subunit for the Clp !1ATP-dependent protease in prokaryotes and eukaryotes. !$#cross-references MUID:90239044; PMID:2185473 !$#accession C35905 !'##molecule_type DNA !'##residues 1-860 ##label GOT !'##cross-references GB:M32229 REFERENCE S18723 !$#authors Mattick, J.S. !$#submission submitted to the EMBL Data Library, April 1990 !$#accession S18723 !'##molecule_type DNA !'##residues 541-860 ##label MAT !'##cross-references EMBL:M32230 !'##experimental_source serotype E1 !'##note the source is designated as Bacteroides nodosus REFERENCE S15240 !$#authors Hobbs, M.; Dalrymple, B.P.; Cox, P.T.; Livingstone, S.P.; !1Delaney, S.F.; Mattick, J.S. !$#journal Mol. Microbiol. (1991) 5:543-560 !$#title Organization of the fimbrial gene region of Bacteroides !1nodosus: class I and class II strains. !$#cross-references MUID:91260439; PMID:1675418 !$#accession S15253 !'##molecule_type DNA !'##residues 847-860 ##label HOB !'##cross-references EMBL:M32230 !'##experimental_source serotype E1 !'##note the source is designated as Bacteroides nodosus !$#accession S15254 !'##molecule_type DNA !'##residues 847-860 ##label HO2 !'##cross-references EMBL:X52390; NID:g39703; PIDN:CAA36623.1; !1PID:g809658 !'##experimental_source serotype H1 !'##note the source is designated as Bacteroides nodosus !$#accession S15257 !'##molecule_type DNA !'##residues 847-860 ##label HO3 !'##cross-references EMBL:X52410; NID:g39691; PIDN:CAA36664.1; !1PID:g747704 !'##experimental_source serotype I !'##note the source is designated as Bacteroides nodosus GENETICS !$#gene clpB FUNCTION !$#description allows clpP to hydrolyze polypeptides and proteins, probably !1by a chaperone-like activity that makes protein substrates !1more accessible to the clpP active site; independently has !1ATPase activity; ATP hydrolysis is required for Clp !1hydrolysis of proteins but not of smaller polypeptides CLASSIFICATION #superfamily endopeptidase Clp ATP-binding chain KEYWORDS ATP; hydrolase; molecular chaperone; nucleotide binding; !1P-loop; serine proteinase FEATURE !$210-217 #region nucleotide-binding motif A (P-loop)\ !$278-282 #region nucleotide-binding motif B\ !$610-617 #region nucleotide-binding motif A (P-loop)\ !$678-683 #region nucleotide-binding motif B\ !$216 #binding_site ATP (Lys) #status predicted\ !$616 #binding_site ATP (Lys) #status predicted SUMMARY #length 860 #molecular-weight 96270 #checksum 9074 SEQUENCE /// ENTRY S61476 #type complete TITLE endopeptidase Clp (EC 3.4.21.-) ATP-binding chain HSP104 [similarity] - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES clpB protein homolog; heat shock protein 104; protein L0948; protein YLL026w CONTAINS adenosinetriphosphatase (EC 3.6.1.3) ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Feb-2001 ACCESSIONS S61476; S17877; S64777; S64774; S69380 REFERENCE S61476 !$#authors Lindquist, S. !$#submission submitted to the EMBL Data Library, July 1991 !$#accession S61476 !'##molecule_type DNA !'##residues 1-908 ##label LIN !'##cross-references EMBL:M67479; NID:g557872; PIDN:AAA50477.1; !1PID:g557873 REFERENCE S17877 !$#authors Parsell, D.A.; Sanchez, Y.; Stitzel, J.D.; Lindquist, S. !$#journal Nature (1991) 353:270-273 !$#title Hsp104 is a highly conserved protein with two essential !1nucleotide-binding sites. !$#cross-references MUID:91375541; PMID:1896074 !$#accession S17877 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-235,'I',237-418,'QSIAIDSSRD',429,'SSRERVECRLH',441-442, !1'RK',445-491,'V',493-499,'R',501-908 ##label PAR !'##cross-references EMBL:M67479 REFERENCE S64775 !$#authors Duesterhoeft, A.; Floeth, M.; Heuss-Neitzel, D.; Hilbert, !1H.; Moestl, D. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64777 !'##molecule_type DNA !'##residues 1-908 ##label DUE !'##cross-references EMBL:Z73131; NID:g1360205; PIDN:CAA97475.1; !1PID:g1360206; GSPDB:GN00012; MIPS:YLL026w !'##experimental_source strain S288C REFERENCE S64761 !$#authors Goffeau, A.; Purnelle, B. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64774 !'##molecule_type DNA !'##residues 749-908 ##label GOF !'##cross-references EMBL:Z73131; GSPDB:GN00012; MIPS:YLL026w !'##experimental_source strain S288C REFERENCE S69380 !$#authors Purnelle, B.; Goffeau, A. !$#submission submitted to the EMBL Data Library, April 1996 !$#description The sequence of 32 kb on the left arm of yeast chromosome !1XII reveals 14 open reading frames among which HSP104, SSA2, !1SPA2, KNS1, DPS1/APS, SDC25, a new member of the !1seripauperins family and a new ABC transporter homologous to !1the human multidrug resistance protein. !$#accession S69380 !'##molecule_type DNA !'##residues 749-908 ##label PUR !'##cross-references EMBL:X97560; NID:g1297003; PIDN:CAA66164.1; !1PID:g1297004 GENETICS !$#gene SGD:HSP104; MIPS:YLL026w !'##cross-references SGD:S0003949; MIPS:YLL026w !$#map_position 12L FUNCTION !$#description allows clpP to hydrolyze polypeptides and proteins, probably !1by a chaperone-like activity that makes protein substrates !1more accessible to the clpP active site; independently has !1ATPase activity; ATP hydrolysis is required for Clp !1hydrolysis of proteins but not of smaller polypeptides CLASSIFICATION #superfamily endopeptidase Clp ATP-binding chain KEYWORDS ATP; heat shock; hydrolase; molecular chaperone; nucleotide !1binding; P-loop; serine proteinase; stress-induced protein FEATURE !$212-219 #region nucleotide-binding motif A (P-loop)\ !$280-284 #region nucleotide-binding motif B\ !$614-621 #region nucleotide-binding motif A (P-loop)\ !$682-686 #region nucleotide-binding motif B\ !$218 #binding_site ATP (Lys) #status predicted\ !$620 #binding_site ATP (Lys) #status predicted SUMMARY #length 908 #molecular-weight 102034 #checksum 8369 SEQUENCE /// ENTRY E35905 #type complete TITLE endopeptidase Clp (EC 3.4.21.-) ATP-binding chain clpB [similarity] - Trypanosoma brucei ALTERNATE_NAMES ATP-dependent Clp proteinase regulatory chain B CONTAINS adenosinetriphosphatase (EC 3.6.1.3) ORGANISM #formal_name Trypanosoma brucei DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 19-Jan-2001 ACCESSIONS E35905 REFERENCE A35905 !$#authors Gottesman, S.; Squires, C.; Pichersky, E.; Carrington, M.; !1Hobbs, M.; Mattick, J.S.; Dalrymple, B.; Kuramitsu, H.; !1Shiroza, T.; Foster, T.; Clark, W.P.; Ross, B.; Squires, !1C.L.; Maurizi, M.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:3513-3517 !$#title Conservation of the regulatory subunit for the Clp !1ATP-dependent protease in prokaryotes and eukaryotes. !$#cross-references MUID:90239044; PMID:2185473 !$#accession E35905 !'##molecule_type DNA !'##residues 1-862 ##label GOT !'##cross-references GB:M32225 GENETICS !$#gene clpB FUNCTION !$#description allows clpP to hydrolyze polypeptides and proteins, probably !1by a chaperone-like activity that makes protein substrates !1more accessible to the clpP active site; independently has !1ATPase activity; ATP hydrolysis is required for Clp !1hydrolysis of proteins but not of smaller polypeptides CLASSIFICATION #superfamily endopeptidase Clp ATP-binding chain KEYWORDS ATP; hydrolase; molecular chaperone; nucleotide binding; !1P-loop; serine proteinase FEATURE !$198-205 #region nucleotide-binding motif A (P-loop)\ !$266-270 #region nucleotide-binding motif B\ !$597-604 #region nucleotide-binding motif A (P-loop)\ !$665-669 #region nucleotide-binding motif B\ !$204 #binding_site ATP (Lys) #status predicted\ !$603 #binding_site ATP (Lys) #status predicted SUMMARY #length 862 #molecular-weight 96314 #checksum 5076 SEQUENCE /// ENTRY T07807 #type complete TITLE endopeptidase Clp (EC 3.4.21.-) ATP-binding chain SB100 [similarity] - soybean CONTAINS adenosinetriphosphatase (EC 3.6.1.3) ORGANISM #formal_name Glycine max #common_name soybean DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 02-Feb-2001 ACCESSIONS T07807 REFERENCE Z06049 !$#authors Lee Y-R, J.; Nagao, R.T.; Key, J.L. !$#journal Plant Cell (1994) 6:1889-1897 !$#title A soybean 101-kD heat shock protein complements a yeast !1HSP104 deletion mutant in acquiring thermotolerance. !$#cross-references MUID:95170290; PMID:7866031 !$#accession T07807 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-911 ##label LEE !'##cross-references EMBL:L35272; NID:g530206; PIDN:AAA66338.1; !1PID:g530207 GENETICS !$#gene SB100 CLASSIFICATION #superfamily endopeptidase Clp ATP-binding chain KEYWORDS ATP; hydrolase; molecular chaperone; nucleotide binding; !1P-loop; serine proteinase FEATURE !$208-215 #region nucleotide-binding motif A (P-loop)\ !$276-281 #region nucleotide-binding motif B\ !$606-613 #region nucleotide-binding motif A (P-loop)\ !$674-679 #region nucleotide-binding motif B\ !$214 #binding_site ATP (Lys) #status predicted\ !$612 #binding_site ATP (Lys) #status predicted SUMMARY #length 911 #molecular-weight 101328 #checksum 1945 SEQUENCE /// ENTRY A70204 #type complete TITLE endopeptidase Clp (EC 3.4.21.-) ATP-binding chain BB0834 [similarity] - Lyme disease spirochete ALTERNATE_NAMES ATP-dependent Clp proteinase regulatory chain CONTAINS adenosinetriphosphatase (EC 3.6.1.3) ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 24-May-2001 ACCESSIONS A70204 REFERENCE A70100 !$#authors Fraser, C.M.; Casjens, S.; Huang, W.M.; Sutton, G.G.; !1Clayton, R.; Lathigra, R.; White, O.; Ketchum, K.A.; Dodson, !1R.; Hickey, E.K.; Gwinn, M.; Dougherty, B.; Tomb, J.F.; !1Fleischmann, R.D.; Richardson, D.; Peterson, J.; Kerlavage, !1A.R.; Quackenbush, J.; Salzberg, S.; Hanson, M.; Vugt, R.V.; !1Palmer, N.; Adams, M.D.; Gocayne, J.; Weidman, J.; !1Utterback, T.; Watthey, L.; McDonald, L.; Artiach, P.; !1Bowman, C.; Garland, S.; Fujii, C.; Cotton, M.D.; Horst, K.; !1Roberts, K.; Hatch, B.; Smith, H.O.; Venter, J.C. !$#journal Nature (1997) 390:580-586 !$#title Genomic sequence of a Lyme disease spirochaete, Borrelia !1burgdorferi. !$#cross-references MUID:98065943; PMID:9403685 !$#accession A70204 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-739 ##label KLE !'##cross-references GB:AE001181; GB:AE000783; NID:g2688772; !1PIDN:AAC67178.1; PID:g2688774; TIGR:BB0834 !'##experimental_source strain B31 FUNCTION !$#description allows clpP to hydrolyze polypeptides and proteins, probably !1by a chaperone-like activity that makes protein substrates !1more accessible to the clpP active site; independently has !1ATPase activity; ATP hydrolysis is required for Clp !1hydrolysis of proteins but not of smaller polypeptides CLASSIFICATION #superfamily endopeptidase Clp ATP-binding chain KEYWORDS ATP; hydrolase; molecular chaperone; nucleotide binding; !1P-loop; serine proteinase FEATURE !$203-210 #region nucleotide-binding motif A (P-loop)\ !$270-275 #region nucleotide-binding motif B\ !$481-488 #region nucleotide-binding motif A (P-loop)\ !$636-641 #region nucleotide-binding motif B\ !$209 #binding_site ATP (Lys) #status predicted\ !$487 #binding_site ATP (Lys) #status predicted SUMMARY #length 739 #molecular-weight 84442 #checksum 799 SEQUENCE /// ENTRY S24353 #type complete TITLE proteasome 26S subunit MSS1 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S24353 REFERENCE S24353 !$#authors Shibuya, H.; Irie, K.; Ninomiya-Tsuji, J.; Goebl, M.; !1Taniguchi, T.; Matsumoto, K. !$#journal Nature (1992) 357:700-702 !$#title New human gene encoding a positive modulator of HIV !1Tat-mediated transactivation. !$#cross-references MUID:92310549; PMID:1377363 !$#accession S24353 !'##molecule_type mRNA !'##residues 1-433 ##label SHI !'##cross-references EMBL:D11094; NID:g219930; PIDN:BAA01868.1; !1PID:g219931 GENETICS !$#gene GDB:PSMC2; MSS1; S7 !'##cross-references GDB:683325; OMIM:154365 !$#map_position 6p21.3-6p21.3 CLASSIFICATION #superfamily ATP-dependent 26S proteinase; FtsH/SEC18/ !1CDC48-type ATP-binding domain homology KEYWORDS ATP; nucleotide binding; P-loop; proteasome; protein !1degradation FEATURE !$189-399 #domain FtsH/SEC18/CDC48-type ATP-binding domain !8homology #label VATP\ !$216-223 #region nucleotide-binding motif A (P-loop) SUMMARY #length 433 #molecular-weight 48633 #checksum 8623 SEQUENCE /// ENTRY VPPG #type complete TITLE transitional endoplasmic reticulum ATPase - pig ALTERNATE_NAMES CDC48 homolog; TER ATPase; valosin-containing protein CONTAINS ATPase (EC 3.6.1.-) ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 13-Aug-1986 #sequence_revision 16-Feb-1996 #text_change 19-Jan-2001 ACCESSIONS A26360; A01627 REFERENCE A26360 !$#authors Koller, K.J.; Brownstein, M.J. !$#journal Nature (1987) 325:542-545 !$#title Use of a cDNA clone to identify a supposed precursor protein !1containing valosin. !$#cross-references MUID:87115844; PMID:3468358 !$#accession A26360 !'##molecule_type mRNA !'##residues 1-806 ##label KOL !'##cross-references GB:M30143 REFERENCE A01627 !$#authors Schmidt, W.E.; Mutt, V.; Carlquist, M.; Kratzin, H.; Conlon, !1J.M.; Creutzfeldt, W. !$#journal FEBS Lett. (1985) 191:264-268 !$#title Valosin: isolation and characterization of a novel peptide !1from porcine intestine. !$#cross-references MUID:86030678; PMID:4054310 !$#accession A01627 !'##molecule_type protein !'##residues 493-517 ##label SCH COMMENT The peptide valosin is probably a breakdown product with no !1physiological significance. CLASSIFICATION #superfamily transitional endoplasmic reticulum ATPase; !1FtsH/SEC18/CDC48-type ATP-binding domain homology KEYWORDS ATP; duplication; hydrolase; nucleotide binding; P-loop; !1phosphoprotein FEATURE !$218-425 #domain FtsH/SEC18/CDC48-type ATP-binding domain !8homology #label VAT1\ !$245-252 #region nucleotide-binding motif A (P-loop)\ !$491-701 #domain FtsH/SEC18/CDC48-type ATP-binding domain !8homology #label VAT2\ !$518-525 #region nucleotide-binding motif A (P-loop) SUMMARY #length 806 #molecular-weight 89302 #checksum 9687 SEQUENCE /// ENTRY A55190 #type complete TITLE transitional endoplasmic reticulum ATPase (EC 3.6.1.-) [validated] - rat ALTERNATE_NAMES CDC48 homolog; TER ATPase; valosin-containing protein ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 27-Jan-1995 #sequence_revision 13-Mar-1997 #text_change 19-Jan-2001 ACCESSIONS A55190 REFERENCE A55190 !$#authors Zhang, L.; Ashendel, C.L.; Becker, G.W.; Morre, D.J. !$#journal J. Cell Biol. (1994) 127:1871-1883 !$#title Isolation and characterization of the principal ATPase !1associated with transitional endoplasmic reticulum of rat !1liver. !$#cross-references MUID:95105231; PMID:7806566 !$#accession A55190 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-806 ##label ZHA !'##cross-references GB:U11760; NID:g641972; PIDN:AAC52154.1; !1PID:g641973 !'##experimental_source liver COMPLEX hexamer of six 100K chains [validated, MUID:95105231]; !1ring-shaped structure with six-fold rotational symmetry FUNCTION !$#description EC 3.6.1.-; ATPase [validated, MUID:95105231] !$#note the enzyme is phosphorylated in the presence of magnesium CLASSIFICATION #superfamily transitional endoplasmic reticulum ATPase; !1FtsH/SEC18/CDC48-type ATP-binding domain homology KEYWORDS ATP; duplication; hydrolase; nucleotide binding; P-loop; !1phosphoprotein FEATURE !$218-425 #domain FtsH/SEC18/CDC48-type ATP-binding domain !8homology #label VAT1\ !$245-252 #region nucleotide-binding motif A (P-loop)\ !$491-701 #domain FtsH/SEC18/CDC48-type ATP-binding domain !8homology #label VAT2\ !$518-525 #region nucleotide-binding motif A (P-loop) SUMMARY #length 806 #molecular-weight 89348 #checksum 9802 SEQUENCE /// ENTRY S25197 #type complete TITLE transitional endoplasmic reticulum ATPase - mouse ALTERNATE_NAMES CDC48 homolog; TER ATPase; valosin-containing protein CONTAINS ATPase (EC 3.6.1.-) ORGANISM #formal_name Mus musculus #common_name house mouse DATE 07-May-1993 #sequence_revision 13-Mar-1997 #text_change 19-Jan-2001 ACCESSIONS S25197; S30329 REFERENCE S25197 !$#authors Egerton, M.; Ashe, O.R.; Chen, D.; Druker, B.J.; Burgess, !1W.H.; Samelson, L.E. !$#journal EMBO J. (1992) 11:3533-3540 !$#title VCP, the mammalian homolog of cdc48, is tyrosine !1phosphorylated in response to T cell antigen receptor !1activation. !$#cross-references MUID:93010943; PMID:1382975 !$#accession S25197 !'##molecule_type mRNA !'##residues 1-806 ##label EGE !'##cross-references EMBL:Z14044; NID:g55216; PIDN:CAA78412.1; !1PID:g55217 !$#accession S30329 !'##molecule_type protein !'##residues 20-40;295-309;425-438 ##label EG2 CLASSIFICATION #superfamily transitional endoplasmic reticulum ATPase; !1FtsH/SEC18/CDC48-type ATP-binding domain homology KEYWORDS ATP; duplication; hydrolase; nucleotide binding; P-loop; !1phosphoprotein FEATURE !$218-425 #domain FtsH/SEC18/CDC48-type ATP-binding domain !8homology #label VAT1\ !$245-252 #region nucleotide-binding motif A (P-loop)\ !$491-701 #domain FtsH/SEC18/CDC48-type ATP-binding domain !8homology #label VAT2\ !$518-525 #region nucleotide-binding motif A (P-loop) SUMMARY #length 806 #molecular-weight 89307 #checksum 522 SEQUENCE /// ENTRY S19738 #type complete TITLE transitional endoplasmic reticulum ATPase (EC 3.6.1.-) 97K chain - African clawed frog ALTERNATE_NAMES CDC48 homolog; valosin-containing protein CONTAINS adenosinetriphosphatase (EC 3.6.1.3) [validated] ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 07-May-1993 #sequence_revision 13-Mar-1997 #text_change 19-Jan-2001 ACCESSIONS S19738; S12537 REFERENCE S19738 !$#authors Peters, J. !$#submission submitted to the EMBL Data Library, July 1991 !$#accession S19738 !'##molecule_type mRNA !'##residues 1-805 ##label PET !'##cross-references EMBL:X54240; NID:g64965; PIDN:CAA38146.1; !1PID:g64966 REFERENCE S12537 !$#authors Peters, J.M.; Walsh, M.J.; Franke, W.W. !$#journal EMBO J. (1990) 9:1757-1767 !$#title An abundant and ubiquitous homo-oligomeric ringshaped ATPase !1particle related to the putative vesicle fusion proteins !1Sec18p and NSF. !$#cross-references MUID:90269209; PMID:2140770 !$#accession S12537 !'##molecule_type mRNA !'##residues 442-805 ##label PET2 !'##cross-references EMBL:X54240 !'##note the authors translated the codon GGG for residue 455 as Ala COMPLEX homooligomer [validated, MUID:90269209] FUNCTION !$#description may be the transitional endoplasmic reticulum ATPase CLASSIFICATION #superfamily transitional endoplasmic reticulum ATPase; !1FtsH/SEC18/CDC48-type ATP-binding domain homology KEYWORDS ATP; duplication; hydrolase; nucleotide binding; P-loop FEATURE !$218-425 #domain FtsH/SEC18/CDC48-type ATP-binding domain !8homology #label VAT1\ !$245-252 #region nucleotide-binding motif A (P-loop)\ !$491-701 #domain FtsH/SEC18/CDC48-type ATP-binding domain !8homology #label VAT2\ !$518-525 #region nucleotide-binding motif A (P-loop) SUMMARY #length 805 #molecular-weight 89131 #checksum 8009 SEQUENCE /// ENTRY S60112 #type complete TITLE transitional endoplasmic reticulum ATPase - Arabidopsis thaliana ALTERNATE_NAMES cell division control protein CDC48 homolog CONTAINS ATPase (EC 3.6.1.-) ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S60112 REFERENCE S60112 !$#authors Feiler, H.S.; Desprez, T.; Santoni, V.; Kronenberger, J.; !1Caboche, M.; Traas, J. !$#journal EMBO J. (1995) 14:5626-5637 !$#title The higher plant Arabidopsis thaliana encodes a functional !1CDC48 homologue which is highly expressed in dividing and !1expanding cells. !$#cross-references MUID:96091135; PMID:8521820 !$#accession S60112 !'##status preliminary !'##molecule_type mRNA !'##residues 1-809 ##label FEI !'##cross-references EMBL:U37587; NID:g1019903; PIDN:AAC49120.1; !1PID:g1019904 CLASSIFICATION #superfamily transitional endoplasmic reticulum ATPase; !1FtsH/SEC18/CDC48-type ATP-binding domain homology KEYWORDS ATP; duplication; hydrolase; nucleotide binding; P-loop FEATURE !$221-428 #domain FtsH/SEC18/CDC48-type ATP-binding domain !8homology #label VAT1\ !$248-255 #region nucleotide-binding motif A (P-loop)\ !$494-705 #domain FtsH/SEC18/CDC48-type ATP-binding domain !8homology #label VAT2\ !$521-528 #region nucleotide-binding motif A (P-loop) SUMMARY #length 809 #molecular-weight 89392 #checksum 7590 SEQUENCE /// ENTRY S67669 #type complete TITLE transitional endoplasmic reticulum ATPase [validated] - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES cell division control protein CDC48; protein D2228; protein YDL126c CONTAINS ATPase (EC 3.6.1.-) ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S67669; A39977; S71951 REFERENCE S67655 !$#authors Rieger, M.; Mueller-Auer, S.; Brueckner, M.; Schaefer, M.; !1Wagner, G. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67669 !'##molecule_type DNA !'##residues 1-835 ##label RIE !'##cross-references EMBL:Z74174; NID:g1431188; PIDN:CAA98694.1; !1PID:g1431189; GSPDB:GN00004; MIPS:YDL126c !'##experimental_source strain S288C REFERENCE A39977 !$#authors Froehlich, K.U.; Fries, H.W.; Ruediger, M.; Erdmann, R.; !1Botstein, D.; Mecke, D. !$#journal J. Cell Biol. (1991) 114:443-453 !$#title Yeast cell cycle protein CDC48p shows full-length homology !1to the mammalian protein VCP and is a member of a protein !1family involved in secretion, peroxisome formation, and gene !1expression. !$#cross-references MUID:91317863; PMID:1860879 !$#accession A39977 !'##molecule_type DNA !'##residues 1-12,14,'STC',18-189,'I',191-835 ##label FRO !'##cross-references GB:X56956 REFERENCE S71950 !$#authors Ghislain, M.; Dohmen, R.J.; Levy, F.; Varshavsky, A. !$#journal EMBO J. (1996) 15:4884-4899 !$#title Cdc48p interacts with Ufd3p, a WD repeat protein required !1for ubiquitin-mediated proteolysis in Saccharomyces !1cerevisiae. !$#cross-references MUID:97045097; PMID:8890162 !$#accession S71951 !'##molecule_type protein !'##residues 2-13 ##label GHI GENETICS !$#gene SGD:CDC48; MIPS:YDL126c !'##cross-references SGD:S0002284; MIPS:YDL126c !$#map_position 4L FUNCTION !$#description plays an essential role in cell division cycle, probably at !1the spindle pole body respectively the centrosome, and has a !1function in the homotypic fusion of endoplasmic reticulum !1vesicles [validated, MUID:98099694] !$#note the location of CDC48 changes in a cell cycle-dependent !1manner; CDC48 enters the nucleus during late G1; nuclear !1import is regulated by a cell cycle-dependent !1phosphorylation of a tyrosine residue CLASSIFICATION #superfamily transitional endoplasmic reticulum ATPase; !1FtsH/SEC18/CDC48-type ATP-binding domain homology KEYWORDS ATP; duplication; hydrolase; nucleotide binding; P-loop; !1phosphoprotein FEATURE !$2-835 #product cell division control protein CDC48 #status !8experimental #label MAT\ !$16-33 #region nuclear localization signal #status !8experimental\ !$228-435 #domain FtsH/SEC18/CDC48-type ATP-binding domain !8homology #label VAT1\ !$255-262 #region nucleotide-binding motif A (P-loop)\ !$501-711 #domain FtsH/SEC18/CDC48-type ATP-binding domain !8homology #label VAT2\ !$528-535 #region nucleotide-binding motif A (P-loop)\ !$834 #binding_site phosphate (Tyr) (covalent) #status !8experimental SUMMARY #length 835 #molecular-weight 91995 #checksum 1540 SEQUENCE /// ENTRY C64444 #type complete TITLE cell division control protein CDC48 homolog - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS C64444 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession C64444 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-903 ##label BUL !'##cross-references GB:U67557; GB:L77117; NID:g1591777; !1PIDN:AAB99153.1; PID:g1591785; TIGR:MJ1156 GENETICS !$#map_position REV1097124-1094413 CLASSIFICATION #superfamily transitional endoplasmic reticulum ATPase; !1FtsH/SEC18/CDC48-type ATP-binding domain homology KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$193-400 #domain FtsH/SEC18/CDC48-type ATP-binding domain !8homology #label VAT1\ !$220-227 #region nucleotide-binding motif A (P-loop)\ !$466-674 #domain FtsH/SEC18/CDC48-type ATP-binding domain !8homology #label VAT2\ !$493-500 #region nucleotide-binding motif A (P-loop) SUMMARY #length 903 #molecular-weight 100402 #checksum 3620 SEQUENCE /// ENTRY S43859 #type complete TITLE ATPase - Sulfolobus acidocaldarius ORGANISM #formal_name Sulfolobus acidocaldarius DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S43859 REFERENCE S43859 !$#authors Confalonieri, F.; Marsault, J.; Duguet, M. !$#journal J. Mol. Biol. (1994) 235:396-401 !$#title SAV, an archaebacterial gene with extensive homology to a !1family of highly conserved eukaryotic ATPases. !$#cross-references MUID:94118286; PMID:8289263 !$#accession S43859 !'##status preliminary; nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-780 ##label CON !'##cross-references EMBL:L17042; NID:g310599; PIDN:AAA72002.1; !1PID:g310600 CLASSIFICATION #superfamily transitional endoplasmic reticulum ATPase; !1FtsH/SEC18/CDC48-type ATP-binding domain homology KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$226-433 #domain FtsH/SEC18/CDC48-type ATP-binding domain !8homology #label VAT1\ !$253-260 #region nucleotide-binding motif A (P-loop)\ !$501-709 #domain FtsH/SEC18/CDC48-type ATP-binding domain !8homology #label VAT2\ !$528-535 #region nucleotide-binding motif A (P-loop) SUMMARY #length 780 #molecular-weight 87480 #checksum 9222 SEQUENCE /// ENTRY S47018 #type complete TITLE cdcH protein - Halobacterium salinarum ORGANISM #formal_name Halobacterium salinarum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S47018 REFERENCE S47018 !$#authors Bibikov, S.I.; Oesterhelt, D. !$#submission submitted to the EMBL Data Library, June 1994 !$#description Tyrosine phosphorylation of the novel ATPase in !1Halobacterium salinarium. !$#accession S47018 !'##status preliminary !'##molecule_type DNA !'##residues 1-742 ##label BIB !'##cross-references EMBL:X79560; NID:g517389; PIDN:CAA56097.1; !1PID:g517390 !'##note the source is designated as Halobacterium salinarium CLASSIFICATION #superfamily transitional endoplasmic reticulum ATPase; !1FtsH/SEC18/CDC48-type ATP-binding domain homology KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$203-410 #domain FtsH/SEC18/CDC48-type ATP-binding domain !8homology #label VAT1\ !$230-237 #region nucleotide-binding motif A (P-loop)\ !$476-684 #domain FtsH/SEC18/CDC48-type ATP-binding domain !8homology #label VAT2\ !$503-510 #region nucleotide-binding motif A (P-loop) SUMMARY #length 742 #molecular-weight 81643 #checksum 421 SEQUENCE /// ENTRY S39110 #type complete TITLE valosin-containing protein homolog AFG2 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES CDC48 protein homolog; protein L8084.16; protein YLR397c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S39110; S55953 REFERENCE S39110 !$#authors Thorsness, P.E.; White, K.H.; Ong, W.C. !$#journal Yeast (1993) 9:1267-1271 !$#title AFG2, an essential gene in yeast, encodes a new member of !1the Sec18p, Pas1p, Cdc48p, TBP-1 family of putative ATPases. !$#cross-references MUID:94152174; PMID:8109176 !$#accession S39110 !'##molecule_type DNA !'##residues 1-780 ##label THO !'##cross-references EMBL:L14615; NID:g295572; PIDN:AAC37367.1; !1PID:g295573 REFERENCE S55944 !$#authors Du, Z. !$#submission submitted to the EMBL Data Library, January 1995 !$#description The sequence of S. cerevisiae cosmid 8084. !$#accession S55953 !'##molecule_type DNA !'##residues 1-780 ##label DUZ !'##cross-references EMBL:U19729; NID:g625097; PIDN:AAB82355.1; !1PID:g625113; GSPDB:GN00012; MIPS:YLR397c !'##experimental_source strain S288C (AB972) GENETICS !$#gene SGD:AFG2; DRG1; MIPS:YLR397c !'##cross-references SGD:S0004389; MIPS:YLR397c !$#map_position 12R CLASSIFICATION #superfamily transitional endoplasmic reticulum ATPase; !1FtsH/SEC18/CDC48-type ATP-binding domain homology KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$259-471 #domain FtsH/SEC18/CDC48-type ATP-binding domain !8homology #label VAT1\ !$286-293 #region nucleotide-binding motif A (P-loop)\ !$530-738 #domain FtsH/SEC18/CDC48-type ATP-binding domain !8homology #label VAT2 SUMMARY #length 780 #molecular-weight 84747 #checksum 6125 SEQUENCE /// ENTRY S37606 #type complete TITLE SEC18 protein - yeast (Candida albicans) ORGANISM #formal_name Candida albicans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S37606 REFERENCE S37606 !$#authors Nieto, A.; Sanz, P.; Sentandreu, R.; del Castillo Agudo, L. !$#journal Yeast (1993) 9:875-887 !$#title Cloning and characterization of the SEC18 gene from Candida !1albicans. !$#cross-references MUID:94025979; PMID:8212895 !$#accession S37606 !'##molecule_type DNA !'##residues 1-794 ##label NIE !'##cross-references EMBL:X66467 !'##note the sequence from Fig. 7 is inconsistent with that from Fig. 6 !1in lacking 680-Leu GENETICS !$#gene SEC18 CLASSIFICATION #superfamily transitional endoplasmic reticulum ATPase; !1FtsH/SEC18/CDC48-type ATP-binding domain homology KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$290-513 #domain FtsH/SEC18/CDC48-type ATP-binding domain !8homology #label VATP\ !$317-324 #region nucleotide-binding motif A (P-loop)\ !$381-386 #region nucleotide-binding motif B SUMMARY #length 794 #molecular-weight 88977 #checksum 3116 SEQUENCE /// ENTRY S45477 #type complete TITLE SEC18 protein - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YBR0736; protein YBR080c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S45477; S45945; A30813; S59715; S39231 REFERENCE S45462 !$#authors van der Aart, Q.J.M.; Barthe, C.; Doignon, F.; Aigle, M.; !1Crouzet, M.; Steensma, H.Y. !$#journal Yeast (1994) 10:959-964 !$#title Sequence analysis of a 31 kb DNA fragment from the right arm !1of Saccharomyces cerevisiae chromosome II. !$#cross-references MUID:95076715; PMID:7985423 !$#accession S45477 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-758 ##label VAN !'##cross-references EMBL:X76294; NID:g974203; PIDN:CAA53939.1; !1PID:g433846 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1993 REFERENCE S45932 !$#authors Steensma, H.Y.; van der Aart, Q.J.M. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S45945 !'##molecule_type DNA !'##residues 1-758 ##label STE !'##cross-references EMBL:Z35949; NID:g536339; PIDN:CAA85025.1; !1PID:g536340; GSPDB:GN00002; MIPS:YBR080c REFERENCE A30813 !$#authors Eakle, K.A.; Bernstein, M.; Emr, S.D. !$#journal Mol. Cell. Biol. (1988) 8:4098-4109 !$#title Characterization of a component of the yeast secretion !1machinery: identification of the SEC18 gene product. !$#cross-references MUID:89039834; PMID:3054509 !$#accession A30813 !'##molecule_type DNA !'##residues 1-380,382-758 ##label EAK !'##cross-references EMBL:M20662; NID:g172562; PIDN:AAA35030.1; !1PID:g172563 REFERENCE S59702 !$#authors van der Aart, Q.J.M. !$#submission submitted to the EMBL Data Library, August 1995 !$#accession S59715 !'##molecule_type DNA !'##residues 1-758 ##label VAW !'##cross-references EMBL:X76294; NID:g974203; PIDN:CAA53939.1; !1PID:g433846 !'##experimental_source strain S288C GENETICS !$#gene SGD:SEC18; MIPS:YBR080c !'##cross-references SGD:S0000284; MIPS:YBR080c !$#map_position 2R CLASSIFICATION #superfamily transitional endoplasmic reticulum ATPase; !1FtsH/SEC18/CDC48-type ATP-binding domain homology KEYWORDS ATP; membrane trafficking; nucleotide binding; P-loop FEATURE !$254-476 #domain FtsH/SEC18/CDC48-type ATP-binding domain !8homology #label VATP\ !$281-288 #region nucleotide-binding motif A (P-loop)\ !$564-571 #region nucleotide-binding motif A (P-loop) SUMMARY #length 758 #molecular-weight 84055 #checksum 9693 SEQUENCE /// ENTRY PRBEI1 #type complete TITLE 56K serine proteinase (EC 3.4.21.-) - ictalurid herpesvirus 1 (strain auburn 1) ORGANISM #formal_name ictalurid herpesvirus 1 #note host Ictalurus punctatus (channel catfish) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS C36791 REFERENCE A36804 !$#authors Davison, A.J. !$#submission submitted to GenBank, January 1992 !$#description Channel catfish virus: a new type of herpesvirus. !$#accession C36791 !'##molecule_type DNA !'##residues 1-518 ##label DAV !'##cross-references GB:M75136; NID:g331209; PIDN:AAA88150.1; !1PID:g331257 REFERENCE A39447 !$#authors Davison, A.J. !$#journal Virology (1992) 186:9-14 !$#title Channel catfish virus: a new type of herpesvirus. !$#cross-references MUID:92087490; PMID:1727613 !$#contents annotation !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 47 CLASSIFICATION #superfamily ictalurid herpesvirus 56K serine proteinase; !1subtilisin homology KEYWORDS hydrolase; serine proteinase FEATURE !$150-350 #domain subtilisin homology #label SBT SUMMARY #length 518 #molecular-weight 55984 #checksum 4227 SEQUENCE /// ENTRY S57342 #type complete TITLE endopeptidase La homolog (EC 3.4.21.-) precursor, mitochondrial (version 1) - human ALTERNATE_NAMES ATP-dependent proteinase lon homolog CONTAINS adenosinetriphosphatase (EC 3.6.1.3) ORGANISM #formal_name Homo sapiens #common_name man DATE 23-Apr-1999 #sequence_revision 23-Apr-1999 #text_change 19-Jan-2001 ACCESSIONS S57342 REFERENCE S57342 !$#authors Wang, N.; Gottesman, S.; Willingham, M.C.; Gottesman, M.M.; !1Maurizi, M.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:11247-11251 !$#title A human mitochondrial ATP-dependent protease that is highly !1homologous to bacterial Lon protease. !$#cross-references MUID:94068581; PMID:8248235 !$#accession S57342 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-962 ##label WAN !'##cross-references EMBL:U02389; NID:g639426; PIDN:AAA61616.1; !1PID:g440874 COMMENT This enzyme can also serve as a molecular chaperone and is !1essential for respiration. GENETICS !$#gene GDB:LON !'##cross-references GDB:269860 CLASSIFICATION #superfamily ATP-dependent serine proteinase La KEYWORDS ATP; DNA binding; hydrolase; mitochondrion; molecular !1chaperone; nucleotide binding; P-loop; serine proteinase FEATURE !$526-533 #region nucleotide-binding motif A (P-loop)\ !$589-594 #region nucleotide-binding motif B\ !$532 #binding_site ATP (Lys) #status predicted\ !$858 #active_site Ser #status predicted SUMMARY #length 962 #molecular-weight 106466 #checksum 3799 SEQUENCE /// ENTRY S42366 #type complete TITLE endopeptidase La homolog (EC 3.4.21.-) precursor, mitochondrial (version 2) - human ALTERNATE_NAMES ATP-dependent proteinase lon homolog CONTAINS adenosinetriphosphatase (EC 3.6.1.3) ORGANISM #formal_name Homo sapiens #common_name man DATE 23-Apr-1999 #sequence_revision 23-Apr-1999 #text_change 19-Jan-2001 ACCESSIONS S42366; S38500; S38860; S42365 REFERENCE S42365 !$#authors Amerik, A.Y.; Petukhova, G.V.; Grigorenko, V.G.; Lykov, !1I.P.; Yarovoi, S.V.; Lipkin, V.M.; Gorbalenya, A.E. !$#journal FEBS Lett. (1994) 340:25-28 !$#title Cloning and sequence analysis of cDNA for a human homolog of !1eubacterial ATP-dependent Lon proteases. !$#cross-references MUID:94164302; PMID:8119403 !$#accession S42366 !'##molecule_type mRNA !'##residues 1-937 ##label AME !'##cross-references EMBL:X76040; NID:g429099; PIDN:CAA53625.1; !1PID:g429100 !'##note the authors translated the codon ATT for residue 39 as Leu COMMENT This enzyme can also serve as a molecular chaperone and is !1essential for respiration. GENETICS !$#gene GDB:LON !'##cross-references GDB:269860 CLASSIFICATION #superfamily ATP-dependent serine proteinase La KEYWORDS ATP; DNA binding; hydrolase; mitochondrion; molecular !1chaperone; nucleotide binding; P-loop; serine proteinase FEATURE !$501-508 #region nucleotide-binding motif A (P-loop)\ !$564-569 #region nucleotide-binding motif B\ !$507 #binding_site ATP (Lys) #status predicted\ !$833 #active_site Ser #status predicted SUMMARY #length 937 #molecular-weight 103999 #checksum 915 SEQUENCE /// ENTRY S43938 #type complete TITLE endopeptidase La-like enzyme (EC 3.4.21.-) PIM1 precursor, mitochondrial - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES ATP-dependent proteinase lon homolog; protein YBL022c; protein YBL0440 CONTAINS adenosinetriphosphatase (EC 3.6.1.3) ORGANISM #formal_name Saccharomyces cerevisiae DATE 23-Apr-1999 #sequence_revision 23-Apr-1999 #text_change 19-Jan-2001 ACCESSIONS S43938; S45756; S44598; B28123 REFERENCE S43937 !$#authors van Dyck, L.; Pearce, D.A.; Sherman, F. !$#journal J. Biol. Chem. (1994) 269:238-242 !$#title PIM1 encodes a mitochondrial ATP-dependent protease that is !1required for mitochondrial function in the yeast !1Saccharomyces cerevisiae. !$#cross-references MUID:94103216; PMID:8276800 !$#accession S43938 !'##molecule_type DNA !'##residues 1-1133 ##label VAN !'##cross-references EMBL:X74544; NID:g453234; PIDN:CAA52634.1; !1PID:g453236 REFERENCE S45745 !$#authors Goffeau, A.; Jonniaux, J.L.; Purnelle, B.; Skala, J.; de !1Wergifosse, P.; van Dyck, L. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S45756 !'##molecule_type DNA !'##residues 1-1133 ##label GOF !'##cross-references EMBL:Z35783; NID:g536018; PIDN:CAA84841.1; !1PID:g536019; GSPDB:GN00002; MIPS:YBL022c REFERENCE S44598 !$#authors Suzuki, C.K.; Suda, K.; Wang, N.; Schatz, G. !$#submission submitted to the EMBL Data Library, February 1994 !$#description Requirement for the yeast gene LON in intramitochondrial !1proteolysis and the maintenance of respiratory function. !$#accession S44598 !'##molecule_type mRNA !'##residues 1-508,'R',510-1133 ##label SUZ !'##cross-references EMBL:L28110; NID:g452153; PIDN:AAA53625.1; !1PID:g454438 REFERENCE A93110 !$#authors Hahn, S.; Pinkham, J.; Wei, R.; Miller, R.; Guarente, L. !$#journal Mol. Cell. Biol. (1988) 8:655-663 !$#title The HAP3 regulatory locus of Saccharomyces cerevisiae !1encodes divergent overlapping transcripts. !$#cross-references MUID:88174707; PMID:2832732 !$#accession B28123 !'##molecule_type DNA !'##residues 1-216 ##label HAH !'##cross-references EMBL:M20318 GENETICS !$#gene SGD:PIM1; MIPS:YBL022c !'##cross-references SGD:S0000118; MIPS:YBL022c !$#map_position 2L !$#genome nuclear FUNCTION !$#description serine proteinase; hydrolase !$#note can also serve as a molecular chaperone; may be involved in !1heat shock response; is essential for maintenance of !1respiratory function CLASSIFICATION #superfamily ATP-dependent serine proteinase La KEYWORDS ATP; DNA binding; heat shock; hydrolase; mitochondrial !1matrix; mitochondrion; molecular chaperone; nucleotide !1binding; P-loop; serine proteinase FEATURE !$632-639 #region nucleotide-binding motif A (P-loop)\ !$695-700 #region nucleotide-binding motif B\ !$638 #binding_site ATP (Lys) #status predicted\ !$1015 #active_site Ser #status predicted SUMMARY #length 1133 #molecular-weight 127111 #checksum 1982 SEQUENCE /// ENTRY S62421 #type complete TITLE endopeptidase La homolog (EC 3.4.21.-) PIM1 precursor, mitochondrial - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES ATP-dependent proteinase lon homolog; hypothetical protein SPAC22F3.06c CONTAINS adenosinetriphosphatase (EC 3.6.1.3) ORGANISM #formal_name Schizosaccharomyces pombe DATE 23-Apr-1999 #sequence_revision 23-Apr-1999 #text_change 19-Jan-2001 ACCESSIONS S62421; T38185 REFERENCE S62416 !$#authors Lye, G.; Churcher, C.M. !$#submission submitted to the EMBL Data Library, October 1995 !$#accession S62421 !'##status preliminary !'##molecule_type DNA !'##residues 1-1067 ##label LYE !'##cross-references EMBL:Z54285; NID:g1008429; PIDN:CAA91071.1; !1PID:g1008434 REFERENCE Z21776 !$#authors Lye, G.; Churcher, C.M.; Barrell, B.G.; Rajandream, M.A.; !1Walsh, S.V. !$#submission submitted to the EMBL Data Library, October 1995 !$#accession T38185 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-1067 ##label LY2 !'##cross-references EMBL:Z54285; PIDN:CAA91071.1; GSPDB:GN00066; !1SPDB:SPAC22F3.06c !'##experimental_source strain 972h-; cosmid c22F3 COMMENT This enzyme can also serve as a molecular chaperone and is !1essential for respiration. GENETICS !$#gene SPDB:SPAC22F3.06c !$#map_position 1L FUNCTION !$#description serine proteinase !$#note may be involved in heat shock response CLASSIFICATION #superfamily ATP-dependent serine proteinase La KEYWORDS ATP; DNA binding; heat shock; hydrolase; mitochondrial !1matrix; mitochondrion; molecular chaperone; nucleotide !1binding; P-loop; serine proteinase FEATURE !$578-585 #region nucleotide-binding motif A (P-loop)\ !$641-646 #region nucleotide-binding motif B\ !$584 #binding_site ATP (Lys) #status predicted\ !$946 #active_site Ser #status predicted SUMMARY #length 1067 #molecular-weight 118641 #checksum 3559 SEQUENCE /// ENTRY T04325 #type complete TITLE probable ATP-dependent proteinase LON2 (EC 3.4.21.-), mitochondrial - maize ORGANISM #formal_name Zea mays #common_name maize DATE 23-Apr-1999 #sequence_revision 23-Apr-1999 #text_change 19-Jan-2001 ACCESSIONS T04325 REFERENCE Z15282 !$#authors Barakat, S.; Pearce, D.A.; Sherman, F.; Rapp, W.D. !$#journal Plant Mol. Biol. (1998) 37:141-154 !$#title Maize contains a Lon protease gene that can partially !1complement a yeast pim1-deletion mutant. !$#cross-references MUID:98281582; PMID:9620272 !$#accession T04325 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-964 ##label BAR !'##cross-references EMBL:U85495; NID:g1816587; PIDN:AAC50021.1; !1PID:g1816588 !'##experimental_source strain B73 GENETICS !$#gene LON2 FUNCTION !$#description serine proteinase CLASSIFICATION #superfamily ATP-dependent serine proteinase La KEYWORDS ATP; DNA binding; hydrolase; mitochondrial matrix; !1mitochondrion; molecular chaperone; nucleotide binding; !1P-loop; serine proteinase FEATURE !$455-462 #region nucleotide-binding motif A (P-loop)\ !$518-523 #region nucleotide-binding motif B\ !$461 #binding_site ATP (Lys) #status predicted\ !$863 #active_site Ser #status predicted SUMMARY #length 964 #molecular-weight 105658 #checksum 8719 SEQUENCE /// ENTRY T01765 #type complete TITLE endopeptidase La-like proteinase (EC 3.4.21.-) precursor, mitochondrial - Arabidopsis thaliana ALTERNATE_NAMES ATP-dependent proteinase LON; hypothetical protein A_IG002P16.23 CONTAINS adenosinetriphosphatase (EC 3.6.1.3) ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 23-Apr-1999 #sequence_revision 23-Apr-1999 #text_change 19-Jan-2001 ACCESSIONS T01765 REFERENCE Z14421 !$#authors Miller, N.; Beck, C.; Kramer, J. !$#submission submitted to the EMBL Data Library, June 1997 !$#description The sequence of A. thaliana IG002P16. !$#accession T01765 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-1096 ##label MIL !'##cross-references EMBL:AF007270; NID:g2191157; PIDN:AAB61060.1; !1PID:g2191174; GSPDB:GN00063; ATSP:A_IG002P16.23 GENETICS !$#gene ATSP:A_IG002P16.23 !$#map_position 5 !$#introns 99/3; 133/3; 155/3; 217/3; 239/3; 253/3; 296/1; 311/2; 329/ !13; 351/3; 398/3; 412/1; 518/2; 560/1; 603/3; 638/3; 651/3; !1721/1; 770/3; 804/3; 1020/1 FUNCTION !$#description serine proteinase CLASSIFICATION #superfamily ATP-dependent serine proteinase La KEYWORDS ATP; DNA binding; hydrolase; mitochondrial matrix; !1mitochondrion; molecular chaperone; nucleotide binding; !1P-loop; serine proteinase FEATURE !$567-574 #region nucleotide-binding motif A (P-loop)\ !$630-635 #region nucleotide-binding motif B\ !$573 #binding_site ATP (Lys) #status predicted\ !$982 #active_site Ser #status predicted SUMMARY #length 1096 #molecular-weight 122766 #checksum 2720 SEQUENCE /// ENTRY T04321 #type complete TITLE endopeptidase La homolog (EC 3.4.21.-) LON1 precursor, mitochondrial - maize ALTERNATE_NAMES ATP-dependent proteinase LON1; ATP-dependent serine proteinase La homolog CONTAINS adenosinetriphosphatase (EC 3.6.1.3) ORGANISM #formal_name Zea mays #common_name maize DATE 23-Apr-1999 #sequence_revision 23-Apr-1999 #text_change 19-Jan-2001 ACCESSIONS T04321 REFERENCE Z15282 !$#authors Barakat, S.; Pearce, D.A.; Sherman, F.; Rapp, W.D. !$#journal Plant Mol. Biol. (1998) 37:141-154 !$#title Maize contains a Lon protease gene that can partially !1complement a yeast pim1-deletion mutant. !$#cross-references MUID:98281582; PMID:9620272 !$#accession T04321 !'##status preliminary !'##molecule_type mRNA !'##residues 1-885 ##label BAR !'##cross-references EMBL:U85494; NID:g1816585; PIDN:AAC50011.1; !1PID:g1816586 GENETICS !$#gene LON2 FUNCTION !$#description serine proteinase CLASSIFICATION #superfamily ATP-dependent serine proteinase La KEYWORDS ATP; DNA binding; hydrolase; mitochondrial matrix; !1mitochondrion; molecular chaperone; nucleotide binding; !1P-loop; serine proteinase FEATURE !$409-416 #region nucleotide-binding motif A (P-loop)\ !$472-477 #region nucleotide-binding motif B\ !$781 #active_site Ser #status predicted SUMMARY #length 885 #molecular-weight 97732 #checksum 8611 SEQUENCE /// ENTRY SUECLA #type complete TITLE endopeptidase La (EC 3.4.21.53) - Escherichia coli (strain K-12) ALTERNATE_NAMES ATP-dependent proteinase lon; ATP-dependent serine proteinase La CONTAINS adenosinetriphosphatase (EC 3.6.1.3) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1991 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS G64773; JN0303; S06368; A31069; I53680 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64773 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-784 ##label BLAT !'##cross-references GB:AE000150; GB:U00096; NID:g1786639; !1PIDN:AAC73542.1; PID:g1786643; UWGP:b0439 !'##experimental_source strain K-12, substrain MG1655 REFERENCE JN0303 !$#authors Amerik, A.Y.; Autonov, V.K.; Ostroumova, N.I.; Rotanova, !1T.V.; Chistyakova, L.G. !$#journal Bioorg. Khim. (1990) 16:869-880 !$#title Cloning, structure and expression of the full lon gene of !1Escherichia coli coding for ATP-dependent protease La. !$#cross-references MUID:91054626; PMID:2242054 !$#accession JN0303 !'##molecule_type DNA !'##residues 1-187,'E',189-784 ##label AME !'##note this is a revision to the sequence from reference S06368 !'##note the authors translated the codon GAG for residue 188 as Asp REFERENCE S06368 !$#authors Amerik, A.Y.; Chistyakova, L.G.; Ostroumova, N.I.; Gurevich, !1A.I.; Antonov, V.K. !$#journal Bioorg. Khim. (1988) 14:408-411 !$#title Cloning, expression and structure of the shortened, !1functionally active Lon gene of Escherichia coli. !$#cross-references MUID:88251494; PMID:3289547 !$#accession S06368 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-778,'HHSLRRRCSTASTYYWAAS' ##label AM2 !'##cross-references GB:M38347; NID:g146643; PIDN:AAA24079.1; !1PID:g146644 REFERENCE A31069 !$#authors Chin, D.T.; Goff, S.A.; Webster, T.; Smith, T.; Goldberg, !1A.L. !$#journal J. Biol. Chem. (1988) 263:11718-11728 !$#title Sequence of the lon gene in Escherichia coli. A heat-shock !1gene which encodes the ATP-dependent protease La. !$#cross-references MUID:88298842; PMID:3042779 !$#accession A31069 !'##molecule_type DNA !'##residues 1-263,'R',265,'RQ',268,'R',270,'RTGVAE',316, !1'ENDVSDVGRSDRSAWLYRLDGTGAVECAYEGQKRPASGA',318-538, !1'RACVVWSVKSPNCVA',554,'RLSSYCSIT',564-784 ##label CHI !'##cross-references EMBL:J03896; NID:g146641; PIDN:AAA24078.1; !1PID:g146642 REFERENCE I53680 !$#authors Thomas, C.D.; Modha, J.; Razzaq, T.M.; Cullis, P.M.; Rivett, !1A.J. !$#journal Gene (1993) 136:237-242 !$#title Controlled high-level expression of the lon gene of !1Escherichia coli allows overproduction of Lon protease. !$#cross-references MUID:94124005; PMID:8294008 !$#accession I53680 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-784 ##label RES !'##cross-references GB:L12349; NID:g290453; PIDN:AAC36871.1; !1PID:g290454 COMMENT This allosteric enzyme catalyzes the hydrolysis of large !1proteins in the presence of ATP and Mg++. The enzyme is !1induced by accumulation of abnormal proteins at high !1temperature. GENETICS !$#gene lon; capR; deg; muc; lopA !$#map_position 10 min COMPLEX homotetramer CLASSIFICATION #superfamily ATP-dependent serine proteinase La KEYWORDS allosteric regulation; ATP; DNA binding; heat shock; !1homotetramer; hydrolase; nucleotide binding; P-loop; serine !1proteinase; stress-induced protein FEATURE !$356-363 #region nucleotide-binding motif A (P-loop)\ !$419-424 #region nucleotide-binding motif B\ !$679 #active_site Ser #status predicted SUMMARY #length 784 #molecular-weight 87437 #checksum 8643 SEQUENCE /// ENTRY S47270 #type complete TITLE endopeptidase La (EC 3.4.21.53) - Erwinia amylovora ALTERNATE_NAMES ATP-dependent proteinase lon; ATP-dependent serine proteinase La CONTAINS adenosinetriphosphatase (EC 3.6.1.3) ORGANISM #formal_name Erwinia amylovora DATE 09-Apr-1999 #sequence_revision 09-Apr-1999 #text_change 19-Jan-2001 ACCESSIONS S47270 REFERENCE S47270 !$#authors Eastgate, J.A.; Taylor, N.; Coleman, M.J.; Healy, B.; !1Roberts, I.S. !$#submission submitted to the EMBL Data Library, February 1994 !$#description Cloning, expression and characterisation of the lon gene of !1Erwinia amylovora: evidence for a heat-shock response in !1Erwinia amylovora. !$#accession S47270 !'##molecule_type DNA !'##residues 1-784 ##label EAS !'##cross-references EMBL:X77706; NID:g535160; PIDN:CAA54779.1; !1PID:g535161 !'##experimental_source strain OT1 COMMENT This allosteric enzyme catalyzes the hydrolysis of large !1proteins in the presence of ATP and Mg++. The enzyme is !1induced by accumulation of abnormal proteins at high !1temperature. GENETICS !$#gene lon COMPLEX homotetramer CLASSIFICATION #superfamily ATP-dependent serine proteinase La KEYWORDS allosteric regulation; ATP; DNA binding; heat shock; !1homotetramer; hydrolase; nucleotide binding; P-loop; serine !1proteinase; stress-induced protein FEATURE !$356-363 #region nucleotide-binding motif A (P-loop)\ !$419-424 #region nucleotide-binding motif B\ !$679 #active_site Ser #status predicted SUMMARY #length 784 #molecular-weight 87670 #checksum 9864 SEQUENCE /// ENTRY A64070 #type complete TITLE endopeptidase La (EC 3.4.21.53) - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES ATP-dependent proteinase lon; ATP-dependent serine proteinase La CONTAINS adenosinetriphosphatase (EC 3.6.1.3) ORGANISM #formal_name Haemophilus influenzae DATE 09-Apr-1999 #sequence_revision 09-Apr-1999 #text_change 19-Jan-2001 ACCESSIONS A64070 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession A64070 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-803 ##label TIGR !'##cross-references GB:U32729; GB:L42023; NID:g1573439; !1PIDN:AAC22121.1; PID:g1573440; TIGR:HI0462 COMMENT This allosteric enzyme catalyzes the hydrolysis of large !1proteins in the presence of ATP and Mg++. The enzyme is !1induced by accumulation of abnormal proteins at high !1temperature. GENETICS !$#gene lon; lon-A CLASSIFICATION #superfamily ATP-dependent serine proteinase La KEYWORDS allosteric regulation; ATP; DNA binding; heat shock; !1hydrolase; nucleotide binding; P-loop; serine proteinase; !1stress-induced protein FEATURE !$356-363 #region nucleotide-binding motif A (P-loop)\ !$419-424 #region nucleotide-binding motif B\ !$679 #active_site Ser #status predicted SUMMARY #length 803 #molecular-weight 89346 #checksum 6406 SEQUENCE /// ENTRY JC6045 #type complete TITLE endopeptidase La (EC 3.4.21.53) - Azospirillum brasilense ALTERNATE_NAMES ATP-dependent proteinase lon; ATP-dependent serine proteinase La CONTAINS adenosinetriphosphatase (EC 3.6.1.3) ORGANISM #formal_name Azospirillum brasilense DATE 09-Apr-1999 #sequence_revision 09-Apr-1999 #text_change 19-Jan-2001 ACCESSIONS JC6045 REFERENCE JC6045 !$#authors Mori, E.; Fulchieri, M.; Indorato, C.; Fani, R.; !1Bazzicalupo, M. !$#journal J. Bacteriol. (1996) 178:3440-3446 !$#title Cloning, nucleotide sequencing, and expression of the !1Azospirillum brasilense lon gene: Involvement in iron !1uptake. !$#cross-references MUID:96256595; PMID:8655539 !$#accession JC6045 !'##molecule_type mRNA !'##residues 1-810 ##label MOR !'##cross-references GB:U35611; NID:g1616639; PIDN:AAB16819.1; !1PID:g1504124 !'##experimental_source strain SPF94 !'##note the authors translated the codon AAG for residue 627 as Phe COMMENT This protein is involved in iron uptake and in heat shock !1response, and it regulates the synthesis of membrane !1proteins induced by iron deprivation. COMMENT This allosteric enzyme catalyzes the hydrolysis of large !1proteins in the presence of ATP and Mg++. The enzyme is !1induced by accumulation of abnormal proteins at high !1temperature. GENETICS !$#gene lon CLASSIFICATION #superfamily ATP-dependent serine proteinase La KEYWORDS allosteric regulation; ATP; DNA binding; heat shock; !1hydrolase; nucleotide binding; P-loop; serine proteinase; !1stress-induced protein FEATURE !$361-368 #region nucleotide-binding motif A (P-loop)\ !$424-429 #region nucleotide-binding motif B\ !$685 #active_site Ser #status predicted SUMMARY #length 810 #molecular-weight 90142 #checksum 7947 SEQUENCE /// ENTRY A49844 #type complete TITLE endopeptidase La (EC 3.4.21.53) 1 - Myxococcus xanthus ALTERNATE_NAMES ATP-dependent proteinase lonV; ATP-dependent serine proteinase La CONTAINS adenosinetriphosphatase (EC 3.6.1.3) ORGANISM #formal_name Myxococcus xanthus DATE 09-Apr-1999 #sequence_revision 09-Apr-1999 #text_change 19-Jan-2001 ACCESSIONS A49844 REFERENCE A49844 !$#authors Tojo, N.; Inouye, S.; Komano, T. !$#journal J. Bacteriol. (1993) 175:2271-2277 !$#title Cloning and nucleotide sequence of the Myxococcus xanthus !1lon gene: indispensability of lon for vegetative growth. !$#cross-references MUID:93224448; PMID:8468287 !$#accession A49844 !'##status preliminary !'##molecule_type DNA !'##residues 1-817 ##label TOJ !'##cross-references GB:D12923; NID:g303711; PIDN:BAA02307.1; !1PID:g303712 !'##note sequence extracted from NCBI backbone (NCBIP:129174) COMMENT This allosteric enzyme catalyzes the hydrolysis of large !1proteins in the presence of ATP and Mg++. The enzyme is !1induced by accumulation of abnormal proteins at high !1temperature. GENETICS !$#gene lon; lonV CLASSIFICATION #superfamily ATP-dependent serine proteinase La KEYWORDS allosteric regulation; ATP; DNA binding; heat shock; !1hydrolase; nucleotide binding; P-loop; serine proteinase; !1stress-induced protein FEATURE !$368-375 #region nucleotide-binding motif A (P-loop)\ !$431-436 #region nucleotide-binding motif B\ !$691 #active_site Ser #status predicted SUMMARY #length 817 #molecular-weight 91814 #checksum 87 SEQUENCE /// ENTRY B42375 #type complete TITLE endopeptidase La (EC 3.4.21.53) [validated] - Bacillus brevis ALTERNATE_NAMES ATP-dependent proteinase lon; ATP-dependent serine proteinase La CONTAINS adenosinetriphosphatase (EC 3.6.1.3) ORGANISM #formal_name Bacillus brevis DATE 09-Apr-1999 #sequence_revision 09-Apr-1999 #text_change 19-Jan-2001 ACCESSIONS B42375; I39874; JQ0901 REFERENCE A42375 !$#authors Ito, K.; Udaka, S.; Yamagata, H. !$#journal J. Bacteriol. (1992) 174:2281-2287 !$#title Cloning, characterization, and inactivation of the Bacillus !1brevis lon gene. !$#cross-references MUID:92202157; PMID:1551846 !$#accession B42375 !'##molecule_type DNA !'##residues 1-779 ##label ITO !'##cross-references GB:D00863; NID:g216293; PIDN:BAA00737.1; !1PID:g402504 !'##experimental_source strain HPD31 COMMENT This allosteric enzyme catalyzes the hydrolysis of large !1proteins in the presence of ATP and Mg++. The enzyme is !1induced by accumulation of abnormal proteins at high !1temperature. GENETICS !$#gene lon !$#start_codon TTG FUNCTION !$#description responsible for degradation of abnormal polypeptides !1[validated, MUID:92202157] CLASSIFICATION #superfamily ATP-dependent serine proteinase La KEYWORDS allosteric regulation; ATP; DNA binding; heat shock; !1hydrolase; nucleotide binding; P-loop; serine proteinase; !1stress-induced protein FEATURE !$355-362 #region nucleotide-binding motif A (P-loop)\ !$418-423 #region nucleotide-binding motif B\ !$678 #active_site Ser #status predicted SUMMARY #length 779 #molecular-weight 87421 #checksum 8522 SEQUENCE /// ENTRY I40421 #type complete TITLE endopeptidase La (EC 3.4.21.53) - Bacillus subtilis ALTERNATE_NAMES ATP-dependent serine proteinase La; class III heat-shock ATP-dependent lonA proteinase CONTAINS adenosinetriphosphatase (EC 3.6.1.3) ORGANISM #formal_name Bacillus subtilis DATE 09-Apr-1999 #sequence_revision 09-Apr-1999 #text_change 19-Jan-2001 ACCESSIONS I40421; F69652; S45101 REFERENCE I40420 !$#authors Riethdorf, S.; Volker, U.; Gerth, U.; Winkler, A.; !1Engelmann, S.; Hecker, M. !$#journal J. Bacteriol. (1994) 176:6518-6527 !$#title Cloning, nucleotide sequence, and expression of the Bacillus !1subtilis lon gene. !$#cross-references MUID:95050209; PMID:7961402 !$#accession I40421 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-774 ##label RES !'##cross-references EMBL:X76424; NID:g496556; PIDN:CAA53984.1; !1PID:g496557 !'##experimental_source strain 168, substrain IS58 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69652 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-774 ##label KUN !'##cross-references GB:Z99118; GB:AL009126; NID:g2635200; !1PIDN:CAB14780.1; PID:g2635285 !'##experimental_source strain 168 COMMENT This allosteric enzyme catalyzes the hydrolysis of large !1proteins in the presence of ATP and Mg++. The enzyme is !1induced by accumulation of abnormal proteins at high !1temperature. GENETICS !$#gene lonA CLASSIFICATION #superfamily ATP-dependent serine proteinase La KEYWORDS allosteric regulation; ATP; DNA binding; heat shock; !1hydrolase; nucleotide binding; P-loop; serine proteinase; !1stress-induced protein FEATURE !$354-361 #region nucleotide-binding motif A (P-loop)\ !$417-422 #region nucleotide-binding motif B\ !$677 #active_site Ser #status predicted SUMMARY #length 774 #molecular-weight 86606 #checksum 8361 SEQUENCE /// ENTRY A71704 #type complete TITLE endopeptidase La (EC 3.4.21.53) - Rickettsia prowazekii ALTERNATE_NAMES ATP-dependent proteinase lon; ATP-dependent serine proteinase La CONTAINS adenosinetriphosphatase (EC 3.6.1.3) ORGANISM #formal_name Rickettsia prowazekii DATE 09-Apr-1999 #sequence_revision 09-Apr-1999 #text_change 19-Jan-2001 ACCESSIONS A71704 REFERENCE A71630 !$#authors Andersson, S.G.E.; Zomorodipour, A.; Andersson, J.O.; !1Sicheritz-Ponten, T.; Alsmark, U.C.M.; Podowski, R.M.; !1Naeslund, A.K.; Eriksson, A.S.; Winkler, H.H.; Kurland, C.G. !$#journal Nature (1998) 396:133-140 !$#title The genome sequence of Rickettsia prowazekii and the origin !1of mitochondria. !$#cross-references MUID:99039499; PMID:9823893 !$#accession A71704 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-784 ##label AND !'##cross-references GB:AJ235271; GB:AJ235269; NID:g3868717; !1PIDN:CAA14907.1; PID:g3861007; GSPDB:GN00081 !'##experimental_source strain Madrid E COMMENT This allosteric enzyme catalyzes the hydrolysis of large !1proteins in the presence of ATP and Mg++. The enzyme is !1induced by accumulation of abnormal proteins at high !1temperature. GENETICS !$#gene lon; RP450 CLASSIFICATION #superfamily ATP-dependent serine proteinase La KEYWORDS allosteric regulation; ATP; DNA binding; heat shock; !1hydrolase; nucleotide binding; P-loop; serine proteinase; !1stress-induced protein FEATURE !$356-363 #region nucleotide-binding motif A (P-loop)\ !$419-424 #region nucleotide-binding motif B\ !$679 #active_site Ser #status predicted SUMMARY #length 784 #molecular-weight 88070 #checksum 143 SEQUENCE /// ENTRY A70322 #type complete TITLE endopeptidase La (EC 3.4.21.53) - Aquifex aeolicus ALTERNATE_NAMES ATP-dependent proteinase lon; ATP-dependent serine proteinase La CONTAINS adenosinetriphosphatase (EC 3.6.1.3) ORGANISM #formal_name Aquifex aeolicus DATE 09-Apr-1999 #sequence_revision 09-Apr-1999 #text_change 19-Jan-2001 ACCESSIONS A70322 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession A70322 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-795 ##label AQF !'##cross-references GB:AE000680; NID:g2982948; PIDN:AAC06568.1; !1PID:g2982953; GB:AE000657 !'##experimental_source strain VF5 COMMENT This allosteric enzyme catalyzes the hydrolysis of large !1proteins in the presence of ATP and Mg++. The enzyme is !1induced by accumulation of abnormal proteins at high !1temperature. GENETICS !$#gene lon CLASSIFICATION #superfamily ATP-dependent serine proteinase La KEYWORDS allosteric regulation; ATP; DNA binding; heat shock; !1hydrolase; nucleotide binding; P-loop; serine proteinase; !1stress-induced protein FEATURE !$370-377 #region nucleotide-binding motif A (P-loop)\ !$433-438 #region nucleotide-binding motif B\ !$692 #active_site Ser #status predicted SUMMARY #length 795 #molecular-weight 89971 #checksum 2747 SEQUENCE /// ENTRY A36895 #type complete TITLE endopeptidase La (EC 3.4.21.53) 2 - Myxococcus xanthus ALTERNATE_NAMES ATP-dependent proteinase BsgA; ATP-dependent proteinase lonD; ATP-dependent serine proteinase La CONTAINS adenosinetriphosphatase (EC 3.6.1.3) ORGANISM #formal_name Myxococcus xanthus DATE 09-Apr-1999 #sequence_revision 09-Apr-1999 #text_change 19-Jan-2001 ACCESSIONS A36895; A36894 REFERENCE A36895 !$#authors Tojo, N.; Inouye, S.; Komano, T. !$#journal J. Bacteriol. (1993) 175:4545-4549 !$#title The lonD gene is homologous to the lon gene encoding an !1ATP-dependent protease and is essential for the development !1of Myxococcus xanthus. !$#cross-references MUID:93322335; PMID:8331083 !$#accession A36895 !'##status preliminary !'##molecule_type DNA !'##residues 1-827 ##label TOJ !'##cross-references GB:D13204; NID:g435450; PIDN:BAA02491.1; !1PID:g435451 !'##experimental_source strain DZF1 REFERENCE A36894 !$#authors Gill, R.E.; Karlok, M.; Benton, D. !$#journal J. Bacteriol. (1993) 175:4538-4544 !$#title Myxococcus xanthus encodes an ATP-dependent protease which !1is required for developmental gene transcription and !1intercellular signaling. !$#cross-references MUID:93322334; PMID:8331082 !$#accession A36894 !'##status preliminary !'##molecule_type DNA !'##residues 1-659,'RP',662-827 ##label GIL !'##cross-references GB:L19301 COMMENT This allosteric enzyme catalyzes the hydrolysis of large !1proteins in the presence of ATP and Mg++. The enzyme is !1induced by accumulation of abnormal proteins at high !1temperature. GENETICS !$#gene lonD; bsgA CLASSIFICATION #superfamily ATP-dependent serine proteinase La KEYWORDS allosteric regulation; ATP; DNA binding; heat shock; !1hydrolase; nucleotide binding; P-loop; serine proteinase; !1stress-induced protein FEATURE !$379-386 #region nucleotide-binding motif A (P-loop)\ !$442-447 #region nucleotide-binding motif B\ !$702 #active_site Ser #status predicted SUMMARY #length 827 #molecular-weight 90438 #checksum 5169 SEQUENCE /// ENTRY D64226 #type complete TITLE endopeptidase La (EC 3.4.21.53) - Mycoplasma genitalium ALTERNATE_NAMES ATP-dependent proteinase lon; ATP-dependent serine proteinase La CONTAINS adenosinetriphosphatase (EC 3.6.1.3) ORGANISM #formal_name Mycoplasma genitalium DATE 09-Apr-1999 #sequence_revision 09-Apr-1999 #text_change 19-Jan-2001 ACCESSIONS D64226 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession D64226 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-795 ##label TIGR !'##cross-references GB:U39702; GB:L43967; NID:g1045928; PID:g1045929; !1TIGR:MG239 !'##experimental_source strain G-37 COMMENT This enzyme catalyzes the hydrolysis of large proteins in !1the presence of ATP and Mg++. The enzyme is induced by !1accumulation of abnormal proteins at high temperature. GENETICS !$#gene lon !$#genetic_code SGC3 CLASSIFICATION #superfamily ATP-dependent serine proteinase La KEYWORDS ATP; DNA binding; heat shock; hydrolase; nucleotide binding; !1P-loop; serine proteinase; stress-induced protein FEATURE !$379-386 #region nucleotide-binding motif A (P-loop)\ !$442-447 #region nucleotide-binding motif B\ !$702 #active_site Ser #status predicted SUMMARY #length 795 #molecular-weight 89987 #checksum 7802 SEQUENCE /// ENTRY S73830 #type complete TITLE endopeptidase La (EC 3.4.21.53) - Mycoplasma pneumoniae (strain ATCC 29342) ALTERNATE_NAMES ATP-dependent proteinase lon; ATP-dependent serine proteinase La; hypothetical protein F10_orf795 CONTAINS adenosinetriphosphatase (EC 3.6.1.3) ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 09-Apr-1999 #sequence_revision 09-Apr-1999 #text_change 19-Jan-2001 ACCESSIONS S73830 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73830 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-795 ##label HIM !'##cross-references EMBL:AE000050; GB:U00089; NID:g1674197; !1PIDN:AAB96152.1; PID:g1674198 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 COMMENT This enzyme catalyzes the hydrolysis of large proteins in !1the presence of ATP and Mg++. The enzyme is induced by !1accumulation of abnormal proteins at high temperature. GENETICS !$#gene lon; F10_orf795 !$#genetic_code SGC3 CLASSIFICATION #superfamily ATP-dependent serine proteinase La KEYWORDS ATP; DNA binding; heat shock; hydrolase; nucleotide binding; !1P-loop; serine proteinase; stress-induced protein FEATURE !$379-386 #region nucleotide-binding motif A (P-loop)\ !$442-447 #region nucleotide-binding motif B\ !$702 #active_site Ser #status predicted SUMMARY #length 795 #molecular-weight 90203 #checksum 5194 SEQUENCE /// ENTRY D70176 #type complete TITLE endopeptidase La (EC 3.4.21.53) 2 - Lyme disease spirochete ALTERNATE_NAMES ATP-dependent proteinase lon-2; ATP-dependent serine proteinase La CONTAINS adenosinetriphosphatase (EC 3.6.1.3) ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 09-Apr-1999 #sequence_revision 09-Apr-1999 #text_change 19-Jan-2001 ACCESSIONS D70176 REFERENCE A70100 !$#authors Fraser, C.M.; Casjens, S.; Huang, W.M.; Sutton, G.G.; !1Clayton, R.; Lathigra, R.; White, O.; Ketchum, K.A.; Dodson, !1R.; Hickey, E.K.; Gwinn, M.; Dougherty, B.; Tomb, J.F.; !1Fleischmann, R.D.; Richardson, D.; Peterson, J.; Kerlavage, !1A.R.; Quackenbush, J.; Salzberg, S.; Hanson, M.; Vugt, R.V.; !1Palmer, N.; Adams, M.D.; Gocayne, J.; Weidman, J.; !1Utterback, T.; Watthey, L.; McDonald, L.; Artiach, P.; !1Bowman, C.; Garland, S.; Fujii, C.; Cotton, M.D.; Horst, K.; !1Roberts, K.; Hatch, B.; Smith, H.O.; Venter, J.C. !$#journal Nature (1997) 390:580-586 !$#title Genomic sequence of a Lyme disease spirochaete, Borrelia !1burgdorferi. !$#cross-references MUID:98065943; PMID:9403685 !$#accession D70176 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-813 ##label KLE !'##cross-references GB:AE001162; GB:AE000783; NID:g2688528; !1PIDN:AAC66962.1; PID:g2688530; TIGR:BB0613 !'##experimental_source strain B31 COMMENT This enzyme catalyzes the hydrolysis of large proteins in !1the presence of ATP and Mg++. The enzyme is induced by !1accumulation of abnormal proteins at high temperature. GENETICS !$#gene lon-2 CLASSIFICATION #superfamily ATP-dependent serine proteinase La KEYWORDS ATP; DNA binding; heat shock; hydrolase; nucleotide binding; !1P-loop; serine proteinase; stress-induced protein FEATURE !$369-376 #region nucleotide-binding motif A (P-loop)\ !$432-437 #region nucleotide-binding motif B\ !$719 #active_site Ser #status predicted SUMMARY #length 813 #molecular-weight 92311 #checksum 9342 SEQUENCE /// ENTRY C64692 #type complete TITLE endopeptidase La (EC 3.4.21.53) - Helicobacter pylori (strain 26695) ALTERNATE_NAMES ATP-dependent proteinase lon; ATP-dependent serine proteinase La CONTAINS adenosinetriphosphatase (EC 3.6.1.3) ORGANISM #formal_name Helicobacter pylori DATE 09-Apr-1999 #sequence_revision 09-Apr-1999 #text_change 19-Jan-2001 ACCESSIONS C64692 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession C64692 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-835 ##label TOM !'##cross-references GB:AE000638; GB:AE000511; NID:g2314547; !1PIDN:AAD08421.1; PID:g2314549; TIGR:HP1379 COMMENT This enzyme catalyzes the hydrolysis of large proteins in !1the presence of ATP and Mg++. The enzyme is induced by !1accumulation of abnormal proteins at high temperature. CLASSIFICATION #superfamily ATP-dependent serine proteinase La KEYWORDS ATP; DNA binding; heat shock; hydrolase; nucleotide binding; !1P-loop; serine proteinase; stress-induced protein FEATURE !$367-374 #region nucleotide-binding motif A (P-loop)\ !$430-435 #region nucleotide-binding motif B\ !$741 #active_site Ser #status predicted SUMMARY #length 835 #molecular-weight 94418 #checksum 9250 SEQUENCE /// ENTRY A71825 #type complete TITLE endopeptidase La (EC 3.4.21.53) - Helicobacter pylori (strain J99) ALTERNATE_NAMES ATP-dependent proteinase lon; ATP-dependent serine proteinase La CONTAINS adenosinetriphosphatase (EC 3.6.1.3) ORGANISM #formal_name Helicobacter pylori #variety strain J99 DATE 09-Apr-1999 #sequence_revision 09-Apr-1999 #text_change 19-Jan-2001 ACCESSIONS A71825 REFERENCE A71800 !$#authors Alm, R.A.; Ling, L.S.L.; Moir, D.T.; King, B.L.; Brown, !1E.D.; Doig, P.C.; Smith, D.R.; Noonan, B.; Guild, B.C.; !1deJonge, B.L.; Carmel, G.; Tummino, P.J.; Caruso, A.; !1Uria-Nickelsen, M.; Mills, D.M.; Ives, C.; Gibson, R.; !1Merberg, D.; Mills, S.D.; Jiang, Q.; Taylor, D.E.; Vovis, !1G.F.; Trust, T.J. !$#journal Nature (1999) 397:176-180 !$#title Genomic sequence comparison of two unrelated isolates of the !1human gastric pathogen Helicobacter pylori. !$#cross-references MUID:99120557; PMID:9923682 !$#accession A71825 !'##status preliminary !'##molecule_type DNA !'##residues 1-831 ##label ARN !'##cross-references GB:AE001552; GB:AE001439; NID:g4155898; !1PIDN:AAD06875.1; PID:g4155905 !'##experimental_source strain J99 COMMENT This enzyme catalyzes the hydrolysis of large proteins in !1the presence of ATP and Mg++. The enzyme is induced by !1accumulation of abnormal proteins at high temperature. GENETICS !$#gene lon CLASSIFICATION #superfamily ATP-dependent serine proteinase La KEYWORDS ATP; DNA binding; heat shock; hydrolase; nucleotide binding; !1P-loop; serine proteinase; stress-induced protein FEATURE !$367-374 #region nucleotide-binding motif A (P-loop)\ !$430-435 #region nucleotide-binding motif B\ !$737 #active_site Ser #status predicted SUMMARY #length 831 #molecular-weight 93946 #checksum 4146 SEQUENCE /// ENTRY C71527 #type complete TITLE endopeptidase La (EC 3.4.21.53) - Chlamydia trachomatis (serotype D, strain UW3/Cx) ALTERNATE_NAMES ATP-dependent proteinase lon; ATP-dependent serine proteinase La CONTAINS adenosinetriphosphatase (EC 3.6.1.3) ORGANISM #formal_name Chlamydia trachomatis DATE 09-Apr-1999 #sequence_revision 09-Apr-1999 #text_change 19-Jan-2001 ACCESSIONS C71527 REFERENCE A71570 !$#authors Stephens, R.S.; Kalman, S.; Lammel, C.J.; Fan, J.; Marathe, !1R.; Aravind, L.; Mitchell, W.P.; Olinger, L.; Tatusov, R.L.; !1Zhao, Q.; Koonin, E.V.; Davis, R.W. !$#journal Science (1998) 282:754-759 !$#title Genome sequence of an obligate intracellular pathogen of !1humans: Chlamydia trachomatis. !$#cross-references MUID:99000809; PMID:9784136 !$#accession C71527 !'##status preliminary !'##molecule_type DNA !'##residues 1-819 ##label ARN !'##cross-references GB:AE001307; GB:AE001273; NID:g3328757; !1PIDN:AAC67939.1; PID:g3328764 !'##experimental_source serotype D, strain UW-3/Cx COMMENT This enzyme catalyzes the hydrolysis of large proteins in !1the presence of ATP and Mg++. The enzyme is induced by !1accumulation of abnormal proteins at high temperature. GENETICS !$#gene lon CLASSIFICATION #superfamily ATP-dependent serine proteinase La KEYWORDS ATP; DNA binding; heat shock; hydrolase; nucleotide binding; !1P-loop; serine proteinase; stress-induced protein FEATURE !$392-399 #region nucleotide-binding motif A (P-loop)\ !$455-460 #region nucleotide-binding motif B\ !$724 #active_site Ser #status predicted SUMMARY #length 819 #molecular-weight 91964 #checksum 509 SEQUENCE /// ENTRY B72128 #type complete TITLE endopeptidase La (EC 3.4.21.53) - Chlamydophila pneumoniae (strains CWL029 and AR39) ALTERNATE_NAMES ATP-dependent proteinase lon; ATP-dependent serine proteinase La CONTAINS adenosinetriphosphatase (EC 3.6.1.3) ORGANISM #formal_name Chlamydophila pneumoniae, Chlamydia pneumoniae DATE 30-Apr-1999 #sequence_revision 30-Apr-1999 #text_change 19-Jan-2001 ACCESSIONS B72128; C81543 REFERENCE A72000 !$#authors Kalman, S.; Mitchell, W.; Marathe, R.; Lammel, C.; Fan, J.; !1Olinger, L.; Grimwood, J.; Davis, R.W.; Stephens, R.S. !$#journal Nature Genet. (1999) 21:385-389 !$#title Comparative genomes of Clamydia pneumoniae and C. !1trachomatis. !$#cross-references MUID:99206606; PMID:10192388 !$#accession B72128 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-819 ##label ARN !'##cross-references GB:AE001588; GB:AE001363; NID:g4376277; !1PIDN:AAD18180.1; PID:g4376280 !'##experimental_source strain CWL029 REFERENCE A81500 !$#authors Read, T.D.; Brunham, R.C.; Shen, C.; Gill, S.R.; Heidelberg, !1J.F.; White, O.; Hickey, E.K.; Peterson, J.; Utterback, T.; !1Berry, K.; Bass, S.; Linher, K.; Weidman, J.; Khouri, H.; !1Craven, B.; Bowman, C.; Dodson, R.; Gwinn, M.; Nelson, W.; !1DeBoy, R.; Kolonay, J.; McClarty, G.; Salzberg, S.L.; Eisen, !1J.; Fraser, C.M. !$#journal Nucleic Acids Res. (2000) 28:1397-1406 !$#title Genome sequences of Chlamydia trachomatis MoPn and Chlamydia !1pneumoniae AR39. !$#cross-references MUID:20150255; PMID:10684935 !$#accession C81543 !'##molecule_type DNA !'##residues 1-819 ##label REA !'##cross-references GB:AE002233; GB:AE002161; NID:g7189657; !1PIDN:AAF38554.1; PID:g7189665; GSPDB:GN00122; TIGR:CP0749 !'##experimental_source strain AR39, HL cells COMMENT This enzyme catalyzes the hydrolysis of large proteins in !1the presence of ATP and Mg++. The enzyme is induced by !1accumulation of abnormal proteins at high temperature. GENETICS !$#gene lon; CP0749 CLASSIFICATION #superfamily ATP-dependent serine proteinase La KEYWORDS ATP; DNA binding; heat shock; hydrolase; nucleotide binding; !1P-loop; serine proteinase; stress-induced protein FEATURE !$393-400 #region nucleotide-binding motif A (P-loop)\ !$456-461 #region nucleotide-binding motif B\ !$723 #active_site Ser #status predicted SUMMARY #length 819 #molecular-weight 92275 #checksum 3072 SEQUENCE /// ENTRY B71316 #type complete TITLE endopeptidase La (EC 3.4.21.53) 2 - syphilis spirochete ALTERNATE_NAMES ATP-dependent proteinase lon-2; ATP-dependent serine proteinase La CONTAINS adenosinetriphosphatase (EC 3.6.1.3) ORGANISM #formal_name Treponema pallidum subsp. pallidum #common_name syphilis spirochete DATE 09-Apr-1999 #sequence_revision 09-Apr-1999 #text_change 19-Jan-2001 ACCESSIONS B71316 REFERENCE A71250 !$#authors Fraser, C.M.; Norris, S.J.; Weinstock, G.M.; White, O.; !1Sutton, G.G.; Dodson, R.; Gwinn, M.; Hickey, E.K.; Clayton, !1R.; Ketchum, K.A.; Sodergren, E.; Hardham, J.M.; McLeod, !1M.P.; Salzberg, S.; Peterson, J.; Khalak, H.; Richardson, !1D.; Howell, J.K.; Chidambaram, M.; Utterback, T.; McDonald, !1L.; Artiach, P.; Bowman, C.; Cotton, M.D.; Fujii, C.; !1Garland, S.; Hatch, B.; Horst, K.; Roberts, K.; Watthey, L.; !1Weidman, J.; Smith, H.O.; Venter, J.C. !$#journal Science (1998) 281:375-388 !$#title Complete genome sequence of Treponema pallidum, the syphilis !1spirochete. !$#cross-references MUID:98332770; PMID:9665876 !$#accession B71316 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-881 ##label COL !'##cross-references GB:AE001227; GB:AE000520; NID:g3322797; !1PIDN:AAC65510.1; PID:g3322814 !'##experimental_source strain Nichols COMMENT This enzyme catalyzes the hydrolysis of large proteins in !1the presence of ATP and Mg++. The enzyme is induced by !1accumulation of abnormal proteins at high temperature. GENETICS !$#gene TP0524; lon-2 CLASSIFICATION #superfamily ATP-dependent serine proteinase La KEYWORDS ATP; DNA binding; heat shock; hydrolase; nucleotide binding; !1P-loop; serine proteinase; stress-induced protein FEATURE !$440-447 #region nucleotide-binding motif A (P-loop)\ !$503-508 #region nucleotide-binding motif B\ !$767 #active_site Ser #status predicted SUMMARY #length 881 #molecular-weight 97727 #checksum 3206 SEQUENCE /// ENTRY E70131 #type complete TITLE endopeptidase La (EC 3.4.21.53) 1 - Lyme disease spirochete ALTERNATE_NAMES ATP-dependent proteinase lon-1; ATP-dependent serine proteinase La CONTAINS adenosinetriphosphatase (EC 3.6.1.3) ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 09-Apr-1999 #sequence_revision 09-Apr-1999 #text_change 19-Jan-2001 ACCESSIONS E70131 REFERENCE A70100 !$#authors Fraser, C.M.; Casjens, S.; Huang, W.M.; Sutton, G.G.; !1Clayton, R.; Lathigra, R.; White, O.; Ketchum, K.A.; Dodson, !1R.; Hickey, E.K.; Gwinn, M.; Dougherty, B.; Tomb, J.F.; !1Fleischmann, R.D.; Richardson, D.; Peterson, J.; Kerlavage, !1A.R.; Quackenbush, J.; Salzberg, S.; Hanson, M.; Vugt, R.V.; !1Palmer, N.; Adams, M.D.; Gocayne, J.; Weidman, J.; !1Utterback, T.; Watthey, L.; McDonald, L.; Artiach, P.; !1Bowman, C.; Garland, S.; Fujii, C.; Cotton, M.D.; Horst, K.; !1Roberts, K.; Hatch, B.; Smith, H.O.; Venter, J.C. !$#journal Nature (1997) 390:580-586 !$#title Genomic sequence of a Lyme disease spirochaete, Borrelia !1burgdorferi. !$#cross-references MUID:98065943; PMID:9403685 !$#accession E70131 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-806 ##label KLE !'##cross-references GB:AE001135; GB:AE000783; NID:g2688144; !1PIDN:AAB91493.1; PID:g2688145; TIGR:BB0253 !'##experimental_source strain B31 COMMENT This enzyme catalyzes the hydrolysis of large proteins in !1the presence of ATP and Mg++. The enzyme is induced by !1accumulation of abnormal proteins at high temperature. CLASSIFICATION #superfamily ATP-dependent serine proteinase La KEYWORDS ATP; DNA binding; heat shock; hydrolase; nucleotide binding; !1P-loop; serine proteinase; stress-induced protein FEATURE !$389-396 #region nucleotide-binding motif A (P-loop)\ !$452-457 #region nucleotide-binding motif B\ !$714 #active_site Ser #status predicted SUMMARY #length 806 #molecular-weight 90709 #checksum 9528 SEQUENCE /// ENTRY H64476 #type complete TITLE endopeptidase La homolog (EC 3.4.21.-) - Methanococcus jannaschii ALTERNATE_NAMES ATP-dependent proteinase lon homolog ORGANISM #formal_name Methanococcus jannaschii DATE 30-Apr-1999 #sequence_revision 30-Apr-1999 #text_change 19-Jan-2001 ACCESSIONS H64476 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession H64476 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-649 ##label BUL !'##cross-references GB:U67582; GB:L77117; NID:g1592064; !1PIDN:AAB99427.1; PID:g1592066; TIGR:MJ1417 GENETICS !$#map_position FOR1378485-1380434 CLASSIFICATION #superfamily Methanococcus endopeptidase La homolog; !1Methanococcus endopeptidase La homolog P-loop-containing !1homology KEYWORDS ATP; hydrolase; nucleotide binding; P-loop; serine !1proteinase FEATURE !$6-89 #domain Methanococcus endopeptidase La homolog !8P-loop-containing homology #label MLAP\ !$47-54 #region nucleotide-binding motif A (P-loop)\ !$238-243 #region nucleotide-binding motif B\ !$550 #active_site Ser #status predicted SUMMARY #length 649 #molecular-weight 71917 #checksum 9421 SEQUENCE /// ENTRY H69204 #type complete TITLE endopeptidase La homolog (EC 3.4.21.-) - Methanobacterium thermoautotrophicum (strain Delta H) ALTERNATE_NAMES ATP-dependent proteinase lon homolog ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 30-Apr-1999 #sequence_revision 30-Apr-1999 #text_change 19-Jan-2001 ACCESSIONS H69204 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession H69204 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-644 ##label MTH !'##cross-references GB:AE000856; GB:AE000666; NID:g2621862; !1PIDN:AAB85287.1; PID:g2621875 !'##experimental_source strain Delta H GENETICS !$#gene MTH785 CLASSIFICATION #superfamily Methanococcus endopeptidase La homolog; !1Methanococcus endopeptidase La homolog P-loop-containing !1homology KEYWORDS ATP; hydrolase; nucleotide binding; P-loop; serine !1proteinase FEATURE !$31-110 #domain Methanococcus endopeptidase La homolog !8P-loop-containing homology #label MLAP\ !$71-78 #region nucleotide-binding motif A (P-loop)\ !$242-247 #region nucleotide-binding motif B\ !$524 #active_site Ser #status predicted SUMMARY #length 644 #molecular-weight 70211 #checksum 7360 SEQUENCE /// ENTRY D69295 #type complete TITLE endopeptidase La homolog (EC 3.4.21.-) - Archaeoglobus fulgidus ALTERNATE_NAMES ATP-dependent proteinase lon homolog ORGANISM #formal_name Archaeoglobus fulgidus DATE 30-Apr-1999 #sequence_revision 30-Apr-1999 #text_change 19-Jan-2001 ACCESSIONS D69295 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession D69295 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-621 ##label KLE !'##cross-references GB:AE001079; GB:AE000782; NID:g2689402; !1PIDN:AAB90868.1; PID:g2650266; TIGR:AF0364 CLASSIFICATION #superfamily Methanococcus endopeptidase La homolog; !1Methanococcus endopeptidase La homolog P-loop-containing !1homology KEYWORDS ATP; hydrolase; nucleotide binding; P-loop; serine !1proteinase FEATURE !$14-93 #domain Methanococcus endopeptidase La homolog !8P-loop-containing homology #label MLAP\ !$54-61 #region nucleotide-binding motif A (P-loop)\ !$227-232 #region nucleotide-binding motif B\ !$509 #active_site Ser #status predicted SUMMARY #length 621 #molecular-weight 68207 #checksum 207 SEQUENCE /// ENTRY E71156 #type complete TITLE endopeptidase La homolog (EC 3.4.21.-) - Pyrococcus horikoshii ALTERNATE_NAMES ATP-dependent proteinase lon homolog ORGANISM #formal_name Pyrococcus horikoshii DATE 30-Apr-1999 #sequence_revision 30-Apr-1999 #text_change 19-Jan-2001 ACCESSIONS E71156 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession E71156 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1127 ##label KAW !'##cross-references GB:AP000002; NID:g3236129; PIDN:BAA29538.1; !1PID:g3256855 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0452 CLASSIFICATION #superfamily Pyrococcus endopeptidase La homolog; !1Methanococcus endopeptidase La homolog P-loop-containing !1homology KEYWORDS ATP; hydrolase; nucleotide binding; P-loop; serine !1proteinase FEATURE !$19-98 #domain Methanococcus endopeptidase La homolog !8P-loop-containing homology #label MLAP\ !$59-66 #region nucleotide-binding motif A (P-loop)\ !$708-713 #region nucleotide-binding motif B\ !$990 #active_site Ser #status predicted SUMMARY #length 1127 #molecular-weight 126991 #checksum 1230 SEQUENCE /// ENTRY C69219 #type complete TITLE endopeptidase La-related protein - Methanobacterium thermoautotrophicum (strain Delta H) ALTERNATE_NAMES ATP-dependent proteainse lon homolog ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 30-Apr-1999 #sequence_revision 30-Apr-1999 #text_change 19-Jan-2001 ACCESSIONS C69219 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession C69219 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-501 ##label MTH !'##cross-references GB:AE000865; GB:AE000666; NID:g2621984; !1PIDN:AAB85390.1; PID:g2621987 !'##experimental_source strain Delta H COMMENT This protein is missing the characteristic serine active !1site motif. GENETICS !$#gene MTH892 CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum !1endopeptidase La-related protein; Methanococcus !1endopeptidase La homolog P-loop-containing homology KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$13-91 #domain Methanococcus endopeptidase La homolog !8P-loop-containing homology #label MLAP\ !$53-60 #region nucleotide-binding motif A (P-loop)\ !$284-289 #region nucleotide-binding motif B SUMMARY #length 501 #molecular-weight 56284 #checksum 3769 SEQUENCE /// ENTRY G69652 #type complete TITLE endopeptidase La (EC 3.4.21.-) homolog lonB - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 30-Apr-1999 #sequence_revision 30-Apr-1999 #text_change 24-May-2001 ACCESSIONS G69652; I40420 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69652 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-552 ##label KUN !'##cross-references GB:Z99118; GB:AL009126; NID:g2635200; !1PIDN:CAB14781.1; PID:g2635286 !'##experimental_source strain 168 REFERENCE I40420 !$#authors Riethdorf, S.; Volker, U.; Gerth, U.; Winkler, A.; !1Engelmann, S.; Hecker, M. !$#journal J. Bacteriol. (1994) 176:6518-6527 !$#title Cloning, nucleotide sequence, and expression of the Bacillus !1subtilis lon gene. !$#cross-references MUID:95050209; PMID:7961402 !$#accession I40420 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 499,'G',501-552 ##label RES !'##cross-references EMBL:X76424; NID:g496556; PIDN:CAA53987.1; !1PID:g695456 GENETICS !$#gene lonB CLASSIFICATION #superfamily Bacillus subtilis endopeptidase La homolog lonB KEYWORDS ATP; hydrolase; nucleotide binding; P-loop; serine !1proteinase FEATURE !$97-104 #region nucleotide-binding motif A (P-loop)\ !$182-187 #region nucleotide-binding motif B\ !$445 #active_site Ser #status predicted SUMMARY #length 552 #molecular-weight 60428 #checksum 295 SEQUENCE /// ENTRY KXHUF #type complete TITLE furin (EC 3.4.21.75) precursor - human ALTERNATE_NAMES kexin homolog; paired-basic endopeptidase; prohormone-processing endoproteinase; serine proteinase homolog fur ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 21-Jul-2000 ACCESSIONS A39552; A38424; S08226; A24892; I52283; I37395 REFERENCE A39552 !$#authors Barr, P.J.; Mason, O.B.; Landsberg, K.E.; Wong, P.A.; !1Kiefer, M.C.; Brake, A.J. !$#journal DNA Cell Biol. (1991) 10:319-328 !$#title cDNA and gene structure for a human subtilisin-like protease !1with cleavage specificity for paired basic amino acid !1residues. !$#cross-references MUID:91321735; PMID:1713771 !$#accession A39552 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-794 ##label BAR REFERENCE A38424 !$#authors Wise, R.J.; Barr, P.J.; Wong, P.A.; Kiefer, M.C.; Brake, !1A.J.; Kaufman, R.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:9378-9382 !$#title Expression of a human proprotein processing enzyme: correct !1cleavage of the von Willebrand factor precursor at a paired !1basic amino acid site. !$#cross-references MUID:91067709; PMID:2251280 !$#accession A38424 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-794 ##label WIS REFERENCE S08226 !$#authors van den Ouweland, A.M.W.; van Duijnhoven, H.L.P.; Keizer, !1G.D.; Dorssers, L.C.J.; van de Ven, W.J.M. !$#journal Nucleic Acids Res. (1990) 18:664 !$#title Structural homology between the human fur gene product and !1the subtilisin-like protease encoded by yeast KEX2. !$#cross-references MUID:90175002; PMID:2408021 !$#accession S08226 !'##molecule_type mRNA !'##residues 1-794 ##label VAN !'##cross-references EMBL:X17094; NID:g31477; PIDN:CAA34948.1; !1PID:g31478 REFERENCE A24892 !$#authors Roebroek, A.J.M.; Schalken, J.A.; Leunissen, J.A.M.; !1Onnekink, C.; Bloemers, H.P.J.; Van de Ven, W.J.M. !$#journal EMBO J. (1986) 5:2197-2202 !$#title Evolutionary conserved close linkage of the c-fes/fps !1proto-oncogene and genetic sequences encoding a !1receptor-like protein. !$#cross-references MUID:87053858; PMID:3023061 !$#accession A24892 !'##molecule_type DNA !'##residues 296-794 ##label ROE !'##cross-references EMBL:X04329; NID:g31479; PIDN:CAA27860.1; !1PID:g3892585 REFERENCE I52283 !$#authors Takahashi, S.; Kasai, K.; Hatsuzawa, K.; Kitamura, N.; !1Misumi, Y.; Ikehara, Y.; Murakami, K.; Nakayama, K. !$#journal Biochem. Biophys. Res. Commun. (1993) 195:1019-1026 !$#title A mutation of furin causes the lack of precursor-processing !1activity in human colon carcinoma LoVo cells. !$#cross-references MUID:93384545; PMID:7690548 !$#accession I52283 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 402-428,'WTQAPWWPWPRIGPQWPPSGSASSTSSPSPKTSGNGSRCGRP' !1##label RES !'##cross-references GB:S65442; NID:g415477; PIDN:AAB28140.1; !1PID:g415478 !'##experimental_source human colon carcinoma LoVo cells (non-endocrine !1cells defective in cleavage at R-X-K/R-R sites) !'##note this reports represents a mutant form that has lost !1endoproteinase activity REFERENCE I37395 !$#authors Van den Ouweland, A.M.; Van Groningen, J.J.; Roebroek, A.J.; !1Onnekink, C.; Van de Ven, W.J. !$#journal Nucleic Acids Res. (1989) 17:7101-7102 !$#title Nucleotide sequence analysis of the human fur gene. !$#cross-references MUID:89386060; PMID:2674906 !$#accession I37395 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-280 ##label RE2 !'##cross-references EMBL:X15723; NID:g31481; PIDN:CAA33745.1; !1PID:g31482 COMMENT This subtilisin-like endoproteinase removes paired basic !1residues to process precursor proteins. It contains several !1such sites near its amino end and may be autolytic. GENETICS !$#gene GDB:PACE !'##cross-references GDB:119240; OMIM:136950 !$#map_position 15q26.1-15q26.1 !$#introns 59/3; 92/3; 124/3; 168/3; 193/2; 223/1; 280/3; 351/3; 385/2; !1519/2; 561/1; 598/1 FUNCTION !$#description cleavage of precursor proteins during constitutive secretory !1pathway at R-X-K/R-R sites, as in insulin receptor or !1hepatocyte growth factor receptor CLASSIFICATION #superfamily kexin; subtilisin homology KEYWORDS glycoprotein; hydrolase; serine proteinase; transmembrane !1protein FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-794 #product furin #status predicted #label MAT\ !$27-715 #domain extracellular #status predicted #label EXT\ !$144-382 #domain subtilisin homology #label SBT\ !$716-736 #domain transmembrane #status predicted #label TMM\ !$737-794 #domain intracellular #status predicted #label INT\ !$153,194,368 #active_site Asp, His, Ser #status predicted\ !$387,440,553 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 794 #molecular-weight 86677 #checksum 4116 SEQUENCE /// ENTRY I46044 #type complete TITLE furin (EC 3.4.21.75) precursor - bovine ALTERNATE_NAMES kexin homolog; paired-basic endopeptidase; prohormone-processing endoproteinase; serine proteinase homolog fur ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 19-May-2000 #sequence_revision 19-May-2000 #text_change 19-May-2000 ACCESSIONS I46044; S41191 REFERENCE A55189 !$#authors Vey, M.; Schafer, W.; Berghofer, S.; Klenk, H.D.; Garten, W. !$#journal J. Cell Biol. (1994) 127:1829-1842 !$#title Maturation of the trans-Golgi network protease furin: !1compartmentalization of propeptide removal, substrate !1cleavage, and COOH-terminal truncation. !$#cross-references MUID:95105228; PMID:7806563 !$#accession I46044 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-797 ##label VEY !'##cross-references EMBL:X75956; NID:g439648; PIDN:CAA53569.1; !1PID:g439649 FUNCTION !$#description cleavage of precursor proteins during constitutive secretory !1pathway at R-X-K/R-R sites, as in insulin receptor or !1hepatocyte growth factor receptor CLASSIFICATION #superfamily kexin; subtilisin homology KEYWORDS glycoprotein; hydrolase; serine proteinase; transmembrane !1protein FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-797 #product furin #status predicted #label MAT\ !$27-718 #domain extracellular #status predicted #label EXT\ !$144-382 #domain subtilisin homology #label SBT\ !$719-739 #domain transmembrane #status predicted #label TMM\ !$740-797 #domain intracellular #status predicted #label INT\ !$153,194,368 #active_site Asp, His, Ser #status predicted\ !$387,440,553 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 797 #molecular-weight 87250 #checksum 2889 SEQUENCE /// ENTRY KXMSF #type complete TITLE furin (EC 3.4.21.75) precursor - mouse ALTERNATE_NAMES kexin homolog; paired-basic endopeptidase; prohormone-processing endoproteinase ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 18-Jun-1999 ACCESSIONS A23679; I49677 REFERENCE A23679 !$#authors Hatsuzawa, K.; Hosaka, M.; Nakagawa, T.; Nagase, M.; Shoda, !1A.; Murakami, K.; Nakayama, K. !$#journal J. Biol. Chem. (1990) 265:22075-22078 !$#title Structure and expression of mouse furin, a yeast !1Kex2-related protease. Lack of processing of coexpressed !1prorenin in GH-4C-1 cells. !$#cross-references MUID:91093035; PMID:2266110 !$#accession A23679 !'##molecule_type mRNA !'##residues 1-793 ##label HAT !'##cross-references GB:X54056; NID:g50996; PIDN:CAA37988.1; PID:g50997 REFERENCE I49677 !$#authors Creemers, J.J.W.; Roebroek, A.A.J.; van den Ouweland, !1A.A.M.; van Duijnhoven, H.H.L.; Van De Ven, W.W.J. !$#journal Mol. Biol. (1992) 11:127-138 !$#title Cloning and functional expression of a 4.3 kbp mouse fur !1cDNA: Evidence for differential expression. !$#accession I49677 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-745,'V',747-793 ##label RES !'##cross-references GB:L26489; NID:g432275; PIDN:AAA37643.1; !1PID:g432276 COMMENT This subtilisin-like endoproteinase removes paired basic !1residues to process precursor proteins. It contains several !1such sites near its amino end and may be autolytic. GENETICS !$#gene FUR CLASSIFICATION #superfamily kexin; subtilisin homology KEYWORDS glycoprotein; hydrolase; serine proteinase; transmembrane !1protein FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-793 #product furin #status predicted #label MAT\ !$27-714 #domain extracellular #status predicted #label EXT\ !$144-382 #domain subtilisin homology #label SBT\ !$715-735 #domain transmembrane #status predicted #label TMM\ !$736-793 #domain intracellular #status predicted #label INT\ !$153,194,368 #active_site Asp, His, Ser #status predicted\ !$387,440,553 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 793 #molecular-weight 86804 #checksum 3710 SEQUENCE /// ENTRY KXRTF #type complete TITLE furin (EC 3.4.21.75) precursor - rat ALTERNATE_NAMES kexin homolog; paired-basic endopeptidase; prohormone-processing endoproteinase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 18-Jun-1999 ACCESSIONS S13106 REFERENCE S13106 !$#authors Misumi, Y.; Sohda, M.; Ikehara, Y. !$#journal Nucleic Acids Res. (1990) 18:6719 !$#title Sequence of the cDNA encoding rat furin, a possible !1propeptide-processing endoprotease. !$#cross-references MUID:91067492; PMID:2251148 !$#accession S13106 !'##molecule_type mRNA !'##residues 1-793 ##label MIS !'##cross-references EMBL:X55660; NID:g56171; PIDN:CAA39193.1; !1PID:g56172 COMMENT This subtilisin-like endoproteinase removes paired basic !1residues to process precursor proteins. It contains several !1such sites near its amino end and may be autolytic. CLASSIFICATION #superfamily kexin; subtilisin homology KEYWORDS glycoprotein; hydrolase; serine proteinase; transmembrane !1protein FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-793 #product furin #status predicted #label MAT\ !$27-714 #domain extracellular #status predicted #label EXT\ !$144-382 #domain subtilisin homology #label SBT\ !$715-735 #domain transmembrane #status predicted #label TMM\ !$736-793 #domain intracellular #status predicted #label INT\ !$153,194,368 #active_site Asp, His, Ser #status predicted\ !$387,440,553 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 793 #molecular-weight 86652 #checksum 3134 SEQUENCE /// ENTRY A54306 #type complete TITLE proprotein convertase 4 (EC 3.4.21.-) precursor - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 19-May-2000 #sequence_revision 19-May-2000 #text_change 16-Jun-2000 ACCESSIONS A54306; A42151; D45357 REFERENCE A54306 !$#authors Mbikay, M.; Raffin-Sanson, M.L.; Tadros, H.; Sirois, F.; !1Seidah, N.G.; Chretien, M. !$#journal Genomics (1994) 20:231-237 !$#title Structure of the gene for the testis-specific proprotein !1convertase 4 and of its alternate messenger RNA isoforms. !$#cross-references MUID:94292203; PMID:8020970 !$#accession A54306 !'##status preliminary !'##molecule_type DNA !'##residues 1-655 ##label MBI !'##cross-references GB:L21210 !'##note authors translated the codon AAC for residue 65 as Asp, and CCG !1for residue 87 as Arg REFERENCE A42151 !$#authors Nakayama, K.; Kim, W.S.; Torii, S.; Hosaka, M.; Nakagawa, !1T.; Ikemizu, J.; Baba, T.; Murakami, K. !$#journal J. Biol. Chem. (1992) 267:5897-5900 !$#title Identification of the fourth member of the mammalian !1endoprotease family homologous to the yeast Kex2 protease. !1Its testis-specific expression. !$#cross-references MUID:92210552; PMID:1372895 !$#accession A42151 !'##status preliminary !'##molecule_type mRNA !'##residues 1-64,'D',66-86,'R',88-655 ##label NAK !'##cross-references GB:D01093; NID:g220563; PIDN:BAA00877.1; !1PID:g220564 REFERENCE A45357 !$#authors Seidah, N.G.; Day, R.; Hamelin, J.; Gaspar, A.; Collard, !1M.W.; Chretien, M. !$#journal Mol. Endocrinol. (1992) 6:1559-1570 !$#title Testicular expression of PC4 in the rat: molecular diversity !1of a novel germ cell-specific Kex2/subtilisin-like !1proprotein convertase. !$#cross-references MUID:93078790; PMID:1448111 !$#accession D45357 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 586-639 ##label SEI !'##note sequence extracted from NCBI backbone (NCBIP:118886) GENETICS !$#gene PC4 CLASSIFICATION #superfamily kexin; subtilisin homology KEYWORDS hydrolase; serine proteinase; testis; zymogen FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$146-384 #domain subtilisin homology #label SBT\ !$155,196,370 #active_site Asp, His, Ser #status predicted SUMMARY #length 655 #molecular-weight 73153 #checksum 1439 SEQUENCE /// ENTRY I77530 #type complete TITLE proprotein convertase 4 (EC 3.4.21.-) precursor, membrane-bound splice form - black rat ORGANISM #formal_name Rattus rattus #common_name black rat, roof rat DATE 19-May-2000 #sequence_revision 19-May-2000 #text_change 31-Dec-2000 ACCESSIONS I77530; I77531 REFERENCE A45357 !$#authors Seidah, N.G.; Day, R.; Hamelin, J.; Gaspar, A.; Collard, !1M.W.; Chretien, M. !$#journal Mol. Endocrinol. (1992) 6:1559-1570 !$#title Testicular expression of PC4 in the rat: molecular diversity !1of a novel germ cell-specific Kex2/subtilisin-like !1proprotein convertase. !$#cross-references MUID:93078790; PMID:1448111 !$#accession I77530 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-678 ##label RES !'##cross-references GB:L14937; NID:g294607; PIDN:AAA41815.1; !1PID:g294609 !$#accession I77531 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-590,601-678 ##label RE2 !'##cross-references GB:L14937; NID:g294607; PIDN:AAA41814.1; !1PID:g294608 COMMENT For an alternative splice form, see PIR:A45357. GENETICS !$#introns 589/3 CLASSIFICATION #superfamily kexin; subtilisin homology KEYWORDS alternative splicing; hydrolase; serine proteinase; !1transmembrane protein; zymogen FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$146-384 #domain subtilisin homology #label SBT\ !$660-676 #domain transmembrane #status predicted #label TMM SUMMARY #length 678 #molecular-weight 75739 #checksum 3857 SEQUENCE /// ENTRY KXHUC2 #type complete TITLE proprotein convertase 2 (EC 3.4.21.94) precursor - human ALTERNATE_NAMES furin homolog PC2; kexin homolog PC2; prohormone convertase PC2 ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1992 #sequence_revision 19-May-1995 #text_change 19-May-2000 ACCESSIONS A45382; A35062 REFERENCE A45382 !$#authors Ohagi, S.; LaMendola, J.; LeBeau, M.M.; Espinosa III, R.; !1Takeda, J.; Smeekens, S.P.; Chan, S.J.; Steiner, D.F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:4977-4981 !$#title Identification and analysis of the gene encoding human PC2, !1a prohormone convertase expressed in neuroendocrine tissues. !$#cross-references MUID:92279249; PMID:1594602 !$#accession A45382 !'##molecule_type DNA !'##residues 1-638 ##label OHA !'##cross-references GB:M95971; GB:M90702; NID:g189129; PIDN:AAA59919.1; !1PID:g189131 !'##note sequence extracted from NCBI backbone (NCBIN:104351, !1NCBIP:104350) REFERENCE A35062 !$#authors Smeekens, S.P.; Steiner, D.F. !$#journal J. Biol. Chem. (1990) 265:2997-3000 !$#title Identification of a human insulinoma cDNA encoding a novel !1mammalian protein structurally related to the yeast dibasic !1processing protease Kex2. !$#cross-references MUID:90153937; PMID:2154467 !$#accession A35062 !'##molecule_type mRNA !'##residues 1-282,'DV',285-638 ##label SME !'##cross-references GB:J05252; NID:g189651; PIDN:AAA60032.1; !1PID:g189652 COMMENT This calcium-dependent enzyme is a member of a family of !1subtilisin-like proteinases responsible for tissue-specific !1processing of protein precursor molecules before and after !1paired basic residues. COMMENT This protein lacks a classical hydrophobic transmembrane !1segment but may associate with the membrane by other means. GENETICS !$#gene GDB:PCSK2; NEC2 !'##cross-references GDB:128519; OMIM:162151 !$#map_position 20p11.2-20p11.2 !$#introns 59/3; 94/3; 132/3; 169/1; 181/3; 207/2; 237/1; 295/3; 367/3; !1401/2; 477/3 CLASSIFICATION #superfamily kexin; subtilisin homology KEYWORDS glycoprotein; hydrolase; serine proteinase FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-109 #domain propeptide #status predicted #label PRO\ !$110-638 #product prohormone-processing proteinase PC2 #status !8predicted #label MAT\ !$158-398 #domain subtilisin homology #label SBT\ !$167,208,384 #active_site Asp, His, Ser #status predicted\ !$375,514,524 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 638 #molecular-weight 70565 #checksum 1609 SEQUENCE /// ENTRY KXMSC2 #type complete TITLE proprotein convertase 2 (EC 3.4.21.94) precursor - mouse ALTERNATE_NAMES furin homolog PC2; kexin homolog PC2; prohormone convertase PC2 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-May-2000 ACCESSIONS B35571 REFERENCE A35571 !$#authors Seidah, N.G.; Gaspar, L.; Mion, P.; Marcinkiewicz, M.; !1Mbikay, M.; Chretien, M. !$#journal DNA Cell Biol. (1990) 9:415-424 !$#title cDNA sequence of two distinct pituitary proteins homologous !1to Kex2 and furin gene products: tissue-specific mRNAs !1encoding candidates for pro-hormone processing proteinases. !$#cross-references MUID:91000356; PMID:2169760 !$#accession B35571 !'##molecule_type mRNA !'##residues 1-637 ##label SEI !'##cross-references GB:M55669; NID:g198591; PIDN:AAA39376.1; !1PID:g198592 COMMENT This protein is a member of a family of subtilisin-like !1proteinases responsible for tissue-specific processing of !1protein precursor molecules before and after paired basic !1residues. COMMENT This protein lacks a classical hydrophobic transmembrane !1segment but may associate with the membrane by other means. CLASSIFICATION #superfamily kexin; subtilisin homology KEYWORDS glycoprotein; hydrolase; serine proteinase FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-108 #domain propeptide #status predicted #label PRO\ !$109-637 #product prohormone-processing proteinase PC2 #status !8predicted #label MAT\ !$157-397 #domain subtilisin homology #label SBT\ !$166,207,383 #active_site Asp, His, Ser #status predicted\ !$513,523 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 637 #molecular-weight 70785 #checksum 1997 SEQUENCE /// ENTRY KXRTC2 #type complete TITLE proprotein convertase 2 (EC 3.4.21.94) precursor - rat ALTERNATE_NAMES furin homolog PC2; kexin homolog PC2; prohormone convertase PC2; type 2 proinsulin processing endopeptidase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-May-2000 ACCESSIONS B41556; S27362; S36359; A42751 REFERENCE A41556 !$#authors Bloomquist, B.T.; Eipper, B.A.; Mains, R.E. !$#journal Mol. Endocrinol. (1991) 5:2014-2024 !$#title Prohormone-converting enzymes: regulation and evaluation of !1function using antisense RNA. !$#cross-references MUID:92168040; PMID:1791845 !$#accession B41556 !'##molecule_type mRNA !'##residues 1-637 ##label BLO !'##cross-references GB:M76706; NID:g457370; PIDN:AAA40946.1; !1PID:g203511 REFERENCE S27361 !$#authors Hakes, D.J.; Birch, N.P.; Mezey, A.; Dixon, J.E. !$#journal Endocrinology (1991) 129:3053-3063 !$#title Isolation of two complementary deoxyribonucleic acid clones !1from a rat insulinoma cell line based on similarities to !1Kex2 and furin sequences and the specific localization of !1each transcript to endocrine and neuroendocrine tissues in !1rats. !$#cross-references MUID:92063860; PMID:1954888 !$#accession S27362 !'##molecule_type mRNA !'##residues 1-341,'H',343-637 ##label HAK !'##cross-references EMBL:M83746 REFERENCE S36358 !$#authors Hakes, D.J.; Birch, N.P.; Mezey, A.; Dixon, J.E. !$#submission submitted to the EMBL Data Library, February 1992 !$#accession S36359 !'##molecule_type mRNA !'##residues 1-320,'I',321-341,'H',343-637 ##label HA2 !'##cross-references EMBL:M83746; NID:g205064; PIDN:AAA41477.1; !1PID:g205065 REFERENCE A42751 !$#authors Bennett, D.L.; Bailyes, E.M.; Nielsen, E.; Guest, P.C.; !1Rutherford, N.G.; Arden, S.D.; Hutton, J.C. !$#journal J. Biol. Chem. (1992) 267:15229-15236 !$#title Identification of the type 2 proinsulin processing !1endopeptidase as PC2, a member of the eukaryote subtilisin !1family. !$#cross-references MUID:92340579; PMID:1634553 !$#accession A42751 !'##molecule_type mRNA !'##residues 'IP',162-360,'S',362-388,'NS' ##label BEN !'##cross-references GB:S40669; NID:g252085; PIDN:AAB22663.1; !1PID:g252086 !'##experimental_source insulinoma !'##note sequence extracted from NCBI backbone (NCBIN:109491, !1NCBIP:109492) !'##note sequences of amino ends of mature forms determined !'##note mature form is glycosylated !'##note found in pancreatic islets neurointermediate and anterior !1pituitary COMMENT This calcium-dependent enzyme is a member of a family of !1subtilisin-like proteinases responsible for tissue-specific !1processing of protein precursor molecules before and after !1paired basic residues. COMMENT This protein lacks a classical hydrophobic transmembrane !1segment but may associate with the membrane by other means. CLASSIFICATION #superfamily kexin; subtilisin homology KEYWORDS glycoprotein; hydrolase; serine proteinase FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-108 #domain propeptide #status predicted #label PRO\ !$109-637 #product prohormone-processing proteinase PC2 #status !8experimental #label MAT\ !$112-637 #product prohormone-processing proteinase PC2, !8shorter form #status experimental #label MAT2\ !$157-397 #domain subtilisin homology #label SBT\ !$166,207,383 #active_site Asp, His, Ser #status predicted\ !$374,513,523 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 637 #molecular-weight 70753 #checksum 2497 SEQUENCE /// ENTRY KXHUC1 #type complete TITLE proprotein convertase 1 (EC 3.4.21.93) precursor - human ALTERNATE_NAMES prohormone convertase 1 (PC1); proprotein-processing enzyme; type I endoproteinase ORGANISM #formal_name Homo sapiens #common_name man DATE 22-Nov-1993 #sequence_revision 06-Sep-1996 #text_change 19-May-2000 ACCESSIONS S21106; I52991 REFERENCE S21106 !$#authors Creemers, J.W.M.; Roebroek, A.J.M.; van de Ven, W.J.M. !$#journal FEBS Lett. (1992) 300:82-88 !$#title Expression in human lung tumor cells of the proprotein !1processing enzyme PC1/PC3. Cloning and primary sequence of a !15 kb cDNA. !$#cross-references MUID:92192290; PMID:1547893 !$#accession S21106 !'##molecule_type mRNA !'##residues 1-753 ##label CRE !'##cross-references EMBL:X64810; GB:S88573; NID:g35317; !1PIDN:CAA46031.1; PID:g35318 REFERENCE I52991 !$#authors Seidah, N.G.; Hamelin, J.; Gaspar, A.M.; Day, R.; Chretien, !1M. !$#journal DNA Cell Biol. (1992) 11:283-289 !$#title The cDNA sequence of the human pro-hormone and pro-protein !1convertase PC1. !$#cross-references MUID:92297154; PMID:1605851 !$#accession I52991 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-356,'S',358-753 ##label RES !'##cross-references GB:M90753; NID:g189116; PIDN:AAA59918.1; !1PID:g189117 GENETICS !$#gene GDB:PCSK1; NEC1 !'##cross-references GDB:128033; OMIM:162150 !$#map_position 5q15-5q21 FUNCTION !$#description endoproteinase hydrolyzing the carboxyl peptide bond of a !1pair of arginine residues CLASSIFICATION #superfamily kexin; subtilisin homology KEYWORDS glycoprotein; hydrolase; serine proteinase FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-110 #domain propeptide #status predicted #label PRO\ !$111-753 #product prohormone-processing proteinase PC1/PC3 !8#status predicted #label MAT\ !$158-396 #domain subtilisin homology #label SBT\ !$739-751 #domain amphipathic helix #status predicted #label !8APH\ !$167,208,382 #active_site Asp, His, Ser #status predicted\ !$173,401 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 753 #molecular-weight 84121 #checksum 9989 SEQUENCE /// ENTRY KXRTC1 #type complete TITLE proprotein convertase 1 (EC 3.4.21.93) precursor - rat ALTERNATE_NAMES furin homolog PC1; kexin homolog PC1; prohormone cleavage enzyme; prohormone convertase 1; prohormone-processing endoproteinase PC3; prohormone-processing proteinase BDP ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-May-2000 ACCESSIONS A41556; S27361; S36358 REFERENCE A41556 !$#authors Bloomquist, B.T.; Eipper, B.A.; Mains, R.E. !$#journal Mol. Endocrinol. (1991) 5:2014-2024 !$#title Prohormone-converting enzymes: regulation and evaluation of !1function using antisense RNA. !$#cross-references MUID:92168040; PMID:1791845 !$#accession A41556 !'##molecule_type mRNA !'##residues 1-752 ##label BLO !'##cross-references GB:M76705; NID:g203508; PIDN:AAA40945.1; !1PID:g203509 REFERENCE S27361 !$#authors Hakes, D.J.; Birch, N.P.; Mezey, A.; Dixon, J.E. !$#journal Endocrinology (1991) 129:3053-3063 !$#title Isolation of two complementary deoxyribonucleic acid clones !1from a rat insulinoma cell line based on similarities to !1Kex2 and furin sequences and the specific localization of !1each transcript to endocrine and neuroendocrine tissues in !1rats. !$#cross-references MUID:92063860; PMID:1954888 !$#accession S27361 !'##molecule_type mRNA !'##residues 1-513,'A',515-752 ##label HAK !'##cross-references EMBL:M83745 REFERENCE S36358 !$#authors Hakes, D.J.; Birch, N.P.; Mezey, A.; Dixon, J.E. !$#submission submitted to the EMBL Data Library, February 1992 !$#accession S36358 !'##molecule_type mRNA !'##residues 1-366,'T',367-513,'A',515-752 ##label HA2 !'##cross-references EMBL:M83745; NID:g205062; PIDN:AAA41476.1; !1PID:g205063 COMMENT This protein is a member of a family of subtilisin-like !1proteinases responsible for tissue-specific processing of !1protein precursor molecules before and after paired basic !1residues. COMMENT This protein lacks a classical hydrophobic transmembrane !1segment but may associate with the membrane by other means. CLASSIFICATION #superfamily kexin; subtilisin homology KEYWORDS glycoprotein; hydrolase; serine proteinase FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-110 #domain propeptide #status predicted #label PRO\ !$111-752 #product prohormone-processing proteinase PC1 #status !8predicted #label MAT\ !$158-396 #domain subtilisin homology #label SBT\ !$167,208,382 #active_site Asp, His, Ser #status predicted\ !$173,401,645 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 752 #molecular-weight 84120 #checksum 5235 SEQUENCE /// ENTRY KXMSC1 #type complete TITLE proprotein convertase 1 (EC 3.4.21.93) precursor - mouse ALTERNATE_NAMES furin homolog PC1; kexin homolog PC1; prohormone cleavage enzyme; prohormone convertase 1; prohormone-processing endoproteinase PC3 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-May-2000 ACCESSIONS JX0171; S19165; A39604; A35571; A39002; A37951; A46622 REFERENCE JX0171 !$#authors Nakayama, K.; Hosaka, M.; Hatsuzawa, K.; Murakami, K. !$#journal J. Biochem. (1991) 109:803-806 !$#title Cloning and functional expression of a novel endoprotease !1involved in prohormone processing at dibasic sites. !$#cross-references MUID:92041727; PMID:1657897 !$#accession JX0171 !'##molecule_type mRNA !'##residues 1-753 ##label NAK !'##experimental_source pituitary AtT-20 cells REFERENCE S19165 !$#authors Nakayama, K. !$#submission submitted to the EMBL Data Library, December 1990 !$#accession S19165 !'##molecule_type mRNA !'##residues 1-111,'F',113-116,'P',118-121,'T',123-127,'H',129-281,'K', !1283-731,'E',733-753 ##label NA2 !'##cross-references EMBL:X57088; NID:g50054; PIDN:CAA40368.1; !1PID:g50055 REFERENCE A39604 !$#authors Korner, J.; Chun, J.; Harter, D.; Axel, R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:6834-6838 !$#title Isolation and functional expression of a mammalian !1prohormone processing enzyme, murine prohormone convertase !11. !$#cross-references MUID:91319778; PMID:1862107 !$#accession A39604 !'##molecule_type mRNA !'##residues 1-609 ##label KOR !'##cross-references GB:M69196 REFERENCE A35571 !$#authors Seidah, N.G.; Gaspar, L.; Mion, P.; Marcinkiewicz, M.; !1Mbikay, M.; Chretien, M. !$#journal DNA Cell Biol. (1990) 9:415-424 !$#title cDNA sequence of two distinct pituitary proteins homologous !1to Kex2 and furin gene products: tissue-specific mRNAs !1encoding candidates for pro-hormone processing proteinases. !$#cross-references MUID:91000356; PMID:2169760 !$#accession A35571 !'##molecule_type mRNA !'##residues 214-478 ##label SEI !'##note the authors gave the codon for residue 330-Ser as CTC REFERENCE A39002 !$#authors Smeekens, S.P.; Avruch, A.S.; LaMendola, J.; Chan, S.J.; !1Steiner, D.F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:340-344 !$#title Identification of a cDNA encoding a second putative !1prohormone convertase related to PC2 in AtT20 cells and !1islets of Langerhans. !$#cross-references MUID:91110525; PMID:1988934 !$#accession A39002 !'##molecule_type mRNA !'##residues 1-22,'S',24-753 ##label SME !'##cross-references GB:M58507; NID:g200242; PIDN:AAA39896.1; !1PID:g200243 !'##experimental_source pituitary AtT-20 cells REFERENCE A37951 !$#authors Seidah, N.G.; Marcinkiewicz, M.; Benjannet, S.; Gaspar, L.; !1Beaubien, G.; Mattei, M.G.; Lazure, C.; Mbikay, M.; !1Chretien, M. !$#journal Mol. Endocrinol. (1991) 5:111-122 !$#title Cloning and primary sequence of a mouse candidate prohormone !1convertase PC1 homologous to PC2, Furin, and Kex2: distinct !1chromosomal localization and messenger RNA distribution in !1brain and pituitary compared to PC2. !$#cross-references MUID:91203919; PMID:2017186 !$#accession A37951 !'##molecule_type mRNA !'##residues 1-360,'S',362-363,'P',365-753 ##label SE2 !'##cross-references GB:M58589 REFERENCE A46622 !$#authors Zhou, Y.; Lindberg, I. !$#journal J. Biol. Chem. (1993) 268:5615-5623 !$#title Purification and characterization of the prohormone !1convertase PC1(PC3). !$#cross-references MUID:93194858; PMID:8449925 !$#accession A46622 !'##molecule_type protein !'##residues 111-120 ##label ZHO COMMENT This protein is a member of a family of subtilisin-like !1proteinases responsible for tissue-specific processing of !1protein precursor molecules before and after paired basic !1residues. COMMENT This protein lacks a classical hydrophobic transmembrane !1segment but may associate with the membrane by other means. GENETICS !$#map_position 13C CLASSIFICATION #superfamily kexin; subtilisin homology KEYWORDS glycoprotein; hydrolase; serine proteinase FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-110 #domain propeptide #status predicted #label PRO\ !$111-753 #product prohormone-processing proteinase PC1 #status !8predicted #label MAT\ !$158-396 #domain subtilisin homology #label SBT\ !$167,208,382 #active_site Asp, His, Ser #status predicted\ !$173,401,645 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 753 #molecular-weight 84173 #checksum 5211 SEQUENCE /// ENTRY KXBY #type complete TITLE kexin (EC 3.4.21.61) 2 precursor - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES KEX2 proteinase; paired-basic endopeptidase; prohormone-processing endoproteinase; prohormone-processing enzyme KEX2; protein N1122; protein YNL238w ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 21-Jul-2000 ACCESSIONS A28931; S42157; S63204; C45108; S67360; S72078 REFERENCE A28931 !$#authors Mizuno, K.; Nakamura, T.; Ohshima, T.; Tanaka, S.; Matsuo, !1H. !$#journal Biochem. Biophys. Res. Commun. (1988) 156:246-254 !$#title Yeast KEX2 gene encodes an endopeptidase homologous to !1subtilisin-like serine proteases. !$#cross-references MUID:89025851; PMID:2845974 !$#accession A28931 !'##molecule_type DNA !'##residues 1-814 ##label MIZ !'##cross-references GB:M22870; NID:g340775; PIDN:AAA34719.1; !1PID:g531007 REFERENCE S42157 !$#authors Fuller, R.S.; Brake, A.; Thorner, J. !$#submission submitted to the EMBL Data Library, May 1989 !$#description Yeast prohormone processing enzyme (KEX2 gene product) is a !1Ca2+ -dependent serine protease. !$#accession S42157 !'##molecule_type DNA !'##residues 1-814 ##label FUL !'##cross-references EMBL:M24201; NID:g171780; PIDN:AAA34718.1; !1PID:g171781 REFERENCE S63188 !$#authors Pandolfo, D.; De Antoni, A.; Lanfranchi, G.; Valle, G. !$#submission submitted to the Protein Sequence Database, April 1996 !$#accession S63204 !'##molecule_type DNA !'##residues 1-814 ##label PAN !'##cross-references EMBL:Z71514; NID:g1302269; PIDN:CAA96143.1; !1PID:g1302270; GSPDB:GN00014; MIPS:YNL238w !'##experimental_source strain S288C REFERENCE A45108 !$#authors Kambouris, N.G.; Burke, D.J.; Creutz, C.E. !$#journal J. Biol. Chem. (1992) 267:21570-21576 !$#title Cloning and characterization of a cysteine proteinase from !1Saccharomyces cerevisiae. !$#cross-references MUID:93016103; PMID:1400467 !$#accession C45108 !'##status translation not shown !'##molecule_type DNA !'##residues 1-53,'I' ##label KAM !'##cross-references GB:M97910 REFERENCE S67355 !$#authors Pandolfo, D.; de Antoni, A.; Lanfranchi, G.; Valle, G. !$#submission submitted to the EMBL Data Library, February 1996 !$#description DNA sequence of cosmid 14-5 from chromosome XIV. !$#accession S67360 !'##molecule_type DNA !'##residues 1-814 ##label PAW !'##cross-references EMBL:Z69381; NID:g1183970; PIDN:CAA93360.1; !1PID:g1183976 REFERENCE S72073 !$#authors Pandolfo, D.; de Antoni, A.; Lanfranchi, G.; Valle, G. !$#journal Yeast (1996) 12:1071-1076 !$#title The DNA sequence of cosmid 14-5 from chromosome XIV reveals !121 open reading frames including a novel gene encoding a !1globin-like domain. !$#cross-references MUID:97051596; PMID:8896273 !$#accession S72078 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-814 ##label PAF !'##cross-references EMBL:Z69381; NID:g1183970; PIDN:CAA93360.1; !1PID:g1183976 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1February 1996 COMMENT This enzyme is calcium-dependent and probably contains !1O-linked glycosylation sites as well as N-linked. GENETICS !$#gene SGD:KEX2; QDS1; MIPS:YNL238w !'##cross-references MIPS:YNL238w; SGD:S0005182 !$#map_position 14L FUNCTION !$#description kexins cleave after Lys-Arg or Arg-Arg to process !1alpha-factor, secreted toxins, and other protein precursors CLASSIFICATION #superfamily Saccharomyces kexin; subtilisin homology KEYWORDS glycoprotein; hydrolase; serine proteinase; transmembrane !1protein FEATURE !$166-399 #domain subtilisin homology #label SBT\ !$617-672 #region serine/threonine-rich\ !$679-699 #domain transmembrane #status predicted #label TMM\ !$700-814 #domain intracellular #status predicted #label INT\ !$42,146,163,404,480 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$175,213,385 #active_site Asp, His, Ser #status predicted SUMMARY #length 814 #molecular-weight 90002 #checksum 5495 SEQUENCE /// ENTRY S01013 #type complete TITLE kexin (EC 3.4.21.61) 1 precursor - yeast (Kluyveromyces marxianus var. lactis) ALTERNATE_NAMES KEX1 proteinase ORGANISM #formal_name Kluyveromyces marxianus var. lactis, Candida sphaerica DATE 30-Sep-1989 #sequence_revision 19-Jul-1996 #text_change 18-Jun-1999 ACCESSIONS S01013 REFERENCE S01013 !$#authors Tanguy-Rougeau, C.; Wesolowski-Louvel, M.; Fukuhara, H. !$#journal FEBS Lett. (1988) 234:464-470 !$#title The Kluyveromyces lactis KEX1 gene encodes a subtilisin-type !1serine proteinase. !$#cross-references MUID:88271677; PMID:3292294 !$#accession S01013 !'##molecule_type DNA !'##residues 1-700 ##label TAN !'##cross-references EMBL:X07038; NID:g2834; PIDN:CAA30088.1; PID:g2835 GENETICS !$#gene KEX1 FUNCTION !$#description kexins cleave after Lys-Arg or Arg-Arg to process alpha !1factor, secreted toxins, and other protein precursors !$#note mutants do not secrete killer toxin and are deficient in !1sporulation CLASSIFICATION #superfamily Saccharomyces kexin; subtilisin homology KEYWORDS glycoprotein; hydrolase; serine proteinase; transmembrane !1protein FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-700 #product kexin 1 #status predicted #label MAT\ !$155-387 #domain subtilisin homology #label SBT\ !$603-627 #region serine/threonine-rich\ !$641-661 #domain transmembrane #status predicted #label TMM\ !$662-700 #domain intracellular #status predicted #label INT\ !$121,144,152,392,538 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$164,202,373 #active_site Asp, His, Ser #status predicted SUMMARY #length 700 #molecular-weight 77600 #checksum 7372 SEQUENCE /// ENTRY A39490 #type complete TITLE subtilisin-like proprotein convertase (EC 3.4.21.-) PACE4 precursor, splice form A - human ALTERNATE_NAMES kexin homolog ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 31-Mar-2000 ACCESSIONS A39490 REFERENCE A39490 !$#authors Kiefer, M.C.; Tucker, J.E.; Joh, R.; Landsberg, K.E.; !1Saltman, D.; Barr, P.J. !$#journal DNA Cell Biol. (1991) 10:757-769 !$#title Identification of a second human subtilisin-like protease !1gene in the fes/fps region of chromosome 15. !$#cross-references MUID:92075167; PMID:1741956 !$#accession A39490 !'##molecule_type mRNA !'##residues 1-969 ##label KIE !'##cross-references GB:M80482; NID:g189531; PIDN:AAA59998.1; !1PID:g189532 GENETICS !$#gene GDB:PACE4 !'##cross-references GDB:131390; OMIM:167405 !$#map_position 15q26-15q26 CLASSIFICATION #superfamily subtilisin-like proteinase PACE4; subtilisin !1homology KEYWORDS alternative splicing; hydrolase; serine proteinase FEATURE !$150-969 #product serine proteinase PACE4 #status predicted !8#label SIG\ !$196-434 #domain subtilisin homology #label SBT\ !$205,246,420 #active_site Asp, His, Ser #status predicted SUMMARY #length 969 #molecular-weight 106419 #checksum 710 SEQUENCE /// ENTRY A48225 #type complete TITLE subtilisin-like proprotein convertase (EC 3.4.21.-) PC5 precursor - mouse ALTERNATE_NAMES kexin homolog; serine proteinase PC6 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A48225; JX0248 REFERENCE A48225 !$#authors Lusson, J.; Vieau, D.; Hamelin, J.; Day, R.; Chretien, M.; !1Seidah, N.G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:6691-6695 !$#title cDNA structure of the mouse and rat subtilisin/kexin-like !1PC5: a candidate proprotein convertase expressed in !1endocrine and nonendocrine cells. !$#cross-references MUID:93342056; PMID:8341687 !$#accession A48225 !'##status preliminary !'##molecule_type mRNA !'##residues 1-915 ##label LUS !'##cross-references GB:L14932; NID:g293327; PIDN:AAA74636.1; !1PID:g293328 REFERENCE JX0248 !$#authors Nakagawa, T.; Hosaka, M.; Torii, S.; Watanabe, T.; Murakami, !1K.; Nakayama, K. !$#journal J. Biochem. (1993) 113:132-135 !$#title Identification and functional expression of a new member of !1the mammalian Kex2-like processing endoprotease family: its !1striking structural similarity to PACE4. !$#cross-references MUID:93224489; PMID:8468318 !$#accession JX0248 !'##molecule_type mRNA !'##residues 1-915 ##label NAK !'##cross-references DDBJ:D12619; NID:g220565; PIDN:BAA02143.1; !1PID:g220566 !'##note the authors translated the codon GGC for residue 915 as Ala CLASSIFICATION #superfamily subtilisin-like proteinase PACE4; subtilisin !1homology KEYWORDS duplication; glycoprotein; hydrolase; integrin binding; !1serine proteinase FEATURE !$1-34 #domain signal sequence #status predicted #label SIG\ !$35-116 #domain propeptide #status predicted #label PRO\ !$117-915 #product proprotein convertase PC5 #status !8experimental #label MAT\ !$164-402 #domain subtilisin homology #label SBT\ !$173,214,388 #active_site Asp, His, Ser #status predicted SUMMARY #length 915 #molecular-weight 101489 #checksum 4243 SEQUENCE /// ENTRY JC2192 #type complete TITLE subtilisin-like proprotein convertase (EC 3.4.21.-) PACE4 precursor, splice form D - human ALTERNATE_NAMES kexin-like protease ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 20-Apr-2000 ACCESSIONS JC2192 REFERENCE JC2191 !$#authors Tsuji, A.; Higashine, K.; Hine, C.; Mori, K.; Tamai, Y.; !1Nagamune, H.; Matsuda, Y. !$#journal Biochem. Biophys. Res. Commun. (1994) 200:943-950 !$#title Identification of novel cDNAs encoding human kexin-like !1protease, PACE4 isoforms. !$#cross-references MUID:94235049; PMID:8179631 !$#accession JC2192 !'##molecule_type mRNA !'##residues 1-497 ##label TSU COMMENT This protein consists of a subtilisin-like catalytic domain !1and a P-domain and is not a functional protease. COMMENT This protein cleaves precursor proteins at dibasic amino !1acid residues. GENETICS !$#gene GDB:PACE4 !'##cross-references GDB:131390; OMIM:167405 !$#map_position 15q26-15q26 CLASSIFICATION #superfamily subtilisin-like proteinase PACE4; subtilisin !1homology KEYWORDS alternative splicing; hydrolase; serine proteinase FEATURE !$29-267 #domain subtilisin homology #label SBT\ !$38,79,253 #active_site Asp, His, Ser #status predicted SUMMARY #length 497 #molecular-weight 54899 #checksum 812 SEQUENCE /// ENTRY JC2191 #type complete TITLE subtilisin-like proprotein convertase (EC 3.4.21.-) PACE4 precursor, splice form C - human ALTERNATE_NAMES kexin-like protease isoform ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 20-Apr-2000 ACCESSIONS JC2191 REFERENCE JC2191 !$#authors Tsuji, A.; Higashine, K.; Hine, C.; Mori, K.; Tamai, Y.; !1Nagamune, H.; Matsuda, Y. !$#journal Biochem. Biophys. Res. Commun. (1994) 200:943-950 !$#title Identification of novel cDNAs encoding human kexin-like !1protease, PACE4 isoforms. !$#cross-references MUID:94235049; PMID:8179631 !$#accession JC2191 !'##molecule_type mRNA !'##residues 1-652 ##label TSU COMMENT This protein consists of a signal peptide, a propeptide, a !1substilisin-like catalytic domain and a homoB region !1(P-domain). COMMENT This protein cleaves precursor proteins at dibasic amino !1acid residues. GENETICS !$#gene GDB:PACE4 !'##cross-references GDB:131390; OMIM:167405 !$#map_position 15q26-15q26 CLASSIFICATION #superfamily subtilisin-like proteinase PACE4; subtilisin !1homology KEYWORDS alternative splicing; hydrolase; serine proteinase FEATURE !$196-434 #domain subtilisin homology #label SBT\ !$205,246,420 #active_site Asp, His, Ser #status predicted SUMMARY #length 652 #molecular-weight 71770 #checksum 9847 SEQUENCE /// ENTRY PPPA #type complete TITLE papain (EC 3.4.22.2) precursor - papaya ORGANISM #formal_name Carica papaya #common_name papaya DATE 24-Apr-1984 #sequence_revision 31-Mar-1992 #text_change 18-Jun-1999 ACCESSIONS A26466; A00974; A37903 REFERENCE A26466 !$#authors Cohen, L.W.; Coghlan, V.M.; Dihel, L.C. !$#journal Gene (1986) 48:219-227 !$#title Cloning and sequencing of papain-encoding cDNA. !$#cross-references MUID:87163525; PMID:2881845 !$#accession A26466 !'##molecule_type mRNA !'##residues 1-345 ##label COH !'##cross-references GB:M15203; NID:g167390; PIDN:AAB02650.1; !1PID:g167391 REFERENCE A92062 !$#authors Mitchel, R.E.J.; Chaiken, I.M.; Smith, E.L. !$#journal J. Biol. Chem. (1970) 245:3485-3492 !$#title The complete amino acid sequence of papain. Additions and !1corrections. !$#cross-references MUID:71007899; PMID:5470818 !$#accession A00974 !'##molecule_type protein !'##residues 134-179,'Q',181-196,'D',198-218,'PY',221-250,'Q',252-267, !1'Q',269-299,'N',301,'G',303-345 ##label MIT REFERENCE A93155 !$#authors Drenth, J.; Jansonius, J.N.; Koekoek, R.; Swen, H.M.; !1Wolthers, B.G. !$#journal Nature (1968) 218:929-932 !$#title Structure of papain. !$#cross-references MUID:69006973; PMID:5681232 !$#contents annotation; X-ray crystallography, 2.8 angstroms REFERENCE A37903 !$#authors Vernet, T.; Tessier, D.C.; Richardson, C.; Laliberte, F.; !1Khouri, H.E.; Bell, A.W.; Storer, A.C.; Thomas, D.Y. !$#journal J. Biol. Chem. (1990) 265:16661-16666 !$#title Secretion of functional papain precursor from insect cells. !1Requirement for N-glycosylation of the pro-region. !$#cross-references MUID:90375542; PMID:2204628 !$#accession A37903 !'##molecule_type protein !'##residues 27-39 ##label VER !'##experimental_source recombinant gene expression in a baculovirus/ !1insect cell system CLASSIFICATION #superfamily papain KEYWORDS cysteine proteinase; hydrolase FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-133 #domain propeptide #status predicted #label PPT\ !$134-345 #product papain #status experimental #label MAT\ !$155-196,189-228, !$286-333 #disulfide_bonds #status experimental\ !$158,292,308 #active_site Cys, His, Asn #status experimental SUMMARY #length 345 #molecular-weight 38922 #checksum 4796 SEQUENCE /// ENTRY TAGB #type complete TITLE actinidain (EC 3.4.22.14) precursor - kiwi fruit ALTERNATE_NAMES actinidin ORGANISM #formal_name Actinidia chinensis var. deliciosa #common_name kiwi fruit DATE 30-Nov-1980 #sequence_revision 31-May-1996 #text_change 18-Jun-1999 ACCESSIONS S12618; S12315; S12316; S06587; A00975 REFERENCE S12618 !$#authors Snowden, K.C.; Gardner, R.C. !$#journal Nucleic Acids Res. (1990) 18:6684 !$#title Nucleotide sequence of an actinidin genomic clone. !$#cross-references MUID:91067459; PMID:2251128 !$#accession S12618 !'##molecule_type DNA !'##residues 1-380 ##label SNO !'##cross-references EMBL:M38422; NID:g166316; PIDN:AAA32629.1; !1PID:g166317 REFERENCE S12315 !$#authors Keeling, J.; Maxwell, P.; Gardner, R.C. !$#journal Plant Mol. Biol. (1990) 15:787-788 !$#title Nucleotide sequence of the promoter region from kiwifruit !1actinidin genes. !$#cross-references MUID:91346716; PMID:2102886 !$#accession S12315 !'##status preliminary !'##molecule_type DNA !'##residues 81-100 ##label KEE !'##cross-references EMBL:M35795 !$#accession S12316 !'##status preliminary !'##molecule_type DNA !'##residues 1-13 ##label KE2 !'##cross-references EMBL:M35795; NID:g166322; PIDN:AAA32632.1; !1PID:g553033 REFERENCE S06587 !$#authors Podivinsky, E.; Forster, R.L.S.; Gardner, R.C. !$#journal Nucleic Acids Res. (1989) 17:8363 !$#title Nucleotide sequence of actinidin, a kiwi fruit protease. !$#cross-references MUID:90045955; PMID:2813065 !$#accession S06587 !'##molecule_type mRNA !'##residues 1-122,'F',124-225,'LD',228-271,'H',273-348,'H',350,'K', !1352-372,'D',374-380 ##label POD !'##cross-references EMBL:X16466; NID:g15983; PIDN:CAA34486.1; !1PID:g15984 !'##experimental_source clone pKIWI450 REFERENCE A90300 !$#authors Carne, A.; Moore, C.H. !$#journal Biochem. J. (1978) 173:73-83 !$#title The amino acid sequence of the tryptic peptides from !1actinidin, a proteolytic enzyme from the fruit of Actinidia !1chinensis. !$#cross-references MUID:78256777; PMID:687380 !$#accession A00975 !'##molecule_type protein !'##residues 127-166,'TS',169,'S',171-191,'D',193-205,'D',207-211,'Z', !1213-222,'D',224,'D',226,'A',228-229,'DQ',232-273,'A', !1275-285,'V',287-289,'IV',292-300,'V',302-346 ##label CAR !'##note tryptic peptides were positioned on the basis of X-ray !1crystallographic data REFERENCE A92859 !$#authors Baker, E.N. !$#journal J. Mol. Biol. (1980) 141:441-484 !$#title Structure of actinidin, after refinement at 1.7 angstrom !1resolution. !$#cross-references MUID:81072298; PMID:7003158 !$#contents annotation; X-ray crystallography, 1.7 angstroms !$#note Asp-212 changed to Glx on the basis of the X-ray data GENETICS !$#introns 149/1; 228/3; 275/3; 364/3 FUNCTION !$#description cysteine proteinase with broad specificity CLASSIFICATION #superfamily papain KEYWORDS cysteine proteinase; hydrolase FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-126 #domain amino-terminal propeptide #status predicted !8#label PRO\ !$127-346 #product actinidin #status experimental #label MAT\ !$347-380 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$148-191,182-224, !$282-332 #disulfide_bonds #status experimental\ !$151,288,345 #active_site Cys, His, Asn #status predicted SUMMARY #length 380 #molecular-weight 42142 #checksum 6142 SEQUENCE /// ENTRY S12581 #type complete TITLE cysteine proteinase (EC 3.4.22.-) precursor - black gram ALTERNATE_NAMES cysteine endopeptidase; sulfhydryl endopeptidase ORGANISM #formal_name Vigna mungo #common_name black gram DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 04-Feb-2000 ACCESSIONS S12581; S05497; S20213; S48684 REFERENCE S12581 !$#authors Akasofu, H.; Yamauchi, D.; Minamikawa, T. !$#journal Nucleic Acids Res. (1990) 18:1892 !$#title Nucleotide sequence of the gene for the Vigna mungo !1sulfhydryl-endopeptidase (SH-EP). !$#cross-references MUID:90245586; PMID:2336365 !$#accession S12581 !'##molecule_type DNA !'##residues 1-362 ##label AKA1 !'##cross-references EMBL:X51900; NID:g22065; PIDN:CAA36181.1; !1PID:g22066 REFERENCE S05497 !$#authors Akasofu, H.; Yamauchi, D.; Mitsuhashi, W.; Minamikawa, T. !$#journal Nucleic Acids Res. (1989) 17:6733 !$#title Nucleotide sequence of cDNA for sulfhydryl-endopeptidase !1(SH-EP) from cotyledons of germinating Vigna mungo seeds. !$#cross-references MUID:89386007; PMID:2780300 !$#accession S05497 !'##molecule_type mRNA !'##residues 1-362 ##label AKA2 !'##cross-references EMBL:X15732; NID:g22061; PIDN:CAA33753.1; !1PID:g22062 !$#accession S20213 !'##molecule_type protein !'##residues 132-140 ##label AKA3 REFERENCE S48684 !$#authors Okamoto, T.; Nakayama, H.; Seta, K.; Isobe, T.; Minamikawa, !1T. !$#journal FEBS Lett. (1994) 351:31-34 !$#title Posttranslational processing of a carboxy-terminal !1propeptide containing a KDEL sequence of plant vacuolar !1cysteine endopeptidase (SH-EP). !$#cross-references MUID:94357273; PMID:8076688 !$#accession S48684 !'##molecule_type protein !'##residues 127-140;197-216;324-333;339-352 ##label OKA GENETICS !$#introns 150/1; 228/3; 275/3 CLASSIFICATION #superfamily papain KEYWORDS cysteine proteinase; hydrolase FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-362 #product cysteine proteinase #status predicted #label !8MAT\ !$152,288,309 #active_site Cys, His, Asn #status predicted SUMMARY #length 362 #molecular-weight 40222 #checksum 1863 SEQUENCE /// ENTRY KHRZOA #type complete TITLE oryzain (EC 3.4.22.-) alpha precursor - rice ORGANISM #formal_name Oryza sativa #common_name rice DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jun-2000 ACCESSIONS JU0388; A40053 REFERENCE JU0388 !$#authors Watanabe, H.; Abe, K.; Emori, Y.; Hosoyama, H.; Arai, S. !$#submission submitted to JIPID, May 1991 !$#accession JU0388 !'##molecule_type DNA !'##residues 1-458 ##label WAT1 REFERENCE A40053 !$#authors Watanabe, H.; Abe, K.; Emori, Y.; Hosoyama, H.; Arai, S. !$#journal J. Biol. Chem. (1991) 266:16897-16902 !$#title Molecular cloning and gibberellin-induced expression of !1multiple cysteine proteinases of rice seeds (oryzains). !$#cross-references MUID:91358494; PMID:1885617 !$#accession A40053 !'##molecule_type mRNA !'##residues 1-458 ##label WAT2 !'##cross-references GB:D90406; NID:g218180; PIDN:BAA14402.1; !1PID:g218181 CLASSIFICATION #superfamily papain KEYWORDS cysteine proteinase; glycoprotein; hydrolase; seed FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-128 #domain amino-terminal propeptide #status predicted !8#label PRO\ !$129-348 #product oryzain alpha #status predicted #label MAT\ !$349-458 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$150-192,184-225, !$283-334 #disulfide_bonds #status predicted\ !$153,289,309 #active_site Cys, His, Asn #status predicted\ !$445 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 458 #molecular-weight 50274 #checksum 1235 SEQUENCE /// ENTRY KHRZOB #type complete TITLE oryzain (EC 3.4.22.-) beta precursor - rice ORGANISM #formal_name Oryza sativa #common_name rice DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jun-2000 ACCESSIONS JU0389; B40053 REFERENCE JU0388 !$#authors Watanabe, H.; Abe, K.; Emori, Y.; Hosoyama, H.; Arai, S. !$#submission submitted to JIPID, May 1991 !$#accession JU0389 !'##molecule_type mRNA !'##residues 1-471 ##label WAT1 REFERENCE A40053 !$#authors Watanabe, H.; Abe, K.; Emori, Y.; Hosoyama, H.; Arai, S. !$#journal J. Biol. Chem. (1991) 266:16897-16902 !$#title Molecular cloning and gibberellin-induced expression of !1multiple cysteine proteinases of rice seeds (oryzains). !$#cross-references MUID:91358494; PMID:1885617 !$#accession B40053 !'##molecule_type mRNA !'##residues 1-471 ##label WAT2 !'##cross-references GB:D90407; NID:g218182; PIDN:BAA14403.1; !1PID:g218183 CLASSIFICATION #superfamily papain KEYWORDS cysteine proteinase; glycoprotein; hydrolase; seed FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-139 #domain amino-terminal propeptide #status predicted !8#label PRO\ !$140-360 #product oryzain beta #status predicted #label MAT\ !$361-471 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$161-204,195-237, !$295-346 #disulfide_bonds #status predicted\ !$164,301,321 #active_site Cys, His, Asn #status predicted\ !$340,388 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 471 #molecular-weight 50505 #checksum 4349 SEQUENCE /// ENTRY KHRZOG #type complete TITLE oryzain (EC 3.4.22.-) gamma precursor - rice ORGANISM #formal_name Oryza sativa #common_name rice DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jun-2000 ACCESSIONS JU0390; C40053 REFERENCE JU0388 !$#authors Watanabe, H.; Abe, K.; Emori, Y.; Hosoyama, H.; Arai, S. !$#submission submitted to JIPID, May 1991 !$#accession JU0390 !'##molecule_type mRNA !'##residues 1-362 ##label WAT1 REFERENCE A40053 !$#authors Watanabe, H.; Abe, K.; Emori, Y.; Hosoyama, H.; Arai, S. !$#journal J. Biol. Chem. (1991) 266:16897-16902 !$#title Molecular cloning and gibberellin-induced expression of !1multiple cysteine proteinases of rice seeds (oryzains). !$#cross-references MUID:91358494; PMID:1885617 !$#accession C40053 !'##molecule_type mRNA !'##residues 1-362 ##label WAT2 !'##cross-references GB:D90408; NID:g218184; PIDN:BAA14404.1; !1PID:g218185 CLASSIFICATION #superfamily papain KEYWORDS cysteine proteinase; glycoprotein; hydrolase; seed FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-144 #domain propeptide #status predicted #label PRO\ !$145-362 #product oryzain gamma #status predicted #label MAT\ !$128,258 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$166-209,200-242, !$300-350 #disulfide_bonds #status predicted\ !$169,309,329 #active_site Cys, His, Asn #status predicted SUMMARY #length 362 #molecular-weight 39204 #checksum 2710 SEQUENCE /// ENTRY KHDO #type complete TITLE cysteine proteinase 1 (EC 3.4.22.-) precursor - slime mold (Dictyostelium discoideum) ORGANISM #formal_name Dictyostelium discoideum DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 16-Jun-2000 ACCESSIONS A22827 REFERENCE A22827 !$#authors Williams, J.G.; North, M.J.; Mahbubani, H. !$#journal EMBO J. (1985) 4:999-1006 !$#title A developmentally regulated cysteine proteinase in !1Dictyostelium discoideum. !$#cross-references MUID:85257519; PMID:2990918 !$#accession A22827 !'##molecule_type mRNA !'##residues 1-343 ##label WIL !'##cross-references GB:X02407; NID:g7235; PIDN:CAA26255.1; PID:g1617037 CLASSIFICATION #superfamily papain KEYWORDS cysteine proteinase; glycoprotein; hydrolase FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-117 #domain propeptide #status predicted #label PPT\ !$118-343 #product cysteine proteinase 1 #status predicted !8#label MPT\ !$139-177,173-224, !$279-332 #disulfide_bonds #status predicted\ !$142,286,311 #active_site Cys, His, Asn #status predicted\ !$237,244 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 343 #molecular-weight 38495 #checksum 7591 SEQUENCE /// ENTRY KHDOP #type complete TITLE prestalk cathepsin (EC 3.4.22.-) precursor - slime mold (Dictyostelium discoideum) ALTERNATE_NAMES cysteine proteinase 2 ORGANISM #formal_name Dictyostelium discoideum DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 16-Jun-2000 ACCESSIONS A25439; A24110 REFERENCE A93090 !$#authors Datta, S.; Firtel, R.A. !$#journal Mol. Cell. Biol. (1987) 7:149-159 !$#title Identification of the sequences controlling cyclic AMP !1regulation and cell-type-specific expression of a !1prestalk-specific gene in Dictyostelium discoideum. !$#cross-references MUID:87172698; PMID:3031453 !$#accession A25439 !'##molecule_type DNA !'##residues 1-376 ##label DAT !'##cross-references GB:M16039; NID:g167859; PIDN:AAA33240.1; !1PID:g167860 REFERENCE A93604 !$#authors Pears, C.J.; Mahbubani, H.M.; Williams, J.G. !$#journal Nucleic Acids Res. (1985) 13:8853-8866 !$#title Characterization of two highly diverged but developmentally !1co-regulated cysteine proteinase genes in Dictyostelium !1discoideum. !$#cross-references MUID:86093683; PMID:3909109 !$#accession A24110 !'##molecule_type mRNA !'##residues 1-376 ##label PEA !'##cross-references GB:X03344; NID:g7240; PIDN:CAA27050.1; PID:g1834417 GENETICS !$#introns 146/1; 194/2; 356/1; 364/2 CLASSIFICATION #superfamily papain KEYWORDS cAMP binding; cysteine proteinase; glycoprotein; hydrolase FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-121 #domain propeptide #status predicted #label PRO\ !$122-376 #product prestalk cathepsin #status predicted #label !8MAT\ !$144-187,178-221, !$279-365 #disulfide_bonds #status predicted\ !$147,286,343 #active_site Cys, His, Asn #status predicted\ !$224,237 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 376 #molecular-weight 41851 #checksum 2639 SEQUENCE /// ENTRY KHHUL #type complete TITLE cathepsin L (EC 3.4.22.15) precursor [validated] - human ALTERNATE_NAMES major excreted protein (MEP); procathepsin L ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 08-Dec-2000 ACCESSIONS S01002; B32333; S09065; A45043; S00323; B27011; A26069; !1A32683; D27011; F27011 REFERENCE S01002 !$#authors Gal, S.; Gottesman, M.M. !$#journal Biochem. J. (1988) 253:303-306 !$#title Isolation and sequence of a cDNA for human pro-(cathepsin !1L). !$#cross-references MUID:88339905; PMID:3421948 !$#accession S01002 !'##molecule_type mRNA !'##residues 1-333 ##label GAL !'##cross-references GB:X12451; NID:g29714; PIDN:CAA30981.1; PID:g29715 REFERENCE A92768 !$#authors Joseph, L.J.; Chang, L.C.; Stamenkovich, D.; Sukhatme, V.P. !$#journal J. Clin. Invest. (1988) 81:1621-1629 !$#title Complete nucleotide and deduced amino acid sequences of !1human and murine preprocathepsin L. An abundant transcript !1induced by transformation of fibroblasts. !$#cross-references MUID:88213715; PMID:2835398 !$#accession B32333 !'##molecule_type mRNA !'##residues 1-333 ##label JOS !'##cross-references GB:M20496; NID:g809235; PIDN:AAA66974.1; !1PID:g190418 REFERENCE S09065 !$#authors Joseph, L.; Lapid, S.; Sukhatme, V. !$#journal Nucleic Acids Res. (1987) 15:3186 !$#title The major ras induced protein in NIH3T3 cells is cathepsin !1L. !$#cross-references MUID:87174843; PMID:3550705 !$#accession S09065 !'##molecule_type mRNA !'##residues 113-154 ##label JO2 !'##cross-references EMBL:X05256; NID:g29718; PIDN:CAA28877.1; !1PID:g1340178 REFERENCE A45043 !$#authors Chauhan, S.S.; Popescu, N.C.; Ray, D.; Fleischmann, R.; !1Gottesman, M.M.; Troen, B.R. !$#journal J. Biol. Chem. (1993) 268:1039-1045 !$#title Cloning, genomic organization, and chromosomal localization !1of human cathepsin L. !$#cross-references MUID:93123212; PMID:8419312 !$#accession A45043 !'##molecule_type DNA !'##residues 40-46;82-86;130-135;205-210;259-264;299-304 ##label CHA !'##cross-references GB:L06426 !'##note only exon-intron splice junctions are shown REFERENCE S00322 !$#authors Ritonja, A.; Popovic, T.; Kotnik, M.; Machleidt, W.; Turk, !1V. !$#journal FEBS Lett. (1988) 228:341-345 !$#title Amino acid sequences of the human kidney cathepsins H and L. !$#cross-references MUID:88137635; PMID:3342889 !$#accession S00323 !'##molecule_type protein !'##residues 114-147,'P',148-220,'X',222-267,'N',269-288;292-333 ##label !1RIT REFERENCE A27011 !$#authors Machleidt, W.; Ritonja, A.; Popovic, T.; Kotnik, M.; Brzin, !1J.; Turk, V.; Machleidt, I.; Mueller-Esterl, W. !$#book Cysteine Proteinases and Their Inhibitors, Turk, V., ed., !1pp.3-18, Walter de Gruyter, Berlin, 1986 !$#title Human cathepsins B, H and L: characterization by amino acid !1sequences and some kinetics of inhibition by the kininogens. !$#accession B27011 !'##molecule_type protein !'##residues 'X',115-129,'M',131-133,'E',135-141;292-307,'TD',310-333 !1##label MA2 REFERENCE A26069 !$#authors Mason, R.W.; Walker, J.E.; Northrop, F.D. !$#journal Biochem. J. (1986) 240:373-377 !$#title The N-terminal amino acid sequences of the heavy and light !1chains of human cathepsin L. !$#cross-references MUID:87127952; PMID:3545185 !$#accession A26069 !'##molecule_type protein !'##residues 114-147,'P',149-152,'Y';292-333 ##label MAS REFERENCE A32683 !$#authors Smith, S.M.; Gottesman, M.M. !$#journal J. Biol. Chem. (1989) 264:20487-20495 !$#title Activity and deletion analysis of recombinant human !1cathepsin L expressed in Escherichia coli. !$#cross-references MUID:90062183; PMID:2684978 !$#contents annotation GENETICS !$#gene GDB:CTSL !'##cross-references GDB:119824; OMIM:116880 !$#map_position 9q22.1-9q22.2 !$#introns 42/3; 83/3; 132/3; 207/3; 262/1; 301/2 COMPLEX heterodimer of disulfide linked chains produced from a !1single chain precursor FUNCTION !$#description catalyzes hydrolysis of peptide bonds in proteins !$#pathway intracellular protein degradation !$#note important role in the lysosomal degradation of proteins CLASSIFICATION #superfamily papain KEYWORDS cysteine proteinase; glycoprotein; heterodimer; hydrolase; !1lysosome; protein degradation FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-113 #domain propeptide #status predicted #label PRO\ !$114-333 #product cathepsin L #status experimental #label MAT\ !$114-288 #product cathepsin L heavy chain #status experimental !8#label HCH\ !$292-333 #product cathepsin L light chain #status experimental !8#label LCH\ !$135-178,169-211, !$269-322 #disulfide_bonds #status predicted\ !$138,276,300 #active_site Cys, His, Asn #status predicted\ !$221 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 333 #molecular-weight 37564 #checksum 8412 SEQUENCE /// ENTRY KHRTL #type complete TITLE cathepsin L (EC 3.4.22.15) precursor - rat ALTERNATE_NAMES cyclic protein-2; major excreted protein (MEP); procathepsin L ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 18-Jun-1999 ACCESSIONS S07098; S00155; S02445; A41550; S02446 REFERENCE S07098 !$#authors Ishidoh, K.; Kominami, E.; Suzuki, K.; Katunuma, N. !$#journal FEBS Lett. (1989) 259:71-74 !$#title Gene structure and 5'-upstream sequence of rat cathepsin L. !$#cross-references MUID:90092543; PMID:2599113 !$#accession S07098 !'##molecule_type DNA !'##residues 1-334 ##label ISH1 !'##cross-references EMBL:X51648; NID:g57532 !'##note only part of the nucleotide sequence is given REFERENCE S00155 !$#authors Ishidoh, K.; Towatari, T.; Imajoh, S.; Kawasaki, H.; !1Kominami, E.; Katunuma, N.; Suzuki, K. !$#journal FEBS Lett. (1987) 223:69-73 !$#title Molecular cloning and sequencing of cDNA for rat cathepsin !1L. !$#cross-references MUID:88030047; PMID:3666143 !$#accession S00155 !'##molecule_type mRNA !'##residues 1-30,'Q',32-237,'P',239-334 ##label ISH2 !'##cross-references EMBL:Y00697; NID:g55887; PIDN:CAA68691.1; !1PID:g55888 REFERENCE S02445 !$#authors Towatari, T.; Katunuma, N. !$#journal FEBS Lett. (1988) 236:57-61 !$#title Amino acid sequence of rat liver cathepsin L. !$#cross-references MUID:88296890; PMID:3402618 !$#accession S02445 !'##molecule_type protein !'##residues 114-288;291-334 ##label TOW REFERENCE A41550 !$#authors Erickson-Lawrence, M.; Zabludoff, S.D.; Wright, W.W. !$#journal Mol. Endocrinol. (1991) 5:1789-1798 !$#title Cyclic protein-2, a secretory product of rat sertoli cells, !1is the proenzyme form of cathepsin L. !$#cross-references MUID:92168015; PMID:1791830 !$#accession A41550 !'##status preliminary !'##molecule_type mRNA !'##residues 88-334 ##label ERI !'##cross-references GB:S85184; NID:g246147; PIDN:AAB21516.1; !1PID:g246148 GENETICS !$#introns 42/3; 83/3; 132/3; 207/3; 262/1; 301/2 COMPLEX heterodimer of disulfide linked chains produced from a !1single chain precursor FUNCTION !$#description catalyzes hydrolysis of peptide bonds in proteins !$#pathway intracellular protein degradation !$#note important role in the lysosomal degradation of proteins CLASSIFICATION #superfamily papain KEYWORDS cysteine proteinase; glycoprotein; heterodimer; hydrolase; !1lysosome; protein degradation FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-113 #domain propeptide #status predicted #label PRO\ !$114-288 #product cathepsin L heavy chain #status experimental !8#label HCH\ !$291-334 #product cathepsin L light chain #status experimental !8#label LCH\ !$135-178,169-211, !$269-322 #disulfide_bonds #status predicted\ !$138,276,300 #active_site Cys, His, Asn #status predicted\ !$221 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 334 #molecular-weight 37669 #checksum 4025 SEQUENCE /// ENTRY KHMSL #type complete TITLE cathepsin L (EC 3.4.22.15) precursor - mouse ALTERNATE_NAMES major excreted protein (MEP); procathepsin L ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 18-Jun-1999 ACCESSIONS S01177; A34972; A25999; A32333; A45927; S13890; S48734; !1S64672 REFERENCE S01177 !$#authors Troen, B.R.; Gal, S.; Gottesman, M.M. !$#journal Biochem. J. (1987) 246:731-735 !$#title Sequence and expression of the cDNA for MEP (major excreted !1protein), a transformation-regulated secreted cathepsin. !$#cross-references MUID:88076849; PMID:3689328 !$#accession S01177 !'##molecule_type mRNA !'##residues 1-334 ##label TRO1 !'##cross-references EMBL:X06086; NID:g53046; PIDN:CAA29470.1; !1PID:g53047 !$#accession A34972 !'##molecule_type protein !'##residues 18-28 ##label TRO2 REFERENCE A25999 !$#authors Portnoy, D.A.; Erickson, A.H.; Kochan, J.; Ravetch, J.V.; !1Unkeless, J.C. !$#journal J. Biol. Chem. (1986) 261:14697-14703 !$#title Cloning and characterization of a mouse cysteine proteinase. !$#cross-references MUID:87033683; PMID:3533924 !$#accession A25999 !'##molecule_type mRNA !'##residues 1-334 ##label POR !'##cross-references EMBL:J02583; NID:g192681; PIDN:AAA37445.1; !1PID:g309186 REFERENCE A92768 !$#authors Joseph, L.J.; Chang, L.C.; Stamenkovich, D.; Sukhatme, V.P. !$#journal J. Clin. Invest. (1988) 81:1621-1629 !$#title Complete nucleotide and deduced amino acid sequences of !1human and murine preprocathepsin L. An abundant transcript !1induced by transformation of fibroblasts. !$#cross-references MUID:88213715; PMID:2835398 !$#accession A32333 !'##molecule_type mRNA !'##residues 1-57,'I',59-334 ##label JOS !'##cross-references GB:M20495; NID:g200500; PIDN:AAA39984.1; !1PID:g200501 REFERENCE A45927 !$#authors Denhardt, D.T.; Hamilton, R.T.; Parfett, C.L.J.; Edwards, !1D.R.; St.Pierre, R.; Waterhouse, P.; Nilsen-Hamilton, M. !$#journal Cancer Res. (1986) 46:4590-4593 !$#title Close relationship of the major excreted protein of !1transformed murine fibroblasts to thiol-dependent !1cathepsins. !$#cross-references MUID:86271744; PMID:3755373 !$#accession A45927 !'##molecule_type mRNA !'##residues 89-300 ##label DEN !'##cross-references GB:X04392; NID:g53050; PIDN:CAA27980.1; PID:g929719 REFERENCE S13890 !$#authors Stearns, N.A.; Dong, J.; Pan, J.X.; Brenner, D.A.; Sahagian, !1G.G. !$#journal Arch. Biochem. Biophys. (1990) 283:447-457 !$#title Comparison of cathepsin L synthesized by normal and !1transformed cells at the gene, message, protein, and !1oligosaccharide levels. !$#cross-references MUID:91112761; PMID:2275556 !$#accession S13890 !'##status preliminary !'##molecule_type mRNA !'##residues 1-334 ##label STE REFERENCE S48734 !$#authors Ishidoh, K.; Kominami, E. !$#journal FEBS Lett. (1994) 352:281-284 !$#title Multi-step processing of procathepsin L in vitro. !$#cross-references MUID:95010724; PMID:7925987 !$#accession S48734 !'##molecule_type protein !'##residues 104-124 ##label ISH REFERENCE S64672 !$#authors Jean, D.; Hermann, J.; Rodrigues-Lima, F.; Barel, M.; Balbo, !1M.; Frade, R. !$#journal Biochem. J. (1995) 312:961-969 !$#title Identification on melanoma cells of p39, a cysteine !1proteinase that cleaves C3, the third component of !1complement: amino-acid-sequence identities with procathepsin !1L. !$#cross-references MUID:96128086; PMID:8554545 !$#accession S64672 !'##status preliminary !'##molecule_type protein !'##residues 18-34;273-292;295-313 ##label JEA FUNCTION !$#description catalyzes hydrolysis of peptide bonds in proteins !$#pathway intracellular protein degradation !$#note important role in the lysosomal degradation of proteins CLASSIFICATION #superfamily papain KEYWORDS cysteine proteinase; glycoprotein; heterodimer; hydrolase; !1lysosome; protein degradation FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-113 #domain propeptide #status predicted #label PRO\ !$114-288 #product cathepsin L heavy chain #status predicted !8#label HCH\ !$291-334 #product cathepsin L light chain #status predicted !8#label LCH\ !$135-178,169-211, !$269-322 #disulfide_bonds #status predicted\ !$138,276,300 #active_site Cys, His, Asn #status predicted\ !$221,268 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 334 #molecular-weight 37547 #checksum 3155 SEQUENCE /// ENTRY KHCHL #type complete TITLE cathepsin L (EC 3.4.22.15) - chicken ALTERNATE_NAMES major excreted protein (MEP); procathepsin L ORGANISM #formal_name Gallus gallus #common_name chicken DATE 31-Mar-1992 #sequence_revision 18-Oct-1996 #text_change 18-Mar-1997 ACCESSIONS S00081; A25654; A26818; B25654 REFERENCE S00081 !$#authors Wada, K.; Takai, T.; Tanabe, T. !$#journal Eur. J. Biochem. (1987) 167:13-18 !$#title Amino acid sequence of chicken liver cathepsin L. !$#cross-references MUID:87304227; PMID:3305012 !$#accession S00081 !'##molecule_type protein !'##residues 1-176;177-218 ##label WAD REFERENCE A91372 !$#authors Wada, K.; Tanabe, T. !$#journal FEBS Lett. (1986) 209:330-334 !$#title N-terminal amino acid sequences of the heavy and light !1chains of chicken liver cathepsin L. !$#cross-references MUID:87080783; PMID:3792553 !$#accession A25654 !'##molecule_type protein !'##residues 1-37;177-216 ##label WA2 REFERENCE A26818 !$#authors Dufour, E.; Obled, A.; Valin, C.; Bechet, D.; !1Ribadeau-Dumas, B.; Huet, J.C. !$#journal Biochemistry (1987) 26:5689-5695 !$#title Purification and amino acid sequence of chicken liver !1cathepsin L. !$#cross-references MUID:88050863; PMID:3676277 !$#accession A26818 !'##molecule_type protein !'##residues 1-20,'I',22-28,'N',30-39,'F',41-96,99-108,'K', !1110-175;177-196,'Q',198-218 ##label DUF COMPLEX heterodimer of disulfide linked chains produced from a !1single chain precursor FUNCTION !$#description catalyzes hydrolysis of peptide bonds in proteins !$#pathway intracellular protein degradation !$#note important role in the lysosomal degradation of proteins CLASSIFICATION #superfamily papain KEYWORDS cysteine proteinase; glycoprotein; heterodimer; hydrolase; !1liver; lysosome; protein degradation FEATURE !$1-176 #product cathepsin L heavy chain #status experimental !8#label HCH\ !$177-218 #product cathepsin L light chain #status experimental !8#label LCH\ !$22-65,56-99,158-207 #disulfide_bonds #status predicted\ !$25,165,185 #active_site Cys, His, Asn #status predicted\ !$109 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 218 #molecular-weight 23963 #checksum 2849 SEQUENCE /// ENTRY I52525 #type complete TITLE testin precursor - rat ALTERNATE_NAMES testin I; testin II ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 02-Aug-1996 #sequence_revision 02-Aug-1996 #text_change 18-Jun-1999 ACCESSIONS I52525; A34199; B34199; PC1250 REFERENCE I52525 !$#authors Grima, J.; Zhu, L.J.; Zong, S.D.; Catterall, J.F.; Bardin, !1C.W.; Cheng, C.Y. !$#journal Biol. Reprod. (1995) 52:340-355 !$#title Rat testin is a newly identified component of the junctional !1complexes in various tissues whose mRNA is predominantly !1expressed in the testis and ovary. !$#cross-references MUID:95226598; PMID:7711203 !$#accession I52525 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-333 ##label RES !'##cross-references EMBL:U16858; NID:g577429; PIDN:AAC52162.1; !1PID:g577430 REFERENCE A92740 !$#authors Cheng, C.Y.; Grima, J.; Stahler, M.S.; Lockshin, R.A.; !1Bardin, C.W. !$#journal J. Biol. Chem. (1989) 264:21386-21393 !$#title Testins are structurally related Sertoli cell proteins whose !1secretion is tightly coupled to the presence of germ cells. !$#cross-references MUID:90078247; PMID:2592382 !$#accession A34199 !'##molecule_type protein !'##residues 20-49 ##label CHE !'##note this secreted form was designated testin I !$#accession B34199 !'##molecule_type protein !'##residues 'X',18-19,'X',21-28,'X',30-31,'X',33-35 ##label CH2 !'##note this secreted form was designated testin II COMMENT This junctional complex protein, although closely related to !1cathepsin L, is unlikely to be active as a proteinase. CLASSIFICATION #superfamily papain KEYWORDS glycoprotein; monomer; testis FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-333 #product testin II #status predicted #label MAT2\ !$20-333 #product testin I1 #status predicted #label MAT1\ !$138,276,300 #region defective catalytic triad\ !$135-178,169-211, !$269-322 #disulfide_bonds #status predicted\ !$173 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 333 #molecular-weight 38033 #checksum 2710 SEQUENCE /// ENTRY KHHUH #type complete TITLE cathepsin H (EC 3.4.22.16) precursor [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1990 #sequence_revision 30-Jun-1991 #text_change 08-Dec-2000 ACCESSIONS S12486; S07634; S00818; S00322; A27011; C27011; S00635 REFERENCE S12486 !$#authors Fuchs, R. !$#submission submitted to the EMBL Data Library, October 1989 !$#accession S12486 !'##molecule_type mRNA !'##residues 1-335 ##label FUC !'##cross-references EMBL:X16832; NID:g29709; PIDN:CAA34734.1; !1PID:g29710 REFERENCE S07634 !$#authors Fuchs, R.; Gassen, H.G. !$#journal Nucleic Acids Res. (1989) 17:9471 !$#title Nucleotide sequence of human preprocathepsin H, a lysosomal !1cysteine proteinase. !$#cross-references MUID:90067944; PMID:2587265 !$#accession S07634 !'##molecule_type mRNA !'##residues 1-115 ##label FU2 !'##cross-references EMBL:X16832 REFERENCE S00818 !$#authors Fuchs, R.; Machleidt, W.; Gassen, H.G. !$#journal Biol. Chem. Hoppe-Seyler (1988) 369:469-475 !$#title Molecular cloning and sequencing of a cDNA coding for mature !1human kidney cathepsin H. !$#cross-references MUID:89076480; PMID:2849458 !$#accession S00818 !'##molecule_type mRNA !'##residues 88-335 ##label FU3 !'##cross-references EMBL:X07549; NID:g29707; PIDN:CAA30428.1; !1PID:g29708 REFERENCE S00322 !$#authors Ritonja, A.; Popovic, T.; Kotnik, M.; Machleidt, W.; Turk, !1V. !$#journal FEBS Lett. (1988) 228:341-345 !$#title Amino acid sequences of the human kidney cathepsins H and L. !$#cross-references MUID:88137635; PMID:3342889 !$#accession S00322 !'##molecule_type protein !'##residues 98-105;114-178,'H',180-305,'E',307-335 ##label RIT REFERENCE A27011 !$#authors Machleidt, W.; Ritonja, A.; Popovic, T.; Kotnik, M.; Brzin, !1J.; Turk, V.; Machleidt, I.; Mueller-Esterl, W. !$#book Cysteine Proteinases and Their Inhibitors, Turk, V., ed., !1pp.3-18, Walter de Gruyter, Berlin, 1986 !$#title Human cathepsins B, H and L: characterization by amino acid !1sequences and some kinetics of inhibition by the kininogens. !$#contents annotation COMMENT Cathepsin H is composed of a minichain and a large chain. !1The large chain may be split into heavy and light chain. All !1chains are held together by disulfide bonds. GENETICS !$#gene GDB:CTSH !'##cross-references GDB:120602; OMIM:116820 !$#map_position 15q24-15q25 CLASSIFICATION #superfamily papain KEYWORDS cysteine proteinase; glycoprotein; hydrolase; lysosome FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-97 #domain propeptide #status predicted #label PRO\ !$98-105 #product cathepsin H minichain #status experimental !8#label MCH\ !$114-335 #product cathepsin H large chain (minor form) #status !8experimental #label MAT2\ !$116-335 #product cathepsin H large chain #status experimental !8#label MAT1\ !$116-292 #product cathepsin H heavy chain #status experimental !8#label HCH\ !$293-335 #product cathepsin H light chain #status experimental !8#label LCH\ !$72 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$101,230 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$102-327,138-181, !$172-214,272-322 #disulfide_bonds #status predicted\ !$141,281,301 #active_site Cys, His, Asn #status predicted SUMMARY #length 335 #molecular-weight 37403 #checksum 8904 SEQUENCE /// ENTRY KHRTH #type complete TITLE cathepsin H (EC 3.4.22.16) precursor - rat ALTERNATE_NAMES cathepsin B3; cathepsin Ba ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 18-Apr-1984 #sequence_revision 30-Jun-1993 #text_change 21-Jul-2000 ACCESSIONS S00211; S05213; A00976; A60371 REFERENCE S00211 !$#authors Ishidoh, K.; Imajoh, S.; Emori, Y.; Ohno, S.; Kawasaki, H.; !1Minami, Y.; Kominami, E.; Katunuma, N.; Suzuki, K. !$#journal FEBS Lett. (1987) 226:33-37 !$#title Molecular cloning and sequencing of cDNA for rat cathepsin !1H. Homology in pro-peptide regions of cysteine proteinases. !$#cross-references MUID:88083632; PMID:3691815 !$#accession S00211 !'##molecule_type mRNA !'##residues 1-333 ##label ISH !'##cross-references GB:M36320; NID:g55885; PIDN:CAA68699.1; PID:g55886 REFERENCE S05213 !$#authors Ishidoh, K.; Kominami, E.; Katunuma, N.; Suzuki, K. !$#journal FEBS Lett. (1989) 253:103-107 !$#title Gene structure of rat cathepsin H. !$#cross-references MUID:89338722; PMID:2759235 !$#accession S05213 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-286,'A',288-333 ##label ISH2 REFERENCE A00976 !$#authors Takio, K.; Towatari, T.; Katunuma, N.; Teller, D.C.; Titani, !1K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:3666-3670 !$#title Homology of amino acid sequences of rat liver cathepsins B !1and H with that of papain. !$#cross-references MUID:83221657; PMID:6574504 !$#accession A00976 !'##molecule_type protein !'##residues 114-333 ##label TAK REFERENCE A60371 !$#authors Qian, F.; Frankfater, A.; Miller, R.V.; Chan, S.J.; Steiner, !1D.F. !$#journal Int. J. Biochem. (1990) 22:1457-1464 !$#title Molecular cloning of rat precursor cathepsin H and the !1expression of five lysosomal cathepsins in normal tissues !1and in a rat carcinosarcoma. !$#cross-references MUID:91114797; PMID:2276418 !$#accession A60371 !'##molecule_type mRNA !'##residues 4-333 ##label QIA !'##cross-references GB:M38135 COMMENT Cathepsin H is composed of a minichain and a large chain. !1The large chain may be split into heavy and light chain. All !1chains are held together by disulfide bonds. GENETICS !$#introns 29/1; 39/3; 75/1; 98/3; 133/3; 162/3; 181/2; 208/3; 231/3; !1267/2; 309/2 CLASSIFICATION #superfamily papain KEYWORDS cysteine proteinase; glycoprotein; hydrolase; lysosome FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-95 #domain propeptide #status predicted #label PRO\ !$96-102 #product cathepsin H minichain #status predicted !8#label MCH\ !$114-333 #product cathepsin H large chain #status experimental !8#label MAT\ !$114-290 #product cathepsin H heavy chain #status predicted !8#label HCH\ !$291-333 #product cathepsin H light chain #status predicted !8#label LCH\ !$70,99 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$136-179,170-212, !$270-320 #disulfide_bonds #status predicted\ !$139,279,299 #active_site Cys, His, Asn #status predicted\ !$228 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 333 #molecular-weight 37104 #checksum 2907 SEQUENCE /// ENTRY KHSYO4 #type complete TITLE oil bodies-associated protein P34 precursor - soybean CONTAINS oil bodies-associated protein P32 ORGANISM #formal_name Glycine max #common_name soybean DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 13-Jun-1997 ACCESSIONS A37126 REFERENCE A37126 !$#authors Kalinski, A.; Weisemann, J.M.; Matthews, B.F.; Herman, E.M. !$#journal J. Biol. Chem. (1990) 265:13843-13848 !$#title Molecular cloning of a protein associated with soybean seed !1oil bodies that is similar to thiol proteases of the papain !1family. !$#cross-references MUID:90338001; PMID:2380191 !$#accession A37126 !'##molecule_type DNA !'##residues 1-379 ##label KAL !'##cross-references GB:J05560 CLASSIFICATION #superfamily papain KEYWORDS glycoprotein; seed FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-122 #domain propeptide #status predicted #label PRO\ !$123-379 #product oil bodies-associated protein P34 #status !8predicted #label MATL\ !$133-379 #product oil bodies-associated protein P32 #status !8predicted #label MATS\ !$159,301,321 #region defective catalytic triad\ !$70,292 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$190-230,293-346 #disulfide_bonds #status predicted SUMMARY #length 379 #molecular-weight 42794 #checksum 1255 SEQUENCE /// ENTRY KHBH #type complete TITLE aleurain (EC 3.4.22.-) precursor - barley ORGANISM #formal_name Hordeum vulgare #common_name barley DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 04-Oct-1996 ACCESSIONS A25492; B25492 REFERENCE A25492 !$#authors Rogers, J.C.; Dean, D.; Heck, G.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:6512-6516 !$#title Aleurain: a barley thiol protease closely related to !1mammalian cathepsin H. !$#cross-references MUID:86016732; PMID:3901004 !$#accession A25492 !'##molecule_type DNA !'##residues 1-361 ##label ROG1 !$#accession B25492 !'##molecule_type mRNA !'##residues 1-361 ##label ROG2 !'##cross-references GB:X05167; GB:M11760; GB:M15209; GB:Y00107 COMMENT Aleurain is synthesized by the aleurone cells stimulated by !1gibberellic or abscisic acid. CLASSIFICATION #superfamily papain KEYWORDS aleurone cell; cysteine proteinase; germination; !1glycoprotein; hydrolase; seed FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-143 #domain propeptide #status predicted #label PRO\ !$144-361 #product aleurain #status predicted #label MAT\ !$165-208,199-240, !$298-348 #disulfide_bonds #status predicted\ !$168,307,327 #active_site Cys, His, Asn #status predicted\ !$188,256 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 361 #molecular-weight 38996 #checksum 9984 SEQUENCE /// ENTRY KHQBTT #type complete TITLE cysteine proteinase (EC 3.4.22.-) precursor - Theileria parva ORGANISM #formal_name Theileria parva #note host Bos primigenius taurus (cattle) DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 18-Jun-1999 ACCESSIONS A36083 REFERENCE A36083 !$#authors Nene, V.; Gobright, E.; Musoke, A.J.; Lonsdale-Eccles, J.D. !$#journal J. Biol. Chem. (1990) 265:18047-18050 !$#title A single exon codes for the enzyme domain of a protozoan !1cysteine protease. !$#cross-references MUID:91009278; PMID:2120221 !$#accession A36083 !'##molecule_type DNA !'##residues 1-439 ##label NEN !'##cross-references GB:M37791; NID:g161872; PIDN:AAA30131.1; !1PID:g161873 GENETICS !$#introns 159/3 CLASSIFICATION #superfamily papain KEYWORDS cysteine proteinase; glycoprotein; hydrolase FEATURE !$1-56 #domain signal sequence #status predicted #label SIG\ !$57-227 #domain propeptide #status predicted #label PRO\ !$228-439 #product cysteine proteinase #status predicted #label !8MAT\ !$205 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$249-290,283-322, !$375-427 #disulfide_bonds #status predicted\ !$252,381,403 #active_site Cys, His, Asn #status predicted SUMMARY #length 439 #molecular-weight 50179 #checksum 1163 SEQUENCE /// ENTRY KHHUB #type complete TITLE cathepsin B (EC 3.4.22.1) precursor [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 15-Sep-2000 ACCESSIONS A26498; I53727; A25432; A27139; S23973; S16513; S16514 REFERENCE A26498 !$#authors Chan, S.J.; San Segundo, B.; McCormick, M.B.; Steiner, D.F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:7721-7725 !$#title Nucleotide and predicted amino acid sequences of cloned !1human and mouse preprocathepsin B cDNAs. !$#cross-references MUID:87017021; PMID:3463996 !$#accession A26498 !'##molecule_type mRNA !'##residues 1-339 ##label CHA !'##cross-references GB:M14221; NID:g181191; PIDN:AAA52129.1; !1PID:g181192 REFERENCE I53727 !$#authors Cao, L.; Taggart, R.T.; Berquin, I.M.; Moin, K.; Fong, D.; !1Sloane, B.F. !$#journal Gene (1994) 139:163-169 !$#title Human gastric adenocarcinoma cathepsin B: isolation and !1sequencing of full-length cDNAs and polymorphisms of the !1gene. !$#cross-references MUID:94156194; PMID:8112600 !$#accession I53727 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-25,'L',27-339 ##label CAO !'##cross-references GB:L16510; NID:g291887; PIDN:AAC37547.1; !1PID:g291888 REFERENCE A25432 !$#authors Fong, D.; Calhoun, D.H.; Hsieh, W.T.; Lee, B.; Wells, R.D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:2909-2913 !$#title Isolation of a cDNA clone for the human lysosomal proteinase !1cathepsin B. !$#cross-references MUID:86206063; PMID:3010323 !$#accession A25432 !'##molecule_type mRNA !'##residues 131-339 ##label FON !'##cross-references GB:M13230; NID:g181177; PIDN:AAA52125.1; !1PID:g181178 REFERENCE A27139 !$#authors Ritonja, A.; Popovic, T.; Turk, V.; Wiedenmann, K.; !1Machleidt, W. !$#journal FEBS Lett. (1985) 181:169-172 !$#title Amino acid sequence of human liver cathepsin B. !$#cross-references MUID:85127484; PMID:3972105 !$#accession A27139 !'##molecule_type protein !'##residues 80-126;129-227,'D',229-333 ##label RIT REFERENCE S23973 !$#authors Moin, K.; Day, N.A.; Sameni, M.; Hasnain, S.; Hirama, T.; !1Sloane, B.F. !$#journal Biochem. J. (1992) 285:427-434 !$#title Human tumour cathepsin B. Comparison with normal liver !1cathepsin B. !$#cross-references MUID:92344620; PMID:1637335 !$#accession S23973 !'##molecule_type protein !'##residues 80-89,'X',91;129-139 ##label MOI REFERENCE A67019 !$#authors Musil, D.; Bode, W. !$#submission submitted to the Brookhaven Protein Data Bank, April 1993 !$#cross-references PDB:1HUC !$#contents annotation; X-ray crystallography, 2.1 angstroms, residues !180-126;129-333 REFERENCE S16513 !$#authors Musil, D.; Zucic, D.; Turk, D.; Engh, R.A.; Mayr, I.; Huber, !1R.; Popovic, T.; Turk, V.; Towatari, T.; Katunuma, N.; Bode, !1W. !$#journal EMBO J. (1991) 10:2321-2330 !$#title The refined 2.15 angstroms X-ray crystal structure of human !1liver cathepsin B: the structural basis for its specificity. !$#cross-references MUID:91330854; PMID:1868826 !$#contents annotation; X-ray crystallography, 2.1 angstroms COMMENT Cathepsin B is enzymatically active both in the single chain !1form and in the two chain form. GENETICS !$#gene GDB:CTSB !'##cross-references GDB:119087; OMIM:116810 !$#map_position 8p22-8p22 COMPLEX monomer (single chain form) or heterodimer of disulfide !1bonded light and heavy chains derived from the same !1precursor (two chain form) FUNCTION !$#description broad specificity endopeptidase and peptidyl dipeptidase !$#pathway intracellular protein degradation CLASSIFICATION #superfamily papain KEYWORDS cysteine proteinase; glycoprotein; hydrolase; lysosome; !1protein degradation FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-79 #domain propeptide #status predicted #label PRO\ !$80-333 #product cathepsin B (single chain form) #status !8experimental #label MAT1\ !$80-126 #domain light chain #status experimental #label CHL\ !$80-126,129-333 #product cathepsin B #status experimental #label !8MAT2\ !$129-333 #domain heavy chain #status experimental #label CHH\ !$93-122,105-150, !$141-207,142-146, !$179-211,187-198 #disulfide_bonds #status experimental\ !$108,278,298 #active_site Cys, His, Asn #status predicted\ !$192 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$289 #binding_site carbohydrate (Asn) (covalent) #status !8absent SUMMARY #length 339 #molecular-weight 37807 #checksum 6015 SEQUENCE /// ENTRY KHBOB #type complete TITLE cathepsin B (EC 3.4.22.1) precursor - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Mar-1992 #sequence_revision 22-Apr-1995 #text_change 20-Apr-2000 ACCESSIONS S38328; A39475; A28103; A27013; S02674; A05143; S69337; !1I46007 REFERENCE S38328 !$#authors Mordier, S.; Bechet, D.; Roux, M.P.; Obled, A.; Ferrara, M. !$#journal Biochim. Biophys. Acta (1993) 1174:305-311 !$#title Nucleotide sequence of bovine preprocathepsin B. A study of !1polymorphism in the protein coding region. !$#cross-references MUID:93385163; PMID:8373811 !$#accession S38328 !'##molecule_type mRNA !'##residues 1-335 ##label MOR !'##cross-references EMBL:L06075; NID:g289401; PIDN:AAA03064.1; !1PID:g289402 REFERENCE A39475 !$#authors Bechet, D.M.; Ferrara, M.J.; Mordier, S.B.; Roux, M.P.; !1Deval, C.D.; Obled, A. !$#journal J. Biol. Chem. (1991) 266:14104-14112 !$#title Expression of lysosomal cathepsin B during calf !1myoblast-myotube differentiation. Characterization of a cDNA !1encoding bovine cathepsin B. !$#cross-references MUID:91310702; PMID:1856234 !$#accession A39475 !'##molecule_type mRNA !'##residues 214-335 ##label BEC !'##cross-references GB:M64620; NID:g162812; PIDN:AAA30434.1; !1PID:g162813 REFERENCE A28103 !$#authors Meloun, B.; Baudys, M.; Pohl, J.; Pavlik, M.; Kostka, V. !$#journal J. Biol. Chem. (1988) 263:9087-9093 !$#title Amino acid sequence of bovine spleen cathepsin B. !$#cross-references MUID:88243785; PMID:3379063 !$#accession A28103 !'##molecule_type protein !'##residues 80-153,'E',155-207,'N',209-296,'A',298-332 ##label MEL !'##experimental_source spleen REFERENCE A27013 !$#authors Meloun, B.; Pohl, J.; Kostka, V. !$#book Cysteine Proteinases and Their Inhibitors, Turk, V., ed., !1pp.19-29, Walter de Gruyter, Berlin and New York, 1986 !$#title Tentative amino acid sequence of bovine spleen cathepsin B. !$#accession A27013 !'##molecule_type protein !'##residues 80-153,'E',155-163,'G',165-207,'N',209-220,'ZB',223-296, !1'AB',299-302,'B',304-305,'BB',308-332,'X' ##label ME2 REFERENCE S02674 !$#authors Baudys, M.; Meloun, B.; Pohl, J.; Kostka, V. !$#journal Biol. Chem. Hoppe-Seyler (1988) 369(Suppl.):169-174 !$#title Identification of the second (buried) cysteine residue and !1of the C-terminal disulfide bridge of bovine spleen !1cathepsin B. !$#cross-references MUID:89076501; PMID:3144290 !$#accession S02674 !'##molecule_type protein !'##residues 224-237;310-332 ##label BAU !'##note 319-Cys is not involved in a disulfide bond REFERENCE A05143 !$#authors Pohl, J.; Baudys, M.; Tomasek, V.; Kostka, V. !$#journal FEBS Lett. (1982) 142:23-26 !$#cross-references MUID:82262056; PMID:7106283 !$#accession A05143 !'##molecule_type protein !'##residues 80-126 ##label POH REFERENCE I46007 !$#authors Mordier, S.B.; Bechet, D.M.; Roux, M.P.; Obled, A.; Ferrara, !1M.J. !$#journal Eur. J. Biochem. (1995) 229:35-44 !$#title The structure of the bovine cathepsin B gene. Genetic !1variability in the 3' untranslated region. !$#cross-references MUID:95262685; PMID:7744047 !$#accession S69337 !'##molecule_type DNA !'##residues 1-335 ##label MOW !'##cross-references EMBL:U16336; NID:g809477; PIDN:AAA80198.1; !1PID:g809479 !'##note the authors translated the codon CAG for residue 334 as Glu COMMENT Cathepsin B is enzymatically active both in the single chain !1form and in the disulfide-linked heavy and light chain form. GENETICS !$#introns 42/3; 71/2; 109/3; 149/2; 178/1; 226/1; 265/1; 308/1 FUNCTION !$#description broad specificity endopeptidase and peptidyl dipeptidase !$#pathway intracellular protein degradation CLASSIFICATION #superfamily papain KEYWORDS cysteine proteinase; glycoprotein; hydrolase; lysosome; !1protein degradation FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-79 #domain propeptide #status predicted #label PRO\ !$80-332 #product cathepsin B #status experimental #label MAT\ !$80-126 #product cathepsin B light chain #status experimental !8#label MAL\ !$129-332 #product cathepsin B heavy chain #status experimental !8#label MAH\ !$93-122,227-331 #disulfide_bonds #status experimental\ !$105-150,141-207, !$142-146,179-211, !$187-198 #disulfide_bonds #status predicted\ !$108 #active_site Cys #status experimental\ !$192 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$278,298 #active_site His, Asn #status predicted\ !$289 #binding_site carbohydrate (Asn) (covalent) #status !8absent SUMMARY #length 335 #molecular-weight 36661 #checksum 5181 SEQUENCE /// ENTRY KHRTB #type complete TITLE cathepsin B (EC 3.4.22.1) precursor - rat ALTERNATE_NAMES cathepsin B1; RSG-2 protein ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 18-Apr-1984 #sequence_revision 01-Dec-1995 #text_change 16-Jun-2000 ACCESSIONS S51041; A00977; I59019 REFERENCE S51041 !$#authors Guenette, R.S.; Mooibroek, M.; Wong, K.; Wong, P.; !1Tenniswood, M. !$#journal Eur. J. Biochem. (1994) 226:311-321 !$#title Cathepsin B, a cysteine protease implicated in metastatic !1progression, is also expressed during regression of the rat !1prostate and mammary glands. !$#cross-references MUID:95094788; PMID:8001549 !$#accession S51041 !'##status preliminary !'##molecule_type mRNA !'##residues 1-339 ##label GUE !'##cross-references GB:X82396; NID:g1524327; PIDN:CAA57792.1; !1PID:g1524328 REFERENCE A00976 !$#authors Takio, K.; Towatari, T.; Katunuma, N.; Teller, D.C.; Titani, !1K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:3666-3670 !$#title Homology of amino acid sequences of rat liver cathepsins B !1and H with that of papain. !$#cross-references MUID:83221657; PMID:6574504 !$#accession A00977 !'##molecule_type protein !'##residues 80-126,129-158,'G',160-333 ##label TAK REFERENCE I59019 !$#authors San Segundo, B.; Chan, S.J.; Steiner, D.F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:2320-2324 !$#title Identification of cDNA clones encoding a precursor of rat !1liver cathepsin B. !$#cross-references MUID:85190489; PMID:2986112 !$#accession I59019 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 69-339 ##label RES !'##cross-references GB:M11305; NID:g203647; PIDN:AAA40993.1; !1PID:g203648 FUNCTION !$#description broad specificity endopeptidase and peptidyl dipeptidase !$#pathway intracellular protein degradation CLASSIFICATION #superfamily papain KEYWORDS cysteine proteinase; glycoprotein; hydrolase; lysosome; !1protein degradation FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-79 #domain propeptide #status predicted #label PRO\ !$80-126 #domain light chain #status experimental #label CHL\ !$80-126,129-333 #product cathepsin B #status experimental #label MAT\ !$129-333 #domain heavy chain #status experimental #label CHH\ !$93-122,105-150, !$141-207,142-146, !$179-211,187-198 #disulfide_bonds #status predicted\ !$108,278,298 #active_site Cys, His, Asn #status predicted\ !$192 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 339 #molecular-weight 37470 #checksum 3297 SEQUENCE /// ENTRY KHMSB #type complete TITLE cathepsin B (EC 3.4.22.1) precursor - mouse ALTERNATE_NAMES preprocathepsin B ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Mar-1992 #sequence_revision 26-Apr-1996 #text_change 18-Jun-1999 ACCESSIONS A38458; A49826; B26498; S12901; PS0360 REFERENCE A38458 !$#authors Qian, F.; Frankfater, A.; Chan, S.J.; Steiner, D.F. !$#journal DNA Cell Biol. (1991) 10:159-168 !$#title The structure of the mouse cathepsin B gene and its putative !1promoter. !$#cross-references MUID:91190267; PMID:2012677 !$#accession A38458 !'##molecule_type DNA !'##residues 1-339 ##label QIA !'##cross-references GB:M63999 REFERENCE A49826 !$#authors Qian, F.; Frankfater, A.; Steiner, D.F.; Bajkowski, A.S.; !1Chan, S.J. !$#journal Anticancer Res. (1991) 11:1445-1451 !$#title Characterization of multiple cathepsin B mRNAs in murine !1B16a melanoma. !$#cross-references MUID:92082172; PMID:1746902 !$#accession A49826 !'##molecule_type mRNA !'##residues 1-339 ##label QI2 !'##cross-references GB:S69034; NID:g239906; PIDN:AAB20536.1; !1PID:g239907 !'##experimental_source B16a melanoma !'##note sequence extracted from NCBI backbone (NCBIN:69034, !1NCBIP:69039) !'##note three mRNA forms from B16a melanoma celss were found to have !1identical coding sequences; normal tissues appeared to !1produce only the smallest of the three forms REFERENCE A26498 !$#authors Chan, S.J.; San Segundo, B.; McCormick, M.B.; Steiner, D.F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:7721-7725 !$#title Nucleotide and predicted amino acid sequences of cloned !1human and mouse preprocathepsin B cDNAs. !$#cross-references MUID:87017021; PMID:3463996 !$#accession B26498 !'##molecule_type mRNA !'##residues 1-159,'N',161-173,'D',175-176,'I',178-283,'V',285-339 !1##label CHA !'##cross-references GB:M14222; NID:g192841; PIDN:AAA37494.1; !1PID:g309202 REFERENCE S12901 !$#authors Ferrara, M.; Wojcik, F.; Rhaissi, H.; Mordier, S.; Roux, !1M.P.; Bechet, D. !$#journal FEBS Lett. (1990) 273:195-199 !$#title Gene structure of mouse cathepsin B. !$#cross-references MUID:91032179; PMID:2226854 !$#accession S12901 !'##molecule_type DNA !'##residues 1-159,'N',161-173,'D',175-176,'I',178-283,'V',285-339 !1##label FER REFERENCE PS0360 !$#authors Friemert, C.; Closs, E.I.; Silbermann, M.; Erfle, V.; !1Strauss, P.G. !$#journal Gene (1991) 103:259-261 !$#title Isolation of a cathepsin B-encoding cDNA from murine !1osteogenic cells. !$#cross-references MUID:91365255; PMID:1889751 !$#accession PS0360 !'##status translation not shown !'##molecule_type mRNA !'##residues 314-339 ##label FRI !'##cross-references EMBL:X54966; NID:g50596; PIDN:CAA38713.1; !1PID:g50597 GENETICS !$#note single copy gene FUNCTION !$#description broad specificity endopeptidase and peptidyl dipeptidase !$#pathway intracellular protein degradation CLASSIFICATION #superfamily papain KEYWORDS cysteine proteinase; glycoprotein; hydrolase; lysosome; !1protein degradation FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$80-339 #product cathepsin B #status predicted #label MAT\ !$38,192 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$93-122,105-150, !$141-207,142-146, !$179-211,187-198 #disulfide_bonds #status predicted\ !$108,278,298 #active_site Cys, His, Asn #status predicted SUMMARY #length 339 #molecular-weight 37280 #checksum 745 SEQUENCE /// ENTRY BPSOP #type complete TITLE streptopain (EC 3.4.22.10) precursor - Streptococcus pyogenes ALTERNATE_NAMES streptococcal cysteine proteinase; streptococcal peptidase A ORGANISM #formal_name Streptococcus pyogenes DATE 24-Apr-1984 #sequence_revision 07-Oct-1994 #text_change 07-Oct-1994 ACCESSIONS S07668; A00978 REFERENCE S07668 !$#authors Yonaha, K.; Elliott, S.D.; Liu, T.Y. !$#journal J. Protein Chem. (1982) 1:317-334 !$#title Primary structure of zymogen of streptococcal proteinase. !$#accession S07668 !'##molecule_type protein !'##residues 1-337 ##label YON REFERENCE A00978 !$#authors Tai, J.Y.; Kortt, A.A.; Liu, T.Y.; Elliott, S.D. !$#journal J. Biol. Chem. (1976) 251:1955-1959 !$#title Primary structure of streptococcal proteinase. III. !1Isolation of cyanogen bromide peptides: complete covalent !1structure of the polypeptide chain. !$#cross-references MUID:76190087; PMID:1270417 !$#accession A00978 !'##molecule_type protein !'##residues 85-107,'L',109-244,'N',246-337 ##label TAI !'##note Trp-298 is at the binding site of the enzyme COMMENT This enzyme can remove the activation peptide from the !1proenzyme. CLASSIFICATION #superfamily streptococcal cysteine proteinase KEYWORDS cysteine proteinase; hydrolase; zymogen FEATURE !$1-84 #domain activation peptide #status experimental !8#label PRO\ !$85-337 #product streptopain #status experimental #label MAT\ !$131,279 #active_site Cys, His #status experimental SUMMARY #length 337 #molecular-weight 36721 #checksum 7142 SEQUENCE /// ENTRY CIHUH #type complete TITLE calpain (EC 3.4.22.17) large chain 1 [validated] - human ALTERNATE_NAMES calpain chain L-1; calpain I catalytic chain; low-calcium requiring, calcium activated neutral proteinase (CANP) large subunit; mu-calpain (micromolar) heavy chain CONTAINS chemotactic factor ORGANISM #formal_name Homo sapiens #common_name man DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 08-Dec-2000 ACCESSIONS A26213; A36740; S10591 REFERENCE A26213 !$#authors Aoki, K.; Imajoh, S.; Ohno, S.; Emori, Y.; Koike, M.; !1Kosaki, G.; Suzuki, K. !$#journal FEBS Lett. (1986) 205:313-317 !$#title Complete amino acid sequence of the large subunit of the !1low-Ca2+-requiring form of human Ca2+-activated neutral !1protease (muCANP) deduced from its cDNA sequence. !$#cross-references MUID:86301172; PMID:3017764 !$#accession A26213 !'##molecule_type mRNA !'##residues 1-714 ##label AOK !'##cross-references EMBL:X04366; NID:g29663; PIDN:CAA27881.1; !1PID:g29664 REFERENCE A36740 !$#authors Kunimatsu, M.; Higashiyama, S.; Sato, K.; Ohkubo, I.; !1Sasaki, M. !$#journal Biochem. Biophys. Res. Commun. (1989) 164:875-882 !$#title Calcium dependent cysteine proteinase is a precursor of a !1chemotactic factor for neutrophils. !$#cross-references MUID:90056492; PMID:2554904 !$#accession A36740 !'##molecule_type protein !'##residues 2-10 ##label KUN !'##experimental_source erythrocytes REFERENCE S10589 !$#authors Sorimachi, H.; Ohmi, S.; Emori, Y.; Kawasaki, H.; Saido, !1T.C.; Ohno, S.; Minami, Y.; Suzuki, K. !$#journal Biol. Chem. Hoppe-Seyler (1990) 371(Suppl.):171-176 !$#title A novel member of the calcium-dependent cysteine protease !1family. !$#cross-references MUID:90380278; PMID:2400579 !$#contents annotation !$#note comparison with other gene products COMMENT Calpain I is activated by micromolar concentrations of !1calcium. GENETICS !$#gene GDB:CAPN1; mu-CANP !'##cross-references GDB:119749; OMIM:114220 !$#map_position 11pter-11qter COMPLEX heterodimer of L (large) and S (small) chains FUNCTION !$#description catalyzes the hydolysis of peptides !$#note cleaves preferentially after tyrosine, methionine, or !1arginine residues and before leucine or valine residues CLASSIFICATION #superfamily calpain large chain; calmodulin repeat !1homology; calpain catalytic domain homology KEYWORDS acetylated amino end; calcium binding; cysteine proteinase; !1duplication; EF hand; heterodimer; hydrolase FEATURE !$2-714 #product calpain large chain 1 #status predicted !8#label MAT\ !$2-10 #product chemotactic factor #status experimental !8#label CHF\ !$85-337 #domain calpain catalytic domain homology #label !8CALP\ !$542-573 #domain calmodulin repeat homology #label EF1\ !$585-617 #domain calmodulin repeat homology #label EF2\ !$618-647 #domain calmodulin repeat homology #label EF3\ !$650-682 #domain calmodulin repeat homology #label EF4\ !$683-714 #domain calmodulin repeat homology #label EF5\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental\ !$115,272,296 #active_site Cys, His, Asn #status predicted SUMMARY #length 714 #molecular-weight 81889 #checksum 2019 SEQUENCE /// ENTRY CICHH #type complete TITLE calpain (EC 3.4.22.17) large chain 4 - chicken ALTERNATE_NAMES calpain catalytic chain; intermediate calcium activated neutral proteinase (CANP); mu/m-type calpain heavy chain ORGANISM #formal_name Gallus gallus #common_name chicken DATE 17-May-1985 #sequence_revision 09-Aug-1997 #text_change 24-Nov-1999 ACCESSIONS A00979 REFERENCE A93348 !$#authors Ohno, S.; Emori, Y.; Imajoh, S.; Kawasaki, H.; Kisaragi, M.; !1Suzuki, K. !$#journal Nature (1984) 312:566-570 !$#title Evolutionary origin of a calcium-dependent protease by !1fusion of genes for a thiol protease and a calcium-binding !1protein? !$#cross-references MUID:85061606; PMID:6095110 !$#accession A00979 !'##molecule_type mRNA !'##residues 1-705 ##label OHN !'##cross-references EMBL:X01415; NID:g63332; PIDN:CAA25658.1; !1PID:g63333 REFERENCE A91354 !$#authors Emori, Y.; Ohno, S.; Tobita, M.; Suzuki, K. !$#journal FEBS Lett. (1986) 194:249-252 !$#cross-references MUID:86082358; PMID:3000828 !$#contents annotation; gene structure COMMENT This calpain has calcium requirements intermediate between !1those of the high- and low-calcium activated calpains. GENETICS !$#introns 82/3; 106/1; 145/3; 190/2; 246/3; 274/3; 303/2; 328/2; 382/ !11; 438/3; 442/3; 513/2; 526/3; 548/3; 568/1; 589/3; 612/3; !1639/1; 678/1; 697/3 COMPLEX heterodimer of L (large) and S (small) chains FUNCTION !$#description catalyzes the hydolysis of peptides !$#note cleaves preferentially after tyrosine, methionine, or !1arginine residues and before leucine or valine residues CLASSIFICATION #superfamily calpain large chain; calmodulin repeat !1homology; calpain catalytic domain homology KEYWORDS blocked amino end; calcium binding; cysteine proteinase; !1duplication; EF hand; heterodimer; hydrolase FEATURE !$78-330 #domain calpain catalytic domain homology #label !8CALP\ !$533-564 #domain calmodulin repeat homology #label EF1\ !$576-608 #domain calmodulin repeat homology #label EF2\ !$609-638 #domain calmodulin repeat homology #label EF3\ !$641-673 #domain calmodulin repeat homology #label EF4\ !$674-705 #domain calmodulin repeat homology #label EF5\ !$2 #modified_site blocked amino end (Met) (in mature !8form) #status experimental\ !$108,265,289 #active_site Cys, His, Asn #status predicted SUMMARY #length 705 #molecular-weight 80351 #checksum 5631 SEQUENCE /// ENTRY CIHUH2 #type complete TITLE calpain (EC 3.4.22.17) large chain 2 - human ALTERNATE_NAMES calpain chain L-2; calpain II catalytic chain; high-calcium requiring, calcium activated neutral proteinase (CANP) large subunit; m-calpain (millimolar) heavy chain ORGANISM #formal_name Homo sapiens #common_name man DATE 21-Nov-1993 #sequence_revision 09-Aug-1997 #text_change 16-Jul-1999 ACCESSIONS S10590; A31218; A33529 REFERENCE S10589 !$#authors Sorimachi, H.; Ohmi, S.; Emori, Y.; Kawasaki, H.; Saido, !1T.C.; Ohno, S.; Minami, Y.; Suzuki, K. !$#journal Biol. Chem. Hoppe-Seyler (1990) 371(Suppl.):171-176 !$#title A novel member of the calcium-dependent cysteine protease !1family. !$#cross-references MUID:90380278; PMID:2400579 !$#accession S10590 !'##molecule_type mRNA !'##residues 1-700 ##label SOR REFERENCE A31218 !$#authors Imajoh, S.; Aoki, K.; Ohno, S.; Emori, Y.; Kawasaki, H.; !1Sugihara, H.; Suzuki, K. !$#journal Biochemistry (1988) 27:8122-8128 !$#title Molecular cloning of the cDNA for the large subunit of the !1high-Ca(2+)-requiring form of human Ca(2+)-activated neutral !1protease. !$#cross-references MUID:89166474; PMID:2852952 !$#accession A31218 !'##molecule_type mRNA; protein !'##residues 1-210,'I',212-394,'D',396-445,'I',447-700 ##label IMA !'##cross-references GB:M23254; NID:g511636; PIDN:AAA35645.1; !1PID:g511637 !'##note parts of this sequence were determined by protein sequencing; !1the amino end of the mature protein is blocked REFERENCE A33529 !$#authors Hata, A.; Ohno, S.; Akita, Y.; Suzuki, K. !$#journal J. Biol. Chem. (1989) 264:6404-6411 !$#title Tandemly reiterated negative enhancer-like elements regulate !1transcription of a human gene for the large subunit of !1calcium-dependent protease. !$#cross-references MUID:89197947; PMID:2539381 !$#accession A33529 !'##molecule_type DNA !'##residues 1-67,'G',69-72,'IE',75-78,'R' ##label HAT !'##cross-references DDBJ:J04700; NID:g179910; PIDN:AAA52760.1; !1PID:g463086 GENETICS !$#gene GDB:CAPN2; mCANP; CANPml !'##cross-references GDB:119750; OMIM:114230 !$#map_position 1pter-1qter COMPLEX heterodimer of L (large) and S (small) chains FUNCTION !$#description catalyzes the hydolysis of peptides !$#note cleaves preferentially after tyrosine, methionine, or !1arginine residues and before leucine or valine residues CLASSIFICATION #superfamily calpain large chain; calmodulin repeat !1homology; calpain catalytic domain homology KEYWORDS acetylated amino end; calcium binding; cysteine proteinase; !1EF hand; heterodimer; hydrolase FEATURE !$2-700 #product calpain large chain 2 #status predicted !8#label MAT\ !$75-327 #domain calpain catalytic domain homology #label !8CALP\ !$529-560 #domain calmodulin repeat homology #label EF1\ !$572-604 #domain calmodulin repeat homology #label EF2\ !$605-634 #domain calmodulin repeat homology #label EF3\ !$637-669 #domain calmodulin repeat homology #label EF4\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status predicted\ !$105,262,286 #active_site Cys, His, Asn #status predicted SUMMARY #length 700 #molecular-weight 80020 #checksum 8484 SEQUENCE /// ENTRY CIHUH3 #type complete TITLE calpain (EC 3.4.22.17) large chain 3 - human ALTERNATE_NAMES calpain chain L-3; calpain III catalytic chain; muscle specific, calcium activated neutral proteinase 3 (CANP3) large subunit; skeletal muscle protein p94 ORGANISM #formal_name Homo sapiens #common_name man DATE 28-Apr-1995 #sequence_revision 09-Aug-1997 #text_change 16-Jul-1999 ACCESSIONS A56218; A34488 REFERENCE A56218 !$#authors Richard, I.; Broux, O.; Allamand, V.; Fougerousse, F.; !1Chiannilkulchai, N.; Bourg, N.; Brenguier, L.; Devaud, C.; !1Pasturaud, P.; Roudaut, C.; Hillaire, D.; Passos-Bueno, !1M.R.; Zatz, M.; Tischfield, J.A.; Fardeau, M.; Jackson, !1C.E.; Cohen, D.; Beckmann, J.S. !$#journal Cell (1995) 81:27-40 !$#title Mutations in the proteolytic enzyme calpain 3 cause !1limb-girdle muscular dystrophy type 2A. !$#cross-references MUID:95236448; PMID:7720071 !$#accession A56218 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-821 ##label RIC !'##cross-references GB:X85030; NID:g791039; PIDN:CAA59403.1; !1PID:g791040 REFERENCE A94688 !$#authors Sorimachi, H.; Imajoh-Ohmi, S.; Emori, Y.; Kawasaki, H.; !1Ohno, S.; Minami, Y.; Suzuki, K. !$#journal J. Biol. Chem. (1989) 264:20106-20111 !$#title Molecular cloning of a novel mammalian calcium-dependent !1protease distinct from both m- and mu- types. Specific !1expression of the mRNA in skeletal muscle. !$#cross-references MUID:90062125; PMID:2555341 !$#accession A34488 !'##molecule_type mRNA !'##residues 44-445,'AA',448-458,'P',460-461,'P',463-484,'T',486-821 !1##label SOR GENETICS !$#gene GDB:CAPN3; CANP3; LGMD2A; LGMD2 !'##cross-references GDB:119751; OMIM:114240; OMIM:253600 !$#map_position 15pter-15qter !$#note defects in this gene can cause limb girdle muscular !1dystrophy 2A COMPLEX heterodimer of L (large) and S (small) chains FUNCTION !$#description catalyzes the hydolysis of peptides !$#note cleaves preferentially after tyrosine, methionine, or !1arginine residues and before leucine or valine residues CLASSIFICATION #superfamily calpain large chain; calmodulin repeat !1homology; calpain catalytic domain homology KEYWORDS calcium binding; cysteine proteinase; EF hand; hydrolase; !1muscular dystrophy FEATURE !$99-267,323-400 #domain calpain catalytic domain homology #status !8atypical #label CALP\ !$649-680 #domain calmodulin repeat homology #label EF1\ !$692-724 #domain calmodulin repeat homology #label EF2\ !$725-754 #domain calmodulin repeat homology #label EF3\ !$757-789 #domain calmodulin repeat homology #label EF4\ !$790-821 #domain calmodulin repeat homology #label EF5\ !$129,334,358 #active_site Cys, His, Asn #status predicted SUMMARY #length 821 #molecular-weight 94253 #checksum 9513 SEQUENCE /// ENTRY B34488 #type complete TITLE calpain (EC 3.4.22.17) large chain 3 - rat ALTERNATE_NAMES cysteine proteinase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B34488; S10589 REFERENCE A94688 !$#authors Sorimachi, H.; Imajoh-Ohmi, S.; Emori, Y.; Kawasaki, H.; !1Ohno, S.; Minami, Y.; Suzuki, K. !$#journal J. Biol. Chem. (1989) 264:20106-20111 !$#title Molecular cloning of a novel mammalian calcium-dependent !1protease distinct from both m- and mu- types. Specific !1expression of the mRNA in skeletal muscle. !$#cross-references MUID:90062125; PMID:2555341 !$#accession B34488 !'##molecule_type mRNA !'##residues 1-821 ##label SOR !'##cross-references GB:J05121; NID:g205955; PIDN:AAA41790.1; !1PID:g205956 REFERENCE S10589 !$#authors Sorimachi, H.; Ohmi, S.; Emori, Y.; Kawasaki, H.; Saido, !1T.C.; Ohno, S.; Minami, Y.; Suzuki, K. !$#journal Biol. Chem. Hoppe-Seyler (1990) 371(Suppl.):171-176 !$#title A novel member of the calcium-dependent cysteine protease !1family. !$#cross-references MUID:90380278; PMID:2400579 !$#accession S10589 !'##status preliminary !'##molecule_type mRNA !'##residues 1-50,'E',52-211,'V',213-252,'K',254-821 ##label SO2 CLASSIFICATION #superfamily calpain large chain; calmodulin repeat !1homology; calpain catalytic domain homology KEYWORDS calcium binding; cysteine proteinase; EF hand; hydrolase FEATURE !$99-400 #domain calpain catalytic domain homology #status !8atypical #label CALP\ !$649-680 #domain calmodulin repeat homology #label EF1\ !$692-724 #domain calmodulin repeat homology #label EF2\ !$725-754 #domain calmodulin repeat homology #label EF3\ !$757-789 #domain calmodulin repeat homology #label EF4\ !$790-821 #domain calmodulin repeat homology #label EF5\ !$129,334,358 #active_site Cys, His, Asn #status predicted SUMMARY #length 821 #molecular-weight 94127 #checksum 7401 SEQUENCE /// ENTRY S57196 #type complete TITLE calpain (EC 3.4.22.17) large chain 3 - chicken ALTERNATE_NAMES calpain p94 heavy chain; n-calpain-1 heavy chain ORGANISM #formal_name Gallus gallus #common_name chicken DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S57196 REFERENCE S57194 !$#authors Sorimachi, H.; Tsukahara, T.; Okada-Ban, M.; Sugita, H.; !1Ishiura, S.; Suzuki, K. !$#journal Biochim. Biophys. Acta (1995) 1261:381-393 !$#title Identification of a third ubiquitous calpain species - !1chicken muscle expresses four distinct calpains. !$#cross-references MUID:95260862; PMID:7742367 !$#accession S57196 !'##status preliminary !'##molecule_type mRNA !'##residues 1-810 ##label SOR !'##cross-references EMBL:D38028; NID:g882072; PIDN:BAA07230.1; !1PID:g1552167 CLASSIFICATION #superfamily calpain large chain; calmodulin repeat !1homology; calpain catalytic domain homology KEYWORDS cysteine proteinase; EF hand; hydrolase FEATURE !$93-393 #domain calpain catalytic domain homology #label !8CALP\ !$746-778 #domain calmodulin repeat homology #label EFH SUMMARY #length 810 #molecular-weight 93560 #checksum 6725 SEQUENCE /// ENTRY A39343 #type complete TITLE calpain (EC 3.4.22.17) large chain - fluke (Schistosoma mansoni) ORGANISM #formal_name Schistosoma mansoni DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A39343; A45642 REFERENCE A39343 !$#authors Andresen, K.; Tom, T.D.; Strand, M. !$#journal J. Biol. Chem. (1991) 266:15085-15090 !$#title Characterization of cDNA clones encoding a novel !1calcium-activated neutral proteinase from Schistosoma !1mansoni. !$#cross-references MUID:91332027; PMID:1869543 !$#accession A39343 !'##status preliminary !'##molecule_type mRNA !'##residues 1-758 ##label AND !'##cross-references GB:M67499; NID:g160936; PIDN:AAA29858.1; !1PID:g160937 REFERENCE A45642 !$#authors Karcz, S.R.; Podesta, R.B.; Siddiqui, A.A.; Dekaban, G.A.; !1Strejan, G.H.; Clarke, M.W. !$#journal Mol. Biochem. Parasitol. (1991) 49:333-336 !$#title Molecular cloning and sequence analysis of a !1calcium-activated neutral protease (calpain) from !1Schistosoma mansoni. !$#cross-references MUID:92131071; PMID:1775175 !$#accession A45642 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-14,'A',16-120,'A',121-127,'H',129-213,'R',215-384,'VTC', !1388-440,'S',442-754,'S',756,'Y',758 ##label KAR !'##cross-references GB:M74233; NID:g160934 !'##note sequence extracted from NCBI backbone (NCBIP:79194) CLASSIFICATION #superfamily calpain large chain; calmodulin repeat !1homology; calpain catalytic domain homology KEYWORDS calcium binding; cysteine proteinase; duplication; EF hand; !1hydrolase FEATURE !$124-380 #domain calpain catalytic domain homology #label !8CALP\ !$628-660 #domain calmodulin repeat homology #label EF1\ !$661-690 #domain calmodulin repeat homology #label EF2\ !$693-726 #domain calmodulin repeat homology #label EF3\ !$727-758 #domain calmodulin repeat homology #label EF4\ !$154,313,337 #active_site Cys, His, Asn #status predicted SUMMARY #length 758 #molecular-weight 86920 #checksum 9832 SEQUENCE /// ENTRY A55054 #type complete TITLE calpain (EC 3.4.22.17) large chain - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 08-Jul-1995 #sequence_revision 03-Aug-1995 #text_change 18-Jun-1999 ACCESSIONS A55054 REFERENCE A55054 !$#authors Emori, Y.; Saigo, K. !$#journal J. Biol. Chem. (1994) 269:25137-25142 !$#title Calpain localization changes in coordination with !1actin-related cytoskeletal changes during early embryonic !1development of Drosophila. !$#cross-references MUID:95014293; PMID:7929201 !$#accession A55054 !'##status preliminary; nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-805 ##label EMO !'##cross-references GB:X78555; NID:g562287; PIDN:CAA55297.1; !1PID:g562288 GENETICS !$#gene FlyBase:CalpA !'##cross-references FlyBase:FBgn0012051 CLASSIFICATION #superfamily calpain large chain; calmodulin repeat !1homology; calpain catalytic domain homology KEYWORDS cysteine proteinase; duplication; EF hand; hydrolase FEATURE !$90-347 #domain calpain catalytic domain homology #label !8CALP\ !$676-708 #domain calmodulin repeat homology #label EF1\ !$709-738 #domain calmodulin repeat homology #label EF2\ !$741-773 #domain calmodulin repeat homology #label EF3\ !$774-805 #domain calmodulin repeat homology #label EF4 SUMMARY #length 805 #molecular-weight 91522 #checksum 5426 SEQUENCE /// ENTRY S44749 #type complete TITLE C06G4.2 protein - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S44749 REFERENCE S44747 !$#authors Waterston, R. !$#submission submitted to the EMBL Data Library, November 1993 !$#description Sequence of the C. elegans cosmid C06G4. !$#accession S44749 !'##status preliminary !'##molecule_type DNA !'##residues 1-653 ##label WAT !'##cross-references EMBL:L25598; NID:g409290; PIDN:AAA27940.1; !1PID:g409293 GENETICS !$#introns 26/1; 69/1; 216/3; 269/3; 357/2; 401/2; 558/1; 583/3; 613/3 CLASSIFICATION #superfamily C06G4.2 protein; calpain catalytic domain !1homology FEATURE !$245-498 #domain calpain catalytic domain homology #label CALP SUMMARY #length 653 #molecular-weight 70893 #checksum 2833 SEQUENCE /// ENTRY CIHUL #type complete TITLE calpain (EC 3.4.22.17) small chain - human ALTERNATE_NAMES calcium-activated neutral proteinase (CANP) ORGANISM #formal_name Homo sapiens #common_name man DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 16-Jul-1999 ACCESSIONS A26107; A23650 REFERENCE A93648 !$#authors Miyake, S.; Emori, Y.; Suzuki, K. !$#journal Nucleic Acids Res. (1986) 14:8805-8817 !$#title Gene organization of the small subunit of human !1calcium-activated neutral protease. !$#cross-references MUID:87066759; PMID:3024120 !$#accession A26107 !'##molecule_type DNA !'##residues 1-268 ##label MIY !'##cross-references GB:M31502 REFERENCE A93631 !$#authors Ohno, S.; Emori, Y.; Suzuki, K. !$#journal Nucleic Acids Res. (1986) 14:5559 !$#title Nucleotide sequence of a cDNA coding for the small subunit !1of human calcium-dependent protease. !$#cross-references MUID:86286563; PMID:3016651 !$#accession A23650 !'##molecule_type mRNA !'##residues 1-268 ##label OHN !'##cross-references EMBL:X04106; NID:g35327; PIDN:CAA27726.1; !1PID:g35328 GENETICS !$#gene GDB:CAPN4 !'##cross-references GDB:119752; OMIM:114170 !$#map_position 19pter-19qter !$#introns 70/2; 81/3; 111/3; 131/1; 152/3; 175/3; 202/1; 241/1; 260/3 COMPLEX heterodimer of L (large) and S (small) chains FUNCTION !$#description catalyzes the hydolysis of peptides !$#note cleaves preferentially after tyrosine, methionine, or !1arginine residues and before leucine or valine residues CLASSIFICATION #superfamily calpain small chain; calmodulin repeat homology KEYWORDS calcium binding; cysteine proteinase; duplication; EF hand; !1heterodimer; hydrolase FEATURE !$1-56 #domain glycine-rich #label GLY\ !$96-127 #domain calmodulin repeat homology #label EF1\ !$139-171 #domain calmodulin repeat homology #label EF2\ !$172-201 #domain calmodulin repeat homology #label EF3\ !$204-236 #domain calmodulin repeat homology #label EF4\ !$237-268 #domain calmodulin repeat homology #label EF5 SUMMARY #length 268 #molecular-weight 28316 #checksum 7141 SEQUENCE /// ENTRY CIPGL #type complete TITLE calpain (EC 3.4.22.17) small chain - pig ALTERNATE_NAMES calcium-activated neutral proteinase (CANP); calpain light chain; calpain regulatory chain; calpain S chain;CIHUL ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 16-Jul-1999 ACCESSIONS A25166; B25166 REFERENCE A25166 !$#authors Sakihama, T.; Kakidani, H.; Zenita, K.; Yumoto, N.; Kikuchi, !1T.; Sasaki, T.; Kannagi, R.; Nakanishi, S.; Ohmori, M.; !1Takio, K.; Titani, K.; Murachi, T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:6075-6079 !$#title A putative Ca2+-binding protein: structure of the light !1subunit of porcine calpain elucidated by molecular cloning !1and protein sequence analysis. !$#cross-references MUID:85298299; PMID:2994060 !$#accession A25166 !'##molecule_type mRNA !'##residues 1-266 ##label SAK !'##cross-references GB:M11778; NID:g164402; PIDN:AAA31010.1; !1PID:g164403; GB:M11779; NID:g164404; PID:g164405 !$#accession B25166 !'##molecule_type protein !'##residues 2-56;125-143;157-177;247-248;250-256;265-266 ##label SA2 COMPLEX heterodimer of L (large) and S (small) chains FUNCTION !$#description catalyzes the hydolysis of peptides !$#note cleaves preferentially after tyrosine, methionine, or !1arginine residues and before leucine or valine residues CLASSIFICATION #superfamily calpain small chain; calmodulin repeat homology KEYWORDS acetylated amino end; calcium binding; cysteine proteinase; !1duplication; EF hand; heterodimer; hydrolase FEATURE !$1-54 #domain glycine-rich #label GLY\ !$94-125 #domain calmodulin repeat homology #label EF1\ !$137-169 #domain calmodulin repeat homology #label EF2\ !$170-199 #domain calmodulin repeat homology #label EF3\ !$202-234 #domain calmodulin repeat homology #label EF4\ !$235-266 #domain calmodulin repeat homology #label EF5\ !$1 #modified_site acetylated amino end (Met) #status !8experimental SUMMARY #length 266 #molecular-weight 28068 #checksum 1230 SEQUENCE /// ENTRY CIRBL #type complete TITLE calpain (EC 3.4.22.17) small chain - rabbit ALTERNATE_NAMES calcium-activated neutral proteinase (CANP); calpain light chain; calpain regulatory chain; calpain S chain;CIHUL ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 16-Jul-1999 ACCESSIONS A24816 REFERENCE A24816 !$#authors Emori, Y.; Kawasaki, H.; Imajoh, S.; Kawashima, S.; Suzuki, !1K. !$#journal J. Biol. Chem. (1986) 261:9472-9476 !$#title Isolation and sequence analysis of cDNA clones for the small !1subunit of rabbit calcium-dependent protease. !$#cross-references MUID:86250903; PMID:3013892 !$#accession A24816 !'##molecule_type mRNA !'##residues 1-266 ##label EMO !'##cross-references GB:M13364; NID:g164875; PIDN:AAA81565.1; !1PID:g164876 COMPLEX heterodimer of L (large) and S (small) chains FUNCTION !$#description catalyzes the hydolysis of peptides !$#note cleaves preferentially after tyrosine, methionine, or !1arginine residues and before leucine or valine residues CLASSIFICATION #superfamily calpain small chain; calmodulin repeat homology KEYWORDS calcium binding; cysteine proteinase; duplication; EF hand; !1heterodimer; hydrolase FEATURE !$1-54 #domain glycine-rich #label GLY\ !$94-125 #domain calmodulin repeat homology #label EF1\ !$137-169 #domain calmodulin repeat homology #label EF2\ !$170-199 #domain calmodulin repeat homology #label EF3\ !$202-234 #domain calmodulin repeat homology #label EF4\ !$235-266 #domain calmodulin repeat homology #label EF5 SUMMARY #length 266 #molecular-weight 28239 #checksum 390 SEQUENCE /// ENTRY PEHU #type complete TITLE pepsin A (EC 3.4.23.1) 3 precursor [validated] - human ALTERNATE_NAMES pepsinogen A isozyme 3 ORGANISM #formal_name Homo sapiens #common_name man DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 08-Dec-2000 ACCESSIONS A00980; PX0023; S02663; F22434; I54252; PX0024 REFERENCE A00980 !$#authors Sogawa, K.; Fujii-Kuriyama, Y.; Mizukami, Y.; Ichihara, Y.; !1Takahashi, K. !$#journal J. Biol. Chem. (1983) 258:5306-5311 !$#title Primary structure of human pepsinogen gene. !$#cross-references MUID:83161158; PMID:6300126 !$#accession A00980 !'##molecule_type DNA !'##residues 1-388 ##label SOG !'##cross-references GB:J00279 REFERENCE PX0023 !$#authors Athauda, S.B.P.; Tanji, M.; Kageyama, T.; Takahashi, K. !$#journal J. Biochem. (1989) 106:920-927 !$#title A comparative study on the NH2-terminal amino acid sequences !1and some other properties of six isozymic forms of human !1pepsinogens and pepsins. !$#cross-references MUID:90130402; PMID:2515193 !$#accession PX0023 !'##molecule_type protein !'##residues 16-100 ##label ATH REFERENCE S02663 !$#authors Foltmann, B. !$#journal FEBS Lett. (1988) 241:69-72 !$#title Activation of human pepsinogens. !$#cross-references MUID:89065108; PMID:3197840 !$#accession S02663 !'##molecule_type protein !'##residues 16-68 ##label FOL REFERENCE A22434 !$#authors Ichihara, Y.; Sogawa, K.; Takahashi, K. !$#journal J. Biochem. (1985) 98:483-492 !$#title Isolation of human, swine, and rat prepepsinogens and calf !1preprochymosin, and determination of the primary structures !1of their NH2-terminal signal sequences. !$#cross-references MUID:86059312; PMID:2415509 !$#accession F22434 !'##molecule_type protein !'##residues 1-15,'XXX',19-20,'X',22,'XX',25-26,'X',28 ##label ICH REFERENCE I54252 !$#authors Evers, M.P.J.; Zelle, B.; Peeper, D.S.; Mager, W.H.; Planta, !1R.J.; Eriksson, A.W.; Frants, R.R. !$#journal Hum. Genet. (1987) 77:182-187 !$#title Molecular cloning of a pair of human pepsinogen A genes !1which differ by a Glu->Lys mutation in the activation !1peptide. !$#cross-references MUID:88006181; PMID:3115885 !$#accession I54252 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-27,'F',29-73 ##label RES !'##cross-references GB:M27598; NID:g189834; PIDN:AAA36431.1; !1PID:g189836 GENETICS !$#gene GDB:PGA3 !'##cross-references GDB:119482; OMIM:169710 !$#map_position 11q13.1-11q13.5 !$#introns 19/2; 73/3; 113/1; 152/3; 219/2; 258/2; 306/3; 339/3 CLASSIFICATION #superfamily pepsin KEYWORDS aspartic proteinase; gastric juice; hydrolase; !1phosphoprotein; protein digestion; stomach FEATURE !$1-15 #domain signal sequence #status experimental #label !8SIG\ !$16-388 #product pepsinogen A 3 #status experimental #label !8ZYM\ !$16-62 #domain activation peptide #status experimental !8#label APT\ !$60-388 #product pepsin A 3, minor variant #status !8experimental #label MIN\ !$63-388 #product pepsin A 3 #status experimental #label MAT\ !$94,277 #active_site Asp #status predicted\ !$130 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 388 #molecular-weight 41977 #checksum 8874 SEQUENCE /// ENTRY PEMQAR #type complete TITLE pepsin A (EC 3.4.23.1) precursor - rhesus macaque ALTERNATE_NAMES pepsinogen A ORGANISM #formal_name Macaca mulatta #common_name rhesus macaque DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 18-Jun-1999 ACCESSIONS JT0309 REFERENCE JT0309 !$#authors Evers, M.P.J.; Zelle, B.; Bebelman, J.P.; Pronk, J.C.; !1Mager, W.H.; Planta, R.J.; Eriksson, A.W.; Frants, R.R. !$#journal Gene (1988) 65:179-185 !$#title Cloning and sequencing of rhesus monkey pepsinogen A cDNA. !$#cross-references MUID:88313666; PMID:2900796 !$#accession JT0309 !'##molecule_type mRNA !'##residues 1-388 ##label EVE !'##cross-references GB:M20788; NID:g342274; PIDN:AAA36902.1; !1PID:g342275 CLASSIFICATION #superfamily pepsin KEYWORDS aspartic proteinase; gastric juice; hydrolase; !1phosphoprotein; protein digestion; stomach FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-388 #product pepsinogen #status predicted #label MAT\ !$16-62 #domain activation peptide #status predicted #label !8APT\ !$63-388 #product pepsin #status predicted #label ENZ\ !$94,277 #active_site Asp #status predicted SUMMARY #length 388 #molecular-weight 41696 #checksum 8161 SEQUENCE /// ENTRY PEMQAJ #type complete TITLE pepsin A (EC 3.4.23.1) 1 precursor - Japanese macaque ALTERNATE_NAMES pepsinogen A isozyme 1 ORGANISM #formal_name Macaca fuscata #common_name Japanese macaque DATE 13-Aug-1986 #sequence_revision 19-Oct-1995 #text_change 18-Jun-1999 ACCESSIONS S19681; A91960; A92579; A00981 REFERENCE S19681 !$#authors Kageyama, T.; Tanabe, K.; Koiwai, O. !$#journal Eur. J. Biochem. (1991) 202:205-215 !$#title Development-dependent expression of isozymogens of monkey !1pepsinogens and structural differences between them. !$#cross-references MUID:92037645; PMID:1935977 !$#accession S19681 !'##molecule_type mRNA !'##residues 1-388 ##label KAG !'##cross-references EMBL:X59752; NID:g38074; PIDN:CAA42424.1; !1PID:g38075 !'##note parts of sequence, including amino ends of pepsinogen and !1activation intermediates, confirmed by protein sequencing REFERENCE A91960 !$#authors Kageyama, T.; Takahashi, K. !$#journal J. Biochem. (1980) 88:9-16 !$#title Monkey pepsinogens and pepsins. IV. The amino acid sequence !1of the activation peptide segment of Japanese monkey !1pepsinogen. !$#cross-references MUID:81006790; PMID:6773933 !$#accession A91960 !'##molecule_type protein !'##residues 16-62 ##label KA2 REFERENCE A92579 !$#authors Kageyama, T.; Takahashi, K. !$#journal J. Biol. Chem. (1986) 261:4395-4405 !$#title The complete amino acid sequence of monkey pepsinogen A. !$#cross-references MUID:86168132; PMID:3514596 !$#accession A92579 !'##molecule_type protein !'##residues 41-261,'D',263-388 ##label KA3 COMMENT This is the major pepsin isozyme in juveniles and adults. COMMENT Activation is a one-step process. CLASSIFICATION #superfamily pepsin KEYWORDS aspartic proteinase; gastric juice; hydrolase; !1phosphoprotein; protein digestion; stomach FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-62 #domain activation peptide #status experimental !8#label APT\ !$63-388 #product pepsin A 1 #status experimental #label ENZ\ !$94,277 #active_site Asp #status predicted\ !$107-112,268-272, !$311-344 #disulfide_bonds #status experimental\ !$130 #binding_site phosphate (Ser) (covalent) #status !8experimental SUMMARY #length 388 #molecular-weight 41623 #checksum 6710 SEQUENCE /// ENTRY S19684 #type complete TITLE pepsin A (EC 3.4.23.1) 2/3 precursor - Japanese macaque ALTERNATE_NAMES pepsinogen A isozyme 2/3 ORGANISM #formal_name Macaca fuscata #common_name Japanese macaque DATE 22-Nov-1993 #sequence_revision 19-Oct-1995 #text_change 18-Jun-1999 ACCESSIONS S19684; S16064 REFERENCE S19681 !$#authors Kageyama, T.; Tanabe, K.; Koiwai, O. !$#journal Eur. J. Biochem. (1991) 202:205-215 !$#title Development-dependent expression of isozymogens of monkey !1pepsinogens and structural differences between them. !$#cross-references MUID:92037645; PMID:1935977 !$#accession S19684 !'##molecule_type mRNA !'##residues 1-388 ##label KAG !'##cross-references EMBL:X59755; NID:g38068; PIDN:CAA42427.1; !1PID:g38069 !'##note parts of sequence, including amino ends of pepsinogen and !1activation intermediates, confirmed by protein sequencing COMMENT It could not be determined if this sequence represents !1isozyme 2 or 3, which appear to be very similar. Isozyme 3 !1is the major pepsin found in newborns, whereas isozyme 2 is !1the major pepsin by 4 months of age. COMMENT Although two-step activation is observerd, activation is !1predominantly a one-step process. CLASSIFICATION #superfamily pepsin KEYWORDS aspartic proteinase; gastric juice; hydrolase; !1phosphoprotein; protein digestion; stomach FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-388 #product pepsinogen A 2/3 #status experimental #label !8PPT\ !$16-62 #domain activation peptide #status experimental !8#label APT\ !$63-388 #product pepsin A 2/3 #status experimental #label !8ENZ\ !$40-41 #cleavage_site Asp-Phe (pepsin) #status experimental\ !$62-63 #cleavage_site Leu-Ile (pepsin) #status experimental\ !$94,277 #active_site Asp #status predicted\ !$107-112,268-272, !$311-344 #disulfide_bonds #status predicted\ !$130 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 388 #molecular-weight 41703 #checksum 6474 SEQUENCE /// ENTRY S19682 #type complete TITLE pepsin A (EC 3.4.23.1) 4 precursor - Japanese macaque ALTERNATE_NAMES pepsinogen A isozyme 4 ORGANISM #formal_name Macaca fuscata #common_name Japanese macaque DATE 22-Nov-1993 #sequence_revision 19-Oct-1995 #text_change 18-Jun-1999 ACCESSIONS S19682; S16065 REFERENCE S19681 !$#authors Kageyama, T.; Tanabe, K.; Koiwai, O. !$#journal Eur. J. Biochem. (1991) 202:205-215 !$#title Development-dependent expression of isozymogens of monkey !1pepsinogens and structural differences between them. !$#cross-references MUID:92037645; PMID:1935977 !$#accession S19682 !'##molecule_type mRNA !'##residues 1-388 ##label KAG !'##cross-references EMBL:X59753; NID:g38070; PIDN:CAA42425.1; !1PID:g38071 !'##note parts of sequence, including amino ends of pepsinogen and !1activation intermediates, confirmed by protein sequencing COMMENT This is a minor component of pepsin at all post-partum !1stages. COMMENT Although two-step activation is observerd, activation is !1predominantly a one-step process. CLASSIFICATION #superfamily pepsin KEYWORDS aspartic proteinase; gastric juice; hydrolase; !1phosphoprotein; protein digestion; stomach FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-388 #product pepsinogen A 4 #status experimental #label !8PPT\ !$16-62 #domain activation peptide #status experimental !8#label APT\ !$63-388 #product pepsin A 4 #status experimental #label ENZ\ !$38-39 #cleavage_site Leu-Lys (pepsin) #status experimental\ !$62-63 #cleavage_site Leu-Ile (pepsin) #status experimental\ !$94,277 #active_site Asp #status predicted\ !$107-112,268-272, !$311-344 #disulfide_bonds #status predicted\ !$130 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 388 #molecular-weight 41955 #checksum 8474 SEQUENCE /// ENTRY PEPG #type complete TITLE pepsin A (EC 3.4.23.1) precursor - pig ALTERNATE_NAMES pepsinogen A ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 24-Apr-1984 #sequence_revision 22-Jul-1994 #text_change 18-Jun-1999 ACCESSIONS JT0307; A32455; B22434; A91410; A90185; A92039; A92179; !1PN0145; A00982 REFERENCE JT0307 !$#authors Tsukagoshi, N.; Ando, Y.; Tomita, Y.; Uchida, R.; Takemura, !1T.; Sasaki, T.; Yamagata, H.; Udaka, S.; Ichihara, Y.; !1Takahashi, K. !$#journal Gene (1988) 65:285-292 !$#title Nucleotide sequence and expression in Escherichia coli of !1cDNA of swine pepsinogen: involvement of the amino-terminal !1portion of the activation peptide segment in restoration of !1the functional protein. !$#cross-references MUID:88313677; PMID:3044927 !$#accession JT0307 !'##molecule_type mRNA !'##residues 1-386 ##label TSU !'##cross-references GB:M20920; NID:g164601; PIDN:AAA31095.1; !1PID:g164602 REFERENCE A32455 !$#authors Lin, X.; Wong, R.N.S.; Tang, J. !$#journal J. Biol. Chem. (1989) 264:4482-4489 !$#title Synthesis, purification, and active site mutagenesis of !1recombinant porcine pepsinogen. !$#cross-references MUID:89174702; PMID:2494172 !$#accession A32455 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-288,290-301,'Y',303-386 ##label LIN !'##cross-references GB:J04601; NID:g164603; PIDN:AAA31096.1; !1PID:g164604 !'##note replacement of 91-Asp by Ala prevents autocatalytic activation REFERENCE A22434 !$#authors Ichihara, Y.; Sogawa, K.; Takahashi, K. !$#journal J. Biochem. (1985) 98:483-492 !$#title Isolation of human, swine, and rat prepepsinogens and calf !1preprochymosin, and determination of the primary structures !1of their NH2-terminal signal sequences. !$#cross-references MUID:86059312; PMID:2415509 !$#accession B22434 !'##molecule_type protein !'##residues 1-19,'XX',22,'X',24-26 ##label ICH REFERENCE A91410 !$#authors Moravek, L.; Kostka, V. !$#journal FEBS Lett. (1974) 43:207-211 !$#title Complete amino acid sequence of hog pepsin. !$#cross-references MUID:74299591; PMID:4604255 !$#accession A91410 !'##molecule_type protein !'##residues 60-288,290-386 ##label MOR REFERENCE A90185 !$#authors Stepanov, V.M.; Baratova, L.A.; Pugacheva, I.B.; Belyanova, !1L.P.; Revina, L.P.; Timokhina, E.A. !$#journal Biochem. Biophys. Res. Commun. (1973) 54:1164-1170 !$#title N-terminal sequence of swine pepsinogen and pepsin. The site !1of pepsinogen activation. !$#cross-references MUID:74031413; PMID:4584879 !$#accession A90185 !'##molecule_type protein !'##residues 16-33,'D',35-118,'SD',121-127,'E',129-134 ##label STE !'##note the authors point out the similarity of residues 31-43 and !159-71 REFERENCE A92039 !$#authors Ong, E.B.; Perlmann, G.E. !$#journal J. Biol. Chem. (1968) 243:6104-6109 !$#title The amino-terminal sequence of porcine pepsinogen. !$#cross-references MUID:69054241; PMID:4881358 !$#accession A92039 !'##molecule_type protein !'##residues 16-33,'D',35-54,'AE' ##label ONG REFERENCE A92179 !$#authors Sepulveda, P.; Marciniszyn Jr., J.; Liu, D.; Tang, J. !$#journal J. Biol. Chem. (1975) 250:5082-5088 !$#title Primary structure of porcine pepsin. III. Amino acid !1sequence of a cyanogen bromide fragment, CB2A, and the !1complete structure of porcine pepsin. !$#cross-references MUID:75211282; PMID:1097438 !$#contents active site !$#accession A92179 !'##molecule_type protein !'##residues 58-288,290-322,'D',324-349 ##label SEP !'##note this is the final paper in a series !'##note variants having 314-Gln or an Ile between residues 288 and 290 !1were also found REFERENCE PN0145 !$#authors Revina, L.P.; Vakhitova, E.A.; Pugacheva, I.B.; Lapuk, Y.I.; !1Stepanov, V.M. !$#journal Biokhimiia (1972) 37:1074-1080 !$#title Investigation of peptides produced from N-terminal fragment !1of pepsin by hydrolysis with thermolysin. !$#cross-references MUID:73048197; PMID:4564536 !$#accession PN0145 !'##molecule_type protein !'##residues 60-75;102-118,'SD',121-127,'E',129-134 ##label REV !'##note article in Russian with English abstract REFERENCE A90016 !$#authors Andreeva, N.S.; Gustchina, A.E.; Fedorov, A.A.; Shutzkever, !1N.E.; Volnova, T.V. !$#journal Adv. Exp. Med. Biol. (1977) 95:23-31 !$#title X-ray crystallographic studies of pepsin. !$#cross-references MUID:78077917; PMID:339692 !$#contents annotation; X-ray crystallography, 3.0-2.7 angstroms COMMENT Minor amounts of the active enzyme occur with Ala-58 at the !1amino end. CLASSIFICATION #superfamily pepsin KEYWORDS aspartic proteinase; gastric juice; hydrolase; !1phosphoprotein; protein digestion; stomach; zymogen FEATURE !$1-15 #domain signal sequence #status experimental #label !8SIG\ !$16-59 #domain activation peptide #status experimental !8#label APD\ !$60-386 #product pepsin A #status experimental #label MAT\ !$59-60 #cleavage_site Leu-Ile (pepsinogen) #status !8experimental\ !$91,274 #active_site Asp #status experimental\ !$104-109,265-269, !$309-342 #disulfide_bonds #status experimental\ !$127 #binding_site phosphate (Ser) (covalent) #status !8experimental SUMMARY #length 386 #molecular-weight 41375 #checksum 7333 SEQUENCE /// ENTRY PEBO #type fragment TITLE pepsin A (EC 3.4.23.1) precursor - bovine (fragment) ALTERNATE_NAMES pepsinogen A ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 23-Oct-1981 #sequence_revision 23-Oct-1981 #text_change 21-Jan-1997 ACCESSIONS A92157; A91424; A00983 REFERENCE A92157 !$#authors Harboe, M.; Andersen, P.M.; Foltmann, B.; Kay, J.; Kassell, !1B. !$#journal J. Biol. Chem. (1974) 249:4487-4494 !$#title The activation of bovine pepsinogen. Sequence of the !1peptides released, identification of a pepsin inhibitor. !$#cross-references MUID:74287628; PMID:4603017 !$#accession A92157 !'##molecule_type protein !'##residues 1-47 ##label HAR !'##note the enzyme is inhibited by the peptide comprising residues 1-17 REFERENCE A91424 !$#authors Harboe, M.K.; Foltmann, B. !$#journal FEBS Lett. (1975) 60:133-136 !$#title Bovine pepsin: the sequence of the first 65 amino acid !1residues (completing the sequence of the first 110 residues !1of bovine pepsinogen). !$#cross-references MUID:76210768; PMID:776669 !$#accession A91424 !'##molecule_type protein !'##residues 41-110 ##label HA2 CLASSIFICATION #superfamily pepsin KEYWORDS aspartic proteinase; gastric juice; hydrolase; protein !1digestion; stomach FEATURE !$1-45 #domain activation peptide #status experimental !8#label APT\ !$46-110 #product pepsin A (fragment) #status predicted #label !8MAT\ !$77 #active_site Asp #status experimental\ !$90-95 #disulfide_bonds #status experimental SUMMARY #length 110 #checksum 9070 SEQUENCE /// ENTRY PECH #type complete TITLE pepsin A (EC 3.4.23.1) precursor - chicken ALTERNATE_NAMES pepsinogen A ORGANISM #formal_name Gallus gallus #common_name chicken DATE 18-Apr-1984 #sequence_revision 01-Dec-2000 #text_change 01-Dec-2000 ACCESSIONS JE0370; A00984 REFERENCE JE0370 !$#authors Sakamoto, N.; Saiga, H.; Yasugi, S. !$#journal Biochem. Biophys. Res. Commun. (1998) 250:420-424 !$#title Analysis of temporal expression pattern and cis-regulatory !1sequences of chicken pepsinogen A and C. !$#cross-references MUID:98440813; PMID:9753645 !$#accession JE0370 !'##status preliminary !'##molecule_type mRNA !'##residues 1-382 ##label SAK !'##cross-references GB:AB025281; NID:g4589837; PIDN:BAA76891.1; !1PID:g4589838 REFERENCE A00984 !$#authors Baudys, M.; Kostka, V. !$#journal Eur. J. Biochem. (1983) 136:89-99 !$#title Covalent structure of chicken pepsinogen. !$#cross-references MUID:84004412; PMID:6617663 !$#accession A00984 !'##molecule_type protein !'##residues 16-87,'S',89-382 ##label BAU CLASSIFICATION #superfamily pepsin KEYWORDS aspartic proteinase; gastric juice; glycoprotein; hydrolase; !1protein digestion; stomach FEATURE !$16-57 #domain activation peptide #status experimental !8#label APT\ !$58-382 #product pepsin A #status predicted #label MAT\ !$92,275 #active_site Asp #status predicted\ !$105-110,266-270, !$305-338 #disulfide_bonds #status experimental\ !$128 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 382 #molecular-weight 42056 #checksum 4584 SEQUENCE /// ENTRY CMBO #type complete TITLE chymosin (EC 3.4.23.4) precursor - bovine ALTERNATE_NAMES preprochymosin; preprorennin; rennin B CONTAINS chymosin; prochymosin ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 24-Apr-1984 #sequence_revision 09-Sep-1994 #text_change 18-Jun-1999 ACCESSIONS A25631; A93419; A44608; A92259; A44620; A91935; A91495; !1D22434; A00985 REFERENCE A25631 !$#authors Hidaka, M.; Sasaki, K.; Uozumi, T.; Beppu, T. !$#journal Gene (1986) 43:197-203 !$#title Cloning and structural analysis of the calf prochymosin !1gene. !$#cross-references MUID:86301873; PMID:3091454 !$#accession A25631 !'##molecule_type DNA !'##residues 1-16,'T',18-381 ##label HID REFERENCE A93419 !$#authors Harris, T.J.R.; Lowe, P.A.; Lyons, A.; Thomas, P.G.; Eaton, !1M.A.W.; Millican, T.A.; Patel, T.P.; Bose, C.C.; Carey, !1N.H.; Doel, M.T. !$#journal Nucleic Acids Res. (1982) 10:2177-2187 !$#title Molecular cloning and nucleotide sequence of cDNA coding for !1calf preprochymosin. !$#cross-references MUID:82221400; PMID:6283469 !$#contents prochymosin B !$#accession A93419 !'##molecule_type mRNA !'##residues 1-229,'N',231-381 ##label HAR !'##cross-references GB:J00003; NID:g162859; PIDN:AAA30448.1; !1PID:g162860 REFERENCE A44608 !$#authors Nishimori, K.; Kawaguchi, Y.; Hidaka, M.; Uozumi, T.; Beppu, !1T. !$#journal J. Biochem. (1982) 91:1085-1088 !$#title Nucleotide sequence of calf prorennin cDNA cloned in !1Escherichia coli. !$#cross-references MUID:82189915; PMID:6804449 !$#accession A44608 !'##molecule_type mRNA !'##residues 7-14,'X',16-42,'L',44-87,'N',89-301,'D',303-324,'I', !1326-334,'G',336-342,'T',344-379,'T',381 ##label NIS !'##cross-references GB:J00004 !'##note authors translated the codon TTG for residue 43 as Phe, ACC for !1residue 82 as Tyr, AAC for residue 88 as Thr, ATC for !1residue 325 as Met, ACT for residue 343 as Ser, and ACC for !1residue 380 as Ala REFERENCE A92259 !$#authors Foltmann, B.; Pedersen, V.B.; Kauffman, D.; Wybrandt, G. !$#journal J. Biol. Chem. (1979) 254:8447-8456 !$#title The primary structure of calf chymosin. !$#cross-references MUID:79239460; PMID:381305 !$#contents chymosin B; disulfide bonds !$#accession A92259 !'##molecule_type protein !'##residues 59-217,'D',219-381 ##label FOL REFERENCE A44620 !$#authors Foltmann, B.; Pedersen, V.B.; Jacobsen, H.; Kauffman, D.; !1Wybrandt, G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1977) 74:2321-2324 !$#title The complete amino acid sequence of prochymosin. !$#cross-references MUID:77234648; PMID:329280 !$#accession A44620 !'##molecule_type protein !'##residues 17-173,'T',175-217,'D',219-251,'Y',253-381 ##label FO2 REFERENCE A91935 !$#authors Chang, W.J.; Takahashi, K. !$#journal J. Biochem. (1974) 76:467-474 !$#title The structure and function of acid proteases. III. Isolation !1and characterization of the active-site peptides from bovine !1rennin. !$#cross-references MUID:75060332; PMID:4612029 !$#contents active site peptides !$#accession A91935 !'##molecule_type protein !'##residues 92-96;274-278,280 ##label CHA !'##note the authors did not find Lys-279 in their active site peptide REFERENCE A91495 !$#authors Moir, D.; Mao, J.; Schumm, J.W.; Vovis, G.F.; Alford, B.L.; !1Taunton-Rigby, A. !$#journal Gene (1982) 19:127-138 !$#title Molecular cloning and characterization of double-stranded !1cDNA coding for bovine chymosin. !$#cross-references MUID:83054629; PMID:6183168 !$#contents prochymosin A !$#accession A91495 !'##molecule_type mRNA !'##residues 1-301,'D',303-381 ##label MOI REFERENCE A22434 !$#authors Ichihara, Y.; Sogawa, K.; Takahashi, K. !$#journal J. Biochem. (1985) 98:483-492 !$#title Isolation of human, swine, and rat prepepsinogens and calf !1preprochymosin, and determination of the primary structures !1of their NH2-terminal signal sequences. !$#cross-references MUID:86059312; PMID:2415509 !$#accession D22434 !'##molecule_type protein !'##residues 1-18,'XX',21,'XX',24,'X',26,'X',28,'X',30 ##label ICH COMMENT The sequence of variant B is shown. COMMENT Chymosin is synthesized in the mucosa of the abomasum !1(fourth stomach) of young (unweaned) ruminants. The enzyme !1hydrolyzes casein to paracasein. COMMENT Forms A and B are probably allelic variants. Chymosin B is !1the predominant form. GENETICS !$#introns 21/2; 71/3; 111/1; 150/3; 217/2; 255/2; 303/3; 336/3 CLASSIFICATION #superfamily pepsin KEYWORDS aspartic proteinase; gastric juice; hydrolase; protein !1digestion; stomach; zymogen FEATURE !$1-16 #domain signal sequence #status experimental #label !8SIG\ !$17-58 #domain activation peptide #status experimental !8#label APT\ !$59-381 #product chymosin #status experimental #label MPT\ !$92,274 #active_site Asp #status experimental\ !$105-110,265-269, !$308-341 #disulfide_bonds #status experimental SUMMARY #length 381 #molecular-weight 42179 #checksum 5095 SEQUENCE /// ENTRY CMSHB #type complete TITLE chymosin (EC 3.4.23.4) B precursor - sheep ORGANISM #formal_name Ovis orientalis aries, Ovis ammon aries #common_name domestic sheep DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 18-Jun-1999 ACCESSIONS S10996 REFERENCE S10996 !$#authors Pungercar, J.; Strukelj, B.; Gubensek, F.; Turk, V.; Kregar, !1I. !$#journal Nucleic Acids Res. (1990) 18:4602 !$#title Complete primary structure of lamb preprochymosin deduced !1from cDNA. !$#cross-references MUID:90356410; PMID:2117748 !$#accession S10996 !'##molecule_type mRNA !'##residues 1-381 ##label PUN !'##cross-references EMBL:X53037; NID:g1373; PIDN:CAA37209.1; PID:g1374 CLASSIFICATION #superfamily pepsin KEYWORDS aspartic proteinase; gastric juice; hydrolase; protein !1digestion; stomach FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-58 #domain activation peptide #status predicted #label !8APT\ !$59-381 #product chymosin B #status predicted #label MAT\ !$92,274 #active_site Asp #status predicted\ !$105-110,265-269, !$308-341 #disulfide_bonds #status predicted SUMMARY #length 381 #molecular-weight 42074 #checksum 5159 SEQUENCE /// ENTRY PEMQCJ #type fragment TITLE gastricsin (EC 3.4.23.3) precursor - Japanese macaque (fragment) ALTERNATE_NAMES pepsin C ORGANISM #formal_name Macaca fuscata #common_name Japanese macaque DATE 13-Aug-1986 #sequence_revision 19-Oct-1995 #text_change 18-Jun-1999 ACCESSIONS S19683; A00986; A22402; S16066 REFERENCE S19681 !$#authors Kageyama, T.; Tanabe, K.; Koiwai, O. !$#journal Eur. J. Biochem. (1991) 202:205-215 !$#title Development-dependent expression of isozymogens of monkey !1pepsinogens and structural differences between them. !$#cross-references MUID:92037645; PMID:1935977 !$#accession S19683 !'##molecule_type mRNA !'##residues 1-377 ##label KAG !'##cross-references EMBL:X59754; NID:g38072; PIDN:CAA42426.1; !1PID:g38073 REFERENCE A00986 !$#authors Kageyama, T.; Takahashi, K. !$#journal J. Biol. Chem. (1986) 261:4406-4419 !$#title The complete amino acid sequence of monkey progastricsin. !$#cross-references MUID:86168133; PMID:3514597 !$#accession A00986 !'##molecule_type protein !'##residues 6-330,'V',332-349,'VY',350-377 ##label KA2 REFERENCE A22402 !$#authors Kageyama, T.; Takahashi, K. !$#journal J. Biochem. (1985) 97:1235-1246 !$#title Monkey pepsinogens and pepsins. VII. Analysis of the !1activation process and determination of the NH2-terminal !160-residue sequence of Japanese monkey progastricsin, and !1molecular evolution of pepsinogens. !$#cross-references MUID:85289106; PMID:3928607 !$#accession A22402 !'##molecule_type protein !'##residues 6-65 ##label KA3 COMMENT This enzyme has more restricted specificity than pepsin A. COMMENT The enzyme is activated in a two-step process that gives !1rise to two end products. The shorter, Ser-gastricsin, is !1the major product. CLASSIFICATION #superfamily pepsin KEYWORDS aspartic proteinase; gastric juice; hydrolase; protein !1digestion; stomach FEATURE !$1-5 #domain signal sequence (fragment) #status predicted !8#label SIG\ !$6-377 #product progastricsin #status experimental #label !8ZYM\ !$6-45 #domain activation peptide #status experimental !8#label APT\ !$46-377 #product Gly-gastricsin #status experimental #label !8MIN\ !$49-377 #product Ser-gastricsin #status experimental #label !8MAT\ !$31-32 #cleavage_site Phe-Leu (pepsin) #status experimental\ !$45-46 #cleavage_site Phe-Gly (pepsin) #status experimental\ !$48-49 #cleavage_site Leu-Ser (pepsin) #status experimental\ !$80,265 #active_site Asp #status predicted\ !$93-98,256-260, !$299-332 #disulfide_bonds #status experimental SUMMARY #length 377 #checksum 8114 SEQUENCE /// ENTRY A24608 #type complete TITLE gastricsin (EC 3.4.23.3) precursor - rat ALTERNATE_NAMES pepsinogen C CONTAINS pepsin A (EC 3.4.23.1) precursor ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1988 #sequence_revision 05-Aug-1994 #text_change 18-Jun-1999 ACCESSIONS A33510; A24608; C22434; A05145; A61298 REFERENCE A33510 !$#authors Ishihara, T.; Ichihara, Y.; Hayano, T.; Katsura, I.; Sogawa, !1K.; Fujii-Kuriyama, Y.; Takahashi, K. !$#journal J. Biol. Chem. (1989) 264:10193-10199 !$#title Primary structure and transcriptional regulation of rat !1pepsinogen C gene. !$#cross-references MUID:89255508; PMID:2722863 !$#accession A33510 !'##molecule_type DNA !'##residues 1-392 ##label ISH !'##cross-references GB:M25985 REFERENCE A24608 !$#authors Ichihara, Y.; Sogawa, K.; Morohashi, K.; Fujii-Kuriyama, Y.; !1Takahashi, K. !$#journal Eur. J. Biochem. (1986) 161:7-12 !$#title Nucleotide sequence of a nearly full-length cDNA coding for !1pepsinogen of rat gastric mucosa. !$#cross-references MUID:87054020; PMID:3780741 !$#accession A24608 !'##molecule_type mRNA !'##residues 1-392 ##label ICH !'##cross-references GB:X04644; NID:g56880; PIDN:CAA28305.1; PID:g56881 REFERENCE A22434 !$#authors Ichihara, Y.; Sogawa, K.; Takahashi, K. !$#journal J. Biochem. (1985) 98:483-492 !$#title Isolation of human, swine, and rat prepepsinogens and calf !1preprochymosin, and determination of the primary structures !1of their NH2-terminal signal sequences. !$#cross-references MUID:86059312; PMID:2415509 !$#accession C22434 !'##molecule_type protein !'##residues 1-19,'X',21-23,'X',25-29 ##label IC2 REFERENCE A05145 !$#authors Arai, K.M.; Muto, N.; Tani, S.; Akahane, K. !$#journal Biochim. Biophys. Acta (1984) 788:256-261 !$#title The N-terminal sequence of rat pepsinogen. !$#cross-references MUID:84257697; PMID:6743670 !$#accession A05145 !'##molecule_type protein !'##residues 17-30,'Q',32-102,'A',104-108,'L',110-112 ##label ARA !'##experimental_source Wistar strain REFERENCE A61298 !$#authors Ichihara, Y.; Sogawa, K.; Takahashi, K. !$#journal J. Biochem. (1982) 92:603-606 !$#title Rat gastric prepepsinogen: in vitro synthesis and partial !1amino-terminal signal sequence. !$#cross-references MUID:83030750; PMID:6182139 !$#accession A61298 !'##molecule_type protein !'##residues 1,'XX',4-6,'X',8-9,'X',11,'X',13-14,'XXX',18-19,'X',21,'X', !123,'XX',26,'X' ##label IC3 COMMENT This enzyme has more restricted specificity than pepsin A. !1It is the major form of pepsinogen in rat gastric mucosa. GENETICS !$#introns 20/2; 73/3; 113/1; 152/3; 219/2; 259/2; 309/3; 342/3 !$#note there are at least two very similar genes for gastricsin in !1rat CLASSIFICATION #superfamily pepsin KEYWORDS aspartic proteinase; gastric juice; hydrolase; protein !1digestion; stomach FEATURE !$1-16 #domain signal sequence #status experimental #label !8SIG\ !$17-392 #product pepsinogen #status experimental #label MAT\ !$17-62 #domain activation peptide #status experimental !8#label ACT\ !$94,280 #active_site Asp #status predicted\ !$107-112,270-275, !$314-347 #disulfide_bonds #status predicted SUMMARY #length 392 #molecular-weight 42833 #checksum 4014 SEQUENCE /// ENTRY A26681 #type complete TITLE rhizopuspepsin (EC 3.4.23.21) II precursor - Rhizopus chinensis ALTERNATE_NAMES microbial aspartic proteinase ORGANISM #formal_name Rhizopus chinensis DATE 19-Nov-1988 #sequence_revision 05-Aug-1994 #text_change 18-Aug-2000 ACCESSIONS A26681; A40425; A26682; B41415; A61330 REFERENCE A26681 !$#authors Delaney, R.; Wong, R.N.S.; Meng, G.Z.; Wu, N.H.; Tang, J. !$#journal J. Biol. Chem. (1987) 262:1461-1467 !$#title Amino acid sequence of rhizopuspepsin isozyme pI 5. !$#cross-references MUID:87109284; PMID:3027093 !$#accession A26681 !'##molecule_type mRNA !'##residues 42-393 ##label DEL !'##cross-references GB:J02651; NID:g169739; PIDN:AAA33879.1; !1PID:g169740 REFERENCE A40425 !$#authors Chen, Z.; Koelsch, G.; Han, H.; Wang, X.J.; Lin, X.; !1Hartsuck, J.A.; Tang, J. !$#journal J. Biol. Chem. (1991) 266:11718-11725 !$#title Recombinant rhizopuspepsinogen. Expression, purification, !1and activation properties of recombinant !1rhizopuspepsinogens. !$#cross-references MUID:91268039; PMID:2050673 !$#accession A40425 !'##molecule_type mRNA !'##residues 1-79 ##label CHE !'##cross-references GB:M63451 !'##note the nucleotide sequence of this mRNA started from the second !1nucleotide of the presumed start codon REFERENCE A26682 !$#authors Takahashi, K. !$#journal J. Biol. Chem. (1987) 262:1468-1478 !$#title The amino acid sequence of rhizopuspepsin, an aspartic !1proteinase from Rhizopus chinensis. !$#cross-references MUID:87109285; PMID:3100534 !$#accession A26682 !'##molecule_type protein !'##residues 69-393 ##label TAK !'##note this sequence showed two different residues at each of eight !1positions REFERENCE A41415 !$#authors Takahashi, K. !$#journal J. Biochem. (1988) 103:162-167 !$#title Determination of the amino acid sequences of the two major !1isozymes of rhizopuspepsin. !$#cross-references MUID:88198096; PMID:3283113 !$#accession B41415 !'##molecule_type protein !'##residues 69-393 ##label TA2 REFERENCE A61330 !$#authors Nakamura, S.; Takahashi, K. !$#journal J. Biochem. (1977) 81:805-807 !$#title Amino acid sequences around 1,2-epoxy-3- !1(p-nitrophenoxy)propane-reactive residues in Rhizopus !1chinensis acid protease: homology with pepsin and rennin. !$#cross-references MUID:77187769; PMID:16879 !$#accession A61330 !'##molecule_type protein !'##residues 103-108;286-291 ##label NAK !'##note these peptides were isolated after modification of the protein !1by reagents targeted to active site residues COMMENT This isozyme has an isoelectric point of 5.8. CLASSIFICATION #superfamily pepsin KEYWORDS aspartic proteinase; hydrolase; zymogen FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-68 #domain propeptide #status predicted #label PRO\ !$69-393 #product rhizopuspepsin II #status experimental !8#label MAT\ !$103,286 #active_site Asp #status experimental\ !$116-119,320-353 #disulfide_bonds #status experimental SUMMARY #length 393 #molecular-weight 41300 #checksum 355 SEQUENCE /// ENTRY KHHUD #type complete TITLE cathepsin D (EC 3.4.23.5) precursor [validated] - human ALTERNATE_NAMES preprocathepsin D ORGANISM #formal_name Homo sapiens #common_name man DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 15-Sep-2000 ACCESSIONS A25771; S30749; PC2066; I59236; I57716 REFERENCE A25771 !$#authors Faust, P.L.; Kornfeld, S.; Chirgwin, J.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:4910-4914 !$#title Cloning and sequence analysis of cDNA for human cathepsin D. !$#cross-references MUID:85270436; PMID:3927292 !$#accession A25771 !'##molecule_type mRNA !'##residues 1-412 ##label FAU !'##cross-references EMBL:M11233; NID:g181179; PIDN:AAB59529.1; !1PID:g181180 REFERENCE S30749 !$#authors Westley, B.R.; May, F.E.B. !$#journal Nucleic Acids Res. (1987) 15:3773-3786 !$#title Oestrogen regulates cathepsin D mRNA levels in oestrogen !1responsive human breast cancer cells. !$#cross-references MUID:87231068; PMID:3588310 !$#accession S30749 !'##molecule_type mRNA !'##residues 1-412 ##label WES !'##cross-references EMBL:X05344; NID:g29677; PIDN:CAA28955.1; !1PID:g29678 REFERENCE PC2066 !$#authors May, F.E.B.; Smith, D.J.; Westley, B.R. !$#journal Gene (1993) 134:277-282 !$#title The human cathepsin D-encoding gene is transcribed from an !1estrogen-regulated and a constitutive start point. !$#cross-references MUID:94085791; PMID:8262386 !$#accession PC2066 !'##molecule_type DNA !'##residues 1-23 ##label MAY !'##cross-references GB:L12980; NID:g291930; PIDN:AAA16314.1; !1PID:g455429 !'##experimental_source MCF-7 cell REFERENCE I59236 !$#authors Cavailles, V.; Augereau, P.; Rochefort, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:203-207 !$#title Cathepsin D gene is controlled by a mixed promoter, and !1estrogens stimulate only TATA-dependent transcription in !1breast cancer cells. !$#cross-references MUID:93126342; PMID:8419924 !$#accession I59236 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-22 ##label CAV1 !'##cross-references GB:S52557; NID:g263124; PIDN:AAD13868.1; !1PID:g4261568 REFERENCE I57716 !$#authors Augereau, P.; Miralles, F.; Cavailles, V.; Gaudelet, C.; !1Parker, M.; Rochefort, H. !$#journal Mol. Endocrinol. (1994) 8:693-703 !$#title Characterization of the proximal estrogen-responsive element !1of human cathepsin D gene. !$#cross-references MUID:95021301; PMID:7935485 !$#accession I57716 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-22 ##label CAV2 !'##cross-references GB:S74689; NID:g786350; PIDN:AAD14156.1; !1PID:g4261856 REFERENCE A51839 !$#authors Baldwin, E.T.; Bhat, T.N.; Gulnik, S.; Erickson, J.W. !$#submission submitted to the Brookhaven Protein Data Bank, April 1993 !$#cross-references PDB:1LYA !$#contents annotation; X-ray crystallography, 2.5 angstroms, residues !165-161;170-241 REFERENCE A51840 !$#authors Baldwin, E.T.; Bhat, T.N.; Gulnik, S.; Erickson, J.W. !$#submission submitted to the Brookhaven Protein Data Bank, April 1993 !$#cross-references PDB:1LYB !$#contents annotation; X-ray crystallography, 2.5 angstroms, with !1inhibitor residues 65-161;170-241 REFERENCE A48229 !$#authors Baldwin, E.T.; Bhat, T.N.; Gulnik, S.; Hosur, M.V.; Sowder !1II, R.C.; Cachau, R.E.; Collins, J.; Silva, A.M.; Erickson, !1J.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:6796-6800 !$#title Crystal structures of native and inhibited forms of human !1cathepsin D: implications for lysosomal targeting and drug !1design. !$#cross-references MUID:93342076; PMID:8393577 !$#contents annotation; X-ray crystallography, 2.5 angstroms COMMENT Cathepsin D is a ubiquitous lysosomal proteinase. COMMENT In addition to the propeptide, residues 163-168 and 411-412 !1are proteolytically removed. Residues 169 and 170 are also !1partially removed. COMMENT The carbohydrate bound to 134-Asn contains a !1mannose-6-phosphate that is bound near 267-Lys and the !1phosphotransferase recognition region. GENETICS !$#gene GDB:CTSD !'##cross-references GDB:120512; OMIM:116840 !$#map_position 11p15.5-11p15.5 FUNCTION !$#description limited specificity endopeptidase !$#pathway intracellular protein degradation CLASSIFICATION #superfamily pepsin KEYWORDS aspartic proteinase; glycoprotein; hydrolase; lysosome; !1protein degradation FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-64 #domain propeptide #status predicted #label PRO\ !$65-162,169-410 #product cathepsin D #status experimental #label MAT\ !$267,329-356 #region phosphotransferase recognition\ !$91-160,110-117, !$286-290,329-366 #disulfide_bonds #status experimental\ !$97,295 #active_site Asp #status experimental\ !$134,263 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 412 #molecular-weight 44552 #checksum 8846 SEQUENCE /// ENTRY KHPGD #type complete TITLE cathepsin D (EC 3.4.23.5) - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 18-Apr-1984 #sequence_revision 31-Dec-1991 #text_change 18-Mar-1997 ACCESSIONS A92425; A93990; B31918; A00987 REFERENCE A92425 !$#authors Takahashi, T.; Tang, J. !$#journal J. Biol. Chem. (1983) 258:6435-6443 !$#title Amino acid sequence of porcine spleen cathepsin D light !1chain. !$#cross-references MUID:83213348; PMID:6406481 !$#accession A92425 !'##molecule_type protein !'##residues 1-95,'S',97 ##label TAK !'##experimental_source spleen REFERENCE A93990 !$#authors Shewale, J.G.; Tang, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:3703-3707 !$#title Amino acid sequence of porcine spleen cathepsin D. !$#cross-references MUID:84222027; PMID:6587385 !$#accession A93990 !'##molecule_type protein !'##residues 103-344 ##label SHE !'##experimental_source spleen !'##note 233-Lys and 246-Gln were also found REFERENCE A92681 !$#authors Yonezawa, S.; Takahashi, T.; Wang, X.; Wong, R.N.S.; !1Hartsuck, J.A.; Tang, J. !$#journal J. Biol. Chem. (1988) 263:16504-16511 !$#title Structures at the proteolytic processing region of cathepsin !1D. !$#cross-references MUID:89034127; PMID:3182800 !$#accession B31918 !'##molecule_type mRNA !'##residues 74-146 ##label YON !'##note the sequence from Fig. 1 is inconsistent with that from Fig. S6 !1in having an additional Thr after 146-Val. An alignment !1shown in Fig. 1 has an additional Ser after 88-Ser FUNCTION !$#description limited specificity endopeptidase !$#pathway intracellular protein degradation CLASSIFICATION #superfamily pepsin KEYWORDS aspartic proteinase; glycoprotein; hydrolase; lysosome; !1protein degradation FEATURE !$1-97 #product cathepsin D light chain #status experimental !8#label CDL\ !$103-344 #product cathepsin D heavy chain #status experimental !8#label CDH\ !$33,229 #active_site Asp #status experimental\ !$46-53,220-224, !$263-300 #disulfide_bonds #status predicted\ !$70,197 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$287 #binding_site carbohydrate (Asn) (covalent) #status !8absent SUMMARY #length 344 #molecular-weight 37207 #checksum 1263 SEQUENCE /// ENTRY KHRTD #type complete TITLE cathepsin D (EC 3.4.23.5) precursor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 18-Jun-1999 ACCESSIONS S13111; C31918; JQ1177; PQ0222 REFERENCE S13111 !$#authors Birch, N.P.; Loh, Y.P. !$#journal Nucleic Acids Res. (1990) 18:6445-6446 !$#title Cloning, sequence and expression of rat cathepsin D. !$#cross-references MUID:91057150; PMID:2243802 !$#accession S13111 !'##molecule_type mRNA !'##residues 1-407 ##label BIR !'##cross-references EMBL:X54467; NID:g55881; PIDN:CAA38349.1; !1PID:g55882 REFERENCE A92681 !$#authors Yonezawa, S.; Takahashi, T.; Wang, X.; Wong, R.N.S.; !1Hartsuck, J.A.; Tang, J. !$#journal J. Biol. Chem. (1988) 263:16504-16511 !$#title Structures at the proteolytic processing region of cathepsin !1D. !$#cross-references MUID:89034127; PMID:3182800 !$#accession C31918 !'##molecule_type protein !'##residues 134-162,'T',164-170 ##label YON REFERENCE JQ1177 !$#authors Fujita, H.; Tanaka, Y.; Noguchi, Y.; Kono, A.; Himeno, M.; !1Kato, K. !$#journal Biochem. Biophys. Res. Commun. (1991) 179:190-196 !$#title Isolation and sequencing of a cDNA clone encoding rat liver !1lysosomal cathepsin D and the structure of three forms of !1mature enzymes. !$#cross-references MUID:91354249; PMID:1883350 !$#accession JQ1177 !'##molecule_type mRNA !'##residues 1-14,'A',16-204,'N',206-261,'N',263-407 ##label FUJ !$#accession PQ0222 !'##molecule_type protein !'##residues 65-74;118-127;165-174 ##label FU2 !'##experimental_source liver COMMENT Cathepsin D in rat liver lysosome occurs as a mixture of !1both a single chain form and two types of two chain forms. FUNCTION !$#description limited specificity endopeptidase !$#pathway intracellular protein degradation CLASSIFICATION #superfamily pepsin KEYWORDS aspartic proteinase; glycoprotein; hydrolase; lysosome; !1protein degradation FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-64 #domain propeptide #status predicted #label PRO\ !$65-407 #product cathepsin D, 43K single-chain form #status !8predicted #label MAT\ !$65-164 #product (or 65-165) cathepsin D 12K light chain !8#status predicted #label MA2\ !$65-117 #product cathepsin D 9K light chain #status predicted !8#label MA4\ !$118-407 #product cathepsin D 34K heavy chain #status !8predicted #label MA5\ !$165-407 #product (or 166-407) cathepsin D 30K heavy chain !8#status predicted #label MA3\ !$91-160,110-117, !$281-285,324-361 #disulfide_bonds #status predicted\ !$97,290 #active_site Asp #status predicted\ !$134,258 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 407 #molecular-weight 44680 #checksum 3203 SEQUENCE /// ENTRY KHMSD #type complete TITLE cathepsin D (EC 3.4.23.5) precursor - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 18-Jun-1999 ACCESSIONS I48278; S14704; S12587 REFERENCE I48278 !$#authors Hetman, M.; Perschl, A.; Saftig, P.; Von Figura, K.; Peters, !1C. !$#journal DNA Cell Biol. (1994) 13:419-427 !$#title Mouse cathepsin D gene: molecular organization, !1characterization of the promoter, and chromosomal !1localization. !$#cross-references MUID:94280622; PMID:8011168 !$#accession I48278 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-410 ##label RES !'##cross-references EMBL:X68378; NID:g50302; PIDN:CAA48453.1; !1PID:g817945 REFERENCE S14704 !$#authors Diedrich, J.F.; Staskus, K.A.; Retzel, E.F.; Haase, A.T. !$#journal Nucleic Acids Res. (1990) 18:7184 !$#title Nucleotide sequence of a cDNA encoding mouse cathepsin D. !$#cross-references MUID:91088345; PMID:2263503 !$#accession S14704 !'##molecule_type mRNA !'##residues 1-410 ##label DIE !'##cross-references EMBL:X53337; NID:g50300; PIDN:CAA37423.1; !1PID:g50301 REFERENCE S12587 !$#authors Grusby, M.J.; Mitchell, S.C.; Glimcher, L.H. !$#journal Nucleic Acids Res. (1990) 18:4008 !$#title Molecular cloning of mouse cathepsin D. !$#cross-references MUID:90326544; PMID:2374732 !$#accession S12587 !'##molecule_type mRNA !'##residues 1-410 ##label GRU !'##cross-references EMBL:X52886; NID:g50298; PIDN:CAA37067.1; !1PID:g50299 GENETICS !$#introns 23/2; 76/3; 118/1; 157/3; 233/2; 274/2; 322/3; 355/3 FUNCTION !$#description limited specificity endopeptidase !$#pathway intracellular protein degradation CLASSIFICATION #superfamily pepsin KEYWORDS aspartic proteinase; glycoprotein; hydrolase; lysosome; !1protein degradation FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-64 #domain propeptide #status predicted #label PRO\ !$65-410 #product cathepsin D, single-chain form #status !8predicted #label MAT\ !$91-160,110-117, !$284-288,327-364 #disulfide_bonds #status predicted\ !$97,293 #active_site Asp #status predicted\ !$134,261 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 410 #molecular-weight 44954 #checksum 6486 SEQUENCE /// ENTRY RERTK #type complete TITLE renin (EC 3.4.23.15) precursor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 18-Jun-1999 ACCESSIONS A29991; S00923; S02090; A32702; A60837 REFERENCE A29991 !$#authors Fukamizu, A.; Nishi, K.; Cho, T.; Saitoh, M.; Nakayama, K.; !1Ohkubo, H.; Nakanishi, S.; Murakami, K. !$#journal J. Mol. Biol. (1988) 201:443-450 !$#title Structure of the rat renin gene. !$#cross-references MUID:88332979; PMID:3047403 !$#accession A29991 !'##molecule_type DNA !'##residues 1-402 ##label FUK !'##cross-references GB:X07907 REFERENCE S00923 !$#authors Tada, M.; Fukamizu, A.; Seo, M.S.; Takahashi, S.; Murakami, !1K. !$#journal Nucleic Acids Res. (1988) 16:3576 !$#title Nucleotide sequence of rat renin cDNA. !$#cross-references MUID:88233945; PMID:3287330 !$#accession S00923 !'##molecule_type mRNA !'##residues 1-402 ##label TAD !'##cross-references EMBL:X07033 !'##note the authors translated the codon AAA for residue 98 as Leu REFERENCE S02090 !$#authors Murakami, K. !$#submission submitted to the EMBL Data Library, March 1988 !$#accession S02090 !'##molecule_type mRNA !'##residues 1-199,'V',201-270,'L',272-402 ##label MUR !'##cross-references EMBL:X07033; NID:g57045; PIDN:CAA30082.1; !1PID:g57046 REFERENCE A32702 !$#authors Burnham, C.E.; Hawelu-Johnson, C.L.; Frank, B.M.; Lynch, !1K.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:5605-5609 !$#title Molecular cloning of rat renin cDNA and its gene. !$#cross-references MUID:87289653; PMID:3039496 !$#accession A32702 !'##molecule_type mRNA !'##residues 1-402 ##label BUR !'##cross-references GB:J02941 REFERENCE A60837 !$#authors Makrides, S.C.; Mulinari, R.; Zannis, V.I.; Gavras, H. !$#journal Hypertension (1988) 12:405-410 !$#title Regulation of renin gene expression in hypertensive rats. !$#cross-references MUID:89007008; PMID:3049341 !$#accession A60837 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 308-402 ##label MAK REFERENCE A39772 !$#authors Kim, S.; Hosoi, M.; Kikuchi, N.; Yamamoto, K. !$#journal J. Biol. Chem. (1991) 266:7044-7050 !$#title Amino-terminal amino acid sequence and heterogeneity in !1glycosylation of rat renal renin. !$#cross-references MUID:91201358; PMID:2016314 !$#contents annotation; processing sites GENETICS !$#introns 31/2; 81/3; 123/1; 162/3; 228/2; 268/2; 316/3; 349/3 CLASSIFICATION #superfamily pepsin KEYWORDS aspartic proteinase; blood pressure control; glycoprotein; !1hydrolase; kidney; plasma FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-71 #domain propeptide #status predicted #label PRO\ !$72-352 #product renin heavy chain #status experimental !8#label MATH\ !$355-402 #product renin light chain #status experimental !8#label MATL\ !$69,139,320 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$102,287 #active_site Asp #status predicted\ !$115-122,278-282, !$321-358 #disulfide_bonds #status predicted SUMMARY #length 402 #molecular-weight 44275 #checksum 4370 SEQUENCE /// ENTRY REMSS #type complete TITLE renin (EC 3.4.23.15) precursor, submandibular - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 15-Oct-1982 #sequence_revision 17-Dec-1982 #text_change 18-Jun-1999 ACCESSIONS A93923; A93285; B93285; B22058; A00988 REFERENCE A93923 !$#authors Misono, K.S.; Chang, J.J.; Inagami, T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:4858-4862 !$#title Amino acid sequence of mouse submaxillary gland renin. !$#cross-references MUID:83014991; PMID:6812055 !$#accession A93923 !'##molecule_type protein !'##residues 64-351;354-401 ##label MIS REFERENCE A93285 !$#authors Panthier, J.J.; Foote, S.; Chambraud, B.; Strosberg, A.D.; !1Corvol, P.; Rougeon, F. !$#journal Nature (1982) 298:90-92 !$#title Complete amino acid sequence and maturation of the mouse !1submaxillary gland renin precursor. !$#cross-references MUID:82220074; PMID:6283373 !$#accession A93285 !'##molecule_type mRNA !'##residues 1-98,'M',100-194,'LSRS',199-394,'V',396-401 ##label PA1 !'##cross-references GB:J00621; GB:V00845; NID:g200701; PIDN:AAA40050.1; !1PID:g200702 !'##note the authors translated codon ATG for residue 99 as Ile !$#accession B93285 !'##molecule_type protein !'##residues 64-84;354-374 ##label PA2 REFERENCE A92439 !$#authors Poe, M.; Liesch, J.M. !$#journal J. Biol. Chem. (1983) 258:9856-9860 !$#title Mouse submaxillary gland renin contains a noncovalently !1attached fatty acid. !$#cross-references MUID:83290909; PMID:6350284 !$#contents annotation; fatty acid binding REFERENCE A22058 !$#authors Panthier, J.J.; Dreyfus, M.; Roux, D.T.L.; Rougeon, F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:5489-5493 !$#title Mouse kidney and submaxillary gland renin genes differ in !1their 5' putative regulatory sequences. !$#cross-references MUID:84298161; PMID:6089205 !$#accession B22058 !'##molecule_type DNA !'##residues 1-29 ##label PAN COMMENT The enzyme contains a noncovalently attached fatty acid. COMMENT Submandibular renin has catalytic and antigenic activities !1similar to renal renin. COMMENT This renin is synthesized in the submandibular gland of !1males only. GENETICS !$#gene REN2 CLASSIFICATION #superfamily pepsin KEYWORDS aspartic proteinase; hydrolase; salivary gland; !1submandibular gland FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-63 #domain activation peptide #status predicted #label !8ACP\ !$64-351 #product renin, submandibular, heavy chain #status !8experimental #label RSH\ !$354-401 #product renin, submandibular, light chain #status !8experimental #label RSL\ !$101,286 #active_site Asp #status experimental\ !$114-121,277-281, !$320-357 #disulfide_bonds #status predicted SUMMARY #length 401 #molecular-weight 44282 #checksum 5039 SEQUENCE /// ENTRY REMSK #type complete TITLE renin (EC 3.4.23.15) precursor, renal - mouse ALTERNATE_NAMES angiotensin-forming enzyme; angiotensinogenase; renin 1 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 18-Jun-1999 ACCESSIONS A00989; S07636; A22766; A22058; I57576; A05137; JH0083 REFERENCE A00989 !$#authors Holm, I.; Ollo, R.; Panthier, J.J.; Rougeon, F. !$#journal EMBO J. (1984) 3:557-562 !$#title Evolution of aspartyl proteases by gene duplication: the !1mouse renin gene is organized in two homologous clusters of !1four exons. !$#cross-references MUID:84182525; PMID:6370686 !$#accession A00989 !'##molecule_type DNA !'##residues 1-402 ##label HOL !'##cross-references EMBL:X00850 REFERENCE S07636 !$#authors Kim, W.S.; Murakami, K.; Nakayama, K. !$#journal Nucleic Acids Res. (1989) 17:9480 !$#title Nucleotide sequence of a cDNA coding for mouse Ren1 !1preprorenin. !$#cross-references MUID:90067953; PMID:2685761 !$#accession S07636 !'##molecule_type mRNA !'##residues 1-402 ##label KIM !'##cross-references EMBL:X16642; NID:g53930; PIDN:CAA34636.1; !1PID:g53931 REFERENCE A90968 !$#authors Mullins, J.J.; Burt, D.W.; Windass, J.D.; McTurk, P.; !1George, H.; Brammar, W.J. !$#journal EMBO J. (1982) 1:1461-1466 !$#title Molecular cloning of two distinct renin genes from the DBA/2 !1mouse. !$#cross-references MUID:84207899; PMID:6327270 !$#accession A22766 !'##molecule_type mRNA !'##residues 269-314,'D',316 ##label MUL REFERENCE A22058 !$#authors Panthier, J.J.; Dreyfus, M.; Roux, D.T.L.; Rougeon, F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:5489-5493 !$#title Mouse kidney and submaxillary gland renin genes differ in !1their 5' putative regulatory sequences. !$#cross-references MUID:84298161; PMID:6089205 !$#accession A22058 !'##molecule_type DNA !'##residues 1-30 ##label PAN REFERENCE I57576 !$#authors Field, L.J.; Philbrick, W.M.; Howles, P.N.; Dickinson, D.P.; !1McGowan, R.A.; Gross, K.W. !$#journal Mol. Cell. Biol. (1984) 4:2321-2331 !$#title Expression of tissue-specific Ren-1 and Ren-2 genes of mice: !1Comparative analysis of 5'-proximal flanking regions. !$#cross-references MUID:85085936; PMID:6392850 !$#accession I57576 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-31 ##label RES !'##cross-references GB:K02800; NID:g200689; PIDN:AAA40044.1; !1PID:g200690 COMMENT The only known function of renal renin is to release !1angiotensin I from angiotensinogen in the plasma, initiating !1a cascade of reactions that produces an elevation of blood !1pressure and increased sodium retention by the kidney. COMMENT Renal renin is synthesized by the juxtaglomerular cells of !1the kidney in response to decreased blood pressure and !1sodium concentration. GENETICS !$#gene Ren-1 !$#introns 31/2; 81/3; 123/1; 162/3; 228/2; 268/2; 316/3; 349/3 CLASSIFICATION #superfamily pepsin KEYWORDS aspartic proteinase; blood pressure control; glycoprotein; !1hydrolase; kidney; plasma FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-64 #domain propeptide #status predicted #label PRO\ !$65-402 #product renin #status predicted #label MAT\ !$69,139,320 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$102,287 #active_site Asp #status predicted SUMMARY #length 402 #molecular-weight 44342 #checksum 4638 SEQUENCE /// ENTRY REHUK #type complete TITLE renin (EC 3.4.23.15) precursor [validated] - human ALTERNATE_NAMES angiotensinogenase ORGANISM #formal_name Homo sapiens #common_name man DATE 27-Nov-1985 #sequence_revision 30-Jun-1993 #text_change 08-Dec-2000 ACCESSIONS A21454; A21190; A21673; A00990; A26531; I52884; I55306; !1I53999; A35688; A36504; A27367; A39906 REFERENCE A21454 !$#authors Hardman, J.A.; Hort, Y.J.; Catanzaro, D.F.; Tellam, J.T.; !1Baxter, J.D.; Morris, B.J.; Shine, J. !$#journal DNA (1984) 3:457-468 !$#title Primary structure of the human renin gene. !$#cross-references MUID:85076176; PMID:6391881 !$#accession A21454 !'##molecule_type DNA !'##residues 1-406 ##label HAR !'##cross-references EMBL:X01732 REFERENCE A21190 !$#authors Imai, T.; Miyazaki, H.; Hirose, S.; Hori, H.; Hayashi, T.; !1Kageyama, R.; Ohkubo, H.; Nakanishi, S.; Murakami, K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:7405-7409 !$#title Cloning and sequence analysis of cDNA for human renin !1precursor. !$#cross-references MUID:84170236; PMID:6324167 !$#accession A21190 !'##molecule_type mRNA !'##residues 1-406 ##label IMA !'##cross-references GB:L00073; EMBL:K01169; NID:g190992; !1PIDN:AAA60363.1; PID:g190994 REFERENCE A21673 !$#authors Hobart, P.M.; Fogliano, M.; O'Connor, B.A.; Schaefer, I.M.; !1Chirgwin, J.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:5026-5030 !$#title Human renin gene: structure and sequence analysis. !$#cross-references MUID:84298075; PMID:6089171 !$#accession A21673 !'##molecule_type DNA !'##residues 1-230,234-403 ##label HOB !'##cross-references EMBL:K02225 !'##experimental_source submandibular gland REFERENCE A00990 !$#authors Soubrier, F.; Panthier, J.J.; Corvol, P.; Rougeon, F. !$#journal Nucleic Acids Res. (1983) 11:7181-7190 !$#title Molecular cloning and nucleotide sequence of a human renin !1cDNA fragment. !$#cross-references MUID:84041513; PMID:6138751 !$#accession A00990 !'##molecule_type mRNA !'##residues 108-350,'I',352-406 ##label SOU !'##cross-references EMBL:X00063 REFERENCE A26531 !$#authors Fukamizu, A.; Nishi, K.; Nishimatsu, S.; Miyazaki, H.; !1Hirose, S.; Murakami, K. !$#journal Gene (1986) 49:139-145 !$#title Human renin gene of renin-secreting tumor. !$#cross-references MUID:87191993; PMID:3032746 !$#accession A26531 !'##molecule_type DNA !'##residues 1-33 ##label FUK !'##cross-references GB:M15410; NID:g337341; PIDN:AAA60263.1; !1PID:g337342 !'##experimental_source JGC tumor genomic library REFERENCE I52884 !$#authors Morris, B.J. !$#journal Clin. Sci. (1986) 71:345-355 !$#title New possibilities for intracellular renin and inactive renin !1now that the structure of the human renin gene has been !1elucidated. !$#cross-references MUID:87003365; PMID:3530608 !$#accession I52884 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-54,'S',56-188,'Q',190-230,234-303,'C',305-406 ##label MOR !'##cross-references GB:M26901; NID:g337345; PIDN:AAA60364.1; !1PID:g337347 REFERENCE I55306 !$#authors Burt, D.W.; Nakamura, N.; Kelley, P.; Dzau, V.J. !$#journal J. Biol. Chem. (1989) 264:7357-7362 !$#title Identification of negative and positive regulatory elements !1in the human renin gene. !$#cross-references MUID:89214174; PMID:2540188 !$#accession I55306 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-33 ##label BUR !'##cross-references GB:M26440; NID:g341497; PIDN:AAA60365.1; !1PID:g620039 REFERENCE I53999 !$#authors Soubrier, F.; Panthier, J.J.; Houot, A.M.; Rougeon, F.; !1Corvol, P. !$#journal Gene (1986) 41:85-92 !$#title Segmental homology between the promoter region of the human !1renin gene and the mouse ren1 and ren2 promoter regions. !$#cross-references MUID:86193583; PMID:3516796 !$#accession I53999 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-33 ##label SO2 !'##cross-references GB:M13253; NID:g190995; PIDN:AAA60262.1; !1PID:g190996 REFERENCE A35688 !$#authors Vlahos, C.J.; Walls, J.D.; Berg, D.T.; Grinnell, B.W. !$#journal Biochem. Biophys. Res. Commun. (1990) 171:375-383 !$#title The purification and characterization of recombinant human !1renin expressed in the human kidney cell line 293. !$#cross-references MUID:90365733; PMID:2203348 !$#accession A35688 !'##molecule_type protein !'##residues 67-84;120-137 ##label VLA REFERENCE A36504 !$#authors Higashimori, K.; Mizuno, K.; Nakajo, S.; Boehm, F.H.; !1Marcotte, P.A.; Egan, D.A.; Holleman, W.H.; Heusser, C.; !1Poisner, A.M.; Inagami, T. !$#journal J. Biol. Chem. (1989) 264:14662-14667 !$#title Pure human inactive renin. Evidence that native inactive !1renin is prorenin. !$#cross-references MUID:89359256; PMID:2670924 !$#accession A36504 !'##molecule_type protein !'##residues 24-35 ##label HIG !'##experimental_source chorion laeve REFERENCE A39906 !$#authors Pratt, R.E.; Carleton, J.E.; Richie, J.P.; Heusser, C.; !1Dzau, V.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:7837-7840 !$#title Human renin biosynthesis and secretion in normal and !1ischemic kidneys. !$#cross-references MUID:88068494; PMID:3317396 !$#contents annotation; prorenin demonstrated by radiosequencing REFERENCE A27367 !$#authors Fritz, L.C.; Haidar, M.A.; Arfsten, A.E.; Schilling, J.W.; !1Carilli, C.; Shine, J.; Baxter, J.D.; Reudelhuber, T.L. !$#journal J. Biol. Chem. (1987) 262:12409-12412 !$#title Human renin is correctly processed and targeted to the !1regulated secretory pathway in mouse pituitary AtT-20 cells. !$#cross-references MUID:87308259; PMID:3305508 !$#contents annotation; radiosequencing of propeptide and mature protein !1in recombinant system COMMENT The only known function of renal renin is to release !1angiotensin I from angiotensinogen in the plasma, initiating !1a cascade of reactions that produce an elevation of blood !1pressure and increased sodium retention by the kidney. COMMENT Renal renin is synthesized by the juxtaglomerular cells of !1the kidney in response to decreased blood pressure and !1sodium concentration. GENETICS !$#gene GDB:REN !'##cross-references GDB:120345; OMIM:179820 !$#map_position 1q32-1q32 !$#introns 33/2; 83/3; 125/1; 164/3; 230/2; 233/2; 273/2; 320/3; 353/3 CLASSIFICATION #superfamily pepsin KEYWORDS aspartic proteinase; blood pressure control; glycoprotein; !1hydrolase; kidney; plasma FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-406 #product prorenin #status experimental #label PMAT\ !$24-66 #domain propeptide #status experimental #label PRO\ !$67-406 #product renin #status experimental #label MAT\ !$71 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$104,292 #active_site Asp #status predicted\ !$117-124 #disulfide_bonds #status experimental\ !$141 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$283-287,325-362 #disulfide_bonds #status predicted SUMMARY #length 406 #molecular-weight 45057 #checksum 3096 SEQUENCE /// ENTRY PEPLBJ #type complete TITLE penicillopepsin (EC 3.4.23.20) - Penicillium janthinellum ORGANISM #formal_name Penicillium janthinellum DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 12-Jun-1998 ACCESSIONS A00991; A38008 REFERENCE A00991 !$#authors James, M.N.G.; Sielecki, A.R. !$#journal J. Mol. Biol. (1983) 163:299-361 !$#title Structure and refinement of penicillopepsin at 1.8 angstrom !1resolution. !$#cross-references MUID:83189085; PMID:6341600 !$#accession A00991 !'##molecule_type protein !'##residues 1-323 ##label JAM !'##note the sequence shown is derived from the best amino acid sequence !1data as modified by the X-ray data and was subsequently !1revised by a note added in proof (see reference A38008); see !1article for citations to earlier reports !'##note the crystal structure was determined to a resolution of 1.8 !1angstroms REFERENCE A38008 !$#authors Hofmann, T. !$#citation unpublished results, cited by James, M.N.G., and Sielecki, !1A.R., J. Mol. Biol. 163, 299-361, 1983 !$#accession A38008 !'##molecule_type protein !'##residues 1-323 ##label HOF REFERENCE A38009 !$#authors Sodek, J.; Hofmann, T. !$#journal Can. J. Biochem. (1970) 48:1014-1016 !$#title Amino acid sequence around the active site aspartic acid in !1penicillopepsin. !$#cross-references MUID:71018406; PMID:5475460 !$#contents annotation !$#note active site residues were determined CLASSIFICATION #superfamily pepsin KEYWORDS aspartic proteinase; hydrolase FEATURE !$33,213 #active_site Asp #status experimental\ !$249-283 #disulfide_bonds #status experimental SUMMARY #length 323 #molecular-weight 33460 #checksum 2208 SEQUENCE /// ENTRY CMUMF #type complete TITLE mucorpepsin (EC 3.4.23.23) precursor - Rhizomucor miehei ORGANISM #formal_name Rhizomucor miehei DATE 30-Nov-1980 #sequence_revision 03-Feb-1994 #text_change 18-Jun-1999 ACCESSIONS A29039; A26537; A00992 REFERENCE A29039 !$#authors Gray, G.L.; Hayenga, K.; Cullen, D.; Wilson, L.J.; Norton, !1S. !$#journal Gene (1986) 48:41-53 !$#title Primary structure of Mucor miehei aspartyl protease: !1evidence for a zymogen intermediate. !$#cross-references MUID:87163515; PMID:3549462 !$#accession A29039 !'##molecule_type DNA !'##residues 1-430 ##label GRA !'##cross-references GB:M15267; NID:g168364; PIDN:AAA33421.1; !1PID:g168365 REFERENCE A26537 !$#authors Boel, E.; Bech, A.M.; Randrup, K.; Draeger, B.; Fiil, N.P.; !1Foltmann, B. !$#journal Proteins (1986) 1:363-369 !$#title Primary structure of a precursor to the aspartic proteinase !1from Rhizomucor miehei shows that the enzyme is synthesized !1as a zymogen. !$#cross-references MUID:88217880; PMID:3329734 !$#accession A26537 !'##molecule_type mRNA !'##residues 1-430 ##label BOE !'##cross-references GB:M18411; NID:g168376; PIDN:AAA33423.1; !1PID:g168377 REFERENCE A00992 !$#authors Bech, A.M.; Foltmann, B. !$#journal Neth. Milk Dairy J. (1981) 35:275-280 !$#title Partial primary structure of Mucor miehei protease. !$#contents annotation; disulfide bonds; carbohydrate binding site; !1partial sequence !$#note 262-Ser was also found CLASSIFICATION #superfamily pepsin KEYWORDS aspartic proteinase; glycoprotein; hydrolase FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-69 #domain propeptide #status predicted #label PRO\ !$70-430 #product mucorpepsin #status experimental #label MAT\ !$107,306 #active_site Asp #status predicted\ !$120-126,341-385 #disulfide_bonds #status experimental\ !$148,257 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 430 #molecular-weight 46167 #checksum 5776 SEQUENCE /// ENTRY PEIKL #type complete TITLE polyporopepsin (EC 3.4.23.29) - Irpex lacteus ORGANISM #formal_name Irpex lacteus DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 31-Dec-1993 ACCESSIONS JU0057 REFERENCE JU0057 !$#authors Kobayashi, H.; Sekibata, S.; Shibuya, H.; Yoshida, S.; !1Kusakabe, I.; Murakami, K. !$#journal Agric. Biol. Chem. (1989) 53:1927-1933 !$#title Cloning and sequence analysis of cDNA for Irpex lacteus !1aspartic proteinase. !$#accession JU0057 !'##molecule_type mRNA !'##residues 1-340 ##label KOB !'##note the amino-terminal 24 residues were sequenced on the isolated !1proteinase CLASSIFICATION #superfamily pepsin KEYWORDS aspartic proteinase; glycoprotein; hydrolase FEATURE !$32,212 #active_site Asp #status predicted\ !$192,238 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 340 #molecular-weight 35050 #checksum 9667 SEQUENCE /// ENTRY A36866 #type complete TITLE microbial collagenase (EC 3.4.24.3) precursor - Clostridium perfringens ORGANISM #formal_name Clostridium perfringens DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A36866 REFERENCE A36866 !$#authors Matsushita, O.; Yoshihara, K.; Katayama, S.I.; Minami, J.; !1Okabe, A. !$#journal J. Bacteriol. (1994) 176:149-156 !$#title Purification and characterization of a Clostridium !1perfringens 120-kilodalton collagenase and nucleotide !1sequence of the corresponding gene. !$#cross-references MUID:94110220; PMID:8282691 !$#accession A36866 !'##status preliminary !'##molecule_type DNA !'##residues 1-1104 ##label MAT !'##cross-references GB:D13791; NID:g440850; PIDN:BAA02941.1; !1PID:g440851 GENETICS !$#gene colA CLASSIFICATION #superfamily microbial collagenase KEYWORDS hydrolase; metalloproteinase SUMMARY #length 1104 #molecular-weight 126105 #checksum 6362 SEQUENCE /// ENTRY KCHUI #type complete TITLE interstitial collagenase (EC 3.4.24.7) precursor [validated] - human ALTERNATE_NAMES fibroblast collagenase; matrix metalloproteinase 1 (MMP1); tissue collagenase; type I collagenase; vertebrate collagenase ORGANISM #formal_name Homo sapiens #common_name man DATE 13-Aug-1986 #sequence_revision 30-Sep-1992 #text_change 08-Dec-2000 ACCESSIONS A37308; S22766; I57620; A00996; D29157; A44518; S06132; !1B60964; S10595; S53438 REFERENCE A37308 !$#authors Templeton, N.S.; Brown, P.D.; Levy, A.T.; Margulies, I.M.K.; !1Liotta, L.A.; Stetler-Stevenson, W.G. !$#journal Cancer Res. (1990) 50:5431-5437 !$#title Cloning and characterization of human tumor cell !1interstitial collagenase. !$#cross-references MUID:90352587; PMID:2167156 !$#accession A37308 !'##molecule_type mRNA !'##residues 1-469 ##label TEM !'##cross-references GB:X54925; NID:g30125; PIDN:CAA38691.1; PID:g30126 REFERENCE S22766 !$#authors Brinckerhoff, C.E.; Ruby, P.L.; Austin, S.D.; Fini, M.E.; !1White, H.D. !$#journal J. Clin. Invest. (1987) 79:542-546 !$#title Molecular cloning of human synovial cell collagenase and !1selection of a single gene from genomic DNA. !$#cross-references MUID:87109799; PMID:3027129 !$#accession S22766 !'##molecule_type DNA !'##residues 1-63,65-70 ##label BRI !'##cross-references EMBL:M15996; NID:g180666; PIDN:AAA35700.1; !1PID:g180667 REFERENCE I57620 !$#authors Angel, P.; Baumann, I.; Stein, B.; Delius, H.; Rahmsdorf, !1H.J.; Herrlich, P. !$#journal Mol. Cell. Biol. (1987) 7:2256-2266 !$#title 12-O-tetradecanoyl-phorbol-13-acetate induction of the human !1collagenase gene is mediated by an inducible enhancer !1element located in the 5'-flanking region. !$#cross-references MUID:87257941; PMID:3037355 !$#accession I57620 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-35 ##label RES !'##cross-references GB:M16567; NID:g180668; PIDN:AAA52033.1; !1PID:g180669 REFERENCE A00996 !$#authors Goldberg, G.I.; Wilhelm, S.M.; Kronberger, A.; Bauer, E.A.; !1Grant, G.A.; Eisen, A.Z. !$#journal J. Biol. Chem. (1986) 261:6600-6605 !$#title Human fibroblast collagenase. Complete primary structure and !1homology to an oncogene transformation-induced rat protein. !$#cross-references MUID:86196089; PMID:3009463 !$#accession A00996 !'##molecule_type mRNA !'##residues 1-114,'R',116-409,'S',411-469 ##label GOL !'##cross-references GB:M13509; NID:g180664; PIDN:AAA35699.1; !1PID:g180665 !'##note part of this sequence was confirmed by protein sequencing of !1the proenzyme REFERENCE A90336 !$#authors Whitham, S.E.; Murphy, G.; Angel, P.; Rahmsdorf, H.J.; !1Smith, B.J.; Lyons, A.; Harris, T.J.R.; Reynolds, J.J.; !1Herrlich, P.; Docherty, A.J.P. !$#journal Biochem. J. (1986) 240:913-916 !$#title Comparison of human stromelysin and collagenase by cloning !1and sequence analysis. !$#cross-references MUID:87156645; PMID:3030290 !$#accession D29157 !'##molecule_type mRNA !'##residues 1-199,'H',201-207,'T',209-469 ##label WHI !'##cross-references EMBL:X05231; NID:g38266; PIDN:CAA28858.1; !1PID:g38267 !'##note parts of this sequence, including the amino end of the !1proenzyme and of the mature protein, were confirmed by !1protein sequencing REFERENCE A44518 !$#authors Birkedal-Hansen, B.; Moore, W.G.I.; Taylor, R.E.; Bhown, !1A.S.; Birkedal-Hansen, H. !$#journal Biochemistry (1988) 27:6751-6758 !$#title Monoclonal antibodies to human fibroblast procollagenase. !1Inhibition of enzymatic activity, affinity purification of !1the enzyme, and evidence for clustering of epitopes in the !1NH-2-terminal end of the activated enzyme. !$#cross-references MUID:89062403; PMID:2461732 !$#accession A44518 !'##molecule_type protein !'##residues 270-305 ##label BIR REFERENCE S06132 !$#authors Clark, I.M.; Cawston, T.E. !$#journal Biochem. J. (1989) 263:201-206 !$#title Fragments of human fibroblast collagenase. Purification and !1characterization. !$#cross-references MUID:90104231; PMID:2557822 !$#accession S06132 !'##status preliminary !'##molecule_type protein !'##residues 100-102,'P',104-107,'XX',110-112;270-277,'X',279-280,'X', !1282-287 ##label CLA REFERENCE A60964 !$#authors Lark, M.W.; Walakovits, L.A.; Shah, T.K.; Vanmiddlesworth, !1J.; Cameron, P.M.; Lin, T.Y. !$#journal Connect. Tissue Res. (1990) 25:49-65 !$#title Production and purification of prostromelysin and !1procollagenase from IL-1 beta-stimulated human gingival !1fibroblasts. !$#cross-references MUID:91059606; PMID:2173990 !$#accession B60964 !'##molecule_type protein !'##residues 24-35;100-108;270-272,'X',274,'X',276 ##label LAR REFERENCE S10595 !$#authors Suzuki, K.; Nagase, H.; Ito, A.; Enghild, J.J.; Salvesen, G. !$#journal Biol. Chem. Hoppe-Seyler (1990) 371(Suppl.):305-310 !$#title The role of matrix metalloproteinase 3 in the stepwise !1activation of human rheumatoid synovial procollagenase. !$#cross-references MUID:90380300; PMID:2169257 !$#accession S10595 !'##molecule_type protein !'##residues 20-102 ##label SUZ REFERENCE S53438 !$#authors Suzuki, K.; Lees, M.; Newlands, G.F.J.; Nagase, H.; Woolley, !1D.E. !$#journal Biochem. J. (1995) 305:301-306 !$#title Activation of precursors for matrix metalloproteinases 1 !1(interstitial collagenase) and 3 (stromelysin) by rat !1mast-cell proteinases I and II. !$#cross-references MUID:95126921; PMID:7826345 !$#accession S53438 !'##status preliminary !'##molecule_type protein !'##residues 20-108 ##label SU2 REFERENCE A44517 !$#authors Springman, E.B.; Angleton, E.L.; Birkedal-Hansen, H.; Van !1Wart, H.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:364-368 !$#title Multiple modes of activation of latent human fibroblast !1collagenase: evidence for the role of a Cys73 active-site !1zinc complex in latency and a "cysteine switch" mechanism !1for activation. !$#cross-references MUID:90115877; PMID:2153297 !$#contents annotation; disulfide bond; activation mechanism REFERENCE A43031 !$#authors Salowe, S.P.; Marcy, A.I.; Cuca, G.C.; Smith, C.K.; Kopka, !1I.E.; Hagmann, W.K.; Hermes, J.D. !$#journal Biochemistry (1992) 31:4535-4540 !$#title Characterization of zinc-binding sites in human !1stromelysin-1: stoichiometry of the catalytic domain and !1identification of a cysteine ligand in the proenzyme. !$#cross-references MUID:92256384; PMID:1581308 !$#contents annotation; zinc ligand in proenzyme !$#note Cys-92 binds zinc in the proenzyme. Both active and !1proenzyme forms of the catalytic domain appear to bind two !1zinc atoms per molecule COMMENT Procollagenase can be activated without removal of the !1activation peptide. Stromelysin 1 activates the proenzyme !1either slowly by itself or very rapidly after cleavage(s) !1within the activation peptide by other proteinases. COMMENT Procollagenase is found in glycosylated and unglycosylated !1forms, both of which can be activated. GENETICS !$#gene GDB:MMP1; CLG !'##cross-references GDB:119783; OMIM:120353 !$#map_position 11q22.2-11q22.3 FUNCTION !$#description hydrolyzes collagens, in particular types I, II, III, and X, !1serpins, and alpha-macroglobulins at Gly-Ile sites in !1collagenous helix domains CLASSIFICATION #superfamily interstitial collagenase; hemopexin repeat !1homology; matrix metalloproteinase homology KEYWORDS calcium; extracellular matrix; fibroblast; glycoprotein; !1hydrolase; metalloproteinase; zinc; zymogen FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-469 #product procollagenase #status experimental #label !8PRO\ !$20-99 #domain activation peptide #status experimental !8#label ACT\ !$60-261 #domain matrix metalloproteinase homology #label MMP\ !$90-97 #region autoinhibitory\ !$100-469 #product interstitial collagenase #status !8experimental #label MAT\ !$272-466 #domain hemopexin repeat homology #label PXN\ !$92,218,222,228 #binding_site zinc, catalytic (Cys, His, His, His) !8(inhibited) #status experimental\ !$120,143 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$218,222,228 #binding_site zinc, catalytic (His) (active) #status !8predicted\ !$219 #active_site Glu #status predicted\ !$269-270 #cleavage_site Pro-Ile (autolytic) #status !8experimental\ !$278-466 #disulfide_bonds #status experimental SUMMARY #length 469 #molecular-weight 54007 #checksum 5879 SEQUENCE /// ENTRY KCRBI #type complete TITLE interstitial collagenase (EC 3.4.24.7) precursor - rabbit ALTERNATE_NAMES fibroblast collagenase; matrix metalloproteinase 1 (MMP1); tissue collagenase; type I collagenase; vertebrate collagenase ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS A27500; B27500; I46694 REFERENCE A27500 !$#authors Fini, M.E.; Plucinska, I.M.; Mayer, A.S.; Gross, R.H.; !1Brinckerhoff, C.E. !$#journal Biochemistry (1987) 26:6156-6165 !$#title A gene for rabbit synovial cell collagenase: member of a !1family of metalloproteinases that degrade the connective !1tissue matrix. !$#cross-references MUID:88077876; PMID:2825772 !$#accession A27500 !'##molecule_type mRNA !'##residues 1-468 ##label FIN !'##cross-references GB:M19240 !$#accession B27500 !'##molecule_type DNA !'##residues 1-391;399-468 ##label FI2 !'##cross-references GB:M17820 !'##note the location of the intron between exons 7 and 8 is approximate REFERENCE I46694 !$#authors Fini, M.E.; Austin, S.D.; Holt, P.T.; Ruby, P.L.; Gross, !1R.H.; White, H.D.; Brinckerhoff, C.E. !$#journal Coll. Relat. Res. (1986) 6:239-248 !$#title Homology between exon-containing portions of rabbit genomic !1clones for synovial cell collagenase and human foreskin and !1synovial cell mRNAs. !$#cross-references MUID:87029174; PMID:3021384 !$#accession I46694 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 449-468 ##label FI3 !'##cross-references GB:M25663; NID:g531211; PIDN:AAA31203.1; !1PID:g531212 COMMENT This enzyme cleaves collagens of types I, II, and III at a !1Gly-Ile site in the helical domain. Type X collagen, !1serpins, and alpha-macroglobulins are also cleaved by this !1enzyme. COMMENT Procollagenase can be activated without removal of the !1activation peptide. Stromelysin 1 activates the proenzyme !1either slowly by itself or very rapidly after cleavage(s) !1within the activation peptide by other proteinases. COMMENT Procollagenase is found in glycosylated and unglycosylated !1forms, both of which can be activated. GENETICS !$#introns 34/3; 116/2; 166/1; 208/1; 260/1; 299/2; 344/1; 398/1; 433/1 FUNCTION !$#description hydrolyzes collagens, in particular types I, II, III, and X, !1serpins, and alpha-macroglobulins at Gly-Ile sites in !1collagenous helix domains CLASSIFICATION #superfamily interstitial collagenase; hemopexin repeat !1homology; matrix metalloproteinase homology KEYWORDS calcium; extracellular matrix; fibroblast; glycoprotein; !1hydrolase; metalloproteinase; zinc; zymogen FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-468 #product procollagenase #status predicted #label PRO\ !$19-98 #domain activation peptide #status predicted #label !8ACT\ !$59-260 #domain matrix metalloproteinase homology #label MMP\ !$89-96 #region autoinhibitory\ !$99-468 #product interstitial collagenase #status predicted !8#label MAT\ !$271-465 #domain hemopexin repeat homology #label PXN\ !$91,217,221,227 #binding_site zinc, catalytic (Cys, His, His, His) !8(inhibited) #status predicted\ !$119,142 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$217,221,227 #binding_site zinc, catalytic (His) (active) #status !8predicted\ !$218 #active_site Glu #status predicted\ !$277-465 #disulfide_bonds #status predicted SUMMARY #length 468 #molecular-weight 53739 #checksum 7146 SEQUENCE /// ENTRY KCPGI #type complete TITLE interstitial collagenase (EC 3.4.24.7) precursor [validated] - pig ALTERNATE_NAMES fibroblast collagenase; matrix metalloproteinase 1 (MMP1); tissue collagenase; type I collagenase; vertebrate collagenase ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 15-Sep-2000 ACCESSIONS S15986; S13597 REFERENCE S15986 !$#authors Richards, C.D.; Rafferty, J.A.; Reynolds, J.J.; Saklatvala, !1J. !$#journal Matrix (1991) 11:161-167 !$#title Porcine collagenase from synovial fibroblasts: cDNA sequence !1and modulation of expression of RNA in vitro by various !1cytokines. !$#cross-references MUID:91333421; PMID:1651440 !$#accession S15986 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-469 ##label RIC !'##note part of the sequence, including the amino end of the proenzyme, !1was confirmed by protein sequencing REFERENCE S13597 !$#authors Clarke, N.J.; O'Hare, M.C.; Cawston, T.E.; Harper, G.P. !$#journal Nucleic Acids Res. (1990) 18:6703 !$#title Nucleotide sequence of a cDNA for porcine type I !1collagenase, obtained by PCR. !$#cross-references MUID:91067477; PMID:2174547 !$#accession S13597 !'##molecule_type mRNA !'##residues 25-469 ##label CLA !'##cross-references EMBL:X54724; NID:g2016; PIDN:CAA38526.1; !1PID:g930269 REFERENCE A65568 !$#authors Li, J.; Brick, P.; Blow, D.M. !$#submission submitted to the Brookhaven Protein Data Bank, April 1995 !$#cross-references PDB:1FBL !$#contents annotation; X-ray crystallography, 2.5 angstroms, residues !1100-466 COMMENT Procollagenase can be activated without removal of the !1activation peptide. Stromelysin 1 activates the proenzyme !1either slowly by itself or very rapidly after cleavage(s) !1within the activation peptide by other proteinases. COMMENT Procollagenase is found in glycosylated and unglycosylated !1forms, both of which can be activated. FUNCTION !$#description hydrolyzes collagens, in particular types I, II, III, and X, !1serpins, and alpha-macroglobulins at Gly-Ile sites in !1collagenous helix domains !$#note also hydrolyzes type X collagen, serpins, and !1alpha-macroglobulins CLASSIFICATION #superfamily interstitial collagenase; hemopexin repeat !1homology; matrix metalloproteinase homology KEYWORDS calcium; extracellular matrix; fibroblast; glycoprotein; !1hydrolase; metalloproteinase; zinc; zymogen FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-469 #product procollagenase #status predicted #label PRO\ !$20-99 #domain activation peptide #status experimental !8#label ACT\ !$60-261 #domain matrix metalloproteinase homology #label MMP\ !$100-469 #product interstitial collagenase #status predicted !8#label MAT\ !$272-466 #domain hemopexin repeat homology #label PXN\ !$92,218,222,228 #binding_site zinc, catalytic (Cys, His, His, His) !8(inhibited) #status predicted\ !$120,143 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$218,222,228 #binding_site zinc, catalytic (His) (active) #status !8experimental\ !$219 #active_site Glu #status predicted\ !$278-466 #disulfide_bonds #status experimental SUMMARY #length 469 #molecular-weight 53666 #checksum 7112 SEQUENCE /// ENTRY KCBOI #type complete TITLE interstitial collagenase (EC 3.4.24.7) precursor - bovine ALTERNATE_NAMES fibroblast collagenase; matrix metalloproteinase 1 (MMP1); tissue collagenase; type I collagenase; vertebrate collagenase ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS S14654; S20336; S14655 REFERENCE S14654 !$#authors Tamura, M.; Shimokawa, H.; Sasaki, S. !$#submission submitted to the EMBL Data Library, March 1991 !$#accession S14654 !'##molecule_type mRNA !'##residues 1-469 ##label TAM !'##cross-references EMBL:X58256; NID:g259; PIDN:CAA41210.1; PID:g260 REFERENCE S20336 !$#authors Sudbeck, B.D.; Jeffrey, J.J.; Welgus, H.G.; Mecham, R.P.; !1McCourt, D.; Parks, W.C. !$#journal Arch. Biochem. Biophys. (1992) 293:370-376 !$#title Purification and characterization of bovine interstitial !1collagenase and tissue inhibitor of metalloproteinases. !$#cross-references MUID:92161820; PMID:1311165 !$#accession S20336 !'##molecule_type protein !'##residues 19-21,'FP',24-29,'L',31-34,'LL',37-39,'F';86-105,'NPR', !1109-112,'D',114-125 ##label SUD COMMENT This enzyme cleaves collagens of types I, II, and III at a !1Gly-Ile site in the helical domain. Type X collagen, !1serpins, and alpha-macroglobulins are also cleaved by this !1enzyme. COMMENT Procollagenase can be activated without removal of the !1activation peptide. Stromelysin 1 activates the proenzyme !1either slowly by itself or very rapidly after cleavage(s) !1within the activation peptide by other proteinases. COMMENT Procollagenase is found in glycosylated and unglycosylated !1forms, both of which can be activated. FUNCTION !$#description hydrolyzes collagens, in particular types I, II, III, and X, !1serpins, and alpha-macroglobulins at Gly-Ile sites in !1collagenous helix domains CLASSIFICATION #superfamily interstitial collagenase; hemopexin repeat !1homology; matrix metalloproteinase homology KEYWORDS calcium; extracellular matrix; fibroblast; glycoprotein; !1hydrolase; metalloproteinase; zinc; zymogen FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-469 #product procollagenase #status predicted #label PRO\ !$19-99 #domain activation peptide #status predicted #label !8ACT\ !$60-261 #domain matrix metalloproteinase homology #label MMP\ !$90-97 #region autoinhibitory\ !$100-469 #product interstitial collagenase #status predicted !8#label MAT\ !$272-466 #domain hemopexin repeat homology #label PXN\ !$92,218,222,228 #binding_site zinc, catalytic (Cys, His, His, His) !8(inhibited) #status predicted\ !$120,143 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$218,222,228 #binding_site zinc, catalytic (His) (active) #status !8predicted\ !$219 #active_site Glu #status predicted\ !$278-466 #disulfide_bonds #status predicted SUMMARY #length 469 #molecular-weight 53354 #checksum 7657 SEQUENCE /// ENTRY KCHUN #type complete TITLE neutrophil collagenase (EC 3.4.24.34) precursor [validated] - human ALTERNATE_NAMES matrix metalloproteinase 8 ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 23-Mar-2001 ACCESSIONS A37073; A61175; B61175; A36230; S09680; S11026; S19576; !1S27225; S32527; S62608 REFERENCE A37073 !$#authors Hasty, K.A.; Pourmotabbed, T.F.; Goldberg, G.I.; Thompson, !1J.P.; Spinella, D.G.; Stevens, R.M.; Mainardi, C.L. !$#journal J. Biol. Chem. (1990) 265:11421-11424 !$#title Human neutrophil collagenase. A distinct gene product with !1homology to other matrix metalloproteinases. !$#cross-references MUID:90307647; PMID:2164002 !$#accession A37073 !'##molecule_type mRNA !'##residues 1-467 ##label HAS !'##cross-references GB:J05556; NID:g180617; PIDN:AAA88021.1; !1PID:g180618 REFERENCE A61175 !$#authors Devarajan, P.; Mookhtiar, K.; Van Wart, H.; Berliner, N. !$#journal Blood (1991) 77:2731-2738 !$#title Structure and expression of the cDNA encoding human !1neutrophil collagenase. !$#cross-references MUID:91255696; PMID:1646048 !$#accession A61175 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-31,'I',33-86,'E',88-467 ##label DEV !$#accession B61175 !'##molecule_type protein !'##residues 263-264,'X',266-270,'X',272-273,'X',275,'X',277 ##label DE2 REFERENCE A36230 !$#authors Mallya, S.K.; Mookhtiar, K.A.; Gao, Y.; Brew, K.; Dioszegi, !1M.; Birkedal-Hansen, H.; Van Wart, H.E. !$#journal Biochemistry (1990) 29:10628-10634 !$#title Characterization of 58-kilodalton human neutrophil !1collagenase: comparison with human fibroblast collagenase. !$#cross-references MUID:91104978; PMID:2176876 !$#accession A36230 !'##molecule_type protein !'##residues 'X',86-87,'X',89-90,'X',92-97,'X',99-111,'X',113-120 !1##label MAL REFERENCE S09680 !$#authors Knaeuper, V.; Kraemer, S.; Reinke, H.; Tschesche, H. !$#journal Eur. J. Biochem. (1990) 189:295-300 !$#title Characterization and activation of procollagenase from human !1polymorphonuclear leucocytes. N-terminal sequence !1determination of the proenzyme and various proteolytically !1activated forms. !$#cross-references MUID:90249372; PMID:2159879 !$#accession S09680 !'##molecule_type protein !'##residues 21-31,'I',33-39,'I',41-47,'V',49-53,'I',55-72,'G',74-86, !1'E',88-111,'X',113-140 ##label KNA !'##note 67-Lys was also found REFERENCE S11026 !$#authors Knaeuper, V.; Kraemer, S.; Reinke, H.; Tschesche, H. !$#journal Biol. Chem. Hoppe-Seyler (1990) 371:733 !$#title Corrigendum. Partial amino-acid sequence of human PMN !1leukocyte procollagenase. !$#cross-references MUID:91000455; PMID:2169766 !$#note original publication was Biol. Chem. Hoppe-Seyler 371 !1(Suppl.), 295-304, 1990 !$#accession S11026 !'##molecule_type protein !'##residues 21-31,'I',33-53,'I',55-72,'G',74-111,'X',113-140;183-203, !1'X',205-209;248-261;305-306,'N',308-314,'T';321-338;'E', !1370-377,'X',379-380,'F';397-403,'K',405-456;462-467 ##label !1KN2 !'##note 87-Glu was also found REFERENCE S19576 !$#authors Blaeser, J.; Knaeuper, V.; Osthues, A.; Reinke, H.; !1Tschesche, H. !$#journal Eur. J. Biochem. (1991) 202:1223-1230 !$#title Mercurial activation of human polymorphonuclear leucocyte !1procollagenase. !$#cross-references MUID:92111500; PMID:1662606 !$#accession S19576 !'##molecule_type protein !'##residues 69-103 ##label BL2 REFERENCE S27225 !$#authors Blaeser, J.; Triebel, S.; Reinke, H.; Tschesche, H. !$#journal FEBS Lett. (1992) 313:59-61 !$#title Formation of a covalent Hg-Cys-bond during mercurial !1activation of PMNL procollagenase gives evidence of a !1cysteine-switch mechanism. !$#cross-references MUID:93050220; PMID:1330697 !$#accession S27225 !'##molecule_type protein !'##residues 68-103 ##label BLA REFERENCE S32527 !$#authors Knaeuper, V.; Osthues, A.; DeClerck, Y.A.; Langley, K.E.; !1Blaeser, J.; Tschesche, H. !$#journal Biochem. J. (1993) 291:847-854 !$#title Fragmentation of human polymorphonuclear-leucocyte !1collagenase. !$#cross-references MUID:93256897; PMID:8489511 !$#accession S32527 !'##molecule_type protein !'##residues 100-112;263-276 ##label KN3 REFERENCE S62608 !$#authors Knaeuper, V.; Murphy, G.; Tschesche, H. !$#journal Eur. J. Biochem. (1996) 235:187-191 !$#title Activation of human neutrophil procollagenase by stromelysin !12. !$#cross-references MUID:96202934; PMID:8631328 !$#accession S62608 !'##molecule_type protein !'##residues 21-39,'I',41-47,'V',49-122 ##label KN4 REFERENCE A67078 !$#authors Stams, T.; Spurlino, J.C.; Smith, D.L.; Rubin, B. !$#submission submitted to the Brookhaven Protein Data Bank, January 1994 !$#cross-references PDB:1MNC !$#contents annotation; X-ray crystallography, 2.1 angstroms, residues !1'G',106-149,'G',151-169,'G',171-262 REFERENCE A58274 !$#authors Stams, T.; Spurlino, J.C.; Smith, D.L.; Wahl, R.C.; Ho, !1T.F.; Qoronfleh, M.W.; Banks, T.M.; Rubin, B. !$#journal Nat. Struct. Biol. (1994) 1:119-123 !$#title Structure of human neutrophil collagenase reveals large S1' !1specificity pocket. !$#cross-references MUID:95384762; PMID:7656015 !$#contents annotation; X-ray crystallography, 2.1 angstroms, residues !1'G',106-149,'G',151-169,'G',171-262 COMMENT This protein is more highly glycosylated than interstitial !1collagenase and is stored in intracellular granules. GENETICS !$#gene GDB:MMP8; CLG1 !'##cross-references GDB:128173; OMIM:120355 !$#map_position 11q22.2-11q22.3 FUNCTION !$#description hydrolyzes collagen types I, II, and III at Gly-Ile sites in !1collagenous helix domains !$#note cleaves type I collagen most rapidly CLASSIFICATION #superfamily interstitial collagenase; hemopexin repeat !1homology; matrix metalloproteinase homology KEYWORDS calcium; extracellular matrix; glycoprotein; hydrolase; !1metalloproteinase; neutrophil; polymorphonuclear leukocyte; !1zinc; zymogen FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-467 #product procollagenase #status predicted #label PRO\ !$21-100 #domain activation peptide #status experimental !8#label ACT\ !$59-262 #domain matrix metalloproteinase homology #label MMP\ !$89-96 #region autoinhibitory\ !$101-467 #product neutrophil collagenase #status predicted !8#label MAT\ !$273-464 #domain hemopexin repeat homology #label PXN\ !$54,73,112,119,204, !$246 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$73-74 #cleavage_site Asn-Val (autolytic) #status !8experimental\ !$84-85 #cleavage_site Asp-Met (autolytic) #status !8experimental\ !$91,217,221,227 #binding_site zinc, catalytic (Cys, His, His, His) !8(inhibited) #status predicted\ !$99-100 #cleavage_site Phe-Met (autolytic) #status !8experimental\ !$167,169,182,195 #binding_site zinc, noncatalytic (His, Asp, His, His) !8#status experimental\ !$174,175,177,179, !$197,200 #binding_site calcium (Asp, Gly, Asn, Ile, Asp, Glu) !8#status experimental\ !$217,221,227 #binding_site zinc, catalytic (His) (active) #status !8experimental\ !$218 #active_site Glu #status predicted\ !$262-263 #cleavage_site Gly-Leu (autolytic) #status !8experimental\ !$279-464 #disulfide_bonds #status predicted SUMMARY #length 467 #molecular-weight 53412 #checksum 7218 SEQUENCE /// ENTRY KCHUS1 #type complete TITLE stromelysin 1 (EC 3.4.24.17) precursor [validated] - human ALTERNATE_NAMES angiostatin-converting enzyme; collagenase activating protein; matrix metalloproteinase 3 (MMP3); procollagenase activator; proteoglycanase; transin-1 ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1992 #sequence_revision 08-May-1998 #text_change 15-Sep-2000 ACCESSIONS A28156; C29157; A28399; A60964; S15427 REFERENCE A28156 !$#authors Saus, J.; Quinones, S.; Otani, Y.; Nagase, H.; Harris Jr., !1E.D.; Kurkinen, M. !$#journal J. Biol. Chem. (1988) 263:6742-6745 !$#title The complete primary structure of human matrix !1metalloproteinase-3. Identity with stromelysin. !$#cross-references MUID:88198243; PMID:3360803 !$#accession A28156 !'##molecule_type mRNA !'##residues 1-44,'E',46-477 ##label SAU !'##cross-references GB:J03209; NID:g188618; PIDN:AAA36321.1; !1PID:g188619 REFERENCE A90336 !$#authors Whitham, S.E.; Murphy, G.; Angel, P.; Rahmsdorf, H.J.; !1Smith, B.J.; Lyons, A.; Harris, T.J.R.; Reynolds, J.J.; !1Herrlich, P.; Docherty, A.J.P. !$#journal Biochem. J. (1986) 240:913-916 !$#title Comparison of human stromelysin and collagenase by cloning !1and sequence analysis. !$#cross-references MUID:87156645; PMID:3030290 !$#accession C29157 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-477 ##label WHI !'##cross-references EMBL:X05232; NID:g36632; PIDN:CAA28859.1; !1PID:g36633 REFERENCE A28399 !$#authors Wilhelm, S.M.; Collier, I.E.; Kronberger, A.; Eisen, A.Z.; !1Marmer, B.L.; Grant, G.A.; Bauer, E.A.; Goldberg, G.I. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:6725-6729 !$#title Human skin fibroblast stromelysin: structure, glycosylation, !1substrate specificity, and differential expression in normal !1and tumorigenic cells. !$#cross-references MUID:88016164; PMID:3477804 !$#accession A28399 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type mRNA !'##residues 1-49,'G',51-419,'L',421-477 ##label WIL !'##cross-references GB:U78045; NID:g1688257; PIDN:AAB36942.1; !1PID:g1688259 !'##note part of the sequence, including the amino end of the proenzyme, !1was confirmed by protein sequencing REFERENCE A60964 !$#authors Lark, M.W.; Walakovits, L.A.; Shah, T.K.; Vanmiddlesworth, !1J.; Cameron, P.M.; Lin, T.Y. !$#journal Connect. Tissue Res. (1990) 25:49-65 !$#title Production and purification of prostromelysin and !1procollagenase from IL-1 beta-stimulated human gingival !1fibroblasts. !$#cross-references MUID:91059606; PMID:2173990 !$#accession A60964 !'##molecule_type protein !'##residues 18-29;100-108 ##label LAR REFERENCE S15427 !$#authors Koklitis, P.A.; Murphy, G.; Sutton, C.; Angal, S. !$#journal Biochem. J. (1991) 276:217-221 !$#title Purification of recombinant human prostromelysin. Studies on !1heat activation to give high-M(r) and low-M(r) active forms, !1and a comparison of recombinant with natural stromelysin !1activities. !$#cross-references MUID:91248150; PMID:2039471 !$#accession S15427 !'##status preliminary !'##molecule_type protein !'##residues 18-23 ##label BIO REFERENCE A58812 !$#authors Lijnen, H.R.; Ugwu, F.; Bini, A.; Collen, D. !$#journal Biochemistry (1998) 37:4699-4702 !$#title Generation of an angiostatin-like fragment from plasminogen !1by stromelysin-1 (MMP-3). !$#cross-references MUID:9548733; PMID:9548733 !$#contents annotation REFERENCE A68466 !$#authors Becker, J.W. !$#submission submitted to the Brookhaven Protein Data Bank, February 1997 !$#cross-references PDB:1HFS !$#contents annotation; X-ray crystallography, 1.70 angstroms, residues !1105-160 REFERENCE A58814 !$#authors Becker, J.W.; Marcy, A.I.; Rokosz, L.L.; Axel, M.G.; !1Burbaum, J.J.; Fitzgerald, P.M.D.; Cameron, P.M.; Esser, !1C.K.; Hagmann, W.K.; Hermes, J.D.; Springer, J.P. !$#journal Protein Sci. (1995) 4:1966-1976 !$#title Stromelysin-1: three-dimensional structure of the inhibited !1catalytic domain and of the C-truncated proenzyme. !$#cross-references MUID:96117647; PMID:8535233 !$#contents annotation; X-ray crystallography, 1.70 angstroms REFERENCE A39589 !$#authors Marcy, A.I.; Eiberger, L.L.; Harrison, R.; Chan, H.K.; !1Hutchinson, N.I.; Hagmann, W.K.; Cameron, P.M.; Boulton, !1D.A.; Hermes, J.D. !$#journal Biochemistry (1991) 30:6476-6483 !$#title Human fibroblast stromelysin catalytic domain: expression, !1purification, and characterization of a C-terminally !1truncated form. !$#cross-references MUID:91274298; PMID:1647201 !$#contents annotation REFERENCE A66637 !$#authors Becker, J.W. !$#submission submitted to the Brookhaven Protein Data Bank, August 1995 !$#cross-references PDB:1SLM !$#contents annotation; X-ray crystallography, 1.90 angstroms, residues !133-47;57-267 REFERENCE A67284 !$#authors Gooley, P.R.; O'connell, J.F. !$#submission submitted to the Brookhaven Protein Data Bank, March 1995 !$#cross-references PDB:2SRT !$#contents annotation; conformation by (1)H-NMR, residues 100-272 REFERENCE A58815 !$#authors Gooley, P.R.; Johnson, B.A.; Marcy, A.I.; Cuca, G.C.; !1Salowe, S.P.; Hagmann, W.K.; Esser, C.K.; Springer, J.P. !$#journal Biochemistry (1993) 32:13098-14008 !$#title Secondary structure and zinc ligation of human recombinant !1short-form stromelysin by multidimensional heteronuclear !1NMR. !$#cross-references MUID:94059987; PMID:8241164 !$#contents annotation; conformation by (1)H-NMR COMMENT Stromelysin 1 activates its proenzyme after cleavage(s) !1within the activation peptide by other proteinases. COMMENT Prostromelysin is found in glycosylated and unglycosylated !1forms, both of which can be activated. GENETICS !$#gene GDB:MMP3; STMY; STMY1 !'##cross-references GDB:120727; OMIM:185250 !$#map_position 11q23-11q23 FUNCTION !$#description endopeptidase preferentially hydrolyzing peptide bonds on !1the carboxyl side of hydrophobic residues !$#note degrades various extracellular matrix proteins, including !1fibronectin, plasminogen, laminin, cartilage proteoglycans, !1and collagens of types II, IV, IX, X, and XI; hydrolyzes !1peptide bonds in plasminogen to yield a fragment with !1angiostatin activity CLASSIFICATION #superfamily interstitial collagenase; hemopexin repeat !1homology; matrix metalloproteinase homology KEYWORDS calcium; extracellular matrix; fibroblast; glycoprotein; !1hydrolase; metalloproteinase; zinc; zymogen FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-477 #product prostromelysin 1 #status experimental #label !8PRO\ !$18-99 #domain activation peptide #status experimental !8#label ACT\ !$60-264 #domain matrix metalloproteinase homology #label MMP\ !$100-477 #product stromelysin 1 #status experimental #label !8MAT\ !$284-477 #domain hemopexin repeat homology #label PXN\ !$92,218,222,228 #binding_site zinc, catalytic (Cys, His, His, His) !8(inhibited) #status experimental\ !$120 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$218,222,228 #binding_site zinc, catalytic (His) (active) #status !8experimental\ !$219 #active_site Glu #status predicted\ !$290-477 #disulfide_bonds #status predicted SUMMARY #length 477 #molecular-weight 53977 #checksum 1937 SEQUENCE /// ENTRY KCRBS1 #type complete TITLE stromelysin 1 (EC 3.4.24.17) precursor - rabbit ALTERNATE_NAMES collagenase activating protein; matrix metalloproteinase 3 (MMP3); procollagenase activator; proteoglycanase; transin-1 ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS A37306; A29157 REFERENCE A37306 !$#authors Fini, M.E.; Karmilowicz, M.J.; Ruby, P.L.; Beeman, A.M.; !1Borges, K.A.; Brinckerhoff, C.E. !$#journal Arthritis Rheum. (1987) 30:1254-1264 !$#title Cloning of a complementary DNA for rabbit proactivator. A !1metalloproteinase that activates synovial cell collagenase, !1shares homology with stromelysin and transin, and is !1coordinately regulted with collagenase. !$#cross-references MUID:88077214; PMID:2825726 !$#accession A37306 !'##molecule_type mRNA !'##residues 1-478 ##label FIN !'##cross-references GB:M25664; NID:g165709; PIDN:AAA31467.1; !1PID:g165710 REFERENCE A90336 !$#authors Whitham, S.E.; Murphy, G.; Angel, P.; Rahmsdorf, H.J.; !1Smith, B.J.; Lyons, A.; Harris, T.J.R.; Reynolds, J.J.; !1Herrlich, P.; Docherty, A.J.P. !$#journal Biochem. J. (1986) 240:913-916 !$#title Comparison of human stromelysin and collagenase by cloning !1and sequence analysis. !$#cross-references MUID:87156645; PMID:3030290 !$#accession A29157 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type mRNA !'##residues 1-82,'D',84-127,'K',129-167,'GNS' ##label WHI COMMENT This enzyme degrades various extracellular matrix proteins, !1including fibronectin, plasminogen, laminin, cartilage !1proteoglycans, and collagens of types II, IV, IX, X, and XI. COMMENT Stromolysin 1 hydrolyzes peptide bonds in plasminogen to !1yield a fragment with angiostatin activity. COMMENT Stromelysin 1 activates its proenzyme after cleavage(s) !1within the activation peptide by other proteinases. COMMENT Prostromolysin is found in glycosylated and unglycosylated !1forms, both of which can be activated. FUNCTION !$#description endopeptidase preferentially hydrolyzing peptide bonds on !1the carboxyl side of hydrophobic residues CLASSIFICATION #superfamily interstitial collagenase; hemopexin repeat !1homology; matrix metalloproteinase homology KEYWORDS calcium; extracellular matrix; fibroblast; glycoprotein; !1hydrolase; metalloproteinase; zinc; zymogen FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-478 #product prostromelysin 1 #status predicted #label !8PRO\ !$18-100 #domain activation peptide #status predicted #label !8ACT\ !$61-265 #domain matrix metalloproteinase homology #label MMP\ !$91-98 #region autoinhibitory\ !$101-478 #product stromelysin 1 #status predicted #label MAT\ !$285-478 #domain hemopexin repeat homology #label PXN\ !$93,219,223,229 #binding_site zinc, catalytic (Cys, His, His, His) !8(inhibited) #status predicted\ !$121 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$219,223,229 #binding_site zinc, catalytic (His) (active) #status !8predicted\ !$220 #active_site Glu #status predicted\ !$291-478 #disulfide_bonds #status predicted SUMMARY #length 478 #molecular-weight 53942 #checksum 3421 SEQUENCE /// ENTRY KCMSS1 #type complete TITLE stromelysin 1 (EC 3.4.24.17) precursor - mouse ALTERNATE_NAMES collagenase activating protein; matrix metalloproteinase 3 (MMP3); procollagenase activator; proteoglycanase; transin-1 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Sep-1992 #sequence_revision 30-Sep-1993 #text_change 18-Jun-1999 ACCESSIONS JC1476; S18867; B32963; S33139 REFERENCE JC1476 !$#authors Hammani, K.; Henriet, P.; Eeckhout, Y. !$#journal Gene (1992) 120:321-322 !$#title Cloning and sequencing of a cDNA encoding mouse stromelysin !11. !$#cross-references MUID:93013057; PMID:1398148 !$#accession JC1476 !'##molecule_type mRNA !'##residues 1-477 ##label HAM !'##cross-references EMBL:X66402; NID:g296167; PIDN:CAA47029.1; !1PID:g296168 !'##note it is uncertain whether Met-1 is the initiator or whether !1translation is initiated two codons upstream to the !1sequenced region REFERENCE S18867 !$#authors Li, F.; Strange, R.; Saurer, S.; Niemann, H.; Friis, R.R. !$#submission submitted to the EMBL Data Library, August 1991 !$#accession S18867 !'##molecule_type mRNA !'##residues 'MK',1-477 ##label LIF !'##cross-references EMBL:X63162; NID:g54871; PIDN:CAA44860.1; !1PID:g54872 REFERENCE A32963 !$#authors Brenner, C.A.; Adler, R.R.; Rappolee, D.A.; Pedersen, R.A.; !1Werb, Z. !$#journal Genes Dev. (1989) 3:848-859 !$#title Genes for extracellular matrix-degrading metalloproteinases !1and their inhibitor, TIMP, are expressed during early !1mammalian development. !$#cross-references MUID:89306621; PMID:2744464 !$#accession B32963 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type mRNA !'##residues 415-467,'T',469 ##label BRE !'##experimental_source clone EMS-2 COMMENT Stromelysin 1 activates its proenzyme after cleavage(s) !1within the activation peptide by other proteinases. COMMENT This enzyme degrades various extracellular matrix proteins, !1including fibronectin, plasminogen, laminin, cartilage !1proteoglycans, and collagens of types II, IV, IX, X, and XI. COMMENT Stromolysin 1 hydrolyzes peptide bonds in plasminogen to !1yield a fragment with angiostatin activity. COMMENT Prostromelysin is found in glycosylated and unglycosylated !1forms, both of which can be activated. FUNCTION !$#description endopeptidase preferentially hydrolyzing peptide bonds on !1the carboxyl side of hydrophobic residues CLASSIFICATION #superfamily interstitial collagenase; hemopexin repeat !1homology; matrix metalloproteinase homology KEYWORDS calcium; extracellular matrix; fibroblast; glycoprotein; !1hydrolase; metalloproteinase; zinc; zymogen FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-477 #product prostromelysin 1 #status predicted #label !8PRO\ !$18-99 #domain activation peptide #status predicted #label !8ACT\ !$60-264 #domain matrix metalloproteinase homology #label MMP\ !$90-97 #region autoinhibitory\ !$100-477 #product stromelysin 1 #status predicted #label MAT\ !$284-477 #domain hemopexin repeat homology #label PXN\ !$92,218,222,228 #binding_site zinc, catalytic (Cys, His, His, His) !8(inhibited) #status predicted\ !$218,222,228 #binding_site zinc, catalytic (His) (active) #status !8predicted\ !$219 #active_site Glu #status predicted\ !$290-477 #disulfide_bonds #status predicted SUMMARY #length 477 #molecular-weight 53845 #checksum 2078 SEQUENCE /// ENTRY KCRTIH #type complete TITLE stromelysin 1 (EC 3.4.24.17) precursor - rat ALTERNATE_NAMES collagenase activating protein; matrix metalloproteinase 3 (MMP3); procollagenase activator; proteoglycanase; pTR1 protein; transin-1 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 13-Aug-1986 #sequence_revision 13-Aug-1986 #text_change 18-Jun-1999 ACCESSIONS A00997; PS0150; S22767 REFERENCE A00997 !$#authors Matrisian, L.M.; Glaichenhaus, N.; Gesnel, M.C.; Breathnach, !1R. !$#journal EMBO J. (1985) 4:1435-1440 !$#title Epidermal growth factor and oncogenes induce transcription !1of the same cellular mRNA in rat fibroblasts. !$#cross-references MUID:85284930; PMID:3875482 !$#accession A00997 !'##molecule_type mRNA !'##residues 1-475 ##label MA1 !'##cross-references GB:X02601; NID:g57460; PIDN:CAA26448.1; PID:g57461 REFERENCE PS0150 !$#authors Umenishi, F.; Yasumitsu, H.; Ashida, Y.; Yamauti, J.; Umeda, !1M.; Miyazaki, K. !$#journal J. Biochem. (1990) 108:537-543 !$#title Purification and properties of extracellular !1matrix-degrading metallo-proteinase overproduced by Rous !1sarcoma virus-transformed rat liver cell line, and its !1identification as transin. !$#cross-references MUID:91154156; PMID:1963430 !$#accession PS0150 !'##molecule_type protein !'##residues 19-20,'X',22-28;110-112,'X',114-115,'X',117,'X',119;309-325 !1##label UME REFERENCE A26403 !$#authors Breathnach, R.; Matrisian, L.M.; Gesnel, M.C.; Staub, A.; !1Leroy, P. !$#journal Nucleic Acids Res. (1987) 15:1139-1151 !$#title Sequences coding for part of oncogene-induced transin are !1highly conserved in a related rat gene. !$#cross-references MUID:87146421; PMID:3547333 !$#contents annotation; introns !$#note intron positions were determined by comparison of the !1previously reported cDNA sequence to genomic sequences (not !1shown) REFERENCE S22767 !$#authors Sanchez-Lopez, R.; Nicholson, R.; Gesnel, M.C.; Matrisian, !1L.M.; Breathnach, R. !$#journal J. Biol. Chem. (1988) 263:11892-11899 !$#title Structure-function relationships in the collagenase family !1member transin. !$#cross-references MUID:88298869; PMID:2841336 !$#contents annotation; active site; activation !$#note molecules with mutations in the autoinhibitory region showed !1a much increased tendency to undergo spontaneous activation !$#note mutations of His-216, Glu-217, and His-226 inactivate the !1enzyme REFERENCE A43028 !$#authors Park, A.J.; Matrisian, L.M.; Kells, A.F.; Pearson, R.; Yuan, !1Z.; Navre, M. !$#journal J. Biol. Chem. (1991) 266:1584-1590 !$#title Mutational analysis of the transin (rat stromelysin) !1autoinhibitor region demonstrates a role for residues !1surrounding the "cysteine switch". !$#cross-references MUID:91107652; PMID:1988438 !$#contents annotation; autoinhibitory region !$#note Arg-89 and Cys-92 are essential for maintaining latency COMMENT This enzyme degrades various extracellular matrix proteins, !1including fibronectin, plasminogen, laminin, cartilage !1proteoglycans, and collagens of types II, IV, IX, X, and XI. COMMENT Stromolysin 1 hydrolyzes peptide bonds in plasminogen to !1yield a fragment with angiostatin activity. COMMENT Stromelysin 1 activates its proenzyme after cleavage(s) !1within the activation peptide by other proteinases. COMMENT Prostromelysin is found in glycosylated and unglycosylated !1forms, both of which can be activated. GENETICS !$#introns 33/3; 115/2; 165/1; 207/1; 262/1; 310/2; 355/1; 408/2; 443/1 FUNCTION !$#description endopeptidase preferentially hydrolyzing peptide bonds on !1the carboxyl side of hydrophobic residues CLASSIFICATION #superfamily interstitial collagenase; hemopexin repeat !1homology; matrix metalloproteinase homology KEYWORDS calcium; extracellular matrix; fibroblast; glycoprotein; !1hydrolase; metalloproteinase; zinc; zymogen FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-475 #product prostromelysin 1 #status predicted #label !8PRO\ !$18-97 #domain activation peptide #status predicted #label !8ACT\ !$58-262 #domain matrix metalloproteinase homology #label MMP\ !$88-95 #region autoinhibitory\ !$98-475 #product stromelysin 1 #status predicted #label MAT\ !$282-475 #domain hemopexin repeat homology #label PXN\ !$90,216,220,226 #binding_site zinc, catalytic (Cys, His, His, His) !8(inhibited) #status predicted\ !$118 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$216,220,226 #binding_site zinc, catalytic (His) (active) #status !8predicted\ !$217 #active_site Glu #status experimental\ !$288-475 #disulfide_bonds #status predicted SUMMARY #length 475 #molecular-weight 53427 #checksum 849 SEQUENCE /// ENTRY KCHUS2 #type complete TITLE stromelysin 2 (EC 3.4.24.22) precursor [validated] - human ALTERNATE_NAMES matrix metalloproteinase 10 (MMP10); transin-2 ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 08-Dec-2000 ACCESSIONS A28816; A47496 REFERENCE A90339 !$#authors Muller, D.; Quantin, B.; Gesnel, M.C.; Millon-Collard, R.; !1Abecassis, J.; Breathnach, R. !$#journal Biochem. J. (1988) 253:187-192 !$#title The collagenase gene family in humans consists of at least !1four members. !$#cross-references MUID:88339885; PMID:2844164 !$#accession A28816 !'##molecule_type mRNA !'##residues 1-476 ##label MUL !'##cross-references EMBL:X07820; NID:g36628; PIDN:CAA30679.1; !1PID:g36629 !'##note mRNA for this protein was detected in several human tumors REFERENCE A47496 !$#authors Windsor, L.J.; Grenett, H.; Birkedal-Hansen, B.; Bodden, !1M.K.; Engler, J.A.; Birkedal-Hansen, H. !$#journal J. Biol. Chem. (1993) 268:17341-17347 !$#title Cell type-specific regulation of SL-1 and SL-2 genes. !1Induction of the SL-2 gene but not the SL-1 gene by human !1keratinocytes in response to cytokines and phorbolesters. !$#cross-references MUID:93352520; PMID:8349617 !$#accession A47496 !'##molecule_type protein !'##residues 17-33 ##label WIN COMMENT This enzyme degrades various extracellular matrix proteins, !1including fibronectin, collagens of types III, IV, and V, !1and gelatins formed from several denatured collagen types. GENETICS !$#gene GDB:MMP10; STMY2 !'##cross-references GDB:120392; OMIM:185260 !$#map_position 11q22.3-11q23 CLASSIFICATION #superfamily interstitial collagenase; hemopexin repeat !1homology; matrix metalloproteinase homology KEYWORDS calcium; extracellular matrix; fibroblast; glycoprotein; !1hydrolase; metalloproteinase; zinc; zymogen FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-476 #product prostromelysin 2 #status experimental #label !8PRO\ !$17-98 #domain activation peptide #status predicted #label !8ACT\ !$59-263 #domain matrix metalloproteinase homology #label MMP\ !$89-96 #region autoinhibitory\ !$99-476 #product stromelysin 2 #status predicted #label MAT\ !$283-476 #domain hemopexin repeat homology #label PXN\ !$91,217,221,227 #binding_site zinc, catalytic (Cys, His, His, His) !8(inhibited) #status predicted\ !$119 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$217,221,227 #binding_site zinc, catalytic (His) (active) #status !8predicted\ !$218 #active_site Glu #status predicted\ !$289-476 #disulfide_bonds #status predicted SUMMARY #length 476 #molecular-weight 54151 #checksum 699 SEQUENCE /// ENTRY KCRTS2 #type complete TITLE stromelysin 2 (EC 3.4.24.22) precursor - rat ALTERNATE_NAMES matrix metalloproteinase 10 (MMP10); transin-2 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS B26403; A41775; S26498 REFERENCE A26403 !$#authors Breathnach, R.; Matrisian, L.M.; Gesnel, M.C.; Staub, A.; !1Leroy, P. !$#journal Nucleic Acids Res. (1987) 15:1139-1151 !$#title Sequences coding for part of oncogene-induced transin are !1highly conserved in a related rat gene. !$#cross-references MUID:87146421; PMID:3547333 !$#accession B26403 !'##molecule_type mRNA !'##residues 1-476 ##label BRE !'##cross-references EMBL:X05083; NID:g57388; PIDN:CAA28739.1; !1PID:g57389 !'##note intron positions were determined by comparison of the cDNA !1sequence to genomic sequences (not shown) !'##note mRNA for this protein was expressed in several transformed rat !1embryo fibroblast cell lines but not in normal cells REFERENCE A41775 !$#authors Chan, J.C.; Scanlon, M.; Zhang, H.Z.; Jia, L.B.; Yu, D.H.; !1Hung, M.C.; French, M.; Eastman, E.M. !$#journal J. Biol. Chem. (1992) 267:1099-1103 !$#title Molecular cloning and characterization of v-mos-activated !1transformation-associated proteins. !$#cross-references MUID:92112748; PMID:1370458 !$#accession A41775 !'##molecule_type mRNA !'##residues 1-476 ##label CHA !'##cross-references GB:M65253; NID:g207150; PIDN:AAA42202.1; !1PID:g207151 !'##note sequence extracted from NCBI backbone (NCBIP:76184) REFERENCE S26496 !$#authors de Vouge, M.W.; Mukherjee, B.B. !$#journal Oncogene (1992) 7:109-119 !$#title Transformation of normal rat kidney cells by v-K-ras !1enhances expression of transin 2 and an S-100-related !1calcium-binding protein. !$#cross-references MUID:92158347; PMID:1741158 !$#accession S26498 !'##status preliminary; translation not shown !'##molecule_type mRNA !'##residues 31-103,'L',241-242,'TQMEEKPH',251,'L',253-254,'CE',293-294, !1'L',296 ##label DEV !'##cross-references EMBL:X64020 GENETICS !$#introns 35/3; 117/2; 167/1; 209/1; 264/1; 311/2; 356/1; 409/2; 444/1 CLASSIFICATION #superfamily interstitial collagenase; hemopexin repeat !1homology; matrix metalloproteinase homology KEYWORDS calcium; extracellular matrix; fibroblast; glycoprotein; !1hydrolase; metalloproteinase; zinc; zymogen FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-476 #product prostromelysin 2 #status predicted #label !8PRO\ !$18-99 #domain activation peptide #status predicted #label !8ACT\ !$60-264 #domain matrix metalloproteinase homology #label MMP\ !$90-97 #region autoinhibitory\ !$100-476 #product stromelysin 2 #status predicted #label MAT\ !$283-476 #domain hemopexin repeat homology #label PXN\ !$92,218,222,228 #binding_site zinc, catalytic (Cys, His, His, His) !8(inhibited) #status predicted\ !$120 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$218,222,228 #binding_site zinc, catalytic (His) (active) #status !8predicted\ !$219 #active_site Glu #status predicted\ !$289-476 #disulfide_bonds #status predicted SUMMARY #length 476 #molecular-weight 54221 #checksum 8372 SEQUENCE /// ENTRY JC6505 #type complete TITLE stromelysin 2 (EC 3.4.24.22) precursor - mouse ALTERNATE_NAMES matrix metalloproteinase 10 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 16-Oct-1998 #sequence_revision 16-Oct-1998 #text_change 21-Jul-2000 ACCESSIONS JC6505 REFERENCE JC6505 !$#authors Madlener, M.; Werner, S. !$#journal Gene (1997) 202:75-81 !$#title cDNA cloning and expression of the gene encoding murine !1stromelysin-2 (MMP-10). !$#cross-references MUID:98087420; PMID:9427548 !$#accession JC6505 !'##molecule_type mRNA !'##residues 1-476 ##label MAD !'##cross-references GB:Y13185; NID:g2791311; PIDN:CAA73641.1; !1PID:g2791312 COMMENT This enzyme degrades various extracellular matrix proteins, !1including fibronectin, collagens of types III, IV, and V, !1and gelatins formed from several denatured collagen types. GENETICS !$#gene MMP-10 CLASSIFICATION #superfamily interstitial collagenase; hemopexin repeat !1homology; matrix metalloproteinase homology KEYWORDS calcium; extracellular matrix; fibroblast; glycoprotein; !1hydrolase; metalloproteinase; zinc; zymogen FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-476 #product prostromelysin 2 #status predicted #label !8PRO\ !$18-99 #domain activation peptide #status predicted #label !8ACT\ !$60-264 #domain matrix metalloproteinase homology #label MMP\ !$90-97 #region autoinhibitory\ !$100-476 #product stromelysin 2 #status predicted #label MAT\ !$283-476 #domain hemopexin repeat homology #label PXN\ !$92,218,222,228 #binding_site zinc, catalytic (Cys, His, His, His) !8(inhibited) #status predicted\ !$120 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$218,222,228 #binding_site zinc, catalytic (His) (active) #status !8predicted\ !$219 #active_site Glu #status predicted\ !$289-476 #disulfide_bonds #status predicted SUMMARY #length 476 #molecular-weight 53911 #checksum 9443 SEQUENCE /// ENTRY I51645 #type complete TITLE stromelysin 3 (EC 3.4.24.-) - African clawed frog ALTERNATE_NAMES matrix metalloproteinase 11 (MMP11) ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS I51645; S38623 REFERENCE I51645 !$#authors Patterton, D.; Hayes, W.P.; Shi, Y.B. !$#journal Dev. Biol. (1995) 167:252-262 !$#title Transcriptional activation of the matrix metalloproteinase !1gene stromelysin-3 coincides with thyroid hormone-induced !1cell death during frog metamorphosis. !$#cross-references MUID:95154568; PMID:7851646 !$#accession I51645 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-477 ##label PAT !'##cross-references EMBL:Z27093; NID:g414917; PIDN:CAA81616.1; !1PID:g414918 CLASSIFICATION #superfamily interstitial collagenase; hemopexin repeat !1homology; matrix metalloproteinase homology KEYWORDS extracellular matrix; hydrolase; metalloproteinase; zinc; !1zymogen FEATURE !$33-246 #domain matrix metalloproteinase homology #label MMP\ !$63-70 #region autoinhibitory\ !$273-466 #domain hemopexin repeat homology #label PXN\ !$65,203,207,213 #binding_site zinc, catalytic (Cys, His, His, His) !8(inhibited) #status experimental\ !$203,207,213 #binding_site zinc, catalytic (His) (active) #status !8predicted\ !$204 #active_site Glu #status predicted SUMMARY #length 477 #molecular-weight 54441 #checksum 7366 SEQUENCE /// ENTRY KCHUM #type complete TITLE matrilysin (EC 3.4.24.23) precursor - human ALTERNATE_NAMES matrin; matrix metalloproteinase 7 (MMP7); probable metalloproteinase-1 (pump-1); uterine metalloendopeptidase CONTAINS promatrilysin ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS B28816; A60539; S24324 REFERENCE A90339 !$#authors Muller, D.; Quantin, B.; Gesnel, M.C.; Millon-Collard, R.; !1Abecassis, J.; Breathnach, R. !$#journal Biochem. J. (1988) 253:187-192 !$#title The collagenase gene family in humans consists of at least !1four members. !$#cross-references MUID:88339885; PMID:2844164 !$#accession B28816 !'##molecule_type mRNA !'##residues 1-267 ##label MUL !'##cross-references EMBL:X07819; NID:g35798; PIDN:CAA30678.1; !1PID:g35799 REFERENCE A60539 !$#authors Miyazaki, K.; Hattori, Y.; Umenishi, F.; Yasumitsu, H.; !1Umeda, M. !$#journal Cancer Res. (1990) 50:7758-7764 !$#title Purification and characterization of extracellular !1matrix-degrading metalloproteinase, matrin (pump-1), !1secreted from human rectal carcinoma cell line. !$#cross-references MUID:91070531; PMID:2253219 !$#accession A60539 !'##molecule_type protein !'##residues 18-35,'X',37-42 ##label MIY REFERENCE S24324 !$#authors Marti, H.P.; McNeil, L.; Thomas, G.; Davies, M.; Lovett, !1D.H. !$#journal Biochem. J. (1992) 285:899-905 !$#title Molecular characterization of a low-molecular-mass matrix !1metalloproteinase secreted by glomerular mesangial cells as !1PUMP-1. !$#cross-references MUID:92359961; PMID:1497627 !$#accession S24324 !'##status preliminary !'##molecule_type DNA !'##residues 1-267 ##label MAR !'##cross-references EMBL:Z11887; NID:g35802; PIDN:CAA77942.1; !1PID:g35803 COMMENT This enzyme is similar in its activity to stromelysin and !1degrades various extracellular matrix proteins, including !1fibronectin, plasminogen, laminin, cartilage proteoglycans, !1and collagens of types II, IV, IX, X, and XI. COMMENT Matrilysin hydrolyzes peptide bonds in plasminogen to yield !1a fragment with angiostatin activity. GENETICS !$#gene GDB:MMP7; MPSL1 !'##cross-references GDB:125751; OMIM:178990 !$#map_position 11q21-11q22 CLASSIFICATION #superfamily matrilysin; matrix metalloproteinase homology KEYWORDS calcium; extracellular matrix; fibroblast; hydrolase; !1metalloproteinase; zinc; zymogen FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-267 #product promatrilysin #status predicted #label PRO\ !$18-94 #domain activation peptide #status predicted #label !8ACT\ !$55-259 #domain matrix metalloproteinase homology #label MMP\ !$85-92 #region autoinhibitory\ !$95-267 #product matrilysin #status predicted #label MAT\ !$87,214,218,224 #binding_site zinc, catalytic (Cys, His, His, His) !8(inhibited) #status predicted\ !$214,218,224 #binding_site zinc, catalytic (His) (active) #status !8predicted\ !$215 #active_site Glu #status predicted SUMMARY #length 267 #molecular-weight 29677 #checksum 4028 SEQUENCE /// ENTRY A28153 #type complete TITLE gelatinase A (EC 3.4.24.24) precursor - human ALTERNATE_NAMES collagenase type IV; matrix metalloproteinase 2 (MMP2); progelatinase A ORGANISM #formal_name Homo sapiens #common_name man DATE 28-Aug-1989 #sequence_revision 07-Jul-1995 #text_change 18-Jun-1999 ACCESSIONS A28153; A34202; A42225; A60187; S13858; S39436; A31480; !1S44432; A61498; S55327; S13953 REFERENCE A28153 !$#authors Collier, I.E.; Wilhelm, S.M.; Eisen, A.Z.; Marmer, B.L.; !1Grant, G.A.; Seltzer, J.L.; Kronberger, A.; He, C.; Bauer, !1E.A.; Goldberg, G.I. !$#journal J. Biol. Chem. (1988) 263:6579-6587 !$#title H-ras oncogene-transformed human bronchial epithelial cells !1(TBE-1) secrete a single metalloprotease capable of !1degrading basement membrane collagen. !$#cross-references MUID:88198218; PMID:2834383 !$#accession A28153 !'##molecule_type mRNA !'##residues 30-660 ##label COL !'##cross-references GB:J03210; NID:g180670; PIDN:AAA35701.1; !1PID:g180671 REFERENCE A34202 !$#authors Huhtala, P.; Eddy, R.L.; Fan, Y.S.; Byers, M.G.; Shows, !1T.B.; Tryggvason, K. !$#journal Genomics (1990) 6:554-559 !$#title Completion of the primary structure of the human type IV !1collagenase preproenzyme and assignment of the gene (CLG4) !1to the q21 region of chromosome 16. !$#cross-references MUID:90228972; PMID:2158484 !$#accession A34202 !'##molecule_type DNA !'##residues 1-51 ##label HU2 !'##cross-references GB:M33789; NID:g180600; PIDN:AAA52027.1; !1PID:g180601 REFERENCE A42225 !$#authors Huhtala, P.; Chow, L.T.; Tryggvason, K. !$#journal J. Biol. Chem. (1990) 265:11077-11082 !$#title Structure of the human type IV collagenase gene. !$#cross-references MUID:90293047; PMID:2162831 !$#accession A42225 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-51;220-393 ##label HUH !'##cross-references GB:M55593; GB:J05471; NID:g180614; PIDN:AAA52028.1; !1PID:g180616 !'##note neither the complete amino acid nor the complete nucleotide !1sequence is given in this paper REFERENCE A60187 !$#authors Frisch, S.M.; Reich, R.; Collier, I.E.; Genrich, L.T.; !1Martin, G.; Goldberg, G.I. !$#journal Oncogene (1990) 5:75-83 !$#title Adenovirus E1A represses protease gene expression and !1inhibits metastasis of human tumor cells. !$#cross-references MUID:90206614; PMID:2157183 !$#accession A60187 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-58 ##label FRI REFERENCE S13858 !$#authors Okada, Y.; Morodomi, T.; Enghild, J.J.; Suzuki, K.; Yasui, !1A.; Nakanishi, I.; Salvesen, G.; Nagase, H. !$#journal Eur. J. Biochem. (1990) 194:721-730 !$#title Matrix metalloproteinase 2 from human rheumatoid synovial !1fibroblasts. Purification and activation of the precursor !1and enzymic properties. !$#cross-references MUID:91099351; PMID:2269296 !$#accession S13858 !'##molecule_type protein !'##residues 30-45;110-124 ##label OKA REFERENCE S39436 !$#authors Crabbe, T.; Ioannou, C.; Docherty, A.J.P. !$#journal Eur. J. Biochem. (1993) 218:431-438 !$#title Human progelatinase A can be activated by autolysis at a !1rate that is concentration-dependent and enhanced by heparin !1bound to the C-terminal domain. !$#cross-references MUID:94094834; PMID:8269931 !$#accession S39436 !'##molecule_type protein !'##residues 30-44;444-456 ##label CR2 REFERENCE A31480 !$#authors Stetler-Stevenson, W.G.; Krutzsch, H.C.; Wacher, M.P.; !1Margulies, I.M.K.; Liotta, L.A. !$#journal J. Biol. Chem. (1989) 264:1353-1356 !$#title The activation of human type IV collagenase proenzyme. !1Sequence identification of the major conversion product !1following organomercurial activation. !$#cross-references MUID:89109136; PMID:2536363 !$#accession A31480 !'##molecule_type protein !'##residues 110-123 ##label STE REFERENCE S44432 !$#authors Crabbe, T.; Smith, B.; O'Connell, J.; Docherty, A. !$#journal FEBS Lett. (1994) 345:14-16 !$#title Human progelatinase A can be activated by matrilysin. !$#cross-references MUID:94252395; PMID:8194591 !$#accession S44432 !'##molecule_type protein !'##residues 110-115 ##label CRA REFERENCE A61498 !$#authors Brown, D.; Chwa, M.; Escobar, M.; Kenney, M.C. !$#journal Exp. Eye Res. (1991) 52:5-16 !$#title Characterization of the major matrix degrading !1metalloproteinase of human corneal stroma. Evidence for an !1enzyme/inhibitor complex. !$#cross-references MUID:91330998; PMID:1868885 !$#accession A61498 !'##molecule_type protein !'##residues 'X',31,'X',33-46,'X',48-50,'Q' ##label BRO !'##experimental_source corneal stroma REFERENCE S55327 !$#authors Itoh, Y.; Binner, S.; Nagase, H. !$#journal Biochem. J. (1995) 308:645-651 !$#title Steps involved in activation of the complex of pro-matrix !1metalloproteinase 2 (progelatinase A) and tissue inhibitor !1of metalloproteinases (TIMP)-2 by 4-aminophenylmercuric !1acetate. !$#cross-references MUID:95290003; PMID:7772054 !$#accession S55327 !'##molecule_type protein !'##residues 110-114 ##label ITO GENETICS !$#gene GDB:MMP2; CLG4; CLG4A !'##cross-references GDB:120592; OMIM:120360 !$#map_position 16q13-16q13 !$#introns 51/3; 127/2; 178/1; 220/1; 278/1; 336/1; 394/1; 446/1; 491/ !12; 537/1; 590/2; 627/1 FUNCTION !$#description proteolytic cleavage of gelatin type I and collagen types !1IV, V, VII, and X CLASSIFICATION #superfamily gelatinase A; fibronectin type II repeat !1homology; hemopexin repeat homology; matrix !1metalloproteinase homology KEYWORDS extracellular matrix; fibroblast; glycoprotein; hydrolase; !1metalloproteinase; zinc; zymogen FEATURE !$1-29 #domain signal sequence #status predicted #label SIG\ !$30-660 #product progelatinase A #status predicted #label !8PRO\ !$30-109 #domain activation peptide #status predicted #label !8ACT\ !$70-219,394-446 #domain matrix metalloproteinase homology #status !8atypical #label MMP\ !$110-660 #product gelatinase A #status predicted #label MAT\ !$233-390 #region collagen binding #status predicted\ !$233-274 #domain fibronectin type II repeat homology #label !82F1\ !$291-332 #domain fibronectin type II repeat homology #label !82F8\ !$349-390 #domain fibronectin type II repeat homology #label !82F9\ !$463-660 #domain hemopexin repeat homology #label PXN\ !$102,403,407,413 #binding_site zinc, catalytic (Cys, His, His, His) !8(inhibited) #status predicted\ !$403,407,413 #binding_site zinc, catalytic (His) (active) #status !8predicted\ !$404 #active_site Glu #status predicted\ !$469-660 #disulfide_bonds #status predicted\ !$573,642 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 660 #molecular-weight 73882 #checksum 9220 SEQUENCE /// ENTRY S46492 #type complete TITLE gelatinase A (EC 3.4.24.24) precursor - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S46492 REFERENCE S46492 !$#authors Aimes, R.T.; French, D.L.; Quigley, J.P. !$#journal Biochem. J. (1994) 300:729-736 !$#title Cloning of a 72 kDa matrix metalloproteinase (gelatinase) !1from chicken embryo fibroblasts using gene family PCR: !1expression of the gelatinase increases upon malignant !1transformation. !$#cross-references MUID:94280397; PMID:8010954 !$#accession S46492 !'##status preliminary !'##molecule_type mRNA !'##residues 1-663 ##label AIM !'##cross-references EMBL:U07775; NID:g504475; PIDN:AAA19596.1; !1PID:g504476 !'##note in the authors' translation 205-Asp is shown after residue 201 !1and, consequently, residues 202-204 are displaced one codon !1to the right CLASSIFICATION #superfamily gelatinase A; fibronectin type II repeat !1homology; hemopexin repeat homology; matrix !1metalloproteinase homology KEYWORDS hydrolase; metalloproteinase; zinc; zymogen FEATURE !$67-216,391-443 #domain matrix metalloproteinase homology #status !8atypical #label MMP\ !$230-271 #domain fibronectin type II repeat homology #label !82F1\ !$288-329 #domain fibronectin type II repeat homology #label !82F8\ !$346-387 #domain fibronectin type II repeat homology #label !82F9\ !$466-663 #domain hemopexin repeat homology #label PXN\ !$99,400,404,410 #binding_site zinc, catalytic (Cys, His, His, His) !8(inhibited) #status predicted\ !$400,404,410 #binding_site zinc, catalytic (His) (active) #status !8predicted\ !$401 #active_site Glu #status predicted SUMMARY #length 663 #molecular-weight 74941 #checksum 837 SEQUENCE /// ENTRY I46031 #type complete TITLE gelatinase B (EC 3.4.24.35) - bovine ALTERNATE_NAMES matrix metalloproteinase 9 (MMP9) ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS I46031; S43112 REFERENCE I46031 !$#authors Baylis, H.A.; Megson, A.; Hall, R. !$#journal Mol. Biochem. Parasitol. (1995) 69:211-222 !$#title Infection with Theileria annulata induces expression of !1matrix metalloproteinase 9 and transcription factor AP-1 in !1bovine leucocytes. !$#cross-references MUID:95287902; PMID:7770085 !$#accession I46031 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-712 ##label BAY !'##cross-references EMBL:X78324; NID:g467620; PIDN:CAA55127.1; !1PID:g467621 !'##note submitted to the EMBL Data Library, March 1994 GENETICS !$#gene mmp9 CLASSIFICATION #superfamily gelatinase A; fibronectin type II repeat !1homology; hemopexin repeat homology; matrix !1metalloproteinase homology KEYWORDS hydrolase; metalloproteinase; zinc; zymogen FEATURE !$67-216,392-444 #domain matrix metalloproteinase homology #status !8atypical #label MMP\ !$230-271 #domain fibronectin type II repeat homology #label !82F1\ !$288-329 #domain fibronectin type II repeat homology #label !82F2\ !$347-388 #domain fibronectin type II repeat homology #label !82F3\ !$515-709 #domain hemopexin repeat homology #label PXN\ !$99,401,405,411 #binding_site zinc, catalytic (Cys, His, His, His) !8(inhibited) #status predicted\ !$401,405,411 #binding_site zinc, catalytic (His) (active) #status !8predicted\ !$402 #active_site Glu #status predicted SUMMARY #length 712 #molecular-weight 79087 #checksum 5624 SEQUENCE /// ENTRY A53796 #type complete TITLE gelatinase B (EC 3.4.24.35) precursor - rabbit ALTERNATE_NAMES 92K matrix metalloproteinase; 92K type IV collagenase; matrix metalloproteinase 9 (MMP9) ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A53796; A55398 REFERENCE A53796 !$#authors Tezuka, K.; Nemoto, K.; Tezuka, Y.; Sato, T.; Ikeda, Y.; !1Kobori, M.; Kawashima, H.; Eguchi, H.; Hakeda, Y.; Kumegawa, !1M. !$#journal J. Biol. Chem. (1994) 269:15006-15009 !$#title Identification of matrix metalloproteinase 9 in rabbit !1osteoclasts. !$#cross-references MUID:94253056; PMID:8195136 !$#accession A53796 !'##molecule_type mRNA !'##residues 1-707 ##label TEZ !'##cross-references GB:D26514; NID:g499372; PIDN:BAA05520.1; !1PID:g499373 !'##experimental_source osteoclasts REFERENCE A55398 !$#authors Fini, M.E.; Bartlett, J.D.; Matsubara, M.; Rinehart, W.B.; !1Mody, M.K.; Girard, M.T.; Rainville, M. !$#journal J. Biol. Chem. (1994) 269:28620-28628 !$#title The rabbit gene for 92-kDa matrix metalloproteinase. Role of !1AP1 and AP2 in cell type-specific transcription. !$#cross-references MUID:95050662; PMID:7961810 !$#accession A55398 !'##status translation not shown !'##molecule_type DNA !'##residues 1-75,'P',77-99,'ASR',103-171 ##label FIN !'##cross-references GB:L36050; NID:g535714; PIDN:AAA64358.1; !1PID:g535715 GENETICS !$#introns 46/3; 124/2 CLASSIFICATION #superfamily gelatinase A; fibronectin type II repeat !1homology; hemopexin repeat homology; matrix !1metalloproteinase homology KEYWORDS glycoprotein; hydrolase; metalloproteinase; zinc; zymogen FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-106 #domain activation peptide #status predicted #label !8PRO\ !$107-707 #product 91K neutrophil gelatinase B #status !8predicted #label MAT\ !$230-271 #domain fibronectin type II repeat homology #label !82F9\ !$288-329 #domain fibronectin type II repeat homology #label !82F8\ !$347-388 #domain fibronectin type II repeat homology #label !82F1\ !$510-704 #domain hemopexin repeat homology #label PXN\ !$88,120,127 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$99,401,405,411 #binding_site zinc, catalytic (Cys, His, His, His) !8(inhibited) #status predicted\ !$401,405,411 #binding_site zinc, catalytic (His) (active) #status !8predicted\ !$402 #active_site Glu #status predicted SUMMARY #length 707 #molecular-weight 78307 #checksum 4186 SEQUENCE /// ENTRY A34458 #type complete TITLE gelatinase B (EC 3.4.24.35) precursor - human ALTERNATE_NAMES 92K gelatinase; 92K type IV collagenase; matrix metalloproteinase 9 (MMP9) CONTAINS 91K neutrophil gelatinase B ORGANISM #formal_name Homo sapiens #common_name man DATE 03-Aug-1992 #sequence_revision 07-Apr-1994 #text_change 18-Jun-1999 ACCESSIONS A34458; A41166; A42253; A45114; B45114; B48417; A61385; !1S16097; S59488 REFERENCE A34458 !$#authors Wilhelm, S.M.; Collier, I.E.; Marmer, B.L.; Eisen, A.Z.; !1Grant, G.A.; Goldberg, G.I. !$#journal J. Biol. Chem. (1989) 264:17213-17221 !$#title SV40-transformed human lung fibroblasts secrete a 92-kDa !1type IV collagenase which is identical to that secreted by !1normal human macrophages. !$#cross-references MUID:90008879; PMID:2551898 !$#accession A34458 !'##molecule_type mRNA !'##residues 1-11,'L',13-667,'R',669-707 ##label WIL !'##cross-references GB:J05070; NID:g177204; PIDN:AAA51539.1; !1PID:g177205 REFERENCE A41166 !$#authors Huhtala, P.; Tuuttila, A.; Chow, L.T.; Lohi, J.; Keski-Oja, !1J.; Tryggvason, K. !$#journal J. Biol. Chem. (1991) 266:16485-16490 !$#title Complete structure of the human gene for 92-kDa type IV !1collagenase. Divergent regulation of expression for the 92- !1and 72-kilodalton enzyme genes in HT-1080 cells. !$#cross-references MUID:91358433; PMID:1653238 !$#accession A41166 !'##molecule_type DNA !'##residues !11-49;121-127;171-177;214-220;272-278;330-336;389-395; !1439-542;582-587;631-637;666-672;705-707 ##label HUH !'##cross-references GB:M68343; GB:M68344; GB:M68345; GB:M68346; !1GB:M68347; GB:M68348; GB:M68349; GB:M68350; GB:M68351; !1GB:M68352; GB:M68353; GB:M68354; GB:M68355; GB:D10051 !'##note the authors translated the codon CTC for residue 276 as Lys REFERENCE A42253 !$#authors Ogata, Y.; Enghild, J.J.; Nagase, H. !$#journal J. Biol. Chem. (1992) 267:3581-3584 !$#title Matrix metalloproteinase 3 (stromelysin) activates the !1precursor for the human matrix metalloproteinase 9. !$#cross-references MUID:92156083; PMID:1371271 !$#accession A42253 !'##molecule_type protein !'##residues 20-34;60-71;107-118 ##label OGA REFERENCE A45114 !$#authors Okada, Y.; Gonoji, Y.; Naka, K.; Tomita, K.; Nakanishi, I.; !1Iwata, K.; Yamashita, K.; Hayakawa, T. !$#journal J. Biol. Chem. (1992) 267:21712-21719 !$#title Matrix metalloproteinase 9 (92-kDa gelatinase/type IV !1collagenase) from HT 1080 human fibrosarcoma cells. !1Purification and activation of the precursor and enzymic !1properties. !$#cross-references MUID:93016125; PMID:1400481 !$#accession A45114 !'##molecule_type protein !'##residues 20-32 ##label OKA !'##experimental_source HT 1080 fibrosarcoma cells !'##note sequence extracted from NCBI backbone (NCBIP:119576) !$#accession B45114 !'##molecule_type protein !'##residues 94-111 ##label OK2 !'##experimental_source HT 1080 fibrosarcoma cells !'##note sequence extracted from NCBI backbone (NCBIP:116742) !'##note amino ends of the proenzyme and two activated forms REFERENCE A48417 !$#authors Van Ranst, M.; Norga, K.; Masure, S.; Proost, P.; !1Vandekerckhove, F.; Auwerx, J.; Van Damme, J.; Opdenakker, !1G. !$#journal Cytokine (1991) 3:231-239 !$#title The cytokine-protease connection: identification of a 96-kD !1THP-1 gelatinase and regulation by interleukin-1 and !1cytokine inducers. !$#cross-references MUID:91355647; PMID:1653055 !$#accession B48417 !'##molecule_type protein !'##residues 20-25,'X',27-37 ##label VAN !'##experimental_source monocytic cell line THP-1 !'##note sequence extracted from NCBI backbone (NCBIP:63812) and !1corrected to correspond with the published sequence REFERENCE A61385 !$#authors Opdenakker, G.; Masure, S.; Grillet, B.; Van Damme, J. !$#journal Lymphokine Cytokine Res. (1991) 10:317-324 !$#title Cytokine-mediated regulation of human leukocyte gelatinases !1and role in arthritis. !$#cross-references MUID:92032113; PMID:1932376 !$#accession A61385 !'##molecule_type protein !'##residues 28-37 ##label OPD REFERENCE S16097 !$#authors Masure, S.; Proost, P.; van Damme, J.; Opdenakker, G. !$#journal Eur. J. Biochem. (1991) 198:391-398 !$#title Purification and identification of 91-kDa neutrophil !1gelatinase. Release by the activating peptide interleukin-8. !$#cross-references MUID:91249834; PMID:1645657 !$#accession S16097 !'##molecule_type protein !'##residues 28-42,'X',44-60,'XX',63 ##label MAS REFERENCE S59488 !$#authors Sang, Q.X.; Birkedal-Hansen, H.; van Wart, H.E. !$#journal Biochim. Biophys. Acta (1995) 1251:99-108 !$#title Proteolytic and non-proteolytic activation of human !1neutrophil progelatinase B. !$#cross-references MUID:95399447; PMID:7669817 !$#accession S59488 !'##molecule_type protein !'##residues 20-27;60-67;94-98,'X',100-101;107-114 ##label SAN COMMENT Gelatinase B hydrolyzes peptide bonds in plasminogen to !1yield a fragment with angiostatin activity. GENETICS !$#gene GDB:MMP9; CLG4B !'##cross-references GDB:125224; OMIM:120361 !$#map_position 20q12-20q13 !$#introns 46/3; 124/2; 174/1; 217/1; 275/1; 333/1; 392/1; 444/1; 537/ !12; 584/1; 634/2; 669/1 FUNCTION !$#description hydrolyzes type IV collagen CLASSIFICATION #superfamily gelatinase A; fibronectin type II repeat !1homology; hemopexin repeat homology; matrix !1metalloproteinase homology KEYWORDS glycoprotein; hydrolase; metalloproteinase; zinc; zymogen FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-707 #product gelatinase B proenzyme #status predicted !8#label PRE\ !$20-106 #domain activation peptide #status experimental !8#label PRO\ !$28-707 #product 91K neutrophil gelatinase B proenzyme !8#status predicted #label PR2\ !$107-707 #product 91K neutrophil gelatinase B #status !8predicted #label MAT\ !$230-271 #domain fibronectin type II repeat homology #label !82F9\ !$288-329 #domain fibronectin type II repeat homology #label !82F8\ !$347-388 #domain fibronectin type II repeat homology #label !82F1\ !$445-497 #region proline-rich\ !$509-704 #domain hemopexin repeat homology #label PXN\ !$38,120,127 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$99,401,405,411 #binding_site zinc, catalytic (Cys, His, His, His) !8(inhibited) #status predicted\ !$401,405,411 #binding_site zinc, catalytic (His) (active) #status !8predicted\ !$402 #active_site Glu #status predicted SUMMARY #length 707 #molecular-weight 78384 #checksum 9255 SEQUENCE /// ENTRY I52580 #type complete TITLE gelatinase B (EC 3.4.24.35) precursor - mouse ALTERNATE_NAMES collagenase type IV ORGANISM #formal_name Mus sp. #common_name mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS I52580 REFERENCE I52580 !$#authors Graubert, T.; Johnston, J.; Berliner, N. !$#journal Blood (1993) 82:3192-3197 !$#title Cloning and expression of the cDNA encoding mouse neutrophil !1gelatinase: demonstration of coordinate secondary granule !1protein gene expression during terminal neutrophil !1maturation. !$#cross-references MUID:94033534; PMID:8219207 !$#accession I52580 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-730 ##label RES !'##cross-references GB:S67830; NID:g460863; PIDN:AAB28942.1; !1PID:g460864 CLASSIFICATION #superfamily gelatinase A; fibronectin type II repeat !1homology; hemopexin repeat homology; matrix !1metalloproteinase homology KEYWORDS hydrolase; metalloproteinase; zinc; zymogen FEATURE !$230-271 #domain fibronectin type II repeat homology #label !82F1\ !$288-329 #domain fibronectin type II repeat homology #label !82F2\ !$347-388 #domain fibronectin type II repeat homology #label !82F3\ !$529-729 #domain hemopexin repeat homology #label PXN\ !$100,401,405,411 #binding_site zinc, catalytic (Cys, His, His, His) !8(inhibited) #status predicted\ !$401,405,411 #binding_site zinc, catalytic (His) (active) #status !8predicted\ !$402 #active_site Glu #status predicted SUMMARY #length 730 #molecular-weight 80468 #checksum 2890 SEQUENCE /// ENTRY HYHUN #type complete TITLE neprilysin (EC 3.4.24.11) [validated] - human ALTERNATE_NAMES CD10; common acute lymphocytic leukemia antigen; endopeptidase 24.11; enkephalinase; kidney-brush-border neutral peptidase; neutral endopeptidase ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 08-Dec-2000 ACCESSIONS A41387; A36173; S05275; JL0084; S00350; S02228 REFERENCE A41387 !$#authors D'Adamio, L.; Shipp, M.A.; Masteller, E.L.; Reinherz, E.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:7103-7107 !$#title Organization of the gene encoding common acute lymphoblastic !1leukemia antigen (neutral endopeptidase 24.11): multiple !1miniexons and separate 5' untranslated regions. !$#cross-references MUID:89386688; PMID:2528730 !$#accession A41387 !'##molecule_type DNA !'##residues 1-750 ##label DAA !'##cross-references GB:M26605 !'##note the authors translated the codon AAC for residues 14 and 72 as !1Asp REFERENCE A36173 !$#authors Shipp, M.A.; Richardson, N.E.; Sayre, P.H.; Brown, N.R.; !1Masteller, E.L.; Clayton, L.K.; Ritz, J.; Reinherz, E.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:4819-4823 !$#title Molecular cloning of the common acute lymphoblastic leukemia !1antigen (CALLA) identifies a type II integral membrane !1protein. !$#cross-references MUID:88263038; PMID:2968607 !$#accession A36173 !'##molecule_type mRNA !'##residues 1-750 ##label SHI !'##cross-references GB:J03779 !'##note part of this sequence was confirmed by protein sequencing REFERENCE S05275 !$#authors Jongeneel, C.V. !$#submission submitted to the EMBL Data Library, August 1988 !$#accession S05275 !'##molecule_type mRNA !'##residues 1-750 ##label JON !'##cross-references EMBL:Y00811; NID:g29625; PIDN:CAA68752.1; !1PID:g29626 REFERENCE JL0084 !$#authors Letarte, M.; Vera, S.; Tran, R.; Addis, J.B.L.; Onizuka, !1R.J.; Quackenbush, E.J.; Jongeneel, C.V.; McInnes, R.R. !$#journal J. Exp. Med. (1988) 168:1247-1253 !$#title Common acute lymphocytic leukemia antigen is identical to !1neutral endopeptidase. !$#cross-references MUID:89010526; PMID:2971756 !$#accession JL0084 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 2-191;211-737 ##label LET !'##cross-references EMBL:Y00811 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE S00350 !$#authors Malfroy, B.; Kuang, W.J.; Seeburg, P.H.; Mason, A.J.; !1Schofield, P.R. !$#journal FEBS Lett. (1988) 229:206-210 !$#title Molecular cloning and amino acid sequence of human !1enkephalinase (neutral endopeptidase). !$#cross-references MUID:88152222; PMID:3162217 !$#accession S00350 !'##molecule_type mRNA !'##residues 3-750 ##label MAL !'##cross-references EMBL:X07166 !'##note 467-Thr was also found COMMENT This enzyme inactivates a variety of peptide hormones, !1cleaving on the amino side of hydrophobic residues. Although !1widely distributed in animal tissues, it is particularly !1abundant in kidney. COMMENT This antigen is an important cell surface marker !1glycoprotein in the diagnosis of human lymphocytic leukemia. GENETICS !$#gene GDB:MME !'##cross-references GDB:120190; OMIM:120520 !$#map_position 3q25.1-3q25.2 !$#introns 54/1; 66/1; 120/1; 147/1; 179/1; 218/3; 240/3; 285/3; 319/3; !1365/2; 396/3; 439/3; 472/3; 499/3; 534/2; 554/1; 594/1; 638/ !13; 660/3; 692/3; 718/2 CLASSIFICATION #superfamily neprilysin KEYWORDS glycoprotein; hydrolase; metalloproteinase; oligopeptidase; !1surface antigen; transmembrane protein; zinc FEATURE !$2-750 #product neprilysin #status experimental #label MAT\ !$16-23 #region stop-transfer sequence\ !$29-51 #domain transmembrane #status predicted #label TMN\ !$52-750 #domain extracellular #status predicted #label EXT\ !$145,285,311,325, !$335,628 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$584,588 #binding_site zinc (His) #status predicted\ !$585 #active_site Glu #status predicted SUMMARY #length 750 #molecular-weight 85513 #checksum 1829 SEQUENCE /// ENTRY HYRTN #type complete TITLE neprilysin (EC 3.4.24.11) - rat ALTERNATE_NAMES CD10; common acute lymphocytic leukemia antigen; endopeptidase 24.11; enkephalinase; kidney-brush-border neutral peptidase; neutral endopeptidase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS A29295; A33521 REFERENCE A29295 !$#authors Malfroy, B.; Schofield, P.R.; Kuang, W.J.; Seeburg, P.H.; !1Mason, A.J.; Henzel, W.J. !$#journal Biochem. Biophys. Res. Commun. (1987) 144:59-66 !$#title Molecular cloning and amino acid sequence of rat !1enkephalinase. !$#cross-references MUID:87213218; PMID:3555489 !$#accession A29295 !'##molecule_type mRNA !'##residues 1-750 ##label MAL !'##cross-references GB:M15944; NID:g204031; PIDN:AAA41116.1; !1PID:g204032 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE A33521 !$#authors Bateman Jr., R.C.; Jackson, D.; Slaughter, C.A.; Unnithan, !1S.; Chai, Y.G.; Moomaw, C.; Hersh, L.B. !$#journal J. Biol. Chem. (1989) 264:6151-6157 !$#title Identification of the active-site arginine in rat neutral !1endopeptidase 24.11 (enkephalinase) as arginine 102 and !1analysis of a glutamine 102 mutant. !$#cross-references MUID:89197908; PMID:2703483 !$#accession A33521 !'##molecule_type protein !'##residues 95-102,'X',104-129 ##label BAT COMMENT This enzyme inactivates a variety of peptide hormones, !1cleaving on the amino side of hydrophobic residues. Although !1widely distributed in animal tissues, it is particularly !1abundant in kidney. CLASSIFICATION #superfamily neprilysin KEYWORDS glycoprotein; hydrolase; metalloproteinase; oligopeptidase; !1surface antigen; transmembrane protein; zinc FEATURE !$9-750 #product neprilysin #status experimental #label MAT\ !$16-23 #region stop-transfer sequence\ !$29-51 #domain transmembrane #status predicted #label TMN\ !$52-750 #domain extracellular #status predicted #label EXT\ !$145,285,325,628 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$311 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$584,588 #binding_site zinc (His) #status predicted\ !$585 #active_site Glu #status predicted SUMMARY #length 750 #molecular-weight 85794 #checksum 2668 SEQUENCE /// ENTRY HYRBN #type complete TITLE neprilysin (EC 3.4.24.11) - rabbit ALTERNATE_NAMES CD10; common acute lymphocytic leukemia antigen; endopeptidase 24.11; enkephalinase; kidney-brush-border neutral peptidase; neutral endopeptidase ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS A29451; I46872 REFERENCE A29451 !$#authors Devault, A.; Lazure, C.; Nault, C.; Le Moual, H.; Seidah, !1N.G.; Chretien, M.; Kahn, P.; Powell, J.; Mallet, J.; !1Beaumont, A.; Roques, B.P.; Crine, P.; Boileau, G. !$#journal EMBO J. (1987) 6:1317-1322 !$#title Amino acid sequence of rabbit kidney neutral endopeptidase !124.11 (enkephalinase) deduced from a complementary DNA. !$#cross-references MUID:87275825; PMID:2440677 !$#accession A29451 !'##molecule_type mRNA !'##residues 1-751 ##label DEV !'##cross-references EMBL:X05338 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE I46872 !$#authors Kahn, P.H.; Powell, J.F.; Beaumont, A.; Roques, B.P.; !1Mallet, J.J. !$#journal Biochem. Biophys. Res. Commun. (1987) 145:488-493 !$#title An antibody purified with a lambda GT11 fusion protein !1precipitates enkephalinase activity. !$#cross-references MUID:87241544; PMID:3297057 !$#accession I46872 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 207-275 ##label KAH !'##cross-references GB:M16593; NID:g165556; PIDN:AAA53694.1; !1PID:g165557 COMMENT This enzyme inactivates a variety of peptide hormones, !1cleaving on the amino side of hydrophobic residues. Although !1widely distributed in animal tissues, it is particularly !1abundant in kidney. CLASSIFICATION #superfamily neprilysin KEYWORDS glycoprotein; hydrolase; metalloproteinase; oligopeptidase; !1surface antigen; transmembrane protein; zinc FEATURE !$2-751 #product neprilysin #status experimental #label MAT\ !$16-23 #region stop-transfer sequence\ !$29-51 #domain transmembrane #status predicted #label TMN\ !$52-751 #domain extracellular #status predicted #label EXT\ !$145,286,312,326 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$585,589 #binding_site zinc (His) #status predicted\ !$586 #active_site Glu #status predicted\ !$629 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 751 #molecular-weight 85680 #checksum 4388 SEQUENCE /// ENTRY HYHUK #type complete TITLE Kell blood group protein (EC 3.4.24.-) - human ALTERNATE_NAMES Kell immunogen ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS A41127; I52609; I52602 REFERENCE A41127 !$#authors Lee, S.; Zambas, E.D.; Marsh, W.L.; Redman, C.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:6353-6357 !$#title Molecular cloning and primary structure of Kell blood group !1protein. !$#cross-references MUID:91296819; PMID:1712490 !$#accession A41127 !'##molecule_type mRNA !'##residues 1-732 ##label LEE !'##cross-references GB:M64934 REFERENCE I52609 !$#authors Lee, S.; Wu, X.; Reid, M.; Zelinski, T.; Redman, C. !$#journal Blood (1995) 85:912-916 !$#title Molecular basis of the Kell (K1) phenotype. !$#cross-references MUID:95152068; PMID:7849312 !$#accession I52609 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 185-192,'M',194-199 ##label RES !'##cross-references GB:S76770; NID:g914223; PIDN:AAB33389.1; !1PID:g914224 !'##note allele K1 REFERENCE I52602 !$#authors Lee, S.; Zambas, E.; Green, E.D.; Redman, C. !$#journal Blood (1995) 85:1364-1370 !$#title Organization of the gene encoding the human Kell blood group !1protein. !$#cross-references MUID:95161764; PMID:7858266 !$#accession I52602 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 'S',2-56,'L',58-732 ##label RE2 !'##cross-references GB:S76819; NID:g912984; PIDN:AAB33459.1; !1PID:g912985 COMMENT This glycoprotein carries the Kell blood group antigens. It !1is probably a zinc metalloendopeptidase. GENETICS !$#gene GDB:KEL !'##cross-references GDB:118742; OMIM:110900 !$#map_position 7q33-7q33 !$#introns 27/3; 75/1; 134/1; 175/3; 224/3; 245/3; 308/3; 358/2; 401/3; !1438/3; 471/3; 497/3; 531/2; 568/2; 591/1; 647/3; 679/3 CLASSIFICATION #superfamily neprilysin KEYWORDS erythrocyte; glycoprotein; hydrolase; metalloproteinase; !1surface antigen; transmembrane protein; zinc FEATURE !$2-732 #product Kell blood group protein #status predicted !8#label MAT\ !$48-67 #domain transmembrane #status predicted #label TMN\ !$69-732 #domain extracellular #status predicted #label EXT\ !$94,115,191,345,627, !$724 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$581,585 #binding_site zinc (His) #status predicted\ !$582 #active_site Glu #status predicted SUMMARY #length 732 #molecular-weight 82807 #checksum 9733 SEQUENCE /// ENTRY HYHUTH #type complete TITLE thimet oligopeptidase (EC 3.4.24.15) - human ALTERNATE_NAMES beta-amyloid precursor protein processing metalloproteinase; metalloendopeptidase; MP78 ORGANISM #formal_name Homo sapiens #common_name man DATE 27-Sep-1995 #sequence_revision 17-Nov-1995 #text_change 18-Jun-1999 ACCESSIONS JC4197; PC4053; G01881; G01882; A53633 REFERENCE JC4197 !$#authors Thompson, A.; Huber, G.; Malherbe, P. !$#journal Biochem. Biophys. Res. Commun. (1995) 213:66-73 !$#title Cloning and functional expression of a metalloendopeptidase !1from human brain with the ability to cleave a beta-APP !1substrate peptide. !$#cross-references MUID:95367027; PMID:7639763 !$#accession JC4197 !'##molecule_type mRNA !'##residues 1-689 ##label THO1 !'##cross-references GB:Z50115; NID:g1030054; PIDN:CAA90477.1; !1PID:g1030055 !'##experimental_source brain !$#accession PC4053 !'##molecule_type protein !'##residues 67-78;181-200 ##label THO2 REFERENCE H00694 !$#authors Munroe, D.G. !$#submission submitted to the EMBL Data Library, June 1995 !$#accession G01881 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-689 ##label MUN1 !'##cross-references EMBL:U29366; NID:g1098599; PIDN:AAA82607.1; !1PID:g1098600 REFERENCE H00695 !$#authors Munroe, D.G. !$#submission submitted to the EMBL Data Library, June 1995 !$#accession G01882 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-5 ##label MUN2 !'##cross-references EMBL:U29367; NID:g1098597; PIDN:AAA82606.1; !1PID:g1098598 REFERENCE A53633 !$#authors Papastoitsis, G.; Siman, R.; Scott, R.; Abraham, C.R. !$#journal Biochemistry (1994) 33:192-199 !$#title Identification of a metalloprotease from Alzheimer's disease !1brain able to degrade the beta-amyloid precursor protein and !1generate amyloidogenic fragments. !$#cross-references MUID:94114484; PMID:8286339 !$#accession A53633 !'##molecule_type protein !'##residues 67-78;181-197,'X',199-200 ##label PAP !'##experimental_source brain of Alzheimer's disease patient !'##note sequence modified after extraction from NCBI backbone COMMENT This metalloproteinase is responsible for cleaving a Met-Asp !1bond in the Alzheimer's disease amyloid beta protein !1precursor (see PIR:QRHUA4) that yields the beta protein !1found in senile plaques. GENETICS !$#gene GDB:THOP1; GDB:ME78 !'##cross-references GDB:595011; GDB:642232; OMIM:601117 !$#map_position 19q13.3-19q13.3 FUNCTION !$#description endopeptidase preferentially hydrolyzing peptide bonds on !1the carboxyl side of hydrophobic residues (P1 and P2) and !1the amino side of small residues (P1') CLASSIFICATION #superfamily thimet oligopeptidase KEYWORDS Alzheimer's disease; amyloid; brain; glycoprotein; !1hydrolase; metalloproteinase; zinc FEATURE !$2-689 #product thimet oligopeptidase #status predicted !8#label MAT\ !$451 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$473,477,480 #binding_site zinc (His) #status predicted\ !$474 #active_site Glu #status predicted SUMMARY #length 689 #molecular-weight 78839 #checksum 8409 SEQUENCE /// ENTRY HYRTTH #type complete TITLE thimet oligopeptidase (EC 3.4.24.15) - rat ALTERNATE_NAMES endo-oligopeptidase A; endopeptidase 24.15; Pz-peptidase; soluble metalloendopeptidase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1992 #sequence_revision 17-Nov-1995 #text_change 07-May-1999 ACCESSIONS S38760; A54152; S55999; A36165 REFERENCE S38760 !$#authors McKie, N.; Dando, P.M.; Rawlings, N.D.; Barrett, A.J. !$#journal Biochem. J. (1993) 295:57-60 !$#title Thimet oligopeptidase: similarity to 'soluble angiotensin !1II-binding protein' and some corrections to the published !1amino acid sequence of the rat testis enzyme. !$#cross-references MUID:94029935; PMID:8216239 !$#accession S38760 !'##molecule_type mRNA !'##residues 1-687 ##label MCK REFERENCE A54152 !$#authors Pierotti, A.; Dong, K.W.; Glucksman, M.J.; Orlowski, M.; !1Roberts, J.L. !$#journal Biochemistry (1994) 33:622 !$#cross-references MUID:94114549; PMID:8286394 !$#contents corrections !$#accession A54152 !'##molecule_type mRNA !'##residues 320-350;578-597,'F',599-687 ##label PIE !'##experimental_source testis !'##note sequence extracted from NCBI backbone (NCBIN:142522, !1NCBIN:142524, NCBIP:142525, NCBIP:142527) and corrected to !1correspond with the published sequences !'##note this report is a correction to A36165 REFERENCE S55999 !$#authors McKie, N.; Dando, P.M.; Brown, M.A.; Barrett, A.J. !$#journal Biochem. J. (1995) 309:203-207 !$#title Rat thimet oligopeptidase: large-scale expression in !1Escherichia coli and characterization of the recombinant !1enzyme. !$#cross-references MUID:95344370; PMID:7619057 !$#accession S55999 !'##molecule_type protein !'##residues 1-9 ##label MC2 !'##note this is an engineered sequence expressed in Escherichia coli REFERENCE A36165 !$#authors Pierotti, A.; Dong, K.W.; Glucksman, M.J.; Orlowski, M.; !1Roberts, J.L. !$#journal Biochemistry (1990) 29:10323-10329 !$#title Molecular cloning and primary structure of rat testes !1metalloendopeptidase EC 3.4.24.15. !$#cross-references MUID:91084500; PMID:2261476 !$#accession A36165 !'##status significant sequence differences !'##molecule_type mRNA !'##cross-references GB:M61142 !'##note parts of this sequence, including the amino end of the mature !1protein, were confirmed by protein sequencing COMMENT This enzyme is found in testes, brain, and pituitary !1predominantly in a soluble form. A membrane-bound form !1accounts for about 20% of activity. FUNCTION !$#description hydrolyzes peptide bonds on the carboxyl side of hydrophobic !1residues in peptides of 20 or fewer amino acids CLASSIFICATION #superfamily thimet oligopeptidase KEYWORDS hydrolase; metalloproteinase; oligopeptidase; zinc FEATURE !$2-687 #product thimet oligopeptidase #status predicted !8#label MAT\ !$473,477,480 #binding_site zinc (His) #status predicted\ !$474 #active_site Glu #status predicted SUMMARY #length 687 #molecular-weight 78308 #checksum 8346 SEQUENCE /// ENTRY A46273 #type complete TITLE mitochondrial intermediate peptidase (EC 3.4.24.-) - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 21-Sep-1993 #sequence_revision 14-Jul-1994 #text_change 08-Dec-2000 ACCESSIONS A46273; S23380 REFERENCE A46273 !$#authors Isaya, G.; Kalousek, F.; Rosenberg, L.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:8317-8321 !$#title Sequence analysis of rat mitochondrial intermediate !1peptidase: similarity to zinc metallopeptidases and to a !1putative yeast homologue. !$#cross-references MUID:92390438; PMID:1518864 !$#accession A46273 !'##molecule_type mRNA !'##residues 1-710 ##label ISA !'##cross-references GB:M96633; NID:g206271; PIDN:AAA41899.1; !1PID:g206272 !'##experimental_source liver !'##note sequence extracted from NCBI backbone (NCBIN:113132, !1NCBIP:113133) CLASSIFICATION #superfamily thimet oligopeptidase KEYWORDS hydrolase; metalloproteinase; mitochondrial matrix; !1mitochondrion; zinc FEATURE !$492,496,499 #binding_site zinc (His) #status predicted\ !$493 #active_site Glu #status predicted SUMMARY #length 710 #molecular-weight 80673 #checksum 1361 SEQUENCE /// ENTRY HYHUMA #type complete TITLE meprin A (EC 3.4.24.18) alpha chain precursor - human ALTERNATE_NAMES intestinal brush border metalloendopeptidase; N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase; PABA peptide hydrolase (PPH) alpha chain ORGANISM #formal_name Homo sapiens #common_name man DATE 19-May-1994 #sequence_revision 16-Feb-1996 #text_change 18-Jun-1999 ACCESSIONS S60193; S39464; S39465; A41196 REFERENCE S60193 !$#authors Eldering, J.A.; Grunberg, J.; Sterchi, E.E. !$#submission submitted to the EMBL Data Library, August 1994 !$#accession S60193 !'##molecule_type mRNA !'##residues 1-746 ##label ELD !'##cross-references EMBL:M82962; NID:g535474; PIDN:AAA21338.1; !1PID:g535475 REFERENCE S39464 !$#authors Dumermuth, E.; Eldering, J.A.; Gruenberg, J.; Jiang, W.; !1Sterchi, E.E. !$#journal FEBS Lett. (1993) 335:367-375 !$#title Cloning of the PABA peptide hydrolase alpha subunit !1(PPH-alpha) from human small intestine and its expression in !1COS-1 cells. !$#cross-references MUID:94085556; PMID:8262185 !$#accession S39464 !'##molecule_type mRNA !'##residues 33-746 ##label DUM !$#accession S39465 !'##molecule_type protein !'##residues 66-83 ##label DU2 !'##note human meprin A alpha chain appears to be expressed in intestine !1but not in kidney REFERENCE A41196 !$#authors Dumermuth, E.; Sterchi, E.E.; Jiang, W.; Wolz, R.L.; Bond, !1J.S.; Flannery, A.V.; Beynon, R.J. !$#journal J. Biol. Chem. (1991) 266:21381-21385 !$#title The astacin family of metalloendopeptidases. !$#cross-references MUID:92042028; PMID:1939172 !$#accession A41196 !'##molecule_type mRNA !'##residues 65-263 ##label DU3 !'##cross-references GB:M82962; GB:M74238 GENETICS !$#gene GDB:MEP1A !'##cross-references GDB:371059; OMIM:600388 !$#map_position 6p21.2-6p21.1 COMPLEX may form homodimers, homotetramers, or heterotetramers with !1two alpha chains and two beta chains (see PIR:HYHUMB) FUNCTION !$#description zinc metalloproteinase CLASSIFICATION #superfamily meprin A; astacin homology; EGF homology; MAM !1homology KEYWORDS glycoprotein; hydrolase; metalloproteinase; transmembrane !1protein; zinc FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-65 #domain propeptide #status predicted #label PRO\ !$66-746 #product meprin A alpha chain #status predicted !8#label MAT\ !$75-261 #domain astacin homology #label AST\ !$264-433 #domain MAM homology #label MAM\ !$674-709 #domain EGF homology #label EGF\ !$718-740 #domain transmembrane #status predicted #label TRM\ !$107-259,128-147, !$674-685,679-694, !$696-709 #disulfide_bonds #status predicted\ !$140,222,414,440, !$447,539 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$155,159,165,214 #binding_site zinc (His, His, His, Tyr) #status !8predicted\ !$156 #active_site Glu #status predicted SUMMARY #length 746 #molecular-weight 84367 #checksum 7669 SEQUENCE /// ENTRY HYHUMB #type complete TITLE meprin A (EC 3.4.24.18) beta chain precursor - human ALTERNATE_NAMES N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase; PABA peptide hydrolase (PPH) beta chain ORGANISM #formal_name Homo sapiens #common_name man DATE 16-Feb-1995 #sequence_revision 16-Feb-1996 #text_change 18-Jun-1999 ACCESSIONS S49383; S39466 REFERENCE S49383 !$#authors Eldering, J.A.; Groenberg, J.; Sterchi, E.E. !$#submission submitted to the EMBL Data Library, September 1994 !$#description Cloning and the PABA-peptide hydrolase beta subunit: !1coexpression is required for plasma membrane localization of !1the alpha subunit in COS-1 cells. !$#accession S49383 !'##status preliminary !'##molecule_type mRNA !'##residues 1-700 ##label ELD !'##cross-references EMBL:X81333; NID:g557645; PIDN:CAA57107.1; !1PID:g557646 REFERENCE S39464 !$#authors Dumermuth, E.; Eldering, J.A.; Gruenberg, J.; Jiang, W.; !1Sterchi, E.E. !$#journal FEBS Lett. (1993) 335:367-375 !$#title Cloning of the PABA peptide hydrolase alpha subunit !1(PPH-alpha) from human small intestine and its expression in !1COS-1 cells. !$#cross-references MUID:94085556; PMID:8262185 !$#accession S39466 !'##molecule_type protein !'##residues 62-70,'S',72-73,'P',75-79 ##label DUM GENETICS !$#gene GDB:MEP1B !'##cross-references GDB:371066 !$#map_position 18q12.2-18q12.3 COMPLEX may form homodimers, homotetramers, or heterotetramers with !1two alpha chains (see PIR:HYHUMA) and two beta chains FUNCTION !$#description endopeptidase preferentially hydrolyzing peptide bonds on !1the carboxyl side of hydrophobic residues CLASSIFICATION #superfamily meprin A; astacin homology; EGF homology; MAM !1homology KEYWORDS glycoprotein; hydrolase; metalloproteinase; transmembrane !1protein; zinc FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-61 #domain propeptide #status predicted #label PRO\ !$62-700 #product meprin A beta chain #status predicted #label !8MAT\ !$71-257 #domain astacin homology #label AST\ !$260-429 #domain MAM homology #label MAM\ !$608-643 #domain EGF homology #label EGF\ !$653-678 #domain transmembrane #status predicted #label TRM\ !$103-255,124-144, !$608-619,613-628, !$630-643 #disulfide_bonds #status predicted\ !$152,156,162,211 #binding_site zinc (His, His, His, Tyr) #status !8predicted\ !$153 #active_site Glu #status predicted\ !$218,370,421,436, !$445,547,592,692 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 700 #molecular-weight 79458 #checksum 916 SEQUENCE /// ENTRY A42908 #type complete TITLE meprin A (EC 3.4.24.18) beta chain - rat ALTERNATE_NAMES endopeptidase-2 beta chain; meprin beta chain; meprin-a beta chain ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A42908 REFERENCE A42908 !$#authors Johnson, G.D.; Hersh, L.B. !$#journal J. Biol. Chem. (1992) 267:13505-13512 !$#title Cloning a rat meprin cDNA reveals the enzyme is a !1heterodimer. !$#cross-references MUID:92317075; PMID:1377685 !$#accession A42908 !'##status preliminary !'##molecule_type mRNA !'##residues 1-668 ##label JOH !'##note sequence extracted from NCBI backbone (NCBIP:107784) CLASSIFICATION #superfamily meprin A; astacin homology; EGF homology; MAM !1homology KEYWORDS heterodimer; hydrolase; metalloproteinase; zinc FEATURE !$72-258 #domain astacin homology #label AST\ !$261-430 #domain MAM homology #label MAM\ !$153,157,163,212 #binding_site zinc (His, His, His, Tyr) #status !8predicted\ !$154 #active_site Glu #status predicted SUMMARY #length 668 #molecular-weight 75049 #checksum 9806 SEQUENCE /// ENTRY HYCY #type complete TITLE astacin (EC 3.4.24.21) precursor [validated] - broad-fingered crayfish ALTERNATE_NAMES Astacus proteinase; crayfish small-molecule proteinase ORGANISM #formal_name Astacus astacus, Astacus fluviatilis #common_name broad-fingered crayfish DATE 30-Sep-1992 #sequence_revision 29-May-1998 #text_change 15-Sep-2000 ACCESSIONS A58830; A25829 REFERENCE A58830 !$#authors Geier, G.; Jacob, E.; Stoecker, W.; Zwilling, R. !$#journal Arch. Biochem. Biophys. (1997) 337:300-307 !$#title Genomic organization of the zinc-endopeptidase astacin. !$#cross-references MUID:97169019; PMID:9016826 !$#accession A58830 !'##molecule_type DNA !'##residues 1-251 ##label GEI !'##cross-references GB:X95684; NID:g1200202; PIDN:CAA64981.1; !1PID:g1200203 REFERENCE A25829 !$#authors Titani, K.; Torff, H.J.; Hormel, S.; Kumar, S.; Walsh, K.A.; !1Rodl, J.; Neurath, H.; Zwilling, R. !$#journal Biochemistry (1987) 26:222-226 !$#title Amino acid sequence of a unique protease from the crayfish !1Astacus fluviatilis. !$#cross-references MUID:87157616; PMID:3548817 !$#accession A25829 !'##molecule_type protein !'##residues 50-249 ##label TIT REFERENCE A38849 !$#authors Bode, W.; Gomis-Rueth, F.X.; Huber, R.; Zwilling, R.; !1Stoecker, W. !$#journal Nature (1992) 358:164-167 !$#title Structure of astacin and implications for activation of !1astacins and zinc-ligation of collagenases. !$#cross-references MUID:92310594; PMID:1319561 !$#contents annotation; X-ray crystallography, 1.8 angstroms REFERENCE A58831 !$#authors Gomis-Rueth, F.X.; Stoecker, W.; Huber, R.; Zwilling, R.; !1Bode, W. !$#journal J. Mol. Biol. (1993) 229:945-968 !$#title Refined 1.8 angstroms x-ray crystal structure of astacin, a !1zinc-endopeptidase from the crayfish Astacus astacus L. !1Structure determination, refinement, molecular structure and !1comparison with thermolysin. !$#cross-references MUID:93188025; PMID:8445658 !$#contents annotation; X-ray crystallography, 1.8 angstroms REFERENCE A52277 !$#authors Bode, W.; Gomis-Rueth, F.X.; Stoecker, W. !$#submission submitted to the Brookhaven Protein Data Bank, April 1993 !$#cross-references PDB:1AST !$#contents annotation; X-ray crystallography, 1.8 angstroms, with zinc, !1residues 50-249 REFERENCE A54159 !$#authors Gomis-Rueth, F.X.; Grams, F.; Yiallouros, I.; Nar, H.; !1Kuesthardt, U.; Zwilling, R.; Bode, W.; Stoecker, W. !$#journal J. Biol. Chem. (1994) 269:17111-17117 !$#title Crystal structures, spectroscopic features, and catalytic !1properties of cobalt(II), copper(II), nickel(II), and !1mercury(II) derivatives of the zinc endopeptidase astacin. A !1correlation of structure and proteolytic activity. !$#cross-references MUID:94274700; PMID:8006015 !$#contents annotation; X-ray crystallography REFERENCE A52597 !$#authors Gomis-rueth, F.X.; Stoecker, W.; Bode, W. !$#submission submitted to the Brookhaven Protein Data Bank, May 1994 !$#cross-references PDB:1IAA !$#contents annotation; X-ray crystallography, 1.9 angstroms, with !1copper, residues 50-249 REFERENCE A52598 !$#authors Gomis-Rueth, F.X.; Stoecker, W.; Bode, W. !$#submission submitted to the Brookhaven Protein Data Bank, May 1994 !$#cross-references PDB:1IAB !$#contents annotation; X-ray crystallography, 1.79 angstroms, with !1cobalt, residues 50-249 REFERENCE A52599 !$#authors Gomis-Rueth, F.X.; Stoecker, W.; Bode, W. !$#submission submitted to the Brookhaven Protein Data Bank, May 1994 !$#cross-references PDB:1IAC !$#contents annotation; X-ray crystallography, 2.1 angstroms, with !1mercury, residues 50-249 REFERENCE A52600 !$#authors Gomis-Rueth, F.X.; Stoecker, W.; Bode, W. !$#submission submitted to the Brookhaven Protein Data Bank, May 1994 !$#cross-references PDB:1IAD !$#contents annotation; X-ray crystallography, 2.3 angstroms, without !1zinc, residues 50-249 REFERENCE A52601 !$#authors Grams, F.; Stoecker, W.; Bode, W. !$#submission submitted to the Brookhaven Protein Data Bank, May 1994 !$#cross-references PDB:1IAE !$#contents annotation; X-ray crystallography, 1.83 angstroms, with !1nickel, residues 50-249 COMMENT It is not certain whether the carboxyl-terminal Arg-His !1dipeptide is removed during activation or by extracellular !1modification. The propetide may be cleaved by activated !1astacin. GENETICS !$#introns 4/3; 112/1; 172/1; 223/1 FUNCTION !$#description endopeptidase preferentially hydrolyzing peptide bonds on !1the amino side of alanine (P1') and proline (P2') CLASSIFICATION #superfamily astacin; astacin homology KEYWORDS hydrolase; metalloproteinase; zinc; zymogen FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-49 #domain propeptide #status predicted #label PRO\ !$50-249 #product astacin #status experimental #label MAT\ !$59-249 #domain astacin homology #label AST\ !$91-247,113-133 #disulfide_bonds #status experimental\ !$141,145,151,198 #binding_site zinc (His, His, His, Tyr) #status !8experimental\ !$142 #active_site Glu #status predicted SUMMARY #length 251 #molecular-weight 28092 #checksum 7459 SEQUENCE /// ENTRY BMHU1 #type complete TITLE procollagen C-endopeptidase (EC 3.4.24.19) precursor, splice form BMP1 - human ALTERNATE_NAMES bone morphogenic protein 1 (BMP1) ORGANISM #formal_name Homo sapiens #common_name man DATE 16-Sep-1992 #sequence_revision 03-Aug-1995 #text_change 18-Jun-1999 ACCESSIONS A37278; E58788 REFERENCE A37278 !$#authors Wozney, J.M.; Rosen, V.; Celeste, A.J.; Mitsock, L.M.; !1Whitters, M.J.; Kriz, R.W.; Hewick, R.M.; Wang, E.A. !$#journal Science (1988) 242:1528-1534 !$#title Novel regulators of bone formation: molecular clones and !1activities. !$#cross-references MUID:89072730; PMID:3201241 !$#accession A37278 !'##molecule_type mRNA !'##residues 1-730 ##label WOZ !'##cross-references GB:M22488; NID:g179499; PIDN:AAA51833.1; !1PID:g179500 GENETICS !$#gene GDB:BMP1 !'##cross-references GDB:125203; OMIM:112264 !$#map_position 8p21-8p21 FUNCTION !$#description catalyzes hydrolysis of the carboxyl-terminal propeptide of !1collagen type I, II and III alpha chains CLASSIFICATION #superfamily procollagen C-endopeptidase; astacin homology; !1C1r/C1s repeat homology; EGF homology KEYWORDS alternative splicing; beta-hydroxyasparagine; bone; calcium; !1duplication; glycoprotein; hydrolase; metalloproteinase; !1zinc FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-730 #product procollagen C-endopeptidase splice form BMP1 !8#status predicted #label MAT\ !$130-321 #domain astacin homology #label AST\ !$322-431 #domain C1r/C1s repeat homology #label C1R1\ !$435-544 #domain C1r/C1s repeat homology #label C1R2\ !$551-587 #domain EGF homology #label EGF\ !$591-700 #domain C1r/C1s repeat homology #label C1R3\ !$91,142,332,363,599 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$163-319,185-205, !$322-348,375-397, !$435-461,488-510, !$551-563,559-572, !$574-587,591-617, !$644-666 #disulfide_bonds #status predicted\ !$213,217,223,272 #binding_site zinc (His, His, His, Tyr) #status !8predicted\ !$214 #active_site Glu #status predicted\ !$565 #modified_site erythro-beta-hydroxyasparagine (Asn) !8#status predicted SUMMARY #length 730 #molecular-weight 82899 #checksum 287 SEQUENCE /// ENTRY A58788 #type complete TITLE procollagen C-endopeptidase (EC 3.4.24.19) precursor, splice form HIS - human ALTERNATE_NAMES bone morphogenic protein splice form BMP-1/His ORGANISM #formal_name Homo sapiens #common_name man DATE 28-Mar-1998 #sequence_revision 09-Apr-1998 #text_change 18-Jun-1999 ACCESSIONS A37278; A58788 REFERENCE A37278 !$#authors Wozney, J.M.; Rosen, V.; Celeste, A.J.; Mitsock, L.M.; !1Whitters, M.J.; Kriz, R.W.; Hewick, R.M.; Wang, E.A. !$#journal Science (1988) 242:1528-1534 !$#title Novel regulators of bone formation: molecular clones and !1activities. !$#cross-references MUID:89072730; PMID:3201241 !$#accession A37278 !'##molecule_type mRNA !'##residues 1-702,'EKRPALQPPRGRPHQLKFRVQKRNRTPQ' ##label WOZ !'##cross-references GB:M22488; NID:g179499; PIDN:AAA51833.1; !1PID:g179500 REFERENCE A58788 !$#authors Takahara, K.; Lyons, G.E.; Greenspan, D.S. !$#journal J. Biol. Chem. (1994) 269:32572-32578 !$#title Bone morphogenetic protein-1 and a mammalian tolloid !1homologue (mTld) are encoded by alternatively spliced !1transcripts which are differentially expressed in some !1tissues. !$#cross-references MUID:95096114; PMID:7798260 !$#accession A58788 !'##molecule_type mRNA !'##residues 703-823 ##label TAK !'##cross-references GB:L35278; NID:g619423; PIDN:AAC41703.1; !1PID:g619424 GENETICS !$#gene GDB:BMP1; BMP-1 !'##cross-references GDB:125203; OMIM:112264 !$#map_position 8p21-8p21 FUNCTION !$#description catalyzes hydrolysis of the carboxyl-terminal propeptide of !1collagen type I, II and III alpha chains CLASSIFICATION #superfamily procollagen C-endopeptidase; astacin homology; !1C1r/C1s repeat homology; EGF homology KEYWORDS alternative splicing; beta-hydroxyasparagine; bone; calcium; !1duplication; glycoprotein; hydrolase; metalloproteinase; !1zinc FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-823 #product procollagen C-endopeptidase splice form HIS !8#status predicted #label MAT\ !$130-321 #domain astacin homology #label AST\ !$322-431 #domain C1r/C1s repeat homology #label C1R1\ !$435-544 #domain C1r/C1s repeat homology #label C1R2\ !$551-587 #domain EGF homology #label EGF\ !$591-700 #domain C1r/C1s repeat homology #label C1R3\ !$738-752 #region histidine-rich\ !$91,142,332,363,599 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$163-319,185-205, !$322-348,375-397, !$435-461,488-510, !$551-563,559-572, !$574-587,591-617, !$644-666 #disulfide_bonds #status predicted\ !$213,217,223,272 #binding_site zinc (His, His, His, Tyr) #status !8predicted\ !$214 #active_site Glu #status predicted\ !$565 #modified_site erythro-beta-hydroxyasparagine (Asn) !8#status predicted SUMMARY #length 823 #molecular-weight 92654 #checksum 873 SEQUENCE /// ENTRY B58788 #type complete TITLE procollagen C-endopeptidase (EC 3.4.24.19) precursor, tolloid-like splice form - human ALTERNATE_NAMES bone morphogenic protein 1, tolloid-like splice form ORGANISM #formal_name Homo sapiens #common_name man DATE 28-Mar-1998 #sequence_revision 09-Apr-1998 #text_change 16-Jul-1999 ACCESSIONS A37278; B58788 REFERENCE A37278 !$#authors Wozney, J.M.; Rosen, V.; Celeste, A.J.; Mitsock, L.M.; !1Whitters, M.J.; Kriz, R.W.; Hewick, R.M.; Wang, E.A. !$#journal Science (1988) 242:1528-1534 !$#title Novel regulators of bone formation: molecular clones and !1activities. !$#cross-references MUID:89072730; PMID:3201241 !$#accession A37278 !'##molecule_type mRNA !'##residues 1-702,'EKRPALQPPRGRPHQLKFRVQKRNRTPQ' ##label WOZ !'##cross-references GB:M22488; NID:g179499; PIDN:AAA51833.1; !1PID:g179500 REFERENCE A58788 !$#authors Takahara, K.; Lyons, G.E.; Greenspan, D.S. !$#journal J. Biol. Chem. (1994) 269:32572-32578 !$#title Bone morphogenetic protein-1 and a mammalian tolloid !1homologue (mTld) are encoded by alternatively spliced !1transcripts which are differentially expressed in some !1tissues. !$#cross-references MUID:95096114; PMID:7798260 !$#accession B58788 !'##molecule_type mRNA !'##residues 703-986 ##label TAK !'##cross-references GB:L35279; NID:g619860; PIDN:AAC41710.1; !1PID:g619861 GENETICS !$#gene GDB:BMP1; BMP-1 !'##cross-references GDB:125203; OMIM:112264 !$#map_position 8p21-8p21 FUNCTION !$#description catalyzes hydrolysis of the carboxyl-terminal propeptide of !1collagen type I, II and III alpha chains CLASSIFICATION #superfamily procollagen C-endopeptidase; astacin homology; !1C1r/C1s repeat homology; EGF homology KEYWORDS alternative splicing; beta-hydroxyasparagine; bone; calcium; !1duplication; glycoprotein; hydrolase; metalloproteinase; !1zinc FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-986 #product procollagen C-endopeptidase tolloid-like !8splice form #status predicted #label MAT\ !$130-321 #domain astacin homology #label AST\ !$322-431 #domain C1r/C1s repeat homology #label C1R1\ !$435-544 #domain C1r/C1s repeat homology #label C1R2\ !$551-587 #domain EGF homology #label EG1\ !$591-700 #domain C1r/C1s repeat homology #label C1R3\ !$707-742 #domain EGF homology #label EG2\ !$747-856 #domain C1r/C1s repeat homology #label C1R4\ !$860-973 #domain C1r/C1s repeat homology #label C1R5\ !$91,142,332,363,599 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$163-319,185-205, !$322-348,375-397, !$435-461,488-510, !$551-563,559-572, !$574-587,591-617, !$644-666,707-718, !$714-727,729-742, !$747-773,800-822, !$860-890,917-939 #disulfide_bonds #status predicted\ !$213,217,223,272 #binding_site zinc (His, His, His, Tyr) #status !8predicted\ !$214 #active_site Glu #status predicted\ !$565,720 #modified_site erythro-beta-hydroxyasparagine (Asn) !8#status predicted SUMMARY #length 986 #molecular-weight 111178 #checksum 7231 SEQUENCE /// ENTRY A39288 #type complete TITLE dorsal-ventral patterning protein tolloid (EC 3.4.24.-) - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A39288 REFERENCE A39288 !$#authors Shimell, M.J.; Ferguson, E.L.; Childs, S.R.; O'Connor, M.B. !$#journal Cell (1991) 67:469-481 !$#title The Drosophila dorsal-ventral patterning gene tolloid is !1related to human bone morphogenetic protein 1. !$#cross-references MUID:92034970; PMID:1840509 !$#accession A39288 !'##status preliminary !'##molecule_type mRNA !'##residues 1-1057 ##label SHI !'##cross-references GB:M76976; NID:g157305; PIDN:AAA28491.1; !1PID:g157306 GENETICS !$#gene FlyBase:tld !'##cross-references FlyBase:FBgn0003719 CLASSIFICATION #superfamily dorsal-ventral patterning protein tolloid; !1astacin homology; C1r/C1s repeat homology; EGF homology KEYWORDS duplication; hydrolase; metalloproteinase; zinc FEATURE !$136-329 #domain astacin homology #label AST\ !$352-464 #domain C1r/C1s repeat homology #label C1R1\ !$468-578 #domain C1r/C1s repeat homology #label C1R2\ !$585-620 #domain EGF homology #label EG1\ !$624-740 #domain C1r/C1s repeat homology #label C1R3\ !$747-782 #domain EGF homology #label EG2\ !$787-896 #domain C1r/C1s repeat homology #label C1R4\ !$900-1013 #domain C1r/C1s repeat homology #label C1R5\ !$221,225,231,280 #binding_site zinc (His, His, His, Tyr) #status !8predicted\ !$222 #active_site Glu #status predicted SUMMARY #length 1057 #molecular-weight 120575 #checksum 7223 SEQUENCE /// ENTRY HYBS #type complete TITLE bacillolysin (EC 3.4.24.28) precursor - Bacillus subtilis (strain 168) ALTERNATE_NAMES Bacillus metalloendopeptidase; Bacillus subtilis neutral proteinase; microbial metalloproteinase ORGANISM #formal_name Bacillus subtilis DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 18-Jun-1999 ACCESSIONS A25414; A33895; S13061; JQ0080; S13950; S13951; S13952 REFERENCE A25414 !$#authors Yang, M.Y.; Ferrari, E.; Henner, D.J. !$#journal J. Bacteriol. (1984) 160:15-21 !$#title Cloning of the neutral protease gene of Bacillus subtilis !1and the use of the cloned gene to create an in vitro-derived !1deletion mutation. !$#cross-references MUID:85006776; PMID:6090407 !$#accession A25414 !'##molecule_type DNA !'##residues 1-521 ##label YAN !'##cross-references GB:K01985; NID:g143257; PIDN:AAA22627.1; !1PID:g143258 REFERENCE A33895 !$#authors Stoeva, S.; Kleinschmidt, T.; Mesrob, B.; Braunitzer, G. !$#journal Biochemistry (1990) 29:527-534 !$#title Primary structure of a zinc protease from Bacillus !1mesentericus strain 76. !$#cross-references MUID:90148980; PMID:2302386 !$#accession A33895 !'##molecule_type protein !'##residues 222-521 ##label STO REFERENCE S13061 !$#authors van den Burg, B.; Eijsink, V.G.H.; Stulp, B.K.; Venema, G. !$#journal Biochem. J. (1990) 272:93-97 !$#title Identification of autodigestion target sites in Bacillus !1subtilis neutral proteinase. !$#cross-references MUID:91090741; PMID:2124807 !$#accession S13061 !'##molecule_type protein !'##residues 222-228;335-348;377-384;419-425 ##label VAN !'##note sequence of fragments from amino ends after controlled !1autolysis, performed to study similarity of enzyme to !1thermolysin in structure; some autolytic sites identical GENETICS !$#gene nprE !$#map_position 35 C !$#start_codon GTG CLASSIFICATION #superfamily thermolysin KEYWORDS calcium; extracellular protein; hydrolase; !1metalloproteinase; zinc FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-221 #domain propeptide #status predicted #label PRO\ !$222-521 #product bacillolysin #status experimental #label !8MAT\ !$364,368,388 #binding_site zinc (His, His, Glu) #status predicted\ !$365,449 #active_site Glu, His #status predicted SUMMARY #length 521 #molecular-weight 56563 #checksum 4389 SEQUENCE /// ENTRY HYBSN #type complete TITLE bacillolysin (EC 3.4.24.28) precursor - Bacillus amyloliquefaciens ALTERNATE_NAMES Bacillus metalloendopeptidase; microbial metalloproteinase; neutral proteinase ORGANISM #formal_name Bacillus amyloliquefaciens DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 18-Jun-1999 ACCESSIONS A25415 REFERENCE A25415 !$#authors Vasantha, N.; Thompson, L.D.; Rhodes, C.; Banner, C.; Nagle, !1J.; Filpula, D. !$#journal J. Bacteriol. (1984) 159:811-819 !$#title Genes for alkaline protease and neutral protease from !1Bacillus amyloliquefaciens contain a large open reading !1frame between the regions coding for signal sequence and !1mature protein. !$#cross-references MUID:85006739; PMID:6090391 !$#accession A25415 !'##molecule_type DNA !'##residues 1-521 ##label YAN !'##cross-references GB:K02497; NID:g143248; PIDN:AAB05346.1; !1PID:g143249 GENETICS !$#gene npr !$#start_codon GTG CLASSIFICATION #superfamily thermolysin KEYWORDS calcium; extracellular protein; hydrolase; !1metalloproteinase; zinc FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-221 #domain propeptide #status predicted #label PRO\ !$222-521 #product bacillolysin #status predicted #label MAT\ !$364,368,388 #binding_site zinc (His, His, Glu) #status predicted\ !$365,449 #active_site Glu, His #status predicted SUMMARY #length 521 #molecular-weight 56840 #checksum 7195 SEQUENCE /// ENTRY HYBSU #type complete TITLE bacillolysin (EC 3.4.24.28) precursor [validated] - Bacillus cereus ALTERNATE_NAMES Bacillus metalloendopeptidase; microbial metalloproteinase; neutral proteinase; thermolysin-like neutral proteinase ORGANISM #formal_name Bacillus cereus DATE 30-Jun-1988 #sequence_revision 12-Apr-1996 #text_change 15-Sep-2000 ACCESSIONS S22690; A24306; I39914 REFERENCE S22690 !$#authors Wetmore, D.R.; Wong, S.L.; Roche, R.S. !$#journal Mol. Microbiol. (1992) 6:1593-1604 !$#title The role of the pro-sequence in the processing and secretion !1of the thermolysin-like neutral protease from Bacillus !1cereus. !$#cross-references MUID:92356823; PMID:1495388 !$#accession S22690 !'##molecule_type DNA !'##residues 1-566 ##label WET !'##cross-references EMBL:M83910; NID:g143242; PIDN:AAA22620.1; !1PID:g143243 REFERENCE A24306 !$#authors Sidler, W.; Niederer, E.; Suter, F.; Zuber, H. !$#journal Biol. Chem. Hoppe-Seyler (1986) 367:643-657 !$#title The primary structure of Bacillus cereus neutral proteinase !1and comparison with thermolysin and Bacillus subtilis !1neutral proteinase. !$#cross-references MUID:87000170; PMID:3092843 !$#accession A24306 !'##molecule_type protein !'##residues 250-566 ##label SID !'##experimental_source strain DSM3101 REFERENCE A51318 !$#authors Stark, W.; Pauptit, R.A.; Jansonius, J.N. !$#submission submitted to the Brookhaven Protein Data Bank, January 1992 !$#cross-references PDB:1NPC !$#contents annotation; X-ray crystallography, 2.0 angstroms, residues !1250-566 REFERENCE A38850 !$#authors Pauptit, R.A.; Karlsson, R.; Picot, D.; Jenkins, J.A.; !1Niklaus-Reimer, A.S.; Jansonius, J.N. !$#journal J. Mol. Biol. (1988) 199:525-537 !$#title Crystal structure of neutral protease from Bacillus cereus !1refined at 3.0 A resolution and comparison with the !1homologous but more thermostable enzyme thermolysin. !$#cross-references MUID:88172498; PMID:3127592 !$#contents annotation; X-ray crystallography, 3.0 angstroms GENETICS !$#gene cnp; nprC FUNCTION !$#description hydrolyzes peptide bonds on the amino side of hydrophobic !1residues CLASSIFICATION #superfamily thermolysin KEYWORDS calcium; extracellular protein; hydrolase; !1metalloproteinase; zinc FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-249 #domain activation peptide #status predicted #label !8ACP\ !$250-566 #product bacillolysin #status experimental #label !8MAT\ !$307,309,311 #binding_site calcium (Asp, Asp, Val) #status !8experimental\ !$388,427,435,437,440 #binding_site calcium (Asp, Glu, Asp, Glu, Glu) !8#status experimental\ !$392,396,416 #binding_site zinc (His, His, Glu) #status !8experimental\ !$393,481 #active_site Glu, His #status predicted\ !$427,433,435,440 #binding_site calcium (Glu, Asn, Asp, Glu) #status !8experimental\ !$443,444,447,450 #binding_site calcium (Tyr, Thr, Lys, Asp) #status !8experimental SUMMARY #length 566 #molecular-weight 60919 #checksum 862 SEQUENCE /// ENTRY HYBST #type complete TITLE thermolysin (EC 3.4.24.27) precursor [validated] - Bacillus "thermoproteolyticus" ALTERNATE_NAMES Bacillus thermoproteolyticus neutral proteinase; microbial metalloproteinase ORGANISM #formal_name Bacillus "thermoproteolyticus" DATE 24-Apr-1984 #sequence_revision 07-Jun-1996 #text_change 15-Sep-2000 ACCESSIONS I40579; A00993; S41312 REFERENCE I40579 !$#authors O'Donohue, M.J.; Roques, B.P.; Beaumont, A. !$#journal Biochem. J. (1994) 300:599-603 !$#title Cloning and expression in Bacillus subtilis of the npr gene !1from Bacillus thermoproteolyticus Rokko coding for the !1thermostable metalloprotease thermolysin. !$#cross-references MUID:94271180; PMID:8002967 !$#accession I40579 !'##molecule_type DNA !'##residues 1-408,'K',410-548 ##label OAD !'##cross-references EMBL:X76986; NID:g441266; PIDN:CAA54291.1; !1PID:g441267 !'##note submitted to the EMBL Data Library, December 1993 REFERENCE A00993 !$#authors Titani, K.; Hermodson, M.A.; Ericsson, L.H.; Walsh, K.A.; !1Neurath, H. !$#journal Nature New Biol. (1972) 238:35-37 !$#title Amino-acid sequence of thermolysin. !$#accession A00993 !'##molecule_type protein !'##residues 233-268,'D',270-350,'E',352-399,'I',401-548 ##label TIT REFERENCE A50631 !$#authors Matthews, B.W.; Holmes, M.A. !$#submission submitted to the Brookhaven Protein Data Bank, February 1982 !$#cross-references PDB:3TLN !$#contents annotation; X-ray crystallography, 1.6 angstroms, residues !1233-268,'D',270-350,'E',352-399,'I',401-548 REFERENCE A92888 !$#authors Holmes, M.A.; Matthews, B.W. !$#journal J. Mol. Biol. (1982) 160:623-639 !$#title Structure of thermolysin redefined at 1.6 A resolution. !$#cross-references MUID:83085812; PMID:7175940 !$#contents annotation; X-ray crystallography, 1.6 angstroms REFERENCE A92165 !$#authors Matthews, B.W.; Weaver, L.H.; Kester, W.R. !$#journal J. Biol. Chem. (1974) 249:8030-8044 !$#title The conformation of thermolysin. !$#cross-references MUID:75041142; PMID:4214815 !$#contents annotation; X-ray crystallography, 2.3 angstroms REFERENCE A90377 !$#authors Burstein, Y.; Walsh, K.A.; Neurath, H. !$#journal Biochemistry (1974) 13:205-210 !$#title Evidence of an essential histidine residue in thermolysin. !$#cross-references MUID:74052951; PMID:4808703 !$#contents annotation; active site FUNCTION !$#description metalloendopeptidase preferentially hydrolyzes peptide bonds !1on the amino side of leucine and phenylalanine CLASSIFICATION #superfamily thermolysin KEYWORDS calcium; extracellular protein; hydrolase; !1metalloproteinase; zinc FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-232 #domain propeptide #status predicted #label PRO\ !$233-548 #product thermolysin #status experimental #label MAT\ !$289,291,293 #binding_site calcium (Asp, Asp, Gln) #status !8experimental\ !$370,409,417,419,422 #binding_site calcium (Asp, Glu, Asp, Glu, Glu) !8#status experimental\ !$374,378,398 #binding_site zinc (His, His, Glu) #status !8experimental\ !$375,463 #active_site Glu, His #status predicted\ !$409,415,417,422 #binding_site calcium (Glu, Asn, Asp, Glu) #status !8experimental\ !$425,426,429,432 #binding_site calcium (Tyr, Thr, Ile, Asp) #status !8experimental SUMMARY #length 548 #molecular-weight 60122 #checksum 2942 SEQUENCE /// ENTRY HYBSS #type complete TITLE bacillolysin (EC 3.4.24.28) precursor - Bacillus stearothermophilus ALTERNATE_NAMES Bacillus metalloendopeptidase; microbial metalloproteinase; neutral proteinase ORGANISM #formal_name Bacillus stearothermophilus DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 18-Jun-1999 ACCESSIONS A24924; B24924; A25253 REFERENCE A24924 !$#authors Takagi, M.; Imanaka, T.; Aiba, S. !$#journal J. Bacteriol. (1985) 163:824-831 !$#title Nucleotide sequence and promoter region for the neutral !1protease gene from Bacillus stearothermophilus. !$#cross-references MUID:85289021; PMID:2993245 !$#accession A24924 !'##molecule_type DNA !'##residues 1-548 ##label TAK !'##cross-references GB:M11446; NID:g143246; PIDN:AAA22621.1; !1PID:g143247 !$#accession B24924 !'##molecule_type protein !'##residues 230-243 ##label TAK2 GENETICS !$#gene nprT CLASSIFICATION #superfamily thermolysin KEYWORDS calcium; extracellular protein; hydrolase; !1metalloproteinase; zinc FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-229 #domain propeptide #status predicted #label PRO\ !$230-548 #product bacillolysin #status experimental #label !8MAT\ !$374,378,398 #binding_site zinc (His, His, Glu) #status predicted\ !$375,463 #active_site Glu, His #status predicted SUMMARY #length 548 #molecular-weight 59580 #checksum 2930 SEQUENCE /// ENTRY HYBSPA #type complete TITLE pseudolysin (EC 3.4.24.26) precursor [validated] - Pseudomonas aeruginosa ALTERNATE_NAMES elastin-specific metalloproteinase; Pseudomonas aeruginosa neutral metalloproteinase; Pseudomonas elastase ORGANISM #formal_name Pseudomonas aeruginosa DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 31-Dec-2000 ACCESSIONS A32359; A32815; B38166; C38166; A38166; B40159; H83180 REFERENCE A32359 !$#authors Bever, R.A.; Iglewski, B.H. !$#journal J. Bacteriol. (1988) 170:4309-4314 !$#title Molecular characterization and nucleotide sequence of the !1Pseudomonas aeruginosa elastase structural gene. !$#cross-references MUID:88314935; PMID:2842313 !$#accession A32359 !'##molecule_type DNA !'##residues 1-498 ##label BEV !'##cross-references GB:M19472; NID:g1684933; PIDN:AAB36615.1; !1PID:g151210 !'##experimental_source strain PAO1 REFERENCE A32815 !$#authors Fukushima, J.; Yamamoto, S.; Morihara, K.; Atsumi, Y.; !1Takeuchi, H.; Kawamoto, S.; Okuda, K. !$#journal J. Bacteriol. (1989) 171:1698-1704 !$#title Structural gene and complete amino acid sequence of !1Pseudomonas aeruginosa IFO 3455 elastase. !$#cross-references MUID:89155481; PMID:2493453 !$#accession A32815 !'##molecule_type DNA !'##residues 1-324,'V',326-498 ##label FUK !'##cross-references GB:M24531; NID:g151211; PIDN:AAA25811.1; !1PID:g151212 !'##experimental_source strain IFO 3455 REFERENCE A38166 !$#authors Tanaka, E.; Kawamoto, S.; Fukushima, J.; Hamajima, K.; !1Onishi, H.; Miyagi, Y.; Inami, S.; Morihara, K.; Okuda, K. !$#journal J. Bacteriol. (1991) 173:6153-6158 !$#title Detection of elastase production in Escherichia coli with !1the elastase structural gene from several !1non-elastase-producing strains of Pseudomonas aeruginosa. !$#cross-references MUID:92011376; PMID:1917848 !$#accession B38166 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-74,'T',76-101,'R',103-184,'Y',186-240,'G',242-281,'D', !1283-470,'S',472-498 ##label TAN1 !'##experimental_source strain PA103 !'##note this strain does not have pseudolysin elastase activity, but !1the gene cloned in Escherichia coli does confer this !1activity !$#accession C38166 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-74,'T',76-101,'R',103-184,'Y',186-240,'G',242-281,'D', !1283-498 ##label TAN2 !'##experimental_source strain N-10 !'##note this strain does not have pseudolysin elastase activity, but !1the gene cloned in Escherichia coli does confer this !1activity !$#accession A38166 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-74,'T',76-184,'Y',186-406, !1'STTRRSTTTASTCTTPAACTTVRSTCWPIR', !1'RAGIPARPSRCSSTPTATTGPPPATTTAAPAG' ##label TAN3 !'##experimental_source strain IFO 3080 !'##note this strain does not have pseudolysin elastase activity and the !1gene cloned in Escherichia coli does not confer this !1activity; this sequence has a one base deletion after codon !1406, and lacks an active site residue REFERENCE A40159 !$#authors Haese, C.C.; Finkelstein, R.A. !$#journal Infect. Immun. (1990) 58:4011-4015 !$#title Comparison of the Vibrio cholerae hemagglutinin/protease and !1the Pseudomonas aeruginosa elastase. !$#cross-references MUID:91071884; PMID:2123831 !$#accession B40159 !'##molecule_type protein !'##residues 198-217 ##label HAE REFERENCE A51162 !$#authors Thayer, M.M.; Flaherty, K.M.; McKay, D.B. !$#submission submitted to the Brookhaven Protein Data Bank, January 1992 !$#cross-references PDB:1EZM !$#contents annotation; X-ray crystallography, 1.5 angstroms, residues !1198-495 REFERENCE A38851 !$#authors Thayer, M.M.; Flaherty, K.M.; McKay, D.B. !$#journal J. Biol. Chem. (1991) 266:2864-2871 !$#title Three-dimensional structure of the elastase of Pseudomonas !1aeruginosa at 1.5-A resolution. !$#cross-references MUID:91131579; PMID:1899664 !$#contents annotation; X-ray crystallography, 1.5 angstroms REFERENCE A82950 !$#authors Stover, C.K.; Pham, X.Q.; Erwin, A.L.; Mizoguchi, S.D.; !1Warrener, P.; Hickey, M.J.; Brinkman, F.S.L.; Hufnagle, !1W.O.; Kowalik, D.J.; Lagrou, M.; Garber, R.L.; Goltry, L.; !1Tolentino, E.; Westbrook-Wadman, S.; Yuan, Y.; Brody, L.L.; !1Coulter, S.N.; Folger, K.R.; Kas, A.; Larbig, K.; Lim, R.M.; !1Smith, K.A.; Spencer, D.H.; Wong, G.K.S.; Wu, Z.; Paulsen, !1I.T.; Reizer, J.; Saier, M.H.; Hancock, R.E.W.; Lory, S.; !1Olson, M.V. !$#journal Nature (2000) 406:959-964 !$#title Complete genome sequence of Pseudomonas aeruginosa PA01, an !1opportunistic pathogen. !$#cross-references MUID:20437337; PMID:10984043 !$#accession H83180 !'##status preliminary !'##molecule_type DNA !'##residues 1-498 ##label STO !'##cross-references GB:AE004791; GB:AE004091; NID:g9949882; !1PIDN:AAG07111.1; GSPDB:GN00131; PASP:PA3724 !'##experimental_source strain PAO1 GENETICS !$#gene lasB; PA3724 CLASSIFICATION #superfamily thermolysin KEYWORDS calcium; extracellular protein; hydrolase; !1metalloproteinase; zinc FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-197 #domain activation peptide #status predicted #label !8ACT\ !$198-498 #product pseudolysin #status experimental #label MAT\ !$227-255,467-494 #disulfide_bonds #status experimental\ !$333,369,372,380,382 #binding_site calcium (Asp, Glu, Glu, Asp, Leu) !8#status experimental\ !$337,341,361 #binding_site zinc (His, His, Glu) #status predicted\ !$338,420 #active_site Glu, His #status predicted SUMMARY #length 498 #molecular-weight 53687 #checksum 2989 SEQUENCE /// ENTRY JT0903 #type complete TITLE vibriolysin (EC 3.4.24.-) precursor - Vibrio proteolyticus ALTERNATE_NAMES zinc metalloproteinase ORGANISM #formal_name Vibrio proteolyticus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JT0903; PU0030 REFERENCE JT0903 !$#authors David, V.A.; Deutch, A.H.; Sloma, A.; Pawlyk, D.; Ally, A.; !1Durham, D.R. !$#journal Gene (1992) 112:107-112 !$#title Cloning, sequencing and expression of the gene encoding the !1extracellular neutral protease, vibriolysin, of Vibrio !1proteolyticus. !$#cross-references MUID:92201689; PMID:1551587 !$#accession JT0903 !'##molecule_type DNA !'##residues 1-609 ##label DAV !'##cross-references GB:M64809; NID:g155245; PIDN:AAA27548.1; !1PID:g155246 !$#accession PU0030 !'##molecule_type protein !'##residues 197-204,'X',206-215 ##label DAV1 COMMENT This vibriolysin is a thermostable, neutral metalloprotease !1containing one zinc atom. GENETICS !$#gene nprV CLASSIFICATION #superfamily thermolysin KEYWORDS hydrolase; metalloproteinase; zinc FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-196 #domain propeptide #status predicted #label PRO\ !$197-609 #product vibriolysin #status experimental #label VIB\ !$231-257,473-502 #disulfide_bonds #status predicted\ !$343,347,367 #binding_site zinc (His, His, Glu) #status predicted\ !$344,426 #active_site Glu, His #status predicted SUMMARY #length 609 #molecular-weight 66362 #checksum 5798 SEQUENCE /// ENTRY A47015 #type complete TITLE vibriolysin (EC 3.4.24.-) precursor - Vibrio anguillarum ALTERNATE_NAMES invasion metalloproteinase; zinc metalloproteinase ORGANISM #formal_name Vibrio anguillarum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A47015; A41466 REFERENCE A47015 !$#authors Milton, D.L.; Norqvist, A.; Wolf-Watz, H. !$#journal J. Bacteriol. (1992) 174:7235-7244 !$#title Cloning of a metalloprotease gene involved in the virulence !1mechanism of Vibrio anguillarum. !$#cross-references MUID:93054337; PMID:1429449 !$#accession A47015 !'##status preliminary !'##molecule_type DNA !'##residues 1-611 ##label MIL !'##cross-references GB:L02528; NID:g155164; PIDN:AAA27517.1; !1PID:g155165 !'##note sequence extracted from NCBI backbone (NCBIN:118023, !1NCBIP:118024) !'##note strain NB10; this publication is not cited in GenBank entry !1VIBEMPA, release 106.0 REFERENCE A41466 !$#authors Norqvist, A.; Norrman, B.; Wolf-Watz, H. !$#journal Infect. Immun. (1990) 58:3731-3736 !$#title Identification and characterization of a zinc !1metalloprotease associated with invasion by the fish !1pathogen Vibrio anguillarum. !$#cross-references MUID:91034188; PMID:2228244 !$#accession A41466 !'##molecule_type protein !'##residues 200-219 ##label NOR CLASSIFICATION #superfamily thermolysin KEYWORDS hydrolase; metalloproteinase; zinc FEATURE !$234-260,476-505 #disulfide_bonds #status predicted\ !$346,350,370 #binding_site zinc (His, His, Glu) #status predicted\ !$347,429 #active_site Glu, His #status predicted SUMMARY #length 611 #molecular-weight 66726 #checksum 1819 SEQUENCE /// ENTRY A42358 #type complete TITLE vibriolysin (EC 3.4.24.-) precursor [validated] - Vibrio cholerae (strain N16961 serogroup O1) ALTERNATE_NAMES hemagglutinin/proteinase; zinc metalloproteinase ORGANISM #formal_name Vibrio cholerae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 02-Feb-2001 ACCESSIONS A42358; A40159; B82407 REFERENCE A42358 !$#authors Haese, C.C.; Finkelstein, R.A. !$#journal J. Bacteriol. (1991) 173:3311-3317 !$#title Cloning and nucleotide sequence of the Vibrio cholerae !1hemagglutinin/protease (HA/protease) gene and construction !1of an HA/protease-negative strain. !$#cross-references MUID:91258311; PMID:2045361 !$#accession A42358 !'##molecule_type DNA !'##residues 1-609 ##label HAE !'##cross-references GB:M59466; NID:g155307; PIDN:AAA27579.1; !1PID:g155308 !'##note the authors translated the codon TCC for residue 582 as Phe REFERENCE A40159 !$#authors Haese, C.C.; Finkelstein, R.A. !$#journal Infect. Immun. (1990) 58:4011-4015 !$#title Comparison of the Vibrio cholerae hemagglutinin/protease and !1the Pseudomonas aeruginosa elastase. !$#cross-references MUID:91071884; PMID:2123831 !$#accession A40159 !'##status preliminary !'##molecule_type protein !'##residues 196-217 ##label HA2 REFERENCE A82035 !$#authors Heidelberg, J.F.; Eisen, J.A.; Nelson, W.C.; Clayton, R.A.; !1Gwinn, M.L.; Dodson, R.J.; Haft, D.H.; Hickey, E.K.; !1Peterson, J.D.; Umayam, L.A.; Gill, S.R.; Nelson, K.E.; !1Read, T.D.; Tettelin, H.; Richardson, D.; Ermolaeva, M.D.; !1Vamathevan, J.; Bass, S.; Qin, H.; Dragoi, I.; Sellers, P.; !1McDonald, L.; Utterback, T.; Fleishmann, R.D.; Nierman, !1W.C.; White, O.; Salzberg, S.L.; Smith, H.O.; Colwell, R.R.; !1Mekalanos, J.J.; Venter, J.C.; Fraser, C.M. !$#journal Nature (2000) 406:477-483 !$#title DNA Sequence of both chromosomes of the cholera pathogen !1Vibrio cholerae. !$#cross-references MUID:20406833; PMID:10952301 !$#accession B82407 !'##status preliminary !'##molecule_type DNA !'##residues 1-609 ##label HEI !'##cross-references GB:AE004414; GB:AE003853; NID:g9658293; !1PIDN:AAF96763.1; GSPDB:GN00127; TIGR:VCA0865 !'##experimental_source serogroup O1; strain N16961; biotype El Tor GENETICS !$#gene VCA0865 !$#map_position 2 CLASSIFICATION #superfamily thermolysin KEYWORDS hydrolase; metalloproteinase; zinc FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-195 #domain propeptide #status predicted #label PRO\ !$196-609 #product vibriolysin #status predicted #label MAT\ !$231-257,473-502 #disulfide_bonds #status predicted\ !$343,347,367 #binding_site zinc (His, His, Glu) #status predicted\ !$344,426 #active_site Glu, His #status predicted SUMMARY #length 609 #molecular-weight 65891 #checksum 405 SEQUENCE /// ENTRY HYSMCA #type complete TITLE mycolysin (EC 3.4.24.31) precursor - Streptomyces cacaoi ALTERNATE_NAMES neutral metalloproteinase; pronase component ORGANISM #formal_name Streptomyces cacaoi DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS JQ0530; A42262 REFERENCE JQ0530 !$#authors Chang, P.C.; Kuo, T.C.; Tsugita, A.; Lee, Y.H.W. !$#journal Gene (1990) 88:87-95 !$#title Extracellular metalloprotease gene of Streptomyces cacaoi: !1structure, nucleotide sequence and characterization of the !1cloned gene product. !$#cross-references MUID:90255973; PMID:2341042 !$#accession JQ0530 !'##molecule_type DNA !'##residues 1-550 ##label CHA !'##cross-references GB:M37055; NID:g153374; PIDN:AAA26789.1; !1PID:g153375 !'##experimental_source strain YM15 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE A42262 !$#authors Chang, P.C.; Lee, Y.H.W. !$#journal J. Biol. Chem. (1992) 267:3952-3958 !$#title Extracellular autoprocessing of a metalloprotease from !1Streptomyces cacaoi. !$#cross-references MUID:92156138; PMID:1740443 !$#accession A42262 !'##molecule_type protein !'##residues 35-49;206-214 ##label CH2 GENETICS !$#gene npr CLASSIFICATION #superfamily mycolysin KEYWORDS extracellular protein; hydrolase; metalloproteinase; zinc FEATURE !$1-34 #domain signal sequence #status predicted #label SIG\ !$35-205 #domain propeptide #status experimental #label PRO\ !$206-550 #product mycolysin #status experimental #label MAT\ !$407,411,445 #binding_site zinc (His, His, Glu) #status !8experimental\ !$408 #active_site Glu #status experimental SUMMARY #length 550 #molecular-weight 58678 #checksum 9210 SEQUENCE /// ENTRY LYYXLY #type complete TITLE beta-lytic metalloendopeptidase (EC 3.4.24.32) precursor - Achromobacter lyticus ALTERNATE_NAMES achromopeptidase component; beta-lytic proteinase ORGANISM #formal_name Achromobacter lyticus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS A37151; B37151 REFERENCE A37151 !$#authors Li, S.L.; Norioka, S.; Sakiyama, F. !$#journal J. Bacteriol. (1990) 172:6506-6511 !$#title Molecular cloning and nucleotide sequence of the beta-lytic !1protease gene from Achromobacter lyticus. !$#cross-references MUID:91035265; PMID:2228973 !$#accession A37151 !'##molecule_type DNA !'##residues 1-374 ##label LIA1 !'##cross-references GB:M60896; NID:g141805; PIDN:AAA21906.1; !1PID:g141806 !'##experimental_source strain M497-1 !$#accession B37151 !'##molecule_type protein !'##residues 196-219 ##label LIA2 CLASSIFICATION #superfamily beta-lytic metalloendopeptidase KEYWORDS cell wall lysis; hydrolase; metalloproteinase; zinc FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-195 #domain propeptide #status predicted #label PRO\ !$196-374 #product beta-lytic metalloendopeptidase #status !8experimental #label MAT\ !$261-307,351-364 #disulfide_bonds #status predicted SUMMARY #length 374 #molecular-weight 40084 #checksum 9460 SEQUENCE /// ENTRY LYYXB4 #type complete TITLE beta-lytic metalloendopeptidase (EC 3.4.24.32) - Lysobacter enzymogenes ALTERNATE_NAMES achromopeptidase component; beta-lytic proteinase ORGANISM #formal_name Lysobacter enzymogenes DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 17-Feb-1995 ACCESSIONS A00994 REFERENCE A00994 !$#authors Damaglou, A.P.; Allen, L.C.; Whitaker, D.R. !$#submission submitted to the Atlas, March 1974 !$#accession A00994 !'##molecule_type protein !'##residues 1-178 ##label DAM !'##experimental_source ATCC 29487 CLASSIFICATION #superfamily beta-lytic metalloendopeptidase KEYWORDS cell wall lysis; hydrolase; metalloproteinase; zinc FEATURE !$65-111,155-168 #disulfide_bonds #status predicted SUMMARY #length 178 #molecular-weight 19100 #checksum 4630 SEQUENCE /// ENTRY A45621 #type complete TITLE leishmanolysin (EC 3.4.24.36) precursor - Leishmania donovani ALTERNATE_NAMES surfase endopeptidase glycoprotein gp63 ORGANISM #formal_name Leishmania donovani DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jan-2000 ACCESSIONS A45621 REFERENCE A45621 !$#authors Webb, J.R.; Button, L.L.; McMaster, W.R. !$#journal Mol. Biochem. Parasitol. (1991) 48:173-184 !$#title Heterogeneity of the genes encoding the major surface !1glycoprotein of Leishmania donovani. !$#cross-references MUID:92107220; PMID:1762629 !$#accession A45621 !'##status preliminary !'##molecule_type DNA !'##residues 1-590 ##label WEB !'##experimental_source LV9 !'##note sequence extracted from NCBI backbone (NCBIN:74958, !1NCBIP:74959) FUNCTION !$#description catalyzes the hydrolysis of peptide bonds between two !1hydrophobic residues followed by one or two basic residues !$#note the activated form can activate the proenzyme form CLASSIFICATION #superfamily leishmanolysin KEYWORDS blocked carboxyl end; cell adhesion; glycoprotein; !1hydrolase; lipoprotein; membrane bound; metalloproteinase; !1phosphatidylinositol linkage; phosphoprotein; zinc; zymogen FEATURE !$1-39 #domain signal sequence #status predicted #label SIG\ !$40-87 #domain activation peptide #status predicted #label !8ATP\ !$88-565 #product leishmanolysin #status predicted #label MAT\ !$566-590 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$48,251,255,321 #binding_site zinc, catalytic (Cys, His, His, His) !8(inhibited) #status predicted\ !$112-129,178-217, !$301-373,380-443, !$393-412,402-477, !$454-498,503-553, !$523-546 #disulfide_bonds #status predicted\ !$251,255,321 #binding_site zinc, catalytic (His) (active) #status !8predicted\ !$252 #active_site Glu #status predicted\ !$287 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$565 #modified_site GPI-anchor ethanolamine amidated !8carboxyl end (Asn) (in mature form) #status predicted SUMMARY #length 590 #molecular-weight 63037 #checksum 7579 SEQUENCE /// ENTRY PL0221 #type complete TITLE leishmanolysin (EC 3.4.24.36) precursor [validated] - Leishmania major ALTERNATE_NAMES promastigote surface proteinase; surface endopeptidase glycoprotein gp63 ORGANISM #formal_name Leishmania major DATE 16-Sep-1992 #sequence_revision 16-Sep-1992 #text_change 15-Sep-2000 ACCESSIONS PL0221; A27598; A60648 REFERENCE PL0221 !$#authors Button, L.L.; McMaster, W.R. !$#journal J. Exp. Med. (1990) 171:589 !$#contents erratum !$#accession PL0221 !'##molecule_type DNA !'##residues 1-602 ##label BUT !'##cross-references GB:Y00647; NID:g9554; PIDN:CAA68673.1; PID:g9555 !'##note this is a revision to the sequence from reference A27598 REFERENCE A27598 !$#authors Button, L.L.; McMaster, W.R. !$#journal J. Exp. Med. (1988) 167:724-729 !$#title Molecular cloning of the major surface antigen of !1Leishmania. !$#cross-references MUID:88154764; PMID:3346625 !$#accession A27598 !'##status significant sequence differences !'##molecule_type DNA REFERENCE A60648 !$#authors Bouvier, J.; Bordier, C.; Vogel, H.; Reichelt, R.; Etges, R. !$#journal Mol. Biochem. Parasitol. (1989) 37:235-246 !$#title Characterization of the promastigote surface protease of !1Leishmania as a membrane-bound zinc endopeptidase. !$#cross-references MUID:90114330; PMID:2608099 !$#accession A60648 !'##molecule_type protein !'##residues 101,'E',103-118,'SV',121-123 ##label BOU !'##experimental_source strain LEM513 REFERENCE A68135 !$#authors Schlagenhauf, E.; Etges, R.; Metcalf, P. !$#submission submitted to the Brookhaven Protein Data Bank, March 1997 !$#cross-references PDB:1LML !$#contents annotation; X-ray crystallography, 1.86 angstroms, residues !1100-407,412-498,505-574 !$#note strain LRC-L119 COMPLEX homodimer FUNCTION !$#description catalyzes the hydrolysis of peptide bonds between two !1hydrophobic residues followed by one or two basic residues !$#note the activated form can activate the proenzyme form CLASSIFICATION #superfamily leishmanolysin KEYWORDS blocked carboxyl end; cell adhesion; glycoprotein; !1homodimer; hydrolase; lipoprotein; membrane bound; !1metalloproteinase; phosphatidylinositol linkage; !1phosphoprotein; zinc; zymogen FEATURE !$1-39 #domain signal sequence #status predicted #label SIG\ !$40-100 #domain activation peptide #status predicted #label !8ATP\ !$101-577 #product leishmanolysin #status experimental #label !8MAT\ !$578-602 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$48,264,268,334 #binding_site zinc, catalytic (Cys, His, His, His) !8(inhibited) #status predicted\ !$100-101 #cleavage_site Val-Val (autolytic) #status !8experimental\ !$125-142,191-230, !$314-386,393-455, !$406-425,415-489, !$466-510,515-565, !$535-558 #disulfide_bonds #status experimental\ !$264,268,334 #binding_site zinc, catalytic (His) (active) #status !8experimental\ !$265 #active_site Glu #status predicted\ !$300,407 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$577 #modified_site GPI-anchor ethanolamine amidated !8carboxyl end (Asn) (in mature form) #status predicted SUMMARY #length 602 #molecular-weight 63953 #checksum 775 SEQUENCE /// ENTRY S19916 #type complete TITLE leishmanolysin (EC 3.4.24.36) precursor - Leishmania mexicana ALTERNATE_NAMES surface metalloproteinase glycoprotein gp63 ORGANISM #formal_name Leishmania mexicana DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S19916; A48564 REFERENCE S19916 !$#authors Medina-Acosta, E.; Karess, R.E.; Russell, D. !$#submission submitted to the EMBL Data Library, February 1992 !$#description Structurally distinct genes for the surface protease (gp63) !1of Leishmania mexicana are developmentally regulated. !$#accession S19916 !'##molecule_type mRNA !'##residues 1-646 ##label MED !'##cross-references EMBL:X64394; NID:g9559; PIDN:CAA45733.1; PID:g9560 REFERENCE A48564 !$#authors Medina-Acosta, E.; Karess, R.E.; Russell, D.G. !$#journal Mol. Biochem. Parasitol. (1993) 57:31-45 !$#title Structurally distinct genes for the surface protease of !1Leishmania mexicana are developmentally regulated. !$#cross-references MUID:93149206; PMID:8426614 !$#accession A48564 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-176,'Q',178-646 ##label ME2 !'##cross-references EMBL:X64394; NID:g9559 !'##note sequence extracted from NCBI backbone (NCBIP:123747) GENETICS !$#gene gp63-C1 !$#map_position 700kb chromosomal band FUNCTION !$#description catalyzes the hydrolysis of peptide bonds between two !1hydropho !$#note the activated form can activate the proenzyme form CLASSIFICATION #superfamily leishmanolysin KEYWORDS cell adhesion; glycoprotein; hydrolase; membrane bound; !1metalloproteinase; zinc; zymogen FEATURE !$1-39 #domain signal sequence #status predicted #label SIG\ !$40-102 #domain activation peptide #status predicted #label !8ATP\ !$103-646 #product leishmanolysin #status predicted #label MAT\ !$604-620 #domain transmembrane #status predicted #label TM1\ !$48,266,270,336 #binding_site zinc, catalytic (Cys, His, His, His) !8(inhibited) #status predicted\ !$86,297,399,409,433, !$445,466,501 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$127-144,193-232, !$316-388,395-458, !$408-427,417-492, !$469-513,518-568, !$538-561 #disulfide_bonds #status experimental\ !$266,270,336 #binding_site zinc, catalytic (His) (active) #status !8predicted\ !$267 #active_site Glu #status predicted SUMMARY #length 646 #molecular-weight 69054 #checksum 7422 SEQUENCE /// ENTRY HYSE15 #type complete TITLE serralysin (EC 3.4.24.40) precursor - Serratia sp. (strain E-15) ALTERNATE_NAMES extracellular proteinase ORGANISM #formal_name Serratia sp. DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS A23596; A37310; A05321 REFERENCE A23596 !$#authors Nakahama, K.; Yoshimura, K.; Marumoto, R.; Kikuchi, M.; Lee, !1I.S.; Hase, T.; Matsubara, H. !$#journal Nucleic Acids Res. (1986) 14:5843-5855 !$#title Cloning and sequencing of Serratia protease gene. !$#cross-references MUID:86286592; PMID:3016665 !$#accession A23596 !'##molecule_type DNA !'##residues 1-486 ##label NAK !'##cross-references EMBL:X04127; NID:g47590; PIDN:CAA27738.1; !1PID:g47591 REFERENCE A37310 !$#authors Lee, I.S.; Wakabayashi, S.; Matsubara, H.; Miyata, K.; !1Tomoda, K. !$#journal Fed. Proc. (1985) 44:1057 !$#title Serratia protease. Amino acid sequences of the N-terminal !1half including a zinc binding site and of the C-terminal !1peptide. !$#accession A37310 !'##molecule_type protein !'##residues 17-35,'D',37-40,'GD',43-62,'D',64-294;474-486 ##label LEE CLASSIFICATION #superfamily serralysin KEYWORDS extracellular protein; hydrolase; metalloproteinase; tandem !1repeat; zinc FEATURE !$1-16 #domain propeptide #status predicted #label PRO\ !$17-486 #product serralysin #status experimental #label MAT\ !$363-389 #region 9-residue repeats (V-L-X-G-G-A-G-X-D)\ !$192,196,202,232 #binding_site zinc (His, His, His, Tyr) #status !8predicted\ !$193 #active_site Glu #status predicted SUMMARY #length 486 #molecular-weight 52406 #checksum 6995 SEQUENCE /// ENTRY S26699 #type complete TITLE alkaline metalloproteinase (EC 3.4.24.-) aprA precursor - Pseudomonas aeruginosa ALTERNATE_NAMES alkaline proteinase ORGANISM #formal_name Pseudomonas aeruginosa DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 31-Dec-2000 ACCESSIONS S26699; A83490 REFERENCE S26696 !$#authors Duong, F.; Lazdunski, A.; Cami, B.; Murgier, M. !$#journal Gene (1992) 121:47-54 !$#title Sequence of a cluster of genes controlling synthesis and !1secretion of alkaline protease in Pseudomonas aeruginosa: !1relationships to other secretory pathways. !$#cross-references MUID:93051361; PMID:1427098 !$#accession S26699 !'##status preliminary !'##molecule_type DNA !'##residues 1-479 ##label DUO !'##cross-references EMBL:X64558; NID:g45279; PIDN:CAA45858.1; !1PID:g45283 REFERENCE A82950 !$#authors Stover, C.K.; Pham, X.Q.; Erwin, A.L.; Mizoguchi, S.D.; !1Warrener, P.; Hickey, M.J.; Brinkman, F.S.L.; Hufnagle, !1W.O.; Kowalik, D.J.; Lagrou, M.; Garber, R.L.; Goltry, L.; !1Tolentino, E.; Westbrook-Wadman, S.; Yuan, Y.; Brody, L.L.; !1Coulter, S.N.; Folger, K.R.; Kas, A.; Larbig, K.; Lim, R.M.; !1Smith, K.A.; Spencer, D.H.; Wong, G.K.S.; Wu, Z.; Paulsen, !1I.T.; Reizer, J.; Saier, M.H.; Hancock, R.E.W.; Lory, S.; !1Olson, M.V. !$#journal Nature (2000) 406:959-964 !$#title Complete genome sequence of Pseudomonas aeruginosa PA01, an !1opportunistic pathogen. !$#cross-references MUID:20437337; PMID:10984043 !$#accession A83490 !'##status preliminary !'##molecule_type DNA !'##residues 1-479 ##label STO !'##cross-references GB:AE004554; GB:AE004091; NID:g9947174; !1PIDN:AAG04638.1; GSPDB:GN00131; PASP:PA1249 !'##experimental_source strain PAO1 GENETICS !$#gene aprA; PA1249 CLASSIFICATION #superfamily serralysin KEYWORDS hydrolase; metalloproteinase; zinc FEATURE !$185,189,195,225 #binding_site zinc (His, His, His, Tyr) #status !8predicted\ !$186 #active_site Glu #status predicted SUMMARY #length 479 #molecular-weight 50432 #checksum 3628 SEQUENCE /// ENTRY HYRSAC #type complete TITLE atrolysin C (EC 3.4.24.42) precursor - western diamondback rattlesnake ALTERNATE_NAMES Crotalus atrox metalloendopeptidase c; hemorrhagic toxin c; hemorrhagic toxin d ORGANISM #formal_name Crotalus atrox #common_name western diamondback rattlesnake DATE 30-Sep-1992 #sequence_revision 12-Apr-1996 #text_change 18-Jun-1999 ACCESSIONS S41610; A34166 REFERENCE S41607 !$#authors Hite, L.A.; Jia, L.G.; Bjarnason, J.B.; Fox, J.W. !$#journal Arch. Biochem. Biophys. (1994) 308:182-191 !$#title cDNA sequences for four snake venom metalloproteinases: !1structure, classification, and their relationship to !1mammalian reproductive proteins. !$#cross-references MUID:94145078; PMID:8311451 !$#accession S41610 !'##status preliminary; translation not shown !'##molecule_type mRNA !'##residues 1-414 ##label HIT !'##cross-references GB:U01237; NID:g402263; PIDN:AAA03352.1; !1PID:g402264 REFERENCE A34166 !$#authors Shannon, J.D.; Baramova, E.N.; Bjarnason, J.B.; Fox, J.W. !$#journal J. Biol. Chem. (1989) 264:11575-11583 !$#title Amino acid sequence of a Crotalus atrox venom !1metalloproteinase which cleaves type IV collagen and !1gelatin. !$#cross-references MUID:89308543; PMID:2745407 !$#accession A34166 !'##molecule_type protein !'##residues 191-393 ##label SHA !'##note 204-Ile was also found !'##note a variant lacking 192-Gln was also found CLASSIFICATION #superfamily atrolysin C KEYWORDS hydrolase; metalloproteinase; pyroglutamic acid; venom; zinc FEATURE !$1-12 #domain signal sequence #status predicted #label SIG\ !$13-190 #domain amino-terminal propeptide #status predicted !8#label PRO\ !$191-393 #product atrolysin C #status experimental #label MAT\ !$394-414 #domain carboxyl-terminal propeptide #status !8predicted #label CPT\ !$191 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$308-388,348-355 #disulfide_bonds #status experimental\ !$333,337,343 #binding_site zinc (His) #status predicted\ !$334 #active_site Glu #status predicted SUMMARY #length 414 #molecular-weight 46844 #checksum 2452 SEQUENCE /// ENTRY HYRSR #type complete TITLE ruberlysin (EC 3.4.24.48) - red diamond rattlesnake ALTERNATE_NAMES Crotalus ruber metalloendopeptidase II; hemorrhagic metalloproteinase HT-2; hemorrhagic toxin II ORGANISM #formal_name Crotalus ruber ruber #common_name red diamond rattlesnake DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 05-Aug-1994 ACCESSIONS JX0139 REFERENCE JX0139 !$#authors Takeya, H.; Onikura, A.; Nikai, T.; Sugihara, H.; Iwanaga, !1S. !$#journal J. Biochem. (1990) 108:711-719 !$#title Primary structure of a hemorrhagic metalloproteinase, HT-2, !1isolated from the venom of Crotalus ruber ruber. !$#cross-references MUID:91185324; PMID:2081731 !$#accession JX0139 !'##molecule_type protein !'##residues 1-202 ##label TAK CLASSIFICATION #superfamily atrolysin C KEYWORDS hydrolase; metalloproteinase; pyroglutamic acid; venom; zinc FEATURE !$1 #modified_site pyrrolidone carboxylic acid (Gln) !8#status experimental\ !$117-197,157-164 #disulfide_bonds #status experimental\ !$142,146,152 #binding_site zinc (His) #status predicted\ !$143 #active_site Glu #status predicted SUMMARY #length 202 #molecular-weight 23320 #checksum 6836 SEQUENCE /// ENTRY HYSNFA #type complete TITLE fibrolase (EC 3.4.24.-) precursor - southern copperhead ORGANISM #formal_name Agkistrodon contortrix contortrix #common_name southern copperhead DATE 30-Sep-1992 #sequence_revision 09-Apr-1998 #text_change 18-Jun-1999 ACCESSIONS S66259; A41827; S25461; A37303 REFERENCE S66259 !$#authors Selistre de Araujo, H.S.; Ownby, C.L. !$#journal Arch. Biochem. Biophys. (1995) 320:141-148 !$#title Molecular cloning and sequence analysis of cDNAs for !1metalloproteinases from broad-banded copperhead Agkistrodon !1contortrix laticinctus. !$#cross-references MUID:95314311; PMID:7793974 !$#accession S66259 !'##molecule_type mRNA !'##residues 1-411 ##label SEL !'##cross-references EMBL:U18233; NID:g603214; PIDN:AAC59703.1; !1PID:g603215 REFERENCE A37303 !$#authors Randolph, A.; Chamberlain, S.H.; Chu, H.L.C.; Retzios, A.D.; !1Markland Jr., F.S.; Masiarz, F.R. !$#journal Protein Sci. (1992) 1:590-600 !$#title Amino acid sequence of fibrolase, a direct-acting !1fibrinolytic enzyme from Agkistrodon contortrix contortrix !1venom. !$#cross-references MUID:93278288; PMID:1304358 !$#accession A41827 !'##molecule_type protein !'##residues 191-192,'R',194-199,'Q',201-240,'Q',242,'T',244-357,'AAM', !1361-381,'T',383-393 ##label RAN !'##note 379-Glu and 382-Leu were also found !'##note a variant lacking 192-Gln was also found REFERENCE S17490 !$#authors Guan, A.L.; Retzios, A.D.; Henderson, G.N.; Markland Jr., !1F.S. !$#journal Arch. Biochem. Biophys. (1991) 289:197-207 !$#title Purification and characterization of a fibrinolytic enzyme !1from venom of the southern copperhead snake (Agkistrodon !1contortrix contortrix). !$#cross-references MUID:91378546; PMID:1898066 !$#accession S25461 !'##molecule_type protein !'##residues 331-341 ##label GUA GENETICS !$#gene ACLPREF CLASSIFICATION #superfamily atrolysin C KEYWORDS hydrolase; metalloproteinase; pyroglutamic acid; venom; zinc FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-190 #domain propeptide #status predicted #label PRO\ !$191-411 #product fibrolase #status experimental #label MAT\ !$191 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$308-388 #disulfide_bonds #status experimental\ !$333,337,343 #binding_site zinc (His) #status predicted\ !$334 #active_site Glu #status predicted\ !$348-355,350-372 #disulfide_bonds #status predicted SUMMARY #length 411 #molecular-weight 46231 #checksum 3092 SEQUENCE /// ENTRY HYTV2 #type complete TITLE trimerelysin II (EC 3.4.24.53) - habu ALTERNATE_NAMES proteinase H2; Trimeresurus metalloendopeptidase II ORGANISM #formal_name Trimeresurus flavoviridis #common_name habu DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 05-Aug-1994 ACCESSIONS JU0037 REFERENCE JU0037 !$#authors Takeya, H.; Arakawa, M.; Miyata, T.; Iwanaga, S.; !1Omori-Satoh, T. !$#journal J. Biochem. (1989) 106:151-157 !$#title Primary structure of H-2-proteinase, a non-hemorrhagic !1metalloproteinase, isolated from the venom of the habu !1snake, Trimeresurus flavoviridis. !$#cross-references MUID:89380121; PMID:2777746 !$#accession JU0037 !'##molecule_type protein !'##residues 1-201 ##label TAK COMMENT This proteinase is a major venom non-hemorrhagic !1metalloproteinase. CLASSIFICATION #superfamily atrolysin C KEYWORDS hydrolase; metalloproteinase; pyroglutamic acid; venom; zinc FEATURE !$1 #modified_site pyrrolidone carboxylic acid (Gln) !8#status experimental\ !$117-196,158-180, !$160-163 #disulfide_bonds #status experimental\ !$142,146,152 #binding_site zinc (His) #status predicted\ !$143 #active_site Glu #status predicted SUMMARY #length 201 #molecular-weight 23014 #checksum 2883 SEQUENCE /// ENTRY HYTVH2 #type complete TITLE hemorrhagic protein HR2a (EC 3.4.24.-) - habu ORGANISM #formal_name Trimeresurus flavoviridis #common_name habu DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 06-Dec-1996 ACCESSIONS JX0074 REFERENCE JX0074 !$#authors Miyata, T.; Takeya, H.; Ozeki, Y.; Arakawa, M.; Tokunaga, !1F.; Iwanaga, S.; Omori-Satoh, T. !$#journal J. Biochem. (1989) 105:847-853 !$#title Primary structure of hemorrhagic protein, HR2a, isolated !1from the venom of Trimeresurus flavoviridis. !$#cross-references MUID:89327213; PMID:2753880 !$#accession JX0074 !'##molecule_type protein !'##residues 1-202 ##label MIY !'##experimental_source venom !'##note a variant lacking 2-Gln was also found CLASSIFICATION #superfamily atrolysin C KEYWORDS glycoprotein; hydrolase; metalloproteinase; pyroglutamic !1acid; venom; zinc FEATURE !$1 #modified_site pyrrolidone carboxylic acid (Gln) !8#status experimental\ !$103 #binding_site carbohydrate (Asn) (covalent) #status !8absent\ !$118-197,159-181, !$161-164 #disulfide_bonds #status experimental\ !$143,147,153 #binding_site zinc (His) #status predicted\ !$144 #active_site Glu #status predicted SUMMARY #length 202 #molecular-weight 23038 #checksum 4865 SEQUENCE /// ENTRY A30065 #type complete TITLE trigramin precursor - Indian green tree viper CONTAINS hemorrhagic proteinase (EC 3.4.24.-); platelet aggregation inhibitor (disintegrin) trigramin ORGANISM #formal_name Trimeresurus gramineus #common_name Indian green tree viper DATE 16-Sep-1992 #sequence_revision 16-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS S12589; A30065; A29784 REFERENCE S12589 !$#authors Neeper, M.P.; Jacobson, M.A. !$#journal Nucleic Acids Res. (1990) 18:4255 !$#title Sequence of a cDNA encoding the platelet aggregation !1inhibitor trigramin. !$#cross-references MUID:90332429; PMID:2377470 !$#accession S12589 !'##molecule_type mRNA !'##residues 1-480 ##label NEE !'##cross-references EMBL:X51530; NID:g64407; PIDN:CAA35910.1; !1PID:g64408 !'##note translation of the signal sequence and the mature protein but !1not of the propeptide is given REFERENCE A30065 !$#authors Huang, T.F.; Holt, J.C.; Kirby, E.P.; Niewiarowski, S. !$#journal Biochemistry (1989) 28:661-666 !$#title Trigramin: primary structure and its inhibition of von !1Willebrand factor binding to glycoprotein IIb/IIIa complex !1on human platelets. !$#cross-references MUID:89229063; PMID:2653425 !$#accession A30065 !'##molecule_type protein !'##residues 408-479 ##label HUA REFERENCE A29784 !$#authors Huang, T.F.; Holt, J.C.; Lukasiewicz, H.; Niewiarowski, S. !$#journal J. Biol. Chem. (1987) 262:16157-16163 !$#title Trigramin. A low molecular weight peptide inhibiting !1fibrinogen interaction with platelet receptors expressed on !1glycoprotein IIb-IIIa complex. !$#cross-references MUID:88058981; PMID:3680247 !$#accession A29784 !'##molecule_type protein !'##residues 408-419 ##label HU2 CLASSIFICATION #superfamily trigramin precursor; disintegrin homology KEYWORDS anticoagulant; glycoprotein; hydrolase; metalloproteinase; !1venom; zinc; zymogen FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$398-476 #domain disintegrin homology #label DIS\ !$408-479 #product trigramin #status experimental #label MAT\ !$458-460 #region cell attachment (R-G-D) motif\ !$279 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$333,337,343 #binding_site zinc (His) #status predicted\ !$334 #active_site Glu #status predicted SUMMARY #length 480 #molecular-weight 53494 #checksum 1021 SEQUENCE /// ENTRY ZPECS #type complete TITLE signal peptidase I (EC 3.4.21.89) - Escherichia coli (strain K-12) ALTERNATE_NAMES leader peptidase; SPase I ORGANISM #formal_name Escherichia coli DATE 25-Feb-1985 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS G65034; A00998 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65034 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-324 ##label BLAT !'##cross-references GB:AE000343; GB:U00096; NID:g2367139; !1PIDN:AAC75621.1; PID:g1788921; UWGP:b2568 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A00998 !$#authors Wolfe, P.B.; Wickner, W.; Goodman, J.M. !$#journal J. Biol. Chem. (1983) 258:12073-12080 !$#title Sequence of the leader peptidase gene of Escherichia coli !1and the orientation of leader peptidase in the bacterial !1envelope. !$#cross-references MUID:84008229; PMID:6311837 !$#accession A00998 !'##molecule_type DNA !'##residues 1-41,'R',44-122,'N',124-182,'A',184-324 ##label WOL !'##cross-references GB:K00426; GB:J03295; NID:g146598; PIDN:AAA24064.1; !1PID:g146600 COMMENT This enzyme catalyzes the removal of signal peptides from !1membrane and secreted protein precursors in E. coli; it is !1found in the inner membrane of the cell with most of the !1polypeptide chain exposed on the outer surface. It is !1distinct from the lipoprotein signal peptidase, which !1specifically removes signal peptides from prolipoproteins. GENETICS !$#gene lepB; lep !$#map_position 55 min CLASSIFICATION #superfamily signal peptidase I KEYWORDS blocked amino end; hydrolase; serine proteinase; !1transmembrane protein FEATURE !$4-22 #domain transmembrane #status experimental #label !8TM1\ !$23-62 #domain intracellular #status experimental #label !8INT\ !$63-77 #domain transmembrane #status experimental #label !8TM2\ !$1 #modified_site blocked amino end (Met) #status !8experimental SUMMARY #length 324 #molecular-weight 35960 #checksum 8977 SEQUENCE /// ENTRY S48484 #type complete TITLE signal peptidase (EC 3.4.99.-) SEC11 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YIR022w; signal sequence-processing protein SEC11 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 12-Nov-1999 ACCESSIONS S48484; A30184 REFERENCE S48478 !$#authors Rowley, K. !$#submission submitted to the EMBL Data Library, October 1994 !$#accession S48484 !'##molecule_type DNA !'##residues 1-167 ##label ROW !'##cross-references GB:Z47047; EMBL:Z38061; NID:g603997; PID:g763367; !1GSPDB:GN00009; MIPS:YIR022w REFERENCE A30184 !$#authors Boehni, P.C.; Deshaies, R.J.; Schekman, R.W. !$#journal J. Cell Biol. (1988) 106:1035-1042 !$#title SEC11 is required for signal peptide processing and yeast !1cell growth. !$#cross-references MUID:88198347; PMID:3283143 !$#accession A30184 !'##molecule_type DNA !'##residues 1-161,'R',163-167 ##label BOE !'##cross-references GB:X07694; NID:g4432; PIDN:CAA30533.1; PID:g4433 GENETICS !$#gene SGD:SEC11; MIPS:YIR022w !'##cross-references SGD:S0001461; MIPS:YIR022w !$#map_position 9R CLASSIFICATION #superfamily signal peptidase SEC11 KEYWORDS hydrolase; transmembrane protein FEATURE !$13-29 #domain transmembrane #status predicted #label TMM SUMMARY #length 167 #molecular-weight 18762 #checksum 8300 SEQUENCE /// ENTRY ZPBOC1 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) core protein I precursor - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 03-Jun-2002 ACCESSIONS S16220 REFERENCE S16220 !$#authors Gencic, S.; Schaegger, H.; von Jagow, G. !$#journal Eur. J. Biochem. (1991) 199:123-131 !$#title Core I protein of bovine ubiquinol-cytochrome-c reductase; !1an additional member of the mitochondrial-protein-processing !1family. Cloning of bovine core I and core II cDNAs and !1primary structure of the proteins. !$#cross-references MUID:91293112; PMID:1712295 !$#accession S16220 !'##molecule_type mRNA !'##residues 1-362 ##label EUR !'##cross-references GB:X59692 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing CLASSIFICATION #superfamily mitochondrial processing peptidase alpha chain KEYWORDS hydrolase; mitochondrial matrix; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain FEATURE !$1-34 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$35-362 #product ubiquinol-cytochrome-c reductase core !8protein I #status experimental #label MAT SUMMARY #length 362 #molecular-weight 39359 #checksum 5351 SEQUENCE /// ENTRY A32629 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) core protein II precursor - human ORGANISM #formal_name Homo sapiens #common_name man DATE 21-May-1990 #sequence_revision 14-Jul-1994 #text_change 03-Jun-2002 ACCESSIONS A32629 REFERENCE A32629 !$#authors Hosokawa, Y.; Suzuki, H.; Toda, H.; Nishikimi, M.; Ozawa, T. !$#journal J. Biol. Chem. (1989) 264:13483-13488 !$#title Complementary DNA encoding core protein II of human !1mitochondrial cytochrome bc-1 complex. Substantial diversity !1in deduced primary structure from its yeast counterpart. !$#cross-references MUID:89340421; PMID:2547763 !$#accession A32629 !'##molecule_type mRNA !'##residues 1-453 ##label HOS !'##cross-references GB:J04973; NID:g180927; PIDN:AAA35710.1; !1PID:g180928 !'##note the authors translated the codon AGA for residue 360 as Thr GENETICS !$#gene GDB:UQCRC2 !'##cross-references GDB:141851; OMIM:191329 !$#map_position 16p12.3-16p12.3 CLASSIFICATION #superfamily mitochondrial processing peptidase alpha chain KEYWORDS hydrolase; mitochondrial matrix; mitochondrion; oxidative !1phosphorylation; oxidoreductase; proteinase; respiratory !1chain FEATURE !$1-14 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$15-453 #product ubiquinol-cytochrome-c reductase core !8protein II #status predicted #label MAT SUMMARY #length 453 #molecular-weight 48470 #checksum 879 SEQUENCE /// ENTRY ZPBOC2 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) core protein II precursor - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 03-Jun-2002 ACCESSIONS S16221; S14093 REFERENCE S16220 !$#authors Gencic, S.; Schaegger, H.; von Jagow, G. !$#journal Eur. J. Biochem. (1991) 199:123-131 !$#title Core I protein of bovine ubiquinol-cytochrome-c reductase; !1an additional member of the mitochondrial-protein-processing !1family. Cloning of bovine core I and core II cDNAs and !1primary structure of the proteins. !$#cross-references MUID:91293112; PMID:1712295 !$#accession S16221 !'##molecule_type mRNA !'##residues 1-453 ##label GEN !'##cross-references GB:X59693; NID:g299; PIDN:CAA42214.1; PID:g300 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE S14093 !$#authors Cocco, T.; Lorusso, M.; Sardanelli, A.M.; Minuto, M.; !1Ronchi, S.; Tedeschi, G.; Papa, S. !$#journal Eur. J. Biochem. (1991) 195:731-734 !$#title Structural and functional characteristics of polypeptide !1subunits of the bovine heart ubiquinol - cytochrome-c !1reductase complex. !$#cross-references MUID:91153313; PMID:1847870 !$#accession S14093 !'##molecule_type protein !'##residues 'T',16-40,'R',42-46 ##label COC CLASSIFICATION #superfamily mitochondrial processing peptidase alpha chain KEYWORDS hydrolase; mitochondrial matrix; mitochondrion; oxidative !1phosphorylation; oxidoreductase; proteinase; respiratory !1chain FEATURE !$1-14 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$15-453 #product ubiquinol-cytochrome-c reductase core !8protein II #status experimental #label MAT SUMMARY #length 453 #molecular-weight 48148 #checksum 9802 SEQUENCE /// ENTRY S29510 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) core protein II precursor - rat ALTERNATE_NAMES cytochrome bc1 complex core protein II ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 07-May-1993 #sequence_revision 14-Jul-1994 #text_change 03-Jun-2002 ACCESSIONS S29510 REFERENCE S29510 !$#authors Hosokawa, Y.; Suzuki, H.; Toda, H.; Nishikimi, M.; Ozawa, T. !$#journal Biochem. Int. (1990) 20:731-737 !$#title The primary structure of the precursor to core protein II, a !1putative member of mitochondrial processing protease family, !1of rat mitochondrial cytochrome bc1 complex deduced from !1cDNA sequence analysis. !$#cross-references MUID:90282728; PMID:2162168 !$#accession S29510 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-452 ##label HOS GENETICS !$#genome nuclear CLASSIFICATION #superfamily mitochondrial processing peptidase alpha chain KEYWORDS mitochondrial matrix; mitochondrion; oxidative !1phosphorylation; oxidoreductase; respiratory chain FEATURE !$1-14 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$15-452 #product ubiquinol-cytochrome-c reductase core !8protein II #status predicted #label MAT SUMMARY #length 452 #molecular-weight 48373 #checksum 7597 SEQUENCE /// ENTRY ZPBY #type complete TITLE mitochondrial processing peptidase (EC 3.4.24.64) alpha chain precursor - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES mitochondrial processing peptidase chain MAS2; processing-enhancing protein chain 2; protein YHR024c ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 23-Mar-2001 ACCESSIONS S05738; S46778; S36360; B38734 REFERENCE S05738 !$#authors Pollock, R.A.; Hartl, F.U.; Cheng, M.Y.; Ostermann, J.; !1Horwich, A.; Neupert, W. !$#journal EMBO J. (1988) 7:3493-3500 !$#title The processing peptidase of yeast mitochondria: the two !1co-operating components MPP and PEP are structurally !1related. !$#cross-references MUID:89091093; PMID:3061797 !$#accession S05738 !'##molecule_type DNA !'##residues 1-482 ##label POL !'##cross-references EMBL:X13455; NID:g2948; PIDN:CAA31804.1; PID:g2949 !'##experimental_source strain MC3 REFERENCE S46773 !$#authors Du, Z. !$#submission submitted to the EMBL Data Library, June 1994 !$#description The sequence of S. cerevisiae cosmid 8082. !$#accession S46778 !'##molecule_type DNA !'##residues 1-482 ##label DUZ !'##cross-references EMBL:U10399; NID:g500689; PIDN:AAB68877.1; !1PID:g500696; GSPDB:GN00008; MIPS:YHR024c REFERENCE S36360 !$#authors Jensen, R.E.; Yaffe, M.P. !$#journal EMBO J. (1988) 7:3863-3871 !$#title Import of proteins into yeast mitochondria: the nuclear MAS2 !1gene encodes a component of the processing protease that is !1homologous to the MAS1-encoded subunit. !$#cross-references MUID:89091135; PMID:3061808 !$#accession S36360 !'##molecule_type DNA !'##residues 1-234,'P',236-482 ##label JEN !'##cross-references EMBL:X14105; NID:g3888; PIDN:CAA32262.1; PID:g3889 REFERENCE A38734 !$#authors Yang, M.; Geli, V.; Oppliger, W.; Suda, K.; James, P.; !1Schatz, G. !$#journal J. Biol. Chem. (1991) 266:6416-6423 !$#title The MAS-encoded processing protease of yeast mitochondria. !1Interaction of the purified enzyme with signal peptides and !1a purified precursor protein. !$#cross-references MUID:91177897; PMID:2007593 !$#accession B38734 !'##molecule_type protein !'##residues 14-22 ##label YAN GENETICS !$#gene SGD:MAS2; MPP; MIF2; MIPS:YHR024c !'##cross-references SGD:S0001066; MIPS:YHR024c !$#map_position 8R !$#genome nuclear COMPLEX heterodimer; alpha and beta chain FUNCTION !$#description cleavage of transit peptides upon transport into !1mitochondria; hydrolase; metalloproteinase CLASSIFICATION #superfamily mitochondrial processing peptidase alpha chain KEYWORDS heterodimer; hydrolase; metalloproteinase; mitochondrial !1matrix; mitochondrion FEATURE !$1-13 #domain transit peptide (mitochondrion) #status !8experimental #label TNP\ !$14-482 #product mitochondrial processing peptidase alpha !8chain #status experimental #label MAT SUMMARY #length 482 #molecular-weight 53337 #checksum 4410 SEQUENCE /// ENTRY A36205 #type complete TITLE mitochondrial processing peptidase (EC 3.4.24.64) alpha chain precursor [validated] - rat ALTERNATE_NAMES alpha-MPP; mitochondrial processing peptidase catalytic chain; MPP; P-55 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 28-Mar-1991 #sequence_revision 14-Jul-1994 #text_change 19-Jan-2001 ACCESSIONS A36205; B36205; S36361 REFERENCE A36205 !$#authors Kleiber, J.; Kalousek, F.; Swaroop, M.; Rosenberg, L.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:7978-7982 !$#title The general mitochondrial matrix processing protease from !1rat liver: structural characterization of the catalytic !1subunit. !$#cross-references MUID:91045920; PMID:2236012 !$#accession A36205 !'##molecule_type mRNA !'##residues 1-524 ##label KLE !'##cross-references GB:M57728; GB:M38282; NID:g205516; PIDN:AAA41632.1; !1PID:g205517 !$#accession B36205 !'##molecule_type protein !'##residues 'X',34-44;113-121;188-202;223-231;235-242;362-369;486-510 !1##label KL2 !'##experimental_source strain Sprague-Dawley; liver CLASSIFICATION #superfamily mitochondrial processing peptidase alpha chain KEYWORDS hydrolase; metalloproteinase; mitochondrial matrix; !1mitochondrion FEATURE !$1-32 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$33-524 #product mitochondrial processing peptidase alpha !8chain #status experimental #label MAT SUMMARY #length 524 #molecular-weight 58607 #checksum 6739 SEQUENCE /// ENTRY S23558 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) alpha chain precursor - potato ALTERNATE_NAMES alpha-MPP; mitochondrial processing peptidase catalytic chain; MPP; ubiquinol-cytochrome c reductase (EC 1.10.2.2) core protein III ORGANISM #formal_name Solanum tuberosum #common_name potato #variety Hansa DATE 22-Nov-1993 #sequence_revision 14-Jul-1994 #text_change 03-Jun-2002 ACCESSIONS S23558; S36127; S51633 REFERENCE S23558 !$#authors Braun, H.P.; Emmermann, M.; Kruft, V.; Schmitz, U.K. !$#journal EMBO J. (1992) 11:3219-3227 !$#title The general mitochondrial processing peptidase from potato !1is an integral part of cytochrome c reductase of the !1respiratory chain. !$#cross-references MUID:92371428; PMID:1324169 !$#accession S23558 !'##molecule_type mRNA !'##residues 1-504 ##label BRA !'##cross-references EMBL:X66284; NID:g21492; PIDN:CAA46990.1; !1PID:g21493 !'##note the sequence from Fig. 6 is inconsistent with that from Fig. 5 !1in lacking 317-Trp !$#accession S36127 !'##molecule_type protein !'##residues 270-280;400-419 ##label BR2 REFERENCE S51590 !$#authors Emmermann, M.; Braun, H.P.; Schmitz, U.K. !$#journal Mol. Gen. Genet. (1994) 245:237-245 !$#title The mitochondrial processing peptidase from potato: a !1self-processing enzyme encoded by two differentially !1expressed genes. !$#cross-references MUID:95115672; PMID:7816032 !$#accession S51633 !'##molecule_type protein !'##residues 25-38 ##label EMM !'##note the sequence from Fig. 5 is inconsistent with that from Fig. 2 !1in having 9-X GENETICS !$#genome nuclear CLASSIFICATION #superfamily mitochondrial processing peptidase alpha chain KEYWORDS hydrolase; metalloproteinase; mitochondrial matrix; !1mitochondrion; oxidative phosphorylation; oxidoreductase; !1respiratory chain FEATURE !$1-24 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$25-504 #product mitochondrial processing peptidase alpha !8chain #status experimental #label MAT SUMMARY #length 504 #molecular-weight 54677 #checksum 4870 SEQUENCE /// ENTRY A36442 #type complete TITLE mitochondrial processing peptidase (EC 3.4.24.64) alpha chain precursor - Neurospora crassa ALTERNATE_NAMES alpha-MPP; mitochondrial processing peptidase catalytic chain; MPP ORGANISM #formal_name Neurospora crassa DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 19-Jan-2001 ACCESSIONS A36442; S36362 REFERENCE A36442 !$#authors Schneider, H.; Arretz, M.; Wachter, E.; Neupert, W. !$#journal J. Biol. Chem. (1990) 265:9881-9887 !$#title Matrix processing peptidase of mitochondria. !1Structure-function relationships. !$#cross-references MUID:90277682; PMID:2141023 !$#accession A36442 !'##molecule_type mRNA !'##residues 1-577 ##label SCH1 !'##cross-references GB:J05484 REFERENCE S36362 !$#authors Schneider, H.; Arretz, M.; Wachter, E.; Neupert, W. !$#submission submitted to the EMBL Data Library, July 1990 !$#accession S36362 !'##molecule_type mRNA !'##residues 1-106,'A',108-577 ##label SCH2 !'##cross-references GB:J05484; NID:g168840; PIDN:AAA33597.1; !1PID:g168841 GENETICS !$#gene MPP !$#genome nuclear CLASSIFICATION #superfamily mitochondrial processing peptidase alpha chain KEYWORDS heterodimer; hydrolase; metalloproteinase; mitochondrial !1matrix; mitochondrion FEATURE !$1-35 #domain transit peptide (mitochondrion) #status !8predicted #label TPP\ !$36-577 #product mitochondrial processing peptidase alpha !8chain #status predicted #label MAT SUMMARY #length 577 #molecular-weight 63027 #checksum 4482 SEQUENCE /// ENTRY A29881 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) beta chain precursor - Neurospora crassa ALTERNATE_NAMES beta-MPP; mitochondrial processing peptidase enhancing protein; PEP; ubiquinol-cytochrome-c reductase (EC 1.10.2.2) core protein I ORGANISM #formal_name Neurospora crassa DATE 31-Dec-1993 #sequence_revision 14-Jul-1994 #text_change 03-Jun-2002 ACCESSIONS A29881; B29881; S03968 REFERENCE A29881 !$#authors Hawlitschek, G.; Schneider, H.; Schmidt, B.; Tropschug, M.; !1Hartl, F.U.; Neupert, W. !$#journal Cell (1988) 53:795-806 !$#title Mitochondrial protein import: identification of processing !1peptidase and of PEP, a processing enhancing protein. !$#cross-references MUID:88223372; PMID:2967109 !$#accession A29881 !'##molecule_type mRNA !'##residues 1-476 ##label HAW !'##cross-references EMBL:M20928; NID:g168857; PIDN:AAA33606.1; !1PID:g168858 !$#accession B29881 !'##molecule_type protein !'##residues 'XX',31-34 ##label HA2 REFERENCE S03968 !$#authors Schulte, U.; Arretz, M.; Schneider, H.; Tropschug, M.; !1Wachter, E.; Neupert, W.; Weiss, H. !$#journal Nature (1989) 339:147-149 !$#title A family of mitochondrial proteins involved in bioenergetics !1and biogenesis. !$#cross-references MUID:89238559; PMID:2524007 !$#accession S03968 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-476 ##label SCH !'##cross-references EMBL:M20928; NID:g168857; PIDN:AAA33606.1; !1PID:g168858 !'##note part of this sequence was confirmed by protein sequencing COMMENT In Neurospora crassa the beta chain of the mitochondrial !1processing peptidase and the core I protein of !1ubiquinol-cytochrome-c reductase are identical. The protein !1is bifunctional and participates both in protein processing !1and electron transport. CLASSIFICATION #superfamily mitochondrial processing peptidase alpha chain KEYWORDS heterodimer; hydrolase; metalloproteinase; mitochondrial !1matrix; mitochondrion; oxidative phosphorylation; !1oxidoreductase; respiratory chain FEATURE !$1-28 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$29-476 #product mitochondrial processing peptidase beta !8chain #status experimental #label MAT SUMMARY #length 476 #molecular-weight 52556 #checksum 9473 SEQUENCE /// ENTRY S00552 #type complete TITLE mitochondrial processing peptidase (EC 3.4.24.64) beta chain precursor - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES mitochondrial processing proteinase 48K chain; processing-enhancing protein; protein L9632_10; protein YLR163c ORGANISM #formal_name Saccharomyces cerevisiae DATE 28-Feb-1990 #sequence_revision 14-Jul-1994 #text_change 08-Dec-2000 ACCESSIONS S00552; A38734; S68479 REFERENCE S00552 !$#authors Witte, C.; Jensen, R.E.; Yaffe, M.P.; Schatz, G. !$#journal EMBO J. (1988) 7:1439-1447 !$#title MAS1, a gene essential for yeast mitochondrial assembly, !1encodes a subunit of the mitochondrial processing protease. !$#cross-references MUID:88312592; PMID:3044780 !$#accession S00552 !'##molecule_type DNA !'##residues 1-462 ##label WIT !'##cross-references EMBL:X07649; NID:g3886; PIDN:CAA30489.1; PID:g3887 REFERENCE A38734 !$#authors Yang, M.; Geli, V.; Oppliger, W.; Suda, K.; James, P.; !1Schatz, G. !$#journal J. Biol. Chem. (1991) 266:6416-6423 !$#title The MAS-encoded processing protease of yeast mitochondria. !1Interaction of the purified enzyme with signal peptides and !1a purified precursor protein. !$#cross-references MUID:91177897; PMID:2007593 !$#accession A38734 !'##molecule_type protein !'##residues 21-32 ##label YAN REFERENCE S68471 !$#authors Vaudin, M. !$#submission submitted to the EMBL Data Library, July 1996 !$#description The sequence of S. cerevisiae cosmid 9362. !$#accession S68479 !'##molecule_type DNA !'##residues 1-462 ##label VAU !'##cross-references EMBL:U51921; NID:g1234842; PIDN:AAB67487.1; !1PID:g1234852; GSPDB:GN00012; MIPS:YLR163c GENETICS !$#gene SGD:MAS1; MIF1; PEB; MIPS:YLR163c !'##cross-references SGD:S0004153; MIPS:YLR163c !$#map_position 12R !$#genome nuclear CLASSIFICATION #superfamily mitochondrial processing peptidase alpha chain KEYWORDS heterodimer; hydrolase; metalloproteinase; mitochondrial !1matrix; mitochondrion FEATURE !$1-20 #domain transit peptide (mitochondrion) #status !8experimental #label TNP\ !$21-462 #product mitochondrial processing peptidase beta !8chain #status experimental #label MAT SUMMARY #length 462 #molecular-weight 51083 #checksum 7257 SEQUENCE /// ENTRY S36390 #type complete TITLE mitochondrial processing peptidase (EC 3.4.24.64) beta chain precursor [validated] - rat ALTERNATE_NAMES beta-MPP; mitochondrial processing proteinase chain P52 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 09-Dec-1993 #sequence_revision 14-Jul-1994 #text_change 31-Dec-2000 ACCESSIONS S36390; S36391; PC1229 REFERENCE S36390 !$#authors Paces, V.; Rosenberg, L.E.; Fenton, W.A.; Kalousek, F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:5355-5358 !$#title The beta subunit of the mitochondrial processing peptidase !1from rat liver: cloning and sequencing of a cDNA and !1comparison with a proposed family of metallopeptidases. !$#cross-references MUID:93281757; PMID:8506385 !$#accession S36390 !'##molecule_type mRNA !'##residues 1-489 ##label PAC !'##cross-references GB:L12965; NID:g294588; PIDN:AAA41633.1; !1PID:g294589 !$#accession S36391 !'##molecule_type protein !'##residues 46-67;92-104;116-125;409-423;432-441 ##label PA2 GENETICS !$#genome nuclear CLASSIFICATION #superfamily mitochondrial processing peptidase alpha chain KEYWORDS heterodimer; hydrolase; metalloproteinase; mitochondrial !1matrix; mitochondrion; zinc FEATURE !$1-45 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$46-489 #product mitochondrial processing peptidase beta !8chain #status experimental #label MAT\ !$101,105 #binding_site zinc (His) #status predicted\ !$104 #active_site Glu #status predicted SUMMARY #length 489 #molecular-weight 54318 #checksum 4820 SEQUENCE /// ENTRY A48529 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) 55K protein precursor - potato ALTERNATE_NAMES P-55; ubiquinol-cytochrome-c reductase (EC 1.10.2.2) core protein I ORGANISM #formal_name Solanum tuberosum #common_name potato DATE 28-Mar-1994 #sequence_revision 14-Jul-1994 #text_change 03-Jun-2002 ACCESSIONS A48529 REFERENCE A48529 !$#authors Emmermann, M.; Braun, H.P.; Arretz, M.; Schmitz, U.K. !$#journal J. Biol. Chem. (1993) 268:18936-18942 !$#title Characterization of the bifunctional cytochrome c !1reductase-processing peptidase complex from potato !1mitochondria. !$#cross-references MUID:93366812; PMID:8360183 !$#accession A48529 !'##molecule_type mRNA !'##residues 1-534 ##label EMM !'##experimental_source var. Marfona, tuber !'##note sequence extracted from NCBI backbone (NCBIP:136740) CLASSIFICATION #superfamily mitochondrial processing peptidase alpha chain KEYWORDS hydrolase; metalloproteinase; mitochondrial matrix; !1mitochondrion; oxidative phosphorylation; oxidoreductase; !1respiratory chain FEATURE !$1-32 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$33-534 #product mitochondrial processing peptidase 55K !8protein #status experimental #label MAT SUMMARY #length 534 #molecular-weight 59933 #checksum 2729 SEQUENCE /// ENTRY B48529 #type complete TITLE ubiquinol-cytochrome-c reductase (EC 1.10.2.2) beta chain precursor - potato ALTERNATE_NAMES P-53; ubiquinol-cytochrome-c reductase (EC 1.10.2.2) core protein II ORGANISM #formal_name Solanum tuberosum #common_name potato DATE 28-Mar-1994 #sequence_revision 14-Jul-1994 #text_change 03-Jun-2002 ACCESSIONS B48529 REFERENCE A48529 !$#authors Emmermann, M.; Braun, H.P.; Arretz, M.; Schmitz, U.K. !$#journal J. Biol. Chem. (1993) 268:18936-18942 !$#title Characterization of the bifunctional cytochrome c !1reductase-processing peptidase complex from potato !1mitochondria. !$#cross-references MUID:93366812; PMID:8360183 !$#accession B48529 !'##molecule_type mRNA !'##residues 1-530 ##label EMM !'##experimental_source var. Marfona, tuber !'##note sequence extracted from NCBI backbone (NCBIP:136741) CLASSIFICATION #superfamily mitochondrial processing peptidase alpha chain KEYWORDS hydrolase; metalloproteinase; mitochondrial matrix; !1mitochondrion; oxidative phosphorylation; oxidoreductase; !1respiratory chain FEATURE !$1-28 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$29-530 #product mitochondrial processing peptidase beta !8chain #status experimental #label MAT SUMMARY #length 530 #molecular-weight 59272 #checksum 2276 SEQUENCE /// ENTRY SNECPI #type complete TITLE pitrilysin (EC 3.4.24.55) precursor [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES endopeptidase Pi; proteinase III ORGANISM #formal_name Escherichia coli DATE 31-Mar-1993 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS F65064; A29093; A25765; B25532 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65064 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-962 ##label BLAT !'##cross-references GB:AE000365; GB:U00096; NID:g2367163; !1PIDN:AAC75860.1; PID:g2367164; UWGP:b2821 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A29093 !$#authors Claverie-Martin, F.; Diaz-Torres, M.R.; Kushner, S.R. !$#journal Gene (1987) 54:185-195 !$#title Analysis of the regulatory region of the protease III (ptr) !1gene of Escherichia coli K-12. !$#cross-references MUID:88005781; PMID:3308636 !$#accession A29093 !'##molecule_type DNA !'##residues 1-276,'HYHSLR',283,'W',285-296 ##label CLA !'##cross-references GB:M17095; NID:g147390; PIDN:AAA24436.1; !1PID:g147391 !'##experimental_source strain K12 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE A25765 !$#authors Finch, P.W.; Wilson, R.E.; Brown, K.; Hickson, I.D.; !1Emmerson, P.T. !$#journal Nucleic Acids Res. (1986) 14:7695-7703 !$#title Complete nucleotide sequence of the Escherichia coli ptr !1gene encoding protease III. !$#cross-references MUID:87040734; PMID:3534791 !$#accession A25765 !'##molecule_type DNA !'##residues 1-962 ##label FIN !'##cross-references GB:X06227; NID:g42560; PIDN:CAA29576.1; PID:g42561 REFERENCE A38854 !$#authors Becker, A.B.; Roth, R.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:3835-3839 !$#title An unusual active site identified in a family of zinc !1metalloendopeptidases. !$#cross-references MUID:92237263; PMID:1570301 !$#contents annotation; active site GENETICS !$#gene ptr !$#map_position 61 FUNCTION !$#description endopeptidase degrades small peptides [validated, !1MUID:92237263] !$#pathway protein degradation CLASSIFICATION #superfamily insulysin KEYWORDS hydrolase; metalloproteinase; monomer; periplasmic space; !1protein degradation; zinc FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-962 #product pitrilysin #status experimental #label MAT\ !$88,92 #binding_site zinc (His) #status experimental\ !$91 #active_site Glu #status experimental SUMMARY #length 962 #molecular-weight 107708 #checksum 9914 SEQUENCE /// ENTRY SNHUIN #type complete TITLE insulysin (EC 3.4.24.56) [validated] - human ALTERNATE_NAMES insulin-degrading proteinase; insulinase ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1993 #sequence_revision 18-Feb-2000 #text_change 18-Feb-2000 ACCESSIONS A40119; A59179; A36115 REFERENCE A40119 !$#authors Affholter, J.A.; Fried, V.A.; Roth, R.A. !$#journal Science (1988) 242:1415-1418 !$#title Human insulin-degrading enzyme shares structural and !1functional homologies with Escherichia coli protease III. !$#cross-references MUID:89072709; PMID:3059494 !$#accession A40119 !'##molecule_type mRNA !'##residues 1-77,'I',79-951,'R' ##label AFF1 !'##cross-references GB:M21188; NID:g184555 !'##note this sequence is revised in reference A36115 !'##note the amino end of the mature protein is blocked REFERENCE A36115 !$#authors Affholter, J.A.; Hsieh, C.L.; Francke, U.; Roth, R.A. !$#journal Mol. Endocrinol. (1990) 4:1125-1135 !$#title Insulin-degrading enzyme: stable expression of the human !1complementary DNA, characterization of its protein product, !1and chromosomal mapping of the human and mouse genes. !$#cross-references MUID:91155945; PMID:2293021 !$#accession A59179 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-1019 ##label AFF2 !'##cross-references GB:M21188; NID:g184555; PIDN:AAA52712.1; !1PID:g184556 !'##experimental_source cell type lymphocyte; tissue type hepatoma !$#accession A36115 !'##molecule_type mRNA !'##residues 948-1019 ##label AFF3 !'##cross-references GB:M21188; NID:g184555 REFERENCE A38854 !$#authors Becker, A.B.; Roth, R.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:3835-3839 !$#title An unusual active site identified in a family of zinc !1metalloendopeptidases. !$#cross-references MUID:92237263; PMID:1570301 !$#contents annotation; active site GENETICS !$#gene GDB:IDE !'##cross-references GDB:118817; OMIM:146680 !$#map_position 10q23-10q25 FUNCTION !$#description catalyzes the hydrolysis of small peptides [validated, !1MUID:89072709] !$#pathway protein degradation CLASSIFICATION #superfamily insulysin KEYWORDS blocked amino end; hydrolase; metalloproteinase; protein !1degradation; zinc FEATURE !$108,112 #binding_site zinc (His) #status predicted\ !$111 #active_site Glu #status predicted SUMMARY #length 1019 #molecular-weight 118021 #checksum 1712 SEQUENCE /// ENTRY S29509 #type complete TITLE insulysin (EC 3.4.24.56) precursor [validated] - rat ALTERNATE_NAMES insulin-degrading enzyme; insulinase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 17-Jul-1998 #sequence_revision 17-Jul-1998 #text_change 18-Feb-2000 ACCESSIONS S29509; S19556; I53265 REFERENCE S29509 !$#authors Baumeister, H.; Mueller, D.; Rehbein, M.; Richter, D. !$#journal FEBS Lett. (1993) 317:250-254 !$#title The rat insulin-degrading enzyme. Molecular cloning and !1characterization of tissue-specific transcripts. !$#cross-references MUID:93146169; PMID:8425612 !$#accession S29509 !'##molecule_type mRNA !'##residues 1-1019 ##label BAU !'##cross-references EMBL:X67269; NID:g56491; PIDN:CAA47689.1; !1PID:g56492 !'##note it is uncertain whether Met-1 or Met-42 is the initiator REFERENCE S19556 !$#authors Mueller, D.; Baumeister, H.; Buck, F.; Richter, D. !$#journal Eur. J. Biochem. (1991) 202:285-292 !$#title Atrial natriuretic peptide (ANP) is a high-affinity !1substrate for rat insulin-degrading enzyme. !$#cross-references MUID:92104146; PMID:1836994 !$#accession S19556 !'##molecule_type protein !'##residues 290-299;329-335;403-408,'F',410-413;528-541;848-861 ##label !1MUE REFERENCE I53265 !$#authors Kuo, W.L.; Montag, A.G.; Rosner, M.R. !$#journal Endocrinology (1993) 132:604-611 !$#title Insulin-degrading enzyme is differentially expressed and !1developmentally regulated in various rat tissues. !$#cross-references MUID:93145867; PMID:7678795 !$#accession I53265 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 898-995 ##label KUO !'##cross-references GB:S53721; NID:g264628; PIDN:AAB25205.1; !1PID:g264629 FUNCTION !$#description catalyzes the hydolysis of small peptides [validated, !1MUID:92104146] !$#pathway protein degradation CLASSIFICATION #superfamily insulysin KEYWORDS hydrolase; metalloproteinase; protein degradation; zinc FEATURE !$108,112 #binding_site zinc (His) #status predicted\ !$111 #active_site Glu #status predicted SUMMARY #length 1019 #molecular-weight 117709 #checksum 2251 SEQUENCE /// ENTRY SNFFIN #type complete TITLE insulysin (EC 3.4.24.56) - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES insulin-degrading metalloproteinase; insulinase ORGANISM #formal_name Drosophila melanogaster DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 18-Feb-2000 ACCESSIONS A37254; A38855 REFERENCE A37254 !$#authors Kuo, W.L.; Gehm, B.D.; Rosner, M.R. !$#journal Mol. Endocrinol. (1990) 4:1580-1591 !$#title Cloning and expression of the cDNA for a Drosophila !1insulin-degrading enzyme. !$#cross-references MUID:91133431; PMID:2126597 !$#accession A37254 !'##molecule_type mRNA !'##residues 1-990 ##label KUO !'##cross-references GB:M58465 REFERENCE A38855 !$#authors Garcia, J.V.; Fenton, B.W.; Rosner, M.R. !$#journal Biochemistry (1988) 27:4237-4244 !$#title Isolation and characterization of an insulin-degrading !1enzyme from Drosophila melanogaster. !$#cross-references MUID:89000606; PMID:3139025 !$#accession A38855 !'##molecule_type protein !'##residues 'X',3-10,'A',12,'X',14-16 ##label GAR REFERENCE A38854 !$#authors Becker, A.B.; Roth, R.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:3835-3839 !$#title An unusual active site identified in a family of zinc !1metalloendopeptidases. !$#cross-references MUID:92237263; PMID:1570301 !$#contents annotation; active site GENETICS !$#gene FlyBase:Ide !'##cross-references FlyBase:FBgn0001247 !$#map_position 3L (band 77B) FUNCTION !$#description catalyzes the hydolysis of small peptides !$#pathway protein degradation CLASSIFICATION #superfamily insulysin KEYWORDS hydrolase; metalloproteinase; monomer; protein degradation; !1zinc FEATURE !$2-990 #product insulysin #status experimental #label MAT\ !$81,85 #binding_site zinc (His) #status predicted\ !$84 #active_site Glu #status predicted SUMMARY #length 990 #molecular-weight 113633 #checksum 6723 SEQUENCE /// ENTRY SNHUC9 #type complete TITLE C 3.4.25.1 proteasome endopeptidase complex () chain C9 - human ALTERNATE_NAMES multicatalytic proteinase complex chain C9; proteasome chain C9 ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 03-Jun-2002 ACCESSIONS S15972; PC2324 REFERENCE S15897 !$#authors Tamura, T.; Lee, D.H.; Osaka, F.; Fujiwara, T.; Shin, S.; !1Chung, C.H.; Tanaka, K.; Ichihara, A. !$#journal Biochim. Biophys. Acta (1991) 1089:95-102 !$#title Molecular cloning and sequence analysis of cDNAs for five !1major subunits of human proteasomes (multi-catalytic !1proteinase complexes). !$#cross-references MUID:91223105; PMID:2025653 !$#accession S15972 !'##molecule_type mRNA !'##residues 1-261 ##label TAM !'##cross-references GB:D00763; NID:g220029; PIDN:BAA00660.1; !1PID:g220030 REFERENCE PC2315 !$#authors Kristensen, P.; Johnsen, A.H.; Uerkvitz, W.; Tanaka, K.; !1Hendil, K.B. !$#journal Biochem. Biophys. Res. Commun. (1994) 205:1785-1789 !$#title Human proteasome subunits from 2-dimensional gels identified !1by partial sequencing. !$#cross-references MUID:95110324; PMID:7811265 !$#accession PC2324 !'##molecule_type protein !'##residues 18-39 ##label KRI !'##experimental_source placenta COMMENT The proteasome consists of subunits of 21K-30K arranged in !1four stacked rings. GENETICS !$#gene GDB:PSMA4 !'##cross-references GDB:567220 !$#map_position 14q23-14q23 CLASSIFICATION #superfamily multicatalytic endopeptidase complex chain C9 KEYWORDS hydrolase; proteasome; protein degradation; proteinase SUMMARY #length 261 #molecular-weight 29484 #checksum 2435 SEQUENCE /// ENTRY SNRTC9 #type complete TITLE C 3.4.25.1 proteasome endopeptidase complex () chain C9 - rat ALTERNATE_NAMES ingensin chain C9; macropain chain C9; multicatalytic proteinase chain C9; proteasome chain C9; proteasome chain L ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Jun-2002 ACCESSIONS S10566; A38765; S15066; A38766; JQ0653 REFERENCE S10566 !$#authors Kumatori, A.; Tanaka, K.; Tamura, T.; Fujiwara, T.; !1Ichihara, A.; Tokunaga, F.; Onikura, A.; Iwanaga, S. !$#journal FEBS Lett. (1990) 264:279-282 !$#title cDNA cloning and sequencing of component C9 of proteasomes !1from rat hepatoma cells. !$#cross-references MUID:90292225; PMID:2358075 !$#accession S10566 !'##molecule_type mRNA !'##residues 1-261 ##label KUM !'##cross-references EMBL:X53304; NID:g56999; PIDN:CAA37390.1; !1PID:g57000 !$#accession A38765 !'##molecule_type protein !'##residues 65-79;128-141,'X',143-152;161-176;181-187;200-205 ##label !1KUM2 REFERENCE S14004 !$#authors Sorimachi, H.; Tsukahara, T.; Kawasaki, H.; Ishiura, S.; !1Emori, Y.; Sugita, H.; Suzuki, K. !$#journal Eur. J. Biochem. (1990) 193:775-781 !$#title Molecular cloning of cDNAs for two subunits of rat !1multicatalytic proteinase. Existence of N-terminal conserved !1and C-terminal diverged sequences among subunits. !$#cross-references MUID:91065384; PMID:2249692 !$#accession S15066 !'##molecule_type mRNA !'##residues 1-261 ##label SOR !'##cross-references EMBL:X55986; NID:g56640; PIDN:CAA39458.1; !1PID:g56641 !$#accession A38766 !'##molecule_type protein !'##residues 119-125;143-157;211-220 ##label SOR2 CLASSIFICATION #superfamily multicatalytic endopeptidase complex chain C9 KEYWORDS hydrolase; proteasome; protein degradation; proteinase SUMMARY #length 261 #molecular-weight 29498 #checksum 2937 SEQUENCE /// ENTRY SNBYY3 #type complete TITLE C 3.4.25.1 proteasome endopeptidase complex () chain Y13 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES ingensin chain Y13; multicatalytic proteinase chain Y13; proteasome chain Y13; protein G6405; protein YGR135w ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Jun-2002 ACCESSIONS S12940; A38774; S64444 REFERENCE S12938 !$#authors Emori, Y.; Tsukahara, T.; Kawasaki, H.; Ishiura, S.; Sugita, !1H.; Suzuki, K. !$#journal Mol. Cell. Biol. (1991) 11:344-353 !$#title Molecular cloning and functional analysis of three subunits !1of yeast proteasome. !$#cross-references MUID:91094849; PMID:1898763 !$#accession S12940 !'##molecule_type DNA !'##residues 1-258 ##label EMO !'##cross-references GB:M63851; NID:g172261; PIDN:AAA34907.1; !1PID:g172262 !'##experimental_source strain X2180-1A !$#accession A38774 !'##molecule_type protein !'##residues 73-86,'X',88-92;120-139;200-236 ##label EMO2 REFERENCE S64428 !$#authors Van Dyck, L.; Skala, J.; de Wergifosse, P.; Purnelle, B.; !1Talla, E.; Nawrocki, A.; Del Bino, S.; Goffeau, A. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64444 !'##molecule_type DNA !'##residues 1-258 ##label VAN !'##cross-references EMBL:Z72920; NID:g1323224; PIDN:CAA97148.1; !1PID:g1323225; GSPDB:GN00007; MIPS:YGR135w !'##experimental_source strain S288C GENETICS !$#gene SGD:PRE9; PRS5; Y13; MIPS:YGR135w !'##cross-references SGD:S0003367; MIPS:YGR135w !$#map_position 7R CLASSIFICATION #superfamily multicatalytic endopeptidase complex chain C9 KEYWORDS hydrolase; proteasome; protein degradation; proteinase SUMMARY #length 258 #molecular-weight 28714 #checksum 9558 SEQUENCE /// ENTRY SNRTC2 #type complete TITLE C 3.4.25.1 proteasome endopeptidase complex () chain C2 - rat ALTERNATE_NAMES multicatalytic proteinase component C2; proteasome chain C2 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 03-Jun-2002 ACCESSIONS A32968; A38799; S09741 REFERENCE A32968 !$#authors Fujiwara, T.; Tanaka, K.; Kumatori, A.; Shin, S.; Yoshimura, !1T.; Ichihara, A.; Tokunaga, F.; Aruga, R.; Iwanaga, S.; !1Kakizuka, A.; Nakanishi, S. !$#journal Biochemistry (1989) 28:7332-7340 !$#title Molecular cloning of cDNA for proteasomes (multicatalytic !1proteinase complexes) from rat liver: primary structure of !1the largest component (C2). !$#cross-references MUID:90057428; PMID:2819072 !$#accession A32968 !'##molecule_type mRNA !'##residues 1-263 ##label FUJ1 !'##cross-references EMBL:M29859; NID:g206381; PIDN:AAA41943.1; !1PID:g206382 !$#accession A38799 !'##molecule_type protein !'##residues 2-25;42-58;63-74,'X',76-79,'X',81;116-135;190-203;218-226, !1'XX',229,'X',231;244-246,'X',248-262 ##label FUJ2 REFERENCE S09741 !$#authors Tokunaga, F.; Aruga, R.; Iwanaga, S.; Tanaka, K.; Ichihara, !1A.; Takao, T.; Shimonishi, Y. !$#journal FEBS Lett. (1990) 263:373-375 !$#title The NH2-terminal residues of rat liver proteasome !1(multicatalytic proteinase complex) subunits, C2, C3 and C8, !1are N-alpha-acetylated. !$#cross-references MUID:90243011; PMID:2335242 !$#accession S09741 !'##molecule_type protein !'##residues 1-30 ##label TOK CLASSIFICATION #superfamily multicatalytic endopeptidase complex chain C9 KEYWORDS acetylated amino end; hydrolase; proteasome; protein !1degradation; proteinase FEATURE !$1-263 #product multicatalytic endopeptidase complex chain !8C2 #status experimental #label MAT\ !$1 #modified_site acetylated amino end (Met) #status !8experimental SUMMARY #length 263 #molecular-weight 29517 #checksum 9238 SEQUENCE /// ENTRY JC1445 #type complete TITLE C 3.4.25.1 proteasome endopeptidase complex () chain C2, long splice form - human ALTERNATE_NAMES macropain nu chain; multicatalytic endopeptidase complex HC2 chain; multicatalytic endopeptidase complex nu chain; multicatalytic proteinase chain C2; prosome 30-33K chain; proteasome alpha 1 subunit; proteasome chain C2; proteasome nu chain CONTAINS multicatalytic endopeptidase complex chain C2, short splice form ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS JC1445; S15897; S17520; S25410; PC2321 REFERENCE JC1445 !$#authors Pereira, I.S.; Bey, F.; Coux, O.; Scherrer, K. !$#journal Gene (1992) 120:235-242 !$#title Two mRNAs exist for the Hs PROS-30 gene encoding a component !1of human prosomes. !$#cross-references MUID:93013039; PMID:1398136 !$#accession JC1445 !'##molecule_type mRNA !'##residues 1-269 ##label PER !'##cross-references GB:M64992 REFERENCE S15897 !$#authors Tamura, T.; Lee, D.H.; Osaka, F.; Fujiwara, T.; Shin, S.; !1Chung, C.H.; Tanaka, K.; Ichihara, A. !$#journal Biochim. Biophys. Acta (1991) 1089:95-102 !$#title Molecular cloning and sequence analysis of cDNAs for five !1major subunits of human proteasomes (multi-catalytic !1proteinase complexes). !$#cross-references MUID:91223105; PMID:2025653 !$#accession S15897 !'##molecule_type mRNA !'##residues 'M',8-269 ##label TAM !'##cross-references EMBL:D00759; NID:g220021; PIDN:BAA00656.1; !1PID:g220022 REFERENCE S17520 !$#authors DeMartino, G.N.; Orth, K.; McCullough, M.L.; Lee, L.W.; !1Munn, T.Z.; Moomaw, C.R.; Dawson, P.A.; Slaughter, C.A. !$#journal Biochim. Biophys. Acta (1991) 1079:29-38 !$#title The primary structures of four subunits of the human, !1high-molecular-weight proteinase, macropain (proteasome), !1are distinct but homologous. !$#cross-references MUID:91363412; PMID:1888762 !$#accession S17520 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 'M',8-269 ##label DEM !'##cross-references GB:X61969; NID:g296737; PIDN:CAA43961.1; !1PID:g296738 !$#accession S25410 !'##molecule_type protein !'##residues !110-40;46-61;68-75;89-95;103-128;132-148;164-168;176-195; !1203-223;225-267 ##label DE2 REFERENCE PC2315 !$#authors Kristensen, P.; Johnsen, A.H.; Uerkvitz, W.; Tanaka, K.; !1Hendil, K.B. !$#journal Biochem. Biophys. Res. Commun. (1994) 205:1785-1789 !$#title Human proteasome subunits from 2-dimensional gels identified !1by partial sequencing. !$#cross-references MUID:95110324; PMID:7811265 !$#accession PC2321 !'##molecule_type protein !'##residues 69-88 ##label KRI !'##experimental_source placenta COMMENT The proteasome consists of subunits of 21K-30K arranged in 4 !1stacked rings. GENETICS !$#gene GDB:PSMA1; HsPROS-30 !'##cross-references GDB:134040 !$#map_position 11q-11q CLASSIFICATION #superfamily multicatalytic endopeptidase complex chain C9 KEYWORDS hydrolase; phosphoprotein; proteasome; protein degradation; !1proteinase FEATURE !$2-269 #product multicatalytic endopeptidase complex chain !8C2, long splice form #status predicted #label MATL\ !$8-269 #product multicatalytic endopeptidase complex chain !8C2, short splice form #status predicted #label MATS\ !$230 #binding_site phosphate (Tyr) (covalent) #status !8predicted SUMMARY #length 269 #molecular-weight 30239 #checksum 5946 SEQUENCE /// ENTRY SNFF5K #type complete TITLE C 3.4.25.1 proteasome endopeptidase complex () 35K chain - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES 19S cylinder particle 35K chain; multicatalytic proteinase 35K chain; prosome 35K chain; proteasome 35K chain ORGANISM #formal_name Drosophila melanogaster DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Jun-2002 ACCESSIONS S23450; S05507; A38761 REFERENCE S23450 !$#authors Frentzel, S.; Troxell, M.; Haass, C.; Pesold-Hurt, B.; !1Glaetzer, K.H.; Kloetzel, P.M. !$#journal Eur. J. Biochem. (1992) 205:1043-1051 !$#title Molecular characterization of the genomic regions of the !1Drosophila alpha-type subunit proteasome genes PROS-Dm28.1 !1and PROS-Dm35. !$#cross-references MUID:92249308; PMID:1374331 !$#accession S23450 !'##molecule_type DNA !'##residues 1-279 ##label FREN !'##cross-references EMBL:X62285; NID:g8387; PIDN:CAA44173.1; PID:g8388 !'##experimental_source strain Canton S REFERENCE S05507 !$#authors Haass, C.; Pesold-Hurt, B.; Multhaup, G.; Beyreuther, K.; !1Kloetzel, P.M. !$#journal EMBO J. (1989) 8:2373-2379 !$#title The PROS-35 gene encodes the 35 kd protein subunit of !1Drosophila melanogaster proteasome. !$#cross-references MUID:90005444; PMID:2477245 !$#accession S05507 !'##molecule_type mRNA !'##residues 1-279 ##label HAA !'##cross-references EMBL:X15497; NID:g8381; PIDN:CAA33520.1; PID:g8382 !$#accession A38761 !'##molecule_type protein !'##residues 4-18;194-206 ##label HAA2 GENETICS !$#gene PROS-35 !'##cross-references FlyBase:FBgn0003151 !$#map_position 89F-90A !$#introns 1/3; 211/3 CLASSIFICATION #superfamily multicatalytic endopeptidase complex chain C9 KEYWORDS hydrolase; phosphoprotein; proteasome; protein degradation; !1proteinase SUMMARY #length 279 #molecular-weight 31058 #checksum 365 SEQUENCE /// ENTRY SNHUC3 #type complete TITLE C 3.4.25.1 proteasome endopeptidase complex () chain C3 - human ALTERNATE_NAMES multicatalytic proteinase complex chain C3; proteasome alpha-type HC3; proteasome chain C3 ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 03-Jun-2002 ACCESSIONS S15970; PC2325; S53758 REFERENCE S15897 !$#authors Tamura, T.; Lee, D.H.; Osaka, F.; Fujiwara, T.; Shin, S.; !1Chung, C.H.; Tanaka, K.; Ichihara, A. !$#journal Biochim. Biophys. Acta (1991) 1089:95-102 !$#title Molecular cloning and sequence analysis of cDNAs for five !1major subunits of human proteasomes (multi-catalytic !1proteinase complexes). !$#cross-references MUID:91223105; PMID:2025653 !$#accession S15970 !'##molecule_type mRNA !'##residues 1-234 ##label TAM !'##cross-references GB:D00760; NID:g220023; PIDN:BAA00657.1; !1PID:g220024 REFERENCE PC2315 !$#authors Kristensen, P.; Johnsen, A.H.; Uerkvitz, W.; Tanaka, K.; !1Hendil, K.B. !$#journal Biochem. Biophys. Res. Commun. (1994) 205:1785-1789 !$#title Human proteasome subunits from 2-dimensional gels identified !1by partial sequencing. !$#cross-references MUID:95110324; PMID:7811265 !$#accession PC2325 !'##molecule_type protein !'##residues 5-14 ##label KRI REFERENCE S53758 !$#authors Tamura, T.; Osaka, F.; Kawamura, Y.; Higuti, T.; Ishida, N.; !1Nothwang, H.G.; Tsurumi, C.; Tanaka, K.; Ichihara, A. !$#journal J. Mol. Biol. (1994) 244:117-124 !$#title Isolation and characterization of alpha-type HC3 and !1beta-type HC5 subunit genes of human proteasomes. !$#cross-references MUID:95055741; PMID:7966316 !$#accession S53758 !'##molecule_type DNA !'##residues 1-14 ##label TA2 GENETICS !$#gene GDB:PSMA2 !'##cross-references GDB:567219; OMIM:176842 !$#map_position 6q27-6q27 CLASSIFICATION #superfamily multicatalytic endopeptidase complex chain C9 KEYWORDS hydrolase; phosphoprotein; proteasome; protein degradation; !1proteinase SUMMARY #length 234 #molecular-weight 25898 #checksum 8446 SEQUENCE /// ENTRY SNRTC3 #type complete TITLE proteasome chain C3 - rat ALTERNATE_NAMES multicatalytic proteinase component C3 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 03-Mar-2000 ACCESSIONS A34535; A38800; S09742 REFERENCE A34535 !$#authors Tanaka, K.; Fujiwara, T.; Kumatori, A.; Shin, S.; Yoshimura, !1T.; Ichihara, A.; Tokunaga, F.; Aruga, R.; Iwanaga, S.; !1Kakizuka, A.; Nakanishi, S. !$#journal Biochemistry (1990) 29:3777-3785 !$#title Molecular cloning of cDNA for proteasomes from rat liver: !1primary structure of component C3 with a possible tyrosine !1phosphorylation site. !$#cross-references MUID:90254106; PMID:2340272 !$#accession A34535 !'##molecule_type mRNA !'##residues 1-234 ##label TAN1 !'##cross-references EMBL:J02897; NID:g203202; PIDN:AAA40838.1; !1PID:g203203 !$#accession A38800 !'##molecule_type protein !'##residues 'X',6-11,'X',13-50;54-92;160-176;197-226 ##label TAN2 REFERENCE S09741 !$#authors Tokunaga, F.; Aruga, R.; Iwanaga, S.; Tanaka, K.; Ichihara, !1A.; Takao, T.; Shimonishi, Y. !$#journal FEBS Lett. (1990) 263:373-375 !$#title The NH2-terminal residues of rat liver proteasome !1(multicatalytic proteinase complex) subunits, C2, C3 and C8, !1are N-alpha-acetylated. !$#cross-references MUID:90243011; PMID:2335242 !$#accession S09742 !'##molecule_type protein !'##residues 2-30 ##label TOK CLASSIFICATION #superfamily multicatalytic endopeptidase complex chain C9 KEYWORDS acetylated amino end; phosphoprotein; proteasome; protein !1degradation FEATURE !$2-234 #product proteasome chain C3 #status experimental !8#label MAT\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental SUMMARY #length 234 #molecular-weight 25926 #checksum 8838 SEQUENCE /// ENTRY SNBYY7 #type complete TITLE C 3.4.25.1 proteasome endopeptidase complex () chain Y7 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES ingensin chain Y7; multicatalytic proteinase chain Y7; proteasome chain Y7; protein YML092c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Jun-2002 ACCESSIONS S12938; A38773; S49635 REFERENCE S12938 !$#authors Emori, Y.; Tsukahara, T.; Kawasaki, H.; Ishiura, S.; Sugita, !1H.; Suzuki, K. !$#journal Mol. Cell. Biol. (1991) 11:344-353 !$#title Molecular cloning and functional analysis of three subunits !1of yeast proteasome. !$#cross-references MUID:91094849; PMID:1898763 !$#accession S12938 !'##molecule_type DNA !'##residues 1-250 ##label EMO !'##cross-references GB:X56731; GB:M63640; NID:g506481; PIDN:CAA40055.1; !1PID:g506482 !$#accession A38773 !'##molecule_type protein !'##residues 18-25,'X',27;64-83;92-98;173-177;232-237 ##label EMO2 !'##experimental_source strain X2180-1A REFERENCE S49627 !$#authors Gentles, S.; Bowman, S. !$#submission submitted to the EMBL Data Library, November 1994 !$#accession S49635 !'##molecule_type DNA !'##residues 1-250 ##label GEN !'##cross-references EMBL:Z46660; NID:g575702; PIDN:CAA86646.1; !1PID:g575711; GSPDB:GN00013; MIPS:YML092c GENETICS !$#gene SGD:PRE8; MIPS:YML092c !'##cross-references SGD:S0004557; MIPS:YML092c !$#map_position 13L CLASSIFICATION #superfamily multicatalytic endopeptidase complex chain C9 KEYWORDS hydrolase; proteasome; protein degradation; proteinase SUMMARY #length 250 #molecular-weight 27162 #checksum 4523 SEQUENCE /// ENTRY S30274 #type complete TITLE C 3.4.25.1 proteasome endopeptidase complex () iota chain - human ALTERNATE_NAMES macropain iota chain; prosome protein, 27K; proteasome alpha 6 subunit; proteasome iota chain; RNA-binding protein, 27K ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S30274; S17523; S25413; PC2322 REFERENCE S30274 !$#authors Bey, F.; Pereira, I.S.; Coux, O.; Viegas-Pequignot, E.; !1Targa, F.R.; Nothwang, H.G.; Dutrillaux, B.; Scherrer, K. !$#journal Mol. Gen. Genet. (1993) 237:193-205 !$#title The prosomal RNA-binding protein p27K is a member of the !1alpha-type human prosomal gene family. !$#cross-references MUID:93204895; PMID:7681138 !$#accession S30274 !'##molecule_type mRNA !'##residues 1-246 ##label BEY !'##cross-references EMBL:X59417; NID:g35681; PIDN:CAA42052.1; !1PID:g35682 REFERENCE S17520 !$#authors DeMartino, G.N.; Orth, K.; McCullough, M.L.; Lee, L.W.; !1Munn, T.Z.; Moomaw, C.R.; Dawson, P.A.; Slaughter, C.A. !$#journal Biochim. Biophys. Acta (1991) 1079:29-38 !$#title The primary structures of four subunits of the human, !1high-molecular-weight proteinase, macropain (proteasome), !1are distinct but homologous. !$#cross-references MUID:91363412; PMID:1888762 !$#accession S17523 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 26-58,'C',60-246 ##label DEM !'##cross-references EMBL:X61972; NID:g296735; PIDN:CAA43964.1; !1PID:g296736 !$#accession S25413 !'##molecule_type protein !'##residues 12-58,'C',60-88;94-116;118-164;172-181;229-245 ##label DE2 REFERENCE PC2315 !$#authors Kristensen, P.; Johnsen, A.H.; Uerkvitz, W.; Tanaka, K.; !1Hendil, K.B. !$#journal Biochem. Biophys. Res. Commun. (1994) 205:1785-1789 !$#title Human proteasome subunits from 2-dimensional gels identified !1by partial sequencing. !$#cross-references MUID:95110324; PMID:7811265 !$#accession PC2322 !'##molecule_type protein !'##residues 96-100;105-114,'X',116 ##label KRI !'##experimental_source placenta COMMENT The proteasome consists of subunits of 21K-30K arranged in 4 !1stacked rings. GENETICS !$#gene GDB:PSMA6; PROS-27 !'##cross-references GDB:134042 !$#map_position 14q13-14q13 CLASSIFICATION #superfamily multicatalytic endopeptidase complex chain C9 KEYWORDS hydrolase; proteasome; protein degradation; proteinase FEATURE !$2-246 #product multicatalytic endopeptidase complex iota !8chain #status predicted #label MAT SUMMARY #length 246 #molecular-weight 27399 #checksum 8690 SEQUENCE /// ENTRY JX0230 #type complete TITLE C 3.4.25.1 proteasome endopeptidase complex () iota chain - rat ALTERNATE_NAMES proteasome iota chain ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS JX0230 REFERENCE JX0228 !$#authors Tamura, T.; Shimbara, N.; Aki, M.; Ishida, N.; Bey, F.; !1Scherrer, K.; Tanaka, K.; Ichihara, A. !$#journal J. Biochem. (1992) 112:530-534 !$#title Molecular cloning of cDNAs for rat proteasomes: Deduced !1primary structures of four other subunits. !$#cross-references MUID:93147071; PMID:1491007 !$#accession JX0230 !'##molecule_type mRNA !'##residues 1-246 ##label TAM !'##cross-references DDBJ:D10755; NID:g286249; PIDN:BAA01587.1; !1PID:g286250 COMMENT Proteasome consists of 15 nonidentical subunits of similar !1sizes. CLASSIFICATION #superfamily multicatalytic endopeptidase complex chain C9 KEYWORDS hydrolase; proteasome; protein degradation SUMMARY #length 246 #molecular-weight 27399 #checksum 8690 SEQUENCE /// ENTRY SNBYS1 #type complete TITLE C 3.4.25.1 proteasome endopeptidase complex () chain YC7-alpha - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES ingensin chain YC7-alpha; multicatalytic proteinase chain YC7-alpha; proteasome chain Y8; proteasome chain YC7-alpha; protein G3728; protein YGL011c; SCL1 protein ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1990 #sequence_revision 30-Sep-1991 #text_change 03-Jun-2002 ACCESSIONS S11199; A38770; S12939; A38771; S11658; JQ0115; S31557; !1S64013; S07846; S07953 REFERENCE S11182 !$#authors Fujiwara, T.; Tanaka, K.; Orino, E.; Yoshimura, T.; !1Kumatori, A.; Tamura, T.; Chung, C.H.; Nakai, T.; Yamaguchi, !1K.; Shin, S.; Kakizuka, A.; Nakanishi, S.; Ichihara, A. !$#journal J. Biol. Chem. (1990) 265:16604-16613 !$#title Proteasomes are essential for yeast proliferation. cDNA !1cloning and gene disruption of two major subunits. !$#cross-references MUID:90375535; PMID:1697860 !$#accession S11199 !'##molecule_type mRNA !'##residues 1-252 ##label FUJ !'##cross-references EMBL:M55440; NID:g173205; PIDN:AAA35228.1; !1PID:g173206 !$#accession A38770 !'##molecule_type protein !'##residues 175-187;189-198 ##label FUJ2 REFERENCE S12938 !$#authors Emori, Y.; Tsukahara, T.; Kawasaki, H.; Ishiura, S.; Sugita, !1H.; Suzuki, K. !$#journal Mol. Cell. Biol. (1991) 11:344-353 !$#title Molecular cloning and functional analysis of three subunits !1of yeast proteasome. !$#cross-references MUID:91094849; PMID:1898763 !$#accession S12939 !'##molecule_type DNA !'##residues 1-252 ##label EMO !'##cross-references EMBL:M63641; NID:g172265; PIDN:AAA34909.1; !1PID:g172266 !$#accession A38771 !'##molecule_type protein !'##residues 99-107;157-167;202-208,'X',210-215,'X', !1217-218;221-228;233-251 ##label EMO2 REFERENCE S11658 !$#authors Balzi, E. !$#submission submitted to MIPS, December 1990 !$#accession S11658 !'##molecule_type DNA !'##residues 1-252 ##label BAL !'##note this is a revision to the sequence from reference JQ0115 REFERENCE JQ0115 !$#authors Balzi, E.; Chen, W.; Capieaux, E.; McCusker, J.H.; Haber, !1J.E.; Goffeau, A. !$#journal Gene (1989) 83:271-279 !$#title The suppressor gene scl1+ of Saccharomyces cerevisiae is !1essential for growth. !$#cross-references MUID:90060839; PMID:2684789 !$#accession JQ0115 !'##molecule_type DNA !'##residues 'MLNHIRAETKQSEKNILQSCRVLLLHLLLVMTGTSLSFPPRVV',26-252 !1##label BAL2 !'##cross-references GB:M31430; NID:g172545; PIDN:AAA35020.1; !1PID:g172546 !'##note this sequence has been revised in reference S11658 !'##note the difference at the amino end is due to a frameshift error REFERENCE S15040 !$#authors Chen, W.; Balzi, E.; Capieaux, E.; Choder, M.; Goffeau, A. !$#journal Yeast (1991) 7:287-299 !$#title The DNA sequencing of the 17 kb HindIII fragment spanning !1the LEU1 and ATE1 loci on chromosome VII from Saccharomyces !1cerevisiae reveals the PDR6 gene, a new member of the !1genetic network controlling pleiotropic drug resistance. !$#cross-references MUID:91353083; PMID:1882553 !$#accession S31557 !'##status translation not shown !'##molecule_type DNA !'##residues 1-252 ##label CHE !'##cross-references GB:S58126; NID:g234321; PIDN:AAD13894.1; !1PID:g4261594 REFERENCE S64003 !$#authors Hebling, U.; Hofmann, B.; Delius, H. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64013 !'##molecule_type DNA !'##residues 1-252 ##label HEB !'##cross-references EMBL:Z72533; NID:g1322466; PIDN:CAA96711.1; !1PID:g1322467; GSPDB:GN00007; MIPS:YGL011c !'##experimental_source strain S288C GENETICS !$#gene SGD:SCL1; PRS2; MIPS:YGL011c !'##cross-references SGD:S0002979; MIPS:YGL011c !$#map_position 7L CLASSIFICATION #superfamily multicatalytic endopeptidase complex chain C9 KEYWORDS hydrolase; proteasome; protein degradation; proteinase SUMMARY #length 252 #molecular-weight 28001 #checksum 5646 SEQUENCE /// ENTRY S39900 #type complete TITLE multicatalytic endopeptidase complex 30K chain homolog - Arabidopsis thaliana ALTERNATE_NAMES proteasome chain PSM30 homolog ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS S39900 REFERENCE S39900 !$#authors Shirley, B.W.; Goodman, H.M. !$#journal Mol. Gen. Genet. (1993) 241:586-594 !$#title An Arabidopsis gene homologous to mammalian and insect genes !1encoding the largest proteasome subunit. !$#cross-references MUID:94088452; PMID:8264533 !$#accession S39900 !'##molecule_type DNA !'##residues 1-278 ##label SHI !'##cross-references EMBL:M98495; NID:g166829; PIDN:AAA16326.1; !1PID:g166830 GENETICS !$#gene PSM30 !$#introns 117/3 CLASSIFICATION #superfamily multicatalytic endopeptidase complex chain C9 KEYWORDS proteasome; protein degradation SUMMARY #length 278 #molecular-weight 30476 #checksum 6023 SEQUENCE /// ENTRY SNBYC1 #type complete TITLE C 3.4.25.1 proteasome endopeptidase complex () chain YC1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES proteasome chain YC1; protein O6650; protein YOR362c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Jun-2002 ACCESSIONS S11182; A38769; S67274 REFERENCE S11182 !$#authors Fujiwara, T.; Tanaka, K.; Orino, E.; Yoshimura, T.; !1Kumatori, A.; Tamura, T.; Chung, C.H.; Nakai, T.; Yamaguchi, !1K.; Shin, S.; Kakizuka, A.; Nakanishi, S.; Ichihara, A. !$#journal J. Biol. Chem. (1990) 265:16604-16613 !$#title Proteasomes are essential for yeast proliferation. cDNA !1cloning and gene disruption of two major subunits. !$#cross-references MUID:90375535; PMID:1697860 !$#accession S11182 !'##molecule_type mRNA !'##residues 1-288 ##label FUJ !'##cross-references EMBL:M55436; NID:g173203; PIDN:AAA35227.1; !1PID:g173204 !$#accession A38769 !'##molecule_type protein !'##residues 105-134;179-194;199-208 ##label FUJ2 REFERENCE S67261 !$#authors Delius, H.; Hebling, U.; Hofmann, B. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67274 !'##molecule_type DNA !'##residues 1-288 ##label DEL !'##cross-references EMBL:Z75270; NID:g1420785; PIDN:CAA99691.1; !1PID:g1420786; GSPDB:GN00015; MIPS:YOR362c !'##experimental_source strain S288C GENETICS !$#gene SGD:PRE10; PRS1; MIPS:YOR362c !'##cross-references SGD:S0005889; MIPS:YOR362c !$#map_position 15R CLASSIFICATION #superfamily multicatalytic endopeptidase complex chain C9 KEYWORDS blocked amino end; hydrolase; proteasome; protein !1degradation; proteinase FEATURE !$2-288 #product multicatalytic endopeptidase complex chain !8YC1 #status predicted #label MAT\ !$2 #modified_site blocked amino end (Thr) (in mature !8form) #status experimental SUMMARY #length 288 #molecular-weight 31536 #checksum 3337 SEQUENCE /// ENTRY SNHUC8 #type complete TITLE C 3.4.25.1 proteasome endopeptidase complex () chain C8 - human ALTERNATE_NAMES multicatalytic proteinase complex chain C8; proteasome chain C8 ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 03-Jun-2002 ACCESSIONS S15971; PC2317 REFERENCE S15897 !$#authors Tamura, T.; Lee, D.H.; Osaka, F.; Fujiwara, T.; Shin, S.; !1Chung, C.H.; Tanaka, K.; Ichihara, A. !$#journal Biochim. Biophys. Acta (1991) 1089:95-102 !$#title Molecular cloning and sequence analysis of cDNAs for five !1major subunits of human proteasomes (multi-catalytic !1proteinase complexes). !$#cross-references MUID:91223105; PMID:2025653 !$#accession S15971 !'##molecule_type mRNA !'##residues 1-255 ##label TAM !'##cross-references GB:D00762; NID:g220027; PIDN:BAA00659.1; !1PID:g220028 REFERENCE PC2315 !$#authors Kristensen, P.; Johnsen, A.H.; Uerkvitz, W.; Tanaka, K.; !1Hendil, K.B. !$#journal Biochem. Biophys. Res. Commun. (1994) 205:1785-1789 !$#title Human proteasome subunits from 2-dimensional gels identified !1by partial sequencing. !$#cross-references MUID:95110324; PMID:7811265 !$#accession PC2317 !'##molecule_type protein !'##residues 116-120,'X',122-130 ##label KRI !'##experimental_source placenta GENETICS !$#gene GDB:PSMA3 !'##cross-references GDB:511352; OMIM:176843 !$#map_position 14q23-14q23 CLASSIFICATION #superfamily multicatalytic endopeptidase complex chain C9 KEYWORDS hydrolase; proteasome; protein degradation; proteinase SUMMARY #length 255 #molecular-weight 28433 #checksum 8869 SEQUENCE /// ENTRY SNRTC8 #type complete TITLE C 3.4.25.1 proteasome endopeptidase complex () chain C8 - rat ALTERNATE_NAMES ingensin chain C8; macropain chain C8; multicatalytic proteinase chain C8; proteasome chain C8; proteasome chain K ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 03-Jun-2002 ACCESSIONS S14004; A30482; A35894; B35894; S09743; JQ0652 REFERENCE S14004 !$#authors Sorimachi, H.; Tsukahara, T.; Kawasaki, H.; Ishiura, S.; !1Emori, Y.; Sugita, H.; Suzuki, K. !$#journal Eur. J. Biochem. (1990) 193:775-781 !$#title Molecular cloning of cDNAs for two subunits of rat !1multicatalytic proteinase. Existence of N-terminal conserved !1and C-terminal diverged sequences among subunits. !$#cross-references MUID:91065384; PMID:2249692 !$#accession S14004 !'##molecule_type mRNA !'##residues 1-255 ##label SOR !'##cross-references EMBL:X55985; NID:g56638; PIDN:CAA39457.1; !1PID:g56639 !$#accession A30482 !'##molecule_type protein !'##residues 66-94;209-214,'X',216-222 ##label SOR2 REFERENCE A35894 !$#authors Tanaka, K.; Kanayama, H.; Tamura, T.; Lee, D.H.; Kumatori, !1A.; Fujiwara, T.; Ichihara, A.; Tokunaga, F.; Aruga, R.; !1Iwanaga, S. !$#journal Biochem. Biophys. Res. Commun. (1990) 171:676-683 !$#title cDNA cloning and sequencing of component C8 of proteasomes !1from rat hepatoma cells. !$#cross-references MUID:90386639; PMID:2403356 !$#accession A35894 !'##molecule_type mRNA !'##residues 1-255 ##label TAN !'##cross-references GB:M58593; NID:g203206; PIDN:AAA40840.1; !1PID:g203207 !$#accession B35894 !'##molecule_type protein !'##residues 'X',3-43;66-104,'X',106,'X',108-109;'X',112-114,'X', !1116-134;184-192;223-230 ##label TAN2 REFERENCE S09741 !$#authors Tokunaga, F.; Aruga, R.; Iwanaga, S.; Tanaka, K.; Ichihara, !1A.; Takao, T.; Shimonishi, Y. !$#journal FEBS Lett. (1990) 263:373-375 !$#title The NH2-terminal residues of rat liver proteasome !1(multicatalytic proteinase complex) subunits, C2, C3 and C8, !1are N-alpha-acetylated. !$#cross-references MUID:90243011; PMID:2335242 !$#accession S09743 !'##molecule_type protein !'##residues 2-29 ##label TOK CLASSIFICATION #superfamily multicatalytic endopeptidase complex chain C9 KEYWORDS acetylated amino end; hydrolase; proteasome; protein !1degradation; proteinase FEATURE !$2-255 #product proteasome chain C8 #status experimental !8#label MAT\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental SUMMARY #length 255 #molecular-weight 28419 #checksum 9015 SEQUENCE /// ENTRY S32507 #type complete TITLE C 3.4.25.1 proteasome endopeptidase complex () beta-type chain N3 precursor - rat ALTERNATE_NAMES proteasome beta-type chain N3; proteasome chain N3 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S32507; S69598 REFERENCE S32507 !$#authors Thomson, S.; Balson, D.F.; Rivett, A.J. !$#journal FEBS Lett. (1993) 322:135-138 !$#title cDNA cloning of a new type of subunit of mammalian !1proteasomes. !$#cross-references MUID:93245975; PMID:8482379 !$#accession S32507 !'##molecule_type mRNA !'##residues 32-263 ##label THO !'##cross-references GB:L17127; NID:g310213; PIDN:AAA42054.1; !1PID:g310214 !'##note the authors translated the codon CAG for residue 74 as Glu, CAA !1for residue 78 as Glu, CAG for residue 82 as Glu, and CAG !1for residue 160 as Glu REFERENCE S69598 !$#authors Thomson, S.; Rivett, A.J. !$#journal Biochem. J. (1996) 315:733-738 !$#title Processing of N3, a mammalian proteasome beta-type subunit. !$#cross-references MUID:96220681; PMID:8645151 !$#accession S69598 !'##molecule_type mRNA !'##residues 1-40,'P',42-49,'V',51-59,'S',61-79,'L',81,'N',83-85,'F', !187-88,'L',90-140 ##label THW !'##cross-references EMBL:S82190 !'##experimental_source liver !'##note the authors translated the codon TCC for residue 60 as Phe, CTC !1for residue 80 as Phe, AAT for residue 82 as Ile, TTT for !1residue 86 as Ile, CTC for residue 89 as Val, CAG for !1residue 105 as Glu, CAA for residue 109 as Glu, and CAG for !1residue 113 as Glu COMPLEX multimeric proteinase complex; cylindrical structure is made !1up of four stacked rings of seven subunits each FUNCTION !$#description endopeptidase; peptidylglutamyl-peptide hydrolase activity !$#pathway protein degradation !$#note constitutes the major non-lysosomal proteolytic machinery; !1requires covalent linking of proteins to multiple ubiquitin !1molecules; ATP dependant CLASSIFICATION #superfamily multicatalytic endopeptidase complex chain N3 KEYWORDS ATP; hydrolase; proteasome; protein degradation; proteinase FEATURE !$1-31 #domain propeptide #status predicted #label PRO\ !$32-263 #product multicatalytic endopeptidase complex chain !8N3 #status predicted #label MAT SUMMARY #length 263 #molecular-weight 29200 #checksum 9981 SEQUENCE /// ENTRY SNHUC5 #type complete TITLE C 3.4.25.1 proteasome endopeptidase complex () beta chain C5 [validated] - human ALTERNATE_NAMES macropain gamma chain; multicatalytic proteinase complex chain C5; proteasome beta-1; proteasome chain C5; proteasome gamma chain ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 03-Jun-2002 ACCESSIONS S15973; S08187; PC2327; S53759 REFERENCE S15897 !$#authors Tamura, T.; Lee, D.H.; Osaka, F.; Fujiwara, T.; Shin, S.; !1Chung, C.H.; Tanaka, K.; Ichihara, A. !$#journal Biochim. Biophys. Acta (1991) 1089:95-102 !$#title Molecular cloning and sequence analysis of cDNAs for five !1major subunits of human proteasomes (multi-catalytic !1proteinase complexes). !$#cross-references MUID:91223105; PMID:2025653 !$#accession S15973 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-241 ##label TAM !'##cross-references GB:D00761; NID:g220025; PIDN:BAA00658.1; !1PID:g220026 REFERENCE S08185 !$#authors Lee, L.W.; Moomaw, C.R.; Orth, K.; McGuire, M.J.; DeMartino, !1G.N.; Slaughter, C.A. !$#journal Biochim. Biophys. Acta (1990) 1037:178-185 !$#title Relationships among the subunits of the high molecular !1weight proteinase, macropain (proteasome). !$#cross-references MUID:90167111; PMID:2306472 !$#accession S08187 !'##molecule_type protein !'##residues 'X',30-52 ##label LEE REFERENCE PC2315 !$#authors Kristensen, P.; Johnsen, A.H.; Uerkvitz, W.; Tanaka, K.; !1Hendil, K.B. !$#journal Biochem. Biophys. Res. Commun. (1994) 205:1785-1789 !$#title Human proteasome subunits from 2-dimensional gels identified !1by partial sequencing. !$#cross-references MUID:95110324; PMID:7811265 !$#accession PC2327 !'##molecule_type protein !'##residues 147-160;185-198 ##label KRI !'##experimental_source placenta REFERENCE S53758 !$#authors Tamura, T.; Osaka, F.; Kawamura, Y.; Higuti, T.; Ishida, N.; !1Nothwang, H.G.; Tsurumi, C.; Tanaka, K.; Ichihara, A. !$#journal J. Mol. Biol. (1994) 244:117-124 !$#title Isolation and characterization of alpha-type HC3 and !1beta-type HC5 subunit genes of human proteasomes. !$#cross-references MUID:95055741; PMID:7966316 !$#accession S53759 !'##molecule_type DNA !'##residues 1-10,'A',12-38 ##label TA2 COMMENT The proteasome consists of subunits of 21K-30K arranged in 4 !1stacked rings. GENETICS !$#gene GDB:PSMB1 !'##cross-references GDB:567221 !$#map_position 7p13-7p12 CLASSIFICATION #superfamily multicatalytic endopeptidase complex chain C5 KEYWORDS hydrolase; proteasome; protein degradation; proteinase FEATURE !$29-241 #product multicatalytic endopeptidase complex chain !8C5 #status experimental #label MAT SUMMARY #length 241 #molecular-weight 26489 #checksum 7494 SEQUENCE /// ENTRY A33490 #type complete TITLE type IV prepilin peptidase (EC 3.4.99.-) - Bacillus subtilis ALTERNATE_NAMES genetic transformation late competence protein ComC CONTAINS type IV pilin N-methyltransferase (EC 2.1.1.-) ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A33490; E40646; F40646; B69602 REFERENCE A33490 !$#authors Mohan, S.; Aghion, J.; Guillen, N.; Dubnau, D. !$#journal J. Bacteriol. (1989) 171:6043-6051 !$#title Molecular cloning and characterization of comC, a late !1competence gene of Bacillus subtilis. !$#cross-references MUID:90036690; PMID:2553669 !$#accession A33490 !'##molecule_type DNA !'##residues 1-248 ##label MOH !'##cross-references GB:M30805; NID:g142703; PIDN:AAA83365.1; !1PID:g142704 REFERENCE A40646 !$#authors Margolis, P.S.; Driks, A.; Losick, R. !$#journal J. Bacteriol. (1993) 175:528-540 !$#title Sporulation gene spoIIB from Bacillus subtilis. !$#cross-references MUID:93123172; PMID:8419299 !$#accession E40646 !'##molecule_type DNA !'##residues 1-46 ##label MA1 !'##cross-references GB:L04520; NID:g142934; PIDN:AAB59022.1; !1PID:g142937 !'##note sequence extracted from NCBI backbone (NCBIN:122728, !1NCBIP:122731) !$#accession F40646 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 181-248 ##label MA2 !'##cross-references GB:L04519; NID:g143622; PIDN:AAB59025.1; !1PID:g143623 !'##note sequence extracted from NCBI backbone (NCBIP:122736) REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69602 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-248 ##label KUN !'##cross-references GB:Z99118; GB:AL009126; NID:g2635200; !1PIDN:CAB14767.1; PID:g2635272 !'##experimental_source strain 168 COMMENT This protein is required for the processing and !1translocation of the exogenous DNA-binding protein comGC. GENETICS !$#gene comC CLASSIFICATION #superfamily type IV prepilin peptidase KEYWORDS hydrolase; methyltransferase; S-adenosylmethionine; !1transmembrane protein SUMMARY #length 248 #molecular-weight 26520 #checksum 9368 SEQUENCE /// ENTRY S74490 #type complete TITLE type IV prepilin peptidase (EC 3.4.99.-) hofD - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein slr1120 CONTAINS type IV pilin N-methyltransferase (EC 2.1.1.-) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S74490 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74490 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-269 ##label KAN !'##cross-references EMBL:D90899; GB:AB001339; NID:g1651650; !1PIDN:BAA16642.1; PID:g1651714 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene hofD CLASSIFICATION #superfamily type IV prepilin peptidase KEYWORDS hydrolase; methyltransferase; S-adenosylmethionine SUMMARY #length 269 #molecular-weight 29767 #checksum 692 SEQUENCE /// ENTRY A39131 #type complete TITLE type IV prepilin peptidase (EC 3.4.99.-) pilD - Pseudomonas aeruginosa ALTERNATE_NAMES inner membrane protein xcpA CONTAINS type IV pilin N-methyltransferase (EC 2.1.1.-) ORGANISM #formal_name Pseudomonas aeruginosa DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 31-Dec-2000 ACCESSIONS A39131; C35384; D83078 REFERENCE A39131 !$#authors Bally, M.; Ball, G.; Badere, A.; Lazdunski, A. !$#journal J. Bacteriol. (1991) 173:479-486 !$#title Protein secretion in Pseudomonas aeruginosa: the xcpA gene !1encodes an integral inner membrane protein homologous to !1Klebsiella pneumoniae secretion function protein PulO. !$#cross-references MUID:91100333; PMID:1898929 !$#accession A39131 !'##status preliminary !'##molecule_type DNA !'##residues 1-290 ##label BAL !'##cross-references GB:M61096; GB:M38720; NID:g151641; PIDN:AAA26023.1; !1PID:g151642 REFERENCE A35384 !$#authors Nunn, D.; Bergman, S.; Lory, S. !$#journal J. Bacteriol. (1990) 172:2911-2919 !$#title Products of three accessory genes, pilB, pilC, and pilD, are !1required for biogenesis of Pseudomonas aeruginosa pili. !$#cross-references MUID:90264276; PMID:1971619 !$#accession C35384 !'##status preliminary !'##molecule_type DNA !'##residues 1-17,'A',19-290 ##label NUN !'##cross-references GB:M32066; NID:g151064; PIDN:AAA25734.1; !1PID:g151067 !'##note the authors translated the codon AAC for residue 30 as Ala REFERENCE A82950 !$#authors Stover, C.K.; Pham, X.Q.; Erwin, A.L.; Mizoguchi, S.D.; !1Warrener, P.; Hickey, M.J.; Brinkman, F.S.L.; Hufnagle, !1W.O.; Kowalik, D.J.; Lagrou, M.; Garber, R.L.; Goltry, L.; !1Tolentino, E.; Westbrook-Wadman, S.; Yuan, Y.; Brody, L.L.; !1Coulter, S.N.; Folger, K.R.; Kas, A.; Larbig, K.; Lim, R.M.; !1Smith, K.A.; Spencer, D.H.; Wong, G.K.S.; Wu, Z.; Paulsen, !1I.T.; Reizer, J.; Saier, M.H.; Hancock, R.E.W.; Lory, S.; !1Olson, M.V. !$#journal Nature (2000) 406:959-964 !$#title Complete genome sequence of Pseudomonas aeruginosa PA01, an !1opportunistic pathogen. !$#cross-references MUID:20437337; PMID:10984043 !$#accession D83078 !'##status preliminary !'##molecule_type DNA !'##residues 1-290 ##label STO !'##cross-references GB:AE004867; GB:AE004091; NID:g9950769; !1PIDN:AAG07916.1; GSPDB:GN00131; PASP:PA4528 !'##experimental_source strain PAO1 GENETICS !$#gene pilD; xcpA; pilD; PA4528 CLASSIFICATION #superfamily type IV prepilin peptidase KEYWORDS hydrolase; methyltransferase; S-adenosylmethionine; !1transmembrane protein SUMMARY #length 290 #molecular-weight 31870 #checksum 7644 SEQUENCE /// ENTRY B36961 #type complete TITLE type IV prepilin peptidase (EC 3.4.-.-) - Pseudomonas putida CONTAINS type IV pilin N-methyltransferase (EC 2.1.1.-) ORGANISM #formal_name Pseudomonas putida DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B36961; S35953 REFERENCE A36961 !$#authors de Groot, A.; Heijnen, I.; de Cock, H.; Filloux, A.; !1Tommassen, J. !$#journal J. Bacteriol. (1994) 176:642-650 !$#title Characterization of type IV pilus genes in plant !1growth-promoting Pseudomonas putida WCS358. !$#cross-references MUID:94131942; PMID:7905475 !$#accession B36961 !'##status preliminary !'##molecule_type DNA !'##residues 1-288 ##label DEA !'##cross-references EMBL:X74276; NID:g396262; PIDN:CAA52334.1; !1PID:g396265 GENETICS !$#gene pilD; xcpA CLASSIFICATION #superfamily type IV prepilin peptidase KEYWORDS hydrolase; methyltransferase; S-adenosylmethionine SUMMARY #length 288 #molecular-weight 31972 #checksum 7014 SEQUENCE /// ENTRY S11803 #type complete TITLE pullulanase secretion protein pulO - Klebsiella pneumoniae ORGANISM #formal_name Klebsiella pneumoniae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S11803 REFERENCE S11799 !$#authors Pugsley, A.P.; Reyss, I. !$#journal Mol. Microbiol. (1990) 4:365-379 !$#title Five genes at the 3' end of the Klebsiella pneumoniae pulC !1operon are required for pullulanase secretion. !$#cross-references MUID:90286914; PMID:2162463 !$#accession S11803 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-228 ##label PUG !'##cross-references GB:X52462; NID:g43917; PIDN:CAA36700.1; PID:g43922 GENETICS !$#gene pulO CLASSIFICATION #superfamily type IV prepilin peptidase KEYWORDS transmembrane protein SUMMARY #length 228 #molecular-weight 24753 #checksum 8274 SEQUENCE /// ENTRY S32869 #type complete TITLE secretion protein outO - Erwinia carotovora subsp. carotovora ORGANISM #formal_name Erwinia carotovora subsp. carotovora DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S32869; S31758 REFERENCE S32857 !$#authors Reeves, P.J.; Whitcombe, D.; Wharam, S.; Gibson, M.; !1Allison, G.; Bunce, N.; Barallon, R.; Douglas, P.; !1Mulholland, V.; Stevens, S.; Walker, D.; Salmond, G.P.C. !$#journal Mol. Microbiol. (1993) 8:443-456 !$#title Molecular cloning and characterization of 13 out genes from !1Erwinia carotovora subspecies carotovora: genes encoding !1members of a general secretion pathway (GSP) widespread in !1gram-negative bacteria. !$#cross-references MUID:93316842; PMID:8326859 !$#accession S32869 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-279 ##label REE !'##cross-references EMBL:X70049; NID:g42184; PIDN:CAA49656.1; !1PID:g581154 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1992 GENETICS !$#gene outO !$#start_codon GTG CLASSIFICATION #superfamily type IV prepilin peptidase SUMMARY #length 279 #molecular-weight 31131 #checksum 5854 SEQUENCE /// ENTRY S70810 #type complete TITLE type IV prepilin peptidase (EC 3.4.99.-) xpsO - Xanthomonas campestris pv. campestris CONTAINS type IV pilin N-methyltransferase (EC 2.1.1.-) ORGANISM #formal_name Xanthomonas campestris pv. campestris DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S70810 REFERENCE S70809 !$#authors Hu, N.T.; Lee, P.F.; Chen, C. !$#journal Mol. Microbiol. (1995) 18:769-777 !$#title The type IV pre-pilin leader peptidase of Xanthomonas !1campestris pv. campestris is functional without conserved !1cysteine residues. !$#cross-references MUID:96414476; PMID:8817497 !$#accession S70810 !'##status preliminary !'##molecule_type DNA !'##residues 1-287 ##label HUN !'##cross-references EMBL:U12432; NID:g529681; PIDN:AAC43571.1; !1PID:g529683 GENETICS !$#gene xpsO CLASSIFICATION #superfamily type IV prepilin peptidase KEYWORDS hydrolase; methyltransferase; S-adenosylmethionine SUMMARY #length 287 #molecular-weight 31843 #checksum 233 SEQUENCE /// ENTRY S70875 #type complete TITLE type IV prepilin peptidase (EC 3.4.99.-) tapD - Aeromonas hydrophila ALTERNATE_NAMES prepilin type IV peptidase CONTAINS type IV pilin N-methyltransferase (EC 2.1.1.-) ORGANISM #formal_name Aeromonas hydrophila DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S70875 REFERENCE S70872 !$#authors Pepe, C.M.; Eklund, M.W.; Strom, M.S. !$#journal Mol. Microbiol. (1996) 19:857-869 !$#title Cloning of an Aeromonas hydrophila type IV pilus biogenesis !1gene cluster: complementation of pilus assembly functions !1and characterization of a type IV leader peptidase/ !1N-methyltransferase required for extracellular protein !1secretion. !$#cross-references MUID:96417863; PMID:8820654 !$#accession S70875 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-290 ##label PEP !'##cross-references EMBL:U20255; NID:g695159; PIDN:AAC43998.1; !1PID:g663118 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1995 GENETICS !$#gene tapD CLASSIFICATION #superfamily type IV prepilin peptidase KEYWORDS hydrolase; methyltransferase; S-adenosylmethionine SUMMARY #length 290 #molecular-weight 32308 #checksum 2223 SEQUENCE /// ENTRY C47755 #type complete TITLE pectic enzyme secretion protein OutO - Erwinia chrysanthemi ORGANISM #formal_name Erwinia chrysanthemi DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C47755 REFERENCE A47021 !$#authors Lindeberg, M.; Collmer, A. !$#journal J. Bacteriol. (1992) 174:7385-7397 !$#title Analysis of eight out genes in a cluster required for pectic !1enzyme secretion by Erwinia chrysanthemi: sequence !1comparison with secretion genes from other gram-negative !1bacteria. !$#cross-references MUID:93054355; PMID:1429461 !$#accession C47755 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-283 ##label LIN !'##cross-references GB:L02214; NID:g148432; PIDN:AAA24841.1; !1PID:g148444 !'##note sequence extracted from NCBI backbone (NCBIP:118281) CLASSIFICATION #superfamily type IV prepilin peptidase KEYWORDS transmembrane protein SUMMARY #length 283 #molecular-weight 31355 #checksum 9186 SEQUENCE /// ENTRY B65083 #type complete TITLE secretion protein b2972 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS B65083 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65083 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-310 ##label BLAT !'##cross-references GB:AE000379; GB:U00096; NID:g2367179; !1PIDN:AAC76008.1; PID:g1789343; UWGP:b2972 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily type IV prepilin peptidase SUMMARY #length 310 #molecular-weight 34273 #checksum 8819 SEQUENCE /// ENTRY A40582 #type complete TITLE type IV prepilin peptidase (EC 3.4.99.-) tcpJ - Vibrio cholerae ALTERNATE_NAMES tcpJ protein; toxin-coregulated pilin signal peptidase (TCP) CONTAINS type IV pilin N-methyltransferase (EC 2.1.1.-) ORGANISM #formal_name Vibrio cholerae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A40582; C45247; S23275; S38788; PC1107 REFERENCE A40582 !$#authors Kaufman, M.R.; Seyer, J.M.; Taylor, R.K. !$#journal Genes Dev. (1991) 5:1834-1846 !$#title Processing of TCP pilin by TcpJ typifies a common step !1intrinsic to a newly recognized pathway of extracellular !1protein secretion by gram-negative bacteria. !$#cross-references MUID:92009174; PMID:1680773 !$#accession A40582 !'##status preliminary !'##molecule_type DNA !'##residues 1-253 ##label KAU !'##cross-references GB:M74708; NID:g155288; PIDN:AAA63557.1; !1PID:g155289 !'##note the authors translated the codon CCA for residue 149 as Gln, !1and CAA for residue 151 as Pro REFERENCE A45247 !$#authors Higgins, D.E.; Nazareno, E.; DiRita, V.J. !$#journal J. Bacteriol. (1992) 174:6974-6980 !$#title The virulence gene activator ToxT from Vibrio cholerae is a !1member of the AraC family of transcriptional activators. !$#cross-references MUID:93015761; PMID:1400247 !$#accession C45247 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-20 ##label HIG !'##cross-references GB:L01623; NID:g155283 !'##experimental_source strain 569B !'##note sequence extracted from NCBI backbone (NCBIP:116935) REFERENCE S23274 !$#authors Ogierman, M.A.; Manning, P.A. !$#journal Gene (1992) 116:93-97 !$#title Homology of TcpN, a putative regulatory protein of Vibrio !1cholerae, to the AraC family of transcriptional activators. !$#cross-references MUID:92331956; PMID:1352761 !$#accession S23275 !'##molecule_type DNA !'##residues 1-38,'NG',41,'G',43-71,'N' ##label OGI !'##cross-references EMBL:X64098 !'##experimental_source strain ssp. classical 01, Z17561 REFERENCE S23261 !$#authors Manning, P.A. !$#submission submitted to the EMBL Data Library, January 1992 !$#accession S38788 !'##molecule_type DNA !'##residues 1-71,'N' ##label MAN !'##cross-references EMBL:X64098; NID:g48404; PIDN:CAA45466.1; !1PID:g48419 !'##experimental_source strain ssp. classical 01, Z17561 GENETICS !$#gene tcpJ CLASSIFICATION #superfamily type IV prepilin peptidase KEYWORDS hydrolase; methyltransferase; S-adenosylmethionine; !1transmembrane protein SUMMARY #length 253 #molecular-weight 29351 #checksum 762 SEQUENCE /// ENTRY S47153 #type complete TITLE type IV prepilin peptidase (EC 3.4.99.-) BfpP - Escherichia coli CONTAINS type IV pilin N-methyltransferase (EC 2.1.1.-) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S47153; S70974 REFERENCE S47153 !$#authors Zhang, H.; Lory, S.; Donnenberg, M.S. !$#submission submitted to the EMBL Data Library, June 1994 !$#description A plasmid encoded prepilin peptidase from enteropathogenic !1Escherichia coli. !$#accession S47153 !'##molecule_type DNA !'##residues 1-249 ##label ZHA !'##cross-references EMBL:Z34464; NID:g499386; PIDN:CAA84229.1; !1PID:g499387 REFERENCE S70966 !$#authors Stone, K.D.; Zhang, H.Z.; Carlson, L.K.; Donnenberg, M.S. !$#journal Mol. Microbiol. (1996) 20:325-337 !$#title A cluster of fourteen genes from enteropathogenic !1Escherichia coli is sufficient for the biogenesis of a type !1IV pilus. !$#cross-references MUID:96310370; PMID:8733231 !$#accession S70974 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-249 ##label STO !'##cross-references EMBL:Z68186; NID:g1122399; PIDN:CAA92334.1; !1PID:g1122408 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1995 GENETICS !$#gene bfpP CLASSIFICATION #superfamily type IV prepilin peptidase KEYWORDS hydrolase; methyltransferase; S-adenosylmethionine SUMMARY #length 249 #molecular-weight 27986 #checksum 8083 SEQUENCE /// ENTRY ZPECL #type complete TITLE signal peptidase II (EC 3.4.23.36) - Escherichia coli (strain K-12) ALTERNATE_NAMES premurein leader peptidase; prolipoprotein signal peptidase; signal peptidase II ORGANISM #formal_name Escherichia coli DATE 25-Feb-1985 #sequence_revision 05-Dec-1997 #text_change 03-Jun-2002 ACCESSIONS C64723; B91325; B93991; S40550; A00999 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64723 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-164 ##label BLAT !'##cross-references GB:AE000113; GB:U00096; NID:g2367095; !1PIDN:AAC73138.1; PID:g1786210; UWGP:b0027 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A91325 !$#authors Yu, F.; Yamada, H.; Daishima, K.; Mizushima, S. !$#journal FEBS Lett. (1984) 173:264-268 !$#title Nucleotide sequence of the lspA gene, the structural gene !1for lipoprotein signal peptidase of Escherichia coli. !$#cross-references MUID:84261953; PMID:6378662 !$#accession B91325 !'##molecule_type DNA !'##residues 1-9,'V',11-164 ##label YUF REFERENCE A93991 !$#authors Innis, M.A.; Tokunaga, M.; Williams, M.E.; Loranger, J.M.; !1Chang, S.Y.; Chang, S.; Wu, H.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:3708-3712 !$#title Nucleotide sequence of the Escherichia coli prolipoprotein !1signal peptidase (lsp) gene. !$#cross-references MUID:84222028; PMID:6374664 !$#accession B93991 !'##molecule_type DNA !'##residues 1-164 ##label INN !'##cross-references GB:D10483; GB:J01597; GB:J01683; GB:J01706; !1GB:K01298; GB:K01990; GB:M10420; GB:M10611; GB:M12544; !1GB:V00259; GB:X04711; GB:X54847; GB:X54945; GB:X55034; !1GB:X56742; NID:g216434; PIDN:BAA01305.1; PID:g216454 REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40550 !'##status preliminary !'##molecule_type DNA !'##residues 1-164 ##label YUR !'##cross-references EMBL:D10483; NID:g216434; PIDN:BAA01305.1; !1PID:g216454 COMMENT This protein is one of the two peptidases identified in E. !1coli; it specifically catalyzes the removal of signal !1peptides from prolipoproteins. It is believed to be a !1transmembrane protein. GENETICS !$#gene lspA !$#map_position 1 min CLASSIFICATION #superfamily lipoprotein signal peptidase KEYWORDS aspartic proteinase; hydrolase; transmembrane protein FEATURE !$15-31 #domain transmembrane #status predicted #label TM1\ !$71-87 #domain transmembrane #status predicted #label TM2\ !$137-153 #domain transmembrane #status predicted #label TM3 SUMMARY #length 164 #molecular-weight 18156 #checksum 5145 SEQUENCE /// ENTRY PRECT4 #type complete TITLE proteinase IV (EC 3.4.-.-) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS F64936; A24813; I59590; I81186; I81187; I81194; I81189; !1I81192; I81193; I81207; I81208; I81190; I81188 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64936 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-618 ##label BLAT !'##cross-references GB:AE000271; GB:U00096; NID:g1788058; !1PIDN:AAC74836.1; PID:g1788064; UWGP:b1766 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A24813 !$#authors Ichihara, S.; Suzuki, T.; Suzuki, M.; Mizushima, S. !$#journal J. Biol. Chem. (1986) 261:9405-9411 !$#title Molecular cloning and sequencing of the sppA gene and !1characterization of the encoded protease IV, a signal !1peptide peptidase, of Escherichia coli. !$#cross-references MUID:86250892; PMID:3522590 !$#accession A24813 !'##molecule_type DNA !'##residues 1-377,'T',379-618 ##label ICH !'##cross-references GB:M13359; NID:g147867; PIDN:AAA24648.1; !1PID:g147868 REFERENCE I59590 !$#authors Guttman, D.S.; Dykhuizen, D.E. !$#journal Science (1994) 266:1380-1383 !$#title Clonal divergence in Escherichia coli is driven by !1recombination, not mutation. !$#cross-references MUID:95064015; PMID:7973728 !$#accession I59590 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 110-377,'T',379-433 ##label RES !'##cross-references EMBL:U13772; NID:g535523; PIDN:AAA57008.1; !1PID:g535524 !'##experimental_source strain ECOR4 !$#accession I81186 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 110-377,'T',379-433 ##label RE2 !'##cross-references EMBL:U13773; NID:g535525; PIDN:AAA57009.1; !1PID:g535526 !'##experimental_source strain ECOR8 !$#accession I81187 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 110-377,'T',379-433 ##label RE3 !'##cross-references EMBL:U13774; NID:g535527; PIDN:AAA57010.1; !1PID:g535528 !'##experimental_source strain ECOR10 !$#accession I81194 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 110-377,'T',379-433 ##label RE4 !'##cross-references EMBL:U13782; NID:g535541; PIDN:AAA57017.1; !1PID:g535542 !'##experimental_source strain K12 !$#accession I81189 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 110-251,'Q',253-293,'T',295-377,'T',379-433 ##label RE5 !'##cross-references EMBL:U13776; NID:g535531; PIDN:AAA57012.1; !1PID:g535532 !'##experimental_source strain ECOR65 !$#accession I81192 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 110-251,'Q',253-293,'T',295-377,'T',379-433 ##label RE6 !'##cross-references EMBL:U13779; NID:g535537; PIDN:AAA57015.1; !1PID:g535538 !'##experimental_source strain ECOR40 !$#accession I81193 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 110-251,'Q',253-293,'T',295-377,'T',379-433 ##label RE7 !'##cross-references EMBL:U13780; NID:g535539; PIDN:AAA57016.1; !1PID:g535540 !'##experimental_source strain ECOR39 !$#accession I81207 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 110-251,'Q',253-293,'T',295-377,'T',379-433 ##label RE8 !'##cross-references EMBL:U13833; NID:g535567; PIDN:AAA57030.1; !1PID:g535568 !'##experimental_source strain ECOR38 !$#accession I81208 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 110-251,'Q',253-377,'T',379-433 ##label RE9 !'##cross-references EMBL:U13834; NID:g535569; PIDN:AAA57031.1; !1PID:g535570 !'##experimental_source strain ECOR68 !$#accession I81190 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 110-150,'I',152-251,'Q',253-293,'T',295-377,'T',379-433 !1##label RE0 !'##cross-references EMBL:U13777; NID:g535533; PIDN:AAA57013.1; !1PID:g535534 !'##experimental_source strain ECOR50 !$#accession I81188 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 110-185,'S',187-251,'H',253-377,'T',379-433 ##label RE11 !'##cross-references EMBL:U13775; NID:g535529; PIDN:AAA57011.1; !1PID:g535530 !'##experimental_source strain ECOR16 COMMENT The signal peptide peptidase activity of this membrane !1protein is necessary to maintain proper secretion of mature !1proteins across the membrane. GENETICS !$#gene sppA COMPLEX homotetramer FUNCTION !$#description catalyzes the hydrolysis of cleaved signal peptides CLASSIFICATION #superfamily proteinase IV KEYWORDS homotetramer; hydrolase; transmembrane protein FEATURE !$29-45 #domain transmembrane #status predicted #label TM1\ !$398-414 #domain transmembrane #status predicted #label TM2\ !$421-441 #domain transmembrane #status predicted #label TM3 SUMMARY #length 618 #molecular-weight 67219 #checksum 5853 SEQUENCE /// ENTRY W2AD35 #type complete TITLE late L3 23K proteinase (EC 3.4.22.-) - human adenovirus 2 ORGANISM #formal_name Mastadenovirus h2 #common_name human adenovirus 2 #note host Homo sapiens (man) DATE 30-Apr-1981 #sequence_revision 08-Oct-1981 #text_change 23-Feb-1997 ACCESSIONS A03823; B03823 REFERENCE A93720 !$#authors Akusjarvi, G.; Zabielski, J.; Perricaudet, M.; Pettersson, !1U. !$#journal Nucleic Acids Res. (1981) 9:1-17 !$#title The sequence of the 3' non-coding region of the hexon mRNA !1discloses a novel adenovirus gene. !$#cross-references MUID:81150446; PMID:6259616 !$#accession A03823 !'##molecule_type mRNA !'##residues 1-204 ##label AKU !'##note this protein is translated from the 3'-terminal nucleotides of !1the hexon mRNA REFERENCE A91283 !$#authors Buttner, W.; Veres-Molnar, Z. !$#journal FEBS Lett. (1980) 122:317-321 !$#title Localization of the 3'-terminal end of the EcoRI B !1fragment-specific early mRNA of adenovirus type 2. !$#cross-references MUID:81138857; PMID:6258984 !$#accession B03823 !'##molecule_type DNA !'##residues 167-204 ##label BUT CLASSIFICATION #superfamily adenovirus late L3 23K proteinase KEYWORDS cysteine proteinase; hydrolase; late protein FEATURE !$54,71,122 #active_site His, Glu, Cys #status experimental SUMMARY #length 204 #molecular-weight 23087 #checksum 5737 SEQUENCE /// ENTRY W2AD55 #type complete TITLE late L3 23K proteinase (EC 3.4.22.-) - human adenovirus 5 ORGANISM #formal_name Mastadenovirus h5 #common_name human adenovirus 5 #note host Homo sapiens (man) DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 22-Oct-1999 ACCESSIONS C03823; A03823 REFERENCE A93716 !$#authors Kruijer, W.; van Schaik, F.M.A.; Sussenbach, J.S. !$#journal Nucleic Acids Res. (1980) 8:6033-6042 !$#title Nucleotide sequence analysis of a region of adenovirus 5 DNA !1encoding a hitherto unidentified gene. !$#cross-references MUID:81124316; PMID:6258160 !$#accession C03823 !'##molecule_type DNA !'##residues 1-204 ##label KRU !'##cross-references GB:X02997; GB:J01966; GB:J01980; GB:K02368; !1GB:V00029; GB:V00030; NID:g58498; PIDN:CAA26754.1; !1PID:g563779 CLASSIFICATION #superfamily adenovirus late L3 23K proteinase KEYWORDS cysteine proteinase; hydrolase; late protein FEATURE !$54,71,122 #active_site His, Glu, Cys #status predicted SUMMARY #length 204 #molecular-weight 23068 #checksum 5677 SEQUENCE /// ENTRY W2AD04 #type complete TITLE late L3 23K proteinase (EC 3.4.22.-) - human adenovirus 4 ORGANISM #formal_name Mastadenovirus h4 #common_name human adenovirus 4 DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 18-Jun-1999 ACCESSIONS A27473 REFERENCE A27473 !$#authors Houde, A.; Weber, J.M. !$#journal Gene (1987) 54:51-56 !$#title Sequence of the protease of human subgroup E adenovirus type !14. !$#cross-references MUID:87277432; PMID:3301540 !$#accession A27473 !'##molecule_type DNA !'##residues 1-201 ##label HOU !'##cross-references GB:M16692; NID:g209875; PIDN:AAA42466.1; !1PID:g209876 GENETICS !$#map_position 59.8-61.9 CLASSIFICATION #superfamily adenovirus late L3 23K proteinase KEYWORDS cysteine proteinase; hydrolase; late protein FEATURE !$56,73,127 #active_site His, Asp, Cys #status predicted SUMMARY #length 201 #molecular-weight 22787 #checksum 3796 SEQUENCE /// ENTRY W2AD12 #type complete TITLE late L3 23K proteinase (EC 3.4.22.-) - human adenovirus 12 (strain Pereira 1131) ALTERNATE_NAMES late protein 3 ORGANISM #formal_name Mastadenovirus h12 #common_name human adenovirus 12 #variety strain Pereira 1131 #note host Homo sapiens (man) DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 18-Jun-1999 ACCESSIONS S01731; S33943 REFERENCE S01730 !$#authors Houde, A.; Weber, J.M. !$#journal Nucleic Acids Res. (1988) 16:7195 !$#title The primary structure of human adenovirus type 12 protease. !$#cross-references MUID:88303354; PMID:3043380 !$#accession S01731 !'##status translation not shown !'##molecule_type DNA !'##residues 1-206 ##label HOU !'##cross-references EMBL:X07655; NID:g58468; PIDN:CAA30501.1; !1PID:g58470 REFERENCE S33928 !$#authors Sprengel, J. !$#submission submitted to the EMBL Data Library, June 1993 !$#accession S33943 !'##molecule_type DNA !'##residues 1-179,'N',181-206 ##label SPR !'##cross-references EMBL:X73487; NID:g313361; PIDN:CAA51892.1; !1PID:g313377 CLASSIFICATION #superfamily adenovirus late L3 23K proteinase KEYWORDS cysteine proteinase; hydrolase; late protein FEATURE !$54,71,122 #active_site His, Asp, Cys #status predicted SUMMARY #length 206 #molecular-weight 23455 #checksum 9781 SEQUENCE /// ENTRY W2AD40 #type complete TITLE late L3 23K proteinase (EC 3.4.22.-) - human adenovirus 40 ORGANISM #formal_name Mastadenovirus h40 #common_name human adenovirus 40 DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 18-Jun-1999 ACCESSIONS B28645 REFERENCE A94371 !$#authors Vos, H.L.; van der Lee, F.M.; Reemst, A.M.C.B.; van Loon, !1A.E.; Sussenbach, J.S. !$#journal Virology (1988) 163:1-10 !$#title The genes encoding the DNA binding protein and the 23K !1protease of adenovirus types 40 and 41. !$#cross-references MUID:88160034; PMID:3279700 !$#accession B28645 !'##molecule_type DNA !'##residues 1-205 ##label VOS !'##cross-references GB:L19443; NID:g303969; PIDN:AAC13968.1; !1PID:g303990 CLASSIFICATION #superfamily adenovirus late L3 23K proteinase KEYWORDS cysteine proteinase; hydrolase; late protein FEATURE !$54,71,122 #active_site His, Asp, Cys #status predicted SUMMARY #length 205 #molecular-weight 23337 #checksum 5550 SEQUENCE /// ENTRY W2AD41 #type complete TITLE late L3 23K proteinase (EC 3.4.22.-) - human adenovirus 41 ORGANISM #formal_name Mastadenovirus h41 #common_name human adenovirus 41 DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 18-Jun-1999 ACCESSIONS E28645; S08658 REFERENCE A94371 !$#authors Vos, H.L.; van der Lee, F.M.; Reemst, A.M.C.B.; van Loon, !1A.E.; Sussenbach, J.S. !$#journal Virology (1988) 163:1-10 !$#title The genes encoding the DNA binding protein and the 23K !1protease of adenovirus types 40 and 41. !$#cross-references MUID:88160034; PMID:3279700 !$#accession E28645 !'##molecule_type DNA !'##residues 1-214 ##label VOS !'##cross-references GB:M21163; NID:g209865; PIDN:AAA42462.1; !1PID:g209869 REFERENCE S08656 !$#authors Toogood, C.I.A.; Murali, R.; Burnett, M.; Hay, R.T. !$#submission submitted to the EMBL Data Library, February 1990 !$#accession S08658 !'##molecule_type DNA !'##residues 1-198 ##label TOO !'##cross-references EMBL:X51783; NID:g58562; PIDN:CAA36080.1; !1PID:g58565 CLASSIFICATION #superfamily adenovirus late L3 23K proteinase KEYWORDS cysteine proteinase; hydrolase; late protein FEATURE !$54,71,122 #active_site His, Asp, Cys #status predicted SUMMARY #length 214 #molecular-weight 24482 #checksum 2097 SEQUENCE /// ENTRY B48550 #type complete TITLE late L3 23K proteinase (EC 3.4.22.-) - canine adenovirus 1 ALTERNATE_NAMES endoproteinase ORGANISM #formal_name Mastadenovirus can1 #common_name canine adenovirus 1 DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 18-Jun-1999 ACCESSIONS B48550 REFERENCE A48550 !$#authors Cai, F.; Weber, J.M. !$#journal Virus Genes (1992) 6:307-312 !$#title Nucleotide and deduced amino acid sequence of the canine !1adenovirus type 1 proteinase. !$#cross-references MUID:93033182; PMID:1413543 !$#accession B48550 !'##molecule_type DNA !'##residues 1-206 ##label CAI !'##cross-references GB:M72715; NID:g210022; PIDN:AAA42529.1; !1PID:g210024 !'##note sequence extracted from NCBI backbone (NCBIN:114644, !1NCBIP:114648) CLASSIFICATION #superfamily adenovirus late L3 23K proteinase KEYWORDS cysteine proteinase; hydrolase; late protein FEATURE !$57,74,125 #active_site His, Asp, Cys #status predicted SUMMARY #length 206 #molecular-weight 23326 #checksum 9247 SEQUENCE /// ENTRY PRVZWR #type complete TITLE retroviral proteinase-like protein - vaccinia virus (strain WR) ALTERNATE_NAMES F2L protein ORGANISM #formal_name vaccinia virus DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 18-Jun-1999 ACCESSIONS A32907; H36213; A31310 REFERENCE A32907 !$#authors Slabaugh, M.B.; Roseman, N.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:4152-4155 !$#title Retroviral protease-like gene in the vaccinia virus genome. !$#cross-references MUID:89264577; PMID:2657744 !$#accession A32907 !'##molecule_type DNA !'##residues 1-144 ##label SLA !'##cross-references GB:M25392; NID:g335616; PIDN:AAA48238.1; !1PID:g335617 REFERENCE A36213 !$#authors Roseman, N.A.; Slabaugh, M.B. !$#journal Virology (1990) 178:410-418 !$#title The vaccinia virus HindIII F fragment: nucleotide sequence !1of the left 6.2 kb. !$#cross-references MUID:91020979; PMID:2219701 !$#accession H36213 !'##molecule_type DNA !'##residues 1-144 ##label ROS !'##cross-references EMBL:M34368 CLASSIFICATION #superfamily retroviral proteinase SUMMARY #length 144 #molecular-weight 16012 #checksum 9571 SEQUENCE /// ENTRY PRVZ7F #type complete TITLE probable dUTP diphosphatase (EC 3.6.1.23) - vaccinia virus (strain Copenhagen and Ankara) ALTERNATE_NAMES dUTPase; F2L protein ORGANISM #formal_name vaccinia virus #variety strain Ankara and Copenhagen #note host Homo sapiens (man) DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 03-Jun-2002 ACCESSIONS G42506; T30780 REFERENCE A42501 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:517-563 !$#title Appendix to "The complete DNA sequence of vaccinia virus". !$#accession G42506 !'##molecule_type DNA !'##residues 1-147 ##label GOE !'##cross-references GB:M35027; NID:g335317; PIDN:AAA48015.1; !1PID:g335363 !'##experimental_source strain Copenhagen REFERENCE A42531 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:247-266 !$#title The complete DNA sequence of vaccinia virus. !$#cross-references MUID:91021027; PMID:2219722 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given REFERENCE Z20877 !$#authors Antoine, G.; Scheiflinger, F.; Falkner, F.G.; Dorner, F. !$#submission submitted to the EMBL Data Library, March 1997 !$#description The complete genomic sequence of the Modified Vaccinia !1Ankara (MVA) strain. !$#accession T30780 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-147 ##label ANT !'##cross-references EMBL:U94848; PIDN:AAB96413.1 !'##experimental_source strain Ankara GENETICS !$#note MVA030L CLASSIFICATION #superfamily retroviral proteinase KEYWORDS hydrolase; nucleotide metabolism; proteinase SUMMARY #length 147 #molecular-weight 16264 #checksum 5962 SEQUENCE /// ENTRY XDEC #type complete TITLE asparaginase (EC 3.5.1.1) II precursor [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 24-Apr-1984 #sequence_revision 31-Dec-1990 #text_change 01-Mar-2002 ACCESSIONS A35132; JU0301; A01000; D65081 REFERENCE A35132 !$#authors Jennings, M.P.; Beacham, I.R. !$#journal J. Bacteriol. (1990) 172:1491-1498 !$#title Analysis of the Escherichia coli gene encoding !1L-asparaginase II, ansB, and its regulation by cyclic AMP !1receptor and FNR proteins. !$#cross-references MUID:90170867; PMID:2407723 !$#accession A35132 !'##molecule_type DNA !'##residues 1-348 ##label JEN !'##cross-references EMBL:X52540 REFERENCE JU0301 !$#authors Bonthron, D.T. !$#journal Gene (1990) 91:101-105 !$#title L-Asparaginase II of Escherichia coli K-12: cloning, mapping !1and sequencing of the ansB gene. !$#cross-references MUID:90382683; PMID:2144836 !$#accession JU0301 !'##molecule_type DNA !'##residues 1-348 ##label BON !'##cross-references GB:M34234; NID:g145276; PIDN:AAA23445.1; !1PID:g145277 !'##experimental_source strain K12 JM108 REFERENCE A01000 !$#authors Maita, T.; Matsuda, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1980) 361:105-117 !$#title The primary structure of L-asparaginase from Escherichia !1coli. !$#cross-references MUID:80135739; PMID:6766894 !$#accession A01000 !'##molecule_type protein !'##residues 23-48,'A',50-85,'D',87-131,133-155,157-170,172-205,'D', !1207-267,'D',269-273,'T',275-284,'D',286-289,291-329,331-348 !1##label MAI REFERENCE A32655 !$#authors Peterson, R.G.; Richards, F.F.; Handschumacher, R.E. !$#journal J. Biol. Chem. (1977) 252:2072-2076 !$#title Structure of peptide from active site region of Escherichia !1coli L-asparaginase. !$#cross-references MUID:77140944; PMID:321449 !$#contents annotation; active site REFERENCE A37451 !$#authors Greenquist, A.C.; Wriston Jr., J.C. !$#journal Arch. Biochem. Biophys. (1972) 152:280-286 !$#title Chemical evidence for identical subunits in L-asparginase !1from Escherichia coli B. !$#cross-references MUID:73007901; PMID:4561256 !$#contents annotation !$#note the cysteine residues were quantitated and shown to form !1intrachain bonds REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65081 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-348 ##label BLAT !'##cross-references GB:AE000378; GB:U00096; NID:g1789319; !1PIDN:AAC75994.1; PID:g1789327; UWGP:b2957 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ansB !$#map_position 64 min COMPLEX homotetramer FUNCTION !$#description EC 3.5.1.1 [validated, MUID:90170867]; catalyzes the !1hydrolysis of asparagine to aspartic acid !$#note has a higher affinity for asparagine than asparaginase I !1(PIR:XDEC1) !$#note positively regulated by cAMP receptor protein (CRP) !1(PIR:QRECC) and by FNR protein (PIR:RGECF) [validated, !1MUID:94018602] CLASSIFICATION #superfamily asparaginase KEYWORDS extracellular protein; homotetramer; hydrolase FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-348 #product asparaginase #status experimental #label !8MAT\ !$99-127 #disulfide_bonds #status experimental\ !$142 #active_site Ser #status experimental SUMMARY #length 348 #molecular-weight 36850 #checksum 788 SEQUENCE /// ENTRY A28063 #type complete TITLE (EC 3.5.1.38) (EC 3.5.1.38) - Acinetobacter calcoaceticus ALTERNATE_NAMES glutaminase-asparaginase ORGANISM #formal_name Acinetobacter calcoaceticus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS A28063 REFERENCE A28063 !$#authors Tanaka, S.; Robinson, E.A.; Appella, E.; Miller, M.; Ammon, !1H.L.; Roberts, J.; Weber, I.T.; Wlodawer, A. !$#journal J. Biol. Chem. (1988) 263:8583-8591 !$#title Structures of amidohydrolases. Amino acid sequence of a !1glutaminase-asparaginase from Acinetobacter !1glutaminasificans and preliminary crystallographic data for !1an asparaginase from Erwinia chrysanthemi. !$#cross-references MUID:88243706; PMID:3379033 !$#accession A28063 !'##molecule_type protein !'##residues 1-331 ##label TAN !'##note the source is designated as Acinetobacter glutaminasificans CLASSIFICATION #superfamily asparaginase KEYWORDS hydrolase SUMMARY #length 331 #molecular-weight 35485 #checksum 4526 SEQUENCE /// ENTRY A26054 #type complete TITLE asparaginase (EC 3.5.1.1) precursor - Erwinia chrysanthemi ORGANISM #formal_name Erwinia chrysanthemi DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A26054; S03681 REFERENCE A26054 !$#authors Minton, N.P.; Bullman, H.M.S.; Scawen, M.D.; Atkinson, T.; !1Gilbert, H.J. !$#journal Gene (1986) 46:25-35 !$#title Nucleotide sequence of the Erwinia chrysanthemi NCPPB 1066 !1L-asparaginase gene. !$#cross-references MUID:87106840; PMID:3026924 !$#accession A26054 !'##molecule_type DNA !'##residues 1-348 ##label MIN !'##cross-references GB:M14741; GB:X14777; NID:g42965; PIDN:CAA32884.1; !1PID:g4185897 !'##note the authors translated the codon AAG for residue 286 as Leu REFERENCE S03681 !$#authors Filpula, D.; Nagle, J.W.; Pulford, S.; Anderson, D.M. !$#journal Nucleic Acids Res. (1988) 16:10385 !$#title Sequence of L-asparaginase gene from Erwinia chrysanthemi !1NCPPB 1125. !$#cross-references MUID:89057497; PMID:3194219 !$#accession S03681 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-176,'I',178-198,'R',200-287,'L',289-294,'M',296-348 !1##label FIL !'##cross-references GB:X12746; NID:g40993; PIDN:CAA31239.1; PID:g40994 CLASSIFICATION #superfamily asparaginase KEYWORDS hydrolase FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-348 #product asparaginase #status predicted #label MAT SUMMARY #length 348 #molecular-weight 37575 #checksum 9603 SEQUENCE /// ENTRY A39440 #type complete TITLE asparaginase (EC 3.5.1.1) ansA - Bacillus subtilis ALTERNATE_NAMES L-asparaginase ansA ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A39440; C40617; H69585 REFERENCE A39440 !$#authors Sun, D.; Setlow, P. !$#journal J. Bacteriol. (1991) 173:3831-3845 !$#title Cloning, nucleotide sequence, and expression of the Bacillus !1subtilis ans operon, which codes for L-asparaginase and !1L-aspartase. !$#cross-references MUID:91267950; PMID:1711029 !$#accession A39440 !'##molecule_type DNA !'##residues 1-329 ##label SUN !'##cross-references GB:M63264; NID:g142516; PIDN:AAA22243.1; !1PID:g142517 REFERENCE A40617 !$#authors Sun, D.; Setlow, P. !$#journal J. Bacteriol. (1993) 175:2501-2506 !$#title Cloning and nucleotide sequence of the Bacillus subtilis !1ansR gene, which encodes a repressor of the ans operon !1coding for L-asparaginase and L-aspartase. !$#cross-references MUID:93239674; PMID:8478318 !$#accession C40617 !'##molecule_type DNA !'##residues 1-23 ##label SU2 !'##note sequence extracted from NCBI backbone (NCBIN:130324, !1NCBIP:130336) REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69585 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-329 ##label KUN !'##cross-references GB:Z99116; GB:AL009126; NID:g2634723; !1PIDN:CAB14290.1; PID:g2634793 !'##experimental_source strain 168 GENETICS !$#gene ansA CLASSIFICATION #superfamily asparaginase KEYWORDS hydrolase SUMMARY #length 329 #molecular-weight 36454 #checksum 9433 SEQUENCE /// ENTRY JS0633 #type complete TITLE amidase (EC 3.5.1.4) - Aspergillus oryzae ALTERNATE_NAMES acetamidase ORGANISM #formal_name Aspergillus oryzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS JS0633; JQ1120 REFERENCE JS0633 !$#authors Gomi, K.; Kitamoto, K.; Kumagai, C. !$#journal Gene (1991) 108:91-98 !$#title Cloning and molecular characterization of the !1acetamidase-encoding gene (amdS) from Aspergillus oryzae. !$#cross-references MUID:92104511; PMID:1840550 !$#accession JS0633 !'##molecule_type DNA !'##residues 1-545 ##label GOM !'##cross-references GB:D10492; GB:D90466; NID:g217804; PIDN:BAA01373.1; !1PID:g217805 !'##experimental_source strain RIB40 REFERENCE JQ1120 !$#authors Gomi, K.; Kitamoto, K.; Kumagai, C. !$#submission submitted to JIPID, August 1991 !$#accession JQ1120 !'##molecule_type DNA !'##residues 1-507,'D',509-545 ##label GO2 !'##experimental_source strain RIB40 GENETICS !$#gene amdS !$#introns 89/3; 136/3; 227/1; 277/1; 329/3; 379/3 CLASSIFICATION #superfamily amidase KEYWORDS hydrolase SUMMARY #length 545 #molecular-weight 60156 #checksum 6286 SEQUENCE /// ENTRY A26511 #type complete TITLE amdS protein - Emericella nidulans ORGANISM #formal_name Emericella nidulans, Aspergillus nidulans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 24-Sep-1999 ACCESSIONS A26511 REFERENCE A26511 !$#authors Corrick, C.M.; Twomey, A.P.; Hynes, M.J. !$#journal Gene (1987) 53:63-71 !$#title The nucleotide sequence of the amdS gene of Aspergillus !1nidulans and the molecular characterization of 5' mutations. !$#cross-references MUID:87248110; PMID:3036667 !$#accession A26511 !'##status preliminary !'##molecule_type mRNA !'##residues 1-548 ##label COR !'##cross-references GB:M16371; NID:g168014; PIDN:AAA33295.1; !1PID:g168015 CLASSIFICATION #superfamily amidase SUMMARY #length 548 #molecular-weight 60228 #checksum 4254 SEQUENCE /// ENTRY S54538 #type complete TITLE amidase (EC 3.5.1.4) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YD8419.09; protein YDR242w ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-Nov-1999 ACCESSIONS S54538; S12326 REFERENCE S54530 !$#authors Oliver, K.; Harris, D. !$#submission submitted to the EMBL Data Library, May 1995 !$#accession S54538 !'##molecule_type DNA !'##residues 1-549 ##label OLI !'##cross-references EMBL:Z49701; NID:g817819; PIDN:CAA89728.1; !1PID:g817828; GSPDB:GN00004; MIPS:YDR242w !'##experimental_source strain AB972 REFERENCE S12326 !$#authors Chang, T.H.; Abelson, J. !$#journal Nucleic Acids Res. (1990) 18:7180 !$#title Identification of a putative amidase gene in yeast !1Saccharomyces cerevisiae. !$#cross-references MUID:91088341; PMID:2263500 !$#accession S12326 !'##molecule_type DNA !'##residues 1-524,'S',526-549 ##label CHA !'##cross-references EMBL:X56043; NID:g3363; PIDN:CAA39514.1; PID:g3364 GENETICS !$#gene SGD:AMD2; AMDY1; MIPS:YDR242w !'##cross-references SGD:S0002650; MIPS:YDR242w !$#map_position 4R CLASSIFICATION #superfamily amidase KEYWORDS hydrolase; transmembrane protein FEATURE !$159-175 #domain transmembrane #status predicted #label TMM SUMMARY #length 549 #molecular-weight 61409 #checksum 5708 SEQUENCE /// ENTRY URJB #type complete TITLE urease (EC 3.5.1.5) - jack bean ALTERNATE_NAMES urea amidohydrolase ORGANISM #formal_name Canavalia ensiformis #common_name jack bean DATE 28-Dec-1987 #sequence_revision 30-Sep-1993 #text_change 07-May-1999 ACCESSIONS JC1396; S01021; JT0001; A60883; S03364; JS0642 REFERENCE JC1396 !$#authors Riddles, P.W.; Whan, V.; Blakeley, R.L.; Zerner, B. !$#journal Gene (1992) 121:399-400 !$#cross-references MUID:93077062; PMID:1446838 !$#contents erratum !$#accession JC1396 !'##molecule_type mRNA !'##residues 1-840 ##label RID !'##cross-references GB:M65260 REFERENCE JS0642 !$#authors Riddles, P.W.; Whan, V.; Blakeley, R.L.; Zerner, B. !$#journal Gene (1991) 108:265-267 !$#title Cloning and sequencing of a jack bean urease-encoding cDNA. !$#cross-references MUID:92084145; PMID:1721034 !$#contents annotation !$#note this sequence has been revised in reference JC1396 REFERENCE S01021 !$#authors Takishima, K.; Suga, T.; Mamiya, G. !$#journal Eur. J. Biochem. (1988) 175:151-165 !$#title The structure of jack bean urease. The complete amino acid !1sequence, limited proteolysis and reactive cysteine !1residues. !$#cross-references MUID:88296463; PMID:3402446 !$#accession S01021 !'##molecule_type protein !'##residues 1-246,'R',248-840 ##label TA1 REFERENCE JT0001 !$#authors Mamiya, G.; Takishima, K.; Masakuni, M.; Kayumi, T.; Ogawa, !1K.; Sekita, T. !$#journal Proc. Jpn. Acad. B Phys. Biol. Sci. (1985) 61:395-398 !$#title Complete amino acid sequence of jack bean urease. !$#accession JT0001 !'##molecule_type protein !'##residues 1-246,'R',248-257,'P',259-268,'S',270-840 ##label TA2 REFERENCE A60883 !$#authors Mamiya, G.; Takishima, K.; Masakuni, M.; Kayumi, T.; Ogawa, !1K. !$#journal J. Protein Chem. (1987) 6:55-59 !$#title Complete amino acid sequence of jack bean urease. !$#accession A60883 !'##molecule_type protein !'##residues 1-246,'R',248-840 ##label TA3 REFERENCE S03364 !$#authors Takishima, K.; Mamiya, G. !$#journal Protein Seq. Data Anal. (1987) 1:103-106 !$#title Location of the essential cysteine residue of jack bean !1urease. !$#cross-references MUID:88190054; PMID:3447159 !$#accession S03364 !'##molecule_type protein !'##residues 591-637 ##label TA4 COMMENT Each chain of the hexamer binds two nickel ions. CLASSIFICATION #superfamily urease; urease 11K chain homology; urease 12K !1chain homology; urease 62K chain homology KEYWORDS homohexamer; hydrolase; metalloprotein; nickel FEATURE !$1-101 #domain urease 11K chain homology #label U11\ !$134-230 #domain urease 12K chain homology #label U12\ !$274-823 #domain urease 62K chain homology #label U62\ !$407,409,490,633 #binding_site nickel 2 (His, His, Lys, Asp) #status !8predicted\ !$490,519,545 #binding_site nickel 1 (Lys, His, His) #status !8predicted\ !$490 #binding_site carbon dioxide (Lys) (covalent) (by !8urease activase) #status predicted SUMMARY #length 840 #molecular-weight 90747 #checksum 7420 SEQUENCE /// ENTRY A36138 #type complete TITLE urease (EC 3.5.1.5) 11K chain [validated] - Klebsiella pneumoniae ALTERNATE_NAMES urea amidohydrolase; urease chain A; urease gamma chain ORGANISM #formal_name Klebsiella pneumoniae DATE 30-Nov-1990 #sequence_revision 02-Dec-1994 #text_change 05-Jan-2003 ACCESSIONS A36138; S32938 REFERENCE A36138 !$#authors Mulrooney, S.B.; Hausinger, R.P. !$#journal J. Bacteriol. (1990) 172:5837-5843 !$#title Sequence of the Klebsiella aerogenes urease genes and !1evidence for accessory proteins facilitating nickel !1incorporation. !$#cross-references MUID:91008957; PMID:2211515 !$#accession A36138 !'##molecule_type DNA !'##residues 1-100 ##label MUL !'##cross-references GB:M36068; NID:g149335; PIDN:AAA25149.1; !1PID:g149336 REFERENCE S32937 !$#authors Collins, C.M.; Gutman, D.M.; Laman, H. !$#journal Mol. Microbiol. (1993) 8:187-198 !$#title Identification of a nitrogen-regulated promoter controlling !1expression of Klebsiella pneumoniae urease genes. !$#cross-references MUID:93268094; PMID:8497192 !$#accession S32938 !'##molecule_type DNA !'##residues 1-66,'K',68-100 ##label COL !'##cross-references EMBL:L07039; NID:g149330; PIDN:AAA25147.1; !1PID:g149332 REFERENCE A65977 !$#authors Jabri, E.; Karplus, P.A. !$#submission submitted to the Brookhaven Protein Data Bank, June 1995 !$#cross-references PDB:1KRA !$#contents annotation; X-ray crystallography, 2.3 angstroms, residues !11-100 REFERENCE A56340 !$#authors Jabri, E.; Carr, M.B.; Hausinger, R.P.; Karplus, P.A. !$#journal Science (1995) 268:998-1004 !$#title The crystal structure of urease from Klebsiella aerogenes. !$#cross-references MUID:95273988; PMID:7754395 !$#contents annotation; X-ray crystallography, 2.3 angstroms GENETICS !$#gene ureA COMPLEX trimer of heterotrimeric subunits consisting of 11K (gamma), !112K (beta), and 62K (alpha) chains FUNCTION !$#description catalyzes the hydrolysis of one molecule of urea to carbon !1dioxide and two molecules of ammonia CLASSIFICATION #superfamily urease, gamma subunit; urease 11K chain !1homology KEYWORDS heterotrimer; hydrolase; metalloprotein FEATURE !$1-100 #domain urease 11K chain homology #label U11 SUMMARY #length 100 #molecular-weight 11087 #checksum 6873 SEQUENCE /// ENTRY B43719 #type complete TITLE urease (EC 3.5.1.5) 11K chain - Proteus mirabilis ALTERNATE_NAMES urease gamma chain ORGANISM #formal_name Proteus mirabilis DATE 03-Mar-1993 #sequence_revision 02-Dec-1994 #text_change 05-Jan-2003 ACCESSIONS B43719 REFERENCE A43719 !$#authors Jones, B.D.; Mobley, H.L.T. !$#journal J. Bacteriol. (1989) 171:6414-6422 !$#title Proteus mirabilis urease: nucleotide sequence determination !1and comparison with jack bean urease. !$#cross-references MUID:90078080; PMID:2687233 !$#accession B43719 !'##molecule_type DNA !'##residues 1-100 ##label JON !'##cross-references GB:M31834; NID:g150914; PIDN:AAA25667.1; !1PID:g150916 GENETICS !$#gene ureA FUNCTION !$#description catalyzes the hydrolysis of one molecule of urea to carbon !1dioxide and two molecules of ammonia CLASSIFICATION #superfamily urease, gamma subunit; urease 11K chain !1homology KEYWORDS heterotrimer; hydrolase; metalloprotein FEATURE !$1-100 #domain urease 11K chain homology #label U11 SUMMARY #length 100 #molecular-weight 10998 #checksum 7051 SEQUENCE /// ENTRY S08478 #type complete TITLE urease (EC 3.5.1.5) 11K chain - Proteus vulgaris ALTERNATE_NAMES urease gamma chain ORGANISM #formal_name Proteus vulgaris DATE 29-Jan-1993 #sequence_revision 02-Dec-1994 #text_change 05-Jan-2003 ACCESSIONS S08478 REFERENCE S08478 !$#authors Moersdorf, G.; Kaltwasser, H. !$#journal FEMS Microbiol. Lett. (1991) 66:67-74 !$#title Cloning of the genes encoding urease from Proteus vulgaris !1and sequencing of the structural genes. !$#cross-references MUID:92038908; PMID:1936938 !$#accession S08478 !'##molecule_type DNA !'##residues 1-100 ##label MOE !'##cross-references EMBL:X51816; NID:g45933; PIDN:CAA36113.1; !1PID:g45934 GENETICS !$#gene ureA COMPLEX trimer of heterotrimeric subunits consisting of 11K (gamma), !112K (beta), and 62K (alpha) chains FUNCTION !$#description catalyzes the hydrolysis of one molecule of urea to carbon !1dioxide and two molecules of ammonia CLASSIFICATION #superfamily urease, gamma subunit; urease 11K chain !1homology KEYWORDS heterotrimer; hydrolase; metalloprotein FEATURE !$1-100 #domain urease 11K chain homology #label U11 SUMMARY #length 100 #molecular-weight 10955 #checksum 5884 SEQUENCE /// ENTRY S10030 #type complete TITLE urease (EC 3.5.1.5) 11K chain - Ureaplasma urealyticum ALTERNATE_NAMES urease gamma chain ORGANISM #formal_name Ureaplasma urealyticum DATE 31-Dec-1990 #sequence_revision 02-Dec-1994 #text_change 05-Jan-2003 ACCESSIONS S10030 REFERENCE S10030 !$#authors Blanchard, A. !$#journal Mol. Microbiol. (1990) 4:669-676 !$#title Ureaplasma urealyticum urease genes; use of a UGA tryptophan !1codon. !$#cross-references MUID:90279510; PMID:2191184 !$#accession S10030 !'##molecule_type DNA !'##residues 1-101 ##label BLA !'##cross-references EMBL:X51315; NID:g914896; PIDN:CAA35695.1; !1PID:g48319 GENETICS !$#genetic_code SGC3 COMPLEX trimer of heterotrimeric subunits consisting of 11K (gamma), !112K (beta), and 62K (alpha) chains FUNCTION !$#description catalyzes the hydrolysis of one molecule of urea to carbon !1dioxide and two molecules of ammonia CLASSIFICATION #superfamily urease, gamma subunit; urease 11K chain !1homology KEYWORDS heterotrimer; hydrolase; metalloprotein FEATURE !$1-100 #domain urease 11K chain homology #label U11 SUMMARY #length 101 #molecular-weight 11242 #checksum 1945 SEQUENCE /// ENTRY B36138 #type complete TITLE urease (EC 3.5.1.5) 12K chain [validated] - Klebsiella pneumoniae ALTERNATE_NAMES urea amidohydrolase; urease beta chain; urease chain B ORGANISM #formal_name Klebsiella pneumoniae DATE 30-Nov-1990 #sequence_revision 02-Dec-1994 #text_change 23-Dec-2002 ACCESSIONS B36138 REFERENCE A36138 !$#authors Mulrooney, S.B.; Hausinger, R.P. !$#journal J. Bacteriol. (1990) 172:5837-5843 !$#title Sequence of the Klebsiella aerogenes urease genes and !1evidence for accessory proteins facilitating nickel !1incorporation. !$#cross-references MUID:91008957; PMID:2211515 !$#accession B36138 !'##molecule_type DNA !'##residues 1-106 ##label MUL !'##cross-references GB:M36068; NID:g149335; PIDN:AAA25150.1; !1PID:g149337 REFERENCE A65977 !$#authors Jabri, E.; Karplus, P.A. !$#submission submitted to the Brookhaven Protein Data Bank, June 1995 !$#cross-references PDB:1KRA !$#contents annotation; X-ray crystallography, 2.3 angstroms, residues !11-101 REFERENCE A56340 !$#authors Jabri, E.; Carr, M.B.; Hausinger, R.P.; Karplus, P.A. !$#journal Science (1995) 268:998-1004 !$#title The crystal structure of urease from Klebsiella aerogenes. !$#cross-references MUID:95273988; PMID:7754395 !$#contents annotation; X-ray crystallography, 2.3 angstroms GENETICS !$#gene ureB COMPLEX trimer of heterotrimeric subunits consisting of 11K (gamma), !112K (beta), and 62K (alpha) chains FUNCTION !$#description catalyzes the hydrolysis of one molecule of urea to carbon !1dioxide and two molecules of ammonia CLASSIFICATION #superfamily urease, beta subunit; urease 12K chain homology KEYWORDS heterotrimer; hydrolase; metalloprotein FEATURE !$3-99 #domain urease 12K chain homology #label U12 SUMMARY #length 106 #molecular-weight 11695 #checksum 6339 SEQUENCE /// ENTRY C43719 #type complete TITLE urease (EC 3.5.1.5) 12K chain - Proteus mirabilis ALTERNATE_NAMES urease beta chain ORGANISM #formal_name Proteus mirabilis DATE 03-Mar-1993 #sequence_revision 02-Dec-1994 #text_change 23-Dec-2002 ACCESSIONS C43719 REFERENCE A43719 !$#authors Jones, B.D.; Mobley, H.L.T. !$#journal J. Bacteriol. (1989) 171:6414-6422 !$#title Proteus mirabilis urease: nucleotide sequence determination !1and comparison with jack bean urease. !$#cross-references MUID:90078080; PMID:2687233 !$#accession C43719 !'##molecule_type DNA !'##residues 1-109 ##label JON !'##cross-references GB:M31834; NID:g150914; PIDN:AAA25668.1; !1PID:g150917 GENETICS !$#gene ureB COMPLEX trimer of heterotrimeric subunits consisting of 11K (gamma), !112K (beta), and 62K (alpha) chains FUNCTION !$#description catalyzes the hydrolysis of one molecule of urea to carbon !1dioxide and two molecules of ammonia CLASSIFICATION #superfamily urease, beta subunit; urease 12K chain homology KEYWORDS heterotrimer; hydrolase; metalloprotein FEATURE !$3-102 #domain urease 12K chain homology #label U12 SUMMARY #length 109 #molecular-weight 12169 #checksum 8612 SEQUENCE /// ENTRY S08479 #type complete TITLE urease (EC 3.5.1.5) 12K chain - Proteus vulgaris ALTERNATE_NAMES urease beta chain ORGANISM #formal_name Proteus vulgaris DATE 29-Jan-1993 #sequence_revision 02-Dec-1994 #text_change 23-Dec-2002 ACCESSIONS S08479 REFERENCE S08478 !$#authors Moersdorf, G.; Kaltwasser, H. !$#journal FEMS Microbiol. Lett. (1991) 66:67-74 !$#title Cloning of the genes encoding urease from Proteus vulgaris !1and sequencing of the structural genes. !$#cross-references MUID:92038908; PMID:1936938 !$#accession S08479 !'##molecule_type DNA !'##residues 1-108 ##label MOE !'##cross-references EMBL:X51816; NID:g45933; PIDN:CAA36114.1; !1PID:g45935 GENETICS !$#gene ureB COMPLEX trimer of heterotrimeric subunits consisting of 11K (gamma), !112K (beta), and 62K (alpha) chains FUNCTION !$#description catalyzes the hydrolysis of one molecule of urea to carbon !1dioxide and two molecules of ammonia CLASSIFICATION #superfamily urease, beta subunit; urease 12K chain homology KEYWORDS heterotrimer; hydrolase; metalloprotein FEATURE !$3-101 #domain urease 12K chain homology #label U12 SUMMARY #length 108 #molecular-weight 12152 #checksum 4916 SEQUENCE /// ENTRY S10031 #type complete TITLE urease (EC 3.5.1.5) 14K chain - Ureaplasma urealyticum ALTERNATE_NAMES urease beta chain ORGANISM #formal_name Ureaplasma urealyticum DATE 31-Dec-1990 #sequence_revision 02-Dec-1994 #text_change 23-Dec-2002 ACCESSIONS S10031; B60335; A60335 REFERENCE S10030 !$#authors Blanchard, A. !$#journal Mol. Microbiol. (1990) 4:669-676 !$#title Ureaplasma urealyticum urease genes; use of a UGA tryptophan !1codon. !$#cross-references MUID:90279510; PMID:2191184 !$#accession S10031 !'##molecule_type DNA !'##residues 1-121 ##label BLA !'##cross-references EMBL:X51315; NID:g914896; PIDN:CAA35696.1; !1PID:g48320 REFERENCE A60335 !$#authors Willoughby, J.J.; Russell, W.C.; Thirkell, D.; Burdon, M.G. !$#journal Infect. Immun. (1991) 59:2463-2469 !$#title Isolation and detection of urease genes in Ureaplasma !1urealyticum. !$#cross-references MUID:91267627; PMID:2050410 !$#accession B60335 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1,'SGS',9-121 ##label WIL !'##cross-references GB:M36190 !'##note the authors translated the codon TTC for residue 20 as Pro !$#accession A60335 !'##molecule_type protein !'##residues 'XGS',9-36 ##label WI2 GENETICS !$#genetic_code SGC3 COMPLEX trimer of heterotrimeric subunits consisting of 11K (gamma), !112K (beta), and 62K (alpha) chains FUNCTION !$#description catalyzes the hydrolysis of one molecule of urea to carbon !1dioxide and two molecules of ammonia CLASSIFICATION #superfamily urease, beta subunit; urease 12K chain homology KEYWORDS heterotrimer; hydrolase; metalloprotein FEATURE !$13-121 #domain urease 12K chain homology #label U12 SUMMARY #length 121 #molecular-weight 13585 #checksum 3683 SEQUENCE /// ENTRY S42604 #type complete TITLE urease (EC 3.5.1.5) 12K chain - Rhizobium meliloti ALTERNATE_NAMES urease beta chain; urease chain B ORGANISM #formal_name Rhizobium meliloti DATE 25-Dec-1994 #sequence_revision 10-May-1996 #text_change 23-Dec-2002 ACCESSIONS S42604 REFERENCE S42601 !$#authors Miksch, G.; Arnold, W.; Lentzsch, P.; Priefer, U.B.; !1Puehler, A. !$#journal Mol. Gen. Genet. (1994) 242:539-550 !$#title A 4.6 kb DNA region of Rhizobium meliloti involved in !1determining urease and hydrogenase activities carries the !1structural genes for urease (ureaA, ureB, ureC) interrupted !1by other open reading frames. !$#cross-references MUID:94166766; PMID:8121412 !$#accession S42604 !'##status preliminary !'##molecule_type DNA !'##residues 1-101 ##label MIK !'##cross-references GB:S69145; NID:g545795; PIDN:AAB30136.1; !1PID:g545799 GENETICS !$#gene ureB COMPLEX heterodecamer; dimer of pentamers; each pentamer contains !1one alpha (62K) chain, two beta (12K) chains, and two gamma !1(11K) chains CLASSIFICATION #superfamily urease, beta subunit; urease 12K chain homology KEYWORDS heterodecamer; hydrolase FEATURE !$3-99 #domain urease 12K chain homology #label U12 SUMMARY #length 101 #molecular-weight 10886 #checksum 139 SEQUENCE /// ENTRY B36950 #type complete TITLE urease (EC 3.5.1.5) 12k chain - Bacillus sp. (strain TB-90) ALTERNATE_NAMES ureB protein ORGANISM #formal_name Bacillus sp. DATE 07-Jul-1995 #sequence_revision 10-May-1996 #text_change 23-Dec-2002 ACCESSIONS B36950 REFERENCE A36950 !$#authors Maeda, M.; Hidaka, M.; Nakamura, A.; Masaki, H.; Uozumi, T. !$#journal J. Bacteriol. (1994) 176:432-442 !$#title Cloning, sequencing, and expression of thermophilic Bacillus !1sp. strain TB-90 urease gene complex in Escherichia coli. !$#cross-references MUID:94117379; PMID:8288539 !$#accession B36950 !'##status preliminary !'##molecule_type DNA !'##residues 1-107 ##label MAE !'##cross-references GB:D14439; NID:g393296; PIDN:BAA03324.1; !1PID:g216361 CLASSIFICATION #superfamily urease, beta subunit; urease 12K chain homology KEYWORDS hydrolase FEATURE !$3-99 #domain urease 12K chain homology #label U12 SUMMARY #length 107 #molecular-weight 12183 #checksum 3507 SEQUENCE /// ENTRY I64075 #type complete TITLE urease (EC 3.5.1.5) 12K chain - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES urease beta chain; urease chain B ORGANISM #formal_name Haemophilus influenzae DATE 18-Aug-1995 #sequence_revision 10-May-1996 #text_change 23-Dec-2002 ACCESSIONS I64075 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession I64075 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-101 ##label TIGR !'##cross-references GB:U32736; GB:L42023; NID:g1573519; !1PIDN:AAC22198.1; PID:g1573525; TIGR:HI0540 !'##note named as homolog to a protein from Escherichia coli GENETICS !$#gene ureB CLASSIFICATION #superfamily urease, beta subunit; urease 12K chain homology KEYWORDS hydrolase FEATURE !$3-99 #domain urease 12K chain homology #label U12 SUMMARY #length 101 #molecular-weight 11161 #checksum 283 SEQUENCE /// ENTRY S31418 #type complete TITLE urease (EC 3.5.1.5) yeuB - Yersinia enterocolitica ORGANISM #formal_name Yersinia enterocolitica DATE 03-Mar-1994 #sequence_revision 10-May-1996 #text_change 23-Dec-2002 ACCESSIONS S31418; S36027 REFERENCE S31417 !$#authors Skurnik, M.; Batsford, S.; Mertz, A.; Schiltz, E.; Toivanen, !1P. !$#submission submitted to the EMBL Data Library, December 1992 !$#description The putative arthritogenic cationic 19 kD antigen of !1Yersinia enterocolitica is a urease beta-subunit. !$#accession S31418 !'##status preliminary !'##molecule_type DNA !'##residues 1-164 ##label SKU !'##cross-references EMBL:Z18865 REFERENCE S36026 !$#authors Skurnik, M. !$#submission submitted to the EMBL Data Library, December 1992 !$#accession S36027 !'##status preliminary !'##molecule_type DNA !'##residues 1-30,'S',32-164 ##label SK2 !'##cross-references EMBL:Z18865; NID:g1016360; PIDN:CAA79315.1; !1PID:g296318 GENETICS !$#gene yeuB CLASSIFICATION #superfamily urease, beta subunit; urease 12K chain homology KEYWORDS hydrolase FEATURE !$37-133 #domain urease 12K chain homology #label U12 SUMMARY #length 164 #molecular-weight 17927 #checksum 7066 SEQUENCE /// ENTRY S38484 #type complete TITLE urease (EC 3.5.1.5) beta chain - Staphylococcus xylosus ORGANISM #formal_name Staphylococcus xylosus DATE 22-Jan-1994 #sequence_revision 10-May-1996 #text_change 23-Dec-2002 ACCESSIONS S38484 REFERENCE S38483 !$#authors Jose, J.; Schaefer, U.K.; Kaltwasser, H. !$#submission submitted to the EMBL Data Library, August 1993 !$#description Threonine is present instead of Cysteine at the active site !1of urease from S.xylosus. !$#accession S38484 !'##status preliminary !'##molecule_type DNA !'##residues 1-137 ##label JOS !'##cross-references EMBL:X74600; NID:g410513; PIDN:CAA52679.1; !1PID:g410515 CLASSIFICATION #superfamily urease, beta subunit; urease 12K chain homology KEYWORDS hydrolase FEATURE !$3-99 #domain urease 12K chain homology #label U12 SUMMARY #length 137 #molecular-weight 15432 #checksum 8943 SEQUENCE /// ENTRY URKCAP #type complete TITLE urease (EC 3.5.1.5) 26K chain - Helicobacter pylori (strains 26695 and others) ALTERNATE_NAMES urea amidohydrolase; urease alpha chain ORGANISM #formal_name Helicobacter pylori DATE 30-Sep-1991 #sequence_revision 15-Aug-1997 #text_change 05-Jan-2003 ACCESSIONS A38537; A64529; S07884; B35306; A41502; A61371; E49215 REFERENCE A38537 !$#authors Labigne, A.; Cussac, V.; Courcoux, P. !$#journal J. Bacteriol. (1991) 173:1920-1931 !$#title Shuttle cloning and nucleotide sequences of Helicobacter !1pylori genes responsible for urease activity. !$#cross-references MUID:91161505; PMID:2001995 !$#accession A38537 !'##molecule_type DNA !'##residues 1-238 ##label LAB !'##cross-references GB:M60398; NID:g149007; PIDN:AAA25020.1; !1PID:g149010; GB:X57132 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession A64529 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-238 ##label TOM !'##cross-references GB:AE000529; GB:AE000511; NID:g2313152; !1PIDN:AAD07144.1; PID:g2313154; TIGR:HP0073 !'##experimental_source strain 26695 REFERENCE S07884 !$#authors Clayton, C.L.; Pallen, M.J.; Kleanthous, H.; Wren, B.W.; !1Tabaqchali, S. !$#journal Nucleic Acids Res. (1990) 18:362 !$#title Nucleotide sequence of two genes from Helicobacter pylori !1encoding for urease subunits. !$#cross-references MUID:90221820; PMID:2326167 !$#accession S07884 !'##molecule_type DNA !'##residues 1-36,'R',38-48,'R',50-131,'PP',134-238 ##label CLA !'##cross-references EMBL:X17079; NID:g43633; PIDN:CAA34932.1; !1PID:g43634 REFERENCE A35306 !$#authors Dunn, B.E.; Campbell, G.P.; Perez-Perez, G.I.; Blaser, M.J. !$#journal J. Biol. Chem. (1990) 265:9464-9469 !$#title Purification and characterization of urease from !1Helicobacter pylori. !$#cross-references MUID:90264448; PMID:2188975 !$#accession B35306 !'##molecule_type protein !'##residues 1-20 ##label DUN REFERENCE A41502 !$#authors Hu, L.T.; Mobley, H.L.T. !$#journal Infect. Immun. (1990) 58:992-998 !$#title Purification and N-terminal analysis of urease from !1Helicobacter pylori. !$#cross-references MUID:90202165; PMID:2318539 !$#accession A41502 !'##molecule_type protein !'##residues 1-13,'S',15-20 ##label HUA !'##experimental_source strain UMAB41 REFERENCE A61371 !$#authors Evans Jr., D.J.; Evans, D.G.; Kirkpatrick, S.S.; Graham, !1D.Y. !$#journal Microb. Pathog. (1991) 10:15-26 !$#title Characterization of the Helicobacter pylori urease and !1purification of its subunits. !$#cross-references MUID:91312104; PMID:1857197 !$#accession A61371 !'##molecule_type protein !'##residues 1-5,'R',7-20,'R',22-30 ##label EVA REFERENCE A49215 !$#authors Turbett, G.R.; Hoj, P.B.; Horne, R.; Mee, B.J. !$#journal Infect. Immun. (1992) 60:5259-5266 !$#title Purification and characterization of the urease enzymes of !1Helicobacter species from humans and animals. !$#cross-references MUID:93084378; PMID:1452359 !$#accession E49215 !'##status preliminary !'##molecule_type protein !'##residues 1-12 ##label TUR !'##cross-references PIDN:AAB24359.1; PID:g260968 !'##experimental_source strain NCTC 11637 !'##note sequence extracted from NCBI backbone (NCBIP:119486) GENETICS !$#gene ureA; HP0073 COMPLEX heterodimer of 26K chain and 62K chain (see PIR:URKCBP) FUNCTION !$#description catalyzes the hydrolysis of one molecule of urea to carbon !1dioxide and two molecules of ammonia CLASSIFICATION #superfamily urease, fused gamma/beta subunit; urease 11K !1chain homology; urease 12K chain homology KEYWORDS heterodimer; hydrolase; metalloprotein FEATURE !$1-238 #product urease 26K chain #status experimental #label !8MAT\ !$1-101 #domain urease 11K chain homology #label U11\ !$108-204 #domain urease 12K chain homology #label U12 SUMMARY #length 238 #molecular-weight 26539 #checksum 5801 SEQUENCE /// ENTRY S35290 #type complete TITLE urease (EC 3.5.1.5) 26K chain - Helicobacter felis ALTERNATE_NAMES urease alpha chain ORGANISM #formal_name Helicobacter felis DATE 31-Dec-1993 #sequence_revision 02-Dec-1994 #text_change 05-Jan-2003 ACCESSIONS S35290 REFERENCE S35290 !$#authors Ferrero, R.L.; Labigne, A. !$#journal Mol. Microbiol. (1993) 9:323-333 !$#title Cloning, expression and sequencing of Helicobacter felis !1urease genes. !$#cross-references MUID:94018627; PMID:8412683 !$#accession S35290 !'##molecule_type DNA !'##residues 1-237 ##label FER !'##cross-references EMBL:X69080; NID:g396160; PIDN:CAA48825.1; !1PID:g396161 GENETICS !$#gene ureA COMPLEX heterodimer FUNCTION !$#description catalyzes the hydrolysis of one molecule of urea to carbon !1dioxide and two molecules of ammonia CLASSIFICATION #superfamily urease, fused gamma/beta subunit; urease 11K !1chain homology; urease 12K chain homology KEYWORDS heterodimer; hydrolase; metalloprotein FEATURE !$1-101 #domain urease 11K chain homology #label U11\ !$108-204 #domain urease 12K chain homology #label U12 SUMMARY #length 237 #molecular-weight 26091 #checksum 8023 SEQUENCE /// ENTRY URKCBP #type complete TITLE urease (EC 3.5.1.5) 62K chain - Helicobacter pylori (strains 26695, J99, and others) ALTERNATE_NAMES urease beta chain; urease chain B; urease large subunit ORGANISM #formal_name Helicobacter pylori DATE 30-Sep-1991 #sequence_revision 02-Dec-1994 #text_change 05-Jan-2003 ACCESSIONS B38537; H64528; A71977; F41834; S07885; S12487; A49215; !1B61371; A35306; B41502 REFERENCE A38537 !$#authors Labigne, A.; Cussac, V.; Courcoux, P. !$#journal J. Bacteriol. (1991) 173:1920-1931 !$#title Shuttle cloning and nucleotide sequences of Helicobacter !1pylori genes responsible for urease activity. !$#cross-references MUID:91161505; PMID:2001995 !$#accession B38537 !'##molecule_type DNA !'##residues 1-569 ##label LAB !'##cross-references GB:M60398; NID:g149007; PIDN:AAA25021.1; !1PID:g149011; GB:X57132 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession H64528 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-569 ##label TOM !'##cross-references GB:AE000529; GB:AE000511; NID:g2313152; !1PIDN:AAD07143.1; PID:g2313153; TIGR:HP0072 !'##experimental_source strain 26695 REFERENCE A71800 !$#authors Alm, R.A.; Ling, L.S.L.; Moir, D.T.; King, B.L.; Brown, !1E.D.; Doig, P.C.; Smith, D.R.; Noonan, B.; Guild, B.C.; !1deJonge, B.L.; Carmel, G.; Tummino, P.J.; Caruso, A.; !1Uria-Nickelsen, M.; Mills, D.M.; Ives, C.; Gibson, R.; !1Merberg, D.; Mills, S.D.; Jiang, Q.; Taylor, D.E.; Vovis, !1G.F.; Trust, T.J. !$#journal Nature (1999) 397:176-180 !$#title Genomic sequence comparison of two unrelated isolates of the !1human gastric pathogen Helicobacter pylori. !$#cross-references MUID:99120557; PMID:9923682 !$#accession A71977 !'##molecule_type DNA !'##residues 1-569 ##label ARN !'##cross-references GB:AE001446; GB:AE001439; NID:g4154573; !1PIDN:AAD05651.1; PID:g4154576 !'##experimental_source strain J99 REFERENCE A41834 !$#authors Cussac, V.; Ferrero, R.L.; Labigne, A. !$#journal J. Bacteriol. (1992) 174:2466-2473 !$#title Expression of Helicobacter pylori urease genes in !1Escherichia coli grown under nitrogen-limiting conditions. !$#cross-references MUID:92210488; PMID:1313413 !$#accession F41834 !'##status preliminary !'##molecule_type DNA !'##residues 565-569 ##label CUS !'##cross-references GB:M84338 REFERENCE S07884 !$#authors Clayton, C.L.; Pallen, M.J.; Kleanthous, H.; Wren, B.W.; !1Tabaqchali, S. !$#journal Nucleic Acids Res. (1990) 18:362 !$#title Nucleotide sequence of two genes from Helicobacter pylori !1encoding for urease subunits. !$#cross-references MUID:90221820; PMID:2326167 !$#accession S07885 !'##molecule_type DNA !'##residues 1-9,'A',11-18,'A',20-103,'T',105-180,'F',182-192,'F', !1194-217,'L',219-272,'Y',274-539,'S',541-553,'LNQPIK' ##label !1CLA !'##cross-references EMBL:X17079 REFERENCE S12487 !$#authors Clayton, C.L. !$#submission submitted to the EMBL Data Library, October 1989 !$#accession S12487 !'##molecule_type DNA !'##residues 1-9,'A',11-103,'T',105-180,'F',182-192,'F',194-217,'L', !1219-272,'Y',274-539,'S',541-553,'LNQPIK' ##label CL2 !'##cross-references EMBL:X17079; NID:g43633; PIDN:CAA34933.1; !1PID:g43635 REFERENCE A49215 !$#authors Turbett, G.R.; Hoj, P.B.; Horne, R.; Mee, B.J. !$#journal Infect. Immun. (1992) 60:5259-5266 !$#title Purification and characterization of the urease enzymes of !1Helicobacter species from humans and animals. !$#cross-references MUID:93084378; PMID:1452359 !$#accession A49215 !'##status preliminary !'##molecule_type protein !'##residues 1-12 ##label TUR !'##cross-references PIDN:AAB24355.1; PID:g260964 !'##experimental_source strain NCTC 11637 !'##note sequence extracted from NCBI backbone (NCBIP:119482) REFERENCE A61371 !$#authors Evans Jr., D.J.; Evans, D.G.; Kirkpatrick, S.S.; Graham, !1D.Y. !$#journal Microb. Pathog. (1991) 10:15-26 !$#title Characterization of the Helicobacter pylori urease and !1purification of its subunits. !$#cross-references MUID:91312104; PMID:1857197 !$#accession B61371 !'##molecule_type protein !'##residues 1-21,'C',23-26,'C',28,'I',30 ##label EVA REFERENCE A35306 !$#authors Dunn, B.E.; Campbell, G.P.; Perez-Perez, G.I.; Blaser, M.J. !$#journal J. Biol. Chem. (1990) 265:9464-9469 !$#title Purification and characterization of urease from !1Helicobacter pylori. !$#cross-references MUID:90264448; PMID:2188975 !$#accession A35306 !'##molecule_type protein !'##residues 1-20 ##label DUN REFERENCE A41502 !$#authors Hu, L.T.; Mobley, H.L.T. !$#journal Infect. Immun. (1990) 58:992-998 !$#title Purification and N-terminal analysis of urease from !1Helicobacter pylori. !$#cross-references MUID:90202165; PMID:2318539 !$#accession B41502 !'##molecule_type protein !'##residues 1-5,'A',7-15 ##label HUA GENETICS !$#gene ureB; HP0072 COMPLEX heterodimer of 26K chain (see PIR:URKCAP) and 62K chain FUNCTION !$#description catalyzes the hydrolysis of one molecule of urea to carbon !1dioxide and two molecules of ammonia CLASSIFICATION #superfamily urease, alpha subunit; urease 62K chain !1homology KEYWORDS heterodimer; hydrolase; metalloprotein; nickel FEATURE !$4-552 #domain urease 62K chain homology #label U62\ !$136,138,219,362 #binding_site nickel 2 (His, His, Lys, Asp) #status !8predicted\ !$219,248,274 #binding_site nickel 1 (Lys, His, His) #status !8predicted\ !$219 #binding_site carbon dioxide (Lys) (covalent) (by !8urease activase) #status predicted\ !$221,322 #active_site His #status predicted SUMMARY #length 569 #molecular-weight 61683 #checksum 8247 SEQUENCE /// ENTRY S35291 #type complete TITLE urease (EC 3.5.1.5) 62K chain - Helicobacter felis ALTERNATE_NAMES urease beta chain ORGANISM #formal_name Helicobacter felis DATE 31-Dec-1993 #sequence_revision 02-Dec-1994 #text_change 05-Jan-2003 ACCESSIONS S35291 REFERENCE S35290 !$#authors Ferrero, R.L.; Labigne, A. !$#journal Mol. Microbiol. (1993) 9:323-333 !$#title Cloning, expression and sequencing of Helicobacter felis !1urease genes. !$#cross-references MUID:94018627; PMID:8412683 !$#accession S35291 !'##molecule_type DNA !'##residues 1-569 ##label FER !'##cross-references EMBL:X69080; NID:g396160; PIDN:CAA48826.1; !1PID:g396162 GENETICS !$#gene ureB COMPLEX heterodimer FUNCTION !$#description catalyzes the hydrolysis of one molecule of urea to carbon !1dioxide and two molecules of ammonia CLASSIFICATION #superfamily urease, alpha subunit; urease 62K chain !1homology KEYWORDS heterodimer; hydrolase; metalloprotein; nickel FEATURE !$1-569 #product urease 62K chain #status experimental #label !8MAT\ !$4-552 #domain urease 62K chain homology #label U62\ !$136,138,219,362 #binding_site nickel 2 (His, His, Lys, Asp) #status !8predicted\ !$219,248,274 #binding_site nickel 1 (Lys, His, His) #status !8predicted\ !$219 #binding_site carbon dioxide (Lys) (covalent) (by !8urease activase) #status predicted\ !$221,322 #active_site His #status predicted SUMMARY #length 569 #molecular-weight 61702 #checksum 5120 SEQUENCE /// ENTRY D43719 #type complete TITLE urease (EC 3.5.1.5) 62K chain - Proteus mirabilis ALTERNATE_NAMES urease alpha chain ORGANISM #formal_name Proteus mirabilis DATE 03-Mar-1993 #sequence_revision 02-Dec-1994 #text_change 05-Jan-2003 ACCESSIONS D43719 REFERENCE A43719 !$#authors Jones, B.D.; Mobley, H.L.T. !$#journal J. Bacteriol. (1989) 171:6414-6422 !$#title Proteus mirabilis urease: nucleotide sequence determination !1and comparison with jack bean urease. !$#cross-references MUID:90078080; PMID:2687233 !$#accession D43719 !'##molecule_type DNA !'##residues 1-567 ##label JON !'##cross-references GB:M31834; NID:g150914; PIDN:AAA25669.1; !1PID:g150918 GENETICS !$#gene ureC COMPLEX trimer of heterotrimeric subunits consisting of 11K (gamma), !112K (beta), and 62K (alpha) chains FUNCTION !$#description catalyzes the hydrolysis of one molecule of urea to carbon !1dioxide and two molecules of ammonia CLASSIFICATION #superfamily urease, alpha subunit; urease 62K chain !1homology KEYWORDS heterotrimer; hydrolase; metalloprotein; nickel FEATURE !$4-550 #domain urease 62K chain homology #label U62\ !$134,136,217,360 #binding_site nickel 2 (His, His, Lys, Asp) #status !8predicted\ !$217,246,272 #binding_site nickel 1 (Lys, His, His) #status !8predicted\ !$217 #binding_site carbon dioxide (Lys) (covalent) (by !8urease activase) #status predicted\ !$219,320 #active_site His #status predicted SUMMARY #length 567 #molecular-weight 61012 #checksum 3229 SEQUENCE /// ENTRY S08480 #type complete TITLE urease (EC 3.5.1.5) 62K chain - Proteus vulgaris ALTERNATE_NAMES urease alpha chain ORGANISM #formal_name Proteus vulgaris DATE 29-Jan-1993 #sequence_revision 02-Dec-1994 #text_change 05-Jan-2003 ACCESSIONS S08480 REFERENCE S08478 !$#authors Moersdorf, G.; Kaltwasser, H. !$#journal FEMS Microbiol. Lett. (1991) 66:67-74 !$#title Cloning of the genes encoding urease from Proteus vulgaris !1and sequencing of the structural genes. !$#cross-references MUID:92038908; PMID:1936938 !$#accession S08480 !'##molecule_type DNA !'##residues 1-567 ##label MOE !'##cross-references EMBL:X51816; NID:g45933; PIDN:CAA36115.1; !1PID:g45936 GENETICS !$#gene ureC COMPLEX trimer of heterotrimeric subunits consisting of 11K (gamma), !112K (beta), and 62K (alpha) chains FUNCTION !$#description catalyzes the hydrolysis of one molecule of urea to carbon !1dioxide and two molecules of ammonia CLASSIFICATION #superfamily urease, alpha subunit; urease 62K chain !1homology KEYWORDS heterotrimer; hydrolase; metalloprotein; nickel FEATURE !$4-550 #domain urease 62K chain homology #label U62\ !$134,136,217,360 #binding_site nickel 2 (His, His, Lys, Asp) #status !8predicted\ !$217,246,272 #binding_site nickel 1 (Lys, His, His) #status !8predicted\ !$217 #binding_site carbon dioxide (Lys) (covalent) (by !8urease activase) #status predicted\ !$219,320 #active_site His #status predicted SUMMARY #length 567 #molecular-weight 60934 #checksum 1397 SEQUENCE /// ENTRY C36138 #type complete TITLE urease (EC 3.5.1.5) 62K chain [validated] - Klebsiella pneumoniae ALTERNATE_NAMES urea amidohydrolase; urease alpha chain; urease chain C ORGANISM #formal_name Klebsiella pneumoniae DATE 30-Nov-1990 #sequence_revision 02-Dec-1994 #text_change 05-Jan-2003 ACCESSIONS C36138 REFERENCE A36138 !$#authors Mulrooney, S.B.; Hausinger, R.P. !$#journal J. Bacteriol. (1990) 172:5837-5843 !$#title Sequence of the Klebsiella aerogenes urease genes and !1evidence for accessory proteins facilitating nickel !1incorporation. !$#cross-references MUID:91008957; PMID:2211515 !$#accession C36138 !'##molecule_type DNA !'##residues 1-567 ##label MUL !'##cross-references GB:M36068; NID:g149335; PIDN:AAA25151.1; !1PID:g149338 REFERENCE A65977 !$#authors Jabri, E.; Karplus, P.A. !$#submission submitted to the Brookhaven Protein Data Bank, June 1995 !$#cross-references PDB:1KRA !$#contents annotation; X-ray crystallography, 2.3 angstroms, residues !12-567 REFERENCE A56340 !$#authors Jabri, E.; Carr, M.B.; Hausinger, R.P.; Karplus, P.A. !$#journal Science (1995) 268:998-1004 !$#title The crystal structure of urease from Klebsiella aerogenes. !$#cross-references MUID:95273988; PMID:7754395 !$#contents annotation; X-ray crystallography, 2.3 angstroms REFERENCE A58580 !$#authors Jabri, E.; Karplus, P.A. !$#journal Biochemistry (1996) 35:10616-10626 !$#title Structures of the Klebsiella aerogenes urease apoenzyme and !1two active-site mutants. !$#cross-references MUID:96346054; PMID:8718850 !$#contents annotation; X-ray crystallography, 2.3 angstroms; active !1site mutagenesis GENETICS !$#gene ureC COMPLEX trimer of heterotrimeric subunits consisting of 11K (gamma), !112K (beta), and 62K (alpha) chains FUNCTION !$#description catalyzes the hydrolysis of one molecule of urea to carbon !1dioxide and two molecules of ammonia CLASSIFICATION #superfamily urease, alpha subunit; urease 62K chain !1homology KEYWORDS heterotrimer; hydrolase; metalloprotein; nickel FEATURE !$2-567 #product urease 62K chain #status experimental #label !8MAT\ !$4-550 #domain urease 62K chain homology #label U62\ !$134,136,217,360 #binding_site nickel 2 (His, His, Lys, Asp) #status !8experimental\ !$217,246,272 #binding_site nickel 1 (Lys, His, His) #status !8experimental\ !$217 #binding_site carbon dioxide (Lys) (covalent) (by !8urease activase) #status experimental\ !$219,320 #active_site His #status experimental SUMMARY #length 567 #molecular-weight 60304 #checksum 8296 SEQUENCE /// ENTRY S10032 #type complete TITLE urease (EC 3.5.1.5) 72K chain - Ureaplasma urealyticum ALTERNATE_NAMES urease alpha chain ORGANISM #formal_name Ureaplasma urealyticum DATE 31-Dec-1990 #sequence_revision 02-Dec-1994 #text_change 05-Jan-2003 ACCESSIONS S10032; D60335; C60335 REFERENCE S10030 !$#authors Blanchard, A. !$#journal Mol. Microbiol. (1990) 4:669-676 !$#title Ureaplasma urealyticum urease genes; use of a UGA tryptophan !1codon. !$#cross-references MUID:90279510; PMID:2191184 !$#accession S10032 !'##molecule_type DNA !'##residues 1-614 ##label BLA !'##cross-references EMBL:X51315 REFERENCE A60335 !$#authors Willoughby, J.J.; Russell, W.C.; Thirkell, D.; Burdon, M.G. !$#journal Infect. Immun. (1991) 59:2463-2469 !$#title Isolation and detection of urease genes in Ureaplasma !1urealyticum. !$#cross-references MUID:91267627; PMID:2050410 !$#accession D60335 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-41 ##label WIL !'##cross-references GB:M36190; NID:g155145; PIDN:AAA79777.1; !1PID:g1030757 !$#accession C60335 !'##molecule_type protein !'##residues 1-28,'E',30,'I',32-36 ##label WI2 GENETICS !$#genetic_code SGC3 COMPLEX trimer of heterotrimeric subunits consisting of 11K (gamma), !112K (beta), and 62K (alpha) chains FUNCTION !$#description catalyzes the hydrolysis of one molecule of urea to carbon !1dioxide and two molecules of ammonia CLASSIFICATION #superfamily urease, alpha subunit; urease 62K chain !1homology KEYWORDS heterotrimer; hydrolase; metalloprotein; nickel FEATURE !$4-556 #domain urease 62K chain homology #label U62\ !$142,144,223,366 #binding_site nickel 2 (His, His, Lys, Asp) #status !8predicted\ !$223,252 #binding_site nickel 1 (Lys, His) #status predicted\ !$223 #binding_site carbon dioxide (Lys) (covalent) (by !8urease activase) #status predicted\ !$225,326 #active_site His #status predicted SUMMARY #length 614 #molecular-weight 66679 #checksum 6846 SEQUENCE /// ENTRY PNECA #type complete TITLE penicillin amidase (EC 3.5.1.11) precursor - Escherichia coli ALTERNATE_NAMES penicillin G acylase; penicillin G amidohydrolase ORGANISM #formal_name Escherichia coli DATE 30-Sep-1987 #sequence_revision 26-Jan-1996 #text_change 18-Jun-1999 ACCESSIONS A23593; S23375; A23983; I54005; S15375; I56367; I73437 REFERENCE A23593 !$#authors Schumacher, G.; Sizmann, D.; Haug, H.; Buckel, P.; Bock, A. !$#journal Nucleic Acids Res. (1986) 14:5713-5727 !$#title Penicillin acylase from E. coli: unique gene-protein !1relation. !$#cross-references MUID:86286584; PMID:3016663 !$#accession A23593 !'##molecule_type DNA !'##residues 1-846 ##label SCH !'##cross-references GB:X04114; NID:g42247; PIDN:CAA27728.1; PID:g42248 REFERENCE S23375 !$#authors Oh, S.J.; Kim, Y.C.; Park, Y.W.; Min, S.Y.; Kim, I.S.; Kang, !1H.S. !$#journal Gene (1987) 56:87-97 !$#title Complete nucleotide sequence of the penicillin G acylase !1gene and the flanking regions, and its expression in !1Escherichia coli. !$#cross-references MUID:88056318; PMID:3315861 !$#accession S23375 !'##molecule_type DNA !'##residues 1-129,'T',131-271,'A',273-631,'P',633-846 ##label OHS !'##cross-references EMBL:M17609; NID:g147161; PIDN:AAA24324.1; !1PID:g147162 REFERENCE A23983 !$#authors Oliver, G.; Valle, F.; Rosetti, F.; Gomez-Pedrozo, M.; !1Santamaria, P.; Gosset, G.; Bolivar, F. !$#journal Gene (1985) 40:9-14 !$#title A common precursor for the two subunits of the penicillin !1acylase from Escherichia coli ATCC11105. !$#cross-references MUID:86137424; PMID:3005131 !$#accession A23983 !'##molecule_type DNA !'##residues 1-102,'R',104-271,'A',273-304,'R',306-368 ##label OLI !'##experimental_source ATCC 11105 REFERENCE I54005 !$#authors Valle, F.; Gosset, G.; Tenorio, B.; Oliver, G.; Bolivar, F. !$#journal Gene (1986) 50:119-122 !$#title Characterization of the regulatory region of the Escherichia !1coli penicillin acylase structural gene. !$#cross-references MUID:87219870; PMID:3556321 !$#accession I54005 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-20 ##label RES !'##cross-references GB:M15950; NID:g147062; PIDN:AAA24269.1; !1PID:g147063 REFERENCE S15375 !$#authors Slade, A.; Horrocks, A.J.; Lindsay, C.D.; Dunbar, B.; !1Virden, R. !$#journal Eur. J. Biochem. (1991) 197:75-80 !$#title Site-directed chemical conversion of serine to cysteine in !1penicillin acylase from Escherichia coli ATCC 11105. Effect !1on conformation and catalytic activity. !$#cross-references MUID:91200064; PMID:1849824 !$#accession S15375 !'##molecule_type protein !'##residues 27-36;291-299 ##label SLA REFERENCE I56367 !$#authors Bruns, W.; Hoppe, J.; Tsai, H.; Bruening, H.J.; Maywald, F.; !1Collins, J.; Mayer, H. !$#journal J. Mol. Appl. Genet. (1985) 3:36-44 !$#title Structure of the penicillin acylase gene from Escherichia !1coli: A periplasmic enzyme that undergoes multiple !1proteolytic processing. !$#cross-references MUID:85236066; PMID:2989404 !$#accession I56367 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-67,'R',69-76,'R',78-96,'S',98-129,'T',131-216,'G', !1218-341,'L',343,'WF',376-378,'MV' ##label RE2 !'##cross-references GB:M11672; NID:g147044; PIDN:AAA24258.1; !1PID:g147047 !$#accession I73437 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 741-788,'Q',790-846 ##label RE3 !'##cross-references GB:M12373; NID:g147045; PIDN:AAA24259.1; !1PID:g147048 GENETICS !$#gene pac; pga FUNCTION !$#description hydrolyzes penicillins G and V into fatty acid and !16-aminopenicillanic acid (6-APA) CLASSIFICATION #superfamily penicillin amidase KEYWORDS antibiotic resistance; hydrolase; penicillin resistance FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-846 #product penicillin amidase zymogen #status predicted !8#label PRO\ !$290-846 #product penicillin amidase heavy chain #status !8predicted #label MPT SUMMARY #length 846 #molecular-weight 94670 #checksum 3062 SEQUENCE /// ENTRY A26528 #type complete TITLE penicillin amidase (EC 3.5.1.11) - Kluyvera cryocrescens ALTERNATE_NAMES penicillin acylase; penicillin amidohydrolase ORGANISM #formal_name Kluyvera cryocrescens DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A26528 REFERENCE A26528 !$#authors Barbero, J.L.; Buesa, J.M.; Gonzalez de Buitrago, G.; !1Mendez, E.; Perez-Aranda, A.; Garcia, J.L. !$#journal Gene (1986) 49:69-80 !$#title Complete nucleotide sequence of the penicillin acylase gene !1from Kluyvera citrophila. !$#cross-references MUID:87192002; PMID:3032748 !$#accession A26528 !'##molecule_type mRNA !'##residues 1-844 ##label BAR !'##cross-references GB:M15418 !'##experimental_source ATCC 21285 !'##note the authors translated the codon CAG for residue 719 as Glu !'##note the source is designated as Kluyvera citrophila GENETICS !$#gene pac CLASSIFICATION #superfamily penicillin amidase KEYWORDS antibiotic resistance; hydrolase; penicillin resistance SUMMARY #length 844 #molecular-weight 93573 #checksum 6611 SEQUENCE /// ENTRY A56681 #type complete TITLE penicillin amidase (EC 3.5.1.11) precursor - Providencia rettgeri ALTERNATE_NAMES penicillin G amidase ORGANISM #formal_name Providencia rettgeri DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A56681 REFERENCE A56681 !$#authors Ljubijankic, G.; Konstantinovic, M.; Glisin, V. !$#journal DNA Seq. (1992) 3:195-200 !$#title The primary structure of Providencia rettgeri penicillin G !1amidase gene and its relationship to other gram negative !1amidases. !$#cross-references MUID:93113002; PMID:1472713 !$#accession A56681 !'##status preliminary !'##molecule_type DNA !'##residues 1-837 ##label LJU !'##cross-references GB:M86533 CLASSIFICATION #superfamily penicillin amidase KEYWORDS hydrolase SUMMARY #length 837 #molecular-weight 94373 #checksum 6460 SEQUENCE /// ENTRY A48953 #type complete TITLE choloylglycine hydrolase (EC 3.5.1.24) - Lactobacillus plantarum ALTERNATE_NAMES conjugated bile acid hydrolase ORGANISM #formal_name Lactobacillus plantarum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A48953 REFERENCE A48953 !$#authors Christiaens, H.; Leer, R.J.; Pouwels, P.H.; Verstraete, W. !$#journal Appl. Environ. Microbiol. (1992) 58:3792-3798 !$#title Cloning and expression of a conjugated bile acid hydrolase !1gene from Lactobacillus plantarum by using a direct plate !1assay. !$#cross-references MUID:93119131; PMID:1476424 !$#contents 80 !$#accession A48953 !'##status preliminary !'##molecule_type DNA !'##residues 1-324 ##label CHR !'##cross-references GB:S51638; NID:g262675; PIDN:AAB24746.1; !1PID:g262676 !'##note sequence extracted from NCBI backbone (NCBIN:121574, !1NCBIP:121575) CLASSIFICATION #superfamily choloylglycine hydrolase KEYWORDS hydrolase SUMMARY #length 324 #molecular-weight 37078 #checksum 6134 SEQUENCE /// ENTRY MUHUGD #type complete TITLE N4-(beta-N-acetylglucosaminyl)-L-asparaginase (EC 3.5.1.26) precursor [validated] - human ALTERNATE_NAMES aspartylglucosaminidase; glycosylasparaginase CONTAINS N4-(beta-N-acetylglucosaminyl)-L-asparaginase alpha chain; N4-(beta-N-acetylglucosaminyl)-L-asparaginase beta chain ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 20-Apr-2001 ACCESSIONS S11343; S12992; S13448; S18515; A38639; S27353; S27354; !1S15428; I55337; I70078; I70077; S44460; S11571; S21256; !1S22424; S29005; S29006; S29007 REFERENCE S11343 !$#authors Fisher, K.J.; Tollersrud, O.K.; Aronson Jr., N.N. !$#journal FEBS Lett. (1990) 269:440-444 !$#title Cloning and sequence analysis of a cDNA for human !1glycosylasparaginase. !$#cross-references MUID:90382595; PMID:2401370 !$#accession S11343 !'##molecule_type mRNA !'##residues 1-24,'C',26-346 ##label FIS1 !'##cross-references EMBL:X55762; GB:S57449; NID:g34759; !1PIDN:CAA39288.1; PID:g34760 !'##note this sequence has been revised in reference S12992; in GenBank !1entry HSMRNAG, release 109.0, PID:g34760 applies to the !1corrected sequence REFERENCE S12992 !$#authors Fisher, K.J.; Tollersrud, O.K.; Aronson Jr., N.N. !$#journal FEBS Lett. (1990) 276:232 !$#title Corrigendum. Cloning and sequence analysis of a cDNA for !1human glycosylasparaginase. A single gene encodes the !1subunits of this lysosomal amidase. !$#cross-references MUID:91092426; PMID:2265705 !$#accession S12992 !'##molecule_type mRNA !'##residues 24-26 ##label FIS2 !'##cross-references EMBL:X55762; GB:S57449; NID:g34759 REFERENCE S13448 !$#authors Ikonen, E.; Baumann, M.; Groen, K.; Syvaenen, A.C.; Enomaa, !1N.; Halila, R.; Aula, P.; Peltonen, L. !$#journal EMBO J. (1991) 10:51-58 !$#title Aspartylglucosaminuria: cDNA encoding human !1aspartylglucosaminidase and the missense mutation causing !1the disease. !$#cross-references MUID:91114712; PMID:1703489 !$#accession S13448 !'##molecule_type mRNA !'##residues 1-346 ##label IKO !'##cross-references GB:X55330; NID:g28533; PIDN:CAA39029.1; PID:g28534 !$#accession S18515 !'##molecule_type protein !'##residues !126-37;41-51;55-63;71-79;89-91;98-103;111-117;119-127; !1140-143;145-156;164-167;178-185;206-234,235-265,266-277, !1278-287;289-292;336-342 ##label IKO2 !'##note authors found the alpha chain to be blocked (but see reference !1S27353) REFERENCE A38639 !$#authors Mononen, I.; Heisterkamp, N.; Kaartinen, V.; Williams, J.C.; !1Yates III, J.R.; Griffin, P.R.; Hood, L.E.; Groffen, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:2941-2945 !$#title Aspartylglycosaminuria in the Finnish population: !1identification of two point mutations in the heavy chain of !1glycoasparaginase. !$#cross-references MUID:91187907; PMID:2011603 !$#accession A38639 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type mRNA; protein !'##residues 24,'C',26-346 ##label MON !'##cross-references GB:M60808 REFERENCE S27353 !$#authors Rip, J.W.; Coulter-Mackie, M.B.; Rupar, C.A.; Gordon, B.A. !$#journal Biochem. J. (1992) 288:1005-1010 !$#title Purification and structure of human liver !1aspartylglucosaminidase. !$#cross-references MUID:93111925; PMID:1281977 !$#accession S27353 !'##molecule_type protein !'##residues 25-37,'X',39-44 ##label RIP1 !'##note authors found alpha chain not be blocked and found one !1additional residue in some of the purified protein !$#accession S27354 !'##molecule_type protein !'##residues 206-231 ##label RIP2 REFERENCE S15428 !$#authors Halila, R.; Baumann, M.; Ikonen, E.; Enomaa, N.; Peltonen, !1L. !$#journal Biochem. J. (1991) 276:251-256 !$#title Human leucocyte aspartylglucosaminidase. Evidence for two !1different subunits in a more complex native structure. !$#cross-references MUID:91248155; PMID:2039475 !$#accession S15428 !'##status preliminary !'##molecule_type protein !'##residues 206-235 ##label HAL REFERENCE I55337 !$#authors Fisher, K.J.; Aronson, N.N. !$#journal J. Biol. Chem. (1991) 266:12105-12113 !$#title Characterization of the mutation responsible for !1Aspartylglucosaminuria in three finnish patients: Amino acid !1substitution Cys-163 Ser abolishes the activity of lysosomal !1glycosylasparaginase and its conversion into subunits. !$#cross-references MUID:91268094; PMID:1904874 !$#accession I55337 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-160,'Q',162,'S',164-346 ##label FIS3 !'##cross-references GB:M64073; NID:g183329; PIDN:AAA35903.1; !1PID:g183330 !'##note this sequence represents a Finnish population !1aspartylglucosaminuria mutant form; mutation of 163-Cys to !1Ser blocks processing of the single chain precursor into its !1alpha and beta chains and abolishes activity !$#accession I70078 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 103-207,'AV' ##label FIS4 !'##cross-references GB:M64076; NID:g183333; PIDN:AAA35905.1; !1PID:g183334 !'##note this sequence represents a minor splice form found in normal !1controls as well as aspartylglucosaminuria patients and !1encodes a protein chain nearly identical to the alpha chain !1processed from the major splice form !$#accession I70077 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 103-226,237-249 ##label FIS5 !'##cross-references GB:M64075; NID:g183331; PIDN:AAA35904.1; !1PID:g553306 !'##experimental_source fibroblast cell line TC79-842, !1aspartylglucosaminuria patient, American REFERENCE S44460 !$#authors Tollersrud, O.K.; Heiskanen, T.; Peltonen, L. !$#journal Biochem. J. (1994) 300:541-544 !$#title Human leucocyte glycosylasparaginase is an alpha/ !1beta-heterodimer of 19 kDa alpha-subunit and 17 and 18 kDa !1beta-subunit. !$#cross-references MUID:94271172; PMID:8002961 !$#accession S44460 !'##molecule_type protein !'##residues 206-215;24-32 ##label TOL REFERENCE A65113 !$#authors Rouvinen, J.; Oinonen, C. !$#submission submitted to the Brookhaven Protein Data Bank, June 1995 !$#cross-references PDB:1APZ !$#contents annotation; X-ray crystallography, 2.3 angstroms, residues !125-185,206-346 REFERENCE A65112 !$#authors Rouvinen, J.; Oinonen, C. !$#submission submitted to the Brookhaven Protein Data Bank, June 1995 !$#cross-references PDB:1APY !$#contents annotation; X-ray crystallography, 2.0 angstroms, residues !125-185,206-346 REFERENCE A57566 !$#authors Oinonen, C.; Tikkanen, R.; Rouvinen, J.; Peltonen, L. !$#journal Nat. Struct. Biol. (1995) 2:1102-1108 !$#title Three-dimensional structure of human lysosomal !1aspartylglucosaminidase. !$#cross-references MUID:96110871; PMID:8846222 !$#contents annotation; X-ray crystallography, 2.0 angstroms !$#note Cys-61 has a free sulfhydryl; both glycosylation sites have !1phosphoglycans GENETICS !$#gene GDB:AGA !'##cross-references GDB:118981; OMIM:208400 !$#map_position 4q32-4q33 !$#note a defect in this gene may result in the lysosomal storage !1disease aspartylglycosaminuria COMPLEX heterotetramer of two alpha and two beta chains derived from !1a common precursor FUNCTION !$#description hydrolyzes N(4)-(beta-N-acetyl-D-glucosaminyl)-L-asparagine !1to N-acetyl-beta-D-glucosaminylamine and L-aspartic acid !$#pathway protein degradation CLASSIFICATION #superfamily N4-(beta-N-acetylglucosaminyl)-L-asparaginase KEYWORDS aspartylglucosaminuria; blocked amino end; glycoprotein; !1heterotetramer; hydrolase; lysosome; protein degradation FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-205 #product N4- !8(beta-N-acetylglucosaminyl)-L-asparaginase alpha !8chain #status experimental #label ACH\ !$206-346 #product N4- !8(beta-N-acetylglucosaminyl)-L-asparaginase beta chain !8#status experimental #label BCH\ !$38,308 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$64-69,163-179, !$286-306,317-345 #disulfide_bonds #status experimental\ !$206 #active_site Thr #status predicted\ !$234,237 #binding_site substrate (Arg, Asp) #status !8experimental SUMMARY #length 346 #molecular-weight 37194 #checksum 2715 SEQUENCE /// ENTRY MUBPA7 #type complete TITLE N-acetylmuramoyl-L-alanine amidase (EC 3.5.1.28) - phage T7 ALTERNATE_NAMES T7 lysozyme ORGANISM #formal_name phage T7 DATE 01-Sep-1981 #sequence_revision 01-Sep-1981 #text_change 18-Jun-1999 ACCESSIONS C94615; D92866; S42302; S43502; A01001 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession C94615 !'##molecule_type DNA !'##residues 1-151 ##label DU1 REFERENCE A92866 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1981) 148:303-330 !$#title Nucleotide sequence from the genetic left end of !1bacteriophage T7 DNA to the beginning of gene 4. !$#cross-references MUID:82078034; PMID:7310871 !$#accession D92866 !'##molecule_type DNA !'##residues 1-151 ##label DU2 REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42302 !'##molecule_type DNA !'##residues 1-38,'E',40-151 ##label DUN !'##cross-references EMBL:V01146 REFERENCE S43501 !$#authors Dunn, J.J.; Studier, F.W. !$#submission submitted to the EMBL Data Library, October 1993 !$#accession S43502 !'##molecule_type DNA !'##residues 1-38,'E',40-118,'V',120-151 ##label DUW !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24403.1; !1PID:g431190 COMMENT This late gene protein is not required for lysis but plays !1an important role in T7 DNA synthesis. It is known to detach !1the host chromosome from the bacterial membrane to which it !1is normally bound. The functional significance of this is !1not clear. GENETICS !$#gene 3.5 !$#map_position 26.77-27.90 CLASSIFICATION #superfamily phage T7 N-acetylmuramoyl-L-alanine amidase KEYWORDS hydrolase SUMMARY #length 151 #molecular-weight 16923 #checksum 6141 SEQUENCE /// ENTRY I39938 #type complete TITLE N-acetylmuramoyl-L-alanine amidase xlyA - Bacillus subtilis prophage PBSX ALTERNATE_NAMES PBSX prophage-mediated lysis protein xlyA ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS I39938; S47316; A69734; S65592 REFERENCE I39935 !$#authors Longchamp, P.F.; Mauel, C.; Karamata, D. !$#journal Microbiology (1994) 140:1855-1867 !$#title Lytic enzymes associated with defective prophages of !1Bacillus subtilis: Sequencing and characterization of the !1unit comprising the N-acetylmuramoyl-L-alanine amidase of !1the B. subtilis 168 prophage PBSX. !$#cross-references MUID:95005440; PMID:7921239 !$#accession I39938 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-297 ##label RES !'##cross-references GB:L25924; NID:g496172; PIDN:AAA22645.1; !1PID:g496176 REFERENCE S47313 !$#authors Krogh, S.; Joergensen, S.T.; Diderichsen, B.; Devine, K.M. !$#submission submitted to the EMBL Data Library, September 1994 !$#description Sequence of the lysis gene cluster of PBSX. !$#accession S47316 !'##status preliminary !'##molecule_type DNA !'##residues 1-297 ##label KRO !'##cross-references EMBL:Z36941; NID:g535793; PIDN:CAA85403.1; !1PID:g535797 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69734 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-297 ##label KUN !'##cross-references GB:Z99110; GB:AL009126; NID:g2633472; !1PIDN:CAB13138.1; PID:g2633635 !'##experimental_source strain 168 GENETICS !$#gene xlyA CLASSIFICATION #superfamily Bacillus N-acetylmuramoyl-L-alanine amidase SUMMARY #length 297 #molecular-weight 31913 #checksum 4205 SEQUENCE /// ENTRY S08306 #type complete TITLE hydrolase - Bacillus sp. ORGANISM #formal_name Bacillus sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S08306 REFERENCE S08306 !$#authors Potvin, C.; Leclerc, D.; Tremblay, G.; Asselin, A.; !1Bellemare, G. !$#journal Mol. Gen. Genet. (1988) 214:241-248 !$#title Cloning, sequencing and expression of a Bacillus !1bacteriolytic enzyme in Escherichia coli. !$#cross-references MUID:89181523; PMID:3070348 !$#accession S08306 !'##status preliminary !'##molecule_type DNA !'##residues 1-251 ##label POT !'##cross-references EMBL:X13524; NID:g39949; PIDN:CAA31877.1; !1PID:g39950 CLASSIFICATION #superfamily Bacillus N-acetylmuramoyl-L-alanine amidase SUMMARY #length 251 #molecular-weight 28473 #checksum 7229 SEQUENCE /// ENTRY MUBPCP #type complete TITLE N-acetylmuramoyl-L-alanine amidase (EC 3.5.1.28) - phage CP-1 ORGANISM #formal_name phage CP-1 #note host Streptococcus pneumoniae DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 09-Apr-1998 ACCESSIONS A31086 REFERENCE A31086 !$#authors Garcia, E.; Garcia, J.L.; Garcia, P.; Arraras, A.; !1Sanchez-Puelles, J.M.; Lopez, R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:914-918 !$#title Molecular evolution of lytic enzymes of Streptococcus !1pneumoniae and its bacteriophages. !$#cross-references MUID:88124951; PMID:3422470 !$#accession A31086 !'##molecule_type DNA !'##residues 1-339 ##label GAR COMMENT This lytic enzyme is responsible for the separation of the !1host daughter cells at the end of cell division and !1participates in the liberation of progeny bacteriophage into !1the medium. GENETICS !$#gene cpl CLASSIFICATION #superfamily phage CP-1 N-acetylmuramoyl-L-alanine amidase; !1Chalara lysozyme homology; cpl repeat homology KEYWORDS hydrolase; tandem repeat FEATURE !$10-158 #domain Chalara lysozyme homology #label CHL\ !$209-229 #domain cpl repeat homology #label CP1\ !$230-250 #domain cpl repeat homology #label CP2\ !$251-270 #domain cpl repeat homology #label CP3\ !$271-290 #domain cpl repeat homology #label CP4\ !$291-312 #domain cpl repeat homology #label CP5\ !$313-334 #domain cpl repeat homology #label CP6\ !$10,37 #active_site Asp, Glu #status predicted SUMMARY #length 339 #molecular-weight 39189 #checksum 6407 SEQUENCE /// ENTRY MUBPC9 #type complete TITLE N-acetylmuramoyl-L-alanine amidase (EC 3.5.1.28) - phage CP-9 ALTERNATE_NAMES muramidase ORGANISM #formal_name phage CP-9 #note host Streptococcus pneumoniae DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 18-Jun-1999 ACCESSIONS JQ0438 REFERENCE JQ0437 !$#authors Garcia, P.; Garcia, J.L.; Garcia, E.; Sanchez-Puelles, J.M.; !1Lopez, R. !$#journal Gene (1990) 86:81-88 !$#title Modular organization of the lytic enzymes of Streptococcus !1pneumoniae and its bacteriophages. !$#cross-references MUID:90185251; PMID:2311937 !$#accession JQ0438 !'##molecule_type DNA !'##residues 1-339 ##label GAR !'##cross-references GB:M34780; NID:g166187; PIDN:AAA72845.1; !1PID:g166188 COMMENT This lytic enzyme is responsible for the separation of the !1host daughter cells at the end of cell division and !1participates in the liberation of progeny bacteriophages !1into the medium. GENETICS !$#gene cpl9 CLASSIFICATION #superfamily phage CP-1 N-acetylmuramoyl-L-alanine amidase; !1Chalara lysozyme homology; cpl repeat homology KEYWORDS hydrolase; tandem repeat FEATURE !$10-158 #domain Chalara lysozyme homology #label CHL\ !$209-229 #domain cpl repeat homology #label CP1\ !$230-250 #domain cpl repeat homology #label CP2\ !$251-270 #domain cpl repeat homology #label CP3\ !$271-290 #domain cpl repeat homology #label CP4\ !$291-312 #domain cpl repeat homology #label CP5\ !$313-334 #domain cpl repeat homology #label CP6\ !$10,37 #active_site Asp, Glu #status predicted SUMMARY #length 339 #molecular-weight 39150 #checksum 7773 SEQUENCE /// ENTRY MUBPC7 #type complete TITLE N-acetylmuramoyl-L-alanine amidase (EC 3.5.1.28) - phage CP-7 ALTERNATE_NAMES muramidase ORGANISM #formal_name phage CP-7 #note host Streptococcus pneumoniae DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 09-Apr-1998 ACCESSIONS JQ0437 REFERENCE JQ0437 !$#authors Garcia, P.; Garcia, J.L.; Garcia, E.; Sanchez-Puelles, J.M.; !1Lopez, R. !$#journal Gene (1990) 86:81-88 !$#title Modular organization of the lytic enzymes of Streptococcus !1pneumoniae and its bacteriophages. !$#cross-references MUID:90185251; PMID:2311937 !$#accession JQ0437 !'##molecule_type DNA !'##residues 1-342 ##label GAR !'##cross-references GB:M34779 COMMENT This lytic enzyme is responsible for the separation of the !1host daughter cells at the end of cell division and !1participates in the liberation of progeny bacteriophages !1into the medium. GENETICS !$#gene cpl7 CLASSIFICATION #superfamily phage CP-7 N-acetylmuramoyl-L-alanine amidase; !1Chalara lysozyme homology KEYWORDS hydrolase FEATURE !$10-158 #domain Chalara lysozyme homology #label CHL\ !$205-252 #domain cpl7 repeat #label CP7A\ !$253-300 #domain cpl7 repeat #label CP7B\ !$301-342 #domain cpl7 repeat #label CP7C\ !$10,37 #active_site Asp, Glu #status predicted SUMMARY #length 342 #molecular-weight 38556 #checksum 167 SEQUENCE /// ENTRY S16016 #type complete TITLE N-acetylmuramoyl-L-alanine amidase (EC 3.5.1.28) - Streptococcus pneumoniae phage HB-3 ALTERNATE_NAMES lytic amidase ORGANISM #formal_name Streptococcus pneumoniae phage HB-3 DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 18-Jun-1999 ACCESSIONS S16016; S27095 REFERENCE S16016 !$#authors Romero, A.; Lopez, R.; Garcia, P. !$#journal J. Bacteriol. (1990) 172:5064-5070 !$#title Sequence of the Streptococcus pneumoniae bacteriophage HB-3 !1amidase reveals high homology with the major host autolysin. !$#cross-references MUID:90368559; PMID:1975580 !$#accession S16016 !'##molecule_type DNA !'##residues 1-318 ##label ROM1 !'##cross-references GB:M34652; NID:g215055; PIDN:AAA50574.1; !1PID:g215056 REFERENCE S27095 !$#authors Romero, A.; Lopez, R.; Garcia, P. !$#journal J. Virol. (1990) 64:137-142 !$#title Characterization of the pneumococcal bacteriophage HB-3 !1amidase: cloning and expression in Escherichia coli. !$#cross-references MUID:90080114; PMID:1967150 !$#accession S27095 !'##molecule_type protein !'##residues 1-21 ##label ROM2 GENETICS !$#gene hbl CLASSIFICATION #superfamily phage HB-3 N-acetylmuramoyl-L-alanine amidase; !1cpl repeat homology KEYWORDS hydrolase; tandem repeat FEATURE !$1-318 #product N-acetylmuramoyl-L-alanine amidase #status !8experimental #label MAT\ !$185-205 #domain cpl repeat homology #label CP1\ !$206-226 #domain cpl repeat homology #label CP2\ !$228-247 #domain cpl repeat homology #label CP3\ !$248-267 #domain cpl repeat homology #label CP4A\ !$268-289 #domain cpl repeat homology #label CP4\ !$292-313 #domain cpl repeat homology #label CP5 SUMMARY #length 318 #molecular-weight 36509 #checksum 6122 SEQUENCE /// ENTRY A42936 #type complete TITLE N-acetylmuramoyl-L-alanine amidase (EC 3.5.1.28) - phage EJ-1 ORGANISM #formal_name phage EJ-1 #note host Streptococcus pneumoniae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A42936 REFERENCE A42936 !$#authors Diaz, E.; Lopez, R.; Garcia, J.L. !$#journal J. Bacteriol. (1992) 174:5516-5525 !$#title EJ-1, a temperate bacteriophage of Streptococcus pneumoniae !1with a Myoviridae morphotype. !$#cross-references MUID:92380924; PMID:1355083 !$#contents Streptococcus pneumoniae 101/87 !$#accession A42936 !'##molecule_type DNA !'##residues 1-316 ##label DIA !'##cross-references GB:S43512; NID:g254539; PIDN:AAB23083.1; !1PID:g254540 !'##note sequence extracted from NCBI backbone (NCBIN:112096, !1NCBIP:112097) CLASSIFICATION #superfamily phage HB-3 N-acetylmuramoyl-L-alanine amidase; !1cpl repeat homology KEYWORDS hydrolase; tandem repeat FEATURE !$185-205 #domain cpl repeat homology #label CP1\ !$206-226 #domain cpl repeat homology #label CP2\ !$248-267 #domain cpl repeat homology #label CP3 SUMMARY #length 316 #molecular-weight 36575 #checksum 1948 SEQUENCE /// ENTRY A42935 #type complete TITLE N-acetylmuramoyl-L-alanine amidase (EC 3.5.1.28) - Streptococcus pneumoniae ALTERNATE_NAMES lytic amidase ORGANISM #formal_name Streptococcus pneumoniae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A42935 REFERENCE A42935 !$#authors Diaz, E.; Lopez, R.; Garcia, J.L. !$#journal J. Bacteriol. (1992) 174:5508-5515 !$#title Role of the major pneumococcal autolysin in the atypical !1response of a clinical isolate of Streptococcus pneumoniae. !$#cross-references MUID:92380923; PMID:1355082 !$#accession A42935 !'##molecule_type DNA !'##residues 1-316 ##label DIA !'##cross-references GB:S43511; NID:g254537; PIDN:AAB23082.1; !1PID:g254538 !'##experimental_source strain 101/87 !'##note sequence extracted from NCBI backbone (NCBIN:112094, !1NCBIP:112095) CLASSIFICATION #superfamily phage HB-3 N-acetylmuramoyl-L-alanine amidase; !1cpl repeat homology KEYWORDS hydrolase FEATURE !$185-205 #domain cpl repeat homology #label CP1\ !$206-226 #domain cpl repeat homology #label CP2\ !$248-267 #domain cpl repeat homology #label CP3 SUMMARY #length 316 #molecular-weight 36513 #checksum 50 SEQUENCE /// ENTRY JN0885 #type complete TITLE N-carbamyl-L-amino acid amidohydrolase (EC 3.5.1.-) [validated] - Bacillus stearothermophilus (strain NS1122A) ORGANISM #formal_name Bacillus stearothermophilus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Sep-2000 ACCESSIONS JN0885; PN0679; I40357 REFERENCE JN0885 !$#authors Mukohara, Y.; Ishikawa, T.; Watabe, K.; Nakamura, H. !$#journal Biosci. Biotechnol. Biochem. (1993) 57:1935-1937 !$#title Molecular cloning and sequencing of the gene for a !1thermostable N-carbamyl-L-amino acid amidohydrolase from !1Bacillus stearothermophilus strain NS1122A. !$#cross-references MUID:94115050; PMID:7764340 !$#accession JN0885 !'##molecule_type DNA !'##residues 1-409 ##label MUK !'##cross-references GB:S67784; NID:g460894; PIDN:AAC60456.1; !1PID:g460895 !$#accession PN0679 !'##molecule_type protein !'##residues 1-13 ##label MU2 REFERENCE I40357 !$#authors Sakanyan, V.; Desmarez, L.; Legrain, C.; Charlier, D.; Mett, !1T.; Kochikyan, A.; Savchenko, A.; Boyen, A.; Falmagne, P.; !1Pirard, A.; Glansdorff, N. !$#journal Appl. Environ. Microbiol. (1993) 59:3878-3888 !$#title Gene cloning, sequence analysis, purification, and !1characterization of a thermostable aminoacylase from !1Bacillus stearothermophilus. !$#cross-references MUID:94113715; PMID:8285691 !$#accession I40357 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 'DRE',63-198,'A',200-219,'A',221,'P',223-314,'L',316-323, !1'A',325-329,'EV',332-333,'Q',335-337,'R',339-340,'KQ', !1343-346,'P',348-357,'G',359-392,'V',394-409 ##label RES !'##cross-references EMBL:X74289; NID:g436795; PIDN:CAA52341.1; !1PID:g436796 FUNCTION !$#description catalyzes the hydrolysis of an N-carbamoyl-L-amino acid to !1ammonia, carbon dioxide, and amino acid CLASSIFICATION #superfamily N-carbamyl-L-amino acid amidohydrolase KEYWORDS hydrolase SUMMARY #length 409 #molecular-weight 44248 #checksum 5034 SEQUENCE /// ENTRY D42594 #type complete TITLE N-carbamyl-L-amino acid amidohydrolase (EC 3.5.1.-) hyuC [similarity] - Pseudomonas sp. plasmid pHN671 ORGANISM #formal_name Pseudomonas sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Sep-2000 ACCESSIONS D42594 REFERENCE A42594 !$#authors Watabe, K.; Ishikawa, T.; Mukohara, Y.; Nakamura, H. !$#journal J. Bacteriol. (1992) 174:962-969 !$#title Cloning and sequencing of the genes involved in the !1conversion of 5-substituted hydantoins to the corresponding !1L-amino acids from the native plasmid of Pseudomonas sp. !1strain NS671. !$#cross-references MUID:92121137; PMID:1732229 !$#accession D42594 !'##status preliminary !'##molecule_type DNA !'##residues 1-414 ##label WAT !'##note sequence extracted from NCBI backbone (NCBIN:77753, !1NCBIP:77763) CLASSIFICATION #superfamily N-carbamyl-L-amino acid amidohydrolase KEYWORDS hydrolase SUMMARY #length 414 #molecular-weight 45683 #checksum 3908 SEQUENCE /// ENTRY G70017 #type complete TITLE probable N-carbamyl-L-amino acid amidohydrolase (EC 3.5.1.-) yurH [similarity] - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 08-Sep-2000 ACCESSIONS G70017 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G70017 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-412 ##label KUN !'##cross-references GB:Z99120; GB:AL009126; NID:g2635613; !1PIDN:CAB15243.1; PID:g2635750 !'##experimental_source strain 168 GENETICS !$#gene yurH CLASSIFICATION #superfamily N-carbamyl-L-amino acid amidohydrolase KEYWORDS hydrolase SUMMARY #length 412 #molecular-weight 45519 #checksum 7065 SEQUENCE /// ENTRY C64783 #type complete TITLE probable N-carbamyl-L-amino acid amidohydrolase (EC 3.5.1.-) ylbB [similarity] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS C64783 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64783 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-411 ##label BLAT !'##cross-references GB:AE000157; GB:U00096; NID:g1786716; !1PIDN:AAC73618.1; PID:g1786726; UWGP:b0516 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ylbB CLASSIFICATION #superfamily N-carbamyl-L-amino acid amidohydrolase KEYWORDS hydrolase SUMMARY #length 411 #molecular-weight 45694 #checksum 4210 SEQUENCE /// ENTRY D64079 #type complete TITLE probable N-carbamyl-L-amino acid amidohydrolase (EC 3.5.1.-) HI0588 [similarity] - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 08-Sep-2000 ACCESSIONS D64079 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession D64079 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-411 ##label TIGR !'##cross-references GB:U32740; GB:L42023; NID:g1573572; !1PIDN:AAC22245.1; PID:g1573578; TIGR:HI0588 CLASSIFICATION #superfamily N-carbamyl-L-amino acid amidohydrolase KEYWORDS hydrolase SUMMARY #length 411 #molecular-weight 45091 #checksum 7426 SEQUENCE /// ENTRY PNFMGF #type complete TITLE peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase (EC 3.5.1.52) precursor [validated] - Flavobacterium meningosepticum ALTERNATE_NAMES N-glycopeptidase F; N-glycosidase F; PNGase F ORGANISM #formal_name Flavobacterium meningosepticum DATE 28-Jun-1991 #sequence_revision 05-Apr-1995 #text_change 15-Sep-2000 ACCESSIONS A38365; A35759; A35760 REFERENCE A38365 !$#authors Lemp, D.; Haselbeck, A.; Klebl, F. !$#journal J. Biol. Chem. (1990) 265:15606-15610 !$#title Molecular cloning and heterologous expression of !1N-glycosidase F from Flavobacterium meningosepticum. !$#cross-references MUID:90368767; PMID:2203781 !$#accession A38365 !'##molecule_type DNA !'##residues 1-354 ##label LEM !'##cross-references GB:M57237; NID:g148708; PIDN:AAA24928.1; !1PID:g148709 !'##note the sequence in GenBank entry FVBNGLF, release 111.0, !1(PID:g148709) has the codon GGT for 101-Arg rather than the !1published CGT !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing REFERENCE A35759 !$#authors Tarentino, A.L.; Quinones, G.; Trumble, A.; Changchien, !1L.M.; Duceman, B.; Maley, F.; Plummer Jr., T.H. !$#journal J. Biol. Chem. (1990) 265:6961-6966 !$#title Molecular cloning and amino acid sequence of peptide-N(4)- !1(N-acetyl-beta-D-glucosaminyl)asparagine amidase from !1Flavobacterium meningosepticum. !$#cross-references MUID:90216731; PMID:2182634 !$#accession A35759 !'##molecule_type DNA !'##residues 1-32,'G',34-282,'I',284-354 ##label TAR !'##cross-references GB:J05449; NID:g148718; PIDN:AAA85323.1; !1PID:g148719 !'##note the authors translated the codon GGG for residue 33 as Arg, and !1ATT for residue 283 as Asn !'##note parts of this sequence, including the amino end of the mature !1recombinant protein expressed in Escherichia coli, were !1determined by protein sequencing !'##note the protein expressed in Escherichia coli was processed to !1begin with Ala-41 REFERENCE A35760 !$#authors Barsomian, G.D.; Johnson, T.L.; Borowski, M.; Denman, J.; !1Ollington, J.F.; Hirani, S.; McNeilly, D.S.; Rasmussen, J.R. !$#journal J. Biol. Chem. (1990) 265:6967-6972 !$#title Cloning and expression of peptide-N(4)- !1(N-acetyl-beta-D-glucosaminyl)asparagine amidase F in !1Escherichia coli. !$#cross-references MUID:90216732; PMID:2182635 !$#accession A35760 !'##molecule_type DNA !'##residues 1-159,'C',161-354 ##label BAR !'##cross-references GB:J05411; NID:g148720; PIDN:AAA24932.1; !1PID:g148721 !'##note the protein expressed in Escherichia coli was processed to !1begin with Val-23, Ala-26 and Ala-41 !'##note the amino end of the mature protein from Flavobacterium !1meningosepticum was not determined but was thought to be !1Ala-41 REFERENCE A66389 !$#authors Van Roey, P.; Kuhn, P. !$#submission submitted to the Brookhaven Protein Data Bank, October 1995 !$#cross-references PDB:1PNF !$#contents annotation; X-ray crystallography, 2.0 angstroms, residues !141-354 REFERENCE A52826 !$#authors Van Roey, P.; Kuhn, P. !$#submission submitted to the Brookhaven Protein Data Bank, June 1994 !$#cross-references PDB:1PNG !$#contents annotation; X-ray crystallography, 2.2 angstroms, residues !145-354 REFERENCE A67130 !$#authors Norris, G.E.; Stillman, T.J.; Anderson, B.F.; Baker, E.N. !$#submission submitted to the Brookhaven Protein Data Bank, October 1994 !$#cross-references PDB:1PGS !$#contents annotation; X-ray crystallography, 1.8 angstroms, residues !144-284,'T',286-354 REFERENCE A57726 !$#authors Kuhn, P.; Guan, C.; Cui, T.; Tarentino, A.L.; Plummer Jr., !1T.H.; Van Roey, P. !$#journal J. Biol. Chem. (1995) 270:29493-29497 !$#title Active site and oligosaccharide recognition residues of !1peptide-N(4)-(N-acetyl-beta-D-glucosaminyl)asparagine !1amidase F. !$#cross-references MUID:96094350; PMID:7493989 !$#contents annotation; active site REFERENCE A55833 !$#authors Kuhn, P.; Tarentino, A.L.; Plummer Jr., T.H.; Van Roey, P. !$#journal Biochemistry (1994) 33:11699-11706 !$#title Crystal structure of peptide-N(4)- !1(N-acetyl-beta-D-glucosaminyl)asparagine amidase F at !12.2-angstrom resolution. !$#cross-references MUID:95001878; PMID:7918386 !$#contents annotation; X-ray crystallography, 2.2 angstroms FUNCTION !$#description hydrolyzes the beta-aspartylglucosaminyl bond to !1peptide-aspartic acid and 1-aminooligosaccharide, which !1spontaneously hydrolyzes to ammonia and oligosaccharide !$#pathway protein degradation CLASSIFICATION #superfamily peptide-N4- !1(N-acetyl-beta-glucosaminyl)asparagine amidase KEYWORDS blocked amino end; hydrolase; protein degradation FEATURE !$1-42 #domain leader peptide #status predicted #label PRO\ !$43-354 #product peptide-N4- !8(N-acetyl-beta-glucosaminyl)asparagine amidase !8#status experimental #label MAT\ !$43 #modified_site blocked amino end (Ala) (in mature !8form) (partial) #status experimental\ !$91-96,244-248, !$271-292 #disulfide_bonds #status experimental\ !$100,158,246 #active_site Asp, Glu, Glu #status predicted SUMMARY #length 354 #molecular-weight 39032 #checksum 6837 SEQUENCE /// ENTRY DEECOO #type complete TITLE dihydroorotase (EC 3.5.2.3) - Escherichia coli (strain K-12) ALTERNATE_NAMES carbamoylaspartic dehydrase ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 01-Mar-2002 ACCESSIONS A25008; A27084; C64849 REFERENCE A91177 !$#authors Backstrom, D.; Sjoberg, R.M.; Lundberg, L.G. !$#journal Eur. J. Biochem. (1986) 160:77-82 !$#title Nucleotide sequence of the structural gene for !1dihydroorotase of Escherichia coli K12. !$#cross-references MUID:87030260; PMID:2876892 !$#accession A25008 !'##molecule_type DNA !'##residues 1-348 ##label BAC !'##cross-references EMBL:X04469; NID:g42605; PIDN:CAA28157.1; !1PID:g42607 !'##experimental_source strain K-12 REFERENCE A91836 !$#authors Wilson, H.R.; Chan, P.T.; Turnbough Jr., C.L. !$#journal J. Bacteriol. (1987) 169:3051-3058 !$#title Nucleotide sequence and expression of the pyrC gene of !1Escherichia coli K-12. !$#cross-references MUID:87250268; PMID:2885307 !$#accession A27084 !'##molecule_type mRNA !'##residues 1-348 ##label WIL !'##cross-references EMBL:M16752; NID:g147472; PIDN:AAA24482.1; !1PID:g147473 !'##experimental_source strain K-12 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64849 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-348 ##label BLAT !'##cross-references GB:AE000207; GB:U00096; NID:g1787293; !1PIDN:AAC74146.1; PID:g1787301; UWGP:b1062 !'##experimental_source strain K-12, substrain MG1655 COMMENT The de novo synthesis of UMP, the precursor of all !1pyrimidine nucleotides, is catalyzed by six enzymes encoded !1by six unlinked genes and operons. pyrC and pyrD expression !1appears to be repressed primarily by a cytidine nucleotide. GENETICS !$#gene pyrC !$#map_position 23 min FUNCTION !$#description catalyzes conversion of N-carbamoyl-L-aspartate into !1dihydroorotate !$#pathway pyrimidine nucleotide biosynthesis !$#note zinc required for catalytic activity CLASSIFICATION #superfamily dihydroorotase KEYWORDS homodimer; hydrolase; pyrimidine nucleotide biosynthesis; !1zinc FEATURE !$17,19 #binding_site zinc (His) #status predicted SUMMARY #length 348 #molecular-weight 38827 #checksum 5705 SEQUENCE /// ENTRY DEEBOT #type complete TITLE dihydroorotase (EC 3.5.2.3) - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 18-Jun-1999 ACCESSIONS A27143 REFERENCE A27143 !$#authors Neuhard, J.; Kelln, R.A.; Stauning, E. !$#journal Eur. J. Biochem. (1986) 157:335-342 !$#title Cloning and structural characterization of the Salmonella !1typhimurium pyrC gene encoding dihydroorotase. !$#cross-references MUID:86220211; PMID:2872051 !$#accession A27143 !'##molecule_type DNA !'##residues 1-348 ##label NEU !'##cross-references GB:X03928; NID:g47865; PIDN:CAA27567.1; PID:g47867 !'##experimental_source strain LT2 COMMENT The de novo synthesis of UMP, the precursor of all !1pyrimidine nucleotides, is catalyzed by six enzymes encoded !1by six unlinked genes and operons. pyrC and pyrD expression !1appears to be repressed primarily by a cytidine nucleotide. GENETICS !$#gene pyrC !$#map_position 23 min FUNCTION !$#description catalyzes conversion of N-carbamoyl-L-aspartate into !1dihydroorotate !$#pathway pyrimidine nucleotide biosynthesis !$#note zinc required for catalytic activity CLASSIFICATION #superfamily dihydroorotase KEYWORDS homodimer; hydrolase; pyrimidine nucleotide biosynthesis; !1zinc FEATURE !$17,19 #binding_site zinc (His) #status predicted SUMMARY #length 348 #molecular-weight 38563 #checksum 2219 SEQUENCE /// ENTRY DEBYO #type complete TITLE dihydroorotase (EC 3.5.2.3) URA4 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein L9931.1; protein YLR420w ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1993 #sequence_revision 23-Feb-1996 #text_change 12-Nov-1999 ACCESSIONS S59385; S00902 REFERENCE S59376 !$#authors Favello, A. !$#submission submitted to the EMBL Data Library, January 1995 !$#description The sequence of S. cerevisiae cosmid 9931. !$#accession S59385 !'##molecule_type DNA !'##residues 1-364 ##label FAV !'##cross-references EMBL:U20162; NID:g632669; PIDN:AAB67491.1; !1PID:g632670; GSPDB:GN00012; MIPS:YLR420w !'##experimental_source strain S288C (AB972) REFERENCE S00902 !$#authors Guyonvarch, A.; Nguyen-Juilleret, M.; Hubert, J.C.; !1Lacroute, F. !$#journal Mol. Gen. Genet. (1988) 212:134-141 !$#title Structure of the Saccharomyces cerevisiae URA4 gene encoding !1dihydroorotase. !$#cross-references MUID:88232423; PMID:2897615 !$#accession S00902 !'##molecule_type DNA !'##residues 1-106,'IRLL',111,'WIQMTSAH',120-155,'R',157-239,'R', !1241-268,'K',270-318,'M',320-364 ##label GUY !'##cross-references EMBL:X07561; NID:g4764; PIDN:CAA30444.1; PID:g4765 !'##experimental_source strain FL100 !'##note the authors translated the codon TAT for residue 252 as Ile and !1TAC for residue 278 as Ile COMMENT The active enzyme with tightly bound zinc catalyzes the !1reversible cyclization of carbamyl aspartate to !1dihydroorotate, one step in the synthesis of UMP, the !1precursor of all pyrimidine nucleotides. GENETICS !$#gene SGD:URA4; MIPS:YLR420w !'##cross-references SGD:S0004412; MIPS:YLR420w !$#map_position 12R CLASSIFICATION #superfamily dihydroorotase KEYWORDS hydrolase; pyrimidine nucleotide biosynthesis; zinc SUMMARY #length 364 #molecular-weight 40313 #checksum 9812 SEQUENCE /// ENTRY DEUSO #type complete TITLE dihydroorotase (EC 3.5.2.3) - smut fungus (Ustilago maydis) ORGANISM #formal_name Ustilago maydis #common_name corn smut DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 18-Jun-1999 ACCESSIONS JQ1667; S18886 REFERENCE JQ1667 !$#authors Spanos, A.; Kanuga, N.; Holden, D.W.; Banks, G.R. !$#journal Gene (1992) 117:73-79 !$#title The Ustilago maydis pyr3 gene: sequence and transcriptional !1analysis. !$#cross-references MUID:92354940; PMID:1353740 !$#accession JQ1667 !'##molecule_type DNA !'##residues 1-391 ##label SP2 !'##cross-references EMBL:X63181; NID:g5233; PIDN:CAA44866.1; PID:g5234; !1GB:M59757 COMMENT The active enzyme with tightly bound zinc catalyzes the !1reversible cyclization of carbamyl aspartate to !1dihydroorotate, one step in the synthesis of UMP, the !1precursor of all pyrimidine nucleotides. GENETICS !$#gene pyr3 CLASSIFICATION #superfamily dihydroorotase KEYWORDS hydrolase; pyrimidine nucleotide biosynthesis; zinc SUMMARY #length 391 #molecular-weight 42537 #checksum 8234 SEQUENCE /// ENTRY DEBSO #type complete TITLE dihydroorotase (EC 3.5.2.3) - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 21-Jul-2000 ACCESSIONS D39845; C69686 REFERENCE A39845 !$#authors Quinn, C.L.; Stephenson, B.T.; Switzer, R.L. !$#journal J. Biol. Chem. (1991) 266:9113-9127 !$#title Functional organization and nucleotide sequence of the !1Bacillus subtilis pyrimidine biosynthetic operon. !$#cross-references MUID:91225016; PMID:1709162 !$#accession D39845 !'##molecule_type DNA !'##residues 1-428 ##label QUI !'##cross-references GB:M59757; NID:g4887706; PIDN:AAA21268.1; !1PID:g143388 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69686 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-428 ##label KUN !'##cross-references GB:Z99112; GB:AL009126; NID:g2633902; !1PIDN:CAB13424.1; PID:g2633923 !'##experimental_source strain 168 COMMENT The active enzyme is a dimer of identical chains with one !1tightly bound zinc atom per chain; it catalyzes the !1reversible cyclization of carbamyl aspartate to !1dihydroorotate, one step in the synthesis of UMP. GENETICS !$#gene pyrC CLASSIFICATION #superfamily Bacillus dihydroorotase; Bacillus !1dihydroorotase homology KEYWORDS homodimer; hydrolase; pyrimidine nucleotide biosynthesis; !1zinc FEATURE !$45-428 #domain Bacillus dihydroorotase homology #label DHO SUMMARY #length 428 #molecular-weight 46609 #checksum 6261 SEQUENCE /// ENTRY S48489 #type complete TITLE allantoinase (EC 3.5.2.5) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YIR027c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 12-Nov-1999 ACCESSIONS S48489; S28649 REFERENCE S48478 !$#authors Rowley, K. !$#submission submitted to the EMBL Data Library, October 1994 !$#accession S48489 !'##molecule_type DNA !'##residues 1-460 ##label ROW !'##cross-references GB:Z47047; EMBL:Z38061; NID:g603997; PID:g763372; !1GSPDB:GN00009; MIPS:YIR027c REFERENCE S28649 !$#authors Buckholz, R.G.; Cooper, T.G. !$#journal Yeast (1991) 7:913-923 !$#title The allantoinase (DAL1) gene of Saccharomyces cerevisiae. !$#cross-references MUID:92206070; PMID:1803816 !$#accession S28649 !'##molecule_type DNA !'##residues 1-437,'WYIRMPTESRKHHWVKLCLILDVKLKLQIFIKEIL' ##label BUC !'##cross-references EMBL:M69294; NID:g171365; PIDN:AAA34553.1; !1PID:g171366 GENETICS !$#gene SGD:DAL1; MIPS:YIR027c !'##cross-references SGD:S0001466; MIPS:YIR027c !$#map_position 9R CLASSIFICATION #superfamily allantoinase; Bacillus dihydroorotase homology KEYWORDS hydrolase FEATURE !$56-447 #domain Bacillus dihydroorotase homology #label DHO SUMMARY #length 460 #molecular-weight 50126 #checksum 825 SEQUENCE /// ENTRY A53595 #type complete TITLE allantoinase (EC 3.5.2.5) precursor - bullfrog ORGANISM #formal_name Rana catesbeiana #common_name bullfrog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A53595 REFERENCE A53595 !$#authors Hayashi, S.; Jain, S.; Chu, R.; Alvares, K.; Xu, B.; !1Erfurth, F.; Usuda, N.; Rao, M.S.; Reddy, S.K.; Noguchi, T.; !1Reddy, J.K.; Yeldandi, A.V. !$#journal J. Biol. Chem. (1994) 269:12269-12276 !$#title Amphibian allantoinase. Molecular cloning, tissue !1distribution, and functional expression. !$#cross-references MUID:94216348; PMID:8163532 !$#accession A53595 !'##status preliminary !'##molecule_type mRNA !'##residues 1-483 ##label HAY !'##cross-references GB:U03471 CLASSIFICATION #superfamily allantoinase; Bacillus dihydroorotase homology KEYWORDS hydrolase; mitochondrion SUMMARY #length 483 #molecular-weight 53186 #checksum 7164 SEQUENCE /// ENTRY C70016 #type complete TITLE allantoinase homolog yunH - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS C70016 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C70016 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-446 ##label KUN !'##cross-references GB:Z99120; GB:AL009126; NID:g2635613; !1PIDN:CAB15231.1; PID:g2635738 !'##experimental_source strain 168 GENETICS !$#gene yunH CLASSIFICATION #superfamily allantoinase; Bacillus dihydroorotase homology FEATURE !$46-434 #domain Bacillus dihydroorotase homology #label DHO SUMMARY #length 446 #molecular-weight 48331 #checksum 8614 SEQUENCE /// ENTRY G64782 #type complete TITLE probable allantoinase (EC 3.5.2.5) - Escherichia coli (strain K-12) ALTERNATE_NAMES protein b0512 ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS G64782 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64782 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-453 ##label BLAT !'##cross-references GB:AE000157; GB:U00096; NID:g1786716; !1PIDN:AAC73614.1; PID:g1786722; UWGP:b0512 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ybbX CLASSIFICATION #superfamily allantoinase; Bacillus dihydroorotase homology KEYWORDS hydrolase FEATURE !$45-438 #domain Bacillus dihydroorotase homology #label DHO SUMMARY #length 453 #molecular-weight 49601 #checksum 2222 SEQUENCE /// ENTRY JC2310 #type complete TITLE dihydropyrimidinase (EC 3.5.2.2) - Bacillus stearothermophilus ALTERNATE_NAMES hydantoinase ORGANISM #formal_name Bacillus stearothermophilus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JC2310; PC2206 REFERENCE JC2310 !$#authors Mukohara, Y.; Ishikawa, T.; Watabe, K.; Nakamura, H. !$#journal Biosci. Biotechnol. Biochem. (1994) 58:1621-1626 !$#title A thermostable hydantoinase of Bacillus stearothermophilus !1NS1122A: Cloning, sequencing, and high expression of the !1enzyme gene, and some properties of the expressed enzyme. !$#cross-references MUID:95036870; PMID:7765480 !$#contents NS1122A !$#accession JC2310 !'##molecule_type DNA !'##residues 1-471 ##label MUK !'##cross-references GB:S73773; NID:g688287; PIDN:AAC60487.1; !1PID:g688288 !$#accession PC2206 !'##molecule_type protein !'##residues 1-20 ##label MU2 COMMENT This enzyme is a metalloenzyme and the oligomeric structure !1is required for activity. CLASSIFICATION #superfamily allantoinase; Bacillus dihydroorotase homology KEYWORDS hydrolase SUMMARY #length 471 #molecular-weight 51725 #checksum 7559 SEQUENCE /// ENTRY PNSAP #type complete TITLE beta-lactamase (EC 3.5.2.6) precursor - Staphylococcus aureus ALTERNATE_NAMES cephalosporinase; penicillinase ORGANISM #formal_name Staphylococcus aureus DATE 30-Apr-1982 #sequence_revision 30-Apr-1982 #text_change 18-Jun-1999 ACCESSIONS A01002; A23600; A90289; S06757; A45789; B45789; D45789; !1C45789; S11784; A60992 REFERENCE A92295 !$#authors McLaughlin, J.R.; Murray, C.L.; Rabinowitz, J.C. !$#journal J. Biol. Chem. (1981) 256:11283-11291 !$#title Unique features in the ribosome binding site sequence of the !1gram-positive Staphylococcus aureus beta-lactamase gene. !$#cross-references MUID:82030947; PMID:6793593 !$#accession A01002 !'##molecule_type DNA !'##residues 1-47 ##label MCL !'##cross-references GB:X04121 REFERENCE A23600 !$#authors Chan, P.T. !$#journal Nucleic Acids Res. (1986) 14:5940 !$#title Nucleotide sequence of the Staphylococcus aureus PC1 !1beta-lactamase gene. !$#cross-references MUID:86286605; PMID:3488540 !$#accession A23600 !'##molecule_type DNA !'##residues 1-281 ##label CHA !'##cross-references GB:X04121; NID:g46626; PIDN:CAA27733.1; PID:g581568 !'##experimental_source strain PC-1 REFERENCE A90289 !$#authors Ambler, R.P. !$#journal Biochem. J. (1975) 151:197-218 !$#title The amino acid sequence of Staphylococcus aureus !1penicillinase. !$#cross-references MUID:76135454; PMID:1218078 !$#accession A90289 !'##molecule_type protein !'##residues 25-281 ##label AMB !'##experimental_source strain PC-1 REFERENCE S06757 !$#authors Gillespie, M.T.; Skurray, R.A. !$#journal Nucleic Acids Res. (1989) 17:8854 !$#title Nucleotide sequence of the blaZ gene of the Staphylococcus !1aureus beta-lactamase transposon Tn4002. !$#cross-references MUID:90067850; PMID:2555777 !$#accession S06757 !'##molecule_type DNA !'##residues 1-281 ##label GIL !'##cross-references EMBL:X16471; NID:g46761; PIDN:CAA34491.1; !1PID:g581591 REFERENCE A45789 !$#authors East, A.K.; Dyke, K.G.H. !$#journal J. Gen. Microbiol. (1989) 135:1001-1015 !$#title Cloning and sequence determination of six Staphylococcus !1aureus beta-lactamases and their expression in Escherichia !1coli and Staphylococcus aureus. !$#cross-references MUID:90095428; PMID:2689591 !$#accession A45789 !'##status preliminary !'##molecule_type DNA !'##residues 1-281 ##label EAS !'##cross-references GB:M25252; NID:g341307; PIDN:AAA26642.1; !1PID:g537336 !'##experimental_source strain PC-1 !'##note in the authors' translation residues 20-21 are omitted !$#accession B45789 !'##status preliminary !'##molecule_type DNA !'##residues 1-8,'A',10-21,'P',23-25,'K',27-76,'I',78-85,'I',87-111,'E', !1113-216,'S',218-219,'C',221-281 ##label EA4 !'##cross-references GB:M25254; NID:g341309; PIDN:AAA26644.1; !1PID:g537338 !'##experimental_source strain pI1071 !'##note in the authors' translation residues 20-21 are omitted !$#accession D45789 !'##status preliminary !'##molecule_type DNA !'##residues 1-8,'A',10-19,22-85,'I',87-106,'A',108-111,'E',113-118,'A', !1120-216,'S',218-219,'C',221-281 ##label EA5 !'##cross-references GB:M25257 !'##experimental_source strain pUB101 !$#accession C45789 !'##status preliminary !'##molecule_type DNA !'##residues 1-9,'M',11-106,'A',108-109 ##label EA3 !'##cross-references GB:M25256; NID:g341311; PIDN:AAA26646.1; !1PID:g537340 !'##experimental_source strain pII3804 !'##note in the authors' translation residues 20-21 are omitted REFERENCE S11779 !$#authors Rowland, S.J.; Dyke, K.G.H. !$#journal Mol. Microbiol. (1990) 4:961-975 !$#title Tn552, a novel transposable element from Staphylococcus !1aureus. !$#cross-references MUID:91014696; PMID:2170815 !$#accession S11784 !'##molecule_type DNA !'##residues 1-281 ##label ROW !'##cross-references EMBL:X52734; NID:g46754; PIDN:CAA36953.1; !1PID:g581590 !'##experimental_source transposable element Tn552 REFERENCE A60992 !$#authors East, A.K.; Curnock, S.P.; Dyke, K.G.H. !$#journal FEMS Microbiol. Lett. (1990) 69:249-254 !$#title Change of a single amino acid in the leader peptide of a !1staphylococcal beta-lactamase prevents the appearance of the !1enzyme in the medium. !$#accession A60992 !'##molecule_type DNA !'##residues 1-9,'M',11-106,'A',108-192,'K',194-195,'N',197-201,'IF', !1204-206,'N',208-281 ##label EA2 !'##experimental_source strain 3804 GENETICS !$#gene blaZ !$#start_codon TTG CLASSIFICATION #superfamily beta-lactamase I KEYWORDS antibiotic resistance; extracellular protein; hydrolase FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-281 #product beta-lactamase #status experimental #label !8MAT\ !$63 #active_site Ser #status predicted SUMMARY #length 281 #molecular-weight 31349 #checksum 2867 SEQUENCE /// ENTRY PNBSL #type complete TITLE beta-lactamase (EC 3.5.2.6) precursor - Bacillus licheniformis ALTERNATE_NAMES exopenicillinase CONTAINS large beta-lactamase; small beta-lactamase ORGANISM #formal_name Bacillus licheniformis DATE 29-Jul-1981 #sequence_revision 29-Jul-1981 #text_change 18-Jun-1999 ACCESSIONS A93727; A91488; A90244; A28183; A01003; S31043 REFERENCE A93727 !$#authors Neugebauer, K.; Sprengel, R.; Schaller, H. !$#journal Nucleic Acids Res. (1981) 9:2577-2588 !$#title Penicillinase from Bacillus licheniformis: nucleotide !1sequence of the gene and implications for the biosynthesis !1of a secretory protein in a gram-positive bacterium. !$#cross-references MUID:82014856; PMID:6269055 !$#accession A93727 !'##molecule_type DNA !'##residues 1-307 ##label NEU !'##cross-references GB:V00093; GB:J01544; GB:J01545; NID:g39574; !1PIDN:CAA23431.1; PID:g39575 !'##experimental_source strain 749/C REFERENCE A91488 !$#authors Kroyer, J.; Chang, S. !$#journal Gene (1981) 15:343-347 !$#title The promoter-proximal region of the Bacillus licheniformis !1penicillinase gene: nucleotide sequence and predicted leader !1peptide sequence. !$#cross-references MUID:82140109; PMID:6977472 !$#accession A91488 !'##molecule_type DNA !'##residues 1-72 ##label KRO !'##experimental_source strain 749/C REFERENCE A90244 !$#authors Meadway, R.J. !$#journal Biochem. J. (1969) 115:12-13 !$#title The amino acid sequence of penicillinase from Bacillus !1licheniformis. !$#accession A90244 !'##molecule_type protein !'##residues 43-307 ##label MEA REFERENCE A90439 !$#authors Izui, K.; Nielsen, J.B.K.; Caulfield, M.P.; Lampen, J.O. !$#journal Biochemistry (1980) 19:1882-1886 !$#title Large exopenicillinase, initial extracellular form detected !1in cultures of Bacillus licheniformis. !$#cross-references MUID:80198329; PMID:6966510 !$#contents annotation; confirmation of amino ends of large and small !1exopenicillinase REFERENCE A28183 !$#authors Wittman, V.; Wong, H.C. !$#journal J. Bacteriol. (1988) 170:3206-3212 !$#title Regulation of the penicillinase genes of Bacillus !1licheniformis: interaction of the pen repressor with its !1operators. !$#cross-references MUID:88257041; PMID:3260234 !$#accession A28183 !'##molecule_type DNA !'##residues 1-15 ##label WIT !'##cross-references GB:M21337; NID:g143295; PIDN:AAA22649.1; !1PID:g143296 !'##experimental_source strain 749/C COMMENT Large beta-lactamase is the primary secretion product; it !1can be converted to small beta-lactamase. CLASSIFICATION #superfamily beta-lactamase I KEYWORDS antibiotic resistance; extracellular protein; hydrolase FEATURE !$1-34 #domain signal sequence #status predicted #label SIG\ !$35-307 #product large beta-lactamase #status predicted !8#label MATL\ !$43-307 #product small beta-lactamase #status predicted !8#label MATS\ !$86 #active_site Ser #status predicted SUMMARY #length 307 #molecular-weight 33995 #checksum 2919 SEQUENCE /// ENTRY PNBSU #type complete TITLE beta-lactamase (EC 3.5.2.6) I precursor - Bacillus cereus ALTERNATE_NAMES penicillinase I ORGANISM #formal_name Bacillus cereus DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 18-Jun-1999 ACCESSIONS A01004 REFERENCE A01004 !$#authors Sloma, A.; Gross, M. !$#journal Nucleic Acids Res. (1983) 11:4997-5004 !$#title Molecular cloning and nucleotide sequence of the type I !1beta-lactamase gene from Bacillus cereus. !$#cross-references MUID:83272946; PMID:6308567 !$#accession A01004 !'##molecule_type DNA !'##residues 1-306 ##label SLO !'##cross-references GB:X01602; GB:M12608; NID:g39433; PIDN:CAA25753.1; !1PID:g39434 COMMENT beta-Lactamases are enzymes having varying specificities for !1hydrolyzing beta-lactams; some act more rapidly on !1penicillins, some more rapidly on cephalosporins. In B. !1cereus, two types are found. CLASSIFICATION #superfamily beta-lactamase I KEYWORDS antibiotic resistance; glycoprotein; hydrolase; membrane !1protein FEATURE !$1-29 #domain signal sequence #status predicted #label SIG\ !$30-306 #product beta-lactamase I #status predicted #label !8MAT\ !$91 #active_site Ser #status predicted SUMMARY #length 306 #molecular-weight 33322 #checksum 2943 SEQUENCE /// ENTRY PNBS5B #type complete TITLE beta-lactamase (EC 3.5.2.6) I precursor - Bacillus cereus (strain 5/B) ALTERNATE_NAMES penicillinase I ORGANISM #formal_name Bacillus cereus DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 18-Jun-1999 ACCESSIONS A23097; B23097 REFERENCE A23097 !$#authors Wang, W.; Mezes, P.S.F.; Yang, Y.Q.; Blacher, R.W.; Lampen, !1J.O. !$#journal J. Bacteriol. (1985) 163:487-492 !$#title Cloning and sequencing of the beta-lactamase I gene of !1Bacillus cereus 5/B and its expression in Bacillus subtilis. !$#cross-references MUID:85261055; PMID:2991192 !$#accession A23097 !'##molecule_type DNA !'##residues 1-306 ##label WAN !'##cross-references GB:M12607; NID:g143345; PIDN:AAA22668.1; !1PID:g551722 !$#accession B23097 !'##molecule_type protein !'##residues 44-63 ##label WAN2 COMMENT This secreted enzyme is a class A beta-lactamase and !1preferentially acts on penicillins. GENETICS !$#gene penPC !$#start_codon TTG CLASSIFICATION #superfamily beta-lactamase I KEYWORDS antibiotic resistance; extracellular protein; hydrolase FEATURE !$1-43 #domain signal sequence #status predicted #label SIG\ !$44-306 #product beta-lactamase I #status predicted #label !8BL1\ !$89 #active_site Ser #status predicted SUMMARY #length 306 #molecular-weight 33596 #checksum 4118 SEQUENCE /// ENTRY PNBSLC #type complete TITLE beta-lactamase (EC 3.5.2.6) III precursor - Bacillus cereus ALTERNATE_NAMES penicillinase III ORGANISM #formal_name Bacillus cereus DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 12-Apr-1996 ACCESSIONS A27755 REFERENCE A27755 !$#authors Hussain, M.; Pastor, F.I.J.; Lampen, J.O. !$#journal J. Bacteriol. (1987) 169:579-586 !$#title Cloning and sequencing of the blaZ gene encoding !1beta-lactamase III, a lipoprotein of Bacillus cereus 569/H. !$#cross-references MUID:87109042; PMID:3027036 !$#accession A27755 !'##molecule_type DNA !'##residues 1-316 ##label HSN !'##experimental_source strain 569/H COMMENT This membrane-bound enzyme resembles several gram-positive !1class A beta-lactamases in having both membrane-bound and !1secreted forms that differ only at their amino ends. COMMENT This enzyme is an acyl-glyceride thioether-linked !1lipoprotein with the hydrophobic moiety functioning to !1anchor the protein in the membrane lipid bilayer. GENETICS !$#gene blaZ CLASSIFICATION #superfamily beta-lactamase I KEYWORDS antibiotic resistance; hydrolase; lipoprotein; membrane !1protein; penicillin resistance FEATURE !$1-29 #domain signal sequence #status predicted #label SIG\ !$30-316 #product beta-lactamase III #status predicted #label !8MAT\ !$95 #active_site Ser #status predicted SUMMARY #length 316 #molecular-weight 35041 #checksum 9967 SEQUENCE /// ENTRY PNSM1U #type complete TITLE beta-lactamase (EC 3.5.2.6) precursor - Streptomyces albus ALTERNATE_NAMES penicillinase ORGANISM #formal_name Streptomyces albus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 18-Jun-1999 ACCESSIONS S00057; S18494; S01468 REFERENCE S00057 !$#authors Dehottay, P.; Dusart, J.; de Meester, F.; Joris, B.; van !1Beeumen, J.; Erpicum, T.; Frere, J.M.; Ghuysen, J.M. !$#journal Eur. J. Biochem. (1987) 166:345-350 !$#title Nucleotide sequence of the gene encoding the Streptomyces !1albus G beta-lactamase precursor. !$#cross-references MUID:87275916; PMID:3038538 !$#accession S00057 !'##molecule_type DNA !'##residues 1-314 ##label DEH !'##cross-references EMBL:M28303; NID:g153338; PIDN:AAA26775.1; !1PID:g153339 !'##experimental_source strain G; plasmid pDML6 !'##note the authors translated the initiation codon GTG for residue 1 !1as Val !$#accession S18494 !'##molecule_type protein !'##residues 40-55;187-209 ##label DEH2 REFERENCE S01468 !$#authors de Meester, F.; Joris, B.; Lenzini, M.V.; Dehottay, P.; !1Erpicium, T.; Dusart, J.; Klein, D.; Ghuysen, J.M.; Frere, !1J.M.; van Beeumen, J. !$#journal Biochem. J. (1987) 244:427-432 !$#title The active sites of the beta-lactamases of Streptomyces !1cacaoi and Streptomyces albus G. !$#cross-references MUID:88024011; PMID:2822004 !$#accession S01468 !'##molecule_type protein !'##residues 81-92 ##label DEM !'##experimental_source strain G; cloned gene from plasmid pDML6 !1overexpressed in Streptomyces lividans COMMENT This is a class A beta-lactamase. GENETICS !$#start_codon GTG CLASSIFICATION #superfamily beta-lactamase I KEYWORDS antibiotic resistance; extracellular protein; hydrolase FEATURE !$1-39 #domain signal sequence #status predicted #label SIG\ !$40-314 #product beta-lactamase #status experimental #label !8MAT\ !$89 #active_site Ser #status experimental SUMMARY #length 314 #molecular-weight 33265 #checksum 9207 SEQUENCE /// ENTRY C45822 #type complete TITLE beta-lactamase (EC 3.5.2.6) precursor - Streptomyces lavendulae ORGANISM #formal_name Streptomyces lavendulae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C45822 REFERENCE A45822 !$#authors Forsman, M.; Haeggstroem, B.; Lindgren, L.; Jaurin, B. !$#journal J. Gen. Microbiol. (1990) 136:589-598 !$#title Molecular analysis of beta-lactamases from four species of !1Streptomyces: comparison of amino acid sequences with those !1of other beta-lactamases. !$#cross-references MUID:90362045; PMID:2391494 !$#accession C45822 !'##status preliminary !'##molecule_type DNA !'##residues 1-305 ##label FOR !'##cross-references GB:M34180; NID:g153184; PIDN:AAA26708.1; !1PID:g153185 CLASSIFICATION #superfamily beta-lactamase I KEYWORDS hydrolase SUMMARY #length 305 #molecular-weight 32353 #checksum 2722 SEQUENCE /// ENTRY B45822 #type complete TITLE beta-lactamase (EC 3.5.2.6) precursor - Streptomyces fradiae ORGANISM #formal_name Streptomyces fradiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B45822; PC1180 REFERENCE A45822 !$#authors Forsman, M.; Haeggstroem, B.; Lindgren, L.; Jaurin, B. !$#journal J. Gen. Microbiol. (1990) 136:589-598 !$#title Molecular analysis of beta-lactamases from four species of !1Streptomyces: comparison of amino acid sequences with those !1of other beta-lactamases. !$#cross-references MUID:90362045; PMID:2391494 !$#accession B45822 !'##status preliminary !'##molecule_type DNA !'##residues 1-306 ##label FOR !'##cross-references GB:M34179; NID:g153186; PIDN:AAA26709.1; !1PID:g153187 REFERENCE PC1180 !$#authors Forsman, M.; Granstroem, M. !$#journal Gene (1992) 121:87-94 !$#title Mutagenic analysis of the promoter of the Streptomyces !1fradiae beta-lactamase-encoding gene. !$#cross-references MUID:93051366; PMID:1385267 !$#accession PC1180 !'##molecule_type DNA !'##residues 1-40 ##label FO2 !'##cross-references GB:M94255; NID:g153188; PIDN:AAC41397.1; !1PID:g153189 !'##note the authors translated the initiation codon GTG for residue 1 !1as Val GENETICS !$#start_codon GTG CLASSIFICATION #superfamily beta-lactamase I KEYWORDS hydrolase SUMMARY #length 306 #molecular-weight 32931 #checksum 5498 SEQUENCE /// ENTRY S02714 #type complete TITLE beta-lactamase (EC 3.5.2.6) precursor - Streptomyces aureofaciens ORGANISM #formal_name Streptomyces aureofaciens DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S02714 REFERENCE S02714 !$#authors Reynes, J.P.; Drocourt, D.; Tiraby, G. !$#submission submitted to the EMBL Data Library, November 1988 !$#accession S02714 !'##molecule_type DNA !'##residues 1-311 ##label REY !'##cross-references EMBL:X13597; NID:g46527; PIDN:CAA31933.1; !1PID:g581548 GENETICS !$#gene bla !$#start_codon GTG CLASSIFICATION #superfamily beta-lactamase I KEYWORDS antibiotic resistance; hydrolase FEATURE !$1-31 #domain signal sequence #status predicted #label SIG\ !$32-311 #product beta-lactamase #status predicted #label MAT SUMMARY #length 311 #molecular-weight 32486 #checksum 461 SEQUENCE /// ENTRY PNECP #type complete TITLE beta-lactamase (EC 3.5.2.6) precursor - Escherichia coli plasmids ALTERNATE_NAMES beta-lactamase TEM-6 (for blaT-6 DNA); penicillinase ORGANISM #formal_name Escherichia coli DATE 30-Nov-1980 #sequence_revision 01-Sep-1981 #text_change 21-Jul-2000 ACCESSIONS A93821; A93820; A35387; S24415; A01005 REFERENCE A93821 !$#authors Sutcliffe, J.G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1978) 75:3737-3741 !$#title Nucleotide sequence of the ampicillin resistance gene of !1Escherichia coli plasmid pBR322. !$#cross-references MUID:79012484; PMID:358200 !$#accession A93821 !'##molecule_type DNA !'##residues 1-286 ##label SUT !'##cross-references GB:V00613; GB:J01832; NID:g43710; PIDN:CAA23886.1; !1PID:g43713 !'##experimental_source plasmid pBR322 REFERENCE A93820 !$#authors Ambler, R.P.; Scott, G.K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1978) 75:3732-3736 !$#title Partial amino acid sequence of penicillinase coded by !1Escherichia coli plasmid R6K. !$#cross-references MUID:79012483; PMID:358199 !$#accession A93820 !'##molecule_type protein !'##residues 24-36,'K',38-286 ##label AMB !'##experimental_source plasmid R6K REFERENCE A35387 !$#authors Kornacki, J.A.; Burlage, R.S.; Figurski, D.H. !$#journal J. Bacteriol. (1990) 172:3040-3050 !$#title The kil-kor regulon of broad-host-range plasmid RK2: !1nucleotide sequence, polypeptide product, and expression of !1regulatory gene korC. !$#cross-references MUID:90264294; PMID:2160936 !$#accession A35387 !'##molecule_type DNA !'##residues 182-286 ##label KOR !'##cross-references GB:M32794; NID:g152521; PIDN:AAA26408.1; !1PID:g152522 !'##experimental_source PK2 REFERENCE S24415 !$#authors Goussard, S.; Sougakoff, W.; Mabilat, C.; Bauernfeind, A.; !1Courvalin, P. !$#journal J. Gen. Microbiol. (1991) 137:2681-2687 !$#title An IS1-like element is responsible for high-level synthesis !1of extended-spectrum beta-lactamase TEM-6 in !1Enterobacteriaceae. !$#cross-references MUID:92166702; PMID:1665171 !$#accession S24415 !'##status translation not shown !'##molecule_type DNA !'##residues 1-101,'K',103-161,'H',163-286 ##label GOU !'##cross-references EMBL:X57972; NID:g41816; PIDN:CAA41038.1; !1PID:g41817 !'##experimental_source ISI-like blaT-6 DNA REFERENCE A90923 !$#authors Sutcliffe, J.G. !$#journal Cold Spring Harb. Symp. Quant. Biol. (1979) 43:77-90 !$#title Complete nucleotide sequence of the Escherichia coli plasmid !1pBR322. !$#cross-references MUID:80002802; PMID:383387 !$#contents annotation COMMENT Like most penicillinases from gram-negative bacteria, this !1enzyme, coded by a resistance transfer plasmid, is !1noninducible and cell-bound. GENETICS !$#genome plasmid CLASSIFICATION #superfamily beta-lactamase I KEYWORDS antibiotic resistance; hydrolase; membrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-286 #product beta-lactamase #status experimental #label !8MAT\ !$68 #active_site Ser #status predicted\ !$75-121 #disulfide_bonds #status predicted SUMMARY #length 286 #molecular-weight 31515 #checksum 5209 SEQUENCE /// ENTRY A44996 #type complete TITLE beta-lactamase (EC 3.5.2.6) shv-1 precursor - Klebsiella sp. plasmid R974 ORGANISM #formal_name Klebsiella sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A44996 REFERENCE A44996 !$#authors Mercier, J.; Levesque, R.C. !$#journal Antimicrob. Agents Chemother. (1990) 34:1577-1583 !$#title Cloning of SHV-2, OHIO-1, and OXA-6 beta-lactamases and !1cloning and sequencing of SHV-1 beta-lactamase. !$#cross-references MUID:91024126; PMID:2221867 !$#accession A44996 !'##status preliminary !'##molecule_type DNA !'##residues 1-287 ##label MER !'##cross-references GB:M59181; NID:g151860; PIDN:AAA26087.1; !1PID:g151861 GENETICS !$#genome plasmid CLASSIFICATION #superfamily beta-lactamase I KEYWORDS hydrolase SUMMARY #length 287 #molecular-weight 31374 #checksum 416 SEQUENCE /// ENTRY A44998 #type complete TITLE beta-lactamase (EC 3.5.2.6) SHV-2 - Klebsiella ozaenae plasmid pBP60 ORGANISM #formal_name Klebsiella ozaenae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A44998; S12703 REFERENCE A44998 !$#authors Huletsky, A.; Couture, F.; Levesque, R.C. !$#journal Antimicrob. Agents Chemother. (1990) 34:1725-1732 !$#title Nucleotide sequence and phylogeny of SHV-2 beta-lactamase. !$#cross-references MUID:91136192; PMID:2285285 !$#accession A44998 !'##status preliminary !'##molecule_type DNA !'##residues 1-286 ##label HUL !'##cross-references GB:M95179; NID:g150488; PIDN:AAA25526.1; !1PID:g150489 REFERENCE S12703 !$#authors Podbielski, A.; Melzer, B. !$#journal Nucleic Acids Res. (1990) 18:4916 !$#title Nucleotide sequence of the gene encoding the SHV-2 !1beta-lactamase (bla(SHV-2)) of Klebsiella ozaenae. !$#cross-references MUID:90370479; PMID:2395654 !$#accession S12703 !'##status translation not shown !'##molecule_type DNA !'##residues 1-286 ##label POD !'##cross-references EMBL:X53433; NID:g43789; PIDN:CAA37524.1; !1PID:g43790 GENETICS !$#genome plasmid CLASSIFICATION #superfamily beta-lactamase I KEYWORDS antibiotic resistance; hydrolase SUMMARY #length 286 #molecular-weight 31254 #checksum 8808 SEQUENCE /// ENTRY A44958 #type complete TITLE beta-lactamase (EC 3.5.2.6) (OHIO-1) - Enterobacter cloacae plasmid pDS075 ORGANISM #formal_name Enterobacter cloacae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A44958 REFERENCE A44958 !$#authors Shlaes, D.M.; Currie-McCumber, C.; Hull, A.; Behlau, I.; !1Kron, M. !$#journal Antimicrob. Agents Chemother. (1990) 34:1570-1576 !$#title OHIO-1 beta-lactamase is part of the SHV-1 family. !$#cross-references MUID:91024125; PMID:2121093 !$#accession A44958 !'##status preliminary !'##molecule_type DNA !'##residues 1-286 ##label SHL !'##cross-references EMBL:M33655; NID:g148354; PIDN:AAA72078.1; !1PID:g148355 !'##note the authors translated the codon CGT for residue 215 as Pro GENETICS !$#genome plasmid CLASSIFICATION #superfamily beta-lactamase I KEYWORDS hydrolase SUMMARY #length 286 #molecular-weight 31354 #checksum 8418 SEQUENCE /// ENTRY PNBSU2 #type complete TITLE beta-lactamase (EC 3.5.2.6) II precursor - Bacillus cereus ALTERNATE_NAMES cephalosporinase II; penicillinase II ORGANISM #formal_name Bacillus cereus DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 18-Jun-1999 ACCESSIONS A91806; A91344; A01006 REFERENCE A91806 !$#authors Hussain, M.; Carlino, A.; Madonna, M.J.; Lampen, J.O. !$#journal J. Bacteriol. (1985) 164:223-229 !$#title Cloning and sequencing of the metallothioprotein !1beta-lactamase II gene of Bacillus cereus 569/H in !1Escherichia coli. !$#cross-references MUID:86008056; PMID:3930467 !$#accession A91806 !'##molecule_type DNA !'##residues 1-257 ##label HUS !'##cross-references GB:M11189; NID:g142603; PIDN:AAA22276.1; !1PID:g142604 !'##experimental_source strain 569/H REFERENCE A91344 !$#authors Ambler, R.P.; Daniel, M.; Fleming, J.; Hermoso, J.M.; Pang, !1C.; Waley, S.G. !$#journal FEBS Lett. (1985) 189:207-211 !$#title The amino acid sequence of the zinc-requiring beta-lactamase !1II from the bacterium Bacillus cereus 569. !$#cross-references MUID:86005446; PMID:3930290 !$#accession A91344 !'##molecule_type protein !'##residues 31-183;187-210;214-257 ##label AMB !'##experimental_source strain 569/H/9 COMMENT beta-Lactamase II from Bacillus spp. and beta-lactamase L-1 !1from Pseudomonas maltophilia are classified together as !1class B beta-lactamases, which hydrolyze cephalosporins and !1penicillins. COMMENT beta-Lactamase II binds two Zn(II) ions per molecule. Zinc !1at the higher affinity site is necessary for activity of the !1enzyme. Zinc at the lower affinity site (not specified) !1increases hydrolysis of cephalosporin C but not of !1benzylpenicillin. CLASSIFICATION #superfamily beta-lactamase II KEYWORDS antibiotic resistance; hydrolase; metalloprotein; zinc FEATURE !$1-30 #domain signal sequence #status predicted #label SIG\ !$31-257 #product beta-lactamase II #status experimental !8#label MPT\ !$67 #active_site Glu #status predicted\ !$116,118,198,240 #binding_site zinc, high affinity (His, His, Cys, !8His) #status experimental SUMMARY #length 257 #molecular-weight 28092 #checksum 2889 SEQUENCE /// ENTRY PNBS2S #type complete TITLE beta-lactamase (EC 3.5.2.6) II precursor - Bacillus sp. ALTERNATE_NAMES penicillinase II ORGANISM #formal_name Bacillus sp. DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 18-Jun-1999 ACCESSIONS A24393; B24393 REFERENCE A24393 !$#authors Kato, C.; Kudo, T.; Watanabe, K.; Horikoshi, K. !$#journal J. Gen. Microbiol. (1985) 131:3317-3324 !$#title Nucleotide sequence of the beta-lactamase gene of !1alkalophilic Bacillus sp. strain 170. !$#cross-references MUID:86170399; PMID:3938474 !$#accession A24393 !'##molecule_type DNA !'##residues 1-257 ##label KAT !'##cross-references GB:M15350; NID:g142601; PIDN:AAA22275.1; !1PID:g142602 !'##experimental_source strain 170 !$#accession B24393 !'##molecule_type protein !'##residues 31-48 ##label KAT2 CLASSIFICATION #superfamily beta-lactamase II KEYWORDS antibiotic resistance; hydrolase; metalloprotein; zinc FEATURE !$1-30 #domain signal sequence #status predicted #label SIG\ !$31-257 #product beta-lactamase II #status predicted #label !8BL2\ !$67 #active_site Glu #status predicted\ !$116,118,198,240 #binding_site zinc, high affinity (His, His, Cys, !8His) #status predicted SUMMARY #length 257 #molecular-weight 28153 #checksum 2375 SEQUENCE /// ENTRY QKEC #type complete TITLE beta-lactamase (EC 3.5.2.6) precursor - Escherichia coli (strain K-12) ALTERNATE_NAMES cephalosporinase ORGANISM #formal_name Escherichia coli DATE 02-Apr-1982 #sequence_revision 02-Apr-1982 #text_change 01-Mar-2002 ACCESSIONS A01007; S56378; A21197; I41132; D65225 REFERENCE A01007 !$#authors Jaurin, B.; Grundstrom, T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:4897-4901 !$#title ampC cephalosporinase of Escherichia coli K-12 has a !1different evolutionary origin from that of beta-lactamases !1of the penicillinase type. !$#cross-references MUID:82060161; PMID:6795623 !$#accession A01007 !'##molecule_type DNA !'##residues 1-377 ##label JAU !'##cross-references GB:J01611; GB:J01583; NID:g145261; PIDN:AAA23441.1; !1PID:g145267 !'##experimental_source strain K12 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56378 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-377 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97049.1; !1PID:g536994 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A21197 !$#authors Olsson, O.; Bergstroem, S.; Lindberg, F.P.; Normark, S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:7556-7560 !$#title ampC beta-lactamase hyperproduction in Escherichia coli: !1natural ampicillin resistance generated by horizontal !1chromosomal DNA transfer from Shigella. !$#cross-references MUID:84170267; PMID:6369321 !$#accession A21197 !'##status preliminary !'##molecule_type DNA !'##residues 1-21;22,40-54;74-90 ##label OLS REFERENCE I41132 !$#authors Olsson, O.; Bergstrom, S.; Normark, S. !$#journal EMBO J. (1982) 1:1411-1416 !$#title Identification of a novel ampC beta-lactamase promoter in a !1clinical isolate of Escherichia coli. !$#cross-references MUID:84207893; PMID:6765197 !$#accession I41132 !'##status preliminary !'##molecule_type DNA !'##residues 1-6 ##label RES !'##cross-references GB:M24174; NID:g145259; PIDN:AAA23435.1; !1PID:g145260 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65225 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-377 ##label BLAT !'##cross-references GB:AE000487; GB:U00096; NID:g1790582; !1PIDN:AAC77110.1; PID:g1790593; UWGP:b4150 !'##experimental_source strain K-12, substrain MG1655 COMMENT This protein is a serine beta-lactamase with a substrate !1specificity for cephalosporins that shows no sequence !1homologies to serine penicillinase or serine D-alanine !1carboxypeptidase. GENETICS !$#gene ampC !$#map_position 93.8 min CLASSIFICATION #superfamily Escherichia coli beta-lactamase KEYWORDS antibiotic resistance; hydrolase FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-377 #product beta-lactamase #status predicted #label MAT\ !$80 #active_site Ser #status experimental SUMMARY #length 377 #molecular-weight 41555 #checksum 4142 SEQUENCE /// ENTRY PNKBM #type complete TITLE beta-lactamase (EC 3.5.2.6) precursor - Enterobacter cloacae (strain MNH1) ALTERNATE_NAMES cephalosporinase ORGANISM #formal_name Enterobacter cloacae DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 30-Jun-1993 ACCESSIONS S00406 REFERENCE S00404 !$#authors Galleni, M.; Lindberg, F.; Normark, S.; Cole, S.; Honore, !1N.; Joris, B.; Frere, J.M. !$#journal Biochem. J. (1988) 250:753-760 !$#title Sequence and comparative analysis of three Enterobacter !1cloacae ampC beta-lactamase genes and their products. !$#cross-references MUID:88268750; PMID:3260487 !$#accession S00406 !'##molecule_type DNA !'##residues 1-381 ##label GAL !'##cross-references EMBL:X08082 COMMENT This protein is a class C beta-lactamase. GENETICS !$#gene ampC CLASSIFICATION #superfamily Escherichia coli beta-lactamase KEYWORDS antibiotic resistance; hydrolase FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-381 #product beta-lactamase #status predicted #label MAT\ !$84 #active_site Ser #status predicted SUMMARY #length 381 #molecular-weight 41286 #checksum 1311 SEQUENCE /// ENTRY PNKBQ #type fragment TITLE beta-lactamase (EC 3.5.2.6) precursor - Enterobacter cloacae (strain Q908R) (fragment) ALTERNATE_NAMES cephalosporinase ORGANISM #formal_name Enterobacter cloacae DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 18-Jun-1999 ACCESSIONS S00405 REFERENCE S00404 !$#authors Galleni, M.; Lindberg, F.; Normark, S.; Cole, S.; Honore, !1N.; Joris, B.; Frere, J.M. !$#journal Biochem. J. (1988) 250:753-760 !$#title Sequence and comparative analysis of three Enterobacter !1cloacae ampC beta-lactamase genes and their products. !$#cross-references MUID:88268750; PMID:3260487 !$#accession S00405 !'##molecule_type DNA !'##residues 1-375 ##label GAL !'##cross-references EMBL:X08081; NID:g42611; PIDN:CAA30878.1; !1PID:g757841 !'##note parts of this sequence, including the amino and carboxyl ends !1of the mature protein, were confirmed by protein sequencing COMMENT This protein is a class C beta-lactamase. GENETICS !$#gene ampC CLASSIFICATION #superfamily Escherichia coli beta-lactamase KEYWORDS antibiotic resistance; hydrolase FEATURE !$1-14 #domain signal sequence (fragment) #status predicted !8#label SIG\ !$15-375 #product beta-lactamase #status experimental #label !8MAT\ !$78 #active_site Ser #status predicted SUMMARY #length 375 #checksum 9705 SEQUENCE /// ENTRY PNKBP #type complete TITLE beta-lactamase (EC 3.5.2.6) precursor - Enterobacter cloacae (strain P99) ALTERNATE_NAMES cephalosporinase ORGANISM #formal_name Enterobacter cloacae DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 18-Jun-1999 ACCESSIONS S00404 REFERENCE S00404 !$#authors Galleni, M.; Lindberg, F.; Normark, S.; Cole, S.; Honore, !1N.; Joris, B.; Frere, J.M. !$#journal Biochem. J. (1988) 250:753-760 !$#title Sequence and comparative analysis of three Enterobacter !1cloacae ampC beta-lactamase genes and their products. !$#cross-references MUID:88268750; PMID:3260487 !$#accession S00404 !'##molecule_type DNA !'##residues 1-381 ##label GAL !'##cross-references EMBL:X07274; NID:g42260; PIDN:CAA30257.1; !1PID:g42261 !'##note part of this sequence, including the carboxyl end of the mature !1protein, was confirmed by protein sequencing COMMENT This protein is a class C beta-lactamase. GENETICS !$#gene ampC CLASSIFICATION #superfamily Escherichia coli beta-lactamase KEYWORDS antibiotic resistance; hydrolase FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-381 #product beta-lactamase #status experimental #label !8MAT\ !$84 #active_site Ser #status predicted SUMMARY #length 381 #molecular-weight 41301 #checksum 735 SEQUENCE /// ENTRY QKSE #type complete TITLE beta-lactamase (EC 3.5.2.6) precursor - Serratia marcescens ORGANISM #formal_name Serratia marcescens DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 18-Jun-1999 ACCESSIONS A48176; S11710 REFERENCE A48176 !$#authors Nomura, K.; Yoshida, T. !$#journal FEMS Microbiol. Lett. (1990) 70:295-300 !$#title Nucleotide sequence of the Serratia marcescens SR50 !1chromosomal ampC beta-lactamase gene. !$#accession A48176 !'##molecule_type DNA !'##residues 1-376 ##label NOM !'##cross-references EMBL:X52964; NID:g47223; PIDN:CAA37137.1; !1PID:g47224 !'##note submitted to the EMBL Data Library, May 1990 !'##note the authors translated the codon GTA for residue 258 as Asp GENETICS !$#gene ampC CLASSIFICATION #superfamily Escherichia coli beta-lactamase KEYWORDS antibiotic resistance; hydrolase FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-376 #product beta-lactamase #status predicted #label MAT\ !$79 #active_site Ser #status predicted SUMMARY #length 376 #molecular-weight 41096 #checksum 107 SEQUENCE /// ENTRY S48220 #type complete TITLE serine-type D-Ala-D-Ala carboxypeptidase (EC 3.4.16.4) precursor - Streptomyces sp. ALTERNATE_NAMES D-alanyl-D-alanine carboxypeptidase; DD-peptidase ORGANISM #formal_name Streptomyces sp. DATE 15-Jul-1995 #sequence_revision 11-Apr-1997 #text_change 18-Jun-1999 ACCESSIONS S48220; S00765; S11947 REFERENCE S48220 !$#authors Duez, C.; Piron-Fraipont, C.; Joris, B.; Dusart, J.; Urdea, !1M.S.; Martial, J.A.; Frere, J.M.; Ghuysen, J.M. !$#journal Eur. J. Biochem. (1994) 224:1079 !$#title Correction. Primary structure of the Streptomyces R61 !1extracellular DD-peptidase. 1. Cloning into Streptomyces !1lividans and nucleotide sequence of the gene. !$#cross-references MUID:95010068; PMID:7925404 !$#accession S48220 !'##molecule_type DNA !'##residues 1-406 ##label DUE1 !'##cross-references GB:M26842; NID:g153447; PIDN:AAA62239.1; !1PID:g153448 !'##note correction to sequence S00765 REFERENCE S00765 !$#authors Duez, C.; Piron-Fraipont, C.; Joris, B.; Dusart, J.; Urdea, !1M.S.; Martial, J.A.; Frere, J.M.; Ghuysen, J.M. !$#journal Eur. J. Biochem. (1987) 162:509-518 !$#title Primary structure of the Streptomyces R61 extracellular !1DD-peptidase. 1. Cloning into Streptomyces lividans and !1nucleotide sequence of the gene. !$#cross-references MUID:87161818; PMID:3830154 !$#accession S00765 !'##molecule_type DNA !'##residues 1-266,'TGA',270-346,'QAH',350-380,'GEAAQRDLLGDHRGAP', !1397-406 ##label DUE2 !'##cross-references EMBL:X05109; GB:M26842; NID:g515049 REFERENCE S11947 !$#authors Piron-Fraipont, C.; Lenzini, M.V.; Dusart, J.; Ghuysen, J.M. !$#journal Mol. Gen. Genet. (1990) 223:114-120 !$#title Transcriptional analysis of the DD-peptidase/ !1penicillin-binding protein-encoding dac gene of Streptomyces !1R61: use of the promoter and signal sequences in a secretion !1vector. !$#cross-references MUID:91080851; PMID:2175384 !$#accession S11947 !'##molecule_type DNA !'##residues 1-91;171-173 ##label PIR !'##cross-references EMBL:X55810; NID:g296314 FUNCTION !$#description catalyzes the hydrolysis of carboxyl-terminal !1D-alanyl-D-alanyl peptide bonds CLASSIFICATION #superfamily Escherichia coli beta-lactamase KEYWORDS hydrolase; serine carboxypeptidase FEATURE !$1-31 #domain signal sequence #status predicted #label SIG\ !$32-380 #product serine-type D-Ala-D-Ala carboxypeptidase !8#status predicted #label MAT\ !$381-406 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$93 #active_site Ser #status predicted SUMMARY #length 406 #molecular-weight 42917 #checksum 9255 SEQUENCE /// ENTRY A42209 #type complete TITLE D-stereospecific aminopeptidase (EC 3.4.11.19) - Ochrobactrum anthropi ORGANISM #formal_name Ochrobactrum anthropi DATE 04-Mar-1993 #sequence_revision 11-Apr-1997 #text_change 01-Feb-2002 ACCESSIONS A42209; A43991 REFERENCE A42209 !$#authors Asano, Y.; Kato, Y.; Yamada, A.; Kondo, K. !$#journal Biochemistry (1992) 31:2316-2328 !$#title Structural similarity of D-aminopeptidase to !1carboxypeptidase DD and beta-lactamases. !$#cross-references MUID:92172855; PMID:1540587 !$#accession A42209 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-520 ##label ASA1 !'##cross-references GB:M84523; DDBJ:J05361; NID:g150442; !1PIDN:AAA25519.1; PID:g150443 !'##experimental_source strain SCRC C1-38 !'##note sequence extracted from NCBI backbone (NCBIP:87140); protein !1data from reference A43991 is also presented !'##note site directed mutagenesis indicates the active site is serine !1rather than cysteine REFERENCE A43991 !$#authors Asano, Y.; Nakazawa, A.; Kato, Y.; Kondo, K. !$#journal J. Biol. Chem. (1989) 264:14233-14239 !$#title Properties of a novel D-stereospecific aminopeptidase from !1Ochrobactrum anthropi. !$#cross-references MUID:89340535; PMID:2760064 !$#accession A43991 !'##molecule_type protein !'##residues 2-13,'XX',16-24,'X',26 ##label ASA2 FUNCTION !$#description catalyzes the hydrolysis of amino-terminal D-amino acids, !1preferentially D-Ala, D-Ser or D-Thr !$#note also hydrolyzes amides and methyl esters of D-amino acids !1and glycine CLASSIFICATION #superfamily D-stereospecific aminopeptidase KEYWORDS aminopeptidase FEATURE !$2-520 #product D-stereospecific aminopeptidase #status !8predicted #label MAT\ !$62 #active_site Ser #status predicted SUMMARY #length 520 #molecular-weight 57391 #checksum 7573 SEQUENCE /// ENTRY PNEBT #type complete TITLE beta-lactamase (EC 3.5.2.6) OXA2 precursor - Salmonella typhimurium plasmids ALTERNATE_NAMES penicillinase ORGANISM #formal_name Salmonella typhimurium DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 18-Jul-2001 ACCESSIONS A91350; S03557; A90325; JQ1755; A45792; D26839; A24008; !1S03852 REFERENCE A91350 !$#authors Dale, J.W.; Godwin, D.; Mossakowska, D.; Stephenson, P.; !1Wall, S. !$#journal FEBS Lett. (1985) 191:39-44 !$#title Sequence of the OXA2 beta-lactamase: comparison with other !1penicillin-reactive enzymes. !$#cross-references MUID:86030657; PMID:3876949 !$#accession A91350 !'##molecule_type DNA !'##residues 1-275 ##label DAL !'##cross-references EMBL:X07260; NID:g47874; PIDN:CAA30246.1; !1PID:g47875 !'##experimental_source plasmid R67 REFERENCE S03557 !$#authors Mossakowska, D.; Ali, N.A.; Dale, J.W. !$#journal Eur. J. Biochem. (1989) 180:309-318 !$#title Oxacillin-hydrolysing beta-lactamases. A comparative !1analysis at nucleotide and amino acid sequence levels. !$#cross-references MUID:89170730; PMID:2538329 !$#accession S03557 !'##molecule_type DNA !'##residues 1-275 ##label MOS !'##cross-references EMBL:X07260; NID:g47874; PIDN:CAA30246.1; !1PID:g47875 REFERENCE A90325 !$#authors Holland, S.; Dale, J.W. !$#journal Biochem. J. (1984) 224:1009-1013 !$#title Improved purification and characterization of the OXA-2 !1beta- lactamase. !$#cross-references MUID:85121787; PMID:6335398 !$#accession A90325 !'##molecule_type protein !'##residues 22-32 ##label HOL !'##experimental_source plasmid R67 REFERENCE JQ1755 !$#authors Stokes, H.W.; Hall, R.M. !$#journal Plasmid (1992) 28:225-234 !$#title The integron in1 in plasmid R46 includes two copies of the !1oxa2 gene cassette. !$#cross-references MUID:93096861; PMID:1334268 !$#accession JQ1755 !'##molecule_type DNA !'##residues 1-275 ##label STO !'##cross-references GB:M95287; NID:g151816; PIDN:AAB59082.1; !1PID:g151818 !'##experimental_source plasmid R67 REFERENCE A45792 !$#authors Nuecken, E.J.; Henschke, R.B.; Schmidt, F.R.J. !$#journal J. Gen. Microbiol. (1989) 135:761-765 !$#title Nucleotide sequence of an OXA-2 beta-lactamase gene from the !1R-plasmid R1767 derived plasmid pBP11 and comparison to !1closely related resistance determinants found in R46 and !1Tn2603. !$#cross-references MUID:90095432; PMID:2689593 !$#accession A45792 !'##status preliminary !'##molecule_type DNA !'##residues 1-275 ##label NUE !'##cross-references GB:M25261; NID:g154221; PIDN:AAA98357.1; !1PID:g154222 !'##experimental_source plasmid R1767 REFERENCE A26839 !$#authors Hall, R.M.; Vockler, C. !$#journal Nucleic Acids Res. (1987) 15:7491-7501 !$#title The region of the IncN plasmid R46 coding for resistance to !1beta-lactam antibiotics, streptomycin/spectinomycin and !1sulphonamides is closely related to antibiotic resistance !1segments found in IncW plasmids and in Tn21-like !1transposons. !$#cross-references MUID:88015610; PMID:2821509 !$#accession D26839 !'##molecule_type DNA !'##residues 1-275 ##label HAL !'##cross-references GB:X06046; NID:g42204; PIDN:CAA29443.1; PID:g42208 !'##experimental_source plasmid R46 !'##note Escherichia coli was used as a host for the R46 plasmid COMMENT This enzyme is found in some clinical isolates of !1gram-negative bacteria resistant to D-aminobenzyl penicillin !1(ampicillin). GENETICS !$#gene bla; OXA2 !$#genome plasmid FUNCTION !$#description a group of enzymes of varying specificity hydrolyzing !1beta-lactams CLASSIFICATION #superfamily beta-lactamase OXA2; beta-lactamase OXA2 !1homology KEYWORDS antibiotic resistance; hydrolase; penicillin resistance FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-275 #product beta-lactamase OXA2 #status predicted #label !8MAT\ !$34-263 #domain beta-lactamase OXA2 homology #label OXA2\ !$72 #active_site Ser #status predicted SUMMARY #length 275 #molecular-weight 31686 #checksum 6389 SEQUENCE /// ENTRY WZBYR #type complete TITLE arginase (EC 3.5.3.1) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein LPH15w; protein YPL111w ORGANISM #formal_name Saccharomyces cerevisiae DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 21-Jul-2000 ACCESSIONS A01008; S62010 REFERENCE A01008 !$#authors Sumrada, R.A.; Cooper, T.G. !$#journal J. Bacteriol. (1984) 160:1078-1087 !$#title Nucleotide sequence of the Saccharomyces cerevisiae arginase !1gene (CAR1) and its transcription under various !1physiological conditions. !$#cross-references MUID:85054621; PMID:6094498 !$#accession A01008 !'##molecule_type DNA !'##residues 1-333 ##label SUM !'##cross-references EMBL:M10110; NID:g171160; PIDN:AAA34469.1; !1PID:g171161 REFERENCE S61996 !$#authors Schlenstedt, G.; Silver, P.A. !$#submission submitted to the EMBL Data Library, December 1995 !$#accession S62010 !'##molecule_type DNA !'##residues 1-333 ##label SCH !'##cross-references EMBL:U43503; NID:g1163087; PIDN:AAB68250.1; !1PID:g1163102; GSPDB:GN00016; MIPS:YPL111w COMMENT This enzyme catalyzes the hydrolysis of arginine to !1ornithine and urea, the first step in arginine degradation; !1the arginase activity can be induced by arginine or !1homoarginine. GENETICS !$#gene SGD:CAR1; MIPS:YPL111w !'##cross-references SGD:S0006032; MIPS:YPL111w !$#map_position 16L CLASSIFICATION #superfamily arginase KEYWORDS hydrolase SUMMARY #length 333 #molecular-weight 35662 #checksum 6933 SEQUENCE /// ENTRY S45455 #type complete TITLE arginase (EC 3.5.3.1) - fission yeast (Schizosaccharomyces pombe) ORGANISM #formal_name Schizosaccharomyces pombe DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S45455; S42775 REFERENCE S45455 !$#authors van Huffel, C.; Dubois, E.; Messenguy, F. !$#journal Yeast (1994) 10:923-933 !$#title Cloning and sequencing of Schizosaccharomyces pombe car1 !1gene encoding arginase. Expression of the arginine anabolic !1and catabolic genes in response to arginine and related !1metabolites. !$#cross-references MUID:95076711; PMID:7985419 !$#accession S45455 !'##molecule_type DNA !'##residues 1-323 ##label VAN !'##cross-references EMBL:X75559; NID:g414913; PIDN:CAA53236.1; !1PID:g414914 GENETICS !$#gene car1 CLASSIFICATION #superfamily arginase KEYWORDS hydrolase SUMMARY #length 323 #molecular-weight 35721 #checksum 3927 SEQUENCE /// ENTRY S55795 #type complete TITLE arginase (EC 3.5.3.1) rocF - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S55795; B69694; S49269 REFERENCE S55793 !$#authors Gardan, R.; Rapoport, G.; Debarbouille, M. !$#journal J. Mol. Biol. (1995) 249:843-856 !$#title Expression of the rocDEF operon involved in arginine !1catabolism in Bacillus subtilis. !$#cross-references MUID:95311309; PMID:7540694 !$#accession S55795 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-296 ##label GAR !'##cross-references EMBL:X81802; NID:g550310; PIDN:CAA57400.1; !1PID:g550313 !'##experimental_source strain 168 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69694 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-296 ##label KUN !'##cross-references GB:Z99124; GB:AL009126; NID:g2636442; !1PIDN:CAB16069.1; PID:g2636579 !'##experimental_source strain 168 GENETICS !$#gene rocF FUNCTION !$#description hydrolyzes L-arginine to L-ornithine and urea; also !1hydrolyzes alpha-N-substituted L-arginines and canavanine !$#pathway arginine catabolism !$#note manganese cofactor; transcription induced by arginine, !1ornithine or citrulline CLASSIFICATION #superfamily arginase KEYWORDS arginine catabolism; hydrolase SUMMARY #length 296 #molecular-weight 32154 #checksum 8227 SEQUENCE /// ENTRY JC5866 #type complete TITLE arginase (EC 3.5.3.1) - Bacillus brevis ALTERNATE_NAMES arginine amidinase; Canavanase ORGANISM #formal_name Bacillus brevis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS JC5866; PC4503 REFERENCE JC5866 !$#authors Shimotohno, K.W.; Miwa, I.; Endo, T. !$#journal Biosci. Biotechnol. Biochem. (1997) 61:1459-1464 !$#title Molecular cloning and nucleotide sequence of the arginase !1gene of Bacillus brevis TT02-8 and its expression in !1Escherichia coli. !$#cross-references MUID:97480930; PMID:9339546 !$#accession JC5866 !'##molecule_type DNA !'##residues 1-298 ##label SHI !'##experimental_source strain TT02-8 !$#accession PC4503 !'##molecule_type protein !'##residues 1-36 ##label SH2 !'##note the authors translated the codon CTC for residue 54 as Arg COMMENT This enzyme catalyzes the first step of arginine catabolism, !1producing arginine metabolites for protein synthesis or !1carbon and nitrogen sources. CLASSIFICATION #superfamily arginase KEYWORDS hydrolase SUMMARY #length 298 #molecular-weight 31878 #checksum 9183 SEQUENCE /// ENTRY S68863 #type complete TITLE arginase (EC 3.5.3.1) - Bacillus caldovelox ORGANISM #formal_name Bacillus caldovelox DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S68863; S74304 REFERENCE S68863 !$#authors Bewley, M.C.; Lott, J.S.; Baker, E.N.; Patchett, M.L. !$#journal FEBS Lett. (1996) 386:215-218 !$#title The cloning, expression and crystallisation of a !1thermostable arginase. !$#cross-references MUID:96228067; PMID:8647285 !$#accession S68863 !'##molecule_type DNA !'##residues 1-299 ##label BEW !'##cross-references EMBL:U48226; NID:g1276984; PIDN:AAB06939.1; !1PID:g1276985 !'##experimental_source DSM 411 !$#accession S74304 !'##molecule_type protein !'##residues 1-15 ##label BEL COMPLEX homohexamer FUNCTION !$#description catalyzes hydrolysis of L-arginine to L-ornithine and urea; !1also hydrolyzes alpha-N-substituted L-arginines and !1canavanine !$#pathway arginine catabolism !$#note manganese cofactor; thermostable CLASSIFICATION #superfamily arginase KEYWORDS arginine catabolism; hydrolase FEATURE !$1-299 #product arginase #status experimental #label MAT SUMMARY #length 299 #molecular-weight 32433 #checksum 1845 SEQUENCE /// ENTRY JC4033 #type complete TITLE arginase (EC 3.5.3.1) - Coccidioides immitis ORGANISM #formal_name Coccidioides immitis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS JC4033 REFERENCE JC4033 !$#authors Pan, S.; Zhang, M.; Cole, G.T. !$#journal Gene (1995) 154:115-118 !$#title Isolation and characterization of the arginase-encoding gene !1(arg) from coccidioides immitis. !$#cross-references MUID:95172390; PMID:7867937 !$#accession JC4033 !'##molecule_type DNA !'##residues 1-322 ##label PAN !'##cross-references GB:L36550; NID:g550471; PIDN:AAA65960.1; !1PID:g550472 GENETICS !$#gene arg !$#introns 29/3; 222/2 CLASSIFICATION #superfamily arginase KEYWORDS hydrolase SUMMARY #length 322 #molecular-weight 35125 #checksum 7132 SEQUENCE /// ENTRY A26370 #type complete TITLE arginase (EC 3.5.3.1), hepatic - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S02132; A26370; S13038 REFERENCE S02132 !$#authors Takiguchi, M.; Haraguchi, Y.; Mori, M. !$#journal Nucleic Acids Res. (1988) 16:8789-8802 !$#title Human liver-type arginase gene: structure of the gene and !1analysis of the promoter region. !$#cross-references MUID:89016562; PMID:3174433 !$#accession S02132 !'##molecule_type DNA !'##residues 1-322 ##label TAK !'##cross-references EMBL:X12662; NID:g28829; PIDN:CAA31188.1; !1PID:g1197498 REFERENCE A94160 !$#authors Haraguchi, Y.; Takiguchi, M.; Amaya, Y.; Kawamoto, S.; !1Matsuda, I.; Mori, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:412-415 !$#title Molecular cloning and nucleotide sequence of cDNA for human !1liver arginase. !$#cross-references MUID:87092419; PMID:3540966 !$#accession A26370 !'##molecule_type mRNA !'##residues 1-85,'Q',87-322 ##label HAR !'##cross-references GB:M14502; NID:g178994; PIDN:AAA51776.1; !1PID:g178995 REFERENCE S13038 !$#authors Ikemoto, M.; Tabata, M.; Miyake, T.; Kono, T.; Mori, M.; !1Totani, M.; Murachi, T. !$#journal Biochem. J. (1990) 270:697-703 !$#title Expression of human liver arginase in Escherichia coli. !1Purification and properties of the product. !$#cross-references MUID:91054360; PMID:2241902 !$#accession S13038 !'##status preliminary !'##molecule_type mRNA !'##residues 1-13 ##label IKE GENETICS !$#gene GDB:ARG1 !'##cross-references GDB:119006; OMIM:207800 !$#map_position 6q23-6q23 !$#introns 19/3; 44/1; 102/2; 155/3; 187/2; 222/2; 268/1 CLASSIFICATION #superfamily arginase KEYWORDS hydrolase; liver; urea cycle SUMMARY #length 322 #molecular-weight 34735 #checksum 2400 SEQUENCE /// ENTRY A26702 #type complete TITLE arginase (EC 3.5.3.1), hepatic - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A26702; B26370; A28358 REFERENCE A26702 !$#authors Kawamoto, S.; Amaya, Y.; Murakami, K.; Tokunaga, F.; !1Iwanaga, S.; Kobayashi, K.; Saheki, T.; Kimura, S.; Mori, M. !$#journal J. Biol. Chem. (1987) 262:6280-6283 !$#title Complete nucleotide sequence of cDNA and deduced amino acid !1sequence of rat liver arginase. !$#cross-references MUID:87194847; PMID:3571256 !$#accession A26702 !'##molecule_type mRNA !'##residues 1-323 ##label KAW !'##cross-references GB:J02720; NID:g202980; PIDN:AAA40761.1; !1PID:g202981 REFERENCE A94160 !$#authors Haraguchi, Y.; Takiguchi, M.; Amaya, Y.; Kawamoto, S.; !1Matsuda, I.; Mori, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:412-415 !$#title Molecular cloning and nucleotide sequence of cDNA for human !1liver arginase. !$#cross-references MUID:87092419; PMID:3540966 !$#accession B26370 !'##molecule_type protein !'##residues 1-255,'G',257-323 ##label HAR REFERENCE A28358 !$#authors Ohtake, A.; Takiguchi, M.; Shigeto, Y.; Amaya, Y.; Kawamoto, !1S.; Mori, M. !$#journal J. Biol. Chem. (1988) 263:2245-2249 !$#title Structural organization of the gene for rat liver-type !1arginase. !$#cross-references MUID:88115364; PMID:2892837 !$#accession A28358 !'##molecule_type DNA !'##residues 1-297,'A',299-323 ##label OHT !'##cross-references GB:M17924 CLASSIFICATION #superfamily arginase KEYWORDS hydrolase; liver; urea cycle SUMMARY #length 323 #molecular-weight 34999 #checksum 6406 SEQUENCE /// ENTRY S52134 #type complete TITLE arginase (EC 3.5.3.1) - bullfrog ORGANISM #formal_name Rana catesbeiana #common_name bullfrog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S52134 REFERENCE S52133 !$#authors Iwase, K.; Yamauchi, K.; Ishikawa, K. !$#journal Biochim. Biophys. Acta (1995) 1260:139-146 !$#title Cloning of cDNAs encoding argininosuccinate lyase and !1arginase from Rana catesbeiana liver and regulation of their !1mRNAs during spontaneous and thyroid hormone-induced !1metamorphosis. !$#cross-references MUID:95143270; PMID:7841190 !$#accession S52134 !'##molecule_type mRNA !'##residues 1-321 ##label IWA !'##cross-references GB:D38303; NID:g1549229; PIDN:BAA07422.1; !1PID:g944977 !'##note the sequence from Fig. 4 is inconsistent with that from Fig. 3 !1in having 76-Glu CLASSIFICATION #superfamily arginase KEYWORDS hydrolase; trimer; urea cycle SUMMARY #length 321 #molecular-weight 35088 #checksum 2584 SEQUENCE /// ENTRY H69215 #type complete TITLE agmatine ureohydrolase - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H69215 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession H69215 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-286 ##label MTH !'##cross-references GB:AE000863; GB:AE000666; NID:g2621956; !1PIDN:AAB85366.1; PID:g2621961 !'##experimental_source strain Delta H GENETICS !$#gene MTH868 !$#start_codon TTG CLASSIFICATION #superfamily arginase SUMMARY #length 286 #molecular-weight 30749 #checksum 5414 SEQUENCE /// ENTRY F64338 #type complete TITLE agmatinase (EC 3.5.3.11) - Methanococcus jannaschii ALTERNATE_NAMES ureohydrolase ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F64338 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession F64338 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-284 ##label BUL !'##cross-references GB:U67485; GB:L77117; NID:g1591020; !1PIDN:AAB98295.1; PID:g1591030; TIGR:MJ0309 GENETICS !$#map_position REV290135-289281 CLASSIFICATION #superfamily arginase KEYWORDS hydrolase SUMMARY #length 284 #molecular-weight 32477 #checksum 1248 SEQUENCE /// ENTRY H70057 #type complete TITLE agmatinase homolog ywhG - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H70057 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H70057 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-290 ##label KUN !'##cross-references GB:Z99123; GB:AL009126; NID:g2636240; !1PIDN:CAB15776.1; PID:g2636285 !'##experimental_source strain 168 GENETICS !$#gene ywhG CLASSIFICATION #superfamily arginase SUMMARY #length 290 #molecular-weight 32417 #checksum 8018 SEQUENCE /// ENTRY F69330 #type complete TITLE agmatinase (speB) homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F69330 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession F69330 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-275 ##label KLE !'##cross-references GB:AE001060; GB:AE000782; NID:g2689383; !1PIDN:AAB90592.1; PID:g2649971; TIGR:AF0646 CLASSIFICATION #superfamily arginase SUMMARY #length 275 #molecular-weight 30707 #checksum 9764 SEQUENCE /// ENTRY S57669 #type complete TITLE Proclavaminic acid amidino hydrolase - Streptomyces clavuligerus ORGANISM #formal_name Streptomyces clavuligerus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S57669 REFERENCE S57668 !$#authors Hodgson, J.E.; Fosberry, A.; Rawlinson, N.S.; Ross, H.N.M.; !1Neal, R.J.; Arnell, J.C.; Earl, A.J.; Lawlor, E.J. !$#submission submitted to the EMBL Data Library, January 1995 !$#description Clavulanic acid biosynthesis in Streptomyces clavuligerus: !1gene cloning and characterization. !$#accession S57669 !'##status preliminary !'##molecule_type DNA !'##residues 1-313 ##label HOD !'##cross-references EMBL:X84101; NID:g886938; PIDN:CAA58904.1; !1PID:g886940 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily arginase SUMMARY #length 313 #molecular-weight 33401 #checksum 5207 SEQUENCE /// ENTRY S74558 #type complete TITLE arginase (EC 3.5.3.1) - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein sll0228 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S74558 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74558 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-306 ##label KAN !'##cross-references EMBL:D90900; GB:AB001339; NID:g1651768; !1PIDN:BAA16710.1; PID:g1651783 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily arginase KEYWORDS hydrolase SUMMARY #length 306 #molecular-weight 33463 #checksum 981 SEQUENCE /// ENTRY C42604 #type complete TITLE agmatinase (EC 3.5.3.11) [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES agmatine ureohydrolase ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS C42604; JV0067; B37771; H65078 REFERENCE A42604 !$#authors Szumanski, M.B.; Boyle, S.M. !$#journal J. Bacteriol. (1992) 174:758-764 !$#title Influence of cyclic AMP, agmatine, and a novel protein !1encoded by a flanking gene on speB (agmatine ureohydrolase) !1in Escherichia coli. !$#cross-references MUID:92121113; PMID:1310091 !$#accession C42604 !'##status preliminary !'##molecule_type DNA !'##residues 1-306 ##label SZU1 !'##cross-references GB:M32363; NID:g147858; PIDN:AAA83909.1; !1PID:g147859 !'##note sequence extracted from NCBI backbone (NCBIN:77509, !1NCBIP:77512) REFERENCE JV0067 !$#authors Szumanski, M.B.W.; Boyle, S.M. !$#journal J. Bacteriol. (1990) 172:538-547 !$#title Analysis and sequence of the speB gene encoding agmatine !1ureohydrolase, a putrescine biosynthetic enzyme in !1Escherichia coli. !$#cross-references MUID:90130284; PMID:2153656 !$#accession JV0067 !'##molecule_type DNA !'##residues 1-306 ##label SZU2 REFERENCE A37771 !$#authors Moore, R.C.; Boyle, S.M. !$#journal J. Bacteriol. (1990) 172:4631-4640 !$#title Nucleotide sequence and analysis of the speA gene encoding !1biosynthetic arginine decarboxylase in Escherichia coli. !$#cross-references MUID:90330576; PMID:2198270 !$#accession B37771 !'##status preliminary !'##molecule_type DNA !'##residues 1-45 ##label MOO !'##cross-references GB:M31770; NID:g147854; PIDN:AAA24647.1; !1PID:g551839 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65078 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-306 ##label BLAT !'##cross-references GB:AE000377; GB:U00096; NID:g2367178; !1PIDN:AAC75974.1; PID:g1789306; UWGP:b2937 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene speB !$#map_position 64 min FUNCTION !$#description EC 3.5.3.11 [validated, MUID:90130284]; catalyzes the !1hydrolysis of agmatine to urea and putrescine !$#pathway polyamine biosynthesis CLASSIFICATION #superfamily arginase KEYWORDS hydrolase SUMMARY #length 306 #molecular-weight 33557 #checksum 714 SEQUENCE /// ENTRY DIMSR1 #type complete TITLE protein-arginine deiminase (EC 3.5.3.15) 1 - mouse ALTERNATE_NAMES peptidylarginine deiminase (PAD) ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Mar-1994 #sequence_revision 21-Feb-1997 #text_change 18-Jun-1999 ACCESSIONS S35038; A58509; PH0202 REFERENCE S35038 !$#authors Tsuchida, M.; Takahara, H.; Minami, N.; Arai, T.; Kobayashi, !1Y.; Tsujimoto, H.; Fukazawa, C.; Sugawara, K. !$#journal Eur. J. Biochem. (1993) 215:677-685 !$#title cDNA nucleotide sequence and primary structure of mouse !1uterine peptidylarginine deiminase. Detection of a !13'-untranslated nucleotide sequence common to the mRNA of !1transiently expressed genes and rapid turnover of this !1enzyme's mRNA in the estrous cycle. !$#cross-references MUID:93358890; PMID:8354274 !$#accession S35038 !'##molecule_type mRNA !'##residues 1-673 ##label TSU !'##cross-references DDBJ:D16580; NID:g391765; PIDN:BAA04012.1; !1PID:g435120 !'##experimental_source uterus !'##note submitted to DDBJ June 30, 1993 by M. Tsuchida !$#accession A58509 !'##molecule_type protein !'##residues 1-46;345-360;392-408;539-560;668-673 ##label TS2 REFERENCE PH0202 !$#authors Tsuchida, M.; Minami, N.; Tsujimoto, H.; Fukazawa, C.; !1Takahara, H.; Sugawara, K. !$#journal Agric. Biol. Chem. (1991) 55:295-297 !$#title Molecular cloning of mouse peptidylarginine deiminase, and !1its possible isozyme cDNAs. !$#cross-references MUID:91248493; PMID:1368671 !$#accession PH0202 !'##status preliminary !'##molecule_type mRNA !'##residues 386-673 ##label TS3 GENETICS !$#gene PAD FUNCTION !$#description catalyzes the hydrolysis of peptidyl-arginine residues to !1peptidyl-citrulline and ammonia CLASSIFICATION #superfamily protein-arginine deiminase KEYWORDS acetylated amino end; calcium; citrulline; hydrolase; !1metalloprotein FEATURE !$1-673 #product protein-arginine deiminase #status !8experimental #label MAT\ !$1 #modified_site acetylated amino end (Met) #status !8experimental\ !$352 #modified_site citrulline (Arg) #status experimental\ !$542 #binding_site carbohydrate (Asn) (covalent) #status !8absent SUMMARY #length 673 #molecular-weight 76219 #checksum 4173 SEQUENCE /// ENTRY DIRTR1 #type complete TITLE protein-arginine deiminase (EC 3.5.3.15) 1 - rat ALTERNATE_NAMES peptidylarginine deiminase (PAD) ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 22-Jun-1990 #sequence_revision 21-Feb-1997 #text_change 18-Jun-1999 ACCESSIONS A34339; I53660 REFERENCE A34339 !$#authors Watanabe, K.; Senshu, T. !$#journal J. Biol. Chem. (1989) 264:15255-15260 !$#title Isolation and characterization of cDNA clones encoding rat !1skeletal muscle peptidylarginine deiminase. !$#cross-references MUID:89359350; PMID:2768262 !$#accession A34339 !'##molecule_type mRNA; protein !'##residues 1-665 ##label WAT !'##cross-references GB:J05022; NID:g205959; PIDN:AAA41793.1; !1PID:g205960 !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing !'##note although the authors report that the protein may be !1glycosylated and suggest that it may be at Asn-534, that !1residue was not absent during peptide sequencing REFERENCE I53660 !$#authors Watanabe, K.; Nomoto, M.; Nagata, S.; Itoh, Y.; Hikichi, K.; !1Maruyama, N.; Mita, T.; Senshu, T. !$#journal Gene (1992) 114:261-265 !$#title The rat peptidylarginine deiminase-encoding gene: structural !1analysis and the 5'-flanking sequence. !$#cross-references MUID:92290286; PMID:1601308 !$#accession I53660 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-14 ##label RES !'##cross-references DDBJ:D10459; NID:g220859; PIDN:BAA01253.1; !1PID:g220860 !'##note exon junctions and translations are reported but not provided !1in the GenBank entry GENETICS !$#gene PAD !$#introns 31/2; 92/3; 117/1; 137/3; 177/1; 219/1; 278/3; 313/2; 350/3; !1386/3; 437/2; 485/3; 517/1; 545/3; 588/3 FUNCTION !$#description catalyzes the hydrolysis of peptidyl-arginine residues to !1peptidyl-citrulline and ammonia CLASSIFICATION #superfamily protein-arginine deiminase KEYWORDS calcium; citrulline; hydrolase; metalloprotein FEATURE !$1-665 #product protein-arginine deiminase #status predicted !8#label MAT\ !$505-516 #region calcium binding #status predicted\ !$344 #modified_site citrulline (Arg) #status predicted\ !$534 #binding_site carbohydrate (Asn) (covalent) #status !8absent SUMMARY #length 665 #molecular-weight 75356 #checksum 2347 SEQUENCE /// ENTRY S65593 #type complete TITLE adenosine deaminase (EC 3.5.-.-), double-stranded RNA-specific - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S65593 REFERENCE S65593 !$#authors Kim, U.; Wang, Y.; Sanford, T.; Zeng, Y.; Nishikura, K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1994) 91:11457-11461 !$#title Molecular cloning of cDNA for double-stranded RNA adenosine !1deaminase, a candidate enzyme for nuclear RNA editing. !$#cross-references MUID:95062287; PMID:7972084 !$#accession S65593 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-1226 ##label KIM !'##cross-references EMBL:U10439; NID:g577169; PIDN:AAB06697.1; !1PID:g577170 GENETICS !$#gene GDB:ADAR !'##cross-references GDB:439344 !$#map_position 1q21.1-1q21.2 CLASSIFICATION #superfamily double-stranded RNA-specific adenosine !1deaminase; double-stranded RNA-binding repeat homology KEYWORDS hydrolase; metalloprotein; RNA binding; RNA editing; zinc FEATURE !$502-572 #domain double-stranded RNA-binding repeat homology !8#label DSR1\ !$611-683 #domain double-stranded RNA-binding repeat homology !8#label DSR2\ !$724-795 #domain double-stranded RNA-binding repeat homology !8#label DSR3\ !$910,966,1036 #binding_site zinc (His, Cys, Cys) #status predicted SUMMARY #length 1226 #molecular-weight 135966 #checksum 3597 SEQUENCE /// ENTRY DUHUA #type complete TITLE adenosine deaminase (EC 3.5.4.4) - human ALTERNATE_NAMES adenosine aminohydrolase ORGANISM #formal_name Homo sapiens #common_name man DATE 25-Feb-1985 #sequence_revision 13-Aug-1986 #text_change 21-Jul-2000 ACCESSIONS A91032; A92446; A24638; A21127; A01009 REFERENCE A91032 !$#authors Valerio, D.; Duyvesteyn, M.G.C.; Dekker, B.M.M.; Weeda, G.; !1Berkvens, T.M.; van der Voorn, L.; van Ormondt, H.; van der !1Eb, A.J. !$#journal EMBO J. (1985) 4:437-443 !$#title Adenosine deaminase: characterization and expression of a !1gene with a remarkable promoter. !$#cross-references MUID:85257473; PMID:3839456 !$#accession A91032 !'##molecule_type DNA !'##residues 1-363 ##label VAL !'##cross-references GB:X02189; NID:g28358; PIDN:CAA26130.1; !1PID:g1197210 REFERENCE A92446 !$#authors Daddona, P.E.; Shewach, D.S.; Kelley, W.N.; Argos, P.; !1Markham, A.F.; Orkin, S.H. !$#journal J. Biol. Chem. (1984) 259:12101-12106 !$#title Human adenosine deaminase. cDNA and complete primary amino !1acid sequence. !$#cross-references MUID:85006946; PMID:6090454 !$#accession A92446 !'##molecule_type mRNA !'##residues 1-363 ##label DAD !'##cross-references GB:K02567; NID:g28379; PIDN:CAA26734.1; PID:g28380 REFERENCE A24638 !$#authors Wiginton, D.A.; Kaplan, D.J.; States, J.C.; Akeson, A.L.; !1Perme, C.M.; Bilyk, I.J.; Vaughn, A.J.; Lattier, D.L.; !1Hutton, J.J. !$#journal Biochemistry (1986) 25:8234-8244 !$#title Complete sequence and structure of the gene for human !1adenosine deaminase. !$#cross-references MUID:87128922; PMID:3028473 !$#accession A24638 !'##molecule_type DNA !'##residues 1-363 ##label WIG !'##cross-references GB:M13792; NID:g178076; PIDN:AAA78791.1; !1PID:g178077 REFERENCE A21127 !$#authors Wiginton, D.A.; Adrian, G.S.; Hutton, J.J. !$#journal Nucleic Acids Res. (1984) 12:2439-2446 !$#title Sequence of human adenosine deaminase cDNA including the !1coding region and a small intron. !$#cross-references MUID:84169545; PMID:6546794 !$#accession A21127 !'##molecule_type mRNA !'##residues 1-363 ##label WI2 !'##cross-references GB:X02994; NID:g28379; PIDN:CAA26734.1; PID:g28380 COMMENT This enzyme, found in all tissues, occurs in large amounts !1in T-lymphocytes and at the time of weaning in !1gastrointestinal tissues. COMMENT Absence or diminished activity of this enzyme in lymphocytes !1causes one form of severe combined immunodeficiency disease !1(SCID). COMMENT In hereditary hemolytic anemia, the level of this enzyme in !1erythrocytes increases 50-70 times. GENETICS !$#gene GDB:ADA !'##cross-references GDB:119649; OMIM:102700 !$#map_position 20q13.11-20q13.11 !$#introns 11/3; 32/2; 73/2; 121/2; 160/1; 202/3; 226/3; 260/3; 282/2; !1325/3; 360/1 FUNCTION !$#description catalyzes the hydrolysis of adenosine to inosine and ammonia !$#pathway purine catabolism !$#note also active on deoxyadenosine CLASSIFICATION #superfamily adenosine deaminase KEYWORDS hereditary hemolytic anemia; hydrolase; metalloprotein; !1purine catabolism; severe combined immunodeficiency; zinc FEATURE !$15,17,214,295 #binding_site zinc (His, His, His, Asp) #status !8predicted\ !$217,238,295 #active_site Glu, His, Asp #status predicted SUMMARY #length 363 #molecular-weight 40764 #checksum 2020 SEQUENCE /// ENTRY DUMSA #type complete TITLE adenosine deaminase (EC 3.5.4.4) [validated] - mouse ALTERNATE_NAMES ADA; adenosine aminohydrolase ORGANISM #formal_name Mus musculus #common_name house mouse DATE 13-Aug-1986 #sequence_revision 13-Aug-1986 #text_change 15-Sep-2000 ACCESSIONS A01010 REFERENCE A01010 !$#authors Yeung, C.Y.; Ingolia, D.E.; Roth, D.B.; Shoemaker, C.; !1Al-Ubaidi, M.R.; Yen, J.Y.; Ching, C.; Bobonis, C.; Kaufman, !1R.J.; Kellems, R.E. !$#journal J. Biol. Chem. (1985) 260:10299-10307 !$#title Identification of functional murine adenosine deaminase cDNA !1clones by complementation in Escherichia coli. !$#cross-references MUID:85261456; PMID:2410423 !$#accession A01010 !'##molecule_type mRNA !'##residues 1-352 ##label YEU !'##cross-references GB:M10319; NID:g191673; PIDN:AAA37173.1; !1PID:g309091 REFERENCE A67211 !$#authors Wilson, D.K.; Quiocho, F.A. !$#submission submitted to the Brookhaven Protein Data Bank, December 1994 !$#cross-references PDB:2ADA !$#contents annotation; X-ray crystallography, 2.4 angstroms, residues !14-352 REFERENCE A51593 !$#authors Wilson, D.K.; Quiocho, F.A. !$#submission submitted to the Brookhaven Protein Data Bank, December 1992 !$#cross-references PDB:1ADD !$#contents annotation; X-ray crystallography, 2.4 angstroms, residues !14-352 REFERENCE A41938 !$#authors Wilson, D.K.; Rudolph, F.B.; Quiocho, F.A. !$#journal Science (1991) 252:1278-1284 !$#title Atomic structure of adenosine deaminase complexed with a !1transition-state analog: understanding catalysis and !1immunodeficiency mutations. !$#cross-references MUID:92022516; PMID:1925539 !$#contents annotation; X-ray crystallography, 2.4 angstroms REFERENCE A46331 !$#authors Wilson, D.K.; Quiocho, F.A. !$#journal Biochemistry (1993) 32:1689-1694 !$#title A pre-transition-state mimic of an enzyme: X-ray structure !1of adenosine deaminase with bound 1-deazaadenosine and !1zinc-activated water. !$#cross-references MUID:93176749; PMID:8439534 !$#contents annotation; X-ray crystallography, 2.4 angstroms COMMENT This enzyme, found in all tissues, occurs in large amounts !1in T-lymphocytes and at the time of weaning in !1gastrointestinal tissues. FUNCTION !$#description catalyzes the hydrolysis of adenosine to inosine and ammonia !$#pathway purine catabolism !$#note also active on deoxyadenosine CLASSIFICATION #superfamily adenosine deaminase KEYWORDS hydrolase; metalloprotein; purine catabolism; severe !1combined immunodeficiency; zinc FEATURE !$15,17,214,295 #binding_site zinc (His, His, His, Asp) #status !8experimental\ !$19,184,296 #binding_site substrate (Asp, Gly, Asp) #status !8experimental\ !$217,238,295 #active_site Glu, His, Asp #status experimental SUMMARY #length 352 #molecular-weight 39991 #checksum 8022 SEQUENCE /// ENTRY A64919 #type complete TITLE adenosine deaminase (EC 3.5.4.4) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS A64919; A37943 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64919 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-333 ##label BLAT !'##cross-references GB:AE000258; GB:U00096; NID:g2367121; !1PIDN:AAC74695.1; PID:g1787910; UWGP:b1623 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A37943 !$#authors Chang, Z.; Nygaard, P.; Chinault, A.C.; Kellems, R.E. !$#journal Biochemistry (1991) 30:2273-2280 !$#title Deduced amino acid sequence of Escherichia coli adenosine !1deaminase reveals evolutionarily conserved amino acid !1residues: implications for catalytic function. !$#cross-references MUID:91152042; PMID:1998686 !$#accession A37943 !'##status preliminary !'##molecule_type DNA !'##residues 1-144,146-333 ##label CHA !'##cross-references GB:M59033; GB:J05320; NID:g145200; PIDN:AAA23419.1; !1PID:g145201 GENETICS !$#gene add FUNCTION !$#description catalyzes the hydrolysis of adenosine to inosine and ammonia !$#pathway nucleotide metabolism; purine catabolism CLASSIFICATION #superfamily adenosine deaminase KEYWORDS hydrolase; metalloprotein; purine catabolism; zinc FEATURE !$12,14,197,278 #binding_site zinc (His, His, His, Asp) #status !8predicted\ !$200,221,278 #active_site Glu, His, Asp #status predicted SUMMARY #length 333 #molecular-weight 36397 #checksum 5283 SEQUENCE /// ENTRY S55143 #type complete TITLE adenosine deaminase homolog YNL141w - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein JTB347; protein N1208; protein N1825 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S55143; S59248; S63086 REFERENCE S55136 !$#authors Mallet, L.; Bussereau, F.; Jacquet, M. !$#submission submitted to the EMBL Data Library, November 1994 !$#description A 43.5 kb fragment of the chromosome XIV. !$#accession S55143 !'##molecule_type DNA !'##residues 1-347 ##label MAL !'##cross-references EMBL:Z46843; NID:g861113; PIDN:CAA86885.1; !1PID:g854497 REFERENCE S59241 !$#authors Mallet, L.; Bussereau, F.; Jacquet, M. !$#journal Yeast (1995) 11:1195-1209 !$#title A 43.5 kb segment of yeast chromosome XIV, which contains !1MFA2, MEP2, CAP/SRV2, NAM9, FKB1/FPR1/RBP1, MOM22 and CPT1, !1predicts an adenosine deaminase gene and 14 new open reading !1frames. !$#cross-references MUID:96109932; PMID:8619318 !$#accession S59248 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-334 ##label MAW !'##cross-references EMBL:Z46843 REFERENCE S63069 !$#authors Mallet, L.; Bussereau, F.; Jacquet, M. !$#submission submitted to the Protein Sequence Database, April 1996 !$#accession S63086 !'##molecule_type DNA !'##residues 1-347 ##label MAF !'##cross-references EMBL:Z71417; NID:g1302088; PIDN:CAA96024.1; !1PID:g1302089; GSPDB:GN00014; MIPS:YNL141w !'##experimental_source strain S288C GENETICS !$#gene SGD:AAH1; MIPS:YNL141w !'##cross-references SGD:S0005085 !$#map_position 14L CLASSIFICATION #superfamily adenosine deaminase SUMMARY #length 347 #molecular-weight 39635 #checksum 2414 SEQUENCE /// ENTRY A70177 #type complete TITLE cytidine deaminase (cdd) homolog - Lyme disease spirochete ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A70177 REFERENCE A70100 !$#authors Fraser, C.M.; Casjens, S.; Huang, W.M.; Sutton, G.G.; !1Clayton, R.; Lathigra, R.; White, O.; Ketchum, K.A.; Dodson, !1R.; Hickey, E.K.; Gwinn, M.; Dougherty, B.; Tomb, J.F.; !1Fleischmann, R.D.; Richardson, D.; Peterson, J.; Kerlavage, !1A.R.; Quackenbush, J.; Salzberg, S.; Hanson, M.; Vugt, R.V.; !1Palmer, N.; Adams, M.D.; Gocayne, J.; Weidman, J.; !1Utterback, T.; Watthey, L.; McDonald, L.; Artiach, P.; !1Bowman, C.; Garland, S.; Fujii, C.; Cotton, M.D.; Horst, K.; !1Roberts, K.; Hatch, B.; Smith, H.O.; Venter, J.C. !$#journal Nature (1997) 390:580-586 !$#title Genomic sequence of a Lyme disease spirochaete, Borrelia !1burgdorferi. !$#cross-references MUID:98065943; PMID:9403685 !$#accession A70177 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-154 ##label KLE !'##cross-references GB:AE001163; GB:AE000783; NID:g2688541; !1PIDN:AAC66978.1; PID:g2688547; TIGR:BB0618 !'##experimental_source strain B31 CLASSIFICATION #superfamily cytidine deaminase SUMMARY #length 154 #molecular-weight 17548 #checksum 1136 SEQUENCE /// ENTRY D53312 #type complete TITLE cytidine deaminase (EC 3.5.4.5) - Mycoplasma pirum (strain BER) ORGANISM #formal_name Mycoplasma pirum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 07-Dec-1999 ACCESSIONS D53312 REFERENCE A53312 !$#authors Tham, T.N.; Ferris, S.; Kovacic, R.; Montagnier, L.; !1Blanchard, A. !$#journal J. Bacteriol. (1993) 175:5281-5285 !$#title Identification of Mycoplasma pirum genes involved in the !1salvage pathways for nucleosides. !$#cross-references MUID:93352438; PMID:8349569 !$#accession D53312 !'##status preliminary !'##molecule_type DNA !'##residues 1-133 ##label THA !'##cross-references GB:L13289; NID:g401781; PIDN:AAA25433.1; !1PID:g401785 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily cytidine deaminase KEYWORDS hydrolase SUMMARY #length 133 #molecular-weight 15018 #checksum 6718 SEQUENCE /// ENTRY S73415 #type complete TITLE cytidine deaminase (EC 3.5.4.5) cdd - Mycoplasma pneumoniae (strain ATCC 29342) ALTERNATE_NAMES hypothetical protein D09_orf133 ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Dec-1999 ACCESSIONS S73415 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73415 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-133 ##label HIM !'##cross-references EMBL:AE000011; GB:U00089; NID:g1673740; !1PIDN:AAB95737.1; PID:g1673744 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily cytidine deaminase KEYWORDS hydrolase SUMMARY #length 133 #molecular-weight 15185 #checksum 5351 SEQUENCE /// ENTRY G64205 #type complete TITLE cytidine deaminase (EC 3.5.4.5) - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G64205 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession G64205 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-130 ##label TIGR !'##cross-references GB:U39684; GB:L43967; NID:g3844650; !1PIDN:AAC71268.1; PID:g1045725; TIGR:MG052 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily cytidine deaminase KEYWORDS hydrolase SUMMARY #length 130 #molecular-weight 14974 #checksum 2729 SEQUENCE /// ENTRY S59391 #type complete TITLE hypothetical protein YLR245c - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein L9672.13 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S59391 REFERENCE S59386 !$#authors Johnson, D. !$#submission submitted to the EMBL Data Library, February 1995 !$#description The sequence of S. cerevisiae cosmid 9672. !$#accession S59391 !'##molecule_type DNA !'##residues 1-142 ##label JOH !'##cross-references EMBL:U20865; NID:g662330; PIDN:AAB67399.1; !1PID:g662343; GSPDB:GN00012; MIPS:YLR245c !'##experimental_source strain S288C (AB972) GENETICS !$#gene SGD:CDD1; MIPS:YLR245c !'##cross-references SGD:S0004235 !$#map_position 12R CLASSIFICATION #superfamily cytidine deaminase SUMMARY #length 142 #molecular-weight 15536 #checksum 2935 SEQUENCE /// ENTRY JE0022 #type complete TITLE cytidine/deoxycytidine deaminase (EC 3.5.4.-) cdd - Bacillus subtilis ALTERNATE_NAMES cytidine 12'-deoxycytidine aminohydrolase; P43 protein ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS JE0022; I39955; F69597; S04425 REFERENCE JE0022 !$#authors Song, B.H.; Neuhard, J. !$#journal Mol. Gen. Genet. (1989) 216:462-468 !$#title Chromosomal location, cloning and nucleotide sequence of the !1Bacillus subtilis cdd gene encoding cytidine/deoxycytidine !1deaminase. !$#cross-references MUID:89313687; PMID:2526291 !$#accession JE0022 !'##molecule_type DNA !'##residues 1-136 ##label SON !'##cross-references GB:U18532; NID:g606743; PIDN:AAB59993.1; !1PID:g606744 REFERENCE I39955 !$#authors Wang, P. !$#journal J. Biol. Chem. (1984) 259:8619-8625 !$#title Overlapping promoters transcribed by Bacillus subtilis !1sigma-55 and sigma-37 RNA polymerase holoenzymes during !1growth and stationary phases. !$#cross-references MUID:84239852; PMID:6330116 !$#accession I39955 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-10 ##label RES !'##cross-references GB:K02174; NID:g143349; PIDN:AAB05347.1; !1PID:g551724 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69597 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-136 ##label KUN !'##cross-references GB:Z99116; GB:Z99117; GB:AL009126; NID:g2634966; !1PIDN:CAB14472.1; PID:g2634976; NID:g2634723; PID:g2634962 !'##experimental_source strain 168 GENETICS !$#gene cdd !$#map_position 225 (degrees) CLASSIFICATION #superfamily cytidine deaminase KEYWORDS hydrolase SUMMARY #length 136 #molecular-weight 14854 #checksum 9048 SEQUENCE /// ENTRY I52710 #type complete TITLE cytidine deaminase (EC 3.5.4.5) [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS I52710; PC1224 REFERENCE I52710 !$#authors Laliberte, J.; Momparler, R.L. !$#journal Cancer Res. (1994) 54:5401-5407 !$#title Human cytidine deaminase: Purification of enzyme, cloning, !1and expression of its complementary DNA. !$#cross-references MUID:95007561; PMID:7923172 !$#accession I52710 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-146 ##label RES !'##cross-references GB:L27943; NID:g602451; PIDN:AAA57254.1; !1PID:g598149 !'##note part of this sequence was confirmed by protein sequencing REFERENCE PC1224 !$#authors Kuehn, K.; Bertling, W.M.; Emmrich, F. !$#journal Biochem. Biophys. Res. Commun. (1993) 190:1-7 !$#title Cloning of a functional cDNA for human cytidine deaminase !1(CDD) and its use as a marker of monocyte/macrophage !1differentiation. !$#cross-references MUID:93135752; PMID:8422236 !$#accession PC1224 !'##molecule_type mRNA !'##residues 2-26,'Q',28-146 ##label KUE !'##cross-references GB:S52873; NID:g263656; PIDN:AAB24946.1; !1PID:g263657 GENETICS !$#gene GDB:CDA !'##cross-references GDB:137169; OMIM:123920 !$#map_position 1p36.2-1p35 FUNCTION !$#description EC 3.5.4.5 [validated, MUID:95007561]; catalyzes the !1irreversible hydrolytic deamination of cytidine, !1deoxycytidine, and several of their analogs to the !1corresponding uridine derivatives CLASSIFICATION #superfamily cytidine deaminase KEYWORDS hydrolase SUMMARY #length 146 #molecular-weight 16185 #checksum 9335 SEQUENCE /// ENTRY A27366 #type complete TITLE AMP deaminase (EC 3.5.4.6), skeletal muscle - rat ALTERNATE_NAMES adenylic acid deaminase; AMP aminase; myoadenylate deaminase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A27366; I57509 REFERENCE A27366 !$#authors Sabina, R.L.; Marquetant, R.; Desai, N.M.; Kaletha, K.; !1Holmes, E.W. !$#journal J. Biol. Chem. (1987) 262:12397-12400 !$#title Cloning and sequence of rat myoadenylate deaminase cDNA. !1Evidence for tissue-specific and developmental regulation. !$#cross-references MUID:87308255; PMID:3624265 !$#accession A27366 !'##molecule_type mRNA !'##residues 1-747 ##label SAB !'##cross-references GB:J02811; NID:g202882; PIDN:AAB54086.1; !1PID:g202883 REFERENCE I57509 !$#authors Mineo, I.; Clarke, P.R.H.; Sabina, R.L.; Holmes, E.W. !$#journal Mol. Cell. Biol. (1990) 10:5271-5278 !$#title A novel pathway for alternative splicing: Identification of !1an RNA intermediate that generates an alternative 5' splice !1donor site not present in the primary transcript of AMPD1. !$#cross-references MUID:90377216; PMID:2398891 !$#accession I57509 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-17 ##label RES !'##cross-references GB:M58688; NID:g202875; PIDN:AAA40726.1; !1PID:g554413 GENETICS !$#gene AMPD1 !$#introns 8/1; 12/1 CLASSIFICATION #superfamily AMP deaminase KEYWORDS hydrolase; muscle; skeletal muscle SUMMARY #length 747 #molecular-weight 86431 #checksum 3147 SEQUENCE /// ENTRY DUBPC2 #type complete TITLE dCMP deaminase (EC 3.5.4.12) - phage T2 ALTERNATE_NAMES deoxycytidylate deaminase ORGANISM #formal_name phage T2 #note host Escherichia coli DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 31-Dec-1993 ACCESSIONS A01011 REFERENCE A01011 !$#authors Maley, G.F.; Guarino, D.U.; Maley, F. !$#journal J. Biol. Chem. (1983) 258:8290-8297 !$#title Complete amino acid sequence of an allosteric enzyme, T2 !1bacteriophage deoxycytidylate deaminase. !$#cross-references MUID:83238442; PMID:6345541 !$#accession A01011 !'##molecule_type protein !'##residues 1-188 ##label MAL COMMENT The active enzyme is a hexamer of identical chains. COMMENT This is an allosteric enzyme whose activity is greatly !1influenced by the end products of its metabolic pathway, !1dCTP and dTTP. CLASSIFICATION #superfamily phage T4 dCMP deaminase KEYWORDS allosteric regulation; hexamer; hydrolase SUMMARY #length 188 #molecular-weight 20599 #checksum 2845 SEQUENCE /// ENTRY DUBPT4 #type complete TITLE dCMP deaminase (EC 3.5.4.12) - phage T4 ALTERNATE_NAMES deoxycytidylate deaminase ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 18-Jun-1999 ACCESSIONS JN0081 REFERENCE JN0081 !$#authors Maley, G.F.; Duceman, B.W.; Wang, A.M.; Martinez, J.; Maley, !1F. !$#journal J. Biol. Chem. (1990) 265:47-51 !$#title Cloning, sequence analysis, and expression of the !1bacteriophage T4 cd gene. !$#cross-references MUID:90094440; PMID:2136740 !$#accession JN0081 !'##molecule_type DNA !'##residues 1-193 ##label MAL !'##cross-references GB:J05172; NID:g215837; PIDN:AAA32489.1; !1PID:g215838 GENETICS !$#gene cd CLASSIFICATION #superfamily phage T4 dCMP deaminase KEYWORDS allosteric regulation; hydrolase SUMMARY #length 193 #molecular-weight 21198 #checksum 9988 SEQUENCE /// ENTRY A28658 #type complete TITLE nitrilase (EC 3.5.5.1) - Klebsiella ozaenae ORGANISM #formal_name Klebsiella ozaenae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A28658 REFERENCE A28658 !$#authors Stalker, D.M.; Malyj, L.D.; McBride, K.E. !$#journal J. Biol. Chem. (1988) 263:6310-6314 !$#title Purification and properties of a nitrilase specific for the !1herbicide bromoxynil and corresponding nucleotide sequence !1analysis of the bxn gene. !$#cross-references MUID:88198177; PMID:2834373 !$#accession A28658 !'##molecule_type DNA !'##residues 1-349 ##label STA !'##cross-references GB:J03196; NID:g149174; PIDN:AAA25057.1; !1PID:g149175 CLASSIFICATION #superfamily nitrilase KEYWORDS hydrolase SUMMARY #length 349 #molecular-weight 37801 #checksum 2897 SEQUENCE /// ENTRY A42940 #type complete TITLE dCTP deaminase (EC 3.5.4.13) dcd [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES dut (dUTPase) mutation suppressor ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS A42940; H64972 REFERENCE A42940 !$#authors Wang, L.; Weiss, B. !$#journal J. Bacteriol. (1992) 174:5647-5653 !$#title dcd (dCTP deaminase) gene of Escherichia coli: mapping, !1cloning, sequencing, and identification as a locus of !1suppressors of lethal dut (dUTPase) mutations. !$#cross-references MUID:92380941; PMID:1324907 !$#accession A42940 !'##status preliminary !'##molecule_type DNA !'##residues 1-193 ##label WAN !'##cross-references GB:M90069; NID:g145715; PIDN:AAA23669.1; !1PID:g145716 !'##note sequence extracted from NCBI backbone (NCBIN:112699, !1NCBIP:112716) REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64972 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-193 ##label BLAT !'##cross-references GB:AE000296; GB:U00096; NID:g1788373; !1PIDN:AAC75126.1; PID:g1788379; UWGP:b2065 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene dcd FUNCTION !$#description EC 3.5.4.13 [validated, MUID:92380941] CLASSIFICATION #superfamily dCTP deaminase KEYWORDS hydrolase SUMMARY #length 193 #molecular-weight 21249 #checksum 5549 SEQUENCE /// ENTRY A64050 #type complete TITLE dCTP deaminase (EC 3.5.4.13) HI0133 [similarity] - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS A64050 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession A64050 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-195 ##label TIGR !'##cross-references GB:U32699; GB:L42023; NID:g3212180; !1PIDN:AAC21805.1; PID:g1573087; TIGR:HI0133 CLASSIFICATION #superfamily dCTP deaminase KEYWORDS hydrolase SUMMARY #length 195 #molecular-weight 21616 #checksum 9462 SEQUENCE /// ENTRY D64566 #type complete TITLE dCTP deaminase (EC 3.5.4.13) HP0372 [similarity] - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 31-Mar-2000 ACCESSIONS D64566 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession D64566 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-190 ##label TOM !'##cross-references GB:AE000554; GB:AE000511; NID:g2313475; !1PIDN:AAD07441.1; PID:g2313476; TIGR:HP0372 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily dCTP deaminase KEYWORDS hydrolase SUMMARY #length 190 #molecular-weight 21191 #checksum 993 SEQUENCE /// ENTRY S75588 #type complete TITLE dCTP deaminase (EC 3.5.4.13) sll1258 [similarity] - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S75588 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75588 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-193 ##label KAN !'##cross-references EMBL:D90912; GB:AB001339; NID:g1653228; !1PIDN:BAA18149.1; PID:g1653234 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily dCTP deaminase KEYWORDS hydrolase SUMMARY #length 193 #molecular-weight 21378 #checksum 1932 SEQUENCE /// ENTRY G64383 #type complete TITLE riboflavin-specific deaminase (EC 3.5.4.-) - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G64383 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession G64383 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-224 ##label BUL !'##cross-references GB:U67514; GB:L77117; NID:g2826304; !1PIDN:AAB98665.1; PID:g1591385; TIGR:MJ0671 GENETICS !$#map_position REV597638-596964 !$#start_codon TTG CLASSIFICATION #superfamily riboflavin-specific deaminase KEYWORDS hydrolase SUMMARY #length 224 #molecular-weight 25037 #checksum 2215 SEQUENCE /// ENTRY F69500 #type complete TITLE riboflavin-specific deaminase (ribG) homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS F69500 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession F69500 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-219 ##label KLE !'##cross-references GB:AE000964; GB:AE000782; NID:g2689287; !1PIDN:AAB89247.1; PID:g2648530; TIGR:AF2007 CLASSIFICATION #superfamily riboflavin-specific deaminase SUMMARY #length 219 #molecular-weight 24578 #checksum 4460 SEQUENCE /// ENTRY C69129 #type complete TITLE riboflavin-specific deaminase - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C69129 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession C69129 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-216 ##label MTH !'##cross-references GB:AE000810; GB:AE000666; NID:g2621277; !1PIDN:AAB84741.1; PID:g2621283 !'##experimental_source strain Delta H GENETICS !$#gene MTH235 CLASSIFICATION #superfamily riboflavin-specific deaminase SUMMARY #length 216 #molecular-weight 23576 #checksum 5693 SEQUENCE /// ENTRY G70339 #type complete TITLE riboflavin specific deaminase - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS G70339 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession G70339 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-224 ##label AQF !'##cross-references GB:AE000690; NID:g2983100; PIDN:AAC06708.1; !1PID:g2983103; GB:AE000657 !'##experimental_source strain VF5 GENETICS !$#gene ribD2 CLASSIFICATION #superfamily riboflavin-specific deaminase SUMMARY #length 224 #molecular-weight 25256 #checksum 8159 SEQUENCE /// ENTRY S74011 #type complete TITLE probable riboflavin-specific deaminase (EC 3.5.4.-) - Sulfolobus solfataricus ALTERNATE_NAMES protein c0625 ORGANISM #formal_name Sulfolobus solfataricus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S74011 REFERENCE S73076 !$#authors Sensen, C.W.; Klenk, H.P.; Singh, R.K.; Allard, G.; Chan, !1C.C.Y.; Liu, Q.Y.; Penny, S.L.; Young, F.; Schenk, M.E.; !1Gaasterland, T.; Doolittle, W.F.; Ragan, M.A.; Charlebois, !1R.L. !$#journal Mol. Microbiol. (1996) 22:175-191 !$#title Organizational characteristics and information content of an !1archaeal genome: 156 kb of sequence from Sulfolobus !1solfataricus P2. !$#cross-references MUID:97055432; PMID:8899719 !$#accession S74011 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-213 ##label SEN !'##cross-references EMBL:Y08256; NID:g1707679; PIDN:CAA69508.1; !1PID:g1707704 !'##experimental_source strain P2 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1September 1996 CLASSIFICATION #superfamily riboflavin-specific deaminase KEYWORDS hydrolase SUMMARY #length 213 #molecular-weight 24561 #checksum 2051 SEQUENCE /// ENTRY A39080 #type complete TITLE GTP cyclohydrolase I (EC 3.5.4.16) precursor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A39080; PC2256 REFERENCE A39080 !$#authors Hatakeyama, K.; Inoue, Y.; Harada, T.; Kagamiyama, H. !$#journal J. Biol. Chem. (1991) 266:765-769 !$#title Cloning and sequencing of cDNA encoding rat GTP !1cyclohydrolase I. The first enzyme of the !1tetrahydrobiopterin biosynthetic pathway. !$#cross-references MUID:91093270; PMID:1985963 !$#accession A39080 !'##status preliminary !'##molecule_type mRNA !'##residues 1-241 ##label HAT !'##cross-references GB:M58364; GB:J05729; NID:g204536; PIDN:AAA41299.1; !1PID:g204537 REFERENCE PC2256 !$#authors Imazumi, K.; Sasaki, T.; Takahashi, K.; Takai, Y. !$#journal Biochem. Biophys. Res. Commun. (1994) 205:1409-1416 !$#title Identification of a Rabphilin-3A-interacting protein as GTP !1cyclohydrolase I in PC12 cells. !$#cross-references MUID:95100975; PMID:7802677 !$#accession PC2256 !'##molecule_type protein !'##residues 37-46;99-116 ##label IMA !'##experimental_source PC12 cell CLASSIFICATION #superfamily GTP cyclohydrolase I KEYWORDS hydrolase SUMMARY #length 241 #molecular-weight 27057 #checksum 1270 SEQUENCE /// ENTRY JQ1934 #type complete TITLE GTP cyclohydrolase I (EC 3.5.4.16) - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JQ1934 REFERENCE JQ1934 !$#authors Nomura, T.; Ichinose, H.; Sumi-Ichinose, C.; Nomura, H.; !1Hagino, Y.; Fujita, K.; Nagatsu, T. !$#journal Biochem. Biophys. Res. Commun. (1993) 191:523-527 !$#title Cloning and sequencing of cDNA encoding mouse GTP !1cyclohydrolase I. !$#cross-references MUID:93213288; PMID:8461009 !$#accession JQ1934 !'##molecule_type mRNA !'##residues 1-241 ##label NOM !'##cross-references GB:L09737; NID:g293356; PIDN:AAA37757.1; !1PID:g293357 !'##experimental_source brain, strain ICR CLASSIFICATION #superfamily GTP cyclohydrolase I KEYWORDS hydrolase FEATURE !$76-96 #region pterin binding #status predicted SUMMARY #length 241 #molecular-weight 27014 #checksum 2792 SEQUENCE /// ENTRY A38256 #type complete TITLE GTP cyclohydrolase I (EC 3.5.4.16) mtrA - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A38256; A39409; G69661 REFERENCE A38256 !$#authors Gollnick, P.; Ishino, S.; Kuroda, M.I.; Henner, D.J.; !1Yanofsky, C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:8726-8730 !$#title The mtr locus is a two-gene operon required for !1transcription attenuation in the trp operon of Bacillus !1subtilis. !$#cross-references MUID:91062353; PMID:2123343 !$#accession A38256 !'##molecule_type DNA !'##residues 1-190 ##label GOL !'##cross-references GB:M37320; NID:g143230; PIDN:AAA22615.1; !1PID:g143231 REFERENCE A39409 !$#authors Micka, B.; Groch, N.; Heinemann, U.; Marahiel, M.A. !$#journal J. Bacteriol. (1991) 173:3191-3198 !$#title Molecular cloning, nucleotide sequence, and characterization !1of the Bacillus subtilis gene encoding the DNA-binding !1protein HBsu. !$#cross-references MUID:91216992; PMID:1902464 !$#accession A39409 !'##molecule_type DNA !'##residues 1-19 ##label MIC !'##cross-references GB:X52418 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69661 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-190 ##label KUN !'##cross-references GB:Z99115; GB:AL009126; NID:g2634478; !1PIDN:CAB14194.1; PID:g2634696 !'##experimental_source strain 168 COMMENT This enzyme catalyzes the first step of the synthesis of !1tetrahydrobiopterin, a cofactor in the synthesis of aromatic !1amino acids. GENETICS !$#gene mtrA !$#note the two genes in this methyltryptophan resistance (mtr) !1operon are mtrA and mrtB CLASSIFICATION #superfamily GTP cyclohydrolase I KEYWORDS hydrolase SUMMARY #length 190 #molecular-weight 21219 #checksum 1098 SEQUENCE /// ENTRY SHBY #type complete TITLE phosphoribosyl-AMP cyclohydrolase (EC 3.5.4.19) / phosphoribosyl-ATP diphosphatase (EC 3.6.1.31) / histidinol dehydrogenase (EC 1.1.1.23) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YCL030c; protein YCL183 ORGANISM #formal_name Saccharomyces cerevisiae DATE 18-Aug-1982 #sequence_revision 30-Sep-1993 #text_change 16-Aug-2002 ACCESSIONS S17473; S19358; A01012 REFERENCE S17471 !$#authors Ramezani Rad, M.; Luetzenkirchen, K.; Xu, G.; Kleinhans, U.; !1Hollenberg, C.P. !$#journal Yeast (1991) 7:533-538 !$#title The complete sequence of a 11,953 bp fragment from C1G on !1chromosome III encompasses four new open reading frames. !$#cross-references MUID:91377317; PMID:1897318 !$#accession S17473 !'##status translation not shown !'##molecule_type DNA !'##residues 1-799 ##label RAM !'##cross-references EMBL:X59720; NID:g1907116; PIDN:CAA42355.1; !1PID:g5334 REFERENCE S19350 !$#authors Hollenberg, C.P.; Kleinhans, U.; Lutzenkirchen, K.; Ramezani !1Rad, M.; Xu, G. !$#submission submitted to the Protein Sequence Database, March 1992 !$#accession S19358 !'##molecule_type DNA !'##residues 1-799 ##label HOL !'##cross-references EMBL:X59720; NID:g1907116; PIDN:CAA42355.1; !1PID:g5334; GSPDB:GN00003; MIPS:YCL030c REFERENCE A01012 !$#authors Donahue, T.F.; Farabaugh, P.J.; Fink, G.R. !$#journal Gene (1982) 18:47-59 !$#title The nucleotide sequence of the HIS4 region of yeast. !$#cross-references MUID:82262805; PMID:7049842 !$#accession A01012 !'##molecule_type DNA !'##residues 1-52,'R',54-374,'S',376-385,'Y',387-401,'VF',404-440,'N', !1442-793,'F',795-799 ##label DON !'##cross-references EMBL:V01310; NID:g3784; PIDN:CAA24617.1; PID:g3785 COMMENT This protein catalyzes the second, third, and tenth steps of !1the histidine biosynthesis pathway. GENETICS !$#gene SGD:HIS4; MIPS:YCL030c !'##cross-references SGD:S0000535; MIPS:YCL030c !$#map_position 3L CLASSIFICATION #superfamily hisI-hisD trifunctional enzyme; hisI !1bifunctional enzyme homology; hisI protein homology; !1histidinol dehydrogenase homology KEYWORDS histidine biosynthesis; hydrolase; multifunctional enzyme; !1oxidoreductase FEATURE !$143-329 #domain hisI bifunctional enzyme homology #label HSI\ !$143-241 #domain hisI protein homology #label HIS\ !$246-313 #region hisE protein homology\ !$390-789 #domain histidinol dehydrogenase homology #label HID SUMMARY #length 799 #molecular-weight 87790 #checksum 7213 SEQUENCE /// ENTRY SHNC #type complete TITLE phosphoribosyl-AMP cyclohydrolase (EC 3.5.4.19) / phosphoribosyl-ATP diphosphatase (EC 3.6.1.31) / histidinol dehydrogenase (EC 1.1.1.23) - Neurospora crassa ORGANISM #formal_name Neurospora crassa DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Aug-2002 ACCESSIONS A23978 REFERENCE A23978 !$#authors Legerton, T.L.; Yanofsky, C. !$#journal Gene (1985) 39:129-140 !$#title Cloning and characterization of the multifunctional his-3 !1gene of Neurospora crassa. !$#cross-references MUID:86137380; PMID:3005109 !$#accession A23978 !'##molecule_type DNA !'##residues 1-863 ##label LEG !'##cross-references GB:M27531; NID:g168817; PIDN:AAA33588.1; !1PID:g168818 GENETICS !$#gene his3 !$#introns 800/1 CLASSIFICATION #superfamily hisI-hisD trifunctional enzyme; hisI !1bifunctional enzyme homology; hisI protein homology; !1histidinol dehydrogenase homology KEYWORDS histidine biosynthesis; hydrolase; multifunctional enzyme; !1oxidoreductase FEATURE !$200-383 #domain hisI bifunctional enzyme homology #label HSI\ !$200-296 #domain hisI protein homology #label HIS\ !$300-367 #region hisE protein homology\ !$464-857 #domain histidinol dehydrogenase homology #label HID SUMMARY #length 863 #molecular-weight 94658 #checksum 7562 SEQUENCE /// ENTRY YNECHI #type complete TITLE phosphoribosyl-AMP cyclohydrolase (EC 3.5.4.19) / phosphoribosyl-ATP diphosphatase (EC 3.6.1.31) - Escherichia coli (strain K-12) ALTERNATE_NAMES N(1)-(5-phospho-D-ribosyl)-AMP 1,6-hydrolase / phosphoribosyl-ATP pyrophosphohydrolase ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Aug-2002 ACCESSIONS JS0135; C26022; I73528; A64968; I76778 REFERENCE JS0131 !$#authors Carlomagno, M.S.; Chiariotti, L.; Alifano, P.; Nappo, A.G.; !1Bruni, C.B. !$#journal J. Mol. Biol. (1988) 203:585-606 !$#title Structure and function of the Salmonella typhimurium and !1Escherichia coli K-12 histidine operons. !$#cross-references MUID:89094829; PMID:3062174 !$#accession JS0135 !'##molecule_type DNA !'##residues 1-203 ##label CAR !'##cross-references GB:X13462; NID:g41706; PIDN:CAA31818.1; PID:g41715 !'##experimental_source strain K12 !'##note the authors translated the codon TGG for residue 62 as Val REFERENCE A26022 !$#authors Chiariotti, L.; Alifano, P.; Carlomagno, M.S.; Bruni, C.B. !$#journal Mol. Gen. Genet. (1986) 203:382-388 !$#title Nucleotide sequence of the Escherichia coli hisD gene and of !1the Escherichia coli and Salmonella typhimurium hisIE !1region. !$#cross-references MUID:86310273; PMID:3018428 !$#accession C26022 !'##molecule_type DNA !'##residues 1-67,'S',69-203 ##label CHI !'##cross-references GB:X03974; NID:g41699; PIDN:CAA27613.1; PID:g41700 REFERENCE I56436 !$#authors Jovanovic, G.; Kostic, T.; Jankovic, M.; Savic, D.J. !$#journal J. Mol. Biol. (1994) 239:433-435 !$#title Nucleotide sequence of the Escherichia coli K-12 histidine !1operon revisited. !$#cross-references MUID:94260549; PMID:8201624 !$#accession I73528 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-67,'S',69-192,'T',194-203 ##label RES !'##cross-references EMBL:U02072; NID:g509820; PIDN:AAA19744.1; !1PID:g509821 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64968 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-67,'S',69-192,'T',194-203 ##label BLAT !'##cross-references GB:AE000293; GB:U00096; NID:g2367127; !1PIDN:AAC75087.1; PID:g2367128; UWGP:b2026 !'##experimental_source strain K-12, substrain MG1655 REFERENCE I57096 !$#authors Sugiyama, T.; Kido, N.; Komatsu, T.; Ohta, M.; Jann, K.; !1Jann, B.; Saeki, A.; Kato, N. !$#journal Microbiology (1994) 140:59-71 !$#title Genetic analysis of Escherichia coli O9 rfb: identification !1and DNA sequence of phosphomannomutase and GDP-mannose !1pyrophosphorylase genes. !$#cross-references MUID:94214678; PMID:8162191 !$#accession I76778 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-4,'L',6-45,'I',47-67,'S',69-163,'N',165-191,'GE',194-195, !1'D',197-198,'KN',201-202 ##label REF !'##cross-references GB:D43637; NID:g598464; PIDN:BAA07753.1; !1PID:g598473 COMMENT This bifunctional enzyme catalyzes two reactions in the !1histidine biosynthetic pathway. GENETICS !$#gene hisI (hisE) !$#map_position 44 min CLASSIFICATION #superfamily hisI bifunctional enzyme; hisI bifunctional !1enzyme homology; hisI protein homology KEYWORDS histidine biosynthesis; hydrolase; multifunctional enzyme FEATURE !$8-203 #domain hisI bifunctional enzyme homology #label HSI\ !$8-108 #domain hisI protein homology #label HIS\ !$116-187 #region similar to hisE protein SUMMARY #length 203 #molecular-weight 22762 #checksum 7389 SEQUENCE /// ENTRY YNEBHI #type complete TITLE phosphoribosyl-AMP cyclohydrolase (EC 3.5.4.19) / phosphoribosyl-ATP diphosphatase (EC 3.6.1.31) - Salmonella typhimurium ALTERNATE_NAMES N(1)-(5-phospho-D-ribosyl)-AMP 1,6-hydrolase/ phosphoribosyl-ATP pyrophosphohydrolase ORGANISM #formal_name Salmonella typhimurium DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Aug-2002 ACCESSIONS B26022; C26022 REFERENCE A26022 !$#authors Chiariotti, L.; Alifano, P.; Carlomagno, M.S.; Bruni, C.B. !$#journal Mol. Gen. Genet. (1986) 203:382-388 !$#title Nucleotide sequence of the Escherichia coli hisD gene and of !1the Escherichia coli and Salmonella typhimurium hisIE !1region. !$#cross-references MUID:86310273; PMID:3018428 !$#accession B26022 !'##molecule_type DNA !'##residues 1-203 ##label CHI !'##cross-references GB:X03975; NID:g47715; PIDN:CAA27614.1; PID:g47716 COMMENT This bifunctional enzyme catalyzes two reactions in the !1histidine biosynthetic pathway. GENETICS !$#gene hisI (hisE) !$#map_position 42 min CLASSIFICATION #superfamily hisI bifunctional enzyme; hisI bifunctional !1enzyme homology; hisI protein homology KEYWORDS histidine biosynthesis; hydrolase; multifunctional enzyme FEATURE !$8-203 #domain hisI bifunctional enzyme homology #label HSI\ !$8-108 #domain hisI protein homology #label HIS\ !$116-187 #region hisE protein homology SUMMARY #length 203 #molecular-weight 22665 #checksum 8456 SEQUENCE /// ENTRY C47754 #type complete TITLE phosphoribosyl-AMP cyclohydrolase (EC 3.5.4.19) / phosphoribosyl-ATP diphosphatase (EC 3.6.1.31) - Lactococcus lactis subsp. lactis ORGANISM #formal_name Lactococcus lactis subsp. lactis DATE 24-Feb-1994 #sequence_revision 02-Dec-1994 #text_change 16-Aug-2002 ACCESSIONS C47754 REFERENCE A45734 !$#authors Delorme, C.; Ehrlich, S.D.; Renault, P. !$#journal J. Bacteriol. (1992) 174:6571-6579 !$#title Histidine biosynthesis genes in Lactococcus lactis subsp. !1lactis. !$#cross-references MUID:93015709; PMID:1400209 !$#accession C47754 !'##molecule_type DNA !'##residues 1-212 ##label DEL !'##cross-references GB:U92974; GB:M90760; GB:M90761; NID:g2565137; !1PIDN:AAB81910.1; PID:g2565148 !'##experimental_source NCDO2118 !'##note sequence extracted from NCBI backbone (NCBIN:115814, !1NCBIP:115835) COMMENT This bifunctional enzyme catalyzes two reactions in the !1histidine biosynthetic pathway. GENETICS !$#gene hisI (hisE) CLASSIFICATION #superfamily hisI bifunctional enzyme; hisI bifunctional !1enzyme homology; hisI protein homology KEYWORDS histidine biosynthesis; hydrolase; multifunctional enzyme FEATURE !$1-198 #domain hisI bifunctional enzyme homology #label HSI\ !$1-100 #domain hisI protein homology #label HIS\ !$111-182 #region hisE protein homology SUMMARY #length 212 #molecular-weight 24675 #checksum 8684 SEQUENCE /// ENTRY S45545 #type complete TITLE GTP cyclohydrolase II (EC 3.5.4.25) / 3, 4-dihydroxy-2-butanone 4-phosphate synthase (EC 5.4.99.-) ribA - Bacillus subtilis ALTERNATE_NAMES ribA protein ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S45545; B69692 REFERENCE S45533 !$#authors Sorokin, A.; Zumstein, E.; Azevedo, V.; Ehrlich, S.D.; !1Serror, P. !$#submission submitted to the EMBL Data Library, November 1993 !$#accession S45545 !'##molecule_type DNA !'##residues 1-398 ##label SOR !'##cross-references EMBL:L09228; NID:g410114; PIDN:AAA67483.1; !1PID:g410127 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69692 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-398 ##label KUN !'##cross-references GB:Z99116; GB:AL009126; NID:g2634723; !1PIDN:CAB14258.1; PID:g2634761 !'##experimental_source strain 168 GENETICS !$#gene ribA CLASSIFICATION #superfamily ribA bifunctional protein; 3, !14-dihydroxy-2-butanone 4-phosphate synthase homology; !1cyclohydrolase homology KEYWORDS GTP; heat shock; hydrolase; intramolecular transferase; !1isomerase; multifunctional enzyme; riboflavin biosynthesis; !1stress-induced protein FEATURE !$8-197 #domain 3,4-dihydroxy-2-butanone 4-phosphate synthase !8homology #label HBPS\ !$247-396 #domain cyclohydrolase homology #label CYCH SUMMARY #length 398 #molecular-weight 44121 #checksum 6222 SEQUENCE /// ENTRY S75629 #type complete TITLE GTP cyclohydrolase II (EC 3.5.4.25) / 3, 4-dihydroxy-2-butanone 4-phosphate synthase (EC 5.4.99.-) ribA - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein sll1894 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S75629 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75629 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-556 ##label KAN !'##cross-references EMBL:D90912; GB:AB001339; NID:g1653228; !1PIDN:BAA18190.1; PID:g1653275 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene ribA CLASSIFICATION #superfamily ribA bifunctional protein; 3, !14-dihydroxy-2-butanone 4-phosphate synthase homology; !1cyclohydrolase homology KEYWORDS GTP; heat shock; hydrolase; intramolecular transferase; !1isomerase; riboflavin biosynthesis; stress-induced protein FEATURE !$8-200 #domain 3,4-dihydroxy-2-butanone 4-phosphate synthase !8homology #label HBPS\ !$251-400 #domain cyclohydrolase homology #label CYCH SUMMARY #length 556 #molecular-weight 61681 #checksum 4051 SEQUENCE /// ENTRY JC1188 #type complete TITLE GTP cyclohydrolase II (EC 3.5.4.25) / 3, 4-dihydroxy-2-butanone 4-phosphate synthase (EC 5.4.99.-) - Photobacterium leiognathi ORGANISM #formal_name Photobacterium leiognathi DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JC1188 REFERENCE JC1187 !$#authors Lee, C.Y.; Meighen, E.A. !$#journal Biochem. Biophys. Res. Commun. (1992) 186:690-697 !$#title The LUX genes in photobacterium leiognathi are closely !1linked with genes corresponding in sequence to riboflavin !1synthesis genes. !$#cross-references MUID:92360014; PMID:1339274 !$#accession JC1188 !'##molecule_type DNA !'##residues 1-364 ##label LEE !'##cross-references GB:M90094 !'##experimental_source ATCC 25521 !'##note the authors translated the codon CTG for residue 74 as Val, CAT !1for residue 134 as Asp CLASSIFICATION #superfamily ribA bifunctional protein; 3, !14-dihydroxy-2-butanone 4-phosphate synthase homology; !1cyclohydrolase homology KEYWORDS GTP; heat shock; hydrolase; intramolecular transferase; !1isomerase; riboflavin biosynthesis; stress-induced protein FEATURE !$9-199 #domain 3,4-dihydroxy-2-butanone 4-phosphate synthase !8homology #label HBPS\ !$248-364 #domain cyclohydrolase homology #label CYCH SUMMARY #length 364 #molecular-weight 39983 #checksum 1358 SEQUENCE /// ENTRY D64620 #type complete TITLE GTP cyclohydrolase II (EC 3.5.4.25) / 3, 4-dihydroxy-2-butanone 4-phosphate synthase (EC 5.4.99.-) - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS D64620 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession D64620 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-344 ##label TOM !'##cross-references GB:AE000592; GB:AE000511; NID:g2313929; !1PIDN:AAD07852.1; PID:g2313934; TIGR:HP0804 CLASSIFICATION #superfamily ribA bifunctional protein; 3, !14-dihydroxy-2-butanone 4-phosphate synthase homology; !1cyclohydrolase homology KEYWORDS GTP; heat shock; hydrolase; intramolecular transferase; !1isomerase; riboflavin biosynthesis; stress-induced protein FEATURE !$9-200 #domain 3,4-dihydroxy-2-butanone 4-phosphate synthase !8homology #label HBPS\ !$249-340 #domain cyclohydrolase homology #label CYCH SUMMARY #length 344 #molecular-weight 38972 #checksum 3378 SEQUENCE /// ENTRY A40654 #type complete TITLE GTP cyclohydrolase II (EC 3.5.4.25) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS A40654; S22376; H64875; S25160 REFERENCE A40654 !$#authors Richter, G.; Ritz, H.; Katzenmeier, G.; Volk, R.; Kohnle, !1A.; Lottspeich, F.; Allendorf, D.; Bacher, A. !$#journal J. Bacteriol. (1993) 175:4045-4051 !$#title Biosynthesis of riboflavin: cloning, sequencing, mapping, !1and expression of the gene coding for GTP cyclohydrolase II !1in Escherichia coli. !$#cross-references MUID:93308083; PMID:8320220 !$#accession A40654 !'##molecule_type DNA !'##residues 1-196 ##label RIC !'##cross-references EMBL:X67876; NID:g42737; PIDN:CAA48075.1; !1PID:g42738 !'##experimental_source strain K-12, substrain RR28 REFERENCE S22374 !$#authors Prodromou, C.; Artymiuk, P.J.; Guest, J.R. !$#journal Eur. J. Biochem. (1992) 204:599-609 !$#title The aconitase of Escherichia coli. Nucleotide sequence of !1the aconitase gene and amino acid sequence similarity with !1mitochondrial aconitases, the !1iron-responsive-element-binding protein and isopropylmalate !1isomerases. !$#cross-references MUID:92174916; PMID:1541275 !$#accession S22376 !'##molecule_type DNA !'##residues 107-196 ##label PRO !'##cross-references EMBL:X60293; NID:g40894; PIDN:CAA42835.1; !1PID:g40897 !'##experimental_source strain K-12, substrain W3110 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64875 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-196 ##label BLAT !'##cross-references GB:AE000226; GB:U00096; NID:g2367115; !1PIDN:AAC74359.1; PID:g1787533; UWGP:b1277 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ribA FUNCTION !$#pathway riboflavin biosynthesis !$#note cofactor magnesium CLASSIFICATION #superfamily Escherichia coli cyclohydrolase II; !1cyclohydrolase homology KEYWORDS GTP; hydrolase; magnesium; monomer; riboflavin biosynthesis FEATURE !$45-192 #domain cyclohydrolase homology #label CYCH SUMMARY #length 196 #molecular-weight 21836 #checksum 164 SEQUENCE /// ENTRY A64055 #type complete TITLE GTP cyclohydrolase II (EC 3.5.4.25) - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A64055 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession A64055 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-224 ##label TIGR !'##cross-references GB:U32706; GB:L42023; NID:g1573170; !1PIDN:AAC21880.1; PID:g1573172; TIGR:HI0212 GENETICS !$#gene ribA FUNCTION !$#pathway riboflavin biosynthesis CLASSIFICATION #superfamily Escherichia coli cyclohydrolase II; !1cyclohydrolase homology KEYWORDS GTP; hydrolase; riboflavin biosynthesis FEATURE !$55-204 #domain cyclohydrolase homology #label CYCH SUMMARY #length 224 #molecular-weight 25295 #checksum 9538 SEQUENCE /// ENTRY JC4209 #type complete TITLE GTP cyclohydrolase II (EC 3.5.4.25) - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS JC4209 REFERENCE JC4209 !$#authors Kobayashi, M.; Sugiyama, M.; Yamamoto, K. !$#journal Gene (1995) 160:303-304 !$#title Isolation of cDNAs encoding GTP cyclohydrolase II from !1Arabidopsis thaliana. !$#cross-references MUID:95369709; PMID:7642114 !$#accession JC4209 !'##molecule_type mRNA !'##residues 1-245 ##label KOB !'##cross-references DDBJ:D45165; NID:g940382; PIDN:BAA08113.1; !1PID:g940383 COMMENT This enzyme is involved in riboflavin (vitamin B2) !1biosynthesis, catalyzing the release of formate and !1inorganic pyrophosphate under formation of 2, !15-diamino-6-ribosylamino-4(3H)-pyrimidine 5'-phosphate from !1GTP. CLASSIFICATION #superfamily Escherichia coli cyclohydrolase II; !1cyclohydrolase homology KEYWORDS GTP; hydrolase; riboflavin biosynthesis FEATURE !$77-227 #domain cyclohydrolase homology #label CYCH SUMMARY #length 245 #molecular-weight 27269 #checksum 4705 SEQUENCE /// ENTRY B64620 #type complete TITLE GTP cyclohydrolase II (EC 3.5.4.25) - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B64620 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession B64620 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-192 ##label TOM !'##cross-references GB:AE000592; GB:AE000511; NID:g2313929; !1PIDN:AAD07851.1; PID:g2313933; TIGR:HP0802 GENETICS !$#start_codon TTG CLASSIFICATION #superfamily Escherichia coli cyclohydrolase II; !1cyclohydrolase homology KEYWORDS GTP; hydrolase; riboflavin biosynthesis FEATURE !$47-192 #domain cyclohydrolase homology #label CYCH SUMMARY #length 192 #molecular-weight 21715 #checksum 6065 SEQUENCE /// ENTRY I39498 #type complete TITLE GTP cyclohydrolase II (EC 3.5.4.25) - Azospirillum brasilense ORGANISM #formal_name Azospirillum brasilense DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS I39498 REFERENCE I39498 !$#authors Van Bastelaere, E.; Keijers, V.; Vanderleyden, J. !$#journal Gene (1995) 153:141-142 !$#title Cloning and sequencing of the putative Azospirillum !1brasilense gene encoding GTP cyclohydrolase II. !$#cross-references MUID:95189096; PMID:7883178 !$#accession I39498 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-385 ##label RES !'##cross-references EMBL:U09869; NID:g497270; PIDN:AAA82170.1; !1PID:g497271 COMMENT This enzyme is involved in riboflavin (vitamin B2) !1biosynthesis, catalyzing the release of formate and !1inorganic pyrophosphate under formation of 2, !15-diamino-6-ribosylamino-4(3H)-pyrimidine 5'-phosphate from !1GTP. CLASSIFICATION #superfamily Azospirillum cyclohydrolase II; cyclohydrolase !1homology KEYWORDS heat shock; hydrolase; riboflavin biosynthesis; !1stress-induced protein FEATURE !$236-385 #domain cyclohydrolase homology #label CYCH SUMMARY #length 385 #molecular-weight 40971 #checksum 2702 SEQUENCE /// ENTRY S45767 #type complete TITLE probable GTP cyclohydrolase II (EC 3.5.4.25) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YBL033c; protein YBL0417 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-Nov-1999 ACCESSIONS S45767; S46565; S50971 REFERENCE S45745 !$#authors Goffeau, A.; Jonniaux, J.L.; Purnelle, B.; Skala, J.; de !1Wergifosse, P.; van Dyck, L. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S45767 !'##molecule_type DNA !'##residues 1-345 ##label GOF !'##cross-references EMBL:Z35794; NID:g536040; PID:g536041; !1GSPDB:GN00002; MIPS:YBL033c !'##experimental_source strain S288C REFERENCE S46565 !$#authors Skala, J.; van Dyck, L.; Purnelle, B.; Goffeau, A. !$#journal Yeast (1994) 10(Suppl.A):S13-S24 !$#title The sequence of an 8.8 kb segment on the left arm of !1chromosome II from Saccharomyces cerevisiae reveals four new !1open reading frames including homologs of animal DNA !1polymerase alpha-primases and bacterial GTP cyclohydrolase !1II. !$#cross-references MUID:94378718; PMID:8091857 !$#accession S46565 !'##molecule_type DNA !'##residues 1-345 ##label SKA !'##cross-references EMBL:X74738; NID:g511140; PIDN:CAA52759.1; !1PID:g511141 !'##experimental_source strain S288C REFERENCE S50971 !$#authors Saiz, J.; Santos, M.A.; Plaza, M.A.; Revuelta, J.L. !$#submission submitted to the EMBL Data Library, February 1993 !$#description Cloning and sequencing of the RIB1 gene from Saccharomyces !1cerevisiae. !$#accession S50971 !'##molecule_type DNA !'##residues 1-180,'N',182-345 ##label SAI !'##cross-references EMBL:Z21617; NID:g642218; PIDN:CAA79741.1; !1PID:g642219 GENETICS !$#gene SGD:RIB1; MIPS:YBL033c !'##cross-references SGD:S0000129; MIPS:YBL033c !$#map_position 2L FUNCTION !$#description catalyzes formation of 2,5-diamino-6-ribosylamino-4 !1(3H)-pyrimidine 5'-phosphate from GTP releasing formate and !1inorganic pyrophosphate !$#pathway riboflavin (vitamin B2) biosynthesis CLASSIFICATION #superfamily yeast cyclohydrolase II; cyclohydrolase !1homology KEYWORDS GTP; hydrolase; riboflavin biosynthesis FEATURE !$139-309 #domain cyclohydrolase homology #label CYCH SUMMARY #length 345 #molecular-weight 38346 #checksum 7596 SEQUENCE /// ENTRY S57373 #type complete TITLE GTP cyclohydrolase II (EC 3.5.4.25) - Pichia guilliermondii ORGANISM #formal_name Pichia guilliermondii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S57373; S54165 REFERENCE S57373 !$#authors Liauta-Teglivets, O.; Hasslacher, M.; Boretskii, I.R.; !1Kohlwein, S.D.; Shavlovskii, G.M. !$#journal Yeast (1995) 11:945-952 !$#title Molecular cloning of the GTP-cyclohydrolase structural gene !1RIB1 of Pichia guilliermondii involved in riboflavin !1biosynthesis. !$#cross-references MUID:96021605; PMID:8533469 !$#accession S57373 !'##molecule_type DNA !'##residues 1-344 ##label LIA !'##cross-references EMBL:Z49093; NID:g1430926; PIDN:CAA88916.1; !1PID:g791095 !'##experimental_source strain L2 COMMENT This enzyme is involved in riboflavin (vitamin B2) !1biosynthesis, catalyzing the release of formate and !1inorganic pyrophosphate under formation of 2, !15-diamino-6-ribosylamino-4(3H)-pyrimidine 5'-phosphate from !1GTP. GENETICS !$#gene RIB1 CLASSIFICATION #superfamily yeast cyclohydrolase II; cyclohydrolase !1homology KEYWORDS GTP; hydrolase; riboflavin biosynthesis FEATURE !$167-326 #domain cyclohydrolase homology #label CYCH SUMMARY #length 344 #molecular-weight 38706 #checksum 7265 SEQUENCE /// ENTRY YNEC #type complete TITLE cyanate hydratase (EC 4.2.1.104) - Escherichia coli (strain K-12) ALTERNATE_NAMES cyanase; cyanate aminohydrolase; cyanate C-N-lyase; cyanate hydrolase ORGANISM #formal_name Escherichia coli DATE 13-Jun-1983 #sequence_revision 31-Dec-1988 #text_change 21-Jun-2002 ACCESSIONS A91850; A92414; A92672; D64761; A01013; A29833; B31977 REFERENCE A91850 !$#authors Sung, Y.C.; Anderson, P.M.; Fuchs, J.A. !$#journal J. Bacteriol. (1987) 169:5224-5230 !$#title Characterization of high-level expression and sequencing of !1the Escherichia coli K-12 cynS gene encoding cyanase. !$#cross-references MUID:88032847; PMID:2822670 !$#accession A91850 !'##molecule_type DNA !'##residues 1-156 ##label SUN1 !'##cross-references GB:M17891; GB:M17890; NID:g145647; PIDN:AAA23629.1; !1PID:g145648 REFERENCE A92414 !$#authors Chin, C.C.Q.; Anderson, P.M.; Wold, F. !$#journal J. Biol. Chem. (1983) 258:276-282 !$#title The amino acid sequence of Escherichia coli cyanase. !$#cross-references MUID:83082877; PMID:6336748 !$#accession A92414 !'##molecule_type protein !'##residues 1-33,'N',35-67,'N',69-73,'S',75-124,'D',126-156 ##label CHI REFERENCE A92672 !$#authors Sung, Y.; Fuchs, J.A. !$#journal J. Biol. Chem. (1988) 263:14769-14775 !$#title Characterization of the cyn operon in Escherichia coli K12. !$#cross-references MUID:89008347; PMID:3049588 !$#accession A92672 !'##molecule_type DNA !'##residues 1-156 ##label SUN2 !'##cross-references GB:M23219; NID:g145641; PIDN:AAA23626.1; !1PID:g145643 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64761 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-156 ##label BLAT !'##cross-references GB:AE000141; GB:U00096; NID:g1786532; !1PIDN:AAC73443.1; PID:g1786535; UWGP:b0340 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene cynS !$#map_position 8 min !$#note part of the cyn operon COMPLEX the active form is a homodecamer, consisting of five !1subunits, which are dimers covalently linked through Cys-83 FUNCTION !$#description catalyzes the reversible reaction of cyanate and bicarbonate !1to form carbamate and carbon dioxide !$#pathway nitrogen metabolism CLASSIFICATION #superfamily cyanate lyase KEYWORDS carbon-nitrogen lyase; carbon-oxygen lyase; cyanate !1resistance; hydro-lyase FEATURE !$83 #disulfide_bonds interchain #status experimental SUMMARY #length 156 #molecular-weight 17049 #checksum 5589 SEQUENCE /// ENTRY PWBY #type complete TITLE inorganic diphosphatase (EC 3.6.1.1) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YBR011c; protein YBR0202; pyrophosphate phosphohydrolase ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Nov-1980 #sequence_revision 09-Sep-1994 #text_change 03-Jun-2002 ACCESSIONS S45864; S07679; A01014; S29189 REFERENCE S45862 !$#authors Entian, K.D.; Koetter, P.; Rose, M.; Li, Z.; Thermann, R.; !1Brendel, M.; Baur, A.; Boles, E.; Miosga, T.; !1Schaaff-Gerstenschlaeger, I.; Zimmermann, F.K. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S45864 !'##molecule_type DNA !'##residues 1-287 ##label ENT !'##cross-references EMBL:Z35880; NID:g536205; PIDN:CAA84949.1; !1PID:g536206; GSPDB:GN00002; MIPS:YBR011c !'##experimental_source strain S288C REFERENCE S07679 !$#authors Kolakowski Jr., L.F.; Schloesser, M.; Cooperman, B.S. !$#journal Nucleic Acids Res. (1988) 16:10441-10452 !$#title Cloning, molecular characterization and chromosome !1localization of the inorganic pyrophosphatase (PPA) gene !1from S. cerevisiae. !$#cross-references MUID:89083474; PMID:2849749 !$#accession S07679 !'##molecule_type DNA !'##residues 1-266,'L',268-287 ##label KOL !'##cross-references EMBL:X13253; NID:g4198; PIDN:CAA31629.1; PID:g4199 REFERENCE A92241 !$#authors Cohen, S.A.; Sterner, R.; Keim, P.S.; Heinrikson, R.L. !$#journal J. Biol. Chem. (1978) 253:889-897 !$#title Covalent structural analysis of yeast inorganic !1pyrophosphatase. !$#cross-references MUID:78087552; PMID:340461 !$#accession A01014 !'##molecule_type protein !'##residues 2-40,'D',42-71,'N',73,75-117,'N',119-123,'Q',125-136,'E', !1138-186,'D',188-224,'N',226-287 ##label COH !'##note this is the final paper in a series !'##note no disulfide bonds are present REFERENCE S29189 !$#authors Raznikov, A.V.; Sklyankina, V.A.; Avaeva, S.M. !$#journal FEBS Lett. (1992) 308:62-64 !$#title Tyrosine-89 is important for enzymatic activity of S. !1cerevisiae inorganic pyrophosphatase. !$#cross-references MUID:92354770; PMID:1322842 !$#accession S29189 !'##molecule_type protein !'##residues 83-105,'E',107-112 ##label RAZ REFERENCE A90443 !$#authors Bond, M.W.; Chiu, N.Y.; Cooperman, B.S. !$#journal Biochemistry (1980) 19:94-102 !$#title Identification of an arginine important for enzymatic !1activity within the covalent structure of yeast inorganic !1pyrophosphatase. !$#contents annotation; active site GENETICS !$#gene SGD:IPP1; PPA; MIPS:YBR011c !'##cross-references SGD:S0000215; MIPS:YBR011c !$#map_position 2R FUNCTION !$#description catalyzes hydrolysis of pyrophosphate to orthophosphate !$#note requires divalent metal cation CLASSIFICATION #superfamily inorganic pyrophosphatase KEYWORDS homodimer; hydrolase FEATURE !$2-287 #product inorganic pyrophosphatase #status !8experimental #label MAT\ !$79 #binding_site pyrophosphate (Arg) #status !8experimental SUMMARY #length 287 #molecular-weight 32299 #checksum 4194 SEQUENCE /// ENTRY S11496 #type complete TITLE inorganic diphosphatase (EC 3.6.1.1) - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES pyrophosphate phosphohydrolase ORGANISM #formal_name Schizosaccharomyces pombe DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S11496; T38243 REFERENCE S11496 !$#authors Kawasaki, I.; Adachi, N.; Ikeda, H. !$#journal Nucleic Acids Res. (1990) 18:5888 !$#title Nucleotide sequence of S. pombe inorganic pyrophosphatase. !$#cross-references MUID:91016938; PMID:2170949 !$#accession S11496 !'##molecule_type DNA !'##residues 1-289 ##label KAW !'##cross-references EMBL:X54301; NID:g5013; PIDN:CAA38199.1; PID:g5014 REFERENCE Z21781 !$#authors Brown, D.; Churcher, C.M.; Barrell, B.G.; Rajandream, M.A.; !1Wood, V. !$#submission submitted to the EMBL Data Library, August 1995 !$#accession T38243 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-289 ##label BRO !'##cross-references EMBL:Z98559; PIDN:CAB11158.1; GSPDB:GN00066; !1SPDB:SPAC23C11.05 !'##experimental_source strain 972h-; cosmid c23C11 GENETICS !$#gene PPA !$#map_position 1 CLASSIFICATION #superfamily inorganic pyrophosphatase KEYWORDS hydrolase FEATURE !$80 #active_site Arg #status predicted SUMMARY #length 289 #molecular-weight 32467 #checksum 5076 SEQUENCE /// ENTRY PWVKL #type complete TITLE inorganic diphosphatase (EC 3.6.1.1) - yeast (Kluyveromyces marxianus var. lactis) ORGANISM #formal_name Kluyveromyces marxianus var. lactis, Candida sphaerica DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 03-Jun-2002 ACCESSIONS S07894 REFERENCE S07892 !$#authors Stark, M.J.R.; Milner, J.S. !$#journal Yeast (1989) 5:35-50 !$#title Cloning and analysis of the Kluyveromyces lactis TRP1 gene: !1a chromosomal locus flanked by genes encoding inorganic !1pyrophosphatase and histone H3. !$#cross-references MUID:89189093; PMID:2538971 !$#accession S07894 !'##molecule_type DNA !'##residues 1-287 ##label STA !'##cross-references EMBL:X14230; NID:g2900; PIDN:CAA32446.1; PID:g2903 GENETICS !$#gene IPP CLASSIFICATION #superfamily inorganic pyrophosphatase KEYWORDS hydrolase FEATURE !$79,151 #active_site Arg, Glu #status predicted SUMMARY #length 287 #molecular-weight 32165 #checksum 3660 SEQUENCE /// ENTRY PWEC #type complete TITLE inorganic diphosphatase (EC 3.6.1.1) - Escherichia coli (strain K-12) ALTERNATE_NAMES pyrophosphate phosphohydrolase ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 03-Jun-2002 ACCESSIONS A27648; S56452; E65234 REFERENCE A27648 !$#authors Lahti, R.; Pitkaeranta, T.; Valve, E.; Ilta, I.; !1Kukko-Kalske, E.; Heinonen, J. !$#journal J. Bacteriol. (1988) 170:5901-5907 !$#title Cloning and characterization of the gene encoding inorganic !1pyrophosphatase of Escherichia coli K-12. !$#cross-references MUID:89053923; PMID:2848015 !$#accession A27648 !'##molecule_type DNA !'##residues 1-176 ##label LAH !'##cross-references GB:M23550; NID:g340944; PIDN:AAB88583.1; !1PID:g450373 !'##experimental_source strain K12 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56452 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-176 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97123.1; !1PID:g537068 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65234 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-176 ##label BLAT !'##cross-references GB:AE000494; GB:U00096; NID:g1790670; !1PIDN:AAC77183.1; PID:g1790673; UWGP:b4226 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ppa !$#map_position 100 min COMPLEX homohexamer FUNCTION !$#description catalyzes the hydrolysis of pyrophosphate to orthophosphate !1in the presence of divalent metal cations; provides a !1thermodynamic pull for biosynthetic reactions such as !1protein, RNA, and DNA synthesis CLASSIFICATION #superfamily inorganic pyrophosphatase KEYWORDS hydrolase FEATURE !$2-176 #product inorganic pyrophosphatase #status predicted !8#label MAT SUMMARY #length 176 #molecular-weight 19703 #checksum 3827 SEQUENCE /// ENTRY A38230 #type complete TITLE inorganic diphosphatase (EC 3.6.1.1), H+-translocating pyrophosphate-energized - Arabidopsis thaliana ALTERNATE_NAMES H+-PPase; pyrophosphate-energized vacuolar membrane proton pump ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS A38230; S29437; S29438 REFERENCE A38230 !$#authors Sarafian, V.; Kim, Y.; Poole, R.J.; Rea, P.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:1775-1779 !$#title Molecular cloning and sequence of cDNA encoding the !1pyrophosphate-energized vacuolar membrane proton pump of !1Arabidopsis thaliana. !$#cross-references MUID:92179265; PMID:1311852 !$#accession A38230 !'##status preliminary !'##molecule_type mRNA !'##residues 1-770 ##label SAR !'##cross-references GB:M81892; NID:g166633; PIDN:AAA32754.1; !1PID:g166634 !'##experimental_source cv. Columbia !'##note sequence extracted from NCBI backbone (NCBIP:87190) REFERENCE S29400 !$#authors Raynal, M.; Grellet, F.; Laudie, M.; Meyer, Y.; Cooke, R.; !1Delseny, M. !$#submission submitted to the EMBL Data Library, October 1992 !$#accession S29437 !'##molecule_type mRNA !'##residues 554-575,'A',577-583,'P',585-671 ##label RAY1 !'##cross-references EMBL:Z17694 !$#accession S29438 !'##molecule_type mRNA !'##residues 'VQR',719-770 ##label RAY2 !'##cross-references EMBL:Z17695 CLASSIFICATION #superfamily inorganic pyrophosphatase, H+-translocating !1pyrophosphate-energized KEYWORDS hydrolase; membrane protein SUMMARY #length 770 #molecular-weight 80819 #checksum 7125 SEQUENCE /// ENTRY JC1466 #type complete TITLE inorganic diphosphatase (EC 3.6.1.1) - barley ORGANISM #formal_name Hordeum vulgare #common_name barley DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS JC1466 REFERENCE JC1466 !$#authors Tanaka, Y.; Chiba, K.; Maeda, M.; Maeshima, M. !$#journal Biochem. Biophys. Res. Commun. (1993) 190:1110-1114 !$#title Molecular cloning of cDNA for vacuolar membrane !1proton-translocating inorganic pyrophosphatase in hordeum !1vulgare. !$#cross-references MUID:93176156; PMID:8382487 !$#accession JC1466 !'##molecule_type mRNA !'##residues 1-761 ##label TAN !'##cross-references DDBJ:D13472; NID:g285637; PIDN:BAA02717.1; !1PID:g285638 !'##experimental_source root CLASSIFICATION #superfamily inorganic pyrophosphatase, H+-translocating !1pyrophosphate-energized KEYWORDS hydrolase; transmembrane protein FEATURE !$11-32 #domain transmembrane #status predicted #label TM1\ !$91-110 #domain transmembrane #status predicted #label TM2\ !$131-154 #domain transmembrane #status predicted #label TM3\ !$184-204 #domain transmembrane #status predicted #label TM4\ !$217-236 #domain transmembrane #status predicted #label TM5\ !$306-341 #domain transmembrane #status predicted #label TM6\ !$360-381 #domain transmembrane #status predicted #label TM7\ !$398-417 #domain transmembrane #status predicted #label TM8\ !$454-477 #domain transmembrane #status predicted #label TM9\ !$534-555 #domain transmembrane #status predicted #label TM10\ !$570-589 #domain transmembrane #status predicted #label TM11\ !$649-672 #domain transmembrane #status predicted #label TM12 SUMMARY #length 761 #molecular-weight 79841 #checksum 2342 SEQUENCE /// ENTRY QPHO #type complete TITLE acylphosphatase (EC 3.6.1.7) Ho1, skeletal muscle - horse ALTERNATE_NAMES acylphosphate phosphohydrolase ORGANISM #formal_name Equus caballus #common_name domestic horse DATE 31-Aug-1980 #sequence_revision 31-Aug-1980 #text_change 17-May-1996 ACCESSIONS A01015 REFERENCE A01015 !$#authors Cappugi, G.; Manao, G.; Camici, G.; Ramponi, G. !$#journal J. Biol. Chem. (1980) 255:6868-6874 !$#title The complete amino acid sequence of horse muscle !1acylphosphatase. !$#cross-references MUID:80227852; PMID:6248536 !$#accession A01015 !'##molecule_type protein !'##residues 1-98 ##label CAP COMMENT In the absence of reducing factors, the enzyme tends to !1dimerize by the formation of a disulfide bond. COMMENT 1,3-Diphosphoglycerate and carbamoylphosphate are possible !1substrates of this enzyme in mammalian tissues. CLASSIFICATION #superfamily acylphosphatase KEYWORDS acetylated amino end; hydrolase FEATURE !$1 #modified_site acetylated amino end (Ser) #status !8experimental\ !$21 #disulfide_bonds interchain (partial) #status !8experimental\ !$21 #binding_site glutathione (Cys) (covalent) (partial) !8#status experimental SUMMARY #length 98 #molecular-weight 11016 #checksum 6094 SEQUENCE /// ENTRY QPPG #type complete TITLE acylphosphatase (EC 3.6.1.7), skeletal muscle - pig ALTERNATE_NAMES acylphosphate phosphohydrolase ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 10-May-1996 ACCESSIONS A01016 REFERENCE A01016 !$#authors Mizuno, Y.; Yamazaki, M.; Takasawa, T.; Kizaki, T.; !1Shiokawa, H. !$#journal J. Biochem. (1985) 97:1135-1142 !$#title Amino acid sequence of acylphosphatase from porcine skeletal !1muscle. !$#cross-references MUID:85289095; PMID:2993259 !$#accession A01016 !'##molecule_type protein !'##residues 1-98 ##label MIZ COMMENT 1,3-Diphosphoglycerate and carbamoylphosphate are possible !1substrates of this enzyme in mammalian tissues. CLASSIFICATION #superfamily acylphosphatase KEYWORDS acetylated amino end; hydrolase FEATURE !$1 #modified_site acetylated amino end (Ser) #status !8experimental\ !$21 #disulfide_bonds interchain #status predicted\ !$21 #binding_site glutathione (Cys) (covalent) #status !8predicted SUMMARY #length 98 #molecular-weight 11074 #checksum 5938 SEQUENCE /// ENTRY QPBO #type complete TITLE acylphosphatase (EC 3.6.1.7), skeletal muscle - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 10-May-1996 ACCESSIONS A29578 REFERENCE A29578 !$#authors Camici, G.; Manao, G.; Modesti, A.; Stefani, M.; Berti, A.; !1Cappugi, G.; Ramponi, G. !$#journal Ital. J. Biochem. (1986) 35:1-15 !$#title The complete amino acid sequence of bovine skeletal muscle !1acylphosphatase. !$#cross-references MUID:86223180; PMID:3011706 !$#accession A29578 !'##molecule_type protein !'##residues 1-98 ##label CAM CLASSIFICATION #superfamily acylphosphatase KEYWORDS acetylated amino end; hydrolase FEATURE !$1 #modified_site acetylated amino end (Ser) #status !8experimental\ !$21 #disulfide_bonds interchain #status predicted\ !$21 #binding_site glutathione (Cys) (covalent) #status !8predicted SUMMARY #length 98 #molecular-weight 11046 #checksum 6089 SEQUENCE /// ENTRY QPRB #type complete TITLE acylphosphatase (EC 3.6.1.7), skeletal muscle - rabbit ALTERNATE_NAMES acylphosphate phosphohydrolase ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 17-May-1996 ACCESSIONS A91988; A90076; A01017 REFERENCE A91988 !$#authors Kizaki, T.; Takasawa, T.; Mizuno, Y.; Shiokawa, H. !$#journal J. Biochem. (1985) 97:1155-1161 !$#title Amino acid sequence of acylphosphatase from rabbit skeletal !1muscle. !$#cross-references MUID:85289097; PMID:2993260 !$#accession A91988 !'##molecule_type protein !'##residues 1-98 ##label KIZ REFERENCE A90076 !$#authors Manao, G.; Camici, G.; Cappugi, G.; Stefani, M.; Liguri, G.; !1Berti, A.; Ramponi, G. !$#journal Arch. Biochem. Biophys. (1985) 241:418-423 !$#title Rabbit skeletal muscle acylphosphatase: the amino acid !1sequence of form Ra1. !$#cross-references MUID:85305733; PMID:2994566 !$#accession A90076 !'##molecule_type protein !'##residues 1-98 ##label MAN COMMENT In the absence of reducing factors, the enzyme tends to !1dimerize by the formation of a disulfide bond. COMMENT 1,3-Diphosphoglycerate and carbamoylphosphate are possible !1substrates of this enzyme in mammalian tissues. CLASSIFICATION #superfamily acylphosphatase KEYWORDS acetylated amino end; hydrolase FEATURE !$1 #modified_site acetylated amino end (Ser) #status !8experimental\ !$21 #disulfide_bonds interchain (partial) #status !8experimental\ !$21 #binding_site glutathione (Cys) (covalent) (partial) !8#status experimental SUMMARY #length 98 #molecular-weight 10861 #checksum 5848 SEQUENCE /// ENTRY QPGP #type complete TITLE acylphosphatase (EC 3.6.1.7), skeletal muscle - guinea pig ORGANISM #formal_name Cavia porcellus #common_name guinea pig DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 10-May-1996 ACCESSIONS A60893 REFERENCE A60893 !$#authors Manao, G.; Cappugi, G.; Modesti, A.; Stefani, M.; !1Marzocchini, R.; Degl'Innocenti, D.; Camici, G. !$#journal J. Protein Chem. (1988) 7:417-426 !$#title Guinea pig acylphosphatase: the amino acid sequence. !$#cross-references MUID:89351588; PMID:2855598 !$#accession A60893 !'##molecule_type protein !'##residues 1-98 ##label MAN CLASSIFICATION #superfamily acylphosphatase KEYWORDS acetylated amino end; hydrolase FEATURE !$1 #modified_site acetylated amino end (Ser) #status !8experimental\ !$21 #disulfide_bonds interchain #status predicted\ !$21 #binding_site glutathione (Cys) (covalent) #status !8predicted SUMMARY #length 98 #molecular-weight 10876 #checksum 5819 SEQUENCE /// ENTRY QPTK #type complete TITLE acylphosphatase (EC 3.6.1.7) Tu1, skeletal muscle - turkey ALTERNATE_NAMES acylphosphate phosphohydrolase ORGANISM #formal_name Meleagris gallopavo #common_name common turkey DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 17-May-1996 ACCESSIONS A01018 REFERENCE A01018 !$#authors Camici, G.; Manao, G.; Cappugi, G.; Berti, A.; Stefani, M.; !1Liguri, G.; Ramponi, G. !$#journal Eur. J. Biochem. (1983) 137:269-277 !$#title The primary structure of turkey muscle acylphosphatase. !$#cross-references MUID:84084611; PMID:6317387 !$#accession A01018 !'##molecule_type protein !'##residues 1-102 ##label CAM !'##experimental_source domestic breed COMMENT In the absence of reducing factors, the enzyme tends to !1dimerize by the formation of a disulfide bond. CLASSIFICATION #superfamily acylphosphatase KEYWORDS acetylated amino end; hydrolase FEATURE !$1 #modified_site acetylated amino end (Ser) #status !8experimental\ !$25 #disulfide_bonds interchain (partial) #status !8experimental\ !$25 #binding_site glutathione (Cys) (covalent) (partial) !8#status experimental SUMMARY #length 102 #molecular-weight 11317 #checksum 9799 SEQUENCE /// ENTRY QPCH #type complete TITLE acylphosphatase (EC 3.6.1.7) Ch1, skeletal muscle - chicken ALTERNATE_NAMES acylphosphate phosphohydrolase ORGANISM #formal_name Gallus gallus #common_name chicken DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 10-May-1996 ACCESSIONS A41512 REFERENCE A41512 !$#authors Minowa, O.; Ohba, Y.; Mizuno, Y.; Shiokawa, H. !$#journal J. Biochem. (1987) 102:1213-1220 !$#title The primary structure of chicken muscle acylphosphatase !1isozyme Ch1. !$#cross-references MUID:88139273; PMID:2830253 !$#accession A41512 !'##molecule_type protein !'##residues 1-102 ##label MIN CLASSIFICATION #superfamily acylphosphatase KEYWORDS acetylated amino end; hydrolase FEATURE !$1 #modified_site acetylated amino end (Ser) #status !8experimental\ !$25 #disulfide_bonds interchain #status predicted\ !$25 #binding_site glutathione (Cys) (covalent) #status !8predicted SUMMARY #length 102 #molecular-weight 11278 #checksum 9930 SEQUENCE /// ENTRY QPCH2 #type complete TITLE acylphosphatase (EC 3.6.1.7) Ch2, skeletal muscle - chicken ALTERNATE_NAMES acylphosphate phosphohydrolase ORGANISM #formal_name Gallus gallus #common_name chicken DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 05-Aug-1994 ACCESSIONS A41513 REFERENCE A41513 !$#authors Ohba, Y.; Minowa, O.; Mizuno, Y.; Shiokawa, H. !$#journal J. Biochem. (1987) 102:1221-1229 !$#title The primary structure of chicken muscle acylphosphatase !1isozyme Ch2. !$#cross-references MUID:88139274; PMID:2830254 !$#accession A41513 !'##molecule_type protein !'##residues 1-98 ##label OHB CLASSIFICATION #superfamily acylphosphatase KEYWORDS acetylated amino end; hydrolase FEATURE !$1 #modified_site acetylated amino end (Ala) #status !8experimental SUMMARY #length 98 #molecular-weight 11019 #checksum 2208 SEQUENCE /// ENTRY QPHUE #type complete TITLE acylphosphatase (EC 3.6.1.7), erythrocyte [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1993 #sequence_revision 02-Jul-1998 #text_change 08-Dec-2000 ACCESSIONS S66187; A25587; S59137; S52326 REFERENCE S66187 !$#authors Fiaschi, T.; Raugei, G.; Marzocchini, R.; Chiarugi, P.; !1Cirri, P.; Ramponi, G. !$#journal FEBS Lett. (1995) 367:145-148 !$#title Cloning and expression of the cDNA coding for the !1erythrocyte isoenzyme of human acylphosphatase. !$#cross-references MUID:95317414; PMID:7796909 !$#accession S66187 !'##molecule_type mRNA !'##residues 1-99 ##label FIA !'##cross-references GB:X84194; NID:g1816490; PIDN:CAA58987.1; !1PID:g1834464 !'##experimental_source placenta !'##note the authors translated the codon ACC for residue 6 as Tyr REFERENCE A25587 !$#authors Liguri, G.; Camici, G.; Manao, G.; Cappugi, G.; Nassi, P.; !1Modesti, A.; Ramponi, G. !$#journal Biochemistry (1986) 25:8089-8094 !$#title A new acylphosphatase isoenzyme from human erythrocytes: !1purification, characterization, and primary structure. !$#cross-references MUID:87101109; PMID:3026468 !$#accession A25587 !'##molecule_type protein !'##residues 2-99 ##label LIG REFERENCE S59137 !$#authors Chiarugi, P.; Raugei, G.; Marzocchini, R.; Fiaschi, T.; !1Ciccarelli, C.; Berti, A.; Ramponi, G. !$#journal Biochem. J. (1995) 311:567-573 !$#title Differential modulation of expression of the two !1acylphosphatase isoenzymes by thyroid hormone. !$#cross-references MUID:96033055; PMID:7487897 !$#accession S59137 !'##molecule_type mRNA !'##residues 10-19,'R',21-86 ##label CHW !'##cross-references EMBL:X84194 !'##experimental_source placenta !'##note the authors translated the codon AGG for residue 11 as Gly GENETICS !$#gene GDB:ACYPE !'##cross-references GDB:638808 FUNCTION !$#description catalyzes the hydrolysis of the carboxyl-phosphate bond of !1acylphosphates CLASSIFICATION #superfamily acylphosphatase KEYWORDS acetylated amino end; cytosol; erythrocyte; hydrolase FEATURE !$2-99 #product acylphosphatase #status experimental #label !8MAT\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental SUMMARY #length 99 #molecular-weight 11261 #checksum 6721 SEQUENCE /// ENTRY A61449 #type complete TITLE acylphosphatase (EC 3.6.1.7), testis form 2 - bovine CONTAINS acylphosphatase, testis form 1 ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 07-Oct-1994 #sequence_revision 02-Dec-1994 #text_change 08-Dec-1994 ACCESSIONS A61449 REFERENCE A61449 !$#authors Pazzagli, L.; Cappugi, G.; Camici, G.; Manao, G.; Ramponi, !1G. !$#journal J. Protein Chem. (1993) 12:593-601 !$#title Bovine testis acylphosphatase: purification and amino acid !1sequence. !$#cross-references MUID:94190457; PMID:8142002 !$#accession A61449 !'##molecule_type protein !'##residues 1-100 ##label PAZ CLASSIFICATION #superfamily acylphosphatase KEYWORDS acetylated amino end; hydrolase; testis FEATURE !$1-100 #product acylphosphatase, testis form 2 #status !8experimental #label MAT1\ !$3-100 #product acylphosphatase, testis form 1 #status !8experimental #label MAT2\ !$1 #modified_site acetylated amino end (Ser) #status !8experimental\ !$3 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental SUMMARY #length 100 #molecular-weight 11301 #checksum 9940 SEQUENCE /// ENTRY A45333 #type complete TITLE exopolyphosphatase (EC 3.6.1.11) ppx - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS A45333; E65026 REFERENCE A45333 !$#authors Akiyama, M.; Crooke, E.; Kornberg, A. !$#journal J. Biol. Chem. (1993) 268:633-639 !$#title An exopolyphosphatase of Escherichia coli. The enzyme and !1its ppx gene in a polyphosphate operon. !$#cross-references MUID:93107072; PMID:8380170 !$#accession A45333 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-513 ##label AKI !'##cross-references GB:L06129; NID:g147342; PIDN:AAA24415.1; !1PID:g147343 !'##note sequence extracted from NCBI backbone (NCBIP:121474) REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65026 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-513 ##label BLAT !'##cross-references GB:AE000336; GB:U00096; NID:g1788839; !1PIDN:AAC75555.1; PID:g1788848; UWGP:b2502 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ppx CLASSIFICATION #superfamily exopolyphosphatase KEYWORDS hydrolase SUMMARY #length 513 #molecular-weight 58135 #checksum 574 SEQUENCE /// ENTRY A39216 #type complete TITLE nucleotide diphosphatase (EC 3.6.1.9) - human CONTAINS nucleotide pyrophosphatase (EC 3.6.1.9); phosphodiesterase I (EC 3.1.4.1) ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS A39216; S21706; S23587; S51030 REFERENCE A39216 !$#authors Buckley, M.F.; Loveland, K.A.; McKinstry, W.J.; Garson, !1O.M.; Goding, J.W. !$#journal J. Biol. Chem. (1990) 265:17506-17511 !$#title Plasma cell membrane glycoprotein PC-1. cDNA cloning of the !1human molecule, amino acid sequence, and chromosomal !1location. !$#cross-references MUID:91009202; PMID:2211644 !$#accession A39216 !'##status preliminary !'##molecule_type mRNA !'##residues 1-925 ##label BUC !'##cross-references GB:J05654 REFERENCE S21706 !$#authors Funakoshi, I.; Kato, H.; Horie, K.; Yano, T.; Hori, Y.; !1Kobayashi, H.; Inoue, T.; Suzuki, H.; Fukui, S.; Tsukahara, !1M.; Kajii, T.; Yamashina, I. !$#journal Arch. Biochem. Biophys. (1992) 295:180-187 !$#title Molecular cloning of cDNAs for human fibroblast nucleotide !1pyrophosphatase. !$#cross-references MUID:92246539; PMID:1315502 !$#accession S21706 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-925 ##label FUN1 !$#accession S23587 !'##molecule_type protein !'##residues 116-121;247-271,'X',273-275;279-280,'X', !1282-283;303-316;362-364;449-465;482-525;529-534,'X',536-551, !1'X',553,'X',555-556;597-606;'X',727-730;775-782;840-846, !1'XX',849-852,'X',854-859 ##label FUN2 !'##note it is uncertain whether Met-1 or Met-53 is the initiator REFERENCE S51030 !$#authors Belli, S.I.; Goding, J.W. !$#journal Eur. J. Biochem. (1994) 226:433-443 !$#title Biochemical characterization of human PC-1, an enzyme !1possessing alkaline phosphodiesterase I and nucleotide !1pyrophosphatase activities. !$#cross-references MUID:95094801; PMID:8001561 !$#accession S51030 !'##status preliminary !'##molecule_type mRNA !'##residues 1-80 ##label BEL GENETICS !$#gene GDB:PDNP1; M6S1; NPPS !'##cross-references GDB:132615; OMIM:173335 !$#map_position 6q22-6q23 CLASSIFICATION #superfamily nucleotide pyrophosphatase; somatomedin B !1homology KEYWORDS coenzyme A; glycoprotein; phosphoprotein; phosphoric diester !1hydrolase; transmembrane protein FEATURE !$77-97 #domain transmembrane #status predicted #label TMM\ !$104-144 #domain somatomedin B homology #label SBH1\ !$145-188 #domain somatomedin B homology #label SBH2\ !$179,285,341,477, !$578,585,643,700, !$731,748 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$256 #binding_site AMP (Thr) (covalent) #status predicted SUMMARY #length 925 #molecular-weight 104924 #checksum 7446 SEQUENCE /// ENTRY A27410 #type complete TITLE nucleotide diphosphatase (EC 3.6.1.9) - mouse ALTERNATE_NAMES nucleotide pyrophosphatase (EC 3.6.1.9); phosphodiesterase I (EC 3.1.4.1) ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS A27410; I59055; S38354 REFERENCE A27410 !$#authors van Driel, I.R.; Goding, J.W. !$#journal J. Biol. Chem. (1987) 262:4882-4887 !$#title Plasma cell membrane glycoprotein PC-1. Primary structure !1deduced from cDNA clones. !$#cross-references MUID:87165906; PMID:3104326 !$#accession A27410 !'##molecule_type mRNA !'##residues 1-905 ##label VAN !'##cross-references GB:J02700; NID:g200236; PIDN:AAA39893.1; !1PID:g200237 !'##note the authors translated the codon CAG for residue 24 as Glu REFERENCE I59055 !$#authors van Driel, I.R.; Wilks, A.F.; Pietersz, G.A.; Goding, J.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:8619-8623 !$#title Murine plasma cell membrane antigen PC-1: Molecular cloning !1of cDNA and analysis of expression. !$#cross-references MUID:86094275; PMID:3001713 !$#accession I59055 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 203-219 ##label RES !'##cross-references GB:M12552; NID:g200234; PIDN:AAA39892.1; !1PID:g200235 REFERENCE S38354 !$#authors Belli, S.I.; van Driel, I.R.; Goding, J.W. !$#journal Eur. J. Biochem. (1993) 217:421-428 !$#title Identification and characterization of a soluble form of the !1plasma cell membrane glycoprotein PC-1 (5'-nucleotide !1phosphodiesterase). !$#cross-references MUID:94039066; PMID:8223581 !$#accession S38354 !'##status preliminary !'##molecule_type DNA !'##residues 35-219 ##label BEL !'##cross-references EMBL:L04516 GENETICS !$#introns 62/3; 87/1; 126/1; 168/1; 188/2 CLASSIFICATION #superfamily nucleotide pyrophosphatase; somatomedin B !1homology KEYWORDS coenzyme A; glycoprotein; phosphoprotein; phosphoric diester !1hydrolase; transmembrane protein FEATURE !$86-126 #domain somatomedin B homology #label SBH1\ !$127-170 #domain somatomedin B homology #label SBH2\ !$161,267,323,459, !$567,624 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$238 #binding_site AMP (Thr) (covalent) #status predicted SUMMARY #length 905 #molecular-weight 102880 #checksum 1749 SEQUENCE /// ENTRY A55144 #type complete TITLE autotaxin precursor - human CONTAINS phosphodiesterase I (EC 3.1.4.1) ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A55144; A42329 REFERENCE A55144 !$#authors Murata, J.; Lee, H.Y.; Clair, T.; Krutzsch, H.C.; Arestad, !1A.A.; Sobel, M.E.; Liotta, L.A.; Stracke, M.L. !$#journal J. Biol. Chem. (1994) 269:30479-30484 !$#title cDNA cloning of the human tumor motility-stimulating !1protein, autotaxin, reveals a homology with !1phosphodiesterases. !$#cross-references MUID:95074054; PMID:7982964 !$#accession A55144 !'##molecule_type mRNA !'##residues 1-915 ##label MUR !'##cross-references GB:L35594; NID:g537905; PIDN:AAA64785.1; !1PID:g537906 !'##note parts of this sequence were confirmed by peptide sequencing REFERENCE A42329 !$#authors Stracke, M.L.; Krutzsch, H.C.; Unsworth, E.J.; Arestad, A.; !1Cioce, V.; Schiffmann, E.; Liotta, L.A. !$#journal J. Biol. Chem. (1992) 267:2524-2529 !$#title Identification, purification, and partial sequence analysis !1of autotaxin, a novel motility-stimulating protein. !$#cross-references MUID:92129337; PMID:1733949 !$#accession A42329 !'##molecule_type protein !'##residues 256-266;422-444;504-507,'AN';510,'X',511-515;533-548;'S', !1554-559,'N',561-562;597-601,'X',603-605, !1'L';691-695;758-762;881-892 ##label STR !'##experimental_source A2058 melanoma cells !'##note sequence extracted from NCBI backbone (NCBIP:78526, !1NCBIP:78523, NCBIP:78521, NCBIP:78518, NCBIP:78515, !1NCBIP:78511, NCBIP:78510, NCBIP:78509, NCBIP:78508, !1NCBIP:78503) !'##note a peptide fragment Tyr-Asp-Val-Pro-Trp-Asn-Glu-Thr-Ile was also !1found COMMENT This protein acts as an autocrine factor to stimulate tumor !1cell motility. GENETICS !$#gene GDB:ATX !'##cross-references GDB:378346 !$#map_position 8q22-8qter CLASSIFICATION #superfamily nucleotide pyrophosphatase; somatomedin B !1homology KEYWORDS EF hand; glycoprotein; phosphoprotein; phosphoric diester !1hydrolase FEATURE !$55-98 #domain somatomedin B homology #label SBH1\ !$99-142 #domain somatomedin B homology #label SBH2\ !$54,463,577,859 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$210 #binding_site AMP (Thr) (covalent) #status predicted SUMMARY #length 915 #molecular-weight 105246 #checksum 2939 SEQUENCE /// ENTRY A55453 #type complete TITLE nucleotide diphosphatase (EC 3.6.1.9) - rat CONTAINS nucleotide pyrophosphatase (EC 3.6.1.9); phosphodiesterase I (EC 3.1.4.1) ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS A55453; JU0187 REFERENCE A55453 !$#authors Narita, M.; Goji, J.; Nakamura, H.; Sano, K. !$#journal J. Biol. Chem. (1994) 269:28235-28242 !$#title Molecular cloning, expression, and localization of a !1brain-specific phosphodiesterase I/nucleotide !1pyrophosphatase (PD-Ialpha) from rat brain. !$#cross-references MUID:95050605; PMID:7961762 !$#accession A55453 !'##molecule_type mRNA !'##residues 1-885 ##label NAR !'##cross-references GB:D28560; NID:g464196; PIDN:BAA05910.1; !1PID:g464197 REFERENCE JU0187 !$#authors Narita, M.; Goji, J.; Sano, K.; Nakamura, H. !$#submission submitted to JIPID, February 1994 !$#description Cloning and expression of brain-specific nucleotide !1diphosphohydrolase. !$#accession JU0187 !'##molecule_type mRNA !'##residues 1-66,'Q',68-81,'T',83-94,'C',96,'A',98-195,'A',197-514,'E', !1516-621,'E',623-634,'I',636-842,'C',844-885 ##label NA2 !'##experimental_source strain Sprague-Dawley CLASSIFICATION #superfamily nucleotide pyrophosphatase; somatomedin B !1homology KEYWORDS coenzyme A; exonuclease; glycoprotein; phosphoprotein; !1phosphoric diester hydrolase FEATURE !$54-97 #domain somatomedin B homology #label SBH1\ !$98-141 #domain somatomedin B homology #label SBH2\ !$53,150,396,408,522, !$608,829 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$207 #binding_site AMP (Thr) (covalent) #status predicted SUMMARY #length 885 #molecular-weight 101309 #checksum 6120 SEQUENCE /// ENTRY A57080 #type complete TITLE cell surface antigen RB13-6 - rat CONTAINS phosphodiesterase I (EC 3.1.4.1) ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A57080 REFERENCE A57080 !$#authors Deissler, H.; Lottspeich, F.; Rajewsky, M.F. !$#journal J. Biol. Chem. (1995) 270:9849-9855 !$#title Affinity purification and cDNA cloning of rat neural !1differentiation and tumor cell surface antigen gp130(RB13-6) !1reveals relationship to human and murine PC-1. !$#cross-references MUID:95247775; PMID:7730366 !$#accession A57080 !'##status preliminary !'##molecule_type mRNA !'##residues 1-875 ##label DEI !'##cross-references GB:Z47987; NID:g806378; PIDN:CAA88029.1; !1PID:g806379 CLASSIFICATION #superfamily nucleotide pyrophosphatase; somatomedin B !1homology KEYWORDS exonuclease; glycoprotein; phosphoprotein; phosphoric !1diester hydrolase; surface antigen; transmembrane protein FEATURE !$1-22 #domain cytosolic #status predicted #label CYT\ !$23-45 #domain transmembrane #status predicted #label TMM\ !$46-875 #domain extracellular #status predicted #label EXT\ !$51-94 #domain somatomedin B homology #label SBH\ !$95-138 #domain somatomedin B homology #label SBH2\ !$206 #binding_site AMP (Thr) (covalent) #status predicted\ !$237,280,289,533, !$574,594,702,789 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 875 #molecular-weight 99087 #checksum 9719 SEQUENCE /// ENTRY NPVZ17 #type complete TITLE nucleoside-triphosphatase (EC 3.6.1.15) I - vaccinia virus ALTERNATE_NAMES D11L protein ORGANISM #formal_name vaccinia virus DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 17-Nov-2000 ACCESSIONS A94144; B01146; A34125; A42516; A03887; A03891; A26657 REFERENCE A94144 !$#authors Rodriguez, J.F.; Kahn, J.S.; Esteban, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:9566-9570 !$#title Molecular cloning, encoding sequence, and expression of !1vaccinia virus nucleic acid-dependent nucleoside !1triphosphatase gene. !$#cross-references MUID:87092289; PMID:3025846 !$#accession A94144 !'##molecule_type DNA !'##residues 1-631 ##label ROD !'##cross-references GB:M14629; NID:g335723; PIDN:AAA48301.1; !1PID:g335724 !'##experimental_source strain WR REFERENCE A01146 !$#authors Niles, E.G.; Condit, R.C.; Caro, P.; Davidson, K.; Matusick, !1L.; Seto, J. !$#journal Virology (1986) 153:96-112 !$#title Nucleotide sequence and genetic map of the 16-kb vaccinia !1virus HindIII D fragment. !$#cross-references MUID:86291159; PMID:3739227 !$#accession B01146 !'##molecule_type DNA !'##residues 1-631 ##label NIL !'##cross-references GB:M15058; NID:g335640; PIDN:AAA48267.1; !1PID:g335655 !'##experimental_source strain WR REFERENCE A94623 !$#authors Niles, E.G. !$#submission submitted to the Protein Sequence Database, February 1988 !$#contents annotation; revisions REFERENCE A34125 !$#authors Kahn, J.S.; Esteban, M. !$#journal Virology (1990) 174:459-471 !$#title Identification of the point mutations in two vaccinia virus !1nucleoside triphosphate phosphohydrolase I !1temperature-sensitive mutants and role of this DNA-dependent !1ATPase enzyme in virus gene expression. !$#cross-references MUID:90163214; PMID:2154883 !$#accession A34125 !'##status preliminary !'##molecule_type DNA !'##residues 1-65,'D',67-137,'A',139-205 ##label KAH !'##cross-references GB:M32854; NID:g335725; PIDN:AAA48302.1; !1PID:g335726 !'##experimental_source strain WR REFERENCE A42501 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:517-563 !$#title Appendix to "The complete DNA sequence of vaccinia virus". !$#accession A42516 !'##molecule_type DNA !'##residues 1-328,'N',330-341,'K',343-346,'K',348-567,'K',569-631 !1##label GOE !'##cross-references GB:M35027; NID:g335317; PIDN:AAA48110.1; !1PID:g335458 !'##experimental_source strain Copenhagen REFERENCE A42531 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:247-266 !$#title The complete DNA sequence of vaccinia virus. !$#cross-references MUID:91021027; PMID:2219722 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given FUNCTION !$#description hydrolyzes nucleoside triphosphates to nucleoside !1diphosphates and phosphate !$#note NTPase-I hydrolyzes only ATP or dATP, whereas NTPase-II !1hydrolyzes all four ribo- or deoxyribonucleoside !1triphosphates CLASSIFICATION #superfamily vaccinia virus nucleoside-triphosphatase I KEYWORDS hydrolase SUMMARY #length 631 #molecular-weight 72310 #checksum 7415 SEQUENCE /// ENTRY NPVZCP #type complete TITLE nucleoside-triphosphatase (EC 3.6.1.15) I - Choristoneura biennis poxvirus ORGANISM #formal_name Choristoneura biennis poxvirus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 17-Nov-2000 ACCESSIONS A39154 REFERENCE A39154 !$#authors Yuen, L.; Noiseux, M.; Gomes, M. !$#journal Virology (1991) 182:403-406 !$#title DNA sequence of the nucleoside triphosphate phosphohydrolase !1I (NPH I) of the Choristoneura biennis entomopoxvirus. !$#cross-references MUID:91220681; PMID:1850911 !$#accession A39154 !'##molecule_type DNA !'##residues 1-648 ##label YUE !'##cross-references GB:M60400; NID:g323271; PIDN:AAA42886.1; !1PID:g323272 CLASSIFICATION #superfamily vaccinia virus nucleoside-triphosphatase I KEYWORDS ATP; hydrolase FEATURE !$48-76 #region ATP binding #status predicted\ !$395-424 #region ATP binding #status predicted SUMMARY #length 648 #molecular-weight 76115 #checksum 8656 SEQUENCE /// ENTRY NPVZAM #type complete TITLE nucleoside-triphosphatase (EC 3.6.1.15) I - Amsacta moorei poxvirus ALTERNATE_NAMES G6L protein; spheroidin ORGANISM #formal_name Amsacta moorei poxvirus DATE 31-Dec-1992 #sequence_revision 03-May-1996 #text_change 19-Jan-2001 ACCESSIONS F41561; A44279 REFERENCE A41561 !$#authors Hall, R.L.; Moyer, R.W. !$#journal J. Virol. (1991) 65:6516-6527 !$#title Identification, cloning, and sequencing of a fragment of !1Amsacta moorei entomopoxvirus DNA containing the spheroidin !1gene and three vaccinia virus-related open reading frames. !$#cross-references MUID:92046310; PMID:1942245 !$#accession F41561 !'##molecule_type DNA !'##residues 1-163 ##label HAL !'##cross-references GB:M77182 REFERENCE A44279 !$#authors Hall, R.L.; Moyer, R.W. !$#journal Virology (1993) 192:179-187 !$#title Identification of an Amsacta spheroidin-like protein within !1the occlusion bodies of Choristoneura entomopoxviruses. !$#cross-references MUID:93297103; PMID:8517016 !$#accession A44279 !'##status preliminary !'##molecule_type DNA !'##residues 164-648 ##label HA2 !'##cross-references GB:M77182 CLASSIFICATION #superfamily vaccinia virus nucleoside-triphosphatase I KEYWORDS ATP; hydrolase; nucleotide binding; P-loop FEATURE !$61-68 #region nucleotide-binding motif A (P-loop)\ !$146-151 #region nucleotide-binding motif B\ !$150-153 #region DEXH motif SUMMARY #length 648 #molecular-weight 76108 #checksum 1069 SEQUENCE /// ENTRY WPECDU #type complete TITLE dUTP diphosphatase (EC 3.6.1.23) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 03-Jun-2002 ACCESSIONS A30388; B65165; Q00497 REFERENCE A30388 !$#authors Lundberg, L.G.; Thoresson, H.O.; Karlstroem, O.H.; Nyman, !1P.O. !$#journal EMBO J. (1983) 2:967-971 !$#title Nucleotide sequence of the structural gene for dUTPase of !1Escherichia coli K-12. !$#cross-references MUID:84057777; PMID:6139280 !$#accession A30388 !'##molecule_type DNA !'##residues 1-151 ##label LUN !'##cross-references GB:X01714; NID:g41296; PIDN:CAA25859.1; PID:g41297 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65165 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-151 ##label BLAT !'##cross-references GB:AE000441; GB:U00096; NID:g1790063; !1PIDN:AAC76664.1; PID:g1790071; UWGP:b3640 !'##experimental_source strain K-12, substrain MG1655 COMMENT This enzyme catalyzes the hydrolysis of dUTP (deoxyuridine !15'-triphosphate) to dUMP, the immediate precursor of !1thymidine nucleotides; it is also responsible for decreasing !1the intracellular concentration of dUTP. GENETICS !$#gene dut !$#map_position 82 min CLASSIFICATION #superfamily dUTP pyrophosphatase KEYWORDS hydrolase; nucleotide metabolism SUMMARY #length 151 #molecular-weight 16155 #checksum 3484 SEQUENCE /// ENTRY WZBE8 #type complete TITLE dUTP diphosphatase (EC 3.6.1.23) - human herpesvirus 3 ALTERNATE_NAMES deoxyuridine triphosphatase ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 03-Jun-2002 ACCESSIONS H27212 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession H27212 !'##molecule_type DNA !'##residues 1-396 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27891.1; !1PID:g59997 GENETICS !$#gene 8 CLASSIFICATION #superfamily herpesvirus dUTP pyrophosphatase KEYWORDS hydrolase SUMMARY #length 396 #molecular-weight 44818 #checksum 2657 SEQUENCE /// ENTRY WMBEY0 #type complete TITLE dUTP diphosphatase (EC 3.6.1.23) - human herpesvirus 1 (strain 17) ALTERNATE_NAMES deoxyuridine triphosphatase ORGANISM #formal_name human herpesvirus 1 DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 03-Jun-2002 ACCESSIONS E30089 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession E30089 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-371 ##label MCG !'##cross-references GB:X14112; NID:g1944536; PIDN:CAA32301.1; !1PID:g59550; GB:D00317 GENETICS !$#gene UL50 CLASSIFICATION #superfamily herpesvirus dUTP pyrophosphatase KEYWORDS hydrolase SUMMARY #length 371 #molecular-weight 39128 #checksum 9221 SEQUENCE /// ENTRY QQBE17 #type complete TITLE dUTP diphosphatase (EC 3.6.1.23) - human herpesvirus 4 (strain B95-8) ALTERNATE_NAMES deoxyuridine triphosphatase ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 03-Jun-2002 ACCESSIONS A03758; S33004 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession A03758 !'##molecule_type DNA !'##residues 1-278 ##label BAN !'##cross-references EMBL:V01555; NID:g59074; PIDN:CAA24850.1; !1PID:g1334864 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region CLASSIFICATION #superfamily herpesvirus dUTP pyrophosphatase KEYWORDS hydrolase SUMMARY #length 278 #molecular-weight 30952 #checksum 32 SEQUENCE /// ENTRY WZBEP1 #type complete TITLE dUTP diphosphatase (EC 3.6.1.23) - saimiriine herpesvirus 1 (strain 11) ORGANISM #formal_name saimiriine herpesvirus 1 #note host Saimiri sciureus (common squirrel monkey) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 03-Jun-2002 ACCESSIONS G36811 REFERENCE A36806 !$#authors Albrecht, J. !$#submission submitted to the EMBL Data Library, January 1992 !$#description Primary structure of the herpesvirus saimiri genome. !$#accession G36811 !'##molecule_type DNA !'##residues 1-287 ##label ALB !'##cross-references GB:X64346; NID:g60320; PIDN:CAA45677.1; PID:g60375 REFERENCE A37309 !$#authors Albrecht, J.C.; Nicholas, J.; Biller, D.; Cameron, K.R.; !1Biesinger, B.; Newman, C.; Wittmann, S.; Craxton, M.A.; !1Coleman, H.; Fleckenstein, B.; Honess, R.W. !$#journal J. Virol. (1992) 66:5047-5058 !$#title Primary structure of the herpesvirus saimiri genome. !$#cross-references MUID:92333688; PMID:1321287 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 54 CLASSIFICATION #superfamily herpesvirus dUTP pyrophosphatase KEYWORDS hydrolase SUMMARY #length 287 #molecular-weight 32507 #checksum 532 SEQUENCE /// ENTRY WZBEA8 #type complete TITLE dUTP diphosphatase (EC 3.6.1.23) - equine herpesvirus 1 (strain Ab4p) ALTERNATE_NAMES deoxyuridine triphosphatase ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 03-Jun-2002 ACCESSIONS A36796 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession A36796 !'##molecule_type DNA !'##residues 1-326 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02444.1; !1PID:g330801 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 9 CLASSIFICATION #superfamily herpesvirus dUTP pyrophosphatase KEYWORDS hydrolase SUMMARY #length 326 #molecular-weight 35208 #checksum 531 SEQUENCE /// ENTRY S55649 #type complete TITLE deoxyuridine triphosphatase 54 - equine herpesvirus 2 ORGANISM #formal_name equine herpesvirus 2 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S55649 REFERENCE S55594 !$#authors Telford, E.A.R.; Watson, M.S.; Aird, H.C.; Perry, J.; !1Davison, A.J. !$#journal J. Mol. Biol. (1995) 249:520-528 !$#title The DNA sequence of equine herpesvirus 2. !$#cross-references MUID:95302501; PMID:7783207 !$#accession S55649 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-289 ##label TEL !'##cross-references GB:U20824; NID:g695172; PIDN:AAC13842.1; !1PID:g695227 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1February 1995 CLASSIFICATION #superfamily herpesvirus dUTP pyrophosphatase SUMMARY #length 289 #molecular-weight 32957 #checksum 2683 SEQUENCE /// ENTRY WZBEI1 #type complete TITLE dUTP diphosphatase (EC 3.6.1.23) - ictalurid herpesvirus 1 (strain auburn 1) ALTERNATE_NAMES deoxyuridine triphosphatase ORGANISM #formal_name ictalurid herpesvirus 1 #note host Ictalurus punctatus (channel catfish) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 03-Jun-2002 ACCESSIONS E36791 REFERENCE A36804 !$#authors Davison, A.J. !$#submission submitted to GenBank, January 1992 !$#description Channel catfish virus: a new type of herpesvirus. !$#accession E36791 !'##molecule_type DNA !'##residues 1-188 ##label DAV !'##cross-references GB:M75136; NID:g331209; PIDN:AAA88152.1; !1PID:g331259 REFERENCE A39447 !$#authors Davison, A.J. !$#journal Virology (1992) 186:9-14 !$#title Channel catfish virus: a new type of herpesvirus. !$#cross-references MUID:92087490; PMID:1727613 !$#contents annotation !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 49 CLASSIFICATION #superfamily ictalurid herpesvirus dUTP pyrophosphatase KEYWORDS hydrolase SUMMARY #length 188 #molecular-weight 20128 #checksum 3597 SEQUENCE /// ENTRY PSECCD #type complete TITLE CDPdiacylglycerol diphosphatase (EC 3.6.1.26) - Escherichia coli (strain K-12) ALTERNATE_NAMES CDP-diacylglycerol phosphatidylhydrolase ORGANISM #formal_name Escherichia coli DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 03-Jun-2002 ACCESSIONS A01019; S40861; B94501; C25206; A65198 REFERENCE A01019 !$#authors Icho, T.; Bulawa, C.E.; Raetz, C.R.H. !$#journal J. Biol. Chem. (1985) 260:12092-12098 !$#title Molecular cloning and sequencing of the gene for !1CDP-diglyceride hydrolase of Escherichia coli. !$#cross-references MUID:86008270; PMID:2995360 !$#accession A01019 !'##molecule_type DNA !'##residues 1-251 ##label ICH !'##cross-references GB:M11331; NID:g145471; PIDN:AAA23543.1; !1PID:g145472 REFERENCE S40802 !$#authors Plunkett III, G.; Burland, V.; Daniels, D.L.; Blattner, F.R. !$#journal Nucleic Acids Res. (1993) 21:3391-3398 !$#title Analysis of the Escherichia coli genome. III. DNA sequence !1of the region from 87.2 to 89.2 minutes. !$#cross-references MUID:93347969; PMID:8346018 !$#accession S40861 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-251 ##label PLU !'##cross-references EMBL:L19201; NID:g304961; PIDN:AAB03050.1; !1PID:g305021 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1993 REFERENCE A94501 !$#authors Evans, P.R. !$#submission submitted to the EMBL Data Library, October 1986 !$#accession B94501 !'##molecule_type DNA !'##residues 1-154,'IT','IW',190,'TSAAAGCHCQVVCAGMNTCASGNGKRTGTTQ',192, !1'IYDAGRRST',202-251 ##label EVA REFERENCE A91144 !$#authors Hellinga, H.W.; Evans, P.R. !$#journal Eur. J. Biochem. (1985) 149:363-373 !$#title Nucleotide sequence and high-level expression of the major !1Escherichia coli phosphofructokinase. !$#cross-references MUID:85203917; PMID:3158524 !$#accession C25206 !'##molecule_type DNA !'##residues 1-154,'IT','IW',190,'TSAAAGCHCQVVCAGMNTCASGNGKRTGTTQ',192, !1'IYDAGRRST',202-251 ##label HEL !'##cross-references GB:X02519; NID:g42365; PIDN:CAA26358.1; PID:g42368 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65198 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-251 ##label BLAT !'##cross-references GB:AE000466; GB:U00096; NID:g2367328; !1PIDN:AAC76900.1; PID:g1790352; UWGP:b3918 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene cdh !$#map_position 88 min FUNCTION !$#description catalyzes the cleavage of CDP-diglyceride, the precursor of !1all the glycerophospholipids, to phosphatidic acid and CMP; !1also catalyzes the transfer of CMP from CDP-diglyceride to !1phosphate and numerous phosphomonoesters !$#pathway lipid biosynthesis CLASSIFICATION #superfamily CDPdiacylglycerol pyrophosphatase KEYWORDS hydrolase; lipid biosynthesis; membrane protein SUMMARY #length 251 #molecular-weight 28451 #checksum 7868 SEQUENCE /// ENTRY S04172 #type complete TITLE UDP-sugar hydrolase precursor - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S04172 REFERENCE S04172 !$#authors Garrett, A.R.; Johnson, L.A.; Beacham, I.R. !$#journal Mol. Microbiol. (1989) 3:177-186 !$#title Isolation, molecular characterization and expression of the !1ushB gene of Salmonella typhimurium which encodes a !1membrane-bound UDP-sugar hydrolase. !$#cross-references MUID:89343621; PMID:2548058 !$#accession S04172 !'##molecule_type DNA !'##residues 1-251 ##label GAR !'##cross-references EMBL:X13380; NID:g47954; PIDN:CAA31757.1; !1PID:g47955 GENETICS !$#gene ushB CLASSIFICATION #superfamily CDPdiacylglycerol pyrophosphatase FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-251 #product UDP-sugar hydrolase #status predicted #label !8MAT SUMMARY #length 251 #molecular-weight 28381 #checksum 6191 SEQUENCE /// ENTRY PWHUA #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) alpha chain precursor - human ALTERNATE_NAMES F1-ATPase ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 14-Dec-2001 ACCESSIONS S17193; JN0546; S47519; S20720 REFERENCE S17193 !$#authors Kataoka, H.; Biswas, C. !$#journal Biochim. Biophys. Acta (1991) 1089:393-395 !$#title Nucleotide sequence of a cDNA for the alpha subunit of human !1mitochondrial ATP synthase. !$#cross-references MUID:91316142; PMID:1830491 !$#accession S17193 !'##molecule_type mRNA !'##residues 1-553 ##label KAT !'##cross-references EMBL:X59066; NID:g28937; PIDN:CAA41789.1; !1PID:g28938 REFERENCE JN0546 !$#authors Godbout, R.; Bisgrove, D.A.; Honore, L.H.; Day III, R.S. !$#journal Gene (1993) 123:195-201 !$#title Amplification of the gene encoding the alpha-subunit of the !1mitochondrial ATP synthase complex in a human retinoblastoma !1cell line. !$#cross-references MUID:93154584; PMID:8428659 !$#accession JN0546 !'##molecule_type mRNA !'##residues 1-553 ##label GOD !'##cross-references EMBL:X65460; NID:g34467; PIDN:CAA46452.1; !1PID:g34468 REFERENCE S47519 !$#authors Akiyama, S.; Endo, H.; Inohara, N.; Ohta, S.; Kagawa, Y. !$#journal Biochim. Biophys. Acta (1994) 1219:129-140 !$#title Gene structure and cell type-specific expression of the !1human ATP synthase alpha subunit. !$#cross-references MUID:94368840; PMID:8086450 !$#accession S47519 !'##status preliminary !'##molecule_type DNA !'##residues 1-553 ##label AKI !'##cross-references DDBJ:D28126; NID:g559316; PIDN:BAA05672.1; !1PID:g559317 GENETICS !$#gene GDB:ATP5A1 !'##cross-references GDB:137185 !$#map_position 10pter-10qter !$#introns 20/3; 47/1; 103/3; 161/3; 217/2; 267/1; 317/3; 392/3; 428/3; !1477/1; 527/2 COMPLEX the ATP synthase F1 complex consists of three alpha chains, !1three beta chains (see PIR:A33370), one gamma chain (see !1PIR:A49108), one delta chain (see PIR:S22348), and one !1epsilon chain; the F1 complex binds to the intrinsic !1membrane F0 complex FUNCTION !$#description catalyzes the formation of ATP from ADP and phosphate using !1the free energy derived from proton transport down the !1gradient maintained by cytochrome-c oxidase across the !1mitochondrial inner-membrane !$#pathway oxidative phosphorylation CLASSIFICATION #superfamily H+-transporting ATP synthase alpha chain; !1H+-transporting ATP synthase alpha chain homology KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; nucleotide binding; oxidative !1phosphorylation; P-loop; pyroglutamic acid FEATURE !$1-43 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$44-553 #product H+-transporting ATP synthase alpha chain !8#status predicted #label MAT\ !$212-219 #region nucleotide-binding motif A (P-loop)\ !$245-417 #domain H+-transporting ATP synthase alpha chain !8homology #label ATP\ !$308-313 #region nucleotide-binding motif B\ !$44 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status predicted\ !$218 #binding_site ATP (Lys) #status predicted SUMMARY #length 553 #molecular-weight 59750 #checksum 8066 SEQUENCE /// ENTRY PWBOA #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) alpha chain precursor, cardiac [validated] - bovine ALTERNATE_NAMES F1-ATPase; hydrogen ion-transporting ATPase alpha chain; mitochondrial ATPase alpha chain ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Sep-1991 #sequence_revision 05-Apr-1995 #text_change 14-Dec-2001 ACCESSIONS S27201; A30245; S07275; A35373 REFERENCE S27201 !$#authors Pierce, D.J.; Jordan, E.M.; Breen, G.A.M. !$#journal Biochim. Biophys. Acta (1992) 1132:265-275 !$#title Structural organization of a nuclear gene for the !1alpha-subunit of the bovine mitochondrial ATP synthase !1complex. !$#cross-references MUID:93041927; PMID:1420306 !$#accession S27201 !'##molecule_type DNA !'##residues 1-553 ##label PIE !'##cross-references GB:X64565; NID:g101; PIDN:CAA45865.1; PID:g102 REFERENCE A30245 !$#authors Walker, J.E.; Powell, S.J.; Vinas, O.; Runswick, M.J. !$#journal Biochemistry (1989) 28:4702-4708 !$#title ATP synthase from bovine mitochondria: complementary DNA !1sequence of the import precursor of a heart isoform of the !1alpha subunit. !$#cross-references MUID:89352541; PMID:2527557 !$#accession A30245 !'##molecule_type mRNA !'##residues 1-523,'G',525-553 ##label WAL1 !'##cross-references GB:M22465; GB:J02851; NID:g162720 !'##experimental_source heart REFERENCE S07275 !$#authors Walker, J.E.; Fearnley, I.M.; Gay, N.J.; Gibson, B.W.; !1Northrop, F.D.; Powell, S.J.; Runswick, M.J.; Saraste, M.; !1Tybulewicz, V.L.J. !$#journal J. Mol. Biol. (1985) 184:677-701 !$#title Primary structure and subunit stoichiometry of F(1)-ATPase !1from bovine mitochondria. !$#cross-references MUID:86011574; PMID:2864455 !$#accession S07275 !'##molecule_type protein !'##residues 44-523,'G',525-552 ##label WAL2 !'##experimental_source heart REFERENCE A35373 !$#authors Verburg, J.G.; Allison, W.S. !$#journal J. Biol. Chem. (1990) 265:8065-8074 !$#title Tyrosine alpha244 is derivatized when the bovine heart !1mitochondrial F-1-ATPase is inactivated with !15'-p-fluorosulfonylbenzoylethenoadenosine. !$#cross-references MUID:90243682; PMID:2139876 !$#accession A35373 !'##molecule_type protein !'##residues 270-286,'X',288-294 ##label VER !'##experimental_source heart !'##note Tyr-287 is near the nucleotide binding site but does not !1participate catalytically REFERENCE A65186 !$#authors Abrahams, J.P.; Leslie, A.G.W.; Lutter, R.; Walker, J.E. !$#submission submitted to the Brookhaven Protein Data Bank, March 1996 !$#cross-references PDB:1BMF !$#contents annotation; X-ray crystallography, 2.85 angstroms, residues !167-523,'G',525-553 REFERENCE A65313 !$#authors Van Raaij, M.; Abrahams, J.P.; Leslie, A.G.W.; Walker, J.E. !$#submission submitted to the Brookhaven Protein Data Bank, May 1996 !$#cross-references PDB:1COW !$#contents annotation; X-ray crystallography, 3.1 angstroms, with !1aurovertin B, residues 67-523,'G',525-553 REFERENCE A65505 !$#authors Abrahams, J.P.; Buchanan, S.K.; Van Raaij, M.J.; Fearnley, !1I.M.; Leslie, A.G.W.; Walker, J.E. !$#submission submitted to the Brookhaven Protein Data Bank, May 1996 !$#cross-references PDB:1EFR !$#contents annotation; X-ray crystallography, 3.1 angstroms, with !1efrapeptin, residues 67-523,'G',525-553 REFERENCE A44750 !$#authors Abrahams, J.P.; Leslie, A.G.W.; Lutter, R.; Walker, J.E. !$#journal Nature (1994) 370:621-628 !$#title Structure at 2.8 angstroms resolution of F1-ATPase from !1bovine heart mitochondria. !$#cross-references MUID:94344236; PMID:8065448 !$#contents annotation; X-ray crystallography, 2.8 angstroms; structure !1of complex with alpha, beta and gamma chains REFERENCE S09181 !$#authors Boekema, E.J.; Berden, J.A.; van Heel, M.G. !$#journal Biochim. Biophys. Acta (1986) 851:353-360 !$#title Structure of mitochondrial F(1)-ATPase studied by electron !1microscopy and image processing. !$#cross-references MUID:87000571; PMID:2875733 !$#contents annotation; electron microscopy; image processing GENETICS !$#gene ATPA1 !$#introns 20/3; 47/1; 103/3; 161/3; 217/2; 267/1; 317/3; 392/3; 428/3; !1477/1; 527/2 COMPLEX the ATP synthase F1 complex consists of three alpha chains, !1three beta chains (see PIR:PWBOB), one gamma chain (see !1PIR:PWBOG), one delta chain (see PIR:PWBOD), and one epsilon !1chain (see PIR:PWBOE); the F1 complex binds to the intrinsic !1membrane F0 complex FUNCTION !$#description catalyzes the formation of ATP from ADP and phosphate using !1the free energy derived from proton transport down the !1gradient maintained by cytochrome-c oxidase across the !1mitochondrial inner-membrane !$#pathway oxidative phosphorylation CLASSIFICATION #superfamily H+-transporting ATP synthase alpha chain; !1H+-transporting ATP synthase alpha chain homology KEYWORDS ATP biosynthesis; cardiac muscle; heart; hydrolase; !1membrane-associated complex; mitochondrion; nucleotide !1binding; oxidative phosphorylation; P-loop; pyroglutamic !1acid FEATURE !$1-43 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$44-553 #product H+-transporting ATP synthase alpha chain !8#status experimental #label MAT\ !$212-219 #region nucleotide-binding motif A (P-loop)\ !$245-417 #domain H+-transporting ATP synthase alpha chain !8homology #label ATP\ !$308-313 #region nucleotide-binding motif B\ !$44 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$218 #binding_site ATP (Lys) #status experimental\ !$416 #active_site Arg #status predicted SUMMARY #length 553 #molecular-weight 59719 #checksum 7716 SEQUENCE /// ENTRY PWBYA #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) alpha chain precursor - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES ATPase alpha chain; protein YBL0827; protein YBL099w ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1992 #sequence_revision 09-Sep-1994 #text_change 14-Dec-2001 ACCESSIONS S45401; S45840; A25934; S59198 REFERENCE S45387 !$#authors Obermaier, B.; Gassenhuber, J.; Piravandi, E.; Domdey, H. !$#submission submitted to the EMBL Data Library, May 1994 !$#description Sequence analysis of a 78,6 kb segment of the left end of !1Saccaromyces cerevisiae chromosome II. !$#accession S45401 !'##molecule_type DNA !'##residues 1-545 ##label OBE !'##cross-references EMBL:X79489; NID:g496661; PIDN:CAA56001.1; !1PID:g496674 REFERENCE S45816 !$#authors Domdey, H.; Gassenhuber, H.; Obermaier, B.; Piravandi, E. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S45840 !'##molecule_type DNA !'##residues 1-545 ##label DOM !'##cross-references EMBL:Z35861; NID:g536163; PIDN:CAA84924.1; !1PID:g536167; GSPDB:GN00002; MIPS:YBL099w REFERENCE A25934 !$#authors Takeda, M.; Chen, W.J.; Saltzgaber, J.; Douglas, M.G. !$#journal J. Biol. Chem. (1986) 261:15126-15133 !$#title Nuclear genes encoding the yeast mitochondrial ATPase !1complex. !$#cross-references MUID:87033754; PMID:2876995 !$#accession A25934 !'##molecule_type DNA !'##residues 1-310,'ASL',314-320,'M',322-339,'S',341-384,'A',386-458, !1'Q',460-478,'SMI',482,484-489,'SGWY',494-545 ##label TAK !'##cross-references EMBL:J02603; NID:g171115; PIDN:AAA66888.1; !1PID:g171116 REFERENCE S59184 !$#authors Obermaier, B.; Gassenhuber, J.; Piravandi, E.; Domdey, H. !$#journal Yeast (1995) 11:1103-1112 !$#title Sequence analysis of a 78.6 kb segment of the left end of !1Saccharomyces cerevisiae chromosome II. !$#cross-references MUID:96076635; PMID:7502586 !$#accession S59198 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-545 ##label OBW !'##cross-references EMBL:X79489; NID:g496661; PIDN:CAA56001.1; !1PID:g496674 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1May 1994 GENETICS !$#gene SGD:ATP1; MIPS:YBL099w !'##cross-references SGD:S0000195; MIPS:YBL099w !$#map_position 2L !$#genome nuclear FUNCTION !$#description catalyzes the formation of ATP from ADP and phosphate using !1the free energy derived from proton transport down the !1gradient maintained by cytochrome-c oxidase across the !1mitochondrial inner-membrane !$#pathway oxidative phosphorylation CLASSIFICATION #superfamily H+-transporting ATP synthase alpha chain; !1H+-transporting ATP synthase alpha chain homology KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; nucleotide binding; oxidative !1phosphorylation; P-loop FEATURE !$1-31 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$32-545 #product H+-transporting ATP synthase alpha chain !8#status predicted #label MAT\ !$206-213 #region nucleotide-binding motif A (P-loop)\ !$239-411 #domain H+-transporting ATP synthase alpha chain !8homology #label ATP\ !$302-307 #region nucleotide-binding motif B\ !$212 #binding_site ATP (Lys) #status predicted\ !$410 #active_site Arg #status predicted SUMMARY #length 545 #molecular-weight 58617 #checksum 2007 SEQUENCE /// ENTRY A39036 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) alpha chain precursor - fission yeast (Schizosaccharomyces pombe) ORGANISM #formal_name Schizosaccharomyces pombe DATE 23-Aug-1991 #sequence_revision 04-Nov-1994 #text_change 14-Dec-2001 ACCESSIONS A39036; A45782; T37699 REFERENCE A39036 !$#authors Falson, P.; Maffey, L.; Conrath, K.; Boutry, M. !$#journal J. Biol. Chem. (1991) 266:287-293 !$#title alpha subunit of mitochondrial F-1-ATPase from the fission !1yeast. !$#cross-references MUID:91093138; PMID:1824697 !$#accession A39036 !'##molecule_type DNA !'##residues 1-536 ##label FAL !'##cross-references GB:M57955; GB:J05715; NID:g173346; PIDN:AAA35286.1; !1PID:g173347 REFERENCE A45782 !$#authors Divita, G.; Jault, J.M.; Gautheron, D.C.; Di Pietro, A. !$#journal Biochemistry (1993) 32:1017-1024 !$#title Chemical modification of alpha-subunit tryptophan residues !1in Schizosaccharomyces pombe mitochondrial F-1 adenosine !15'-triphosphatase: differential reactivity and role in !1activity. !$#cross-references MUID:93144302; PMID:8424930 !$#accession A45782 !'##molecule_type protein !'##residues 28-38;282-292 ##label DIV REFERENCE Z21737 !$#authors Devlin, K.; Churcher, C.M.; Barrell, B.G.; Rajandream, M.A.; !1Wood, V. !$#submission submitted to the EMBL Data Library, August 1997 !$#accession T37699 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-536 ##label DEV !'##cross-references EMBL:Z98596; PIDN:CAB11207.1; GSPDB:GN00066; !1SPDB:SPAC14C4.14 !'##experimental_source strain 972h-; cosmid c14C4 GENETICS !$#gene atp1 !$#map_position 1 !$#genome nuclear !$#introns 21/3; 41/3 FUNCTION !$#description catalyzes the formation of ATP from ADP and phosphate using !1the free energy derived from proton transport down the !1gradient maintained by cytochrome-c oxidase across the !1mitochondrial inner-membrane !$#pathway oxidative phosphorylation CLASSIFICATION #superfamily H+-transporting ATP synthase alpha chain; !1H+-transporting ATP synthase alpha chain homology KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; nucleotide binding; oxidative !1phosphorylation; P-loop FEATURE !$1-27 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$28-536 #product H+-transporting ATP synthase alpha chain !8#status experimental #label MAT\ !$197-204 #region nucleotide-binding motif A (P-loop)\ !$230-402 #domain H+-transporting ATP synthase alpha chain !8homology #label ATP\ !$293-297 #region nucleotide-binding motif B\ !$203 #binding_site ATP (Lys) #status predicted\ !$401 #active_site Arg #status predicted SUMMARY #length 536 #molecular-weight 58587 #checksum 1747 SEQUENCE /// ENTRY PWECA #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) alpha chain - Escherichia coli (strain K-12) ALTERNATE_NAMES hydrogen ion-transporting ATPase alpha chain ORGANISM #formal_name Escherichia coli DATE 23-Oct-1981 #sequence_revision 21-Nov-1997 #text_change 01-Mar-2002 ACCESSIONS G65176; A93726; A90103; I41275; T45006; A01020 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65176 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-513 ##label BLAT !'##cross-references GB:AE000450; GB:U00096; NID:g1790166; !1PIDN:AAC76757.1; PID:g1790172; UWGP:b3734 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A93726 !$#authors Gay, N.J.; Walker, J.E. !$#journal Nucleic Acids Res. (1981) 9:2187-2194 !$#title The atp operon: nucleotide sequence of the region encoding !1the alpha-subunit of Escherichia coli ATP-synthase. !$#cross-references MUID:82059532; PMID:6272228 !$#accession A93726 !'##molecule_type DNA !'##residues 1-176,'R',178-238,'RMPVAL',245-299,'MLQ',303-513 ##label !1GAY !'##cross-references GB:V00265; NID:g41029; PIDN:CAA23519.1; PID:g41030 REFERENCE A90103 !$#authors Kanazawa, H.; Kayano, T.; Mabuchi, K.; Futai, M. !$#journal Biochem. Biophys. Res. Commun. (1981) 103:604-612 !$#title Nucleotide sequence of the genes coding for alpha, beta and !1gamma subunits of the proton-translocating ATPase of !1Escherichia coli. !$#cross-references MUID:82134798; PMID:6277310 !$#accession A90103 !'##molecule_type DNA !'##residues 1-238,'RMPVAL',245-513 ##label KAN !'##cross-references GB:V00312; NID:g42282; PIDN:CAA23596.1; PID:g42283 REFERENCE I41271 !$#authors Kanazawa, H.; Futai, M. !$#journal Ann. N. Y. Acad. Sci. (1982) 402:45-64 !$#title Structure and function of H+-ATPase: What we have learned !1from Escherichia coli H+-ATPase. !$#cross-references MUID:83176724; PMID:6301339 !$#accession I41275 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-90,'I',92-238,'RMPVAL',245-513 ##label RES !'##cross-references GB:M25464; NID:g146318; PIDN:AAA83873.1; !1PID:g146323 REFERENCE Z22893 !$#authors Nielsen, J.; Hansen, F.G.; Hoppe, J.; Friedl, P.; Von !1Meyenburg, K. !$#journal Mol. Gen. Genet. (1981) 184:33-39 !$#title The nucleotide sequence of the atp genes coding for the F-0 !1subunits a, b, c and the F-1 subunit delta of the membrane !1bound ATP synthase of Escherichia coli. !$#cross-references MUID:82147764; PMID:6278247 !$#accession T45006 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-50 ##label NIE !'##cross-references EMBL:V00266; NID:g41031; PIDN:CAA23525.1; !1PID:g41035 COMMENT This is one of the five chains of the enzymatic component !1(F1) of the ATPase complex. GENETICS !$#gene atpA; uncA !$#map_position 84 min CLASSIFICATION #superfamily H+-transporting ATP synthase alpha chain; !1H+-transporting ATP synthase alpha chain homology KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1nucleotide binding; oxidative phosphorylation; P-loop FEATURE !$169-176 #region nucleotide-binding motif A (P-loop)\ !$194-377 #domain H+-transporting ATP synthase alpha chain !8homology #label ATP\ !$257-262 #region nucleotide-binding motif B\ !$175 #binding_site ATP (Lys) #status predicted\ !$376 #active_site Arg #status predicted SUMMARY #length 513 #molecular-weight 55222 #checksum 9348 SEQUENCE /// ENTRY PWQFA #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) alpha chain - Rhodospirillum rubrum ORGANISM #formal_name Rhodospirillum rubrum DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 14-Dec-2001 ACCESSIONS S08581; S29220 REFERENCE S07132 !$#authors Falk, G.; Hampe, A.; Walker, J.E. !$#journal Biochem. J. (1985) 228:391-407 !$#title Nucleotide sequence of the Rhodospirillum rubrum atp operon. !$#cross-references MUID:85251588; PMID:2861810 !$#accession S08581 !'##molecule_type DNA !'##residues 1-510 ##label FAL !'##cross-references EMBL:X02499; NID:g46360; PIDN:CAA26338.1; !1PID:g46366 REFERENCE S29220 !$#authors Andralojc, P.J.; Harris, D.A. !$#journal FEBS Lett. (1992) 310:187-192 !$#title Isolation and characterisation of a functional alphabeta !1heterodimer from the ATP synthase of Rhodospirillum rubrum. !$#cross-references MUID:93011913; PMID:1327870 !$#accession S29220 !'##status preliminary !'##molecule_type protein !'##residues 1-15 ##label AND GENETICS !$#gene atpA CLASSIFICATION #superfamily H+-transporting ATP synthase alpha chain; !1H+-transporting ATP synthase alpha chain homology KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1nucleotide binding; oxidative phosphorylation; P-loop FEATURE !$169-176 #region nucleotide-binding motif A (P-loop)\ !$203-375 #domain H+-transporting ATP synthase alpha chain !8homology #label ATP\ !$266-271 #region nucleotide-binding motif B\ !$175 #binding_site ATP (Lys) #status predicted\ !$374 #active_site Arg #status predicted SUMMARY #length 510 #molecular-weight 55026 #checksum 5288 SEQUENCE /// ENTRY PWYCA #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) alpha chain - Synechococcus sp. (strain PCC 6301) ORGANISM #formal_name Synechococcus sp. DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 14-Dec-2001 ACCESSIONS S10831 REFERENCE S07286 !$#authors Cozens, A.L.; Walker, J.E. !$#journal J. Mol. Biol. (1987) 194:359-383 !$#title The organization and sequence of the genes for ATP synthase !1subunits in the cyanobacterium Synechococcus 6301. Support !1for an endosymbiotic origin of chloroplasts. !$#cross-references MUID:87311713; PMID:3041005 !$#accession S10831 !'##molecule_type DNA !'##residues 1-505 ##label COZ !'##cross-references EMBL:X05302; NID:g48009; PIDN:CAA28928.1; !1PID:g48017 CLASSIFICATION #superfamily H+-transporting ATP synthase alpha chain; !1H+-transporting ATP synthase alpha chain homology KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1nucleotide binding; oxidative phosphorylation; P-loop FEATURE !$170-177 #region nucleotide-binding motif A (P-loop)\ !$195-367 #domain H+-transporting ATP synthase alpha chain !8homology #label ATP\ !$258-263 #region nucleotide-binding motif B\ !$176 #binding_site ATP (Lys) #status predicted\ !$366 #active_site Arg #status predicted SUMMARY #length 505 #molecular-weight 54072 #checksum 4596 SEQUENCE /// ENTRY PWYBA #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) alpha chain - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES ATP synthase chain a ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 14-Dec-2001 ACCESSIONS S17751; S74583; S14866 REFERENCE S17745 !$#authors Lill, H.; Nelson, N. !$#journal Plant Mol. Biol. (1991) 17:641-652 !$#title The atp1 and atp2 operons of the cyanobacterium !1Synechocystis sp. PCC 6803. !$#cross-references MUID:92003679; PMID:1832989 !$#accession S17751 !'##molecule_type DNA !'##residues 1-503 ##label LIL !'##cross-references EMBL:X58128; NID:g47506; PIDN:CAA41135.1; !1PID:g47513 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74583 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-503 ##label KAN !'##cross-references EMBL:D90900; GB:AB001339; NID:g1651768; !1PIDN:BAA16735.1; PID:g1651808 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene atpA CLASSIFICATION #superfamily H+-transporting ATP synthase alpha chain; !1H+-transporting ATP synthase alpha chain homology KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1nucleotide binding; oxidative phosphorylation; P-loop FEATURE !$170-177 #region nucleotide-binding motif A (P-loop)\ !$195-367 #domain H+-transporting ATP synthase alpha chain !8homology #label ATP\ !$258-263 #region nucleotide-binding motif B\ !$176 #binding_site ATP (Lys) #status predicted\ !$366 #active_site Arg #status predicted SUMMARY #length 503 #molecular-weight 53965 #checksum 34 SEQUENCE /// ENTRY PWRPA #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) alpha chain - rape mitochondrion ORGANISM #formal_name mitochondrion Brassica napus #common_name rape DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 14-Dec-2001 ACCESSIONS S13382; S30090 REFERENCE S13382 !$#authors Handa, H.; Nakajima, K. !$#journal Plant Mol. Biol. (1991) 16:361-364 !$#title Nucleotide sequence and transcription analyses of the !1rapeseed (Brassica napus L.) mitochondrial F(1)-ATPase !1alpha-subunit gene. !$#cross-references MUID:91370881; PMID:1832575 !$#accession S13382 !'##molecule_type DNA !'##residues 1-507 ##label HAN !'##cross-references EMBL:X56008; NID:g19553; PIDN:CAA39483.1; !1PID:g19554 !'##experimental_source strain Polima REFERENCE S30089 !$#authors Bonhomme, S.; Budar, F.; Lancelin, D.; Small, I.; Defrance, !1M.C.; Pelletier, G. !$#journal Mol. Gen. Genet. (1992) 235:340-348 !$#title Sequence and transcript analysis of the Nco2.5 !1Ogura-specific fragment correlated with cytoplasmic male !1sterility in Brassica cybrids. !$#cross-references MUID:93101139; PMID:1281515 !$#accession S30090 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-111 ##label BON !'##cross-references EMBL:Z12627; NID:g14388; PIDN:CAA78274.1; !1PID:g14389 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1992 GENETICS !$#gene atpA !$#genome mitochondrion CLASSIFICATION #superfamily H+-transporting ATP synthase alpha chain; !1H+-transporting ATP synthase alpha chain homology KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; nucleotide binding; oxidative !1phosphorylation; P-loop FEATURE !$171-178 #region nucleotide-binding motif A (P-loop)\ !$205-377 #domain H+-transporting ATP synthase alpha chain !8homology #label ATP\ !$268-273 #region nucleotide-binding motif B\ !$177 #binding_site ATP (Lys) #status predicted\ !$376 #active_site Arg #status predicted SUMMARY #length 507 #molecular-weight 55142 #checksum 4264 SEQUENCE /// ENTRY PWNTAC #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) alpha chain - curled-leaved tobacco mitochondrion ORGANISM #formal_name mitochondrion Nicotiana plumbaginifolia #common_name curled-leaved tobacco DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 14-Dec-2001 ACCESSIONS S00956 REFERENCE S00956 !$#authors Chaumont, F.; Boutry, M.; Briquet, M.; Vassarotti, A. !$#journal Nucleic Acids Res. (1988) 16:6247 !$#title Sequence of the gene encoding the mitochondrial F1-ATPase !1alpha subunit from Nicotiana plumbaginifolia. !$#cross-references MUID:88289387; PMID:2899872 !$#accession S00956 !'##molecule_type DNA !'##residues 1-509 ##label CHA !'##cross-references EMBL:X07745; NID:g13152; PIDN:CAA30568.1; !1PID:g13153 GENETICS !$#gene atpA !$#genome mitochondrion CLASSIFICATION #superfamily H+-transporting ATP synthase alpha chain; !1H+-transporting ATP synthase alpha chain homology KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; nucleotide binding; oxidative !1phosphorylation; P-loop FEATURE !$171-178 #region nucleotide-binding motif A (P-loop)\ !$205-377 #domain H+-transporting ATP synthase alpha chain !8homology #label ATP\ !$268-273 #region nucleotide-binding motif B\ !$177 #binding_site ATP (Lys) #status predicted\ !$376 #active_site Arg #status predicted SUMMARY #length 509 #molecular-weight 55225 #checksum 3863 SEQUENCE /// ENTRY PWWTAM #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) alpha chain - wheat mitochondrion ORGANISM #formal_name mitochondrion Triticum aestivum #common_name common wheat DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 14-Dec-2001 ACCESSIONS S06007 REFERENCE S06007 !$#authors Schulte, E.; Staubach, S.; Laser, B.; Kueck, U. !$#journal Nucleic Acids Res. (1989) 17:7531 !$#title Wheat mitochondrial DNA: organization and sequences of the !1atpA and atp9 genes. !$#cross-references MUID:90016824; PMID:2529479 !$#accession S06007 !'##status translation not shown !'##molecule_type DNA !'##residues 1-509 ##label SCH !'##cross-references EMBL:X15918 GENETICS !$#gene atpA !$#genome mitochondrion CLASSIFICATION #superfamily H+-transporting ATP synthase alpha chain; !1H+-transporting ATP synthase alpha chain homology KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; nucleotide binding; oxidative !1phosphorylation; P-loop FEATURE !$171-178 #region nucleotide-binding motif A (P-loop)\ !$205-377 #domain H+-transporting ATP synthase alpha chain !8homology #label ATP\ !$268-273 #region nucleotide-binding motif B\ !$177 #binding_site ATP (Lys) #status predicted\ !$376 #active_site Arg #status predicted SUMMARY #length 509 #molecular-weight 55264 #checksum 6126 SEQUENCE /// ENTRY PWZMAM #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) alpha chain - maize mitochondrion ALTERNATE_NAMES ATPase alpha chain ORGANISM #formal_name mitochondrion Zea mays #common_name maize DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 14-Dec-2001 ACCESSIONS A23757 REFERENCE A23757 !$#authors Braun, C.J.; Levings III, C.S. !$#journal Plant Physiol. (1985) 79:571-577 !$#title Nucleotide sequence of the F1-ATPase alpha subunit gene from !1maize mitochondria. !$#accession A23757 !'##molecule_type DNA !'##residues 1-508 ##label BRA !'##cross-references EMBL:M16222; NID:g342633; PIDN:AAA70269.1; !1PID:g897619 GENETICS !$#gene atpA !$#genome mitochondrion CLASSIFICATION #superfamily H+-transporting ATP synthase alpha chain; !1H+-transporting ATP synthase alpha chain homology KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; nucleotide binding; oxidative !1phosphorylation; P-loop FEATURE !$171-178 #region nucleotide-binding motif A (P-loop)\ !$205-377 #domain H+-transporting ATP synthase alpha chain !8homology #label ATP\ !$268-273 #region nucleotide-binding motif B\ !$177 #binding_site ATP (Lys) #status predicted\ !$376 #active_site Arg #status predicted SUMMARY #length 508 #molecular-weight 55180 #checksum 9847 SEQUENCE /// ENTRY PWRZAM #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) alpha chain - rice mitochondrion ORGANISM #formal_name mitochondrion Oryza sativa #common_name rice DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 14-Dec-2001 ACCESSIONS JQ0411 REFERENCE JQ0411 !$#authors Kadowaki, K.; Kazama, S.; Suzuki, T. !$#journal Nucleic Acids Res. (1990) 18:1302 !$#title Nucleotide sequence of the F1-ATPase alpha subunit gene from !1rice mitochondria. !$#cross-references MUID:90206808; PMID:2138730 !$#accession JQ0411 !'##molecule_type DNA !'##residues 1-509 ##label KAD !'##cross-references EMBL:X51422; NID:g13958; PIDN:CAA35787.1; !1PID:g13959 GENETICS !$#gene atpA !$#genome mitochondrion CLASSIFICATION #superfamily H+-transporting ATP synthase alpha chain; !1H+-transporting ATP synthase alpha chain homology KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; nucleotide binding; oxidative !1phosphorylation; P-loop FEATURE !$171-178 #region nucleotide-binding motif A (P-loop)\ !$205-377 #domain H+-transporting ATP synthase alpha chain !8homology #label ATP\ !$268-273 #region nucleotide-binding motif B\ !$177 #binding_site ATP (Lys) #status predicted\ !$376 #active_site Arg #status predicted SUMMARY #length 509 #molecular-weight 55281 #checksum 3841 SEQUENCE /// ENTRY PWLVA #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) alpha chain - liverwort (Marchantia polymorpha) chloroplast ALTERNATE_NAMES hydrogen ion-transporting ATPase alpha chain ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 14-Dec-2001 ACCESSIONS A01021; S01580 REFERENCE A00150 !$#authors Ohyama, K. !$#submission submitted to the EMBL Data Library, October 1986 !$#accession A01021 !'##molecule_type DNA !'##residues 1-507 ##label OHY REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features REFERENCE S01567 !$#authors Umesono, K.; Inokuchi, H.; Shiki, Y.; Takeuchi, M.; Chang, !1Z.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Ohyama, K.; Ozeki, !1H. !$#journal J. Mol. Biol. (1988) 203:299-331 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. II. Gene organization of the large !1single copy region from rps'12 to atpB. !$#cross-references MUID:89068686; PMID:2974085 !$#accession S01580 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-507 ##label UME !'##cross-references GB:X04465; GB:Y00686; NID:g11640; PIDN:CAA28068.1; !1PID:g11655 COMMENT This is one of the five chains of the enzymatic component !1(coupling factor CF1) of the chloroplast ATPase complex, !1which is bound to the chloroplast thylakoid membrane. GENETICS !$#gene atpA !$#genome chloroplast CLASSIFICATION #superfamily H+-transporting ATP synthase alpha chain; !1H+-transporting ATP synthase alpha chain homology KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; nucleotide binding; oxidative !1phosphorylation; P-loop; thylakoid FEATURE !$170-177 #region nucleotide-binding motif A (P-loop)\ !$195-367 #domain H+-transporting ATP synthase alpha chain !8homology #label ATP\ !$258-263 #region nucleotide-binding motif B\ !$176 #binding_site ATP (Lys) #status predicted\ !$366 #active_site Arg #status predicted SUMMARY #length 507 #molecular-weight 55312 #checksum 5879 SEQUENCE /// ENTRY PWNTA #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) alpha chain - common tobacco chloroplast ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 14-Dec-2001 ACCESSIONS A01022; S65738; S65737; T02950 REFERENCE A01022 !$#authors Deno, H.; Shinozaki, K.; Sugiura, M. !$#journal Nucleic Acids Res. (1983) 11:2185-2191 !$#title Nucleotide sequence of tobacco chloroplst gene for the alpha !1subunit of proton-translocating ATPase. !$#cross-references MUID:83168953; PMID:6300797 !$#accession A01022 !'##molecule_type DNA !'##residues 1-507 ##label DEN !'##cross-references GB:V00162; GB:J01447; NID:g11768; PIDN:CAA23471.1; !1PID:g11769 !'##experimental_source cv. Bright Yellow 4 REFERENCE S65735 !$#authors Hirose, T.; Fan, H.; Suzuki, J.Y.; Wakasugi, T.; Tsudzuki, !1T.; Koessel, H.; Sugiura, M. !$#journal Plant Mol. Biol. (1996) 30:667-672 !$#title Occurrence of silent RNA editing in chloroplasts: its !1species specificity and the influence of environmental and !1developmental conditions. !$#cross-references MUID:96189279; PMID:8605316 !$#accession S65738 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type mRNA !'##residues 260-263,'L',265-269 ##label HIR !'##note 264-Leu is due to RNA editing !$#accession S65737 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type DNA !'##residues 260-269 ##label HIW REFERENCE A45834 !$#authors Hayashi, H.; Ooba, T.; Nakayama, S.; Sekimata, M.; Kano, K.; !1Takiguchi, M. !$#journal Immunogenetics (1990) 32:195-199 !$#title Allospecificities between HLA-Bw53 and HLA-B35 are generated !1by substitution of the residues associated with HLA-Bw4/Bw6 !1public epitopes. !$#cross-references MUID:91033941; PMID:1699887 !$#accession T02950 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-33 ##label DE2 !'##cross-references EMBL:M10124; NID:g343483; PIDN:AAA84684.1; !1PID:g552957 GENETICS !$#gene atpA !$#genome chloroplast CLASSIFICATION #superfamily H+-transporting ATP synthase alpha chain; !1H+-transporting ATP synthase alpha chain homology KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; nucleotide binding; oxidative !1phosphorylation; P-loop; thylakoid FEATURE !$170-177 #region nucleotide-binding motif A (P-loop)\ !$195-367 #domain H+-transporting ATP synthase alpha chain !8homology #label ATP\ !$258-263 #region nucleotide-binding motif B\ !$176 #binding_site ATP (Lys) #status predicted\ !$366 #active_site Arg #status predicted SUMMARY #length 507 #molecular-weight 55438 #checksum 7272 SEQUENCE /// ENTRY PWSPA #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) alpha chain - spinach chloroplast ORGANISM #formal_name chloroplast Spinacia oleracea #common_name spinach DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 14-Dec-2001 ACCESSIONS S00584; S14422; S17224 REFERENCE S00581 !$#authors Hudson, G.S.; Mason, J.G.; Holton, T.A.; Koller, B.; Cox, !1G.B.; Whitfeld, P.R.; Bottomley, W. !$#journal J. Mol. Biol. (1987) 196:283-298 !$#title A gene cluster in the spinach and pea chloroplast genomes !1encoding one CF-1 and three CF-0 subunits of the H(+)-ATP !1synthase complex and the ribosomal protein S2. !$#cross-references MUID:88011330; PMID:2443718 !$#accession S00584 !'##molecule_type DNA !'##residues 1-507 ##label HUD !'##cross-references EMBL:X05916; NID:g12255; PIDN:CAA29346.1; !1PID:g12261 REFERENCE S00420 !$#authors Hennig, J.; Herrmann, R.G. !$#journal Mol. Gen. Genet. (1986) 203:117-128 !$#title Chloroplast ATP synthase of spinach contains nine !1nonidentical subunit species, six of which are encoded by !1plastid chromosomes in two operons in a phylogenetically !1conserved arrangement. !$#accession S14422 !'##molecule_type DNA !'##residues 1-83 ##label HEN !'##cross-references EMBL:X03775; NID:g12249; PIDN:CAA27403.1; !1PID:g12254 REFERENCE S17224 !$#authors Horbach, M.; Meyer, H.E.; Bickel-Sandkoetter, S. !$#journal Eur. J. Biochem. (1991) 200:449-456 !$#title Inactivation of chloroplast H(+)-ATPase by modification of !1Lys-beta-359, Lys-alpha-176 and Lys-alpha-266. !$#cross-references MUID:91364694; PMID:1832378 !$#accession S17224 !'##molecule_type protein !'##residues 158-170,'XX',173-175,'X',177;221-229;252-261 ##label HOR GENETICS !$#gene atpA !$#genome chloroplast CLASSIFICATION #superfamily H+-transporting ATP synthase alpha chain; !1H+-transporting ATP synthase alpha chain homology KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; nucleotide binding; oxidative !1phosphorylation; P-loop; thylakoid FEATURE !$170-177 #region nucleotide-binding motif A (P-loop)\ !$195-367 #domain H+-transporting ATP synthase alpha chain !8homology #label ATP\ !$258-263 #region nucleotide-binding motif B\ !$176 #binding_site ATP (Lys) #status predicted\ !$366 #active_site Arg #status predicted SUMMARY #length 507 #molecular-weight 55451 #checksum 5706 SEQUENCE /// ENTRY PWPMA #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) alpha chain - garden pea chloroplast ORGANISM #formal_name chloroplast Pisum sativum #common_name garden pea DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 14-Dec-2001 ACCESSIONS S00588 REFERENCE S00581 !$#authors Hudson, G.S.; Mason, J.G.; Holton, T.A.; Koller, B.; Cox, !1G.B.; Whitfeld, P.R.; Bottomley, W. !$#journal J. Mol. Biol. (1987) 196:283-298 !$#title A gene cluster in the spinach and pea chloroplast genomes !1encoding one CF-1 and three CF-0 subunits of the H(+)-ATP !1synthase complex and the ribosomal protein S2. !$#cross-references MUID:88011330; PMID:2443718 !$#accession S00588 !'##molecule_type DNA !'##residues 1-501 ##label HUD !'##cross-references EMBL:X05917; NID:g12139; PIDN:CAA29352.1; !1PID:g12143 GENETICS !$#gene atpA !$#genome chloroplast CLASSIFICATION #superfamily H+-transporting ATP synthase alpha chain; !1H+-transporting ATP synthase alpha chain homology KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; nucleotide binding; oxidative !1phosphorylation; P-loop; thylakoid FEATURE !$170-177 #region nucleotide-binding motif A (P-loop)\ !$195-367 #domain H+-transporting ATP synthase alpha chain !8homology #label ATP\ !$258-263 #region nucleotide-binding motif B\ !$176 #binding_site ATP (Lys) #status predicted\ !$366 #active_site Arg #status predicted SUMMARY #length 501 #molecular-weight 54625 #checksum 7761 SEQUENCE /// ENTRY PWRZA #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) alpha chain - rice chloroplast ALTERNATE_NAMES ATPase alpha chain ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 14-Dec-2001 ACCESSIONS JQ0220; S05100 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0220 !'##molecule_type DNA !'##residues 1-507 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05100 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-507 ##label HIR !'##cross-references EMBL:X15901; NID:g11957; PIDN:CAA33993.1; !1PID:g11979 !'##experimental_source cv. Nihonbare GENETICS !$#gene atpA !$#map_position CP34210-35733 !$#genome chloroplast CLASSIFICATION #superfamily H+-transporting ATP synthase alpha chain; !1H+-transporting ATP synthase alpha chain homology KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; nucleotide binding; oxidative !1phosphorylation; P-loop; thylakoid FEATURE !$170-177 #region nucleotide-binding motif A (P-loop)\ !$195-367 #domain H+-transporting ATP synthase alpha chain !8homology #label ATP\ !$258-263 #region nucleotide-binding motif B\ !$176 #binding_site ATP (Lys) #status predicted\ !$366 #active_site Arg #status predicted SUMMARY #length 507 #molecular-weight 55664 #checksum 4930 SEQUENCE /// ENTRY PWZMA #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) alpha chain - maize chloroplast ORGANISM #formal_name chloroplast Zea mays #common_name maize DATE 31-Dec-1990 #sequence_revision 31-Mar-1993 #text_change 14-Dec-2001 ACCESSIONS S06291; S58549 REFERENCE S06291 !$#authors Rodermel, S.R.; Bogorad, L. !$#journal Genetics (1987) 116:127-139 !$#title Molecular evolution and nucleotide sequences of the maize !1plastid genes for the alpha subunit of CF(1) (atpA) and the !1proteolipid subunit of CF(0) (atpH). !$#cross-references MUID:87248033; PMID:2885245 !$#accession S06291 !'##molecule_type DNA !'##residues 1-507 ##label ROD !'##cross-references EMBL:X05255; NID:g12402; PIDN:CAA28876.1; !1PID:g12403 REFERENCE S58531 !$#authors Maier, R.M.; Neckermann, K.; Igloi, G.L.; Koessel, H. !$#journal J. Mol. Biol. (1995) 251:614-628 !$#title Complete sequence of the maize chloroplast genome: gene !1content, hotspots of divergence and fine tuning of genetic !1information by transcript editing. !$#cross-references MUID:95395841; PMID:7666415 !$#accession S58549 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-507 ##label MAI !'##cross-references EMBL:X86563; NID:g902200; PIDN:CAA60283.1; !1PID:g902219 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1995 GENETICS !$#gene atpA !$#genome chloroplast CLASSIFICATION #superfamily H+-transporting ATP synthase alpha chain; !1H+-transporting ATP synthase alpha chain homology KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; nucleotide binding; oxidative !1phosphorylation; P-loop; peripheral membrane protein; !1thylakoid FEATURE !$170-177 #region nucleotide-binding motif A (P-loop)\ !$195-367 #domain H+-transporting ATP synthase alpha chain !8homology #label ATP\ !$258-263 #region nucleotide-binding motif B\ !$176 #binding_site ATP (Lys) #status predicted\ !$366 #active_site Arg #status predicted SUMMARY #length 507 #molecular-weight 55706 #checksum 6977 SEQUENCE /// ENTRY PWWTA #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) alpha chain - wheat chloroplast ORGANISM #formal_name chloroplast Triticum aestivum #common_name common wheat DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 14-Dec-2001 ACCESSIONS S09351 REFERENCE S07399 !$#authors Howe, C.J.; Fearnley, I.M.; Walker, J.E.; Dyer, T.A.; Gray, !1J.C. !$#journal Plant Mol. Biol. (1985) 4:333-345 !$#title Nucleotide sequences of the genes for the alpha, beta and !1epsilon subunits of wheat chloroplast ATP synthase. !$#accession S09351 !'##molecule_type DNA !'##residues 1-504 ##label HOW !'##cross-references EMBL:M16842; NID:g343674; PIDN:AAA84725.1; !1PID:g552976 GENETICS !$#genome chloroplast CLASSIFICATION #superfamily H+-transporting ATP synthase alpha chain; !1H+-transporting ATP synthase alpha chain homology KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; nucleotide binding; oxidative !1phosphorylation; P-loop; thylakoid FEATURE !$170-177 #region nucleotide-binding motif A (P-loop)\ !$195-367 #domain H+-transporting ATP synthase alpha chain !8homology #label ATP\ !$258-263 #region nucleotide-binding motif B\ !$176 #binding_site ATP (Lys) #status predicted\ !$366 #active_site Arg #status predicted SUMMARY #length 504 #molecular-weight 55264 #checksum 5543 SEQUENCE /// ENTRY PWKMA #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) alpha chain - Chlamydomonas reinhardtii chloroplast ALTERNATE_NAMES adenosinetriphosphatase ORGANISM #formal_name chloroplast Chlamydomonas reinhardtii DATE 31-Mar-1992 #sequence_revision 18-Jul-1997 #text_change 14-Dec-2001 ACCESSIONS S20503; A05002; S17093; S68388 REFERENCE S20503 !$#authors Leu, S.; Schlesinger, J.; Michaels, A.; Shavit, N. !$#journal Plant Mol. Biol. (1992) 18:613-616 !$#title Complete DNA sequence of the Chlamydomonas reinhardtii !1chloroplast atpA gene. !$#cross-references MUID:92163030; PMID:1531617 !$#accession S20503 !'##molecule_type DNA !'##residues 1-508 ##label LEU !'##cross-references GB:X60298; NID:g11427 REFERENCE A92892 !$#authors Dron, M.; Rahire, M.; Rochaix, J.D. !$#journal J. Mol. Biol. (1982) 162:775-793 !$#title Sequence of the chloroplast DNA region of Chlamydomonas !1reinhardtii containing the gene of the large subunit of !1ribulose bisphosphate carboxylase and parts of its flanking !1genes. !$#cross-references MUID:83189072; PMID:6302265 !$#accession A05002 !'##molecule_type DNA !'##residues 1-112 ##label DRO !'##cross-references GB:J01399; NID:g336683 REFERENCE S17093 !$#authors Leu, S.; Schlesinger, J.; Michaels, A.; Shavit, N. !$#submission submitted to the EMBL Data Library, September 1991 !$#accession S17093 !'##molecule_type DNA !'##residues 55-112,'A',114-508 ##label LEW !'##cross-references EMBL:X60298; NID:g11427; PIDN:CAA42840.1; !1PID:g1334356 REFERENCE S68388 !$#authors Fiedler, H.R.; Schmid, R.; Leu, S.; Shavit, N.; Strotmann, !1H. !$#journal FEBS Lett. (1995) 377:163-166 !$#title Isolation of CF(0)CF(1) from Chlamydomonas reinhardtii cw15 !1and the N-terminal amino acid sequences of the CF(0)CF(1) !1subunits. !$#cross-references MUID:96128220; PMID:8543042 !$#accession S68388 !'##molecule_type protein !'##residues 2-9,'XX',12-13 ##label FIE !'##experimental_source strain CW15 GENETICS !$#gene atpA !$#genome chloroplast CLASSIFICATION #superfamily H+-transporting ATP synthase alpha chain; !1H+-transporting ATP synthase alpha chain homology KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; nucleotide binding; oxidative !1phosphorylation; P-loop; peripheral membrane protein; !1thylakoid FEATURE !$170-177 #region nucleotide-binding motif A (P-loop)\ !$195-367 #domain H+-transporting ATP synthase alpha chain !8homology #label ATP\ !$258-263 #region nucleotide-binding motif B #status atypical\ !$176 #binding_site ATP (Lys) #status predicted\ !$366 #active_site Arg #status predicted SUMMARY #length 508 #molecular-weight 54777 #checksum 9178 SEQUENCE /// ENTRY PWEGA #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) alpha chain - Euglena gracilis chloroplast ALTERNATE_NAMES ATP synthase CF1 alpha chain ORGANISM #formal_name chloroplast Euglena gracilis DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 14-Dec-2001 ACCESSIONS S29801; S34536; S34903; S26093 REFERENCE S29797 !$#authors Drager, R.G.; Hallick, R.B. !$#journal Curr. Genet. (1993) 23:271-280 !$#title A novel Euglena gracilis chloroplast operon encoding four !1ATP synthase subunits and two ribosomal proteins contains 17 !1introns. !$#cross-references MUID:93169691; PMID:8435857 !$#accession S29801 !'##molecule_type DNA !'##residues 1-506 ##label DRA !'##cross-references GB:Z11874; GB:S55425; NID:g14353; PIDN:CAA77932.1; !1PID:g14382 REFERENCE S34494 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.; Monfort, !1A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#submission submitted to the EMBL Data Library, January 1993 !$#description The complete sequence of the Euglena gracilis chloroplast !1genome (tentative). !$#accession S34536 !'##molecule_type DNA !'##residues 1-506 ##label HAL1 !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50115.1; !1PID:g415771 REFERENCE S34862 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.R.; !1Monfort, A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#journal Nucleic Acids Res. (1993) 21:3537-3544 !$#title Complete sequence of Euglena gracilis chloroplast DNA. !$#cross-references MUID:93347989; PMID:8346031 !$#accession S34903 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-506 ##label HAL2 !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50115.1; !1PID:g415771 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1993 GENETICS !$#gene atpA !$#genome chloroplast !$#introns 251/1; 265/3 CLASSIFICATION #superfamily H+-transporting ATP synthase alpha chain; !1H+-transporting ATP synthase alpha chain homology KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; nucleotide binding; oxidative !1phosphorylation; P-loop; thylakoid FEATURE !$170-177 #region nucleotide-binding motif A (P-loop)\ !$195-367 #domain H+-transporting ATP synthase alpha chain !8homology #label ATP\ !$258-263 #region nucleotide-binding motif B\ !$176 #binding_site ATP (Lys) #status predicted\ !$366 #active_site Arg #status predicted SUMMARY #length 506 #molecular-weight 55187 #checksum 87 SEQUENCE /// ENTRY PWECB #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) beta chain - Escherichia coli (strain K-12) ALTERNATE_NAMES ATPase F(1) subunit beta chain; hydrogen ion-transporting ATPase beta chain ORGANISM #formal_name Escherichia coli DATE 06-Jul-1982 #sequence_revision 06-Jul-1982 #text_change 01-Mar-2002 ACCESSIONS A93742; A90106; S02748; I41277; E65176; A01023 REFERENCE A93742 !$#authors Saraste, M.; Gay, N.J.; Eberle, A.; Runswick, M.J.; Walker, !1J.E. !$#journal Nucleic Acids Res. (1981) 9:5287-5296 !$#title The atp operon: nucleotide sequence of the genes for the !1gamma,beta, and epsilon subunits of Escherichia coli ATP !1synthase. !$#cross-references MUID:82059507; PMID:6272217 !$#accession A93742 !'##molecule_type DNA !'##residues 1-460 ##label SAR !'##cross-references GB:V00267; NID:g41036; PIDN:CAA23527.1; PID:g41038 REFERENCE A90106 !$#authors Kanazawa, H.; Kayano, T.; Kiyasu, T.; Futai, M. !$#journal Biochem. Biophys. Res. Commun. (1982) 105:1257-1264 !$#title Nucleotide sequence of the genes for beta and epsilon !1subunits of proton-translocating ATPase from Escherichia !1coli. !$#cross-references MUID:82256510; PMID:6285901 !$#accession A90106 !'##molecule_type DNA !'##residues 1-460 ##label KAN !'##cross-references GB:J01594; GB:J01595; GB:K02181; GB:M25634; !1GB:V00264; GB:V00313; GB:X00771; NID:g148131; !1PIDN:AAA24737.1; PID:g148139; GB:V00311; NID:g42276; !1PID:g42277 !'##note the authors translated the codon GAG for residue 212 as Gln REFERENCE S02748 !$#authors Wise, J.G.; Hicke, B.J.; Boyer, P.D. !$#journal FEBS Lett. (1987) 223:395-401 !$#title Catalytic and noncatalytic nucleotide binding sites of the !1Escherichia coli F1 ATPase. Amino acid sequences of !1beta-subunit tryptic peptides labeled with 2-azido-ATP. !$#cross-references MUID:88030084; PMID:2889623 !$#accession S02748 !'##molecule_type protein !'##residues 325-359 ##label WIS REFERENCE I41271 !$#authors Kanazawa, H.; Futai, M. !$#journal Ann. N. Y. Acad. Sci. (1982) 402:45-64 !$#title Structure and function of H+-ATPase: What we have learned !1from Escherichia coli H+-ATPase. !$#cross-references MUID:83176724; PMID:6301339 !$#accession I41277 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-460 ##label RES !'##cross-references GB:M25464; NID:g146318; PIDN:AAA83875.1; !1PID:g146325 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65176 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-460 ##label BLAT !'##cross-references GB:AE000450; GB:U00096; NID:g1790166; !1PIDN:AAC76755.1; PID:g1790170; UWGP:b3732 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene atpD; uncD !$#map_position 84 min COMPLEX this is one of the five chains of the enzymatic component !1(F1) of the ATPase complex CLASSIFICATION #superfamily H+-transporting ATP synthase alpha chain; !1H+-transporting ATP synthase alpha chain homology KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1nucleotide binding; P-loop FEATURE !$150-157 #region nucleotide-binding motif A (P-loop)\ !$176-344 #domain H+-transporting ATP synthase alpha chain !8homology #label ATP SUMMARY #length 460 #molecular-weight 50325 #checksum 5707 SEQUENCE /// ENTRY PWLVB #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) beta chain - liverwort (Marchantia polymorpha) chloroplast ALTERNATE_NAMES hydrogen ion-transporting ATPase beta chain ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 14-Dec-2001 ACCESSIONS A01024; S01597 REFERENCE A00150 !$#authors Ohyama, K. !$#submission submitted to the EMBL Data Library, October 1986 !$#accession A01024 !'##molecule_type DNA !'##residues 1-492 ##label OHY REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features REFERENCE S01567 !$#authors Umesono, K.; Inokuchi, H.; Shiki, Y.; Takeuchi, M.; Chang, !1Z.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Ohyama, K.; Ozeki, !1H. !$#journal J. Mol. Biol. (1988) 203:299-331 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. II. Gene organization of the large !1single copy region from rps'12 to atpB. !$#cross-references MUID:89068686; PMID:2974085 !$#accession S01597 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-492 ##label UME !'##cross-references GB:X04465; GB:Y00686; NID:g11640; PIDN:CAA28091.1; !1PID:g11679 COMMENT This is one of the five chains of the enzymatic component !1(coupling factor CF1) of the chloroplast ATPase complex, !1which is bound to the chloroplast thylakoid membrane. GENETICS !$#gene atpB !$#genome chloroplast CLASSIFICATION #superfamily H+-transporting ATP synthase alpha chain; !1H+-transporting ATP synthase alpha chain homology KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; nucleotide binding; P-loop; !1thylakoid FEATURE !$170-177 #region nucleotide-binding motif A (P-loop)\ !$196-372 #domain H+-transporting ATP synthase alpha chain !8homology #label ATP SUMMARY #length 492 #molecular-weight 53180 #checksum 8528 SEQUENCE /// ENTRY PWFNBT #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) beta chain - turnip fern chloroplast ORGANISM #formal_name chloroplast Angiopteris lygodiifolia #common_name turnip fern DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 14-Dec-2001 ACCESSIONS S19228 REFERENCE S19228 !$#authors Yoshinaga, K.; Kubota, Y.; Ishii, T.; Wada, K. !$#journal Plant Mol. Biol. (1992) 18:79-82 !$#title Nucleotide sequence of atpB, rbcL, trnR, dedB and psaI !1chloroplast genes from a fern Angiopteris lygodiifolia: a !1possible emergence of Spermatophyta lineage before the !1separation of Bryophyta and Pteridophyta. !$#cross-references MUID:92119238; PMID:1731980 !$#accession S19228 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-492 ##label YOS !'##cross-references EMBL:X58429; NID:g11189; PIDN:CAA41331.1; !1PID:g11190 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1March 1991 GENETICS !$#gene atpB !$#genome chloroplast CLASSIFICATION #superfamily H+-transporting ATP synthase alpha chain; !1H+-transporting ATP synthase alpha chain homology KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; nucleotide binding; P-loop; !1thylakoid FEATURE !$170-177 #region nucleotide-binding motif A (P-loop)\ !$196-372 #domain H+-transporting ATP synthase alpha chain !8homology #label ATP SUMMARY #length 492 #molecular-weight 52838 #checksum 9116 SEQUENCE /// ENTRY PWZMB #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) beta chain - maize chloroplast ALTERNATE_NAMES hydrogen ion-transporting ATPase beta chain ORGANISM #formal_name chloroplast Zea mays #common_name maize DATE 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 14-Dec-2001 ACCESSIONS A01025; S58559 REFERENCE A93437 !$#authors Krebbers, E.T.; Larrinua, I.M.; McIntosh, L.; Bogorad, L. !$#journal Nucleic Acids Res. (1982) 10:4985-5002 !$#title The maize chloroplast genes for the beta and epsilon !1subunits of the photosynthetic coupling factor CF-1 are !1fused. !$#cross-references MUID:83038650; PMID:6290998 !$#accession A01025 !'##molecule_type DNA !'##residues 1-498 ##label KRE !'##cross-references GB:J01421; NID:g342576; PIDN:AAA85356.1; !1PID:g552732 !'##note this is one of the five chains of the enzymatic component !1(coupling factor CF1) of the chloroplast ATPase complex, !1which is bound to the chloroplast thylakoid membrane; the !1sequence is 67% identical with its counterpart from E. coli REFERENCE S58531 !$#authors Maier, R.M.; Neckermann, K.; Igloi, G.L.; Koessel, H. !$#journal J. Mol. Biol. (1995) 251:614-628 !$#title Complete sequence of the maize chloroplast genome: gene !1content, hotspots of divergence and fine tuning of genetic !1information by transcript editing. !$#cross-references MUID:95395841; PMID:7666415 !$#accession S58559 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-498 ##label MAI !'##cross-references EMBL:X86563; NID:g902200; PIDN:CAA60293.1; !1PID:g902229 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1995 GENETICS !$#gene atpB !$#genome chloroplast CLASSIFICATION #superfamily H+-transporting ATP synthase alpha chain; !1H+-transporting ATP synthase alpha chain homology KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; nucleotide binding; P-loop; !1peripheral membrane protein; thylakoid FEATURE !$172-179 #region nucleotide-binding motif A (P-loop)\ !$198-374 #domain H+-transporting ATP synthase alpha chain !8homology #label ATP SUMMARY #length 498 #molecular-weight 54040 #checksum 8172 SEQUENCE /// ENTRY PWWTB #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) beta chain - wheat chloroplast ORGANISM #formal_name chloroplast Triticum aestivum #common_name common wheat DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 14-Dec-2001 ACCESSIONS S07399 REFERENCE S07399 !$#authors Howe, C.J.; Fearnley, I.M.; Walker, J.E.; Dyer, T.A.; Gray, !1J.C. !$#journal Plant Mol. Biol. (1985) 4:333-345 !$#title Nucleotide sequences of the genes for the alpha, beta and !1epsilon subunits of wheat chloroplast ATP synthase. !$#accession S07399 !'##molecule_type DNA !'##residues 1-498 ##label HOW !'##cross-references EMBL:M16843; NID:g343676; PIDN:AAA84726.1; !1PID:g473690 GENETICS !$#genome chloroplast CLASSIFICATION #superfamily H+-transporting ATP synthase alpha chain; !1H+-transporting ATP synthase alpha chain homology KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; nucleotide binding; P-loop; !1thylakoid FEATURE !$172-179 #region nucleotide-binding motif A (P-loop)\ !$198-374 #domain H+-transporting ATP synthase alpha chain !8homology #label ATP SUMMARY #length 498 #molecular-weight 53857 #checksum 8486 SEQUENCE /// ENTRY PWBHB #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) beta chain - barley chloroplast ALTERNATE_NAMES hydrogen ion-transporting ATPase beta chain ORGANISM #formal_name chloroplast Hordeum vulgare #common_name barley DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 14-Dec-2001 ACCESSIONS A01026; S07243 REFERENCE A93509 !$#authors Zurawski, G.; Clegg, M.T. !$#journal Nucleic Acids Res. (1984) 12:2549-2559 !$#title The barley chloroplast DNA atpBE, trnM2, and trnV1 loci. !$#cross-references MUID:84169555; PMID:6231529 !$#accession A01026 !'##molecule_type DNA !'##residues 1-498 ##label ZUR !'##cross-references GB:X00408; NID:g11582; PIDN:CAA25114.1; PID:g11583 REFERENCE S07243 !$#authors Zurawski, G.; Clegg, M.T.; Brown, A.H.D. !$#journal Genetics (1984) 106:735-749 !$#title The nature of nucleotide sequence divergence between barley !1and maize chloroplast DNA. !$#accession S07243 !'##status translation not shown !'##molecule_type DNA !'##residues 1-37 ##label ZU2 !'##cross-references EMBL:X00630 COMMENT This is one of the five chains of the enzymatic component !1(coupling factor CF1) of the chloroplast ATPase complex, !1which is bound to the chloroplast thylakoid membrane; the !1sequence is 63% identical with its counterpart from E. coli. GENETICS !$#gene atpB !$#genome chloroplast CLASSIFICATION #superfamily H+-transporting ATP synthase alpha chain; !1H+-transporting ATP synthase alpha chain homology KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; nucleotide binding; P-loop; !1thylakoid FEATURE !$172-179 #region nucleotide-binding motif A (P-loop)\ !$198-374 #domain H+-transporting ATP synthase alpha chain !8homology #label ATP SUMMARY #length 498 #molecular-weight 53875 #checksum 8281 SEQUENCE /// ENTRY PWRZB #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) beta chain - rice chloroplast ALTERNATE_NAMES ATPase beta chain ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 14-Dec-2001 ACCESSIONS JQ0230; S05110; JQ0591 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0230 !'##molecule_type DNA !'##residues 1-498 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05110 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-498 ##label HIR !'##cross-references EMBL:X15901; NID:g11957; PIDN:CAA34003.1; !1PID:g11991 !'##experimental_source cv. Nihonbare REFERENCE JQ0591 !$#authors Nishizawa, Y.; Hirai, A. !$#journal Jpn. J. Genet. (1989) 64:223-229 !$#title The nucleotide sequences and expression of genes for the !1beta and epsilon subunits of ATP synthase from rice (Oryza !1sativa L.). !$#cross-references MUID:90212087; PMID:2534354 !$#accession JQ0591 !'##molecule_type DNA !'##residues 1-498 ##label NIS !'##cross-references GB:D00432; NID:g344013; PIDN:BAA00334.1; !1PID:g344014 GENETICS !$#gene atpB !$#map_position CP53310-51814 !$#genome chloroplast CLASSIFICATION #superfamily H+-transporting ATP synthase alpha chain; !1H+-transporting ATP synthase alpha chain homology KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; nucleotide binding; P-loop; !1thylakoid FEATURE !$172-179 #region nucleotide-binding motif A (P-loop)\ !$198-374 #domain H+-transporting ATP synthase alpha chain !8homology #label ATP SUMMARY #length 498 #molecular-weight 54013 #checksum 9623 SEQUENCE /// ENTRY PWNTB #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) beta chain - common tobacco chloroplast ALTERNATE_NAMES CF1-beta; coupling factor-1 beta; proton-ATPase beta subunit ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 14-Dec-2001 ACCESSIONS A01027; S15726; A43264 REFERENCE A91502 !$#authors Shinozaki, K.; Deno, H.; Kato, A.; Sugiura, M. !$#journal Gene (1983) 24:147-155 !$#title Overlap and cotranscription of the genes for the beta and !1epsilon subunits of tobacco chloroplast ATPase. !$#cross-references MUID:84059075; PMID:6227526 !$#accession A01027 !'##molecule_type DNA !'##residues 1-498 ##label SHI !'##cross-references EMBL:K00507; NID:g343480; PIDN:AAA84676.1; !1PID:g552954 !'##experimental_source variety BY4 REFERENCE S15722 !$#authors Avni, A.; Anderson, J.D.; Rochhaix, J.D.; Edelman, M. !$#submission submitted to the EMBL Data Library, July 1991 !$#description The receptor site for tentoxin sensitivity in chloroplasts. !$#accession S15726 !'##molecule_type DNA !'##residues 1-498 ##label AVN !'##cross-references EMBL:X61319; NID:g11788; PIDN:CAA43612.1; !1PID:g11789 REFERENCE A43264 !$#authors Avni, A.; Anderson, J.D.; Holland, N.; Rochaix, J.D.; !1Gromet-Elhanan, Z.; Edelman, M. !$#journal Science (1992) 257:1245-1247 !$#title Tentoxin sensitivity of chloroplasts determined by codon 83 !1of beta subunit of proton-ATPase. !$#cross-references MUID:92390714; PMID:1387730 !$#accession A43264 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type DNA !'##residues 1-76,'V',78-153,'K',155-498 ##label AV2 !'##experimental_source var. Xanthi, tentoxin-resistant !'##note sequence extracted from NCBI backbone (NCBIP:112485) !'##note variants of Nicotiana sp. and engineered sequences with Glu-83 !1showed tentoxin resistance, while those with Asp-83 showed !1sensitivity GENETICS !$#genome chloroplast CLASSIFICATION #superfamily H+-transporting ATP synthase alpha chain; !1H+-transporting ATP synthase alpha chain homology KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; nucleotide binding; P-loop; !1thylakoid FEATURE !$172-179 #region nucleotide-binding motif A (P-loop)\ !$198-374 #domain H+-transporting ATP synthase alpha chain !8homology #label ATP SUMMARY #length 498 #molecular-weight 53554 #checksum 8600 SEQUENCE /// ENTRY PWNTBB #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) beta chain - Bigelov's tobacco chloroplast ORGANISM #formal_name chloroplast Nicotiana bigelovii #common_name Bigelov's tobacco DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 14-Dec-2001 ACCESSIONS S15722 REFERENCE S15722 !$#authors Avni, A.; Anderson, J.D.; Rochhaix, J.D.; Edelman, M. !$#submission submitted to the EMBL Data Library, July 1991 !$#description The receptor site for tentoxin sensitivity in chloroplasts. !$#accession S15722 !'##molecule_type DNA !'##residues 1-498 ##label AVN !'##cross-references EMBL:X61316; NID:g11745; PIDN:CAA43609.1; !1PID:g11746 GENETICS !$#gene atpB !$#genome chloroplast CLASSIFICATION #superfamily H+-transporting ATP synthase alpha chain; !1H+-transporting ATP synthase alpha chain homology KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; nucleotide binding; P-loop; !1thylakoid FEATURE !$172-179 #region nucleotide-binding motif A (P-loop)\ !$198-374 #domain H+-transporting ATP synthase alpha chain !8homology #label ATP SUMMARY #length 498 #molecular-weight 53525 #checksum 9074 SEQUENCE /// ENTRY PWNTBC #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) beta chain - curled-leaved tobacco chloroplast ORGANISM #formal_name chloroplast Nicotiana plumbaginifolia #common_name curled-leaved tobacco DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 14-Dec-2001 ACCESSIONS S15723 REFERENCE S15722 !$#authors Avni, A.; Anderson, J.D.; Rochhaix, J.D.; Edelman, M. !$#submission submitted to the EMBL Data Library, July 1991 !$#description The receptor site for tentoxin sensitivity in chloroplasts. !$#accession S15723 !'##molecule_type DNA !'##residues 1-498 ##label AVN !'##cross-references EMBL:X61320; NID:g11756; PIDN:CAA43613.1; !1PID:g11757 GENETICS !$#gene atpB !$#genome chloroplast CLASSIFICATION #superfamily H+-transporting ATP synthase alpha chain; !1H+-transporting ATP synthase alpha chain homology KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; nucleotide binding; P-loop; !1thylakoid FEATURE !$172-179 #region nucleotide-binding motif A (P-loop)\ !$198-374 #domain H+-transporting ATP synthase alpha chain !8homology #label ATP SUMMARY #length 498 #molecular-weight 53525 #checksum 9074 SEQUENCE /// ENTRY PWNTB9 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) beta chain - tobacco chloroplast ORGANISM #formal_name chloroplast Nicotiana sp. #common_name tobacco DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 14-Dec-2001 ACCESSIONS S15725 REFERENCE S15722 !$#authors Avni, A.; Anderson, J.D.; Rochhaix, J.D.; Edelman, M. !$#submission submitted to the EMBL Data Library, July 1991 !$#description The receptor site for tentoxin sensitivity in chloroplasts. !$#accession S15725 !'##molecule_type DNA !'##residues 1-498 ##label AVN !'##cross-references EMBL:X61317; NID:g11765; PIDN:CAA43610.1; !1PID:g11766 GENETICS !$#gene atpB !$#genome chloroplast CLASSIFICATION #superfamily H+-transporting ATP synthase alpha chain; !1H+-transporting ATP synthase alpha chain homology KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; nucleotide binding; P-loop; !1thylakoid FEATURE !$172-179 #region nucleotide-binding motif A (P-loop)\ !$198-374 #domain H+-transporting ATP synthase alpha chain !8homology #label ATP SUMMARY #length 498 #molecular-weight 53584 #checksum 9022 SEQUENCE /// ENTRY PWNTBZ #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) beta chain - Aztec tobacco chloroplast ORGANISM #formal_name chloroplast Nicotiana rustica #common_name Aztec tobacco DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 14-Dec-2001 ACCESSIONS S15724 REFERENCE S15722 !$#authors Avni, A.; Anderson, J.D.; Rochhaix, J.D.; Edelman, M. !$#submission submitted to the EMBL Data Library, July 1991 !$#description The receptor site for tentoxin sensitivity in chloroplasts. !$#accession S15724 !'##molecule_type DNA !'##residues 1-498 ##label AVN !'##cross-references EMBL:X61318; NID:g11763; PIDN:CAA43611.1; !1PID:g11764 GENETICS !$#gene atpB !$#genome chloroplast CLASSIFICATION #superfamily H+-transporting ATP synthase alpha chain; !1H+-transporting ATP synthase alpha chain homology KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; nucleotide binding; P-loop; !1thylakoid FEATURE !$172-179 #region nucleotide-binding motif A (P-loop)\ !$198-374 #domain H+-transporting ATP synthase alpha chain !8homology #label ATP SUMMARY #length 498 #molecular-weight 53470 #checksum 8908 SEQUENCE /// ENTRY PWSPB #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) beta chain - spinach chloroplast ALTERNATE_NAMES hydrogen ion-transporting ATPase beta chain ORGANISM #formal_name chloroplast Spinacia oleracea #common_name spinach DATE 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 14-Dec-2001 ACCESSIONS A01028; S17645; S27228 REFERENCE A93929 !$#authors Zurawski, G.; Bottomley, W.; Whitfeld, P.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:6260-6264 !$#title Structures of the genes for the beta and epsilon subunits of !1spinach chloroplast ATPase indicate a dicistronic mRNA and !1an overlapping translation stop/start signal. !$#accession A01028 !'##molecule_type DNA !'##residues 1-498 ##label ZUR !'##cross-references GB:J01441; NID:g343354; PIDN:AAA84626.1; !1PID:g343355 !'##note this is one of the five chains of the enzymatic component (CF1) !1of the chloroplast ATPase complex; the sequence is 67% !1identical with its counterpart from E. coli REFERENCE S17224 !$#authors Horbach, M.; Meyer, H.E.; Bickel-Sandkoetter, S. !$#journal Eur. J. Biochem. (1991) 200:449-456 !$#title Inactivation of chloroplast H(+)-ATPase by modification of !1Lys-beta-359, Lys-alpha-176 and Lys-alpha-266. !$#cross-references MUID:91364694; PMID:1832378 !$#accession S17645 !'##molecule_type protein !'##residues 'XX',295-302;'XX',309-311,'X',313-314,'X',316-319,'X',321, !1'X';375-383 ##label HOR REFERENCE S27228 !$#authors Michel, L.; Garin, J.; Girault, G.; Vignais, P.V. !$#journal FEBS Lett. (1992) 313:90-93 !$#title Photolabeling of the phosphate binding site of chloroplast !1coupling factor 1 with [(32)P]azidonitrophenyl phosphate. !$#cross-references MUID:93050228; PMID:1426274 !$#accession S27228 !'##molecule_type protein !'##residues 313-354 ##label MIC GENETICS !$#genome chloroplast CLASSIFICATION #superfamily H+-transporting ATP synthase alpha chain; !1H+-transporting ATP synthase alpha chain homology KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; nucleotide binding; P-loop; !1thylakoid FEATURE !$172-179 #region nucleotide-binding motif A (P-loop)\ !$198-374 #domain H+-transporting ATP synthase alpha chain !8homology #label ATP SUMMARY #length 498 #molecular-weight 53867 #checksum 7902 SEQUENCE /// ENTRY PWPFBL #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) beta chain - brown alga (Pylaiella littoralis) chloroplast ORGANISM #formal_name chloroplast Pylaiella littoralis DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 14-Dec-2001 ACCESSIONS S20848; S17102 REFERENCE S20848 !$#authors Jouannic, S.; Kerbourc'h, C.; Kloareg, B.; Loiseaux-de Goer, !1S. !$#journal Plant Mol. Biol. (1992) 18:819-822 !$#title Nucleotide sequences of the atpB and the atpE genes of the !1brown alga Pylaiella littoralis (L.) Kjellm. !$#cross-references MUID:92216062; PMID:1532750 !$#accession S20848 !'##molecule_type DNA !'##residues 1-481 ##label JOU !'##cross-references EMBL:X60329; NID:g14180; PIDN:CAA42899.1; !1PID:g14181 GENETICS !$#gene atpB !$#genome chloroplast CLASSIFICATION #superfamily H+-transporting ATP synthase alpha chain; !1H+-transporting ATP synthase alpha chain homology KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; nucleotide binding; P-loop; !1thylakoid FEATURE !$161-168 #region nucleotide-binding motif A (P-loop)\ !$187-363 #domain H+-transporting ATP synthase alpha chain !8homology #label ATP SUMMARY #length 481 #molecular-weight 52025 #checksum 1572 SEQUENCE /// ENTRY PWYCB #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) beta chain - Synechococcus sp. (strain PCC 6301) ORGANISM #formal_name Synechococcus sp. DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 14-Dec-2001 ACCESSIONS S10837 REFERENCE S07286 !$#authors Cozens, A.L.; Walker, J.E. !$#journal J. Mol. Biol. (1987) 194:359-383 !$#title The organization and sequence of the genes for ATP synthase !1subunits in the cyanobacterium Synechococcus 6301. Support !1for an endosymbiotic origin of chloroplasts. !$#cross-references MUID:87311713; PMID:3041005 !$#accession S10837 !'##molecule_type DNA !'##residues 1-484 ##label COZ !'##cross-references EMBL:X05925; NID:g48021; PIDN:CAA29362.1; !1PID:g48024 CLASSIFICATION #superfamily H+-transporting ATP synthase alpha chain; !1H+-transporting ATP synthase alpha chain homology KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1nucleotide binding; P-loop FEATURE !$162-169 #region nucleotide-binding motif A (P-loop)\ !$188-364 #domain H+-transporting ATP synthase alpha chain !8homology #label ATP SUMMARY #length 484 #molecular-weight 52213 #checksum 6452 SEQUENCE /// ENTRY PWYBB #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) beta chain - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES ATP synthase b chain ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 14-Dec-2001 ACCESSIONS S17753; S75526; S14858 REFERENCE S17745 !$#authors Lill, H.; Nelson, N. !$#journal Plant Mol. Biol. (1991) 17:641-652 !$#title The atp1 and atp2 operons of the cyanobacterium !1Synechocystis sp. PCC 6803. !$#cross-references MUID:92003679; PMID:1832989 !$#accession S17753 !'##molecule_type DNA !'##residues 1-483 ##label LIL !'##cross-references EMBL:X58129; NID:g47515; PIDN:CAA41137.1; !1PID:g47516 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75526 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-483 ##label KAN !'##cross-references EMBL:D90911; GB:AB001339; NID:g1653083; !1PIDN:BAA18087.1; PID:g1653171 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene atpB CLASSIFICATION #superfamily H+-transporting ATP synthase alpha chain; !1H+-transporting ATP synthase alpha chain homology KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1nucleotide binding; P-loop FEATURE !$162-169 #region nucleotide-binding motif A (P-loop)\ !$188-364 #domain H+-transporting ATP synthase alpha chain !8homology #label ATP SUMMARY #length 483 #molecular-weight 51733 #checksum 4430 SEQUENCE /// ENTRY PWBOB #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) beta chain precursor, mitochondrial [validated] - bovine ALTERNATE_NAMES F1-ATPase; hydrogen ion-transporting ATPase beta chain; mitochondrial ATPase beta chain ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 18-Apr-1984 #sequence_revision 07-Oct-1994 #text_change 14-Dec-2001 ACCESSIONS A28717; S06282; A40052; B60809; A01029; A33368; A33843; !1S17831; S10043 REFERENCE A28717 !$#authors Breen, G.A.M.; Holmans, P.L.; Garnett, K.E. !$#journal Biochemistry (1988) 27:3955-3961 !$#title Isolation and characterization of a complementary DNA for !1the nuclear-coded precursor of the beta-subunit of bovine !1mitochondrial F1-ATPase. !$#cross-references MUID:88326906; PMID:2458129 !$#accession A28717 !'##molecule_type mRNA !'##residues 1-528 ##label BRE !'##cross-references GB:M20929; NID:g162710; PIDN:AAA30395.1; !1PID:g162711 REFERENCE S06282 !$#authors Wallace, D.C.; Ye, J.; Neckelmann, S.N.; Singh, G.; Webster, !1K.A.; Greenberg, B.D. !$#journal Curr. Genet. (1987) 12:81-90 !$#title Sequence analysis of cDNAs for the human and bovine ATP !1synthase beta subunit: mitochondrial DNA genes sustain !1seventeen times more mutations. !$#cross-references MUID:88210529; PMID:2896550 !$#accession S06282 !'##molecule_type mRNA !'##residues 172-195,'I',197-528 ##label WAL1 !'##cross-references EMBL:X05605; NID:g103; PIDN:CAA29094.1; PID:g104 REFERENCE A39566 !$#authors Walker, J.E.; Lutter, R.; Dupuis, A.; Runswick, M.J. !$#journal Biochemistry (1991) 30:5369-5378 !$#title Identification of the subunits of F-1F-0-ATPase from bovine !1heart mitochondria. !$#cross-references MUID:91242449; PMID:1827992 !$#accession A40052 !'##molecule_type protein !'##residues 47-55 ##label WAL2 REFERENCE A60809 !$#authors Gibson, B.W.; Daley, D.J.; Williams, D.H. !$#journal Anal. Biochem. (1988) 169:217-226 !$#title Structural elucidation of N-terminal post-translational !1modifications by mass spectrometry: application to chicken !1enolase and the alpha- and beta-subunits of bovine !1mitochondrial F-1-ATPase. !$#cross-references MUID:88250539; PMID:2898218 !$#accession B60809 !'##molecule_type protein !'##residues 49-55 ##label GIB !'##note amino-terminal sequences beginning at 51-Ser were also found REFERENCE A92415 !$#authors Runswick, M.J.; Walker, J.E. !$#journal J. Biol. Chem. (1983) 258:3081-3089 !$#title The amino acid sequence of the beta-subunit of ATP synthase !1from bovine heart mitochondria. !$#cross-references MUID:83135760; PMID:6298222 !$#accession A01029 !'##molecule_type protein !'##residues 51-181,'L',183-186,'D',188-214,'F',216-273,'Q',275-337,'N', !1339-373,'V',375-408,'N',410-528 ##label RUN REFERENCE A33368 !$#authors Wu, J.C.; Lin, J.; Chuan, H.; Wang, J.H. !$#journal Biochemistry (1989) 28:8905-8911 !$#title Determination of the roles of active sites in F-1-ATPase by !1controlled affinity labeling. !$#cross-references MUID:90105427; PMID:2532546 !$#accession A33368 !'##molecule_type protein !'##residues 347-352 ##label WUJ REFERENCE A33843 !$#authors Bullough, D.A.; Ceccarelli, E.A.; Verburg, J.G.; Allison, !1W.S. !$#journal J. Biol. Chem. (1989) 264:9155-9163 !$#title Localization of sites modified during inactivation of the !1bovine heart mitochondrial F-1-ATPase by quinacrine mustard !1using [(3)H]aniline as a probe. !$#cross-references MUID:89255403; PMID:2524484 !$#accession A33843 !'##molecule_type protein !'##residues 351-355;388-397;444-458 ##label BUL REFERENCE S17831 !$#authors Milgrom, Y.M. !$#journal Eur. J. Biochem. (1991) 200:789-795 !$#title When beef-heart mitochondrial F(1)-ATPase is inhibited by !1inhibitor protein a nucleotide is trapped in one of the !1catalytic sites. !$#cross-references MUID:92007858; PMID:1833193 !$#accession S17831 !'##molecule_type protein !'##residues 388-394,'X',396-417,'X',419-422 ##label MIL REFERENCE A92436 !$#authors Hollemans, M.; Runswick, M.J.; Fearnley, I.M.; Walker, J.E. !$#journal J. Biol. Chem. (1983) 258:9307-9313 !$#title The sites of labeling of the beta-subunit of bovine !1mitochondrial F-1-ATPase with 8-azido-ATP. !$#cross-references MUID:83265727; PMID:6223927 !$#contents annotation; ATP binding site !$#note Lys-351, Ile-354, and Tyr-361 may be in the ATP binding site REFERENCE A65186 !$#authors Abrahams, J.P.; Leslie, A.G.W.; Lutter, R.; Walker, J.E. !$#submission submitted to the Brookhaven Protein Data Bank, March 1996 !$#cross-references PDB:1BMF !$#contents annotation; X-ray crystallography, 2.85 angstroms, residues !159-525 REFERENCE A65313 !$#authors Van Raaij, M.; Abrahams, J.P.; Leslie, A.G.W.; Walker, J.E. !$#submission submitted to the Brookhaven Protein Data Bank, May 1996 !$#cross-references PDB:1COW !$#contents annotation; X-ray crystallography, 3.1 angstroms, with !1aurovertin B, residues 59-525 REFERENCE A65505 !$#authors Abrahams, J.P.; Buchanan, S.K.; Van Raaij, M.J.; Fearnley, !1I.M.; Leslie, A.G.W.; Walker, J.E. !$#submission submitted to the Brookhaven Protein Data Bank, May 1996 !$#cross-references PDB:1EFR !$#contents annotation; X-ray crystallography, 3.1 angstroms, with !1efrapeptin, residues 59-525 REFERENCE A44750 !$#authors Abrahams, J.P.; Leslie, A.G.W.; Lutter, R.; Walker, J.E. !$#journal Nature (1994) 370:621-628 !$#title Structure at 2.8 angstroms resolution of F1-ATPase from !1bovine heart mitochondria. !$#cross-references MUID:94344236; PMID:8065448 !$#contents annotation; X-ray crystallography, 2.8 angstroms COMPLEX the ATP synthase F1 complex consists of three alpha chains !1(see PIR:PWBOA), three beta chains, one gamma chain (see !1PIR:PWBOG), one delta chain (see PIR:PWBOD), and one epsilon !1chain (see PIR:PWBOE); the F1 complex binds to the intrinsic !1membrane F0 complex FUNCTION !$#description catalyzes the formation of ATP from ADP and phosphate using !1the free energy derived from proton transport down the !1gradient maintained by cytochrome-c oxidase across the !1mitochondrial inner-membrane !$#pathway oxidative phosphorylation CLASSIFICATION #superfamily H+-transporting ATP synthase alpha chain; !1H+-transporting ATP synthase alpha chain homology KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; nucleotide binding; oxidative !1phosphorylation; P-loop; pyroglutamic acid FEATURE !$1-46 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$49-528 #product H+-transporting ATP synthase beta chain, !8mitochondrial #status experimental #label MAT\ !$206-213 #region nucleotide-binding motif A (P-loop)\ !$232-407 #domain H+-transporting ATP synthase alpha chain !8homology #label ATP\ !$49 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) (partial) #status experimental\ !$212 #binding_site ATP (Lys) #status experimental\ !$238 #active_site Glu #status predicted SUMMARY #length 528 #molecular-weight 56283 #checksum 2437 SEQUENCE /// ENTRY PWQFB #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) beta chain - Rhodospirillum rubrum ORGANISM #formal_name Rhodospirillum rubrum DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 14-Dec-2001 ACCESSIONS S08583; S29221 REFERENCE S07132 !$#authors Falk, G.; Hampe, A.; Walker, J.E. !$#journal Biochem. J. (1985) 228:391-407 !$#title Nucleotide sequence of the Rhodospirillum rubrum atp operon. !$#cross-references MUID:85251588; PMID:2861810 !$#accession S08583 !'##molecule_type DNA !'##residues 1-474 ##label FAL !'##cross-references EMBL:X02499; NID:g46360; PIDN:CAA26340.1; !1PID:g46368 REFERENCE S29220 !$#authors Andralojc, P.J.; Harris, D.A. !$#journal FEBS Lett. (1992) 310:187-192 !$#title Isolation and characterisation of a functional alphabeta !1heterodimer from the ATP synthase of Rhodospirillum rubrum. !$#cross-references MUID:93011913; PMID:1327870 !$#accession S29221 !'##status preliminary !'##molecule_type protein !'##residues 2-20 ##label AND GENETICS !$#gene atpD CLASSIFICATION #superfamily H+-transporting ATP synthase alpha chain; !1H+-transporting ATP synthase alpha chain homology KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1nucleotide binding; P-loop FEATURE !$152-159 #region nucleotide-binding motif A (P-loop)\ !$178-353 #domain H+-transporting ATP synthase alpha chain !8homology #label ATP SUMMARY #length 474 #molecular-weight 50852 #checksum 582 SEQUENCE /// ENTRY PWBYB #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) beta chain precursor - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES ATPase beta chain; F1-ATPase beta chain; protein J2041; protein YJR121w ORGANISM #formal_name Saccharomyces cerevisiae DATE 03-Aug-1984 #sequence_revision 19-Oct-1995 #text_change 14-Dec-2001 ACCESSIONS S57144; S27278; S27276; A24260; A01030; A60715 REFERENCE S56848 !$#authors Rose, M.; Koetter, P.; Entian, K.D. !$#submission submitted to the Protein Sequence Database, September 1995 !$#accession S57144 !'##molecule_type DNA !'##residues 1-511 ##label ROS !'##cross-references EMBL:Z49621; NID:g1015844; PIDN:CAA89652.1; !1PID:g1015845; GSPDB:GN00010; MIPS:YJR121w REFERENCE S27278 !$#authors Takeda, M. !$#submission submitted to the EMBL Data Library, July 1986 !$#accession S27278 !'##molecule_type DNA !'##residues 1-217,'A',219-353,'S',355,'S',357,'S',359-364,'SS',367-500, !1'R',502-507,'R',509-511 ##label TAK !'##cross-references EMBL:M12082; NID:g171109; PIDN:AAA34444.1; !1PID:g171110 !'##note this is a revision to the sequence from reference A24260 REFERENCE S27276 !$#authors Takeda, M.; Vassarotti, A.; Douglas, M.G. !$#journal J. Biol. Chem. (1986) 261:10466 !$#contents erratum !$#accession S27276 !'##molecule_type DNA !'##residues 1-36 ##label TA3 !'##cross-references EMBL:M12082 !'##note this is a revision to the sequence from reference A24260 REFERENCE A24260 !$#authors Takeda, M.; Vassarotti, A.; Douglas, M.G. !$#journal J. Biol. Chem. (1985) 260:15458-15465 !$#title Nuclear genes coding the yeast mitochondrial adenosine !1triphosphatase complex. Primary sequence analysis of ATP2 !1encoding the F-1-ATPase beta-subunit precursor. !$#cross-references MUID:86059413; PMID:2866186 !$#accession A24260 !'##molecule_type DNA !'##residues 1-12,'LLLQPNIS',23-157,'R',159-217,'A',219-231,'H',233-234, !1'EDS',238-251,'Y',253-353,'S',355,'S',357,'S',359-364,'SS', !1367-403,'R',405-500,'R',502-503,'Q',505-507,'R',509,'P',511 !1##label TA2 !'##cross-references EMBL:M12082 !'##note the authors translated the codon CGA for residue 158 as Ala, !1CGG for residue 404 as Ala, CAA for residue 504 as Glu, and !1CCC for residue 510 as Ala !'##note this sequence has been revised in references S27276 and S27278 REFERENCE A01030 !$#authors Saltzgaber-Muller, J.; Kunapuli, S.P.; Douglas, M.G. !$#journal J. Biol. Chem. (1983) 258:11465-11470 !$#title Nuclear genes coding the yeast mitochondrial adenosine !1triphosphate complex. Isolation of ATP2 coding the F !1(1)-ATPase beta subunit. !$#cross-references MUID:84008136; PMID:6225776 !$#accession A01030 !'##molecule_type DNA !'##residues 195-200,'M',202-217,'A',219-231,'H',233-234,'EDS',238-259, !1'E',261-286,'Y',289-353,'S',355,'S',357,'S',359-364,'SS', !1367-468,'R',470,'RCL',474-488,'R',490-507 ##label SAL !'##cross-references EMBL:K00560; NID:g171107; PIDN:AAA34443.1; !1PID:g171108 !'##note the authors translated the codon TTC for residue 252 as Tyr and !1GAA for residue 260 as Gly REFERENCE A60715 !$#authors Jenkins, J.R.; Pocklington, M.J.; Orr, E. !$#journal J. Cell Sci. (1990) 96:675-682 !$#title The F-1 ATP synthetase beta-subunit: a major yeast !1novobiocin binding protein. !$#cross-references MUID:91131709; PMID:2178164 !$#accession A60715 !'##molecule_type protein !'##residues 34-37,'N',39-52 ##label JEN GENETICS !$#gene SGD:ATP2; MIPS:YJR121w !'##cross-references SGD:S0003882; MIPS:YJR121w !$#map_position 10R !$#genome nuclear CLASSIFICATION #superfamily H+-transporting ATP synthase alpha chain; !1H+-transporting ATP synthase alpha chain homology KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; nucleotide binding; P-loop; peripheral !1membrane protein FEATURE !$1-33 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$34-511 #product H+-transporting ATP synthase beta chain !8#status experimental #label MAT\ !$190-197 #region nucleotide-binding motif A (P-loop)\ !$216-390 #domain H+-transporting ATP synthase alpha chain !8homology #label ATP SUMMARY #length 511 #molecular-weight 54793 #checksum 6918 SEQUENCE /// ENTRY PWBSBM #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) beta chain - Bacillus megaterium ALTERNATE_NAMES hydrogen ion-transporting ATPase epsilon chain ORGANISM #formal_name Bacillus megaterium DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 14-Dec-2001 ACCESSIONS A28599 REFERENCE A90141 !$#authors Hawthorne, C.A.; Brusilow, W.S.A. !$#journal Biochem. Biophys. Res. Commun. (1988) 151:926-931 !$#title Sequence of the genes for the beta and epsilon subunits of !1the ATP synthase of Bacillus megaterium QM B1551. !$#cross-references MUID:88162920; PMID:2894831 !$#accession A28599 !'##molecule_type DNA !'##residues 1-472 ##label HAW !'##cross-references GB:M20255; GB:J04455; GB:M18352; GB:M23924; !1NID:g142553; PIDN:AAA82526.1; PID:g142561 !'##experimental_source strain QM B1551 COMMENT This is one of five chains of the enzymatic component (F1) !1of the ATPase complex. CLASSIFICATION #superfamily H+-transporting ATP synthase alpha chain; !1H+-transporting ATP synthase alpha chain homology KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1nucleotide binding; P-loop FEATURE !$158-165 #region nucleotide-binding motif A (P-loop)\ !$184-353 #domain H+-transporting ATP synthase alpha chain !8homology #label ATP SUMMARY #length 472 #molecular-weight 51299 #checksum 814 SEQUENCE /// ENTRY PWBSBF #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) beta chain - Bacillus firmus (strain RAB) ORGANISM #formal_name Bacillus firmus DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 14-Dec-2001 ACCESSIONS S12743; S15060 REFERENCE S12743 !$#authors Ivey, D.M.; Krulwich, T.A. !$#journal Nucleic Acids Res. (1990) 18:1296 !$#title Sequence of the gene encoding the ATP synthase beta subunit !1from alkaliphilic Bacillus firmus RAB. !$#cross-references MUID:90206802; PMID:2181405 !$#accession S12743 !'##molecule_type DNA !'##residues 1-467 ##label IVE1 !'##cross-references EMBL:M31107 REFERENCE S15060 !$#authors Ivey, D.M.; Krulwich, T.A. !$#submission submitted to the EMBL Data Library, January 1990 !$#accession S15060 !'##molecule_type DNA !'##residues 1-249,'V',251-467 ##label IVE2 !'##cross-references EMBL:M31107; NID:g142563; PIDN:AAA22253.1; !1PID:g142564 CLASSIFICATION #superfamily H+-transporting ATP synthase alpha chain; !1H+-transporting ATP synthase alpha chain homology KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1nucleotide binding; P-loop FEATURE !$156-163 #region nucleotide-binding motif A (P-loop)\ !$182-350 #domain H+-transporting ATP synthase alpha chain !8homology #label ATP SUMMARY #length 467 #molecular-weight 50712 #checksum 7482 SEQUENCE /// ENTRY PWBSAS #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) alpha chain fliI, flagellar-specific, - Bacillus subtilis ALTERNATE_NAMES FliI protein homolog ORGANISM #formal_name Bacillus subtilis DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 14-Dec-2001 ACCESSIONS D42365; E69624; S14497 REFERENCE A42365 !$#authors Albertini, A.M.; Caramori, T.; Crabb, W.D.; Scoffone, F.; !1Galizzi, A. !$#journal J. Bacteriol. (1991) 173:3573-3579 !$#title The flaA locus of Bacillus subtilis is part of a large !1operon coding for flagellar structures, motility functions, !1and an ATPase-like polypeptide. !$#cross-references MUID:91258343; PMID:1828465 !$#accession D42365 !'##molecule_type DNA !'##residues 1-440 ##label AL2 !'##cross-references EMBL:X56049; NID:g39904; PIDN:CAA39523.1; !1PID:g580859 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69624 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-440 ##label KUN !'##cross-references GB:Z99112; GB:AL009126; NID:g2633902; !1PIDN:CAB13497.1; PID:g2633996 !'##experimental_source strain 168 GENETICS !$#gene fliI !$#start_codon GTG CLASSIFICATION #superfamily H+-transporting ATP synthase alpha chain; !1H+-transporting ATP synthase alpha chain homology KEYWORDS ATP biosynthesis; hydrolase; nucleotide binding; P-loop FEATURE !$167-174 #region nucleotide-binding motif A (P-loop)\ !$190-358 #domain H+-transporting ATP synthase alpha chain !8homology #label ATP\ !$253-258 #region nucleotide-binding motif B\ !$173 #binding_site ATP (Lys) #status predicted\ !$357 #active_site Arg #status predicted SUMMARY #length 440 #molecular-weight 47870 #checksum 4768 SEQUENCE /// ENTRY S14733 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) beta chain [validated] - Halobacterium salinarum ORGANISM #formal_name Halobacterium salinarum DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 03-Jun-2002 ACCESSIONS S14733; S18499 REFERENCE S14732 !$#authors Ihara, K.; Mukohata, Y. !$#journal Arch. Biochem. Biophys. (1991) 286:111-116 !$#title The ATP synthase of Halobacterium salinarium (halobium) is !1an archaebacterial type as revealed from the amino acid !1sequences of its two major subunits. !$#cross-references MUID:91378275; PMID:1832829 !$#accession S14733 !'##molecule_type DNA !'##residues 1-471 ##label IHA !'##cross-references GB:X70294; GB:S56356; NID:g43639; PIDN:CAA49776.1; !1PID:g43641 !'##note the source is given as Halobacterium salinarium !$#accession S18499 !'##molecule_type protein !'##residues 1-8;272-344;425-444;446-469 ##label IHA2 GENETICS !$#gene atpB COMPLEX atpA (PIR:S14732) and atpB (PIR:S14733) are the head piece !1of the ATP synthase in Halobacterium FUNCTION !$#description EC 3.6.3.14 [validated, PMID:9137827] !$#note the alpha chain is considered to be catalytic CLASSIFICATION #superfamily H+-transporting ATP synthase alpha chain; !1H+-transporting ATP synthase alpha chain homology KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1nucleotide binding; P-loop FEATURE !$1-471 #product H+-transporting ATP synthase beta chain !8#status experimental #label MAT\ !$58-65 #region nucleotide-binding motif A (P-loop)\ !$186-357 #domain H+-transporting ATP synthase alpha chain !8homology #label ATP SUMMARY #length 471 #molecular-weight 51956 #checksum 8906 SEQUENCE /// ENTRY I40360 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) chain i (atpI) - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 14-Dec-2001 ACCESSIONS I40360; E69592; S39249 REFERENCE I40360 !$#authors Santana, M.; Ionescu, M.S.; Vertes, A.; Longin, R.; Kunst, !1F.; Danchin, A.; Glaser, P. !$#journal J. Bacteriol. (1994) 176:6802-6811 !$#title Bacillus subtilis F0F1 ATPase: DNA sequence of the atp !1operon and characterization of atp mutants. !$#cross-references MUID:95050246; PMID:7961438 !$#accession I40360 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-127 ##label RES !'##cross-references EMBL:Z28592; NID:g433983; PIDN:CAA82253.1; !1PID:g433984 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69592 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-127 ##label KUN !'##cross-references GB:Z99122; GB:AL009126; NID:g2636029; !1PIDN:CAB15705.1; PID:g2636213 !'##experimental_source strain 168 GENETICS !$#gene atpI CLASSIFICATION #superfamily Bacillus H+-transporting ATP synthase chain I KEYWORDS hydrolase SUMMARY #length 127 #molecular-weight 14487 #checksum 1838 SEQUENCE /// ENTRY PWBYD #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) delta chain precursor - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES H+-transporting ATP synthase chain 5; oligomycin sensitivity-conferring protein; protein D9740.11; protein YDR198c ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 19-Apr-2002 ACCESSIONS S05726; A36594; S61184; S13350 REFERENCE S05726 !$#authors Lee, M.; Jones, D.; Mueller, D.M. !$#journal Nucleic Acids Res. (1988) 16:8181 !$#title Sequence of the yeast ATP5 gene. !$#cross-references MUID:88335563; PMID:2971156 !$#accession S05726 !'##molecule_type DNA !'##residues 1-212 ##label LEE !'##cross-references EMBL:X12356; NID:g3403; PIDN:CAA30917.1; PID:g3404 REFERENCE A36594 !$#authors Uh, M.; Jones, D.; Mueller, D.M. !$#journal J. Biol. Chem. (1990) 265:19047-19052 !$#title The gene coding for the yeast oligomycin !1sensitivity-conferring protein. !$#cross-references MUID:91035431; PMID:2146269 !$#accession A36594 !'##molecule_type DNA !'##residues 1-212 ##label UHM !'##cross-references GB:M32487; NID:g172086; PIDN:AAA34836.1; !1PID:g172087 REFERENCE S61160 !$#authors Ding, H. !$#submission submitted to the EMBL Data Library, June 1995 !$#description The sequence of S. cerevisiae cosmid 9740. !$#accession S61184 !'##molecule_type DNA !'##residues 1-212 ##label DIN !'##cross-references EMBL:U28374; NID:g849207; PIDN:AAB64734.1; !1PID:g849218; GSPDB:GN00004; MIPS:YDR198c GENETICS !$#gene SGD:ATP5; ATP5; OSCP; MIPS:YDR198c !'##cross-references SGD:S0002706 !$#map_position 4R !$#genome nuclear CLASSIFICATION #superfamily H+-transporting ATP synthase delta chain KEYWORDS ATP biosynthesis; hydrolase; mitochondrial inner membrane; !1mitochondrion; oxidative phosphorylation SUMMARY #length 212 #molecular-weight 22814 #checksum 2472 SEQUENCE /// ENTRY PWECD #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) delta chain - Escherichia coli (strain K-12) ALTERNATE_NAMES hydrogen ion-transporting ATPase delta chain ORGANISM #formal_name Escherichia coli DATE 18-Dec-1981 #sequence_revision 02-Apr-1982 #text_change 01-Mar-2002 ACCESSIONS A93732; A90101; I41274; H65176; T45005; A01031 REFERENCE A93732 !$#authors Gay, N.J.; Walker, J.E. !$#journal Nucleic Acids Res. (1981) 9:3919-3926 !$#title The atp operon: nucleotide sequence of the promoter and the !1genes for the membrane proteins, and the delta subunit of !1Escherichia coli ATP-synthase. !$#cross-references MUID:82059437; PMID:6272190 !$#accession A93732 !'##molecule_type DNA !'##residues 1-177 ##label GAY !'##cross-references GB:V00264; GB:X00771; NID:g41023; PIDN:CAA23517.1; !1PID:g41028 REFERENCE A90101 !$#authors Mabuchi, K.; Kanazawa, H.; Kayano, T.; Futai, M. !$#journal Biochem. Biophys. Res. Commun. (1981) 102:172-179 !$#title Nucleotide sequence of the gene coding for the delta subunit !1of proton-translocating ATPase of Escherichia coli. !$#cross-references MUID:82068433; PMID:6458296 !$#accession A90101 !'##molecule_type DNA !'##residues 1-81,'D',83-177 ##label MAB !'##cross-references GB:M12212; GB:M12213; NID:g145396; PIDN:AAA20044.1; !1PID:g145398 REFERENCE I41271 !$#authors Kanazawa, H.; Futai, M. !$#journal Ann. N. Y. Acad. Sci. (1982) 402:45-64 !$#title Structure and function of H+-ATPase: What we have learned !1from Escherichia coli H+-ATPase. !$#cross-references MUID:83176724; PMID:6301339 !$#accession I41274 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-177 ##label RES !'##cross-references GB:M25464; NID:g146318; PIDN:AAA83872.1; !1PID:g146322 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65176 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-177 ##label BLAT !'##cross-references GB:AE000450; GB:U00096; NID:g1790166; !1PIDN:AAC76758.1; PID:g1790173; UWGP:b3735 !'##experimental_source strain K-12, substrain MG1655 REFERENCE Z22893 !$#authors Nielsen, J.; Hansen, F.G.; Hoppe, J.; Friedl, P.; Von !1Meyenburg, K. !$#journal Mol. Gen. Genet. (1981) 184:33-39 !$#title The nucleotide sequence of the atp genes coding for the F-0 !1subunits a, b, c and the F-1 subunit delta of the membrane !1bound ATP synthase of Escherichia coli. !$#cross-references MUID:82147764; PMID:6278247 !$#accession T45005 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-177 ##label NIE !'##cross-references EMBL:V00266; NID:g41031; PIDN:CAA23524.1; !1PID:g41034 GENETICS !$#gene atpH; uncH !$#map_position 84 min COMPLEX this is one of the five chains of the enzymatic component !1(F1) of the ATPase complex CLASSIFICATION #superfamily H+-transporting ATP synthase delta chain KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex SUMMARY #length 177 #molecular-weight 19332 #checksum 4221 SEQUENCE /// ENTRY PWQFD #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) delta chain - Rhodospirillum rubrum ORGANISM #formal_name Rhodospirillum rubrum DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 14-Dec-2001 ACCESSIONS S08580 REFERENCE S07132 !$#authors Falk, G.; Hampe, A.; Walker, J.E. !$#journal Biochem. J. (1985) 228:391-407 !$#title Nucleotide sequence of the Rhodospirillum rubrum atp operon. !$#cross-references MUID:85251588; PMID:2861810 !$#accession S08580 !'##molecule_type DNA !'##residues 1-186 ##label FAL !'##cross-references EMBL:X02499; NID:g46360; PIDN:CAA26337.1; !1PID:g581524 GENETICS !$#gene atpH !$#start_codon GTG CLASSIFICATION #superfamily H+-transporting ATP synthase delta chain KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex SUMMARY #length 186 #molecular-weight 19575 #checksum 5427 SEQUENCE /// ENTRY PWYCD #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) delta chain - Synechococcus sp. (strain PCC 6301) ORGANISM #formal_name Synechococcus sp. DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 14-Dec-2001 ACCESSIONS S10830 REFERENCE S07286 !$#authors Cozens, A.L.; Walker, J.E. !$#journal J. Mol. Biol. (1987) 194:359-383 !$#title The organization and sequence of the genes for ATP synthase !1subunits in the cyanobacterium Synechococcus 6301. Support !1for an endosymbiotic origin of chloroplasts. !$#cross-references MUID:87311713; PMID:3041005 !$#accession S10830 !'##molecule_type DNA !'##residues 1-180 ##label COZ !'##cross-references EMBL:X05302; NID:g48009; PIDN:CAA28927.1; !1PID:g48016 CLASSIFICATION #superfamily H+-transporting ATP synthase delta chain KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex SUMMARY #length 180 #molecular-weight 19500 #checksum 9443 SEQUENCE /// ENTRY PWYBD #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) delta chain - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES ATP synthase chain d ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 14-Dec-2001 ACCESSIONS S17750; S74584; S14865 REFERENCE S17745 !$#authors Lill, H.; Nelson, N. !$#journal Plant Mol. Biol. (1991) 17:641-652 !$#title The atp1 and atp2 operons of the cyanobacterium !1Synechocystis sp. PCC 6803. !$#cross-references MUID:92003679; PMID:1832989 !$#accession S17750 !'##molecule_type DNA !'##residues 1-185 ##label LIL !'##cross-references EMBL:X58128; NID:g47506; PIDN:CAA41134.1; !1PID:g47512 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74584 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-185 ##label KAN !'##cross-references EMBL:D90900; GB:AB001339; NID:g1651768; !1PIDN:BAA16736.1; PID:g1651809 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene atpD CLASSIFICATION #superfamily H+-transporting ATP synthase delta chain KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex SUMMARY #length 185 #molecular-weight 20093 #checksum 9106 SEQUENCE /// ENTRY PWSPD #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) delta chain precursor, chloroplast - spinach ORGANISM #formal_name Spinacia oleracea #common_name spinach DATE 31-Mar-1989 #sequence_revision 31-Mar-1992 #text_change 14-Dec-2001 ACCESSIONS S11424; JA0061; S06343 REFERENCE S11424 !$#authors Bichler, J.; Herrmann, R.G. !$#journal Eur. J. Biochem. (1990) 190:415-426 !$#title Analysis of the promotors of the single-copy genes for !1plastocyanin and subunit delta of the chloroplast ATP !1synthase from spinach. !$#cross-references MUID:90306042; PMID:2194803 !$#accession S11424 !'##molecule_type DNA !'##residues 1-257 ##label BIC !'##cross-references GB:X61362; EMBL:X52287; NID:g21239; !1PIDN:CAA43634.1; PID:g21240 !'##note the authors translated the codon ACT for residue 222 as Ile REFERENCE JA0061 !$#authors Hermans, J.; Rother, C.; Bichler, J.; Steppuhn, J.; !1Herrmann, R.G. !$#journal Plant Mol. Biol. (1988) 10:323-330 !$#title Nucleotide sequence of cDNA clones encoding the complete !1precursor for subunit delta of thylakoid-located ATP !1synthase from spinach. !$#accession JA0061 !'##molecule_type mRNA !'##residues 1-28,'P',30-257 ##label HER REFERENCE S06343 !$#authors Berzborn, R.J.; Finke, W.; Otto, J.; Meyer, H.E. !$#journal Z. Naturforsch. C Biosci. (1987) 42:1231-1238 !$#title Protein sequence and structure of N-terminal amino acids of !1subunit delta of spinach photosynthetic ATP-synthase CF1. !$#accession S06343 !'##molecule_type protein !'##residues 71-105 ##label BER GENETICS !$#gene atpD !$#introns 110/3 CLASSIFICATION #superfamily H+-transporting ATP synthase delta chain KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; thylakoid FEATURE !$1-70 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$71-257 #product H+-transporting ATP synthase delta chain !8#status experimental #label MAT SUMMARY #length 257 #molecular-weight 27680 #checksum 9168 SEQUENCE /// ENTRY PWBOE #type fragment TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) epsilon chain precursor - bovine (fragment) ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 14-Dec-2001 ACCESSIONS S08239; S10042; C39566 REFERENCE S08239 !$#authors Vinas, O.; Powell, S.J.; Runswick, M.J.; Iacobazzi, V.; !1Walker, J.E. !$#journal Biochem. J. (1990) 265:321-326 !$#title The epsilon-subunit of ATP synthase from bovine heart !1mitochondria. Complementary DNA sequence, expression in !1bovine tissues and evidence of homologous sequences in man !1and rat. !$#cross-references MUID:90147593; PMID:2137333 !$#accession S08239 !'##molecule_type mRNA !'##residues 1-60 ##label VIN !'##cross-references EMBL:X16978; NID:g105; PIDN:CAA34849.1; PID:g642167 !'##note the authors translated the codon ATC for residue 9 as Leu !'##note it is uncertain whether Met-10 is the initiator or whether !1translation is initiated 5' to the sequenced region REFERENCE S07275 !$#authors Walker, J.E.; Fearnley, I.M.; Gay, N.J.; Gibson, B.W.; !1Northrop, F.D.; Powell, S.J.; Runswick, M.J.; Saraste, M.; !1Tybulewicz, V.L.J. !$#journal J. Mol. Biol. (1985) 184:677-701 !$#title Primary structure and subunit stoichiometry of F(1)-ATPase !1from bovine mitochondria. !$#cross-references MUID:86011574; PMID:2864455 !$#accession S10042 !'##molecule_type protein !'##residues 11-60 ##label WAL REFERENCE A39566 !$#authors Walker, J.E.; Lutter, R.; Dupuis, A.; Runswick, M.J. !$#journal Biochemistry (1991) 30:5369-5378 !$#title Identification of the subunits of F-1F-0-ATPase from bovine !1heart mitochondria. !$#cross-references MUID:91242449; PMID:1827992 !$#accession C39566 !'##molecule_type protein !'##residues 11-16 ##label WA2 CLASSIFICATION #superfamily bovine H+-transporting ATP synthase epsilon !1chain KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; oxidative phosphorylation FEATURE !$1-10 #domain transit peptide (mitochondrion) (fragment) !8#status predicted #label TNP\ !$11-60 #product H+-transporting ATP synthase epsilon chain !8#status experimental #label MAT SUMMARY #length 60 #checksum 6962 SEQUENCE /// ENTRY B44300 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) epsilon chain - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1993 #sequence_revision 28-Oct-1994 #text_change 14-Dec-2001 ACCESSIONS B44300; C33160; JS0742 REFERENCE A44300 !$#authors Higuti, T.; Yoshihara, Y.; Kuroiwa, K.; Kawamura, Y.; Toda, !1H.; Sakiyama, F. !$#journal J. Biol. Chem. (1992) 267:22658-22661 !$#title A simple, rapid method for purification of epsilon-subunit, !1coupling factor 6, subunit d, and subunit e from rat liver H !1(+)-ATP synthase and determination of the complete amino !1acid sequence of epsilon-subunit. !$#cross-references MUID:93054567; PMID:1429613 !$#accession B44300 !'##molecule_type protein !'##residues 1-50 ##label HIG !'##experimental_source liver !'##note sequence extracted from NCBI backbone (NCBIP:117198) REFERENCE A33160 !$#authors Godinot, C. !$#submission submitted to the Protein Sequence Database, February 1991 !$#accession C33160 !'##molecule_type protein !'##residues 1-17,'X',19,'X',21,'XVR' ##label GOD CLASSIFICATION #superfamily bovine H+-transporting ATP synthase epsilon !1chain KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; oxidative phosphorylation FEATURE !$1-50 #product H+-transporting ATP synthase epsilon chain !8#status experimental #label MAT SUMMARY #length 50 #molecular-weight 5636 #checksum 6303 SEQUENCE /// ENTRY A45315 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) epsilon chain - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein P0345; protein YPL271w ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 14-Dec-2001 ACCESSIONS A45315; S13742; S65304; S65325; S20128 REFERENCE A45315 !$#authors Guelin, E.; Chevallier, J.; Rigoulet, M.; Guerin, B.; !1Velours, J. !$#journal J. Biol. Chem. (1993) 268:161-167 !$#title ATP synthase of yeast mitochondria. Isolation and disruption !1of the ATP epsilon gene. !$#cross-references MUID:93106994; PMID:8416924 !$#accession A45315 !'##molecule_type DNA !'##residues 1-62 ##label GUE !'##cross-references EMBL:X64767; NID:g3407; PIDN:CAA46014.1; PID:g3408 !'##note sequence extracted from NCBI backbone (NCBIP:121309) REFERENCE S13742 !$#authors Arselin, G.; Gandar, J.C.; Guerin, B.; Velours, J. !$#journal J. Biol. Chem. (1991) 266:723-727 !$#title Isolation and complete amino acid sequence of the !1mitochondrial ATP synthase epsilon-subunit of the yeast !1Saccharomyces cerevisiae. !$#cross-references MUID:91093263; PMID:1985960 !$#accession S13742 !'##molecule_type protein !'##residues 2-62 ##label ARS REFERENCE S65292 !$#authors Duesterhoeft, A.; Floeth, M.; Fritz, M.; Hilbert, H.; !1Moestl, D. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S65304 !'##molecule_type DNA !'##residues 1-62 ##label DUE !'##cross-references EMBL:Z73627; NID:g1370558; PIDN:CAA98007.1; !1PID:g1370559; GSPDB:GN00016; MIPS:YPL271w !'##experimental_source strain S288C (AB972) REFERENCE S64967 !$#authors Delius, H.; Hebling, U. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S65325 !'##molecule_type DNA !'##residues 1-62 ##label DEL !'##cross-references EMBL:Z73627; NID:g1370558; PIDN:CAA98007.1; !1PID:g1370559; GSPDB:GN00016; MIPS:YPL271w !'##experimental_source strain S288C (AB972) GENETICS !$#gene SGD:ATP15; MIPS:YPL271w !'##cross-references SGD:S0006192; MIPS:YPL271w !$#map_position 16L !$#genome nuclear CLASSIFICATION #superfamily bovine H+-transporting ATP synthase epsilon !1chain KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; oxidative phosphorylation; peripheral !1membrane protein FEATURE !$2-62 #product H+-transporting ATP synthase epsilon chain !8#status experimental #label MAT SUMMARY #length 62 #molecular-weight 6743 #checksum 8635 SEQUENCE /// ENTRY PWBOD #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) delta chain precursor - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 14-Dec-2001 ACCESSIONS S09202; S10041; A35473; F39566 REFERENCE S09202 !$#authors Runswick, M.J.; Medd, S.M.; Walker, J.E. !$#journal Biochem. J. (1990) 266:421-426 !$#title The delta-subunit of ATP synthase from bovine heart !1mitochondria: complementary DNA sequence of its import !1precursor cloned with the aid of the polymerase chain !1reaction. !$#cross-references MUID:90197618; PMID:2138455 !$#accession S09202 !'##molecule_type mRNA !'##residues 1-168 ##label RUN !'##cross-references EMBL:X17019; NID:g109; PIDN:CAA34885.1; PID:g110 REFERENCE S07275 !$#authors Walker, J.E.; Fearnley, I.M.; Gay, N.J.; Gibson, B.W.; !1Northrop, F.D.; Powell, S.J.; Runswick, M.J.; Saraste, M.; !1Tybulewicz, V.L.J. !$#journal J. Mol. Biol. (1985) 184:677-701 !$#title Primary structure and subunit stoichiometry of F(1)-ATPase !1from bovine mitochondria. !$#cross-references MUID:86011574; PMID:2864455 !$#accession S10041 !'##molecule_type protein !'##residues 23-168 ##label WAL REFERENCE A35473 !$#authors Woldegiorgis, G.; Contreras, L.; Shrago, E. !$#journal Biochem. Biophys. Res. Commun. (1990) 169:339-345 !$#title Characterization of a low molecular weight protein of the !1ATP synthetase complex from beef heart and rat liver !1mitochondria with a high affinity monoclonal antibody. !$#cross-references MUID:90290465; PMID:2141466 !$#accession A35473 !'##molecule_type protein !'##residues 23-28,'E',30-36,'E',38-42 ##label WOL REFERENCE A39566 !$#authors Walker, J.E.; Lutter, R.; Dupuis, A.; Runswick, M.J. !$#journal Biochemistry (1991) 30:5369-5378 !$#title Identification of the subunits of F-1F-0-ATPase from bovine !1heart mitochondria. !$#cross-references MUID:91242449; PMID:1827992 !$#accession F39566 !'##molecule_type protein !'##residues 23-31 ##label WA2 CLASSIFICATION #superfamily H+-transporting ATP synthase epsilon chain KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; oxidative phosphorylation FEATURE !$1-22 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$23-168 #product H+-transporting ATP synthase delta chain !8#status experimental #label MAT SUMMARY #length 168 #molecular-weight 17612 #checksum 3975 SEQUENCE /// ENTRY PWECE #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) epsilon chain - Escherichia coli (strain K-12) ALTERNATE_NAMES hydrogen ion-transporting ATPase epsilon chain ORGANISM #formal_name Escherichia coli DATE 06-Jul-1982 #sequence_revision 06-Jul-1982 #text_change 01-Mar-2002 ACCESSIONS B90106; B93742; I41278; D65176; A01032 REFERENCE A90106 !$#authors Kanazawa, H.; Kayano, T.; Kiyasu, T.; Futai, M. !$#journal Biochem. Biophys. Res. Commun. (1982) 105:1257-1264 !$#title Nucleotide sequence of the genes for beta and epsilon !1subunits of proton-translocating ATPase from Escherichia !1coli. !$#cross-references MUID:82256510; PMID:6285901 !$#accession B90106 !'##molecule_type DNA !'##residues 1-139 ##label KAN !'##cross-references GB:J01594; GB:J01595; GB:K02181; GB:M25634; !1GB:V00264; GB:V00313; GB:X00771; NID:g148131; !1PIDN:AAA24738.1; PID:g148140 REFERENCE A93742 !$#authors Saraste, M.; Gay, N.J.; Eberle, A.; Runswick, M.J.; Walker, !1J.E. !$#journal Nucleic Acids Res. (1981) 9:5287-5296 !$#title The atp operon: nucleotide sequence of the genes for the !1gamma,beta, and epsilon subunits of Escherichia coli ATP !1synthase. !$#cross-references MUID:82059507; PMID:6272217 !$#accession B93742 !'##molecule_type DNA !'##residues 1-130,'LSS' ##label SAR !'##cross-references GB:V00267; NID:g41036; PIDN:CAA23528.1; PID:g41039 !'##note the different carboxyl-terminal sequence is due to a difference !1in the nucleotide sequence that changes the reading frame REFERENCE I41271 !$#authors Kanazawa, H.; Futai, M. !$#journal Ann. N. Y. Acad. Sci. (1982) 402:45-64 !$#title Structure and function of H+-ATPase: What we have learned !1from Escherichia coli H+-ATPase. !$#cross-references MUID:83176724; PMID:6301339 !$#accession I41278 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-139 ##label RES !'##cross-references GB:M25464; NID:g146318; PIDN:AAA83876.1; !1PID:g146326 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65176 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-139 ##label BLAT !'##cross-references GB:AE000450; GB:U00096; NID:g1790166; !1PIDN:AAC76754.1; PID:g1790169; UWGP:b3731 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene atpC; uncC !$#map_position 84 min COMPLEX this is one of the five chains of the enzymatic component !1(F1) of the ATPase complex. CLASSIFICATION #superfamily H+-transporting ATP synthase epsilon chain KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex SUMMARY #length 139 #molecular-weight 15068 #checksum 2612 SEQUENCE /// ENTRY PWQFE #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) epsilon chain - Rhodospirillum rubrum ORGANISM #formal_name Rhodospirillum rubrum DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 14-Dec-2001 ACCESSIONS S08584 REFERENCE S07132 !$#authors Falk, G.; Hampe, A.; Walker, J.E. !$#journal Biochem. J. (1985) 228:391-407 !$#title Nucleotide sequence of the Rhodospirillum rubrum atp operon. !$#cross-references MUID:85251588; PMID:2861810 !$#accession S08584 !'##molecule_type DNA !'##residues 1-134 ##label FAL !'##cross-references EMBL:X02499 GENETICS !$#gene atpC CLASSIFICATION #superfamily H+-transporting ATP synthase epsilon chain KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex SUMMARY #length 134 #molecular-weight 14307 #checksum 4015 SEQUENCE /// ENTRY PWYCE #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) epsilon chain - Synechococcus sp. (strain PCC 6301) ORGANISM #formal_name Synechococcus sp. DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 14-Dec-2001 ACCESSIONS S10838 REFERENCE S07286 !$#authors Cozens, A.L.; Walker, J.E. !$#journal J. Mol. Biol. (1987) 194:359-383 !$#title The organization and sequence of the genes for ATP synthase !1subunits in the cyanobacterium Synechococcus 6301. Support !1for an endosymbiotic origin of chloroplasts. !$#cross-references MUID:87311713; PMID:3041005 !$#accession S10838 !'##molecule_type DNA !'##residues 1-137 ##label COZ !'##cross-references EMBL:X05925; NID:g48021; PIDN:CAA29363.1; !1PID:g48025 CLASSIFICATION #superfamily H+-transporting ATP synthase epsilon chain KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex SUMMARY #length 137 #molecular-weight 14745 #checksum 9246 SEQUENCE /// ENTRY B26926 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) epsilon chain - Anabaena sp. ALTERNATE_NAMES ATPase epsilon chain ORGANISM #formal_name Anabaena sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 14-Dec-2001 ACCESSIONS B26926 REFERENCE A91862 !$#authors Curtis, S.E. !$#journal J. Bacteriol. (1987) 169:80-86 !$#title Genes encoding the beta and epsilon subunits of the !1proton-translocating ATPase from Anabaena sp. strain PCC !17120. !$#cross-references MUID:87083415; PMID:2878921 !$#accession B26926 !'##molecule_type DNA !'##residues 1-137 ##label CUR !'##cross-references GB:M15336; NID:g142005; PIDN:AAA21994.1; !1PID:g142007 !'##experimental_source PCC 7120 GENETICS !$#gene atpE CLASSIFICATION #superfamily H+-transporting ATP synthase epsilon chain KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex SUMMARY #length 137 #molecular-weight 14688 #checksum 4780 SEQUENCE /// ENTRY B42697 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) epsilon chain - Prochloron didemni ORGANISM #formal_name Prochloron didemni DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 14-Dec-2001 ACCESSIONS B42697 REFERENCE A42697 !$#authors Lockhart, P.J.; Beanland, T.J.; Howe, C.J.; Larkum, A.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:2742-2746 !$#title Sequence of Prochloron didemni atpBE and the inference of !1chloroplast origins. !$#cross-references MUID:92212905; PMID:1532658 !$#accession B42697 !'##status preliminary !'##molecule_type DNA !'##residues 1-136 ##label LOC !'##cross-references GB:M86384; NID:g150557; PIDN:AAA25557.1; !1PID:g150559 !'##note sequence extracted from NCBI backbone (NCBIN:92188, !1NCBIP:92190) CLASSIFICATION #superfamily H+-transporting ATP synthase epsilon chain KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex SUMMARY #length 136 #molecular-weight 14781 #checksum 846 SEQUENCE /// ENTRY PWPFEL #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) epsilon chain - brown alga (Pylaiella littoralis) chloroplast ORGANISM #formal_name chloroplast Pylaiella littoralis DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 14-Dec-2001 ACCESSIONS S20849; S17103 REFERENCE S20848 !$#authors Jouannic, S.; Kerbourc'h, C.; Kloareg, B.; Loiseaux-de Goer, !1S. !$#journal Plant Mol. Biol. (1992) 18:819-822 !$#title Nucleotide sequences of the atpB and the atpE genes of the !1brown alga Pylaiella littoralis (L.) Kjellm. !$#cross-references MUID:92216062; PMID:1532750 !$#accession S20849 !'##molecule_type DNA !'##residues 1-132 ##label JOU !'##cross-references EMBL:X60329; NID:g14180; PIDN:CAA42900.1; !1PID:g14182 !'##note the authors translated the codon TTA for residue 77 as Ile, ATT !1for residue 78 as Ser, AGT for residue 79 as Gly, GGA for !1residue 80 as Val, and GTA for residue 81 as Glu GENETICS !$#gene atpE !$#genome chloroplast CLASSIFICATION #superfamily H+-transporting ATP synthase epsilon chain KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; thylakoid SUMMARY #length 132 #molecular-weight 14183 #checksum 2396 SEQUENCE /// ENTRY PWLVE #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) epsilon chain - liverwort (Marchantia polymorpha) chloroplast ALTERNATE_NAMES hydrogen ion-transporting ATPase epsilon chain ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 14-Dec-2001 ACCESSIONS A01033; S01598 REFERENCE A00150 !$#authors Ohyama, K. !$#submission submitted to the EMBL Data Library, October 1986 !$#accession A01033 !'##molecule_type DNA !'##residues 1-135 ##label OHY REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features REFERENCE S01567 !$#authors Umesono, K.; Inokuchi, H.; Shiki, Y.; Takeuchi, M.; Chang, !1Z.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Ohyama, K.; Ozeki, !1H. !$#journal J. Mol. Biol. (1988) 203:299-331 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. II. Gene organization of the large !1single copy region from rps'12 to atpB. !$#cross-references MUID:89068686; PMID:2974085 !$#accession S01598 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-135 ##label UME !'##cross-references GB:X04465; GB:Y00686; NID:g11640; PIDN:CAA28090.1; !1PID:g11678 COMMENT This is one of the five chains of the enzymatic component !1(coupling factor CF1) of the chloroplast ATPase complex, !1which is bound to the chloroplast thylakoid membrane. GENETICS !$#gene atpE !$#genome chloroplast CLASSIFICATION #superfamily H+-transporting ATP synthase epsilon chain KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; thylakoid SUMMARY #length 135 #molecular-weight 15054 #checksum 5688 SEQUENCE /// ENTRY PWSPE #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) epsilon chain - spinach chloroplast ALTERNATE_NAMES hydrogen ion-transporting ATPase epsilon chain ORGANISM #formal_name chloroplast Spinacia oleracea #common_name spinach DATE 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 14-Dec-2001 ACCESSIONS A01034 REFERENCE A93929 !$#authors Zurawski, G.; Bottomley, W.; Whitfeld, P.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:6260-6264 !$#title Structures of the genes for the beta and epsilon subunits of !1spinach chloroplast ATPase indicate a dicistronic mRNA and !1an overlapping translation stop/start signal. !$#accession A01034 !'##molecule_type DNA !'##residues 1-134 ##label ZUR !'##note this is one of the five chains of the enzymatic component (CF1) !1of the chloroplast ATPase complex; the sequence is 26% !1identical with its counterpart from E. coli GENETICS !$#genome chloroplast CLASSIFICATION #superfamily H+-transporting ATP synthase epsilon chain KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; thylakoid SUMMARY #length 134 #molecular-weight 14700 #checksum 5689 SEQUENCE /// ENTRY PWNTE #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) epsilon chain - common tobacco chloroplast ALTERNATE_NAMES hydrogen ion-transporting ATPase epsilon chain ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 14-Dec-2001 ACCESSIONS A01035 REFERENCE A91502 !$#authors Shinozaki, K.; Deno, H.; Kato, A.; Sugiura, M. !$#journal Gene (1983) 24:147-155 !$#title Overlap and cotranscription of the genes for the beta and !1epsilon subunits of tobacco chloroplast ATPase. !$#cross-references MUID:84059075; PMID:6227526 !$#accession A01035 !'##molecule_type DNA !'##residues 1-133 ##label SHI !'##cross-references GB:K00507; NID:g343480; PIDN:AAA84677.1; !1PID:g552955 GENETICS !$#genome chloroplast CLASSIFICATION #superfamily H+-transporting ATP synthase epsilon chain KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; thylakoid SUMMARY #length 133 #molecular-weight 14607 #checksum 3795 SEQUENCE /// ENTRY PWZME #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) epsilon chain - maize chloroplast ALTERNATE_NAMES hydrogen ion-transporting ATPase epsilon chain ORGANISM #formal_name chloroplast Zea mays #common_name maize DATE 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 14-Dec-2001 ACCESSIONS A01036; S58558 REFERENCE A93437 !$#authors Krebbers, E.T.; Larrinua, I.M.; McIntosh, L.; Bogorad, L. !$#journal Nucleic Acids Res. (1982) 10:4985-5002 !$#title The maize chloroplast genes for the beta and epsilon !1subunits of the photosynthetic coupling factor CF-1 are !1fused. !$#cross-references MUID:83038650; PMID:6290998 !$#accession A01036 !'##molecule_type DNA !'##residues 1-137 ##label KRE !'##cross-references GB:J01421; NID:g342576; PIDN:AAA85357.1; !1PID:g342578 !'##note this is one of the five chains of the enzymatic component !1(coupling factor CF1) of the chloroplast ATPase complex, !1which is bound to the chloroplast thylakoid membrane; the !1sequence is 23% identical with its counterpart from E. coli REFERENCE S58531 !$#authors Maier, R.M.; Neckermann, K.; Igloi, G.L.; Koessel, H. !$#journal J. Mol. Biol. (1995) 251:614-628 !$#title Complete sequence of the maize chloroplast genome: gene !1content, hotspots of divergence and fine tuning of genetic !1information by transcript editing. !$#cross-references MUID:95395841; PMID:7666415 !$#accession S58558 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-137 ##label MAI !'##cross-references EMBL:X86563; NID:g902200; PIDN:CAA60292.1; !1PID:g902228 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1995 GENETICS !$#gene atpE !$#genome chloroplast CLASSIFICATION #superfamily H+-transporting ATP synthase epsilon chain KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; peripheral membrane protein; !1thylakoid SUMMARY #length 137 #molecular-weight 15217 #checksum 9456 SEQUENCE /// ENTRY PWRZE #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) epsilon chain - rice chloroplast ALTERNATE_NAMES ATPase epsilon chain ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 14-Dec-2001 ACCESSIONS JQ0229; S05109; JQ0592 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0229 !'##molecule_type DNA !'##residues 1-137 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05109 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-137 ##label HIR !'##cross-references EMBL:X15901; NID:g11957; PIDN:CAA34002.1; !1PID:g11990 !'##experimental_source cv. Nihonbare REFERENCE JQ0591 !$#authors Nishizawa, Y.; Hirai, A. !$#journal Jpn. J. Genet. (1989) 64:223-229 !$#title The nucleotide sequences and expression of genes for the !1beta and epsilon subunits of ATP synthase from rice (Oryza !1sativa L.). !$#cross-references MUID:90212087; PMID:2534354 !$#accession JQ0592 !'##molecule_type DNA !'##residues 1-15,'A',17-137 ##label NIS !'##cross-references GB:D00432; NID:g344013; PIDN:BAA00335.1; !1PID:g344015 GENETICS !$#gene atpE !$#map_position CP51817-51404 !$#genome chloroplast CLASSIFICATION #superfamily H+-transporting ATP synthase epsilon chain KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; thylakoid SUMMARY #length 137 #molecular-weight 15217 #checksum 309 SEQUENCE /// ENTRY PWWTE #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) epsilon chain - wheat chloroplast ORGANISM #formal_name chloroplast Triticum aestivum #common_name common wheat DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 14-Dec-2001 ACCESSIONS S07938; A38805 REFERENCE S07399 !$#authors Howe, C.J.; Fearnley, I.M.; Walker, J.E.; Dyer, T.A.; Gray, !1J.C. !$#journal Plant Mol. Biol. (1985) 4:333-345 !$#title Nucleotide sequences of the genes for the alpha, beta and !1epsilon subunits of wheat chloroplast ATP synthase. !$#accession S07938 !'##molecule_type DNA !'##residues 1-137 ##label HOW !'##cross-references EMBL:M16843; NID:g343676; PIDN:AAA84727.1; !1PID:g343678 !$#accession A38805 !'##molecule_type protein !'##residues 'X',3-8,'X',10-12,'X',14,'X',16,'X',18,'XX',21 ##label HOW2 GENETICS !$#genome chloroplast CLASSIFICATION #superfamily H+-transporting ATP synthase epsilon chain KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; thylakoid FEATURE !$2-137 #product H+-transporting ATP synthase epsilon chain !8#status experimental #label MAT SUMMARY #length 137 #molecular-weight 15217 #checksum 9004 SEQUENCE /// ENTRY PWBHE #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) epsilon chain - barley chloroplast ALTERNATE_NAMES hydrogen ion-transporting ATPase epsilon chain ORGANISM #formal_name chloroplast Hordeum vulgare #common_name barley DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 14-Dec-2001 ACCESSIONS A01037 REFERENCE A93509 !$#authors Zurawski, G.; Clegg, M.T. !$#journal Nucleic Acids Res. (1984) 12:2549-2559 !$#title The barley chloroplast DNA atpBE, trnM2, and trnV1 loci. !$#cross-references MUID:84169555; PMID:6231529 !$#accession A01037 !'##molecule_type DNA !'##residues 1-137 ##label ZUR !'##experimental_source var. Clipper !'##note the authors translated the codon AGT for residue 112 as Asp COMMENT This is one of the five chains of the enzymatic component !1(coupling factor CF1) of the chloroplast ATPase complex, !1which is bound to the chloroplast thylakoid membrane. GENETICS !$#genome chloroplast CLASSIFICATION #superfamily H+-transporting ATP synthase epsilon chain KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; thylakoid SUMMARY #length 137 #molecular-weight 15189 #checksum 9829 SEQUENCE /// ENTRY PWKME #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) epsilon chain - Chlamydomonas reinhardtii chloroplast ALTERNATE_NAMES ATP synthase chain E ORGANISM #formal_name chloroplast Chlamydomonas reinhardtii DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 14-Dec-2001 ACCESSIONS S11898; S06249; S68395 REFERENCE S11897 !$#authors Robertson, D.; Boynton, J.E.; Gillham, N.W. !$#journal Mol. Gen. Genet. (1990) 221:155-163 !$#title Cotranscription of the wild-type chloroplast atpE gene !1encoding the CF(1)/CF(0) epsilon subunit with the 3' half of !1the rps7 gene in Chlamydomonas reinhardtii and !1characterization of frameshift mutations in atpE. !$#cross-references MUID:90318312; PMID:2196429 !$#accession S11898 !'##molecule_type DNA !'##residues 1-141 ##label ROB !'##cross-references EMBL:X53977; NID:g11429; PIDN:CAA37928.1; !1PID:g11431 !'##note the authors translated the codon CGT for residue 127 as Ala and !1GCT for residue 128 as Arg REFERENCE S06249 !$#authors Woessner, J.P.; Gillham, N.W.; Boynton, J.E. !$#journal Plant Mol. Biol. (1987) 8:151-158 !$#title Chloroplast genes encoding subunits of the H(+)-ATPase !1complex of Chlamydomonas reinhardtii are rearranged compared !1to higher plants: sequence of the atpE gene and location of !1the atpF and atpI genes. !$#accession S06249 !'##molecule_type DNA !'##residues 1-119,'V',121-141 ##label WOE !'##cross-references EMBL:M17168; NID:g336668; PIDN:AAA84147.1; !1PID:g336669 REFERENCE S68388 !$#authors Fiedler, H.R.; Schmid, R.; Leu, S.; Shavit, N.; Strotmann, !1H. !$#journal FEBS Lett. (1995) 377:163-166 !$#title Isolation of CF(0)CF(1) from Chlamydomonas reinhardtii cw15 !1and the N-terminal amino acid sequences of the CF(0)CF(1) !1subunits. !$#cross-references MUID:96128220; PMID:8543042 !$#accession S68395 !'##molecule_type protein !'##residues 2-26 ##label FIE !'##experimental_source strain CW15 GENETICS !$#gene atpE !$#genome chloroplast CLASSIFICATION #superfamily H+-transporting ATP synthase epsilon chain KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; peripheral membrane protein; !1thylakoid SUMMARY #length 141 #molecular-weight 15374 #checksum 4355 SEQUENCE /// ENTRY PWBSEM #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) epsilon chain - Bacillus megaterium ALTERNATE_NAMES hydrogen ion-transporting ATPase epsilon chain ORGANISM #formal_name Bacillus megaterium DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 14-Dec-2001 ACCESSIONS B28599 REFERENCE A90141 !$#authors Hawthorne, C.A.; Brusilow, W.S.A. !$#journal Biochem. Biophys. Res. Commun. (1988) 151:926-931 !$#title Sequence of the genes for the beta and epsilon subunits of !1the ATP synthase of Bacillus megaterium QM B1551. !$#cross-references MUID:88162920; PMID:2894831 !$#accession B28599 !'##molecule_type DNA !'##residues 1-134 ##label HAW !'##cross-references GB:M20255; GB:J04455; GB:M18352; GB:M23924; !1NID:g142553; PIDN:AAA82527.1; PID:g142562 !'##experimental_source strain QM B1551 COMMENT This is one of five chains of the enzymatic component (F1) !1of the ATPase complex. CLASSIFICATION #superfamily H+-transporting ATP synthase epsilon chain KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex SUMMARY #length 134 #molecular-weight 14645 #checksum 4952 SEQUENCE /// ENTRY S02256 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) epsilon chain - thermophilic bacterium PS-3 ALTERNATE_NAMES ATPase epsilon chain ORGANISM #formal_name thermophilic bacterium PS-3 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 14-Dec-2001 ACCESSIONS S02256; A24474 REFERENCE S01397 !$#authors Ohta, S.; Yohda, M.; Ishizuka, M.; Hirata, H.; Hamamoto, T.; !1Otawara-Hamamoto, Y.; Matsuda, K.; Kagawa, Y. !$#journal Biochim. Biophys. Acta (1988) 933:141-155 !$#title Sequence and over-expression of subunits of adenosine !1triphosphate synthase in thermophilic bacterium PS3. !$#cross-references MUID:88163679; PMID:2894854 !$#accession S02256 !'##molecule_type DNA !'##residues 1-132 ##label OHT !'##cross-references EMBL:X07804; NID:g45808; PIDN:CAA30656.1; !1PID:g45818 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE A24474 !$#authors Saishu, T.; Nojima, H.; Kagawa, Y. !$#journal Biochim. Biophys. Acta (1986) 867:97-106 !$#title Stability of structures of the epsilon subunit and !1terminator of thermophilic ATPase. !$#cross-references MUID:86243450; PMID:2872924 !$#accession A24474 !'##molecule_type DNA !'##residues 1-132 ##label SAI !'##cross-references GB:X03969; NID:g45805; PIDN:CAA27607.1; PID:g45807 CLASSIFICATION #superfamily H+-transporting ATP synthase epsilon chain KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex FEATURE !$1-132 #product H+-transporting ATP synthase epsilon chain !8#status experimental #label MAT SUMMARY #length 132 #molecular-weight 14333 #checksum 1589 SEQUENCE /// ENTRY I40369 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) epsilon chain (atpC) - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 14-Dec-2001 ACCESSIONS I40369; G69591; S39257 REFERENCE I40360 !$#authors Santana, M.; Ionescu, M.S.; Vertes, A.; Longin, R.; Kunst, !1F.; Danchin, A.; Glaser, P. !$#journal J. Bacteriol. (1994) 176:6802-6811 !$#title Bacillus subtilis F0F1 ATPase: DNA sequence of the atp !1operon and characterization of atp mutants. !$#cross-references MUID:95050246; PMID:7961438 !$#accession I40369 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-132 ##label RES !'##cross-references EMBL:Z28592; NID:g433983; PIDN:CAA82261.1; !1PID:g433992 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69591 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-132 ##label KUN !'##cross-references GB:Z99122; GB:AL009126; NID:g2636029; !1PIDN:CAB15697.1; PID:g2636205 !'##experimental_source strain 168 GENETICS !$#gene atpC CLASSIFICATION #superfamily H+-transporting ATP synthase epsilon chain KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex SUMMARY #length 132 #molecular-weight 14209 #checksum 1243 SEQUENCE /// ENTRY S17727 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) epsilon chain - Bacillus firmus ORGANISM #formal_name Bacillus firmus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 14-Dec-2001 ACCESSIONS S17727 REFERENCE S17719 !$#authors Ivey, D.M.; Krulwich, T.A. !$#journal Mol. Gen. Genet. (1991) 229:292-300 !$#title Organization and nucleotide sequence of the atp genes !1encoding the ATP synthase from alkaliphilic Bacillus firmus !1OF4. !$#cross-references MUID:92017665; PMID:1833620 !$#accession S17727 !'##molecule_type DNA !'##residues 1-133 ##label IVE !'##cross-references EMBL:M60117; NID:g2988387; PIDN:AAC08045.1; !1PID:g142552 GENETICS !$#gene atpC CLASSIFICATION #superfamily H+-transporting ATP synthase epsilon chain KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex SUMMARY #length 133 #molecular-weight 14448 #checksum 6240 SEQUENCE /// ENTRY A69228 #type complete TITLE ATP synthase, subunit C - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A69228 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession A69228 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-385 ##label MTH !'##cross-references GB:AE000869; GB:AE000666; NID:g2622042; !1PIDN:AAB85453.1; PID:g2622054 !'##experimental_source strain Delta H GENETICS !$#gene MTH957 CLASSIFICATION #superfamily H+ transporting ATP synthase C subunit SUMMARY #length 385 #molecular-weight 42440 #checksum 2794 SEQUENCE /// ENTRY D64327 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) subunit C - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 14-Dec-2001 ACCESSIONS D64327 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession D64327 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-399 ##label BUL !'##cross-references GB:U67477; GB:L77117; NID:g1590949; !1PIDN:AAB98202.1; PID:g1590956; TIGR:MJ0219 GENETICS !$#map_position REV210517-209318 CLASSIFICATION #superfamily H+ transporting ATP synthase C subunit KEYWORDS hydrolase SUMMARY #length 399 #molecular-weight 44828 #checksum 5582 SEQUENCE /// ENTRY C69395 #type complete TITLE H+-transporting ATP synthase, subunit C (atpC) homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C69395 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession C69395 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-342 ##label KLE !'##cross-references GB:AE001023; GB:AE000782; NID:g2689346; !1PIDN:AAB90075.1; PID:g2649417; TIGR:AF1164 CLASSIFICATION #superfamily H+ transporting ATP synthase C subunit SUMMARY #length 342 #molecular-weight 40098 #checksum 2376 SEQUENCE /// ENTRY E54392 #type complete TITLE ntpP protein - Enterococcus hirae ALTERNATE_NAMES ntpC protein ORGANISM #formal_name Enterococcus hirae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS E54392; D53610 REFERENCE A54392 !$#authors Solioz, M.; Davies, K. !$#journal J. Biol. Chem. (1994) 269:9453-9459 !$#title Operon of vacuolar-type Na(+)-ATPase of Enterococcus hirae. !$#cross-references MUID:94193617; PMID:8144530 !$#accession E54392 !'##status preliminary !'##molecule_type DNA !'##residues 1-328 ##label SOL !'##cross-references GB:X76913; NID:g472916; PIDN:CAA54239.1; !1PID:g472921 REFERENCE A53610 !$#authors Takase, K.; Kakinuma, S.; Yamato, I.; Konishi, K.; Igarashi, !1K.; Kakinuma, Y. !$#journal J. Biol. Chem. (1994) 269:11037-11044 !$#title Sequencing and characterization of the ntp gene cluster for !1vacuolar-type Na(+)-translocating ATPase of Enterococcus !1hirae. !$#cross-references MUID:94209269; PMID:8157629 !$#accession D53610 !'##status preliminary !'##molecule_type DNA !'##residues 1-328 ##label TAK !'##cross-references GB:D17462; NID:g487271; PIDN:BAA04273.1; !1PID:g487276 GENETICS !$#gene ntpP; ntpC CLASSIFICATION #superfamily H+ transporting ATP synthase C subunit SUMMARY #length 328 #molecular-weight 38163 #checksum 4689 SEQUENCE /// ENTRY PWBOG #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) gamma chain precursor [validated] - bovine ALTERNATE_NAMES F1-ATPase; hydrogen ion-transporting ATPase gamma chain; mitochondrial ATPase gamma chain CONTAINS H+-transporting two-sector ATPase (EC 3.6.3.14) gamma chain, splice form H; H+-transporting two-sector ATPase (EC 3.6.3.14) gamma chain, splice form L ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Sep-1991 #sequence_revision 23-Mar-1995 #text_change 14-Dec-2001 ACCESSIONS A32019; A34999; S10040; A35000; H39566; A38930; S33749; !1B38930; S33750; A30860 REFERENCE A32019 !$#authors Dyer, M.R.; Gay, N.J.; Powell, S.J.; Walker, J.E. !$#journal Biochemistry (1989) 28:3670-3680 !$#title ATP synthase from bovine mitochondria: complementary DNA !1sequence of the mitochondrial import precursor of the !1gamma-subunit and the genomic sequence of the mature !1protein. !$#cross-references MUID:89323066; PMID:2526651 !$#accession A32019 !'##molecule_type DNA !'##residues 1-297 ##label DYE1 !'##cross-references GB:M22463; GB:J02850; NID:g162716; PIDN:AAA30398.1; !1PID:g162717 !$#accession A34999 !'##molecule_type mRNA !'##residues 1-297 ##label DYE2 !'##cross-references GB:M22463; GB:J02850; GB:M22464; NID:g162716; !1PIDN:AAA30398.1; PID:g162717 REFERENCE S07275 !$#authors Walker, J.E.; Fearnley, I.M.; Gay, N.J.; Gibson, B.W.; !1Northrop, F.D.; Powell, S.J.; Runswick, M.J.; Saraste, M.; !1Tybulewicz, V.L.J. !$#journal J. Mol. Biol. (1985) 184:677-701 !$#title Primary structure and subunit stoichiometry of F(1)-ATPase !1from bovine mitochondria. !$#cross-references MUID:86011574; PMID:2864455 !$#accession S10040 !'##molecule_type protein !'##residues 26-189;192-297 ##label WAL1 !$#accession A35000 !'##molecule_type mRNA !'##residues 174-297 ##label WAL2 !'##cross-references GB:X55389; NID:g287733; PIDN:CAA39064.1; !1PID:g599905 REFERENCE A39566 !$#authors Walker, J.E.; Lutter, R.; Dupuis, A.; Runswick, M.J. !$#journal Biochemistry (1991) 30:5369-5378 !$#title Identification of the subunits of F-1F-0-ATPase from bovine !1heart mitochondria. !$#cross-references MUID:91242449; PMID:1827992 !$#accession H39566 !'##molecule_type protein !'##residues 26-30 ##label WAL3 REFERENCE S33749 !$#authors Matsuda, C.; Endo, H.; Hirata, H.; Morosawa, H.; Nakanishi, !1M.; Kagawa, Y. !$#journal FEBS Lett. (1993) 325:281-284 !$#title Tissue-specific isoforms of the bovine mitochondrial ATP !1synthase gamma-subunit. !$#cross-references MUID:93307511; PMID:8391483 !$#accession A38930 !'##molecule_type mRNA !'##residues 295-298 ##label MA1 !'##experimental_source liver !$#accession S33749 !'##molecule_type protein !'##residues 286-298 ##label MA2 !'##experimental_source liver !$#accession B38930 !'##molecule_type mRNA !'##residues 295-297 ##label MA3 !'##experimental_source heart !$#accession S33750 !'##molecule_type protein !'##residues 286-297 ##label MA4 !'##experimental_source heart REFERENCE A65186 !$#authors Abrahams, J.P.; Leslie, A.G.W.; Lutter, R.; Walker, J.E. !$#submission submitted to the Brookhaven Protein Data Bank, March 1996 !$#cross-references PDB:1BMF !$#contents annotation; X-ray crystallography, 2.85 angstroms, residues !126-69;102-115;234-297 REFERENCE A65313 !$#authors Van Raaij, M.; Abrahams, J.P.; Leslie, A.G.W.; Walker, J.E. !$#submission submitted to the Brookhaven Protein Data Bank, May 1996 !$#cross-references PDB:1COW !$#contents annotation; X-ray crystallography, 3.1 angstroms, with !1aurovertin B, residues 26-69;102-115;234-297 REFERENCE A65505 !$#authors Abrahams, J.P.; Buchanan, S.K.; Van Raaij, M.J.; Fearnley, !1I.M.; Leslie, A.G.W.; Walker, J.E. !$#submission submitted to the Brookhaven Protein Data Bank, May 1996 !$#cross-references PDB:1EFR !$#contents annotation; X-ray crystallography, 3.1 angstroms, with !1efrapeptin, residues 26-69;102-115;234-297 REFERENCE A44750 !$#authors Abrahams, J.P.; Leslie, A.G.W.; Lutter, R.; Walker, J.E. !$#journal Nature (1994) 370:621-628 !$#title Structure at 2.8 angstroms resolution of F1-ATPase from !1bovine heart mitochondria. !$#cross-references MUID:94344236; PMID:8065448 !$#contents annotation; X-ray crystallography, 2.8 angstroms; structure !1of complex with alpha, beta and gamma chains COMPLEX the ATP synthase F1 complex consists of three alpha chains !1(see PIR:PWBOA), three beta chains (see PIR:PWBOB), one !1gamma chain, one delta chain (see PIR:PWBOD), and one !1epsilon chain (see PIR:PWBOE); the F1 complex binds to the !1intrinsic membrane F0 complex FUNCTION !$#description catalyzes the formation of ATP from ADP and phosphate using !1the free energy derived from proton transport down the !1gradient maintained by cytochrome-c oxidase across the !1mitochondrial inner-membrane !$#pathway oxidative phosphorylation CLASSIFICATION #superfamily H+-transporting ATP synthase gamma chain KEYWORDS alternative splicing; ATP biosynthesis; hydrolase; !1membrane-associated complex; mitochondrion; oxidative !1phosphorylation FEATURE !$1-25 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$26-298 #product H+-transporting ATP synthase gamma chain, !8splice form L #status experimental #label MATL\ !$26-297 #product H+-transporting ATP synthase gamma chain, !8splice form H #status experimental #label MATH SUMMARY #length 298 #molecular-weight 33072 #checksum 5814 SEQUENCE /// ENTRY PWECG #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) gamma chain - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 02-Apr-1982 #sequence_revision 15-Oct-1982 #text_change 01-Mar-2002 ACCESSIONS A01038; I41276; A01039; I55328; A53160; F65176 REFERENCE A93742 !$#authors Saraste, M.; Gay, N.J.; Eberle, A.; Runswick, M.J.; Walker, !1J.E. !$#journal Nucleic Acids Res. (1981) 9:5287-5296 !$#title The atp operon: nucleotide sequence of the genes for the !1gamma,beta, and epsilon subunits of Escherichia coli ATP !1synthase. !$#cross-references MUID:82059507; PMID:6272217 !$#accession A01038 !'##molecule_type DNA !'##residues 1-287 ##label SAR !'##cross-references GB:V00267; NID:g41036; PIDN:CAA23526.1; PID:g41037 REFERENCE I41271 !$#authors Kanazawa, H.; Futai, M. !$#journal Ann. N. Y. Acad. Sci. (1982) 402:45-64 !$#title Structure and function of H+-ATPase: What we have learned !1from Escherichia coli H+-ATPase. !$#cross-references MUID:83176724; PMID:6301339 !$#accession I41276 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-287 ##label RES !'##cross-references GB:M25464; NID:g146318; PIDN:AAA83874.1; !1PID:g146324 REFERENCE A90103 !$#authors Kanazawa, H.; Kayano, T.; Mabuchi, K.; Futai, M. !$#journal Biochem. Biophys. Res. Commun. (1981) 103:604-612 !$#title Nucleotide sequence of the genes coding for alpha, beta and !1gamma subunits of the proton-translocating ATPase of !1Escherichia coli. !$#cross-references MUID:82134798; PMID:6277310 !$#accession A01039 !'##molecule_type DNA !'##residues 1-37,'AWRPAVLMQKPGAQ',52-82,'I',84-92,'T',94-111, !1'HSTSQGAAR',121,'D',123-127,'A',129-165,'Y',167-197,'V', !1199-262,'T',264,'D',266-287 ##label KAN !'##cross-references GB:V00312; NID:g42282; PIDN:CAA23597.1; PID:g42284 REFERENCE I55328 !$#authors Iwamoto, A.; Miki, J.; Maeda, M.; Futai, M. !$#journal J. Biol. Chem. (1990) 265:5043-5048 !$#title H+-ATPase gamma-subunit of Escherichia coli: Role of the !1conserved carboxyl-terminal region. !$#cross-references MUID:90202983; PMID:2138624 !$#accession I55328 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 261-287 ##label RE2 !'##cross-references GB:M34095; NID:g148146; PIDN:AAA24742.1; !1PID:g148147 REFERENCE A53160 !$#authors Tang, C.; Wilkens, S.; Capaldi, R.A. !$#journal J. Biol. Chem. (1994) 269:4467-4472 !$#title Structure of the gamma subunit of Escherichia coli F-1 !1ATPase probed in trypsin digestion and biotin-avidin binding !1studies. !$#cross-references MUID:94140880; PMID:7508444 !$#accession A53160 !'##status preliminary !'##molecule_type protein !'##residues 2-8;72-81;82,204-208;214-220 ##label TAN REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65176 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-287 ##label BLAT !'##cross-references GB:AE000450; GB:U00096; NID:g1790166; !1PIDN:AAC76756.1; PID:g1790171; UWGP:b3733 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene atpG; uncG !$#map_position 84 min CLASSIFICATION #superfamily H+-transporting ATP synthase gamma chain KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex SUMMARY #length 287 #molecular-weight 31577 #checksum 2089 SEQUENCE /// ENTRY S06081 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) gamma chain - Vibrio alginolyticus ORGANISM #formal_name Vibrio alginolyticus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 14-Dec-2001 ACCESSIONS S06081 REFERENCE S06075 !$#authors Krumholz, L.R.; Esser, U.; Simoni, R.D. !$#journal Nucleic Acids Res. (1989) 17:7993-7994 !$#title Nucleotide sequence of the unc operon of Vibrio !1alginolyticus. !$#cross-references MUID:90016889; PMID:2529481 !$#accession S06081 !'##status translation not shown !'##molecule_type DNA !'##residues 1-288 ##label KRU !'##cross-references EMBL:X16050; NID:g48331; PIDN:CAA34180.1; !1PID:g48338 GENETICS !$#gene uncG CLASSIFICATION #superfamily H+-transporting ATP synthase gamma chain KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex SUMMARY #length 288 #molecular-weight 31889 #checksum 9858 SEQUENCE /// ENTRY E64071 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) gamma chain - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 14-Dec-2001 ACCESSIONS E64071 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession E64071 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-289 ##label TIGR !'##cross-references GB:U32730; GB:L42023; NID:g3212191; !1PIDN:AAC22138.1; PID:g1573458; TIGR:HI0480 CLASSIFICATION #superfamily H+-transporting ATP synthase gamma chain KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex SUMMARY #length 289 #molecular-weight 32069 #checksum 4356 SEQUENCE /// ENTRY PWQFG #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) gamma chain - Rhodospirillum rubrum ORGANISM #formal_name Rhodospirillum rubrum DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 14-Dec-2001 ACCESSIONS S08582 REFERENCE S07132 !$#authors Falk, G.; Hampe, A.; Walker, J.E. !$#journal Biochem. J. (1985) 228:391-407 !$#title Nucleotide sequence of the Rhodospirillum rubrum atp operon. !$#cross-references MUID:85251588; PMID:2861810 !$#accession S08582 !'##molecule_type DNA !'##residues 1-299 ##label FAL !'##cross-references EMBL:X02499; NID:g46360; PIDN:CAA26339.1; !1PID:g46367 GENETICS !$#gene atpG CLASSIFICATION #superfamily H+-transporting ATP synthase gamma chain KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex SUMMARY #length 299 #molecular-weight 32437 #checksum 1001 SEQUENCE /// ENTRY PWBYG #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) gamma chain - Synechocystis sp. ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 14-Dec-2001 ACCESSIONS S08257; S17752; S74582; A34256; S14867 REFERENCE A34256 !$#authors Werner, S.; Schumann, J.; Strotmann, H. !$#journal FEBS Lett. (1990) 261:204-208 !$#title The primary structure of the gamma-subunit of the ATPase !1from Synechocystis 6803. !$#cross-references MUID:90169116; PMID:2137788 !$#accession S08257 !'##molecule_type DNA !'##residues 1-314 ##label WER !'##cross-references EMBL:Y07532; NID:g48007; PIDN:CAA68819.1; !1PID:g48008 REFERENCE S17745 !$#authors Lill, H.; Nelson, N. !$#journal Plant Mol. Biol. (1991) 17:641-652 !$#title The atp1 and atp2 operons of the cyanobacterium !1Synechocystis sp. PCC 6803. !$#cross-references MUID:92003679; PMID:1832989 !$#accession S17752 !'##molecule_type DNA !'##residues 1-314 ##label LIL !'##cross-references EMBL:X58128; NID:g47506; PIDN:CAA41136.1; !1PID:g47514 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74582 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-314 ##label KAN !'##cross-references EMBL:D90900; GB:AB001339; NID:g1651768; !1PIDN:BAA16734.1; PID:g1651807 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene atpC CLASSIFICATION #superfamily H+-transporting ATP synthase gamma chain KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex SUMMARY #length 314 #molecular-weight 34605 #checksum 8352 SEQUENCE /// ENTRY PWYCG #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) gamma chain - Synechococcus sp. (strain PCC 6301) ORGANISM #formal_name Synechococcus sp. DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 14-Dec-2001 ACCESSIONS S10832; S00604 REFERENCE S07286 !$#authors Cozens, A.L.; Walker, J.E. !$#journal J. Mol. Biol. (1987) 194:359-383 !$#title The organization and sequence of the genes for ATP synthase !1subunits in the cyanobacterium Synechococcus 6301. Support !1for an endosymbiotic origin of chloroplasts. !$#cross-references MUID:87311713; PMID:3041005 !$#accession S10832 !'##molecule_type DNA !'##residues 1-316 ##label COZ !'##cross-references EMBL:X05302; NID:g48009; PIDN:CAA28929.1; !1PID:g48018 CLASSIFICATION #superfamily H+-transporting ATP synthase gamma chain KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex SUMMARY #length 316 #molecular-weight 34806 #checksum 4221 SEQUENCE /// ENTRY PWSPG #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) gamma chain precursor, chloroplast - spinach ORGANISM #formal_name Spinacia oleracea #common_name spinach DATE 30-Jun-1990 #sequence_revision 30-Jun-1991 #text_change 14-Dec-2001 ACCESSIONS S10163; A34970; S00614; A34971; S47468; S62643; S08543 REFERENCE S10163 !$#authors Mason, J.G.; Whitfeld, P.R. !$#journal Plant Mol. Biol. (1990) 14:1007-1018 !$#title The gamma-subunit of spinach chloroplast ATP synthase: !1isolation and characterisation of cDNA and genomic clones. !$#cross-references MUID:91346685; PMID:2151716 !$#accession S10163 !'##molecule_type DNA !'##residues 1-364 ##label MAS !'##cross-references EMBL:X17257; NID:g21237; PIDN:CAA35158.1; !1PID:g21238 !$#accession A34970 !'##molecule_type mRNA !'##residues 1-364 ##label MAS2 !'##cross-references GB:X17257; NID:g21237; PIDN:CAA35158.1; PID:g21238 REFERENCE S00614 !$#authors Miki, J.; Maeda, M.; Mukohata, Y.; Futai, M. !$#journal FEBS Lett. (1988) 232:221-226 !$#title The gamma-subunit of ATP synthase from spinach chloroplasts. !1Primary structure deduced from the cloned cDNA sequence. !$#cross-references MUID:88211863; PMID:2896606 !$#accession S00614 !'##molecule_type mRNA !'##residues 36-364 ##label MIK !'##cross-references EMBL:Y00758; NID:g21241; PIDN:CAA68727.1; !1PID:g755801 !$#accession A34971 !'##molecule_type protein !'##residues 42-61 ##label MIK2 REFERENCE S08543 !$#authors Moroney, J.V.; Fullmer, C.S.; McCarty, R.E. !$#journal J. Biol. Chem. (1984) 259:7281-7285 !$#title Characterization of the cysteinyl-containing peptides of the !1gamma subunit of coupling factor 1. !$#cross-references MUID:84212589; PMID:6233281 !$#contents annotation; disulfide bonds !$#note the Cys-130 residue has a free thiol that is readily !1alkylated by 4-vinylpyridine REFERENCE S47468 !$#authors Bolle, X.Y.Z.; Kusnetsov, X.Y.Z.; Herrmann, X.Y.Z.; !1Oelmueller, R. !$#submission submitted to the EMBL Data Library, November 1993 !$#accession S47468 !'##status preliminary !'##molecule_type DNA !'##residues 1-364 ##label BOL !'##cross-references EMBL:X76131; NID:g531110; PIDN:CAA53734.1; !1PID:g531111 REFERENCE S62643 !$#authors Komatsu-Takaki, M. !$#journal Eur. J. Biochem. (1996) 236:470-475 !$#title Energizing effects of illumination on the reactivities of !1lysine residues of the gamma subunit of chloroplast ATP !1synthase. !$#cross-references MUID:96195654; PMID:8612618 !$#accession S62643 !'##status preliminary !'##molecule_type protein !'##residues 42-50;63-66;148-153;207-215;239-242;254-257;262-273;333-337 !1##label KOM GENETICS !$#gene atpC !$#genome nuclear !$#introns 178/2; 262/1 CLASSIFICATION #superfamily H+-transporting ATP synthase gamma chain KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; thylakoid FEATURE !$1-41 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$42-364 #product H+-transporting ATP synthase gamma chain !8#status experimental #label MAT\ !$130 #active_site Cys #status experimental\ !$240-246 #disulfide_bonds #status experimental SUMMARY #length 364 #molecular-weight 40074 #checksum 7743 SEQUENCE /// ENTRY PWNTG #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) gamma chain precursor, chloroplast - common tobacco ORGANISM #formal_name Nicotiana tabacum #common_name common tobacco DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 14-Dec-2001 ACCESSIONS S22486; S23615; S18949 REFERENCE S22486 !$#authors Larsson, K.H.; Napier, J.A.; Gray, J.C. !$#journal Plant Mol. Biol. (1992) 19:343-349 !$#title Import and processing of the precursor form of the gamma !1subunit of the chloroplast ATP synthase from tobacco. !$#cross-references MUID:92322965; PMID:1535803 !$#accession S22486 !'##molecule_type mRNA !'##residues 1-377 ##label LAR !'##cross-references EMBL:X63606; NID:g19784; PIDN:CAA45152.1; !1PID:g19785 !$#accession S23615 !'##molecule_type protein !'##residues 56-57,'X',59-60 ##label LA2 GENETICS !$#gene atpC CLASSIFICATION #superfamily H+-transporting ATP synthase gamma chain KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; thylakoid FEATURE !$1-55 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$56-377 #product H+-transporting ATP synthase gamma chain !8#status experimental #label MAT\ !$253-259 #disulfide_bonds #status predicted SUMMARY #length 377 #molecular-weight 41446 #checksum 4007 SEQUENCE /// ENTRY PWKMG #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) gamma chain precursor, chloroplast - Chlamydomonas reinhardtii ALTERNATE_NAMES ATP synthase gamma chain ORGANISM #formal_name Chlamydomonas reinhardtii DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 14-Dec-2001 ACCESSIONS A32004; S68390 REFERENCE A32004 !$#authors Yu, L.M.; Selman, B.R. !$#journal J. Biol. Chem. (1988) 263:19342-19345 !$#title cDNA sequence and predicted primary structure of the gamma !1subunit from the ATP synthase from Chlamydomonas !1reinhardtii. !$#cross-references MUID:89066748; PMID:2904436 !$#accession A32004 !'##molecule_type mRNA !'##residues 1-358 ##label YUL !'##cross-references GB:J04219; NID:g167404; PIDN:AAA33080.1; !1PID:g167405 !'##note the authors translated the codon CCC for residue 77 as Thr REFERENCE S68388 !$#authors Fiedler, H.R.; Schmid, R.; Leu, S.; Shavit, N.; Strotmann, !1H. !$#journal FEBS Lett. (1995) 377:163-166 !$#title Isolation of CF(0)CF(1) from Chlamydomonas reinhardtii cw15 !1and the N-terminal amino acid sequences of the CF(0)CF(1) !1subunits. !$#cross-references MUID:96128220; PMID:8543042 !$#accession S68390 !'##molecule_type protein !'##residues 36-62 ##label FIE !'##experimental_source strain CW15 GENETICS !$#genome nuclear CLASSIFICATION #superfamily H+-transporting ATP synthase gamma chain KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; peripheral membrane protein; !1thylakoid FEATURE !$1-35 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$36-358 #product H+-transporting ATP synthase gamma chain !8#status experimental #label MAT\ !$233-239 #disulfide_bonds #status predicted SUMMARY #length 358 #molecular-weight 38760 #checksum 8519 SEQUENCE /// ENTRY H69227 #type complete TITLE ATP synthase, subunit F - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS H69227 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession H69227 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-106 ##label MTH !'##cross-references GB:AE000869; GB:AE000666; NID:g2622042; !1PIDN:AAB85452.1; PID:g2622053 !'##experimental_source strain Delta H GENETICS !$#gene MTH956 CLASSIFICATION #superfamily H+-transporting ATP synthase subunit F SUMMARY #length 106 #molecular-weight 11764 #checksum 8465 SEQUENCE /// ENTRY C64327 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) subunit F - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 14-Dec-2001 ACCESSIONS C64327 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession C64327 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-98 ##label BUL !'##cross-references GB:U67477; GB:L77117; NID:g1590949; !1PIDN:AAB98201.1; PID:g1498994; TIGR:MJ0218 GENETICS !$#map_position REV209307-209011 CLASSIFICATION #superfamily H+-transporting ATP synthase subunit F KEYWORDS hydrolase SUMMARY #length 98 #molecular-weight 10941 #checksum 7251 SEQUENCE /// ENTRY S34066 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) lipid-binding protein P1 precursor, mitochondrial [validated] - human ALTERNATE_NAMES H+-transporting ATP synthase chain 9.1; H+-transporting ATP synthase chain c form P1 ORGANISM #formal_name Homo sapiens #common_name man DATE 26-Aug-1999 #sequence_revision 26-Aug-1999 #text_change 14-Dec-2001 ACCESSIONS S34066; S32519; A27036; T12475; S58658; JS0743 REFERENCE S34066 !$#authors Dyer, M.R.; Walker, J.E. !$#journal Biochem. J. (1993) 293:51-64 !$#title Sequences of members of the human gene family for the c !1subunit of mitochondrial ATP synthase. !$#cross-references MUID:93319529; PMID:8328972 !$#accession S34066 !'##molecule_type DNA !'##residues 1-136 ##label DYE !'##cross-references EMBL:X69907; NID:g38429; PIDN:CAA49532.1; !1PID:g38430 REFERENCE S32519 !$#authors Higuti, T.; Kawamura, Y.; Kuroiwa, K.; Miyazaki, S.; !1Tsujita, H. !$#journal Biochim. Biophys. Acta (1993) 1173:87-90 !$#title Molecular cloning and sequence of two cDNAs for human !1subunit c of H(+)-ATP synthase in mitochondria. !$#cross-references MUID:93250054; PMID:8485160 !$#accession S32519 !'##molecule_type mRNA !'##residues 1-136 ##label HI2 !'##cross-references DDBJ:D13118; NID:g285907; PIDN:BAA02420.1; !1PID:g285908 !'##experimental_source hepatocyte, cell line HepG2 !'##note submitted to JIPID, September 1992 REFERENCE A90132 !$#authors Farrell, L.B.; Nagley, P. !$#journal Biochem. Biophys. Res. Commun. (1987) 144:1257-1264 !$#title Human liver cDNA clones encoding proteolipid subunit 9 of !1the mitochondrial ATPase complex. !$#cross-references MUID:87213321; PMID:2883974 !$#accession A27036 !'##molecule_type mRNA !'##residues 37-52,'G',54-136 ##label FAR !'##cross-references GB:M16453; NID:g179254; PIDN:AAA51806.1; !1PID:g179255 !'##note the authors translated the codon GGC for residue 53 as Glu and !1CCG for residue 101 as Arg REFERENCE Z17526 !$#authors Blum, H.; Bauersachs, S.; Mewes, H.W.; Gassenhuber, J.; !1Wiemann, S. !$#submission submitted to the Protein Sequence Database, June 1999 !$#accession T12475 !'##status preliminary !'##molecule_type mRNA !'##residues 1-136 ##label BLU !'##cross-references EMBL:AL080089 !'##experimental_source fetal brain; clone DKFZp564L2362 REFERENCE S58658 !$#authors Katz, M.L.; Gao, C.L.; Tompkins, J.A.; Bronson, R.T.; Chin, !1D.T. !$#journal Biochem. J. (1995) 310:887-892 !$#title Mitochondrial ATP synthase subunit c stored in hereditary !1ceroid-lipofuscinosis contains trimethyl-lysine. !$#cross-references MUID:96013188; PMID:7575423 !$#accession S58658 !'##status preliminary !'##molecule_type protein !'##residues 62-103,'X',105-109 ##label KAT !'##note trimethyllysine occurs in the abnormal, lysosomal storage !1disease form, and not in the normal mitochondrial form GENETICS !$#gene GDB:ATP5G1; ATP5G !'##cross-references GDB:137190 !$#map_position 14pter-14qter !$#genome nuclear !$#introns 13/3; 39/3; 99/2 !$#note DKFZp564L2362.1 CLASSIFICATION #superfamily H+-transporting ATP synthase lipid-binding !1protein KEYWORDS ATP biosynthesis; hydrolase; lysosomal storage disease; !1membrane-associated complex; methylated amino acid; !1mitochondrion; oxidative phosphorylation; transmembrane !1protein FEATURE !$1-61 #domain transit peptide (mitochondrion) #status !8predicted #label TRP\ !$62-136 #product H+-transporting ATP synthase lipid-binding !8protein #status experimental #label MAT\ !$69-97 #domain transmembrane #status predicted #label TM1\ !$107-136 #domain transmembrane #status predicted #label TM2\ !$104 #modified_site N6,N6,N6-trimethyllysine (Lys) (in !8lysosomal form) #status atypical\ !$119 #active_site Glu #status predicted SUMMARY #length 136 #molecular-weight 14277 #checksum 3281 SEQUENCE /// ENTRY LWBOA #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) lipid-binding protein P1 precursor - bovine ALTERNATE_NAMES H+-transporting ATP synthase chain 9.1; H+-transporting ATP synthase chain c form P1 ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Jul-1979 #sequence_revision 23-Mar-1995 #text_change 14-Dec-2001 ACCESSIONS A24578; A01040; B39566 REFERENCE A91026 !$#authors Gay, N.J.; Walker, J.E. !$#journal EMBO J. (1985) 4:3519-3524 !$#title Two genes encoding the bovine mitochondrial ATP synthase !1proteolipid specify precursors with different import !1sequences and are expressed in a tissue-specific manner. !$#cross-references MUID:86135991; PMID:2868890 !$#accession A24578 !'##molecule_type mRNA !'##residues 1-136 ##label GAY !'##cross-references GB:X05218; NID:g95; PIDN:CAA28845.1; PID:g96 REFERENCE A94415 !$#authors Sebald, W.; Hoppe, J.; Wachter, E. !$#book Function and Molecular Aspects of Biomembrane Transport, !1Quagliariello, E., et al., eds., pp.63-74, Elsevier/ !1North-Holland, Amsterdam, 1979 !$#title Amino acid sequence of the ATPase proteolipid from !1mitochondria, chloroplasts and bacteria (wild type and !1mutants). !$#accession A01040 !'##molecule_type protein !'##residues 62-136 ##label SEB !'##experimental_source heart REFERENCE A39566 !$#authors Walker, J.E.; Lutter, R.; Dupuis, A.; Runswick, M.J. !$#journal Biochemistry (1991) 30:5369-5378 !$#title Identification of the subunits of F-1F-0-ATPase from bovine !1heart mitochondria. !$#cross-references MUID:91242449; PMID:1827992 !$#accession B39566 !'##molecule_type protein !'##residues 62-71 ##label WAL GENETICS !$#gene P1 CLASSIFICATION #superfamily H+-transporting ATP synthase lipid-binding !1protein KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; oxidative phosphorylation; transmembrane !1protein FEATURE !$1-61 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$62-136 #product H+-transporting ATP synthase lipid-binding !8protein #status experimental #label MAT\ !$69-97 #domain transmembrane #status predicted #label TM1\ !$107-136 #domain transmembrane #status predicted #label TM2\ !$119 #active_site Glu #status predicted SUMMARY #length 136 #molecular-weight 14222 #checksum 3642 SEQUENCE /// ENTRY S31769 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) lipid-binding protein P1 precursor - sheep ALTERNATE_NAMES H+-transporting ATP synthase chain 9.1; H+-transporting ATP synthase chain c form P1 ORGANISM #formal_name Ovis orientalis aries, Ovis ammon aries #common_name domestic sheep DATE 26-Aug-1999 #sequence_revision 26-Aug-1999 #text_change 14-Dec-2001 ACCESSIONS S34068; S10673; A32859; S58659; S31769 REFERENCE S34068 !$#authors Medd, S.M.; Walker, J.E.; Jolly, R.D. !$#journal Biochem. J. (1993) 293:65-73 !$#title Characterization of the expressed genes for subunit c of !1mitochondrial ATP synthase in sheep with ceroid !1lipofuscinosis. !$#cross-references MUID:93319530; PMID:8328973 !$#accession S34068 !'##molecule_type mRNA !'##residues 1-136 ##label ME2 !'##cross-references EMBL:X69904; NID:g1200; PIDN:CAA49529.1; PID:g1201 REFERENCE S10673 !$#authors Fearnley, I.M.; Walker, J.E.; Martinus, R.D.; Jolly, R.D.; !1Kirkland, K.B.; Shaw, G.J.; Palmer, D.N. !$#journal Biochem. J. (1990) 268:751-758 !$#title The sequence of the major protein stored in ovine ceroid !1lipofuscinosis is identical with that of the !1dicyclohexylcarbodi-imide-reactive proteolipid of !1mitochondrial ATP synthase. !$#cross-references MUID:90303272; PMID:2141977 !$#accession S10673 !'##molecule_type protein !'##residues 62-136 ##label FEA REFERENCE A32859 !$#authors Palmer, D.N.; Martinus, R.D.; Cooper, S.M.; Midwinter, G.G.; !1Reid, J.C.; Jolly, R.D. !$#journal J. Biol. Chem. (1989) 264:5736-5740 !$#title Ovine ceroid lipofuscinosis. The major lipopigment protein !1and the lipid-binding subunit of mitochondrial ATP synthase !1have the same NH-2-terminal sequence. !$#cross-references MUID:89174627; PMID:2522438 !$#accession A32859 !'##status preliminary !'##molecule_type protein !'##residues 62-101 ##label PAL REFERENCE S58658 !$#authors Katz, M.L.; Gao, C.L.; Tompkins, J.A.; Bronson, R.T.; Chin, !1D.T. !$#journal Biochem. J. (1995) 310:887-892 !$#title Mitochondrial ATP synthase subunit c stored in hereditary !1ceroid-lipofuscinosis contains trimethyl-lysine. !$#cross-references MUID:96013188; PMID:7575423 !$#accession S58659 !'##molecule_type protein !'##residues 62-71;100-103,'X',105-109 ##label KAT !'##note trimethyllysine occurs in the abnormal, lysosomal storage !1disease form, and not in the normal mitochondrial form GENETICS !$#genome nuclear CLASSIFICATION #superfamily H+-transporting ATP synthase lipid-binding !1protein KEYWORDS ATP biosynthesis; hydrolase; lysosomal storage disease; !1membrane-associated complex; methylated amino acid; !1mitochondrion; oxidative phosphorylation; transmembrane !1protein FEATURE !$1-61 #domain transit peptide (mitochondrion) #status !8predicted #label TRP\ !$62-136 #product H+-transporting ATP synthase lipid-binding !8protein #status experimental #label MAT\ !$69-97 #domain transmembrane #status predicted #label TM1\ !$107-136 #domain transmembrane #status predicted #label TM2\ !$104 #modified_site N6,N6,N6-trimethyllysine (Lys) (in !8lysosomal form) #status atypical\ !$119 #active_site Glu #status predicted SUMMARY #length 136 #molecular-weight 14191 #checksum 3606 SEQUENCE /// ENTRY S34067 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) lipid-binding protein P2 precursor, mitochondrial - human ALTERNATE_NAMES H+-transporting ATP synthase c chain form P2; H+-transporting ATP synthase chain 9.2 ORGANISM #formal_name Homo sapiens #common_name man DATE 26-Aug-1999 #sequence_revision 26-Aug-1999 #text_change 14-Dec-2001 ACCESSIONS S34067; JS0744; S32520; B27036 REFERENCE S34066 !$#authors Dyer, M.R.; Walker, J.E. !$#journal Biochem. J. (1993) 293:51-64 !$#title Sequences of members of the human gene family for the c !1subunit of mitochondrial ATP synthase. !$#cross-references MUID:93319529; PMID:8328972 !$#accession S34067 !'##molecule_type DNA !'##residues 1-141 ##label DYE !'##cross-references EMBL:X69908; NID:g38431; PIDN:CAA49533.1; !1PID:g38432 REFERENCE JS0743 !$#authors Higuti, T.; Kawamura, Y.; Kuroiwa, K.; Tsujita, H. !$#submission submitted to JIPID, September 1992 !$#description Molecular cloning of cDNA for the import precursor of human !1subunit c of H+-ATP synthase in mitochondria encoded by the !1P2 gene. !$#accession JS0744 !'##molecule_type mRNA !'##residues 1-141 ##label HIG1 !'##cross-references DDBJ:D13119; NID:g285909; PIDN:BAA02421.1; !1PID:g285910 !'##experimental_source hepatocyte, cell line HepG2 REFERENCE S32519 !$#authors Higuti, T.; Kawamura, Y.; Kuroiwa, K.; Miyazaki, S.; !1Tsujita, H. !$#journal Biochim. Biophys. Acta (1993) 1173:87-90 !$#title Molecular cloning and sequence of two cDNAs for human !1subunit c of H(+)-ATP synthase in mitochondria. !$#cross-references MUID:93250054; PMID:8485160 !$#accession S32520 !'##status preliminary !'##molecule_type mRNA !'##residues 1-141 ##label HIG2 !'##note this publication is not cited in GenBank entry HUMATPSCP2, !1release 111.0 REFERENCE A90132 !$#authors Farrell, L.B.; Nagley, P. !$#journal Biochem. Biophys. Res. Commun. (1987) 144:1257-1264 !$#title Human liver cDNA clones encoding proteolipid subunit 9 of !1the mitochondrial ATPase complex. !$#cross-references MUID:87213321; PMID:2883974 !$#accession B27036 !'##molecule_type mRNA !'##residues 'RLS',87-141 ##label FAR !'##cross-references GB:M16439; NID:g179233; PIDN:AAA51804.1; !1PID:g179234 !'##note the sequence in GenBank entry HUMATPASE, release 111.0, !1(PIDN:AAA51804.1, PID:g179234) has the codon GTG for 35-Leu !1rather than the published CTG GENETICS !$#gene GDB:ATP5G2 !'##cross-references GDB:373090 !$#map_position 14pter-14qter !$#genome nuclear !$#introns 13/3; 39/3; 104/2 CLASSIFICATION #superfamily H+-transporting ATP synthase lipid-binding !1protein KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; oxidative phosphorylation; transmembrane !1protein FEATURE !$1-66 #domain transit peptide (mitochondrion) #status !8predicted #label TRP\ !$67-141 #product H+-transporting ATP synthase lipid-binding !8protein #status predicted #label MAT\ !$74-102 #domain transmembrane #status predicted #label TM1\ !$112-141 #domain transmembrane #status predicted #label TM2\ !$124 #active_site Glu #status predicted SUMMARY #length 141 #molecular-weight 14637 #checksum 3093 SEQUENCE /// ENTRY S04230 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) lipid-binding protein P2 precursor - bovine ALTERNATE_NAMES H+-transporting ATP synthase chain 9.2; H+-transporting ATP synthase chain c form P2 ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 28-Feb-1990 #sequence_revision 23-Mar-1995 #text_change 14-Dec-2001 ACCESSIONS S04230; B24578; A01040; B39566 REFERENCE S04230 !$#authors Dyer, M.R.; Gay, N.J.; Walker, J.E. !$#journal Biochem. J. (1989) 260:249-258 !$#title DNA sequences of a bovine gene and of two related !1pseudogenes for the proteolipid subunit of mitochondrial ATP !1synthase. !$#cross-references MUID:89374049; PMID:2549952 !$#accession S04230 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-143 ##label DYE REFERENCE A91026 !$#authors Gay, N.J.; Walker, J.E. !$#journal EMBO J. (1985) 4:3519-3524 !$#title Two genes encoding the bovine mitochondrial ATP synthase !1proteolipid specify precursors with different import !1sequences and are expressed in a tissue-specific manner. !$#cross-references MUID:86135991; PMID:2868890 !$#accession B24578 !'##molecule_type mRNA !'##residues 1-143 ##label GAY !'##cross-references GB:X05219; NID:g98; PIDN:CAA28846.1; PID:g99 REFERENCE A94415 !$#authors Sebald, W.; Hoppe, J.; Wachter, E. !$#book Function and Molecular Aspects of Biomembrane Transport, !1Quagliariello, E., et al., eds., pp.63-74, Elsevier/ !1North-Holland, Amsterdam, 1979 !$#title Amino acid sequence of the ATPase proteolipid from !1mitochondria, chloroplasts and bacteria (wild type and !1mutants). !$#accession A01040 !'##molecule_type protein !'##residues 69-143 ##label SEB !'##experimental_source heart REFERENCE A39566 !$#authors Walker, J.E.; Lutter, R.; Dupuis, A.; Runswick, M.J. !$#journal Biochemistry (1991) 30:5369-5378 !$#title Identification of the subunits of F-1F-0-ATPase from bovine !1heart mitochondria. !$#cross-references MUID:91242449; PMID:1827992 !$#accession B39566 !'##molecule_type protein !'##residues 69-78 ##label WAL GENETICS !$#gene P2 !$#introns 13/3; 39/3; 106/2 CLASSIFICATION #superfamily H+-transporting ATP synthase lipid-binding !1protein KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; oxidative phosphorylation; transmembrane !1protein FEATURE !$1-68 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$69-143 #product H+-transporting ATP synthase lipid-binding !8protein #status experimental #label MAT\ !$76-104 #domain transmembrane #status predicted #label TM1\ !$114-143 #domain transmembrane #status predicted #label TM2\ !$126 #active_site Glu #status predicted SUMMARY #length 143 #molecular-weight 15028 #checksum 8642 SEQUENCE /// ENTRY I38612 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) lipid-binding protein P3 precursor, mitochondrial - human ALTERNATE_NAMES H+-transporting ATP synthase chain 9.3; H+-transporting ATP synthase chain c form P3 ORGANISM #formal_name Homo sapiens #common_name man DATE 26-Aug-1999 #sequence_revision 26-Aug-1999 #text_change 14-Dec-2001 ACCESSIONS I38612 REFERENCE A55687 !$#authors Yan, W.L.; Lerner, T.J.; Haines, J.L.; Gusella, J.F. !$#journal Genomics (1994) 24:375-377 !$#title Sequence analysis and mapping of a novel human mitochondrial !1ATP synthase subunit 9 cDNA (ATP5G3). !$#cross-references MUID:95213032; PMID:7698763 !$#accession I38612 !'##status preliminary !'##molecule_type mRNA !'##residues 1-142 ##label YAN !'##cross-references EMBL:U09813; NID:g1008454; PIDN:AAA78807.1; !1PID:g511450 GENETICS !$#gene GDB:ATP5G3 !'##cross-references GDB:375306 !$#map_position 2pter-2qter !$#genome nuclear CLASSIFICATION #superfamily H+-transporting ATP synthase lipid-binding !1protein KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; oxidative phosphorylation; transmembrane !1protein FEATURE !$1-67 #domain transit peptide (mitochondrion) #status !8predicted #label TRP\ !$68-142 #product H+-transporting ATP synthase lipid-binding !8protein #status predicted #label MAT\ !$75-103 #domain transmembrane #status predicted #label TM1\ !$113-142 #domain transmembrane #status predicted #label TM2\ !$125 #active_site Glu #status predicted SUMMARY #length 142 #molecular-weight 14693 #checksum 2178 SEQUENCE /// ENTRY LWZMA #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) lipid-binding protein - maize mitochondrion ALTERNATE_NAMES hydrogen ion-transporting ATP synthase protein 9 ORGANISM #formal_name mitochondrion Zea mays #common_name maize DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 14-Dec-2001 ACCESSIONS A01041; S70026 REFERENCE A01041 !$#authors Dewey, R.E.; Schuster, A.M.; Levings III, C.S.; Timothy, !1D.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:1015-1019 !$#title Nucleotide sequence of F0-ATPase proteolipid (subunit 9) !1gene of maize mitochondria. !$#accession A01041 !'##molecule_type DNA !'##residues 1-74 ##label DEW !'##cross-references EMBL:M10408; NID:g342637; PIDN:AAA70271.1; !1PID:g897621 REFERENCE S70024 !$#authors Grosskopf, D.; Mulligan, R.M. !$#journal Curr. Genet. (1996) 29:556-563 !$#title Developmental- and tissue-specificity of RNA editing in !1mitochondria of suspension-cultured maize cells and !1seedlings. !$#cross-references MUID:96269915; PMID:8662195 !$#accession S70026 !'##molecule_type DNA !'##residues 1-74 ##label GRO GENETICS !$#gene atp9 !$#genome mitochondrion CLASSIFICATION #superfamily H+-transporting ATP synthase lipid-binding !1protein KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; oxidative phosphorylation; RNA editing; !1transmembrane protein FEATURE !$8-32 #domain transmembrane #status predicted #label TM1\ !$45-74 #domain transmembrane #status predicted #label TM2\ !$57 #active_site Glu #status predicted SUMMARY #length 74 #molecular-weight 7377 #checksum 5509 SEQUENCE /// ENTRY LWFSM #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) lipid-binding protein - common sunflower mitochondrion ALTERNATE_NAMES mitochondrial ATPase subunit 9 ORGANISM #formal_name mitochondrion Helianthus annuus #common_name common sunflower DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 14-Dec-2001 ACCESSIONS S09241 REFERENCE S09241 !$#authors Recipon, H. !$#journal Nucleic Acids Res. (1990) 18:1644 !$#title The sequence of the sunflower mitochondrial ATPase subunit 9 !1gene. !$#cross-references MUID:90221908; PMID:2139211 !$#accession S09241 !'##molecule_type DNA !'##residues 1-83 ##label REC !'##cross-references EMBL:X51895; NID:g12983; PIDN:CAA36177.1; !1PID:g12984 GENETICS !$#gene atp9 !$#genome mitochondrion CLASSIFICATION #superfamily H+-transporting ATP synthase lipid-binding !1protein KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; oxidative phosphorylation; transmembrane !1protein FEATURE !$8-32 #domain transmembrane #status predicted #label TM1\ !$45-74 #domain transmembrane #status predicted #label TM2\ !$57 #active_site Glu #status predicted SUMMARY #length 83 #molecular-weight 8268 #checksum 286 SEQUENCE /// ENTRY LWPJA #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) lipid-binding protein (atp9-2) - garden petunia mitochondrion ALTERNATE_NAMES H+-transporting ATP synthase protein 9; proteolipid ORGANISM #formal_name mitochondrion Petunia x hybrida #common_name garden petunia DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 14-Dec-2001 ACCESSIONS S00271 REFERENCE S00271 !$#authors Rothenberg, M.; Hanson, M.R. !$#journal Mol. Gen. Genet. (1987) 209:21-27 !$#title Different transcript abundance of two divergent ATP synthase !1subunit 9 genes in the mitochondrial genome of Petunia !1hybrida. !$#accession S00271 !'##molecule_type DNA !'##residues 1-77 ##label ROT !'##cross-references EMBL:X05807 !'##note the authors translated the codon AAT for residues 15 and 59 as !1Ile; the sequence shown follows the authors' translation GENETICS !$#gene atp9-2 !$#genome mitochondrion CLASSIFICATION #superfamily H+-transporting ATP synthase lipid-binding !1protein KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; oxidative phosphorylation; transmembrane !1protein FEATURE !$8-32 #domain transmembrane #status predicted #label TM1\ !$45-74 #domain transmembrane #status predicted #label TM2\ !$57 #active_site Glu #status predicted SUMMARY #length 77 #molecular-weight 7792 #checksum 9791 SEQUENCE /// ENTRY LWTOA #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) lipid-binding protein - tomato mitochondrion ALTERNATE_NAMES H+-transporting ATP synthase protein 9 ORGANISM #formal_name mitochondrion Lycopersicon esculentum #common_name tomato DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 14-Dec-2001 ACCESSIONS S11494 REFERENCE S11494 !$#authors Kazama, S.; Suzuki, T.; Kadowaki, K.; Akihama, T. !$#journal Nucleic Acids Res. (1990) 18:5879 !$#title Nucleotide sequence of the F0-ATPase subunit 9 gene from !1tomato mitochondria. !$#cross-references MUID:91016929; PMID:2145550 !$#accession S11494 !'##molecule_type DNA !'##residues 1-77 ##label KAZ !'##cross-references EMBL:X54409; NID:g13077; PIDN:CAA38272.1; !1PID:g13078 GENETICS !$#gene atp9 !$#genome mitochondrion CLASSIFICATION #superfamily H+-transporting ATP synthase lipid-binding !1protein KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; oxidative phosphorylation; transmembrane !1protein FEATURE !$8-32 #domain transmembrane #status predicted #label TM1\ !$45-74 #domain transmembrane #status predicted #label TM2\ !$57 #active_site Glu #status predicted SUMMARY #length 77 #molecular-weight 7792 #checksum 9791 SEQUENCE /// ENTRY LWNTM #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) lipid-binding protein - common tobacco mitochondrion ALTERNATE_NAMES H+-transporting ATP synthase protein 9 ORGANISM #formal_name mitochondrion Nicotiana tabacum #common_name common tobacco DATE 30-Jun-1992 #sequence_revision 14-Aug-1998 #text_change 14-Dec-2001 ACCESSIONS S22640; S78109; S01846; S19862 REFERENCE S22640 !$#authors Hernould, M.; Mouras, A.; Litvak, S.; Araya, A. !$#journal Nucleic Acids Res. (1992) 20:1809 !$#title RNA editing of the mitochondrial atp9 transcript from !1tobacco. !$#cross-references MUID:92253394; PMID:1533714 !$#accession S22640 !'##molecule_type mRNA !'##residues 1-74 ##label HER !'##cross-references EMBL:X64423; NID:g14136; PIDN:CAA45770.1; !1PID:g14137 !'##experimental_source strain SR1 !'##note the authors translated the codon TTA for residue 71 as Ser !'##note 7-Leu, 17-Leu, 28-Phe, 31-Leu, 61-Leu, and 64-Leu are due to !1RNA editing !$#accession S78109 !'##molecule_type DNA !'##residues 1-6,'S',8-16,'S',18-27,'L',29-30,'S',32-60,'S',62-63,'P', !165-74 ##label HEW !'##cross-references EMBL:X64423 REFERENCE S01427 !$#authors Bland, M.M.; Levings III, C.S.; Matzinger, D.F. !$#journal Mol. Gen. Genet. (1986) 204:8-16 !$#title The tobacco mitochondrial ATPase subunit 9 gene is closely !1linked to an open reading frame for a ribosomal protein. !$#cross-references MUID:86310310; PMID:2875379 !$#accession S01846 !'##molecule_type DNA !'##residues 1-6,'S',8-16,'S',18-27,'L',29-30,'S',32-60,'S',62-63,'P', !165-70,'S',72-74,'QVR' ##label BLA !'##cross-references EMBL:X04019; NID:g13148; PIDN:CAA27644.1; !1PID:g13149 GENETICS !$#gene atp9 !$#genome mitochondrion CLASSIFICATION #superfamily H+-transporting ATP synthase lipid-binding !1protein KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; oxidative phosphorylation; RNA editing; !1transmembrane protein FEATURE !$8-32 #domain transmembrane #status predicted #label TM1\ !$45-74 #domain transmembrane #status predicted #label TM2\ !$57 #active_site Glu #status predicted SUMMARY #length 74 #molecular-weight 7589 #checksum 4352 SEQUENCE /// ENTRY LWRZM #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) lipid-binding protein - rice mitochondrion ALTERNATE_NAMES ATP synthase protein 9 ORGANISM #formal_name mitochondrion Oryza sativa #common_name rice DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 14-Dec-2001 ACCESSIONS JQ0563; S12166; JQ0165; S07876; S10510 REFERENCE JQ0563 !$#authors Xie, Y.; Wu, R. !$#journal Nucleic Acids Res. (1990) 18:4268 !$#title Nucleotide sequences of mitochondrial ATPase subunit 9 genes !1from three lines of rice (Oryza sativa L.). !$#cross-references MUID:90332441; PMID:2143016 !$#accession JQ0563 !'##molecule_type DNA !'##residues 1-77 ##label XIE !'##note the cited EMBL accession number, X52651, is not in Genbank !1release 101.0 REFERENCE S12166 !$#authors Wu, R. !$#submission submitted to the EMBL Data Library, April 1990 !$#accession S12166 !'##molecule_type DNA !'##residues 1-17,'R',19-77 ##label WUR !'##note the cited EMBL accession number, X52651, is not in Genbank !1release 101.0 REFERENCE JQ0165 !$#authors Kaleikau, E.K.; Andre, C.P.; Walbot, V. !$#journal Nucleic Acids Res. (1990) 18:370 !$#title Sequence of the F0-atpase proteolipid (atp9) gene from rice !1mitochondria. !$#cross-references MUID:90221828; PMID:2139209 !$#accession JQ0165 !'##molecule_type DNA !'##residues 1-7,'I',9-16,'L',18-21,'V',23-60,'L',62-74,'DHIFLGVDISLCK' !1##label KAL !'##cross-references EMBL:X16936; NID:g13204; PIDN:CAA34810.1; !1PID:g13205 GENETICS !$#gene atp9 !$#genome mitochondrion CLASSIFICATION #superfamily H+-transporting ATP synthase lipid-binding !1protein KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; oxidative phosphorylation; transmembrane !1protein FEATURE !$8-32 #domain transmembrane #status predicted #label TM1\ !$45-74 #domain transmembrane #status predicted #label TM2\ !$57 #active_site Glu #status predicted SUMMARY #length 77 #molecular-weight 7877 #checksum 131 SEQUENCE /// ENTRY LWET9 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) lipid-binding protein - beet mitochondrion ALTERNATE_NAMES H+-transporting ATP synthase protein 9 ORGANISM #formal_name mitochondrion Beta vulgaris #common_name beet DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 14-Dec-2001 ACCESSIONS S14907; S06697 REFERENCE S14907 !$#authors Xue, Y.; Thomas, C.M.; Davies, D.R. !$#journal Nucleic Acids Res. (1989) 17:8857 !$#title Nucleotide sequence and transcription of the sugar beet !1mitochondrial F0F1-ATPase subunit 9 gene. !$#cross-references MUID:90067852; PMID:2531368 !$#accession S14907 !'##molecule_type DNA !'##residues 1-88 ##label XUE !'##cross-references EMBL:X16593; NID:g12816; PIDN:CAA34604.1; !1PID:g12817 GENETICS !$#gene atp9 !$#genome mitochondrion CLASSIFICATION #superfamily H+-transporting ATP synthase lipid-binding !1protein KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; oxidative phosphorylation; transmembrane !1protein FEATURE !$8-32 #domain transmembrane #status predicted #label TM1\ !$45-74 #domain transmembrane #status predicted #label TM2\ !$57 #active_site Glu #status predicted SUMMARY #length 88 #molecular-weight 9007 #checksum 9680 SEQUENCE /// ENTRY LWVFM #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) lipid-binding protein - fava bean mitochondrion ALTERNATE_NAMES ATP synthase protein 9 ORGANISM #formal_name mitochondrion Vicia faba #common_name fava bean DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 14-Dec-2001 ACCESSIONS S01226 REFERENCE S01221 !$#authors Wahleithner, J.A.; Wolstenholme, D.R. !$#journal Nucleic Acids Res. (1988) 16:6897-6913 !$#title Ribosomal protein S14 genes in broad bean mitochondrial DNA. !$#cross-references MUID:88303319; PMID:3405753 !$#accession S01226 !'##molecule_type DNA !'##residues 1-74 ##label WAH !'##cross-references EMBL:X07236; NID:g13877; PIDN:CAA30224.1; !1PID:g13879 GENETICS !$#gene atp9 !$#genome mitochondrion CLASSIFICATION #superfamily H+-transporting ATP synthase lipid-binding !1protein KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; oxidative phosphorylation; transmembrane !1protein FEATURE !$8-32 #domain transmembrane #status predicted #label TM1\ !$45-74 #domain transmembrane #status predicted #label TM2\ !$57 #active_site Glu #status predicted SUMMARY #length 74 #molecular-weight 7505 #checksum 4774 SEQUENCE /// ENTRY LWWTM #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) lipid-binding protein - wheat mitochondrion ALTERNATE_NAMES H+-transporting ATP synthase protein 9 ORGANISM #formal_name mitochondrion Triticum aestivum #common_name common wheat DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 14-Dec-2001 ACCESSIONS S12631; JQ0989; A38836; S10656; S06737; S06008 REFERENCE S12631 !$#authors Nowak, C.; Kueck, U. !$#journal Nucleic Acids Res. (1990) 18:7164 !$#title RNA editing of the mitochondrial atp9 transcript from wheat. !$#cross-references MUID:91088325; PMID:1702206 !$#accession S12631 !'##molecule_type mRNA !'##residues 1-74 ##label NOW !'##cross-references EMBL:X54621; NID:g13684; PIDN:CAA38441.1; !1PID:g13685 REFERENCE JQ0989 !$#authors Begu, D.; Graves, P.V.; Domec, C.; Arselin, G.; Litvak, S.; !1Araya, A. !$#journal Plant Cell (1990) 2:1283-1290 !$#title RNA editing of wheat mitochondrial ATP synthase subunit 9: !1direct protein and cDNA sequencing. !$#cross-references MUID:93044480; PMID:1726783 !$#accession JQ0989 !'##molecule_type mRNA !'##residues 1-74 ##label BEG !'##cross-references GB:S47364; NID:g259020; PIDN:AAB23976.1; !1PID:g259021 !$#accession A38836 !'##molecule_type protein !'##residues 67-74 ##label BEG2 REFERENCE S10656 !$#authors Graves, P.V.; Begu, D.; Velours, J.; Neau, E.; Belloc, F.; !1Litvak, S.; Araya, A. !$#journal J. Mol. Biol. (1990) 214:1-6 !$#title Direct protein sequencing of wheat mitochondrial ATP !1synthase subunit 9 confirms RNA editing in plants. !$#cross-references MUID:90317813; PMID:2196374 !$#accession S10656 !'##molecule_type protein !'##residues 1-32 ##label GRA REFERENCE S06737 !$#authors Bonhomme, S.; Bird, S.; Bonen, L. !$#journal Plant Mol. Biol. (1989) 13:395-397 !$#title Comparison of the wheat mitochondrial atp9 gene sequence !1with mitochondrial and chloroplast homologues from other !1plants. !$#cross-references MUID:91370821; PMID:2535257 !$#accession S06737 !'##molecule_type DNA !'##residues 1-6,'S',8-27,'L',29-44,'S',46-63,'P',65-70,'S',72-74, !1'RSHKKS' ##label BON !'##cross-references EMBL:X15083; NID:g13686; PIDN:CAA33193.1; !1PID:g13687 REFERENCE S06007 !$#authors Schulte, E.; Staubach, S.; Laser, B.; Kueck, U. !$#journal Nucleic Acids Res. (1989) 17:7531 !$#title Wheat mitochondrial DNA: organization and sequences of the !1atpA and atp9 genes. !$#cross-references MUID:90016824; PMID:2529479 !$#accession S06008 !'##status translation not shown !'##molecule_type DNA !'##residues 1-6,'S',8-27,'L',29-44,'S',46-63,'P',65-70,'S',72-74, !1'RSHKKS' ##label SCH !'##cross-references EMBL:X15919; NID:g13720; PIDN:CAA34061.1; !1PID:g13721 GENETICS !$#gene atp9 !$#genome mitochondrion CLASSIFICATION #superfamily H+-transporting ATP synthase lipid-binding !1protein KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; oxidative phosphorylation; RNA editing; !1transmembrane protein FEATURE !$8-32 #domain transmembrane #status predicted #label TM1\ !$45-74 #domain transmembrane #status predicted #label TM2\ !$57 #active_site Glu #status predicted SUMMARY #length 74 #molecular-weight 7557 #checksum 4606 SEQUENCE /// ENTRY LWPJ9M #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) lipid-binding protein (atp9-1) - garden petunia mitochondrion ALTERNATE_NAMES H+-transporting ATP synthase protein 9 ORGANISM #formal_name mitochondrion Petunia x hybrida #common_name garden petunia DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 14-Dec-2001 ACCESSIONS S14134; A25545 REFERENCE S14134 !$#authors Wintz, H.; Hanson, M.R. !$#journal Curr. Genet. (1991) 19:61-64 !$#title A termination codon is created by RNA editing in the petunia !1mitochondrial atp9 gene transcript. !$#cross-references MUID:91243208; PMID:1709830 !$#accession S14134 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-74 ##label CUR !'##experimental_source line 3704 !'##note 7-Leu, 17-Leu, 28-Phe, 31-Leu, 61-Leu, 64-Leu, 71-Leu and the !1premature stop-codon are due to RNA editing REFERENCE A25545 !$#authors Young, E.G.; Hanson, M.R.; Dierks, P.M. !$#journal Nucleic Acids Res. (1986) 14:7995-8006 !$#title Sequence and transcription analysis of the Petunia !1mitochondrial gene for the ATP synthase proteolipid subunit. !$#cross-references MUID:87040769; PMID:2877439 !$#accession A25545 !'##molecule_type DNA !'##residues 1-6,'S',8-16,'S',18-27,'L',29-30,'S',32-60,'S',62-63,'P', !165-70,'S',72-74,'QVR' ##label YOU !'##cross-references EMBL:X04504; NID:g13323; PIDN:CAA28189.1; !1PID:g13324 GENETICS !$#gene atp9-1 !$#genome mitochondrion CLASSIFICATION #superfamily H+-transporting ATP synthase lipid-binding !1protein KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; oxidative phosphorylation; RNA editing; !1transmembrane protein FEATURE !$8-32 #domain transmembrane #status predicted #label TM1\ !$45-74 #domain transmembrane #status predicted #label TM2\ !$57 #active_site Glu #status predicted SUMMARY #length 74 #molecular-weight 7589 #checksum 4352 SEQUENCE /// ENTRY LWOBM #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) lipid-binding protein - evening primrose mitochondrion ALTERNATE_NAMES H+-transporting ATP synthase protein 9 ORGANISM #formal_name mitochondrion Oenothera villaricae #common_name evening primrose DATE 30-Jun-1992 #sequence_revision 31-Dec-1992 #text_change 14-Dec-2001 ACCESSIONS S11055; S21064; S07802 REFERENCE S11055 !$#authors Schuster, W.; Brennicke, A. !$#journal FEBS Lett. (1990) 268:252-256 !$#title RNA editing of ATPase subunit 9 transcripts in Oenothera !1mitochondria. !$#cross-references MUID:90346152; PMID:1696551 !$#accession S11055 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-74 ##label SCH !$#accession S21064 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-6,'S',8-16,'S',18-63,'P',65-74,'RSVK' ##label SCH1 REFERENCE S07802 !$#authors Schuster, W.; Brennicke, A. !$#journal Curr. Genet. (1989) 15:187-192 !$#title Conserved sequence elements at putative processing sites in !1plant mitochondria. !$#cross-references MUID:89354668; PMID:2766381 !$#accession S07802 !'##molecule_type DNA !'##residues 1-6,'S',8-9,'S',11-63,'P',65-74,'RSVK' ##label SCH2 !'##cross-references EMBL:X15765; NID:g13158; PIDN:CAA33771.1; !1PID:g13159 !'##note this sequence has been revised in reference S11055 GENETICS !$#gene atp9 !$#genome mitochondrion CLASSIFICATION #superfamily H+-transporting ATP synthase lipid-binding !1protein KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; oxidative phosphorylation; RNA editing; !1transmembrane protein FEATURE !$8-32 #domain transmembrane #status predicted #label TM1\ !$45-72 #domain transmembrane #status predicted #label TM2\ !$57 #active_site Glu #status predicted SUMMARY #length 74 #molecular-weight 7589 #checksum 4352 SEQUENCE /// ENTRY LWBYA #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) lipid-binding protein - yeast (Saccharomyces cerevisiae) mitochondrion ALTERNATE_NAMES dicyclohexylcarbodiimide-binding protein; H+-transporting ATP synthase protein 9; H+-transporting ATP synthase proteolipid; protein Q0130 ORGANISM #formal_name mitochondrion Saccharomyces cerevisiae DATE 30-Nov-1980 #sequence_revision 23-Oct-1981 #text_change 19-Apr-2002 ACCESSIONS A23024; S05730; A93830; A01042; S78668; S78669; S05893; !1S07687 REFERENCE A23024 !$#authors Ooi, B.G.; McMullen, G.L.; Linnane, A.W.; Nagley, P.; !1Novitski, C.E. !$#journal Nucleic Acids Res. (1985) 13:1327-1339 !$#title Biogenesis of mitochondria: DNA sequence analysis of mit- !1mutations in the mitochondrial oli1 gene coding for !1mitochondrial ATPase subunit 9 in Saccharomyces cerevisiae. !$#cross-references MUID:85215549; PMID:2860638 !$#accession A23024 !'##molecule_type DNA !'##residues 1-76 ##label OOI !'##cross-references EMBL:V00707 REFERENCE A92252 !$#authors Macino, G.; Tzagoloff, A. !$#journal J. Biol. Chem. (1979) 254:4617-4623 !$#title Assembly of the mitochondrial membrane system. The DNA !1sequence of a mitochondrial ATPase gene in Saccharomyces !1cerevisiae. !$#cross-references MUID:79173209; PMID:155696 !$#accession S05730 !'##molecule_type DNA !'##residues 1-52,'F',54-76 ##label MAC !'##cross-references EMBL:V00707; NID:g13614; PIDN:CAA24079.1; !1PID:g13615 !'##experimental_source oligomycin-resistant mutant !'##note the authors translated the codon CTA for residue 46 according !1to the standard code REFERENCE A93830 !$#authors Hensgens, L.A.M.; Grivell, L.A.; Borst, P.; Bos, J.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1979) 76:1663-1667 !$#title Nucleotide sequence of the mitochondrial structural gene for !1subunit 9 of yeast ATPase complex. !$#cross-references MUID:79201660; PMID:156363 !$#accession A93830 !'##molecule_type DNA !'##residues 1-52,'F',54-76 ##label HEN !'##cross-references EMBL:J01460 !'##experimental_source oligomycin-resistant mutant !'##note the authors translated the codon CTA for residue 46 according !1to the standard code REFERENCE A94415 !$#authors Sebald, W.; Hoppe, J.; Wachter, E. !$#book Function and Molecular Aspects of Biomembrane Transport, !1Quagliariello, E., et al., eds., pp.63-74, Elsevier/ !1North-Holland, Amsterdam, 1979 !$#title Amino acid sequence of the ATPase proteolipid from !1mitochondria, chloroplasts and bacteria (wild type and !1mutants). !$#accession A01042 !'##molecule_type protein !'##residues 1-76 ##label SEB !'##note oligomycin-resistant mutants exhibit the following amino acid !1exchanges: 53-Phe, 57-Val, and 65-Ser; the mutant at !1position 57 shows cross-resistance to venturicidin REFERENCE S78634 !$#authors Foury, F.; Roganti, T.; Lecrenier, N.; Purnelle, B. !$#submission submitted to the Protein Sequence Database, December 1998 !$#accession S78668 !'##molecule_type DNA !'##residues 1-76 ##label FOU1 !'##cross-references EMBL:AJ011856; MIPS:Q0130 !'##experimental_source strain FY1679, isogenic derivative of strain !1S288C REFERENCE Z13743 !$#authors Foury, F.; Roganti, T.; Lecrenier, N.; Purnelle, B. !$#journal FEBS Lett. (1998) 440:325-331 !$#title The complete sequence of the mitochondrial genome of !1Saccharomyces cerevisiae. !$#cross-references MUID:99087401; PMID:9872396 !$#accession S78669 !'##molecule_type DNA !'##residues 1-76 ##label FOU2 !'##cross-references EMBL:AJ011856; NID:g4160362; PIDN:CAA09838.1; !1PID:g4160380 !'##experimental_source strain FY1679, isogenic derivative of strain !1S288C GENETICS !$#gene SGD:OLI1; atp9; oli1; pho2 !'##cross-references SGD:S0007274 !$#genome mitochondrion !$#genetic_code SGC2 CLASSIFICATION #superfamily H+-transporting ATP synthase lipid-binding !1protein KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; transmembrane protein FEATURE !$1-76 #product H+-transporting ATP synthase lipid-binding !8protein #status experimental #label MAT\ !$1-37 #domain transmembrane #status predicted #label TM1\ !$47-76 #domain transmembrane #status predicted #label TM2\ !$1 #modified_site N-formylmethionine #status predicted\ !$59 #active_site Glu #status predicted SUMMARY #length 76 #molecular-weight 7759 #checksum 7655 SEQUENCE /// ENTRY LWNCA #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) lipid-binding protein precursor - Neurospora crassa ORGANISM #formal_name Neurospora crassa DATE 31-Jul-1979 #sequence_revision 31-Dec-1991 #text_change 14-Dec-2001 ACCESSIONS S07173; A38803; A01043 REFERENCE S07173 !$#authors Viebrock, A.; Perz, A.; Sebald, W. !$#journal EMBO J. (1982) 1:565-571 !$#title The imported preprotein of the proteolipid subunit of the !1mitochondrial ATP synthase from Neurospora crassa. Molecular !1cloning and sequencing of the mRNA. !$#cross-references MUID:84236015; PMID:6329691 !$#accession S07173 !'##molecule_type mRNA !'##residues 1-126,'S',128-147 ##label VIE !'##cross-references EMBL:V00864; NID:g2981; PIDN:CAA24230.1; PID:g2982 !$#accession A38803 !'##molecule_type protein !'##residues 2,'XXXX',7-8,'XX',11-12 ##label VIE2 !'##note the sequence is derived from the oligomycin-resistant strain !1AP-12 REFERENCE A94415 !$#authors Sebald, W.; Hoppe, J.; Wachter, E. !$#book Function and Molecular Aspects of Biomembrane Transport, !1Quagliariello, E., et al., eds., pp.63-74, Elsevier/ !1North-Holland, Amsterdam, 1979 !$#title Amino acid sequence of the ATPase proteolipid from !1mitochondria, chloroplasts and bacteria (wild type and !1mutants). !$#accession A01043 !'##molecule_type protein !'##residues 67-147 ##label SEB !'##note in sequence studies of oligomycin-resistant mutants, three !1amino acid substitutions have been identified. Phe-127 is !1replaced by Ser or Tyr and, in another mutant, Phe-136 is !1replaced by Tyr CLASSIFICATION #superfamily H+-transporting ATP synthase lipid-binding !1protein KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; oxidative phosphorylation; transmembrane !1protein FEATURE !$1-66 #domain transit peptide (mitochondrion) #status !8experimental #label TNP\ !$67-147 #product H+-transporting ATP synthase lipid-binding !8protein #status experimental #label MAT\ !$78-103 #domain transmembrane #status predicted #label TM1\ !$121-147 #domain transmembrane #status predicted #label TM2\ !$131 #active_site Glu #status predicted SUMMARY #length 147 #molecular-weight 15408 #checksum 4125 SEQUENCE /// ENTRY LWSPA #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) lipid-binding protein - spinach chloroplast ALTERNATE_NAMES H+-transporting ATP synthase chain c; H+-transporting ATP synthase chain III; H+-transporting ATP synthase proteolipid ORGANISM #formal_name chloroplast Spinacia oleracea #common_name spinach DATE 31-Jul-1979 #sequence_revision 23-Oct-1981 #text_change 14-Dec-2001 ACCESSIONS S14423; S14421; A01044; S00422 REFERENCE S00581 !$#authors Hudson, G.S.; Mason, J.G.; Holton, T.A.; Koller, B.; Cox, !1G.B.; Whitfeld, P.R.; Bottomley, W. !$#journal J. Mol. Biol. (1987) 196:283-298 !$#title A gene cluster in the spinach and pea chloroplast genomes !1encoding one CF-1 and three CF-0 subunits of the H(+)-ATP !1synthase complex and the ribosomal protein S2. !$#cross-references MUID:88011330; PMID:2443718 !$#accession S14423 !'##molecule_type DNA !'##residues 1-81 ##label HUD !'##cross-references EMBL:X05916; NID:g12255; PIDN:CAA29345.1; !1PID:g12258 REFERENCE S00420 !$#authors Hennig, J.; Herrmann, R.G. !$#journal Mol. Gen. Genet. (1986) 203:117-128 !$#title Chloroplast ATP synthase of spinach contains nine !1nonidentical subunit species, six of which are encoded by !1plastid chromosomes in two operons in a phylogenetically !1conserved arrangement. !$#accession S14421 !'##molecule_type DNA !'##residues 1-81 ##label HEN !'##cross-references EMBL:X03775; NID:g12249; PIDN:CAA27402.1; !1PID:g12251 REFERENCE A01044 !$#authors Sebald, W.; Wachter, E. !$#journal FEBS Lett. (1980) 122:307-311 !$#title Amino acid sequence of the proteolipid subunit of the ATP !1synthase from spinach chloroplasts. !$#accession A01044 !'##molecule_type protein !'##residues 1-81 ##label SEB GENETICS !$#gene atpH !$#genome chloroplast CLASSIFICATION #superfamily H+-transporting ATP synthase lipid-binding !1protein KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; thylakoid; transmembrane !1protein FEATURE !$1-81 #product H+-transporting ATP synthase lipid-binding !8protein #status experimental #label MAT\ !$7-33 #domain transmembrane #status predicted #label TM1\ !$51-77 #domain transmembrane #status predicted #label TM2\ !$1 #modified_site N-formylmethionine #status !8experimental\ !$61 #active_site Glu #status predicted SUMMARY #length 81 #molecular-weight 7974 #checksum 5986 SEQUENCE /// ENTRY LWRZA #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) lipid-binding protein - rice chloroplast ALTERNATE_NAMES ATPase chain III ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 14-Dec-2001 ACCESSIONS JQ0218; S05098 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0218 !'##molecule_type DNA !'##residues 1-81 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05098 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-81 ##label HIR !'##cross-references EMBL:X15901; NID:g11957; PIDN:CAA33991.1; !1PID:g11976 !'##experimental_source cv. Nihonbare COMMENT This protein is one of the polypeptide chains of the !1nonenzymatic component (CFO) of ATPase. GENETICS !$#gene atpH !$#map_position CP32039-32284 !$#genome chloroplast CLASSIFICATION #superfamily H+-transporting ATP synthase lipid-binding !1protein KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; thylakoid; transmembrane !1protein FEATURE !$7-33 #domain transmembrane #status predicted #label TM1\ !$51-77 #domain transmembrane #status predicted #label TM2\ !$61 #active_site Glu #status predicted SUMMARY #length 81 #molecular-weight 7974 #checksum 5986 SEQUENCE /// ENTRY LWZMC #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) lipid-binding protein - maize chloroplast ALTERNATE_NAMES H+-transporting ATP synthase chain c; H+-transporting ATP synthase chain III; H+-transporting ATP synthase proteolipid ORGANISM #formal_name chloroplast Zea mays #common_name maize DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 14-Dec-2001 ACCESSIONS S07677; S58547 REFERENCE S06291 !$#authors Rodermel, S.R.; Bogorad, L. !$#journal Genetics (1987) 116:127-139 !$#title Molecular evolution and nucleotide sequences of the maize !1plastid genes for the alpha subunit of CF(1) (atpA) and the !1proteolipid subunit of CF(0) (atpH). !$#cross-references MUID:87248033; PMID:2885245 !$#accession S07677 !'##molecule_type DNA !'##residues 1-81 ##label ROD !'##cross-references EMBL:X05254; NID:g12406; PIDN:CAA28875.1; !1PID:g12407 REFERENCE S58531 !$#authors Maier, R.M.; Neckermann, K.; Igloi, G.L.; Koessel, H. !$#journal J. Mol. Biol. (1995) 251:614-628 !$#title Complete sequence of the maize chloroplast genome: gene !1content, hotspots of divergence and fine tuning of genetic !1information by transcript editing. !$#cross-references MUID:95395841; PMID:7666415 !$#accession S58547 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-81 ##label MAI !'##cross-references EMBL:X86563; NID:g902200; PIDN:CAA60281.1; !1PID:g902217 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1995 GENETICS !$#gene atpH !$#genome chloroplast CLASSIFICATION #superfamily H+-transporting ATP synthase lipid-binding !1protein KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; thylakoid; transmembrane !1protein FEATURE !$7-33 #domain transmembrane #status predicted #label TM1\ !$51-77 #domain transmembrane #status predicted #label TM2\ !$61 #active_site Glu #status predicted SUMMARY #length 81 #molecular-weight 7974 #checksum 5986 SEQUENCE /// ENTRY LWNTA #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) lipid-binding protein - common tobacco chloroplast ALTERNATE_NAMES hydrogen ion-transporting ATP synthase chain III; hydrogen ion-transporting ATP synthase lipid-binding protein ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 14-Dec-2001 ACCESSIONS A01045; T02944 REFERENCE A00149 !$#authors Sugiura, M. !$#submission submitted to the EMBL Data Library, August 1986 !$#accession A01045 !'##molecule_type DNA !'##residues 1-81 ##label SUG !'##cross-references GB:Z00044; GB:S54304; NID:g2924257; !1PIDN:CAA77343.1; PID:g11812 !'##experimental_source cv. Bright Yellow 4 REFERENCE A38013 !$#authors Shinozaki, K.; Ohme, M.; Tanaka, M.; Wakasugi, T.; !1Hayashida, N.; Matsubayashi, T.; Zaita, N.; Chunwongse, J.; !1Obokata, J.; Yamaguchi-Shinozaki, K.; Ohto, C.; Torazawa, !1K.; Meng, B.Y.; Sugita, M.; Deno, H.; Kamogashira, T.; !1Yamada, K.; Kusuda, J.; Takaiwa, F.; Kato, A.; Tohdoh, N.; !1Shimada, H.; Sugiura, M. !$#journal EMBO J. (1986) 5:2043-2049 !$#title The complete nucleotide sequence of the tobacco chloroplast !1genome: its gene organization and expression. !$#contents annotation; gene organization, sites, features !$#note the GenBank Accessions and NID cross-references in PIR !1Accession A01045 above cover the complete chloroplast genome REFERENCE A45834 !$#authors Hayashi, H.; Ooba, T.; Nakayama, S.; Sekimata, M.; Kano, K.; !1Takiguchi, M. !$#journal Immunogenetics (1990) 32:195-199 !$#title Allospecificities between HLA-Bw53 and HLA-B35 are generated !1by substitution of the residues associated with HLA-Bw4/Bw6 !1public epitopes. !$#cross-references MUID:91033941; PMID:1699887 !$#accession T02944 !'##status preliminary !'##molecule_type DNA !'##residues 1-81 ##label HAY !'##cross-references EMBL:M10124; NID:g343483; PIDN:AAA84678.1; !1PID:g343484 COMMENT This protein is one of the polypeptide chains of the !1nonenzymatic component (CF0) of ATPase. GENETICS !$#gene atpH !$#genome chloroplast CLASSIFICATION #superfamily H+-transporting ATP synthase lipid-binding !1protein KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; thylakoid; transmembrane !1protein FEATURE !$7-33 #domain transmembrane #status predicted #label TM1\ !$51-77 #domain transmembrane #status predicted #label TM2\ !$61 #active_site Glu #status predicted SUMMARY #length 81 #molecular-weight 7990 #checksum 6094 SEQUENCE /// ENTRY LWLVA #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) lipid-binding protein - liverwort (Marchantia polymorpha) chloroplast ALTERNATE_NAMES hydrogen ion-transporting ATP synthase chain III; hydrogen ion-transporting ATP synthase lipid-binding protein ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 14-Dec-2001 ACCESSIONS A01046; S01578 REFERENCE A00150 !$#authors Ohyama, K. !$#submission submitted to the EMBL Data Library, October 1986 !$#accession A01046 !'##molecule_type DNA !'##residues 1-81 ##label OHY REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features REFERENCE S01567 !$#authors Umesono, K.; Inokuchi, H.; Shiki, Y.; Takeuchi, M.; Chang, !1Z.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Ohyama, K.; Ozeki, !1H. !$#journal J. Mol. Biol. (1988) 203:299-331 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. II. Gene organization of the large !1single copy region from rps'12 to atpB. !$#cross-references MUID:89068686; PMID:2974085 !$#accession S01578 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-81 ##label UME !'##cross-references GB:X04465; GB:Y00686; NID:g11640; PIDN:CAA28066.1; !1PID:g11653 COMMENT This protein is one of the polypeptide chains of the !1nonenzymatic component (CF0) of ATPase. GENETICS !$#gene atpH !$#genome chloroplast CLASSIFICATION #superfamily H+-transporting ATP synthase lipid-binding !1protein KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; thylakoid; transmembrane !1protein FEATURE !$7-33 #domain transmembrane #status predicted #label TM1\ !$51-77 #domain transmembrane #status predicted #label TM2\ !$61 #active_site Glu #status predicted SUMMARY #length 81 #molecular-weight 8004 #checksum 5756 SEQUENCE /// ENTRY LWPMA #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) lipid-binding protein - garden pea chloroplast ALTERNATE_NAMES H+-transporting ATP synthase chain III ORGANISM #formal_name chloroplast Pisum sativum #common_name garden pea DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 14-Dec-2001 ACCESSIONS S14424; B24621; JQ0746 REFERENCE S00581 !$#authors Hudson, G.S.; Mason, J.G.; Holton, T.A.; Koller, B.; Cox, !1G.B.; Whitfeld, P.R.; Bottomley, W. !$#journal J. Mol. Biol. (1987) 196:283-298 !$#title A gene cluster in the spinach and pea chloroplast genomes !1encoding one CF-1 and three CF-0 subunits of the H(+)-ATP !1synthase complex and the ribosomal protein S2. !$#cross-references MUID:88011330; PMID:2443718 !$#accession S14424 !'##molecule_type DNA !'##residues 1-81 ##label HUD !'##cross-references EMBL:X05917; NID:g12139; PIDN:CAA29350.1; !1PID:g311714 REFERENCE A91049 !$#authors Cozens, A.L.; Walker, J.E.; Phillips, A.L.; Huttly, A.K.; !1Gray, J.C. !$#journal EMBO J. (1986) 5:217-222 !$#title A sixth subunit of ATP synthase, an F(0) component, is !1encoded in the pea chloroplast genome. !$#accession B24621 !'##molecule_type DNA !'##residues 1-32 ##label COZ REFERENCE JQ0746 !$#authors Huttly, A.K.; Plant, A.L.; Phillips, A.L.; Auffret, A.D.; !1Gray, J.C. !$#journal Gene (1990) 90:227-233 !$#title Nucleotide sequence and transcripts of the pea chloroplast !1gene encoding CF0 subunit III of ATP synthase. !$#cross-references MUID:90382670; PMID:2129529 !$#accession JQ0746 !'##molecule_type DNA !'##residues 1-81 ##label HUT !'##cross-references GB:M57711; NID:g343017; PIDN:AAA84541.1; !1PID:g552815 !'##note residues 1-21 were confirmed by peptide sequencing GENETICS !$#gene atpH !$#genome chloroplast CLASSIFICATION #superfamily H+-transporting ATP synthase lipid-binding !1protein KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; thylakoid; transmembrane !1protein FEATURE !$7-33 #domain transmembrane #status predicted #label TM1\ !$51-77 #domain transmembrane #status predicted #label TM2\ !$61 #active_site Glu #status predicted SUMMARY #length 81 #molecular-weight 8032 #checksum 5845 SEQUENCE /// ENTRY LWYCA #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) lipid-binding protein - Synechococcus sp. (strain PCC 6301) ALTERNATE_NAMES H+-transporting ATP synthase chain c ORGANISM #formal_name Synechococcus sp. DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 14-Dec-2001 ACCESSIONS S10827 REFERENCE S07286 !$#authors Cozens, A.L.; Walker, J.E. !$#journal J. Mol. Biol. (1987) 194:359-383 !$#title The organization and sequence of the genes for ATP synthase !1subunits in the cyanobacterium Synechococcus 6301. Support !1for an endosymbiotic origin of chloroplasts. !$#cross-references MUID:87311713; PMID:3041005 !$#accession S10827 !'##molecule_type DNA !'##residues 1-81 ##label COZ !'##cross-references EMBL:X05302; NID:g48009; PIDN:CAA28924.1; !1PID:g48013 CLASSIFICATION #superfamily H+-transporting ATP synthase lipid-binding !1protein KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1transmembrane protein FEATURE !$7-33 #domain transmembrane #status predicted #label TM1\ !$51-77 #domain transmembrane #status predicted #label TM2\ !$61 #active_site Glu #status predicted SUMMARY #length 81 #molecular-weight 7967 #checksum 5173 SEQUENCE /// ENTRY PWYBLB #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) lipid-binding protein - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES ATP synthase chain d; H+-transporting ATP synthase chain c ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 14-Dec-2001 ACCESSIONS S17747; S74587; S14862 REFERENCE S17745 !$#authors Lill, H.; Nelson, N. !$#journal Plant Mol. Biol. (1991) 17:641-652 !$#title The atp1 and atp2 operons of the cyanobacterium !1Synechocystis sp. PCC 6803. !$#cross-references MUID:92003679; PMID:1832989 !$#accession S17747 !'##molecule_type DNA !'##residues 1-81 ##label LIL !'##cross-references EMBL:X58128; NID:g47506; PIDN:CAA41131.1; !1PID:g47509 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74587 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-81 ##label KAN !'##cross-references EMBL:D90900; GB:AB001339; NID:g1651768; !1PIDN:BAA16739.1; PID:g1651812 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene atpH CLASSIFICATION #superfamily H+-transporting ATP synthase lipid-binding !1protein KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1transmembrane protein FEATURE !$6-27 #domain transmembrane #status predicted #label TM1\ !$63-81 #domain transmembrane #status predicted #label TM2\ !$61 #active_site Glu #status predicted SUMMARY #length 81 #molecular-weight 7968 #checksum 6115 SEQUENCE /// ENTRY LWEGC #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) lipid-binding protein - Euglena gracilis chloroplast ALTERNATE_NAMES ATP synthase CF0 chain III ORGANISM #formal_name chloroplast Euglena gracilis #variety strain Pringsheim Z DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 14-Dec-2001 ACCESSIONS S34901; S29799; S26091; S34534 REFERENCE S34862 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.R.; !1Monfort, A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#journal Nucleic Acids Res. (1993) 21:3537-3544 !$#title Complete sequence of Euglena gracilis chloroplast DNA. !$#cross-references MUID:93347989; PMID:8346031 !$#accession S34901 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-81 ##label HAL !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50113.1; !1PID:g415769 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1993 REFERENCE S29797 !$#authors Drager, R.G.; Hallick, R.B. !$#journal Curr. Genet. (1993) 23:271-280 !$#title A novel Euglena gracilis chloroplast operon encoding four !1ATP synthase subunits and two ribosomal proteins contains 17 !1introns. !$#cross-references MUID:93169691; PMID:8435857 !$#accession S29799 !'##molecule_type DNA !'##residues 1-81 ##label DRA !'##cross-references EMBL:Z11874; NID:g14353; PIDN:CAA77930.1; !1PID:g14380 GENETICS !$#gene atpH !$#genome chloroplast CLASSIFICATION #superfamily H+-transporting ATP synthase lipid-binding !1protein KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; thylakoid; transmembrane !1protein FEATURE !$7-33 #domain transmembrane #status predicted #label TM1\ !$51-77 #domain transmembrane #status predicted #label TM2\ !$61 #active_site Glu #status predicted SUMMARY #length 81 #molecular-weight 8020 #checksum 5157 SEQUENCE /// ENTRY PWQFL #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) lipid-binding protein - Euglena gracilis chloroplast (strain Z) ALTERNATE_NAMES ATP synthase chain III ORGANISM #formal_name chloroplast Euglena gracilis DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 14-Dec-2001 ACCESSIONS S07400 REFERENCE S07400 !$#authors Passavant, C.W.; Hallick, R.B. !$#journal Plant Mol. Biol. (1985) 4:347-354 !$#title Location, nucleotide sequence and expression of the !1proton-translocating subunit gene of the E. gracilis !1chloroplast ATP synthase. !$#accession S07400 !'##molecule_type DNA !'##residues 1-77 ##label PAS !'##cross-references EMBL:M16844; NID:g336867; PIDN:AAA84220.1; !1PID:g336868 GENETICS !$#gene atpH !$#genome chloroplast CLASSIFICATION #superfamily H+-transporting ATP synthase lipid-binding !1protein KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; thylakoid; transmembrane !1protein FEATURE !$7-29 #domain transmembrane #status predicted #label TM1\ !$47-73 #domain transmembrane #status predicted #label TM2\ !$57 #active_site Glu #status predicted SUMMARY #length 77 #molecular-weight 8140 #checksum 8915 SEQUENCE /// ENTRY LWECA #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) lipid-binding protein - Escherichia coli (strain K-12) ALTERNATE_NAMES DCCD-binding protein; hydrogen ion-transporting ATPase chain c ORGANISM #formal_name Escherichia coli DATE 31-Jul-1979 #sequence_revision 02-Apr-1982 #text_change 01-Mar-2002 ACCESSIONS B93732; A90098; A94415; A91279; A90320; I41272; I52349; !1B65177; T45003; A01047 REFERENCE A93732 !$#authors Gay, N.J.; Walker, J.E. !$#journal Nucleic Acids Res. (1981) 9:3919-3926 !$#title The atp operon: nucleotide sequence of the promoter and the !1genes for the membrane proteins, and the delta subunit of !1Escherichia coli ATP-synthase. !$#cross-references MUID:82059437; PMID:6272190 !$#accession B93732 !'##molecule_type DNA !'##residues 1-79 ##label GAY !'##cross-references GB:V00264; GB:X00771; NID:g41023; PIDN:CAA23515.1; !1PID:g41026 REFERENCE A90098 !$#authors Kanazawa, H.; Mabuchi, K.; Kayano, T.; Tamura, F.; Futai, M. !$#journal Biochem. Biophys. Res. Commun. (1981) 100:219-225 !$#title Nucleotide sequence of genes coding for !1dicyclohexylcarbodiimide-binding protein and the alpha !1subunit of proton-translocating ATPase of Escherichia coli. !$#cross-references MUID:81255758; PMID:6266400 !$#accession A90098 !'##molecule_type DNA !'##residues 1-36,'Q',38-79 ##label KAN REFERENCE A94415 !$#authors Sebald, W.; Hoppe, J.; Wachter, E. !$#book Function and Molecular Aspects of Biomembrane Transport, !1Quagliariello, E., et al., eds., pp.63-74, Elsevier/ !1North-Holland, Amsterdam, 1979 !$#title Amino acid sequence of the ATPase proteolipid from !1mitochondria, chloroplasts and bacteria (wild type and !1mutants). !$#accession A94415 !'##molecule_type protein !'##residues 1-79 ##label SEB REFERENCE A91279 !$#authors Wachter, E.; Schmid, R.; Deckers, G.; Altendorf, K. !$#journal FEBS Lett. (1980) 113:265-270 !$#title Amino acid replacement in dicyclohexylcarbodiimide-reactive !1proteins from mutant strains of Escherichia coli defective !1in the energy-transducing ATPase complex. !$#cross-references MUID:80225057; PMID:6446460 !$#accession A91279 !'##molecule_type protein !'##residues 1-79 ##label WAC !'##experimental_source strain K12, mutants DG 7/1 and DC1 !'##note the mutant DG 7/1 contains an enzymatically active F1 !1component, but no functional F0 component, of the ATPase !1complex; its lipid-binding protein differs from that shown !1in having 61-Gly !'##note the mutant DC1 has a functional F0 as well as F1 part; however, !1the ATPase activity is inhibited; its lipid-binding protein !1differs from that shown in having 28-Val REFERENCE A90320 !$#authors Jans, D.A.; Fimmel, A.L.; Langman, L.; James, L.B.; Downie, !1J.A.; Senior, A.E.; Ash, G.R.; Gibson, F.; Cox, G.B. !$#journal Biochem. J. (1983) 211:717-726 !$#title Mutations in the uncE gene affecting assembly of the c- !1subunit of the adenosine triphosphatase of Escherichia coli. !$#cross-references MUID:83282613; PMID:6309138 !$#accession A90320 !'##molecule_type DNA !'##residues 1-79 ##label JAN !'##experimental_source mutants uncE429, uncE408, and uncE463 !'##note the uncE429 sequence differs from that shown in having 23-Asp; !1the uncE408 and unc463 sequences differ from that shown in !1having 31-Phe. All three mutant proteins are unable to !1assemble in the membrane REFERENCE I41271 !$#authors Kanazawa, H.; Futai, M. !$#journal Ann. N. Y. Acad. Sci. (1982) 402:45-64 !$#title Structure and function of H+-ATPase: What we have learned !1from Escherichia coli H+-ATPase. !$#cross-references MUID:83176724; PMID:6301339 !$#accession I41272 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-79 ##label RES !'##cross-references GB:M25464; NID:g146318; PIDN:AAA83870.1; !1PID:g146320 REFERENCE I52349 !$#authors Fimmel, A.L.; Jans, D.A.; Langman, L.; James, L.B.; Ash, !1G.R.; Downie, J.A.; Senior, A.E.; Gibson, F.; Cox, G.B. !$#journal Biochem. J. (1983) 213:451-458 !$#title The F1F0-ATPase of Escherichia coli. Substitution of proline !1by leucine at position 64 in the c-subunit causes loss of !1oxidative phosphorylation. !$#cross-references MUID:83308564; PMID:6193778 !$#accession I52349 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-79 ##label RE2 !'##cross-references EMBL:V01506; NID:g43269; PIDN:CAA24752.1; !1PID:g43270 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65177 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-79 ##label BLAT !'##cross-references GB:AE000450; GB:U00096; NID:g1790166; !1PIDN:AAC76760.1; PID:g1790175; UWGP:b3737 !'##experimental_source strain K-12, substrain MG1655 REFERENCE Z22893 !$#authors Nielsen, J.; Hansen, F.G.; Hoppe, J.; Friedl, P.; Von !1Meyenburg, K. !$#journal Mol. Gen. Genet. (1981) 184:33-39 !$#title The nucleotide sequence of the atp genes coding for the F-0 !1subunits a, b, c and the F-1 subunit delta of the membrane !1bound ATP synthase of Escherichia coli. !$#cross-references MUID:82147764; PMID:6278247 !$#accession T45003 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-79 ##label NIE !'##cross-references EMBL:V00266; NID:g41031; PIDN:CAA23522.1; !1PID:g41032 GENETICS !$#gene atpE; uncE !$#map_position 84 min COMPLEX it is one of the three chains of the nonenzymatic membrane !1component (F0) of the ATPase comple CLASSIFICATION #superfamily H+-transporting ATP synthase lipid-binding !1protein KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1transmembrane protein FEATURE !$7-33 #domain transmembrane #status predicted #label TM1\ !$51-77 #domain transmembrane #status predicted #label TM2\ !$1 #modified_site N-formylmethionine #status !8experimental\ !$61 #active_site Asp #status predicted SUMMARY #length 79 #molecular-weight 8256 #checksum 1957 SEQUENCE /// ENTRY LWHWA3 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) lipid-binding protein - thermophilic bacterium PS-3 ALTERNATE_NAMES H+-transporting ATP synthase chain c; hydrogen ion-transporting ATPase lipid-binding protein ORGANISM #formal_name thermophilic bacterium PS-3 DATE 31-Jul-1979 #sequence_revision 23-Oct-1981 #text_change 14-Dec-2001 ACCESSIONS S02255; A01048 REFERENCE S01397 !$#authors Ohta, S.; Yohda, M.; Ishizuka, M.; Hirata, H.; Hamamoto, T.; !1Otawara-Hamamoto, Y.; Matsuda, K.; Kagawa, Y. !$#journal Biochim. Biophys. Acta (1988) 933:141-155 !$#title Sequence and over-expression of subunits of adenosine !1triphosphate synthase in thermophilic bacterium PS3. !$#cross-references MUID:88163679; PMID:2894854 !$#accession S02255 !'##molecule_type DNA !'##residues 1-72 ##label OHT !'##cross-references EMBL:X07804; NID:g45808; PIDN:CAA30649.1; !1PID:g45811 !'##note this sequence was confirmed by protein sequencing REFERENCE A01048 !$#authors Hoppe, J.; Sebald, W. !$#journal Eur. J. Biochem. (1980) 107:57-65 !$#title Amino acid sequence of the proteolipid subunit of the !1proton-translocating ATPase complex from the thermophilic !1bacterium PS-3. !$#cross-references MUID:80245993; PMID:6447066 !$#accession A01048 !'##molecule_type protein !'##residues 1-72 ##label HOP COMMENT This protein is a nonenzymatic component of ATPase. CLASSIFICATION #superfamily H+-transporting ATP synthase lipid-binding !1protein KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1transmembrane protein FEATURE !$1-72 #product H+-transporting ATP synthase lipid-binding !8protein #status experimental #label MAT\ !$2-28 #domain transmembrane #status predicted #label TM1\ !$46-72 #domain transmembrane #status predicted #label TM2\ !$1 #modified_site N-formylmethionine #status !8experimental\ !$56 #active_site Glu #status predicted SUMMARY #length 72 #molecular-weight 7334 #checksum 4469 SEQUENCE /// ENTRY JN0362 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) lipid-binding protein - Enterococcus faecalis ORGANISM #formal_name Enterococcus faecalis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 14-Dec-2001 ACCESSIONS JN0362 REFERENCE JN0362 !$#authors Kocherginskaya, S.A.; Shakhparonov, M.I.; Aldanova, N.A.; !1Modyanov, N.N.; Ovchinnikov, Y.A. !$#journal Bioorg. Khim. (1982) 8:1569-1571 !$#title Proton-translocating adenosinetriphosphatase from !1Streptococcus faecalis. Structure of the !1dicyclohexylcarbodiimide-binding subunit. !$#accession JN0362 !'##molecule_type protein !'##residues 1-71 ##label KOC CLASSIFICATION #superfamily H+-transporting ATP synthase lipid-binding !1protein KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1transmembrane protein FEATURE !$1-26 #domain transmembrane #status predicted #label TM1\ !$44-70 #domain transmembrane #status predicted #label TM2\ !$1 #modified_site N-formylmethionine #status !8experimental\ !$54 #active_site Glu #status predicted SUMMARY #length 71 #molecular-weight 7264 #checksum 3680 SEQUENCE /// ENTRY S17721 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) lipid-binding protein - Bacillus firmus ALTERNATE_NAMES H+-transporting ATP synthase chain c ORGANISM #formal_name Bacillus firmus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 14-Dec-2001 ACCESSIONS S17721 REFERENCE S17719 !$#authors Ivey, D.M.; Krulwich, T.A. !$#journal Mol. Gen. Genet. (1991) 229:292-300 !$#title Organization and nucleotide sequence of the atp genes !1encoding the ATP synthase from alkaliphilic Bacillus firmus !1OF4. !$#cross-references MUID:92017665; PMID:1833620 !$#accession S17721 !'##molecule_type DNA !'##residues 1-69 ##label IVE !'##cross-references EMBL:M60117; NID:g2988387; PIDN:AAC08039.1; !1PID:g142546 GENETICS !$#gene atpE CLASSIFICATION #superfamily H+-transporting ATP synthase lipid-binding !1protein KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1transmembrane protein FEATURE !$1-26 #domain transmembrane #status predicted #label TM1\ !$54 #active_site Glu #status predicted SUMMARY #length 69 #molecular-weight 6956 #checksum 643 SEQUENCE /// ENTRY C31482 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) lipid-binding protein - Bacillus megaterium ALTERNATE_NAMES H+-transporting ATP synthase chain c ORGANISM #formal_name Bacillus megaterium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 14-Dec-2001 ACCESSIONS C31482 REFERENCE A31482 !$#authors Brusilow, W.S.A.; Scarpetta, M.A.; Hawthorne, C.A.; Clark, !1W.P. !$#journal J. Biol. Chem. (1989) 264:1528-1533 !$#title Organization and sequence of the genes coding for the !1proton-translocating ATPase of Bacillus megaterium. !$#cross-references MUID:89109162; PMID:2521483 !$#accession C31482 !'##status preliminary !'##molecule_type DNA !'##residues 1-70 ##label BRU !'##cross-references GB:M20255; GB:J04455; GB:M18352; GB:M23924; !1NID:g142553; PIDN:AAA82521.1; PID:g142556 CLASSIFICATION #superfamily H+-transporting ATP synthase lipid-binding !1protein KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1transmembrane protein FEATURE !$1-26 #domain transmembrane #status predicted #label TM1\ !$44-70 #domain transmembrane #status predicted #label TM2\ !$54 #active_site Glu #status predicted SUMMARY #length 70 #molecular-weight 6951 #checksum 1958 SEQUENCE /// ENTRY I40363 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) chain c (atpE) - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 14-Dec-2001 ACCESSIONS I40363; A69592; S39251 REFERENCE I40360 !$#authors Santana, M.; Ionescu, M.S.; Vertes, A.; Longin, R.; Kunst, !1F.; Danchin, A.; Glaser, P. !$#journal J. Bacteriol. (1994) 176:6802-6811 !$#title Bacillus subtilis F0F1 ATPase: DNA sequence of the atp !1operon and characterization of atp mutants. !$#cross-references MUID:95050246; PMID:7961438 !$#accession I40363 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-70 ##label RES !'##cross-references EMBL:Z28592; NID:g433983; PIDN:CAA82255.1; !1PID:g433986 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69592 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-70 ##label KUN !'##cross-references GB:Z99122; GB:AL009126; NID:g2636029; !1PIDN:CAB15703.1; PID:g2636211 !'##experimental_source strain 168 GENETICS !$#gene atpE CLASSIFICATION #superfamily H+-transporting ATP synthase lipid-binding !1protein KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1transmembrane protein FEATURE !$1-26 #domain transmembrane #status predicted #label TM1\ !$44-70 #domain transmembrane #status predicted #label TM2\ !$54 #active_site Glu #status predicted SUMMARY #length 70 #molecular-weight 7093 #checksum 9699 SEQUENCE /// ENTRY PWHU6 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) protein 6 - human mitochondrion ALTERNATE_NAMES hydrogen ion-transporting ATP synthase protein 6 ORGANISM #formal_name mitochondrion Homo sapiens #common_name man DATE 22-May-1981 #sequence_revision 23-Oct-1981 #text_change 14-Dec-2001 ACCESSIONS A01049 REFERENCE A00151 !$#authors Anderson, S.; Bankier, A.T.; Barrell, B.G.; de Bruijn, !1M.H.L.; Coulson, A.R.; Drouin, J.; Eperon, I.C.; Nierlich, !1D.P.; Roe, B.A.; Sanger, F.; Schreier, P.H.; Smith, A.J.H.; !1Staden, R.; Young, I.G. !$#journal Nature (1981) 290:457-465 !$#title Sequence and organization of the human mitochondrial genome. !$#cross-references MUID:81173052; PMID:7219534 !$#accession A01049 !'##molecule_type DNA !'##residues 1-226 ##label AND !'##cross-references GB:J01415; GB:M12548; GB:M58503; GB:M63932; !1GB:M63933; NID:g1944628; PIDN:AAB58948.1; PID:g2052364; !1EMBL:V00662; NID:g13003; PID:g13009; GSPDB:GN00100 GENETICS !$#gene GDB:MTATP6 !'##cross-references GDB:118897; OMIM:516060 !$#map_position MTH8527-9207 !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily H+-transporting ATP synthase protein 6 KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; oxidative phosphorylation; transmembrane !1protein SUMMARY #length 226 #molecular-weight 24817 #checksum 296 SEQUENCE /// ENTRY PWBO6 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) protein 6 - bovine mitochondrion ALTERNATE_NAMES hydrogen ion-transporting ATP synthase protein 6 ORGANISM #formal_name mitochondrion Bos primigenius taurus #common_name cattle DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 14-Dec-2001 ACCESSIONS A01050 REFERENCE A00152 !$#authors Anderson, S.; de Bruijn, M.H.L.; Coulson, A.R.; Eperon, !1I.C.; Sanger, F.; Young, I.G. !$#journal J. Mol. Biol. (1982) 156:683-717 !$#title Complete sequence of bovine mitochondrial DNA. Conserved !1features of the mammalian mitochondrial genome. !$#cross-references MUID:83010260; PMID:7120390 !$#accession A01050 !'##molecule_type DNA !'##residues 1-226 ##label AND !'##cross-references GB:J01394; NID:g336430; PIDN:AAB59273.1; !1PID:g336436; EMBL:V00654; NID:g12800; PID:g12806 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily H+-transporting ATP synthase protein 6 KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; oxidative phosphorylation; transmembrane !1protein SUMMARY #length 226 #molecular-weight 24788 #checksum 1526 SEQUENCE /// ENTRY PWMS6 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) protein 6 - mouse mitochondrion ALTERNATE_NAMES hydrogen ion-transporting ATP synthase protein 6 ORGANISM #formal_name mitochondrion Mus musculus #common_name house mouse DATE 02-Apr-1982 #sequence_revision 02-Apr-1982 #text_change 14-Dec-2001 ACCESSIONS A01051 REFERENCE A00153 !$#authors Bibb, M.J.; Van Etten, R.A.; Wright, C.T.; Walberg, M.W.; !1Clayton, D.A. !$#journal Cell (1981) 26:167-180 !$#title Sequence and gene organization of mouse mitochondrial DNA. !$#cross-references MUID:82137051; PMID:7332926 !$#accession A01051 !'##molecule_type DNA !'##residues 1-226 ##label BIB !'##cross-references GB:J01420; NID:g342520; PIDN:AAB48649.1; !1PID:g342523; EMBL:V00711; NID:g13838; PID:g13844 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily H+-transporting ATP synthase protein 6 KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; oxidative phosphorylation; transmembrane !1protein SUMMARY #length 226 #molecular-weight 25095 #checksum 8139 SEQUENCE /// ENTRY PWXL6 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) protein 6 - African clawed frog mitochondrion ALTERNATE_NAMES hydrogen ion-transporting ATP synthase protein 6 ORGANISM #formal_name mitochondrion Xenopus laevis #common_name African clawed frog DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 14-Dec-2001 ACCESSIONS A01052 REFERENCE A00155 !$#authors Roe, B.A.; Ma, D.P.; Wilson, R.K.; Wong, J.F.H. !$#journal J. Biol. Chem. (1985) 260:9759-9774 !$#title The complete nucleotide sequence of the Xenopus laevis !1mitochondrial genome. !$#cross-references MUID:85261388; PMID:4019494 !$#accession A01052 !'##molecule_type DNA !'##residues 1-226 ##label ROE !'##cross-references GB:M10217; GB:X01600; GB:X01601; GB:X02890; !1NID:g343717; PIDN:AAA66463.1; PID:g807687 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily H+-transporting ATP synthase protein 6 KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; oxidative phosphorylation; transmembrane !1protein SUMMARY #length 226 #molecular-weight 24943 #checksum 1643 SEQUENCE /// ENTRY PWFF6 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) protein 6 - fruit fly (Drosophila melanogaster) mitochondrion ALTERNATE_NAMES hydrogen ion-transporting ATP synthase protein 6 ORGANISM #formal_name mitochondrion Drosophila melanogaster DATE 18-Apr-1984 #sequence_revision 18-Apr-1984 #text_change 14-Dec-2001 ACCESSIONS A01053 REFERENCE A93307 !$#authors de Bruijn, M.H.L. !$#journal Nature (1983) 304:234-241 !$#title Drosophila melanogaster mitochondrial DNA, a novel !1organization and genetic code. !$#cross-references MUID:83245048; PMID:6408489 !$#accession A01053 !'##molecule_type DNA !'##residues 1-224 ##label DEB !'##cross-references GB:J01404; GB:J01405; GB:J01407; NID:g336811; !1PIDN:AAB59242.1; PID:g472810 GENETICS !$#gene FlyBase:mt:ATPase6 !'##cross-references FlyBase:FBgn0013672 !$#genome mitochondrion !$#genetic_code SGC4 CLASSIFICATION #superfamily H+-transporting ATP synthase protein 6 KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; oxidative phosphorylation; transmembrane !1protein SUMMARY #length 224 #molecular-weight 25227 #checksum 2144 SEQUENCE /// ENTRY PWFF6Y #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) protein 6 - fruit fly (Drosophila yakuba) mitochondrion ALTERNATE_NAMES ATPase protein 6; hydrogen ion-transporting ATP synthase protein 6 ORGANISM #formal_name mitochondrion Drosophila yakuba DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 14-Dec-2001 ACCESSIONS C93477; E25797; A01053 REFERENCE A93477 !$#authors Clary, D.O.; Wolstenholme, D.R. !$#journal Nucleic Acids Res. (1983) 11:4211-4227 !$#title Nucleotide sequence of a segment of Drosophila mitochondrial !1DNA that contains the genes for cytochrome c oxidase !1subunits II and III and ATPase subunit 6. !$#cross-references MUID:83246544; PMID:6306579 !$#accession C93477 !'##molecule_type DNA !'##residues 1-224 ##label CLA !'##cross-references GB:X03240; NID:g12923; PIDN:CAA26989.1; PID:g12928; !1GB:X00924; NID:g12918; PID:g12921 !'##note the authors translated the codon AGA for residues 23, 95, 149, !1216, and 221 as Arg REFERENCE A92962 !$#authors Clary, D.O.; Wolstenholme, D.R. !$#journal J. Mol. Evol. (1985) 22:252-271 !$#title The mitochondrial DNA molecule of Drosophila yakuba: !1nucleotide sequence, gene organization, and genetic code. !$#cross-references MUID:86089137; PMID:3001325 !$#accession E25797 !'##molecule_type DNA !'##residues 1-224 ##label CL2 !'##cross-references GB:X03240; GB:J01400; GB:J01402; GB:J01403; !1GB:J01406; GB:J01408; GB:V01521; GB:X00563; NID:g12923; !1PIDN:CAA26989.1; PID:g12928 GENETICS !$#gene FlyBase:Dyak/mt:ATPase6 !'##cross-references FlyBase:FBgn0013177 !$#genome mitochondrion !$#genetic_code SGC4 CLASSIFICATION #superfamily H+-transporting ATP synthase protein 6 KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; oxidative phosphorylation; transmembrane !1protein SUMMARY #length 224 #molecular-weight 25141 #checksum 2953 SEQUENCE /// ENTRY PWWT6 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) protein 6 precursor - wheat mitochondrion ORGANISM #formal_name mitochondrion Triticum aestivum #common_name common wheat DATE 31-Mar-1992 #sequence_revision 30-Jun-1992 #text_change 14-Dec-2001 ACCESSIONS JA0095; PC2052 REFERENCE JA0095 !$#authors Bonen, L.; Bird, S. !$#journal Gene (1988) 73:47-56 !$#title Sequence analysis of the wheat mitochondrial atp6 gene !1reveals a fused upstream reading frame and markedly !1divergent N termini among plant ATP6 proteins. !$#cross-references MUID:89211959; PMID:2907499 !$#accession JA0095 !'##molecule_type DNA !'##residues 1-386 ##label BON !'##cross-references GB:M24084 !'##note the authors translated the codon CGG for residue 109 as Trp, !1assuming a special genetic code for plant mitochondria !'##note it is uncertain whether Met-1 or Met-114 is the initiator REFERENCE JC2100 !$#authors Mohr, S.; Schulte-Kappert, E.; Odenbach, W.; Oettler, G.; !1Kueck, U. !$#journal Theor. Appl. Genet. (1993) 86:259-268 !$#title Mitochondrial DNA of cytoplasmic male-sterile Triticum !1timopheevi: rearrangement of upstream sequences of the atp6 !1and orf25 genes. !$#accession PC2052 !'##molecule_type DNA !'##residues 1-23 ##label MOH !'##experimental_source seedling, fertile GENETICS !$#gene atp6 !$#genome mitochondrion CLASSIFICATION #superfamily H+-transporting ATP synthase protein 6 KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; oxidative phosphorylation; transmembrane !1protein FEATURE !$1-113 #domain propeptide #status predicted #label PRO\ !$114-386 #product H+-transporting ATP synthase protein 6 !8#status predicted #label MAT SUMMARY #length 386 #molecular-weight 42992 #checksum 1690 SEQUENCE /// ENTRY PWZM6M #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) protein 6 - maize mitochondrion ALTERNATE_NAMES ATPase protein 6; H+-transporting ATP synthase chain a ORGANISM #formal_name mitochondrion Zea mays #common_name maize DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 14-Dec-2001 ACCESSIONS JN0042 REFERENCE JN0042 !$#authors Dewey, R.E.; Levings III, C.S.; Timothy, D.H. !$#journal Plant Physiol. (1985) 79:914-919 !$#title Nucleotide sequence of ATPase subunit 6 gene of maize !1mitochondria. !$#accession JN0042 !'##molecule_type DNA !'##residues 1-291 ##label DEW !'##cross-references EMBL:M16223; NID:g342635; PIDN:AAA70270.1; !1PID:g897620 GENETICS !$#gene atp6 !$#genome mitochondrion CLASSIFICATION #superfamily H+-transporting ATP synthase protein 6 KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; oxidative phosphorylation; transmembrane !1protein SUMMARY #length 291 #molecular-weight 31758 #checksum 273 SEQUENCE /// ENTRY PWNT6M #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) protein 6 - common tobacco mitochondrion ALTERNATE_NAMES H+-transporting ATP synthase chain a ORGANISM #formal_name mitochondrion Nicotiana tabacum #common_name common tobacco DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 14-Dec-2001 ACCESSIONS S00651 REFERENCE S00651 !$#authors Bland, M.M.; Levings III, C.S.; Matzinger, D.F. !$#journal Curr. Genet. (1987) 12:475-481 !$#title The ATPase subunit 6 gene of tobacco mitochondria contains !1an unusual sequence. !$#cross-references MUID:88194695; PMID:2896073 !$#accession S00651 !'##molecule_type DNA !'##residues 1-395 ##label BLA !'##cross-references EMBL:X06595; NID:g13146; PIDN:CAA29816.1; !1PID:g13147 GENETICS !$#gene atp6 !$#genome mitochondrion CLASSIFICATION #superfamily H+-transporting ATP synthase protein 6 KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; oxidative phosphorylation; transmembrane !1protein SUMMARY #length 395 #molecular-weight 43503 #checksum 7703 SEQUENCE /// ENTRY PWAS6N #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) protein 6 - Emericella nidulans mitochondrion ALTERNATE_NAMES hydrogen ion-transporting ATP synthase protein 6 ORGANISM #formal_name mitochondrion Emericella nidulans, Aspergillus nidulans DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 14-Dec-2001 ACCESSIONS C93436; B93428; A01054 REFERENCE A93436 !$#authors Netzker, R.; Kochel, H.G.; Basak, N.; Kuntzel, H. !$#journal Nucleic Acids Res. (1982) 10:4783-4794 !$#title Nucleotide sequence of Aspergillus nidulans mitochondrial !1genes coding for ATPase subunit 6, cytochrome oxidase !1subunit 3, seven unidentified proteins, four tRNAs and !1L-rRNA. !$#cross-references MUID:83038633; PMID:6290989 !$#accession C93436 !'##molecule_type DNA !'##residues 1-256 ##label NET !'##cross-references GB:J01390; NID:g336905; PIDN:AAA99205.1; !1PID:g336906 !'##experimental_source imperfect stage REFERENCE A93428 !$#authors Grisi, E.; Brown, T.A.; Waring, R.B.; Scazzocchio, C.; !1Davies, R.W. !$#journal Nucleic Acids Res. (1982) 10:3531-3539 !$#title Nucleotide sequence of a region of the mitochondrial genome !1of Aspergillus nidulans including the gene for ATPase !1subunit 6. !$#cross-references MUID:82247225; PMID:6285306 !$#accession B93428 !'##molecule_type DNA !'##residues 1-256 ##label GRI !'##cross-references GB:X01507; GB:K01799; NID:g12698; PIDN:CAA25707.1; !1PID:g12700 !'##experimental_source imperfect stage GENETICS !$#genome mitochondrion !$#genetic_code SGC3 CLASSIFICATION #superfamily H+-transporting ATP synthase protein 6 KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; oxidative phosphorylation; transmembrane !1protein SUMMARY #length 256 #molecular-weight 28400 #checksum 2304 SEQUENCE /// ENTRY PWKQ6 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) protein 6 - fungus (Cochliobolus heterostrophus) mitochondrion ORGANISM #formal_name mitochondrion Cochliobolus heterostrophus, Bipolaris maydis DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 14-Dec-2001 ACCESSIONS S06444 REFERENCE S06444 !$#authors Lin, J.J.; Garber, R.C.; Yoder, O.C. !$#journal Nucleic Acids Res. (1988) 16:9875 !$#title Nucleotide sequence of a fungal plasmid-like DNA containing !1the mitochondrial ATPase subunit 6 gene. !$#cross-references MUID:89041590; PMID:2972996 !$#accession S06444 !'##status translation not shown !'##molecule_type DNA !'##residues 1-257 ##label LIN !'##cross-references EMBL:X13439; NID:g12869; PIDN:CAA31791.1; !1PID:g12870 GENETICS !$#genome mitochondrion !$#genetic_code SGC3 CLASSIFICATION #superfamily H+-transporting ATP synthase protein 6 KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; oxidative phosphorylation; transmembrane !1protein SUMMARY #length 257 #molecular-weight 28599 #checksum 2965 SEQUENCE /// ENTRY PWAS6M #type fragment TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) protein 6 - Aspergillus amstelodami mitochondrion (fragment) ALTERNATE_NAMES hydrogen ion-transporting ATP synthase protein 6 ORGANISM #formal_name mitochondrion Aspergillus amstelodami DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 14-Dec-2001 ACCESSIONS A01055 REFERENCE A94634 !$#authors Lazarus, C.M.; Kuntzel, H. !$#submission submitted to the Protein Sequence Database, March 1984 !$#accession A01055 !'##molecule_type DNA !'##residues 1-78 ##label LAZ GENETICS !$#genome mitochondrion !$#genetic_code SGC3 CLASSIFICATION #superfamily H+-transporting ATP synthase protein 6 KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; oxidative phosphorylation; transmembrane !1protein SUMMARY #length 78 #checksum 4936 SEQUENCE /// ENTRY S42271 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) protein 6 - Penicillium chrysogenum mitochondrion ORGANISM #formal_name mitochondrion Penicillium chrysogenum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 14-Dec-2001 ACCESSIONS S42271 REFERENCE S42271 !$#authors Sheen, J.; Kho, Y.H.; Bae, K.S. !$#journal Nucleic Acids Res. (1993) 21:4393 !$#title Genomic sequence of mitochondrial genes coding for ATPase !1subunit 6 and small subunit ribosomal RNA from Penicillium !1chrysogenum: a key for molecular systematics on fungi. !$#cross-references MUID:94021392; PMID:8414999 !$#accession S42271 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-257 ##label SHE !'##cross-references EMBL:Z23072; NID:g397506; PIDN:CAA80613.1; !1PID:g397507 !'##experimental_source KCTC1262 (NRRL 1951.B25) !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1993 GENETICS !$#genome mitochondrion !$#genetic_code SGC3 CLASSIFICATION #superfamily H+-transporting ATP synthase protein 6 KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; oxidative phosphorylation; transmembrane !1protein SUMMARY #length 257 #molecular-weight 28482 #checksum 6460 SEQUENCE /// ENTRY S02157 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) protein 6 - Podospora anserina mitochondrion ORGANISM #formal_name mitochondrion Podospora anserina DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 14-Dec-2001 ACCESSIONS S02157 REFERENCE S02153 !$#authors Cummings, D.J.; Domenico, J.M. !$#journal J. Mol. Biol. (1988) 204:815-839 !$#title Sequence analysis of mitochondrial DNA from Podospora !1anserina. Pervasiveness of a class I intron in three !1separate genes. !$#cross-references MUID:89125610; PMID:2975708 !$#accession S02157 !'##molecule_type DNA !'##residues 1-264 ##label CUM !'##cross-references EMBL:X15602; NID:g13232; PIDN:CAA33625.1; !1PID:g295782 GENETICS !$#genome mitochondrion !$#genetic_code SGC3 !$#introns 196/3 CLASSIFICATION #superfamily H+-transporting ATP synthase protein 6 KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; oxidative phosphorylation; transmembrane !1protein SUMMARY #length 264 #molecular-weight 29317 #checksum 244 SEQUENCE /// ENTRY PWBY3 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) protein 6 - yeast (Saccharomyces cerevisiae) mitochondrion (strain D273-10B/A1) ORGANISM #formal_name mitochondrion Saccharomyces cerevisiae DATE 31-Mar-1981 #sequence_revision 30-Sep-1991 #text_change 19-Apr-2002 ACCESSIONS A01056; JT0464; A38679; S43947 REFERENCE A01056 !$#authors Macino, G.; Tzagoloff, A. !$#journal Cell (1980) 20:507-517 !$#title Assembly of the mitochondrial membrane system: sequence !1analysis of a yeast mitochondrial ATPase gene containing the !1oli-2 and oli-4 loci. !$#cross-references MUID:80222894; PMID:6446405 !$#accession A01056 !'##molecule_type DNA !'##residues 1-259 ##label MAC !'##cross-references GB:V00683 !'##note the authors translated the codon ATA for residue 80 as Ile REFERENCE JT0464 !$#authors Ray, M.K.; Connerton, I.F.; Griffiths, D.E. !$#journal Biochim. Biophys. Acta (1988) 951:213-219 !$#title DNA sequence analysis of the Oli r 2-76 and Oss r 1-92 !1alleles of the Oli-2 region of the yeast Saccharomyces !1cerevisiae. Analysis of related amino-acid substitutions and !1protein-antibiotic interaction. !$#cross-references MUID:89051013; PMID:2973353 !$#accession JT0464 !'##molecule_type DNA !'##residues 1-259 ##label RAY !'##note the authors translated the codons CTT for residues 83 and 245 !1as Leu REFERENCE A38679 !$#authors Nakagawa, K.; Morishima, N.; Shibata, T. !$#journal J. Biol. Chem. (1991) 266:1977-1984 !$#title A maturase-like subunit of the sequence-specific !1endonuclease Endo.SceI from yeast mitochondria. !$#cross-references MUID:91107706; PMID:1988456 !$#accession A38679 !'##molecule_type DNA !'##residues 233-259 ##label NAK !'##cross-references GB:M63839 REFERENCE S43945 !$#authors Novitski, C.E.; Macreadie, I.G.; Maxwell, R.J.; Lukins, !1H.B.; Linnane, A.W.; Nagley, P. !$#journal Curr. Genet. (1984) 8:135-146 !$#title Biogenesis of mitochondria: genetic and molecular analysis !1of the oli2 region of mitochondrial DNA in Saccharomyces !1cerevisiae. !$#accession S43947 !'##molecule_type DNA !'##residues 1-259 ##label NOV !'##cross-references EMBL:M36379 GENETICS !$#gene SGD:ATP6; ATP6; OLI2; OLI4; PHO1 !'##cross-references SGD:S0007268 !$#map_position 61.6-61.9 !$#genome mitochondrion !$#genetic_code SGC2 CLASSIFICATION #superfamily H+-transporting ATP synthase protein 6 KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; transmembrane protein SUMMARY #length 259 #molecular-weight 29151 #checksum 5798 SEQUENCE /// ENTRY PWBYJ6 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) protein 6 - yeast (Saccharomyces cerevisiae) mitochondrion ALTERNATE_NAMES protein Q0085 ORGANISM #formal_name mitochondrion Saccharomyces cerevisiae DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 19-Apr-2002 ACCESSIONS A25869; S78656; S78657; S05747 REFERENCE A25869 !$#authors John, U.P.; Nagley, P. !$#journal Nucleic Acids Res. (1987) 15:366 !$#title Sequence of the mitochondrial oli2 gene coding for subunit 6 !1of the mitochondrial ATPase complex in different strains of !1Saccharomyces. !$#cross-references MUID:87146348; PMID:2950378 !$#accession A25869 !'##molecule_type DNA !'##residues 1-259 ##label JOH !'##cross-references EMBL:X05056; NID:g13574; PIDN:CAA28727.1; !1PID:g13575 !'##experimental_source strain JM6 REFERENCE S78634 !$#authors Foury, F.; Roganti, T.; Lecrenier, N.; Purnelle, B. !$#submission submitted to the Protein Sequence Database, December 1998 !$#accession S78656 !'##molecule_type DNA !'##residues 1-259 ##label FOU1 !'##cross-references EMBL:AJ011856; MIPS:Q0085 !'##experimental_source strain FY1679, isogenic derivative of strain !1S288C REFERENCE Z13743 !$#authors Foury, F.; Roganti, T.; Lecrenier, N.; Purnelle, B. !$#journal FEBS Lett. (1998) 440:325-331 !$#title The complete sequence of the mitochondrial genome of !1Saccharomyces cerevisiae. !$#cross-references MUID:99087401; PMID:9872396 !$#accession S78657 !'##molecule_type DNA !'##residues 1-259 ##label FOU2 !'##cross-references EMBL:AJ011856; NID:g4160362; PIDN:CAA09832.1; !1PID:g4160374 !'##experimental_source strain FY1679, isogenic derivative of strain !1S288C GENETICS !$#gene SGD:ATP6; OLI2; atp6 !'##cross-references SGD:S0007268 !$#genome mitochondrion !$#genetic_code SGC2 CLASSIFICATION #superfamily H+-transporting ATP synthase protein 6 KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; oxidative phosphorylation; transmembrane !1protein SUMMARY #length 259 #molecular-weight 29099 #checksum 5080 SEQUENCE /// ENTRY PWYCA6 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) chain a - Synechococcus sp. (strain PCC 6301) ALTERNATE_NAMES H+-transporting ATP synthase protein 6 ORGANISM #formal_name Synechococcus sp. DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 14-Dec-2001 ACCESSIONS S10826 REFERENCE S07286 !$#authors Cozens, A.L.; Walker, J.E. !$#journal J. Mol. Biol. (1987) 194:359-383 !$#title The organization and sequence of the genes for ATP synthase !1subunits in the cyanobacterium Synechococcus 6301. Support !1for an endosymbiotic origin of chloroplasts. !$#cross-references MUID:87311713; PMID:3041005 !$#accession S10826 !'##molecule_type DNA !'##residues 1-261 ##label COZ !'##cross-references EMBL:X05302; NID:g48009; PIDN:CAA28923.1; !1PID:g48012 CLASSIFICATION #superfamily H+-transporting ATP synthase protein 6 KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1transmembrane protein SUMMARY #length 261 #molecular-weight 28982 #checksum 6401 SEQUENCE /// ENTRY PWYBAA #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) chain a - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES ATP synthase chain a ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 14-Dec-2001 ACCESSIONS S17746; S74588; S14861 REFERENCE S17745 !$#authors Lill, H.; Nelson, N. !$#journal Plant Mol. Biol. (1991) 17:641-652 !$#title The atp1 and atp2 operons of the cyanobacterium !1Synechocystis sp. PCC 6803. !$#cross-references MUID:92003679; PMID:1832989 !$#accession S17746 !'##molecule_type DNA !'##residues 1-276 ##label LIL !'##cross-references EMBL:X58128; NID:g47506; PIDN:CAA41130.1; !1PID:g47508 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74588 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-276 ##label KAN !'##cross-references EMBL:D90900; GB:AB001339; NID:g1651768; !1PIDN:BAA16740.1; PID:g1651813 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene atpI CLASSIFICATION #superfamily H+-transporting ATP synthase protein 6 KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1transmembrane protein FEATURE !$27-44 #domain transmembrane #status predicted #label TM1\ !$63-82 #domain transmembrane #status predicted #label TM2\ !$122-140 #domain transmembrane #status predicted #label TM3\ !$160-179 #domain transmembrane #status predicted #label TM4\ !$225-242 #domain transmembrane #status predicted #label TM5\ !$247-265 #domain transmembrane #status predicted #label TM6 SUMMARY #length 276 #molecular-weight 30698 #checksum 438 SEQUENCE /// ENTRY PWPMA6 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) chain a - garden pea chloroplast ALTERNATE_NAMES ATPase chain a; H+-transporting ATP synthase protein 6 ORGANISM #formal_name chloroplast Pisum sativum #common_name garden pea DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 14-Dec-2001 ACCESSIONS S00586; A24621 REFERENCE S00581 !$#authors Hudson, G.S.; Mason, J.G.; Holton, T.A.; Koller, B.; Cox, !1G.B.; Whitfeld, P.R.; Bottomley, W. !$#journal J. Mol. Biol. (1987) 196:283-298 !$#title A gene cluster in the spinach and pea chloroplast genomes !1encoding one CF-1 and three CF-0 subunits of the H(+)-ATP !1synthase complex and the ribosomal protein S2. !$#cross-references MUID:88011330; PMID:2443718 !$#accession S00586 !'##molecule_type DNA !'##residues 1-247 ##label HUD !'##cross-references EMBL:X05917; NID:g12139; PIDN:CAA29349.1; !1PID:g12140 REFERENCE A91049 !$#authors Cozens, A.L.; Walker, J.E.; Phillips, A.L.; Huttly, A.K.; !1Gray, J.C. !$#journal EMBO J. (1986) 5:217-222 !$#title A sixth subunit of ATP synthase, an F(0) component, is !1encoded in the pea chloroplast genome. !$#accession A24621 !'##molecule_type DNA !'##residues 1-247 ##label COZ !'##cross-references GB:X03575; NID:g12144; PIDN:CAA27255.1; PID:g12145 GENETICS !$#gene atpI !$#genome chloroplast CLASSIFICATION #superfamily H+-transporting ATP synthase protein 6 KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; thylakoid; transmembrane !1protein FEATURE !$19-247 #product H+-transporting ATP synthase chain a #status !8predicted #label MAT\ !$39-58 #domain transmembrane #status predicted #label TM1\ !$97-115 #domain transmembrane #status predicted #label TM2\ !$134-153 #domain transmembrane #status predicted #label TM3\ !$221-240 #domain transmembrane #status predicted #label TM4 SUMMARY #length 247 #molecular-weight 27482 #checksum 3813 SEQUENCE /// ENTRY PWSPA6 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) chain a precursor - spinach chloroplast ALTERNATE_NAMES H+-transporting ATP synthase chain IV; H+-transporting ATP synthase protein 6 ORGANISM #formal_name chloroplast Spinacia oleracea #common_name spinach DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 14-Dec-2001 ACCESSIONS S00582; S00423; S00024 REFERENCE S00581 !$#authors Hudson, G.S.; Mason, J.G.; Holton, T.A.; Koller, B.; Cox, !1G.B.; Whitfeld, P.R.; Bottomley, W. !$#journal J. Mol. Biol. (1987) 196:283-298 !$#title A gene cluster in the spinach and pea chloroplast genomes !1encoding one CF-1 and three CF-0 subunits of the H(+)-ATP !1synthase complex and the ribosomal protein S2. !$#cross-references MUID:88011330; PMID:2443718 !$#accession S00582 !'##molecule_type DNA !'##residues 1-247 ##label HUD !'##cross-references EMBL:X05916; NID:g12255; PIDN:CAA29344.1; !1PID:g12257 REFERENCE S00420 !$#authors Hennig, J.; Herrmann, R.G. !$#journal Mol. Gen. Genet. (1986) 203:117-128 !$#title Chloroplast ATP synthase of spinach contains nine !1nonidentical subunit species, six of which are encoded by !1plastid chromosomes in two operons in a phylogenetically !1conserved arrangement. !$#accession S00423 !'##molecule_type DNA !'##residues 1-36,'DKA',40-143,'A',145-247 ##label HEN !'##cross-references EMBL:X03775; NID:g12249; PIDN:CAA27401.1; !1PID:g12250 !'##note the sequence from Fig. 3 is inconsistent with that from Fig. 2 !1in having 45-Phe, 46-Phe, 197-Glu, 198-Asp, 241-Asp, and !1244-Asp, and in lacking 35-Ile, 79-Ile, 126-Glu, 177-Leu, !1and 222-Phe REFERENCE S00024 !$#authors Fromme, P.; Graeber, P.; Salnikow, J. !$#journal FEBS Lett. (1987) 218:27-30 !$#title Isolation and identification of a fourth subunit in the !1membrane part of the chloroplast ATP-synthase. !$#accession S00024 !'##molecule_type protein !'##residues 'X',20-29,'X',31-34 ##label FRO GENETICS !$#gene atpI !$#genome chloroplast CLASSIFICATION #superfamily H+-transporting ATP synthase protein 6 KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; thylakoid; transmembrane !1protein FEATURE !$1-18 #domain propeptide #status predicted #label PRO\ !$19-247 #product H+-transporting ATP synthase chain a #status !8experimental #label MAT\ !$39-58 #domain transmembrane #status predicted #label TM1\ !$97-115 #domain transmembrane #status predicted #label TM2\ !$134-154 #domain transmembrane #status predicted #label TM3\ !$221-240 #domain transmembrane #status predicted #label TM4 SUMMARY #length 247 #molecular-weight 27087 #checksum 1575 SEQUENCE /// ENTRY LWNT6 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) chain a - common tobacco chloroplast ALTERNATE_NAMES hydrogen ion-transporting ATP synthase protein 6 ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 14-Dec-2001 ACCESSIONS A01057 REFERENCE A00149 !$#authors Sugiura, M. !$#submission submitted to the EMBL Data Library, August 1986 !$#accession A01057 !'##molecule_type DNA !'##residues 1-247 ##label SUG !'##experimental_source cv. Bright Yellow 4 REFERENCE A38013 !$#authors Shinozaki, K.; Ohme, M.; Tanaka, M.; Wakasugi, T.; !1Hayashida, N.; Matsubayashi, T.; Zaita, N.; Chunwongse, J.; !1Obokata, J.; Yamaguchi-Shinozaki, K.; Ohto, C.; Torazawa, !1K.; Meng, B.Y.; Sugita, M.; Deno, H.; Kamogashira, T.; !1Yamada, K.; Kusuda, J.; Takaiwa, F.; Kato, A.; Tohdoh, N.; !1Shimada, H.; Sugiura, M. !$#journal EMBO J. (1986) 5:2043-2049 !$#title The complete nucleotide sequence of the tobacco chloroplast !1genome: its gene organization and expression. !$#contents annotation; gene organization, sites, features COMMENT This is one of the chains of the nonenzymatic membrane !1component (CF0) of the ATPase complex; its sequence is !1homologous with those of ATPase protein 6 from Escherichia !1coli and mitochondria. GENETICS !$#gene atpI !$#genome chloroplast CLASSIFICATION #superfamily H+-transporting ATP synthase protein 6 KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; thylakoid; transmembrane !1protein SUMMARY #length 247 #molecular-weight 27002 #checksum 2928 SEQUENCE /// ENTRY LWRZ6 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) chain a - rice chloroplast ALTERNATE_NAMES ATPase protein 6 ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 14-Dec-2001 ACCESSIONS JQ0217; S05097 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0217 !'##molecule_type DNA !'##residues 1-247 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05097 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-247 ##label HIR !'##cross-references EMBL:X15901; NID:g11957; PIDN:CAA33990.1; !1PID:g11975 !'##experimental_source cv. Nihonbare COMMENT This is one of the chains of the nonenzymatic membrane !1component (CFO) of the ATPase complex; its sequence is !1homologus with those of ATPase protein 6 from Escherichia !1coli and mitochondria. GENETICS !$#gene atpI !$#map_position CP30501-31244 !$#genome chloroplast CLASSIFICATION #superfamily H+-transporting ATP synthase protein 6 KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; thylakoid; transmembrane !1protein SUMMARY #length 247 #molecular-weight 27305 #checksum 2457 SEQUENCE /// ENTRY LWLV6 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) chain a - liverwort (Marchantia polymorpha) chloroplast ALTERNATE_NAMES H+-transporting ATP synthase chain IV; hydrogen ion-transporting ATPase chain a ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 14-Dec-2001 ACCESSIONS A01058; S01577 REFERENCE A00150 !$#authors Ohyama, K. !$#submission submitted to the EMBL Data Library, October 1986 !$#accession A01058 !'##molecule_type DNA !'##residues 1-248 ##label OHY REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features REFERENCE S01567 !$#authors Umesono, K.; Inokuchi, H.; Shiki, Y.; Takeuchi, M.; Chang, !1Z.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Ohyama, K.; Ozeki, !1H. !$#journal J. Mol. Biol. (1988) 203:299-331 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. II. Gene organization of the large !1single copy region from rps'12 to atpB. !$#cross-references MUID:89068686; PMID:2974085 !$#accession S01577 !'##molecule_type DNA !'##residues 1-248 ##label UME !'##cross-references EMBL:X04465; NID:g11640; PIDN:CAA28065.1; !1PID:g11652 COMMENT This is one of the chains of the nonenzymatic membrane !1component (CF0) of the ATPase complex; its sequence is !1homologous with those of ATPase protein 6 from Escherichia !1coli and mitochondria. GENETICS !$#gene atpI !$#genome chloroplast CLASSIFICATION #superfamily H+-transporting ATP synthase protein 6 KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; thylakoid; transmembrane !1protein SUMMARY #length 248 #molecular-weight 27742 #checksum 4337 SEQUENCE /// ENTRY PWEGAC #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) chain a - Euglena gracilis chloroplast ALTERNATE_NAMES ATP synthase CF0 chain IV ORGANISM #formal_name chloroplast Euglena gracilis DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 14-Dec-2001 ACCESSIONS S29798; S34533; S34900; S26090 REFERENCE S29797 !$#authors Drager, R.G.; Hallick, R.B. !$#journal Curr. Genet. (1993) 23:271-280 !$#title A novel Euglena gracilis chloroplast operon encoding four !1ATP synthase subunits and two ribosomal proteins contains 17 !1introns. !$#cross-references MUID:93169691; PMID:8435857 !$#accession S29798 !'##molecule_type DNA !'##residues 1-251 ##label DRA !'##cross-references EMBL:Z11874; NID:g14353; PIDN:CAA77929.1; !1PID:g14379 REFERENCE S34494 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.; Monfort, !1A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#submission submitted to the EMBL Data Library, January 1993 !$#description The complete sequence of the Euglena gracilis chloroplast !1genome (tentative). !$#accession S34533 !'##molecule_type DNA !'##residues 1-251 ##label HAL1 !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50112.1; !1PID:g415768 REFERENCE S34862 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.R.; !1Monfort, A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#journal Nucleic Acids Res. (1993) 21:3537-3544 !$#title Complete sequence of Euglena gracilis chloroplast DNA. !$#cross-references MUID:93347989; PMID:8346031 !$#accession S34900 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-251 ##label HAL2 !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50112.1; !1PID:g415768 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1993 GENETICS !$#gene atpI !$#genome chloroplast !$#introns 9/2; 19/1; 23/3; 138/2; 162/2; 241/3 CLASSIFICATION #superfamily H+-transporting ATP synthase protein 6 KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; thylakoid; transmembrane !1protein SUMMARY #length 251 #molecular-weight 28046 #checksum 62 SEQUENCE /// ENTRY LWEC6 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) protein 6 [similarity] - Escherichia coli (strain K-12) ALTERNATE_NAMES hydrogen ion-transporting ATP synthase chain a ORGANISM #formal_name Escherichia coli DATE 02-Apr-1982 #sequence_revision 02-Apr-1982 #text_change 01-Mar-2002 ACCESSIONS C93732; A90104; B23223; I55244; I55243; I41271; C65177; !1T45001; T45002; A01059 REFERENCE A93732 !$#authors Gay, N.J.; Walker, J.E. !$#journal Nucleic Acids Res. (1981) 9:3919-3926 !$#title The atp operon: nucleotide sequence of the promoter and the !1genes for the membrane proteins, and the delta subunit of !1Escherichia coli ATP-synthase. !$#cross-references MUID:82059437; PMID:6272190 !$#accession C93732 !'##molecule_type DNA !'##residues 1-271 ##label GAY !'##cross-references GB:V00264; GB:X00771; NID:g41023; PIDN:CAA23514.1; !1PID:g41025 REFERENCE A90104 !$#authors Kanazawa, H.; Mabuchi, K.; Kayano, T.; Noumi, T.; Sekiya, !1T.; Futai, M. !$#journal Biochem. Biophys. Res. Commun. (1981) 103:613-620 !$#title Nucleotide sequence of the genes for F-0 components of the !1proton-translocating ATPase from Escherichia coli: !1prediction of the primary structure of F-0 subunits. !$#cross-references MUID:82134799; PMID:6277311 !$#accession A90104 !'##molecule_type DNA !'##residues 1-178,'RCST',183-271 ##label KAN1 !'##cross-references GB:V00310; NID:g42268; PIDN:CAA23590.1; PID:g42270 REFERENCE A23223 !$#authors Kanazawa, H.; Kiyasu, T.; Noumi, T.; Futai, M. !$#journal J. Bacteriol. (1984) 158:300-306 !$#title Overproduction of subunit a of the F0 component of !1proton-translocation ATPase inhibits growth of Escherichia !1coli cells. !$#cross-references MUID:84185438; PMID:6325392 !$#accession B23223 !'##molecule_type DNA !'##residues 1-92 ##label KAN2 REFERENCE I55244 !$#authors Cai, B.D.; Simoni, R.D. !$#journal J. Biol. Chem. (1986) 261:10043-10050 !$#title Impaired proton conductivity resulting from mutations in the !1a subunit of F-1 F-0 ATPase in Escherichia coli. !$#cross-references MUID:86278048; PMID:2874137 !$#accession I55244 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-187,'S',189-271 ##label CAI !'##cross-references GB:M14019; NID:g148142; PIDN:AAA24740.1; !1PID:g148143 REFERENCE I55243 !$#authors Kumamoto, C.A.; Simoni, R.D. !$#journal J. Biol. Chem. (1986) 261:10037-10042 !$#title Genetic evidence for interaction between the a and b !1subunits of the F-O portion of the Escherichia coli proton !1translocating ATPase. !$#cross-references MUID:86278047; PMID:2874136 !$#accession I55243 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 235-271 ##label KUM !'##cross-references GB:M29174; NID:g147366; PIDN:AAA24423.1; !1PID:g147367 REFERENCE I41271 !$#authors Kanazawa, H.; Futai, M. !$#journal Ann. N. Y. Acad. Sci. (1982) 402:45-64 !$#title Structure and function of H+-ATPase: What we have learned !1from Escherichia coli H+-ATPase. !$#cross-references MUID:83176724; PMID:6301339 !$#accession I41271 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-178,'RCST',183-271 ##label KAN3 !'##cross-references GB:M25464; NID:g146318; PIDN:AAA83869.1; !1PID:g146319 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65177 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-271 ##label BLAT !'##cross-references GB:AE000450; GB:U00096; NID:g1790166; !1PIDN:AAC76761.1; PID:g1790176; UWGP:b3738 !'##experimental_source strain K-12, substrain MG1655 REFERENCE Z22893 !$#authors Nielsen, J.; Hansen, F.G.; Hoppe, J.; Friedl, P.; Von !1Meyenburg, K. !$#journal Mol. Gen. Genet. (1981) 184:33-39 !$#title The nucleotide sequence of the atp genes coding for the F-0 !1subunits a, b, c and the F-1 subunit delta of the membrane !1bound ATP synthase of Escherichia coli. !$#cross-references MUID:82147764; PMID:6278247 !$#accession T45001 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-271 ##label NIE1 !'##cross-references EMBL:V00266; NID:g41031; PIDN:CAA23520.1; !1PID:g669111 !$#accession T45002 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 'M',72-271 ##label NIE2 !'##cross-references EMBL:V00266; NID:g41031; PIDN:CAA23521.1; !1PID:g669112 !'##note it is not clear, whether this or an other (longer) reading !1frame really corresponds to atpB but this reading frame !1would provide the molecular weight observed in vivo COMMENT This is one of the three chains of the nonenzymatic membrane !1component (F0) of the ATPase complex. GENETICS !$#gene atpB; uncB !$#map_position 84 min CLASSIFICATION #superfamily H+-transporting ATP synthase protein 6 KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1transmembrane protein SUMMARY #length 271 #molecular-weight 30303 #checksum 6351 SEQUENCE /// ENTRY S06076 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) protein 6 - Vibrio alginolyticus ALTERNATE_NAMES H+-transporting ATP synthase chain a ORGANISM #formal_name Vibrio alginolyticus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 14-Dec-2001 ACCESSIONS S06076 REFERENCE S06075 !$#authors Krumholz, L.R.; Esser, U.; Simoni, R.D. !$#journal Nucleic Acids Res. (1989) 17:7993-7994 !$#title Nucleotide sequence of the unc operon of Vibrio !1alginolyticus. !$#cross-references MUID:90016889; PMID:2529481 !$#accession S06076 !'##status translation not shown !'##molecule_type DNA !'##residues 1-270 ##label KRU !'##cross-references EMBL:X16050; NID:g48331; PIDN:CAA34175.1; !1PID:g48333 GENETICS !$#gene uncB CLASSIFICATION #superfamily H+-transporting ATP synthase protein 6 KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1transmembrane protein SUMMARY #length 270 #molecular-weight 30134 #checksum 9669 SEQUENCE /// ENTRY A64072 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) protein 6 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 14-Dec-2001 ACCESSIONS A64072 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession A64072 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-262 ##label TIGR !'##cross-references GB:U32730; GB:L42023; NID:g3212191; !1PIDN:AAC22143.1; PID:g1573463; TIGR:HI0485 CLASSIFICATION #superfamily H+-transporting ATP synthase protein 6 KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1transmembrane protein SUMMARY #length 262 #molecular-weight 29333 #checksum 5232 SEQUENCE /// ENTRY LWRZ1 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) chain I - rice chloroplast ALTERNATE_NAMES ATPase chain I ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 14-Dec-2001 ACCESSIONS JQ0219; S05099 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0219 !'##molecule_type DNA !'##residues 1-180 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05099 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-180 ##label HIR !'##cross-references EMBL:X15901; NID:g11957; PIDN:CAA33992.1; !1PID:g669080 !'##experimental_source cv. Nihonbare GENETICS !$#gene atpF !$#map_position CP32741-32885,33714-34111 !$#genome chloroplast !$#introns 49/1 CLASSIFICATION #superfamily H+-transporting ATP synthase chain I KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; thylakoid; transmembrane !1protein FEATURE !$26-45 #domain transmembrane #status predicted #label TMM SUMMARY #length 180 #molecular-weight 20554 #checksum 1081 SEQUENCE /// ENTRY PWWT1 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) chain I - wheat chloroplast ALTERNATE_NAMES ATPase chain I; H+-transporting ATP synthase chain b ORGANISM #formal_name chloroplast Triticum aestivum #common_name common wheat DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 14-Dec-2001 ACCESSIONS A22721 REFERENCE A22721 !$#authors Bird, C.R.; Koller, B.; Auffret, A.D.; Huttly, A.K.; Howe, !1C.J.; Dyer, T.A.; Gray, J.C. !$#journal EMBO J. (1985) 4:1381-1388 !$#title The wheat chloroplast gene for CF-0 subunit I of ATP !1synthase contains a large intron. !$#accession A22721 !'##molecule_type DNA !'##residues 1-183 ##label BIR GENETICS !$#gene atpF !$#genome chloroplast !$#introns 49/1 CLASSIFICATION #superfamily H+-transporting ATP synthase chain I KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; thylakoid; transmembrane !1protein FEATURE !$18-183 #product H+-transporting ATP synthase chain I #status !8predicted #label MAT\ !$26-45 #domain transmembrane #status predicted #label TMM SUMMARY #length 183 #molecular-weight 20977 #checksum 3025 SEQUENCE /// ENTRY LWNT1 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) chain I - common tobacco chloroplast ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 14-Dec-2001 ACCESSIONS A01060; S65736; S65735 REFERENCE A00149 !$#authors Sugiura, M. !$#submission submitted to the EMBL Data Library, August 1986 !$#accession A01060 !'##molecule_type DNA !'##residues 1-184 ##label SUG !'##experimental_source cv. Bright Yellow 4 REFERENCE A38013 !$#authors Shinozaki, K.; Ohme, M.; Tanaka, M.; Wakasugi, T.; !1Hayashida, N.; Matsubayashi, T.; Zaita, N.; Chunwongse, J.; !1Obokata, J.; Yamaguchi-Shinozaki, K.; Ohto, C.; Torazawa, !1K.; Meng, B.Y.; Sugita, M.; Deno, H.; Kamogashira, T.; !1Yamada, K.; Kusuda, J.; Takaiwa, F.; Kato, A.; Tohdoh, N.; !1Shimada, H.; Sugiura, M. !$#journal EMBO J. (1986) 5:2043-2049 !$#title The complete nucleotide sequence of the tobacco chloroplast !1genome: its gene organization and expression. !$#contents annotation; gene organization, sites, features REFERENCE S65735 !$#authors Hirose, T.; Fan, H.; Suzuki, J.Y.; Wakasugi, T.; Tsudzuki, !1T.; Koessel, H.; Sugiura, M. !$#journal Plant Mol. Biol. (1996) 30:667-672 !$#title Occurrence of silent RNA editing in chloroplasts: its !1species specificity and the influence of environmental and !1developmental conditions. !$#cross-references MUID:96189279; PMID:8605316 !$#accession S65736 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type mRNA !'##residues 27-30,'L',32-36 ##label HIR !'##note 31-Leu is due to RNA-editing !$#accession S65735 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type DNA !'##residues 27-36 ##label HIW GENETICS !$#gene atpF !$#genome chloroplast !$#introns 49/1 CLASSIFICATION #superfamily H+-transporting ATP synthase chain I KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; thylakoid; transmembrane !1protein FEATURE !$26-45 #domain transmembrane #status predicted #label TMM SUMMARY #length 184 #molecular-weight 20943 #checksum 6350 SEQUENCE /// ENTRY PWSP1 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) chain I - spinach chloroplast ALTERNATE_NAMES H+-transporting ATP synthase chain b ORGANISM #formal_name chloroplast Spinacia oleracea #common_name spinach DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 14-Dec-2001 ACCESSIONS S00583; S00420; S14420 REFERENCE S00581 !$#authors Hudson, G.S.; Mason, J.G.; Holton, T.A.; Koller, B.; Cox, !1G.B.; Whitfeld, P.R.; Bottomley, W. !$#journal J. Mol. Biol. (1987) 196:283-298 !$#title A gene cluster in the spinach and pea chloroplast genomes !1encoding one CF-1 and three CF-0 subunits of the H(+)-ATP !1synthase complex and the ribosomal protein S2. !$#cross-references MUID:88011330; PMID:2443718 !$#accession S00583 !'##molecule_type DNA !'##residues 1-184 ##label HUD !'##cross-references EMBL:X05916; NID:g12255; PIDN:CAA29347.1; !1PID:g853792 REFERENCE S00420 !$#authors Hennig, J.; Herrmann, R.G. !$#journal Mol. Gen. Genet. (1986) 203:117-128 !$#title Chloroplast ATP synthase of spinach contains nine !1nonidentical subunit species, six of which are encoded by !1plastid chromosomes in two operons in a phylogenetically !1conserved arrangement. !$#accession S00420 !'##molecule_type DNA !'##residues 1-184 ##label HEN !'##cross-references EMBL:X03775 !'##note the sequence from Fig. 5 is inconsistent with that from Fig. 2 !1in lacking 84-Arg REFERENCE A22721 !$#authors Bird, C.R.; Koller, B.; Auffret, A.D.; Huttly, A.K.; Howe, !1C.J.; Dyer, T.A.; Gray, J.C. !$#journal EMBO J. (1985) 4:1381-1388 !$#title The wheat chloroplast gene for CF-0 subunit I of ATP !1synthase contains a large intron. !$#accession S14420 !'##molecule_type protein !'##residues 18-22,'X',24-30 ##label BIR GENETICS !$#gene atpF !$#genome chloroplast !$#introns 49/1 CLASSIFICATION #superfamily H+-transporting ATP synthase chain I KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; thylakoid; transmembrane !1protein FEATURE !$18-184 #product H+-transporting ATP synthase chain I #status !8experimental #label MAT\ !$26-45 #domain transmembrane #status predicted #label TMM SUMMARY #length 184 #molecular-weight 20990 #checksum 3661 SEQUENCE /// ENTRY PWPM1 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) chain I - garden pea chloroplast ORGANISM #formal_name chloroplast Pisum sativum #common_name garden pea DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 14-Dec-2001 ACCESSIONS S00587 REFERENCE S00581 !$#authors Hudson, G.S.; Mason, J.G.; Holton, T.A.; Koller, B.; Cox, !1G.B.; Whitfeld, P.R.; Bottomley, W. !$#journal J. Mol. Biol. (1987) 196:283-298 !$#title A gene cluster in the spinach and pea chloroplast genomes !1encoding one CF-1 and three CF-0 subunits of the H(+)-ATP !1synthase complex and the ribosomal protein S2. !$#cross-references MUID:88011330; PMID:2443718 !$#accession S00587 !'##molecule_type DNA !'##residues 1-172 ##label HUD !'##cross-references EMBL:X05917; NID:g12139; PIDN:CAA29351.1; !1PID:g311715 GENETICS !$#gene atpF !$#genome chloroplast !$#introns 38/1 CLASSIFICATION #superfamily H+-transporting ATP synthase chain I KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; thylakoid; transmembrane !1protein FEATURE !$7-172 #product H+-transporting ATP synthase chain I #status !8predicted #label MAT\ !$15-34 #domain transmembrane #status predicted #label TMM SUMMARY #length 172 #molecular-weight 19527 #checksum 6060 SEQUENCE /// ENTRY LWLV1 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) chain I - liverwort (Marchantia polymorpha) chloroplast ALTERNATE_NAMES hydrogen ion-transporting ATP synthase chain I ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 14-Dec-2001 ACCESSIONS A01061; S01579 REFERENCE A00150 !$#authors Ohyama, K. !$#submission submitted to the EMBL Data Library, October 1986 !$#accession A01061 !'##molecule_type DNA !'##residues 1-184 ##label OHY REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features REFERENCE S01567 !$#authors Umesono, K.; Inokuchi, H.; Shiki, Y.; Takeuchi, M.; Chang, !1Z.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Ohyama, K.; Ozeki, !1H. !$#journal J. Mol. Biol. (1988) 203:299-331 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. II. Gene organization of the large !1single copy region from rps'12 to atpB. !$#cross-references MUID:89068686; PMID:2974085 !$#accession S01579 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-184 ##label UME !'##cross-references GB:X04465; GB:Y00686; NID:g11640; PIDN:CAA28067.1; !1PID:g453592 GENETICS !$#gene atpF !$#genome chloroplast !$#introns 49/1 CLASSIFICATION #superfamily H+-transporting ATP synthase chain I KEYWORDS ATP biosynthesis; chloroplast; hydrolase; !1membrane-associated complex; thylakoid; transmembrane !1protein FEATURE !$26-45 #domain transmembrane #status predicted #label TMM SUMMARY #length 184 #molecular-weight 21081 #checksum 4566 SEQUENCE /// ENTRY PWEGI #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) chain I - Euglena gracilis chloroplast ALTERNATE_NAMES ATP synthase CF0 chain I ORGANISM #formal_name chloroplast Euglena gracilis DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 14-Dec-2001 ACCESSIONS S29800; S34535; S34902; S26092 REFERENCE S29797 !$#authors Drager, R.G.; Hallick, R.B. !$#journal Curr. Genet. (1993) 23:271-280 !$#title A novel Euglena gracilis chloroplast operon encoding four !1ATP synthase subunits and two ribosomal proteins contains 17 !1introns. !$#cross-references MUID:93169691; PMID:8435857 !$#accession S29800 !'##molecule_type DNA !'##residues 1-183 ##label DRA !'##cross-references EMBL:Z11874; NID:g14353; PIDN:CAA77931.1; !1PID:g2673885 REFERENCE S34494 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.; Monfort, !1A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#submission submitted to the EMBL Data Library, January 1993 !$#description The complete sequence of the Euglena gracilis chloroplast !1genome (tentative). !$#accession S34535 !'##molecule_type DNA !'##residues 1-183 ##label HAL1 !'##cross-references EMBL:X70810; NID:g415327; PID:g1185110 REFERENCE S34862 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.R.; !1Monfort, A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#journal Nucleic Acids Res. (1993) 21:3537-3544 !$#title Complete sequence of Euglena gracilis chloroplast DNA. !$#cross-references MUID:93347989; PMID:8346031 !$#accession S34902 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-183 ##label HAL2 !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50114.1; !1PID:g2673853 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1993 GENETICS !$#gene atpF !$#genome chloroplast !$#start_codon GTG !$#introns 2/2; 47/1; 101/1 CLASSIFICATION #superfamily H+-transporting ATP synthase chain I KEYWORDS ATP biosynthesis; chloroplast; hydrolase; thylakoid; !1transmembrane protein FEATURE !$24-43 #domain transmembrane #status predicted #label TMM SUMMARY #length 183 #molecular-weight 21127 #checksum 4471 SEQUENCE /// ENTRY S26960 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) chain b - red alga (Antithamnion sp.) chloroplast (strain LB 95.79) ORGANISM #formal_name chloroplast Antithamnion sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 14-Dec-2001 ACCESSIONS S26960 REFERENCE S26957 !$#authors Kostrzewa, M.; Zetsche, K. !$#journal J. Mol. Biol. (1992) 227:961-970 !$#title Large ATP synthase operon of the red alga Antithamnion sp. !1resembles the corresponding operon in cyanobacteria. !$#cross-references MUID:93021132; PMID:1404401 !$#accession S26960 !'##molecule_type DNA !'##residues 1-182 ##label KOS !'##cross-references EMBL:X63382 GENETICS !$#gene atpF !$#genome chloroplast !$#start_codon GTG CLASSIFICATION #superfamily H+-transporting ATP synthase chain I KEYWORDS ATP biosynthesis; chloroplast; hydrolase; membrane protein; !1thylakoid SUMMARY #length 182 #molecular-weight 20470 #checksum 4012 SEQUENCE /// ENTRY LWYC1 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) chain b - Synechococcus sp. (strain PCC 6301) ORGANISM #formal_name Synechococcus sp. DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 14-Dec-2001 ACCESSIONS S10829 REFERENCE S07286 !$#authors Cozens, A.L.; Walker, J.E. !$#journal J. Mol. Biol. (1987) 194:359-383 !$#title The organization and sequence of the genes for ATP synthase !1subunits in the cyanobacterium Synechococcus 6301. Support !1for an endosymbiotic origin of chloroplasts. !$#cross-references MUID:87311713; PMID:3041005 !$#accession S10829 !'##molecule_type DNA !'##residues 1-171 ##label COZ !'##cross-references EMBL:X05302; NID:g48009; PIDN:CAA28926.1; !1PID:g48015 CLASSIFICATION #superfamily H+-transporting ATP synthase chain I KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1transmembrane protein FEATURE !$21-40 #domain transmembrane #status predicted #label TMM SUMMARY #length 171 #molecular-weight 18681 #checksum 9641 SEQUENCE /// ENTRY PWYBBB #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) chain b - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES hypothetical protein sll1324 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 30-Jun-1992 #sequence_revision 23-May-1997 #text_change 14-Dec-2001 ACCESSIONS S74585; S17749; S14864 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74585 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-179 ##label KAN !'##cross-references EMBL:D90900; GB:AB001339; NID:g1651768; !1PIDN:BAA16737.1; PID:g1651810 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 REFERENCE S17745 !$#authors Lill, H.; Nelson, N. !$#journal Plant Mol. Biol. (1991) 17:641-652 !$#title The atp1 and atp2 operons of the cyanobacterium !1Synechocystis sp. PCC 6803. !$#cross-references MUID:92003679; PMID:1832989 !$#accession S17749 !'##molecule_type DNA !'##residues 1-120,'IE',123-179 ##label LIL !'##cross-references EMBL:X58128; NID:g47506; PIDN:CAA41133.1; !1PID:g47511 GENETICS !$#gene atpF CLASSIFICATION #superfamily H+-transporting ATP synthase chain I KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1transmembrane protein FEATURE !$29-46 #domain transmembrane #status predicted #label TMM SUMMARY #length 179 #molecular-weight 19804 #checksum 327 SEQUENCE /// ENTRY S36963 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) chain b - Synechococcus sp. (PCC 6716) ORGANISM #formal_name Synechococcus sp. #variety PCC 6716 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 14-Dec-2001 ACCESSIONS S36963; S31887 REFERENCE S36960 !$#authors van Walraven, H.S.; Lutter, R.; Walker, J.E. !$#journal Biochem. J. (1993) 294:239-251 !$#title Organization and sequences of genes for the subunits of ATP !1synthase in the thermophilic cyanobacterium Synechococcus !16716. !$#cross-references MUID:93371369; PMID:8363578 !$#accession S36963 !'##molecule_type DNA !'##residues 1-176 ##label VAN !'##cross-references EMBL:X70431; NID:g49213; PIDN:CAA49873.1; !1PID:g49217 !'##experimental_source PCC 6716 CLASSIFICATION #superfamily H+-transporting ATP synthase chain I KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex SUMMARY #length 176 #molecular-weight 19260 #checksum 924 SEQUENCE /// ENTRY E31090 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) chain b - Anabaena sp. ORGANISM #formal_name Anabaena sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 14-Dec-2001 ACCESSIONS E31090 REFERENCE A91875 !$#authors McCarn, D.F.; Whitaker, R.A.; Alam, J.; Vrba, J.M.; Curtis, !1S.E. !$#journal J. Bacteriol. (1988) 170:3448-3458 !$#title Genes encoding the alpha, gamma, delta, and four F-0 !1subunits of ATP synthase constitute an operon in the !1cyanobacterium Anabaena sp. strain PCC 7120. !$#cross-references MUID:88298650; PMID:2900236 !$#accession E31090 !'##molecule_type mRNA !'##residues 1-187 ##label MCC !'##cross-references GB:M21659; NID:g141996; PIDN:AAA21989.1; !1PID:g142001 !'##experimental_source PCC 7120 GENETICS !$#gene atpF CLASSIFICATION #superfamily H+-transporting ATP synthase chain I KEYWORDS ATP biosynthesis; hydrogen ion transport; hydrolase SUMMARY #length 187 #molecular-weight 19773 #checksum 8309 SEQUENCE /// ENTRY LWYCBB #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) chain b' - Synechococcus sp. (strain PCC 6301) ORGANISM #formal_name Synechococcus sp. DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 14-Dec-2001 ACCESSIONS S10828 REFERENCE S07286 !$#authors Cozens, A.L.; Walker, J.E. !$#journal J. Mol. Biol. (1987) 194:359-383 !$#title The organization and sequence of the genes for ATP synthase !1subunits in the cyanobacterium Synechococcus 6301. Support !1for an endosymbiotic origin of chloroplasts. !$#cross-references MUID:87311713; PMID:3041005 !$#accession S10828 !'##molecule_type DNA !'##residues 1-158 ##label COZ !'##cross-references EMBL:X05302; NID:g48009; PIDN:CAA28925.1; !1PID:g48014 CLASSIFICATION #superfamily H+-transporting ATP synthase chain I KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1transmembrane protein SUMMARY #length 158 #molecular-weight 17412 #checksum 128 SEQUENCE /// ENTRY PWYBBI #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) chain b' - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES ATP synthase chain b ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 14-Dec-2001 ACCESSIONS S17748; S74586; S14863 REFERENCE S17745 !$#authors Lill, H.; Nelson, N. !$#journal Plant Mol. Biol. (1991) 17:641-652 !$#title The atp1 and atp2 operons of the cyanobacterium !1Synechocystis sp. PCC 6803. !$#cross-references MUID:92003679; PMID:1832989 !$#accession S17748 !'##molecule_type DNA !'##residues 1-143 ##label LIL !'##cross-references EMBL:X58128; NID:g47506; PIDN:CAA41132.1; !1PID:g47510 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74586 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-143 ##label KAN !'##cross-references EMBL:D90900; GB:AB001339; NID:g1651768; !1PIDN:BAA16738.1; PID:g1651811 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene atpG CLASSIFICATION #superfamily H+-transporting ATP synthase chain I KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1transmembrane protein SUMMARY #length 143 #molecular-weight 16245 #checksum 7523 SEQUENCE /// ENTRY D31090 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) chain b' - Anabaena sp. ORGANISM #formal_name Anabaena sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 14-Dec-2001 ACCESSIONS D31090 REFERENCE A91875 !$#authors McCarn, D.F.; Whitaker, R.A.; Alam, J.; Vrba, J.M.; Curtis, !1S.E. !$#journal J. Bacteriol. (1988) 170:3448-3458 !$#title Genes encoding the alpha, gamma, delta, and four F-0 !1subunits of ATP synthase constitute an operon in the !1cyanobacterium Anabaena sp. strain PCC 7120. !$#cross-references MUID:88298650; PMID:2900236 !$#accession D31090 !'##molecule_type mRNA !'##residues 1-163 ##label MCC !'##cross-references GB:M21659; NID:g141996; PIDN:AAA21988.1; !1PID:g142000 !'##experimental_source PCC 7120 GENETICS !$#gene atpG CLASSIFICATION #superfamily H+-transporting ATP synthase chain I KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1transmembrane protein SUMMARY #length 163 #molecular-weight 17972 #checksum 5177 SEQUENCE /// ENTRY LWECB #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) chain b - Escherichia coli (strain K-12) ALTERNATE_NAMES hydrogen ion-transporting ATP synthase chain b; proton-translocating ATPase chain b ORGANISM #formal_name Escherichia coli DATE 02-Apr-1982 #sequence_revision 06-Jul-1982 #text_change 01-Mar-2002 ACCESSIONS D93732; B90104; B90101; I41273; I55242; A65177; T45004; !1A01070 REFERENCE A93732 !$#authors Gay, N.J.; Walker, J.E. !$#journal Nucleic Acids Res. (1981) 9:3919-3926 !$#title The atp operon: nucleotide sequence of the promoter and the !1genes for the membrane proteins, and the delta subunit of !1Escherichia coli ATP-synthase. !$#cross-references MUID:82059437; PMID:6272190 !$#accession D93732 !'##molecule_type DNA !'##residues 1-156 ##label GAY !'##cross-references GB:V00264; GB:X00771; NID:g41023; PIDN:CAA23516.1; !1PID:g581045 REFERENCE A90104 !$#authors Kanazawa, H.; Mabuchi, K.; Kayano, T.; Noumi, T.; Sekiya, !1T.; Futai, M. !$#journal Biochem. Biophys. Res. Commun. (1981) 103:613-620 !$#title Nucleotide sequence of the genes for F-0 components of the !1proton-translocating ATPase from Escherichia coli: !1prediction of the primary structure of F-0 subunits. !$#cross-references MUID:82134799; PMID:6277311 !$#accession B90104 !'##molecule_type DNA !'##residues 1-32,'F',34-71,'D',73-131 ##label KAN REFERENCE A90101 !$#authors Mabuchi, K.; Kanazawa, H.; Kayano, T.; Futai, M. !$#journal Biochem. Biophys. Res. Commun. (1981) 102:172-179 !$#title Nucleotide sequence of the gene coding for the delta subunit !1of proton-translocating ATPase of Escherichia coli. !$#cross-references MUID:82068433; PMID:6458296 !$#accession B90101 !'##molecule_type DNA !'##residues 132-156 ##label MAB !'##cross-references GB:M12212; GB:M12213; NID:g145396; PIDN:AAA20043.1; !1PID:g145397 REFERENCE I41271 !$#authors Kanazawa, H.; Futai, M. !$#journal Ann. N. Y. Acad. Sci. (1982) 402:45-64 !$#title Structure and function of H+-ATPase: What we have learned !1from Escherichia coli H+-ATPase. !$#cross-references MUID:83176724; PMID:6301339 !$#accession I41273 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-156 ##label RES !'##cross-references GB:M25464; NID:g146318; PIDN:AAA83871.1; !1PID:g146321 REFERENCE I55242 !$#authors Porter, A.C.G.; Kumamoto, C.; Aldape, K.; Simoni, R.D. !$#journal J. Biol. Chem. (1985) 260:8182-8187 !$#title Role of the b subunit of the Escherichia coli !1proton-translocating ATPase: A mutagenic analysis. !$#cross-references MUID:85234519; PMID:2861200 !$#accession I55242 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-61,'N',63-156 ##label REW !'##cross-references GB:M10422; NID:g148144; PIDN:AAA24741.1; !1PID:g148145 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65177 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-156 ##label BLAT !'##cross-references GB:AE000450; GB:U00096; NID:g1790166; !1PIDN:AAC76759.1; PID:g1790174; UWGP:b3736 !'##experimental_source strain K-12, substrain MG1655 REFERENCE Z22893 !$#authors Nielsen, J.; Hansen, F.G.; Hoppe, J.; Friedl, P.; Von !1Meyenburg, K. !$#journal Mol. Gen. Genet. (1981) 184:33-39 !$#title The nucleotide sequence of the atp genes coding for the F-0 !1subunits a, b, c and the F-1 subunit delta of the membrane !1bound ATP synthase of Escherichia coli. !$#cross-references MUID:82147764; PMID:6278247 !$#accession T45004 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-156 ##label NIE !'##cross-references EMBL:V00266; NID:g41031; PIDN:CAA23523.1; !1PID:g581046 GENETICS !$#gene atpF; uncF !$#map_position 84 min !$#start_codon GTG COMPLEX this is one of the three chains of the nonenzymatic membrane !1component (F0) of the ATPase complex CLASSIFICATION #superfamily H+-transporting ATP synthase chain I KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1transmembrane protein SUMMARY #length 156 #molecular-weight 17264 #checksum 9321 SEQUENCE /// ENTRY S06078 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) chain b - Vibrio alginolyticus ORGANISM #formal_name Vibrio alginolyticus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 14-Dec-2001 ACCESSIONS S06078 REFERENCE S06075 !$#authors Krumholz, L.R.; Esser, U.; Simoni, R.D. !$#journal Nucleic Acids Res. (1989) 17:7993-7994 !$#title Nucleotide sequence of the unc operon of Vibrio !1alginolyticus. !$#cross-references MUID:90016889; PMID:2529481 !$#accession S06078 !'##status translation not shown !'##molecule_type DNA !'##residues 1-156 ##label KRU !'##cross-references EMBL:X16050; NID:g48331; PIDN:CAA34177.1; !1PID:g581814 GENETICS !$#gene uncF !$#start_codon GTG CLASSIFICATION #superfamily H+-transporting ATP synthase chain I KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1transmembrane protein SUMMARY #length 156 #molecular-weight 17532 #checksum 8395 SEQUENCE /// ENTRY H64071 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) chain b - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 14-Dec-2001 ACCESSIONS H64071 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession H64071 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-156 ##label TIGR !'##cross-references GB:U32730; GB:L42023; NID:g3212191; !1PIDN:AAC22141.1; PID:g1573461; TIGR:HI0483 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily H+-transporting ATP synthase chain I KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1transmembrane protein SUMMARY #length 156 #molecular-weight 17172 #checksum 9710 SEQUENCE /// ENTRY S01399 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) chain b precursor - thermophilic bacterium PS-3 ORGANISM #formal_name thermophilic bacterium PS-3 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 14-Dec-2001 ACCESSIONS S01399 REFERENCE S01397 !$#authors Ohta, S.; Yohda, M.; Ishizuka, M.; Hirata, H.; Hamamoto, T.; !1Otawara-Hamamoto, Y.; Matsuda, K.; Kagawa, Y. !$#journal Biochim. Biophys. Acta (1988) 933:141-155 !$#title Sequence and over-expression of subunits of adenosine !1triphosphate synthase in thermophilic bacterium PS3. !$#cross-references MUID:88163679; PMID:2894854 !$#accession S01399 !'##molecule_type DNA !'##residues 1-163 ##label OHT !'##cross-references EMBL:X07804; NID:g45808; PIDN:CAA30650.1; !1PID:g581473 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing GENETICS !$#start_codon GTG CLASSIFICATION #superfamily H+-transporting ATP synthase chain I KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1transmembrane protein FEATURE !$12-163 #product H+-transporting ATP synthase chain b #status !8experimental #label MAT SUMMARY #length 163 #molecular-weight 18566 #checksum 7537 SEQUENCE /// ENTRY D31482 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) chain b - Bacillus megaterium ORGANISM #formal_name Bacillus megaterium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 14-Dec-2001 ACCESSIONS D31482 REFERENCE A31482 !$#authors Brusilow, W.S.A.; Scarpetta, M.A.; Hawthorne, C.A.; Clark, !1W.P. !$#journal J. Biol. Chem. (1989) 264:1528-1533 !$#title Organization and sequence of the genes coding for the !1proton-translocating ATPase of Bacillus megaterium. !$#cross-references MUID:89109162; PMID:2521483 !$#accession D31482 !'##status preliminary !'##molecule_type DNA !'##residues 1-172 ##label BRU !'##cross-references GB:M20255; GB:J04455; GB:M18352; GB:M23924; !1NID:g142553; PIDN:AAA82522.1; PID:g142557 CLASSIFICATION #superfamily H+-transporting ATP synthase chain I KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1transmembrane protein SUMMARY #length 172 #molecular-weight 19377 #checksum 9689 SEQUENCE /// ENTRY I40364 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) chain b (atpF) - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 14-Dec-2001 ACCESSIONS I40364; B69592; S39252 REFERENCE I40360 !$#authors Santana, M.; Ionescu, M.S.; Vertes, A.; Longin, R.; Kunst, !1F.; Danchin, A.; Glaser, P. !$#journal J. Bacteriol. (1994) 176:6802-6811 !$#title Bacillus subtilis F0F1 ATPase: DNA sequence of the atp !1operon and characterization of atp mutants. !$#cross-references MUID:95050246; PMID:7961438 !$#accession I40364 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-170 ##label RES !'##cross-references EMBL:Z28592; NID:g433983; PIDN:CAA82256.1; !1PID:g433987 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69592 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-170 ##label KUN !'##cross-references GB:Z99122; GB:AL009126; NID:g2636029; !1PIDN:CAB15702.1; PID:g2636210 !'##experimental_source strain 168 GENETICS !$#gene atpF CLASSIFICATION #superfamily H+-transporting ATP synthase chain I KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1transmembrane protein SUMMARY #length 170 #molecular-weight 19208 #checksum 5676 SEQUENCE /// ENTRY S17722 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) chain b - Bacillus firmus ORGANISM #formal_name Bacillus firmus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 14-Dec-2001 ACCESSIONS S17722 REFERENCE S17719 !$#authors Ivey, D.M.; Krulwich, T.A. !$#journal Mol. Gen. Genet. (1991) 229:292-300 !$#title Organization and nucleotide sequence of the atp genes !1encoding the ATP synthase from alkaliphilic Bacillus firmus !1OF4. !$#cross-references MUID:92017665; PMID:1833620 !$#accession S17722 !'##molecule_type DNA !'##residues 1-153 ##label IVE !'##cross-references EMBL:M60117; NID:g142543; PID:g142547 !'##note the authors translated the codon GAG for residue 51 as Asp GENETICS !$#gene atpF !$#start_codon GTG CLASSIFICATION #superfamily H+-transporting ATP synthase chain I KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1transmembrane protein SUMMARY #length 153 #molecular-weight 17511 #checksum 5980 SEQUENCE /// ENTRY S23323 #type complete TITLE Na+-transporting ATP synthase (EC 3.6.1.-) chain b - Propionigenium modestum ORGANISM #formal_name Propionigenium modestum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S23323; S29037; S24369; S36001; S12620; S28864; S23336 REFERENCE S12611 !$#authors Esser, U.; Krumholz, L.R.; Simoni, R.D. !$#journal Nucleic Acids Res. (1990) 18:5887 !$#title Nucleotide sequence of the F(0) subunits of the sodium !1dependent F(1)F(0) ATPase of Propionigenium modestum. !$#cross-references MUID:91016937; PMID:2170948 !$#accession S23323 !'##status translation not shown !'##molecule_type DNA !'##residues 1-168 ##label ESS !'##cross-references EMBL:X53960; NID:g45643; PIDN:CAA37913.1; !1PID:g581457 REFERENCE S29034 !$#authors Krumholz, L.R.; Esser, U.; Simoni, R.D. !$#journal FEMS Microbiol. Lett. (1992) 91:37-42 !$#title Characterization of the genes coding for the F(1)F(0) !1subunits of the sodium dependent ATPase of Propionigenium !1modestum. !$#accession S29037 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 6-168 ##label KRU !'##cross-references EMBL:X58461; NID:g897797; PIDN:CAA41370.1; !1PID:g45651 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1March 1991 REFERENCE S24366 !$#authors Kaim, G.; Ludwig, W.; Dimroth, P.; Schleifer, K.H. !$#journal Eur. J. Biochem. (1992) 207:463-470 !$#title Cloning, sequencing and in vivo expression of genes encoding !1the F(0) part of the sodium-ion-dependent ATP synthase of !1Propionigenium modestum in Escherichia coli. !$#cross-references MUID:92339434; PMID:1386022 !$#accession S24369 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 6-141,'A',143-168 ##label KAI !'##cross-references EMBL:X66102 REFERENCE S36000 !$#authors Ludwig, W. !$#submission submitted to the EMBL Data Library, May 1992 !$#accession S36001 !'##molecule_type DNA !'##residues 6-168 ##label LUD !'##cross-references EMBL:X66102; NID:g45599; PIDN:CAA46896.1; !1PID:g45603 REFERENCE S12619 !$#authors Kaim, G.; Ludwig, W.; Dimroth, P.; Schleifer, K.H. !$#journal Nucleic Acids Res. (1990) 18:6697 !$#title Sequence of subunits a and b of the sodium ion translocating !1adenosine triphosphate synthase of Propionigenium modestum. !$#cross-references MUID:91067471; PMID:2174545 !$#accession S12620 !'##molecule_type DNA !'##residues 6-168 ##label KAW !'##cross-references EMBL:X54810; NID:g45609; PIDN:CAA38580.1; !1PID:g45610 REFERENCE S28863 !$#authors Gerike, U.; Dimroth, P. !$#journal FEBS Lett. (1993) 316:89-92 !$#title N-terminal amino acid sequences of the subunits of the Na !1(+)-translocating F(1)F(0)ATPase from Propionigenium !1modestum. !$#cross-references MUID:93138123; PMID:8422943 !$#accession S28864 !'##molecule_type DNA !'##residues 1-7 ##label GER GENETICS !$#gene uncF !$#start_codon TTG CLASSIFICATION #superfamily H+-transporting ATP synthase chain I KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1transmembrane protein SUMMARY #length 168 #molecular-weight 19201 #checksum 4379 SEQUENCE /// ENTRY PWHU8 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) protein 8 - human mitochondrion ALTERNATE_NAMES hydrogen ion-transporting ATP synthase protein 8 ORGANISM #formal_name mitochondrion Homo sapiens #common_name man DATE 22-May-1981 #sequence_revision 23-Oct-1981 #text_change 14-Dec-2001 ACCESSIONS A01062; I80237 REFERENCE A00151 !$#authors Anderson, S.; Bankier, A.T.; Barrell, B.G.; de Bruijn, !1M.H.L.; Coulson, A.R.; Drouin, J.; Eperon, I.C.; Nierlich, !1D.P.; Roe, B.A.; Sanger, F.; Schreier, P.H.; Smith, A.J.H.; !1Staden, R.; Young, I.G. !$#journal Nature (1981) 290:457-465 !$#title Sequence and organization of the human mitochondrial genome. !$#cross-references MUID:81173052; PMID:7219534 !$#accession A01062 !'##molecule_type DNA !'##residues 1-68 ##label AND !'##cross-references GB:J01415; GB:M12548; GB:M58503; GB:M63932; !1GB:M63933; NID:g1944628; PIDN:AAB58947.1; PID:g337193; !1EMBL:V00662; NID:g13003; PID:g13008; GSPDB:GN00100 REFERENCE I59384 !$#authors Horai, S.; Hayasaka, K.; Kondo, R.; Tsugane, K.; Takahata, !1N. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1995) 92:532-536 !$#title Recent African origin of modern humans revealed by complete !1sequences of hominoid mitochondrial DNAs. !$#cross-references MUID:95132634; PMID:7530363 !$#accession I80237 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-31,'S',33-68 ##label RES !'##cross-references GB:D38112; NID:g644480; PIDN:BAA07294.1; !1PID:g704445 GENETICS !$#gene GDB:MTATP8 !'##cross-references GDB:118898; OMIM:516070 !$#map_position MTH8366-8572 !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily H+-transporting ATP synthase protein 8 KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; oxidative phosphorylation SUMMARY #length 68 #molecular-weight 7992 #checksum 5544 SEQUENCE /// ENTRY PWBO8 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) protein 8 - bovine mitochondrion ALTERNATE_NAMES A6L protein; hydrogen ion-transporting ATP synthase protein 8 ORGANISM #formal_name mitochondrion Bos primigenius taurus #common_name cattle DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 14-Dec-2001 ACCESSIONS A01063; A25474; D39566 REFERENCE A00152 !$#authors Anderson, S.; de Bruijn, M.H.L.; Coulson, A.R.; Eperon, !1I.C.; Sanger, F.; Young, I.G. !$#journal J. Mol. Biol. (1982) 156:683-717 !$#title Complete sequence of bovine mitochondrial DNA. Conserved !1features of the mammalian mitochondrial genome. !$#cross-references MUID:83010260; PMID:7120390 !$#accession A01063 !'##molecule_type DNA !'##residues 1-66 ##label AND !'##cross-references GB:J01394; NID:g336430; PIDN:AAB59272.1; !1PID:g336435; EMBL:V00654; NID:g12800; PID:g12805 REFERENCE A25474 !$#authors Fearnley, I.M.; Walker, J.E. !$#journal EMBO J. (1986) 5:2003-2008 !$#title Two overlapping genes in bovine mitochondrial DNA encode !1membrane components of ATP synthase. !$#cross-references MUID:87004570; PMID:2875870 !$#accession A25474 !'##molecule_type protein !'##residues 1-37;45-50;52-53 ##label FEA REFERENCE A39566 !$#authors Walker, J.E.; Lutter, R.; Dupuis, A.; Runswick, M.J. !$#journal Biochemistry (1991) 30:5369-5378 !$#title Identification of the subunits of F-1F-0-ATPase from bovine !1heart mitochondria. !$#cross-references MUID:91242449; PMID:1827992 !$#accession D39566 !'##molecule_type protein !'##residues 1-5 ##label WAL GENETICS !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily H+-transporting ATP synthase protein 8 KEYWORDS ATP biosynthesis; blocked amino end; hydrolase; !1membrane-associated complex; mitochondrion; oxidative !1phosphorylation FEATURE !$1 #modified_site blocked amino end (Met) (probably !8formylated) #status experimental SUMMARY #length 66 #molecular-weight 7936 #checksum 3000 SEQUENCE /// ENTRY PWMS8 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) protein 8 - mouse mitochondrion ALTERNATE_NAMES hydrogen ion-transporting ATP synthase protein 8 ORGANISM #formal_name mitochondrion Mus musculus #common_name house mouse DATE 02-Apr-1982 #sequence_revision 02-Apr-1982 #text_change 14-Dec-2001 ACCESSIONS A01064 REFERENCE A00153 !$#authors Bibb, M.J.; Van Etten, R.A.; Wright, C.T.; Walberg, M.W.; !1Clayton, D.A. !$#journal Cell (1981) 26:167-180 !$#title Sequence and gene organization of mouse mitochondrial DNA. !$#cross-references MUID:82137051; PMID:7332926 !$#accession A01064 !'##molecule_type DNA !'##residues 1-67 ##label BIB !'##cross-references GB:J01420; NID:g342520; PIDN:AAB48648.1; !1PID:g896296; EMBL:V00711; NID:g13838; PID:g13843 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily H+-transporting ATP synthase protein 8 KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; oxidative phosphorylation SUMMARY #length 67 #molecular-weight 7766 #checksum 4567 SEQUENCE /// ENTRY S04619 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) protein 8 - chicken mitochondrion ORGANISM #formal_name mitochondrion Gallus gallus #common_name chicken DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 14-Dec-2001 ACCESSIONS S04619; S10191 REFERENCE S04619 !$#authors Desjardins, P.; L'Abbe, D.; Lang, B.F.; Morais, R. !$#journal J. Mol. Biol. (1989) 207:625-629 !$#title Putative chicken "muscle-specific 7 S RNA" is related to the !1mitochondrial ATPase 6 gene. !$#cross-references MUID:89342447; PMID:2474659 !$#accession S04619 !'##molecule_type DNA !'##residues 1-54 ##label DES1 !'##cross-references EMBL:X15841; NID:g12957; PIDN:CAA33841.1; !1PID:g12958 REFERENCE S10187 !$#authors Desjardins, P.; Morais, R. !$#journal J. Mol. Biol. (1990) 212:599-634 !$#title Sequence and gene organization of the chicken mitochondrial !1genome. A novel gene order in higher vertebrates. !$#cross-references MUID:90230301; PMID:2329578 !$#accession S10191 !'##molecule_type DNA !'##residues 1-54 ##label DES2 !'##cross-references EMBL:X52392; NID:g12960; PIDN:CAA36629.1; !1PID:g12965 GENETICS !$#gene ATPase 8 !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily H+-transporting ATP synthase protein 8 KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; oxidative phosphorylation SUMMARY #length 54 #molecular-weight 6376 #checksum 8374 SEQUENCE /// ENTRY PWXL8 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) protein 8 - African clawed frog mitochondrion ALTERNATE_NAMES hydrogen ion-transporting ATP synthase protein 8 ORGANISM #formal_name mitochondrion Xenopus laevis #common_name African clawed frog DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 14-Dec-2001 ACCESSIONS A01065 REFERENCE A00155 !$#authors Roe, B.A.; Ma, D.P.; Wilson, R.K.; Wong, J.F.H. !$#journal J. Biol. Chem. (1985) 260:9759-9774 !$#title The complete nucleotide sequence of the Xenopus laevis !1mitochondrial genome. !$#cross-references MUID:85261388; PMID:4019494 !$#accession A01065 !'##molecule_type DNA !'##residues 1-55 ##label ROE !'##cross-references GB:M10217; GB:X01600; GB:X01601; GB:X02890; !1NID:g343717; PIDN:AAA66462.1; PID:g343722 GENETICS !$#genome mitochondrion !$#genetic_code SGC1 CLASSIFICATION #superfamily H+-transporting ATP synthase protein 8 KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; oxidative phosphorylation SUMMARY #length 55 #molecular-weight 6531 #checksum 1445 SEQUENCE /// ENTRY PWFF8 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) protein 8 - fruit fly (Drosophila melanogaster) mitochondrion ALTERNATE_NAMES hydrogen ion-transporting ATP synthase protein 8 ORGANISM #formal_name mitochondrion Drosophila melanogaster DATE 18-Apr-1984 #sequence_revision 18-Apr-1984 #text_change 14-Dec-2001 ACCESSIONS A01066; A93307 REFERENCE A93307 !$#authors de Bruijn, M.H.L. !$#journal Nature (1983) 304:234-241 !$#title Drosophila melanogaster mitochondrial DNA, a novel !1organization and genetic code. !$#cross-references MUID:83245048; PMID:6408489 !$#accession A01066 !'##molecule_type DNA !'##residues 1-53 ##label DEB !'##cross-references GB:J01404; GB:J01405; GB:J01407; NID:g336811; !1PIDN:AAB59241.1; PID:g895684 !'##note the author translated the initiation codon ATT for residue 1 as !1Ile GENETICS !$#gene FlyBase:mt:ATPase8 !'##cross-references FlyBase:FBgn0013673 !$#genome mitochondrion !$#genetic_code SGC4 !$#start_codon ATT CLASSIFICATION #superfamily H+-transporting ATP synthase protein 8 KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; oxidative phosphorylation SUMMARY #length 53 #molecular-weight 6364 #checksum 2132 SEQUENCE /// ENTRY PWFF8Y #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) protein 8 - fruit fly (Drosophila yakuba) mitochondrion ALTERNATE_NAMES ATPase protein 8; hydrogen ion-transporting ATP synthase protein 8 ORGANISM #formal_name mitochondrion Drosophila yakuba DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 14-Dec-2001 ACCESSIONS D93477; D25797; A01066; A93477 REFERENCE A93477 !$#authors Clary, D.O.; Wolstenholme, D.R. !$#journal Nucleic Acids Res. (1983) 11:4211-4227 !$#title Nucleotide sequence of a segment of Drosophila mitochondrial !1DNA that contains the genes for cytochrome c oxidase !1subunits II and III and ATPase subunit 6. !$#cross-references MUID:83246544; PMID:6306579 !$#accession D93477 !'##molecule_type DNA !'##residues 1-53 ##label CLA !'##cross-references GB:X03240; NID:g12923; PIDN:CAA26988.1; !1PID:g529256; GB:X00924; NID:g12918; PID:g578701 !'##note the authors translated the initiation codon ATT for residue 1 !1as Ile and AGA for residue 8 as Arg REFERENCE A92962 !$#authors Clary, D.O.; Wolstenholme, D.R. !$#journal J. Mol. Evol. (1985) 22:252-271 !$#title The mitochondrial DNA molecule of Drosophila yakuba: !1nucleotide sequence, gene organization, and genetic code. !$#cross-references MUID:86089137; PMID:3001325 !$#accession D25797 !'##molecule_type DNA !'##residues 1-53 ##label CL2 !'##cross-references GB:X03240; GB:J01400; GB:J01402; GB:J01403; !1GB:J01406; GB:J01408; GB:V01521; GB:X00563; NID:g12923; !1PIDN:CAA26988.1; PID:g529256 GENETICS !$#gene FlyBase:Dyak/mt:ATPase8 !'##cross-references FlyBase:FBgn0013178 !$#genome mitochondrion !$#genetic_code SGC4 !$#start_codon ATT CLASSIFICATION #superfamily H+-transporting ATP synthase protein 8 KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; oxidative phosphorylation SUMMARY #length 53 #molecular-weight 6337 #checksum 2531 SEQUENCE /// ENTRY A55910 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) chain D - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 14-Dec-2001 ACCESSIONS A55910 REFERENCE A55910 !$#authors Nelson, H.; Mandiyan, S.; Nelson, N. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1995) 92:497-501 !$#title A bovine cDNA and a yeast gene (VMA8) encoding the subunit D !1of the vacuolar H(+)-ATPase. !$#cross-references MUID:95132627; PMID:7831318 !$#accession A55910 !'##status preliminary !'##molecule_type mRNA !'##residues 1-247 ##label NEL !'##cross-references GB:U11927; NID:g517445; PIDN:AAC48458.1; !1PID:g517446 CLASSIFICATION #superfamily H+-transporting ATPase chain D KEYWORDS hydrolase SUMMARY #length 247 #molecular-weight 28334 #checksum 4509 SEQUENCE /// ENTRY S40985 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) chain D - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 14-Dec-2001 ACCESSIONS S40985 REFERENCE S40984 !$#authors Craxton, M.; Hawkins, T.; Thomas, K. !$#submission submitted to the EMBL Data Library, October 1993 !$#accession S40985 !'##status preliminary !'##molecule_type DNA !'##residues 1-257 ##label CRA !'##cross-references EMBL:Z27080; NID:g414620; PID:g414622 GENETICS !$#introns 16/2; 55/3; 105/1; 223/3 CLASSIFICATION #superfamily H+-transporting ATPase chain D KEYWORDS hydrolase SUMMARY #length 257 #molecular-weight 28786 #checksum 2869 SEQUENCE /// ENTRY S30826 #type complete TITLE H+-exporting ATPase (EC 3.6.3.6) chain D, vacuolar - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YEL051w ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S30826; S50493 REFERENCE S30812 !$#authors Mulligan, J.T.; Dietrich, F.S.; Hennessey, K.M.; Sehl, P.; !1Komp, C.; Wei, Y.; Taylor, P.; Nakahara, K.; Roberts, D.; !1Davis, R.W. !$#submission submitted to the EMBL Data Library, February 1993 !$#accession S30826 !'##molecule_type DNA !'##residues 1-256 ##label MUL !'##cross-references GB:U18779; EMBL:L10830; NID:g603625; !1PIDN:AAB64991.1; PID:g603628 REFERENCE S50491 !$#authors Dietrich, F.S. !$#submission submitted to the EMBL Data Library, December 1994 !$#description The sequence of S. cerevisiae cosmids 8199, 8334, and 9871. !$#accession S50493 !'##molecule_type DNA !'##residues 1-256 ##label DIE !'##cross-references EMBL:U18779; NID:g603625; PIDN:AAB64991.1; !1PID:g603628; GSPDB:GN00005; MIPS:YEL051w GENETICS !$#gene SGD:VMA8; MIPS:YEL051w !'##cross-references SGD:S0000777; MIPS:YEL051w !$#map_position 5L CLASSIFICATION #superfamily H+-transporting ATPase chain D KEYWORDS ATP; hydrolase; membrane-associated complex; yeast vacuole SUMMARY #length 256 #molecular-weight 29194 #checksum 5549 SEQUENCE /// ENTRY E69227 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) chain D - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 14-Dec-2001 ACCESSIONS E69227 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession E69227 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-213 ##label MTH !'##cross-references GB:AE000869; GB:AE000666; NID:g2622042; !1PIDN:AAB85449.1; PID:g2622050 !'##experimental_source strain Delta H GENETICS !$#gene MTH953 CLASSIFICATION #superfamily H+-transporting ATPase chain D KEYWORDS hydrolase SUMMARY #length 213 #molecular-weight 24522 #checksum 5594 SEQUENCE /// ENTRY G64376 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) chain D - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 14-Dec-2001 ACCESSIONS G64376 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession G64376 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-216 ##label BUL !'##cross-references GB:U67510; GB:L77117; NID:g1591325; !1PIDN:AAB98610.1; PID:g1592298; TIGR:MJ0615 GENETICS !$#map_position REV546347-545697 CLASSIFICATION #superfamily H+-transporting ATPase chain D KEYWORDS hydrolase SUMMARY #length 216 #molecular-weight 24951 #checksum 2130 SEQUENCE /// ENTRY G69395 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) chain D - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 14-Dec-2001 ACCESSIONS G69395 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession G69395 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-209 ##label KLE !'##cross-references GB:AE001023; GB:AE000782; NID:g2689346; !1PIDN:AAB90072.1; PID:g2649414; TIGR:AF1168 CLASSIFICATION #superfamily H+-transporting ATPase chain D KEYWORDS hydrolase SUMMARY #length 209 #molecular-weight 24083 #checksum 3519 SEQUENCE /// ENTRY F53610 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) chain D - Enterococcus hirae ORGANISM #formal_name Enterococcus hirae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 14-Dec-2001 ACCESSIONS F53610 REFERENCE A53610 !$#authors Takase, K.; Kakinuma, S.; Yamato, I.; Konishi, K.; Igarashi, !1K.; Kakinuma, Y. !$#journal J. Biol. Chem. (1994) 269:11037-11044 !$#title Sequencing and characterization of the ntp gene cluster for !1vacuolar-type Na(+)-translocating ATPase of Enterococcus !1hirae. !$#cross-references MUID:94209269; PMID:8157629 !$#accession F53610 !'##status preliminary !'##molecule_type DNA !'##residues 1-230 ##label TAK !'##cross-references GB:D17462; NID:g487271; PIDN:BAA04277.1; !1PID:g487280 CLASSIFICATION #superfamily H+-transporting ATPase chain D KEYWORDS hydrolase SUMMARY #length 230 #molecular-weight 27093 #checksum 3865 SEQUENCE /// ENTRY B36493 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) gamma chain - Sulfolobus acidocaldarius ORGANISM #formal_name Sulfolobus acidocaldarius DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 14-Dec-2001 ACCESSIONS B36493 REFERENCE A36493 !$#authors Denda, K.; Konishi, J.; Hajiro, K.; Oshima, T.; Date, T.; !1Yoshida, M. !$#journal J. Biol. Chem. (1990) 265:21509-21513 !$#title Structure of an ATPase operon of an acidothermophilic !1archaebacterium, Sulfolobus acidocaldarius. !$#cross-references MUID:91072342; PMID:2147683 !$#accession B36493 !'##status preliminary !'##molecule_type DNA !'##residues 1-216 ##label DEN !'##cross-references GB:J05671 CLASSIFICATION #superfamily H+-transporting ATPase chain D KEYWORDS hydrolase SUMMARY #length 216 #molecular-weight 25105 #checksum 3935 SEQUENCE /// ENTRY D70111 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) chain D - Lyme disease spirochete ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 14-Dec-2001 ACCESSIONS D70111 REFERENCE A70100 !$#authors Fraser, C.M.; Casjens, S.; Huang, W.M.; Sutton, G.G.; !1Clayton, R.; Lathigra, R.; White, O.; Ketchum, K.A.; Dodson, !1R.; Hickey, E.K.; Gwinn, M.; Dougherty, B.; Tomb, J.F.; !1Fleischmann, R.D.; Richardson, D.; Peterson, J.; Kerlavage, !1A.R.; Quackenbush, J.; Salzberg, S.; Hanson, M.; Vugt, R.V.; !1Palmer, N.; Adams, M.D.; Gocayne, J.; Weidman, J.; !1Utterback, T.; Watthey, L.; McDonald, L.; Artiach, P.; !1Bowman, C.; Garland, S.; Fujii, C.; Cotton, M.D.; Horst, K.; !1Roberts, K.; Hatch, B.; Smith, H.O.; Venter, J.C. !$#journal Nature (1997) 390:580-586 !$#title Genomic sequence of a Lyme disease spirochaete, Borrelia !1burgdorferi. !$#cross-references MUID:98065943; PMID:9403685 !$#accession D70111 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-204 ##label KLE !'##cross-references GB:AE001122; GB:AE000783; NID:g2687974; !1PIDN:AAC66485.1; PID:g2687981; TIGR:BB0092 !'##experimental_source strain B31 CLASSIFICATION #superfamily H+-transporting ATPase chain D KEYWORDS hydrolase SUMMARY #length 204 #molecular-weight 24025 #checksum 1586 SEQUENCE /// ENTRY E64327 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) subunit E - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 14-Dec-2001 ACCESSIONS E64327 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession E64327 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-206 ##label BUL !'##cross-references GB:U67477; GB:L77117; NID:g1590949; !1PIDN:AAB98203.1; PID:g1590957; TIGR:MJ0220 GENETICS !$#map_position REV211241-210621 !$#start_codon GTG CLASSIFICATION #superfamily ATP synthase subunit E KEYWORDS hydrolase SUMMARY #length 206 #molecular-weight 23137 #checksum 3483 SEQUENCE /// ENTRY B69228 #type complete TITLE ATP synthase, subunit E - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B69228 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession B69228 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-206 ##label MTH !'##cross-references GB:AE000869; GB:AE000666; NID:g2622042; !1PIDN:AAB85454.1; PID:g2622055 !'##experimental_source strain Delta H GENETICS !$#gene MTH958 CLASSIFICATION #superfamily ATP synthase subunit E SUMMARY #length 206 #molecular-weight 22664 #checksum 7253 SEQUENCE /// ENTRY EWBY8 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) protein 8 - yeast (Saccharomyces cerevisiae) mitochondrion ALTERNATE_NAMES ATPase-associated proteolipid component; protein Q0080 ORGANISM #formal_name mitochondrion Saccharomyces cerevisiae DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 19-Apr-2002 ACCESSIONS S05820; A01067; S22219; S43946; S78654; S78655; JC2450 REFERENCE S05820 !$#authors Simon, M.; Faye, G. !$#journal Mol. Gen. Genet. (1984) 196:266-274 !$#title Organization and processing of the mitochondrial oxi3/oli2 !1multigenic transcript in yeast. !$#cross-references MUID:85035872; PMID:6387398 !$#accession S05820 !'##molecule_type DNA !'##residues 1-48 ##label SIM !'##cross-references EMBL:X00960; NID:g13563; PIDN:CAA25473.1; !1PID:g13565 REFERENCE A01067 !$#authors Macreadie, I.G.; Novitski, C.E.; Maxwell, R.J.; John, U.; !1Ooi, B.G.; McMullen, G.L.; Lukins, H.B.; Linnane, A.W.; !1Nagley, P. !$#journal Nucleic Acids Res. (1983) 11:4435-4451 !$#title Biogenesis of mitochondria: the mitochondrial gene (aap1) !1coding for mitochondrial ATPase subunit 8 in Saccharomyces !1cerevisiae. !$#cross-references MUID:83246560; PMID:6223276 !$#accession A01067 !'##molecule_type DNA !'##residues 1-48 ##label MAC !'##cross-references EMBL:X00895; NID:g14222; PIDN:CAA25423.1; !1PID:g14223 REFERENCE S22219 !$#authors Velours, J.; Esparza, M.; Hoppe, J.; Sebald, W.; Guerin, B. !$#journal EMBO J. (1984) 3:207-212 !$#title Amino acid sequence of a new mitochondrially synthesized !1proteolipid of the ATP synthase of Saccharomyces cerevisiae. !$#cross-references MUID:84158531; PMID:6323165 !$#accession S22219 !'##molecule_type protein !'##residues 1-48 ##label VEL REFERENCE S43945 !$#authors Novitski, C.E.; Macreadie, I.G.; Maxwell, R.J.; Lukins, !1H.B.; Linnane, A.W.; Nagley, P. !$#journal Curr. Genet. (1984) 8:135-146 !$#title Biogenesis of mitochondria: genetic and molecular analysis !1of the oli2 region of mitochondrial DNA in Saccharomyces !1cerevisiae. !$#accession S43946 !'##molecule_type DNA !'##residues 1-13,'M',15-48 ##label NOV !'##cross-references EMBL:M36379 REFERENCE S78634 !$#authors Foury, F.; Roganti, T.; Lecrenier, N.; Purnelle, B. !$#submission submitted to the Protein Sequence Database, December 1998 !$#accession S78654 !'##molecule_type DNA !'##residues 1-48 ##label FOU1 !'##cross-references EMBL:AJ011856; MIPS:Q0080 !'##experimental_source strain FY1679, isogenic derivative of strain !1S288C REFERENCE Z13743 !$#authors Foury, F.; Roganti, T.; Lecrenier, N.; Purnelle, B. !$#journal FEBS Lett. (1998) 440:325-331 !$#title The complete sequence of the mitochondrial genome of !1Saccharomyces cerevisiae. !$#cross-references MUID:99087401; PMID:9872396 !$#accession S78655 !'##molecule_type DNA !'##residues 1-48 ##label FOU2 !'##cross-references EMBL:AJ011856; NID:g4160362; PIDN:CAA09831.1; !1PID:g4160373 !'##experimental_source strain FY1679, isogenic derivative of strain !1S288C GENETICS !$#gene SGD:AAP1; atp8; aap1 !'##cross-references SGD:S0007267 !$#genome mitochondrion !$#genetic_code SGC2 CLASSIFICATION #superfamily yeast H+-transporting ATP synthase protein 8 KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrial inner membrane; mitochondrion; oxidative !1phosphorylation; transmembrane protein FEATURE !$1-48 #product H+-transporting ATP synthase protein 8 !8#status experimental #label MAT\ !$14-31 #region hydrophobic SUMMARY #length 48 #molecular-weight 5822 #checksum 1175 SEQUENCE /// ENTRY PWCK8P #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) protein 8 - yeast (Candida parapsilosis) mitochondrion ORGANISM #formal_name mitochondrion Candida parapsilosis DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 14-Dec-2001 ACCESSIONS S10465 REFERENCE S10465 !$#authors Guelin, E.; Velours, J.; Guerin, M. !$#journal Nucleic Acids Res. (1990) 18:4267 !$#title Cloning and sequencing of a fragment of the linear !1mitochondrial DNA of the yeast Candida parapsilosis !1supporting genes encoding subunit 8 of Fo ATP synthase and a !1putative t-RNA(Pro). !$#cross-references MUID:90332440; PMID:2143015 !$#accession S10465 !'##molecule_type DNA !'##residues 1-48 ##label GUE !'##cross-references EMBL:X52115; NID:g12890; PIDN:CAA36361.1; !1PID:g829334 GENETICS !$#gene aap1 !$#genome mitochondrion !$#genetic_code SGC3 CLASSIFICATION #superfamily yeast H+-transporting ATP synthase protein 8 KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; oxidative phosphorylation SUMMARY #length 48 #molecular-weight 5492 #checksum 9683 SEQUENCE /// ENTRY EWAS8 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) protein 8 - Emericella nidulans mitochondrion ALTERNATE_NAMES hydrogen ion-transporting ATP synthase protein 8; hypothetical protein X ORGANISM #formal_name mitochondrion Emericella nidulans, Aspergillus nidulans DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 14-Dec-2001 ACCESSIONS A93436; A93428; A01068 REFERENCE A93436 !$#authors Netzker, R.; Kochel, H.G.; Basak, N.; Kuntzel, H. !$#journal Nucleic Acids Res. (1982) 10:4783-4794 !$#title Nucleotide sequence of Aspergillus nidulans mitochondrial !1genes coding for ATPase subunit 6, cytochrome oxidase !1subunit 3, seven unidentified proteins, four tRNAs and !1L-rRNA. !$#cross-references MUID:83038633; PMID:6290989 !$#accession A93436 !'##molecule_type DNA !'##residues 1-48 ##label NET !'##cross-references GB:J01390; NID:g336905; PIDN:AAA99204.1; !1PID:g472820 !'##experimental_source imperfect stage REFERENCE A93428 !$#authors Grisi, E.; Brown, T.A.; Waring, R.B.; Scazzocchio, C.; !1Davies, R.W. !$#journal Nucleic Acids Res. (1982) 10:3531-3539 !$#title Nucleotide sequence of a region of the mitochondrial genome !1of Aspergillus nidulans including the gene for ATPase !1subunit 6. !$#cross-references MUID:82247225; PMID:6285306 !$#accession A93428 !'##molecule_type DNA !'##residues 1-48 ##label GRI !'##cross-references GB:X01507; GB:K01799; NID:g12698; PIDN:CAA25708.1; !1PID:g4379156 !'##experimental_source imperfect stage GENETICS !$#genome mitochondrion !$#genetic_code SGC3 CLASSIFICATION #superfamily yeast H+-transporting ATP synthase protein 8 KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; oxidative phosphorylation SUMMARY #length 48 #molecular-weight 5770 #checksum 2348 SEQUENCE /// ENTRY EWAS8M #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) protein 8 - Aspergillus amstelodami mitochondrion ALTERNATE_NAMES hydrogen ion-transporting ATP synthase protein 8 ORGANISM #formal_name mitochondrion Aspergillus amstelodami DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 14-Dec-2001 ACCESSIONS A01069 REFERENCE A94634 !$#authors Lazarus, C.M.; Kuntzel, H. !$#submission submitted to the Protein Sequence Database, March 1984 !$#accession A01069 !'##molecule_type DNA !'##residues 1-48 ##label LAZ GENETICS !$#genome mitochondrion !$#genetic_code SGC3 CLASSIFICATION #superfamily yeast H+-transporting ATP synthase protein 8 KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; oxidative phosphorylation SUMMARY #length 48 #molecular-weight 5772 #checksum 831 SEQUENCE /// ENTRY PWBYBC #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) chain b precursor - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES H+-transporting ATP synthase protein 4; protein LPF7c; protein YPL078c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1991 #sequence_revision 12-Apr-1996 #text_change 14-Dec-2001 ACCESSIONS S61109; S00283; A27189 REFERENCE S59677 !$#authors Hall, J.; Ahmed, A.; Bussey, H.; Fortin, N.; Friesen, J.D.; !1Storms, R.K.; Vo, D.H.; Wang, Y.; Winnett, E. !$#submission submitted to the EMBL Data Library, August 1995 !$#description The sequence of Saccharomyces cerevisiae chromosome XVI left !1arm. !$#accession S61109 !'##molecule_type DNA !'##residues 1-244 ##label HAL !'##cross-references EMBL:U41849; NID:g1147608; PIDN:AAB68260.1; !1PID:g1147615; GSPDB:GN00016; MIPS:YPL078c REFERENCE S00283 !$#authors Velours, J.; Durrens, P.; Aigle, M.; Guerin, B. !$#journal Eur. J. Biochem. (1988) 170:637-642 !$#title ATP4, the structural gene for yeast F(0)F(1) ATPase subunit !14. !$#cross-references MUID:88111651; PMID:2892678 !$#accession S00283 !'##molecule_type DNA !'##residues 1-171,'R',173-244 ##label VEL !'##cross-references EMBL:X06732; NID:g3397; PIDN:CAA29909.1; PID:g3398 REFERENCE A27189 !$#authors Velours, J.; Arselin de Chateaubodeau, G.; Galante, M.; !1Guerin, B. !$#journal Eur. J. Biochem. (1987) 164:579-584 !$#title Subunit 4 of ATP synthase (F-0-F-1) from yeast mitochondria. !1Purification, amino-acid composition and partial N-terminal !1sequence. !$#cross-references MUID:87190430; PMID:2883007 !$#accession A27189 !'##molecule_type protein !'##residues 36-45 ##label VEL2 GENETICS !$#gene SGD:ATP4; MIPS:YPL078c !'##cross-references SGD:S0005999; MIPS:YPL078c !$#map_position 16L !$#genome nuclear CLASSIFICATION #superfamily yeast H+-transporting ATP synthase chain b KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1mitochondrion; oxidative phosphorylation; transmembrane !1protein FEATURE !$1-35 #domain transit peptide (mitochondrion) #status !8experimental #label TNP\ !$36-244 #product H+-transporting ATP synthase chain b #status !8experimental #label MAT SUMMARY #length 244 #molecular-weight 26925 #checksum 7183 SEQUENCE /// ENTRY PXBYVA #type complete TITLE H+-exporting ATPase (EC 3.6.3.6) chain A precursor, vacuolar - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein D1286; protein YDL185w CONTAINS DNA endonuclease PI-1 (EC 3.1.-.-); H+-transporting ATPase (EC 3.6.3.6) chain A ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 03-Jun-2002 ACCESSIONS A35746; S22834; S17484; S58732; S67740 REFERENCE A35746 !$#authors Hirata, R.; Ohsumi, Y.; Nakano, A.; Kawasaki, H.; Suzuki, !1K.; Anraku, Y. !$#journal J. Biol. Chem. (1990) 265:6726-6733 !$#title Molecular structure of a gene, VMA1, encoding the catalytic !1subunit of H+-translocating adenosine triphosphatase from !1vacuolar membranes of Saccharomyces cerevisiae. !$#cross-references MUID:90216698; PMID:2139027 !$#accession A35746 !'##molecule_type DNA !'##residues 1-1071 ##label HIR !'##cross-references GB:J05409; NID:g171649; PIDN:AAA34664.1; !1PID:g171650 !'##note part of this sequence was confirmed by protein sequencing REFERENCE S22834 !$#authors Shih, C.K.; Wagner, R.; Feinstein, S.; Kanik-Ennulat, C.; !1Neff, N. !$#journal Mol. Cell. Biol. (1988) 8:3094-3103 !$#title A dominant trifluoperazine resistance gene from !1Saccharomyces cerevisiae has homology with F0F1 ATP synthase !1and confers calcium-sensitive growth. !$#cross-references MUID:89096895; PMID:2905423 !$#accession S22834 !'##molecule_type DNA !'##residues 41-874,'D',876-1071 ##label SHI !'##cross-references EMBL:M21609; NID:g172906; PIDN:AAB63978.1; !1PID:g172907 REFERENCE A41525 !$#authors Ronne, H.; Carlberg, M.; Hu, G.Z.; Nehlin, J.O. !$#journal Mol. Cell. Biol. (1991) 11:4876-4884 !$#title Protein phosphatase 2A in Saccharomyces cerevisiae: effects !1on cell growth and bud morphogenesis. !$#cross-references MUID:92017761; PMID:1656215 !$#accession S17484 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-33 ##label RON !'##cross-references EMBL:X58857 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1991 REFERENCE S58730 !$#authors Verhasselt, P.; Voet, M.; Volckaert, G. !$#journal Yeast (1995) 11:961-966 !$#title New open reading frames, one of which is similar to the nifV !1gene of Azotobacter vinelandii, found on a 12.5 kbp fragment !1of chromosome IV of Saccharomyces cerevisiae. !$#cross-references MUID:96021607; PMID:8533471 !$#accession S58732 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1071 ##label VER !'##cross-references EMBL:X83276; NID:g1004294; PIDN:CAA58261.1; !1PID:g1004309 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1994 REFERENCE S67735 !$#authors Volckaert, G.; Verhasselt, P.; Voet, M. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67740 !'##molecule_type DNA !'##residues 1-1071 ##label VOL !'##cross-references EMBL:Z74233; NID:g1431300; PIDN:CAA98760.1; !1PID:g1431301; GSPDB:GN00004; MIPS:YDL185w !'##experimental_source strain S288C REFERENCE S71549 !$#authors Kane, P.M.; Yamashiro, C.T.; Wolczyk, D.F.; Neff, N.; !1Goebel, M.; Stevens, T.H. !$#journal Science (1990) 250:651-657 !$#title Protein splicing converts the yeast TFP1 gene product to the !169-kD subunit of the vacuolar H+-adenosine triphosphatase. !$#cross-references MUID:91047969; PMID:2146742 !$#contents annotation REFERENCE S35372 !$#authors Cooper, A.A.; Chen, Y.J.; Lindorfer, M.A.; Stevens, T.H. !$#journal EMBO J. (1993) 12:2575-2583 !$#title Protein splicing of the yeast TFP1 intervening protein !1sequence: a model for self-excision. !$#cross-references MUID:93285129; PMID:8508780 !$#contents annotation; self-splicing mechanism GENETICS !$#gene SGD:TFP1; VMA1; MIPS:YDL185w !'##cross-references SGD:S0002344; MIPS:YDL185w !$#map_position 4L FUNCTION HYD !$#description hydrolase; hydrogen ion transport !$#note H+-transporting ATPase chain A FUNCTION END !$#description endonuclease; hydrolase !$#note DNA endonuclease PI-SceI CLASSIFICATION #superfamily yeast vacuolar H+-transporting ATPase chain A; !1H+-transporting ATP synthase alpha chain homology KEYWORDS ATP; endonuclease; hydrogen ion transport; hydrolase; !1nucleotide binding; P-loop; protein splicing; yeast vacuole FEATURE !$1-283,738-1071 #product H+-transporting ATPase chain A #status !8predicted #label MAT1\ !$1-283 #domain H+-transporting ATPase chain A extein 1 !8#status predicted #label XT1\ !$257-264 #region nucleotide-binding motif A (P-loop)\ !$284-737 #product DNA endonuclease PI-1 (ATPase intein) !8#status predicted #label MAT2\ !$734-918 #domain H+-transporting ATP synthase alpha chain !8homology #label ATP\ !$738-1071 #domain H+-transporting ATPase chain A extein 2 !8#status predicted #label XT2\ !$283-738 #cross-link peptide (Gly-Cys) #status experimental SUMMARY #length 1071 #molecular-weight 118636 #checksum 55 SEQUENCE /// ENTRY PXPZV9 #type complete TITLE H+-exporting ATPase (EC 3.6.3.6), vacuolar, 69K chain - carrot ALTERNATE_NAMES ATPase 69K polypeptide, vacuolar ORGANISM #formal_name Daucus carota #common_name carrot DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 03-Jun-2002 ACCESSIONS A28105; A35368 REFERENCE A28105 !$#authors Zimniak, L.; Dittrich, P.; Gogarten, J.P.; Kibak, H.; Taiz, !1L. !$#journal J. Biol. Chem. (1988) 263:9102-9112 !$#title The cDNA sequence of the 69-kDa subunit of the carrot !1vacuolar H(+)-ATPase. Homology to the beta-chain of !1F-0-F-1-ATPases. !$#cross-references MUID:88243787; PMID:2897965 !$#accession A28105 !'##molecule_type mRNA !'##residues 1-623 ##label ZIM !'##cross-references GB:J03769; NID:g167559; PIDN:AAA33139.1; !1PID:g167560 REFERENCE A35368 !$#authors Struve, I.; Rausch, T.; Bernasconi, P.; Taiz, L. !$#journal J. Biol. Chem. (1990) 265:7927-7932 !$#title Structure and function of the promoter of the carrot V-type !1H+-ATPase catalytic subunit gene. !$#cross-references MUID:90243663; PMID:2139875 !$#accession A35368 !'##molecule_type DNA !'##residues 1-39,'S',41-68 ##label STR !'##cross-references GB:J05429; NID:g167548; PIDN:AAA33135.1; !1PID:g553048 !'##note the authors translated the codon TCG for residue 40 as Ala GENETICS !$#introns 26/3 CLASSIFICATION #superfamily vacuolar H+-transporting ATPase 69K chain; !1H+-transporting ATP synthase alpha chain homology KEYWORDS ATP; hydrogen ion transport; hydrolase; nucleotide binding; !1P-loop FEATURE !$252-259 #region nucleotide-binding motif A (P-loop)\ !$275-460 #domain H+-transporting ATP synthase alpha chain !8homology #label ATP SUMMARY #length 623 #molecular-weight 68835 #checksum 5654 SEQUENCE /// ENTRY PXNCV7 #type complete TITLE H+-exporting ATPase (EC 3.6.3.6), vacuolar, 67K chain - Neurospora crassa ALTERNATE_NAMES vacuolar proton pump 67K chain ORGANISM #formal_name Neurospora crassa DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 03-Jun-2002 ACCESSIONS A30799; B30799 REFERENCE A30799 !$#authors Bowman, E.J.; Tenney, K.; Bowman, B.J. !$#journal J. Biol. Chem. (1988) 263:13994-14001 !$#title Isolation of genes encoding the Neurospora vacuolar ATPase. !1Analysis of vma-1 encoding the 67-kDa subunit reveals !1homology to other ATPases. !$#cross-references MUID:89008230; PMID:2971651 !$#accession A30799 !'##molecule_type DNA !'##residues 1-607 ##label BOW1 !'##cross-references GB:J03955; NID:g168925; PIDN:AAA33621.1; !1PID:g168926 !$#accession B30799 !'##molecule_type mRNA !'##residues 1-607 ##label BOW2 !'##cross-references GB:J03955; NID:g168925; PIDN:AAA33621.1; !1PID:g168926 GENETICS !$#gene vma1 !$#introns 3/3; 16/1; 23/2; 39/3; 68/1; 589/3 CLASSIFICATION #superfamily vacuolar H+-transporting ATPase 69K chain; !1H+-transporting ATP synthase alpha chain homology KEYWORDS ATP; hydrogen ion transport; hydrolase; nucleotide binding; !1P-loop FEATURE !$246-253 #region nucleotide-binding motif A (P-loop)\ !$269-453 #domain H+-transporting ATP synthase alpha chain !8homology #label ATP SUMMARY #length 607 #molecular-weight 67121 #checksum 6303 SEQUENCE /// ENTRY S14732 #type complete TITLE H+-transporting two-sector ATPase (EC 3.6.3.14) alpha chain [validated] - Halobacterium salinarum ORGANISM #formal_name Halobacterium salinarum DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 03-Jun-2002 ACCESSIONS S14732; S18498 REFERENCE S14732 !$#authors Ihara, K.; Mukohata, Y. !$#journal Arch. Biochem. Biophys. (1991) 286:111-116 !$#title The ATP synthase of Halobacterium salinarium (halobium) is !1an archaebacterial type as revealed from the amino acid !1sequences of its two major subunits. !$#cross-references MUID:91378275; PMID:1832829 !$#accession S14732 !'##molecule_type DNA !'##residues 1-585 ##label IHA !'##cross-references GB:X70294; GB:S56356; NID:g43639; PIDN:CAA49775.1; !1PID:g43640 !'##note the source is given as Halobacterium salinarium !$#accession S18498 !'##molecule_type protein !'##residues !1111-122;124-142;260-276;412-413;415-422;439-451;459-467; !1522-542;555-570 ##label IHA1 GENETICS !$#gene atpA COMPLEX atpA (PIR:S14732) and atpB (PIR:S14733) are the head piece !1of the ATP synthase in Halobacterium FUNCTION !$#description EC 3.6.3.14 [validated, PMID:9137827] !$#note the alpha chain is considered to be catalytic CLASSIFICATION #superfamily vacuolar H+-transporting ATPase 69K chain; !1H+-transporting ATP synthase alpha chain homology KEYWORDS ATP biosynthesis; hydrolase; membrane-associated complex; !1nucleotide binding; P-loop FEATURE !$235-242 #region nucleotide-binding motif A (P-loop)\ !$258-438 #domain H+-transporting ATP synthase alpha chain !8homology #label ATP\ !$241 #binding_site ATP (Lys) #status predicted SUMMARY #length 585 #molecular-weight 64104 #checksum 3642 SEQUENCE /// ENTRY PXBOV6 #type complete TITLE H+-exporting ATPase (EC 3.6.3.6), vacuolar, 16K chain - bovine ALTERNATE_NAMES vacuolar proton pump 16K proteolipid chain ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 03-Jun-2002 ACCESSIONS A31320; S05209 REFERENCE A31320 !$#authors Mandel, M.; Moriyama, Y.; Hulmes, J.D.; Pan, Y.C.E.; Nelson, !1H.; Nelson, N. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:5521-5524 !$#title cDNA sequence encoding the 16-kDa proteolipid of chromaffin !1granules implies gene duplication in the evolution of H !1(+)-ATPases. !$#cross-references MUID:88289753; PMID:2456571 !$#accession A31320 !'##molecule_type mRNA !'##residues 1-155 ##label MAN !'##cross-references GB:J03835 REFERENCE S05209 !$#authors Dermietzel, R.; Voelker, M.; Hwang, T.K.; Berzborn, R.J.; !1Meyer, H.E. !$#journal FEBS Lett. (1989) 253:1-5 !$#title A 16 kDa protein co-isolating with gap junctions from brain !1tissue belonging to the class of proteolipids of the !1vacuolar H+-ATPases. !$#cross-references MUID:89338721; PMID:2527163 !$#accession S05209 !'##molecule_type protein !'##residues 'X',8-26 ##label DER CLASSIFICATION #superfamily vacuolar H+-transporting ATPase 16K chain KEYWORDS ATP; hydrogen ion transport; hydrolase; transmembrane !1protein SUMMARY #length 155 #molecular-weight 15848 #checksum 5000 SEQUENCE /// ENTRY A39367 #type complete TITLE H+-exporting ATPase (EC 3.6.3.6) chain PKD1 - human ALTERNATE_NAMES vacuolar H+-transporting ATPase 16K chain ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS A39367; PH0847 REFERENCE A39367 !$#authors Gillespie, G.A.J.; Somlo, S.; Germino, G.G.; !1Weinstat-Saslow, D.; Reeders, S.T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:4289-4293 !$#title CpG island in the region of an autosomal dominant polycystic !1kidney disease locus defines the 5' end of a gene encoding a !1putative proton channel. !$#cross-references MUID:91239553; PMID:1709739 !$#accession A39367 !'##molecule_type mRNA !'##residues 1-155 ##label GIL !'##cross-references GB:M62762; NID:g189675; PIDN:AAA60039.1; !1PID:g189676 REFERENCE PH0847 !$#authors Hasebe, M.; Hanada, H.; Moriyama, Y.; Maeda, M.; Futai, M. !$#journal Biochem. Biophys. Res. Commun. (1992) 183:856-863 !$#title Vacuolar type H+-ATPase genes: presence of four genes !1including pseudogenes for the 16-kDa proteolipid subunit in !1the human genome. !$#cross-references MUID:92198482; PMID:1532310 !$#accession PH0847 !'##status preliminary !'##molecule_type DNA !'##residues 28-155 ##label HAS GENETICS !$#gene GDB:ATP6C; ATPL !'##cross-references GDB:128131 !$#map_position 16p13.3-16p13.3 CLASSIFICATION #superfamily vacuolar H+-transporting ATPase 16K chain KEYWORDS ATP; hydrogen ion transport; hydrolase; transmembrane !1protein SUMMARY #length 155 #molecular-weight 15736 #checksum 3284 SEQUENCE /// ENTRY JX0226 #type complete TITLE H+-exporting ATPase (EC 3.6.3.6) 16K chain, vacuolar - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS JX0226 REFERENCE JX0226 !$#authors Nezu, J.; Motojima, K.; Tamura, H.; Ohkuma, S. !$#journal J. Biochem. (1992) 112:212-219 !$#title Molecular cloning of a rat liver cDNA encoding the 16kDa !1subunit of vacuolar H+-ATPases: organellar and tissue !1distribution of 16kDa proteolipids. !$#cross-references MUID:93015781; PMID:1400263 !$#accession JX0226 !'##molecule_type mRNA !'##residues 1-155 ##label NEZ !'##cross-references GB:D10874; GB:D01244; NID:g220905; PIDN:BAA01643.1; !1PID:g1707357 !'##experimental_source liver CLASSIFICATION #superfamily vacuolar H+-transporting ATPase 16K chain KEYWORDS ATP; hydrogen ion transport; hydrolase; transmembrane !1protein SUMMARY #length 155 #molecular-weight 15808 #checksum 4130 SEQUENCE /// ENTRY S08261 #type complete TITLE H+-exporting ATPase (EC 3.6.3.6) 15K chain - marbled electric ray ALTERNATE_NAMES proteolipid, 15K ORGANISM #formal_name Torpedo marmorata #common_name marbled electric ray DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S08261 REFERENCE S08261 !$#authors Birman, S.; Meunier, F.M.; Lesbats, B.; le Caer, J.P.; !1Rossier, J.; Israel, M. !$#journal FEBS Lett. (1990) 261:303-306 !$#title A 15 kDa proteolipid found in mediatophore preparations from !1Torpedo electric organ presents high sequence homology with !1the bovine chromaffin granule protonophore. !$#cross-references MUID:90184466; PMID:2155824 !$#accession S08261 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-154 ##label BIR !'##cross-references GB:X52002; NID:g64412; PIDN:CAA36253.1; PID:g64413 !'##note part of this sequence was confirmed by protein sequencing CLASSIFICATION #superfamily vacuolar H+-transporting ATPase 16K chain KEYWORDS ATP; hydrogen ion transport; hydrolase; transmembrane !1protein SUMMARY #length 154 #molecular-weight 15511 #checksum 9344 SEQUENCE /// ENTRY PXBYL6 #type complete TITLE H+-exporting ATPase (EC 3.6.3.6) chain c.CUP5, vacuolar - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES H+-ATPase proteolipid subunit; H+-transporting ATPase lipid-binding protein; protein YEL027w ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 03-Jun-2002 ACCESSIONS S22257; S50432 REFERENCE S22257 !$#authors Nelson, H.; Nelson, N. !$#journal FEBS Lett. (1989) 247:147-153 !$#title The progenitor of ATP synthases was closely related to the !1current vacuolar H(+)-ATPase. !$#cross-references MUID:89211433; PMID:2540044 !$#accession S22257 !'##molecule_type DNA !'##residues 1-160 ##label NEL !'##cross-references EMBL:X15155; NID:g3405; PIDN:CAA33249.1; PID:g3406 REFERENCE S50428 !$#authors Dietrich, F.S. !$#submission submitted to the EMBL Data Library, December 1994 !$#description Saccharomyces cerevisiae chromosome V cosmids 9871, 8199, !19867, 9495 and lambda clones 6693 and 5898. !$#accession S50432 !'##molecule_type DNA !'##residues 1-160 ##label DIE !'##cross-references EMBL:U18530; NID:g602367; PIDN:AAB64504.1; !1PID:g602394; GSPDB:GN00005; MIPS:YEL027w GENETICS !$#gene SGD:CUP5; MIPS:YEL027w !'##cross-references SGD:S0000753; MIPS:YEL027w !$#map_position 5L CLASSIFICATION #superfamily vacuolar H+-transporting ATPase 16K chain KEYWORDS ATP; hydrogen ion transport; hydrolase; membrane-associated !1complex; transmembrane protein; yeast vacuole FEATURE !$7-23 #domain transmembrane #status predicted #label TM1\ !$58-74 #domain transmembrane #status predicted #label TM2\ !$95-111 #domain transmembrane #status predicted #label TM3\ !$125-141 #domain transmembrane #status predicted #label TM4 SUMMARY #length 160 #molecular-weight 16350 #checksum 525 SEQUENCE /// ENTRY S43893 #type complete TITLE H+-exporting ATPase (EC 3.6.3.6) lipid-binding protein - Neurospora crassa ORGANISM #formal_name Neurospora crassa DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S43893 REFERENCE S43893 !$#authors Sista, H.; Wechser, M.A.; Bowman, B.J. !$#journal Mol. Gen. Genet. (1994) 243:82-90 !$#title The proteolipid subunit of the Neurospora crassa vacuolar !1ATPase: isolation of the protein and the vma-3 gene. !$#cross-references MUID:94247360; PMID:8190074 !$#accession S43893 !'##status preliminary !'##molecule_type DNA !'##residues 1-161 ##label SIS !'##cross-references EMBL:L07105; NID:g168929; PIDN:AAA19974.1; !1PID:g168930 !'##note the authors translated the codon ATC for residue 63 as Tyr and !1GCT for residue 155 as Arg GENETICS !$#introns 5/2; 9/3; 53/1; 141/1 CLASSIFICATION #superfamily vacuolar H+-transporting ATPase 16K chain KEYWORDS ATP; hydrolase SUMMARY #length 161 #molecular-weight 16329 #checksum 3315 SEQUENCE /// ENTRY JN0456 #type complete TITLE H+-exporting ATPase (EC 3.6.3.6) 16K chain, vacuolar - tobacco hornworm ALTERNATE_NAMES H+-transporting ATPase, lipid-binding protein, vacuolar ORGANISM #formal_name Manduca sexta #common_name tobacco hornworm DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS JN0456; S19985 REFERENCE JN0456 !$#authors Dow, J.A.T.; Goodwin, S.F.; Kaiser, K. !$#journal Gene (1992) 122:355-360 !$#title Analysis of the gene encoding a 16-kDa proteolipid subunit !1of the vacuolar H+-ATPase from Manduca sexta midgut and !1tubules. !$#cross-references MUID:93138407; PMID:1283142 !$#accession JN0456 !'##molecule_type mRNA !'##residues 1-156 ##label DOW !'##cross-references EMBL:X65051; NID:g9730; PIDN:CAA46187.1; PID:g9731 CLASSIFICATION #superfamily vacuolar H+-transporting ATPase 16K chain KEYWORDS ATP; hydrogen ion transport; hydrolase; transmembrane !1protein SUMMARY #length 156 #molecular-weight 15978 #checksum 7841 SEQUENCE /// ENTRY S42878 #type complete TITLE H+-exporting ATPase (EC 3.6.3.6) 16K chain, vacuolar - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES ductin; H+-transporting ATPase chain c; H+-transporting ATPase proteolipid; vacuolar proton channel ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S42878; S13117 REFERENCE S42878 !$#authors Finbow, M.E.; Meagher, L.; Goodwin, S.; Lane, N.J.; Keen, !1J.; Findlay, J.B.C.; Kaiser, K. !$#submission submitted to the EMBL Data Library, January 1994 !$#description Functional and genetic analysis of ductin in insects- a !1putative component of the vacoular H+ -ATPase and gap !1junctions. !$#accession S42878 !'##molecule_type DNA !'##residues 1-159 ##label FIN !'##cross-references EMBL:X77936; NID:g457730; PIDN:CAA54908.1; !1PID:g457731 REFERENCE S13117 !$#authors Meagher, L.; McLean, P.; Finbow, M.E. !$#journal Nucleic Acids Res. (1990) 18:6712 !$#title Sequence of a cDNA from Drosophila coding for the 16kD !1proteolipid component of the vacuolar H(+)-ATPase. !$#cross-references MUID:91067485; PMID:2147478 !$#accession S13117 !'##molecule_type mRNA !'##residues 1-159 ##label MEA !'##cross-references EMBL:X55979; NID:g8811; PIDN:CAA39449.1; PID:g8812 GENETICS !$#gene FlyBase:Vha16 !'##cross-references FlyBase:FBgn0004145 !$#introns 29/1; 92/2 CLASSIFICATION #superfamily vacuolar H+-transporting ATPase 16K chain KEYWORDS ATP; hydrolase; transmembrane protein SUMMARY #length 159 #molecular-weight 16267 #checksum 5556 SEQUENCE /// ENTRY A40814 #type complete TITLE H+-exporting ATPase (EC 3.6.3.6) proteolipid chain, vacuolar - oat ORGANISM #formal_name Avena sativa #common_name oat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS A40814 REFERENCE A40814 !$#authors Lai, S.; Watson, J.C.; Hansen, J.N.; Sze, H. !$#journal J. Biol. Chem. (1991) 266:16078-16084 !$#title Molecular cloning and sequencing of cDNAs encoding the !1proteolipid subunit of the vacuolar H(+)-ATPase from a !1higher plant. !$#cross-references MUID:91340758; PMID:1831453 !$#accession A40814 !'##molecule_type mRNA !'##residues 1-165 ##label LAI !'##cross-references GB:M73232; NID:g166548; PIDN:AAA32712.1; !1PID:g166549 CLASSIFICATION #superfamily vacuolar H+-transporting ATPase 16K chain KEYWORDS ATP; hydrogen ion transport; hydrolase; transmembrane !1protein SUMMARY #length 165 #molecular-weight 16621 #checksum 6268 SEQUENCE /// ENTRY A42970 #type complete TITLE H+-exporting ATPase (EC 3.6.3.6) 95K chain, vacuolar - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein O5430c; protein YOR270c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS A42970; S67167; S67172; S72041 REFERENCE A42970 !$#authors Manolson, M.F.; Proteau, D.; Preston, R.A.; Stenbit, A.; !1Roberts, B.T.; Hoyt, M.A.; Preuss, D.; Mulholland, J.; !1Botstein, D.; Jones, E.W. !$#journal J. Biol. Chem. (1992) 267:14294-14303 !$#title The VPH1 gene encodes a 95-kDa integral membrane polypeptide !1required for in vivo assembly and activity of the yeast !1vacuolar H(+)-ATPase. !$#cross-references MUID:92332542; PMID:1385813 !$#accession A42970 !'##molecule_type DNA !'##residues 1-840 ##label MAN !'##cross-references GB:M89778; NID:g173172; PIDN:AAA35211.1; !1PID:g173173 !'##experimental_source strain X2180-1b; vacuolar !1acidification-defective mutants !'##note sequence extracted from NCBI backbone (NCBIN:108529, !1NCBIP:108530) REFERENCE S67143 !$#authors Jauniaux, J.C.; Poirey, R. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67167 !'##molecule_type DNA !'##residues 1-840 ##label JAU !'##cross-references EMBL:Z75178; NID:g1420605; PIDN:CAA99494.1; !1PID:g1420606; GSPDB:GN00015; MIPS:YOR270c !'##experimental_source strain S288C REFERENCE S67169 !$#authors Cheret, G.; Sor, F. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67172 !'##molecule_type DNA !'##residues 1-840 ##label CHE !'##cross-references EMBL:Z75178; NID:g1420605; PIDN:CAA99494.1; !1PID:g1420606; GSPDB:GN00015; MIPS:YOR270c !'##experimental_source strain S288C REFERENCE S72039 !$#authors Cheret, G.; Bernardi, A.; Sor, F. !$#journal Yeast (1996) 12:1059-1064 !$#title DNA sequence analysis of the VPH1-SNF2 region on chromosome !1XV of Saccharomyces cerevisiae. !$#cross-references MUID:97051594; PMID:8896271 !$#accession S72041 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-840 ##label CHW !'##cross-references EMBL:X89633; NID:g1279694; PIDN:CAA61776.1; !1PID:g1279697 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1995 GENETICS !$#gene SGD:VPH1; MIPS:YOR270c !'##cross-references MIPS:YOR270c; SGD:S0005796 !$#map_position 15R FUNCTION !$#description hydrogen ion transport; hydrolase; required for assembly and !1activity of the vacuolar ATPase; essential for vacuolar !1acidification and vacuolar H-ATPase activity CLASSIFICATION #superfamily vacuolar ATP synthase 95K chain KEYWORDS ATP; glycoprotein; hydrogen ion transport; hydrolase; !1membrane-associated complex; transmembrane protein; yeast !1vacuole FEATURE !$407-441 #domain transmembrane #status predicted #label TM1\ !$457-478 #domain transmembrane #status predicted #label TM2\ !$539-558 #domain transmembrane #status predicted #label TM3\ !$565-591 #domain transmembrane #status predicted #label TM4\ !$635-656 #domain transmembrane #status predicted #label TM5\ !$733-795 #domain transmembrane #status predicted #label TM6 SUMMARY #length 840 #molecular-weight 95528 #checksum 1196 SEQUENCE /// ENTRY PWECAK #type complete TITLE H+/K+-exchanging ATPase (EC 3.6.3.10) chain A [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES ATP phosphohydrolase (potassium-transporting) chain A; H+/ K+-transporting ATPase chain A; potassium-transporting ATPase chain A ORGANISM #formal_name Escherichia coli DATE 13-Aug-1986 #sequence_revision 31-Dec-1989 #text_change 19-Apr-2002 ACCESSIONS A01071; A64805; T48909 REFERENCE A93999 !$#authors Hesse, J.E.; Wieczorek, L.; Altendorf, K.; Reicin, A.S.; !1Dorus, E.; Epstein, W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:4746-4750 !$#title Sequence homology between two membrane transport ATPases, !1the Kdp-ATPase of Escherichia coli and the Ca(2+)-ATPase of !1sarcoplasmic reticulum. !$#cross-references MUID:84272710; PMID:6146979 !$#accession A01071 !'##molecule_type DNA !'##residues 1-557 ##label HES !'##cross-references GB:K02670; NID:g2772547; PIDN:AAB96335.1; !1PID:g146547 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64805 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-557 ##label BLAT !'##cross-references GB:AE000173; GB:U00096; NID:g1786910; !1PIDN:AAC73792.1; PID:g1786915; UWGP:b0698 !'##experimental_source strain K-12, substrain MG1655 REFERENCE Z25006 !$#authors Oshima, T.; Aiba, H.; Baba, T.; Fujita, K.; Hayashi, K.; !1Honjo, A.; Ikemoto, K.; Inada, T.; Itoh, T.; Kajihara, M.; !1Kanai, K.; Kashimoto, K.; Kimura, S.; Kitagawa, M.; Makino, !1K.; Masuda, S.; Miki, T.; Mizobuchi, K.; Mori, H.; Motomura, !1K.; Nakamura, Y.; Nashimoto, H.; Nishio, Y.; Saito, N.; !1Sampei, G.; Seki, Y.; Tagami, H.; Takemoto, K.; Wada, C.; !1Yamamoto, Y.; Yano, M.; Horiuchi, T. !$#journal DNA Res. (1996) 3:137-155 !$#title A 718-kb DNA Sequence of Escherichia coli K-12 Genome !1Corresponding to the 12.7-28.0 min Region on the Linkage !1Map. !$#cross-references MUID:97061202; PMID:8905232 !$#accession T48909 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-557 ##label OSH !'##cross-references EMBL:D90709; NID:g1651305; PIDN:BAA35356.1; !1PID:g1651307 !'##experimental_source strain K12; Kohara clone 174 GENETICS !$#gene kdpA !$#map_position 15.7-16.0 !$#note transcription unit kdpFABC [validated, MUID:20076462] COMPLEX oligomer; two alpha chains (PIR:PWECAK), two beta chains !1(PIR:PWECBK), two gamma chains (PIR:PWECCK) and probably one !1kdpF chain (PIR:T48910) [validated, MUID:99077600] FUNCTION CPLX !$#description EC 3.6.3.10 [validated, MUID:99077600]; catalyzes the !1hydrolysis of ATP coupled with the exchange of hydrogen and !1potassium ions FUNCTION CHA !$#description chain A is responsible for binding and transport of K+ !1[validated, MUID:95204461] CLASSIFICATION #superfamily H+/K+-transporting ATPase chain A KEYWORDS ATP; hydrolase; potassium transport; transmembrane protein FEATURE !$3-19 #domain transmembrane #status predicted #label TM1\ !$66-82 #domain transmembrane #status predicted #label TM2\ !$138-154 #domain transmembrane #status predicted #label TM3\ !$173-189 #domain transmembrane #status predicted #label TM4\ !$253-269 #domain transmembrane #status predicted #label TM5\ !$282-298 #domain transmembrane #status predicted #label TM6\ !$334-350 #domain transmembrane #status predicted #label TM7\ !$382-398 #domain transmembrane #status predicted #label TM8\ !$418-434 #domain transmembrane #status predicted #label TM9\ !$484-500 #domain transmembrane #status predicted #label TM10\ !$528-544 #domain transmembrane #status predicted #label TM11 SUMMARY #length 557 #molecular-weight 59189 #checksum 7907 SEQUENCE /// ENTRY PWECBK #type complete TITLE H+/K+-exchanging ATPase (EC 3.6.3.10) chain B [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES ATP phosphohydrolase (potassium-transporting) chain B; H+/ K+-transporting ATPase chain B; potassium-transporting ATPase chain B ORGANISM #formal_name Escherichia coli DATE 13-Aug-1986 #sequence_revision 31-Oct-1997 #text_change 19-Apr-2002 ACCESSIONS H64804; A01072; T48908 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64804 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-682 ##label BLAT !'##cross-references GB:AE000173; GB:U00096; NID:g1786910; !1PIDN:AAC73791.1; PID:g1786914; UWGP:b0697 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A93999 !$#authors Hesse, J.E.; Wieczorek, L.; Altendorf, K.; Reicin, A.S.; !1Dorus, E.; Epstein, W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:4746-4750 !$#title Sequence homology between two membrane transport ATPases, !1the Kdp-ATPase of Escherichia coli and the Ca(2+)-ATPase of !1sarcoplasmic reticulum. !$#cross-references MUID:84272710; PMID:6146979 !$#accession A01072 !'##molecule_type DNA !'##residues 1-110,'DA',113-273,'SA',276-455,'A',457-682 ##label HES REFERENCE Z25006 !$#authors Oshima, T.; Aiba, H.; Baba, T.; Fujita, K.; Hayashi, K.; !1Honjo, A.; Ikemoto, K.; Inada, T.; Itoh, T.; Kajihara, M.; !1Kanai, K.; Kashimoto, K.; Kimura, S.; Kitagawa, M.; Makino, !1K.; Masuda, S.; Miki, T.; Mizobuchi, K.; Mori, H.; Motomura, !1K.; Nakamura, Y.; Nashimoto, H.; Nishio, Y.; Saito, N.; !1Sampei, G.; Seki, Y.; Tagami, H.; Takemoto, K.; Wada, C.; !1Yamamoto, Y.; Yano, M.; Horiuchi, T. !$#journal DNA Res. (1996) 3:137-155 !$#title A 718-kb DNA Sequence of Escherichia coli K-12 Genome !1Corresponding to the 12.7-28.0 min Region on the Linkage !1Map. !$#cross-references MUID:97061202; PMID:8905232 !$#accession T48908 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-74 ##label OSH !'##cross-references EMBL:D90709; GB:AB001340; NID:g1651305; !1PIDN:BAA35355.1; PID:g1651306 !'##experimental_source strain K12; Kohara clone 174 GENETICS !$#gene kdpB !$#map_position 15.7-16.0 !$#note transcription unit kdpFABC [validated, MUID:20076462] COMPLEX oligomer; two alpha chains (see PIR:PWECAK), two beta chains !1(see PIR:PWECBK), two gamma chains (see PIR:PWECCK) and !1probably one kdpF chain (see PIR:T48910) [validated, !1MUID:99077600] FUNCTION CPLX !$#description EC 3.6.3.10 [validated, MUID:99077600]; catalyzes the !1hydrolysis of ATP coupled with the exchange of hydrogen and !1potassium ions FUNCTION CHB !$#description chain B is the catalytic chain, responsible for energy !1coupling; [validated, MUID:93116589] CLASSIFICATION #superfamily H+/K+-transporting ATPase chain B; ATPase !1nucleotide-binding domain homology KEYWORDS ATP; hydrolase; phosphoprotein; potassium transport; !1transmembrane protein FEATURE !$35-51 #domain transmembrane #status predicted #label TM1\ !$62-78 #domain transmembrane #status predicted #label TM2\ !$219-235 #domain transmembrane #status predicted #label TM3\ !$249-265 #domain transmembrane #status predicted #label TM4\ !$441-583 #domain ATPase nucleotide-binding domain homology !8#label ATN\ !$616-632 #domain transmembrane #status predicted #label TM5\ !$662-678 #domain transmembrane #status predicted #label TM6 SUMMARY #length 682 #molecular-weight 72198 #checksum 8158 SEQUENCE /// ENTRY PWECCK #type complete TITLE H+/K+-exchanging ATPase (EC 3.6.3.10) chain C [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES ATP phosphohydrolase (potassium-transporting) chain C; H+/ K+-transporting ATPase chain C; potassium-transporting ATPase chain C ORGANISM #formal_name Escherichia coli DATE 13-Aug-1986 #sequence_revision 13-Aug-1986 #text_change 19-Apr-2002 ACCESSIONS A01073; A42372; G64804 REFERENCE A93999 !$#authors Hesse, J.E.; Wieczorek, L.; Altendorf, K.; Reicin, A.S.; !1Dorus, E.; Epstein, W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:4746-4750 !$#title Sequence homology between two membrane transport ATPases, !1the Kdp-ATPase of Escherichia coli and the Ca(2+)-ATPase of !1sarcoplasmic reticulum. !$#cross-references MUID:84272710; PMID:6146979 !$#accession A01073 !'##molecule_type DNA !'##residues 1-190 ##label HES !'##cross-references GB:K02670; NID:g2772547; PIDN:AAB96337.1; !1PID:g146549 REFERENCE A42372 !$#authors Walderhaug, M.O.; Polarek, J.W.; Voelkner, P.; Daniel, J.M.; !1Hesse, J.E.; Altendorf, K.; Epstein, W. !$#journal J. Bacteriol. (1992) 174:2152-2159 !$#title KdpD and KdpE, proteins that control expression of the !1kdpABC operon, are members of the two-component !1sensor-effector class of regulators. !$#cross-references MUID:92202141; PMID:1532388 !$#accession A42372 !'##molecule_type DNA !'##residues 143-190 ##label WAL !'##cross-references GB:M36066 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64804 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-190 ##label BLAT !'##cross-references GB:AE000173; GB:U00096; NID:g1786910; !1PIDN:AAC73790.1; PID:g1786913; UWGP:b0696 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene kdpC !$#map_position 16 min !$#note transcription unit kdpFABC [validated, MUID:20076462] COMPLEX oligomer; two alpha chains (PIR:PWECAK), two beta chains !1(PIR:PWECBK), two gamma chains (PIR:PWECCK) and probably one !1kdpF chain (PIR:T48910) [validated, MUID:99077600] FUNCTION CPLX !$#description EC 3.6.3.10 [validated, MUID:99077600]; catalyzes the !1hydrolysis of ATP coupled with the exchange of hydrogen and !1potassium ions FUNCTION CHC !$#description forms strong interactions with the KdpA chain, serving to !1assemble and stabilize the high affinity ATP-driven !1K+-transport system (kdpFABC complex) [validated, !1MUID:99077600] CLASSIFICATION #superfamily H+/K+-transporting ATPase chain C KEYWORDS ATP; hydrolase; inner membrane; potassium transport; !1transmembrane protein FEATURE !$12-28 #domain transmembrane #status predicted #label TMM SUMMARY #length 190 #molecular-weight 20267 #checksum 2878 SEQUENCE /// ENTRY S00801 #type complete TITLE Na+/K+-exchanging ATPase (EC 3.6.3.9) alpha-3 chain - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 19-Apr-2002 ACCESSIONS S00801; S04019; A27397; S02275 REFERENCE S00801 !$#authors Ovchinnikov, Y.A.; Monastyrskaya, G.S.; Broude, N.E.; !1Ushkaryov, Y.A.; Melkov, A.M.; Smirnov, Y.V.; Malyshev, !1I.V.; Allikmets, R.L.; Kostina, M.B.; Dulubova, I.E.; !1Kiyatkin, N.I.; Grishin, A.V.; Modyanov, N.N.; Sverdlov, !1E.D. !$#journal FEBS Lett. (1988) 233:87-94 !$#title Family of human Na,K-ATPase genes. Structure of the gene for !1the catalytic subunit (alpha-III-form) and its relationship !1with structural features of the protein. !$#cross-references MUID:88255304; PMID:2838329 !$#accession S00801 !'##molecule_type DNA !'##residues 1-1013 ##label OVC !'##cross-references EMBL:M37456 REFERENCE S04019 !$#authors Sverdlov, E.D.; Monastyrskaya, G.S.; Broude, N.E.; Ushkarev, !1Y.A.; Melkov, A.M.; Smirnov, Y.V.; Malyshev, I.V.; !1Allikmets, R.L.; Kostina, M.B.; Dulubova, I.E.; Kiyatkin, !1N.I.; Grishin, A.V.; Modyanov, N.N.; Ovchinnikov, Y.A. !$#journal Dokl. Biochem. (1987) 297:426-431 !$#title Family of human Na(+),K(+)-ATPase genes. Structure of the !1gene of isoform alpha-III. !$#accession S04019 !'##molecule_type DNA !'##residues 1,'EIH',3-1013 ##label SVE1 !'##cross-references EMBL:X12910; NID:g28963 !'##note the authors translated the codon TTC for residue 283 as Ser and !1TCT for residue 986 as Phe; the sequence shown follows the !1authors' translation at position 986 !'##note this paper is a translation of the Russian paper published in !1Dokl. Akad. Nauk SSSR (1987) 297: 1488-1494 REFERENCE A27397 !$#authors Sverdlov, E.D.; Monastyrskaya, G.S.; Broude, N.E.; !1Ushkaryov, Y.A.; Allikmets, R.L.; Melkov, A.M.; Smirnov, !1Y.V.; Malyshev, I.V.; Dulobova, I.E.; Petrukhin, K.E.; !1Grishin, A.V.; Kijatkin, N.I.; Kostina, M.B.; Sverdlov, !1V.E.; Modyanov, N.N.; Ovchnikov, Y.A. !$#journal FEBS Lett. (1987) 217:275-278 !$#title The family of human Na+,K+-ATPase genes. No less than five !1genes and/or pseudogenes related to the alpha-subunit. !$#cross-references MUID:87247232; PMID:3036582 !$#accession A27397 !'##molecule_type mRNA !'##residues 243-434 ##label SVE2 !'##cross-references GB:M27570 GENETICS !$#gene GDB:ATP1A3 !'##cross-references GDB:119713; OMIM:182350 !$#map_position 19q13.2-19q13.2 !$#introns 2/3; 31/3; 51/3; 119/3; 157/3; 202/3; 242/1; 331/3; 398/1; !1435/2; 479/3; 544/1; 602/3; 648/2; 698/3; 755/1; 806/3; 848/ !11; 896/3; 940/2; 974/2; 1005/1 CLASSIFICATION #superfamily Na+/K+-transporting ATPase alpha chain; ATPase !1nucleotide-binding domain homology KEYWORDS ATP; heterodimer; hydrolase; ion transport; phosphoprotein; !1potassium transport; sodium transport; transmembrane protein FEATURE !$86-110 #domain transmembrane #status predicted #label TM1\ !$120-139 #domain transmembrane #status predicted #label TM2\ !$140-280 #domain intracellular #status predicted #label INT2\ !$281-303 #domain transmembrane #status predicted #label TM3\ !$310-338 #domain transmembrane #status predicted #label TM4\ !$339-776 #domain intracellular #status predicted #label INT3\ !$577-773 #domain ATPase nucleotide-binding domain homology !8#label ATN\ !$777-800 #domain transmembrane #status predicted #label TM5\ !$839-864 #domain transmembrane #status predicted #label TM6\ !$865-942 #domain intracellular #status predicted #label INT4\ !$943-968 #domain transmembrane #status predicted #label TM7\ !$969-1013 #domain extracellular #status predicted #label EXT\ !$366 #active_site Asp (aspartylphosphate intermediate) !8#status predicted\ !$498 #binding_site ATP (Lys) #status predicted\ !$707,711,716 #active_site Asp, Asp, Lys #status predicted SUMMARY #length 1013 #molecular-weight 111691 #checksum 3550 SEQUENCE /// ENTRY A24639 #type complete TITLE Na+/K+-exchanging ATPase (EC 3.6.3.9) alpha-1 chain [validated] - rat ALTERNATE_NAMES Na+/K+-transporting ATPase alpha chain, kidney-type CONTAINS Na+/K+-transporting ATPase alpha-S chain ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 18-Aug-2000 #sequence_revision 18-Aug-2000 #text_change 19-Apr-2002 ACCESSIONS A24639; S00460; A27180; S11020; A25171; S29877; S10758 REFERENCE A90512 !$#authors Shull, G.E.; Greeb, J.; Lingrel, J.B. !$#journal Biochemistry (1986) 25:8125-8132 !$#title Molecular cloning of three distinct forms of the Na+, !1K+-ATPase alpha-subunit from rat brain. !$#cross-references MUID:87128908; PMID:3028470 !$#accession A24639 !'##molecule_type mRNA !'##residues 1-1023 ##label SHU !'##cross-references EMBL:M14511; NID:g203026; PIDN:AAA40775.1; !1PID:g203027 REFERENCE S00460 !$#authors Hara, Y.; Urayama, O.; Kawakami, K.; Nojima, H.; Nagamune, !1H.; Kojima, T.; Ohta, T.; Nagano, K.; Nakao, M. !$#journal J. Biochem. (1987) 102:43-58 !$#title Primary structures of two types of alpha-subunit of rat !1brain Na(+),K(+)-ATPase deduced from cDNA sequences. !$#cross-references MUID:88032933; PMID:2822682 !$#accession S00460 !'##molecule_type mRNA !'##residues 1-1023 ##label HAR !'##cross-references EMBL:X05882; NID:g55771; PIDN:CAA29306.1; !1PID:g55772 REFERENCE A92749 !$#authors Herrera, V.L.M.; Emanuel, J.R.; Ruiz-Opazo, N.; Levenson, !1R.; Nadal-Ginard, B. !$#journal J. Cell Biol. (1987) 105:1855-1865 !$#title Three differentially expressed Na,K-ATPase alpha subunit !1isoforms: structural and functional implications. !$#cross-references MUID:88033255; PMID:2822726 !$#accession A27180 !'##molecule_type mRNA !'##residues 1-67,'PV',70-174,'E',176-187,'V',189-334,'V',336-1023 !1##label HER !'##cross-references EMBL:M28647; NID:g205631; PIDN:AAA41671.1; !1PID:g205632 REFERENCE S11020 !$#authors Yagawa, Y.; Kawakami, K.; Nagano, K. !$#journal Biochim. Biophys. Acta (1990) 1049:286-292 !$#title Cloning and analysis of the 5'-flanking region of rat Na(+)/ !1K(+)-ATPase alpha-1 subunit gene. !$#cross-references MUID:90344872; PMID:2166579 !$#accession S11020 !'##status translation not shown !'##molecule_type DNA !'##residues 1-41 ##label YAG !'##cross-references EMBL:X53233 REFERENCE A25171 !$#authors Schneider, J.W.; Mercer, R.W.; Caplan, M.; Emanuel, J.R.; !1Sweadner, K.J.; Benz Jr., E.J.; Levenson, R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:6357-6361 !$#title Molecular cloning of rat brain Na,K-ATPase alpha-subunit !1cDNA. !$#cross-references MUID:85298352; PMID:2994074 !$#accession A25171 !'##molecule_type mRNA !'##residues 489-533 ##label SCH REFERENCE S29877 !$#authors Lytton, J. !$#journal Biochem. Biophys. Res. Commun. (1985) 132:764-769 !$#title The catalytic subunits of the (Na(+), K(+))-ATPase alpha and !1alpha(+) isozymes are the products of different genes. !$#cross-references MUID:86050667; PMID:2998384 !$#accession S29877 !'##status preliminary !'##molecule_type protein !'##residues 6-19 ##label LYT REFERENCE S10758 !$#authors Kurihara, K.; Hosoi, K.; Kodama, A.; Ueha, T. !$#journal Biochim. Biophys. Acta (1990) 1039:234-240 !$#title A new electrophoretic variant of alpha subunit of Na(+)/K !1(+)-ATPase from the submandibular gland of rats. !$#cross-references MUID:90304196; PMID:2163680 !$#accession S10758 !'##molecule_type protein !'##residues 6,'X',8-10,'X',12-16 ##label KUR !'##experimental_source submandibular gland !'##note designated alpha-S form; thought to arise from alpha-1 chain by !1post-translational modification GENETICS !$#gene NKAA1 !$#introns 4/3 !$#note the list of introns may be incomplete CLASSIFICATION #superfamily Na+/K+-transporting ATPase alpha chain; ATPase !1nucleotide-binding domain homology KEYWORDS ATP; heterodimer; hydrolase; ion transport; phosphoprotein; !1potassium transport; sodium transport; transmembrane protein FEATURE !$6-1023 #product Na+/K+-transporting ATPase alpha-1 chain !8#status experimental #label MAT\ !$6-95 #domain intracellular #status predicted #label INT1\ !$96-120 #domain transmembrane #status predicted #label TM1\ !$130-149 #domain transmembrane #status predicted #label TM2\ !$150-290 #domain intracellular #status predicted #label INT2\ !$291-313 #domain transmembrane #status predicted #label TM3\ !$320-348 #domain transmembrane #status predicted #label TM4\ !$349-786 #domain intracellular #status predicted #label INT3\ !$587-783 #domain ATPase nucleotide-binding domain homology !8#label ATN\ !$787-810 #domain transmembrane #status predicted #label TM5\ !$849-874 #domain transmembrane #status predicted #label TM6\ !$875-952 #domain intracellular #status predicted #label INT4\ !$953-978 #domain transmembrane #status predicted #label TM7\ !$979-1023 #domain extracellular #status predicted #label EXT\ !$376 #active_site Asp (aspartylphosphate intermediate) !8#status predicted\ !$508 #binding_site ATP (Lys) #status predicted\ !$717,721,726 #active_site Asp, Asp, Lys #status predicted SUMMARY #length 1023 #molecular-weight 113053 #checksum 5607 SEQUENCE /// ENTRY S04630 #type complete TITLE Na+/K+-exchanging ATPase (EC 3.6.3.9) alpha-1 chain - horse ORGANISM #formal_name Equus caballus #common_name domestic horse DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 19-Apr-2002 ACCESSIONS S04630 REFERENCE S04630 !$#authors Kano, I.; Nagai, F.; Satoh, K.; Ushiyama, K.; Nakao, T.; !1Kano, K. !$#journal FEBS Lett. (1989) 250:91-98 !$#title Structure of the alpha(1) subunit of horse Na,K-ATPase gene. !$#cross-references MUID:89290042; PMID:2544461 !$#accession S04630 !'##molecule_type DNA !'##residues 1-1021 ##label KAN !'##cross-references EMBL:X16773; NID:g1010; PIDN:CAA34716.1; !1PID:g871026 GENETICS !$#introns 4/3; 39/3; 59/3; 127/3; 165/3; 210/3; 250/1; 339/3; 406/1; !1442/3; 487/3; 552/1; 610/3; 656/2; 706/3; 763/1; 814/3; 856/ !11; 904/3; 948/2; 982/2; 1013/1 CLASSIFICATION #superfamily Na+/K+-transporting ATPase alpha chain; ATPase !1nucleotide-binding domain homology KEYWORDS ATP; heterodimer; hydrolase; ion transport; phosphoprotein; !1potassium transport; sodium transport; transmembrane protein FEATURE !$6-1021 #product Na+/K+-transporting ATPase alpha-1 chain !8#status predicted #label MAT\ !$6-93 #domain intracellular #status predicted #label INT1\ !$94-118 #domain transmembrane #status predicted #label TM1\ !$128-147 #domain transmembrane #status predicted #label TM2\ !$148-288 #domain intracellular #status predicted #label INT2\ !$289-311 #domain transmembrane #status predicted #label TM3\ !$318-346 #domain transmembrane #status predicted #label TM4\ !$347-784 #domain intracellular #status predicted #label INT3\ !$585-781 #domain ATPase nucleotide-binding domain homology !8#label ATN\ !$785-808 #domain transmembrane #status predicted #label TM5\ !$847-872 #domain transmembrane #status predicted #label TM6\ !$873-950 #domain intracellular #status predicted #label INT4\ !$951-976 #domain transmembrane #status predicted #label TM7\ !$977-1021 #domain extracellular #status predicted #label EXT\ !$374 #active_site Asp (aspartylphosphate intermediate) !8#status predicted\ !$506 #binding_site ATP (Lys) #status predicted\ !$715,719,724 #active_site Asp, Asp, Lys #status predicted SUMMARY #length 1021 #molecular-weight 112696 #checksum 6699 SEQUENCE /// ENTRY PWSHNA #type complete TITLE Na+/K+-exchanging ATPase (EC 3.6.3.9) alpha chain precursor - sheep ALTERNATE_NAMES sodium pump alpha chain; sodium/potassium-dependent ATPase alpha chain; sodium/potassium-transporting ATPase alpha chain ORGANISM #formal_name Ovis orientalis aries, Ovis ammon aries #common_name domestic sheep DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 19-Apr-2002 ACCESSIONS A01074; A35426 REFERENCE A01074 !$#authors Shull, G.E.; Schwartz, A.; Lingrel, J.B. !$#journal Nature (1985) 316:691-695 !$#title Amino-acid sequence of the catalytic subunit of the (Na(+)+K !1(+)) ATPase deduced from a complementary DNA. !$#cross-references MUID:85296299; PMID:2993903 !$#accession A01074 !'##molecule_type mRNA !'##residues 1-1021 ##label SHU !'##cross-references GB:X02813; NID:g1205; PIDN:CAA26581.1; PID:g1206 REFERENCE A35426 !$#authors Hinz, H.R.; Kirley, T.L. !$#journal J. Biol. Chem. (1990) 265:10260-10265 !$#title Lysine 480 is an essential residue in the putative ATP site !1of lamb kidney (Na,K)-ATPase. Identification of the !1pyridoxal 5'-diphospho-5'-adenosine and pyridoxal phosphate !1reactive residue. !$#cross-references MUID:90285144; PMID:2162343 !$#accession A35426 !'##status preliminary !'##molecule_type protein !'##residues 475-492 ##label HIN COMMENT This is the catalytic component of the active enzyme, which !1catalyzes the hydrolysis of ATP coupled with the exchange of !1sodium and potassium ions across the plasma membrane. This !1action creates the electrochemical gradient of sodium and !1potassium, providing the energy for active transport of !1various nutrients. The other component (beta chain) of the !1enzyme is a glycoprotein of unknown function. COMMENT This enzyme is specifically inhibited by cardiac glycosides !1such as digoxin or ouabain. CLASSIFICATION #superfamily Na+/K+-transporting ATPase alpha chain; ATPase !1nucleotide-binding domain homology KEYWORDS ATP; hydrolase; phosphoprotein; potassium transport; sodium !1transport; transmembrane protein FEATURE !$6-1021 #product Na+/K+-transporting ATPase alpha chain !8#status predicted #label MAT\ !$94-115 #domain transmembrane #status predicted #label TM1\ !$128-144 #domain transmembrane #status predicted #label TM2\ !$289-311 #domain transmembrane #status predicted #label TM3\ !$318-346 #domain transmembrane #status predicted #label TM4\ !$585-781 #domain ATPase nucleotide-binding domain homology !8#label ATN\ !$785-808 #domain transmembrane #status predicted #label TM5\ !$847-872 #domain transmembrane #status predicted #label TM6\ !$951-976 #domain transmembrane #status predicted #label TM7\ !$315 #binding_site cardiac glycoside (Trp) #status !8predicted\ !$374 #active_site Asp (aspartylphosphate intermediate) !8#status predicted\ !$506 #binding_site ATP (Lys) #status predicted SUMMARY #length 1021 #molecular-weight 112657 #checksum 5126 SEQUENCE /// ENTRY PWCCNM #type complete TITLE Na+/K+-exchanging ATPase (EC 3.6.3.9) alpha chain - white sucker ORGANISM #formal_name Catostomus commersoni #common_name white sucker DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-Apr-2002 ACCESSIONS S14740 REFERENCE S14740 !$#authors Schoenrock, C.; Morley, S.D.; Okawara, Y.; Lederis, K.; !1Richter, D. !$#journal Biol. Chem. Hoppe-Seyler (1991) 372:279-286 !$#title Sodium and potassium ATPase of the teleost fish Catostomus !1commersoni. Sequence, protein structure and evolutionary !1conservation of the alpha-subunit. !$#cross-references MUID:91282983; PMID:1711856 !$#accession S14740 !'##molecule_type mRNA !'##residues 1-1027 ##label SCH !'##cross-references EMBL:X58629; NID:g62641; PIDN:CAA41483.1; !1PID:g62642 CLASSIFICATION #superfamily Na+/K+-transporting ATPase alpha chain; ATPase !1nucleotide-binding domain homology KEYWORDS ATP; hydrolase; ion transport; phosphoprotein; potassium !1transport; sodium transport; transmembrane protein FEATURE !$99-124 #domain transmembrane #status predicted #label TM1\ !$133-152 #domain transmembrane #status predicted #label TM2\ !$153-293 #domain intracellular #status predicted #label INT2\ !$294-316 #domain transmembrane #status predicted #label TM3\ !$323-351 #domain transmembrane #status predicted #label TM4\ !$352-790 #domain intracellular #status predicted #label INT3\ !$591-787 #domain ATPase nucleotide-binding domain homology !8#label ATN\ !$791-814 #domain transmembrane #status predicted #label TM5\ !$853-878 #domain transmembrane #status predicted #label TM6\ !$879-956 #domain intracellular #status predicted #label INT4\ !$957-982 #domain transmembrane #status predicted #label TM7\ !$983-1027 #domain extracellular #status predicted #label EXT\ !$379 #active_site Asp (aspartylphosphate intermediate) !8#status predicted\ !$512 #binding_site ATP (Lys) #status predicted\ !$721,725,730 #active_site Asp, Asp, Lys #status predicted SUMMARY #length 1027 #molecular-weight 113312 #checksum 4660 SEQUENCE /// ENTRY S24650 #type complete TITLE Na+/K+-exchanging ATPase (EC 3.6.3.9) alpha-1 chain - giant toad ORGANISM #formal_name Bufo marinus #common_name giant toad DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 19-Apr-2002 ACCESSIONS A43451; S24650 REFERENCE A43451 !$#authors Jaisser, F.; Canessa, C.M.; Horisberger, J.D.; Rossier, B.C. !$#journal J. Biol. Chem. (1992) 267:16895-16903 !$#title Primary sequence and functional expression of a novel !1ouabain-resistant Na,K-ATPase. The beta subunit modulates !1potassium activation of the Na,K-pump. !$#cross-references MUID:92380991; PMID:1380956 !$#accession A43451 !'##status preliminary !'##molecule_type mRNA !'##residues 1-1023 ##label JAI !'##cross-references EMBL:Z11798; NID:g62491; PIDN:CAA77842.1; !1PID:g62492 !'##experimental_source urinary bladder cell line TBM 18-23 !'##note submitted to the EMBL Data Library, March 1992 !'##note sequence extracted from NCBI backbone (NCBIP:111876) CLASSIFICATION #superfamily Na+/K+-transporting ATPase alpha chain; ATPase !1nucleotide-binding domain homology KEYWORDS ATP; heterodimer; hydrolase; ion transport; phosphoprotein; !1potassium transport; sodium transport; transmembrane protein FEATURE !$6-1023 #product Na+/K+-transporting ATPase alpha-1 chain !8#status predicted #label MAT\ !$6-95 #domain intracellular #status predicted #label INT1\ !$96-120 #domain transmembrane #status predicted #label TM1\ !$130-149 #domain transmembrane #status predicted #label TM2\ !$150-290 #domain intracellular #status predicted #label INT2\ !$291-313 #domain transmembrane #status predicted #label TM3\ !$320-348 #domain transmembrane #status predicted #label TM4\ !$349-786 #domain intracellular #status predicted #label INT3\ !$587-783 #domain ATPase nucleotide-binding domain homology !8#label ATN\ !$787-810 #domain transmembrane #status predicted #label TM5\ !$849-874 #domain transmembrane #status predicted #label TM6\ !$875-952 #domain intracellular #status predicted #label INT4\ !$953-978 #domain transmembrane #status predicted #label TM7\ !$979-1023 #domain extracellular #status predicted #label EXT\ !$376 #active_site Asp (aspartylphosphate intermediate) !8#status predicted\ !$508 #binding_site ATP (Lys) #status predicted\ !$717,721,726 #active_site Asp, Asp, Lys #status predicted SUMMARY #length 1023 #molecular-weight 112599 #checksum 2209 SEQUENCE /// ENTRY S00503 #type complete TITLE Na+/K+-exchanging ATPase (EC 3.6.3.9) alpha chain - Pacific electric ray ORGANISM #formal_name Torpedo californica #common_name Pacific electric ray DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 19-Apr-2002 ACCESSIONS S00503; S28885; S29880 REFERENCE S00503 !$#authors Kawakami, K.; Noguchi, S.; Noda, M.; Takahashi, H.; Ohta, !1T.; Kawamura, M.; Nojima, H.; Nagano, K.; Hirose, T.; !1Inayama, S.; Hayashida, H.; Miyata, T.; Numa, S. !$#journal Nature (1985) 316:733-736 !$#title Primary structure of the alpha-subunit of Torpedo !1californica (Na(+)+K(+))ATPase deduced from cDNA sequence. !$#cross-references MUID:85296307; PMID:2993905 !$#accession S00503 !'##molecule_type mRNA !'##residues 1-1022 ##label KAW1 !'##cross-references EMBL:X02810; NID:g64399; PIDN:CAA26578.1; !1PID:g64400 !$#accession S28885 !'##molecule_type protein !'##residues 228-240;431-438;535-550;671-690;1011-1022 ##label KAW2 REFERENCE S29880 !$#authors Ohta, T.; Nagano, K.; Yoshida, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:2071-2075 !$#title The active site structure of Na(+)/K(+)-transporting ATPase: !1location of the 5'-(p-fluorosulfonyl)benzoyladenosine !1binding site and soluble peptides released by trypsin. !$#cross-references MUID:86177549; PMID:3008150 !$#accession S29880 !'##molecule_type protein !'##residues 386-402;502-512;671-689;887-906 ##label OHT CLASSIFICATION #superfamily Na+/K+-transporting ATPase alpha chain; ATPase !1nucleotide-binding domain homology KEYWORDS ATP; heterodimer; hydrolase; ion transport; phosphoprotein; !1potassium transport; sodium transport; transmembrane protein FEATURE !$96-120 #domain transmembrane #status predicted #label TM1\ !$130-149 #domain transmembrane #status predicted #label TM2\ !$150-290 #domain intracellular #status predicted #label INT2\ !$291-313 #domain transmembrane #status predicted #label TM3\ !$320-348 #domain transmembrane #status predicted #label TM4\ !$349-785 #domain intracellular #status predicted #label INT3\ !$586-782 #domain ATPase nucleotide-binding domain homology !8#label ATN\ !$786-809 #domain transmembrane #status predicted #label TM5\ !$848-873 #domain transmembrane #status predicted #label TM6\ !$874-951 #domain intracellular #status predicted #label INT4\ !$952-977 #domain transmembrane #status predicted #label TM7\ !$978-1022 #domain extracellular #status predicted #label EXT\ !$376 #active_site Asp (aspartylphosphate intermediate) !8#status predicted\ !$507 #binding_site ATP (Lys) #status predicted\ !$716,720,725 #active_site Asp, Asp, Lys #status predicted SUMMARY #length 1022 #molecular-weight 112429 #checksum 4199 SEQUENCE /// ENTRY S06635 #type complete TITLE Na+/K+-exchanging ATPase (EC 3.6.3.9) alpha chain (clone alpha-2850) - brine shrimp ORGANISM #formal_name Artemia franciscana #common_name brine shrimp DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 19-Apr-2002 ACCESSIONS S06635 REFERENCE S06635 !$#authors Baxter-Lowe, L.A.; Guo, J.Z.; Bergstrom, E.E.; Hokin, L.E. !$#journal FEBS Lett. (1989) 257:181-187 !$#title Molecular cloning of the Na, K-ATPase alpha-subunit in !1developing brine shrimp and sequence comparison with higher !1organisms. !$#cross-references MUID:90033341; PMID:2553490 !$#accession S06635 !'##molecule_type mRNA !'##residues 1-996 ##label BAX !'##cross-references EMBL:Y07513; NID:g5669; PIDN:CAA68811.1; PID:g5670 !'##note it is uncertain whether 1-Met is the initiator or whether !1translation is initiated 5' of the sequenced region CLASSIFICATION #superfamily Na+/K+-transporting ATPase alpha chain; ATPase !1nucleotide-binding domain homology KEYWORDS ATP; heterodimer; hydrolase; ion transport; phosphoprotein; !1potassium transport; sodium transport; transmembrane protein FEATURE !$73-94 #domain transmembrane #status predicted #label TM1\ !$107-126 #domain transmembrane #status predicted #label TM2\ !$127-267 #domain intracellular #status predicted #label INT2\ !$268-292 #domain transmembrane #status predicted #label TM3\ !$297-325 #domain transmembrane #status predicted #label TM4\ !$326-761 #domain intracellular #status predicted #label INT\ !$562-758 #domain ATPase nucleotide-binding domain homology !8#label ATN\ !$762-785 #domain transmembrane #status predicted #label TM5\ !$822-847 #domain transmembrane #status predicted #label TM6\ !$848-928 #domain intracellular #status predicted #label INT4\ !$929-947 #domain transmembrane #status predicted #label TM7\ !$948-996 #domain extracellular #status predicted #label EXT\ !$353 #active_site Asp (aspartylphosphate intermediate) !8#status predicted\ !$483 #binding_site ATP (Lys) #status predicted\ !$692,696,701 #active_site Asp, Asp, Lys #status predicted SUMMARY #length 996 #molecular-weight 111021 #checksum 1058 SEQUENCE /// ENTRY S03632 #type complete TITLE Na+/K+-exchanging ATPase (EC 3.6.3.9) alpha chain - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES sodium pump alpha chain ORGANISM #formal_name Drosophila melanogaster DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 21-Jun-2002 ACCESSIONS S03632; S07049 REFERENCE S03632 !$#authors Lebovitz, R.M.; Takeyasu, K.; Fambrough, D.M. !$#journal EMBO J. (1989) 8:193-202 !$#title Molecular characterization and expression of the !1(Na+K)-ATPase alpha-subunit in Drosophila melanogaster. !$#cross-references MUID:89231618; PMID:2540956 !$#accession S03632 !'##molecule_type mRNA !'##residues 1-1038 ##label LEB !'##cross-references EMBL:X14476 !'##note the sequence from Fig. 9 is inconsistent with that from Fig. 8 !1in having 89-Asp, 169-Leu, and 504-Gly !'##note it is uncertain whether Met-1 or Met-40 is the initiator REFERENCE S07049 !$#authors Varadi, A.; Gilmore-Heber, M.; Benz Jr., E.J. !$#journal FEBS Lett. (1989) 258:203-207 !$#title Amplification of the phosphorylation site - ATP-binding site !1cDNA fragment of the Na(+),K(+)-ATPase and the Ca(2+)-ATPase !1of Drosophila melanogaster by polymerase chain reaction. !$#cross-references MUID:90092469; PMID:2557235 !$#accession S07049 !'##molecule_type mRNA !'##residues 397-521 ##label VAR !'##cross-references EMBL:X17471 !'##note the authors translated the codon ACC for residue 3 as Asn and !1AAT for residue 89 as Ile; the sequence shown follows the !1authors' translation GENETICS !$#gene FlyBase:Atp-alpha !'##cross-references FlyBase:FBgn0002921 !$#map_position 3R 93B CLASSIFICATION #superfamily Na+/K+-transporting ATPase alpha chain; ATPase !1nucleotide-binding domain homology KEYWORDS ATP; heterodimer; hydrolase; ion transport; phosphoprotein; !1potassium transport; sodium transport; transmembrane protein FEATURE !$113-135 #domain transmembrane #status predicted #label TM1\ !$146-165 #domain transmembrane #status predicted #label TM2\ !$166-305 #domain intracellular #status predicted #label INT2\ !$306-328 #domain transmembrane #status predicted #label TM3\ !$335-363 #domain transmembrane #status predicted #label TM4\ !$364-801 #domain intracellular #status predicted #label INT3\ !$602-798 #domain ATPase nucleotide-binding domain homology !8#label ATN\ !$802-825 #domain transmembrane #status predicted #label TM5\ !$864-889 #domain transmembrane #status predicted #label TM6\ !$890-966 #domain intracellular #status predicted #label INT4\ !$967-993 #domain transmembrane #status predicted #label TM7\ !$994-1038 #domain extracellular #status predicted #label EXT\ !$391 #active_site Asp (aspartylphosphate intermediate) !8#status predicted\ !$523 #binding_site ATP (Lys) #status predicted\ !$732,736,741 #active_site Asp, Asp, Lys #status predicted SUMMARY #length 1038 #molecular-weight 115369 #checksum 871 SEQUENCE /// ENTRY PWRBFC #type complete TITLE Ca2+-transporting ATPase (EC 3.6.3.8), fast twitch skeletal muscle sarcoplasmic reticulum - rabbit ALTERNATE_NAMES calcium pump, fast twitch skeletal muscle; calcium-transporting ATPase, fast twitch skeletal muscle ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 19-Apr-2002 ACCESSIONS A01075; A60868; S56010; I46681; A54228; S39163; S71874 REFERENCE A01075 !$#authors Brandl, C.J.; Green, N.M.; Korczak, B.; MacLennan, D.H. !$#journal Cell (1986) 44:597-607 !$#title Two Ca(2+) ATPase genes: homologies and mechanistic !1implications of deduced amino acid sequences. !$#cross-references MUID:86133552; PMID:2936465 !$#accession A01075 !'##molecule_type mRNA !'##residues 1-1001 ##label BRA !'##cross-references GB:M12898; NID:g164778; PIDN:AAA31165.1; !1PID:g164779 !'##experimental_source fast twitch skeletal muscle; sarcoplasmic !1reticulum REFERENCE A60868 !$#authors Andersen, J.P.; Vilsen, B.; Collins, J.H.; Jorgensen, P.L. !$#journal J. Membr. Biol. (1986) 93:85-92 !$#title Localization of E-1-E-2 conformational transitions of !1sarcoplasmic reticulum Ca-ATPase by tryptic cleavage and !1hydrophobic labeling. !$#cross-references MUID:87086741; PMID:2948019 !$#accession A60868 !'##molecule_type protein !'##residues 199-212;335-348;506-519 ##label AND !'##note this protein is readily cleaved by trypsin after 198-Arg in the !1E-1 conformational state but not in the E-2 conformational !1state REFERENCE S56010 !$#authors Korczak, B.; Zarain-Herzberg, A.; Brandl, C.J.; Ingles, !1C.J.; Green, N.M.; MacLennan, D.H. !$#submission submitted to the EMBL Data Library, February 1989 !$#accession S56010 !'##molecule_type DNA !'##residues 1-39 ##label KOR !'##cross-references EMBL:M20531; NID:g164798; PIDN:AAA31172.1; !1PID:g552369 !'##experimental_source fast twitch skeletal muscle; sarcoplasmic !1reticulum REFERENCE I46681 !$#authors Brandl, C.J.; DeLeon, S.; Martin, D.R.; MacLennan, D.H. !$#journal J. Biol. Chem. (1987) 262:3768-3774 !$#title Adult forms of the Ca2+ ATPase of sarcoplasmic reticulum: !1Expression in developing skeletal muscle. !$#cross-references MUID:87137681; PMID:3029125 !$#accession I46681 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 973-1001 ##label BR2 !'##cross-references GB:M15351; NID:g164780; PIDN:AAA31166.1; !1PID:g164781 !'##experimental_source fast twitch skeletal muscle; sarcoplasmic !1reticulum REFERENCE A54228 !$#authors Lacapere, J.J.; Garin, J. !$#journal Biochemistry (1994) 33:2586-2593 !$#title Interaction of 4-azido-2-nitrophenyl phosphate, a !1pseudosubstrate, with the sarcoplasmic reticulum Ca-ATPase. !$#cross-references MUID:94162275; PMID:8117720 !$#accession A54228 !'##status preliminary !'##molecule_type protein !'##residues 506-513;584-591 ##label LAC REFERENCE S39163 !$#authors Wawrzynow, A.; Collins, J.H. !$#journal Biochim. Biophys. Acta (1993) 1203:60-70 !$#title Chemical modification of the Ca(2+)-ATPase of rabbit !1skeletal muscle sarcoplasmic reticulum: identification of !1sites labeled with aryl isothiocyanates and thiol-directed !1conformational probes. !$#cross-references MUID:94032459; PMID:8218393 !$#accession S39163 !'##molecule_type protein !'##residues 335-363,'X',365;468-470,'X',472-476;493-497,'X', !1499-502;513-514,'X',516-524,'X',526-529;606-613,'X', !1615;630-635,'X',637,'EAXR' ##label WAW !'##experimental_source skeletal muscle; sarcoplasmic reticulum REFERENCE S71874 !$#authors Corbalan-Garcia, S.; Teruel, J.A.; Gomez-Fernandez, J.C. !$#journal Biochem. J. (1996) 318:179-186 !$#title Involvement of an arginyl residue in the nucleotide-binding !1site of Ca(2+)-ATPase from sarcoplasmatic reticulum as seen !1by reaction with phenylglyoxal. !$#cross-references MUID:96358503; PMID:8761469 !$#accession S71874 !'##molecule_type protein !'##residues 134-140;490-495 ##label COR !'##experimental_source fast twitch skeletal muscle; sarcoplasmic !1reticulum COMMENT In rabbit, homologous enzymes are found in fast twitch and !1slow twitch skeletal muscle sarcoplasmic reticulum. !1Deficiency of the enzyme in fast twitch muscle causes !1Brody's disease, a disorder of skeletal muscle relaxation. FUNCTION !$#description catalyzes hydrolysis of one molecule ATP coupled to !1translocation of two calcium ions; catalyzes active !1transport of Ca2+ ions accross cellular membranes; borders !1Ca2+-sequestering stores such as the sarcoplasmic or !1endoplasmic reticulum; Ca2+ pump !$#pathway oxidative phosphorylation !$#note membrane-bound enzyme; magnesium-dependent; P-type ATPase CLASSIFICATION #superfamily Na+/K+-transporting ATPase alpha chain; ATPase !1nucleotide-binding domain homology KEYWORDS alternative splicing; ATP; calcium transport; hydrolase; ion !1transport; magnesium; phosphoprotein; skeletal muscle; !1transmembrane protein FEATURE !$40-57 #domain calcium binding #status predicted #label CA1\ !$60-78 #domain transmembrane #status predicted #label TM01\ !$87-107 #domain transmembrane #status predicted #label TM02\ !$111-131 #domain calcium binding #status predicted #label CA2\ !$132-238 #domain transduction #status predicted #label TSD\ !$238-256 #domain calcium binding #status predicted #label CA3\ !$258-277 #domain transmembrane #status predicted #label TM03\ !$288-307 #domain transmembrane #status predicted #label TM04\ !$310-329 #domain calcium binding #status predicted #label CA4\ !$330-505 #domain catalytic #status predicted #label PHY\ !$506-680 #domain nucleotide binding #status predicted #label !8NBD\ !$595-768 #domain ATPase nucleotide-binding domain homology !8#label ATN\ !$681-738 #domain hinge #status predicted #label HNG\ !$739-760 #domain calcium binding #status predicted #label CA5\ !$761-782 #domain transmembrane #status predicted #label TM05\ !$789-809 #domain transmembrane #status predicted #label TM06\ !$832-854 #domain transmembrane #status predicted #label TM07\ !$897-916 #domain transmembrane #status predicted #label TM08\ !$928-948 #domain transmembrane #status predicted #label TM09\ !$961-982 #domain transmembrane #status predicted #label TM10\ !$351 #active_site Asp (aspartylphosphate intermediate) !8#status predicted\ !$515 #binding_site ATP (Lys) #status predicted SUMMARY #length 1001 #molecular-weight 110458 #checksum 35 SEQUENCE /// ENTRY PWRBSC #type complete TITLE Ca2+-transporting ATPase (EC 3.6.3.8), slow twitch skeletal muscle - rabbit ALTERNATE_NAMES calcium pump, slow twitch skeletal muscle; calcium-transporting ATPase, slow twitch skeletal muscle ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 19-Apr-2002 ACCESSIONS A01076 REFERENCE A01076 !$#authors MacLennan, D.H.; Brandl, C.J.; Korczak, B.; Green, N.M. !$#journal Nature (1985) 316:696-700 !$#title Amino-acid sequence of a Ca(2+)+Mg(2+)-dependent ATPase from !1rabbit muscle sarcoplasmic reticulum, deduced from its !1complementary DNA sequence. !$#cross-references MUID:85296300; PMID:2993904 !$#accession A01076 !'##molecule_type mRNA !'##residues 1-997 ##label MAC !'##cross-references GB:X02814; GB:J02682; GB:M15159; NID:g1468; !1PIDN:CAA26583.1; PID:g1469 COMMENT This magnesium-dependent, membrane-bound enzyme catalyzes !1the hydrolysis of ATP coupled with the transport of the !1calcium. In rabbit, homologous enzymes are found in fast !1twitch and slow twitch skeletal muscle sarcoplasmic !1reticulum; the slow twitch enzyme is low in activity. !1Deficiency of the enzyme in fast twitch muscle causes !1Brody's disease, a disorder of skeletal muscle relaxation. CLASSIFICATION #superfamily Na+/K+-transporting ATPase alpha chain; ATPase !1nucleotide-binding domain homology KEYWORDS alternative splicing; ATP; calcium transport; hydrolase; !1magnesium; phosphoprotein; transmembrane protein FEATURE !$40-57 #domain calcium binding #status predicted #label CA1\ !$60-78 #domain transmembrane #status predicted #label TM01\ !$87-107 #domain transmembrane #status predicted #label TM02\ !$107-131 #domain calcium binding #status predicted #label CA2\ !$132-238 #domain transduction #label TSD\ !$238-256 #domain calcium binding #status predicted #label CA3\ !$258-277 #domain transmembrane #status predicted #label TM03\ !$288-307 #domain transmembrane #status predicted #label TM04\ !$310-329 #domain calcium binding #status predicted #label CA4\ !$506-680 #domain nucleotide binding #status predicted #label !8NBD\ !$594-767 #domain ATPase nucleotide-binding domain homology !8#label ATN\ !$680-740 #domain hinge #label HNG\ !$738-759 #domain calcium binding #status predicted #label CA5\ !$760-781 #domain transmembrane #status predicted #label TM05\ !$788-808 #domain transmembrane #status predicted #label TM06\ !$831-853 #domain transmembrane #status predicted #label TM07\ !$896-915 #domain transmembrane #status predicted #label TM08\ !$927-947 #domain transmembrane #status predicted #label TM09\ !$960-981 #domain transmembrane #status predicted #label TM10\ !$351 #active_site Asp (aspartylphosphate intermediate) !8#status predicted\ !$514 #binding_site ATP (Lys) #status predicted SUMMARY #length 997 #molecular-weight 109643 #checksum 7486 SEQUENCE /// ENTRY PWRBMC #type complete TITLE Ca2+-transporting ATPase (EC 3.6.3.8), smooth muscle sarcoplasmic reticulum - rabbit ALTERNATE_NAMES calcium pump ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 19-Apr-2002 ACCESSIONS S10335 REFERENCE S10335 !$#authors Khan, I.; Grover, A.K. !$#journal Nucleic Acids Res. (1990) 18:4026 !$#title Cloning of internal Ca pump from rabbit stomach smooth !1muscle. !$#cross-references MUID:90326561; PMID:2165260 !$#accession S10335 !'##molecule_type mRNA !'##residues 1-1042 ##label KHA !'##cross-references EMBL:X52496; NID:g1496; PIDN:CAA36737.1; !1PID:g3805934 !'##experimental_source stomach; smooth muscle; sarcoplasmic reticulum FUNCTION !$#description catalyzes hydrolysis of one molecule ATP coupled to !1translocation of two calcium ions; catalyzes active !1transport of Ca2+ ions accross cellular membranes; borders !1Ca2+-sequestering stores such as the sarcoplasmic or !1endoplasmic reticulum; Ca2+ pump !$#pathway oxidative phosphorylation !$#note membrane-bound enzyme; magnesium-dependent; P-type ATPase CLASSIFICATION #superfamily Na+/K+-transporting ATPase alpha chain; ATPase !1nucleotide-binding domain homology KEYWORDS alternative splicing; ATP; calcium transport; hydrolase; ion !1transport; magnesium; phosphoprotein; smooth muscle; !1transmembrane protein FEATURE !$40-57 #domain calcium binding #status predicted #label CA1\ !$60-78 #domain transmembrane #status predicted #label TM01\ !$87-107 #domain transmembrane #status predicted #label TM02\ !$107-131 #domain calcium binding #status predicted #label CA2\ !$108-257 #domain intracellular #status predicted #label INT1\ !$132-238 #domain transduction #status predicted #label TSD\ !$238-256 #domain calcium binding #status predicted #label CA3\ !$263-279 #domain transmembrane #status predicted #label TM03\ !$298-316 #domain transmembrane #status predicted #label TM04\ !$308-759 #domain intracellular #status predicted #label INT2\ !$310-329 #domain calcium binding #status predicted #label CA4\ !$330-505 #domain catalytic #status predicted #label PHY\ !$506-680 #domain ATP binding #status predicted #label ATP\ !$594-767 #domain ATPase nucleotide-binding domain homology !8#label ATN\ !$680-737 #domain hinge #status predicted #label HNG\ !$738-759 #domain calcium binding #status predicted #label CA5\ !$762-783 #domain transmembrane #status predicted #label TM05\ !$787-808 #domain transmembrane #status predicted #label TM06\ !$836-856 #domain transmembrane #status predicted #label TM07\ !$893-912 #domain transmembrane #status predicted #label TM08\ !$930-949 #domain transmembrane #status predicted #label TM09\ !$958-979 #domain transmembrane #status predicted #label TM10\ !$1013-1029 #domain transmembrane #status predicted #label TM11\ !$351 #active_site Asp (aspartylphosphate intermediate) !8#status predicted\ !$514 #binding_site ATP (Lys) #status predicted SUMMARY #length 1042 #molecular-weight 114704 #checksum 5950 SEQUENCE /// ENTRY A45598 #type complete TITLE H+-exporting ATPase (EC 3.6.3.6) - Trypanosoma brucei ORGANISM #formal_name Trypanosoma brucei DATE 22-Apr-1993 #sequence_revision 02-Jun-1994 #text_change 03-Jun-2002 ACCESSIONS A45598 REFERENCE A45598 !$#authors Revelard, P.; Pays, E. !$#journal Mol. Biochem. Parasitol. (1991) 46:241-251 !$#title Structure and transcription of a P-ATPase gene from !1Trypanosoma brucei. !$#cross-references MUID:92018021; PMID:1833643 !$#accession A45598 !'##molecule_type DNA !'##residues 1-1011 ##label REV !'##note sequence extracted from NCBI backbone (NCBIN:61106, !1NCBIP:61107) GENETICS !$#gene TBA1 CLASSIFICATION #superfamily Na+/K+-transporting ATPase alpha chain; ATPase !1nucleotide-binding domain homology KEYWORDS ATP; hydrolase; magnesium; membrane protein; phosphoprotein FEATURE !$594-767 #domain ATPase nucleotide-binding domain homology !8#label ATN SUMMARY #length 1011 #molecular-weight 110318 #checksum 7303 SEQUENCE /// ENTRY PWBYR1 #type complete TITLE Ca2+-transporting ATPase (EC 3.6.3.8) PMR1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES calcium pump PMR1; protein G1666; protein YGL167c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 19-Apr-2002 ACCESSIONS A30990; S41992; S59653; S64184; S72015; S05787; S19075 REFERENCE A30990 !$#authors Rudolph, H.K.; Antebi, A.; Fink, G.R.; Buckley, C.M.; !1Dorman, T.E.; LeVitre, J.; Davidow, L.S.; Mao, J.I.; Moir, !1D.T. !$#journal Cell (1989) 58:133-145 !$#title The yeast secretory pathway is perturbed by mutations in !1PMR1, a member of a Ca(2+) ATPase family. !$#cross-references MUID:89324047; PMID:2526682 !$#accession A30990 !'##molecule_type DNA !'##residues 1-950 ##label RUD !'##cross-references EMBL:M25488; NID:g515760; PIDN:AAA34884.1; !1PID:g172199 REFERENCE S41991 !$#authors Na, J.G.; Pinto, I.; Hampsey, M. !$#journal Genetics (1992) 131:791-801 !$#title Isolation and characterization of SUA5, a novel gene !1required for normal growth in Saccharomyces cerevisiae. !$#cross-references MUID:92387519; PMID:1325384 !$#accession S41992 !'##status translation not shown !'##molecule_type DNA !'##residues 863-950 ##label NAJ !'##cross-references EMBL:X64319; NID:g4565; PIDN:CAA45599.1; !1PID:g832923 REFERENCE S59649 !$#authors Klima, R.; Coglievina, M.; Zaccaria, P.; Bertani, I.; !1Bruschi, C.V. !$#submission submitted to the EMBL Data Library, March 1995 !$#description A putative helicase, the SUA5, PMR1, tRNA-lys1 genes and !1four open reading frames have been found in the DNA sequence !1of a 8.6 kb fragment of the left arm of Saccharomyces !1cerevisiae. !$#accession S59653 !'##molecule_type DNA !'##residues 1-950 ##label KLI !'##cross-references EMBL:X85757; NID:g971381; PIDN:CAA59762.1; !1PID:g971386 REFERENCE S64183 !$#authors Bruschi, C.V.; Coglievina, M.; Bertani, I.; Klima, R.; !1Zaccaria, P.; Delneri, D. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64184 !'##molecule_type DNA !'##residues 1-950 ##label BRU !'##cross-references EMBL:Z72690; GSPDB:GN00007; MIPS:YGL167c; !1NID:g1322766; PIDN:CAA96880.1; PID:g1322768 !'##experimental_source strain S288C REFERENCE S72011 !$#authors Klima, R.; Coglievina, M.; Zaccaria, P.; Bertani, I.; !1Bruschi, C.V. !$#journal Yeast (1996) 12:1033-1040 !$#title A putative helicase, the SUA5, PMR1, tRNA(Lys1) genes and !1four open reading frames have been detected in the DNA !1sequence of an 8.8 kb fragment of the left arm of chromosome !1VII of Saccharomyces cerevisiae. !$#cross-references MUID:97051590; PMID:8896267 !$#accession S72015 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-950 ##label KLW !'##cross-references EMBL:X85757; NID:g971381; PIDN:CAA59762.1; !1PID:g971386 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1March 1995 GENETICS !$#gene SGD:PMR1; SSC1; BSD1; MIPS:YGL167c !'##cross-references MIPS:YGL167c; SGD:S0003135 !$#map_position 7L CLASSIFICATION #superfamily Na+/K+-transporting ATPase alpha chain; ATPase !1nucleotide-binding domain homology KEYWORDS ATP; calcium transport; hydrolase; ion transport; !1phosphoprotein; transmembrane protein FEATURE !$45-70 #domain calcium binding #status predicted #label CA1\ !$98-114 #domain transmembrane #status predicted #label TM1\ !$117-133 #domain transmembrane #status predicted #label TM2\ !$291-307 #domain transmembrane #status predicted #label TM3\ !$331-347 #domain transmembrane #status predicted #label TM4\ !$574-746 #domain ATPase nucleotide-binding domain homology !8#label ATN\ !$743-759 #domain transmembrane #status predicted #label TM5\ !$815-831 #domain transmembrane #status predicted #label TM6\ !$885-901 #domain transmembrane #status predicted #label TM7\ !$912-928 #domain transmembrane #status predicted #label TM8\ !$371 #active_site Asp (aspartylphosphate intermediate) !8#status predicted\ !$501 #binding_site ATP (Lys) #status predicted SUMMARY #length 950 #molecular-weight 104570 #checksum 7363 SEQUENCE /// ENTRY PWBYR2 #type complete TITLE Ca2+-transporting ATPase (EC 3.6.3.8) ENA1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES calcium pump PMR2; plasma membrane protein PMR2A; protein D4130; protein YD6888.02c; protein YDR040c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 19-Apr-2002 ACCESSIONS S05788; S59278; S58391; S67854; B30990 REFERENCE A30990 !$#authors Rudolph, H.K.; Antebi, A.; Fink, G.R.; Buckley, C.M.; !1Dorman, T.E.; LeVitre, J.; Davidow, L.S.; Mao, J.I.; Moir, !1D.T. !$#journal Cell (1989) 58:133-145 !$#title The yeast secretory pathway is perturbed by mutations in !1PMR1, a member of a Ca(2+) ATPase family. !$#cross-references MUID:89324047; PMID:2526682 !$#accession S05788 !'##molecule_type DNA !'##residues 1-1091 ##label RUD !'##cross-references GB:U24069; EMBL:M25489; NID:g790260; !1PIDN:AAA65600.1; PID:g790261 REFERENCE S59277 !$#authors Murphy, L.; Harris, D. !$#submission submitted to the EMBL Data Library, September 1995 !$#accession S59278 !'##molecule_type DNA !'##residues 1-1091 ##label MUR !'##cross-references EMBL:Z54075; NID:g976128; PIDN:CAA90779.1; !1PID:g976130; GSPDB:GN00004; MIPS:YDR040c REFERENCE S58391 !$#authors Wieland, J.; Nitsche, A.M.; Strayle, J.; Steiner, H.; !1Rudolph, H.K. !$#journal EMBO J. (1995) 14:3870-3882 !$#title The PMR2 gene cluster encodes functionally distinct isoforms !1of a putative Na(+) pump in the yeast plasma membrane. !$#cross-references MUID:95393964; PMID:7664728 !$#accession S58391 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1091 ##label WIE !'##cross-references EMBL:U24069; NID:g790260; PIDN:AAA65600.1; !1PID:g790261 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1995 REFERENCE S67842 !$#authors Arnold, W.; Becker, A.; Jaeger, W.; Kuester, H.; Nussbaumer, !1B. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67854 !'##molecule_type DNA !'##residues 967-1091 ##label ARN !'##cross-references EMBL:Z74336; GSPDB:GN00004; MIPS:YDR040c !'##experimental_source strain S288C GENETICS !$#gene SGD:ENA1; PMR2; MIPS:YDR040c !'##cross-references SGD:S0002447; MIPS:YDR040c !$#map_position 4R CLASSIFICATION #superfamily Na+/K+-transporting ATPase alpha chain; ATPase !1nucleotide-binding domain homology KEYWORDS ATP; calcium transport; hydrolase; phosphoprotein; !1transmembrane protein FEATURE !$70-86 #domain transmembrane #status predicted #label TM1\ !$94-110 #domain transmembrane #status predicted #label TM2\ !$286-302 #domain transmembrane #status predicted #label TM3\ !$329-345 #domain transmembrane #status predicted #label TM4\ !$643-823 #domain ATPase nucleotide-binding domain homology !8#label ATN\ !$819-835 #domain transmembrane #status predicted #label TM5\ !$852-868 #domain transmembrane #status predicted #label TM6\ !$946-962 #domain transmembrane #status predicted #label TM7\ !$996-1012 #domain transmembrane #status predicted #label TM8\ !$1022-1038 #domain transmembrane #status predicted #label TM9\ !$369 #active_site Asp (aspartylphosphate intermediate) !8#status predicted\ !$561 #binding_site ATP (Lys) #status predicted SUMMARY #length 1091 #molecular-weight 120356 #checksum 4741 SEQUENCE /// ENTRY PXBY1P #type complete TITLE H+-exporting ATPase (EC 3.6.3.6) 1, plasma membrane - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein G3737; protein YGL008c; proton pump ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1992 #sequence_revision 19-Jul-1996 #text_change 03-Jun-2002 ACCESSIONS S64010; A25823; A35004 REFERENCE S64003 !$#authors Hebling, U.; Hofmann, B.; Delius, H. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64010 !'##molecule_type DNA !'##residues 1-918 ##label HEB !'##cross-references EMBL:Z72530; NID:g1322460; PIDN:CAA96708.1; !1PID:g1322461; GSPDB:GN00007; MIPS:YGL008c !'##experimental_source strain S288C REFERENCE A25823 !$#authors Serrano, R.; Kielland-Brandt, M.C.; Fink, G.R. !$#journal Nature (1986) 319:689-693 !$#title Yeast plasma membrane ATPase is essential for growth and has !1homology with (Na(1+) and K(1+)), K(1+)- and Ca(2+)-ATPases. !$#cross-references MUID:86146844; PMID:3005867 !$#accession A25823 !'##molecule_type DNA !'##residues 1-478,'SA',481-918 ##label SER !'##cross-references EMBL:X03534 !'##note the species of yeast is not given explicitly in this reference !1but was verified by personal communication from the author REFERENCE A35004 !$#authors Davis, C.B.; Smith, K.E.; Campbell Jr., B.N.; Hammes, G.G. !$#journal J. Biol. Chem. (1990) 265:1300-1305 !$#title The ATP binding site of the yeast plasma membrane !1proton-translocating ATPase. !$#cross-references MUID:90110179; PMID:2136852 !$#accession A35004 !'##status preliminary !'##molecule_type protein !'##residues 556-565 ##label DAV GENETICS !$#gene SGD:PMA1; MIPS:YGL008c !'##cross-references SGD:S0002976; MIPS:YGL008c !$#map_position 7L !$#introns #status absent FUNCTION !$#description transports protons across the plasma membrane to regulate !1intracellular pH and ion balance and to generate the !1electrochemical gradient that drives nutrient uptake CLASSIFICATION #superfamily Na+/K+-transporting ATPase alpha chain; ATPase !1nucleotide-binding domain homology KEYWORDS ATP; hydrogen ion transport; hydrolase; phosphoprotein; !1transmembrane protein FEATURE !$116-137 #domain transmembrane #status predicted #label TM1\ !$141-163 #domain transmembrane #status predicted #label TM2\ !$292-314 #domain transmembrane #status predicted #label TM3\ !$325-347 #domain transmembrane #status predicted #label TM4\ !$528-699 #domain ATPase nucleotide-binding domain homology !8#label ATN\ !$719-743 #domain transmembrane #status predicted #label TM5\ !$755-777 #domain transmembrane #status predicted #label TM6\ !$825-846 #domain transmembrane #status predicted #label TM7\ !$860-882 #domain transmembrane #status predicted #label TM8\ !$378 #active_site Asp (aspartylphosphate intermediate) !8#status predicted SUMMARY #length 918 #molecular-weight 99618 #checksum 3757 SEQUENCE /// ENTRY PXBY2P #type complete TITLE H+-exporting ATPase (EC 3.6.3.6) 2, plasma membrane - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein P7102.14; protein YPL036w; proton pump ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1992 #sequence_revision 19-Jul-1996 #text_change 03-Jun-2002 ACCESSIONS S62039; A32023; A35004 REFERENCE S62026 !$#authors Dietrich, F.S.; Allen, E.; Araujo, R.; Aparicio, A.; !1Carpenter, J.; Cherry, J.M.; Chung, E.; Davis, K.; Duncan, !1M.; Hunicke-Smith, S.; Hyman, R.; Kalman, S.; Komp, C.; !1Kurdi, O.; Lashkari, D.; Lew, H.; Lin, A.; Lin, D.; Marathe, !1R.; Mirtipati, S.; Namath, A.; Oefner, P.; Petel, F.X.; !1Roberts, D.; Schramm, S.; Schroeder, M.; Botstein, D.; !1Davis, R.W. !$#submission submitted to the EMBL Data Library, December 1995 !$#accession S62039 !'##molecule_type DNA !'##residues 1-947 ##label DIE !'##cross-references EMBL:U44030; NID:g1171408; PIDN:AAB68184.1; !1PID:g1171422; GSPDB:GN00016; MIPS:YPL036w REFERENCE A32023 !$#authors Schlesser, A.; Ulaszewski, S.; Ghislain, M.; Goffeau, A. !$#journal J. Biol. Chem. (1988) 263:19480-19487 !$#title A second transport ATPase gene in Saccharomyces cerevisiae. !$#cross-references MUID:89066768; PMID:2904437 !$#accession A32023 !'##molecule_type DNA !'##residues 1-652,'D',654-943,'D',945-947 ##label SCH !'##cross-references GB:J04421 !'##note the authors translated the codon GAC for residue 653 as Asn REFERENCE A35004 !$#authors Davis, C.B.; Smith, K.E.; Campbell Jr., B.N.; Hammes, G.G. !$#journal J. Biol. Chem. (1990) 265:1300-1305 !$#title The ATP binding site of the yeast plasma membrane !1proton-translocating ATPase. !$#cross-references MUID:90110179; PMID:2136852 !$#accession A35004 !'##status preliminary !'##molecule_type protein !'##residues 585-594 ##label DAV COMMENT This ATPase transports protons across the plasma membrane to !1regulate intracellular pH and ion balance and to generate !1the electrochemical gradient that drives nutrient uptake. GENETICS !$#gene SGD:PMA2; MIPS:YPL036w !'##cross-references SGD:S0005957; MIPS:YPL036w !$#map_position 16L CLASSIFICATION #superfamily Na+/K+-transporting ATPase alpha chain; ATPase !1nucleotide-binding domain homology KEYWORDS ATP; hydrogen ion transport; hydrolase; phosphoprotein; !1transmembrane protein FEATURE !$145-166 #domain transmembrane #status predicted #label TM1\ !$170-192 #domain transmembrane #status predicted #label TM2\ !$321-343 #domain transmembrane #status predicted #label TM3\ !$354-376 #domain transmembrane #status predicted #label TM4\ !$557-728 #domain ATPase nucleotide-binding domain homology !8#label ATN\ !$748-772 #domain transmembrane #status predicted #label TM5\ !$784-806 #domain transmembrane #status predicted #label TM6\ !$854-875 #domain transmembrane #status predicted #label TM7\ !$889-911 #domain transmembrane #status predicted #label TM8\ !$407 #active_site Asp (aspartylphosphate intermediate) !8#status predicted SUMMARY #length 947 #molecular-weight 102171 #checksum 767 SEQUENCE /// ENTRY PXKZP #type complete TITLE H+-exporting ATPase (EC 3.6.3.6), plasma membrane - yeast (Zygosaccharomyces rouxii) ALTERNATE_NAMES proton pump ORGANISM #formal_name Zygosaccharomyces rouxii, Candida mogii DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 03-Jun-2002 ACCESSIONS JX0181 REFERENCE JX0181 !$#authors Watanabe, Y.; Shiramizu, M.; Tamai, Y. !$#journal J. Biochem. (1991) 110:237-240 !$#title Molecular cloning and sequencing of plasma membrane !1H+-ATPase gene from the salt-tolerant yeast !1Zygosaccharomyces rouxii. !$#cross-references MUID:92105054; PMID:1837019 !$#accession JX0181 !'##molecule_type DNA !'##residues 1-920 ##label WAT !'##cross-references DDBJ:D10764; NID:g218530; PIDN:BAA01594.1; !1PID:g218531 !'##experimental_source ATCC 42981 COMMENT This ATPase transports protons across the plasma membrane to !1regulate intracellular pH and ion balance and to generate !1the electrochemical gradient that drives nutrient uptake. CLASSIFICATION #superfamily Na+/K+-transporting ATPase alpha chain; ATPase !1nucleotide-binding domain homology KEYWORDS ATP; hydrogen ion transport; hydrolase; phosphoprotein; !1transmembrane protein FEATURE !$114-138 #domain transmembrane #status predicted #label TM01\ !$144-162 #domain transmembrane #status predicted #label TM02\ !$294-315 #domain transmembrane #status predicted #label TM03\ !$329-353 #domain transmembrane #status predicted #label TM04\ !$530-701 #domain ATPase nucleotide-binding domain homology !8#label ATN\ !$662-679 #domain transmembrane #status predicted #label TM05\ !$694-713 #domain transmembrane #status predicted #label TM06\ !$723-740 #domain transmembrane #status predicted #label TM07\ !$757-781 #domain transmembrane #status predicted #label TM08\ !$827-847 #domain transmembrane #status predicted #label TM09\ !$854-877 #domain transmembrane #status predicted #label TM10\ !$380 #active_site Asp (aspartylphosphate intermediate) !8#status predicted SUMMARY #length 920 #molecular-weight 100061 #checksum 1710 SEQUENCE /// ENTRY PXZP1P #type complete TITLE H+-exporting ATPase (EC 3.6.3.6) 1, plasma membrane - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES proton-transporting ATPase ORGANISM #formal_name Schizosaccharomyces pombe DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 03-Jun-2002 ACCESSIONS A28454; T37492 REFERENCE A28454 !$#authors Ghislain, M.; Schlesser, A.; Goffeau, A. !$#journal J. Biol. Chem. (1987) 262:17549-17555 !$#title Mutation of a conserved glycine residue modifies the !1vanadate sensitivity of the plasma membrane H(+)-ATPase from !1Schizosaccharomyces pombe. !$#cross-references MUID:88087042; PMID:2891694 !$#accession A28454 !'##molecule_type DNA !'##residues 1-919 ##label GHI !'##cross-references GB:J03498; NID:g173428; PIDN:AAA35324.1; !1PID:g173429 REFERENCE Z21718 !$#authors Bothe, G.; Pohl, T.; McDougall, R.C.; Rajandream, M.A.; !1Barrell, B.G. !$#submission submitted to the EMBL Data Library, November 1999 !$#accession T37492 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-919 ##label BOT !'##cross-references EMBL:AL132769; PIDN:CAB59886.1; GSPDB:GN00066; !1SPDB:SPAC1071.10c !'##experimental_source strain 972h-; cosmid c1071 COMMENT This ATPase transports protons across the plasma membrane to !1regulate intracellular pH and ion balance and to generate !1the electrochemical gradient that drives nutrient uptake. GENETICS !$#gene PMA1 !$#map_position 1 !$#introns #status absent CLASSIFICATION #superfamily Na+/K+-transporting ATPase alpha chain; ATPase !1nucleotide-binding domain homology KEYWORDS ATP; hydrogen ion transport; hydrolase; membrane protein; !1phosphoprotein FEATURE !$526-697 #domain ATPase nucleotide-binding domain homology !8#label ATN\ !$376 #active_site Asp (aspartylphosphate intermediate) !8#status predicted SUMMARY #length 919 #molecular-weight 99883 #checksum 8230 SEQUENCE /// ENTRY PXZP2P #type complete TITLE H+-exporting ATPase (EC 3.6.3.6) 2, plasma membrane [validated] - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES proton pump ORGANISM #formal_name Schizosaccharomyces pombe DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 03-Jun-2002 ACCESSIONS A40945; T40840; T40949 REFERENCE A40945 !$#authors Ghislain, M.; Goffeau, A. !$#journal J. Biol. Chem. (1991) 266:18276-18279 !$#title The pma1 and pma2 H(+)-ATPases from Schizosaccharomyces !1pombe are functionally interchangeable. !$#cross-references MUID:92011563; PMID:1833395 !$#accession A40945 !'##molecule_type DNA !'##residues 1-1010 ##label GHI !'##cross-references GB:M60471; NID:g173430; PIDN:AAA35325.1; !1PID:g173431 REFERENCE Z21950 !$#authors Oliver, K.; Harris, D.; Wood, V.; Lyne, M.; Rajandream, !1M.A.; Barrell, B.G. !$#submission submitted to the EMBL Data Library, May 1998 !$#accession T40840 !'##molecule_type DNA !'##residues 1-573 ##label OLI !'##cross-references EMBL:AL023518; PIDN:CAA18989.1; GSPDB:GN00068; !1SPDB:SPCC1020.01c !'##experimental_source strain 972h(-) REFERENCE Z21940 !$#authors Wood, V.; Rajandream, M.A.; Barrell, B.G.; Volckaert, G. !$#submission submitted to the EMBL Data Library, February 1999 !$#accession T40949 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 466-1010 ##label WOO !'##cross-references EMBL:AL035592; PIDN:CAB38157.1; GSPDB:GN00068; !1SPDB:SPCC1393.01 !'##experimental_source strain 972h-; cosmid c1393 COMMENT This ATPase transports protons across the plasma membrane to !1regulate intracellular pH and ion balance and to generate !1the electrochemical gradient that drives nutrient uptake. COMMENT In addition to transient phosphorylation of the active site !1Asp residue, this protein, but not the product of the PMA1 !1locus (PIR:PXZP1P), is phosphorylated efficiently in !1isolated plasma membrane. GENETICS !$#gene PMA2; SPDB:SPCC1393.01 !$#map_position 3L !$#introns #status absent CLASSIFICATION #superfamily Na+/K+-transporting ATPase alpha chain; ATPase !1nucleotide-binding domain homology KEYWORDS ATP; hydrogen ion transport; hydrolase; phosphoprotein; !1transmembrane protein FEATURE !$202-222 #domain transmembrane #status predicted #label TM1\ !$227-246 #domain transmembrane #status predicted #label TM2\ !$379-400 #domain transmembrane #status predicted #label TM3\ !$411-428 #domain transmembrane #status predicted #label TM4\ !$614-785 #domain ATPase nucleotide-binding domain homology !8#label ATN\ !$807-825 #domain transmembrane #status predicted #label TM5\ !$841-859 #domain transmembrane #status predicted #label TM6\ !$913-933 #domain transmembrane #status predicted #label TM7\ !$941-965 #domain transmembrane #status predicted #label TM8\ !$464 #active_site Asp (aspartylphosphate intermediate) !8#status predicted SUMMARY #length 1010 #molecular-weight 110127 #checksum 6895 SEQUENCE /// ENTRY PXCKP #type complete TITLE H+-exporting ATPase (EC 3.6.3.6), plasma membrane - yeast (Candida albicans) ALTERNATE_NAMES proton pump ORGANISM #formal_name Candida albicans DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 03-Jun-2002 ACCESSIONS A41336 REFERENCE A41336 !$#authors Monk, B.C.; Kurtz, M.B.; Marrinan, J.A.; Perlin, D.S. !$#journal J. Bacteriol. (1991) 173:6826-6836 !$#title Cloning and characterization of the plasma membrane H !1(+)-ATPase from Candida albicans. !$#cross-references MUID:92041566; PMID:1834633 !$#accession A41336 !'##molecule_type DNA !'##residues 1-895 ##label MON !'##cross-references GB:M74075; NID:g170817; PIDN:AAA34319.1; !1PID:g170818 !'##note the authors translated the codon ATT for residue 741 as Val !'##note part of this sequence was confirmed by protein sequencing COMMENT This ATPase transports protons across the plasma membrane to !1regulate intracellular pH and ion balance and to generate !1the electrochemical gradient that drives nutrient uptake. GENETICS !$#gene PMA1 !$#map_position 3 CLASSIFICATION #superfamily Na+/K+-transporting ATPase alpha chain; ATPase !1nucleotide-binding domain homology KEYWORDS ATP; hydrogen ion transport; hydrolase; phosphoprotein; !1transmembrane protein FEATURE !$93-114 #domain transmembrane #status predicted #label TM1\ !$118-140 #domain transmembrane #status predicted #label TM2\ !$269-291 #domain transmembrane #status predicted #label TM3\ !$302-324 #domain transmembrane #status predicted #label TM4\ !$505-676 #domain ATPase nucleotide-binding domain homology !8#label ATN\ !$696-720 #domain transmembrane #status predicted #label TM5\ !$732-754 #domain transmembrane #status predicted #label TM6\ !$802-823 #domain transmembrane #status predicted #label TM7\ !$837-859 #domain transmembrane #status predicted #label TM8\ !$355 #active_site Asp (aspartylphosphate intermediate) !8#status predicted SUMMARY #length 895 #molecular-weight 97459 #checksum 6936 SEQUENCE /// ENTRY PXNCP #type complete TITLE H+-exporting ATPase (EC 3.6.3.6), plasma membrane [similarity] - Neurospora crassa ALTERNATE_NAMES B1D1.210; proton pump ORGANISM #formal_name Neurospora crassa DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 03-Jun-2002 ACCESSIONS A26497; A25939; A37880; A33846; A60806; T49367 REFERENCE A26497 !$#authors Hager, K.M.; Mandala, S.M.; Davenport, J.W.; Speicher, D.W.; !1Benz Jr., E.J.; Slayman, C.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:7693-7697 !$#title Amino acid sequence of the plasma membrane ATPase of !1Neurospora crassa: deduction from genomic and cDNA !1sequences. !$#cross-references MUID:87017015; PMID:2876429 !$#accession A26497 !'##molecule_type DNA !'##residues 1-920 ##label HAG !'##cross-references GB:M14085; NID:g168760; PIDN:AAA33561.1; !1PID:g168761 REFERENCE A25939 !$#authors Addison, R. !$#journal J. Biol. Chem. (1986) 261:14896-14901 !$#title Primary structure of the Neurospora plasma membrane !1H+-ATPase deduced from the gene sequence. !$#cross-references MUID:87033715; PMID:2876992 !$#accession A25939 !'##molecule_type DNA !'##residues 1-7,'A',9-920 ##label ADD !'##cross-references GB:J02602 REFERENCE A37880 !$#authors Scarborough, G.A.; Hennessey Jr., J.P. !$#journal J. Biol. Chem. (1990) 265:16145-16149 !$#title Identification of the major cytoplasmic regions of the !1Neurospora crassa plasma membrane H(+)-ATPase using protein !1chemical techniques. !$#cross-references MUID:90375470; PMID:2144525 !$#accession A37880 !'##molecule_type protein !'##residues !174-81;86-95;190-201;242-252;445-454;475-494;502-508;549-555; !1571-582;584-595;616-637;644-659 ##label SCA !'##note these fragments were released by proteinases from the !1cytoplasmic face of proteoliposomes and represent portions !1of the cytoplasmic domains of this protein REFERENCE A33846 !$#authors Pardo, J.P.; Slayman, C.W. !$#journal J. Biol. Chem. (1989) 264:9373-9379 !$#title Cysteine 532 and cysteine 545 are the !1N-ethylmaleimide-reactive residues of the Neurospora plasma !1membrane H(+)-ATPase. !$#cross-references MUID:89255436; PMID:2524486 !$#accession A33846 !'##molecule_type protein !'##residues 363-375,'X',377-379;520-531,'X',533-537;543-544,'X',546-548 !1##label PAR REFERENCE A60806 !$#authors Rao, U.S.; Hennessey Jr., J.P.; Scarborough, G.A. !$#journal Anal. Biochem. (1988) 173:251-264 !$#title Protein chemistry of the Neurospora crassa plasma membrane H !1(+)-ATPase. !$#cross-references MUID:89048299; PMID:2903697 !$#accession A60806 !'##molecule_type protein !'##residues 272-284,'F',286-291;660-680,'Y',682-698 ##label RAO REFERENCE Z25022 !$#authors Schulte, U.; Aign, V.; Hoheisel, J.; Brandt, P.; Fartmann, !1B.; Holland, R.; Nyakatura, G.; Mewes, H.W.; Mannhaupt, G. !$#submission submitted to the Protein Sequence Database, May 2000 !$#accession T49367 !'##status preliminary !'##molecule_type DNA !'##residues 1-920 ##label SCH !'##cross-references EMBL:AL355927; GSPDB:GN00116; NCSP:B1D1.210 !'##experimental_source BAC clone B1D1; strain OR74A COMMENT This ATPase transports protons across the plasma membrane to !1regulate intracellular pH and ion balance and to generate !1the electrochemical gradient that drives nutrient uptake. COMMENT Topological study of this protein shows certain regions to !1be accessible to proteinases on the cytoplasmic face !1(reference A37880) and 5 of 8 Cys residues to be accessible !1to water-sulfhydryl reagents (reference A33846). GENETICS !$#gene NCSP:B1D1.210 !$#map_position 6 !$#introns 60/3; 129/3; 174/2; 906/1 CLASSIFICATION #superfamily Na+/K+-transporting ATPase alpha chain; ATPase !1nucleotide-binding domain homology KEYWORDS ATP; hydrogen ion transport; hydrolase; phosphoprotein; !1transmembrane protein FEATURE !$116-137 #domain transmembrane #status predicted #label TM1\ !$141-163 #domain transmembrane #status experimental #label !8TM2\ !$292-314 #domain transmembrane #status predicted #label TM3\ !$325-347 #domain transmembrane #status predicted #label TM4\ !$528-699 #domain ATPase nucleotide-binding domain homology !8#label ATN\ !$719-743 #domain transmembrane #status predicted #label TM5\ !$755-777 #domain transmembrane #status predicted #label TM6\ !$827-848 #domain transmembrane #status experimental #label !8TM7\ !$862-884 #domain transmembrane #status experimental #label !8TM8\ !$378 #active_site Asp (aspartylphosphate intermediate) !8#status predicted SUMMARY #length 920 #molecular-weight 99886 #checksum 6736 SEQUENCE /// ENTRY PXMUP1 #type complete TITLE H+-exporting ATPase (EC 3.6.3.6) type 1, plasma membrane - Arabidopsis thaliana ALTERNATE_NAMES plasma membrane proton ATPase (PMA); proton pump ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 30-Sep-1992 #sequence_revision 22-Oct-1999 #text_change 03-Jun-2002 ACCESSIONS T01624; A32326; G84570 REFERENCE Z14153 !$#authors Rounsley, S.D.; Lin, X.; Ketchum, K.A.; Crosby, M.L.; !1Brandon, R.C.; Sykes, S.M.; Kaul, S.; Mason, T.M.; !1Kerlavage, A.R.; Adams, M.D.; Somerville, C.R.; Venter, J.C. !$#submission submitted to the EMBL Data Library, April 1998 !$#description Arabidopsis thaliana chromosome II BAC F19F24 genomic !1sequence. !$#accession T01624 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-949 ##label ROU !'##cross-references EMBL:AC003673; NID:g3004543; PIDN:AAC09030.1; !1PID:g3004557; GSPDB:GN00060; ATSP:F19F24.16 REFERENCE A32326 !$#authors Harper, J.F.; Surowy, T.K.; Sussman, M.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:1234-1238 !$#title Molecular cloning and sequence of cDNA encoding the plasma !1membrane proton pump (H(+)-ATPase) of Arabidopsis thaliana. !$#cross-references MUID:89145217; PMID:2521951 !$#accession A32326 !'##molecule_type mRNA !'##residues 1-770,'L',772-777,'Y',779-949 ##label HAR !'##cross-references GB:M24107; NID:g166745; PIDN:AAA32813.1; !1PID:g166746 REFERENCE A84420 !$#authors Lin, X.; Kaul, S.; Rounsley, S.D.; Shea, T.P.; Benito, M.I.; !1Town, C.D.; Fujii, C.Y.; Mason, T.M.; Bowman, C.L.; !1Barnstead, M.E.; Feldblyum, T.V.; Buell, C.R.; Ketchum, !1K.A.; Lee, J.J.; Ronning, C.M.; Koo, H.; Moffat, K.S.; !1Cronin, L.A.; Shen, M.; VanAken, S.E.; Umayam, L.; Tallon, !1L.J.; Gill, J.E.; Adams, M.D.; Carrera, A.J.; Creasy, T.H.; !1Goodman, H.M.; Somerville, C.R.; Copenhaver, G.P.; Preuss, !1D.; Nierman, W.C.; White, O.; Eisen, J.A.; Salzberg, S.L.; !1Fraser, C.M.; Venter, J.C. !$#journal Nature (1999) 402:761-768 !$#title Sequence and analysis of chromosome 2 of the plant !1Arabidopsis thaliana. !$#cross-references MUID:20083487; PMID:10617197 !$#accession G84570 !'##status preliminary !'##molecule_type DNA !'##residues 1-949 ##label STO !'##cross-references GB:AE002093; NID:g3004557; PIDN:AAC09030.1; !1GSPDB:GN00139 COMMENT This ATPase transports protons across the plasma membrane to !1regulate intracellular pH and ion balance and to generate !1the electrochemical gradient that drives nutrient uptake. GENETICS !$#gene AHA1; ATSP:F19F24.16; At2g18960 !$#map_position 2 !$#introns 14/3; 54/3; 133/3; 387/3; 428/3; 463/3; 512/1; 567/1; 646/3; !1657/3; 685/1; 738/3; 796/3; 857/3; 918/2 CLASSIFICATION #superfamily Na+/K+-transporting ATPase alpha chain; ATPase !1nucleotide-binding domain homology KEYWORDS ATP; hydrogen ion transport; hydrolase; membrane protein; !1phosphoprotein FEATURE !$481-653 #domain ATPase nucleotide-binding domain homology !8#label ATN\ !$329 #active_site Asp (aspartylphosphate intermediate) !8#status predicted\ !$423 #binding_site ATP (Lys) #status predicted SUMMARY #length 949 #molecular-weight 104223 #checksum 2278 SEQUENCE /// ENTRY PXMUP2 #type complete TITLE H+-exporting ATPase (EC 3.6.3.6) type 2, plasma membrane - Arabidopsis thaliana ALTERNATE_NAMES protein F9N11.40; proton pump ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 03-Jun-2002 ACCESSIONS A37116; T14079 REFERENCE A37116 !$#authors Harper, J.F.; Manney, L.; DeWitt, N.D.; Yoo, M.H.; Sussman, !1M.R. !$#journal J. Biol. Chem. (1990) 265:13601-13608 !$#title The Arabidopsis thaliana plasma membrane H+-ATPase multigene !1family. Genomic sequence and expression of a third isoform. !$#cross-references MUID:90337967; PMID:2143186 !$#accession A37116 !'##molecule_type DNA !'##residues 1-948 ##label HAR !'##cross-references GB:J05570; NID:g166628; PIDN:AAA32751.1; !1PID:g166629 REFERENCE Z17873 !$#authors Bevan, M.; Kalicki, J.; Wohldmann, P.; Smith, A.; Bancroft, !1I.; Mewes, H.W.; Mayer, K.F.X.; Lemcke, K.; Schueller, C. !$#submission submitted to the Protein Sequence Database, August 1999 !$#accession T14079 !'##molecule_type DNA !'##residues 1-948 ##label BEV !'##cross-references EMBL:AL109796 !'##experimental_source cultivar Columbia; BAC clone F9N11 COMMENT This ATPase transports protons across the plasma membrane to !1regulate intracellular pH and ion balance and to generate !1the electrochemical gradient that drives nutrient uptake. GENETICS !$#gene AHA2; ATSP:F9N11.40 !$#map_position 4 !$#introns 14/3; 54/3; 133/3; 387/3; 428/3; 463/3; 512/1; 567/1; 646/3; !1657/3; 685/1; 738/3; 796/3; 918/2 CLASSIFICATION #superfamily Na+/K+-transporting ATPase alpha chain; ATPase !1nucleotide-binding domain homology KEYWORDS ATP; hydrogen ion transport; hydrolase; membrane protein; !1phosphoprotein FEATURE !$481-653 #domain ATPase nucleotide-binding domain homology !8#label ATN\ !$329 #active_site Asp (aspartylphosphate intermediate) !8#status predicted\ !$423 #binding_site ATP (Lys) #status predicted SUMMARY #length 948 #molecular-weight 104400 #checksum 1085 SEQUENCE /// ENTRY PXMUP3 #type complete TITLE H+-exporting ATPase (EC 3.6.3.6) type 3, plasma membrane - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 03-Jun-2002 ACCESSIONS A33698; B33698 REFERENCE A33698 !$#authors Pardo, J.M.; Serrano, R. !$#journal J. Biol. Chem. (1989) 264:8557-8562 !$#title Structure of a plasma membrane H(+)-ATPase gene from the !1plant Arabidopsis thaliana. !$#cross-references MUID:89255309; PMID:2524481 !$#accession A33698 !'##molecule_type DNA !'##residues 1-949 ##label PA1 !'##cross-references GB:J04737; NID:g166624; PIDN:AAA32750.1; !1PID:g166625 !$#accession B33698 !'##molecule_type mRNA !'##residues 1-949 ##label PA2 !'##cross-references GB:J04737; NID:g166624; PIDN:AAA32750.1; !1PID:g166625 COMMENT This ATPase transports protons across the plasma membrane to !1regulate intracellular pH and ion balance and to generate !1the electrochemical gradient that drives nutrient uptake. GENETICS !$#gene AHA3 !$#introns 15/3; 55/3; 134/3; 388/3; 429/3; 464/3; 513/1; 568/1; 647/3; !1658/3; 686/1; 739/3; 797/3; 858/3; 919/2 CLASSIFICATION #superfamily Na+/K+-transporting ATPase alpha chain; ATPase !1nucleotide-binding domain homology KEYWORDS ATP; hydrogen ion transport; hydrolase; membrane protein; !1phosphoprotein FEATURE !$482-654 #domain ATPase nucleotide-binding domain homology !8#label ATN\ !$330 #active_site Asp (aspartylphosphate intermediate) !8#status predicted\ !$424 #binding_site ATP (Lys) #status predicted SUMMARY #length 949 #molecular-weight 104449 #checksum 8914 SEQUENCE /// ENTRY PXLNPD #type complete TITLE H+-exporting ATPase (EC 3.6.3.6), plasma membrane - Leishmania donovani ALTERNATE_NAMES proton-transporting ATPase ORGANISM #formal_name Leishmania donovani DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 03-Jun-2002 ACCESSIONS A27124 REFERENCE A27124 !$#authors Meade, J.C.; Shaw, J.; Lemaster, S.; Gallagher, G.; !1Stringer, J.R. !$#journal Mol. Cell. Biol. (1987) 7:3937-3946 !$#title Structure and expression of a tandem gene pair in Leishmania !1donovani that encodes a protein structurally homologous to !1eucaryotic cation-transporting ATPases. !$#cross-references MUID:88122116; PMID:2828921 !$#accession A27124 !'##molecule_type DNA !'##residues 1-974 ##label MEA !'##cross-references GB:M17889; NID:g159291; PIDN:AAA29227.1; !1PID:g159294 !'##note the authors translated the codon AGA for residue 352 as Lys CLASSIFICATION #superfamily Na+/K+-transporting ATPase alpha chain; ATPase !1nucleotide-binding domain homology KEYWORDS ATP; hydrogen ion transport; hydrolase; membrane protein; !1phosphoprotein FEATURE !$495-670 #domain ATPase nucleotide-binding domain homology !8#label ATN\ !$351 #active_site Asp (aspartylphosphate intermediate) !8#status predicted SUMMARY #length 974 #molecular-weight 107476 #checksum 834 SEQUENCE /// ENTRY PWHUNB #type complete TITLE Na+/K+-exchanging ATPase (EC 3.6.3.9) beta chain - human ALTERNATE_NAMES Na,K-ATPase beta chain; sodium pump beta chain; sodium/ potassium-dependent ATPase beta chain; sodium/ potassium-transporting ATPase beta chain ORGANISM #formal_name Homo sapiens #common_name man DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 19-Apr-2002 ACCESSIONS A23764; S51555; S51554 REFERENCE A23764 !$#authors Kawakami, K.; Nojima, H.; Ohta, T.; Nagano, K. !$#journal Nucleic Acids Res. (1986) 14:2833-2844 !$#title Molecular cloning and sequence analysis of human Na,K-ATPase !1beta-subunit. !$#cross-references MUID:86176770; PMID:3008098 !$#accession A23764 !'##molecule_type mRNA !'##residues 1-303 ##label KAW !'##cross-references GB:X03747; NID:g28932; PIDN:CAA27385.1; PID:g28933 REFERENCE S51555 !$#authors Lane, L.K.; Shull, M.M.; Whitmer, K.R.; Lingrel, J.B. !$#submission submitted to the EMBL Data Library, June 1989 !$#description Characterization of two genes for the human Na, K-Atpase !1beta subunit. !$#accession S51555 !'##status preliminary !'##molecule_type DNA !'##residues 1-303 ##label LAN !'##cross-references GB:M25161 REFERENCE S51554 !$#authors Lane, L.K.; Shull, M.M.; Whitmer, K.R.; Lingrel, J.B. !$#journal Genomics (1989) 5:445-453 !$#title Characterization of two genes for the human Na,K-ATPase beta !1subunit. !$#cross-references MUID:90129037; PMID:2559024 !$#accession S51554 !'##status preliminary !'##molecule_type DNA !'##residues 1-10 ##label LA2 !'##cross-references GB:M25161 COMMENT This polypeptide chain is an important structural component !1of the active enzyme. It associates with the alpha chain in !1a region close to the ouabain-binding site; therefore, it !1may be involved in the cellular resistance to ouabain. GENETICS !$#gene GDB:ATP1B1; ATP1B !'##cross-references GDB:120557; OMIM:182330 !$#map_position 1q22-1q25 !$#introns 33/1; 76/1; 128/1; 189/3; 216/3 CLASSIFICATION #superfamily Na+/K+-transporting ATPase beta chain KEYWORDS hydrolase; potassium transport; sodium transport; !1transmembrane protein SUMMARY #length 303 #molecular-weight 35061 #checksum 4872 SEQUENCE /// ENTRY PWRTNB #type complete TITLE Na+/K+-exchanging ATPase (EC 3.6.3.9) beta-1 chain - rat ALTERNATE_NAMES Na+/K+-transporting ATPase beta-1 chain; sodium pump beta chain; sodium/potassium-dependent ATPase beta chain ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 19-Apr-2002 ACCESSIONS A25082; A27411; S21088 REFERENCE A25082 !$#authors Mercer, R.W.; Schneider, J.W.; Savitz, A.; Emanuel, J.; Benz !1Jr., E.J.; Levenson, R. !$#journal Mol. Cell. Biol. (1986) 6:3884-3890 !$#title Rat-brain Na,K-ATPase beta-chain gene: primary structure, !1tissue-specific expression, and amplification in !1ouabain-resistant HeLa C+ cells. !$#cross-references MUID:87089731; PMID:3025616 !$#accession A25082 !'##molecule_type mRNA !'##residues 1-304 ##label MER !'##cross-references GB:M14137; NID:g203040; PIDN:AAA40781.1; !1PID:g203041 !'##experimental_source brain REFERENCE A27411 !$#authors Young, R.M.; Shull, G.E.; Lingrel, J.B. !$#journal J. Biol. Chem. (1987) 262:4905-4910 !$#title Multiple mRNAs from rat kidney and brain encode a single !1Na+,K+-ATPase beta subunit protein. !$#cross-references MUID:87165910; PMID:3031033 !$#accession A27411 !'##molecule_type mRNA !'##residues 1-182,'M',184-304 ##label YOU !'##cross-references GB:J02701; NID:g203038; PIDN:AAA40780.1; !1PID:g203039 REFERENCE S21088 !$#authors Liu, B.; Gick, G. !$#journal Biochim. Biophys. Acta (1992) 1130:336-338 !$#title Characterization of the 5' flanking region of the rat Na(+)/ !1K(+)-ATPase beta1 subunit gene. !$#cross-references MUID:92223118; PMID:1314096 !$#accession S21088 !'##molecule_type DNA !'##residues 1-32 ##label LIU !'##cross-references EMBL:X63375 CLASSIFICATION #superfamily Na+/K+-transporting ATPase beta chain KEYWORDS glycoprotein; hydrolase; potassium transport; sodium !1transport; transmembrane protein FEATURE !$35-61 #domain transmembrane #status predicted #label TMM\ !$158,193,266 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 304 #molecular-weight 35201 #checksum 4559 SEQUENCE /// ENTRY S09601 #type complete TITLE Na+/K+-exchanging ATPase (EC 3.6.3.9) beta chain - mouse ALTERNATE_NAMES Na+/K+-transporting ATPase beta chain ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 19-Apr-2002 ACCESSIONS S09601; S37712 REFERENCE S09601 !$#authors Gloor, S. !$#journal Nucleic Acids Res. (1989) 17:10117 !$#title Cloning and nucleotide sequence of the mouse Na,K-ATPase !1beta-subunit. !$#cross-references MUID:90098791; PMID:2557580 !$#accession S09601 !'##molecule_type mRNA !'##residues 1-304 ##label GLO !'##cross-references EMBL:X16646; NID:g53316; PIDN:CAA34639.1; !1PID:g53317 REFERENCE S37707 !$#authors Kato, K. !$#journal J. Neurosci. (1991) 2:704-711 !$#title A collection of cDNA clones with specific expression !1patterns in mouse brain. !$#accession S37712 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type mRNA !'##residues 33-304 ##label KAT !'##cross-references EMBL:X61433; NID:g54129; PIDN:CAA43675.1; !1PID:g54130 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1991 CLASSIFICATION #superfamily Na+/K+-transporting ATPase beta chain KEYWORDS glycoprotein; heterodimer; hydrolase; ion transport; !1potassium transport; sodium transport; transmembrane protein FEATURE !$35-61 #domain transmembrane #status predicted #label TM1\ !$62-304 #domain extracellular #status predicted #label EXT\ !$126-149,159-175, !$214-277 #disulfide_bonds #status predicted\ !$158,193,266 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 304 #molecular-weight 35194 #checksum 5751 SEQUENCE /// ENTRY PWDGB #type complete TITLE Na+/K+-exchanging ATPase (EC 3.6.3.9) beta chain - dog ORGANISM #formal_name Canis lupus familiaris #common_name dog DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 19-Apr-2002 ACCESSIONS S07148; S20839; S20840; S07152 REFERENCE S07148 !$#authors Brown, T.A.; Horowitz, B.; Miller, R.P.; McDonough, A.A.; !1Farley, R.A. !$#journal Biochim. Biophys. Acta (1987) 912:244-253 !$#title Molecular cloning and sequence analysis of the (Na+ + !1K+)-ATPase beta subunit from dog kidney. !$#cross-references MUID:87157751; PMID:3030434 !$#accession S07148 !'##molecule_type DNA !'##residues 1-303 ##label BRO !'##cross-references EMBL:X05297; NID:g874; PIDN:CAA28917.1; PID:g875 !$#accession S20839 !'##molecule_type mRNA !'##residues 1-303 ##label BRO1 !'##cross-references GB:X05297; NID:g874; PIDN:CAA28917.1; PID:g875 !$#accession S20840 !'##molecule_type protein !'##residues 2-21;72-85,86-90,'XR',93-96;224-248;278-288 ##label BRO2 REFERENCE S07152 !$#authors Miller, R.P.; Farley, R.A. !$#journal Biochim. Biophys. Acta (1988) 954:50-57 !$#title All three potential N-glycosylation sites of the dog kidney !1(Na(+)+K(+))-ATPase beta-subunit contain oligosaccharide. !$#cross-references MUID:88193100; PMID:2833926 !$#accession S07152 !'##molecule_type protein !'##residues 151-174,'X',176-179;183-202;259-273 ##label MIL CLASSIFICATION #superfamily Na+/K+-transporting ATPase beta chain KEYWORDS glycoprotein; hydrolase; ion transport; potassium transport; !1sodium transport; transmembrane protein FEATURE !$2-303 #product Na+/K+-transporting ATPase beta chain !8#status experimental #label MAT\ !$2-34 #domain intracellular #status predicted #label INT\ !$35-61 #domain transmembrane #status predicted #label TMM\ !$62-303 #domain extracellular #status predicted #label EXT\ !$126-149,213-276 #disulfide_bonds #status predicted\ !$158,193,265 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$159-175 #disulfide_bonds #status experimental SUMMARY #length 303 #molecular-weight 35239 #checksum 5358 SEQUENCE /// ENTRY PWRYNB #type complete TITLE Na+/K+-exchanging ATPase (EC 3.6.3.9) beta chain - Pacific electric ray ALTERNATE_NAMES sodium pump beta chain; sodium/potassium transporting ATPase beta chain; sodium/potassium-dependent ATPase beta chain ORGANISM #formal_name Torpedo californica #common_name Pacific electric ray DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 19-Apr-2002 ACCESSIONS A23625 REFERENCE A23625 !$#authors Noguchi, S.; Noda, M.; Takahashi, H.; Kawakami, K.; Ohta, !1T.; Nagano, K.; Hirose, T.; Inayama, S.; Kawamura, M.; Numa, !1S. !$#journal FEBS Lett. (1986) 196:315-320 !$#title Primary structure of the beta-subunit of Torpedo californica !1(Na+ + K+)-ATPase deduced from the cDNA sequence. !$#cross-references MUID:86136540; PMID:3005037 !$#accession A23625 !'##molecule_type mRNA !'##residues 1-305 ##label NOG !'##cross-references GB:X03471; NID:g64397; PIDN:CAA27188.1; PID:g64398 CLASSIFICATION #superfamily Na+/K+-transporting ATPase beta chain KEYWORDS hydrolase; potassium transport; sodium transport; !1transmembrane protein SUMMARY #length 305 #molecular-weight 34672 #checksum 971 SEQUENCE /// ENTRY S43793 #type complete TITLE copper-transporting ATPase (EC 3.6.1.-) - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS S43793; S43792 REFERENCE S43793 !$#authors Levinson, B.; Vulpe, C.; Elder, B.; Martin, C.; Verley, F.; !1Packman, S.; Gitschier, J. !$#journal Nature Genet. (1994) 6:369-373 !$#title The mottled gene is the mouse homologue of the Menkes !1disease gene. !$#cross-references MUID:94332144; PMID:8054976 !$#accession S43793 !'##status preliminary !'##molecule_type mRNA !'##residues 1-1491 ##label LEV !'##cross-references EMBL:U03434; NID:g451486; PIDN:AAA57445.1; !1PID:g451487 REFERENCE S43792 !$#authors Mercer, J.F.B.; Grimes, A.; Ambrosini, L.; Lockhart, P.; !1Paynter, J.A.; Dierick, H.; Glover, T.W. !$#journal Nature Genet. (1994) 6:374-378 !$#title Mutations in the murine homologue of the Menkes gene in !1dappled and blotchy mice. !$#cross-references MUID:94332145; PMID:8054977 !$#accession S43792 !'##status preliminary !'##molecule_type mRNA !'##residues 28-43,'E',45-102,'I',104-171,'M',173-244,'PI',247-445,'A', !1446-469,'P',471-514,'M',516-716,'F',718-769,'A',771-774,'S', !1776-884,'T',886-1168,'H',1170-1203,'P',1205-1216,'I', !11218-1252,'R',1254-1491 ##label MER !'##cross-references EMBL:U03736; NID:g458223; PIDN:AAB08487.1; !1PID:g458224 CLASSIFICATION #superfamily human copper-transporting ATPase; ATPase !1nucleotide-binding domain homology; ATPase transduction !1domain homology; heavy-metal-associated homology KEYWORDS copper transport; hydrolase; ion transport; transmembrane !1protein FEATURE !$14-43 #domain heavy-metal-associated homology #label HMA1\ !$177-206 #domain heavy-metal-associated homology #label HMA2\ !$283-312 #domain heavy-metal-associated homology #label HMA3\ !$383-412 #domain heavy-metal-associated homology #label HMA4\ !$485-514 #domain heavy-metal-associated homology #label HMA5\ !$561-590 #domain heavy-metal-associated homology #label HMA6\ !$709-1083 #domain ATPase transduction domain homology #label !8ATT\ !$1215-1357 #domain ATPase nucleotide-binding domain homology !8#label ATN\ !$17,19,22 #binding_site copper (Met, Cys, Cys) #status !8predicted\ !$180,182,185 #binding_site copper (Met, Cys, Cys) #status !8predicted\ !$286,288,291 #binding_site copper (Met, Cys, Cys) #status !8predicted\ !$386,388,391 #binding_site copper (Met, Cys, Cys) #status !8predicted\ !$488,490,493 #binding_site copper (Met, Cys, Cys) #status !8predicted\ !$564,566,569 #binding_site copper (Met, Cys, Cys) #status !8predicted SUMMARY #length 1491 #molecular-weight 161914 #checksum 6994 SEQUENCE /// ENTRY S78555 #type complete TITLE copper-transporting ATPase (EC 3.6.1.-) beta - human ALTERNATE_NAMES Cu2+-transporting ATPase P-type; Wilson disease protein ORGANISM #formal_name Homo sapiens #common_name man DATE 05-Dec-1998 #sequence_revision 05-Dec-1998 #text_change 18-Jun-1999 ACCESSIONS S78555; S40526; S78552; S78553; JC2027; I58117 REFERENCE S78555 !$#authors Petrukhin, K. !$#submission submitted to the EMBL Data Library, June 1994 !$#accession S78555 !'##molecule_type mRNA !'##residues 1-1465 ##label PET !'##cross-references EMBL:U11700; NID:g551501; PIDN:AAA92667.1; !1PID:g551502 REFERENCE I58117 !$#authors Tanzi, R.E.; Petrukhin, K.; Chernov, I.; Pellequer, J.L.; !1Wasco, W.; Ross, B.; Romano, D.M.; Parano, E.; Pavone, L.; !1Brzustowicz, L.M.; Devoto, M.; Peppercorn, J.; Bush, A.I.; !1Sternlieb, I.; Pirastu, M.; Gusella, J.F.; Evgrafov, O.; !1Penchaszadeh, G.K.; Honig, B.; Edelman, I.S.; Soares, M.B.; !1Scheinberg, I.H.; Gilliam, T.C. !$#journal Nature Genet. (1993) 5:344-350 !$#title The Wilson disease gene is a copper transporting ATPase with !1homology to the Menkes disease gene. !$#cross-references MUID:94129611; PMID:8298641 !$#accession S40526 !'##molecule_type mRNA !'##residues 149-623,786-910,956-1006,'T',1008-1465 ##label TAN REFERENCE S78552 !$#authors Tanzi, R.E.; Petrukhin, K.; Chernov, I.; Pellequer, J.L.; !1Wasco, W.; Ross, B.; Romano, D.M.; Parano, E.; Pavone, L.; !1Brzustowicz, L.M.; Devoto, M.; Peppercorn, J.; Bush, A.I.; !1Sternlieb, I.; Pirastu, M.; Gusella, J.F.; Evgrafov, O.; !1Penchaszadeh, G.K.; Honig, B.; Edelman, I.S.; Soares, M.B.; !1Scheinberg, I.H.; Gilliam, T.C. !$#submission submitted to the EMBL Data Library, February 1994 !$#accession S78552 !'##molecule_type mRNA !'##residues 152-455,'CRKWLPTLGGSLQTMPRTSWQSPHNQPEQWHRRSASYRSKA' ##label !1TAW !'##cross-references EMBL:L25591; NID:g452074; PIDN:AAA79211.1; !1PID:g452075 !'##note the differences are due to a frameshift error !$#accession S78553 !'##molecule_type mRNA !'##residues 497-623,786-910,956-1465 ##label TAF !'##cross-references EMBL:L25591; NID:g452074; PIDN:AAA79212.1; !1PID:g452076 REFERENCE JC2027 !$#authors Yamaguchi, Y.; Heiny, M.E.; Gitlin, J.D. !$#journal Biochem. Biophys. Res. Commun. (1993) 197:271-277 !$#title Isolation and characterization of a human liver cDNA as a !1candidate gene for Wilson disease. !$#cross-references MUID:94071954; PMID:8250934 !$#accession JC2027 !'##molecule_type mRNA !'##residues 'G',489-634,'T',636-766,'L',768-830,'RQGGPWG' ##label YAM COMMENT Wilson disease is an autosomal recessive defect in copper !1excretion, which results in damage to liver, brain, and !1other organs. GENETICS !$#gene GDB:ATP7B; WND !'##cross-references GDB:120494; OMIM:277900 !$#map_position 13q14.3-13q21.1 CLASSIFICATION #superfamily human copper-transporting ATPase; ATPase !1nucleotide-binding domain homology; ATPase transduction !1domain homology; heavy-metal-associated homology KEYWORDS alternative splicing; ATP; copper transport; hydrolase; ion !1transport; metal binding; transmembrane protein; Wilson !1disease FEATURE !$64-93 #domain heavy-metal-associated homology #label HMA1\ !$149-178 #domain heavy-metal-associated homology #label HMA2\ !$263-292 #domain heavy-metal-associated homology #label HMA3\ !$365-394 #domain heavy-metal-associated homology #label HMA4\ !$494-523 #domain heavy-metal-associated homology #label HMA5\ !$570-599 #domain heavy-metal-associated homology #label HMA6\ !$701-1075 #domain ATPase transduction domain homology #label !8ATT\ !$1190-1332 #domain ATPase nucleotide-binding domain homology !8#label ATN\ !$67,69,72 #binding_site copper (Met, Cys, Cys) #status !8predicted\ !$152,154,157 #binding_site copper (Met, Cys, Cys) #status !8predicted\ !$266,268,271 #binding_site copper (Met, Cys, Cys) #status !8predicted\ !$368,370,373 #binding_site copper (Met, Cys, Cys) #status !8predicted\ !$497,499,502 #binding_site copper (Met, Cys, Cys) #status !8predicted\ !$573,575,578 #binding_site copper (Met, Cys, Cys) #status !8predicted SUMMARY #length 1465 #molecular-weight 157390 #checksum 7445 SEQUENCE /// ENTRY I58124 #type complete TITLE copper-transporting ATPase (EC 3.6.1.-) beta chain - rat ALTERNATE_NAMES Wilson disease protein ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS I58124; S46482 REFERENCE I58124 !$#authors Wu, J.; Forbes, J.R.; Chen, H.S.; Cox, D.W. !$#journal Nature Genet. (1994) 7:541-545 !$#title The LEC rat has a deletion in the copper transporting ATPase !1gene homologous to the Wilson disease gene. !$#cross-references MUID:95038843; PMID:7951327 !$#accession I58124 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-1451 ##label RES !'##cross-references EMBL:U08344; NID:g555675; PIDN:AAA62157.1; !1PID:g555676 REFERENCE S46482 !$#authors Yamaguchi, Y.; Heiny, M.E.; Shimizu, N.; Aoki, T.; Gitlin, !1J.D. !$#journal Biochem. J. (1994) 301:1-4 !$#title Expression of the Wilson disease gene is deficient in the !1Long-Evans Cinnamon rat. !$#cross-references MUID:94311817; PMID:8037655 !$#accession S46482 !'##molecule_type mRNA !'##residues 530-575,'AC',578-584,'F',586-605 ##label YAM CLASSIFICATION #superfamily human copper-transporting ATPase; ATPase !1nucleotide-binding domain homology; ATPase transduction !1domain homology; heavy-metal-associated homology KEYWORDS copper transport; hydrolase; ion transport; transmembrane !1protein FEATURE !$63-92 #domain heavy-metal-associated homology #label HMA1\ !$148-177 #domain heavy-metal-associated homology #label HMA2\ !$262-291 #domain heavy-metal-associated homology #label HMA3\ !$487-516 #domain heavy-metal-associated homology #label HMA5\ !$563-592 #domain heavy-metal-associated homology #label HMA6\ !$694-1068 #domain ATPase transduction domain homology #label !8ATT\ !$1178-1320 #domain ATPase nucleotide-binding domain homology !8#label ATN SUMMARY #length 1451 #molecular-weight 155989 #checksum 2972 SEQUENCE /// ENTRY JC5573 #type complete TITLE copper-transporting ATPase (EC 3.6.1.-) P-type - Caenorhabditis elegans ALTERNATE_NAMES Cu2+-transporting ATPase P-type ORGANISM #formal_name Caenorhabditis elegans DATE 05-Dec-1998 #sequence_revision 05-Dec-1998 #text_change 16-Jun-2000 ACCESSIONS JC5573; T22243; T27419 REFERENCE JC5573 !$#authors Sambongi, Y.; Wakabayashi, T.; Yoshimizu, T.; Omote, H.; !1Oka, T.; Futai, M. !$#journal J. Biochem. (1997) 121:1169-1175 !$#title Caenorhabditis elegans cDNA for a Menkes/Wilson disease gene !1homologue and its function in a yeast CCC2 gene deletion !1mutant. !$#cross-references MUID:98014484; PMID:9354393 !$#accession JC5573 !'##molecule_type mRNA !'##residues 1-1238 ##label SAM !'##cross-references DDBJ:D83665; NID:g2217939; PIDN:BAA20550.1; !1PID:g2217940 REFERENCE Z19535 !$#authors Lindsay, S. !$#submission submitted to the EMBL Data Library, March 1997 !$#accession T22243 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 123-1238 ##label WIL !'##cross-references EMBL:Z93382; PIDN:CAB07620.1; GSPDB:GN00021; !1CESP:Y76A2A.2 !'##experimental_source clone F45G2 REFERENCE Z20362 !$#authors Steward, C. !$#submission submitted to the EMBL Data Library, October 1998 !$#accession T27419 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 123-1238 ##label WI2 !'##cross-references EMBL:AL032665; PIDN:CAA21773.1; GSPDB:GN00021; !1CESP:Y76A2A.2 !'##experimental_source clone Y76A2A GENETICS !$#gene CESP:Y76A2A.2 !$#map_position 3 !$#introns 170/1; 202/1; 243/3; 334/3; 414/2; 472/3; 634/1; 717/3; 779/ !13; 840/3; 910/1; 960/1; 1115/1 CLASSIFICATION #superfamily Caenorhabditis elegans copper-transporting !1ATPase; ATPase nucleotide-binding domain homology; ATPase !1transduction domain homology; heavy-metal-associated !1homology KEYWORDS ATP; copper transport; hydrolase; ion transport; metal !1binding; phosphoprotein; transmembrane protein FEATURE !$53-82 #domain heavy-metal-associated homology #label HMA1\ !$136-165 #domain heavy-metal-associated homology #label HMA2\ !$256-285 #domain heavy-metal-associated homology #label HMA3\ !$466-834 #domain ATPase transduction domain homology #label !8ATT\ !$964-1106 #domain ATPase nucleotide-binding domain homology !8#label ATN\ !$56,58,61 #binding_site copper (Met, Cys, Cys) #status !8predicted\ !$139,141,144 #binding_site copper (Met, Cys, Cys) #status !8predicted\ !$259,261,264 #binding_site copper (Met, Cys, Cys) #status !8predicted\ !$786 #active_site Asp (aspartylphosphate intermediate) !8#status predicted SUMMARY #length 1238 #molecular-weight 133468 #checksum 2906 SEQUENCE /// ENTRY S55353 #type complete TITLE probable copper-transporting ATPase (EC 3.6.1.-) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein D9954.6; protein YDR270w ORGANISM #formal_name Saccharomyces cerevisiae DATE 05-Dec-1998 #sequence_revision 05-Dec-1998 #text_change 21-Jul-2000 ACCESSIONS S55353; S70129; S48298 REFERENCE S55353 !$#authors Fu, D.; Beeler, T.J.; Dunn, T.M. !$#journal Yeast (1995) 11:283-292 !$#title Sequence, mapping and disruption of CCC2, a gene that !1cross-complements the Ca(2+)-sensitive phenotype of csg1 !1mutants and encodes a P-type ATPase belonging to the Cu !1(2+)-ATPase subfamily. !$#cross-references MUID:95304841; PMID:7785328 !$#accession S55353 !'##molecule_type DNA !'##residues 1-1004 ##label FUD !'##cross-references EMBL:L36317; NID:g538514; PIDN:AAC37425.1; !1PID:g538515 REFERENCE S70124 !$#authors Le, T. !$#submission submitted to the EMBL Data Library, May 1996 !$#description The sequence of S. cerevisiae cosmid 9954. !$#accession S70129 !'##molecule_type DNA !'##residues 1-1004 ##label LET !'##cross-references EMBL:U51030; NID:g1332633; PIDN:AAB64451.1; !1PID:g1230642; GSPDB:GN00004; MIPS:YDR270w GENETICS !$#gene SGD:CCC2; MIPS:YDR270w !'##cross-references SGD:S0002678; MIPS:YDR270w !$#map_position 4R CLASSIFICATION #superfamily yeast copper-transporting ATPase; ATPase !1nucleotide-binding domain homology; ATPase transduction !1domain homology; heavy-metal-associated homology KEYWORDS ATP; copper transport; hydrolase; ion transport; metal !1binding; transmembrane protein FEATURE !$8-37 #domain heavy-metal-associated homology #label HMA1\ !$86-115 #domain heavy-metal-associated homology #label HMA2\ !$262-278 #domain transmembrane #status predicted #label TM1\ !$304-320 #domain transmembrane #status predicted #label TM2\ !$308-676 #domain ATPase transduction domain homology #label !8ATT\ !$340-356 #domain transmembrane #status predicted #label TM3\ !$533-549 #domain transmembrane #status predicted #label TM4\ !$574-590 #domain transmembrane #status predicted #label TM5\ !$757-909 #domain ATPase nucleotide-binding domain homology !8#label ATN\ !$905-921 #domain transmembrane #status predicted #label TM6\ !$934-950 #domain transmembrane #status predicted #label TM7\ !$11,13,16 #binding_site copper (Met, Cys, Cys) #status !8predicted\ !$89,91,94 #binding_site copper (Met, Cys, Cys) #status !8predicted SUMMARY #length 1004 #molecular-weight 109828 #checksum 5012 SEQUENCE /// ENTRY A29576 #type complete TITLE H+/K+-exchanging ATPase (EC 3.6.3.10) - Enterococcus faecalis ALTERNATE_NAMES H+/K+-transporting ATPase ORGANISM #formal_name Enterococcus faecalis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS A29576 REFERENCE A29576 !$#authors Solioz, M.; Mathews, S.; Furst, P. !$#journal J. Biol. Chem. (1987) 262:7358-7362 !$#title Cloning of the K+-ATPase of Streptococcus faecalis. !1Structural and evolutionary implications of its homology to !1the KdpB-protein of Escherichia coli. !$#cross-references MUID:87222343; PMID:2953719 !$#accession A29576 !'##molecule_type DNA !'##residues 1-583 ##label SOL CLASSIFICATION #superfamily Enterococcus H+/K+-exchanging ATPase; ATPase !1nucleotide-binding domain homology; ATPase transduction !1domain homology KEYWORDS hydrolase; phosphoprotein; transmembrane protein FEATURE !$1-324 #domain ATPase transduction domain homology #label !8ATT\ !$399-541 #domain ATPase nucleotide-binding domain homology !8#label ATN SUMMARY #length 583 #molecular-weight 63152 #checksum 6674 SEQUENCE /// ENTRY B45995 #type complete TITLE copper-transporting ATPase (EC 3.6.1.-) copB - Enterococcus hirae ORGANISM #formal_name Enterococcus hirae DATE 16-Oct-1998 #sequence_revision 16-Oct-1998 #text_change 18-Jun-1999 ACCESSIONS B45995 REFERENCE A45995 !$#authors Odermatt, A.; Suter, H.; Krapf, R.; Solioz, M. !$#journal J. Biol. Chem. (1993) 268:12775-12779 !$#title Primary structure of two P-type ATPases involved in copper !1homeostasis in Enterococcus hirae. !$#cross-references MUID:93286122; PMID:8048974 !$#accession B45995 !'##molecule_type DNA !'##residues 1-745 ##label ODE !'##cross-references GB:L13292; NID:g290641; PIDN:AAA61836.1; !1PID:g290643 COMMENT This is one of two P-type copper-transporting ATPases !1involved in copper homeostasis, the other being the copA !1ATPase (see PIR:A45995). They are regulated by the !1transacting transcription regulatory proteins copY (see !1PIR:A56085) and copZ (see PIR:B56085). GENETICS !$#gene copB FUNCTION !$#description copper transport coupled with ATP hydrolysis !$#note believed to be involved in copper extrusion CLASSIFICATION #superfamily Enterococcus copper-transporting ATPase copB; !1ATPase nucleotide-binding domain homology; ATPase !1transduction domain homology KEYWORDS copper transport; hydrolase; ion transport; phosphoprotein; !1transmembrane protein FEATURE !$39-99 #region His-rich\ !$109-128 #domain transmembrane #status predicted #label TM1\ !$140-160 #domain transmembrane #status predicted #label TM2\ !$143-486 #domain ATPase transduction domain homology #label !8ATT\ !$173-191 #domain transmembrane #status predicted #label TM3\ !$201-217 #domain transmembrane #status predicted #label TM4\ !$360-379 #domain transmembrane #status predicted #label TM5\ !$389-409 #domain transmembrane #status predicted #label TM6\ !$561-703 #domain ATPase nucleotide-binding domain homology !8#label ATN\ !$704-721 #domain transmembrane #status predicted #label TM7\ !$724-744 #domain transmembrane #status predicted #label TM8\ !$296 #active_site Glu #status predicted\ !$440 #active_site Asp (aspartylphosphate intermediate) !8#status predicted SUMMARY #length 745 #molecular-weight 81522 #checksum 3824 SEQUENCE /// ENTRY JC2464 #type complete TITLE probable copper-transporting ATPase (EC 3.6.1.-) HRA-1 - Enterobacteriaceae spp. ORGANISM #formal_name Enterobacteriaceae spp. DATE 16-Oct-1998 #sequence_revision 16-Oct-1998 #text_change 18-Jun-1999 ACCESSIONS JC2464 REFERENCE JC2464 !$#authors Trenor III., C.; Lin, W.; Andrews, N.C. !$#journal Biochem. Biophys. Res. Commun. (1994) 205:1644-1650 !$#title Novel bacterial P-type ATPases with histidine-rich !1heavy-metal-associated sequences. !$#cross-references MUID:95110304; PMID:7811248 !$#accession JC2464 !'##molecule_type mRNA !'##residues 1-731 ##label TRE !'##cross-references GB:U16658; NID:g643612; PIDN:AAA62113.1; !1PID:g643613 !'##experimental_source human small intestine cDNA library !'##note the source species is uncertain; the cloned sequence did not !1hybridize with human DNA but did with Escherichia coli CLASSIFICATION #superfamily Enterococcus copper-transporting ATPase copB; !1ATPase nucleotide-binding domain homology; ATPase !1transduction domain homology KEYWORDS ATP; copper transport; hydrolase; ion transport; !1phosphoprotein; transmembrane protein FEATURE !$7-92 #region His-rich\ !$135-477 #domain ATPase transduction domain homology #label !8ATT\ !$544-685 #domain ATPase nucleotide-binding domain homology !8#label ATN\ !$287 #active_site Glu #status predicted\ !$431 #active_site Asp (aspartylphosphate intermediate) !8#status predicted SUMMARY #length 731 #molecular-weight 78453 #checksum 1432 SEQUENCE /// ENTRY JC2465 #type complete TITLE copper-transporting ATPase (EC 3.6.1.-) HRA-2 - Enterobacteriaceae spp. ORGANISM #formal_name Enterobacteriaceae spp. DATE 16-Oct-1998 #sequence_revision 16-Oct-1998 #text_change 18-Jun-1999 ACCESSIONS JC2465 REFERENCE JC2464 !$#authors Trenor III., C.; Lin, W.; Andrews, N.C. !$#journal Biochem. Biophys. Res. Commun. (1994) 205:1644-1650 !$#title Novel bacterial P-type ATPases with histidine-rich !1heavy-metal-associated sequences. !$#cross-references MUID:95110304; PMID:7811248 !$#accession JC2465 !'##molecule_type mRNA !'##residues 1-708 ##label TRE !'##cross-references GB:U16659; NID:g643614; PIDN:AAA62114.1; !1PID:g643615 !'##experimental_source human small intestine cDNA library !'##note the source species is uncertain; the cloned sequence did not !1hybridize with human DNA but did with Escherichia coli FUNCTION !$#description copper transport coupled with ATP hydrolysis CLASSIFICATION #superfamily Enterococcus copper-transporting ATPase copB; !1ATPase nucleotide-binding domain homology; ATPase !1transduction domain homology KEYWORDS copper transport; hydrolase; ion transport; phosphoprotein; !1transmembrane protein FEATURE !$5-60 #region His-rich\ !$83-99 #domain transmembrane #status predicted #label TM1\ !$114-130 #domain transmembrane #status predicted #label TM2\ !$115-455 #domain ATPase transduction domain homology #label !8ATT\ !$147-163 #domain transmembrane #status predicted #label TM3\ !$173-189 #domain transmembrane #status predicted #label TM4\ !$331-347 #domain transmembrane #status predicted #label TM5\ !$351-367 #domain transmembrane #status predicted #label TM6\ !$524-665 #domain ATPase nucleotide-binding domain homology !8#label ATN\ !$666-682 #domain transmembrane #status predicted #label TM7\ !$685-701 #domain transmembrane #status predicted #label TM8\ !$267 #active_site Glu #status predicted\ !$411 #active_site Asp (aspartylphosphate intermediate) !8#status predicted SUMMARY #length 708 #molecular-weight 76926 #checksum 9657 SEQUENCE /// ENTRY A45995 #type complete TITLE copper-transporting ATPase (EC 3.6.1.-) copA - Enterococcus hirae ORGANISM #formal_name Enterococcus hirae DATE 16-Oct-1998 #sequence_revision 16-Oct-1998 #text_change 18-Jun-1999 ACCESSIONS A45995; C56085 REFERENCE A45995 !$#authors Odermatt, A.; Suter, H.; Krapf, R.; Solioz, M. !$#journal J. Biol. Chem. (1993) 268:12775-12779 !$#title Primary structure of two P-type ATPases involved in copper !1homeostasis in Enterococcus hirae. !$#cross-references MUID:93286122; PMID:8048974 !$#accession A45995 !'##molecule_type DNA !'##residues 1-727 ##label ODE !'##cross-references GB:L13292; NID:g290641; PIDN:AAA61835.1; !1PID:g290642 REFERENCE A56085 !$#authors Odermatt, A.; Solioz, M. !$#journal J. Biol. Chem. (1995) 270:4349-4354 !$#title Two trans-acting metalloregulatory proteins controlling !1expression of the copper-ATPases of Enterococcus hirae. !$#cross-references MUID:95181419; PMID:7876197 !$#accession C56085 !'##molecule_type DNA !'##residues 1-9 ##label OD2 !'##cross-references GB:Z46807; NID:g662918; PIDN:CAA86837.1; !1PID:g662922 COMMENT This is one of two P-type copper-transporting ATPases !1involved in copper homeostasis, the other being the copB !1ATPase (see PIR:B45995). They are regulated by the !1transacting transcription regulatory proteins copY (see !1PIR:A56085) and copZ (see PIR:B56085). GENETICS !$#gene copA FUNCTION !$#description copper transport coupled with ATP hydrolysis !$#note believed to be involved in copper uptake CLASSIFICATION #superfamily Enterococcus copper-transporting ATPase copA; !1ATPase nucleotide-binding domain homology; ATPase !1transduction domain homology; heavy-metal-associated !1homology KEYWORDS ATP; copper transport; hydrolase; ion transport; !1phosphoprotein; transmembrane protein FEATURE !$12-41 #domain heavy-metal-associated homology #label HMA\ !$95-115 #domain transmembrane #status predicted #label TM1\ !$120-137 #domain transmembrane #status predicted #label TM2\ !$132-465 #domain ATPase transduction domain homology #label !8ATT\ !$162-181 #domain transmembrane #status predicted #label TM3\ !$188-203 #domain transmembrane #status predicted #label TM4\ !$342-362 #domain transmembrane #status predicted #label TM5\ !$376-396 #domain transmembrane #status predicted #label TM6\ !$542-686 #domain ATPase nucleotide-binding domain homology !8#label ATN\ !$679-698 #domain transmembrane #status predicted #label TM7\ !$701-721 #domain transmembrane #status predicted #label TM8\ !$17,20 #binding_site copper (Cys) #status predicted\ !$425 #active_site Asp (aspartylphosphate intermediate) !8#status predicted SUMMARY #length 727 #molecular-weight 78387 #checksum 3862 SEQUENCE /// ENTRY S75354 #type complete TITLE probable copper-transporting ATPase (EC 3.6.1.-) sll1920 - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein sll1920 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 16-Oct-1998 #sequence_revision 16-Oct-1998 #text_change 16-Jun-2000 ACCESSIONS S75354 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75354 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-745 ##label KAN !'##cross-references EMBL:D90904; GB:AB001339; NID:g1652225; !1PIDN:BAA17268.1; PID:g1652345 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 FUNCTION !$#description copper transport coupled with ATP hydrolysis CLASSIFICATION #superfamily Enterococcus copper-transporting ATPase copA; !1ATPase nucleotide-binding domain homology; ATPase !1transduction domain homology; heavy-metal-associated !1homology KEYWORDS ATP; copper transport; hydrolase; ion transport; !1phosphoprotein; transmembrane protein FEATURE !$9-38 #domain heavy-metal-associated homology #label HMA\ !$129-476 #domain ATPase transduction domain homology #label !8ATT\ !$556-698 #domain ATPase nucleotide-binding domain homology !8#label ATN\ !$14,17 #binding_site copper (Cys) #status predicted\ !$283 #active_site Glu #status predicted\ !$428 #active_site Asp (aspartylphosphate intermediate) !8#status predicted SUMMARY #length 745 #molecular-weight 79950 #checksum 3637 SEQUENCE /// ENTRY S36741 #type complete TITLE probable copper-transporting ATPase (EC 3.6.1.-) pacS - Synechococcus sp. ORGANISM #formal_name Synechococcus sp. DATE 16-Oct-1998 #sequence_revision 16-Oct-1998 #text_change 16-Jun-2000 ACCESSIONS S36741 REFERENCE S36741 !$#authors Kanamaru, K.; Kashiwagi, S.; Mizuno, T. !$#journal FEBS Lett. (1993) 330:99-104 !$#title The cyanobacterium, Synechococcus sp. PCC7942, possesses two !1distinct genes encoding cation-transporting P-type ATPases. !$#cross-references MUID:93380581; PMID:8370468 !$#accession S36741 !'##molecule_type DNA !'##residues 1-747 ##label KAN !'##cross-references GB:D16437; NID:g435124; PIDN:BAA03907.1; !1PID:g435125 FUNCTION !$#description copper transport coupled with ATP hydrolysis CLASSIFICATION #superfamily Enterococcus copper-transporting ATPase copA; !1ATPase nucleotide-binding domain homology; ATPase !1transduction domain homology; heavy-metal-associated !1homology KEYWORDS ATP; copper transport; hydrolase; ion transport; !1phosphoprotein; transmembrane protein FEATURE !$9-38 #domain heavy-metal-associated homology #label HMA\ !$136-480 #domain ATPase transduction domain homology #label !8ATT\ !$557-699 #domain ATPase nucleotide-binding domain homology !8#label ATN\ !$14,17 #binding_site copper (Cys) #status predicted\ !$289 #active_site Glu #status predicted\ !$434 #active_site Asp (aspartylphosphate intermediate) !8#status predicted SUMMARY #length 747 #molecular-weight 79731 #checksum 7482 SEQUENCE /// ENTRY S76487 #type complete TITLE probable copper-transporting ATPase (EC 3.6.1.-) - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 16-Oct-1998 #sequence_revision 16-Oct-1998 #text_change 16-Jun-2000 ACCESSIONS S76487 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76487 !'##status preliminary !'##molecule_type DNA !'##residues 1-780 ##label KAN !'##cross-references EMBL:D90915; GB:AB001339; NID:g1653604; !1PIDN:BAA18616.1; PID:g1653704 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 FUNCTION !$#description copper transport coupled with ATP hydrolysis CLASSIFICATION #superfamily Enterococcus copper-transporting ATPase copA; !1ATPase nucleotide-binding domain homology; ATPase !1transduction domain homology; heavy-metal-associated !1homology KEYWORDS ATP; copper transport; hydrolase; ion transport; !1phosphoprotein; transmembrane protein FEATURE !$30-59 #domain heavy-metal-associated homology #label HMA\ !$149-505 #domain ATPase transduction domain homology #label !8ATT\ !$581-725 #domain ATPase nucleotide-binding domain homology !8#label ATN\ !$35,38 #binding_site copper (Cys) #status predicted\ !$302 #active_site Glu #status predicted\ !$460 #active_site Asp (aspartylphosphate intermediate) !8#status predicted SUMMARY #length 780 #molecular-weight 82571 #checksum 3311 SEQUENCE /// ENTRY H64653 #type complete TITLE copper-transporting ATPase (EC 3.6.1.-), P-type - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 16-Oct-1998 #sequence_revision 16-Oct-1998 #text_change 18-Jun-1999 ACCESSIONS H64653; S60899 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession H64653 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-745 ##label TOM !'##cross-references GB:AE000614; GB:AE000511; NID:g2314216; !1PIDN:AAD08117.1; PID:g2314221; TIGR:HP1072 REFERENCE S60899 !$#authors Ge, Z.; Hiratsuka, K.; Taylor, D.E. !$#journal Mol. Microbiol. (1995) 15:97-106 !$#title Nucleotide sequence and mutational analysis indicate that !1two Helicobacter pylori genes encode a P-type ATPase and a !1cation-binding protein associated with copper transport. !$#cross-references MUID:95272397; PMID:7752900 !$#accession S60899 !'##status preliminary !'##molecule_type DNA !'##residues 135-136,'W',138-180,'D',182-235,'I',237-238,'D',240-260, !1'TL',263-323,'V',325-327,'H',329-355,'A',357-392,'SCFRIGYA', !1401-409,'SEFFRII',417-463,'N',465-493,'E',495-532,'Q', !1534-536,'NFSL',541-545,'N',547-569,'V',571-591,'K',593-595, !1'L',597-623,'R',625-711,'I',713-745 ##label GEZ !'##cross-references EMBL:L33259; NID:g1518875 FUNCTION !$#description copper transport coupled with ATP hydrolysis CLASSIFICATION #superfamily Enterococcus copper-transporting ATPase copA; !1ATPase nucleotide-binding domain homology; ATPase !1transduction domain homology; heavy-metal-associated !1homology KEYWORDS ATP; copper transport; hydrolase; ion transport; !1phosphoprotein; transmembrane protein FEATURE !$7-36 #domain heavy-metal-associated homology #label HMA\ !$128-478 #domain ATPase transduction domain homology #label !8ATT\ !$554-696 #domain ATPase nucleotide-binding domain homology !8#label ATN\ !$12,15 #binding_site copper (Cys) #status predicted\ !$284 #active_site Glu #status predicted\ !$435 #active_site Asp (aspartylphosphate intermediate) !8#status predicted SUMMARY #length 745 #molecular-weight 81852 #checksum 841 SEQUENCE /// ENTRY S77015 #type complete TITLE cadmium-transporting ATPase (EC 3.6.1.-) cadA-2 - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein slr0798 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 16-Oct-1998 #sequence_revision 16-Oct-1998 #text_change 16-Jun-2000 ACCESSIONS S77015 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S77015 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-721 ##label KAN !'##cross-references EMBL:D64005; GB:AB001339; NID:g1001779; !1PIDN:BAA10707.1; PID:g1001826 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene cadA_2 FUNCTION !$#description transition metal ion transport coupled with ATP hydrolysis CLASSIFICATION #superfamily Enterococcus copper-transporting ATPase copA; !1ATPase nucleotide-binding domain homology; ATPase !1transduction domain homology; heavy-metal-associated !1homology KEYWORDS ATP; hydrolase; ion transport; phosphoprotein; transmembrane !1protein FEATURE !$14-43 #domain heavy-metal-associated homology #label HMA\ !$135-470 #domain ATPase transduction domain homology #label !8ATT\ !$538-684 #domain ATPase nucleotide-binding domain homology !8#label ATN\ !$19,22 #binding_site transition metal ions (Cys) #status !8predicted\ !$278 #active_site Glu #status predicted\ !$425 #active_site Asp (aspartylphosphate intermediate) !8#status predicted SUMMARY #length 721 #molecular-weight 76883 #checksum 189 SEQUENCE /// ENTRY E70041 #type complete TITLE probable copper-transporting ATPase (EC 3.6.1.-) yvgX - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 16-Oct-1998 #sequence_revision 16-Oct-1998 #text_change 16-Jun-2000 ACCESSIONS E70041 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E70041 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-803 ##label KUN !'##cross-references GB:Z99121; GB:AL009126; NID:g2635827; !1PIDN:CAB15355.1; PID:g2635863 !'##experimental_source strain 168 GENETICS !$#gene yvgX FUNCTION !$#description copper transport coupled with ATP hydrolysis CLASSIFICATION #superfamily Bacillus probable copper-transporting ATPase !1yvgX; ATPase nucleotide-binding domain homology; ATPase !1transduction domain homology; heavy-metal-associated !1homology KEYWORDS ATP; copper transport; hydrolase; ion transport; !1phosphoprotein; transmembrane protein FEATURE !$12-41 #domain heavy-metal-associated homology #label HMA1\ !$80-109 #domain heavy-metal-associated homology #label HMA2\ !$201-545 #domain ATPase transduction domain homology #label !8ATT\ !$622-764 #domain ATPase nucleotide-binding domain homology !8#label ATN\ !$17,20 #binding_site copper (Cys) #status predicted\ !$85,88 #binding_site copper (Cys) #status predicted\ !$353 #active_site Glu #status predicted\ !$500 #active_site Asp (aspartylphosphate intermediate) !8#status predicted SUMMARY #length 803 #molecular-weight 86024 #checksum 6736 SEQUENCE /// ENTRY G69071 #type complete TITLE heavy-metal-transporting ATPase (EC 3.6.1.-) MTH1535 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 16-Oct-1998 #sequence_revision 16-Oct-1998 #text_change 18-Jun-1999 ACCESSIONS G69071 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession G69071 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-790 ##label MTH !'##cross-references GB:AE000913; GB:AE000666; NID:g2622646; !1PIDN:AAB86009.1; PID:g2622654 !'##experimental_source strain Delta H GENETICS !$#gene MTH1535 FUNCTION !$#description transition metal ion transport coupled with ATP hydrolysis CLASSIFICATION #superfamily Bacillus probable copper-transporting ATPase !1yvgX; ATPase nucleotide-binding domain homology; ATPase !1transduction domain homology; heavy-metal-associated !1homology KEYWORDS ATP; copper transport; hydrolase; ion transport; !1phosphoprotein; transmembrane protein FEATURE !$8-37 #domain heavy-metal-associated homology #label HMA1\ !$76-105 #domain heavy-metal-associated homology #label HMA2\ !$183-515 #domain ATPase transduction domain homology #label !8ATT\ !$590-732 #domain ATPase nucleotide-binding domain homology !8#label ATN\ !$13,16 #binding_site transition metal ions (Cys) #status !8predicted\ !$81,84 #binding_site transition metal ions (Cys) #status !8predicted\ !$331 #active_site Glu #status predicted\ !$477 #active_site Asp (aspartylphosphate intermediate) !8#status predicted SUMMARY #length 790 #molecular-weight 84010 #checksum 7946 SEQUENCE /// ENTRY C64779 #type complete TITLE probable copper-transporting ATPase (EC 3.6.1.-) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 05-Dec-1998 #sequence_revision 05-Dec-1998 #text_change 01-Mar-2002 ACCESSIONS C64779 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64779 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-834 ##label BLAT !'##cross-references GB:AE000154; GB:U00096; NID:g1786683; !1PIDN:AAC73586.1; PID:g1786691; UWGP:b0484 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ybaR CLASSIFICATION #superfamily Bacillus probable copper-transporting ATPase !1yvgX; ATPase nucleotide-binding domain homology; ATPase !1transduction domain homology; heavy-metal-associated !1homology KEYWORDS ATP; copper binding; hydrolase; ion transport; metal !1binding; phosphoprotein; transmembrane protein FEATURE !$9-38 #domain heavy-metal-associated homology #label HMA1\ !$105-134 #domain heavy-metal-associated homology #label HMA2\ !$189-205 #domain transmembrane #status predicted #label TM1\ !$218-234 #domain transmembrane #status predicted #label TM2\ !$224-568 #domain ATPase transduction domain homology #label !8ATT\ !$438-454 #domain transmembrane #status predicted #label TM3\ !$468-484 #domain transmembrane #status predicted #label TM4\ !$631-647 #domain transmembrane #status predicted #label TM5\ !$643-785 #domain ATPase nucleotide-binding domain homology !8#label ATN\ !$806-822 #domain transmembrane #status predicted #label TM6\ !$108,110,113 #binding_site copper (Met, Cys, Cys) #status !8predicted\ !$523 #active_site Asp (aspartylphosphate intermediate) !8#status predicted SUMMARY #length 834 #molecular-weight 87872 #checksum 9908 SEQUENCE /// ENTRY A69309 #type complete TITLE probable heavy-metal-transporting ATPase (EC 3.6.1.-) AF0473 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 16-Oct-1998 #sequence_revision 16-Oct-1998 #text_change 18-Jun-1999 ACCESSIONS A69309 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession A69309 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-804 ##label KLE !'##cross-references GB:AE001071; GB:AE000782; NID:g2689394; !1PIDN:AAB90763.1; PID:g2650152; TIGR:AF0473 FUNCTION !$#description transition metal ion transport coupled with ATP hydrolysis CLASSIFICATION #superfamily Archaeoglobus probable heavy-metal-transporting !1ATPase AF0473; ATPase nucleotide-binding domain homology; !1ATPase transduction domain homology; heavy-metal-associated !1homology KEYWORDS ATP; hydrolase; ion transport; phosphoprotein; transmembrane !1protein FEATURE !$22-51 #domain heavy-metal-associated homology #label HMA1\ !$130-468 #domain ATPase transduction domain homology #label !8ATT\ !$542-683 #domain ATPase nucleotide-binding domain homology !8#label ATN\ !$746-774 #domain heavy-metal-associated homology #label HMA2\ !$27,30 #binding_site transition metal ions (Cys) #status !8predicted\ !$278 #active_site Glu #status predicted\ !$424 #active_site Asp (aspartylphosphate intermediate) !8#status predicted\ !$751,754 #binding_site transition metal ions (Cys) #status !8predicted SUMMARY #length 804 #molecular-weight 86431 #checksum 3399 SEQUENCE /// ENTRY BVECAI #type complete TITLE DNA helicase I (EC 3.6.1.-) - Escherichia coli plasmids ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 21-Jul-2000 #text_change 19-Jan-2001 ACCESSIONS S10660; PS0322; PS0321; PS0068; T00299; T42198 REFERENCE S10658 !$#authors Yoshioka, Y.; Fujita, Y.; Ohtsubo, E. !$#journal J. Mol. Biol. (1990) 214:39-53 !$#title Nucleotide sequence of the promoter-distal region of the tra !1operon of plasmid R100, including traI (DNA helicase I) and !1traD genes. !$#cross-references MUID:90317835; PMID:2164585 !$#accession S10660 !'##molecule_type DNA !'##residues 1-1756 ##label YOS !'##cross-references EMBL:X55815; NID:g42620; PIDN:CAA39337.1; !1PID:g42623 !'##experimental_source plasmid R100 REFERENCE JQ1338 !$#authors Cram, D.S.; Loh, S.M.; Cheah, K.C.; Skurray, R.A. !$#journal Gene (1991) 104:85-90 !$#title Sequence and conservation of genes at the distal end of the !1transfer region on plasmids F and R6-5. !$#cross-references MUID:92009201; PMID:1916281 !$#accession PS0322 !'##molecule_type DNA !'##residues 1747-1756 ##label CRA1 !'##cross-references GB:M38048 !'##experimental_source plasmid R6-5 !$#accession PS0321 !'##molecule_type DNA !'##residues 1747-1756 ##label CRA2 !'##cross-references GB:M38047; NID:g148651; PIDN:AAA98090.1; !1PID:g148652 !'##experimental_source plasmid F REFERENCE JS0293 !$#authors Jalajakumari, M.B.; Manning, P.A. !$#journal Gene (1989) 81:195-202 !$#title Nucleotide sequence of the traD region in the Escherichia !1coli F sex factor. !$#cross-references MUID:90034191; PMID:2680768 !$#accession PS0068 !'##molecule_type DNA !'##residues 1,'M',3,'IAQ',7,'R',9-35,'R',37-68,'CRMAVTR',76-150 ##label !1JAL !'##cross-references GB:M29254; NID:g148618; PIDN:AAA83930.1; !1PID:g551859 !'##experimental_source strain K12; F factor !'##note the authors translated the codon CTG for residue 41 as Glu REFERENCE Z14127 !$#authors Makino, K.; Ishii, K.; Yasunaga, T.; Hattori, M.; Yokoyama, !1K.; Yatsudo, H.C.; Kubota, Y.; Yamaichi, Y.; Iida, T.; !1Yamamoto, K.; Honda, T.; Han, C.; Ohtsubo, A.; Kasamatsu, !1M.; Hayashi, T.; Kuhara, S.; Shinagawa, H. !$#journal DNA Res. (1998) 5:1-9 !$#title Complete nucleotide sequences of 93-kb and 3.3-kb plasmids !1of an enterohemorrhagic Escherichia coli O157:H7 derived !1from Sakai outbreak. !$#cross-references MUID:98290540; PMID:9628576 !$#accession T00299 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 'S',1108-1109,'F',1111,'G',1113,'FN',1295-1301,'R', !11303-1309,'Q',1311-1332,'P',1334-1335,'T',1337-1352,'G', !11354-1375,'G',1377-1385,'A',1387-1421,'S',1423-1469,'F', !11471-1481,'E',1483-1630,'N',1632-1682,'R',1684-1696,'E', !11698-1699,'VTS',1703-1715,'P',1717-1719,'R',1721-1726,'V', !11728-1738,'M',1740-1756 ##label MAK !'##cross-references EMBL:AB011549; PIDN:BAA31818.1 !'##experimental_source strain EHEC O157:H7, substrain RIMD 0509952 REFERENCE Z22068 !$#authors Burland, V.; Shao, Y.; Perna, N.T.; Plunkett, G.; Sofia, !1H.J.; Blattner, F.R. !$#journal Nucleic Acids Res. (1998) 26:4196-4204 !$#title The complete DNA sequence and analysis of the large !1virulence plasmid of Escherichia coli O157:H7. !$#cross-references MUID:98391744; PMID:9722640 !$#accession T42198 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 'M',1326-1332,'P',1334-1335,'T',1337-1352,'G',1354-1375, !1'G',1377-1385,'A',1387-1421,'S',1423-1469,'F',1471-1481,'E', !11483-1630,'N',1632-1682,'R',1684-1696,'E',1698-1699,'VTS', !11703-1715,'P',1717-1719,'R',1721-1726,'V',1728-1738,'M', !11740-1756 ##label BUR !'##cross-references EMBL:AF074613; PIDN:AAC70166.1 !'##experimental_source strain EDL933; serotype O157:H7 COMMENT This is one of the proteins that control the transfer of F !1plasmid. COMMENT There seems to be some variation or dissagreement regarding !1the translation start site for this protein. GENETICS !$#gene traI !$#genome plasmid CLASSIFICATION #superfamily helicase I KEYWORDS ATP; DNA binding; DNA repair; DNA replication; F pilin !1formation; hydrolase; nucleotide binding; P-loop FEATURE !$992-999 #region nucleotide-binding motif A (P-loop) SUMMARY #length 1756 #molecular-weight 191680 #checksum 8474 SEQUENCE /// ENTRY HJBYDH #type complete TITLE helicase (EC 3.6.1.-) HPR5 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein J0913; protein YJL092w ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1991 #sequence_revision 17-Feb-1995 #text_change 19-Jan-2001 ACCESSIONS S46586; S07617; S56869; S47059 REFERENCE S46584 !$#authors Miosga, T.; Witzel, A.; Zimmermann, F.K. !$#journal Yeast (1994) 10:965-973 !$#title Sequence and function analysis of a 9.46 kb fragment of !1Saccharomyces cerevisiae chromosome X. !$#cross-references MUID:95076716; PMID:7985424 !$#accession S46586 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1174 ##label MIO !'##cross-references EMBL:X77087; NID:g521093; PIDN:CAA54361.1; !1PID:g521096 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1994 REFERENCE S07617 !$#authors Aboussekhra, A.; Chanet, R.; Zgaga, Z.; Cassier-Chauvat, C.; !1Heude, M.; Fabre, F. !$#journal Nucleic Acids Res. (1989) 17:7211-7219 !$#title RADH, a gene of Saccharomyces cerevisiae encoding a putative !1DNA helicase involved in DNA repair. Characteristics of radH !1mutants and sequence of the gene. !$#cross-references MUID:90016783; PMID:2552405 !$#accession S07617 !'##molecule_type DNA !'##residues 1-172,'TQETDIKAKI',183-533,'VRILGTRMVR',543-544,'MS',547, !1'F',549-804,'M',806-916,'N',918-1174 ##label ABO !'##cross-references EMBL:X15665 REFERENCE S56855 !$#authors Miosga, T.; Schaaff-Gerstenschlaeger, I.; Baur, A.; Boles, !1E.; Chalwatzis, N.; Fournier, C.; Schmitt, S.; Velten, C.; !1Wilhelm, N.; Witzel, A.; Zimmermann, F.K. !$#submission submitted to the Protein Sequence Database, September 1995 !$#accession S56869 !'##molecule_type DNA !'##residues 1-1174 ##label MIW !'##cross-references EMBL:Z49367; NID:g1008263; PIDN:CAA89385.1; !1PID:g1008264; GSPDB:GN00010; MIPS:YJL092w GENETICS !$#gene SGD:HPR5; RADH1; SRS2; MIPS:YJL092w !'##cross-references SGD:S0003628; MIPS:YJL092w !$#map_position 10L FUNCTION !$#description DNA repair; hydrolase CLASSIFICATION #superfamily helicase II KEYWORDS ATP; DNA binding; DNA repair; DNA replication; hydrolase; !1leucine zipper; nucleotide binding; P-loop FEATURE !$35-42 #region nucleotide-binding motif A (P-loop)\ !$222-243 #region leucine zipper motif\ !$41 #binding_site ATP (Lys) #status predicted SUMMARY #length 1174 #molecular-weight 134305 #checksum 8619 SEQUENCE /// ENTRY HJECD2 #type complete TITLE DNA helicase II (EC 3.6.1.-) [validated] - Escherichia coli (strain K-12) CONTAINS adenosinetriphosphatase (EC 3.6.1.3) ORGANISM #formal_name Escherichia coli DATE 17-Mar-1987 #sequence_revision 10-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS F65185; JS0014; A93528; A93498; S30703; E37841; A03549 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65185 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-720 ##label BLAT !'##cross-references GB:AE000457; GB:U00096; NID:g2367294; !1PIDN:AAC76816.1; PID:g2367296; UWGP:b3813 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A92004 !$#authors Yamamoto, Y.; Ogawa, T.; Shinagawa, H.; Nakayama, T.; !1Matsuo, H.; Ogawa, H. !$#journal J. Biochem. (1986) 99:1579-1590 !$#title Determination of the initiation sites of transcription and !1translation of the uvrD gene of Escherichia coli. !$#cross-references MUID:86304220; PMID:2943729 !$#accession JS0014 !'##molecule_type DNA !'##residues 1-437,'R',439-720 ##label YAM !'##cross-references GB:D00069; GB:N00069; NID:g216672; PIDN:BAA00048.1; !1PID:g216673 !'##note residues 1-24 were confirmed by protein sequencing REFERENCE A93528 !$#authors Finch, P.W.; Emmerson, P.T. !$#journal Nucleic Acids Res. (1984) 12:5789-5799 !$#title The nucleotide sequence of the uvrD gene of Escherichia !1coli. !$#cross-references MUID:84272253; PMID:6379604 !$#accession A93528 !'##molecule_type DNA !'##residues 1-223,'N',225-290,'N',292,'R',294-329,'T',331-539,'V', !1541-720 ##label FIN !'##cross-references GB:X00738; GB:K01148; GB:X00225; NID:g43296; !1PIDN:CAA25321.1; PID:g43297 REFERENCE A93498 !$#authors Easton, A.M.; Kushner, S.R. !$#journal Nucleic Acids Res. (1983) 11:8625-8640 !$#title Transcription of the uvrD gene of Escherichia coli is !1controlled by the lexA repressor and by attenuation. !$#cross-references MUID:84169504; PMID:6324092 !$#accession A93498 !'##molecule_type DNA !'##residues 1-258 ##label EAS !'##cross-references GB:X00225; NID:g43294; PIDN:CAA25043.1; PID:g43295 REFERENCE S30660 !$#authors Daniels, D.L.; Plunkett III, G.; Burland, V.; Blattner, F.R. !$#journal Science (1992) 257:771-778 !$#title Analysis of the Escherichia coli genome: DNA sequence of the !1region from 84.5 to 86.5 minutes. !$#cross-references MUID:92358234; PMID:1379743 !$#accession S30703 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-47,'X',49-91,'X',93-97,'XX',100-720 ##label DAN !'##cross-references EMBL:M87049 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1992 REFERENCE A37841 !$#authors Colloms, S.D.; Sykora, P.; Szatmari, G.; Sherratt, D.J. !$#journal J. Bacteriol. (1990) 172:6973-6980 !$#title Recombination at ColE1 cer requires the Escherichia coli !1xerC gene product, a member of the lambda integrase family !1of site-specific recombinases. !$#cross-references MUID:91072248; PMID:2254268 !$#accession E37841 !'##status preliminary !'##molecule_type DNA !'##residues 1-17 ##label COL !'##cross-references GB:M38257 COMMENT The gene that codes for this protein is induced during the !1SOS response; the expression of the gene may be controlled !1by transcription attenuation as well as by the lexA !1repressor. GENETICS !$#gene uvrD !$#map_position 86 min !$#note expression is induced by DNA-damaging agents, e.g. nalidixic !1acid or mitomycin C FUNCTION HEL !$#description shows ATP-dependent DNA-unwinding activity [validated, !1MUID:84111621] FUNCTION ATP !$#description adenosinetriphosphatase (EC 3.6.1.3), single-stranded !1DNA-dependent [validated, MUID:84111621] CLASSIFICATION #superfamily helicase II KEYWORDS ATP; DNA binding; DNA repair; DNA replication; hydrolase; !1nucleotide binding; P-loop; SOS response FEATURE !$29-36 #region nucleotide-binding motif A (P-loop) SUMMARY #length 720 #molecular-weight 81989 #checksum 3972 SEQUENCE /// ENTRY HJECDR #type complete TITLE ATP-dependent DNA helicase Rep (EC 3.6.1.-) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Sep-1988 #sequence_revision 10-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS E65181; S30673; A26438; I54860 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65181 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-673 ##label BLAT !'##cross-references GB:AE000454; GB:U00096; NID:g2367278; !1PIDN:AAC76783.1; PID:g1790212; UWGP:b3778 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S30660 !$#authors Daniels, D.L.; Plunkett III, G.; Burland, V.; Blattner, F.R. !$#journal Science (1992) 257:771-778 !$#title Analysis of the Escherichia coli genome: DNA sequence of the !1region from 84.5 to 86.5 minutes. !$#cross-references MUID:92358234; PMID:1379743 !$#accession S30673 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-673 ##label DAN !'##cross-references EMBL:M87049; NID:g836656; PIDN:AAA67579.1; !1PID:g148182 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1992 REFERENCE A26438 !$#authors Gilchrist, C.A.; Denhardt, D.T. !$#journal Nucleic Acids Res. (1987) 15:465-475 !$#title Escherichia coli rep gene: sequence of the gene, the encoded !1helicase, and its homology with uvrD. !$#cross-references MUID:87146372; PMID:3029683 !$#accession A26438 !'##molecule_type DNA !'##residues 1-72,'H',74-75,'Q',77-162,'LLL',166-195,'R',197-201,'NG', !1204-619,'NWCARSRAA',629,'CWSCRRMI' ##label GIL !'##cross-references GB:X04794; NID:g42712; PIDN:CAA28481.1; PID:g42713 !'##note the authors translated the codon ACC for residue 15 as Tyr and !1TAT for residue 45 as Thr REFERENCE I54860 !$#authors Bialkowska-Hobrzanska, H.; Gilchrist, C.A.; Denhardt, D.T. !$#journal J. Bacteriol. (1985) 164:1004-1010 !$#title Escherichia coli rep gene: Identification of the promoter !1and N terminus of the Rep protein. !$#cross-references MUID:86059188; PMID:2999067 !$#accession I54860 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-13 ##label RES !'##cross-references GB:M11055; NID:g147563; PIDN:AAA24518.1; !1PID:g147564 COMMENT rep helicase is a single-stranded DNA-dependent ATPase !1involved in DNA replication; it can initiate unwinding at a !1nick in the DNA. It binds to the single-stranded DNA and !1acts in a progressive fashion along the DNA in the 3' to 5' !1direction. GENETICS !$#gene rep !$#map_position 85 min CLASSIFICATION #superfamily helicase II KEYWORDS ATP; DNA binding; DNA repair; DNA replication; hydrolase; !1nucleotide binding; P-loop FEATURE !$22-29 #region nucleotide-binding motif A (P-loop) SUMMARY #length 673 #molecular-weight 76938 #checksum 715 SEQUENCE /// ENTRY E69055 #type complete TITLE ATP-dependent RNA helicase, eIF-4A family - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-May-2001 ACCESSIONS E69055 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession E69055 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-738 ##label MTH !'##cross-references GB:AE000903; GB:AE000666; NID:g2622514; !1PIDN:AAB85892.1; PID:g2622527 !'##experimental_source strain Delta H GENETICS !$#gene MTH1415 CLASSIFICATION #superfamily ATP-dependent RNA helicase eIF-4A KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$38-45 #region nucleotide-binding motif A (P-loop)\ !$134-139 #region nucleotide-binding motif B\ !$138-141 #region DEXH motif SUMMARY #length 738 #molecular-weight 83913 #checksum 6313 SEQUENCE /// ENTRY A69432 #type complete TITLE ATP-dependent RNA helicase homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 24-May-2001 ACCESSIONS A69432 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession A69432 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-741 ##label KLE !'##cross-references GB:AE001002; GB:AE000782; NID:g2689325; !1PIDN:AAB89786.1; PID:g2649107; TIGR:AF1458 CLASSIFICATION #superfamily ATP-dependent RNA helicase eIF-4A KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$36-43 #region nucleotide-binding motif A (P-loop)\ !$132-137 #region nucleotide-binding motif B\ !$136-139 #region DEAD/H motif SUMMARY #length 741 #molecular-weight 84045 #checksum 6739 SEQUENCE /// ENTRY HJECD4 #type complete TITLE helicase (EC 3.6.1.-) IV - Escherichia coli (strain K-12) ALTERNATE_NAMES 75K helicase ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 21-Nov-1997 #text_change 01-Mar-2002 ACCESSIONS A64837; JV0021 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64837 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-684 ##label BLAT !'##cross-references GB:AE000198; GB:U00096; NID:g1787189; !1PIDN:AAC74048.1; PID:g1787196; UWGP:b0962 !'##experimental_source strain K-12, substrain MG1655 REFERENCE JV0021 !$#authors Wood, E.R.; Matson, S.W. !$#journal J. Biol. Chem. (1989) 264:8297-8303 !$#title The molecular cloning of the gene encoding the Escherichia !1coli 75-kDa helicase and the determination of its nucleotide !1sequence and genetic map position. !$#cross-references MUID:89255269; PMID:2542273 !$#accession JV0021 !'##molecule_type DNA !'##residues 1-69,'P',71-136,'LRVA',141-364,'ID',367-684 ##label WOO !'##cross-references GB:J04726; NID:g146327; PIDN:AAA23952.1; !1PID:g146328 !'##note residues 1-27 were confirmed by protein sequencing GENETICS !$#gene helD !$#map_position 22 min FUNCTION !$#description catalyzes the unwinding and separation of duplex DNA in vivo !$#note dependent on ATP hydrolysis CLASSIFICATION #superfamily helicase IV KEYWORDS ATP; DNA binding; DNA repair; DNA replication; hydrolase; !1nucleotide binding; P-loop FEATURE !$216-223 #region nucleotide-binding motif A (P-loop) SUMMARY #length 684 #molecular-weight 77975 #checksum 8841 SEQUENCE /// ENTRY HJNVAV #type complete TITLE helicase (EC 3.6.1.-) - Autographa californica nuclear polyhedrosis virus ORGANISM #formal_name Autographa californica nuclear polyhedrosis virus, AcMNPV DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 19-Jan-2001 ACCESSIONS A38499; H72861 REFERENCE A38499 !$#authors Lu, A.; Carstens, E.B. !$#journal Virology (1991) 181:336-347 !$#title Nucleotide sequence of a gene essential for viral DNA !1replication in the baculovirus Autographa californica !1nuclear polyhedrosis virus. !$#cross-references MUID:91134998; PMID:1994581 !$#accession A38499 !'##molecule_type DNA !'##residues 1-1221 ##label LUA !'##cross-references EMBL:M57687 REFERENCE A72850 !$#authors Ayres, M.D.; Howard, S.C.; Kuzio, J.; Lopez-Ferber, M.; !1Possee, R.D. !$#journal Virology (1994) 202:586-605 !$#title The complete DNA sequence of Autographa californica nuclear !1polyhedrosis virus. !$#cross-references MUID:94303173; PMID:8030224 !$#accession H72861 !'##status preliminary !'##molecule_type DNA !'##residues 1-125,'F',127-1148,'F',1150-1221 ##label AYR !'##cross-references GB:L22858; NID:g510708; PIDN:AAA66725.1; !1PID:g559164 GENETICS !$#gene Ac-helicase CLASSIFICATION #superfamily AcMNPV helicase KEYWORDS ATP; DNA binding; DNA repair; DNA replication; hydrolase; !1nucleotide binding; P-loop FEATURE !$917-924 #region nucleotide-binding motif A (P-loop) SUMMARY #length 1221 #molecular-weight 143119 #checksum 2531 SEQUENCE /// ENTRY HJBEI1 #type complete TITLE helicase (EC 3.6.1.-) - ictalurid herpesvirus 1 (strain auburn 1) ORGANISM #formal_name ictalurid herpesvirus 1 #note host Ictalurus punctatus (channel catfish) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 19-Jan-2001 ACCESSIONS H36788 REFERENCE A36804 !$#authors Davison, A.J. !$#submission submitted to GenBank, January 1992 !$#description Channel catfish virus: a new type of herpesvirus. !$#accession H36788 !'##molecule_type DNA !'##residues 1-498 ##label DAV !'##cross-references GB:M75136; NID:g331209; PIDN:AAA88128.1; !1PID:g331235 REFERENCE A39447 !$#authors Davison, A.J. !$#journal Virology (1992) 186:9-14 !$#title Channel catfish virus: a new type of herpesvirus. !$#cross-references MUID:92087490; PMID:1727613 !$#contents annotation !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 25 CLASSIFICATION #superfamily ictalurid herpesvirus helicase KEYWORDS ATP; DNA binding; DNA repair; DNA replication; hydrolase; !1nucleotide binding; P-loop FEATURE !$37-44 #region nucleotide-binding motif A (P-loop) SUMMARY #length 498 #molecular-weight 55761 #checksum 1389 SEQUENCE /// ENTRY BVECRQ #type complete TITLE DNA helicase recQ - Escherichia coli (strain K-12) ALTERNATE_NAMES DNA-dependent ATPase recQ (EC 3.6.1.-) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 10-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS G65186; JS0137; A35776; S30712 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65186 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-610 ##label BLAT !'##cross-references GB:AE000458; GB:U00096; NID:g2367299; !1PIDN:AAC76825.1; PID:g2367301; UWGP:b3822 !'##experimental_source strain K-12, substrain MG1655 REFERENCE JS0137 !$#authors Irino, N.; Nakayama, K.; Nakayama, H. !$#journal Mol. Gen. Genet. (1986) 205:298-304 !$#title The recQ gene of Escherichia coli K-12: primary structure !1and evidence for SOS regulation. !$#cross-references MUID:87115164; PMID:3027506 !$#accession JS0137 !'##molecule_type DNA !'##residues 1-256,'A',258-610 ##label IRI !'##experimental_source strain K12 !'##note it is uncertain whether residue 1, 3, 8 (all coded by GTG), or !19 (coded by TTG) is the initiator REFERENCE A35776 !$#authors Umezu, K.; Nakayama, K.; Nakayama, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:5363-5367 !$#title Escherichia coli recQ protein is a DNA helicase. !$#cross-references MUID:90319113; PMID:2164680 !$#accession A35776 !'##status preliminary !'##molecule_type protein !'##residues 4-8 ##label UME REFERENCE S30660 !$#authors Daniels, D.L.; Plunkett III, G.; Burland, V.; Blattner, F.R. !$#journal Science (1992) 257:771-778 !$#title Analysis of the Escherichia coli genome: DNA sequence of the !1region from 84.5 to 86.5 minutes. !$#cross-references MUID:92358234; PMID:1379743 !$#accession S30712 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 'V',2-256,'A',258-610 ##label DAN !'##cross-references EMBL:M87049 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1992 GENETICS !$#gene recQ !$#map_position 85 min !$#start_codon GTG FUNCTION !$#description involved in the recF recombination pathway; its gene !1expression is under the regulation of the SOS system !$#pathway recF recombination CLASSIFICATION #superfamily recQ protein; recQ helicase homology KEYWORDS ATP; DNA binding; hydrolase; nucleotide binding; P-loop; !1recF recombination pathway FEATURE !$49-56 #region nucleotide-binding motif A (P-loop)\ !$144-149 #region nucleotide-binding motif B\ !$148-151 #region DEAH motif\ !$369-402 #domain recQ helicase homology #label RHH SUMMARY #length 610 #molecular-weight 68434 #checksum 5881 SEQUENCE /// ENTRY C71367 #type complete TITLE probable ATP-dependent DNA helicase - syphilis spirochete ORGANISM #formal_name Treponema pallidum subsp. pallidum #common_name syphilis spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS C71367 REFERENCE A71250 !$#authors Fraser, C.M.; Norris, S.J.; Weinstock, G.M.; White, O.; !1Sutton, G.G.; Dodson, R.; Gwinn, M.; Hickey, E.K.; Clayton, !1R.; Ketchum, K.A.; Sodergren, E.; Hardham, J.M.; McLeod, !1M.P.; Salzberg, S.; Peterson, J.; Khalak, H.; Richardson, !1D.; Howell, J.K.; Chidambaram, M.; Utterback, T.; McDonald, !1L.; Artiach, P.; Bowman, C.; Cotton, M.D.; Fujii, C.; !1Garland, S.; Hatch, B.; Horst, K.; Roberts, K.; Watthey, L.; !1Weidman, J.; Smith, H.O.; Venter, J.C. !$#journal Science (1998) 281:375-388 !$#title Complete genome sequence of Treponema pallidum, the syphilis !1spirochete. !$#cross-references MUID:98332770; PMID:9665876 !$#accession C71367 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-607 ##label COL !'##cross-references GB:AE001194; GB:AE000520; NID:g3322355; !1PIDN:AAC65098.1; PID:g3322364 !'##experimental_source strain Nichols GENETICS !$#gene TP0103 CLASSIFICATION #superfamily syphilis spirochete probable ATP-dependent DNA !1helicase KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$128-135 #region nucleotide-binding motif A (P-loop)\ !$281-286 #region nucleotide-binding motif B\ !$285-288 #region DEAH motif SUMMARY #length 607 #molecular-weight 67286 #checksum 737 SEQUENCE /// ENTRY S66085 #type complete TITLE transcription-repair coupling factor mfd - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S66085; F69657 REFERENCE S65967 !$#authors Ogasawara, N.; Nakai, S.; Yoshikawa, H. !$#journal DNA Res. (1994) 1:1-14 !$#title Systematic sequencing of the 180 kilobase region of the !1Bacillus subtilis chromosome containing the replication !1origin. !$#cross-references MUID:96051385; PMID:7584024 !$#accession S66085 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-1177 ##label OGA !'##cross-references EMBL:D26185; NID:g467326; PIDN:BAA05290.1; !1PID:g467444 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1993 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69657 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-1177 ##label KUN !'##cross-references GB:Z99104; GB:AL009126; NID:g2632267; !1PIDN:CAB11831.1; PID:g2632322 !'##experimental_source strain 168 GENETICS !$#gene mfd CLASSIFICATION #superfamily transcription-repair coupling protein KEYWORDS ATP; DNA repair; leucine zipper; nucleotide binding; P-loop; !1transcription FEATURE !$651-658 #region nucleotide-binding motif A (P-loop)\ !$748-753 #region nucleotide-binding motif B\ !$752-755 #region DEAD/H motif #status atypical SUMMARY #length 1177 #molecular-weight 133811 #checksum 5249 SEQUENCE /// ENTRY F70177 #type complete TITLE transcription-repair coupling factor (mfd) homolog - Lyme disease spirochete ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS F70177 REFERENCE A70100 !$#authors Fraser, C.M.; Casjens, S.; Huang, W.M.; Sutton, G.G.; !1Clayton, R.; Lathigra, R.; White, O.; Ketchum, K.A.; Dodson, !1R.; Hickey, E.K.; Gwinn, M.; Dougherty, B.; Tomb, J.F.; !1Fleischmann, R.D.; Richardson, D.; Peterson, J.; Kerlavage, !1A.R.; Quackenbush, J.; Salzberg, S.; Hanson, M.; Vugt, R.V.; !1Palmer, N.; Adams, M.D.; Gocayne, J.; Weidman, J.; !1Utterback, T.; Watthey, L.; McDonald, L.; Artiach, P.; !1Bowman, C.; Garland, S.; Fujii, C.; Cotton, M.D.; Horst, K.; !1Roberts, K.; Hatch, B.; Smith, H.O.; Venter, J.C. !$#journal Nature (1997) 390:580-586 !$#title Genomic sequence of a Lyme disease spirochaete, Borrelia !1burgdorferi. !$#cross-references MUID:98065943; PMID:9403685 !$#accession F70177 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-1125 ##label KLE !'##cross-references GB:AE001163; GB:AE000783; NID:g2688541; !1PIDN:AAC66973.1; PID:g2688542; TIGR:BB0623 !'##experimental_source strain B31 CLASSIFICATION #superfamily transcription-repair coupling protein KEYWORDS ATP; DNA repair; leucine zipper; nucleotide binding; P-loop; !1transcription FEATURE !$610-617 #region nucleotide-binding motif A (P-loop)\ !$707-712 #region nucleotide-binding motif B\ !$711-714 #region DEAD/H motif #status atypical SUMMARY #length 1125 #molecular-weight 130729 #checksum 5104 SEQUENCE /// ENTRY I64112 #type complete TITLE transcription/repair-coupling protein - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES mutation frequency decline protein ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS I64112 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession I64112 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1146 ##label TIGR !'##cross-references GB:U32805; GB:L42023; NID:g1574180; !1PIDN:AAC22905.1; PID:g1574188; TIGR:HI1258 GENETICS !$#gene mfd FUNCTION !$#description required for strand-specific repair; displaces RNAP stalled !1at a lesion in an ATP-dependent reaction; binds to the !1damage recognition subunit of excision nuclease; stimulates !1repair of the transcribed strand only when transcription !1takes place CLASSIFICATION #superfamily transcription-repair coupling protein KEYWORDS ATP; DNA repair; leucine zipper; nucleotide binding; P-loop; !1transcription FEATURE !$630-637 #region nucleotide-binding motif A (P-loop)\ !$727-732 #region nucleotide-binding motif B\ !$731-734 #region DEAH motif SUMMARY #length 1146 #molecular-weight 130129 #checksum 7772 SEQUENCE /// ENTRY G64855 #type complete TITLE transcription/repair-coupling protein - Escherichia coli (strain K-12) ALTERNATE_NAMES mutation frequency decline protein ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS G64855; A46215 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64855 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1148 ##label BLAT !'##cross-references GB:AE000211; GB:U00096; NID:g1787345; !1PIDN:AAC74198.1; PID:g1787357; UWGP:b1114 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A46215 !$#authors Selby, C.P.; Sancar, A. !$#journal Science (1993) 260:53-58 !$#title Molecular mechanism of transcription-repair coupling. !$#cross-references MUID:93219833; PMID:8465200 !$#accession A46215 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type DNA !'##residues 1-364,'R',366-1148 ##label SEL GENETICS !$#gene mfd; trcF FUNCTION !$#description required for strand-specific repair; displaces RNAP stalled !1at a lesion in an ATP-dependent reaction; binds to the !1damage recognition chain of the excision nuclease; !1stimulates the repair of the transcribed strand only when !1transcription is taking place CLASSIFICATION #superfamily transcription-repair coupling protein KEYWORDS ATP; DNA repair; leucine zipper; nucleotide binding; P-loop; !1transcription FEATURE !$628-635 #region nucleotide-binding motif A (P-loop)\ !$725-730 #region nucleotide-binding motif B\ !$729-732 #region DEAH motif SUMMARY #length 1148 #molecular-weight 129981 #checksum 132 SEQUENCE /// ENTRY S76549 #type complete TITLE transcription-repair coupling protein - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S76549 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76549 !'##status preliminary !'##molecule_type DNA !'##residues 1-1199 ##label KAN !'##cross-references EMBL:D64002; GB:AB001339; NID:g1001612; !1PIDN:BAA10395.1; PID:g1001661 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily transcription-repair coupling protein KEYWORDS ATP; DNA repair; leucine zipper; nucleotide binding; P-loop; !1transcription FEATURE !$673-680 #region nucleotide-binding motif A (P-loop)\ !$771-776 #region nucleotide-binding motif B\ !$775-778 #region DEAD/H motif #status atypical SUMMARY #length 1199 #molecular-weight 134534 #checksum 5360 SEQUENCE /// ENTRY D70172 #type complete TITLE DNA recombinase (recG) homolog - Lyme disease spirochete ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS D70172 REFERENCE A70100 !$#authors Fraser, C.M.; Casjens, S.; Huang, W.M.; Sutton, G.G.; !1Clayton, R.; Lathigra, R.; White, O.; Ketchum, K.A.; Dodson, !1R.; Hickey, E.K.; Gwinn, M.; Dougherty, B.; Tomb, J.F.; !1Fleischmann, R.D.; Richardson, D.; Peterson, J.; Kerlavage, !1A.R.; Quackenbush, J.; Salzberg, S.; Hanson, M.; Vugt, R.V.; !1Palmer, N.; Adams, M.D.; Gocayne, J.; Weidman, J.; !1Utterback, T.; Watthey, L.; McDonald, L.; Artiach, P.; !1Bowman, C.; Garland, S.; Fujii, C.; Cotton, M.D.; Horst, K.; !1Roberts, K.; Hatch, B.; Smith, H.O.; Venter, J.C. !$#journal Nature (1997) 390:580-586 !$#title Genomic sequence of a Lyme disease spirochaete, Borrelia !1burgdorferi. !$#cross-references MUID:98065943; PMID:9403685 !$#accession D70172 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-686 ##label KLE !'##cross-references GB:AE001159; GB:AE000783; NID:g2688496; !1PIDN:AAC66942.1; PID:g2688498; TIGR:BB0581 !'##experimental_source strain B31 CLASSIFICATION #superfamily DNA helicase recG KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$290-297 #region nucleotide-binding motif A (P-loop)\ !$387-392 #region nucleotide-binding motif B\ !$391-394 #region DEXH motif SUMMARY #length 686 #molecular-weight 79043 #checksum 4495 SEQUENCE /// ENTRY H69879 #type complete TITLE ATP-dependent DNA helicase homolog ylpB - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS H69879 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69879 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-682 ##label KUN !'##cross-references GB:Z99112; GB:AL009126; NID:g2633902; !1PIDN:CAB13460.1; PID:g2633959 !'##experimental_source strain 168 GENETICS !$#gene ylpB CLASSIFICATION #superfamily DNA helicase recG KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$284-291 #region nucleotide-binding motif A (P-loop)\ !$381-386 #region nucleotide-binding motif B\ !$385-388 #region DEXH motif SUMMARY #length 682 #molecular-weight 78140 #checksum 7823 SEQUENCE /// ENTRY S71016 #type complete TITLE helicase recG homolog - Streptococcus pneumoniae ORGANISM #formal_name Streptococcus pneumoniae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S71016 REFERENCE S71015 !$#authors Martin, B.; Sharples, G.J.; Humbert, O.; Lloyd, R.G.; !1Claverys, J.P. !$#journal Mol. Microbiol. (1996) 19:1035-1045 !$#title The mmsA locus of Streptococcus pneumoniae encodes a !1RecG-like protein involved in DNA repair and in three-strand !1recombination. !$#cross-references MUID:96249697; PMID:8830261 !$#accession S71016 !'##status preliminary; nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-671 ##label MAR !'##cross-references EMBL:Z49988; NID:g1150618; PIDN:CAA90280.1; !1PID:g1150620 CLASSIFICATION #superfamily DNA helicase recG KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$280-287 #region nucleotide-binding motif A (P-loop)\ !$375-380 #region nucleotide-binding motif B\ !$379-382 #region DEXH motif SUMMARY #length 671 #molecular-weight 75188 #checksum 7350 SEQUENCE /// ENTRY E64139 #type complete TITLE DNA helicase recG protein - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS E64139; T09431 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession E64139 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-693 ##label TIGR !'##cross-references GB:U32847; GB:L42023; NID:g3212238; !1PIDN:AAC23387.1; PID:g1574599; TIGR:HI1740 REFERENCE Z16667 !$#authors White, O.; Clayton, R.A.; Kerlavage, A.R.; Fleischmann, !1R.D.; Peterson, J.; Hickey, E.; Dodson, R.; Gwinn, M. !$#submission submitted to the EMBL Data Library, May 1998 !$#accession T09431 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-693 ##label WHI !'##cross-references EMBL:U32847; NID:g3212238; PID:g1574599 GENETICS !$#gene recG; HI1740 CLASSIFICATION #superfamily DNA helicase recG KEYWORDS ATP; DNA binding; nucleotide binding; P-loop FEATURE !$296-303 #region nucleotide-binding motif A (P-loop)\ !$393-398 #region nucleotide-binding motif B\ !$397-400 #region DEXH motif SUMMARY #length 693 #molecular-weight 78085 #checksum 4137 SEQUENCE /// ENTRY JH0265 #type complete TITLE DNA recombinase (EC 3.6.1.-) - Escherichia coli (strain K-12) ALTERNATE_NAMES RecG protein ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS JH0265; S18195; F65166 REFERENCE JH0265 !$#authors Kalman, M.; Murphy, H.; Cashel, M. !$#journal Gene (1992) 110:95-99 !$#title The nucleotide sequence of recG, the distal spo operon gene !1in Escherichia coli K-12. !$#cross-references MUID:92184121; PMID:1544582 !$#accession JH0265 !'##molecule_type DNA !'##residues 1-693 ##label KAL !'##cross-references GB:M64367; NID:g147543; PIDN:AAA24513.1; !1PID:g147545 !'##experimental_source strain K12 REFERENCE S18195 !$#authors Lloyd, R.G.; Sharples, G.J. !$#journal J. Bacteriol. (1991) 173:6837-6843 !$#title Molecular organization and nucleotide sequence of the recG !1locus of Escherichia coli K-12. !$#cross-references MUID:92041567; PMID:1938888 !$#accession S18195 !'##status preliminary !'##molecule_type DNA !'##residues 1-693 ##label LLO !'##cross-references EMBL:X59550; NID:g42668; PIDN:CAA42123.1; !1PID:g42669 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65166 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-693 ##label BLAT !'##cross-references GB:AE000442; GB:U00096; NID:g2367253; !1PIDN:AAC76676.1; PID:g2367254; UWGP:b3652 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene recG !$#map_position 82 min CLASSIFICATION #superfamily DNA helicase recG KEYWORDS ATP; DNA binding; hydrolase; nucleotide binding; P-loop FEATURE !$296-303 #region nucleotide-binding motif A (P-loop)\ !$393-398 #region nucleotide-binding motif B\ !$397-400 #region DEXH motif SUMMARY #length 693 #molecular-weight 76430 #checksum 6052 SEQUENCE /// ENTRY S76355 #type complete TITLE DNA helicase recG - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S76355 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76355 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-831 ##label KAN !'##cross-references EMBL:D64000; GB:AB001339; NID:g1001484; !1PIDN:BAA10207.1; PID:g1001580 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily DNA helicase recG KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$433-440 #region nucleotide-binding motif A (P-loop)\ !$530-535 #region nucleotide-binding motif B\ !$534-537 #region DEXH motif SUMMARY #length 831 #molecular-weight 93658 #checksum 1732 SEQUENCE /// ENTRY I84741 #type complete TITLE RNA helicase - mouse ALTERNATE_NAMES RNA helicase ERH ORGANISM #formal_name Mus musculus #common_name house mouse DATE 18-Aug-2000 #sequence_revision 18-Aug-2000 #text_change 19-Jan-2001 ACCESSIONS I84741; S56112 REFERENCE I49731 !$#authors Gee, S.L.; Conboy, J.G. !$#journal Gene (1994) 140:171-177 !$#title Mouse erythroid cells express multiple putative RNA helicase !1genes exhibiting high sequence conservation from yeast to !1mammals. !$#cross-references MUID:94192995; PMID:8144024 !$#accession I84741 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-662 ##label RES !'##cross-references GB:L25126; NID:g407995; PIDN:AAA53630.1; !1PID:g407996 !'##genetics RES1 REFERENCE S56112 !$#authors Sowden, J.; Putt, W.; Morrison, K.; Beddington, R.; Edwards, !1Y. !$#journal Biochem. J. (1995) 308:839-846 !$#title The embryonic RNA helicase gene (ERH): a new member of the !1DEAD box family of RNA helicases. !$#cross-references MUID:97104282; PMID:8948440 !$#accession S56112 !'##molecule_type mRNA !'##residues 1-229,'R',231-662 ##label SOW !'##cross-references GB:Z38117; NID:g1835121; PID:g1835122 !'##experimental_source strain c57bl/6; notochord !'##genetics SOW1 !'##note the sequence is revised in GenBank entry MMDBRNAHL, release !1117, (PID:1835122) !'##note the revised sequence is now identical to PIR accession I84741 GENETICS RES1 !$#gene Eif4a-rs1; MGI:Ddx19 !'##cross-references MGI:99526 GENETICS SOW1 !$#gene MGI:Ddx3 !'##cross-references MGI:103064 !$#map_position 1 CLASSIFICATION #superfamily ATP-dependent RNA helicase DBP1 KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$224-231 #region nucleotide-binding motif A (P-loop)\ !$343-348 #region nucleotide-binding motif B\ !$347-350 #region DEAD motif SUMMARY #length 662 #molecular-weight 73101 #checksum 91 SEQUENCE /// ENTRY S13654 #type complete TITLE ATP-dependent RNA helicase - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S13654; S29676 REFERENCE S13654 !$#authors Gururajan, R.; Perry-O'Keefe, H.; Melton, D.A.; Weeks, D.L. !$#journal Nature (1991) 349:717-719 !$#title The Xenopus localized messenger RNA An3 may encode an !1ATP-dependent RNA helicase. !$#cross-references MUID:91141586; PMID:1996140 !$#accession S13654 !'##molecule_type mRNA !'##residues 1-697 ##label GUR !'##cross-references EMBL:X57328; NID:g65059; PIDN:CAA40605.1; !1PID:g65060 CLASSIFICATION #superfamily ATP-dependent RNA helicase DBP1 KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$260-272 #region ATP binding #status predicted\ !$265-272 #region nucleotide-binding motif A (P-loop)\ !$384-389 #region nucleotide-binding motif B\ !$386-398 #region ATP binding #status predicted\ !$388-391 #region DEAD motif SUMMARY #length 697 #molecular-weight 77302 #checksum 4426 SEQUENCE /// ENTRY I48385 #type complete TITLE RNA helicase TNZ2 - mouse ALTERNATE_NAMES p68 RNA helicase ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS I48385; S21453 REFERENCE I48385 !$#authors Lemaire, L.; Heinlein, U.A. !$#journal Life Sci. (1993) 52:917-926 !$#title High-level expression in male germ cells of murine P68 RNA !1helicase mRNA. !$#cross-references MUID:93188611; PMID:8445986 !$#accession I48385 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-614 ##label RES !'##cross-references EMBL:X65627; NID:g51262; PIDN:CAA46581.1; !1PID:g51263 GENETICS !$#gene TNZ2 CLASSIFICATION #superfamily ATP-dependent RNA helicase DBP1 KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$138-145 #region nucleotide-binding motif A (P-loop)\ !$244-249 #region nucleotide-binding motif B\ !$248-251 #region DEAD motif SUMMARY #length 614 #molecular-weight 69320 #checksum 4605 SEQUENCE /// ENTRY S14048 #type complete TITLE RNA helicase dbp2 [similarity] - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES nuclear protein p68; RNA-dependent ATPase dbp2 ORGANISM #formal_name Schizosaccharomyces pombe DATE 10-Sep-1999 #sequence_revision 18-Aug-2000 #text_change 19-Jan-2001 ACCESSIONS T40810; T43875; S14048 REFERENCE Z21949 !$#authors Beck, A.; Reinhardt, R.; Lyne, M.; Rajandream, M.A.; !1Barrell, B.G. !$#submission submitted to the EMBL Data Library, October 1998 !$#accession T40810 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-550 ##label BEC !'##cross-references EMBL:AL032684; PIDN:CAA21801.1; GSPDB:GN00067; !1SPDB:SPBP8B7.16c !'##experimental_source strain 972h-; clone p1 p8B7 REFERENCE S13757 !$#authors Iggo, R.D.; Jamieson, D.J.; MacNeill, S.A.; Southgate, J.; !1McPheat, J.; Lane, D.P. !$#journal Mol. Cell. Biol. (1991) 11:1326-1333 !$#title p68 RNA helicase: identification of a nucleolar form and !1cloning of related genes containing a conserved intron in !1yeasts. !$#cross-references MUID:91141480; PMID:1996094 !$#accession T43875 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-550 ##label IGG !'##cross-references EMBL:L11574; NID:g173418; PIDN:AAA35319.1; !1PID:g173419 !$#accession S14048 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-234,'L',236-239,'L',241-550 ##label IG2 !'##cross-references EMBL:X52648; NID:g5269; PIDN:CAA36873.1; PID:g5270 GENETICS !$#gene dbp2; SPBP8B7.16c !$#map_position 2 !$#introns 23/2; 434/1 CLASSIFICATION #superfamily ATP-dependent RNA helicase DBP1 KEYWORDS ATP; nucleotide binding; nucleus; P-loop FEATURE !$166-173 #region nucleotide-binding motif A (P-loop)\ !$272-277 #region nucleotide-binding motif B\ !$276-279 #region DEAD motif SUMMARY #length 550 #molecular-weight 61548 #checksum 100 SEQUENCE /// ENTRY S13757 #type complete TITLE RNA helicase DBP2 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES nuclear protein p68; protein N1945; protein YNL112w; RNA-dependent ATPase DBP2 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 14-Dec-2001 ACCESSIONS S13757; B39418; S63053; S67346 REFERENCE S13757 !$#authors Iggo, R.D.; Jamieson, D.J.; MacNeill, S.A.; Southgate, J.; !1McPheat, J.; Lane, D.P. !$#journal Mol. Cell. Biol. (1991) 11:1326-1333 !$#title p68 RNA helicase: identification of a nucleolar form and !1cloning of related genes containing a conserved intron in !1yeasts. !$#cross-references MUID:91141480; PMID:1996094 !$#accession S13757 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-546 ##label IGG !'##cross-references EMBL:X52649; NID:g5271; PIDN:CAA36874.1; PID:g5272 REFERENCE A39418 !$#authors Dequard-Chablat, M.; Riva, M.; Carles, C.; Sentenac, A. !$#journal J. Biol. Chem. (1991) 266:15300-15307 !$#title RPC19, the gene for a subunit common to yeast RNA !1polymerases A (I) and C (III). !$#cross-references MUID:91332053; PMID:1869554 !$#accession B39418 !'##molecule_type DNA !'##residues 1-18 ##label DEQ !'##cross-references GB:M64991 !'##note codons for the first eighteen amino acid residues of RNA !1helicase were found downstream of the RPC19 gene coding for !1the AC19 subunit of RNA polymerase REFERENCE S63047 !$#authors De Antoni, A.; D Angelo, M.; Dal Pero, F.; Sartorello, F.; !1Pandolfo, D.; Lanfranchi, G.; Valle, G. !$#submission submitted to the Protein Sequence Database, April 1996 !$#accession S63053 !'##molecule_type DNA !'##residues 1-546 ##label DEA !'##cross-references EMBL:Z71388; NID:g1302033; PIDN:CAA95991.1; !1PID:g1302034; GSPDB:GN00014; MIPS:YNL112w !'##experimental_source strain S288C REFERENCE S67327 !$#authors d'Antoni, A.; d'Angelo, M.; dal Pero, F.; Sartorello, F.; !1Pandolfo, D.; Lanfranchi, G.; Valle, G. !$#submission submitted to the EMBL Data Library, February 1996 !$#description The DNA sequence of cosmid 14-13b from chromosome XIV of !1Saccharomyces cerevisiae reveals an unusually high number of !1overlapping ORFs. !$#accession S67346 !'##molecule_type DNA !'##residues 1-424,'GN',426-546 ##label DAN !'##cross-references EMBL:Z69382; NID:g1183941; PIDN:CAA93395.1; !1PID:g1183961 GENETICS !$#gene SGD:DBP2; MIPS:YNL112w !'##cross-references SGD:S0005056; MIPS:YNL112w !$#map_position 14L !$#introns 425/1 CLASSIFICATION #superfamily ATP-dependent RNA helicase DBP1 KEYWORDS ATP; nucleotide binding; nucleus; P-loop FEATURE !$157-164 #region nucleotide-binding motif A (P-loop)\ !$263-268 #region nucleotide-binding motif B\ !$267-270 #region DEAD motif SUMMARY #length 546 #molecular-weight 60999 #checksum 483 SEQUENCE /// ENTRY S11485 #type complete TITLE RNA helicase - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S11485 REFERENCE S11485 !$#authors Dorer, D.R.; Christensen, A.C.; Johnson, D.H. !$#journal Nucleic Acids Res. (1990) 18:5489-5494 !$#title A novel RNA helicase gene tightly linked to the !1Triplo-lethal locus of Drosophila. !$#cross-references MUID:91016833; PMID:2170937 !$#accession S11485 !'##status preliminary !'##molecule_type mRNA !'##residues 1-575 ##label DOR !'##cross-references EMBL:X52846; NID:g8443; PIDN:CAA37037.1; PID:g8444 GENETICS !$#gene FlyBase:Rm62 !'##cross-references FlyBase:FBgn0003261 CLASSIFICATION #superfamily ATP-dependent RNA helicase DBP1 KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$181-188 #region nucleotide-binding motif A (P-loop)\ !$287-292 #region nucleotide-binding motif B\ !$291-294 #region DEAD motif SUMMARY #length 575 #molecular-weight 62329 #checksum 2050 SEQUENCE /// ENTRY S30805 #type complete TITLE probable RNA helicase CA3 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein G3210; protein YGL078c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S30805; B34848; S64085 REFERENCE S30805 !$#authors Johnston, M.; Nogae, I. !$#submission submitted to the EMBL Data Library, December 1991 !$#accession S30805 !'##molecule_type DNA !'##residues 1-523 ##label JOH !'##cross-references EMBL:M80437; NID:g172581; PIDN:AAA73137.1; !1PID:g172582 REFERENCE A34848 !$#authors Chang, T.H.; Arenas, J.; Abelson, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:1571-1575 !$#title Identification of five putative yeast RNA helicase genes. !$#cross-references MUID:90160368; PMID:2406722 !$#accession B34848 !'##molecule_type DNA !'##residues 260-440,'A',442-443,'I',445-448 ##label CHA REFERENCE S64071 !$#authors Rieger, M.; Mueller-Auer, S.; Brueckner, M.; Schaefer, M. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64085 !'##molecule_type DNA !'##residues 1-523 ##label RIE !'##cross-references EMBL:Z72600; NID:g1322594; PIDN:CAA96783.1; !1PID:g1322595; GSPDB:GN00007; MIPS:YGL078c !'##experimental_source strain S288C GENETICS !$#gene SGD:DBP3; MIPS:YGL078c !'##cross-references SGD:S0003046; MIPS:YGL078c !$#map_position 7L CLASSIFICATION #superfamily ATP-dependent RNA helicase DBP1 KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$156-163 #region nucleotide-binding motif A (P-loop)\ !$258-263 #region nucleotide-binding motif B\ !$262-265 #region DEAD motif SUMMARY #length 523 #molecular-weight 58826 #checksum 3235 SEQUENCE /// ENTRY S42639 #type complete TITLE ATP-dependent RNA helicase DB10 - wood tobacco ORGANISM #formal_name Nicotiana sylvestris #common_name wood tobacco DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S42639 REFERENCE S42639 !$#authors Itadani, H.; Sugita, M.; Sugiura, M. !$#journal Plant Mol. Biol. (1994) 24:249-252 !$#title Structure and expression of a cDNA encoding an RNA !1helicase-like protein in tobacco. !$#cross-references MUID:94154240; PMID:8111024 !$#accession S42639 !'##status preliminary !'##molecule_type mRNA !'##residues 1-607 ##label ITA !'##cross-references GB:D16247; NID:g466572; PIDN:BAA03763.1; !1PID:g563986 CLASSIFICATION #superfamily tobacco ATP-dependent RNA helicase DB10; WW !1repeat homology KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$18-56 #domain WW repeat homology #label WW1\ !$189-196 #region nucleotide-binding motif A (P-loop)\ !$294-299 #region nucleotide-binding motif B\ !$298-301 #region DEAD motif SUMMARY #length 607 #molecular-weight 65989 #checksum 1255 SEQUENCE /// ENTRY S31229 #type complete TITLE probable RNA helicase (EC 3.6.1.-) DHH1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein D1520; protein YDL160c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S31229; S61053; S67712; S21571 REFERENCE S31229 !$#authors Strahl-Bolsinger, S.; Tanner, W. !$#journal Yeast (1993) 9:429-432 !$#title A yeast gene encoding a putative RNA helicase of the !1"DEAD"-box family. !$#cross-references MUID:93289822; PMID:8511971 !$#accession S31229 !'##molecule_type DNA !'##residues 1-506 ##label STR !'##cross-references EMBL:X66057; NID:g4352; PIDN:CAA46853.1; PID:g4353 REFERENCE S61010 !$#authors Pohl, T.M. !$#submission submitted to the EMBL Data Library, November 1995 !$#accession S61053 !'##molecule_type DNA !'##residues 1-506 ##label POH !'##cross-references EMBL:Z67750; NID:g1061256; PIDN:CAA91586.1; !1PID:g1061279 REFERENCE S67708 !$#authors Pohl, T.M. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67712 !'##molecule_type DNA !'##residues 1-506 ##label POW !'##cross-references EMBL:Z74208; NID:g1431253; PIDN:CAA98734.1; !1PID:g1431254; GSPDB:GN00004; MIPS:YDL160c !'##experimental_source strain S288C GENETICS !$#gene SGD:DHH1; MIPS:YDL160c !'##cross-references SGD:S0002319; MIPS:YDL160c !$#map_position 4L CLASSIFICATION #superfamily ATP-dependent RNA helicase DHH1 KEYWORDS ATP; hydrolase; nucleotide binding; P-loop FEATURE !$90-97 #region nucleotide-binding motif A (P-loop)\ !$191-196 #region nucleotide-binding motif B\ !$195-198 #region DEAD motif SUMMARY #length 506 #molecular-weight 57544 #checksum 1312 SEQUENCE /// ENTRY S46654 #type complete TITLE probable ATP-dependent RNA helicase ste13p - fission yeast (Schizosaccharomyces pombe) ORGANISM #formal_name Schizosaccharomyces pombe DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S46654; T40679 REFERENCE S46654 !$#authors Maekawa, H.; Nakagawa, T.; Uno, Y.; Kitamura, K.; Shimoda, !1C. !$#journal Mol. Gen. Genet. (1994) 244:456-464 !$#title The ste13(+) gene encoding a putative RNA helicase is !1essential for nitrogen starvation-induced G1 arrest and !1initiation of sexual development in the fission yeast !1Schizosaccharomyces pombe. !$#cross-references MUID:94359471; PMID:8078473 !$#accession S46654 !'##molecule_type DNA !'##residues 1-485 ##label MAE !'##cross-references EMBL:D29795; NID:g474321; PIDN:BAA06178.1; !1PID:g703066 REFERENCE Z21944 !$#authors Lyne, M.; Rajandream, M.A.; Barrell, B.G.; Wedler, H.; !1Kutzner, M.; Wambutt, R. !$#submission submitted to the EMBL Data Library, January 1999 !$#accession T40679 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-485 ##label LYN !'##cross-references EMBL:AL035263; PIDN:CAA22882.1; GSPDB:GN00067; !1SPDB:SPBC776.09 !'##experimental_source strain 972h-; cosmid c776 GENETICS !$#gene ste13; SPBC776.09 !$#map_position 2 !$#introns 36/3; 53/2 CLASSIFICATION #superfamily ATP-dependent RNA helicase DHH1 KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$88-95 #region nucleotide-binding motif A (P-loop)\ !$189-194 #region nucleotide-binding motif B\ !$193-196 #region DEAD motif SUMMARY #length 485 #molecular-weight 54794 #checksum 8005 SEQUENCE /// ENTRY S22651 #type complete TITLE probable RNA helicase (EC 3.6.1.-) RCK - human ALTERNATE_NAMES 54K RNA helicase; DEAD box polypeptide 6; HLR2 protein; RCK protein ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S22651; I52691 REFERENCE S22651 !$#authors Lu, D.; Yunis, J.J. !$#journal Nucleic Acids Res. (1992) 20:1967-1972 !$#title Cloning, expression and localization of an RNA helicase gene !1from a human lymphoid cell line with chromosomal breakpoint !111q23.3. !$#cross-references MUID:92253419; PMID:1579499 !$#accession S22651 !'##status preliminary !'##molecule_type mRNA !'##residues 1-292,'E',294-483 ##label LUD !'##cross-references EMBL:Z11685; NID:g36096 !'##note the codon given for 293-Gln (GAG) is inconsistent with the !1authors' translation !'##note this ORF is not annotated in GenBank entry HSRNAHX, release 103 REFERENCE I52691 !$#authors Akao, Y.; Seto, M.; Yamamoto, K.; Iida, S.; Nakazawa, S.; !1Inazawa, J.; Abe, T.; Takahashi, T.; Ueda, R. !$#journal Cancer Res. (1992) 52:6083-6087 !$#title The RCK gene associated with t(11;14) translocation is !1distinct from the MLL/ALL-1 gene with t(4;11) and t(11;19) !1translocation. !$#cross-references MUID:93008012; PMID:1394235 !$#accession I52691 !'##molecule_type mRNA !'##residues 12-483 ##label AKO !'##cross-references GB:D17532; NID:g402515; PIDN:BAA04482.1; !1PID:g458727 GENETICS !$#gene GDB:DDX6; RCK; HLR2 !'##cross-references GDB:132676; OMIM:600326 !$#map_position 11q23.3-11q23.3 CLASSIFICATION #superfamily ATP-dependent RNA helicase DHH1 KEYWORDS ATP; hydrolase; nucleotide binding; P-loop FEATURE !$140-147 #region nucleotide-binding motif A (P-loop)\ !$242-247 #region nucleotide-binding motif B\ !$246-249 #region DEAD motif SUMMARY #length 483 #molecular-weight 54416 #checksum 8826 SEQUENCE /// ENTRY A38565 #type complete TITLE polycomb (Pc) protein - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A38565 REFERENCE A38565 !$#authors Paro, R.; Hogness, D.S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:263-267 !$#title The polycomb protein shares a homologous domain with a !1heterochromatin-associated protein of Drosophila. !$#cross-references MUID:91095442; PMID:1898775 !$#accession A38565 !'##status preliminary !'##molecule_type DNA !'##residues 1-390 ##label PAR !'##cross-references GB:X55702; NID:g8321; PIDN:CAA39229.1; PID:g603986 GENETICS !$#gene FlyBase:Pc !'##cross-references FlyBase:FBgn0003042 CLASSIFICATION #superfamily polycomb protein; chromobox homology FEATURE !$26-63 #domain chromobox homology #label CBH SUMMARY #length 390 #molecular-weight 43976 #checksum 1541 SEQUENCE /// ENTRY A47392 #type complete TITLE chromodomain-helicase-DNA-binding protein, CHD-1 - mouse ALTERNATE_NAMES KYBP protein ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Dec-2002 ACCESSIONS A47392; S21568 REFERENCE A47392 !$#authors Delmas, V.; Stokes, D.G.; Perry, R.P. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:2414-2418 !$#title A mammalian DNA-binding protein that contains a chromodomain !1and an SNF2/SWI2-like helicase domain. !$#cross-references MUID:93211972; PMID:8460153 !$#accession A47392 !'##status preliminary !'##molecule_type mRNA !'##residues 1-1711 ##label DEL !'##experimental_source S194 plasmacytoma cells !'##note sequence inconsistent with the nucleotide translation !'##note sequence extracted from NCBI backbone (NCBIN:128272, !1NCBIP:128273) REFERENCE S21568 !$#authors Delmas, V.; Perry, R.P. !$#submission submitted to the EMBL Data Library, May 1992 !$#description KYBP, a mammalian protein that contains the SNF2/SWI2 !1helicase domain also has DNA binding capability. !$#accession S21568 !'##molecule_type mRNA !'##residues 772-1711 ##label DE2 !'##cross-references EMBL:X66028 CLASSIFICATION #superfamily chromodomain helicase CHD1; chromobox homology KEYWORDS DNA binding FEATURE !$293-336 #domain chromobox homology #label CB1\ !$387-427 #domain chromobox homology #label CB2 SUMMARY #length 1711 #molecular-weight 196409 #checksum 7641 SEQUENCE /// ENTRY S30818 #type complete TITLE hypothetical protein YER164w - yeast (Saccharomyces cerevisiae) ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Dec-2002 ACCESSIONS S30818; S50667 REFERENCE S30812 !$#authors Mulligan, J.T.; Dietrich, F.S.; Hennessey, K.M.; Sehl, P.; !1Komp, C.; Wei, Y.; Taylor, P.; Nakahara, K.; Roberts, D.; !1Davis, R.W. !$#submission submitted to the EMBL Data Library, February 1993 !$#accession S30818 !'##molecule_type DNA !'##residues 1-1468 ##label MUL !'##cross-references GB:U18917; EMBL:L10718; NID:g603377; !1PIDN:AAB64691.1; PID:g603404 REFERENCE S50667 !$#authors Dietrich, F.S. !$#submission submitted to the EMBL Data Library, December 1994 !$#description The sequence of S. cerevisiae cosmids 8229, 9115, 9132, !19981, and lambda clones 7990 and 6134. !$#accession S50667 !'##molecule_type DNA !'##residues 1-1468 ##label DIE !'##cross-references EMBL:U18917; NID:g603377; PIDN:AAB64691.1; !1PID:g603404; GSPDB:GN00005; MIPS:YER164w GENETICS !$#gene SGD:CHD1; MIPS:YER164w !'##cross-references SGD:S0000966; MIPS:YER164w !$#map_position 5R CLASSIFICATION #superfamily chromodomain helicase CHD1; chromobox homology KEYWORDS DNA binding; nucleus FEATURE !$195-233 #domain chromobox homology #label CB1\ !$285-327 #domain chromobox homology #label CB2 SUMMARY #length 1468 #molecular-weight 168240 #checksum 8253 SEQUENCE /// ENTRY A25937 #type complete TITLE arsenical pump-driving ATPase (EC 3.6.1.-) - Escherichia coli plasmid R773 ORGANISM #formal_name Escherichia coli DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 19-Jan-2001 ACCESSIONS A25937 REFERENCE A92563 !$#authors Chen, C.M.; Misra, T.K.; Silver, S.; Rosen, B.P. !$#journal J. Biol. Chem. (1986) 261:15030-15038 !$#title Nucleotide sequence of the structural genes for an anion !1pump. !$#cross-references MUID:87033737; PMID:3021763 !$#accession A25937 !'##molecule_type DNA !'##residues 1-583 ##label CHE !'##cross-references GB:J02591 COMMENT This anion-transporting ATPase catalyzes the extrusion of !1the oxyanions arsenite, antimonite, and arsenate, thus !1lowering the intracellular concentration of these toxic !1oxyanions. GENETICS !$#gene arsA !$#genome plasmid CLASSIFICATION #superfamily Escherichia coli plasmid R773 arsenical !1pump-driving ATPase KEYWORDS ATP; hydrolase; nucleotide binding; P-loop; toxic oxyanion !1resistance FEATURE !$15-22 #region nucleotide-binding motif A (P-loop)\ !$117-121 #region nucleotide-binding motif B\ !$334-341 #region nucleotide-binding motif A (P-loop)\ !$443-447 #region nucleotide-binding motif B SUMMARY #length 583 #molecular-weight 63219 #checksum 8849 SEQUENCE /// ENTRY S15791 #type complete TITLE probable arsenical pump-driving ATPase (EC 3.6.1.-) - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S15791 REFERENCE S15786 !$#authors Craxton, M.; Ainscough, R.; Coulson, A.; Dear, S.; Du, Z.; !1Durbin, R.; Green, P.; Halloran, N.; Hawkins, T.; Hillier, !1L.; Kozono, Y.; Lee, C.; Lutterbach, B.; Metzstein, M.; Qiu, !1Q.; Shownkeen, R.; Staden, R.; Sulston, J.; Thierry-Mieg, !1J.; Thomas, K.; Waterston, R.; Wilson, R. !$#submission submitted to the EMBL Data Library, May 1991 !$#accession S15791 !'##molecule_type DNA !'##residues 1-342 ##label CRA !'##cross-references EMBL:Z11115; NID:g6953; PID:g6959 GENETICS !$#introns 145/2; 231/3; 301/3 CLASSIFICATION #superfamily arsenical pump-driving ATPase KEYWORDS ATP; hydrolase; nucleotide binding; P-loop FEATURE !$25-32 #region nucleotide-binding motif A (P-loop) SUMMARY #length 342 #molecular-weight 37554 #checksum 9491 SEQUENCE /// ENTRY S67642 #type complete TITLE probable arsenical pump-driving ATPase (EC 3.6.1.-) YDL100c - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein D2371 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S67642; S67419 REFERENCE S67629 !$#authors Ballesta, J.P.G.; Remacha, M.; Soler-Mira, A.; Jimenez, A.; !1Garcia-Cantalejo, J.M.; Boskovic, J.; del Rey, F.; Revuelta, !1J.L.; Buitrago, M.J.; Sanz, J.E. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67642 !'##molecule_type DNA !'##residues 1-354 ##label BAL !'##cross-references EMBL:Z74148; NID:g1431137; PIDN:CAA98667.1; !1PID:g1431138; GSPDB:GN00004; MIPS:YDL100c !'##experimental_source strain S288C REFERENCE S67406 !$#authors Boskovic, J.; Saiz, J.E.; Soler-Mira, A.; Garcia-Cantalejo, !1J.; Revuelta, J.L.; Jiminez, A.; Ballesta, J.P.G.; del Rey, !1F.; Remacha, M. !$#submission submitted to the EMBL Data Library, February 1996 !$#accession S67419 !'##molecule_type DNA !'##residues 1-354 ##label BOS !'##cross-references EMBL:X95644; NID:g1199535; PIDN:CAA64913.1; !1PID:g1199549 GENETICS !$#gene MIPS:YDL100c !'##cross-references SGD:S0002258 !$#map_position 4L CLASSIFICATION #superfamily arsenical pump-driving ATPase KEYWORDS ATP; hydrolase; nucleotide binding; P-loop FEATURE !$25-32 #region nucleotide-binding motif A (P-loop) SUMMARY #length 354 #molecular-weight 39353 #checksum 6101 SEQUENCE /// ENTRY F69068 #type complete TITLE probable arsenical pump-driving ATPase (EC 3.6.1.-) - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS F69068 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession F69068 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-324 ##label MTH !'##cross-references GB:AE000911; GB:AE000666; NID:g2622623; !1PIDN:AAB85986.1; PID:g2622629 !'##experimental_source strain Delta H GENETICS !$#gene MTH1511 CLASSIFICATION #superfamily arsenical pump-driving ATPase KEYWORDS ATP; hydrolase; nucleotide binding; P-loop FEATURE !$21-28 #region nucleotide-binding motif A (P-loop) SUMMARY #length 324 #molecular-weight 36544 #checksum 3267 SEQUENCE /// ENTRY E64442 #type complete TITLE probable arsenical pump-driving ATPase (EC 3.6.1.-) - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS E64442 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession E64442 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-349 ##label BUL !'##cross-references GB:U67556; GB:L77117; NID:g1591766; !1PIDN:AAB99142.1; PID:g1591774; TIGR:MJ1142 GENETICS !$#map_position FOR1081432-1082481 CLASSIFICATION #superfamily arsenical pump-driving ATPase KEYWORDS ATP; hydrolase; nucleotide binding; P-loop FEATURE !$33-40 #region nucleotide-binding motif A (P-loop) SUMMARY #length 349 #molecular-weight 39918 #checksum 7111 SEQUENCE /// ENTRY F70330 #type complete TITLE probable arsenical pump-driving ATPase (EC 3.6.1.-) - Aquifex aeolicus ALTERNATE_NAMES anion transporting ATPase ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS F70330 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession F70330 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-299 ##label AQF !'##cross-references GB:AE000684; NID:g2983009; PIDN:AAC06625.1; !1PID:g2983014; GB:AE000657 !'##experimental_source strain VF5 GENETICS !$#gene arsA2 CLASSIFICATION #superfamily arsenical pump-driving ATPase KEYWORDS ATP; hydrolase; nucleotide binding; P-loop FEATURE !$8-15 #region nucleotide-binding motif A (P-loop) SUMMARY #length 299 #molecular-weight 34559 #checksum 6513 SEQUENCE /// ENTRY HJAGI #type complete TITLE indoleacetamide hydrolase (EC 3.5.1.-) TA - Agrobacterium tumefaciens plasmid pTiTm4 ORGANISM #formal_name Agrobacterium tumefaciens DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 13-Jun-1997 ACCESSIONS S15001; S15452 REFERENCE S15001 !$#authors Bonnard, G.; Vincent, F.; Otten, L. !$#journal Plant Mol. Biol. (1991) 16:733-738 !$#title Sequence of Agrobacterium tumefaciens biotype III auxin !1genes. !$#cross-references MUID:91329707; PMID:1868204 !$#accession S15001 !'##molecule_type DNA !'##residues 1-467 ##label PLA !'##cross-references EMBL:X56185 GENETICS !$#gene iaaH !$#genome plasmid CLASSIFICATION #superfamily indoleacetamide hydrolase KEYWORDS hydrolase SUMMARY #length 467 #molecular-weight 49941 #checksum 153 SEQUENCE /// ENTRY S30104 #type complete TITLE indoleacetamide hydrolase (EC 3.5.1.-) - Agrobacterium vitis plasmid pTiS4 ORGANISM #formal_name Agrobacterium vitis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S30104 REFERENCE S30104 !$#authors Canaday, J.; Gerard, J.C.; Crouzet, P.; Otten, L. !$#journal Mol. Gen. Genet. (1992) 235:292-303 !$#title Organization and functional analysis of three T-DNAs from !1the vitopine Ti plasmid pTiS4. !$#cross-references MUID:93101133; PMID:1465104 !$#accession S30104 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-462 ##label CAN !'##cross-references EMBL:M91609; NID:g149127; PIDN:AAA98148.1; !1PID:g149128 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1992 GENETICS !$#gene iaaH !$#genome plasmid CLASSIFICATION #superfamily indoleacetamide hydrolase KEYWORDS hydrolase SUMMARY #length 462 #molecular-weight 49809 #checksum 8617 SEQUENCE /// ENTRY Q2AGAT #type complete TITLE indoleacetamide hydrolase (EC 3.5.1.-) - Agrobacterium tumefaciens plasmids ORGANISM #formal_name Agrobacterium tumefaciens DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 18-Jun-1999 ACCESSIONS A04501; B20966; S28686 REFERENCE A04501 !$#authors Sciaky, D.; Thomashow, M.F. !$#journal Nucleic Acids Res. (1984) 12:1447-1461 !$#title The sequence of the tms transcript 2 locus of the !1Agrobacterium tumefaciens plasmid pTiA6 and characterization !1of the mutation in pTiA66 that is responsible for auxin !1attenuation. !$#cross-references MUID:84144041; PMID:6366736 !$#accession A04501 !'##molecule_type DNA !'##residues 1-467 ##label SCI !'##cross-references GB:X00409; NID:g39176; PIDN:CAA25116.1; PID:g39177 REFERENCE A20966 !$#authors Klee, H.; Montoya, A.; Horodyski, F.; Lichtenstein, C.; !1Garfinkel, D.; Fuller, S.; Flores, C.; Peschon, J.; Nester, !1E.; Gordon, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:1728-1732 !$#title Nucleotide sequence of the tms genes of the pTiA6NC octopine !1Ti plasmid: two gene products involved in plant !1tumorigenesis. !$#cross-references MUID:84170374; PMID:6584906 !$#accession B20966 !'##status preliminary !'##molecule_type DNA !'##residues 1-467 ##label KLE !'##cross-references GB:K02553; NID:g154746; PIDN:AAA92549.1; !1PID:g455373 !'##experimental_source plasmid pTiA6 REFERENCE S28683 !$#authors Barker, R.F.; Idler, K.B.; Thompson, D.V.; Kemp, J.D. !$#journal Plant Mol. Biol. (1983) 2:335-350 !$#title Nucleotide sequence of the T-DNA region from the !1Agrobacterium tumefaciens octopine Ti plasmid pTi15955. !$#accession S28686 !'##status translation not shown !'##molecule_type DNA !'##residues 1-467 ##label BAR !'##cross-references EMBL:X00493; NID:g39062; PIDN:CAA25166.1; !1PID:g39066 !'##experimental_source plasmid pTi15955 !'##note the Ti plasmid in Agrobacterium induces tumor (crown gall) in !1dicotyledonous plants by transferring a plasmid segment from !1the bacterium to the plant cell GENETICS !$#gene tms !$#genome plasmid FUNCTION !$#description the transcript 2 gene, from which this protein is coded, may !1be responsible for the uncontrolled proliferation of plant !1cells in tumors CLASSIFICATION #superfamily indoleacetamide hydrolase KEYWORDS crown gall tumor; hydrolase SUMMARY #length 467 #molecular-weight 49805 #checksum 691 SEQUENCE /// ENTRY F64623 #type complete TITLE amidase - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS F64623 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession F64623 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-453 ##label TOM !'##cross-references GB:AE000594; GB:AE000511; NID:g2313957; !1PIDN:AAD07880.1; PID:g2313964; TIGR:HP0830 CLASSIFICATION #superfamily indoleacetamide hydrolase SUMMARY #length 453 #molecular-weight 49652 #checksum 3505 SEQUENCE /// ENTRY S77264 #type complete TITLE amidase slr0877 - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein slr0877 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S77264 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S77264 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-483 ##label KAN !'##cross-references EMBL:D90907; GB:AB001339; NID:g1652618; !1PIDN:BAA17598.1; PID:g1652678 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily indoleacetamide hydrolase SUMMARY #length 483 #molecular-weight 51470 #checksum 7995 SEQUENCE /// ENTRY S73920 #type complete TITLE amidase homolog G07_orf478V - Mycoplasma pneumoniae (strain ATCC 29342) ALTERNATE_NAMES hypothetical protein G07_orf478V ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Dec-1999 ACCESSIONS S73920 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73920 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-478 ##label HIM !'##cross-references EMBL:AE000058; GB:U00089; NID:g1674291; !1PIDN:AAB96242.1; PID:g1674296 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#genetic_code SGC3 !$#start_codon GTG CLASSIFICATION #superfamily indoleacetamide hydrolase SUMMARY #length 478 #molecular-weight 53229 #checksum 4205 SEQUENCE /// ENTRY S47454 #type complete TITLE amidase homolog YMR293c - yeast (Saccharomyces cerevisiae) ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S47454 REFERENCE S47445 !$#authors Barrell, B.G. !$#submission submitted to the EMBL Data Library, August 1994 !$#accession S47454 !'##molecule_type DNA !'##residues 1-464 ##label BAR !'##cross-references EMBL:X80836; NID:g1289327; PIDN:CAA56802.1; !1PID:g530350; GSPDB:GN00013; MIPS:YMR293c GENETICS !$#gene MIPS:YMR293c !'##cross-references SGD:S0004907 !$#map_position 13R CLASSIFICATION #superfamily indoleacetamide hydrolase SUMMARY #length 464 #molecular-weight 50918 #checksum 8601 SEQUENCE /// ENTRY A41326 #type complete TITLE enantiomer-selective amidase - Rhodococcus sp. ORGANISM #formal_name Rhodococcus sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A41326 REFERENCE A41326 !$#authors Mayaux, J.F.; Cerbelaud, E.; Soubrier, F.; Yeh, P.; Blanche, !1F.; Petre, D. !$#journal J. Bacteriol. (1991) 173:6694-6704 !$#title Purification, cloning, and primary structure of a new !1enantiomer-selective amidase from a Rhodococcus strain: !1structural evidence for a conserved genetic coupling with !1nitrile hydratase. !$#cross-references MUID:92041549; PMID:1938876 !$#accession A41326 !'##status preliminary !'##molecule_type DNA !'##residues 1-462 ##label MAY !'##cross-references GB:M74531; NID:g152051; PIDN:AAA26183.1; !1PID:g152052 CLASSIFICATION #superfamily indoleacetamide hydrolase SUMMARY #length 462 #molecular-weight 48609 #checksum 9836 SEQUENCE /// ENTRY B25493 #type complete TITLE indoleacetamide hydrolase - Pseudomonas syringae pv. savastanoi ORGANISM #formal_name Pseudomonas syringae pv. savastanoi DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B25493 REFERENCE A94062 !$#authors Yamada, T.; Palm, C.J.; Brooks, B.; Kosuge, T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:6522-6526 !$#title Nucleotide sequences of the Pseudomonas savastanoi !1indoleacetic acid genes show homology with Agrobacterium !1tumefaciens T-DNA. !$#accession B25493 !'##molecule_type DNA !'##residues 1-455 ##label YAM GENETICS !$#gene iaaH CLASSIFICATION #superfamily indoleacetamide hydrolase SUMMARY #length 455 #molecular-weight 48577 #checksum 390 SEQUENCE /// ENTRY S13642 #type complete TITLE thyroxine deiodinase (EC 3.8.1.4) type I - rat ALTERNATE_NAMES thyroxine 5-deiodinase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S13642 REFERENCE S13642 !$#authors Berry, M.J.; Banu, L.; Larsen, P.R. !$#journal Nature (1991) 349:438-440 !$#title Type I iodothyronine deiodinase is a !1selenocysteine-containing enzyme. !$#cross-references MUID:91125465; PMID:1825132 !$#accession S13642 !'##molecule_type mRNA !'##residues 1-257 ##label BER !'##cross-references EMBL:X57999; NID:g57330; PIDN:CAA41063.1; !1PID:g2654263 !'##note in Genbank entry RNTDEIOD, release 111.0, PID:g2654263 the !1selenocysteine UGA codon for residue 126 is translated as !1'X' FUNCTION !$#description catalyzes the reduction of L-thyroxine by a proton donor to !13',3'',5'-triiodo-L-thyronine and hydrogen iodide !$#note glutathione can serve as the proton donor; in spite of its !1Enzyme Commission classification, this enzyme is not a !1hydrolase but an oxidoreductase CLASSIFICATION #superfamily vertebrate thyroxine deiodinase I KEYWORDS oxidoreductase; selenocysteine FEATURE !$126 #modified_site selenocysteine #status predicted SUMMARY #length 257 #molecular-weight 29683 #checksum 7656 SEQUENCE /// ENTRY A42560 #type complete TITLE 4-chlorobenzoate dehalogenase (EC 3.8.1.6), 30K chain - Pseudomonas sp. (strain CBS-3) ORGANISM #formal_name Pseudomonas sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A42560 REFERENCE A42560 !$#authors Babbitt, P.C.; Kenyon, G.L.; Martin, B.M.; Charest, H.; !1Slyvestre, M.; Scholten, J.D.; Chang, K.H.; Liang, P.H.; !1Dunaway-Mariano, D. !$#journal Biochemistry (1992) 31:5594-5604 !$#title Ancestry of the 4-chlorobenzoate dehalogenase: analysis of !1amino acid sequence identities among families of acyl:adenyl !1ligases, enoyl-CoA hydratases/isomerases, and acyl-CoA !1thioesterases. !$#cross-references MUID:92304934; PMID:1351742 !$#accession A42560 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-269 ##label BAB CLASSIFICATION #superfamily 4-chlorobenzoate-CoA dehalogenase 30K chain; !1enoyl-CoA hydratase homology KEYWORDS hydrolase FEATURE !$25-182 #domain enoyl-CoA hydratase homology #label ECH SUMMARY #length 269 #molecular-weight 29843 #checksum 3259 SEQUENCE /// ENTRY A48956 #type complete TITLE 4-chlorobenzoate-CoA dehalogenase - Arthrobacter sp. ORGANISM #formal_name Arthrobacter sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A48956 REFERENCE A48956 !$#authors Schmitz, A.; Gartemann, K.H.; Fiedler, J.; Grund, E.; !1Eichenlaub, R. !$#journal Appl. Environ. Microbiol. (1992) 58:4068-4071 !$#title Cloning and sequence analysis of genes for dehalogenation of !14-chlorobenzoate from Arthrobacter sp. strain SU. !$#cross-references MUID:93119160; PMID:1476446 !$#accession A48956 !'##status preliminary !'##molecule_type DNA !'##residues 1-276 ##label SCH !'##cross-references GB:M93187; NID:g1941926; PIDN:AAC80223.1; !1PID:g142207 !'##experimental_source SU !'##note sequence extracted from NCBI backbone (NCBIN:121607, !1NCBIP:121609) CLASSIFICATION #superfamily 4-chlorobenzoate-CoA dehalogenase 30K chain; !1enoyl-CoA hydratase homology FEATURE !$29-185 #domain enoyl-CoA hydratase homology #label ECH SUMMARY #length 276 #molecular-weight 29899 #checksum 9695 SEQUENCE /// ENTRY A32515 #type complete TITLE acetolactate decarboxylase (EC 4.1.1.5) - Enterobacter aerogenes ORGANISM #formal_name Enterobacter aerogenes DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A32515; A47069 REFERENCE A32515 !$#authors Sone, H.; Fujii, T.; Kondo, K.; Shimizu, F.; Tanaka, J.I.; !1Inoue, T. !$#journal Appl. Environ. Microbiol. (1988) 54:38-42 !$#title Nucleotide sequence and expression of the Enterobacter !1aerogenes alpha-acetolactate decarboxylase gene in brewer's !1yeast. !$#cross-references MUID:88149041; PMID:3278689 !$#accession A32515 !'##molecule_type DNA !'##residues 1-260 ##label SON !'##cross-references GB:J03433; NID:g148344; PIDN:AAA24794.1; !1PID:g148345 !'##note it is uncertain whether Met-1, Met-2, or Met-3 is the initiator REFERENCE A47069 !$#authors Blomqvist, K.; Nikkola, M.; Lehtovaara, P.; Suihko, M.L.; !1Airaksinen, U.; Straby, K.B.; Knowles, J.K.; Penttila, M.E. !$#journal J. Bacteriol. (1993) 175:1392-1404 !$#title Characterization of the genes of the 2,3-butanediol operons !1from Klebsiella terrigena and Enterobacter aerogenes. !$#cross-references MUID:93186707; PMID:8444801 !$#accession A47069 !'##status preliminary !'##molecule_type DNA !'##residues 1-23,'Q',25-44,'V',46,'E',48-112,'NG',115-136,'V',139-256, !1'A',258-260 ##label BLO !'##cross-references GB:L04506; NID:g148342; PIDN:AAA56801.1; !1PID:g148343 !'##experimental_source VTT-E-87292 !'##note sequence extracted from NCBI backbone (NCBIN:126763, !1NCBIP:126764) COMMENT This enzyme is not secreted in this species. CLASSIFICATION #superfamily acetolactate decarboxylase KEYWORDS carbon-carbon lyase; carboxy-lyase SUMMARY #length 260 #molecular-weight 29031 #checksum 3256 SEQUENCE /// ENTRY C47069 #type complete TITLE acetolactate decarboxylase (EC 4.1.1.5) - Klebsiella terrigena ORGANISM #formal_name Klebsiella terrigena DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C47069 REFERENCE A47069 !$#authors Blomqvist, K.; Nikkola, M.; Lehtovaara, P.; Suihko, M.L.; !1Airaksinen, U.; Straby, K.B.; Knowles, J.K.; Penttila, M.E. !$#journal J. Bacteriol. (1993) 175:1392-1404 !$#title Characterization of the genes of the 2,3-butanediol operons !1from Klebsiella terrigena and Enterobacter aerogenes. !$#cross-references MUID:93186707; PMID:8444801 !$#accession C47069 !'##status preliminary !'##molecule_type DNA !'##residues 1-259 ##label BLO !'##cross-references GB:L04507; NID:g149170; PIDN:AAA25054.1; !1PID:g149171 !'##experimental_source VTT-E-74023 !'##note sequence extracted from NCBI backbone (NCBIN:126766, !1NCBIP:126767) CLASSIFICATION #superfamily acetolactate decarboxylase KEYWORDS carbon-carbon lyase; carboxy-lyase SUMMARY #length 259 #molecular-weight 29193 #checksum 1100 SEQUENCE /// ENTRY A37757 #type complete TITLE acetolactate decarboxylase (EC 4.1.1.5) precursor - Bacillus brevis ORGANISM #formal_name Bacillus brevis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A37757; A61026 REFERENCE A37757 !$#authors Diderichsen, B.; Wedsted, U.; Hedegaard, L.; Jensen, B.R.; !1Sjoholm, C. !$#journal J. Bacteriol. (1990) 172:4315-4321 !$#title Cloning of aldB, which encodes alpha-acetolactate !1decarboxylase, an exoenzyme from Bacillus brevis. !$#cross-references MUID:90330534; PMID:2198252 !$#accession A37757 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-285 ##label DID !'##note the amino end of both forms of the mature protein was confirmed !1by protein sequencing REFERENCE A61026 !$#authors Svendsen, I.; Jensen, B.R.; Ottesen, M. !$#journal Carlsberg Res. Commun. (1989) 54:157-163 !$#title Complete amino acid sequence of alpha-acetolactate !1decarboxylase from Bacillus brevis. !$#cross-references MUID:90180129; PMID:2627258 !$#accession A61026 !'##molecule_type protein !'##residues 26-106,'V',108-273,'Q',275-285 ##label SVE !'##note 58-Gly and 107-Thr were also found COMMENT This enzyme is secreted in this species. GENETICS !$#gene aldB CLASSIFICATION #superfamily acetolactate decarboxylase KEYWORDS carbon-carbon lyase; carboxy-lyase; extracellular protein FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-285 #product acetolactate decarboxylase, long form !8#status experimental #label MAL\ !$29-285 #product acetolactate decarboxylase, short form !8#status experimental #label MAS SUMMARY #length 285 #molecular-weight 31586 #checksum 363 SEQUENCE /// ENTRY B47126 #type complete TITLE acetolactate decarboxylase (EC 4.1.1.5) alsD - Bacillus subtilis ALTERNATE_NAMES alpha-acetolactate decarboxylase alsD ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS B47126; F69584 REFERENCE A47126 !$#authors Renna, M.C.; Najimudin, N.; Winik, L.R.; Zahler, S.A. !$#journal J. Bacteriol. (1993) 175:3863-3875 !$#title Regulation of the Bacillus subtilis alsS, alsD, and alsR !1genes involved in post-exponential-phase production of !1acetoin. !$#cross-references MUID:93286000; PMID:7685336 !$#accession B47126 !'##status preliminary !'##molecule_type DNA !'##residues 1-255 ##label REN !'##cross-references GB:L04470; NID:g142468; PIDN:AAA22223.1; !1PID:g142471 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69584 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-255 ##label KUN !'##cross-references GB:Z99122; GB:AL009126; NID:g2636029; !1PIDN:CAB15617.1; PID:g2636125 !'##experimental_source strain 168 GENETICS !$#gene alsD CLASSIFICATION #superfamily acetolactate decarboxylase KEYWORDS carbon-carbon lyase; carboxy-lyase SUMMARY #length 255 #molecular-weight 28799 #checksum 3010 SEQUENCE /// ENTRY S38533 #type complete TITLE glutamate decarboxylase (EC 4.1.1.15) 2 - mouse ALTERNATE_NAMES glutamate decarboxylase GAD65; L-glutamate 1-carboxy-lyase ORGANISM #formal_name Mus musculus #common_name house mouse DATE 20-May-1994 #sequence_revision 23-Mar-1995 #text_change 01-Dec-2000 ACCESSIONS S38533; I67412 REFERENCE S38533 !$#authors Lee, D.S.; Tian, J.; Phan, T.; Kaufman, D.L. !$#journal Biochim. Biophys. Acta (1993) 1216:157-160 !$#title Cloning and sequence analysis of a murine cDNA encoding !1glutamate decarboxylase (GAD65). !$#cross-references MUID:94032481; PMID:8218409 !$#accession S38533 !'##status preliminary !'##molecule_type mRNA !'##residues 1-585 ##label LEE !'##cross-references GB:L16980; NID:g413867; PIDN:AAA93049.1; !1PID:g413868 REFERENCE I53274 !$#authors Faulkner-Jones, B.E.; Cram, D.S.; Kun, J.; Harrison, L.C. !$#journal Endocrinology (1993) 133:2962-2972 !$#title Localization and quantitation of expression of two glutamate !1decarboxylase genes in pancreatic beta-cells and other !1peripheral tissues of mouse and rat. !$#cross-references MUID:94062679; PMID:8243324 !$#accession I67412 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 175-318,'S',320-379 ##label RES !'##cross-references GB:S67454; NID:g456852 COMMENT This enzyme (GAD) catalyzes the formation of an inhibitory !1neurotransmitter, gamma-aminobutyric acid, from L-glutamic !1acid; it has several isoforms, each encoded by a separate !1gene. CLASSIFICATION #superfamily human glutamate decarboxylase KEYWORDS carbon-carbon lyase; carboxy-lyase; phosphoprotein; !1pyridoxal phosphate FEATURE !$396 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 585 #molecular-weight 65224 #checksum 7599 SEQUENCE /// ENTRY B41935 #type complete TITLE glutamate decarboxylase (EC 4.1.1.15) 1 - human ALTERNATE_NAMES glutamate decarboxylase GAD67; L-glutamate 1-carboxy-lyase ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1993 #sequence_revision 23-Mar-1995 #text_change 18-Jun-1999 ACCESSIONS B41935; JH0805; JH0806; A61406; PQ0157; PQ0158; B41367; !1A36463; A54778 REFERENCE A41935 !$#authors Bu, D.F.; Erlander, M.G.; Hitz, B.C.; Tillakaratne, N.J.K.; !1Kaufman, D.L.; Wagner-McPherson, C.B.; Evans, G.A.; Tobin, !1A.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:2115-2119 !$#title Two human glutamate decarboxylases, 65-kDa GAD and 67-kDa !1GAD, are each encoded by a single gene. !$#cross-references MUID:92196068; PMID:1549570 !$#accession B41935 !'##molecule_type mRNA !'##residues 1-594 ##label BU1 !'##cross-references GB:M81883; NID:g182935; PIDN:AAA62368.1; !1PID:g182936 !'##experimental_source pancreatic islet !'##note sequence extracted from NCBI backbone (NCBIP:88006) REFERENCE JH0805 !$#authors Kawasaki, E.; Moriuchi, R.; Watanabe, M.; Saitoh, K.; !1Charles Brunicardi, F.; Watt, P.C.; Yamaguchi, T.; Mullen, !1Y.; Akazawa, S.; Miyamoto, T.; Nagataki, S. !$#journal Biochem. Biophys. Res. Commun. (1993) 192:1353-1359 !$#title Cloning and expression of large isoform of glutamic acid !1decarboxylase from human pancreatic islet. !$#cross-references MUID:93282845; PMID:8507203 !$#accession JH0805 !'##molecule_type mRNA !'##residues 1-17,'N',19-30,'N',32-67,'K',69-115,'L',117-154,'T', !1156-301,'C',303-476,'G',478-491,'G',493-594 ##label KAW !'##cross-references GB:S61898; NID:g385310; PIDN:AAB26938.1; !1PID:g385311 !'##experimental_source pancreatic islet REFERENCE JH0806 !$#authors Yamashita, K.; Cram, D.S.; Harrison, L.C. !$#journal Biochem. Biophys. Res. Commun. (1993) 192:1347-1352 !$#title Molecular cloning of full-length glutamic acid decarboxylase !167 from human pancreas and islets. !$#cross-references MUID:93282844; PMID:8507202 !$#accession JH0806 !'##molecule_type mRNA !'##residues 1-67,'K',69-435,'L',437-511,'S',513-594 ##label YAM !'##cross-references GB:S61897; NID:g385450; PIDN:AAB26937.1; !1PID:g385451 !'##experimental_source pancreatic islet REFERENCE A61406 !$#authors Kelly, C.; Carter, N.D.; Johnstone, A.P.; Nussey, S.S. !$#journal Lancet (1991) 338:1468-1469 !$#title Cloning of large isoform of human brain glutamic acid !1decarboxylase. !$#cross-references MUID:92065769; PMID:1683462 !$#accession A61406 !'##molecule_type mRNA !'##residues 62-67,'K',69-205,'N',207-564,'L',566-594 ##label KEL !'##experimental_source brain REFERENCE PQ0157 !$#authors Cram, D.S.; Barnett, L.D.; Joseph, J.L.; Harrison, L.C. !$#journal Biochem. Biophys. Res. Commun. (1991) 176:1239-1244 !$#title Cloning and partial nucleotide sequence of human glutamic !1acid decarboxylase cDNA from brain and pancreatic islets. !$#cross-references MUID:91248209; PMID:2039509 !$#accession PQ0157 !'##molecule_type mRNA !'##residues 218-463 ##label CR1 !'##cross-references GB:M70434 !'##experimental_source brain !$#accession PQ0158 !'##molecule_type mRNA !'##residues 218-234,'K',236-240,'N',242-288,'H',290-323,'L',325-329, !1'D',331-338,'L',340-390,'S',392-397 ##label CR2 !'##cross-references GB:M70435; NID:g182941; PIDN:AAA52513.1; !1PID:g182942 !'##experimental_source pancreatic islet REFERENCE A41367 !$#authors Michelsen, B.K.; Petersen, J.S.; Boel, E.; Moldrup, A.; !1Dyrberg, T.; Madsen, O.D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:8754-8758 !$#title Cloning, characterization, and autoimmune recognition of rat !1islet glutamic acid decarboxylase in insulin-dependent !1diabetes mellitus. !$#cross-references MUID:92020930; PMID:1924335 !$#accession B41367 !'##molecule_type mRNA !'##residues 317-482,'R',484-594 ##label MIC REFERENCE A36463 !$#authors Persson, H.; Pelto-Huikko, M.; Metsis, M.; Soeder, O.; !1Brene, S.; Skog, S.; Hoekfelt, T.; Ritzen, E.M. !$#journal Mol. Cell. Biol. (1990) 10:4701-4711 !$#title Expression of the neurotransmitter-synthesizing enzyme !1glutamic acid decarboxylase in male germ cells. !$#cross-references MUID:90355986; PMID:1697032 !$#accession A36463 !'##molecule_type mRNA !'##residues 527-594 ##label PER !'##cross-references GB:M55574; NID:g182929; PIDN:AAA72938.1; !1PID:g182930 REFERENCE A54778 !$#authors Bu, D.F.; Tobin, A.J. !$#journal Genomics (1994) 21:222-228 !$#title The exon-intron organization of the genes (GAD1 and GAD2) !1encoding two human glutamate decarboxylases (GAD-67 and !1GAD-65) suggests that they derive from a common ancestral !1GAD. !$#cross-references MUID:94375018; PMID:8088791 !$#contents annotation; intron-exon organization COMMENT This enzyme (GAD) catalyzes the formation of an inhibitory !1neurotransmitter, gamma-aminobutyric acid, from L-glutamic !1acid; it has several isoforms, each encoded by a separate !1gene. GAD has also been implicated as an autoantigen in !1autoimmune disease stiff-man syndrome and insulin-dependent !1diabetes mellitus. GENETICS !$#gene GDB:GAD1; GAD !'##cross-references GDB:119244; OMIM:266100 !$#map_position 2q31-2q31 CLASSIFICATION #superfamily human glutamate decarboxylase KEYWORDS alternative splicing; carbon-carbon lyase; carboxy-lyase; !1phosphoprotein; pyridoxal phosphate FEATURE !$405 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 594 #molecular-weight 66924 #checksum 6189 SEQUENCE /// ENTRY A46758 #type complete TITLE glutamate decarboxylase (EC 4.1.1.15) 1 - cat ALTERNATE_NAMES glutamate decarboxylase GAD67; L-glutamate 1-carboxy-lyase ORGANISM #formal_name Felis silvestris catus #common_name domestic cat DATE 31-Dec-1993 #sequence_revision 23-Mar-1995 #text_change 18-Jun-1999 ACCESSIONS A46758; A45671 REFERENCE A46758 !$#authors Kobayashi, Y.; Kaufman, D.L.; Tobin, A.J. !$#submission submitted to GenBank, September 1989 !$#accession A46758 !'##molecule_type mRNA !'##residues 1-594 ##label KOB !'##cross-references GB:M18629; NID:g163858; PIDN:AAA51430.1; !1PID:g163859 REFERENCE A45671 !$#authors Kobayashi, Y.; Kaufman, D.L.; Tobin, A.J. !$#journal J. Neurosci. (1987) 7:2768-2772 !$#title Glutamic acid decarboxylase cDNA: nucleotide sequence !1encoding an enzymatically active fusion protein. !$#cross-references MUID:87310623; PMID:3453123 !$#accession A45671 !'##molecule_type mRNA !'##residues 1-558,'RGTRPTFSGWSSRTQLLHSPILTSSSRR' ##label KO2 !'##note this sequence has been revised in reference A46758 COMMENT This enzyme (GAD) catalyzes the formation of an inhibitory !1neurotransmitter, gamma-aminobutyric acid, from L-glutamic !1acid; it has several isoforms, each encoded by a separate !1gene. GENETICS !$#gene GAD1 CLASSIFICATION #superfamily human glutamate decarboxylase KEYWORDS carbon-carbon lyase; carboxy-lyase; phosphoprotein; !1pyridoxal phosphate FEATURE !$405 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 594 #molecular-weight 66824 #checksum 5630 SEQUENCE /// ENTRY A41367 #type complete TITLE glutamate decarboxylase (EC 4.1.1.15) 1 - rat ALTERNATE_NAMES glutamate decarboxylase GAD67; L-glutamate 1-carboxy-lyase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 12-Jun-1992 #sequence_revision 23-Mar-1995 #text_change 18-Jun-1999 ACCESSIONS A41367; A43756; JH0195 REFERENCE A41367 !$#authors Michelsen, B.K.; Petersen, J.S.; Boel, E.; Moldrup, A.; !1Dyrberg, T.; Madsen, O.D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:8754-8758 !$#title Cloning, characterization, and autoimmune recognition of rat !1islet glutamic acid decarboxylase in insulin-dependent !1diabetes mellitus. !$#cross-references MUID:92020930; PMID:1924335 !$#accession A41367 !'##status preliminary !'##molecule_type mRNA !'##residues 1-593 ##label MIC !'##cross-references GB:M76177; NID:g204227; PIDN:AAA41184.1; !1PID:g204228 REFERENCE A43756 !$#authors Wyborski, R.J.; Bond, R.W.; Gottlieb, D.I. !$#journal Brain Res. Mol. Brain Res. (1990) 8:193-198 !$#title Characterization of a cDNA coding for rat glutamic acid !1decarboxylase. !$#cross-references MUID:91014554; PMID:2170798 !$#accession A43756 !'##status preliminary !'##molecule_type mRNA !'##residues 1-593 ##label WYB !'##cross-references GB:X57573; NID:g56183; PIDN:CAA40801.1; PID:g56184 !'##note the authors translated the codon TGT for residue 412 as Ser and !1TCT for residue 413 as Cys REFERENCE JH0195 !$#authors Julien, J.F.; Samama, P.; Mallet, J. !$#journal J. Neurochem. (1990) 54:703-705 !$#title Rat brain glutamic acid decarboxylase sequence deduced from !1a cloned cDNA. !$#cross-references MUID:90132703; PMID:2299361 !$#accession JH0195 !'##molecule_type mRNA !'##residues 1-102,'V',104-283,'S',285-286,'AD',289-343,'EA',346,'I', !1348-351,'LE',354-379,'R',381-593 ##label JUL !'##cross-references GB:X57572; NID:g56185; PIDN:CAA40800.1; PID:g56186 COMMENT This enzyme (GAD) catalyzes the formation of an inhibitory !1neurotransmitter, gamma-aminobutyric acid, from L-glutamic !1acid; it has several isoforms, each encoded by a separate !1gene. CLASSIFICATION #superfamily human glutamate decarboxylase KEYWORDS carbon-carbon lyase; carboxy-lyase; phosphoprotein; !1pyridoxal phosphate FEATURE !$404 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 593 #molecular-weight 66640 #checksum 3971 SEQUENCE /// ENTRY A30999 #type complete TITLE glutamate decarboxylase (EC 4.1.1.15) C1 - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES L-glutamate 1-carboxy-lyase ORGANISM #formal_name Drosophila melanogaster DATE 26-Oct-1989 #sequence_revision 23-Mar-1995 #text_change 18-Jun-1999 ACCESSIONS JH0192; PS0301; A30999 REFERENCE JH0192 !$#authors Jackson, F.R.; Newby, L.M.; Kulkarni, S.J. !$#journal J. Neurochem. (1990) 54:1068-1078 !$#title Drosophila GABAergic systems; sequence and expression of !1glutamic acid decarboxylase. !$#cross-references MUID:90155291; PMID:1689376 !$#accession JH0192 !'##molecule_type mRNA !'##residues 1-510 ##label JAC !'##cross-references GB:X76198; NID:g433082; PIDN:CAA53791.1; !1PID:g433083 !$#accession PS0301 !'##molecule_type mRNA !'##residues 156-200,'F',202-300,'K',302-384,'L',386-510 ##label JA2 COMMENT This enzyme (GAD) catalyzes the formation of an inhibitory !1neurotransmitter, gamma-aminobutyric acid, from L-glutamic !1acid; it has several isoforms, each encoded by a separate !1gene. GENETICS !$#gene FlyBase:Gad1 !'##cross-references FlyBase:FBgn0004516 CLASSIFICATION #superfamily human glutamate decarboxylase KEYWORDS carbon-carbon lyase; carboxy-lyase; phosphoprotein; !1pyridoxal phosphate FEATURE !$322 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 510 #molecular-weight 57758 #checksum 3194 SEQUENCE /// ENTRY A41292 #type complete TITLE glutamate decarboxylase (EC 4.1.1.15) 2 - human ALTERNATE_NAMES glutamate decarboxylase GAD65; L-glutamate 1-carboxy-lyase ORGANISM #formal_name Homo sapiens #common_name man DATE 13-May-1992 #sequence_revision 23-Mar-1995 #text_change 18-Jun-1999 ACCESSIONS A41935; A41292; S30058; B54778 REFERENCE A41935 !$#authors Bu, D.F.; Erlander, M.G.; Hitz, B.C.; Tillakaratne, N.J.K.; !1Kaufman, D.L.; Wagner-McPherson, C.B.; Evans, G.A.; Tobin, !1A.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:2115-2119 !$#title Two human glutamate decarboxylases, 65-kDa GAD and 67-kDa !1GAD, are each encoded by a single gene. !$#cross-references MUID:92196068; PMID:1549570 !$#accession A41935 !'##molecule_type mRNA !'##residues 1-585 ##label BU1 !'##cross-references GB:M81882; NID:g182933; PIDN:AAA62367.1; !1PID:g182934 !'##experimental_source brain !'##note sequence extracted from NCBI backbone (NCBIP:88007) REFERENCE A41292 !$#authors Karlsen, A.E.; Hagopian, W.A.; Grubin, C.E.; Dube, S.; !1Disteche, C.M.; Adler, D.A.; Baermeier, H.; Mathewes, S.; !1Grant, F.J.; Foster, D.; Lernmark, A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:8337-8341 !$#title Cloning and primary structure of a human islet isoform of !1glutamic acid decarboxylase from chromosome 10. !$#cross-references MUID:92020848; PMID:1924293 !$#accession A41292 !'##molecule_type mRNA !'##residues 1-585 ##label KAR !'##cross-references GB:M74826; NID:g182931; PIDN:AAA58491.1; !1PID:g182932 !'##experimental_source pancreatic islet REFERENCE S30058 !$#authors Mauch, L.; Abney, C.C.; Berg, H.; Scherbaum, W.A.; !1Liedvogel, B.; Northemann, W. !$#journal Eur. J. Biochem. (1993) 212:597-603 !$#title Characterization of a linear epitope within the human !1pancreatic 64-kDa glutamic acid decarboxylase and its !1autoimmune recognition by sera from insulin-dependent !1diabetes mellitus patients. !$#cross-references MUID:93185681; PMID:7680313 !$#accession S30058 !'##molecule_type mRNA !'##residues 6-585 ##label MAU !'##cross-references EMBL:X69936 !'##experimental_source pancreatic islet REFERENCE A54778 !$#authors Bu, D.F.; Tobin, A.J. !$#journal Genomics (1994) 21:222-228 !$#title The exon-intron organization of the genes (GAD1 and GAD2) !1encoding two human glutamate decarboxylases (GAD-67 and !1GAD-65) suggests that they derive from a common ancestral !1GAD. !$#cross-references MUID:94375018; PMID:8088791 !$#contents annotation; intron-exon boundaries COMMENT This enzyme (GAD) catalyzes the formation of an inhibitory !1neurotransmitter, gamma-aminobutyric acid, from L-glutamic !1acid; it has several isoforms, each encoded by a separate !1gene. GAD has also been implicated as an autoantigen in !1autoimmune disease stiff-man syndrome and insulin-dependent !1diabetes mellitus. GENETICS !$#gene GDB:GAD2 !'##cross-references GDB:128595; OMIM:138275 !$#map_position 10p11.23-10p11.23 CLASSIFICATION #superfamily human glutamate decarboxylase KEYWORDS carbon-carbon lyase; carboxy-lyase; phosphoprotein; !1pyridoxal phosphate FEATURE !$396 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 585 #molecular-weight 65411 #checksum 4799 SEQUENCE /// ENTRY JH0423 #type complete TITLE glutamate decarboxylase (EC 4.1.1.15) 2 [validated] - rat ALTERNATE_NAMES glutamate decarboxylase GAD65; L-glutamate 1-carboxy-lyase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1992 #sequence_revision 23-Mar-1995 #text_change 26-May-2000 ACCESSIONS JH0423; A60888 REFERENCE JH0423 !$#authors Erlander, M.G.; Tillakaratne, N.J.K.; Feldblum, S.; Patel, !1N.; Tobin, A.J. !$#journal Neuron (1991) 7:91-100 !$#title Two genes encode distinct glutamate decarboxylases. !$#cross-references MUID:91299343; PMID:2069816 !$#accession JH0423 !'##molecule_type mRNA !'##residues 1-585 ##label ERL !'##cross-references GB:M72422; NID:g204225; PIDN:AAA63488.1; !1PID:g204226 !'##experimental_source brain !'##note the authors translated the codon GAT for residue 86 as His, TCA !1for residue 198 as Ala, and CAG for residue 428 as Trp REFERENCE A60888 !$#authors Chang, Y.C.; Gottlieb, D.I. !$#journal J. Neurosci. (1988) 8:2123-2130 !$#title Characterization of the proteins purified with monoclonal !1antibodies to glutamic acid decarboxylase. !$#cross-references MUID:88258610; PMID:3385490 !$#accession A60888 !'##status preliminary !'##molecule_type protein !'##residues 'V',191-194,'X',196-203,'XX',206-219;'X',225-234,'X', !1236-247,'X',249-266,'X';524-537,539-543,'V',547-549,'X', !1551-553,'X',555-558 ##label CHA FUNCTION !$#description EC 4.1.1.15 [validated, MUID:88258610]; catalyzes the !1conversion of L-glutamic acid into gamma-aminobutyric acid !$#note gamma-aminobutyric acid is an inhibitory neurotransmitter CLASSIFICATION #superfamily human glutamate decarboxylase KEYWORDS carbon-carbon lyase; carboxy-lyase; phosphoprotein; !1pyridoxal phosphate FEATURE !$396 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 585 #molecular-weight 65402 #checksum 7756 SEQUENCE /// ENTRY JH0827 #type complete TITLE glutamate decarboxylase (EC 4.1.1.15) C2 - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES L-glutamate 1-carboxy-lyase ORGANISM #formal_name Drosophila melanogaster DATE 30-Sep-1993 #sequence_revision 23-Mar-1995 #text_change 28-May-1999 ACCESSIONS JH0827 REFERENCE JH0827 !$#authors Phillips, A.M.; Salkoff, L.B.; Kelly, L.E. !$#journal J. Neurochem. (1993) 61:1291-1301 !$#title A neural gene from Drosophila melanogaster with homology to !1vertebrate and invertebrate glutamate decarboxylases. !$#cross-references MUID:93389479; PMID:8376987 !$#accession JH0827 !'##molecule_type mRNA !'##residues 1-575 ##label PHI !'##cross-references GB:U01239; NID:g402251; PIDN:AAC46466.1; !1PID:g402252 COMMENT This enzyme (GAD) catalyzes the formation of an inhibitory !1neurotransmitter, gamma-aminobutyric acid, from L-glutamic !1acid; it has several isoforms, each encoded by a separate !1gene. GENETICS !$#gene FlyBase:Gad2 !'##cross-references FlyBase:FBgn0005622 CLASSIFICATION #superfamily human glutamate decarboxylase KEYWORDS carbon-carbon lyase; carboxy-lyase; phosphoprotein; !1pyridoxal phosphate FEATURE !$68-76 #region asparagine-rich\ !$153-251 #domain substrate binding #status predicted #label !8SBB\ !$324-460 #domain decarboxylation #status predicted #label DEC\ !$387 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 575 #molecular-weight 64795 #checksum 6232 SEQUENCE /// ENTRY B43332 #type complete TITLE glutamate decarboxylase (EC 4.1.1.15) beta - Escherichia coli (strain K-12) ALTERNATE_NAMES L-glutamate 1-carboxy-lyase ORGANISM #formal_name Escherichia coli DATE 10-Mar-1994 #sequence_revision 23-Mar-1995 #text_change 01-Mar-2002 ACCESSIONS B43332; S30261; H64902 REFERENCE A43332 !$#authors Smith, D.K.; Kassam, T.; Singh, B.; Elliott, J.F. !$#journal J. Bacteriol. (1992) 174:5820-5826 !$#title Escherichia coli has two homologous glutamate decarboxylase !1genes that map to distinct loci. !$#cross-references MUID:92394884; PMID:1522060 !$#accession B43332 !'##molecule_type DNA !'##residues 1-466 ##label SMI !'##cross-references GB:M84025; NID:g146059; PIDN:AAA23834.1; !1PID:g146060 REFERENCE S30261 !$#authors Yoshida, T.; Ueguchi, C.; Yamada, H.; Mizuno, T. !$#journal Mol. Gen. Genet. (1993) 237:113-122 !$#title Function of the Escherichia coli nucleoid protein, H-NS: !1molecular analysis of a subset of proteins whose expression !1is enhanced in a hns deletion mutant. !$#cross-references MUID:93204884; PMID:8455549 !$#accession S30261 !'##molecule_type protein !'##residues 1-4,'LQVL',7-15 ##label YOS REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64902 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-466 ##label BLAT !'##cross-references GB:AE000246; GB:U00096; NID:g1787764; !1PIDN:AAC74566.1; PID:g1787769; UWGP:b1493 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene gadB !$#map_position 78 min FUNCTION !$#description catalyzes the formation of gamma-aminobutyric acid, from !1L-glutamic acid !$#note in E. coli, two isoforms (alpha and beta) have been found, !1each encoded by a separate gene CLASSIFICATION #superfamily Escherichia coli glutamate decarboxylase KEYWORDS carbon-carbon lyase; carboxy-lyase; homohexamer; !1phosphoprotein; pyridoxal phosphate FEATURE !$276 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 466 #molecular-weight 52668 #checksum 1993 SEQUENCE /// ENTRY S24234 #type complete TITLE glutamate decarboxylase (EC 4.1.1.15) alpha - Escherichia coli (strain K-12) ALTERNATE_NAMES GAD alpha protein; L-glutamate 1-carboxy-lyase ORGANISM #formal_name Escherichia coli DATE 22-Jan-1993 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS S47737; H65149; S24234; S23421; A43332; PN0616 REFERENCE S47666 !$#authors Plunkett, G. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S47737 !'##status preliminary !'##molecule_type DNA !'##residues 1-466 ##label PLU !'##cross-references EMBL:U00039; NID:g466582; PIDN:AAB18493.1; !1PID:g466654 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65149 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-466 ##label BLAT !'##cross-references GB:AE000428; GB:U00096; NID:g1789931; !1PIDN:AAC76542.1; PID:g1789934; UWGP:b3517 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S23421 !$#authors Maras, B.; Sweeney, G.; Barra, D.; Bossa, F.; John, R.A. !$#journal Eur. J. Biochem. (1992) 204:93-98 !$#title The amino acid sequence of glutamate decarboxylase from !1Escherichia coli. Evolutionary relationship between !1mammalian and bacterial enzymes. !$#cross-references MUID:92155241; PMID:1740158 !$#accession S24234 !'##molecule_type protein !'##residues 1-63,'S',65-72,'R',74-152,'N',154-164,'S',166-354,'N', !1356-466 ##label MAR !$#accession S23421 !'##molecule_type DNA !'##residues 148-164,'S',166-207,'N',209-294,'V',296-431 ##label MAR1 !'##cross-references GB:X63123; NID:g41601; PIDN:CAA44834.1; PID:g938166 REFERENCE A43332 !$#authors Smith, D.K.; Kassam, T.; Singh, B.; Elliott, J.F. !$#journal J. Bacteriol. (1992) 174:5820-5826 !$#title Escherichia coli has two homologous glutamate decarboxylase !1genes that map to distinct loci. !$#cross-references MUID:92394884; PMID:1522060 !$#accession A43332 !'##molecule_type DNA !'##residues 1-466 ##label SMI !'##cross-references GB:M84024; NID:g146057; PIDN:AAA23833.1; !1PID:g146058 !'##note sequence extracted from NCBI backbone (NCBIN:112979, !1NCBIP:112980) REFERENCE PN0616 !$#authors Yoshida, T.; Yamashino, T.; Ueguchi, C.; Mizuno, T. !$#journal Biosci. Biotechnol. Biochem. (1993) 57:1568-1569 !$#title Expression of the Escherichia coli dimorphic glutamic acid !1decarboxylases is regulated by the nucleoid protein H-NS. !$#cross-references MUID:94033862; PMID:7764225 !$#accession PN0616 !'##molecule_type protein !'##residues 1-21,'X' ##label YOS GENETICS !$#gene gadA !$#map_position 78 min FUNCTION !$#description catalyzes the formation of gamma-aminobutyric acid, from !1L-glutamic acid !$#note in E. coli, two isoforms (alpha and beta) have been found, !1each encoded by a separate gene CLASSIFICATION #superfamily Escherichia coli glutamate decarboxylase KEYWORDS carbon-carbon lyase; carboxy-lyase; homohexamer; !1phosphoprotein; pyridoxal phosphate FEATURE !$276 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 466 #molecular-weight 52685 #checksum 1476 SEQUENCE /// ENTRY DCHUO #type complete TITLE ornithine decarboxylase (EC 4.1.1.17) - human ALTERNATE_NAMES ODC ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS S06900; A33388; JQ0792; A26957; S14539; A46555; I38077 REFERENCE S06900 !$#authors van Steeg, H.; van Oostrom, C.T.M.; Martens, J.W.M.; van !1Kreyl, C.F.; Schepens, J.; Wieringa, B. !$#journal Nucleic Acids Res. (1989) 17:8855-8856 !$#title Nucleotide sequence of the human ornithine decarboxylase !1gene. !$#cross-references MUID:90067851; PMID:2587220 !$#accession S06900 !'##status translation not shown !'##molecule_type DNA !'##residues 1-461 ##label VAN !'##cross-references EMBL:X16277; NID:g35137; PIDN:CAA34353.1; !1PID:g296667 REFERENCE A33388 !$#authors Fitzgerald, M.C.; Flanagan, M.A. !$#journal DNA (1989) 8:623-634 !$#title Characterization and sequence analysis of the human !1ornithine decarboxylase gene. !$#cross-references MUID:90126232; PMID:2693021 !$#accession A33388 !'##molecule_type DNA !'##residues 1-461 ##label FIT !'##cross-references GB:M81740; NID:g189370; PIDN:AAA59967.1; !1PID:g189371; GB:M31061; NID:g338277; PID:g338278 REFERENCE JQ0792 !$#authors Hickok, N.J.; Wahlfors, J.; Crozat, A.; Halmekytoe, M.; !1Alhonen, L.; Jaenne, J.; Jaenne, O.A. !$#journal Gene (1990) 93:257-263 !$#title Human ornithine decarboxylase-encoding loci: nucleotide !1sequence of the expressed gene and characterization of a !1pseudogene. !$#cross-references MUID:91033036; PMID:2227439 !$#accession JQ0792 !'##molecule_type DNA !'##residues 1-461 ##label HIC1 !'##cross-references GB:M33764; NID:g338279; PIDN:AAA60564.1; !1PID:g338280 REFERENCE A26957 !$#authors Hickok, N.J.; Seppaenen, P.J.; Gunsalus, G.L.; Jaenne, O.A. !$#journal DNA (1987) 6:179-187 !$#title Complete amino acid sequence of human ornithine !1decarboxylase deduced from complementary DNA. !$#cross-references MUID:87246067; PMID:3595418 !$#accession A26957 !'##molecule_type mRNA !'##residues 1-461 ##label HIC2 !'##cross-references GB:M16650 REFERENCE S14539 !$#authors Flanagan, M.A.; Streng, K.A.; Wagner III, R.L. !$#submission submitted to the EMBL Data Library, November 1990 !$#description Nucleotide sequence of a human ornithine decarboxylase cDNA. !$#accession S14539 !'##molecule_type mRNA !'##residues 1-461 ##label FLA !'##cross-references EMBL:X55362; NID:g35135; PIDN:CAA39047.1; !1PID:g35136 REFERENCE A46555 !$#authors Kaczmarek, L.; Calabretta, B.; Ferrari, S.; de Riel, J.K. !$#journal J. Cell. Physiol. (1987) 132:545-551 !$#title Cell-cycle-dependent expression of human ornithine !1decarboxylase. !$#cross-references MUID:88007889; PMID:3308908 !$#accession A46555 !'##molecule_type mRNA !'##residues 112-461 ##label KAC !'##cross-references GB:M20372; NID:g189372; PIDN:AAA59968.1; !1PID:g189373 REFERENCE I38077 !$#authors Hsieh, J.T.; Denning, M.F.; Heidel, S.M.; Verma, A.K. !$#journal Cancer Res. (1990) 50:2239-2244 !$#title Expression of human chromosome 2 ornithine decarboxylase !1gene in ornithine decarboxylase-deficient Chinese hamster !1ovary cells. !$#cross-references MUID:90199754; PMID:2317811 !$#accession I38077 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-22 ##label HSI !'##cross-references EMBL:X53271; NID:g288102; PIDN:CAA37369.1; !1PID:g288103 GENETICS !$#gene GDB:ODC1 !'##cross-references GDB:119462; OMIM:165640 !$#map_position 2p25-2p25 !$#introns 34/3; 92/3; 150/2; 195/2; 222/3; 250/3; 305/1; 342/3; 414/2 FUNCTION !$#description catalyzes the decarboxylation of ornithine to putrescine !$#pathway polyamine biosynthesis !$#note the first and rate-limiting reaction in the pathway CLASSIFICATION #superfamily ornithine decarboxylase KEYWORDS carbon-carbon lyase; carboxy-lyase; phosphoprotein; !1polyamine biosynthesis; pyridoxal phosphate FEATURE !$69 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted\ !$360 #active_site Cys (shared with dimeric partner) !8#status predicted SUMMARY #length 461 #molecular-weight 51148 #checksum 1395 SEQUENCE /// ENTRY DCMSO #type complete TITLE ornithine decarboxylase (EC 4.1.1.17) [validated] - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 18-Aug-2000 ACCESSIONS A01077; A22295; S02124; A25427; B25427; I55283; S34065 REFERENCE A01077 !$#authors Kahana, C.; Nathans, D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:1673-1677 !$#title Nucleotide sequence of murine ornithine decarboxylase mRNA. !$#cross-references MUID:85166193; PMID:3856848 !$#accession A01077 !'##molecule_type mRNA !'##residues 1-461 ##label KAH !'##cross-references GB:M10624; NID:g200119; PIDN:AAA39845.1; !1PID:g200120 REFERENCE A22295 !$#authors Gupta, M.; Coffino, P. !$#journal J. Biol. Chem. (1985) 260:2941-2944 !$#title Mouse ornithine decarboxylase. Complete amino acid sequence !1deduced from cDNA. !$#cross-references MUID:85131068; PMID:2982844 !$#accession A22295 !'##molecule_type mRNA !'##residues 1-461 ##label GUP !'##cross-references GB:M19521; GB:M20617; GB:J03615; NID:g200127; !1PIDN:AAA51638.1; PID:g387500; GB:M10616 REFERENCE S02124 !$#authors Coffino, P.; Chen, E.L. !$#journal Nucleic Acids Res. (1988) 16:2731-2732 !$#title Nucleotide sequence of the mouse ornithine decarboxylase !1gene. !$#cross-references MUID:88203223; PMID:3362685 !$#accession S02124 !'##status translation not shown !'##molecule_type DNA !'##residues 1-461 ##label COF !'##cross-references EMBL:X07392; NID:g53517; PIDN:CAA30301.1; !1PID:g53518 REFERENCE A94117 !$#authors Hickok, N.J.; Seppanen, P.J.; Kontula, K.K.; Janne, P.A.; !1Bardin, C.W.; Janne, O.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:594-598 !$#title Two ornithine decarboxylase mRNA species in mouse kidney !1arise from size heterogeneity at their 3' termini. !$#cross-references MUID:86120987; PMID:3456155 !$#accession A25427 !'##molecule_type mRNA !'##residues 55-56,180-205,'E',207-461 ##label HIC1 !'##cross-references GB:M12330; NID:g200121; PIDN:AAA39846.1; !1PID:g387499 !'##note this mRNA was designated as clone poDC16 !$#accession B25427 !'##molecule_type mRNA !'##residues 320-349,'H',351-461 ##label HIC2 !'##cross-references GB:M12331; NID:g200130; PIDN:AAA39848.1; !1PID:g200131 !'##note this mRNA was designated as clone pODC74 !'##note the authors translated the codon CAT for residue 330 as Tyr REFERENCE A41744 !$#authors Poulin, R.; Lu, L.; Ackermann, B.; Bey, P.; Pegg, A.E. !$#journal J. Biol. Chem. (1992) 267:150-158 !$#title Mechanism of the irreversible inactivation of mouse !1ornithine decarboxylase by alpha-difluoromethylornithine. !1Characterization of sequences at the inhibitor and coenzyme !1binding sites. !$#cross-references MUID:92112641; PMID:1730582 !$#contents annotation; active site REFERENCE I55283 !$#authors Katz, A.; Kahana, C. !$#journal J. Biol. Chem. (1988) 263:7604-7609 !$#title Isolation and characterization of the mouse orinithine !1decarboxylase gene. !$#cross-references MUID:88227956; PMID:3372502 !$#accession I55283 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-461 ##label RES !'##cross-references GB:J03733; NID:g200132; PIDN:AAA39849.1; !1PID:g387501 REFERENCE S34065 !$#authors Tsirka, S.E.; Turck, C.W.; Coffino, P. !$#journal Biochem. J. (1993) 293:289-295 !$#title Multiple active conformers of mouse ornithine decarboxylase. !$#cross-references MUID:93319524; PMID:8328969 !$#accession S34065 !'##molecule_type protein !'##residues 357-359,'X',361-367 ##label TSI GENETICS !$#introns 34/3; 92/3; 150/2; 195/2; 222/3; 250/3; 305/1; 342/3; 414/2 COMPLEX homodimer FUNCTION !$#description catalyzes the decarboxylation of ornithine to putrescine !$#pathway polyamine biosynthesis !$#note the first and rate-limiting reaction in the pathway CLASSIFICATION #superfamily ornithine decarboxylase KEYWORDS carbon-carbon lyase; carboxy-lyase; homodimer; !1phosphoprotein; polyamine biosynthesis; pyridoxal phosphate FEATURE !$69 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status experimental\ !$360 #active_site Cys (shared with dimeric partner) !8#status experimental SUMMARY #length 461 #molecular-weight 51163 #checksum 161 SEQUENCE /// ENTRY DCRTO #type complete TITLE ornithine decarboxylase (EC 4.1.1.17) - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 18-Jun-1999 ACCESSIONS A27361; A33710; C33710; S01406; S14352 REFERENCE A27361 !$#authors van Kranen, H.J.; van de Zande, L.; van Kreijl, C.F.; !1Bisschop, A.; Wieringa, B. !$#journal Gene (1987) 60:145-155 !$#title Cloning and nucleotide sequence of rat ornithine !1decarboxylase cDNA. !$#cross-references MUID:88167817; PMID:3443298 !$#accession A27361 !'##molecule_type mRNA !'##residues 1-461 ##label VAN !'##cross-references GB:M16982; NID:g205803; PIDN:AAA41737.1; !1PID:g205804; GB:M19157 !'##experimental_source clone pODC.E10 REFERENCE A33710 !$#authors Wen, L.; Huang, J.K.; Blackshear, P.J. !$#journal J. Biol. Chem. (1989) 264:9016-9021 !$#title Rat ornithine decarboxylase gene. Nucleotide sequence, !1potential regulatory elements, and comparison to the mouse !1gene. !$#cross-references MUID:89255378; PMID:2722815 !$#accession A33710 !'##molecule_type DNA !'##residues 1-461 ##label WEN1 !'##cross-references GB:J04792 !$#accession C33710 !'##molecule_type mRNA !'##residues 1-461 ##label WEN2 !'##cross-references GB:J04791; NID:g205807; PIDN:AAA66164.1; !1PID:g205808 REFERENCE S01406 !$#authors van Steeg, H.; van Oostrom, C.T.M.; van Kranen, H.J.; van !1Kreijl, C.F. !$#journal Nucleic Acids Res. (1988) 16:8173-8174 !$#title Nucleotide sequence of the rat ornithine decarboxylase gene. !$#cross-references MUID:88335556; PMID:3419906 !$#accession S01406 !'##status translation not shown !'##molecule_type DNA !'##residues 1-461 ##label VAN2 !'##cross-references EMBL:X07944; NID:g56786; PIDN:CAA30765.1; !1PID:g56787 REFERENCE S14352 !$#authors van Steeg, H.; van Oostrom, C.T.M.; Hodemaekers, H.M.; !1Peters, L.; Thomas, A.A.M. !$#journal Biochem. J. (1991) 274:521-526 !$#title The translation in vitro of rat ornithine decarboxylase mRNA !1is blocked by its 5' untranslated region in a !1polyamine-independent way. !$#cross-references MUID:91174765; PMID:2006916 !$#accession S14352 !'##molecule_type mRNA !'##residues 1-37 ##label STE COMMENT This pyridoxal phosphate enzyme, which belongs to a !1multigene family, catalyzes the decarboxylation of ornithine !1to putrescine, the first enzymatic reaction and also the !1rate-limiting step in the pathway of polyamine biosynthesis. GENETICS !$#introns 34/3; 92/3; 150/2; 195/2; 222/3; 250/3; 305/1; 342/3; 414/2 CLASSIFICATION #superfamily ornithine decarboxylase KEYWORDS carbon-carbon lyase; carboxy-lyase; phosphoprotein; !1polyamine biosynthesis; pyridoxal phosphate FEATURE !$69 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted\ !$360 #active_site Cys (shared with dimeric partner) !8#status predicted SUMMARY #length 461 #molecular-weight 51047 #checksum 2254 SEQUENCE /// ENTRY DCHYOC #type complete TITLE ornithine decarboxylase (EC 4.1.1.17) - Chinese hamster ORGANISM #formal_name Cricetulus griseus #common_name Chinese hamster DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS S09574; A27379 REFERENCE S09574 !$#authors Grens, A.; Steglich, C.; Pilz, R.; Scheffler, I.E. !$#journal Nucleic Acids Res. (1989) 17:10497 !$#title Nucleotide sequence of the Chinese hamster ornithine !1decarboxylase gene. !$#cross-references MUID:90098890; PMID:2602162 !$#accession S09574 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-455 ##label GRE !'##cross-references EMBL:X16910; NID:g49439; PIDN:CAA34784.1; !1PID:g49440 REFERENCE A27379 !$#authors Srinivasan, P.R.; Tonin, P.N.; Wensing, E.J.; Lewis, W.H. !$#journal J. Biol. Chem. (1987) 262:12871-12878 !$#title The gene for ornithine decarboxylase is co-amplified in !1hydroxyurea-resistant hamster cells. !$#cross-references MUID:87308329; PMID:2887574 !$#accession A27379 !'##molecule_type mRNA !'##residues 163-295,'EQP',296-451,'R',453-455 ##label SRI !'##cross-references GB:J02813 CLASSIFICATION #superfamily ornithine decarboxylase KEYWORDS carbon-carbon lyase; carboxy-lyase; phosphoprotein; !1polyamine biosynthesis; pyridoxal phosphate FEATURE !$67 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted\ !$354 #active_site Cys (shared with dimeric partner) !8#status predicted SUMMARY #length 455 #molecular-weight 50453 #checksum 408 SEQUENCE /// ENTRY DCCHO #type fragment TITLE ornithine decarboxylase (EC 4.1.1.17) - chicken (fragment) ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS A48386; S19892 REFERENCE A48386 !$#authors Johnson, R.; Bulfield, G. !$#journal Anim. Genet. (1992) 23:403-409 !$#title Molecular cloning and sequence analysis of a chicken !1ornithine decarboxylase cDNA. !$#cross-references MUID:93036582; PMID:1416246 !$#accession A48386 !'##molecule_type mRNA !'##residues 1-450 ##label JO2 !'##cross-references EMBL:X64710; NID:g63712; PIDN:CAA45965.1; !1PID:g63713 !'##experimental_source embryos !'##note sequence extracted from NCBI backbone (NCBIP:115105) FUNCTION !$#description This enzyme catalyzes the decarboxylation of ornithine to !1putrescine, the first enzymatic reaction and also the !1rate-limiting step in the pathway of polyamine biosynthesis. CLASSIFICATION #superfamily ornithine decarboxylase KEYWORDS carbon-carbon lyase; carboxy-lyase; phosphoprotein; !1polyamine biosynthesis; pyridoxal phosphate FEATURE !$59 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted\ !$350 #active_site Cys (shared with dimeric partner) !8#status predicted SUMMARY #length 450 #checksum 7400 SEQUENCE /// ENTRY DCUTOB #type complete TITLE ornithine decarboxylase (EC 4.1.1.17) - Trypanosoma brucei ORGANISM #formal_name Trypanosoma brucei DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS A29309 REFERENCE A29309 !$#authors Phillips, M.A.; Coffino, P.; Wang, C.C. !$#journal J. Biol. Chem. (1987) 262:8721-8727 !$#title Cloning and sequencing of the ornithine decarboxylase gene !1from Trypanosoma brucei. Implications for enzyme turnover !1and selective difluoromethylornithine inhibition. !$#cross-references MUID:87250494; PMID:3036823 !$#accession A29309 !'##molecule_type DNA !'##residues 1-445 ##label PHI !'##cross-references GB:J02771; NID:g162173; PIDN:AAA30218.1; !1PID:g162174 CLASSIFICATION #superfamily ornithine decarboxylase KEYWORDS carbon-carbon lyase; carboxy-lyase; phosphoprotein; !1polyamine biosynthesis; pyridoxal phosphate FEATURE !$89 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted\ !$380 #active_site Cys (shared with dimeric partner) !8#status predicted SUMMARY #length 445 #molecular-weight 49176 #checksum 1897 SEQUENCE /// ENTRY DCBYO #type complete TITLE ornithine decarboxylase (EC 4.1.1.17) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YKL184w ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 21-Jul-2000 ACCESSIONS A28437; S34686; S38016 REFERENCE A28437 !$#authors Fonzi, W.A.; Sypherd, P.S. !$#journal J. Biol. Chem. (1987) 262:10127-10133 !$#title The gene and the primary structure of ornithine !1decarboxylase from Saccharomyces cerevisiae. !$#cross-references MUID:87280032; PMID:3038869 !$#accession A28437 !'##molecule_type DNA !'##residues 1-466 ##label FON !'##cross-references GB:J02777; NID:g172069; PIDN:AAA34829.1; !1PID:g172070 REFERENCE S34679 !$#authors Wieman, S.; Voss, H.; Schwagaer, C.; Rupp, T.; Stegemann, !1J.; Zimmermann, J.; Grothues, D.; Sensen, C.; Erfle, H.; !1Hewitt, N.; Banrevi, A.; Ansorge, W. !$#submission submitted to the EMBL Data Library, July 1993 !$#description Sequencing and analysis of 51.5 kilobases on the left arm of !1chromosome XI from Saccharomyces cerevisiae reveals 23 open !1reading frames including the FAS1 gene. !$#accession S34686 !'##molecule_type DNA !'##residues 1-466 ##label WIE !'##cross-references EMBL:X74151; NID:g450365; PIDN:CAA52254.1; !1PID:g395241 !'##experimental_source strain S288C REFERENCE S37825 !$#authors Wiemann, S.; Voss, H.; Schwager, C.; Rupp, T.; Grothues, D.; !1Sensen, C.; Stegemann, J.; Zimmermann, J.; Erfle, H.; !1Hewitt, N.; Ansorge, W. !$#submission submitted to the Protein Sequence Database, March 1994 !$#accession S38016 !'##molecule_type DNA !'##residues 1-466 ##label WI2 !'##cross-references EMBL:Z28184; NID:g486324; PIDN:CAA82027.1; !1PID:g486325; GSPDB:GN00011; MIPS:YKL184w !'##experimental_source strain S288C GENETICS !$#gene SGD:SPE1; ORD1; MIPS:YKL184w !'##cross-references SGD:S0001667; MIPS:YKL184w !$#map_position 11L CLASSIFICATION #superfamily ornithine decarboxylase KEYWORDS carbon-carbon lyase; carboxy-lyase; phosphoprotein; !1polyamine biosynthesis; pyridoxal phosphate FEATURE !$116 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted\ !$411 #active_site Cys (shared with dimeric partner) !8#status predicted SUMMARY #length 466 #molecular-weight 52285 #checksum 7050 SEQUENCE /// ENTRY S59553 #type complete TITLE arginine decarboxylase (EC 4.1.1.19) - garden pea ORGANISM #formal_name Pisum sativum #common_name garden pea DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S59553; S52217 REFERENCE S59553 !$#authors Perez-Amador, M.A.; Carbonell, J.; Granell, A. !$#journal Plant Mol. Biol. (1995) 28:997-1009 !$#title Expression of arginine decarboxylase is induced during early !1fruit development and in young tissues of Pisum sativum !1(L.). !$#cross-references MUID:96011747; PMID:7548836 !$#accession S59553 !'##molecule_type mRNA !'##residues 1-728 ##label PER !'##cross-references EMBL:Z37540; NID:g609219; PIDN:CAA85773.1; !1PID:g609220 CLASSIFICATION #superfamily arginine decarboxylase KEYWORDS carbon-carbon lyase; carboxy-lyase; polyamine biosynthesis SUMMARY #length 728 #molecular-weight 78710 #checksum 3427 SEQUENCE /// ENTRY JQ2341 #type complete TITLE arginine decarboxylase (EC 4.1.1.19) - tomato ORGANISM #formal_name Lycopersicon esculentum #common_name tomato DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JQ2341 REFERENCE JQ2341 !$#authors Rastogi, R.; Dulson, J.; Rothstein, S.J. !$#journal Plant Physiol. (1993) 103:829-834 !$#title Cloning of tomato (Lycopersicon esculentum Mill.) arginine !1decarboxylase gene and its expression during fruit ripening. !$#cross-references MUID:94294562; PMID:8022938 !$#accession JQ2341 !'##molecule_type DNA !'##residues 1-502 ##label RAS !'##cross-references GB:L16582; NID:g295349; PIDN:AAA61347.1; !1PID:g295350 COMMENT This enzyme is responsible for putrescine biosynthesis. CLASSIFICATION #superfamily arginine decarboxylase KEYWORDS carbon-carbon lyase; carboxy-lyase SUMMARY #length 502 #molecular-weight 54581 #checksum 8607 SEQUENCE /// ENTRY S12265 #type complete TITLE arginine decarboxylase (EC 4.1.1.19) - oat ORGANISM #formal_name Avena sativa #common_name oat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S12265 REFERENCE S12265 !$#authors Bell, E.; Malmberg, R.L. !$#journal Mol. Gen. Genet. (1990) 224:431-436 !$#title Analysis of a cDNA encoding arginine decarboxylase from oat !1reveals similarity to the Escherichia coli arginine !1decarboxylase and evidence of protein processing. !$#cross-references MUID:91094781; PMID:2266946 !$#accession S12265 !'##molecule_type mRNA !'##residues 1-607 ##label BEL !'##cross-references EMBL:X56802; NID:g16119; PIDN:CAA40137.1; !1PID:g16120 GENETICS !$#gene spe1 CLASSIFICATION #superfamily arginine decarboxylase KEYWORDS carbon-carbon lyase; carboxy-lyase SUMMARY #length 607 #molecular-weight 66705 #checksum 6389 SEQUENCE /// ENTRY A65079 #type complete TITLE arginine decarboxylase (EC 4.1.1.19) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS A65079; A37771; D42604 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65079 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-658 ##label BLAT !'##cross-references GB:AE000377; GB:U00096; NID:g2367178; !1PIDN:AAC75975.1; PID:g1789307; UWGP:b2938 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A37771 !$#authors Moore, R.C.; Boyle, S.M. !$#journal J. Bacteriol. (1990) 172:4631-4640 !$#title Nucleotide sequence and analysis of the speA gene encoding !1biosynthetic arginine decarboxylase in Escherichia coli. !$#cross-references MUID:90330576; PMID:2198270 !$#accession A37771 !'##status preliminary !'##molecule_type DNA !'##residues 1-225,'R',227-658 ##label MOO !'##cross-references GB:M31770; NID:g147854; PIDN:AAA24646.1; !1PID:g147856 REFERENCE A42604 !$#authors Szumanski, M.B.; Boyle, S.M. !$#journal J. Bacteriol. (1992) 174:758-764 !$#title Influence of cyclic AMP, agmatine, and a novel protein !1encoded by a flanking gene on speB (agmatine ureohydrolase) !1in Escherichia coli. !$#cross-references MUID:92121113; PMID:1310091 !$#accession D42604 !'##status preliminary !'##molecule_type DNA !'##residues 634-658 ##label SZU !'##note sequence extracted from NCBI backbone (NCBIN:77509, !1NCBIP:77513) GENETICS !$#gene speA !$#map_position 64 min CLASSIFICATION #superfamily arginine decarboxylase KEYWORDS carbon-carbon lyase; carboxy-lyase SUMMARY #length 658 #molecular-weight 73898 #checksum 1633 SEQUENCE /// ENTRY DCECD #type complete TITLE diaminopimelate decarboxylase (EC 4.1.1.20) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 20-Sep-1984 #sequence_revision 20-Sep-1984 #text_change 01-Mar-2002 ACCESSIONS A01078; G65066 REFERENCE A92900 !$#authors Stragier, P.; Danos, O.; Patte, J.C. !$#journal J. Mol. Biol. (1983) 168:321-331 !$#title Regulation of diaminopimelate decarboxylase synthesis in !1Escherichia coli. II. Nucleotide sequence of the lysA gene !1and its regulatory region. !$#cross-references MUID:83294516; PMID:6350601 !$#accession A01078 !'##molecule_type DNA !'##residues 1-420 ##label STR !'##cross-references GB:J01614; NID:g146067; PIDN:AAA83861.1; !1PID:g455170 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65066 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-420 ##label BLAT !'##cross-references GB:AE000367; GB:U00096; NID:g1789195; !1PIDN:AAC75877.1; PID:g1789203; UWGP:b2838 !'##experimental_source strain K-12, substrain MG1655 COMMENT This enzyme has an absolute requirement for pyridoxal !1phosphate as a cofactor. GENETICS !$#gene lysA !$#map_position 61 min CLASSIFICATION #superfamily diaminopimelate decarboxylase KEYWORDS carbon-carbon lyase; carboxy-lyase SUMMARY #length 420 #molecular-weight 46177 #checksum 7300 SEQUENCE /// ENTRY B64556 #type complete TITLE diaminopimelate decarboxylase (EC 4.1.1.20) - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B64556 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession B64556 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-405 ##label TOM !'##cross-references GB:AE000547; GB:AE000511; NID:g2313377; !1PIDN:AAD07356.1; PID:g2313384; TIGR:HP0290 CLASSIFICATION #superfamily diaminopimelate decarboxylase KEYWORDS carbon-carbon lyase; carboxy-lyase; pyridoxal phosphate SUMMARY #length 405 #molecular-weight 45240 #checksum 3960 SEQUENCE /// ENTRY A31133 #type complete TITLE diaminopimelate decarboxylase (EC 4.1.1.20) - Pseudomonas aeruginosa ORGANISM #formal_name Pseudomonas aeruginosa DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A31133 REFERENCE A31133 !$#authors Martin, C.; Cami, B.; Yeh, P.; Stragier, P.; Parsot, C.; !1Patte, J.C. !$#journal Mol. Biol. Evol. (1988) 5:549-559 !$#title Pseudomonas aeruginosa diaminopimelate decarboxylase: !1evolutionary relationship with other amino acid !1decarboxylases. !$#cross-references MUID:89056708; PMID:3143046 !$#accession A31133 !'##molecule_type DNA !'##residues 1-415 ##label MAR !'##note the authors translated the codon GGG for residue 15 as Gln, GGC !1for residue 103 as Gln, GGG for residue 149 as Ala, CAG for !1residue 392 as Glu and GAA for residue 404 as Gln CLASSIFICATION #superfamily diaminopimelate decarboxylase KEYWORDS carbon-carbon lyase; carboxy-lyase; pyridoxal phosphate SUMMARY #length 415 #molecular-weight 45490 #checksum 6379 SEQUENCE /// ENTRY B64089 #type complete TITLE diaminopimelate decarboxylase (EC 4.1.1.20) - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B64089 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession B64089 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-415 ##label TIGR !'##cross-references GB:U32756; GB:L42023; NID:g1573729; !1PIDN:AAC22385.1; PID:g1573731; TIGR:HI0727 CLASSIFICATION #superfamily diaminopimelate decarboxylase KEYWORDS carbon-carbon lyase; carboxy-lyase; pyridoxal phosphate SUMMARY #length 415 #molecular-weight 46107 #checksum 5052 SEQUENCE /// ENTRY C70404 #type complete TITLE diaminopimelate decarboxylase (EC 4.1.1.20) - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C70404 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession C70404 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-420 ##label AQF !'##cross-references GB:AE000728; NID:g2983641; PIDN:AAC07209.1; !1PID:g2983642; GB:AE000657 !'##experimental_source strain VF5 GENETICS !$#gene lysA CLASSIFICATION #superfamily diaminopimelate decarboxylase KEYWORDS carbon-carbon lyase; carboxy-lyase; pyridoxal phosphate SUMMARY #length 420 #molecular-weight 46966 #checksum 4011 SEQUENCE /// ENTRY JU0471 #type complete TITLE diaminopimelate decarboxylase (EC 4.1.1.20) lysA - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S45535; JU0471; S09603; H69653 REFERENCE S45533 !$#authors Sorokin, A.; Zumstein, E.; Azevedo, V.; Ehrlich, S.D.; !1Serror, P. !$#submission submitted to the EMBL Data Library, November 1993 !$#accession S45535 !'##molecule_type DNA !'##residues 1-439 ##label SOR !'##cross-references EMBL:L09228; NID:g410114; PIDN:AAA67473.1; !1PID:g410117 REFERENCE JU0471 !$#authors Yamamoto, J.; Shimizu, M.; Yamane, K. !$#journal Agric. Biol. Chem. (1991) 55:1615-1626 !$#title Molecular cloning and analysis of nucleotide sequence of the !1Bacillus subtilis lysA gene region using B. subtilis phage !1vectors and a multi-copy plasmid, pUB110. !$#cross-references MUID:91345841; PMID:1368705 !$#accession JU0471 !'##molecule_type DNA !'##residues 'MTL',2-89, !1'ESYIRLLQQAFRQNASTFMETIRAGKNCGWRLSTASAALWWIISMKSS',138-158, !1'R',160-384,'LYR',389-439 ##label YAM !'##cross-references GB:D90189; GB:S50865; NID:g216389; PIDN:BAA14211.1; !1PID:g216391 !'##note the authors translated the codon CGA for residue 159 as Gly and !1GGA for residue 364 as Lys !'##note the major region of difference represents a frameshift relative !1to the sequence shown; the sequence report with accession !1number S45535 gives more consistent homology to related !1sequences from other species REFERENCE S09603 !$#authors Yamamoto, J.; Shimizu, M.; Yamane, K. !$#journal Nucleic Acids Res. (1989) 17:10105 !$#title Nucleotide sequence of the diaminopimelate-decarboxylase !1gene from Bacillus subtilis. !$#cross-references MUID:90098781; PMID:2513554 !$#accession S09603 !'##molecule_type DNA !'##residues 'MTL',2-89, !1'ESYIRLLQQAFRQNASTFMETIRAGKNCGWRLSTASAALWWIISMKSS',138-312, !1'DKLYNRFIIRRAN' ##label YA2 !'##cross-references EMBL:X17013; NID:g39893; PIDN:CAA34876.1; !1PID:g39894 !'##note this sequence appears to have been corrected, in part, in !1reference JU0471 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69653 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-439 ##label KUN !'##cross-references GB:Z99116; GB:AL009126; NID:g2634723; !1PIDN:CAB14270.1; PID:g2634773 !'##experimental_source strain 168 COMMENT This enzyme is involved in the biosynthesis of lysine from !1arginine. GENETICS !$#gene lysA !$#start_codon TTG CLASSIFICATION #superfamily diaminopimelate decarboxylase KEYWORDS carbon-carbon lyase; carboxy-lyase; pyridoxal phosphate SUMMARY #length 439 #molecular-weight 48574 #checksum 3831 SEQUENCE /// ENTRY I39877 #type complete TITLE diaminopimelate decarboxylase (EC 4.1.1.20) - Bacillus methanolicus ORGANISM #formal_name Bacillus methanolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS I39877 REFERENCE I39877 !$#authors Mills, D.A.; Flickinger, M.C. !$#journal Appl. Environ. Microbiol. (1993) 59:2927-2937 !$#title Cloning and sequence analysis of the meso-diaminopimelate !1decarboxylase gene from Bacillus methanolicus MGA3 and !1comparison to other decarboxylase genes. !$#cross-references MUID:94028923; PMID:8215365 !$#accession I39877 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-432 ##label MIL !'##cross-references GB:L18879; NID:g304154; PIDN:AAC36985.1; !1PID:g304155 GENETICS !$#gene lysA CLASSIFICATION #superfamily diaminopimelate decarboxylase KEYWORDS carbon-carbon lyase; carboxy-lyase; pyridoxal phosphate SUMMARY #length 432 #molecular-weight 47820 #checksum 999 SEQUENCE /// ENTRY S03827 #type complete TITLE diaminopimelate decarboxylase (EC 4.1.1.20) - Corynebacterium glutamicum ORGANISM #formal_name Corynebacterium glutamicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S03827; B49936; S12228; S42851 REFERENCE S03827 !$#authors Yeh, P.; Sicard, A.M.; Sinskey, A.J. !$#journal Mol. Gen. Genet. (1988) 212:112-119 !$#title Nucleotide sequence of the lysA gene of Corynebacterium !1glutamicum and possible mechanisms for modulation of its !1expression. !$#cross-references MUID:88232419; PMID:2836698 !$#accession S03827 !'##molecule_type DNA !'##residues 1-445 ##label YEH !'##cross-references EMBL:X07563; NID:g40513; PIDN:CAA30445.1; !1PID:g40514 REFERENCE A49936 !$#authors Oguiza, J.A.; Malumbres, M.; Eriani, G.; Pisabarro, A.; !1Mateos, L.M.; Martin, F.; Martin, J.F. !$#journal J. Bacteriol. (1993) 175:7356-7362 !$#title A gene encoding arginyl-tRNA synthetase is located in the !1upstream region of the lysA gene in Brevibacterium !1lactofermentum: regulation of argS-lysA cluster expression !1by arginine. !$#cross-references MUID:94042911; PMID:8226683 !$#accession B49936 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-49 ##label OGU !'##cross-references EMBL:Z21501; NID:g433533; PIDN:CAA79711.1; !1PID:g433535 REFERENCE S12227 !$#authors Marcel, T.; Archer, J.A.C.; Mengin-Lecreulx, D.; Sinskey, !1A.J. !$#journal Mol. Microbiol. (1990) 4:1819-1830 !$#title Nucleotide sequence and organization of the upstream region !1of the Corynebacterium glutamicum lysA gene. !$#cross-references MUID:91186817; PMID:2082143 !$#accession S12228 !'##status preliminary !'##molecule_type DNA !'##residues 1-49 ##label MAR !'##cross-references GB:X54740; NID:g40524; PIDN:CAA38538.1; PID:g40526 GENETICS !$#gene lysA CLASSIFICATION #superfamily diaminopimelate decarboxylase KEYWORDS carbon-carbon lyase; carboxy-lyase; pyridoxal phosphate SUMMARY #length 445 #molecular-weight 47411 #checksum 9613 SEQUENCE /// ENTRY A70773 #type complete TITLE diaminopimelate decarboxylase (EC 4.1.1.20) lysA - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A70773; JN0507 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession A70773 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-447 ##label COL !'##cross-references GB:Z73419; GB:AL123456; NID:g3261573; !1PIDN:CAA97758.1; PID:g1322417 !'##experimental_source strain H37Rv REFERENCE JN0507 !$#authors Andersen, A.B.; Hansen, E.B. !$#journal Gene (1993) 124:105-109 !$#title Cloning of the lysA gene from Mycobacterium tuberculosis. !$#cross-references MUID:93178957; PMID:8440471 !$#accession JN0507 !'##molecule_type DNA !'##residues 1-345,'G',347-388,'TIFGPAIWLRLPPPALLLFAVESLQHGRPSRCGSGAR', !1427-447 ##label AND !'##cross-references GB:M94109; NID:g149963; PIDN:AAA25361.1; !1PID:g149964 COMMENT This enzyme catalyzes the conversion of diaminopimelic acid !1to lysine. GENETICS !$#gene lysA !$#start_codon GTG CLASSIFICATION #superfamily diaminopimelate decarboxylase KEYWORDS carbon-carbon lyase; carboxy-lyase; pyridoxal phosphate SUMMARY #length 447 #molecular-weight 47457 #checksum 6228 SEQUENCE /// ENTRY S75984 #type complete TITLE diaminopimelate decarboxylase (EC 4.1.1.20) - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein sll0504 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S75984 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75984 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-469 ##label KAN !'##cross-references EMBL:D64006; GB:AB001339; NID:g1001291; !1PIDN:BAA10831.1; PID:g1001344 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene lysA CLASSIFICATION #superfamily diaminopimelate decarboxylase KEYWORDS carbon-carbon lyase; carboxy-lyase; pyridoxal phosphate SUMMARY #length 469 #molecular-weight 50847 #checksum 4254 SEQUENCE /// ENTRY E69044 #type complete TITLE diaminopimelate decarboxylase (EC 4.1.1.20) - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS E69044 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession E69044 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-428 ##label MTH !'##cross-references GB:AE000897; GB:AE000666; NID:g2622439; !1PIDN:AAB85813.1; PID:g2622442 !'##experimental_source strain Delta H GENETICS !$#gene MTH1335 CLASSIFICATION #superfamily diaminopimelate decarboxylase KEYWORDS carbon-carbon lyase; carboxy-lyase; pyridoxal phosphate SUMMARY #length 428 #molecular-weight 47689 #checksum 9947 SEQUENCE /// ENTRY H69349 #type complete TITLE diaminopimelate decarboxylase (EC 4.1.1.20) - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS H69349 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession H69349 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-419 ##label KLE !'##cross-references GB:AE001049; GB:AE000782; NID:g2689372; !1PIDN:AAB90438.1; PID:g2649806; TIGR:AF0800 CLASSIFICATION #superfamily diaminopimelate decarboxylase KEYWORDS carbon-carbon lyase; carboxy-lyase; pyridoxal phosphate SUMMARY #length 419 #molecular-weight 45871 #checksum 5695 SEQUENCE /// ENTRY H64436 #type complete TITLE diaminopimelate decarboxylase (EC 4.1.1.20) - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H64436 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession H64436 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-438 ##label BUL !'##cross-references GB:U67552; GB:L77117; NID:g1591737; !1PIDN:AAB99100.1; PID:g1591741; TIGR:MJ1097 GENETICS !$#map_position REV1038517-1037201 !$#start_codon GTG CLASSIFICATION #superfamily diaminopimelate decarboxylase KEYWORDS carbon-carbon lyase; carboxy-lyase; pyridoxal phosphate SUMMARY #length 438 #molecular-weight 48899 #checksum 4284 SEQUENCE /// ENTRY DEECPE #type complete TITLE phosphoribosylaminoimidazole carboxylase (EC 4.1.1.21) catalytic chain - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 01-Mar-2002 ACCESSIONS JT0499; A32237; B64784 REFERENCE JT0499 !$#authors Watanabe, W.; Sampei, G.; Aiba, A.; Mizobuchi, K. !$#journal J. Bacteriol. (1989) 171:198-204 !$#title Identification and sequence analysis of Escherichia coli !1purE and purK genes encoding !15'-phosphoribosyl-5-amino-4-imidazole carboxylase for de !1novo purine biosynthesis. !$#cross-references MUID:89123018; PMID:2644189 !$#accession JT0499 !'##molecule_type DNA !'##residues 1-169 ##label WAT !'##cross-references GB:M19657; NID:g147411; PIDN:AAA24449.1; !1PID:g147412 REFERENCE A32237 !$#authors Tiedeman, A.A.; Keyhani, J.; Kamholz, J.; Daum III, H.A.; !1Gots, J.S.; Smith, J.M. !$#journal J. Bacteriol. (1989) 171:205-212 !$#title Nucleotide sequence analysis of the purEK operon encoding !15'-phosphoribosyl-5-aminoimidazole carboxylase of !1Escherichia coli K-12. !$#cross-references MUID:89123019; PMID:2464576 !$#accession A32237 !'##molecule_type DNA !'##residues 1-169 ##label TIE !'##cross-references GB:X12982; NID:g42587; PIDN:CAA31420.1; PID:g42588 !'##experimental_source strain K12 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64784 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-169 ##label BLAT !'##cross-references GB:AE000158; GB:U00096; NID:g1786728; !1PIDN:AAC73625.1; PID:g1786734; UWGP:b0523 !'##experimental_source strain K-12, substrain MG1655 COMMENT This is the catalytic component of the enzyme that catalyzes !1the conversion of 5-phosphoribosyl-5-amino-4-imidazole to !1carboxyl-5'-phosphoribosyl-5-amino-4-imidazole in de novo !1purine biosynthesis. GENETICS !$#gene purE !$#map_position 12 min CLASSIFICATION #superfamily phosphoribosylaminoimidazole carboxylase !1catalytic chain; phosphoribosylaminoimidazole carboxylase !1catalytic chain homology KEYWORDS carbon-carbon lyase; carboxy-lyase; purine nucleotide !1biosynthesis FEATURE !$8-143 #domain phosphoribosylaminoimidazole carboxylase !8catalytic chain homology #label PCC SUMMARY #length 169 #molecular-weight 17780 #checksum 6844 SEQUENCE /// ENTRY DEBSPE #type complete TITLE phosphoribosylaminoimidazole carboxylase (EC 4.1.1.21) catalytic chain - Bacillus subtilis ALTERNATE_NAMES phosphoribosylaminoimidazole carboxylase chain I ORGANISM #formal_name Bacillus subtilis DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jun-2000 ACCESSIONS A29326; D69684 REFERENCE A29326 !$#authors Ebbole, D.J.; Zalkin, H. !$#journal J. Biol. Chem. (1987) 262:8274-8287 !$#title Cloning and characterization of a 12-gene cluster from !1Bacillus subtilis encoding nine enzymes for de novo purine !1nucleotide synthesis. !$#cross-references MUID:87250425; PMID:3036807 !$#accession A29326 !'##molecule_type DNA !'##residues 1-162 ##label EBB !'##cross-references EMBL:J02732; NID:g143363; PIDN:AAA22674.1; !1PID:g143364 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D69684 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-162 ##label KUN !'##cross-references GB:Z99107; GB:AL009126; NID:g2632866; !1PIDN:CAB12462.1; PID:g2632956 !'##experimental_source strain 168 GENETICS !$#gene purE !$#map_position 18 min CLASSIFICATION #superfamily phosphoribosylaminoimidazole carboxylase !1catalytic chain; phosphoribosylaminoimidazole carboxylase !1catalytic chain homology KEYWORDS carbon-carbon lyase; carboxy-lyase; purine nucleotide !1biosynthesis FEATURE !$3-138 #domain phosphoribosylaminoimidazole carboxylase !8catalytic chain homology #label PCC SUMMARY #length 162 #molecular-weight 17174 #checksum 2396 SEQUENCE /// ENTRY DCECPK #type complete TITLE phosphoribosylaminoimidazole carboxylase (EC 4.1.1.21) carbon dioxide-fixation chain - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 01-Mar-2002 ACCESSIONS JU0001; B32237; A64784 REFERENCE JT0499 !$#authors Watanabe, W.; Sampei, G.; Aiba, A.; Mizobuchi, K. !$#journal J. Bacteriol. (1989) 171:198-204 !$#title Identification and sequence analysis of Escherichia coli !1purE and purK genes encoding !15'-phosphoribosyl-5-amino-4-imidazole carboxylase for de !1novo purine biosynthesis. !$#cross-references MUID:89123018; PMID:2644189 !$#accession JU0001 !'##molecule_type DNA !'##residues 1-355 ##label WAT !'##cross-references GB:M19657; NID:g147411; PIDN:AAA24450.1; !1PID:g147413 !'##experimental_source strain NK6051 REFERENCE A32237 !$#authors Tiedeman, A.A.; Keyhani, J.; Kamholz, J.; Daum III, H.A.; !1Gots, J.S.; Smith, J.M. !$#journal J. Bacteriol. (1989) 171:205-212 !$#title Nucleotide sequence analysis of the purEK operon encoding !15'-phosphoribosyl-5-aminoimidazole carboxylase of !1Escherichia coli K-12. !$#cross-references MUID:89123019; PMID:2464576 !$#accession B32237 !'##molecule_type DNA !'##residues 1-63,'PD',66-355 ##label TIE !'##cross-references GB:X12982; NID:g42587; PIDN:CAA31421.1; PID:g42589 !'##experimental_source strain K12 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64784 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-355 ##label BLAT !'##cross-references GB:AE000158; GB:U00096; NID:g1786728; !1PIDN:AAC73624.1; PID:g1786733; UWGP:b0522 !'##experimental_source strain K-12, substrain MG1655 COMMENT This is the noncatalytic component of the enzyme that !1catalyzes the conversion of !15-phosphoribosyl-5-amino-4-imidazole to !1carboxyl-5'-phosphoribosyl-5-amino-4-imidazole in de novo !1biosynthesis. GENETICS !$#gene purK !$#map_position 12 min CLASSIFICATION #superfamily phosphoribosylaminoimidazole carboxylase carbon !1dioxide-fixation chain; phosphoribosylaminoimidazole !1carboxylase carbon dioxide-fixation chain homology KEYWORDS carbon dioxide fixation; carbon-carbon lyase; carboxy-lyase; !1purine nucleotide biosynthesis FEATURE !$1-320 #domain phosphoribosylaminoimidazole carboxylase !8carbon dioxide-fixation chain homology #label PCD SUMMARY #length 355 #molecular-weight 39461 #checksum 918 SEQUENCE /// ENTRY H64132 #type complete TITLE phosphoribosylaminoimidazole carboxylase (EC 4.1.1.21) carbon dioxide-fixation chain - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS H64132 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession H64132 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-362 ##label TIGR !'##cross-references GB:U32835; GB:L42023; NID:g1574459; !1PIDN:AAC23264.1; PID:g1574462; TIGR:HI1616 CLASSIFICATION #superfamily phosphoribosylaminoimidazole carboxylase carbon !1dioxide-fixation chain; phosphoribosylaminoimidazole !1carboxylase carbon dioxide-fixation chain homology KEYWORDS carbon dioxide fixation; carbon-carbon lyase; carboxy-lyase; !1purine nucleotide biosynthesis FEATURE !$7-327 #domain phosphoribosylaminoimidazole carboxylase !8carbon dioxide-fixation chain homology #label PCD SUMMARY #length 362 #molecular-weight 41273 #checksum 9648 SEQUENCE /// ENTRY DCBSPK #type complete TITLE phosphoribosylaminoimidazole carboxylase (EC 4.1.1.21) carbon dioxide-fixation chain - Bacillus subtilis ALTERNATE_NAMES phosphoribosylaminoimidazole carboxylase chain II ORGANISM #formal_name Bacillus subtilis DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jun-2000 ACCESSIONS B29326; G69684 REFERENCE A29326 !$#authors Ebbole, D.J.; Zalkin, H. !$#journal J. Biol. Chem. (1987) 262:8274-8287 !$#title Cloning and characterization of a 12-gene cluster from !1Bacillus subtilis encoding nine enzymes for de novo purine !1nucleotide synthesis. !$#cross-references MUID:87250425; PMID:3036807 !$#accession B29326 !'##molecule_type DNA !'##residues 1-379 ##label EBB !'##cross-references EMBL:J02732; NID:g143363; PIDN:AAA22675.1; !1PID:g143365 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69684 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-379 ##label KUN !'##cross-references GB:Z99107; GB:AL009126; NID:g2632866; !1PIDN:CAB12463.1; PID:g2632957 !'##experimental_source strain 168 GENETICS !$#gene purK !$#map_position 18 min CLASSIFICATION #superfamily phosphoribosylaminoimidazole carboxylase carbon !1dioxide-fixation chain; phosphoribosylaminoimidazole !1carboxylase carbon dioxide-fixation chain homology KEYWORDS carbon dioxide fixation; carbon-carbon lyase; carboxy-lyase; !1purine nucleotide biosynthesis FEATURE !$23-354 #domain phosphoribosylaminoimidazole carboxylase !8carbon dioxide-fixation chain homology #label PCD SUMMARY #length 379 #molecular-weight 42163 #checksum 1877 SEQUENCE /// ENTRY E69685 #type complete TITLE phosphoribosylglycinamide formyltransferase 2 (EC 2.1.2.-) purT [validated] - Bacillus subtilis ALTERNATE_NAMES 5'-phosphoribosyl-1-glycinamide transformylase T ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS E69685; S47267 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69685 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-384 ##label KUN !'##cross-references GB:Z99105; GB:AL009126; NID:g2632457; !1PIDN:CAB12017.1; PID:g2632509 !'##experimental_source strain 168 REFERENCE S47267 !$#authors Saxild, H.H.; Jacobsen, J.H.; Nygaard, P. !$#submission submitted to the EMBL Data Library, April 1994 !$#description On the occurence of formate-dependent 5'- !1phosphoribosyl-1-glycinamide transformylase T activity in !1microorganisms: isolation and characterization of the purT !1gene from Bacillus subtilis. !$#accession S47267 !'##molecule_type DNA !'##residues 1-239,'ND',242-384 ##label SAX !'##cross-references EMBL:X78962; NID:g534938; PIDN:CAA55557.1; !1PID:g534939 !'##experimental_source strain 168 GENETICS !$#gene purT FUNCTION !$#description catalyzes the production of beta-formyl glycinamide !1ribonucleotide from formate, ATP and glycinamide !1ribonucleotide !$#pathway purine nucleotide biosynthesis !$#note cofactor magnesium CLASSIFICATION #superfamily phosphoribosylaminoimidazole carboxylase carbon !1dioxide-fixation chain; phosphoribosylaminoimidazole !1carboxylase carbon dioxide-fixation chain homology KEYWORDS magnesium; purine nucleotide biosynthesis; transferase FEATURE !$18-362 #domain phosphoribosylaminoimidazole carboxylase !8carbon dioxide-fixation chain homology #label PCD SUMMARY #length 384 #molecular-weight 42093 #checksum 9136 SEQUENCE /// ENTRY A54227 #type complete TITLE phosphoribosylglycinamide formyltransferase 2 (EC 2.1.2.-) purT [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES GAR transformylase; glycinamide ribonucleotide transformylase ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS A54227; A64947 REFERENCE A54227 !$#authors Marolewski, A.; Smith, J.M.; Benkovic, S.J. !$#journal Biochemistry (1994) 33:2531-2537 !$#title Cloning and characterization of a new purine biosynthetic !1enzyme: a non-folate glycinamide ribonucleotide !1transformylase from Escherichia coli. !$#cross-references MUID:94162268; PMID:8117714 !$#accession A54227 !'##status preliminary !'##molecule_type DNA !'##residues 1-392 ##label MAR !'##cross-references GB:L20897; NID:g304883; PIDN:AAA23861.1; !1PID:g304887 !'##experimental_source strain K-12 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64947 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-392 ##label BLAT !'##cross-references GB:AE000279; GB:U00096; NID:g1788154; !1PIDN:AAC74919.1; PID:g1788155; UWGP:b1849 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene purT FUNCTION !$#description catalyzes the production of beta-formyl glycinamide !1ribonucleotide from formate, ATP and glycinamide !1ribonucleotide !$#pathway purine nucleotide biosynthesis !$#note cofactor magnesium CLASSIFICATION #superfamily phosphoribosylaminoimidazole carboxylase carbon !1dioxide-fixation chain; phosphoribosylaminoimidazole !1carboxylase carbon dioxide-fixation chain homology KEYWORDS magnesium; monomer; purine nucleotide biosynthesis; !1transferase FEATURE !$26-369 #domain phosphoribosylaminoimidazole carboxylase !8carbon dioxide-fixation chain homology #label PCD SUMMARY #length 392 #molecular-weight 42433 #checksum 9078 SEQUENCE /// ENTRY A56691 #type complete TITLE phosphoribosylglycinamide formyltransferase 2 (EC 2.1.2.-) [similarity] - Pasteurella haemolytica ALTERNATE_NAMES membrane antigen 1 ORGANISM #formal_name Pasteurella haemolytica DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 31-Mar-2000 ACCESSIONS A56691 REFERENCE A56691 !$#authors Chang, Y.F.; Ma, D.P.; Young, R.; Struck, D.K. !$#journal DNA Seq. (1993) 3:357-367 !$#title Cloning, sequencing and expression of a Pasteurella !1haemolytica A1 gene encoding a PurK-like protein. !$#cross-references MUID:94033621; PMID:8219279 !$#accession A56691 !'##status preliminary !'##molecule_type DNA !'##residues 1-392 ##label CHA !'##cross-references GB:S68137; NID:g469474; PIDN:AAB28915.1; !1PID:g469475 GENETICS !$#gene mpa1 FUNCTION !$#description catalyzes the production of beta-formyl glycinamide !1ribonucleotide from formate, ATP and glycinamide !1ribonucleotide !$#pathway purine nucleotide biosynthesis !$#note cofactor magnesium CLASSIFICATION #superfamily phosphoribosylaminoimidazole carboxylase carbon !1dioxide-fixation chain; phosphoribosylaminoimidazole !1carboxylase carbon dioxide-fixation chain homology KEYWORDS inner membrane; magnesium; purine nucleotide biosynthesis; !1surface antigen; transferase FEATURE !$26-369 #domain phosphoribosylaminoimidazole carboxylase !8carbon dioxide-fixation chain homology #label PCD SUMMARY #length 392 #molecular-weight 43131 #checksum 1040 SEQUENCE /// ENTRY E64485 #type complete TITLE phosphoribosylglycinamide formyltransferase 2 (EC 2.1.2.-) MJ1486 [similarity] - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E64485 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession E64485 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-393 ##label BUL !'##cross-references GB:U67589; GB:L77117; NID:g2826417; !1PIDN:AAB99496.1; PID:g1592123; TIGR:MJ1486 GENETICS !$#map_position REV1458908-1457727 !$#start_codon TTG FUNCTION !$#description catalyzes the production of beta-formyl glycinamide !1ribonucleotide from formate, ATP and glycinamide !1ribonucleotide !$#pathway purine nucleotide biosynthesis !$#note cofactor magnesium CLASSIFICATION #superfamily phosphoribosylaminoimidazole carboxylase carbon !1dioxide-fixation chain; phosphoribosylaminoimidazole !1carboxylase carbon dioxide-fixation chain homology KEYWORDS magnesium; purine nucleotide biosynthesis; transferase FEATURE !$29-371 #domain phosphoribosylaminoimidazole carboxylase !8carbon dioxide-fixation chain homology #label PCD SUMMARY #length 393 #molecular-weight 43553 #checksum 6279 SEQUENCE /// ENTRY DEZPP #type complete TITLE phosphoribosylaminoimidazole carboxylase (EC 4.1.1.21) - fission yeast (Schizosaccharomyces pombe) ORGANISM #formal_name Schizosaccharomyces pombe DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 10-Dec-1999 ACCESSIONS S02159; T40944 REFERENCE S02159 !$#authors Szankasi, P.; Heyer, W.D.; Schuchert, P.; Kohli, J. !$#journal J. Mol. Biol. (1988) 204:917-925 !$#title DNA sequence analysis of the ade6 gene of !1Schizosaccharomyces pombe. Wild-type and mutant alleles !1including the recombination hot spot allele ade6-M26. !$#cross-references MUID:89125617; PMID:3221399 !$#accession S02159 !'##molecule_type DNA !'##residues 1-552 ##label SZA !'##cross-references EMBL:X14488; NID:g4901; PIDN:CAA32650.1; PID:g4902; !1GB:M37264; NID:g173341; PID:g173342 REFERENCE Z21959 !$#authors Lucas, M.; Gaillardin, C.; Lyne, M.; Rajandream, M.A.; !1Barrell, B.G. !$#submission submitted to the EMBL Data Library, January 1999 !$#accession T40944 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-552 ##label LUC !'##cross-references EMBL:AL035259; PIDN:CAA22866.1; GSPDB:GN00068; !1SPDB:SPCC1322.13 !'##experimental_source strain 972h-; cosmid c1322 GENETICS !$#gene ade6 !$#map_position 3 CLASSIFICATION #superfamily phosphoribosylaminoimidazole carboxylase; !1phosphoribosylaminoimidazole carboxylase carbon !1dioxide-fixation chain homology; !1phosphoribosylaminoimidazole carboxylase catalytic chain !1homology KEYWORDS carbon dioxide fixation; carbon-carbon lyase; carboxy-lyase; !1purine nucleotide biosynthesis FEATURE !$18-361 #domain phosphoribosylaminoimidazole carboxylase !8carbon dioxide-fixation chain homology #label PCD\ !$386-519 #domain phosphoribosylaminoimidazole carboxylase !8catalytic chain homology #label PCC SUMMARY #length 552 #molecular-weight 60013 #checksum 1133 SEQUENCE /// ENTRY DEBYP #type complete TITLE phosphoribosylaminoimidazole carboxylase (EC 4.1.1.21) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein O3293; protein YOR128c; protein YOR3293c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 21-Jul-2000 ACCESSIONS JN0098; S44056; S61004; S61684; S67013; S63881; S25373 REFERENCE JN0098 !$#authors Stotz, A.; Linder, P. !$#journal Gene (1990) 95:91-98 !$#title The ADE2 gene from Saccharomyces cerevisiae: sequence and !1new vectors. !$#cross-references MUID:91071612; PMID:2253890 !$#accession JN0098 !'##molecule_type DNA !'##residues 1-571 ##label STO !'##cross-references GB:M32013; GB:M59824; NID:g171002; PIDN:AAA34401.1; !1PID:g171003 REFERENCE S44056 !$#authors Sasnauskas, K.; Janulaitis, A. !$#submission submitted to the EMBL Data Library, February 1991 !$#accession S44056 !'##molecule_type DNA !'##residues 1-100,'G',102-185,'G',187-205,'F',207-240,'KMQSNFSRLWYI', !1254-386,'L',388-406,'V',408-430,'T',432-433,'L',435-501,'T', !1503-571 ##label SAS !'##cross-references EMBL:M58324; NID:g171016; PIDN:AAA34407.1; !1PID:g171017 REFERENCE S60983 !$#authors Wiemann, S.; Rechmann, S.; Benes, V.; Voss, H.; Schwager, !1C.; Vlcek, C.; Stegemann, J.; Zimmermann, J.; Erfle, H.; !1Paces, V.; Ansorge, W. !$#submission submitted to the EMBL Data Library, August 1995 !$#description Sequencing of 51 kilobases on the right arm of chromosome XV !1from S. cerevisiae reveals 30 open reading frames. !$#accession S61004 !'##molecule_type DNA !'##residues 1-571 ##label WIE !'##cross-references EMBL:X90518; NID:g1050808; PIDN:CAA62125.1; !1PID:g1050830 REFERENCE S61643 !$#authors Benes, V.; Andrade, M.A.; Rechmann, S.; Teodoru, C.; !1Banrevi, A.; Sander, C.; Valencia, A.; Ansorge, W.; Voss, H. !$#submission submitted to the EMBL Data Library, December 1995 !$#description Nucleotide sequence and analysis of a 130 kb fragment of !1yeast chromosome XV. !$#accession S61684 !'##molecule_type DNA !'##residues 1-571 ##label BEN !'##cross-references EMBL:X94335; NID:g1262139; PIDN:CAA64047.1; !1PID:g1164972 REFERENCE S66965 !$#authors Voss, H.; Benes, V.; Rechmann, S.; Teodoru, C.; Schwager, !1C.; Paces, V.; Ansorge, W. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67013 !'##molecule_type DNA !'##residues 1-571 ##label VOS !'##cross-references EMBL:Z75036; NID:g1420331; PIDN:CAA99327.1; !1PID:g1420332; GSPDB:GN00015; MIPS:YOR128c !'##experimental_source strain S288C REFERENCE S63860 !$#authors Wiemann, S.; Rechmann, S.; Benes, V.; Voss, H.; Schwager, !1C.; Vlcek, C.; Stegemann, J.; Zimmermann, J.; Erfle, H.; !1Paces, V.; Ansorge, W. !$#journal Yeast (1996) 12:281-288 !$#title Sequencing and analysis of 51 kb on the right arm of !1chromosome XV from Saccharomyces cerevisiae reveals 30 open !1reading frames. !$#cross-references MUID:97060020; PMID:8904341 !$#accession S63881 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-571 ##label WIW !'##cross-references EMBL:X90518; NID:g1050808; PIDN:CAA62125.1; !1PID:g1050830 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1995 GENETICS !$#gene SGD:ADE2; MIPS:YOR128c !'##cross-references SGD:S0005654; MIPS:YOR128c !$#map_position 15R CLASSIFICATION #superfamily phosphoribosylaminoimidazole carboxylase; !1phosphoribosylaminoimidazole carboxylase carbon !1dioxide-fixation chain homology; !1phosphoribosylaminoimidazole carboxylase catalytic chain !1homology KEYWORDS carbon dioxide fixation; carbon-carbon lyase; carboxy-lyase; !1purine nucleotide biosynthesis FEATURE !$17-364 #domain phosphoribosylaminoimidazole carboxylase !8carbon dioxide-fixation chain homology #label PCD\ !$403-536 #domain phosphoribosylaminoimidazole carboxylase !8catalytic chain homology #label PCC SUMMARY #length 571 #molecular-weight 62339 #checksum 8337 SEQUENCE /// ENTRY S39112 #type complete TITLE phosphoribosylaminoimidazole carboxylase (EC 4.1.1.21) - yeast (Pichia methanolica) ORGANISM #formal_name Pichia methanolica DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S39112 REFERENCE S39112 !$#authors Hiep, T.T.; Kulikov, V.N.; Noskov, V.N.; Sizonenko, G.I.; !1Chernoff, Y.O.; Pavlov, Y.I. !$#journal Yeast (1993) 9:1251-1258 !$#title The 5-aminoimidazole ribonucleotide-carboxylase structural !1gene of the methylotrophic yeast Pichia methanolica: !1cloning, sequencing and homology analysis. !$#cross-references MUID:94152172; PMID:8109174 !$#accession S39112 !'##molecule_type DNA !'##residues 1-543 ##label PIC !'##cross-references EMBL:X76529; NID:g457701; PIDN:CAA54041.1; !1PID:g457702 GENETICS !$#gene ADE1 CLASSIFICATION #superfamily phosphoribosylaminoimidazole carboxylase; !1phosphoribosylaminoimidazole carboxylase carbon !1dioxide-fixation chain homology; !1phosphoribosylaminoimidazole carboxylase catalytic chain !1homology KEYWORDS carbon dioxide fixation; carbon-carbon lyase; carboxy-lyase; !1purine nucleotide biosynthesis FEATURE !$17-362 #domain phosphoribosylaminoimidazole carboxylase !8carbon dioxide-fixation chain homology #label PCD\ !$402-535 #domain phosphoribosylaminoimidazole carboxylase !8catalytic chain homology #label PCC SUMMARY #length 543 #molecular-weight 58544 #checksum 7682 SEQUENCE /// ENTRY S43322 #type complete TITLE phosphoribosylaminoimidazole carboxylase (EC 4.1.1.21) - moth bean ALTERNATE_NAMES 5-aminoimidazole ribonucleotide carboxylase ORGANISM #formal_name Vigna aconitifolia #common_name moth bean DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S43322 REFERENCE S43322 !$#authors Chapman, K.A.; Delauney, A.J.; Kim, J.H.; Verma, D.P.S. !$#journal Plant Mol. Biol. (1994) 24:389-395 !$#title Structural organization of de novo purine biosynthesis !1enzymes in plants: 5-aminoimidazole ribonucleotide !1carboxylase and 5-aminoimidazole-4-N-succinocarboxamide !1ribonucleotide synthetase cDNAs from Vigna aconitifolia. !$#cross-references MUID:94154258; PMID:8111040 !$#accession S43322 !'##status preliminary !'##molecule_type mRNA !'##residues 1-557 ##label CHA !'##cross-references EMBL:L22584; NID:g349158; PIDN:AAC37400.1; !1PID:g349159 !'##note the sequence of residues 547-557 and the corresponding !1nucleotide sequence are not shown in this paper CLASSIFICATION #superfamily phosphoribosylaminoimidazole carboxylase; !1phosphoribosylaminoimidazole carboxylase carbon !1dioxide-fixation chain homology; !1phosphoribosylaminoimidazole carboxylase catalytic chain !1homology KEYWORDS carbon dioxide fixation; carbon-carbon lyase; carboxy-lyase; !1purine nucleotide biosynthesis FEATURE !$18-359 #domain phosphoribosylaminoimidazole carboxylase !8carbon dioxide-fixation chain homology #label PCD\ !$389-522 #domain phosphoribosylaminoimidazole carboxylase !8catalytic chain homology #label PCC SUMMARY #length 557 #molecular-weight 60942 #checksum 4242 SEQUENCE /// ENTRY DCLBHP #type complete TITLE histidine decarboxylase (EC 4.1.1.22) precursor [validated] - Lactobacillus sp. CONTAINS histidine decarboxylase large (alpha) chain; histidine decarboxylase precursor (pi) chain; histidine decarboxylase small (beta) chain ORGANISM #formal_name Lactobacillus sp. DATE 13-Jun-1983 #sequence_revision 22-Nov-1996 #text_change 03-Nov-2000 ACCESSIONS A25932; A92349; A92470; A01079 REFERENCE A25932 !$#authors Vanderslice, P.; Copeland, W.C.; Robertus, J.D. !$#journal J. Biol. Chem. (1986) 261:15186-15191 !$#title Cloning and nucleotide sequence of wild type and a mutant !1histidine decarboxylase from Lactobacillus 30a. !$#cross-references MUID:87033764; PMID:3021766 !$#accession A25932 !'##molecule_type DNA !'##residues 1-311 ##label VAN !'##cross-references GB:J02613; NID:g149550; PIDN:AAB59151.1; !1PID:g149551 !'##experimental_source strain 30a, ATCC 33222 !'##note translation of initiation codon is not shown REFERENCE A92349 !$#authors Vaaler, G.L.; Recsei, P.A.; Fox, J.L.; Snell, E.E. !$#journal J. Biol. Chem. (1982) 257:12770-12774 !$#title Histidine decarboxylase of Lactobacillus 30a. Comparative !1sequences of the beta chain from wild type and mutant !1enzymes. !$#cross-references MUID:83030804; PMID:6752140 !$#accession A92349 !'##molecule_type protein !'##residues 2-82 ##label VAA !'##experimental_source strain 30a, ATCC 33222 !'##note the initial methionine was observed in 15% of the chains REFERENCE A92470 !$#authors Huynh, Q.K.; Recsei, P.A.; Vaaler, G.L.; Snell, E.E. !$#journal J. Biol. Chem. (1984) 259:2833-2839 !$#title Histidine decarboxylase of Lactobacillus 30a. Sequences of !1the overlapping peptides, the complete alpha chain, and !1prohistidine decarboxylase. !$#cross-references MUID:84135771; PMID:6698997 !$#accession A92470 !'##molecule_type protein !'##residues 83-206,'D',208-265,'I',267-270,'L',272-284;288-311 ##label !1HUY !'##experimental_source strain 30a REFERENCE A51934 !$#authors Gallagher, T.; Rozwarski, D.A.; Ernst, S.R.; Hackert, M.L. !$#submission submitted to the Brookhaven Protein Data Bank, December 1992 !$#cross-references PDB:1PYA !$#contents annotation; X-ray crystallography, 2.5 angstroms, residues !12-82;83-311 REFERENCE A58363 !$#authors Gallagher, T.; Rozwarski, D.A.; Ernst, S.R.; Hackert, M.L. !$#journal J. Mol. Biol. (1993) 230:516-528 !$#title Refined structure of the pyruvoyl-dependent histidine !1decarboxylase from Lactobacillus 30a. !$#cross-references MUID:93217991; PMID:8464063 !$#contents annotation; X-ray crystallography, 2.5 angstroms, residues !12-82;83-311 REFERENCE A58364 !$#authors Gallagher, T.; Snell, E.E.; Hackert, M.L. !$#journal J. Biol. Chem. (1989) 264:12737-12743 !$#title Pyruvoyl-dependent histidine decarboxylase. Active site !1structure and mechanistic analysis. !$#cross-references MUID:89308713; PMID:2745463 !$#contents annotation; active site COMMENT The precursor is activated by cleavage between Ser-82 and !1Ser-83 and conversion of Ser-83 to the pyruvoyl prosthetic !1group. GENETICS !$#gene hdcA !$#start_codon ATT COMPLEX the proenzyme is a homohexamer of precursor (pi) chains; the !1active enzyme is a dodecamer of six small (beta) and six !1large (alpha) chains FUNCTION !$#description catalyzes the decarboxylation of histidine to histamine CLASSIFICATION #superfamily Lactobacillus histidine decarboxylase KEYWORDS blocked amino end; carbon-carbon lyase; carboxy-lyase FEATURE !$2-311 #product histidine decarboxylase precursor (pi) chain !8#status predicted #label PIC\ !$2-82 #product histidine decarboxylase small (beta) chain !8#status experimental #label BET\ !$83-311 #product histidine decarboxylase large (alpha) chain !8#status experimental #label ALF\ !$64,82 #binding_site substrate (Asp, Ser) #status !8experimental\ !$82-83 #cleavage_site Ser-Ser (autolytic) #status predicted\ !$83 #modified_site pyruvic acid (Ser) (in mature form) !8#status experimental\ !$198 #active_site Glu #status predicted SUMMARY #length 311 #molecular-weight 34233 #checksum 4222 SEQUENCE /// ENTRY DCLBHB #type fragment TITLE histidine decarboxylase (EC 4.1.1.22) precursor - Lactobacillus buchneri (fragment) ALTERNATE_NAMES histidine decarboxylase pi chain ORGANISM #formal_name Lactobacillus buchneri DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 03-Nov-2000 ACCESSIONS A01080 REFERENCE A92512 !$#authors Huynh, Q.K.; Snell, E.E. !$#journal J. Biol. Chem. (1985) 260:2798-2803 !$#title Pyruvoyl-dependent histidine decarboxylases. Preparation and !1amino acid sequences of the beta chains of histidine !1decarboxylase from Clostridium perfringens and Lactobacillus !1buchneri. !$#cross-references MUID:85131044; PMID:2857718 !$#accession A01080 !'##molecule_type protein !'##residues 1-114 ##label HUY COMMENT This enzyme catalyzes the decarboxylation of histidine to !1histamine. In Lactobacillus, the active enzyme is a hexamer; !1each monomer contains one small (or beta) and one large (or !1alpha) chain. COMMENT The proenzyme is a hexamer of identical chains (pi chains). !1Each pi chain cleaves between Ser-81 and Ser-82 !1nonhydrolytically to form the beta chain and amino end of !1the alpha chain. Ser-82 is converted to a pyruvoyl !1prosthetic group, covalently bound to the phenylalanine !1residue at the amino end of the alpha chain. CLASSIFICATION #superfamily Lactobacillus histidine decarboxylase KEYWORDS blocked amino end; carbon-carbon lyase; carboxy-lyase FEATURE !$1-114 #product histidine decarboxylase precursor (pi) chain !8(fragment) #status experimental #label MAT\ !$1-81 #domain histidine decarboxylase small (beta) chain !8#label BET\ !$82-114 #domain histidine decarboxylase large (alpha) chain !8(fragment) #label ALF\ !$81-82 #cleavage_site Ser-Ser (autolytic) #status predicted\ !$82 #modified_site pyruvic acid (Ser) (in mature form) !8#status experimental SUMMARY #length 114 #checksum 3792 SEQUENCE /// ENTRY DCCLHP #type complete TITLE histidine decarboxylase (EC 4.1.1.22) precursor - Clostridium perfringens CONTAINS histidine decarboxylase large (alpha) chain; histidine decarboxylase precursor (pi) chain; histidine decarboxylase small (beta) chain ORGANISM #formal_name Clostridium perfringens DATE 04-Dec-1986 #sequence_revision 22-Nov-1996 #text_change 03-Nov-2000 ACCESSIONS A33770; A01081 REFERENCE A90544 !$#authors van Poelje, P.D.; Snell, E.E. !$#journal Biochemistry (1990) 29:132-139 !$#title Cloning, sequencing, expression, and site-directed !1mutagenesis of the gene from Clostridium perfringens !1encoding pyruvoyl-dependent histidine decarboxylase. !$#cross-references MUID:90212559; PMID:2108713 !$#accession A33770 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-320 ##label POE !'##cross-references GB:J02880; NID:g144833; PIDN:AAA83526.1; !1PID:g144834 !'##experimental_source ATCC 13124 !'##note parts of this sequence were determined by protein sequencing; !1the amino-terminal Asn of the precursor is blocked and the !1initial Met is absent REFERENCE A92512 !$#authors Huynh, Q.K.; Snell, E.E. !$#journal J. Biol. Chem. (1985) 260:2798-2803 !$#title Pyruvoyl-dependent histidine decarboxylases. Preparation and !1amino acid sequences of the beta chains of histidine !1decarboxylase from Clostridium perfringens and Lactobacillus !1buchneri. !$#cross-references MUID:85131044; PMID:2857718 !$#accession A01081 !'##molecule_type protein !'##residues 12-50,'D',52-97;98-108,'V',110-113,'S',115-122,'F',124-128, !1'M',130 ##label HUY COMMENT The precursor is activated by cleavage between Ser-97 and !1Ser-98 and conversion of Ser-98 to the pyruvoyl prosthetic !1group. COMPLEX the proenzyme is a homohexamer of precursor (pi) chains; the !1active enzyme is a dodecamer of six small (beta) and six !1large (alpha) chains FUNCTION !$#description catalyzes the decarboxylation of histidine to histamine CLASSIFICATION #superfamily Lactobacillus histidine decarboxylase KEYWORDS blocked amino end; carbon-carbon lyase; carboxy-lyase FEATURE !$1-11 #domain signal sequence #status predicted #label SIG\ !$2-320 #product histidine decarboxylase precursor (pi) chain !8#status predicted #label PIC\ !$12-97 #domain histidine decarboxylase small (beta) chain !8#status experimental #label BET\ !$98-320 #domain histidine decarboxylase large (alpha) chain !8#status predicted #label ALF\ !$2 #modified_site blocked amino end (Asn) (in precursor !8form) #link PIC #status experimental\ !$97-98 #cleavage_site Ser-Ser (autolytic) #status predicted\ !$98 #modified_site pyruvic acid (Ser) (in mature form) !8#status experimental\ !$215 #active_site Glu #status predicted SUMMARY #length 320 #molecular-weight 35524 #checksum 3335 SEQUENCE /// ENTRY A40004 #type complete TITLE histidine decarboxylase (EC 4.1.1.22) - Enterobacter aerogenes ORGANISM #formal_name Enterobacter aerogenes DATE 20-Mar-1992 #sequence_revision 20-Mar-1992 #text_change 18-Jun-1999 ACCESSIONS A40004 REFERENCE A40004 !$#authors Kamath, A.V.; Vaaler, G.L.; Snell, E.E. !$#journal J. Biol. Chem. (1991) 266:9432-9437 !$#title Pyridoxal phosphate-dependent histidine decarboxylases. !1Cloning, sequencing, and expression of genes from Klebsiella !1planticola and Enterobacter aerogenes and properties of the !1overexpressed enzymes. !$#cross-references MUID:91236707; PMID:2033044 !$#accession A40004 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-378 ##label KAM !'##cross-references GB:M62745; NID:g435593; PIDN:AAA24802.1; !1PID:g435594 CLASSIFICATION #superfamily Klebsiella histidine decarboxylase KEYWORDS carbon-carbon lyase; carboxy-lyase; phosphoprotein; !1pyridoxal phosphate FEATURE !$233 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 378 #molecular-weight 42434 #checksum 9477 SEQUENCE /// ENTRY B40004 #type complete TITLE histidine decarboxylase (EC 4.1.1.22) - Klebsiella planticola ORGANISM #formal_name Klebsiella planticola DATE 20-Mar-1992 #sequence_revision 20-Mar-1992 #text_change 05-Dec-1998 ACCESSIONS B40004 REFERENCE A40004 !$#authors Kamath, A.V.; Vaaler, G.L.; Snell, E.E. !$#journal J. Biol. Chem. (1991) 266:9432-9437 !$#title Pyridoxal phosphate-dependent histidine decarboxylases. !1Cloning, sequencing, and expression of genes from Klebsiella !1planticola and Enterobacter aerogenes and properties of the !1overexpressed enzymes. !$#cross-references MUID:91236707; PMID:2033044 !$#accession B40004 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-378 ##label KAM CLASSIFICATION #superfamily Klebsiella histidine decarboxylase KEYWORDS carbon-carbon lyase; carboxy-lyase; phosphoprotein; !1pyridoxal phosphate FEATURE !$233 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 378 #molecular-weight 42897 #checksum 9144 SEQUENCE /// ENTRY A25013 #type complete TITLE histidine decarboxylase (EC 4.1.1.22) - Morganella morganii ORGANISM #formal_name Morganella morganii DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 18-Jun-1999 ACCESSIONS A25013; B26751; A26751 REFERENCE A25013 !$#authors Vaaler, G.L.; Brasch, M.A.; Snell, E.E. !$#journal J. Biol. Chem. (1986) 261:11010-11014 !$#title Pyridoxal 5'-phosphate-dependent histidine decarboxylase. !1Nucleotide sequence of the hdc gene and the corresponding !1amino acid sequence. !$#cross-references MUID:86278193; PMID:3015950 !$#accession A25013 !'##molecule_type DNA !'##residues 1-378 ##label VAA !'##cross-references GB:J02577; NID:g149858; PIDN:AAA25321.1; !1PID:g149859 !'##note translation of initiator Met is not shown; parts of this !1sequence, including the amino end of the mature protein, !1were determined by protein sequencing REFERENCE A92554 !$#authors Hayashi, H.; Tanase, S.; Snell, E.E. !$#journal J. Biol. Chem. (1986) 261:11003-11009 !$#title Pyridoxal 5'-phosphate-dependent histidine decarboxylase. !1Inactivation by alpha-fluoromethylhistidine and comparative !1sequences at the inhibitor- and coenzyme-binding sites. !$#cross-references MUID:86278192; PMID:3733745 !$#accession B26751 !'##molecule_type protein !'##residues 233-247 ##label HAY !'##note pyridoxal phosphate site !$#accession A26751 !'##molecule_type protein !'##residues 322-334 ##label HA2 !'##note suicide inhibitor site CLASSIFICATION #superfamily Klebsiella histidine decarboxylase KEYWORDS carbon-carbon lyase; carboxy-lyase; phosphoprotein; !1pyridoxal phosphate FEATURE !$2-378 #product histidine decarboxylase #status predicted !8#label MAT\ !$233 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status experimental\ !$323 #active_site Ser #status predicted SUMMARY #length 378 #molecular-weight 42875 #checksum 6874 SEQUENCE /// ENTRY S49218 #type complete TITLE histidine decarboxylase (EC 4.1.1.22) - Vibrio anguillarum ORGANISM #formal_name Vibrio anguillarum DATE 16-Feb-1995 #sequence_revision 12-May-1995 #text_change 18-Jun-1999 ACCESSIONS S60898; S49218 REFERENCE S60898 !$#authors Tolmasky, M.E.; Actis, L.A.; Crosa, J.H. !$#journal Mol. Microbiol. (1995) 15:87-95 !$#title A histidine decarboxylase gene encoded by the Vibrio !1anguillarum plasmid pJM1 is essential for virulence: !1histamine is a precursor in the biosynthesis of anguibactin. !$#cross-references MUID:95272396; PMID:7752899 !$#accession S60898 !'##status preliminary !'##molecule_type DNA !'##residues 1-386 ##label TO2 !'##cross-references EMBL:Z33880; NID:g535938; PIDN:CAA83945.1; !1PID:g535939 CLASSIFICATION #superfamily Klebsiella histidine decarboxylase KEYWORDS carbon-carbon lyase; carboxy-lyase; phosphoprotein; !1pyridoxal phosphate FEATURE !$233 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 386 #molecular-weight 44260 #checksum 4338 SEQUENCE /// ENTRY S39554 #type complete TITLE histidine decarboxylase (EC 4.1.1.22) - tomato ORGANISM #formal_name Lycopersicon esculentum #common_name tomato DATE 18-Feb-1994 #sequence_revision 10-Nov-1995 #text_change 18-Jun-1999 ACCESSIONS S39554 REFERENCE S39554 !$#authors Picton, S.; Gray, J.E.; Payton, S.; Barton, S.L.; Lowe, A.; !1Grierson, D. !$#journal Plant Mol. Biol. (1993) 23:627-631 !$#title A histidine decarboxylase-like mRNA is involved in tomato !1fruit ripening. !$#cross-references MUID:94033342; PMID:8219096 !$#accession S39554 !'##molecule_type mRNA !'##residues 1-413 ##label PIC !'##cross-references EMBL:X71900; NID:g416533; PIDN:CAA50719.1; !1PID:g416534 !'##note the authors did not translate the codon for residue 33 CLASSIFICATION #superfamily Klebsiella histidine decarboxylase KEYWORDS carbon-carbon lyase; carboxy-lyase; phosphoprotein; !1pyridoxal phosphate FEATURE !$242 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 413 #molecular-weight 47628 #checksum 7578 SEQUENCE /// ENTRY A49882 #type complete TITLE histidine decarboxylase (EC 4.1.1.22) - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1995 #sequence_revision 30-Jun-1995 #text_change 16-Jun-2000 ACCESSIONS A49882; S11492; S29263; A56625 REFERENCE A49882 !$#authors Yatsunami, K.; Ohtsu, H.; Tsuchikawa, M.; Higuchi, T.; !1Ishibashi, K.; Shida, A.; Shima, Y.; Nakagawa, S.; Yamauchi, !1K.; Yamamoto, M.; Hayashi, N.; Watanabe, T.; Ichikawa, A. !$#journal J. Biol. Chem. (1994) 269:1554-1559 !$#title Structure of the L-histidine decarboxylase gene. !$#cross-references MUID:94117478; PMID:8288622 !$#accession A49882 !'##molecule_type DNA !'##residues 1-662 ##label YAT !'##cross-references GB:D16583; NID:g516770; PIDN:BAA04015.1; !1PID:g516771 !'##note only intron-exon junctions shown REFERENCE S11492 !$#authors Yamauchi, K.; Sato, R.; Tanno, Y.; Ohkawara, Y.; Maeyama, !1K.; Watanabe, T.; Satoh, K.; Yoshizawa, M.; Shibahara, S.; !1Takishima, T. !$#journal Nucleic Acids Res. (1990) 18:5891 !$#title Nucleotide sequence of the cDNA encoding L-histidine !1decarboxylase derived from human basophilic leukemia cell !1line, KU-812-F. !$#cross-references MUID:91016941; PMID:2216786 !$#accession S11492 !'##molecule_type mRNA !'##residues 1-147,'Q',149-662 ##label YAM !'##cross-references EMBL:X54297; NID:g32108; PIDN:CAA38196.1; !1PID:g32109 REFERENCE S29263 !$#authors Mamune-Sato, R.; Yamauchi, K.; Tanno, Y.; Ohkawara, Y.; !1Ohtsu, H.; Katayose, D.; Maeyama, K.; Watanabe, T.; !1Shibahara, S.; Takishima, T. !$#journal Eur. J. Biochem. (1992) 209:533-539 !$#title Functional analysis of alternatively spliced transcripts of !1the human histidine decarboxylase gene and its expression in !1human tissues and basophilic leukemia cells. !$#cross-references MUID:93049295; PMID:1425659 !$#accession S29263 !'##molecule_type mRNA !'##residues 1-117,'M',119-147,'Q',149-499,'M',501-662 ##label MAM REFERENCE A56625 !$#authors Zahnow, C.A.; Yi, H.F.; McBride, O.W.; Joseph, D.R. !$#journal DNA Seq. (1991) 1:395-400 !$#title Cloning of the cDNA encoding human histidine decarboxylase !1from an erythroleukemia cell line and mapping of the gene !1locus to chromosome 15. !$#cross-references MUID:92119328; PMID:1768863 !$#accession A56625 !'##status preliminary !'##molecule_type mRNA !'##residues 1-662 ##label ZAH !'##cross-references GB:M60445; NID:g183924; PIDN:AAC41698.1; !1PID:g183925 !'##experimental_source erythroleukemia cell line !'##note sequence extracted from NCBI backbone (NCBIN:77739, !1NCBIP:77742) GENETICS !$#gene GDB:HDC !'##cross-references GDB:128639; OMIM:142704 !$#map_position 15pter-15qter !$#introns 11/1; 68/3; 106/3; 147/3; 192/3; 240/3; 263/1; 317/2; 347/3; !1380/3; 414/3 CLASSIFICATION #superfamily human histidine decarboxylase; animal histidine !1decarboxylase homology KEYWORDS alternative splicing; carbon-carbon lyase; carboxy-lyase; !1phosphoprotein; pyridoxal phosphate FEATURE !$3-471 #domain animal histidine decarboxylase homology !8#label HDC\ !$125 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 662 #molecular-weight 74140 #checksum 1533 SEQUENCE /// ENTRY A34890 #type complete TITLE histidine decarboxylase (EC 4.1.1.22) - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 30-Apr-1999 ACCESSIONS A34890; A36072 REFERENCE A34890 !$#authors Joseph, D.R.; Sullivan, P.M.; Wang, Y.M.; Kozak, C.; !1Fenstermacher, D.A.; Behrendsen, M.E.; Zahnow, C.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:733-737 !$#title Characterization and expression of the complementary DNA !1encoding rat histidine decarboxylase. !$#cross-references MUID:90138901; PMID:2300558 !$#accession A34890 !'##molecule_type mRNA !'##residues 1-101,'STAWGSRGLPA',114-656 ##label JOS !'##experimental_source fetal liver !'##note a correction to this paper was published and has accession !1number A36072 REFERENCE A36072 !$#authors Joseph, D.R.; Sullivan, P.M.; Wang, Y.M.; Kozak, C.; !1Fenstermacher, D.A.; Behrendsen, M.E.; Zahnow, C.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:7346 !$#cross-references MUID:90385003; PMID:2402512 !$#accession A36072 !'##molecule_type mRNA !'##residues 102-113 ##label JO2 !'##cross-references GB:M29591 !'##note this sequence was published as a correction COMMENT This molecule may be a precursor of a smaller mature !1protein. CLASSIFICATION #superfamily human histidine decarboxylase; animal histidine !1decarboxylase homology KEYWORDS alternative splicing; carbon-carbon lyase; carboxy-lyase; !1phosphoprotein; pyridoxal phosphate FEATURE !$6-474 #domain animal histidine decarboxylase homology !8#label HDC\ !$128 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 656 #molecular-weight 73635 #checksum 525 SEQUENCE /// ENTRY S12989 #type complete TITLE histidine decarboxylase (EC 4.1.1.22) - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 21-Nov-1993 #sequence_revision 10-Nov-1995 #text_change 18-Jun-1999 ACCESSIONS S12989; S39788; I52287 REFERENCE S12989 !$#authors Yamamoto, J.; Yatsunami, K.; Ohmori, E.; Sugimoto, Y.; !1Fukui, T.; Katayama, T.; Ichikawa, A. !$#journal FEBS Lett. (1990) 276:214-218 !$#title cDNA-derived amino acid sequence of L-histidine !1decarboxylase from mouse mastocytoma P-815 cells. !$#cross-references MUID:91092422; PMID:2125007 !$#accession S12989 !'##molecule_type mRNA !'##residues 1-662 ##label YAM !'##cross-references GB:X57437; NID:g52903; PIDN:CAA40685.1; PID:g52904 REFERENCE S39788 !$#authors Yamamoto, J.; Fukui, T.; Suzuki, K.; Tanaka, S.; Yatsunami, !1K.; Ichikawa, A. !$#journal Biochim. Biophys. Acta (1993) 1216:431-440 !$#title Expression and characterization of recombinant mouse !1mastocytoma histidine decarboxylase. !$#cross-references MUID:94092736; PMID:8268224 !$#accession S39788 !'##molecule_type protein !'##residues 173-186;207-214;380-406;437-450;496-512 ##label ECM REFERENCE I52287 !$#authors Ohgoh, M.; Yamamoto, J.; Kawata, M.; Yamamura, I.; Fukui, !1T.; Ichikawa, A. !$#journal Biochem. Biophys. Res. Commun. (1993) 196:1113-1119 !$#title Enhanced expression of the mouse L-histidine decarboxylase !1gene with a combination of dexamethasone and !112-O-tetradecanoylphorbol-13-acetate. !$#cross-references MUID:94071861; PMID:8250869 !$#accession I52287 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-17 ##label RES !'##cross-references GB:S67000; NID:g453095; PIDN:AAB29093.1; !1PID:g453096 CLASSIFICATION #superfamily human histidine decarboxylase; animal histidine !1decarboxylase homology KEYWORDS carbon-carbon lyase; carboxy-lyase; phosphoprotein; !1pyridoxal phosphate FEATURE !$10-478 #domain animal histidine decarboxylase homology !8#label HDC\ !$132 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 662 #molecular-weight 74017 #checksum 4542 SEQUENCE /// ENTRY S36337 #type complete TITLE histidine decarboxylase (EC 4.1.1.22) - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 18-Jun-1999 ACCESSIONS S36337 REFERENCE S36337 !$#authors Burg, M.G.; Sarthy, P.V.; Koliantz, G.; Pak, W.L. !$#journal EMBO J. (1993) 12:911-919 !$#title Genetic and molecular identification of a Drosophila !1histidine decarboxylase gene required in photoreceptor !1transmitter synthesis. !$#cross-references MUID:93209238; PMID:8096176 !$#accession S36337 !'##molecule_type mRNA !'##residues 1-847 ##label BUR !'##cross-references EMBL:X70644; NID:g287837; PIDN:CAA49989.1; !1PID:g287838 GENETICS !$#gene FlyBase:Hdc !'##cross-references FlyBase:FBgn0005619 CLASSIFICATION #superfamily Drosophila histidine decarboxylase; animal !1histidine decarboxylase homology KEYWORDS carbon-carbon lyase; carboxy-lyase; phosphoprotein; !1pyridoxal phosphate FEATURE !$2-470 #domain animal histidine decarboxylase homology !8#label HDC\ !$124 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 847 #molecular-weight 94106 #checksum 7108 SEQUENCE /// ENTRY DCMSOP #type complete TITLE orotidine-5'-phosphate decarboxylase (EC 4.1.1.23) - mouse ALTERNATE_NAMES OMP decarboxylase; orotidine-5'-phosphate carboxy-lyase ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 27-Jun-1994 ACCESSIONS A25323 REFERENCE A25323 !$#authors Ohmstede, C.A.; Langdon, S.D.; Chae, C.B.; Jones, M.E. !$#journal J. Biol. Chem. (1986) 261:4276-4282 !$#title Expression and sequence analysis of a cDNA encoding the !1orotidine-5'-monophosphate decarboxylase domain from Ehrlich !1ascites uridylate synthase. !$#cross-references MUID:86140253; PMID:2419341 !$#accession A25323 !'##molecule_type mRNA !'##residues 1-274 ##label OHM !'##cross-references GB:M26019 CLASSIFICATION #superfamily orotidine-5'-phosphate decarboxylase; !1orotidine-5'-phosphate decarboxylase homology KEYWORDS carbon-carbon lyase; carboxy-lyase; pyrimidine nucleotide !1biosynthesis FEATURE !$18-272 #domain orotidine-5'-phosphate decarboxylase homology !8#label OPD SUMMARY #length 274 #molecular-weight 29722 #checksum 8708 SEQUENCE /// ENTRY DEBYOP #type complete TITLE orotidine-5'-phosphate decarboxylase (EC 4.1.1.23) - yeast (Saccharomyces cerevisiae) (strain +D4) ALTERNATE_NAMES OMP decarboxylase; orotidine-5'-phosphate carboxy-lyase ORGANISM #formal_name Saccharomyces cerevisiae #variety strain +D4 DATE 13-Aug-1986 #sequence_revision 13-Aug-1986 #text_change 19-Apr-2002 ACCESSIONS A01082; A25665 REFERENCE A01082 !$#authors Rose, M.; Grisafi, P.; Botstein, D. !$#journal Gene (1984) 29:113-124 !$#title Structure and function of the yeast URA3 gene: expression in !1Escherichia coli. !$#cross-references MUID:85028421; PMID:6092217 !$#accession A01082 !'##molecule_type DNA !'##residues 1-267 ##label ROS !'##cross-references EMBL:K02206; NID:g172059; PIDN:AAA34824.1; !1PID:g172060 !'##experimental_source strain +D4 REFERENCE A25665 !$#authors Yarger, J.G.; Armilei, G.; Gorman, M.C. !$#journal Mol. Cell. Biol. (1986) 6:1095-1101 !$#title Transcription terminator-like element within a Saccharomyces !1cerevisiae promoter region. !$#cross-references MUID:87064375; PMID:3023868 !$#accession A25665 !'##molecule_type DNA !'##residues 1-70 ##label YAR !'##cross-references GB:M12926 COMMENT This enzyme catalyzes the conversion of !1orotidine-5'-phosphate to uridine monophosphate, an !1essential step in the biosynthesis of pyrimidines. GENETICS !$#gene URA3 !'##cross-references SGD:S0000747 !$#map_position 5L CLASSIFICATION #superfamily orotidine-5'-phosphate decarboxylase; !1orotidine-5'-phosphate decarboxylase homology KEYWORDS carbon-carbon lyase; carboxy-lyase; pyrimidine nucleotide !1biosynthesis FEATURE !$4-264 #domain orotidine-5'-phosphate decarboxylase homology !8#label OPD SUMMARY #length 267 #molecular-weight 29255 #checksum 1882 SEQUENCE /// ENTRY DCBYOF #type complete TITLE orotidine-5'-phosphate decarboxylase (EC 4.1.1.23) - yeast (Saccharomyces cerevisiae) (strain FL100 and S288c) ALTERNATE_NAMES OMP decarboxylase; orotidine-5'-phosphate carboxy-lyase; protein YEL021w ORGANISM #formal_name Saccharomyces cerevisiae #variety strain FL100; strain S288c DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 05-Nov-1999 ACCESSIONS S05735; S50438 REFERENCE A01082 !$#authors Rose, M.; Grisafi, P.; Botstein, D. !$#journal Gene (1984) 29:113-124 !$#title Structure and function of the yeast URA3 gene: expression in !1Escherichia coli. !$#cross-references MUID:85028421; PMID:6092217 !$#accession S05735 !'##molecule_type DNA !'##residues 1-267 ##label ROS !'##cross-references EMBL:K02207; NID:g172061; PIDN:AAA34825.1; !1PID:g172062 !'##experimental_source strain FL100 REFERENCE S50428 !$#authors Dietrich, F.S. !$#submission submitted to the EMBL Data Library, December 1994 !$#description Saccharomyces cerevisiae chromosome V cosmids 9871, 8199, !19867, 9495 and lambda clones 6693 and 5898. !$#accession S50438 !'##molecule_type DNA !'##residues 1-267 ##label DIE !'##cross-references EMBL:U18530; NID:g602367; PIDN:AAB64498.1; !1PID:g602388; GSPDB:GN00005; MIPS:YEL021w !'##experimental_source strain S288c (AB972) GENETICS !$#gene SGD:URA3; MIPS:YEL021w !'##cross-references SGD:S0000747; MIPS:YEL021w !$#map_position 5L CLASSIFICATION #superfamily orotidine-5'-phosphate decarboxylase; !1orotidine-5'-phosphate decarboxylase homology KEYWORDS carbon-carbon lyase; carboxy-lyase; pyrimidine nucleotide !1biosynthesis FEATURE !$4-264 #domain orotidine-5'-phosphate decarboxylase homology !8#label OPD SUMMARY #length 267 #molecular-weight 29239 #checksum 1054 SEQUENCE /// ENTRY S33964 #type complete TITLE orotidine-5'-phosphate decarboxylase (EC 4.1.1.23) - yeast (Kluyveromyces marxianus) ALTERNATE_NAMES OMP decarboxylase; orotidine-5'-phosphate carboxy-lyase ORGANISM #formal_name Kluyveromyces marxianus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S33964 REFERENCE S33964 !$#authors Bergkamp, R.J.M.; Geerse, R.H.; Verbakel, J.M.A.; Planta, !1R.J. !$#journal Yeast (1993) 9:677-681 !$#title Cloning and sequencing of the URA3 gene of Kluyveromyces !1marxianus CBS 6556. !$#cross-references MUID:93348780; PMID:8346683 !$#accession S33964 !'##molecule_type DNA !'##residues 1-267 ##label BER !'##cross-references EMBL:Z21934; NID:g313024; PIDN:CAA79928.1; !1PID:g313025 GENETICS !$#gene URA3 !$#map_position 6 CLASSIFICATION #superfamily orotidine-5'-phosphate decarboxylase; !1orotidine-5'-phosphate decarboxylase homology KEYWORDS carbon-carbon lyase; carboxy-lyase; pyrimidine nucleotide !1biosynthesis FEATURE !$4-264 #domain orotidine-5'-phosphate decarboxylase homology !8#label OPD SUMMARY #length 267 #molecular-weight 29295 #checksum 1627 SEQUENCE /// ENTRY DCVKOP #type complete TITLE orotidine-5'-phosphate decarboxylase (EC 4.1.1.23) - yeast (Kluyveromyces marxianus var. lactis) ALTERNATE_NAMES OMP decarboxylase; orotidine-5'-phosphate carboxy-lyase ORGANISM #formal_name Kluyveromyces marxianus var. lactis, Candida sphaerica DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jun-2000 ACCESSIONS A27836; JT0411 REFERENCE A27836 !$#authors Shuster, J.R.; Moyer, D.; Irvine, B. !$#journal Nucleic Acids Res. (1987) 15:8573 !$#title Sequence of the Kluyveromyces lactis URA3 gene. !$#cross-references MUID:88040483; PMID:3671096 !$#accession A27836 !'##molecule_type DNA !'##residues 1-267 ##label SHU !'##cross-references GB:Y00454; NID:g2905; PIDN:CAA68509.1; PID:g2906 REFERENCE JT0411 !$#authors Mizukami, M.; Hishinuma, F. !$#journal Agric. Biol. Chem. (1988) 52:3067-3071 !$#title Isolation and nucleotide sequence analysis of the URA3 !1(orotidine 5'-phosphate decarboxylase) gene of Kluyveromyces !1lactis. !$#accession JT0411 !'##molecule_type DNA !'##residues 1-267 ##label MIZ !'##cross-references GB:D00431; NID:g218526; PIDN:BAA00333.1; !1PID:g218527 GENETICS !$#gene ura3 CLASSIFICATION #superfamily orotidine-5'-phosphate decarboxylase; !1orotidine-5'-phosphate decarboxylase homology KEYWORDS carbon-carbon lyase; carboxy-lyase; pyrimidine nucleotide !1biosynthesis FEATURE !$4-264 #domain orotidine-5'-phosphate decarboxylase homology !8#label OPD SUMMARY #length 267 #molecular-weight 29241 #checksum 2671 SEQUENCE /// ENTRY S31323 #type complete TITLE orotidine-5'-phosphate decarboxylase (EC 4.1.1.23) - yeast (Pichia angusta) ORGANISM #formal_name Pichia angusta DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 20-Apr-2000 ACCESSIONS S31323 REFERENCE S31323 !$#authors Merckelbach, A.; Goedecke, S.; Janowicz, Z.A.; Hollenberg, !1C.P. !$#submission submitted to the EMBL Data Library, November 1992 !$#description Cloning and sequencing of the URA3 locus of the !1methylotrophic yeast Hansenula polymorpha and its use for !1the generation of a deletion by gene replacement. !$#accession S31323 !'##status preliminary !'##molecule_type DNA !'##residues 1-263 ##label MER !'##cross-references EMBL:X69461; NID:g2783; PIDN:CAA49221.1; PID:g2784 CLASSIFICATION #superfamily orotidine-5'-phosphate decarboxylase; !1orotidine-5'-phosphate decarboxylase homology KEYWORDS carbon-carbon lyase; carboxy-lyase FEATURE !$3-263 #domain orotidine-5'-phosphate decarboxylase homology !8#label OPD SUMMARY #length 263 #molecular-weight 29275 #checksum 2775 SEQUENCE /// ENTRY S08503 #type complete TITLE orotidine 5'-phosphate decarboxylase - fission yeast (Schizosaccharomyces pombe) ORGANISM #formal_name Schizosaccharomyces pombe DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Dec-1999 ACCESSIONS S08503; T41315 REFERENCE S08503 !$#authors Grimm, C.; Kohli, J.; Murray, J.; Maundrell, K. !$#journal Mol. Gen. Genet. (1988) 215:81-86 !$#title Genetic engineering of Schizosaccharomyces pombe: a system !1for gene disruption and replacement using the ura4 gene as a !1selectable marker. !$#cross-references MUID:89201250; PMID:3241624 !$#accession S08503 !'##status preliminary !'##molecule_type DNA !'##residues 1-264 ##label GRI !'##cross-references EMBL:X13976; NID:g5133; PIDN:CAA32157.1; PID:g5134 REFERENCE Z21987 !$#authors Gwilliam, R.; Barrell, B.G.; Rajandream, M.A.; Wedler, H.; !1Wambutt, R. !$#submission submitted to the EMBL Data Library, September 1998 !$#accession T41315 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-264 ##label GWI !'##cross-references EMBL:AL031603; PIDN:CAA20910.1; GSPDB:GN00068; !1SPDB:SPCC330.05c !'##experimental_source strain 972h-; cosmid c330 GENETICS !$#gene SPCC330.05c !$#map_position 3 CLASSIFICATION #superfamily orotidine-5'-phosphate decarboxylase; !1orotidine-5'-phosphate decarboxylase homology FEATURE !$7-262 #domain orotidine-5'-phosphate decarboxylase homology !8#label OPD SUMMARY #length 264 #molecular-weight 29362 #checksum 4904 SEQUENCE /// ENTRY DCCKA #type complete TITLE orotidine-5'-phosphate decarboxylase (EC 4.1.1.23) - yeast (Candida albicans) ALTERNATE_NAMES OMP decarboxylase; orotidine-5'-phosphate carboxy-lyase ORGANISM #formal_name Candida albicans DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 07-May-1999 ACCESSIONS A48331; S05969 REFERENCE A48331 !$#authors Losberger, C.; Ernst, J.F. !$#journal Curr. Genet. (1989) 16:153-157 !$#title Sequence and transcript analysis of the Candida albicans !1URA3 gene encoding orotidine-5'-phosphate decarboxylase. !$#cross-references MUID:90090693; PMID:2574635 !$#accession A48331 !'##molecule_type DNA !'##residues 1-270 ##label LOS !'##cross-references EMBL:X14198 !'##note submitted to the EMBL Data Library, January 1989 GENETICS !$#gene URA3 CLASSIFICATION #superfamily orotidine-5'-phosphate decarboxylase; !1orotidine-5'-phosphate decarboxylase homology KEYWORDS carbon-carbon lyase; carboxy-lyase; pyrimidine nucleotide !1biosynthesis FEATURE !$6-268 #domain orotidine-5'-phosphate decarboxylase homology !8#label OPD SUMMARY #length 270 #molecular-weight 30004 #checksum 3315 SEQUENCE /// ENTRY JS0721 #type complete TITLE orotidine-5'-phosphate decarboxylase (EC 4.1.1.23) - yeast (Candida maltosa) ALTERNATE_NAMES OMP decarboxylase; orotidine-5'-phosphate carboxy-lyase ORGANISM #formal_name Candida maltosa DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jun-2000 ACCESSIONS S29791; JS0721 REFERENCE S29791 !$#authors Ohkuma, M.; Muraoka, S.; Hwang, C.W.; Ohta, A.; Takagi, M. !$#journal Curr. Genet. (1993) 23:205-210 !$#title Cloning of the C-URA3 gene and construction of a triple !1auxotroph (his5, ade1, ura3) as a useful host for the !1genetic engineering of Candida maltosa. !$#cross-references MUID:93169682; PMID:8435849 !$#accession S29791 !'##molecule_type DNA !'##residues 1-266 ##label OHK !'##cross-references EMBL:D12720; NID:g218375; PIDN:BAA02215.1; !1PID:g218376 GENETICS !$#gene C-URA3; pyrG CLASSIFICATION #superfamily orotidine-5'-phosphate decarboxylase; !1orotidine-5'-phosphate decarboxylase homology KEYWORDS carbon-carbon lyase; carboxy-lyase; pyrimidine nucleotide !1biosynthesis FEATURE !$5-265 #domain orotidine-5'-phosphate decarboxylase homology !8#label OPD SUMMARY #length 266 #molecular-weight 29306 #checksum 2521 SEQUENCE /// ENTRY DCUMOP #type complete TITLE orotidine-5'-phosphate decarboxylase (EC 4.1.1.23) - Phycomyces blakesleeanus ALTERNATE_NAMES OMP decarboxylase; orotidine-5'-phosphate carboxy-lyase ORGANISM #formal_name Phycomyces blakesleeanus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS S13736 REFERENCE S13736 !$#authors Diaz-Minguez, J.M.; Iturriaga, E.A.; Benito, E.P.; !1Corrochano, L.M.; Eslava, A.P. !$#journal Mol. Gen. Genet. (1990) 224:269-278 !$#title Isolation and molecular analysis of the !1orotidine-5'-phosphate decarboxylase gene (pyrG) of !1Phycomyces blakesleeanus. !$#cross-references MUID:91117195; PMID:2277645 !$#accession S13736 !'##molecule_type DNA !'##residues 1-267 ##label DIA !'##cross-references GB:X53601; NID:g3114; PIDN:CAA37670.1; PID:g3115 CLASSIFICATION #superfamily orotidine-5'-phosphate decarboxylase; !1orotidine-5'-phosphate decarboxylase homology KEYWORDS carbon-carbon lyase; carboxy-lyase; pyrimidine nucleotide !1biosynthesis FEATURE !$7-263 #domain orotidine-5'-phosphate decarboxylase homology !8#label OPD SUMMARY #length 267 #molecular-weight 29899 #checksum 1905 SEQUENCE /// ENTRY JC1177 #type complete TITLE orotidine-5'-phosphate decarboxylase (EC 4.1.1.23) - Rhizomucor circinelloides ALTERNATE_NAMES OMP decarboxylase; orotidine-5'-phosphate carboxy-lyase ORGANISM #formal_name Rhizomucor circinelloides DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 07-Jul-1995 ACCESSIONS JC1177 REFERENCE JC1177 !$#authors Benito, E.P.; Diaz-Minguez, J.M.; Iturriaga, E.A.; !1Campuzano, V.; Eslava, A.P. !$#journal Gene (1992) 116:59-67 !$#title Cloning and sequence analysis of the Mucor circinelloides !1pyrG gene encoding orotidine-5'-monophosphate decarboxylase: !1Use of pyrG for homologous transformation. !$#cross-references MUID:92331950; PMID:1628845 !$#accession JC1177 !'##molecule_type DNA !'##residues 1-265 ##label BEN !'##cross-references GB:M69112 !'##note the authors translated the codon CAA for residue 244 as Glu GENETICS !$#gene pyrG !$#introns 60/3; 98/1 CLASSIFICATION #superfamily orotidine-5'-phosphate decarboxylase; !1orotidine-5'-phosphate decarboxylase homology KEYWORDS carbon-carbon lyase; carboxy-lyase; pyrimidine nucleotide !1biosynthesis FEATURE !$5-261 #domain orotidine-5'-phosphate decarboxylase homology !8#label OPD SUMMARY #length 265 #molecular-weight 29514 #checksum 4264 SEQUENCE /// ENTRY DCSJOS #type complete TITLE orotidine-5'-phosphate decarboxylase (EC 4.1.1.23) - bracket fungus (Schizophyllum commune) ALTERNATE_NAMES OMP decarboxylase; orotidine-5'-phosphate carboxy-lyase ORGANISM #formal_name Schizophyllum commune DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS JQ0122 REFERENCE JQ0122 !$#authors Froeliger, E.H.; Ullrich, R.C.; Novotny, C.P. !$#journal Gene (1989) 83:387-393 !$#title Sequence analysis of the URA1 gene encoding !1orotidine-5'-monophosphate decarboxylase of Schizophyllum !1commune. !$#cross-references MUID:90060853; PMID:2684794 !$#accession JQ0122 !'##molecule_type DNA !'##residues 1-278 ##label FRO !'##cross-references GB:M26019; NID:g169872; PIDN:AAA33928.1; !1PID:g169873 COMMENT This enzyme catalyzes the conversion of !1orotidine-5'-monophosphate to UMP in the last enzymatic !1reaction in the biosynthesis of pyrimidines. GENETICS !$#gene URA1 !$#introns 62/3; 101/1 CLASSIFICATION #superfamily orotidine-5'-phosphate decarboxylase; !1orotidine-5'-phosphate decarboxylase homology KEYWORDS carbon-carbon lyase; carboxy-lyase; pyrimidine nucleotide !1biosynthesis FEATURE !$7-275 #domain orotidine-5'-phosphate decarboxylase homology !8#label OPD SUMMARY #length 278 #molecular-weight 29979 #checksum 740 SEQUENCE /// ENTRY DCUSOP #type complete TITLE orotidine-5'-phosphate decarboxylase (EC 4.1.1.23) - smut fungus (Ustilago maydis) ALTERNATE_NAMES OMP decarboxylase; orotidine-5'-phosphate carboxy-lyase ORGANISM #formal_name Ustilago maydis #common_name corn smut DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 27-Jun-1994 ACCESSIONS JQ0013 REFERENCE JQ0013 !$#authors Kronstad, J.W.; Wang, J.; Covert, S.F.; Holden, D.W.; !1McKnight, G.L.; Leong, S.A. !$#journal Gene (1989) 79:97-106 !$#title Isolation of metabolic genes and demonstration of gene !1disruption in the phytopathogenic fungus Ustilago maydis. !$#cross-references MUID:89378782; PMID:2673937 !$#accession JQ0013 !'##molecule_type mRNA !'##residues 1-283 ##label KRO !'##cross-references GB:M27247 COMMENT This basidiomycetous fungus causes boil smut on maize (Zea !1mays). GENETICS !$#gene pyr6 CLASSIFICATION #superfamily orotidine-5'-phosphate decarboxylase; !1orotidine-5'-phosphate decarboxylase homology KEYWORDS carbon-carbon lyase; carboxy-lyase; pyrimidine nucleotide !1biosynthesis FEATURE !$7-272 #domain orotidine-5'-phosphate decarboxylase homology !8#label OPD SUMMARY #length 283 #molecular-weight 30894 #checksum 7317 SEQUENCE /// ENTRY DCPLOC #type complete TITLE orotidine-5'-phosphate decarboxylase (EC 4.1.1.23) - Penicillium chrysogenum ALTERNATE_NAMES OMP decarboxylase; orotidine-5'-phosphate carboxy-lyase ORGANISM #formal_name Penicillium chrysogenum DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 27-Jun-1994 ACCESSIONS S01287 REFERENCE S01287 !$#authors Cantoral, J.M.; Barredo, J.L.; Alvarez, E.; Diez, B.; !1Martin, J.F. !$#journal Nucleic Acids Res. (1988) 16:8177 !$#title Nucleotide sequence of the Penicillium chrysogenum pyrG !1(orotidine-5'-phosphate decarboxylase) gene. !$#cross-references MUID:88335559; PMID:3138658 !$#accession S01287 !'##molecule_type DNA !'##residues 1-275 ##label CAN !'##cross-references EMBL:X08037 GENETICS !$#gene pyrG !$#introns 53/1 CLASSIFICATION #superfamily orotidine-5'-phosphate decarboxylase; !1orotidine-5'-phosphate decarboxylase homology KEYWORDS carbon-carbon lyase; carboxy-lyase; pyrimidine nucleotide !1biosynthesis FEATURE !$7-273 #domain orotidine-5'-phosphate decarboxylase homology !8#label OPD SUMMARY #length 275 #molecular-weight 29813 #checksum 698 SEQUENCE /// ENTRY DCASON #type complete TITLE orotidine-5'-phosphate decarboxylase (EC 4.1.1.23) - Aspergillus niger ALTERNATE_NAMES OMP decarboxylase; orotidine-5'-phosphate carboxy-lyase ORGANISM #formal_name Aspergillus niger DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS S03652 REFERENCE S03652 !$#authors Wilson, L.J.; Carmona, C.L.; Ward, M. !$#journal Nucleic Acids Res. (1988) 16:2339 !$#title Sequence of the Aspergillus niger pyrG gene. !$#cross-references MUID:88189829; PMID:3357784 !$#accession S03652 !'##molecule_type DNA !'##residues 1-277 ##label WIL !'##cross-references EMBL:X06626; NID:g2394; PIDN:CAA29838.1; PID:g2395 GENETICS !$#gene pyrG !$#introns 53/1 CLASSIFICATION #superfamily orotidine-5'-phosphate decarboxylase; !1orotidine-5'-phosphate decarboxylase homology KEYWORDS carbon-carbon lyase; carboxy-lyase; pyrimidine nucleotide !1biosynthesis FEATURE !$7-275 #domain orotidine-5'-phosphate decarboxylase homology !8#label OPD SUMMARY #length 277 #molecular-weight 30196 #checksum 7500 SEQUENCE /// ENTRY DCASOE #type complete TITLE orotidine-5'-phosphate decarboxylase (EC 4.1.1.23) - Emericella nidulans ALTERNATE_NAMES OMP decarboxylase; orotidine-5'-phosphate carboxy-lyase ORGANISM #formal_name Emericella nidulans, Aspergillus nidulans DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS A29630 REFERENCE A29630 !$#authors Oakley, B.R.; Rinehart, J.E.; Mitchell, B.L.; Oakley, C.E.; !1Carmona, C.; Gray, G.L.; May, G.S. !$#journal Gene (1987) 61:385-399 !$#title Cloning, mapping and molecular analysis of the pyrG !1(orotidine-5'-phosphate decarboxylase) gene of Aspergillus !1nidulans. !$#cross-references MUID:88185841; PMID:3328733 !$#accession A29630 !'##molecule_type DNA !'##residues 1-274 ##label OAK !'##cross-references GB:M19132; NID:g168075; PIDN:AAB66359.1; !1PID:g168076 !'##note the authors translated the codon GAT for residue 70 as Pro, CTC !1for residue 71 as Ser, and CTT for residue 164 as Glu GENETICS !$#gene pyrG !$#introns 53/1 CLASSIFICATION #superfamily orotidine-5'-phosphate decarboxylase; !1orotidine-5'-phosphate decarboxylase homology KEYWORDS carbon-carbon lyase; carboxy-lyase; pyrimidine nucleotide !1biosynthesis FEATURE !$7-273 #domain orotidine-5'-phosphate decarboxylase homology !8#label OPD SUMMARY #length 274 #molecular-weight 30053 #checksum 5020 SEQUENCE /// ENTRY S74852 #type complete TITLE orotidine 5' monophosphate decarboxylase - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein sll0838 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S74852 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74852 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-231 ##label KAN !'##cross-references EMBL:D90909; GB:AB001339; NID:g1652844; !1PIDN:BAA17813.1; PID:g1652895 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene pyrF CLASSIFICATION #superfamily orotidine-5'-phosphate decarboxylase; !1orotidine-5'-phosphate decarboxylase homology SUMMARY #length 231 #molecular-weight 24705 #checksum 6579 SEQUENCE /// ENTRY I40172 #type complete TITLE orotidine-5'-phosphate decarboxylase (EC 4.1.1.23) - Bacillus caldolyticus ORGANISM #formal_name Bacillus caldolyticus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS I40172; S34324 REFERENCE I40166 !$#authors Ghim, S.Y.; Neuhard, J. !$#journal J. Bacteriol. (1994) 176:3698-3707 !$#title The pyrimidine biosynthesis operon of the thermophile !1Bacillus caldolyticus includes genes for uracil !1phosphoribosyltransferase and uracil permease. !$#cross-references MUID:94266723; PMID:8206848 !$#accession I40172 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-244 ##label RES !'##cross-references EMBL:X73308; NID:g312439; PIDN:CAA51742.1; !1PID:g580762 GENETICS !$#gene pyrF !$#start_codon GTG CLASSIFICATION #superfamily orotidine-5'-phosphate decarboxylase; !1orotidine-5'-phosphate decarboxylase homology KEYWORDS carbon-carbon lyase; carboxy-lyase SUMMARY #length 244 #molecular-weight 26579 #checksum 7530 SEQUENCE /// ENTRY DCCEOC #type complete TITLE orotidine-5'-phosphate decarboxylase (EC 4.1.1.23) - fungus (Acremonium chrysogenum) ALTERNATE_NAMES OMP decarboxylase; orotidine-5'-phosphate carboxy-lyase ORGANISM #formal_name Acremonium chrysogenum DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS S06746 REFERENCE S06746 !$#authors Vian, A.; Penalva, M.A. !$#journal Nucleic Acids Res. (1989) 17:8874 !$#title Nucleotide sequence of the Cephalosporium acremonium pyr4 !1gene. !$#cross-references MUID:90067869; PMID:2587233 !$#accession S06746 !'##molecule_type DNA !'##residues 1-376 ##label VIA !'##cross-references EMBL:X15937; NID:g2514; PIDN:CAA34063.1; PID:g2515 !'##note the source is designated as Cephalosporium acremonium GENETICS !$#gene pyr4 CLASSIFICATION #superfamily orotidine-5'-phosphate decarboxylase; !1orotidine-5'-phosphate decarboxylase homology KEYWORDS carbon-carbon lyase; carboxy-lyase; pyrimidine nucleotide !1biosynthesis FEATURE !$9-376 #domain orotidine-5'-phosphate decarboxylase homology !8#label OPD SUMMARY #length 376 #molecular-weight 41128 #checksum 8185 SEQUENCE /// ENTRY DCNCOP #type complete TITLE orotidine-5'-phosphate decarboxylase (EC 4.1.1.23) - Neurospora crassa ALTERNATE_NAMES OMP decarboxylase; orotidine-5'-phosphate carboxy-lyase ORGANISM #formal_name Neurospora crassa DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS A24398 REFERENCE A24398 !$#authors Newbury, S.F.; Glazebrook, J.A.; Radford, A. !$#journal Gene (1986) 43:51-58 !$#title Sequence analysis of the pyr-4 (orotidine 5'-P !1decarboxylase) gene of Neurospora crassa. !$#cross-references MUID:87005949; PMID:3019837 !$#accession A24398 !'##molecule_type DNA !'##residues 1-397 ##label NEW !'##cross-references GB:M13448; NID:g168867; PIDN:AAA33611.1; !1PID:g168868 GENETICS !$#gene pyr4 CLASSIFICATION #superfamily orotidine-5'-phosphate decarboxylase; !1orotidine-5'-phosphate decarboxylase homology KEYWORDS carbon-carbon lyase; carboxy-lyase; pyrimidine nucleotide !1biosynthesis FEATURE !$15-394 #domain orotidine-5'-phosphate decarboxylase homology !8#label OPD SUMMARY #length 397 #molecular-weight 43903 #checksum 9845 SEQUENCE /// ENTRY DCECOP #type complete TITLE orotidine-5'-phosphate decarboxylase (EC 4.1.1.23) - Escherichia coli (strain K-12) ALTERNATE_NAMES OMP decarboxylase; orotidine-5'-phosphate carboxy-lyase ORGANISM #formal_name Escherichia coli DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 01-Mar-2002 ACCESSIONS A28440; D64876 REFERENCE A92598 !$#authors Turnbough Jr., C.L.; Kerr, K.H.; Funderburg, W.R.; Donahue, !1J.P.; Powell, F.E. !$#journal J. Biol. Chem. (1987) 262:10239-10245 !$#title Nucleotide sequence and characterization of the pyrF operon !1of Escherichia coli K12. !$#cross-references MUID:87280048; PMID:2956254 !$#accession A28440 !'##molecule_type DNA !'##residues 1-245 ##label TUR !'##cross-references GB:J02768; NID:g147474; PIDN:AAA24483.1; !1PID:g147475 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64876 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-245 ##label BLAT !'##cross-references GB:AE000226; GB:U00096; NID:g2367115; !1PIDN:AAC74363.1; PID:g1787537; UWGP:b1281 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene pyrF; purF !$#map_position 28 min FUNCTION !$#description catalyzes the cleavage of orotidine 5'-phosphate into carbon !1dioxide and UMP !$#pathway pyrimidine nucleotide biosynthesis CLASSIFICATION #superfamily orotidine-5'-phosphate decarboxylase; !1orotidine-5'-phosphate decarboxylase homology KEYWORDS carbon-carbon lyase; carboxy-lyase; homodimer; pyrimidine !1nucleotide biosynthesis FEATURE !$1-245 #domain orotidine-5'-phosphate decarboxylase homology !8#label OPD\ !$73 #active_site Lys #status predicted SUMMARY #length 245 #molecular-weight 26350 #checksum 1499 SEQUENCE /// ENTRY DCEBOT #type complete TITLE orotidine-5'-phosphate decarboxylase (EC 4.1.1.23) - Salmonella typhimurium ALTERNATE_NAMES OMP decarboxylase; orotidine-5'-phosphate carboxy-lyase ORGANISM #formal_name Salmonella typhimurium DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS A27190 REFERENCE A91182 !$#authors Theisen, M.; Kelln, R.A.; Neuhard, J. !$#journal Eur. J. Biochem. (1987) 164:613-619 !$#title Cloning and characterization of the pyrF operon of !1Salmonella typhimurium. !$#cross-references MUID:87190435; PMID:2436909 !$#accession A27190 !'##molecule_type DNA !'##residues 1-245 ##label THE !'##cross-references GB:X05382; NID:g403031; PIDN:CAA28973.1; !1PID:g805068 GENETICS !$#gene pyrF !$#map_position 33 min FUNCTION !$#description catalyzes the cleavage of orotidine 5'-phosphate into carbon !1dioxide and UMP !$#pathway pyrimidine nucleotide biosynthesis CLASSIFICATION #superfamily orotidine-5'-phosphate decarboxylase; !1orotidine-5'-phosphate decarboxylase homology KEYWORDS carbon-carbon lyase; carboxy-lyase; homodimer; pyrimidine !1nucleotide biosynthesis FEATURE !$1-245 #domain orotidine-5'-phosphate decarboxylase homology !8#label OPD\ !$73 #active_site Lys #status predicted SUMMARY #length 245 #molecular-weight 26243 #checksum 237 SEQUENCE /// ENTRY DCHUA #type complete TITLE aromatic-L-amino-acid decarboxylase (EC 4.1.1.28) - human ALTERNATE_NAMES DOPA decarboxylase; hydroxytryptophan decarboxylase; tryptophan decarboxylase ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 31-Mar-2000 ACCESSIONS A33663; A42205; I54174; I52961; I39381; A45191; B42205; !1B45191; C42205; C45191; D42205; D45191; E42205; F42205; !1G42205; H42205; I42205; J42205 REFERENCE A33663 !$#authors Ichinose, H.; Kurosawa, Y.; Titani, K.; Fujita, K.; Nagatsu, !1T. !$#journal Biochem. Biophys. Res. Commun. (1989) 164:1024-1030 !$#title Isolation and characterization of a cDNA clone encoding !1human aromatic L-amino acid decarboxylase. !$#cross-references MUID:90073624; PMID:2590185 !$#accession A33663 !'##molecule_type mRNA !'##residues 1-480 ##label ICH !'##cross-references GB:M76180; NID:g181520; PIDN:AAA58437.1; !1PID:g181521 REFERENCE A42205 !$#authors Sumi-Ichinose, C.; Ichinose, H.; Takahashi, E.; Hori, T.; !1Nagatsu, T. !$#journal Biochemistry (1992) 31:2229-2238 !$#title Molecular cloning of genomic DNA and chromosomal assignment !1of the gene for human aromatic L-amino acid decarboxylase, !1the enzyme for catecholamine and serotonin biosynthesis. !$#cross-references MUID:92172843; PMID:1540578 !$#accession A42205 !'##molecule_type DNA !'##residues !11-6;65-70;103-108;143-149;189-193;236-241;258-263;290-295; !1313-318;338-343;345-351;379-383;412-417 ##label SUM !'##experimental_source placenta !'##note sequence modified after extraction from NCBI backbone !'##note intron-exon boundaries are shown REFERENCE I54174 !$#authors Scherer, L.J.; McPherson, J.D.; Wasmuth, J.J.; Marsh, J.L. !$#journal Genomics (1992) 13:469-471 !$#title Human dopa decarboxylase: localization to human chromosome !17p11 and characterization of hepatic cDNAs. !$#cross-references MUID:92307691; PMID:1612608 !$#accession I54174 !'##status preliminary; nucleic acid sequence not shown; translated from !1GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-480 ##label RES !'##cross-references GB:M88700; NID:g181650; PIDN:AAA20894.1; !1PID:g181651 REFERENCE I52961 !$#authors Craig, S.P.; Thai, A.L.; Weber, M.; Craig, I.W. !$#journal Cytogenet. Cell Genet. (1992) 61:114-116 !$#title Localisation of the gene for human aromatic L-amino acid !1decarboxylase (DDC) to chromosome 7p13-->p11 by in situ !1hybridisation. !$#cross-references MUID:93009861; PMID:1395716 !$#accession I52961 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 68-105 ##label RE2 !'##cross-references GB:S46516; NID:g257537; PIDN:AAB23675.1; !1PID:g257538 REFERENCE I39381 !$#authors Le Van Thai, A.; Coste, E.; Allen, J.M.; Palmiter, R.D.; !1Weber, M.J. !$#journal Brain Res. Mol. Brain Res. (1993) 17:227-238 !$#title Identification of a neuron-specific promoter of human !1aromatic L-amino acid decarboxylase gene. !$#cross-references MUID:93287794; PMID:8510497 !$#accession I39381 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-48,'G',50-67 ##label RE3 !'##cross-references GB:L05075; NID:g177935; PIDN:AAB59432.1; !1PID:g177937 COMMENT This enzyme catalyzes the decarboxylation of aromatic amino !1acids, including tryptophan, 5-hydroxy-tryptophan, and !1dihydroxy-phenylalanine (DOPA), to corresponding amines. GENETICS !$#gene GDB:DDC; AADC !'##cross-references GDB:127738; OMIM:107930 !$#map_position 7p11-7p11 !$#introns 67/3; 105/3; 145/3; 190/3; 238/3; 261/1; 293/1; 315/2; 341/ !11; 347/3; 380/3; 414/3 CLASSIFICATION #superfamily aromatic-L-amino-acid decarboxylase; animal !1histidine decarboxylase homology KEYWORDS carbon-carbon lyase; carboxy-lyase; phosphoprotein; !1pyridoxal phosphate FEATURE !$2-471 #domain animal histidine decarboxylase homology !8#label HDC\ !$303 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 480 #molecular-weight 53894 #checksum 7665 SEQUENCE /// ENTRY DEGPA #type complete TITLE aromatic-L-amino-acid decarboxylase (EC 4.1.1.28) - guinea pig ALTERNATE_NAMES DOPA decarboxylase; hydroxytryptophan decarboxylase; tryptophan decarboxylase ORGANISM #formal_name Cavia porcellus #common_name guinea pig DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 31-Mar-2000 ACCESSIONS A35710 REFERENCE A35710 !$#authors Taketoshi, M.; Horio, Y.; Imamura, I.; Tanaka, T.; Fukui, !1H.; Wada, H. !$#journal Biochem. Biophys. Res. Commun. (1990) 170:1229-1235 !$#title Molecular cloning of guinea-pig aromatic-L-amino acid !1decarboxylase cDNA. !$#cross-references MUID:90358824; PMID:2390088 !$#accession A35710 !'##molecule_type mRNA !'##residues 1-480 ##label TAK !'##cross-references GB:M58049; NID:g191254; PIDN:AAA51530.1; !1PID:g191255 CLASSIFICATION #superfamily aromatic-L-amino-acid decarboxylase; animal !1histidine decarboxylase homology KEYWORDS carbon-carbon lyase; carboxy-lyase; phosphoprotein; !1pyridoxal phosphate FEATURE !$2-471 #domain animal histidine decarboxylase homology !8#label HDC\ !$303 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 480 #molecular-weight 54150 #checksum 1776 SEQUENCE /// ENTRY DCRTA #type complete TITLE aromatic-L-amino-acid decarboxylase (EC 4.1.1.28) - rat ALTERNATE_NAMES DOPA decarboxylase; hydroxytryptophan decarboxylase; tryptophan decarboxylase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 31-Mar-2000 ACCESSIONS A33994; I59415; A47192 REFERENCE A33994 !$#authors Tanaka, T.; Horio, Y.; Taketoshi, M.; Imamura, I.; !1Ando-Yamamoto, M.; Kangawa, K.; Matsuo, H.; Kuroda, M.; !1Wada, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:8142-8146 !$#title Molecular cloning and sequencing of a cDNA of rat dopa !1decarboxylase: partial amino acid homologies with other !1enzymes synthesizing catecholamines. !$#cross-references MUID:90046754; PMID:2813383 !$#accession A33994 !'##molecule_type mRNA !'##residues 1-480 ##label TAN !'##cross-references GB:M27716; NID:g203949; PIDN:AAA41087.1; !1PID:g203950 REFERENCE I59415 !$#authors Rorsman, F.; Husebye, E.S.; Winqvist, O.; Bjork, E.; !1Karlsson, F.A.; Kampe, O. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1995) 92:8626-8629 !$#title Aromatic-L-amino-acid decarboxylase, a pyridoxal !1phosphate-dependent enzyme, is a beta-cell autoantigen. !$#cross-references MUID:96004593; PMID:7567987 !$#accession I59415 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-197,'X',199-475,'IDFSVTSQ' ##label RES !'##cross-references EMBL:U31884; NID:g975308; PIDN:AAA85565.1; !1PID:g975309 !'##experimental_source insulinoma cells REFERENCE A47192 !$#authors Albert, V.R.; Lee, M.R.; Bolden, A.H.; Wurzburger, R.J.; !1Aguanno, A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:12053-12057 !$#title Distinct promoters direct neuronal and nonneuronal !1expression of rat aromatic L-amino acid decarboxylase. !$#cross-references MUID:93101665; PMID:1465439 !$#accession A47192 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-67 ##label RE2 !'##cross-references GB:L03417; NID:g453687; PIDN:AAA99905.1; !1PID:g453689 CLASSIFICATION #superfamily aromatic-L-amino-acid decarboxylase; animal !1histidine decarboxylase homology KEYWORDS alternative splicing; carbon-carbon lyase; carboxy-lyase; !1phosphoprotein; pyridoxal phosphate FEATURE !$2-471 #domain animal histidine decarboxylase homology !8#label HDC\ !$303 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 480 #molecular-weight 54053 #checksum 2385 SEQUENCE /// ENTRY DCFFD1 #type complete TITLE aromatic-L-amino-acid decarboxylase (EC 4.1.1.28) 1 - fruit fly (Drosophila sp.) ALTERNATE_NAMES DOPA decarboxylase long isozyme; hydroxytryptophan decarboxylase long isozyme; tryptophan decarboxylase long isozyme ORGANISM #formal_name Drosophila sp. DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 31-Mar-2000 ACCESSIONS A25697 REFERENCE A91053 !$#authors Eveleth, D.D.; Gietz, R.D.; Spencer, C.A.; Nargang, F.E.; !1Hodgetts, R.B.; Marsh, J.L. !$#journal EMBO J. (1986) 5:2663-2672 !$#title Sequence and structure of the dopa decarboxylase gene of !1Drosophila: evidence for novel RNA splicing variants. !$#cross-references MUID:87053836; PMID:3023054 !$#accession A25697 !'##molecule_type DNA !'##residues 1-511 ##label EVE !'##cross-references GB:X04426 COMMENT This enzyme catalyzes the decarboxylation of aromatic amino !1acids, including tryptophan, 5-hydroxy-tryptophan, and !1dihydroxy-phenylalanine (DOPA), to corresponding amines. In !1fruit fly, it is essential for the central nervous system, !1and it is necessary in the hypoderm for pigmentation and !1hardening of the cuticle. GENETICS !$#gene Ddc !'##cross-references FlyBase:FBgn0000422 !$#introns 33/3; 62/2 CLASSIFICATION #superfamily aromatic-L-amino-acid decarboxylase; animal !1histidine decarboxylase homology KEYWORDS alternative splicing; carbon-carbon lyase; carboxy-lyase; !1phosphoprotein; pyridoxal phosphate FEATURE !$37-504 #domain animal histidine decarboxylase homology !8#label HDC\ !$338 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 511 #molecular-weight 56771 #checksum 3215 SEQUENCE /// ENTRY DCFFD2 #type complete TITLE aromatic-L-amino-acid decarboxylase (EC 4.1.1.28) 2 - fruit fly (Drosophila sp.) ALTERNATE_NAMES DOPA decarboxylase short isozyme; hydroxytryptophan decarboxylase short isozyme; tryptophan decarboxylase short isozyme ORGANISM #formal_name Drosophila sp. DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 31-Mar-2000 ACCESSIONS B25697 REFERENCE A91053 !$#authors Eveleth, D.D.; Gietz, R.D.; Spencer, C.A.; Nargang, F.E.; !1Hodgetts, R.B.; Marsh, J.L. !$#journal EMBO J. (1986) 5:2663-2672 !$#title Sequence and structure of the dopa decarboxylase gene of !1Drosophila: evidence for novel RNA splicing variants. !$#cross-references MUID:87053836; PMID:3023054 !$#accession B25697 !'##molecule_type DNA !'##residues 1-503 ##label EVE !'##cross-references GB:X04426 GENETICS !$#gene Ddc !'##cross-references FlyBase:FBgn0000422 !$#introns 54/2 CLASSIFICATION #superfamily aromatic-L-amino-acid decarboxylase; animal !1histidine decarboxylase homology KEYWORDS alternative splicing; carbon-carbon lyase; carboxy-lyase; !1phosphoprotein; pyridoxal phosphate FEATURE !$29-496 #domain animal histidine decarboxylase homology !8#label HDC\ !$330 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 503 #molecular-weight 56346 #checksum 3754 SEQUENCE /// ENTRY DCFFA #type complete TITLE aromatic-L-amino-acid decarboxylase (EC 4.1.1.28) - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES DOPA decarboxylase; hydroxytryptophan decarboxylase; tryptophan decarboxylase ORGANISM #formal_name Drosophila melanogaster DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 21-Jul-2000 ACCESSIONS A25709; S01106 REFERENCE A25709 !$#authors Morgan, B.A.; Johnson, W.A.; Hirsh, J. !$#journal EMBO J. (1986) 5:3335-3342 !$#title Regulated splicing produces different forms of dopa !1decarboxylase in the central nervous system and hypoderm of !1Drosophila melanogaster. !$#cross-references MUID:87133496; PMID:3102230 !$#accession A25709 !'##molecule_type DNA !'##residues 1-510 ##label MOR !'##cross-references GB:X04661; GB:M24111; GB:X16802 REFERENCE S01102 !$#authors Eveleth, D.D.; Marsh, J.L. !$#journal Mol. Gen. Genet. (1987) 209:290-298 !$#title Overlapping transcription units in Drosophila: sequence and !1structure of the Cs gene. !$#cross-references MUID:88038375; PMID:3478553 !$#accession S01106 !'##status translation not shown !'##molecule_type DNA !'##residues 493-510 ##label EVE !'##cross-references EMBL:X05991; NID:g7759; PIDN:CAA29409.2; !1PID:g4455923 GENETICS !$#gene FlyBase:Ddc !'##cross-references FlyBase:FBgn0000422 !$#introns 33/3; 62/2 CLASSIFICATION #superfamily aromatic-L-amino-acid decarboxylase; animal !1histidine decarboxylase homology KEYWORDS carbon-carbon lyase; carboxy-lyase; phosphoprotein; !1pyridoxal phosphate FEATURE !$37-503 #domain animal histidine decarboxylase homology !8#label HDC\ !$337 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 510 #molecular-weight 57202 #checksum 8059 SEQUENCE /// ENTRY DCJAAP #type complete TITLE aromatic-L-amino-acid decarboxylase (EC 4.1.1.28) - Madagascar periwinkle ALTERNATE_NAMES DOPA decarboxylase; hydroxytryptophan decarboxylase; tryptophan decarboxylase ORGANISM #formal_name Catharanthus roseus #common_name Madagascar periwinkle DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 31-Mar-2000 ACCESSIONS A32103; S41726; S25471 REFERENCE A32103 !$#authors De Luca, V.; Marineau, C.; Brisson, N. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:2582-2586 !$#title Molecular cloning and analysis of cDNA encoding a plant !1tryptophan decarboxylase: comparison with animal dopa !1decarboxylases. !$#cross-references MUID:89202373; PMID:2704736 !$#accession A32103 !'##molecule_type mRNA !'##residues 1-500 ##label DEL !'##cross-references GB:M25151; NID:g167489; PIDN:AAA33109.1; !1PID:g167490; GB:J04521 REFERENCE S41726 !$#authors Goddijn, O.J.M.; Lohman, F.P.; de Kam, R.J.; Schilperoort, !1R.A.; Hoge, J.H.C. !$#journal Mol. Gen. Genet. (1994) 242:217-225 !$#title Nucleotide sequence of the tryptophan decarboxylase gene of !1Catharanthus roseus and expression of tdc-gusA gene fusions !1in Nicotiana tabacum. !$#cross-references MUID:94211212; PMID:8159173 !$#accession S41726 !'##status preliminary !'##molecule_type DNA !'##residues 1-500 ##label GOD !'##cross-references EMBL:X67662; NID:g18225; PIDN:CAA47898.1; !1PID:g18226 COMMENT This enzyme catalyzes the decarboxylation of aromatic amino !1acids, including tryptophan, 5-hydroxy-tryptophan, and !1dihydroxy-phenylalanine (DOPA), to corresponding amines. CLASSIFICATION #superfamily aromatic-L-amino-acid decarboxylase; animal !1histidine decarboxylase homology KEYWORDS carbon-carbon lyase; carboxy-lyase; phosphoprotein; !1pyridoxal phosphate FEATURE !$23-493 #domain animal histidine decarboxylase homology !8#label HDC\ !$319 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 500 #molecular-weight 56206 #checksum 107 SEQUENCE /// ENTRY A44405 #type complete TITLE tyrosine decarboxylase (EC 4.1.1.25) - parsley ORGANISM #formal_name Petroselinum crispum #common_name parsley DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 31-Mar-2000 ACCESSIONS A44405 REFERENCE A44405 !$#authors Kawalleck, P.; Keller, H.; Hahlbrock, K.; Scheel, D.; !1Somssich, I.E. !$#journal J. Biol. Chem. (1993) 268:2189-2194 !$#title A pathogen-responsive gene of parsley encodes tyrosine !1decarboxylase. !$#cross-references MUID:93131981; PMID:8420986 !$#accession A44405 !'##molecule_type DNA !'##residues 1-514 ##label KAW !'##cross-references GB:M96070; NID:g169670; PIDN:AAA33860.1; !1PID:g169671 !'##note sequence extracted from NCBI backbone (NCBIP:123215) GENETICS !$#gene tyrCD CLASSIFICATION #superfamily aromatic-L-amino-acid decarboxylase; animal !1histidine decarboxylase homology KEYWORDS carbon-carbon lyase; carboxy-lyase; pyridoxal phosphate FEATURE !$21-496 #domain animal histidine decarboxylase homology !8#label HDC SUMMARY #length 514 #molecular-weight 57449 #checksum 7428 SEQUENCE /// ENTRY QYMG #type complete TITLE phosphoenolpyruvate carboxylase (EC 4.1.1.31) - sorghum ORGANISM #formal_name Sorghum bicolor DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 18-Jul-2001 ACCESSIONS S08216 REFERENCE S08216 !$#authors Cretin, C.; Keryer, E.; Tagu, D.; Lepiniec, L.; Vidal, J.; !1Gadal, P. !$#journal Nucleic Acids Res. (1990) 18:658 !$#title Complete cDNA sequence of sorghum phosphoenolpyruvate !1carboxylase involved in C4 photosynthesis. !$#cross-references MUID:90174996; PMID:2308851 !$#accession S08216 !'##molecule_type mRNA !'##residues 1-952 ##label CRE !'##cross-references EMBL:X17379 COMMENT This enzyme catalyzes the carboxylation (by carbon dioxide) !1of phosphoenolpyruvate to form oxaloacetate, a four-carbon !1dicarboxylic acid source for the tricarboxylic acid cycle. CLASSIFICATION #superfamily phosphoenolpyruvate carboxylase KEYWORDS allosteric regulation; carbon dioxide fixation; !1carbon-carbon lyase; carboxy-lyase; phosphoprotein SUMMARY #length 952 #molecular-weight 107742 #checksum 57 SEQUENCE /// ENTRY QYZM #type complete TITLE phosphoenolpyruvate carboxylase (EC 4.1.1.31) - maize ORGANISM #formal_name Zea mays #common_name maize #variety strain B73 DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 18-Jun-1999 ACCESSIONS S04546; S28889; A30937; A23509; S00348; S13491 REFERENCE S04546 !$#authors Hudspeth, R.L.; Grula, J.W. !$#journal Plant Mol. Biol. (1989) 12:579-589 !$#title Structure and expression of the maize gene encoding the !1phosphoenolpyruvate carboxylase isozyme involved in C(4) !1photosynthesis. !$#accession S04546 !'##molecule_type DNA !'##residues 1-970 ##label HUD1 !'##cross-references GB:X15239; NID:g22407; PIDN:CAA33317.1; PID:g22408 !$#accession S28889 !'##molecule_type mRNA !'##residues 1-238,'A',240-970 ##label HUD2 !'##cross-references EMBL:X15238; NID:g22562; PIDN:CAA33316.1; !1PID:g22563 REFERENCE A30937 !$#authors Hudspeth, R.L.; Grula, J.W. !$#submission submitted to GenBank, May 1989 !$#accession A30937 !'##molecule_type DNA !'##residues 1-840,842-970 ##label HUD3 !'##cross-references GB:X15238 REFERENCE A23509 !$#authors Izui, K.; Ishijima, S.; Yamaguchi, Y.; Katagiri, F.; Murata, !1T.; Shigesada, K.; Sugiyama, T.; Katsuki, H. !$#journal Nucleic Acids Res. (1986) 14:1615-1628 !$#title Cloning and sequence analysis of cDNA encoding active !1phosphoenolpyruvate carboxylase of the C4-pathway from !1maize. !$#cross-references MUID:86148496; PMID:3005978 !$#accession A23509 !'##molecule_type mRNA !'##residues 39-337,'DV',340-481,'S',483-556,'PAV',560-569,'S',571-572, !1'LR',575-686,'S',688-735,'P',737-962,'R',964-970 ##label IZU !'##cross-references GB:X15238 REFERENCE S00348 !$#authors Yanagisawa, S.; Izui, K.; Yamaguchi, Y.; Shigesada, K.; !1Katsuki, H. !$#journal FEBS Lett. (1988) 229:107-110 !$#title Further analysis of cDNA clones for maize !1phosphoenolpyruvate carboxylase involved in C4 !1photosynthesis. Nucleotide sequence of entire open reading !1frame and evidence for polyadenylation of mRNA at multiple !1sites in vivo. !$#cross-references MUID:88152202; PMID:2894322 !$#accession S00348 !'##molecule_type mRNA !'##residues 1-82 ##label YAN !'##cross-references EMBL:X07168 REFERENCE S13491 !$#authors Jiao, J.; Podesta, F.E.; Chollet, R.; O'Leary, M.H.; Andreo, !1C.S. !$#journal Biochim. Biophys. Acta (1990) 1041:291-295 !$#title Isolation and sequence of an active-site peptide from maize !1leaf phosphoenolpyruvate carboxylase inactivated by !1pyridoxal 5'-phosphate. !$#cross-references MUID:91098247; PMID:2268676 !$#accession S13491 !'##molecule_type protein !'##residues 599-610 ##label JIA COMMENT This enzyme catalyzes the carboxylation (by carbon dioxide) !1of phosphoenolpyruvate to form oxaloacetate, a four-carbon !1dicarboxylic acid source for the tricarboxylic acid cycle. GENETICS !$#introns 60/3; 192/2; 220/3; 295/1; 329/3; 360/1; 411/3; 744/3; 873/3 CLASSIFICATION #superfamily phosphoenolpyruvate carboxylase KEYWORDS carbon dioxide fixation; carbon-carbon lyase; carboxy-lyase; !1homotetramer; phosphoprotein SUMMARY #length 970 #molecular-weight 109340 #checksum 5258 SEQUENCE /// ENTRY QYNT #type complete TITLE phosphoenolpyruvate carboxylase (EC 4.1.1.31) - common tobacco ORGANISM #formal_name Nicotiana tabacum #common_name common tobacco DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 18-Jun-1999 ACCESSIONS S17440 REFERENCE S17440 !$#authors Koizumi, N.; Sato, F.; Terano, Y.; Yamada, Y. !$#journal Plant Mol. Biol. (1991) 17:535-539 !$#title Sequence analysis of cDNA encoding phosphoenolpyruvate !1carboxylase from cultured tobacco cells. !$#cross-references MUID:91355949; PMID:1884006 !$#accession S17440 !'##molecule_type mRNA !'##residues 1-964 ##label KOI !'##cross-references EMBL:X59016; NID:g22588; PIDN:CAA41758.1; !1PID:g22589 CLASSIFICATION #superfamily phosphoenolpyruvate carboxylase KEYWORDS carbon dioxide fixation; carbon-carbon lyase; carboxy-lyase; !1phosphoprotein SUMMARY #length 964 #molecular-weight 110162 #checksum 8848 SEQUENCE /// ENTRY QYIX2 #type complete TITLE phosphoenolpyruvate carboxylase (EC 4.1.1.31) 2 - common ice plant ORGANISM #formal_name Mesembryanthemum crystallinum #common_name common ice plant DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 21-Jul-2000 ACCESSIONS S05550 REFERENCE S05550 !$#authors Cushman, J.C.; Bohnert, H.J. !$#journal Nucleic Acids Res. (1989) 17:6743-6744 !$#title Nucleotide sequence of the Ppc2 gene encoding a housekeeping !1isoform of phosphoenolpyruvate carboxylase from !1Mesembryanthemum crystallinum. !$#cross-references MUID:89386016; PMID:2780305 !$#accession S05550 !'##molecule_type DNA !'##residues 1-960 ##label CUS !'##cross-references EMBL:X14588; NID:g22560; PIDN:CAA32728.2; !1PID:g4469271 COMMENT This enzyme catalyzes the carboxylation (by carbon dioxide) !1of phosphoenolpyruvate to form oxaloacetate, a four-carbon !1dicarboxylic acid source for the tricarboxylic acid cycle. GENETICS !$#gene ppc2 !$#introns 48/3; 180/2; 208/3; 283/1; 317/3; 347/1; 398/3; 731/3; 860/2 CLASSIFICATION #superfamily phosphoenolpyruvate carboxylase KEYWORDS carbon dioxide fixation; carbon-carbon lyase; carboxy-lyase SUMMARY #length 960 #molecular-weight 109182 #checksum 8998 SEQUENCE /// ENTRY QYIX1 #type complete TITLE phosphoenolpyruvate carboxylase (EC 4.1.1.31) 1 - common ice plant ORGANISM #formal_name Mesembryanthemum crystallinum #common_name common ice plant DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 18-Jun-1999 ACCESSIONS S05506; S02716; S26236 REFERENCE S05506 !$#authors Cushman, J.C.; Bohnert, H.J. !$#journal Nucleic Acids Res. (1989) 17:6745 !$#title Nucleotide sequence of the gene encoding a CAM specific !1isoform of phosphoenolpyruvate carboxylase from !1Mesembryanthemum crystallinum. !$#cross-references MUID:89386017; PMID:2780306 !$#accession S05506 !'##molecule_type DNA !'##residues 1-966 ##label CUS !'##cross-references EMBL:X14587; NID:g22558; PIDN:CAA32727.1; !1PID:g22559 REFERENCE S02716 !$#authors Rickers, J.; Cushman, J.C.; Michalowski, C.B.; Schmitt, !1J.M.; Bohnert, H.J. !$#journal Mol. Gen. Genet. (1989) 215:447-454 !$#title Expression of the CAM-form of phospho(enol)pyruvate !1carboxylase and nucleotide sequence of a full length cDNA !1from Mesembryanthemum crystallinum. !$#cross-references MUID:89218954; PMID:2710107 !$#accession S02716 !'##molecule_type mRNA !'##residues 1-966 ##label RIC !'##cross-references EMBL:X13660; NID:g19535; PIDN:CAA31956.1; !1PID:g19536 REFERENCE S26236 !$#authors Cushman, J.C.; Bohnert, H.J. !$#journal Plant Mol. Biol. (1992) 20:411-424 !$#title Salt stress alters A/T-rich DNA-binding factor interactions !1within the phosphoenolpyruvate carboxylase promoter from !1Mesembryanthemum crystallinum. !$#cross-references MUID:93043032; PMID:1421145 !$#accession S26236 !'##molecule_type DNA !'##residues 1-25 ##label CU2 !'##cross-references EMBL:X63774; NID:g19533; PIDN:CAA45309.1; !1PID:g19534 COMMENT This enzyme catalyzes the carboxylation (by carbon dioxide) !1of phosphoenolpyruvate to form oxaloacetate, a four-carbon !1dicarboxylic acid source for the tricarboxylic acid cycle. GENETICS !$#gene ppc1 !$#introns 56/3; 188/2; 216/3; 291/1; 325/3; 354/3; 406/3; 739/3; 868/3 CLASSIFICATION #superfamily phosphoenolpyruvate carboxylase KEYWORDS carbon dioxide fixation; carbon-carbon lyase; carboxy-lyase; !1phosphoprotein SUMMARY #length 966 #molecular-weight 110659 #checksum 725 SEQUENCE /// ENTRY QYEC #type complete TITLE phosphoenolpyruvate carboxylase (EC 4.1.1.31) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 01-Mar-2002 ACCESSIONS A01083; C42377; I58235; G65202; I55248 REFERENCE A01083 !$#authors Fujita, N.; Miwa, T.; Ishijima, S.; Izui, K.; Katsuki, H. !$#journal J. Biochem. (1984) 95:909-916 !$#title The primary structure of phosphoenolpyruvate carboxylase of !1Escherichia coli. Nucleotide sequence of the ppc gene and !1deduced amino acid sequence. !$#cross-references MUID:84264425; PMID:6086598 !$#accession A01083 !'##molecule_type DNA !'##residues 1-883 ##label FUJ !'##cross-references GB:X05903; NID:g48665; PIDN:CAA29332.1; PID:g48666 REFERENCE A42377 !$#authors Meinnel, T.; Schmitt, E.; Mechulam, Y.; Blanquet, S. !$#journal J. Bacteriol. (1992) 174:2323-2331 !$#title Structural and biochemical characterization of the !1Escherichia coli argE gene product. !$#cross-references MUID:92202162; PMID:1551850 !$#accession C42377 !'##status preliminary !'##molecule_type DNA !'##residues 1-37 ##label MEI !'##cross-references GB:X55417 REFERENCE I58235 !$#authors Izui, K.; Miwa, T.; Kajitani, M.; Fujita, N.; Sabe, H.; !1Ishihama, A.; Katsuki, H. !$#journal Nucleic Acids Res. (1985) 13:59-71 !$#title Promoter analysis of the phosphoenolpyruvate carboxylase !1gene of Escherichia coli. !$#cross-references MUID:85215476; PMID:3889833 !$#accession I58235 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-41 ##label RES !'##cross-references EMBL:X01700; NID:g42476; PIDN:CAA25847.1; !1PID:g42477 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65202 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-883 ##label BLAT !'##cross-references GB:AE000469; GB:U00096; NID:g1790385; !1PIDN:AAC76938.1; PID:g1790393; UWGP:b3956 !'##experimental_source strain K-12, substrain MG1655 REFERENCE I55248 !$#authors Sutton, F.; Butler, E.T. !$#journal J. Biol. Chem. (1986) 261:16078-16081 !$#title Isolation of the structural gene encoding a mutant form of !1Escherichia coli phosphoenolpyruvate carboxylase deficient !1in regulation by fructose 1,6-bisphosphate: Identification !1of an amino acid substitution in the mutant. !$#cross-references MUID:87057272; PMID:3536922 !$#accession I55248 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 173-187,'I',189-271 ##label RE2 !'##cross-references GB:J02632; NID:g147340; PIDN:AAA24414.1; !1PID:g147341 !'##experimental_source mutant strain PpcI !'##note the replacement of 188-Thr by Ile is the single change !1responsible for inability of the mutant form to be activated !1by fructose 1,6-bisphosphate GENETICS !$#gene ppc !$#map_position 89 min COMPLEX homotetramer FUNCTION !$#description catalyzes the carboxylation (by carbon dioxide) of !1phosphoenolpyruvate to form oxaloacetate, a four-carbon !1dicarboxylic acid source for the tricarboxylic acid cycle; !1it has distinct binding sites for each of the allosteric !1effectors such as acetyl-CoA, fructose 1,6-bisphosphate, !1guanosine 3'-diphosphate 5'-diphosphate, long chain fatty !1acids, and L-aspartate CLASSIFICATION #superfamily phosphoenolpyruvate carboxylase KEYWORDS allosteric regulation; carbon dioxide fixation; !1carbon-carbon lyase; carboxy-lyase SUMMARY #length 883 #molecular-weight 99062 #checksum 8180 SEQUENCE /// ENTRY QYFKG #type complete TITLE phosphoenolpyruvate carboxylase (EC 4.1.1.31) - Corynebacterium glutamicum ORGANISM #formal_name Corynebacterium glutamicum DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 18-Jun-1999 ACCESSIONS S05512; JS0183 REFERENCE S05511 !$#authors Eikmanns, B.J.; Follettie, M.T.; Griot, M.U.; Sinskey, A.J. !$#journal Mol. Gen. Genet. (1989) 218:330-339 !$#title The phosphoenolpyruvate carboxylase gene of Corynebacterium !1glutamicum: molecular cloning, nucleotide sequence, and !1expression. !$#cross-references MUID:89384460; PMID:2779518 !$#accession S05512 !'##molecule_type DNA !'##residues 1-919 ##label EIK !'##cross-references GB:X14234; NID:g48688; PIDN:CAA32450.1; PID:g48689 !'##note the authors translated the codon ATT for residue 387 as Glu, !1AAA for residue 553 as His, TTA for residue 800 as Phe, and !1CCC for residue 801 as Thr REFERENCE JS0183 !$#authors O'Regan, M.; Thierbach, G.; Bachmann, B.; Villeval, D.; !1Lepage, P.; Viret, J.F.; Lemoine, Y. !$#journal Gene (1989) 77:237-251 !$#title Cloning and nucleotide sequence of the phosphoenolpyruvate !1carboxylase-coding gene of Corynebacterium glutamicum !1ATCC13032. !$#cross-references MUID:89326141; PMID:2666264 !$#accession JS0183 !'##molecule_type DNA !'##residues 1-606,'KL',609-799,'FT',802-914,'L',916-919 ##label ORE !'##cross-references GB:M25819; NID:g144984; PIDN:AAA83537.1; !1PID:g144985 !'##experimental_source ATCC 13032 !'##note residues 2-15 were confirmed by protein sequencing COMMENT This enzyme catalyzes the carboxylation (by carbon dioxide) !1of phosphoenolpyruvate to form oxaloacetate, a four-carbon !1dicarboxylic acid source for the tricarboxylic acid cycle. COMMENT The activity of this protein is not stimulated by acetyl-CoA !1in the absence of any allosteric inhibitor, whereas the !1corresponding protein from Escherichia coli is strongly !1stimulated. GENETICS !$#gene ppc CLASSIFICATION #superfamily phosphoenolpyruvate carboxylase KEYWORDS allosteric regulation; carbon dioxide fixation; !1carbon-carbon lyase; carboxy-lyase FEATURE !$2-919 #product phosphoenolpyruvate carboxylase #status !8predicted #label MAT\ !$611-624 #region substrate binding #status predicted SUMMARY #length 919 #molecular-weight 103116 #checksum 6803 SEQUENCE /// ENTRY QYYC #type complete TITLE phosphoenolpyruvate carboxylase (EC 4.1.1.31) - Synechococcus sp. (strain PCC 6301) ORGANISM #formal_name Synechococcus sp. DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 28-May-1999 ACCESSIONS A24517 REFERENCE A24517 !$#authors Katagiri, F.; Kodaki, T.; Fujita, N.; Izui, K.; Katsuki, H. !$#journal Gene (1985) 38:265-269 !$#title Nucleotide sequence of the phosphoenolpyruvate carboxylase !1gene of the cyanobacterium Anacystis nidulans. !$#cross-references MUID:86056986; PMID:2998946 !$#accession A24517 !'##molecule_type DNA !'##residues 1-1053 ##label KAT !'##cross-references GB:M11198; NID:g142140; PIDN:AAA22052.1; !1PID:g142141 !'##note the source is designated as Anacystis nidulans COMMENT This enzyme catalyzes the carboxylation (by carbon dioxide) !1of phosphoenolpyruvate to form oxaloacetate, a four-carbon !1dicarboxylic acid source for the tricarboxylic acid cycle. GENETICS !$#gene ppc CLASSIFICATION #superfamily phosphoenolpyruvate carboxylase KEYWORDS allosteric regulation; carbon dioxide fixation; !1carbon-carbon lyase; carboxy-lyase SUMMARY #length 1053 #molecular-weight 121083 #checksum 3712 SEQUENCE /// ENTRY A44831 #type complete TITLE phosphoenolpyruvate carboxylase (EC 4.1.1.31) - Anabaena sp. ORGANISM #formal_name Anabaena sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A44831 REFERENCE A44831 !$#authors Luinenburg, I.; Coleman, J.R. !$#journal J. Gen. Microbiol. (1992) 138:685-691 !$#title Identification, characterization and sequence analysis of !1the gene encoding phosphoenolpyruvate carboxylase in !1Anabaena sp. PCC 7120. !$#cross-references MUID:92268848; PMID:1588304 !$#accession A44831 !'##molecule_type DNA !'##residues 1-982 ##label LUI !'##experimental_source PCC 7120 !'##note sequence extracted from NCBI backbone (NCBIN:103682, !1NCBIP:103683) CLASSIFICATION #superfamily phosphoenolpyruvate carboxylase KEYWORDS allosteric regulation; carbon dioxide fixation; !1carbon-carbon lyase; carboxy-lyase SUMMARY #length 982 #molecular-weight 112696 #checksum 1580 SEQUENCE /// ENTRY QYRTGP #type complete TITLE phosphoenolpyruvate carboxykinase (GTP) (EC 4.1.1.32), cytosolic - rat ALTERNATE_NAMES phosphoenolpyruvate carboxylase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 18-Jun-1999 ACCESSIONS A23927; B23927; A31803; S34603 REFERENCE A23927 !$#authors Beale, E.G.; Chrapkiewicz, N.B.; Scoble, H.A.; Metz, R.J.; !1Quick, D.P.; Noble, R.L.; Donelson, J.E.; Biemann, K.; !1Granner, D.K. !$#journal J. Biol. Chem. (1985) 260:10748-10760 !$#title Rat hepatic cytosolic phosphoenolpyruvate carboxykinase !1(GTP). Structures of the protein, messenger RNA, and gene. !$#cross-references MUID:85289263; PMID:2993287 !$#accession A23927 !'##molecule_type DNA !'##residues 1-622 ##label BEA !'##cross-references GB:K03248; NID:g206065; PIDN:AAC98698.1; !1PID:g206067 !$#accession B23927 !'##molecule_type mRNA !'##residues 1-622 ##label BEA2 !'##cross-references GB:K03243; GB:K03244; GB:K03245; GB:K03246; !1GB:K03247; GB:K03248; NID:g206065; PIDN:AAC98698.1; !1PID:g206067 REFERENCE A31803 !$#authors Lewis, C.T.; Seyer, J.M.; Carlson, G.M. !$#journal J. Biol. Chem. (1989) 264:27-33 !$#title Cysteine 288: an essential hyperreactive thiol of cytosolic !1phosphoenolpyruvate carboxykinase (GTP). !$#cross-references MUID:89079663; PMID:2909519 !$#accession A31803 !'##molecule_type protein !'##residues 279-290 ##label LEW REFERENCE S34602 !$#authors Rojas, M.C.; Encinas, M.V.; Kemp, R.G.; Latshaw, S.P.; !1Cardemil, E. !$#journal Biochim. Biophys. Acta (1993) 1164:143-151 !$#title Identification of reactive vicinal cysteines in !1Saccharomyces cerevisiae (ATP) and cytosolic rat liver (GTP) !1phosphoenolpyruvate carboxykinases. !$#cross-references MUID:93320103; PMID:8329445 !$#accession S34603 !'##status preliminary !'##molecule_type protein !'##residues 279-287,'X',289-290,406-412,'X',414-425 ##label ROJ COMMENT This enzyme catalyzes the formation of phosphoenolpyruvate !1by transferring the phosphate group from GTP to oxaloacetate !1with decarboxylation; it is a rate-limiting gluconeogenic !1enzyme whose activity is affected by a number of hormones !1regulating this metabolic process. COMMENT This enzyme is not to be confused with phosphoenolpyruvate !1carboxylase (EC 4.1.1.31), which catalyzes a similar !1reaction using orthophosphate (instead of GTP) as the !1phosphate donor. GENETICS !$#introns 75/2; 136/1; 204/1; 266/3; 321/1; 396/1; 439/3; 472/1 CLASSIFICATION #superfamily phosphoenolpyruvate carboxykinase (GTP) KEYWORDS carbon-carbon lyase; carboxy-lyase; gluconeogenesis; GTP !1binding; P-loop FEATURE !$237-244 #region nucleotide-binding motif A (P-loop) #status !8atypical\ !$288 #active_site Cys #status experimental SUMMARY #length 622 #molecular-weight 69415 #checksum 6006 SEQUENCE /// ENTRY QYCHGC #type complete TITLE phosphoenolpyruvate carboxykinase (GTP) (EC 4.1.1.32), cytosolic - chicken ALTERNATE_NAMES phosphoenolpyruvate carboxylase ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS A26494 REFERENCE A26494 !$#authors Cook, J.S.; Weldon, S.L.; Garcia-Ruiz, J.P.; Hod, Y.; !1Hanson, R.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:7583-7587 !$#title Nucleotide sequence of the mRNA encoding the cytosolic form !1of phosphoenolpyruvate carboxykinase (GTP) from the chicken. !$#cross-references MUID:87016993; PMID:3094011 !$#accession A26494 !'##molecule_type mRNA !'##residues 1-622 ##label COO !'##cross-references GB:M14229; NID:g212537; PIDN:AAA49005.1; !1PID:g212538 COMMENT This enzyme catalyzes the formation of phosphoenolpyruvate !1by transferring the phosphate group from GTP to oxaloacetate !1with decarboxylation; it is a rate-limiting gluconeogenic !1enzyme whose activity is affected by a number of hormones !1regulating this metabolic process. CLASSIFICATION #superfamily phosphoenolpyruvate carboxykinase (GTP) KEYWORDS carbon-carbon lyase; carboxy-lyase; gluconeogenesis; GTP !1binding; P-loop FEATURE !$237-244 #region nucleotide-binding motif A (P-loop) #status !8atypical\ !$288 #active_site Cys #status predicted SUMMARY #length 622 #molecular-weight 69528 #checksum 2313 SEQUENCE /// ENTRY QYCHGM #type complete TITLE phosphoenolpyruvate carboxykinase (GTP) (EC 4.1.1.32) precursor, mitochondrial - chicken ALTERNATE_NAMES phosphoenolpyruvate carboxylase ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 28-Feb-1997 ACCESSIONS A35191 REFERENCE A35191 !$#authors Weldon, S.L.; Rando, A.; Matathias, A.S.; Hod, Y.; Kalonick, !1P.A.; Savon, S.; Cook, J.S.; Hanson, R.W. !$#journal J. Biol. Chem. (1990) 265:7308-7317 !$#title Mitochondrial phosphoenolpyruvate carboxykinase from the !1chicken. Comparison of the cDNA and protein sequences with !1the cytosolic isozyme. !$#cross-references MUID:90237025; PMID:2110163 !$#accession A35191 !'##molecule_type mRNA !'##residues 1-640 ##label WEL !'##cross-references GB:J05419 COMMENT This enzyme catalyzes the formation of phosphoenolpyruvate !1by transferring the phosphate group from GTP to oxaloacetate !1with decarboxylation; it is a rate-limiting gluconeogenic !1enzyme whose activity is affected by a number of hormones !1regulating this metabolic process. CLASSIFICATION #superfamily phosphoenolpyruvate carboxykinase (GTP) KEYWORDS carbon-carbon lyase; carboxy-lyase; gluconeogenesis; GTP !1binding; mitochondrion; P-loop FEATURE !$1-33 #domain transit peptide (mitochondrion) #status !8predicted #label TRP\ !$34-640 #product phosphoenolpyruvate carboxykinase (GTP) !8#status predicted #label MAT\ !$255-262 #region nucleotide-binding motif A (P-loop) #status !8atypical\ !$306 #active_site Cys #status predicted SUMMARY #length 640 #molecular-weight 70971 #checksum 68 SEQUENCE /// ENTRY QYFFGM #type complete TITLE phosphoenolpyruvate carboxykinase (GTP) (EC 4.1.1.32) precursor, mitochondrial - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES phosphoenolpyruvate carboxylase ORGANISM #formal_name Drosophila melanogaster DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS A26809 REFERENCE A26809 !$#authors Gundelfinger, E.D.; Hermans-Borgmeyer, I.; Grenningloh, G.; !1Zopf, D. !$#journal Nucleic Acids Res. (1987) 15:6745 !$#title Nucleotide and deduced amino acid sequence of the !1phosphoenolpyruvate carboxykinase (GTP) from Drosophila !1melanogaster. !$#cross-references MUID:87316942; PMID:3114718 !$#accession A26809 !'##molecule_type mRNA !'##residues 1-647 ##label GUN !'##cross-references GB:Y00402; NID:g8326; PIDN:CAA68463.1; PID:g8327 COMMENT This enzyme catalyzes the formation of phosphoenolpyruvate !1by transferring the phosphate group from GTP to oxaloacetate !1with decarboxylation; it is a rate-limiting gluconeogenic !1enzyme whose activity is affected by a number of hormones !1regulating this metabolic process. GENETICS !$#gene zdf4 !'##cross-references FlyBase:FBgn0003067 CLASSIFICATION #superfamily phosphoenolpyruvate carboxykinase (GTP) KEYWORDS carbon-carbon lyase; carboxy-lyase; gluconeogenesis; GTP !1binding; mitochondrion; P-loop FEATURE !$263-270 #region nucleotide-binding motif A (P-loop) #status !8atypical\ !$314 #active_site Cys #status predicted SUMMARY #length 647 #molecular-weight 71127 #checksum 6652 SEQUENCE /// ENTRY RKMDS #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain - Cryptomonas sp. chloroplast ORGANISM #formal_name chloroplast Cryptomonas sp. DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 05-Sep-1997 ACCESSIONS S05289; S23706 REFERENCE S05288 !$#authors Douglas, S.E.; Durnford, D.G. !$#journal Plant Mol. Biol. (1989) 13:13-20 !$#title The small subunit of ribulose-1,5-bisphosphate carboxylase !1is plastid-encoded in the chlorophyll c-containing alga !1Cryptomonas phi. !$#cross-references MUID:93357429; PMID:2562756 !$#accession S05289 !'##molecule_type DNA !'##residues 1-139 ##label DOU !'##cross-references EMBL:X14171; NID:g11396; PID:g11398 REFERENCE S23705 !$#authors Douglas, S.E.; Durnford, D.G.; Morden, C.W. !$#journal J. Phycol. (1990) 26:500-508 !$#title Nucleotide sequence of the gene for the large subunit of !1ribulose-1,5-bisphosphate carboxylase/oxygenase from !1Cryptomonas phi: evidence supporting the polyphyletic origin !1of plastids. !$#accession S23706 !'##molecule_type DNA !'##residues 1-46 ##label DO2 !'##cross-references EMBL:X62349; NID:g11297; PID:g11299 GENETICS !$#genome chloroplast CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; monooxygenase; photorespiration SUMMARY #length 139 #molecular-weight 15984 #checksum 8813 SEQUENCE /// ENTRY RKAUS #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain - brown alga (Ectocarpus siliculosus) chloroplast ORGANISM #formal_name chloroplast Ectocarpus siliculosus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 18-Jun-1999 ACCESSIONS S13124 REFERENCE S13123 !$#authors Valentin, K.; Zetsche, K. !$#journal Plant Mol. Biol. (1990) 15:575-584 !$#title Rubisco genes indicate a close phylogenetic relation between !1the plastids of Chromophyta and Rhodophyta. !$#cross-references MUID:91338696; PMID:2102375 !$#accession S13124 !'##molecule_type DNA !'##residues 1-139 ##label VAL !'##cross-references EMBL:X52503; NID:g11543; PIDN:CAA36744.1; !1PID:g11545 GENETICS !$#genome chloroplast CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; monooxygenase; photorespiration SUMMARY #length 139 #molecular-weight 15938 #checksum 9975 SEQUENCE /// ENTRY RKPFSL #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain - brown alga (Pylaiella littoralis) chloroplast ORGANISM #formal_name chloroplast Pylaiella littoralis DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 18-Jun-1999 ACCESSIONS S17764 REFERENCE S17764 !$#authors Assali, N.E.; Martin, W.F.; Sommerville, C.C.; Loiseaux-de !1Goer, S. !$#journal Plant Mol. Biol. (1991) 17:853-863 !$#title Evolution of the Rubisco operon from prokaryotes to algae: !1structure and analysis of the rbcS gene of the brown alga !1Pylaiella littoralis. !$#cross-references MUID:92003695; PMID:1840691 !$#accession S17764 !'##molecule_type DNA !'##residues 1-139 ##label ASS !'##cross-references EMBL:X55372; NID:g14186; PIDN:CAA39052.1; !1PID:g14188 GENETICS !$#gene rbcS !$#genome chloroplast CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; monooxygenase; photorespiration; !1photosynthesis SUMMARY #length 139 #molecular-weight 15897 #checksum 9364 SEQUENCE /// ENTRY RKQMSY #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain - diatom (Cylindrotheca sp.) chloroplast (strain N1) ORGANISM #formal_name chloroplast Cylindrotheca sp. DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 18-Jun-1999 ACCESSIONS B38728 REFERENCE A38728 !$#authors Hwang, S.R.; Tabita, F.R. !$#journal J. Biol. Chem. (1991) 266:6271-6279 !$#title Cotranscription, deduced primary structure, and expression !1of the chloroplast-encoded rbcL and rbcS genes of the marine !1diatom Cylindrotheca sp. strain N1. !$#cross-references MUID:91177877; PMID:1706714 !$#accession B38728 !'##molecule_type DNA !'##residues 1-139 ##label HWA !'##cross-references GB:M59080; NID:g336750; PIDN:AAA84193.1; !1PID:g552515 GENETICS !$#gene rbcS !$#genome chloroplast CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; monooxygenase; photorespiration SUMMARY #length 139 #molecular-weight 15936 #checksum 7089 SEQUENCE /// ENTRY RKMLS #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain - golden alga (Olisthodiscus luteus) chloroplast ORGANISM #formal_name chloroplast Olisthodiscus luteus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 18-Jun-1999 ACCESSIONS A32940 REFERENCE A32940 !$#authors Boczar, B.A.; Delaney, T.P.; Cattolico, R.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:4996-4999 !$#title Gene for the ribulose-1,5-bisphosphate carboxylase small !1subunit protein of the marine chromophyte Olisthodiscus !1luteus is similar to that of a chemoautotrophic bacterium. !$#cross-references MUID:89296930; PMID:2740337 !$#accession A32940 !'##molecule_type DNA !'##residues 1-139 ##label BOC !'##cross-references GB:M24288; NID:g342811; PIDN:AAA84532.1; !1PID:g552794 GENETICS !$#gene rbcS !$#genome chloroplast CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carbon-oxygen lyase; carboxy-lyase; chloroplast; !1monooxygenase; photorespiration SUMMARY #length 139 #molecular-weight 15958 #checksum 8892 SEQUENCE /// ENTRY RKKKSA #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain - red alga (Antithamnion sp.) chloroplast ORGANISM #formal_name chloroplast Antithamnion sp. DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 30-Jun-1993 ACCESSIONS S14155 REFERENCE S14126 !$#authors Kostrzewa, M.; Valentin, K.; Maid, U.; Radetzky, R.; !1Zetsche, K. !$#journal Curr. Genet. (1990) 18:465-469 !$#title Structure of the rubisco operon from the multicellular red !1alga Antithamnion spec. !$#cross-references MUID:91176557; PMID:2078870 !$#accession S14155 !'##molecule_type DNA !'##residues 1-138 ##label KOS !'##cross-references EMBL:X54532 GENETICS !$#gene rbcS !$#genome chloroplast !$#start_codon GTG CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carbon-oxygen lyase; carboxy-lyase; chloroplast; !1monooxygenase; photorespiration SUMMARY #length 138 #molecular-weight 16143 #checksum 6380 SEQUENCE /// ENTRY RKKKSC #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain - red alga (Cyanidium caldarium) chloroplast ORGANISM #formal_name chloroplast Cyanidium caldarium DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 30-Jun-1993 ACCESSIONS S11942 REFERENCE S11941 !$#authors Valentin, K.; Zetsche, K. !$#journal Mol. Gen. Genet. (1990) 222:425-430 !$#title Structure of the Rubisco operon from the unicellular red !1alga Cyanidium caldarium: evidence for a polyphyletic origin !1of the plastids. !$#cross-references MUID:91109732; PMID:2274041 !$#accession S11942 !'##molecule_type DNA !'##residues 1-138 ##label VAL GENETICS !$#gene rbcS !$#genome chloroplast CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carbon-oxygen lyase; carboxy-lyase; chloroplast; !1monooxygenase; photorespiration SUMMARY #length 138 #molecular-weight 16205 #checksum 5529 SEQUENCE /// ENTRY RKALSE #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain - Alcaligenes eutrophus ORGANISM #formal_name Alcaligenes eutrophus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 05-Sep-1997 ACCESSIONS B26954 REFERENCE A91843 !$#authors Andersen, K.; Caton, J. !$#journal J. Bacteriol. (1987) 169:4547-4558 !$#title Sequence analysis of the Alcaligenes eutrophus chromosomally !1encoded ribulose bisphosphate carboxylase large and small !1subunit genes and their gene products. !$#cross-references MUID:88007394; PMID:2820933 !$#accession B26954 !'##molecule_type DNA !'##residues 1-135 ##label AND !'##cross-references GB:M17744; NID:g141966; PID:g141968 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS carbon dioxide fixation; carbon-carbon lyase; carbon-oxygen !1lyase; carboxy-lyase; monooxygenase; photorespiration SUMMARY #length 135 #molecular-weight 15579 #checksum 2357 SEQUENCE /// ENTRY RKQXSX #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain - Xanthobacter flavus ORGANISM #formal_name Xanthobacter flavus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 18-Jun-1999 ACCESSIONS S13574 REFERENCE S13573 !$#authors Meijer, W.G.; Arnberg, A.C.; Enequist, H.G.; Terpstra, P.; !1Lidstrom, M.E.; Dijkhuizen, L. !$#journal Mol. Gen. Genet. (1991) 225:320-330 !$#title Identification and organization of carbon dioxide fixation !1genes in Xanthobacter flavus H4-14. !$#cross-references MUID:91172133; PMID:1900916 !$#accession S13574 !'##molecule_type DNA !'##residues 1-133 ##label MEI !'##cross-references EMBL:X17252; NID:g48543; PIDN:CAA35116.1; !1PID:g48545 GENETICS !$#gene cfxS CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carbon-oxygen lyase; carboxy-lyase; monooxygenase; !1photorespiration SUMMARY #length 133 #molecular-weight 15318 #checksum 9204 SEQUENCE /// ENTRY RKRFAS #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) A small chain - Rhodobacter sphaeroides ORGANISM #formal_name Rhodobacter sphaeroides DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS E40767 REFERENCE A40767 !$#authors Gibson, J.L.; Falcone, D.L.; Tabita, F.R. !$#journal J. Biol. Chem. (1991) 266:14646-14653 !$#title Nucleotide sequence, transcriptional analysis, and !1expression of genes encoded within the form I CO-2 fixation !1operon of Rhodobacter sphaeroides. !$#cross-references MUID:91317831; PMID:1907281 !$#accession E40767 !'##molecule_type DNA !'##residues 1-129 ##label GIB !'##cross-references GB:M64624; NID:g151920; PIDN:AAA26116.1; !1PID:g151925 COMMENT This protein is encoded within the form I !1ribulose-bisphosphate carboxylase operon, which predominates !1when carbon dioxide is limiting. GENETICS !$#gene rbcS CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase SUMMARY #length 129 #molecular-weight 15164 #checksum 4601 SEQUENCE /// ENTRY RKKHS #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain precursor (clone pGLRu117) - tamarack ORGANISM #formal_name Larix laricina #common_name tamarack, American larch DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 18-Jun-1999 ACCESSIONS S15771; S08072 REFERENCE S15771 !$#authors Hutchison, K.W.; Harvie, P.D.; Singer, P.B.; Brunner, A.F.; !1Greenwood, M.S. !$#journal Plant Mol. Biol. (1990) 14:281-284 !$#title Nucleotide sequence of the small subunit of ribulose-1, !15-bisphosphate carboxylase from the conifer Larix laricina. !$#cross-references MUID:91329683; PMID:2101694 !$#accession S15771 !'##status preliminary !'##molecule_type DNA !'##residues 1-189 ##label HUT !'##cross-references EMBL:X16039; NID:g19467; PIDN:CAA34161.1; !1PID:g295822 !'##note submitted to the EMBL Data Library, August 1989 GENETICS !$#gene rbcS !$#introns 69/3; 113/3 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; monooxygenase; photorespiration FEATURE !$1-67 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$68-189 #product ribulose-bisphosphate carboxylase small !8chain #status predicted #label MAT SUMMARY #length 189 #molecular-weight 21191 #checksum 1222 SEQUENCE /// ENTRY RKSZSJ #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain precursor - Japanese black pine ORGANISM #formal_name Pinus thunbergiana #common_name Japanese black pine DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 18-Jun-1999 ACCESSIONS S02046 REFERENCE S02046 !$#authors Yamamoto, N.; Kano-Murakami, Y.; Matsuoka, M.; Ohashi, Y.; !1Tanaka, Y. !$#journal Nucleic Acids Res. (1988) 16:11830 !$#title Nucleotide sequence of a full length cDNA clone of ribulose !1bisphosphate carboxylase small subunit gene from green !1dark-grown pine (Pinus tunbergii) seedling. !$#cross-references MUID:89098344; PMID:3211759 !$#accession S02046 !'##molecule_type mRNA !'##residues 1-171 ##label YAM !'##cross-references EMBL:X13408; NID:g20957; PIDN:CAA31774.1; !1PID:g20958 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; monooxygenase; photorespiration FEATURE !$1-51 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$52-171 #product ribulose-bisphosphate carboxylase small !8chain #status predicted #label MAT SUMMARY #length 171 #molecular-weight 19312 #checksum 2194 SEQUENCE /// ENTRY RKIXS #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain precursor - common ice plant ORGANISM #formal_name Mesembryanthemum crystallinum #common_name common ice plant DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 18-Jun-1999 ACCESSIONS A29118 REFERENCE A29118 !$#authors DeRocher, E.J.; Ramage, R.T.; Michalowski, C.B.; Bohnert, !1H.J. !$#journal Nucleic Acids Res. (1987) 15:6301 !$#title Nucleotide sequence of a cDNA encoding rbcS from the desert !1plant Mesembryanthemum crystallinum. !$#cross-references MUID:87316892; PMID:3627990 !$#accession A29118 !'##molecule_type mRNA !'##residues 1-182 ##label DER !'##cross-references GB:M31640; NID:g167267; PIDN:AAA33035.1; !1PID:g167268 COMMENT Ribulose-bisphosphate carboxylase, a major component of leaf !1protein, is also a monooxygenase; it catalyzes the !1carboxylation of D-ribulose 1,5-bisphosphate (the primary !1event in photosynthetic carbon dioxide fixation) as well as !1the oxidative fragmentation of the pentose substrate in the !1photorespiration process. These reactions occur !1simultaneously and in competition at the same active site. COMMENT Each active molecule contains eight large chains, !1synthesized on the chloroplast ribosomes and containing the !1active site, and eight small chains, the precursors of which !1are synthesized on cytoplasmic ribosomes and converted to !1mature small chains during or immediately after transport !1into the chloroplast. COMMENT This protein is coded by one member of a small multigene !1family. CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carbon-oxygen lyase; carboxy-lyase; chloroplast; !1monooxygenase; photorespiration FEATURE !$1-57 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$58-182 #product ribulose-bisphosphate carboxylase small !8chain #status predicted #label MAT SUMMARY #length 182 #molecular-weight 20331 #checksum 5305 SEQUENCE /// ENTRY RKSYS #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain precursor SRS1 - soybean ORGANISM #formal_name Glycine max #common_name soybean DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 18-Jun-1999 ACCESSIONS A01084 REFERENCE A01084 !$#authors Berry-Lowe, S.L.; McKnight, T.D.; Shah, D.M.; Meagher, R.B. !$#journal J. Mol. Appl. Genet. (1982) 1:483-498 !$#title The nucleotide sequence, expression, and evolution of one !1member of a multigene family encoding the small subunit of !1ribulose-1,5-bisphosphate carboxylase in soybean. !$#cross-references MUID:83110645; PMID:7153686 !$#accession A01084 !'##molecule_type DNA !'##residues 1-178 ##label BER !'##cross-references GB:V00458; GB:J01307; NID:g18741; PIDN:CAA23736.1; !1PID:g18742 !'##experimental_source cv. Wayne COMMENT Ribulose-bisphosphate carboxylase, a major component of leaf !1protein, is also a monooxygenase; it catalyzes the !1carboxylation of D-ribulose 1,5-bisphosphate (the primary !1event in photosynthetic carbon dioxide fixation) as well as !1the oxidative fragmentation of the pentose substrate in the !1photorespiration process. These reactions occur !1simultaneously and in competition at the same active site. COMMENT Each active molecule contains eight large chains, !1synthesized on the chloroplast ribosomes and containing the !1active site, and eight small chains, the precursors of which !1are synthesized on cytoplasmic ribosomes and converted to !1mature small chains during or immediately after transport !1into the chloroplast. COMMENT This protein is coded by one member of a small multigene !1family. GENETICS !$#gene SRS1 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; monooxygenase; photorespiration FEATURE !$1-55 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$56-178 #product ribulose-bisphosphate carboxylase small !8chain #status experimental #label MAT SUMMARY #length 178 #molecular-weight 20072 #checksum 9922 SEQUENCE /// ENTRY RKSYS4 #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain precursor SRS4 - soybean ORGANISM #formal_name Glycine max #common_name soybean DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 18-Jun-1999 ACCESSIONS A30837 REFERENCE A30837 !$#authors Grandbastien, M.A.; Berry-Lowe, S.; Shirley, B.W.; Meagher, !1R.B. !$#journal Plant Mol. Biol. (1986) 7:451-465 !$#title Two soybean ribulose-1,5-bisphosphate carboxylase small !1subunit genes share extensive homology even in distant !1flanking sequences. !$#accession A30837 !'##molecule_type DNA !'##residues 1-178 ##label GRA !'##cross-references GB:M16889; NID:g170057; PIDN:AAA34008.1; !1PID:g170058 GENETICS !$#gene SRS4 !$#introns 57/3; 102/3 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carbon-oxygen lyase; carboxy-lyase; chloroplast; !1monooxygenase; photorespiration FEATURE !$1-55 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$56-178 #product ribulose-bisphosphate carboxylase small !8chain #status predicted #label MAT SUMMARY #length 178 #molecular-weight 20017 #checksum 18 SEQUENCE /// ENTRY RKNTSV #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain precursor - curled-leaved tobacco ORGANISM #formal_name Nicotiana plumbaginifolia #common_name curled-leaved tobacco DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 18-Jun-1999 ACCESSIONS S08318 REFERENCE S08318 !$#authors Poulsen, C.; Fluhr, R.; Kauffman, J.M.; Boutry, M.; Chua, !1N.H. !$#journal Mol. Gen. Genet. (1986) 205:193-200 !$#title Characterization of an rbcS gene from Nicotiana !1plumbaginifolia and expression of an rbcS-CAT chimeric gene !1in homologous and heterologous nuclear background. !$#accession S08318 !'##molecule_type DNA !'##residues 1-180 ##label POU !'##cross-references EMBL:X13711; NID:g19705; PIDN:CAA31994.1; !1PID:g19706 GENETICS !$#gene rbcS-8B !$#introns 59/3; 104/3; 122/3 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carbon-oxygen lyase; carboxy-lyase; chloroplast; !1monooxygenase; photorespiration FEATURE !$1-57 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$58-180 #product ribulose-bisphosphate carboxylase small !8chain #status experimental #label MAT SUMMARY #length 180 #molecular-weight 20358 #checksum 3351 SEQUENCE /// ENTRY RKNTSP #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain precursor - common tobacco ORGANISM #formal_name Nicotiana tabacum #common_name common tobacco DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 18-Jun-1999 ACCESSIONS A22934; A27292; A01086; A44957; A12152 REFERENCE A22934 !$#authors Mazur, B.J.; Chui, C.F. !$#journal Nucleic Acids Res. (1985) 13:2373-2386 !$#title Sequence of a genomic DNA clone for the small subunit of !1ribulose bisphosphate carboxylase-oxygenase from tobacco. !$#cross-references MUID:85215620; PMID:4000958 !$#accession A22934 !'##molecule_type DNA !'##residues 1-180 ##label MAZ !'##cross-references GB:X02353; NID:g20023; PIDN:CAA26208.1; PID:g20024 !'##note clone NtSS23 REFERENCE A27292 !$#authors O'Neal, J.K.; Pokalsky, A.R.; Kiehne, K.L.; Shewmaker, C.K. !$#journal Nucleic Acids Res. (1987) 15:8661-8677 !$#title Isolation of tobacco SSU genes: characterization of a !1transcriptionally active pseudogene. !$#cross-references MUID:88067689; PMID:3684569 !$#accession A27292 !'##molecule_type DNA !'##residues 1-101 ##label ONE !'##cross-references GB:M32419; NID:g170327; PIDN:AAA34116.1; !1PID:g170328 !'##note clone TSSU3-8 REFERENCE A01086 !$#authors Muller, K.D.; Salnikow, J.; Vater, J. !$#journal Biochim. Biophys. Acta (1983) 742:78-83 !$#title Amino acid sequence of the small subunit of !1D-ribulosebisphosphate carboxylase/oxygenase from Nicotiana !1tabacum. !$#accession A01086 !'##molecule_type protein !'##residues 58-84,'L',86,'PD',89-92,'D',94-144,'G',146-152,'E',154-180 !1##label MUL REFERENCE A44957 !$#authors Takeda, S.; Sato, F.; Ida, K.; Yamada, Y. !$#journal Plant Cell Physiol. (1990) 31:215-221 !$#title Characterization of polypeptides that accumulate in cultured !1Nicotiana tabacum cells. !$#accession A44957 !'##molecule_type protein !'##residues 'X',59-86 ##label TAK !'##experimental_source cv. Samsun NN REFERENCE A12152 !$#authors Gibbons, G.C.; Strobaek, S.; Haslett, B.; Boulter, D. !$#journal Experientia (1975) 15:1040-1041 !$#title The N-terminal amino acid sequence of the small subunit of !1ribulose-1,5-diphosphate carboxylase from Nicotiana tabacum. !$#accession A12152 !'##molecule_type protein !'##residues 58-63,'Y',65-78 ##label GIB !'##note 64-Ile was also found COMMENT Ribulose-bisphosphate carboxylase, a major component of leaf !1protein, is also a monooxygenase; it catalyzes the !1carboxylation of D-ribulose 1,5-bisphosphate (the primary !1event in photosynthetic carbon dioxide fixation) as well as !1the oxidative fragmentation of the pentose substrate in the !1photorespiration process. Both reactions occur !1simultaneously and in competition at the same active site. COMMENT Each active molecule contains eight large chains, !1synthesized on the chloroplast ribosomes and containing the !1active site, and eight small chains, the precursors of which !1are synthesized on cytoplasmic ribosomes and converted to !1mature small chains during or immediately after transport !1into the chloroplast. GENETICS !$#introns 59/3; 104/3; 122/2 !$#note there are multiple copies of this gene CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; monooxygenase; photorespiration FEATURE !$1-57 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$58-180 #product ribulose-bisphosphate carboxylase small !8chain #status experimental #label MAT SUMMARY #length 180 #molecular-weight 20311 #checksum 3372 SEQUENCE /// ENTRY RKQHS #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain precursor - white campion ORGANISM #formal_name Silene pratensis, Lychnis alba #common_name white campion, evening lychnis DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 18-Jun-1999 ACCESSIONS B30836 REFERENCE A93764 !$#authors Smeekens, S.; van Oosten, J.; de Groot, M.; Weisbeek, P. !$#journal Plant Mol. Biol. (1986) 7:433-440 !$#title Silene cDNA clones for a divergent chlorophyll-a/b-binding !1protein and a small subunit of ribulosebisphosphate !1carboxylase. !$#accession B30836 !'##molecule_type mRNA !'##residues 1-177 ##label SME !'##cross-references GB:M16888; NID:g169891; PIDN:AAB39037.1; !1PID:g169892 !'##note the authors translated the codon ACC for residue 49 as Ser COMMENT Ribulose-bisphosphate carboxylase, a major component of leaf !1protein, is also a monooxygenase; it catalyzes the !1carboxylation of D-ribulose 1,5-bisphosphate (the primary !1event in photosynthetic carbon dioxide fixation) as well as !1the oxidative fragmentation of the pentose substrate in the !1photorespiration process. These reactions occur !1simultaneously and in competition at the same active site. COMMENT Each active molecule contains eight large chains, !1synthesized on the chloroplast ribosomes and containing the !1active site, and eight small chains, the precursors of which !1are synthesized on cytoplasmic ribosomes and converted to !1mature small chains during or immediately after transport !1into the chloroplast. COMMENT This protein is coded by one member of a small multigene !1family. CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carbon-oxygen lyase; carboxy-lyase; chloroplast; !1monooxygenase; photorespiration FEATURE !$1-56 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$57-177 #product ribulose-bisphosphate carboxylase small !8chain #status predicted #label MAT SUMMARY #length 177 #molecular-weight 19697 #checksum 1231 SEQUENCE /// ENTRY RKRVS #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain precursor - radish ORGANISM #formal_name Raphanus sativus #common_name radish DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 18-Jun-1999 ACCESSIONS S00839 REFERENCE S00839 !$#authors Guidet, F.; Fourcroy, P. !$#journal Nucleic Acids Res. (1988) 16:2336 !$#title Nucleotide sequence of a radish ribulose 1,5 bisphosphate !1carboxylase small subunit (rbcS) cDNA. !$#cross-references MUID:88189826; PMID:3357781 !$#accession S00839 !'##molecule_type mRNA !'##residues 1-181 ##label GUI !'##cross-references EMBL:X06558; NID:g21378; PIDN:CAA29801.1; !1PID:g755803 GENETICS !$#gene rbcS CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; monooxygenase; photorespiration FEATURE !$1-55 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$56-181 #product ribulose-bisphosphate carboxylase small !8chain #status predicted #label MAT SUMMARY #length 181 #molecular-weight 20324 #checksum 3312 SEQUENCE /// ENTRY RKMUB3 #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain B3 precursor - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 18-Jun-1999 ACCESSIONS S03719 REFERENCE S03717 !$#authors Krebbers, E.; Seurinck, J.; Herdies, L.; Cashmore, A.R.; !1Timko, M.P. !$#journal Plant Mol. Biol. (1988) 11:745-759 !$#title Four genes in two diverged subfamilies encode the !1ribulose-1,5-bisphosphate carboxylase small subunit !1polypeptides of Arabidopsis thaliana. !$#accession S03719 !'##molecule_type DNA !'##residues 1-181 ##label KRE !'##cross-references GB:X14564; EMBL:X13610; NID:g16192; !1PIDN:CAA32702.1; PID:g16195 GENETICS !$#gene ats3B; rbcS !$#introns 57/3; 102/3 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; photorespiration FEATURE !$1-55 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$56-181 #product ribulose-bisphosphate carboxylase small !8chain B3 #status predicted #label MAT SUMMARY #length 181 #molecular-weight 20314 #checksum 2826 SEQUENCE /// ENTRY RKMUB2 #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain B2 precursor - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 18-Jun-1999 ACCESSIONS S03718 REFERENCE S03717 !$#authors Krebbers, E.; Seurinck, J.; Herdies, L.; Cashmore, A.R.; !1Timko, M.P. !$#journal Plant Mol. Biol. (1988) 11:745-759 !$#title Four genes in two diverged subfamilies encode the !1ribulose-1,5-bisphosphate carboxylase small subunit !1polypeptides of Arabidopsis thaliana. !$#accession S03718 !'##molecule_type DNA !'##residues 1-181 ##label KRE !'##cross-references GB:X14564; EMBL:X13610; NID:g16192; !1PIDN:CAA32701.1; PID:g16194 GENETICS !$#gene ats2B; rbcS !$#introns 57/3; 102/3 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; photorespiration FEATURE !$1-55 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$56-181 #product ribulose-bisphosphate carboxylase small !8chain B2 #status predicted #label MAT SUMMARY #length 181 #molecular-weight 20316 #checksum 2955 SEQUENCE /// ENTRY RKMUB1 #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain B1 precursor - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 18-Jun-1999 ACCESSIONS S03717 REFERENCE S03717 !$#authors Krebbers, E.; Seurinck, J.; Herdies, L.; Cashmore, A.R.; !1Timko, M.P. !$#journal Plant Mol. Biol. (1988) 11:745-759 !$#title Four genes in two diverged subfamilies encode the !1ribulose-1,5-bisphosphate carboxylase small subunit !1polypeptides of Arabidopsis thaliana. !$#accession S03717 !'##molecule_type DNA !'##residues 1-181 ##label KRE !'##cross-references GB:X14564; EMBL:X13610; NID:g16192; !1PIDN:CAA32700.1; PID:g16193 GENETICS !$#gene ats1B; rbcS !$#introns 57/3; 102/3 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; photorespiration FEATURE !$1-55 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$56-181 #product ribulose-bisphosphate carboxylase small !8chain B1 #status predicted #label MAT SUMMARY #length 181 #molecular-weight 20286 #checksum 2795 SEQUENCE /// ENTRY RKMUA1 #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain A1 precursor - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 30-Jun-1993 ACCESSIONS S03720 REFERENCE S03717 !$#authors Krebbers, E.; Seurinck, J.; Herdies, L.; Cashmore, A.R.; !1Timko, M.P. !$#journal Plant Mol. Biol. (1988) 11:745-759 !$#title Four genes in two diverged subfamilies encode the !1ribulose-1,5-bisphosphate carboxylase small subunit !1polypeptides of Arabidopsis thaliana. !$#accession S03720 !'##molecule_type DNA !'##residues 1-180 ##label KRE !'##cross-references EMBL:X13611 GENETICS !$#gene ats1A; rbcS !$#introns 57/3; 102/3 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; photorespiration FEATURE !$1-55 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$56-180 #product ribulose-bisphosphate carboxylase small !8chain A1 #status predicted #label MAT SUMMARY #length 180 #molecular-weight 20202 #checksum 1409 SEQUENCE /// ENTRY RKRPS #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain precursor - rape ORGANISM #formal_name Brassica napus #common_name rape DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 18-Jun-1999 ACCESSIONS S00934 REFERENCE S00934 !$#authors Baszczynski, C.L.; Fallis, L.; Bellemare, G. !$#journal Nucleic Acids Res. (1988) 16:4732 !$#title Nucleotide sequence of a full length cDNA clone of a !1Brassica napus ribulose bisphosphate carboxylase-oxygenase !1small subunit gene. !$#cross-references MUID:88247783; PMID:3380701 !$#accession S00934 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-181 ##label BAS !'##cross-references EMBL:X07367; NID:g17854; PIDN:CAA30290.1; !1PID:g17855 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; monooxygenase; photorespiration FEATURE !$1-55 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$56-181 #product ribulose-bisphosphate carboxylase small !8chain #status predicted #label MAT SUMMARY #length 181 #molecular-weight 20314 #checksum 4995 SEQUENCE /// ENTRY RKRPF1 #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain precursor (gene rbcSF1) - rape ORGANISM #formal_name Brassica napus #common_name rape DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 18-Jun-1999 ACCESSIONS S16253 REFERENCE S16253 !$#authors Nantel, A.M.; Lafleur, F.; Boivin, R.; Baszczynski, C.L.; !1Bellemare, G. !$#journal Plant Mol. Biol. (1991) 16:955-966 !$#title Promoter for a Brassica napus ribulose bisphosphate !1carboxylase/oxygenase small subunit gene binds multiple !1nuclear factors and contains a negative-strand open reading !1frame encoding a putative transmembrane protein. !$#cross-references MUID:91322510; PMID:1863768 !$#accession S16253 !'##molecule_type DNA !'##residues 1-181 ##label NAN !'##cross-references EMBL:X55937; NID:g17851; PIDN:CAA39402.1; !1PID:g17852 GENETICS !$#gene rbcSF1 !$#introns 57/3; 102/3 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; heterohexadecamer; !1photorespiration FEATURE !$1-55 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$56-181 #product ribulose-bisphosphate carboxylase small !8chain #status predicted #label MAT SUMMARY #length 181 #molecular-weight 20183 #checksum 2480 SEQUENCE /// ENTRY RKCNSU #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain precursor - upland cotton ORGANISM #formal_name Gossypium hirsutum #common_name upland cotton DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 18-Jun-1999 ACCESSIONS S18344; S19089 REFERENCE S18344 !$#authors Sagliocco, F.; Kapazoglou, A.; Dure III, L. !$#journal Plant Mol. Biol. (1991) 17:1275-1276 !$#title Sequence of an rbcS gene from cotton. !$#cross-references MUID:92032796; PMID:1932702 !$#accession S18344 !'##molecule_type DNA !'##residues 1-182 ##label SAG !'##cross-references EMBL:X54091; NID:g450504; PIDN:CAA38026.1; !1PID:g450505 !'##note 66-Thr, 98-Val and 148-Glu were also found REFERENCE S19089 !$#authors Dure, L. !$#submission submitted to the EMBL Data Library, July 1990 !$#accession S19089 !'##molecule_type DNA !'##residues 1-94,'KG',97-182 ##label DUR !'##cross-references EMBL:X54091 GENETICS !$#gene rbcS !$#introns 61/3; 106/3 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; heterohexadecamer; !1photorespiration FEATURE !$1-59 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$60-182 #product ribulose-bisphosphate carboxylase small !8chain #status predicted #label MAT SUMMARY #length 182 #molecular-weight 20535 #checksum 3385 SEQUENCE /// ENTRY RKFPST #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain precursor - Flaveria trinervia ORGANISM #formal_name Flaveria trinervia DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 18-Jun-1999 ACCESSIONS S07378; B34921 REFERENCE S07378 !$#authors Adams, C.A.; Babcock, M.; Leung, F.; Sun, S.M. !$#journal Nucleic Acids Res. (1987) 15:1875 !$#title Sequence of a ribulose 1,5-bisphosphate carboxylase/ !1oxygenase cDNA from the C4 dicot Flaveria trinervia. !$#cross-references MUID:87146504; PMID:3822845 !$#accession S07378 !'##molecule_type mRNA !'##residues 1-173 ##label ADA !'##cross-references EMBL:X05037; NID:g18465; PIDN:CAA28711.1; !1PID:g18466 REFERENCE A34921 !$#authors Hudson, G.S.; Mahon, J.D.; Anderson, P.A.; Gibbs, M.J.; !1Badger, M.R.; Andrews, T.J.; Whitfeld, P.R. !$#journal J. Biol. Chem. (1990) 265:808-814 !$#title Comparisons of rbcL genes for the large subunit of !1ribulose-bisphosphate carboxylase from closely related C-3 !1and C-4 plant species. !$#cross-references MUID:90110139; PMID:2295620 !$#accession B34921 !'##molecule_type protein !'##residues 51-75 ##label HUD CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; monooxygenase; photorespiration FEATURE !$1-50 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$51-173 #product ribulose-bisphosphate carboxylase small !8chain #status experimental #label MAT SUMMARY #length 173 #molecular-weight 19546 #checksum 2641 SEQUENCE /// ENTRY RKKVS #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain precursor - cucumber ORGANISM #formal_name Cucumis sativus #common_name cucumber DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 18-Jun-1999 ACCESSIONS S07410 REFERENCE S07410 !$#authors Greenland, A.J.; Thomas, M.V.; Walden, R.M. !$#journal Planta (1987) 170:99-110 !$#title Expression of two nuclear genes encoding chloroplast !1proteins during early development of cucumber seedlings. !$#accession S07410 !'##molecule_type mRNA !'##residues 1-189 ##label GRE !'##cross-references EMBL:M16056; NID:g167541; PIDN:AAA33131.1; !1PID:g167542 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; monooxygenase; photorespiration FEATURE !$1-59 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$60-189 #product ribulose-bisphosphate carboxylase small !8chain #status predicted #label MAT SUMMARY #length 189 #molecular-weight 21063 #checksum 2265 SEQUENCE /// ENTRY RKNTSS #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain precursor - wood tobacco ORGANISM #formal_name Nicotiana sylvestris #common_name wood tobacco DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 18-Jun-1999 ACCESSIONS A01085 REFERENCE A01085 !$#authors Pinck, M.; Guilley, E.; Durr, A.; Hoff, M.; Pinck, L.; !1Fleck, J. !$#journal Biochimie (1984) 66:539-545 !$#title Complete sequence of one of the mRNAs coding for the small !1subunit of ribulose bisphosphate carboxylase of Nicotiana !1sylvestris. !$#cross-references MUID:85150283; PMID:6549380 !$#accession A01085 !'##molecule_type mRNA !'##residues 1-180 ##label PIN !'##cross-references GB:X01722; NID:g19759; PIDN:CAA25862.1; PID:g19760 COMMENT Ribulose-bisphosphate carboxylase, a major component of leaf !1protein, is also a monooxygenase; it catalyzes the !1carboxylation of D-ribulose 1,5-bisphosphate (the primary !1event in photosynthetic carbon dioxide fixation) as well as !1the oxidative fragmentation of the pentose substrate in the !1photorespiration process. These reactions occur !1simultaneously and in competition at the same active site. COMMENT Each active molecule contains eight large chains, !1synthesized on the chloroplast ribosomes and containing the !1active site, and eight small chains, the precursors of which !1are synthesized on cytoplasmic ribosomes and converted to !1mature small chains during or immediately after transport !1into the chloroplast. COMMENT This protein is coded by one member of a small multigene !1family. CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; monooxygenase; photorespiration; !1photosynthesis FEATURE !$1-57 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$58-180 #product ribulose-bisphosphate carboxylase small !8chain #status predicted #label MAT SUMMARY #length 180 #molecular-weight 20311 #checksum 3372 SEQUENCE /// ENTRY RKNT41 #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain SS41 precursor - wood tobacco ORGANISM #formal_name Nicotiana sylvestris #common_name wood tobacco DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 18-Jun-1999 ACCESSIONS S10987 REFERENCE S10987 !$#authors Jamet, E.; Fargeas, C.; Durr, A.; Fleck, J. !$#journal Nucleic Acids Res. (1990) 18:4589 !$#title Nucleotide sequences of two genes encoding the small subunit !1of RUBISCO in Nicotiana sylvestris. !$#cross-references MUID:90356397; PMID:2388836 !$#accession S10987 !'##molecule_type DNA !'##residues 1-181 ##label JAM !'##cross-references EMBL:X53426; NID:g19763; PIDN:CAA37516.1; !1PID:g295823 GENETICS !$#introns 60/3; 105/3 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; monooxygenase; photorespiration FEATURE !$1-58 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$59-181 #product ribulose-bisphosphate carboxylase small !8chain #status predicted #label MAT SUMMARY #length 181 #molecular-weight 20474 #checksum 3832 SEQUENCE /// ENTRY RKTO3B #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain 3B precursor - tomato ORGANISM #formal_name Lycopersicon esculentum #common_name tomato DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 18-Jun-1999 ACCESSIONS S01107 REFERENCE S01107 !$#authors Sugita, M.; Manzara, T.; Pichersky, E.; Cashmore, A.; !1Gruissem, W. !$#journal Mol. Gen. Genet. (1987) 209:247-256 !$#title Genomic organization, sequence analysis and expression of !1all five genes encoding the small subunit of ribulose-1, !15-bisphosphate carboxylase/oxygenase from tomato. !$#cross-references MUID:88038372; PMID:3478552 !$#accession S01107 !'##molecule_type DNA !'##residues 1-180 ##label SUG !'##cross-references EMBL:X05985; NID:g19335; PIDN:CAA29403.1; !1PID:g19336 GENETICS !$#gene rbcS-3B !$#map_position 2 !$#introns 59/3; 104/3 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; monooxygenase; photorespiration FEATURE !$1-57 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$58-180 #product ribulose-bisphosphate carboxylase small !8chain 3B #status predicted #label MAT SUMMARY #length 180 #molecular-weight 20213 #checksum 3668 SEQUENCE /// ENTRY RKTO3C #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain 3A precursor - tomato ALTERNATE_NAMES ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain 3C precursor ORGANISM #formal_name Lycopersicon esculentum #common_name tomato DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 23-Mar-2001 ACCESSIONS S01109; S01108; C24885; D24885; S21582 REFERENCE S01107 !$#authors Sugita, M.; Manzara, T.; Pichersky, E.; Cashmore, A.; !1Gruissem, W. !$#journal Mol. Gen. Genet. (1987) 209:247-256 !$#title Genomic organization, sequence analysis and expression of !1all five genes encoding the small subunit of ribulose-1, !15-bisphosphate carboxylase/oxygenase from tomato. !$#cross-references MUID:88038372; PMID:3478552 !$#accession S01109 !'##molecule_type DNA !'##residues 1-180 ##label SUG1 !'##cross-references EMBL:X05986; NID:g19337; PIDN:CAA29404.1; !1PID:g19338 !'##genetics RS3A !$#accession S01108 !'##molecule_type DNA !'##residues 1-180 ##label SUG2 !'##cross-references EMBL:X05984; NID:g19333; PIDN:CAA29402.1; !1PID:g19334 !'##genetics RS3C REFERENCE A24885 !$#authors Pichersky, E.; Bernatzky, R.; Tanksley, S.D.; Cashmore, A.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:3880-3884 !$#title Evidence for selection as a mechanism in the concerted !1evolution of Lycopersicon esculentum (tomato) genes encoding !1the small subunit of ribulose-1,5-bisphosphate carboxylase/ !1oxygenase. !$#cross-references MUID:86233336; PMID:3012537 !$#accession C24885 !'##molecule_type DNA !'##residues 1-180 ##label PIC !'##cross-references EMBL:M13544; NID:g170499; PIDN:AAA34190.1; !1PID:g170500 !$#accession D24885 !'##molecule_type mRNA !'##residues 1-161 ##label PIC2 !'##note the authors translated the codon GTA for residue 5 as Ala REFERENCE S21582 !$#authors Manzara, T.; Carrasco, P.; Gruissem, W. !$#submission submitted to the EMBL Data Library, April 1992 !$#description Developmental and organ-specific changes in DNA-protein !1interactions in the tomato rbcS1, rbcS2 amd rbcS3A promoter !1regions. !$#accession S21582 !'##molecule_type DNA !'##residues 1-20 ##label MAN !'##cross-references EMBL:X66072; NID:g22626; PIDN:CAA46872.1; !1PID:g22627 !'##genetics RS3C GENETICS RS3A !$#gene rbcS-3A GENETICS RS3C !$#gene rbcS-3C !$#map_position 2 !$#introns 59/3; 104/3 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; monooxygenase; photorespiration FEATURE !$1-57 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$58-180 #product ribulose-bisphosphate carboxylase small !8chain 3A #status predicted #label MAT SUMMARY #length 180 #molecular-weight 20231 #checksum 3679 SEQUENCE /// ENTRY RKTOS2 #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain 2 precursor - tomato ORGANISM #formal_name Lycopersicon esculentum #common_name tomato DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 21-Jul-2000 ACCESSIONS S02363; B24885; B29037; T07157 REFERENCE S01107 !$#authors Sugita, M.; Manzara, T.; Pichersky, E.; Cashmore, A.; !1Gruissem, W. !$#journal Mol. Gen. Genet. (1987) 209:247-256 !$#title Genomic organization, sequence analysis and expression of !1all five genes encoding the small subunit of ribulose-1, !15-bisphosphate carboxylase/oxygenase from tomato. !$#cross-references MUID:88038372; PMID:3478552 !$#accession S02363 !'##molecule_type DNA !'##residues 1-180 ##label SUG !'##cross-references EMBL:X05983; NID:g19331; PIDN:CAA29401.2; !1PID:g4456641 !'##note the authors translated the codon TCA for residue 32 as Thr and !1ACT for residue 34 as Ser REFERENCE A24885 !$#authors Pichersky, E.; Bernatzky, R.; Tanksley, S.D.; Cashmore, A.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:3880-3884 !$#title Evidence for selection as a mechanism in the concerted !1evolution of Lycopersicon esculentum (tomato) genes encoding !1the small subunit of ribulose-1,5-bisphosphate carboxylase/ !1oxygenase. !$#cross-references MUID:86233336; PMID:3012537 !$#accession B24885 !'##molecule_type mRNA !'##residues 1-180 ##label PIC !'##cross-references EMBL:M13543; NID:g170497; PIDN:AAA34189.1; !1PID:g170498 !'##note the authors translated the codon GTC for residue 5 as Ala REFERENCE A29037 !$#authors McKnight, T.D.; Alexander, D.C.; Babcock, M.S.; Simpson, !1R.B. !$#journal Gene (1986) 48:23-32 !$#title Nucleotide sequence and molecular evolution of two tomato !1genes encoding the small subunit of ribulose-1, !15-bisphosphate carboxylase. !$#cross-references MUID:87163513; PMID:3557127 !$#accession B29037 !'##molecule_type mRNA !'##residues 1-86,'V',88-180 ##label MCK !'##cross-references EMBL:M15236; NID:g170503; PIDN:AAA34192.1; !1PID:g170504 REFERENCE Z15964 !$#authors Manzara, T. !$#submission submitted to the EMBL Data Library, August 1989 !$#accession T07157 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-180 ##label MAN !'##cross-references EMBL:X05983; NID:g19331; PIDN:CAA29401.2 !'##experimental_source cultivar VFNT LA1221 cherry line GENETICS !$#gene rbcS-2 !$#map_position 3 !$#introns 59/3; 104/3; 122/2 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; monooxygenase; photorespiration FEATURE !$1-57 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$58-180 #product ribulose-bisphosphate carboxylase small !8chain 2 #status predicted #label MAT SUMMARY #length 180 #molecular-weight 20278 #checksum 4535 SEQUENCE /// ENTRY RKTOS1 #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain 1 precursor - tomato ORGANISM #formal_name Lycopersicon esculentum #common_name tomato DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 18-Jun-1999 ACCESSIONS S02364; A24885; A29037; S21583 REFERENCE S01107 !$#authors Sugita, M.; Manzara, T.; Pichersky, E.; Cashmore, A.; !1Gruissem, W. !$#journal Mol. Gen. Genet. (1987) 209:247-256 !$#title Genomic organization, sequence analysis and expression of !1all five genes encoding the small subunit of ribulose-1, !15-bisphosphate carboxylase/oxygenase from tomato. !$#cross-references MUID:88038372; PMID:3478552 !$#accession S02364 !'##molecule_type DNA !'##residues 1-181 ##label SUG !'##cross-references EMBL:X05982; NID:g19326; PIDN:CAA29400.1; !1PID:g295814 !'##note the authors translated the codon CTT for residue 49 as Ile REFERENCE A24885 !$#authors Pichersky, E.; Bernatzky, R.; Tanksley, S.D.; Cashmore, A.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:3880-3884 !$#title Evidence for selection as a mechanism in the concerted !1evolution of Lycopersicon esculentum (tomato) genes encoding !1the small subunit of ribulose-1,5-bisphosphate carboxylase/ !1oxygenase. !$#cross-references MUID:86233336; PMID:3012537 !$#accession A24885 !'##molecule_type DNA !'##residues 1-181 ##label PIC !'##cross-references EMBL:M13542; NID:g170495; PIDN:AAA34188.1; !1PID:g170496 REFERENCE A29037 !$#authors McKnight, T.D.; Alexander, D.C.; Babcock, M.S.; Simpson, !1R.B. !$#journal Gene (1986) 48:23-32 !$#title Nucleotide sequence and molecular evolution of two tomato !1genes encoding the small subunit of ribulose-1, !15-bisphosphate carboxylase. !$#cross-references MUID:87163513; PMID:3557127 !$#accession A29037 !'##molecule_type mRNA !'##residues 1-181 ##label MCK !'##cross-references EMBL:M15235 REFERENCE S21582 !$#authors Manzara, T.; Carrasco, P.; Gruissem, W. !$#submission submitted to the EMBL Data Library, April 1992 !$#description Developmental and organ-specific changes in DNA-protein !1interactions in the tomato rbcS1, rbcS2 amd rbcS3A promoter !1regions. !$#accession S21583 !'##molecule_type DNA !'##residues 1-20 ##label MAN !'##cross-references EMBL:X66068; NID:g22621; PIDN:CAA46868.1; !1PID:g22622 GENETICS !$#gene rbcS-1 !$#map_position 2 !$#introns 60/3; 105/3 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; monooxygenase; photorespiration FEATURE !$1-58 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$59-181 #product ribulose-bisphosphate carboxylase small !8chain 1 #status predicted #label MAT SUMMARY #length 181 #molecular-weight 20307 #checksum 5240 SEQUENCE /// ENTRY RKPOSC #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) precursor small chain rbcS-c - potato ORGANISM #formal_name Solanum tuberosum #common_name potato DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 18-Jun-1999 ACCESSIONS A31083 REFERENCE A31083 !$#authors Wolter, F.P.; Fritz, C.C.; Willmitzer, L.; Schell, J.; !1Schreier, P.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:846-850 !$#title rbcS genes in Solanum tuberosum: conservation of transit !1peptide and exon shuffling during evolution. !$#cross-references MUID:88124937; PMID:3422467 !$#accession A31083 !'##molecule_type mRNA !'##residues 1-181 ##label WOL !'##cross-references GB:J03613; NID:g169556; PIDN:AAA33838.1; !1PID:g169557 !'##experimental_source strain HH1201/7 COMMENT Ribulose-bisphosphate carboxylase, a major component of leaf !1protein, is also a monooxygenase; it catalyzes the !1carboxylation of D-ribulose 1,5-bisphosphate (the primary !1event in photosynthetic carbon dioxide fixation) as well as !1the oxidative fragmentation of the pentose substrate in the !1photorespiration process. These reactions occur !1simultaneously and in competition at the same active site. COMMENT Each active molecule contains eight large chains, !1synthesized on the chloroplast ribosomes and containing the !1active site, and eight small chains, the precursors of which !1are synthesized on cytoplasmic ribosomes and converted to !1mature small chains during or immediately after transport !1into the chloroplast. COMMENT This protein is coded by one member of a small multigene !1family. GENETICS !$#gene rbcS-c CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carbon-oxygen lyase; carboxy-lyase; chloroplast; !1monooxygenase; photorespiration FEATURE !$1-57 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$58-181 #product ribulose-bisphosphate carboxylase small !8chain rbcS-c #status predicted #label MAT SUMMARY #length 181 #molecular-weight 20368 #checksum 4699 SEQUENCE /// ENTRY RKPOS1 #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) precursor small chain rbcS-1 - potato ORGANISM #formal_name Solanum tuberosum #common_name potato DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 23-Mar-2001 ACCESSIONS B31083; S31497 REFERENCE A31083 !$#authors Wolter, F.P.; Fritz, C.C.; Willmitzer, L.; Schell, J.; !1Schreier, P.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:846-850 !$#title rbcS genes in Solanum tuberosum: conservation of transit !1peptide and exon shuffling during evolution. !$#cross-references MUID:88124937; PMID:3422467 !$#accession B31083 !'##molecule_type DNA !'##residues 1-181 ##label WOL REFERENCE S31494 !$#authors Fritz, C.C.; Wolter, F.P.; Schenkemeyer, V.; Herget, T.; !1Schreier, P.H. !$#submission submitted to the EMBL Data Library, December 1992 !$#description The gene-family of ribulose-(1,5) bisphosphate carboxylase/ !1oxygenase small subunit from Potato. !$#accession S31497 !'##status preliminary !'##molecule_type DNA !'##residues 1-181 ##label FRI !'##cross-references EMBL:X69759; NID:g21562; PIDN:CAA49413.1; !1PID:g21563 GENETICS !$#gene rbcS-1 !$#introns 59/3; 102/3 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carbon-oxygen lyase; carboxy-lyase; chloroplast; !1monooxygenase; photorespiration FEATURE !$1-57 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$58-181 #product ribulose-bisphosphate carboxylase small !8chain rbcS-1 #status predicted #label MAT SUMMARY #length 181 #molecular-weight 20556 #checksum 4863 SEQUENCE /// ENTRY RKPOS2 #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) precursor small chain rbcS-2a - potato ORGANISM #formal_name Solanum tuberosum #common_name potato DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 23-Mar-2001 ACCESSIONS C31083; S31495 REFERENCE A31083 !$#authors Wolter, F.P.; Fritz, C.C.; Willmitzer, L.; Schell, J.; !1Schreier, P.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:846-850 !$#title rbcS genes in Solanum tuberosum: conservation of transit !1peptide and exon shuffling during evolution. !$#cross-references MUID:88124937; PMID:3422467 !$#accession C31083 !'##molecule_type DNA !'##residues 1-180 ##label WOL REFERENCE S31494 !$#authors Fritz, C.C.; Wolter, F.P.; Schenkemeyer, V.; Herget, T.; !1Schreier, P.H. !$#submission submitted to the EMBL Data Library, December 1992 !$#description The gene-family of ribulose-(1,5) bisphosphate carboxylase/ !1oxygenase small subunit from Potato. !$#accession S31495 !'##status preliminary !'##molecule_type DNA !'##residues 1-180 ##label FRI !'##cross-references EMBL:X69760; NID:g21564; PIDN:CAA49414.1; !1PID:g21565 GENETICS !$#gene rbcS-2a !$#introns 59/3; 102/3 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carbon-oxygen lyase; carboxy-lyase; chloroplast; !1monooxygenase; photorespiration FEATURE !$1-57 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$58-180 #product ribulose-bisphosphate carboxylase small !8chain rbcS-2a #status predicted #label MAT SUMMARY #length 180 #molecular-weight 20289 #checksum 2599 SEQUENCE /// ENTRY RKPO2B #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) precursor small chain rbcS-2b - potato ORGANISM #formal_name Solanum tuberosum #common_name potato DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 23-Mar-2001 ACCESSIONS D31083; S31496 REFERENCE A31083 !$#authors Wolter, F.P.; Fritz, C.C.; Willmitzer, L.; Schell, J.; !1Schreier, P.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:846-850 !$#title rbcS genes in Solanum tuberosum: conservation of transit !1peptide and exon shuffling during evolution. !$#cross-references MUID:88124937; PMID:3422467 !$#accession D31083 !'##molecule_type DNA !'##residues 1-180 ##label WOL REFERENCE S31494 !$#authors Fritz, C.C.; Wolter, F.P.; Schenkemeyer, V.; Herget, T.; !1Schreier, P.H. !$#submission submitted to the EMBL Data Library, December 1992 !$#description The gene-family of ribulose-(1,5) bisphosphate carboxylase/ !1oxygenase small subunit from Potato. !$#accession S31496 !'##status preliminary !'##molecule_type DNA !'##residues 1-180 ##label FRI !'##cross-references EMBL:X69761; NID:g21566; PIDN:CAA49415.1; !1PID:g21567 GENETICS !$#gene rbcS-2b !$#introns 59/3; 102/3 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carbon-oxygen lyase; carboxy-lyase; chloroplast; !1monooxygenase; photorespiration FEATURE !$1-57 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$58-180 #product ribulose-bisphosphate carboxylase small !8chain rbcS-2b #status predicted #label MAT SUMMARY #length 180 #molecular-weight 20301 #checksum 3250 SEQUENCE /// ENTRY RKPO2C #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) precursor small chain rbcS-2c - potato ORGANISM #formal_name Solanum tuberosum #common_name potato DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 23-Mar-2001 ACCESSIONS E31083; S31494 REFERENCE A31083 !$#authors Wolter, F.P.; Fritz, C.C.; Willmitzer, L.; Schell, J.; !1Schreier, P.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:846-850 !$#title rbcS genes in Solanum tuberosum: conservation of transit !1peptide and exon shuffling during evolution. !$#cross-references MUID:88124937; PMID:3422467 !$#accession E31083 !'##molecule_type DNA !'##residues 1-180 ##label WOL REFERENCE S31494 !$#authors Fritz, C.C.; Wolter, F.P.; Schenkemeyer, V.; Herget, T.; !1Schreier, P.H. !$#submission submitted to the EMBL Data Library, December 1992 !$#description The gene-family of ribulose-(1,5) bisphosphate carboxylase/ !1oxygenase small subunit from Potato. !$#accession S31494 !'##status preliminary !'##molecule_type DNA !'##residues 1-180 ##label FRI !'##cross-references EMBL:X69762; NID:g21568; PIDN:CAA49416.1; !1PID:g21569 GENETICS !$#gene rbcS-2c !$#introns 59/3; 102/3 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carbon-oxygen lyase; carboxy-lyase; chloroplast; !1monooxygenase; photorespiration FEATURE !$1-57 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$58-180 #product ribulose-bisphosphate carboxylase small !8chain rbcS-2c #status predicted #label MAT SUMMARY #length 180 #molecular-weight 20319 #checksum 3207 SEQUENCE /// ENTRY RKPMS #type fragment TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain precursor (clone pSSU1) - garden pea (fragment) ORGANISM #formal_name Pisum sativum #common_name garden pea DATE 31-Dec-1980 #sequence_revision 31-Dec-1980 #text_change 12-Apr-1996 ACCESSIONS A01087 REFERENCE A01087 !$#authors Bedbrook, J.R.; Smith, S.M.; Ellis, R.J. !$#journal Nature (1980) 287:692-697 !$#title Molecular cloning and sequencing of cDNA encoding the !1precursor to the small subunit of chloroplast ribulose-1, !15-bisphosphate carboxylase. !$#accession A01087 !'##molecule_type mRNA !'##residues 1-136 ##label BED !'##note the authors translated the codon GTT for residue 100 as Leu CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; monooxygenase; photorespiration FEATURE !$1-13 #domain transit peptide (chloroplast) (fragment) !8#status predicted #label TNP\ !$14-136 #product ribulose-bisphosphate carboxylase small !8chain #status predicted #label MAT SUMMARY #length 136 #checksum 5431 SEQUENCE /// ENTRY RKPMS5 #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain 3C precursor - garden pea ORGANISM #formal_name Pisum sativum #common_name garden pea DATE 15-Nov-1984 #sequence_revision 25-Feb-1985 #text_change 18-Jun-1999 ACCESSIONS A01088; A92406; B24890 REFERENCE A90987 !$#authors Coruzzi, G.; Broglie, R.; Edwards, C.; Chua, N.H. !$#journal EMBO J. (1984) 3:1671-1679 !$#title Tissue-specific and light-regulated expression of a pea !1nuclear gene encoding the small subunit of ribulose-1, !15-bisphosphate carboxylase. !$#cross-references MUID:85003579; PMID:6479146 !$#accession A01088 !'##molecule_type DNA !'##residues 1-180 ##label COR1 !'##cross-references GB:X00806; NID:g20858; PIDN:CAA25390.1; PID:g20859 !'##experimental_source cv. Progress No. 9, pPS-2.4 REFERENCE A92406 !$#authors Coruzzi, G.; Broglie, R.; Cashmore, A.; Chua, N.H. !$#journal J. Biol. Chem. (1983) 258:1399-1402 !$#title Nucleotide sequences of two pea cDNA clones encoding the !1small subunit of ribulose 1,5-bisphosphate carboxylase and !1the major chlorophyll a/b-binding thylakoid polypeptide. !$#cross-references MUID:83108917; PMID:6296093 !$#accession A92406 !'##molecule_type mRNA !'##residues 25-180 ##label COR2 !'##experimental_source clone pSS15 !'##note this sequence has been revised in reference A90987 REFERENCE A91047 !$#authors Fluhr, R.; Moses, P.; Morelli, G.; Coruzzi, G.; Chua, N.H. !$#journal EMBO J. (1986) 5:2063-2071 !$#title Expression dynamics of the pea rbcS multigene family and !1organ distribution of the transcripts. !$#accession B24890 !'##molecule_type DNA !'##residues 1-180 ##label FLU !'##experimental_source cv. Progress No. 9, rbcS-3C COMMENT Ribulose-bisphosphate carboxylase, a major component of leaf !1protein, is also a monooxygenase; it catalyzes the !1carboxylation of D-ribulose 1,5-bisphosphate (the primary !1event in photosynthetic carbon dioxide fixation) as well as !1the oxidative fragmentation of the pentose substrate in the !1photorespiration process. These reactions occur !1simultaneously and in competition at the same active site. COMMENT Each active molecule contains eight large chains, !1synthesized on the chloroplast ribosomes and containing the !1active site, and eight small chains, the precursors of which !1are synthesized on cytoplasmic ribosomes and converted to !1mature small chains during or immediately after transport !1into the chloroplast. COMMENT This protein is coded by one member of a small multigene !1family. GENETICS !$#gene pPS-2.4; rbcS-3C !$#introns 59/3; 114/3 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; monooxygenase; photorespiration FEATURE !$1-57 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$58-180 #product ribulose-bisphosphate carboxylase small !8chain #status predicted #label MAT SUMMARY #length 180 #molecular-weight 20244 #checksum 4633 SEQUENCE /// ENTRY RKPMS3 #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain 3A precursor - garden pea ORGANISM #formal_name Pisum sativum #common_name garden pea DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 18-Jun-1999 ACCESSIONS A27874; A24890 REFERENCE A27874 !$#authors Anderson, S.; Smith, S.M. !$#journal Biochem. J. (1986) 240:709-715 !$#title Synthesis of the small subunit of ribulose-bisphosphate !1carboxylase from genes cloned into plasmids containing the !1SP6 promoter. !$#cross-references MUID:87156615; PMID:3827863 !$#accession A27874 !'##molecule_type DNA !'##residues 1-180 ##label AND !'##cross-references GB:M25613 REFERENCE A91047 !$#authors Fluhr, R.; Moses, P.; Morelli, G.; Coruzzi, G.; Chua, N.H. !$#journal EMBO J. (1986) 5:2063-2071 !$#title Expression dynamics of the pea rbcS multigene family and !1organ distribution of the transcripts. !$#accession A24890 !'##molecule_type DNA !'##residues 1-180 ##label FLU !'##cross-references GB:X04333; NID:g20854; PIDN:CAA27864.1; PID:g20855 !'##experimental_source cv. Progress No. 9, rbcS-3A GENETICS !$#gene rbcS; rbcS-3A !$#introns 59/3; 114/3 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carbon-oxygen lyase; carboxy-lyase; chloroplast; !1monooxygenase; photorespiration FEATURE !$1-57 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$58-180 #product ribulose-bisphosphate carboxylase small !8chain 3A #status predicted #label MAT SUMMARY #length 180 #molecular-weight 20231 #checksum 4954 SEQUENCE /// ENTRY RKJYS #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain precursor - white clover ORGANISM #formal_name Trifolium repens #common_name white clover DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 18-Jun-1999 ACCESSIONS S12704; S21328 REFERENCE S12704 !$#authors Ellison, N.W.; Yu, P.L.; White, D.W.R. !$#journal Nucleic Acids Res. (1990) 18:4914 !$#title Nucleotide sequence of a white clover ribulose bisphosphate !1carboxylase small subunit gene. !$#cross-references MUID:90370477; PMID:2395652 !$#accession S12704 !'##status translation not shown !'##molecule_type DNA !'##residues 1-178 ##label ELL !'##cross-references EMBL:X52293; NID:g21956; PIDN:CAA36542.1; !1PID:g295846 REFERENCE S21328 !$#authors Ellison, N.W. !$#submission submitted to the EMBL Data Library, July 1990 !$#accession S21328 !'##molecule_type mRNA !'##residues 104-178 ##label EL2 !'##cross-references EMBL:X53954; NID:g21960; PIDN:CAA37905.1; !1PID:g388253 GENETICS !$#gene rbcS !$#introns 57/3; 102/3 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carbon-oxygen lyase; carboxy-lyase; chloroplast; !1monooxygenase; photorespiration FEATURE !$1-57 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$58-178 #product ribulose-bisphosphate carboxylase small !8chain #status predicted #label MAT SUMMARY #length 178 #molecular-weight 20038 #checksum 3079 SEQUENCE /// ENTRY RKPJS1 #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain (ssu11A) precursor - garden petunia ORGANISM #formal_name Petunia x hybrida #common_name garden petunia DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 18-Jun-1999 ACCESSIONS B24917 REFERENCE A93619 !$#authors Tumer, N.E.; Clark, W.G.; Tabor, G.J.; Hironaka, C.M.; !1Fraley, R.T.; Shah, D.M. !$#journal Nucleic Acids Res. (1986) 14:3325-3342 !$#title The genes encoding the small subunit of ribulose-1, !15-bisphosphate carboxylase are expressed differentially in !1petunia leaves. !$#cross-references MUID:86205237; PMID:3010233 !$#accession B24917 !'##molecule_type DNA !'##residues 1-180 ##label TUM !'##cross-references GB:X03821; NID:g20492; PIDN:CAA27445.1; PID:g20493 !'##experimental_source strain Mitchell GENETICS !$#gene rbcS !$#introns 59/3; 104/3 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carbon-oxygen lyase; carboxy-lyase; chloroplast; !1monooxygenase; photorespiration FEATURE !$1-57 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$58-180 #product ribulose-bisphosphate carboxylase small !8chain (ssu11A) #status predicted #label MAT SUMMARY #length 180 #molecular-weight 20335 #checksum 2249 SEQUENCE /// ENTRY RKPJS8 #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain (ssu8) precursor - garden petunia ORGANISM #formal_name Petunia x hybrida #common_name garden petunia DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 18-Jun-1999 ACCESSIONS A24917 REFERENCE A93619 !$#authors Tumer, N.E.; Clark, W.G.; Tabor, G.J.; Hironaka, C.M.; !1Fraley, R.T.; Shah, D.M. !$#journal Nucleic Acids Res. (1986) 14:3325-3342 !$#title The genes encoding the small subunit of ribulose-1, !15-bisphosphate carboxylase are expressed differentially in !1petunia leaves. !$#cross-references MUID:86205237; PMID:3010233 !$#accession A24917 !'##molecule_type DNA !'##residues 1-180 ##label TUM !'##cross-references GB:X03820; NID:g20490; PIDN:CAA27444.1; PID:g20491 GENETICS !$#gene rbcS !$#introns 59/3; 104/3; 122/3 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carbon-oxygen lyase; carboxy-lyase; chloroplast; !1monooxygenase; photorespiration FEATURE !$1-57 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$58-180 #product ribulose-bisphosphate carboxylase small !8chain (ssu8) #status predicted #label MAT SUMMARY #length 180 #molecular-weight 20370 #checksum 2967 SEQUENCE /// ENTRY RKFSS #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain precursor - common sunflower ORGANISM #formal_name Helianthus annuus #common_name common sunflower DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 18-Jun-1999 ACCESSIONS A26852; A25749 REFERENCE A26852 !$#authors Waksman, G.; Lebrun, M.; Freyssinet, G. !$#journal Nucleic Acids Res. (1987) 15:7181 !$#title Nucleotide sequence of a gene encoding sunflower ribulose-1, !15-bisphosphate carboxylase/oxygenase small subunit (rbcs). !$#cross-references MUID:88015557; PMID:3658679 !$#accession A26852 !'##molecule_type DNA !'##residues 1-178 ##label WAK !'##cross-references GB:Y00431; NID:g18807; PIDN:CAA68490.1; PID:g18808 REFERENCE A25749 !$#authors Waksman, G.; Freyssinet, G. !$#journal Nucleic Acids Res. (1987) 15:1328 !$#title Nucleotide sequence of a cDNA encoding the ribulose-1, !15-bisphosphate carboxylase/oxygenase from sunflower !1(Helianthus annuus). !$#cross-references MUID:87146436; PMID:3822825 !$#accession A25749 !'##molecule_type mRNA !'##residues 1-178 ##label WAK2 !'##cross-references GB:X05079; NID:g18809; PIDN:CAA28737.1; PID:g755735 !'##note the authors translated the codon AAA for residue 91 as Gly GENETICS !$#introns 57/3; 102/3 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carbon-oxygen lyase; carboxy-lyase; chloroplast; !1monooxygenase; photorespiration FEATURE !$1-57 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$58-178 #product ribulose-bisphosphate carboxylase small !8chain #status predicted #label MAT SUMMARY #length 178 #molecular-weight 20211 #checksum 607 SEQUENCE /// ENTRY RKSPS #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain - spinach (tentative sequence) ORGANISM #formal_name Spinacia oleracea #common_name spinach DATE 30-Nov-1980 #sequence_revision 19-Feb-1984 #text_change 31-Mar-2000 ACCESSIONS A01089; A94607 REFERENCE A90094 !$#authors Martin, P.G. !$#journal Aust. J. Plant Physiol. (1979) 6:401-408 !$#accession A01089 !'##molecule_type protein !'##residues 1-67,71-123 ##label MAR !'##note this sequence has since been revised !'##note the amino end is frequently modified !'##note 94-Tyr was also found REFERENCE A94607 !$#authors Martin, P.G. !$#submission submitted to the Atlas, October 1982 !$#accession A94607 !'##molecule_type protein !'##residues 68-70 ##label MAR2 COMMENT Ribulose-bisphosphate carboxylase, a major component of leaf !1protein, is also a monooxygenase; it catalyzes the !1carboxylation of D-ribulose 1,5-bisphosphate (the primary !1event in photosynthetic carbon dioxide fixation) as well as !1the oxidative fragmentation of the pentose substrate in the !1photorespiration process. Both reactions occur !1simultaneously and in competition at the same active site. COMMENT Each active molecule contains eight large chains, !1synthesized on the chloroplast ribosomes and containing the !1active site, and eight small chains, the precursors of which !1are synthesized on cytoplasmic ribosomes and converted to !1mature small chains during or immediately after transport !1into the chloroplast. CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; monooxygenase; photorespiration SUMMARY #length 123 #molecular-weight 14282 #checksum 5120 SEQUENCE /// ENTRY RKZMS #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain precursor - maize ORGANISM #formal_name Zea mays #common_name maize DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 24-Sep-1999 ACCESSIONS S00534; S12317; S00997; PQ0301 REFERENCE S00534 !$#authors Matsuoka, M.; Kano-Murakami, Y.; Tanaka, Y.; Ozeki, Y.; !1Yamamoto, N. !$#journal J. Biochem. (1987) 102:673-676 !$#title Nucleotide sequence of cDNA encoding the small subunit of !1ribulose-1,5-bisphosphate carboxylase from maize. !$#cross-references MUID:88139216; PMID:3436948 !$#accession S00534 !'##molecule_type mRNA !'##residues 1-170 ##label MATS !'##cross-references EMBL:X06535; NID:g22473; PIDN:CAA29784.1; !1PID:g22474 REFERENCE S12317 !$#authors Lebrun, M.; Waksman, G.; Freyssinet, G. !$#journal Nucleic Acids Res. (1987) 15:4360 !$#title Nucleotide sequence of a gene encoding corn ribulose-1, !15-bisphosphate carboxylase/oxygenase small subunit (rbcs). !$#cross-references MUID:87231019; PMID:3588298 !$#accession S12317 !'##molecule_type DNA !'##residues 1-79,81-170 ##label LEB !'##cross-references EMBL:Y00322; NID:g22464; PIDN:CAA68419.1; !1PID:g22465 REFERENCE S00997 !$#authors Ren, L.; Salnikow, J.; Vater, J. !$#journal Biol. Chem. Hoppe-Seyler (1988) 369:609-615 !$#title Ribulose-1,5-bisphosphate carboxylase/oxygenase from Zea !1mays: amino-acid sequence of the small subunit. !$#cross-references MUID:89134398; PMID:3066367 !$#accession S00997 !'##molecule_type protein !'##residues 48-170 ##label REN !'##note this protein is highly polymorphic. 6-Ile, 7-Val, 17-Ile, !120-Gln, 34-Ile, 35-Val, 38-Glu, 45-Val, 47-Leu, 54-Gln, !177-Thr, 81-Leu, 84-Ile, 85-Val, 89-Val, 90-Val, 91-Ala, !192-Ala, 95-Gly, 106-Val, 107-Arg, 115-Gln, 116-Leu, 117-His, !1and 118-Gly were also found REFERENCE PQ0301 !$#authors Schaeffner, A.R.; Sheen, J. !$#journal Plant Cell (1991) 3:997-1012 !$#title Maize rbcS promoter activity depends on sequence elements !1not found in dicot rbcS promoters. !$#cross-references MUID:92361248; PMID:1822995 !$#accession PQ0301 !'##molecule_type DNA !'##residues 1-10 ##label SCH !'##cross-references GB:S42508; NID:g253496; PIDN:AAD13825.1; !1PID:g4261531 !'##experimental_source hybrid line FR9CmsxFR37 GENETICS !$#gene rbcS !$#introns 49/3 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; photorespiration FEATURE !$1-47 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$48-170 #product ribulose-bisphosphate carboxylase small !8chain #status experimental #label MAT SUMMARY #length 170 #molecular-weight 19151 #checksum 529 SEQUENCE /// ENTRY RKWTS #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain precursor (clone pWS4.3) - wheat ORGANISM #formal_name Triticum aestivum #common_name common wheat DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 12-Apr-1996 ACCESSIONS A01090 REFERENCE A01090 !$#authors Broglie, R.; Coruzzi, G.; Lamppa, G.; Keith, B.; Chua, N.H. !$#journal Bio/Technology (1983) 1:55-61 !$#title Structural analysis of nuclear genes coding for the !1precursor to the small subunit of wheat ribulose-1, !15-bisphosphate carboxylase. !$#accession A01090 !'##molecule_type DNA !'##residues 1-174 ##label BRO !'##cross-references GB:M37477 !'##experimental_source cv. ERA COMMENT Ribulose-bisphosphate carboxylase, a major component of leaf !1protein, is also a monooxygenase; it catalyzes the !1carboxylation of D-ribulose 1,5-bisphosphate (the primary !1event in photosynthetic carbon dioxide fixation) as well as !1the oxidative fragmentation of the pentose substrate in the !1photorespiration process. These reactions occur !1simultaneously and in competition at the same active site. COMMENT Each active molecule contains eight large chains, !1synthesized on the chloroplast ribosomes and containing the !1active site, and eight small chains, the precursors of which !1are synthesized on cytoplasmic ribosomes and converted to !1mature small chains during or immediately after transport !1into the chloroplast. COMMENT This protein is coded by one member of a small multigene !1family. GENETICS !$#introns 47/3 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; monooxygenase; photorespiration FEATURE !$1-46 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$47-174 #product ribulose-bisphosphate carboxylase small !8chain #status predicted #label MAT SUMMARY #length 174 #molecular-weight 19443 #checksum 3778 SEQUENCE /// ENTRY RKWTS9 #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain precursor (clone pW9) - wheat ORGANISM #formal_name Triticum aestivum #common_name common wheat DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Feb-1994 ACCESSIONS S00505 REFERENCE A01090 !$#authors Broglie, R.; Coruzzi, G.; Lamppa, G.; Keith, B.; Chua, N.H. !$#journal Bio/Technology (1983) 1:55-61 !$#title Structural analysis of nuclear genes coding for the !1precursor to the small subunit of wheat ribulose-1, !15-bisphosphate carboxylase. !$#accession S00505 !'##molecule_type mRNA !'##residues 1-175 ##label BRO !'##cross-references GB:M37328 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carbon-oxygen lyase; carboxy-lyase; chloroplast; !1monooxygenase; photorespiration FEATURE !$1-47 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$48-175 #product ribulose-bisphosphate carboxylase small !8chain #status predicted #label MAT SUMMARY #length 175 #molecular-weight 19454 #checksum 3427 SEQUENCE /// ENTRY RKWTS5 #type fragment TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain (clone 512) - wheat (fragment) ORGANISM #formal_name Triticum aestivum #common_name common wheat DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 18-Jun-1999 ACCESSIONS A20899; A05006 REFERENCE A93499 !$#authors Smith, S.M.; Bedbrook, J.; Speirs, J. !$#journal Nucleic Acids Res. (1983) 11:8719-8734 !$#title Characterisation of three cDNA clones encoding different !1mRNAs for the precursor to the small subunit of wheat !1ribulosebisphosphate carboxylase. !$#cross-references MUID:84169511; PMID:6324097 !$#accession A20899 !'##molecule_type mRNA !'##residues 1-113 ##label SMI !'##cross-references GB:X00234; NID:g21865; PIDN:CAA25057.1; PID:g21866 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; monooxygenase; photorespiration SUMMARY #length 113 #checksum 8558 SEQUENCE /// ENTRY RKRZS #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain precursor - rice ORGANISM #formal_name Oryza sativa #common_name rice DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 18-Jun-1999 ACCESSIONS S01235 REFERENCE S01235 !$#authors Xie, Y.; Wu, R. !$#journal Nucleic Acids Res. (1988) 16:7749 !$#title Nucleotide sequence of a ribulose-1,5-bisphosphate !1carboxylase/oxygenase small subunit gene (rbcS) in rice. !$#cross-references MUID:88319987; PMID:3412915 !$#accession S01235 !'##molecule_type DNA !'##residues 1-172 ##label XIE !'##cross-references EMBL:X07515; NID:g20340; PIDN:CAA30393.1; !1PID:g20341 COMMENT Ribulose-bisphosphate carboxylase, a major component of leaf !1protein, is also a monooxygenase; it catalyzes the !1carboxylation of D-ribulose 1,5-bisphosphate (the primary !1event in photosynthetic carbon dioxide fixation) as well as !1the oxidative fragmentation of the pentose substrate in the !1photorespiration process. These reactions occur !1simultaneously and in competition at the same active site. COMMENT Each active molecule contains eight large chains, !1synthesized on the chloroplast ribosomes and containing the !1active site, and eight small chains, the precursors of which !1are synthesized on cytoplasmic ribosomes and converted to !1mature small chains during or immediately after transport !1into the chloroplast. COMMENT This protein is coded by one member of a small multigene !1family. GENETICS !$#gene rbcS !$#introns 47/3 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; monooxygenase; photorespiration FEATURE !$1-45 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$46-172 #product ribulose-bisphosphate carboxylase small !8chain #status predicted #label MAT SUMMARY #length 172 #molecular-weight 19468 #checksum 1371 SEQUENCE /// ENTRY RKRZS9 #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain precursor (clone pOSSS1139) - rice ORGANISM #formal_name Oryza sativa #common_name rice DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jun-2000 ACCESSIONS JA0070 REFERENCE JA0070 !$#authors Matsuoka, M.; Kano-Murakami, Y.; Tanaka, Y.; Ozeki, Y.; !1Yamamoto, N. !$#journal Plant Cell Physiol. (1988) 29:1015-1022 !$#title Classification and nucleotide sequence of cDNA encoding the !1small subunit of ribulose-1,5-bisphosphate carboxylase from !1rice. !$#accession JA0070 !'##molecule_type mRNA !'##residues 1-175 ##label MTS !'##cross-references GB:D00643; NID:g218207; PIDN:BAA00538.1; !1PID:g218208 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carbon-oxygen lyase; carboxy-lyase; chloroplast; !1monooxygenase; photorespiration FEATURE !$1-47 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$48-175 #product ribulose-bisphosphate carboxylase small !8chain #status predicted #label MAT SUMMARY #length 175 #molecular-weight 19647 #checksum 2813 SEQUENCE /// ENTRY RKRZS6 #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain precursor (clone pOSSS2106) - rice ORGANISM #formal_name Oryza sativa #common_name rice DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jun-2000 ACCESSIONS JU0005 REFERENCE JA0070 !$#authors Matsuoka, M.; Kano-Murakami, Y.; Tanaka, Y.; Ozeki, Y.; !1Yamamoto, N. !$#journal Plant Cell Physiol. (1988) 29:1015-1022 !$#title Classification and nucleotide sequence of cDNA encoding the !1small subunit of ribulose-1,5-bisphosphate carboxylase from !1rice. !$#accession JU0005 !'##molecule_type mRNA !'##residues 1-175 ##label MTS !'##cross-references GB:D00644; NID:g218209; PIDN:BAA00539.1; !1PID:g218210 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; monooxygenase; photorespiration FEATURE !$1-47 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$48-175 #product ribulose-bisphosphate carboxylase small !8chain #status predicted #label MAT SUMMARY #length 175 #molecular-weight 19689 #checksum 2696 SEQUENCE /// ENTRY RKDWS #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain precursor (clone pLgSSU1) - swollen duckweed ORGANISM #formal_name Lemna gibba #common_name swollen duckweed DATE 17-May-1985 #sequence_revision 31-Mar-1991 #text_change 12-Apr-1996 ACCESSIONS A01091; S12280 REFERENCE A01091 !$#authors Stiekema, W.J.; Wimpee, C.F.; Tobin, E.M. !$#journal Nucleic Acids Res. (1983) 11:8051-8061 !$#title Nucleotide sequence encoding the precursor of the small !1subunit of ribulose 1,5-bisphosphate carboxylase from Lemna !1gibba L.G-3. !$#cross-references MUID:84069822; PMID:6316282 !$#accession A01091 !'##molecule_type mRNA !'##residues 1-70,'F',72,'LS',75-173 ##label STI !'##note this sequence has been revised in reference S11680 !'##note the codon given for residue 108 (AAC) is inconsistent with the !1authors' translation REFERENCE S11680 !$#authors Silverthorne, J.; Wimpee, C.F.; Yamada, T.; Rolfe, S.A.; !1Tobin, E.M. !$#journal Plant Mol. Biol. (1990) 15:49-58 !$#title Differential expression of individual genes encoding the !1small subunit of ribulose-1,5-bisphosphate carboxylase in !1Lemna gibba. !$#cross-references MUID:91355864; PMID:2103442 !$#accession S12280 !'##molecule_type mRNA !'##residues 71-74 ##label SIL COMMENT Ribulose-bisphosphate carboxylase, a major component of leaf !1protein, is also a monooxygenase; it catalyzes the !1carboxylation of D-ribulose 1,5-bisphosphate (the primary !1event in photosynthetic carbon dioxide fixation) as well as !1the oxidative fragmentation of the pentose substrate in the !1photorespiration process. These reactions occur !1simultaneously and in competition at the same active site. COMMENT Each active molecule contains eight large chains, !1synthesized on the chloroplast ribosomes and containing the !1active site, and eight small chains, the precursors of which !1are synthesized on cytoplasmic ribosomes and converted to !1mature small chains during or immediately after transport !1into the chloroplast. COMMENT This protein is coded by one member of a small multigene !1family. CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; monooxygenase; photorespiration FEATURE !$1-53 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$54-173 #product ribulose-bisphosphate carboxylase small !8chain #status predicted #label MAT SUMMARY #length 173 #molecular-weight 19545 #checksum 1451 SEQUENCE /// ENTRY RKDWSU #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain precursor (clone SSU5B) - swollen duckweed ALTERNATE_NAMES ribulose-1,5-bisphosphate carboxylase/oxygenase ORGANISM #formal_name Lemna gibba #common_name swollen duckweed DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 18-Jun-1999 ACCESSIONS S11684 REFERENCE S11680 !$#authors Silverthorne, J.; Wimpee, C.F.; Yamada, T.; Rolfe, S.A.; !1Tobin, E.M. !$#journal Plant Mol. Biol. (1990) 15:49-58 !$#title Differential expression of individual genes encoding the !1small subunit of ribulose-1,5-bisphosphate carboxylase in !1Lemna gibba. !$#cross-references MUID:91355864; PMID:2103442 !$#accession S11684 !'##molecule_type DNA !'##residues 1-177 ##label SIL !'##cross-references EMBL:X17231; NID:g19431; PIDN:CAA35100.1; !1PID:g295821 GENETICS !$#gene rbcS !$#introns 103/3 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; photorespiration FEATURE !$1-57 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$58-177 #product ribulose-bisphosphate carboxylase small !8chain #status predicted #label MAT SUMMARY #length 177 #molecular-weight 19872 #checksum 471 SEQUENCE /// ENTRY RKDWSB #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain precursor (clone SSU40B) - swollen duckweed ALTERNATE_NAMES ribulose-1,5-bisphosphate carboxylase/oxygenase ORGANISM #formal_name Lemna gibba #common_name swollen duckweed DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 18-Jun-1999 ACCESSIONS S11682; S12069 REFERENCE S11680 !$#authors Silverthorne, J.; Wimpee, C.F.; Yamada, T.; Rolfe, S.A.; !1Tobin, E.M. !$#journal Plant Mol. Biol. (1990) 15:49-58 !$#title Differential expression of individual genes encoding the !1small subunit of ribulose-1,5-bisphosphate carboxylase in !1Lemna gibba. !$#cross-references MUID:91355864; PMID:2103442 !$#accession S11682 !'##molecule_type DNA !'##residues 1-177 ##label SIL !'##cross-references EMBL:X17234 REFERENCE S12065 !$#authors Tobin, E.M. !$#submission submitted to the EMBL Data Library, December 1989 !$#accession S12069 !'##molecule_type DNA !'##residues 1-11,'A',12-23,25-33,'P',35-177 ##label TOB !'##cross-references EMBL:X17234; NID:g19421; PIDN:CAA35103.1; !1PID:g295819 GENETICS !$#gene rbcS !$#introns 103/3 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; photorespiration FEATURE !$1-57 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$58-177 #product ribulose-bisphosphate carboxylase small !8chain #status predicted #label MAT SUMMARY #length 177 #molecular-weight 19848 #checksum 9727 SEQUENCE /// ENTRY RKDWSA #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain precursor (clone SSU5A) - swollen duckweed ALTERNATE_NAMES ribulose-1,5-bisphosphate carboxylase/oxygenase ORGANISM #formal_name Lemna gibba #common_name swollen duckweed DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 18-Jun-1999 ACCESSIONS S11683 REFERENCE S11680 !$#authors Silverthorne, J.; Wimpee, C.F.; Yamada, T.; Rolfe, S.A.; !1Tobin, E.M. !$#journal Plant Mol. Biol. (1990) 15:49-58 !$#title Differential expression of individual genes encoding the !1small subunit of ribulose-1,5-bisphosphate carboxylase in !1Lemna gibba. !$#cross-references MUID:91355864; PMID:2103442 !$#accession S11683 !'##molecule_type DNA !'##residues 1-177 ##label SIL !'##cross-references EMBL:X17230; NID:g19426; PIDN:CAA35099.1; !1PID:g295820 GENETICS !$#gene rbcS !$#introns 103/3 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; photorespiration FEATURE !$1-57 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$58-177 #product ribulose-bisphosphate carboxylase small !8chain #status predicted #label MAT SUMMARY #length 177 #molecular-weight 19802 #checksum 241 SEQUENCE /// ENTRY RKDWS4 #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain precursor (clone SSU40A) - swollen duckweed ALTERNATE_NAMES ribulose-1,5-bisphosphate carboxylase/oxygenase ORGANISM #formal_name Lemna gibba #common_name swollen duckweed DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 18-Jun-1999 ACCESSIONS S11681; S12065 REFERENCE S11680 !$#authors Silverthorne, J.; Wimpee, C.F.; Yamada, T.; Rolfe, S.A.; !1Tobin, E.M. !$#journal Plant Mol. Biol. (1990) 15:49-58 !$#title Differential expression of individual genes encoding the !1small subunit of ribulose-1,5-bisphosphate carboxylase in !1Lemna gibba. !$#cross-references MUID:91355864; PMID:2103442 !$#accession S11681 !'##molecule_type DNA !'##residues 1-177 ##label SIL !'##cross-references EMBL:X17233 REFERENCE S12065 !$#authors Tobin, E.M. !$#submission submitted to the EMBL Data Library, December 1989 !$#accession S12065 !'##molecule_type DNA !'##residues 1-11,'A',12-23,25-33,'P',35-177 ##label TOB !'##cross-references EMBL:X17233; NID:g19416; PIDN:CAA35102.1; !1PID:g295818 GENETICS !$#gene rbcS !$#introns 103/3 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; photorespiration FEATURE !$1-57 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$58-177 #product ribulose-bisphosphate carboxylase small !8chain #status predicted #label MAT SUMMARY #length 177 #molecular-weight 19775 #checksum 9652 SEQUENCE /// ENTRY RKDWS6 #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain precursor (clone SSU26) - swollen duckweed ALTERNATE_NAMES ribulose-1,5-bisphosphate carboxylase/oxygenase ORGANISM #formal_name Lemna gibba #common_name swollen duckweed DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 18-Jun-1999 ACCESSIONS S11680 REFERENCE S11680 !$#authors Silverthorne, J.; Wimpee, C.F.; Yamada, T.; Rolfe, S.A.; !1Tobin, E.M. !$#journal Plant Mol. Biol. (1990) 15:49-58 !$#title Differential expression of individual genes encoding the !1small subunit of ribulose-1,5-bisphosphate carboxylase in !1Lemna gibba. !$#cross-references MUID:91355864; PMID:2103442 !$#accession S11680 !'##molecule_type DNA !'##residues 1-177 ##label SIL !'##cross-references EMBL:X17232; NID:g19411; PIDN:CAA35101.1; !1PID:g295817 GENETICS !$#gene rbcS !$#introns 103/3 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; photorespiration FEATURE !$1-57 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$58-177 #product ribulose-bisphosphate carboxylase small !8chain #status predicted #label MAT SUMMARY #length 177 #molecular-weight 19815 #checksum 69 SEQUENCE /// ENTRY RKJK3M #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain 3 precursor - Acetabularia mediterranea ORGANISM #formal_name Acetabularia mediterranea DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 07-Dec-1999 ACCESSIONS S07117 REFERENCE S05349 !$#authors Schneider, S.U.; Leible, M.B.; Yang, X.P. !$#journal Mol. Gen. Genet. (1989) 218:445-452 !$#title Strong homology between the small subunit of ribulose-1, !15-bisphosphate carboxylase/oxygenase of two species of !1Acetabularia and the occurrence of unusual codon usage. !$#cross-references MUID:90066347; PMID:2573818 !$#accession S07117 !'##molecule_type mRNA !'##residues 1-182 ##label SCH !'##cross-references EMBL:X51813; NID:g16038; PIDN:CAA36110.1; !1PID:g732553 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing GENETICS !$#gene rbcS !$#genetic_code SGC5 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; photorespiration FEATURE !$1-42 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$43-182 #product ribulose-bisphosphate carboxylase small !8chain #status experimental #label MAT SUMMARY #length 182 #molecular-weight 20571 #checksum 4675 SEQUENCE /// ENTRY RKJK1M #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain 1 precursor - Acetabularia mediterranea ORGANISM #formal_name Acetabularia mediterranea DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 07-Dec-1999 ACCESSIONS S05349 REFERENCE S05349 !$#authors Schneider, S.U.; Leible, M.B.; Yang, X.P. !$#journal Mol. Gen. Genet. (1989) 218:445-452 !$#title Strong homology between the small subunit of ribulose-1, !15-bisphosphate carboxylase/oxygenase of two species of !1Acetabularia and the occurrence of unusual codon usage. !$#cross-references MUID:90066347; PMID:2573818 !$#accession S05349 !'##molecule_type mRNA !'##residues 1-182 ##label SCH !'##cross-references EMBL:X51811; NID:g16032; PIDN:CAA36108.1; !1PID:g732551 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing GENETICS !$#gene rbcS !$#genetic_code SGC5 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; photorespiration FEATURE !$1-42 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$43-182 #product ribulose-bisphosphate carboxylase small !8chain #status experimental #label MAT SUMMARY #length 182 #molecular-weight 20659 #checksum 4945 SEQUENCE /// ENTRY RKJK4M #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain 4 precursor - Acetabularia mediterranea ORGANISM #formal_name Acetabularia mediterranea DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 07-Dec-1999 ACCESSIONS S05350 REFERENCE S05349 !$#authors Schneider, S.U.; Leible, M.B.; Yang, X.P. !$#journal Mol. Gen. Genet. (1989) 218:445-452 !$#title Strong homology between the small subunit of ribulose-1, !15-bisphosphate carboxylase/oxygenase of two species of !1Acetabularia and the occurrence of unusual codon usage. !$#cross-references MUID:90066347; PMID:2573818 !$#accession S05350 !'##molecule_type mRNA !'##residues 1-182 ##label SCH !'##cross-references EMBL:X51814; NID:g16042; PIDN:CAA36111.1; !1PID:g732554 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing GENETICS !$#gene rbcS !$#genetic_code SGC5 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; photorespiration FEATURE !$1-42 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$43-182 #product ribulose-bisphosphate carboxylase small !8chain #status experimental #label MAT SUMMARY #length 182 #molecular-weight 20533 #checksum 5862 SEQUENCE /// ENTRY RKJK5M #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain 5 precursor - Acetabularia mediterranea ORGANISM #formal_name Acetabularia mediterranea DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 07-Dec-1999 ACCESSIONS S05351 REFERENCE S05349 !$#authors Schneider, S.U.; Leible, M.B.; Yang, X.P. !$#journal Mol. Gen. Genet. (1989) 218:445-452 !$#title Strong homology between the small subunit of ribulose-1, !15-bisphosphate carboxylase/oxygenase of two species of !1Acetabularia and the occurrence of unusual codon usage. !$#cross-references MUID:90066347; PMID:2573818 !$#accession S05351 !'##molecule_type mRNA !'##residues 1-183 ##label SCH !'##cross-references EMBL:X51815; NID:g16046; PIDN:CAA36112.1; !1PID:g732555 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing GENETICS !$#gene rbcS !$#genetic_code SGC5 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; photorespiration FEATURE !$1-43 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$44-182 #product ribulose-bisphosphate carboxylase small !8chain #status experimental #label MAT SUMMARY #length 183 #molecular-weight 20555 #checksum 6015 SEQUENCE /// ENTRY RKJK4C #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain 4 precursor - Acetabularia cliftonii ORGANISM #formal_name Acetabularia cliftonii DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 07-Dec-1999 ACCESSIONS S05353 REFERENCE S05349 !$#authors Schneider, S.U.; Leible, M.B.; Yang, X.P. !$#journal Mol. Gen. Genet. (1989) 218:445-452 !$#title Strong homology between the small subunit of ribulose-1, !15-bisphosphate carboxylase/oxygenase of two species of !1Acetabularia and the occurrence of unusual codon usage. !$#cross-references MUID:90066347; PMID:2573818 !$#accession S05353 !'##molecule_type mRNA !'##residues 1-182 ##label SCH !'##cross-references EMBL:X51809; NID:g15971; PIDN:CAA36106.1; !1PID:g732547 GENETICS !$#gene rbcS !$#genetic_code SGC5 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; photorespiration FEATURE !$1-42 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$43-182 #product ribulose-bisphosphate carboxylase small !8chain #status experimental #label MAT SUMMARY #length 182 #molecular-weight 20647 #checksum 4992 SEQUENCE /// ENTRY RKJK5C #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain 5 precursor - Acetabularia cliftonii ORGANISM #formal_name Acetabularia cliftonii DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 07-Dec-1999 ACCESSIONS S05354 REFERENCE S05349 !$#authors Schneider, S.U.; Leible, M.B.; Yang, X.P. !$#journal Mol. Gen. Genet. (1989) 218:445-452 !$#title Strong homology between the small subunit of ribulose-1, !15-bisphosphate carboxylase/oxygenase of two species of !1Acetabularia and the occurrence of unusual codon usage. !$#cross-references MUID:90066347; PMID:2573818 !$#accession S05354 !'##molecule_type mRNA !'##residues 1-184 ##label SCH !'##cross-references EMBL:X51810; NID:g15975; PIDN:CAA36107.1; !1PID:g732548 GENETICS !$#gene rbcS !$#genetic_code SGC5 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; photorespiration FEATURE !$1-44 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$45-182 #product ribulose-bisphosphate carboxylase small !8chain #status experimental #label MAT SUMMARY #length 184 #molecular-weight 20684 #checksum 5269 SEQUENCE /// ENTRY RKJK3C #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain 3 precursor - Acetabularia cliftonii ORGANISM #formal_name Acetabularia cliftonii DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 07-Dec-1999 ACCESSIONS S05352 REFERENCE S05349 !$#authors Schneider, S.U.; Leible, M.B.; Yang, X.P. !$#journal Mol. Gen. Genet. (1989) 218:445-452 !$#title Strong homology between the small subunit of ribulose-1, !15-bisphosphate carboxylase/oxygenase of two species of !1Acetabularia and the occurrence of unusual codon usage. !$#cross-references MUID:90066347; PMID:2573818 !$#accession S05352 !'##molecule_type mRNA !'##residues 1-183 ##label SCH !'##cross-references EMBL:X51808; NID:g15967; PIDN:CAA36105.1; !1PID:g732546 GENETICS !$#gene rbcS !$#genetic_code SGC5 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; photorespiration FEATURE !$1-43 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$44-182 #product ribulose-bisphosphate carboxylase small !8chain #status experimental #label MAT SUMMARY #length 183 #molecular-weight 20804 #checksum 5926 SEQUENCE /// ENTRY RKKMS1 #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain 1 precursor - Chlamydomonas reinhardtii ORGANISM #formal_name Chlamydomonas reinhardtii DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 30-Jun-1993 ACCESSIONS A25785 REFERENCE A92933 !$#authors Goldschmidt-Clermont, M.; Rahire, M. !$#journal J. Mol. Biol. (1986) 191:421-432 !$#title Sequence, evolution and differential expression of the two !1genes encoding variant small subunits of ribulose !1bisphosphate carboxylase/oxygenase in Chlamydomonas !1reinhardtii. !$#cross-references MUID:87141171; PMID:3820291 !$#accession A25785 !'##molecule_type DNA !'##residues 1-185 ##label GOL !'##cross-references GB:X04471 GENETICS !$#gene rbcS1 !$#introns 55/2; 82/1; 110/3 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carbon-oxygen lyase; carboxy-lyase; chloroplast; !1monooxygenase; photorespiration FEATURE !$1-45 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$46-185 #product ribulose-bisphosphate carboxylase small !8chain #status predicted #label MAT SUMMARY #length 185 #molecular-weight 20620 #checksum 7484 SEQUENCE /// ENTRY RKKMS2 #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain 2 precursor - Chlamydomonas reinhardtii ORGANISM #formal_name Chlamydomonas reinhardtii DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 18-Jun-1999 ACCESSIONS B25785; S39044 REFERENCE A92933 !$#authors Goldschmidt-Clermont, M.; Rahire, M. !$#journal J. Mol. Biol. (1986) 191:421-432 !$#title Sequence, evolution and differential expression of the two !1genes encoding variant small subunits of ribulose !1bisphosphate carboxylase/oxygenase in Chlamydomonas !1reinhardtii. !$#cross-references MUID:87141171; PMID:3820291 !$#accession B25785 !'##molecule_type DNA !'##residues 1-185 ##label GOL !'##cross-references GB:X04472; NID:g18205; PIDN:CAA28160.1; PID:g295799 REFERENCE S39044 !$#authors Su, Q.; Boschetti, A. !$#journal Eur. J. Biochem. (1993) 217:1039-1047 !$#title Partial purification and properties of enzymes involved in !1the processing of a chloroplast import protein from !1Chlamydomonas reinhardii. !$#cross-references MUID:94039124; PMID:8223627 !$#accession S39044 !'##status preliminary !'##molecule_type protein !'##residues 25-60 ##label SUA GENETICS !$#gene rbcS2 !$#introns 55/2; 82/1; 110/3 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carbon-oxygen lyase; carboxy-lyase; chloroplast; !1monooxygenase; photorespiration FEATURE !$1-45 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$46-185 #product ribulose-bisphosphate carboxylase small !8chain #status predicted #label MAT SUMMARY #length 185 #molecular-weight 20647 #checksum 8204 SEQUENCE /// ENTRY RKAIS #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain - Anabaena sp. ORGANISM #formal_name Anabaena sp. DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 18-Jun-1999 ACCESSIONS A22046 REFERENCE A22046 !$#authors Nierzwicki-Bauer, S.A.; Curtis, S.E.; Haselkorn, R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:5961-5965 !$#title Cotranscription of genes encoding the small and large !1subunits of ribulose-1,5-bisphosphate carboxylase in the !1cyanobacterium Anabaena 7120. !$#cross-references MUID:85014888; PMID:6091125 !$#accession A22046 !'##molecule_type DNA !'##residues 1-109 ##label NIE !'##cross-references GB:J01540; NID:g142104; PIDN:AAA22042.1; !1PID:g142106 GENETICS !$#gene rbcS CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carbon-oxygen lyase; carboxy-lyase; monooxygenase; !1photorespiration SUMMARY #length 109 #molecular-weight 12827 #checksum 7339 SEQUENCE /// ENTRY RKYCS #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain - Synechococcus sp. (strain PCC 6301) ORGANISM #formal_name Synechococcus sp. #variety PCC 6301 DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 18-Jun-1999 ACCESSIONS S07351 REFERENCE S07351 !$#authors Shinozaki, K.; Sugiura, M. !$#journal Nucleic Acids Res. (1983) 11:6957-6964 !$#title The gene for the small subunit of ribulose-1,5-bisphosphate !1carboxylase/oxygenase is located close to the gene for the !1large subunit in the cyanobacterium Anacystis nidulans 6301. !$#cross-references MUID:84041496; PMID:6415615 !$#accession S07351 !'##molecule_type DNA !'##residues 1-111 ##label SHI !'##cross-references GB:X03220; NID:g38924; PIDN:CAA26973.1; PID:g38928 !'##experimental_source PCC 6301 GENETICS !$#gene rbcS FUNCTION !$#description carbon dioxide fixation; carbon-carbon lyase; carbon-oxygen !1lyase; carboxy-lyase; monooxygenase !$#pathway Calvin cycle !$#note photorespiration is a side reaction of this enzyme CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carbon-oxygen lyase; carboxy-lyase; monooxygenase; !1photorespiration SUMMARY #length 111 #molecular-weight 13333 #checksum 291 SEQUENCE /// ENTRY RKKRS1 #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain rbcB - Chromatium vinosum ORGANISM #formal_name Chromatium vinosum DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 26-Feb-1999 ACCESSIONS B32303; D36095; B60823 REFERENCE A32303 !$#authors Viale, A.M.; Kobayashi, H.; Akazawa, T. !$#journal J. Bacteriol. (1989) 171:2391-2400 !$#title Expressed genes for plant-type ribulose 1,5-bisphosphate !1carboxylase/oxygenase in the photosynthetic bacterium !1Chromatium vinosum, which possesses two complete sets of the !1genes. !$#cross-references MUID:89213919; PMID:2708310 !$#accession B32303 !'##molecule_type DNA !'##residues 1-118 ##label VIA !'##cross-references GB:M26396 REFERENCE A36095 !$#authors Viale, A.M.; Kobayashi, H.; Akazawa, T. !$#journal J. Biol. Chem. (1990) 265:18386-18392 !$#title Distinct properties of Escherichia coli products of !1plant-type ribulose-1,5-bisphosphate carboxylase/oxygenase !1directed by two sets of genes from the photosynthetic !1bacterium Chromatium vinosum. !$#cross-references MUID:91009333; PMID:2211708 !$#accession D36095 !'##molecule_type protein !'##residues 2-27 ##label VI2 REFERENCE A60823 !$#authors Torres-Ruiz, J.; McFadden, B.A. !$#journal Arch. Biochem. Biophys. (1987) 254:63-68 !$#title The nature of L-8 and L-8S-8 forms of ribulose bisphosphate !1carboxylase/oxygenase from Chromatium vinosum. !$#cross-references MUID:87212016; PMID:3579306 !$#accession B60823 !'##molecule_type protein !'##residues 2-4,'E',6-9,'T',11-29,'W',32-39,'F',41-44,'X',46-50 ##label !1TOR COMMENT Two distinct sets of genes (i.e., rbcA-rbcB and rbcL-rbcS) !1for fully active ribulose-1,5-bisphosphate carboxylase exist !1in C. vinosum. The rbcL-rbcS set was barely expressed in the !1bacterium under standard photoautotrophic growth conditions. GENETICS !$#gene rbcB CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; heterohexadecamer; monooxygenase; !1photorespiration; photosynthesis SUMMARY #length 118 #molecular-weight 13794 #checksum 1696 SEQUENCE /// ENTRY RKJVSA #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain - Alvinoconcha hessleri symbiotic bacterium ORGANISM #formal_name Alvinoconcha hessleri symbiotic bacterium DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 18-Jun-1999 ACCESSIONS B38262 REFERENCE A38262 !$#authors Stein, J.L.; Haygood, M.; Felbeck, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:8850-8854 !$#title Nucleotide sequence and expression of a deep-sea ribulose-1, !15-bisphosphate carboxylase gene cloned from a !1chemoautotrophic bacterial endosymbiont. !$#cross-references MUID:91062376; PMID:2247456 !$#accession B38262 !'##molecule_type DNA !'##residues 1-121 ##label STE !'##cross-references GB:M34536; NID:g154656; PIDN:AAA27388.1; !1PID:g154658 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carbon-oxygen lyase; carboxy-lyase; monooxygenase; !1photorespiration SUMMARY #length 121 #molecular-weight 13856 #checksum 4029 SEQUENCE /// ENTRY RKKRS2 #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) small chain 2 - Chromatium vinosum ORGANISM #formal_name Chromatium vinosum DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jun-2000 ACCESSIONS JQ0587; C36095 REFERENCE JQ0586 !$#authors Kobayashi, H.; Viale, A.M.; Takabe, T.; Akazawa, T.; Wada, !1K.; Shinozaki, K.; Kobayashi, K.; Sugiura, M. !$#journal Gene (1991) 97:55-62 !$#title Sequence and expression of genes encoding the large and !1small subunits of ribulose 1,5-bisphosphate carboxylase/ !1oxygenase from Chromatium vinosum. !$#cross-references MUID:91138986; PMID:1899846 !$#accession JQ0587 !'##molecule_type DNA !'##residues 1-113 ##label KOB !'##cross-references GB:D90204; NID:g804820; PIDN:BAA14230.1; !1PID:g804822 REFERENCE A36095 !$#authors Viale, A.M.; Kobayashi, H.; Akazawa, T. !$#journal J. Biol. Chem. (1990) 265:18386-18392 !$#title Distinct properties of Escherichia coli products of !1plant-type ribulose-1,5-bisphosphate carboxylase/oxygenase !1directed by two sets of genes from the photosynthetic !1bacterium Chromatium vinosum. !$#cross-references MUID:91009333; PMID:2211708 !$#accession C36095 !'##status preliminary !'##molecule_type protein !'##residues 1-24 ##label VIA GENETICS !$#gene rbcS !$#note two distinct sets of genes (i.e., rbcA-rbcB and rbcL-rbcS) !1for fully active ribulose-1,5-bisphosphate carboxylase exist !1in C. vinosum; the rbcL-rbcS set was barely expressed in the !1bacterium under standard photoautotrophic growth conditions CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase small chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carbon-oxygen lyase; carboxy-lyase; monooxygenase; !1photorespiration SUMMARY #length 113 #molecular-weight 13391 #checksum 7645 SEQUENCE /// ENTRY S53636 #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) short chain precursor - Euglena gracilis ORGANISM #formal_name Euglena gracilis DATE 18-Feb-2000 #sequence_revision 18-Feb-2000 #text_change 16-Jun-2000 ACCESSIONS S53636; S08382; S23105 REFERENCE S53636 !$#authors Tessier, L.H.; Paulus, F.; Keller, M.; Vial, C.; Imbault, P. !$#journal J. Mol. Biol. (1995) 245:22-33 !$#title Structure and expression of Euglena gracilis nuclear rbcS !1genes encoding the small subunits of the ribulose 1, !15-bisphosphate carboxylase/oxygenase: a novel splicing !1process for unusual intervening sequences? !$#cross-references MUID:95123643; PMID:7823317 !$#accession S53636 !'##status preliminary !'##molecule_type DNA !'##residues 1-1275 ##label TES1 !'##cross-references EMBL:X79152; NID:g642976; PIDN:CAA55779.1; !1PID:g642977 REFERENCE S08382 !$#authors Chan, R.L.; Keller, M.; Canaday, J.; Weil, J.H.; Imbault, P. !$#journal EMBO J. (1990) 9:333-338 !$#title Eight small subunits of Euglena ribulose 1-5 bisphosphate !1carboxylase/oxygenase are translated from a large mRNA as a !1polyprotein. !$#cross-references MUID:90151605; PMID:2105882 !$#accession S08382 !'##molecule_type mRNA !'##residues 1-410,412-492,'H',494-565,'D',567-698,700-843,'S',844-962, !1964-997,'D',999-1141,'E',1143-1275 ##label CHA !'##cross-references EMBL:X17546; NID:g18427; PIDN:CAA35584.1; !1PID:g18428 REFERENCE S23105 !$#authors Tessier, L.H.; Chan, R.L.; Keller, M.; Weil, J.H.; Imbault, !1P. !$#journal FEBS Lett. (1992) 304:252-255 !$#title The Euglena gracilis rbcS gene contains introns with unusual !1borders. !$#cross-references MUID:92316242; PMID:1618332 !$#accession S23105 !'##molecule_type DNA !'##residues 1-271;1269-1275 ##label TES2 !'##cross-references EMBL:X66617; NID:g18432; PIDN:CAA47180.1; !1PID:g1360729 !'##note the translated sequence in GenBank entry EGRBCS5, release !1111.0, (PIDN:CAA47180.1) differs from the published sequence !1in using incorrectly placed splice boundaries GENETICS !$#gene rbcS !$#introns 98/3; 202/3 !$#note the list of introns may be incomplete CLASSIFICATION #superfamily Euglena ribulose-bisphosphate carboxylase small !1chain polyprotein KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carbon-oxygen lyase; carboxy-lyase; chloroplast; !1duplication; monooxygenase; photorespiration; polyprotein FEATURE !$1-134 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$135-268 #product ribulose-bisphosphate carboxylase small !8chain #status predicted #label MAT1\ !$279-411 #product ribulose-bisphosphate carboxylase small !8chain #status predicted #label MAT2\ !$422-555 #product ribulose-bisphosphate carboxylase small !8chain #status predicted #label MAT3\ !$566-698 #product ribulose-bisphosphate carboxylase small !8chain #status predicted #label MAT4\ !$709-843 #product ribulose-bisphosphate carboxylase small !8chain #status predicted #label MAT5\ !$854-986 #product ribulose-bisphosphate carboxylase small !8chain #status predicted #label MAT6\ !$997-1130 #product ribulose-bisphosphate carboxylase small !8chain #status predicted #label MAT7\ !$1141-1273 #product ribulose-bisphosphate carboxylase small !8chain #status predicted #label MAT8 SUMMARY #length 1275 #molecular-weight 142058 #checksum 4071 SEQUENCE /// ENTRY RKKHLD #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain precursor - Douglas fir chloroplast ORGANISM #formal_name chloroplast Pseudotsuga menziesii #common_name Douglas fir DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS S12798 REFERENCE S12798 !$#authors Hipkins, V.D.; Tsai, C.H.; Strauss, S.H. !$#journal Plant Mol. Biol. (1990) 15:505-507 !$#title Sequence of the gene for the large subunit of ribulose 1, !15-bisphosphate carboxylase from a gymnosperm, Douglas fir. !$#cross-references MUID:91355899; PMID:2103468 !$#accession S12798 !'##molecule_type DNA !'##residues 1-475 ##label HIP !'##cross-references EMBL:X52937; NID:g12122; PIDN:CAA37107.1; !1PID:g12123 COMMENT In addition to Lys-201, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. GENETICS !$#genome chloroplast FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; magnesium; monooxygenase; !1photorespiration; photosynthesis FEATURE !$3-475 #product ribulose-bisphosphate carboxylase large !8chain #status predicted #label MAT\ !$175,334 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$201 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$203 #binding_site magnesium (Asp) #status predicted SUMMARY #length 475 #molecular-weight 52727 #checksum 7209 SEQUENCE /// ENTRY RKKHLG #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain precursor - Japanese larch chloroplast ORGANISM #formal_name chloroplast Pseudolarix kaempferi #common_name Japanese larch DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS S14648 REFERENCE S14648 !$#authors Doerksen, A.H.; Strauss, S.; Price, R. !$#submission submitted to the EMBL Data Library, March 1991 !$#accession S14648 !'##molecule_type DNA !'##residues 1-475 ##label DOE !'##cross-references EMBL:X58782; NID:g14166; PIDN:CAA41587.1; !1PID:g14167 COMMENT In addition to Lys-201, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. GENETICS !$#genome chloroplast FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; magnesium; monooxygenase; !1photorespiration; photosynthesis FEATURE !$3-475 #product ribulose-bisphosphate carboxylase large !8chain #status predicted #label MAT\ !$175,334 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$201 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$203 #binding_site magnesium (Asp) #status predicted SUMMARY #length 475 #molecular-weight 52768 #checksum 7061 SEQUENCE /// ENTRY RKKHLR #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain precursor - red fir chloroplast ORGANISM #formal_name chloroplast Abies magnifica #common_name red fir DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS S14869 REFERENCE S14648 !$#authors Doerksen, A.H.; Strauss, S.; Price, R. !$#submission submitted to the EMBL Data Library, March 1991 !$#accession S14869 !'##molecule_type DNA !'##residues 1-475 ##label DOE !'##cross-references EMBL:X58391; NID:g16030; PIDN:CAA41280.1; !1PID:g16031 COMMENT In addition to Lys-201, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. GENETICS !$#genome chloroplast FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; magnesium; monooxygenase; !1photorespiration; photosynthesis FEATURE !$3-475 #product ribulose-bisphosphate carboxylase large !8chain #status predicted #label MAT\ !$175,334 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$201 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$203 #binding_site magnesium (Asp) #status predicted SUMMARY #length 475 #molecular-weight 52723 #checksum 6942 SEQUENCE /// ENTRY RKSZLN #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain precursor - pinyon chloroplast ORGANISM #formal_name chloroplast Pinus edulis #common_name pinyon DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS H46161; S15490 REFERENCE A46161 !$#authors Bousquet, J.; Strauss, S.H.; Doerksen, A.H.; Price, R.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:7844-7848 !$#title Extensive variation in evolutionary rate of rbcL gene !1sequences among seed plants. !$#cross-references MUID:92366559; PMID:1502205 !$#accession H46161 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-475 ##label BOU !'##cross-references EMBL:X58137; NID:g12095; PIDN:CAA41145.1; !1PID:g12096 COMMENT In addition to Lys-201, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. GENETICS !$#gene rbcL !$#genome chloroplast FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; magnesium; monooxygenase; !1photorespiration; photosynthesis FEATURE !$3-475 #product ribulose-bisphosphate carboxylase large !8chain #status predicted #label MAT\ !$175,334 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$201 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$203 #binding_site magnesium (Asp) #status predicted SUMMARY #length 475 #molecular-weight 52696 #checksum 5712 SEQUENCE /// ENTRY RKSZLH #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain precursor - Himalayan white pine chloroplast ORGANISM #formal_name chloroplast Pinus griffithii #common_name Himalayan white pine DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS C46161; S15491 REFERENCE A46161 !$#authors Bousquet, J.; Strauss, S.H.; Doerksen, A.H.; Price, R.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:7844-7848 !$#title Extensive variation in evolutionary rate of rbcL gene !1sequences among seed plants. !$#cross-references MUID:92366559; PMID:1502205 !$#accession C46161 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-475 ##label BOU !'##cross-references EMBL:X58131; NID:g12099; PIDN:CAA41139.1; !1PID:g12100 COMMENT In addition to Lys-201, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. GENETICS !$#gene rbcL !$#genome chloroplast FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; magnesium; monooxygenase; !1photorespiration; photosynthesis FEATURE !$3-475 #product ribulose-bisphosphate carboxylase large !8chain #status predicted #label MAT\ !$175,334 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$201 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$203 #binding_site magnesium (Asp) #status predicted SUMMARY #length 475 #molecular-weight 52656 #checksum 5365 SEQUENCE /// ENTRY RKSZLA #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain precursor - African fern pine chloroplast ORGANISM #formal_name chloroplast Podocarpus gracilior #common_name African fern pine DATE 30-Sep-1992 #sequence_revision 23-Mar-1995 #text_change 18-Jun-1999 ACCESSIONS G46161; S15492 REFERENCE A46161 !$#authors Bousquet, J.; Strauss, S.H.; Doerksen, A.H.; Price, R.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:7844-7848 !$#title Extensive variation in evolutionary rate of rbcL gene !1sequences among seed plants. !$#cross-references MUID:92366559; PMID:1502205 !$#accession G46161 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-475 ##label BOU !'##cross-references GB:X58135; NID:g12097; PIDN:CAA41143.1; PID:g12098 COMMENT In addition to Lys-201, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. GENETICS !$#gene rbcL !$#genome chloroplast FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; magnesium; monooxygenase; !1photorespiration; photosynthesis FEATURE !$3-475 #product ribulose-bisphosphate carboxylase large !8chain #status predicted #label MAT\ !$175,334 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$201 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$203 #binding_site magnesium (Asp) #status predicted SUMMARY #length 475 #molecular-weight 52663 #checksum 6233 SEQUENCE /// ENTRY RKSZLP #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain precursor - pine (Pinus longaeva) chloroplast ORGANISM #formal_name chloroplast Pinus longaeva #common_name pine DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS D46161; S15493 REFERENCE A46161 !$#authors Bousquet, J.; Strauss, S.H.; Doerksen, A.H.; Price, R.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:7844-7848 !$#title Extensive variation in evolutionary rate of rbcL gene !1sequences among seed plants. !$#cross-references MUID:92366559; PMID:1502205 !$#accession D46161 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-475 ##label BOU !'##cross-references EMBL:X58132; NID:g12113; PIDN:CAA41140.1; !1PID:g12114 COMMENT In addition to Lys-201, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. GENETICS !$#gene rbcL !$#genome chloroplast FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; magnesium; monooxygenase; !1photorespiration; photosynthesis FEATURE !$3-475 #product ribulose-bisphosphate carboxylase large !8chain #status predicted #label MAT\ !$175,334 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$201 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$203 #binding_site magnesium (Asp) #status predicted SUMMARY #length 475 #molecular-weight 52749 #checksum 5804 SEQUENCE /// ENTRY RKSZLI #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain precursor - Italian stone pine chloroplast ORGANISM #formal_name chloroplast Pinus pinea #common_name Italian stone pine DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS E46161; S15495 REFERENCE A46161 !$#authors Bousquet, J.; Strauss, S.H.; Doerksen, A.H.; Price, R.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:7844-7848 !$#title Extensive variation in evolutionary rate of rbcL gene !1sequences among seed plants. !$#cross-references MUID:92366559; PMID:1502205 !$#accession E46161 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-475 ##label BOU !'##cross-references EMBL:X58133; NID:g12128; PIDN:CAA41141.1; !1PID:g12129 COMMENT In addition to Lys-201, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. GENETICS !$#gene rbcL !$#genome chloroplast FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; magnesium; monooxygenase; !1photorespiration; photosynthesis FEATURE !$3-475 #product ribulose-bisphosphate carboxylase large !8chain #status predicted #label MAT\ !$175,334 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$201 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$203 #binding_site magnesium (Asp) #status predicted SUMMARY #length 475 #molecular-weight 52742 #checksum 6412 SEQUENCE /// ENTRY RKSZLM #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain precursor - Monterey pine chloroplast ORGANISM #formal_name chloroplast Pinus radiata #common_name Monterey pine DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS F46161; S15496 REFERENCE A46161 !$#authors Bousquet, J.; Strauss, S.H.; Doerksen, A.H.; Price, R.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:7844-7848 !$#title Extensive variation in evolutionary rate of rbcL gene !1sequences among seed plants. !$#cross-references MUID:92366559; PMID:1502205 !$#accession F46161 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-475 ##label BOU !'##cross-references EMBL:X58134; NID:g12132; PIDN:CAA41142.1; !1PID:g12133 COMMENT In addition to Lys-201, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. GENETICS !$#gene rbcL !$#genome chloroplast FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; magnesium; monooxygenase; !1photorespiration; photosynthesis FEATURE !$3-475 #product ribulose-bisphosphate carboxylase large !8chain #status predicted #label MAT\ !$175,334 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$201 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$203 #binding_site magnesium (Asp) #status predicted SUMMARY #length 475 #molecular-weight 52762 #checksum 5588 SEQUENCE /// ENTRY RKKHLC #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain precursor - deodar chloroplast ORGANISM #formal_name chloroplast Cedrus deodara #common_name deodar DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS S19215 REFERENCE S19215 !$#authors Doerksen, A.; Strauss, S.; Price, R. !$#submission submitted to the EMBL Data Library, January 1992 !$#accession S19215 !'##molecule_type DNA !'##residues 1-475 ##label DOE !'##cross-references EMBL:X63662; NID:g11295; PIDN:CAA45202.1; !1PID:g11296 COMMENT In addition to Lys-201, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. GENETICS !$#genome chloroplast FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; magnesium; monooxygenase; !1photorespiration; photosynthesis FEATURE !$3-475 #product ribulose-bisphosphate carboxylase large !8chain #status predicted #label MAT\ !$175,334 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$201 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$203 #binding_site magnesium (Asp) #status predicted SUMMARY #length 475 #molecular-weight 52658 #checksum 7047 SEQUENCE /// ENTRY RKKHLW #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain precursor - western larch chloroplast ORGANISM #formal_name chloroplast Larix occidentalis #common_name western larch DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS S19217 REFERENCE S19215 !$#authors Doerksen, A.; Strauss, S.; Price, R. !$#submission submitted to the EMBL Data Library, January 1992 !$#accession S19217 !'##molecule_type DNA !'##residues 1-475 ##label DOE !'##cross-references EMBL:X63663; NID:g12618; PIDN:CAA45203.1; !1PID:g12619 COMMENT In addition to Lys-201, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. GENETICS !$#genome chloroplast FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; magnesium; monooxygenase; !1photorespiration; photosynthesis FEATURE !$3-475 #product ribulose-bisphosphate carboxylase large !8chain #status predicted #label MAT\ !$175,334 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$201 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$203 #binding_site magnesium (Asp) #status predicted SUMMARY #length 475 #molecular-weight 52727 #checksum 7209 SEQUENCE /// ENTRY RKKHLK #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain precursor - Krempf's pine chloroplast ORGANISM #formal_name chloroplast Pinus krempfii #common_name Krempf's pine DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS S19221 REFERENCE S19215 !$#authors Doerksen, A.; Strauss, S.; Price, R. !$#submission submitted to the EMBL Data Library, January 1992 !$#accession S19221 !'##molecule_type DNA !'##residues 1-475 ##label DOE !'##cross-references EMBL:X63665; NID:g14168; PIDN:CAA45205.1; !1PID:g14169 COMMENT In addition to Lys-201, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. GENETICS !$#genome chloroplast FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; magnesium; monooxygenase; !1photorespiration; photosynthesis FEATURE !$3-475 #product ribulose-bisphosphate carboxylase large !8chain #status predicted #label MAT\ !$175,334 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$201 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$203 #binding_site magnesium (Asp) #status predicted SUMMARY #length 475 #molecular-weight 52641 #checksum 5149 SEQUENCE /// ENTRY RKJQLK #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain precursor - Sitka spruce chloroplast ORGANISM #formal_name chloroplast Picea sitchensis #common_name Sitka spruce DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS S19222 REFERENCE S19215 !$#authors Doerksen, A.; Strauss, S.; Price, R. !$#submission submitted to the EMBL Data Library, January 1992 !$#accession S19222 !'##molecule_type DNA !'##residues 1-475 ##label DOE !'##cross-references EMBL:X63660; NID:g14202; PIDN:CAA45200.1; !1PID:g14203 COMMENT In addition to Lys-201, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. GENETICS !$#genome chloroplast FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; magnesium; monooxygenase; !1photorespiration; photosynthesis FEATURE !$3-475 #product ribulose-bisphosphate carboxylase large !8chain #status predicted #label MAT\ !$175,334 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$201 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$203 #binding_site magnesium (Asp) #status predicted SUMMARY #length 475 #molecular-weight 52679 #checksum 6624 SEQUENCE /// ENTRY RKJQLC #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain precursor - Colorado spruce chloroplast ORGANISM #formal_name chloroplast Picea pungens #common_name Colorado spruce DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS S15494 REFERENCE S15490 !$#authors Doerksen, A.; Strauss, S.; Price, R. !$#submission submitted to the EMBL Data Library, March 1991 !$#accession S15494 !'##molecule_type DNA !'##residues 1-475 ##label DOE !'##cross-references EMBL:X58136; NID:g12126; PIDN:CAA41144.1; !1PID:g12127 COMMENT In addition to Lys-201, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. GENETICS !$#genome chloroplast FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; magnesium; monooxygenase; !1photorespiration; photosynthesis FEATURE !$3-475 #product ribulose-bisphosphate carboxylase large !8chain #status predicted #label MAT\ !$175,334 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$201 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$203 #binding_site magnesium (Asp) #status predicted SUMMARY #length 475 #molecular-weight 52591 #checksum 5368 SEQUENCE /// ENTRY RKSZLX #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain precursor - foxtail pine chloroplast ORGANISM #formal_name chloroplast Pinus balfouriana #common_name foxtail pine DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS S19219 REFERENCE S19215 !$#authors Doerksen, A.; Strauss, S.; Price, R. !$#submission submitted to the EMBL Data Library, January 1992 !$#accession S19219 !'##molecule_type DNA !'##residues 1-475 ##label DOE !'##cross-references EMBL:X63661; NID:g14154; PIDN:CAA45201.1; !1PID:g14155 COMMENT In addition to Lys-201, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. GENETICS !$#genome chloroplast FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; magnesium; monooxygenase; !1photorespiration; photosynthesis FEATURE !$3-475 #product ribulose-bisphosphate carboxylase large !8chain #status predicted #label MAT\ !$175,334 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$201 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$203 #binding_site magnesium (Asp) #status predicted SUMMARY #length 475 #molecular-weight 52713 #checksum 4971 SEQUENCE /// ENTRY RKFNLT #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain precursor - turnip fern chloroplast ORGANISM #formal_name chloroplast Angiopteris lygodiifolia #common_name turnip fern DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 18-Jun-1999 ACCESSIONS S19229 REFERENCE S19228 !$#authors Yoshinaga, K.; Kubota, Y.; Ishii, T.; Wada, K. !$#journal Plant Mol. Biol. (1992) 18:79-82 !$#title Nucleotide sequence of atpB, rbcL, trnR, dedB and psaI !1chloroplast genes from a fern Angiopteris lygodiifolia: a !1possible emergence of Spermatophyta lineage before the !1separation of Bryophyta and Pteridophyta. !$#cross-references MUID:92119238; PMID:1731980 !$#accession S19229 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-475 ##label YOS !'##cross-references EMBL:X58429; NID:g11189; PIDN:CAA41332.1; !1PID:g11191 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1March 1991 GENETICS !$#gene rbcL !$#genome chloroplast FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; magnesium; monooxygenase; !1photorespiration; photosynthesis FEATURE !$3-475 #product ribulose-bisphosphate carboxylase large !8chain #status predicted #label MAT\ !$175,334 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$201 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$203 #binding_site magnesium (Asp) #status predicted SUMMARY #length 475 #molecular-weight 52772 #checksum 5791 SEQUENCE /// ENTRY RKZML #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain precursor - maize chloroplast ORGANISM #formal_name chloroplast Zea mays #common_name maize DATE 29-Jun-1981 #sequence_revision 23-Oct-1981 #text_change 18-Jun-1999 ACCESSIONS A01093 REFERENCE A01093 !$#authors McIntosh, L.; Poulsen, C.; Bogorad, L. !$#journal Nature (1980) 288:556-560 !$#title Chloroplast gene sequence for the large subunit of ribulose !1bisphosphatecarboxylase of maize. !$#accession A01093 !'##molecule_type DNA !'##residues 1-475 ##label MCI !'##cross-references GB:J01423; NID:g342623; PIDN:CAA23474.1; !1PID:g342624; GB:V00171; NID:g12394; PID:g12395 COMMENT In addition to Lys-202, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. GENETICS !$#genome chloroplast FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; magnesium; monooxygenase; !1photorespiration; photosynthesis FEATURE !$3-475 #product ribulose-bisphosphate carboxylase large !8chain #status predicted #label MAT\ !$176,334 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$202 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$204 #binding_site magnesium (Asp) #status predicted SUMMARY #length 475 #molecular-weight 52500 #checksum 5423 SEQUENCE /// ENTRY RKSPL #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain precursor - spinach chloroplast ORGANISM #formal_name chloroplast Spinacia oleracea #common_name spinach DATE 08-Oct-1981 #sequence_revision 23-Oct-1981 #text_change 21-Jul-2000 ACCESSIONS A01094; A32395 REFERENCE A93730 !$#authors Zurawski, G.; Perrot, B.; Bottomley, W.; Whitfeld, P.R. !$#journal Nucleic Acids Res. (1981) 9:3251-3270 !$#title The structure of the gene for the large subunit of ribulose !11,5-bisphosphate carboxylase from spinach chloroplast DNA. !$#cross-references MUID:82014906; PMID:6269077 !$#accession A01094 !'##molecule_type DNA !'##residues 1-475 ##label ZUR !'##cross-references GB:J01443; GB:V00168; NID:g12290; PIDN:CAA23473.1; !1PID:g12291 !'##note the authors translated the codon AAT for residue 287 as Ile REFERENCE A32395 !$#authors Houtz, R.L.; Stults, J.T.; Mulligan, R.M.; Tolbert, N.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:1855-1859 !$#title Post-translational modifications in the large subunit of !1ribulose bisphosphate carboxylase/oxygenase. !$#cross-references MUID:89184526; PMID:2928307 !$#accession A32395 !'##molecule_type protein !'##residues 3-21 ##label HOU REFERENCE A90208 !$#authors Stringer, C.D.; Hartman, F.C. !$#journal Biochem. Biophys. Res. Commun. (1978) 80:1043-1048 !$#title Sequences of two active-site peptides from spinach !1ribulosebisphosphate carboxylase/oxygenase. !$#cross-references MUID:78144263; PMID:637859 !$#contents annotation; active site REFERENCE A94606 !$#authors Lorimer, G.H. !$#submission submitted to the Atlas, October 1982 !$#contents annotation; activation COMMENT In addition to Lys-201, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. GENETICS !$#genome chloroplast FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS acetylated amino end; Calvin cycle; carbon dioxide fixation; !1carbon-carbon lyase; carboxy-lyase; chloroplast; magnesium; !1monooxygenase; photorespiration; photosynthesis FEATURE !$3-475 #product ribulose-bisphosphate carboxylase large !8chain #status experimental #label MAT1\ !$3 #modified_site acetylated amino end (Pro) (in mature !8form) #status experimental\ !$14 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8absent\ !$175,334 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$201 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status experimental\ !$203 #binding_site magnesium (Asp) #status predicted SUMMARY #length 475 #molecular-weight 52740 #checksum 9015 SEQUENCE /// ENTRY RKUBL #type fragment TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain - Atriplex patula chloroplast (fragment) ORGANISM #formal_name chloroplast Atriplex patula DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 18-Jun-1999 ACCESSIONS E34921; S11745 REFERENCE A34921 !$#authors Hudson, G.S.; Mahon, J.D.; Anderson, P.A.; Gibbs, M.J.; !1Badger, M.R.; Andrews, T.J.; Whitfeld, P.R. !$#journal J. Biol. Chem. (1990) 265:808-814 !$#title Comparisons of rbcL genes for the large subunit of !1ribulose-bisphosphate carboxylase from closely related C-3 !1and C-4 plant species. !$#cross-references MUID:90110139; PMID:2295620 !$#accession E34921 !'##status preliminary !'##molecule_type DNA !'##residues 1-469 ##label HUD !'##cross-references GB:X15925; NID:g11320; PIDN:CAA34062.1; PID:g11321; !1GB:M33794 !'##note submitted to the EMBL Data Library, July 1989 COMMENT In addition to Lys-201, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. GENETICS !$#gene rbcL !$#genome chloroplast FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; magnesium; monooxygenase; !1photorespiration; photosynthesis FEATURE !$3-469 #product ribulose-bisphosphate carboxylase large !8chain (fragment) #status predicted #label MAT\ !$175,334 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$201 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$203 #binding_site magnesium (Asp) #status predicted SUMMARY #length 469 #checksum 432 SEQUENCE /// ENTRY RKMHLP #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain precursor - prince's feather chloroplast ORGANISM #formal_name chloroplast Amaranthus hybridus var. erythrostachys #common_name prince's feather DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS S15931; S08681 REFERENCE S15931 !$#authors Michalowski, C.B.; Bohnert, H.J.; Klessig, D.F.; Berry, J.O. !$#journal Nucleic Acids Res. (1990) 18:2187 !$#title Nucleotide sequence of rbcL from Amaranthus hypochondriacus !1chloroplasts. !$#cross-references MUID:90245680; PMID:2336404 !$#accession S15931 !'##molecule_type DNA !'##residues 1-475 ##label MIC !'##cross-references EMBL:X51964; NID:g11313; PIDN:CAA36223.1; !1PID:g11314 !'##note the authors translated the codon TTA for residue 105 as Arg COMMENT In addition to Lys-201, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. GENETICS !$#gene rbcL !$#genome chloroplast FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; magnesium; monooxygenase; !1photorespiration; photosynthesis FEATURE !$3-475 #product ribulose-bisphosphate carboxylase large !8chain #status predicted #label MAT\ !$175,334 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$201 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$203 #binding_site magnesium (Asp) #status predicted SUMMARY #length 475 #molecular-weight 52593 #checksum 8567 SEQUENCE /// ENTRY RKAALC #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain precursor - alfalfa chloroplast ORGANISM #formal_name chloroplast Medicago sativa #common_name alfalfa DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS A25578 REFERENCE A25578 !$#authors Aldrich, J.; Cherney, B.; Merlin, E.; Palmer, J. !$#journal Nucleic Acids Res. (1986) 14:9535 !$#title Sequence of the rbcL gene for the large subunit of ribulose !1bisphosphate carboxylase-oxygenase from alfalfa. !$#cross-references MUID:87091586; PMID:3797252 !$#accession A25578 !'##molecule_type DNA !'##residues 1-474 ##label ALD !'##cross-references GB:X04975; NID:g11737; PIDN:CAA28648.1; PID:g11738 COMMENT In addition to Lys-201, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. GENETICS !$#gene rbcL !$#genome chloroplast FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; magnesium; monooxygenase; !1photorespiration; photosynthesis FEATURE !$3-474 #product ribulose-bisphosphate carboxylase large !8chain #status predicted #label MAT\ !$175,334 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$201 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$203 #binding_site magnesium (Asp) #status predicted SUMMARY #length 474 #molecular-weight 52625 #checksum 2374 SEQUENCE /// ENTRY RKFPLP #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain - Flaveria pringlei chloroplast ORGANISM #formal_name chloroplast Flaveria pringlei DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 18-Jun-1999 ACCESSIONS C34921; S11751 REFERENCE A34921 !$#authors Hudson, G.S.; Mahon, J.D.; Anderson, P.A.; Gibbs, M.J.; !1Badger, M.R.; Andrews, T.J.; Whitfeld, P.R. !$#journal J. Biol. Chem. (1990) 265:808-814 !$#title Comparisons of rbcL genes for the large subunit of !1ribulose-bisphosphate carboxylase from closely related C-3 !1and C-4 plant species. !$#cross-references MUID:90110139; PMID:2295620 !$#accession C34921 !'##molecule_type DNA !'##residues 1-485 ##label HUD !'##cross-references EMBL:X55829; GB:X15922; NID:g11556; !1PIDN:CAA39355.1; PID:g11557 !'##note X55829 submitted to the EMBL Data Library, July 1989 COMMENT In addition to Lys-201, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. GENETICS !$#gene rbcL !$#genome chloroplast FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; magnesium; monooxygenase; !1photorespiration; photosynthesis FEATURE !$3-485 #product ribulose-bisphosphate carboxylase large !8chain #status predicted #label MAT1\ !$175,334 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$201 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$203 #binding_site magnesium (Asp) #status predicted SUMMARY #length 485 #molecular-weight 53875 #checksum 4981 SEQUENCE /// ENTRY RKFPLB #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain - Flaveria bidentis chloroplast ORGANISM #formal_name chloroplast Flaveria bidentis DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 18-Jun-1999 ACCESSIONS D34921; S11750 REFERENCE A34921 !$#authors Hudson, G.S.; Mahon, J.D.; Anderson, P.A.; Gibbs, M.J.; !1Badger, M.R.; Andrews, T.J.; Whitfeld, P.R. !$#journal J. Biol. Chem. (1990) 265:808-814 !$#title Comparisons of rbcL genes for the large subunit of !1ribulose-bisphosphate carboxylase from closely related C-3 !1and C-4 plant species. !$#cross-references MUID:90110139; PMID:2295620 !$#accession D34921 !'##molecule_type DNA !'##residues 1-485 ##label HUD !'##cross-references EMBL:X55830; NID:g11552; PIDN:CAA39356.1; !1PID:g11553; GB:M33793; GB:X15923 !'##note submitted to the EMBL Data Library, July 1989 COMMENT In addition to Lys-201, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. GENETICS !$#gene rbcL !$#genome chloroplast FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; magnesium; monooxygenase; !1photorespiration; photosynthesis FEATURE !$3-485 #product ribulose-bisphosphate carboxylase large !8chain #status predicted #label MAT\ !$175,334 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$201 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$203 #binding_site magnesium (Asp) #status predicted SUMMARY #length 485 #molecular-weight 53813 #checksum 4264 SEQUENCE /// ENTRY RKNTL #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain precursor - common tobacco chloroplast ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 13-Jun-1983 #sequence_revision 30-Sep-1991 #text_change 21-May-1999 ACCESSIONS A01095; S14945; C32395; S14927 REFERENCE A01095 !$#authors Shinozaki, K.; Sugiura, M. !$#journal Gene (1982) 20:91-102 !$#title The nucleotide sequence of the tobacco chloroplast gene for !1the large subunit of ribulose-1,5-bisphosphate carboxylase/ !1oxygenase. !$#cross-references MUID:83133301; PMID:7160620 !$#accession A01095 !'##molecule_type DNA !'##residues 1-376,'E',378-477 ##label SHI !'##cross-references EMBL:J01450; NID:g343510; PID:g552961 REFERENCE S14945 !$#authors Amiri, I.; Salnikow, J.; Vater, J. !$#journal Biochim. Biophys. Acta (1984) 784:116-123 !$#title Amino-acid sequence of the large subunit of !1D-ribulosebisphosphate carboxylase/oxygenase from Nicotiana !1tabacum. !$#accession S14945 !'##molecule_type protein !'##residues 5-283,'G',285-477 ##label AMI !'##note 394-Val and 405-Met were also found !'##note two forms of this protein are found; one corresponds to !1residues 5-477 and the other, to residues 15-477 REFERENCE A32395 !$#authors Houtz, R.L.; Stults, J.T.; Mulligan, R.M.; Tolbert, N.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:1855-1859 !$#title Post-translational modifications in the large subunit of !1ribulose bisphosphate carboxylase/oxygenase. !$#cross-references MUID:89184526; PMID:2928307 !$#accession C32395 !'##molecule_type protein !'##residues 3-21 ##label HOU COMMENT In addition to Lys-201, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. GENETICS !$#gene rbcL !$#genome chloroplast FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS acetylated amino end; Calvin cycle; carbon dioxide fixation; !1carbon-carbon lyase; carboxy-lyase; chloroplast; magnesium; !1methylated amino acid; monooxygenase; photorespiration; !1photosynthesis FEATURE !$3-477 #product ribulose-bisphosphate carboxylase large !8chain (long form) #status experimental #label MAT\ !$5-477 #product ribulose-bisphosphate carboxylase large !8chain (medium form) #status experimental #label MAT1\ !$15-477 #product ribulose-bisphosphate carboxylase large !8chain (short form) #status experimental #label MAT2\ !$3 #modified_site acetylated amino end (Pro) (in mature !8form) #status experimental\ !$14 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental\ !$175,334 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$201 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$203 #binding_site magnesium (Asp) #status predicted SUMMARY #length 477 #molecular-weight 52898 #checksum 9540 SEQUENCE /// ENTRY RKNTLO #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain precursor - tobacco (Nicotiana otophora) chloroplast ORGANISM #formal_name chloroplast Nicotiana otophora #common_name tobacco DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 18-Jun-1999 ACCESSIONS S07402 REFERENCE S07402 !$#authors Lin, C.M.; Liu, Z.Q.; Kung, S.D. !$#journal Plant Mol. Biol. (1986) 6:81-87 !$#title Nicotiana chloroplast genome: X. Correlation between the DNA !1sequences and the isoelectric focusing patterns of the LS of !1Rubisco. !$#accession S07402 !'##status translation not shown !'##molecule_type DNA !'##residues 1-477 ##label LIN !'##cross-references EMBL:M16867; NID:g343506; PIDN:AAA84692.1; !1PID:g552959 COMMENT In addition to Lys-201, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. GENETICS !$#gene rbcL !$#genome chloroplast FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; magnesium; monooxygenase; !1photorespiration; photosynthesis FEATURE !$3-477 #product ribulose-bisphosphate carboxylase large !8chain #status predicted #label MAT\ !$175,334 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$201 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$203 #binding_site magnesium (Asp) #status predicted SUMMARY #length 477 #molecular-weight 52929 #checksum 9664 SEQUENCE /// ENTRY RKNTLA #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain precursor - acuminate tobacco chloroplast ORGANISM #formal_name chloroplast Nicotiana acuminata #common_name acuminate tobacco DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 18-Jun-1999 ACCESSIONS S07936 REFERENCE S07402 !$#authors Lin, C.M.; Liu, Z.Q.; Kung, S.D. !$#journal Plant Mol. Biol. (1986) 6:81-87 !$#title Nicotiana chloroplast genome: X. Correlation between the DNA !1sequences and the isoelectric focusing patterns of the LS of !1Rubisco. !$#accession S07936 !'##status translation not shown !'##molecule_type DNA !'##residues 1-477 ##label LIN !'##cross-references EMBL:M16896; NID:g343508; PIDN:AAA84693.1; !1PID:g552960 COMMENT In addition to Lys-201, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. GENETICS !$#gene rbcL !$#genome chloroplast FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; magnesium; monooxygenase; !1photorespiration; photosynthesis FEATURE !$3-477 #product ribulose-bisphosphate carboxylase large !8chain #status predicted #label MAT\ !$175,334 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$201 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$203 #binding_site magnesium (Asp) #status predicted SUMMARY #length 477 #molecular-weight 52941 #checksum 9414 SEQUENCE /// ENTRY RKPJLC #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain precursor - garden petunia chloroplast ORGANISM #formal_name chloroplast Petunia x hybrida #common_name garden petunia DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS A25577 REFERENCE A25577 !$#authors Aldrich, J.; Cherney, B.; Merlin, E.; Palmer, J. !$#journal Nucleic Acids Res. (1986) 14:9534 !$#title Sequence of the rbcL gene for the large subunit of ribulose !1bisphosphate carboxylase-oxygenase from petunia. !$#cross-references MUID:87091585; PMID:3467303 !$#accession A25577 !'##molecule_type DNA !'##residues 1-477 ##label ALD !'##cross-references GB:X04976; NID:g12105; PIDN:CAA28649.1; PID:g12106 COMMENT In addition to Lys-201, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. GENETICS !$#genome chloroplast FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; magnesium; monooxygenase; !1photorespiration; photosynthesis FEATURE !$3-477 #product ribulose-bisphosphate carboxylase large !8chain #status predicted #label MAT\ !$175,334 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$201 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$203 #binding_site magnesium (Asp) #status predicted SUMMARY #length 477 #molecular-weight 53033 #checksum 9210 SEQUENCE /// ENTRY RKIELP #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain precursor - common morning-glory chloroplast ORGANISM #formal_name chloroplast Ipomoea purpurea #common_name common morning-glory DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 18-Jun-1999 ACCESSIONS S20847 REFERENCE S20847 !$#authors Haberhausen, G.; Zetsche, K. !$#journal Plant Mol. Biol. (1992) 18:823-825 !$#title Nucleotide sequence of the rbcL gene and the intergenic !1promoter region between the divergently transcribed rbcL and !1atpB genes of Ipomoea purpurea (L.). !$#cross-references MUID:92216063; PMID:1532751 !$#accession S20847 !'##molecule_type DNA !'##residues 1-480 ##label HAB !'##cross-references EMBL:X60663; NID:g58379; PIDN:CAA43070.1; !1PID:g58380 GENETICS !$#gene rbcL !$#genome chloroplast FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; magnesium; monooxygenase; !1photorespiration; photosynthesis FEATURE !$3-480 #product ribulose-bisphosphate carboxylase large !8chain #status predicted #label MAT\ !$175,334 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$201 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$203 #binding_site magnesium (Asp) #status predicted SUMMARY #length 480 #molecular-weight 53387 #checksum 4790 SEQUENCE /// ENTRY RKRZL #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain precursor - rice chloroplast ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 18-Jun-1999 ACCESSIONS JQ0231; S05111; A93043 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0231 !'##molecule_type DNA !'##residues 1-477 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05111 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-477 ##label HIR !'##cross-references EMBL:X15901; NID:g11957; PIDN:CAA34004.1; !1PID:g11992 !'##experimental_source cv. Nihonbare REFERENCE A93043 !$#authors Nishizawa, Y.; Hirai, A. !$#journal Jpn. J. Genet. (1987) 62:389-395 !$#title Nucleotide sequence and expression of the gene for the large !1subunit of rice ribulose 1,5-bisphosphate carboxylase. !$#accession A93043 !'##molecule_type DNA !'##residues 1-420,'W',422-477 ##label NIS !'##cross-references DDBJ:D00207; NID:g344016; PIDN:BAA00147.1; !1PID:g344017 COMMENT The enzyme is composed of two chains, large (LS) and small !1(SS); the LS is encoded by a chloroplast gene, rbcL and the !1SS by a nuclear gene, rbcS. COMMENT The enzyme is one of the major proteins in plants and acts !1as a key enzyme in photosynthesis fixing CO2 in the Calvin !1cycle. COMMENT In addition to Lys-201, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. GENETICS !$#gene rbcL !$#map_position CP54095-55528 !$#genome chloroplast FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; magnesium; monooxygenase; !1photorespiration; photosynthesis FEATURE !$3-477 #product ribulose-bisphosphate carboxylase large !8chain #status predicted #label MAT\ !$175,334 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$201 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$203 #binding_site magnesium (Asp) #status predicted SUMMARY #length 477 #molecular-weight 52881 #checksum 9403 SEQUENCE /// ENTRY RKNULT #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain - Neurachne tenuifolia chloroplast ORGANISM #formal_name chloroplast Neurachne tenuifolia DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 18-Jun-1999 ACCESSIONS G34921; S11753 REFERENCE A34921 !$#authors Hudson, G.S.; Mahon, J.D.; Anderson, P.A.; Gibbs, M.J.; !1Badger, M.R.; Andrews, T.J.; Whitfeld, P.R. !$#journal J. Biol. Chem. (1990) 265:808-814 !$#title Comparisons of rbcL genes for the large subunit of !1ribulose-bisphosphate carboxylase from closely related C-3 !1and C-4 plant species. !$#cross-references MUID:90110139; PMID:2295620 !$#accession G34921 !'##molecule_type DNA !'##residues 1-478 ##label HUD !'##cross-references GB:X55827; NID:g11797; PIDN:CAA39353.1; PID:g11798; !1GB:M33796; GB:X15920 !'##note submitted to the EMBL Data Library, July 1989 COMMENT In addition to Lys-201, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. GENETICS !$#gene rbcL !$#genome chloroplast FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; magnesium; monooxygenase; !1photorespiration; photosynthesis FEATURE !$3-478 #product ribulose-bisphosphate carboxylase large !8chain #status predicted #label MAT\ !$175,334 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$201 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$203 #binding_site magnesium (Asp) #status predicted SUMMARY #length 478 #molecular-weight 52889 #checksum 9692 SEQUENCE /// ENTRY RKNULM #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain - Neurachne munroi chloroplast ORGANISM #formal_name chloroplast Neurachne munroi DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 18-Jun-1999 ACCESSIONS H34921; S11752 REFERENCE A34921 !$#authors Hudson, G.S.; Mahon, J.D.; Anderson, P.A.; Gibbs, M.J.; !1Badger, M.R.; Andrews, T.J.; Whitfeld, P.R. !$#journal J. Biol. Chem. (1990) 265:808-814 !$#title Comparisons of rbcL genes for the large subunit of !1ribulose-bisphosphate carboxylase from closely related C-3 !1and C-4 plant species. !$#cross-references MUID:90110139; PMID:2295620 !$#accession H34921 !'##molecule_type DNA !'##residues 1-478 ##label HUD !'##cross-references EMBL:X55828; NID:g11750; PIDN:CAA39354.1; !1PID:g11751 !'##note submitted to the EMBL Data Library, July 1989 COMMENT In addition to Lys-201, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. GENETICS !$#gene rbcL !$#genome chloroplast FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; magnesium; monooxygenase; !1photorespiration; photosynthesis FEATURE !$3-478 #product ribulose-bisphosphate carboxylase large !8chain #status predicted #label MAT\ !$175,334 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$201 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$203 #binding_site magnesium (Asp) #status predicted SUMMARY #length 478 #molecular-weight 52947 #checksum 1563 SEQUENCE /// ENTRY RKBHLC #type fragment TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain precursor - barley chloroplast (fragment) ORGANISM #formal_name chloroplast Hordeum vulgare #common_name barley DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS S08610 REFERENCE S07243 !$#authors Zurawski, G.; Clegg, M.T.; Brown, A.H.D. !$#journal Genetics (1984) 106:735-749 !$#title The nature of nucleotide sequence divergence between barley !1and maize chloroplast DNA. !$#accession S08610 !'##molecule_type DNA !'##residues 1-426 ##label VAL !'##cross-references EMBL:X00630; NID:g11585; PIDN:CAA25265.1; !1PID:g11587 COMMENT In addition to Lys-201, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. GENETICS !$#genome chloroplast FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; magnesium; monooxygenase; !1photorespiration; photosynthesis FEATURE !$3-426 #product ribulose-bisphosphate carboxylase large !8chain (fragment) #status predicted #label MAT\ !$175,334 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$201 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$203 #binding_site magnesium (Asp) #status predicted SUMMARY #length 426 #checksum 7459 SEQUENCE /// ENTRY RKWTLC #type fragments TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain - wheat chloroplast (fragments) ORGANISM #formal_name chloroplast Triticum aestivum #common_name common wheat DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 23-Mar-2001 ACCESSIONS B32395; S17323 REFERENCE A32395 !$#authors Houtz, R.L.; Stults, J.T.; Mulligan, R.M.; Tolbert, N.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:1855-1859 !$#title Post-translational modifications in the large subunit of !1ribulose bisphosphate carboxylase/oxygenase. !$#cross-references MUID:89184526; PMID:2928307 !$#accession B32395 !'##molecule_type protein !'##residues 1-19 ##label HOU REFERENCE S17319 !$#authors Ogihara, Y.; Terachi, T.; Sasahuma, T. !$#submission submitted to the EMBL Data Library, August 1991 !$#description Molecular analysis of the hot spot region related to length !1mutations in wheat chloroplast DNAs I. Nucleotide divergence !1of genes and intergenic spaces regions located in the hot !1spot region. !$#accession S17323 !'##molecule_type DNA !'##residues 20-441 ##label OGI !'##cross-references EMBL:X62117; NID:g12343; PIDN:CAA44027.1; !1PID:g12344 COMMENT In addition to Lys-165, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. GENETICS !$#gene rbcL !$#genome chloroplast FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS acetylated amino end; Calvin cycle; carbon dioxide fixation; !1carbon-carbon lyase; carboxy-lyase; chloroplast; magnesium; !1monooxygenase; photorespiration; photosynthesis FEATURE !$1 #modified_site acetylated amino end (Pro) #status !8experimental\ !$12 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8absent\ !$139,298 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$165 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$167 #binding_site magnesium (Asp) #status predicted SUMMARY #length 441 #checksum 1007 SEQUENCE /// ENTRY RKPMLC #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain precursor - garden pea chloroplast ORGANISM #formal_name chloroplast Pisum sativum #common_name garden pea DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 21-May-1999 ACCESSIONS A24471 REFERENCE A24471 !$#authors Zurawski, G.; Whitfeld, P.R.; Bottomley, W. !$#journal Nucleic Acids Res. (1986) 14:3975 !$#title Sequence of the gene for the large subunit of ribulose 1, !15-bisphosphate carboxylase from pea chloroplasts. !$#cross-references MUID:86232636; PMID:3714502 !$#accession A24471 !'##molecule_type DNA !'##residues 1-475 ##label ZUR !'##cross-references GB:X03853 COMMENT In addition to Lys-201, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. GENETICS !$#gene rbcL !$#genome chloroplast FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; magnesium; monooxygenase; !1photorespiration; photosynthesis FEATURE !$3-475 #product ribulose-bisphosphate carboxylase large !8chain #status predicted #label MAT\ !$175,334 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$201 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$203 #binding_site magnesium (Asp) #status predicted SUMMARY #length 475 #molecular-weight 52763 #checksum 6530 SEQUENCE /// ENTRY RKCNLU #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain precursor - upland cotton chloroplast ORGANISM #formal_name chloroplast Gossypium hirsutum #common_name upland cotton DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 18-Jun-1999 ACCESSIONS S07582 REFERENCE S07582 !$#authors Gulov, M.K.; Ulmasov, T.N.; Aliev, K.A.; Andrianov, V.M.; !1Piruzian, E.S. !$#journal Nucleic Acids Res. (1990) 18:185 !$#title Nucleotide sequence of the chloroplast rbcL gene from cotton !1Gossypium hirsutum. !$#cross-references MUID:90174918; PMID:2308826 !$#accession S07582 !'##status translation not shown !'##molecule_type DNA !'##residues 1-475 ##label GUL !'##cross-references EMBL:X15886; NID:g11562; PIDN:CAA33896.1; !1PID:g11563 COMMENT In addition to Lys-201, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. GENETICS !$#gene rbcL !$#genome chloroplast FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; magnesium; monooxygenase; !1photorespiration; photosynthesis FEATURE !$3-475 #product ribulose-bisphosphate carboxylase large !8chain #status predicted #label MAT\ !$175,334 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$201 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$203 #binding_site magnesium (Asp) #status predicted SUMMARY #length 475 #molecular-weight 52770 #checksum 4774 SEQUENCE /// ENTRY RKLVL #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain precursor - liverwort (Marchantia polymorpha) chloroplast ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 18-Jun-1999 ACCESSIONS S01529; A01096 REFERENCE S01529 !$#authors Fukuzawa, H.; Kohchi, T.; Sano, T.; Shirai, H.; Umesono, K.; !1Inokuchi, H.; Ozeki, H.; Ohyama, K. !$#journal J. Mol. Biol. (1988) 203:333-351 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. III. Gene organization of the large !1single copy region from rbcL to trnI(CAU). !$#cross-references MUID:89068687; PMID:3199436 !$#accession S01529 !'##molecule_type DNA !'##residues 1-475 ##label FUK !'##cross-references GB:X04465; NID:g11640; PIDN:CAA28092.1; PID:g11680; !1GB:X01647 REFERENCE A00150 !$#authors Ohyama, K. !$#submission submitted to the EMBL Data Library, October 1986 !$#accession A01096 !'##molecule_type DNA !'##residues 1-475 ##label OHY !'##cross-references EMBL:X04465; NID:g11640; PIDN:CAA28092.1; !1PID:g11680 REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features COMMENT In addition to Lys-201, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. GENETICS !$#gene rbcL !$#genome chloroplast FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; magnesium; monooxygenase; !1photorespiration; photosynthesis FEATURE !$3-475 #product ribulose-bisphosphate carboxylase large !8chain #status predicted #label MAT\ !$175,334 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$201 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$203 #binding_site magnesium (Asp) #status predicted SUMMARY #length 475 #molecular-weight 52790 #checksum 7932 SEQUENCE /// ENTRY RKKLLP #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain precursor - Chlorella ellipsoidea chloroplast ORGANISM #formal_name chloroplast Chlorella ellipsoidea DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS A37257 REFERENCE JE0011 !$#authors Yoshinaga, K.; Ohta, T.; Suzuki, Y.; Sugiura, M. !$#journal Plant Mol. Biol. (1988) 10:245-250 !$#title Chlorella chloroplast DNA sequence containing a gene for the !1large subunit of ribulose-1,5-bisphosphate carboxylase/ !1oxygenase and a part of a possible gene for the beta' !1subunit of RNA polymerase. !$#accession A37257 !'##molecule_type DNA !'##residues 1-475 ##label YOS !'##cross-references GB:M20655; NID:g336510; PIDN:AAA84108.1; !1PID:g336512 !'##experimental_source strain Tamiya COMMENT In addition to Lys-201, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. GENETICS !$#gene rbcL !$#genome chloroplast FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; magnesium; monooxygenase; !1photorespiration; photosynthesis FEATURE !$3-475 #product ribulose-bisphosphate carboxylase large !8chain #status predicted #label MAT\ !$175,334 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$201 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$203 #binding_site magnesium (Asp) #status predicted SUMMARY #length 475 #molecular-weight 52568 #checksum 5085 SEQUENCE /// ENTRY RKKML #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain precursor - Chlamydomonas reinhardtii chloroplast ORGANISM #formal_name chloroplast Chlamydomonas reinhardtii DATE 13-Jun-1983 #sequence_revision 27-Jun-1983 #text_change 18-Jun-1999 ACCESSIONS A01097 REFERENCE A92892 !$#authors Dron, M.; Rahire, M.; Rochaix, J.D. !$#journal J. Mol. Biol. (1982) 162:775-793 !$#title Sequence of the chloroplast DNA region of Chlamydomonas !1reinhardtii containing the gene of the large subunit of !1ribulose bisphosphate carboxylase and parts of its flanking !1genes. !$#cross-references MUID:83189072; PMID:6302265 !$#accession A01097 !'##molecule_type DNA !'##residues 1-475 ##label DRO !'##cross-references GB:J01399; NID:g336683; PIDN:AAA84449.1; !1PID:g336684 COMMENT In addition to Lys-201, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. COMMENT Chlamydomonas reinhardtii is a unicellular green alga. GENETICS !$#genome chloroplast FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; magnesium; monooxygenase; !1photorespiration; photosynthesis FEATURE !$3-475 #product ribulose-bisphosphate carboxylase large !8chain #status predicted #label MAT\ !$175,334 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$201 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$203 #binding_site magnesium (Asp) #status predicted SUMMARY #length 475 #molecular-weight 52543 #checksum 4694 SEQUENCE /// ENTRY RKKMLM #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain precursor - Chlamydomonas moewusii chloroplast ORGANISM #formal_name chloroplast Chlamydomonas moewusii DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS A29497 REFERENCE A29497 !$#authors Yang, R.C.A.; Dove, M.; Seligy, V.L.; Lemieux, C.; Turmel, !1M.; Narang, S.A. !$#journal Gene (1986) 50:259-270 !$#title Complete nucleotide sequence and mRNA-mapping of the large !1subunit gene of ribulose-1,5-bisphosphate carboxylase/ !1oxygenase (Rubisco) from Chlamydomonas moewusii. !$#cross-references MUID:87219884; PMID:3034732 !$#accession A29497 !'##molecule_type DNA !'##residues 1-475 ##label YAN !'##cross-references GB:M15842; NID:g336671; PIDN:AAA84152.1; !1PID:g336672 COMMENT In addition to Lys-201, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. GENETICS !$#genome chloroplast FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; magnesium; monooxygenase; !1photorespiration; photosynthesis FEATURE !$3-475 #product ribulose-bisphosphate carboxylase large !8chain #status predicted #label MAT\ !$175,334 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$201 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$203 #binding_site magnesium (Asp) #status predicted SUMMARY #length 475 #molecular-weight 52453 #checksum 4004 SEQUENCE /// ENTRY RKBML #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain precursor - green alga (Bryopsis maxima) chloroplast ORGANISM #formal_name chloroplast Bryopsis maxima DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 18-Jun-1999 ACCESSIONS S17431; S20209 REFERENCE S17431 !$#authors Kono, M.; Satoh, H.; Okabe, Y.; Abe, Y.; Nakayama, K.; !1Okada, M. !$#journal Plant Mol. Biol. (1991) 17:505-508 !$#title Nucleotide sequence of the large subunit of ribulose-1, !15-bisphosphate carboxylase/oxygenase from the green alga !1Bryopsis maxima. !$#cross-references MUID:91355942; PMID:1884001 !$#accession S17431 !'##molecule_type DNA !'##residues 1-475 ##label KON !'##cross-references EMBL:X55877; NID:g11335; PIDN:CAA39361.1; !1PID:g11336 !$#accession S20209 !'##molecule_type protein !'##residues 2-8 ##label KO2 COMMENT In addition to Lys-201, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. GENETICS !$#gene rbcL !$#genome chloroplast !$#introns 268/3 FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; magnesium; monooxygenase; !1photorespiration; photosynthesis FEATURE !$2-475 #product ribulose-bisphosphate carboxylase large !8chain #status experimental #label MAT\ !$175,334 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$201 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$203 #binding_site magnesium (Asp) #status predicted SUMMARY #length 475 #molecular-weight 52631 #checksum 4536 SEQUENCE /// ENTRY RKEGL #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain precursor - Euglena gracilis chloroplast ORGANISM #formal_name chloroplast Euglena gracilis DATE 03-Aug-1984 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS A24556; A01098; S34909; S34542 REFERENCE A24556 !$#authors Gingrich, J.C.; Hallick, R.B. !$#journal J. Biol. Chem. (1985) 260:16162-16168 !$#title The Euglena gracilis chloroplast ribulose-1,5-bisphosphate !1carboxylase gene: II. The spliced mRNA and its product. !$#cross-references MUID:86059520; PMID:3934171 !$#accession A24556 !'##molecule_type mRNA !'##residues 1-475 ##label GIN !'##cross-references GB:M12109; NID:g336872; PIDN:AAA84453.1; !1PID:g336873; GB:M12110 REFERENCE A01098 !$#authors Koller, B.; Gingrich, J.C.; Stiegler, G.L.; Farley, M.A.; !1Delius, H.; Hallick, R.B. !$#journal Cell (1984) 36:545-553 !$#title Nine introns with conserved boundary sequences in the !1Euglena gracilis chloroplast ribulose-1,5-bisphosphate !1carboxylase gene. !$#cross-references MUID:84106859; PMID:6319030 !$#accession A01098 !'##molecule_type DNA !'##residues 84-102,'SLLIF',108-204 ##label KOL !'##cross-references GB:M15391; NID:g336874; PIDN:AAA84221.1; !1PID:g336875 REFERENCE S34862 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.R.; !1Monfort, A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#journal Nucleic Acids Res. (1993) 21:3537-3544 !$#title Complete sequence of Euglena gracilis chloroplast DNA. !$#cross-references MUID:93347989; PMID:8346031 !$#accession S34909 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-475 ##label HAL1 !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50123.1; !1PID:g415779 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1993 COMMENT In addition to Lys-201, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. GENETICS !$#gene rbcL !$#genome chloroplast !$#introns 15/3; 31/3; 50/3; 83/2; 204/3; 250/3; 268/2; 414/3; 430/3 FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; magnesium; monooxygenase; !1photorespiration; photosynthesis FEATURE !$3-475 #product ribulose-bisphosphate carboxylase large !8chain #status predicted #label MAT\ !$175,334 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$201 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$203 #binding_site magnesium (Asp) #status predicted SUMMARY #length 475 #molecular-weight 52608 #checksum 5351 SEQUENCE /// ENTRY RKAIL7 #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain - Anabaena sp. ORGANISM #formal_name Anabaena sp. DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 21-May-1999 ACCESSIONS A01099 REFERENCE A01099 !$#authors Curtis, S.E.; Haselkorn, R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:1835-1839 !$#title Isolation and sequence of the gene for the large subunit of !1ribulose-1,5-bisphosphate carboxylase from the !1cyanobacterium Anabaena 7120. !$#accession A01099 !'##molecule_type DNA !'##residues 1-476 ##label CUR !'##cross-references GB:J01540 !'##experimental_source PCC 7120 COMMENT Anabaena is a blue-green alga. COMMENT In addition to Lys-202, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. GENETICS !$#gene rbcA FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; magnesium; monooxygenase; photorespiration; !1photosynthesis FEATURE !$16-476 #product ribulose-bisphosphate carboxylase large !8chain #status predicted #label MAT\ !$176,335 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$202 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$204 #binding_site magnesium (Asp) #status predicted SUMMARY #length 476 #molecular-weight 53118 #checksum 3611 SEQUENCE /// ENTRY RKYCL #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain - Synechococcus sp. ORGANISM #formal_name Synechococcus sp. #note Synechococcus is a unicellular, coccoid blue-green alga; Synechococcus sp. PCC 6301 (ATCC 27144) was named Anacystis nidulans in other culture collections, e.g., CCAP, SAUG, and UTEX DATE 13-Jun-1983 #sequence_revision 14-Nov-1983 #text_change 18-Feb-2000 ACCESSIONS A90941; A93957; S45498; A01100 REFERENCE A90941 !$#authors Reichelt, B.Y.; Delaney, S.F. !$#journal DNA (1983) 2:121-129 !$#title The nucleotide sequence for the large subunit of ribulose 1, !15-bisphosphate carboxylase from a unicellular !1cyanobacterium, Synechococcus PCC6301. !$#cross-references MUID:83261206; PMID:6307620 !$#accession A90941 !'##molecule_type DNA !'##residues 1-472 ##label REI !'##cross-references GB:X03220; NID:g154598 !'##experimental_source PCC 6301 !'##note this translation is not annotated in GenBank entry !1synechococcus, release 116.0 REFERENCE A93957 !$#authors Shinozaki, K.; Yamada, C.; Takahata, N.; Sugiura, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:4050-4054 !$#title Molecular cloning and sequence analysis of the !1cyanobacterial gene for the large subunit of ribulose-1, !15-bisphosphate carboxylase/oxygenase. !$#accession A93957 !'##molecule_type DNA !'##residues 1-37,'RF',40-352,'A',354-472 ##label SHI !'##cross-references GB:X03220; NID:g38924; PIDN:CAA26972.1; PID:g38927 !'##note the authors translated the codon AAC for residue 160 as Thr REFERENCE S45498 !$#authors Read, B.A.; Tabita, F.R. !$#journal Arch. Biochem. Biophys. (1994) 312:210-218 !$#title High substrate specificity factor ribulose bisphosphate !1carboxylase/oxygenase from eukaryotic marine algae and !1properties of recombinant cyanobacterial rubisco containing !1"algal" residue modifications. !$#cross-references MUID:94304214; PMID:8031129 !$#accession S45498 !'##status preliminary !'##molecule_type protein !'##residues 333-342 ##label REA COMMENT In addition to Lys-198, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. GENETICS !$#gene rbcA FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; magnesium; monooxygenase; photorespiration; !1photosynthesis FEATURE !$16-472 #product ribulose-bisphosphate carboxylase large !8chain #status predicted #label MAT\ !$172,331 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$198 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$200 #binding_site magnesium (Asp) #status predicted SUMMARY #length 472 #molecular-weight 52425 #checksum 3320 SEQUENCE /// ENTRY RKJQLW #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain - western hemlock chloroplast ORGANISM #formal_name chloroplast Tsuga heterophylla #common_name western hemlock DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS S19223 REFERENCE S19215 !$#authors Doerksen, A.; Strauss, S.; Price, R. !$#submission submitted to the EMBL Data Library, January 1992 !$#accession S19223 !'##molecule_type DNA !'##residues 1-475 ##label DOE !'##cross-references EMBL:X63659; NID:g14273; PIDN:CAA45199.1; !1PID:g14274 COMMENT In addition to Lys-201, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. GENETICS !$#genome chloroplast FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; magnesium; monooxygenase; !1photorespiration; photosynthesis FEATURE !$175,334 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$201 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$203 #binding_site magnesium (Asp) #status predicted SUMMARY #length 475 #molecular-weight 52785 #checksum 7852 SEQUENCE /// ENTRY RKKHLE #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain - Keteleeria davidiana chloroplast ORGANISM #formal_name chloroplast Keteleeria davidiana DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS S19216 REFERENCE S19215 !$#authors Doerksen, A.; Strauss, S.; Price, R. !$#submission submitted to the EMBL Data Library, January 1992 !$#accession S19216 !'##molecule_type DNA !'##residues 1-475 ##label DOE !'##cross-references EMBL:X63664; NID:g12596; PIDN:CAA45204.1; !1PID:g12597 COMMENT In addition to Lys-201, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. GENETICS !$#genome chloroplast FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; magnesium; monooxygenase; !1photorespiration; photosynthesis FEATURE !$175,334 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$201 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$203 #binding_site magnesium (Asp) #status predicted SUMMARY #length 475 #molecular-weight 52668 #checksum 6393 SEQUENCE /// ENTRY RKKTLX #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain - Cyanophora paradoxa cyanelle ORGANISM #formal_name cyanelle Cyanophora paradoxa DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS S14117; T06928 REFERENCE S14117 !$#authors Valentin, K.; Zetsche, K. !$#journal Curr. Genet. (1990) 18:199-202 !$#title Nucleotide sequence of the gene for the large subunit of !1Rubisco from Cyanophora paradoxa - phylogenetic !1implications. !$#cross-references MUID:91064754; PMID:2123417 !$#accession S14117 !'##molecule_type DNA !'##residues 1-475 ##label VAL !'##cross-references EMBL:X53045; NID:g11394; PIDN:CAA37214.1; !1PID:g11395 REFERENCE Z15840 !$#authors Stirewalt, V.L.; Michalowski, C.B.; Luffelhardt, W.; !1Bohnert, H.J.; Bryant, D.A. !$#submission submitted to the EMBL Data Library, July 1995 !$#description Nucleotide sequence of the cyanelle genome from Cyanophora !1paradoxa. !$#accession T06928 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-246,'T',248-475 ##label STI !'##cross-references EMBL:U30821; NID:g1016083; PIDN:AAA81271.1; !1PID:g1016184 !'##experimental_source strain Pringsheim LB555 COMMENT In addition to Lys-201, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. GENETICS !$#gene rbcL !$#genome cyanelle FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid !$#pathway Calvin cycle CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; cyanelle; magnesium; monooxygenase; !1photorespiration; photosynthesis FEATURE !$175,334 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$201 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$203 #binding_site magnesium (Asp) #status predicted SUMMARY #length 475 #molecular-weight 52752 #checksum 4960 SEQUENCE /// ENTRY RKMWLX #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain - Prochlorothrix hollandica ORGANISM #formal_name Prochlorothrix hollandica DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS S16436 REFERENCE S16436 !$#authors Morden, C.W.; Golden, S.S. !$#journal J. Mol. Evol. (1991) 32:379-395 !$#title Sequence analysis and phylogenetic reconstruction of the !1genes encoding the large and small subunits of ribulose-1, !15-bisphosphate carboxylase/oxygenase from the chlorophyll !1b-containing prokaryote Prochlorothrix hollandica. !$#cross-references MUID:91251137; PMID:1904095 !$#accession S16436 !'##molecule_type DNA !'##residues 1-470 ##label MOR !'##cross-references EMBL:X57359; NID:g45542; PIDN:CAA40632.1; !1PID:g45543 COMMENT In addition to Lys-196, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; magnesium; monooxygenase; photorespiration; !1photosynthesis FEATURE !$170,329 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$196 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$198 #binding_site magnesium (Asp) #status predicted SUMMARY #length 470 #molecular-weight 52496 #checksum 2881 SEQUENCE /// ENTRY RKOALG #type fragment TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain - Aegilops squarrosa (fragment) ORGANISM #formal_name Aegilops squarrosa DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 23-Mar-2001 ACCESSIONS S17319 REFERENCE S17319 !$#authors Ogihara, Y.; Terachi, T.; Sasahuma, T. !$#submission submitted to the EMBL Data Library, August 1991 !$#description Molecular analysis of the hot spot region related to length !1mutations in wheat chloroplast DNAs I. Nucleotide divergence !1of genes and intergenic spaces regions located in the hot !1spot region. !$#accession S17319 !'##molecule_type DNA !'##residues 1-421 ##label OGI !'##cross-references EMBL:X62119; NID:g11324; PIDN:CAA44038.1; !1PID:g11325 COMMENT In addition to Lys-146, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; magnesium; monooxygenase; photorespiration; !1photosynthesis FEATURE !$120,279 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$146 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$148 #binding_site magnesium (Asp) #status predicted SUMMARY #length 421 #checksum 3856 SEQUENCE /// ENTRY RKITL #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain - euglenid (Astasia longa) plastid ORGANISM #formal_name plastid Astasia longa DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 21-May-1999 ACCESSIONS S11855 REFERENCE S11855 !$#authors Siemeister, G.; Hachtel, W. !$#journal Plant Mol. Biol. (1990) 14:825-833 !$#title Structure and expression of a gene encoding the large !1subunit of ribulose-1,5-bisphosphate carboxylase (rbcL) in !1the colourless euglenoid flagellate Astasia longa. !$#cross-references MUID:91346673; PMID:2102860 !$#accession S11855 !'##molecule_type DNA !'##residues 1-475 ##label PLA !'##cross-references EMBL:X16004 GENETICS !$#gene rbcL !$#genome plastid !$#start_codon ATA !$#introns 15/3; 31/3; 83/2; 204/3; 268/2; 414/3; 430/3 FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS carbon dioxide fixation; carbon-carbon lyase; carboxy-lyase; !1magnesium; monooxygenase; photorespiration; plastid FEATURE !$175,334 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$201 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$203 #binding_site magnesium (Asp) #status predicted SUMMARY #length 475 #molecular-weight 52825 #checksum 3637 SEQUENCE /// ENTRY RKBCLT #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain - Thiobacillus ferrooxidans ORGANISM #formal_name Thiobacillus ferrooxidans DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jun-2000 ACCESSIONS A41323; A49698 REFERENCE A41323 !$#authors Kusano, T.; Takeshima, T.; Inoue, C.; Sugawara, K. !$#journal J. Bacteriol. (1991) 173:7313-7323 !$#title Evidence for two sets of structural genes coding for !1ribulose bisphosphate carboxylase in Thiobacillus !1ferrooxidans. !$#cross-references MUID:92041630; PMID:1718945 !$#accession A41323 !'##molecule_type DNA !'##residues 1-473 ##label KUS !'##cross-references GB:D90113; NID:g217159; PIDN:BAA14141.1; !1PID:g217160 !'##note in addition to Lys-194, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation REFERENCE A49698 !$#authors Kusano, T.; Sugawara, K. !$#journal J. Bacteriol. (1993) 175:1019-1025 !$#title Specific binding of Thiobacillus ferrooxidans RbcR to the !1intergenic sequence between the rbc operon and the rbcR !1gene. !$#cross-references MUID:93163027; PMID:8432695 !$#accession A49698 !'##status preliminary !'##molecule_type DNA !'##residues 1-23 ##label KU2 !'##cross-references GB:D11141; NID:g287464; PIDN:BAA01916.1; !1PID:g287465 !'##experimental_source strain Fe1 !'##note sequence extracted from NCBI backbone (NCBIN:124697, !1NCBIP:124698) GENETICS !$#gene rbcL !$#note there are two identical copies of the gene for this protein FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; magnesium; monooxygenase; photorespiration; !1photosynthesis FEATURE !$168,327 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$194 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$196 #binding_site magnesium (Asp) #status predicted SUMMARY #length 473 #molecular-weight 52500 #checksum 4440 SEQUENCE /// ENTRY RKKRL1 #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain rbcA - Chromatium vinosum ORGANISM #formal_name Chromatium vinosum DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS A32303; B36095; A60823 REFERENCE A32303 !$#authors Viale, A.M.; Kobayashi, H.; Akazawa, T. !$#journal J. Bacteriol. (1989) 171:2391-2400 !$#title Expressed genes for plant-type ribulose 1,5-bisphosphate !1carboxylase/oxygenase in the photosynthetic bacterium !1Chromatium vinosum, which possesses two complete sets of the !1genes. !$#cross-references MUID:89213919; PMID:2708310 !$#accession A32303 !'##molecule_type DNA !'##residues 1-472 ##label VIA !'##cross-references GB:M26396; NID:g341476; PIDN:AAA23328.1; !1PID:g516602 REFERENCE A36095 !$#authors Viale, A.M.; Kobayashi, H.; Akazawa, T. !$#journal J. Biol. Chem. (1990) 265:18386-18392 !$#title Distinct properties of Escherichia coli products of !1plant-type ribulose-1,5-bisphosphate carboxylase/oxygenase !1directed by two sets of genes from the photosynthetic !1bacterium Chromatium vinosum. !$#cross-references MUID:91009333; PMID:2211708 !$#accession B36095 !'##molecule_type protein !'##residues 2-25 ##label VI2 REFERENCE A60823 !$#authors Torres-Ruiz, J.; McFadden, B.A. !$#journal Arch. Biochem. Biophys. (1987) 254:63-68 !$#title The nature of L-8 and L-8S-8 forms of ribulose bisphosphate !1carboxylase/oxygenase from Chromatium vinosum. !$#cross-references MUID:87212016; PMID:3579306 !$#accession A60823 !'##molecule_type protein !'##residues 'S',3-16,'Y',18-21 ##label TOR COMMENT There are two distinct sets of genes, rbcA-rbcB and !1rbcL-rbcS, for fully active ribulose-1,5-bisphosphate !1carboxylase in C. vinosum. The rbcL-rbcS set was barely !1expressed in the bacterium under standard photoautotrophic !1growth conditions. COMMENT This copy of the rubisco large chain gene is found in both !1form I (L-8,S-8) and form II (L subunits only). It is the !1predominant form in this organism. COMMENT In addition to Lys-193, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. GENETICS !$#gene rbcA FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; heterohexadecamer; magnesium; monooxygenase; !1photorespiration; photosynthesis FEATURE !$167,326 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$193 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$195 #binding_site magnesium (Asp) #status predicted SUMMARY #length 472 #molecular-weight 52523 #checksum 7064 SEQUENCE /// ENTRY RKKRL2 #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain 2 - Chromatium vinosum ORGANISM #formal_name Chromatium vinosum DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jun-2000 ACCESSIONS JQ0586; A36095 REFERENCE JQ0586 !$#authors Kobayashi, H.; Viale, A.M.; Takabe, T.; Akazawa, T.; Wada, !1K.; Shinozaki, K.; Kobayashi, K.; Sugiura, M. !$#journal Gene (1991) 97:55-62 !$#title Sequence and expression of genes encoding the large and !1small subunits of ribulose 1,5-bisphosphate carboxylase/ !1oxygenase from Chromatium vinosum. !$#cross-references MUID:91138986; PMID:1899846 !$#accession JQ0586 !'##molecule_type DNA !'##residues 1-471 ##label KOB !'##cross-references GB:D90204; NID:g804820; PIDN:BAA14229.1; !1PID:g804821 !'##note in addition to Lys-194, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation REFERENCE A36095 !$#authors Viale, A.M.; Kobayashi, H.; Akazawa, T. !$#journal J. Biol. Chem. (1990) 265:18386-18392 !$#title Distinct properties of Escherichia coli products of !1plant-type ribulose-1,5-bisphosphate carboxylase/oxygenase !1directed by two sets of genes from the photosynthetic !1bacterium Chromatium vinosum. !$#cross-references MUID:91009333; PMID:2211708 !$#accession A36095 !'##status preliminary !'##molecule_type protein !'##residues 2-26 ##label VIA GENETICS !$#gene rbcL !$#note there are two distinct sets of genes, rbcA-rbcB and !1rbcL-rbcS, for fully active ribulose-1,5-bisphosphate !1carboxylase in C. vinosum; the rbcL-rbcS set was barely !1expressed in the bacterium under standard photoautotrophic !1growth conditions FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; magnesium; monooxygenase; photorespiration; !1photosynthesis FEATURE !$8-471 #product ribulose-bisphosphate carboxylase large !8chain #status predicted #label MAT1\ !$168,327 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$194 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$196 #binding_site magnesium (Asp) #status predicted SUMMARY #length 471 #molecular-weight 52394 #checksum 8863 SEQUENCE /// ENTRY RKQXLX #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain - Xanthobacter flavus ORGANISM #formal_name Xanthobacter flavus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 18-Jun-1999 ACCESSIONS S13573; B36925; S35407 REFERENCE S13573 !$#authors Meijer, W.G.; Arnberg, A.C.; Enequist, H.G.; Terpstra, P.; !1Lidstrom, M.E.; Dijkhuizen, L. !$#journal Mol. Gen. Genet. (1991) 225:320-330 !$#title Identification and organization of carbon dioxide fixation !1genes in Xanthobacter flavus H4-14. !$#cross-references MUID:91172133; PMID:1900916 !$#accession S13573 !'##molecule_type DNA !'##residues 1-488 ##label MEI !'##cross-references EMBL:X17252; NID:g48543; PIDN:CAA35115.1; !1PID:g48544 !'##note in addition to Lys-206, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation REFERENCE A36925 !$#authors van den Bergh, E.R.E.; Dijkhuizen, L.; Meijer, W.G. !$#journal J. Bacteriol. (1993) 175:6097-6104 !$#title CbbR, a LysR-type transcriptional activator, is required for !1expression of the autotrophic CO-2 fixation enzymes of !1Xanthobacter flavus. !$#cross-references MUID:94012468; PMID:8407781 !$#accession B36925 !'##status preliminary !'##molecule_type DNA !'##residues 1-40 ##label VAN !'##cross-references GB:Z22705 COMMENT In addition to Lys-206, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. GENETICS !$#gene cfxL; cbbL FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; magnesium; monooxygenase; photorespiration; !1photosynthesis FEATURE !$180,338 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$206 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$208 #binding_site magnesium (Asp) #status predicted SUMMARY #length 488 #molecular-weight 53882 #checksum 3255 SEQUENCE /// ENTRY RKRFAL #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain A - Rhodobacter sphaeroides ORGANISM #formal_name Rhodobacter sphaeroides DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS D40767 REFERENCE A40767 !$#authors Gibson, J.L.; Falcone, D.L.; Tabita, F.R. !$#journal J. Biol. Chem. (1991) 266:14646-14653 !$#title Nucleotide sequence, transcriptional analysis, and !1expression of genes encoded within the form I CO-2 fixation !1operon of Rhodobacter sphaeroides. !$#cross-references MUID:91317831; PMID:1907281 !$#accession D40767 !'##molecule_type DNA !'##residues 1-486 ##label GIB !'##cross-references GB:M64624; NID:g151920; PIDN:AAA26115.1; !1PID:g151924 COMMENT This is the form of ribulose-bisphosphate carboxylase large !1chain that predominates when carbon dioxide is limited. COMMENT In addition to Lys-203, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. GENETICS !$#gene rbcL FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; magnesium; monooxygenase; photorespiration; !1photosynthesis FEATURE !$177,335 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$203 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$205 #binding_site magnesium (Asp) #status predicted SUMMARY #length 486 #molecular-weight 53686 #checksum 8447 SEQUENCE /// ENTRY RKALLE #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain - Alcaligenes eutrophus ORGANISM #formal_name Alcaligenes eutrophus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 21-May-1999 ACCESSIONS A26954 REFERENCE A91843 !$#authors Andersen, K.; Caton, J. !$#journal J. Bacteriol. (1987) 169:4547-4558 !$#title Sequence analysis of the Alcaligenes eutrophus chromosomally !1encoded ribulose bisphosphate carboxylase large and small !1subunit genes and their gene products. !$#cross-references MUID:88007394; PMID:2820933 !$#accession A26954 !'##molecule_type DNA !'##residues 1-487 ##label AND !'##cross-references GB:M17744; NID:g141966; PID:g141967 COMMENT In addition to Lys-204, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; magnesium; monooxygenase; photorespiration; !1photosynthesis FEATURE !$2-487 #product ribulose-bisphosphate carboxylase large !8chain #status experimental #label MAT\ !$178,336 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$204 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$206 #binding_site magnesium (Asp) #status predicted SUMMARY #length 487 #molecular-weight 54007 #checksum 9995 SEQUENCE /// ENTRY RKPFLE #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain precursor - brown alga (Ectocarpus siliculosus) chloroplast ORGANISM #formal_name chloroplast Ectocarpus siliculosus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS S13123 REFERENCE S13123 !$#authors Valentin, K.; Zetsche, K. !$#journal Plant Mol. Biol. (1990) 15:575-584 !$#title Rubisco genes indicate a close phylogenetic relation between !1the plastids of Chromophyta and Rhodophyta. !$#cross-references MUID:91338696; PMID:2102375 !$#accession S13123 !'##molecule_type DNA !'##residues 1-488 ##label VAL !'##cross-references EMBL:X52503; NID:g11543; PIDN:CAA36743.1; !1PID:g11544 COMMENT In addition to Lys-205, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. GENETICS !$#genome chloroplast FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; magnesium; monooxygenase; !1photorespiration; photosynthesis FEATURE !$16-488 #product ribulose-bisphosphate carboxylase large !8chain #status predicted #label MAT\ !$179,337 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$205 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$207 #binding_site magnesium (Asp) #status predicted SUMMARY #length 488 #molecular-weight 53904 #checksum 2273 SEQUENCE /// ENTRY RKPFLL #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain precursor - brown alga (Pylaiella littoralis) chloroplast ORGANISM #formal_name chloroplast Pylaiella littoralis DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 18-Jun-1999 ACCESSIONS S11964 REFERENCE S11964 !$#authors Assali, N.E.; Mache, R.; Loiseaux-de Goer, S. !$#journal Plant Mol. Biol. (1990) 15:307-315 !$#title Evidence for a composite phylogenetic origin of the plastid !1genome of the brown alga Pylaiella littoralis (L.) Kjellm. !$#cross-references MUID:91355877; PMID:2103450 !$#accession S11964 !'##molecule_type DNA !'##residues 1-488 ##label ASS !'##cross-references EMBL:X55372; NID:g14186; PIDN:CAA39051.1; !1PID:g14187 GENETICS !$#gene rbcL !$#genome chloroplast FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; magnesium; monooxygenase; !1photorespiration; photosynthesis FEATURE !$16-488 #product ribulose-bisphosphate carboxylase large !8chain #status predicted #label MAT\ !$179,337 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$205 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$207 #binding_site magnesium (Asp) #status predicted SUMMARY #length 488 #molecular-weight 54124 #checksum 1178 SEQUENCE /// ENTRY RKKKLA #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain - red alga (Antithamnion sp.) ORGANISM #formal_name Antithamnion sp. DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS S14126 REFERENCE S14126 !$#authors Kostrzewa, M.; Valentin, K.; Maid, U.; Radetzky, R.; !1Zetsche, K. !$#journal Curr. Genet. (1990) 18:465-469 !$#title Structure of the rubisco operon from the multicellular red !1alga Antithamnion spec. !$#cross-references MUID:91176557; PMID:2078870 !$#accession S14126 !'##molecule_type DNA !'##residues 1-488 ##label KOS !'##cross-references GB:X54532; NID:g11230; PIDN:CAA38398.1; PID:g11231 COMMENT In addition to Lys-205, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; magnesium; monooxygenase; photorespiration; !1photosynthesis FEATURE !$16-488 #product ribulose-bisphosphate carboxylase large !8chain #status predicted #label MAT\ !$179,337 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$205 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$207 #binding_site magnesium (Asp) #status predicted SUMMARY #length 488 #molecular-weight 54179 #checksum 737 SEQUENCE /// ENTRY RKKKLC #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain precursor - red alga (Cyanidium caldarium) chloroplast ORGANISM #formal_name chloroplast Cyanidium caldarium DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 19-May-2000 ACCESSIONS S11941 REFERENCE S11941 !$#authors Valentin, K.; Zetsche, K. !$#journal Mol. Gen. Genet. (1990) 222:425-430 !$#title Structure of the Rubisco operon from the unicellular red !1alga Cyanidium caldarium: evidence for a polyphyletic origin !1of the plastids. !$#cross-references MUID:91109732; PMID:2274041 !$#accession S11941 !'##molecule_type DNA !'##residues 1-493 ##label VAL !'##cross-references GB:X55524; NID:g296344; PIDN:CAA39140.1; !1PID:g296345 COMMENT In addition to Lys-210, another lysine, it is not certain !1which, may be the site of autocatalytic carbamylation. FUNCTION !$#description catalyzes the reaction of carbon dioxide with D-ribulose 1, !15-bisphosphate to form two molecules of 3-phospho-D-glyceric !1acid CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS Calvin cycle; carbon dioxide fixation; carbon-carbon lyase; !1carboxy-lyase; chloroplast; magnesium; monooxygenase; !1photorespiration; photosynthesis FEATURE !$21-493 #product ribulose-bisphosphate carboxylase large !8chain #status predicted #label MAT\ !$184,342 #active_site Lys (ribulose-bisphosphate-binding) !8#status predicted\ !$210 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$212 #binding_site magnesium (Asp) #status predicted SUMMARY #length 493 #molecular-weight 54989 #checksum 1135 SEQUENCE /// ENTRY B69448 #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain AF1587 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 18-Feb-2000 ACCESSIONS B69448 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession B69448 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-437 ##label KLE !'##cross-references GB:AE000993; GB:AE000782; NID:g2689316; !1PIDN:AAB89661.1; PID:g2648975; TIGR:AF1587 CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS carbon dioxide fixation; carbon-carbon lyase; carboxy-lyase FEATURE !$202 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$204 #binding_site magnesium (Asp) #status predicted SUMMARY #length 437 #molecular-weight 48560 #checksum 91 SEQUENCE /// ENTRY G69863 #type complete TITLE ribulose-bisphosphate carboxylase (EC 4.1.1.39) large chain homolog ykrW - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS G69863 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69863 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-414 ##label KUN !'##cross-references GB:Z99111; GB:AL009126; NID:g2633699; !1PIDN:CAB13232.1; PID:g2633730 !'##experimental_source strain 168 GENETICS !$#gene ykrW CLASSIFICATION #superfamily ribulose-bisphosphate carboxylase large chain KEYWORDS carbon dioxide fixation; carbon-carbon lyase; carboxy-lyase FEATURE !$176 #binding_site carbon dioxide (Lys) (covalent) (by !8Rubisco activase) #status predicted\ !$178 #binding_site magnesium (Asp) #status predicted SUMMARY #length 414 #molecular-weight 45048 #checksum 5905 SEQUENCE /// ENTRY A59389 #type complete TITLE probable phosphodiesterase I (EC 3.1.4.1) / nucleotide diphosphatase (EC 3.6.1.9) 4 - human ALTERNATE_NAMES ectonucleotide pyrophosphatase/phosphodiesterase 4; KIAA0879 protein; NPP4 ORGANISM #formal_name Homo sapiens #common_name man DATE 18-Jul-2001 #sequence_revision 18-Jul-2001 #text_change 16-Aug-2002 ACCESSIONS A59389; B59391 REFERENCE A59389 !$#authors Nagase, T.; Ishikawa, K.; Suyama, M.; Kikuno, R.; Hirosawa, !1M.; Miyajima, N.; Tanaka, A.; Kotani, H.; Nomura, N.; Ohara, !1O. !$#journal DNA Res. (1998) 5:355-364 !$#title Prediction of the coding sequences of unidentified human !1genes. XII. The complete sequences of 100 new cDNA clones !1from brain which code for large proteins in vitro. !$#cross-references MUID:99156230; PMID:10048485 !$#accession A59389 !'##molecule_type mRNA !'##residues 1-453 ##label NAG !'##cross-references GB:AB020686; NID:g4240247; PIDN:BAA74902.1 !'##experimental_source adult brain REFERENCE A59390 !$#authors Gijsbers, R.; Ceulemans, H.; Stalmans, W.; Bollen, M. !$#journal J. Biol. Chem. (2001) 276:1361-1368 !$#title Structural and catalytic similarities between nucleotide !1pyrophosphatases/phosphodiesterases and alkaline !1phosphatases. !$#cross-references MUID:21125673; PMID:11027689 !$#contents annotation REFERENCE A59391 !$#authors Smalley, C. !$#submission submitted to the EMBL Data Library, September 1999 !$#description Contains actin, gamma pseudogene 9, a gene similar to !1PLASMA-CELL MEMBRANE GLYCOPROTEIN PC-1, the gene for !1KIAA0879 protein, STSs and GSSs, complete sequence. !$#accession B59391 !'##molecule_type DNA !'##residues 1-453 ##label SMA !'##cross-references GB:AL035701; NID:g5924008; PIDN:CAB56567.1 GENETICS !$#gene ENPP4 !$#map_position 6p11.2-6p21.1 CLASSIFICATION #superfamily human phosphodiesterase I / nucleotide !1pyrophosphatase 4 KEYWORDS coenzyme A; metalloprotein; phosphoric diester hydrolase FEATURE !$70 #active_site Thr #status predicted SUMMARY #length 453 #molecular-weight 51641 #checksum 9806 SEQUENCE /// ENTRY A59391 #type complete TITLE probable phosphodiesterase I (EC 3.1.4.1) / nucleotide diphosphatase (EC 3.6.1.9) 5 - human ALTERNATE_NAMES ectonucleotide pyrophosphatase/phosphodiesterase 5; NPP5 ORGANISM #formal_name Homo sapiens #common_name man DATE 18-Jul-2001 #sequence_revision 18-Jul-2001 #text_change 16-Aug-2002 ACCESSIONS A59391 REFERENCE A59391 !$#authors Smalley, C. !$#submission submitted to the EMBL Data Library, September 1999 !$#description Contains actin, gamma pseudogene 9, a gene similar to !1PLASMA-CELL MEMBRANE GLYCOPROTEIN PC-1, the gene for !1KIAA0879 protein, STSs and GSSs, complete sequence. !$#accession A59391 !'##molecule_type DNA !'##residues 1-477 ##label SMA !'##cross-references GB:AL035701; NID:g5924007; PIDN:CAB56566.1 REFERENCE A59390 !$#authors Gijsbers, R.; Ceulemans, H.; Stalmans, W.; Bollen, M. !$#journal J. Biol. Chem. (2001) 276:1361-1368 !$#title Structural and catalytic similarities between nucleotide !1pyrophosphatases/phosphodiesterases and alkaline !1phosphatases. !$#cross-references MUID:21125673; PMID:11027689 !$#contents annotation GENETICS !$#gene ENPP5 !$#map_position 6p11.2-6p21.1 CLASSIFICATION #superfamily human phosphodiesterase I / nucleotide !1pyrophosphatase 4 KEYWORDS coenzyme A; metalloprotein; phosphoric diester hydrolase FEATURE !$72 #active_site Thr #status predicted SUMMARY #length 477 #molecular-weight 54665 #checksum 6430 SEQUENCE /// ENTRY A59390 #type complete TITLE probable phosphodiesterase I (EC 3.1.4.1) / nucleotide diphosphatase (EC 3.6.1.9) 5 - mouse ALTERNATE_NAMES ectonucleotide pyrophosphatase/phosphodiesterase 5; NPP5 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 18-Jul-2001 #sequence_revision 18-Jul-2001 #text_change 16-Aug-2002 ACCESSIONS A59390 REFERENCE A59390 !$#authors Gijsbers, R.; Ceulemans, H.; Stalmans, W.; Bollen, M. !$#journal J. Biol. Chem. (2001) 276:1361-1368 !$#title Structural and catalytic similarities between nucleotide !1pyrophosphatases/phosphodiesterases and alkaline !1phosphatases. !$#cross-references MUID:21125673; PMID:11027689 !$#accession A59390 !'##molecule_type DNA !'##residues 1-477 ##label GIJ !'##cross-references GB:AF233377; NID:g12231525; PIDN:AAG49143.1 !'##experimental_source strain C57BL/6J CLASSIFICATION #superfamily human phosphodiesterase I / nucleotide !1pyrophosphatase 4 KEYWORDS coenzyme A; metalloprotein; phosphoric diester hydrolase FEATURE !$72 #active_site Thr #status predicted SUMMARY #length 477 #molecular-weight 54386 #checksum 6589 SEQUENCE /// ENTRY DCPSMP #type fragment TITLE 4-carboxymuconolactone decarboxylase (EC 4.1.1.44) - Pseudomonas putida (fragment) ORGANISM #formal_name Pseudomonas putida DATE 30-Apr-1982 #sequence_revision 30-Apr-1982 #text_change 31-Dec-1993 ACCESSIONS A01101 REFERENCE A01101 !$#authors Yeh, W.K.; Fletcher, P.; Ornston, N. !$#journal J. Biol. Chem. (1980) 255:6347-6354 !$#title Homologies in the NH-2-terminal amino acid sequences of !1gamma-carboxymuconolactone decarboxylases and muconolactone !1isomerases. !$#cross-references MUID:80227765; PMID:7391024 !$#accession A01101 !'##molecule_type protein !'##residues 1-48 ##label YEH CLASSIFICATION #superfamily 4-carboxymuconolactone decarboxylase KEYWORDS carbon-carbon lyase; carboxy-lyase SUMMARY #length 48 #checksum 6550 SEQUENCE /// ENTRY DCHUDM #type complete TITLE adenosylmethionine decarboxylase (EC 4.1.1.50) precursor - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 24-Sep-1999 ACCESSIONS A31786 REFERENCE A92685 !$#authors Pajunen, A.; Crozat, A.; Jaenne, O.A.; Ihalainen, R.; !1Laitinen, P.H.; Stanley, B.; Madhubala, R.; Pegg, A.E. !$#journal J. Biol. Chem. (1988) 263:17040-17049 !$#title Structure and regulation of mammalian S-adenosylmethionine !1decarboxylase. !$#cross-references MUID:89034205; PMID:2460457 !$#accession A31786 !'##molecule_type mRNA !'##residues 1-334 ##label PAJ !'##cross-references GB:M34464 COMMENT The proenzyme is cleaved after translation into an alpha !1chain and a beta chain; the larger (beta) chain covalently !1binds a pyruvoyl prosthetic group, which is derived from !188-Ser and is required for enzyme activity. The active !1enzyme catalyzes the decarboxylation of !1S-adenosylmethionine, an essential step in spermidine !1biosynthesis. GENETICS !$#gene GDB:AMD1 !'##cross-references GDB:119674; OMIM:180980 !$#map_position 6pter-6qter CLASSIFICATION #superfamily eukaryotic adenosylmethionine decarboxylase KEYWORDS blocked amino end; carbon-carbon lyase; carboxy-lyase; !1polyamine biosynthesis FEATURE !$1-67 #domain alpha chain #status predicted #label CHA\ !$1-67,68-334 #product adenosylmethionine decarboxylase #status !8predicted #label MAT\ !$68-334 #domain beta chain #status predicted #label CHB\ !$68 #modified_site pyruvic acid (Ser) (in mature form) !8#status predicted SUMMARY #length 334 #molecular-weight 38325 #checksum 581 SEQUENCE /// ENTRY DCHYDM #type complete TITLE adenosylmethionine decarboxylase (EC 4.1.1.50) precursor - golden hamster ORGANISM #formal_name Mesocricetus auratus #common_name golden hamster DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 24-Sep-1999 ACCESSIONS S22358; S19871 REFERENCE S22358 !$#authors Tekwani, B.L.; Stanley, B.A.; Pegg, A.E. !$#journal Biochim. Biophys. Acta (1992) 1130:221-223 !$#title Nucleotide sequence of hamster S-adenosylmethionine !1decarboxylase cDNA. !$#cross-references MUID:92223099; PMID:1562599 !$#accession S22358 !'##molecule_type mRNA !'##residues 1-334 ##label TEK !'##cross-references EMBL:X63861; NID:g55521; PIDN:CAA45343.1; !1PID:g55522 !'##experimental_source liver of Syrian golden hamster !'##note the authors translated the codon ACA for residue 221 as Leu and !1AAG for residue 328 as Ala COMMENT The proenzyme is cleaved after translation into an alpha !1chain and a beta chain; the larger (beta) chain covalently !1binds a pyruvoyl prosthetic group, which is derived from !168-Ser and is required for enzyme activity. The active !1enzyme catalyzes the decarboxylation of !1S-adenosylmethionine, an essential step in spermidine !1biosynthesis. CLASSIFICATION #superfamily eukaryotic adenosylmethionine decarboxylase KEYWORDS blocked amino end; carbon-carbon lyase; carboxy-lyase; !1polyamine biosynthesis FEATURE !$1-67 #domain alpha chain #status predicted #label CHA\ !$1-67,68-334 #product adenosylmethionine decarboxylase #status !8predicted #label MAT\ !$68-334 #domain beta chain #status predicted #label CHB\ !$68 #modified_site pyruvic acid (Ser) (in mature form) !8#status predicted SUMMARY #length 334 #molecular-weight 38313 #checksum 1014 SEQUENCE /// ENTRY DCRTDM #type complete TITLE adenosylmethionine decarboxylase (EC 4.1.1.50) precursor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 24-Sep-1999 ACCESSIONS JQ0439; B31786; S18487; A47002 REFERENCE JQ0439 !$#authors Pulkka, A.; Keraenen, M.R.; Salmela, A.; Salmikangas, P.; !1Ihalainen, R.; Pajunen, A. !$#journal Gene (1990) 86:193-199 !$#title Nucleotide sequence of rat S-adenosylmethionine !1decarboxylase cDNA: comparison with an intronless rat !1pseudogene. !$#cross-references MUID:90215298; PMID:2323572 !$#accession JQ0439 !'##molecule_type mRNA !'##residues 1-333 ##label PUL !'##cross-references GB:M34464; NID:g202754; PIDN:AAA40683.1; !1PID:g202755 REFERENCE A92685 !$#authors Pajunen, A.; Crozat, A.; Jaenne, O.A.; Ihalainen, R.; !1Laitinen, P.H.; Stanley, B.; Madhubala, R.; Pegg, A.E. !$#journal J. Biol. Chem. (1988) 263:17040-17049 !$#title Structure and regulation of mammalian S-adenosylmethionine !1decarboxylase. !$#cross-references MUID:89034205; PMID:2460457 !$#accession B31786 !'##molecule_type mRNA !'##residues 1-4,'P',6-145,'A',147-333 ##label PAJ !'##cross-references GB:M34464 REFERENCE S18487 !$#authors Pulkka, A.; Ihalainen, R.; Aatsinki, J.; Pajunen, A. !$#journal FEBS Lett. (1991) 291:289-295 !$#title Structure and organization of the gene encoding rat !1S-adenosylmethionine decarboxylase. !$#cross-references MUID:92038054; PMID:1936275 !$#accession S18487 !'##status translation not shown !'##molecule_type DNA !'##residues 1-145,'A',147-333 ##label PU2 !'##cross-references GB:M64274; NID:g206843; PIDN:AAA42105.1; !1PID:g206844 REFERENCE A47002 !$#authors Pulkka, A.; Ihalainen, R.; Suorsa, A.; Riviere, M.; Szpirer, !1J.; Pajunen, A. !$#journal Genomics (1993) 16:342-349 !$#title Structures and chromosomal localizations of two rat genes !1encoding S-adenosylmethionine decarboxylase. !$#cross-references MUID:93300506; PMID:8314573 !$#accession A47002 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-145,'A',147-333 ##label RES !'##cross-references EMBL:Z15109; NID:g55705; PIDN:CAA78814.1; !1PID:g818018 COMMENT The proenzyme is cleaved after translation into an alpha !1chain and a beta chain; the larger (beta) chain covalently !1binds a pyruvoyl prosthetic group, which is derived from !168-Ser and is required for enzyme activity. The active !1enzyme catalyzes the decarboxylation of !1S-adenosylmethionine, an essential step in spermidine !1biosynthesis. COMMENT This is a key enzyme in the biosynthesis of polyamine. GENETICS !$#gene AMD1B !$#introns 37/2; 66/2; 108/3; 143/1; 157/2; 236/3; 288/3 CLASSIFICATION #superfamily eukaryotic adenosylmethionine decarboxylase KEYWORDS blocked amino end; carbon-carbon lyase; carboxy-lyase; !1polyamine biosynthesis FEATURE !$1-67 #domain alpha chain #status predicted #label CHA\ !$1-67,68-333 #product adenosylmethionine decarboxylase #status !8predicted #label MAT\ !$68-333 #domain beta chain #status predicted #label CHB\ !$68 #modified_site pyruvic acid (Ser) (in mature form) !8#status predicted SUMMARY #length 333 #molecular-weight 38123 #checksum 7517 SEQUENCE /// ENTRY DCBYDM #type complete TITLE adenosylmethionine decarboxylase (EC 4.1.1.50) precursor - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein O1275; protein YOL052c ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 23-Mar-2001 ACCESSIONS S12772; A30469; S59299; S61729; S66737; S66744 REFERENCE S12772 !$#authors Kashiwagi, K.; Taneja, S.K.; Liu, T.Y.; Tabor, C.W.; Tabor, !1H. !$#journal J. Biol. Chem. (1990) 265:22321-22328 !$#title Spermidine biosynthesis in Saccharomyces cerevisiae. !1Biosynthesis and processing of a proenzyme form of !1S-adenosylmethionine decarboxylase. !$#cross-references MUID:91093074; PMID:2266128 !$#accession S12772 !'##molecule_type DNA !'##residues 1-396 ##label KAS1 !'##cross-references EMBL:M38434; NID:g171054; PIDN:AAA34421.1; !1PID:g171055 !$#accession A30469 !'##molecule_type protein !'##residues 2-19;'A',89-101,'X',103-104 ##label KAS2 REFERENCE S59285 !$#authors Mannhaupt, G.; Vetter, I.; Schwarzlose, C.; Mitzel, S.; !1Feldmann, H. !$#submission submitted to the EMBL Data Library, August 1995 !$#description Analysis of a 26kb region on the left arm of yeast !1chromosome XV. !$#accession S59299 !'##molecule_type DNA !'##residues 1-396 ##label FEL !'##cross-references EMBL:X91067; NID:g984177; PIDN:CAA62536.1; !1PID:g984192 REFERENCE S61715 !$#authors Mannhaupt, G.; Vetter, I.; Schwarzlose, C.; Mitzel, S.; !1Feldmann, H. !$#journal Yeast (1996) 12:67-76 !$#title Analysis of a 26 kb region on the left arm of yeast !1chromosome XV. !$#cross-references MUID:96381248; PMID:8789261 !$#accession S61729 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-396 ##label MAN !'##cross-references EMBL:X91067; NID:g984177; PIDN:CAA62536.1; !1PID:g984192 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1995 REFERENCE S66723 !$#authors Ansorge, W.; Benes, V.; Rechmann, S.; Schwager, C.; Teodoru, !1C.; Voss, H.; Wiemann, S. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S66737 !'##molecule_type DNA !'##residues 1-396 ##label ANS !'##cross-references EMBL:Z74794; NID:g1419858; PIDN:CAA99058.1; !1PID:g1419859; GSPDB:GN00015; MIPS:YOL052c !'##experimental_source strain S288C REFERENCE S66743 !$#authors Feldmann, H.; Mannhaupt, G.; Vetter, I. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S66744 !'##molecule_type DNA !'##residues 1-396 ##label FEW !'##cross-references EMBL:Z74794; NID:g1419858; PIDN:CAA99058.1; !1PID:g1419859; GSPDB:GN00015; MIPS:YOL052c !'##experimental_source strain S288C COMMENT The pyruvoyl group derived from 88-Ser is required for !1catalytic activity and forms a Schiff base with the !1substrate or product. GENETICS !$#gene SGD:SPE2; MIPS:YOL052c !'##cross-references SGD:S0005412; MIPS:YOL052c !$#map_position 15L CLASSIFICATION #superfamily eukaryotic adenosylmethionine decarboxylase KEYWORDS blocked amino end; carbon-carbon lyase; carboxy-lyase; !1polyamine biosynthesis FEATURE !$2-87 #domain beta chain #status experimental #label CHB\ !$2-87,88-396 #product adenosylmethionine decarboxylase #status !8experimental #label MAT\ !$88-396 #domain alpha chain #status experimental #label CHA\ !$88 #modified_site pyruvic acid (Ser) (in mature form) !8#status experimental SUMMARY #length 396 #molecular-weight 46232 #checksum 4299 SEQUENCE /// ENTRY DCECDM #type complete TITLE adenosylmethionine decarboxylase (EC 4.1.1.50) precursor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 01-Mar-2002 ACCESSIONS B29778; S45197; H64734 REFERENCE A29778 !$#authors Tabor, C.W.; Tabor, H. !$#journal J. Biol. Chem. (1987) 262:16037-16040 !$#title The speEspeD operon of Escherichia coli. Formation and !1processing of a proenzyme form of S-adenosylmethionine !1decarboxylase. !$#cross-references MUID:88058963; PMID:3316212 !$#accession B29778 !'##molecule_type DNA !'##residues 1-264 ##label TAB !'##cross-references GB:J02804; NID:g147850; PIDN:AAA24644.1; !1PID:g551838; GB:J04247 REFERENCE S45181 !$#authors Fujita, N. !$#submission submitted to the EMBL Data Library, January 1994 !$#accession S45197 !'##molecule_type DNA !'##residues 'L',2-264 ##label FUJ !'##cross-references EMBL:D26562 !'##experimental_source strain K-12 substrain W3110 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64734 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-264 ##label BLAT !'##cross-references GB:AE000121; GB:U00096; NID:g1786306; !1PIDN:AAC73231.1; PID:g1786311; UWGP:b0120 !'##experimental_source strain K-12, substrain MG1655 COMMENT The proenzyme is cleaved after translation into a 12K !1polypeptide (beta chain) and an 18K polypeptide (alpha !1chain); the larger chain covalently binds a pyruvoyl !1prosthetic group, which is essential for enzyme activity. !1The active enzyme catalyzes the decarboxylation of !1S-adenosylmethionine, an essential step in spermidine !1biosynthesis. GENETICS !$#gene speD !$#map_position 3 min !$#start_codon TTG CLASSIFICATION #superfamily bacterial adenosylmethionine decarboxylase KEYWORDS carbon-carbon lyase; carboxy-lyase; polyamine biosynthesis FEATURE !$1-111 #product adenosylmethionine decarboxylase beta chain !8#status experimental #label PTB\ !$112-264 #product adenosylmethionine decarboxylase alpha chain !8#status experimental #label PTA SUMMARY #length 264 #molecular-weight 30384 #checksum 4664 SEQUENCE /// ENTRY ADECD #type complete TITLE deoxyribose-phosphate aldolase (EC 4.1.2.4) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 01-Mar-2002 ACCESSIONS A01102; S56605; D65253 REFERENCE A01102 !$#authors Valentin-Hansen, P.; Boetius, F.; Hammer-Jespersen, K.; !1Svendsen, I. !$#journal Eur. J. Biochem. (1982) 125:561-566 !$#title The primary structure of Escherichia coli K12 2-deoxyribose !15-phosphate aldolase. Nucleotide sequence of the deoC gene !1and the amino acid sequence of the enzyme. !$#cross-references MUID:83003651; PMID:6749498 !$#accession A01102 !'##molecule_type DNA !'##residues 1-259 ##label VAL !'##experimental_source strain K12 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56605 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-259 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97277.1; !1PID:g537221 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65253 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-259 ##label BLAT !'##cross-references GB:AE000508; GB:U00096; NID:g2367382; !1PIDN:AAC77334.1; PID:g1790841; UWGP:b4381 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene deoC !$#map_position 100 min FUNCTION !$#description catalyzes the interconversion of deoxyribose-phosphate to !1glyceraldehyde 3-phosphate and acetaldehyde !$#pathway nucleotide catabolism CLASSIFICATION #superfamily deoxyribose-phosphate aldolase KEYWORDS aldehyde-lyase; carbon-carbon lyase; nucleotide catabolism SUMMARY #length 259 #molecular-weight 27733 #checksum 8247 SEQUENCE /// ENTRY ADHUA #type complete TITLE fructose-bisphosphate aldolase (EC 4.1.2.13) A [validated] - human ALTERNATE_NAMES aldolase A; fructose-1,6-bisphosphate triosephosphate-lyase A ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 08-Dec-2000 ACCESSIONS S14084; A27186; S01014; S00290; S02338; A05177; S03874; !1S23919; I39429; I39435 REFERENCE S14084 !$#authors Mukai, T.; Arai, Y.; Yatsuki, H.; Joh, K.; Hori, K. !$#journal Eur. J. Biochem. (1991) 195:781-787 !$#title An additional promoter functions in the human aldolase A !1gene, but not in rat. !$#cross-references MUID:91153319; PMID:1999195 !$#accession S14084 !'##molecule_type DNA !'##residues 1-364 ##label MUK REFERENCE A27186 !$#authors Izzo, P.; Costanzo, P.; Lupo, A.; Rippa, E.; Borghese, A.M.; !1Paolella, G.; Salvatore, F. !$#journal Eur. J. Biochem. (1987) 164:9-13 !$#title A new human species of aldolase A mRNA from fibroblasts. !$#cross-references MUID:87161904; PMID:3030757 !$#accession A27186 !'##molecule_type mRNA !'##residues 1-364 ##label IZZ !'##cross-references GB:X05236; NID:g28596; PIDN:CAA28861.1; PID:g28597 !'##experimental_source fibroblast REFERENCE S01014 !$#authors Izzo, P.; Costanzo, P.; Lupo, A.; Rippa, E.; Paolella, G.; !1Salvatore, F. !$#journal Eur. J. Biochem. (1988) 174:569-578 !$#title Human aldolase A gene. Structural organization and !1tissue-specific expression by multiple promoters and !1alternate mRNA processing. !$#cross-references MUID:88271327; PMID:3391172 !$#accession S01014 !'##molecule_type DNA !'##residues 1-72,'G',74-195,'A',197-229,'N',231-279,'S',281-364 ##label !1IZ2 !'##cross-references GB:X12447; NID:g28613; PIDN:CAA30979.1; PID:g28614 REFERENCE S00290 !$#authors Freemont, P.S.; Dunbar, B.; Fothergill-Gilmore, L.A. !$#journal Biochem. J. (1988) 249:779-788 !$#title The complete amino acid sequence of human skeletal-muscle !1fructose-bisphosphate aldolase. !$#cross-references MUID:88183272; PMID:3355497 !$#accession S00290 !'##molecule_type protein !'##residues 2-358,'I',360-364 ##label FRE REFERENCE S02338 !$#authors Maire, P.; Gautron, S.; Hakim, V.; Gregori, C.; Mennecier, !1F.; Kahn, A. !$#journal J. Mol. Biol. (1987) 197:425-438 !$#title Characterization of three optional promoters in the 5' !1region of the human aldolase A gene. !$#cross-references MUID:88155643; PMID:3441006 !$#accession S02338 !'##molecule_type DNA !'##residues 1-108 ##label MAI !'##cross-references EMBL:X06352; NID:g28594; PIDN:CAA29654.1; !1PID:g28595 REFERENCE A05177 !$#authors Freemont, P.S.; Dunbar, B.; Fothergill, L.A. !$#journal Arch. Biochem. Biophys. (1984) 228:342-352 !$#title Human skeletal-muscle aldolase: N-terminal sequence analysis !1of CNBr- and o-iodosobenzoic acid-cleavage fragments. !$#cross-references MUID:84126818; PMID:6696436 !$#accession A05177 !'##molecule_type protein !'##residues 2-63;148-358 ##label FR2 REFERENCE S03874 !$#authors Sakakibara, M.; Takahashi, I.; Takasaki, Y.; Mukai, T.; !1Hori, K. !$#journal Biochim. Biophys. Acta (1989) 1007:334-342 !$#title Construction and expression of human aldolase A and B !1expression plasmids in Escherichia coli host. !$#cross-references MUID:89194215; PMID:2649152 !$#accession S03874 !'##molecule_type mRNA !'##residues 1-33;357-364 ##label SAK REFERENCE S23919 !$#authors Lee, K.N.; Maxwell, M.D.; Patterson Jr., M.K.; Birckbichler, !1P.J.; Conway, E. !$#journal Biochim. Biophys. Acta (1992) 1136:12-16 !$#title Identification of transglutaminase substrates in HT29 colon !1cancer cells: use of 5-(biotinamido) pentylamine as a !1transglutaminase-specific probe. !$#cross-references MUID:92353128; PMID:1353685 !$#accession S23919 !'##molecule_type protein !'##residues 2-16 ##label LEE REFERENCE A43787 !$#authors Gamblin, S.J.; Davies, G.J.; Grimes, J.M.; Jackson, R.M.; !1Littlechild, J.A.; Watson, H.C. !$#journal J. Mol. Biol. (1991) 219:573-576 !$#title Activity and Specificity of Human Aldolases. !$#cross-references MUID:91278081; PMID:2056525 !$#contents annotation; active site REFERENCE I39429 !$#authors Sakakibara, M.; Mukai, T.; Hori, K. !$#journal Biochem. Biophys. Res. Commun. (1985) 131:413-420 !$#title Nucleotide sequence of a cDNA clone for human aldolase: a !1messenger RNA in the liver. !$#cross-references MUID:85306986; PMID:3840020 !$#accession I39429 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-364 ##label RES !'##cross-references GB:M11560; NID:g178350; PIDN:AAA51690.1; !1PID:g178351 REFERENCE I39435 !$#authors Tolan, D.R.; Niclas, J.; Bruce, B.D.; Lebo, R.V. !$#journal Am. J. Hum. Genet. (1987) 41:907-924 !$#title Evolutionary implications of the human aldolase-A, -B, -C, !1and -pseudogene chromosome locations. !$#cross-references MUID:88046782; PMID:3674018 !$#accession I39435 !'##molecule_type mRNA !'##residues 139-364 ##label TOL !'##cross-references GB:M21190; NID:g178403; PIDN:AAA51697.1; !1PID:g178404 COMMENT In vertebrates, three forms of this ubiquitous glycolytic !1enzyme are found, aldolase A in muscle, aldolase B in liver, !1and aldolase C in brain. GENETICS !$#gene GDB:ALDOA !'##cross-references GDB:118993; OMIM:103850 !$#map_position 16q22.2-16q22.2 !$#introns 38/1 CLASSIFICATION #superfamily fructose-bisphosphate aldolase KEYWORDS aldehyde-lyase; carbon-carbon lyase; gluconeogenesis; !1glycolysis; muscle; pentose phosphate pathway; tetramer FEATURE !$2-364 #product fructose-bisphosphate aldolase A #status !8experimental #label MAT\ !$147,230,364 #active_site Lys, Lys, Tyr #status experimental SUMMARY #length 364 #molecular-weight 39420 #checksum 8498 SEQUENCE /// ENTRY ADRBA #type complete TITLE fructose-bisphosphate aldolase (EC 4.1.2.13) A - rabbit ALTERNATE_NAMES aldolase A; fructose-1,6-bisphosphate triosephosphate-lyase A ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 24-Apr-1984 #sequence_revision 27-Nov-1985 #text_change 18-Jun-1999 ACCESSIONS A92444; A90059; A90305; A90060; I46474; I46475; A01103 REFERENCE A92444 !$#authors Tolan, D.R.; Amsden, A.B.; Putney, S.D.; Urdea, M.S.; !1Penhoet, E.E. !$#journal J. Biol. Chem. (1984) 259:1127-1131 !$#title The complete nucleotide sequence for rabbit muscle aldolase !1A messenger RNA. !$#cross-references MUID:84111505; PMID:6546378 !$#accession A92444 !'##molecule_type mRNA !'##residues 1-363 ##label TOL !'##cross-references GB:K02300; NID:g164751; PIDN:AAA31156.1; !1PID:g164752 !'##note initiator Met not shown REFERENCE A94244 !$#authors Lai, C.Y.; Nakai, N.; Chang, D. !$#journal Science (1974) 183:1204-1206 !$#title Amino acid sequence of rabbit muscle aldolase and the !1structure of the active center. !$#cross-references MUID:74094688; PMID:4812352 !$#contents annotation !$#note the sequence reported in this paper has been revised in !1references A90305 and A90060 REFERENCE A90059 !$#authors Nakai, N.; Chang, D.; Lai, C.Y. !$#journal Arch. Biochem. Biophys. (1975) 166:347-357 !$#title Studies on the structure of rabbit muscle aldolase. Ordering !1of the tryptic peptides; sequence of 164 amino acid residues !1in the NH-2-terminal BrCN peptide. !$#cross-references MUID:75145171; PMID:1122141 !$#accession A90059 !'##molecule_type protein !'##residues 1-33,'Q',35-164 ##label NAK REFERENCE A90305 !$#authors Benfield, P.A.; Forcina, B.G.; Gibbons, I.; Perham, R.N. !$#journal Biochem. J. (1979) 183:429-444 !$#title Extended amino acid sequences around the active-site lysine !1residue of class-I fructose 1,6-bisphosphate aldolases from !1rabbit muscle, sturgeon muscle, trout muscle and ox liver. !$#cross-references MUID:80109133; PMID:534504 !$#accession A90305 !'##molecule_type protein !'##residues 173-200 ##label BEN REFERENCE A90060 !$#authors Lai, C.Y. !$#journal Arch. Biochem. Biophys. (1975) 166:358-368 !$#title Studies on the structure of rabbit muscle aldolase. !1Determination of the primary structure of the COOH-terminal !1BrCN peptide; the complete sequence of the subunit !1polypeptide chain. !$#cross-references MUID:75145172; PMID:1122142 !$#accession A90060 !'##molecule_type protein !'##residues 251-272,'S',274,'E',276-277,'G',279-292,'W',294,'K',296-363 !1##label LAI2 REFERENCE A92191 !$#authors Hartman, F.C.; Brown, J.P. !$#journal J. Biol. Chem. (1976) 251:3057-3062 !$#title Affinity labeling of a previously undetected essential lysyl !1residue in class I fructose bisphosphate aldolase. !$#cross-references MUID:76190154; PMID:5453 !$#contents annotation; active site REFERENCE I46471 !$#authors Putney, S.D.; Herlihy, W.C.; Schimmel, P. !$#journal Nature (1983) 302:718-721 !$#title A new troponin T and cDNA clones for 13 different muscle !1proteins, found by shotgun sequencing. !$#cross-references MUID:83167564; PMID:6687628 !$#accession I46474 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 37-55 ##label PUT !'##cross-references EMBL:V00876; NID:g1444; PIDN:CAA24245.1; !1PID:g929753 !$#accession I46475 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 349-352,'R',354-363 ##label PU2 !'##cross-references EMBL:V00877; NID:g1446; PIDN:CAA24246.1; !1PID:g833792 COMMENT In vertebrates, three forms of this ubiquitous glycolytic !1enzyme are found, aldolase A in muscle, aldolase B in liver, !1and aldolase C in brain. CLASSIFICATION #superfamily fructose-bisphosphate aldolase KEYWORDS aldehyde-lyase; carbon-carbon lyase; gluconeogenesis; !1glycolysis; muscle; pentose phosphate pathway; tetramer FEATURE !$2-363 #product fructose-bisphosphate aldolase A #status !8predicted #label MAT\ !$146,229,363 #active_site Lys, Lys, Tyr #status predicted SUMMARY #length 363 #molecular-weight 39211 #checksum 6800 SEQUENCE /// ENTRY ADMSA #type complete TITLE fructose-bisphosphate aldolase (EC 4.1.2.13) A - mouse ALTERNATE_NAMES aldolase A; fructose-1,6-bisphosphate triosephosphate-lyase A ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 18-Jun-1999 ACCESSIONS S06323; B25388; A37062 REFERENCE S06323 !$#authors Mestek, A.; Stauffer, J.; Tolan, D.R.; Ciejek-Baez, E. !$#journal Nucleic Acids Res. (1987) 15:10595 !$#title Sequence of a mouse brain aldolase A cDNA. !$#cross-references MUID:88096598; PMID:3697100 !$#accession S06323 !'##molecule_type mRNA !'##residues 1-364 ##label MES !'##cross-references GB:Y00516; NID:g49914; PIDN:CAA68571.1; PID:g49915 !'##experimental_source brain REFERENCE A91165 !$#authors Paolella, G.; Buono, P.; Mancini, F.P.; Izzo, P.; Salvatore, !1F. !$#journal Eur. J. Biochem. (1986) 156:229-235 !$#title Structure and expression of mouse aldolase genes. !1Brain-specific aldolase C amino acid sequence is closely !1related to aldolase A. !$#cross-references MUID:86192445; PMID:3009179 !$#accession B25388 !'##molecule_type mRNA !'##residues 99-280,'C',282-355 ##label PAO !'##cross-references GB:X03797; NID:g49916; PIDN:CAA27423.1; PID:g929677 !'##experimental_source brain REFERENCE A37062 !$#authors Stauffer, J.K.; Colbert, M.C.; Ciejek-Baez, E. !$#journal J. Biol. Chem. (1990) 265:11773-11782 !$#title Nonconservative utilization of aldolase A alternative !1promoters. !$#cross-references MUID:90307699; PMID:2365699 !$#accession A37062 !'##molecule_type DNA !'##residues 1-266;295-364 ##label STA !'##cross-references GB:J05517 !'##experimental_source strain RIII S/J CLASSIFICATION #superfamily fructose-bisphosphate aldolase KEYWORDS aldehyde-lyase; carbon-carbon lyase; gluconeogenesis; !1glycolysis; muscle; pentose phosphate pathway; tetramer FEATURE !$2-364 #product fructose-bisphosphate aldolase A #status !8predicted #label MAT\ !$147,230,364 #active_site Lys, Lys, Tyr #status predicted SUMMARY #length 364 #molecular-weight 39356 #checksum 9067 SEQUENCE /// ENTRY ADRTA #type complete TITLE fructose-bisphosphate aldolase (EC 4.1.2.13) A - rat ALTERNATE_NAMES aldolase A; fructose-1,6-bisphosphate triosephosphate-lyase A ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jun-2000 ACCESSIONS A24532; A25383; I53307; I56408 REFERENCE A24532 !$#authors Joh, K.; Mukai, T.; Yatsuki, H.; Hori, K. !$#journal Gene (1985) 39:17-24 !$#title Rat aldolase A messenger RNA: the nucleotide sequence and !1multiple mRNA species with different 5'-terminal regions. !$#cross-references MUID:86083188; PMID:2416636 !$#accession A24532 !'##molecule_type mRNA !'##residues 1-364 ##label JOH !'##cross-references GB:M14420; NID:g202836; PIDN:AAA40715.1; !1PID:g202837 REFERENCE A25383 !$#authors Mukai, T.; Joh, K.; Arai, Y.; Yatsuki, H.; Hori, K. !$#journal J. Biol. Chem. (1986) 261:3347-3354 !$#title Tissue-specific expression of rat aldolase A mRNAs: three !1molecular species differing only in the 5'-terminal !1sequences. !$#cross-references MUID:86140113; PMID:3753977 !$#accession A25383 !'##molecule_type mRNA !'##residues 1-144,'F',146-164,'M',166-364 ##label MUK !'##cross-references GB:M12919; NID:g202834; PIDN:AAA40714.1; !1PID:g202835 REFERENCE I53307 !$#authors Tsutsumi, R.; Tsutsumi, K. !$#journal Eur. J. Biochem. (1984) 142:161-164 !$#title Two different aldolase A mRNA species in rat tissues. !$#cross-references MUID:84261525; PMID:6086339 !$#accession I53307 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 324-329,'Q',331-356 ##label RES !'##cross-references GB:M28282; NID:g202849; PIDN:AAA40720.1; !1PID:g202850 REFERENCE I56408 !$#authors Joh, K.; Arai, Y.; Mukai, T.; Hori, K. !$#journal J. Mol. Biol. (1986) 190:401-410 !$#title Expression of three mRNA species from a single rat aldolase !1A gene, differing in their 5' non-coding regions. !$#cross-references MUID:87060996; PMID:3783705 !$#accession I56408 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-108 ##label RE2 !'##cross-references EMBL:X04261; NID:g55639; PIDN:CAA27815.1; !1PID:g1619605 GENETICS !$#introns 38/1 CLASSIFICATION #superfamily fructose-bisphosphate aldolase KEYWORDS aldehyde-lyase; carbon-carbon lyase; gluconeogenesis; !1glycolysis; muscle; pentose phosphate pathway; tetramer FEATURE !$2-364 #product fructose-bisphosphate aldolase A #status !8predicted #label MAT\ !$147,230,364 #active_site Lys, Lys, Tyr #status predicted SUMMARY #length 364 #molecular-weight 39259 #checksum 317 SEQUENCE /// ENTRY ADHUC #type complete TITLE fructose-bisphosphate aldolase (EC 4.1.2.13) C - human ALTERNATE_NAMES aldolase C; fructose-1,6-bisphosphate triosephosphate-lyase C ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 18-Jun-1999 ACCESSIONS A25861; S00863; S13192 REFERENCE A25861 !$#authors Rottmann, W.H.; Deselms, K.R.; Niclas, J.; Camerato, T.; !1Holman, P.S.; Green, C.J.; Tolan, D.R. !$#journal Biochimie (1987) 69:137-145 !$#title The complete amino acid sequence of the human aldolase C !1isozyme derived from genomic clones. !$#cross-references MUID:87185595; PMID:3105602 !$#accession A25861 !'##molecule_type DNA !'##residues 1-364 ##label ROT !'##cross-references GB:X05196; NID:g28598; PIDN:CAA28825.1; PID:g28599 REFERENCE S00863 !$#authors Buono, P.; Paolella, G.; Mancini, F.P.; Izzo, P.; Salvatore, !1F. !$#journal Nucleic Acids Res. (1988) 16:4733 !$#title The complete nucleotide sequence of the gene coding for the !1human aldolase C. !$#cross-references MUID:88247784; PMID:3267224 !$#accession S00863 !'##status translation not shown !'##molecule_type DNA !'##residues 1-310,'V',312-364 ##label BUO1 !'##cross-references GB:X07292; NID:g28600; PIDN:CAA30270.1; PID:g312137 REFERENCE S13192 !$#authors Buono, P.; Mancini, F.P.; Izzo, P.; Salvatore, F. !$#journal Eur. J. Biochem. (1990) 192:805-811 !$#title Characterization of the transcription-initiation site and of !1the promoter region within the 5' flanking region of the !1human aldolase C gene. !$#cross-references MUID:91006178; PMID:2209624 !$#accession S13192 !'##molecule_type DNA !'##residues 1-310,'V',312-364 ##label BUO2 !'##cross-references GB:X07292; GB:M84921; NID:g28600; PIDN:CAA30270.1; !1PID:g312137 GENETICS !$#gene GDB:ALDOC !'##cross-references GDB:119670; OMIM:103870 !$#map_position 17pter-17qter !$#introns 38/1; 108/3; 127/1; 180/3; 208/3; 267/1; 333/3 CLASSIFICATION #superfamily fructose-bisphosphate aldolase KEYWORDS aldehyde-lyase; brain; carbon-carbon lyase; gluconeogenesis; !1glycolysis; pentose phosphate pathway; tetramer FEATURE !$2-364 #product fructose-bisphosphate aldolase C #status !8predicted #label MAT\ !$147,230,364 #active_site Lys, Lys, Tyr #status predicted SUMMARY #length 364 #molecular-weight 39456 #checksum 9625 SEQUENCE /// ENTRY ADRTC #type complete TITLE fructose-bisphosphate aldolase (EC 4.1.2.13) C - rat ALTERNATE_NAMES aldolase C; fructose-1,6-bisphosphate triosephosphate-lyase C; fructose-bisphosphate aldolase, brain ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jun-2000 ACCESSIONS S00326; A38817; JN0127; I53313 REFERENCE S00326 !$#authors Kukita, A.; Mukai, T.; Miyata, T.; Hori, K. !$#journal Eur. J. Biochem. (1988) 171:471-478 !$#title The structure of brain-specific rat aldolase C mRNA and the !1evolution of aldolase isozyme genes. !$#cross-references MUID:88151941; PMID:2831050 !$#accession S00326 !'##molecule_type mRNA !'##residues 1-363 ##label KUK !'##cross-references EMBL:X06984; NID:g55634; PIDN:CAA30044.1; !1PID:g1334163 !$#accession A38817 !'##molecule_type protein !'##residues 2-21 ##label KU2 REFERENCE JN0127 !$#authors Mukai, T.; Yatsuki, H.; Masuko, S.; Arai, Y.; Joh, K.; Hori, !1K. !$#journal Biochem. Biophys. Res. Commun. (1991) 174:1035-1042 !$#title The structure of the brain-specific rat aldolase C gene and !1its regional expression. !$#cross-references MUID:91128359; PMID:1993044 !$#accession JN0127 !'##molecule_type DNA !'##residues 1-336,'LAA',340-363 ##label MUK !'##cross-references GB:M63656; NID:g202841; PIDN:AAA40717.1; !1PID:g202842 REFERENCE I53313 !$#authors Skala, H.; Vibert, M.; Lamas, E.; Maire, P.; Schweighoffer, !1F.; Kahn, A. !$#journal Eur. J. Biochem. (1987) 163:513-518 !$#title Molecular cloning and expression of rat aldolase C messenger !1RNA during development and hepatocarcinogenesis. !$#cross-references MUID:87161851; PMID:3830170 !$#accession I53313 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 251-363 ##label RES !'##cross-references EMBL:X05277; NID:g55632; PIDN:CAA28889.1; !1PID:g55633 GENETICS !$#introns 38/1; 108/3; 127/1; 180/3; 208/3; 267/1; 333/3 CLASSIFICATION #superfamily fructose-bisphosphate aldolase KEYWORDS aldehyde-lyase; brain; carbon-carbon lyase; gluconeogenesis; !1glycolysis; pentose phosphate pathway; tetramer FEATURE !$2-363 #product fructose-bisphosphate aldolase C #status !8experimental #label MAT\ !$147,230,363 #active_site Lys, Lys, Tyr #status predicted SUMMARY #length 363 #molecular-weight 39289 #checksum 7546 SEQUENCE /// ENTRY ADMSC #type fragment TITLE fructose-bisphosphate aldolase (EC 4.1.2.13) C - mouse (fragment) ALTERNATE_NAMES aldolase C; fructose-1,6-bisphosphate triosephosphate-lyase C ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 18-Jun-1999 ACCESSIONS A25388 REFERENCE A91165 !$#authors Paolella, G.; Buono, P.; Mancini, F.P.; Izzo, P.; Salvatore, !1F. !$#journal Eur. J. Biochem. (1986) 156:229-235 !$#title Structure and expression of mouse aldolase genes. !1Brain-specific aldolase C amino acid sequence is closely !1related to aldolase A. !$#cross-references MUID:86192445; PMID:3009179 !$#accession A25388 !'##molecule_type mRNA !'##residues 1-227 ##label PAO !'##cross-references GB:X03796; NID:g49918; PIDN:CAA27422.1; PID:g49919 CLASSIFICATION #superfamily fructose-bisphosphate aldolase KEYWORDS aldehyde-lyase; brain; carbon-carbon lyase; gluconeogenesis; !1glycolysis; pentose phosphate pathway; tetramer FEATURE !$2-227 #product fructose-bisphosphate aldolase C #status !8predicted #label MAT\ !$147 #active_site Lys #status predicted SUMMARY #length 227 #checksum 7428 SEQUENCE /// ENTRY ADHUB #type complete TITLE fructose-bisphosphate aldolase (EC 4.1.2.13) B - human ALTERNATE_NAMES aldolase B; fructose-1,6-bisphosphate triosephosphate-lyase B ORGANISM #formal_name Homo sapiens #common_name man DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 18-Jun-1999 ACCESSIONS A41505; A23788; A20979; A54642; S03875; I37160; A05178 REFERENCE A41505 !$#authors Mukai, T.; Yatsuki, H.; Arai, Y.; Joh, K.; Matsuhashi, S.; !1Hori, K. !$#journal J. Biochem. (1987) 102:1043-1051 !$#title Human aldolase B gene: characterization of the genomic !1aldolase B gene and analysis of sequences required for !1multiple polyadenylations. !$#cross-references MUID:88139255; PMID:2830249 !$#accession A41505 !'##molecule_type DNA !'##residues 1-364 ##label MUK !'##cross-references GB:D00176 !'##note the authors translated the codon GAA for residue 51 as Gln REFERENCE A23788 !$#authors Sakakibara, M.; Mukai, T.; Yatsuki, H.; Hori, K. !$#journal Nucleic Acids Res. (1985) 13:5055-5069 !$#title Human aldolase isozyme gene: the structure of multispecies !1aldolase B mRNAs. !$#cross-references MUID:85269627; PMID:2410860 !$#accession A23788 !'##molecule_type mRNA !'##residues 1-364 ##label SAK !'##cross-references GB:X02747; NID:g28616; PIDN:CAA26526.1; PID:g28617 REFERENCE A20979 !$#authors Rottmann, W.H.; Tolan, D.R.; Penhoet, E.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:2738-2742 !$#title Complete amino acid sequence for human aldolase B derived !1from cDNA and genomic clones. !$#cross-references MUID:84194081; PMID:6585824 !$#accession A20979 !'##molecule_type mRNA !'##residues 1-308,'V',310-364 ##label ROT !'##cross-references GB:K01177; NID:g178352; PIDN:AAB59377.1; !1PID:g178353 REFERENCE A54642 !$#authors Tolan, D.R.; Penhoet, E.E. !$#journal Mol. Biol. Med. (1986) 3:245-264 !$#title Characterization of the human aldolase B gene. !$#cross-references MUID:86284198; PMID:3016456 !$#accession A54642 !'##molecule_type DNA !'##residues 1-53,'D',55-364 ##label TOL !'##cross-references GB:M15657; GB:M15656; NID:g178355; PIDN:AAA51691.1; !1PID:g178357 !'##note authors translated the codon GAC for residue 54 as Glu REFERENCE S03874 !$#authors Sakakibara, M.; Takahashi, I.; Takasaki, Y.; Mukai, T.; !1Hori, K. !$#journal Biochim. Biophys. Acta (1989) 1007:334-342 !$#title Construction and expression of human aldolase A and B !1expression plasmids in Escherichia coli host. !$#cross-references MUID:89194215; PMID:2649152 !$#accession S03875 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-33;357-364 ##label SA2 !'##note parts of this sequence, including the amino and carboxyl ends !1of the mature protein, were determined by amino acid !1sequencing REFERENCE I37160 !$#authors Besmond, C.; Dreyfus, J.C.; Gregori, C.; Frain, M.; Zakin, !1M.M.; Sala Trepat, J.; Kahn, A. !$#journal Biochem. Biophys. Res. Commun. (1983) 117:601-609 !$#title Nucleotide sequence of a cDNA clone for human aldolase B. !$#cross-references MUID:84104270; PMID:6689266 !$#accession I37160 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 238-249,'D',251-364 ##label RES !'##cross-references EMBL:X00270; NID:g28611; PIDN:CAA25072.1; !1PID:g563884 COMMENT Mutations of the gene for aldolase B cause hereditary !1fructose intolerance. GENETICS !$#gene GDB:ALDOB !'##cross-references GDB:119669; OMIM:229600 !$#map_position 9q22-9q22 !$#introns 38/1; 108/3; 127/1; 180/3; 208/3; 267/1; 333/3 CLASSIFICATION #superfamily fructose-bisphosphate aldolase KEYWORDS aldehyde-lyase; carbon-carbon lyase; gluconeogenesis; !1glycolysis; liver; pentose phosphate pathway; tetramer FEATURE !$2-364 #product fructose-bisphosphate aldolase B #status !8predicted #label MAT\ !$147,230,364 #active_site Lys, Lys, Tyr #status predicted SUMMARY #length 364 #molecular-weight 39473 #checksum 5123 SEQUENCE /// ENTRY ADRTB #type complete TITLE fructose-bisphosphate aldolase (EC 4.1.2.13) B - rat ALTERNATE_NAMES aldolase B; fructose-1,6-bisphosphate triosephosphate-lyase B ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 15-Nov-1984 #sequence_revision 30-Sep-1987 #text_change 16-Jun-2000 ACCESSIONS A22585; A40842; I55228; I56392; A01104; A05179 REFERENCE A22585 !$#authors Tsutsumi, K.; Mukai, T.; Tsutsumi, R.; Mori, M.; Daimon, M.; !1Tanaka, T.; Yatsuki, H.; Hori, K.; Ishikawa, K. !$#journal J. Biol. Chem. (1984) 259:14572-14575 !$#title Nucleotide sequence of rat liver aldolase B messenger RNA. !$#cross-references MUID:85054935; PMID:6094564 !$#accession A22585 !'##molecule_type mRNA !'##residues 1-364 ##label TSU !'##cross-references GB:M10149; NID:g202839; PIDN:AAA40716.1; !1PID:g202840 REFERENCE A40842 !$#authors Brand, I.A.; Heinickel, A. !$#journal J. Biol. Chem. (1991) 266:20984-20989 !$#title Key enzymes of carbohydrate metabolism as targets of the !111.5-kDa Zn(2+)-binding protein (parathymosin). !$#cross-references MUID:92041965; PMID:1834654 !$#accession A40842 !'##status preliminary !'##molecule_type protein !'##residues 41-63,'X',65-68 ##label BRA REFERENCE I55228 !$#authors Tsutsumi, K.; Mukai, T.; Hidaka, S.; Miyahara, H.; Tsutsumi, !1R.; Tanaka, T.; Hori, K.; Ishikawa, K. !$#journal J. Biol. Chem. (1983) 258:6537-6542 !$#title Rat aldolase isozyme gene. !$#cross-references MUID:83213364; PMID:6304044 !$#accession I55228 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 185-364 ##label RES !'##cross-references EMBL:V01223; NID:g55636; PIDN:CAA24533.1; !1PID:g55637 REFERENCE I56392 !$#authors Tsutsumi, K.; Mukai, T.; Tsutsumi, R.; Hidaka, S.; Arai, Y.; !1Hori, K.; Ishikawa, K. !$#journal J. Mol. Biol. (1985) 181:153-160 !$#title Structure and genomic organization of the rat aldolase B !1gene. !$#cross-references MUID:85160837; PMID:2580098 !$#accession I56392 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-37 ##label RE2 !'##cross-references EMBL:X02284; NID:g55655; PIDN:CAA26156.1; !1PID:g1619606 CLASSIFICATION #superfamily fructose-bisphosphate aldolase KEYWORDS aldehyde-lyase; carbon-carbon lyase; gluconeogenesis; !1glycolysis; liver; pentose phosphate pathway; tetramer FEATURE !$2-364 #product fructose-bisphosphate aldolase B #status !8predicted #label MAT\ !$147,230,364 #active_site Lys, Lys, Tyr #status predicted SUMMARY #length 364 #molecular-weight 39618 #checksum 7733 SEQUENCE /// ENTRY ADCHB #type complete TITLE fructose-bisphosphate aldolase (EC 4.1.2.13) B - chicken ALTERNATE_NAMES aldolase B; fructose-1,6-bisphosphate triosephosphate-lyase B ORGANISM #formal_name Gallus gallus #common_name chicken DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 18-Jun-1999 ACCESSIONS A22568 REFERENCE A22568 !$#authors Burgess, D.G.; Penhoet, E.E. !$#journal J. Biol. Chem. (1985) 260:4604-4614 !$#title Characterization of the chicken aldolase B gene. !$#cross-references MUID:85182565; PMID:2985560 !$#accession A22568 !'##molecule_type DNA !'##residues 1-364 ##label BUR !'##cross-references GB:M10946; NID:g211128; PIDN:AAA48587.1; !1PID:g211129 GENETICS !$#introns 38/1; 108/3; 127/1; 180/3; 208/3; 267/1; 333/3 CLASSIFICATION #superfamily fructose-bisphosphate aldolase KEYWORDS aldehyde-lyase; carbon-carbon lyase; gluconeogenesis; !1glycolysis; liver; pentose phosphate pathway; tetramer FEATURE !$2-364 #product fructose-bisphosphate aldolase B #status !8predicted #label MAT\ !$147,230,364 #active_site Lys, Lys, Tyr #status predicted SUMMARY #length 364 #molecular-weight 39295 #checksum 438 SEQUENCE /// ENTRY ADFF #type complete TITLE fructose-bisphosphate aldolase (EC 4.1.2.13) - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 30-Sep-1991 #sequence_revision 31-Dec-1992 #text_change 18-Jun-1999 ACCESSIONS B42027; S06439; A28855; S22186 REFERENCE A42027 !$#authors Kim, J.; Yim, J.J.; Wang, S.; Dorsett, D. !$#journal Mol. Cell. Biol. (1992) 12:773-783 !$#title Alternate use of divergent forms of an ancient exon in the !1fructose-1,6-bisphosphate aldolase gene of Drosophila !1melanogaster. !$#cross-references MUID:92123202; PMID:1732743 !$#accession B42027 !'##molecule_type DNA !'##residues 1-361 ##label KIM !'##cross-references EMBL:X60064; NID:g7571; PIDN:CAA42667.1; PID:g7573 !'##note sequence extracted from NCBI backbone (NCBIN:76664, !1NCBIP:87828) REFERENCE S06439 !$#authors Malek, A.A.; Hy, M.; Honegger, A.; Rose, K.; !1Brenner-Holzach, O. !$#journal Arch. Biochem. Biophys. (1988) 266:10-31 !$#title Fructose-1,6-bisphosphate aldolase from Drosophila !1melanogaster: primary structure analysis, secondary !1structure prediction, and comparison with vertebrate !1aldolases. !$#cross-references MUID:89024658; PMID:3140728 !$#accession S06439 !'##molecule_type protein !'##residues 2-110,'K',112-200,'R',202-250,'A',252-361 ##label MAL REFERENCE A28855 !$#authors Brenner-Holzach, O.; Zumsteg, C. !$#journal Arch. Biochem. Biophys. (1982) 214:89-101 !$#title Fructose 1,6-bisphosphate aldolase of Drosophila !1melanogaster: comparative sequence analyses around the !1substrate-binding lysyl residue. !$#cross-references MUID:82205133; PMID:6805442 !$#accession A28855 !'##molecule_type protein !'##residues 170-179,'QS',182-200,'R',202-224,'Q',226-250,'A',252-272 !1##label BRE !'##note peptides were ordered by homology with the rabbit sequence GENETICS !$#gene FlyBase:Ald !'##cross-references FlyBase:FBgn0000064 CLASSIFICATION #superfamily fructose-bisphosphate aldolase KEYWORDS aldehyde-lyase; carbon-carbon lyase; gluconeogenesis; !1glycolysis; pentose phosphate pathway FEATURE !$2-361 #product fructose-bisphosphate aldolase #status !8experimental #label MAT\ !$147,230,361 #active_site Lys, Lys, Tyr #status predicted SUMMARY #length 361 #molecular-weight 38979 #checksum 3328 SEQUENCE /// ENTRY ADFFR #type complete TITLE aldolase-related protein - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 18-Jun-1999 ACCESSIONS A42027; C42027; S22185 REFERENCE A42027 !$#authors Kim, J.; Yim, J.J.; Wang, S.; Dorsett, D. !$#journal Mol. Cell. Biol. (1992) 12:773-783 !$#title Alternate use of divergent forms of an ancient exon in the !1fructose-1,6-bisphosphate aldolase gene of Drosophila !1melanogaster. !$#cross-references MUID:92123202; PMID:1732743 !$#accession A42027 !'##molecule_type DNA !'##residues 1-395 ##label KIM !'##cross-references EMBL:X60064; NID:g7571; PIDN:CAA42666.1; PID:g7572 !'##note sequence extracted from NCBI backbone (NCBIN:76664, !1NCBIP:76666) GENETICS !$#gene FlyBase:Ald !'##cross-references FlyBase:FBgn0000064 CLASSIFICATION #superfamily fructose-bisphosphate aldolase KEYWORDS alternative splicing FEATURE !$1-333,363-395 #product aldolase-related protein 2 #status predicted !8#label AD2 SUMMARY #length 395 #molecular-weight 42966 #checksum 628 SEQUENCE /// ENTRY ADZM #type complete TITLE fructose-bisphosphate aldolase (EC 4.1.2.13), cytosolic - maize ALTERNATE_NAMES aldolase, cytosolic; fructose-1,6-bisphosphate triosephosphate-lyase, cytosolic ORGANISM #formal_name Zea mays #common_name maize DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 18-Jun-1999 ACCESSIONS S07789; S10638 REFERENCE S07789 !$#authors Dennis, E.S.; Gerlach, W.L.; Walker, J.C.; Lavin, M.; !1Peacock, W.J. !$#journal J. Mol. Biol. (1988) 202:759-767 !$#title Anaerobically regulated aldolase gene of maize. A chimaeric !1origin? !$#cross-references MUID:89012000; PMID:3172237 !$#accession S07789 !'##status translation not shown !'##molecule_type DNA !'##residues 1-355 ##label DEN !'##cross-references EMBL:X12872; NID:g22144; PIDN:CAA31366.1; !1PID:g295850 REFERENCE S10638 !$#authors Kelley, P.M.; Tolan, D.R. !$#journal Plant Physiol. (1986) 82:1076-1080 !$#title The complete amino acid sequence for the anaerobically !1induced aldolase from maize derived from cDNA clones. !$#accession S10638 !'##molecule_type mRNA !'##residues 1-355 ##label KEL !'##cross-references EMBL:M16220; NID:g168419; PIDN:AAA33435.1; !1PID:g168420 GENETICS !$#introns 10/1 CLASSIFICATION #superfamily fructose-bisphosphate aldolase KEYWORDS aldehyde-lyase; carbon-carbon lyase; gluconeogenesis; !1glycolysis; pentose phosphate pathway FEATURE !$142,225,355 #active_site Lys, Lys, Tyr #status predicted SUMMARY #length 355 #molecular-weight 38604 #checksum 5690 SEQUENCE /// ENTRY ADRZY #type complete TITLE fructose-bisphosphate aldolase (EC 4.1.2.13), cytosolic - rice ALTERNATE_NAMES aldolase, cytosolic; fructose-1,6-bisphosphate triosephosphate-lyase, cytosolic ORGANISM #formal_name Oryza sativa #common_name rice DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 18-Jun-1999 ACCESSIONS JQ0543 REFERENCE JQ0543 !$#authors Hidaka, S.; Kadowaki, K.; Tsutsumi, K.; Ishikawa, K. !$#journal Nucleic Acids Res. (1990) 18:3991 !$#title Nucleotide sequence of the rice cytoplasmic aldolase cDNA. !$#cross-references MUID:90326527; PMID:2374721 !$#accession JQ0543 !'##molecule_type mRNA !'##residues 1-358 ##label HID !'##cross-references EMBL:X53130; NID:g20203; PIDN:CAA37290.1; !1PID:g20204 !'##experimental_source cv. Nihonbare CLASSIFICATION #superfamily fructose-bisphosphate aldolase KEYWORDS aldehyde-lyase; carbon-carbon lyase; gluconeogenesis; !1glycolysis; pentose phosphate pathway FEATURE !$142,225,358 #active_site Lys, Lys, Tyr #status predicted SUMMARY #length 358 #molecular-weight 38810 #checksum 146 SEQUENCE /// ENTRY ADSPAC #type complete TITLE fructose-bisphosphate aldolase (EC 4.1.2.13), cytosolic - spinach ALTERNATE_NAMES aldolase, cytosolic; fructose-1,6-bisphosphate triosephosphate-lyase, cytosolic ORGANISM #formal_name Spinacia oleracea #common_name spinach DATE 31-Dec-1992 #sequence_revision 30-Sep-1993 #text_change 18-Jun-1999 ACCESSIONS S31091; S22093 REFERENCE S31090 !$#authors Pelzer-Reith, B.; Penger, A.; Schnarrenberger, C. !$#journal Plant Mol. Biol. (1993) 21:331-340 !$#title Plant aldolase: cDNA and deduced amino-acid sequences of the !1chloroplast and cytosol enzyme from spinach. !$#cross-references MUID:93144707; PMID:8425060 !$#accession S31091 !'##molecule_type mRNA !'##residues 1-357 ##label PEL1 !'##cross-references EMBL:X65742 REFERENCE S22092 !$#authors Pelzer-Reith, B.; Penger, A.; Schnaorenberger, C. !$#submission submitted to the EMBL Data Library, June 1992 !$#accession S22093 !'##molecule_type mRNA !'##residues 1-227,'I',229-357 ##label PEL2 !'##cross-references EMBL:X65742; NID:g22619; PIDN:CAA46649.1; !1PID:g22620 CLASSIFICATION #superfamily fructose-bisphosphate aldolase KEYWORDS aldehyde-lyase; blocked amino end; carbon-carbon lyase; !1gluconeogenesis; glycolysis; pentose phosphate pathway; !1tetramer FEATURE !$142,225,357 #active_site Lys, Lys, Tyr #status predicted SUMMARY #length 357 #molecular-weight 38488 #checksum 9046 SEQUENCE /// ENTRY ADMU #type complete TITLE fructose-bisphosphate aldolase (EC 4.1.2.13) - Arabidopsis thaliana ALTERNATE_NAMES aldolase, cytosolic; fructose-1,6-bisphosphate triosephosphate-lyase, cytosolic; protein M3E9.50 ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 31-Mar-2000 ACCESSIONS S11958; T05052 REFERENCE S11958 !$#authors Chopra, S.; Dolferus, R.; Jacobs, M. !$#journal Plant Mol. Biol. (1990) 15:517-520 !$#title Cloning and sequencing of the Arabidopsis aldolase gene. !$#cross-references MUID:91355902; PMID:2103470 !$#accession S11958 !'##molecule_type DNA !'##residues 1-358 ##label CHO !'##cross-references EMBL:X53058; NID:g16283; PIDN:CAA37226.1; !1PID:g16284 REFERENCE Z15396 !$#authors Bevan, M.; Vandenbol, M.; Jallet, C.; Portetelle, D.; !1Hoheisel, J.; Mewes, H.W.; Mayer, K.F.X.; Schueller, C. !$#submission submitted to the Protein Sequence Database, March 1999 !$#accession T05052 !'##molecule_type DNA !'##residues 1-137,'A',139-358 ##label BEV !'##cross-references EMBL:AL022223; GSPDB:GN00062; ATSP:M3E9.50 !'##experimental_source cultivar Columbia; BAC clone M3E9 GENETICS !$#gene ATSP:M3E9.50 !$#map_position 4 !$#introns 10/1; 94/3; 237/3 CLASSIFICATION #superfamily fructose-bisphosphate aldolase KEYWORDS aldehyde-lyase; carbon-carbon lyase; gluconeogenesis; !1glycolysis; pentose phosphate pathway FEATURE !$142,225,358 #active_site Lys, Lys, Tyr #status predicted SUMMARY #length 358 #molecular-weight 38796 #checksum 1120 SEQUENCE /// ENTRY ADUT #type complete TITLE fructose-bisphosphate aldolase (EC 4.1.2.13) - Trypanosoma brucei ALTERNATE_NAMES aldolase A; fructose-1,6-bisphosphate triosephosphate-lyase A ORGANISM #formal_name Trypanosoma brucei DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 18-Jun-1999 ACCESSIONS A24678; S15063; S12675 REFERENCE A24678 !$#authors Clayton, C.E. !$#journal EMBO J. (1985) 4:2997-3003 !$#title Structure and regulated expression of genes encoding !1fructose biphosphate aldolase in Trypanosoma brucei. !$#cross-references MUID:86055739; PMID:2998772 !$#accession A24678 !'##molecule_type mRNA !'##residues 1-372 ##label CLA1 !'##cross-references GB:X03061; NID:g10379; PIDN:CAA26867.1; PID:g10380 REFERENCE S15063 !$#authors Clayton, C.E. !$#submission submitted to the EMBL Data Library, April 1990 !$#accession S15063 !'##molecule_type DNA !'##residues 1-372 ##label CLA2 !'##cross-references EMBL:X52586; NID:g10397; PIDN:CAA36819.1; !1PID:g10400 REFERENCE S12673 !$#authors Vijayasarathy, S.; Ernest, I.; Itzhaki, J.E.; Sherman, D.; !1Mowatt, M.R.; Michels, P.A.M.; Clayton, C.E. !$#journal Nucleic Acids Res. (1990) 18:2967-2975 !$#title The genes encoding fructose bisphosphate aldolase in !1Trypanosoma brucei are interspersed with unrelated genes. !$#cross-references MUID:90272402; PMID:2349093 !$#accession S12675 !'##molecule_type DNA !'##residues 1-11 ##label VIJ !'##cross-references EMBL:X52586 CLASSIFICATION #superfamily fructose-bisphosphate aldolase KEYWORDS aldehyde-lyase; carbon-carbon lyase; gluconeogenesis; !1glycolysis; pentose phosphate pathway FEATURE !$157,240,372 #active_site Lys, Lys, Tyr #status predicted SUMMARY #length 372 #molecular-weight 41178 #checksum 4100 SEQUENCE /// ENTRY ADSPAP #type complete TITLE fructose-bisphosphate aldolase (EC 4.1.2.13) precursor, chloroplast - spinach ALTERNATE_NAMES aldolase; fructose-1,6-bisphosphate triosephosphate-lyase ORGANISM #formal_name Spinacia oleracea #common_name spinach DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 18-Jun-1999 ACCESSIONS S31090; A21815; S22092 REFERENCE S31090 !$#authors Pelzer-Reith, B.; Penger, A.; Schnarrenberger, C. !$#journal Plant Mol. Biol. (1993) 21:331-340 !$#title Plant aldolase: cDNA and deduced amino-acid sequences of the !1chloroplast and cytosol enzyme from spinach. !$#cross-references MUID:93144707; PMID:8425060 !$#accession S31090 !'##molecule_type mRNA !'##residues 1-393 ##label PEL !'##cross-references EMBL:X66814; NID:g22632; PIDN:CAA47293.1; !1PID:g22633 REFERENCE A21815 !$#authors Lebherz, H.G.; Leadbetter, M.M.; Bradshaw, R.A. !$#journal J. Biol. Chem. (1984) 259:1011-1017 !$#title Isolation and characterization of the cytosolic and !1chloroplast forms of spinach leaf fructose diphosphate !1aldolase. !$#cross-references MUID:84111487; PMID:6420397 !$#accession A21815 !'##molecule_type protein !'##residues 47-64 ##label LEB CLASSIFICATION #superfamily fructose-bisphosphate aldolase KEYWORDS aldehyde-lyase; Calvin cycle; carbon-carbon lyase; !1chloroplast; pentose phosphate pathway; tetramer FEATURE !$1-46 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$47-393 #product fructose-bisphosphate aldolase #status !8experimental #label MAT\ !$183,264,393 #active_site Lys, Lys, Tyr #status predicted SUMMARY #length 393 #molecular-weight 42476 #checksum 7489 SEQUENCE /// ENTRY ADEC2A #type complete TITLE fructose-bisphosphate aldolase (EC 4.1.2.13) II [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES metal-dependent fructose-bisphosphate aldolase ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 01-Mar-2002 ACCESSIONS S02177; A38058; D65077; S04734 REFERENCE S02177 !$#authors Alefounder, P.R.; Baldwin, S.A.; Perham, R.N.; Short, N.J. !$#journal Biochem. J. (1989) 257:529-534 !$#title Cloning, sequence analysis and over-expression of the gene !1for the class II fructose 1,6-bisphosphate aldolase of !1Escherichia coli. !$#cross-references MUID:89193446; PMID:2649077 !$#accession S02177 !'##molecule_type DNA !'##residues 1-359 ##label ALE !'##cross-references GB:X14436; EMBL:X14682; NID:g41417; !1PIDN:CAA32605.1; PID:g41423 !$#accession A38058 !'##molecule_type protein !'##residues 165-167;213-216;277-285;337-345 ##label ALE2 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65077 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-359 ##label BLAT !'##cross-references GB:AE000376; GB:U00096; NID:g2367176; !1PIDN:AAC75962.1; PID:g1789293; UWGP:b2925 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene fba; fda !$#map_position 63 min COMPLEX homodimer [validated, MUID:89193446] FUNCTION !$#description EC 4.1.2.13 [validated, MUID:89193446] !$#note class II enzymes utilize a divalent metal ion to act as the !1electron sink CLASSIFICATION #superfamily fructose-bisphosphate aldolase II KEYWORDS aldehyde-lyase; carbon-carbon lyase; gluconeogenesis; !1glycolysis; homodimer; pentose phosphate pathway; zinc FEATURE !$2-359 #product fructose-bisphosphate aldolase #status !8experimental #label MAT SUMMARY #length 359 #molecular-weight 39147 #checksum 6863 SEQUENCE /// ENTRY ADBY2 #type complete TITLE fructose-bisphosphate aldolase (EC 4.1.2.13) II - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YKL060c; protein YKL320 ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 12-Nov-1999 ACCESSIONS S07855; S37882; S12945; S39178; S44523 REFERENCE S07855 !$#authors Schwelberger, H.G.; Kohlwein, S.D.; Paltauf, F. !$#journal Eur. J. Biochem. (1989) 180:301-308 !$#title Molecular cloning, primary structure and disruption of the !1structural gene of aldolase from Saccharomyces cerevisiae. !$#cross-references MUID:89170729; PMID:2647491 !$#accession S07855 !'##molecule_type DNA !'##residues 1-359 ##label SCH !'##cross-references EMBL:X15003; NID:g3695; PIDN:CAA33111.1; PID:g3696 REFERENCE S37872 !$#authors Rasmussen, S.; von Wettstein, D. !$#submission submitted to the Protein Sequence Database, March 1994 !$#accession S37882 !'##molecule_type DNA !'##residues 1-359 ##label RAS !'##cross-references EMBL:Z28060; NID:g486080; PIDN:CAA81897.1; !1PID:g486081; GSPDB:GN00011; MIPS:YKL060c !'##experimental_source strain S288C REFERENCE S12945 !$#authors Gatignol, A.; Dassain, M.; Tiraby, G. !$#journal Gene (1990) 91:35-41 !$#title Cloning of Saccharomyces cerevisiae promoters using a probe !1vector based on phleomycin resistance. !$#cross-references MUID:90382695; PMID:1698168 !$#accession S12945 !'##molecule_type DNA !'##residues 1-96 ##label GAT !'##cross-references GB:M32026 REFERENCE S39168 !$#authors Rasmussen, S.W. !$#submission submitted to the EMBL Data Library, November 1993 !$#accession S39178 !'##molecule_type DNA !'##residues 1-359 ##label RA2 !'##cross-references EMBL:X75781; NID:g433634; PIDN:CAA53412.1; !1PID:g433637 !'##experimental_source strain S288C REFERENCE S44521 !$#authors Rasmussen, S.W. !$#journal Yeast (1994) 10:63-68 !$#title Sequence of a 28.6 kb region of yeast chromosome XI includes !1the FBA1 and TOA2 genes, an open reading frame (ORF) similar !1to a translationally controlled tumour protein, one ORF !1containing motifs also found in plant storage proteins and !113 ORFs with weak or no homology to known proteins. !$#accession S44523 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-359 ##label RAW !'##cross-references EMBL:X75781; NID:g433634; PIDN:CAA53412.1; !1PID:g433637 !'##experimental_source strain S288C !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1993 GENETICS !$#gene SGD:FBA1; MIPS:YKL060c !'##cross-references SGD:S0001543; MIPS:YKL060c !$#map_position 11L CLASSIFICATION #superfamily fructose-bisphosphate aldolase II KEYWORDS aldehyde-lyase; carbon-carbon lyase; glycolysis; homodimer; !1pentose phosphate pathway; zinc SUMMARY #length 359 #molecular-weight 39620 #checksum 586 SEQUENCE /// ENTRY ADRFAS #type complete TITLE fructose-bisphosphate aldolase (EC 4.1.2.13) - Rhodobacter sphaeroides ALTERNATE_NAMES aldolase; fructose-1,6-bisphosphate triosephosphate-lyase ORGANISM #formal_name Rhodobacter sphaeroides DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 24-Feb-1994 ACCESSIONS B40767 REFERENCE A40767 !$#authors Gibson, J.L.; Falcone, D.L.; Tabita, F.R. !$#journal J. Biol. Chem. (1991) 266:14646-14653 !$#title Nucleotide sequence, transcriptional analysis, and !1expression of genes encoded within the form I CO-2 fixation !1operon of Rhodobacter sphaeroides. !$#cross-references MUID:91317831; PMID:1907281 !$#accession B40767 !'##molecule_type DNA !'##residues 1-359 ##label GIB !'##cross-references GB:M64624 COMMENT This protein is encoded within the form I !1ribulose-bisphosphate carboxylase operon, which predominates !1when carbon dioxide is limiting. GENETICS !$#gene cfxA CLASSIFICATION #superfamily fructose-bisphosphate aldolase II KEYWORDS aldehyde-lyase; Calvin cycle; carbon-carbon lyase; !1gluconeogenesis SUMMARY #length 359 #molecular-weight 38872 #checksum 1874 SEQUENCE /// ENTRY D32354 #type complete TITLE fructose-bisphosphate aldolase (EC 4.1.2.13) fbaA - Bacillus subtilis ALTERNATE_NAMES 30K phosphoprotein orfY-tsr; fructose-1,6-bisphosphate aldolase ORGANISM #formal_name Bacillus subtilis DATE 03-Mar-1994 #sequence_revision 03-Mar-1994 #text_change 16-Jun-2000 ACCESSIONS S55426; D32354; E32354; D41835; B69621 REFERENCE S55414 !$#authors Glaser, P.; Danchin, A. !$#submission submitted to the EMBL Data Library, May 1995 !$#description Cloning and sequencing of the Bacillus subtilis chromosomal !1region from 320 degrees to 321 degrees. !$#accession S55426 !'##molecule_type DNA !'##residues 1-285 ##label GLA !'##cross-references EMBL:Z49782; NID:g853752; PIDN:CAA89873.1; !1PID:g853765 REFERENCE A91883 !$#authors Trach, K.; Chapman, J.W.; Piggot, P.; LeCoq, D.; Hoch, J.A. !$#journal J. Bacteriol. (1988) 170:4194-4208 !$#title Complete sequence and transcriptional analysis of the spo0F !1region of the Bacillus subtilis chromosome. !$#cross-references MUID:88314920; PMID:2457578 !$#accession D32354 !'##molecule_type DNA !'##residues 'MLGWKAFFARRQSGYIRRTFD',1-16,'RVRCRTI' ##label TR1 !'##cross-references GB:M22039 !'##note this sequence has been revised !'##note prior to the correction of a frameshift error, this portion of !1the sequence was designated orfY !$#accession E32354 !'##molecule_type DNA !'##residues 'M',77-285 ##label TR2 !'##cross-references GB:M22039 !'##note this sequence has been revised !'##note prior to the correction of a frameshift error, this portion of !1the sequence was designated tsr and was believed to begin !1with a GTG start codon REFERENCE A41835 !$#authors Mitchell, C.; Morris, P.W.; Vary, J.C. !$#journal J. Bacteriol. (1992) 174:2474-2477 !$#title Identification of proteins phosphorylated by ATP during !1sporulation of Bacillus subtilis. !$#cross-references MUID:92210489; PMID:1556067 !$#accession D41835 !'##molecule_type protein !'##residues 1-26 ##label MIT !'##note this sequence was obtained from the amino end REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69621 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-285 ##label KUN !'##cross-references GB:Z99122; GB:Z99123; GB:AL009126; NID:g2636240; !1PIDN:CAB15740.1; PID:g2636249; NID:g2636029; PID:g2636237 !'##experimental_source strain 168 COMMENT This sequence is based on translation of residues 3270-3317 !1and 3319-4128 of accession M22039 (GenBank release 80.0) to !1correct a frameshift error and the assignment of the start !1of translation. This correction is confirmed by direct !1protein sequencing in the region of the error. COMMENT This gene lies immediately 3' to Spo0F but is not part of !1the same cistron. GENETICS !$#gene fbaA CLASSIFICATION #superfamily fructose-bisphosphate aldolase II KEYWORDS aldehyde-lyase; carbon-carbon lyase; phosphoprotein SUMMARY #length 285 #molecular-weight 30400 #checksum 391 SEQUENCE /// ENTRY ADPSGP #type complete TITLE 2-dehydro-3-deoxy-phosphogluconate aldolase (EC 4.1.2.14) [validated] - Pseudomonas putida (tentative sequence) ALTERNATE_NAMES phospho-2-dehydro-3-deoxygluconate aldolase; phospho-2-keto-3-deoxygluconate aldolase ORGANISM #formal_name Pseudomonas putida DATE 30-Nov-1980 #sequence_revision 30-Nov-1980 #text_change 03-Jun-2002 ACCESSIONS A01105 REFERENCE A92273 !$#authors Suzuki, N.; Wood, W.A. !$#journal J. Biol. Chem. (1980) 255:3427-3435 !$#title Complete primary structure of !12-keto-3-deoxy-6-phosphogluconate aldolase. !$#cross-references MUID:80159956; PMID:6988426 !$#accession A01105 !'##molecule_type protein !'##residues 1-225 ##label SUZ REFERENCE A90397 !$#authors Mavridis, I.M.; Tulinsky, A. !$#journal Biochemistry (1976) 15:4410-4417 !$#title The folding and quaternary structure of trimeric !12-keto-3-deoxy-6-phosphogluconic aldolase at 3.5-angstrom !1resolution. !$#cross-references MUID:77022062; PMID:974067 !$#contents annotation; X-ray crystallography, 3.5 angstroms CLASSIFICATION #superfamily 2-dehydro-3-deoxyphosphogluconate aldolase KEYWORDS aldehyde-lyase; carbon-carbon lyase; homotrimer FEATURE !$56,60,63 #active_site Glu, Arg, His #status predicted\ !$144 #active_site Lys (covalent pyruvate-binding) #status !8experimental SUMMARY #length 225 #molecular-weight 23937 #checksum 6637 SEQUENCE /// ENTRY ADECOG #type complete TITLE 2-dehydro-3-deoxy-phosphogluconate aldolase (EC 4.1.2.14) - Escherichia coli (strain K-12) ALTERNATE_NAMES 2-keto-4-hydroxyglutarate aldolase (KHG aldolase); phospho-2-keto-3-deoxygluconate aldolase (KDPG aldolase) CONTAINS 2-dehydro-3-deoxyphosphogluconate aldolase (EC 4.1.2.14) [validated]; 4-hydroxy-2-oxoglutarate aldolase (EC 4.1.3.16) [validated] ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 03-Jun-2002 ACCESSIONS B42986; A43308; A31067; S35912; A23672; B64947 REFERENCE A42986 !$#authors Egan, S.E.; Fliege, R.; Tong, S.; Shibata, A.; Wolf Jr., !1R.E.; Conway, T. !$#journal J. Bacteriol. (1992) 174:4638-4646 !$#title Molecular characterization of the Entner-Doudoroff pathway !1in Escherichia coli: sequence analysis and localization of !1promoters for the edd-eda operon. !$#cross-references MUID:92325055; PMID:1624451 !$#accession B42986 !'##molecule_type DNA !'##residues 1-213 ##label EGA !'##cross-references GB:M87458; GB:M87456; NID:g145825; PIDN:AAA23723.1; !1PID:g145827 !'##note sequence extracted from NCBI backbone (NCBIN:108145, !1NCBIP:108147) REFERENCE A43308 !$#authors Patil, R.V.; Dekker, E.E. !$#journal J. Bacteriol. (1992) 174:102-107 !$#title Cloning, nucleotide sequence, overexpression, and !1inactivation of the Escherichia coli !12-keto-4-hydroxyglutarate aldolase gene. !$#cross-references MUID:92104948; PMID:1339418 !$#accession A43308 !'##molecule_type DNA !'##residues 1-213 ##label PAT !'##cross-references GB:X68871; GB:S75227; NID:g41688; PIDN:CAA48732.1; !1PID:g41689 !'##experimental_source K-12, strain W-1485 !'##note sequence extracted from NCBI backbone (NCBIN:75227, !1NCBIP:75228) REFERENCE A31067 !$#authors Vlahos, C.J.; Dekker, E.E. !$#journal J. Biol. Chem. (1988) 263:11683-11691 !$#title The complete amino acid sequence and identification of the !1active-site arginine peptide of Escherichia coli !12-keto-4-hydroxyglutarate aldolase. !$#cross-references MUID:88298837; PMID:3136164 !$#accession A31067 !'##molecule_type protein !'##residues 1-213 ##label VLA REFERENCE S35910 !$#authors Carter, A.T. !$#submission submitted to the EMBL Data Library, January 1992 !$#accession S35912 !'##molecule_type DNA !'##residues 1-213 ##label CAR !'##cross-references EMBL:X63694; NID:g395401; PIDN:CAA45222.1; !1PID:g395404 !'##experimental_source strain K-12 REFERENCE A23672 !$#authors Vlahos, C.J.; Dekker, E.E. !$#journal J. Biol. Chem. (1990) 265:20384-20389 !$#title Active-site residues of 2-keto-4-hydroxyglutarate aldolase !1from Escherichia coli. Bromopyruvate inactivation and !1labeling of glutamate 45. !$#cross-references MUID:91056084; PMID:1978721 !$#accession A23672 !'##status preliminary !'##molecule_type mRNA !'##residues 'SV',36,'CI',39-41;44-49;158-170 ##label VL2 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64947 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-213 ##label BLAT !'##cross-references GB:AE000279; GB:U00096; NID:g1788154; !1PIDN:AAC74920.1; PID:g1788156; UWGP:b1850 !'##experimental_source strain K-12, substrain MG1655 COMMENT The enzyme is a class I "lysine-type" aldolase. GENETICS !$#gene eda; hga; kdgA !$#map_position 4 min COMPLEX homotrimer FUNCTION KHG !$#description as 4-hydroxy-2-oxoglutarate aldolase catalyzes the formation !1of 4-hydroxy-2-oxoglutarate from pyruvate and glyoxylate !$#note participates in regulating the intracellular level of !1glyoxylate FUNCTION KDPG !$#description as 2-dehydro-3-deoxyphosphogluconate aldolase catalyzes the !1formation of 2-dehydro-3-deoxyphosphogluconate from pruvate !1and glyceraldehyde 3-phosphate !$#pathway Entner-Doudoroff pathway CLASSIFICATION #superfamily 2-dehydro-3-deoxyphosphogluconate aldolase KEYWORDS aldehyde-lyase; carbon-carbon lyase; homotrimer; !1oxo-acid-lyase FEATURE !$45 #active_site Glu #status predicted\ !$49 #active_site Arg #status experimental\ !$133 #active_site Lys (covalent pyruvate-binding) #status !8experimental SUMMARY #length 213 #molecular-weight 22284 #checksum 478 SEQUENCE /// ENTRY ADECHF #type complete TITLE 2-dehydro-3-deoxy-phosphoheptonate aldolase (EC 4.1.2.15) (Phe-sensitive) - Escherichia coli (strain K-12) ALTERNATE_NAMES phospho-2-dehydro-3-deoxyheptonate aldolase; phospho-2-keto-3-deoxyheptonate aldolase ORGANISM #formal_name Escherichia coli DATE 18-Aug-1982 #sequence_revision 17-Dec-1982 #text_change 03-Jun-2002 ACCESSIONS A01106; B64811 REFERENCE A01106 !$#authors Davies, W.D.; Davidson, B.E. !$#journal Nucleic Acids Res. (1982) 10:4045-4058 !$#title The nucleotide sequence of aroG, the gene for !13-deoxy-D-arabinoheptulosonate-7 phosphate synthetase (phe) !1in Escherichia coli K12. !$#cross-references MUID:82274236; PMID:6125934 !$#accession A01106 !'##molecule_type DNA !'##residues 1-350 ##label DAV !'##cross-references GB:J01591; NID:g145367; PIDN:AAA23492.1; !1PID:g145368 !'##experimental_source strain K12 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64811 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-350 ##label BLAT !'##cross-references GB:AE000178; GB:U00096; NID:g1786967; !1PIDN:AAC73841.1; PID:g1786969; UWGP:b0754 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene aroG !$#map_position 17 min FUNCTION !$#description aldehyde-lyase; carbon-carbon lyase; this is one of the DAHP !1synthases that catalyze condensation of phosphoenolpyruvate !1and D-erythrose-4-phosphate to form !13-deoxy-D-arabinoheptulosonic acid-7-phosphate !$#pathway aromatic amino acid biosynthesis; shikimate pathway !$#note the first reaction in aromatic amino acid biosynthesis !$#note feedback-inhibited by phenylalanine; the other two DAHP !1synthases are tyrosine- and tryptophan-sensitive, !1respectively CLASSIFICATION #superfamily phospho-2-dehydro-3-deoxyheptonate aldolase KEYWORDS aldehyde-lyase; aromatic amino acid biosynthesis; !1carbon-carbon lyase; shikimate pathway SUMMARY #length 350 #molecular-weight 38009 #checksum 9580 SEQUENCE /// ENTRY ADECH #type complete TITLE 2-dehydro-3-deoxy-phosphoheptonate aldolase (EC 4.1.2.15) (Trp-sensitive) - Escherichia coli (strain K-12) ALTERNATE_NAMES 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase; phospho-2-dehydro-3-deoxyheptonate aldolase; phospho-2-keto-3-deoxyheptonate aldolase ORGANISM #formal_name Escherichia coli DATE 22-May-1981 #sequence_revision 31-Oct-1997 #text_change 03-Jun-2002 ACCESSIONS H64928; JQ1131; A31384; A01107 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64928 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-348 ##label BLAT !'##cross-references GB:AE000265; GB:U00096; NID:g2367122; !1PIDN:AAC74774.1; PID:g1787996; UWGP:b1704 !'##experimental_source strain K-12, substrain MG1655 REFERENCE JQ1131 !$#authors Hudson, G.S.; Rellos, P.; Davidson, B.E. !$#journal Gene (1991) 102:87-91 !$#title Two promoters control the aroH gene of Escherichia coli. !$#cross-references MUID:91323737; PMID:1677907 !$#accession JQ1131 !'##molecule_type DNA !'##residues 1-332,'S',334-348 ##label HUD !'##cross-references GB:M38266; NID:g145376; PIDN:AAA23497.1; !1PID:g145378 REFERENCE A31384 !$#authors Ray, J.M.; Yanofsky, C.; Bauerle, R. !$#journal J. Bacteriol. (1988) 170:5500-5506 !$#title Mutational analysis of the catalytic and feedback sites of !1the tryptophan-sensitive !13-deoxy-D-arabino-heptulosonate-7-phosphate synthase of !1Escherichia coli. !$#cross-references MUID:89053867; PMID:2903857 !$#accession A31384 !'##molecule_type DNA !'##residues 1-122,'A',124-202;204,'Q',206-332,'RQ',335-348 ##label RAY !'##cross-references GB:J04221 REFERENCE A01107 !$#authors Zurawski, G.; Gunsalus, R.P.; Brown, K.D.; Yanofsky, C. !$#journal J. Mol. Biol. (1981) 145:47-73 !$#title Structure and regulation of aroH, the structural gene for !1the tryptophan-repressible 3-deoxy-D-arabino-heptulosonic !1acid-7-phosphate synthetase of Escherichia coli. !$#cross-references MUID:81267314; PMID:6167722 !$#accession A01107 !'##molecule_type DNA !'##residues 1-36;231-332,'RQ',335-348 ##label ZUR !'##cross-references GB:J01592; GB:J01593 GENETICS !$#gene aroH !$#map_position 37 min FUNCTION !$#description aldehyde-lyase; carbon-carbon lyase; this is one of the DAHP !1synthases that catalyze condensation of phosphoenolpyruvate !1and D-erythrose-4-phosphate to form !13-deoxy-D-arabinoheptulosonic acid-7-phosphate !$#pathway aromatic amino acid biosynthesis; shikimate pathway !$#note the first reaction in aromatic amino acid biosynthesis !$#note feedback-inhibited by tryptophan; the other two DAHP !1synthases are tyrosine- and phenylalanine-sensitive, !1respectively CLASSIFICATION #superfamily phospho-2-dehydro-3-deoxyheptonate aldolase KEYWORDS aldehyde-lyase; aromatic amino acid biosynthesis; !1carbon-carbon lyase; shikimate pathway SUMMARY #length 348 #molecular-weight 38735 #checksum 7543 SEQUENCE /// ENTRY JN0865 #type complete TITLE 2-dehydro-3-deoxy-phosphoheptonate aldolase (EC 4.1.2.15) ARO3 - yeast (Candida albicans) ALTERNATE_NAMES 3-deoxy-D-arabinoheptulosonate-7-phosphate synthase ORGANISM #formal_name Candida albicans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS JN0865 REFERENCE JN0865 !$#authors Pereira, S.A.; Livi, G.P. !$#journal Gene (1993) 132:159-165 !$#title Cloning and expression of the ARO3 gene encoding DAHP !1synthase from Candida albicans. !$#cross-references MUID:94040757; PMID:7901125 !$#accession JN0865 !'##molecule_type mRNA !'##residues 1-368 ##label PER !'##cross-references GB:L12217; NID:g410314; PIDN:AAA71966.1; !1PID:g410315 COMMENT This enzyme catalyzes the condensation of !1erythrose-4-phosphate and phosphoenol pyruvate to !13-deoxy-D-arabinoheptulosonate-7-phosphate. GENETICS !$#gene ARO3 CLASSIFICATION #superfamily phospho-2-dehydro-3-deoxyheptonate aldolase KEYWORDS aldehyde-lyase; aromatic amino acid biosynthesis; !1carbon-carbon lyase SUMMARY #length 368 #molecular-weight 40730 #checksum 4968 SEQUENCE /// ENTRY A35253 #type complete TITLE 2-dehydro-3-deoxy-phosphoheptonate aldolase (EC 4.1.2.15) - Salmonella typhimurium ALTERNATE_NAMES phospho-2-dehydro-3-deoxyheptonate aldolase ORGANISM #formal_name Salmonella typhimurium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS A35253 REFERENCE A35253 !$#authors Muday, G.K.; Herrmann, K.M. !$#journal J. Bacteriol. (1990) 172:2259-2266 !$#title Regulation of the Salmonella typhimurium aroF gene in !1Escherichia coli. !$#cross-references MUID:90236877; PMID:1970560 !$#accession A35253 !'##status preliminary !'##molecule_type DNA !'##residues 1-356 ##label MUD !'##cross-references GB:M31302; NID:g153879; PIDN:AAA27030.1; !1PID:g153880 CLASSIFICATION #superfamily phospho-2-dehydro-3-deoxyheptonate aldolase KEYWORDS aldehyde-lyase; carbon-carbon lyase SUMMARY #length 356 #molecular-weight 38727 #checksum 3491 SEQUENCE /// ENTRY I40837 #type complete TITLE 2-dehydro-3-deoxy-phosphoheptonate aldolase (EC 4.1.2.15) - Corynebacterium glutamicum ALTERNATE_NAMES 3-deoxy-D-arabinoheptulosonate-7-phosphate synthase ORGANISM #formal_name Corynebacterium glutamicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS I40837 REFERENCE I40837 !$#authors Chen, C. !$#journal FEMS Microbiol. Lett. (1993) 107:223-230 !$#title The cloning and nucleotide sequence of Corynebacterium !1glutamicum 3-deoxy-D-arabinoheptulosonate-7-phosphate !1synthase gene. !$#cross-references MUID:93231468; PMID:8097175 !$#accession I40837 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-367 ##label RES !'##cross-references GB:L07603; NID:g144964; PIDN:AAA23292.1; !1PID:g144965 CLASSIFICATION #superfamily phospho-2-dehydro-3-deoxyheptonate aldolase KEYWORDS aldehyde-lyase; carbon-carbon lyase SUMMARY #length 367 #molecular-weight 39305 #checksum 2207 SEQUENCE /// ENTRY ADECHY #type complete TITLE 2-dehydro-3-deoxy-phosphoheptonate aldolase (EC 4.1.2.15) (Tyr-sensitive) - Escherichia coli (strain K-12) ALTERNATE_NAMES phospho-2-dehydro-3-deoxyheptonate aldolase; phospho-2-keto-3-deoxyheptonate aldolase ORGANISM #formal_name Escherichia coli DATE 30-Apr-1982 #sequence_revision 27-Feb-1997 #text_change 03-Jun-2002 ACCESSIONS I41141; A01108; I41142; A37154; D65038 REFERENCE I41141 !$#authors Shultz, J.; Hermodson, M.A.; Garner, C.C.; Herrmann, K.M. !$#journal J. Biol. Chem. (1984) 259:9655-9661 !$#title The nucleotide sequence of the aroF gene of Escherichia coli !1and the amino acid sequence of the encoded protein, the !1tyrosine-sensitive 3-deoxy-D-arabino-heptulosonate !17-phosphate synthase. !$#cross-references MUID:84264621; PMID:6146618 !$#accession I41141 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-356 ##label RES !'##cross-references GB:K01989; NID:g145361; PIDN:AAA23489.1; !1PID:g145362 REFERENCE A01108 !$#authors Herrmann, K.M.; Shultz, J.; Hermodson, M.A. !$#journal J. Biol. Chem. (1980) 255:7079-7081 !$#title Sequence homology between the tyrosine-sensitive !13-deoxy-D-arabino-heptulosonate 7-phosphate synthase from !1Escherichia coli and hemerythrin from Sipunculida. !$#cross-references MUID:80227887; PMID:6104668 !$#accession A01108 !'##molecule_type protein !'##residues 1-30 ##label HER REFERENCE I41142 !$#authors Garner, C.C.; Herrmann, K.M. !$#journal J. Biol. Chem. (1985) 260:3820-3825 !$#title Operator mutations of the escherichia coli aroF gene. !$#cross-references MUID:85131196; PMID:2857723 !$#accession I41142 !'##status preliminary !'##molecule_type DNA !'##residues 1-6 ##label RE2 !'##cross-references GB:K03453; NID:g145363; PIDN:AAA23490.1; !1PID:g145364 REFERENCE A37154 !$#authors Weaver, L.M.; Herrmann, K.M. !$#journal J. Bacteriol. (1990) 172:6581-6584 !$#title Cloning of an aroF allele encoding a tyrosine-insensitive !13-deoxy-D-arabino-heptulosonate 7-phosphate synthase. !$#cross-references MUID:91035275; PMID:1977738 !$#accession A37154 !'##status preliminary !'##molecule_type DNA !'##residues 124-187 ##label WEA !'##cross-references GB:M60890; NID:g145365; PIDN:AAA23491.1; !1PID:g145366 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65038 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-356 ##label BLAT !'##cross-references GB:AE000346; GB:U00096; NID:g2367141; !1PIDN:AAC75650.1; PID:g1788953; UWGP:b2601 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene aroF !$#map_position 57 min FUNCTION !$#description aldehyde-lyase; carbon-carbon lyase; this is one of the DAHP !1synthases that catalyze condensation of phosphoenolpyruvate !1and D-erythrose-4-phosphate to form !13-deoxy-D-arabinoheptulosonic acid-7-phosphate !$#pathway aromatic amino acid biosynthesis; shikimate pathway !$#note the first reaction in aromatic amino acid biosynthesis !$#note feedback-inhibited by tyrosine; the other two DAHP synthases !1are tryptophan- and phenylalanine-sensitive, respectively CLASSIFICATION #superfamily phospho-2-dehydro-3-deoxyheptonate aldolase KEYWORDS aldehyde-lyase; aromatic amino acid biosynthesis; !1carbon-carbon lyase; shikimate pathway SUMMARY #length 356 #molecular-weight 38804 #checksum 3817 SEQUENCE /// ENTRY WZCNIU #type complete TITLE isocitrate lyase (EC 4.1.3.1) - upland cotton ALTERNATE_NAMES isocitrase; isocitratase; isocitritase ORGANISM #formal_name Gossypium hirsutum #common_name upland cotton DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS S10771; S10396 REFERENCE S10771 !$#authors Turley, R.B.; Choe, S.M.; Trelease, R.N. !$#journal Biochim. Biophys. Acta (1990) 1049:223-226 !$#title Characterization of a cDNA clone encoding the complete amino !1acid sequence of cotton isocitrate lyase. !$#cross-references MUID:90304228; PMID:2194576 !$#accession S10771 !'##molecule_type mRNA !'##residues 1-576 ##label TUR !'##cross-references EMBL:X52136; NID:g18485; PIDN:CAA36381.1; !1PID:g18486 COMMENT This enzyme catalyzes the reversible conversion of !1isocitrate to succinate and glyoxylate. This is the first !1step in the glyoxylate bypass, an alternate to the !1tricarboxylic acid cycle. It is involved in mobilization of !1sored lipids during the growth of higher plant seedlings. CLASSIFICATION #superfamily isocitrate lyase KEYWORDS carbon-carbon lyase; glyoxylate bypass; oxo-acid-lyase SUMMARY #length 576 #molecular-weight 64733 #checksum 5014 SEQUENCE /// ENTRY WZCSI #type complete TITLE isocitrate lyase (EC 4.1.3.1) - castor bean ALTERNATE_NAMES isocitrase; isocitratase; isocitritase ORGANISM #formal_name Ricinus communis var. zanzibarensis #common_name castor bean DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS S06274 REFERENCE S06274 !$#authors Beeching, J.R.; Northcote, D.H. !$#journal Plant Mol. Biol. (1987) 8:471-475 !$#title Nucleic acid (cDNA) and amino acid sequences of isocitrate !1lyase from castor bean. !$#accession S06274 !'##molecule_type mRNA !'##residues 1-576 ##label BEE !'##cross-references GB:M17145; NID:g169706; PIDN:AAA53378.1; !1PID:g169707 COMMENT This enzyme catalyzes the reversible conversion of !1isocitrate to succinate and glyoxylate. This is the first !1step in the glyoxylate bypass, an alternate to the !1tricarboxylic acid cycle. It is involved in storage lipid !1mobilization during the growth of higher plant seedlings. CLASSIFICATION #superfamily isocitrate lyase KEYWORDS carbon-carbon lyase; glyoxylate bypass; oxo-acid-lyase SUMMARY #length 576 #molecular-weight 64751 #checksum 2498 SEQUENCE /// ENTRY WZRPI #type complete TITLE isocitrate lyase (EC 4.1.3.1) - rape ALTERNATE_NAMES isocitrase; isocitratase; isocitritase ORGANISM #formal_name Brassica napus #common_name rape DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 30-Jun-1993 ACCESSIONS JQ1105 REFERENCE JQ1105 !$#authors Comai, L.; Dietrich, R.A.; Maslyar, D.J.; Baden, C.S.; !1Harada, J.J. !$#journal Plant Cell (1989) 1:293-300 !$#title Coordinate expression of transcriptionally regulated !1isocitrate lyase and malate synthase genes in Brassica napus !1L. !$#cross-references MUID:92393389; PMID:2535504 !$#accession JQ1105 !'##molecule_type mRNA !'##residues 1-576 ##label COM COMMENT This enzyme catalyzes the reversible conversion of !1isocitrate to succinate and glyoxylate. This is the first !1step in the glyoxylate bypass, an alternate to the !1tricarboxylic acid cycle. It is involved in storage lipid !1mobilization during the growth of higher plant seedlings. CLASSIFICATION #superfamily isocitrate lyase KEYWORDS carbon-carbon lyase; glyoxylate bypass; oxo-acid-lyase SUMMARY #length 576 #molecular-weight 64325 #checksum 341 SEQUENCE /// ENTRY WZBYI #type complete TITLE isocitrate lyase (EC 4.1.3.1) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES isocitrase; isocitratase; isocitritase; protein YER065c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 10-May-2001 ACCESSIONS S22386; S31850; S50568; S17026; S28235 REFERENCE S22386 !$#authors Fernandez, E.; Moreno, F.; Rodicio, R. !$#journal Eur. J. Biochem. (1992) 204:983-990 !$#title The ICL1 gene from Saccharomyces cerevisiae. !$#cross-references MUID:92201212; PMID:1551398 !$#accession S22386 !'##molecule_type DNA !'##residues 1-557 ##label FER !'##cross-references EMBL:X61271; NID:g3807; PIDN:CAA43575.1; PID:g3808 REFERENCE S31850 !$#authors Schoeler, A.; Schueller, H.J. !$#journal Curr. Genet. (1993) 23:375-381 !$#title Structure and regulation of the isocitrate lyase gene ICL1 !1from the yeast Saccharomyces cerevisiae. !$#cross-references MUID:93306737; PMID:8319292 !$#accession S31850 !'##molecule_type DNA !'##residues 1-557 ##label SCH !'##cross-references EMBL:X65554; NID:g3809; PIDN:CAA46523.1; PID:g3810 REFERENCE S50427 !$#authors Dietrich, F.S. !$#submission submitted to the EMBL Data Library, December 1994 !$#description The sequence of S. cerevisiae lambda clones 6592, 4678, !14742, and 3612. !$#accession S50568 !'##molecule_type DNA !'##residues 1-557 ##label DIE !'##cross-references EMBL:U18813; NID:g1381127; PIDN:AAB64601.1; !1PID:g603301; GSPDB:GN00005; MIPS:YER065c GENETICS !$#gene SGD:ICL1; MIPS:YER065c !'##cross-references SGD:S0000867; MIPS:YER065c !$#map_position 5R FUNCTION !$#description catalyzes the reversible conversion of isocitrate to !1succinate and glyoxylate !$#pathway glyoxylate bypass !$#note first step CLASSIFICATION #superfamily isocitrate lyase KEYWORDS carbon-carbon lyase; glyoxylate bypass; oxo-acid-lyase SUMMARY #length 557 #molecular-weight 62408 #checksum 9264 SEQUENCE /// ENTRY WZCKI #type complete TITLE isocitrate lyase (EC 4.1.3.1), peroxisomal - yeast (Candida tropicalis) ALTERNATE_NAMES isocitrase; isocitratase; isocitritase ORGANISM #formal_name Candida tropicalis DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jun-2000 ACCESSIONS JX0105 REFERENCE JX0105 !$#authors Atomi, H.; Ueda, M.; Hikida, M.; Hishida, T.; Teranishi, Y.; !1Tanaka, A. !$#journal J. Biochem. (1990) 107:262-266 !$#title Peroxisomal isocitrate lyase of the n-alkane-assimilating !1yeast Candida tropicalis: gene analysis and !1characterization. !$#cross-references MUID:90299863; PMID:2361956 !$#accession JX0105 !'##molecule_type DNA !'##residues 1-550 ##label ATO !'##cross-references GB:D00703; NID:g218381; PIDN:BAA00611.1; !1PID:g218382 COMMENT This enzyme catalyzes the reversible conversion of !1isocitrate to succinate and glyoxylate. This is the first !1step in the glyoxylate bypass, an alternate to the !1tricarboxylic acid cycle. CLASSIFICATION #superfamily isocitrate lyase KEYWORDS carbon-carbon lyase; glyoxylate bypass; oxo-acid-lyase; !1peroxisome SUMMARY #length 550 #molecular-weight 61576 #checksum 1135 SEQUENCE /// ENTRY WZECIC #type complete TITLE isocitrate lyase (EC 4.1.3.1) - Escherichia coli (strain K-12) ALTERNATE_NAMES isocitrase; isocitratase; isocitritase ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 30-Sep-1992 #text_change 01-Mar-2002 ACCESSIONS S05692; S05691; A31837; S00931; A32016; F65208 REFERENCE S05692 !$#authors Byrne, C. !$#submission submitted to the EMBL Data Library, July 1988 !$#accession S05692 !'##molecule_type DNA !'##residues 1-434 ##label BYR1 !'##cross-references EMBL:X12431; NID:g40886; PIDN:CAA30974.1; !1PID:g40888 REFERENCE S01438 !$#authors Byrne, C.; Stokes, H.W.; Ward, K.A. !$#journal Nucleic Acids Res. (1988) 16:9342 !$#title Nucleotide sequence of the aceB gene encoding malate !1synthase A in Escherichia coli. !$#cross-references MUID:89016638; PMID:3050899 !$#accession S05691 !'##molecule_type DNA !'##residues 1-23 ##label BYR2 !'##cross-references EMBL:X12431 REFERENCE A31837 !$#authors Matsuoka, M.; McFadden, B.A. !$#journal J. Bacteriol. (1988) 170:4528-4536 !$#title Isolation, hyperexpression, and sequencing of the aceA gene !1encoding isocitrate lyase in Escherichia coli. !$#cross-references MUID:89008064; PMID:3049537 !$#accession A31837 !'##molecule_type DNA !'##residues 1-418,'DVFSHRADRLH' ##label MAT !'##cross-references GB:M22621; NID:g340728; PIDN:AAC13650.1; !1PID:g556177 REFERENCE S00931 !$#authors Rieul, C.; Bleicher, F.; Duclos, B.; Cortay, J.C.; Cozzone, !1A.J. !$#journal Nucleic Acids Res. (1988) 16:5689 !$#title Nucleotide sequence of the aceA gene coding for isocitrate !1lyase in Escherichia coli. !$#cross-references MUID:88262573; PMID:3290857 !$#accession S00931 !'##molecule_type DNA !'##residues 1-100,'WRPACIRISRSIRQTRC',118-214,'P',216-337,'E',339-434 !1##label RIE !'##cross-references GB:X07543; NID:g40884; PIDN:CAA30416.1; PID:g40885 REFERENCE A32016 !$#authors Klumpp, D.J.; Plank, D.W.; Bowdin, L.J.; Stueland, C.S.; !1Chung, T.; LaPorte, D.C. !$#journal J. Bacteriol. (1988) 170:2763-2769 !$#title Nucleotide sequence of aceK, the gene encoding isocitrate !1dehydrogenase kinase/phosphatase. !$#cross-references MUID:88227861; PMID:2836370 !$#accession A32016 !'##molecule_type DNA !'##residues 'R',294-434 ##label KLU !'##cross-references GB:M20714; NID:g146442; PIDN:AAA24009.1; !1PID:g146443 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65208 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-434 ##label BLAT !'##cross-references GB:AE000474; GB:U00096; NID:g1790440; !1PIDN:AAC76985.1; PID:g1790445; UWGP:b4015 !'##experimental_source strain K-12, substrain MG1655 COMMENT This enzyme catalyzes the reversible conversion of !1isocitrate to succinate and glyoxylate. This is the first !1step in the glyoxylate bypass, an alternate to the !1tricarboxylic acid cycle. GENETICS !$#gene aceA !$#map_position 91 min CLASSIFICATION #superfamily isocitrate lyase KEYWORDS carbon-carbon lyase; glyoxylate bypass; oxo-acid-lyase SUMMARY #length 434 #molecular-weight 47521 #checksum 2396 SEQUENCE /// ENTRY S52819 #type complete TITLE isocitrate lyase (EC 4.1.3.1) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein LPZ6c; hypothetical protein YP9723.06c; protein YPR006c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Dec-1999 ACCESSIONS S52819; S59751 REFERENCE S52814 !$#authors Pearson, D.; Bowman, S. !$#submission submitted to the EMBL Data Library, April 1995 !$#accession S52819 !'##molecule_type DNA !'##residues 1-575 ##label PEA !'##cross-references EMBL:Z48951; NID:g762999; PIDN:CAA88784.1; !1PID:g763005; GSPDB:GN00016; MIPS:YPR006c !'##experimental_source strain AB972 REFERENCE S59746 !$#authors Wang, Y.; Ahmed, A.; Bussey, H.; Fortin, N.; Friesen, J.D.; !1Hall, J.; Storms, R.K.; Vo, D.H.; Winnett, E. !$#submission submitted to the EMBL Data Library, July 1995 !$#description The sequence of Saccharomyces cerevisiae chromosome XVI !1right arm. !$#accession S59751 !'##molecule_type DNA !'##residues 1-575 ##label WAN !'##cross-references EMBL:U31900; NID:g1276597; PIDN:AAA97585.1; !1PID:g939740; GSPDB:GN00016; MIPS:YPR006c GENETICS !$#gene SGD:ICL2; MIPS:YPR006c !'##cross-references SGD:S0006210; MIPS:YPR006c !$#map_position 16R FUNCTION !$#description catalyzes the reversible conversion of isocitrate to !1succinate and glyoxylate CLASSIFICATION #superfamily isocitrate lyase KEYWORDS carbon-carbon lyase; oxo-acid-lyase SUMMARY #length 575 #molecular-weight 64975 #checksum 543 SEQUENCE /// ENTRY SYECMA #type complete TITLE malate synthase (EC 4.1.3.2) A - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 01-Mar-2002 ACCESSIONS A32649; A30378; E65208; Q00592 REFERENCE S05692 !$#authors Byrne, C. !$#submission submitted to the EMBL Data Library, July 1988 !$#accession A32649 !'##molecule_type DNA !'##residues 1-533 ##label BYR1 REFERENCE A30378 !$#authors Byrne, C.R.; Stokes, H.W.; Ward, K.A. !$#journal Nucleic Acids Res. (1988) 16:10924 !$#title Nucleotide sequence of the aceB gene encoding malate !1synthase A in Escherichia coli. !$#cross-references MUID:89083515; PMID:3060852 !$#accession A30378 !'##molecule_type DNA !'##residues 1-533 ##label BYR2 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65208 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-533 ##label BLAT !'##cross-references GB:AE000474; GB:U00096; NID:g1790440; !1PIDN:AAC76984.1; PID:g1790444; UWGP:b4014 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene aceB !$#map_position 91 min CLASSIFICATION #superfamily malate synthase KEYWORDS carbon-carbon lyase; coenzyme A; glyoxylate bypass; !1oxo-acid-lyase SUMMARY #length 533 #molecular-weight 60273 #checksum 1098 SEQUENCE /// ENTRY SYRPMA #type complete TITLE malate synthase (EC 4.1.3.2), glyoxysomal - rape ORGANISM #formal_name Brassica napus #common_name rape DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 05-May-2000 ACCESSIONS A31428 REFERENCE A31428 !$#authors Comai, L.; Baden, C.S.; Harada, J.J. !$#journal J. Biol. Chem. (1989) 264:2778-2782 !$#title Deduced sequence of a malate synthase polypeptide encoded by !1a subclass of the gene family. !$#cross-references MUID:89123375; PMID:2914930 !$#accession A31428 !'##molecule_type DNA !'##residues 1-561 ##label COM !'##cross-references GB:J04468; NID:g167149; PIDN:AAA32996.1; !1PID:g167150 COMMENT This enzyme, together with isocitrate lyase, is very !1important to the glyoxylate cycle, which catalyzes the net !1conversion of acetate into succinate. CLASSIFICATION #superfamily malate synthase KEYWORDS carbon-carbon lyase; coenzyme A; glyoxylate bypass; !1glyoxysome; oxo-acid-lyase FEATURE !$559-561 #region peroxisome/glyoxysome location signal !8(S-[RKH]-L) motif SUMMARY #length 561 #molecular-weight 63728 #checksum 326 SEQUENCE /// ENTRY SYKVMA #type complete TITLE malate synthase (EC 4.1.3.2) - cucumber ALTERNATE_NAMES glyoxylate transacetylase; malate condensing enzyme; malate synthetase ORGANISM #formal_name Cucumis sativus #common_name cucumber DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 05-May-2000 ACCESSIONS S07550; JQ0170 REFERENCE S07550 !$#authors Graham, I.A.; Smith, L.M.; Brown, J.W.S.; Leaver, C.J.; !1Smith, S.M. !$#journal Plant Mol. Biol. (1989) 13:673-684 !$#title The malate synthase gene of cucumber. !$#cross-references MUID:91370851; PMID:2491683 !$#accession S07550 !'##molecule_type DNA !'##residues 1-568 ##label GRA !'##cross-references GB:M16219 REFERENCE JQ0170 !$#authors Smith, S.M.; Leaver, C.J. !$#journal Plant Physiol. (1986) 81:762-767 !$#title Glyoxysomal malate synthase of cucumber: molecular cloning !1of a cDNA and regulation of enzyme synthesis during !1germination. !$#accession JQ0170 !'##molecule_type mRNA !'##residues 'G',476-568 ##label SMI !'##cross-references GB:M16219; NID:g167520; PIDN:AAA33123.1; !1PID:g167521 COMMENT This enzyme, together with isocitrate lyase, is very !1important to the glyoxylate cycle, which catalyzes the net !1conversion of acetate into succinate. GENETICS !$#introns 131/3; 240/2; 350/3 CLASSIFICATION #superfamily malate synthase KEYWORDS carbon-carbon lyase; coenzyme A; glyoxylate bypass; !1glyoxysome; oxo-acid-lyase FEATURE !$566-568 #region peroxisome/glyoxysome location signal !8(S-[RKH]-L) motif SUMMARY #length 568 #molecular-weight 64961 #checksum 8514 SEQUENCE /// ENTRY SYCNMU #type complete TITLE malate synthase (EC 4.1.3.2) - upland cotton ORGANISM #formal_name Gossypium hirsutum #common_name upland cotton DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 05-May-2000 ACCESSIONS S12735 REFERENCE S12735 !$#authors Turley, R.B.; Choe, S.M.; Ni, W.; Trelease, R.N. !$#journal Nucleic Acids Res. (1990) 18:3643 !$#title Nucleotide sequence of cottonseed malate synthase. !$#cross-references MUID:90301492; PMID:2362818 !$#accession S12735 !'##molecule_type mRNA !'##residues 1-567 ##label TUR !'##cross-references EMBL:X52305; NID:g18506; PIDN:CAA36546.1; !1PID:g18507 CLASSIFICATION #superfamily malate synthase KEYWORDS carbon-carbon lyase; coenzyme A; glyoxylate bypass; !1glyoxysome; oxo-acid-lyase FEATURE !$565-567 #region peroxisome/glyoxysome location signal !8(S-[RKH]-L) motif SUMMARY #length 567 #molecular-weight 64668 #checksum 4105 SEQUENCE /// ENTRY SYCSM2 #type complete TITLE malate synthase (EC 4.1.3.2) (clone MS2) - castor bean ORGANISM #formal_name Ricinus communis #common_name castor bean DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 05-May-2000 ACCESSIONS S14677; S11631; S11636; S14678 REFERENCE S14677 !$#authors Rodriguez, D.; Ginger, R.S.; Baker, A.; Northcote, D.H. !$#journal Plant Mol. Biol. (1990) 15:501-504 !$#title Nucleotide sequence analysis of a cDNA clone encoding malate !1synthase of castor bean (Ricinus communis) reveals homology !1to DAL7, a gene involved in allantoin degradation in !1Saccharomyces cerevisiae. !$#cross-references MUID:91355898; PMID:2103467 !$#accession S14677 !'##molecule_type mRNA !'##residues 1-567 ##label ROD !'##cross-references EMBL:X52806; NID:g21075; PIDN:CAA36994.1; !1PID:g21076 CLASSIFICATION #superfamily malate synthase KEYWORDS carbon-carbon lyase; coenzyme A; glyoxylate bypass; !1glyoxysome; oxo-acid-lyase FEATURE !$565-567 #region peroxisome/glyoxysome location signal !8(S-[RKH]-L) motif SUMMARY #length 567 #molecular-weight 64262 #checksum 2952 SEQUENCE /// ENTRY SYHQMA #type complete TITLE malate synthase (EC 4.1.3.2), microbody - yeast (Pichia angusta) ORGANISM #formal_name Pichia angusta DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 05-May-2000 ACCESSIONS S09294 REFERENCE S09294 !$#authors Bruinenberg, P.G.; Blaauw, M.; Kazemier, B.; AB, G. !$#journal Yeast (1990) 6:245-254 !$#title Cloning and sequencing of the malate synthase gene from !1Hansenula polymorpha. !$#cross-references MUID:90273778; PMID:2349836 !$#accession S09294 !'##molecule_type DNA !'##residues 1-555 ##label BRU COMMENT This enzyme, together with isocitrate lyase, is very !1important to the glyoxylate cycle, which catalyzes the net !1conversion of acetate into succinate. GENETICS !$#gene MAS CLASSIFICATION #superfamily malate synthase KEYWORDS carbon-carbon lyase; coenzyme A; glyoxylate bypass; !1oxo-acid-lyase; tricarboxylic acid cycle SUMMARY #length 555 #molecular-weight 63254 #checksum 6837 SEQUENCE /// ENTRY SYECOL #type complete TITLE 2-dehydro-3-deoxy-phosphooctonate aldolase (EC 4.1.2.16) - Escherichia coli (strain K-12) ALTERNATE_NAMES 3-deoxy-D-manno-octulosonic acid 8-phosphate synthetase; phospho-2-dehydro-3-deoxyoctonate aldolase ORGANISM #formal_name Escherichia coli DATE 31-Mar-1990 #sequence_revision 17-Oct-1997 #text_change 03-Jun-2002 ACCESSIONS I83573; D64868; A30390; Q00205 REFERENCE I60364 !$#authors Strohmaier, H.; Remler, P.; Renner, W.; Hogenauer, G. !$#journal J. Bacteriol. (1995) 177:4488-4500 !$#title Expression of genes kdsA and kdsB involved in !13-deoxy-D-manno-octulosonic acid metabolism and biosynthesis !1of enterobacterial lipopolysaccharide is growth phase !1regulated primarily at the transcriptional level in !1Escherichia coli K-12. !$#cross-references MUID:95362678; PMID:7543480 !$#accession I83573 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-284 ##label RES !'##cross-references EMBL:U18555; NID:g968925; PIDN:AAC43441.1; !1PID:g968934 !'##experimental_source strain K-12 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64868 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-284 ##label BLAT !'##cross-references GB:AE000219; GB:U00096; NID:g1787453; !1PIDN:AAC74299.1; PID:g1787466; UWGP:b1215 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A30390 !$#authors Woisetschlaeger, M.; Hoegenauer, G. !$#journal Mol. Gen. Genet. (1987) 207:369-373 !$#title The kdsA gene coding for 3-deoxy-D-manno-octulosonic acid !18-phosphate synthetase is part of an operon in Escherichia !1coli. !$#cross-references MUID:87286380; PMID:3039295 !$#accession A30390 !'##molecule_type DNA !'##residues 1-21,'L',23-284 ##label WOI !'##cross-references EMBL:X05552; NID:g41871; PIDN:CAA29067.1; !1PID:g940498 GENETICS !$#gene kdsA !$#map_position 27 min FUNCTION !$#description catalyzes the condensation of D-arabinose-5-phosphate and !1phosphoenolpyruvate to form !18-phospho-2-dehydro-3-deoxy-D-octonate that is then !1dephosphorylated enzymatically to D-manno-octulosonic acid, !1an integral part of bacterial liposaccharide !$#pathway lipopolysaccharide biosynthesis !$#note inhibited by ribose-5-phosphate CLASSIFICATION #superfamily phospho-2-dehydro-3-deoxyoctonate aldolase KEYWORDS aldehyde-lyase; carbon-carbon lyase; homotrimer; !1lipopolysaccharide biosynthesis SUMMARY #length 284 #molecular-weight 30832 #checksum 8556 SEQUENCE /// ENTRY C40626 #type complete TITLE dihydrodipicolinate synthase (EC 4.2.1.52) precursor [similarity] - Corynebacterium glutamicum ALTERNATE_NAMES L-2,3-dihydrodipicolinate synthetase ORGANISM #formal_name Corynebacterium glutamicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 17-Mar-2000 ACCESSIONS C40626; S12105 REFERENCE A40626 !$#authors Pisabarro, A.; Malumbres, M.; Mateos, L.M.; Oguiza, J.A.; !1Martin, J.F. !$#journal J. Bacteriol. (1993) 175:2743-2749 !$#title A cluster of three genes (dapA, orf2, and dapB) of !1Brevibacterium lactofermentum encodes dihydrodipicolinate !1synthase, dihydrodipicolinate reductase, and a third !1polypeptide of unknown function. !$#cross-references MUID:93239702; PMID:8478336 !$#accession C40626 !'##molecule_type DNA !'##residues 1-301 ##label PIS !'##cross-references GB:Z21502; GB:S59668; NID:g311767; PIDN:CAA79714.1; !1PID:g311770 !'##experimental_source ATCC 13869 !'##note sequence extracted from NCBI backbone (NCBIN:130448, !1NCBIP:130451) !'##note the source is designated as Brevibacterium lactofermentum REFERENCE S12105 !$#authors Bonnassie, S.; Oreglia, J.; Sicard, A.M. !$#journal Nucleic Acids Res. (1990) 18:6421 !$#title Nucleotide sequence of the dapA gene from Corynebacterium !1glutamicum. !$#cross-references MUID:91057127; PMID:2129555 !$#accession S12105 !'##molecule_type DNA !'##residues 1-265,'S',267-301 ##label BON !'##cross-references EMBL:X53993; NID:g40490; PIDN:CAA37940.1; !1PID:g40491 !'##experimental_source AS019 GENETICS !$#gene dapA FUNCTION !$#description catalyzes the condensation of pyruvate and L-aspartate !14-semialdehyde to L-2,3-dihydrodipicolinate !$#pathway diaminopimelate-lysine biosynthesis !$#note this enzyme may catalyze only the condensation of pyruvate !1and L-aspartate 4-semialdehyde to !1L-2-amino-6-oxo-4-heptenedioate CLASSIFICATION #superfamily dihydrodipicolinate synthase KEYWORDS carbon-oxygen lyase; diaminopimelate-lysine biosynthesis; !1hydro-lyase FEATURE !$173 #active_site Lys (covalent pyruvate-binding) #status !8predicted SUMMARY #length 301 #molecular-weight 31261 #checksum 1980 SEQUENCE /// ENTRY F69752 #type complete TITLE 5-dehydro-4-deoxyglucarate dehydratase homolog ycbC - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS F69752 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69752 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-308 ##label KUN !'##cross-references GB:Z99105; GB:AL009126; NID:g2632457; !1PIDN:CAB12040.1; PID:g2632532 !'##experimental_source strain 168 GENETICS !$#gene ycbC CLASSIFICATION #superfamily dihydrodipicolinate synthase SUMMARY #length 308 #molecular-weight 34039 #checksum 8694 SEQUENCE /// ENTRY SYECDP #type complete TITLE dihydrodipicolinate synthase (EC 4.2.1.52) [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1990 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS E65023; A30381; S27165; A36146; Q00342 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65023 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-292 ##label BLAT !'##cross-references GB:AE000335; GB:U00096; NID:g1788821; !1PIDN:AAC75531.1; PID:g1788823; UWGP:b2478 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A30381 !$#authors Richaud, F.; Richaud, C.; Ratet, P.; Patte, J.C. !$#journal J. Bacteriol. (1986) 166:297-300 !$#title Chromosomal location and nucleotide sequence of the !1Escherichia coli dapA gene. !$#cross-references MUID:86168031; PMID:3514578 !$#accession A30381 !'##molecule_type DNA !'##residues 1-206,'T',208-223,'E',225-292 ##label RIC !'##cross-references EMBL:M12844; NID:g145707; PIDN:AAA23665.1; !1PID:g145708 REFERENCE S27165 !$#authors Laber, B.; Gomis-Rueth, F.X.; Romao, M.J.; Huber, R. !$#journal Biochem. J. (1992) 288:691-695 !$#title Escherichia coli dihydrodipicolinate synthase. !1Identification of the active site and crystallization. !$#cross-references MUID:93098829; PMID:1463470 !$#accession S27165 !'##molecule_type DNA !'##residues 1-206,'T',208-223,'E',225-292 ##label LAB REFERENCE A36146 !$#authors Tiedeman, A.A.; DeMarini, D.J.; Parker, J.; Smith, J.M. !$#journal J. Bacteriol. (1990) 172:6035-6041 !$#title DNA sequence of the purC gene encoding !15'-phosphoribosyl-5-aminoimidazole-4-N-succinocarboxamide !1synthetase and organization of the dapA-purC region of !1Escherichia coli K-12. !$#cross-references MUID:91008982; PMID:2120198 !$#accession A36146 !'##molecule_type DNA !'##residues 288-292 ##label TIE !'##cross-references GB:M33928 REFERENCE A65412 !$#authors Mirwaldt, C.; Korndoerfer, I.; Huber, R. !$#submission submitted to the Brookhaven Protein Data Bank, February 1995 !$#cross-references PDB:1DHP !$#contents annotation; X-ray crystallography, 2.5 angstroms, residues !11-292 REFERENCE A59217 !$#authors Mirwaldt, C.; Korndoerfer, I.; Huber, R. !$#journal J. Mol. Biol. (1995) 246:227-239 !$#title The crystal structure of dihydrodipicolinate synthase from !1Escherichia coli at 2.5 A resolution. !$#cross-references MUID:95156485; PMID:7853400 !$#contents annotation; X-ray crystallography, 2.5 angstroms GENETICS !$#gene dapA !$#map_position 53 min FUNCTION !$#description catalyzes the formation of dihydrodipicolinate from !1L-aspartate 4-semialdehyde and pyruvate !$#pathway first step in diaminopimelate and lysine biosynthesis !$#note the reaction is sensitive to lysine inhibition CLASSIFICATION #superfamily dihydrodipicolinate synthase KEYWORDS carbon-oxygen lyase; diaminopimelate biosynthesis; !1hydro-lyase; lysine biosynthesis FEATURE !$161 #active_site Lys (covalent pyruvate-binding) #status !8experimental SUMMARY #length 292 #molecular-weight 31270 #checksum 8540 SEQUENCE /// ENTRY WZWTH7 #type complete TITLE dihydrodipicolinate synthase (EC 4.2.1.52) precursor (clone pDA17) [similarity] - wheat ORGANISM #formal_name Triticum aestivum #common_name common wheat DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 17-Mar-2000 ACCESSIONS A39213 REFERENCE A39213 !$#authors Kaneko, T.; Hashimoto, T.; Kumpaisal, R.; Yamada, Y. !$#journal J. Biol. Chem. (1990) 265:17451-17455 !$#title Molecular cloning of wheat dihydrodipicolinate synthase. !$#cross-references MUID:91009193; PMID:2211639 !$#accession A39213 !'##molecule_type mRNA !'##residues 1-388 ##label KAN !'##cross-references GB:M60598; GB:J05649; NID:g170679; PIDN:AAA34263.1; !1PID:g170680 !'##note the authors translated the codon TCT for residue 237 as Cys FUNCTION !$#description catalyzes the formation of dihydrodipicolinate from !1L-aspartate 4-semialdehyde and pyruvate !$#pathway first step in diaminopimelate and lysine biosynthesis !$#note the reaction is sensitive to lysine inhibition CLASSIFICATION #superfamily dihydrodipicolinate synthase KEYWORDS carbon-oxygen lyase; chloroplast; diaminopimelate !1biosynthesis; hydro-lyase; lysine biosynthesis; tetramer FEATURE !$1-62 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$63-388 #product dihydrodipicolinate synthase #status !8predicted #label MAT\ !$245 #active_site Lys (covalent pyruvate-binding) #status !8predicted SUMMARY #length 388 #molecular-weight 42413 #checksum 5186 SEQUENCE /// ENTRY WZWTH6 #type complete TITLE dihydrodipicolinate synthase (EC 4.2.1.52) precursor (clone pDA26) [validated] - wheat ORGANISM #formal_name Triticum aestivum #common_name common wheat DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 17-Mar-2000 ACCESSIONS B39213 REFERENCE A39213 !$#authors Kaneko, T.; Hashimoto, T.; Kumpaisal, R.; Yamada, Y. !$#journal J. Biol. Chem. (1990) 265:17451-17455 !$#title Molecular cloning of wheat dihydrodipicolinate synthase. !$#cross-references MUID:91009193; PMID:2211639 !$#accession B39213 !'##molecule_type mRNA !'##residues 1-377 ##label KAN !'##cross-references GB:M60599; GB:J05649; NID:g170681; PIDN:AAA34264.1; !1PID:g170682 !'##note the authors translated the codon ACT for residue 226 as Ser COMMENT This enzyme catalyzes the formation of dihydrodipicolinate !1from L-aspartate 4-semialdehyde and pyruvate. The reaction !1is the first step in diaminopimelate and lysine !1biosynthesis; it is sensitive to lysine inhibition. CLASSIFICATION #superfamily dihydrodipicolinate synthase KEYWORDS carbon-oxygen lyase; chloroplast; diaminopimelate !1biosynthesis; hydro-lyase; lysine biosynthesis; tetramer FEATURE !$1-51 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$52-377 #product dihydrodipicolinate synthase #status !8experimental #label MAT\ !$234 #active_site Lys (covalent pyruvate-binding) #status !8predicted SUMMARY #length 377 #molecular-weight 40875 #checksum 5761 SEQUENCE /// ENTRY WZZMP #type complete TITLE dihydrodipicolinate synthase (EC 4.2.1.52) precursor [validated] - maize ORGANISM #formal_name Zea mays #common_name maize DATE 30-Jun-1992 #sequence_revision 17-Mar-2000 #text_change 17-Mar-2000 ACCESSIONS S16560; S20241; A59219; S18298 REFERENCE S16560 !$#authors Frisch, D.A.; Tommey, A.M.; Gengenbach, B.G.; Somers, D.A. !$#journal Mol. Gen. Genet. (1991) 228:287-293 !$#title Direct genetic selection of a maize cDNA for !1dihydrodipicolinate synthase in an Escherichia coli dapA(-) !1auxotroph. !$#cross-references MUID:91360078; PMID:1886613 !$#accession S16560 !'##molecule_type mRNA !'##residues 1-366,'Q',368-380 ##label FRI1 !'##cross-references EMBL:X52850; NID:g1638870 !$#accession S20241 !'##molecule_type protein !'##residues 55-62 ##label FRI2 !$#accession A59219 !'##molecule_type mRNA !'##residues 1-380 ##label FRI3 !'##cross-references EMBL:X52850; NID:g1638870; PIDN:CAA37038.1; !1PID:g1638871 !'##note the sequence is revised in GenBank entry ZMDHPS, release 114.0, !1PIDN:CAA37038.1 REFERENCE S18298 !$#authors Frisch, D.A. !$#submission submitted to the EMBL Data Library, May 1990 !$#accession S18298 !'##molecule_type mRNA !'##residues 1-366,'RF' ##label FRI4 !'##cross-references EMBL:X52850; NID:g1638870 FUNCTION !$#description catalyzes the formation of dihydrodipicolinate from !1L-aspartate 4-semialdehyde and pyruvate !$#pathway first step in diaminopimelate and lysine biosynthesis !$#note the reaction is sensitive to lysine inhibition CLASSIFICATION #superfamily dihydrodipicolinate synthase KEYWORDS carbon-oxygen lyase; chloroplast; diaminopimelate !1biosynthesis; hydro-lyase; lysine biosynthesis FEATURE !$1-54 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$55-380 #product dihydrodipicolinate synthase #status !8experimental #label MAT\ !$237 #active_site Lys (covalent pyruvate-binding) #status !8predicted SUMMARY #length 380 #molecular-weight 41185 #checksum 6061 SEQUENCE /// ENTRY WZECN #type complete TITLE N-acetylneuraminate lyase (EC 4.1.3.3) - Escherichia coli (strain K-12) ALTERNATE_NAMES N-acetylneuraminate aldolase ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 30-Sep-1990 #text_change 01-Mar-2002 ACCESSIONS JP0002; A24109; C65114 REFERENCE A90021 !$#authors Kawakami, B.; Kudo, T.; Narahashi, Y.; Horikoshi, K. !$#journal Agric. Biol. Chem. (1986) 50:2155-2158 !$#title Nucleotide sequence of the N-acetylneuraminate lyase gene of !1Escherichia coli. !$#accession JP0002 !'##molecule_type DNA !'##residues 1-297 ##label KAW !'##experimental_source K12, strain HB101 REFERENCE A93603 !$#authors Ohta, Y.; Watanabe, K.; Kimura, A. !$#journal Nucleic Acids Res. (1985) 13:8843-8852 !$#title Complete nucleotide sequence of the E. coli !1N-acetylneuraminate lyase. !$#cross-references MUID:86093682; PMID:3909108 !$#accession A24109 !'##molecule_type DNA !'##residues 1-69,'G',71-83,'T',85-297 ##label OHT !'##experimental_source K12, strain C600 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65114 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-297 ##label BLAT !'##cross-references GB:AE000402; GB:U00096; NID:g1789619; !1PIDN:AAC76257.1; PID:g1789620; UWGP:b3225 !'##experimental_source strain K-12, substrain MG1655 COMMENT This enzyme catalyzes the conversion of N-acetylneuraminic !1acid to pyruvate and N-acetylmannosamine. GENETICS !$#gene nanA; npl !$#map_position 69 min CLASSIFICATION #superfamily dihydrodipicolinate synthase KEYWORDS carbon-carbon lyase; oxo-acid-lyase FEATURE !$165 #active_site Lys (covalent pyruvate-binding) #status !8predicted SUMMARY #length 297 #molecular-weight 32593 #checksum 8294 SEQUENCE /// ENTRY S27618 #type complete TITLE 5-dehydro-4-deoxyglucarate dehydratase (EC 4.2.1.41) - Pseudomonas putida ALTERNATE_NAMES 5-keto-4-deoxyglucarate dehydratase ORGANISM #formal_name Pseudomonas putida DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S27618 REFERENCE S27612 !$#authors Burlingame, R.P.; Maruya, A.; Ally, A.; Ally, D.; Backman, !1K.C. !$#submission submitted to the EMBL Data Library, June 1992 !$#description Nucleotide sequences of hydroxyproline-specific !1alpha-ketoglutarate semialdehyde dehydrogenase genes from !1two strains of pseudomonas putida. !$#accession S27618 !'##status preliminary !'##molecule_type DNA !'##residues 1-303 ##label BUR !'##cross-references EMBL:M69160; NID:g151313; PIDN:AAA25869.1; !1PID:g151316 CLASSIFICATION #superfamily dihydrodipicolinate synthase KEYWORDS carbon-oxygen lyase; hydro-lyase SUMMARY #length 303 #molecular-weight 32808 #checksum 5117 SEQUENCE /// ENTRY B53308 #type complete TITLE mosA protein - Rhizobium meliloti (strain L5-30) ORGANISM #formal_name Rhizobium meliloti DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B53308 REFERENCE A53308 !$#authors Murphy, P.J.; Trenz, S.P.; Grzemski, W.; De Bruijn, F.J.; !1Schell, J. !$#journal J. Bacteriol. (1993) 175:5193-5204 !$#title The Rhizobium meliloti rhizopine mos locus is a mosaic !1structure facilitating its symbiotic regulation. !$#cross-references MUID:93352426; PMID:8349559 !$#accession B53308 !'##status preliminary !'##molecule_type DNA !'##residues 1-333 ##label MUR !'##cross-references GB:L17071; NID:g310301; PIDN:AAA26301.1; !1PID:g310303 GENETICS !$#gene mosA CLASSIFICATION #superfamily dihydrodipicolinate synthase SUMMARY #length 333 #molecular-weight 35787 #checksum 8868 SEQUENCE /// ENTRY S56523 #type complete TITLE dihydrodipicolinate synthase homolog yjhH - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS S56523; D65243 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56523 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-319 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97194.1; !1PID:g537139 !'##experimental_source strain K-12 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65243 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-319 ##label BLAT !'##cross-references GB:AE000500; GB:U00096; NID:g2367369; !1PIDN:AAC77254.1; PID:g1790751; UWGP:b4298 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yjhH CLASSIFICATION #superfamily dihydrodipicolinate synthase SUMMARY #length 319 #molecular-weight 34869 #checksum 6897 SEQUENCE /// ENTRY A45470 #type complete TITLE hydroxymethylglutaryl-CoA lyase (EC 4.1.3.4) - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 24-Sep-1999 ACCESSIONS A45470 REFERENCE A45470 !$#authors Mitchell, G.A.; Robert, M.F.; Hruz, P.W.; Wang, S.; !1Fontaine, G.; Behnke, C.E.; Mende-Mueller, L.M.; Schappert, !1K.; Lee, C.; Gibson, K.M.; Miziorko, H.M. !$#journal J. Biol. Chem. (1993) 268:4376-4381 !$#title 3-Hydroxy-3-methylglutaryl coenzyme A lyase (HL). Cloning of !1human and chicken liver HL cDNAs and characterization of a !1mutation causing human HL deficiency. !$#cross-references MUID:93179448; PMID:8440722 !$#accession A45470 !'##status preliminary !'##molecule_type mRNA !'##residues 1-325 ##label MIT !'##cross-references GB:L07033; NID:g184502; PIDN:AAA92733.1; !1PID:g184503 !'##experimental_source liver !'##note sequence extracted from NCBI backbone (NCBIN:125920, !1NCBIP:125925) GENETICS !$#gene GDB:HMGCL; HL !'##cross-references GDB:138445; OMIM:246450 !$#map_position 1p36.1-1p35 CLASSIFICATION #superfamily hydroxymethylglutaryl-CoA lyase KEYWORDS carbon-carbon lyase; mitochondrion; oxo-acid-lyase SUMMARY #length 325 #molecular-weight 34390 #checksum 4439 SEQUENCE /// ENTRY D69893 #type complete TITLE hydroxymethylglutaryl-CoA lyase homolog yngG - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS D69893 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D69893 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-299 ##label KUN !'##cross-references GB:Z99113; GB:AL009126; NID:g2634090; !1PIDN:CAB13706.1; PID:g2634206 !'##experimental_source strain 168 GENETICS !$#gene yngG CLASSIFICATION #superfamily hydroxymethylglutaryl-CoA lyase SUMMARY #length 299 #molecular-weight 32644 #checksum 4484 SEQUENCE /// ENTRY S67674 #type complete TITLE homocitrate synthase homolog YDL131w - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein D2195 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S67674; S67677 REFERENCE S67655 !$#authors Rieger, M.; Mueller-Auer, S.; Brueckner, M.; Schaefer, M.; !1Wagner, G. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67674 !'##molecule_type DNA !'##residues 1-440 ##label RIE !'##cross-references EMBL:Z74179; NID:g1431198; PIDN:CAA98700.1; !1PID:g1431199; GSPDB:GN00004; MIPS:YDL131w !'##experimental_source strain S288C REFERENCE S67677 !$#authors Saluz, H.P.; Woelfl, S.; Hanemann, V. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67677 !'##molecule_type DNA !'##residues 1-440 ##label SAL !'##cross-references EMBL:Z74179; NID:g1431198; PIDN:CAA98700.1; !1PID:g1431199; GSPDB:GN00004; MIPS:YDL131w !'##experimental_source strain S288C GENETICS !$#gene SGD:LYS21; MIPS:YDL131w !'##cross-references SGD:S0002289 !$#map_position 4L CLASSIFICATION #superfamily hydroxymethylglutaryl-CoA lyase SUMMARY #length 440 #molecular-weight 48594 #checksum 8837 SEQUENCE /// ENTRY YKPG #type complete TITLE citrate (si)-synthase (EC 4.1.3.7) precursor - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 15-Oct-1982 #sequence_revision 30-Sep-1992 #text_change 05-May-2000 ACCESSIONS A29966; A01109; A61347 REFERENCE A29966 !$#authors Evans, C.T.; Owens, D.D.; Sumegi, B.; Kispal, G.; Srere, !1P.A. !$#journal Biochemistry (1988) 27:4680-4686 !$#title Isolation, nucleotide sequence, and expression of a cDNA !1encoding pig citrate synthase. !$#cross-references MUID:89000665; PMID:3048387 !$#accession A29966 !'##molecule_type mRNA !'##residues 1-464 ##label EVA !'##cross-references EMBL:M21197; NID:g164418; PIDN:AAA31017.1; !1PID:g164419 REFERENCE A90457 !$#authors Bloxham, D.P.; Parmelee, D.C.; Kumar, S.; Walsh, K.A.; !1Titani, K. !$#journal Biochemistry (1982) 21:2028-2036 !$#title Complete amino acid sequence of porcine heart citrate !1synthase. !$#cross-references MUID:82231993; PMID:7093227 !$#accession A01109 !'##molecule_type protein !'##residues 28-464 ##label BLO REFERENCE A61347 !$#authors Bloxham, D.P.; Parmelee, D.C.; Kumar, S.; Wade, R.D.; !1Ericsson, L.H.; Neurath, H.; Walsh, K.A.; Titani, K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:5381-5385 !$#title Primary structure of porcine heart citrate synthase. !$#cross-references MUID:82060250; PMID:6795632 !$#accession A61347 !'##molecule_type protein !'##residues 28-464 ##label BL2 REFERENCE A92884 !$#authors Remington, S.; Wiegand, G.; Huber, R. !$#journal J. Mol. Biol. (1982) 158:111-152 !$#title Crystallographic refinement and atomic models of two !1different forms of citrate synthase at 2.7 and 1.7 angstroms !1resolution. !$#cross-references MUID:83010291; PMID:7120407 !$#contents annotation; X-ray crystallography, 2.7 and 1.7 angstroms COMMENT Citrate (si)-synthase is found in nearly all cells capable !1of oxidative metabolism. It catalyzes the condensation of !1oxaloacetate and acetyl-CoA to form citrate in the !1tricarboxylic acid cycle. COMMENT It is synthesized in the cytoplasm but functions in the !1mitochondrion of eukaryote cells. COMMENT This molecule is a dimer of identical chains. Each dimer !1binds two molecules of acetyl-CoA and two molecules of !1oxaloacetate at two active sites. CLASSIFICATION #superfamily citrate (si)-synthase KEYWORDS carbon-carbon lyase; coenzyme A; homodimer; methylated amino !1acid; mitochondrion; oxo-acid-lyase; tricarboxylic acid !1cycle FEATURE !$1-27 #domain transit peptide (mitochondrion) #status !8predicted #label SIG\ !$28-464 #product citrate (si)-synthase #status experimental !8#label MAT\ !$301,347,402 #active_site His, His, Asp #status predicted\ !$395 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental SUMMARY #length 464 #molecular-weight 51629 #checksum 3548 SEQUENCE /// ENTRY YKBY #type complete TITLE citrate (si)-synthase (EC 4.1.3.7) precursor, mitochondrial - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein N2019; protein YNR001c ORGANISM #formal_name Saccharomyces cerevisiae DATE 25-Feb-1985 #sequence_revision 10-Feb-1995 #text_change 23-Mar-2001 ACCESSIONS S35390; S45124; S48338; A01110; S63327 REFERENCE S35390 !$#authors Lindner, P. !$#submission submitted to the EMBL Data Library, July 1993 !$#accession S35390 !'##molecule_type DNA !'##residues 1-479 ##label LIN !'##cross-references EMBL:Z23259; NID:g313749; PIDN:CAA80781.1; !1PID:g313750 REFERENCE S45119 !$#authors Verhasselt, P.; Aert, R.; Voet, M.; Volckaert, G. !$#submission submitted to the EMBL Data Library, January 1994 !$#description Twelve open reading frames revealed on the 23.6 kbp segment !1flanking the centromere on the Saccharomyces cerevisiae !1chromosome XIV right arm. !$#accession S45124 !'##molecule_type DNA !'##residues 1-479 ##label VER !'##cross-references EMBL:X77395; NID:g496717; PIDN:CAA54569.1; !1PID:g496718 REFERENCE S48338 !$#authors Verhasselt, P.; Aert, R.; Voet, M.; Volckaert, G. !$#journal Yeast (1994) 10:1355-1361 !$#title Twelve open reading frames revealed in the 23.6 kb segment !1flanking the centromere on the Saccharomyces cerevisiae !1chromosome XIV right arm. !$#cross-references MUID:95208356; PMID:7900425 !$#accession S48338 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-479 ##label VE2 !'##cross-references EMBL:X77395; NID:g496717; PIDN:CAA54569.1; !1PID:g496718 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1994 REFERENCE A01110 !$#authors Suissa, M.; Suda, K.; Schatz, G. !$#journal EMBO J. (1984) 3:1773-1781 !$#title Isolation of the nuclear yeast genes for citrate synthase !1and fifteen other mitochondrial proteins by a new screening !1method. !$#cross-references MUID:85003587; PMID:6090126 !$#accession A01110 !'##molecule_type DNA !'##residues 1-57,'Q',59-77,'E',78-479 ##label SUI !'##cross-references GB:X00782; NID:g3602; PIDN:CAA25359.1; PID:g3603 !'##experimental_source strain D273-10B REFERENCE S62910 !$#authors Aert, R.; Verhasselt, P.; Voet, M.; Volckaert, G. !$#submission submitted to the Protein Sequence Database, April 1996 !$#accession S63327 !'##molecule_type DNA !'##residues 1-479 ##label AER !'##cross-references EMBL:Z71616; NID:g1302468; PIDN:CAA96277.1; !1PID:g1302469; GSPDB:GN00014; MIPS:YNR001c !'##experimental_source strain S288C GENETICS !$#gene SGD:CIT1; MIPS:YNR001c !'##cross-references SGD:S0005284; MIPS:YNR001c !$#map_position 14R !$#genome nuclear COMPLEX homodimer FUNCTION !$#description carbon-carbon lyase; catalyzes condensation of oxaloacetate !1and acetyl-CoA to form citrate; oxo-acid-lyase !$#pathway tricarboxylic acid cycle CLASSIFICATION #superfamily citrate (si)-synthase KEYWORDS acetyl-CoA; carbon-carbon lyase; coenzyme A; homodimer; !1mitochondrion; oxo-acid-lyase; tricarboxylic acid cycle FEATURE !$1-39 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$40-479 #product citrate (si)-synthase #status predicted !8#label MAT\ !$312,358,413 #active_site His, His, Asp #status predicted SUMMARY #length 479 #molecular-weight 53360 #checksum 4782 SEQUENCE /// ENTRY YKBYC #type complete TITLE citrate (si)-synthase (EC 4.1.3.7), peroxisomal - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YCR005c; protein YCR043 ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 21-Jul-2000 ACCESSIONS A25393; S26734; S19474; S12944; A39664 REFERENCE A25393 !$#authors Rosenkrantz, M.; Alam, T.; Kim, K.S.; Clark, B.J.; Srere, !1P.A.; Guarente, L.P. !$#journal Mol. Cell. Biol. (1986) 6:4509-4515 !$#title Mitochondrial and nonmitochondrial citrate synthases in !1Saccharomyces cerevisiae are encoded by distinct homologous !1genes. !$#cross-references MUID:87089811; PMID:3540614 !$#accession A25393 !'##molecule_type DNA !'##residues 1-460 ##label ROS !'##cross-references EMBL:Z11113; NID:g3297; PIDN:CAA77442.1; PID:g3299; !1GB:M14686; NID:g171226; PID:g171227 REFERENCE S22265 !$#authors Biteau, N.; Fremaux, C.; Hebrard, S.; Menara, A.; Aigle, M.; !1Crouzet, M. !$#journal Yeast (1992) 8:61-70 !$#title The complete sequence of a 10.8kb fragment to the right of !1the chromosome III centromere of Saccharomyces cerevisiae. !$#cross-references MUID:92254505; PMID:1580102 !$#accession S26734 !'##status translation not shown !'##molecule_type DNA !'##residues 1-460 ##label BIT !'##cross-references EMBL:X59720; NID:g1907116; PIDN:CAA42342.1; !1PID:g1907148 REFERENCE S19452 !$#authors Aigle, M.; Biteau, N.; Crouzet, M. !$#submission submitted to the Protein Sequence Database, March 1992 !$#accession S19474 !'##molecule_type DNA !'##residues 1-460 ##label AIG !'##cross-references EMBL:X59720; NID:g1907116; PIDN:CAA42342.1; !1PID:g1907148; GSPDB:GN00003; MIPS:YCR005c REFERENCE A39664 !$#authors Liao, X.; Small, W.C.; Srere, P.A.; Butow, R.A. !$#journal Mol. Cell. Biol. (1991) 11:38-46 !$#title Intramitochondrial functions regulate nonmitochondrial !1citrate synthase (CIT2) expression in Saccharomyces !1cerevisiae. !$#cross-references MUID:91094853; PMID:1986232 !$#accession S12944 !'##molecule_type DNA !'##residues 1-24 ##label LIA !'##cross-references EMBL:M54982; NID:g171228; PIDN:AAA34498.1; !1PID:g171229 GENETICS !$#gene SGD:CIT2; MIPS:YCR005c !'##cross-references SGD:S0000598; MIPS:YCR005c !$#map_position 3R CLASSIFICATION #superfamily citrate (si)-synthase KEYWORDS acetyl-CoA; carbon-carbon lyase; coenzyme A; homodimer; !1oxo-acid-lyase; peroxisome; tricarboxylic acid cycle FEATURE !$458-460 #region peroxisome/glyoxysome location signal !8(S-[RKH]-L) motif\ !$293,339,394 #active_site His, His, Asp #status predicted SUMMARY #length 460 #molecular-weight 51413 #checksum 1279 SEQUENCE /// ENTRY YKMUM #type complete TITLE citrate (si)-synthase (EC 4.1.3.7) precursor, mitochondrial - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jun-2000 ACCESSIONS JA0149; S07004 REFERENCE JA0149 !$#authors Unger, E.A.; Hand, J.M.; Cashmore, A.R.; Vasconcelos, A.C. !$#journal Plant Mol. Biol. (1989) 13:411-418 !$#title Isolation of a cDNA encoding mitochondrial citrate synthase !1from Arabidopsis thaliana. !$#cross-references MUID:91370823; PMID:2491664 !$#accession JA0149 !'##molecule_type mRNA !'##residues 1-472 ##label UNG !'##cross-references EMBL:X17528; NID:g11243; PIDN:CAA35570.1; !1PID:g2652924 !'##note the sequence from Fig. 2 is inconsistent with that from Fig. 1 !1in having 47-Gly, 125-Trp, 141-Leu, 151-Ser, 185-Asn, !1187-Asn, 191-Asn, 348-Leu, an additional Gly after 89-Trp, !1an additional Val after 393-Cys and two additional Arg after !1228-Arg, in lacking 114-Leu and residues 233 to 241 GENETICS !$#genome nuclear COMPLEX homodimer CLASSIFICATION #superfamily citrate (si)-synthase KEYWORDS carbon-carbon lyase; coenzyme A; homodimer; mitochondrion; !1oxo-acid-lyase; tricarboxylic acid cycle FEATURE !$343-375 #region acetyl-CoA binding #status predicted\ !$309,355,407 #active_site His, His, Asp #status predicted SUMMARY #length 472 #molecular-weight 52941 #checksum 9626 SEQUENCE /// ENTRY YKEC #type complete TITLE citrate (si)-synthase (EC 4.1.3.7) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 18-Apr-1984 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS G64807; A01111; A91310; A90486; A39494; I41237; I41236; !1I41238 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64807 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-427 ##label BLAT !'##cross-references GB:AE000175; GB:U00096; NID:g1786934; !1PIDN:AAC73814.1; PID:g1786939; UWGP:b0720 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A90477 !$#authors Ner, S.S.; Bhayana, V.; Bell, A.W.; Giles, I.G.; Duckworth, !1H.W.; Bloxham, D.P. !$#journal Biochemistry (1983) 22:5243-5249 !$#title Complete sequence of the gltA gene encoding citrate synthase !1in Escherichia coli. !$#accession A01111 !'##molecule_type DNA !'##residues 1-170,'I',172-288,'F',290-413,'I',415-427 ##label NER !'##cross-references GB:J01619 REFERENCE A91310 !$#authors Hull, E.P.; Spencer, M.E.; Wood, D.; Guest, J.R. !$#journal FEBS Lett. (1983) 156:366-370 !$#title Nucleotide sequence of the promoter region of the citrate !1synthase gene (gltA) of Escherichia coli. !$#cross-references MUID:83210236; PMID:6343122 !$#accession A91310 !'##molecule_type DNA !'##residues 1-91,'MVKPT' ##label HUL !'##cross-references GB:K00542; GB:M11121 REFERENCE A90486 !$#authors Bhayana, V.; Duckworth, H.W. !$#journal Biochemistry (1984) 23:2900-2905 !$#title Amino acid sequence of Escherichia coli citrate synthase. !$#cross-references MUID:84280857; PMID:6380576 !$#accession A90486 !'##molecule_type protein !'##residues 1-10,'D',12-101;110-217;220-288,'F',290-427 ##label BHA REFERENCE A39494 !$#authors Donald, L.J.; Crane, B.R.; Anderson, D.H.; Duckworth, H.W. !$#journal J. Biol. Chem. (1991) 266:20709-20713 !$#title The role of cysteine 206 in allosteric inhibition of !1Escherichia coli citrate synthase. Studies by chemical !1modification, site-directed mutagenesis, and (19)F NMR. !$#cross-references MUID:92041923; PMID:1939121 !$#accession A39494 !'##status preliminary !'##molecule_type protein !'##residues 203-206,'X',208-212 ##label DON REFERENCE I41237 !$#authors Ner, S.S.; Bloxham, D.P.; Handford, P.A.; Akhtar, M. !$#journal Int. J. Biochem. (1986) 18:257-262 !$#title The synthesis and use of oligodeoxynucleotides in plasmid !1DNA sequencing. !$#cross-references MUID:86165297; PMID:3514304 !$#accession I41237 !'##status preliminary !'##molecule_type DNA !'##residues 360-388 ##label RES !'##cross-references GB:M29373; NID:g146205; PIDN:AAA23902.1; !1PID:g551807 REFERENCE I41112 !$#authors Wilde, R.J.; Guest, J.R. !$#journal J. Gen. Microbiol. (1986) 132:3239-3251 !$#title Transcript analysis of the citrate synthase and succinate !1dehydrogenase genes of Escherichia coli k-12. !$#cross-references MUID:88009821; PMID:3309132 !$#accession I41236 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-33 ##label RE2 !'##cross-references GB:M28987; NID:g342040; PIDN:AAA23901.1; !1PID:g495024 !$#accession I41238 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 393-399,'T',401-427 ##label RE3 !'##cross-references GB:M28988; NID:g342041; PIDN:AAA23903.1; !1PID:g495780 GENETICS !$#gene gltA; gluT; icdB !$#map_position 17 min COMPLEX homohexamer FUNCTION !$#description catalyzes condensation of oxaloacetate and acetyl-CoA to !1form citrate !$#pathway tricarboxylic acid cycle !$#note the E. coli enzyme is sensitive to NADH inhibition CLASSIFICATION #superfamily citrate (si)-synthase KEYWORDS allosteric regulation; carbon-carbon lyase; coenzyme A; !1homohexamer; oxo-acid-lyase; tricarboxylic acid cycle FEATURE !$306 #active_site His #status predicted SUMMARY #length 427 #molecular-weight 48015 #checksum 6879 SEQUENCE /// ENTRY YKRECP #type complete TITLE citrate (si)-synthase (EC 4.1.3.7) - Rickettsia prowazekii ALTERNATE_NAMES citrate synthase gltA; RP844 ORGANISM #formal_name Rickettsia prowazekii DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 03-Nov-2000 ACCESSIONS A26971; PC4091; D71646 REFERENCE A26971 !$#authors Wood, D.O.; Williamson, L.R.; Winkler, H.H.; Krause, D.C. !$#journal J. Bacteriol. (1987) 169:3564-3572 !$#title Nucleotide sequence of the Rickettsia prowazekii citrate !1synthase gene. !$#cross-references MUID:87279904; PMID:3112124 !$#accession A26971 !'##molecule_type DNA !'##residues 1-436 ##label WOO !'##cross-references GB:M17149; NID:g152471; PIDN:AAA26383.1; !1PID:g152472 REFERENCE PC4091 !$#authors Cai, J.; Pang, H.; Wood, D.O.; Winkler, H.H. !$#journal Gene (1995) 163:115-119 !$#title The citrate synthase-encoding gene of Rickettsia prowazekii !1is controlled by two promoters. !$#cross-references MUID:96001254; PMID:7557459 !$#accession PC4091 !'##molecule_type mRNA !'##residues 1-35 ##label CAI !'##cross-references GB:U14334; NID:g540094; PIDN:AAA85524.1; !1PID:g540095 REFERENCE A71630 !$#authors Andersson, S.G.E.; Zomorodipour, A.; Andersson, J.O.; !1Sicheritz-Ponten, T.; Alsmark, U.C.M.; Podowski, R.M.; !1Naeslund, A.K.; Eriksson, A.S.; Winkler, H.H.; Kurland, C.G. !$#journal Nature (1998) 396:133-140 !$#title The genome sequence of Rickettsia prowazekii and the origin !1of mitochondria. !$#cross-references MUID:99039499; PMID:9823893 !$#accession D71646 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-436 ##label AND !'##cross-references GB:AJ235273; GB:AJ235269; NID:g3861237; !1PIDN:CAA15268.1; PID:g3861369; GSPDB:GN00081 !'##experimental_source strain Madrid E GENETICS !$#gene gltA; RP844 COMPLEX homohexamer FUNCTION !$#description carbon-carbon lyase; oxo-acid-lyase; catalyzes synthesis of !1citrate from acetyl-CoA and oxaloacetic acid !$#pathway tricarboxylic acid cycle !$#note activity is inhibited by ATP, but not by NADH and !1alpha-ketoglutarate CLASSIFICATION #superfamily citrate (si)-synthase KEYWORDS allosteric regulation; carbon-carbon lyase; coenzyme A; !1homohexamer; oxo-acid-lyase; tricarboxylic acid cycle FEATURE !$311 #active_site His #status predicted SUMMARY #length 436 #molecular-weight 49323 #checksum 1907 SEQUENCE /// ENTRY YKQPC #type complete TITLE citrate (si)-synthase (EC 4.1.3.7) - Acetobacter aceti ORGANISM #formal_name Acetobacter aceti DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 05-May-2000 ACCESSIONS A35157 REFERENCE A35157 !$#authors Fukaya, M.; Takemura, H.; Okumura, H.; Kawamura, Y.; !1Horinouchi, S.; Beppu, T. !$#journal J. Bacteriol. (1990) 172:2096-2104 !$#title Cloning of genes responsible for acetic acid resistance in !1Acetobacter aceti. !$#cross-references MUID:90202732; PMID:2156811 !$#accession A35157 !'##molecule_type DNA !'##residues 1-436 ##label FUK !'##cross-references GB:M34830; NID:g141729; PIDN:AAA21883.1; !1PID:g141730 COMPLEX homohexamer FUNCTION !$#description carbon-carbon lyase; oxo-acid-lyase; catalyzes synthesis of !1citrate from acetyl-CoA and oxaloacetic acid !$#pathway tricarboxylic acid cycle CLASSIFICATION #superfamily citrate (si)-synthase KEYWORDS allosteric regulation; carbon-carbon lyase; coenzyme A; !1homohexamer; oxo-acid-lyase; tricarboxylic acid cycle FEATURE !$313 #active_site His #status predicted SUMMARY #length 436 #molecular-weight 48196 #checksum 9071 SEQUENCE /// ENTRY YKPSCA #type complete TITLE citrate (si)-synthase (EC 4.1.3.7) - Pseudomonas aeruginosa ORGANISM #formal_name Pseudomonas aeruginosa DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 05-May-2000 ACCESSIONS A33596 REFERENCE A33596 !$#authors Donald, L.J.; Molgat, G.F.; Duckworth, H.W. !$#journal J. Bacteriol. (1989) 171:5542-5550 !$#title Cloning, sequencing, and expression of the gene for !1NADH-sensitive citrate synthase of Pseudomonas aeruginosa. !$#cross-references MUID:90008792; PMID:2507528 !$#accession A33596 !'##molecule_type DNA !'##residues 1-428 ##label DON !'##cross-references GB:M29728 COMPLEX homohexamer FUNCTION !$#description carbon-carbon lyase; oxo-acid-lyase; catalyzes synthesis of !1citrate from acetyl-CoA and oxaloacetic acid !$#pathway tricarboxylic acid cycle !$#note the citrate synthase of gram-negative bacteria is an !1allosteric enzyme whose activity is inhibited strongly and !1specifically by NADH CLASSIFICATION #superfamily citrate (si)-synthase KEYWORDS allosteric regulation; carbon-carbon lyase; coenzyme A; !1homohexamer; oxo-acid-lyase; tricarboxylic acid cycle FEATURE !$306 #active_site His #status predicted SUMMARY #length 428 #molecular-weight 47681 #checksum 7548 SEQUENCE /// ENTRY YKYT #type complete TITLE citrate (si)-synthase (EC 4.1.3.7) - Thermoplasma acidophilum ORGANISM #formal_name Thermoplasma acidophilum DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 05-May-2000 ACCESSIONS S13831; A29714 REFERENCE S13831 !$#authors Sutherland, K.J.; Henneke, C.M.; Towner, P.; Hough, D.W.; !1Danson, M.J. !$#journal Eur. J. Biochem. (1990) 194:839-844 !$#title Citrate synthase from the thermophilic archaebacterium !1Thermoplasma acidophilum. Cloning and sequencing of the !1gene. !$#cross-references MUID:91099366; PMID:2269303 !$#accession S13831 !'##molecule_type DNA !'##residues 1-385 ##label SUT !'##cross-references GB:X55282; NID:g48073; PIDN:CAA38996.1; PID:g48074 REFERENCE A29714 !$#authors Smith, L.D.; Stevenson, K.J.; Hough, D.W.; Danson, M.J. !$#journal FEBS Lett. (1987) 225:277-281 !$#title Citrate synthase from the thermophilic archaebacteria !1Thermoplasma acidophilum and Sulfolobus acidocaldarius. !$#accession A29714 !'##status preliminary !'##molecule_type protein !'##residues 2-17 ##label SMI CLASSIFICATION #superfamily citrate (si)-synthase KEYWORDS allosteric regulation; carbon-carbon lyase; coenzyme A; !1homohexamer; oxo-acid-lyase SUMMARY #length 385 #molecular-weight 43072 #checksum 209 SEQUENCE /// ENTRY YKMY #type complete TITLE citrate (si)-synthase (EC 4.1.3.7) - Mycobacterium smegmatis ORGANISM #formal_name Mycobacterium smegmatis DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 05-May-2000 ACCESSIONS S17168 REFERENCE S17168 !$#authors David, M.; Lubinsky-Mink, S.; Ben-Zvi, A.; Suissa, M.; !1Ulitzur, S.; Kuhn, J. !$#journal Biochem. J. (1991) 278:225-234 !$#title Citrate synthase from Mycobacterium smegmatis. Cloning, !1sequence determination and expression in Escherichia coli. !$#cross-references MUID:91354207; PMID:1883331 !$#accession S17168 !'##molecule_type DNA !'##residues 1-375 ##label DAV !'##cross-references EMBL:X60513; NID:g44513; PIDN:CAA43028.1; !1PID:g44514 GENETICS !$#gene gltA CLASSIFICATION #superfamily citrate (si)-synthase KEYWORDS acetyl-CoA; carbon-carbon lyase; coenzyme A; oxo-acid-lyase; !1tricarboxylic acid cycle FEATURE !$227,266,317 #active_site His, His, Asp #status predicted SUMMARY #length 375 #molecular-weight 41501 #checksum 2051 SEQUENCE /// ENTRY DEECPC #type complete TITLE pyruvate dehydrogenase (cytochrome) (EC 1.2.2.2) - Escherichia coli (strain K-12) ALTERNATE_NAMES pyruvate oxidase ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 01-Mar-2002 ACCESSIONS A23648; G64825; I55291; I57856 REFERENCE A23648 !$#authors Grabau, C.; Cronan Jr., J.E. !$#journal Nucleic Acids Res. (1986) 14:5449-5460 !$#title Nucleotide sequence and deduced amino acid sequence of !1Escherichia coli pyruvate oxidase, a lipid-activated !1flavoprotein. !$#cross-references MUID:86286555; PMID:3016647 !$#accession A23648 !'##molecule_type DNA !'##residues 1-572 ##label GRA !'##cross-references GB:X04105; GB:M13947; GB:M13948; NID:g42472; !1PIDN:CAA27725.1; PID:g42473 !'##experimental_source strain K-12 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64825 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-572 ##label BLAT !'##cross-references GB:AE000188; GB:U00096; NID:g1787084; !1PIDN:AAC73958.1; PID:g1787096; UWGP:b0871 !'##experimental_source strain K-12, substrain MG1655 REFERENCE I55291 !$#authors Grabau, C.; Chang, Y.Y.; Cronan, J.E. !$#journal J. Biol. Chem. (1989) 264:12510-12519 !$#title Lipid binding by Escherichia coli pyruvate oxidase is !1disrupted by small alterations of the carboxyl-terminal !1region. !$#cross-references MUID:89308683; PMID:2663858 !$#accession I55291 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-363,'HE',366-413,'HGV',417-572 ##label RES !'##cross-references GB:M28208; NID:g1009024; PIDN:AAB59101.1; !1PID:g1009025 !'##experimental_source strain K-12 REFERENCE I57856 !$#authors Chang, Y.Y.; Wang, A.Y.; Cronan, J.E. !$#journal Mol. Microbiol. (1994) 11:1019-1028 !$#title Expression of Escherichia coli pyruvate oxidase (PoxB) !1depends on the sigma factor encoded by the rpoS(katF) gene. !$#cross-references MUID:94293772; PMID:8022274 !$#accession I57856 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-22 ##label RE2 !'##cross-references GB:S73268; NID:g685127; PIDN:AAB31180.1; !1PID:g685128 COMMENT The sequence of this protein was shown to be homologous with !1those of the large (or I) chains of acetolactate synthase !1isozymes, which catalyze an entirely different class of !1reaction although pyruvate is the end product. COMMENT This protein is not to be confused with a similar enzyme, !1pyruvate (or pyruvic) oxidase (EC 1.2.3.3), which in the !1presence of molecular oxygen and water catalyzes a !1phosphorylating oxidation of pyruvate to acetyl phosphate, !1carbon dioxide, and hydrogen peroxide. GENETICS !$#gene poxB !$#map_position 19 min COMPLEX homotetramer FUNCTION !$#description catalyzes the conversion of pyruvate to acetate and carbon !1dioxide in the presence of cytochrome b !$#note in the presence of pyruvate and cofactor thiamine !1pyrophosphate, the addition of a wide variety of lipids or !1detergents results in a 20- to 25-fold increase in activity CLASSIFICATION #superfamily acetolactate synthase large chain; thiamin !1pyrophosphate-binding domain homology KEYWORDS FAD; flavoprotein; homotetramer; lipid binding; magnesium; !1membrane protein; oxidoreductase; thiamin pyrophosphate FEATURE !$422-470 #domain thiamin pyrophosphate-binding domain homology !8#label TPB\ !$50 #active_site Glu #status predicted SUMMARY #length 572 #molecular-weight 62011 #checksum 5885 SEQUENCE /// ENTRY YCNT1 #type complete TITLE acetolactate synthase (EC 4.1.3.18) class I precursor - common tobacco ORGANISM #formal_name Nicotiana tabacum #common_name common tobacco DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 15-Oct-1999 ACCESSIONS S00545; S02852 REFERENCE S00545 !$#authors Lee, K.Y.; Townsend, J.; Tepperman, J.; Black, M.; Chui, !1C.F.; Mazur, B.; Dunsmuir, P.; Bedbrook, J. !$#journal EMBO J. (1988) 7:1241-1248 !$#title The molecular basis of sulfonylurea herbicide resistance in !1tobacco. !$#accession S00545 !'##molecule_type DNA !'##residues 1-667 ##label LEE !'##cross-references EMBL:X07644; NID:g19776; PIDN:CAA30484.1; !1PID:g19777 !'##experimental_source strain S4-Hra !'##note the authors translated the codon ATT for residue 247 as Val and !1GTA for residue 607 as Asn !'##note the second base of the codon for residue 179 is missing from !1Fig. 5; this has been corrected in reference S02852 REFERENCE S02823 !$#authors Lee, K.Y. !$#submission submitted to the EMBL Data Library, August 1988 !$#accession S02852 !'##molecule_type DNA !'##residues 179 ##label LED2 !'##cross-references EMBL:X07644; NID:g19776; PIDN:CAA30484.1; !1PID:g19777 GENETICS !$#gene SuRA !$#genome nuclear FUNCTION !$#pathway branched-chain amino acid biosynthesis !$#note first step CLASSIFICATION #superfamily acetolactate synthase large chain; thiamin !1pyrophosphate-binding domain homology KEYWORDS branched-chain amino acid biosynthesis; carbon-carbon lyase; !1chloroplast; flavoprotein; magnesium; oxo-acid-lyase; !1thiamin pyrophosphate FEATURE !$1-94 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$95-667 #product acetolactate synthase class I #status !8predicted #label MAT\ !$524-572 #domain thiamin pyrophosphate-binding domain homology !8#label TPB\ !$141 #active_site Glu #status predicted SUMMARY #length 667 #molecular-weight 72868 #checksum 6353 SEQUENCE /// ENTRY YCNT2 #type complete TITLE acetolactate synthase (EC 4.1.3.18) class II precursor - common tobacco ORGANISM #formal_name Nicotiana tabacum #common_name common tobacco DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 05-Nov-1999 ACCESSIONS S00546; A37583; S02852 REFERENCE S00545 !$#authors Lee, K.Y.; Townsend, J.; Tepperman, J.; Black, M.; Chui, !1C.F.; Mazur, B.; Dunsmuir, P.; Bedbrook, J. !$#journal EMBO J. (1988) 7:1241-1248 !$#title The molecular basis of sulfonylurea herbicide resistance in !1tobacco. !$#accession S00546 !'##molecule_type DNA !'##residues 1-664 ##label LEE !'##cross-references EMBL:X07645; NID:g19778; PIDN:CAA30485.1; !1PID:g19779 !'##note the authors translated the codon GTA for residue 604 as Asn !'##note the second base of the codon for residue 176 is missing from !1Fig. 5; this has been corrected in reference S02852 REFERENCE S02823 !$#authors Lee, K.Y. !$#submission submitted to the EMBL Data Library, August 1988 !$#accession A37583 !'##molecule_type DNA !'##residues 176 ##label LEE2 !'##cross-references EMBL:X07645 COMMENT Acetolactate synthase catalyzes the first step in the !1biosynthesis of branched-chain amino acids. GENETICS !$#gene SuRB CLASSIFICATION #superfamily acetolactate synthase large chain; thiamin !1pyrophosphate-binding domain homology KEYWORDS branched-chain amino acid biosynthesis; carbon-carbon lyase; !1chloroplast; flavoprotein; magnesium; oxo-acid-lyase; !1thiamin pyrophosphate FEATURE !$1-91 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$92-664 #product acetolactate synthase class II #status !8predicted #label MAT\ !$521-569 #domain thiamin pyrophosphate-binding domain homology !8#label TPB SUMMARY #length 664 #molecular-weight 72417 #checksum 1721 SEQUENCE /// ENTRY YCMU #type complete TITLE acetolactate synthase (EC 4.1.3.18) precursor - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 18-Feb-2000 ACCESSIONS S09502; T46200 REFERENCE S09502 !$#authors Sathasivan, K.; Haughn, G.W.; Murai, N. !$#journal Nucleic Acids Res. (1990) 18:2188 !$#title Nucleotide sequence of a mutant acetolactate synthase gene !1from an imidazolinone-resistant Arabidopsis thaliana var. !1Columbia. !$#cross-references MUID:90245681; PMID:2336405 !$#accession S09502 !'##molecule_type DNA !'##residues 1-670 ##label SAT !'##cross-references EMBL:X51514 !'##note the mutant GH90 sequence differs from that shown in having !1653-Asn REFERENCE Z23008 !$#authors Choisne, N.; Robert, C.; Brottier, P.; Wincker, P.; !1Cattolico, L.; Artiguenave, F.; Saurin, W.; Weissenbach, J.; !1Mewes, H.W.; Mayer, K.F.X.; Lemcke, K.; Schueller, C.; !1Quetier, F.; Salanoubat, M. !$#submission submitted to the Protein Sequence Database, December 1999 !$#accession T46200 !'##status preliminary !'##molecule_type DNA !'##residues 1-670 ##label CHO !'##cross-references EMBL:AL133315 !'##experimental_source cultivar Columbia; BAC clone T8P19 COMMENT Acetolactate synthase, a flavoprotein, catalyzes the !1formation of acetohydroxy acids from the corresponding !1alpha-keto acids (i.e., the first step common to the !1biosynthesis of all branched-chain amino acids) in the !1presence of thiamine pyrophosphate and magnesium ion. GENETICS !$#gene T8P19.70 !$#map_position 3 CLASSIFICATION #superfamily acetolactate synthase large chain; thiamin !1pyrophosphate-binding domain homology KEYWORDS branched-chain amino acid biosynthesis; carbon-carbon lyase; !1chloroplast; oxo-acid-lyase; valine resistance FEATURE !$1-97 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$98-670 #product acetolactate synthase #status predicted !8#label MAT\ !$527-575 #domain thiamin pyrophosphate-binding domain homology !8#label TPB SUMMARY #length 670 #molecular-weight 72584 #checksum 562 SEQUENCE /// ENTRY YCRP #type complete TITLE acetolactate synthase (EC 4.1.3.18) 2 precursor - rape ORGANISM #formal_name Brassica napus #common_name rape DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 15-Oct-1999 ACCESSIONS JQ0357; S17692; S07026 REFERENCE JQ0357 !$#authors Wiersma, P.A.; Schmiemann, M.G.; Condie, J.A.; Crosby, W.L.; !1Moloney, M.M. !$#journal Mol. Gen. Genet. (1989) 219:413-420 !$#title Isolation, expression and phylogenetic inheritance of an !1acetolactate synthase gene from Brassica napus. !$#cross-references MUID:90158503; PMID:2482934 !$#accession JQ0357 !'##molecule_type DNA !'##residues 1-637 ##label WIE !'##cross-references EMBL:X16708; NID:g17777; PIDN:CAA34680.1; !1PID:g17778 REFERENCE S17691 !$#authors Rutledge, R.G.; Quellet, T.; Hattori, J.; Miki, B.L. !$#journal Mol. Gen. Genet. (1991) 229:31-40 !$#title Molecular characterization and genetic origin of the !1Brassica napus acetohydroxyacid synthase multigene family. !$#cross-references MUID:91375448; PMID:1896019 !$#accession S17692 !'##molecule_type DNA !'##residues 1-637 ##label RUT !'##cross-references EMBL:Z11525; NID:g17773; PIDN:CAA77614.1; !1PID:g17774 !'##note the authors translated the codon GCT for residue 2 as Met COMMENT Acetolactate synthase, a flavoprotein, catalyzes the !1formation of acetohydroxy acids from the corresponding !1alpha-keto acids (i.e., the first step common to the !1biosynthesis of all branched-chain amino acids) in the !1presence of thiamine pyrophosphate and magnesium ion. CLASSIFICATION #superfamily acetolactate synthase large chain; thiamin !1pyrophosphate-binding domain homology KEYWORDS branched-chain amino acid biosynthesis; carbon-carbon lyase; !1chloroplast; flavoprotein; magnesium; oxo-acid-lyase; !1thiamin pyrophosphate FEATURE !$1-61 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$62-637 #product acetolactate synthase #status predicted !8#label MAT\ !$502-550 #domain thiamin pyrophosphate-binding domain homology !8#label TPB SUMMARY #length 637 #molecular-weight 69970 #checksum 9749 SEQUENCE /// ENTRY YCBYI #type complete TITLE acetolactate synthase (EC 4.1.3.18) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES acetohydroxy-acid synthase; protein YM9718.07; protein YMR108w ORGANISM #formal_name Saccharomyces cerevisiae DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 21-Jul-2000 ACCESSIONS A23808; S54569 REFERENCE A23808 !$#authors Falco, S.C.; Dumas, K.S.; Livak, K.J. !$#journal Nucleic Acids Res. (1985) 13:4011-4027 !$#title Nucleotide sequence of the yeast ILV2 gene which encodes !1acetolactate synthase. !$#cross-references MUID:85242085; PMID:2989783 !$#accession A23808 !'##molecule_type DNA !'##residues 1-687 ##label FAL !'##cross-references EMBL:X02549; NID:g3824; PIDN:CAA26400.1; PID:g3825 REFERENCE S54510 !$#authors Hunt, S.; Bowman, S. !$#submission submitted to the EMBL Data Library, May 1995 !$#accession S54569 !'##molecule_type DNA !'##residues 1-687 ##label HUN !'##cross-references EMBL:Z49702; NID:g817859; PIDN:CAA89744.1; !1PID:g817866; GSPDB:GN00013; MIPS:YMR108w !'##experimental_source strain AB972 GENETICS !$#gene SGD:ILV2; MIPS:YMR108w !'##cross-references SGD:S0004714; MIPS:YMR108w !$#map_position 13R CLASSIFICATION #superfamily acetolactate synthase large chain; thiamin !1pyrophosphate-binding domain homology KEYWORDS branched-chain amino acid biosynthesis; carbon-carbon lyase; !1flavoprotein; magnesium; oxo-acid-lyase; thiamin !1pyrophosphate FEATURE !$539-587 #domain thiamin pyrophosphate-binding domain homology !8#label TPB SUMMARY #length 687 #molecular-weight 74936 #checksum 6886 SEQUENCE /// ENTRY S39111 #type complete TITLE acetolactate synthase (EC 4.1.3.18) precursor - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES acetohydroxy-acid synthase ORGANISM #formal_name Schizosaccharomyces pombe DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 15-Oct-1999 ACCESSIONS S39111 REFERENCE S39111 !$#authors Bekkaoui, F.; Nadin-Davis, S.A.; Crosby, W.L. !$#journal Curr. Genet. (1993) 24:544-547 !$#title Isolation and structure of an acetolactate synthase gene !1from Schizosaccharomyces pombe and complementation of the !1ilv2 mutation in Saccharomyces cerevisiae. !$#cross-references MUID:94130341; PMID:8299177 !$#accession S39111 !'##molecule_type DNA !'##residues 1-669 ##label BEK !'##cross-references GB:L11293; NID:g406191; PIDN:AAA35315.1; !1PID:g406192 GENETICS !$#gene ilv1 CLASSIFICATION #superfamily acetolactate synthase large chain; thiamin !1pyrophosphate-binding domain homology KEYWORDS branched-chain amino acid biosynthesis; carbon-carbon lyase; !1flavoprotein; magnesium; mitochondrion; oxo-acid-lyase; !1thiamin pyrophosphate FEATURE !$1-141 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$142-669 #product acetolactate synthase #status predicted !8#label MAT\ !$537-585 #domain thiamin pyrophosphate-binding domain homology !8#label TPB SUMMARY #length 669 #molecular-weight 73185 #checksum 2688 SEQUENCE /// ENTRY S28920 #type complete TITLE acetolactate synthase (EC 4.1.3.18) - red alga (Porphyra umbilicalis) chloroplast ORGANISM #formal_name chloroplast Porphyra umbilicalis #common_name laver DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 15-Oct-1999 ACCESSIONS S28920; S27402 REFERENCE S28920 !$#authors Reith, M.; Munholland, J. !$#journal Curr. Genet. (1993) 23:59-65 !$#title Two amino-acid biosynthetic genes are encoded on the plastid !1genome of the red alga Porphyra umbilicalis. !$#cross-references MUID:93153832; PMID:8381336 !$#accession S28920 !'##molecule_type DNA !'##residues 1-590 ##label REI !'##cross-references EMBL:M94625; NID:g343129; PIDN:AAA03052.1; !1PID:g343130 GENETICS !$#gene ilvB !$#genome chloroplast CLASSIFICATION #superfamily acetolactate synthase large chain; thiamin !1pyrophosphate-binding domain homology KEYWORDS branched-chain amino acid biosynthesis; carbon-carbon lyase; !1chloroplast; flavoprotein; oxo-acid-lyase; thiamin !1pyrophosphate FEATURE !$444-492 #domain thiamin pyrophosphate-binding domain homology !8#label TPB SUMMARY #length 590 #molecular-weight 64929 #checksum 7828 SEQUENCE /// ENTRY A48648 #type complete TITLE acetolactate synthase (EC 4.1.3.18) large chain - Corynebacterium glutamicum ALTERNATE_NAMES acetohydroxy acid synthase ORGANISM #formal_name Corynebacterium glutamicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 15-Oct-1999 ACCESSIONS A48648 REFERENCE A48648 !$#authors Keilhauer, C.; Eggeling, L.; Sahm, H. !$#journal J. Bacteriol. (1993) 175:5595-5603 !$#title Isoleucine synthesis in Corynebacterium glutamicum: !1molecular analysis of the ilvB-ilvN-ilvC operon. !$#cross-references MUID:93374855; PMID:8366043 !$#accession A48648 !'##status preliminary !'##molecule_type DNA !'##residues 1-626 ##label KEI !'##cross-references GB:L09232; NID:g551777; PIDN:AAA62429.1; !1PID:g400334 !'##experimental_source ATCC 13032 GENETICS !$#gene ilvB !$#start_codon GTG CLASSIFICATION #superfamily acetolactate synthase large chain; thiamin !1pyrophosphate-binding domain homology KEYWORDS branched-chain amino acid biosynthesis; carbon-carbon lyase; !1flavoprotein; magnesium; oxo-acid-lyase; thiamin !1pyrophosphate FEATURE !$456-504 #domain thiamin pyrophosphate-binding domain homology !8#label TPB\ !$73 #active_site Glu #status predicted SUMMARY #length 626 #molecular-weight 66845 #checksum 4205 SEQUENCE /// ENTRY A56684 #type complete TITLE acetohydroxy acid synthase large chain - Brevibacterium flavum ORGANISM #formal_name Brevibacterium flavum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A56684 REFERENCE A56684 !$#authors Inui, M.; Vertes, A.A.; Kobayashi, M.; Kurusu, Y.; Yukawa, !1H. !$#journal DNA Seq. (1993) 3:303-310 !$#title Cloning and sequence determination of the acetohydroxy acid !1synthase genes from Brevibacterium flavum MJ233 by using the !1polymerase chain reaction. !$#cross-references MUID:94003401; PMID:8400360 !$#accession A56684 !'##status preliminary !'##molecule_type DNA !'##residues 1-594 ##label INU !'##cross-references GB:D13290; NID:g397822; PIDN:BAA02547.1; !1PID:g398941 GENETICS !$#gene ilvL CLASSIFICATION #superfamily acetolactate synthase large chain; thiamin !1pyrophosphate-binding domain homology KEYWORDS isoleucine-valine biosynthesis; leucine biosynthesis FEATURE !$431-479 #domain thiamin pyrophosphate-binding domain homology !8#label TPB SUMMARY #length 594 #molecular-weight 63553 #checksum 8231 SEQUENCE /// ENTRY JC1218 #type complete TITLE acetolactate synthase (EC 4.1.3.18), FAD-independent - Klebsiella pneumoniae ORGANISM #formal_name Klebsiella pneumoniae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 15-Oct-1999 ACCESSIONS JC1218 REFERENCE JC1218 !$#authors Peng, H.L.; Wang, P.Y.; Wu, C.M.; Hwang, D.C.; Chang, H.Y. !$#journal Gene (1992) 117:125-130 !$#title Cloning, sequencing and heterologous expression of a !1Klebsiella pneumoniae gene encoding an FAD-independent !1acetolactate synthase. !$#cross-references MUID:92354924; PMID:1644303 !$#accession JC1218 !'##molecule_type DNA !'##residues 1-559 ##label PEN !'##cross-references GB:M73842; NID:g149210; PIDN:AAA25079.1; !1PID:g149211 !'##note the authors translated the codon ATG for residue 550 as Leu, !1GGC for residue 551 as Met, CAG for residue 552 as Gly, and !1CTG for residue 553 as Gln COMMENT This enzyme is valine resistant and is the major enzyme for !1acetolactate synthesis in the 2,3-butanediol pathway. GENETICS !$#gene ilvK CLASSIFICATION #superfamily acetolactate synthase large chain; thiamin !1pyrophosphate-binding domain homology KEYWORDS carbon-carbon lyase; oxo-acid-lyase SUMMARY #length 559 #molecular-weight 60338 #checksum 361 SEQUENCE /// ENTRY D47069 #type complete TITLE alpha-acetolactate synthase - Klebsiella terrigena ORGANISM #formal_name Klebsiella terrigena DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 15-Oct-1999 ACCESSIONS D47069 REFERENCE A47069 !$#authors Blomqvist, K.; Nikkola, M.; Lehtovaara, P.; Suihko, M.L.; !1Airaksinen, U.; Straby, K.B.; Knowles, J.K.; Penttila, M.E. !$#journal J. Bacteriol. (1993) 175:1392-1404 !$#title Characterization of the genes of the 2,3-butanediol operons !1from Klebsiella terrigena and Enterobacter aerogenes. !$#cross-references MUID:93186707; PMID:8444801 !$#accession D47069 !'##status preliminary !'##molecule_type DNA !'##residues 1-559 ##label BLO !'##cross-references GB:L04507; NID:g149170; PIDN:AAA25055.1; !1PID:g149172 !'##experimental_source VTT-E-74023 !'##note sequence extracted from NCBI backbone (NCBIN:126766, !1NCBIP:126768) CLASSIFICATION #superfamily acetolactate synthase large chain; thiamin !1pyrophosphate-binding domain homology SUMMARY #length 559 #molecular-weight 60152 #checksum 7871 SEQUENCE /// ENTRY YCEC1L #type complete TITLE acetolactate synthase (EC 4.1.3.18) I large chain - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 01-Mar-2002 ACCESSIONS A93569; A93568; H65168; A23803; A23804 REFERENCE A93569 !$#authors Wek, R.C.; Hausser, C.A.; Hatfield, G.W. !$#journal Nucleic Acids Res. (1985) 13:3995-4010 !$#title The nucleotide sequence of the ilvBN operon of Escherichia !1coli: sequence homologies of the acetohydroxy acid synthase !1isozymes. !$#cross-references MUID:85242084; PMID:2989782 !$#accession A93569 !'##molecule_type DNA !'##residues 1-562 ##label WEK !'##cross-references GB:X02541; GB:J01633; GB:X01131; NID:g41783; !1PIDN:CAA26387.1; PID:g41785 REFERENCE A93568 !$#authors Friden, P.; Donegan, J.; Mullen, J.; Tsui, P.; Freundlich, !1M. !$#journal Nucleic Acids Res. (1985) 13:3979-3993 !$#title The ilvB locus of Escherichia coli K-12 is an operon !1encoding both subunits of acetohydroxy acid synthase I. !$#cross-references MUID:85242083; PMID:2989781 !$#accession A93568 !'##molecule_type DNA !'##residues 1-562 ##label FRI !'##cross-references GB:X02541; GB:J01633; GB:X01131; NID:g41783; !1PIDN:CAA26387.1; PID:g41785 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65168 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-562 ##label BLAT !'##cross-references GB:AE000444; GB:U00096; NID:g2367258; !1PIDN:AAC76694.1; PID:g1790104; UWGP:b3671 !'##experimental_source strain K-12, substrain MG1655 COMMENT Acetolactate synthase, a flavoprotein, catalyzes the !1formation of acetohydroxy acids from the corresponding !1alpha-keto acids (i.e., the first step common to the !1biosynthesis of branched-chain amino acids) in the presence !1of thiamine pyrophosphate and magnesium ion. The !1FAD-requiring active isozyme I, which is composed of a large !1chain and a small chain, is one of the isozymes sensitive to !1valine inhibition. GENETICS !$#gene ilvB !$#map_position 82 min CLASSIFICATION #superfamily acetolactate synthase large chain; thiamin !1pyrophosphate-binding domain homology KEYWORDS branched-chain amino acid biosynthesis; carbon-carbon lyase; !1FAD; flavoprotein; magnesium; oxo-acid-lyase; thiamin !1pyrophosphate; valine inhibition FEATURE !$433-481 #domain thiamin pyrophosphate-binding domain homology !8#label TPB SUMMARY #length 562 #molecular-weight 60440 #checksum 2238 SEQUENCE /// ENTRY YCEC #type complete TITLE acetolactate synthase (EC 4.1.3.18) II large chain, ilv0 phenotype - Escherichia coli (strain K-12) ALTERNATE_NAMES acetohydroxy acid synthase II large chain; acetolactate synthase large chain active form; acetolactate synthase valine-resistant isozyme; hypothetical protein o221; ilvG protein ORGANISM #formal_name Escherichia coli DATE 18-Dec-1981 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS A26570; S48893; A01112; JQ0875; S30665; S30666; B65180; !1C65180 REFERENCE A26570 !$#authors Lawther, R.P.; Wek, R.C.; Lopes, J.M.; Pereira, R.; Taillon, !1B.E.; Hatfield, G.W. !$#journal Nucleic Acids Res. (1987) 15:2137-2155 !$#title The complete nucleotide sequence of the ilvGMEDA operon of !1Escherichia coli K-12. !$#cross-references MUID:87174741; PMID:3550695 !$#accession A26570 !'##molecule_type DNA !'##residues 1-283,'S',285-548 ##label LAW1 !'##cross-references GB:M32253; NID:g146465; PIDN:AAA24021.1; !1PID:g146467 !'##genetics WLD REFERENCE S48893 !$#authors Lawther, R.P. !$#submission submitted to the EMBL Data Library, December 1987 !$#accession S48893 !'##molecule_type DNA !'##residues 1-548 ##label LAW2 !'##cross-references EMBL:X04890; NID:g288528; PIDN:CAA28573.1; !1PID:g288529 !'##genetics WLD REFERENCE A01112 !$#authors Lawther, R.P.; Calhoun, D.H.; Adams, C.W.; Hauser, C.A.; !1Gray, J.; Hatfield, G.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:922-925 !$#title Molecular basis of valine resistance in Escherichia coli !1K-12. !$#cross-references MUID:81199435; PMID:7015336 !$#accession A01112 !'##molecule_type DNA !'##residues 28-311,'A',313-503,'L',505-548 ##label LAW3 !'##cross-references GB:V00290; NID:g41797; PIDN:CAA23558.1; PID:g41799 !'##experimental_source K12, ilvG+ mutant ilv02096 REFERENCE JQ0872 !$#authors Coppola, G.; Huang, F.; Riley, J.; Cox, J.L.; Hantzopoulos, !1P.; Zhou, L.B.; Calhoun, D.H. !$#journal Gene (1991) 97:21-27 !$#title Sequence and transcriptional activity of the Escherichia !1coli K-12 chromosome region between rrnC and ilvGMEDA. !$#cross-references MUID:91138982; PMID:1995430 !$#accession JQ0875 !'##molecule_type DNA !'##residues 1-402 ##label COP !'##cross-references GB:M37337; NID:g147772; PIDN:AAA24608.1; !1PID:g147773 REFERENCE S30660 !$#authors Daniels, D.L.; Plunkett III, G.; Burland, V.; Blattner, F.R. !$#journal Science (1992) 257:771-778 !$#title Analysis of the Escherichia coli genome: DNA sequence of the !1region from 84.5 to 86.5 minutes. !$#cross-references MUID:92358234; PMID:1379743 !$#accession S30665 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-178,'XX',181-327 ##label DAN1 !'##cross-references EMBL:M87049; NID:g836656; PIDN:AAA67571.1; !1PID:g148175 !'##genetics PSU1 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1992 !$#accession S30666 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 'N',329-548 ##label DAN2 !'##cross-references EMBL:M87049 !'##genetics PSU2 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1992 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65180 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-327 ##label BLA1 !'##cross-references GB:AE000453; GB:U00096; NID:g2367276; !1PIDN:AAC77488.1; PID:g1790203; UWGP:b3767 !'##experimental_source strain K-12, substrain MG1655 !'##genetics PSU1 !$#accession C65180 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 'N',329-548 ##label BLA2 !'##cross-references GB:U00096; UWGP:b3768 !'##experimental_source strain K-12, substrain MG1655 !'##genetics PSU2 COMMENT The genomes of wild-type E. coli strains contain genes for !1three isozymes, but only the valine-inhibitable ones, ilvB !1(isozyme I) and ilvIH (isozyme III), are expressed; ilvG !1(isozyme II, valine-resistant) is expressed in strains !1having the ilv0 mutation. The ilv02096 mutation (an !1insertion of 2 base pairs) causes a frameshift in !1translation, permitting the expression of this isozyme. GENETICS WLD !$#gene ilvG !$#map_position 85 min GENETICS PSU1 !$#gene ilvG_1 !$#map_position 85 min GENETICS PSU2 !$#gene ilvG_2 !$#map_position 85 min !$#note a pseudogene FUNCTION !$#description catalyzes the reaction of carbon dioxide with acetolactic !1acid (2-hydroxy-2-methyl-3-oxobutanoic acid) to form 2 !1molecules of lactic acid !$#pathway branched-chain amino acid biosynthesis CLASSIFICATION #superfamily acetolactate synthase large chain; thiamin !1pyrophosphate-binding domain homology KEYWORDS branched-chain amino acid biosynthesis; carbon-carbon lyase; !1flavoprotein; oxo-acid-lyase; thiamin pyrophosphate; valine !1resistance FEATURE !$1-548 #product acetolactate synthase II large chain, active !8form #status predicted #label MAT2\ !$1-327 #product acetolactate synthase II large chain, !8inactive form #status predicted #label MAT1\ !$328-548 #region ilvG_2 pseudogene derived\ !$417-465 #domain thiamin pyrophosphate-binding domain homology !8#label TPB\ !$47 #active_site Glu #status predicted SUMMARY #length 548 #molecular-weight 59284 #checksum 826 SEQUENCE /// ENTRY YCEC3I #type complete TITLE acetolactate synthase (EC 4.1.3.18) III large chain - Escherichia coli (strain K-12) ALTERNATE_NAMES acetohydroxy-acid synthase III large chain ORGANISM #formal_name Escherichia coli DATE 28-Aug-1985 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS E64729; S14385; S40590; A01113; I41305 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64729 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-604 ##label BLAT !'##cross-references GB:AE000118; GB:U00096; NID:g1786262; !1PIDN:AAC73188.1; PID:g1786265; UWGP:b0077 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S14385 !$#authors Ayala, J.A. !$#submission submitted to the EMBL Data Library, January 1991 !$#accession S14385 !'##status preliminary !'##molecule_type DNA !'##residues 31-231,'SV',234-235,'V',237-283,'V',285-451,'S',453-536, !1'RG',540-552,'G',597,'KANLA',603, !1'RWNRCAIIAWCLLMLPSMAASTSTRCRFAGAEWMKCG' ##label AYA !'##cross-references EMBL:X55034 REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40590 !'##molecule_type DNA !'##residues 31-231,'SV',234-235,'V',237-283,'V',285-451,'S',453-536, !1'RG',540-552,'G',597,'KANLA',603, !1'RWNRCAIIAWCLLMLPSMAASTSTRCRFAGAEWMKCG' ##label YUR !'##cross-references EMBL:D10483 REFERENCE A93482 !$#authors Squires, C.H.; DeFelice, M.; Devereux, J.; Calvo, J.M. !$#journal Nucleic Acids Res. (1983) 11:5299-5313 !$#title Molecular structure of ilvIH and its evolutionary !1relationship to ilvG in Escherichia coli K12. !$#cross-references MUID:83272971; PMID:6308579 !$#accession A01113 !'##molecule_type DNA !'##residues 31-231,'SV',234-235,'V',237-283,'V',285-451,'S',453-536, !1'RG',540-552,'G',597,'KANLA',603, !1'RWNRCAIIAWCLLMLPSMAASTSTRCRFAGAEWMKCG' ##label SQU !'##cross-references GB:X01609; NID:g41794; PIDN:CAA25755.1; PID:g41795 REFERENCE I41305 !$#authors Haughn, G.W.; Squires, C.H.; DeFelice, M.; Largo, C.T.; !1Calvo, J.M. !$#journal J. Bacteriol. (1985) 163:186-198 !$#title Unusual organization of the ilvIH promoter of Escherichia !1coli. !$#cross-references MUID:85234358; PMID:3891724 !$#accession I41305 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 31-38 ##label RES !'##cross-references GB:M10738; NID:g146472; PIDN:AAA24026.1; !1PID:g146473 COMMENT Isozyme III is one of the isozymes sensitive to valine !1inhibition. GENETICS !$#gene ilvI !$#map_position 2 min COMPLEX heterodimer; composed of large chain and small chain FUNCTION !$#description catalyzes formation of acetohydroxy acids from the !1corresponding alpha-keto acids !$#pathway branched-chain amino acid biosynthesis !$#note thiamine pyrophosphate cofactor; magnesium required CLASSIFICATION #superfamily acetolactate synthase large chain; thiamin !1pyrophosphate-binding domain homology KEYWORDS branched-chain amino acid biosynthesis; carbon-carbon lyase; !1flavoprotein; magnesium; oxo-acid-lyase; thiamin !1pyrophosphate FEATURE !$467-515 #domain thiamin pyrophosphate-binding domain homology !8#label TPB\ !$81 #active_site Glu #status predicted SUMMARY #length 604 #molecular-weight 66475 #checksum 6599 SEQUENCE /// ENTRY C64131 #type complete TITLE acetolactate synthase (EC 4.1.3.18) III large chain - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 15-Oct-1999 ACCESSIONS C64131 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession C64131 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-573 ##label TIGR !'##cross-references GB:U32832; GB:L42023; NID:g1574421; !1PIDN:AAC23233.1; PID:g1574426; TIGR:HI1585 CLASSIFICATION #superfamily acetolactate synthase large chain; thiamin !1pyrophosphate-binding domain homology KEYWORDS branched-chain amino acid biosynthesis; carbon-carbon lyase; !1flavoprotein; magnesium; oxo-acid-lyase; thiamin !1pyrophosphate FEATURE !$436-484 #domain thiamin pyrophosphate-binding domain homology !8#label TPB SUMMARY #length 573 #molecular-weight 62619 #checksum 6746 SEQUENCE /// ENTRY S35138 #type complete TITLE acetolactate synthase (EC 4.1.3.18) - Lactococcus lactis subsp. lactis ORGANISM #formal_name Lactococcus lactis subsp. lactis #variety strain NCDO2118 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS S35138 REFERENCE S35132 !$#authors Godon, J.J.; Chopin, M.C.; Ehrlich, S.D. !$#journal J. Bacteriol. (1992) 174:6580-6589 !$#title Branched-chain amino acid biosynthesis genes in Lactococcus !1lactis subsp. lactis. !$#cross-references MUID:93015710; PMID:1400210 !$#accession S35138 !'##molecule_type DNA !'##residues 1-575 ##label GOD !'##cross-references EMBL:M90761; NID:g2565137; PIDN:AAB81919.1; !1PID:g2565157 GENETICS !$#gene ilvB CLASSIFICATION #superfamily acetolactate synthase large chain; thiamin !1pyrophosphate-binding domain homology KEYWORDS branched-chain amino acid biosynthesis; carbon-carbon lyase; !1flavoprotein; magnesium; oxo-acid-lyase; thiamin !1pyrophosphate FEATURE !$435-483 #domain thiamin pyrophosphate-binding domain homology !8#label TPB\ !$57 #active_site Glu #status predicted SUMMARY #length 575 #molecular-weight 63025 #checksum 5785 SEQUENCE /// ENTRY DCZMP #type complete TITLE pyruvate decarboxylase (EC 4.1.1.1) - maize ALTERNATE_NAMES alpha-ketoacid carboxylase ORGANISM #formal_name Zea mays #common_name maize DATE 30-Sep-1992 #sequence_revision 19-Oct-1995 #text_change 21-Jul-2000 ACCESSIONS S18347; S07001 REFERENCE S18347 !$#authors Kelley, P.M.; Godfrey, K.; Lal, S.K.; Alleman, M. !$#journal Plant Mol. Biol. (1991) 17:1259-1261 !$#title Characterization of the maize pyruvate decarboxylase gene. !$#cross-references MUID:92032792; PMID:1932699 !$#accession S18347 !'##molecule_type DNA !'##residues 1-610 ##label KEL !'##cross-references EMBL:X59546; NID:g22394; PIDN:CAA42120.1; !1PID:g22395 REFERENCE S07001 !$#authors Kelley, P.M. !$#journal Plant Mol. Biol. (1989) 13:213-222 !$#title Maize pyruvate decarboxylase mRNA is induced anaerobically. !$#cross-references MUID:92003668; PMID:2519113 !$#accession S07001 !'##molecule_type mRNA !'##residues 1-566,'MA',569-570,'D',572-610 ##label KE2 !'##cross-references GB:X17555; NID:g22393; PIDN:CAA35589.1; !1PID:g3970823 GENETICS !$#gene pdc !$#introns 180/3; 491/3; 554/3 CLASSIFICATION #superfamily acetolactate synthase large chain; thiamin !1pyrophosphate-binding domain homology KEYWORDS carbon-carbon lyase; carboxy-lyase; flavoprotein; !1homotetramer; thiamin pyrophosphate FEATURE !$476-522 #domain thiamin pyrophosphate-binding domain homology !8#label TPB SUMMARY #length 610 #molecular-weight 65427 #checksum 3601 SEQUENCE /// ENTRY DCBYP #type complete TITLE pyruvate decarboxylase (EC 4.1.1.1) 1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES alpha-ketoacid carboxylase; protein L2104; protein YLR044c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1991 #sequence_revision 19-Jul-1996 #text_change 16-Jun-2000 ACCESSIONS S64871; S64872; B37293; A26110; A37291; S61618 REFERENCE S64863 !$#authors Koetter, P.; Rose, M.; Entian, K.D. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64871 !'##molecule_type DNA !'##residues 1-563 ##label KOE !'##cross-references EMBL:Z73216; NID:g1360374; PIDN:CAA97573.1; !1PID:g1360375; GSPDB:GN00012; MIPS:YLR044c !'##note experimental_source strain S288C REFERENCE S64872 !$#authors Andre, B.; Urrestarazu, L.A. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64872 !'##molecule_type DNA !'##residues 1-139 ##label AND !'##cross-references EMBL:Z73216; GSPDB:GN00012; MIPS:YLR044c !'##note experimental_source strain S288C REFERENCE A37293 !$#authors Hohmann, S.; Cederberg, H. !$#journal Eur. J. Biochem. (1990) 188:615-621 !$#title Autoregulation may control the expression of yeast pyruvate !1decarboxylase structural genes PDC1 and PDC5. !$#cross-references MUID:90235833; PMID:2185016 !$#accession B37293 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type DNA !'##residues 1-105,'S',107-252,'S',254-335,'N',337-537,'V',539-550,'K', !1552-563 ##label HOH1 REFERENCE A26110 !$#authors Kellermann, E.; Seeboth, P.G.; Hollenberg, C.P. !$#journal Nucleic Acids Res. (1986) 14:8963-8977 !$#title Analysis of the primary structure and promoter function of a !1pyruvate decarboxylase gene (PDC1) from Saccharomyces !1cerevisiae. !$#cross-references MUID:87066770; PMID:3537965 !$#accession A26110 !'##molecule_type DNA !'##residues 1-105,'S',107-113,115-142,'C',144,'PQ',147-205,'V',207-252, !1'S',254-335,'N',337-537,'V',539-544,'CSTK',549,'G' ##label !1KEL !'##cross-references GB:X04675; NID:g4108; PIDN:CAA28380.1; PID:g4109 REFERENCE A37291 !$#authors Hohmann, S. !$#submission submitted to the Protein Sequence Database, March 1991 !$#accession A37291 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-54,'R',56-105,'S',107-142,'C',144-205,'V',207,'A', !1209-252,'S',254-335,'N',337-537,'V',539-563 ##label HOH2 REFERENCE S61618 !$#authors Urrestarazu, L.A. !$#submission submitted to the EMBL Data Library, December 1995 !$#accession S61618 !'##molecule_type DNA !'##residues 1-139 ##label URR !'##cross-references EMBL:X94607; NID:g1181264; PIDN:CAA64291.1; !1PID:g1181265 GENETICS !$#gene SGD:PDC1; MIPS:YLR044c !'##cross-references SGD:S0004034; MIPS:YLR044c !$#map_position 12R FUNCTION !$#description nonoxidative decarboxylation of pyruvate to acetaldehyde and !1carbon dioxide !$#note participates in the alcoholic fermentation pathway CLASSIFICATION #superfamily acetolactate synthase large chain; thiamin !1pyrophosphate-binding domain homology KEYWORDS carbon-carbon lyase; carboxy-lyase; flavoprotein; !1homotetramer; thiamin pyrophosphate FEATURE !$433-479 #domain thiamin pyrophosphate-binding domain homology !8#label TPB SUMMARY #length 563 #molecular-weight 61495 #checksum 5966 SEQUENCE /// ENTRY S36363 #type complete TITLE pyruvate decarboxylase (EC 4.1.1.1) - yeast (Kluyveromyces marxianus) ALTERNATE_NAMES alpha-ketoacid carboxylase ORGANISM #formal_name Kluyveromyces marxianus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-Nov-1999 ACCESSIONS S36363 REFERENCE S36363 !$#authors Holloway, P.; Subden, R.E. !$#journal Curr. Genet. (1993) 24:274-277 !$#title The isolation and nucleotide sequence of the pyruvate !1decarboxylase gene from Kluyveromyces marxianus. !$#cross-references MUID:94037155; PMID:8221939 !$#accession S36363 !'##molecule_type DNA !'##residues 1-564 ##label HOL !'##cross-references EMBL:L09727; NID:g173308; PIDN:AAA35267.1; !1PID:g173309 GENETICS !$#gene PDC1 CLASSIFICATION #superfamily acetolactate synthase large chain; thiamin !1pyrophosphate-binding domain homology KEYWORDS carbon-carbon lyase; carboxy-lyase FEATURE !$433-479 #domain thiamin pyrophosphate-binding domain homology !8#label TPB SUMMARY #length 564 #molecular-weight 61900 #checksum 5744 SEQUENCE /// ENTRY DCZYPZ #type complete TITLE pyruvate decarboxylase (EC 4.1.1.1) - Zymomonas mobilis ALTERNATE_NAMES alpha-ketoacid carboxylase ORGANISM #formal_name Zymomonas mobilis DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 15-Oct-1999 ACCESSIONS A26672; A28188; S29616 REFERENCE A26672 !$#authors Neale, A.D.; Scopes, R.K.; Wettenhall, R.E.H.; Hoogenraad, !1N.J. !$#journal Nucleic Acids Res. (1987) 15:1753-1761 !$#title Nucleotide sequence of the pyruvate decarboxylase gene from !1Zymomonas mobilis. !$#cross-references MUID:87146492; PMID:3029726 !$#accession A26672 !'##molecule_type DNA !'##residues 1-568 ##label NEA !'##cross-references GB:M15368; NID:g155599; PIDN:AAA27697.1; !1PID:g155600 !'##experimental_source strain ZM6, ATCC 29191 !'##note parts of this sequence were confirmed by protein sequencing REFERENCE A28188 !$#authors Reynen, M.; Sahm, H. !$#journal J. Bacteriol. (1988) 170:3310-3313 !$#title Comparison of the structural genes for pyruvate !1decarboxylase in different Zymomonas mobilis strains. !$#cross-references MUID:88257061; PMID:2838467 !$#accession A28188 !'##molecule_type DNA !'##residues 1-77,'H',79-156,'AK',159-199,'D',201-232,'T',234-340,'S', !1342-506,'A',508-568 ##label REY !'##cross-references GB:M20667 !'##experimental_source strain ZM6, ATCC 29191 REFERENCE S29616 !$#authors Candy, J.M.; Diefenbach, R.J.; Mattick, J.S.; Duggleby, R.G. !$#submission submitted to the EMBL Data Library, April 1991 !$#description Nucleotide sequence of the pyruvate decarboxylase gene from !1Zymomonas mobilis. !$#accession S29616 !'##status preliminary !'##molecule_type DNA !'##residues 1-568 ##label CAN !'##cross-references EMBL:X59558; NID:g48659; PIDN:CAA42157.1; !1PID:g48660 COMMENT This enzyme catalyzes the nonoxidative decarboxylation of !1pyruvate to produce acetaldehyde and carbon dioxide in the !1alcoholic fermentation pathway. GENETICS !$#gene pdc CLASSIFICATION #superfamily acetolactate synthase large chain; thiamin !1pyrophosphate-binding domain homology KEYWORDS carbon-carbon lyase; carboxy-lyase; flavoprotein; !1homotetramer; thiamin pyrophosphate FEATURE !$429-475 #domain thiamin pyrophosphate-binding domain homology !8#label TPB SUMMARY #length 568 #molecular-weight 60925 #checksum 4732 SEQUENCE /// ENTRY DCZYPC #type complete TITLE pyruvate decarboxylase (EC 4.1.1.1) - Zymomonas mobilis (strain CP4) ALTERNATE_NAMES alpha-ketoacid carboxylase ORGANISM #formal_name Zymomonas mobilis DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 05-Nov-1999 ACCESSIONS A26947 REFERENCE A26947 !$#authors Conway, T.; Osman, Y.A.; Konnan, J.I.; Hoffmann, E.M.; !1Ingram, L.O. !$#journal J. Bacteriol. (1987) 169:949-954 !$#title Promoter and nucleotide sequences of the Zymomonas mobilis !1pyruvate decarboxylase. !$#cross-references MUID:87137309; PMID:3029037 !$#accession A26947 !'##molecule_type DNA !'##residues 1-559 ##label CON !'##cross-references GB:M15393; NID:g155597; PIDN:AAA27696.1; !1PID:g155598 COMMENT This enzyme catalyzes the nonoxidative decarboxylation of !1pyruvate to produce acetaldehyde and carbon dioxide in the !1alcoholic fermentation pathway. GENETICS !$#gene pdc CLASSIFICATION #superfamily acetolactate synthase large chain; thiamin !1pyrophosphate-binding domain homology KEYWORDS carbon-carbon lyase; carboxy-lyase; flavoprotein; !1homotetramer; thiamin pyrophosphate FEATURE !$427-473 #domain thiamin pyrophosphate-binding domain homology !8#label TPB SUMMARY #length 559 #molecular-weight 60002 #checksum 8846 SEQUENCE /// ENTRY JN0782 #type complete TITLE pyruvate decarboxylase (EC 4.1.1.1) - Neurospora crassa ALTERNATE_NAMES cytosolic filament associated protein P59Nc (cfp) ORGANISM #formal_name Neurospora crassa DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Sep-2000 ACCESSIONS JN0782; PN0617; T46575 REFERENCE JN0782 !$#authors Alvarez, M.E.; Rosa, A.L.; Temporini, E.D.; Wolstenholme, !1A.; Panzetta, G.; Patrito, L.; Maccioni, H.J.F. !$#journal Gene (1993) 130:253-258 !$#title The 59-kDa polypeptide constituent of 8-10-nm cytoplasmic !1filaments in Neurospora crassa is a pyruvate decarboxylase. !$#cross-references MUID:93366182; PMID:8359692 !$#accession JN0782 !'##molecule_type mRNA !'##residues 1-570 ##label ALV !'##cross-references GB:L09125; NID:g293947; PIDN:AAA33567.1; !1PID:g293948 !$#accession PN0617 !'##molecule_type protein !'##residues 3-25 ##label AL1 REFERENCE Z23088 !$#authors Haedo, S.D.; Temporini, E.D.; Alvarez, M.E.; Maccioni, H.J.; !1Rosa, A.L. !$#journal Genetics (1992) 131:575-580 !$#title Molecular cloning of a gene (cfp) encoding the cytoplasmic !1filament protein P59Nc and its genetic relationship to the !1snowflake locus of Neurospora crassa. !$#cross-references MUID:92331897; PMID:1352758 !$#accession T46575 !'##status preliminary !'##molecule_type mRNA; protein !'##residues 3-25 ##label HAE !'##cross-references EMBL:S40298; NID:g251465; PIDN:AAB22524.1; !1PID:g251466 !'##note in GenBank entry S40298 the first two codons are not translated CLASSIFICATION #superfamily acetolactate synthase large chain; thiamin !1pyrophosphate-binding domain homology KEYWORDS carbon-carbon lyase; carboxy-lyase; flavoprotein; thiamin !1pyrophosphate FEATURE !$433-479 #domain thiamin pyrophosphate-binding domain homology !8#label TPB SUMMARY #length 570 #molecular-weight 62263 #checksum 9093 SEQUENCE /// ENTRY S44486 #type complete TITLE indole-3-pyruvate decarboxylase - Azospirillum brasilense ORGANISM #formal_name Azospirillum brasilense DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 15-Oct-1999 ACCESSIONS S44486 REFERENCE S44486 !$#authors Costacurta, A.; Keijers, V.; Vanderleyden, J. !$#journal Mol. Gen. Genet. (1994) 243:463-472 !$#title Molecular cloning and sequence analysis of an Azospirillum !1brasilense indole-3-pyruvate decarboxylase gene. !$#cross-references MUID:94261114; PMID:8202090 !$#accession S44486 !'##status preliminary !'##molecule_type DNA !'##residues 1-545 ##label COS !'##cross-references EMBL:L26240; NID:g442391; PIDN:AAC36886.1; !1PID:g508716 CLASSIFICATION #superfamily acetolactate synthase large chain; thiamin !1pyrophosphate-binding domain homology SUMMARY #length 545 #molecular-weight 57980 #checksum 1624 SEQUENCE /// ENTRY C44767 #type complete TITLE benzoylformate decarboxylase (EC 4.1.1.7) - Pseudomonas putida ORGANISM #formal_name Pseudomonas putida DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 15-Oct-1999 ACCESSIONS C44767 REFERENCE A44767 !$#authors Tsou, A.Y.; Ransom, S.C.; Gerlt, J.A.; Buechter, D.D.; !1Babbitt, P.C.; Kenyon, G.L. !$#journal Biochemistry (1990) 29:9856-9862 !$#title Mandelate pathway of Pseudomonas putida: sequence !1relationships involving mandelate racemase, (S)-mandelate !1dehydrogenase, and benzoylformate decarboxylase and !1expression of benzoylformate decarboxylase in Escherichia !1coli. !$#cross-references MUID:91104894; PMID:2271624 !$#accession C44767 !'##status preliminary !'##molecule_type DNA !'##residues 1-499 ##label TSO !'##cross-references EMBL:J05293; NID:g151353; PID:g151354 CLASSIFICATION #superfamily acetolactate synthase large chain; thiamin !1pyrophosphate-binding domain homology KEYWORDS carbon-carbon lyase; carboxy-lyase SUMMARY #length 499 #molecular-weight 53614 #checksum 3057 SEQUENCE /// ENTRY JT0742 #type complete TITLE tartronate-semialdehyde synthase (EC 4.1.1.47) - Escherichia coli (strain K-12) ALTERNATE_NAMES glyoxylate carbo-ligase ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS JT0742; PN0053; B64782 REFERENCE JT0742 !$#authors Chang, Y.Y.; Wang, A.Y.; Cronan Jr., J.E. !$#journal J. Biol. Chem. (1993) 268:3911-3919 !$#title Molecular cloning, DNA sequencing, and biochemical analyses !1of Escherichia coli glyoxylate carboligase. !$#cross-references MUID:93179387; PMID:8440684 !$#accession JT0742 !'##molecule_type DNA !'##residues 1-593 ##label CHA !'##cross-references GB:L03845; NID:g146118; PIDN:AAA23864.1; !1PID:g146119 !'##experimental_source strain K-12 !$#accession PN0053 !'##molecule_type protein !'##residues 2-31 ##label CH2 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64782 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-593 ##label BLAT !'##cross-references GB:AE000157; GB:U00096; NID:g1786716; !1PIDN:AAC73609.1; PID:g1786717; UWGP:b0507 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene gcl FUNCTION !$#description catalyzes condensation of two molecules of glyoxylate to !1give tartronic semialdehyde !$#pathway glyoxylate catabolism CLASSIFICATION #superfamily acetolactate synthase large chain; thiamin !1pyrophosphate-binding domain homology KEYWORDS carbon-carbon lyase; carboxy-lyase; FAD; flavoprotein; !1thiamin pyrophosphate FEATURE !$2-593 #product tartronate-semialdehyde synthase #status !8experimental #label MAT\ !$435-483 #domain thiamin pyrophosphate-binding domain homology !8#label TPB SUMMARY #length 593 #molecular-weight 64731 #checksum 8186 SEQUENCE /// ENTRY YCEC3H #type complete TITLE acetolactate synthase (EC 4.1.3.18) III small chain - Escherichia coli (strain K-12) ALTERNATE_NAMES acetohydroxy-acid synthase III small chain ORGANISM #formal_name Escherichia coli DATE 28-Aug-1985 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS F64729; S14386; S40591; A01114; PS0152 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64729 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-163 ##label BLAT !'##cross-references GB:AE000118; GB:U00096; NID:g1786262; !1PIDN:AAC73189.1; PID:g1786266; UWGP:b0078 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S14385 !$#authors Ayala, J.A. !$#submission submitted to the EMBL Data Library, January 1991 !$#accession S14386 !'##status preliminary !'##molecule_type DNA !'##residues 1-131,'S',133-163 ##label AYA !'##cross-references EMBL:X55034; NID:g40841; PIDN:CAA38855.1; !1PID:g40846 REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40591 !'##status preliminary !'##molecule_type DNA !'##residues 1-131,'S',133-163 ##label YUR !'##cross-references EMBL:D10483; NID:g216434; PIDN:BAA01346.1; !1PID:g216495 REFERENCE A93482 !$#authors Squires, C.H.; DeFelice, M.; Devereux, J.; Calvo, J.M. !$#journal Nucleic Acids Res. (1983) 11:5299-5313 !$#title Molecular structure of ilvIH and its evolutionary !1relationship to ilvG in Escherichia coli K12. !$#cross-references MUID:83272971; PMID:6308579 !$#accession A01114 !'##molecule_type DNA !'##residues 1-131,'S',133-158,'V',160 ##label SQU !'##cross-references GB:X01609; NID:g41794; PIDN:CAA25756.1; PID:g41796 REFERENCE JU0297 !$#authors Leclerc, G.; Noel, G.; Drapeau, G.R. !$#journal J. Bacteriol. (1990) 172:4696-4700 !$#title Molecular cloning, nucleotide sequence, and expression of !1shl, a new gene in the 2-minute region of the genetic map of !1Escherichia coli. !$#cross-references MUID:90330585; PMID:2198273 !$#accession PS0152 !'##status translation not shown !'##molecule_type DNA !'##residues 130-163 ##label LEC !'##cross-references GB:M35034; NID:g147815; PIDN:AAA24627.1; !1PID:g147816 GENETICS !$#gene ilvH !$#map_position 2 min COMPLEX the active isozyme III is composed of chain H and chain I FUNCTION !$#description catalyzes formation of acetohydroxy acids from the !1corresponding alpha-keto acids !$#pathway branched-chain amino acid biosynthesis !$#note thiamine pyrophosphate cofactor; magnesium required !$#note sensitive to valine inhibition CLASSIFICATION #superfamily acetolactate synthase small chain KEYWORDS branched-chain amino acid biosynthesis; carbon-carbon lyase; !1flavoprotein; magnesium; oxo-acid-lyase; thiamin !1pyrophosphate; valine inhibition SUMMARY #length 163 #molecular-weight 17977 #checksum 7095 SEQUENCE /// ENTRY YCEC1S #type complete TITLE acetolactate synthase (EC 4.1.3.18) I small chain - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1988 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS G65168; B93569; B93568; D26925; B23803; B23804 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65168 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-96 ##label BLAT !'##cross-references GB:AE000444; GB:U00096; NID:g2367258; !1PIDN:AAC76693.1; PID:g1790103; UWGP:b3670 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A93569 !$#authors Wek, R.C.; Hausser, C.A.; Hatfield, G.W. !$#journal Nucleic Acids Res. (1985) 13:3995-4010 !$#title The nucleotide sequence of the ilvBN operon of Escherichia !1coli: sequence homologies of the acetohydroxy acid synthase !1isozymes. !$#cross-references MUID:85242084; PMID:2989782 !$#accession B93569 !'##molecule_type DNA !'##residues 1-23,'D',25-96 ##label WEK !'##cross-references GB:X02541; GB:J01633; GB:X01131; NID:g41783; !1PIDN:CAA26388.1; PID:g41786 REFERENCE A93568 !$#authors Friden, P.; Donegan, J.; Mullen, J.; Tsui, P.; Freundlich, !1M. !$#journal Nucleic Acids Res. (1985) 13:3979-3993 !$#title The ilvB locus of Escherichia coli K-12 is an operon !1encoding both subunits of acetohydroxy acid synthase I. !$#cross-references MUID:85242083; PMID:2989781 !$#accession B93568 !'##molecule_type DNA !'##residues 1-23,'D',25-96 ##label FRI !'##cross-references GB:X02541; GB:J01633; GB:X01131; NID:g41783; !1PIDN:CAA26388.1; PID:g41786 REFERENCE A30395 !$#authors Friedrich, M.J.; Kadner, R.J. !$#journal J. Bacteriol. (1987) 169:3556-3563 !$#title Nucleotide sequence of the uhp region of Escherichia coli. !$#cross-references MUID:87279903; PMID:3301805 !$#accession D26925 !'##molecule_type DNA !'##residues 69-96 ##label FR2 !'##cross-references GB:M17102; NID:g148110; PIDN:AAA24719.1; !1PID:g148111 GENETICS !$#gene ilvN !$#map_position 82 min COMPLEX heterodimer of large and small chain FUNCTION !$#description acetolactate synthase, a flavoprotein, catalyzes the !1formation of acetohydroxy acids from the corresponding !1alpha-keto acids (i.e., the first step common to the !1biosynthesis of branched-chain amino acids) in the presence !1of thiamine pyrophosphate and magnesium ion; the !1FAD-requiring active isozyme I is composed of a large and a !1small chain; the small chain may be responsible for the !1sensitivity of the isozyme to valine inhibition. !$#pathway branched-chain amino acid biosynthesis CLASSIFICATION #superfamily acetolactate synthase small chain KEYWORDS branched-chain amino acid biosynthesis; carbon-carbon lyase; !1FAD; flavoprotein; magnesium; oxo-acid-lyase; thiamin !1pyrophosphate; valine inhibition SUMMARY #length 96 #molecular-weight 11106 #checksum 5744 SEQUENCE /// ENTRY NNEC1 #type complete TITLE anthranilate synthase (EC 4.1.3.27) component I - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Nov-1980 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS C64874; D93746; A94643; I56371; A01115 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64874 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-520 ##label BLAT !'##cross-references GB:AE000224; GB:U00096; NID:g1787509; !1PIDN:AAC74346.1; PID:g1787518; UWGP:b1264 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A93746 !$#authors Yanofsky, C.; Platt, T.; Crawford, I.P.; Nichols, B.P.; !1Christie, G.E.; Horowitz, H.; van Cleemput, M.; Wu, A.M. !$#journal Nucleic Acids Res. (1981) 9:6647-6668 !$#title The complete nucleotide sequence of the tryptophan operon of !1Escherichia coli. !$#cross-references MUID:82150258; PMID:7038627 !$#accession D93746 !'##molecule_type DNA !'##residues 1-146,'S',148-520 ##label YAN !'##cross-references GB:J01714; GB:M12471; GB:M12472; GB:M24865; !1GB:M25264; GB:M25593; GB:M59208; NID:g147953; !1PIDN:AAA57297.1; PID:g147955 REFERENCE A94643 !$#authors Li, S.L.; Hanlon, J.; Yanofsky, C. !$#journal Biochemistry (1974) 13:1736-1744 !$#title Separation of anthranilate synthetase components I and II of !1Escherichia coli, Salmonella typhimurium, and Serratia !1marcescens and determination of their amino-terminal !1sequences by automatic Edman degradation. !$#cross-references MUID:74173403; PMID:4598537 !$#accession A94643 !'##molecule_type protein !'##residues 1-12,'S',14-25 ##label LIS !'##experimental_source strain trpA2/ColVB REFERENCE I56371 !$#authors Nichols, B.P.; van Cleemput, M.; Yanofsky, C. !$#journal J. Mol. Biol. (1981) 146:45-54 !$#title Nucleotide sequence of Escherichia coli trpE. Anthranilate !1synthetase component I contains no tryptophan residues. !$#cross-references MUID:81267360; PMID:7021857 !$#accession I56371 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-146,'S',148-520 ##label RES !'##cross-references EMBL:V00368; NID:g43195; PIDN:CAA23666.1; !1PID:g43196 GENETICS !$#gene trpE !$#map_position 28 min COMPLEX heterotetramer; two components I and two components II FUNCTION COM !$#description anthranilate synthase catalyzes biosynthesis of anthranilate !1from chorismate and glutamine !$#pathway tryptophan biosynthesis !$#note component II is larger and its carboxyl-terminal two-thirds !1has anthranilate phosphoribosyltransferase (EC 2.4.2.18) !1activity FUNCTION COI !$#description component I catalyzes the formation of anthranilate using !1ammonia rather than glutamine FUNCTION COII !$#description component II provides the glutamine amidotransferase !1activity CLASSIFICATION #superfamily anthranilate synthase component I KEYWORDS carbon-carbon lyase; oxo-acid-lyase; tryptophan biosynthesis SUMMARY #length 520 #molecular-weight 57494 #checksum 2157 SEQUENCE /// ENTRY NNEB1C #type fragment TITLE anthranilate synthase (EC 4.1.3.27) component I - Citrobacter freundii (fragment) ORGANISM #formal_name Citrobacter freundii DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 05-Dec-1998 ACCESSIONS A01116 REFERENCE A91792 !$#authors Blumenberg, M.; Yanofsky, C. !$#journal J. Bacteriol. (1982) 152:57-62 !$#title Evolutionary divergence of the Citrobacter freundii !1tryptophan operon regulatory region: comparison with other !1enteric bacteria. !$#cross-references MUID:83007061; PMID:6749821 !$#accession A01116 !'##molecule_type DNA !'##residues 1-150 ##label BLU GENETICS !$#gene trpE FUNCTION !$#description anthranilate synthase catalyzes biosynthesis of anthranilate !1from chorismate and glutamine !$#pathway tryptophan biosynthesis CLASSIFICATION #superfamily anthranilate synthase component I KEYWORDS carbon-carbon lyase; oxo-acid-lyase; tryptophan biosynthesis SUMMARY #length 150 #checksum 9123 SEQUENCE /// ENTRY I40052 #type complete TITLE anthranilate synthase (EC 4.1.3.27) component I - Buchnera aphidicola ORGANISM #formal_name Buchnera aphidicola DATE 09-Mar-1996 #sequence_revision 12-Apr-1996 #text_change 18-Jun-1999 ACCESSIONS I40052; I40054; S44087; S44089 REFERENCE A55261 !$#authors Lai, C.Y.; Baumann, L.; Baumann, P. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1994) 91:3819-3823 !$#title Amplification of trpEG: adaptation of Buchnera aphidicola to !1an endosymbiotic association with aphids. !$#cross-references MUID:94224833; PMID:8170994 !$#accession I40052 !'##status preliminary !'##molecule_type DNA !'##residues 1-515 ##label RES !'##cross-references EMBL:Z21938; NID:g472880; PIDN:CAA79931.1; !1PID:g472881 !$#accession I40054 !'##molecule_type DNA !'##residues 1-49 ##label RE2 !'##cross-references EMBL:Z21938; NID:g472880; PIDN:CAA79933.1; !1PID:g472883 GENETICS !$#gene trpE COMPLEX tetramer; two component I and two component II chains FUNCTION !$#description anthranilate synthase catalyzes biosynthesis of anthranilate !1from chorismate and glutamine !$#pathway tryptophan biosynthesis FUNCTION COI !$#description component I catalyzes the formation of anthranilate using !1ammonia rather than glutamine FUNCTION COII !$#description component II provides the glutamine amidotransferase !1activity CLASSIFICATION #superfamily anthranilate synthase component I KEYWORDS carbon-carbon lyase; oxo-acid-lyase; tryptophan biosynthesis SUMMARY #length 515 #molecular-weight 58687 #checksum 1089 SEQUENCE /// ENTRY NNEB1T #type complete TITLE anthranilate synthase (EC 4.1.3.27) component I - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 29-Jul-1981 #sequence_revision 27-Jun-1983 #text_change 18-Jun-1999 ACCESSIONS A92878; C94643; A92850; E92860; A39812; A01118 REFERENCE A92878 !$#authors Yanofsky, C.; van Cleemput, M. !$#journal J. Mol. Biol. (1982) 155:235-246 !$#title Nucleotide sequence of trpE of Salmonella typhimurium and !1its homology with the corresponding sequence of Escherichia !1coli. !$#cross-references MUID:82192438; PMID:7042989 !$#accession A92878 !'##molecule_type DNA !'##residues 1-520 ##label YAN REFERENCE A94643 !$#authors Li, S.L.; Hanlon, J.; Yanofsky, C. !$#journal Biochemistry (1974) 13:1736-1744 !$#title Separation of anthranilate synthetase components I and II of !1Escherichia coli, Salmonella typhimurium, and Serratia !1marcescens and determination of their amino-terminal !1sequences by automatic Edman degradation. !$#cross-references MUID:74173403; PMID:4598537 !$#accession C94643 !'##molecule_type protein !'##residues 1-25 ##label LIS !'##experimental_source strain St-13 REFERENCE A92850 !$#authors Lee, F.; Bertrand, K.; Bennett, G.; Yanofsky, C. !$#journal J. Mol. Biol. (1978) 121:193-217 !$#title Comparison of the nucleotide sequences of the initial !1transcribed regions of the tryptophan operons of Escherichia !1coli and Salmonella typhimurium. !$#cross-references MUID:78196931; PMID:351195 !$#accession A92850 !'##molecule_type DNA !'##residues 1-39 ##label LEE !'##cross-references GB:M24960; NID:g154399; PIDN:AAA27238.1; !1PID:g154400 REFERENCE A92860 !$#authors Nichols, B.P.; Miozzari, G.F.; van Cleemput, M.; Bennett, !1G.N.; Yanofsky, C. !$#journal J. Mol. Biol. (1980) 142:503-517 !$#title Nucleotide sequences of the trpG regions of Escherichia !1coli, Shigella dysenteriae, Salmonella typhimurium and !1Serratia marcescens. !$#cross-references MUID:81119810; PMID:7007652 !$#accession E92860 !'##molecule_type DNA !'##residues 495-520 ##label NIC !'##cross-references GB:J01811; NID:g154390; PIDN:AAA57311.1; !1PID:g154391 !'##experimental_source strain LT-2 REFERENCE A39812 !$#authors Caligiuri, M.G.; Bauerle, R. !$#journal J. Biol. Chem. (1991) 266:8328-8335 !$#title Identification of amino acid residues involved in feedback !1regulation of the anthranilate synthase complex from !1Salmonella typhimurium. Evidence for an amino-terminal !1regulatory site. !$#cross-references MUID:91217069; PMID:2022650 !$#accession A39812 !'##status preliminary; nucleic acid sequence not shown; not compared !1with conceptual translation !'##molecule_type DNA !'##residues 1-60,'I',62-69,'I',71-114,'D',116-163,'L',165-186,'Q', !1188-347,'I',349-358,'LS',361-367,'L',369-394,'Y',396,'M', !1398-439,'E',441,'D',443-480,'Q',482-520 ##label CAL GENETICS !$#gene trpE !$#map_position 34 min COMPLEX heterotetramer; two components I and two components II FUNCTION COM !$#description anthranilate synthase catalyzes biosynthesis of anthranilate !1from chorismate and glutamine !$#pathway tryptophan biosynthesis !$#note component II is larger and its carboxyl-terminal two-thirds !1has anthranilate phosphoribosyltransferase (EC 2.4.2.18) !1activity FUNCTION COI !$#description component I catalyzes the formation of anthranilate using !1ammonia rather than glutamine FUNCTION COII !$#description component II provides the glutamine amidotransferase !1activity CLASSIFICATION #superfamily anthranilate synthase component I KEYWORDS carbon-carbon lyase; oxo-acid-lyase; tryptophan biosynthesis SUMMARY #length 520 #molecular-weight 56996 #checksum 684 SEQUENCE /// ENTRY NNBS1 #type complete TITLE anthranilate synthase (EC 4.1.3.27) component I - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 13-Aug-1986 #sequence_revision 10-Feb-1995 #text_change 21-Jul-2000 ACCESSIONS A01119; A22794; A22063; I40036; C69726 REFERENCE A91509 !$#authors Band, L.; Shimotsu, H.; Henner, D.J. !$#journal Gene (1984) 27:55-65 !$#title Nucleotide sequence of the Bacillus subtilis trpE and trpD !1genes. !$#cross-references MUID:84183611; PMID:6425119 !$#accession A01119 !'##molecule_type DNA !'##residues 1-79,'P',81-119,'S',121-342, !1'DITCSLILPETISRQSSRVWFCFCAGVHKNCFLFTCHAHYLGGYRPIEKRGSSCRCTDV !1C',403-515 ##label BAN !'##note this sequence has been corrected REFERENCE A91520 !$#authors Henner, D.J.; Band, L.; Shimotsu, H. !$#journal Gene (1985) 34:169-177 !$#title Nucleotide sequence of the Bacillus subtilis tryptophan !1operon. !$#cross-references MUID:85232062; PMID:3924737 !$#accession A22794 !'##molecule_type DNA !'##residues 1-515 ##label HEN !'##cross-references GB:K01391; NID:g143767; PIDN:AAA22865.1; !1PID:g143768 REFERENCE A22063 !$#authors Shimotsu, H.; Henner, D.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:6315-6319 !$#title Characterization of the Bacillus subtilis tryptophan !1promoter region. !$#cross-references MUID:85038507; PMID:6436812 !$#accession A22063 !'##molecule_type DNA !'##residues 1-40 ##label SHI REFERENCE I40036 !$#authors Shimotsu, H.; Kuroda, M.I.; Yanofsky, C.; Henner, D.J. !$#journal J. Bacteriol. (1986) 166:461-471 !$#title Novel form of transcription attenuation regulates expression !1of the Bacillus subtilis tryptophan operon. !$#cross-references MUID:86195832; PMID:2422155 !$#accession I40036 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-40 ##label RES !'##cross-references GB:M27566; NID:g143787; PIDN:AAA22875.1; !1PID:g143788 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69726 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-515 ##label KUN !'##cross-references GB:Z99115; GB:AL009126; NID:g2634478; !1PIDN:CAB14184.1; PID:g2634686 !'##experimental_source strain 168 GENETICS !$#gene trpE !$#map_position 205 (degrees) CLASSIFICATION #superfamily anthranilate synthase component I KEYWORDS carbon-carbon lyase; oxo-acid-lyase; tryptophan biosynthesis SUMMARY #length 515 #molecular-weight 58116 #checksum 4011 SEQUENCE /// ENTRY NNBY1 #type complete TITLE anthranilate synthase (EC 4.1.3.27) component I - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YER090w ORGANISM #formal_name Saccharomyces cerevisiae DATE 20-Sep-1984 #sequence_revision 17-Feb-1995 #text_change 23-Mar-2001 ACCESSIONS A49701; A01120; S50593; S55760; S25640 REFERENCE A49701 !$#authors Graf, R.; Mehmann, B.; Braus, G.H. !$#journal J. Bacteriol. (1993) 175:1061-1068 !$#title Analysis of feedback-resistant anthranilate synthases from !1Saccharomyces cerevisiae. !$#cross-references MUID:93163033; PMID:8432699 !$#accession A49701 !'##molecule_type DNA !'##residues 1-507 ##label GRA !'##cross-references EMBL:X68327; NID:g4669; PIDN:CAA48402.1; PID:g4670 !'##experimental_source strain S288C !'##note sequence extracted from NCBI backbone (NCBIN:124747, !1NCBIP:124748) REFERENCE A92473 !$#authors Zalkin, H.; Paluh, J.L.; van Cleemput, M.; Moye, W.S.; !1Yanofsky, C. !$#journal J. Biol. Chem. (1984) 259:3985-3992 !$#title Nucleotide sequence of Saccharomyces cerevisiae genes TRP2 !1and TRP3 encoding bifunctional anthranilate !1synthase:indole-3-glycerol phosphate synthase. !$#cross-references MUID:84162082; PMID:6323449 !$#accession A01120 !'##molecule_type DNA !'##residues 1-203,'DRRFLANTI',213-219,'PNQLLNRMWARKVTKITSP',239-261, !1'SRYILSIFTD',269-275,'I',277-322,'A',324-329,'G',331-400, !1'TN',403-460, !1'LTCKLAVVLFTIQLSTMNMLETMNNDGQSQYYCASRRIVGRYRRISLKRAFSVFFPLDD !1IFIVFE' ##label ZAL !'##cross-references GB:K01388; NID:g173042; PIDN:AAA35175.1; !1PID:g173043 REFERENCE S50436 !$#authors Dietrich, F.S. !$#submission submitted to the EMBL Data Library, December 1994 !$#description The sequence of S. cerevisiae cosmids 9747, 8198, 9781, and !1lambda clones 3612 and 6052. !$#accession S50593 !'##molecule_type DNA !'##residues 1-507 ##label DIE !'##cross-references EMBL:U18839; NID:g603313; PIDN:AAB64645.1; !1PID:g603328; GSPDB:GN00005; MIPS:YER090w REFERENCE S55757 !$#authors Boucherie, H.; Dujardin, G.; Kermorgant, M.; Monribot, C.; !1Slonimski, P.; Perrot, M. !$#journal Yeast (1995) 11:601-613 !$#title Two-dimensional protein map of Saccharomyces cerevisiae: !1construction of a gene-protein index. !$#cross-references MUID:96093904; PMID:7483834 !$#accession S55760 !'##molecule_type protein !'##residues 3-14,'X',16 ##label BOU COMMENT Anthranilate synthase catalyzes the biosynthesis of !1anthranilate from chorismate and glutamine. It contains two !1chains with different catalytic activities: component I !1catalyzes the formation of anthranilate using ammonia rather !1than glutamine, whereas component II provides the glutamine !1amidotransferase activity. In yeast, component II is smaller !1and its carboxyl end also has indole-3-glycerol phosphate !1synthase (EC 4.1.1.48) activity. GENETICS !$#gene SGD:TRP2; MIPS:YER090w !'##cross-references SGD:S0000892; MIPS:YER090w !$#map_position 5R FUNCTION !$#description carbon-carbon lyase; oxo-acid-lyase !$#pathway tryptophan biosynthesis CLASSIFICATION #superfamily anthranilate synthase component I KEYWORDS carbon-carbon lyase; heterodimer; oxo-acid-lyase; tryptophan !1biosynthesis SUMMARY #length 507 #molecular-weight 56767 #checksum 4221 SEQUENCE /// ENTRY AGEC1 #type complete TITLE p-aminobenzoate synthase (EC 4.1.3.-) component I - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 01-Mar-2002 ACCESSIONS A30251; I54137; D64942 REFERENCE A30251 !$#authors Goncharoff, P.; Nichols, B.P. !$#journal J. Bacteriol. (1984) 159:57-62 !$#title Nucleotide sequence of Escherichia coli pabB indicates a !1common evolutionary origin of p-aminobenzoate synthetase and !1anthranilate synthetase. !$#cross-references MUID:84239604; PMID:6330050 !$#accession A30251 !'##molecule_type DNA !'##residues 1-453 ##label GON !'##cross-references EMBL:K02673; NID:g147057; PIDN:AAA24266.1; !1PID:g147058 REFERENCE I54137 !$#authors Guttman, D.S.; Dykhuizen, D.E. !$#journal Genetics (1994) 138:993-1003 !$#title Detecting selective sweeps in naturally occurring !1Escherichia coli. !$#cross-references MUID:95203706; PMID:7896119 !$#accession I54137 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 42-377 ##label RES !'##cross-references EMBL:U07748; NID:g468152; PIDN:AAC43269.1; !1PID:g468153 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64942 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-453 ##label BLAT !'##cross-references GB:AE000275; GB:U00096; NID:g1788106; !1PIDN:AAC74882.1; PID:g1788114; UWGP:b1812 !'##experimental_source strain K-12, substrain MG1655 COMMENT This enzyme catalyzes the biosynthesis of p-aminobenzoate !1(PABA) from chorismate and glutamine. It consists of two !1nonidentical chains: component I catalyzes the formation of !1PABA by binding chorismate and ammonia; component II !1provides the glutamine amidotransferase activity. GENETICS !$#gene pabB !$#map_position 40 min CLASSIFICATION #superfamily anthranilate synthase component I KEYWORDS carbon-carbon lyase; oxo-acid-lyase; p-aminobenzoate !1biosynthesis SUMMARY #length 453 #molecular-weight 50969 #checksum 4792 SEQUENCE /// ENTRY S63364 #type complete TITLE p-aminobenzoate synthase (EC 4.1.3.-) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein N3286; protein YNR033w CONTAINS chorismate aminase; glutamine amidotransferase ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S63364; S62014; S33968; S70383 REFERENCE S63346 !$#authors Pohl, T.M. !$#submission submitted to the Protein Sequence Database, April 1996 !$#accession S63364 !'##molecule_type DNA !'##residues 1-787 ##label POH !'##cross-references EMBL:Z71648; NID:g1302530; PIDN:CAA96313.1; !1PID:g1302531; GSPDB:GN00014; MIPS:YNR033w !'##experimental_source strain S288C REFERENCE S62014 !$#authors Shen, W.C.; Stanford, D.R.; Hopper, A.K. !$#submission submitted to the EMBL Data Library, December 1995 !$#description Los1p, involved in yeast pre-tRNA splicing, positively !1regulates members of the SOL gene family. !$#accession S62014 !'##molecule_type DNA !'##residues 1-170,'P',172-580,'KVFEVGMQ',589,'HAK',592-721,'L',722-787 !1##label SHE !'##cross-references EMBL:U43608; NID:g1163190; PIDN:AAB49319.1; !1PID:g1163191 REFERENCE S33968 !$#authors Edman, J.C.; Goldstein, A.L.; Erbe, J.G. !$#journal Yeast (1993) 9:669-675 !$#title Para-aminobenzoate synthase gene of Saccharomyces cerevisiae !1encodes a bifunctional enzyme. !$#cross-references MUID:93348779; PMID:8346682 !$#accession S33968 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-170,'P',172-532,'T',534-579,'VKVFEVGMQ',589,'HS',592,'L', !1593-620,'S',622-715,'QWWST',718,'WLQRCH',725,'II',728,'L' !1##label EDM REFERENCE S70383 !$#authors Shen, W.C.; Stanford, D.R.; Hopper, A.K. !$#journal Genetics (1996) 143:699-712 !$#title Los1p, involved in yeast pre-tRNA splicing, positively !1regulates members of the SOL gene family. !$#cross-references MUID:96363906; PMID:8725220 !$#accession S70383 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-170,'P',172-580,'KVFEVGMQ',589,'HAK',592-721,'L',722-787 !1##label SHW !'##cross-references EMBL:U43608; NID:g1163190; PIDN:AAB49319.1; !1PID:g1163191 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1995 GENETICS !$#gene SGD:ABZ1; MIPS:YNR033w !'##cross-references SGD:S0005316; MIPS:YNR033w !$#map_position 14R CLASSIFICATION #superfamily yeast p-aminobenzoate synthase; trpG homology KEYWORDS carbon-carbon lyase; multifunctional enzyme; oxo-acid-lyase; !1p-aminobenzoate biosynthesis; transferase FEATURE !$17-224 #domain trpG homology #label TRG\ !$112 #active_site Cys #status predicted SUMMARY #length 787 #molecular-weight 88543 #checksum 7020 SEQUENCE /// ENTRY JN0531 #type complete TITLE p-aminobenzoic acid synthase (EC 4.1.3.-) - Streptomyces griseus ORGANISM #formal_name Streptomyces griseus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JN0531 REFERENCE JN0530 !$#authors Criado, L.M.; Martin, J.F.; Gil, J.A. !$#journal Gene (1993) 126:135-139 !$#title The pab gene of Streptomyces griseus, encoding !1p-aminobenzoic acid synthase, is located between genes !1possibly involved in candicidin biosynthesis. !$#cross-references MUID:93231527; PMID:8472954 !$#accession JN0531 !'##molecule_type DNA !'##residues 1-723 ##label CRI !'##cross-references GB:M93058; NID:g153396; PIDN:AAA72111.1; !1PID:g388263 GENETICS !$#gene pabAB CLASSIFICATION #superfamily yeast p-aminobenzoate synthase; trpG homology KEYWORDS carbon-carbon lyase; multifunctional enzyme; oxo-acid-lyase; !1p-aminobenzoate biosynthesis; transferase FEATURE !$3-186 #domain trpG homology #label TRG\ !$82 #active_site Cys #status predicted SUMMARY #length 723 #molecular-weight 77900 #checksum 4972 SEQUENCE /// ENTRY NNSE2 #type complete TITLE anthranilate synthase (EC 4.1.3.27) component II - Serratia marcescens ALTERNATE_NAMES glutamine amidotransferase ORGANISM #formal_name Serratia marcescens DATE 30-Nov-1980 #sequence_revision 29-Jun-1981 #text_change 18-Jun-1999 ACCESSIONS D92860; A92268; B94643; A01121 REFERENCE A92860 !$#authors Nichols, B.P.; Miozzari, G.F.; van Cleemput, M.; Bennett, !1G.N.; Yanofsky, C. !$#journal J. Mol. Biol. (1980) 142:503-517 !$#title Nucleotide sequences of the trpG regions of Escherichia !1coli, Shigella dysenteriae, Salmonella typhimurium and !1Serratia marcescens. !$#cross-references MUID:81119810; PMID:7007652 !$#accession D92860 !'##molecule_type DNA !'##residues 1-192 ##label NIC !'##cross-references GB:J01792; NID:g152876; PIDN:AAA57309.1; !1PID:g152878 !'##note initiator Met not shown REFERENCE A92268 !$#authors Tso, J.Y.; Hermodson, M.A.; Zalkin, H. !$#journal J. Biol. Chem. (1980) 255:1451-1457 !$#title Primary structure of Serratia marcescens anthranilate !1synthase component II. !$#cross-references MUID:80115658; PMID:6986371 !$#accession A92268 !'##molecule_type protein !'##residues 1-34,'A',36,'Q',38-40,'X',42-43,'E',45-46,'T',48-75,'R', !177-148,'F',150-192 ##label TSO REFERENCE A94643 !$#authors Li, S.L.; Hanlon, J.; Yanofsky, C. !$#journal Biochemistry (1974) 13:1736-1744 !$#title Separation of anthranilate synthetase components I and II of !1Escherichia coli, Salmonella typhimurium, and Serratia !1marcescens and determination of their amino-terminal !1sequences by automatic Edman degradation. !$#cross-references MUID:74173403; PMID:4598537 !$#accession B94643 !'##molecule_type protein !'##residues 1-36,'Q',38-44,'Q',46,'X',48-58,'A',60,'V' ##label LIS COMMENT Anthranilate synthase catalyzes the first step of tryptophan !1synthesis in microorganisms, the biosynthesis of !1anthranilate from chorismate and glutamine. The two !1components have different catalytic activities: component I !1catalyzes the formation of anthranilate using ammonia rather !1than glutamine, whereas component II provides the glutamine !1amidotransferase activity. The active enzyme is a tetramer !1containing two chains each of components I and II. GENETICS !$#gene trpG CLASSIFICATION #superfamily glutamine amidotransferase; trpG homology KEYWORDS carbon-carbon lyase; oxo-acid-lyase; transferase; tryptophan !1biosynthesis FEATURE !$3-186 #domain trpG homology #label TRG\ !$83 #active_site Cys #status experimental SUMMARY #length 192 #molecular-weight 20737 #checksum 1893 SEQUENCE /// ENTRY I40053 #type complete TITLE anthranilate synthase (EC 4.1.3.27) component II - Buchnera aphidicola ALTERNATE_NAMES glutamine amidotransferase ORGANISM #formal_name Buchnera aphidicola DATE 09-Mar-1996 #sequence_revision 12-Apr-1996 #text_change 18-Jun-1999 ACCESSIONS I40053; S44088 REFERENCE A55261 !$#authors Lai, C.Y.; Baumann, L.; Baumann, P. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1994) 91:3819-3823 !$#title Amplification of trpEG: adaptation of Buchnera aphidicola to !1an endosymbiotic association with aphids. !$#cross-references MUID:94224833; PMID:8170994 !$#accession I40053 !'##status preliminary !'##molecule_type DNA !'##residues 1-196 ##label RES !'##cross-references EMBL:Z21938; NID:g472880; PIDN:CAA79932.1; !1PID:g472882 GENETICS !$#gene trpG COMPLEX tetramer containing two chains each of components I and II FUNCTION !$#description anthranilate synthase catalyzes the first step of tryptophan !1synthesis in microorganisms, the biosynthesis of !1anthranilate from chorismate and glutamine; two components !1have different catalytic activities: component I catalyzes !1the formation of anthranilate using ammonia rather than !1glutamine, whereas component II provides the glutamine !1amidotransferase activity !$#pathway tryptophan biosynthesis CLASSIFICATION #superfamily glutamine amidotransferase; trpG homology KEYWORDS carbon-carbon lyase; oxo-acid-lyase; transferase; tryptophan !1biosynthesis FEATURE !$4-187 #domain trpG homology #label TRG\ !$84 #active_site Cys #status experimental SUMMARY #length 196 #molecular-weight 21866 #checksum 1904 SEQUENCE /// ENTRY NNPS2P #type complete TITLE anthranilate synthase (EC 4.1.3.27) component II [validated] - Pseudomonas putida ALTERNATE_NAMES anthranilate synthase beta chain; glutamine amidotransferase ORGANISM #formal_name Pseudomonas putida DATE 30-Nov-1980 #sequence_revision 30-Nov-1980 #text_change 17-Mar-2000 ACCESSIONS A01122; B35115 REFERENCE A01122 !$#authors Kawamura, M.; Keim, P.S.; Goto, Y.; Zalkin, H.; Heinrikson, !1R.L. !$#journal J. Biol. Chem. (1978) 253:4659-4668 !$#title Anthranilate synthetase component II from Pseudomonas !1putida. Covalent structure and identification of the !1cysteine residue involved in catalysis. !$#cross-references MUID:78194198; PMID:659439 !$#accession A01122 !'##molecule_type protein !'##residues 1-197 ##label KAW REFERENCE A35115 !$#authors Essar, D.W.; Eberly, L.; Crawford, I.P. !$#journal J. Bacteriol. (1990) 172:867-883 !$#title Evolutionary differences in chromosomal locations of four !1early genes of the tryptophan pathway in fluorescent !1pseudomonads: DNA sequences and characterization of !1Pseudomonas putida trpE and trpGDC. !$#cross-references MUID:90130325; PMID:2404959 !$#accession B35115 !'##molecule_type DNA !'##residues 1-4,'M',5-197 ##label ESS !'##cross-references GB:M33799; NID:g151627; PIDN:AAA80553.1; !1PID:g151631; GB:M33800; GB:M33801 GENETICS !$#gene trpG COMPLEX heterotetramer; two component I chains, two component II !1chains FUNCTION ANT !$#description EC 4.1.3.27 [validated, MUID:90130325] FUNCTION COM2 !$#description component II of the anthranilate synthase provides the !1glutamine amidotransferase activity CLASSIFICATION #superfamily glutamine amidotransferase; trpG homology KEYWORDS carbon-carbon lyase; oxo-acid-lyase; transferase; tryptophan !1biosynthesis FEATURE !$1-197 #product anthranilate synthase component II #status !8experimental #label MAT\ !$2-190 #domain trpG homology #label TRG\ !$79 #active_site Cys #status experimental SUMMARY #length 197 #molecular-weight 21693 #checksum 5844 SEQUENCE /// ENTRY NNKE2C #type complete TITLE anthranilate synthase (EC 4.1.3.27) component II - Acinetobacter calcoaceticus ALTERNATE_NAMES glutamine amidotransferase (EC 2.6.1.-) ORGANISM #formal_name Acinetobacter calcoaceticus DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 24-Sep-1999 ACCESSIONS A01123 REFERENCE A93052 !$#authors Kaplan, J.B.; Goncharoff, P.; Seibold, A.M.; Nichols, B.P. !$#journal Mol. Biol. Evol. (1984) 1:456-472 !$#title Nucleotide sequence of the Acinetobacter calcoaceticus !1trpGDC gene cluster. !$#cross-references MUID:88174326; PMID:6599977 !$#accession A01123 !'##molecule_type DNA !'##residues 1-194 ##label KAP !'##cross-references GB:M36636; NID:g141799; PIDN:AAA21903.1; !1PID:g141800 COMMENT Anthranilate synthase catalyzes the biosynthesis of !1anthranilate from chorismate and glutamine. It contains two !1chains with different catalytic activities: component I !1catalyzes the formation of anthranilate using ammonia rather !1than glutamine, whereas component II provides the glutamine !1amidotransferase activity. In E. coli and certain other !1bacteria, component II is larger and its carboxyl-terminal !1two-thirds has anthranilate phosphoribosyltransferase (EC !12.4.2.18) activity. GENETICS !$#gene trpG CLASSIFICATION #superfamily glutamine amidotransferase; trpG homology KEYWORDS aminotransferase; carbon-carbon lyase; oxo-acid-lyase; !1tryptophan biosynthesis FEATURE !$2-190 #domain trpG homology #label TRG\ !$79 #active_site Cys #status predicted SUMMARY #length 194 #molecular-weight 21794 #checksum 1355 SEQUENCE /// ENTRY AGEC2 #type complete TITLE p-aminobenzoate synthase (EC 4.1.3.-) component II - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 20-Sep-1984 #sequence_revision 20-Sep-1984 #text_change 01-Mar-2002 ACCESSIONS A01124; B33867; C65130 REFERENCE A01124 !$#authors Kaplan, J.B.; Nichols, B.P. !$#journal J. Mol. Biol. (1983) 168:451-468 !$#title Nucleotide sequence of Escherichia coli pabA and its !1evolutionary relationship to trp(G)D. !$#cross-references MUID:83294525; PMID:6350604 !$#accession A01124 !'##molecule_type DNA !'##residues 1-187 ##label KAP !'##cross-references GB:K00030; NID:g147049; PIDN:AAA24260.1; !1PID:g147050 REFERENCE A33867 !$#authors Kawamukai, M.; Matsuda, H.; Fujii, W.; Utsumi, R.; Komano, !1T. !$#journal J. Bacteriol. (1989) 171:4525-4529 !$#title Nucleotide sequences of fic and fic-1 genes involved in cell !1filamentation induced by cyclic AMP in Escherichia coli. !$#cross-references MUID:89327179; PMID:2546924 !$#accession B33867 !'##status preliminary !'##molecule_type DNA !'##residues 1-150 ##label KAW !'##cross-references GB:M28363; NID:g145952; PIDN:AAA23774.1; !1PID:g551804 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65130 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-187 ##label BLAT !'##cross-references GB:AE000412; GB:U00096; NID:g1789758; !1PIDN:AAC76385.1; PID:g1789760; UWGP:b3360 !'##experimental_source strain K-12, substrain MG1655 COMMENT p-Aminobenzoate synthase catalyzes a reaction, the formation !1of p-aminobenzoate, in the dihydrofolate pathway. The active !1E. coli enzyme contains two chains with different catalytic !1activities: component I catalyzes the aromatization of !1chorismate using glutamine, whereas component II provides !1the glutamine amidotransferase activity. GENETICS !$#gene pabA !$#map_position 74 min CLASSIFICATION #superfamily glutamine amidotransferase; trpG homology KEYWORDS carbon-carbon lyase; oxo-acid-lyase; transferase; tryptophan !1biosynthesis FEATURE !$2-185 #domain trpG homology #label TRG\ !$79 #active_site Cys #status predicted SUMMARY #length 187 #molecular-weight 20772 #checksum 6616 SEQUENCE /// ENTRY C32840 #type complete TITLE anthranilate synthase (EC 4.1.3.27) component II - Leptospira biflexa ORGANISM #formal_name Leptospira biflexa DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C32840 REFERENCE A32840 !$#authors Yelton, D.B.; Peng, S.L. !$#journal J. Bacteriol. (1989) 171:2083-2089 !$#title Identification and nucleotide sequence of the Leptospira !1biflexa serovar patoc trpE and trpG genes. !$#cross-references MUID:89197778; PMID:2703466 !$#accession C32840 !'##status preliminary !'##molecule_type DNA !'##residues 1-201 ##label YEL !'##cross-references GB:M22468; NID:g149627; PIDN:AAA88217.1; !1PID:g149629 !'##note the authors translated the codon AAT for residue 107 as Asp CLASSIFICATION #superfamily glutamine amidotransferase; trpG homology KEYWORDS carbon-carbon lyase; oxo-acid-lyase FEATURE !$3-199 #domain trpG homology #label TRG\ !$89 #active_site Cys #status predicted SUMMARY #length 201 #molecular-weight 22157 #checksum 7799 SEQUENCE /// ENTRY NNEC2 #type complete TITLE anthranilate synthase (EC 4.1.3.27) component II - Escherichia coli (strain K-12) CONTAINS anthranilate phosphoribosyltransferase (EC 2.4.2.18); glutamine amidotransferase ORGANISM #formal_name Escherichia coli DATE 30-Nov-1980 #sequence_revision 21-Nov-1997 #text_change 01-Mar-2002 ACCESSIONS B64874; A93746; A93168; I56374; A01125 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64874 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-531 ##label BLAT !'##cross-references GB:AE000224; GB:U00096; NID:g1787509; !1PIDN:AAC74345.1; PID:g1787517; UWGP:b1263 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A93746 !$#authors Yanofsky, C.; Platt, T.; Crawford, I.P.; Nichols, B.P.; !1Christie, G.E.; Horowitz, H.; van Cleemput, M.; Wu, A.M. !$#journal Nucleic Acids Res. (1981) 9:6647-6668 !$#title The complete nucleotide sequence of the tryptophan operon of !1Escherichia coli. !$#cross-references MUID:82150258; PMID:7038627 !$#accession A93746 !'##molecule_type DNA !'##residues 1-191,'H',193-531 ##label YAN !'##cross-references GB:J01714; GB:M12471; GB:M12472; GB:M24865; !1GB:M25264; GB:M25593; GB:M59208; NID:g147953; !1PIDN:AAA57298.1; PID:g147956 REFERENCE A93168 !$#authors Li, S.L.; Hanlon, J.; Yanofsky, C. !$#journal Nature (1974) 248:48-50 !$#title Structural homology of the glutamine amidotransferase !1subunits of the anthranilate synthetases of Escherichia !1coli, Salmonella typhimurium and Serratia marcescens. !$#cross-references MUID:74130093; PMID:4594441 !$#accession A93168 !'##molecule_type protein !'##residues 1-60,'A' ##label LIS REFERENCE I56374 !$#authors Horowitz, H.; Christie, G.E.; Platt, T. !$#journal J. Mol. Biol. (1982) 156:245-256 !$#title Nucleotide sequence of the trpD gene, encoding anthranilate !1synthetase component II of Escherichia coli. !$#cross-references MUID:82216842; PMID:6283099 !$#accession I56374 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-191,'H',193-531 ##label RES !'##cross-references EMBL:V00367; NID:g43193; PIDN:CAA23665.1; !1PID:g43194 GENETICS !$#gene trpG-trpD !$#map_position 28 min COMPLEX heterotetramer; two components I and two components II FUNCTION COM !$#description anthranilate synthase catalyzes biosynthesis of anthranilate !1from chorismate and glutamine !$#pathway tryptophan biosynthesis !$#note component II is larger and its carboxyl-terminal two-thirds !1has anthranilate phosphoribosyltransferase (EC 2.4.2.18) !1activity FUNCTION COI !$#description component I catalyzes the formation of anthranilate using !1ammonia rather than glutamine FUNCTION COII !$#description component II provides the glutamine amidotransferase !1activity CLASSIFICATION #superfamily trpG-trpD bifunctional enzyme; trpD homology; !1trpG homology KEYWORDS carbon-carbon lyase; glycosyltransferase; oxo-acid-lyase; !1pentosyltransferase; tryptophan biosynthesis FEATURE !$4-187 #domain trpG homology #label TRG\ !$203-530 #domain trpD homology #label TRD\ !$84 #active_site Cys #status predicted SUMMARY #length 531 #molecular-weight 56869 #checksum 6704 SEQUENCE /// ENTRY NNEB2T #type complete TITLE anthranilate synthase (EC 4.1.3.27) component II - Salmonella typhimurium CONTAINS anthranilate phosphoribosyltransferase (EC 2.4.2.18); glutamine amidotransferase ORGANISM #formal_name Salmonella typhimurium DATE 31-Dec-1980 #sequence_revision 18-Apr-1984 #text_change 19-Apr-2002 ACCESSIONS A92907; A92860; A01126 REFERENCE A92907 !$#authors Horowitz, H.; Van Arsdell, J.; Platt, T. !$#journal J. Mol. Biol. (1983) 169:775-797 !$#title Nucleotide sequence of the trpD and trpC genes of Salmonella !1typhimurium. !$#cross-references MUID:84036180; PMID:6355484 !$#accession A92907 !'##molecule_type DNA !'##residues 1-530 ##label HOR REFERENCE A92860 !$#authors Nichols, B.P.; Miozzari, G.F.; van Cleemput, M.; Bennett, !1G.N.; Yanofsky, C. !$#journal J. Mol. Biol. (1980) 142:503-517 !$#title Nucleotide sequences of the trpG regions of Escherichia !1coli, Shigella dysenteriae, Salmonella typhimurium and !1Serratia marcescens. !$#cross-references MUID:81119810; PMID:7007652 !$#accession A92860 !'##molecule_type DNA !'##residues 1-200 ##label NIC COMMENT The initiator Met is not shown. GENETICS !$#gene trpG-trpD FUNCTION !$#description anthranilate synthase catalyzes biosynthesis of anthranilate !1from chorismate and glutamine !$#pathway tryptophan biosynthesis !$#note component II is larger and its carboxyl-terminal two-thirds !1has anthranilate phosphoribosyltransferase (EC 2.4.2.18) !1activity FUNCTION COI !$#description component I catalyzes the formation of anthranilate using !1ammonia rather than glutamine FUNCTION COII !$#description component II provides the glutamine amidotransferase !1activity CLASSIFICATION #superfamily trpG-trpD bifunctional enzyme; trpD homology; !1trpG homology KEYWORDS carbon-carbon lyase; glycosyltransferase; oxo-acid-lyase; !1pentosyltransferase; tryptophan biosynthesis FEATURE !$3-186 #domain trpG homology #label TRG\ !$202-529 #domain trpD homology #label TRD\ !$83 #active_site Cys #status predicted SUMMARY #length 530 #molecular-weight 56786 #checksum 6464 SEQUENCE /// ENTRY NNEB2D #type fragment TITLE anthranilate synthase (EC 4.1.3.27) component II - Shigella dysenteriae (fragment) CONTAINS anthranilate phosphoribosyltransferase (EC 2.4.2.18); glutamine amidotransferase ORGANISM #formal_name Shigella dysenteriae DATE 31-Dec-1980 #sequence_revision 31-Dec-1980 #text_change 02-Jun-2000 ACCESSIONS B92860; A01127 REFERENCE A92860 !$#authors Nichols, B.P.; Miozzari, G.F.; van Cleemput, M.; Bennett, !1G.N.; Yanofsky, C. !$#journal J. Mol. Biol. (1980) 142:503-517 !$#title Nucleotide sequences of the trpG regions of Escherichia !1coli, Shigella dysenteriae, Salmonella typhimurium and !1Serratia marcescens. !$#cross-references MUID:81119810; PMID:7007652 !$#accession B92860 !'##molecule_type DNA !'##residues 1-200 ##label NIC !'##cross-references GB:J01787; NID:g152796; PIDN:AAA57307.1; !1PID:g152798 !'##note initiator Met not shown GENETICS !$#gene trpG-trpD FUNCTION COM !$#description anthranilate synthase catalyzes biosynthesis of anthranilate !1from chorismate and glutamine !$#pathway tryptophan biosynthesis !$#note component II is larger and its carboxyl-terminal two-thirds !1has anthranilate phosphoribosyltransferase (EC 2.4.2.18) !1activity FUNCTION COI !$#description component I catalyzes the formation of anthranilate using !1ammonia rather than glutamine FUNCTION COII !$#description component II provides the glutamine amidotransferase !1activity CLASSIFICATION #superfamily trpG-trpD bifunctional enzyme; trpD homology; !1trpG homology KEYWORDS carbon-carbon lyase; glycosyltransferase; oxo-acid-lyase; !1pentosyltransferase; tryptophan biosynthesis FEATURE !$3-186 #domain trpG homology #label TRG\ !$83 #active_site Cys #status predicted SUMMARY #length 200 #checksum 7931 SEQUENCE /// ENTRY SYRTCA #type complete TITLE carbamoyl-phosphate synthase (ammonia) (EC 6.3.4.16) I precursor - rat ALTERNATE_NAMES carbamyl phosphate synthetase I; carbon-dioxide-ammonia ligase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 31-Dec-2000 ACCESSIONS A28481; A23580 REFERENCE A28481 !$#authors Lagace, M.; Howell, B.W.; Burak, R.; Lusty, C.J.; Shore, !1G.C. !$#journal J. Biol. Chem. (1987) 262:10415-10418 !$#title Rat carbamyl-phosphate synthetase I gene. Promoter sequence !1and tissue-specific transcriptional regulation in vitro. !$#cross-references MUID:87280088; PMID:3038878 !$#accession A28481 !'##molecule_type DNA !'##residues 1-42 ##label LAG !'##cross-references GB:J02805; NID:g203577; PIDN:AAA40959.1; !1PID:g203578 REFERENCE A23580 !$#authors Nyunoya, H.; Broglie, K.E.; Widgren, E.E.; Lusty, C.J. !$#journal J. Biol. Chem. (1985) 260:9346-9356 !$#title Characterization and derivation of the gene coding for !1mitochondrial carbamyl phosphate synthetase I of rat. !$#cross-references MUID:85261323; PMID:2991241 !$#accession A23580 !'##molecule_type mRNA !'##residues 1-1500 ##label NYU !'##cross-references GB:M11710 REFERENCE A42051 !$#authors Potter, M.D.; Powers-Lee, S.G. !$#journal J. Biol. Chem. (1992) 267:2023-2031 !$#title Location of the ATP-gamma-phosphate-binding sites on rat !1liver carbamoyl-phosphate synthetase I. Studies with the ATP !1analog 5'-p-fluorosulfonylbenzoyl adenosine. !$#cross-references MUID:92112936; PMID:1730733 !$#contents annotation; MgATP binding sites COMMENT This enzyme, which requires N-acetylglutamate as allosteric !1activator, catalyzes the synthesis of carbamoyl phosphate !1from ammonia, carbonate, and ATP. COMMENT This enzyme of the mitochondrial matrix is expressed !1specifically in hepatocytes and and in epithelial cells of !1intestinal mucosa. COMMENT This enzyme binds two molecules of ATP at discrete sites for !1use in discrete steps. CLASSIFICATION #superfamily carbamoyl-phosphate synthase (ammonia); biotin !1carboxylase homology; carbamoyl-phosphate synthase (ammonia) !1homology; carbamoyl-phosphate synthase !1(glutamine-hydrolyzing) large chain homology; !1carbamoyl-phosphate synthase (glutamine-hydrolyzing) small !1chain homology; trpG homology KEYWORDS ATP; duplication; ligase; mitochondrion; urea cycle FEATURE !$1-38 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$39-1500 #product carbamoyl-phosphate synthase (ammonia) !8#status predicted #label MAT\ !$48-1479 #domain carbamoyl-phosphate synthase (ammonia) !8homology #label CPA\ !$48-395 #domain carbamoyl-phosphate synthase !8(glutamine-hydrolyzing) small chain homology #label !8CPS\ !$220-395 #domain trpG homology #label TRG\ !$424-1476 #domain carbamoyl-phosphate synthase !8(glutamine-hydrolyzing) large chain homology #label !8CPL\ !$424-886 #domain biotin carboxylase homology #label BC1\ !$631-638,1327-1348 #region ATP binding (for bicarbonate activation) !8#status experimental\ !$975-1426 #domain biotin carboxylase homology #label BC2\ !$1310-1317,1445-1454 #region ATP binding (for carbamate activation) !8#status experimental SUMMARY #length 1500 #molecular-weight 164579 #checksum 8372 SEQUENCE /// ENTRY JQ1348 #type complete TITLE carbamoyl-phosphate synthase (ammonia) (EC 6.3.4.16) precursor - human ALTERNATE_NAMES carbamyl phosphate synthetase I; carbon-dioxide-ammonia ligase ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1992 #sequence_revision 02-Jun-1994 #text_change 16-Jun-2000 ACCESSIONS JQ1348 REFERENCE JQ1348 !$#authors Haraguchi, Y.; Uchino, T.; Takiguchi, M.; Endo, F.; Mori, !1M.; Matsuda, I. !$#journal Gene (1991) 107:335-340 !$#title Cloning and sequence of a cDNA encoding human carbamyl !1phosphate synthetase I: molecular analysis of !1hyperammonemia. !$#cross-references MUID:92084128; PMID:1840546 !$#accession JQ1348 !'##molecule_type mRNA !'##residues 1-1500 ##label HAR !'##cross-references DDBJ:D90282; NID:g219552; PIDN:BAA14328.1; !1PID:g219553 COMMENT This is the first enzyme of the urea cycle; it catalyzes the !1synthesis of carbamyl phosphate from bicarbonate, ATP, and !1ammonia. GENETICS !$#gene GDB:CPS1 !'##cross-references GDB:119799; OMIM:237300 !$#map_position 2q33-2q36 CLASSIFICATION #superfamily carbamoyl-phosphate synthase (ammonia); biotin !1carboxylase homology; carbamoyl-phosphate synthase (ammonia) !1homology; carbamoyl-phosphate synthase !1(glutamine-hydrolyzing) large chain homology; !1carbamoyl-phosphate synthase (glutamine-hydrolyzing) small !1chain homology; trpG homology KEYWORDS ATP; ligase; urea cycle FEATURE !$1-38 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$39-1500 #product carbamoyl-phosphate synthase (ammonia) !8#status predicted #label CAR\ !$48-1479 #domain carbamoyl-phosphate synthase (ammonia) !8homology #label CPA\ !$48-395 #domain carbamoyl-phosphate synthase !8(glutamine-hydrolyzing) small chain homology #label !8CPS\ !$220-395 #domain trpG homology #label TRG\ !$424-1476 #domain carbamoyl-phosphate synthase !8(glutamine-hydrolyzing) large chain homology #label !8CPL\ !$424-886 #domain biotin carboxylase homology #label BC1\ !$975-1426 #domain biotin carboxylase homology #label BC2 SUMMARY #length 1500 #molecular-weight 164829 #checksum 523 SEQUENCE /// ENTRY A64472 #type complete TITLE carbamoyl-phosphate synthase, large chain (EC 6.3.-.-) - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A64472 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession A64472 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-487 ##label BUL !'##cross-references GB:U67577; GB:L77117; NID:g1592013; PID:g1592023; !1TIGR:MJ1378; PID:g1511394 GENETICS !$#map_position FOR1326866-1328329 !$#start_codon TTG CLASSIFICATION #superfamily carbamoyl-phosphate synthase large chain; !1biotin carboxylase homology KEYWORDS ligase FEATURE !$11-470 #domain biotin carboxylase homology #label BCH SUMMARY #length 487 #molecular-weight 54338 #checksum 1900 SEQUENCE /// ENTRY QZFF #type complete TITLE rudimentary protein - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES CAD protein CONTAINS aspartate carbamoyltransferase (EC 2.1.3.2); carbamoyl-phosphate synthase (glutamine-hydrolyzing) (EC 6.3.5.5); dihydroorotase (EC 3.5.2.3) ORGANISM #formal_name Drosophila melanogaster DATE 31-Mar-1989 #sequence_revision 23-Feb-1996 #text_change 18-Jun-1999 ACCESSIONS A29106; S53752; S35447; S35446 REFERENCE A29106 !$#authors Freund, J.N.; Jarry, B.P. !$#journal J. Mol. Biol. (1987) 193:1-13 !$#title The rudimentary gene of Drosophila melanogaster encodes four !1enzymic functions. !$#cross-references MUID:87226179; PMID:2884325 !$#accession A29106 !'##molecule_type mRNA !'##residues 1-2074,'WRLEERTDRALAGPPADPVQCEPAVMWRRD',2105-2130, !1'ECAARHGCALHDSHS',2146-2236 ##label FRE !'##cross-references GB:X04813; NID:g8508; PIDN:CAA28502.1; PID:g8509 !'##note this sequence has been revised in reference S53752 REFERENCE S53752 !$#authors Davidson, J.N.; Kern, C.B. !$#journal J. Mol. Biol. (1994) 243:364-366 !$#title Revision in sequence of CAD aspartate transcarbamylase !1domain of Drosophila. !$#cross-references MUID:95018278; PMID:7932764 !$#accession S53752 !'##molecule_type mRNA !'##residues 2068-2148 ##label DAV !'##cross-references GB:S74010; NID:g693827; PIDN:AAB32204.1; !1PID:g693828 !'##note this is a revision to the sequence from reference A29106 REFERENCE S35447 !$#authors Zerges, B.; Udvardy, A.; Schedl, P. !$#submission submitted to the EMBL Data Library, August 1990 !$#accession S35447 !'##molecule_type DNA !'##residues 1-132 ##label ZER1 !'##cross-references EMBL:M37783; NID:g158367; PIDN:AAA28873.1; !1PID:g158368 REFERENCE S35446 !$#authors Zerges, W.; Udvardy, A.; Schedl, P. !$#journal Nucleic Acids Res. (1992) 20:4639-4647 !$#title Molecular characterization of the 5' end of the rudimentary !1gene in Drosophila and analysis of three P element !1insertions. !$#cross-references MUID:93027163; PMID:1329025 !$#accession S35446 !'##molecule_type DNA !'##residues 1-109 ##label ZER2 !'##cross-references EMBL:M37783 GENETICS !$#gene FlyBase:r !'##cross-references FlyBase:FBgn0003189 CLASSIFICATION #superfamily rudimentary enzyme; aspartate/ornithine !1carbamoyltransferase homology; Bacillus dihydroorotase !1homology; biotin carboxylase homology; carbamoyl-phosphate !1synthase (ammonia) homology; carbamoyl-phosphate synthase !1(glutamine-hydrolyzing) large chain homology; !1carbamoyl-phosphate synthase (glutamine-hydrolyzing) small !1chain homology; trpG homology KEYWORDS hydrolase; ligase; multifunctional enzyme; pyrimidine !1nucleotide biosynthesis; transferase FEATURE !$8-1460 #domain carbamoyl-phosphate synthase (ammonia) !8homology #label CPA\ !$8-380 #domain carbamoyl-phosphate synthase !8(glutamine-hydrolyzing) small chain homology #label !8CPS\ !$201-376 #domain trpG homology #label TRG\ !$408-865 #domain biotin carboxylase homology #label BC1\ !$410-1457 #domain carbamoyl-phosphate synthase !8(glutamine-hydrolyzing) large chain homology #label !8CPL\ !$953-1396 #domain biotin carboxylase homology #label BC2\ !$1475-1818 #domain Bacillus dihydroorotase homology #label DHO\ !$1923-2219 #domain aspartate/ornithine carbamoyltransferase !8homology #label ACT\ !$274 #active_site Cys #status predicted SUMMARY #length 2236 #molecular-weight 249238 #checksum 8341 SEQUENCE /// ENTRY A23443 #type complete TITLE pyrimidine synthesis multifunctional protein CAD - golden hamster CONTAINS aspartate carbamoyltransferase (EC 2.1.3.2); carbamoyl-phosphate synthase (glutamine-hydrolyzing) (EC 6.3.5.5) large chain; dihydroorotase (EC 3.5.2.3) ORGANISM #formal_name Mesocricetus auratus #common_name golden hamster DATE 29-Aug-1987 #sequence_revision 02-Jun-1994 #text_change 18-Jun-1999 ACCESSIONS A38653; A35432; PS0159; A23443; A30794; A34803; I48154 REFERENCE A38653 !$#authors Bein, K.; Simmer, J.P.; Evans, D.R. !$#journal J. Biol. Chem. (1991) 266:3791-3799 !$#title Molecular cloning of a cDNA encoding the amino end of the !1mammalian multifunctional protein CAD and analysis of the !15'-flanking region of the CAD gene. !$#cross-references MUID:91139675; PMID:1671675 !$#accession A38653 !'##molecule_type mRNA !'##residues 1-169 ##label BEI !'##cross-references GB:M60078; NID:g191338; PIDN:AAA63617.1; !1PID:g191339 REFERENCE A35432 !$#authors Simmer, J.P.; Kelly, R.E.; Rinker Jr., A.G.; Scully, J.L.; !1Evans, D.R. !$#journal J. Biol. Chem. (1990) 265:10395-10402 !$#title Mammalian carbamyl phosphate synthetase (CPS). cDNA sequence !1and evolution of the CPS domain of the Syrian hamster !1multifunctional protein CAD. !$#cross-references MUID:90285162; PMID:1972379 !$#accession A35432 !'##molecule_type mRNA !'##residues 156-1455 ##label SIM !'##cross-references GB:J05503; NID:g191332; PIDN:AAA37062.1; !1PID:g191333 REFERENCE PS0159 !$#authors Williams, N.K.; Simpson, R.J.; Moritz, R.L.; Peide, Y.; !1Crofts, L.; Minasian, E.; Leach, S.J.; Wake, R.G.; !1Christopherson, R.I. !$#journal Gene (1990) 94:283-288 !$#title Location of the dihydroorotase domain within trifunctional !1hamster dihydroorotate synthetase. !$#cross-references MUID:91078651; PMID:1979549 !$#accession PS0159 !'##molecule_type mRNA !'##residues 1403-2110 ##label WIL !'##cross-references GB:M33702; NID:g191172; PIDN:AAA37009.1; !1PID:g191173 REFERENCE A23443 !$#authors Shigesada, K.; Stark, G.R.; Maley, J.A.; Niswander, L.A.; !1Davidson, J.N. !$#journal Mol. Cell. Biol. (1985) 5:1735-1742 !$#title Construction of a cDNA to the hamster CAD gene and its !1application toward defining the domain for aspartate !1transcarbamylase. !$#cross-references MUID:85267690; PMID:2862577 !$#accession A23443 !'##molecule_type mRNA !'##residues 2074-2225 ##label SHI !'##cross-references GB:M11242; NID:g191330; PIDN:AAA37061.1; !1PID:g387067 REFERENCE A30794 !$#authors Maley, J.A.; Davidson, J.N. !$#journal Biochem. Biophys. Res. Commun. (1988) 154:1047-1053 !$#title Identification of the junction between the glutamine !1amidotransferase and carbamyl phosphate synthetase domains !1of the mammalian CAD protein. !$#cross-references MUID:88309082; PMID:2900634 !$#accession A30794 !'##molecule_type mRNA !'##residues 246-464 ##label MAL !'##cross-references GB:M21927 REFERENCE A34803 !$#authors Simmer, J.P.; Kelly, R.E.; Rinker Jr., A.G.; Zimmermann, !1B.H.; Scully, J.L.; Kim, H.; Evans, D.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:174-178 !$#title Mammalian dihydroorotase: nucleotide sequence, peptide !1sequences, and evolution of the dihydroorotase domain of the !1multifunctional protein CAD. !$#cross-references MUID:90115834; PMID:1967494 !$#accession A34803 !'##molecule_type mRNA !'##residues 1391-1870 ##label SI2 !'##cross-references GB:M28866; NID:g191363; PIDN:AAA37073.1; !1PID:g191364 !'##note parts of this sequence were confirmed by peptide sequencing REFERENCE I48154 !$#authors Farnham, P.J.; Kollmar, R. !$#journal Cell Growth Differ. (1990) 1:179-189 !$#title Characterization of the 5' end of the growth-regulated !1Syrian hamster CAD gene. !$#cross-references MUID:91190717; PMID:1982061 !$#accession I48154 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-73 ##label RES !'##cross-references GB:M31621; NID:g191326; PIDN:AAA37060.1; !1PID:g553847 GENETICS !$#gene CAD !$#map_position B9 short arm !$#introns 28/1 CLASSIFICATION #superfamily rudimentary enzyme; aspartate/ornithine !1carbamoyltransferase homology; Bacillus dihydroorotase !1homology; biotin carboxylase homology; carbamoyl-phosphate !1synthase (ammonia) homology; carbamoyl-phosphate synthase !1(glutamine-hydrolyzing) large chain homology; !1carbamoyl-phosphate synthase (glutamine-hydrolyzing) small !1chain homology; trpG homology KEYWORDS hydrolase; ligase; methyltransferase; multifunctional !1enzyme; phosphoprotein; pyrimidine nucleotide biosynthesis; !1zinc FEATURE !$4-1442 #domain carbamoyl-phosphate synthase (ammonia) !8homology #label CPA\ !$4-354 #domain carbamoyl-phosphate synthase !8(glutamine-hydrolyzing) small chain homology #label !8CPS\ !$178-354 #domain trpG homology #label TRG\ !$395-1439 #domain carbamoyl-phosphate synthase !8(glutamine-hydrolyzing) large chain homology #label !8CPL\ !$395-845 #domain biotin carboxylase homology #label BC1\ !$934-1380 #domain biotin carboxylase homology #label BC2\ !$1457-1801 #domain Bacillus dihydroorotase homology #label DHO\ !$1924-2222 #domain aspartate/ornithine carbamoyltransferase !8homology #label ACT\ !$252 #active_site Cys #status predicted SUMMARY #length 2225 #molecular-weight 243126 #checksum 6376 SEQUENCE /// ENTRY QZBYU2 #type complete TITLE pyrimidine synthesis protein URA2 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein J0686; protein YJL130c CONTAINS aspartate carbamoyltransferase (EC 2.1.3.2); carbamoyl-phosphate synthase (glutamine-hydrolyzing) (EC 6.3.5.5) ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1991 #sequence_revision 08-Sep-1995 #text_change 12-Nov-1999 ACCESSIONS S56911; S56912; S05767; S05859; S55182; S13358; S71667; !1S22790; A33820; JQ0014 REFERENCE S56891 !$#authors Cziepluch, C.; Kordes, E.; Pujol, A.; Jauniaux, J.C. !$#submission submitted to the Protein Sequence Database, September 1995 !$#accession S56911 !'##molecule_type DNA !'##residues 1-276 ##label CZI !'##cross-references EMBL:Z49405; GSPDB:GN00010; MIPS:YJL130c REFERENCE S56912 !$#authors Katsoulou, C.; Tzermia, M.; Alexandraki, D. !$#submission submitted to the Protein Sequence Database, September 1995 !$#accession S56912 !'##molecule_type DNA !'##residues 175-2214 ##label KAT !'##cross-references EMBL:Z49405; GSPDB:GN00010; MIPS:YJL130c REFERENCE S05766 !$#authors Souciet, J.L.; Nagy, M.; le Gouar, M.; Lacroute, F.; Potier, !1S. !$#journal Gene (1989) 79:59-70 !$#title Organization of the yeast URA2 gene: identification of a !1defective dihydroorotase-like domain in the multifunctional !1carbamoylphosphate synthetase-aspartate transcarbamylase !1complex. !$#cross-references MUID:89378778; PMID:2570735 !$#accession S05767 !'##molecule_type DNA !'##residues 1-122,'A',124-249,'RI',250,'SCSMD',258-269,'Y',271-312, !1'VQ',315-371,'RF',374-393,'EIQNSCL',396,403-430,'QGT', !1434-851,'V',853-1410,'S',1413-1581,'M',1583-1587,'K', !11589-1591,'G',1593-1594,'A',1596-2214 ##label SOU1 !'##cross-references EMBL:M27174 REFERENCE S05859 !$#authors Souciet, J.L.; Potier, S.; Hubert, J.C.; Lacroute, F. !$#journal Mol. Gen. Genet. (1987) 207:314-319 !$#title Nucleotide sequence of the pyrimidine specific carbamoyl !1phosphate synthetase, a part of the yeast multifunctional !1protein encoded by the URA2 gene. !$#cross-references MUID:87286375; PMID:3039294 !$#accession S05859 !'##molecule_type DNA !'##residues 1-85,'D',87-122,'A',124-249,'RI',250,'SCSMD',258-269,'Y', !1271-312,'VQ',315-371,'RF',374-393,'EIQNSCL',396,403-430, !1'QGT',434-481,'T',483-484,'N',486-491,'G',493-500,'N',502, !1'AKQRD',505,'D',506 ##label SOU2 !'##cross-references EMBL:X05553; NID:g4760; PIDN:CAA29068.1; PID:g4761 !'##note the authors translated the codon GAC for residue 85 as His REFERENCE S55159 !$#authors Katsoulou, C.; Tzermia, M.; Alexandraki, D. !$#submission submitted to the EMBL Data Library, May 1995 !$#description The complete sequence of a 40.7 kb segment located on the !1left arm of yeast chromosome X identified 13 known genes and !1revealed 13 new open reading frames including homologues to !1other yeast hypothetical proteins. !$#accession S55182 !'##molecule_type DNA !'##residues 175-2214 ##label KA2 !'##cross-references EMBL:X87371; NID:g854542; PIDN:CAA60825.1; !1PID:g854566 REFERENCE S13358 !$#authors Denis-Duphil, M.; Lecaer, J.P.; Hardie, D.G.; Carrey, E.A. !$#journal Eur. J. Biochem. (1990) 193:581-587 !$#title Yeast carbamoyl-phosphate-synthetase - !1aspartate-transcarbamylase multidomain protein is !1phosphorylated in vitro by cAMP-dependent protein kinase. !$#cross-references MUID:91031508; PMID:1977585 !$#accession S13358 !'##molecule_type protein !'##residues 1855-1882 ##label DEN REFERENCE S71643 !$#authors Katsoulou, C.; Tzermia, M.; Tavernarakis, N.; Alexandraki, !1D. !$#journal Yeast (1996) 12:787-797 !$#title Sequence analysis of a 40.7 kb segment from the left arm of !1yeast chromosome X reveals 14 known genes and 13 new open !1reading frames including homologues of genes clustered on !1the right arm of chromosome XI. !$#cross-references MUID:96408771; PMID:8813765 !$#accession S71667 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 175-2214 ##label KAW !'##cross-references EMBL:X87371; NID:g854542; PIDN:CAA60825.1; !1PID:g854566 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1May 1995 REFERENCE A33820 !$#authors Nagy, M.; le Gouar, M.; Potier, S.; Souciet, J.L.; Herve, G. !$#journal J. Biol. Chem. (1989) 264:8366-8374 !$#title The primary structure of the aspartate transcarbamylase !1region of the URA2 gene product in Saccharomyces cerevisiae. !$#cross-references MUID:89255278; PMID:2498313 !$#accession S22790 !'##molecule_type DNA !'##residues 1268-1410,'S',1413-1581,'M',1583-1587,'K',1589-1591,'G', !11593-1594,'A',1596-2214 ##label NAG !'##cross-references EMBL:J04711 GENETICS !$#gene SGD:URA2; MIPS:YJL130c !'##cross-references SGD:S0003666; MIPS:YJL130c !$#map_position 10L FUNCTION !$#description ligase; methyltransferase !$#pathway pyrimidine nucleotide biosynthesis CLASSIFICATION #superfamily rudimentary enzyme; aspartate/ornithine !1carbamoyltransferase homology; Bacillus dihydroorotase !1homology; biotin carboxylase homology; carbamoyl-phosphate !1synthase (ammonia) homology; carbamoyl-phosphate synthase !1(glutamine-hydrolyzing) large chain homology; !1carbamoyl-phosphate synthase (glutamine-hydrolyzing) small !1chain homology; trpG homology KEYWORDS ligase; methyltransferase; multifunctional enzyme; nucleus; !1phosphoprotein; pyrimidine nucleotide biosynthesis FEATURE !$24-1487 #domain carbamoyl-phosphate synthase (ammonia) !8homology #label CPA\ !$24-404 #domain carbamoyl-phosphate synthase !8(glutamine-hydrolyzing) small chain homology #label !8CPS\ !$229-404 #domain trpG homology #label TRG\ !$440-1484 #domain carbamoyl-phosphate synthase !8(glutamine-hydrolyzing) large chain homology #label !8CPL\ !$440-891 #domain biotin carboxylase homology #label BC1\ !$981-1424 #domain biotin carboxylase homology #label BC2\ !$1500-1825 #domain Bacillus dihydroorotase homology #label DHO\ !$1911-2210 #domain aspartate/ornithine carbamoyltransferase !8homology #label ACT\ !$302 #active_site Cys #status predicted SUMMARY #length 2214 #molecular-weight 245124 #checksum 8700 SEQUENCE /// ENTRY QZDOP3 #type fragments TITLE pyrimidine synthesis protein PYR1-3 - slime mold (Dictyostelium discoideum) (fragments) CONTAINS aspartate carbamoyltransferase (EC 2.1.3.2); carbamoyl-phosphate synthase (glutamine-hydrolyzing) (EC 6.3.5.5); dihydroorotase (EC 3.5.2.3) ORGANISM #formal_name Dictyostelium discoideum DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 07-Aug-1998 ACCESSIONS S02800 REFERENCE S02800 !$#authors Faure, M.; Camonis, J.H.; Jacquet, M. !$#journal Eur. J. Biochem. (1989) 179:345-358 !$#title Molecular characterization of a Dictyostelium discoideum !1gene encoding a multifunctional enzyme of the pyrimidine !1pathway. !$#cross-references MUID:89137111; PMID:2917570 !$#accession S02800 !'##molecule_type DNA !'##residues 1-467;468-1481 ##label FAU !'##cross-references EMBL:X14633 !'##experimental_source strain AX3 GENETICS !$#gene PYR1-3 CLASSIFICATION #superfamily rudimentary enzyme; aspartate/ornithine !1carbamoyltransferase homology; Bacillus dihydroorotase !1homology; biotin carboxylase homology; carbamoyl-phosphate !1synthase (ammonia) homology; carbamoyl-phosphate synthase !1(glutamine-hydrolyzing) large chain homology; !1carbamoyl-phosphate synthase (glutamine-hydrolyzing) small !1chain homology; trpG homology KEYWORDS hydrolase; ligase; methyltransferase; multifunctional !1enzyme; pyrimidine nucleotide biosynthesis FEATURE !$1-707 #domain carbamoyl-phosphate synthase (ammonia) !8homology (fragments) #label CPA\ !$1-340 #domain carbamoyl-phosphate synthase !8(glutamine-hydrolyzing) small chain homology #label !8CPS\ !$158-340 #domain trpG homology #label TRG\ !$357-704 #domain carbamoyl-phosphate synthase !8(glutamine-hydrolyzing) large chain homology !8(fragments) #label CPL\ !$367-467 #domain biotin carboxylase homology (fragment) #label !8BC1\ !$468-651 #domain biotin carboxylase homology (fragment) #label !8BC2\ !$721-1066 #domain Bacillus dihydroorotase homology #label DHO\ !$1179-1477 #domain aspartate/ornithine carbamoyltransferase !8homology #label ACT\ !$236 #active_site Cys #status predicted SUMMARY #length 1481 #checksum 8678 SEQUENCE /// ENTRY SYECCS #type complete TITLE carbamoyl-phosphate synthase (glutamine-hydrolyzing) (EC 6.3.5.5) small chain [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES carbamoyl-phosphate synthetase glutamine chain ORGANISM #formal_name Escherichia coli DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 01-Mar-2002 ACCESSIONS A01128; S40555; H64723 REFERENCE A01128 !$#authors Lusty, C.J. !$#submission submitted to the Protein Sequence Database, April 1984 !$#accession A01128 !'##molecule_type protein !'##residues 1-382 ##label LUS REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40555 !'##molecule_type DNA !'##residues 'L',2-382 ##label YUR !'##cross-references EMBL:D10483 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64723 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-382 ##label BLAT !'##cross-references GB:AE000113; GB:U00096; NID:g2367095; !1PIDN:AAC73143.1; PID:g1786215; UWGP:b0032 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene carA; pyrA !$#map_position 1 min COMPLEX heterodimer; large chain (PIR:SYECCP) and small chain !1(PIR:SYECCS) [validated, MUID:99190825] FUNCTION !$#description EC 6.3.5.5 [validated, MUID:99190825]; catalyzes formation !1of carbamoyl-phosphate using glutamine; the small chain !1promotes hydrolysis of glutamine to ammonia, which is used !1to synthesize carbamoyl-phosphate by the large chain !$#pathway glutamate metabolism; pyrimidine nucleotide biosynthesis !$#note sequence of the second half (residues 190-382) of the small !1chain is homologous to the trpG-encoded domain; the first !1half (residues 1-189) shows some similarity to the carboxyl !1end of the trpD-encoded domain CLASSIFICATION #superfamily carbamoyl-phosphate synthase !1(glutamine-hydrolyzing) small chain; carbamoyl-phosphate !1synthase (glutamine-hydrolyzing) small chain homology; trpG !1homology KEYWORDS arginine biosynthesis; heterodimer; ligase; pyrimidine !1nucleotide biosynthesis FEATURE !$7-371 #domain carbamoyl-phosphate synthase !8(glutamine-hydrolyzing) small chain homology #label !8CPS\ !$194-371 #domain trpG homology #label TRG\ !$269 #active_site Cys #status predicted SUMMARY #length 382 #molecular-weight 41431 #checksum 3036 SEQUENCE /// ENTRY S01319 #type complete TITLE carbamoyl-phosphate synthase (glutamine-hydrolyzing) (EC 6.3.5.5) small chain - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 18-Jun-1999 ACCESSIONS S01319 REFERENCE S01319 !$#authors Kilstrup, M.; Lu, C.D.; Abdelal, A.; Neuhard, J. !$#journal Eur. J. Biochem. (1988) 176:421-429 !$#title Nucleotide sequence of the carA gene and regulation of the !1carAB operon in Salmonella typhimurium. !$#cross-references MUID:88329100; PMID:2843375 !$#accession S01319 !'##molecule_type DNA !'##residues 1-382 ##label KIL !'##cross-references GB:U81260; EMBL:X13200; NID:g1750390; !1PIDN:AAB39255.1; PID:g1750391 COMMENT This enzyme catalyzes the formation of carbamoyl phosphate !1from glutamine. In E. coli it is composed of two chains; the !1small (or glutamine) chain promotes the hydrolysis of !1glutamine to ammonia, which is used by the large (or !1ammonia) chain to synthesize carbamoyl phosphate. GENETICS !$#gene carA !$#start_codon TTG CLASSIFICATION #superfamily carbamoyl-phosphate synthase !1(glutamine-hydrolyzing) small chain; carbamoyl-phosphate !1synthase (glutamine-hydrolyzing) small chain homology; trpG !1homology KEYWORDS arginine biosynthesis; heterodimer; ligase; pyrimidine !1nucleotide biosynthesis FEATURE !$7-371 #domain carbamoyl-phosphate synthase !8(glutamine-hydrolyzing) small chain homology #label !8CPS\ !$194-371 #domain trpG homology #label TRG\ !$269 #active_site Cys #status predicted SUMMARY #length 382 #molecular-weight 41646 #checksum 5040 SEQUENCE /// ENTRY SYBYCS #type complete TITLE carbamoyl-phosphate synthase (glutamine-hydrolyzing) (EC 6.3.5.5) small chain - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES carbamoyl-phosphate synthetase (glutamine-hydrolyzing) glutamine chain; protein O5645; protein YOR303w ORGANISM #formal_name Saccharomyces cerevisiae DATE 28-Dec-1987 #sequence_revision 02-Aug-1996 #text_change 21-Jul-2000 ACCESSIONS S67207; A21714; S05834; S05898 REFERENCE S67194 !$#authors Cziepluch, C.; Jauniaux, J.C.; Kordes, E.; Poirey, R.; !1Pujol, A.; Tobiasch, E. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67207 !'##molecule_type DNA !'##residues 1-411 ##label CZI !'##cross-references EMBL:Z75211; NID:g1420668; PIDN:CAA99621.1; !1PID:g1420669; GSPDB:GN00015; MIPS:YOR303w !'##experimental_source strain S288C REFERENCE A21714 !$#authors Werner, M.; Feller, A.; Pierard, A. !$#journal Eur. J. Biochem. (1985) 146:371-381 !$#title Nucleotide sequence of yeast gene CPA1 encoding the small !1subunit of arginine-pathway carbamoyl-phosphate synthetase: !1homology of the deduced amino acid sequence to other !1glutamine amidotransferases. !$#cross-references MUID:85101411; PMID:3881260 !$#accession A21714 !'##molecule_type DNA !'##residues 1-88,'Y',90-411 ##label WER !'##cross-references EMBL:X01764 !'##note the authors translated the codon TAT for residue 89 as His and !1GGT for residue 284 as Gln REFERENCE S05834 !$#authors Nyunoya, H.; Lusty, C.J. !$#journal J. Biol. Chem. (1984) 259:9790-9798 !$#title Sequence of the small subunit of yeast carbamyl phosphate !1synthetase and identification of its catalytic domain. !$#cross-references MUID:84264639; PMID:6086650 !$#accession S05834 !'##molecule_type DNA !'##residues 1-411 ##label NYU !'##cross-references EMBL:K02132; NID:g171304; PIDN:AAA34525.1; !1PID:g171305 GENETICS !$#gene SGD:CPA1; MIPS:YOR303w !'##cross-references SGD:S0005829; MIPS:YOR303w !$#map_position 15R CLASSIFICATION #superfamily carbamoyl-phosphate synthase !1(glutamine-hydrolyzing) small chain; carbamoyl-phosphate !1synthase (glutamine-hydrolyzing) small chain homology; trpG !1homology KEYWORDS arginine biosynthesis; heterodimer; ligase; pyrimidine !1nucleotide biosynthesis FEATURE !$10-367 #domain carbamoyl-phosphate synthase !8(glutamine-hydrolyzing) small chain homology #label !8CPS\ !$186-367 #domain trpG homology #label TRG\ !$264 #active_site Cys #status predicted SUMMARY #length 411 #molecular-weight 45361 #checksum 7932 SEQUENCE /// ENTRY NNBY2 #type complete TITLE anthranilate synthase multifunctional enzyme - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YKL211c CONTAINS anthranilate synthase (EC 4.1.3.27); glutamine amidotransferase (EC 2.6.1.-); indole-3-glycerol-phosphate synthase (EC 4.1.1.48) ORGANISM #formal_name Saccharomyces cerevisiae DATE 20-Sep-1984 #sequence_revision 02-May-1994 #text_change 12-Nov-1999 ACCESSIONS S38049; S38054; S44327; A01129; S05752 REFERENCE S37897 !$#authors Pohl, T.M.; Pohl, F.M. !$#submission submitted to the Protein Sequence Database, March 1994 !$#accession S38049 !'##molecule_type DNA !'##residues 1-484 ##label POH !'##cross-references EMBL:Z28211; NID:g486376; PIDN:CAA82056.1; !1PID:g486377; GSPDB:GN00011; MIPS:YKL211c !'##experimental_source strain S288C REFERENCE S38054 !$#authors Alexandraki, D.; Tzermia, M. !$#submission submitted to the Protein Sequence Database, March 1994 !$#accession S38054 !'##molecule_type DNA !'##residues 1-484 ##label ALE !'##cross-references EMBL:Z28211; NID:g486376; PIDN:CAA82056.1; !1PID:g486377; GSPDB:GN00011; MIPS:YKL211c !'##experimental_source strain S288C REFERENCE S44319 !$#authors Tzermia, M.; Horaitis, O.; Alexandraki, D. !$#journal Yeast (1994) 10:663-679 !$#title The complete sequencing of a 24.6 kb segment of yeast !1chromosome XI identified the known loci URA1, SAC1 and TRP3, !1and revealed 6 new open reading frames including homologues !1to the threonine dehydratases, membrane transporters, !1hydantoinases and the phospholipase A(2)-activating protein. !$#cross-references MUID:95028164; PMID:7941750 !$#accession S44327 !'##status translation not shown !'##molecule_type DNA !'##residues 1-484 ##label TZE !'##cross-references EMBL:X75951; NID:g473130; PIDN:CAA53562.1; !1PID:g473139 REFERENCE A92473 !$#authors Zalkin, H.; Paluh, J.L.; van Cleemput, M.; Moye, W.S.; !1Yanofsky, C. !$#journal J. Biol. Chem. (1984) 259:3985-3992 !$#title Nucleotide sequence of Saccharomyces cerevisiae genes TRP2 !1and TRP3 encoding bifunctional anthranilate !1synthase:indole-3-glycerol phosphate synthase. !$#cross-references MUID:84162082; PMID:6323449 !$#accession A01129 !'##molecule_type DNA !'##residues 1-128,'R',130-484 ##label ZAL !'##cross-references EMBL:K01386; NID:g173044; PIDN:AAA35176.1; !1PID:g173045 REFERENCE S05752 !$#authors Aebi, M.; Furter, R.; Prantl, F.; Niederberger, P.; Huetter, !1R. !$#journal Curr. Genet. (1984) 8:165-172 !$#title Structure and function of the TRP3 gene of Saccharomyces !1cerevisiae: analysis of transcription, promoter sequence, !1and sequence coding for a glutamine amidotransferase. !$#accession S05752 !'##molecule_type DNA !'##residues 1-62,'L',64,'L',66-235,'S',237-280 ##label AEB !'##cross-references EMBL:M36300 !'##note the authors translated the codon TCC for residue 32 as Cys, TAC !1for residue 170 as His, and ACC for residue 238 as Tyr; the !1sequence shown follows the author's translation at positions !132 and 170 COMMENT Anthranilate synthase catalyzes the biosynthesis of !1anthranilate from chorismate and glutamine. It contains two !1chains with different catalytic activities: component I !1catalyzes the formation of anthranilate using ammonia rather !1than glutamine, whereas component II provides the glutamine !1amidotransferase activity. In yeast, component II is smaller !1and its carboxyl end also has indole-3-glycerol-phosphate !1synthase activity. GENETICS !$#gene SGD:TRP3; MIPS:YKL211c !'##cross-references SGD:S0001694; MIPS:YKL211c !$#map_position 11L CLASSIFICATION #superfamily trpG-trpC bifunctional enzyme; trpC homology; !1trpG homology KEYWORDS aminotransferase; carbon-carbon lyase; carboxy-lyase; !1multifunctional enzyme; oxo-acid-lyase; P-loop; purine !1nucleotide binding; tryptophan biosynthesis FEATURE !$14-198 #domain trpG homology #label TRG\ !$110-117 #region nucleotide-binding motif A (P-loop)\ !$216-482 #domain trpC homology #label TRC\ !$92,116 #active_site Cys, Lys #status predicted\ !$116 #binding_site ATP/GTP (Lys) #status predicted SUMMARY #length 484 #molecular-weight 53489 #checksum 944 SEQUENCE /// ENTRY NNNC2 #type complete TITLE anthranilate synthase (EC 4.1.3.27) component II - Neurospora crassa CONTAINS glutamine amidotransferase; indole-3-glycerol-phosphate synthase (EC 4.1.1.48); phosphoribosylanthranilate isomerase (EC 5.3.1.24) ORGANISM #formal_name Neurospora crassa DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 05-Jun-1998 ACCESSIONS A01130 REFERENCE A01130 !$#authors Schechtman, M.G.; Yanofsky, C. !$#journal J. Mol. Appl. Genet. (1983) 2:83-99 !$#title Structure of the trifunctional trp-1 gene from Neurospora !1crassa and its aberrant expression in Escherichia coli. !$#cross-references MUID:83187993; PMID:6221060 !$#accession A01130 !'##molecule_type DNA !'##residues 1-762 ##label SCH COMMENT In N. crassa, component I (trp-2 gene product) of this !1enzyme catalyzes the formation of anthranilate using ammonia !1rather than glutamine, whereas component II (trp-1 gene !1product) is a trifunctional polypeptide bearing the !1glutamine amidotransferase (trpG), !1indole-3-glycerol-phosphate synthase (trpC), and !1phosphoribosylanthranilate isomerase (trpF) activities. COMMENT The active enzyme is a tetramer containing two chains each !1of components I and II. GENETICS !$#gene trp-1 (trpG-trpC-trpF) CLASSIFICATION #superfamily trpG-trpC-trpF trifunctional enzyme; trpC !1homology; trpF homology; trpG homology KEYWORDS carbon-carbon lyase; carboxy-lyase; intramolecular !1oxidoreductase; isomerase; oxo-acid-lyase; tryptophan !1biosynthesis FEATURE !$26-215 #domain trpG homology #label TRG\ !$251-514 #domain trpC homology #label TRC\ !$533-758 #domain trpF homology #label TRF\ !$104 #active_site Cys #status predicted SUMMARY #length 762 #molecular-weight 82520 #checksum 2714 SEQUENCE /// ENTRY JT0383 #type complete TITLE anthranilate synthase (EC 4.1.3.27) component II - Phycomyces blakesleeanus CONTAINS glutamine amidotransferase (EC 2.6.1.-); indole-3-glycerol-phosphate synthase (EC 4.1.1.48); N- (5'-phosphoribosyl)anthranilate isomerase (EC 5.3.1.-) ORGANISM #formal_name Phycomyces blakesleeanus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 31-Mar-2000 ACCESSIONS JT0383; A27780 REFERENCE JT0383 !$#authors Choi, H.T.; Revuelta, J.L.; Sadhu, C.; Jayaram, M. !$#journal Gene (1988) 71:85-95 !$#title Structural organization of the TRP1 gene of Phycomyces !1blakesleeanus: implications for evolutionary gene fusion in !1fungi. !$#cross-references MUID:89108051; PMID:3215529 !$#accession JT0383 !'##molecule_type DNA !'##residues 1-765 ##label CHO GENETICS !$#gene TRP1 (TrpG-TrpC-TrpF) CLASSIFICATION #superfamily trpG-trpC-trpF trifunctional enzyme; trpC !1homology; trpF homology; trpG homology KEYWORDS aminotransferase; carbon-carbon lyase; carboxy-lyase; !1intramolecular oxidoreductase; isomerase; multifunctional !1enzyme; oxo-acid-lyase; tryptophan biosynthesis FEATURE !$3-187 #domain trpG homology #label TRG\ !$232-493 #domain trpC homology #label TRC\ !$514-759 #domain trpF homology #label TRF\ !$81 #active_site Cys #status predicted SUMMARY #length 765 #molecular-weight 83422 #checksum 9336 SEQUENCE /// ENTRY S15239 #type complete TITLE anthranilate synthase multifunctional enzyme - basidiomycete (Phanerochaete chrysosporium) ALTERNATE_NAMES anthranilate synthase multifunctional protein CONTAINS anthranilate synthase (EC 4.1.3.27); glutamine amidotransferase (EC 2.6.1.-); indole-3-glycerol-phosphate synthase (EC 4.1.1.48); N-(5'-phosphoribosyl)anthranilate isomerase (EC 5.5.-.-) ORGANISM #formal_name Phanerochaete chrysosporium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S15239 REFERENCE S15239 !$#authors Schrank, A.; Tempelaars, C.; Sims, P.F.G.; Oliver, S.G.; !1Broda, P. !$#journal Mol. Microbiol. (1991) 5:467-476 !$#title The trpC gene of Phanerochaete chrysosporium is unique in !1containing an intron but nevertheless maintains the order of !1functional domains seen in other fungi. !$#cross-references MUID:91251778; PMID:2041479 !$#accession S15239 !'##molecule_type DNA !'##residues 1-788 ##label SCH !'##cross-references EMBL:X56047; NID:g3165; PIDN:CAA39518.1; PID:g3166 GENETICS !$#gene trpC !$#introns 106/2 CLASSIFICATION #superfamily trpG-trpC-trpF trifunctional enzyme; trpC !1homology; trpF homology; trpG homology KEYWORDS aminotransferase; carbon-carbon lyase; carboxy-lyase; !1intramolecular lyase; isomerase; multifunctional enzyme; !1oxo-acid-lyase; tryptophan biosynthesis FEATURE !$13-198 #domain trpG homology #label TRG\ !$238-502 #domain trpC homology #label TRC\ !$522-785 #domain trpF homology #label TRF\ !$91 #active_site Cys #status predicted SUMMARY #length 788 #molecular-weight 85344 #checksum 6137 SEQUENCE /// ENTRY GWEC #type complete TITLE indole-3-glycerol-phosphate synthase (EC 4.1.1.48) / phosphoribosylanthranilate isomerase (EC 5.3.1.24) [validated] - Escherichia coli (strain K-12) CONTAINS indole-3-glycerol-phosphate synthase (EC 4.1.1.48); phosphoribosylanthranilate isomerase (EC 5.3.1.24) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1980 #sequence_revision 21-Nov-1997 #text_change 02-Apr-2002 ACCESSIONS A64874; A01131; B93746; I54118; A93746 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64874 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-453 ##label BLAT !'##cross-references GB:AE000224; GB:U00096; NID:g1787509; !1PIDN:AAC74344.1; PID:g1787516; UWGP:b1262 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A92861 !$#authors Christie, G.E.; Platt, T. !$#journal J. Mol. Biol. (1980) 142:519-530 !$#title Gene structure in the tryptophan operon of Escherichia coli. !1Nucleotide sequence of trpC and the flanking intercistronic !1regions. !$#cross-references MUID:81119811; PMID:7007653 !$#accession A01131 !'##molecule_type DNA !'##residues 2-329,'V',331-453 ##label CHR !'##note this sequence has since been revised REFERENCE A92907 !$#authors Horowitz, H.; Van Arsdell, J.; Platt, T. !$#journal J. Mol. Biol. (1983) 169:775-797 !$#title Nucleotide sequence of the trpD and trpC genes of Salmonella !1typhimurium. !$#cross-references MUID:84036180; PMID:6355484 !$#contents annotation; revisions to residues 94 and 398 REFERENCE A93746 !$#authors Yanofsky, C.; Platt, T.; Crawford, I.P.; Nichols, B.P.; !1Christie, G.E.; Horowitz, H.; van Cleemput, M.; Wu, A.M. !$#journal Nucleic Acids Res. (1981) 9:6647-6668 !$#title The complete nucleotide sequence of the tryptophan operon of !1Escherichia coli. !$#cross-references MUID:82150258; PMID:7038627 !$#accession B93746 !'##molecule_type DNA !'##residues 2-30,32-94,'R',96-284,286-293,'D',295-329,'V',331-398,'T', !1400-453 ##label YAN !'##cross-references GB:V00372; NID:g43201; PIDN:CAA23673.1; PID:g43204 REFERENCE I54118 !$#authors Milkman, R.; Bridges, M.M. !$#journal Genetics (1993) 133:455-468 !$#title Molecular evolution of the Escherichia coli chromosome. IV. !1Sequence comparisons. !$#cross-references MUID:93202463; PMID:8095913 !$#accession I54118 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 2-398,'T',400-453 ##label RES !'##cross-references EMBL:U23490; NID:g775130; PIDN:AAA65138.1; !1PID:g775131 REFERENCE A59407 !$#authors Darimont, B.; Stehlin, C.; Szadkowski, H.; Kirschner, K. !$#journal Protein Sci. (1998) 7:1221-1232 !$#cross-references MUID:98266365; PMID:9605328 !$#contents annotation; active site !$#note the catalytic mechanism involves two enzyme-bound !1intermediates and general acid-base catalysis by Lys-115 and !1Glu-164 with the suport of Glu-54 and Asn-184 GENETICS !$#gene trpC-trpF !$#map_position 28 min FUNCTION PRAI !$#description phosphoribosylanthranilate isomerase catalyzes conversion of !1N-5'-phosphoribosyl-anthranilate to 1- !1(2-carboxyphenylamino)-1-deoxyribulose 5-phosphate !$#pathway tryptophan biosynthesis !$#note third step; catalyzed by the trpF homology domain FUNCTION IGPS !$#description indole-3-glycerol phosphate synthase catalyzes the ring !1closure to indol-3-glycerol-phosphate !$#pathway tryptophan biosynthesis !$#note fourth step; catalyzed by the trpC homology domain CLASSIFICATION #superfamily trpC-trpF bifunctional enzyme; trpC homology; !1trpF homology KEYWORDS carbon-carbon lyase; carboxy-lyase; intramolecular !1oxidoreductase; isomerase; monomer; tryptophan biosynthesis FEATURE !$5-253 #domain trpC homology #label TRC\ !$259-450 #domain trpF homology #label TRF\ !$115,164 #active_site Lys, Glu #status experimental SUMMARY #length 453 #molecular-weight 49492 #checksum 9929 SEQUENCE /// ENTRY GWEBT #type complete TITLE indole-3-glycerol-phosphate synthase (EC 4.1.1.48) / phosphoribosylanthranilate isomerase (EC 5.3.1.24) - Salmonella typhimurium CONTAINS indole-3-glycerol-phosphate synthase (EC 4.1.1.48); phosphoribosylanthranilate isomerase (EC 5.3.1.24) ORGANISM #formal_name Salmonella typhimurium DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 19-Apr-2002 ACCESSIONS A01132 REFERENCE A92907 !$#authors Horowitz, H.; Van Arsdell, J.; Platt, T. !$#journal J. Mol. Biol. (1983) 169:775-797 !$#title Nucleotide sequence of the trpD and trpC genes of Salmonella !1typhimurium. !$#cross-references MUID:84036180; PMID:6355484 !$#accession A01132 !'##molecule_type DNA !'##residues 1-452 ##label HOR !'##cross-references GB:M30286; NID:g154394; PIDN:AAA27237.1; !1PID:g154397 GENETICS !$#gene trpC-trpF !$#map_position 34 min FUNCTION PRAI !$#description phosphoribosylanthranilate isomerase catalyzes conversion of !1N-5'-phosphoribosyl-anthranilate to 1- !1(2-carboxyphenylamino)-1-deoxyribulose 5-phosphate !$#pathway tryptophan biosynthesis !$#note third step; catalyzed by the trpF homology domain FUNCTION IGPS !$#description indole-3-glycerol phosphate synthase catalyzes the ring !1closure to indol-3-glycerol-phosphate !$#pathway tryptophan biosynthesis !$#note fourth step; catalyzed by the trpC homology domain CLASSIFICATION #superfamily trpC-trpF bifunctional enzyme; trpC homology; !1trpF homology KEYWORDS carbon-carbon lyase; carboxy-lyase; intramolecular !1oxidoreductase; isomerase; monomer; tryptophan biosynthesis FEATURE !$4-252 #domain trpC homology #label TRC\ !$258-449 #domain trpF homology #label TRF SUMMARY #length 452 #molecular-weight 49201 #checksum 6305 SEQUENCE /// ENTRY E24723 #type complete TITLE trpC protein - Corynebacterium glutamicum ORGANISM #formal_name Corynebacterium glutamicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS E24723 REFERENCE A93606 !$#authors Matsui, K.; Sano, K.; Ohtsubo, E. !$#journal Nucleic Acids Res. (1986) 14:10113-10114 !$#title Complete nucleotide and deduced amino acid sequences of the !1Brevibacterium lactofermentum tryptophan operon. !$#cross-references MUID:87117512; PMID:3808947 !$#contents B. lactofermentum !$#accession E24723 !'##molecule_type DNA !'##residues 1-474 ##label MAT !'##cross-references GB:X04960; NID:g39591; PIDN:CAA28626.1; PID:g39596 GENETICS !$#gene trpC CLASSIFICATION #superfamily trpC-trpF bifunctional enzyme; trpC homology; !1trpF homology FEATURE !$9-258 #domain trpC homology #label TRC\ !$264-460 #domain trpF homology #label TRF SUMMARY #length 474 #molecular-weight 50903 #checksum 8887 SEQUENCE /// ENTRY GWKECC #type complete TITLE indole-3-glycerol-phosphate synthase (EC 4.1.1.48) - Acinetobacter calcoaceticus ALTERNATE_NAMES 1-(2-carboxyphenylamino)-1-decarboxy-D-ribulose-5-phosphate carboxy-lyase (cyclizing) ORGANISM #formal_name Acinetobacter calcoaceticus DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 18-Jun-1999 ACCESSIONS A01133 REFERENCE A93052 !$#authors Kaplan, J.B.; Goncharoff, P.; Seibold, A.M.; Nichols, B.P. !$#journal Mol. Biol. Evol. (1984) 1:456-472 !$#title Nucleotide sequence of the Acinetobacter calcoaceticus !1trpGDC gene cluster. !$#cross-references MUID:88174326; PMID:6599977 !$#accession A01133 !'##molecule_type DNA !'##residues 1-268 ##label KAP !'##cross-references GB:M36636; NID:g141799; PIDN:AAA21905.1; !1PID:g141802 GENETICS !$#gene trpC CLASSIFICATION #superfamily indole-3-glycerol-phosphate synthase; trpC !1homology KEYWORDS carbon-carbon lyase; carboxy-lyase; tryptophan biosynthesis FEATURE !$8-261 #domain trpC homology #label TRC SUMMARY #length 268 #molecular-weight 30216 #checksum 3504 SEQUENCE /// ENTRY C35114 #type complete TITLE indole-3-glycerol-phosphate synthase (EC 4.1.1.48) - Pseudomonas aeruginosa ALTERNATE_NAMES trpC ORGANISM #formal_name Pseudomonas aeruginosa DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 31-Dec-2000 ACCESSIONS C35114; B55540; A83564 REFERENCE A35114 !$#authors Essar, D.W.; Eberly, L.; Han, C.Y.; Crawford, I.P. !$#journal J. Bacteriol. (1990) 172:853-866 !$#title DNA sequences and characterization of four early genes of !1the tryptophan pathway in Pseudomonas aeruginosa. !$#cross-references MUID:90130324; PMID:2105306 !$#accession C35114 !'##molecule_type DNA !'##residues 1-278 ##label ESS !'##cross-references GB:M33814; NID:g151232; PIDN:AAA25825.1; !1PID:g151235 REFERENCE A55540 !$#authors West, S.E.H.; Sample, A.K.; Runyen-Janecky, L.J. !$#journal J. Bacteriol. (1994) 176:7532-7542 !$#title The vfr gene product, required for Pseudomonas aeruginosa !1exotoxin A and protease production, belongs to the cyclic !1AMP receptor protein family. !$#cross-references MUID:95095922; PMID:8002577 !$#accession B55540 !'##molecule_type DNA !'##residues 258-278 ##label WES !'##cross-references GB:U16318 REFERENCE A82950 !$#authors Stover, C.K.; Pham, X.Q.; Erwin, A.L.; Mizoguchi, S.D.; !1Warrener, P.; Hickey, M.J.; Brinkman, F.S.L.; Hufnagle, !1W.O.; Kowalik, D.J.; Lagrou, M.; Garber, R.L.; Goltry, L.; !1Tolentino, E.; Westbrook-Wadman, S.; Yuan, Y.; Brody, L.L.; !1Coulter, S.N.; Folger, K.R.; Kas, A.; Larbig, K.; Lim, R.M.; !1Smith, K.A.; Spencer, D.H.; Wong, G.K.S.; Wu, Z.; Paulsen, !1I.T.; Reizer, J.; Saier, M.H.; Hancock, R.E.W.; Lory, S.; !1Olson, M.V. !$#journal Nature (2000) 406:959-964 !$#title Complete genome sequence of Pseudomonas aeruginosa PA01, an !1opportunistic pathogen. !$#cross-references MUID:20437337; PMID:10984043 !$#accession A83564 !'##status preliminary !'##molecule_type DNA !'##residues 1-278 ##label STO !'##cross-references GB:AE004500; GB:AE004091; NID:g9946522; !1PIDN:AAG04040.1; GSPDB:GN00131; PASP:PA0651 !'##experimental_source strain PAO1 GENETICS !$#gene trpC; PA0651 !$#start_codon GTG CLASSIFICATION #superfamily indole-3-glycerol-phosphate synthase; trpC !1homology KEYWORDS carbon-carbon lyase; carboxy-lyase; tryptophan biosynthesis FEATURE !$6-263 #domain trpC homology #label TRC SUMMARY #length 278 #molecular-weight 30347 #checksum 9472 SEQUENCE /// ENTRY D35115 #type complete TITLE indole-3-glycerol-phosphate synthase (EC 4.1.1.48) - Pseudomonas putida ORGANISM #formal_name Pseudomonas putida DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS D35115 REFERENCE A35115 !$#authors Essar, D.W.; Eberly, L.; Crawford, I.P. !$#journal J. Bacteriol. (1990) 172:867-883 !$#title Evolutionary differences in chromosomal locations of four !1early genes of the tryptophan pathway in fluorescent !1pseudomonads: DNA sequences and characterization of !1Pseudomonas putida trpE and trpGDC. !$#cross-references MUID:90130325; PMID:2404959 !$#accession D35115 !'##status preliminary !'##molecule_type DNA !'##residues 1-277 ##label ESS !'##cross-references GB:M33799; NID:g151627; PIDN:AAA80555.1; !1PID:g1052830; GB:M33800; GB:M33801 CLASSIFICATION #superfamily indole-3-glycerol-phosphate synthase; trpC !1homology KEYWORDS carbon-carbon lyase; carboxy-lyase FEATURE !$6-263 #domain trpC homology #label TRC SUMMARY #length 277 #molecular-weight 30550 #checksum 776 SEQUENCE /// ENTRY S17705 #type complete TITLE indole-3-glycerol-phosphate synthase (EC 4.1.1.48) - Azospirillum brasilense ORGANISM #formal_name Azospirillum brasilense DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S17705 REFERENCE S17702 !$#authors Zimmer, W.; Aparicio, C.; Elmerich, C. !$#journal Mol. Gen. Genet. (1991) 229:41-51 !$#title Relationship between tryptophan biosynthesis and !1indole-3-acetic acid production in Azospirillum: !1identification and sequencing of a trpGDC cluster. !$#cross-references MUID:91375449; PMID:1896020 !$#accession S17705 !'##molecule_type DNA !'##residues 1-262 ##label ZIM !'##cross-references EMBL:X57853; NID:g48840; PIDN:CAA40986.1; !1PID:g48844 CLASSIFICATION #superfamily indole-3-glycerol-phosphate synthase; trpC !1homology KEYWORDS carbon-carbon lyase; carboxy-lyase FEATURE !$4-260 #domain trpC homology #label TRC SUMMARY #length 262 #molecular-weight 28123 #checksum 176 SEQUENCE /// ENTRY A42948 #type complete TITLE indoleglycerol phosphate synthase, TrpC - Rhodobacter capsulatus ORGANISM #formal_name Rhodobacter capsulatus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A42948 REFERENCE A42948 !$#authors Becker-Rudzik, M.; Young, D.A.; Marrs, B.L. !$#journal J. Bacteriol. (1992) 174:5482-5484 !$#title Sequence of the indoleglycerol phosphate synthase (trpC) !1gene from Rhodobacter capsulatus. !$#cross-references MUID:92355531; PMID:1644778 !$#accession A42948 !'##status preliminary !'##molecule_type DNA !'##residues 1-261 ##label BEC !'##cross-references GB:M97640; NID:g152042; PIDN:AAA26181.1; !1PID:g152043 !'##note sequence extracted from NCBI backbone (NCBIN:110571, !1NCBIP:110572) CLASSIFICATION #superfamily indole-3-glycerol-phosphate synthase; trpC !1homology FEATURE !$4-258 #domain trpC homology #label TRC SUMMARY #length 261 #molecular-weight 27975 #checksum 4981 SEQUENCE /// ENTRY GWBS #type complete TITLE indole-3-glycerol-phosphate synthase (EC 4.1.1.48) - Bacillus subtilis ALTERNATE_NAMES 1-(2-carboxyphenylamino)-1-decarboxy-D-ribulose-5-phosphate carboxy-lyase (cyclizing) ORGANISM #formal_name Bacillus subtilis DATE 13-Aug-1986 #sequence_revision 10-Feb-1995 #text_change 21-Jul-2000 ACCESSIONS A01134; C22794; A69726 REFERENCE A91509 !$#authors Band, L.; Shimotsu, H.; Henner, D.J. !$#journal Gene (1984) 27:55-65 !$#title Nucleotide sequence of the Bacillus subtilis trpE and trpD !1genes. !$#cross-references MUID:84183611; PMID:6425119 !$#accession A01134 !'##molecule_type DNA !'##residues 1-73,'RMRFP',79-246 ##label BAN !'##cross-references GB:K01391 !'##note this sequence has been corrected REFERENCE A91520 !$#authors Henner, D.J.; Band, L.; Shimotsu, H. !$#journal Gene (1985) 34:169-177 !$#title Nucleotide sequence of the Bacillus subtilis tryptophan !1operon. !$#cross-references MUID:85232062; PMID:3924737 !$#accession C22794 !'##molecule_type DNA !'##residues 1-250 ##label HEN !'##cross-references GB:K01391; NID:g143767; PIDN:AAA22867.1; !1PID:g143770 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69726 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-250 ##label KUN !'##cross-references GB:Z99115; GB:AL009126; NID:g2634478; !1PIDN:CAB14182.1; PID:g2634684 !'##experimental_source strain 168 GENETICS !$#gene trpC !$#map_position 205 (degrees) CLASSIFICATION #superfamily indole-3-glycerol-phosphate synthase; trpC !1homology KEYWORDS carbon-carbon lyase; carboxy-lyase; tryptophan biosynthesis FEATURE !$1-247 #domain trpC homology #label TRC SUMMARY #length 250 #molecular-weight 27928 #checksum 9024 SEQUENCE /// ENTRY JS0341 #type complete TITLE indole-3-glycerol-phosphate synthase (EC 4.1.1.48) - Lactobacillus casei ALTERNATE_NAMES trpC protein ORGANISM #formal_name Lactobacillus casei DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S42344; JS0341 REFERENCE S42342 !$#authors Natori, Y.; Kano, Y.; Imamoto, F. !$#journal J. Biochem. (1990) 107:248-255 !$#title Nucleotide sequences and genomic constitution of five !1tryptophan genes of Lactobacillus casei. !$#cross-references MUID:90299861; PMID:2113923 !$#accession S42344 !'##molecule_type DNA !'##residues 1-260 ##label NAT !'##cross-references EMBL:D00496; NID:g216754; PIDN:BAA00384.1; !1PID:g216757 !'##experimental_source isolate RNL7 GENETICS !$#gene trpC CLASSIFICATION #superfamily indole-3-glycerol-phosphate synthase; trpC !1homology KEYWORDS carbon-carbon lyase; carboxy-lyase; tryptophan biosynthesis FEATURE !$2-256 #domain trpC homology #label TRC SUMMARY #length 260 #molecular-weight 28943 #checksum 1750 SEQUENCE /// ENTRY C36044 #type complete TITLE indole-3-glycerol-phosphate synthase (EC 4.1.1.48) [validated] - Haloferax volcanii (strain WFD11) ORGANISM #formal_name Haloferax volcanii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 26-May-2000 ACCESSIONS C36044 REFERENCE A36044 !$#authors Lam, W.L.; Cohen, A.; Tsouluhas, D.; Doolittle, W.F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:6614-6618 !$#title Genes for tryptophan biosynthesis in the archaebacterium !1Haloferax volcanii. !$#cross-references MUID:90370836; PMID:2118654 !$#accession C36044 !'##status preliminary !'##molecule_type DNA !'##residues 1-251 ##label LAM !'##cross-references GB:M36177; NID:g149041; PIDN:AAA72862.1; !1PID:g149042 GENETICS !$#gene trpC FUNCTION !$#description EC 4.1.1.48 [validated, MUID:90370836] CLASSIFICATION #superfamily indole-3-glycerol-phosphate synthase; trpC !1homology KEYWORDS carbon-carbon lyase; carboxy-lyase FEATURE !$4-249 #domain trpC homology #label TRC SUMMARY #length 251 #molecular-weight 26754 #checksum 8890 SEQUENCE /// ENTRY F40362 #type complete TITLE trpC protein - Methanobacterium thermoautotrophicum (strain Marburg) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS F40362 REFERENCE A40362 !$#authors Meile, L.; Stettler, R.; Banholzer, R.; Kotik, M.; !1Leisinger, T. !$#journal J. Bacteriol. (1991) 173:5017-5023 !$#title Tryptophan gene cluster of Methanobacterium !1thermoautotrophicum Marburg: molecular cloning and !1nucleotide sequence of a putative trpEGCFBAD operon. !$#cross-references MUID:91317718; PMID:1860817 !$#accession F40362 !'##status preliminary !'##molecule_type DNA !'##residues 1-274 ##label MEI !'##cross-references GB:M65060; NID:g149744; PIDN:AAA73030.1; !1PID:g149747 CLASSIFICATION #superfamily indole-3-glycerol-phosphate synthase; trpC !1homology FEATURE !$3-250 #domain trpC homology #label TRC SUMMARY #length 274 #molecular-weight 30403 #checksum 8177 SEQUENCE /// ENTRY S50179 #type complete TITLE indole-3-glycerol-phosphate synthase - Sulfolobus solfataricus ORGANISM #formal_name Sulfolobus solfataricus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S50179 REFERENCE S50179 !$#authors Andreotti, G.; Tutino, M.L.; Sannia, G.; Marino, G.; !1Cubellis, M.V. !$#journal Biochim. Biophys. Acta (1994) 1208:310-315 !$#title Indole-3-glycerol-phosphate synthase from Sulfolobus !1solfataricus as a model for studying thermostable TIM-barrel !1enzymes. !$#cross-references MUID:95035032; PMID:7947963 !$#accession S50179 !'##status preliminary !'##molecule_type DNA !'##residues 1-248 ##label AND CLASSIFICATION #superfamily indole-3-glycerol-phosphate synthase; trpC !1homology FEATURE !$1-248 #domain trpC homology #label TRC SUMMARY #length 248 #molecular-weight 28562 #checksum 9526 SEQUENCE /// ENTRY S35127 #type complete TITLE indole-3-glycerol-phosphate synthase (EC 4.1.1.48) - Lactococcus lactis subsp. lactis ORGANISM #formal_name Lactococcus lactis subsp. lactis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Aug-2001 ACCESSIONS S35127; C86808 REFERENCE S35123 !$#authors Bardowski, J.; Ehrlich, S.D.; Chopin, A. !$#journal J. Bacteriol. (1992) 174:6563-6570 !$#title Tryptophan biosynthesis genes in Lactococcus lactis subsp. !1lactis. !$#cross-references MUID:93015708; PMID:1400208 !$#accession S35127 !'##molecule_type DNA !'##residues 1-264 ##label BAR !'##cross-references EMBL:M87483; NID:g149514; PIDN:AAA25226.1; !1PID:g149519 REFERENCE A86625 !$#authors Bolotin, A.; Wincker, P.; Mauger, S.; Jaillon, O.; Malarme, !1K.; Weissenbach, J.; Ehrlich, S.D.; Sorokin, A. !$#journal Genome Res. (2001) 11:731-753 !$#title The complete genome sequence of the lactic acid bacterium !1Lactococcus lactis ssp. lactis IL1403. !$#cross-references MUID:21235186; PMID:11337471 !$#accession C86808 !'##status preliminary !'##molecule_type DNA !'##residues 1-264 ##label STO !'##cross-references GB:AE005176; PID:g12724460; PIDN:AAK05565.1; !1GSPDB:GN00146 !'##experimental_source strain IL1403 GENETICS !$#gene trpC CLASSIFICATION #superfamily indole-3-glycerol-phosphate synthase; trpC !1homology KEYWORDS carbon-carbon lyase; carboxy-lyase; tryptophan biosynthesis FEATURE !$8-255 #domain trpC homology #label TRC SUMMARY #length 264 #molecular-weight 29732 #checksum 5121 SEQUENCE /// ENTRY F64414 #type complete TITLE indole-3-glycerol-phosphate synthase (EC 4.1.1.48) - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F64414 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession F64414 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-266 ##label BUL !'##cross-references GB:U67535; GB:L77117; NID:g2826348; !1PIDN:AAB98923.1; PID:g1591591; TIGR:MJ0918 GENETICS !$#map_position REV850478-849678 CLASSIFICATION #superfamily indole-3-glycerol-phosphate synthase; trpC !1homology KEYWORDS carbon-carbon lyase; carboxy-lyase FEATURE !$3-263 #domain trpC homology #label TRC SUMMARY #length 266 #molecular-weight 30027 #checksum 1097 SEQUENCE /// ENTRY S59047 #type complete TITLE indole-3-glycerol phosphate synthase - Thermotoga maritima (strain MSB8) ORGANISM #formal_name Thermotoga maritima DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S59047; B72414 REFERENCE S59045 !$#authors Sterner, R.; Dahm, A.; Darimont, B.; Ivens, A.; Liebl, W.; !1Kirschner, K. !$#journal EMBO J. (1995) 14:4395-4402 !$#title (beta-alpha)(8)-barrel Proteins of tryptophan biosynthesis !1in the hyperthermophile Thermotoga maritima. !$#cross-references MUID:96003619; PMID:7556082 !$#accession S59047 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-252 ##label STE !'##cross-references GB:X92729; NID:g1054858; PIDN:CAA63389.1; !1PID:g3980232 REFERENCE A72200 !$#authors Nelson, K.E.; Clayton, R.A.; Gill, S.R.; Gwinn, M.L.; !1Dodson, R.J.; Haft, D.H.; Hickey, E.K.; Peterson, J.D.; !1Nelson, W.C.; Ketchum, K.A.; McDonald, L.; Utterback, T.R.; !1Malek, J.A.; Linher, K.D.; Garrett, M.M.; Stewart, A.M.; !1Cotton, M.D.; Pratt, M.S.; Phillips, C.A.; Richardson, D.; !1Heidelberg, J.; Sutton, G.G.; Fleischmann, R.D.; White, O.; !1Salzberg, S.L.; Smith, H.O.; Venter, J.C.; Fraser, C.M. !$#journal Nature (1999) 399:323-329 !$#title Evidence for lateral gene transfer between Archaea and !1Bacteria from genome sequence of Thermotoga maritima. !$#cross-references MUID:99287316; PMID:10360571 !$#accession B72414 !'##molecule_type DNA !'##residues 'M',24-225,'N',227-252 ##label ARN !'##cross-references GB:AE001699; GB:AE000512; NID:g4980622; !1PIDN:AAD35233.1; PID:g4980632; TIGR:TM0140 !'##experimental_source strain MSB8 !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing GENETICS !$#gene trpC; TM0140 !$#start_codon ATC CLASSIFICATION #superfamily indole-3-glycerol-phosphate synthase; trpC !1homology FEATURE !$3-247 #domain trpC homology #label TRC SUMMARY #length 252 #molecular-weight 28674 #checksum 9919 SEQUENCE /// ENTRY S76016 #type complete TITLE hypothetical protein - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S76016 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76016 !'##status preliminary !'##molecule_type DNA !'##residues 1-295 ##label KAN !'##cross-references EMBL:D64006; GB:AB001339; NID:g1001291; !1PIDN:BAA10863.1; PID:g1001373 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily indole-3-glycerol-phosphate synthase; trpC !1homology FEATURE !$31-291 #domain trpC homology #label TRC SUMMARY #length 295 #molecular-weight 32952 #checksum 867 SEQUENCE /// ENTRY ISBYN #type complete TITLE phosphoribosylanthranilate isomerase (EC 5.3.1.24) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YD8119.13A; protein YD8119.13B; protein YDR007w ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1981 #sequence_revision 31-Mar-1981 #text_change 21-Jul-2000 ACCESSIONS A01135; S50988; S50989 REFERENCE A01135 !$#authors Tschumper, G.; Carbon, J. !$#journal Gene (1980) 10:157-166 !$#title Sequence of a yeast DNS fragment containing a chromosomal !1replicator and the TRP1 gene. !$#cross-references MUID:80225748; PMID:6248420 !$#accession A01135 !'##molecule_type DNA !'##residues 1-224 ##label TSC !'##cross-references EMBL:V01341 REFERENCE S50976 !$#authors Murphy, L.; Richards, C.; Gentles, S.; Harris, D. !$#submission submitted to the EMBL Data Library, January 1995 !$#accession S50988 !'##molecule_type DNA !'##residues 1-57,'S',59-66 ##label MUR !'##cross-references EMBL:Z48008; NID:g642799; PIDN:CAA88067.1; !1PID:g642812; GSPDB:GN00004; MIPS:YDR007w !'##note due to an ochre mutation the TRP1 gene is split into two parts !1in this strain !$#accession S50989 !'##molecule_type DNA !'##residues 68-224 ##label MUW !'##cross-references EMBL:Z48008; NID:g642799; PIDN:CAA88068.1; !1PID:g1326006 !'##note due to an ochre mutation the TRP1 gene is split into two parts !1in this strain GENETICS !$#gene SGD:TRP1; MIPS:YDR007w !'##cross-references SGD:S0002414; MIPS:YDR007w !$#map_position 4R CLASSIFICATION #superfamily phosphoribosylanthranilate isomerase; trpF !1homology KEYWORDS intramolecular oxidoreductase; isomerase; tryptophan !1biosynthesis FEATURE !$15-222 #domain trpF homology #label TRF SUMMARY #length 224 #molecular-weight 24158 #checksum 4881 SEQUENCE /// ENTRY ISVKNL #type complete TITLE phosphoribosylanthranilate isomerase (EC 5.3.1.24) - yeast (Kluyveromyces marxianus var. lactis) ORGANISM #formal_name Kluyveromyces marxianus var. lactis, Candida sphaerica DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 18-Jun-1999 ACCESSIONS S07893 REFERENCE S07892 !$#authors Stark, M.J.R.; Milner, J.S. !$#journal Yeast (1989) 5:35-50 !$#title Cloning and analysis of the Kluyveromyces lactis TRP1 gene: !1a chromosomal locus flanked by genes encoding inorganic !1pyrophosphatase and histone H3. !$#cross-references MUID:89189093; PMID:2538971 !$#accession S07893 !'##molecule_type DNA !'##residues 1-210 ##label STA !'##cross-references EMBL:X14230; NID:g2900; PIDN:CAA32445.1; PID:g2902 GENETICS !$#gene TRP1 CLASSIFICATION #superfamily phosphoribosylanthranilate isomerase; trpF !1homology KEYWORDS intramolecular oxidoreductase; isomerase; tryptophan !1biosynthesis FEATURE !$4-208 #domain trpF homology #label TRF SUMMARY #length 210 #molecular-weight 22880 #checksum 6201 SEQUENCE /// ENTRY D22794 #type complete TITLE phosphoribosylanthranilate isomerase (EC 5.3.1.24) - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 29-Aug-1987 #sequence_revision 26-Apr-1996 #text_change 16-Jun-2000 ACCESSIONS D22794; D69726 REFERENCE A91520 !$#authors Henner, D.J.; Band, L.; Shimotsu, H. !$#journal Gene (1985) 34:169-177 !$#title Nucleotide sequence of the Bacillus subtilis tryptophan !1operon. !$#cross-references MUID:85232062; PMID:3924737 !$#accession D22794 !'##molecule_type DNA !'##residues 1-215 ##label HEN !'##cross-references GB:K01391; NID:g143767; PIDN:AAA22868.1; !1PID:g143771 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D69726 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-215 ##label KUN !'##cross-references GB:Z99115; GB:AL009126; NID:g2634478; !1PIDN:CAB14181.1; PID:g2634683 !'##experimental_source strain 168 GENETICS !$#gene trpF !$#map_position 205 (degrees) CLASSIFICATION #superfamily phosphoribosylanthranilate isomerase; trpF !1homology KEYWORDS intramolecular oxidoreductase; isomerase; tryptophan !1biosynthesis FEATURE !$7-207 #domain trpF homology #label TRF SUMMARY #length 215 #molecular-weight 24005 #checksum 671 SEQUENCE /// ENTRY PN0501 #type fragment TITLE phosphoribosylanthranilate isomerase (EC 5.3.1.24) - Bacillus amyloliquefaciens (fragment) ORGANISM #formal_name Bacillus amyloliquefaciens #note Bacillus amyloliquefaciens is synonym of K strain of Bacillus subtilis DATE 31-Dec-1993 #sequence_revision 26-Apr-1996 #text_change 26-Feb-1999 ACCESSIONS PN0501 REFERENCE JN0593 !$#authors Kurahashi, O.; Kawashima, H.; Nakamori, S.; Yamane, K. !$#journal Biosci. Biotechnol. Biochem. (1993) 57:1006-1009 !$#title Cloning and nucleotide sequence of the Bacillus subtilis K !1trpB gene encoding tryptophan synthase beta-subunit. !$#cross-references MUID:93344575; PMID:7763866 !$#accession PN0501 !'##molecule_type DNA !'##residues 1-136 ##label KUR !'##cross-references DDBJ:D14069 !'##note the authors translated the codon GAG for residue 9 as Gly and !1GAA for residue 111 as Gly GENETICS !$#gene trpF CLASSIFICATION #superfamily phosphoribosylanthranilate isomerase; trpF !1homology KEYWORDS intramolecular oxidoreductase; isomerase; tryptophan !1biosynthesis FEATURE !$1-136 #domain trpF homology (fragment) #label TRF SUMMARY #length 136 #checksum 9919 SEQUENCE /// ENTRY WZEC #type complete TITLE tryptophanase (EC 4.1.99.1) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 14-Nov-1983 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS E65173; A91789; I41097; I69358; A01136 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65173 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-476 ##label BLAT !'##cross-references GB:AE000448; GB:U00096; NID:g1790142; !1PIDN:AAC76731.1; PID:g1790144; UWGP:b3708 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A91789 !$#authors Deeley, M.C.; Yanofsky, C. !$#journal J. Bacteriol. (1981) 147:787-796 !$#title Nucleotide sequence of the structural gene for tryptophanase !1of Escherichia coli K-12. !$#cross-references MUID:82007678; PMID:6268608 !$#accession A91789 !'##molecule_type DNA !'##residues 6-141,'T',143,'QG',146-383,'TG',386-476 ##label DEE !'##experimental_source strain K-12 !'##note the authors translated the codons GAT, ACG, and CAG for !1residues 142, 144, and 145 as Thr, Gln, and Gly, !1respectively REFERENCE A92100 !$#authors Kagamiyama, H.; Matsubara, H.; Snell, E.E. !$#journal J. Biol. Chem. (1972) 247:1576-1586 !$#title The chemical structure of tryptophanase from Escherichia !1coli. III. Isolation and amino acid sequence of the tryptic !1peptides. !$#cross-references MUID:72134434; PMID:4551944 !$#contents annotation; sequences of tryptic peptides; strain K-12 !$#note Lys-275 binds pyridoxal 5'-phosphate REFERENCE I41097 !$#authors Tokushige, M.; Tsujimoto, N.; Oda, T.; Honda, T.; Yumoto, !1N.; Ito, S.; Yamamoto, M.; Kim, E.H.; Hiragi, Y. !$#journal Biochimie (1989) 71:711-720 !$#title Role of cysteine residues in tryptophanase for monovalent !1cation-induced activation. !$#cross-references MUID:89323226; PMID:2502187 !$#accession I41097 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 6-383,'TG',386-476 ##label RES !'##cross-references EMBL:X15974; NID:g41935; PIDN:CAA34096.1; !1PID:g41936 REFERENCE I54862 !$#authors Stewart, V.J.; Yanofsky, C. !$#journal J. Bacteriol. (1985) 164:731-740 !$#title Evidence for transcription antitermination control of !1tryptophanase operon expression in Escherichia coli K-12. !$#cross-references MUID:86033634; PMID:3902796 !$#accession I69358 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 6-27 ##label RE2 !'##cross-references GB:M11990; NID:g147999; PIDN:AAA24679.1; !1PID:g148001 GENETICS !$#gene tnaA !$#map_position 83 min COMPLEX homotetramer FUNCTION !$#description catalyzes the degradation of tryptophan to indole, pyruvate, !1and ammonia; it also catalyzes the synthesis of tryptophan !1from indole and serine CLASSIFICATION #superfamily tryptophanase KEYWORDS carbon-carbon lyase; homotetramer SUMMARY #length 476 #molecular-weight 53410 #checksum 8080 SEQUENCE /// ENTRY B44038 #type complete TITLE tryptophanase (EC 4.1.99.1) - Proteus vulgaris ALTERNATE_NAMES tryptophan indole-lyase ORGANISM #formal_name Proteus vulgaris DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B44038 REFERENCE A44038 !$#authors Kamath, A.V.; Yanofsky, C. !$#journal J. Biol. Chem. (1992) 267:19978-19985 !$#title Characterization of the tryptophanase operon of Proteus !1vulgaris. Cloning, nucleotide sequence, amino acid homology, !1and in vitro synthesis of the leader peptide and regulatory !1analysis. !$#cross-references MUID:93015858; PMID:1400314 !$#accession B44038 !'##status preliminary !'##molecule_type DNA !'##residues 1-467 ##label KAM !'##cross-references GB:M93277; NID:g150910; PIDN:AAA25664.1; !1PID:g150912 !'##note sequence extracted from NCBI backbone (NCBIP:115637) GENETICS !$#gene tnaA CLASSIFICATION #superfamily tryptophanase KEYWORDS carbon-carbon lyase SUMMARY #length 467 #molecular-weight 52490 #checksum 829 SEQUENCE /// ENTRY A49493 #type complete TITLE tyrosine phenol-lyase (EC 4.1.99.2) - Citrobacter freundii ORGANISM #formal_name Citrobacter freundii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A49493 REFERENCE A49493 !$#authors Antson, A.A.; Demidkina, T.V.; Gollnick, P.; Dauter, Z.; von !1Tersch, R.L.; Long, J.; Berezhnoy, S.N.; Phillips, R.S.; !1Harutyunyan, E.H.; Wilson, K.S. !$#journal Biochemistry (1993) 32:4195-4206 !$#title Three-dimensional structure of tyrosine phenol-lyase. !$#cross-references MUID:93237225; PMID:7916622 !$#accession A49493 !'##status preliminary !'##molecule_type DNA; protein !'##residues 1-456 ##label ANT !'##experimental_source ATCC 29063 !'##note sequence extracted from NCBI backbone (NCBIN:130224, !1NCBIP:130225) CLASSIFICATION #superfamily tryptophanase KEYWORDS carbon-carbon lyase SUMMARY #length 456 #molecular-weight 51382 #checksum 9347 SEQUENCE /// ENTRY WZECD #type complete TITLE deoxyribodipyrimidine photo-lyase (EC 4.1.99.3) [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES DNA photolyase; photoreactivating enzyme ORGANISM #formal_name Escherichia coli DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 01-Mar-2002 ACCESSIONS A01137; C64806; T48920 REFERENCE A01137 !$#authors Sancar, G.B.; Smith, F.W.; Lorence, M.C.; Rupert, C.S.; !1Sancar, A. !$#journal J. Biol. Chem. (1984) 259:6033-6038 !$#title Sequences of the Escherichia coli photolyase gene and !1protein. !$#cross-references MUID:84185763; PMID:6325460 !$#accession A01137 !'##molecule_type DNA !'##residues 1-472 ##label SAN !'##cross-references GB:K01299; NID:g147266; PIDN:AAA24388.1; !1PID:g147268 !'##note part of this sequence was confirmed by protein sequencing REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64806 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-472 ##label BLAT !'##cross-references GB:AE000174; GB:U00096; NID:g1786920; !1PIDN:AAC73802.1; PID:g1786926; UWGP:b0708 !'##experimental_source strain K-12, substrain MG1655 REFERENCE Z25006 !$#authors Oshima, T.; Aiba, H.; Baba, T.; Fujita, K.; Hayashi, K.; !1Honjo, A.; Ikemoto, K.; Inada, T.; Itoh, T.; Kajihara, M.; !1Kanai, K.; Kashimoto, K.; Kimura, S.; Kitagawa, M.; Makino, !1K.; Masuda, S.; Miki, T.; Mizobuchi, K.; Mori, H.; Motomura, !1K.; Nakamura, Y.; Nashimoto, H.; Nishio, Y.; Saito, N.; !1Sampei, G.; Seki, Y.; Tagami, H.; Takemoto, K.; Wada, C.; !1Yamamoto, Y.; Yano, M.; Horiuchi, T. !$#journal DNA Res. (1996) 3:137-155 !$#title A 718-kb DNA Sequence of Escherichia coli K-12 Genome !1Corresponding to the 12.7-28.0 min Region on the Linkage !1Map. !$#cross-references MUID:97061202; PMID:8905232 !$#accession T48920 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-472 ##label OSH !'##cross-references EMBL:D90709; NID:g1651305; PIDN:BAA35367.1; !1PID:g1651311 !'##experimental_source strain K12; Kohara clone 174 GENETICS !$#gene phrB; phr !$#map_position 15.7-16.0 FUNCTION !$#description EC 4.1.99.3 [validated, MUID:92204121]; DNA repair; !1catalyzes the light-dependent (300-600 nm) monomerization of !1cyclobutyl pyrimidine dimers (in cis-syn configuration), !1which are formed between adjacent bases on the same DNA !1strand, upon exposure to ultraviolet radiation CLASSIFICATION #superfamily deoxyribodipyrimidine photo-lyase KEYWORDS carbon-carbon lyase; DNA binding; DNA repair; flavoprotein SUMMARY #length 472 #molecular-weight 53667 #checksum 7265 SEQUENCE /// ENTRY SYFUTP #type complete TITLE trichodiene synthase (EC 4.2.3.6) - fungus (Fusarium sporotrichioides) ALTERNATE_NAMES sesquiterpene cyclase ORGANISM #formal_name Fusarium sporotrichioides DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 21-Jun-2002 ACCESSIONS JU0064 REFERENCE JU0064 !$#authors Hohn, T.M.; Beremand, P.D. !$#journal Gene (1989) 79:131-138 !$#title Isolation and nucleotide sequence of a sesquiterpene cyclase !1gene from the trichothecene-producing fungus Fusarium !1sporotrichioides. !$#cross-references MUID:89378769; PMID:2777086 !$#accession JU0064 !'##molecule_type DNA !'##residues 1-374 ##label HOH !'##cross-references GB:M27246; NID:g4249364; PIDN:AAD13657.1; !1PID:g168160 !'##note amino-terminal sequences from six CNBr peptides were also !1determined COMMENT The trichothecenes are a family of toxic sesquiterpenes !1produced by members of at least eight genera of fungi and by !1the plant genus Baccharis. COMMENT Trichodiene synthase catalyzes the isomerization and !1cyclization of farnesyl pyrophosphate to form trichodiene. GENETICS !$#gene Tox5 !$#introns 157/1 CLASSIFICATION #superfamily trichodiene synthase KEYWORDS carbon-carbon lyase; carbon-oxygen lyase SUMMARY #length 374 #molecular-weight 43999 #checksum 9943 SEQUENCE /// ENTRY G46665 #type complete TITLE dipicolinate synthase chain A - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 03-May-1994 #sequence_revision 06-Feb-1995 #text_change 16-Jun-2000 ACCESSIONS G46665; S35651; F69715; S34597 REFERENCE A46665 !$#authors Chen, N.Y.; Jiang, S.Q.; Klein, D.A.; Paulus, H. !$#journal J. Biol. Chem. (1993) 268:9448-9465 !$#title Organization and nucleotide sequence of the Bacillus !1subtilis diaminopimelate operon, a cluster of genes encoding !1the first three enzymes of diaminopimelate synthesis and !1dipicolinate synthase. !$#cross-references MUID:93252813; PMID:8098035 !$#accession G46665 !'##molecule_type DNA !'##residues 1-297 ##label CHE !'##cross-references EMBL:L08471; NID:g142823; PIDN:AAA22381.1; !1PID:g142826 REFERENCE S35651 !$#authors Daniel, R.A.; Errington, J. !$#journal J. Mol. Biol. (1993) 232:468-483 !$#title Cloning, DNA sequence, functional analysis and !1transcriptional regulation of the genes encoding dipicolinic !1acid synthetase required for sporulation in Bacillus !1subtilis. !$#cross-references MUID:93347235; PMID:8345520 !$#accession S35651 !'##molecule_type DNA !'##residues 1-297 ##label DAN !'##cross-references EMBL:Z22554; NID:g296144; PIDN:CAA80274.1; !1PID:g296145 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69715 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-297 ##label KUN !'##cross-references GB:Z99112; GB:AL009126; NID:g2633902; !1PIDN:CAB13546.1; PID:g2634045 !'##experimental_source strain 168 COMMENT This enzyme is expressed late in sporulation, predominantly !1in the mother cell compartment. It synthesizes dipicolinic !1acid, a substance that accumlates in the prespore to confer !1spore heat resistance. It is negatively regulated by GerE !1(PIR:C27893). GENETICS !$#gene spoVFA CLASSIFICATION #superfamily dipicolinate synthase chain A KEYWORDS sporulation SUMMARY #length 297 #molecular-weight 31948 #checksum 92 SEQUENCE /// ENTRY F46665 #type complete TITLE dipicolinate synthase chain B - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 03-May-1994 #sequence_revision 06-Feb-1995 #text_change 16-Jun-2000 ACCESSIONS F46665; S35652; G69715; S34598 REFERENCE A46665 !$#authors Chen, N.Y.; Jiang, S.Q.; Klein, D.A.; Paulus, H. !$#journal J. Biol. Chem. (1993) 268:9448-9465 !$#title Organization and nucleotide sequence of the Bacillus !1subtilis diaminopimelate operon, a cluster of genes encoding !1the first three enzymes of diaminopimelate synthesis and !1dipicolinate synthase. !$#cross-references MUID:93252813; PMID:8098035 !$#accession F46665 !'##molecule_type DNA !'##residues 1-200 ##label CHE !'##cross-references EMBL:L08471; NID:g142823; PIDN:AAA22382.1; !1PID:g142827 REFERENCE S35651 !$#authors Daniel, R.A.; Errington, J. !$#journal J. Mol. Biol. (1993) 232:468-483 !$#title Cloning, DNA sequence, functional analysis and !1transcriptional regulation of the genes encoding dipicolinic !1acid synthetase required for sporulation in Bacillus !1subtilis. !$#cross-references MUID:93347235; PMID:8345520 !$#accession S35652 !'##molecule_type DNA !'##residues 1-200 ##label DAN !'##cross-references EMBL:Z22554; NID:g296144; PIDN:CAA80275.1; !1PID:g296146 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69715 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-200 ##label KUN !'##cross-references GB:Z99112; GB:AL009126; NID:g2633902; !1PIDN:CAB13547.1; PID:g2634046 !'##experimental_source strain 168 COMMENT This enzyme is expressed late in sporulation, predominantly !1in the mother cell compartment. It synthesizes dipicolinic !1acid, a substance that accumlates in the prespore to confer !1spore heat resistance. It is negatively regulated by GerE !1(PIR:C27893). GENETICS !$#gene spoVFB CLASSIFICATION #superfamily dipicolinate synthase chain B KEYWORDS sporulation SUMMARY #length 200 #molecular-weight 21869 #checksum 183 SEQUENCE /// ENTRY SYSMPG #type complete TITLE dTDP-dihydrostreptose synthase - Streptomyces griseus ORGANISM #formal_name Streptomyces griseus DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 18-Jun-1999 ACCESSIONS S18618; S19783 REFERENCE S18617 !$#authors Pissowotzki, K.; Mansouri, K.; Piepersberg, W. !$#journal Mol. Gen. Genet. (1991) 231:113-123 !$#title Genetics of streptomycin production in Streptomyces griseus: !1molecular structure and putative function of genes !1strELMB2N. !$#cross-references MUID:92092953; PMID:1661369 !$#accession S18618 !'##molecule_type DNA !'##residues 1-304 ##label PIS !'##cross-references EMBL:X62567; NID:g49009; PIDN:CAA44443.1; !1PID:g49013 GENETICS !$#gene strL CLASSIFICATION #superfamily dTDP-dihydrostreptose synthase KEYWORDS streptomycin biosynthesis SUMMARY #length 304 #molecular-weight 32214 #checksum 761 SEQUENCE /// ENTRY CRHU1 #type complete TITLE carbonate dehydratase (EC 4.2.1.1) I [validated] - human ALTERNATE_NAMES carbonic anhydrase I ORGANISM #formal_name Homo sapiens #common_name man DATE 07-May-1981 #sequence_revision 05-May-1995 #text_change 08-Dec-2000 ACCESSIONS JQ0786; A26573; A90668; A90180; A92128; B92147; A01138 REFERENCE JQ0786 !$#authors Lowe, N.; Brady, H.J.M.; Barlow, J.H.; Sowden, J.C.; !1Edwards, M.; Butterworth, P.H.W. !$#journal Gene (1990) 93:277-283 !$#title Structure and methylation patterns of the gene encoding !1human carbonic anhydrase I. !$#cross-references MUID:91033039; PMID:2121614 !$#accession JQ0786 !'##molecule_type DNA !'##residues 1-261 ##label LOW !'##cross-references GB:M33987; NID:g179792; PIDN:AAA51910.1; !1PID:g179793 !'##experimental_source erythrocyte REFERENCE A26573 !$#authors Barlow, J.H.; Lowe, N.; Edwards, Y.H.; Butterworth, P.H.W. !$#journal Nucleic Acids Res. (1987) 15:2386 !$#title Human carbonic anhydrase I cDNA. !$#cross-references MUID:87174760; PMID:3104879 !$#accession A26573 !'##molecule_type mRNA !'##residues 1-261 ##label BAR !'##cross-references GB:X05014; NID:g29599; PIDN:CAA28663.1; PID:g29600 !'##note the authors translated the codon GAG for residue 118 as Gly REFERENCE A90668 !$#authors Giraud, N.; Marriq, C.; Laurent-Tabusse, G. !$#journal Biochimie (1974) 56:1031-1043 !$#title Structure primaire de l'anhydrase carbonique erythrocytaire !1B humaine. III. Sequence des fragments ICNBr et IIICNBr !1(residus 149-260). !$#cross-references MUID:75091068; PMID:4217196 !$#accession A90668 !'##molecule_type protein !'##residues 2-74,'ND',77-261 ##label GIR REFERENCE A90180 !$#authors Andersson, B.; Nyman, P.O.; Strid, L. !$#journal Biochem. Biophys. Res. Commun. (1972) 48:670-677 !$#title Amino acid sequence of human erythrocyte carbonic anhydrase !1B. !$#cross-references MUID:72243008; PMID:4625868 !$#accession A90180 !'##molecule_type protein !'##residues 20-74,'ND',77-261 ##label AND REFERENCE A92128 !$#authors Lin, K.T.D.; Deutsch, H.F. !$#journal J. Biol. Chem. (1973) 248:1885-1893 !$#title Human carbonic anhydrases. XI. The complete primary !1structure of carbonic anhydrase B. !$#cross-references MUID:73134579; PMID:4632246 !$#accession A92128 !'##molecule_type protein !'##residues 12-26,'DQN',30-165,'E',167-261 ##label LIN !'##note this sequence has been revised in reference A92147 REFERENCE A92147 !$#authors Lin, K.T.D.; Deutsch, H.F. !$#journal J. Biol. Chem. (1974) 249:2329-2337 !$#title Human carbonic anhydrases. XII. The complete primary !1structure of the C isozyme. !$#cross-references MUID:74143468; PMID:4207120 !$#accession B92147 !'##molecule_type protein !'##residues 2-74,'ND',77-261 ##label LI2 REFERENCE A93803 !$#authors Kannan, K.K.; Notstrand, B.; Fridborg, K.; Lovgren, S.; !1Ohlsson, A.; Petef, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1975) 72:51-55 !$#title Crystal structure of human erythrocyte carbonic anhydrase B. !1Three-dimensional structure at a nominal 2.2-angstrom !1resolution. !$#cross-references MUID:75120492; PMID:804171 !$#contents annotation; X-ray crystallography, 2.2 angstroms GENETICS !$#gene GDB:CA1 !'##cross-references GDB:119047; OMIM:114800 !$#map_position 8q13-8q22.1 !$#introns 13/1; 79/1; 118/3; 150/3; 171/3; 223/3 !$#note the first intron occurs before the initiator codon FUNCTION !$#description catalyzes the reversible dissociation of carbonic acid to !1carbon dioxide and water !$#note this form is predominantly expressed in erythrocytes CLASSIFICATION #superfamily carbonate dehydratase; carbonic anhydrase !1homology KEYWORDS acetylated amino end; carbon-oxygen lyase; hydro-lyase; !1metalloprotein; zinc FEATURE !$2-261 #product carbonate dehydratase I #status experimental !8#label MAT\ !$6-261 #domain carbonic anhydrase homology #label CAH\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental\ !$95,97,120 #binding_site zinc (His) #status experimental SUMMARY #length 261 #molecular-weight 28870 #checksum 1218 SEQUENCE /// ENTRY CRMQ1R #type complete TITLE carbonate dehydratase (EC 4.2.1.1) I - rhesus macaque (tentative sequence) ALTERNATE_NAMES carbonic anhydrase I ORGANISM #formal_name Macaca mulatta #common_name rhesus macaque DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 31-Mar-2000 ACCESSIONS A01139 REFERENCE A01139 !$#authors Henriksson, D.; Tanis, R.J.; Tashian, R.E. !$#journal Biochem. Biophys. Res. Commun. (1980) 96:135-142 !$#title The amino acid sequence of carbonic anhydrase I from the !1Rhesus macaque. !$#cross-references MUID:81062409; PMID:6776950 !$#accession A01139 !'##molecule_type protein !'##residues 1-260 ##label HEN CLASSIFICATION #superfamily carbonate dehydratase; carbonic anhydrase !1homology KEYWORDS acetylated amino end; carbon-oxygen lyase; hydro-lyase; zinc FEATURE !$5-260 #domain carbonic anhydrase homology #label CAH\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$94,96,119 #binding_site zinc (His) #status predicted SUMMARY #length 260 #molecular-weight 28805 #checksum 9857 SEQUENCE /// ENTRY CRHO1D #type complete TITLE carbonate dehydratase (EC 4.2.1.1) I - horse ALTERNATE_NAMES carbonic anhydrase I ORGANISM #formal_name Equus caballus #common_name domestic horse DATE 22-May-1981 #sequence_revision 22-May-1981 #text_change 11-Nov-1996 ACCESSIONS A01140 REFERENCE A01140 !$#authors Jabusch, J.R.; Bray, R.P.; Deutsch, H.F. !$#journal J. Biol. Chem. (1980) 255:9196-9204 !$#title Sequence of the low activity equine erythrocyte carbonic !1anhydrase and delineation of the amino acid substitutions in !1various polymorphic forms. !$#cross-references MUID:81006999; PMID:6773961 !$#contents D isozyme !$#accession A01140 !'##molecule_type protein !'##residues 1-260 ##label JAB !'##note 65-Gly, 115-His, 157-Gly, 212-Tyr, and 224-Ala were also found !1in the electrophoretically homogeneous D isozyme; the T !1isozyme has 54-Asp; the A2 isozyme has 81-Gly, 82-Cys, and !183-Phe; the A1 isozyme has 183-Arg; and the B isozyme has !1183-Arg and 222-Arg CLASSIFICATION #superfamily carbonate dehydratase; carbonic anhydrase !1homology KEYWORDS carbon-oxygen lyase; hydro-lyase; zinc FEATURE !$5-260 #domain carbonic anhydrase homology #label CAH\ !$94,96,119 #binding_site zinc (His) #status predicted SUMMARY #length 260 #molecular-weight 28895 #checksum 1014 SEQUENCE /// ENTRY CRHU2 #type complete TITLE carbonate dehydratase (EC 4.2.1.1) II [validated] - human ALTERNATE_NAMES carbonic anhydrase II; hepatic carbonic anhydrase ORGANISM #formal_name Homo sapiens #common_name man DATE 07-May-1981 #sequence_revision 05-May-1995 #text_change 15-Sep-2000 ACCESSIONS A27175; A23202; A92194; A92147; I37214; I51863; I51871; !1A01141 REFERENCE A27175 !$#authors Murakami, H.; Marelich, G.P.; Grubb, J.H.; Kyle, J.W.; Sly, !1W.S. !$#journal Genomics (1987) 1:159-166 !$#title Cloning, expression, and sequence homologies of cDNA for !1human carbonic anhydrase II. !$#cross-references MUID:88085190; PMID:3121496 !$#accession A27175 !'##molecule_type mRNA !'##residues 1-260 ##label MUR !'##cross-references GB:J03037; NID:g179771; PIDN:AAA51908.1; !1PID:g179772 REFERENCE A90655 !$#authors Venta, P.J.; Montgomery, C.; Hewett-Emmett, D.; Tashian, !1R.E. !$#journal Biochim. Biophys. Acta (1985) 826:195-201 !$#title Comparison of the 5' regions of human and mouse carbonic !1anhydrase II genes and identification of possible regulatory !1elements. !$#cross-references MUID:86077780; PMID:3000449 !$#accession A23202 !'##molecule_type DNA !'##residues 1-77 ##label VEN !'##cross-references GB:X03251; GB:M18100; GB:M77181; NID:g179778; !1PIDN:AAA51909.1; PID:g179780 REFERENCE A92194 !$#authors Henderson, L.E.; Henriksson, D.; Nyman, P.O. !$#journal J. Biol. Chem. (1976) 251:5457-5463 !$#title The primary structure of human carbonic anhydrase C. !$#cross-references MUID:77006079; PMID:823150 !$#accession A92194 !'##molecule_type protein !'##residues 2-260 ##label HEN REFERENCE A92147 !$#authors Lin, K.T.D.; Deutsch, H.F. !$#journal J. Biol. Chem. (1974) 249:2329-2337 !$#title Human carbonic anhydrases. XII. The complete primary !1structure of the C isozyme. !$#cross-references MUID:74143468; PMID:4207120 !$#accession A92147 !'##molecule_type protein !'##residues 2-260 ##label LIN REFERENCE I37214 !$#authors Montgomery, J.C.; Venta, P.J.; Tashian, R.E.; Hewett-Emmett, !1D. !$#journal Nucleic Acids Res. (1987) 15:4687 !$#title Nucleotide sequence of human liver carbonic anhydrase II !1cDNA. !$#cross-references MUID:87231043; PMID:3108857 !$#accession I37214 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-260 ##label RE3 !'##cross-references EMBL:Y00339; NID:g29586; PIDN:CAA68426.1; !1PID:g29587 !'##experimental_source liver !'##note submitted to the EMBL/GenBank/DDBJ databases by David !1Hewett-Emmett 01-JUL-1987 REFERENCE I51863 !$#authors Venta, P.J.; Welty, R.J.; Johnson, T.M.; Sly, W.S.; Tashian, !1R.E. !$#journal Am. J. Hum. Genet. (1991) 49:1082-1090 !$#title Carbonic anhydrase II deficiency syndrome in a Belgian !1family is caused by a point mutation at an invariant !1histidine residue (107 His->Tyr): complete structure of the !1normal human CA II gene. !$#cross-references MUID:92026087; PMID:1928091 !$#accession I51863 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-260 ##label RES !'##cross-references GB:M77181; NID:g179778; PIDN:AAA51909.1; !1PID:g179780 !'##note the complete nucleotide sequence is not shown REFERENCE I51871 !$#authors Hu, P.Y.; Ernst, A.R.; Sly, W.S.; Venta, P.J.; Skaggs, L.A.; !1Tashian, R.E. !$#journal Am. J. Hum. Genet. (1994) 54:602-608 !$#title Carbonic anhydrase II deficiency: single-base deletion in !1exon 7 is the predominant mutation in Caribbean Hispanic !1patients. !$#cross-references MUID:94175074; PMID:8128957 !$#accession I51871 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 225-242 ##label RE2 !'##cross-references GB:S69526; NID:g545850; PIDN:AAB30170.1; !1PID:g545851 !'##note wild type shown; mutant contains frameshift after residue 226 REFERENCE A50085 !$#authors Eriksson, A.E.; Jones, T.A.; Liljas, A. !$#submission submitted to the Brookhaven Protein Data Bank, February 1989 !$#cross-references PDB:1CA2 !$#contents annotation; X-ray crystallography, 2.0 angstroms, residues !14-259 REFERENCE A93404 !$#authors Liljas, A.; Kannan, K.K.; Bergsten, P.C.; Waara, I.; !1Fridborg, K.; Strandberg, B.; Carlbom, U.; Jarup, L.; !1Lovgren, S.; Petef, M. !$#journal Nature New Biol. (1972) 235:131-137 !$#title Crystal structure of human carbonic anhydrase C. !$#cross-references MUID:72111787; PMID:4621826 !$#contents annotation; X-ray crystallography, 2.0 angstroms !$#note other residues at the active site are His-64, Asn-67, !1Tyr-127, Leu-197, Thr-198, and Thr-199 GENETICS !$#gene GDB:CA2 !'##cross-references GDB:119739; OMIM:259730 !$#map_position 8q13-8q22.1 !$#introns 12/1; 78/1; 117/3; 148/3; 169/3; 221/3 FUNCTION !$#description catalyzes the reversible dissociation of carbonic acid to !1carbon dioxide and water !$#note this form is expressed in erythrocytes and other tissues; !1deficiency of this form of the enzyme results in !1osteopetrosis with renal tubular acidosis and cerebral !1calcification CLASSIFICATION #superfamily carbonate dehydratase; carbonic anhydrase !1homology KEYWORDS acetylated amino end; carbon-oxygen lyase; hydro-lyase; !1metalloprotein; monomer; zinc FEATURE !$2-260 #product carbonate dehydratase II #status !8experimental #label MAT\ !$5-259 #domain carbonic anhydrase homology #label CAH\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental\ !$94,96,119 #binding_site zinc (His) #status experimental SUMMARY #length 260 #molecular-weight 29246 #checksum 8975 SEQUENCE /// ENTRY CRRB2 #type complete TITLE carbonate dehydratase (EC 4.2.1.1) II - rabbit (tentative sequence) ALTERNATE_NAMES carbonic anhydrase II ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 31-Mar-1981 #sequence_revision 31-Mar-1981 #text_change 31-Mar-2000 ACCESSIONS A01142 REFERENCE A01142 !$#authors Ferrell, R.E.; Stroup, S.K.; Tanis, R.J.; Tashian, R.E. !$#journal Biochim. Biophys. Acta (1978) 533:1-11 !$#title Amino acid sequence of rabbit carbonic anhydrase II. !$#cross-references MUID:78144871; PMID:416851 !$#accession A01142 !'##molecule_type protein !'##residues 1-259 ##label FER !'##note 203-Glu was also found CLASSIFICATION #superfamily carbonate dehydratase; carbonic anhydrase !1homology KEYWORDS acetylated amino end; carbon-oxygen lyase; hydro-lyase; zinc FEATURE !$4-258 #domain carbonic anhydrase homology #label CAH\ !$1 #modified_site acetylated amino end (Ser) #status !8experimental\ !$93,95,118 #binding_site zinc (His) #status predicted SUMMARY #length 259 #molecular-weight 29340 #checksum 6573 SEQUENCE /// ENTRY CRMS2 #type complete TITLE carbonate dehydratase (EC 4.2.1.1) II - mouse ALTERNATE_NAMES carbonic anhydrase II ORGANISM #formal_name Mus musculus #common_name house mouse DATE 25-Feb-1985 #sequence_revision 06-Feb-1995 #text_change 18-Jun-1999 ACCESSIONS A23900; B23202; A01143; A20539; I51949 REFERENCE A23900 !$#authors Venta, P.J.; Montgomery, J.C.; Hewett-Emmet, D.; Wiebauer, !1K.; Tashian, R.E. !$#journal J. Biol. Chem. (1985) 260:12130-12135 !$#title Structure and exon to protein domain relationships of the !1mouse carbonic anhydrase II gene. !$#cross-references MUID:86008276; PMID:2995362 !$#accession A23900 !'##molecule_type DNA !'##residues 1-260 ##label VEN !'##experimental_source strain YBR REFERENCE A90655 !$#authors Venta, P.J.; Montgomery, C.; Hewett-Emmett, D.; Tashian, !1R.E. !$#journal Biochim. Biophys. Acta (1985) 826:195-201 !$#title Comparison of the 5' regions of human and mouse carbonic !1anhydrase II genes and identification of possible regulatory !1elements. !$#cross-references MUID:86077780; PMID:3000449 !$#accession B23202 !'##molecule_type DNA !'##residues 1-77 ##label VE2 !'##note the authors translated the codon CAG for residue 39 as His REFERENCE A01143 !$#authors Curtis, P.J.; Withers, E.; Demuth, D.; Watt, R.; Venta, !1P.J.; Tashian, R.E. !$#journal Gene (1983) 25:325-332 !$#title The nucleotide sequence and derived amino acid sequence of !1cDNA coding for mouse carbonic anhydrase II. !$#cross-references MUID:84109569; PMID:6420240 !$#accession A01143 !'##molecule_type mRNA !'##residues 2-38,'H',40-260 ##label CUR !'##cross-references GB:K00811; GB:K00812; GB:M11830; NID:g192333; !1PIDN:AAA37356.1; PID:g309128 !'##note initiator Met not shown REFERENCE A20539 !$#authors Curtis, P.J. !$#journal J. Biol. Chem. (1983) 258:4459-4463 !$#title Cloning of mouse carbonic anhydrase mRNA and its induction !1in mouse erythroleukemic cells. !$#cross-references MUID:83161023; PMID:6187736 !$#accession A20539 !'##molecule_type mRNA !'##residues 155-178;214-240 ##label CU2 REFERENCE I51949 !$#authors Venta, P.J.; Montgomery, J.C.; Wiebauer, K.; Hewett-Emmett, !1D.; Tashian, R.E. !$#journal Ann. N. Y. Acad. Sci. (1984) 429:309-323 !$#title Organization of the mouse and human carbonic anhydrase II !1genes. !$#cross-references MUID:84255152; PMID:6331255 !$#accession I51949 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 241-260 ##label RES !'##cross-references GB:M25944; NID:g199078; PIDN:AAA39505.1; !1PID:g199079 GENETICS !$#gene Car-2 !$#introns 12/1; 78/1; 117/3; 144/1; 169/3; 221/3 CLASSIFICATION #superfamily carbonate dehydratase; carbonic anhydrase !1homology KEYWORDS carbon-oxygen lyase; hydro-lyase; zinc FEATURE !$5-259 #domain carbonic anhydrase homology #label CAH\ !$94,96,119 #binding_site zinc (His) #status predicted SUMMARY #length 260 #molecular-weight 29082 #checksum 6036 SEQUENCE /// ENTRY CRBO2 #type complete TITLE carbonate dehydratase (EC 4.2.1.1) II - bovine (tentative sequence) ALTERNATE_NAMES carbonic anhydrase II ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Mar-1981 #sequence_revision 31-Mar-1981 #text_change 31-Mar-2000 ACCESSIONS A01144 REFERENCE A90669 !$#authors Sciaky, M.; Limozin, N.; Filippi-Foveau, D.; Gulian, J.M.; !1Laurent-Tabusse, G. !$#journal Biochimie (1976) 58:1071-1082 !$#title Structure primaire de l'anhydrase carbonique erythrocytaire !1bovine CI. II. - Sequence complete. !$#cross-references MUID:77065798; PMID:826282 !$#accession A01144 !'##molecule_type protein !'##residues 1-259 ##label SCI REFERENCE A90672 !$#authors Gulian, J.M.; Limozin, N.; Mallet, B.; Di Costanzo, J.; !1Charrel, M. !$#journal Biochimie (1977) 59:293-302 !$#title Independance genetique de deux formes de l'anhydrase !1carbonique erythrocytaire bovine. !$#cross-references MUID:77242599; PMID:19093 !$#contents annotation !$#note one minor and two major forms were isolated !1chromatographically. One of the major forms differs in !1having 56-Gln CLASSIFICATION #superfamily carbonate dehydratase; carbonic anhydrase !1homology KEYWORDS acetylated amino end; carbon-oxygen lyase; hydro-lyase; zinc FEATURE !$4-258 #domain carbonic anhydrase homology #label CAH\ !$1 #modified_site acetylated amino end (Ser) #status !8experimental\ !$93,95,118 #binding_site zinc (His) #status predicted SUMMARY #length 259 #molecular-weight 28980 #checksum 7151 SEQUENCE /// ENTRY CRSH2 #type complete TITLE carbonate dehydratase (EC 4.2.1.1) II - sheep (tentative sequence) ALTERNATE_NAMES carbonic anhydrase II ORGANISM #formal_name Ovis orientalis aries, Ovis ammon aries #common_name domestic sheep DATE 31-Mar-1981 #sequence_revision 31-Mar-1981 #text_change 31-Mar-2000 ACCESSIONS A01145 REFERENCE A90598 !$#authors Tanis, R.J.; Ferrell, R.E.; Tashian, R.E. !$#journal Biochim. Biophys. Acta (1974) 371:534-548 !$#title Amino acid sequence of sheep carbonic anhydrase C. !$#cross-references MUID:75054988; PMID:4215456 !$#accession A01145 !'##molecule_type protein !'##residues 1-259 ##label TAN REFERENCE A90628 !$#authors Mallet, B.; Gulian, J.M.; Sciaky, M.; Laurent, G.; Charrel, !1M. !$#journal Biochim. Biophys. Acta (1979) 576:290-304 !$#title Formes moleculaires multiples de l'anhydrase carbonique !1erythrocytaire ovine. !$#cross-references MUID:79145542; PMID:106895 !$#contents annotation !$#note one minor and three major forms were isolated !1chromatographically. One of these differed from the others !1in having 35-Thr CLASSIFICATION #superfamily carbonate dehydratase; carbonic anhydrase !1homology KEYWORDS acetylated amino end; carbon-oxygen lyase; hydro-lyase; zinc FEATURE !$4-258 #domain carbonic anhydrase homology #label CAH\ !$1 #modified_site acetylated amino end (Ser) #status !8experimental\ !$93,95,118 #binding_site zinc (His) #status predicted SUMMARY #length 259 #molecular-weight 29080 #checksum 7402 SEQUENCE /// ENTRY CRHU3 #type complete TITLE carbonate dehydratase (EC 4.2.1.1) III - human ALTERNATE_NAMES carbonic anhydrase III; muscle carbonic anhydrase ORGANISM #formal_name Homo sapiens #common_name man DATE 05-Feb-1988 #sequence_revision 05-May-1995 #text_change 18-Jun-1999 ACCESSIONS A26658; A26690; A25850 REFERENCE A26658 !$#authors Wade, R.; Gunning, P.; Eddy, R.; Shows, T.; Kedes, L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:9571-9575 !$#title Nucleotide sequence, tissue-specific expression, and !1chromosome location of human carbonic anhydrase III: the !1human CAIII gene is located on the same chromosome as the !1closely linked CAI and CAII genes. !$#cross-references MUID:87092290; PMID:3099285 !$#accession A26658 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-260 ##label WAD !'##cross-references GB:M29458; GB:M22658; NID:g179787; PIDN:AAA52293.1; !1PID:g179789 REFERENCE A26690 !$#authors Lloyd, J.; Brownson, C.; Tweedie, S.; Charlton, J.; Edwards, !1Y.H. !$#journal Genes Dev. (1987) 1:594-602 !$#title Human muscle carbonic anhydrase: gene structure and DNA !1methylation patterns in fetal and adult tissues. !$#cross-references MUID:88056301; PMID:2824285 !$#accession A26690 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-15;74-81;113-121;144-152;165-173;217-225 ##label LL2 !'##cross-references GB:M27974 !'##note the complete sequence is not given REFERENCE A25850 !$#authors Lloyd, J.; McMillan, S.; Hopkinson, D.; Edwards, Y.H. !$#journal Gene (1986) 41:233-239 !$#title Nucleotide sequence and derived amino acid sequence of a !1cDNA encoding human muscle carbonic anhydrase. !$#cross-references MUID:86221704; PMID:3086182 !$#accession A25850 !'##molecule_type mRNA !'##residues 1-30,'I',32-260 ##label LLO !'##cross-references GB:M14995 !'##note allelic variant sequence with 31-Ile; parts of this sequence !1were determined by protein sequencing GENETICS !$#gene GDB:CA3 !'##cross-references GDB:119740; OMIM:114750 !$#map_position 8q13-8q22 !$#introns 12/1; 78/1; 117/3; 148/3; 169/3; 221/3 FUNCTION !$#description catalyzes the reversible dissociation of carbonic acid to !1carbon dioxide and water !$#note this form is predominantly expressed in slow-twitch, !1aerobic, type I muscle fibers CLASSIFICATION #superfamily carbonate dehydratase; carbonic anhydrase !1homology KEYWORDS acetylated amino end; carbon-oxygen lyase; hydro-lyase; !1metalloprotein; muscle; zinc FEATURE !$2-260 #product carbonate dehydratase III #status predicted !8#label MAT\ !$5-259 #domain carbonic anhydrase homology #label CAH\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status predicted\ !$94,96,119 #binding_site zinc (His) #status predicted SUMMARY #length 260 #molecular-weight 29557 #checksum 5700 SEQUENCE /// ENTRY CRHU7 #type complete TITLE carbonate dehydratase (EC 4.2.1.1) VII - human ALTERNATE_NAMES carbonic anhydrase VII ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Feb-1995 #sequence_revision 05-May-1995 #text_change 18-Jun-1999 ACCESSIONS A55272 REFERENCE A55272 !$#authors Montgomery, J.C.; Venta, P.J.; Eddy, R.L.; Fukushima, Y.S.; !1Shows, T.B.; Tashian, R.E. !$#journal Genomics (1991) 11:835-848 !$#title Characterization of the human gene for a newly discovered !1carbonic anhydrase, CA VII, and its localization to !1chromosome 16. !$#cross-references MUID:92147127; PMID:1783392 !$#accession A55272 !'##molecule_type DNA !'##residues 1-264 ##label MON !'##cross-references GB:M76423; NID:g179964; PIDN:AAA51923.1; !1PID:g179967 !'##note sequence extracted from NCBI backbone (NCBIN:80199, !1NCBIN:80201, NCBIN:80205, NCBIN:80207, NCBIP:80210) GENETICS !$#gene GDB:CA7 !'##cross-references GDB:119741; OMIM:114770 !$#map_position 16q22.1-16q22.1 !$#introns 14/1; 80/1; 119/3; 151/3; 172/3; 224/3 FUNCTION !$#description catalyzes the reversible dissociation of carbonic acid to !1carbon dioxide and water !$#note this form is expressed in salivary gland and other tissues CLASSIFICATION #superfamily carbonate dehydratase; carbonic anhydrase !1homology KEYWORDS carbon-oxygen lyase; hydro-lyase; metalloprotein; zinc FEATURE !$2-264 #product carbonate dehydratase VII #status predicted !8#label MAT\ !$7-262 #domain carbonic anhydrase homology #label CAH\ !$96,98,121 #binding_site zinc (His) #status predicted SUMMARY #length 264 #molecular-weight 29658 #checksum 8896 SEQUENCE /// ENTRY CRHU5 #type complete TITLE carbonate dehydratase (EC 4.2.1.1) V precursor [validated] - human ALTERNATE_NAMES carbonic anhydrase V; mitochondrial carbonic anhydrase ORGANISM #formal_name Homo sapiens #common_name man DATE 02-Jun-1994 #sequence_revision 05-May-1995 #text_change 08-Dec-2000 ACCESSIONS A47745 REFERENCE A47745 !$#authors Nagao, Y.; Platero, J.S.; Waheed, A.; Sly, W.S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:7623-7627 !$#title Human mitochondrial carbonic anhydrase: cDNA cloning, !1expression, subcellular localization, and mapping to !1chromosome 16. !$#cross-references MUID:93361499; PMID:8356065 !$#accession A47745 !'##molecule_type mRNA !'##residues 1-305 ##label NAG !'##cross-references GB:L19297; NID:g306482; PIDN:AAA02890.1; !1PID:g306483 !'##experimental_source liver !'##note authors translated the codon TAT for residue 76 as Thr !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing GENETICS !$#gene GDB:CA5 !'##cross-references GDB:218380; OMIM:114761 !$#map_position 16q24.3-16q24.3 FUNCTION !$#description catalyzes the reversible dissociation of carbonic acid to !1carbon dioxide and water !$#note this form is transported into mitochondria CLASSIFICATION #superfamily carbonate dehydratase; carbonic anhydrase !1homology KEYWORDS carbon-oxygen lyase; hydro-lyase; metalloprotein; !1mitochondrion; zinc FEATURE !$1-38 #domain transit peptide (mitochondrion) #status !8predicted #label TRP\ !$39-305 #product carbonate dehydratase V #status experimental !8#label MAT\ !$41-296 #domain carbonic anhydrase homology #label CAH\ !$130,132,155 #binding_site zinc (His) #status predicted SUMMARY #length 305 #molecular-weight 34750 #checksum 5537 SEQUENCE /// ENTRY CRHU6 #type complete TITLE carbonate dehydratase (EC 4.2.1.1) VI precursor - human ALTERNATE_NAMES carbonic anhydrase VI; salivary carbonic anhydrase; secreted carbonic anhydrase ORGANISM #formal_name Homo sapiens #common_name man DATE 31-May-1991 #sequence_revision 05-May-1995 #text_change 02-Sep-1997 ACCESSIONS A37917 REFERENCE A37917 !$#authors Aldred, P.; Fu, P.; Barrett, G.; Penschow, J.D.; Wright, !1R.D.; Coghlan, J.P.; Fernley, R.T. !$#journal Biochemistry (1991) 30:569-575 !$#title Human secreted carbonic anhydrase: cDNA cloning, nucleotide !1sequence, and hybridization histochemistry. !$#cross-references MUID:91105141; PMID:1899030 !$#accession A37917 !'##molecule_type mRNA !'##residues 1-308 ##label ALD !'##cross-references GB:M57892; GB:J05305 !'##experimental_source salivary gland !'##note the authors translated the codon GAG for residue 248 as Gln GENETICS !$#gene GDB:CA6 !'##cross-references GDB:125350; OMIM:114780 !$#map_position 1p36-1p36 FUNCTION !$#description catalyzes the reversible dissociation of carbonic acid to !1carbon dioxide and water !$#note this form is expressed in salivary, parotid, and !1submandibular glands; it is excreted in saliva CLASSIFICATION #superfamily carbonate dehydratase; carbonic anhydrase !1homology KEYWORDS carbon-oxygen lyase; glycoprotein; hydro-lyase; !1metalloprotein; pyroglutamic acid; saliva; zinc FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-308 #product carbonate dehydratase VI #status predicted !8#label MAT\ !$23-278 #domain carbonic anhydrase homology #label CAH\ !$18 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status predicted\ !$42-224 #disulfide_bonds #status predicted\ !$67,256 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$111,113,138 #binding_site zinc (His) #status predicted SUMMARY #length 308 #molecular-weight 35363 #checksum 1588 SEQUENCE /// ENTRY CRHU4 #type complete TITLE carbonate dehydratase (EC 4.2.1.1) IV precursor [validated] - human ALTERNATE_NAMES carbonic anhydrase IV; membrane-associated carbonic anhydrase ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1993 #sequence_revision 05-May-1995 #text_change 08-Dec-2000 ACCESSIONS A45745; A40217; A36280; B36280; S66253; S74148 REFERENCE A45745 !$#authors Okuyama, T.; Batanian, J.R.; Sly, W.S. !$#journal Genomics (1993) 16:678-684 !$#title Genomic organization and localization of gene for human !1carbonic anhydrase IV to chromosome 17q. !$#cross-references MUID:93315160; PMID:8325641 !$#accession A45745 !'##molecule_type DNA !'##residues 1-312 ##label OK1 !'##experimental_source fibroblast !'##note sequence extracted from NCBI backbone (NCBIN:134988, !1NCBIN:134992, NCBIN:134994, NCBIN:134996, NCBIN:134998, !1NCBIP:134999) REFERENCE A40217 !$#authors Okuyama, T.; Sato, S.; Zhu, X.L.; Waheed, A.; Sly, W.S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:1315-1319 !$#title Human carbonic anhydrase IV: cDNA cloning, sequence !1comparison, and expression in COS cell membranes. !$#cross-references MUID:92159040; PMID:1311094 !$#accession A40217 !'##molecule_type mRNA !'##residues 1-312 ##label OK2 !'##cross-references GB:M83670; NID:g179790; PIDN:AAA35630.1; !1PID:g179791 !'##note sequence extracted from NCBI backbone (NCBIN:82232, !1NCBIP:82233) REFERENCE A36280 !$#authors Zhu, X.L.; Sly, W.S. !$#journal J. Biol. Chem. (1990) 265:8795-8801 !$#title Carbonic anhydrase IV from human lung. Purification, !1characterization, and comparison with membrane carbonic !1anhydrase from human kidney. !$#cross-references MUID:90256808; PMID:2111324 !$#accession A36280 !'##molecule_type protein !'##residues 19-23,'E',25-35;113-123;233-239 ##label ZHU !'##experimental_source lung !$#accession B36280 !'##molecule_type protein !'##residues 19-23,'E',25-35;113-122;233-239 ##label ZH2 !'##experimental_source kidney !'##note amino end of the mature protein determined; evidence for !1glycosyl phosphatidylinositol anchor REFERENCE S66253 !$#authors Okuyama, T.; Waheed, A.; Kusumoto, W.; Zhu, X.L.; Sly, W.S. !$#journal Arch. Biochem. Biophys. (1995) 320:315-322 !$#title Carbonic anhydrase IV: role of removal of C-terminal domain !1in glycosylphosphatidylinositol anchoring and realization of !1enzyme activity. !$#cross-references MUID:95351793; PMID:7625839 !$#accession S66253 !'##molecule_type protein !'##residues 19-63;64-77;78-145;146-184;185-198;202-260;261-283 ##label !1OKU !'##experimental_source lung REFERENCE S74148 !$#authors Waheed, A.; Okuyama, T.; Heyduk, T.; Sly, W.S. !$#journal Arch. Biochem. Biophys. (1996) 333:432-438 !$#title Carbonic anhydrase IV: purification of a secretory form of !1the recombinant human enzyme and identification of the !1positions and importance of its disulfide bonds. !$#cross-references MUID:96404944; PMID:8809084 !$#accession S74148 !'##molecule_type protein !'##residues 19-23,'X',25-35,'X',37-40;'W',102-103,'NXQ';152-156;214-232 !1##label WAH GENETICS !$#gene GDB:CA4 !'##cross-references GDB:131660 !$#map_position 17q23-17q23 FUNCTION !$#description catalyzes the reversible dissociation of carbonic acid to !1carbon dioxide and water CLASSIFICATION #superfamily carbonate dehydratase; carbonic anhydrase !1homology KEYWORDS blocked carboxyl end; carbon-oxygen lyase; glycoprotein; !1hydro-lyase; lipoprotein; membrane protein; metalloprotein; !1phosphatidylinositol linkage; phosphoprotein; zinc FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-284 #product carbonate dehydratase IV #status !8experimental #label MAT\ !$23-285 #domain carbonic anhydrase homology #label CAH\ !$285-312 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$24-36,46-229 #disulfide_bonds #status predicted\ !$115,117,140 #binding_site zinc (His) #status predicted\ !$284 #modified_site GPI-anchor ethanolamine amidated !8carboxyl end (Ser) (in mature form) #status predicted SUMMARY #length 312 #molecular-weight 35032 #checksum 2738 SEQUENCE /// ENTRY CRVZW #type complete TITLE cell surface-binding protein D8 - vaccinia virus (strain WR) ALTERNATE_NAMES carbonic anhydrase homolog ORGANISM #formal_name vaccinia virus DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 18-Jun-1999 ACCESSIONS A01146; A35014; A03887 REFERENCE A01146 !$#authors Niles, E.G.; Condit, R.C.; Caro, P.; Davidson, K.; Matusick, !1L.; Seto, J. !$#journal Virology (1986) 153:96-112 !$#title Nucleotide sequence and genetic map of the 16-kb vaccinia !1virus HindIII D fragment. !$#cross-references MUID:86291159; PMID:3739227 !$#accession A01146 !'##molecule_type DNA !'##residues 1-304 ##label NIL !'##cross-references GB:M15058; NID:g335640; PIDN:AAA48264.1; !1PID:g335652 REFERENCE A35014 !$#authors Maa, J.S.; Rodriguez, J.F.; Esteban, M. !$#journal J. Biol. Chem. (1990) 265:1569-1577 !$#title Structural and functional characterization of a cell surface !1binding protein of vaccinia virus. !$#cross-references MUID:90110221; PMID:2104847 !$#accession A35014 !'##molecule_type DNA !'##residues 1-304 ##label MAA CLASSIFICATION #superfamily carbonate dehydratase; carbonic anhydrase !1homology KEYWORDS homodimer; transmembrane protein FEATURE !$276-294 #domain transmembrane #status predicted #label TMM SUMMARY #length 304 #molecular-weight 35446 #checksum 9197 SEQUENCE /// ENTRY CRVZ7P #type complete TITLE cell surface-binding protein D8 - vaccinia virus (strain Copenhagen) ALTERNATE_NAMES carbonic anhydrase; D8L protein ORGANISM #formal_name vaccinia virus #note host Homo sapiens (man) DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 18-Jun-1999 ACCESSIONS G42515 REFERENCE A42501 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:517-563 !$#title Appendix to "The complete DNA sequence of vaccinia virus". !$#accession G42515 !'##molecule_type DNA !'##residues 1-304 ##label GOE !'##cross-references GB:M35027; NID:g335317; PIDN:AAA48107.1; !1PID:g335455 !'##experimental_source strain Copenhagen REFERENCE A42531 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:247-266 !$#title The complete DNA sequence of vaccinia virus. !$#cross-references MUID:91021027; PMID:2219722 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given CLASSIFICATION #superfamily carbonate dehydratase; carbonic anhydrase !1homology KEYWORDS homodimer; transmembrane protein FEATURE !$276-294 #domain transmembrane #status predicted #label TMM SUMMARY #length 304 #molecular-weight 35327 #checksum 546 SEQUENCE /// ENTRY QRECTC #type complete TITLE carbonate dehydratase (EC 4.2.1.1) - Escherichia coli (strain K-12) ALTERNATE_NAMES carbonic anhydrase ORGANISM #formal_name Escherichia coli DATE 31-Mar-1990 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS C64761; A31977; JS0143 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64761 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-219 ##label BLAT !'##cross-references GB:AE000141; GB:U00096; NID:g1786532; !1PIDN:AAC73442.1; PID:g1786534; UWGP:b0339 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A92672 !$#authors Sung, Y.; Fuchs, J.A. !$#journal J. Biol. Chem. (1988) 263:14769-14775 !$#title Characterization of the cyn operon in Escherichia coli K12. !$#cross-references MUID:89008347; PMID:3049588 !$#accession A31977 !'##molecule_type DNA !'##residues 1-173,'G','S',177-211,'R',213-219 ##label SUN !'##cross-references GB:M23219; NID:g145641; PIDN:AAA23625.1; !1PID:g145642 !'##experimental_source strain K12 !'##note the authors identified this protein as cyanate permease GENETICS !$#gene cynT !$#map_position 8 min !$#start_codon GTG !$#note part of the cyn operon FUNCTION !$#description catalyzes the reversible hydratation of carbon dioxide !$#note previously believed to be part of an active transport system !1for cyanate CLASSIFICATION #superfamily Escherichia coli carbonate dehydratase KEYWORDS carbon-oxygen lyase; hydro-lyase; zinc SUMMARY #length 219 #molecular-weight 23764 #checksum 4591 SEQUENCE /// ENTRY D64520 #type complete TITLE carbonate dehydratase (EC 4.2.1.1) - Helicobacter pylori (strain 26695) ALTERNATE_NAMES carbonic anhydrase ORGANISM #formal_name Helicobacter pylori DATE 21-Nov-1998 #sequence_revision 21-Nov-1998 #text_change 18-Jun-1999 ACCESSIONS D64520 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession D64520 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-221 ##label TOM !'##cross-references GB:AE000523; GB:AE000511; NID:g2313077; !1PIDN:AAD07077.1; PID:g2313081; TIGR:HP0004 GENETICS !$#start_codon GTG FUNCTION !$#description catalyzes the reversible hydratation of carbon dioxide CLASSIFICATION #superfamily Escherichia coli carbonate dehydratase KEYWORDS carbon-oxygen lyase; hydro-lyase; zinc SUMMARY #length 221 #molecular-weight 25515 #checksum 4056 SEQUENCE /// ENTRY S28795 #type complete TITLE carbonate dehydratase (EC 4.2.1.1) - Synechococcus sp. (strain PCC 7942) ALTERNATE_NAMES carbonic anhydrase ORGANISM #formal_name Synechococcus sp. DATE 21-Nov-1998 #sequence_revision 21-Nov-1998 #text_change 18-Jun-1999 ACCESSIONS S28795 REFERENCE S28795 !$#authors Fukuzawa, H.; Suzuki, E.; Komukai, Y.; Miyachi, S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:4437-4441 !$#title A gene homologous to chloroplast carbonic anhydrase (icfA) !1is essential to photosynthetic carbon dioxide fixation by !1Synechococcus PCC7942. !$#cross-references MUID:92262454; PMID:1584776 !$#accession S28795 !'##molecule_type DNA !'##residues 1-272 ##label FUK !'##cross-references EMBL:M77095; NID:g154522; PIDN:AAA27315.1; !1PID:g154523 GENETICS !$#gene icfA FUNCTION !$#description catalyzes the reversible hydratation of carbon dioxide CLASSIFICATION #superfamily Escherichia coli carbonate dehydratase KEYWORDS carbon-oxygen lyase; hydro-lyase; zinc SUMMARY #length 272 #molecular-weight 30185 #checksum 1704 SEQUENCE /// ENTRY S75605 #type complete TITLE carbonate dehydratase (EC 4.2.1.1) - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES carbonic anhydrase; protein slr1347 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 21-Nov-1998 #sequence_revision 21-Nov-1998 #text_change 16-Jun-2000 ACCESSIONS S75605 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75605 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-311 ##label KAN !'##cross-references EMBL:D90912; GB:AB001339; NID:g1653228; !1PIDN:BAA18166.1; PID:g1653251 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene icfA FUNCTION !$#description catalyzes the reversible hydratation of carbon dioxide CLASSIFICATION #superfamily Escherichia coli carbonate dehydratase KEYWORDS carbon-oxygen lyase; hydro-lyase; zinc SUMMARY #length 311 #molecular-weight 34806 #checksum 6021 SEQUENCE /// ENTRY A35163 #type complete TITLE carbonate dehydratase (EC 4.2.1.1) precursor, chloroplast - spinach ALTERNATE_NAMES carbonic anhydrase ORGANISM #formal_name Spinacia oleracea #common_name spinach DATE 21-Nov-1998 #sequence_revision 21-Nov-1998 #text_change 29-Oct-1999 ACCESSIONS A35163; S28797; S29092; S29091 REFERENCE A35163 !$#authors Fawcett, T.W.; Browse, J.A.; Volokita, M.; Bartlett, S.G. !$#journal J. Biol. Chem. (1990) 265:5414-5417 !$#title Spinach carbonic anhydrase primary structure deduced from !1the sequence of a cDNA clone. !$#cross-references MUID:90202770; PMID:2108138 !$#accession A35163 !'##molecule_type mRNA !'##residues 1-319 ##label FAW !'##cross-references GB:J05403; NID:g170104; PIDN:AAA34027.1; !1PID:g170105 !'##note these authors suggest that the protein may undergo proteolysis !1after removal of a transit peptide of about 60 residues REFERENCE S28797 !$#authors Burnell, J.N.; Gibbs, M.J.; Mason, J.G. !$#journal Plant Physiol. (1990) 92:37-40 !$#title Spinach chloroplastic carbonic anhydrase. Nucleotide !1sequence analysis of cDNA. !$#accession S28797 !'##molecule_type mRNA !'##residues 66-310,'F',312-319 ##label BUR !'##cross-references EMBL:M27295; NID:g170101 !$#accession S29092 !'##molecule_type protein !'##residues 99-118 ##label BU2 REFERENCE S29091 !$#authors Burnell, J.N.; Gibbs, M.J.; Mason, J.G. !$#submission submitted to the EMBL Data Library, August 1989 !$#accession S29091 !'##molecule_type mRNA !'##residues 66-221,'S',223-310,'F',312-319 ##label BU3 !'##cross-references EMBL:M27295; NID:g170101; PIDN:AAA34026.1; !1PID:g170102 GENETICS !$#genome nuclear COMPLEX homohexamer FUNCTION !$#description catalyzes the reversible hydratation of carbon dioxide CLASSIFICATION #superfamily Escherichia coli carbonate dehydratase KEYWORDS carbon-oxygen lyase; chloroplast; homohexamer; hydro-lyase; !1zinc FEATURE !$1-98 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$99-319 #product carbonate dehydratase #status experimental !8#label MAT SUMMARY #length 319 #molecular-weight 34569 #checksum 4209 SEQUENCE /// ENTRY S28412 #type complete TITLE carbonate dehydratase (EC 4.2.1.1) precursor, chloroplast - Arabidopsis thaliana ALTERNATE_NAMES carbonic anhydrase ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 21-Nov-1998 #sequence_revision 21-Nov-1998 #text_change 18-Jun-1999 ACCESSIONS S28412; S21379 REFERENCE S28412 !$#authors Raines, C.A.; Horsnell, P.R.; Holder, C.; Lloyd, J.C. !$#journal Plant Mol. Biol. (1992) 20:1143-1148 !$#title Arabidopsis thaliana carbonic anhydrase: cDNA sequence and !1effect of CO(2) on mRNA levels. !$#cross-references MUID:93099264; PMID:1463847 !$#accession S28412 !'##molecule_type mRNA !'##residues 1-336 ##label RAI !'##cross-references EMBL:X65541; NID:g14342; PIDN:CAA46508.1; !1PID:g14343 GENETICS !$#genome nuclear COMPLEX homohexamer FUNCTION !$#description catalyzes the reversible hydratation of carbon dioxide CLASSIFICATION #superfamily Escherichia coli carbonate dehydratase KEYWORDS carbon-oxygen lyase; chloroplast; homohexamer; hydro-lyase; !1zinc FEATURE !$1-78 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$79-336 #product carbonate dehydratase, long form #status !8predicted #label MATL\ !$117-336 #product carbonate dehydratase, short form #status !8predicted #label MATS SUMMARY #length 336 #molecular-weight 36144 #checksum 9737 SEQUENCE /// ENTRY S10200 #type complete TITLE carbonate dehydratase (EC 4.2.1.1) precursor, chloroplast - garden pea ALTERNATE_NAMES carbonic anhydrase ORGANISM #formal_name Pisum sativum #common_name garden pea DATE 21-Nov-1998 #sequence_revision 21-Nov-1998 #text_change 18-Jun-1999 ACCESSIONS S10200; S27027; S78006; S28796; S29254 REFERENCE S10200 !$#authors Roeske, C.A.; Ogren, W.L. !$#journal Nucleic Acids Res. (1990) 18:3413 !$#title Nucleotide sequence of pea cDNA encoding chloroplast !1carbonic anhydrase. !$#cross-references MUID:90287736; PMID:2113277 !$#accession S10200 !'##molecule_type mRNA !'##residues 1-328 ##label ROE !'##cross-references EMBL:X52558; NID:g20672; PIDN:CAA36792.1; !1PID:g20673 REFERENCE S27027 !$#authors Johansson, I.M.; Forsman, C. !$#journal FEBS Lett. (1992) 314:232-236 !$#title Processing of the chloroplast transit peptide of pea !1carbonic anhydrase in chloroplasts and in Escherichia coli. !1Identification of two cleavage sites. !$#cross-references MUID:93106157; PMID:1468554 !$#accession S27027 !'##molecule_type mRNA !'##residues 1-112 ##label JOH !'##note two cleavage sites for the cloroplastic transit peptide are !1shown and suggested to be mutually exclusive !$#accession S78006 !'##molecule_type protein !'##residues 71-76;108-113 ##label FOR REFERENCE S28796 !$#authors Majeau, N.; Coleman, J.R. !$#journal Plant Physiol. (1991) 95:264-268 !$#title Isolation and characterization of a cDNA coding for pea !1chloroplastic carbonic anhydrase. !$#accession S28796 !'##molecule_type mRNA !'##residues 1-30,'F',32-43,'S',44-175,'K',177-328 ##label MAJ !'##cross-references EMBL:M63627; NID:g169056; PIDN:AAA33652.1; !1PID:g169057 !$#accession S29254 !'##molecule_type protein !'##residues 156-167 ##label MA2 GENETICS !$#genome nuclear COMPLEX homohexamer FUNCTION !$#description catalyzes the reversible hydratation of carbon dioxide CLASSIFICATION #superfamily Escherichia coli carbonate dehydratase KEYWORDS carbon-oxygen lyase; chloroplast; homohexamer; hydro-lyase; !1zinc FEATURE !$1-70 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$71-328 #product carbonate dehydratase, long form #status !8experimental #label MATL\ !$108-328 #product carbonate dehydratase, short form #status !8experimental #label MATS\ !$70-71 #cleavage_site Met-Gly (unidentified stromal !8peptidase) #status experimental\ !$107-108 #cleavage_site Gly-Thr (unidentified stromal !8peptidase) #status experimental SUMMARY #length 328 #molecular-weight 35377 #checksum 9517 SEQUENCE /// ENTRY S61883 #type complete TITLE carbonate dehydratase (EC 4.2.1.1) precursor, chloroplast - Flaveria linearis ALTERNATE_NAMES carbonic anhydrase ORGANISM #formal_name Flaveria linearis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S61883 REFERENCE S61882 !$#authors Ludwig, M.; Burnell, J.N. !$#journal Plant Mol. Biol. (1995) 29:353-365 !$#title Molecular comparison of carbonic anhydrase from Flaveria !1species demonstrating different photosynthetic pathways. !$#cross-references MUID:96046753; PMID:7579185 !$#accession S61883 !'##status preliminary; nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-330 ##label LUD !'##cross-references EMBL:U19738; NID:g882241; PIDN:AAA86993.1; !1PID:g882242 GENETICS !$#genome nuclear COMPLEX homohexamer FUNCTION !$#description catalyzes the reversible hydratation of carbon dioxide CLASSIFICATION #superfamily Escherichia coli carbonate dehydratase KEYWORDS carbon-oxygen lyase; chloroplast; homohexamer; hydro-lyase; !1zinc SUMMARY #length 330 #molecular-weight 35574 #checksum 6329 SEQUENCE /// ENTRY S61882 #type complete TITLE carbonate dehydratase (EC 4.2.1.1) precursor, chloroplast - Flaveria brownii ALTERNATE_NAMES carbonic anhydrase ORGANISM #formal_name Flaveria brownii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S61882 REFERENCE S61882 !$#authors Ludwig, M.; Burnell, J.N. !$#journal Plant Mol. Biol. (1995) 29:353-365 !$#title Molecular comparison of carbonic anhydrase from Flaveria !1species demonstrating different photosynthetic pathways. !$#cross-references MUID:96046753; PMID:7579185 !$#accession S61882 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-330 ##label LUD !'##cross-references EMBL:U08402; NID:g606812; PIDN:AAA86942.1; !1PID:g606813 GENETICS !$#genome nuclear COMPLEX homohexamer FUNCTION !$#description catalyzes the reversible hydratation of carbon dioxide CLASSIFICATION #superfamily Escherichia coli carbonate dehydratase KEYWORDS carbon-oxygen lyase; chloroplast; homohexamer; hydro-lyase; !1zinc SUMMARY #length 330 #molecular-weight 35547 #checksum 6182 SEQUENCE /// ENTRY S61884 #type complete TITLE carbonate dehydratase (EC 4.2.1.1) precursor, chloroplast - Flaveria pringlei ALTERNATE_NAMES carbonic anhydrase ORGANISM #formal_name Flaveria pringlei DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S61884 REFERENCE S61882 !$#authors Ludwig, M.; Burnell, J.N. !$#journal Plant Mol. Biol. (1995) 29:353-365 !$#title Molecular comparison of carbonic anhydrase from Flaveria !1species demonstrating different photosynthetic pathways. !$#cross-references MUID:96046753; PMID:7579185 !$#accession S61884 !'##status preliminary; nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-329 ##label LUD !'##cross-references EMBL:U19737; NID:g882239; PIDN:AAA86992.1; !1PID:g882240 GENETICS !$#genome nuclear COMPLEX homohexamer FUNCTION !$#description catalyzes the reversible hydratation of carbon dioxide CLASSIFICATION #superfamily Escherichia coli carbonate dehydratase KEYWORDS carbon-oxygen lyase; chloroplast; homohexamer; hydro-lyase; !1zinc SUMMARY #length 329 #molecular-weight 35486 #checksum 2603 SEQUENCE /// ENTRY S48675 #type complete TITLE carbonate dehydratase (EC 4.2.1.1) precursor, chloroplast - Flaveria bidentis ALTERNATE_NAMES carbonic anhydrase ORGANISM #formal_name Flaveria bidentis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S48675 REFERENCE S48675 !$#authors Cavallaro, A.; Ludwig, M.; Burnell, J. !$#journal FEBS Lett. (1994) 350:216-218 !$#title The nucleotide sequence of a complementary DNA encoding !1Flaveria bidentis carbonic anhydrase. !$#cross-references MUID:94350102; PMID:8070567 !$#accession S48675 !'##status preliminary !'##molecule_type mRNA !'##residues 1-331 ##label CAV GENETICS !$#genome nuclear COMPLEX homohexamer FUNCTION !$#description catalyzes the reversible hydratation of carbon dioxide CLASSIFICATION #superfamily Escherichia coli carbonate dehydratase KEYWORDS carbon-oxygen lyase; chloroplast; homohexamer; hydro-lyase; !1zinc SUMMARY #length 331 #molecular-weight 35648 #checksum 73 SEQUENCE /// ENTRY UFECAQ #type complete TITLE fumarate hydratase (EC 4.2.1.2) fumA, iron-dependent - Escherichia coli (strain K-12) ALTERNATE_NAMES fumarase; fumarate hydratase class I ORGANISM #formal_name Escherichia coli DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 01-Mar-2002 ACCESSIONS A03531; PX0048; F64917 REFERENCE A93515 !$#authors Miles, J.S.; Guest, J.R. !$#journal Nucleic Acids Res. (1984) 12:3631-3642 !$#title Complete nucleotide sequence of the fumarase gene fumA, of !1Escherichia coli. !$#cross-references MUID:84221385; PMID:6328431 !$#accession A03531 !'##molecule_type DNA !'##residues 1-548 ##label MIL !'##cross-references GB:X00522; NID:g41510; PIDN:CAA25204.1; PID:g41511 REFERENCE A92783 !$#authors Guest, J.R.; Miles, J.S.; Roberts, R.E.; Woods, S.A. !$#journal J. Gen. Microbiol. (1985) 131:2971-2984 !$#title The fumarase genes of Escherichia coli: location of the fumB !1gene and discovery of a new gene (fumC). !$#cross-references MUID:86142617; PMID:3005475 !$#contents annotation; identification of structural gene REFERENCE PX0048 !$#authors Ueda, Y.; Yumoto, N.; Tokushige, M.; Fukui, K.; !1Ohya-Nishiguchi, H. !$#journal J. Biochem. (1991) 109:728-733 !$#title Purification and characterization of two types of fumarase !1from Escherichia coli. !$#cross-references MUID:92011457; PMID:1917897 !$#accession PX0048 !'##molecule_type protein !'##residues 2-21 ##label UED !'##experimental_source strain W REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64917 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-548 ##label BLAT !'##cross-references GB:AE000256; GB:U00096; NID:g1787888; !1PIDN:AAC74684.1; PID:g1787897; UWGP:b1612 !'##experimental_source strain K-12, substrain MG1655 COMMENT Three fumarate hydratase genes (fumA, fumB, and fumC) have !1been reported; this protein, the fumA-encoded fumarate !1hydratase, is an Fe-dependent 4Fe-4S, oxygen- and !1heat-labile, class I hydratase. GENETICS !$#gene fumA !$#map_position 35.5 min COMPLEX homodimer FUNCTION !$#description catalyzes the stereospecific interconversion of fumarate and !1L-malate !$#pathway tricarboxylic acid cycle !$#note most highly expressed under aerobic growth CLASSIFICATION #superfamily iron-dependent fumarate hydratase; !1iron-dependent tartrate dehydratase alpha chain homology; !1iron-dependent tartrate dehydratase beta chain homology KEYWORDS 4Fe-4S; carbon-oxygen lyase; homodimer; hydro-lyase; !1iron-sulfur protein; metalloprotein FEATURE !$2-548 #product fumarate hydratase, iron-dependent #status !8predicted #label MAT\ !$93-300 #domain iron-dependent tartrate dehydratase alpha !8chain homology #label TTDA\ !$373-537 #domain iron-dependent tartrate dehydratase beta !8chain homology #label TTDB SUMMARY #length 548 #molecular-weight 60298 #checksum 4355 SEQUENCE /// ENTRY B44511 #type complete TITLE fumarate hydratase (EC 4.2.1.2) fumB, iron-dependent - Escherichia coli (strain K-12) ALTERNATE_NAMES fumarase B ORGANISM #formal_name Escherichia coli DATE 03-Mar-1993 #sequence_revision 10-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS A65222; B44511; S56351 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65222 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-548 ##label BLAT !'##cross-references GB:AE000485; GB:U00096; NID:g1790563; !1PIDN:AAC77083.1; PID:g1790564; UWGP:b4122 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A44511 !$#authors Bell, P.J.; Andrews, S.C.; Sivak, M.N.; Guest, J.R. !$#journal J. Bacteriol. (1989) 171:3494-3503 !$#title Nucleotide sequence of the FNR-regulated fumarase gene !1(fumB) of Escherichia coli K-12. !$#cross-references MUID:89255123; PMID:2656658 !$#accession B44511 !'##molecule_type DNA !'##residues 1-49,'V',51-548 ##label BEL !'##cross-references EMBL:M27058; NID:g146046; PIDN:AAA23827.1; !1PID:g146048 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56351 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-49,'X',51-548 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97022.1; !1PID:g536967 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 COMMENT In E. coli, three fumarate hydratase genes (fumA, fumB, and !1fumC) have been reported. This protein, the fumB-encoded !1fumarate hydratase, is an Fe-dependent 4Fe-4S, oxygen- and !1heat-labile, class I hydratase. GENETICS !$#gene fumB !$#map_position 93.5 min COMPLEX homodimer FUNCTION !$#description catalyzes the stereospecific interconversion of fumarate and !1L-malate !$#note expressed at higher level under anaerobic conditions CLASSIFICATION #superfamily iron-dependent fumarate hydratase; !1iron-dependent tartrate dehydratase alpha chain homology; !1iron-dependent tartrate dehydratase beta chain homology KEYWORDS 4Fe-4S; carbon-oxygen lyase; homodimer; hydro-lyase; !1iron-sulfur protein; metalloprotein FEATURE !$2-548 #product fumarate hydratase fumB, iron-dependent !8#status predicted #label MAT\ !$93-300 #domain iron-dependent tartrate dehydratase alpha !8chain homology #label TTDA\ !$373-537 #domain iron-dependent tartrate dehydratase beta !8chain homology #label TTDB SUMMARY #length 548 #molecular-weight 60105 #checksum 3092 SEQUENCE /// ENTRY A47692 #type complete TITLE fumarate hydratase (EC 4.2.1.2), iron-dependent - Bacillus stearothermophilus ALTERNATE_NAMES fumarase ORGANISM #formal_name Bacillus stearothermophilus DATE 19-Dec-1993 #sequence_revision 27-Jan-1995 #text_change 18-Jun-1999 ACCESSIONS A47692 REFERENCE A47692 !$#authors Reaney, S.K.; Bungard, S.J.; Guest, J.R. !$#journal J. Gen. Microbiol. (1993) 139:403-416 !$#title Molecular and enzymological evidence for two classes of !1fumarase in Bacillus stearothermophilus (var. !1non-diastaticus). !$#cross-references MUID:93232761; PMID:8473853 !$#accession A47692 !'##molecule_type DNA !'##residues 1-514 ##label REA !'##cross-references GB:L05611; NID:g142943; PIDN:AAA72317.1; !1PID:g142944 !'##experimental_source var. non-diastaticus, DSM 2334 !'##note sequence extracted from NCBI backbone (NCBIN:129946, !1NCBIP:129947) COMMENT This enzyme catalyzes the stereospecific interconversion of !1fumarate and L-malate in the tricarboxylic acid cycle; it is !1an Fe-dependent 4Fe-4S, oxygen- and heat-labile, class I !1hydratase. GENETICS !$#gene fumA CLASSIFICATION #superfamily iron-dependent fumarate hydratase; !1iron-dependent tartrate dehydratase alpha chain homology; !1iron-dependent tartrate dehydratase beta chain homology KEYWORDS 4Fe-4S; carbon-oxygen lyase; homodimer; hydro-lyase; !1iron-sulfur protein; metalloprotein FEATURE !$2-514 #product fumarate hydratase iron-dependent #status !8predicted #label MAT\ !$50-256 #domain iron-dependent tartrate dehydratase alpha !8chain homology #label TTDA\ !$334-496 #domain iron-dependent tartrate dehydratase beta !8chain homology #label TTDB SUMMARY #length 514 #molecular-weight 56791 #checksum 9221 SEQUENCE /// ENTRY UFHUM #type fragment TITLE fumarate hydratase (EC 4.2.1.2) precursor, mitochondrial - human (fragment) ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS S06213 REFERENCE S06213 !$#authors Kinsella, B.T.; Doonan, S. !$#journal Biosci. Rep. (1986) 6:921-929 !$#title Nucleotide sequence of a cDNA coding for mitochondrial !1fumarase from human liver. !$#cross-references MUID:87157989; PMID:3828494 !$#accession S06213 !'##molecule_type mRNA !'##residues 1-468 ##label KIN !'##cross-references GB:M15502; NID:g182793; PIDN:AAA52483.1; !1PID:g182794 !'##experimental_source liver COMMENT This is a class II fumarase; it is thermostable. GENETICS !$#gene GDB:FH !'##cross-references GDB:119133; OMIM:136850 !$#map_position 1q42.1-1q42.1 !$#genome nuclear COMPLEX homotetramer FUNCTION !$#description catalyzes the stereospecific interconversion of fumarate and !1L-malate !$#pathway tricarboxylic acid cycle CLASSIFICATION #superfamily fumarate hydratase KEYWORDS acetylated amino end; carbon-oxygen lyase; homotetramer; !1hydro-lyase; mitochondrion; tricarboxylic acid cycle FEATURE !$2-468 #product fumarate hydratase #status predicted #label !8MAT SUMMARY #length 468 #checksum 7158 SEQUENCE /// ENTRY UFPG #type complete TITLE fumarate hydratase (EC 4.2.1.2), mitochondrial - pig ALTERNATE_NAMES fumarase ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 21-Nov-1998 ACCESSIONS A27657 REFERENCE A27657 !$#authors Sacchettini, J.C.; Frazier, M.W.; Chiara, D.C.; Banaszak, !1L.J.; Grant, G.A. !$#journal Biochem. Biophys. Res. Commun. (1988) 153:435-440 !$#title Amino acid sequence of porcine heart fumarase. !$#cross-references MUID:88240439; PMID:3377794 !$#accession A27657 !'##molecule_type protein !'##residues 1-466 ##label SAC COMMENT This is a class II fumarase; it is thermostable. GENETICS !$#genome nuclear COMPLEX homotetramer FUNCTION !$#description catalyzes the stereospecific interconversion of fumarate and !1L-malate !$#pathway tricarboxylic acid cycle CLASSIFICATION #superfamily fumarate hydratase KEYWORDS carbon-oxygen lyase; homotetramer; hydro-lyase; !1mitochondrion; tricarboxylic acid cycle SUMMARY #length 466 #molecular-weight 50009 #checksum 5474 SEQUENCE /// ENTRY UFRT #type complete TITLE fumarate hydratase (EC 4.2.1.2) precursor, mitochondrial - rat ALTERNATE_NAMES fumarase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS A31424; S24141 REFERENCE A31424 !$#authors Suzuki, T.; Sato, M.; Yoshida, T.; Tuboi, S. !$#journal J. Biol. Chem. (1989) 264:2581-2586 !$#title Rat liver mitochondrial and cytosolic fumarases with !1identical amino acid sequences are encoded from a single !1gene. !$#cross-references MUID:89123346; PMID:2914923 !$#accession A31424 !'##molecule_type mRNA !'##residues 1-507 ##label SUZ !'##cross-references GB:J04473; NID:g204187; PIDN:AAA41177.1; !1PID:g204188 !'##note parts of this sequence, including the amino ends of the !1mitochondrial and cytoplasmic forms, were determined by !1protein sequencing REFERENCE S24141 !$#authors Suzuki, T.; Yoshida, T.; Tuboi, S. !$#journal Eur. J. Biochem. (1992) 207:767-772 !$#title Evidence that rat liver mitochondrial and cytosolic !1fumarases are synthesized from one species of mRNA by !1alternative translational initiation at two in-phase AUG !1codons. !$#cross-references MUID:92339468; PMID:1633825 !$#accession S24141 !'##status preliminary !'##molecule_type DNA !'##residues 1-86 ##label SU2 COMMENT This is a class II fumarase; it is thermostable. GENETICS !$#gene fum !$#genome nuclear COMPLEX homotetramer FUNCTION !$#description catalyzes the stereospecific interconversion of fumarate and !1L-malate !$#pathway tricarboxylic acid cycle CLASSIFICATION #superfamily fumarate hydratase KEYWORDS acetylated amino end; carbon-oxygen lyase; homotetramer; !1hydro-lyase; mitochondrion; tricarboxylic acid cycle FEATURE !$1-41 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$42-507 #product cytoplasmic fumarate hydratase #status !8experimental #label MAT2\ !$42-507 #product mitochondrial fumarate hydratase #status !8experimental #label MAT1\ !$42 #modified_site acetylated amino end (Ala) (in mature !8form) #link MAT2 #status experimental SUMMARY #length 507 #molecular-weight 54463 #checksum 261 SEQUENCE /// ENTRY UFBYM #type complete TITLE fumarate hydratase (EC 4.2.1.2), cytosolic / fumarate hydratase (EC 4.2.1.2) precursor, mitochondrial [validated] - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES fumarase; protein P0382; protein YPL262w ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1992 #sequence_revision 26-Jul-1996 #text_change 21-Jul-2000 ACCESSIONS S65295; S65316; A29804 REFERENCE S65292 !$#authors Duesterhoeft, A.; Floeth, M.; Fritz, M.; Hilbert, H.; !1Moestl, D. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S65295 !'##molecule_type DNA !'##residues 1-488 ##label DUE !'##cross-references EMBL:Z73618; NID:g1370540; PIDN:CAA97997.1; !1PID:g1370541; GSPDB:GN00016; MIPS:YPL262w !'##experimental_source strain S288C (AB972) REFERENCE S64967 !$#authors Delius, H.; Hebling, U. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S65316 !'##molecule_type DNA !'##residues 1-395 ##label DEL !'##cross-references EMBL:Z73618; GSPDB:GN00016; MIPS:YPL262w !'##experimental_source strain S288C (AB972) REFERENCE A92610 !$#authors Wu, M.; Tzagoloff, A. !$#journal J. Biol. Chem. (1987) 262:12275-12282 !$#title Mitochondrial and cytoplasmic fumarases in Saccharomyces !1cerevisiae are encoded by a single nuclear gene FUM1. !$#cross-references MUID:87308235; PMID:3040736 !$#accession A29804 !'##molecule_type DNA !'##residues 1-172,'V',174-288,'R',290-391,'V',393-488 ##label WUM !'##cross-references GB:J02802; NID:g171522; PIDN:AAA66909.1; !1PID:g171523 COMMENT This is a class II fumarase; it is thermostable. GENETICS !$#gene SGD:FUM1; MIPS:YPL262w !'##cross-references SGD:S0006183; MIPS:YPL262w !$#map_position 16L !$#genome nuclear COMPLEX homotetramer FUNCTION !$#description EC 4.2.1.2 [validated, MUID:92338229]; fumarate hydratase; !1catalyzes the stereospecific interconversion of fumarate and !1L-malate !$#pathway tricarboxylic acid cycle !$#note processing of all FUM1 products takes place in mitochondria, !1most of the enzyme (80 to 90%) ends up in the cytosol !1[validated, MUID:98421470] CLASSIFICATION #superfamily fumarate hydratase KEYWORDS carbon-oxygen lyase; homotetramer; hydro-lyase; !1mitochondrion; tricarboxylic acid cycle FEATURE !$1-32 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$33-488 #product fumarate hydratase, mitochondrial #status !8experimental #label MAT1\ !$33-488 #product fumarate hydratase, cytosolic #status !8experimental #label MAT2 SUMMARY #length 488 #molecular-weight 53151 #checksum 33 SEQUENCE /// ENTRY UFBSC8 #type complete TITLE fumarate hydratase (EC 4.2.1.2) - Bacillus subtilis ALTERNATE_NAMES fumarase ORGANISM #formal_name Bacillus subtilis DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 16-Jun-2000 ACCESSIONS A23033; A33488; A69600 REFERENCE A23033 !$#authors Miles, J.S.; Guest, J.R. !$#journal Nucleic Acids Res. (1985) 13:131-140 !$#title Complete nucleotide sequence of the fumarase gene (citG) of !1Bacillus subtilis 168. !$#cross-references MUID:85215459; PMID:3923430 !$#accession A23033 !'##molecule_type DNA !'##residues 1-462 ##label MIL !'##cross-references GB:X01701; NID:g39842; PIDN:CAA25849.1; PID:g39844 !'##experimental_source strain 168 REFERENCE A33488 !$#authors Price, V.A.; Feavers, I.M.; Moir, A. !$#journal J. Bacteriol. (1989) 171:5933-5939 !$#title Role of sigma H in expression of the fumarase gene (citG) in !1vegetative cells of Bacillus subtilis 168. !$#cross-references MUID:90036677; PMID:2509423 !$#accession A33488 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-50,'N' ##label PRI REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69600 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-65,'A',67-462 ##label KUN !'##cross-references GB:Z99120; GB:AL009126; NID:g2635613; !1PIDN:CAB15294.1; PID:g2635801 !'##experimental_source strain 168 COMMENT This is a class II fumarase; it is thermostable. GENETICS !$#gene citG !$#map_position 295 (degrees) COMPLEX homotetramer FUNCTION !$#description catalyzes the stereospecific interconversion of fumarate and !1L-malate !$#pathway tricarboxylic acid cycle CLASSIFICATION #superfamily fumarate hydratase KEYWORDS ammonia-lyase; carbon-nitrogen lyase; carbon-oxygen lyase; !1homotetramer; hydro-lyase; tricarboxylic acid cycle FEATURE !$276 #active_site His #status predicted SUMMARY #length 462 #molecular-weight 50559 #checksum 8969 SEQUENCE /// ENTRY UFEC #type complete TITLE fumarate hydratase (EC 4.2.1.2) fumC [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES fumarase C; fumarate hydratase class II; protein g48 ORGANISM #formal_name Escherichia coli DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 01-Mar-2002 ACCESSIONS S07138; PS0181; S33825; E64917; A05151 REFERENCE S07138 !$#authors Woods, S.A.; Miles, J.S.; Roberts, R.E.; Guest, J.R. !$#journal Biochem. J. (1986) 237:547-557 !$#title Structural and functional relationships between fumarase and !1aspartase. Nucleotide sequences of the fumarase (fumC) and !1aspartase (aspA) genes of Escherichia coli K12. !$#cross-references MUID:87099873; PMID:3541901 !$#accession S07138 !'##molecule_type DNA !'##residues 1-467 ##label WOO !'##cross-references EMBL:X04065; NID:g41512; PIDN:CAA27698.1; !1PID:g41513 REFERENCE PX0048 !$#authors Ueda, Y.; Yumoto, N.; Tokushige, M.; Fukui, K.; !1Ohya-Nishiguchi, H. !$#journal J. Biochem. (1991) 109:728-733 !$#title Purification and characterization of two types of fumarase !1from Escherichia coli. !$#cross-references MUID:92011457; PMID:1917897 !$#accession PS0181 !'##molecule_type protein !'##residues 1-20 ##label UED REFERENCE A92783 !$#authors Guest, J.R.; Miles, J.S.; Roberts, R.E.; Woods, S.A. !$#journal J. Gen. Microbiol. (1985) 131:2971-2984 !$#title The fumarase genes of Escherichia coli: location of the fumB !1gene and discovery of a new gene (fumC). !$#cross-references MUID:86142617; PMID:3005475 !$#contents annotation; identification of structural gene REFERENCE S33825 !$#authors Weaver, T.M.; Levitt, D.G.; Banaszak, L.J. !$#journal J. Mol. Biol. (1993) 231:141-144 !$#title Purification and crystallization of fumarase C from !1Escherichia coli. !$#cross-references MUID:93267645; PMID:8496960 !$#accession S33825 !'##molecule_type protein !'##residues 1-15 ##label WEA REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64917 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-467 ##label BLAT !'##cross-references GB:AE000256; GB:U00096; NID:g1787888; !1PIDN:AAC74683.1; PID:g1787896; UWGP:b1611 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene fumC !$#map_position 35.5 min !$#note the gene coding for this protein was originally called g48 !1and was identified as the fumarase structural gene, fumC COMPLEX homotetramer [validated, MUID:93267645] FUNCTION !$#description EC 4.2.1.2 [validated, MUID:93267645]; fumarate hydratase; !1catalyzes the stereospecific interconversion of fumarate and !1L-malate !$#pathway tricarboxylic acid cycle !$#note in E. coli three different fumarate hydratase genes (fumA, !1fumB, and fumC) have been reported !$#note fumC-encoded fumarate hydratase is a thermostable and !1iron-independent class II hydratase CLASSIFICATION #superfamily fumarate hydratase KEYWORDS carbon-oxygen lyase; heat-stable protein; homotetramer; !1hydro-lyase; tricarboxylic acid cycle FEATURE !$278 #active_site His #status predicted SUMMARY #length 467 #molecular-weight 50488 #checksum 9950 SEQUENCE /// ENTRY A49760 #type complete TITLE fumarate hydratase (EC 4.2.1.2) fumC - Bradyrhizobium japonicum ALTERNATE_NAMES fumarase ORGANISM #formal_name Bradyrhizobium japonicum DATE 10-Mar-1994 #sequence_revision 27-Jan-1995 #text_change 07-May-1999 ACCESSIONS A49760 REFERENCE A49760 !$#authors Acuna, G.; Ebeling, S.; Hennecke, H. !$#journal J. Gen. Microbiol. (1991) 137:991-1000 !$#title Cloning, sequencing, and mutational analysis of the !1Bradyrhizobium japonicum fumC-like gene: evidence for the !1existence of two different fumarases. !$#cross-references MUID:91311398; PMID:1856685 !$#accession A49760 !'##molecule_type DNA !'##residues 1-487 ##label ACU !'##cross-references GB:M79457 COMMENT In B. japonicum two fumarate hydratase genes have been !1found. This protein, the fumC-encoded fumarate hydratase, is !1a thermostable class II hydratase. GENETICS !$#gene fumC COMPLEX homotetramer FUNCTION !$#description catalyzes the stereospecific interconversion of fumarate and !1L-malate !$#pathway tricarboxylic acid cycle CLASSIFICATION #superfamily fumarate hydratase KEYWORDS carbon-oxygen lyase; homotetramer; hydro-lyase; !1tricarboxylic acid cycle SUMMARY #length 487 #molecular-weight 52593 #checksum 9469 SEQUENCE /// ENTRY UFBSD #type complete TITLE aspartate ammonia-lyase (EC 4.3.1.1) - Bacillus subtilis ALTERNATE_NAMES L-aspartase (ansB) ORGANISM #formal_name Bacillus subtilis DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jun-2000 ACCESSIONS B39440; A69586 REFERENCE A39440 !$#authors Sun, D.; Setlow, P. !$#journal J. Bacteriol. (1991) 173:3831-3845 !$#title Cloning, nucleotide sequence, and expression of the Bacillus !1subtilis ans operon, which codes for L-asparaginase and !1L-aspartase. !$#cross-references MUID:91267950; PMID:1711029 !$#accession B39440 !'##molecule_type DNA !'##residues 1-475 ##label SUN !'##cross-references GB:M63264; NID:g142516; PIDN:AAA22244.1; !1PID:g142518 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69586 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-475 ##label KUN !'##cross-references GB:Z99116; GB:AL009126; NID:g2634723; !1PIDN:CAB14289.1; PID:g2634792 !'##experimental_source strain 168 GENETICS !$#gene ansB; aspA CLASSIFICATION #superfamily fumarate hydratase KEYWORDS ammonia-lyase; carbon-nitrogen lyase SUMMARY #length 475 #molecular-weight 52553 #checksum 4018 SEQUENCE /// ENTRY UFECDW #type complete TITLE aspartate ammonia-lyase (EC 4.3.1.1) [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES aspartase ORGANISM #formal_name Escherichia coli DATE 17-Mar-1987 #sequence_revision 14-May-1999 #text_change 01-Mar-2002 ACCESSIONS A01159; S56367; S08588; A65224 REFERENCE A93560 !$#authors Takagi, J.S.; Ida, N.; Tokushige, M.; Sakamoto, H.; Shimura, !1Y. !$#journal Nucleic Acids Res. (1985) 13:2063-2074 !$#title Cloning and nucleotide sequence of the aspartase gene of !1Escherichia coli W. !$#cross-references MUID:85215599; PMID:2987841 !$#accession A01159 !'##molecule_type DNA; protein !'##residues 1-478 ##label TAK !'##cross-references GB:X02307; NID:g41001; PIDN:CAA26173.1; PID:g41002 !'##experimental_source strain W !'##note parts of this sequence, including the amino and carboxy ends of !1the mature protein, were determined by protein sequencing REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56367 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 'MCLKQIIGSLKKKVH',1-478 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97038.1; !1PID:g536983 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 !'##note an incorrect initiation codon was used REFERENCE S07138 !$#authors Woods, S.A.; Miles, J.S.; Roberts, R.E.; Guest, J.R. !$#journal Biochem. J. (1986) 237:547-557 !$#title Structural and functional relationships between fumarase and !1aspartase. Nucleotide sequences of the fumarase (fumC) and !1aspartase (aspA) genes of Escherichia coli K12. !$#cross-references MUID:87099873; PMID:3541901 !$#accession S08588 !'##molecule_type DNA !'##residues 1-31,'V',33-478 ##label WOO !'##cross-references EMBL:X04066; NID:g41006; PIDN:CAA27701.1; !1PID:g41008 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65224 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 'MCLKQIIGSLKKKVH',1-478 ##label BLAT !'##cross-references GB:AE000486; GB:U00096; NID:g1790574; !1PIDN:AAC77099.1; PID:g1790581; UWGP:b4139 !'##experimental_source strain K-12, substrain MG1655 !'##note an incorrect initiation codon was used REFERENCE A67622 !$#authors Shi, W.; Dunbar, J.; Farber, G.K. !$#submission submitted to the Brookhaven Protein Data Bank, February 1997 !$#cross-references PDB:1JSW !$#contents annotation; X-ray crystallography, 2.8 angstroms, residues !11-459 !$#note the structure was modeled with Met-1 which is not present in !1the mature protein REFERENCE A58956 !$#authors Shi, W.; Dunbar, J.; Jayasekera, M.M.K.; Viola, R.E.; !1Farber, G.K. !$#journal Biochemistry (1997) 36:9136-9144 !$#title The structure of L-aspartate ammonia-lyase from Escherichia !1coli. !$#cross-references MUID:97375637; PMID:9230045 !$#contents annotation; X-ray crystallography, 2.8 angstroms GENETICS !$#gene aspA !$#map_position 94 min COMPLEX homotetramer FUNCTION !$#description catalyzes the reversible conversion of aspartate to fumarate !1and ammonia CLASSIFICATION #superfamily fumarate hydratase KEYWORDS ammonia-lyase; carbon-nitrogen lyase; homotetramer FEATURE !$2-478 #product aspartate ammonia-lyase #status experimental !8#label MAT SUMMARY #length 478 #molecular-weight 52356 #checksum 3757 SEQUENCE /// ENTRY UFPSDF #type complete TITLE aspartate ammonia-lyase (EC 4.3.1.1) - Pseudomonas fluorescens ALTERNATE_NAMES aspartase ORGANISM #formal_name Pseudomonas fluorescens DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 31-Mar-2000 ACCESSIONS A24874 REFERENCE A24874 !$#authors Takagi, J.S.; Tokushige, M.; Shimura, Y. !$#journal J. Biochem. (1986) 100:697-705 !$#title Cloning and nucleotide sequence of the aspartase gene of !1Pseudomonas fluorescens. !$#cross-references MUID:87057132; PMID:3096982 !$#accession A24874 !'##molecule_type DNA !'##residues 1-478 ##label TAK !'##cross-references GB:X04441; NID:g45493; PIDN:CAA28037.1; PID:g45494 CLASSIFICATION #superfamily fumarate hydratase KEYWORDS ammonia-lyase; carbon-nitrogen lyase SUMMARY #length 478 #molecular-weight 51508 #checksum 8586 SEQUENCE /// ENTRY WZBSDS #type complete TITLE adenylosuccinate lyase (EC 4.3.2.2) - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jun-2000 ACCESSIONS C29326; A69684 REFERENCE A29326 !$#authors Ebbole, D.J.; Zalkin, H. !$#journal J. Biol. Chem. (1987) 262:8274-8287 !$#title Cloning and characterization of a 12-gene cluster from !1Bacillus subtilis encoding nine enzymes for de novo purine !1nucleotide synthesis. !$#cross-references MUID:87250425; PMID:3036807 !$#accession C29326 !'##molecule_type DNA !'##residues 1-431 ##label EBB !'##cross-references EMBL:J02732; NID:g143363; PIDN:AAA22676.1; !1PID:g143366 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69684 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-431 ##label KUN !'##cross-references GB:Z99107; GB:AL009126; NID:g2632866; !1PIDN:CAB12464.1; PID:g2632958 !'##experimental_source strain 168 GENETICS !$#gene purB !$#map_position 18 min CLASSIFICATION #superfamily fumarate hydratase KEYWORDS amidine-lyase; carbon-nitrogen lyase; purine nucleotide !1biosynthesis SUMMARY #length 431 #molecular-weight 49484 #checksum 6901 SEQUENCE /// ENTRY DWECDA #type complete TITLE dihydroxy-acid dehydratase (EC 4.2.1.9) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 01-Mar-2002 ACCESSIONS A27310; D26570; S48894; S30669; F65180 REFERENCE A91578 !$#authors Cox, J.L.; Cox, B.J.; Fidanza, V.; Calhoun, D.H. !$#journal Gene (1987) 56:185-198 !$#title The complete nucleotide sequence of the ilvGMEDA cluster of !1Escherichia coli K-12. !$#cross-references MUID:88056322; PMID:3315862 !$#accession A27310 !'##molecule_type DNA !'##residues 1-616 ##label COX !'##cross-references GB:M10313; GB:J01634; GB:J01635; GB:M17624; !1NID:g146457; PIDN:AAB59053.1; PID:g146461 !'##experimental_source strain K12 REFERENCE A26570 !$#authors Lawther, R.P.; Wek, R.C.; Lopes, J.M.; Pereira, R.; Taillon, !1B.E.; Hatfield, G.W. !$#journal Nucleic Acids Res. (1987) 15:2137-2155 !$#title The complete nucleotide sequence of the ilvGMEDA operon of !1Escherichia coli K-12. !$#cross-references MUID:87174741; PMID:3550695 !$#accession D26570 !'##molecule_type DNA !'##residues 1-163,'P',165-407,'VSARWNTPTA',418,'TAAWRCSTVILRKRLHRE', !1438-609,'H',611-616 ##label LAW1 !'##cross-references GB:M32253; NID:g146465; PIDN:AAA24023.1; !1PID:g146469 REFERENCE S48894 !$#authors Lawther, R.P. !$#submission submitted to the EMBL Data Library, December 1987 !$#accession S48894 !'##molecule_type DNA !'##residues 1-616 ##label LAW2 !'##cross-references EMBL:X04890; NID:g288528; PIDN:CAA28576.1; !1PID:g288532 REFERENCE S30660 !$#authors Daniels, D.L.; Plunkett III, G.; Burland, V.; Blattner, F.R. !$#journal Science (1992) 257:771-778 !$#title Analysis of the Escherichia coli genome: DNA sequence of the !1region from 84.5 to 86.5 minutes. !$#cross-references MUID:92358234; PMID:1379743 !$#accession S30669 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 'MVVI',22-23,'VLVRCGP',25-263,'X',265-616 ##label DAN !'##cross-references EMBL:M87049; NID:g836656; PIDN:AAA67574.1; !1PID:g148178 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1992 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65180 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 'MVVI',22-23,'VLVRCGP',25-616 ##label BLAT !'##cross-references GB:AE000453; GB:U00096; NID:g2367276; !1PIDN:AAC77491.1; PID:g1790206; UWGP:b3771 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ilvD !$#map_position 85 min COMPLEX homodimer FUNCTION !$#description catalyzes the dehydration of 2,3-dihydroxy-3-methylbutanoate !1to 3-methyl-2-oxobutanoate !$#pathway isoleucine-valine biosynthesis CLASSIFICATION #superfamily dihydroxy-acid dehydratase KEYWORDS carbon-oxygen lyase; homodimer; hydro-lyase; !1isoleucine-valine biosynthesis SUMMARY #length 616 #molecular-weight 65531 #checksum 5236 SEQUENCE /// ENTRY DWECDQ #type complete TITLE 3-dehydroquinate dehydratase (EC 4.2.1.10) aroD - Escherichia coli (strain K-12) ALTERNATE_NAMES 3-dehydroquinase ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 03-Oct-1995 #text_change 01-Mar-2002 ACCESSIONS S14750; S56119; A24508; E64927 REFERENCE S14749 !$#authors Chaudhuri, S.; Duncan, K.; Graham, L.D.; Coggins, J.R. !$#journal Biochem. J. (1991) 275:1-6 !$#title Identification of the active-site lysine residues of two !1biosynthetic 3-dehydroquinases. !$#cross-references MUID:91207275; PMID:1826831 !$#accession S14750 !'##molecule_type DNA !'##residues 1-252 ##label CHA !'##cross-references GB:X59503; NID:g40974; PIDN:CAA42091.1; PID:g40975 !$#accession S56119 !'##molecule_type protein !'##residues 162-169;171-172 ##label CHA2 REFERENCE A24508 !$#authors Duncan, K.; Chaudhuri, S.; Campbell, M.S.; Coggins, J.R. !$#journal Biochem. J. (1986) 238:475-483 !$#title The overexpression and complete amino acid sequence of !1Escherichia coli 3-dehydroquinase. !$#cross-references MUID:87099996; PMID:3541912 !$#accession A24508 !'##molecule_type DNA !'##residues 1-97,'YCTH',102-209,'E',211-221,'GGN',225,'WCG',229-230, !1'SVCARANLGK' ##label DUN !'##cross-references GB:X04306; NID:g40971; PIDN:CAA27849.1; PID:g40973 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64927 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-252 ##label BLAT !'##cross-references GB:AE000264; GB:U00096; NID:g1787978; !1PIDN:AAC74763.1; PID:g1787984; UWGP:b1693 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene aroD !$#map_position 37 min COMPLEX homodimer FUNCTION !$#description catalyzes the dehydration of 3-dehydroquinate to !13-dehydroshikimate !$#pathway shikimate pathway; aromatic amino acid biosynthesis CLASSIFICATION #superfamily 3-dehydroquinate dehydratase; 3-dehydroquinate !1dehydratase homology KEYWORDS aromatic amino acid biosynthesis; carbon-oxygen lyase; !1homodimer; hydro-lyase FEATURE !$19-239 #domain 3-dehydroquinate dehydratase homology #label !8DQD SUMMARY #length 252 #molecular-weight 27466 #checksum 7538 SEQUENCE /// ENTRY S15652 #type complete TITLE 3-dehydroquinate dehydratase (EC 4.2.1.10) aroD - Salmonella typhi ALTERNATE_NAMES 3-dehydroquinase ORGANISM #formal_name Salmonella typhi DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S15652 REFERENCE S15652 !$#authors Servos, S.; Chatfield, S.; Hone, D.; Levine, M.; !1Dimitriadis, G.; Pickard, D.; Dougan, G.; Fairweather, N.; !1Charles, I. !$#journal J. Gen. Microbiol. (1991) 137:147-152 !$#title Molecular cloning and characterization of the aroD gene !1encoding 3-dehydroquinase from Salmonella typhi. !$#cross-references MUID:91259034; PMID:2045778 !$#accession S15652 !'##molecule_type DNA !'##residues 1-252 ##label SER !'##cross-references EMBL:X54546; NID:g47641; PIDN:CAA38418.1; !1PID:g47642 GENETICS !$#gene aroD FUNCTION !$#description catalyzes the dehydration of 3-dehydroquinate to !13-dehydroshikimate !$#pathway shikimate pathway; aromatic amino acid biosynthesis CLASSIFICATION #superfamily 3-dehydroquinate dehydratase; 3-dehydroquinate !1dehydratase homology KEYWORDS aromatic amino acid biosynthesis; carbon-oxygen lyase; !1hydro-lyase FEATURE !$18-239 #domain 3-dehydroquinate dehydratase homology #label !8DQD SUMMARY #length 252 #molecular-weight 27623 #checksum 1044 SEQUENCE /// ENTRY S45563 #type complete TITLE 3-dehydroquinate dehydratase (EC 4.2.1.10) aroC - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 20-Oct-2000 ACCESSIONS S45563; H69589 REFERENCE S45533 !$#authors Sorokin, A.; Zumstein, E.; Azevedo, V.; Ehrlich, S.D.; !1Serror, P. !$#submission submitted to the EMBL Data Library, November 1993 !$#accession S45563 !'##molecule_type DNA !'##residues 1-255 ##label SOR !'##cross-references EMBL:L09228; NID:g410114; PIDN:AAA67501.1; !1PID:g410145 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69589 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-255 ##label KUN !'##cross-references GB:Z99116; GB:AL009126; NID:g2634723; !1PIDN:CAB14240.1; PID:g2634743 !'##experimental_source strain 168 GENETICS !$#gene aroC !$#start_codon GTG FUNCTION !$#description catalyzes the dehydration of 3-dehydroquinate to !13-dehydroshikimate !$#pathway shikimate pathway; aromatic amino acid biosynthesis CLASSIFICATION #superfamily 3-dehydroquinate dehydratase; 3-dehydroquinate !1dehydratase homology KEYWORDS aromatic amino acid biosynthesis; carbon-oxygen lyase; !1hydro-lyase FEATURE !$19-239 #domain 3-dehydroquinate dehydratase homology #label !8DQD SUMMARY #length 255 #molecular-weight 28131 #checksum 6359 SEQUENCE /// ENTRY D49939 #type complete TITLE hypothetical protein (ebsC 5' region) - Enterococcus faecalis ORGANISM #formal_name Enterococcus faecalis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 20-Oct-2000 ACCESSIONS D49939 REFERENCE A49939 !$#authors Bensing, B.A.; Dunny, G.M. !$#journal J. Bacteriol. (1993) 175:7421-7429 !$#title Cloning and molecular analysis of genes affecting expression !1of binding substance, the recipient-encoded receptor(s) !1mediating mating aggregate formation in Enterococcus !1faecalis. !$#cross-references MUID:94042918; PMID:8226689 !$#accession D49939 !'##status preliminary !'##molecule_type DNA !'##residues 1-253 ##label BEN !'##cross-references GB:L23802; NID:g388106; PIDN:AAC36854.1; !1PID:g388110 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily 3-dehydroquinate dehydratase; 3-dehydroquinate !1dehydratase homology FEATURE !$19-239 #domain 3-dehydroquinate dehydratase homology #label !8DQD SUMMARY #length 253 #molecular-weight 28085 #checksum 5519 SEQUENCE /// ENTRY NOHUG #type complete TITLE phosphopyruvate hydratase (EC 4.2.1.11) gamma - human ALTERNATE_NAMES enolase gamma; neuron-specific enolase ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 18-Jun-1999 ACCESSIONS JU0060; S16163; S02077; I56569; S02616; S38303 REFERENCE JU0060 !$#authors Oliva, D.; Barba, G.; Barbieri, G.; Giallongo, A.; Feo, S. !$#journal Gene (1989) 79:355-360 !$#title Cloning, expression and sequence homologies of cDNA for !1human gamma enolase. !$#cross-references MUID:90006764; PMID:2792767 !$#accession JU0060 !'##molecule_type mRNA !'##residues 1-434 ##label OL1 !'##cross-references GB:M22349; NID:g951199; PIDN:AAB59554.1; !1PID:g182116; GB:M27833 REFERENCE S16163 !$#authors Oliva, D.; Cali, L.; Feo, S.; Giallongo, A. !$#journal Genomics (1991) 10:157-165 !$#title Complete structure of the human gene encoding !1neuron-specific enolase. !$#cross-references MUID:91257823; PMID:2045099 !$#accession S16163 !'##molecule_type DNA !'##residues 1-434 ##label OL2 !'##cross-references GB:X51956; NID:g31164; PIDN:CAA36215.1; PID:g31165 REFERENCE S02077 !$#authors McAleese, S.M.; Dunbar, B.; Fothergill, J.E.; Hinks, L.J.; !1Day, I.N.M. !$#journal Eur. J. Biochem. (1988) 178:413-417 !$#title Complete amino acid sequence of the neurone-specific gamma !1isozyme of enolase (NSE) from human brain and comparison !1with the non-neuronal alpha form (NNE). !$#cross-references MUID:89091176; PMID:3208766 !$#accession S02077 !'##molecule_type mRNA !'##residues 2-3,'Q',5-239,'M',241-434 ##label MCA !'##cross-references EMBL:X13120; NID:g31145; PIDN:CAA31512.1; !1PID:g930063 !'##note part of this sequence was confirmed by protein sequencing !'##note 264-Ala and 395-Ala were also found REFERENCE I56569 !$#authors Van Obberghen, E.; Kamholz, J.; Bishop, J.G. !$#journal J. Neurosci. Res. (1988) 19:450-456 !$#title Human gamma enolase: isolation of a cDNA clone and !1expression in normal and tumor tissues of human origin. !$#cross-references MUID:88259288; PMID:3385803 !$#accession I56569 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 'GC',29-126,'N',128-434 ##label VAN !'##cross-references GB:M36768; NID:g182117; PIDN:AAA52388.1; !1PID:g182118 REFERENCE S02616 !$#authors Day, I.N.M.; Allsopp, M.T.E.P.; Moore, D.C.M.; Thompson, !1R.J. !$#journal FEBS Lett. (1987) 222:139-143 !$#title Sequence conservation in the 3'-untranslated regions of !1neurone-specific enolase, lymphokine and protooncogene !1mRNAs. !$#cross-references MUID:88005129; PMID:3653393 !$#accession S02616 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 425-434 ##label DAY !'##cross-references GB:Y00691; GB:M27610 REFERENCE S38303 !$#authors Harrington, C.R.; Quinn, G.B.; Hurt, J.; Day, I.N.M.; !1Wischik, C.M. !$#journal Biochim. Biophys. Acta (1993) 1158:120-128 !$#title Characterisation of an epitope specific to the !1neuron-specific isoform of human enolase recognised by a !1monoclonal antibody raised against a synthetic peptide !1corresponding to the C-terminus of beta/A4-protein. !$#cross-references MUID:94002176; PMID:7691181 !$#accession S38303 !'##molecule_type protein !'##residues 156-173 ##label HAR COMMENT Enolase occurs with at least three isoforms (alpha, beta, !1and gamma) in mammalian and avian tissues. The gamma form is !1found mainly in neuronal and neuroendocrine cells. COMMENT Thr-191 may be important for the enhanced tolerance to !1chloride ions of neuron-specific enolase. GENETICS !$#gene GDB:ENO2 !'##cross-references GDB:119872; OMIM:131360 !$#map_position 12p13-12p13 !$#introns 29/1; 61/1; 80/3; 104/1; 148/3; 223/1; 289/1; 356/2; 392/2; !1412/2 COMPLEX homodimer FUNCTION !$#description catalyzes the reversible dehydration of 2-phospho-D-glyceric !1acid to phosphoenolpyruvate !$#pathway gluconeogenesis; glycolysis CLASSIFICATION #superfamily enolase KEYWORDS blocked amino end; brain; carbon-oxygen lyase; !1gluconeogenesis; glycolysis; homodimer; hydro-lyase; !1magnesium FEATURE !$2-434 #product phosphopyruvate hydratase gamma #status !8predicted #label MAT\ !$2 #modified_site blocked amino end (Ser) (in mature !8form) (probably acetylated) #status experimental\ !$40 #binding_site magnesium 2 (Ser) #status predicted\ !$210,343 #active_site Glu, Lys #status predicted\ !$245,293,318 #binding_site magnesium 1 (Asp, Glu, Asp) #status !8predicted SUMMARY #length 434 #molecular-weight 47268 #checksum 8212 SEQUENCE /// ENTRY NOMSB #type complete TITLE phosphopyruvate hydratase (EC 4.2.1.11) beta - mouse ALTERNATE_NAMES enolase beta ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 18-Jun-1999 ACCESSIONS S17109; S18036; S29675; A33921 REFERENCE S17109 !$#authors Lamande, N.; Brosset, S.; Keller, A.; Lucas, M.; Lazar, M. !$#submission submitted to the EMBL Data Library, September 1991 !$#accession S17109 !'##molecule_type DNA !'##residues 1-434 ##label LAM !'##cross-references EMBL:X61600; NID:g50848; PIDN:CAA43797.1; !1PID:g50849 REFERENCE S18036 !$#authors Peterson, C.A.; Cho, M.; Rastinejad, F.; Blau, H.M. !$#submission submitted to the EMBL Data Library, October 1991 !$#description Beta-enolase: a gene expressed in undifferentiated postnatal !1myoblasts that does not require the MyoD family of !1regulators. !$#accession S18036 !'##molecule_type mRNA !'##residues 1-434 ##label PET !'##cross-references EMBL:X62667; NID:g50143; PIDN:CAA44540.1; !1PID:g50144 REFERENCE S29675 !$#authors Lazar, M.; Lamande, N.; Brosset, S.; Lucas, M.; Keller, A. !$#submission submitted to the EMBL Data Library, February 1991 !$#accession S29675 !'##status preliminary !'##molecule_type mRNA !'##residues 1-434 ##label LAZ !'##cross-references EMBL:X57747; NID:g50846; PIDN:CAA40913.1; !1PID:g50847 REFERENCE A33921 !$#authors Lamande, N.; Mazo, A.M.; Lucas, M.; Montarras, D.; Pinset, !1C.; Gros, F.; Legault-Demare, L.; Lazar, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:4445-4449 !$#title Murine muscle-specific enolase: cDNA cloning, sequence, and !1developmental expression. !$#cross-references MUID:89282789; PMID:2734297 !$#accession A33921 !'##status preliminary !'##molecule_type mRNA !'##residues 59-233,'NA',236-434 ##label LA2 !'##cross-references GB:M20745; NID:g193029; PIDN:AAA37554.1; !1PID:g387144 !'##experimental_source skeletal muscle GENETICS !$#introns 29/1; 61/1; 80/3; 104/1; 148/3; 223/1; 289/1; 356/2; 392/3; !1412/2 FUNCTION !$#description catalyzes the reversible dehydration of 2-phospho-D-glyceric !1acid to phosphoenolpyruvate !$#pathway gluconeogenesis; glycolysis CLASSIFICATION #superfamily enolase KEYWORDS carbon-carbon lyase; carbon-oxygen lyase; dimer; !1gluconeogenesis; glycolysis; hydro-lyase; magnesium FEATURE !$40 #binding_site magnesium 2 (Ser) #status predicted\ !$210,343 #active_site Glu, Lys #status predicted\ !$245,293,318 #binding_site magnesium 1 (Asp, Glu, Asp) #status !8predicted SUMMARY #length 434 #molecular-weight 47024 #checksum 3655 SEQUENCE /// ENTRY NOXL #type complete TITLE phosphopyruvate hydratase (EC 4.2.1.11) ENO1 - African clawed frog ALTERNATE_NAMES enolase ENO1 ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 18-Jun-1999 ACCESSIONS S00463 REFERENCE S00463 !$#authors Segil, N.; Shrutkowski, A.; Dworkin, M.B.; Dworkin-Rastl, E. !$#journal Biochem. J. (1988) 251:31-39 !$#title Enolase isoenzymes in adult and developing Xenopus laevis !1and characterization of a cloned enolase sequence. !$#cross-references MUID:88268812; PMID:3390159 !$#accession S00463 !'##molecule_type mRNA !'##residues 1-434 ##label SEG !'##cross-references EMBL:Y00718; NID:g64679; PIDN:CAA68706.1; !1PID:g64680 GENETICS !$#gene ENO1 FUNCTION !$#description catalyzes the reversible dehydration of 2-phospho-D-glyceric !1acid to phosphoenolpyruvate !$#pathway gluconeogenesis; glycolysis CLASSIFICATION #superfamily enolase KEYWORDS carbon-oxygen lyase; dimer; gluconeogenesis; glycolysis; !1hydro-lyase; magnesium FEATURE !$40 #binding_site magnesium 2 (Ser) #status predicted\ !$210,343 #active_site Glu, Lys #status predicted\ !$245,293,318 #binding_site magnesium 1 (Asp, Glu, Asp) #status !8predicted SUMMARY #length 434 #molecular-weight 47504 #checksum 7372 SEQUENCE /// ENTRY NOBY #type complete TITLE phosphopyruvate hydratase (EC 4.2.1.11) 1 [validated] - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES enolase 1; protein G9160; protein YGR254w ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1980 #sequence_revision 19-Jul-1996 #text_change 15-Sep-2000 ACCESSIONS S64586; A01147 REFERENCE S64577 !$#authors Agostoni Carbone, M.L.; Panzeri, L.; Melchioretto, P.; !1Carignani, G.; Feroli, F.; Frontali, L.; Mazzoni, C.; !1Rinaldi, T.; Ruzzi, M. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64586 !'##molecule_type DNA !'##residues 1-437 ##label AGO !'##cross-references EMBL:Z73039; NID:g1323461; PIDN:CAA97283.1; !1PID:g1323462; GSPDB:GN00007; MIPS:YGR254w !'##experimental_source strain S288C REFERENCE A92300 !$#authors Holland, M.J.; Holland, J.P.; Thill, G.P.; Jackson, K.A. !$#journal J. Biol. Chem. (1981) 256:1385-1395 !$#title The primary structure of two yeast enolase genes. Homology !1between the 5' noncoding regions of yeast enolase and !1glyceraldehyde-3-phosphate dehydrogenase genes. !$#cross-references MUID:81094138; PMID:6256394 !$#accession A01147 !'##molecule_type DNA !'##residues 1-241,'V',243-437 ##label HOL !'##cross-references EMBL:J01322; NID:g171454; PIDN:AAA88712.1; !1PID:g171455 !'##experimental_source strain F1 REFERENCE A92299 !$#authors Chin, C.C.Q.; Brewer, J.M.; Wold, F. !$#journal J. Biol. Chem. (1981) 256:1377-1384 !$#title The amino acid sequence of yeast enolase. !$#cross-references MUID:81094137; PMID:7005235 !$#contents annotation !$#note the identity and sequence of at least 427 of the 436 !1residues are consistent with the sequence shown REFERENCE A66300 !$#authors Larsen, T.M.; Wedekind, J.E.; Rayment, I.; Reed, G.H. !$#submission submitted to the Brookhaven Protein Data Bank, December 1995 !$#cross-references PDB:1ONE !$#contents annotation; X-ray crystallography, 1.8 angstroms, residues !12-241,'V',243-437 REFERENCE A58593 !$#authors Larsen, T.M.; Wedekind, J.E.; Rayment, I.; Reed, G.H. !$#journal Biochemistry (1996) 35:4349-434358 !$#title A carboxylate oxygen of the substrate bridges the magnesium !1ions at the active site of enolase: structure of the yeast !1enzyme complexed with the equilibrium mixture of !12-phosphoglycerate and phosphoenolpyruvate at 1.8 a !1resulution. !$#cross-references MUID:96183295; PMID:8605183 !$#contents annotation; X-ray crystallography, 1.8 angstroms GENETICS !$#gene SGD:ENO1; ENOA; HSP48; MIPS:YGR254w !'##cross-references SGD:S0003486; MIPS:YGR254w !$#map_position 7R COMPLEX homodimer FUNCTION !$#description catalyzes the reversible dehydration of 2-phospho-D-glyceric !1acid to phosphoenolpyruvate !$#pathway gluconeogenesis; glycolysis !$#note magnesium required for catalysis and for stabilizing the !1dimer CLASSIFICATION #superfamily enolase KEYWORDS carbon-oxygen lyase; gluconeogenesis; glycolysis; homodimer; !1hydro-lyase; magnesium FEATURE !$2-437 #product enolase 1 #status experimental #label MAT\ !$40 #binding_site magnesium 2 (Ser) #status experimental\ !$212,346 #active_site Glu, Lys #status predicted\ !$247,296,321 #binding_site magnesium 1 (Asp, Glu, Asp) #status !8experimental SUMMARY #length 437 #molecular-weight 46816 #checksum 4243 SEQUENCE /// ENTRY NOBY2 #type complete TITLE phosphopyruvate hydratase (EC 4.2.1.11) 2 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES enolase 2; protein YHR174w ORGANISM #formal_name Saccharomyces cerevisiae DATE 18-Aug-1982 #sequence_revision 30-Jun-1992 #text_change 23-Mar-2001 ACCESSIONS A01148; S48913 REFERENCE A92300 !$#authors Holland, M.J.; Holland, J.P.; Thill, G.P.; Jackson, K.A. !$#journal J. Biol. Chem. (1981) 256:1385-1395 !$#title The primary structure of two yeast enolase genes. Homology !1between the 5' noncoding regions of yeast enolase and !1glyceraldehyde-3-phosphate dehydrogenase genes. !$#cross-references MUID:81094138; PMID:6256394 !$#accession A01148 !'##molecule_type DNA !'##residues 1-437 ##label HOL !'##cross-references EMBL:J01323; NID:g171456; PIDN:AAA88713.1; !1PID:g171457 REFERENCE S46673 !$#authors Macri, C. !$#submission submitted to the EMBL Data Library, February 1994 !$#description The sequence of S. cerevisiae cosmid 9986. !$#accession S48913 !'##molecule_type DNA !'##residues 1-437 ##label MAC !'##cross-references EMBL:U00027; NID:g551319; PIDN:AAB68019.1; !1PID:g458897; GSPDB:GN00008; MIPS:YHR174w GENETICS !$#gene SGD:ENO2; ENOB; MIPS:YHR174w !'##cross-references SGD:S0001217; MIPS:YHR174w !$#map_position 8R FUNCTION !$#description catalyzes the reversible dehydration of 2-phospho-D-glyceric !1acid to phosphoenolpyruvate CLASSIFICATION #superfamily enolase KEYWORDS carbon-oxygen lyase; gluconeogenesis; glycolysis; homodimer; !1hydro-lyase; magnesium FEATURE !$2-437 #product phosphopyruvate hydratase 2 #status !8predicted #label MAT\ !$40 #binding_site magnesium 2 (Ser) #status predicted\ !$212,346 #active_site Glu, Lys #status predicted\ !$247,296,321 #binding_site magnesium 1 (Asp, Glu, Asp) #status !8predicted SUMMARY #length 437 #molecular-weight 46914 #checksum 4064 SEQUENCE /// ENTRY NOEC #type complete TITLE phosphopyruvate hydratase (EC 4.2.1.11) - Escherichia coli (strain K-12) ALTERNATE_NAMES 2-phosphoglycerate dehydratase; enolase ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 30-Sep-1997 #text_change 01-Mar-2002 ACCESSIONS G65059; B25608 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65059 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-432 ##label BLAT !'##cross-references GB:AE000361; GB:U00096; NID:g2367160; !1PIDN:AAC75821.1; PID:g1789141; UWGP:b2779 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A92584 !$#authors Weng, M.; Makaroff, C.A.; Zalkin, H. !$#journal J. Biol. Chem. (1986) 261:5568-5574 !$#title Nucleotide sequence of Escherichia coli pyrG encoding CTP !1synthetase. !$#cross-references MUID:86168304; PMID:3514618 !$#accession B25608 !'##molecule_type DNA !'##residues 1-123 ##label WEN COMMENT This enzyme, a dimer of identical chains, catalyzes the !1formation of phosphoenolpyruvate in the glycolytic pathway. !1Magnesium is required for catalysis and stabilization of the !1enzyme. GENETICS !$#gene eno !$#map_position 60 min FUNCTION !$#description catalyzes the reversible dehydration of 2-phospho-D-glyceric !1acid to phosphoenolpyruvate CLASSIFICATION #superfamily enolase KEYWORDS carbon-oxygen lyase; gluconeogenesis; glycolysis; homodimer; !1hydro-lyase; magnesium SUMMARY #length 432 #molecular-weight 45655 #checksum 3164 SEQUENCE /// ENTRY NOHSM #type complete TITLE phosphopyruvate hydratase (EC 4.2.1.11) - Haloarcula marismortui ALTERNATE_NAMES enolase ORGANISM #formal_name Haloarcula marismortui DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 18-Jun-1999 ACCESSIONS F41715 REFERENCE A41715 !$#authors Kroemer, W.J.; Arndt, E. !$#journal J. Biol. Chem. (1991) 266:24573-24579 !$#title Halobacterial S9 operon. Three ribosomal protein genes are !1cotranscribed with genes encoding a tRNA(leu), the enolase, !1and a putative membrane protein in the archaebacterium !1Haloarcula (halobacterium) marismortui. !$#cross-references MUID:92105119; PMID:1840597 !$#accession F41715 !'##molecule_type DNA !'##residues 1-400 ##label KRO !'##cross-references GB:M76567; NID:g148775; PIDN:AAA73101.1; !1PID:g148781 FUNCTION !$#description catalyzes the reversible dehydration of 2-phospho-D-glyceric !1acid to phosphoenolpyruvate !$#pathway gluconeogenesis; glycolysis CLASSIFICATION #superfamily enolase KEYWORDS carbon-oxygen lyase; gluconeogenesis; glycolysis; !1hydro-lyase; magnesium FEATURE !$42 #binding_site magnesium 2 (Ser) #status predicted\ !$195,326 #active_site Glu, Lys #status predicted\ !$231,274,301 #binding_site magnesium 1 (Asp, Glu, Asp) #status !8predicted SUMMARY #length 400 #molecular-weight 41986 #checksum 4239 SEQUENCE /// ENTRY A24102 #type complete TITLE alanine racemase (EC 5.1.1.1), biosynthetic - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 23-Aug-1987 #sequence_revision 23-May-1997 #text_change 18-Jun-1999 ACCESSIONS A24102 REFERENCE A24102 !$#authors Galakatos, N.G.; Daub, E.; Botstein, D.; Walsh, C.T. !$#journal Biochemistry (1986) 25:3255-3260 !$#title Biosynthetic alanine racemase of Salmonella typhimurium: !1purification and characterization of the enzyme encoded by !1the alr gene. !$#cross-references MUID:86269906; PMID:3524676 !$#accession A24102 !'##molecule_type DNA !'##residues 1-359 ##label GAL !'##cross-references GB:M12847; NID:g153864; PIDN:AAA27022.1; !1PID:g153865 GENETICS !$#gene alr !$#map_position 91 CLASSIFICATION #superfamily alanine racemase KEYWORDS isomerase; phosphoprotein; pyridoxal phosphate FEATURE !$34 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 359 #molecular-weight 39075 #checksum 30 SEQUENCE /// ENTRY PC1296 #type complete TITLE alanine racemase (EC 5.1.1.1), biosynthetic - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 14-Jul-1994 #sequence_revision 30-Sep-1997 #text_change 01-Mar-2002 ACCESSIONS D65213; PC1296 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65213 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-359 ##label BLAT !'##cross-references GB:AE000478; GB:U00096; NID:g2367339; !1PIDN:AAC77023.1; PID:g1790487; UWGP:b4053 !'##experimental_source strain K-12, substrain MG1655 REFERENCE PC1295 !$#authors Lilley, P.E.; Stamford, N.P.J.; Vasudevan, S.G.; Dixon, N.E. !$#journal Gene (1993) 129:9-16 !$#title The 92-min region of the Escherichia coli chromosome: !1location and cloning of the ubiA and alr genes. !$#cross-references MUID:93328130; PMID:8335265 !$#accession PC1296 !'##molecule_type DNA !'##residues 1-23,'V',25-26;320-359 ##label LIL GENETICS !$#gene alr !$#map_position 92 min CLASSIFICATION #superfamily alanine racemase KEYWORDS isomerase; phosphoprotein; pyridoxal phosphate FEATURE !$34 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 359 #molecular-weight 39153 #checksum 550 SEQUENCE /// ENTRY E64130 #type complete TITLE alanine racemase (EC 5.1.1.1), biosynthetic - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 18-Aug-1995 #sequence_revision 23-May-1997 #text_change 18-Jun-1999 ACCESSIONS E64130 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession E64130 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-360 ##label TIGR !'##cross-references GB:U32831; GB:L42023; NID:g1574407; !1PIDN:AAC23218.1; PID:g1574412; TIGR:HI1575 GENETICS !$#gene alr CLASSIFICATION #superfamily alanine racemase KEYWORDS isomerase; phosphoprotein; pyridoxal phosphate FEATURE !$36 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 360 #molecular-weight 39705 #checksum 7017 SEQUENCE /// ENTRY A29519 #type complete TITLE alanine racemase (EC 5.1.1.1) precursor, catabolic - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 28-Dec-1987 #sequence_revision 23-May-1997 #text_change 18-Jun-1999 ACCESSIONS A29519 REFERENCE A29519 !$#authors Wasserman, S.A.; Daub, E.; Grisafi, P.; Botstein, D.; Walsh, !1C.T. !$#journal Biochemistry (1984) 23:5182-5187 !$#title Catabolic alanine racemase from Salmonella typhimurium: DNA !1sequence, enzyme purification, and characterization. !$#cross-references MUID:85072808; PMID:6391537 !$#accession A29519 !'##molecule_type DNA !'##residues 1-356 ##label WAS !'##cross-references GB:K02119; NID:g153938; PIDN:AAA27054.1; !1PID:g153939 REFERENCE A29520 !$#authors Roise, D.; Soda, K.; Yagi, T.; Walsh, C.T. !$#journal Biochemistry (1984) 23:5195-5201 !$#title Inactivation of the Pseudomonas striata broad specificity !1amino acid racemase by D and L isomers of beta-substituted !1alanines: kinetics, stoichiometry, active site peptide, and !1mechanistic studies. !$#cross-references MUID:85072810; PMID:6439237 !$#contents annotation; active site peptide GENETICS !$#gene dadB CLASSIFICATION #superfamily alanine racemase KEYWORDS isomerase; monomer; phosphoprotein; pyridoxal phosphate FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-356 #product alanine racemase, catabolic #status !8predicted #label MAT\ !$35 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status experimental SUMMARY #length 356 #molecular-weight 38804 #checksum 1496 SEQUENCE /// ENTRY C53383 #type complete TITLE alanine racemase (EC 5.1.1.1) precursor, catabolic - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 25-Aug-1995 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS C64865; C53383 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64865 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-356 ##label BLAT !'##cross-references GB:AE000217; GB:U00096; NID:g1787434; !1PIDN:AAC74274.1; PID:g1787439; UWGP:b1190 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A53383 !$#authors Lobocka, M.; Hennig, J.; Wild, J.; Klopotowski, T. !$#journal J. Bacteriol. (1994) 176:1500-1510 !$#title Organization and expression of the Escherichia coli K-12 dad !1operon encoding the smaller subunit of D-amino acid !1dehydrogenase and the catabolic alanine racemase. !$#cross-references MUID:94156858; PMID:7906689 !$#accession C53383 !'##molecule_type DNA !'##residues 1-171,'R',173-214,'R',216-280,'L',282-348,'V',350-356 !1##label LOB !'##cross-references GB:L02948; NID:g145701; PIDN:AAC36881.1; !1PID:g145704 !'##experimental_source strain K-12 GENETICS !$#gene dadX; dadB; alnB CLASSIFICATION #superfamily alanine racemase KEYWORDS isomerase; monomer; phosphoprotein; pyridoxal phosphate FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-356 #product alanine racemase, catabolic #status !8predicted #label MAT\ !$35 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 356 #molecular-weight 38844 #checksum 8665 SEQUENCE /// ENTRY A29984 #type complete TITLE alanine racemase (EC 5.1.1.1) - Bacillus stearothermophilus ORGANISM #formal_name Bacillus stearothermophilus DATE 15-Dec-1988 #sequence_revision 23-May-1997 #text_change 18-Jun-1999 ACCESSIONS A29984; A60471; A29521 REFERENCE A29984 !$#authors Tanizawa, K.; Ohshima, A.; Scheidegger, A.; Inagaki, K.; !1Tanaka, H.; Soda, K. !$#journal Biochemistry (1988) 27:1311-1316 !$#title Thermostable alanine racemase from Bacillus !1stearothermophilus: DNA and protein sequence determination !1and secondary structure prediction. !$#cross-references MUID:88209488; PMID:2835089 !$#accession A29984 !'##molecule_type DNA !'##residues 1-386 ##label TAN !'##cross-references GB:M19142; NID:g142466; PIDN:AAA22220.1; !1PID:g142467 REFERENCE A60471 !$#authors Faraci, W.S.; Walsh, C.T. !$#journal Biochemistry (1989) 28:431-437 !$#title Mechanism of inactivation of alanine racemase by beta,beta, !1beta-trifluoroalanine. !$#cross-references MUID:89229030; PMID:2496744 !$#accession A60471 !'##molecule_type protein !'##residues 31-38,'X',40-43 ##label FAR REFERENCE A29521 !$#authors Badet, B.; Inagaki, K.; Soda, K.; Walsh, C.T. !$#journal Biochemistry (1986) 25:3275-3282 !$#title Time-dependent inhibition of Bacillus stearothermophilus !1alanine racemase by (1-aminoethyl) phosphonate isomers by !1isomerization to noncovalent slowly dissociating enzyme- !1(1-aminoethyl) phosphonate complexes. !$#cross-references MUID:86269909; PMID:3730360 !$#accession A29521 !'##molecule_type protein !'##residues 36,'PP',39-43 ##label BAD COMMENT This enzyme catalyzes the racemization of L-alanine to !1D-alanine for synthesis of the cell wall. CLASSIFICATION #superfamily alanine racemase KEYWORDS isomerase; phosphoprotein; pyridoxal phosphate FEATURE !$39 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status experimental SUMMARY #length 386 #molecular-weight 43341 #checksum 5442 SEQUENCE /// ENTRY JS0443 #type complete TITLE alanine racemase (EC 5.1.1.1) - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 07-Sep-1990 #sequence_revision 23-May-1997 #text_change 16-Jun-2000 ACCESSIONS JS0443; G69612 REFERENCE JS0443 !$#authors Ferrari, E.; Henner, D.J.; Yang, M.Y. !$#journal Bio/Technology (1985) 3:1003-1007 !$#title Isolation of an alanine racemase gene from Bacillus subtilis !1and its use for plasmid maintenance in B. subtilis. !$#accession JS0443 !'##molecule_type DNA !'##residues 1-389 ##label FER !'##cross-references EMBL:M16207; NID:g142821; PIDN:AAA22378.1; !1PID:g142822 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69612 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-39,'V',41-65,'V',67-389 ##label KUN !'##cross-references GB:Z99106; GB:AL009126; NID:g2632653; !1PIDN:CAB12271.1; PID:g2632764 !'##experimental_source strain 168 GENETICS !$#gene dal FUNCTION !$#description catalyzes the racemic interconversion of L-alanine and !1D-alanine !$#pathway cell wall synthesis CLASSIFICATION #superfamily alanine racemase KEYWORDS cell wall synthesis; isomerase; phosphoprotein; pyridoxal !1phosphate FEATURE !$41 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 389 #molecular-weight 43327 #checksum 9391 SEQUENCE /// ENTRY S72995 #type complete TITLE alanine racemase (EC 5.1.1.1) - Mycobacterium leprae ALTERNATE_NAMES B229_C3_243 protein ORGANISM #formal_name Mycobacterium leprae DATE 19-Mar-1997 #sequence_revision 23-May-1997 #text_change 23-Mar-2001 ACCESSIONS S72995 REFERENCE S72588 !$#authors Smith, D.R.; Robison, K. !$#submission submitted to the EMBL Data Library, November 1993 !$#description Mycobacterium leprae cosmid B229. !$#accession S72995 !'##molecule_type DNA !'##residues 1-388 ##label SMI !'##cross-references EMBL:U00020; NID:g467102; PIDN:AAA17309.1; !1PID:g467127 GENETICS !$#gene alr !$#start_codon TTG CLASSIFICATION #superfamily alanine racemase KEYWORDS isomerase; phosphoprotein; pyridoxal phosphate FEATURE !$44 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 388 #molecular-weight 41083 #checksum 5142 SEQUENCE /// ENTRY S75775 #type complete TITLE alanine racemase (EC 5.1.1.1) - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein slr0827 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 25-Apr-1997 #sequence_revision 23-May-1997 #text_change 16-Jun-2000 ACCESSIONS S75775 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75775 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-400 ##label KAN !'##cross-references EMBL:D64003; GB:AB001339; NID:g1001200; !1PIDN:BAA10510.1; PID:g1001266 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 COMMENT This enzyme catalyzes the racemization of L-alanine to !1D-alanine for synthesis of the cell wall. GENETICS !$#gene alr CLASSIFICATION #superfamily alanine racemase KEYWORDS isomerase; phosphoprotein; pyridoxal phosphate FEATURE !$65 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 400 #molecular-weight 43691 #checksum 3300 SEQUENCE /// ENTRY S74824 #type complete TITLE glutamate racemase (EC 5.1.1.3) - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein slr1746 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S74824 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74824 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-279 ##label KAN !'##cross-references EMBL:D90909; GB:AB001339; NID:g1652844; !1PIDN:BAA17785.1; PID:g1652867 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene murI CLASSIFICATION #superfamily glutamate racemase KEYWORDS isomerase SUMMARY #length 279 #molecular-weight 31274 #checksum 44 SEQUENCE /// ENTRY S72790 #type complete TITLE glutamate racemase (EC 5.1.1.3) - Mycobacterium leprae ALTERNATE_NAMES B1549_C2_210 protein ORGANISM #formal_name Mycobacterium leprae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 23-Mar-2001 ACCESSIONS S72790 REFERENCE S72582 !$#authors Smith, D.R.; Robison, K. !$#submission submitted to the EMBL Data Library, November 1993 !$#description Mycobacterium leprae cosmid B1549. !$#accession S72790 !'##status preliminary !'##molecule_type DNA !'##residues 1-272 ##label SMI !'##cross-references EMBL:U00014; NID:g466903; PIDN:AAA50890.1; !1PID:g466915 GENETICS !$#gene murI CLASSIFICATION #superfamily glutamate racemase KEYWORDS isomerase SUMMARY #length 272 #molecular-weight 28855 #checksum 8139 SEQUENCE /// ENTRY JC4005 #type complete TITLE glutamate racemase (EC 5.1.1.3) - Lactobacillus brevis ORGANISM #formal_name Lactobacillus brevis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS JC4005; PC4010 REFERENCE JC4005 !$#authors Yagasaki, M.; Iwata, K.; Ishino, S.; Azuma, M.; Ozaki, A. !$#journal Biosci. Biotechnol. Biochem. (1995) 59:610-614 !$#title Cloning, purification, and properties of a !1cofactor-independent glutamate racemase from Lactobacillus !1brevis ATCC 8287. !$#cross-references MUID:95290755; PMID:7772825 !$#accession JC4005 !'##molecule_type DNA !'##residues 1-276 ##label YAG !'##cross-references DDBJ:D29627; NID:g468449; PIDN:BAA06106.1; !1PID:g468450 !$#accession PC4010 !'##molecule_type protein !'##residues 1-10 ##label YA2 !'##experimental_source ATCC 8287 CLASSIFICATION #superfamily glutamate racemase KEYWORDS glutamate biosynthesis; isomerase SUMMARY #length 276 #molecular-weight 29428 #checksum 6732 SEQUENCE /// ENTRY A49473 #type complete TITLE glutamate racemase (EC 5.1.1.3) - Lactobacillus fermentum ORGANISM #formal_name Lactobacillus fermentum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 24-Sep-1999 ACCESSIONS A49473 REFERENCE A49473 !$#authors Gallo, K.A.; Knowles, J.R. !$#journal Biochemistry (1993) 32:3981-3990 !$#title Purification, cloning, and cofactor independence of !1glutamate racemase from Lactobacillus. !$#cross-references MUID:93229497; PMID:8385993 !$#contents ATCC 9338 !$#accession A49473 !'##status preliminary !'##molecule_type DNA; protein !'##residues 1-268 ##label GAL !'##cross-references GB:L02916; NID:g149548; PIDN:AAA25241.1; !1PID:g149549 !'##note sequence extracted from NCBI backbone (NCBIN:129591, !1NCBIP:129593) CLASSIFICATION #superfamily glutamate racemase KEYWORDS isomerase SUMMARY #length 268 #molecular-weight 28313 #checksum 1363 SEQUENCE /// ENTRY E64588 #type complete TITLE glutamate racemase (EC 5.1.1.3) - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS E64588 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession E64588 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-255 ##label TOM !'##cross-references GB:AE000569; GB:AE000511; NID:g2313663; !1PIDN:AAD07615.1; PID:g2313665; TIGR:HP0549 CLASSIFICATION #superfamily glutamate racemase KEYWORDS isomerase SUMMARY #length 255 #molecular-weight 28413 #checksum 747 SEQUENCE /// ENTRY DWECL #type complete TITLE L-serine ammonia-lyase (EC 4.3.1.17) 1 - Escherichia coli (strain K-12) ALTERNATE_NAMES L-serine deaminase 1 ORGANISM #formal_name Escherichia coli DATE 30-Jun-1991 #sequence_revision 21-Nov-1997 #text_change 21-Jun-2002 ACCESSIONS F64942; JV0036 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64942 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-454 ##label BLAT !'##cross-references GB:AE000275; GB:U00096; NID:g1788106; !1PIDN:AAC74884.1; PID:g1788116; UWGP:b1814 !'##experimental_source strain K-12, substrain MG1655 REFERENCE JV0036 !$#authors Su, H.; Lang, B.F.; Newman, E.B. !$#journal J. Bacteriol. (1989) 171:5095-5102 !$#title L-serine degradation in Escherichia coli K-12: cloning and !1sequencing of the sdaA gene. !$#cross-references MUID:89359152; PMID:2504697 !$#accession JV0036 !'##molecule_type DNA !'##residues 7-219,'N',221-454 ##label SUH !'##cross-references GB:M28695 !'##experimental_source strain K12 COMMENT This enzyme converts L-serine to pyruvate. GENETICS !$#gene sdaA CLASSIFICATION #superfamily microbial L-serine dehydratase KEYWORDS ammonia-lyase; carbon-nitrogen lyase; carbon-oxygen lyase; !1gluconeogenesis; hydro-lyase; pyridoxal phosphate; serine !1catabolism SUMMARY #length 454 #molecular-weight 48906 #checksum 2174 SEQUENCE /// ENTRY DWECS #type complete TITLE D-serine ammonia-lyase (EC 4.3.1.18) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Nov-1980 #sequence_revision 31-Oct-1997 #text_change 30-Jun-2002 ACCESSIONS C65010; A31784; A01149 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65010 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-442 ##label BLAT !'##cross-references GB:AE000324; GB:U00096; NID:g1788694; !1PIDN:AAC75425.1; PID:g1788708; UWGP:b2366 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A31784 !$#authors Marceau, M.; McFall, E.; Lewis, S.D.; Shafer, J.A. !$#journal J. Biol. Chem. (1988) 263:16926-16933 !$#title D-Serine dehydratase from Escherichia coli. DNA sequence and !1identification of catalytically inactive glycine to aspartic !1acid variants. !$#cross-references MUID:89034190; PMID:3053699 !$#accession A31784 !'##molecule_type DNA !'##residues 1-203,'T',205-442 ##label MAR !'##cross-references GB:J01603 REFERENCE A01149 !$#authors Schiltz, E.; Schmitt, W. !$#journal FEBS Lett. (1981) 134:57-62 !$#title Sequence of Escherichia coli D-serine dehydratase. !$#cross-references MUID:97365497; PMID:9222324 !$#accession A01149 !'##molecule_type protein !'##residues 1-33,'T',35-161,'YXXXXXY',162-442 ##label SCH !'##experimental_source strain K12, mutant C6 !'##note this enzyme, in contrast to other PLP-dependent enzymes, is a !1monomer GENETICS !$#gene dsdA !$#map_position 51 min CLASSIFICATION #superfamily D-serine dehydratase KEYWORDS ammonia-lyase; carbon-nitrogen lyase; carbon-oxygen lyase; !1hydro-lyase; phosphoprotein; pyridoxal phosphate FEATURE !$118 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status experimental SUMMARY #length 442 #molecular-weight 47900 #checksum 7514 SEQUENCE /// ENTRY DWHUT #type complete TITLE L-serine ammonia-lyase (EC 4.3.1.17) - human ALTERNATE_NAMES L-serine deaminase; threonine deaminase CONTAINS threonine ammonia-lyase (EC 4.3.1.19) ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 19-Jul-2002 ACCESSIONS A34232 REFERENCE A34232 !$#authors Ogawa, H.; Gomi, T.; Konishi, K.; Date, T.; Nakashima, H.; !1Nose, K.; Matsuda, Y.; Peraino, C.; Pitot, H.C.; Fujioka, M. !$#journal J. Biol. Chem. (1989) 264:15818-15823 !$#title Human liver serine dehydratase. cDNA cloning and sequence !1homology with hydroxyamino acid dehydratases from other !1sources. !$#cross-references MUID:89380167; PMID:2674117 !$#accession A34232 !'##molecule_type mRNA !'##residues 1-328 ##label OGA !'##cross-references GB:J05037; NID:g338029; PIDN:AAA36604.1; !1PID:g338030 !'##note the authors translated the codon TGT for residue 183 as Val and !1TGG for residue 270 as Cys COMMENT This enzyme catalyzes the pyridoxal phosphate-dependent !1conversion of L-serine to pyruvate and ammonia. In mammals, !1it is found predominantly in the liver. The rat liver enzyme !1is thought to be identical with threonine dehydratase (EC !14.2.1.16). GENETICS !$#gene GDB:SDS; SDH !'##cross-references GDB:9600595; OMIM:182128 !$#map_position 12pter-12qter CLASSIFICATION #superfamily threonine dehydratase KEYWORDS ammonia-lyase; carbon-nitrogen lyase; carbon-oxygen lyase; !1gluconeogenesis; homodimer; hydro-lyase; liver; !1phosphoprotein; pyridoxal phosphate; serine catabolism FEATURE !$41 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 328 #molecular-weight 34702 #checksum 5735 SEQUENCE /// ENTRY DWRTT #type complete TITLE L-serine ammonia-lyase (EC 4.3.1.17) - rat ALTERNATE_NAMES L-serine deaminase; threonine deaminase CONTAINS threonine ammonia-lyase (EC 4.3.1.19) ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 19-Jul-2002 ACCESSIONS S01009; S04508 REFERENCE S01009 !$#authors Noda, C.; Ito, K.; Nakamura, T.; Ichihara, A. !$#journal FEBS Lett. (1988) 234:331-335 !$#title Primary structure of rat liver serine dehydratase deduced !1from the cDNA sequence. !$#cross-references MUID:88271652; PMID:3391277 !$#accession S01009 !'##molecule_type mRNA !'##residues 1-327 ##label NOD !'##cross-references EMBL:Y00752; NID:g57224; PIDN:CAA68721.1; !1PID:g57225 !'##note the authors translated the codon CAG for residue 178 as Glu, !1AAC for residue 226 as Asp, and GCC for residue 289 as Gly REFERENCE S04508 !$#authors Ogawa, H.; Konishi, K.; Fujioka, M. !$#journal Biochim. Biophys. Acta (1989) 996:139-141 !$#title The peptide sequences near the bound pyridoxal phosphate are !1conserved in serine dehydratase from rat liver, and !1threonine dehydratases from yeast and Escherichia coli. !$#cross-references MUID:89287351; PMID:2660911 !$#accession S04508 !'##molecule_type protein !'##residues 2-5;31-50 ##label OGA !'##experimental_source strain Wistar GENETICS !$#gene SDH2 FUNCTION SDH !$#description as L-serine dehydratase (EC 4.2.1.13) catalyzes the !1conversion of L-serine to pyruvate and ammonia FUNCTION TDH !$#description as L-threonine dehydratase (EC 4.2.1.13) catalyzes the !1conversion of L-threonine to 2-oxobutanoate and ammonia CLASSIFICATION #superfamily threonine dehydratase KEYWORDS acetylated amino end; ammonia-lyase; carbon-nitrogen lyase; !1carbon-oxygen lyase; gluconeogenesis; homodimer; !1hydro-lyase; liver; phosphoprotein; pyridoxal phosphate; !1serine catabolism FEATURE !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental\ !$41 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status experimental SUMMARY #length 327 #molecular-weight 34468 #checksum 3589 SEQUENCE /// ENTRY DWBYLH #type complete TITLE L-serine ammonia-lyase (EC 4.3.1.17) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YCL064c CONTAINS threonine ammonia-lyase (EC 4.3.1.19) ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-Jul-2002 ACCESSIONS S19395; S40889; S19746 REFERENCE S19391 !$#authors Rasmussen, S.W.; von Wettstein, D. !$#submission submitted to the Protein Sequence Database, March 1992 !$#accession S19395 !'##molecule_type DNA !'##residues 1-202 ##label RAS !'##cross-references EMBL:X59720; GSPDB:GN00003; MIPS:YCL064c REFERENCE S40889 !$#authors Bornaes, C.; Petersen, J.G.L.; Holmberg, S. !$#journal Genetics (1992) 131:531-539 !$#title Serine and threonine catabolism in Saccharomyces cerevisiae: !1the CHA1 polypeptide is homologous with other serine and !1threonine dehydratases. !$#cross-references MUID:92331893; PMID:1628804 !$#accession S40889 !'##molecule_type DNA !'##residues 1-33,'A',35-360 ##label BOR !'##cross-references EMBL:M85194; NID:g172588; PIDN:AAA35040.1; !1PID:g172589 !'##note the authors translated the codon GCC for residue 34 as Gly and !1ACT for residue 294 as Tyr !'##note in the authors' translation 177-Val is not shown, residues !1178-184 are displaced one codon to the left, and an !1additional Gly is shown after 184-Gly REFERENCE S19446 !$#authors Dujon, B.; Fairhead, C.; Thierry, A. !$#submission submitted to the Protein Sequence Database, March 1992 !$#accession S19746 !'##molecule_type DNA !'##residues 202-360 ##label DUJ !'##cross-references EMBL:X59720; GSPDB:GN00003; MIPS:YCL064c GENETICS !$#gene SGD:CHA1; MIPS:YCL064c !'##cross-references SGD:S0000569; MIPS:YCL064c !$#map_position 3L CLASSIFICATION #superfamily threonine dehydratase KEYWORDS ammonia-lyase; carbon-nitrogen lyase; carbon-oxygen lyase; !1hydro-lyase; phosphoprotein; pyridoxal phosphate; serine !1catabolism; threonine catabolism FEATURE !$37 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 360 #molecular-weight 39341 #checksum 8224 SEQUENCE /// ENTRY DWBYT #type complete TITLE threonine ammonia-lyase (EC 4.3.1.19) precursor - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YER086w; threonine deaminase ORGANISM #formal_name Saccharomyces cerevisiae DATE 17-May-1985 #sequence_revision 12-May-1995 #text_change 21-Jun-2002 ACCESSIONS S50589; A01150 REFERENCE S50436 !$#authors Dietrich, F.S. !$#submission submitted to the EMBL Data Library, December 1994 !$#description The sequence of S. cerevisiae cosmids 9747, 8198, 9781, and !1lambda clones 3612 and 6052. !$#accession S50589 !'##molecule_type DNA !'##residues 1-576 ##label DIE !'##cross-references EMBL:U18839; NID:g603313; PIDN:AAB64641.1; !1PID:g603324; GSPDB:GN00005; MIPS:YER086w REFERENCE A01150 !$#authors Kielland-Brandt, M.C.; Holmberg, S.; Petersen, J.G.L.; !1Nilsson-Tillgren, T. !$#journal Carlsberg Res. Commun. (1984) 49:567-575 !$#title Nucleotide sequence of the gene for threonine deaminase !1(ILV1) of Saccharomyces cerevisiae. !$#accession A01150 !'##molecule_type DNA !'##residues 1-258,'T',260-576 ##label KIE !'##cross-references EMBL:X01466; NID:g3821; PIDN:CAA25696.1; PID:g3823 GENETICS !$#gene SGD:ILV1; MIPS:YER086w !'##cross-references SGD:S0000888; MIPS:YER086w !$#map_position 5R !$#genome nuclear FUNCTION !$#description catalyzes conversion of threonine to alpha-ketobutyrate and !1ammonia !$#pathway isoleucine biosynthesis !$#note first step CLASSIFICATION #superfamily threonine dehydratase KEYWORDS ammonia-lyase; carbon-nitrogen lyase; carbon-oxygen lyase; !1homotetramer; hydro-lyase; isoleucine biosynthesis; !1mitochondrion; phosphoprotein; pyridoxal phosphate; !1threonine catabolism FEATURE !$109 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 576 #molecular-weight 63831 #checksum 56 SEQUENCE /// ENTRY DWECTS #type complete TITLE threonine ammonia-lyase (EC 4.3.1.19), biosynthetic - Escherichia coli (strain K-12) ALTERNATE_NAMES L-serine dehydratase; serine deaminase; threonine deaminase ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 21-Jun-2002 ACCESSIONS B27310; C26287; E26570; S48895; S30670; I41304; G65180 REFERENCE A91578 !$#authors Cox, J.L.; Cox, B.J.; Fidanza, V.; Calhoun, D.H. !$#journal Gene (1987) 56:185-198 !$#title The complete nucleotide sequence of the ilvGMEDA cluster of !1Escherichia coli K-12. !$#cross-references MUID:88056322; PMID:3315862 !$#accession B27310 !'##molecule_type DNA !'##residues 1-514 ##label COX !'##cross-references GB:M32253 !'##experimental_source strain K12 REFERENCE A92575 !$#authors Wek, R.C.; Hatfield, G.W. !$#journal J. Biol. Chem. (1986) 261:2441-2450 !$#title Nucleotide sequence and in vivo expression of the ilvY and !1ilvC genes in Escherichia coli K12: transcription from !1divergent overlapping promoters. !$#cross-references MUID:86111952; PMID:3003115 !$#accession C26287 !'##molecule_type DNA !'##residues 439-514 ##label WEK !'##cross-references GB:K03503 !'##experimental_source strain K12 REFERENCE A26570 !$#authors Lawther, R.P.; Wek, R.C.; Lopes, J.M.; Pereira, R.; Taillon, !1B.E.; Hatfield, G.W. !$#journal Nucleic Acids Res. (1987) 15:2137-2155 !$#title The complete nucleotide sequence of the ilvGMEDA operon of !1Escherichia coli K-12. !$#cross-references MUID:87174741; PMID:3550695 !$#accession E26570 !'##molecule_type DNA !'##residues 1-242,'G',244-514 ##label LAW1 !'##cross-references GB:M32253; NID:g146465; PIDN:AAA24024.1; !1PID:g146470 REFERENCE S48893 !$#authors Lawther, R.P. !$#submission submitted to the EMBL Data Library, December 1987 !$#accession S48895 !'##molecule_type DNA !'##residues 1-514 ##label LAW2 !'##cross-references EMBL:X04890; NID:g288528; PIDN:CAA28577.1; !1PID:g288533 REFERENCE S30660 !$#authors Daniels, D.L.; Plunkett III, G.; Burland, V.; Blattner, F.R. !$#journal Science (1992) 257:771-778 !$#title Analysis of the Escherichia coli genome: DNA sequence of the !1region from 84.5 to 86.5 minutes. !$#cross-references MUID:92358234; PMID:1379743 !$#accession S30670 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-121,'X',123-139,'R',141-514 ##label DAN !'##cross-references EMBL:M87049; NID:g836656; PIDN:AAA67575.1; !1PID:g148179 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1992 REFERENCE I41304 !$#authors Lopes, J.M.; Lawther, R.P. !$#journal Gene (1989) 76:255-269 !$#title Physical identification of an internal promoter, ilvAp, in !1the distal portion of the ilvGMEDA operon. !$#cross-references MUID:89326124; PMID:2473940 !$#accession I41304 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-10 ##label RES !'##cross-references GB:M25497; NID:g341363; PIDN:AAA24015.1; !1PID:g538347 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65180 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-514 ##label BLAT !'##cross-references GB:AE000453; GB:U00096; NID:g2367276; !1PIDN:AAC77492.1; PID:g1790207; UWGP:b3772 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ilvA !$#map_position 85 min FUNCTION !$#description catalyzes the deamination of threonine to yield !1alpha-ketobutyrate and ammonia !$#pathway isoleucine-valine biosynthesis !$#note this is the first enzyme in the isoleucine biosynthetic !1pathway CLASSIFICATION #superfamily threonine dehydratase KEYWORDS ammonia-lyase; carbon-nitrogen lyase; carbon-oxygen lyase; !1hydro-lyase; isoleucine-valine biosynthesis; phosphoprotein; !1pyridoxal phosphate; threonine catabolism FEATURE !$62 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 514 #molecular-weight 56195 #checksum 5621 SEQUENCE /// ENTRY DWEBTT #type complete TITLE threonine ammonia-lyase (EC 4.3.1.19), biosynthetic - Salmonella typhimurium ALTERNATE_NAMES L-serine dehydratase; serine deaminase; threonine deaminase ORGANISM #formal_name Salmonella typhimurium DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 21-Jun-2002 ACCESSIONS JT0278 REFERENCE JT0278 !$#authors Taillon, B.E.; Little, R.; Lawther, R.P. !$#journal Gene (1988) 63:245-252 !$#title Analysis of the functional domains of biosynthetic threonine !1deaminase by comparison of the amino acid sequences of three !1wild-type alleles to the amino acid sequence of !1biodegradative threonine deaminase. !$#cross-references MUID:88255870; PMID:3290055 !$#accession JT0278 !'##molecule_type DNA !'##residues 1-514 ##label TAI !'##cross-references GB:M26670; NID:g341512; PIDN:AAA27150.1; !1PID:g514966 !'##note the authors translated the codon CTG for residue 169 as Ile GENETICS !$#gene ilvA !$#map_position 83 min FUNCTION !$#description catalyzes the deamination of threonine to yield !1alpha-ketobutyrate and ammonia !$#pathway isoleucine-valine biosynthesis !$#note this is the first enzyme in the isoleucine biosynthetic !1pathway CLASSIFICATION #superfamily threonine dehydratase KEYWORDS ammonia-lyase; carbon-nitrogen lyase; carbon-oxygen lyase; !1hydro-lyase; isoleucine-valine biosynthesis; phosphoprotein; !1pyridoxal phosphate; threonine catabolism FEATURE !$62 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 514 #molecular-weight 56276 #checksum 7575 SEQUENCE /// ENTRY DWECTD #type complete TITLE threonine ammonia-lyase (EC 4.3.1.19), biodegradative [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES threonine deaminase ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 21-Jun-2002 ACCESSIONS A26367; A22317; B65101 REFERENCE A26367 !$#authors Datta, P.; Goss, T.J.; Omnaas, J.R.; Patil, R.V. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:393-397 !$#title Covalent structure of biodegradative threonine dehydratase !1of Escherichia coli: homology with other dehydratases. !$#cross-references MUID:87092415; PMID:3540965 !$#accession A26367 !'##molecule_type DNA !'##residues 1-329 ##label DAT !'##cross-references GB:M21312; NID:g147921; PIDN:AAA24660.1; !1PID:g147923; GB:X14430; NID:g43038; PID:g43043 REFERENCE A90645 !$#authors Kim, S.S.; Datta, P. !$#journal Biochim. Biophys. Acta (1982) 706:27-35 !$#title Chemical characterization of biodegradative threonine !1dehydratases from two enteric bacteria. !$#cross-references MUID:83023208; PMID:6751404 !$#accession A22317 !'##molecule_type protein !'##residues 1-25 ##label KIM REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65101 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-329 ##label BLAT !'##cross-references GB:AE000393; GB:U00096; NID:g1789499; !1PIDN:AAC76152.1; PID:g1789505; UWGP:b3117 !'##experimental_source strain K-12, substrain MG1655 COMMENT This enzyme catalyzes the pyridoxal phosphate-dependent !1dehydration of L-threonine to ammonia and alpha-ketobutyrate !1in the threonine catabolic pathway. Each tetrameric protein !1molecule can bind up to four molecules of AMP, which acts as !1an allosteric activator to the enzyme. The enzyme is !1inhibited by alpha-keto acids and other catabolites. GENETICS !$#gene tdcB; tdc !$#map_position 67 min COMPLEX homotetramer FUNCTION !$#description EC 4.2.1.16 [validated, MUID:87092415] CLASSIFICATION #superfamily threonine dehydratase KEYWORDS ammonia-lyase; carbon-nitrogen lyase; carbon-oxygen lyase; !1homotetramer; hydro-lyase; phosphoprotein; pyridoxal !1phosphate; threonine catabolism FEATURE !$58 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status experimental SUMMARY #length 329 #molecular-weight 35232 #checksum 1565 SEQUENCE /// ENTRY DWFKTG #type complete TITLE threonine synthase (EC 4.2.3.1) - Corynebacterium glutamicum ORGANISM #formal_name Corynebacterium glutamicum DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Jun-2002 ACCESSIONS S01701; S41448 REFERENCE S01701 !$#authors Malumbres, M.; Mateos, L.M.; Guerrero, C.; Martin, J.F. !$#journal Nucleic Acids Res. (1988) 16:9859 !$#title Nucleotide sequence of the threonine synthase (thrC) gene of !1Brevibacterium lactofermentum. !$#cross-references MUID:89041574; PMID:3186450 !$#accession S01701 !'##molecule_type DNA !'##residues 1-352 ##label MAL !'##cross-references GB:Z29562; EMBL:X12797; NID:g452397; !1PIDN:CAA82669.1; PID:g452398 !'##experimental_source ATCC 13869 !'##note the source is designated as Brevibacterium lactofermentum GENETICS !$#gene thrC FUNCTION !$#description catalyzes the hydrolyzation of O-phospho-L-homoserine to !1L-threonine and orthophosphate !$#pathway threonine biosynthesis !$#note pyridoxal phosphate cofactor CLASSIFICATION #superfamily threonine dehydratase KEYWORDS carbon-oxygen lyase; phosphoprotein; pyridoxal phosphate; !1threonine biosynthesis FEATURE !$59 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 352 #molecular-weight 37457 #checksum 6944 SEQUENCE /// ENTRY SYECAC #type complete TITLE cysteine synthase (EC 4.2.99.8) A - Escherichia coli (strain K-12) ALTERNATE_NAMES O-acetylserine (thiol)-lyase A; O-acetylserine sulfhydrolase A; protein SSI5 CONTAINS S-carboxymethylcysteine synthase (EC 4.5.1.5) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 21-Nov-1997 #text_change 01-Mar-2002 ACCESSIONS E65015; F28181; S03094; JU0109; S78621 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65015 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-323 ##label BLAT !'##cross-references GB:AE000329; GB:U00096; NID:g2367137; !1PIDN:AAC75467.1; PID:g1788754; UWGP:b2414 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A28181 !$#authors Byrne, C.R.; Monroe, R.S.; Ward, K.A.; Kredich, N.M. !$#journal J. Bacteriol. (1988) 170:3150-3157 !$#title DNA sequences of the cysK regions of Salmonella typhimurium !1and Escherichia coli and linkage of the cysK regions to !1ptsH. !$#cross-references MUID:88257033; PMID:3290198 !$#accession F28181 !'##molecule_type DNA !'##residues 1-181,'W',183-185,'TP',188-323 ##label BYR !'##cross-references GB:M21451; NID:g145684; PIDN:AAA23654.1; !1PID:g145686 REFERENCE S03093 !$#authors Levy, S.; Danchin, A. !$#journal Mol. Microbiol. (1988) 2:777-783 !$#title Phylogeny of metabolic pathways: O-acetylserine !1sulphydrylase A is homologous to the tryptophan synthase !1beta subunit. !$#cross-references MUID:89096499; PMID:3062311 !$#accession S03094 !'##molecule_type DNA !'##residues 1-323 ##label LEV !'##cross-references EMBL:X12615; NID:g41199; PIDN:CAA31137.1; !1PID:g41201 REFERENCE JU0109 !$#authors Kumagai, H.; Suzuki, H.; Shigematsu, H.; Tochikura, T. !$#journal Agric. Biol. Chem. (1989) 53:2481-2487 !$#title S-carboxymethylcysteine synthase from Escherichia coli. !$#accession JU0109 !'##molecule_type protein !'##residues 2-33,'X',35-37 ##label KUM !'##experimental_source strain W3110 !'##note the enzyme has a molecular weight of 84,000Da and gives a !1subunit weight of 37,000Da !'##note S-carboxymethylcysteine synthase (EC 4.5.1.5) activity was !1shown experimentally for purified enzyme REFERENCE S78617 !$#authors Quadroni, M.; Staudenmann, W.; Kertesz, M.; James, P. !$#journal Eur. J. Biochem. (1996) 239:773-781 !$#title Analysis of global responses by protein and peptide !1fingerprinting of proteins isolated by two-dimensional gel !1electrophoresis. Application to the sulfate-starvation !1response of Escherichia coli. !$#cross-references MUID:96370830; PMID:8774726 !$#accession S78621 !'##molecule_type protein !'##residues 2-11;14-16,'X',18-19;36-42;127-129,'X',131-137;236-238,'X', !1240,'X',242 ##label QUA GENETICS !$#gene cysK !$#map_position 52 min FUNCTION CSYN !$#description catalyzes formation of cysteine and acetate from !1O-acetylserine and hydrogen sulfide (EC 4.2.99.8) FUNCTION SCMC !$#description catalyzes synthesis of S-carboxymethyl-L-cysteine from !13-chloro-alanine and thioglycolic acid (EC 4.5.1.5) CLASSIFICATION #superfamily threonine dehydratase KEYWORDS carbon-halide lyase; carbon-oxygen lyase; cysteine !1biosynthesis; homodimer; phosphoprotein; pyridoxal phosphate FEATURE !$226 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 323 #molecular-weight 34489 #checksum 9792 SEQUENCE /// ENTRY SYEBAC #type complete TITLE cysteine synthase (EC 4.2.99.8) A - Salmonella typhimurium ALTERNATE_NAMES O-acetylserine (thiol)-lyase A; O-acetylserine sulfhydrolase A ORGANISM #formal_name Salmonella typhimurium DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 18-Jun-1999 ACCESSIONS B28181 REFERENCE A28181 !$#authors Byrne, C.R.; Monroe, R.S.; Ward, K.A.; Kredich, N.M. !$#journal J. Bacteriol. (1988) 170:3150-3157 !$#title DNA sequences of the cysK regions of Salmonella typhimurium !1and Escherichia coli and linkage of the cysK regions to !1ptsH. !$#cross-references MUID:88257033; PMID:3290198 !$#accession B28181 !'##molecule_type DNA !'##residues 1-323 ##label BYR !'##cross-references GB:M21450; NID:g153933; PIDN:AAA27051.1; !1PID:g153935 COMMENT This pyridoxal phosphate enzyme catalyzes the formation of !1cysteine and acetate from O-acetylserine and hydrogen !1sulfide. GENETICS !$#gene cysK !$#map_position 49 min CLASSIFICATION #superfamily threonine dehydratase KEYWORDS carbon-oxygen lyase; cysteine biosynthesis; homodimer; !1phosphoprotein; pyridoxal phosphate FEATURE !$226 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 323 #molecular-weight 34638 #checksum 555 SEQUENCE /// ENTRY SYECBC #type complete TITLE cysteine synthase (EC 4.2.99.8) B - Escherichia coli (strain K-12) ALTERNATE_NAMES O-acetylserine (thiol)-lyase B; O-acetylserine sulfhydrolase B ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 01-Mar-2002 ACCESSIONS D35402; D65016 REFERENCE A35402 !$#authors Sirko, A.; Hryniewicz, M.; Hulanicka, D.; Boeck, A. !$#journal J. Bacteriol. (1990) 172:3351-3357 !$#title Sulfate and thiosulfate transport in Escherichia coli K-12: !1nucleotide sequence and expression of the cysTWAM gene !1cluster. !$#cross-references MUID:90264334; PMID:2188958 !$#accession D35402 !'##molecule_type DNA !'##residues 1-303 ##label SIR !'##cross-references GB:M32101; NID:g145657; PIDN:AAA23640.1; !1PID:g145662; GB:M38050 !'##experimental_source strain K12 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65016 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-303 ##label BLAT !'##cross-references GB:AE000329; GB:U00096; NID:g2367137; !1PIDN:AAC75474.1; PID:g2367138; UWGP:b2421 !'##experimental_source strain K-12, substrain MG1655 COMMENT Two cysteine synthase enzymes are found. Both catalyze the !1formation of cysteine and acetate from O-acetylserine and !1hydrogen sulfide. The cysteine synthase B can also use !1thiosulfate in place of sulfide to give cysteine !1thiosulfonate as a product. GENETICS !$#gene cysM !$#map_position 52 min CLASSIFICATION #superfamily threonine dehydratase KEYWORDS carbon-oxygen lyase; cysteine biosynthesis; homodimer; !1phosphoprotein; pyridoxal phosphate FEATURE !$115 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 303 #molecular-weight 32664 #checksum 9401 SEQUENCE /// ENTRY JS0762 #type complete TITLE cysteine synthase (EC 4.2.99.8) precursor - wheat ALTERNATE_NAMES O-acetylserine (thiol)-lyase ORGANISM #formal_name Triticum aestivum #common_name common wheat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS JS0762 REFERENCE JS0761 !$#authors Youssefian, S.; Nakamura, M.; Sano, H. !$#submission submitted to JIPID, September 1992 !$#accession JS0762 !'##molecule_type mRNA !'##residues 1-325 ##label YOU !'##cross-references DDBJ:D13153; NID:g218334; PIDN:BAA02438.1; !1PID:g218335 CLASSIFICATION #superfamily threonine dehydratase KEYWORDS carbon-oxygen lyase; cysteine biosynthesis; phosphoprotein; !1plastid; pyridoxal phosphate FEATURE !$1-37 #domain transit peptide (plastid) #status predicted !8#label TNP\ !$38-325 #product cysteine synthase #status predicted #label !8MAT\ !$226 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 325 #molecular-weight 34114 #checksum 8259 SEQUENCE /// ENTRY S52738 #type complete TITLE cysteine synthase (EC 4.2.99.8) precursor - maize ORGANISM #formal_name Zea mays #common_name maize DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S52738 REFERENCE S52738 !$#authors Brander, K.A.; Owttrim, G.W.; Brunold, C. !$#submission submitted to the EMBL Data Library, March 1995 !$#description Isolation of a putative plastidic isoform of cysteine !1synthase from maize. !$#accession S52738 !'##status preliminary !'##molecule_type mRNA !'##residues 1-325 ##label BRA !'##cross-references EMBL:X85803; NID:g758352; PIDN:CAA59798.1; !1PID:g758353 CLASSIFICATION #superfamily threonine dehydratase KEYWORDS carbon-oxygen lyase; phosphoprotein; pyridoxal phosphate FEATURE !$49 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 325 #molecular-weight 34206 #checksum 9417 SEQUENCE /// ENTRY S46438 #type complete TITLE cysteine synthase (EC 4.2.99.8) - watermelon ORGANISM #formal_name Citrullus lanatus #common_name watermelon DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S46438 REFERENCE S46438 !$#authors Noji, M.; Murakoshi, I.; Saito, K. !$#journal Mol. Gen. Genet. (1994) 244:57-66 !$#title Molecular cloning of a cysteine synthase cDNA from Citrullus !1vulgaris (watermelon) by genetic complementation in an !1Escherichia coli Cys(-) auxotroph. !$#cross-references MUID:94316193; PMID:8041362 !$#accession S46438 !'##molecule_type mRNA !'##residues 1-325 ##label NOJ !'##cross-references EMBL:D28777; NID:g466530; PIDN:BAA05965.1; !1PID:g540497 !'##note the source is designated as Citrullus vulgaris !'##note additional initiators could be Val-32 (GTG) or Met-41 CLASSIFICATION #superfamily threonine dehydratase KEYWORDS carbon-oxygen lyase; cysteine biosynthesis; phosphoprotein; !1pyridoxal phosphate FEATURE !$49 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 325 #molecular-weight 34342 #checksum 7672 SEQUENCE /// ENTRY S55321 #type complete TITLE cysteine synthase (EC 4.2.99.8) - Synechococcus sp. (strain PCC 7942) plasmid pANL ORGANISM #formal_name Synechococcus sp. #variety PCC 7942 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S55321 REFERENCE S55321 !$#authors Nicholson, M.L.; Gaasenbeek, M.; Laudenbach, D.E. !$#journal Mol. Gen. Genet. (1995) 247:623-632 !$#title Two enzymes together capable of cysteine biosynthesis are !1encoded on a cyanobacterial plasmid. !$#cross-references MUID:95327059; PMID:7603442 !$#accession S55321 !'##molecule_type DNA !'##residues 1-329 ##label NIC GENETICS !$#gene srpG !$#genome plasmid pANL CLASSIFICATION #superfamily threonine dehydratase KEYWORDS carbon-oxygen lyase; cysteine biosynthesis; phosphoprotein; !1pyridoxal phosphate FEATURE !$231 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 329 #molecular-weight 34600 #checksum 1551 SEQUENCE /// ENTRY A43407 #type complete TITLE cysteine synthase (EC 4.2.99.8) precursor - pepper ALTERNATE_NAMES O-acetylserine (thiol) lyase; O-acetylserine sulfhydrolase ORGANISM #formal_name Capsicum annuum #common_name pepper DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A43407; S24637 REFERENCE A43407 !$#authors Romer, S.; d'Harlingue, A.; Camara, B.; Schantz, R.; Kuntz, !1M. !$#journal J. Biol. Chem. (1992) 267:17966-17970 !$#title Cysteine synthase from Capsicum annuum chromoplasts. !1Characterization and cDNA cloning of an up-regulated enzyme !1during fruit development. !$#cross-references MUID:92388158; PMID:1381358 !$#accession A43407 !'##molecule_type mRNA !'##residues 1-374 ##label ROM !'##cross-references GB:X64874; NID:g17943; PIDN:CAA46086.1; PID:g17944 !'##note sequence extracted from NCBI backbone (NCBIP:112876) GENETICS !$#genome nuclear CLASSIFICATION #superfamily threonine dehydratase KEYWORDS carbon-oxygen lyase; chloroplast; cysteine biosynthesis; !1phosphoprotein; pyridoxal phosphate FEATURE !$108 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 374 #molecular-weight 39978 #checksum 3613 SEQUENCE /// ENTRY S06477 #type complete TITLE enoyl-CoA hydratase (EC 4.2.1.17) precursor, mitochondrial - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 28-May-1999 #sequence_revision 28-May-1999 #text_change 07-Dec-1999 ACCESSIONS S06477 REFERENCE S06477 !$#authors Minami-Ishii, N.; Taketani, S.; Osumi, T.; Hashimoto, T. !$#journal Eur. J. Biochem. (1989) 185:73-78 !$#title Molecular cloning and sequence analysis of the cDNA for rat !1mitochondrial enoyl-CoA hydratase. Structural and !1evolutionary relationships linked to the bifunctional enzyme !1of the peroxisomal beta-oxidation system. !$#cross-references MUID:90032688; PMID:2806264 !$#accession S06477 !'##molecule_type mRNA !'##residues 1-290 ##label MIN !'##cross-references EMBL:X15958; NID:g56071; PIDN:CAA34080.1; !1PID:g56072 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by amino acid sequencing CLASSIFICATION #superfamily naphthoate synthase; enoyl-CoA hydratase !1homology KEYWORDS carbon-oxygen lyase; fatty acid beta-oxidation; hydro-lyase; !1mitochondrion FEATURE !$1-29 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$30-290 #product enoyl-CoA hydratase, mitochondrial #status !8experimental #label MAT\ !$59-209 #domain enoyl-CoA hydratase homology #label ECH SUMMARY #length 290 #molecular-weight 31516 #checksum 9254 SEQUENCE /// ENTRY S41006 #type complete TITLE enoyl-CoA hydratase (EC 4.2.1.17), mitochondrial - Caenorhabditis elegans ALTERNATE_NAMES hypothetical protein T05G5.6 ORGANISM #formal_name Caenorhabditis elegans DATE 28-May-1999 #sequence_revision 28-May-1999 #text_change 28-May-1999 ACCESSIONS S41006 REFERENCE S41001 !$#authors Thomas, K. !$#submission submitted to the EMBL Data Library, October 1993 !$#accession S41006 !'##molecule_type DNA !'##residues 1-288 ##label THO !'##cross-references EMBL:Z27079; NID:g414641; PID:g414647 GENETICS !$#introns 101/3; 172/1; 271/3 CLASSIFICATION #superfamily naphthoate synthase; enoyl-CoA hydratase !1homology KEYWORDS carbon-oxygen lyase; hydro-lyase; mitochondrion FEATURE !$57-207 #domain enoyl-CoA hydratase homology #label ECH SUMMARY #length 288 #molecular-weight 31172 #checksum 6694 SEQUENCE /// ENTRY D70893 #type complete TITLE enoyl-CoA hydratase (EC 4.2.1.17) echA8 - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 28-May-1999 #sequence_revision 28-May-1999 #text_change 16-Jun-2000 ACCESSIONS D70893 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession D70893 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-257 ##label COL !'##cross-references GB:AL021897; GB:AL123456; NID:g3256022; !1PIDN:CAA17186.1; PID:g2896707 !'##experimental_source strain H37Rv GENETICS !$#gene echA8 CLASSIFICATION #superfamily naphthoate synthase; enoyl-CoA hydratase !1homology KEYWORDS carbon-oxygen lyase; hydro-lyase FEATURE !$26-176 #domain enoyl-CoA hydratase homology #label ECH SUMMARY #length 257 #molecular-weight 27273 #checksum 4699 SEQUENCE /// ENTRY D64890 #type complete TITLE probable enoyl-CoA hydratase (EC 4.2.1.17) ydbS - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 28-May-1999 #sequence_revision 28-May-1999 #text_change 01-Mar-2002 ACCESSIONS D64890 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64890 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-255 ##label BLAT !'##cross-references GB:AE000236; GB:U00096; NID:g1787652; !1PIDN:AAC74475.1; PID:g1787659; UWGP:b1393 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ydbS FUNCTION !$#description may catalyze the reversible conversion of !1(3S)-3-hydroxyacyl-CoA to trans-2(or 3)-enoyl-CoA CLASSIFICATION #superfamily naphthoate synthase; enoyl-CoA hydratase !1homology KEYWORDS carbon-oxygen lyase; fatty acid beta-oxidation; hydro-lyase FEATURE !$24-174 #domain enoyl-CoA hydratase homology #label ECH SUMMARY #length 255 #molecular-weight 27237 #checksum 5717 SEQUENCE /// ENTRY C69370 #type complete TITLE probable enoyl-CoA hydratase (EC 4.2.1.17) fad-3 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 28-May-1999 #sequence_revision 28-May-1999 #text_change 18-Jun-1999 ACCESSIONS C69370 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession C69370 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-259 ##label KLE !'##cross-references GB:AE001038; GB:AE000782; NID:g2689361; !1PIDN:AAB90280.1; PID:g2649635; TIGR:AF0963 CLASSIFICATION #superfamily naphthoate synthase; enoyl-CoA hydratase !1homology KEYWORDS carbon-oxygen lyase; fatty acid beta-oxidation; hydro-lyase FEATURE !$24-176 #domain enoyl-CoA hydratase homology #label ECH SUMMARY #length 259 #molecular-weight 28700 #checksum 3516 SEQUENCE /// ENTRY C69304 #type complete TITLE probable enoyl-CoA hydratase (EC 4.2.1.17) fad-1 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 28-May-1999 #sequence_revision 28-May-1999 #text_change 18-Jun-1999 ACCESSIONS C69304 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession C69304 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-256 ##label KLE !'##cross-references GB:AE001074; GB:AE000782; NID:g2689397; !1PIDN:AAB90798.1; PID:g2650190; TIGR:AF0435 CLASSIFICATION #superfamily naphthoate synthase; enoyl-CoA hydratase !1homology KEYWORDS carbon-oxygen lyase; fatty acid beta-oxidation; hydro-lyase FEATURE !$25-175 #domain enoyl-CoA hydratase homology #label ECH SUMMARY #length 256 #molecular-weight 27764 #checksum 4108 SEQUENCE /// ENTRY C69893 #type complete TITLE probable enoyl-CoA hydratase (EC 4.2.1.17) yngF - Bacillus subtilis ALTERNATE_NAMES 3-hydroxbutyryl-CoA dehydratase homolog ORGANISM #formal_name Bacillus subtilis DATE 28-May-1999 #sequence_revision 28-May-1999 #text_change 16-Jun-2000 ACCESSIONS C69893 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69893 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-260 ##label KUN !'##cross-references GB:Z99113; GB:AL009126; NID:g2634090; !1PIDN:CAB13705.1; PID:g2634205 !'##experimental_source strain 168 GENETICS !$#gene yngF CLASSIFICATION #superfamily naphthoate synthase; enoyl-CoA hydratase !1homology KEYWORDS carbon-oxygen lyase; hydro-lyase FEATURE !$26-179 #domain enoyl-CoA hydratase homology #label ECH SUMMARY #length 260 #molecular-weight 27872 #checksum 4539 SEQUENCE /// ENTRY G69985 #type complete TITLE probable enoyl-CoA hydratase (EC 4.2.1.17) ysiB - Bacillus subtilis ALTERNATE_NAMES 3-hydroxbutyryl-CoA dehydratase homolog ORGANISM #formal_name Bacillus subtilis DATE 28-May-1999 #sequence_revision 28-May-1999 #text_change 16-Jun-2000 ACCESSIONS G69985 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69985 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-258 ##label KUN !'##cross-references GB:Z99118; GB:AL009126; NID:g2635200; !1PIDN:CAB14814.1; PID:g2635319 !'##experimental_source strain 168 GENETICS !$#gene ysiB CLASSIFICATION #superfamily naphthoate synthase; enoyl-CoA hydratase !1homology KEYWORDS carbon-oxygen lyase; hydro-lyase FEATURE !$23-176 #domain enoyl-CoA hydratase homology #label ECH SUMMARY #length 258 #molecular-weight 27553 #checksum 7131 SEQUENCE /// ENTRY C71435 #type complete TITLE probable enoyl-CoA hydratase (EC 4.2.1.17) - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress #variety columbia DATE 28-May-1999 #sequence_revision 28-May-1999 #text_change 16-Jun-2000 ACCESSIONS C71435 REFERENCE A71400 !$#authors Bevan, M.; Bancroft, I.; Bent, E.; Love, K.; Goodman, H.; !1Dean, C.; Bergkamp, R.; Dirkse, W.; Van Staveren, M.; !1Stiekema, W.; Drost, L.; Ridley, P.; Hudson, S.A.; Patel, !1K.; Murphy, G.; Piffanelli, P.; Wedler, H.; Wedler, E.; !1Wambutt, R.; Weitzenegger, T.; Pohl, T.M.; Terryn, N.; !1Gielen, J.; Villarroel, R.; De Clerck, R.; Van Montagu, M.; !1Lecharny, A.; Auborg, S.; Gy, I.; Kreis, M.; Lao, N.; !1Kavanagh, T.; Hempel, S.; Kotter, P.; Entian, K.D.; Rieger, !1M.; Schaeffer, M.; Funk, B.; Mueller-Auer, S.; Silvey, M.; !1James, R.; Montfort, A.; Pons, A.; Puigdomenech, P.; Douka, !1A.; Voukelatou, E.; Milioni, D.; Hatzopoulos, P.; Piravandi, !1E.; Obermaier, B.; Hilbert, H.; Duesterhoft, A.; Moores, T.; !1Jones, J.D.G.; Eneva, T.; Palme, K.; Benes, V.; Rechman, S.; !1Ansorge, W.; Cooke, R.; Berger, C.; Delseny, M.; Voet, M.; !1Volckaert, G.; Mewes, H.W.; Klosterman, S.; Schueller, C.; !1Chalwatzis, N. !$#journal Nature (1998) 391:485-488 !$#title Analysis of 1.9 Mb of contiguous sequence from chromosome 4 !1of Arabidopsis thaliana. !$#cross-references MUID:98121113; PMID:9461215 !$#accession C71435 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-229 ##label BEV !'##cross-references GB:Z97342; NID:g2245031; PIDN:CAB10453.1; !1PID:g2245034 GENETICS !$#map_position 4COP9-4G3845 CLASSIFICATION #superfamily naphthoate synthase; enoyl-CoA hydratase !1homology KEYWORDS carbon-oxygen lyase; hydro-lyase FEATURE !$1-148 #domain enoyl-CoA hydratase homology #status atypical !8#label ECH SUMMARY #length 229 #molecular-weight 24629 #checksum 4957 SEQUENCE /// ENTRY D64997 #type complete TITLE naphthoate synthase (EC 4.1.3.36) [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES DHNA synthase; menaquinone biosynthesis enzyme menB; mitochondrial enoyl-CoA hydratase homolog ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS A42714; D64997 REFERENCE A42714 !$#authors Sharma, V.; Suvarna, K.; Meganathan, R.; Hudspeth, M.E. !$#journal J. Bacteriol. (1992) 174:5057-5062 !$#title Menaquinone (vitamin K2) biosynthesis: nucleotide sequence !1and expression of the menB gene from Escherichia coli. !$#cross-references MUID:92332442; PMID:1629162 !$#accession A42714 !'##status preliminary !'##molecule_type DNA !'##residues 1-285 ##label SHA !'##cross-references GB:M93421; NID:g145739; PIDN:AAA23682.1; !1PID:g145740 !'##note sequence extracted from NCBI backbone (NCBIN:108981, !1NCBIP:108983) REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64997 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-285 ##label BLAT !'##cross-references GB:AE000316; GB:U00096; NID:g1788594; !1PIDN:AAC75322.1; PID:g1788597; UWGP:b2262 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene menB FUNCTION !$#description EC 4.1.3.36 [validated, MUID:92332442]; naphthoate synthase; !1forms the bicyclic ring system of menaquinone by catalyzing !1the conversion of o-succinylbenzoyl-coenzyme A to 1, !14-dihydroxy-2-naphthoic acid !$#pathway menaquinone biosynthesis CLASSIFICATION #superfamily naphthoate synthase; enoyl-CoA hydratase !1homology KEYWORDS carbon-carbon lyase; coenzyme A; oxo-acid-lyase FEATURE !$46-201 #domain enoyl-CoA hydratase homology #label ECH SUMMARY #length 285 #molecular-weight 31633 #checksum 6513 SEQUENCE /// ENTRY B64105 #type complete TITLE naphthoate synthase (EC 4.1.3.36) menB - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-May-2000 ACCESSIONS B64105 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession B64105 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-285 ##label TIGR !'##cross-references GB:U32777; GB:L42023; NID:g1573983; !1PIDN:AAC22625.1; PID:g1573991; TIGR:HI0968 GENETICS !$#gene menB CLASSIFICATION #superfamily naphthoate synthase; enoyl-CoA hydratase !1homology KEYWORDS carbon-carbon lyase; coenzyme A; oxo-acid-lyase FEATURE !$46-201 #domain enoyl-CoA hydratase homology #label ECH SUMMARY #length 285 #molecular-weight 31700 #checksum 6172 SEQUENCE /// ENTRY F69656 #type complete TITLE naphthoate synthase (EC 4.1.3.36) menB - Bacillus subtilis ALTERNATE_NAMES dihydroxynaphthoate synthase; dihydroxynapthoic acid (DHNA) synthetase menB; menaquinone biosynthesis enzyme/enoyl CoA hydratase homolog ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS F69656; A42715; T46643; S27512 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69656 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-271 ##label KUN !'##cross-references GB:Z99119; GB:AL009126; NID:g2635411; !1PIDN:CAB15058.1; PID:g2635564 !'##experimental_source strain 168 REFERENCE A42715 !$#authors Driscoll, J.R.; Taber, H.W. !$#journal J. Bacteriol. (1992) 174:5063-5071 !$#title Sequence organization and regulation of the Bacillus !1subtilis menBE operon. !$#cross-references MUID:92332443; PMID:1629163 !$#accession A42715 !'##molecule_type DNA !'##residues 'MK',13,'FD',16-106,'R',108-271 ##label DRI1 !'##cross-references EMBL:M74521; NID:g557486 !'##note sequence inconsistent with the nucleotide translation; sequence !1extracted from NCBI backbone (NCBIN:108985, NCBIP:108987) !$#accession T46643 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 'MK',13,'FD',16-271 ##label DRI2 !'##cross-references EMBL:M74521; NID:g557486; PIDN:AAA50401.1; !1PID:g557492 REFERENCE S27512 !$#authors Driscoll, J.R.; Taber, H. !$#submission submitted to the EMBL Data Library, October 1991 !$#accession S27512 !'##molecule_type DNA !'##residues 'MK',13,'FD',16-271 ##label DRI3 !'##cross-references EMBL:M74538; NID:g1185287; PIDN:AAC37016.1; !1PID:g143186 !'##experimental_source strain RB1 GENETICS !$#gene menB CLASSIFICATION #superfamily naphthoate synthase; enoyl-CoA hydratase !1homology KEYWORDS carbon-carbon lyase; coenzyme A; oxo-acid-lyase FEATURE !$33-187 #domain enoyl-CoA hydratase homology #label ECH SUMMARY #length 271 #molecular-weight 29899 #checksum 9898 SEQUENCE /// ENTRY S77432 #type complete TITLE naphthoate synthase (EC 4.1.3.36) - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S77432 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S77432 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-275 ##label KAN !'##cross-references EMBL:D90906; GB:AB001339; NID:g1652492; !1PIDN:BAA17535.1; PID:g1652614 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily naphthoate synthase; enoyl-CoA hydratase !1homology KEYWORDS carbon-carbon lyase; coenzyme A; oxo-acid-lyase FEATURE !$32-191 #domain enoyl-CoA hydratase homology #label ECH SUMMARY #length 275 #molecular-weight 30307 #checksum 6017 SEQUENCE /// ENTRY F69398 #type complete TITLE dihydroxynaphthoic acid synthase (menB) homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS F69398 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession F69398 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-277 ##label KLE !'##cross-references GB:AE001022; GB:AE000782; NID:g2689345; !1PIDN:AAB90054.1; PID:g2649394; TIGR:AF1191 CLASSIFICATION #superfamily naphthoate synthase; enoyl-CoA hydratase !1homology FEATURE !$29-192 #domain enoyl-CoA hydratase homology #label ECH SUMMARY #length 277 #molecular-weight 30604 #checksum 4436 SEQUENCE /// ENTRY G70547 #type complete TITLE probable menB protein - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS G70547 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession G70547 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-314 ##label COL !'##cross-references GB:Z95558; GB:AL123456; NID:g3261781; !1PIDN:CAB08959.1; PID:g2114010 !'##experimental_source strain H37Rv GENETICS !$#gene menB CLASSIFICATION #superfamily naphthoate synthase; enoyl-CoA hydratase !1homology FEATURE !$59-230 #domain enoyl-CoA hydratase homology #label ECH SUMMARY #length 314 #molecular-weight 34689 #checksum 8828 SEQUENCE /// ENTRY B70693 #type complete TITLE probable echA16 protein - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS B70693 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession B70693 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-249 ##label COL !'##cross-references GB:Z81331; GB:AL123456; NID:g3261650; !1PIDN:CAB03655.1; PID:g1648889 !'##experimental_source strain H37Rv GENETICS !$#gene echA16 CLASSIFICATION #superfamily naphthoate synthase; enoyl-CoA hydratase !1homology FEATURE !$26-169 #domain enoyl-CoA hydratase homology #label ECH SUMMARY #length 249 #molecular-weight 26630 #checksum 2186 SEQUENCE /// ENTRY F70807 #type complete TITLE probable enoyl coA hydratase - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS F70807 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession F70807 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-263 ##label COL !'##cross-references GB:AL022022; GB:AL123456; NID:g3261554; !1PIDN:CAA17753.1; PID:g2924453 !'##experimental_source strain H37Rv GENETICS !$#gene echA19 CLASSIFICATION #superfamily naphthoate synthase; enoyl-CoA hydratase !1homology FEATURE !$27-182 #domain enoyl-CoA hydratase homology #label ECH SUMMARY #length 263 #molecular-weight 28248 #checksum 4040 SEQUENCE /// ENTRY D70961 #type complete TITLE probable echA1 protein - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS D70961 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession D70961 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-262 ##label COL !'##cross-references GB:Z92669; GB:AL123456; NID:g3242271; !1PIDN:CAB06989.1; PID:g1871595 !'##experimental_source strain H37Rv GENETICS !$#gene echA1 CLASSIFICATION #superfamily naphthoate synthase; enoyl-CoA hydratase !1homology FEATURE !$34-181 #domain enoyl-CoA hydratase homology #label ECH SUMMARY #length 262 #molecular-weight 27280 #checksum 9152 SEQUENCE /// ENTRY S72706 #type complete TITLE probable enoyl-CoA hydratase (EC 4.2.1.17) fcbB - Mycobacterium leprae ALTERNATE_NAMES Lepb1170_C2_224 protein ORGANISM #formal_name Mycobacterium leprae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 18-Feb-2000 ACCESSIONS S72706; T45233 REFERENCE S72693 !$#authors Smith, D.R.; Robison, K. !$#submission submitted to the EMBL Data Library, November 1993 !$#description Mycobacterium leprae cosmid B1170. !$#accession S72706 !'##status preliminary !'##molecule_type DNA !'##residues 1-294 ##label SMI !'##cross-references EMBL:U00010; NID:g466780; PIDN:AAA17070.1; !1PID:g466794 REFERENCE Z22949 !$#authors James, K.D.; Parkhill, J.; Barrell, B.G.; Rajandream, M.A. !$#submission submitted to the EMBL Data Library, March 1999 !$#accession T45233 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-294 ##label JAM !'##cross-references EMBL:AL049913; PIDN:CAB43147.1 !'##experimental_source cosmid B1610 GENETICS !$#gene fcbB; MLCB1610.01 !$#start_codon GTG CLASSIFICATION #superfamily naphthoate synthase; enoyl-CoA hydratase !1homology KEYWORDS carbon-oxygen lyase; hydro-lyase FEATURE !$43-203 #domain enoyl-CoA hydratase homology #label ECH SUMMARY #length 294 #molecular-weight 31491 #checksum 837 SEQUENCE /// ENTRY C70873 #type complete TITLE probable enoyl-CoA hydratase - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS C70873 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession C70873 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-285 ##label COL !'##cross-references GB:AL021184; GB:AL123456; NID:g3261498; !1PIDN:CAA16000.1; PID:g2791406 !'##experimental_source strain H37Rv GENETICS !$#gene echA12 CLASSIFICATION #superfamily naphthoate synthase; enoyl-CoA hydratase !1homology FEATURE !$41-201 #domain enoyl-CoA hydratase homology #label ECH SUMMARY #length 285 #molecular-weight 30575 #checksum 3533 SEQUENCE /// ENTRY F70783 #type complete TITLE probable enoyl-coa hydratase - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS F70783 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession F70783 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-243 ##label COL !'##cross-references GB:Z73101; GB:AL123456; NID:g3261565; !1PIDN:CAA97380.1; PID:g1314045 !'##experimental_source strain H37Rv GENETICS !$#gene echA6 CLASSIFICATION #superfamily naphthoate synthase; enoyl-CoA hydratase !1homology FEATURE !$22-168 #domain enoyl-CoA hydratase homology #label ECH SUMMARY #length 243 #molecular-weight 26029 #checksum 1115 SEQUENCE /// ENTRY S19026 #type complete TITLE enoyl-CoA hydratase homolog - Rhodobacter capsulatus ORGANISM #formal_name Rhodobacter capsulatus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S19026 REFERENCE S19026 !$#authors Beckman, D.L.; Kranz, R.G. !$#journal Gene (1991) 107:171-172 !$#title A bacterial homolog to the mitochondrial enoyl-CoA !1hydratase. !$#cross-references MUID:92077430; PMID:1743516 !$#accession S19026 !'##status preliminary !'##molecule_type DNA !'##residues 1-257 ##label BEC !'##cross-references EMBL:X60194; NID:g45983; PIDN:CAA42750.1; !1PID:g45984 CLASSIFICATION #superfamily naphthoate synthase; enoyl-CoA hydratase !1homology FEATURE !$26-176 #domain enoyl-CoA hydratase homology #label ECH SUMMARY #length 257 #molecular-weight 27362 #checksum 388 SEQUENCE /// ENTRY E64890 #type complete TITLE probable membrane protein b1394 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS E64890 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64890 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-262 ##label BLAT !'##cross-references GB:AE000236; GB:U00096; NID:g1787652; !1PIDN:AAC74476.1; PID:g1787660; UWGP:b1394 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily naphthoate synthase; enoyl-CoA hydratase !1homology KEYWORDS transmembrane protein FEATURE !$25-181 #domain enoyl-CoA hydratase homology #label ECH\ !$102-118 #domain transmembrane #status predicted #label TM01 SUMMARY #length 262 #molecular-weight 28404 #checksum 3266 SEQUENCE /// ENTRY D64724 #type complete TITLE carnitine racemase (EC 5.-.-.-) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS D64724; S40557; I41014 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64724 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-297 ##label BLAT !'##cross-references GB:AE000114; GB:U00096; NID:g1786217; !1PIDN:AAC73147.1; PID:g1786220; UWGP:b0036 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40557 !'##status preliminary !'##molecule_type DNA !'##residues 1-144,'A',146-297 ##label YUR !'##cross-references EMBL:D10483; NID:g216434; PIDN:BAA01312.1; !1PID:g216461 REFERENCE I41010 !$#authors Eichler, K.; Bourgis, F.; Buchet, A.; Kleber, H.P.; !1Mandrand-Berthelot, M.A. !$#journal Mol. Microbiol. (1994) 13:775-786 !$#title Molecular characterization of the cai operon necessary for !1carnitine metabolism in Escherichia coli. !$#cross-references MUID:95115548; PMID:7815937 !$#accession I41014 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-2,'R',4-13,'A',15-282,'L',284-297 ##label RES !'##cross-references EMBL:X73904; NID:g563860; PIDN:CAA52114.1; !1PID:g563865 !'##experimental_source strain 044 K74 GENETICS !$#gene caiD FUNCTION !$#pathway carnitine metabolism CLASSIFICATION #superfamily naphthoate synthase; enoyl-CoA hydratase !1homology KEYWORDS isomerase FEATURE !$60-212 #domain enoyl-CoA hydratase homology #label ECH SUMMARY #length 297 #molecular-weight 32311 #checksum 3276 SEQUENCE /// ENTRY H69454 #type complete TITLE enoyl-CoA hydratase (fad-4) homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS H69454 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession H69454 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-254 ##label KLE !'##cross-references GB:AE000989; GB:AE000782; NID:g2689312; !1PIDN:AAB89601.1; PID:g2648909; TIGR:AF1641 CLASSIFICATION #superfamily naphthoate synthase; enoyl-CoA hydratase !1homology FEATURE !$24-175 #domain enoyl-CoA hydratase homology #label ECH SUMMARY #length 254 #molecular-weight 28641 #checksum 3377 SEQUENCE /// ENTRY E69335 #type complete TITLE enoyl-CoA hydratase (fad-2) homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS E69335 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession E69335 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-308 ##label KLE !'##cross-references GB:AE001057; GB:AE000782; NID:g2689380; !1PIDN:AAB90553.1; PID:g2649929; TIGR:AF0685 CLASSIFICATION #superfamily naphthoate synthase; enoyl-CoA hydratase !1homology FEATURE !$50-208 #domain enoyl-CoA hydratase homology #label ECH SUMMARY #length 308 #molecular-weight 35399 #checksum 3987 SEQUENCE /// ENTRY F71428 #type complete TITLE hypothetical protein - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress #variety columbia DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS F71428 REFERENCE A71400 !$#authors Bevan, M.; Bancroft, I.; Bent, E.; Love, K.; Goodman, H.; !1Dean, C.; Bergkamp, R.; Dirkse, W.; Van Staveren, M.; !1Stiekema, W.; Drost, L.; Ridley, P.; Hudson, S.A.; Patel, !1K.; Murphy, G.; Piffanelli, P.; Wedler, H.; Wedler, E.; !1Wambutt, R.; Weitzenegger, T.; Pohl, T.M.; Terryn, N.; !1Gielen, J.; Villarroel, R.; De Clerck, R.; Van Montagu, M.; !1Lecharny, A.; Auborg, S.; Gy, I.; Kreis, M.; Lao, N.; !1Kavanagh, T.; Hempel, S.; Kotter, P.; Entian, K.D.; Rieger, !1M.; Schaeffer, M.; Funk, B.; Mueller-Auer, S.; Silvey, M.; !1James, R.; Montfort, A.; Pons, A.; Puigdomenech, P.; Douka, !1A.; Voukelatou, E.; Milioni, D.; Hatzopoulos, P.; Piravandi, !1E.; Obermaier, B.; Hilbert, H.; Duesterhoft, A.; Moores, T.; !1Jones, J.D.G.; Eneva, T.; Palme, K.; Benes, V.; Rechman, S.; !1Ansorge, W.; Cooke, R.; Berger, C.; Delseny, M.; Voet, M.; !1Volckaert, G.; Mewes, H.W.; Klosterman, S.; Schueller, C.; !1Chalwatzis, N. !$#journal Nature (1998) 391:485-488 !$#title Analysis of 1.9 Mb of contiguous sequence from chromosome 4 !1of Arabidopsis thaliana. !$#cross-references MUID:98121113; PMID:9461215 !$#accession F71428 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-244 ##label BEV !'##cross-references GB:Z97340; NID:g2244950; PIDN:CAB10400.1; !1PID:g2244979 GENETICS !$#map_position 4COP9-4G3845 CLASSIFICATION #superfamily naphthoate synthase; enoyl-CoA hydratase !1homology FEATURE !$31-180 #domain enoyl-CoA hydratase homology #label ECH SUMMARY #length 244 #molecular-weight 26351 #checksum 9250 SEQUENCE /// ENTRY I37195 #type complete TITLE AU-specific RNA-binding protein / enoyl-CoA hydratase homolog - human ALTERNATE_NAMES brain AUH protein CONTAINS enoyl-CoA hydratase (EC 4.2.1.17) [validated] ORGANISM #formal_name Homo sapiens #common_name man DATE 28-May-1999 #sequence_revision 28-May-1999 #text_change 31-Mar-2000 ACCESSIONS I37195 REFERENCE I37195 !$#authors Nakagawa, J.; Waldner, H.; Meyer-Monard, S.; Hofsteenge, J.; !1Jeno, P.; Moroni, C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1995) 92:2051-2055 !$#title AUH, a gene encoding an AU-specific RNA binding protein with !1intrinsic enoyl-CoA hydratase activity. !$#cross-references MUID:95199290; PMID:7892223 !$#accession I37195 !'##molecule_type mRNA !'##residues 1-339 ##label RES !'##cross-references EMBL:X79888; NID:g780240; PIDN:CAA56260.1; !1PID:g780241 !'##note parts of this sequence, including the amino end of the mature !1protein isolated from brain, were determined by protein !1sequencing COMMENT RNA-binding and enzymatic activities were observed !1simultaneously and may be located in separate domains. The !1physiological substrate of this protein is unknown. GENETICS !$#gene GDB:AUH !'##cross-references GDB:572838; OMIM:600529 !$#map_position Xq12-Xq12 CLASSIFICATION #superfamily AU-specific RNA-binding protein AUH; enoyl-CoA !1hydratase homology KEYWORDS carbon-oxygen lyase; hydro-lyase; RNA binding FEATURE !$68-339 #product AU-specific RNA-binding protein / enoyl-CoA !8hydratase homolog #status experimental #label MAT\ !$101-254 #domain enoyl-CoA hydratase homology #label ECH SUMMARY #length 339 #molecular-weight 35608 #checksum 2728 SEQUENCE /// ENTRY DWRTEP #type complete TITLE dodecenoyl-CoA Delta-isomerase (EC 5.3.3.8) / enoyl-CoA hydratase (EC 4.2.1.17) / 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35), peroxisomal - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 13-Aug-1999 ACCESSIONS A23575; A35531; I55262; S74113 REFERENCE A23575 !$#authors Osumi, T.; Ishii, N.; Hijikata, M.; Kamijo, K.; Ozasa, H.; !1Furuta, S.; Miyazawa, S.; Kondo, K.; Inoue, K.; Kagamiyama, !1H.; Hashimoto, T. !$#journal J. Biol. Chem. (1985) 260:8905-8910 !$#title Molecular cloning and nucleotide sequence of the cDNA for !1rat peroxisomal enoyl-CoA: hydratase-3-hydroxyacyl-CoA !1dehydrogenase bifunctional enzyme. !$#cross-references MUID:85261258; PMID:4019459 !$#accession A23575 !'##molecule_type mRNA !'##residues 1-722 ##label OSU !'##cross-references GB:K03249; NID:g206068; PIDN:AAA41825.1; !1PID:g206069 REFERENCE A35531 !$#authors Palosaari, P.M.; Hiltunen, J.K. !$#journal J. Biol. Chem. (1990) 265:2446-2449 !$#title Peroxisomal bifunctional protein from rat liver is a !1trifunctional enzyme possessing 2-enoyl-CoA hydratase, !13-hydroxyacyl-CoA dehydrogenase, and delta(3),delta !1(2)-enoyl-CoA isomerase activities. !$#cross-references MUID:90153855; PMID:2303409 !$#accession A35531 !'##status preliminary !'##molecule_type protein !'##residues 257-276;516-535 ##label PAL REFERENCE I55262 !$#authors Ishii, N.; Hijikata, M.; Osumi, T.; Hashimoto, T. !$#journal J. Biol. Chem. (1987) 262:8144-8150 !$#title Structural organization of the gene for rat enoyl-CoA: !1hydratase-3-hydroxyacyl-CoA dehydrogenase bifunctional !1enzyme. !$#cross-references MUID:87250406; PMID:3036802 !$#accession I55262 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-24 ##label RES !'##cross-references GB:J02748; NID:g206070; PIDN:AAA41826.1; !1PID:g554482 REFERENCE S74113 !$#authors Dieuaide-Noubhani, M.; Novikov, D.; Baumgart, E.; Vanhooren, !1J.C.T.; Fransen, M.; Goethals, M.; Vandekerckhove, J.; van !1Veldhoven, P.P.; Mannaerts, G.P. !$#journal Eur. J. Biochem. (1996) 240:660-666 !$#title Further characterization of the peroxisomal !13-hydroxyacyl-CoA dehydrogenases from rat liver. !1Relationship between the different dehydrogenases and !1evidence that fatty acids and the C(27) bile acids di- and !1tri-hydroxycoprostanic acids are metabolized by separate !1multifunctional proteins. !$#cross-references MUID:97008958; PMID:8856068 !$#accession S74113 !'##molecule_type protein !'##residues 260-265;294-302;520-531;710-719 ##label DIE COMMENT This bifunctional protein is one of the enzymes of the fatty !1acid beta-oxidation cycle in peroxisomes. GENETICS !$#gene pe-CoA CLASSIFICATION #superfamily enoyl-CoA hydratase/3-hydroxyacyl-CoA !1dehydrogenase; 3-hydroxyacyl-CoA dehydrogenase homology; !1enoyl-CoA hydratase homology KEYWORDS carbon-oxygen lyase; fatty acid beta-oxidation; hydro-lyase; !1intramolecular oxidoreductase; isomerase; multifunctional !1enzyme; NAD; peroxisome FEATURE !$22-168 #domain enoyl-CoA hydratase homology #label ECH\ !$296-582 #domain 3-hydroxyacyl-CoA dehydrogenase homology !8#label HCD\ !$298-326 #region beta-alpha-beta NAD nucleotide-binding fold\ !$720-722 #region peroxisome/glyoxysome location signal !8(S-[RKH]-L) motif SUMMARY #length 722 #molecular-weight 78657 #checksum 5865 SEQUENCE /// ENTRY S57651 #type complete TITLE enoyl-CoA hydratase (EC 4.2.1.17) / 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35), peroxisomal - guinea pig ORGANISM #formal_name Cavia porcellus #common_name guinea pig DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S68697; S57651 REFERENCE S68697 !$#authors Caira, F.; Cherkaoui-Malki, M.; Hoefler, G.; Latruffe, N. !$#journal FEBS Lett. (1996) 378:57-60 !$#title Cloning and tissue expression of two cDNAs encoding the !1peroxisomal 2-enoyl-CoA hydratase/3-hydroxyacyl-CoA !1dehydrogenase in the guinea pig liver. !$#cross-references MUID:96140708; PMID:8549802 !$#accession S68697 !'##molecule_type mRNA !'##residues 1-726 ##label CA2 !'##cross-references EMBL:X85112; EMBL:X92742; NID:g1181205; !1PIDN:CAA63403.1; PID:g1181206 CLASSIFICATION #superfamily enoyl-CoA hydratase/3-hydroxyacyl-CoA !1dehydrogenase; 3-hydroxyacyl-CoA dehydrogenase homology; !1enoyl-CoA hydratase homology KEYWORDS carbon-oxygen lyase; hydro-lyase; NAD; oxidoreductase; !1peroxisome FEATURE !$22-171 #domain enoyl-CoA hydratase homology #label ECH\ !$299-586 #domain 3-hydroxyacyl-CoA dehydrogenase homology !8#label HCD\ !$301-329 #region beta-alpha-beta NAD nucleotide-binding fold\ !$724-726 #region peroxisome/glyoxysome location signal !8(S-[RKH]-L) motif SUMMARY #length 726 #molecular-weight 79374 #checksum 4128 SEQUENCE /// ENTRY A49681 #type complete TITLE long-chain-fatty-acid beta-oxidation multienzyme complex alpha chain precursor, mitochondrial - rat CONTAINS long-chain-3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.211); long-chain-enoyl-CoA hydratase (EC 4.2.1.74) ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A49681 REFERENCE A49681 !$#authors Kamijo, T.; Aoyama, T.; Miyazaki, J.; Hashimoto, T. !$#journal J. Biol. Chem. (1993) 268:26452-26460 !$#title Molecular cloning of the cDNAs for the subunits of rat !1mitochondrial fatty acid beta-oxidation multienzyme complex. !1Structural and functional relationships to other !1mitochondrial and peroxisomal beta-oxidation enzymes. !$#cross-references MUID:94075334; PMID:8253773 !$#accession A49681 !'##status preliminary !'##molecule_type mRNA; protein !'##residues 1-763 ##label KAM !'##cross-references GB:D16478; NID:g510107; PIDN:BAA03939.1; !1PID:g510108 !'##experimental_source Wistar, liver !'##note sequence extracted from NCBI backbone (NCBIN:140844, !1NCBIP:140846) COMPLEX heterooctamer of 4 alpha and 4 beta chains CLASSIFICATION #superfamily enoyl-CoA hydratase/3-hydroxyacyl-CoA !1dehydrogenase; 3-hydroxyacyl-CoA dehydrogenase homology; !1enoyl-CoA hydratase homology KEYWORDS carbon-oxygen lyase; fatty acid beta-oxidation; !1heterooctamer; hydro-lyase; mitochondrion; NAD; !1oxidoreductase FEATURE !$62-218 #domain enoyl-CoA hydratase homology #label ECH\ !$361-640 #domain 3-hydroxyacyl-CoA dehydrogenase homology !8#label HCD\ !$363-391 #region beta-alpha-beta NAD nucleotide-binding fold SUMMARY #length 763 #molecular-weight 82512 #checksum 9788 SEQUENCE /// ENTRY JX0199 #type complete TITLE fatty-acid beta-oxidation multienzyme complex alpha chain - Pseudomonas fragi CONTAINS 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35); enoyl-CoA hydratase (EC 4.2.1.17) ORGANISM #formal_name Pseudomonas fragi DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JX0199; PS0267; JX0308 REFERENCE JX0199 !$#authors Sato, S.; Hayashi, M.; Imamura, S.; Ozeki, Y.; Kawaguchi, A. !$#journal J. Biochem. (1992) 111:8-15 !$#title Primary structures of the genes, faoA and faoB, from !1Pseudomonas fragi B-0771 which encode the two subunits of !1the HDT multienzyme complex involved in fatty acid !1beta-oxidation. !$#cross-references MUID:92299657; PMID:1607366 !$#accession JX0199 !'##molecule_type DNA !'##residues 1-715 ##label SAT !'##cross-references DDBJ:D10710 !'##experimental_source strain B-0771 !$#accession PS0267 !'##molecule_type protein !'##residues 1-94;143-172;182-203;223-238;270-280;284-288,'X',290-297, !1'XX',300;344-359;375-379;'X',400-423,'X',425-430,'X', !1432;440-494,'X',496-502;514-526;531-561;565-570,'X',572-573, !1'X',575-577 ##label SAT1 REFERENCE JX0308 !$#authors Sato, S.; Ozeki, Y.; Kawaguchi, A. !$#journal J. Biochem. (1994) 115:286-292 !$#title Transcription of the faoAB operon which encodes the HDT !1multienzyme complex involved in fatty acid beta-oxidation in !1Pseudomonas fragi B-0771. !$#cross-references MUID:94266755; PMID:8206878 !$#accession JX0308 !'##molecule_type DNA !'##residues 1-95 ##label SA2 GENETICS !$#gene faoA COMPLEX heterotetramer of 2 alpha and 2 beta chains FUNCTION !$#description this multienzyme complex has three enzymatic activities; !1enoyl-CoA hydratase (EC 4.2.1.17), 3-hydroxyacyl-CoA !1dehydrogenase (EC 1.1.1.35) and acetyl-CoA acyltransferase !1(EC 2.3.1.16) !$#pathway fatty acid beta-oxidation CLASSIFICATION #superfamily enoyl-CoA hydratase/3-hydroxyacyl-CoA !1dehydrogenase; 3-hydroxyacyl-CoA dehydrogenase homology; !1enoyl-CoA hydratase homology KEYWORDS carbon-oxygen lyase; fatty acid beta-oxidation; !1heterotetramer; hydro-lyase; NAD; oxidoreductase FEATURE !$30-185 #domain enoyl-CoA hydratase homology #label ECH\ !$314-593 #domain 3-hydroxyacyl-CoA dehydrogenase homology !8#label HCD\ !$316-344 #region beta-alpha-beta NAD nucleotide-binding fold SUMMARY #length 715 #molecular-weight 77137 #checksum 7599 SEQUENCE /// ENTRY A39592 #type complete TITLE fatty acid beta oxidation complex alpha chain - Escherichia coli (strain K-12) CONTAINS 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35); 3-hydroxyacyl-CoA epimerase; dodecenoyl-CoA Delta-isomerase (EC 5.3.3.8); enoyl-CoA hydratase (EC 4.2.1.17) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS A39592; S30737; JV0108; JQ0654; G65189 REFERENCE A39592 !$#authors Yang, X.Y.H.; Schulz, H.; Elzinga, M.; Yang, S.Y. !$#journal Biochemistry (1991) 30:6788-6795 !$#title Nucleotide sequence of the promoter and fadB gene of the !1fadBA operon and primary structure of the multifunctional !1fatty acid oxidation protein from Escherichia coli. !$#cross-references MUID:91291827; PMID:1712230 !$#accession A39592 !'##status preliminary !'##molecule_type DNA !'##residues 1-729 ##label YAN !'##cross-references GB:M74164; GB:J05332; NID:g145902; PIDN:AAA62777.1; !1PID:g145903 REFERENCE S30660 !$#authors Daniels, D.L.; Plunkett III, G.; Burland, V.; Blattner, F.R. !$#journal Science (1992) 257:771-778 !$#title Analysis of the Escherichia coli genome: DNA sequence of the !1region from 84.5 to 86.5 minutes. !$#cross-references MUID:92358234; PMID:1379743 !$#accession S30737 !'##status preliminary !'##molecule_type DNA !'##residues 1-729 ##label DAN !'##cross-references EMBL:M87049; NID:g836656; PIDN:AAA67643.1; !1PID:g148246 REFERENCE JV0108 !$#authors Dirusso, C.C. !$#journal J. Bacteriol. (1990) 172:6459-6468 !$#title Primary sequence of the Escherichia coli fadBA operon, !1encoding the fatty acid-oxidizing multienzyme complex, !1indicates a high degree of homology to eucaryotic enzymes. !$#cross-references MUID:91035260; PMID:1699931 !$#accession JV0108 !'##molecule_type DNA !'##residues 1-517,'R',519-729 ##label DIR !'##cross-references GB:M59368; NID:g145899; PIDN:AAA23750.1; !1PID:g145900 REFERENCE JQ0654 !$#authors Nakahigashi, K.; Inokuchi, H. !$#journal Nucleic Acids Res. (1990) 18:4937 !$#title Nucleotide sequence of the fadA and fadB genes from !1Escherichia coli. !$#cross-references MUID:90370500; PMID:2204034 !$#accession JQ0654 !'##molecule_type DNA !'##residues 1-663,'L',665,'A',667-729 ##label NAK !'##cross-references EMBL:X52837; NID:g41370; PIDN:CAB40809.1; !1PID:g4584722 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65189 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-729 ##label BLAT !'##cross-references GB:AE000460; GB:U00096; NID:g2367315; !1PIDN:AAC76849.1; PID:g1790281; UWGP:b3846 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene fadB !$#map_position 87 min CLASSIFICATION #superfamily enoyl-CoA hydratase/3-hydroxyacyl-CoA !1dehydrogenase; 3-hydroxyacyl-CoA dehydrogenase homology; !1enoyl-CoA hydratase homology KEYWORDS carbon-oxygen lyase; fatty acid beta-oxidation; hydro-lyase; !1intramolecular oxidoreductase; isomerase; NAD; !1oxidoreductase FEATURE !$29-184 #domain enoyl-CoA hydratase homology #label ECH\ !$313-593 #domain 3-hydroxyacyl-CoA dehydrogenase homology !8#label HCD\ !$315-343 #region beta-alpha-beta NAD nucleotide-binding fold SUMMARY #length 729 #molecular-weight 79593 #checksum 2950 SEQUENCE /// ENTRY DWBYH #type complete TITLE imidazoleglycerol-phosphate dehydratase (EC 4.2.1.19) [validated] - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein O4830; protein YOR202w ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1991 #sequence_revision 02-Aug-1996 #text_change 16-Jun-2000 ACCESSIONS S67094; S07681; S05903 REFERENCE S66685 !$#authors Hughes, B.; Pohl, T.M. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67094 !'##molecule_type DNA !'##residues 1-220 ##label HUG !'##cross-references EMBL:Z75110; NID:g1420476; PIDN:CAA99417.1; !1PID:g1420477; GSPDB:GN00015; MIPS:YOR202w !'##experimental_source strain S288C REFERENCE S07681 !$#authors Struhl, K. !$#journal Nucleic Acids Res. (1985) 13:8587-8601 !$#title Nucleotide sequence and transcriptional mapping of the yeast !1pet56-his3-ded1 gene region. !$#cross-references MUID:86093663; PMID:3001645 !$#accession S07681 !'##molecule_type DNA !'##residues 1-108,'LA',112-220 ##label STR !'##cross-references EMBL:X03245; NID:g3778; PIDN:CAA27003.1; PID:g3780 !'##note the authors translated the codon GCG for residue 110 as Gly REFERENCE S05903 !$#authors Struhl, K.; Davis, R.W. !$#journal J. Mol. Biol. (1981) 152:553-568 !$#title Promoter mutants of the yeast his3 gene. !$#cross-references MUID:82122608; PMID:6173490 !$#accession S05903 !'##molecule_type DNA !'##residues 1-32 ##label ST2 !'##cross-references EMBL:J01330; NID:g171684; PIDN:AAA88723.1; !1PID:g1197052 !'##note the authors translated the codon CGT for residue 10 as Leu GENETICS !$#gene SGD:HIS3; MIPS:YOR202w !'##cross-references SGD:S0005728; MIPS:YOR202w !$#map_position 15R COMPLEX the inactive apoprotein is a homotrimer; assembles in !1presence of manganese to an active 24-mer [validated, !1MUID:95194313] FUNCTION !$#description EC4.2.1.19 [validated, MUID:95194313] !$#pathway histidine biosynthesis !$#note Mn(2+) is essential for activity !$#note yeast and plant enzyme is monofunctional lacking the !1histidinol phosphatase activity present in E. coli !1[validated, MUID:94345005] CLASSIFICATION #superfamily imidazoleglycerol-phosphate dehydratase; !1imidazoleglycerol-phosphate dehydratase homology KEYWORDS carbon-oxygen lyase; histidine biosynthesis; hydro-lyase FEATURE !$54-219 #domain imidazoleglycerol-phosphate dehydratase !8homology #label IPD SUMMARY #length 220 #molecular-weight 23833 #checksum 3599 SEQUENCE /// ENTRY S31235 #type complete TITLE imidazoleglycerol-phosphate dehydratase (EC 4.2.1.19) - yeast (Saccharomyces kluyveri) ORGANISM #formal_name Saccharomyces kluyveri DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S31235; S23872 REFERENCE S31234 !$#authors Weinstock, K.G.; Strathern, J.N. !$#journal Yeast (1993) 9:351-361 !$#title Molecular genetics in Saccharomyces kluyveri: the HIS3 !1homolog and its use as a selectable marker gene in S. !1kluyveri and Saccharomyces cerevisiae. !$#cross-references MUID:93289813; PMID:8511965 !$#accession S31235 !'##molecule_type DNA !'##residues 1-232 ##label WEI !'##cross-references EMBL:Z14125; NID:g4864; PIDN:CAA78497.1; PID:g4865 GENETICS !$#gene HIS3 CLASSIFICATION #superfamily imidazoleglycerol-phosphate dehydratase; !1imidazoleglycerol-phosphate dehydratase homology KEYWORDS carbon-oxygen lyase; hydro-lyase FEATURE !$66-231 #domain imidazoleglycerol-phosphate dehydratase !8homology #label IPD SUMMARY #length 232 #molecular-weight 25325 #checksum 5839 SEQUENCE /// ENTRY S26196 #type complete TITLE imidazoleglycerol-phosphate dehydratase (EC 4.2.1.19) - fungus (Trichoderma harzianum) ORGANISM #formal_name Trichoderma harzianum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S26196; S19787 REFERENCE S26196 !$#authors Goldman, G.H.; Demolder, J.; Dewaele, S.; Herrera-Estrella, !1A.; Geremia, R.A.; van Montagu, M.; Contreras, R. !$#journal Mol. Gen. Genet. (1992) 234:481-488 !$#title Molecular cloning of the imidazoleglycerolphosphate !1dehydratase gene of Trichoderma harzianum by genetic !1complementation in Saccharomyces cerevisiae using a direct !1expression vector. !$#cross-references MUID:93024323; PMID:1406594 !$#accession S26196 !'##molecule_type mRNA !'##residues 1-208 ##label GOL !'##cross-references EMBL:Z11528; NID:g5176; PIDN:CAA77617.1; PID:g5177 GENETICS !$#gene igh CLASSIFICATION #superfamily imidazoleglycerol-phosphate dehydratase; !1imidazoleglycerol-phosphate dehydratase homology KEYWORDS carbon-oxygen lyase; histidine biosynthesis; hydro-lyase FEATURE !$58-208 #domain imidazoleglycerol-phosphate dehydratase !8homology #label IPD SUMMARY #length 208 #molecular-weight 22356 #checksum 3322 SEQUENCE /// ENTRY DWECHB #type complete TITLE hisB bifunctional enzyme - Escherichia coli (strain K-12) CONTAINS histidinol-phosphatase (EC 3.1.3.15); imidazoleglycerol-phosphate dehydratase (EC 4.2.1.19) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1989 #sequence_revision 14-Nov-1997 #text_change 01-Mar-2002 ACCESSIONS E64967; A30257 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64967 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-356 ##label BLAT !'##cross-references GB:AE000293; GB:U00096; NID:g2367127; !1PIDN:AAC75083.1; PID:g1788333; UWGP:b2022 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A30257 !$#authors Chiariotti, L.; Nappo, A.G.; Carlomagno, M.S.; Bruni, C.B. !$#journal Mol. Gen. Genet. (1986) 202:42-47 !$#title Gene structure in the histidine operon of Escherichia coli. !1Identification and nucleotide sequence of the hisB gene. !$#cross-references MUID:86174354; PMID:3007936 !$#accession A30257 !'##molecule_type DNA !'##residues 2-356 ##label CHI !'##cross-references GB:X03416; GB:K00054; NID:g41694; PIDN:CAA27151.1; !1PID:g41696 GENETICS !$#gene hisB !$#map_position 44 min !$#start_codon TTG COMPLEX the active form probably is a dimer FUNCTION !$#pathway histidine biosynthesis !$#note this bifunctional enzyme catalyzes the seventh and ninth !1steps of histidine biosynthesis CLASSIFICATION #superfamily hisB bifunctional enzyme; !1imidazoleglycerol-phosphate dehydratase homology KEYWORDS carbon-oxygen lyase; histidine biosynthesis; hydro-lyase; !1phosphoric monoester hydrolase FEATURE !$194-356 #domain imidazoleglycerol-phosphate dehydratase !8homology #label IPD SUMMARY #length 356 #molecular-weight 40409 #checksum 6764 SEQUENCE /// ENTRY DWEBHB #type complete TITLE hisB bifunctional enzyme - Salmonella typhimurium CONTAINS histidinol-phosphatase (EC 3.1.3.15); imidazoleglycerol-phosphate dehydratase (EC 4.2.1.19) ORGANISM #formal_name Salmonella typhimurium DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jun-2000 ACCESSIONS JS0159 REFERENCE JS0131 !$#authors Carlomagno, M.S.; Chiariotti, L.; Alifano, P.; Nappo, A.G.; !1Bruni, C.B. !$#journal J. Mol. Biol. (1988) 203:585-606 !$#title Structure and function of the Salmonella typhimurium and !1Escherichia coli K-12 histidine operons. !$#cross-references MUID:89094829; PMID:3062174 !$#accession JS0159 !'##molecule_type DNA !'##residues 1-354 ##label CAR !'##cross-references GB:X13464; NID:g47719; PIDN:CAA31825.1; !1PID:g1333842 COMMENT This bifunctional enzyme is involved in the histidine !1biosynthetic pathway. GENETICS !$#gene hisB !$#map_position 42 min CLASSIFICATION #superfamily hisB bifunctional enzyme; !1imidazoleglycerol-phosphate dehydratase homology KEYWORDS carbon-oxygen lyase; histidine biosynthesis; hydro-lyase; !1phosphoric monoester hydrolase FEATURE !$193-354 #domain imidazoleglycerol-phosphate dehydratase !8homology #label IPD SUMMARY #length 354 #molecular-weight 40133 #checksum 7202 SEQUENCE /// ENTRY TSECA #type complete TITLE tryptophan synthase (EC 4.2.1.20) alpha chain [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 28-Feb-1980 #sequence_revision 28-Feb-1980 #text_change 01-Mar-2002 ACCESSIONS E93746; A92034; G64873; I52505; T47191; A01151 REFERENCE A93746 !$#authors Yanofsky, C.; Platt, T.; Crawford, I.P.; Nichols, B.P.; !1Christie, G.E.; Horowitz, H.; van Cleemput, M.; Wu, A.M. !$#journal Nucleic Acids Res. (1981) 9:6647-6668 !$#title The complete nucleotide sequence of the tryptophan operon of !1Escherichia coli. !$#cross-references MUID:82150258; PMID:7038627 !$#accession E93746 !'##molecule_type DNA !'##residues 1-268 ##label YAN !'##cross-references GB:J01714; GB:M12471; GB:M12472; GB:M24865; !1GB:M25264; GB:M25593; GB:M59208; NID:g147953; !1PIDN:AAA57301.1; PID:g147959 REFERENCE A92034 !$#authors Guest, J.R.; Drapeau, G.R.; Carlton, B.C.; Yanofsky, C. !$#journal J. Biol. Chem. (1967) 242:5442-5446 !$#title The amino acid sequence of the A protein (alpha subunit) of !1the tryptophan synthetase of Escherichia coli. V. Order of !1tryptic peptides and the complete amino acid sequence. !$#cross-references MUID:68086712; PMID:4863752 !$#accession A92034 !'##molecule_type protein !'##residues 1-268 ##label GUE !'##note this sequence differs slightly from that shown REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64873 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-268 ##label BLAT !'##cross-references GB:AE000224; GB:U00096; NID:g1787509; !1PIDN:AAC74342.1; PID:g1787514; UWGP:b1260 !'##experimental_source strain K-12, substrain MG1655 REFERENCE I52505 !$#authors Tucker, S.D.; Murgola, E.J.; Pagel, F.T. !$#journal Biochimie (1989) 71:729-739 !$#title Missense and nonsense suppressors can correct frameshift !1mutations. !$#cross-references MUID:89323228; PMID:2502189 !$#accession I52505 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 200-208,'IA',211-212,'WYFRPGSGKSSD' ##label RES !'##cross-references EMBL:X16698; NID:g43185; PIDN:CAA34671.1; !1PID:g43186 !'##experimental_source strain K-12 REFERENCE Z24381 !$#authors Milkman, R. !$#submission submitted to the EMBL Data Library, March 1995 !$#accession T47191 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-268 ##label MIL !'##cross-references EMBL:U23494; PIDN:AAA65164.1 !'##experimental_source strain ECOR 31 GENETICS !$#gene trpA !$#map_position 28 min COMPLEX heterotetramer; two alpha and two beta chains FUNCTION !$#description catalyzes conversion of indoleglycerol phosphate and serine !1to tryptophan and glyceraldehyde 3-phosphate !$#pathway tryptophan biosynthesis !$#note cofactor pyridoxal phosphate !$#note last step in pathway CLASSIFICATION #superfamily tryptophan synthase alpha chain; tryptophan !1synthase alpha chain homology KEYWORDS carbon-oxygen lyase; heterotetramer; hydro-lyase; tryptophan !1biosynthesis FEATURE !$18-246 #domain tryptophan synthase alpha chain homology !8#label TRPA\ !$49 #active_site Glu #status predicted SUMMARY #length 268 #molecular-weight 28724 #checksum 3532 SEQUENCE /// ENTRY TSEBAT #type complete TITLE tryptophan synthase (EC 4.2.1.20) alpha chain - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 28-Feb-1980 #sequence_revision 28-Feb-1980 #text_change 24-Sep-1999 ACCESSIONS A93837; A92126; A01152 REFERENCE A93837 !$#authors Nichols, B.P.; Yanofsky, C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1979) 76:5244-5248 !$#title Nucleotide sequences of trpA of Salmonella typhimurium and !1Escherichia coli: an evolutionary comparison. !$#cross-references MUID:80056671; PMID:388433 !$#accession A93837 !'##molecule_type DNA !'##residues 1-268 ##label NIC !'##cross-references GB:V01376; NID:g47938; PIDN:CAA24666.1; PID:g47940 REFERENCE A92126 !$#authors Li, S.L.; Yanofsky, C. !$#journal J. Biol. Chem. (1973) 248:1830-1836 !$#title Amino acid sequence studies with the tryptophan synthetase !1alpha chain of Salmonella typhimurium. !$#cross-references MUID:73149276; PMID:4571777 !$#contents tentative sequence !$#accession A92126 !'##molecule_type protein !'##residues 1-268 ##label LIS GENETICS !$#gene trpA COMPLEX heterotetramer; two alpha and two beta chains FUNCTION !$#description catalyzes conversion of indoleglycerol phosphate and serine !1to tryptophan and glyceraldehyde 3-phosphate !$#pathway tryptophan biosynthesis !$#note cofactor pyridoxal phosphate !$#note last step in pathway CLASSIFICATION #superfamily tryptophan synthase alpha chain; tryptophan !1synthase alpha chain homology KEYWORDS carbon-oxygen lyase; heterotetramer; hydro-lyase; tryptophan !1biosynthesis FEATURE !$18-246 #domain tryptophan synthase alpha chain homology !8#label TRPA\ !$49 #active_site Glu #status predicted SUMMARY #length 268 #molecular-weight 28670 #checksum 5229 SEQUENCE /// ENTRY TSAEAA #type complete TITLE tryptophan synthase (EC 4.2.1.20) alpha chain - Klebsiella pneumoniae ORGANISM #formal_name Klebsiella pneumoniae DATE 29-Jul-1981 #sequence_revision 29-Jul-1981 #text_change 05-Dec-1998 ACCESSIONS A93724; A92127; A01153 REFERENCE A93724 !$#authors Nichols, B.P.; Blumenberg, M.; Yanofsky, C. !$#journal Nucleic Acids Res. (1981) 9:1743-1755 !$#title Comparison of the nucleotide sequence of trpA and sequences !1immediately beyond the trp operon of Klebsiella aerogenes, !1Salmonella typhimurium and Escherichia coli. !$#cross-references MUID:81199002; PMID:6262736 !$#contents Klebsiella aerogenes !$#accession A93724 !'##molecule_type DNA !'##residues 1-269 ##label NIC REFERENCE A92127 !$#authors Li, S.L.; Yanofsky, C. !$#journal J. Biol. Chem. (1973) 248:1837-1843 !$#title Amino acid sequence studies with the tryptophan synthetase !1alpha chain of Aerobacter aerogenes. !$#cross-references MUID:73149277; PMID:4571778 !$#contents Aerobacter aerogenes !$#accession A92127 !'##molecule_type protein !'##residues 1,'Q',3-12,'K',14,'R',16,'G',18-23,'I',25-29,'T',31-55,'N', !157-86,'L',88-90,'N',92-104,'K',106-269 ##label LIS GENETICS !$#gene trpA FUNCTION !$#description catalyzes conversion of indoleglycerol phosphate and serine !1to tryptophan and glyceraldehyde 3-phosphate !$#pathway tryptophan biosynthesis !$#note cofactor pyridoxal phosphate !$#note last step in pathway CLASSIFICATION #superfamily tryptophan synthase alpha chain; tryptophan !1synthase alpha chain homology KEYWORDS carbon-oxygen lyase; hydro-lyase; tryptophan biosynthesis FEATURE !$18-246 #domain tryptophan synthase alpha chain homology !8#label TRPA\ !$49 #active_site Glu #status predicted SUMMARY #length 269 #molecular-weight 28557 #checksum 4991 SEQUENCE /// ENTRY TSPSAA #type complete TITLE tryptophan synthase (EC 4.2.1.20) alpha chain - Pseudomonas aeruginosa ORGANISM #formal_name Pseudomonas aeruginosa DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 16-Feb-1997 ACCESSIONS B25355 REFERENCE A93059 !$#authors Hadero, A.; Crawford, I.P. !$#journal Mol. Biol. Evol. (1986) 3:191-204 !$#title Nucleotide sequence of the genes for tryptophan synthase in !1Pseudomonas aeruginosa. !$#cross-references MUID:88174343; PMID:3127651 !$#accession B25355 !'##molecule_type DNA !'##residues 1-267 ##label HAD GENETICS !$#gene trpA !$#map_position 29 CLASSIFICATION #superfamily tryptophan synthase alpha chain; tryptophan !1synthase alpha chain homology KEYWORDS carbon-oxygen lyase; hydro-lyase; tryptophan biosynthesis FEATURE !$18-244 #domain tryptophan synthase alpha chain homology !8#label TRPA\ !$49 #active_site Glu #status predicted SUMMARY #length 267 #molecular-weight 28417 #checksum 5971 SEQUENCE /// ENTRY JQ2127 #type complete TITLE tryptophan synthase (EC 4.2.1.20) alpha chain - Pseudomonas syringae ORGANISM #formal_name Pseudomonas syringae DATE 03-Feb-1994 #sequence_revision 03-Feb-1994 #text_change 18-Jun-1999 ACCESSIONS JQ2127 REFERENCE JQ2125 !$#authors Auerbach, S.; Gao, J.; Gussin, G.N. !$#journal Gene (1993) 123:25-32 !$#title Nucleotide sequences of the trpI, trpB, and trpA genes of !1Pseudomonas syringae; positive control unique to fluorescent !1pseudomonads. !$#cross-references MUID:93138427; PMID:8423001 !$#accession JQ2127 !'##molecule_type DNA !'##residues 1-269 ##label AUE !'##cross-references GB:M95710; NID:g151618; PIDN:AAA26013.1; !1PID:g151619 GENETICS !$#gene trpA CLASSIFICATION #superfamily tryptophan synthase alpha chain; tryptophan !1synthase alpha chain homology KEYWORDS carbon-oxygen lyase; hydro-lyase; tryptophan biosynthesis FEATURE !$18-245 #domain tryptophan synthase alpha chain homology !8#label TRPA SUMMARY #length 269 #molecular-weight 28439 #checksum 3595 SEQUENCE /// ENTRY A30768 #type complete TITLE tryptophan synthase (EC 4.2.1.20) alpha chain - Pseudomonas putida ORGANISM #formal_name Pseudomonas putida DATE 19-May-1989 #sequence_revision 02-Dec-1994 #text_change 18-Jun-1999 ACCESSIONS A30768; S03836 REFERENCE A94529 !$#authors Eberly, L.; Crawford, I.P. !$#submission submitted to GenBank, October 1988 !$#accession A30768 !'##molecule_type DNA !'##residues 1-269 ##label EBE !'##cross-references EMBL:X13299; NID:g45748; PIDN:CAA31662.1; !1PID:g45750 GENETICS !$#gene trpA CLASSIFICATION #superfamily tryptophan synthase alpha chain; tryptophan !1synthase alpha chain homology KEYWORDS carbon-oxygen lyase; heterotetramer; hydro-lyase; tryptophan !1biosynthesis FEATURE !$2-269 #product tryptophan synthase alpha chain #status !8experimental #label MAT\ !$18-245 #domain tryptophan synthase alpha chain homology !8#label TRPA\ !$49 #active_site Glu #status predicted SUMMARY #length 269 #molecular-weight 28460 #checksum 4318 SEQUENCE /// ENTRY D43664 #type complete TITLE tryptophan synthase (EC 4.2.1.20) alpha chain - Caulobacter crescentus ORGANISM #formal_name Caulobacter crescentus DATE 03-Mar-1993 #sequence_revision 02-Dec-1994 #text_change 18-Jul-2001 ACCESSIONS D43664; E87688 REFERENCE A43664 !$#authors Ross, C.M.; Winkler, M.E. !$#journal J. Bacteriol. (1988) 170:757-768 !$#title Structure of the Caulobacter crescentus trpFBA operon. !$#cross-references MUID:88115177; PMID:2828322 !$#accession D43664 !'##molecule_type DNA !'##residues 1-275 ##label ROS !'##cross-references GB:M19129; NID:g144284; PIDN:AAA23058.1; !1PID:g144288 REFERENCE A87249 !$#authors Nierman, W.C.; Feldblyum, T.V.; Paulsen, I.T.; Nelson, K.E.; !1Eisen, J.; Heidelberg, J.F.; Alley, M.; Ohta, N.; Maddock, !1J.R.; Potocka, I.; Nelson, W.C.; Newton, A.; Stephens, C.; !1Phadke, N.D.; Ely, B.; Laub, M.T.; DeBoy, R.T.; Dodson, !1R.J.; Durkin, A.S.; Gwinn, M.L.; Haft, D.H.; Kolonay, J.F.; !1Smit, J.; Craven, M.; Khouri, H.; Shetty, J.; Berry, K.; !1Utterback, T.; Tran, K.; Wolf, A.; Vamathevan, J.; !1Ermolaeva, M.; White, O.; Salzberg, S.L.; Shapiro, L.; !1Venter, J.C.; Fraser, C.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (2001) 98:4136-4141 !$#title Complete Genome Sequence of Caulobacter crescentus. !$#cross-references MUID:21173698; PMID:11259647 !$#accession E87688 !'##status preliminary !'##molecule_type DNA !'##residues 1-275 ##label STO !'##cross-references GB:AE005673; NID:g13425279; PIDN:AAK25505.1; !1GSPDB:GN00148 GENETICS !$#gene CC3543 CLASSIFICATION #superfamily tryptophan synthase alpha chain; tryptophan !1synthase alpha chain homology KEYWORDS carbon-oxygen lyase; hydro-lyase FEATURE !$20-247 #domain tryptophan synthase alpha chain homology !8#label TRPA\ !$51 #active_site Glu #status predicted SUMMARY #length 275 #molecular-weight 28519 #checksum 1120 SEQUENCE /// ENTRY JS0344 #type complete TITLE tryptophan synthase (EC 4.2.1.20) alpha chain - Lactobacillus casei ORGANISM #formal_name Lactobacillus casei DATE 31-Mar-1990 #sequence_revision 02-Dec-1994 #text_change 16-Jun-2000 ACCESSIONS S42347; JS0344 REFERENCE S42342 !$#authors Natori, Y.; Kano, Y.; Imamoto, F. !$#journal J. Biochem. (1990) 107:248-255 !$#title Nucleotide sequences and genomic constitution of five !1tryptophan genes of Lactobacillus casei. !$#cross-references MUID:90299861; PMID:2113923 !$#accession S42347 !'##status preliminary !'##molecule_type DNA !'##residues 1-266 ##label NAT !'##cross-references EMBL:D00496; NID:g216754; PIDN:BAA00387.1; !1PID:g216760 !'##experimental_source isolate RNL7 GENETICS !$#gene trpA COMPLEX heterodimer of alpha and beta chain FUNCTION !$#description catalyzes the conversion of indolylglycerol phosphate into !1tryptophan and glyceraldehyde phosphate !$#pathway tryptophan biosynthesis CLASSIFICATION #superfamily tryptophan synthase alpha chain; tryptophan !1synthase alpha chain homology KEYWORDS carbon-oxygen lyase; hydro-lyase; tryptophan biosynthesis FEATURE !$15-240 #domain tryptophan synthase alpha chain homology !8#label TRPA\ !$46 #active_site Glu #status predicted SUMMARY #length 266 #molecular-weight 28724 #checksum 3350 SEQUENCE /// ENTRY S35130 #type complete TITLE tryptophan synthase (EC 4.2.1.20) alpha chain - Lactococcus lactis subsp. lactis ORGANISM #formal_name Lactococcus lactis subsp. lactis DATE 03-Feb-1994 #sequence_revision 02-Dec-1994 #text_change 03-Aug-2001 ACCESSIONS S35130; F86807 REFERENCE S35123 !$#authors Bardowski, J.; Ehrlich, S.D.; Chopin, A. !$#journal J. Bacteriol. (1992) 174:6563-6570 !$#title Tryptophan biosynthesis genes in Lactococcus lactis subsp. !1lactis. !$#cross-references MUID:93015708; PMID:1400208 !$#accession S35130 !'##molecule_type DNA !'##residues 1-253 ##label BAR !'##cross-references EMBL:M87483; NID:g149514; PIDN:AAA25229.1; !1PID:g149522 REFERENCE A86625 !$#authors Bolotin, A.; Wincker, P.; Mauger, S.; Jaillon, O.; Malarme, !1K.; Weissenbach, J.; Ehrlich, S.D.; Sorokin, A. !$#journal Genome Res. (2001) 11:731-753 !$#title The complete genome sequence of the lactic acid bacterium !1Lactococcus lactis ssp. lactis IL1403. !$#cross-references MUID:21235186; PMID:11337471 !$#accession F86807 !'##status preliminary !'##molecule_type DNA !'##residues 1-253 ##label STO !'##cross-references GB:AE005176; PID:g12724455; PIDN:AAK05560.1; !1GSPDB:GN00146 !'##experimental_source strain IL1403 GENETICS !$#gene trpA CLASSIFICATION #superfamily tryptophan synthase alpha chain; tryptophan !1synthase alpha chain homology KEYWORDS carbon-oxygen lyase; hydro-lyase; tryptophan biosynthesis FEATURE !$14-240 #domain tryptophan synthase alpha chain homology !8#label TRPA\ !$47 #active_site Glu #status predicted SUMMARY #length 253 #molecular-weight 27685 #checksum 7058 SEQUENCE /// ENTRY TSBYAB #type complete TITLE tryptophan synthase (EC 4.2.1.20) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein G3669; protein YGL026c ORGANISM #formal_name Saccharomyces cerevisiae DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 21-Jul-2000 ACCESSIONS A01154; S05864; S64028 REFERENCE A01154 !$#authors Zalkin, H.; Yanofsky, C. !$#journal J. Biol. Chem. (1982) 257:1491-1500 !$#title Yeast gene TRP5: structure, function, regulation. !$#cross-references MUID:82120087; PMID:6276387 !$#accession A01154 !'##molecule_type DNA !'##residues 1-707 ##label ZAL !'##cross-references EMBL:V01342; NID:g4673; PIDN:CAA24635.1; PID:g4674 REFERENCE S05864 !$#authors Brosius, J.; Walz, A. !$#journal Gene (1982) 17:223-228 !$#title DNA sequences flanking an E.coli insertion element IS2 in a !1cloned yeast TRP5 gene. !$#cross-references MUID:82211822; PMID:6282714 !$#accession S05864 !'##molecule_type DNA !'##residues 1-173 ##label BRO !'##cross-references EMBL:V01343; NID:g4675; PIDN:CAA24636.1; PID:g4676 !'##note the authors translated the codon TTT for residue 127 as Ile !'##note in the authors' translation 134-Pro is not shown and an !1additional Val is inserted after 140-Val REFERENCE S64003 !$#authors Hebling, U.; Hofmann, B.; Delius, H. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64028 !'##molecule_type DNA !'##residues 1-707 ##label HEB !'##cross-references EMBL:Z72548; NID:g1322495; PIDN:CAA96727.1; !1PID:g1322496; GSPDB:GN00007; MIPS:YGL026c !'##experimental_source strain S288C GENETICS !$#gene SGD:TRP5; MIPS:YGL026c !'##cross-references SGD:S0002994; MIPS:YGL026c !$#map_position 7L CLASSIFICATION #superfamily yeast tryptophan synthase; tryptophan synthase !1alpha chain homology; tryptophan synthase beta chain !1homology KEYWORDS carbon-oxygen lyase; hydro-lyase; phosphoprotein; pyridoxal !1phosphate; tryptophan biosynthesis FEATURE !$19-247 #domain tryptophan synthase alpha chain homology !8#label TRPA\ !$302-685 #domain tryptophan synthase beta chain homology !8#label TRPB\ !$50 #active_site Glu (alpha-reaction) #status predicted\ !$384 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 707 #molecular-weight 76626 #checksum 8150 SEQUENCE /// ENTRY A32959 #type complete TITLE tryptophan synthase (EC 4.2.1.20) - Neurospora crassa ORGANISM #formal_name Neurospora crassa DATE 20-Oct-1989 #sequence_revision 02-Dec-1994 #text_change 18-Jun-1999 ACCESSIONS A32959; A28162 REFERENCE A32959 !$#authors Burns, D.M.; Yanofsky, C. !$#journal J. Biol. Chem. (1989) 264:3840-3848 !$#title Nucleotide sequence of the Neurospora crassa trp-3 gene !1encoding tryptophan synthetase and comparison of the trp-3 !1polypeptide with its homologs in Saccharomyces cerevisiae !1and Escherichia coli. !$#cross-references MUID:89139440; PMID:2521855 !$#accession A32959 !'##molecule_type DNA !'##residues 1-708 ##label BUR !'##cross-references GB:J04594; NID:g168915; PIDN:AAA33616.1; !1PID:g168916 REFERENCE A28162 !$#authors Pratt, M.L.; DeMoss, J.A. !$#journal J. Biol. Chem. (1988) 263:6872-6876 !$#title Neurospora tryptophan synthase. Characterization of the !1pyridoxal phosphate binding site. !$#cross-references MUID:88198263; PMID:2966157 !$#accession A28162 !'##molecule_type protein !'##residues 358-376,'Q',378;380-385,'D',387;389;391,393-397 ##label PRA GENETICS !$#gene trp-3 CLASSIFICATION #superfamily yeast tryptophan synthase; tryptophan synthase !1alpha chain homology; tryptophan synthase beta chain !1homology KEYWORDS carbon-oxygen lyase; hydro-lyase; phosphoprotein; pyridoxal !1phosphate; tryptophan biosynthesis FEATURE !$18-246 #domain tryptophan synthase alpha chain homology !8#label TRPA\ !$310-692 #domain tryptophan synthase beta chain homology !8#label TRPB\ !$49 #active_site Glu (alpha-reaction) #status predicted\ !$391,392,535 #active_site His, Lys, Cys (beta-reaction) #status !8predicted\ !$392 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 708 #molecular-weight 76451 #checksum 2834 SEQUENCE /// ENTRY JU0401 #type complete TITLE tryptophan synthase (EC 4.2.1.20) - inky cap (Coprinus cinereus) ORGANISM #formal_name Coprinus cinereus DATE 07-Sep-1990 #sequence_revision 02-Dec-1994 #text_change 18-Jun-1999 ACCESSIONS JU0401 REFERENCE JU0401 !$#authors Skrzynia, C.; Binninger, D.M.; Alspaugh II, J.A.; Pukkila, !1P.J. !$#journal Gene (1989) 81:73-82 !$#title Molecular characterization of TRP1, a gene coding for !1tryptophan synthetase in the basidiomycete Coprinus !1cinereus. !$#cross-references MUID:90034188; PMID:2806911 !$#accession JU0401 !'##molecule_type DNA !'##residues 1-702 ##label SKR !'##cross-references GB:M91661; GB:M25225; NID:g167215; PIDN:AAA51432.1; !1PID:g167217 COMMENT Tryptophan synthase catalyzes the final reaction in the !1tryptophan biosynthetic pathway. GENETICS !$#gene TRP1 !$#introns 66/3; 97/3; 144/2; 176/3; 371/2; 385/3; 448/3; 641/1; 666/3 CLASSIFICATION #superfamily yeast tryptophan synthase; tryptophan synthase !1alpha chain homology; tryptophan synthase beta chain !1homology KEYWORDS carbon-oxygen lyase; hydro-lyase; phosphoprotein; pyridoxal !1phosphate; tryptophan biosynthesis FEATURE !$15-246 #domain tryptophan synthase alpha chain homology !8#label TRPA\ !$296-680 #domain tryptophan synthase beta chain homology !8#label TRPB\ !$46 #active_site Glu (alpha-reaction) #status predicted\ !$377,378,523 #active_site His, Lys, Cys (beta-reaction) #status !8predicted\ !$378 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 702 #molecular-weight 75823 #checksum 2687 SEQUENCE /// ENTRY TSECB #type complete TITLE tryptophan synthase (EC 4.2.1.20) beta chain - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Aug-1980 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS H64873; C93746; A92276; A92091; A92101; A01155 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64873 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-397 ##label BLAT !'##cross-references GB:AE000224; GB:U00096; NID:g1787509; !1PIDN:AAC74343.1; PID:g1787515; UWGP:b1261 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A93746 !$#authors Yanofsky, C.; Platt, T.; Crawford, I.P.; Nichols, B.P.; !1Christie, G.E.; Horowitz, H.; van Cleemput, M.; Wu, A.M. !$#journal Nucleic Acids Res. (1981) 9:6647-6668 !$#title The complete nucleotide sequence of the tryptophan operon of !1Escherichia coli. !$#cross-references MUID:82150258; PMID:7038627 !$#accession C93746 !'##molecule_type DNA !'##residues 2-397 ##label YAN !'##cross-references GB:J01714; GB:M12471; GB:M12472; GB:M24865; !1GB:M25264; GB:M25593; GB:M59208; NID:g147953; !1PIDN:AAA57300.1; PID:g147958 REFERENCE A92276 !$#authors Higgins, W.; Miles, E.W.; Fairwell, T. !$#journal J. Biol. Chem. (1980) 255:512-517 !$#title Location of three active site residues in the NH-2-terminal !1sequence of the beta-2 subunit of tryptophan synthase from !1Escherichia coli. !$#cross-references MUID:80094437; PMID:6985892 !$#accession A92276 !'##molecule_type protein !'##residues 2-77,'K',79-100 ##label HIG REFERENCE A92091 !$#authors Fluri, R.; Jackson, L.E.; Lee, W.E.; Crawford, I.P. !$#journal J. Biol. Chem. (1971) 246:6620-6624 !$#title Tryptophan synthetase beta-2 subunit. Primary structure of !1the pyridoxyl peptide from the Escherichia coli enzyme. !$#cross-references MUID:72076855; PMID:4943677 !$#accession A92091 !'##molecule_type protein !'##residues 77-99 ##label FLU REFERENCE A92101 !$#authors Cotton, R.G.H.; Crawford, I.P. !$#journal J. Biol. Chem. (1972) 247:1883-1891 !$#title Tryptophan synthetase beta-2 subunit. Application of genetic !1analysis to the study of primary structure. !$#cross-references MUID:72136306; PMID:4552018 !$#accession A92101 !'##molecule_type protein !'##residues 363-364,'Z',366,'BBKZ',371-397 ##label COT GENETICS !$#gene trpB !$#map_position 28 min COMPLEX heterotetramer; two alpha and two beta chains FUNCTION !$#description catalyzes conversion of indoleglycerol phosphate and serine !1to tryptophan and glyceraldehyde 3-phosphate !$#pathway tryptophan biosynthesis !$#note cofactor pyridoxal phosphate; last step in pathway CLASSIFICATION #superfamily tryptophan synthase beta chain; tryptophan !1synthase beta chain homology KEYWORDS carbon-oxygen lyase; heterotetramer; hydro-lyase; !1phosphoprotein; pyridoxal phosphate; tryptophan biosynthesis FEATURE !$5-388 #domain tryptophan synthase beta chain homology !8#label TRPB\ !$62 #active_site Cys #status experimental\ !$86 #active_site His #status predicted\ !$87 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status experimental SUMMARY #length 397 #molecular-weight 42983 #checksum 307 SEQUENCE /// ENTRY TSEBBT #type complete TITLE tryptophan synthase (EC 4.2.1.20) beta chain - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 31-Dec-1980 #sequence_revision 31-Dec-1980 #text_change 24-Sep-1999 ACCESSIONS A01156 REFERENCE A01156 !$#authors Crawford, I.P.; Nichols, B.P.; Yanofsky, C. !$#journal J. Mol. Biol. (1980) 142:489-502 !$#title Nucleotide sequence of the trpB gene in Escherichia coli and !1Salmonella typhimurium. !$#cross-references MUID:81119809; PMID:7007651 !$#accession A01156 !'##molecule_type DNA !'##residues 1-396 ##label CRA !'##cross-references GB:V01377; NID:g47941; PIDN:CAA24667.1; PID:g47942 GENETICS !$#gene trpB COMPLEX heterotetramer; two alpha and two beta chains FUNCTION !$#description catalyzes conversion of indoleglycerol phosphate and serine !1to tryptophan and glyceraldehyde 3-phosphate !$#pathway tryptophan biosynthesis !$#note cofactor pyridoxal phosphate; last step in pathway CLASSIFICATION #superfamily tryptophan synthase beta chain; tryptophan !1synthase beta chain homology KEYWORDS carbon-oxygen lyase; heterotetramer; hydro-lyase; !1phosphoprotein; pyridoxal phosphate; tryptophan biosynthesis FEATURE !$4-387 #domain tryptophan synthase beta chain homology !8#label TRPB\ !$85 #active_site His #status predicted\ !$86 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 396 #molecular-weight 42806 #checksum 3244 SEQUENCE /// ENTRY JQ2126 #type complete TITLE tryptophan synthase (EC 4.2.1.20) beta chain - Pseudomonas syringae ORGANISM #formal_name Pseudomonas syringae DATE 03-Feb-1994 #sequence_revision 03-Feb-1994 #text_change 18-Jun-1999 ACCESSIONS JQ2126 REFERENCE JQ2125 !$#authors Auerbach, S.; Gao, J.; Gussin, G.N. !$#journal Gene (1993) 123:25-32 !$#title Nucleotide sequences of the trpI, trpB, and trpA genes of !1Pseudomonas syringae; positive control unique to fluorescent !1pseudomonads. !$#cross-references MUID:93138427; PMID:8423001 !$#accession JQ2126 !'##molecule_type DNA !'##residues 1-408 ##label AUE !'##cross-references GB:M95710; NID:g151618; PIDN:AAA26014.1; !1PID:g151620 GENETICS !$#gene trpB FUNCTION !$#description catalyzes conversion of indoleglycerol phosphate and serine !1to tryptophan and glyceraldehyde 3-phosphate !$#pathway tryptophan biosynthesis !$#note cofactor pyridoxal phosphate; last step in pathway CLASSIFICATION #superfamily tryptophan synthase beta chain; tryptophan !1synthase beta chain homology KEYWORDS carbon-oxygen lyase; hydro-lyase; phosphoprotein; pyridoxal !1phosphate; tryptophan biosynthesis FEATURE !$14-397 #domain tryptophan synthase beta chain homology !8#label TRPB\ !$96 #active_site His #status predicted\ !$97 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 408 #molecular-weight 44507 #checksum 1757 SEQUENCE /// ENTRY TSPSBA #type complete TITLE tryptophan synthase (EC 4.2.1.20) beta chain - Pseudomonas aeruginosa ORGANISM #formal_name Pseudomonas aeruginosa DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 05-Dec-1998 ACCESSIONS A25355 REFERENCE A93059 !$#authors Hadero, A.; Crawford, I.P. !$#journal Mol. Biol. Evol. (1986) 3:191-204 !$#title Nucleotide sequence of the genes for tryptophan synthase in !1Pseudomonas aeruginosa. !$#cross-references MUID:88174343; PMID:3127651 !$#accession A25355 !'##molecule_type DNA !'##residues 1-401 ##label HAD GENETICS !$#gene trpB !$#map_position 29 min COMPLEX heterotetramer; two alpha and two beta chains FUNCTION !$#description catalyzes conversion of indoleglycerol phosphate and serine !1to tryptophan and glyceraldehyde 3-phosphate !$#pathway tryptophan biosynthesis !$#note cofactor pyridoxal phosphate; last step in pathway CLASSIFICATION #superfamily tryptophan synthase beta chain; tryptophan !1synthase beta chain homology KEYWORDS carbon-oxygen lyase; heterotetramer; hydro-lyase; !1phosphoprotein; pyridoxal phosphate; tryptophan biosynthesis FEATURE !$10-392 #domain tryptophan synthase beta chain homology !8#label TRPB\ !$91 #active_site His #status predicted\ !$92 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 401 #molecular-weight 43550 #checksum 9591 SEQUENCE /// ENTRY B36044 #type complete TITLE tryptophan synthase (EC 4.2.1.20) beta chain [validated] - Haloferax volcanii (strain WFD11) ORGANISM #formal_name Haloferax volcanii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 26-May-2000 ACCESSIONS B36044 REFERENCE A36044 !$#authors Lam, W.L.; Cohen, A.; Tsouluhas, D.; Doolittle, W.F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:6614-6618 !$#title Genes for tryptophan biosynthesis in the archaebacterium !1Haloferax volcanii. !$#cross-references MUID:90370836; PMID:2118654 !$#accession B36044 !'##status preliminary !'##molecule_type DNA !'##residues 1-423 ##label LAM !'##cross-references GB:M36177; NID:g149041; PIDN:AAA72863.1; !1PID:g149043 !'##experimental_source strain WFD11 GENETICS !$#gene trpB FUNCTION !$#description EC 4.2.1.20 [validated, MUID:90370836]; catalyzes conversion !1of indoleglycerol phosphate and serine to tryptophan and !1glyceraldehyde 3-phosphate !$#pathway tryptophan biosynthesis !$#note cofactor pyridoxal phosphate; last step in pathway CLASSIFICATION #superfamily tryptophan synthase beta chain; tryptophan !1synthase beta chain homology KEYWORDS carbon-oxygen lyase; hydro-lyase; phosphoprotein; pyridoxal !1phosphate; tryptophan biosynthesis FEATURE !$3-402 #domain tryptophan synthase beta chain homology !8#label TRPB\ !$86 #active_site His #status predicted\ !$87 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 423 #molecular-weight 45942 #checksum 5441 SEQUENCE /// ENTRY A55760 #type complete TITLE cystathionine beta-synthase (EC 4.2.1.22) - human ALTERNATE_NAMES beta-thionase; methylcysteine synthase; protein DKFZp727E011.1; serine sulfhydrase ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 09-Jun-2000 #text_change 09-Jun-2000 ACCESSIONS A55760; A59301; S49459; I54342; T46286 REFERENCE A55760 !$#authors Kruger, W.D.; Cox, D.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1994) 91:6614-6618 !$#title A yeast system for expression of human cystathionine !1beta-synthase: structural and functional conservation of the !1human and yeast genes. !$#cross-references MUID:94294429; PMID:8022826 !$#accession A55760 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type mRNA !'##residues 1-360,'G',362-364,'L',365-417,'S',419-491,'S',493-497,'T', !1499-542,'E',544-551 ##label KRU2 !'##cross-references GB:L14577; NID:g1289361 !'##note the sequence is revised in GenBank entry HUMCBSA, release 113.0 REFERENCE A59301 !$#authors Kruger, W.D. !$#submission submitted to GenBank, March 1996 !$#accession A59301 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-551 ##label KRU1 !'##cross-references GB:L14577; NID:g1289361; PIDN:AAA98524.1; !1PID:g1289362 !'##experimental_source cell line hep G2 REFERENCE S49459 !$#authors Chasse, J.F.; Paris, D.; Paly, E.; Kamoun, P.; London, J. !$#submission submitted to the EMBL Data Library, October 1994 !$#description Characterization of human cystathionine beta-synthase (CBS) !1cDNAs: evidence for various 5' untranslated region. !$#accession S49459 !'##molecule_type mRNA !'##residues 1-551 ##label CHA !'##cross-references EMBL:X82166; NID:g558581; PIDN:CAA57656.1; !1PID:g558582 REFERENCE I54342 !$#authors Kraus, J.P.; Le, K.; Swaroop, M.; Ohura, T.; Tahara, T.; !1Rosenberg, L.E.; Roper, M.D.; Kozich, V. !$#journal Hum. Mol. Genet. (1993) 2:1633-1638 !$#title Human cystathionine beta-synthase cDNA: sequence, !1alternative splicing and expression in cultured cells. !$#cross-references MUID:94093551; PMID:7903580 !$#accession I54342 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-551 ##label KRA !'##cross-references GB:L19501; NID:g388715; PIDN:AAA19874.1; !1PID:g388716 REFERENCE Z23030 !$#authors Poustka, A.; Klein, M.; Mewes, H.W.; Weil, B.; Wiemann, S. !$#submission submitted to the Protein Sequence Database, January 2000 !$#accession T46286 !'##molecule_type mRNA !'##residues 'R',78-230,'P',232-333,'L',335-551 ##label POU !'##cross-references EMBL:AL137314 !'##experimental_source adult breast cancer; clone DKFZp727E011 GENETICS !$#gene GDB:CBS; DKFZp727E011.1 !'##cross-references GDB:119754; OMIM:236200 !$#map_position 21q22.3-21q22.3 !$#note defects in this gene may result in homocystinuria FUNCTION !$#description catalyzes the reaction of L-serine and L-homocysteine to !1form cystathione and water !$#pathway cysteine biosynthesis CLASSIFICATION #superfamily cystathionine beta-synthase; CBS homology KEYWORDS carbon-oxygen lyase; cysteine biosynthesis; hydro-lyase; !1phosphoprotein; pyridoxal phosphate FEATURE !$421-469 #domain CBS homology #label CBS\ !$119 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 551 #molecular-weight 60586 #checksum 1142 SEQUENCE /// ENTRY A42790 #type complete TITLE cystathionine beta-synthase (EC 4.2.1.22), splice form I [validated] - rat ALTERNATE_NAMES beta-thionase; hemoprotein H-450 [misnomer]; methylcysteine synthase; serine sulfhydrase CONTAINS cystathionine beta-synthase, splice form III ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS A42790; B42790; JX0145 REFERENCE A42790 !$#authors Swaroop, M.; Bradley, K.; Ohura, T.; Tahara, T.; Roper, !1M.D.; Rosenberg, L.E.; Kraus, J.P. !$#journal J. Biol. Chem. (1992) 267:11455-11461 !$#title Rat cystathionine beta-synthase. Gene organization and !1alternative splicing. !$#cross-references MUID:92283859; PMID:1597473 !$#accession A42790 !'##molecule_type mRNA; protein !'##residues 1-561 ##label SWA1 !'##cross-references GB:M88344; NID:g1364273; PIDN:AAB02042.1; !1PID:g206597 !'##experimental_source strain Sprague-Dawley; liver; splice form I !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing; sequence !1extracted from NCBI backbone (NCBIP:104763) !$#accession B42790 !'##molecule_type mRNA !'##residues 1-513,'Y',529-561 ##label SWA2 !'##cross-references GB:M88346; NID:g206599; PIDN:AAA42024.1; !1PID:g206600 !'##experimental_source liver; splice form III !'##note sequence extracted from NCBI backbone (NCBIP:104768) and !1corrected to correspond with the published sequence REFERENCE JX0145 !$#authors Ishihara, S.; Morohashi, K.; Sadano, H.; Kawabata, S.; !1Gotoh, O.; Omura, T. !$#journal J. Biochem. (1990) 108:899-902 !$#title Molecular cloning and sequence analysis of cDNA coding for !1rat liver hemoprotein H-450. !$#cross-references MUID:91210211; PMID:2089036 !$#accession JX0145 !'##status preliminary !'##molecule_type mRNA !'##residues 1-414,'P',416-513,'Y',529-561 ##label ISH !'##cross-references GB:D01098; NID:g220758; PIDN:BAA00883.1; !1PID:g220759 COMMENT For alternative splice forms, see PIR:C42790. CLASSIFICATION #superfamily cystathionine beta-synthase; CBS homology KEYWORDS alternative splicing; carbon-oxygen lyase; cysteine !1biosynthesis; hydro-lyase; phosphoprotein; pyridoxal !1phosphate FEATURE !$2-561 #product cystathionine beta-synthase, splice form I !8#status experimental #label MAT1\ !$2-513,'Y',529-561 #product cystathionine beta-synthase, splice form III !8#status experimental #label MAT3\ !$417-465 #domain CBS homology #label CBS\ !$116 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 561 #molecular-weight 61454 #checksum 6830 SEQUENCE /// ENTRY C42790 #type complete TITLE cystathionine beta-synthase (EC 4.2.1.22), splice form IV - rat ALTERNATE_NAMES beta-thionase; methylcysteine synthase; serine sulfhydrase CONTAINS cystathionine beta-synthase, inactive splice form II ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS C42790; D42790 REFERENCE A42790 !$#authors Swaroop, M.; Bradley, K.; Ohura, T.; Tahara, T.; Roper, !1M.D.; Rosenberg, L.E.; Kraus, J.P. !$#journal J. Biol. Chem. (1992) 267:11455-11461 !$#title Rat cystathionine beta-synthase. Gene organization and !1alternative splicing. !$#cross-references MUID:92283859; PMID:1597473 !$#accession C42790 !'##molecule_type mRNA !'##residues 1-478 ##label SWA1 !'##cross-references GB:M88347; NID:g206601 !'##experimental_source liver; splice form 4 !'##note sequence extracted from NCBI backbone (NCBIP:104770); this !1translation is not annotated in GenBank entry RATRCBSD, !1release 113.0 !'##note it is uncertain whether this splice form is translated !$#accession D42790 !'##molecule_type mRNA !'##residues 123-478 ##label SWA2 !'##cross-references GB:M88345; NID:g206598 !'##experimental_source liver; inactive splice form 2 !'##note sequence extracted from NCBI backbone (NCBIP:104766); this ORF !1is not annotated in GenBank entry RATRCBSB, release 113.0 !'##note if this splice form is translated it is inactive COMMENT For alternative splice forms, see PIR:A42790. CLASSIFICATION #superfamily cystathionine beta-synthase; CBS homology KEYWORDS alternative splicing; carbon-oxygen lyase; cysteine !1biosynthesis; hydro-lyase; phosphoprotein; pyridoxal !1phosphate FEATURE !$116 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 478 #molecular-weight 52513 #checksum 271 SEQUENCE /// ENTRY SYECPF #type complete TITLE porphobilinogen synthase (EC 4.2.1.24) ALAD [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES 5-aminolevulinic acid dehydratase; aminolevulinate dehydratase ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 26-May-2000 #text_change 01-Mar-2002 ACCESSIONS A64765; JS0127; S10100; S29771; S78616 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64765 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 'MPLDSTNIRQT',1-324 ##label BLAT !'##cross-references GB:AE000143; GB:U00096; NID:g1786554; !1PIDN:AAC73472.1; PID:g1786566; UWGP:b0369 !'##experimental_source strain K-12, substrain MG1655 REFERENCE JS0127 !$#authors Li, J.M.; Russell, C.S.; Cosloy, S.D. !$#journal Gene (1989) 75:177-184 !$#title The structure of the Escherichia coli hemB gene. !$#cross-references MUID:89252914; PMID:2656410 !$#accession JS0127 !'##molecule_type DNA !'##residues 'MPLDSTNIRQT',1-17,'PR',20-89,'ER',92-103,'P',105-226,'A', !1228,'G',230,'A',232,'Y',234-240,'P',242-253,'N',255-324 !1##label LIJ !'##cross-references GB:M24488; NID:g341174; PIDN:AAA62629.1; !1PID:g450371 !'##note the authors translated the codon GAG for residue 90 as Ser and !1CGA for residue 91 as Asp REFERENCE S10100 !$#authors Echelard, Y.; Dymetryszyn, J.; Drolet, M.; Sasarman, A. !$#journal Mol. Gen. Genet. (1988) 214:503-508 !$#title Nucleotide sequence of the hemB gene of Escherichia coli !1K12. !$#cross-references MUID:89112158; PMID:2464127 !$#accession S10100 !'##molecule_type DNA !'##residues 1-18,'VCLKRQH',26,'A',28,'TTWCCRSLLKKKLT',43-225,'P', !1227-324 ##label ECH !'##cross-references EMBL:X17417; NID:g41661; PIDN:CAA35467.1; !1PID:g41662 !'##experimental_source strain K12 REFERENCE S29771 !$#authors Spencer, P.; Jordan, P.M. !$#journal Biochem. J. (1993) 290:279-287 !$#title Purification and characterization of 5-aminolaevulinic acid !1dehydratase from Escherichia coli and a study of the !1reactive thiols at the metal-binding domain. !$#cross-references MUID:93176130; PMID:8439296 !$#accession S29771 !'##molecule_type protein !'##residues 2-6;96-135;238-254 ##label SPE REFERENCE S78608 !$#authors Nashimoto, H.; Saito, N. !$#submission submitted to the EMBL Data Library, May 1996 !$#description Kohara library:8F10. !$#accession S78616 !'##molecule_type DNA !'##residues 'MPLDSTNIRQT',1-324 ##label NAS !'##cross-references EMBL:D85613 !'##experimental_source strain K12 GENETICS !$#gene hemB !$#map_position 8 min COMPLEX homooctamer [validated, MUID:93176130] FUNCTION !$#description catalyzes the condensation of two molecules of !15-aminolevulinic acid to form monopyrrole porphobilinogen !1[validated, MUID:93176130] !$#pathway tetrapyrrole biosynthesis !$#note cofactor zinc !$#note dehydratases utilizing Zn(2+) are found to be oxygen !1sensitive [validated, MUID:97185725] CLASSIFICATION #superfamily porphobilinogen synthase KEYWORDS carbon-oxygen lyase; hydro-lyase; porphyrin biosynthesis; !1zinc FEATURE !$2-324 #product porphobilinogen synthase ALAD #status !8experimental #label MAT\ !$118-133 #region zinc binding #status predicted\ !$247 #active_site Lys #status predicted SUMMARY #length 324 #molecular-weight 35624 #checksum 8025 SEQUENCE /// ENTRY A49925 #type complete TITLE delta-aminolevulinic acid dehydratase - Bradyrhizobium japonicum ORGANISM #formal_name Bradyrhizobium japonicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A49925 REFERENCE A49925 !$#authors Chauhan, S.; O'Brian, M.R. !$#journal J. Bacteriol. (1993) 175:7222-7227 !$#title Bradyrhizobium japonicum delta-aminolevulinic acid !1dehydratase is essential for symbiosis with soybean and !1contains a novel metal-binding domain. !$#cross-references MUID:94042895; PMID:8226669 !$#accession A49925 !'##status preliminary !'##molecule_type DNA !'##residues 1-353 ##label CHA !'##cross-references GB:L24386; NID:g416154; PIDN:AAA89067.1; !1PID:g416155 GENETICS !$#gene hemB CLASSIFICATION #superfamily porphobilinogen synthase KEYWORDS heme biosynthesis; magnesium SUMMARY #length 353 #molecular-weight 38582 #checksum 9429 SEQUENCE /// ENTRY JC1286 #type complete TITLE porphobilinogen synthase (EC 4.2.1.24) - Methanothermus sociabilis ALTERNATE_NAMES 5-aminolevulinic acid dehydratase ORGANISM #formal_name Methanothermus sociabilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JC1286 REFERENCE JC1286 !$#authors Broecbl, G.; Berchtold, M.; Koenig, H. !$#journal Gene (1992) 119:151-152 !$#title Sequence of the 5-aminolevulinic acid dehydratase-encoding !1gene from the hyperthermophilic methanogen, Methanothermus !1sociabilis. !$#cross-references MUID:93012970; PMID:1398086 !$#accession JC1286 !'##molecule_type DNA !'##residues 1-320 ##label BRO !'##cross-references GB:M90083; NID:g149787; PIDN:AAA73226.1; !1PID:g149788 GENETICS !$#gene aladh CLASSIFICATION #superfamily porphobilinogen synthase KEYWORDS carbon-oxygen lyase; hydro-lyase SUMMARY #length 320 #molecular-weight 35924 #checksum 9440 SEQUENCE /// ENTRY C42728 #type complete TITLE porphobilinogen synthase (EC 4.2.1.24) hemB - Bacillus subtilis ALTERNATE_NAMES delta-aminolevulinic acid dehydratase hemB ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS C42728; D69639 REFERENCE A42728 !$#authors Hansson, M.; Rutberg, L.; Schroeder, I.; Hederstedt, L. !$#journal J. Bacteriol. (1991) 173:2590-2599 !$#title The Bacillus subtilis hemAXCDBL gene cluster, which encodes !1enzymes of the biosynthetic pathway from glutamate to !1uroporphyrinogen III. !$#cross-references MUID:91193218; PMID:1672867 !$#accession C42728 !'##molecule_type DNA !'##residues 1-324 ##label HAN !'##cross-references GB:M57676; NID:g143034; PIDN:AAA22514.1; !1PID:g143039 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D69639 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-324 ##label KUN !'##cross-references GB:Z99118; GB:AL009126; NID:g2635200; !1PIDN:CAB14773.1; PID:g2635278 !'##experimental_source strain 168 GENETICS !$#gene hemB CLASSIFICATION #superfamily porphobilinogen synthase KEYWORDS carbon-oxygen lyase; hydro-lyase SUMMARY #length 324 #molecular-weight 36209 #checksum 3782 SEQUENCE /// ENTRY S03187 #type complete TITLE porphobilinogen synthase (EC 4.2.1.24) - mouse ALTERNATE_NAMES delta-aminolevulinate dehydratase ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S03187 REFERENCE S03187 !$#authors Bishop, T.R.; Hodes, Z.I.; Frelin, L.P.; Boyer, S.H. !$#journal Nucleic Acids Res. (1989) 17:1775 !$#title Cloning and sequence of mouse erythroid !1delta-aminolevulinate dehydratase cDNA. !$#cross-references MUID:89160346; PMID:2922298 !$#accession S03187 !'##molecule_type mRNA !'##residues 1-330 ##label BIS !'##cross-references EMBL:X13752; NID:g52951; PIDN:CAA32015.1; !1PID:g52952 CLASSIFICATION #superfamily porphobilinogen synthase KEYWORDS carbon-oxygen lyase; hydro-lyase; porphyrin biosynthesis SUMMARY #length 330 #molecular-weight 36023 #checksum 7200 SEQUENCE /// ENTRY A24724 #type complete TITLE porphobilinogen synthase (EC 4.2.1.24) - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A24724 REFERENCE A24724 !$#authors Bishop, T.R.; Frelin, L.P.; Boyer, S.H. !$#journal Nucleic Acids Res. (1986) 14:10115 !$#title Nucleotide sequence of rat liver delta-aminolevulinic acid !1dehydratase cDNA. !$#cross-references MUID:87117513; PMID:3808948 !$#accession A24724 !'##molecule_type mRNA !'##residues 1-330 ##label BIS !'##cross-references GB:X04959; GB:M14479; NID:g55625; PIDN:CAA28621.1; !1PID:g55626 CLASSIFICATION #superfamily porphobilinogen synthase KEYWORDS carbon-oxygen lyase; hydro-lyase; porphyrin biosynthesis SUMMARY #length 330 #molecular-weight 36031 #checksum 7563 SEQUENCE /// ENTRY A26478 #type complete TITLE porphobilinogen synthase (EC 4.2.1.24) - human ALTERNATE_NAMES delta-aminolevulinate dehydratase ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 18-Jun-1999 ACCESSIONS A26478; I55569; I70288 REFERENCE A26478 !$#authors Wetmur, J.G.; Bishop, D.F.; Cantelmo, C.; Desnick, R.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:7703-7707 !$#title Human delta-aminolevulinate dehydratase: nucleotide sequence !1of a full-length cDNA clone. !$#cross-references MUID:87017017; PMID:3463993 !$#accession A26478 !'##molecule_type mRNA !'##residues 1-330 ##label WET !'##cross-references GB:M13928; NID:g178328; PIDN:AAA51687.1; !1PID:g178329 REFERENCE I55569 !$#authors Ishida, N.; Fujita, H.; Fukuda, Y.; Noguchi, T.; Doss, M.; !1Kappas, A.; Sassa, S. !$#journal J. Clin. Invest. (1992) 89:1431-1437 !$#title Cloning and expression of the defective genes from a patient !1with delta-aminolevulinate dehydratase porphyria. !$#cross-references MUID:92235256; PMID:1569184 !$#accession I55569 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-239,'W',241-330 ##label ISH1 !'##cross-references GB:S99468; NID:g248838; PIDN:AAC60581.1; !1PID:g248839 !'##experimental_source mutant allele G1 !$#accession I70288 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-273,'T',275-330 ##label ISH2 !'##cross-references GB:S99471; NID:g248840; PIDN:AAC60582.1; !1PID:g248841 !'##experimental_source mutant allele G2 GENETICS !$#gene GDB:ALAD !'##cross-references GDB:119665; OMIM:125270 !$#map_position 9q32-9q34 !$#note defects in this gene can result in acute hepatic porphyria COMPLEX homooctamer FUNCTION !$#description catalyzes the condensation of 2 molecules of !15-aminolevulinic acid to produce porphobilinogen and 2 water !1molecules !$#pathway porphyrin biosynthesis CLASSIFICATION #superfamily porphobilinogen synthase KEYWORDS carbon-oxygen lyase; homooctamer; hydro-lyase; porphyrin !1biosynthesis; zinc FEATURE !$122-132 #region zinc binding #status predicted\ !$252 #active_site Lys #status predicted SUMMARY #length 330 #molecular-weight 36294 #checksum 5574 SEQUENCE /// ENTRY S64042 #type complete TITLE porphobilinogen synthase (EC 4.2.1.24) ALAD [validated] - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES aminolevulinate dehydratase; protein G3610; protein YGL040c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S64042; S64044; A28465 REFERENCE S64003 !$#authors Hebling, U.; Hofmann, B.; Delius, H. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64042 !'##molecule_type DNA !'##residues 1-342 ##label HEB !'##cross-references EMBL:Z72562; NID:g1322523; PIDN:CAA96742.1; !1PID:g1322524; GSPDB:GN00007; MIPS:YGL040c !'##experimental_source strain S288C REFERENCE S64044 !$#authors Feuermann, M.; Potier, S.; Souciet, J.L. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64044 !'##molecule_type DNA !'##residues 41-342 ##label FEU !'##cross-references EMBL:Z72562; GSPDB:GN00007; MIPS:YGL040c !'##experimental_source strain S288C REFERENCE A28465 !$#authors Myers, A.M.; Crivellone, M.D.; Koerner, T.J.; Tzagoloff, A. !$#journal J. Biol. Chem. (1987) 262:16822-16829 !$#title Characterization of the yeast HEM2 gene and transcriptional !1regulation of COX5 and COR1 by heme. !$#cross-references MUID:88059078; PMID:2445751 !$#accession A28465 !'##molecule_type DNA !'##residues 1-290,'D',292-342 ##label MYE !'##cross-references EMBL:J03493; NID:g171663; PIDN:AAA34669.1; !1PID:g171664 GENETICS !$#gene SGD:HEM2; MIPS:YGL040c !'##cross-references SGD:S0003008; MIPS:YGL040c !$#map_position 7L COMPLEX homooctamer [validated, MUID:97406919] FUNCTION !$#description catalyzes the condensation of two molecules of !15-aminolevulinic acid to form monopyrrole porphobilinogen !1[validated, MUID:97129006] !$#pathway tetrapyrrole biosynthesis !$#note cofactor zinc !$#note dehydratases utilizing Zn(2+) are found to be oxygen !1sensitive [validated, MUID:97185725] CLASSIFICATION #superfamily porphobilinogen synthase KEYWORDS carbon-oxygen lyase; hydro-lyase; porphyrin biosynthesis; !1zinc SUMMARY #length 342 #molecular-weight 37740 #checksum 6043 SEQUENCE /// ENTRY A47010 #type complete TITLE 4a-hydroxytetrahydrobiopterin dehydratase (EC 4.2.1.96) [validated] - human ALTERNATE_NAMES 4-alpha-hydroxy-tetrahydropterin dehydratase; dimerization cofactor of hepatocyte nuclear factor 1-alpha; homeodomain protein transregulator; phenylalanine hydroxylase-stimulating protein PHS/PCD; pterin-4-alpha-carbinolamine dehydratase ORGANISM #formal_name Homo sapiens #common_name man DATE 16-Feb-1994 #sequence_revision 18-Nov-1994 #text_change 01-Sep-2000 ACCESSIONS A47010; A45424; S66249 REFERENCE A47010 !$#authors Citron, B.A.; Kaufman, S.; Milstien, S.; Naylor, E.W.; !1Greene, C.L.; Davis, M.D. !$#journal Am. J. Hum. Genet. (1993) 53:768-774 !$#title Mutation in the 4a-carbinolamine dehydratase gene leads to !1mild hyperphenylalaninemia with defective cofactor !1metabolism. !$#cross-references MUID:93356171; PMID:8352282 !$#accession A47010 !'##molecule_type DNA !'##residues 1-104 ##label CIT !'##cross-references GB:L15428; NID:g348906; PIDN:AAA35672.1; !1PID:g348907 !'##experimental_source tissue blood; cell-type leukocyte !'##note sequence extracted from NCBI backbone (NCBIN:136506, !1NCBIP:136507) REFERENCE A45424 !$#authors Hauer, C.R.; Rebrin, I.; Thony, B.; Neuheiser, F.; Curtius, !1H.C.; Hunziker, P.; Blau, N.; Ghisla, S.; Heizmann, C.W. !$#journal J. Biol. Chem. (1993) 268:4828-4831 !$#title Phenylalanine hydroxylase-stimulating protein/pterin-4 !1alpha-carbinolamine dehydratase from rat and human liver. !1Purification, characterization, and complete amino acid !1sequence. !$#cross-references MUID:93186787; PMID:8444860 !$#accession A45424 !'##molecule_type protein !'##residues 2-81,'C',83-104 ##label HAU !'##experimental_source liver !'##note sequence extracted from NCBI backbone (NCBIP:126605) !'##note the rat sequence was determined also and was found to be !1identical !'##note the blocked amino end was the only observed covalent !1modification REFERENCE S66249 !$#authors Koester, S.; Thoeny, B.; Macheroux, P.; Curtius, H.C.; !1Heizmann, C.W.; Pfleiderer, W.; Ghisla, S. !$#journal Eur. J. Biochem. (1995) 231:414-423 !$#title Human pterin-4-alpha-carbinolamine dehydratase/dimerization !1cofactor of hepatocyte nuclear factor-1-alpha. !1Characterization and kinetic analysis of wild-type and !1mutant enzymes. !$#cross-references MUID:95361865; PMID:7635153 !$#accession S66249 !'##molecule_type protein !'##residues 2-6 ##label KOE COMMENT This protein was observed as a tetramer as the cytosolic !1enzyme pterin-4-alpha-carbinolamine dehydratase but observed !1as a dimer as the nuclear protein dimerization cofactor of !1hepatocyte nuclear factor 1-alpha (DCoH). GENETICS !$#gene GDB:PCBD; DCOH; PCD !'##cross-references GDB:138478; OMIM:126090 !$#map_position 10q22-10q22 FUNCTION CYT !$#description accelerates the formation of quinonoid-BH2 from !14alpha-hydroxytetrahydropterin and therefore minimizes !1non-enzymatic chemical rearrangement to anomalous !17-substituted pterins FUNCTION NUC !$#description regulates the dimerization of a nuclear homeobox protein !1involved in transcription CLASSIFICATION #superfamily 4a-hydroxytetrahydrobiopterin dehydratase KEYWORDS acetylated amino end; carbon-oxygen lyase; cytosol; !1homodimer; homotetramer; hydro-lyase; nucleus FEATURE !$2-104 #product 4a-hydroxytetrahydrobiopterin dehydratase !8#status experimental #label MAT\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental SUMMARY #length 104 #molecular-weight 12053 #checksum 9232 SEQUENCE /// ENTRY A47189 #type complete TITLE 4a-hydroxytetrahydrobiopterin dehydratase (EC 4.2.1.96) [validated] - rat ALTERNATE_NAMES 4-alpha-hydroxy-tetrahydropterin dehydratase; dimerization cofactor of hepatocyte nuclear factor 1-alpha (DCoH); homeodomain protein transregulator; phenylalanine hydroxylase-stimulating protein PHS/PCD; pterin-4-alpha-carbinolamine dehydratase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 21-Sep-1993 #sequence_revision 18-Nov-1994 #text_change 28-Jul-2000 ACCESSIONS A47189 REFERENCE A47189 !$#authors Citron, B.A.; Davis, M.D.; Milstien, S.; Gutierrez, J.; !1Mendel, D.B.; Crabtree, G.R.; Kaufman, S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:11891-11894 !$#title Identity of 4a-carbinolamine dehydratase, a component of the !1phenylalanine hydroxylation system, and DCoH, a !1transregulator of homeodomain proteins. !$#cross-references MUID:93101632; PMID:1465414 !$#accession A47189 !'##molecule_type mRNA; protein !'##residues 1-104 ##label CIT !'##experimental_source liver !'##note sequence extracted from NCBI backbone (NCBIN:120668, !1NCBIP:120669) REFERENCE A45424 !$#authors Hauer, C.R.; Rebrin, I.; Thony, B.; Neuheiser, F.; Curtius, !1H.C.; Hunziker, P.; Blau, N.; Ghisla, S.; Heizmann, C.W. !$#journal J. Biol. Chem. (1993) 268:4828-4831 !$#title Phenylalanine hydroxylase-stimulating protein/pterin-4 !1alpha-carbinolamine dehydratase from rat and human liver. !1Purification, characterization, and complete amino acid !1sequence. !$#cross-references MUID:93186787; PMID:8444860 !$#contents annotation COMMENT This protein was observed as a tetramer as the cytosolic !1enzyme pterin-4-alpha-carbinolamine dehydratase but observed !1as a dimer as the nuclear protein dimerization cofactor of !1hepatocyte nuclear factor 1-alpha (DCoH). FUNCTION CYT !$#description accelerates the formation of quinonoid-BH2 from !14alpha-hydroxytetrahydropterin and therefore minimizes !1non-enzymatic chemical rearrangement to anomalous !17-substituted pterins FUNCTION NUC !$#description regulates the dimerization of a nuclear homeobox protein !1involved in transcription CLASSIFICATION #superfamily 4a-hydroxytetrahydrobiopterin dehydratase KEYWORDS acetylated amino end; carbon-oxygen lyase; cytosol; !1homodimer; homotetramer; hydro-lyase; nucleus FEATURE !$2-104 #product pterin-4-alpha-carbinolamine dehydratase !8#status experimental #label MAT\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental SUMMARY #length 104 #molecular-weight 12000 #checksum 8857 SEQUENCE /// ENTRY I51697 #type complete TITLE 4a-hydroxytetrahydrobiopterin dehydratase (EC 4.2.1.96) [similarity] - African clawed frog ALTERNATE_NAMES 4-alpha-hydroxy-tetrahydropterin dehydratase; dimerization cofactor of hepatocyte nuclear factor 1-alpha XDCoH; homeodomain protein transregulator; phenylalanine hydroxylase-stimulating protein PHS/PCD; pterin-4-alpha-carbinolamine dehydratase ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 13-Sep-1996 #sequence_revision 13-Sep-1996 #text_change 28-Jul-2000 ACCESSIONS I51697 REFERENCE I51697 !$#authors Pogge yon Strandmann, E.; Ryffel, G.U. !$#journal Development (1995) 121:1217-1226 !$#title Developmental expression of the maternal protein XDCoH, the !1dimerization cofactor of the homeoprotein LFB1 (HNF1). !$#cross-references MUID:95262566; PMID:7743933 !$#accession I51697 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-104 ##label POG !'##cross-references EMBL:Z37525; NID:g854636; PIDN:CAA85762.1; !1PID:g854637 COMMENT The orthologous protein in rat was observed as a tetramer as !1the cytosolic enzyme pterin-4-alpha-carbinolamine !1dehydratase but observed as a dimer as the nuclear protein !1dimerization cofactor of hepatocyte nuclear factor 1-alpha !1(DCoH). GENETICS !$#gene XDCOH FUNCTION CYT !$#description accelerates the formation of quinonoid-BH2 from !14alpha-hydroxytetrahydropterin and therefore minimizes !1non-enzymatic chemical rearrangement to anomalous !17-substituted pterins FUNCTION NUC !$#description cofactor for the transcription factor LFB1 (HNF1) CLASSIFICATION #superfamily 4a-hydroxytetrahydrobiopterin dehydratase KEYWORDS acetylated amino end; carbon-oxygen lyase; cytosol; !1homodimer; homotetramer; hydro-lyase; nucleus SUMMARY #length 104 #molecular-weight 11920 #checksum 6731 SEQUENCE /// ENTRY S46832 #type complete TITLE probable 4a-hydroxytetrahydrobiopterin dehydratase (EC 4.2.1.96) YHL018w [similarity] - yeast (Saccharomyces cerevisiae) ORGANISM #formal_name Saccharomyces cerevisiae DATE 28-Oct-1994 #sequence_revision 28-Oct-1994 #text_change 19-Apr-2002 ACCESSIONS S46832 REFERENCE S46796 !$#authors Favello, T. !$#submission submitted to the EMBL Data Library, June 1994 !$#description The sequence of S. cerevisiae cosmid 9433. !$#accession S46832 !'##molecule_type DNA !'##residues 1-120 ##label FAV !'##cross-references EMBL:U11582; NID:g2289793; PID:g508754; !1GSPDB:GN00008; MIPS:YHL018w GENETICS !$#gene MIPS:YHL018w !'##cross-references SGD:S0001010 !$#map_position 8L CLASSIFICATION #superfamily 4a-hydroxytetrahydrobiopterin dehydratase KEYWORDS carbon-oxygen lyase; hydro-lyase SUMMARY #length 120 #molecular-weight 14026 #checksum 5168 SEQUENCE /// ENTRY A44153 #type complete TITLE aconitate hydratase (EC 4.2.1.3) - rabbit ALTERNATE_NAMES aconitase; ferritin mRNA repressor protein; iron-responsive element-binding protein ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A44153; S47664; S47665 REFERENCE A44153 !$#authors Patino, M.M.; Walden, W.E. !$#journal J. Biol. Chem. (1992) 267:19011-19016 !$#title Cloning of a functional cDNA for the rabbit ferritin mRNA !1repressor protein. Demonstration of a tissue-specific !1pattern of expression. !$#cross-references MUID:92406828; PMID:1527028 !$#accession A44153 !'##molecule_type mRNA; protein !'##residues 1-889 ##label PAT !'##cross-references EMBL:M95815; NID:g165029; PIDN:AAA31255.1; !1PID:g165030 !'##experimental_source liver !'##note sequence extracted from NCBI backbone (NCBIN:113547, !1NCBIP:113546) REFERENCE S47664 !$#authors Swenson, G.R.; Walden, W.E. !$#journal Nucleic Acids Res. (1994) 22:2627-2633 !$#title Localization of an RNA binding element of the iron !1responsive element binding protein within a proteolytic !1fragment containing iron coordination ligands. !$#cross-references MUID:94316507; PMID:7518918 !$#accession S47664 !'##molecule_type protein !'##residues 133,'X',135-146 ##label SWE !$#accession S47665 !'##molecule_type protein !'##residues 624-635,'X',637-638 ##label SWW GENETICS !$#gene FRP CLASSIFICATION #superfamily iron-responsive element-binding protein KEYWORDS 4Fe-4S; carbon-oxygen lyase; hydro-lyase; iron-sulfur !1protein; metalloprotein; RNA binding FEATURE !$480-623 #domain RNA binding #status predicted #label RNA\ !$125,126,178,205, !$207,302,778 #active_site Asp, His, His, Asp, His, Glu, Ser !8#status predicted\ !$437,503,506 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 889 #molecular-weight 98504 #checksum 6807 SEQUENCE /// ENTRY S61067 #type complete TITLE homoaconitate hydratase (EC 4.2.1.36) precursor - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YD8419.01; protein YD9934.18; protein YDR234w ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S61067; S54530; S59440 REFERENCE S61067 !$#authors Gamonet, F.; Lauquin, J.M. !$#submission submitted to the EMBL Data Library, November 1995 !$#accession S61067 !'##molecule_type DNA !'##residues 1-693 ##label GAM !'##cross-references EMBL:X93502; NID:g1089839; PIDN:CAA63764.1; !1PID:g1089840 !'##experimental_source strain GRF88 REFERENCE S54530 !$#authors Oliver, K.; Harris, D. !$#submission submitted to the EMBL Data Library, May 1995 !$#accession S54530 !'##molecule_type DNA !'##residues 319-693 ##label OLI !'##cross-references EMBL:Z49701; NID:g817819; PIDN:CAA89720.1; !1PID:g817820; GSPDB:GN00004; MIPS:YDR234w !'##experimental_source strain AB972 REFERENCE S59423 !$#authors Murphy, L.; Harris, D. !$#submission submitted to the EMBL Data Library, March 1995 !$#accession S59440 !'##molecule_type DNA !'##residues 1-324 ##label MUR !'##cross-references EMBL:Z48612; NID:g728671; PIDN:CAA88513.1; !1PID:g728689; GSPDB:GN00004; MIPS:YDR234w !'##experimental_source strain AB972 GENETICS !$#gene SGD:LYS4; MIPS:YDR234w !'##cross-references SGD:S0002642; MIPS:YDR234w !$#map_position 4R CLASSIFICATION #superfamily homoaconitate hydratase KEYWORDS carbon-oxygen lyase; hydro-lyase SUMMARY #length 693 #molecular-weight 75150 #checksum 7444 SEQUENCE /// ENTRY QQECRT #type complete TITLE L(+)-tartrate dehydratase (EC 4.2.1.32), iron-dependent, alpha chain - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS C65094; I55714; A29049 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65094 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-303 ##label BLAT !'##cross-references GB:AE000388; GB:U00096; NID:g1789441; !1PIDN:AAC76097.1; PID:g1789442; UWGP:b3061 !'##experimental_source strain K-12, substrain MG1655 REFERENCE I55714 !$#authors Reaney, S.K.; Begg, C.; Bungard, S.; Guest, J.R. !$#journal J. Gen. Microbiol. (1993) 139:1523-1530 !$#title Identification of the L-tartrate dehydratase genes (ttdA and !1ttdB) of Escherichia coli and evolutionary relationship with !1the class I fumarase genes. !$#cross-references MUID:93381464; PMID:8371115 !$#accession I55714 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-10,'L',12-230,'DV',233-303 ##label RES !'##cross-references GB:L14781; NID:g347083; PIDN:AAA03061.1; !1PID:g347084 REFERENCE A91573 !$#authors Nesin, M.; Lupski, J.R.; Svec, P.; Godson, G.N. !$#journal Gene (1987) 51:149-161 !$#title Possible new genes as revealed by molecular analysis of a !15-kb Escherichia coli chromosomal region 5' to the !1rpsU-dnaG-rpoD macromolecular-synthesis operon. !$#cross-references MUID:87248073; PMID:3297921 !$#accession A29049 !'##molecule_type DNA !'##residues 2-10,'L',12-197,'ASHLG',204-219, !1'RPPSQSKSGRTGRTPGRRTQPSGDWSTRADRQQFSDGRTYRICRPPSVNHRRCCLYRLL !1GAS',220-222,'AAGSCRSHL' ##label NES !'##cross-references GB:M16194; GB:X00773; NID:g147764; PIDN:AAA72573.1; !1PID:g147765 GENETICS !$#gene ttdA !$#map_position 67 min COMPLEX a tetramer containing two pairs of non-identical chains, the !1alpha and beta CLASSIFICATION #superfamily iron-dependent tartrate dehydratase alpha !1chain; iron-dependent tartrate dehydratase alpha chain !1homology KEYWORDS 4Fe-4S; carbon-oxygen lyase; hydro-lyase; iron-sulfur !1protein; metalloprotein FEATURE !$59-259 #domain iron-dependent tartrate dehydratase alpha !8chain homology #label TTDA\ !$71,190,277 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 303 #molecular-weight 32733 #checksum 2752 SEQUENCE /// ENTRY E64461 #type complete TITLE fumarate hydratase (EC 4.2.1.2), class I ' - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E64461 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession E64461 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-285 ##label BUL !'##cross-references GB:U67570; GB:L77117; NID:g2826392; !1PIDN:AAB99301.1; PID:g1591932; TIGR:MJ1294 GENETICS !$#map_position REV1242836-1241979 CLASSIFICATION #superfamily iron-dependent tartrate dehydratase alpha !1chain; iron-dependent tartrate dehydratase alpha chain !1homology KEYWORDS carbon-oxygen lyase; hydro-lyase FEATURE !$48-251 #domain iron-dependent tartrate dehydratase alpha !8chain homology #label TTDA SUMMARY #length 285 #molecular-weight 31088 #checksum 7087 SEQUENCE /// ENTRY G64106 #type complete TITLE 3-isopropylmalate dehydratase (EC 4.2.1.33) small chain - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS G64106 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession G64106 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-200 ##label TIGR !'##cross-references GB:U32779; GB:L42023; NID:g1574009; !1PIDN:AAC22650.1; PID:g1574018; TIGR:HI0989 GENETICS !$#gene leuD FUNCTION !$#pathway leucine biosynthesis CLASSIFICATION #superfamily 3-isopropylmalate dehydratase small chain KEYWORDS carbon-oxygen lyase; hydro-lyase; leucine biosynthesis SUMMARY #length 200 #molecular-weight 22812 #checksum 7742 SEQUENCE /// ENTRY QQECRZ #type complete TITLE L(+)-tartrate dehydratase (EC 4.2.1.32), iron-dependent, beta chain - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS D65094; I70799; B29049 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65094 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-201 ##label BLAT !'##cross-references GB:AE000388; GB:U00096; NID:g1789441; !1PIDN:AAC76098.1; PID:g1789443; UWGP:b3062 !'##experimental_source strain K-12, substrain MG1655 REFERENCE I55714 !$#authors Reaney, S.K.; Begg, C.; Bungard, S.; Guest, J.R. !$#journal J. Gen. Microbiol. (1993) 139:1523-1530 !$#title Identification of the L-tartrate dehydratase genes (ttdA and !1ttdB) of Escherichia coli and evolutionary relationship with !1the class I fumarase genes. !$#cross-references MUID:93381464; PMID:8371115 !$#accession I70799 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-79,'QYAYGK',86-164,'A',166-201 ##label RES !'##cross-references GB:L14781; NID:g347083; PIDN:AAA03062.1; !1PID:g347085 REFERENCE A91573 !$#authors Nesin, M.; Lupski, J.R.; Svec, P.; Godson, G.N. !$#journal Gene (1987) 51:149-161 !$#title Possible new genes as revealed by molecular analysis of a !15-kb Escherichia coli chromosomal region 5' to the !1rpsU-dnaG-rpoD macromolecular-synthesis operon. !$#cross-references MUID:87248073; PMID:3297921 !$#accession B29049 !'##molecule_type DNA !'##residues 1-79,'QYAYGK',86-164,'A',166-201 ##label NES !'##cross-references GB:M16194; GB:X00773; NID:g147764; PIDN:AAA72574.1; !1PID:g147766 GENETICS !$#gene ttdB !$#map_position 67 min COMPLEX a tetramer containing two pairs of non-identical chains, the !1alpha and beta FUNCTION !$#description catalyzes the stereospecific interconversion of oxaloacetate !1and (R,R)-tartrate; it is an Fe-dependent 4Fe-4S, class I !1hydratase; it exists in an inactive low-molacular form, !1converted into active enzyme in the presence of ferrous ion !1and thiol CLASSIFICATION #superfamily iron-dependent tartrate dehydratase beta chain; !1iron-dependent tartrate dehydratase beta chain homology KEYWORDS carbon-oxygen lyase; hydro-lyase FEATURE !$13-177 #domain iron-dependent tartrate dehydratase beta !8chain homology #label TTDB SUMMARY #length 201 #molecular-weight 22679 #checksum 1713 SEQUENCE /// ENTRY S27617 #type complete TITLE glucarate dehydratase (EC 4.2.1.40) - Pseudomonas putida ORGANISM #formal_name Pseudomonas putida DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S27617 REFERENCE S27612 !$#authors Burlingame, R.P.; Maruya, A.; Ally, A.; Ally, D.; Backman, !1K.C. !$#submission submitted to the EMBL Data Library, June 1992 !$#description Nucleotide sequences of hydroxyproline-specific !1alpha-ketoglutarate semialdehyde dehydrogenase genes from !1two strains of pseudomonas putida. !$#accession S27617 !'##status preliminary !'##molecule_type DNA !'##residues 1-451 ##label BUR !'##cross-references EMBL:M69160; NID:g151313; PIDN:AAA25868.1; !1PID:g151315 CLASSIFICATION #superfamily glucarate dehydratase KEYWORDS carbon-oxygen lyase; hydro-lyase SUMMARY #length 451 #molecular-weight 49572 #checksum 2472 SEQUENCE /// ENTRY A69753 #type complete TITLE glucarate dehydratase (EC 4.2.1.40) - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A69753 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69753 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-455 ##label KUN !'##cross-references GB:Z99105; GB:AL009126; NID:g2632457; !1PIDN:CAB12043.1; PID:g2632535 !'##experimental_source strain 168 GENETICS !$#gene ycbF CLASSIFICATION #superfamily glucarate dehydratase KEYWORDS carbon-oxygen lyase; hydro-lyase SUMMARY #length 455 #molecular-weight 50782 #checksum 7362 SEQUENCE /// ENTRY DWPSUP #type complete TITLE urocanate hydratase (EC 4.2.1.49) [validated] - Pseudomonas putida ALTERNATE_NAMES urocanase ORGANISM #formal_name Pseudomonas putida DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 20-Apr-2000 ACCESSIONS S17184; S18848 REFERENCE S17184 !$#authors Fessenmaier, M.; Frank, R.; Retey, J.; Schubert, C. !$#journal FEBS Lett. (1991) 286:55-57 !$#title Cloning and sequencing the urocanase gene (hutU) from !1Pseudomonas putida. !$#cross-references MUID:91323532; PMID:1677899 !$#accession S17184 !'##molecule_type DNA !'##residues 1-557 ##label FES !'##cross-references EMBL:X58483; NID:g45695; PIDN:CAA41392.1; !1PID:g581461 !$#accession S18848 !'##molecule_type protein !'##residues 2-22 ##label FES1 GENETICS !$#gene hutU !$#start_codon GTG COMPLEX homodimer FUNCTION !$#description EC 4.2.1.49 [validated, MUID:94039067] !$#note non-covalent but tight binding of cofactor NAD+ to the !1enzyme by 'trapping' the cofactor while folding to the !1nascent protein CLASSIFICATION #superfamily urocanate hydratase KEYWORDS carbon-oxygen lyase; homodimer; hydro-lyase FEATURE !$2-557 #product urocanate hydratase #status experimental !8#label MAT SUMMARY #length 557 #molecular-weight 60803 #checksum 4732 SEQUENCE /// ENTRY C32804 #type complete TITLE prephenate dehydratase (EC 4.2.1.51) - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 20-Oct-1989 #sequence_revision 06-Feb-1995 #text_change 20-Jan-2003 ACCESSIONS C32804; F69675 REFERENCE A32804 !$#authors Trach, K.; Hoch, J.A. !$#journal J. Bacteriol. (1989) 171:1362-1371 !$#title The Bacillus subtilis spo0B stage 0 sporulation operon !1encodes an essential GTP-binding protein. !$#cross-references MUID:89155435; PMID:2537815 !$#accession C32804 !'##molecule_type DNA !'##residues 1-285 ##label TRA !'##cross-references GB:M24537; NID:g341195; PIDN:AAA22507.1; !1PID:g508981 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69675 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-285 ##label KUN !'##cross-references GB:Z99118; GB:AL009126; NID:g2635200; !1PIDN:CAB14750.1; PID:g2635255 !'##experimental_source strain 168 GENETICS !$#gene pheA CLASSIFICATION #superfamily Prephenate dehydratase; prephenate dehydratase !1homology KEYWORDS carbon-oxygen lyase; hydro-lyase; phenylalanine biosynthesis FEATURE !$1-285 #domain prephenate dehydratase homology #label PPW SUMMARY #length 285 #molecular-weight 31901 #checksum 4809 SEQUENCE /// ENTRY DWECHD #type complete TITLE 3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase (EC 4.2.1.60) - Escherichia coli (strain K-12) ALTERNATE_NAMES beta-hydroxydecanoyl thiolester dehydrase ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 21-Nov-1997 #text_change 01-Mar-2002 ACCESSIONS A64836; A28140 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64836 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-172 ##label BLAT !'##cross-references GB:AE000197; GB:U00096; NID:g1787180; !1PIDN:AAC74040.1; PID:g1787187; UWGP:b0954 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A28140 !$#authors Cronan Jr., J.E.; Li, W.B.; Coleman, R.; Narasimhan, M.; de !1Mendoza, D.; Schwab, J.M. !$#journal J. Biol. Chem. (1988) 263:4641-4646 !$#title Derived amino acid sequence and identification of active !1site residues of Escherichia coli beta-hydroxydecanoyl !1thioester dehydrase. !$#cross-references MUID:88169574; PMID:2832401 !$#accession A28140 !'##molecule_type DNA !'##residues 1-169,'LF' ##label CRO GENETICS !$#gene fabA !$#map_position 22 min FUNCTION !$#description catalyzes two reversible reactions, the dehydration of !1(R)-3-hydroxydecanoyl-ACP to (E)-2-decenoyl-ACP and the !1isomerization of (E)-2-decenoyl-ACP to (Z)-3-decenoyl-ACP !$#pathway unsaturated fatty acid biosynthesis CLASSIFICATION #superfamily 3-hydroxydecanoyl-[acyl-carrier-protein] !1dehydratase KEYWORDS carbon-oxygen lyase; fatty acid biosynthesis; homodimer; !1hydro-lyase FEATURE !$70 #active_site Cys #status predicted\ !$71 #active_site His #status experimental SUMMARY #length 172 #molecular-weight 18969 #checksum 4812 SEQUENCE /// ENTRY S04472 #type complete TITLE nitrile hydratase (EC 4.2.1.84) alpha chain [validated] - Rhodococcus sp. ORGANISM #formal_name Rhodococcus sp. DATE 21-Nov-1998 #sequence_revision 21-Nov-1998 #text_change 23-Mar-2001 ACCESSIONS S04472; A30463; S16606; S02070; S54105; S62095; S15071; !1S28887 REFERENCE S04471 !$#authors Ikehata, O.; Nishiyama, M.; Horinouchi, S.; Beppu, T. !$#journal Eur. J. Biochem. (1989) 181:563-570 !$#title Primary structure of nitrile hydratase deduced from the !1nucleotide sequence of a Rhodococcus species and its !1expression in Escherichia coli. !$#cross-references MUID:89276338; PMID:2659343 !$#accession S04472 !'##molecule_type DNA !'##residues 1-207 ##label IKE1 !'##cross-references EMBL:X14668; NID:g46429; PIDN:CAA32797.1; !1PID:g46430 !'##experimental_source strain N-774 !$#accession A30463 !'##molecule_type protein !'##residues 2-19;47-66;144-159 ##label IKE2 REFERENCE S16606 !$#authors Nishiyama, M. !$#submission submitted to the EMBL Data Library, March 1989 !$#accession S16606 !'##molecule_type DNA !'##residues 1-17,'A',19-207 ##label NIS !'##cross-references EMBL:X14668 REFERENCE S02070 !$#authors Endo, T.; Watanabe, I. !$#journal FEBS Lett. (1989) 243:61-64 !$#title Nitrile hydratase of Rhodococcus sp. N-774. Purification and !1amino acid sequences. !$#cross-references MUID:89153549; PMID:2920826 !$#accession S02070 !'##molecule_type protein !'##residues 2-19,'T' ##label END REFERENCE S54104 !$#authors Bigey, F.; Chebrou, H.; Arnaud, A.; Galzy, P. !$#submission submitted to the EMBL Data Library, March 1995 !$#description Cloning, sequencing of the modified nitrile hydratase gene !1from mutant strain Rhodococcus sp. ACV2. !$#accession S54105 !'##molecule_type DNA !'##residues 1-207 ##label BIG !'##cross-references EMBL:Z48769; NID:g769823; PIDN:CAA88685.1; !1PID:g769825 !'##experimental_source strain ACV2 REFERENCE S18291 !$#authors Nishiyama, M. !$#submission submitted to the EMBL Data Library, July 1990 !$#accession S62095 !'##molecule_type DNA !'##residues 1-207 ##label NI2 !'##cross-references EMBL:X54074; NID:g46410; PIDN:CAA38010.1; !1PID:g46412 !'##experimental_source strain N-774 REFERENCE S15070 !$#authors Hashimoto, Y.; Nishiyama, M.; Ikehata, O.; Horinouchi, S.; !1Beppu, T. !$#journal Biochim. Biophys. Acta (1991) 1088:225-233 !$#title Cloning and characterization of an amidase gene from !1Rhodococcus species N-774 and its expression in Escherichia !1coli. !$#cross-references MUID:91159474; PMID:2001397 !$#accession S15071 !'##molecule_type DNA !'##residues 1-29;30,197-207 ##label HAS !'##cross-references EMBL:X54074 !'##experimental_source strain N-774 REFERENCE A73039 !$#authors Huang, W.; Schneider, G.; Lindqvist, Y. !$#submission submitted to the Brookhaven Protein Data Bank, April 1997 !$#cross-references PDB:1AHJ !$#contents annotation; X-ray crystallography, 2.65 angstroms, residues !110-17,'A',19-207 REFERENCE A58907 !$#authors Nagashima, S.; Nakasako, M.; Dohmae, N.; Tsujimura, M.; !1Takio, K.; Odaka, M.; Yohada, M.; Kamiya, N.; Endo, I. !$#journal Nat. Struct. Biol. (1998) 5:347-351 !$#title Novel non-heme iron center of nitrile hydratase with a claw !1setting of oxygen atoms. !$#cross-references MUID:98246406; PMID:9586994 !$#contents annotation; X-ray crystallography, 1.7 angstroms; mass !1spectroscopic identification COMMENT An activating protein (see PIR:JC2313) is required to !1generate the active site of this enzyme. FUNCTION !$#description catalyzes the reaction of one molecule of water and an !1aliphatic nitrile to form the corresponding aliphatic amide CLASSIFICATION #superfamily nitrile hydratase alpha chain KEYWORDS carbon-oxygen lyase; hydro-lyase; iron; metalloprotein FEATURE !$2-207 #product nitrile hydratase alpha chain #status !8experimental #label MAT\ !$110,113,114,115 #binding_site nitrosyl iron (Cys, Cys, Ser, Cys) !8(shared with beta chain) #status experimental\ !$113 #modified_site cysteine sulfinic acid (Cys) #status !8experimental\ !$115 #modified_site cysteine sulfenic acid (Cys) #status !8experimental SUMMARY #length 207 #molecular-weight 22996 #checksum 2749 SEQUENCE /// ENTRY JN0705 #type complete TITLE nitrile hydratase (EC 4.2.1.84) alpha chain - Rhodococcus erythropolis ORGANISM #formal_name Rhodococcus erythropolis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS JN0705 REFERENCE PN0570 !$#authors Duran, R.; Nishiyama, M.; Horinouchi, S.; Beppu, T. !$#journal Biosci. Biotechnol. Biochem. (1993) 57:1323-1328 !$#title Characterization of nitrile hydratase genes cloned by DNA !1screeing from Rhodococcus erythropolis. !$#cross-references MUID:93379358; PMID:7764017 !$#accession JN0705 !'##molecule_type DNA !'##residues 1-207 ##label DUR !'##cross-references DDBJ:D14454; NID:g441203; PIDN:BAA03348.1; !1PID:g559379 !'##experimental_source strain JCM6823 GENETICS !$#gene NHase FUNCTION !$#description catalyzes the reaction of one molecule of water and an !1aliphatic nitrile to form the corresponding aliphatic amide CLASSIFICATION #superfamily nitrile hydratase alpha chain KEYWORDS carbon-oxygen lyase; hydro-lyase; iron; metalloprotein FEATURE !$2-207 #product nitrile hydratase alpha chain #status !8predicted #label MAT\ !$110,113,114,115 #binding_site nitrosyl iron (Cys, Cys, Ser, Cys) !8(shared with beta chain) #status predicted\ !$113 #modified_site cysteine sulfinic acid (Cys) #status !8predicted\ !$115 #modified_site cysteine sulfenic acid (Cys) #status !8predicted SUMMARY #length 207 #molecular-weight 23116 #checksum 4579 SEQUENCE /// ENTRY A42725 #type complete TITLE nitrile hydratase (EC 4.2.1.84) alpha chain - Pseudomonas chlororaphis (strain B23) ORGANISM #formal_name Pseudomonas chlororaphis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A42725 REFERENCE A42725 !$#authors Nishiyama, M.; Horinouchi, S.; Kobayashi, M.; Nagasawa, T.; !1Yamada, H.; Beppu, T. !$#journal J. Bacteriol. (1991) 173:2465-2472 !$#title Cloning and characterization of genes responsible for !1metabolism of nitrile compounds from Pseudomonas !1chlororaphis B23. !$#cross-references MUID:91193202; PMID:2013568 !$#accession A42725 !'##molecule_type DNA !'##residues 1-200 ##label NIS !'##cross-references GB:D90216; NID:g216850; PIDN:BAA14245.1; !1PID:g216852 FUNCTION !$#description catalyzes the reaction of one molecule of water and an !1aliphatic nitrile to form the corresponding aliphatic amide CLASSIFICATION #superfamily nitrile hydratase alpha chain KEYWORDS carbon-oxygen lyase; hydro-lyase; iron; metalloprotein FEATURE !$2-200 #product nitrile hydratase alpha chain #status !8predicted #label MAT\ !$105,108,109,110 #binding_site nitrosyl iron (Cys, Cys, Ser, Cys) !8(shared with beta chain) #status predicted\ !$108 #modified_site cysteine sulfinic acid (Cys) #status !8predicted\ !$110 #modified_site cysteine sulfenic acid (Cys) #status !8predicted SUMMARY #length 200 #molecular-weight 22117 #checksum 6893 SEQUENCE /// ENTRY S04473 #type complete TITLE nitrile hydratase (EC 4.2.1.84) beta chain [validated] - Rhodococcus sp. ORGANISM #formal_name Rhodococcus sp. DATE 21-Nov-1998 #sequence_revision 21-Nov-1998 #text_change 23-Mar-2001 ACCESSIONS S04473; S02071; S15072; S54106; S62096 REFERENCE S04471 !$#authors Ikehata, O.; Nishiyama, M.; Horinouchi, S.; Beppu, T. !$#journal Eur. J. Biochem. (1989) 181:563-570 !$#title Primary structure of nitrile hydratase deduced from the !1nucleotide sequence of a Rhodococcus species and its !1expression in Escherichia coli. !$#cross-references MUID:89276338; PMID:2659343 !$#accession S04473 !'##molecule_type DNA !'##residues 1-212 ##label IKE !'##cross-references EMBL:X14668; NID:g46429; PIDN:CAA32798.1; !1PID:g46431 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE S02070 !$#authors Endo, T.; Watanabe, I. !$#journal FEBS Lett. (1989) 243:61-64 !$#title Nitrile hydratase of Rhodococcus sp. N-774. Purification and !1amino acid sequences. !$#cross-references MUID:89153549; PMID:2920826 !$#accession S02071 !'##molecule_type protein !'##residues 1-19 ##label END REFERENCE S15070 !$#authors Hashimoto, Y.; Nishiyama, M.; Ikehata, O.; Horinouchi, S.; !1Beppu, T. !$#journal Biochim. Biophys. Acta (1991) 1088:225-233 !$#title Cloning and characterization of an amidase gene from !1Rhodococcus species N-774 and its expression in Escherichia !1coli. !$#cross-references MUID:91159474; PMID:2001397 !$#accession S15072 !'##molecule_type DNA !'##residues 1-12;179-212 ##label HAS !'##cross-references EMBL:X54074 !'##experimental_source strain N-774 REFERENCE S54104 !$#authors Bigey, F.; Chebrou, H.; Arnaud, A.; Galzy, P. !$#submission submitted to the EMBL Data Library, March 1995 !$#description Cloning, sequencing of the modified nitrile hydratase gene !1from mutant strain Rhodococcus sp. ACV2. !$#accession S54106 !'##molecule_type DNA !'##residues 1-39,'V',41-212 ##label BIG !'##cross-references EMBL:Z48769; NID:g769823; PIDN:CAA88686.1; !1PID:g769826 REFERENCE A73039 !$#authors Huang, W.; Schneider, G.; Lindqvist, Y. !$#submission submitted to the Brookhaven Protein Data Bank, April 1997 !$#cross-references PDB:1AHJ !$#contents annotation; X-ray crystallography, 2.65 angstroms REFERENCE A58907 !$#authors Nagashima, S.; Nakasako, M.; Dohmae, N.; Tsujimura, M.; !1Takio, K.; Odaka, M.; Yohada, M.; Kamiya, N.; Endo, I. !$#journal Nat. Struct. Biol. (1998) 5:347-351 !$#title Novel non-heme iron center of nitrile hydratase with a claw !1setting of oxygen atoms. !$#cross-references MUID:98246406; PMID:9586994 !$#contents annotation; X-ray crystallography, 1.7 angstroms; mass !1spectroscopic identification FUNCTION !$#description catalyzes the reaction of one molecule of water and an !1aliphatic nitrile to form the corresponding aliphatic amide CLASSIFICATION #superfamily nitrile hydratase beta chain KEYWORDS carbon-oxygen lyase; hydro-lyase; iron; metalloprotein FEATURE !$1-212 #product nitrile hydratase beta chain #status !8experimental #label MAT\ !$56,141 #binding_site nitrosyl iron (Arg) (shared with alpha !8chain) #status experimental SUMMARY #length 212 #molecular-weight 23487 #checksum 2576 SEQUENCE /// ENTRY JN0706 #type complete TITLE nitrile hydratase (EC 4.2.1.84) beta chain - Rhodococcus erythropolis ORGANISM #formal_name Rhodococcus erythropolis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS JN0706 REFERENCE PN0570 !$#authors Duran, R.; Nishiyama, M.; Horinouchi, S.; Beppu, T. !$#journal Biosci. Biotechnol. Biochem. (1993) 57:1323-1328 !$#title Characterization of nitrile hydratase genes cloned by DNA !1screeing from Rhodococcus erythropolis. !$#cross-references MUID:93379358; PMID:7764017 !$#accession JN0706 !'##molecule_type DNA !'##residues 1-212 ##label DUR !'##cross-references DDBJ:D14454; NID:g441203; PIDN:BAA03349.1; !1PID:g559380 !'##experimental_source strain JCM6823 COMMENT This enzyme catalyzes the hydration of nitrile compounds to !1the corresponding amide. CLASSIFICATION #superfamily nitrile hydratase beta chain KEYWORDS carbon-oxygen lyase; hydro-lyase SUMMARY #length 212 #molecular-weight 23487 #checksum 1555 SEQUENCE /// ENTRY B42725 #type complete TITLE nitrile hydratase (EC 4.2.1.84) beta chain - Pseudomonas chlororaphis (strain B23) ORGANISM #formal_name Pseudomonas chlororaphis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS B42725 REFERENCE A42725 !$#authors Nishiyama, M.; Horinouchi, S.; Kobayashi, M.; Nagasawa, T.; !1Yamada, H.; Beppu, T. !$#journal J. Bacteriol. (1991) 173:2465-2472 !$#title Cloning and characterization of genes responsible for !1metabolism of nitrile compounds from Pseudomonas !1chlororaphis B23. !$#cross-references MUID:91193202; PMID:2013568 !$#accession B42725 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-220 ##label NIS !'##cross-references GB:D90216; NID:g216850; PIDN:BAA14246.1; !1PID:g216853 CLASSIFICATION #superfamily nitrile hydratase beta chain KEYWORDS carbon-oxygen lyase; hydro-lyase SUMMARY #length 220 #molecular-weight 24545 #checksum 9648 SEQUENCE /// ENTRY S19715 #type complete TITLE nitrile hydratase (EC 4.2.1.84) beta chain, L-type - Rhodococcus rhodochrous (strain J1) ALTERNATE_NAMES L-nitrilase ORGANISM #formal_name Rhodococcus rhodochrous #variety strain J1 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S19715; S78585 REFERENCE S19713 !$#authors Kobayashi, M.; Nishiyama, M.; Nagasawa, T.; Horinouchi, S.; !1Beppu, T.; Yamada, H. !$#journal Biochim. Biophys. Acta (1991) 1129:23-33 !$#title Cloning, nucleotide sequence and expression in Escherichia !1coli of two cobalt-containing nitrile hydratase genes from !1Rhodococcus rhodochrous J1. !$#cross-references MUID:92096459; PMID:1840499 !$#accession S19715 !'##molecule_type DNA !'##residues 1-226 ##label KOB !'##cross-references EMBL:X64360; NID:g49060; PIDN:CAA45711.1; !1PID:g49061 !'##experimental_source strain J1 !$#accession S78585 !'##molecule_type protein !'##residues 1-31;95-109;110-129;166-197;198-224 ##label KOY FUNCTION !$#description catalyzes the hydration of nitrile compounds to the !1corresponding aliphatic amides !$#pathway cyanoamino acid metabolism CLASSIFICATION #superfamily nitrile hydratase beta chain KEYWORDS carbon-oxygen lyase; cobalt; hydro-lyase FEATURE !$1-226 #product nitrile hydratase beta chain, L-type #status !8experimental #label MAT SUMMARY #length 226 #molecular-weight 25201 #checksum 4628 SEQUENCE /// ENTRY B41326 #type complete TITLE nitrile hydratase (EC 4.2.1.84) beta chain - Rhodococcus sp. ORGANISM #formal_name Rhodococcus sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B41326 REFERENCE A41326 !$#authors Mayaux, J.F.; Cerbelaud, E.; Soubrier, F.; Yeh, P.; Blanche, !1F.; Petre, D. !$#journal J. Bacteriol. (1991) 173:6694-6704 !$#title Purification, cloning, and primary structure of a new !1enantiomer-selective amidase from a Rhodococcus strain: !1structural evidence for a conserved genetic coupling with !1nitrile hydratase. !$#cross-references MUID:92041549; PMID:1938876 !$#accession B41326 !'##status preliminary !'##molecule_type DNA !'##residues 1-235 ##label MAY !'##cross-references GB:M74531; NID:g152051; PIDN:AAA26184.1; !1PID:g152053 CLASSIFICATION #superfamily nitrile hydratase beta chain KEYWORDS carbon-oxygen lyase; hydro-lyase SUMMARY #length 235 #molecular-weight 26078 #checksum 5804 SEQUENCE /// ENTRY S19713 #type complete TITLE nitrile hydratase (EC 4.2.1.84) beta chain, H-type - Rhodococcus rhodochrous (strain J1) ALTERNATE_NAMES H-nitrilase ORGANISM #formal_name Rhodococcus rhodochrous #variety strain J1 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S19713; S78583; S14772 REFERENCE S19713 !$#authors Kobayashi, M.; Nishiyama, M.; Nagasawa, T.; Horinouchi, S.; !1Beppu, T.; Yamada, H. !$#journal Biochim. Biophys. Acta (1991) 1129:23-33 !$#title Cloning, nucleotide sequence and expression in Escherichia !1coli of two cobalt-containing nitrile hydratase genes from !1Rhodococcus rhodochrous J1. !$#cross-references MUID:92096459; PMID:1840499 !$#accession S19713 !'##molecule_type DNA !'##residues 1-229 ##label KOB !'##cross-references EMBL:X64359; NID:g49057; PIDN:CAA45709.1; !1PID:g49058 !'##experimental_source strain J1 !$#accession S78583 !'##molecule_type protein !'##residues 1-28;69-78 ##label KOY REFERENCE S14771 !$#authors Nagasawa, T.; Takeuchi, K.; Yamada, H. !$#journal Eur. J. Biochem. (1991) 196:581-589 !$#title Characterization of a new cobalt-containing nitrile !1hydratase purified from urea-induced cells of Rhodococcus !1rhodochrous J1. !$#cross-references MUID:91192028; PMID:2013281 !$#accession S14772 !'##molecule_type protein !'##residues 1-6,'I',8-28 ##label EUR !'##experimental_source strain J1 FUNCTION !$#description catalyzes the hydration of nitrile compounds to the !1corresponding aliphatic amides !$#pathway cyanoamino acid metabolism CLASSIFICATION #superfamily nitrile hydratase beta chain KEYWORDS carbon-oxygen lyase; cobalt; hydro-lyase FEATURE !$1-229 #product nitrile hydratase beta chain, H-type #status !8experimental #label MAT SUMMARY #length 229 #molecular-weight 26321 #checksum 7356 SEQUENCE /// ENTRY S54799 #type complete TITLE nitrile hydratase (EC 4.2.1.84) beta chain, H-type - Rhodococcus sp. (strain M8) ALTERNATE_NAMES H-nitrilase ORGANISM #formal_name Rhodococcus sp. #variety strain M8 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S54799 REFERENCE S54799 !$#authors Veiko, V.P.; Yanenko, A.S.; Alekseeva, M.G.; Sintin, A.A.; !1Gulko, L.B.; Ratmanova, K.I.; Ovcharova, I.V.; Andreeva, !1L.B.; Voronin, S.P.; Debavov, V.G. !$#submission submitted to the EMBL Data Library, April 1995 !$#description Cloning and nucleotide sequence of cobalt-containing nitrile !1hydratase gene from Rhodococcus sp. M8. !$#accession S54799 !'##molecule_type DNA !'##residues 1-229 ##label VEI !'##cross-references EMBL:X86737; NID:g806579; PIDN:CAA60416.1; !1PID:g806580 !'##experimental_source strain M8 FUNCTION !$#description catalyzes the hydration of nitrile compounds to the !1corresponding aliphatic amides !$#pathway cyanoamino acid metabolism CLASSIFICATION #superfamily nitrile hydratase beta chain KEYWORDS carbon-oxygen lyase; cobalt; hydro-lyase SUMMARY #length 229 #molecular-weight 26293 #checksum 7920 SEQUENCE /// ENTRY DWDXAF #type complete TITLE 2-hydroxyglutaryl-CoA dehydratase (EC 4.2.1.-) alpha chain - Acidaminococcus fermentans ORGANISM #formal_name Acidaminococcus fermentans DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 18-Jun-1999 ACCESSIONS S04477; A33213; S05698; S00198; S36106 REFERENCE S04476 !$#authors Dutscho, R.; Wohlfarth, G.; Buckel, P.; Buckel, W. !$#journal Eur. J. Biochem. (1989) 181:741-746 !$#title Cloning and sequencing of the genes of 2-hydroxyglutaryl-CoA !1dehydratase from Acidaminococcus fermentans. !$#cross-references MUID:89276363; PMID:2659350 !$#accession S04477 !'##molecule_type DNA !'##residues 1-477 ##label DUT !'##cross-references EMBL:X14252 !$#accession A33213 !'##molecule_type protein !'##residues 67-79;197-203 ##label DUT2 REFERENCE S05698 !$#authors Buckel, W. !$#submission submitted to the EMBL Data Library, April 1989 !$#accession S05698 !'##molecule_type DNA !'##residues 1-25,'P',27-477 ##label BUC !'##cross-references EMBL:X14252; NID:g38798; PIDN:CAA32465.1; !1PID:g38800 REFERENCE S00198 !$#authors Schweiger, G.; Dutscho, R.; Buckel, W. !$#journal Eur. J. Biochem. (1987) 169:441-448 !$#title Purification of 2-hydroxyglutaryl-CoA dehydratase from !1Acidaminococcus fermentans: an iron-sulfur protein. !$#cross-references MUID:88082776; PMID:3691501 !$#accession S00198 !'##molecule_type protein !'##residues 2-31,'X',33-34 ##label SCH REFERENCE S36104 !$#authors Bendrat, K.; Mueller, U.; Klees, A.G.; Buckel, W. !$#journal FEBS Lett. (1993) 329:329-331 !$#title Identification of the gene encoding the activator of !1(R)-2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus !1fermentans by gene expression in Escherichia coli. !$#cross-references MUID:93374040; PMID:8365476 !$#accession S36106 !'##status preliminary !'##molecule_type DNA !'##residues 1-23 ##label BEN !'##cross-references EMBL:X59645 GENETICS !$#gene hdgA CLASSIFICATION #superfamily 2-hydroxyglutaryl-CoA dehydratase alpha chain KEYWORDS 4Fe-4S; carbon-oxygen lyase; heterotetramer; hydro-lyase; !1iron-sulfur protein; metalloprotein FEATURE !$2-477 #product 2-hydroxyglutaryl-CoA dehydratase alpha !8chain #status experimental #label MAT SUMMARY #length 477 #molecular-weight 53995 #checksum 3341 SEQUENCE /// ENTRY DWDXBF #type complete TITLE 2-hydroxyglutaryl-CoA dehydratase (EC 4.2.1.-) beta chain - Acidaminococcus fermentans ORGANISM #formal_name Acidaminococcus fermentans DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 18-Jun-1999 ACCESSIONS S04478; S00199 REFERENCE S04476 !$#authors Dutscho, R.; Wohlfarth, G.; Buckel, P.; Buckel, W. !$#journal Eur. J. Biochem. (1989) 181:741-746 !$#title Cloning and sequencing of the genes of 2-hydroxyglutaryl-CoA !1dehydratase from Acidaminococcus fermentans. !$#cross-references MUID:89276363; PMID:2659350 !$#accession S04478 !'##molecule_type DNA !'##residues 1-379 ##label DUT1 !'##cross-references EMBL:X14252; NID:g38798; PIDN:CAA32466.1; !1PID:g38802 REFERENCE S00198 !$#authors Schweiger, G.; Dutscho, R.; Buckel, W. !$#journal Eur. J. Biochem. (1987) 169:441-448 !$#title Purification of 2-hydroxyglutaryl-CoA dehydratase from !1Acidaminococcus fermentans: an iron-sulfur protein. !$#cross-references MUID:88082776; PMID:3691501 !$#accession S00199 !'##molecule_type protein !'##residues 2-33,'X',35-41,'X',43-44 ##label SCH GENETICS !$#gene hdgB CLASSIFICATION #superfamily 2-hydroxyglutaryl-CoA dehydratase beta chain KEYWORDS 4Fe-4S; carbon-oxygen lyase; heterotetramer; hydro-lyase; !1iron-sulfur protein; metalloprotein FEATURE !$2-379 #product 2-hydroxyglutaryl-CoA dehydratase beta chain !8#status experimental #label MAT SUMMARY #length 379 #molecular-weight 41961 #checksum 4369 SEQUENCE /// ENTRY SYECZ1 #type complete TITLE tRNA-pseudouridine synthase I (EC 5.4.99.12) [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES pseudouridine synthase; uracil hydrolyase ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 01-Mar-2002 ACCESSIONS B23792; A28359; I69365; I69366; D65004 REFERENCE A93577 !$#authors Arps, P.J.; Marvel, C.C.; Rubin, B.C.; Tolan, D.A.; Penhoet, !1E.E.; Winkler, M.E. !$#journal Nucleic Acids Res. (1985) 13:5297-5315 !$#title Structural features of the hisT operon of Escherichia coli !1K-12. !$#cross-references MUID:85269644; PMID:2991861 !$#accession B23792 !'##molecule_type DNA !'##residues 1-270 ##label ARP !'##cross-references GB:X02743; NID:g41716; PIDN:CAA26522.1; PID:g41718 !'##experimental_source K12 REFERENCE A28359 !$#authors Kammen, H.O.; Marvel, C.C.; Hardy, L.; Penhoet, E.E. !$#journal J. Biol. Chem. (1988) 263:2255-2263 !$#title Purification, structure, and properties of Escherichia coli !1tRNA pseudouridine synthase I. !$#cross-references MUID:88115366; PMID:3276686 !$#accession A28359 !'##molecule_type protein !'##residues 2-11 ##label KAM REFERENCE I54872 !$#authors Arps, P.J.; Winkler, M.E. !$#journal J. Bacteriol. (1987) 169:1061-1070 !$#title Structural analysis of the Escherichia coli K-12 hisT operon !1by using a kanamycin resistance cassette. !$#cross-references MUID:87137258; PMID:3029016 !$#accession I69365 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-10 ##label AR2 !'##cross-references GB:M15542; NID:g147127; PIDN:AAA24313.1; !1PID:g147133 !$#accession I69366 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 267-270 ##label AR3 !'##cross-references GB:M15543; NID:g147128 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65004 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-270 ##label BLAT !'##cross-references GB:AE000320; GB:U00096; NID:g1788647; !1PIDN:AAC75378.1; PID:g1788657; UWGP:b2318 !'##experimental_source strain K-12, substrain MG1655 COMMENT This enzyme catalyzes the formation of pseudouridine in the !1anticodon stem and loop of tRNAs in E. coli. GENETICS !$#gene truA; hisT !$#map_position 50 min COMPLEX homodimer [validated, MUID:20091078] FUNCTION !$#description EC 5.4.99.12 [validated, MUID:88115366] CLASSIFICATION #superfamily tRNA-pseudouridine synthase I KEYWORDS carbon-oxygen lyase; hydro-lyase; intramolecular !1transferase; isomerase; tRNA modification FEATURE !$2-270 #product pseudouridylate synthase I #status !8experimental #label MAT SUMMARY #length 270 #molecular-weight 30399 #checksum 1175 SEQUENCE /// ENTRY WZWCP1 #type complete TITLE pectate lyase (EC 4.2.2.2) A precursor - Erwinia carotovora ALTERNATE_NAMES pectate lyase 1 precursor; pectate transeliminase ORGANISM #formal_name Erwinia carotovora DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 18-Jun-1999 ACCESSIONS JT0242; A38061; S49305 REFERENCE JT0242 !$#authors Lei, S.P.; Lin, H.C.; Wang, S.S.; Wilcox, G. !$#journal Gene (1988) 62:159-164 !$#title Characterization of the Erwinia carotovora pelA gene and its !1product pectate lyase A. !$#cross-references MUID:88226011; PMID:3371662 !$#accession JT0242 !'##molecule_type DNA !'##residues 1-374 ##label LE1 !'##cross-references GB:M18859 !$#accession A38061 !'##molecule_type protein !'##residues 23-36 ##label LE2 REFERENCE S49305 !$#authors Bartling, S.; Wegener, C.; Olsen, O. !$#submission submitted to the EMBL Data Library, September 1994 !$#description Synergism between Erwinia pectate lyase isoenzymes that !1depolymerize both pectate and pectin. !$#accession S49305 !'##status preliminary !'##molecule_type DNA !'##residues 1-12,'V',14-50,'VDI',54-55,'A',57,'KK',60-61,'S',63-64, !1'AV',67-111,'I',113-127,'M',129-134,'I',136-153,'I',155-194, !1'A',196-227,'Y',229-232,'Y',234-251,'N',253-255,'G',257-313, !1'N',315-356,'S',358-374 ##label BAR !'##cross-references EMBL:X81847; NID:g551237; PIDN:CAA57439.1; !1PID:g551238 GENETICS !$#gene pelA !$#note E. carotovora strain EC has three pectate lyase genes, pelA, !1pelB, and pelC, which encode pectate lyases A, B, and C, !1respectively CLASSIFICATION #superfamily pectate lyase KEYWORDS carbon-oxygen lyase FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-374 #product pectate lyase A #status predicted #label MAT SUMMARY #length 374 #molecular-weight 40281 #checksum 5560 SEQUENCE /// ENTRY WZWCPC #type complete TITLE pectate lyase (EC 4.2.2.2) C precursor - Erwinia carotovora subsp. carotovora ORGANISM #formal_name Erwinia carotovora subsp. carotovora DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS S07652 REFERENCE S07652 !$#authors Hinton, J.C.D.; Sidebotham, J.M.; Gill, D.R.; Salmond, !1G.P.C. !$#journal Mol. Microbiol. (1989) 3:1785-1795 !$#title Extracellular and periplasmic isoenzymes of pectate lyase !1from Erwinia carotovora subspecies carotovora belong to !1different gene families. !$#cross-references MUID:90158126; PMID:2695748 !$#accession S07652 !'##molecule_type DNA !'##residues 1-374 ##label HIN !'##cross-references EMBL:X16398; NID:g41146; PIDN:CAA34433.1; !1PID:g41147 GENETICS !$#gene pelC CLASSIFICATION #superfamily pectate lyase KEYWORDS carbon-oxygen lyase FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-374 #product pectate lyase C #status predicted #label MAT SUMMARY #length 374 #molecular-weight 40565 #checksum 2520 SEQUENCE /// ENTRY WZWCP3 #type complete TITLE pectate lyase (EC 4.2.2.2) III precursor - Erwinia carotovora (strain Er[IAM1068]) ORGANISM #formal_name Erwinia carotovora DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jun-2000 ACCESSIONS JU0462 REFERENCE JU0462 !$#authors Yoshida, A.; Izuta, M.; Ito, K.; Kamio, Y.; Izaki, K. !$#journal Agric. Biol. Chem. (1991) 55:933-940 !$#title Cloning and characterization of the pectate lyase III gene !1of Erwinia carotovora Er. !$#cross-references MUID:91254743; PMID:1368679 !$#accession JU0462 !'##molecule_type DNA !'##residues 1-374 ##label YOS !'##cross-references GB:D10064; NID:g216692; PIDN:BAA00953.1; !1PID:g216693; GB:D01243 GENETICS !$#gene pelIII CLASSIFICATION #superfamily pectate lyase KEYWORDS carbon-oxygen lyase FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-374 #product pectate lyase III #status predicted #label !8MAT SUMMARY #length 374 #molecular-weight 40480 #checksum 2325 SEQUENCE /// ENTRY WZWCPB #type complete TITLE pectate lyase (EC 4.2.2.2) B precursor - Erwinia chrysanthemi (strain EC16) ORGANISM #formal_name Erwinia chrysanthemi DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS B25158 REFERENCE A91826 !$#authors Keen, N.T.; Tamaki, S. !$#journal J. Bacteriol. (1986) 168:595-606 !$#title Structure of two pectate lyase genes from Erwinia !1chrysanthemi EC16 and their high-level expression in !1Escherichia coli. !$#cross-references MUID:87056939; PMID:3536853 !$#accession B25158 !'##molecule_type DNA !'##residues 1-375 ##label KEE !'##cross-references GB:M14510; NID:g148455; PIDN:AAA24847.1; !1PID:g148456 CLASSIFICATION #superfamily pectate lyase KEYWORDS carbon-oxygen lyase FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-375 #product pectate lyase B #status predicted #label MAT SUMMARY #length 375 #molecular-weight 40234 #checksum 1217 SEQUENCE /// ENTRY WZWC6C #type complete TITLE pectate lyase (EC 4.2.2.2) C precursor - Erwinia chrysanthemi (strain EC16) ORGANISM #formal_name Erwinia chrysanthemi DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS A31091 REFERENCE A91876 !$#authors Tamaki, S.J.; Gold, S.; Robeson, M.; Manulis, S.; Keen, N.T. !$#journal J. Bacteriol. (1988) 170:3468-3478 !$#title Structure and organization of the pel genes from Erwinia !1chrysanthemi EC16. !$#cross-references MUID:88298652; PMID:3042750 !$#accession A31091 !'##molecule_type DNA !'##residues 1-375 ##label TAM !'##cross-references GB:M19411; NID:g148459; PIDN:AAA24849.1; !1PID:g148460 COMMENT Pectate lyase is involved in the soft-rotting disease of !1plants caused by E. chrysanthemi. In strain EC16, four !1pectate lyases are produced. GENETICS !$#gene pelC CLASSIFICATION #superfamily pectate lyase KEYWORDS carbon-oxygen lyase FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-375 #product pectate lyase C #status predicted #label MAT SUMMARY #length 375 #molecular-weight 39943 #checksum 3227 SEQUENCE /// ENTRY WZWC6E #type complete TITLE pectate lyase (EC 4.2.2.2) E precursor - Erwinia chrysanthemi (strain EC16) ORGANISM #formal_name Erwinia chrysanthemi DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS A25158 REFERENCE A91826 !$#authors Keen, N.T.; Tamaki, S. !$#journal J. Bacteriol. (1986) 168:595-606 !$#title Structure of two pectate lyase genes from Erwinia !1chrysanthemi EC16 and their high-level expression in !1Escherichia coli. !$#cross-references MUID:87056939; PMID:3536853 !$#accession A25158 !'##molecule_type DNA !'##residues 1-385 ##label KEE !'##cross-references GB:M14509; NID:g148448; PIDN:AAA24844.1; !1PID:g148450 CLASSIFICATION #superfamily pectate lyase KEYWORDS carbon-oxygen lyase FEATURE !$1-30 #domain signal sequence #status predicted #label SIG\ !$31-385 #product pectate lyase E #status predicted #label MAT SUMMARY #length 385 #molecular-weight 41250 #checksum 2109 SEQUENCE /// ENTRY WZWCPE #type complete TITLE pectate lyase (EC 4.2.2.2) E precursor - Erwinia chrysanthemi ORGANISM #formal_name Erwinia chrysanthemi DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS JQ0190; S06968 REFERENCE JQ0189 !$#authors Reverchon, S.; Huang, Y.; Bourson, C.; Robert-Baudouy, J. !$#journal Gene (1989) 85:125-134 !$#title Nucleotide sequences of thr Erwinia chrysanthemi ogl and !1pelE genes negatively regulated by the kdgR gene product. !$#cross-references MUID:90152353; PMID:2695393 !$#accession JQ0190 !'##molecule_type DNA !'##residues 1-404 ##label REV !'##cross-references GB:X17284 !'##experimental_source strain 3937 REFERENCE S06968 !$#authors van Gijsegem, F. !$#journal Mol. Microbiol. (1989) 3:1415-1424 !$#title Relationship between the pel genes of the pelADE cluster in !1Erwinia chrysanthemi strain B374. !$#cross-references MUID:90136069; PMID:2615652 !$#accession S06968 !'##molecule_type DNA !'##residues 1-113,'S',115-203,'F',205-392,'G',394-404 ##label VAN !'##cross-references EMBL:X17284; NID:g42343; PIDN:CAA35175.1; !1PID:g42344 COMMENT This enzyme cleaves the alpha 1-4 glycosidic bond between !1two galacturonate residues. GENETICS !$#gene pelE CLASSIFICATION #superfamily pectate lyase KEYWORDS carbon-oxygen lyase FEATURE !$1-41 #domain signal sequence #status predicted #label SIG\ !$42-404 #product pectate lyase E #status predicted #label MAT SUMMARY #length 404 #molecular-weight 43094 #checksum 9214 SEQUENCE /// ENTRY WZWC6A #type complete TITLE pectate lyase (EC 4.2.2.2) A precursor - Erwinia chrysanthemi (strain EC16) ORGANISM #formal_name Erwinia chrysanthemi DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS B31091 REFERENCE A91876 !$#authors Tamaki, S.J.; Gold, S.; Robeson, M.; Manulis, S.; Keen, N.T. !$#journal J. Bacteriol. (1988) 170:3468-3478 !$#title Structure and organization of the pel genes from Erwinia !1chrysanthemi EC16. !$#cross-references MUID:88298652; PMID:3042750 !$#accession B31091 !'##molecule_type DNA !'##residues 1-393 ##label TAM !'##cross-references GB:M14509; NID:g148448; PIDN:AAA24843.1; !1PID:g148449 GENETICS !$#gene pelA CLASSIFICATION #superfamily pectate lyase KEYWORDS carbon-oxygen lyase FEATURE !$1-32 #domain signal sequence #status predicted #label SIG\ !$33-393 #product pectate lyase A #status predicted #label MAT SUMMARY #length 393 #molecular-weight 42079 #checksum 9354 SEQUENCE /// ENTRY WZWCCC #type complete TITLE pectate lyase (EC 4.2.2.2), periplasmic, precursor - Erwinia carotovora subsp. carotovora ORGANISM #formal_name Erwinia carotovora subsp. carotovora DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS S07653 REFERENCE S07652 !$#authors Hinton, J.C.D.; Sidebotham, J.M.; Gill, D.R.; Salmond, !1G.P.C. !$#journal Mol. Microbiol. (1989) 3:1785-1795 !$#title Extracellular and periplasmic isoenzymes of pectate lyase !1from Erwinia carotovora subspecies carotovora belong to !1different gene families. !$#cross-references MUID:90158126; PMID:2695748 !$#accession S07653 !'##molecule_type DNA !'##residues 1-568 ##label HIN !'##cross-references EMBL:X16397; NID:g41143; PIDN:CAA34432.1; !1PID:g41144 CLASSIFICATION #superfamily pectate lyase, periplasmic KEYWORDS carbon-oxygen lyase; periplasmic space FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-568 #product pectate lyase, periplasmic #status predicted !8#label MAT SUMMARY #length 568 #molecular-weight 63523 #checksum 8236 SEQUENCE /// ENTRY WZEPPY #type complete TITLE pectate lyase (EC 4.2.2.2), periplasmic, precursor - Yersinia pseudotuberculosis ORGANISM #formal_name Yersinia pseudotuberculosis DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS A27742 REFERENCE A27742 !$#authors Manulis, S.; Kobayashi, D.Y.; Keen, N.T. !$#journal J. Bacteriol. (1988) 170:1825-1830 !$#title Molecular cloning and sequencing of a pectate lyase gene !1from Yersinia pseudotuberculosis. !$#cross-references MUID:88169511; PMID:2832382 !$#accession A27742 !'##molecule_type DNA !'##residues 1-541 ##label MAN !'##cross-references GB:M19399; NID:g155482; PIDN:AAA27660.1; !1PID:g155483 !'##experimental_source TCPB 3821 GENETICS !$#gene pelY CLASSIFICATION #superfamily pectate lyase, periplasmic KEYWORDS carbon-oxygen lyase; periplasmic space FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-541 #product pectate lyase, periplasmic #status predicted !8#label MAT SUMMARY #length 541 #molecular-weight 60738 #checksum 5618 SEQUENCE /// ENTRY SYBSR #type complete TITLE threonine synthase (EC 4.2.3.1) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YCR053w ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 03-Jun-2002 ACCESSIONS S22836; S20154; S19467 REFERENCE S22836 !$#authors Mannhaupt, G.; van der Linden, G.; Vetter, I.; Maurer, K.; !1Pilz, U.; Planta, R.; Feldmann, H. !$#journal Yeast (1990) 6:353-361 !$#title Analysis of the THR4 region on chromosome III of the yeast !1Saccharomyces cerevisiae. !$#cross-references MUID:90371958; PMID:2204248 !$#accession S22836 !'##molecule_type DNA !'##residues 1-514 ##label MAN !'##cross-references EMBL:X59720; NID:g1907116; PIDN:CAA42284.1; !1PID:g1907196 REFERENCE S20154 !$#authors Aas, S.F.; Rognes, S.E. !$#journal Nucleic Acids Res. (1990) 18:665 !$#title Nucleotide sequence of the yeast THR4 gene encoding !1threonine synthase. !$#cross-references MUID:90175003; PMID:2408022 !$#accession S20154 !'##molecule_type DNA !'##residues 1-514 ##label AAS !'##cross-references EMBL:X17256; NID:g4615; PIDN:CAA35157.1; PID:g4616 REFERENCE S19415 !$#authors van der Linden, C.G.; Maurer, C.T.C.; Planta, R.J.; van !1Vliet-Reedijk, J.C.; Vreken, P. !$#submission submitted to the Protein Sequence Database, March 1992 !$#accession S19467 !'##molecule_type DNA !'##residues 1-514 ##label LIN !'##cross-references EMBL:X59720; NID:g1907116; PIDN:CAA42284.1; !1PID:g1907196; GSPDB:GN00003; MIPS:YCR053w GENETICS !$#gene SGD:THR4; MIPS:YCR053w !'##cross-references SGD:S0000649; MIPS:YCR053w !$#map_position 3R CLASSIFICATION #superfamily threonine synthase KEYWORDS carbon-oxygen lyase; phosphoprotein; pyridoxal phosphate; !1threonine biosynthesis FEATURE !$124 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 514 #molecular-weight 57474 #checksum 6686 SEQUENCE /// ENTRY SYECR #type complete TITLE threonine synthase (EC 4.2.3.1) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 03-Jun-2002 ACCESSIONS A01157; S40533; S56631; D64720 REFERENCE A93492 !$#authors Parsot, C.; Cossart, P.; Saint-Girons, I.; Cohen, G.N. !$#journal Nucleic Acids Res. (1983) 11:7331-7345 !$#title Nucleotide sequence of thrC and of the transcription !1termination region of the threonine operon in Escherichia !1coli K12. !$#cross-references MUID:84069770; PMID:6316258 !$#accession A01157 !'##molecule_type DNA !'##residues 1-428 ##label PAR !'##cross-references GB:D10483; GB:J01597; GB:J01683; GB:J01706; !1GB:K01298; GB:K01990; GB:M10420; GB:M10611; GB:M12544; !1GB:V00259; GB:X04711; GB:X54847; GB:X54945; GB:X55034; !1GB:X56742; NID:g216434; PIDN:BAA01288.1; PID:g216437 REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40533 !'##molecule_type DNA !'##residues 1-428 ##label YUR !'##cross-references EMBL:D10483; NID:g216434; PIDN:BAA01288.1; !1PID:g216437 !'##experimental_source strain K-12 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56631 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-428 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97303.1; !1PID:g537247 !'##experimental_source strain K-12, substrain MG1655 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64720 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-428 ##label BLAT !'##cross-references GB:AE000111; GB:U00096; NID:g1786181; !1PIDN:AAC73115.1; PID:g1786185; UWGP:b0004 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene thrC !$#map_position 0 min CLASSIFICATION #superfamily threonine synthase KEYWORDS carbon-oxygen lyase; phosphoprotein; pyridoxal phosphate; !1threonine biosynthesis FEATURE !$107 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 428 #molecular-weight 47113 #checksum 5103 SEQUENCE /// ENTRY S16043 #type complete TITLE threonine synthase (EC 4.2.3.1) - Serratia marcescens ORGANISM #formal_name Serratia marcescens DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 03-Jun-2002 ACCESSIONS D47057; S16043 REFERENCE A47057 !$#authors Omori, K.; Imai, Y.; Suzuki, S.; Komatsubara, S. !$#journal J. Bacteriol. (1993) 175:785-794 !$#title Nucleotide sequence of the Serratia marcescens threonine !1operon and analysis of the threonine operon mutations which !1alter feedback inhibition of both aspartokinase I and !1homoserine dehydrogenase I. !$#cross-references MUID:93139048; PMID:8423151 !$#accession D47057 !'##molecule_type DNA !'##residues 1-429 ##label OMO !'##cross-references GB:D10387; NID:g216963; PIDN:BAA01222.1; !1PID:g216968 !'##experimental_source 8000 !'##note sequence extracted from NCBI backbone (NCBIN:123552, !1NCBIP:123556) REFERENCE S16040 !$#authors Omori, K.; Suzuki, S.; Komatsubara, S. !$#submission submitted to the EMBL Data Library, July 1991 !$#description Analysis of the thrA1A2BC genes of Serratia marcescens Sr41. !$#accession S16043 !'##molecule_type DNA !'##residues 1-429 ##label OM2 !'##cross-references EMBL:X60821; NID:g47271; PIDN:CAA43214.1; !1PID:g47275 GENETICS !$#gene thrC CLASSIFICATION #superfamily threonine synthase KEYWORDS carbon-oxygen lyase; phosphoprotein; pyridoxal phosphate; !1threonine biosynthesis FEATURE !$107 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 429 #molecular-weight 47094 #checksum 7470 SEQUENCE /// ENTRY SYPSRA #type complete TITLE threonine synthase (EC 4.2.3.1) - Pseudomonas aeruginosa ORGANISM #formal_name Pseudomonas aeruginosa DATE 31-Dec-1992 #sequence_revision 30-Jun-1993 #text_change 03-Jun-2002 ACCESSIONS S27980; S19919 REFERENCE S27979 !$#authors Clepet, C.; Borne, F.; Krishnapillai, V.; Baird, C.; Patte, !1J.C.; Cami, B. !$#journal Mol. Microbiol. (1992) 6:3109-3119 !$#title Isolation, organization and expression of the Pseudomonas !1aeruginosa threonine genes. !$#cross-references MUID:93086420; PMID:1333566 !$#accession S27980 !'##molecule_type DNA !'##residues 1-470 ##label CLE !'##cross-references EMBL:X65033 GENETICS !$#gene thrC !$#map_position 31 min CLASSIFICATION #superfamily threonine synthase KEYWORDS carbon-oxygen lyase; phosphoprotein; pyridoxal phosphate; !1threonine biosynthesis FEATURE !$113 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 470 #molecular-weight 51287 #checksum 927 SEQUENCE /// ENTRY SYECCG #type complete TITLE O-succinylhomoserine (thiol)-lyase (EC 4.2.99.9) - Escherichia coli (strain K-12) ALTERNATE_NAMES cystathionine gamma-synthase ORGANISM #formal_name Escherichia coli DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 01-Mar-2002 ACCESSIONS A01158; S40882; A26865; F65200 REFERENCE A01158 !$#authors Duchange, N.; Zakin, M.M.; Ferrara, P.; Saint-Girons, I.; !1Park, I.; Tran, S.V.; Py, M.C.; Cohen, G.N. !$#journal J. Biol. Chem. (1983) 258:14868-14871 !$#title Structure of the metJBLF cluster in Escherichia coli K12: !1Sequence of` the metB structural gene and of the 5'- and !13'-flanking regions of the metBL operon. !$#cross-references MUID:84087877; PMID:6361020 !$#accession A01158 !'##molecule_type DNA !'##residues 1-386 ##label DUC !'##cross-references GB:K01546; NID:g146842; PIDN:AAA24167.1; !1PID:g146846 !'##experimental_source strain K12 REFERENCE S40802 !$#authors Plunkett III, G.; Burland, V.; Daniels, D.L.; Blattner, F.R. !$#journal Nucleic Acids Res. (1993) 21:3391-3398 !$#title Analysis of the Escherichia coli genome. III. DNA sequence !1of the region from 87.2 to 89.2 minutes. !$#cross-references MUID:93347969; PMID:8346018 !$#accession S40882 !'##molecule_type DNA !'##residues 1-386 ##label PLU !'##cross-references EMBL:L19201; NID:g304961; PIDN:AAB03071.1; !1PID:g305042 REFERENCE A26865 !$#authors Martel, A.; de la Tour, C.B.; Le Goffic, F. !$#journal Biochem. Biophys. Res. Commun. (1987) 147:565-571 !$#title Pyridoxal 5'phosphate binding site of Escherichia coli beta !1cystathionase and cystathionine gamma synthase comparison of !1their sequences. !$#cross-references MUID:87326410; PMID:3307782 !$#accession A26865 !'##molecule_type DNA !'##residues 182-209 ##label MAR REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65200 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-386 ##label BLAT !'##cross-references GB:AE000468; GB:U00096; NID:g1790374; !1PIDN:AAC76921.1; PID:g1790375; UWGP:b3939 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene metB !$#map_position 89 min FUNCTION !$#description catalyzes the formation of cystathionine from !1succinylhomoserine and cysteine; it can also use hydrogen !1sulfide and methanethiol as substrates CLASSIFICATION #superfamily O-succinylhomoserine (thiol)-lyase KEYWORDS carbon-oxygen lyase; methionine biosynthesis; !1phosphoprotein; pyridoxal phosphate FEATURE !$198 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status experimental SUMMARY #length 386 #molecular-weight 41550 #checksum 1432 SEQUENCE /// ENTRY WZECCB #type complete TITLE cystathionine beta-lyase (EC 4.4.1.8) - Escherichia coli (strain K-12) ALTERNATE_NAMES beta-cystathionase; cystine lyase ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 01-Mar-2002 ACCESSIONS A25153; B26865; F65087 REFERENCE A25153 !$#authors Belfaiza, J.; Parsot, C.; Martel, A.; Bouthier De La Tour, !1C.; Margarita, D.; Cohen, G.N.; Saint-Girons, I. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:867-871 !$#title Evolution in biosynthetic pathways: two enzymes catalyzing !1consecutive steps in methionine biosynthesis originate from !1a common ancestor and possess a similar regulatory region. !$#cross-references MUID:86149241; PMID:3513164 !$#accession A25153 !'##molecule_type DNA !'##residues 1-395 ##label BEL !'##cross-references GB:M12858; NID:g146823; PIDN:AAA24158.1; !1PID:g146824 REFERENCE A26865 !$#authors Martel, A.; de la Tour, C.B.; Le Goffic, F. !$#journal Biochem. Biophys. Res. Commun. (1987) 147:565-571 !$#title Pyridoxal 5'phosphate binding site of Escherichia coli beta !1cystathionase and cystathionine gamma synthase comparison of !1their sequences. !$#cross-references MUID:87326410; PMID:3307782 !$#accession B26865 !'##molecule_type protein !'##residues 194-221 ##label MAR REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65087 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-395 ##label BLAT !'##cross-references GB:AE000383; GB:U00096; NID:g2367184; !1PIDN:AAC76044.1; PID:g1789383; UWGP:b3008 !'##experimental_source strain K-12, substrain MG1655 COMMENT This enzyme catalyzes the hydrolysis of cystathione to !1L-homocysteine, ammonia, and pyruvate; it is a pyridoxal !1phosphate protein also catalyzing reactions similar to the !1above using cysteine as substrate. GENETICS !$#gene metC !$#map_position 65 min CLASSIFICATION #superfamily O-succinylhomoserine (thiol)-lyase KEYWORDS carbon-sulfur lyase; methionine biosynthesis; !1phosphoprotein; pyridoxal phosphate FEATURE !$210 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 395 #molecular-weight 43212 #checksum 6834 SEQUENCE /// ENTRY A32412 #type complete TITLE DNA-(apurinic or apyrimidinic site) lyase (EC 4.2.99.18) endonuclease III [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES endonuclease III nth CONTAINS deoxyribodipyrimidine endonucleosidase (EC 3.2.2.17) ORGANISM #formal_name Escherichia coli DATE 04-Jun-1999 #sequence_revision 04-Jun-1999 #text_change 01-Mar-2002 ACCESSIONS A32412; C64920 REFERENCE A32412 !$#authors Asahara, H.; Wistort, P.M.; Bank, J.F.; Bakerian, R.H.; !1Cunningham, R.P. !$#journal Biochemistry (1989) 28:4444-4449 !$#title Purification and characterization of Escherichia coli !1endonuclease III from the cloned nth gene. !$#cross-references MUID:89352503; PMID:2669955 !$#accession A32412 !'##molecule_type DNA !'##residues 1-211 ##label ASA !'##cross-references GB:J02857; NID:g146971; PIDN:AAA24227.1; !1PID:g146972 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64920 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-211 ##label BLAT !'##cross-references GB:AE000258; GB:U00096; NID:g2367121; !1PIDN:AAC74705.1; PID:g1787920; UWGP:b1633 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A67876 !$#authors Thayer, M.M.; Tainer, J.A. !$#submission submitted to the Brookhaven Protein Data Bank, May 1995 !$#cross-references PDB:2ABK !$#contents annotation; X-ray crystallography, 1.85 angstroms, residues !11-211 REFERENCE A51015 !$#authors Kuo, C.F.; McRee, D.E.; Tainer, J.A. !$#submission submitted to the Brookhaven Protein Data Bank, September !11992 !$#cross-references PDB:1ABK !$#contents annotation; X-ray crystallography, 2.0 angstroms, residues !11-211 REFERENCE A58976 !$#authors Kuo, C.F.; McRee, D.E.; Fisher, C.L.; O'Handley, S.F.; !1Cunningham, R.P.; Tainer, J.A. !$#journal Science (1992) 258:434-440 !$#title Atomic structure of the DNA repair [4FE-4S] enzyme !1endonuclease III. !$#cross-references MUID:93030750; PMID:1411536 !$#contents annotation; X-ray crystallography, 2.0 angstroms GENETICS !$#gene nth FUNCTION DGL !$#description as deoxyribodipyrimidine endonucleosidase (EC 3.2.2.17), !1catalyzes cleavage of the 5'-pyrimidine N-glycosidic bond to !1deoxy-D-ribose at a cyclobutadipyrimidine (cross-linked !1pyrimidine dimer) in DNA FUNCTION APE !$#description as DNA-(apurinic or apyrimidinic site) lyase (EC 4.2.99.18), !1catalyzes beta-elimination cleavage of an apyrimidinic !1phosphodiester to produce 3'-terminal 1-oxo-4, !15-dihydroxy-2-pentene and 5'-terminal cyclobutadipyrimidine !1deoxyribose 5'-phosphate DNA !$#note the overall reaction, endonucleolytic cleavage of !1cross-linked pyrimidine dimers to make a 5'-phosphate !1product, has been described as a deoxyribonuclease !1(pyrimidine dimer) (EC 3.1.25.1) activity CLASSIFICATION #superfamily apurinic/apyrimidinic endonuclease III KEYWORDS 4Fe-4S; carbon-oxygen lyase; DNA repair; endonuclease; !1glycosidase; hydrolase; iron-sulfur protein; metalloprotein FEATURE !$187,194,197,203 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8experimental SUMMARY #length 211 #molecular-weight 23562 #checksum 7472 SEQUENCE /// ENTRY UFBSHS #type complete TITLE histidine ammonia-lyase (EC 4.3.1.3) hutH [similarity] - Bacillus subtilis ALTERNATE_NAMES histidase hutH ORGANISM #formal_name Bacillus subtilis DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 21-Jul-2000 ACCESSIONS S18810; C69643; T47089 REFERENCE S18808 !$#authors Oda, M.; Sugishita, A.; Furukawa, K. !$#journal J. Bacteriol. (1988) 170:3199-3205 !$#title Cloning and nucleotide sequences of histidase and regulatory !1genes in the Bacillus subtilis hut operon and positive !1regulation of the operon. !$#cross-references MUID:88257040; PMID:2454913 !$#accession S18810 !'##molecule_type DNA !'##residues 1-508 ##label ODA !'##cross-references EMBL:M20659; NID:g143074; PIDN:AAA22538.1; !1PID:g143076 !'##experimental_source strain 1A270 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69643 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-508 ##label KUN !'##cross-references GB:Z99124; GB:AL009126; NID:g2636442; !1PIDN:CAB15971.1; PID:g2636481 !'##experimental_source strain 168 REFERENCE Z24350 !$#authors Yoshida, K.; Sano, H.; Seki, S.; Oda, M.; Fujimura, M.; !1Fujita, Y. !$#journal Microbiology (1995) 141:337-343 !$#title Cloning and sequencing of a 29 kb region of the Bacillus !1subtilis genome containing the hut and wapA loci. !$#cross-references MUID:95219088; PMID:7704263 !$#accession T47089 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-508 ##label YOS !'##cross-references EMBL:D31856; NID:g603765; PIDN:BAA06644.1; !1PID:g603770 !'##experimental_source strain BGSC1A1 GENETICS !$#gene hutH FUNCTION !$#description catalyzes the formation of (E)-3- !1(1H-imidazol-4-yl)-propenoic acid (urocanic acid) and !1ammonia from histidine !$#pathway histidine catabolism CLASSIFICATION #superfamily Bacillus subtilis histidine ammonia-lyase KEYWORDS ammonia-lyase; carbon-nitrogen lyase; histidine catabolism FEATURE !$141-143 #cross-link 5-imidazolinone (Ala-Gly) #status !8predicted\ !$142 #modified_site dehydroalanine (Ser) #status predicted SUMMARY #length 508 #molecular-weight 55674 #checksum 9462 SEQUENCE /// ENTRY JC1172 #type complete TITLE histidine ammonia-lyase (EC 4.3.1.3) [validated] - Streptomyces griseus ALTERNATE_NAMES histidase ORGANISM #formal_name Streptomyces griseus DATE 14-May-1999 #sequence_revision 14-May-1999 #text_change 17-Mar-2000 ACCESSIONS JC1172; PC1104; B42299 REFERENCE JC1172 !$#authors Wu, P.C.; Kroening, T.A.; White, P.J.; Kendrick, K.E. !$#journal Gene (1992) 115:19-25 !$#title Histidine ammonia-lyase from Streptomyces griseus. !$#cross-references MUID:92307427; PMID:1612436 !$#accession JC1172 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-516 ##label WUP !'##experimental_source strain NRRL B-2682 !$#accession PC1104 !'##molecule_type protein !'##residues 1-12 ##label WU2 REFERENCE A42299 !$#authors Wu, P.C.; Kroening, T.A.; White, P.J.; Kendrick, K.E. !$#journal J. Bacteriol. (1992) 174:1647-1655 !$#title Purification of histidase from Streptomyces griseus and !1nucleotide sequence of the hutH structural gene. !$#cross-references MUID:92165741; PMID:1537807 !$#accession B42299 !'##molecule_type DNA !'##residues 1-516 ##label WUA !'##cross-references GB:M77841; NID:g153316; PIDN:AAA26769.1; !1PID:g153318 GENETICS !$#gene hutH FUNCTION !$#description EC 4.3.1.3; histidine ammonia-lyase; catalyzes the formation !1of (E)-3-(1H-imidazol-4-yl)-propenoic acid (urocanic acid) !1and ammonia from L-histidine [validated, MUID:92165741] !$#pathway histidine catabolism !$#note specific for L-histidine, shows no activity against !1D-histidine !$#note histidinol phosphate functions as competitive inhibitor; !1high concentrations of potassium cyanide inactivate !1histidase in the absence of its substrate or histidinol !1phosphate, suggesting that, as in other histidases, !1dehydroalanine plays an important role in catalysis CLASSIFICATION #superfamily Bacillus subtilis histidine ammonia-lyase KEYWORDS ammonia-lyase; carbon-nitrogen lyase FEATURE !$145-147 #cross-link 5-imidazolinone (Cys-Gly) #status !8predicted\ !$146 #modified_site dehydroalanine (Ser) #status predicted SUMMARY #length 516 #molecular-weight 53357 #checksum 9148 SEQUENCE /// ENTRY A35251 #type complete TITLE histidine ammonia-lyase (EC 4.3.1.3) - Pseudomonas putida ALTERNATE_NAMES histidase ORGANISM #formal_name Pseudomonas putida DATE 14-May-1999 #sequence_revision 14-May-1999 #text_change 18-Jun-1999 ACCESSIONS A35251; S39381 REFERENCE A35251 !$#authors Consevage, M.W.; Phillips, A.T. !$#journal J. Bacteriol. (1990) 172:2224-2229 !$#title Sequence analysis of the hutH gene encoding histidine !1ammonia-lyase in Pseudomonas putida. !$#cross-references MUID:90236871; PMID:2332400 !$#accession A35251 !'##molecule_type DNA !'##residues 1-510 ##label CON !'##cross-references GB:M35140; GB:M28873; NID:g151273; PIDN:AAA25840.1; !1PID:g151274 !'##experimental_source ATCC 12633 !'##note translation of initiation codon is not shown; part of this !1sequence, including the amino end of the mature protein, was !1determined by protein sequencing REFERENCE S39381 !$#authors Hernandez, D.; Stroh, J.G.; Phillips, A.T. !$#journal Arch. Biochem. Biophys. (1993) 307:126-132 !$#title Identification of Ser(143) as the site of modification in !1the active site of histidine ammonia-lyase. !$#cross-references MUID:94058243; PMID:8239649 !$#accession S39381 !'##molecule_type protein !'##residues 139-146 ##label HER REFERENCE A44705 !$#authors Langer, M.; Lieber, A.; Retey, J. !$#journal Biochemistry (1994) 33:14034-14038 !$#title Histidine ammonia-lyase mutant S143C is posttranslationally !1converted into fully active wild-type enzyme. Evidence for !1serine 143 to be the precursor of active site !1dehydroalanine. !$#cross-references MUID:95034846; PMID:7947813 !$#contents annotation !$#note mutational analysis; no chemical characterization REFERENCE A58958 !$#authors Schwede, T.F.; Retey, J.; Schulz, G.E. !$#journal Biochemistry (1999) 38:5355-5361 !$#title Crystal structure of histidine ammonia-lyase revealing a !1novel polypeptide modification as the catalytic !1electrophile. !$#cross-references MUID:99238310; PMID:10220322 !$#contents annotation; X-ray crystallography, 2.1 angstroms COMMENT The modification of serine to dehydroalanine coupled with !1the formation of 5-imidazolinone by the two neighboring !1residues produces the 4-methylidene-imidazole-5-one active !1site of some amino acid ammonia-lyases that differs by UV !1and mass spectrographic evidence from other known !1dehydroalanine containing peptides not containing the second !1modification. GENETICS !$#start_codon GTG FUNCTION !$#description catalyzes the formation of (E)-3- !1(1H-imidazol-4-yl)-propenoic acid (urocanic acid) and !1ammonia from histidine !$#pathway histidine catabolism CLASSIFICATION #superfamily Bacillus subtilis histidine ammonia-lyase KEYWORDS ammonia-lyase; carbon-nitrogen lyase; histidine catabolism FEATURE !$2-510 #product histidine ammonia-lyase #status experimental !8#label MAT\ !$143-145 #cross-link 5-imidazolinone (Ala-Gly) #status !8experimental\ !$144 #modified_site dehydroalanine (Ser) #status !8experimental SUMMARY #length 510 #molecular-weight 53708 #checksum 2261 SEQUENCE /// ENTRY IBHUN #type complete TITLE hydroxymethylbilane synthase (EC 4.3.1.8), nonerythroid long splice form [validated] - human ALTERNATE_NAMES porphobilinogen ammonia-lyase (polymerizing); porphobilinogen deaminase; pre-uroporphyrinogen synthase CONTAINS hydroxymethylbilane synthase, erythroid short splice form ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1988 #sequence_revision 02-Jul-1996 #text_change 08-Dec-2000 ACCESSIONS A45012; I60851; A26416; A25508; A60438; I60127 REFERENCE A45012 !$#authors Yoo, H.W.; Warner, C.A.; Chen, C.H.; Desnick, R.J. !$#journal Genomics (1993) 15:21-29 !$#title Hydroxymethylbilane synthase: complete genomic sequence and !1amplifiable polymorphisms in the human gene. !$#cross-references MUID:93162658; PMID:7916736 !$#accession A45012 !'##status preliminary; translation not shown; translated from GB/EMBL/ !1DDBJ !'##molecule_type DNA !'##residues 1-361 ##label RES !'##cross-references GB:M95623; NID:g292384; PIDN:AAA60029.1; !1PID:g292386 !$#accession I60851 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 18-361 ##label RE3 !'##cross-references GB:M95623; NID:g292384; PIDN:AAA60030.1; !1PID:g292385 REFERENCE A26416 !$#authors Grandchamp, B.; De Verneuil, H.; Beaumont, C.; Chretien, S.; !1Walter, O.; Nordmann, Y. !$#journal Eur. J. Biochem. (1987) 162:105-110 !$#title Tissue-specific expression of porphobilinogen deaminase: two !1isoenzymes from a single gene. !$#cross-references MUID:87133520; PMID:3816774 !$#accession A26416 !'##molecule_type mRNA !'##residues 1-176,'L',178-209,'K',211-361 ##label GRA !'##cross-references GB:X04808; NID:g35308; PIDN:CAA28499.1; PID:g35309 REFERENCE A25508 !$#authors Raich, N.; Romeo, P.H.; Dubart, A.; Beaupain, D.; !1Cohen-Solal, M.; Goossens, M. !$#journal Nucleic Acids Res. (1986) 14:5955-5968 !$#title Molecular cloning and complete primary sequence of human !1erythrocyte porphobilinogen deaminase. !$#cross-references MUID:86312872; PMID:2875434 !$#accession A25508 !'##molecule_type mRNA !'##residues 18-176,'L',178-348,'T',350-361 ##label RAI !'##cross-references GB:X04217; NID:g35306; PIDN:CAA27801.1; PID:g35307 REFERENCE A60438 !$#authors Lannfelt, L.; Wetterberg, L.; Lilius, L.; Thunell, S.; !1Joernvall, H.; Pavlu, B.; Wielburski, A.; Gellerfors, P. !$#journal Scand. J. Clin. Lab. Invest. (1989) 49:677-684 !$#title Porphobilinogen deaminase in human erythrocytes: !1purification of two forms with apparent molecular weights of !140 kDa and 42 kDa. !$#cross-references MUID:90117023; PMID:2609111 !$#accession A60438 !'##molecule_type protein !'##residues 18-36 ##label LAN !'##note this amino-terminal sequence represents a form from !1erythropoietic tissues REFERENCE I60127 !$#authors Chretien, S.; Dubart, A.; Beaupain, D.; Raich, N.; !1Grandchamp, B.; Rosa, J.; Goossens, M.; Romeo, P.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:6-10 !$#title Alternative transcription and splicing of the human !1porphobilinogen deaminase gene result either in !1tissue-specific or in housekeeping expression. !$#cross-references MUID:88124819; PMID:3422427 !$#accession I60127 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-11 ##label RE2 !'##cross-references GB:M18799; NID:g189641; PIDN:AAA60028.1; !1PID:g189644 GENETICS !$#gene GDB:HMBS; PBGD !'##cross-references GDB:120528; OMIM:176000 !$#map_position 11q22.3-11q22.3 !$#introns 11/3; 29/3; 54/1; 70/3; 89/2; 115/2; 141/2; 166/3; 204/3; !1217/3; 257/3; 275/3; 304/3 FUNCTION !$#description catalyzes the stepwise polymerization of four molecules of !1porphobilinogen to hydroxymethylbilane (uroporphyrinogen !1precursor) and four molecules of ammonia !$#pathway porphyrin biosynthesis !$#note acting with uroporphyrinogen-III synthase (cosynthase), !1which cyclizes hydroxymethylbilane, this enzyme produces !1uroporphyrinogen III the precursor for porphyrins CLASSIFICATION #superfamily hydroxymethylbilane synthase KEYWORDS alternative initiators; alternative splicing; ammonia-lyase; !1carbon-nitrogen lyase; porphyrin biosynthesis FEATURE !$1-361 #product hydroxymethylbilane synthase, nonerythroid !8splice form #status predicted #label NER\ !$18-361 #product hydroxymethylbilane synthase, erythroid !8splice form #status experimental #label ERY\ !$261 #modified_site dipyrrolylmethanemethyl (Cys) !8(covalent) #status predicted SUMMARY #length 361 #molecular-weight 39348 #checksum 7533 SEQUENCE /// ENTRY IBRTE #type complete TITLE hydroxymethylbilane synthase (EC 4.3.1.8), nonerythroid splice form - rat ALTERNATE_NAMES porphobilinogen deaminase; pre-uroporphyrinogen synthase CONTAINS hydroxymethylbilane synthase, erythroid splice form ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1992 #sequence_revision 09-Jun-2000 #text_change 19-Jan-2001 ACCESSIONS JE0285; S00746 REFERENCE JE0285 !$#authors Cardalda, C.A.; Batlle, A.; Juknat, A.A. !$#journal Biochem. Biophys. Res. Commun. (1998) 249:438-443 !$#title Sequence and structure of the rat housekeeping PBG-D !1isoform. !$#cross-references MUID:98380280; PMID:9712715 !$#accession JE0285 !'##status preliminary !'##molecule_type DNA !'##residues 1-361 ##label CAR !'##cross-references GB:Y12006; NID:g1911163; PIDN:CAA72734.1; !1PID:g1911164 REFERENCE S00746 !$#authors Stubnicer, A.C.; Picat, C.; Grandchamp, B. !$#journal Nucleic Acids Res. (1988) 16:3102 !$#title Rat porphobilinogen deaminase cDNA: nucleotide sequence of !1the erythropoietic form. !$#cross-references MUID:88217524; PMID:3368319 !$#accession S00746 !'##status translation not shown !'##molecule_type mRNA !'##residues 18-125,'EG',128-251,'D',253-361 ##label STU !'##cross-references EMBL:X06827; NID:g56855; PIDN:CAA29984.1; !1PID:g56856 FUNCTION !$#description catalyzes the stepwise polymerization of four molecules of !1porphobilinogen to hydroxymethylbilane (uroporphyrinogen !1precursor) and four molecules of ammonia !$#pathway porphyrin biosynthesis !$#note acting with uroporphyrinogen-III synthase (cosynthase), !1which cyclizes hydroxymethylbilane, this enzyme produces !1uroporphyrinogen III the precursor for porphyrins CLASSIFICATION #superfamily hydroxymethylbilane synthase KEYWORDS alternative splicing; ammonia-lyase; carbon-nitrogen lyase; !1porphyrin biosynthesis FEATURE !$261 #modified_site dipyrrolylmethanemethyl (Cys) !8(covalent) #status predicted SUMMARY #length 361 #molecular-weight 39361 #checksum 8449 SEQUENCE /// ENTRY IBMSN #type complete TITLE hydroxymethylbilane synthase (EC 4.3.1.8), nonerythropoietic - mouse ALTERNATE_NAMES porphobilinogen deaminase; pre-uroporphyrinogen synthase CONTAINS hydroxymethylbilane synthase, erythropoietic ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 12-Dec-1997 ACCESSIONS A36513 REFERENCE A36513 !$#authors Beaumont, C.; Porcher, C.; Picat, C.; Nordmann, Y.; !1Grandchamp, B. !$#journal J. Biol. Chem. (1989) 264:14829-14834 !$#title The mouse porphobilinogen deaminase gene. Structural !1organization, sequence, and transcriptional analysis. !$#cross-references MUID:89359283; PMID:2768242 !$#accession A36513 !'##molecule_type DNA !'##residues 1-361 ##label BEA !'##cross-references GB:J04981 FUNCTION !$#description catalyzes the stepwise polymerization of four molecules of !1porphobilinogen to hydroxymethylbilane (uroporphyrinogen !1precursor) and four molecules of ammonia !$#pathway porphyrin biosynthesis !$#note acting with uroporphyrinogen-III synthase (cosynthase), !1which cyclizes hydroxymethylbilane, this enzyme produces !1uroporphyrinogen III the precursor for porphyrins CLASSIFICATION #superfamily hydroxymethylbilane synthase KEYWORDS alternative splicing; ammonia-lyase; carbon-nitrogen lyase; !1porphyrin biosynthesis FEATURE !$1-361 #product hydroxymethylbilane synthase, !8nonerythropoietic #status predicted #label NER\ !$18-361 #product hydroxymethylbilane synthase, erythropoietic !8#status predicted #label ERY\ !$261 #modified_site dipyrrolylmethanemethyl (Cys) !8(covalent) #status predicted SUMMARY #length 361 #molecular-weight 39302 #checksum 8134 SEQUENCE /// ENTRY IBEG #type complete TITLE hydroxymethylbilane synthase (EC 4.3.1.8) precursor - Euglena gracilis ALTERNATE_NAMES porphobilinogen deaminase; pre-uroporphyrinogen synthase ORGANISM #formal_name Euglena gracilis DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS S06109 REFERENCE S06109 !$#authors Sharif, A.L.; Smith, A.G.; Abell, C. !$#journal Eur. J. Biochem. (1989) 184:353-359 !$#title Isolation and characterisation of a cDNA clone for a !1chlorophyll synthesis enzyme from Euglena gracilis. The !1chloroplast enzyme hydroxymethylbilane synthase !1(porphobilinogen deaminase) is synthesised with a very long !1transit peptide in Euglena. !$#cross-references MUID:90005485; PMID:2477247 !$#accession S06109 !'##molecule_type mRNA !'##residues 1-480 ##label SHA !'##cross-references GB:X15743; NID:g18411; PIDN:CAA33759.1; PID:g18412 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing !'##note 175-Ala was also found FUNCTION !$#description catalyzes the stepwise polymerization of four molecules of !1porphobilinogen to hydroxymethylbilane (uroporphyrinogen !1precursor) and four molecules of ammonia !$#pathway porphyrin biosynthesis !$#note acting with uroporphyrinogen-III synthase (cosynthase), !1which cyclizes hydroxymethylbilane, this enzyme produces !1uroporphyrinogen III the precursor for porphyrins CLASSIFICATION #superfamily hydroxymethylbilane synthase KEYWORDS ammonia-lyase; carbon-nitrogen lyase; chlorophyll !1biosynthesis; chloroplast; porphyrin biosynthesis FEATURE !$1-139 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$140-480 #product hydroxymethylbilane synthase #status !8experimental #label MAT\ !$395 #modified_site dipyrrolylmethanemethyl (Cys) !8(covalent) #status predicted SUMMARY #length 480 #molecular-weight 51743 #checksum 3402 SEQUENCE /// ENTRY IBEC #type complete TITLE hydroxymethylbilane synthase (EC 4.3.1.8) [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES porphobilinogen deaminase; pre-uroporphyrinogen synthase ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS F65184; A25512; S02226; S01306; S24974; S30695; S19283 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65184 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 'MIMTVTS',1-313 ##label BLAT !'##cross-references GB:AE000456; GB:U00096; NID:g2367291; !1PIDN:AAC76808.1; PID:g2367293; UWGP:b3805 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A25512 !$#authors Thomas, S.D.; Jordan, P.M. !$#journal Nucleic Acids Res. (1986) 14:6215-6226 !$#title Nucleotide sequence of the hemC locus encoding !1porphobilinogen deaminase of Escherichia coli K12. !$#cross-references MUID:86312890; PMID:3529035 !$#accession A25512 !'##molecule_type DNA !'##residues 1-185,'A',187-240,'A',242-260,'G',262-264,'A',266-313 !1##label THO !'##cross-references GB:X04242; NID:g41663; PIDN:CAA27813.1; PID:g41664; !1GB:M35827 !'##experimental_source strain K12 !'##note the authors translated the codon GCA for residue 241 as Gly and !1GGG for residue 261 as Ala REFERENCE S01693 !$#authors Alefounder, P.R.; Abell, C.; Battersby, A.R. !$#journal Nucleic Acids Res. (1988) 16:9871 !$#title The sequence of hemC, hemD and two additional E. coli genes. !$#cross-references MUID:89041586; PMID:3054815 !$#accession S02226 !'##status translation not shown !'##molecule_type DNA !'##residues 1-185,'A',187-264,'A',266-313 ##label ALE !'##cross-references EMBL:X12614; NID:g41665; PIDN:CAA31132.1; !1PID:g41666 REFERENCE S01306 !$#authors Jordan, P.M.; Thomas, S.D.; Warren, M.J. !$#journal Biochem. J. (1988) 254:427-435 !$#title Purification, crystallization and properties of !1porphobilinogen deaminase from a recombinant strain of !1Escherichia coli K12. !$#cross-references MUID:89025710; PMID:3052434 !$#accession S01306 !'##molecule_type protein !'##residues 1-10 ##label JOR REFERENCE S24974 !$#authors Glaser, P.; Sismeiro, O.; Danchin, A. !$#submission submitted to the EMBL Data Library, June 1992 !$#description Phylogeny of enterobacterial cya locus. !$#accession S24974 !'##molecule_type DNA !'##residues 1-89 ##label GLA !'##cross-references EMBL:X66782; NID:g41185; PIDN:CAA47279.1; !1PID:g41186 REFERENCE S30660 !$#authors Daniels, D.L.; Plunkett III, G.; Burland, V.; Blattner, F.R. !$#journal Science (1992) 257:771-778 !$#title Analysis of the Escherichia coli genome: DNA sequence of the !1region from 84.5 to 86.5 minutes. !$#cross-references MUID:92358234; PMID:1379743 !$#accession S30695 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 'MIMTVTS',1-50,'X',52-136,'G',138-299,'X',301-313 ##label !1DAN !'##cross-references EMBL:M87049 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1992 REFERENCE S19283 !$#authors Jordan, P.M.; Woodcock, S.C. !$#journal Biochem. J. (1991) 280:445-449 !$#title Mutagenesis of arginine residues in the catalytic cleft of !1Escherichia coli porphobilinogen deaminase that affects !1dipyrromethane cofactor assembly and tetrapyrrole chain !1initiation and elongation. !$#cross-references MUID:92082485; PMID:1747120 !$#accession S19283 !'##status preliminary !'##molecule_type DNA !'##residues 1-185,'A',187-264,'A',266-313 ##label JO2 GENETICS !$#gene hemC !$#map_position 85 min FUNCTION !$#description EC 4.3.1.8 [validated, MUID:92082485]; catalyzes the !1stepwise polymerization of four molecules of porphobilinogen !1to hydroxymethylbilane (uroporphyrinogen precursor) and four !1molecules of ammonia !$#pathway porphyrin biosynthesis !$#note cofactor dipyrromethane !$#note acting with uroporphyrinogen-III synthase (cosynthase), !1which cyclizes hydroxymethylbilane, this enzyme produces !1uroporphyrinogen III the precursor for porphyrins CLASSIFICATION #superfamily hydroxymethylbilane synthase KEYWORDS ammonia-lyase; carbon-nitrogen lyase; porphyrin biosynthesis FEATURE !$242 #modified_site dipyrrolylmethanemethyl (Cys) !8(covalent) #status experimental SUMMARY #length 313 #molecular-weight 33923 #checksum 6421 SEQUENCE /// ENTRY IBBS #type complete TITLE hydroxymethylbilane synthase (EC 4.3.1.8) - Bacillus subtilis ALTERNATE_NAMES porphobilinogen deaminase hemC; pre-uroporphyrinogen synthase ORGANISM #formal_name Bacillus subtilis DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jun-2000 ACCESSIONS C35252; A42728; E69639 REFERENCE A35252 !$#authors Petricek, M.; Rutberg, L.; Schroeder, I.; Hederstedt, L. !$#journal J. Bacteriol. (1990) 172:2250-2258 !$#title Cloning and characterization of the hemA region of the !1Bacillus subtilis chromosome. !$#cross-references MUID:90236876; PMID:2110138 !$#accession C35252 !'##molecule_type DNA !'##residues 1-314 ##label PET !'##cross-references GB:M57676; NID:g143034; PIDN:AAA22512.1; !1PID:g143037 REFERENCE A42728 !$#authors Hansson, M.; Rutberg, L.; Schroeder, I.; Hederstedt, L. !$#journal J. Bacteriol. (1991) 173:2590-2599 !$#title The Bacillus subtilis hemAXCDBL gene cluster, which encodes !1enzymes of the biosynthetic pathway from glutamate to !1uroporphyrinogen III. !$#cross-references MUID:91193218; PMID:1672867 !$#accession A42728 !'##molecule_type DNA !'##residues 185-314 ##label HAN !'##cross-references GB:M57676 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69639 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-314 ##label KUN !'##cross-references GB:Z99118; GB:AL009126; NID:g2635200; !1PIDN:CAB14775.1; PID:g2635280 !'##experimental_source strain 168 GENETICS !$#gene hemC FUNCTION !$#description catalyzes the stepwise polymerization of four molecules of !1porphobilinogen to hydroxymethylbilane (uroporphyrinogen !1precursor) and four molecules of ammonia !$#pathway porphyrin biosynthesis !$#note acting with uroporphyrinogen-III synthase (cosynthase), !1which cyclizes hydroxymethylbilane, this enzyme produces !1uroporphyrinogen III the precursor for porphyrins CLASSIFICATION #superfamily hydroxymethylbilane synthase KEYWORDS ammonia-lyase; carbon-nitrogen lyase; porphyrin biosynthesis FEATURE !$242 #modified_site dipyrrolylmethanemethyl (Cys) !8(covalent) #status predicted SUMMARY #length 314 #molecular-weight 34838 #checksum 6196 SEQUENCE /// ENTRY DUAGO #type complete TITLE ornithine cyclodeaminase (EC 4.3.1.12) [validated] - Agrobacterium sp. plasmid pTiC58 ORGANISM #formal_name Agrobacterium sp. DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 17-Mar-2000 ACCESSIONS S00402 REFERENCE S00402 !$#authors Sans, N.; Schindler, U.; Schroeder, J. !$#journal Eur. J. Biochem. (1988) 173:123-130 !$#title Ornithine cyclodeaminase from Ti plasmid C58. DNA sequence, !1enzyme properties and regulation of activity by arginine. !$#cross-references MUID:88185308; PMID:3281832 !$#accession S00402 !'##molecule_type DNA !'##residues 1-354 ##label SAN !'##cross-references EMBL:X07435; NID:g39107; PIDN:CAA30316.1; !1PID:g39108 GENETICS !$#gene ocd !$#genome plasmid pTiC58 FUNCTION !$#description EC 4.3.1.12 [validated, MUID:88185308]; ornithine !1cyclodeaminase; catalyzes the conversion of L-ornithine to !1L-proline and ammonia !$#note regulated by L-arginine !$#note cofactor NAD+ CLASSIFICATION #superfamily ornithine cyclodeaminase KEYWORDS ammonia-lyase; carbon-nitrogen lyase; opine catabolism SUMMARY #length 354 #molecular-weight 38984 #checksum 6812 SEQUENCE /// ENTRY WZHURS #type complete TITLE argininosuccinate lyase (EC 4.3.2.1) - human ALTERNATE_NAMES argininosuccinase ORGANISM #formal_name Homo sapiens #common_name man DATE 17-Mar-1987 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS A31658; S01010; S02824; A01160; I59118 REFERENCE A31658 !$#authors Todd, S.; McGill, J.R.; McCombs, J.L.; Moore, C.M.; Weider, !1I.; Naylor, S.L. !$#journal Genomics (1989) 4:53-59 !$#title cDNA sequence, interspecies comparison, and gene mapping !1analysis of argininosuccinate lyase. !$#cross-references MUID:89122032; PMID:2644168 !$#accession A31658 !'##molecule_type mRNA !'##residues 1-464 ##label TOD !'##cross-references GB:J03058; NID:g179088; PIDN:AAA51787.1; !1PID:g179089 REFERENCE S01010 !$#authors Matuo, S.; Tatsuno, M.; Kobayashi, K.; Saheki, T.; Miyata, !1T.; Iwanaga, S.; Amaya, Y.; Mori, M. !$#journal FEBS Lett. (1988) 234:395-399 !$#title Isolation of cDNA clones of human argininosuccinate lyase !1and corrected amino acid sequence. !$#cross-references MUID:88271664; PMID:3391281 !$#accession S01010 !'##molecule_type mRNA !'##residues 1-464 ##label MAT !'##cross-references EMBL:Y00753 !'##note part of this sequence was confirmed by protein sequencing REFERENCE S02824 !$#authors Takeyori, S. !$#submission submitted to the EMBL Data Library, August 1988 !$#accession S02824 !'##molecule_type mRNA !'##residues 1-430,'R',432-464 ##label TAK !'##cross-references EMBL:Y00753; NID:g28877; PIDN:CAA68722.1; !1PID:g28878 REFERENCE A01160 !$#authors O'Brien, W.E.; McInnes, R.; Kalumuck, K.; Adcock, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:7211-7215 !$#title Cloning and sequence analysis of cDNA for human !1argininosuccinate lyase. !$#cross-references MUID:87016917; PMID:3463959 !$#accession A01160 !'##molecule_type mRNA !'##residues 1-386,'PTRLRESC',395,'HGRDQG',402,'RPQPAVTAGAADHQP',418, !1'VLGRRDLR',427,'GLRAQCGAVWCPGRHC',444,'LQRRLAD',453-463 !1##label OBR !'##cross-references GB:M14218 REFERENCE I59118 !$#authors Piatigorsky, J.; O'Brien, W.E.; Norman, B.L.; Kalumuck, K.; !1Wistow, G.J.; Borras, T.; Nickerson, J.M.; Wawrousek, E.F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:3479-3483 !$#title Gene sharing by delta-crystallin and argininosuccinate !1lyase. !$#cross-references MUID:88217924; PMID:3368457 !$#accession I59118 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 5-97 ##label RES !'##cross-references GB:M21007; NID:g179085; PIDN:AAA35566.1; !1PID:g179087 COMMENT The active enzyme catalyzes the formation of arginine and !1fumarate from argininosuccinate, the last step in arginine !1biosynthesis. This enzyme also functions in the urea cycle !1for the disposal of ingested nitrogen. GENETICS !$#gene GDB:ASL !'##cross-references GDB:119703; OMIM:207900 !$#map_position 7q21.3-7q22 !$#introns 69/3 !$#note the list of introns may be incomplete CLASSIFICATION #superfamily argininosuccinate lyase KEYWORDS amidine-lyase; arginine biosynthesis; carbon-nitrogen lyase; !1homotetramer; urea cycle SUMMARY #length 464 #molecular-weight 51743 #checksum 187 SEQUENCE /// ENTRY WZRTRS #type complete TITLE argininosuccinate lyase (EC 4.3.2.1) - rat ALTERNATE_NAMES argininosuccinase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jun-2000 ACCESSIONS A32188; A41416; A60057 REFERENCE A32188 !$#authors Matsubasa, T.; Takiguchi, M.; Amaya, Y.; Matsuda, I.; Mori, !1M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:592-596 !$#title Structure of the rat argininosuccinate lyase gene: close !1similarity to chicken delta-crystallin genes. !$#cross-references MUID:89098976; PMID:2789519 !$#accession A32188 !'##molecule_type DNA !'##residues 1-461 ##label MAT !'##cross-references GB:M22697; GB:J04159; NID:g203006; PIDN:AAA40766.1; !1PID:g203008 REFERENCE A41416 !$#authors Amaya, Y.; Matsubasa, T.; Takiguchi, M.; Kobayashi, K.; !1Saheki, T.; Kawamoto, S.; Mori, M. !$#journal J. Biochem. (1988) 103:177-181 !$#title Amino acid sequence of rat argininosuccinate lyase deduced !1from cDNA. !$#cross-references MUID:88198099; PMID:2834354 !$#accession A41416 !'##molecule_type mRNA !'##residues 1-461 ##label AMA !'##cross-references GB:M22697; GB:D00209; NID:g203006; PIDN:AAA40766.1; !1PID:g203008 !'##experimental_source liver, strain Wistar REFERENCE A60057 !$#authors Kawamoto, S.; Kaneko, T.; Mizuki, N.; Ohsuga, A.; Fukushima, !1J.; Amaya, Y.; Mori, M.; Okuda, K. !$#journal Brain Res. Mol. Brain Res. (1989) 5:235-241 !$#title Molecular cloning and nucleotide sequence of rat brain !1argininosuccinate lyase cDNA with an extremely long !15'-untranslated sequence: evidence for the identity of the !1brain and liver enzymes. !$#cross-references MUID:89260944; PMID:2725197 !$#accession A60057 !'##molecule_type mRNA !'##residues 1-128,'C',130-300,'G',302-461 ##label KAW !'##cross-references GB:D13978; NID:g220660; PIDN:BAA03088.1; !1PID:g220661 !'##experimental_source brain, strain Sprague-Dawley !'##note the authors attribute the two amino acid sequence differences !1from the hepatic sequence to microheterogeneity of the gene !1rather than the presence of multiple genes COMMENT The active enzyme catalyzes the formation of arginine and !1fumarate from argininosuccinate, the last step in arginine !1biosynthesis. This enzyme also functions in the urea cycle !1for the disposal of ingested nitrogen. GENETICS !$#introns 4/3; 69/3; 97/3; 116/3; 149/2; 175/2; 201/2; 219/1; 240/1; !1278/2; 306/3; 326/3; 354/3; 381/3; 417/2 CLASSIFICATION #superfamily argininosuccinate lyase KEYWORDS amidine-lyase; arginine biosynthesis; carbon-nitrogen lyase; !1homotetramer; urea cycle SUMMARY #length 461 #molecular-weight 51549 #checksum 9561 SEQUENCE /// ENTRY CYDKD2 #type complete TITLE delta-2-crystallin - duck CONTAINS argininosuccinate lyase (EC 4.3.2.1) ORGANISM #formal_name Anas platyrhynchos #common_name domestic duck DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 28-Jul-2000 ACCESSIONS JU0453; S53527; S53528 REFERENCE JU0452 !$#authors Wistow, G.J.; Piatigorsky, J. !$#journal Gene (1990) 96:263-270 !$#title Gene conversion and splice-site slippage in the !1argininosuccinate lyases/delta-crystallins of the duck lens: !1members of an enzyme superfamily. !$#cross-references MUID:91099685; PMID:2269436 !$#accession JU0453 !'##molecule_type mRNA !'##residues 1-468 ##label WIS !'##cross-references GB:M35132; NID:g213086; PID:g213087 REFERENCE S53527 !$#authors Li, X.; Wistow, G.J.; Piatigorsky, J. !$#journal Biochim. Biophys. Acta (1995) 1261:25-34 !$#title Linkage and expression of the argininosuccinate lyase/ !1delta-crystallin genes of the duck: insertion of a CR1 !1element in the intergenic spacer. !$#cross-references MUID:95200970; PMID:7893758 !$#accession S53527 !'##status preliminary !'##molecule_type DNA !'##residues 1-6 ##label LIX !'##cross-references EMBL:U06050; NID:g455116; PIDN:AAA83403.1; !1PID:g1122905 !$#accession S53528 !'##status preliminary; translation not shown !'##molecule_type DNA !'##residues 56-75 ##label LI2 !'##cross-references EMBL:U05895; NID:g455114; PIDN:AAA83149.1; !1PID:g455115 COMMENT Delta crystallin, the principal crystallin in embryonic !1lens, is found only in birds and reptiles. In the lens of !1the embryonic duck, two delta crystallins (delta-1 and !1delta-2) are found in equal abundance. Both proteins are !1argininosuccinate lyase homologs; only delta-2 crystallin is !1thought to be enzymatically active. GENETICS !$#introns 71/3 !$#note the list of introns may be incomplete CLASSIFICATION #superfamily argininosuccinate lyase KEYWORDS amidine-lyase; arginine biosynthesis; carbon-nitrogen lyase; !1embryo; eye lens; tetramer SUMMARY #length 468 #molecular-weight 51735 #checksum 1244 SEQUENCE /// ENTRY CYDKD1 #type complete TITLE delta-1-crystallin - duck ALTERNATE_NAMES argininosuccinate lyase homolog ORGANISM #formal_name Anas platyrhynchos #common_name domestic duck DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Aug-2000 ACCESSIONS JU0452; A27544; S51526 REFERENCE JU0452 !$#authors Wistow, G.J.; Piatigorsky, J. !$#journal Gene (1990) 96:263-270 !$#title Gene conversion and splice-site slippage in the !1argininosuccinate lyases/delta-crystallins of the duck lens: !1members of an enzyme superfamily. !$#cross-references MUID:91099685; PMID:2269436 !$#accession JU0452 !'##molecule_type mRNA !'##residues 1-466 ##label WIS !'##cross-references GB:M35133; NID:g213088; PIDN:AAC31659.1; !1PID:g213089 REFERENCE A27544 !$#authors Piatigorsky, J.; Norman, B.; Jones, R.E. !$#journal J. Mol. Evol. (1987) 25:308-317 !$#title Conservation of delta-crystallin gene structure between !1ducks and chickens. !$#cross-references MUID:88036069; PMID:2822941 !$#accession A27544 !'##molecule_type DNA !'##residues 1-2,'XX',5-54 ##label PIA !'##cross-references EMBL:M35133 REFERENCE S51526 !$#authors Lee, H.J.; Lin, C.C.; Chiou, S.H.; Chang, G.G. !$#journal Arch. Biochem. Biophys. (1994) 314:31-38 !$#title Characterization of the multiple forms of duck lens !1delta-crystallin with endogenous argininosuccinate lyase !1activity. !$#cross-references MUID:95031083; PMID:7944404 !$#accession S51526 !'##status preliminary !'##molecule_type protein !'##residues 8-10,'Q',12-17,'X',19-21 ##label LEE COMMENT Delta crystallin, the principal crystallin in embryonic !1lens, is found only in birds and reptiles. In the lens of !1the embryonic duck, two delta crystallins (delta-1 and !1delta-2) are found in equal abundance. Both proteins are !1argininosuccinate lyase homologs; delta-1 crystallin !1probably functions mainly as a crystallin rather than as an !1enzyme. CLASSIFICATION #superfamily argininosuccinate lyase KEYWORDS embryo; eye lens SUMMARY #length 466 #molecular-weight 51135 #checksum 1640 SEQUENCE /// ENTRY CYCHD2 #type complete TITLE delta-2-crystallin - chicken ALTERNATE_NAMES argininosuccinate lyase (EC 4.3.2.1) ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS A25622; I50635 REFERENCE A25622 !$#authors Nickerson, J.M.; Wawrousek, E.F.; Borras, T.; Hawkins, J.W.; !1Norman, B.L.; Filpula, D.R.; Nagle, J.W.; Ally, A.H.; !1Piatigorsky, J. !$#journal J. Biol. Chem. (1986) 261:552-557 !$#title Sequence of the chicken delta-2 crystallin gene and its !1intergenic spacer. Extreme homology with the delta-1 !1crystallin gene. !$#cross-references MUID:86085878; PMID:3941090 !$#accession A25622 !'##molecule_type DNA !'##residues 1-466 ##label NIC !'##cross-references GB:M10806; NID:g211671; PIDN:AAA48727.1; !1PID:g211673 REFERENCE I50634 !$#authors Borras, T.; Nickerson, J.M.; Chepelinsky, A.B.; Piatigorsky, !1J. !$#journal EMBO J. (1985) 4:445-452 !$#title Structural and functional evidence for differential promoter !1activity of the two linked delta-crystallin genes in the !1chicken. !$#cross-references MUID:85257474; PMID:4018032 !$#accession I50635 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-4 ##label BOR !'##cross-references EMBL:X02188; NID:g63352; PIDN:CAA26129.1; !1PID:g584485 COMMENT Delta crystallin, the principal crystallin in embryonic !1lens, is found only in birds and reptiles. In the lens of !1the embryonic chicken, two closely related genes encode for !1delta crystallin. One gene (delta-1) is expressed more !1abundantly than the other (delta-2). Both proteins are !1homologous with argininosuccinate lyases from other species; !1delta-2 crystallin is thought to be the argininosuccinate !1lyase. GENETICS !$#introns 4/3; 69/3; 97/3; 116/3; 149/2; 175/2; 201/2; 219/1; 240/1; !1278/2; 306/3; 326/3; 354/3; 381/3; 417/2 CLASSIFICATION #superfamily argininosuccinate lyase KEYWORDS amidine-lyase; arginine biosynthesis; carbon-nitrogen lyase; !1embryo; eye lens; tetramer SUMMARY #length 466 #molecular-weight 51043 #checksum 1030 SEQUENCE /// ENTRY CYCHD #type complete TITLE delta-1-crystallin - chicken ALTERNATE_NAMES argininosuccinate lyase homolog ORGANISM #formal_name Gallus gallus #common_name chicken DATE 13-Jun-1983 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS A25712; A23017; A25755; A01162; I50634; A24357 REFERENCE A25712 !$#authors Nickerson, J.M.; Wawrousek, E.F.; Hawkins, J.W.; Wakil, !1A.S.; Wistow, G.J.; Thomas, G.; Norman, B.L.; Piatigorsky, !1J. !$#journal J. Biol. Chem. (1985) 260:9100-9105 !$#title The complete sequence of the chicken delta-1 crystallin gene !1and its 5' flanking region. !$#cross-references MUID:85261287; PMID:3839507 !$#accession A25712 !'##molecule_type DNA !'##residues 1-466 ##label NIC !'##cross-references GB:M10806; NID:g211671; PIDN:AAA48726.1; !1PID:g211672 !'##note the authors translated the codon GTT for residue 345 as Ala REFERENCE A23017 !$#authors Ohno, M.; Sakamoto, H.; Yasuda, K.; Okada, T.S.; Shimura, Y. !$#journal Nucleic Acids Res. (1985) 13:1593-1606 !$#title Nucleotide sequence of a chicken Delta-crystallin gene. !$#cross-references MUID:85215567; PMID:2987831 !$#accession A23017 !'##molecule_type DNA !'##residues 1-466 ##label OHN !'##cross-references GB:X02222; NID:g63341; PIDN:CAA26144.1; PID:g313705 !'##note the authors translated the codon CTG for residue 455 as Asp REFERENCE A25755 !$#authors Nickerson, J.M.; Piatigorsky, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:2611-2615 !$#title Sequence of a complete chicken delta-crystallin cDNA. !$#cross-references MUID:84194056; PMID:6585817 !$#accession A25755 !'##molecule_type mRNA !'##residues 1-344,'A',346-442,'H',444-445,'AA' ##label NIC2 !'##cross-references GB:J00843; NID:g211678; PIDN:AAA48728.1; !1PID:g211679 REFERENCE A01162 !$#authors Yasuda, K.; Nakajima, N.; Isobe, T.; Okada, T.S.; Shimura, !1Y. !$#journal EMBO J. (1984) 3:1397-1402 !$#title The nucleotide sequence of a complete chicken !1delta-crystallin cDNA. !$#cross-references MUID:84261433; PMID:6547670 !$#accession A01162 !'##molecule_type mRNA !'##residues 2-117,'L',119-128,'T',130-273,'F',275-344,'A',346-347,'E', !1349-445,'AA' ##label YAS !'##cross-references GB:K03257; NID:g336495; PIDN:AAA51616.1; !1PID:g459706 REFERENCE A24357 !$#authors Hayashi, S.; Kondoh, H.; Yasuda, K.; Soma, G.; Ikawa, Y.; !1Okada, T.S. !$#journal EMBO J. (1985) 4:2201-2207 !$#title Tissue-specific regulation of a chicken delta-crystallin !1gene in mouse cells: involvement of the 5' end region. !$#cross-references MUID:86081725; PMID:3000763 !$#contents annotation; tissue-specific regulation of expression REFERENCE I50634 !$#authors Borras, T.; Nickerson, J.M.; Chepelinsky, A.B.; Piatigorsky, !1J. !$#journal EMBO J. (1985) 4:445-452 !$#title Structural and functional evidence for differential promoter !1activity of the two linked delta-crystallin genes in the !1chicken. !$#cross-references MUID:85257474; PMID:4018032 !$#accession I50634 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-4 ##label BOR !'##cross-references EMBL:X02187; NID:g63351; PIDN:CAA26128.1; !1PID:g584484 COMMENT Delta crystallin, the principal crystallin in embryonic !1lens, is found only in birds and reptiles. In the lens of !1the embryonic chicken, two closely related genes encode for !1delta crystallin. One gene (delta-1) is expressed more !1abundantly than the other (delta-2) in lens. Although the !1sequences of both proteins are homologous with that of !1argininosuccinate lyase, delta-1 crystallin does not appear !1to have full enzyme activity. GENETICS !$#introns 4/3; 69/3; 97/3; 116/3; 149/2; 175/2; 201/2; 219/1; 240/1; !1278/2; 306/3; 326/3; 354/3; 381/3; 417/2 CLASSIFICATION #superfamily argininosuccinate lyase KEYWORDS blocked amino end; embryo; eye lens; tetramer FEATURE !$2-466 #product delta-1 crystallin #status experimental !8#label MAT\ !$2 #modified_site blocked amino end (Ala) (in mature !8form) #status experimental SUMMARY #length 466 #molecular-weight 50795 #checksum 4126 SEQUENCE /// ENTRY WZBYRS #type complete TITLE argininosuccinate lyase (EC 4.3.2.1) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES argininosuccinase; protein YHR018c ORGANISM #formal_name Saccharomyces cerevisiae DATE 17-Mar-1987 #sequence_revision 19-Jul-1996 #text_change 23-Mar-2001 ACCESSIONS S46792; A01161; B31658 REFERENCE S46774 !$#authors Du, Z. !$#submission submitted to the EMBL Data Library, June 1994 !$#description The sequence of S. cerevisiae cosmid L2825. !$#accession S46792 !'##molecule_type DNA !'##residues 1-463 ##label DUZ !'##cross-references EMBL:U10400; NID:g500701; PIDN:AAB68946.1; !1PID:g500711; GSPDB:GN00008; MIPS:YHR018c REFERENCE A01161 !$#authors Beacham, I.R.; Schweitzer, B.W.; Warrick, H.M.; Carbon, J. !$#journal Gene (1984) 29:271-279 !$#title The nucleotide sequence of the yeast ARG4 gene. !$#cross-references MUID:85028448; PMID:6386606 !$#accession A01161 !'##molecule_type DNA !'##residues 1-102,'E',104-463 ##label BEA !'##cross-references GB:K01813; NID:g171078; PIDN:AAA34434.1; !1PID:g171079 REFERENCE A31658 !$#authors Todd, S.; McGill, J.R.; McCombs, J.L.; Moore, C.M.; Weider, !1I.; Naylor, S.L. !$#journal Genomics (1989) 4:53-59 !$#title cDNA sequence, interspecies comparison, and gene mapping !1analysis of argininosuccinate lyase. !$#cross-references MUID:89122032; PMID:2644168 !$#accession B31658 !'##molecule_type mRNA !'##residues 1-102,'E',104-463 ##label TOD GENETICS !$#gene SGD:ARG4; MIPS:YHR018c !'##cross-references SGD:S0001060; MIPS:YHR018c !$#map_position 8R FUNCTION !$#description catalyzes formation of arginine and fumarate from !1argininosuccinate !$#pathway arginine biosynthesis !$#note last step CLASSIFICATION #superfamily argininosuccinate lyase KEYWORDS amidine-lyase; arginine biosynthesis; carbon-nitrogen lyase; !1homotetramer SUMMARY #length 463 #molecular-weight 51989 #checksum 3106 SEQUENCE /// ENTRY WZPSLP #type complete TITLE lactoylglutathione lyase (EC 4.4.1.5) - Pseudomonas putida ALTERNATE_NAMES glyoxalase I ORGANISM #formal_name Pseudomonas putida DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jun-2000 ACCESSIONS JU0070 REFERENCE JU0070 !$#authors Rhee, H.I.; Sato, N.; Murata, K.; Kimura, A. !$#journal Agric. Biol. Chem. (1988) 52:2243-2246 !$#title Nucleotide sequence of the glyoxalase I gene of Pseudomonas !1putida. !$#accession JU0070 !'##molecule_type DNA !'##residues 1-164 ##label RHE !'##cross-references DDBJ:D00342; NID:g216885; PIDN:BAA00248.1; !1PID:g216886 !'##experimental_source strain IFO 3738 !'##note the amino-terminal 9 residues of the purified enzyme were !1sequenced COMMENT The enzyme contains one zinc atom. COMMENT This enzyme catalyzes the conversion of hemimercaptal, !1formed from methylglyoxal and glutathione, to !1S-lactoylglutathione. CLASSIFICATION #superfamily lactoylglutathione lyase KEYWORDS carbon-sulfur lyase; zinc FEATURE !$2-164 #product lactoylglutathione lyase #status predicted !8#label MAT SUMMARY #length 164 #molecular-weight 18443 #checksum 7239 SEQUENCE /// ENTRY T07596 #type complete TITLE 1-aminocyclopropane-1-carboxylate synthase (EC 4.4.1.14) 1A - tomato ALTERNATE_NAMES ACC synthase; S-adenosyl-L-methionine methylthioadenosine-lyase ORGANISM #formal_name Lycopersicon esculentum #common_name tomato DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 03-Dec-1999 ACCESSIONS T07596 REFERENCE Z16039 !$#authors Oono, Y.; Nguyen, M.D.; Hennig, L.; Yu, G.; Rottoman, W.H.; !1Campbell, A.D.; Lincoln, J.E.; Theologis, A. !$#submission submitted to the EMBL Data Library, September 1996 !$#description LE-ACS1A and LE-ACS1B, duplicated genes encoding !11-aminocyclopropane-1-carboxylate synthase in tomato !1(Lycopersicon esculentum). !$#accession T07596 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-485 ##label OON !'##cross-references EMBL:U72389; NID:g1621640; PIDN:AAB17278.1; !1PID:g1621641 !'##experimental_source cultivar Rutgers; clone pLEACS1A3 GENETICS !$#gene ACS1A FUNCTION !$#description catalyzes the conversion of S-adenosylmethionine to !11-aminocyclopropane-1-carboxylate and methylthioadenosine !$#pathway ethylene biosynthesis CLASSIFICATION #superfamily 1-aminocyclopropane-1-carboxylate synthase KEYWORDS carbon-sulfur lyase; ethylene biosynthesis; phosphoprotein; !1pyridoxal phosphate; S-adenosylmethionine FEATURE !$279 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 485 #molecular-weight 54779 #checksum 6426 SEQUENCE /// ENTRY T07601 #type complete TITLE 1-aminocyclopropane-1-carboxylate synthase (EC 4.4.1.14) 1B - tomato ALTERNATE_NAMES ACC synthase; S-adenosyl-L-methionine methylthioadenosine-lyase ORGANISM #formal_name Lycopersicon esculentum #common_name tomato DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 03-Dec-1999 ACCESSIONS T07601 REFERENCE Z16039 !$#authors Oono, Y.; Nguyen, M.D.; Hennig, L.; Yu, G.; Rottoman, W.H.; !1Campbell, A.D.; Lincoln, J.E.; Theologis, A. !$#submission submitted to the EMBL Data Library, September 1996 !$#description LE-ACS1A and LE-ACS1B, duplicated genes encoding !11-aminocyclopropane-1-carboxylate synthase in tomato !1(Lycopersicon esculentum). !$#accession T07601 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-483 ##label OON !'##cross-references EMBL:U72390; NID:g1621642; PIDN:AAB17279.1; !1PID:g1621643 !'##experimental_source cultivar Rutgers; clone pLEACS1B4 GENETICS !$#gene ACS1B FUNCTION !$#description catalyzes the conversion of S-adenosylmethionine to !11-aminocyclopropane-1-carboxylate and methylthioadenosine !$#pathway ethylene biosynthesis CLASSIFICATION #superfamily 1-aminocyclopropane-1-carboxylate synthase KEYWORDS carbon-sulfur lyase; ethylene biosynthesis; phosphoprotein; !1pyridoxal phosphate; S-adenosylmethionine FEATURE !$279 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 483 #molecular-weight 54547 #checksum 3564 SEQUENCE /// ENTRY T04315 #type complete TITLE 1-aminocyclopropane-1-carboxylate synthase (EC 4.4.1.14) - tomato ALTERNATE_NAMES ACC synthase; S-adenosyl-L-methionine methylthioadenosine-lyase ORGANISM #formal_name Lycopersicon esculentum #common_name tomato DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 16-Jun-2000 ACCESSIONS T04315 REFERENCE Z15278 !$#authors Nakajima, N.; Bae, G.; Saji, H.; Aono, M.; Kubo, A.; Kondo, !1N. !$#submission submitted to the EMBL Data Library, April 1998 !$#description Rapid accumulations of transcripts of ethylene biosynthesis !1enzymes in ozone-treated tomato leaves. !$#accession T04315 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-477 ##label NAK !'##cross-references EMBL:AB013346; PIDN:BAA25916.1 !'##experimental_source tissue-type green leaves FUNCTION !$#description catalyzes the conversion of S-adenosylmethionine to !11-aminocyclopropane-1-carboxylate and methylthioadenosine !$#pathway ethylene biosynthesis CLASSIFICATION #superfamily 1-aminocyclopropane-1-carboxylate synthase KEYWORDS carbon-sulfur lyase; ethylene biosynthesis; phosphoprotein; !1pyridoxal phosphate; S-adenosylmethionine FEATURE !$269 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 477 #molecular-weight 53926 #checksum 6742 SEQUENCE /// ENTRY S19677 #type complete TITLE 1-aminocyclopropane-1-carboxylate synthase (EC 4.4.1.14) 2 - tomato ALTERNATE_NAMES ACC synthase; S-adenosyl-L-methionine methylthioadenosine-lyase ORGANISM #formal_name Lycopersicon esculentum #common_name tomato DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 03-Dec-1999 ACCESSIONS S19677; S19678; S24358; B36201; A35516; A41985; B33103 REFERENCE S19677 !$#authors Rottmann, W.H.; Peter, G.F.; Oeller, P.W.; Keller, J.A.; !1Shen, N.F.; Nagy, B.P.; Taylor, L.P.; Campbell, A.D.; !1Theologis, A. !$#journal J. Mol. Biol. (1991) 222:937-961 !$#title 1-aminocyclopropane-1-carboxylate synthase in tomato is !1encoded by a multigene family whose transcription is induced !1during fruit and floral senescence. !$#cross-references MUID:92106351; PMID:1762159 !$#accession S19677 !'##molecule_type DNA !'##residues 1-485 ##label ROT !'##cross-references EMBL:X59139; NID:g19165; PIDN:CAA41855.1; !1PID:g19166 !'##genetics ACC !$#accession S19678 !'##molecule_type mRNA !'##residues 1-123,'V',125-485 ##label ROW !'##cross-references EMBL:X59145; NID:g19167; PIDN:CAA41856.1; !1PID:g19168 REFERENCE S24358 !$#authors Li, N.; Wiesman, Z.; Liu, D.; Mattoo, A.K. !$#journal FEBS Lett. (1992) 306:103-107 !$#title A functional tomato ACC synthase expressed in Escherichia !1coli demonstrates suicidal inactivation by its substrate !1S-adenosylmethionine. !$#cross-references MUID:92339529; PMID:1633863 !$#accession S24358 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type mRNA !'##residues 9-485 ##label LIN !'##cross-references EMBL:X62536; NID:g19163; PIDN:CAA44397.1; !1PID:g19164 !'##experimental_source cv. Pik-Red !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1991 REFERENCE A36201 !$#authors Yip, W.K.; Dong, J.G.; Kenny, J.W.; Thompson, G.A.; Yang, !1S.F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:7930-7934 !$#title Characterization and sequencing of the active site of !11-aminocyclopropane-1-carboxylate synthase. !$#cross-references MUID:91045911; PMID:2122449 !$#accession B36201 !'##molecule_type protein !'##residues 275-286 ##label YIP REFERENCE A35516 !$#authors Van Der Straeten, D.; Van Wiemeersch, L.; Goodman, H.M.; Van !1Montagu, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:4859-4863 !$#title Cloning and sequence of two different cDNAs encoding !11-aminocyclopropane-1-carboxylate synthase in tomato. !$#cross-references MUID:90280476; PMID:2191304 !$#accession A35516 !'##molecule_type mRNA !'##residues 1-321,'P',323-398,'L',400-485 ##label VAN !'##cross-references GB:M34289; NID:g170363; PIDN:AAA81580.1; !1PID:g170364 REFERENCE A41985 !$#authors Yip, W.K.; Moore, T.; Yang, S.F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:2475-2479 !$#title Differential accumulation of transcripts for four tomato !11-aminocyclopropane-1-carboxylate synthase homologs under !1various conditions. !$#cross-references MUID:92196141; PMID:1549612 !$#accession A41985 !'##molecule_type mRNA !'##residues 208-310 ##label YI2 !'##note sequence extracted from NCBI backbone (NCBIN:88505, !1NCBIP:88522) GENETICS ACC !$#gene ACC2 !$#introns 57/3; 100/3; 154/2 FUNCTION !$#description catalyzes the conversion of S-adenosylmethionine to !11-aminocyclopropane-1-carboxylate and methylthioadenosine !$#pathway ethylene biosynthesis CLASSIFICATION #superfamily 1-aminocyclopropane-1-carboxylate synthase KEYWORDS carbon-sulfur lyase; ethylene biosynthesis; phosphoprotein; !1pyridoxal phosphate; S-adenosylmethionine FEATURE !$278 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status experimental SUMMARY #length 485 #molecular-weight 54662 #checksum 3667 SEQUENCE /// ENTRY S19679 #type complete TITLE 1-aminocyclopropane-1-carboxylate synthase (EC 4.4.1.14) 4 - tomato ALTERNATE_NAMES ACC synthase; S-adenosyl-L-methionine methylthioadenosine-lyase ORGANISM #formal_name Lycopersicon esculentum #common_name tomato DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 03-Dec-1999 ACCESSIONS S19679; D41985; A48760; A40960; B35516 REFERENCE S19677 !$#authors Rottmann, W.H.; Peter, G.F.; Oeller, P.W.; Keller, J.A.; !1Shen, N.F.; Nagy, B.P.; Taylor, L.P.; Campbell, A.D.; !1Theologis, A. !$#journal J. Mol. Biol. (1991) 222:937-961 !$#title 1-aminocyclopropane-1-carboxylate synthase in tomato is !1encoded by a multigene family whose transcription is induced !1during fruit and floral senescence. !$#cross-references MUID:92106351; PMID:1762159 !$#accession S19679 !'##molecule_type mRNA !'##residues 1-476 ##label ROT !'##cross-references EMBL:X59146; NID:g19169; PIDN:CAA41857.1; !1PID:g19170 !'##note the authors designated this gene LE-ACC4 REFERENCE A41985 !$#authors Yip, W.K.; Moore, T.; Yang, S.F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:2475-2479 !$#title Differential accumulation of transcripts for four tomato !11-aminocyclopropane-1-carboxylate synthase homologs under !1various conditions. !$#cross-references MUID:92196141; PMID:1549612 !$#accession D41985 !'##molecule_type mRNA !'##residues 228-314 ##label YIP !'##note sequence extracted from NCBI backbone (NCBIN:88520, !1NCBIP:88530) REFERENCE A48760 !$#authors Lincoln, J.E.; Campbell, A.D.; Oetiker, J.; Rottmann, W.H.; !1Oeller, P.W.; Shen, N.F.; Theologis, A. !$#journal J. Biol. Chem. (1993) 268:19422-19430 !$#title LE-ACS4, a fruit ripening and wound-induced !11-aminocyclopropane-1-carboxylate synthase gene of tomato !1(Lycopersicon esculentum). Expression in Escherichia coli, !1structural characterization, expression characteristics, and !1phylogenetic analysis. !$#cross-references MUID:93374928; PMID:8366090 !$#accession A48760 !'##molecule_type DNA !'##residues 1-14,'V',16-252,'S',254-476 ##label LIN !'##cross-references GB:M88487; NID:g397696; PIDN:AAA03164.1; !1PID:g397697 !'##note the authors designated this gene LE-ACS4 REFERENCE A40960 !$#authors Olson, D.C.; White, J.A.; Edelman, L.; Harkins, R.N.; Kende, !1H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:5340-5344 !$#title Differential expression of two genes for !11-aminocyclopropane-1-carboxylate synthase in tomato fruits. !$#cross-references MUID:91271385; PMID:1711229 !$#accession A40960 !'##molecule_type mRNA !'##residues 1-14,'V',16-252,'S',254-476 ##label OLS !'##cross-references GB:M63490; NID:g170359; PIDN:AAA34131.1; !1PID:g170360 !'##note the authors designated this gene ACCSYN2 REFERENCE A35516 !$#authors Van Der Straeten, D.; Van Wiemeersch, L.; Goodman, H.M.; Van !1Montagu, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:4859-4863 !$#title Cloning and sequence of two different cDNAs encoding !11-aminocyclopropane-1-carboxylate synthase in tomato. !$#cross-references MUID:90280476; PMID:2191304 !$#accession B35516 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 20-81,'A',83-159 ##label VAN !'##cross-references GB:M34289 !'##experimental_source clone pcVV4B GENETICS !$#gene ACS4; ACCSYN2; ACC4 !$#introns 106/3; 160/2 !$#note at least six related ACC synthase genes exist in this !1species; this locus is induced by ripening but not by !1wounding FUNCTION !$#description catalyzes the conversion of S-adenosylmethionine to !11-aminocyclopropane-1-carboxylate and methylthioadenosine !$#pathway ethylene biosynthesis CLASSIFICATION #superfamily 1-aminocyclopropane-1-carboxylate synthase KEYWORDS carbon-sulfur lyase; ethylene biosynthesis; phosphoprotein; !1pyridoxal phosphate; S-adenosylmethionine FEATURE !$282 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 476 #molecular-weight 53519 #checksum 6026 SEQUENCE /// ENTRY A41141 #type complete TITLE 1-aminocyclopropane-1-carboxylate synthase (EC 4.4.1.14) 1A - zucchini ALTERNATE_NAMES ACC synthase; S-adenosyl-L-methionine methylthioadenosine-lyase ORGANISM #formal_name Cucurbita pepo var. melopepo #common_name zucchini DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 03-Dec-1999 ACCESSIONS A41141; A38649 REFERENCE A41141 !$#authors Huang, P.L.; Parks, J.E.; Rottmann, W.H.; Theologis, A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:7021-7025 !$#title Two genes encoding 1-aminocyclopropane-1-carboxylate !1synthase in zucchini (Cucurbita pepo) are clustered and !1similar but differentially regulated. !$#cross-references MUID:91334397; PMID:1871117 !$#accession A41141 !'##molecule_type mRNA !'##residues 1-493 ##label HUA !'##cross-references GB:M61195; NID:g167493; PIDN:AAA33111.1; !1PID:g167494 REFERENCE A38649 !$#authors Sato, T.; Oeller, P.W.; Theologis, A. !$#journal J. Biol. Chem. (1991) 266:3752-3759 !$#title The 1-aminocyclopropane-1-carboxylate synthase of Cucurbita. !1Purification, properties, expression in Escherichia coli, !1and primary structure determination by DNA sequence !1analysis. !$#cross-references MUID:91139670; PMID:1995630 !$#accession A38649 !'##molecule_type mRNA !'##residues 1-176,'G',178-493 ##label SAT !'##cross-references GB:M58323; NID:g167496; PIDN:AAA33113.1; !1PID:g167497 GENETICS !$#gene ACCIA COMPLEX homodimer FUNCTION !$#description catalyzes the conversion of S-adenosylmethionine to !11-aminocyclopropane-1-carboxylate and methylthioadenosine !$#pathway ethylene biosynthesis CLASSIFICATION #superfamily 1-aminocyclopropane-1-carboxylate synthase KEYWORDS carbon-sulfur lyase; ethylene biosynthesis; homodimer; !1phosphoprotein; pyridoxal phosphate; S-adenosylmethionine FEATURE !$279 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 493 #molecular-weight 55878 #checksum 8346 SEQUENCE /// ENTRY B41141 #type complete TITLE 1-aminocyclopropane-1-carboxylate synthase (EC 4.4.1.14) 1B - zucchini ALTERNATE_NAMES ACC synthase; S-adenosyl-L-methionine methylthioadenosine-lyase ORGANISM #formal_name Cucurbita pepo var. melopepo #common_name zucchini DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 03-Dec-1999 ACCESSIONS B41141 REFERENCE A41141 !$#authors Huang, P.L.; Parks, J.E.; Rottmann, W.H.; Theologis, A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:7021-7025 !$#title Two genes encoding 1-aminocyclopropane-1-carboxylate !1synthase in zucchini (Cucurbita pepo) are clustered and !1similar but differentially regulated. !$#cross-references MUID:91334397; PMID:1871117 !$#accession B41141 !'##status preliminary; nucleic acid sequence not shown; not compared !1with conceptual translation !'##molecule_type mRNA !'##residues 1-494 ##label HUA !'##cross-references GB:M61195 GENETICS !$#gene ACCIB FUNCTION !$#description catalyzes the conversion of S-adenosylmethionine to !11-aminocyclopropane-1-carboxylate and methylthioadenosine !$#pathway ethylene biosynthesis CLASSIFICATION #superfamily 1-aminocyclopropane-1-carboxylate synthase KEYWORDS carbon-sulfur lyase; ethylene biosynthesis; phosphoprotein; !1pyridoxal phosphate; S-adenosylmethionine FEATURE !$279 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 494 #molecular-weight 55922 #checksum 1797 SEQUENCE /// ENTRY A57540 #type complete TITLE 1-aminocyclopropane-1-carboxylate synthase (EC 4.4.1.14) 3 - tomato (strain VFNT) ALTERNATE_NAMES ACC synthase; S-adenosyl-L-methionine methylthioadenosine-lyase ORGANISM #formal_name Lycopersicon esculentum #common_name tomato DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 03-Dec-1999 ACCESSIONS A57540; B41985; A36201; A33103 REFERENCE A57540 !$#authors Olson, D.C.; Oetiker, J.H.; Yang, S.F. !$#journal J. Biol. Chem. (1995) 270:14056-14061 !$#title Analysis of LE-ACS3, a 1-aminocyclopropane-1-carboxylic acid !1synthase gene expressed during flooding in the roots of !1tomato plants. !$#cross-references MUID:95294010; PMID:7775465 !$#accession A57540 !'##molecule_type DNA !'##residues 1-469 ##label OLS !'##cross-references GB:L34171; NID:g508608; PIDN:AAA78789.1; !1PID:g508609 !'##experimental_source strain VFNT REFERENCE A41985 !$#authors Yip, W.K.; Moore, T.; Yang, S.F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:2475-2479 !$#title Differential accumulation of transcripts for four tomato !11-aminocyclopropane-1-carboxylate synthase homologs under !1various conditions. !$#cross-references MUID:92196141; PMID:1549612 !$#accession B41985 !'##molecule_type mRNA !'##residues 201-219,'V',221-304 ##label YIP !'##note sequence extracted from NCBI backbone (NCBIN:88509, !1NCBIP:88527) REFERENCE A36201 !$#authors Yip, W.K.; Dong, J.G.; Kenny, J.W.; Thompson, G.A.; Yang, !1S.F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:7930-7934 !$#title Characterization and sequencing of the active site of !11-aminocyclopropane-1-carboxylate synthase. !$#cross-references MUID:91045911; PMID:2122449 !$#accession A36201 !'##molecule_type protein !'##residues 269-280 ##label YI2 GENETICS !$#gene ACS3 !$#introns 49/3; 93/3; 147/2 FUNCTION !$#description catalyzes the conversion of S-adenosylmethionine to !11-aminocyclopropane-1-carboxylate and methylthioadenosine !$#pathway ethylene biosynthesis CLASSIFICATION #superfamily 1-aminocyclopropane-1-carboxylate synthase KEYWORDS carbon-sulfur lyase; ethylene biosynthesis; phosphoprotein; !1pyridoxal phosphate; S-adenosylmethionine FEATURE !$272 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status experimental SUMMARY #length 469 #molecular-weight 53094 #checksum 6225 SEQUENCE /// ENTRY T10889 #type complete TITLE 1-aminocyclopropane-1-carboxylate synthase (EC 4.4.1.14) 6 - mung bean ALTERNATE_NAMES ACC synthase; S-adenosyl-L-methionine methylthioadenosine-lyase ORGANISM #formal_name Vigna radiata #common_name mung bean DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 21-Jul-2000 ACCESSIONS T10889; T10842 REFERENCE Z17198 !$#authors Yoon, I.; Mori, H.; Kim, J.; Kang, B.; Imaseki, H. !$#journal Plant Cell Physiol. (1997) 38:217-224 !$#title VR-ACS6 is an auxin-inducible !11-aminocyclopropane-1-carboxylate synthas e gene in mung !1bean (Vigna radiata). !$#cross-references MUID:97294927; PMID:9150600 !$#accession T10889 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-472 ##label YOO !'##cross-references EMBL:AB000679; NID:g1813330; PIDN:BAA19161.1; !1PID:g1813331 REFERENCE Z17182 !$#authors Kim, W. !$#submission submitted to the EMBL Data Library, August 1995 !$#accession T10842 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-37,'Q',39-124,'E',126-389,'QE',392-425,'NG',428-442,'T', !1444-472 ##label KIM !'##cross-references EMBL:U34986; NID:g1006804; PID:g1006805 !'##experimental_source tissue_type etiolated hypocotyls GENETICS !$#gene ACS6 FUNCTION !$#description catalyzes the conversion of S-adenosylmethionine to !11-aminocyclopropane-1-carboxylate and methylthioadenosine !$#pathway ethylene biosynthesis CLASSIFICATION #superfamily 1-aminocyclopropane-1-carboxylate synthase KEYWORDS carbon-sulfur lyase; ethylene biosynthesis; phosphoprotein; !1pyridoxal phosphate; S-adenosylmethionine FEATURE !$275 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 472 #molecular-weight 53572 #checksum 3230 SEQUENCE /// ENTRY OYBY #type complete TITLE adenylate cyclase (EC 4.6.1.1) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES ATP pyrophosphate-lyase; protein J1401; protein YJL005w ORGANISM #formal_name Saccharomyces cerevisiae DATE 28-Dec-1987 #sequence_revision 08-Sep-1995 #text_change 21-Jan-2000 ACCESSIONS S56776; S56775; A24776; S05828; S55183 REFERENCE S56776 !$#authors To Van, D.; Perea, J.; Jacq, C. !$#submission submitted to the Protein Sequence Database, September 1995 !$#accession S56776 !'##molecule_type DNA !'##residues 1-1823 ##label DEH !'##cross-references EMBL:Z49280; GSPDB:GN00010; MIPS:YJL005w REFERENCE S56771 !$#authors de Haan, M.; Grivell, L.A.; Smits, P.H.M. !$#submission submitted to the Protein Sequence Database, September 1995 !$#accession S56775 !'##molecule_type DNA !'##residues 673-2026 ##label ZAG !'##cross-references EMBL:Z49280; GSPDB:GN00010; MIPS:YJL005w REFERENCE A24776 !$#authors Kataoka, T.; Broek, D.; Wigler, M. !$#journal Cell (1985) 43:493-505 !$#title DNA sequence and characterization of the S. cerevisiae gene !1encoding adenylate cyclase. !$#cross-references MUID:86079531; PMID:2934138 !$#accession A24776 !'##molecule_type DNA !'##residues 1-261,'L',263-547,'L',549-591,'H',593-708,'I',710-961,'P', !1963-1387,'S',1389-1565,'S',1567-1734,'G',1736-1995,'F', !11997-2026 ##label KAT !'##cross-references EMBL:M12057; NID:g171359; PIDN:AAA34549.1; !1PID:g171360 !'##note the authors translated the codon TTA for residue 262 as Ser, !1ACG for residue 311 as Ser, CTT for residue 548 as Ser, CAT !1for residue 592 as Asp, GAC for residue 915 as Ala, CCT for !1residue 962 as Leu, TCA for residue 1566 as Ala, GAG for !1residue 1659 as Ala, GGT for residue 1735 as Val, and TTC !1for residue 1996 as Cys REFERENCE S05828 !$#authors Masson, P.; Lenzen, G.; Jacquemin, J.M.; Danchin, A. !$#journal Curr. Genet. (1986) 10:343-352 !$#title Yeast adenylate cyclase catalytic domain is carboxy !1terminal. !$#cross-references MUID:88165073; PMID:3327602 !$#accession S05828 !'##molecule_type DNA !'##residues 1042-1426,'D',1428-1460,'T',1462-1955,'V',1957-2008,'M', !12014-2015,'TNFYKWLRTQRIYQLEFCS' ##label MAS !'##cross-references EMBL:X03449; NID:g3487; PIDN:CAA27175.1; PID:g3488 REFERENCE S55183 !$#authors de Haan, M.; Smits, P.H.M.; Grivell, L.A. !$#submission submitted to the EMBL Data Library, May 1995 !$#accession S55183 !'##molecule_type DNA !'##residues 673-2026 ##label DEW !'##cross-references EMBL:X87611; NID:g854567; PIDN:CAA60917.1; !1PID:g854568 GENETICS !$#gene SGD:CYR1; CDC35; MIPS:YJL005w !'##cross-references SGD:S0003542; MIPS:YJL005w !$#map_position 10L CLASSIFICATION #superfamily yeast adenylate cyclase; leucine-rich !1alpha-2-glycoprotein repeat homology; yeast adenylate !1cyclase catalytic domain homology KEYWORDS cAMP biosynthesis; duplication; phosphorus-oxygen lyase; !1tandem repeat FEATURE !$669-1343 #region leucine-rich 23-residue repeats\ !$1065-1087 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR\ !$1610-2026 #domain catalytic #status predicted #label CAT\ !$1664-1749 #domain yeast adenylate cyclase catalytic domain !8homology #label YACC SUMMARY #length 2026 #molecular-weight 227832 #checksum 2243 SEQUENCE /// ENTRY OYBYK #type complete TITLE adenylate cyclase (EC 4.6.1.1) - yeast (Saccharomyces kluyveri) ALTERNATE_NAMES adenylyl cyclase ORGANISM #formal_name Saccharomyces kluyveri DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 21-Jan-2000 ACCESSIONS JQ1145; S14464 REFERENCE JQ1145 !$#authors Young, D.; O'Neill, K.; Broek, D.; Wigler, M. !$#journal Gene (1991) 102:129-132 !$#title The adenylyl cyclase-encoding gene from Saccharomyces !1kluyveri. !$#cross-references MUID:91323718; PMID:1864503 !$#accession JQ1145 !'##molecule_type DNA !'##residues 1-1839 ##label YOU !'##cross-references EMBL:X56042; NID:g4856; PIDN:CAA39513.1; PID:g4857 GENETICS !$#gene CYR1 CLASSIFICATION #superfamily yeast adenylate cyclase; leucine-rich !1alpha-2-glycoprotein repeat homology; yeast adenylate !1cyclase catalytic domain homology KEYWORDS cAMP biosynthesis; duplication; phosphorus-oxygen lyase FEATURE !$1006-1029 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR\ !$1479-1564 #domain yeast adenylate cyclase catalytic domain !8homology #label YACC SUMMARY #length 1839 #molecular-weight 206894 #checksum 8814 SEQUENCE /// ENTRY OYEC #type complete TITLE adenylate cyclase (EC 4.6.1.1) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 19-Feb-1984 #sequence_revision 10-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS G65184; A01163; S24975; S30696 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65184 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-848 ##label BLAT !'##cross-references GB:AE000456; GB:U00096; NID:g2367291; !1PIDN:AAC76809.1; PID:g1790238; UWGP:b3806 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A93552 !$#authors Aiba, H.; Mori, K.; Tanaka, M.; Ooi, T.; Roy, A.; Danchin, !1A. !$#journal Nucleic Acids Res. (1984) 12:9427-9440 !$#title The complete nucleotide sequence of the adenylate cyclase !1gene of Escherichia coli. !$#cross-references MUID:85087947; PMID:6393056 !$#accession A01163 !'##molecule_type DNA !'##residues 1-222,'G',224-848 ##label AIB !'##cross-references GB:X01653; GB:J01599; GB:K02969; GB:M68875; !1GB:V00271; NID:g41182; PIDN:CAA25817.1; PID:g581057 REFERENCE S24974 !$#authors Glaser, P.; Sismeiro, O.; Danchin, A. !$#submission submitted to the EMBL Data Library, June 1992 !$#description Phylogeny of enterobacterial cya locus. !$#accession S24975 !'##molecule_type DNA !'##residues 1-222,'G',224-848 ##label GLA REFERENCE S30660 !$#authors Daniels, D.L.; Plunkett III, G.; Burland, V.; Blattner, F.R. !$#journal Science (1992) 257:771-778 !$#title Analysis of the Escherichia coli genome: DNA sequence of the !1region from 84.5 to 86.5 minutes. !$#cross-references MUID:92358234; PMID:1379743 !$#accession S30696 !'##molecule_type DNA !'##residues 1-848 ##label DAN !'##cross-references EMBL:M87049; NID:g836656; PIDN:AAA67602.1; !1PID:g148205 COMMENT This enzyme has a carboxyl-terminal regulatory domain !1involved in the regulation of cyclase activity by the carbon !1source and an amino-terminal catalytic domain. GENETICS !$#gene cyaA !$#map_position 85 min FUNCTION !$#description catalyzes the irreversible formation of cAMP and !1pyrophosphate from ATP CLASSIFICATION #superfamily adenylate cyclase KEYWORDS cAMP biosynthesis; phosphoprotein; phosphorus-oxygen lyase FEATURE !$2-828 #product adenylate cyclase #status predicted #label !8MAT SUMMARY #length 848 #molecular-weight 97585 #checksum 8055 SEQUENCE /// ENTRY A39833 #type complete TITLE adenylate cyclase (EC 4.6.1.1) type III - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 31-Mar-2000 ACCESSIONS A39833 REFERENCE A39833 !$#authors Bakalyar, H.A.; Reed, R.R. !$#journal Science (1990) 250:1403-1406 !$#title Identification of a specialized adenylyl cyclase that may !1mediate odorant detection. !$#cross-references MUID:91075227; PMID:2255909 !$#accession A39833 !'##molecule_type mRNA !'##residues 1-1144 ##label BAK !'##cross-references GB:M55075; NID:g202714; PIDN:AAA40677.1; !1PID:g202715 CLASSIFICATION #superfamily human adenylate cyclase; guanylate cyclase !1catalytic domain homology KEYWORDS glycoprotein; olfaction; phosphorus-oxygen lyase; !1transmembrane protein FEATURE !$258-496 #domain guanylate cyclase catalytic domain homology !8#label GCC1\ !$871-1123 #domain guanylate cyclase catalytic domain homology !8#label GCC2\ !$158,734,827 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1144 #molecular-weight 128935 #checksum 17 SEQUENCE /// ENTRY D42088 #type complete TITLE adenylate cyclase (EC 4.6.1.1), Ca2+/calmodulin-responsive - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES rutabaga protein ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS D42088 REFERENCE A42088 !$#authors Levin, L.R.; Han, P.L.; Hwang, P.M.; Feinstein, P.G.; Davis, !1R.L.; Reed, R.R. !$#journal Cell (1992) 68:479-489 !$#title The Drosophila learning and memory gene rutabaga encodes a !1Ca2+/Calmodulin-responsive adenylyl cyclase. !$#cross-references MUID:92154664; PMID:1739965 !$#accession D42088 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-2248 ##label LEV !'##cross-references GB:M81887; NID:g158194; PIDN:AAA28844.1; !1PID:g158195 !'##note sequence extracted from NCBI backbone (NCBIP:82229) GENETICS !$#gene FlyBase:rut !'##cross-references FlyBase:FBgn0003301 CLASSIFICATION #superfamily Drosophila adenylate cyclase; guanylate cyclase !1catalytic domain homology KEYWORDS phosphorus-oxygen lyase; transmembrane protein FEATURE !$218-452 #domain guanylate cyclase catalytic domain homology !8#label GCC1\ !$910-1155 #domain guanylate cyclase catalytic domain homology !8#label GCC2 SUMMARY #length 2248 #molecular-weight 248899 #checksum 5492 SEQUENCE /// ENTRY OYFKQ #type complete TITLE adenylate cyclase (EC 4.6.1.1) - Brevibacterium liquefaciens ORGANISM #formal_name Brevibacterium liquefaciens DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 18-Jun-1999 ACCESSIONS S15273 REFERENCE S15273 !$#authors Peters, E.P.; Wilderspin, A.F.; Wood, S.P.; Zvelebil, !1M.J.J.M.; Sezer, O.; Danchin, A. !$#journal Mol. Microbiol. (1991) 5:1175-1181 !$#title A pyruvate-stimulated adenylate cyclase has a sequence !1related to the fes/fps oncogenes and to eukaryotic cyclases. !$#cross-references MUID:92065813; PMID:1683468 !$#accession S15273 !'##molecule_type DNA !'##residues 1-403 ##label PET !'##cross-references EMBL:X57541; NID:g48831; PIDN:CAA40760.1; !1PID:g48832 GENETICS !$#gene cya CLASSIFICATION #superfamily Brevibacterium liquefaciens adenylate cyclase KEYWORDS cAMP biosynthesis; dimer; phosphorus-oxygen lyase SUMMARY #length 403 #molecular-weight 43898 #checksum 7328 SEQUENCE /// ENTRY JS0029 #type complete TITLE adenylate cyclase (EC 4.6.1.1) precursor, calmodulin-sensitive - Bacillus anthracis ALTERNATE_NAMES anthrax toxin edema factor ORGANISM #formal_name Bacillus anthracis DATE 31-Mar-1992 #sequence_revision 11-Nov-1994 #text_change 19-Jan-2001 ACCESSIONS JS0029; PS0307; JS0602 REFERENCE JS0029 !$#authors Robertson, D.L.; Tippetts, M.T.; Leppla, S.H. !$#journal Gene (1988) 73:363-371 !$#title Nucleotide sequence of the Bacillus anthracis edema factor !1gene (cya): a calmodulin-dependent adenylate cyclase. !$#cross-references MUID:89211974; PMID:3149607 !$#accession JS0029 !'##molecule_type DNA !'##residues 1-800 ##label ROB !'##cross-references GB:M24074; NID:g142812; PIDN:AAA79215.1; !1PID:g142813 !$#accession PS0307 !'##molecule_type protein !'##residues 34-48 ##label RO2 REFERENCE JS0033 !$#authors Escuyer, V.; Duflot, E.; Sezer, O.; Danchin, A.; Mock, M. !$#journal Gene (1988) 71:293-298 !$#title Structural homology between virulence-associated bacterial !1adenylate cyclases. !$#cross-references MUID:89138004; PMID:2906312 !$#accession JS0602 !'##molecule_type DNA !'##residues 1-349,'V',351-509,'Q',511,'EW',514-800 ##label ESC !'##cross-references GB:M23179; NID:g142814; PIDN:AAA22374.1; !1PID:g142815 COMMENT This enzyme is activated by calmodulin and increases the !1intracellular cAMP concentration. GENETICS !$#gene cya CLASSIFICATION #superfamily calmodulin-sensitive adenylate cyclase; !1calmodulin-sensitive adenylate cyclase catalytic domain !1homology; lethal factor amino-terminal homology KEYWORDS nucleotide binding; P-loop; phosphorus-oxygen lyase; toxin FEATURE !$1-33 #domain signal sequence #status predicted #label SIG\ !$34-800 #product adenylate cyclase, calmodulin-sensitive !8#status predicted #label MAT\ !$34-286 #domain lethal factor amino-terminal homology #label !8LFA\ !$303-607 #domain calmodulin-sensitive adenylate cyclase !8catalytic domain homology #label ADE\ !$313-323 #region calmodulin binding #status predicted\ !$347-354 #region nucleotide-binding motif A (P-loop) SUMMARY #length 800 #molecular-weight 92452 #checksum 1971 SEQUENCE /// ENTRY JQ0032 #type complete TITLE anthrax toxin lethal factor pXO1-107 precursor - Bacillus anthracis virulence plasmid pXO1 ORGANISM #formal_name Bacillus anthracis DATE 31-Mar-1990 #sequence_revision 11-Nov-1994 #text_change 11-May-2000 ACCESSIONS JQ0032; C59104 REFERENCE JQ0032 !$#authors Bragg, T.S.; Robertson, D.L. !$#journal Gene (1989) 81:45-54 !$#title Nucleotide sequence and analysis of the lethal factor gene !1(lef) from Bacillus anthracis. !$#cross-references MUID:90034185; PMID:2509294 !$#accession JQ0032 !'##molecule_type DNA !'##residues 1-809 ##label BRA !'##cross-references GB:M29081; NID:g143143; PIDN:AAA79216.1; !1PID:g143144 REFERENCE A59091 !$#authors Okinaka, R.T.; Cloud, K.; Hampton, O.; Hoffmaster, A.R.; !1Hill, K.K.; Keim, P.; Koehler, T.M.; Lamke, G.; Kumano, S.; !1Mahillon, J.; Manter, D.; Martinez, Y.; Ricke, D.; Svensson, !1R.; Jackson, P.J. !$#journal J. Bacteriol. (1999) 181:6509-6515 !$#title Sequence and organization of pXO1, the large Bacillus !1anthracis plasmid harboring the Anthrax toxin genes. !$#cross-references MUID:99445483; PMID:10515943 !$#accession C59104 !'##molecule_type DNA !'##residues 1-809 ##label OKI !'##cross-references GB:AF065404; NID:g4894216; PIDN:AAD32411.1; !1PID:g4894323 !'##experimental_source strain Sterne !'##note similar to Anthrax toxin lethal factor precursor; lef, plasmid !1pXO1, B. anthracis (P15917, M29081, M30210) COMMENT This lethal factor of Bacillus anthracis is part of the !1tripartite protein exotoxin along with the protective !1antigen and the edema factor. Separately the proteins are !1not toxic, but together they cause anthrax, an infectious !1and often fatal disease of cattle, sheep, and other mammals. GENETICS !$#gene lef; pXO1-107 !$#genome plasmid CLASSIFICATION #superfamily anthrax toxin lethal factor; lethal factor !1amino-terminal homology KEYWORDS toxin FEATURE !$1-33 #domain signal sequence #status predicted #label SIG\ !$34-809 #product anthrax toxin lethal factor #status !8predicted #label MAT\ !$44-295 #domain lethal factor amino-terminal homology #label !8LFA SUMMARY #length 809 #molecular-weight 93786 #checksum 871 SEQUENCE /// ENTRY S23097 #type complete TITLE guanylate cyclase (EC 4.6.1.2), soluble, 70K chain - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 20-Apr-2000 ACCESSIONS S23097 REFERENCE S23097 !$#authors Giuili, G.; Scholl, U.; Bulle, F.; Guellaen, G. !$#journal FEBS Lett. (1992) 304:83-88 !$#title Molecular cloning of the cDNAs coding for the two subunits !1of soluble guanylyl cyclase from human brain. !$#cross-references MUID:92316204; PMID:1352257 !$#accession S23097 !'##molecule_type mRNA !'##residues 1-619 ##label GIU !'##cross-references EMBL:X66533; NID:g31685; PIDN:CAA47144.1; !1PID:g31686 GENETICS !$#gene GDB:GUCY1B3; GUC1B3; GC-SB3 !'##cross-references GDB:141992; OMIM:139397 !$#map_position 4q31.3-4q33 CLASSIFICATION #superfamily soluble guanylate cyclase; guanylate cyclase !1catalytic domain homology KEYWORDS heterodimer; phosphorus-oxygen lyase FEATURE !$373-607 #domain guanylate cyclase catalytic domain homology !8#label GCC SUMMARY #length 619 #molecular-weight 70514 #checksum 3861 SEQUENCE /// ENTRY OYBO70 #type complete TITLE guanylate cyclase (EC 4.6.1.2), soluble, beta-1 chain - bovine ALTERNATE_NAMES guanylate cyclase, soluble, 70K chain ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 18-Jun-1999 ACCESSIONS S01653; A38759 REFERENCE S01653 !$#authors Koesling, D.; Herz, J.; Gausepohl, H.; Niroomand, F.; !1Hinsch, K.D.; Muelsch, A.; Boehme, E.; Schultz, G.; Frank, !1R. !$#journal FEBS Lett. (1988) 239:29-34 !$#title The primary structure of the 70 kDa subunit of bovine !1soluble guanylate cyclase. !$#cross-references MUID:89031214; PMID:2903071 !$#accession S01653 !'##molecule_type mRNA !'##residues 1-619 ##label KOE !'##cross-references EMBL:Y00770; NID:g407; PIDN:CAA68739.1; PID:g408 !$#accession A38759 !'##molecule_type protein !'##residues 1-6;28-32;41-45;96-109;337-343;396-406;562-569 ##label KOE2 GENETICS !$#introns 281/3; 392/2 CLASSIFICATION #superfamily soluble guanylate cyclase; guanylate cyclase !1catalytic domain homology KEYWORDS cGMP biosynthesis; heterodimer; phosphorus-oxygen lyase FEATURE !$373-607 #domain guanylate cyclase catalytic domain homology !8#label GCC SUMMARY #length 619 #molecular-weight 70502 #checksum 4156 SEQUENCE /// ENTRY OYRTB1 #type complete TITLE guanylate cyclase (EC 4.6.1.2), soluble, beta-1 chain - rat ALTERNATE_NAMES guanylate cyclase, soluble, 70K chain ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 18-Jun-1999 ACCESSIONS A31871 REFERENCE A31871 !$#authors Nakane, M.; Saheki, S.; Kuno, T.; Ishii, K.; Murad, F. !$#journal Biochem. Biophys. Res. Commun. (1988) 157:1139-1147 !$#title Molecular cloning of a cDNA coding for 70 kilodalton subunit !1of soluble guanylate cyclase from rat lung. !$#cross-references MUID:89087429; PMID:2905128 !$#accession A31871 !'##molecule_type mRNA !'##residues 1-619 ##label NAK !'##cross-references GB:M22562; NID:g204273; PIDN:AAA41204.1; !1PID:g204274 CLASSIFICATION #superfamily soluble guanylate cyclase; guanylate cyclase !1catalytic domain homology KEYWORDS cGMP biosynthesis; heterodimer; phosphorus-oxygen lyase FEATURE !$373-607 #domain guanylate cyclase catalytic domain homology !8#label GCC SUMMARY #length 619 #molecular-weight 70477 #checksum 5038 SEQUENCE /// ENTRY OYBO77 #type complete TITLE guanylate cyclase (EC 4.6.1.2), soluble, alpha-1 chain - bovine ALTERNATE_NAMES guanylate cyclase, soluble, 77K chain ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 18-Jun-1999 ACCESSIONS S10713; A38767 REFERENCE S10713 !$#authors Koesling, D.; Harteneck, C.; Humbert, P.; Bosserhoff, A.; !1Frank, R.; Schultz, G.; Boehme, E. !$#journal FEBS Lett. (1990) 266:128-132 !$#title The primary structure of the larger subunit of soluble !1guanylyl cyclase from bovine lung. Homology between the two !1subunits of the enzyme. !$#cross-references MUID:90306336; PMID:1973124 !$#accession S10713 !'##molecule_type mRNA !'##residues 1-691 ##label KOE1 !'##cross-references EMBL:X54014; NID:g405; PIDN:CAA37960.1; PID:g406 !$#accession A38767 !'##molecule_type protein !'##residues 118-133;226-232;286-293;319-330;412-417;557-571;629-637 !1##label KOE2 CLASSIFICATION #superfamily soluble guanylate cyclase; guanylate cyclase !1catalytic domain homology KEYWORDS cGMP biosynthesis; heterodimer; phosphorus-oxygen lyase FEATURE !$434-662 #domain guanylate cyclase catalytic domain homology !8#label GCC SUMMARY #length 691 #molecular-weight 77532 #checksum 2903 SEQUENCE /// ENTRY OYRTA1 #type complete TITLE guanylate cyclase (EC 4.6.1.2), soluble, alpha-1 chain - rat ALTERNATE_NAMES guanylate cyclase, soluble, 77K chain ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 18-Jun-1999 ACCESSIONS A38297 REFERENCE A38297 !$#authors Nakane, M.; Arai, K.; Saheki, S.; Kuno, T.; Buechler, W.; !1Murad, F. !$#journal J. Biol. Chem. (1990) 265:16841-16845 !$#title Molecular cloning and expression of cDNAs coding for soluble !1guanylate cyclase from rat lung. !$#cross-references MUID:91009100; PMID:1698769 !$#accession A38297 !'##molecule_type mRNA !'##residues 1-690 ##label NAK !'##cross-references GB:M57405; GB:M36075; NID:g204277; PIDN:AAA41206.1; !1PID:g204278 CLASSIFICATION #superfamily soluble guanylate cyclase; guanylate cyclase !1catalytic domain homology KEYWORDS cGMP biosynthesis; heterodimer; phosphorus-oxygen lyase FEATURE !$432-660 #domain guanylate cyclase catalytic domain homology !8#label GCC SUMMARY #length 690 #molecular-weight 77566 #checksum 6429 SEQUENCE /// ENTRY OYRTB2 #type complete TITLE guanylate cyclase (EC 4.6.1.2), soluble, beta-2 chain - rat ALTERNATE_NAMES guanylate cyclase, soluble, 76K chain ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 18-Jun-1999 ACCESSIONS A36228 REFERENCE A36228 !$#authors Yuen, P.S.T.; Potter, L.R.; Garbers, D.L. !$#journal Biochemistry (1990) 29:10872-10878 !$#title A new form of guanylyl cyclase is preferentially expressed !1in rat kidney. !$#cross-references MUID:91105012; PMID:1980215 !$#accession A36228 !'##molecule_type mRNA !'##residues 1-682 ##label YUE !'##cross-references GB:M57507; GB:J05308; NID:g204279; PIDN:AAA41207.1; !1PID:g204280 !'##experimental_source kidney CLASSIFICATION #superfamily soluble guanylate cyclase; guanylate cyclase !1catalytic domain homology KEYWORDS cGMP biosynthesis; heterodimer; phosphorus-oxygen lyase FEATURE !$360-584 #domain guanylate cyclase catalytic domain homology !8#label GCC SUMMARY #length 682 #molecular-weight 76196 #checksum 3778 SEQUENCE /// ENTRY OYHUAR #type complete TITLE natriuretic peptide receptor A precursor - human ALTERNATE_NAMES atrial natriuretic peptide receptor; atrionatriuretic peptide receptor A; guanylate cyclase A, membrane-bound CONTAINS guanylate cyclase (EC 4.6.1.2) A ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 21-Jul-2000 ACCESSIONS S04459; I52846 REFERENCE S04459 !$#authors Lowe, D.G.; Chang, M.S.; Hellmiss, R.; Chen, E.; Singh, S.; !1Garbers, D.L.; Goeddel, D.V. !$#journal EMBO J. (1989) 8:1377-1384 !$#title Human atrial natriuretic peptide receptor defines a new !1paradigm for second messenger signal transduction. !$#cross-references MUID:89356605; PMID:2569967 !$#accession S04459 !'##molecule_type mRNA !'##residues 1-1061 ##label LOW !'##cross-references EMBL:X15357; NID:g28229; PIDN:CAA33417.1; !1PID:g28230 REFERENCE I52846 !$#authors Pardhasaradhi, K.; Kutty, R.K.; Gentleman, S.; Krishna, G. !$#journal Cell. Mol. Neurobiol. (1994) 14:1-7 !$#title Expression of mRNA for atrial natriuretic peptide receptor !1guanylate cyclase (ANPRA) in human retina. !$#cross-references MUID:95042574; PMID:7954658 !$#accession I52846 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 634-1048 ##label RES !'##cross-references GB:S72628; NID:g619241; PIDN:AAD14112.1; !1PID:g4261812 !'##experimental_source retina GENETICS !$#gene GDB:NPR1; NPRA; ANPRA !'##cross-references GDB:125199; OMIM:108960 !$#map_position 1q21-1q22 CLASSIFICATION #superfamily membrane-bound guanylate cyclase; guanylate !1cyclase catalytic domain homology; natriuretic !1peptide-binding domain homology; protein kinase homology KEYWORDS ATP; carbon-oxygen lyase; cGMP biosynthesis; glycoprotein; !1hormone receptor; phosphorus-oxygen lyase; transmembrane !1protein FEATURE !$1-32 #domain signal sequence #status predicted #label SIG\ !$33-1061 #product natriuretic peptide receptor A #status !8predicted #label MAT\ !$33-473 #domain extracellular #status predicted #label EXT\ !$113-453 #domain natriuretic peptide-binding domain homology !8#label NPB\ !$474-494 #domain transmembrane #status predicted #label TMM\ !$495-1061 #domain intracellular #status predicted #label INT\ !$526-808 #domain protein kinase homology #label KIN\ !$828-1055 #domain guanylate cyclase catalytic domain homology !8#label GCC\ !$34,45,212,338,379, !$386,427 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1061 #molecular-weight 118918 #checksum 6297 SEQUENCE /// ENTRY OYRTR #type complete TITLE atrial natriuretic peptide receptor A precursor - rat ALTERNATE_NAMES guanylate cyclase A, membrane-bound CONTAINS guanylate cyclase (EC 4.6.1.2) A ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jul-1999 ACCESSIONS S03348; A41303 REFERENCE S03348 !$#authors Chinkers, M.; Garbers, D.L.; Chang, M.S.; Lowe, D.G.; Chin, !1H.; Goeddel, D.V.; Schulz, S. !$#journal Nature (1989) 338:78-83 !$#title A membrane form of guanylate cyclase is an atrial !1natriuretic peptide receptor. !$#cross-references MUID:89143770; PMID:2563900 !$#accession S03348 !'##molecule_type mRNA !'##residues 1-1057 ##label CHI !'##cross-references EMBL:X14773; NID:g56339; PIDN:CAA32881.1; !1PID:g56340 REFERENCE A41303 !$#authors Duda, T.; Goraczniak, R.M.; Sharma, R.K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:7882-7886 !$#title Site-directed mutational analysis of a membrane guanylate !1cyclase cDNA reveals the atrial natriuretic factor signaling !1site. !$#cross-references MUID:91352095; PMID:1679239 !$#accession A41303 !'##molecule_type mRNA !'##residues 1-365,'H',367-391,'P',393-1057 ##label DUD !'##cross-references GB:M74535; NID:g204269; PIDN:AAA41202.1; !1PID:g204270 CLASSIFICATION #superfamily membrane-bound guanylate cyclase; guanylate !1cyclase catalytic domain homology; natriuretic !1peptide-binding domain homology; protein kinase homology KEYWORDS ATP; carbon-oxygen lyase; cGMP biosynthesis; glycoprotein; !1hormone receptor; phosphorus-oxygen lyase; transmembrane !1protein FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-1057 #product atrial natriuretic peptide receptor #status !8predicted #label MAT\ !$29-469 #domain extracellular #status predicted #label EXT\ !$109-449 #domain natriuretic peptide-binding domain homology !8#label NPB\ !$470-490 #domain transmembrane #status predicted #label TMM\ !$491-1057 #domain intracellular #status predicted #label INT\ !$522-804 #domain protein kinase homology #label KIN\ !$824-1051 #domain guanylate cyclase catalytic domain homology !8#label GCC\ !$41,208,334,375,382, !$423 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1057 #molecular-weight 118950 #checksum 7976 SEQUENCE /// ENTRY OYMSAR #type complete TITLE atrial natriuretic peptide receptor A precursor - mouse ALTERNATE_NAMES guanylate cyclase A, membrane-bound CONTAINS guanylate cyclase (EC 4.6.1.2) A ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS A36568; A33088 REFERENCE A36568 !$#authors Pandey, K.N.; Singh, S. !$#journal J. Biol. Chem. (1990) 265:12342-12348 !$#title Molecular cloning and expression of murine guanylate !1cyclase/atrial natriuretic factor receptor cDNA. !$#cross-references MUID:90324219; PMID:1973687 !$#accession A36568 !'##molecule_type mRNA !'##residues 1-1057 ##label PAN !'##cross-references GB:J05504; NID:g193447; PIDN:AAA37670.1; !1PID:g309246 !'##experimental_source strain C57B1/6J CLASSIFICATION #superfamily membrane-bound guanylate cyclase; guanylate !1cyclase catalytic domain homology; natriuretic !1peptide-binding domain homology; protein kinase homology KEYWORDS ATP; carbon-oxygen lyase; cGMP biosynthesis; glycoprotein; !1hormone receptor; phosphorus-oxygen lyase; transmembrane !1protein FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-1057 #product atrial natriuretic peptide receptor #status !8predicted #label MAT\ !$29-469 #domain extracellular #status predicted #label EXT\ !$109-449 #domain natriuretic peptide-binding domain homology !8#label NPB\ !$470-490 #domain transmembrane #status predicted #label TMM\ !$491-1057 #domain intracellular #status predicted #label INT\ !$522-804 #domain protein kinase homology #label KIN\ !$824-1051 #domain guanylate cyclase catalytic domain homology !8#label GCC\ !$41,208,334,375,382, !$423 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1057 #molecular-weight 119209 #checksum 7269 SEQUENCE /// ENTRY OYHUBR #type complete TITLE natriuretic peptide receptor B precursor - human ALTERNATE_NAMES atrionatriuretic peptide receptor B; brain natriuretic peptide receptor; guanylate cyclase B, membrane-bound CONTAINS guanylate cyclase (EC 4.6.1.2) B ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1991 #sequence_revision 22-Apr-1995 #text_change 16-Jul-1999 ACCESSIONS S05514; A38777 REFERENCE S05514 !$#authors Chang, M.S.; Lowe, D.G.; Lewis, M.; Hellmiss, R.; Chen, E.; !1Goeddel, D.V. !$#journal Nature (1989) 341:68-72 !$#title Differential activation by atrial and brain natriuretic !1peptides of two different receptor guanylate cyclases. !$#cross-references MUID:89365195; PMID:2570358 !$#accession S05514 !'##molecule_type DNA !'##residues 1-207 ##label CHA !$#accession A38777 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 208-1047 ##label CHA2 GENETICS !$#gene GDB:NPR2; NPRB; ANPRB !'##cross-references GDB:125200; OMIM:108961 !$#map_position 9p21-9p12 CLASSIFICATION #superfamily membrane-bound guanylate cyclase; guanylate !1cyclase catalytic domain homology; natriuretic !1peptide-binding domain homology; protein kinase homology KEYWORDS ATP; cGMP biosynthesis; glycoprotein; hormone receptor; !1phosphorus-oxygen lyase; transmembrane protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-1047 #product natriuretic peptide receptor B #status !8predicted #label MAT\ !$23-455 #domain extracellular #status predicted #label EXT\ !$96-437 #domain natriuretic peptide-binding domain homology !8#label NPB\ !$456-478 #domain transmembrane #status predicted #label TMM\ !$479-1047 #domain intracellular #status predicted #label INT\ !$510-793 #domain protein kinase homology #label KIN\ !$813-1040 #domain guanylate cyclase catalytic domain homology !8#label GCC\ !$24,35,161,195,244, !$277,349 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1047 #molecular-weight 117021 #checksum 6891 SEQUENCE /// ENTRY OYRTBR #type complete TITLE atrial natriuretic peptide receptor B precursor - rat ALTERNATE_NAMES guanylate cyclase B, membrane-bound CONTAINS guanylate cyclase (EC 4.6.1.2) B ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS A33300 REFERENCE A33300 !$#authors Schulz, S.; Singh, S.; Bellet, R.A.; Singh, G.; Tubb, D.J.; !1Chin, H.; Garbers, D.L. !$#journal Cell (1989) 58:1155-1162 !$#title The primary structure of a plasma membrane guanylate cyclase !1demonstrates diversity within this new receptor family. !$#cross-references MUID:89376566; PMID:2570641 !$#accession A33300 !'##molecule_type mRNA !'##residues 1-1047 ##label SCH !'##cross-references GB:M26896; NID:g204275; PIDN:AAA41205.1; !1PID:g204276 CLASSIFICATION #superfamily membrane-bound guanylate cyclase; guanylate !1cyclase catalytic domain homology; natriuretic !1peptide-binding domain homology; protein kinase homology KEYWORDS ATP; carbon-oxygen lyase; cGMP biosynthesis; glycoprotein; !1hormone receptor; phosphorus-oxygen lyase; transmembrane !1protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-1047 #product atrial natriuretic peptide receptor #status !8predicted #label MAT\ !$23-458 #domain extracellular #status predicted #label EXT\ !$96-437 #domain natriuretic peptide-binding domain homology !8#label NPB\ !$459-478 #domain transmembrane #status predicted #label TMM\ !$479-1047 #domain intracellular #status predicted #label INT\ !$510-793 #domain protein kinase homology #label KIN\ !$813-1040 #domain guanylate cyclase catalytic domain homology !8#label GCC\ !$24,35,161,195,244, !$277,349 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1047 #molecular-weight 117126 #checksum 7202 SEQUENCE /// ENTRY S55279 #type complete TITLE guanylate cyclase (EC 4.6.1.2) 2 precursor, retinal - bovine ALTERNATE_NAMES guanylyl cyclase ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S55279 REFERENCE S55279 !$#authors Goraczniak, R.M.; Duda, T.; Sitaramayya, A.; Sharma, R.K. !$#journal Biochem. J. (1994) 302:455-461 !$#title Structural and functional characterization of the rod outer !1segment membrane guanylate cyclase. !$#cross-references MUID:94379976; PMID:7916565 !$#accession S55279 !'##status preliminary !'##molecule_type mRNA !'##residues 1-1110 ##label GOR !'##cross-references EMBL:L37089; NID:g559667; PIDN:AAA50790.1; !1PID:g559668 CLASSIFICATION #superfamily membrane-bound guanylate cyclase; guanylate !1cyclase catalytic domain homology; natriuretic !1peptide-binding domain homology; protein kinase homology KEYWORDS cGMP biosynthesis; glycoprotein; phosphorus-oxygen lyase; !1transmembrane protein FEATURE !$529-817 #domain protein kinase homology #label KIN\ !$837-1065 #domain guanylate cyclase catalytic domain homology !8#label GCC SUMMARY #length 1110 #molecular-weight 120368 #checksum 2617 SEQUENCE /// ENTRY OYURGA #type complete TITLE speract receptor precursor - sea urchin (Arbacia punctulata) ALTERNATE_NAMES guanylate cyclase, membrane-bound CONTAINS guanylate cyclase (EC 4.6.1.2) ORGANISM #formal_name Arbacia punctulata #common_name punctuate urchin DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 18-Jun-1999 ACCESSIONS S05480; A38760 REFERENCE S05480 !$#authors Singh, S.; Lowe, D.G.; Thorpe, D.S.; Rodriguez, H.; Kuang, !1W.J.; Dangott, L.J.; Chinkers, M.; Goeddel, D.V.; Garbers, !1D.L. !$#journal Nature (1988) 334:708-712 !$#title Membrane guanylate cyclase is a cell-surface receptor with !1homology to protein kinases. !$#cross-references MUID:88318927; PMID:2901039 !$#accession S05480 !'##molecule_type mRNA !'##residues 1-986 ##label SIN !'##cross-references EMBL:X12874; NID:g5648; PIDN:CAA31367.1; PID:g5649 !$#accession A38760 !'##molecule_type protein !'##residues 22-37;206-212;280-307;366-368,'S',370,'N',372-373,'X', !1375-378;549-552;873-874,'H',876 ##label SIN2 CLASSIFICATION #superfamily membrane-bound guanylate cyclase; guanylate !1cyclase catalytic domain homology; natriuretic !1peptide-binding domain homology; protein kinase homology KEYWORDS ATP; cGMP biosynthesis; chemotaxis; glycoprotein; !1phosphoprotein; phosphorus-oxygen lyase; receptor; !1transmembrane protein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-986 #product guanylate cyclase, membrane-bound #status !8predicted #label MAT\ !$22-499 #domain extracellular #status predicted #label EXT\ !$113-479 #domain natriuretic peptide-binding domain homology !8#label NPB\ !$506-527 #domain transmembrane #status predicted #label TMM\ !$529-986 #domain intracellular #status predicted #label INT\ !$559-843 #domain protein kinase homology #label KIN\ !$185,361,410 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 986 #molecular-weight 111283 #checksum 1922 SEQUENCE /// ENTRY OYURCP #type complete TITLE speract receptor precursor - sea urchin (Strongylocentrotus purpuratus) ALTERNATE_NAMES guanylate cyclase, membrane-bound CONTAINS guanylate cyclase (EC 4.6.1.2) ORGANISM #formal_name Strongylocentrotus purpuratus #common_name purple urchin DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS A33535; A30856 REFERENCE A33535 !$#authors Thorpe, D.S.; Garbers, D.L. !$#journal J. Biol. Chem. (1989) 264:6545-6549 !$#title The membrane form of guanylate cyclase. Homology with a !1subunit of the cytoplasmic form of the enzyme. !$#cross-references MUID:89197965; PMID:2564849 !$#accession A33535 !'##molecule_type mRNA !'##residues 1-1125 ##label THO !'##cross-references GB:M22444; GB:J04693; NID:g161476; PIDN:AAA30051.1; !1PID:g161477 CLASSIFICATION #superfamily membrane-bound guanylate cyclase; guanylate !1cyclase catalytic domain homology; natriuretic !1peptide-binding domain homology; protein kinase homology KEYWORDS ATP; carbon-oxygen lyase; cGMP biosynthesis; glycoprotein; !1hormone receptor; phosphorus-oxygen lyase; transmembrane !1protein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-1125 #product speract receptor #status predicted #label !8MAT\ !$22-510 #domain extracellular #status predicted #label EXT\ !$113-477 #domain natriuretic peptide-binding domain homology !8#label NPB\ !$509-530 #domain transmembrane #status predicted #label TMM\ !$532-1125 #domain intracellular #status predicted #label CYT\ !$562-846 #domain protein kinase homology #label KIN\ !$866-1093 #domain guanylate cyclase catalytic domain homology !8#label GCC\ !$185,409 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1125 #molecular-weight 126256 #checksum 5278 SEQUENCE /// ENTRY OYHUHX #type complete TITLE heat-stable enterotoxin receptor precursor - human ALTERNATE_NAMES guanylate cyclase C, membrane-bound; guanylate cyclase-coupled enterotoxin STa receptor CONTAINS guanylate cyclase (EC 4.6.1.2) C ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1992 #sequence_revision 22-Apr-1995 #text_change 16-Jul-1999 ACCESSIONS A40940; JQ1279; S65754 REFERENCE A40940 !$#authors de Sauvage, F.J.; Camerato, T.R.; Goeddel, D.V. !$#journal J. Biol. Chem. (1991) 266:17912-17918 !$#title Primary structure and functional expression of the human !1receptor for Escherichia coli heat-stable enterotoxin. !$#cross-references MUID:92011512; PMID:1680854 !$#accession A40940 !'##molecule_type mRNA !'##residues 1-1073 ##label DES !'##cross-references GB:M73489; NID:g338501; PIDN:AAA36655.1; !1PID:g338502 !'##experimental_source colonic cell line T84 (ATCC CCL248) REFERENCE JQ1279 !$#authors Singh, S.; Singh, G.; Heim, J.M.; Gerzer, R. !$#journal Biochem. Biophys. Res. Commun. (1991) 179:1455-1463 !$#title Isolation and expression of a guanylate cyclase-coupled heat !1stable enterotoxin receptor cDNA from a human colonic cell !1line. !$#cross-references MUID:92028888; PMID:1718270 !$#accession JQ1279 !'##molecule_type mRNA !'##residues 1-321,'R',323-330,'V',332-508,'V',510-542,'T',544-1073 !1##label SIN !'##experimental_source colonic cell line T84 REFERENCE S65754 !$#authors Mann, E.A.; Jump, M.L.; Giannella, R.A. !$#journal Biochim. Biophys. Acta (1996) 1305:7-10 !$#title Cell line-specific transcriptional activation of the !1promoter of the human guanylyl cyclase C/heat-stable !1enterotoxin receptor gene. !$#cross-references MUID:96180976; PMID:8605253 !$#accession S65754 !'##molecule_type DNA !'##residues 1-72 ##label MAN !'##cross-references EMBL:U20230; NID:g1184045; PIDN:AAC50381.1; !1PID:g1184046 GENETICS !$#gene GDB:GUC2C !'##cross-references GDB:128987; OMIM:601330 !$#map_position 12p12-12p12 CLASSIFICATION #superfamily membrane-bound guanylate cyclase; guanylate !1cyclase catalytic domain homology; natriuretic !1peptide-binding domain homology; protein kinase homology KEYWORDS ATP; carbon-oxygen lyase; cGMP biosynthesis; glycoprotein; !1heat-stable protein; hormone receptor; phosphorus-oxygen !1lyase; receptor; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-1073 #product heat-stable enterotoxin receptor #status !8predicted #label MAT\ !$24-430 #domain extracellular #status predicted #label EXT\ !$119-425 #domain natriuretic peptide-binding domain homology !8#label NPB\ !$431-454 #domain transmembrane #status predicted #label TRM\ !$455-1073 #domain intracellular #status predicted #label CYT\ !$472-752 #domain protein kinase homology #label KIN\ !$776-1004 #domain guanylate cyclase catalytic domain homology !8#label GCC\ !$32,75,79,195,284, !$307,313,345,357,402 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1073 #molecular-weight 123368 #checksum 8799 SEQUENCE /// ENTRY OYRTHX #type complete TITLE heat-stable enterotoxin receptor precursor - rat ALTERNATE_NAMES guanylate cyclase C, membrane-bound CONTAINS guanylate cyclase (EC 4.6.1.2) C ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS A36292 REFERENCE A36292 !$#authors Schulz, S.; Green, C.K.; Yuen, P.S.T.; Garbers, D.L. !$#journal Cell (1990) 63:941-948 !$#title Guanylyl cyclase is a heat-stable enterotoxin receptor. !$#cross-references MUID:91077932; PMID:1701694 !$#accession A36292 !'##molecule_type mRNA !'##residues 1-1075 ##label SCH !'##cross-references GB:M55636 CLASSIFICATION #superfamily membrane-bound guanylate cyclase; guanylate !1cyclase catalytic domain homology; natriuretic !1peptide-binding domain homology; protein kinase homology KEYWORDS ATP; carbon-oxygen lyase; cGMP biosynthesis; glycoprotein; !1heat-stable protein; hormone receptor; phosphorus-oxygen !1lyase; transmembrane protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-1075 #product heat-stable enterotoxin receptor #status !8predicted #label MAT\ !$23-429 #domain extracellular #status predicted #label EXT\ !$118-424 #domain natriuretic peptide-binding domain homology !8#label NPB\ !$430-453 #domain transmembrane #status predicted #label TMM\ !$454-1075 #domain intracellular #status predicted #label CYT\ !$474-754 #domain protein kinase homology #label KIN\ !$778-1006 #domain guanylate cyclase catalytic domain homology !8#label GCC\ !$31,74,78,187,194, !$306,356,401 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1075 #molecular-weight 123753 #checksum 956 SEQUENCE /// ENTRY A42239 #type complete TITLE adenylate cyclase (EC 4.6.1.1) germination stage - slime mold (Dictyostelium discoideum) ORGANISM #formal_name Dictyostelium discoideum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A42239 REFERENCE A42239 !$#authors Pitt, G.S.; Milona, N.; Borleis, J.; Lin, K.C.; Reed, R.R.; !1Devreotes, P.N. !$#journal Cell (1992) 69:305-315 !$#title Structurally distinct and stage-specific adenylyl cyclase !1genes play different roles in Dictyostelium development. !$#cross-references MUID:92233467; PMID:1348970 !$#accession A42239 !'##status preliminary; nucleic acid sequence not shown; not compared !1with conceptual translation !'##molecule_type DNA !'##residues 1-858 ##label PIT !'##cross-references GB:M87278 CLASSIFICATION #superfamily slime mold germination stage adenylate cyclase; !1guanylate cyclase catalytic domain homology KEYWORDS phosphorus-oxygen lyase FEATURE !$351-574 #domain guanylate cyclase catalytic domain homology !8#label GCC SUMMARY #length 858 #molecular-weight 98379 #checksum 74 SEQUENCE /// ENTRY A56699 #type complete TITLE guanylate cyclase (EC 4.6.1.2), receptor-type drgc - fruit fly (Drosophila melanogaster) CONTAINS guanylate cyclase (EC 4.6.1.2) ORGANISM #formal_name Drosophila melanogaster DATE 19-Oct-1995 #sequence_revision 19-Oct-1995 #text_change 16-Jul-1999 ACCESSIONS A56699; A56114 REFERENCE A56699 !$#authors Liu, W.; Yoon, J.; Burg, M.; Chen, L.; Pak, W.L. !$#journal J. Biol. Chem. (1995) 270:12418-12427 !$#title Molecular characterization of two Drosophila guanylate !1cyclases expressed in the nervous system. !$#cross-references MUID:95279366; PMID:7759483 !$#accession A56699 !'##status preliminary !'##molecule_type mRNA !'##residues 1-1525 ##label LIU !'##cross-references GB:U23485; NID:g755873; PIDN:AAA85858.1; !1PID:g755874 REFERENCE A56114 !$#authors McNeil, L.; Chinkers, M.; Forte, M. !$#journal J. Biol. Chem. (1995) 270:7189-7196 !$#title Identification, characterization, and developmental !1regulation of a receptor guanylyl cyclase expressed during !1early stages of Drosophila development. !$#cross-references MUID:95221369; PMID:7706258 !$#accession A56114 !'##status preliminary !'##molecule_type mRNA !'##residues 1-380,'A',382-1525 ##label MCN !'##cross-references GB:L35598; NID:g531187; PIDN:AAA74408.1; !1PID:g531188 GENETICS !$#gene FlyBase:Gyc76C !'##cross-references FlyBase:FBgn0013974 CLASSIFICATION #superfamily Drosophila receptor-type guanylate cyclase; !1guanylate cyclase catalytic domain homology; natriuretic !1peptide-binding domain homology; protein kinase homology KEYWORDS ATP; phosphorus-oxygen lyase; receptor; transmembrane !1protein FEATURE !$98-462 #domain natriuretic peptide-binding domain homology !8#label NPB\ !$493-509 #domain transmembrane #status predicted #label TMN\ !$544-828 #domain protein kinase homology #label KIN\ !$848-1076 #domain guanylate cyclase catalytic domain homology !8#label GCC SUMMARY #length 1525 #molecular-weight 170518 #checksum 8421 SEQUENCE /// ENTRY OYECHF #type complete TITLE imidazoleglycerol-phosphate synthase (EC 4.3.2.-) cyclase chain hisF [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES cyclase ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 01-Mar-2002 ACCESSIONS JS0134; I76779; H64967 REFERENCE JS0131 !$#authors Carlomagno, M.S.; Chiariotti, L.; Alifano, P.; Nappo, A.G.; !1Bruni, C.B. !$#journal J. Mol. Biol. (1988) 203:585-606 !$#title Structure and function of the Salmonella typhimurium and !1Escherichia coli K-12 histidine operons. !$#cross-references MUID:89094829; PMID:3062174 !$#accession JS0134 !'##molecule_type DNA !'##residues 1-258 ##label CAR !'##cross-references GB:X13462; NID:g41706; PIDN:CAA31817.1; PID:g41714 !'##experimental_source strain K12 REFERENCE I57096 !$#authors Sugiyama, T.; Kido, N.; Komatsu, T.; Ohta, M.; Jann, K.; !1Jann, B.; Saeki, A.; Kato, N. !$#journal Microbiology (1994) 140:59-71 !$#title Genetic analysis of Escherichia coli O9 rfb: identification !1and DNA sequence of phosphomannomutase and GDP-mannose !1pyrophosphorylase genes. !$#cross-references MUID:94214678; PMID:8162191 !$#accession I76779 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 109-258 ##label RES !'##cross-references GB:D43637; NID:g598464; PIDN:BAA07754.1; !1PID:g598474 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64967 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-258 ##label BLAT !'##cross-references GB:AE000293; GB:U00096; NID:g2367127; !1PIDN:AAC75086.1; PID:g1788336; UWGP:b2025 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene hisF !$#map_position 44 min FUNCTION !$#description catalyzes the cyclization reaction that produces !1D-erythro-imidazole glycerol phosphate in the histidine !1biosynthetic pathway !$#pathway histidine biosynthesis !$#note hisH and hisF gene products form a dimer that constitutes !1imidazole glycerol phosphate synthase (IPG) CLASSIFICATION #superfamily cyclase hisF KEYWORDS amidine-lyase; carbon-nitrogen lyase; histidine biosynthesis SUMMARY #length 258 #molecular-weight 28454 #checksum 3101 SEQUENCE /// ENTRY OYEBHF #type complete TITLE cyclase hisF - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 28-May-1999 ACCESSIONS JS0162 REFERENCE JS0131 !$#authors Carlomagno, M.S.; Chiariotti, L.; Alifano, P.; Nappo, A.G.; !1Bruni, C.B. !$#journal J. Mol. Biol. (1988) 203:585-606 !$#title Structure and function of the Salmonella typhimurium and !1Escherichia coli K-12 histidine operons. !$#cross-references MUID:89094829; PMID:3062174 !$#accession JS0162 !'##molecule_type DNA !'##residues 1-258 ##label CAR !'##cross-references GB:X13464; NID:g47719; PIDN:CAA31828.1; PID:g47727 COMMENT This enzyme catalyzes the cyclization reaction that produces !1D-erythro-imidazole glycerol phosphate in the histidine !1biosynthetic pathway. GENETICS !$#gene hisF !$#map_position 42 min CLASSIFICATION #superfamily cyclase hisF KEYWORDS histidine biosynthesis SUMMARY #length 258 #molecular-weight 28368 #checksum 2997 SEQUENCE /// ENTRY SYECQ #type complete TITLE 3-dehydroquinate synthase (EC 4.2.3.4) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 21-Jun-2002 ACCESSIONS A24863; S31742; H65133 REFERENCE A24863 !$#authors Millar, G.; Coggins, J.R. !$#journal FEBS Lett. (1986) 200:11-17 !$#title The complete amino acid sequence of 3-dehydroquinate !1synthase of Escherichia coli K12. !$#cross-references MUID:86192828; PMID:3009224 !$#accession A24863 !'##molecule_type DNA !'##residues 1-362 ##label MIL !'##cross-references GB:X03867; NID:g40967; PIDN:CAA27495.1; PID:g40968 !'##experimental_source strain K12 REFERENCE S31739 !$#authors Lyngstadaas, A.; Boye, E. !$#submission submitted to the EMBL Data Library, January 1993 !$#description dam operon. !$#accession S31742 !'##molecule_type DNA !'##residues 1-362 ##label LYN !'##cross-references EMBL:Z19601; NID:g41221; PIDN:CAA79666.1; !1PID:g41225 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65133 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-362 ##label BLAT !'##cross-references GB:AE000414; GB:U00096; NID:g1789783; !1PIDN:AAC76414.1; PID:g1789791; UWGP:b3389 !'##experimental_source strain K-12, substrain MG1655 COMMENT This enzyme occurs naturally at low levels and catalyzes the !1cyclization of 3-deoxy-D-arabino-heptulosonate-7-phosphate !1to 3-dehydroquinate. GENETICS !$#gene aroB !$#map_position 75 min CLASSIFICATION #superfamily 3-dehydroquinate synthase; 3-dehydroquinate !1synthase homology KEYWORDS carbon-oxygen lyase; phosphorus-oxygen lyase; shikimate !1pathway FEATURE !$5-339 #domain 3-dehydroquinate synthase homology #label DQS SUMMARY #length 362 #molecular-weight 38881 #checksum 4137 SEQUENCE /// ENTRY S75507 #type complete TITLE 3-dehydroquinate synthase - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein slr2130 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S75507 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75507 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-361 ##label KAN !'##cross-references EMBL:D90911; GB:AB001339; NID:g1653083; !1PIDN:BAA18068.1; PID:g1653152 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene aroB CLASSIFICATION #superfamily 3-dehydroquinate synthase; 3-dehydroquinate !1synthase homology FEATURE !$6-343 #domain 3-dehydroquinate synthase homology #label DQS SUMMARY #length 361 #molecular-weight 38855 #checksum 7827 SEQUENCE /// ENTRY S17768 #type complete TITLE 3-dehydroquinate synthase (EC 4.2.3.4) aroB - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jun-2002 ACCESSIONS S17768; F70658 REFERENCE S17768 !$#authors Garbe, T.; Servos, S.; Hawkins, A.; Dimitriadis, G.; Young, !1D.; Dougan, G.; Charles, I. !$#journal Mol. Gen. Genet. (1991) 228:385-392 !$#title The Mycobacterium tuberculosis shikimate pathway genes: !1evolutionary relationship between biosynthetic and catabolic !13-dehydroquinases. !$#cross-references MUID:91375423; PMID:1910148 !$#accession S17768 !'##status preliminary !'##molecule_type DNA !'##residues 1-362 ##label GAR !'##cross-references EMBL:X59509; NID:g48905; PIDN:CAA42095.1; !1PID:g48906 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession F70658 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-98,'D',100-362 ##label COL !'##cross-references GB:Z83863; GB:AL123456; NID:g3261685; !1PIDN:CAB06200.1; PID:g1781064 !'##experimental_source strain H37Rv GENETICS !$#gene aroB CLASSIFICATION #superfamily 3-dehydroquinate synthase; 3-dehydroquinate !1synthase homology KEYWORDS carbon-oxygen lyase; phosphorus-oxygen lyase FEATURE !$10-339 #domain 3-dehydroquinate synthase homology #label !8DQS\ !$10-339 #product 3-dehydroquinate synthase #status predicted !8#label MAT SUMMARY #length 362 #molecular-weight 38118 #checksum 9267 SEQUENCE /// ENTRY SYECKR #type complete TITLE chorismate synthase (EC 4.2.3.5) - Escherichia coli (strain K-12) ALTERNATE_NAMES 5-enolpyruvylshikimate-3-phosphate phospholyase ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 05-Dec-1997 #text_change 21-Jun-2002 ACCESSIONS G65005; S00509; S28890; JV0091; I41140 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65005 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-361 ##label BLAT !'##cross-references GB:AE000321; GB:U00096; NID:g1788659; !1PIDN:AAC75389.1; PID:g1788669; UWGP:b2329 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S00509 !$#authors White, P.J.; Millar, G.; Coggins, J.R. !$#journal Biochem. J. (1988) 251:313-322 !$#title The overexpression, purification and complete amino acid !1sequence of chorismate synthase from Escherichia coli K12 !1and its comparison with the enzyme from Neurospora crassa. !$#cross-references MUID:88293429; PMID:2969724 !$#accession S00509 !'##molecule_type DNA !'##residues 1-334,'NAGDRFNGSPVTATGAKCRCED' ##label WHI !'##cross-references EMBL:M33021 !$#accession S28890 !'##molecule_type protein !'##residues 1-31 ##label WHI2 !'##experimental_source strain K12 REFERENCE JV0091 !$#authors Charles, I.G.; Lamb, H.K.; Pickard, D.; Dougan, G.; Hawkins, !1A.R. !$#journal J. Gen. Microbiol. (1990) 136:353-358 !$#title Isolation, characterization and nucleotide sequences of the !1aroC genes encoding chorismate synthase from Salmonella !1typhi and Escherichia coli. !$#cross-references MUID:90218018; PMID:2182772 !$#accession JV0091 !'##molecule_type DNA !'##residues 1-361 ##label CHA !'##cross-references GB:M27714; NID:g145357; PIDN:AAA23487.1; !1PID:g145358 !'##experimental_source isolate C600 !'##note the authors translated the codon TCG for residue 171 as Arg, !1CAA for residue 175 as Leu, CCC for residue 183 as Ala, ATC !1for residue 186 as Leu, GCG for residue 195 as Gly, ATC for !1residue 203 as Pro, AAA for residue 206 as Ile, GAC for !1residue 229 as Thr, GAC for residue 266 as Gln, CAA for !1residue 285 as His, and TTA for residue 340 as Thr GENETICS !$#gene aroC !$#map_position 51 min CLASSIFICATION #superfamily chorismate synthase KEYWORDS aromatic amino acid biosynthesis; carbon-oxygen lyase; FMN; !1homotetramer; phosphorus-oxygen lyase; shikimate pathway FEATURE !$2-356 #product chorismate synthase #status experimental !8#label MAT SUMMARY #length 361 #molecular-weight 39137 #checksum 3546 SEQUENCE /// ENTRY G64053 #type complete TITLE chorismate synthase (EC 4.2.3.5) - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jun-2002 ACCESSIONS G64053 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession G64053 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-357 ##label TIGR !'##cross-references GB:U32704; GB:L42023; NID:g1573143; !1PIDN:AAC21865.1; PID:g1573154; TIGR:HI0196 CLASSIFICATION #superfamily chorismate synthase KEYWORDS aromatic amino acid biosynthesis; carbon-oxygen lyase; !1phosphorus-oxygen lyase; shikimate pathway SUMMARY #length 357 #molecular-weight 38691 #checksum 7346 SEQUENCE /// ENTRY A55510 #type complete TITLE chorismate synthase (EC 4.2.3.5) - Vibrio anguillarum ORGANISM #formal_name Vibrio anguillarum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jun-2002 ACCESSIONS A55510 REFERENCE A55510 !$#authors Chen, Q.; Actis, L.A.; Tolmasky, M.E.; Crosa, J.H. !$#journal J. Bacteriol. (1994) 176:4226-4234 !$#title Chromosome-mediated 2,3-dihydroxybenzoic acid is a precursor !1in the biosynthesis of the plasmid-mediated siderophore !1anguibactin in Vibrio anguillarum. !$#cross-references MUID:94292450; PMID:8021209 !$#accession A55510 !'##status preliminary !'##molecule_type DNA !'##residues 1-372 ##label CHE !'##cross-references GB:L29562 GENETICS !$#gene aroC CLASSIFICATION #superfamily chorismate synthase KEYWORDS carbon-oxygen lyase; phosphorus-oxygen lyase SUMMARY #length 372 #molecular-weight 40505 #checksum 5408 SEQUENCE /// ENTRY A41197 #type complete TITLE chorismate synthase (EC 4.2.3.5) precursor [validated] - pink corydalis ORGANISM #formal_name Corydalis sempervirens #common_name pink corydalis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jun-2002 ACCESSIONS A41197; S13267; S15715 REFERENCE A41197 !$#authors Schaller, A.; Schmid, J.; Leibinger, U.; Amrhein, N. !$#journal J. Biol. Chem. (1991) 266:21434-21438 !$#title Molecular cloning and analysis of a cDNA coding for !1chorismate synthase from the higher plant Corydalis !1sempervirens pers. !$#cross-references MUID:92042037; PMID:1718979 !$#accession A41197 !'##status preliminary !'##molecule_type mRNA !'##residues 1-447 ##label SCH !'##cross-references EMBL:X60544; NID:g18255; PIDN:CAA43034.1; !1PID:g18256 REFERENCE S13267 !$#authors Schaller, A.; Windhofer, V.; Amrhein, N. !$#journal Arch. Biochem. Biophys. (1990) 282:437-442 !$#title Purification of chorismate synthase from a cell culture of !1the higher plant Corydalis sempervirens Pers. !$#cross-references MUID:91053166; PMID:2146922 !$#accession S13267 !'##molecule_type protein !'##residues 'X',307-320 ##label SCW GENETICS !$#genome nuclear COMPLEX homodimer FUNCTION !$#description EC 4.6.1.4 [validated, MUID:91053166]; catalyzes the !1formation of chorismate from !15-enolpyruvylshikimate-3-phosphate CLASSIFICATION #superfamily chorismate synthase KEYWORDS aromatic amino acid biosynthesis; carbon-oxygen lyase; !1chloroplast; phosphorus-oxygen lyase; shikimate pathway FEATURE !$1-57 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$58-447 #product chorismate synthase #status predicted #label !8MAT SUMMARY #length 447 #molecular-weight 48100 #checksum 9389 SEQUENCE /// ENTRY S17246 #type complete TITLE chorismate synthase (EC 4.2.3.5) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein G2501; protein YGL148w ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jun-2002 ACCESSIONS S17246; S64162 REFERENCE S17246 !$#authors Jones, D.G.L.; Reusser, U.; Braus, G.H. !$#journal Mol. Microbiol. (1991) 5:2143-2152 !$#title Molecular cloning, characterization and analysis of the !1regulation of the ARO2 gene, encoding chorismate synthase, !1of Saccharomyces cerevisiae. !$#cross-references MUID:92114793; PMID:1837329 !$#accession S17246 !'##molecule_type DNA !'##residues 1-376 ##label JON !'##cross-references EMBL:X60190; NID:g3386; PIDN:CAA42745.1; PID:g3387 REFERENCE S64153 !$#authors Volckaert, G.; Voet, M.; Verhasselt, P.; Defoor, E. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64162 !'##molecule_type DNA !'##residues 1-376 ##label VOL !'##cross-references EMBL:Z72670; NID:g1322731; PIDN:CAA96860.1; !1PID:g1322732; GSPDB:GN00007; MIPS:YGL148w !'##experimental_source strain S288C GENETICS !$#gene SGD:ARO2; MIPS:YGL148w !'##cross-references SGD:S0003116; MIPS:YGL148w !$#map_position 7L CLASSIFICATION #superfamily chorismate synthase KEYWORDS carbon-oxygen lyase; phosphorus-oxygen lyase; transmembrane !1protein FEATURE !$347-363 #domain transmembrane #status predicted #label TMM SUMMARY #length 376 #molecular-weight 40838 #checksum 1984 SEQUENCE /// ENTRY SYEBKR #type complete TITLE chorismate synthase (EC 4.2.3.5) - Salmonella typhi ALTERNATE_NAMES 5-enolpyruvylshikimate-3-phosphate phospholyase ORGANISM #formal_name Salmonella typhi DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 21-Jun-2002 ACCESSIONS A33119 REFERENCE JV0091 !$#authors Charles, I.G.; Lamb, H.K.; Pickard, D.; Dougan, G.; Hawkins, !1A.R. !$#journal J. Gen. Microbiol. (1990) 136:353-358 !$#title Isolation, characterization and nucleotide sequences of the !1aroC genes encoding chorismate synthase from Salmonella !1typhi and Escherichia coli. !$#cross-references MUID:90218018; PMID:2182772 !$#accession A33119 !'##molecule_type DNA !'##residues 1-361 ##label CHA !'##cross-references GB:M27715; NID:g153877; PIDN:AAA27029.1; !1PID:g153878 !'##note the authors translated the codon GAC for residue 229 as Thr and !1CTG for residue 340 as Thr COMMENT The active enzyme, a tetramer of identical chains, catalyzes !1the conversion of 5-enolpyruvylshikimate-3-phosphate to !1chorismic acid. GENETICS !$#gene aroC CLASSIFICATION #superfamily chorismate synthase KEYWORDS aromatic amino acid biosynthesis; carbon-oxygen lyase; !1phosphorus-oxygen lyase; shikimate pathway FEATURE !$2-361 #product chorismate synthase #status predicted #label !8MAT SUMMARY #length 361 #molecular-weight 39108 #checksum 3356 SEQUENCE /// ENTRY IBBYFC #type complete TITLE ferrochelatase (EC 4.99.1.1) precursor - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein O4605; protein YOR176w ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 21-Jul-2000 ACCESSIONS A35190; S12333; A31066; S67068 REFERENCE A35190 !$#authors Labbe-Bois, R. !$#journal J. Biol. Chem. (1990) 265:7278-7283 !$#title The ferrochelatase from Saccharomyces cerevisiae. Sequence, !1disruption, and expression of its structural gene HEM15. !$#cross-references MUID:90237021; PMID:2185242 !$#accession A35190 !'##molecule_type DNA !'##residues 1-393 ##label LAB !'##cross-references EMBL:J05395; NID:g171659; PIDN:AAA34667.1; !1PID:g171660 REFERENCE S12333 !$#authors Gokhman, I.; Zamir, A. !$#journal Nucleic Acids Res. (1990) 18:6130 !$#title The nucleotide sequence of the ferrochelatase and tRNA(val) !1gene region from Saccharomyces cerevisiae. !$#cross-references MUID:91045082; PMID:2235498 !$#accession S12333 !'##molecule_type DNA !'##residues 1-393 ##label GOK !'##cross-references EMBL:X54514; NID:g3768; PIDN:CAA38371.1; PID:g3769 REFERENCE A31066 !$#authors Camadro, J.M.; Labbe, P. !$#journal J. Biol. Chem. (1988) 263:11675-11682 !$#title Purification and properties of ferrochelatase from the yeast !1Saccharomyces cerevisiae. Evidence for a precursor form of !1the protein. !$#cross-references MUID:88298836; PMID:3042776 !$#accession A31066 !'##molecule_type protein !'##residues 32-33,'E',35-51 ##label CAM REFERENCE S66685 !$#authors Hughes, B.; Pohl, T.M. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67068 !'##molecule_type DNA !'##residues 1-393 ##label HUG !'##cross-references EMBL:Z75084; NID:g1420426; PIDN:CAA99385.1; !1PID:g1420427; GSPDB:GN00015; MIPS:YOR176w !'##experimental_source strain S288C GENETICS !$#gene SGD:HEM15; MIPS:YOR176w !'##cross-references SGD:S0005702; MIPS:YOR176w !$#map_position 15R !$#genome nuclear FUNCTION !$#description catalyzes the insertion of iron into protoporphyrin to !1produce heme !$#pathway heme biosynthesis CLASSIFICATION #superfamily ferrochelatase KEYWORDS heme biosynthesis; iron; lyase; membrane protein; !1mitochondrion FEATURE !$1-31 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$32-393 #product ferrochelatase #status experimental #label !8MAT SUMMARY #length 393 #molecular-weight 44596 #checksum 5201 SEQUENCE /// ENTRY XUECUG #type complete TITLE UDPglucose 4-epimerase (EC 5.1.3.2) - Escherichia coli (strain K-12) ALTERNATE_NAMES UDPgalactose 4-epimerase ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 31-Mar-1992 #text_change 01-Mar-2002 ACCESSIONS S02089; S00759; S14391; G64811; B25764 REFERENCE S02089 !$#authors Lemaire, H.G. !$#submission submitted to the EMBL Data Library, April 1988 !$#accession S02089 !'##molecule_type DNA !'##residues 1-338 ##label LEM1 !'##cross-references EMBL:X06226; NID:g41522; PIDN:CAA29573.1; !1PID:g41523 REFERENCE S00722 !$#authors Lemaire, H.G.; Mueller-Hill, B. !$#journal Nucleic Acids Res. (1986) 14:7705-7711 !$#title Nucleotide sequences of the galE gene and the galT gene of !1E. coli. !$#cross-references MUID:87040735; PMID:3022232 !$#accession S00759 !'##molecule_type DNA !'##residues 1-294,'AFRPTGRTPAKPTVN',310-338 ##label LEM2 !'##cross-references EMBL:X06226 !'##note this sequence has been revised in reference S02089 REFERENCE S14391 !$#authors Bernardi, F.; Bernardi, A. !$#journal DNA Seq. (1990) 1:147-150 !$#title Completed sequence of pKG1800, a vector for determination of !1transcription terminators. !$#cross-references MUID:92190543; PMID:2134186 !$#accession S14391 !'##status translation not shown !'##molecule_type DNA !'##residues 1-139,'LLPIPGQ' ##label BER !'##cross-references EMBL:X51449; NID:g42412; PIDN:CAA35813.1; !1PID:g42413 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64811 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-338 ##label BLAT !'##cross-references GB:AE000178; GB:U00096; NID:g1786967; !1PIDN:AAC73846.1; PID:g1786974; UWGP:b0759 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene galE !$#map_position 17 min FUNCTION !$#description isomerase !$#pathway galactose metabolism CLASSIFICATION #superfamily Escherichia coli UDPglucose 4-epimerase; !1UDPglucose 4-epimerase homology KEYWORDS galactose metabolism; isomerase FEATURE !$3-336 #domain UDPglucose 4-epimerase homology #label UDP SUMMARY #length 338 #molecular-weight 37265 #checksum 2330 SEQUENCE /// ENTRY A37760 #type complete TITLE UDPglucose 4-epimerase (EC 5.1.3.2) - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A37760 REFERENCE A37760 !$#authors Houng, H.S.H.; Kopecko, D.J.; Baron, L.S. !$#journal J. Bacteriol. (1990) 172:4392-4398 !$#title Molecular cloning and physical and functional !1characterization of the Salmonella typhimurium and !1Salmonella typhi galactose utilization operons. !$#cross-references MUID:90330544; PMID:2198256 !$#accession A37760 !'##status preliminary !'##molecule_type DNA !'##residues 1-337 ##label HOU !'##cross-references GB:M33681; NID:g154046; PIDN:AAA27111.1; !1PID:g154047 CLASSIFICATION #superfamily Escherichia coli UDPglucose 4-epimerase; !1UDPglucose 4-epimerase homology KEYWORDS isomerase FEATURE !$3-335 #domain UDPglucose 4-epimerase homology #label UDP SUMMARY #length 337 #molecular-weight 36884 #checksum 8190 SEQUENCE /// ENTRY S51328 #type complete TITLE UDPglucose 4-epimerase (EC 5.1.3.2) - Salmonella typhi ALTERNATE_NAMES UDPgalactose 4-epimerase ORGANISM #formal_name Salmonella typhi DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S51328 REFERENCE S51328 !$#authors McKenna, A.J.; Bygraves, J.A.; Maiden, M.C.J.; Feavers, I.M. !$#submission submitted to the EMBL Data Library, January 1995 !$#description Molecular genetical characterization of the attenuated !1typhoid vaccine Salmonella typhi Ty21a. !$#accession S51328 !'##status preliminary !'##molecule_type DNA !'##residues 1-338 ##label MCK !'##cross-references EMBL:X83927; NID:g634102; PIDN:CAA58779.1; !1PID:g634103 GENETICS !$#gene galE CLASSIFICATION #superfamily Escherichia coli UDPglucose 4-epimerase; !1UDPglucose 4-epimerase homology KEYWORDS galactose metabolism; isomerase FEATURE !$3-336 #domain UDPglucose 4-epimerase homology #label UDP SUMMARY #length 338 #molecular-weight 37110 #checksum 2659 SEQUENCE /// ENTRY A36951 #type complete TITLE UDPglucose 4-epimerase (EC 5.1.3.2) - Erwinia amylovora ALTERNATE_NAMES UDPgalactose 4-epimerase ORGANISM #formal_name Erwinia amylovora DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A36951 REFERENCE A36951 !$#authors Metzger, M.; Bellemann, P.; Bugert, P.; Geider, K. !$#journal J. Bacteriol. (1994) 176:450-459 !$#title Genetics of galactose metabolism of Erwinia amylovora and !1its influence on polysaccharide synthesis and virulence of !1the fire blight pathogen. !$#cross-references MUID:94117381; PMID:7507102 !$#accession A36951 !'##status preliminary !'##molecule_type DNA !'##residues 1-337 ##label MET !'##cross-references GB:X76172; NID:g429077; PIDN:CAA53767.1; !1PID:g429078 !'##note authors translated the codon CAA for residue 22 as Glu, CAA for !1residue 98 as Glu, CAA for residue 118 as Glu, CAG for !1residue 158 as Glu, CAG for residue 188 as Glu, CAG for !1residue 206 as Glu, CAG for residue 287 as Glu, CAG for !1residue 329 as Glu, CAG for residue 331 as Glu, and CAG for !1residue 334 as Glu CLASSIFICATION #superfamily Escherichia coli UDPglucose 4-epimerase; !1UDPglucose 4-epimerase homology KEYWORDS galactose metabolism; isomerase FEATURE !$3-336 #domain UDPglucose 4-epimerase homology #label UDP SUMMARY #length 337 #molecular-weight 36684 #checksum 4289 SEQUENCE /// ENTRY S34984 #type complete TITLE UDPglucose 4-epimerase (EC 5.1.3.2) - Neisseria gonorrhoeae ALTERNATE_NAMES UDPgalactose 4-epimerase ORGANISM #formal_name Neisseria gonorrhoeae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S34984; S28646 REFERENCE S34984 !$#authors Robertson, B.D.; Frosch, M.; van Putten, J.P.M. !$#journal Mol. Microbiol. (1993) 8:891-901 !$#title The role of galE in the biosynthesis and function of !1gonococcal lipopolysaccharide. !$#cross-references MUID:93360819; PMID:8355614 !$#accession S34984 !'##molecule_type DNA !'##residues 1-338 ##label ROB !'##cross-references EMBL:Z21508; NID:g1050924; PIDN:CAA79721.1; !1PID:g1051296 GENETICS !$#gene galE CLASSIFICATION #superfamily Escherichia coli UDPglucose 4-epimerase; !1UDPglucose 4-epimerase homology KEYWORDS galactose metabolism; isomerase FEATURE !$3-336 #domain UDPglucose 4-epimerase homology #label UDP SUMMARY #length 338 #molecular-weight 36885 #checksum 1530 SEQUENCE /// ENTRY S39638 #type complete TITLE UDPglucose 4-epimerase (EC 5.1.3.2) galE NMB0064 [similarity] - Neisseria meningitidis (strain MC58) ALTERNATE_NAMES UDPgalactose 4-epimerase ORGANISM #formal_name Neisseria meningitidis #variety strain MC58 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S39638; G81240 REFERENCE S39638 !$#authors Jennings, M.P.; van der Ley, P.; Wilks, K.E.; Maskell, D.J.; !1Poolman, J.T.; Moxon, E.R. !$#journal Mol. Microbiol. (1993) 10:361-369 !$#title Cloning and molecular analysis of the galE gene of Neisseria !1meningitidis and its role in lipopolysaccharide !1biosynthesis. !$#cross-references MUID:95020536; PMID:7934827 !$#accession S39638 !'##molecule_type DNA !'##residues 1-339 ##label JEN !'##cross-references EMBL:L20495; NID:g406094; PIDN:AAA65535.1; !1PID:g406095 !'##experimental_source strain MC58; clone pKW1 REFERENCE A81000 !$#authors Tettelin, H.; Saunders, N.J.; Heidelberg, J.; Jeffries, !1A.C.; Nelson, K.E.; Eisen, J.A.; Ketchum, K.A.; Hood, D.W.; !1Peden, J.F.; Dodson, R.J.; Nelson, W.C.; Gwinn, M.L.; DeBoy, !1R.; Peterson, J.D.; Hickey, E.K.; Haft, D.H.; Salzberg, !1S.L.; White, O.; Fleischmann, R.D.; Dougherty, B.A.; Mason, !1T.; Ciecko, A.; Parksey, D.S.; Blair, E.; Cittone, H.; !1Clark, E.B.; Cotton, M.D.; Utterback, T.R.; Khouri, H.; Qin, !1H.; Vamathevan, J.; Gill, J.; Scarlato, V.; Masignani, V.; !1Pizza, M.; Grandi, G.; Sun, L.; Smith, H.O.; Fraser, C.M.; !1Moxon, E.R.; Rappuoli, R.; Venter, J.C. !$#journal Science (2000) 287:1809-1815 !$#title Complete genome sequence of Neisseria meningitidis serogroup !1B strain MC58. !$#cross-references MUID:20175755; PMID:10710307 !$#accession G81240 !'##molecule_type DNA !'##residues 1-339 ##label TET !'##cross-references GB:AE002366; GB:AE002098; NID:g7225284; !1PIDN:AAF40532.1; PID:g7225285; GSPDB:GN00119; TIGR:NMB0064 !'##experimental_source serogroup B, strain MC58 GENETICS !$#gene galE; NMB0064 CLASSIFICATION #superfamily Escherichia coli UDPglucose 4-epimerase; !1UDPglucose 4-epimerase homology KEYWORDS galactose metabolism; isomerase FEATURE !$4-337 #domain UDPglucose 4-epimerase homology #label UDP SUMMARY #length 339 #molecular-weight 37062 #checksum 5214 SEQUENCE /// ENTRY S70744 #type complete TITLE UDPglucose 4-epimerase (EC 5.1.3.2) - Yersinia enterocolitica ALTERNATE_NAMES UDPgalactose 4-epimerase ORGANISM #formal_name Yersinia enterocolitica DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S70744; S51268 REFERENCE S70734 !$#authors Skurnik, M.; Venho, R.; Toivanen, P.; Al-Hendy, A. !$#journal Mol. Microbiol. (1995) 17:575-594 !$#title A novel locus of Yersinia enterocolitica serotype O:3 !1involved in lipopolysaccharide outer core biosynthesis. !$#cross-references MUID:96100456; PMID:8559076 !$#accession S70744 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-336 ##label SKU !'##cross-references EMBL:Z47767; NID:g633689; PIDN:CAA87706.1; !1PID:g633700 !'##experimental_source strain 6471/76 serotype O:3 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1995 GENETICS !$#gene galE CLASSIFICATION #superfamily Escherichia coli UDPglucose 4-epimerase; !1UDPglucose 4-epimerase homology KEYWORDS galactose metabolism; isomerase; lipopolysaccharide core !1biosynthesis FEATURE !$3-334 #domain UDPglucose 4-epimerase homology #label UDP SUMMARY #length 336 #molecular-weight 37057 #checksum 5774 SEQUENCE /// ENTRY A64063 #type complete TITLE UDPglucose 4-epimerase (EC 5.1.3.2) - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES UDPgalactose 4-epimerase ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A64063; S15288 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession A64063 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-338 ##label TIGR !'##cross-references GB:U32719; GB:L42023; NID:g1573310; !1PIDN:AAC22012.1; PID:g1573321; TIGR:HI0351 !'##experimental_source strain Rd KW20 REFERENCE S15287 !$#authors Maskell, D.J.; Szabo, M.J.; Butler, P.D.; Williams, A.E.; !1Moxon, E.R. !$#journal Mol. Microbiol. (1991) 5:1013-1022 !$#title Molecular analysis of a complex locus from Haemophilus !1influenzae involved in phase-variable lipopolysaccharide !1biosynthesis. !$#cross-references MUID:92065797; PMID:1956282 !$#accession S15288 !'##molecule_type DNA !'##residues 1-284,'P',286-332,'S',334-338 ##label MAS !'##cross-references EMBL:X57315; NID:g43587; PIDN:CAA40568.1; !1PID:g43589 !'##experimental_source strain RM7004 GENETICS !$#gene galE CLASSIFICATION #superfamily Escherichia coli UDPglucose 4-epimerase; !1UDPglucose 4-epimerase homology KEYWORDS galactose metabolism; isomerase FEATURE !$3-336 #domain UDPglucose 4-epimerase homology #label UDP SUMMARY #length 338 #molecular-weight 37165 #checksum 8845 SEQUENCE /// ENTRY A44509 #type complete TITLE UDPglucose 4-epimerase (EC 5.1.3.2) - Streptococcus thermophilus ALTERNATE_NAMES UDPgalactose 4-epimerase ORGANISM #formal_name Streptococcus thermophilus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A44509 REFERENCE A44509 !$#authors Poolman, B.; Royer, T.J.; Mainzer, S.E.; Schmidt, B.F. !$#journal J. Bacteriol. (1990) 172:4037-4047 !$#title Carbohydrate utilization in Streptococcus thermophilus: !1characterization of the genes for aldose 1-epimerase !1(mutarotase) and UDPglucose 4-epimerase. !$#cross-references MUID:90299833; PMID:1694527 !$#accession A44509 !'##status preliminary !'##molecule_type DNA !'##residues 1-332 ##label POO !'##cross-references EMBL:M38175; NID:g153748; PIDN:AAA26944.1; !1PID:g153749 CLASSIFICATION #superfamily Escherichia coli UDPglucose 4-epimerase; !1UDPglucose 4-epimerase homology KEYWORDS galactose metabolism; isomerase FEATURE !$3-328 #domain UDPglucose 4-epimerase homology #label UDP SUMMARY #length 332 #molecular-weight 36940 #checksum 6679 SEQUENCE /// ENTRY S16300 #type complete TITLE UDPglucose 4-epimerase (EC 5.1.3.2) - Rhizobium meliloti ALTERNATE_NAMES UDPgalactose 4-epimerase ORGANISM #formal_name Rhizobium meliloti DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S16300; S60181 REFERENCE S16299 !$#authors Buendia, A.M.; Enenkel, B.; Koeplin, R.; Niehaus, K.; !1Arnold, W.; Puehler, A. !$#journal Mol. Microbiol. (1991) 5:1519-1530 !$#title The Rhizobium meliloti exoZ/exoB fragment of megaplasmid 2: !1exoB functions as a UDP-glucose 4-epimerase and exoZ shows !1homology to NodX of Rhizobium leguminosarum biovar viciae !1strain TOM. !$#cross-references MUID:92157879; PMID:1787800 !$#accession S16300 !'##molecule_type DNA !'##residues 1-328 ##label BUE !'##cross-references EMBL:X58126; NID:g46267; PIDN:CAA41127.1; !1PID:g581518 !'##note the authors translated the initiation codon GTG for residue 1 !1as Val REFERENCE S60181 !$#authors Becker, A.; Kuester, H.; Niehaus, K.; Puehler, A. !$#journal Mol. Gen. Genet. (1995) 249:487-497 !$#title Extension of the Rhizobium meliloti succinoglycan !1biosynthesis gene cluster: identification of the exsA gene !1encoding an ABC transporter protein, and the exsB gene which !1probably codes for a regulator of succinoglycan !1biosynthesis. !$#cross-references MUID:96133689; PMID:8544814 !$#accession S60181 !'##molecule_type DNA !'##residues 1-43 ##label BEC !'##cross-references EMBL:Z50189; NID:g1143532; PIDN:CAA90567.1; !1PID:g1143533 GENETICS !$#gene exoB !$#start_codon GTG CLASSIFICATION #superfamily Escherichia coli UDPglucose 4-epimerase; !1UDPglucose 4-epimerase homology KEYWORDS galactose metabolism; isomerase FEATURE !$6-328 #domain UDPglucose 4-epimerase homology #label UDP SUMMARY #length 328 #molecular-weight 36112 #checksum 7088 SEQUENCE /// ENTRY XUSMUG #type complete TITLE UDPglucose 4-epimerase (EC 5.1.3.2) - Streptomyces sp. ALTERNATE_NAMES UDPgalactose 4-epimerase ORGANISM #formal_name Streptomyces sp. DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 28-May-1999 ACCESSIONS B28669 REFERENCE A28669 !$#authors Adams, C.W.; Fornwald, J.A.; Schmidt, F.J.; Rosenberg, M.; !1Brawner, M.E. !$#journal J. Bacteriol. (1988) 170:203-212 !$#title Gene organization and structure of the Streptomyces lividans !1gal operon. !$#cross-references MUID:88086869; PMID:3335481 !$#accession B28669 !'##molecule_type DNA !'##residues 1-319 ##label ADA !'##cross-references GB:M18953; NID:g153259; PIDN:AAA26747.1; !1PID:g153261 !'##note the source is designated as Streptomyces lividans GENETICS !$#gene galE CLASSIFICATION #superfamily Escherichia coli UDPglucose 4-epimerase; !1UDPglucose 4-epimerase homology KEYWORDS galactose metabolism; isomerase FEATURE !$5-319 #domain UDPglucose 4-epimerase homology #label UDP SUMMARY #length 319 #molecular-weight 34293 #checksum 3707 SEQUENCE /// ENTRY DWSMGG #type complete TITLE dTDPglucose 4,6-dehydratase (EC 4.2.1.46) [validated] - Streptomyces griseus ORGANISM #formal_name Streptomyces griseus DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 26-May-2000 ACCESSIONS S18617; S19784 REFERENCE S18617 !$#authors Pissowotzki, K.; Mansouri, K.; Piepersberg, W. !$#journal Mol. Gen. Genet. (1991) 231:113-123 !$#title Genetics of streptomycin production in Streptomyces griseus: !1molecular structure and putative function of genes !1strELMB2N. !$#cross-references MUID:92092953; PMID:1661369 !$#accession S18617 !'##molecule_type DNA !'##residues 1-328 ##label PIS !'##cross-references EMBL:X62567; NID:g49009; PIDN:CAA44444.1; !1PID:g581677 !'##note the sequence from Fig. 3 is inconsistent with that from Fig. 2 !1in having an additional Ala-Leu after 1-Met and in having !1271-Asp and 272-Glu !'##note the authors translated the initiation codon TTG for residue 1 !1as Leu GENETICS !$#gene strE !$#start_codon TTG FUNCTION !$#description EC 4.2.1.46 [validated, MUID:92092953] CLASSIFICATION #superfamily Escherichia coli UDPglucose 4-epimerase; !1UDPglucose 4-epimerase homology KEYWORDS carbon-oxygen lyase; hydro-lyase; streptomycin biosynthesis FEATURE !$5-317 #domain UDPglucose 4-epimerase homology #label UDP SUMMARY #length 328 #molecular-weight 35669 #checksum 1739 SEQUENCE /// ENTRY JC4066 #type complete TITLE ADPglyceromanno-heptose 6-epimerase (EC 5.1.3.20) rfaD VC0240 [similarity] - Vibrio cholerae (strain N16961 serogroup O1) ALTERNATE_NAMES ADP-L-glycero-D-mannoheptose-6-epimerase; rfaD protein ORGANISM #formal_name Vibrio cholerae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Feb-2001 ACCESSIONS JC4066; S70952; G82345; S28467 REFERENCE JC4066 !$#authors Stroeher, U.H.; Karageorgos, L.E.; Morona, R.; Manning, P.A. !$#journal Gene (1995) 155:67-72 !$#title In Vibrio cholerae serogroup O1, rfaD is closely linked to !1the rfb operon. !$#cross-references MUID:95212931; PMID:7698669 !$#contents Inaba and Ogawa serotypes, 569B and O17 !$#accession JC4066 !'##molecule_type DNA !'##residues 1-314 ##label STR !'##cross-references EMBL:X59554; NID:g48381; PIDN:CAA42133.1; !1PID:g48382 REFERENCE S70952 !$#authors Bik, E.M.; Bunschoten, A.E.; Willems, R.J.L.; Chang, A.C.Y.; !1Mooi, F.R. !$#journal Mol. Microbiol. (1996) 20:799-811 !$#title Genetic organization and functional analysis of the otn DNA !1essential for cell-wall polysaccharide synthesis in Vibrio !1cholerae O139. !$#cross-references MUID:96386047; PMID:8793876 !$#accession S70952 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-67,'S',69-314 ##label BIK !'##cross-references EMBL:X90547; NID:g1469276; PIDN:CAA62134.1; !1PID:g1107917 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1995 REFERENCE A82035 !$#authors Heidelberg, J.F.; Eisen, J.A.; Nelson, W.C.; Clayton, R.A.; !1Gwinn, M.L.; Dodson, R.J.; Haft, D.H.; Hickey, E.K.; !1Peterson, J.D.; Umayam, L.A.; Gill, S.R.; Nelson, K.E.; !1Read, T.D.; Tettelin, H.; Richardson, D.; Ermolaeva, M.D.; !1Vamathevan, J.; Bass, S.; Qin, H.; Dragoi, I.; Sellers, P.; !1McDonald, L.; Utterback, T.; Fleishmann, R.D.; Nierman, !1W.C.; White, O.; Salzberg, S.L.; Smith, H.O.; Colwell, R.R.; !1Mekalanos, J.J.; Venter, J.C.; Fraser, C.M. !$#journal Nature (2000) 406:477-483 !$#title DNA Sequence of both chromosomes of the cholera pathogen !1Vibrio cholerae. !$#cross-references MUID:20406833; PMID:10952301 !$#accession G82345 !'##status preliminary !'##molecule_type DNA !'##residues 1-314 ##label HEI !'##cross-references GB:AE004113; GB:AE003852; NID:g9654648; !1PIDN:AAF93416.1; GSPDB:GN00126; TIGR:VC0240 !'##experimental_source serogroup O1; strain N16961; biotype El Tor COMMENT This enzyme is required for the biosynthesis of the !1lipopolysaccharide precursor ADP-L-glycero-D-mannoheptose, !1associated with production of the core oligosaccharide. GENETICS !$#gene rfaD; VC0240 !$#map_position 1 CLASSIFICATION #superfamily ADPglyceromanno-heptose 6-epimerase; UDPglucose !14-epimerase homology KEYWORDS isomerase FEATURE !$7-12 #region helix-turn-helix SUMMARY #length 314 #molecular-weight 35244 #checksum 6370 SEQUENCE /// ENTRY F64183 #type complete TITLE ADPglyceromanno-heptose 6-epimerase (EC 5.1.3.20) HI1114 [similarity] - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F64183 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession F64183 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-308 ##label TIGR !'##cross-references GB:U32791; GB:L42023; NID:g1574662; !1PIDN:AAC22768.1; PID:g1574668; TIGR:HI1114 CLASSIFICATION #superfamily ADPglyceromanno-heptose 6-epimerase; UDPglucose !14-epimerase homology KEYWORDS isomerase SUMMARY #length 308 #molecular-weight 34781 #checksum 7674 SEQUENCE /// ENTRY JU0299 #type complete TITLE ADPglyceromanno-heptose 6-epimerase (EC 5.1.3.20) rfaD [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS JU0299; A30500; S47840; S16461; E65162 REFERENCE JU0299 !$#authors Pegues, J.C.; Chen, L.; Gordon, A.W.; Ding, L.; Coleman Jr., !1W.G. !$#journal J. Bacteriol. (1990) 172:4652-4660 !$#title Cloning, expression, and characterization of the Escherichia !1coli K-12 rfaD gene. !$#cross-references MUID:90330578; PMID:2198271 !$#accession JU0299 !'##molecule_type DNA !'##residues 1-310 ##label PEG !'##cross-references GB:M33577; NID:g147575; PIDN:AAA24525.1; !1PID:g147576 !'##experimental_source strain K-12 !$#accession A30500 !'##molecule_type protein !'##residues 1-34 ##label PE2 REFERENCE S47666 !$#authors Plunkett, G. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S47840 !'##status preliminary !'##molecule_type DNA !'##residues 1-310 ##label PLU !'##cross-references EMBL:U00039; NID:g466582; PIDN:AAB18596.1; !1PID:g466757 REFERENCE S16461 !$#authors Raina, S.; Georgopoulos, C. !$#journal Nucleic Acids Res. (1991) 19:3811-3819 !$#title The htrM gene, whose product is essential for Escherichia !1coli viability only at elevated temperatures, is identical !1to the rfaD gene. !$#cross-references MUID:91319536; PMID:1861974 !$#accession S16461 !'##status preliminary !'##molecule_type DNA !'##residues 1-310 ##label RAI !'##cross-references EMBL:X54492; NID:g41762; PIDN:CAA38364.1; !1PID:g41763 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65162 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-310 ##label BLAT !'##cross-references GB:AE000440; GB:U00096; NID:g2367252; !1PIDN:AAC76643.1; PID:g1790049; UWGP:b3619 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene rfaD; htrM !$#map_position 81 min FUNCTION !$#description catalyzes the conversion of ADP-D-glycero-D-mannoheptose to !1ADP-L-glycero-D-mannoheptose CLASSIFICATION #superfamily ADPglyceromanno-heptose 6-epimerase; UDPglucose !14-epimerase homology KEYWORDS isomerase FEATURE !$2-16 #region ADP binding #status predicted SUMMARY #length 310 #molecular-weight 34893 #checksum 2731 SEQUENCE /// ENTRY G70330 #type complete TITLE ADPglyceromanno-heptose 6-epimerase (EC 5.1.3.20) rfaD [similarity] - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS G70330 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession G70330 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-310 ##label AQF !'##cross-references GB:AE000684; NID:g2983009; PIDN:AAC06623.1; !1PID:g2983012; GB:AE000657 !'##experimental_source strain VF5 GENETICS !$#gene rfaD CLASSIFICATION #superfamily ADPglyceromanno-heptose 6-epimerase; UDPglucose !14-epimerase homology KEYWORDS isomerase FEATURE !$3-310 #domain UDPglucose 4-epimerase homology #label UDP SUMMARY #length 310 #molecular-weight 35917 #checksum 2154 SEQUENCE /// ENTRY S72623 #type complete TITLE ribulose-5-phosphate-epimerase (EC 5.1.-.-) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES POS18 protein; protein J0731; protein YJL121c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 12-Nov-1999 ACCESSIONS S72623; S51587; S56902 REFERENCE S72623 !$#authors Juhnke, H.; Krems, B.; Koetter, P.; Entian, K.D. !$#journal Mol. Gen. Genet. (1996) 252:456-464 !$#title Mutant that show increased sensitivity to hydrogen peroxide !1reveal an important role for the pentose phosphate pathway !1in protection of yeast against oxidative stress. !$#cross-references MUID:97033550; PMID:8879247 !$#accession S72623 !'##molecule_type DNA !'##residues 1-238 ##label JUH !'##cross-references EMBL:X83571; NID:g609673; PIDN:CAA58554.1; !1PID:g609674 REFERENCE S51587 !$#authors Juhnke, H. !$#submission submitted to the EMBL Data Library, December 1994 !$#accession S51587 !'##molecule_type DNA !'##residues 1-238 ##label JU2 !'##cross-references EMBL:X83571; NID:g609673; PIDN:CAA58554.1; !1PID:g609674 REFERENCE S56891 !$#authors Cziepluch, C.; Kordes, E.; Pujol, A.; Jauniaux, J.C. !$#submission submitted to the Protein Sequence Database, September 1995 !$#accession S56902 !'##molecule_type DNA !'##residues 1-238 ##label CZI !'##cross-references EMBL:Z49396; NID:g1008312; PIDN:CAA89415.1; !1PID:g1008313; GSPDB:GN00010; MIPS:YJL121c GENETICS !$#gene SGD:RPE1; POS18; SGD:S0003657 !'##cross-references MIPS:YJL121c; SGD:S0003657 !$#map_position 10L CLASSIFICATION #superfamily yeast ribulose-5-phosphate-epimerase KEYWORDS carbohydrate metabolism; isomerase; leucine zipper SUMMARY #length 238 #molecular-weight 25967 #checksum 706 SEQUENCE /// ENTRY XEBYUG #type complete TITLE UDPglucose 4-epimerase (EC 5.1.3.2) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YBR019c; protein YBR0301; uridinediphosphoglucose 4-epimerase ORGANISM #formal_name Saccharomyces cerevisiae DATE 17-Mar-1987 #sequence_revision 09-Sep-1994 #text_change 05-Nov-1999 ACCESSIONS S45875; S45874; S50814; S42761; S42760; A01177; S50323 REFERENCE S45875 !$#authors Grivell, L.A.; de Haan, M.; Maat, M.J.; Smits, P.H.M. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S45875 !'##molecule_type DNA !'##residues 1-500 ##label GRI !'##cross-references EMBL:Z35888; GSPDB:GN00002; MIPS:YBR019c !'##experimental_source strain S288C REFERENCE S45862 !$#authors Entian, K.D.; Koetter, P.; Rose, M.; Li, Z.; Thermann, R.; !1Brendel, M.; Baur, A.; Boles, E.; Miosga, T.; !1Schaaff-Gerstenschlaeger, I.; Zimmermann, F.K. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S45874 !'##molecule_type DNA !'##residues 134-699 ##label ENT !'##cross-references EMBL:Z35888; GSPDB:GN00002; MIPS:YBR019c !'##experimental_source strain S288C REFERENCE S50812 !$#authors Schaaff-Gerstenschlaeger, I.; Schindwolf, T.; Lehnert, W.; !1Rose, M.; Zimmermann, F.K. !$#journal Yeast (1995) 11:79-83 !$#title Sequence and functional analysis of a 7.2 kb fragment of !1Saccharomyces cerevisiae chromosome II including GAL7 and !1GAL10 and a new essential open reading frame. !$#cross-references MUID:95282516; PMID:7762304 !$#accession S50814 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 134-699 ##label SCW !'##cross-references EMBL:X81324; NID:g587572; PIDN:CAA57106.1; !1PID:g587575 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1September 1994 REFERENCE S23294 !$#authors Johnston, M.; Davis, R.W. !$#journal Mol. Cell. Biol. (1984) 4:1440-1448 !$#title Sequences that regulate the divergent GAL1-GAL10 promoter in !1Saccharomyces cerevisiae. !$#cross-references MUID:85036279; PMID:6092912 !$#accession S42761 !'##status translation not shown !'##molecule_type DNA !'##residues 1-46 ##label JOH !'##cross-references EMBL:K02115 REFERENCE S05811 !$#authors Tajima, M.; Nogi, Y.; Fukasawa, T. !$#journal Yeast (1985) 1:67-77 !$#title Primary structure of the Saccharomyces cerevisiae GAL7 gene. !$#cross-references MUID:89131252; PMID:2851900 !$#accession S42760 !'##molecule_type DNA !'##residues 630-699 ##label TAJ !'##cross-references EMBL:M12348 REFERENCE A91795 !$#authors Citron, B.A.; Donelson, J.E. !$#journal J. Bacteriol. (1984) 158:269-278 !$#title Sequence of the Saccharomyces GAL region and its !1transcription in vivo. !$#cross-references MUID:84185433; PMID:6715281 !$#accession A01177 !'##molecule_type DNA !'##residues 1-46;'SWSSVR',307-463,'L',465-478,'NY',481-497,'Q',499-517, !1'I',519-666,'C',668-693,'TL',696-699 ##label CIT !'##cross-references EMBL:K01609 !'##note the source is designated as Saccharomyces carlbergensis GENETICS !$#gene SGD:GAL10; MIPS:YBR019c !'##cross-references SGD:S0000223; MIPS:YBR019c !$#map_position 2R FUNCTION !$#description isomerase CLASSIFICATION #superfamily yeast UDPglucose 4-epimerase; UDPglucose !14-epimerase homology KEYWORDS isomerase FEATURE !$14-355 #domain UDPglucose 4-epimerase homology #label UDP SUMMARY #length 699 #molecular-weight 78195 #checksum 2712 SEQUENCE /// ENTRY XUVKG #type complete TITLE UDPglucose 4-epimerase (EC 5.1.3.2) - yeast (Kluyveromyces marxianus var. lactis) ALTERNATE_NAMES UDPgalactose 4-epimerase ORGANISM #formal_name Kluyveromyces marxianus var. lactis, Candida sphaerica DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 18-Jun-1999 ACCESSIONS S01407 REFERENCE S01407 !$#authors Webster, T.D.; Dickson, R.C. !$#journal Nucleic Acids Res. (1988) 16:8192-8194 !$#title Nucleotide sequence of the galactose gene cluster of !1Kluyveromyces lactis. !$#cross-references MUID:88335573; PMID:3419917 !$#accession S01407 !'##molecule_type DNA !'##residues 1-687 ##label WEB !'##cross-references EMBL:X07039; NID:g2817; PIDN:CAA30090.1; PID:g2819 GENETICS !$#gene GAL10 CLASSIFICATION #superfamily yeast UDPglucose 4-epimerase; UDPglucose !14-epimerase homology KEYWORDS galactose metabolism; isomerase FEATURE !$7-343 #domain UDPglucose 4-epimerase homology #label UDP SUMMARY #length 687 #molecular-weight 76252 #checksum 190 SEQUENCE /// ENTRY S29621 #type complete TITLE UDPglucose 4-epimerase (EC 5.1.3.2) - yeast (Pachysolen tannophilus) ALTERNATE_NAMES UDPgalactose 4-epimerase ORGANISM #formal_name Pachysolen tannophilus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S29621 REFERENCE S29621 !$#authors Skrzypek, M.; Maleszka, R. !$#submission submitted to the EMBL Data Library, October 1992 !$#description Cloning and sequencing of the UDP-galactose-4-epimerase gene !1from Pachysolen tannophilus. !$#accession S29621 !'##molecule_type DNA !'##residues 1-689 ##label SKR !'##cross-references EMBL:X68593; NID:g3264; PIDN:CAA48580.1; PID:g3265 GENETICS !$#gene GAL10 CLASSIFICATION #superfamily yeast UDPglucose 4-epimerase; UDPglucose !14-epimerase homology KEYWORDS galactose metabolism; isomerase FEATURE !$4-343 #domain UDPglucose 4-epimerase homology #label UDP SUMMARY #length 689 #molecular-weight 76670 #checksum 642 SEQUENCE /// ENTRY ISECP4 #type complete TITLE L-ribulose-phosphate 4-epimerase (EC 5.1.3.4) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS E64727; D29022; S13593; S40577; S19260; A38289; A36236; !1JH0221 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64727 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-231 ##label BLAT !'##cross-references GB:AE000116; GB:U00096; NID:g1786240; !1PIDN:AAC73172.1; PID:g1786247; UWGP:b0061 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A91559 !$#authors Lee, N.; Gielow, W.; Martin, R.; Hamilton, E.; Fowler, A. !$#journal Gene (1986) 47:231-244 !$#title The organization of the araBAD operon of Escherichia coli. !$#cross-references MUID:87163495; PMID:3549454 !$#accession D29022 !'##molecule_type DNA !'##residues 1-49,'I',51-69,'A',71-215,'N',217-231 ##label LEE !'##cross-references GB:M15263; NID:g145303; PIDN:AAA23464.1; !1PID:g145306 REFERENCE JH0221 !$#authors Mineno, J.; Fukui, H.; Ishino, Y.; Kato, I.; Shinagawa, H. !$#journal Nucleic Acids Res. (1990) 18:6722 !$#title Nucleotide sequence of the araD gene of Escherichia coli K12 !1encoding the L-ribulose 5-phosphate 4-epimerase. !$#cross-references MUID:91067495; PMID:2251150 !$#accession S13593 !'##molecule_type DNA !'##residues 1-231 ##label MIN !'##cross-references EMBL:X56048; NID:g40938; PIDN:CAA39519.1; !1PID:g40939 !'##experimental_source strain K-12 !'##note the authors translated the codon GAG for residue 192 as Arg REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40577 !'##molecule_type DNA !'##residues 1-231 ##label YUR !'##cross-references EMBL:D10483; NID:g216434; PIDN:BAA01332.1; !1PID:g216481 !'##experimental_source strain K-12 REFERENCE S15943 !$#authors Iwasaki, H.; Ishino, Y.; Toh, H.; Nakata, A.; Shinagawa, H. !$#journal Mol. Gen. Genet. (1991) 226:24-33 !$#title Escherichia coli DNA polymerase II is homologous to !1alpha-like DNA polymerases. !$#cross-references MUID:91238699; PMID:2034216 !$#accession S19260 !'##molecule_type DNA !'##residues 158-231 ##label IWA !'##cross-references EMBL:X54847; NID:g42462 !'##experimental_source strain K-12, substrain W3110 REFERENCE JQ0780 !$#authors Bonner, C.A.; Hays, S.; McEntee, K.; Goodman, M.F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:7663-7667 !$#title DNA polymerase II is encoded by the DNA damage-inducible !1dinA gene of Escherichia coli. !$#cross-references MUID:91017565; PMID:2217198 !$#accession A38289 !'##molecule_type DNA !'##residues 222-231 ##label BON !'##cross-references GB:M37727; NID:g145744; PIDN:AAA23683.1; !1PID:g145745 REFERENCE A36236 !$#authors Chen, H.; Sun, Y.; Stark, T.; Beattie, W.; Moses, R.E. !$#journal DNA Cell Biol. (1990) 9:631-635 !$#title Nucleotide sequence and deletion analysis of the polB gene !1of Escherichia coli. !$#cross-references MUID:91083835; PMID:2261080 !$#accession A36236 !'##molecule_type DNA !'##residues 1-231 ##label CHE !'##cross-references GB:M35371 COMMENT This enzyme catalyzes the conversion of L-ribulose !15-phosphate to D-xylulose 5-phosphate, the third step in the !1metabolism of L-arabinose in E. coli. GENETICS !$#gene araD !$#map_position 1 min FUNCTION !$#description catalyzes the isomerization of L-ribulose 5-phosphate to !1D-xylulose 5-phosaphate CLASSIFICATION #superfamily L-ribulose-phosphate 4-epimerase KEYWORDS arabinose metabolism; isomerase; zinc FEATURE !$76,95,97,171 #binding_site zinc (Asp, His, His, His) #status !8predicted SUMMARY #length 231 #molecular-weight 25519 #checksum 5476 SEQUENCE /// ENTRY ISEB4T #type complete TITLE L-ribulose-phosphate 4-epimerase (EC 5.1.3.4) - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 18-Jun-1999 ACCESSIONS A24986 REFERENCE A24986 !$#authors Lin, H.C.; Lei, S.P.; Studnicka, G.; Wilcox, G. !$#journal Gene (1985) 34:129-134 !$#title The araBAD operon of Salmonella typhimurium LT2. III. !1Nucleotide sequence of araD and its flanking regions, and !1primary structure of its product, L-ribulose-5-phosphate !14-epimerase. !$#cross-references MUID:85232046; PMID:3891514 !$#accession A24986 !'##molecule_type DNA !'##residues 1-248 ##label LIN !'##cross-references GB:M11047; GB:M11045; GB:M11046; NID:g153866; !1PIDN:AAA27025.1; PID:g153869 !'##experimental_source LT2 COMMENT This enzyme catalyzes the conversion of L-ribulose !15-phosphate to D-xylulose 5-phosphate. GENETICS !$#gene araD FUNCTION !$#description catalyzes the isomerization of L-ribulose 5-phosphate to !1D-xylulose 5-phosaphate CLASSIFICATION #superfamily L-ribulose-phosphate 4-epimerase KEYWORDS arabinose metabolism; isomerase; zinc FEATURE !$76,95,97,171 #binding_site zinc (Asp, His, His, His) #status !8predicted SUMMARY #length 248 #molecular-weight 27089 #checksum 2299 SEQUENCE /// ENTRY ADECFP #type complete TITLE L-fuculose-phosphate aldolase (EC 4.1.2.17) [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 01-Mar-2002 ACCESSIONS B33495; B32883; S04703; D65062; PV0013 REFERENCE A33495 !$#authors Chen, Y.M.; Lu, Z.; Lin, E.C.C. !$#journal J. Bacteriol. (1989) 171:6097-6105 !$#title Constitutive activation of the fucAO operon and silencing of !1the divergently transcribed fucPIK operon by an IS5 element !1in Escherichia coli mutants selected for growth on L-1, !12-propanediol. !$#cross-references MUID:90036697; PMID:2553671 !$#accession B33495 !'##molecule_type DNA !'##residues 1-215 ##label CHE !'##cross-references GB:M31059; NID:g146040; PIDN:AAA23823.1; !1PID:g146042 REFERENCE A32883 !$#authors Conway, T.; Ingram, L.O. !$#journal J. Bacteriol. (1989) 171:3754-3759 !$#title Similarity of Escherichia coli propanediol oxidoreductase !1(fucO product) and an unusual alcohol dehydrogenase from !1Zymomonas mobilis and Saccharomyces cerevisiae. !$#cross-references MUID:89291720; PMID:2661535 !$#accession B32883 !'##molecule_type DNA !'##residues 108-215 ##label CON REFERENCE S04702 !$#authors Lu, Z.; Lin, E.C.C. !$#journal Nucleic Acids Res. (1989) 17:4883-4884 !$#title The nucleotide sequence of Escherichia coli genes for !1L-fucose dissimilation. !$#cross-references MUID:89315234; PMID:2664711 !$#accession S04703 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-215 ##label LUZ !'##cross-references EMBL:X15025; NID:g41501; PIDN:CAA33125.1; !1PID:g41503 !'##note this sequence was submitted to EMBL, April 1989 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65062 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-215 ##label BLAT !'##cross-references GB:AE000363; GB:U00096; NID:g1789153; !1PIDN:AAC75842.1; PID:g1789164; UWGP:b2800 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A67347 !$#authors Dreyer, M.K.; Schulz, G.E. !$#submission submitted to the Brookhaven Protein Data Bank, February 1996 !$#cross-references PDB:4FUA !$#contents annotation; X-ray crystallography, 2.13 angstroms, residues !11-206 REFERENCE A59078 !$#authors Dreyer, M.K.; Schulz, G.E. !$#journal J. Mol. Biol. (1993) 231:549-553 !$#title The spatial structure of the class II L-fuculose-1-phosphate !1aldolase from Escherichia coli. !$#cross-references MUID:93294819; PMID:8515438 !$#contents annotation; X-ray crystallography, 2.13 angstroms GENETICS !$#gene fucA !$#map_position 60 min COMPLEX homotetramer [validated, MUID:93294819] FUNCTION !$#description EC 4.1.2.17 [validated, MUID:93294819]; L-fuculose-phosphate !1aldolase; catalyzes the formation of dihydroxyacetone !1phosphate and L-lactaldehyde from L-fuculose-phosphate !$#note activity depends on the presence of metal ions (Zn2+); !1belongs to the class II aldolases CLASSIFICATION #superfamily L-ribulose-phosphate 4-epimerase KEYWORDS aldehyde-lyase; carbon-carbon lyase; zinc FEATURE !$29,43,44,71,72 #binding_site substrate (Asn, Thr, Gly, Ser, Ser) !8#status experimental\ !$73,92,94,155 #binding_site zinc, catalytic (Glu, His, His, His) !8#status experimental\ !$113 #active_site Tyr #status experimental SUMMARY #length 215 #molecular-weight 23775 #checksum 2079 SEQUENCE /// ENTRY C64081 #type complete TITLE L-fuculose-phosphate aldolase (EC 4.1.2.17) - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 15-Oct-1999 ACCESSIONS C64081 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession C64081 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-216 ##label TIGR !'##cross-references GB:U32743; GB:L42023; NID:g1573597; !1PIDN:AAC22270.1; PID:g1573604; TIGR:HI0611 CLASSIFICATION #superfamily L-ribulose-phosphate 4-epimerase KEYWORDS aldehyde-lyase; carbon-carbon lyase SUMMARY #length 216 #molecular-weight 23944 #checksum 6219 SEQUENCE /// ENTRY E71241 #type complete TITLE L-fuculose-phosphate aldolase (EC 4.1.2.17) - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 21-Jul-2000 ACCESSIONS E71241 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession E71241 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-189 ##label KAW !'##cross-references GB:AP000001; NID:g3236128; PIDN:BAA29260.1; !1PID:g3256577 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0191 CLASSIFICATION #superfamily L-ribulose-phosphate 4-epimerase KEYWORDS aldehyde-lyase; carbon-carbon lyase SUMMARY #length 189 #molecular-weight 21256 #checksum 4976 SEQUENCE /// ENTRY C75206 #type complete TITLE L-fuculose-phosphate aldolase (EC 4.1.2.17) - Pyrococcus abyssi (strain Orsay) ORGANISM #formal_name Pyrococcus abyssi DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 16-Jun-2000 ACCESSIONS C75206 REFERENCE A75001 !$#authors anonymous, Genoscope !$#submission submitted to the EMBL Data Library, July 1999 !$#description Pyrococcus abyssi genome sequence: insights into archaeal !1chromosome structure and evolution. !$#accession C75206 !'##status preliminary !'##molecule_type DNA !'##residues 1-194 ##label KAW !'##cross-references GB:AJ248283; GB:AL096836; NID:g5457433; !1PIDN:CAB49098.1; PID:g5457607 !'##experimental_source strain Orsay GENETICS !$#gene fucA; PAB0117 CLASSIFICATION #superfamily L-ribulose-phosphate 4-epimerase KEYWORDS aldehyde-lyase; carbon-carbon lyase SUMMARY #length 194 #molecular-weight 21905 #checksum 2973 SEQUENCE /// ENTRY F65054 #type complete TITLE L-fuculose-phosphate aldolase (EC 4.1.2.17) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 01-Mar-2002 ACCESSIONS F65054 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65054 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-212 ##label BLAT !'##cross-references GB:AE000357; GB:U00096; NID:g2367155; !1PIDN:AAC75780.1; PID:g1789094; UWGP:b2738 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily L-ribulose-phosphate 4-epimerase KEYWORDS aldehyde-lyase; carbon-carbon lyase SUMMARY #length 212 #molecular-weight 23222 #checksum 93 SEQUENCE /// ENTRY B64108 #type complete TITLE L-fuculose-phosphate aldolase (EC 4.1.2.17) - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 28-Jul-2000 ACCESSIONS B64108 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession B64108 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-210 ##label TIGR !'##cross-references GB:U32782; GB:L42023; NID:g1574041; !1PIDN:AAC22673.1; PID:g1574044; TIGR:HI1012 CLASSIFICATION #superfamily L-ribulose-phosphate 4-epimerase KEYWORDS aldehyde-lyase; carbon-carbon lyase SUMMARY #length 210 #molecular-weight 23242 #checksum 9438 SEQUENCE /// ENTRY A64477 #type complete TITLE L-fuculose-phosphate aldolase homolog - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 21-Jul-2000 ACCESSIONS A64477 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession A64477 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-181 ##label BUL !'##cross-references GB:U67582; GB:L77117; NID:g1592064; !1PIDN:AAB99428.1; PID:g1592067; TIGR:MJ1418 GENETICS !$#map_position FOR1381152-1381697 CLASSIFICATION #superfamily L-ribulose-phosphate 4-epimerase SUMMARY #length 181 #molecular-weight 20470 #checksum 6297 SEQUENCE /// ENTRY C69054 #type complete TITLE L-fuculose-phosphate aldolase homolog - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 21-Jul-2000 ACCESSIONS C69054 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession C69054 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-191 ##label MTH !'##cross-references GB:AE000903; GB:AE000666; NID:g2622514; !1PIDN:AAB85883.1; PID:g2622518 !'##experimental_source strain Delta H GENETICS !$#gene MTH1406 !$#start_codon GTG CLASSIFICATION #superfamily L-ribulose-phosphate 4-epimerase SUMMARY #length 191 #molecular-weight 20702 #checksum 1063 SEQUENCE /// ENTRY A72396 #type complete TITLE L-fuculose-phosphate aldolase homolog - Thermotoga maritima (strain MSB8) ORGANISM #formal_name Thermotoga maritima DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 21-Jul-2000 ACCESSIONS A72396 REFERENCE A72200 !$#authors Nelson, K.E.; Clayton, R.A.; Gill, S.R.; Gwinn, M.L.; !1Dodson, R.J.; Haft, D.H.; Hickey, E.K.; Peterson, J.D.; !1Nelson, W.C.; Ketchum, K.A.; McDonald, L.; Utterback, T.R.; !1Malek, J.A.; Linher, K.D.; Garrett, M.M.; Stewart, A.M.; !1Cotton, M.D.; Pratt, M.S.; Phillips, C.A.; Richardson, D.; !1Heidelberg, J.; Sutton, G.G.; Fleischmann, R.D.; White, O.; !1Salzberg, S.L.; Smith, H.O.; Venter, J.C.; Fraser, C.M. !$#journal Nature (1999) 399:323-329 !$#title Evidence for lateral gene transfer between Archaea and !1Bacteria from genome sequence of Thermotoga maritima. !$#cross-references MUID:99287316; PMID:10360571 !$#accession A72396 !'##status preliminary !'##molecule_type DNA !'##residues 1-254 ##label ARN !'##cross-references GB:AE001710; GB:AE000512; NID:g4980775; !1PIDN:AAD35371.1; PID:g4980781; TIGR:TM0283 !'##experimental_source strain MSB8 GENETICS !$#gene TM0283 CLASSIFICATION #superfamily L-ribulose-phosphate 4-epimerase SUMMARY #length 254 #molecular-weight 28182 #checksum 6924 SEQUENCE /// ENTRY E72546 #type complete TITLE L-fuculose-phosphate aldolase homolog - Aeropyrum pernix (strain K1) ORGANISM #formal_name Aeropyrum pernix DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 16-Jun-2000 ACCESSIONS E72546 REFERENCE A72450 !$#authors Kawarabayasi, Y.; Hino, Y.; Horikawa, H.; Yamazaki, S.; !1Haikawa, Y.; Jin-no, K.; Takahashi, M.; Sekine, M.; Baba, !1S.; Ankai, A.; Kosugi, H.; Hosoyama, A.; Fukui, S.; Nagai, !1Y.; Nishijima, K.; Nakazawa, H.; Takamiya, M.; Masuda, S.; !1Funahashi, T.; Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, !1N.; Oguchi, A.; Aoki, K.; Kubota, K.; Nakamura, Y.; Nomura, !1N.; Sako, Y.; Kikuchi, H. !$#journal DNA Res. (1999) 6:83-101 !$#title Complete genome sequence of an aerobic hyper-thermophilic !1Crenarchaeon, Aeropyrum pernix K1. !$#cross-references MUID:99310339; PMID:10382966 !$#accession E72546 !'##status preliminary !'##molecule_type DNA !'##residues 1-215 ##label KAW !'##cross-references DDBJ:AP000062; NID:g5105244; PIDN:BAA80658.1; !1PID:g5105345 !'##experimental_source strain K1 GENETICS !$#gene APE1657 CLASSIFICATION #superfamily L-ribulose-phosphate 4-epimerase SUMMARY #length 215 #molecular-weight 23110 #checksum 1323 SEQUENCE /// ENTRY B70645 #type complete TITLE L-fuculose-phosphate aldolase (EC 4.1.2.17) - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 16-Jun-2000 ACCESSIONS B70645 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession B70645 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-218 ##label COL !'##cross-references GB:Z84395; GB:AL123456; NID:g3261698; !1PIDN:CAB06473.1; PID:g3261699 !'##experimental_source strain H37Rv GENETICS !$#gene fucA CLASSIFICATION #superfamily L-ribulose-phosphate 4-epimerase KEYWORDS aldehyde-lyase; carbon-carbon lyase SUMMARY #length 218 #molecular-weight 23066 #checksum 1153 SEQUENCE /// ENTRY H70469 #type complete TITLE L-fuculose-phosphate aldolase homolog - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 21-Jul-2000 ACCESSIONS H70469 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession H70469 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-208 ##label AQF !'##cross-references GB:AE000766; GB:AE000657; NID:g2984216; !1PIDN:AAC07751.1; PID:g2984222 !'##experimental_source strain VF5 GENETICS !$#gene fucA2 CLASSIFICATION #superfamily L-ribulose-phosphate 4-epimerase SUMMARY #length 208 #molecular-weight 23550 #checksum 9427 SEQUENCE /// ENTRY H69309 #type complete TITLE L-fuculose-phosphate aldolase (EC 4.1.2.17) - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 21-Jul-2000 ACCESSIONS H69309 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession H69309 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-186 ##label KLE !'##cross-references GB:AE001071; GB:AE000782; NID:g2689394; !1PIDN:AAB90758.1; PID:g2650147; TIGR:AF0480 CLASSIFICATION #superfamily L-ribulose-phosphate 4-epimerase KEYWORDS aldehyde-lyase; carbon-carbon lyase SUMMARY #length 186 #molecular-weight 20743 #checksum 3809 SEQUENCE /// ENTRY E70443 #type complete TITLE L-fuculose-phosphate aldolase homolog - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 21-Jul-2000 ACCESSIONS E70443 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession E70443 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-187 ##label AQF !'##cross-references GB:AE000749; GB:AE000657; NID:g2983975; !1PIDN:AAC07526.1; PID:g2983980 !'##experimental_source strain VF5 GENETICS !$#gene fucA1 CLASSIFICATION #superfamily L-ribulose-phosphate 4-epimerase SUMMARY #length 187 #molecular-weight 20729 #checksum 5879 SEQUENCE /// ENTRY B72299 #type complete TITLE L-fuculose-phosphate aldolase homolog - Thermotoga maritima (strain MSB8) ORGANISM #formal_name Thermotoga maritima DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 21-Jul-2000 ACCESSIONS B72299 REFERENCE A72200 !$#authors Nelson, K.E.; Clayton, R.A.; Gill, S.R.; Gwinn, M.L.; !1Dodson, R.J.; Haft, D.H.; Hickey, E.K.; Peterson, J.D.; !1Nelson, W.C.; Ketchum, K.A.; McDonald, L.; Utterback, T.R.; !1Malek, J.A.; Linher, K.D.; Garrett, M.M.; Stewart, A.M.; !1Cotton, M.D.; Pratt, M.S.; Phillips, C.A.; Richardson, D.; !1Heidelberg, J.; Sutton, G.G.; Fleischmann, R.D.; White, O.; !1Salzberg, S.L.; Smith, H.O.; Venter, J.C.; Fraser, C.M. !$#journal Nature (1999) 399:323-329 !$#title Evidence for lateral gene transfer between Archaea and !1Bacteria from genome sequence of Thermotoga maritima. !$#cross-references MUID:99287316; PMID:10360571 !$#accession B72299 !'##status preliminary !'##molecule_type DNA !'##residues 1-236 ##label ARN !'##cross-references GB:AE001767; GB:AE000512; NID:g4981611; !1PIDN:AAD36149.1; PID:g4981616; TIGR:TM1072 !'##experimental_source strain MSB8 GENETICS !$#gene TM1072 CLASSIFICATION #superfamily L-ribulose-phosphate 4-epimerase SUMMARY #length 236 #molecular-weight 26753 #checksum 3771 SEQUENCE /// ENTRY E37854 #type complete TITLE dihydroneopterin aldolase (EC 4.1.2.25) folA - Bacillus subtilis ALTERNATE_NAMES folate biosynthesis protein 1 (sul 3' region) ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS E37854; S66108; C69626 REFERENCE A37854 !$#authors Slock, J.; Stahly, D.P.; Han, C.Y.; Six, E.W.; Crawford, !1I.P. !$#journal J. Bacteriol. (1990) 172:7211-7226 !$#title An apparent Bacillus subtilis folic acid biosynthetic operon !1containing pab, an amphibolic trpG gene, a third gene !1required for synthesis of para-aminobenzoic acid, and the !1dihydropteroate synthase gene. !$#cross-references MUID:91072277; PMID:2123867 !$#accession E37854 !'##molecule_type DNA !'##residues 1-120 ##label SLO !'##cross-references GB:M34053; NID:g143406; PIDN:AAA22698.1; !1PID:g143411 REFERENCE S65967 !$#authors Ogasawara, N.; Nakai, S.; Yoshikawa, H. !$#journal DNA Res. (1994) 1:1-14 !$#title Systematic sequencing of the 180 kilobase region of the !1Bacillus subtilis chromosome containing the replication !1origin. !$#cross-references MUID:96051385; PMID:7584024 !$#accession S66108 !'##status preliminary !'##molecule_type DNA !'##residues 1-120 ##label OGA !'##cross-references EMBL:D26185; NID:g467326; PIDN:BAA05313.1; !1PID:g467467 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69626 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-120 ##label KUN !'##cross-references GB:Z99104; GB:AL009126; NID:g2632267; !1PIDN:CAB11854.1; PID:g2632345 !'##experimental_source strain 168 GENETICS !$#gene folA; folB CLASSIFICATION #superfamily dihydroneopterin aldolase folA; !1dihydroneopterin aldolase homology KEYWORDS aldehyde-lyase; carbon-carbon lyase; folate biosynthesis FEATURE !$2-119 #domain dihydroneopterin aldolase homology #label DHA SUMMARY #length 120 #molecular-weight 13516 #checksum 3667 SEQUENCE /// ENTRY S76177 #type complete TITLE dihydroneopterin aldolase (EC 4.1.2.25) - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S76177 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76177 !'##status preliminary !'##molecule_type DNA !'##residues 1-150 ##label KAN !'##cross-references EMBL:D90914; GB:AB001339; NID:g1653477; !1PIDN:BAA18436.1; PID:g1653523 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily dihydroneopterin aldolase folA; !1dihydroneopterin aldolase homology KEYWORDS aldehyde-lyase; carbon-carbon lyase; folate biosynthesis FEATURE !$34-150 #domain dihydroneopterin aldolase homology #label DHA SUMMARY #length 150 #molecular-weight 16546 #checksum 7915 SEQUENCE /// ENTRY H65093 #type complete TITLE probable dihydroneopterin aldolase (EC 4.1.2.25) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS H65093 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65093 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-123 ##label BLAT !'##cross-references GB:AE000387; GB:U00096; NID:g1789431; !1PIDN:AAC76094.1; PID:g1789438; UWGP:b3058 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ygiG CLASSIFICATION #superfamily dihydroneopterin aldolase folA; !1dihydroneopterin aldolase homology KEYWORDS aldehyde-lyase; carbon-carbon lyase; folate biosynthesis FEATURE !$3-117 #domain dihydroneopterin aldolase homology #label DHA SUMMARY #length 123 #molecular-weight 13751 #checksum 1762 SEQUENCE /// ENTRY XUSMEG #type complete TITLE dTDP-4-dehydrorhamnose 3,5-epimerase (EC 5.1.3.13) - Streptomyces griseus ALTERNATE_NAMES dTDP-4-keto-6-deoxyglucose 3,5-epimerase ORGANISM #formal_name Streptomyces griseus DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 18-Jun-1999 ACCESSIONS S18619; S19782 REFERENCE S18617 !$#authors Pissowotzki, K.; Mansouri, K.; Piepersberg, W. !$#journal Mol. Gen. Genet. (1991) 231:113-123 !$#title Genetics of streptomycin production in Streptomyces griseus: !1molecular structure and putative function of genes !1strELMB2N. !$#cross-references MUID:92092953; PMID:1661369 !$#accession S18619 !'##molecule_type DNA !'##residues 1-200 ##label PIS !'##cross-references EMBL:X62567; NID:g49009; PIDN:CAA44442.1; !1PID:g581676 !'##note the authors translated the initiation codon GTG for residue 1 !1as Val GENETICS !$#gene strM !$#start_codon GTG CLASSIFICATION #superfamily dTDP-4-dehydrorhamnose 3,5-epimerase KEYWORDS isomerase; streptomycin biosynthesis SUMMARY #length 200 #molecular-weight 21956 #checksum 3181 SEQUENCE /// ENTRY S76605 #type complete TITLE phosphoheptose isomerase homolog - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S76605 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76605 !'##status preliminary !'##molecule_type DNA !'##residues 1-194 ##label KAN !'##cross-references EMBL:D64004; GB:AB001339; NID:g1001701; !1PIDN:BAA10549.1; PID:g1001712 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily phosphoheptose isomerase SUMMARY #length 194 #molecular-weight 21137 #checksum 3164 SEQUENCE /// ENTRY F64466 #type complete TITLE phosphoheptose isomerase homolog - Methanococcus jannaschii ALTERNATE_NAMES hypothetical protein homolog MJ1335 ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F64466 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession F64466 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-143 ##label BUL !'##cross-references GB:U67573; GB:L77117; NID:g2826395; !1PIDN:AAB99342.1; PID:g1591976; TIGR:MJ1335 GENETICS !$#map_position FOR1284342-1284773 !$#start_codon TTG CLASSIFICATION #superfamily phosphoheptose isomerase SUMMARY #length 143 #molecular-weight 15599 #checksum 1127 SEQUENCE /// ENTRY A64627 #type complete TITLE phosphoheptose isomerase (EC 5.-.-.-) - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A64627 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession A64627 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-192 ##label TOM !'##cross-references GB:AE000596; GB:AE000511; NID:g2313982; !1PIDN:AAD07903.1; PID:g2313989; TIGR:HP0857 CLASSIFICATION #superfamily phosphoheptose isomerase KEYWORDS isomerase SUMMARY #length 192 #molecular-weight 21102 #checksum 9142 SEQUENCE /// ENTRY G64168 #type complete TITLE phosphoheptose isomerase (EC 5.-.-.-) - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS G64168 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession G64168 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-194 ##label TIGR !'##cross-references GB:U32797; GB:L42023; NID:g1574095; !1PIDN:AAC22832.1; PID:g1574106; TIGR:HI1181 CLASSIFICATION #superfamily phosphoheptose isomerase KEYWORDS isomerase SUMMARY #length 194 #molecular-weight 21378 #checksum 4350 SEQUENCE /// ENTRY G64746 #type complete TITLE phosphoheptose isomerase (EC 5.-.-.-) gmhA - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS G64746 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64746 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-192 ##label BLAT !'##cross-references GB:AE000131; GB:U00096; NID:g1786415; !1PIDN:AAC73326.1; PID:g1786416; UWGP:b0222 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene gmhA FUNCTION !$#description synthesis of glyceromannoheptose 7-phosphate !$#pathway inner core lipopolysaccharide biosynthesis CLASSIFICATION #superfamily phosphoheptose isomerase KEYWORDS isomerase SUMMARY #length 192 #molecular-weight 20815 #checksum 6719 SEQUENCE /// ENTRY A65105 #type complete TITLE phosphoheptose isomerase homolog - Escherichia coli (strain K-12) ALTERNATE_NAMES hypothetical 21.1 kD protein in agai-mtr intergenic region ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS A65105 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65105 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-196 ##label BLAT !'##cross-references GB:AE000396; GB:U00096; NID:g1789536; !1PIDN:AAC76183.1; PID:g1789539; UWGP:b3149 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yraO CLASSIFICATION #superfamily phosphoheptose isomerase SUMMARY #length 196 #molecular-weight 21106 #checksum 6711 SEQUENCE /// ENTRY CSHUA #type complete TITLE peptidylprolyl isomerase (EC 5.2.1.8) A - human ALTERNATE_NAMES cyclophilin A; cyclosporin A-binding protein A ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jul-1999 ACCESSIONS A94496; A29266; S11321 REFERENCE A94496 !$#authors Hofer, E. !$#submission submitted to the EMBL Data Library, March 1987 !$#accession A94496 !'##molecule_type mRNA !'##residues 1-165 ##label HOF !'##cross-references GB:Y00052; NID:g30308; PIDN:CAA68264.1; PID:g30309 REFERENCE A91085 !$#authors Haendler, B.; Hofer-Warbinek, R.; Hofer, E. !$#journal EMBO J. (1987) 6:947-950 !$#title Complementary DNA for human T-cell cyclophilin. !$#cross-references MUID:87246530; PMID:3297675 !$#accession A29266 !'##molecule_type mRNA !'##residues 1-165 ##label HAE1 !'##cross-references GB:Y00052; NID:g30308; PIDN:CAA68264.1; PID:g30309 !'##experimental_source leukemic T-cell line Jurkat REFERENCE S11321 !$#authors Haendler, B.; Hofer, E. !$#journal Eur. J. Biochem. (1990) 190:477-482 !$#title Characterization of the human cyclophilin gene and of !1related processed pseudogenes. !$#cross-references MUID:90322991; PMID:2197089 !$#accession S11321 !'##molecule_type DNA !'##residues 1-165 ##label HAE2 !'##cross-references GB:X52851; NID:g30167; PIDN:CAA37039.1; PID:g30168 GENETICS !$#gene GDB:PPIA !'##cross-references GDB:127769; OMIM:123840 !$#map_position 20q13.1-20q13.1 FUNCTION !$#description catalyzes the cis-trans isomerization of peptidylproline !1peptide bonds CLASSIFICATION #superfamily peptidylprolyl isomerase; cyclophilin homology KEYWORDS cis-trans-isomerase; cyclosporin A binding; T-cell FEATURE !$3-164 #domain cyclophilin homology #label CYP SUMMARY #length 165 #molecular-weight 18012 #checksum 6484 SEQUENCE /// ENTRY CSBOAB #type complete TITLE peptidylprolyl isomerase (EC 5.2.1.8) A - bovine ALTERNATE_NAMES cyclophilin; cyclosporin A-binding protein A ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 16-Jul-1999 ACCESSIONS A01852 REFERENCE A01852 !$#authors Harding, M.W.; Handschumacher, R.E.; Speicher, D.W. !$#journal J. Biol. Chem. (1986) 261:8547-8555 !$#title Isolation and amino acid sequence of cyclophilin. !$#cross-references MUID:86250760; PMID:3522572 !$#accession A01852 !'##molecule_type protein !'##residues 1-163 ##label HAR COMMENT This protein belongs to a class of highly conserved !1proteins, abundant in thymus cytoplasm, that appear to be !1involved with the regulation of T-lymphocyte activation and !1proliferation. FUNCTION !$#description catalyzes the cis-trans isomerization of peptidylproline !1peptide bonds CLASSIFICATION #superfamily peptidylprolyl isomerase; cyclophilin homology KEYWORDS cis-trans-isomerase; cyclosporin A binding; T-cell FEATURE !$2-163 #domain cyclophilin homology #label CYP SUMMARY #length 163 #molecular-weight 17738 #checksum 8871 SEQUENCE /// ENTRY CSPGA #type complete TITLE peptidylprolyl isomerase (EC 5.2.1.8) A - pig ALTERNATE_NAMES cyclophilin A; cyclosporin A-binding protein A ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jul-1999 ACCESSIONS S02172 REFERENCE S02172 !$#authors Takahashi, N.; Hayano, T.; Suzuki, M. !$#journal Nature (1989) 337:473-475 !$#title Peptidyl-prolyl cis-trans isomerase is the cyclosporin !1A-binding protein cyclophilin. !$#cross-references MUID:89127497; PMID:2644542 !$#accession S02172 !'##molecule_type protein !'##residues 1-163 ##label TAK COMMENT This protein belongs to a class of highly conserved !1proteins, abundant in thymus cytoplasm, that appear to be !1involved with the regulation of T-lymphocyte activation and !1proliferation. FUNCTION !$#description catalyzes the cis-trans isomerization of peptidylproline !1peptide bonds CLASSIFICATION #superfamily peptidylprolyl isomerase; cyclophilin homology KEYWORDS cis-trans-isomerase; cyclosporin A binding; T-cell FEATURE !$2-163 #domain cyclophilin homology #label CYP SUMMARY #length 163 #molecular-weight 17738 #checksum 8871 SEQUENCE /// ENTRY CSHYAC #type complete TITLE peptidylprolyl isomerase (EC 5.2.1.8) A - Chinese hamster ALTERNATE_NAMES cyclophilin A; cyclosporin A-binding protein A ORGANISM #formal_name Cricetulus griseus #common_name Chinese hamster DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jul-1999 ACCESSIONS S07597 REFERENCE S07597 !$#authors Bergsma, D.J.; Sylvester, D. !$#journal Nucleic Acids Res. (1990) 18:200 !$#title A Chinese hamster ovary cyclophilin cDNA sequence. !$#cross-references MUID:90174932; PMID:2408007 !$#accession S07597 !'##molecule_type mRNA !'##residues 1-164 ##label BER !'##cross-references EMBL:X17105; NID:g49495; PIDN:CAA34961.1; !1PID:g49496 FUNCTION !$#description catalyzes the cis-trans isomerization of peptidylproline !1peptide bonds CLASSIFICATION #superfamily peptidylprolyl isomerase; cyclophilin homology KEYWORDS cis-trans-isomerase; cyclosporin A binding; T-cell FEATURE !$3-164 #domain cyclophilin homology #label CYP SUMMARY #length 164 #molecular-weight 17899 #checksum 4686 SEQUENCE /// ENTRY CSMSA #type complete TITLE peptidylprolyl isomerase (EC 5.2.1.8) A - mouse ALTERNATE_NAMES cyclophilin A; cyclosporin A-binding protein A ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jul-1999 ACCESSIONS S10327; S66416; S40742 REFERENCE S10327 !$#authors Hasel, K.W.; Sutcliffe, J.G. !$#journal Nucleic Acids Res. (1990) 18:4019 !$#title Nucleotide sequence of a cDNA coding for mouse cyclophilin. !$#cross-references MUID:90326555; PMID:2197604 !$#accession S10327 !'##molecule_type mRNA !'##residues 1-164 ##label HAS !'##cross-references GB:X52803; NID:g50620; PIDN:CAA36989.1; PID:g50621 REFERENCE S66416 !$#authors Krummrei, U.; Bang, R.; Schmidtchen, R.; Brune, K.; Bang, H. !$#journal FEBS Lett. (1995) 371:47-51 !$#title Cyclophilin-A is a zinc-dependent DNA binding protein in !1macrophages. !$#cross-references MUID:95394146; PMID:7664883 !$#accession S66416 !'##molecule_type protein !'##residues 2-21 ##label KRU !'##experimental_source nuclear cyclophilin of H4-7 cells GENETICS !$#gene CypA FUNCTION !$#description catalyzes the cis-trans isomerization of peptidylproline !1peptide bonds CLASSIFICATION #superfamily peptidylprolyl isomerase; cyclophilin homology KEYWORDS cis-trans-isomerase; cyclosporin A binding; DNA binding; !1macrophage; T-cell; zinc FEATURE !$3-164 #domain cyclophilin homology #label CYP SUMMARY #length 164 #molecular-weight 17971 #checksum 4655 SEQUENCE /// ENTRY CSRTA #type complete TITLE peptidylprolyl isomerase (EC 5.2.1.8) A - rat ALTERNATE_NAMES 13.3K protein [misidentification]; cyclophilin A; cyclosporin A-binding protein A; protein P31 [misidentification] ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 04-Feb-2000 ACCESSIONS A29819; A60036; A15632; A58859 REFERENCE A29819 !$#authors Danielson, P.E.; Forss-Petter, S.; Brow, M.A.; Calavetta, !1L.; Douglass, J.; Milner, R.J.; Sutcliffe, J.G. !$#journal DNA (1988) 7:261-267 !$#title p1B15: A cDNA clone of the rat mRNA encoding cyclophilin. !$#cross-references MUID:88283345; PMID:3293952 !$#accession A29819 !'##molecule_type mRNA !'##residues 1-164 ##label DAN !'##cross-references GB:M19533; NID:g203701; PIDN:AAA41009.1; !1PID:g203702 REFERENCE A60036 !$#authors Lad, R.P.; Smith, M.A.; Hilt, D.C. !$#journal Brain Res. Mol. Brain Res. (1991) 9:239-244 !$#title Molecular cloning and regional distribution of rat brain !1cyclophilin. !$#cross-references MUID:91232390; PMID:1851525 !$#accession A60036 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type mRNA !'##residues 1-164 ##label LAD !'##experimental_source brain REFERENCE A15632 !$#authors Theodor, L.; Peleg, D.; Meyuhas, O. !$#journal Biochim. Biophys. Acta (1985) 826:137-146 !$#title P31, a mammalian housekeeping protein encoded by a multigene !1family containing a high proportion of pseudogenes. !$#cross-references MUID:86026347; PMID:2996604 !$#accession A15632 !'##molecule_type mRNA !'##residues 100-148,'MARPARRSPSPTVGNSNFFDLRAFYPSNH', !1'SFCSSGEHPHPICSQYPVISALTEVLWVP','YFPHSPSSLAGLQS' ##label THE !'##cross-references EMBL:M25637 !'##note this sequence was corrected by A58859 REFERENCE A58859 !$#authors Meyuhas, O. !$#submission submitted to GenBank, December 1991 !$#contents erratum !$#accession A58859 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-164 ##label MEY !'##cross-references EMBL:M25637; NID:g951424; PIDN:AAB59719.1; !1PID:g951425 !'##note the submission to GenBank in entry RATP31 is acknowledged as an !1unpublished erratum COMMENT This protein belongs to a class of highly conserved !1proteins, abundant in thymus cytoplasm, that appear to be !1involved with the regulation of T-lymphocyte activation and !1proliferation. FUNCTION !$#description catalyzes the cis-trans isomerization of peptidylproline !1peptide bonds CLASSIFICATION #superfamily peptidylprolyl isomerase; cyclophilin homology KEYWORDS cis-trans-isomerase; cyclosporin A binding; T-cell FEATURE !$3-164 #domain cyclophilin homology #label CYP SUMMARY #length 164 #molecular-weight 17874 #checksum 4343 SEQUENCE /// ENTRY CSHUB #type complete TITLE peptidylprolyl isomerase (EC 5.2.1.8) B precursor [validated] - human ALTERNATE_NAMES cyclophilin B; cyclosporin A-binding protein B; S-cyclophilin ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 08-Dec-2000 ACCESSIONS A39118; A39722; A40515; S65742 REFERENCE A39118 !$#authors Price, E.R.; Zydowsky, L.D.; Jin, M.; Baker, C.H.; McKeon, !1F.D.; Walsh, C.T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:1903-1907 !$#title Human cyclophilin B: a second cyclophilin gene encodes a !1peptidyl-prolyl isomerase with a signal sequence. !$#cross-references MUID:91156714; PMID:2000394 !$#accession A39118 !'##molecule_type mRNA !'##residues 1-208 ##label PRI !'##cross-references GB:M60857; NID:g181334; PIDN:AAA52150.1; !1PID:g181335 REFERENCE A39722 !$#authors Hasel, K.W.; Glass, J.R.; Godbout, M.; Sutcliffe, J.G. !$#journal Mol. Cell. Biol. (1991) 11:3484-3491 !$#title An endoplasmic reticulum-specific cyclophilin. !$#cross-references MUID:91260697; PMID:1710767 !$#accession A39722 !'##molecule_type mRNA !'##residues 1-208 ##label HAS !'##cross-references GB:M60457; NID:g181249; PIDN:AAA35733.1; !1PID:g181250 REFERENCE A40515 !$#authors Spik, G.; Haendler, B.; Delmas, O.; Mariller, C.; Chamoux, !1M.; Maes, P.; Tartar, A.; Montreuil, J.; Stedman, K.; !1Kocher, H.P.; Keller, R.; Hiestand, P.C.; Movva, N.R. !$#journal J. Biol. Chem. (1991) 266:10735-10738 !$#title A novel secreted cyclophilin-like protein (SCYLP). !$#cross-references MUID:91250363; PMID:2040592 !$#accession A40515 !'##molecule_type mRNA !'##residues 'MLRLSERN',1-208 ##label SPI !'##cross-references GB:M63573; NID:g337998; PIDN:AAA36601.1; !1PID:g337999 !'##note the authors' translation begins at an ATG codon in poor context !1for initiation !'##note parts of this sequence, including the amino end of the mature !1form, were confirmed by peptide sequencing REFERENCE S65742 !$#authors Mariller, C.; Allain, F.; Kouach, M.; Spik, G. !$#journal Biochim. Biophys. Acta (1996) 1293:31-38 !$#title Evidence that human milk isolated cyclophilin B corresponds !1to a truncated form. !$#cross-references MUID:96186273; PMID:8652625 !$#accession S65742 !'##molecule_type protein !'##residues 26-30;203 ##label MAR !'##experimental_source milk COMMENT This protein is distinguished from peptidylprolyl isomerase !1A by the presence of an endoplasmic reticulum-directed !1signal sequence. COMMENT This protein binds to and is inhibited by the !1immunosuppressive drug cyclosporin A. GENETICS !$#gene GDB:PPIB !'##cross-references GDB:127610; OMIM:123841 !$#map_position 15q21-15q22 FUNCTION !$#description catalyzes the cis-trans isomerization of peptidylproline !1peptide bonds CLASSIFICATION #superfamily peptidylprolyl isomerase; cyclophilin homology KEYWORDS cis-trans-isomerase; cyclosporin A binding; glycoprotein; !1T-cell FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-203 #product peptidylprolyl isomerase B #status !8experimental #label MAT\ !$35-197 #domain cyclophilin homology #label CYP\ !$140 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 208 #molecular-weight 22742 #checksum 6962 SEQUENCE /// ENTRY CSTO #type complete TITLE peptidylprolyl isomerase (EC 5.2.1.8) - tomato ALTERNATE_NAMES cyclophilin; cyclosporin A-binding protein ORGANISM #formal_name Lycopersicon esculentum #common_name tomato DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jul-1999 ACCESSIONS A39252 REFERENCE A39252 !$#authors Gasser, C.S.; Gunning, D.A.; Budelier, K.A.; Brown, S.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:9519-9523 !$#title Structure and expression of cytosolic cyclophilin/ !1peptidyl-prolyl cis-trans isomerase of higher plants and !1production of active tomato cyclophilin in Escherichia coli. !$#cross-references MUID:91088549; PMID:1702215 !$#accession A39252 !'##molecule_type DNA !'##residues 1-171 ##label GAS !'##cross-references GB:M55019 GENETICS !$#gene cyp; rot1 FUNCTION !$#description catalyzes the cis-trans isomerization of peptidylproline !1peptide bonds CLASSIFICATION #superfamily peptidylprolyl isomerase; cyclophilin homology KEYWORDS cis-trans-isomerase; cyclosporin A binding FEATURE !$3-171 #domain cyclophilin homology #label CYP SUMMARY #length 171 #molecular-weight 17926 #checksum 3370 SEQUENCE /// ENTRY CSRP #type complete TITLE peptidylprolyl isomerase (EC 5.2.1.8) - rape ALTERNATE_NAMES cyclophilin; cyclosporin A-binding protein ORGANISM #formal_name Brassica napus #common_name rape DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jul-1999 ACCESSIONS B39252 REFERENCE A39252 !$#authors Gasser, C.S.; Gunning, D.A.; Budelier, K.A.; Brown, S.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:9519-9523 !$#title Structure and expression of cytosolic cyclophilin/ !1peptidyl-prolyl cis-trans isomerase of higher plants and !1production of active tomato cyclophilin in Escherichia coli. !$#cross-references MUID:91088549; PMID:1702215 !$#accession B39252 !'##molecule_type DNA !'##residues 1-171 ##label GAS !'##cross-references GB:M55018 GENETICS !$#gene cyp; rot1 FUNCTION !$#description catalyzes the cis-trans isomerization of peptidylproline !1peptide bonds CLASSIFICATION #superfamily peptidylprolyl isomerase; cyclophilin homology KEYWORDS cis-trans-isomerase; cyclosporin A binding FEATURE !$3-171 #domain cyclophilin homology #label CYP SUMMARY #length 171 #molecular-weight 18500 #checksum 6450 SEQUENCE /// ENTRY CSZM #type complete TITLE peptidylprolyl isomerase (EC 5.2.1.8) - maize ALTERNATE_NAMES cyclophilin; cyclosporin A-binding protein; peptidyl-prolyl cis-trans isomerase ORGANISM #formal_name Zea mays #common_name maize DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jul-1999 ACCESSIONS C39252; S54760 REFERENCE A39252 !$#authors Gasser, C.S.; Gunning, D.A.; Budelier, K.A.; Brown, S.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:9519-9523 !$#title Structure and expression of cytosolic cyclophilin/ !1peptidyl-prolyl cis-trans isomerase of higher plants and !1production of active tomato cyclophilin in Escherichia coli. !$#cross-references MUID:91088549; PMID:1702215 !$#accession C39252 !'##molecule_type DNA !'##residues 1-172 ##label GAS !'##cross-references GB:M55021; NID:g168460; PIDN:AAA63403.1; !1PID:g168461 REFERENCE S54760 !$#authors Marivet, J.; Frendo, P.; Burkard, G. !$#journal Mol. Gen. Genet. (1995) 247:222-228 !$#title DNA sequence analysis of a cyclophilin gene from maize: !1developmental expression and regulation by salicylic acid. !$#cross-references MUID:95272532; PMID:7753032 !$#accession S54760 !'##status preliminary !'##molecule_type DNA !'##residues 1-172 ##label MAR !'##cross-references EMBL:X68678; NID:g829147; PIDN:CAA48638.1; !1PID:g829148 FUNCTION !$#description catalyzes the cis-trans isomerization of peptidylproline !1peptide bonds CLASSIFICATION #superfamily peptidylprolyl isomerase; cyclophilin homology KEYWORDS cis-trans-isomerase; cyclosporin A binding FEATURE !$3-171 #domain cyclophilin homology #label CYP SUMMARY #length 172 #molecular-weight 18349 #checksum 7015 SEQUENCE /// ENTRY CSBY #type complete TITLE peptidylprolyl isomerase (EC 5.2.1.8), cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES cyclophilin A; cyclosporin A-binding protein; peptidylprolyl isomerase II; protein YD8358.10c; protein YDR155c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 05-Nov-1999 ACCESSIONS S25443; JQ0125; S57980; S29645 REFERENCE S25443 !$#authors Dietmeier, K.; Tropschug, M. !$#journal Nucleic Acids Res. (1990) 18:373 !$#title Nucleotide sequence of a full-length cDNA coding for !1cyclophilin (peptidyl-prolyl cis-trans isomerase) of !1Saccharomyces cerevisiae. !$#cross-references MUID:90221831; PMID:2183184 !$#accession S25443 !'##molecule_type mRNA !'##residues 1-162 ##label DIE !'##cross-references EMBL:X17505; NID:g3617; PIDN:CAA35545.1; PID:g3618 REFERENCE JQ0125 !$#authors Haendler, B.; Keller, R.; Hiestand, P.C.; Kocher, H.P.; !1Wegmann, G.; Movva, N.R. !$#journal Gene (1989) 83:39-46 !$#title Yeast cyclophilin: isolation and characterization of the !1protein, cDNA and gene. !$#cross-references MUID:90076969; PMID:2687115 !$#accession JQ0125 !'##molecule_type DNA !'##residues 1-162 ##label HAE !'##cross-references GB:M30513; NID:g171313; PIDN:AAA34528.1; !1PID:g171314 !'##note part of this sequence was confirmed by protein sequencing REFERENCE S57971 !$#authors Murphy, L.; Richards, C.; Harris, D. !$#submission submitted to the EMBL Data Library, July 1995 !$#accession S57980 !'##molecule_type DNA !'##residues 1-162 ##label MUR !'##cross-references EMBL:Z50046; NID:g899393; PIDN:CAA90376.1; !1PID:g899403; GSPDB:GN00004; MIPS:YDR155c !'##experimental_source strain AB972 REFERENCE S29645 !$#authors Hasumi, H.; Nishikawa, T. !$#journal Biochim. Biophys. Acta (1993) 1161:161-167 !$#title Purification and properties of multiple molecular forms of !1yeast peptidyl prolyl cis-trans isomerase. !$#cross-references MUID:93160233; PMID:8431466 !$#accession S29645 !'##molecule_type protein !'##residues 'X',3-8,'X',10;30-37;75-78;81-85;159-162 ##label HAS GENETICS !$#gene SGD:CPH1; MIPS:YDR155c !'##cross-references SGD:S0002562; MIPS:YDR155c !$#map_position 4R FUNCTION !$#description catalyzes the cis-trans isomerization of peptidylproline !1peptide bonds !$#note activity is one-tenth that of the mammalian protein; high !1binding affinity for cyclosporin A CLASSIFICATION #superfamily peptidylprolyl isomerase; cyclophilin homology KEYWORDS acetylated amino end; blocked amino end; !1cis-trans-isomerase; cyclosporin A binding FEATURE !$1-162 #domain cyclophilin homology #label CYP\ !$2-162 #product peptidylprolyl isomerase, cytosolic #status !8experimental #label MAT\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental SUMMARY #length 162 #molecular-weight 17391 #checksum 9179 SEQUENCE /// ENTRY CSZPA #type complete TITLE peptidylprolyl isomerase (EC 5.2.1.8) A - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES cyclophilin A; cyclosporin A-binding protein A ORGANISM #formal_name Schizosaccharomyces pombe DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 10-Dec-1999 ACCESSIONS S11212; T40046 REFERENCE S11212 !$#authors de Martin, R.; Philipson, L. !$#journal Nucleic Acids Res. (1990) 18:4917 !$#title The gene for cyclophilin (peptidyl-prolyl cis-trans !1isomerase) from Schizosaccharomyces pombe. !$#cross-references MUID:90370480; PMID:2204030 !$#accession S11212 !'##molecule_type DNA !'##residues 1-162 ##label DEM !'##cross-references GB:X53223; NID:g5015; PIDN:CAA37322.1; PID:g5016 REFERENCE Z21902 !$#authors McDougall, R.C.; Rajandream, M.A.; Barrell, B.G.; Stevens, !1K.; Badcock, K.; Churcher, C.M. !$#submission submitted to the EMBL Data Library, October 1999 !$#accession T40046 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-162 ##label MCD !'##cross-references EMBL:AL121795; PIDN:CAB57932.1; GSPDB:GN00067; !1SPDB:SPBC28F2.03 !'##experimental_source strain 972h-; cosmid c28F2 GENETICS !$#gene SPBC28F2.03 !$#map_position 2 FUNCTION !$#description catalyzes the cis-trans isomerization of peptidylproline !1peptide bonds CLASSIFICATION #superfamily peptidylprolyl isomerase; cyclophilin homology KEYWORDS cis-trans-isomerase; cyclosporin A binding FEATURE !$1-162 #domain cyclophilin homology #label CYP SUMMARY #length 162 #molecular-weight 17402 #checksum 650 SEQUENCE /// ENTRY CSNCM #type complete TITLE peptidylprolyl isomerase (EC 5.2.1.8) precursor, mitochondrial - Neurospora crassa ALTERNATE_NAMES cyclophilin B; cyclosporin A-binding protein B CONTAINS peptidylprolyl isomerase (EC 5.2.1.8), cytosolic (cyclophilin A, cyclosporin A-binding protein A) ORGANISM #formal_name Neurospora crassa DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jul-1999 ACCESSIONS B30809; A30809; S07585 REFERENCE A92671 !$#authors Tropschug, M.; Nicholson, D.W.; Hartl, F.U.; Koehler, H.; !1Pfanner, N.; Wachter, E.; Neupert, W. !$#journal J. Biol. Chem. (1988) 263:14433-14440 !$#title Cyclosporin A-binding protein (cyclophilin) of Neurospora !1crassa. One gene codes for both the cytosolic and !1mitochondrial forms. !$#cross-references MUID:89008293; PMID:2971658 !$#accession B30809 !'##molecule_type mRNA !'##residues 1-223 ##label TRO !'##cross-references GB:J03963; NID:g168805; PIDN:AAA33584.1; !1PID:g168806 !$#accession A30809 !'##molecule_type mRNA !'##residues 44-223 ##label TR2 !'##cross-references GB:J03963 REFERENCE S07585 !$#authors Tropschug, M. !$#journal Nucleic Acids Res. (1990) 18:190 !$#title Nucleotide sequence of the gene coding for cyclophilin/ !1peptidyl-prolyl cis-trans isomerase of Neurospora crassa. !$#cross-references MUID:90174923; PMID:2137907 !$#accession S07585 !'##molecule_type DNA !'##residues 1-223 ##label TRO2 !'##cross-references EMBL:X17692; NID:g2998; PIDN:CAA35681.1; !1PID:g295926 COMMENT The mature cytosolic and mitochondrial forms are identical !1in sequence, although their precursors differ. The cytosolic !1form loses its initiator Met during maturation. The longer !1precursor for the mitochondrial form begins at an upstream !1initiator available from alterative splicing, but the !1additional sequence is lost in mitochondrial import and !1processing to yield the same amino-terminal residue. FUNCTION !$#description catalyzes the cis-trans isomerization of peptidylproline !1peptide bonds CLASSIFICATION #superfamily peptidylprolyl isomerase; cyclophilin homology KEYWORDS alternative initiators; alternative splicing; !1cis-trans-isomerase; cyclosporin A binding; mitochondrion FEATURE !$1-180 #product peptidylprolyl isomerase mitochondrial form !8precursor #status predicted #label MPRE\ !$1-36 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$37-44 #domain propeptide #status predicted #label PRO\ !$44-223 #domain cyclophilin homology #label CYP\ !$44-180 #product peptidylprolyl isomerase cytosolic form !8precursor #status predicted #label CPRE\ !$45-180 #product peptidylprolyl isomerase, cytosolic #status !8experimental #label CMAT\ !$45-180 #product peptidylprolyl isomerase, mitochondrial !8#status experimental #label MMAT SUMMARY #length 223 #molecular-weight 24064 #checksum 3180 SEQUENCE /// ENTRY CSCK #type complete TITLE peptidylprolyl isomerase (EC 5.2.1.8) - yeast (Candida albicans) ALTERNATE_NAMES cyclophilin; cyclosporin A-binding protein ORGANISM #formal_name Candida albicans DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jul-1999 ACCESSIONS JQ0888 REFERENCE JQ0888 !$#authors Koser, P.L.; Livi, G.P.; Levy, M.A.; Rosenberg, M.; Bergsma, !1D.J. !$#journal Gene (1990) 96:189-195 !$#title A Candida albicans homolog of a human cyclophilin gene !1encodes a peptidyl-prolyl cis-trans isomerase. !$#cross-references MUID:91099675; PMID:2269432 !$#accession JQ0888 !'##molecule_type DNA !'##residues 1-162 ##label KOS !'##cross-references GB:M60628; NID:g170850; PIDN:AAA34336.1; !1PID:g170851 FUNCTION !$#description catalyzes the cis-trans isomerization of peptidylproline !1peptide bonds CLASSIFICATION #superfamily peptidylprolyl isomerase; cyclophilin homology KEYWORDS acetylated amino end; cis-trans-isomerase; cyclosporin A !1binding FEATURE !$1-162 #domain cyclophilin homology #label CYP\ !$2-162 #product peptidylprolyl isomerase, cytosolic #status !8predicted #label MAT\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status predicted SUMMARY #length 162 #molecular-weight 17575 #checksum 9772 SEQUENCE /// ENTRY CYFFBE #type complete TITLE peptidylprolyl isomerase (EC 5.2.1.8) B, eye-specific, precursor - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES cyclophilin B, eye-specific; cyclosporin A-binding protein B ORGANISM #formal_name Drosophila melanogaster DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jun-2000 ACCESSIONS A33906; S03346; A31275; A38388 REFERENCE A33906 !$#authors Schneuwly, S.; Shortridge, R.D.; Larrivee, D.C.; Ono, T.; !1Ozaki, M.; Pak, W.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:5390-5394 !$#title Drosophila ninaA gene encodes an eye-specific cyclophilin !1(cyclosporine A binding protein). !$#cross-references MUID:89315802; PMID:2664782 !$#accession A33906 !'##molecule_type DNA !'##residues 1-237 ##label SCH2 !'##cross-references GB:M22851; NID:g157960; PIDN:AAA28717.1; !1PID:g157961 REFERENCE S03346 !$#authors Shieh, B.H.; Stamnes, M.A.; Seavello, S.; Harris, G.L.; !1Zuker, C.S. !$#journal Nature (1989) 338:67-70 !$#title The ninaA gene required for visual transduction in !1Drosophila encodes a homologue of cyclosporin A-binding !1protein. !$#cross-references MUID:89143766; PMID:2493138 !$#accession S03346 !'##status translation not shown !'##molecule_type DNA !'##residues 1-237 ##label SHI !'##cross-references GB:X14769; NID:g8291; PIDN:CAA32877.1; PID:g3115853 REFERENCE A38388 !$#authors Stamnes, M.A.; Shieh, B.H.; Chuman, L.; Harris, G.L.; Zuker, !1C.S. !$#journal Cell (1991) 65:219-227 !$#title The cyclophilin homolog ninaA is a tissue-specific integral !1membrane protein required for the proper synthesis of a !1subset of Drosophila rhodopsins. !$#cross-references MUID:91199192; PMID:1707759 !$#contents annotation; membrane targeting, cleavable signal sequence, !1glycosylation GENETICS !$#gene ninaA !'##cross-references FlyBase:FBgn0002936 !$#map_position 2 21D3-E2 !$#introns 47/2; 70/1; 126/3 !$#note Neither Inactivation Nor Afterpotential (nina) A FUNCTION !$#description catalyzes the cis-trans isomerization of peptidylproline !1peptide bonds CLASSIFICATION #superfamily peptidylprolyl isomerase; cyclophilin homology KEYWORDS cis-trans-isomerase; cyclosporin A binding; eye; !1glycoprotein; membrane protein; vision FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-237 #product peptidylprolyl isomerase B, eye-specific !8#status predicted #label MAT\ !$26-191 #domain cyclophilin homology #label CYP\ !$68 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 237 #molecular-weight 26351 #checksum 5644 SEQUENCE /// ENTRY CSECA #type complete TITLE peptidylprolyl isomerase (EC 5.2.1.8) A precursor - Escherichia coli (strain K-12) ALTERNATE_NAMES cyclophilin A; cyclosporin A-binding protein A ORGANISM #formal_name Escherichia coli DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 01-Mar-2002 ACCESSIONS A37964; PV0016; D33867; A35785; F65130 REFERENCE A37964 !$#authors Hayano, T.; Takahashi, N.; Kato, S.; Maki, N.; Suzuki, M. !$#journal Biochemistry (1991) 30:3041-3048 !$#title Two distinct forms of peptidylprolyl-cis-trans-isomerase are !1expressed separately in periplasmic and cytoplasmic !1compartments of Escherichia coli cells. !$#cross-references MUID:91175755; PMID:2007139 !$#accession A37964 !'##molecule_type DNA !'##residues 1-190 ##label HAY !'##cross-references GB:M55429; NID:g145286; PIDN:AAA23451.1; !1PID:g145287 REFERENCE PV0016 !$#authors Tran, P.V.; Bannor, T.A.; Doktor, S.Z.; Nichols, B.P. !$#journal J. Bacteriol. (1990) 172:397-410 !$#title Chromosomal organization and expression of Escherichia coli !1pabA. !$#cross-references MUID:90094246; PMID:2403545 !$#accession PV0016 !'##molecule_type DNA !'##residues 37-190 ##label TRA !'##cross-references GB:M32354; NID:g147051; PIDN:AAA24261.1; !1PID:g147052 REFERENCE A33867 !$#authors Kawamukai, M.; Matsuda, H.; Fujii, W.; Utsumi, R.; Komano, !1T. !$#journal J. Bacteriol. (1989) 171:4525-4529 !$#title Nucleotide sequences of fic and fic-1 genes involved in cell !1filamentation induced by cyclic AMP in Escherichia coli. !$#cross-references MUID:89327179; PMID:2546924 !$#accession D33867 !'##molecule_type DNA !'##residues 1-190 ##label KAW !'##cross-references GB:M28363; NID:g145952; PIDN:AAA23772.1; !1PID:g145954 REFERENCE A35785 !$#authors Liu, J.; Walsh, C.T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:4028-4032 !$#title Peptidyl-prolyl cis-trans-isomerase from Escherichia coli: a !1periplasmic homolog of cyclophilin that is not inhibited by !1cyclosporin A. !$#cross-references MUID:90272647; PMID:2190212 !$#accession A35785 !'##status preliminary; nucleic acid sequence not shown; not compared !1with conceptual translation !'##molecule_type DNA !'##residues 1-30 ##label LIU REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65130 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-190 ##label BLAT !'##cross-references GB:AE000412; GB:U00096; NID:g1789758; !1PIDN:AAC76388.1; PID:g1789763; UWGP:b3363 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ppiA !$#map_position 74 min FUNCTION !$#description catalyzes the cis-trans isomerization of peptidylproline !1peptide bonds CLASSIFICATION #superfamily peptidylprolyl isomerase; cyclophilin homology KEYWORDS cis-trans-isomerase; cyclosporin A binding FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-190 #product peptidylprolyl isomerase a #status predicted !8#label MAT SUMMARY #length 190 #molecular-weight 20431 #checksum 1121 SEQUENCE /// ENTRY CSECB #type complete TITLE peptidylprolyl isomerase (EC 5.2.1.8) B - Escherichia coli (strain K-12) ALTERNATE_NAMES cyclophilin B; cyclosporin A-binding protein B ORGANISM #formal_name Escherichia coli DATE 31-Mar-1992 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS D64784; C37964; S17187 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64784 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-164 ##label BLAT !'##cross-references GB:AE000158; GB:U00096; NID:g1786728; !1PIDN:AAC73627.1; PID:g1786736; UWGP:b0525 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A37964 !$#authors Hayano, T.; Takahashi, N.; Kato, S.; Maki, N.; Suzuki, M. !$#journal Biochemistry (1991) 30:3041-3048 !$#title Two distinct forms of peptidylprolyl-cis-trans-isomerase are !1expressed separately in periplasmic and cytoplasmic !1compartments of Escherichia coli cells. !$#cross-references MUID:91175755; PMID:2007139 !$#accession C37964 !'##molecule_type DNA !'##residues 1-131,'E',133-164 ##label HAY !'##cross-references GB:M55430; NID:g145289; PIDN:AAA23453.1; !1PID:g145290 REFERENCE S17186 !$#authors Avalos, J.; Corrochano, L.M.; Brenner, S. !$#journal FEBS Lett. (1991) 286:176-180 !$#title Cysteinyl-tRNA synthetase is a direct descendant of the !1first aminoacyl-tRNA synthetase. !$#cross-references MUID:91323511; PMID:1864365 !$#accession S17187 !'##status translation not shown !'##molecule_type DNA !'##residues 1-68 ##label AVA !'##cross-references EMBL:X59293; NID:g41204; PIDN:CAA41982.1; !1PID:g41205 !'##experimental_source strain K-12 GENETICS !$#gene ppiB FUNCTION !$#description catalyzes the cis-trans isomerization of peptidylproline !1peptide bonds CLASSIFICATION #superfamily peptidylprolyl isomerase; cyclophilin homology KEYWORDS cis-trans-isomerase; cyclosporin A binding SUMMARY #length 164 #molecular-weight 18153 #checksum 6797 SEQUENCE /// ENTRY CSYC42 #type complete TITLE peptidylprolyl isomerase (EC 5.2.1.8) - Synechococcus sp. (strain PCC 7942) ALTERNATE_NAMES cyclophilin; rotamase ORGANISM #formal_name Synechococcus sp. DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 18-Jun-1999 ACCESSIONS S19922 REFERENCE S19921 !$#authors Kaplan, A. !$#submission submitted to the EMBL Data Library, March 1992 !$#accession S19922 !'##molecule_type DNA !'##residues 1-145 ##label KAP !'##cross-references EMBL:X65028; NID:g46488; PIDN:CAA46162.1; !1PID:g46489 GENETICS !$#gene rot FUNCTION !$#description catalyzes the cis-trans isomerization of peptidylproline !1peptide bonds CLASSIFICATION #superfamily peptidylprolyl isomerase; cyclophilin homology KEYWORDS cis-trans-isomerase; cyclosporin A binding SUMMARY #length 145 #molecular-weight 15657 #checksum 7198 SEQUENCE /// ENTRY S75144 #type complete TITLE FKBP-type peptidyl-prolyl cis-trans isomerase - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein slr1761 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S75144 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75144 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-201 ##label KAN !'##cross-references EMBL:D90903; GB:AB001339; NID:g1652127; !1PIDN:BAA17058.1; PID:g1652134 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene ytfC CLASSIFICATION #superfamily BKBP-type peptidylprolyl isomerase; BKBP-type !1peptidylprolyl isomerase homology FEATURE !$113-160 #domain BKBP-type peptidylprolyl isomerase homology !8#label PPI SUMMARY #length 201 #molecular-weight 21555 #checksum 5810 SEQUENCE /// ENTRY A43328 #type complete TITLE peptidylprolyl isomerase (EC 5.2.1.8) FKBP-12 precursor - Streptomyces chrysomallus ALTERNATE_NAMES FK-506-binding protein; fkbA protein ORGANISM #formal_name Streptomyces chrysomallus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A43328; S46229 REFERENCE A43328 !$#authors Pahl, A.; Keller, U. !$#journal J. Bacteriol. (1992) 174:5888-5894 !$#title FK-506-binding proteins from streptomycetes producing !1immunosuppressive macrolactones of the FK-506 type. !$#cross-references MUID:92394892; PMID:1381710 !$#accession A43328 !'##status preliminary !'##molecule_type DNA; protein !'##residues 1-123 ##label PAH !'##cross-references GB:M98428; NID:g153257; PIDN:AAA26745.1; !1PID:g153258 !'##note sequence extracted from NCBI backbone (NCBIN:113034, !1NCBIP:113035) REFERENCE S46227 !$#authors Pahl, A.; Keller, U. !$#journal EMBO J. (1994) 13:3472-3480 !$#title Streptomyces chrysomallus FKBP-33 is a novel immunophilin !1consisting of two FK506 binding domains; its gene is !1transcriptionally coupled to the FKBP-12 gene. !$#cross-references MUID:94341259; PMID:8062824 !$#accession S46229 !'##molecule_type DNA !'##residues 1-8 ##label PAW !'##cross-references GB:Z34523; NID:g535270; PIDN:CAA84282.1; !1PID:g1806280 !'##experimental_source strain ATCC 11523 GENETICS !$#gene fkbA CLASSIFICATION #superfamily BKBP-type peptidylprolyl isomerase; BKBP-type !1peptidylprolyl isomerase homology KEYWORDS cis-trans-isomerase FEATURE !$34-82 #domain BKBP-type peptidylprolyl isomerase homology !8#label PPI SUMMARY #length 123 #molecular-weight 12804 #checksum 1645 SEQUENCE /// ENTRY I40718 #type complete TITLE probable peptidylprolyl isomerase (EC 5.2.1.8) [similarity] - Corynebacterium glutamicum ORGANISM #formal_name Corynebacterium glutamicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Sep-2000 ACCESSIONS I40718 REFERENCE I40717 !$#authors Eikmanns, B.J.; Thum-Schmitz, N.; Eggeling, L.; Luedtke, !1K.U.; Sahm, H. !$#journal Microbiology (1994) 140:1817-1828 !$#title Nucleotide sequence, expression and transcriptional analysis !1of the Corynebacterium glutamicum gltA gene encoding citrate !1synthase. !$#cross-references MUID:95005436; PMID:7522844 !$#accession I40718 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-118 ##label RES !'##cross-references EMBL:X66112; NID:g505580; PIDN:CAA46903.1; !1PID:g550548 CLASSIFICATION #superfamily BKBP-type peptidylprolyl isomerase; BKBP-type !1peptidylprolyl isomerase homology KEYWORDS cis-trans-isomerase FEATURE !$33-79 #domain BKBP-type peptidylprolyl isomerase homology !8#label PPI SUMMARY #length 118 #molecular-weight 12539 #checksum 746 SEQUENCE /// ENTRY S71237 #type complete TITLE probable peptidylprolyl isomerase (EC 5.2.1.8) FKBP15-1 - Arabidopsis thaliana ALTERNATE_NAMES FK-binding protein 15-1; immunophilin ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S71237 REFERENCE S71237 !$#authors Luan, S.; Kudla, J.; Gruissem, W.; Schreiber, S.L. !$#submission submitted to the EMBL Data Library, March 1996 !$#description Molecular characterization of a FKBP-type immunophilin from !1higher plants. !$#accession S71237 !'##molecule_type mRNA !'##residues 1-146 ##label LUA !'##cross-references EMBL:U52046; NID:g1272405; PIDN:AAC49390.1; !1PID:g1272406 GENETICS !$#gene FKBP15-1 CLASSIFICATION #superfamily BKBP-type peptidylprolyl isomerase; BKBP-type !1peptidylprolyl isomerase homology KEYWORDS cis-trans-isomerase FEATURE !$45-92 #domain BKBP-type peptidylprolyl isomerase homology !8#label PPI SUMMARY #length 146 #molecular-weight 15689 #checksum 830 SEQUENCE /// ENTRY JT0748 #type complete TITLE FK506-binding protein - Botryllus schlosseri ORGANISM #formal_name Botryllus schlosseri DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JT0748; S40074 REFERENCE JT0748 !$#authors Pancer, Z.; Gershon, H.; Rinkevich, B. !$#journal Biochem. Biophys. Res. Commun. (1993) 197:973-977 !$#title cDNA cloning of a putative protochordate FK506-binding !1protein. !$#cross-references MUID:94092189; PMID:7505578 !$#accession JT0748 !'##molecule_type mRNA !'##residues 1-134 ##label PAN !'##cross-references EMBL:X76006; NID:g435470; PIDN:CAA53594.1; !1PID:g435471 CLASSIFICATION #superfamily BKBP-type peptidylprolyl isomerase; BKBP-type !1peptidylprolyl isomerase homology FEATURE !$41-88 #domain BKBP-type peptidylprolyl isomerase homology !8#label PPI SUMMARY #length 134 #molecular-weight 14777 #checksum 6990 SEQUENCE /// ENTRY S55332 #type complete TITLE macrophage infectivity potentiator TcMIP - Trypanosoma cruzi ALTERNATE_NAMES peptidyl-prolyl cis-trans isomerase ORGANISM #formal_name Trypanosoma cruzi DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S55332; S55518 REFERENCE S55332 !$#authors Moro, A.; Ruiz-Cabello, F.; Fernandez-Cano, A.; Stock, R.P.; !1Gonzalez, A. !$#journal EMBO J. (1995) 14:2483-2490 !$#title Secretion by Trypanosoma cruzi of a peptidyl-prolyl !1cis-trans isomerase involved in cell infection. !$#cross-references MUID:95300780; PMID:7540135 !$#accession S55332 !'##status preliminary !'##molecule_type DNA !'##residues 1-196 ##label MOR !'##cross-references EMBL:X69655; NID:g861148; PIDN:CAA49346.1; !1PID:g861149 CLASSIFICATION #superfamily BKBP-type peptidylprolyl isomerase; BKBP-type !1peptidylprolyl isomerase homology FEATURE !$85-130 #domain BKBP-type peptidylprolyl isomerase homology !8#label PPI SUMMARY #length 196 #molecular-weight 22136 #checksum 1720 SEQUENCE /// ENTRY S46228 #type complete TITLE peptidylprolyl isomerase (EC 5.2.1.8) FKBP-33 precursor - Streptomyces chrysomallus ALTERNATE_NAMES fkbB protein ORGANISM #formal_name Streptomyces chrysomallus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S46228 REFERENCE S46227 !$#authors Pahl, A.; Keller, U. !$#journal EMBO J. (1994) 13:3472-3480 !$#title Streptomyces chrysomallus FKBP-33 is a novel immunophilin !1consisting of two FK506 binding domains; its gene is !1transcriptionally coupled to the FKBP-12 gene. !$#cross-references MUID:94341259; PMID:8062824 !$#accession S46228 !'##molecule_type DNA !'##residues 1-311 ##label PAH !'##cross-references GB:Z34523; NID:g535270; PIDN:CAA84280.1; !1PID:g633644 !'##experimental_source ATCC 11523 GENETICS !$#gene fkbB CLASSIFICATION #superfamily peptidylprolyl isomerase FKBP33; BKBP-type !1peptidylprolyl isomerase homology KEYWORDS blocked amino end; cis-trans-isomerase; lipoprotein FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-311 #product peptidylprolyl isomerase FKBP-33 #status !8predicted #label MAT\ !$77-125 #domain BKBP-type peptidylprolyl isomerase homology !8#label PPI1\ !$224-271 #domain BKBP-type peptidylprolyl isomerase homology !8#label PPI2\ !$19 #modified_site fatty acylated amino end (Cys) (in !8mature form) #status predicted\ !$19 #binding_site sn-2,3-diacylglycerol (Cys) (covalent) !8#status predicted SUMMARY #length 311 #molecular-weight 32869 #checksum 7451 SEQUENCE /// ENTRY CSBYC3 #type complete TITLE peptidylprolyl isomerase (EC 5.2.1.8) SCC3 precursor - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES cyclophilin SCC3; PPIase SCC3; protein YCR069w; protein YCR070w ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jun-2000 ACCESSIONS S26658; S26587; S19484; S19517 REFERENCE S26658 !$#authors Franco, L.; Jimenez, A.; Demolder, J.; Molemans, F.; Fiers, !1W.; Contreras, R. !$#journal Yeast (1991) 7:971-979 !$#title The nucleotide sequence of a third cyclophilin-homologous !1gene from Saccharomyces cerevisiae. !$#cross-references MUID:92206076; PMID:1803821 !$#accession S26658 !'##molecule_type DNA !'##residues 1-318 ##label FRA REFERENCE S26587 !$#authors Ballesta, J.P.G.; Franco, L.; Hoenicka, J.; Jimenez, A.; !1Remacha, M.; Sanz, E. !$#submission submitted to the Protein Sequence Database, October 1992 !$#accession S26587 !'##molecule_type DNA !'##residues 1-318 ##label BAL1 !'##cross-references EMBL:X59720; NID:g1907116; PIDN:CAA42275.1; !1PID:g1907209; GSPDB:GN00003; MIPS:YCR069w !'##note this is a revision to the sequence in reference S19482 and !1S19486 REFERENCE S19482 !$#authors Contreras, R.; Demolder, J.; Fiers, W.; Molemans, F. !$#submission submitted to the Protein Sequence Database, March 1992 !$#accession S19484 !'##molecule_type DNA !'##residues 1-170 ##label CON !'##cross-references EMBL:X59720; GSPDB:GN00003; MIPS:YCR069w !'##note this sequence has been revised in reference S26587, resulting !1in extension of the reading frame REFERENCE S19486 !$#authors Ballesta, J.P.G.; Franco, L.; Hoenicka, J.; Jimenez, A.; !1Remacha, M.; Sanz, E. !$#submission submitted to the Protein Sequence Database, March 1992 !$#accession S19517 !'##molecule_type DNA !'##residues 'MTGLKDSQWPILDLILTPRN',165-318 ##label BAL2 !'##cross-references EMBL:X59720 !'##note this was assumed to be protein YCR070w; the difference at the !1amino end is due to a frameshift error !'##note this sequence has been revised in reference S26587 GENETICS !$#gene SGD:SCC3; MIPS:YCR069w !'##cross-references MIPS:YCR069w; SGD:S0000665 !$#map_position 3R FUNCTION !$#description catalyzes the cis-trans isomerization of peptidylproline !1peptide bonds CLASSIFICATION #superfamily peptidylprolyl isomerase SCC3; cyclophilin !1homology KEYWORDS cis-trans-isomerase; glycoprotein; transmembrane protein FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-318 #product peptidylprolyl isomerase SCC3 #status !8predicted #label MAT\ !$51-279 #domain cyclophilin homology #label CYP\ !$286-303 #domain transmembrane #status predicted #label TMM\ !$166 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 318 #molecular-weight 35780 #checksum 5296 SEQUENCE /// ENTRY S63359 #type complete TITLE probable membrane protein YNR028w - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein N3255 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S63359 REFERENCE S63346 !$#authors Pohl, T.M. !$#submission submitted to the Protein Sequence Database, April 1996 !$#accession S63359 !'##molecule_type DNA !'##residues 1-308 ##label POH !'##cross-references EMBL:Z71643; NID:g1302520; PIDN:CAA96308.1; !1PID:g1302521; GSPDB:GN00014; MIPS:YNR028w !'##experimental_source strain S288C GENETICS !$#gene SGD:CPR8; MIPS:YNR028w !'##cross-references SGD:S0005311 !$#map_position 14R CLASSIFICATION #superfamily peptidylprolyl isomerase SCC3; cyclophilin !1homology KEYWORDS transmembrane protein FEATURE !$4-20 #domain transmembrane #status predicted #label TM1\ !$272-288 #domain transmembrane #status predicted #label TM2 SUMMARY #length 308 #molecular-weight 34946 #checksum 1066 SEQUENCE /// ENTRY S72485 #type complete TITLE peptidylprolyl isomerase (EC 5.2.1.8) ROF1 - Arabidopsis thaliana ALTERNATE_NAMES FK506-binding protein; immunophilin; rotamase ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S72485; S72484 REFERENCE S72484 !$#authors Vucich, V.A.; Gasser, C.S. !$#journal Mol. Gen. Genet. (1996) 252:510-517 !$#title Novel structure of a high molecular weight FK506 binding !1protein from Arabidopsis thaliana. !$#cross-references MUID:97071666; PMID:8914512 !$#accession S72485 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-551 ##label VUC !'##cross-references EMBL:U57838; NID:g1373395; PIDN:AAB82062.1; !1PID:g1373396 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1May 1996 !$#accession S72484 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-429,'V',431-551 ##label VUW !'##cross-references EMBL:U49453; NID:g1354206; PIDN:AAB82061.1; !1PID:g1354207 GENETICS !$#gene ROF1 !$#introns 62/1; 91/1; 178/1; 203/1; 230/1; 295/1; 326/1; 384/3; 425/3; !1474/3; 517/2; 549/3 CLASSIFICATION #superfamily peptidylprolyl isomerase ROF1; BKBP-type !1peptidylprolyl isomerase homology; tetratricopeptide repeat !1homology KEYWORDS calmodulin binding; cis-trans-isomerase FEATURE !$57-104 #domain BKBP-type peptidylprolyl isomerase homology !8#label PPI1\ !$173-216 #domain BKBP-type peptidylprolyl isomerase homology !8#label PPI2\ !$290-339 #domain BKBP-type peptidylprolyl isomerase homology !8#label PPI3\ !$414-447 #domain tetratricopeptide repeat homology #label TT1\ !$449-482 #domain tetratricopeptide repeat homology #label TT2\ !$483-516 #domain tetratricopeptide repeat homology #label TT3\ !$529-546 #region calmodulin-binding #status predicted SUMMARY #length 551 #molecular-weight 61453 #checksum 4942 SEQUENCE /// ENTRY S55383 #type complete TITLE peptidylprolyl isomerase (EC 5.2.1.8) - wheat ALTERNATE_NAMES FK506-binding protein; peptidylprolyl cis-trans isomerase; PPIase ORGANISM #formal_name Triticum aestivum #common_name common wheat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S55383 REFERENCE S55383 !$#authors Oshra, B.; Breiman, A. !$#submission submitted to the EMBL Data Library, May 1995 !$#description Wheat FKBP70 - A novel heat shock and calmodulin binding !1PPIase. !$#accession S55383 !'##molecule_type mRNA !'##residues 1-559 ##label OSH !'##cross-references EMBL:X86903; NID:g854625; PIDN:CAA60505.1; !1PID:g854626 GENETICS !$#gene FKBP70 CLASSIFICATION #superfamily peptidylprolyl isomerase ROF1; BKBP-type !1peptidylprolyl isomerase homology; tetratricopeptide repeat !1homology KEYWORDS calmodulin binding; cis-trans-isomerase; cyclosporin A !1binding FEATURE !$60-107 #domain BKBP-type peptidylprolyl isomerase homology !8#label PPI1\ !$176-219 #domain BKBP-type peptidylprolyl isomerase homology !8#label PPI\ !$293-341 #domain BKBP-type peptidylprolyl isomerase homology !8#label PPI2\ !$415-448 #domain tetratricopeptide repeat homology #label TT1\ !$450-483 #domain tetratricopeptide repeat homology #label TT2\ !$484-517 #domain tetratricopeptide repeat homology #label TT3 SUMMARY #length 559 #molecular-weight 62056 #checksum 260 SEQUENCE /// ENTRY A42386 #type complete TITLE hsp 90-binding protein p59 - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A42386 REFERENCE A42386 !$#authors Lebeau, M.C.; Massol, N.; Herrick, J.; Faber, L.E.; Renoir, !1J.M.; Radanyi, C.; Baulieu, E.E. !$#journal J. Biol. Chem. (1992) 267:4281-4284 !$#title P59, an hsp 90-binding protein. Cloning and sequencing of !1its cDNA and preparation of a peptide-directed polyclonal !1antibody. !$#cross-references MUID:92165768; PMID:1537818 !$#accession A42386 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-458 ##label LEB !'##cross-references GB:M84988; NID:g165594; PIDN:AAA31439.1; !1PID:g165595 !'##experimental_source liver !'##note sequence extracted from NCBI backbone (NCBIP:83839) CLASSIFICATION #superfamily human FK506-binding protein FKBP51; BKBP-type !1peptidylprolyl isomerase homology; tetratricopeptide repeat !1homology FEATURE !$50-97 #domain BKBP-type peptidylprolyl isomerase homology !8#label PPI\ !$319-352 #domain tetratricopeptide repeat homology #label TT1\ !$353-386 #domain tetratricopeptide repeat homology #label TT2 SUMMARY #length 458 #molecular-weight 51475 #checksum 5701 SEQUENCE /// ENTRY S55971 #type complete TITLE probable peptidylprolyl isomerase (EC 5.2.1.8) YLR449w [similarity] - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein L9324.3 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S55971 REFERENCE S55966 !$#authors Du, Z. !$#submission submitted to the EMBL Data Library, March 1995 !$#description The sequence of S. cerevisiae cosmid 9324. !$#accession S55971 !'##molecule_type DNA !'##residues 1-392 ##label DUZ !'##cross-references GB:U22382; NID:g717059; PIDN:AAB67528.1; !1PID:g717062; GSPDB:GN00012; MIPS:YLR449w !'##experimental_source strain S288C (AB972) GENETICS !$#gene SGD:FPR4; MIPS:YLR449w !'##cross-references SGD:S0004441 !$#map_position 12R CLASSIFICATION #superfamily yeast peptidylprolyl isomerase FPR3; BKBP-type !1peptidylprolyl isomerase homology KEYWORDS cis-trans-isomerase FEATURE !$306-352 #domain BKBP-type peptidylprolyl isomerase homology !8#label PPI SUMMARY #length 392 #molecular-weight 43903 #checksum 6752 SEQUENCE /// ENTRY JQ1522 #type complete TITLE peptidylprolyl isomerase (EC 5.2.1.8) FKBP3 - human ALTERNATE_NAMES rapamycin/FK506-binding protein 25K (FKBP25) ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JQ1522; JT0605; A42774 REFERENCE JQ1522 !$#authors Hung, D.T.; Schreiber, S.L. !$#journal Biochem. Biophys. Res. Commun. (1992) 184:733-738 !$#title cDNA cloning of a human 25kDa FK506 and rapamycin binding !1protein. !$#cross-references MUID:92246959; PMID:1374240 !$#accession JQ1522 !'##molecule_type mRNA !'##residues 1-224 ##label HUN !'##cross-references GB:M90309; NID:g182643; PIDN:AAA58475.1; !1PID:g182644 !'##experimental_source brain REFERENCE JT0605 !$#authors Wiederrecht, G.; Martin, M.M.; Sigal, N.H.; Siekierka, J.J. !$#journal Biochem. Biophys. Res. Commun. (1992) 185:298-303 !$#title Isolation of a human cDNA encoding A 25 kDa FK-506 and !1rapamycin binding protein. !$#cross-references MUID:92287110; PMID:1376117 !$#accession JT0605 !'##molecule_type mRNA !'##residues 1-224 ##label WIE !'##cross-references GB:M96256; NID:g182625; PIDN:AAA58471.1; !1PID:g182626 REFERENCE A42774 !$#authors Jin, Y.J.; Burakoff, S.J.; Bierer, B.E. !$#journal J. Biol. Chem. (1992) 267:10942-10945 !$#title Molecular cloning of a 25-kDa high affinity rapamycin !1binding protein, FKBP25. !$#cross-references MUID:92283784; PMID:1375932 !$#accession A42774 !'##molecule_type mRNA !'##residues 1-180,'A',182-224 ##label JIN !'##experimental_source thymus !'##note sequence extracted from NCBI backbone (NCBIN:104737, !1NCBIP:104738) GENETICS !$#gene GDB:FKBP3 !'##cross-references GDB:132611; OMIM:186947 !$#map_position 11q13.1-11q13.3 CLASSIFICATION #superfamily human peptidylprolyl isomerase FKPB3; BKBP-type !1peptidylprolyl isomerase homology KEYWORDS cis-trans-isomerase; cyclosporin A binding FEATURE !$128-182 #domain BKBP-type peptidylprolyl isomerase homology !8#label PPI SUMMARY #length 224 #molecular-weight 25177 #checksum 4711 SEQUENCE /// ENTRY S66681 #type complete TITLE peptidylprolyl isomerase (EC 5.2.1.8) A - human ALTERNATE_NAMES cyclophilin; cyclosporin A-binding protein; peptidyl-prolyl cis-trans isomerase ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S66681; S61070 REFERENCE S66681 !$#authors Tropschug, M. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S66681 !'##molecule_type mRNA !'##residues 1-301 ##label TRO !'##note this is a revision to the sequence from reference S61070 REFERENCE S61070 !$#authors Tropschug, M. !$#submission submitted to the Protein Sequence Database, February 1996 !$#accession S61070 !'##molecule_type mRNA !'##residues 67-301 ##label TRW !'##note this sequence has been revised in reference S66681 GENETICS !$#gene CyP33 CLASSIFICATION #superfamily human peptidylprolyl isomerase A; cyclophilin !1homology; ribonucleoprotein repeat homology KEYWORDS cis-trans-isomerase; cyclosporin A binding FEATURE !$7-74 #domain ribonucleoprotein repeat homology #label !8RRM4\ !$139-300 #domain cyclophilin homology #label CYP SUMMARY #length 301 #molecular-weight 33431 #checksum 1947 SEQUENCE /// ENTRY JC4751 #type complete TITLE FK506-binding protein p50 - fluke (Schistosoma mansoni) ORGANISM #formal_name Schistosoma mansoni DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JC4751 REFERENCE JC4751 !$#authors Kiang, D.; Karim, A.M.; LoVerde, P.T. !$#journal Gene (1996) 170:137-140 !$#title Cloning the gene encoding Schistosoma mansoni p50, an !1immunophilin. !$#cross-references MUID:96200870; PMID:8621074 !$#accession JC4751 !'##molecule_type mRNA !'##residues 1-430 ##label KIA !'##cross-references GB:L42969; NID:g862449; PIDN:AAB05213.1; !1PID:g862450 COMMENT This is a member of FK506-binding protein family. It !1functions as molecular chaperones in protein folding. GENETICS !$#gene Smp50 !$#introns 89/1; 134/3; 141/3; 170/3; 349/3; 408/3 CLASSIFICATION #superfamily FK506-binding protein p50; BKBP-type !1peptidylprolyl isomerase homology; tetratricopeptide repeat !1homology FEATURE !$51-102 #domain BKBP-type peptidylprolyl isomerase homology !8#label PPI\ !$307-340 #domain tetratricopeptide repeat homology #label TT1\ !$341-374 #domain tetratricopeptide repeat homology #label TT2 SUMMARY #length 430 #molecular-weight 48208 #checksum 7372 SEQUENCE /// ENTRY ISHUT #type complete TITLE triose-phosphate isomerase (EC 5.3.1.1) [validated] - human ALTERNATE_NAMES triosephosphate mutase ORGANISM #formal_name Homo sapiens #common_name man DATE 28-Feb-1986 #sequence_revision 03-May-1996 #text_change 08-Dec-2000 ACCESSIONS S29743; A01164; A23441; A05104 REFERENCE S29743 !$#authors Belgrader, P.; Boyer, T.; Daar, I.; Cheng, J.; Nesic, D.; !1Maquat, L.E. !$#submission submitted to the EMBL Data Library, December 1992 !$#accession S29743 !'##molecule_type DNA !'##residues 1-249 ##label BEL !'##cross-references EMBL:X69723; NID:g1906326; PIDN:CAA49379.1; !1PID:g37247 REFERENCE A01164 !$#authors Maquat, L.E.; Chilcote, R.; Ryan, P.M. !$#journal J. Biol. Chem. (1985) 260:3748-3753 !$#title Human triosephosphate isomerase cDNA and protein structure. !1Studies of triosephosphate isomerase deficiency in man. !$#cross-references MUID:85131186; PMID:2579079 !$#accession A01164 !'##molecule_type mRNA !'##residues 2-249 ##label MAQ !'##cross-references GB:M10036; NID:g339840; PIDN:AAB59511.1; !1PID:g339841 REFERENCE A23441 !$#authors Brown, J.R.; Daar, I.O.; Krug, J.R.; Maquat, L.E. !$#journal Mol. Cell. Biol. (1985) 5:1694-1706 !$#title Characterization of the functional gene and several !1processed pseudogenes in the human triosephosphate isomerase !1gene family. !$#cross-references MUID:85267686; PMID:4022011 !$#accession A23441 !'##molecule_type DNA !'##residues 2-249 ##label BRO !'##cross-references GB:M10036; GB:M10037; NID:g339840; PIDN:AAB59511.1; !1PID:g339841 REFERENCE A05104 !$#authors Lu, H.S.; Yuan, P.M.; Gracy, R.W. !$#journal J. Biol. Chem. (1984) 259:11958-11968 !$#title Primary structure of human triosephosphate isomerase. !$#cross-references MUID:85006925; PMID:6434534 !$#accession A05104 !'##molecule_type protein !'##residues 2-19,'KN',22-26,'S',28-29,'QG',32-42,'IG',45-48,'L',50-57, !1'Q',59-61,'AG',64-118,'N',120-153,'D',155-166,'N',168-182, !1'E',184-203,'Q',205-230,'I',232-243,'L',245-249 ##label LUH COMMENT The functional molecule catalyzes the interconversion of !1glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. !1It plays an important role in several metabolic pathways. GENETICS !$#gene GDB:TPI1 !'##cross-references GDB:119617; OMIM:190450 !$#map_position 12p13-12p13 !$#introns 39/1; 80/2; 108/3; 153/1; 181/3; 211/1 CLASSIFICATION #superfamily triose-phosphate isomerase KEYWORDS gluconeogenesis; glycolysis; homodimer; intramolecular !1oxidoreductase; isomerase; pentose phosphate pathway FEATURE !$2-249 #product triose-phosphate isomerase #status !8experimental #label MAT\ !$96,166 #active_site His, Glu #status predicted SUMMARY #length 249 #molecular-weight 26669 #checksum 9678 SEQUENCE /// ENTRY ISCZT1 #type complete TITLE triose-phosphate isomerase (EC 5.3.1.1) 1 - chimpanzee ALTERNATE_NAMES triosephosphate mutase ORGANISM #formal_name Pan troglodytes #common_name chimpanzee DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 20-Apr-2000 ACCESSIONS JH0375 REFERENCE JH0375 !$#authors Craig, L.C.; Pirtle, I.L.; Gracy, R.W.; Pirtle, R.M. !$#journal Gene (1991) 99:217-227 !$#title Characterization of the transcription unit and two processed !1pseudogenes of chimpanzee triosephosphate isomerase (TPI). !$#cross-references MUID:91216462; PMID:2022334 !$#accession JH0375 !'##molecule_type DNA !'##residues 1-249 ##label CRA !'##cross-references GB:M57946; NID:g176959; PIDN:AAA35438.1; !1PID:g176960 COMMENT This enzyme catalyzes the interconversion of glyceraldehyde !13-phosphate and dihydroxyacetone phosphate. GENETICS !$#gene TPI !$#introns 39/1; 80/2; 108/3; 153/1; 181/3; 211/1 CLASSIFICATION #superfamily triose-phosphate isomerase KEYWORDS gluconeogenesis; glycolysis; homodimer; intramolecular !1oxidoreductase; isomerase; pentose phosphate pathway FEATURE !$2-249 #product triose-phosphate isomerase #status predicted !8#label MAT\ !$96,166 #active_site His, Glu #status predicted SUMMARY #length 249 #molecular-weight 26669 #checksum 9678 SEQUENCE /// ENTRY ISMQTR #type complete TITLE triose-phosphate isomerase (EC 5.3.1.1) - rhesus macaque ALTERNATE_NAMES triosephosphate mutase ORGANISM #formal_name Macaca mulatta #common_name rhesus macaque DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jun-2000 ACCESSIONS S01378 REFERENCE S01378 !$#authors Old, S.E.; Mohrenweiser, H.W. !$#journal Nucleic Acids Res. (1988) 16:9055 !$#title Nucleotide sequence of the triosephosphate isomerase gene !1from Macaca mulatta. !$#cross-references MUID:89016592; PMID:3174447 !$#accession S01378 !'##molecule_type DNA !'##residues 1-249 ##label OLD !'##cross-references EMBL:X08023; NID:g38101; PID:g1200106 COMMENT This enzyme catalyzes the interconversion of glyceraldehyde !13-phosphate and dihydroxyacetone phosphate. GENETICS !$#introns 39/1; 80/2; 108/3; 153/1; 181/3; 211/1 CLASSIFICATION #superfamily triose-phosphate isomerase KEYWORDS gluconeogenesis; glycolysis; homodimer; intramolecular !1oxidoreductase; isomerase; pentose phosphate pathway FEATURE !$2-249 #product triose-phosphate isomerase #status predicted !8#label MAT\ !$96,166 #active_site His, Glu #status predicted SUMMARY #length 249 #molecular-weight 26710 #checksum 9601 SEQUENCE /// ENTRY ISRBT #type complete TITLE triose-phosphate isomerase (EC 5.3.1.1) - rabbit ALTERNATE_NAMES triosephosphate mutase ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 24-Apr-1984 #sequence_revision 31-Dec-1991 #text_change 20-Apr-2000 ACCESSIONS A01165; I46518 REFERENCE A90279 !$#authors Corran, P.H.; Waley, S.G. !$#journal Biochem. J. (1975) 145:335-344 !$#title The amino acid sequence of rabbit muscle triose phosphate !1isomerase. !$#cross-references MUID:75224611; PMID:1171682 !$#accession A01165 !'##molecule_type protein !'##residues 1-248 ##label COR REFERENCE A90351 !$#authors Hartman, F.C. !$#journal Biochemistry (1971) 10:146-154 !$#title Haloacetol phosphates. Characterization of the active site !1of rabbit muscle triose phosphate isomerase. !$#cross-references MUID:71058464; PMID:4922541 !$#contents annotation; active site REFERENCE I46471 !$#authors Putney, S.D.; Herlihy, W.C.; Schimmel, P. !$#journal Nature (1983) 302:718-721 !$#title A new troponin T and cDNA clones for 13 different muscle !1proteins, found by shotgun sequencing. !$#cross-references MUID:83167564; PMID:6687628 !$#accession I46518 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 56-83 ##label PUT !'##cross-references EMBL:V00902; NID:g1748; PIDN:CAA24267.1; !1PID:g929770 COMMENT The functional molecule catalyzes the interconversion of !1glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. !1It plays an important role in several metabolic pathways. CLASSIFICATION #superfamily triose-phosphate isomerase KEYWORDS gluconeogenesis; glycolysis; homodimer; intramolecular !1oxidoreductase; isomerase; pentose phosphate pathway FEATURE !$95 #active_site His #status predicted\ !$165 #active_site Glu #status experimental SUMMARY #length 248 #molecular-weight 26625 #checksum 7416 SEQUENCE /// ENTRY ISMST #type complete TITLE triose-phosphate isomerase (EC 5.3.1.1) - mouse ALTERNATE_NAMES triosephosphate mutase ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 20-Apr-2000 ACCESSIONS S10490 REFERENCE S10490 !$#authors Cheng, J.; Mielnicki, L.M.; Pruitt, S.C.; Maquat, L.E. !$#journal Nucleic Acids Res. (1990) 18:4261 !$#title Nucleotide sequence of murine triosephosphate isomerase !1cDNA. !$#cross-references MUID:90332435; PMID:2377473 !$#accession S10490 !'##molecule_type mRNA !'##residues 1-249 ##label CHE !'##cross-references GB:X53333; NID:g54854; PIDN:CAA37420.1; PID:g54855 COMMENT This enzyme catalyzes the interconversion of glyceraldehyde !13-phosphate and dihydroxyacetone phosphate. CLASSIFICATION #superfamily triose-phosphate isomerase KEYWORDS gluconeogenesis; glycolysis; homodimer; intramolecular !1oxidoreductase; isomerase; pentose phosphate pathway FEATURE !$2-249 #product triose-phosphate isomerase #status predicted !8#label MAT\ !$96,166 #active_site His, Glu #status predicted SUMMARY #length 249 #molecular-weight 26695 #checksum 9099 SEQUENCE /// ENTRY ISCHT #type complete TITLE triose-phosphate isomerase (EC 5.3.1.1) - chicken ALTERNATE_NAMES triosephosphate mutase ORGANISM #formal_name Gallus gallus #common_name chicken DATE 24-Apr-1984 #sequence_revision 31-Dec-1991 #text_change 20-Apr-2000 ACCESSIONS A23448; A22953; A01166; S71596 REFERENCE A23448 !$#authors Straus, D.; Gilbert, W. !$#journal Mol. Cell. Biol. (1985) 5:3497-3506 !$#title Genetic engineering in the Precambrian: structure of the !1chicken triosephosphate isomerase gene. !$#cross-references MUID:86310829; PMID:3837846 !$#accession A23448 !'##molecule_type DNA !'##residues 1-248 ##label STR !'##cross-references GB:M11941; NID:g212773; PIDN:AAA49095.1; !1PID:g212774 REFERENCE A22953 !$#authors Straus, D.; Gilbert, W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:2014-2018 !$#title Chicken triosephosphate isomerase complements an Escherichia !1coli deficiency. !$#cross-references MUID:85166263; PMID:3885220 !$#accession A22953 !'##molecule_type mRNA !'##residues 1-248 ##label STR2 !'##cross-references GB:M11314; NID:g212771; PIDN:AAA49094.1; !1PID:g212772 REFERENCE A90273 !$#authors Furth, A.J.; Milman, J.D.; Priddle, J.D.; Offord, R.E. !$#journal Biochem. J. (1974) 139:11-22 !$#title Studies on the subunit structure and amino acid sequence of !1triose phosphate isomerase from chicken breast muscle. !$#cross-references MUID:75204720; PMID:4463937 !$#accession A01166 !'##molecule_type protein !'##residues 2-16,'KR',18-28,'D',30-144,'QE',147-193,'T',195-201,'VQS', !1205-248 ##label FUR !'##note this sequence has been corrected in reference A93175 REFERENCE A93175 !$#authors Banner, D.W.; Bloomer, A.C.; Petsko, G.A.; Phillips, D.C.; !1Pogson, C.I.; Wilson, I.A.; Corran, P.H.; Furth, A.J.; !1Milman, J.D.; Offord, R.E.; Priddle, J.D.; Waley, S.G. !$#journal Nature (1975) 255:609-614 !$#title Structure of chicken muscle triose phosphate isomerase !1determined crystallographically at 2.5 angstrom resolution. !$#cross-references MUID:75175220; PMID:1134550 !$#contents annotation; X-ray crystallography, 2.5 angstroms; sequence !1revision REFERENCE S71595 !$#authors Zhang, Y.; Yueksel, K.U.; Gracy, R.W. !$#journal Arch. Biochem. Biophys. (1995) 317:112-120 !$#title Terminal marking of avian triosephosphate isomerases by !1deamidation and oxidation. !$#cross-references MUID:95177640; PMID:7872772 !$#accession S71596 !'##molecule_type protein !'##residues 2-25 ##label ZHA GENETICS !$#introns 38/1; 79/2; 107/3; 152/1; 180/3; 210/1 COMPLEX homodimer FUNCTION !$#description catalyzes interconversion of dihydroxyacetone phosphate and !1D-glyceraldehyd 3-phosphate !$#note plays an important role in several metabolic pathways CLASSIFICATION #superfamily triose-phosphate isomerase KEYWORDS gluconeogenesis; glycolysis; homodimer; intramolecular !1oxidoreductase; isomerase; pentose phosphate pathway FEATURE !$2-248 #product triose-phosphate isomerase #status !8experimental #label MAT\ !$95,165 #active_site His, Glu #status predicted SUMMARY #length 248 #molecular-weight 26620 #checksum 3440 SEQUENCE /// ENTRY ISLAT #type complete TITLE triose-phosphate isomerase (EC 5.3.1.1) - coelacanth (tentative sequence) ALTERNATE_NAMES triosephosphate mutase ORGANISM #formal_name Latimeria chalumnae #common_name coelacanth DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 20-Apr-2000 ACCESSIONS A01167 REFERENCE A01167 !$#authors Kolb, E.; Harris, J.I.; Bridgen, J. !$#journal Biochem. J. (1974) 137:185-197 !$#title Triose phosphate isomerase from the coelacanth. An approach !1to the rapid determination of an amino acid sequence with !1small amounts of material. !$#cross-references MUID:74148425; PMID:4824206 !$#accession A01167 !'##molecule_type protein !'##residues 1-247 ##label KOL COMMENT The functional molecule catalyzes the interconversion of !1glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. !1It plays an important role in several metabolic pathways. CLASSIFICATION #superfamily triose-phosphate isomerase KEYWORDS gluconeogenesis; glycolysis; homodimer; intramolecular !1oxidoreductase; isomerase; pentose phosphate pathway FEATURE !$94,164 #active_site His, Glu #status predicted SUMMARY #length 247 #molecular-weight 26731 #checksum 5743 SEQUENCE /// ENTRY ISZMT #type complete TITLE triose-phosphate isomerase (EC 5.3.1.1) - maize ALTERNATE_NAMES triosephosphate mutase ORGANISM #formal_name Zea mays #common_name maize DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 20-Apr-2000 ACCESSIONS A25501 REFERENCE A25501 !$#authors Marchionni, M.; Gilbert, W. !$#journal Cell (1986) 46:133-141 !$#title The triosephosphate isomerase gene from maize: introns !1antedate the plant-animal divergence. !$#cross-references MUID:86245049; PMID:3755078 !$#accession A25501 !'##molecule_type DNA !'##residues 1-253 ##label MAR !'##cross-references GB:N00043; GB:M13357; GB:L00371; NID:g459897; !1PIDN:AAB81110.1; PID:g168647 COMMENT This enzyme catalyzes the interconversion of glyceraldehyde !13-phosphate and dihydroxyacetone phosphate. GENETICS !$#introns 13/3; 39/1; 80/2; 108/3; 153/1; 184/3; 211/1; 238/3 CLASSIFICATION #superfamily triose-phosphate isomerase KEYWORDS gluconeogenesis; glycolysis; homodimer; intramolecular !1oxidoreductase; isomerase; pentose phosphate pathway FEATURE !$2-249 #product triose-phosphate isomerase #status predicted !8#label MAT\ !$96,166 #active_site His, Glu #status predicted SUMMARY #length 253 #molecular-weight 27025 #checksum 2429 SEQUENCE /// ENTRY ISASTN #type complete TITLE triose-phosphate isomerase (EC 5.3.1.1) - Emericella nidulans ALTERNATE_NAMES triosephosphate mutase ORGANISM #formal_name Emericella nidulans, Aspergillus nidulans DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jun-2000 ACCESSIONS A25502 REFERENCE A25502 !$#authors McKnight, G.L.; O'Hara, P.J.; Parker, M.L. !$#journal Cell (1986) 46:143-147 !$#title Nucleotide sequence of the triosephosphate isomerase gene !1from Aspergillus nidulans: implications for a differential !1loss of introns. !$#cross-references MUID:86245050; PMID:3521890 !$#accession A25502 !'##molecule_type DNA !'##residues 1-249 ##label MCK !'##cross-references GB:D10019; GB:M13362; NID:g217920; PIDN:BAA00908.1; !1PID:g217921 COMMENT This enzyme catalyzes the interconversion of glyceraldehyde !13-phosphate and dihydroxyacetone phosphate. GENETICS !$#introns 13/2; 106/3; 131/3; 169/2; 241/1 CLASSIFICATION #superfamily triose-phosphate isomerase KEYWORDS gluconeogenesis; glycolysis; homodimer; intramolecular !1oxidoreductase; isomerase; pentose phosphate pathway FEATURE !$2-249 #product triose-phosphate isomerase #status predicted !8#label MAT\ !$94,166 #active_site His, Glu #status predicted SUMMARY #length 249 #molecular-weight 27157 #checksum 6121 SEQUENCE /// ENTRY ISBYT #type complete TITLE triose-phosphate isomerase (EC 5.3.1.1) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YD9609.05c; protein YDR050c; triosephosphate mutase ORGANISM #formal_name Saccharomyces cerevisiae DATE 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 21-Jul-2000 ACCESSIONS A01168; S54035 REFERENCE A01168 !$#authors Alber, T.; Kawasaki, G. !$#journal J. Mol. Appl. Genet. (1982) 1:419-434 !$#title Nucleotide sequence of the triose phosphate isomerase gene !1of Saccharomyces cerevisiae. !$#cross-references MUID:83110641; PMID:6759603 !$#accession A01168 !'##molecule_type DNA !'##residues 1-248 ##label ALB !'##cross-references GB:J01366; NID:g173007; PIDN:AAA88757.1; !1PID:g1197083 REFERENCE S54031 !$#authors Hunt, S.; Bowman, S.; Harris, D. !$#submission submitted to the EMBL Data Library, May 1995 !$#accession S54035 !'##molecule_type DNA !'##residues 1-248 ##label HUN !'##cross-references EMBL:Z49209; NID:g798897; PIDN:CAA89080.1; !1PID:g798902; GSPDB:GN00004; MIPS:YDR050c COMMENT The functional molecule catalyzes the interconversion of !1glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. !1It plays an important role in several metabolic pathways. GENETICS !$#gene SGD:TPI1; MIPS:YDR050c !'##cross-references SGD:S0002457; MIPS:YDR050c !$#map_position 4R COMPLEX homodimer CLASSIFICATION #superfamily triose-phosphate isomerase KEYWORDS gluconeogenesis; glycolysis; homodimer; intramolecular !1oxidoreductase; isomerase; pentose phosphate pathway FEATURE !$2-248 #product triose-phosphate isomerase #status predicted !8#label MAT\ !$95,165 #active_site His, Glu #status predicted SUMMARY #length 248 #molecular-weight 26795 #checksum 8957 SEQUENCE /// ENTRY ISZPT #type complete TITLE triose-phosphate isomerase (EC 5.3.1.1) - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES triosephosphate mutase ORGANISM #formal_name Schizosaccharomyces pombe DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 20-Apr-2000 ACCESSIONS A23987; S57640 REFERENCE A23987 !$#authors Russell, P.R. !$#journal Gene (1985) 40:125-130 !$#title Transcription of the triose-phosphate-isomerase gene of !1Schizosaccharomyces pombe initiates from a start point !1different from that in Saccharomyces cerevisiae. !$#cross-references MUID:86137408; PMID:3912263 !$#accession A23987 !'##molecule_type DNA !'##residues 1-250 ##label RUS !'##cross-references GB:M14432 REFERENCE S57640 !$#authors Ropp, P.A.; Copeland, W.C. !$#submission submitted to the EMBL Data Library, January 1995 !$#description Molecular characterization of the gene for the mitochondrial !1DNA polymerase from Schizosaccharomyces pombe. !$#accession S57640 !'##molecule_type DNA !'##residues 195-212,'N',214-240,'H',243-250 ##label ROP !'##cross-references EMBL:Z47976; NID:g1129170; PIDN:CAA88011.1; !1PID:g886715 COMMENT The functional molecule catalyzes the interconversion of !1glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. !1It plays an important role in several metabolic pathways. GENETICS !$#gene tpi CLASSIFICATION #superfamily triose-phosphate isomerase KEYWORDS gluconeogenesis; glycolysis; homodimer; intramolecular !1oxidoreductase; isomerase; pentose phosphate pathway FEATURE !$2-250 #product triose-phosphate isomerase #status predicted !8#label MAT\ !$95,165 #active_site His, Glu #status predicted SUMMARY #length 250 #molecular-weight 27235 #checksum 3665 SEQUENCE /// ENTRY ISUTTB #type complete TITLE triose-phosphate isomerase (EC 5.3.1.1) - Trypanosoma brucei ALTERNATE_NAMES triosephosphate mutase ORGANISM #formal_name Trypanosoma brucei DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 20-Apr-2000 ACCESSIONS A25110; A25186 REFERENCE A25110 !$#authors Swinkels, B.W.; Gibson, W.C.; Osinga, K.A.; Kramer, R.; !1Veeneman, G.H.; van Boom, J.H.; Borst, P. !$#journal EMBO J. (1986) 5:1291-1298 !$#title Characterization of the gene for the microbody (glycosomal) !1triosephosphate isomerase of Trypanosoma brucei. !$#cross-references MUID:86274631; PMID:3015595 !$#accession A25110 !'##molecule_type DNA !'##residues 1-250 ##label SWI !'##cross-references GB:X03921 COMMENT This enzyme catalyzes the interconversion of glyceraldehyde !13-phosphate and dihydroxyacetone phosphate. CLASSIFICATION #superfamily triose-phosphate isomerase KEYWORDS gluconeogenesis; glycolysis; homodimer; intramolecular !1oxidoreductase; isomerase; pentose phosphate pathway FEATURE !$2-250 #product triose-phosphate isomerase #status predicted !8#label MAT\ !$95,167 #active_site His, Glu #status predicted SUMMARY #length 250 #molecular-weight 26920 #checksum 4834 SEQUENCE /// ENTRY ISECT #type complete TITLE triose-phosphate isomerase (EC 5.3.1.1) - Escherichia coli (strain K-12) ALTERNATE_NAMES phosphotriose isomerase; triosephosphate mutase ORGANISM #formal_name Escherichia coli DATE 31-Mar-1989 #sequence_revision 10-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS B65198; A30260; S40862 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65198 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-255 ##label BLAT !'##cross-references GB:AE000466; GB:U00096; NID:g2367328; !1PIDN:AAC76901.1; PID:g1790353; UWGP:b3919 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A30260 !$#authors Pichersky, E.; Gottlieb, L.D.; Hess, J.F. !$#journal Mol. Gen. Genet. (1984) 195:314-320 !$#title Nucleotide sequence of the triose phosphate isomerase gene !1of Escherichia coli. !$#cross-references MUID:85035844; PMID:6092857 !$#accession A30260 !'##molecule_type DNA !'##residues 1-66,'N',68-255 ##label PIC !'##cross-references GB:X00617; NID:g43111; PIDN:CAA25253.1; PID:g43112 REFERENCE S40802 !$#authors Plunkett III, G.; Burland, V.; Daniels, D.L.; Blattner, F.R. !$#journal Nucleic Acids Res. (1993) 21:3391-3398 !$#title Analysis of the Escherichia coli genome. III. DNA sequence !1of the region from 87.2 to 89.2 minutes. !$#cross-references MUID:93347969; PMID:8346018 !$#accession S40862 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-255 ##label PLU !'##cross-references EMBL:L19201; NID:g304961; PIDN:AAB03051.1; !1PID:g305022 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1993 COMMENT This enzyme, a dimer of identical chains, catalyzes the !1interconversion of glyceraldehyde-3-phosphate and !1dihydroxyacetone phosphate. GENETICS !$#gene tpiA !$#map_position 88 min CLASSIFICATION #superfamily triose-phosphate isomerase KEYWORDS gluconeogenesis; glycolysis; intramolecular oxidoreductase; !1isomerase; pentose phosphate pathway FEATURE !$95,167 #active_site His, Glu #status predicted SUMMARY #length 255 #molecular-weight 26972 #checksum 7557 SEQUENCE /// ENTRY ISBSTF #type complete TITLE triose-phosphate isomerase (EC 5.3.1.1) - Bacillus stearothermophilus ORGANISM #formal_name Bacillus stearothermophilus DATE 30-Nov-1980 #sequence_revision 22-Nov-1996 #text_change 18-Jun-1999 ACCESSIONS JT0768; S22079; S32428; A01169 REFERENCE JT0768 !$#authors Rentier-Delrue, F.; Moyens, S.; Lion, M.; Martial, J.A. !$#journal Gene (1993) 134:137-138 !$#title Sequence of the triosephosphate isomerase-encoding gene !1isolated from the thermophile Bacillus stearothermophilus. !$#cross-references MUID:94063509; PMID:8244026 !$#accession JT0768 !'##molecule_type DNA !'##residues 1-253 ##label REN REFERENCE S22079 !$#authors Rentier-Delrue, F.; Mande, S.C.; Moyens, S.; Mainfroid, V.; !1Goraj, K.; Lion, M.; Hol, W.G.J.; Martial, J.A. !$#submission submitted to the EMBL Data Library, June 1992 !$#description Structure and comparison of the proteins expressed from !1cloned triosephosphate isomerase genes of psychrophilic and !1thermophilic bacteriae. !$#accession S22079 !'##molecule_type DNA !'##residues 1-253 ##label RE2 !'##cross-references EMBL:X66129; NID:g49092; PIDN:CAA46920.1; !1PID:g49093 REFERENCE S32427 !$#authors Rentier-Delrue, F.; Mande, S.C.; Moyens, S.; Terpstra, P.; !1Mainfroid, V.; Goraj, K.; Lion, M.; Hol, W.G.J.; Martial, !1J.A. !$#journal J. Mol. Biol. (1993) 229:85-93 !$#title Cloning and overexpression of the triosephosphate isomerase !1genes from psychrophilic and thermophilic bacteria. !1Structural comparison of the predicted protein sequences. !$#cross-references MUID:93132805; PMID:8421318 !$#accession S32428 !'##molecule_type DNA !'##residues 1-106,'D',108-253 ##label RE3 !'##cross-references EMBL:X66129 REFERENCE A01169 !$#authors Artavanis-Tsakonas, S.; Harris, J.I. !$#journal Eur. J. Biochem. (1980) 108:599-611 !$#title Primary structure of triosephosphate isomerase from Bacillus !1stearothermophilus. !$#cross-references MUID:81003882; PMID:6105959 !$#accession A01169 !'##molecule_type protein !'##residues 1-36,'D',38-40,42-46,49-59,'Q',60-69,'BZ',72-99,'H', !1101-103,'Z',105,'BZ',108-109,'B',111-134,'Q',136-137,'E', !1139,'D',141-143,145-156,'QE',159-160,'IIL',165-168,'L', !1170-180,'ZB',183,'B',185-224,'ZZZ',228,'B',230,'A',232-247, !1'Q',249-253 ##label ART !'##note there is no direct positive experimental evidence for the !1identities of residues 99-101; the identifications of !1residues 162-166 are tentative COMMENT This enzyme is a dimeric glycolytic enzyme catalyzing the !1interconversion of dihydroxyacetone phosphate and !1glyceraldehyde-3-phosphate. CLASSIFICATION #superfamily triose-phosphate isomerase KEYWORDS gluconeogenesis; glycolysis; intramolecular oxidoreductase; !1isomerase; pentose phosphate pathway FEATURE !$95 #active_site His #status predicted\ !$167 #active_site Glu #status experimental SUMMARY #length 253 #molecular-weight 27206 #checksum 5741 SEQUENCE /// ENTRY ISECAB #type complete TITLE L-arabinose isomerase (EC 5.3.1.4) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS F64727; A29022; S40578; S35946 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64727 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-500 ##label BLAT !'##cross-references GB:AE000116; GB:U00096; NID:g1786240; !1PIDN:AAC73173.1; PID:g1786248; UWGP:b0062 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A91559 !$#authors Lee, N.; Gielow, W.; Martin, R.; Hamilton, E.; Fowler, A. !$#journal Gene (1986) 47:231-244 !$#title The organization of the araBAD operon of Escherichia coli. !$#cross-references MUID:87163495; PMID:3549454 !$#accession A29022 !'##molecule_type DNA !'##residues 1-247,'E',249-359,'V',361-500 ##label LEE REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40578 !'##molecule_type DNA !'##residues 1-71,'P',73-247,'E',249-359,'V',361-500 ##label YUR !'##cross-references EMBL:D10483; NID:g216434; PIDN:BAA01333.1; !1PID:g216482 REFERENCE S35946 !$#authors Bachellier, S.; Saurin, W.; Perrin, D.; Hofnung, M.; Gilson, !1E. !$#submission submitted to the EMBL Data Library, July 1993 !$#description Two major families of bacterial interspersed mosaic elements !1(BIME) : Differential gyrase binding and synergy with IHF. !$#accession S35946 !'##status preliminary !'##molecule_type DNA !'##residues 458-500 ##label BAC !'##cross-references EMBL:X74279; NID:g417622; PIDN:CAA52340.1; !1PID:g417623 GENETICS !$#gene araA !$#map_position 1 min FUNCTION !$#description catalyzes the conversion of L-arabinose to L-ribulose, the !1first step in arabinose metabolism CLASSIFICATION #superfamily L-arabinose isomerase KEYWORDS arabinose metabolism; intramolecular oxidoreductase; !1isomerase SUMMARY #length 500 #molecular-weight 56074 #checksum 8492 SEQUENCE /// ENTRY ISEBAB #type complete TITLE L-arabinose isomerase (EC 5.3.1.4) - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 18-Jun-1999 ACCESSIONS A24985 REFERENCE A24985 !$#authors Lin, H.C.; Lei, S.P.; Wilcox, G. !$#journal Gene (1985) 34:123-128 !$#title The araBAD operon of Salmonella typhimurium LT2. II. !1Nucleotide sequence of araA and primary structure of its !1product, L-arabinose isomerase. !$#cross-references MUID:85232045; PMID:3891513 !$#accession A24985 !'##molecule_type DNA !'##residues 1-500 ##label LIN !'##cross-references GB:M11047; GB:M11045; GB:M11046; NID:g153866; !1PIDN:AAA27024.1; PID:g153868 !'##experimental_source strain LT2 GENETICS !$#gene araA !$#map_position 2 FUNCTION !$#description catalyzes the conversion of L-arabinose to L-ribulose !$#pathway arabinose metabolism !$#note first step in pathway CLASSIFICATION #superfamily L-arabinose isomerase KEYWORDS arabinose metabolism; intramolecular oxidoreductase; !1isomerase SUMMARY #length 500 #molecular-weight 55877 #checksum 5616 SEQUENCE /// ENTRY ISECX1 #type complete TITLE xylose isomerase (EC 5.3.1.5) - Escherichia coli (strain K-12) ALTERNATE_NAMES xylose ketol-isomerase ORGANISM #formal_name Escherichia coli DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 01-Mar-2002 ACCESSIONS A30252; A01170; S47786; A01171; G65155 REFERENCE A92483 !$#authors Schellenberg, G.D.; Sarthy, A.; Larson, A.E.; Backer, M.P.; !1Crabb, J.W.; Lidstrom, M.; Hall, B.D.; Furlong, C.E. !$#journal J. Biol. Chem. (1984) 259:6826-6832 !$#title Xylose isomerase from Escherichia coli: characterization of !1the protein and the structural gene. !$#cross-references MUID:84212522; PMID:6327696 !$#accession A30252 !'##molecule_type DNA !'##residues 1-440 ##label SCH !'##cross-references GB:K01996; NID:g148278; PIDN:AAA24768.1; !1PID:g148279 REFERENCE A90043 !$#authors Lawlis, V.B.; Dennis, M.S.; Chen, E.Y.; Smith, D.H.; Henner, !1D.J. !$#journal Appl. Environ. Microbiol. (1984) 47:15-21 !$#title Cloning and sequencing of the xylose isomerase and xylulose !1kinase genes of Escherichia coli. !$#cross-references MUID:84126725; PMID:6320721 !$#accession A01170 !'##molecule_type DNA !'##residues 1-440 ##label LAW !'##cross-references GB:X04691; NID:g43313 !'##note the translation in PID:g43314 uses an alternative initiator !1four codons before that shown, and begins 'MEFN' REFERENCE S47666 !$#authors Plunkett, G. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S47786 !'##molecule_type DNA !'##residues 1-440 ##label PLU !'##cross-references EMBL:U00039; NID:g466582; PIDN:AAB18542.1; !1PID:g466703 REFERENCE A01171 !$#authors Briggs, K.A.; Lancashire, W.E.; Hartley, B.S. !$#journal EMBO J. (1984) 3:611-616 !$#title Molecular cloning, DNA structure and expression of the !1Escherichia coli D-xylose isomerase. !$#cross-references MUID:84182534; PMID:6325179 !$#accession A01171 !'##status significant sequence differences !'##molecule_type DNA !'##cross-references GB:X00772; NID:g41303; PID:g41304 !'##note this sequence has several frameshift errors REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65155 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-440 ##label BLAT !'##cross-references GB:AE000433; GB:U00096; NID:g1789977; !1PIDN:AAC76589.1; PID:g1789988; UWGP:b3565 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene xylA !$#map_position 80 min COMPLEX homotetramer FUNCTION !$#description catalyzes isomerization of the aldopentose D-xylose to the !12-ketopentose D-xylulose !$#pathway xylose metabolism CLASSIFICATION #superfamily xylose isomerase KEYWORDS homotetramer; intramolecular oxidoreductase; isomerase; !1magnesium; xylose metabolism FEATURE !$101,104 #active_site His, Asp #status predicted\ !$141,234 #binding_site substrate (Thr, Lys) #status predicted\ !$232,268,296,339 #binding_site magnesium (Glu, Glu, Asp, Asp) #status !8predicted\ !$268,271,307,309 #binding_site magnesium (Glu, His, Asp, Asp) #status !8predicted SUMMARY #length 440 #molecular-weight 49742 #checksum 6429 SEQUENCE /// ENTRY ISKBX #type complete TITLE xylose isomerase (EC 5.3.1.5) - Klebsiella pneumoniae ORGANISM #formal_name Klebsiella pneumoniae DATE 03-Feb-1994 #sequence_revision 06-Dec-1996 #text_change 18-Jun-1999 ACCESSIONS S25069 REFERENCE S25069 !$#authors Feldmann, S.D.; Sahm, H.; Sprenger, G.A. !$#journal Mol. Gen. Genet. (1992) 234:201-210 !$#title Cloning and expression of the genes for xylose isomerase and !1xylulokinase from Klebsiella pneumoniae 1033 in Escherichia !1coli K12. !$#cross-references MUID:92374988; PMID:1324398 !$#accession S25069 !'##molecule_type DNA !'##residues 1-440 ##label FEL !'##cross-references EMBL:X61059; EMBL:S43323; NID:g43951; !1PIDN:CAA43389.1; PID:g43952 GENETICS !$#gene xylA FUNCTION !$#description catalyzes isomerization of the aldopentose D-xylose to the !12-ketopentose D-xylulose !$#pathway xylose metabolism CLASSIFICATION #superfamily xylose isomerase KEYWORDS intramolecular oxidoreductase; isomerase; magnesium; xylose !1metabolism FEATURE !$101,104 #active_site His, Asp #status predicted\ !$141,234 #binding_site substrate (Thr, Lys) #status predicted\ !$232,268,296,339 #binding_site magnesium (Glu, Glu, Asp, Asp) #status !8predicted\ !$268,271,307,309 #binding_site magnesium (Glu, His, Asp, Asp) #status !8predicted SUMMARY #length 440 #molecular-weight 49919 #checksum 7865 SEQUENCE /// ENTRY ISHIX #type complete TITLE xylose isomerase (EC 5.3.1.5) - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 18-Aug-1995 #sequence_revision 06-Dec-1996 #text_change 18-Jun-1999 ACCESSIONS D64183 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession D64183 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-439 ##label TIGR !'##cross-references GB:U32791; GB:L42023; NID:g1574662; !1PIDN:AAC22766.1; PID:g1574666; TIGR:HI1112 GENETICS !$#gene xylA !$#map_position FOR1177317-1178636 FUNCTION !$#description catalyzes isomerization of the aldopentose D-xylose to the !12-ketopentose D-xylulose !$#pathway xylose metabolism CLASSIFICATION #superfamily xylose isomerase KEYWORDS intramolecular oxidoreductase; isomerase; magnesium; xylose !1metabolism FEATURE !$101,104 #active_site His, Asp #status predicted\ !$141,234 #binding_site substrate (Thr, Lys) #status predicted\ !$232,268,296,339 #binding_site magnesium (Glu, Glu, Asp, Asp) #status !8predicted\ !$268,271,307,309 #binding_site magnesium (Glu, His, Asp, Asp) #status !8predicted SUMMARY #length 439 #molecular-weight 49896 #checksum 8502 SEQUENCE /// ENTRY ISCLXH #type complete TITLE xylose isomerase (EC 5.3.1.5) - Thermoanaerobacter thermohydrosulfuricus ALTERNATE_NAMES xylose ketol-isomerase ORGANISM #formal_name Thermoanaerobacter thermohydrosulfuricus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jun-2000 ACCESSIONS JQ0849 REFERENCE JQ0849 !$#authors Dekker, K.; Yamagata, H.; Sakaguchi, K.; Udaka, S. !$#journal Agric. Biol. Chem. (1991) 55:221-227 !$#title Xylose (glucose) isomerase gene from the thermophile !1Clostridium thermohydrosulfuricum; cloning, sequencing, and !1expression in Escherichia coli. !$#cross-references MUID:91248487; PMID:1368665 !$#accession JQ0849 !'##molecule_type DNA !'##residues 1-438 ##label DEK !'##cross-references GB:D00756; NID:g216423; PIDN:BAA00652.1; !1PID:g216424 GENETICS !$#gene xylA COMPLEX homotetramer FUNCTION !$#description catalyzes isomerization of the aldopentose D-xylose to the !12-ketopentose D-xylulose !$#pathway xylose metabolism CLASSIFICATION #superfamily xylose isomerase KEYWORDS homotetramer; intramolecular oxidoreductase; isomerase; !1magnesium; xylose metabolism FEATURE !$100,103 #active_site His, Asp #status predicted\ !$140,233 #binding_site substrate (Thr, Lys) #status predicted\ !$231,267,295,338 #binding_site magnesium (Glu, Glu, Asp, Asp) #status !8predicted\ !$267,270,306,308 #binding_site magnesium (Glu, His, Asp, Asp) #status !8predicted SUMMARY #length 438 #molecular-weight 50157 #checksum 6035 SEQUENCE /// ENTRY ISCLXM #type complete TITLE xylose isomerase (EC 5.3.1.5) - Thermoanaerobacterium thermosulfurigenes ALTERNATE_NAMES xylose ketol-isomerase ORGANISM #formal_name Thermoanaerobacterium thermosulfurigenes DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 18-Jun-1999 ACCESSIONS A36598; S15119 REFERENCE A36598 !$#authors Lee, C.; Bagdasarian, M.; Meng, M.; Zeikus, J.G. !$#journal J. Biol. Chem. (1990) 265:19082-19090 !$#title Catalytic mechanism of xylose (glucose) isomerase from !1Clostridium thermosulfurogenes. Characterization of the !1structural gene and function of active site histidine. !$#cross-references MUID:91035437; PMID:2229064 !$#accession A36598 !'##molecule_type DNA !'##residues 1-439 ##label LEE !'##cross-references GB:J05650; NID:g144929; PIDN:AAA23285.1; !1PID:g144930 REFERENCE S15119 !$#authors Lee, C.; Zeikus, J.G. !$#journal Biochem. J. (1991) 273:565-571 !$#title Purification and characterization of thermostable glucose !1isomerase from Clostridium thermosulfurogenes and !1Thermoanaerobacter strain B6A. !$#cross-references MUID:91144536; PMID:1996956 !$#accession S15119 !'##status preliminary !'##molecule_type protein !'##residues 1-7 ##label BIO !'##note the sequence from page 568 is inconsistent with that from page !1565 in having 6-Gln !'##note the source is given as Clostridium thermosulfurogenes GENETICS !$#gene xylA COMPLEX homotetramer FUNCTION !$#description catalyzes isomerization of the aldopentose D-xylose to the !12-ketopentose D-xylulose !$#pathway xylose metabolism CLASSIFICATION #superfamily xylose isomerase KEYWORDS homotetramer; intramolecular oxidoreductase; isomerase; !1magnesium; xylose metabolism FEATURE !$101,104 #active_site His, Asp #status predicted\ !$141,234 #binding_site substrate (Thr, Lys) #status predicted\ !$232,268,296,339 #binding_site magnesium (Glu, Glu, Asp, Asp) #status !8predicted\ !$268,271,307,309 #binding_site magnesium (Glu, His, Asp, Asp) #status !8predicted SUMMARY #length 439 #molecular-weight 50475 #checksum 8891 SEQUENCE /// ENTRY ISBSXS #type complete TITLE xylose isomerase (EC 5.3.1.5) - Bacillus subtilis ALTERNATE_NAMES xylose isomerase xylA; xylose ketol-isomerase ORGANISM #formal_name Bacillus subtilis DATE 30-Jun-1992 #sequence_revision 05-Dec-1998 #text_change 16-Jun-2000 ACCESSIONS C69735; A24346; I40039 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69735 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-445 ##label KUN !'##cross-references GB:Z99113; GB:AL009126; NID:g2634090; !1PIDN:CAB13644.1; PID:g2634144 !'##experimental_source strain 168 REFERENCE A24346 !$#authors Wilhelm, M.; Hollenberg, C.P. !$#journal Nucleic Acids Res. (1985) 13:5717-5722 !$#title Nucleotide sequence of the Bacillus subtilis xylose !1isomerase gene: extensive homology between the Bacillus and !1Escherichia coli enzyme. !$#cross-references MUID:85297769; PMID:2994009 !$#accession A24346 !'##molecule_type DNA !'##residues 1-8,'V',10-14,'V',16-19,'F',21-23,'A',25-44,'M',46-85,'RA', !188-126,'I',128,'V',130-137,'D',139,'N',141-213,'N',215-229, !1'E',231-245,'T',247-358,'V',360-404,'T',406-420,'N',422,'T', !1424-432,'R',434-435,'P',437-440 ##label WIL !'##cross-references GB:K03311; GB:X02795; NID:g40248; PIDN:CAA26562.1; !1PID:g40249 !'##experimental_source strain W168 REFERENCE I40039 !$#authors Wilhelm, M.; Hollenberg, C.P. !$#journal EMBO J. (1984) 3:2555-2560 !$#title Selective cloning of Bacillus subtilis xylose isomerase and !1xylulokinase in Escherichia coli genes by IS5-mediated !1expression. !$#cross-references MUID:85076575; PMID:6096130 !$#accession I40039 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-8,'V',10-14,'V',16-19,'F',21-23,'A',25-44,'M',46-85,'RA', !188-101,'Q',103-118 ##label RES !'##cross-references GB:K03312; GB:X01109; NID:g143837; PIDN:AAA22895.1; !1PID:g143839 !'##experimental_source strain W168 GENETICS !$#gene xylA COMPLEX homotetramer FUNCTION !$#description catalyzes isomerization of the aldopentose D-xylose to the !12-ketopentose D-xylulose !$#pathway xylose metabolism CLASSIFICATION #superfamily xylose isomerase KEYWORDS homotetramer; intramolecular oxidoreductase; isomerase; !1magnesium; xylose metabolism FEATURE !$107,110 #active_site His, Asp #status predicted\ !$147,240 #binding_site substrate (Thr, Lys) #status predicted\ !$238,274,302,345 #binding_site magnesium (Glu, Glu, Asp, Asp) #status !8predicted\ !$274,277,313,315 #binding_site magnesium (Glu, His, Asp, Asp) #status !8predicted SUMMARY #length 445 #molecular-weight 50252 #checksum 612 SEQUENCE /// ENTRY ISMAXM #type complete TITLE xylose isomerase (EC 5.3.1.5) [validated] - Actinoplanes missouriensis ALTERNATE_NAMES xylose ketol-isomerase ORGANISM #formal_name Actinoplanes missouriensis DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 15-Sep-2000 ACCESSIONS S05998 REFERENCE S05998 !$#authors Amore, R.; Hollenberg, C.P. !$#journal Nucleic Acids Res. (1989) 17:7515 !$#title Xylose isomerase from Actinoplanes missouriensis: primary !1structure of the gene and the protein. !$#cross-references MUID:90016811; PMID:2798103 !$#accession S05998 !'##molecule_type DNA !'##residues 1-394 ##label AMO !'##cross-references EMBL:X16042; NID:g38870; PIDN:CAA34164.1; !1PID:g580713 !'##note the authors translated the initiation codon GTG for residue 1 !1as Val REFERENCE A51549 !$#authors Janin, J. !$#submission submitted to the Brookhaven Protein Data Bank, April 1992 !$#cross-references PDB:6XIM !$#contents annotation; X-ray crystallography, 2.5 angstroms, with !1xylose and magnesium, residues 3-394 REFERENCE A58417 !$#authors Rey, F.; Jenkins, J.; Janin, J.; Lasters, I.; Alard, P.; !1Claessens, M.; Matthyssens, G.; Wodak, S. !$#journal Proteins (1988) 4:165-172 !$#title Structural analysis of the 2.8 angstroms model of xylose !1isomerase from Actinoplanes missouriensis. !$#cross-references MUID:89184498; PMID:3237716 !$#contents annotation; X-ray crystallography, 2.8 angstroms GENETICS !$#start_codon GTG COMPLEX homotetramer FUNCTION !$#description catalyzes isomerization of the aldopentose D-xylose to the !12-ketopentose D-xylulose !$#pathway xylose metabolism CLASSIFICATION #superfamily xylose isomerase KEYWORDS homotetramer; intramolecular oxidoreductase; isomerase; !1magnesium; xylose metabolism FEATURE !$54,57 #active_site His, Asp #status experimental\ !$90,183 #binding_site substrate (Thr, Lys) #status !8experimental\ !$181,217,245,292 #binding_site magnesium (Glu, Glu, Asp, Asp) #status !8experimental\ !$217,220,255,257 #binding_site magnesium (Glu, His, Asp, Asp) #status !8experimental SUMMARY #length 394 #molecular-weight 43498 #checksum 4247 SEQUENCE /// ENTRY ISMAXA #type complete TITLE xylose isomerase (EC 5.3.1.5) - Ampullariella sp. ALTERNATE_NAMES xylose ketol-isomerase ORGANISM #formal_name Ampullariella sp. DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 06-Dec-1996 ACCESSIONS A27756 REFERENCE A27756 !$#authors Saari, G.C.; Kumar, A.A.; Kawasaki, G.H.; Insley, M.Y.; !1O'Hara, P.J. !$#journal J. Bacteriol. (1987) 169:612-618 !$#title Sequence of the Ampullariella sp. strain 3876 gene coding !1for xylose isomerase. !$#cross-references MUID:87109047; PMID:3027039 !$#accession A27756 !'##molecule_type DNA !'##residues 1-394 ##label SAA !'##cross-references GB:M15050 !'##experimental_source strain 3876 GENETICS !$#start_codon GTG COMPLEX homotetramer FUNCTION !$#description catalyzes isomerization of the aldopentose D-xylose to the !12-ketopentose D-xylulose !$#pathway xylose metabolism CLASSIFICATION #superfamily xylose isomerase KEYWORDS homotetramer; intramolecular oxidoreductase; isomerase; !1magnesium; xylose metabolism FEATURE !$54,57 #active_site His, Asp #status predicted\ !$90,183 #binding_site substrate (Thr, Lys) #status predicted\ !$181,217,245,292 #binding_site magnesium (Glu, Glu, Asp, Asp) #status !8predicted\ !$217,220,255,257 #binding_site magnesium (Glu, His, Asp, Asp) #status !8predicted SUMMARY #length 394 #molecular-weight 43336 #checksum 5609 SEQUENCE /// ENTRY S16214 #type complete TITLE xylose isomerase (EC 5.3.1.5) [validated] - Arthrobacter sp. ALTERNATE_NAMES D-glucose isomerase ORGANISM #formal_name Arthrobacter sp. DATE 21-Nov-1993 #sequence_revision 06-Dec-1996 #text_change 15-Sep-2000 ACCESSIONS S16214; S16212; S28154 REFERENCE S16213 !$#authors Loviny-Anderton, T.; Shaw, P.C.; Shin, M.K.; Hartley, B.S. !$#journal Biochem. J. (1991) 277:263-271 !$#title D-Xylose (D-glucose) isomerase from Arthrobacter strain !1N.R.R.L. B3728. Gene cloning, sequence and expression. !$#cross-references MUID:91307531; PMID:1854339 !$#accession S16214 !'##molecule_type DNA !'##residues 1-395 ##label BIO !'##cross-references EMBL:X59466; NID:g39058; PIDN:CAA42073.1; !1PID:g39059 !'##experimental_source strain NRRL B3728 REFERENCE S16212 !$#authors Smith, C.A.; Rangarajan, M.; Hartley, B.S. !$#journal Biochem. J. (1991) 277:255-261 !$#title D-Xylose (D-glucose) isomerase from Arthrobacter strain !1N.R.R.L. B3728. Purification and properties. !$#cross-references MUID:91307530; PMID:1854338 !$#accession S16212 !'##molecule_type protein !'##residues 2-21 ##label SMI !'##experimental_source strain NRRL B3728 !'##note other peptide sequences were also determined REFERENCE S28154 !$#authors Siddiqui, K.S.; Rangarajan, M.; Hartley, B.S.; Kitmitto, A.; !1Panico, M.; Blench, I.P.; Morris, H.R. !$#journal Biochem. J. (1993) 289:201-208 !$#title Arthrobacter D-xylose isomerase: partial proteolysis with !1thermolysin. !$#cross-references MUID:93143669; PMID:8424759 !$#accession S28154 !'##molecule_type protein !'##residues 337-348 ##label SID REFERENCE A50702 !$#authors Henrick, K.; Collyer, C.A.; Blow, D.M. !$#submission submitted to the Brookhaven Protein Data Bank, July 1989 !$#cross-references PDB:4XIA !$#contents annotation; X-ray crystallography, 2.3 angstroms, with !1D-sorbitol, residues 3-31,'A',33-64,'A',66-79,'A',81-395 REFERENCE A58418 !$#authors Henrick, K.; Collyer, C.A.; Blow, D.M. !$#journal J. Mol. Biol. (1989) 208:129-157 !$#title Structures of D-xylose isomerase from Arthrobacter strain !1B3728 containing the inhibitors xylitol and D-sorbitol at !12.5 angstroms and 2.3 angstroms resolution, respectively. !$#cross-references MUID:89362453; PMID:2769749 !$#contents annotation; X-ray crystallography, 2.3 angstroms REFERENCE A51428 !$#authors Collyer, C.A.; Henrick, K.; Blow, D.M. !$#submission submitted to the Brookhaven Protein Data Bank, October 1991 !$#cross-references PDB:1XLC !$#contents annotation; X-ray crystallography, 2.5 angstroms, with !1D-xylose/xylulose and magnesium, residues 3-395 REFERENCE A58419 !$#authors Collyer, C.A.; Henrick, K.; Blow, D.M. !$#journal J. Mol. Biol. (1990) 212:211-235 !$#title Mechanism for aldose-ketose interconversion by D-xylose !1isomerase involving ring opening followed by a 1,2-hydride !1shift. !$#cross-references MUID:90204542; PMID:2319597 !$#contents annotation; X-ray crystallography, 2.5 angstroms GENETICS !$#gene xylA COMPLEX homotetramer FUNCTION !$#description catalyzes isomerization of the aldopentose D-xylose to the !12-ketopentose D-xylulose !$#pathway xylose metabolism CLASSIFICATION #superfamily xylose isomerase KEYWORDS homotetramer; intramolecular oxidoreductase; isomerase; !1magnesium; xylose metabolism FEATURE !$2-395 #product xylose isomerase #status experimental #label !8MAT\ !$54,57 #active_site His, Asp #status experimental\ !$90,183 #binding_site substrate (Thr, Lys) #status !8experimental\ !$181,217,245,293 #binding_site magnesium (Glu, Glu, Asp, Asp) #status !8experimental\ !$217,220,255,257 #binding_site magnesium (Glu, His, Asp, Asp) #status !8experimental SUMMARY #length 395 #molecular-weight 43291 #checksum 8047 SEQUENCE /// ENTRY ISSMXR #type complete TITLE xylose isomerase (EC 5.3.1.5) - Streptomyces rochei ALTERNATE_NAMES xylose ketol-isomerase ORGANISM #formal_name Streptomyces rochei DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 07-May-1999 ACCESSIONS JN0086 REFERENCE JN0086 !$#authors Kikuchi, T.; Itoh, Y.; Kasumi, T.; Fukazawa, C. !$#journal Agric. Biol. Chem. (1990) 54:2469-2472 !$#title Molecular cloning of the xylA gene encoding xylose isomerase !1from Streptomyces griseofuscus S-41; primary structure of !1the gene and its product. !$#cross-references MUID:91136786; PMID:1368583 !$#accession JN0086 !'##molecule_type DNA !'##residues 1-394 ##label KIK COMMENT Phe-26, Phe-94, and Trp-136 have been demonstrated to be !1involved in facilitating substrate binding. GENETICS !$#gene xylA COMPLEX homotetramer FUNCTION !$#description catalyzes isomerization of the aldopentose D-xylose to the !12-ketopentose D-xylulose !$#pathway xylose metabolism CLASSIFICATION #superfamily xylose isomerase KEYWORDS homotetramer; intramolecular oxidoreductase; isomerase; !1magnesium; xylose metabolism FEATURE !$2-394 #product xylose isomerase #status predicted #label !8MAT\ !$54,57 #active_site His, Asp #status predicted\ !$90,182 #binding_site substrate (Thr, Lys) #status predicted\ !$180,216,244,285 #binding_site magnesium (Glu, Glu, Asp, Asp) #status !8predicted\ !$216,219,254,256 #binding_site magnesium (Glu, His, Asp, Asp) #status !8predicted SUMMARY #length 394 #molecular-weight 43644 #checksum 6797 SEQUENCE /// ENTRY ISSMXV #type complete TITLE xylose isomerase (EC 5.3.1.5) - Streptomyces violaceusniger ALTERNATE_NAMES xylose ketol-isomerase ORGANISM #formal_name Streptomyces violaceusniger DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 18-Jun-1999 ACCESSIONS S01436 REFERENCE S01436 !$#authors Drocourt, D.; Bejar, S.; Calmels, T.; Reynes, J.P.; Tiraby, !1G. !$#journal Nucleic Acids Res. (1988) 16:9337 !$#title Nucleotide sequence of the xylose isomerase gene from !1Streptomyces violaceoniger. !$#cross-references MUID:89016633; PMID:3174453 !$#accession S01436 !'##molecule_type DNA !'##residues 1-389 ##label DRO !'##cross-references EMBL:X12816; NID:g48004; PIDN:CAA31304.1; !1PID:g48005 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing GENETICS !$#gene xylA COMPLEX homotetramer FUNCTION !$#description catalyzes isomerization of the aldopentose D-xylose to the !12-ketopentose D-xylulose !$#pathway xylose metabolism CLASSIFICATION #superfamily xylose isomerase KEYWORDS homotetramer; intramolecular oxidoreductase; isomerase; !1magnesium; xylose metabolism FEATURE !$2-389 #product xylose isomerase #status predicted #label !8MAT\ !$54,57 #active_site His, Asp #status predicted\ !$90,183 #binding_site substrate (Thr, Lys) #status predicted\ !$181,217,245,287 #binding_site magnesium (Glu, Glu, Asp, Asp) #status !8predicted\ !$217,220,255,257 #binding_site magnesium (Glu, His, Asp, Asp) #status !8predicted SUMMARY #length 389 #molecular-weight 43144 #checksum 6021 SEQUENCE /// ENTRY B41339 #type complete TITLE xylose isomerase (EC 5.3.1.5) [validated] - Streptomyces rubiginosus ORGANISM #formal_name Streptomyces rubiginosus DATE 28-May-1992 #sequence_revision 06-Dec-1996 #text_change 15-Sep-2000 ACCESSIONS B41339 REFERENCE A41339 !$#authors Wong, H.C.; Ting, Y.; Lin, H.C.; Reichert, F.; Myambo, K.; !1Watt, K.W.K.; Toy, P.L.; Drummond, R.J. !$#journal J. Bacteriol. (1991) 173:6849-6858 !$#title Genetic organization and regulation of the xylose !1degradation genes in Streptomyces rubiginosus. !$#cross-references MUID:92041569; PMID:1657868 !$#accession B41339 !'##molecule_type DNA !'##residues 1-388 ##label WON !'##cross-references GB:M73789; NID:g153532; PIDN:AAA26838.1; !1PID:g153534 !'##note parts of this sequence, including the amino and carboxyl ends !1of the mature protein, were determined by protein sequencing REFERENCE A50791 !$#authors Carrell, H.L.; Glusker, J.P. !$#submission submitted to the Brookhaven Protein Data Bank, October 1990 !$#cross-references PDB:7XIA !$#contents annotation; X-ray crystallography, 1.9 angstroms, residues !11-40,'Q',42-387 REFERENCE A50808 !$#authors Carrell, H.L.; Glusker, J.P. !$#submission submitted to the Brookhaven Protein Data Bank, October 1990 !$#cross-references PDB:8XIA !$#contents annotation; X-ray crystallography, 1.9 angstroms, with !1D-xylose, residues 1-40,'Q',42-387 REFERENCE A58422 !$#authors Carrell, H.L.; Glusker, J.P.; Burger, V.; Manfre, F.; !1Tritsch, D.; Biellmann, J.F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:4440-4444 !$#title X-ray analysis of D-xylose isomerase at 1.9 angstroms: !1native enzyme in complex with substrate and with a !1mechanism-designed inactivator. !$#cross-references MUID:89282788; PMID:2734296 !$#contents annotation; X-ray crystallography, 1.9 angstroms REFERENCE A50703 !$#authors Whitlow, M.; Howard, A.J. !$#submission submitted to the Brookhaven Protein Data Bank, March 1991 !$#cross-references PDB:4XIS !$#contents annotation; X-ray crystallography, 1.60 angstroms, with !1xylose and manganese, residues 2-387 REFERENCE A58421 !$#authors Whitlow, M.; Howard, A.J.; Finzel, B.C.; Poulos, T.L.; !1Winborne, E.; Gilliland, G.L. !$#journal Proteins (1991) 9:153-173 !$#title A metal-mediated hydride shift mechanism for xylose !1isomerase based on the 1.6 angstroms Streptomyces !1rubiginosus structures with xylitol and D-xylose. !$#cross-references MUID:91172741; PMID:2006134 !$#contents annotation; X-ray crystallography, 1.60 angstroms COMPLEX homotetramer FUNCTION !$#description catalyzes isomerization of the aldopentose D-xylose to the !12-ketopentose D-xylulose !$#pathway xylose metabolism CLASSIFICATION #superfamily xylose isomerase KEYWORDS homotetramer; intramolecular oxidoreductase; isomerase; !1magnesium; xylose metabolism FEATURE !$1-388 #product xylose isomerase #status experimental #label !8MAT\ !$54,57 #active_site His, Asp #status experimental\ !$90,183 #binding_site substrate (Thr, Lys) #status !8experimental\ !$181,217,245,287 #binding_site magnesium (Glu, Glu, Asp, Asp) #status !8experimental\ !$217,220,255,257 #binding_site magnesium (Glu, His, Asp, Asp) #status !8experimental SUMMARY #length 388 #molecular-weight 43227 #checksum 3522 SEQUENCE /// ENTRY S28986 #type complete TITLE xylose isomerase (EC 5.3.1.5) [validated] - Streptomyces olivochromogenes ORGANISM #formal_name Streptomyces olivochromogenes DATE 25-Feb-1994 #sequence_revision 06-Dec-1996 #text_change 15-Sep-2000 ACCESSIONS S28986 REFERENCE S28986 !$#authors Farber, G.K.; Glasfeld, A.; Tiraby, G.; Ringe, D.; Petsko, !1G.A. !$#journal Biochemistry (1989) 28:7289-7297 !$#title Crystallographic studies of the mechanism of xylose !1isomerase. !$#cross-references MUID:90057422; PMID:2510821 !$#contents X-ray crystallography, 3.0 angstroms !$#accession S28986 !'##molecule_type protein; DNA !'##residues 1-389 ##label FAR REFERENCE A50637 !$#authors Farber, G.; Petsko, G. !$#submission submitted to the Brookhaven Protein Data Bank, February 1989 !$#cross-references PDB:3XIA !$#contents annotation; X-ray crystallography, 3.0 angstroms, residues !12-378 COMPLEX homodimer FUNCTION !$#description catalyzes isomerization of the aldopentose D-xylose to the !12-ketopentose D-xylulose !$#pathway xylose metabolism CLASSIFICATION #superfamily xylose isomerase KEYWORDS homodimer; intramolecular oxidoreductase; isomerase; !1magnesium; xylose metabolism FEATURE !$2-389 #product xylose isomerase #status experimental #label !8MAT\ !$54,57 #active_site His, Asp #status experimental\ !$90,183 #binding_site substrate (Thr, Lys) #status !8experimental\ !$181,217,245,287 #binding_site magnesium (Glu, Glu, Asp, Asp) #status !8experimental\ !$217,220,255,257 #binding_site magnesium (Glu, His, Asp, Asp) #status !8experimental SUMMARY #length 389 #molecular-weight 43211 #checksum 9250 SEQUENCE /// ENTRY ISECMP #type complete TITLE mannose-6-phosphate isomerase (EC 5.3.1.8) - Escherichia coli (strain K-12) ALTERNATE_NAMES phosphohexomutase; phosphomannose isomerase ORGANISM #formal_name Escherichia coli DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 01-Mar-2002 ACCESSIONS A01172; G64917 REFERENCE A01172 !$#authors Miles, J.S.; Guest, J.R. !$#journal Gene (1984) 32:41-48 !$#title Nucleotide sequence and transcriptional start point of the !1phosphomannose isomerase gene (manA) of Escherichia coli. !$#cross-references MUID:85155484; PMID:6397402 !$#accession A01172 !'##molecule_type DNA !'##residues 1-391 ##label MIL !'##cross-references GB:M15380; NID:g146721; PIDN:AAA24109.1; !1PID:g146722 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64917 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-391 ##label BLAT !'##cross-references GB:AE000257; GB:U00096; NID:g1787898; !1PIDN:AAC74685.1; PID:g1787899; UWGP:b1613 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene manA !$#map_position 35.5 min FUNCTION !$#description catalyzes the interconversion of mannose-6-phosphate and !1fructose 6-phosphate; involved in the conversion of glucose !1to GDP-L-fucose, which can be converted to L-fucose, a !1capsular polysaccharid !$#note zinc cofactor CLASSIFICATION #superfamily mannose-6-phosphate isomerase KEYWORDS intramolecular oxidoreductase; isomerase; zinc SUMMARY #length 391 #molecular-weight 42850 #checksum 1776 SEQUENCE /// ENTRY B43304 #type complete TITLE phosphomannose isomerase-GDP-mannose pyrophosphorylase - Xanthomonas campestris ORGANISM #formal_name Xanthomonas campestris DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B43304 REFERENCE A43304 !$#authors Koplin, R.; Arnold, W.; Hotte, B.; Simon, R.; Wang, G.; !1Puhler, A. !$#journal J. Bacteriol. (1992) 174:191-199 !$#title Genetics of xanthan production in Xanthomonas campestris: !1the xanA and xanB genes are involved in UDP-glucose and !1GDP-mannose biosynthesis. !$#cross-references MUID:92104962; PMID:1370280 !$#accession B43304 !'##status preliminary !'##molecule_type DNA !'##residues 1-466 ##label KOP !'##cross-references GB:M83231; NID:g155394; PIDN:AAA27611.1; !1PID:g155396 !'##experimental_source pv. campestris !'##note sequence extracted from NCBI backbone (NCBIN:75324, !1NCBIP:75331) CLASSIFICATION #superfamily Helicobacter mannose-6-phosphate isomerase SUMMARY #length 466 #molecular-weight 50876 #checksum 817 SEQUENCE /// ENTRY H69386 #type complete TITLE mannose-6-phosphate isomerase/mannose-1-phosphate guanylyl transferase (manC) homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS H69386 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession H69386 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-448 ##label KLE !'##cross-references GB:AE001028; GB:AE000782; NID:g2689351; !1PIDN:AAB90149.1; PID:g2649495; TIGR:AF1097 CLASSIFICATION #superfamily Helicobacter mannose-6-phosphate isomerase SUMMARY #length 448 #molecular-weight 51089 #checksum 7194 SEQUENCE /// ENTRY C64525 #type complete TITLE mannose-6-phosphate isomerase - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C64525 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession C64525 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-470 ##label TOM !'##cross-references GB:AE000526; GB:AE000511; NID:g2313116; !1PIDN:AAD07111.1; PID:g2313118; TIGR:HP0043 CLASSIFICATION #superfamily Helicobacter mannose-6-phosphate isomerase SUMMARY #length 470 #molecular-weight 53371 #checksum 4090 SEQUENCE /// ENTRY NUMS #type complete TITLE glucose-6-phosphate isomerase (EC 5.3.1.9) - mouse ALTERNATE_NAMES neuroleukin; phosphoglucose isomerase; phosphohexose isomerase ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 24-Nov-1999 ACCESSIONS A24439; I49701 REFERENCE A24439 !$#authors Gurney, M.E.; Heinrich, S.P.; Lee, M.R.; Yin, H. !$#journal Science (1986) 234:566-574 !$#title Molecular cloning and expression of neuroleukin, a !1neurotrophic factor for spinal and sensory neurons. !$#cross-references MUID:87018838; PMID:3764429 !$#accession A24439 !'##molecule_type mRNA !'##residues 1-558 ##label GUR !'##cross-references GB:M14220; NID:g200064; PIDN:AAA39825.1; !1PID:g200065 !'##experimental_source salivary REFERENCE I49701 !$#authors Faik, P.; Walker, J.I.; Morgan, M.J. !$#journal Genomics (1994) 21:122-127 !$#title Identification of a novel tandemly repeated sequence present !1in an intron of the glucose phosphate isomerase (GPI) gene !1in mouse and man. !$#cross-references MUID:94375004; PMID:7545951 !$#accession I49701 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 269-558 ##label RES !'##cross-references GB:L09104; NID:g309267; PIDN:AAA65641.1; !1PID:g309268 COMMENT This protein, found in a wide variety of tissues, is a !1potent, pleiotrophic growth factor with multiple targets of !1activity. It promotes neuritic sprouting from motor neurons !1but not from sympathetic or parasympathetic neurons. COMMENT As a lymphokine produced by lectin-stimulated lymphocytes, !1neuroleukin stimulates polyclonal B-cell maturation to !1antibody production. CLASSIFICATION #superfamily glucose-6-phosphate isomerase KEYWORDS blocked amino end; gluconeogenesis; glycolysis; growth !1factor; homodimer; intramolecular oxidoreductase; isomerase; !1lymphokine; neurotrophic factor FEATURE !$2-558 #product glucose-6-phosphate isomerase #status !8predicted #label MAT\ !$2 #modified_site blocked amino end (Ala) (in mature !8form) #status experimental\ !$519 #active_site Lys #status predicted SUMMARY #length 558 #molecular-weight 62767 #checksum 9281 SEQUENCE /// ENTRY NUPG #type complete TITLE glucose-6-phosphate isomerase (EC 5.3.1.9) - pig ALTERNATE_NAMES neuroleukin; phosphoglucose isomerase; phosphohexose isomerase ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 02-Jun-2000 ACCESSIONS S00895; S13506; I46587 REFERENCE S00895 !$#authors Chaput, M.; Claes, V.; Portetelle, D.; Cludts, I.; Cravador, !1A.; Burny, A.; Gras, H.; Tartar, A. !$#journal Nature (1988) 332:454-455 !$#title The neurotrophic factor neuroleukin is 90% homologous with !1phosphohexose isomerase. !$#cross-references MUID:88175070; PMID:3352744 !$#accession S00895 !'##molecule_type mRNA !'##residues 1-558 ##label CHA !'##cross-references GB:X07382; NID:g2042; PIDN:CAA30295.1; PID:g2043 !'##note part of this sequence was confirmed by protein sequencing REFERENCE S13506 !$#authors Claes, V.; Taquet, A.N.; Kettmann, R.; Burny, A. !$#journal Biochim. Biophys. Acta (1990) 1087:339-340 !$#title Sequence analysis of the pig phosphoglucose isomerase gene !1promoter region. !$#cross-references MUID:91064390; PMID:2248981 !$#accession S13506 !'##molecule_type mRNA !'##residues 1-17 ##label CLA !'##cross-references EMBL:X53719; NID:g1848; PIDN:CAA37755.1; PID:g1849 REFERENCE I46587 !$#authors Davies, W.; Harbitz, I.; Hauge, J.G. !$#journal Anim. Genet. (1987) 18:233-240 !$#title A partial cDNA clone for porcine glucosephosphate isomerase: !1Isolation, characterization and use in detection of !1restriction fragment length polymorphims. !$#cross-references MUID:88021976; PMID:2889410 !$#accession I46587 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 238-343,'H',345-357 ##label DAV !'##cross-references GB:M54975; NID:g164481; PIDN:AAA31048.1; !1PID:g552364 COMMENT Neuroleukin promotes neuritic sprouting from motor neurons !1but not from sympathetic or parasympathetic neurons. COMMENT As a lymphokine produced by lectin-stimulated lymphocytes, !1neuroleukin stimulates polyclonal B-cell maturation to !1antibody production. GENETICS !$#gene PGI; gpi CLASSIFICATION #superfamily glucose-6-phosphate isomerase KEYWORDS blocked amino end; gluconeogenesis; glycolysis; growth !1factor; homodimer; intramolecular oxidoreductase; isomerase; !1lymphokine; neurotrophic factor FEATURE !$2-558 #product glucose-6-phosphate isomerase #status !8predicted #label MAT\ !$2 #modified_site blocked amino end (Ala) (in mature !8form) #status experimental\ !$519 #active_site Lys #status predicted SUMMARY #length 558 #molecular-weight 63126 #checksum 627 SEQUENCE /// ENTRY NUEC #type complete TITLE glucose-6-phosphate isomerase (EC 5.3.1.9) - Escherichia coli (strain K-12) ALTERNATE_NAMES phosphoglucose isomerase; phosphohexose isomerase ORGANISM #formal_name Escherichia coli DATE 31-Mar-1990 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS H65209; JS0142; S04396 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65209 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-549 ##label BLAT !'##cross-references GB:AE000476; GB:U00096; NID:g1790456; !1PIDN:AAC76995.1; PID:g1790457; UWGP:b4025 !'##experimental_source strain K-12, substrain MG1655 REFERENCE JS0142 !$#authors Froman, B.E.; Tait, R.C.; Gottlieb, L.D. !$#journal Mol. Gen. Genet. (1989) 217:126-131 !$#title Isolation and characterization of the phosphoglucose !1isomerase gene from Escherichia coli. !$#cross-references MUID:89364675; PMID:2549364 !$#accession JS0142 !'##molecule_type DNA !'##residues 1-316,'V',318-549 ##label FRO !'##cross-references GB:X15196; NID:g42376; PIDN:CAA33268.1; PID:g42377 !'##experimental_source strain JM101 !'##note the authors translated the codon CAG for residue 8 as Trp COMMENT This enzyme catalyzes the reversible isomerization of !1glucose-6-phosphate and fructose-6-phosphate. It is located !1primarily in the cytoplasm. GENETICS !$#gene pgi !$#map_position 91 min CLASSIFICATION #superfamily glucose-6-phosphate isomerase KEYWORDS glycolysis; homodimer; intramolecular oxidoreductase; !1isomerase FEATURE !$514 #active_site Lys #status predicted SUMMARY #length 549 #molecular-weight 61529 #checksum 3760 SEQUENCE /// ENTRY NUUTB #type complete TITLE glucose-6-phosphate isomerase (EC 5.3.1.9) - Trypanosoma brucei ALTERNATE_NAMES phosphoglucose isomerase; phosphohexose isomerase ORGANISM #formal_name Trypanosoma brucei DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 18-Jun-1999 ACCESSIONS S06113 REFERENCE S06113 !$#authors Marchand, M.; Kooystra, U.; Wierenga, R.K.; Lambeir, A.M.; !1van Beeumen, J.; Opperdoes, F.R.; Michels, P.A.M. !$#journal Eur. J. Biochem. (1989) 184:455-464 !$#title Glucosephosphate isomerase from Trypanosoma brucei. Cloning !1and characterization of the gene and analysis of the enzyme. !$#cross-references MUID:90005496; PMID:2792108 !$#accession S06113 !'##molecule_type DNA !'##residues 1-607 ##label MAR !'##cross-references GB:X15540; NID:g10486; PIDN:CAA33547.1; PID:g10487 !'##note part of this sequence was confirmed by protein sequencing CLASSIFICATION #superfamily glucose-6-phosphate isomerase KEYWORDS gluconeogenesis; glycolysis; homodimer; intramolecular !1oxidoreductase; isomerase FEATURE !$571 #active_site Lys #status predicted SUMMARY #length 607 #molecular-weight 67517 #checksum 4076 SEQUENCE /// ENTRY NUBY #type complete TITLE glucose-6-phosphate isomerase (EC 5.3.1.9) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES phosphoglucose isomerase; phosphohexose isomerase; protein YBR1407; protein YBR196c ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 21-Jul-2000 ACCESSIONS JT0484; A40073; S34021; S45445; S46068 REFERENCE JT0484 !$#authors Tekamp-Olson, P.; Najarian, R.; Burke, R.L. !$#journal Gene (1988) 73:153-161 !$#title The isolation, characterization and nucleotide sequence of !1the phosphoglucoisomerase gene of Saccharomyces cerevisiae. !$#cross-references MUID:89211945; PMID:3072254 !$#accession JT0484 !'##molecule_type DNA !'##residues 1-554 ##label TEK !'##cross-references GB:M21696; NID:g172224; PIDN:AAA34894.1; !1PID:g172225 REFERENCE A40073 !$#authors Green, J.B.A.; Wright, A.P.H.; Cheung, W.Y.; Lancashire, !1W.E.; Hartley, B.S. !$#journal Mol. Gen. Genet. (1988) 215:100-106 !$#title The structure and regulation of phosphoglucose isomerase in !1Saccharomyces cerevisiae. !$#cross-references MUID:89201230; PMID:3071735 !$#accession A40073 !'##molecule_type DNA !'##residues 1-554 ##label GRE !'##cross-references GB:M37267; NID:g172141; PIDN:AAA34862.1; !1PID:g172142 REFERENCE S33966 !$#authors Demolis, N.; Mallet, L.; Bussereau, F.; Jacquet, M. !$#journal Yeast (1993) 9:645-659 !$#title RIM2, MSI1 and PGI1 are located within an 8 kb segment of !1Saccharomyces cerevisiae chromosome II, which also contains !1the putative ribosomal gene L21 and a new putative essential !1gene with a leucine zipper motif. !$#cross-references MUID:93348777; PMID:8346681 !$#accession S34021 !'##status translation not shown !'##molecule_type DNA !'##residues 1-554 ##label DEM !'##cross-references EMBL:Z21487; NID:g311665; PIDN:CAA79683.1; !1PID:g311672 REFERENCE S45445 !$#authors Mallet, L.; Bussereau, F.; Jacquet, M. !$#journal Yeast (1994) 10:819-831 !$#title Nucleotide sequence analysis of an 11.7 kb fragment of yeast !1chromosome II including BEM1, a new gene of the WD-40 repeat !1family and a new member of the KRE2/MNT1 family. !$#cross-references MUID:95066384; PMID:7975899 !$#accession S45445 !'##status translation not shown !'##molecule_type DNA !'##residues 1-554 ##label MAL !'##cross-references EMBL:Z21487; NID:g311665; PIDN:CAA79683.1; !1PID:g311672 REFERENCE S46054 !$#authors Bussereau, F.; Demolis, N.; Jacquet, M.; Mallet, L. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S46068 !'##molecule_type DNA !'##residues 1-554 ##label BUS !'##cross-references EMBL:Z36065; NID:g536564; PIDN:CAA85158.1; !1PID:g536565; GSPDB:GN00002; MIPS:YBR196c COMMENT This enzyme catalyzes the interconversion of !1glucose-6-phosphate and fructose-6-phosphate. GENETICS !$#gene SGD:PGI1; MIPS:YBR196c !'##cross-references SGD:S0000400; MIPS:YBR196c !$#map_position 2R CLASSIFICATION #superfamily glucose-6-phosphate isomerase KEYWORDS gluconeogenesis; glycolysis; homodimer; intramolecular !1oxidoreductase; isomerase FEATURE !$520 #active_site Lys #status predicted SUMMARY #length 554 #molecular-weight 61299 #checksum 5475 SEQUENCE /// ENTRY NUVKL #type complete TITLE glucose-6-phosphate isomerase (EC 5.3.1.9) - yeast (Kluyveromyces marxianus var. lactis) ALTERNATE_NAMES phosphoglucose isomerase; phosphohexose isomerase ORGANISM #formal_name Kluyveromyces marxianus var. lactis, Candida sphaerica DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 18-Jun-1999 ACCESSIONS S01414 REFERENCE S01414 !$#authors Wesolowski-Louvel, M.; Goffrini, P.; Ferrero, I. !$#journal Nucleic Acids Res. (1988) 16:8714 !$#title The RAG2 gene of the yeast Kluyveromyces lactis codes for a !1putative phosphoglucose isomerase. !$#cross-references MUID:88335624; PMID:3419932 !$#accession S01414 !'##status translation not shown !'##molecule_type DNA !'##residues 1-557 ##label WES !'##cross-references EMBL:X12360; NID:g2892; PIDN:CAA30923.1; PID:g2893 GENETICS !$#gene RAG2 CLASSIFICATION #superfamily glucose-6-phosphate isomerase KEYWORDS gluconeogenesis; glycolysis; homodimer; intramolecular !1oxidoreductase; isomerase FEATURE !$523 #active_site Lys #status predicted SUMMARY #length 557 #molecular-weight 61979 #checksum 3481 SEQUENCE /// ENTRY NUBSSA #type complete TITLE glucose-6-phosphate isomerase (EC 5.3.1.9) A [validated] - Bacillus stearothermophilus ALTERNATE_NAMES phosphoglucose isomerase; phosphohexose isomerase ORGANISM #formal_name Bacillus stearothermophilus DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 08-Sep-2000 ACCESSIONS S15936; S06196 REFERENCE S15936 !$#authors Tao, W.; Wang, L.; Shen, R.; Sheng, Z. !$#journal Nucleic Acids Res. (1989) 17:10107-10108 !$#title Complete nucleotide sequences of two phosphoglucoisomerase !1isozymes from Bacillus stearothermophilus. !$#cross-references MUID:90098783; PMID:2532320 !$#accession S15936 !'##status preliminary !'##molecule_type DNA !'##residues 1-449 ##label TAO !'##cross-references EMBL:X16639; NID:g40045; PIDN:CAA34634.1; !1PID:g40046 !'##note submitted to the EMBL Data Library, September 1989 GENETICS !$#gene pgiA COMPLEX homodimer FUNCTION !$#description EC 5.3.1.9 [validated, MUID:98080558]; catalyzes the !1interconversion of glucose-6-phosphate and !1fructose-6-phosphate !$#pathway glycolysis !$#note has cell motility stimulating activity on mouse colon cancer !1cells like endogenous autocrine motility factor (AMF); !1enhance neurite outgrowth on neuronal progenitor cells like !1neuroleukin (NLK) [validated, MUID:99254054] CLASSIFICATION #superfamily glucose-6-phosphate isomerase KEYWORDS glycolysis; homodimer; intramolecular oxidoreductase; !1isomerase FEATURE !$311 #active_site His #status experimental SUMMARY #length 449 #molecular-weight 50337 #checksum 2081 SEQUENCE /// ENTRY NUBSS #type complete TITLE glucose-6-phosphate isomerase (EC 5.3.1.9) B [validated] - Bacillus stearothermophilus ALTERNATE_NAMES phosphoglucose isomerase; phosphohexose isomerase ORGANISM #formal_name Bacillus stearothermophilus DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 18-Aug-2000 ACCESSIONS S06198; S15937 REFERENCE S06196 !$#authors Tao, W.; Wang, L.; Shen, R.; Sheng, Z. !$#submission submitted to the EMBL Data Library, September 1989 !$#accession S06198 !'##molecule_type DNA !'##residues 1-445 ##label TAO1 !'##cross-references EMBL:X16640; NID:g40047; PIDN:CAA34635.1; !1PID:g40048 REFERENCE S15936 !$#authors Tao, W.; Wang, L.; Shen, R.; Sheng, Z. !$#journal Nucleic Acids Res. (1989) 17:10107-10108 !$#title Complete nucleotide sequences of two phosphoglucoisomerase !1isozymes from Bacillus stearothermophilus. !$#cross-references MUID:90098783; PMID:2532320 !$#accession S15937 !'##molecule_type DNA !'##residues 1-317,'D',319-445 ##label TAO2 !'##cross-references EMBL:X16640; NID:g40047 GENETICS !$#gene pgiB COMPLEX homodimer FUNCTION !$#description EC 5.3.1.9 [validated, MUID:98080558]; catalyzes the !1interconversion of glucose-6-phosphate and !1fructose-6-phosphate !$#pathway glycolysis !$#note has cell motility stimulating activity on mouse colon cancer !1cells like endogenous autocrine motility factor (AMF); !1enhance neurite outgrowth on neuronal progenitor cells like !1neuroleukin (NLK) [validated, MUID:99254054] CLASSIFICATION #superfamily glucose-6-phosphate isomerase KEYWORDS glycolysis; homodimer; intramolecular oxidoreductase; !1isomerase FEATURE !$420 #active_site Lys #status predicted SUMMARY #length 445 #molecular-weight 50141 #checksum 8385 SEQUENCE /// ENTRY NUZQF #type complete TITLE glucose-6-phosphate isomerase (EC 5.3.1.9) - malaria parasite (Plasmodium falciparum) ORGANISM #formal_name Plasmodium falciparum DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 09-Jun-2000 ACCESSIONS A36567 REFERENCE A36567 !$#authors Kaslow, D.C.; Hill, S. !$#journal J. Biol. Chem. (1990) 265:12337-12341 !$#title Cloning metabolic pathway genes by complementation in !1Escherichia coli. Isolation and expression of Plasmodium !1falciparum glucose phosphate isomerase. !$#cross-references MUID:90324218; PMID:2197273 !$#accession A36567 !'##molecule_type DNA !'##residues 1-591 ##label KAS !'##cross-references GB:J05544; NID:g160309; PIDN:AAA29610.1; !1PID:g160310 CLASSIFICATION #superfamily glucose-6-phosphate isomerase KEYWORDS gluconeogenesis; glycolysis; homodimer; intramolecular !1oxidoreductase; isomerase FEATURE !$540 #active_site Lys #status predicted SUMMARY #length 591 #molecular-weight 68766 #checksum 9231 SEQUENCE /// ENTRY MUECNG #type complete TITLE glucosamine-6-phosphate deaminase (EC 3.5.99.6) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 08-Sep-2002 ACCESSIONS A29895; E64802; B37018 REFERENCE A91590 !$#authors Rogers, M.J.; Ohgi, T.; Plumbridge, J.; Soell, D. !$#journal Gene (1988) 62:197-207 !$#title Nucleotide sequences of the Escherichia coli nagE and nagB !1genes: the structural genes for the N-acetylglucosamine !1transport protein of the bacterial phosphoenolpyruvate:sugar !1phosphotransferase system and for glucosamine-6-phosphate !1deaminase. !$#cross-references MUID:88212176; PMID:3284790 !$#accession A29895 !'##molecule_type DNA !'##residues 1-266 ##label ROG !'##cross-references GB:M19284; GB:M17907; GB:M21684; NID:g146911; !1PIDN:AAA24191.1; PID:g455176 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64802 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-266 ##label BLAT !'##cross-references GB:AE000171; GB:U00096; NID:g1786888; !1PIDN:AAC73772.1; PID:g1786893; UWGP:b0678 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A37018 !$#authors Peri, K.G.; Goldie, H.; Waygood, E.B. !$#journal Biochem. Cell Biol. (1990) 68:123-137 !$#title Cloning and characterization of the N-acetylglucosamine !1operon of Escherichia coli. !$#cross-references MUID:90274974; PMID:2190615 !$#accession B37018 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-71,'M',72-90,92-266 ##label PER !'##cross-references GB:AF052007; NID:g3005593; PIDN:AAC09324.1; !1PID:g3005594 GENETICS !$#gene nagB !$#map_position 16 min CLASSIFICATION #superfamily glucosamine-6-phosphate isomerase KEYWORDS hydrolase; intramolecular oxidoreductase; isomerase SUMMARY #length 266 #molecular-weight 29774 #checksum 8277 SEQUENCE /// ENTRY ISECIC #type complete TITLE 1-(5-phosphoribosyl)-5-[ (5-phosphoribosylamino)methylideneamino)imidazole-4-carboxam ide isomerase (EC 5.3.1.16) [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES compound III isomerase; hisA protein ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 05-Dec-1997 #text_change 03-Jun-2002 ACCESSIONS G64967; JS0133 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64967 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-246 ##label BLAT !'##cross-references GB:AE000293; GB:U00096; NID:g2367127; !1PIDN:AAC75085.1; PID:g1788335; UWGP:b2024 !'##experimental_source strain K-12, substrain MG1655 REFERENCE JS0131 !$#authors Carlomagno, M.S.; Chiariotti, L.; Alifano, P.; Nappo, A.G.; !1Bruni, C.B. !$#journal J. Mol. Biol. (1988) 203:585-606 !$#title Structure and function of the Salmonella typhimurium and !1Escherichia coli K-12 histidine operons. !$#cross-references MUID:89094829; PMID:3062174 !$#accession JS0133 !'##molecule_type DNA !'##residues 2-84,'T',86-126,'V',128-246 ##label CAR !'##cross-references GB:X13462; NID:g41706; PIDN:CAA31816.1; PID:g41713 !'##experimental_source strain K12 GENETICS !$#gene hisA !$#map_position 44 min FUNCTION !$#description EC 5.3.1.16 [validated, MUID:94300623]; catalyzes the ketol !1isomerization of an intermediate in the second step of the !1histidine biosynthetic pathway !$#pathway histidine biosynthesis !$#note important for the synthesis of the imidazole ring CLASSIFICATION #superfamily N-(5'-phospho-D-ribosylformimino)-5-amino-1- !1(5''-phosphoribosyl)-4-imidazolecarboxamide isomerase KEYWORDS histidine biosynthesis; intramolecular oxidoreductase; !1isomerase SUMMARY #length 246 #molecular-weight 26164 #checksum 7859 SEQUENCE /// ENTRY ISEBIC #type complete TITLE 1-(5-phosphoribosyl)-5-[ (5-phosphoribosylamino)methylideneamino)imidazole-4-carboxam ide isomerase (EC 5.3.1.16) - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 03-Jun-2002 ACCESSIONS JS0161 REFERENCE JS0131 !$#authors Carlomagno, M.S.; Chiariotti, L.; Alifano, P.; Nappo, A.G.; !1Bruni, C.B. !$#journal J. Mol. Biol. (1988) 203:585-606 !$#title Structure and function of the Salmonella typhimurium and !1Escherichia coli K-12 histidine operons. !$#cross-references MUID:89094829; PMID:3062174 !$#accession JS0161 !'##molecule_type DNA !'##residues 1-246 ##label CAR !'##cross-references GB:X13464; NID:g47719; PIDN:CAA31827.1; PID:g47726 COMMENT This enzyme catalyzes the ketol isomerization of an !1intermediate in the second step of the histidine !1biosynthetic pathway; it is important for the synthesis of !1the imidazole ring. GENETICS !$#gene hisA !$#map_position 42 min CLASSIFICATION #superfamily N-(5'-phospho-D-ribosylformimino)-5-amino-1- !1(5''-phosphoribosyl)-4-imidazolecarboxamide isomerase KEYWORDS histidine biosynthesis; intramolecular oxidoreductase; !1isomerase SUMMARY #length 246 #molecular-weight 26199 #checksum 8245 SEQUENCE /// ENTRY H64070 #type complete TITLE 1-(5-phosphoribosyl)-5-[ (5-phosphoribosylamino)methylideneamino)imidazole-4-carboxam ide isomerase (EC 5.3.1.16) - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS H64070 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession H64070 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-249 ##label TIGR !'##cross-references GB:U32730; GB:L42023; NID:g3212191; !1PIDN:AAC22132.1; PID:g1573452; TIGR:HI0473 CLASSIFICATION #superfamily N-(5'-phospho-D-ribosylformimino)-5-amino-1- !1(5''-phosphoribosyl)-4-imidazolecarboxamide isomerase KEYWORDS histidine biosynthesis; intramolecular oxidoreductase; !1isomerase SUMMARY #length 249 #molecular-weight 26861 #checksum 3730 SEQUENCE /// ENTRY SIPSDT #type complete TITLE steroid Delta-isomerase (EC 5.3.3.1) - Comamonas testosteroni ALTERNATE_NAMES delta 5-3-ketosteroid isomerase; Delta-5->4-3-oxosteroid isomerase ORGANISM #formal_name Comamonas testosteroni DATE 24-Apr-1984 #sequence_revision 30-Jun-1992 #text_change 18-Jun-1999 ACCESSIONS JT0336; A39944; A01173 REFERENCE JT0336 !$#authors Choi, K.Y.; Benisek, W.F. !$#journal Gene (1988) 69:121-129 !$#title Nucleotide sequence of the gene for the delta !15-3-ketosteroid isomerase of Pseudomonas testosteroni. !$#cross-references MUID:89137982; PMID:3224818 !$#accession JT0336 !'##molecule_type DNA !'##residues 1-125 ##label CHO !'##cross-references GB:M22749; NID:g151321; PIDN:AAA25872.1; !1PID:g151322 REFERENCE A39944 !$#authors Kuliopulos, A.; Shortle, D.; Talalay, P. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:8893-8897 !$#title Isolation and sequencing of the gene encoding delta !1(5)-3-ketosteroid isomerase of Pseudomonas testosteroni: !1overexpression of the protein. !$#cross-references MUID:88097394; PMID:3480517 !$#accession A39944 !'##molecule_type DNA !'##residues 1-125 ##label KUL !'##cross-references GB:J03568; NID:g151319; PIDN:AAA25871.1; !1PID:g151320 !'##experimental_source ATCC 11996 REFERENCE A92096 !$#authors Benson, A.M.; Jarabak, R.; Talalay, P. !$#journal J. Biol. Chem. (1971) 246:7514-7525 !$#title The amino acid sequence of Delta-5-3-ketosteroid isomerase !1of Pseudomonas testosteroni. !$#cross-references MUID:72085988; PMID:5135313 !$#accession A01173 !'##molecule_type protein !'##residues 1-21,'N',23,'N',25-32,'N',34-37,'N',39-76,'Q',78-125 !1##label BEN REFERENCE A91403 !$#authors Weintraub, H.; Vincent, F.; Baulieu, E.E.; Alfsen, A. !$#journal FEBS Lett. (1973) 37:82-88 !$#title Molecular weight determination and structural studies of !1Pseudomonas testosteroni Delta-5->4-3-oxosteroid isomerase !1(EC 5.3.3.1). !$#cross-references MUID:74032505; PMID:4753764 !$#contents annotation COMMENT This steroid-induced enzyme catalyzes the conversion of !1delta-5(6) and of delta-5(10) 3-ketosteroids to the !1corresponding delta-4 3-ketosteroids. GENETICS !$#gene ksi CLASSIFICATION #superfamily steroid Delta-isomerase KEYWORDS homodimer; intramolecular oxidoreductase; isomerase FEATURE !$38 #active_site Asp #status experimental SUMMARY #length 125 #molecular-weight 13398 #checksum 3642 SEQUENCE /// ENTRY SIPSDP #type complete TITLE steroid Delta-isomerase (EC 5.3.3.1) - Pseudomonas putida ORGANISM #formal_name Pseudomonas putida DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 30-Jun-1993 ACCESSIONS A25216 REFERENCE A25216 !$#authors Linden, K.G.; Benisek, W.F. !$#journal J. Biol. Chem. (1986) 261:6454-6460 !$#title The amino acid sequence of a delta-3-oxosteroid isomerase !1from Pseudomonas putida biotype B. !$#cross-references MUID:86196068; PMID:3700400 !$#accession A25216 !'##molecule_type protein !'##residues 1-131 ##label LIN CLASSIFICATION #superfamily steroid Delta-isomerase KEYWORDS homodimer; intramolecular oxidoreductase; isomerase FEATURE !$40 #active_site Asp #status predicted SUMMARY #length 131 #molecular-weight 14535 #checksum 460 SEQUENCE /// ENTRY ISPSMP #type complete TITLE muconolactone Delta-isomerase (EC 5.3.3.4) - Pseudomonas putida ORGANISM #formal_name Pseudomonas putida DATE 30-Apr-1982 #sequence_revision 06-Jan-1995 #text_change 18-Jun-1999 ACCESSIONS B28630; A01174; A61585 REFERENCE A28630 !$#authors Aldrich, T.L.; Chakrabarty, A.M. !$#journal J. Bacteriol. (1988) 170:1297-1304 !$#title Transcriptional regulation, nucleotide sequence, and !1localization of the promoter of the catBC operon in !1Pseudomonas putida. !$#cross-references MUID:88139192; PMID:2449420 !$#accession B28630 !'##molecule_type DNA !'##residues 1-97 ##label ALD !'##cross-references EMBL:M19460; NID:g151124; PIDN:AAA25767.1; !1PID:g151126 REFERENCE A01174 !$#authors McCorkle, G.M.; Yeh, W.K.; Fletcher, P.; Ornston, L.N. !$#journal J. Biol. Chem. (1980) 255:6335-6341 !$#title Repetitions in the NH-2-terminal amino acid sequence of !1beta-ketoadipate enol-lactone hydrolase from Pseudomonas !1putida. !$#cross-references MUID:80227763; PMID:7391022 !$#accession A01174 !'##molecule_type protein !'##residues 1-20,'TQ',23-47,49-51 ##label MCC REFERENCE A61585 !$#authors Meagher, R.B. !$#journal Biochim. Biophys. Acta (1977) 494:33-47 !$#title Purification and partial amino acid sequence of the cyanogen !1bromide fragments of muconolactone isomerase from !1Pseudomonas putida. !$#cross-references MUID:78000419; PMID:901811 !$#accession A61585 !'##molecule_type protein !'##residues 1-7,'B',9,'H',11,'VLV';'B',17,'IL',20,'TZ',23;'B',80,'Z', !182,'B',84-92,'B',94,'BRH' ##label MEA CLASSIFICATION #superfamily muconolactone Delta-isomerase KEYWORDS homotrimer; intramolecular oxidoreductase; isomerase SUMMARY #length 97 #molecular-weight 11213 #checksum 8955 SEQUENCE /// ENTRY A30007 #type complete TITLE dolichyl-diphosphooligosaccharide-protein glycotransferase (EC 2.4.1.119) glycosylation site-binding chain precursor - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 15-Dec-1988 #sequence_revision 26-May-1994 #text_change 03-Jun-2002 ACCESSIONS A30007 REFERENCE A30007 !$#authors Geetha-Habib, M.; Noiva, R.; Kaplan, H.A.; Lennarz, W.J. !$#journal Cell (1988) 54:1053-1060 !$#title Glycosylation site binding protein, a component of !1oligosaccharyl transferase, is highly similar to three other !157 kd luminal proteins of the ER. !$#cross-references MUID:88327849; PMID:2458190 !$#accession A30007 !'##molecule_type mRNA !'##residues 1-508 ##label GEE !'##cross-references EMBL:M22594 CLASSIFICATION #superfamily protein disulfide-isomerase; thioredoxin !1homology KEYWORDS duplication; endoplasmic reticulum; glycosyltransferase; !1hexosyltransferase; redox-active disulfide FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-508 #product dolichyl-diphosphooligosaccharide-protein !8glycotransferase glycosylation site-binding chain !8#status predicted #label MAT\ !$31-118 #domain thioredoxin homology #label TX1\ !$376-461 #domain thioredoxin homology #label TX2\ !$505-508 #region endoplasmic reticulum retention signal\ !$52-55,398-401 #disulfide_bonds redox-active #status predicted\ !$312-343 #disulfide_bonds #status predicted SUMMARY #length 508 #molecular-weight 56965 #checksum 1838 SEQUENCE /// ENTRY ISRTSS #type complete TITLE protein disulfide-isomerase (EC 5.3.4.1) precursor [validated] - rat ALTERNATE_NAMES cellular thyroid hormone-binding protein; diiodothyronine 5'-deiodinase; endoplasmic reticulum protein ERp59; iodothyronine 5'-monodeiodinase; procollagen-proline, 2-oxoglutarate 4-dioxygenase (EC 1.14.11.2) beta chain; prolyl-4 hydroxylase beta chain; S-S rearrangase; thyroxine deiodinase (EC 3.8.1.4) CONTAINS cellular thyroid hormone-binding protein; procollagen-proline dioxygenase (EC 1.14.11.2) beta chain; protein disulfide-isomerase (EC 5.3.4.1); thyroxine deiodinase (EC 3.8.1.4) ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 18-Aug-2000 ACCESSIONS A24595; A48756; A31118; S06419; S39371 REFERENCE A24595 !$#authors Edman, J.C.; Ellis, L.; Blacher, R.W.; Roth, R.A.; Rutter, !1W.J. !$#journal Nature (1985) 317:267-270 !$#title Sequence of protein disulphide isomerase and implications of !1its relationship to thioredoxin. !$#cross-references MUID:86014354; PMID:3840230 !$#accession A24595 !'##molecule_type mRNA !'##residues 1-508 ##label EDM !'##cross-references GB:X02918; NID:g56871; PIDN:CAA26675.1; PID:g56872 REFERENCE A48756 !$#authors Noiva, R.; Freedman, R.B.; Lennarz, W.J. !$#journal J. Biol. Chem. (1993) 268:19210-19217 !$#title Peptide binding to protein disulfide isomerase occurs at a !1site distinct from the active sites. !$#cross-references MUID:93374897; PMID:8366073 !$#accession A48756 !'##molecule_type protein !'##residues 470-493 ##label NOI REFERENCE A31118 !$#authors Boado, R.J.; Campbell, D.A.; Chopra, I.J. !$#journal Biochem. Biophys. Res. Commun. (1988) 155:1297-1304 !$#title Nucleotide sequence of rat liver iodothyronine !15'-monodeiodinase (5'MD): its identity with the protein !1disulfide isomerase. !$#cross-references MUID:89025800; PMID:3178809 !$#accession A31118 !'##molecule_type mRNA !'##residues 28-38,'AL',40-508 ##label BOA !'##cross-references GB:M21018; NID:g202548; PIDN:AAA40620.1; !1PID:g202549 REFERENCE S06419 !$#authors Boado, R.J.; Chopra, I.J.; Flink, I.L.; Campbell, D.A. !$#journal Endocrinology (1988) 123:1264-1273 !$#title Enzyme binding-inhibiting assay for iodothyronine !15'-monodeiodinase (5'-MD) and its application to isolation !1of complementary deoxyribonucleic acid clones for the 5'-MD !1in rat liver. !$#cross-references MUID:88296303; PMID:2841089 !$#accession S06419 !'##molecule_type mRNA !'##residues 128-393 ##label BO2 !'##cross-references EMBL:M21476; NID:g202546; PIDN:AAA40619.1; !1PID:g202547 REFERENCE S39371 !$#authors Yokoi, T.; Nagayama, S.; Kajiwara, R.; Kawaguchi, Y.; !1Horiuchi, R.; Kamataki, T. !$#journal Biochim. Biophys. Acta (1993) 1158:339-344 !$#title Identification of protein disulfide isomerase and !1calreticulin as autoimmune antigens in LEC strain of rats. !$#cross-references MUID:94072621; PMID:8251535 !$#accession S39371 !'##molecule_type protein !'##residues 20-24,'X',26-34 ##label YOK COMMENT This enzyme catalyzes the rearrangement of both intrachain !1and interchain disulfide bonds in proteins to form the !1native structures. COMPLEX homodimer CLASSIFICATION #superfamily protein disulfide-isomerase; thioredoxin !1homology KEYWORDS ascorbic acid; duplication; endoplasmic reticulum; !1homodimer; intramolecular oxidoreductase; isomerase; !1redox-active disulfide FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-508 #product protein disulfide-isomerase #status !8experimental #label MAT\ !$34-120 #domain thioredoxin homology #label TX1\ !$376-461 #domain thioredoxin homology #label TX2\ !$470-508 #domain peptide binding #status experimental #label !8PEPB\ !$505-508 #region endoplasmic reticulum retention signal\ !$54-57,398-401 #disulfide_bonds redox-active #status predicted\ !$313-344 #disulfide_bonds #status predicted SUMMARY #length 508 #molecular-weight 56864 #checksum 1805 SEQUENCE /// ENTRY ISMSSS #type complete TITLE protein disulfide-isomerase (EC 5.3.4.1) precursor - mouse ALTERNATE_NAMES cellular thyroid hormone-binding protein; endoplasmic reticulum protein ERp59; iodothyronine 5'-monodeiodinase; prolyl-4 hydroxylase beta chain CONTAINS procollagen-proline dioxygenase (EC 1.14.11.2) beta chain; thyroxine deiodinase (EC 3.8.1.4) ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 06-Oct-2000 ACCESSIONS A34930; S01634; S50102 REFERENCE A34930 !$#authors Mazzarella, R.A.; Srinivasan, M.; Haugejorden, S.M.; Green, !1M. !$#journal J. Biol. Chem. (1990) 265:1094-1101 !$#title ERp72, an abundant luminal endoplasmic reticulum protein, !1contains three copies of the active site sequences of !1protein disulfide isomerase. !$#cross-references MUID:90110091; PMID:2295602 !$#accession A34930 !'##molecule_type mRNA !'##residues 1-509 ##label MAZ !'##cross-references GB:J05185; NID:g200280; PIDN:AAA39906.1; !1PID:g387509 REFERENCE S01634 !$#authors Gong, Q.; Fukuda, T.; Parkison, C.; Cheng, S. !$#journal Nucleic Acids Res. (1988) 16:1203 !$#title Nucleotide sequence of a full-length cDNA clone encoding a !1mouse cellular thyroid hormone binding protein (p55) that is !1homologous to protein disulfide isomerase and the !1beta-subunit of prolyl-4-hydroxylase. !$#cross-references MUID:88143996; PMID:2830592 !$#accession S01634 !'##molecule_type mRNA !'##residues 1-67,'R',69-509 ##label GON !'##cross-references EMBL:X06453; NID:g54776; PIDN:CAA29759.1; !1PID:g54777 REFERENCE S50102 !$#authors Caubin, J.; Iglesias, T.; Bernal, J.; Munoz, A.; Marquez, !1G.; Barbero, J.L.; Zaballos, A. !$#journal Nucleic Acids Res. (1994) 22:4132-4138 !$#title Isolation of genomic DNA fragments corresponding to genes !1modulated in vivo by a transcription factor. !$#cross-references MUID:95023181; PMID:7937138 !$#accession S50102 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 418-455 ##label CAU !'##cross-references EMBL:Z32539 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1March 1994 COMMENT This enzyme catalyzes the rearrangement of both intrachain !1and interchain disulfide bonds in proteins to form the !1native structures. CLASSIFICATION #superfamily protein disulfide-isomerase; thioredoxin !1homology KEYWORDS ascorbic acid; duplication; endoplasmic reticulum; !1homodimer; intramolecular oxidoreductase; isomerase; !1multifunctional enzyme; redox-active disulfide FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-509 #product protein disulfide-isomerase #status !8predicted #label MAT\ !$34-121 #domain thioredoxin homology #label TX1\ !$377-462 #domain thioredoxin homology #label TX2\ !$506-509 #region endoplasmic reticulum retention signal\ !$55-58,399-402 #disulfide_bonds redox-active #status predicted\ !$314-345 #disulfide_bonds #status predicted SUMMARY #length 509 #molecular-weight 57058 #checksum 6745 SEQUENCE /// ENTRY ISHUSS #type complete TITLE protein disulfide-isomerase (EC 5.3.4.1) precursor - human ALTERNATE_NAMES cellular thyroid hormone-binding protein; endoplasmic reticulum protein ERp59; iodothyronine 5'-monodeiodinase; procollagen-proline,2-oxoglutarate 4-dioxygenase beta chain; proline hydroxylase; proline,2-oxoglutarate 4-dioxygenase; prolyl 4-hydroxylase beta chain; protocollagen hydroxylase CONTAINS procollagen-proline dioxygenase (EC 1.14.11.2) beta chain; thyroxine deiodinase (EC 3.8.1.4) ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1992 #sequence_revision 17-Nov-1995 #text_change 19-May-2000 ACCESSIONS A31913; B31913; A30055; A29787; A26632; A42791; I33178; !1F61002 REFERENCE A31913 !$#authors Tasanen, K.; Parkkonen, T.; Chow, L.T.; Kivirikko, K.I.; !1Pihlajaniemi, T. !$#journal J. Biol. Chem. (1988) 263:16218-16224 !$#title Characterization of the human gene for a polypeptide that !1acts both as the beta-subunit of prolyl 4-hydroxylase and as !1protein disulfide isomerase. !$#cross-references MUID:89034087; PMID:2846539 !$#accession A31913 !'##molecule_type DNA !'##residues 1-118;209-508 ##label TAS !$#accession B31913 !'##molecule_type DNA !'##residues 1-508 ##label TA2 !'##cross-references GB:J04049; GB:J04050; GB:M22803; GB:M22804; !1GB:M22805; GB:M22806; NID:g190382; PIDN:AAC13652.1; !1PID:g190384 REFERENCE A30055 !$#authors Morris, J.I.; Varandani, P.T. !$#journal Biochim. Biophys. Acta (1988) 949:169-180 !$#title Characterization of a cDNA for human glutathione-insulin !1transhydrogenase (protein-disulfide isomerase/ !1oxidoreductase). !$#cross-references MUID:88134925; PMID:3342239 !$#accession A30055 !'##molecule_type mRNA !'##residues 293-351,'R',353-401,'HS',404-459,'Q',461-508 ##label MOR !'##cross-references EMBL:X07077 !'##experimental_source liver REFERENCE A29787 !$#authors Cheng, S.; Gong, Q.; Parkison, C.; Robinson, E.A.; Appella, !1E.; Merlino, G.T.; Pastan, I. !$#journal J. Biol. Chem. (1987) 262:11221-11227 !$#title The nucleotide sequence of a human cellular thyroid hormone !1binding protein present in endoplasmic reticulum. !$#cross-references MUID:87280213; PMID:3611107 !$#accession A29787 !'##molecule_type mRNA !'##residues 1-140,'R',142-359,'RAG',363-371,'P',373-508 ##label CHE !'##cross-references GB:J02783; NID:g339646; PIDN:AAA61169.1; !1PID:g339647 !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing REFERENCE A26632 !$#authors Pihlajaniemi, T.; Helaakoski, T.; Tasanen, K.; Myllyla, R.; !1Huhtala, M.L.; Koivu, J.; Kivirikko, K.I. !$#journal EMBO J. (1987) 6:643-649 !$#title Molecular cloning of the beta-subunit of human prolyl !14-hydroxylase. This subunit and protein disulphide isomerase !1are products of the same gene. !$#cross-references MUID:87218523; PMID:3034602 !$#accession A26632 !'##molecule_type mRNA !'##residues 1-9,'PWX',13-43,'PP',46-48,'H',50-438,'G',440-443,'G', !1445-480,'V',482-508 ##label PIH !'##cross-references EMBL:X05130; NID:g35654; PIDN:CAA28775.1; !1PID:g35655 !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing REFERENCE A42791 !$#authors Tasanen, K.; Oikarinen, J.; Kivirikko, K.I.; Pihlajaniemi, !1T. !$#journal J. Biol. Chem. (1992) 267:11513-11519 !$#title Promoter of the gene for the multifunctional protein !1disulfide isomerase polypeptide. Functional significance of !1the six CCAAT boxes and other promoter elements. !$#cross-references MUID:92283868; PMID:1597478 !$#accession A42791 !'##molecule_type DNA !'##residues 1-25 ##label TA3 !'##cross-references GB:S37207; NID:g249922; PIDN:AAB22262.1; !1PID:g249923 !'##note sequence extracted from NCBI backbone (NCBIN:104755, !1NCBIP:104756) REFERENCE A33178 !$#authors Ward, L.D.; Hong, J.; Whitehead, R.H.; Simpson, R.J. !$#journal Electrophoresis (1990) 11:883-891 !$#title Development of a database of amino acid sequences for human !1colon carcinoma proteins separated by two-dimensional !1polyacrylamide gel electrophoresis. !$#cross-references MUID:91176935; PMID:2079031 !$#accession I33178 !'##molecule_type protein !'##residues 18-24,'X',26 ##label WAR REFERENCE A61002 !$#authors Bauw, G.; Rasmussen, H.H.; Van Den Bulcke, M.; Van Damme, !1J.; Puype, M.; Gesser, B.; Celis, J.E.; Vandekerckhove, J. !$#journal Electrophoresis (1990) 11:528-536 !$#title Two-dimensional gel electrophoresis, protein electroblotting !1and microsequencing: a direct link between proteins and !1genes. !$#cross-references MUID:91031404; PMID:1699755 !$#accession F61002 !'##molecule_type protein !'##residues 317-326;351-363,'X',365-370;402-406,'X',408-419 ##label BAU GENETICS !$#gene GDB:P4HB; PO4DB !'##cross-references GDB:120708; OMIM:176790 !$#map_position 17q25-17q25 !$#introns 49/1; 118/1; 162/3; 208/3; 243/3; 285/3; 352/3; 393/1; 453/ !13; 482/3 COMPLEX in procollagen-proline dioxygenase forms a heterotetramer of !1two alpha chains (see PIR:DAHUA1) and two beta chains FUNCTION DSI !$#description as protein disulfide-isomerase (EC 5.3.4.1) catalyzes the !1rearrangement of both intrachain and interchain disulfide !1bonds in proteins to form the native structures !$#pathway protein synthesis FUNCTION PHB !$#description as procollagen-proline dioxygenase (EC 1.14.11.2) beta chain !1participates in a complex that 4-hydroxylates proline !1residues in the G-X-P-G motif of collagen and collagen-like !1molecules !$#pathway collagen synthesis FUNCTION TDI !$#description as thyroxine deiodinase (EC 3.8.1.4) reduces iodinated !1thyronine residues to release hydrogen iodide CLASSIFICATION #superfamily protein disulfide-isomerase; thioredoxin !1homology KEYWORDS ascorbic acid; duplication; endoplasmic reticulum; !1homodimer; intramolecular oxidoreductase; isomerase; !1redox-active disulfide FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-508 #product protein disulfide-isomerase #status !8predicted #label MAT\ !$32-119 #domain thioredoxin homology #label TX1\ !$375-460 #domain thioredoxin homology #label TX2\ !$505-508 #region endoplasmic reticulum retention signal\ !$53-56,397-400 #disulfide_bonds redox-active #status predicted\ !$312-343 #disulfide_bonds #status predicted SUMMARY #length 508 #molecular-weight 57116 #checksum 1815 SEQUENCE /// ENTRY ISBOSS #type complete TITLE protein disulfide-isomerase (EC 5.3.4.1) precursor - bovine ALTERNATE_NAMES cellular thyroid hormone-binding protein; endoplasmic reticulum protein ERp59; iodothyronine 5'-monodeiodinase; prolyl-4 hydroxylase beta chain CONTAINS procollagen-proline dioxygenase (EC 1.14.11.2) beta chain; thyroxine deiodinase (EC 3.8.1.4) ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 06-Oct-2000 ACCESSIONS A26829 REFERENCE A26829 !$#authors Yamauchi, K.; Yamamoto, T.; Hayashi, H.; Koya, S.; Takikawa, !1H.; Toyoshima, K.; Horiuchi, R. !$#journal Biochem. Biophys. Res. Commun. (1987) 146:1485-1492 !$#title Sequence of membrane-associated thyroid hormone binding !1protein from bovine liver: its identity with protein !1disulphide isomerase. !$#cross-references MUID:87298601; PMID:3619939 !$#accession A26829 !'##molecule_type mRNA !'##residues 1-510 ##label YAM !'##cross-references GB:M17596; NID:g163496; PIDN:AAA30690.1; !1PID:g163497 !'##note the authors translated the codon TTC for residue 175 as Leu COMMENT This enzyme catalyzes the rearrangement of both intrachain !1and interchain disulfide bonds in proteins to form the !1native structures. CLASSIFICATION #superfamily protein disulfide-isomerase; thioredoxin !1homology KEYWORDS ascorbic acid; duplication; endoplasmic reticulum; !1homodimer; intramolecular oxidoreductase; isomerase; !1redox-active disulfide FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-510 #product protein disulfide-isomerase #status !8predicted #label MAT\ !$34-121 #domain thioredoxin homology #label TX1\ !$377-462 #domain thioredoxin homology #label TX2\ !$507-510 #region endoplasmic reticulum retention signal\ !$55-58,399-402 #disulfide_bonds redox-active #status predicted\ !$314-345 #disulfide_bonds #status predicted SUMMARY #length 510 #molecular-weight 57265 #checksum 8487 SEQUENCE /// ENTRY A38362 #type complete TITLE protein disulfide-isomerase (EC 5.3.4.1) precursor - rabbit ALTERNATE_NAMES 55K thyroid hormone-binding protein; cellular thyroid hormone-binding protein; endoplasmic reticulum protein ERp59; iodothyronine 5'-monodeiodinase; prolyl-4 hydroxylase beta chain CONTAINS procollagen-proline dioxygenase (EC 1.14.11.2) beta chain; thyroxine deiodinase (EC 3.8.1.4) ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 28-Jun-1991 #sequence_revision 26-May-1994 #text_change 06-Oct-2000 ACCESSIONS A38362 REFERENCE A38362 !$#authors Fliegel, L.; Newton, E.; Burns, K.; Michalak, M. !$#journal J. Biol. Chem. (1990) 265:15496-15502 !$#title Molecular cloning of cDNA encoding a 55-kDa multifunctional !1thyroid hormone binding protein of skeletal muscle !1sarcoplasmic reticulum. !$#cross-references MUID:90368750; PMID:1697592 !$#accession A38362 !'##molecule_type mRNA !'##residues 1-509 ##label FLI !'##cross-references GB:J05602; NID:g165738; PIDN:AAA31476.1; !1PID:g165739 !'##note the authors translated the codon TGG for residue 19 as Gly, GCG !1for residue 21 as Pro, and GAG for residue 38 as Arg COMMENT This enzyme catalyzes the rearrangement of both intrachain !1and interchain disulfide bonds in proteins to form the !1native structures. CLASSIFICATION #superfamily protein disulfide-isomerase; thioredoxin !1homology KEYWORDS ascorbic acid; duplication; endoplasmic reticulum; !1heterodimer; intramolecular oxidoreductase; isomerase; !1multifunctional enzyme; redox-active disulfide; skeletal !1muscle FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-509 #product protein disulfide-isomerase #status !8predicted #label MAT\ !$33-120 #domain thioredoxin homology #label TX1\ !$376-461 #domain thioredoxin homology #label TX2\ !$506-509 #region endoplasmic reticulum retention signal\ !$54-57,398-401 #disulfide_bonds redox-active #status predicted\ !$313-344 #disulfide_bonds #status predicted SUMMARY #length 509 #molecular-weight 56807 #checksum 2252 SEQUENCE /// ENTRY ISCHSS #type complete TITLE protein disulfide-isomerase (EC 5.3.4.1) precursor - chicken ALTERNATE_NAMES cellular thyroid hormone-binding protein; iodothyronine 5'-monodeiodinase; prolyl-4 hydroxylase beta chain CONTAINS procollagen-proline dioxygenase (EC 1.14.11.2) beta chain; thyroxine deiodinase (EC 3.8.1.4) ORGANISM #formal_name Gallus gallus #common_name chicken DATE 31-Dec-1992 #sequence_revision 03-Oct-1995 #text_change 06-Oct-2000 ACCESSIONS S02084; S25760; PS0008; S03265 REFERENCE S02084 !$#authors Parkkonen, T.; Kivirikko, K.I.; Pihlajaniemi, T. !$#journal Biochem. J. (1988) 256:1005-1011 !$#title Molecular cloning of a multifunctional chicken protein !1acting as the prolyl 4-hydroxylase beta-subunit, protein !1disulphide-isomerase and a cellular thyroid-hormone-binding !1protein. Comparison of cDNA-deduced amino acid sequences !1with those in other species. !$#cross-references MUID:89134157; PMID:2851999 !$#accession S02084 !'##molecule_type mRNA !'##residues 23-515 ##label PAR !'##cross-references EMBL:X13110 !$#accession S25760 !'##molecule_type protein !'##residues 23-32;96-109 ##label PA2 REFERENCE PS0008 !$#authors Nakazawa, M.; Aida, T.; Everson, W.V.; Gonda, M.A.; Hughes, !1S.H.; Kao, W.W.Y. !$#journal Gene (1988) 71:451-460 !$#title Structure of the gene encoding the beta-subunit of chicken !1prolyl 4-hydroxylase. !$#cross-references MUID:89138021; PMID:2852147 !$#accession PS0008 !'##molecule_type DNA !'##residues 1-22,'Q',24-93,'DV', !196-128;163-172;209-218;244-253;286-295;353-358,'Q', !1360-463;483-515 ##label NAK !'##note the authors translated the codon CAG for residues 23 and 359 as !1Glu and His, respectively REFERENCE S03265 !$#authors Bassuk, J.A. !$#submission submitted to the EMBL Data Library, February 1988 !$#accession S03265 !'##molecule_type DNA !'##residues 23-77 ##label BAS !'##cross-references EMBL:X06768 GENETICS !$#introns 54/1; 123/1; 167/3; 213/3; 248/3; 290/3; 357/3; 398/1; 458/ !13; 487/3 FUNCTION !$#description catalyzes the rearrangement of both intrachain and !1interchain disulfide bonds in proteins to form the native !1structures CLASSIFICATION #superfamily protein disulfide-isomerase; thioredoxin !1homology KEYWORDS ascorbic acid; duplication; endoplasmic reticulum; !1intramolecular oxidoreductase; isomerase; multifunctional !1enzyme; redox-active disulfide FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-515 #product protein disulfide-isomerase #status !8experimental #label MAT\ !$37-124 #domain thioredoxin homology #label TX1\ !$380-465 #domain thioredoxin homology #label TX2\ !$512-515 #region endoplasmic reticulum retention signal\ !$58-61,402-405 #disulfide_bonds redox-active #status predicted\ !$317-348 #disulfide_bonds #status predicted SUMMARY #length 515 #molecular-weight 57409 #checksum 1276 SEQUENCE /// ENTRY ISMSER #type complete TITLE protein disulfide-isomerase (EC 5.3.4.1) ERp72 precursor - mouse ALTERNATE_NAMES endoplasmic reticulum protein ERp72 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 18-Jun-1999 ACCESSIONS B34930 REFERENCE A34930 !$#authors Mazzarella, R.A.; Srinivasan, M.; Haugejorden, S.M.; Green, !1M. !$#journal J. Biol. Chem. (1990) 265:1094-1101 !$#title ERp72, an abundant luminal endoplasmic reticulum protein, !1contains three copies of the active site sequences of !1protein disulfide isomerase. !$#cross-references MUID:90110091; PMID:2295602 !$#accession B34930 !'##molecule_type mRNA !'##residues 1-638 ##label MAZ !'##cross-references GB:J05186; NID:g200282; PIDN:AAA39907.1; !1PID:g200283 CLASSIFICATION #superfamily protein disulfide-isomerase; thioredoxin !1homology KEYWORDS duplication; endoplasmic reticulum; glycoprotein; !1intramolecular oxidoreductase; isomerase; redox-active !1disulfide FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-638 #product endoplasmic reticulum protein ERp72 #status !8predicted #label MAT\ !$63-147 #domain thioredoxin homology #label TX1\ !$178-262 #domain thioredoxin homology #label TX2\ !$526-613 #domain thioredoxin homology #label TX3\ !$635-638 #region endoplasmic reticulum retention signal\ !$36 #binding_site carbohydrate (Asn) (covalent) #status !8absent\ !$84-87,199-202, !$548-551 #disulfide_bonds redox-active #status predicted SUMMARY #length 638 #molecular-weight 71973 #checksum 7591 SEQUENCE /// ENTRY A23723 #type complete TITLE protein disulfide-isomerase (EC 5.3.4.1) ERp72 precursor - human ALTERNATE_NAMES endoplasmic reticulum protein ERp72 ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1992 #sequence_revision 27-Jun-1994 #text_change 20-Apr-2000 ACCESSIONS A23723; A36508 REFERENCE A23723 !$#authors Huang, S.H.; Tomich, J.M.; Wu, H.; Jong, A.; Holcenberg, J. !$#journal J. Biol. Chem. (1991) 266:5353 !$#cross-references MUID:91161636; PMID:2002068 !$#contents erratum !$#accession A23723 !'##molecule_type mRNA !'##residues 1-645 ##label HUA !'##cross-references GB:J05016; NID:g181507; PIDN:AAA58460.1; !1PID:g181508 REFERENCE A36508 !$#authors Huang, S.H.; Tomich, J.M.; Wu, H.; Jong, A.; Holcenberg, J. !$#journal J. Biol. Chem. (1989) 264:14762-14768 !$#title Human deoxycytidine kinase. Sequence of cDNA clones and !1analysis of expression in cell lines with and without enzyme !1activity. !$#cross-references MUID:89359272; PMID:2549034 !$#accession A36508 !'##molecule_type DNA !'##residues 1-609,'TKRTQLNLRVETEIWSI' ##label HU2 !'##cross-references GB:J05016 !'##note this sequence has been corrected reference A23723 COMMENT This sequence has no homology to deoxycytidine kinase (EC !12.7.1.74) and the protein has no deoxycytidine kinase !1activity. GENETICS !$#gene GDB:ERP70; ERP72 !'##cross-references GDB:9957774 CLASSIFICATION #superfamily protein disulfide-isomerase; thioredoxin !1homology KEYWORDS duplication; endoplasmic reticulum; intramolecular !1oxidoreductase; isomerase; redox-active disulfide FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-645 #product endoplasmic reticulum protein ERp72 #status !8predicted #label MAT\ !$70-154 #domain thioredoxin homology #label TX1\ !$185-269 #domain thioredoxin homology #label TX2\ !$533-620 #domain thioredoxin homology #label TX3\ !$642-645 #region endoplasmic reticulum retention signal\ !$91-94,206-209, !$555-558 #disulfide_bonds redox-active #status predicted SUMMARY #length 645 #molecular-weight 72932 #checksum 3717 SEQUENCE /// ENTRY S32476 #type complete TITLE protein disulfide-isomerase (EC 5.3.4.1) ERp72 precursor - rat ALTERNATE_NAMES calcium-binding protein 2; endoplasmic reticulum protein ERp72 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 02-Dec-1993 #sequence_revision 27-Jun-1994 #text_change 07-May-1999 ACCESSIONS S32476 REFERENCE S32476 !$#authors Van Nguyen, P.; Rupp, K.; Lampen, A.; Soeling, H.D. !$#journal Eur. J. Biochem. (1993) 213:789-795 !$#title CaBP2 is a rat homolog of ERp72 with proteindisulfide !1isomerase activity. !$#cross-references MUID:93238767; PMID:8477750 !$#accession S32476 !'##molecule_type mRNA !'##residues 1-643 ##label VAN !'##cross-references GB:S59335 CLASSIFICATION #superfamily protein disulfide-isomerase; thioredoxin !1homology KEYWORDS duplication; endoplasmic reticulum; intramolecular !1oxidoreductase; isomerase; redox-active disulfide FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-643 #product endoplasmic reticulum protein ERp72 #status !8predicted #label MAT\ !$68-152 #domain thioredoxin homology #label TX1\ !$183-267 #domain thioredoxin homology #label TX2\ !$531-618 #domain thioredoxin homology #label TX3\ !$640-643 #region endoplasmic reticulum retention signal\ !$89-92,204-207, !$553-556 #disulfide_bonds redox-active #status predicted SUMMARY #length 643 #molecular-weight 72834 #checksum 5161 SEQUENCE /// ENTRY ISAASS #type complete TITLE protein disulfide-isomerase (EC 5.3.4.1) precursor (clone L1) - alfalfa ALTERNATE_NAMES prolyl-4 hydroxylase beta chain ORGANISM #formal_name Medicago sativa #common_name alfalfa DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 18-Jun-1999 ACCESSIONS S22479; S18160 REFERENCE S22479 !$#authors Shorrosh, B.S.; Dixon, R.A. !$#journal Plant Mol. Biol. (1992) 19:319-321 !$#title Sequence analysis and developmental expression of an alfalfa !1protein disulfide isomerase. !$#cross-references MUID:92322960; PMID:1623182 !$#accession S22479 !'##molecule_type mRNA !'##residues 1-512 ##label SHO !'##cross-references EMBL:Z11499; NID:g19653; PIDN:CAA77575.1; !1PID:g19654 COMMENT This enzyme catalyzes the rearrangement of both intrachain !1and interchain disulfide bonds in proteins to form the !1native structures. CLASSIFICATION #superfamily protein disulfide-isomerase; thioredoxin !1homology KEYWORDS duplication; endoplasmic reticulum; hydrolase; !1intramolecular oxidoreductase; isomerase; multifunctional !1enzyme; redox-active disulfide FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-512 #product protein disulfide-isomerase #status !8predicted #label MAT\ !$41-129 #domain thioredoxin homology #label TX1\ !$385-470 #domain thioredoxin homology #label TX2\ !$509-512 #region endoplasmic reticulum retention signal\ !$62-65,407-410 #disulfide_bonds redox-active #status predicted SUMMARY #length 512 #molecular-weight 57087 #checksum 9537 SEQUENCE /// ENTRY A32820 #type complete TITLE protein disulfide-isomerase homolog precursor - Trypanosoma brucei ALTERNATE_NAMES bloodstream-specific protein 2; BS2 protein ORGANISM #formal_name Trypanosoma brucei DATE 12-Oct-1989 #sequence_revision 26-May-1994 #text_change 18-Jun-1999 ACCESSIONS A32820 REFERENCE A32820 !$#authors Hsu, M.P.; Muhich, M.L.; Boothroyd, J.C. !$#journal Biochemistry (1989) 28:6440-6446 !$#title A developmentally regulated gene of trypanosomes encodes a !1homologue of rat protein-disulfide isomerase and !1phosphoinositol-phospholipase C. !$#cross-references MUID:90001196; PMID:2551375 !$#accession A32820 !'##molecule_type mRNA !'##residues 1-497 ##label HSU !'##cross-references GB:J02865; NID:g162010; PIDN:AAA30168.1; !1PID:g162011 COMMENT This protein is more abundant in the bloodstream-form !1trypanosomes in the mammalian host. COMMENT This protein possesses 13 N-X-S/T sites, but it is not known !1if the protein is glycosylated. Its function has not been !1determined. CLASSIFICATION #superfamily protein disulfide-isomerase; thioredoxin !1homology KEYWORDS duplication; endoplasmic reticulum; glycoprotein; !1redox-active disulfide FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-497 #product protein disulfide-isomerase homolog #status !8predicted #label MAT\ !$27-109 #domain thioredoxin homology #label TX1\ !$357-440 #domain thioredoxin homology #label TX2\ !$494-497 #region endoplasmic reticulum retention signal !8#status atypical\ !$30,63,85,153,154, !$250,278,413,465, !$476,482,485,488 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$48-51,378-381 #disulfide_bonds redox-active #status predicted\ !$76-147 #disulfide_bonds #status predicted SUMMARY #length 497 #molecular-weight 55579 #checksum 1064 SEQUENCE /// ENTRY ISBYSS #type complete TITLE protein disulfide-isomerase (EC 5.3.4.1) precursor - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YCL043c; protein YCL313; S-S rearrangase; thioredoxin-related glycoprotein 1; thyroid hormone-binding protein ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 21-Jul-2000 ACCESSIONS JX0182; PS0224; A39376; S15050; JS0634; S40913; A41713; !1S19372; S25349 REFERENCE JX0182 !$#authors Tachikawa, H.; Miura, T.; Katakura, Y.; Mizunaga, T. !$#journal J. Biochem. (1991) 110:306-313 !$#title Molecular structure of a yeast gene, PDI1, encoding protein !1disulfide isomerase that is essential for cell growth. !$#cross-references MUID:92105067; PMID:1761527 !$#accession JX0182 !'##molecule_type DNA !'##residues 1-522 ##label TAC !'##cross-references GB:D00842; NID:g218506; PIDN:BAA00723.1; !1PID:g218507 !$#accession PS0224 !'##molecule_type protein !'##residues 99-112;'X',185-193;211-217;'X',233-237,'X',239;284-286,'X', !1288-298;309-315;325-335 ##label TA2 REFERENCE A39376 !$#authors LaMantia, M.; Miura, T.; Tachikawa, H.; Kaplan, H.A.; !1Lennarz, W.J.; Mizunaga, T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:4453-4457 !$#title Glycosylation site binding protein and protein disulfide !1isomerase are identical and essential for cell viability in !1yeast. !$#cross-references MUID:91239586; PMID:1840696 !$#accession A39376 !'##molecule_type DNA !'##residues 1-522 ##label LAM !'##cross-references GB:M62815 REFERENCE S15050 !$#authors Scherens, B.; Dubois, E.; Messenguy, F. !$#journal Yeast (1991) 7:185-193 !$#title Determination of the sequence of the yeast YCL313 gene !1localized on chromosome III. Homology with the protein !1disulfide isomerase (PDI gene product) of other organisms. !$#cross-references MUID:91289690; PMID:2063627 !$#accession S15050 !'##molecule_type DNA !'##residues 1-522 ##label SCH !'##cross-references EMBL:X57712; NID:g4801; PIDN:CAA40883.1; PID:g4802 REFERENCE JS0634 !$#authors Farquhar, R.; Honey, N.; Murant, S.J.; Bossier, P.; Schultz, !1L.; Montogomery, D.; Ellis, R.W.; Freedman, R.B.; Tuite, !1M.F. !$#journal Gene (1991) 108:81-89 !$#title Protein disulfide isomerase is essential for viability in !1Saccharomyces cerevisiae. !$#cross-references MUID:92104510; PMID:1761235 !$#accession JS0634 !'##molecule_type DNA !'##residues 1-113,'R',115-505,'EADAEAEA',506-522 ##label FAR !'##cross-references EMBL:X54535; NID:g4119; PIDN:CAA38402.1; PID:g4120 REFERENCE S40913 !$#authors Kuentzel, H. !$#submission submitted to the EMBL Data Library, April 1990 !$#accession S40913 !'##molecule_type DNA !'##residues 1-82,'V',84-142,'S',144,146-167,'E',169-225,'V',227-457, !1'S',459-505,'EADAEAEA',506-522 ##label KUE !'##cross-references EMBL:X52313; NID:g3948; PIDN:CAA36550.1; PID:g3949 REFERENCE A41713 !$#authors Guenther, R.; Braeuer, C.; Janetzky, B.; Foerster, H.H.; !1Ehbrecht, I.M.; Lehle, L.; Kuentzel, H. !$#journal J. Biol. Chem. (1991) 266:24557-24563 !$#title The Saccharomyces cerevisiae TRG1 gene is essential for !1growth and encodes a lumenal endoplasmic reticulum !1glycoprotein involved in the maturation of vacuolar !1carboxypeptidase. !$#cross-references MUID:92105117; PMID:1761554 !$#accession A41713 !'##molecule_type DNA !'##residues 1-82,'V',84-142,'S',144,146-167,'E',169-225,'V',227-457, !1'S',459-505,'EADAEAEA',506-522 ##label GUE !'##cross-references GB:M76982; NID:g173023; PIDN:AAA35169.1; !1PID:g173024 REFERENCE S19367 !$#authors Dubois, E.; Pierard, A.; Gigot, D.; Glansdorff, N.; !1Messenguy, F.; Scherens, B. !$#submission submitted to the Protein Sequence Database, March 1992 !$#accession S19372 !'##molecule_type DNA !'##residues 1-522 ##label DUB !'##cross-references EMBL:X59720; NID:g1907116; PIDN:CAA42373.1; !1PID:g5320; GSPDB:GN00003; MIPS:YCL043c REFERENCE S25347 !$#authors Scherens, B.; Messenguy, F.; Gigot, D.; Dubois, E. !$#journal Yeast (1992) 8:577-586 !$#title The complete sequence of a 9,543 bp segment on the left arm !1of chromosome III reveals five open reading frames including !1glucokinase and the protein disulfide isomerase. !$#cross-references MUID:92397595; PMID:1523890 !$#accession S25349 !'##molecule_type DNA !'##residues 1-522 ##label SC2 !'##cross-references EMBL:X59720; EMBL:S43845; EMBL:S49180; EMBL:S58084; !1EMBL:S93798; NID:g1907116; PIDN:CAA42373.1; PID:g5320 GENETICS !$#gene SGD:PDI1; MFP1; TRG1; MIPS:YCL043c !'##cross-references SGD:S0000548; MIPS:YCL043c !$#map_position 3L FUNCTION !$#description catalyzes rearrangement of both intrachain and interchain !1disulfide bonds CLASSIFICATION #superfamily protein disulfide-isomerase; thioredoxin !1homology KEYWORDS duplication; endoplasmic reticulum; glycoprotein; homodimer; !1intramolecular oxidoreductase; isomerase; redox-active !1disulfide FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-522 #product protein disulfide-isomerase #status !8predicted #label MAT\ !$40-125 #domain thioredoxin homology #label TX1\ !$384-470 #domain thioredoxin homology #label TX2\ !$519-522 #region endoplasmic reticulum retention signal\ !$61-64,406-409 #disulfide_bonds redox-active #status predicted\ !$82,117,155,174,425 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$90-97 #disulfide_bonds #status predicted SUMMARY #length 522 #molecular-weight 58227 #checksum 9937 SEQUENCE /// ENTRY A28807 #type complete TITLE protein disulfide-isomerase (EC 5.3.4.1) ER60 precursor - rat ALTERNATE_NAMES endoplasmic reticulum protein ERp60; ER60 proteinase; hormone induced protein 70K (HIP-70) ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1989 #sequence_revision 27-Jun-1994 #text_change 18-Jun-1999 ACCESSIONS A28807; A43050; A43051; A40095 REFERENCE A28807 !$#authors Bennett, C.F.; Balcarek, J.M.; Varrichio, A.; Crooke, S.T. !$#journal Nature (1988) 334:268-270 !$#title Molecular cloning and complete amino-acid sequence of form-I !1phosphoinositide-specific phospholipase C. !$#cross-references MUID:88288403; PMID:3398923 !$#accession A28807 !'##molecule_type mRNA !'##residues 1-504 ##label BEN !'##cross-references GB:X12355; NID:g56904; PIDN:CAA30916.1; PID:g56905 REFERENCE A43050 !$#authors Martin, J.L.; Pumford, N.R.; LaRosa, A.C.; Martin, B.M.; !1Gonzaga, H.M.S.; Beaven, M.A.; Pohl, L.R. !$#journal Biochem. Biophys. Res. Commun. (1991) 178:679-685 !$#title A metabolite of halothane covalently binds to an endoplasmic !1reticulum protein that is highly homologous to !1phosphatidylinositol-specific phospholipase C-alpha but has !1no activity. !$#cross-references MUID:91315499; PMID:1650195 !$#accession A43050 !'##molecule_type protein !'##residues 25-37;95-104;130-138;274-279;366-378;426-450;482-495 !1##label MAR REFERENCE A43051 !$#authors Urade, R.; Nasu, M.; Moriyama, T.; Wada, K.; Kito, M. !$#journal J. Biol. Chem. (1992) 267:15152-15159 !$#title Protein degradation by the phosphoinositide-specific !1phospholipase C-alpha family from rat liver endoplasmic !1reticulum. !$#cross-references MUID:92340568; PMID:1321829 !$#accession A43051 !'##molecule_type protein !'##residues 25-34;173-194;432-459 ##label URA REFERENCE A40095 !$#authors Mobbs, C.V.; Fink, G.; Pfaff, D.W. !$#journal Science (1990) 247:1477-1479 !$#title HIP-70: a protein induced by estrogen in the brain and LH-RH !1in the pituitary. !$#cross-references MUID:90208308; PMID:2181662 !$#accession A40095 !'##molecule_type protein !'##residues 26-43 ##label MOB COMMENT ER60 may be part of a complex capable of catalyzing cleavage !1of itself, of protein disulfide-isomerase, and of !1calreticulin. This activity can be inhibited by !1para-chloromercuribenzoate. COMMENT ER60 protease does not appear to be a cytoplasmic !11-phosphatidylinositol-4,5-bisphosphate phosphodiesterase 1 !1as originally thought. It does not hydrolyze !1phosphatidylinositol, phosphatidylinositol-4-phosphate, or !1phosphatidylinositol-4,6-bisphosphate. CLASSIFICATION #superfamily protein disulfide-isomerase; thioredoxin !1homology KEYWORDS duplication; endoplasmic reticulum; intramolecular !1oxidoreductase; isomerase; redox-active disulfide FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-504 #product ER60 protease #status experimental #label !8MAT\ !$33-118 #domain thioredoxin homology #label TX1\ !$383-469 #domain thioredoxin homology #label TX2\ !$501-504 #region endoplasmic reticulum retention signal !8#status atypical\ !$57-60,405-408 #disulfide_bonds redox-active #status predicted SUMMARY #length 504 #molecular-weight 56623 #checksum 9538 SEQUENCE /// ENTRY S55507 #type complete TITLE protein disulfide-isomerase (EC 5.3.4.1) ER60 precursor - human ALTERNATE_NAMES ER60 proteinase ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S55507 REFERENCE S55507 !$#authors Charnock-Jones, D. !$#submission submitted to the EMBL Data Library, June 1995 !$#description Cloning, expression and genomic organization of human !1placental protein disulfide isomerase (previously identified !1as phospholipase C alpha). !$#accession S55507 !'##status preliminary !'##molecule_type mRNA !'##residues 1-505 ##label CHA !'##cross-references EMBL:Z49835; NID:g860985; PIDN:CAA89996.1; !1PID:g860986 COMMENT ER60 may be part of a complex capable of catalyzing cleavage !1of itself, of protein disulfide-isomerase, and of !1calreticulin. This activity can be inhibited by !1para-chloromercuribenzoate. CLASSIFICATION #superfamily protein disulfide-isomerase; thioredoxin !1homology KEYWORDS duplication; endoplasmic reticulum; intramolecular !1oxidoreductase; isomerase; redox-active disulfide FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-488 #product ER60 protease #status predicted #label MAT\ !$33-118 #domain thioredoxin homology #label TX1\ !$384-470 #domain thioredoxin homology #label TX2\ !$502-505 #region endoplasmic reticulum retention signal\ !$57-60,406-409 #disulfide_bonds redox-active #status predicted SUMMARY #length 505 #molecular-weight 56679 #checksum 1214 SEQUENCE /// ENTRY JC2385 #type complete TITLE protein disulfide-isomerase (EC 5.3.4.1) ER60 precursor - bovine ALTERNATE_NAMES ER60 proteinase ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JC2385 REFERENCE JC2385 !$#authors Hirano, N.; Shibasaki, F.; Kato, H.; Sakai, R.; Tanaka, T.; !1Nishida, J.; Yazaki, Y.; Takenawa, T.; Hirai, H. !$#journal Biochem. Biophys. Res. Commun. (1994) 204:375-382 !$#title Molecular cloning and characterization of a cDNA for bovine !1phospholipase C-alpha: Proposal of redesignation of !1phospholipase C-alpha. !$#cross-references MUID:95032122; PMID:7945384 !$#accession JC2385 !'##molecule_type mRNA !'##residues 1-488 ##label HIR !'##cross-references DDBJ:D16234 !'##experimental_source thymus COMMENT ER60 may be part of a complex capable of catalyzing cleavage !1of itself, of protein disulfide-isomerase, and of !1calreticulin. This activity can be inhibited by !1para-chloromercuribenzoate. COMMENT This enzyme has two Trp-Cys-Gly-His-Cys-Lys motifs. CLASSIFICATION #superfamily protein disulfide-isomerase; thioredoxin !1homology KEYWORDS duplication; endoplasmic reticulum; intramolecular !1oxidoreductase; isomerase; redox-active disulfide FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-488 #product ER60 protease #status predicted #label MAT\ !$33-118 #domain thioredoxin homology #label TX1\ !$367-453 #domain thioredoxin homology #label TX2\ !$485-488 #region endoplasmic reticulum retention signal\ !$57-60,389-392 #disulfide_bonds redox-active #status predicted SUMMARY #length 488 #molecular-weight 54973 #checksum 6631 SEQUENCE /// ENTRY A39292 #type complete TITLE protein disulfide-isomerase (EC 5.3.4.1) dsbA precursor - Escherichia coli (strain K-12) ALTERNATE_NAMES thiol:disulfide interchange protein dsbA ORGANISM #formal_name Escherichia coli DATE 21-Apr-1992 #sequence_revision 27-Jun-1994 #text_change 01-Mar-2002 ACCESSIONS A39292; S40806; A49270; S77942; S19160; H65190; JS0620 REFERENCE A39292 !$#authors Bardwell, J.C.A.; McGovern, K.; Beckwith, J. !$#journal Cell (1991) 67:581-589 !$#title Identification of a protein required for disulfide bond !1formation in vivo. !$#cross-references MUID:92034980; PMID:1934062 !$#accession A39292 !'##molecule_type DNA !'##residues 1-208 ##label BAR !'##cross-references GB:M77746; NID:g145812; PIDN:AAA23715.1; !1PID:g145813 REFERENCE S40802 !$#authors Plunkett III, G.; Burland, V.; Daniels, D.L.; Blattner, F.R. !$#journal Nucleic Acids Res. (1993) 21:3391-3398 !$#title Analysis of the Escherichia coli genome. III. DNA sequence !1of the region from 87.2 to 89.2 minutes. !$#cross-references MUID:93347969; PMID:8346018 !$#accession S40806 !'##molecule_type DNA !'##residues 1-208 ##label PLU !'##cross-references EMBL:L19201; NID:g304961; PIDN:AAB02995.1; !1PID:g304966 REFERENCE A49270 !$#authors Zapun, A.; Bardwell, J.C.A.; Creighton, T.E. !$#journal Biochemistry (1993) 32:5083-5092 !$#title The reactive and destabilizing disulfide bond of DsbA, a !1protein required for protein disulfide bond formation in !1Vivo. !$#cross-references MUID:93264419; PMID:8494885 !$#accession A49270 !'##molecule_type protein !'##residues 20-24 ##label ZAP REFERENCE A43053 !$#authors Martin, J.L.; Bardwell, J.C.A.; Kuriyan, J. !$#journal Nature (1993) 365:464-468 !$#title Crystal structure of the DsbA protein required for !1disulphide bond formation in vivo. !$#cross-references MUID:94019776; PMID:8413591 !$#contents annotation; X-ray crystallography, 2 angstroms; domain !1structure REFERENCE A43052 !$#authors Akiyama, Y.; Kamitani, S.; Kusukawa, N.; Ito, K. !$#journal J. Biol. Chem. (1992) 267:22440-22445 !$#title In vitro catalysis of oxidative folding of disulfide-bonded !1proteins by the Escherichia coli dsbA (ppfA) gene product. !$#cross-references MUID:93054536; PMID:1429594 !$#contents annotation; function REFERENCE S77942 !$#authors Ito, K. !$#submission submitted to the EMBL Data Library, November 1991 !$#accession S77942 !'##molecule_type DNA !'##residues 1-208 ##label ITO !'##cross-references EMBL:X63186; NID:g42478; PIDN:CAA44868.1; !1PID:g42479 REFERENCE JS0620 !$#authors Kamitani, S.; Akiyama, Y.; Ito, K. !$#journal EMBO J. (1992) 11:57-62 !$#title Identification and characterization of an Escherichia coli !1gene required for the formation of correctly folded alkaline !1phosphatase, a periplasmic enzyme. !$#cross-references MUID:92155183; PMID:1740115 !$#accession S19160 !'##molecule_type DNA !'##residues 1-183,'VWIPAIW',190,'FL',193,'SSMLIQ' ##label KAM !'##cross-references EMBL:X63186 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65190 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-208 ##label BLAT !'##cross-references GB:AE000461; GB:U00096; NID:g2367318; !1PIDN:AAC76858.1; PID:g1790291; UWGP:b3860 !'##experimental_source strain K-12, substrain MG1655 COMMENT This protein is unusual in that the reduced form is more !1stable than that with the disulfide bond. GENETICS !$#gene dsbA; ppfA !$#map_position 87.35 !$#note dsbA is preferred FUNCTION !$#description catalyzes disulfide bond formation in certain periplasmic !1proteins CLASSIFICATION #superfamily protein disulfide-isomerase dsbA; thioredoxin !1homology KEYWORDS intramolecular oxidoreductase; isomerase; periplasmic space; !1redox-active disulfide FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-208 #product protein disulfide-isomerase dsbA #status !8predicted #label PAF\ !$29-81,156-186 #domain thioredoxin homology #status atypical #label !8TXN\ !$49-52 #disulfide_bonds redox-active #status experimental SUMMARY #length 208 #molecular-weight 23104 #checksum 8040 SEQUENCE /// ENTRY B46411 #type complete TITLE protein disulfide-isomerase (EC 5.3.4.1) dsbA precursor - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES thiol:disulfide interchange protein dsbA ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B64098; B46411 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession B64098 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-205 ##label TIGR !'##cross-references GB:U32766; GB:L42023; NID:g1573854; !1PIDN:AAC22503.1; PID:g1573860; TIGR:HI0846 REFERENCE A46411 !$#authors Tomb, J.F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:10252-10256 !$#title A periplasmic protein disulfide oxidoreductase is required !1for transformation of Haemophilus influenzae Rd. !$#cross-references MUID:93066217; PMID:1438213 !$#accession B46411 !'##molecule_type DNA !'##residues 1-205 ##label TOM !'##cross-references GB:M94205; NID:g148885; PIDN:AAA24956.1; !1PID:g148887 !'##note sequence extracted from NCBI backbone (NCBIN:117671, !1NCBIP:117677) GENETICS !$#gene por FUNCTION !$#description catalyzes disulfide bond formation in certain periplasmic !1proteins CLASSIFICATION #superfamily protein disulfide-isomerase dsbA; thioredoxin !1homology KEYWORDS intramolecular oxidoreductase; isomerase; periplasmic space; !1redox-active disulfide FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-205 #product protein disulfide-isomerase dsbA #status !8predicted #label PAF\ !$32-84,157-187 #domain thioredoxin homology #status atypical #label !8TXN\ !$52-55 #disulfide_bonds redox-active #status predicted SUMMARY #length 205 #molecular-weight 22964 #checksum 2957 SEQUENCE /// ENTRY A46148 #type complete TITLE protein disulfide-isomerase (EC 5.3.4.1) dsbA precursor VC0034 [imported] - Vibrio cholerae (strain N16961 serogroup O1) ALTERNATE_NAMES thiol/disulfide interchanger TcpG; thiol:disulfide interchange protein ORGANISM #formal_name Vibrio cholerae DATE 10-Sep-1999 #sequence_revision 01-Sep-2000 #text_change 02-Feb-2001 ACCESSIONS E82371; A46148; S25268; S19904 REFERENCE A82035 !$#authors Heidelberg, J.F.; Eisen, J.A.; Nelson, W.C.; Clayton, R.A.; !1Gwinn, M.L.; Dodson, R.J.; Haft, D.H.; Hickey, E.K.; !1Peterson, J.D.; Umayam, L.A.; Gill, S.R.; Nelson, K.E.; !1Read, T.D.; Tettelin, H.; Richardson, D.; Ermolaeva, M.D.; !1Vamathevan, J.; Bass, S.; Qin, H.; Dragoi, I.; Sellers, P.; !1McDonald, L.; Utterback, T.; Fleishmann, R.D.; Nierman, !1W.C.; White, O.; Salzberg, S.L.; Smith, H.O.; Colwell, R.R.; !1Mekalanos, J.J.; Venter, J.C.; Fraser, C.M. !$#journal Nature (2000) 406:477-483 !$#title DNA Sequence of both chromosomes of the cholera pathogen !1Vibrio cholerae. !$#cross-references MUID:20406833; PMID:10952301 !$#accession E82371 !'##molecule_type DNA !'##residues 1-200 ##label HEI !'##cross-references GB:AE004096; GB:AE003852; NID:g9654440; !1PIDN:AAF93212.1; GSPDB:GN00126; TIGR:VC0034 !'##experimental_source serogroup O1; strain N16961; biotype El Tor REFERENCE A46148 !$#authors Peek, J.A.; Taylor, R.K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:6210-6214 !$#title Characterization of a periplasmic thiol:disulfide !1interchange protein required for the functional maturation !1of secreted virulence factors of Vibrio cholerae. !$#cross-references MUID:92335268; PMID:1631111 !$#accession A46148 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-41,'S',43-200 ##label PEE !'##cross-references GB:M93713; NID:g155286; PIDN:AAA27568.1; !1PID:g155287 !'##note sequence extracted from NCBI backbone (NCBIP:108609) REFERENCE S25268 !$#authors Yu, J.; Webb, H.; Hirst, T.R. !$#journal Mol. Microbiol. (1992) 6:1949-1958 !$#title A homologue of the Escherichia coli DsbA protein involved in !1disulphide bond formation is required for enterotoxin !1biogenesis in Vibrio cholerae. !$#cross-references MUID:92374846; PMID:1324389 !$#accession S25268 !'##molecule_type DNA !'##residues 1-200 ##label YUJ !'##cross-references EMBL:X64725; NID:g48353; PIDN:CAA45977.1; !1PID:g48354 REFERENCE A45473 !$#authors Yu, J.; McLaughlin, S.; Freedman, R.B.; Hirst, T.R. !$#journal J. Biol. Chem. (1993) 268:4326-4330 !$#title Cloning and active site mutagenesis of Vibrio cholerae DsbA, !1a periplasmic enzyme that catalyzes disulfide bond !1formation. !$#cross-references MUID:93179441; PMID:8440717 !$#contents annotation; active site; amino end of mature chain GENETICS !$#gene VC0034; dsbA !$#map_position 1 FUNCTION !$#description catalyzes disulfide bond formation in certain periplasmic !1proteins CLASSIFICATION #superfamily protein disulfide-isomerase dsbA; thioredoxin !1homology KEYWORDS intramolecular oxidoreductase; isomerase; periplasmic space; !1redox-active disulfide FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-200 #product protein disulfide-isomerase dsbA #status !8experimental #label MAT\ !$29-78,154-184 #domain thioredoxin homology #status atypical #label !8TXN\ !$49-52 #disulfide_bonds redox-active #status experimental SUMMARY #length 200 #molecular-weight 22567 #checksum 1322 SEQUENCE /// ENTRY S32895 #type complete TITLE protein disulfide-isomerase (EC 5.3.4.1) dsbA homolog precursor - Salmonella typhimurium ALTERNATE_NAMES thiol:disulfide interchange protein dsbA ORGANISM #formal_name Salmonella typhimurium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S32895 REFERENCE S32886 !$#authors Friedrich, M.J.; Kinsey, N.E.; Vila, J.; Kadner, R.J. !$#journal Mol. Microbiol. (1993) 8:543-558 !$#title Nucleotide sequence of a 13.9kb segment of the 90kb !1virulence plasmid of Salmonella typhimurium: the presence of !1fimbrial biosynthetic genes. !$#cross-references MUID:93316852; PMID:8100983 !$#accession S32895 !'##status preliminary !'##molecule_type DNA !'##residues 1-217 ##label FRI !'##cross-references EMBL:L08613; NID:g154239; PIDN:AAC36966.1; !1PID:g154249 GENETICS !$#start_codon GTG FUNCTION !$#description catalyzes disulfide bond formation in certain periplasmic !1proteins CLASSIFICATION #superfamily protein disulfide-isomerase dsbA; thioredoxin !1homology KEYWORDS intramolecular oxidoreductase; isomerase; periplasmic space; !1redox-active disulfide FEATURE !$36-86,161-191 #domain thioredoxin homology #status atypical #label !8TXN\ !$54-57 #disulfide_bonds redox-active #status predicted SUMMARY #length 217 #molecular-weight 24244 #checksum 9580 SEQUENCE /// ENTRY E65073 #type complete TITLE protein disulfide-isomerase (EC 5.3.4.1) dsbC precursor - Escherichia coli (strain K-12) ALTERNATE_NAMES thiol:disulfide interchange protein; xprA protein ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS E65073; B39202 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65073 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-236 ##label BLAT !'##cross-references GB:AE000373; GB:U00096; NID:g2367173; !1PIDN:AAC75931.1; PID:g1789260; UWGP:b2893 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A39202 !$#authors Lovett, S.T.; Kolodner, R.D. !$#journal J. Bacteriol. (1991) 173:353-364 !$#title Nucleotide sequence of the Escherichia coli recJ chromosomal !1region and construction of recJ-overexpression plasmids. !$#cross-references MUID:91100304; PMID:1987126 !$#accession B39202 !'##status preliminary !'##molecule_type DNA !'##residues 1-218,220-236 ##label LOV !'##cross-references GB:M54884; NID:g147547; PIDN:AAA62788.1; !1PID:g147549 REFERENCE A43087 !$#authors Missiakas, D.; Georgopoulos, C.; Raina, S. !$#journal EMBO J. (1994) 13:2013-2020 !$#title The Escherichia coli dsbC (xprA) gene encodes a periplasmic !1protein involved in disulfide bond formation. !$#cross-references MUID:94222049; PMID:8168498 !$#contents annotation; active site; function GENETICS !$#gene dsbC; xprA FUNCTION !$#description catalyzes disulfide bond formation in certain periplasmic !1proteins CLASSIFICATION #superfamily protein disulfide-isomerase dsbC KEYWORDS intramolecular oxidoreductase; isomerase; periplasmic space; !1redox-active disulfide FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-236 #product protein disulfide-isomerase dsbC #status !8predicted #label MAT\ !$118-121 #disulfide_bonds redox-active #status experimental SUMMARY #length 236 #molecular-weight 25621 #checksum 3344 SEQUENCE /// ENTRY S44444 #type complete TITLE protein disulfide-isomerase (EC 5.3.4.1) dsbC precursor - Erwinia chrysanthemi ALTERNATE_NAMES thiol:disulfide interchange protein dsbC ORGANISM #formal_name Erwinia chrysanthemi DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S44444 REFERENCE S44444 !$#authors Shevchik, V.E.; Condemine, G.; Robert-Baudouy, J. !$#journal EMBO J. (1994) 13:2007-2012 !$#title Characterization of DsbC, a periplasmic protein of Erwinia !1chrysanthemi and Escherichia coli with disulfide isomerase !1activity. !$#cross-references MUID:94222048; PMID:8168497 !$#accession S44444 !'##molecule_type DNA !'##residues 1-238 ##label SHE !'##cross-references EMBL:X76687; NID:g495243; PIDN:CAA54108.1; !1PID:g495244 GENETICS !$#gene dsbC FUNCTION !$#description catalyzes disulfide bond formation in certain periplasmic !1proteins CLASSIFICATION #superfamily protein disulfide-isomerase dsbC KEYWORDS intramolecular oxidoreductase; isomerase; periplasmic space; !1redox-active disulfide FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-238 #product protein disulfide-isomerase dsbC #status !8predicted #label MAT\ !$119-122 #disulfide_bonds redox-active #status predicted SUMMARY #length 238 #molecular-weight 25907 #checksum 8220 SEQUENCE /// ENTRY E64110 #type complete TITLE protein disulfide-isomerase (EC 5.3.4.1) dsbC precursor - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES thiol:disulfide interchange protein dsbC ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS E64110 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession E64110 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-229 ##label TIGR !'##cross-references GB:U32800; GB:L42023; NID:g1574133; !1PIDN:AAC22866.1; PID:g1574142; TIGR:HI1213 FUNCTION !$#description catalyzes disulfide bond formation in certain periplasmic !1proteins CLASSIFICATION #superfamily protein disulfide-isomerase dsbC KEYWORDS intramolecular oxidoreductase; isomerase; periplasmic space; !1redox-active disulfide FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-229 #product protein disulfide-isomerase dsbC #status !8predicted #label MAT\ !$116-119 #disulfide_bonds redox-active #status predicted SUMMARY #length 229 #molecular-weight 25351 #checksum 2141 SEQUENCE /// ENTRY PMHUYB #type complete TITLE phosphoglycerate mutase (EC 5.4.2.1) B [validated] - human ALTERNATE_NAMES phosphoglycerate mutase 1; phosphoglycerate mutase brain isozyme; phosphoglycerate phosphomutase; phosphoglyceromutase ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 08-Dec-2000 ACCESSIONS A31782; A31783 REFERENCE A31782 !$#authors Sakoda, S.; Shanske, S.; DiMauro, S.; Schon, E.A. !$#journal J. Biol. Chem. (1988) 263:16899-16905 !$#title Isolation of a cDNA encoding the B isozyme of human !1phosphoglycerate mutase (PGAM) and characterization of the !1PGAM gene family. !$#cross-references MUID:89034186; PMID:2846553 !$#accession A31782 !'##molecule_type mRNA !'##residues 1-254 ##label SAK !'##cross-references GB:J04173; NID:g551173; PIDN:AAA60071.1; !1PID:g551174 REFERENCE A31783 !$#authors Blouquit, Y.; Calvin, M.C.; Rosa, R.; Prome, D.; Prome, !1J.C.; Pratbernou, F.; Cohen-Solal, M.; Rosa, J. !$#journal J. Biol. Chem. (1988) 263:16906-16910 !$#title Sequence of the human erythrocyte phosphoglycerate mutase by !1microsequencer and mass spectrometry. !$#cross-references MUID:89034187; PMID:2846554 !$#accession A31783 !'##molecule_type protein !'##residues 2-254 ##label BLO COMMENT This enzyme catalyzes the interconversion of !12-phosphoglycerate and 3-phosphoglycerate, using 2, !13-bisphosphoglycerate as a cofactor. It also has two !1additional minor activities: the synthesis of 2, !13-bisphosphoglycerate (bisphosphoglycerate synthase, EC !15.4.2.4) and its degradation (bisphosphoglycerate !1phosphatase, EC 3.1.3.13). COMMENT Two isozyme chains exists in mammals: a muscle-specific !1form, M, and a non-muscle-specific (or brain) form, B. Thus !1three types of functional dimers may be found in mammalian !1tissues: MM mainly in muscle; BB mainly in liver, kidney, !1and brain; and MB (with varying proportion of the MM and BB) !1mainly in the heart. GENETICS !$#gene GDB:PGAM1; PGAMA !'##cross-references GDB:120530; OMIM:172250 !$#map_position 10q25.3-10q25.3 CLASSIFICATION #superfamily phosphoglycerate mutase; phosphoglycerate !1mutase homology KEYWORDS dimer; gluconeogenesis; glycolysis; intramolecular !1transferase; isomerase; phosphohistidine; phosphoprotein; !1phosphoric monoester hydrolase FEATURE !$2-254 #product phosphoglycerate mutase #status experimental !8#label MAT\ !$6-221 #domain phosphoglycerate mutase homology #label PGMH\ !$10,62,186 #active_site Arg, Arg, His #status predicted\ !$11 #active_site His (phosphohistidine intermediate) !8#status predicted SUMMARY #length 254 #molecular-weight 28804 #checksum 2353 SEQUENCE /// ENTRY PMHUYM #type complete TITLE phosphoglycerate mutase (EC 5.4.2.1) M - human ALTERNATE_NAMES phosphoglycerate mutase 2; phosphoglycerate mutase muscle isozyme; phosphoglycerate phosphomutase; phosphoglyceromutase ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 18-Jun-1999 ACCESSIONS JQ0750; A34344; A29482 REFERENCE JQ0750 !$#authors Castella-Escola, J.; Ojcius, D.M.; LeBoulch, P.; Joulin, V.; !1Blouquit, Y.; Garel, M.C.; Valentin, C.; Rosa, R.; !1Climent-Romeo, F.; Cohen-Solal, M. !$#journal Gene (1990) 91:225-232 !$#title Isolation and characterization of the gene encoding the !1muscle-specific isozyme of human phosphoglycerate mutase. !$#cross-references MUID:91007279; PMID:2145198 !$#accession JQ0750 !'##molecule_type mRNA !'##residues 1-253 ##label SHA !'##cross-references GB:M55674; GB:M25818; NID:g189870; PIDN:AAA64238.1; !1PID:g189872 REFERENCE A34344 !$#authors Tsujino, S.; Sakoda, S.; Mizuno, R.; Kobayashi, T.; Suzuki, !1T.; Kishimoto, S.; Shanske, S.; DiMauro, S.; Schon, E.A. !$#journal J. Biol. Chem. (1989) 264:15334-15337 !$#title Structure of the gene encoding the muscle-specific subunit !1of human phosphoglycerate mutase. !$#cross-references MUID:89359363; PMID:2549058 !$#accession A34344 !'##molecule_type mRNA !'##residues 1-53,55-64,'P',66-86,'F',88-253 ##label TSU !'##cross-references GB:J05073 REFERENCE A29482 !$#authors Shanske, S.; Sakoda, S.; Hermodson, M.A.; DiMauro, S.; !1Schon, E.A. !$#journal J. Biol. Chem. (1987) 262:14612-14617 !$#title Isolation of a cDNA encoding the muscle-specific subunit of !1human phosphoglycerate mutase. !$#cross-references MUID:88033014; PMID:2822696 !$#accession A29482 !'##molecule_type mRNA !'##residues 1-13,'T',15-86,'F',88-97,'F',99-112,'RS',115-253 ##label !1SHA2 !'##cross-references GB:M18172; NID:g189867; PIDN:AAA60072.1; !1PID:g189868 COMMENT This enzyme catalyzes the interconversion of !12-phosphoglycerate and 3-phosphoglycerate, using 2, !13-bisphosphoglycerate as a cofactor. It also possesses two !1additional minor activities: the synthesis of 2, !13-bisphosphoglycerate (bisphosphoglycerate synthase, EC !15.4.2.4) and its degradation (bisphosphoglycerate !1phosphatase, EC 3.1.3.13). COMMENT Two isozyme chains exists in mammals: a muscle-specific !1form, M, and a non-muscle-specific (or brain) form, B. Thus !1three types of functional dimers may be found in mammalian !1tissues: MM mainly in muscle; BB mainly in liver, kidney, !1and brain; and MB (with varying proportion of the MM and BB) !1mainly in the heart. GENETICS !$#gene GDB:PGAM2 !'##cross-references GDB:120280; OMIM:261670 !$#map_position 7p13-7p12 CLASSIFICATION #superfamily phosphoglycerate mutase; phosphoglycerate !1mutase homology KEYWORDS dimer; gluconeogenesis; glycolysis; intramolecular !1transferase; isomerase; phosphohistidine; phosphoprotein; !1phosphoric monoester hydrolase FEATURE !$2-253 #product phosphoglycerate mutase #status predicted !8#label MAT\ !$6-221 #domain phosphoglycerate mutase homology #label PGMH\ !$10,62,186 #active_site Arg, Arg, His #status predicted\ !$11 #active_site His (phosphohistidine intermediate) !8#status predicted SUMMARY #length 253 #molecular-weight 28766 #checksum 1283 SEQUENCE /// ENTRY PMRTYM #type complete TITLE phosphoglycerate mutase (EC 5.4.2.1) M - rat ALTERNATE_NAMES phosphoglycerate phosphomutase; phosphoglyceromutase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 18-Jun-1999 ACCESSIONS A33793; S33177 REFERENCE A33793 !$#authors Castella-Escola, J.; Montoliu, L.; Pons, G.; Puigdomenech, !1P.; Cohen-Solal, M.; Carreras, J.; Rigau, J.; Climent, F. !$#journal Biochem. Biophys. Res. Commun. (1989) 165:1345-1351 !$#title Sequence of rat skeletal muscle phosphoglycerate mutase !1cDNA. !$#cross-references MUID:90121247; PMID:2558656 !$#accession A33793 !'##molecule_type mRNA !'##residues 1-253 ##label CAS !'##cross-references GB:M31835; NID:g206102; PIDN:AAA41835.1; !1PID:g206103 !'##note the authors translated the codon CAC for residue 91 as Ala REFERENCE S33177 !$#authors Ruiz, P.; Gualberto, A.; Perez de la Osa, P.; de Lecea, L.; !1Climent, F.; Walsh, K.; Pons, G. !$#submission submitted to the EMBL Data Library, October 1992 !$#accession S33177 !'##status preliminary !'##molecule_type DNA !'##residues 1-253 ##label RUI !'##cross-references EMBL:Z17319; NID:g297110; PIDN:CAA78967.1; !1PID:g297111 COMMENT This enzyme catalyzes the interconversion of !12-phosphoglycerate and 3-phosphoglycerate, using 2, !13-bisphosphoglycerate as a cofactor. It also possesses two !1additional minor activities: the synthesis of 2, !13-bisphosphoglycerate (bisphosphoglycerate synthase, EC !15.4.2.4) and its degradation (bisphosphoglycerate !1phosphatase, EC 3.1.3.13). COMMENT Two isozyme chains exists in mammals: a muscle-specific !1form, M, and a non-muscle-specific (or brain) form, B. Thus !1three types of functional dimers may be found in mammalian !1tissues: MM mainly in muscle; BB mainly in liver, kidney, !1and brain; and MB (with varying proportion of the MM and BB) !1mainly in the heart. CLASSIFICATION #superfamily phosphoglycerate mutase; phosphoglycerate !1mutase homology KEYWORDS dimer; gluconeogenesis; glycolysis; intramolecular !1transferase; isomerase; phosphohistidine; phosphoprotein; !1phosphoric monoester hydrolase FEATURE !$2-253 #product phosphoglycerate mutase #status predicted !8#label MAT\ !$6-221 #domain phosphoglycerate mutase homology #label PGMH\ !$10,62,186 #active_site Arg, Arg, His #status predicted\ !$11 #active_site His (phosphohistidine intermediate) !8#status predicted SUMMARY #length 253 #molecular-weight 28755 #checksum 1438 SEQUENCE /// ENTRY PMBYY #type complete TITLE phosphoglycerate mutase (EC 5.4.2.1) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES phosphoglycerate phosphomutase; phosphoglyceromutase; protein YKL152c; protein YKL607 ORGANISM #formal_name Saccharomyces cerevisiae DATE 14-Nov-1983 #sequence_revision 31-Mar-1991 #text_change 16-Jun-2000 ACCESSIONS S00358; S19050; S37798; S37982; S44575; A01176; S20185; !1S43210 REFERENCE S00358 !$#authors White, M.F.; Fothergill-Gilmore, L.A. !$#journal FEBS Lett. (1988) 229:383-387 !$#title Sequence of the gene encoding phosphoglycerate mutase from !1Saccharomyces cerevisiae. !$#cross-references MUID:88152269; PMID:2831102 !$#accession S00358 !'##molecule_type DNA !'##residues 1-247 ##label WHI !'##cross-references EMBL:X06408; NID:g3746; PIDN:CAA29698.1; !1PID:g1326042 REFERENCE S19050 !$#authors Heinisch, J.; von Borstel, R.C.; Rodicio, R. !$#journal Curr. Genet. (1991) 20:167-171 !$#title Sequence and localization of the gene encoding yeast !1phosphoglycerate mutase. !$#cross-references MUID:92035064; PMID:1834353 !$#accession S19050 !'##molecule_type DNA !'##residues 1-247 ##label HEI !'##cross-references EMBL:X58789; NID:g3748; PIDN:CAA41595.1; PID:g3749 REFERENCE S37786 !$#authors Vandenbol, M.; Bolle, P.; Dion, C.; Portetelle, D.; Hilger, !1F. !$#submission submitted to the EMBL Data Library, September 1993 !$#description DNA sequencing of a 36.2 kb fragment located between the !1FAS1 and LAP4 loci of chromosome XI of S. cerevisiae. !$#accession S37798 !'##molecule_type DNA !'##residues 1-247 ##label VAN !'##cross-references EMBL:Z26877; NID:g407482; PIDN:CAA81501.1; !1PID:g407495 !'##experimental_source strain S288C REFERENCE S37976 !$#authors Vandenbol, M.; Bolle, P.A.; Dion, C.; Portetelle, D.; !1Hilger, F. !$#submission submitted to the Protein Sequence Database, March 1994 !$#accession S37982 !'##molecule_type DNA !'##residues 1-247 ##label VA2 !'##cross-references EMBL:Z28152; NID:g486263; PIDN:CAA81994.1; !1PID:g486265; GSPDB:GN00011; MIPS:YKL152c !'##experimental_source strain S288C REFERENCE S44563 !$#authors Vandenbol, M.; Bolle, P.A.; Dion, C.; Portetelle, D.; !1Hilger, F. !$#journal Yeast (1994) 10:35-40 !$#title DNA sequencing of a 36.2 kb fragment located between the !1FAS1 and LAP4 loci of chromosome XI of Saccharomyces !1cerevisiae. !$#accession S44575 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-247 ##label VA3 !'##cross-references EMBL:Z26877; NID:g407482; PIDN:CAA81501.1; !1PID:g407495 !'##experimental_source strain S288C !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1September 1993 REFERENCE A01176 !$#authors Fothergill, L.A.; Harkins, R.N. !$#journal Proc. R. Soc. Lond. B Biol. Sci. (1982) 215:19-44 !$#title The amino acid sequence of yeast phosphoglycerate mutase. !$#cross-references MUID:83039464; PMID:6127696 !$#accession A01176 !'##molecule_type protein !'##residues 2-46,'G',48,'NVL',52,'D',54-93,'E',95-99,'Q',101-169,172, !1'V',174-176,'S',178-207,'P',209,'TI',212-234,237,239-244, !1246-247,'G' ##label FOT REFERENCE A37515 !$#authors Winn, S.I.; Warwicker, J.I.; Watson, H.C. !$#citation unpublished results, cited by Winn, S.I., Watson, H.C., !1Harkins, R.N., and Fothergill, L.A., Phil. Trans. Royal Soc. !1London B 293, 121-130, 1981 !$#contents annotation; X-ray crystallography, 2.8 angstroms GENETICS !$#gene SGD:GPM1; MIPS:YKL152c !'##cross-references SGD:S0001635; MIPS:YKL152c !$#map_position 11L FUNCTION !$#description catalyzes the interconversion of 2-phosphoglycerate and !13-phosphoglycerate, using 2,3-bisphosphoglycerate as !1cofactor CLASSIFICATION #superfamily phosphoglycerate mutase; phosphoglycerate !1mutase homology KEYWORDS gluconeogenesis; glycolysis; homotetramer; intramolecular !1transferase; isomerase; phosphohistidine; phosphoprotein FEATURE !$2-247 #product phosphoglycerate mutase #status experimental !8#label MAT\ !$4-217 #domain phosphoglycerate mutase homology #label PGMH\ !$8,60,182 #active_site Arg, Arg, His #status experimental\ !$9 #active_site His (phosphohistidine intermediate) !8#status experimental SUMMARY #length 247 #molecular-weight 27608 #checksum 9564 SEQUENCE /// ENTRY PMHUBM #type complete TITLE bisphosphoglycerate mutase (EC 5.4.2.4) - human ALTERNATE_NAMES bisphosphoglycerate synthase; diphosphoglycerate mutase; glycerate phosphomutase ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 18-Jun-1999 ACCESSIONS A31999; A24895; A61586; A45482 REFERENCE A31999 !$#authors Joulin, V.; Garel, M.C.; Le Boulch, P.; Valentin, C.; Rosa, !1R.; Rosa, J.; Cohen-Solal, M. !$#journal J. Biol. Chem. (1988) 263:15785-15790 !$#title Isolation and characterization of the human 2, !13-bisphosphoglycerate mutase gene. !$#cross-references MUID:89008494; PMID:2844822 !$#accession A31999 !'##molecule_type DNA !'##residues 1-259 ##label JOU !'##cross-references GB:M23066; GB:M23067; GB:M23068; NID:g179525; !1PIDN:AAA51840.1; PID:g179527; GB:J04059 REFERENCE A24895 !$#authors Joulin, V.; Peduzzi, J.; Romeo, P.H.; Rosa, R.; Valentin, !1C.; Dubart, A.; Lapeyre, B.; Blouquit, Y.; Garel, M.C.; !1Goossens, M.; Rosa, J.; Cohen-Solal, M. !$#journal EMBO J. (1986) 5:2275-2283 !$#title Molecular cloning and sequencing of the human erythrocyte 2, !13-bisphosphoglycerate mutase cDNA: revised amino acid !1sequence. !$#cross-references MUID:87053869; PMID:3023066 !$#accession A24895 !'##molecule_type mRNA !'##residues 1-259 ##label JO2 !'##cross-references GB:X04327; NID:g29480; PIDN:CAA27858.1; PID:g29481 REFERENCE A61586 !$#authors Cohen-Solal, M.; Joulin, V.; Romeo, P.H.; Rosa, R.; !1Valentin, C.; Garel, M.C.; Rosa, J. !$#journal Biomed. Biochim. Acta (1987) 46:S126-S130 !$#title Molecular cloning of the human 2,3-bisphosphoglycerate !1mutase cDNA and revised amino acid sequence. !$#cross-references MUID:87241420; PMID:3036106 !$#accession A61586 !'##molecule_type mRNA !'##residues 1-259 ##label COH REFERENCE A45482 !$#authors Stafforini, D.M.; Rollins, E.N.; Prescott, S.M.; McIntyre, !1T.M. !$#journal J. Biol. Chem. (1993) 268:3857-3865 !$#title The platelet-activating factor acetylhydrolase from human !1erythrocytes. Purification and properties. !$#cross-references MUID:93179380; PMID:8440681 !$#accession A45482 !'##molecule_type protein !'##residues 104-114 ##label STA COMMENT This erythrocyte-specific enzyme plays a major role in !1regulating hemoglobin oxygen affinity as a consequence of !1controlling 2,3-bisphosphoglycerate concentration. It can !1also catalyze the reaction of phosphoglycerate mutase (EC !15.4.2.1) and bisphosphoglycerate phosphatase (EC 3.1.3.13) !1but with a reduced activity. GENETICS !$#gene GDB:BPGM !'##cross-references GDB:119039; OMIM:222800 !$#map_position 7q31-7q34 !$#introns 201/1 CLASSIFICATION #superfamily phosphoglycerate mutase; phosphoglycerate !1mutase homology KEYWORDS erythroid differentiation; homodimer; intramolecular !1transferase; isomerase; phosphohistidine; phosphoprotein; !1phosphoric monoester hydrolase FEATURE !$6-223 #domain phosphoglycerate mutase homology #label PGMH\ !$10,62,188 #active_site Arg, Arg, His #status predicted\ !$11 #active_site His (phosphohistidine intermediate) !8#status predicted SUMMARY #length 259 #molecular-weight 30005 #checksum 9638 SEQUENCE /// ENTRY PMRBBM #type complete TITLE bisphosphoglycerate mutase (EC 5.4.2.4) - rabbit ALTERNATE_NAMES bisphosphoglycerate synthase; diphosphoglycerate mutase; glycerate phosphomutase ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 18-Jun-1999 ACCESSIONS A24973 REFERENCE A24973 !$#authors Yanagawa, S.; Hitomi, K.; Sasaki, R.; Chiba, H. !$#journal Gene (1986) 44:185-191 !$#title Isolation and characterization of cDNA encoding rabbit !1reticulocyte 2,3-bisphosphoglycerate synthase. !$#cross-references MUID:87055234; PMID:3023182 !$#accession A24973 !'##molecule_type mRNA !'##residues 1-259 ##label YAN !'##cross-references GB:M15884; NID:g165000; PIDN:AAA31240.1; !1PID:g165001 !'##experimental_source reticulocyte COMMENT This erythrocyte-specific enzyme plays a major role in !1regulating hemoglobin oxygen affinity as a consequence of !1controlling 2,3-bisphosphoglycerate concentration. It can !1also catalyze the reaction of phosphoglycerate mutase (EC !15.4.2.1) and bisphosphoglycerate phosphatase (EC 3.1.3.13) !1but with a reduced activity. CLASSIFICATION #superfamily phosphoglycerate mutase; phosphoglycerate !1mutase homology KEYWORDS erythrocyte; erythroid differentiation; homodimer; !1intramolecular transferase; isomerase; phosphohistidine; !1phosphoprotein; phosphoric monoester hydrolase FEATURE !$6-223 #domain phosphoglycerate mutase homology #label PGMH\ !$10,62,188 #active_site Arg, Arg, His #status predicted\ !$11 #active_site His (phosphohistidine intermediate) !8#status predicted SUMMARY #length 259 #molecular-weight 30030 #checksum 9344 SEQUENCE /// ENTRY PMMSBM #type complete TITLE bisphosphoglycerate mutase (EC 5.4.2.4) - mouse ALTERNATE_NAMES bisphosphoglycerate synthase; diphosphoglycerate mutase; glycerate phosphomutase ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 18-Jun-1999 ACCESSIONS A31585 REFERENCE A31585 !$#authors Le Boulch, P.; Joulin, V.; Garel, M.C.; Rosa, J.; !1Cohen-Solal, M. !$#journal Biochem. Biophys. Res. Commun. (1988) 156:874-881 !$#title Molecular cloning and nucleotide sequence of murine 2, !13-bisphosphoglycerate mutase cDNA. !$#cross-references MUID:89050120; PMID:2847721 !$#accession A31585 !'##molecule_type mRNA !'##residues 1-259 ##label LEB !'##cross-references GB:X13586; NID:g50183; PIDN:CAA31927.1; PID:g50184 COMMENT This erythrocyte-specific enzyme plays a major role in !1regulating hemoglobin oxygen affinity as a consequence of !1controlling 2,3-bisphosphoglycerate concentration. It can !1also catalyze the reaction of phosphoglycerate mutase (EC !15.4.2.1) and bisphosphoglycerate phosphatase (EC 3.1.3.13) !1but with a reduced activity. CLASSIFICATION #superfamily phosphoglycerate mutase; phosphoglycerate !1mutase homology KEYWORDS erythroid differentiation; homodimer; intramolecular !1transferase; isomerase; phosphohistidine; phosphoprotein; !1phosphoric monoester hydrolase FEATURE !$6-223 #domain phosphoglycerate mutase homology #label PGMH\ !$10,62,188 #active_site Arg, Arg, His #status predicted\ !$11 #active_site His (phosphohistidine intermediate) !8#status predicted SUMMARY #length 259 #molecular-weight 29978 #checksum 9250 SEQUENCE /// ENTRY G65132 #type complete TITLE hypothetical 44.6 kD protein in cysG-trpS intergenic region - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS G65132 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65132 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-408 ##label BLAT !'##cross-references GB:AE000413; GB:U00096; NID:g2367215; !1PIDN:AAC76405.1; PID:g1789781; UWGP:b3380 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yhfW CLASSIFICATION #superfamily phosphopentomutase SUMMARY #length 408 #molecular-weight 44559 #checksum 4055 SEQUENCE /// ENTRY C64667 #type complete TITLE phosphopentomutase - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C64667 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession C64667 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-413 ##label TOM !'##cross-references GB:AE000623; GB:AE000511; NID:g2314327; !1PIDN:AAD08223.1; PID:g2314336; TIGR:HP1179 CLASSIFICATION #superfamily phosphopentomutase SUMMARY #length 413 #molecular-weight 46179 #checksum 5270 SEQUENCE /// ENTRY A41801 #type complete TITLE phosphoglucomutase (EC 5.4.2.2) 1 - human ALTERNATE_NAMES PGM1 ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1993 #sequence_revision 19-May-1994 #text_change 18-Jun-1999 ACCESSIONS A41801 REFERENCE A41801 !$#authors Whitehouse, D.B.; Putt, W.; Lovegrove, J.U.; Morrison, K.; !1Hollyoake, M.; Fox, M.F.; Hopkinson, D.A.; Edwards, Y.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:411-415 !$#title Phosphoglucomutase 1: complete human and rabbit mRNA !1sequences and direct mapping of this highly polymorphic !1marker on human chromosome 1. !$#cross-references MUID:92108065; PMID:1530890 !$#accession A41801 !'##molecule_type mRNA !'##residues 1-562 ##label WHI !'##cross-references GB:M83088; NID:g189925; PIDN:AAA60080.1; !1PID:g189926 !'##note sequence extracted from NCBI backbone (NCBIN:75120, !1NCBIP:75121) COMMENT This enzyme interconverts glucose-1-phosphate and !1glucose-6-phosphate, participating in both the breakdown and !1synthesis of glucose. COMMENT This protein is a major substrate for Ca++/ !1calmodulin-dependent protein kinase. GENETICS !$#gene GDB:PGM1 !'##cross-references GDB:119489; OMIM:171900 !$#map_position 1p31-1p31 !$#note locus is highly polymorphic CLASSIFICATION #superfamily phosphoglucomutase KEYWORDS intramolecular transferase; isomerase; magnesium; monomer; !1phosphoprotein; skeletal muscle FEATURE !$2-562 #product phosphoglucomutase 1 #status predicted !8#label MAT\ !$117 #active_site Ser (phosphoserine intermediate) #status !8predicted\ !$185 #binding_site phosphate (Thr) (covalent) (by !8calmodulin-dependent kinase) #status predicted\ !$408 #binding_site phosphate (Ser) (covalent) (by !8calmodulin-dependent kinase) #status predicted\ !$460 #binding_site phosphate (Ser) (covalent) (by !8calmodulin-dependent kinase) #status predicted\ !$467 #binding_site phosphate (Thr) (covalent) (by !8calmodulin-dependent kinase) #status predicted SUMMARY #length 562 #molecular-weight 61369 #checksum 5808 SEQUENCE /// ENTRY PMRB #type complete TITLE phosphoglucomutase (EC 5.4.2.2) 1, short splice form - rabbit ALTERNATE_NAMES PGM1; sarcoplasmic reticulum-associated phosphoglucomutase; SR-PGM ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 03-Aug-1984 #sequence_revision 19-May-1994 #text_change 18-Jun-1999 ACCESSIONS B41801; B45077; A01175; B60810 REFERENCE A41801 !$#authors Whitehouse, D.B.; Putt, W.; Lovegrove, J.U.; Morrison, K.; !1Hollyoake, M.; Fox, M.F.; Hopkinson, D.A.; Edwards, Y.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:411-415 !$#title Phosphoglucomutase 1: complete human and rabbit mRNA !1sequences and direct mapping of this highly polymorphic !1marker on human chromosome 1. !$#cross-references MUID:92108065; PMID:1530890 !$#accession B41801 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-562 ##label WHI REFERENCE A45077 !$#authors Lee, Y.S.; Marks, A.R.; Gureckas, N.; Lacro, R.; !1Nadal-Ginard, B.; Kim, D.H. !$#journal J. Biol. Chem. (1992) 267:21080-21088 !$#title Purification, characterization, and molecular cloning of a !160-kDa phosphoprotein in rabbit skeletal sarcoplasmic !1reticulum which is an isoform of phosphoglucomutase. !$#cross-references MUID:93016027; PMID:1328221 !$#accession B45077 !'##molecule_type mRNA !'##residues 1-562 ##label LEE !'##cross-references GB:M97664; NID:g165663; PIDN:AAA31454.1; !1PID:g165664 !'##experimental_source skeletal muscle !'##note authors translated the codon GAG for residue 436 as Gln and CAG !1for residue 530 as Glu !'##note these authors refer to this form as isoform 2 or PGM2 REFERENCE A92435 !$#authors Ray Jr., W.J.; Hermodson, M.A.; Puvathingal, J.M.; Mahoney, !1W.C. !$#journal J. Biol. Chem. (1983) 258:9166-9174 !$#title The complete amino acid sequence of rabbit muscle !1phosphoglucomutase. !$#cross-references MUID:83265705; PMID:6223925 !$#accession A01175 !'##molecule_type protein !'##residues 2-562 ##label RAY REFERENCE A60810 !$#authors Yuen, S.; Hunkapiller, M.W.; Wilson, K.J.; Yuan, P.M. !$#journal Anal. Biochem. (1988) 168:5-15 !$#title Applications of tandem microbore liquid chromatography and !1sodium dodecyl sulfate-polyacrylamide gel electrophoresis/ !1electroblotting in microsequence analysis. !$#cross-references MUID:88207910; PMID:3364717 !$#accession B60810 !'##molecule_type protein !'##residues 2-21 ##label YUE REFERENCE A90241 !$#authors Milstein, C.P.; Milstein, C. !$#journal Biochem. J. (1968) 109:93-99 !$#title A tryptic peptide containing a unique serine phosphate !1residue in rabbit phosphoglucomutase. !$#cross-references MUID:68368401; PMID:5669853 !$#contents annotation; active site COMMENT This enzyme interconverts glucose-1-phosphate and !1glucose-6-phosphate, participating in both the breakdown and !1synthesis of glucose. COMMENT This protein is a major substrate for Ca++/ !1calmodulin-dependent protein kinase. CLASSIFICATION #superfamily phosphoglucomutase KEYWORDS alternative splicing; intramolecular transferase; isomerase; !1magnesium; monomer; phosphoprotein; skeletal muscle FEATURE !$2-562 #product phosphoglucomutase 1, short splice form !8#status experimental #label MAT\ !$117 #active_site Ser (phosphoserine intermediate) #status !8experimental\ !$185 #binding_site phosphate (Thr) (covalent) (by !8calmodulin-dependent kinase) #status predicted\ !$408 #binding_site phosphate (Ser) (covalent) (by !8calmodulin-dependent kinase) #status predicted\ !$460 #binding_site phosphate (Ser) (covalent) (by !8calmodulin-dependent kinase) #status predicted\ !$467 #binding_site phosphate (Thr) (covalent) (by !8calmodulin-dependent kinase) #status predicted SUMMARY #length 562 #molecular-weight 61558 #checksum 5088 SEQUENCE /// ENTRY PMRT #type complete TITLE phosphoglucomutase (EC 5.4.2.2) 1 - rat ALTERNATE_NAMES PGM1 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 19-May-1994 #sequence_revision 02-Jun-1994 #text_change 18-Jun-1999 ACCESSIONS JC2011 REFERENCE JC2011 !$#authors Rivera, A.A.; Elton, T.S.; Dey, N.B.; Bounelis, P.; !1Marchase, R.B. !$#journal Gene (1993) 133:261-266 !$#title Isolation and expression of a rat liver cDNA encoding !1phosphoglucomutase. !$#cross-references MUID:94040821; PMID:8224913 !$#accession JC2011 !'##molecule_type mRNA !'##residues 1-562 ##label RIV !'##cross-references GB:L11694; NID:g393212; PIDN:AAA16862.1; !1PID:g393213 !'##experimental_source liver !'##note the authors translated the codon GAC for residue 62 as Cys COMMENT This enzyme interconverts glucose-1-phosphate and !1glucose-6-phosphate, participating in both the breakdown and !1synthesis of glucose. COMMENT This protein is a major substrate for Ca++/ !1calmodulin-dependent protein kinase. CLASSIFICATION #superfamily phosphoglucomutase KEYWORDS intramolecular transferase; isomerase; magnesium; monomer; !1phosphoprotein; skeletal muscle FEATURE !$2-562 #product phosphoglucomutase 1 #status predicted !8#label MAT\ !$117 #active_site Ser (phosphoserine intermediate) #status !8predicted\ !$185 #binding_site phosphate (Thr) (covalent) (by !8calmodulin-dependent kinase) #status predicted\ !$460 #binding_site phosphate (Ser) (covalent) (by !8calmodulin-dependent kinase) #status predicted\ !$467 #binding_site phosphate (Thr) (covalent) (by !8calmodulin-dependent kinase) #status predicted SUMMARY #length 562 #molecular-weight 61403 #checksum 4414 SEQUENCE /// ENTRY PMRBI #type complete TITLE phosphoglucomutase (EC 5.4.2.2) 1, long splice form - rabbit ALTERNATE_NAMES PGM1 ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 17-Feb-1994 #sequence_revision 02-Jun-1994 #text_change 18-Jun-1999 ACCESSIONS A45077 REFERENCE A45077 !$#authors Lee, Y.S.; Marks, A.R.; Gureckas, N.; Lacro, R.; !1Nadal-Ginard, B.; Kim, D.H. !$#journal J. Biol. Chem. (1992) 267:21080-21088 !$#title Purification, characterization, and molecular cloning of a !160-kDa phosphoprotein in rabbit skeletal sarcoplasmic !1reticulum which is an isoform of phosphoglucomutase. !$#cross-references MUID:93016027; PMID:1328221 !$#accession A45077 !'##molecule_type mRNA !'##residues 1-566 ##label LEE !'##cross-references GB:M97663; NID:g165661; PIDN:AAA31453.1; !1PID:g165662 !'##experimental_source skeletal muscle !'##note authors translated the codon GAG for residue 440 as Gln and CAG !1for residue 534 as Glu !'##note these authors refer to this form as isoform 1 or PGM1 COMMENT This enzyme interconverts glucose-1-phosphate and !1glucose-6-phosphate, participating in both the breakdown and !1synthesis of glucose. CLASSIFICATION #superfamily phosphoglucomutase KEYWORDS alternative splicing; intramolecular transferase; isomerase; !1magnesium; monomer; phosphoprotein FEATURE !$6-566 #product phosphoglucomutase 1, long splice form !8#status predicted #label MAT\ !$121 #active_site Ser (phosphoserine intermediate) #status !8predicted\ !$189 #binding_site phosphate (Thr) (covalent) (by !8calmodulin-dependent kinase) #status predicted\ !$412 #binding_site phosphate (Ser) (covalent) (by !8calmodulin-dependent kinase) #status predicted\ !$464 #binding_site phosphate (Ser) (covalent) (by !8calmodulin-dependent kinase) #status predicted\ !$471 #binding_site phosphate (Thr) (covalent) (by !8calmodulin-dependent kinase) #status predicted SUMMARY #length 566 #molecular-weight 62192 #checksum 1576 SEQUENCE /// ENTRY S50973 #type complete TITLE 3,4-dihydroxy-2-butanone 4-phosphate synthase (EC 5.4.99.-) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES DBP synthase; protein YDR487c ORGANISM #formal_name Saccharomyces cerevisiae DATE 21-May-1999 #sequence_revision 21-May-1999 #text_change 23-Mar-2001 ACCESSIONS S50973; S69654 REFERENCE S50973 !$#authors Garcia-Ramirez, J.J.; Santos, M.A.; Revuelta, J.L. !$#submission submitted to the EMBL Data Library, February 1993 !$#description Cloning and sequencing of the RIB3 gene from Saccharomyces !1cerevisiae. !$#accession S50973 !'##molecule_type DNA !'##residues 1-208 ##label GAR !'##cross-references EMBL:Z21619; NID:g642222; PIDN:CAA79743.1; !1PID:g642223 REFERENCE S69554 !$#authors Dietrich, F.S. !$#submission submitted to the EMBL Data Library, August 1995 !$#description The sequence of S. cerevisiae cosmids 9410, 8035, 8166, and !19787. !$#accession S69654 !'##molecule_type DNA !'##residues 1-208 ##label DIE !'##cross-references EMBL:U33050; NID:g927726; PIDN:AAB64927.1; !1PID:g927755; GSPDB:GN00004; MIPS:YDR487c GENETICS !$#gene SGD:RIB3; MIPS:YDR487c !'##cross-references SGD:S0002895; MIPS:YDR487c !$#map_position 4R CLASSIFICATION #superfamily 3,4-dihydroxy-2-butanone 4-phosphate synthase; !13,4-dihydroxy-2-butanone 4-phosphate synthase homology KEYWORDS heat shock; intramolecular transferase; isomerase; !1riboflavin biosynthesis; stress-induced protein FEATURE !$8-206 #domain 3,4-dihydroxy-2-butanone 4-phosphate synthase !8homology #label HBPS SUMMARY #length 208 #molecular-weight 22567 #checksum 8399 SEQUENCE /// ENTRY A38159 #type complete TITLE 3,4-dihydroxy-2-butanone 4-phosphate synthase (EC 5.4.99.-) [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES luxH protein homolog htrP ORGANISM #formal_name Escherichia coli DATE 21-May-1999 #sequence_revision 21-May-1999 #text_change 01-Mar-2002 ACCESSIONS A38159; S22364; A41888; G65091; S24622 REFERENCE A38159 !$#authors Raina, S.; Mabey, L.; Georgopoulos, C. !$#journal J. Bacteriol. (1991) 173:5999-6008 !$#title The Escherichia coli htrP gene product is essential for !1bacterial growth at high temperatures: mapping, cloning, !1sequencing, and transcriptional regulation of htrP. !$#cross-references MUID:92011356; PMID:1917833 !$#accession A38159 !'##molecule_type DNA !'##residues 1-252 ##label RAI !'##cross-references GB:M64472; NID:g146417; PIDN:AAA23996.1; !1PID:g146418 !'##note the authors translated the codon GTT for residue 66 as Gly REFERENCE S22360 !$#authors Yang, T.P.; Depew, R.E. !$#journal Biochim. Biophys. Acta (1992) 1130:227-228 !$#title Nucleotide sequence of a region duplicated in Escherichia !1coli toc mutants. !$#cross-references MUID:92223101; PMID:1314093 !$#accession S22364 !'##status translation not shown !'##molecule_type DNA !'##residues 1-119,'AAIA',123-209,'AHER',214,'AS' ##label YAN !'##cross-references EMBL:M77129; NID:g146676; PIDN:AAA71879.1; !1PID:g455174 !'##experimental_source strain RED44 REFERENCE A41888 !$#authors Richter, G.; Volk, R.; Krieger, C.; Lahm, H.W.; !1Rothlisberger, U.; Bacher, A. !$#journal J. Bacteriol. (1992) 174:4050-4056 !$#title Biosynthesis of riboflavin: cloning, sequencing, and !1expression of the gene coding for 3,4-dihydroxy-2-butanone !14-phosphate synthase of Escherichia coli. !$#cross-references MUID:92283761; PMID:1597419 !$#accession A41888 !'##molecule_type DNA !'##residues 1-119,'AAIA',123-209,'AHER',214,'AS' ##label RI2 !'##cross-references EMBL:X66720; NID:g49099; PIDN:CAA47252.1; !1PID:g49100 !'##experimental_source RR28 !'##note sequence extracted from NCBI backbone (NCBIP:106028) REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65091 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-119,'AAIA',123-209,'AHER',214,'AS' ##label BLAT !'##cross-references GB:AE000386; GB:U00096; NID:g2367187; !1PIDN:AAC76077.1; PID:g1789420; UWGP:b3041 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ribB; luxH !$#map_position 66 min FUNCTION !$#description catalyzes the formation of L-3,4-dihydroxy-2-butanone !14-phosphate from D-ribulose 5-phosphate [validated, !1MUID:92283761] !$#pathway riboflavin biosynthesis CLASSIFICATION #superfamily 3,4-dihydroxy-2-butanone 4-phosphate synthase; !13,4-dihydroxy-2-butanone 4-phosphate synthase homology KEYWORDS heat shock; intramolecular transferase; isomerase; !1riboflavin biosynthesis; stress-induced protein FEATURE !$19-208 #domain 3,4-dihydroxy-2-butanone 4-phosphate synthase !8homology #label HBPS SUMMARY #length 252 #molecular-weight 27471 #checksum 801 SEQUENCE /// ENTRY E64091 #type complete TITLE 3,4-dihydroxy-2-butanone 4-phosphate synthase (EC 5.4.99.-) - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 21-May-1999 #sequence_revision 21-May-1999 #text_change 18-Jun-1999 ACCESSIONS E64091 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession E64091 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-215 ##label TIGR !'##cross-references GB:U32760; GB:L42023; NID:g1573764; !1PIDN:AAC22422.1; PID:g1573772; TIGR:HI0764 CLASSIFICATION #superfamily 3,4-dihydroxy-2-butanone 4-phosphate synthase; !13,4-dihydroxy-2-butanone 4-phosphate synthase homology KEYWORDS heat shock; intramolecular transferase; isomerase; !1riboflavin biosynthesis; stress-induced protein FEATURE !$20-210 #domain 3,4-dihydroxy-2-butanone 4-phosphate synthase !8homology #label HBPS SUMMARY #length 215 #molecular-weight 23254 #checksum 5965 SEQUENCE /// ENTRY C35081 #type complete TITLE 3,4-dihydroxy-2-butanone 4-phosphate synthase (EC 5.4.99.-) - Vibrio harveyi ALTERNATE_NAMES luxH protein ORGANISM #formal_name Vibrio harveyi DATE 21-May-1999 #sequence_revision 21-May-1999 #text_change 18-Jun-1999 ACCESSIONS C35081 REFERENCE A35081 !$#authors Swartzman, E.; Miyamoto, C.; Graham, A.; Meighen, E. !$#journal J. Biol. Chem. (1990) 265:3513-3517 !$#title Delineation of the transcriptional boundaries of the lux !1operon of Vibrio harveyi demonstrates the presence of two !1new lux genes. !$#cross-references MUID:90154014; PMID:2303459 !$#accession C35081 !'##status preliminary !'##molecule_type mRNA !'##residues 1-230 ##label SWA !'##cross-references GB:M27139; NID:g155225; PIDN:AAA27538.1; !1PID:g155227 CLASSIFICATION #superfamily 3,4-dihydroxy-2-butanone 4-phosphate synthase; !13,4-dihydroxy-2-butanone 4-phosphate synthase homology KEYWORDS heat shock; intramolecular transferase; isomerase; !1riboflavin biosynthesis; stress-induced protein FEATURE !$20-210 #domain 3,4-dihydroxy-2-butanone 4-phosphate synthase !8homology #label HBPS SUMMARY #length 230 #molecular-weight 25328 #checksum 2137 SEQUENCE /// ENTRY G64306 #type complete TITLE probable 3,4-dihydroxy-2-butanone 4-phosphate synthase (EC 5.4.99.-) - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 21-May-1999 #sequence_revision 21-May-1999 #text_change 21-Jul-2000 ACCESSIONS G64306 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession G64306 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-227 ##label BUL !'##cross-references GB:U67463; GB:L77117; NID:g1590846; !1PIDN:AAB98035.1; PID:g1590849; TIGR:MJ0055 GENETICS !$#map_position REV55763-55080 CLASSIFICATION #superfamily 3,4-dihydroxy-2-butanone 4-phosphate synthase; !13,4-dihydroxy-2-butanone 4-phosphate synthase homology KEYWORDS intramolecular transferase; isomerase; riboflavin !1biosynthesis FEATURE !$7-220 #domain 3,4-dihydroxy-2-butanone 4-phosphate synthase !8homology #label HBPS SUMMARY #length 227 #molecular-weight 25796 #checksum 6134 SEQUENCE /// ENTRY G69066 #type complete TITLE probable 3,4-dihydroxy-2-butanone 4-phosphate synthase (EC 5.4.99.-) - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 21-May-1999 #sequence_revision 21-May-1999 #text_change 28-Jul-2000 ACCESSIONS G69066 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession G69066 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-229 ##label MTH !'##cross-references GB:AE000910; GB:AE000666; NID:g2622610; !1PIDN:AAB85974.1; PID:g2622616 !'##experimental_source strain Delta H GENETICS !$#gene MTH1499 CLASSIFICATION #superfamily 3,4-dihydroxy-2-butanone 4-phosphate synthase; !13,4-dihydroxy-2-butanone 4-phosphate synthase homology KEYWORDS intramolecular transferase; isomerase; riboflavin !1biosynthesis FEATURE !$10-224 #domain 3,4-dihydroxy-2-butanone 4-phosphate synthase !8homology #label HBP SUMMARY #length 229 #molecular-weight 25638 #checksum 7064 SEQUENCE /// ENTRY C69513 #type complete TITLE probable 3,4-dihydroxy-2-butanone 4-phosphate synthase (EC 5.4.99.-) - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 21-May-1999 #sequence_revision 21-May-1999 #text_change 28-Jul-2000 ACCESSIONS C69513 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession C69513 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-238 ##label KLE !'##cross-references GB:AE000958; GB:AE000782; NID:g2689281; !1PIDN:AAB89141.1; PID:g2648418; TIGR:AF2107 CLASSIFICATION #superfamily 3,4-dihydroxy-2-butanone 4-phosphate synthase; !13,4-dihydroxy-2-butanone 4-phosphate synthase homology KEYWORDS intramolecular transferase; isomerase; riboflavin !1biosynthesis FEATURE !$8-226 #domain 3,4-dihydroxy-2-butanone 4-phosphate synthase !8homology #label HBP SUMMARY #length 238 #molecular-weight 26585 #checksum 1844 SEQUENCE /// ENTRY I40662 #type complete TITLE methylaspartate mutase (EC 5.4.99.1) large chain [validated] - Clostridium cochlearium ALTERNATE_NAMES glutamate mutase chain E; glutamate mutase component E ORGANISM #formal_name Clostridium cochlearium DATE 18-Feb-2000 #sequence_revision 18-Feb-2000 #text_change 18-Feb-2000 ACCESSIONS I40662; S21216; S47464 REFERENCE I40659 !$#authors Zelder, O.; Beatrix, B.; Leutbecher, U.; Buckel, W. !$#journal Eur. J. Biochem. (1994) 226:577-585 !$#title Characterization of the coenzyme-B12-dependent glutamate !1mutase from Clostridium cochlearium produced in Escherichia !1coli. !$#cross-references MUID:95094816; PMID:7880251 !$#accession I40662 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-483 ##label RES !'##cross-references EMBL:X80997; NID:g530005; PIDN:CAA56923.1; !1PID:g530009 REFERENCE S21216 !$#authors Leutbecher, U.; Boecher, R.; Linder, D.; Buckel, W. !$#journal Eur. J. Biochem. (1992) 205:759-765 !$#title Glutamate mutase from Clostridium cochlearium. Purification, !1cobamide content and stereospecific inhibitors. !$#cross-references MUID:92241315; PMID:1315276 !$#accession S21216 !'##molecule_type protein !'##residues 1-26 ##label LEU !'##note 24-Val was also found GENETICS !$#gene glmE COMPLEX heterotetramer of large (E) and small (S) chains (see !1PIR:I40658) [validated, MUID:95094816] FUNCTION !$#description catalyzes coenzyme B12-dependent rearrangement of !1(S)-glutamate to (2S,3S)-3-methylaspartate [validated, !1MUID:95094816] !$#pathway glutamate fermentation CLASSIFICATION #superfamily Clostridium methylaspartate mutase large chain KEYWORDS heterotetramer; intramolecular transferase; isomerase FEATURE !$1-483 #product methylaspartate mutase large chain #status !8experimental #label MAT SUMMARY #length 483 #molecular-weight 53574 #checksum 4915 SEQUENCE /// ENTRY S32433 #type complete TITLE methylaspartate mutase (EC 5.4.99.1) large chain - Clostridium tetanomorphum (strain DSM 528) ALTERNATE_NAMES glutamate mutase chain E ORGANISM #formal_name Clostridium tetanomorphum DATE 18-Feb-2000 #sequence_revision 18-Feb-2000 #text_change 18-Feb-2000 ACCESSIONS S32433; S39106; S29504; S29219; A44285 REFERENCE S32433 !$#authors Brecht, M.; Kellermann, J.; Plueckthun, A. !$#journal FEBS Lett. (1993) 319:84-89 !$#title Cloning and sequencing of glutamate mutase component E from !1Clostridium tetanomorphum. !$#cross-references MUID:93202282; PMID:8454064 !$#accession S32433 !'##molecule_type DNA !'##residues 1-485 ##label BRE1 !'##cross-references EMBL:X70695; NID:g288074; PIDN:CAA50026.1; !1PID:g581007 !$#accession S39106 !'##molecule_type protein !'##residues 1-40;81-100;430-440;478-485 ##label BRE2 REFERENCE S29501 !$#authors Holloway, D.E.; Marsh, E.N.G. !$#journal FEBS Lett. (1993) 317:44-48 !$#title Cloning and sequencing of glutamate mutase component E from !1Clostridium tetanomorphum. Organization of the mut genes. !$#cross-references MUID:93154518; PMID:8428631 !$#accession S29504 !'##molecule_type DNA !'##residues 1-485 ##label HOL !'##cross-references EMBL:X70499; NID:g49238; PIDN:CAA49910.1; !1PID:g581011 REFERENCE S29218 !$#authors Marsh, E.N.G.; Holloway, D.E. !$#journal FEBS Lett. (1992) 310:167-170 !$#title Cloning and sequencing of glutamate mutase component S from !1Clostridium tetanomorphum. Homologies with other !1cobalamin-dependent enzymes. !$#cross-references MUID:93011908; PMID:1397267 !$#accession S29219 !'##molecule_type protein !'##residues 1-7,'L',9-11,'G',13-16,'A',18,'G',20 ##label MAR REFERENCE A44285 !$#authors Goda, S.K.; Minton, N.P.; Botting, N.P.; Gani, D. !$#journal Biochemistry (1992) 31:10747-10756 !$#title Cloning, sequencing, and expression in Escherichia coli of !1the Clostridium tetanomorphum gene encoding !1beta-methylaspartase and characterization of the recombinant !1protein. !$#cross-references MUID:93041773; PMID:1420191 !$#accession A44285 !'##status preliminary !'##molecule_type DNA !'##residues 278-485 ##label GOD !'##cross-references GB:S48141; NID:g259427; PIDN:AAB24069.1; !1PID:g259428 !'##experimental_source H1, ATCC 15920 !'##note sequence extracted from NCBI backbone (NCBIN:118074, !1NCBIP:118075) COMMENT The enzyme contains large (E) and small (S) chains (see !1PIR:S29502) and binds coenzyme B12, which is required for !1activity. GENETICS !$#gene mutE !$#start_codon GTG FUNCTION !$#description catalyzes coenzyme B12-dependent rearrangement of !1(S)-glutamate to (2S,3S)-3-methylaspartate !$#pathway glutamate fermentation CLASSIFICATION #superfamily Clostridium methylaspartate mutase large chain KEYWORDS intramolecular transferase; isomerase FEATURE !$1-485 #product methylaspartate mutase large chain #status !8experimental #label MAT SUMMARY #length 485 #molecular-weight 53740 #checksum 1616 SEQUENCE /// ENTRY T43809 #type complete TITLE methylaspartate mutase (EC 5.4.99.1) large chain [similarity] - Citrobacter amalonaticus ALTERNATE_NAMES glutamate mutase chain E ORGANISM #formal_name Citrobacter amalonaticus DATE 18-Feb-2000 #sequence_revision 18-Feb-2000 #text_change 21-Jul-2000 ACCESSIONS T43809 REFERENCE Z22694 !$#authors Kato, Y.; Asano, Y. !$#journal Appl. Microbiol. Biotechnol. (1998) 50:468-474 !$#title Cloning, nucleotide sequencing, and expression of !13-methylaspartate ammonia-lyase gene from Citrobacter !1amalonaticus strain YG-1002. !$#cross-references MUID:99047790; PMID:9830098 !$#accession T43809 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-481 ##label KAT !'##cross-references EMBL:AB005294; NID:g3184395; PIDN:BAA28708.1; !1PID:g3184396 !'##experimental_source strain YG-1002 CLASSIFICATION #superfamily Clostridium methylaspartate mutase large chain KEYWORDS intramolecular transferase; isomerase SUMMARY #length 481 #molecular-weight 52942 #checksum 1752 SEQUENCE /// ENTRY I40658 #type complete TITLE methylaspartate mutase (EC 5.4.99.1) small chain [validated] - Clostridium cochlearium ALTERNATE_NAMES glutamate mutase component S ORGANISM #formal_name Clostridium cochlearium DATE 18-Feb-2000 #sequence_revision 18-Feb-2000 #text_change 18-Feb-2000 ACCESSIONS I40658; I40660; S21249; S41332; S47462 REFERENCE I40657 !$#authors Zelder, O.; Beatrix, B.; Buckel, W. !$#journal FEMS Microbiol. Lett. (1994) 118:15-21 !$#title Cloning, sequencing and expression in Escherichia coli of !1the gene encoding component S of the coenzyme B12-dependent !1glutamate mutase from Clostridium cochlearium. !$#cross-references MUID:94283856; PMID:8013871 !$#accession I40658 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-137 ##label RES !'##cross-references EMBL:X75890; NID:g441487; PIDN:CAA53484.1; !1PID:g441489 REFERENCE I40659 !$#authors Zelder, O.; Beatrix, B.; Leutbecher, U.; Buckel, W. !$#journal Eur. J. Biochem. (1994) 226:577-585 !$#title Characterization of the coenzyme-B12-dependent glutamate !1mutase from Clostridium cochlearium produced in Escherichia !1coli. !$#cross-references MUID:95094816; PMID:7880251 !$#accession I40660 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-137 ##label RE2 !'##cross-references EMBL:X80997; NID:g530005; PIDN:CAA56921.1; !1PID:g530007 REFERENCE S21216 !$#authors Leutbecher, U.; Boecher, R.; Linder, D.; Buckel, W. !$#journal Eur. J. Biochem. (1992) 205:759-765 !$#title Glutamate mutase from Clostridium cochlearium. Purification, !1cobamide content and stereospecific inhibitors. !$#cross-references MUID:92241315; PMID:1315276 !$#accession S21249 !'##molecule_type protein !'##residues 1-14,'X',16-23 ##label LEU GENETICS !$#gene glmS COMPLEX heterotetramer of large (E) (see PIR:I40662) and small (S) !1chains [validated, MUID:95094816] FUNCTION !$#description catalyzes coenzyme B12-dependent rearrangement of !1(S)-glutamate to (2S,3S)-3-methylaspartate [validated, !1MUID:95094816] CLASSIFICATION #superfamily Clostridium methylaspartate mutase small chain; !1cobalamin-binding homology KEYWORDS cobalt; heterotetramer; intramolecular transferase; !1isomerase FEATURE !$1-137 #product methylaspartate mutase small chain #status !8experimental #label MAT\ !$2-94 #domain cobalamin-binding homology #label VBB SUMMARY #length 137 #molecular-weight 14812 #checksum 7939 SEQUENCE /// ENTRY S29502 #type complete TITLE methylaspartate mutase (EC 5.4.99.1) small chain - Clostridium tetanomorphum (strain NCIMB 11547) ALTERNATE_NAMES glutamate mutase chain S ORGANISM #formal_name Clostridium tetanomorphum DATE 18-Feb-2000 #sequence_revision 18-Feb-2000 #text_change 18-Feb-2000 ACCESSIONS S29502; S29218; S39104; S39105 REFERENCE S29501 !$#authors Holloway, D.E.; Marsh, E.N.G. !$#journal FEBS Lett. (1993) 317:44-48 !$#title Cloning and sequencing of glutamate mutase component E from !1Clostridium tetanomorphum. Organization of the mut genes. !$#cross-references MUID:93154518; PMID:8428631 !$#accession S29502 !'##molecule_type DNA !'##residues 1-137 ##label HOL !'##cross-references EMBL:X70499; NID:g49238; PIDN:CAA49908.1; !1PID:g49240 REFERENCE S29218 !$#authors Marsh, E.N.G.; Holloway, D.E. !$#journal FEBS Lett. (1992) 310:167-170 !$#title Cloning and sequencing of glutamate mutase component S from !1Clostridium tetanomorphum. Homologies with other !1cobalamin-dependent enzymes. !$#cross-references MUID:93011908; PMID:1397267 !$#accession S29218 !'##molecule_type DNA !'##residues 1-137 ##label MAR1 !'##cross-references GB:X68570; GB:S48797; NID:g312757; PIDN:CAA48567.1; !1PID:g312758 !$#accession S39104 !'##molecule_type protein !'##residues 1-14,'X',16-33 ##label MAR2 REFERENCE S32433 !$#authors Brecht, M.; Kellermann, J.; Plueckthun, A. !$#journal FEBS Lett. (1993) 319:84-89 !$#title Cloning and sequencing of glutamate mutase component E from !1Clostridium tetanomorphum. !$#cross-references MUID:93202282; PMID:8454064 !$#accession S39105 !'##molecule_type protein !'##residues 1-14,'D',16-24 ##label BRE COMMENT The enzyme contains small (S) and large (E) chains (see !1PIR:S32433) and binds coenzyme B12, which is required for !1activity. GENETICS !$#gene mutS FUNCTION !$#description catalyzes coenzyme B12-dependent rearrangement of !1(S)-glutamate to (2S,3S)-3-methylaspartate CLASSIFICATION #superfamily Clostridium methylaspartate mutase small chain; !1cobalamin-binding homology KEYWORDS cobalt; intramolecular transferase; isomerase FEATURE !$1-137 #product methylaspartate mutase small chain #status !8experimental #label MAT\ !$2-94 #domain cobalamin-binding homology #label VBB SUMMARY #length 137 #molecular-weight 14748 #checksum 7738 SEQUENCE /// ENTRY A59145 #type complete TITLE methylmalonyl-CoA mutase (EC 5.4.99.2) precursor [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 18-Feb-2000 #sequence_revision 18-Feb-2000 #text_change 18-Feb-2000 ACCESSIONS A59145; S40622; S40623; I55571; I70290; I70291 REFERENCE A59145 !$#authors Ledley, F.D. !$#submission submitted to GenBank, March 1989 !$#accession A59145 !'##molecule_type mRNA !'##residues 1-750 ##label JAN !'##cross-references GB:M65131; GB:M22990; GB:M65022; NID:g187451; !1PIDN:AAA59569.1; PID:g187452 !'##experimental_source tissue type liver; map 6p21; gene MUT; note !1G00-120-204 REFERENCE S40622 !$#authors Jansen, R.; Kalousek, F.; Fenton, W.A.; Rosenberg, L.E.; !1Ledley, F.D. !$#journal Genomics (1989) 4:198-205 !$#title Cloning of full-length methylmalonyl-CoA mutase from a cDNA !1library using the polymerase chain reaction. !$#cross-references MUID:89290848; PMID:2567699 !$#accession S40622 !'##molecule_type mRNA !'##residues 1-152,'L',154-235,'D',237-315,'H',317-435,444-504,'T', !1506-515,'G',517-590,'Y',592-750 ##label JA2 !'##cross-references EMBL:M22990 !'##note the authors translated the codon CAG for residue 35 as Glu !$#accession S40623 !'##molecule_type protein !'##residues 33-34,'E',36-52;67,'D',69-74;76-103;228-235,'D', !1237-238;513-515,'G',517-524;525,582-590,'Y',592-603;616-629 !1##label JAW REFERENCE I55571 !$#authors Crane, A.M.; Jansen, R.; Andrews, E.R.; Ledley, F.D. !$#journal J. Clin. Invest. (1992) 89:385-391 !$#title Cloning and expression of a mutant methylmalonyl coenzyme A !1mutase with altered cobalamin affinity that causes mut- !1methylmalonic aciduria. !$#cross-references MUID:92147850; PMID:1346616 !$#accession I55571 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 531,'R',533 ##label CRA1 !'##cross-references GB:S81159; NID:g245347; PIDN:AAB21416.1; !1PID:g245348 !$#accession I70290 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 670,'I',672 ##label CRA2 !'##cross-references GB:S81163; NID:g245349; PIDN:AAB21417.1; !1PID:g245350 !$#accession I70291 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 716,'V',718 ##label CRA3 !'##cross-references GB:S81167; NID:g245351; PIDN:AAB21418.1; !1PID:g245352 GENETICS !$#gene GDB:MUT !'##cross-references GDB:120204; OMIM:251000 !$#map_position 6p21.2-6p21.1 !$#genome nuclear COMPLEX homodimer [validated, MUID:82229852] FUNCTION !$#description catalyzes the isomerisation of L-methylmalonyl-CoA to !1succinyl-CoA !$#pathway valine, isoleucine, threonine, methionine, odd-chain fatty !1acid and cholesterol catabolism !$#note cofactor adenosylcobalamin; location mitochondrial matrix CLASSIFICATION #superfamily human methylmalonyl-CoA mutase; !1cobalamin-binding homology KEYWORDS cholesterol metabolism; cobalt; fatty acid metabolism; !1homodimer; intramolecular transferase; isomerase; !1mitochondrial matrix; mitochondrion; threonine catabolism FEATURE !$1-32 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$33-750 #product methylmalonyl-CoA mutase #status !8experimental #label MAT\ !$613-705 #domain cobalamin-binding homology #label VBB SUMMARY #length 750 #molecular-weight 83101 #checksum 9041 SEQUENCE /// ENTRY S08680 #type complete TITLE methylmalonyl-CoA mutase (EC 5.4.99.2) precursor - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 18-Feb-2000 #sequence_revision 18-Feb-2000 #text_change 18-Feb-2000 ACCESSIONS S08680; S13043 REFERENCE S08678 !$#authors Wilkemeyer, M.F.; Crane, A.M.; Ledley, F.D. !$#submission submitted to the EMBL Data Library, February 1990 !$#accession S08680 !'##molecule_type mRNA !'##residues 1-748 ##label WIL !'##cross-references EMBL:X51941; NID:g53150; PIDN:CAA36204.1; !1PID:g53151 REFERENCE S13043 !$#authors Wilkemeyer, M.F.; Crane, A.M.; Ledley, F.D. !$#journal Biochem. J. (1990) 271:449-455 !$#title Primary structure and activity of mouse methylmalonyl-CoA !1mutase. !$#cross-references MUID:91054410; PMID:1978672 !$#accession S13043 !'##status preliminary !'##molecule_type mRNA !'##residues 1-406,'Q',408-490,'Q',492-498,'EV',501-504,'NT',507,'V', !1509-560,'G',562-566,'L',568-612,'PR',615-621,'Q',623-656, !1'QH',659-671,'L',673-748 ##label WI2 COMPLEX homodimer [similarity] FUNCTION !$#description catalyzes the isomerisation of L-methylmalonyl-CoA to !1succinyl-CoA !$#pathway valine, isoleucine, threonine, methionine, odd-chain fatty !1acid and cholesterol catabolism !$#note cofactor adenosylcobalamin; location mitochondrial matrix CLASSIFICATION #superfamily human methylmalonyl-CoA mutase; !1cobalamin-binding homology KEYWORDS cholesterol metabolism; cobalt; fatty acid metabolism; !1homodimer; intramolecular transferase; isomerase; !1mitochondrial matrix; mitochondrion; threonine catabolism FEATURE !$1-30 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$31-748 #product methylmalonyl-CoA mutase #status predicted !8#label MAT\ !$611-703 #domain cobalamin-binding homology #label VBB SUMMARY #length 748 #molecular-weight 82965 #checksum 897 SEQUENCE /// ENTRY S43237 #type complete TITLE 2-methyleneglutarate mutase (EC 5.4.99.4) - Clostridium barkeri ORGANISM #formal_name Clostridium barkeri DATE 18-Feb-2000 #sequence_revision 18-Feb-2000 #text_change 18-Feb-2000 ACCESSIONS S43237; S77902; S43552 REFERENCE S43237 !$#authors Beatrix, B.; Zelder, O.; Linder, D.; Buckel, W. !$#journal Eur. J. Biochem. (1994) 221:101-109 !$#title Cloning, sequencing and expression of the gene encoding the !1coenzyme B(12)-dependent 2-methyleneglutarate mutase from !1Clostridium barkeri in Escherichia coli. !$#cross-references MUID:94222050; PMID:8168499 !$#accession S43237 !'##molecule_type DNA !'##residues 1-614 ##label BEA !'##cross-references EMBL:X77484; NID:g472895; PIDN:CAA54625.1; !1PID:g472897 !$#accession S77902 !'##molecule_type protein !'##residues !11-21;68-78;79-103;122-126;141-145;395-409;494-507;547-552; !1564-576 ##label BEW COMMENT This coenzyme B12-dependent enzyme catalyzes the !1isomerization of 2-methyleneglutarate to !1(R)-3-methylitaconate in the fermentation of nicotinic acid. CLASSIFICATION #superfamily Clostridium 2-methyleneglutarate mutase; !1cobalamin-binding homology KEYWORDS cobalt; intramolecular transferase; isomerase FEATURE !$471-564 #domain cobalamin-binding homology #label VBB SUMMARY #length 614 #molecular-weight 66749 #checksum 6246 SEQUENCE /// ENTRY KMECTD #type complete TITLE chorismate mutase (EC 5.4.99.5) / prephenate dehydrogenase (EC 1.3.1.12) tyrA [similarity] - Escherichia coli (strain K-12) ALTERNATE_NAMES chorismate mutase T ORGANISM #formal_name Escherichia coli DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 20-Jan-2003 ACCESSIONS A30274; C65038 REFERENCE A92910 !$#authors Hudson, G.S.; Davidson, B.E. !$#journal J. Mol. Biol. (1984) 180:1023-1051 !$#title Nucleotide sequence and transcription of the phenylalanine !1and tyrosine operons of Escherichia coli K12. !$#cross-references MUID:85134883; PMID:6396419 !$#accession A30274 !'##molecule_type DNA !'##residues 1-373 ##label HUD !'##cross-references GB:M10431; NID:g147172; PIDN:AAA24331.1; !1PID:g457110; EMBL:X02137 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65038 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-373 ##label BLAT !'##cross-references GB:AE000346; GB:U00096; NID:g2367141; !1PIDN:AAC75649.1; PID:g1788952; UWGP:b2600 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene tyrA !$#map_position 57 min FUNCTION !$#description this bifunctional enzyme catalyzes the isomerization of !1chorismate to prephenate and aromatization of prephenate to !14-hydroxyphenylpyruvate in two consecutive steps of the !1tyrosine biosynthesis pathway CLASSIFICATION #superfamily bifunctional chorismate mutase / prephenate !1dehydrogenase (T-protein) KEYWORDS intramolecular transferase; isomerase; multifunctional !1enzyme; oxidoreductase; tyrosine biosynthesis SUMMARY #length 373 #molecular-weight 42042 #checksum 1073 SEQUENCE /// ENTRY S29934 #type complete TITLE chorismate mutase (EC 5.4.99.5) / prephenate dehydrogenase (EC 1.3.1.12) tyrA [similarity] - Erwinia herbicola ORGANISM #formal_name Erwinia herbicola DATE 02-Dec-1993 #sequence_revision 10-May-1996 #text_change 20-Jan-2003 ACCESSIONS S29934; S26054; S78451 REFERENCE S29933 !$#authors Xia, T. !$#submission submitted to the EMBL Data Library, September 1991 !$#accession S29934 !'##molecule_type DNA !'##residues 1-373 ##label XIA !'##cross-references EMBL:X60420; NID:g43343; PIDN:CAA42950.1; !1PID:g43345 REFERENCE S26053 !$#authors Xia, T.; Zhao, G.; Fischer, R.S.; Jensen, R.A. !$#journal J. Gen. Microbiol. (1992) 138:1309-1316 !$#title A monofunctional prephenate dehydrogenase created by !1cleavage of the 5' 109 bp of the tyrA gene from Erwinia !1herbicola. !$#cross-references MUID:92381476; PMID:1512561 !$#accession S26054 !'##molecule_type DNA !'##residues 1-46 ##label XIW !'##cross-references EMBL:X60420 !'##experimental_source ATCC 33243 GENETICS !$#gene tyrA FUNCTION CHM !$#description chorismate mutase catalyzes the isomerization of chorismate !1to prephenate !$#pathway tyrosine biosynthesis FUNCTION PRD !$#description prephenate dehydrogenase catalyzes oxidative aromatization !1of prephenate to 4-hydroxyphenylpyruvate !$#pathway tyrosine biosynthesis CLASSIFICATION #superfamily bifunctional chorismate mutase / prephenate !1dehydrogenase (T-protein) KEYWORDS intramolecular transferase; isomerase; multifunctional !1enzyme; oxidoreductase; tyrosine biosynthesis SUMMARY #length 373 #molecular-weight 41847 #checksum 1048 SEQUENCE /// ENTRY H64114 #type complete TITLE chorismate mutase (EC 5.4.99.5) / prephenate dehydrogenase (EC 1.3.1.12) HI1290 [similarity] - Haemophilus influenzae (strain Rd KW20) CONTAINS chorismate mutase T; prephenate dehydrogenase ORGANISM #formal_name Haemophilus influenzae DATE 18-Aug-1995 #sequence_revision 10-May-1996 #text_change 20-Jan-2003 ACCESSIONS H64114; T09419 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession H64114 !'##molecule_type DNA !'##residues 1-377 ##label TIGR !'##cross-references GB:U32809; GB:L42023; NID:g3212217; !1PIDN:AAC22939.1; PID:g1574749; TIGR:HI1290 !'##note named as homolog to a protein from Erwinia herbicola REFERENCE Z16667 !$#authors White, O.; Clayton, R.A.; Kerlavage, A.R.; Fleischmann, !1R.D.; Peterson, J.; Hickey, E.; Dodson, R.; Gwinn, M. !$#submission submitted to the EMBL Data Library, May 1998 !$#accession T09419 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-377 ##label WHI !'##cross-references EMBL:U32809; NID:g3212217; PIDN:AAC22939.1; !1PID:g1574749 GENETICS !$#gene HI1290 !$#start_codon GTG CLASSIFICATION #superfamily bifunctional chorismate mutase / prephenate !1dehydrogenase (T-protein) KEYWORDS intramolecular transferase; isomerase; multifunctional !1enzyme; oxidoreductase; tyrosine biosynthesis SUMMARY #length 377 #molecular-weight 43022 #checksum 9838 SEQUENCE /// ENTRY KMECPW #type complete TITLE chorismate mutase (EC 5.4.99.5) / prephenate dehydratase (EC 4.2.1.51) pheA [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 20-Jan-2003 ACCESSIONS A30261; C36494; B65038 REFERENCE A92910 !$#authors Hudson, G.S.; Davidson, B.E. !$#journal J. Mol. Biol. (1984) 180:1023-1051 !$#title Nucleotide sequence and transcription of the phenylalanine !1and tyrosine operons of Escherichia coli K12. !$#cross-references MUID:85134883; PMID:6396419 !$#accession A30261 !'##molecule_type DNA !'##residues 1-386 ##label HUD !'##cross-references GB:M10431; NID:g147172; PIDN:AAA24330.1; !1PID:g147175; EMBL:X02137 REFERENCE A36494 !$#authors Gavini, N.; Davidson, B.E. !$#journal J. Biol. Chem. (1990) 265:21532-21535 !$#title pheAo mutants of Escherichia coli have a defective pheA !1attenuator. !$#cross-references MUID:91072346; PMID:2254312 !$#accession C36494 !'##status preliminary !'##molecule_type DNA !'##residues 1-50 ##label GAV !'##cross-references GB:M58024; GB:J05694; NID:g147178; PIDN:AAA62784.1; !1PID:g551824 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65038 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-386 ##label BLAT !'##cross-references GB:AE000346; GB:U00096; NID:g2367141; !1PIDN:AAC75648.1; PID:g1788951; UWGP:b2599 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene pheA !$#map_position 57 min FUNCTION CHM !$#description EC 5.4.99.5 [validated, MUID:98165805]; chorismate mutase !1catalyzes the isomerization of chorismate to prephenate !$#pathway phenylalanine biosynthesis FUNCTION PRD !$#description EC 4.2.1.51 [validated, MUID:98165805]; prephenate !1dehydratase catalyzes aromatization of prephenate to !1phenylpyruvate !$#pathway phenylalanine biosynthesis CLASSIFICATION #superfamily bifunctional chorismate mutase / prephenate !1dehydratase (P-protein); prephenate dehydratase homology KEYWORDS carbon-oxygen lyase; hydro-lyase; intramolecular !1transferase; isomerase; multifunctional enzyme; !1phenylalanine biosynthesis FEATURE !$1-109 #domain chorismate mutase #status experimental #label !8MUT\ !$101-285 #domain prephenate dehydratase #status experimental !8#label DEH\ !$104-380 #domain prephenate dehydratase homology #label PPW\ !$286-386 #domain regulatory (feedback inhibition) #status !8experimental #label REG SUMMARY #length 386 #molecular-weight 43111 #checksum 2207 SEQUENCE /// ENTRY S26053 #type complete TITLE chorismate mutase (EC 5.4.99.5) / prephenate dehydratase (EC 4.2.1.51) pheA [similarity] - Erwinia herbicola ORGANISM #formal_name Erwinia herbicola DATE 22-Nov-1993 #sequence_revision 10-May-1996 #text_change 20-Jan-2003 ACCESSIONS S26053; S29933 REFERENCE S26053 !$#authors Xia, T.; Zhao, G.; Fischer, R.S.; Jensen, R.A. !$#journal J. Gen. Microbiol. (1992) 138:1309-1316 !$#title A monofunctional prephenate dehydrogenase created by !1cleavage of the 5' 109 bp of the tyrA gene from Erwinia !1herbicola. !$#cross-references MUID:92381476; PMID:1512561 !$#accession S26053 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-387 ##label XIA !'##cross-references EMBL:X60420; NID:g43343; PIDN:CAA42949.1; !1PID:g43344 !'##experimental_source ATCC 33243 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1September 1991 GENETICS !$#gene pheA FUNCTION CHM !$#description chorismate mutase catalyzes the isomerization of chorismate !1to prephenate !$#pathway phenylalanine biosynthesis FUNCTION PRD !$#description prephenate dehydratase catalyzes aromatization of prephenate !1to phenylpyruvate !$#pathway phenylalanine biosynthesis CLASSIFICATION #superfamily bifunctional chorismate mutase / prephenate !1dehydratase (P-protein); prephenate dehydratase homology KEYWORDS carbon-oxygen lyase; hydro-lyase; intramolecular !1transferase; isomerase; multifunctional enzyme; !1phenylalanine biosynthesis FEATURE !$104-380 #domain prephenate dehydratase homology #label PPW SUMMARY #length 387 #molecular-weight 43182 #checksum 4335 SEQUENCE /// ENTRY B64186 #type complete TITLE chorismate mutase (EC 5.4.99.5) / prephenate dehydratase (EC 4.2.1.51) HI1145 [similarity] - Haemophilus influenzae (strain Rd KW20) CONTAINS chorismate mutase P; prephenate dehydratase ORGANISM #formal_name Haemophilus influenzae DATE 18-Aug-1995 #sequence_revision 10-May-1996 #text_change 20-Jan-2003 ACCESSIONS B64186 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession B64186 !'##molecule_type DNA !'##residues 1-385 ##label TIGR !'##cross-references GB:U32794; GB:L42023; NID:g1574694; !1PIDN:AAC22800.1; PID:g1574701; TIGR:HI1145 !'##note named as homolog to a protein from Escherichia coli CLASSIFICATION #superfamily bifunctional chorismate mutase / prephenate !1dehydratase (P-protein); prephenate dehydratase homology KEYWORDS carbon-oxygen lyase; hydro-lyase; intramolecular !1transferase; isomerase; multifunctional enzyme; !1phenylalanine biosynthesis FEATURE !$104-380 #domain prephenate dehydratase homology #label PPW SUMMARY #length 385 #molecular-weight 44001 #checksum 3270 SEQUENCE /// ENTRY A44764 #type complete TITLE chorismate mutase (EC 5.4.99.5) / prephenate dehydratase (EC 4.2.1.51) - Pseudomonas stutzeri ORGANISM #formal_name Pseudomonas stutzeri DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 20-Jan-2003 ACCESSIONS A44764 REFERENCE A44764 !$#authors Fischer, R.S.; Zhao, G.; Jensen, R.A. !$#journal J. Gen. Microbiol. (1991) 137:1293-1301 !$#title Cloning, sequencing, and expression of the P-protein gene !1(pheA) of Pseudomonas stutzeri in Escherichia coli: !1implications for evolutionary relationships in phenylalanine !1biosynthesis. !$#cross-references MUID:92013931; PMID:1919506 !$#accession A44764 !'##status preliminary !'##molecule_type DNA !'##residues 1-365 ##label FIS !'##cross-references EMBL:M73971; NID:g151445; PIDN:AAA25935.1; !1PID:g151446 CLASSIFICATION #superfamily bifunctional chorismate mutase / prephenate !1dehydratase (P-protein); prephenate dehydratase homology KEYWORDS carbon-oxygen lyase; hydro-lyase; intramolecular !1transferase; isomerase FEATURE !$95-365 #domain prephenate dehydratase homology #label PPW SUMMARY #length 365 #molecular-weight 40844 #checksum 1037 SEQUENCE /// ENTRY B70382 #type complete TITLE chorismate mutase/prephenate dehydratase - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 20-Jan-2003 ACCESSIONS B70382 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession B70382 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-362 ##label AQF !'##cross-references GB:AE000715; NID:g2983460; PIDN:AAC07041.1; !1PID:g2983461; GB:AE000657 !'##experimental_source strain VF5 GENETICS !$#gene pheA CLASSIFICATION #superfamily bifunctional chorismate mutase / prephenate !1dehydratase (P-protein); prephenate dehydratase homology FEATURE !$91-360 #domain prephenate dehydratase homology #label PPW SUMMARY #length 362 #molecular-weight 41186 #checksum 2503 SEQUENCE /// ENTRY G64330 #type complete TITLE chorismate mutase (EC 5.4.99.5) chain A - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Feb-2003 ACCESSIONS G64330 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession G64330 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-99 ##label BUL !'##cross-references GB:U67480; GB:L77117; NID:g2826265; !1PIDN:AAB98234.1; PID:g1590979; TIGR:MJ0246 GENETICS !$#map_position REV233997-233698 CLASSIFICATION #superfamily chorismate mutase of the AroQ class, !1Prokaryotic type KEYWORDS intramolecular transferase; isomerase SUMMARY #length 99 #molecular-weight 11782 #checksum 2571 SEQUENCE /// ENTRY D69207 #type complete TITLE conserved hypothetical protein MTH804 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Feb-2003 ACCESSIONS D69207 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession D69207 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-98 ##label MTH !'##cross-references GB:AE000858; GB:AE000666; NID:g2621885; !1PIDN:AAB85304.1; PID:g2621894 !'##experimental_source strain Delta H GENETICS !$#gene MTH804 CLASSIFICATION #superfamily chorismate mutase of the AroQ class, !1Prokaryotic type SUMMARY #length 98 #molecular-weight 11664 #checksum 8276 SEQUENCE /// ENTRY SYECIK #type complete TITLE isochorismate synthase (EC 5.4.99.6) [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES isochorismate synthetase ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 01-Mar-2002 ACCESSIONS JT0497; S04323; I73520; G64792 REFERENCE JT0497 !$#authors Ozenberger, B.A.; Brickman, T.J.; McIntosh, M.A. !$#journal J. Bacteriol. (1989) 171:775-783 !$#title Nucleotide sequence of Escherichia coli isochorismate !1synthetase gene entC and evolutionary relationship of !1isochorismate synthetase and other chorismate-utilizing !1enzymes. !$#cross-references MUID:89123153; PMID:2536681 !$#accession JT0497 !'##molecule_type DNA !'##residues 1-391 ##label OZE !'##cross-references GB:M24142; NID:g341117; PIDN:AAA16100.1; !1PID:g450376 REFERENCE S04323 !$#authors Elkins, M.F.; Earhart, C.F. !$#journal FEMS Microbiol. Lett. (1988) 56:35-40 !$#title An Escherichia coli enterobactin cluster gene with sequence !1homology to trpE and pabB. !$#cross-references MUID:90236256; PMID:2110093 !$#accession S04323 !'##status preliminary !'##molecule_type DNA !'##residues 1-304,'TA',307-391 ##label ELK !'##cross-references GB:M36700; EMBL:X12670; NID:g145839; !1PIDN:AAA18491.1; PID:g145840 REFERENCE I56426 !$#authors Brickman, T.J.; Ozenberger, B.A.; McIntosh, M.A. !$#journal J. Mol. Biol. (1990) 212:669-682 !$#title Regulation of divergent transcription from the !1iron-responsive fepB-entC promoter-operator regions in !1Escherichia coli. !$#cross-references MUID:90230305; PMID:2139473 !$#accession I73520 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-33 ##label RES !'##cross-references EMBL:X53274; NID:g48747; PIDN:CAA37371.1; !1PID:g48749 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64792 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-391 ##label BLAT !'##cross-references GB:AE000165; GB:U00096; NID:g1786808; !1PIDN:AAC73694.1; PID:g1786809; UWGP:b0593 !'##experimental_source strain K-12, substrain MG1655 COMMENT This enzyme catalyzes the isomerization of chorismate to !1isochorismate, an early member in the pathway to !1enterobactin, and appears to be involved in chorismate !1binding. The transcription of the entC gene is regulated by !1iron and possibly by the product of the entA gene, 2, !13-dihydro-2,3-dihydroxybenzoate dehydrogenase. GENETICS !$#gene entC; fepF; menF !$#map_position 14 min FUNCTION !$#description EC 5.4.99.6 [validated, MUID:89123153] !$#pathway enterobactin biosynthesis; menaquinone biosynthesis CLASSIFICATION #superfamily isochorismate synthase KEYWORDS enterobactin biosynthesis; intramolecular transferase; !1isomerase SUMMARY #length 391 #molecular-weight 42931 #checksum 8420 SEQUENCE /// ENTRY A69657 #type complete TITLE probable isochorismate synthase (EC 5.4.99.6) menaquinone-specific menF - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A69657; S27507; S27508; I39883; T46638; T46639 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69657 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-471 ##label KUN !'##cross-references GB:Z99119; GB:AL009126; NID:g2635411; !1PIDN:CAB15061.1; PID:g2635567 !'##experimental_source strain 168 REFERENCE S27507 !$#authors Rowland, B.; Hill, K.; Mueller, J.; Driscoll, J.; Taber, H. !$#submission submitted to the EMBL Data Library, October 1991 !$#description Organization of an operon involved in menaquinone !1biosynthesis in Bacillus subtilis. !$#accession S27507 !'##molecule_type DNA !'##residues 1-11,'K',13-110,'WDLCYSEDFLLTLAKKEVHNGTISRKGISLCLRLC' !1##label ROW1 !'##cross-references EMBL:M74538; NID:g1185287 !$#accession S27508 !'##molecule_type DNA !'##residues 151-471 ##label ROW2 !'##cross-references EMBL:M74538; NID:g1185287 REFERENCE I39883 !$#authors Miller, P. !$#journal J. Bacteriol. (1988) 170:2742-2748 !$#title Transcriptional regulation of a promoter in the men gene !1cluster of Bacillus subtilis. !$#cross-references MUID:88227858; PMID:3131310 !$#accession I39883 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-11,'K',13-32 ##label MIL !'##cross-references GB:M21320; NID:g143178; PIDN:AAA22594.1; !1PID:g551715 REFERENCE A42715 !$#authors Driscoll, J.R.; Taber, H.W. !$#journal J. Bacteriol. (1992) 174:5063-5071 !$#title Sequence organization and regulation of the Bacillus !1subtilis menBE operon. !$#cross-references MUID:92332443; PMID:1629163 !$#accession T46638 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-11,'K',13-110,134-135,'LCYSE',141-142,'LL','T',317, !1'AKKEVHN',325,'T',327,'SRKGI',333,'L',335,'LRLC' ##label DRI !'##cross-references EMBL:M74521; NID:g557486; PIDN:AAA50396.1; !1PID:g557487 !$#accession T46639 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 151-471 ##label DR2 !'##cross-references EMBL:M74521; NID:g557486; PIDN:AAA50397.1; !1PID:g557488 GENETICS !$#gene menF CLASSIFICATION #superfamily isochorismate synthase KEYWORDS intramolecular transferase; isomerase SUMMARY #length 471 #molecular-weight 52811 #checksum 8355 SEQUENCE /// ENTRY S58229 #type complete TITLE salicylate biosynthesis isochorismate synthase PA4231 [imported] - Pseudomonas aeruginosa ORGANISM #formal_name Pseudomonas aeruginosa DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 31-Dec-2000 ACCESSIONS S60203; B83117; S58229 REFERENCE S60202 !$#authors Serino, L.; Reimmann, C.; Baur, H.; Beyeler, M.; Visca, P.; !1Haas, D. !$#journal Mol. Gen. Genet. (1995) 249:217-228 !$#title Structural genes for salicylate biosynthesis from chorismate !1in Pseudomonas aeruginosa. !$#cross-references MUID:96086939; PMID:7500944 !$#accession S60203 !'##status preliminary !'##molecule_type DNA !'##residues 1-476 ##label SE2 !'##cross-references EMBL:X82644; NID:g1628425; PIDN:CAA57969.1; !1PID:g929780 !'##note this protein is involved in salicylate biosynthesis REFERENCE A82950 !$#authors Stover, C.K.; Pham, X.Q.; Erwin, A.L.; Mizoguchi, S.D.; !1Warrener, P.; Hickey, M.J.; Brinkman, F.S.L.; Hufnagle, !1W.O.; Kowalik, D.J.; Lagrou, M.; Garber, R.L.; Goltry, L.; !1Tolentino, E.; Westbrook-Wadman, S.; Yuan, Y.; Brody, L.L.; !1Coulter, S.N.; Folger, K.R.; Kas, A.; Larbig, K.; Lim, R.M.; !1Smith, K.A.; Spencer, D.H.; Wong, G.K.S.; Wu, Z.; Paulsen, !1I.T.; Reizer, J.; Saier, M.H.; Hancock, R.E.W.; Lory, S.; !1Olson, M.V. !$#journal Nature (2000) 406:959-964 !$#title Complete genome sequence of Pseudomonas aeruginosa PA01, an !1opportunistic pathogen. !$#cross-references MUID:20437337; PMID:10984043 !$#accession B83117 !'##status preliminary !'##molecule_type DNA !'##residues 1-476 ##label STO !'##cross-references GB:AE004840; GB:AE004091; NID:g9950442; !1PIDN:AAG07619.1; GSPDB:GN00131; PASP:PA4231 !'##experimental_source strain PAO1 GENETICS !$#gene pchA; PA4231 CLASSIFICATION #superfamily isochorismate synthase SUMMARY #length 476 #molecular-weight 52071 #checksum 7909 SEQUENCE /// ENTRY S75568 #type complete TITLE isochorismate synthase (EC 5.4.99.6) - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein slr0817 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S75568 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75568 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-474 ##label KAN !'##cross-references EMBL:D90911; GB:AB001339; NID:g1653083; !1PIDN:BAA18129.1; PID:g1653213 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene entC CLASSIFICATION #superfamily isochorismate synthase KEYWORDS intramolecular transferase; isomerase SUMMARY #length 474 #molecular-weight 52667 #checksum 7982 SEQUENCE /// ENTRY C69615 #type complete TITLE isochorismate synthase dhbC - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS C69615 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69615 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-398 ##label KUN !'##cross-references GB:Z99120; GB:AL009126; NID:g2635613; !1PIDN:CAB15189.1; PID:g2635696 !'##experimental_source strain 168 GENETICS !$#gene dhbC CLASSIFICATION #superfamily isochorismate synthase SUMMARY #length 398 #molecular-weight 43446 #checksum 3814 SEQUENCE /// ENTRY A40365 #type complete TITLE siderophore biosynthetic protein amoA - Aeromonas hydrophila ORGANISM #formal_name Aeromonas hydrophila DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A40365 REFERENCE A40365 !$#authors Barghouthi, S.; Payne, S.M.; Arceneaux, J.E.L.; Byers, B.R. !$#journal J. Bacteriol. (1991) 173:5121-5128 !$#title Cloning, mutagenesis, and nucleotide sequence of a !1siderophore biosynthetic gene (amoA) from Aeromonas !1hydrophila. !$#cross-references MUID:91317731; PMID:1830579 !$#accession A40365 !'##status preliminary !'##molecule_type DNA !'##residues 1-396 ##label BAR !'##cross-references GB:M63339 !'##note the authors translated the codon GAG for residue 393 as Gly CLASSIFICATION #superfamily isochorismate synthase SUMMARY #length 396 #molecular-weight 42042 #checksum 6097 SEQUENCE /// ENTRY A43300 #type complete TITLE squalene-hopene cyclase (EC 5.4.99.-) - Alicyclobacillus acidocaldarius ORGANISM #formal_name Alicyclobacillus acidocaldarius DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A43300; S13856 REFERENCE A43300 !$#authors Ochs, D.; Kaletta, C.; Entian, K.D.; Beck-Sickinger, A.; !1Poralla, K. !$#journal J. Bacteriol. (1992) 174:298-302 !$#title Cloning, expression, and sequencing of squalene-hopene !1cyclase, a key enzyme in triterpenoid metabolism. !$#cross-references MUID:92104976; PMID:1729216 !$#accession A43300 !'##status preliminary !'##molecule_type DNA !'##residues 1-627 ##label OCH !'##experimental_source strain ATCC 27009 !'##note sequence extracted from NCBI backbone (NCBIN:75380, !1NCBIP:75382) REFERENCE S13856 !$#authors Ochs, D.; Tappe, C.H.; Gaertner, P.; Kellner, R.; Poralla, !1K. !$#journal Eur. J. Biochem. (1990) 194:75-80 !$#title Properties of purified squalene-hopene cyclase from Bacillus !1acidocaldarius. !$#cross-references MUID:91071213; PMID:2253626 !$#accession S13856 !'##molecule_type protein !'##residues 2-12,'X',14-16,'X',18-25 ##label OCW !'##experimental_source strain ATCC 27009 FUNCTION !$#pathway triterpenoid metabolism CLASSIFICATION #superfamily squalene-hopene cyclase KEYWORDS intramolecular transferase; isomerase; monomer SUMMARY #length 627 #molecular-weight 69464 #checksum 5469 SEQUENCE /// ENTRY T46549 #type complete TITLE isobutyryl-CoA mutase (EC 5.4.99.13) chain A [validated] - Streptomyces cinnamonensis ORGANISM #formal_name Streptomyces cinnamonensis DATE 18-Feb-2000 #sequence_revision 18-Feb-2000 #text_change 21-Jul-2000 ACCESSIONS T46549 REFERENCE Z23059 !$#authors Zerbe-Burkhardt, K.; Ratnatilleke, A.; Philippon, N.; Birch, !1A.; Leiser, A.; Vrijbloed, J.W.; Hess, D.; Hunziker, P.; !1Robinson, J.A. !$#journal J. Biol. Chem. (1998) 273:6508-6517 !$#title Cloning, sequencing, expression, and insertional !1inactivation of the gene for the large subunit of the !1coenzyme B12-dependent isobutyryl-CoA mutase from !1streptomyces cinnamonensis. !$#cross-references MUID:98165841; PMID:9497386 !$#accession T46549 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-566 ##label ZER !'##cross-references EMBL:U67612; NID:g3002491; PIDN:AAC08713.1; !1PID:g3002492 !'##experimental_source strain A3823.5 !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing GENETICS !$#gene icmA COMPLEX heterodimer of chain A (65K) and B (17K) [validated, !1MUID:98165841] FUNCTION !$#description catalyses coenzyme B12-dependent rearrangement of !1isobutyryl-coenzyme A to n-butyryl-coenzyme A !$#note reaction catalyzed by ICM is very similar to that of !1methylmalonyl-CoA mutase large chain; chain B is required !1and is presumed to bind the coenzyme B12 CLASSIFICATION #superfamily Streptomyces isobutyryl-CoA mutase chain A KEYWORDS intramolecular transferase; isomerase SUMMARY #length 566 #molecular-weight 62487 #checksum 4079 SEQUENCE /// ENTRY T43706 #type complete TITLE isobutyryl-CoA mutase (EC 5.4.99.13) chain A [similarity] - Streptomyces coelicolor ORGANISM #formal_name Streptomyces coelicolor DATE 18-Feb-2000 #sequence_revision 18-Feb-2000 #text_change 18-Feb-2000 ACCESSIONS T43706 REFERENCE Z22640 !$#authors Vrijbloed, J.W.; Zerbe-Burkhardt, K.; Ratnatilleke, A.; !1Grubelnik-Leiser, A.; Robinson, J.A. !$#submission submitted to the EMBL Data Library, April 1999 !$#description Insertional inactivation of the genes encoding B12-dependent !1mutases in Streptomyces cinnamonensis and effects on !1Monensin A production. !$#accession T43706 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-566 ##label VRI !'##cross-references EMBL:AJ237976; PIDN:CAB40912.1 !'##experimental_source strain A3(2) GENETICS !$#gene icmA COMPLEX heterodimer of chain A (65K) and B (17K) [similarity] FUNCTION !$#description catalyses coenzyme B12-dependent rearrangement of !1isobutyryl-coenzyme A to n-butyryl-coenzyme A !$#note reaction catalyzed by ICM is very similar to that of !1methylmalonyl-CoA mutase large chain; chain B is required !1and is presumed to bind the coenzyme B12 CLASSIFICATION #superfamily Streptomyces isobutyryl-CoA mutase chain A KEYWORDS heterodimer; intramolecular transferase; isomerase SUMMARY #length 566 #molecular-weight 62195 #checksum 4210 SEQUENCE /// ENTRY D75425 #type complete TITLE methylmalonyl-CoA mutase (EC 5.4.99.2) chain A [similarity] - Deinococcus radiodurans (strain R1) ORGANISM #formal_name Deinococcus radiodurans DATE 18-Feb-2000 #sequence_revision 18-Feb-2000 #text_change 31-Mar-2000 ACCESSIONS D75425 REFERENCE A75250 !$#authors White, O.; Eisen, J.A.; Heidelberg, J.F.; Hickey, E.K.; !1Peterson, J.D.; Dodson, R.J.; Haft, D.H.; Gwinn, M.L.; !1Nelson, W.C.; Richardson, D.L.; Moffat, K.S.; Qin, H.; !1Jiang, L.; Pamphile, W.; Crosby, M.; Shen, M.; Vamathevan, !1J.J.; Lam, P.; McDonald, L.; Utterback, T.; Zalewski, C.; !1Makarova, K.S.; Aravind, L.; Daly, M.J.; Minton, K.W.; !1Fleischmann, R.D.; Ketchum, K.A.; Nelson, K.E.; Salzberg, !1S.; Smith, H.O.; Venter, J.C.; Fraser, C.M. !$#journal Science (1999) 286:1571-1577 !$#title Genome sequence of the radioresistant bacterium Deinococcus !1radiodurans R1. !$#cross-references MUID:20036896; PMID:10567266 !$#accession D75425 !'##molecule_type DNA !'##residues 1-561 ##label WHI !'##cross-references GB:AE001968; GB:AE000513; NID:g6458930; !1PIDN:AAF10762.1; PID:g6458931; TIGR:DR1189; GSPDB:GN00077 !'##experimental_source strain R1 GENETICS !$#gene DR1189 !$#map_position 1 FUNCTION !$#description catalyzes the isomerisation of L-methylmalonyl-CoA to !1succinyl-CoA !$#pathway valine, isoleucine, threonine, methionine, odd-chain fatty !1acid and cholesterol catabolism CLASSIFICATION #superfamily Streptomyces isobutyryl-CoA mutase chain A KEYWORDS intramolecular transferase; isomerase SUMMARY #length 561 #molecular-weight 62666 #checksum 5239 SEQUENCE /// ENTRY G69526 #type complete TITLE methylmalonyl-CoA mutase (EC 5.4.99.2) chain A [similarity] - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 18-Feb-2000 #sequence_revision 18-Feb-2000 #text_change 21-Jul-2000 ACCESSIONS G69526 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession G69526 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-548 ##label KLE !'##cross-references GB:AE000952; GB:AE000782; NID:g2689275; !1PIDN:AAB89037.1; PID:g2648308; TIGR:AF2215 FUNCTION !$#description catalyzes the isomerisation of L-methylmalonyl-CoA to !1succinyl-CoA !$#pathway valine, isoleucine, threonine, methionine, odd-chain fatty !1acid and cholesterol catabolism CLASSIFICATION #superfamily Streptomyces isobutyryl-CoA mutase chain A KEYWORDS intramolecular transferase; isomerase SUMMARY #length 548 #molecular-weight 62244 #checksum 6852 SEQUENCE /// ENTRY B71001 #type complete TITLE methylmalonyl-CoA mutase (EC 5.4.99.2) chain A [similarity] - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 18-Feb-2000 #sequence_revision 18-Feb-2000 #text_change 16-Jun-2000 ACCESSIONS B71001 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession B71001 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-563 ##label KAW !'##cross-references GB:AP000006; NID:g3236133; PIDN:BAA30410.1; !1PID:g3257727 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1306 FUNCTION !$#description catalyzes the isomerisation of L-methylmalonyl-CoA to !1succinyl-CoA !$#pathway valine, isoleucine, threonine, methionine, odd-chain fatty !1acid and cholesterol catabolism CLASSIFICATION #superfamily Streptomyces isobutyryl-CoA mutase chain A KEYWORDS intramolecular transferase; isomerase SUMMARY #length 563 #molecular-weight 64604 #checksum 9612 SEQUENCE /// ENTRY C75130 #type complete TITLE methylmalonyl-CoA mutase (EC 5.4.99.2) chain A [similarity] - Pyrococcus abyssi (strain Orsay) ALTERNATE_NAMES protein PAB1800 ORGANISM #formal_name Pyrococcus abyssi DATE 18-Feb-2000 #sequence_revision 18-Feb-2000 #text_change 16-Jun-2000 ACCESSIONS C75130 REFERENCE A75001 !$#authors anonymous, Genoscope !$#submission submitted to the EMBL Data Library, July 1999 !$#description Pyrococcus abyssi genome sequence: insights into archaeal !1chromosome structure and evolution. !$#accession C75130 !'##molecule_type DNA !'##residues 1-562 ##label KAW !'##cross-references GB:AJ248285; GB:AL096836; NID:g5458067; !1PIDN:CAB49756.1; PID:g5458267 !'##experimental_source strain Orsay GENETICS !$#gene PAB1800 FUNCTION !$#description catalyzes the isomerisation of L-methylmalonyl-CoA to !1succinyl-CoA !$#pathway valine, isoleucine, threonine, methionine, odd-chain fatty !1acid and cholesterol catabolism CLASSIFICATION #superfamily Streptomyces isobutyryl-CoA mutase chain A KEYWORDS intramolecular transferase; isomerase SUMMARY #length 562 #molecular-weight 64491 #checksum 5266 SEQUENCE /// ENTRY C72550 #type complete TITLE methylmalonyl-CoA mutase (EC 5.4.99.2) chain A [similarity] - Aeropyrum pernix (strain K1) ALTERNATE_NAMES protein APE1687 ORGANISM #formal_name Aeropyrum pernix DATE 18-Feb-2000 #sequence_revision 18-Feb-2000 #text_change 16-Jun-2000 ACCESSIONS C72550 REFERENCE A72450 !$#authors Kawarabayasi, Y.; Hino, Y.; Horikawa, H.; Yamazaki, S.; !1Haikawa, Y.; Jin-no, K.; Takahashi, M.; Sekine, M.; Baba, !1S.; Ankai, A.; Kosugi, H.; Hosoyama, A.; Fukui, S.; Nagai, !1Y.; Nishijima, K.; Nakazawa, H.; Takamiya, M.; Masuda, S.; !1Funahashi, T.; Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, !1N.; Oguchi, A.; Aoki, K.; Kubota, K.; Nakamura, Y.; Nomura, !1N.; Sako, Y.; Kikuchi, H. !$#journal DNA Res. (1999) 6:83-101 !$#title Complete genome sequence of an aerobic hyper-thermophilic !1Crenarchaeon, Aeropyrum pernix K1. !$#cross-references MUID:99310339; PMID:10382966 !$#accession C72550 !'##molecule_type DNA !'##residues 1-565 ##label KAW !'##cross-references DDBJ:AP000062; NID:g5105244; PIDN:BAA80688.1; !1PID:g5105375 !'##experimental_source strain K1 GENETICS !$#gene APE1687 FUNCTION !$#description catalyzes the isomerisation of L-methylmalonyl-CoA to !1succinyl-CoA !$#pathway valine, isoleucine, threonine, methionine, odd-chain fatty !1acid and cholesterol catabolism CLASSIFICATION #superfamily Streptomyces isobutyryl-CoA mutase chain A KEYWORDS intramolecular transferase; isomerase SUMMARY #length 565 #molecular-weight 64884 #checksum 8919 SEQUENCE /// ENTRY B35255 #type complete TITLE chloromuconate cycloisomerase (EC 5.5.1.7) - Alcaligenes eutrophus plasmid pJP4 ALTERNATE_NAMES muconate cycloisomerase II ORGANISM #formal_name Alcaligenes eutrophus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS B35255; S03395; JQ0175 REFERENCE A35255 !$#authors Perkins, E.J.; Gordon, M.P.; Caceres, O.; Lurquin, P.F. !$#journal J. Bacteriol. (1990) 172:2351-2359 !$#title Organization and sequence analysis of the 2,4-dichlorophenol !1hydroxylase and dichlorocatechol oxidative operons of !1plasmid pJP4. !$#cross-references MUID:90236889; PMID:2185214 !$#accession B35255 !'##status preliminary !'##molecule_type DNA !'##residues 1-370 ##label PER !'##cross-references GB:M35097; NID:g150766; PIDN:AAA98263.1; !1PID:g150768; GB:X07754 REFERENCE S03394 !$#authors Perkins, E.J.; Bolton, G.W.; Gordon, M.P.; Lurquin, P.F. !$#journal Nucleic Acids Res. (1988) 16:7200 !$#title Partial nucleotide sequence of the chlorocatechol !1degradative operon tfdCDEF of pJP4 and similarity to !1promoters of the chlorinated aromatic degradative operons !1tfdA and clcABD. !$#cross-references MUID:88303359; PMID:3405772 !$#accession S03395 !'##status translation not shown !'##molecule_type DNA !'##residues 1-166 ##label PE2 !'##cross-references EMBL:X07754; NID:g38789; PIDN:CAA30580.1; !1PID:g580708 REFERENCE JQ0175 !$#authors Ghosal, D.; You, I.S. !$#journal Gene (1989) 83:225-232 !$#title Operon structure and nucleotide homology of the !1chlorocatechol oxidation genes of plasmids pJP4 and pAC27. !$#cross-references MUID:90060834; PMID:2583528 !$#accession JQ0175 !'##molecule_type DNA !'##residues 1-305,'RLHSAYLRFHA',317,'VRL','RTV',326-370 ##label GHO !'##cross-references GB:M31458; NID:g150772; PIDN:AAA98267.1; !1PID:g150773 !'##experimental_source strain JMP134 !'##note the authors translated the codon GTG for residue 1 as Val, GAA !1for residue 287 as Gln, and GAG for residue 340 as Gly GENETICS !$#gene tfdD !$#genome plasmid !$#start_codon GTG CLASSIFICATION #superfamily muconate cycloisomerase KEYWORDS intramolecular lyase; isomerase SUMMARY #length 370 #molecular-weight 39722 #checksum 7917 SEQUENCE /// ENTRY B43673 #type complete TITLE chloromuconate cycloisomerase (EC 5.5.1.7) II [validated] - Pseudomonas sp. (strain P51) ORGANISM #formal_name Pseudomonas sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B43673 REFERENCE A43673 !$#authors van der Meer, J.R.; Eggen, R.I.L.; Zehnder, A.J.B.; de Vos, !1W.M. !$#journal J. Bacteriol. (1991) 173:2425-2434 !$#title Sequence analysis of the Pseudomonas sp. strain P51 tcb gene !1cluster, which encodes metabolism of chlorinated catechols: !1evidence for specialization of catechol 1,2-dioxygenases for !1chlorinated substrates. !$#cross-references MUID:91193197; PMID:2013566 !$#accession B43673 !'##status preliminary !'##molecule_type DNA !'##residues 1-370 ##label VAN !'##cross-references GB:M57629; NID:g4249353; PIDN:AAD13626.1; !1PID:g151578 GENETICS !$#gene tcbD FUNCTION !$#description EC 5.5.1.7 [validated, MUID:91193197]; involved in !1degradation of chlorinated benzenes CLASSIFICATION #superfamily muconate cycloisomerase KEYWORDS intramolecular lyase; isomerase SUMMARY #length 370 #molecular-weight 39487 #checksum 3413 SEQUENCE /// ENTRY F69991 #type complete TITLE N-acylamino acid racemase homolog ytfD - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS F69991 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69991 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-371 ##label KUN !'##cross-references GB:Z99119; GB:AL009126; NID:g2635411; !1PIDN:CAB15056.1; PID:g2635562 !'##experimental_source strain 168 GENETICS !$#gene ytfD CLASSIFICATION #superfamily muconate cycloisomerase SUMMARY #length 371 #molecular-weight 41629 #checksum 6505 SEQUENCE /// ENTRY I39598 #type complete TITLE N-Acylamino acid racemase - Amycolatopsis sp. ORGANISM #formal_name Amycolatopsis sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS I39598 REFERENCE I39598 !$#authors Tokuyama, S.; Hatano, K. !$#journal Appl. Microbiol. Biotechnol. (1995) 42:884-889 !$#title Cloning, DNA sequencing and heterologous expression of the !1gene for thermostable n-acylamino acid racemase from !1amycolatopsis sp. ts-1-60 in escherichia coli. !$#cross-references MUID:95226080; PMID:7766089 !$#accession I39598 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-368 ##label RES !'##cross-references GB:D30738; NID:g975626; PIDN:BAA06400.1; !1PID:g975627 GENETICS !$#gene aaaR !$#start_codon GTG CLASSIFICATION #superfamily muconate cycloisomerase SUMMARY #length 368 #molecular-weight 39406 #checksum 4606 SEQUENCE /// ENTRY H69855 #type complete TITLE chloromuconate cycloisomerase homolog ykfB - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS H69855 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69855 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-366 ##label KUN !'##cross-references GB:Z99110; GB:AL009126; NID:g2633472; !1PIDN:CAB13155.1; PID:g2633652 !'##experimental_source strain 168 GENETICS !$#gene ykfB CLASSIFICATION #superfamily muconate cycloisomerase SUMMARY #length 366 #molecular-weight 39472 #checksum 8039 SEQUENCE /// ENTRY A28630 #type complete TITLE muconate cycloisomerase (EC 5.5.1.1) - Pseudomonas putida ALTERNATE_NAMES Muconate cycloisomerase I; muconate lactonizing enzyme I ORGANISM #formal_name Pseudomonas putida DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A28630; A27316 REFERENCE A28630 !$#authors Aldrich, T.L.; Chakrabarty, A.M. !$#journal J. Bacteriol. (1988) 170:1297-1304 !$#title Transcriptional regulation, nucleotide sequence, and !1localization of the promoter of the catBC operon in !1Pseudomonas putida. !$#cross-references MUID:88139192; PMID:2449420 !$#accession A28630 !'##molecule_type DNA !'##residues 1-375 ##label ALD !'##cross-references EMBL:M19460; NID:g151124; PIDN:AAA25766.1; !1PID:g151125 !'##note the authors translated the codon ACC for residue 65 as Ser REFERENCE A94667 !$#authors Aldrich, T.L.; Frantz, B.; Gill, J.F.; Kilbane, J.J.; !1Chakrabarty, A.M. !$#journal Gene (1987) 52:185-195 !$#title Cloning and complete nucleotide sequence determination of !1the catB gene encoding cis,cis-muconate lactonizing enzyme. !$#cross-references MUID:87277391; PMID:3609743 !$#accession A27316 !'##molecule_type DNA !'##residues 1-32,'T',34-64,'S',66-375 ##label AL2 !'##experimental_source strain PRS2015 GENETICS !$#gene catB CLASSIFICATION #superfamily muconate cycloisomerase KEYWORDS intramolecular lyase; isomerase SUMMARY #length 375 #molecular-weight 40509 #checksum 6422 SEQUENCE /// ENTRY C69512 #type complete TITLE muconate cycloisomerase II (clcB) homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C69512 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession C69512 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-375 ##label KLE !'##cross-references GB:AE000959; GB:AE000782; NID:g2689282; !1PIDN:AAB89156.1; PID:g2648434; TIGR:AF2099 CLASSIFICATION #superfamily muconate cycloisomerase SUMMARY #length 375 #molecular-weight 42824 #checksum 2379 SEQUENCE /// ENTRY ISPJCA #type complete TITLE chalcone isomerase (EC 5.5.1.6) A - garden petunia ALTERNATE_NAMES chalcone flavonone isomerase A ORGANISM #formal_name Petunia x hybrida #common_name garden petunia DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 18-Jun-1999 ACCESSIONS S04725; JQ0963; S00547 REFERENCE S04725 !$#authors van Tunen, A.J.; Hartman, S.A.; Mur, L.A.; Mol, J.N.M. !$#journal Plant Mol. Biol. (1989) 12:539-551 !$#title Regulation of chalcone flavanone isomerase (CHI) gene !1expression in Petunia hybrida: the use of alternative !1promoters in corolla, anthers and pollen. !$#accession S04725 !'##molecule_type DNA !'##residues 1-241 ##label VAN1 !'##cross-references EMBL:X14589; NID:g20517; PIDN:CAA32729.1; !1PID:g20518 REFERENCE JQ0962 !$#authors van Tunen, A.J.; Mur, L.A.; Recourt, K.; Gerats, A.G.M.; !1Mol, J.N.M. !$#journal Plant Cell (1991) 3:39-48 !$#title Regulation and manipulation of flavonoid gene expression in !1anthers of petunia: the molecular basis of the Po mutation. !$#cross-references MUID:92404743; PMID:1824333 !$#accession JQ0963 !'##molecule_type DNA !'##residues 1-241 ##label VAN2 !'##experimental_source var. V30 REFERENCE S00547 !$#authors van Tunen, A.J.; Koes, R.E.; Spelt, C.E.; van der Krol, !1A.R.; Stuitje, A.R.; Mol, J.N.M. !$#journal EMBO J. (1988) 7:1257-1263 !$#title Cloning of the two chalcone flavanone isomerase genes from !1Petunia hybrida: coordinate, light-regulated and !1differential expression of flavonoid genes. !$#cross-references MUID:88312574; PMID:3409864 !$#accession S00547 !'##molecule_type mRNA !'##residues 1-241 ##label VAN3 !'##cross-references EMBL:Y00852; NID:g20515; PIDN:CAA68769.1; !1PID:g20516 !'##experimental_source var. V30 COMMENT This enzyme catalyzes the stereo-specific isomerization of !1naringenin chalcone into flavanones. GENETICS !$#gene chiA !$#introns #status absent CLASSIFICATION #superfamily chalcone isomerase KEYWORDS flavonoid biosynthesis; intramolecular lyase; isomerase SUMMARY #length 241 #molecular-weight 26089 #checksum 7298 SEQUENCE /// ENTRY ISPJA1 #type complete TITLE chalcone isomerase (EC 5.5.1.6) A - garden petunia (var. V31) ORGANISM #formal_name Petunia x hybrida #common_name garden petunia DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 18-Nov-1994 ACCESSIONS JQ0962 REFERENCE JQ0962 !$#authors van Tunen, A.J.; Mur, L.A.; Recourt, K.; Gerats, A.G.M.; !1Mol, J.N.M. !$#journal Plant Cell (1991) 3:39-48 !$#title Regulation and manipulation of flavonoid gene expression in !1anthers of petunia: the molecular basis of the Po mutation. !$#cross-references MUID:92404743; PMID:1824333 !$#accession JQ0962 !'##status translation not shown !'##molecule_type DNA !'##residues 1-241 ##label VAN COMMENT This enzyme is responsible for the isomerization of !1naringenin chalcone into naringenin flavonone. GENETICS !$#gene chiA CLASSIFICATION #superfamily chalcone isomerase KEYWORDS flavonoid biosynthesis; intramolecular lyase; isomerase SUMMARY #length 241 #molecular-weight 26091 #checksum 8097 SEQUENCE /// ENTRY ISPJCB #type complete TITLE chalcone isomerase (EC 5.5.1.6) B - garden petunia ALTERNATE_NAMES chalcone flavonone isomerase B ORGANISM #formal_name Petunia x hybrida #common_name garden petunia DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 18-Jun-1999 ACCESSIONS S04726 REFERENCE S04725 !$#authors van Tunen, A.J.; Hartman, S.A.; Mur, L.A.; Mol, J.N.M. !$#journal Plant Mol. Biol. (1989) 12:539-551 !$#title Regulation of chalcone flavanone isomerase (CHI) gene !1expression in Petunia hybrida: the use of alternative !1promoters in corolla, anthers and pollen. !$#accession S04726 !'##molecule_type DNA !'##residues 1-220 ##label VAN !'##cross-references EMBL:X14590; NID:g20519; PIDN:CAA32730.1; !1PID:g295827 COMMENT This enzyme catalyzes the stereospecific isomerization of !1naringenin chalcone into flavanones. GENETICS !$#gene chiB !$#introns 36/1; 89/1; 163/3 CLASSIFICATION #superfamily chalcone isomerase KEYWORDS flavonoid biosynthesis; intramolecular lyase; isomerase SUMMARY #length 220 #molecular-weight 23944 #checksum 9871 SEQUENCE /// ENTRY ISECTP #type complete TITLE DNA topoisomerase (EC 5.99.1.2) - Escherichia coli (strain K-12) ALTERNATE_NAMES nicking-closing enzyme; omega-protein; relaxing enzyme; swivelase; type I DNA topoisomerase; untwisting enzyme ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 21-Nov-1997 #text_change 01-Mar-2002 ACCESSIONS E64875; A25786; C26695 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64875 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-865 ##label BLAT !'##cross-references GB:AE000225; GB:U00096; NID:g1787523; !1PIDN:AAC74356.1; PID:g1787529; UWGP:b1274 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A92931 !$#authors Tse-Dinh, Y.C.; Wang, J.C. !$#journal J. Mol. Biol. (1986) 191:321-331 !$#title Complete nucleotide sequence of the topA gene encoding !1Escherichia coli DNA topoisomerase I. !$#cross-references MUID:87141163; PMID:3029379 !$#accession A25786 !'##molecule_type DNA !'##residues 1-121,'R',123-142,'A',144-165,'R',167-203,'A',205-280,'S', !1282-283,'L',285-353,'R',355-575,'VSR',580,'VRKRVVCARTR', !1592-635,'V',637-653,'KP',656-865 ##label TSE REFERENCE A92642 !$#authors Ostrowski, J.; Jagura-Burdzy, G.; Kredich, N.M. !$#journal J. Biol. Chem. (1987) 262:5999-6005 !$#title DNA sequences of the cysB regions of Salmonella typhimurium !1and Escherichia coli. !$#cross-references MUID:87194810; PMID:3032952 !$#accession C26695 !'##molecule_type DNA !'##residues 698-786,'R',788-865 ##label OST !'##cross-references GB:M15041; GB:J02687; NID:g145663; PIDN:AAA23641.1; !1PID:g145664 GENETICS !$#gene topA; supX !$#map_position 28 min FUNCTION !$#description catalyzes ATP-independent transient breakage of DNA !1phosphodiester bonds (one strand at a time), and the !1subsequent passage of a single strand across the break in !1another, followed by rejoining; this reaction will lead to !1the conversion of one topological isomer of DNA to another CLASSIFICATION #superfamily bacterial type I DNA topoisomerase KEYWORDS DNA binding; DNA replication; isomerase; monomer; zinc !1finger FEATURE !$599-736 #domain zinc finger #status predicted #label ZNF\ !$319 #active_site Tyr #status predicted SUMMARY #length 865 #molecular-weight 97349 #checksum 2161 SEQUENCE /// ENTRY ISBYT3 #type complete TITLE DNA topoisomerase (EC 5.99.1.2) III - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES nicking-closing enzyme; omega-protein; protein L8083.3; protein YLR234w; relaxing enzyme; swivelase; type I DNA topoisomerase; untwisting enzyme ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 21-Jul-2000 ACCESSIONS A33169; S51455 REFERENCE A33169 !$#authors Wallis, J.W.; Chrebet, G.; Brodsky, G.; Rolfe, M.; !1Rothstein, R. !$#journal Cell (1989) 58:409-419 !$#title A hyper-recombination mutation in Saccharomyces cerevisiae !1identifies a novel eukaryotic topoisomerase. !$#cross-references MUID:89324087; PMID:2546682 !$#accession A33169 !'##molecule_type DNA !'##residues 1-656 ##label WAL !'##cross-references GB:M24939; NID:g173001; PIDN:AAA35161.1; !1PID:g173002 REFERENCE S51443 !$#authors Hallsworth, K. !$#submission submitted to the EMBL Data Library, December 1994 !$#description The sequence of S. cerevisiae cosmid 8083. !$#accession S51455 !'##molecule_type DNA !'##residues 1-656 ##label HAL !'##cross-references EMBL:U19027; NID:g609363; PIDN:AAB67406.1; !1PID:g609366; GSPDB:GN00012; MIPS:YLR234w GENETICS !$#gene SGD:TOP3; EDR1; MIPS:YLR234w !'##cross-references SGD:S0004224; MIPS:YLR234w !$#map_position 12R CLASSIFICATION #superfamily bacterial type I DNA topoisomerase KEYWORDS DNA binding; DNA replication; isomerase SUMMARY #length 656 #molecular-weight 74370 #checksum 878 SEQUENCE /// ENTRY B64506 #type complete TITLE DNA topoisomerase (EC 5.99.1.2) - Methanococcus jannaschii ALTERNATE_NAMES topoisomerase I ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B64506 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession B64506 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-761 ##label BUL !'##cross-references GB:U67605; GB:L77117; NID:g1592227; !1PIDN:AAB99673.1; PID:g1592234; TIGR:MJ1652 GENETICS !$#map_position FOR1633497-1635782 !$#start_codon GTG CLASSIFICATION #superfamily DNA topoisomerase I topA KEYWORDS isomerase SUMMARY #length 761 #molecular-weight 87832 #checksum 1218 SEQUENCE /// ENTRY E71106 #type complete TITLE probable DNA topoisomerase I - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS E71106 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession E71106 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-686 ##label KAW !'##cross-references GB:AP000003; NID:g3236130; PIDN:BAA29711.1; !1PID:g3257028 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0622 CLASSIFICATION #superfamily DNA topoisomerase I topA SUMMARY #length 686 #molecular-weight 78637 #checksum 7380 SEQUENCE /// ENTRY A69084 #type complete TITLE DNA topoisomerase I - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A69084 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession A69084 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-718 ##label MTH !'##cross-references GB:AE000921; GB:AE000666; NID:g2622744; !1PIDN:AAB86097.1; PID:g2622750 !'##experimental_source strain Delta H GENETICS !$#gene MTH1624 !$#start_codon GTG CLASSIFICATION #superfamily DNA topoisomerase I topA SUMMARY #length 718 #molecular-weight 81520 #checksum 2374 SEQUENCE /// ENTRY E69475 #type complete TITLE DNA topoisomerase I (topA) homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS E69475 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession E69475 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-663 ##label KLE !'##cross-references GB:AE000978; GB:AE000782; NID:g2689301; !1PIDN:AAB89443.1; PID:g2648740; TIGR:AF1806 CLASSIFICATION #superfamily DNA topoisomerase I topA SUMMARY #length 663 #molecular-weight 76017 #checksum 786 SEQUENCE /// ENTRY ISHUT1 #type complete TITLE DNA topoisomerase (EC 5.99.1.2) - human ALTERNATE_NAMES nicking-closing enzyme; omega-protein; relaxing enzyme; swivelase; type I DNA topoisomerase; untwisting enzyme ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS A30887; A40008; S13821; S02397; S40643; A34422 REFERENCE A30887 !$#authors D'Arpa, P.; Machlin, P.S.; Ratrie III, H.; Rothfield, N.F.; !1Cleveland, D.W.; Earnshaw, W.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:2543-2547 !$#title cDNA cloning of human DNA topoisomerase I: catalytic !1activity of a 67.7-kDa carboxyl-terminal fragment. !$#cross-references MUID:88190108; PMID:2833744 !$#accession A30887 !'##molecule_type mRNA !'##residues 1-765 ##label DAR !'##cross-references GB:J03250; NID:g339805; PIDN:AAA61207.1; !1PID:g339806 REFERENCE A40008 !$#authors Kunze, N.; Yang, G.; Doelberg, M.; Sundarp, R.; Knippers, !1R.; Richter, A. !$#journal J. Biol. Chem. (1991) 266:9610-9616 !$#title Structure of the human type I DNA topoisomerase gene. !$#cross-references MUID:91236733; PMID:1851751 !$#accession A40008 !'##molecule_type DNA !'##residues 1-144,'A',146-553,'E',555-765 ##label KUN !'##cross-references GB:M60688; GB:M60689; GB:M60690; GB:M60691; !1GB:M60692; GB:M60693; GB:M60694; GB:M60695; GB:M60696; !1GB:M60697; GB:M60698; GB:M60699; GB:M60700; GB:M60701; !1GB:M60702; GB:M60703; GB:M60704; GB:M60705; GB:M60706 REFERENCE S13821 !$#authors Kunze, N.; Klein, M.; Richter, A.; Knippers, R. !$#journal Eur. J. Biochem. (1990) 194:323-330 !$#title Structural characterization of the human DNA topoisomerase I !1gene promoter. !$#cross-references MUID:91099302; PMID:2176592 !$#accession S13821 !'##molecule_type DNA !'##residues 1-20 ##label KU2 !'##cross-references EMBL:X52601 REFERENCE S02397 !$#authors Oddou, P.; Schmidt, U.; Knippers, R.; Richter, A. !$#journal Eur. J. Biochem. (1988) 177:523-529 !$#title Monoclonal antibodies neutralizing mammalian DNA !1topoisomerase I activity. !$#cross-references MUID:89064806; PMID:2461859 !$#accession S02397 !'##molecule_type mRNA !'##residues 344-765 ##label ODD !'##cross-references GB:M60657 REFERENCE S40643 !$#authors Tamura, H.O.; Kohchi, C.; Yamada, R.; Ikeda, T.; Koiwai, O.; !1Patterson, E.; Keene, J.D.; Okada, K.; Kjeldsen, E.; !1Nishikawa, K.; Andoh, T. !$#journal Nucleic Acids Res. (1991) 19:69-75 !$#title Molecular cloning of a cDNA of a camptothecin-resistant !1human DNA topoisomerase I and identification of mutation !1sites. !$#cross-references MUID:91187651; PMID:1849260 !$#accession S40643 !'##status preliminary !'##molecule_type mRNA !'##residues 523-543;573-582,'D',584-593 ##label TAM REFERENCE A34422 !$#authors Maul, G.G.; Jimenez, S.A.; Riggs, E.; Ziemnicka-Kotula, D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:8492-8496 !$#title Determination of an epitope of the diffuse systemic !1sclerosis marker antigen DNA topoisomerase I: sequence !1similarity with retroviral p30(gag) protein suggests a !1possible cause for autoimmunity in systemic sclerosis. !$#cross-references MUID:90046823; PMID:2479024 !$#accession A34422 !'##molecule_type mRNA !'##residues 657-765 ##label MAU !'##cross-references GB:M27913; NID:g339807; PIDN:AAA61208.1; !1PID:g339808 COMMENT Type I DNA topoisomerase catalyzes the ATP-independent !1transient breakage of DNA phosphodiester bonds (one strand !1at a time), and the subsequent passage of a single strand !1across the break in another, followed by rejoining. This !1reaction will lead to the conversion of one topological !1isomer of DNA to another. GENETICS !$#gene GDB:TOP1 !'##cross-references GDB:120444; OMIM:126420 !$#map_position 20q12-20q13.1 !$#introns 11/3; 20/1 !$#note the list of introns is incomplete CLASSIFICATION #superfamily eukaryotic type I DNA topoisomerase KEYWORDS DNA binding; DNA replication; heterotetramer; isomerase FEATURE !$723 #active_site Tyr #status predicted SUMMARY #length 765 #molecular-weight 90753 #checksum 1809 SEQUENCE /// ENTRY ISBYT1 #type complete TITLE DNA topoisomerase (EC 5.99.1.2) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES nicking-closing enzyme; omega-protein; protein O2377; protein YOL006c; relaxing enzyme; swivelase; type I DNA topoisomerase; untwisting enzyme ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 21-Jul-2000 ACCESSIONS A23161; S05792; S66688 REFERENCE A23161 !$#authors Thrash, C.; Bankier, A.T.; Barrell, B.G.; Sternglanz, R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:4374-4378 !$#title Cloning, characterization, and sequence of the yeast DNA !1topoisomerase I gene. !$#cross-references MUID:85242687; PMID:2989818 !$#accession A23161 !'##molecule_type DNA !'##residues 1-769 ##label THR !'##cross-references EMBL:K03077; NID:g173003; PIDN:AAA35162.1; !1PID:g173004 REFERENCE S05792 !$#authors Lynn, R.M.; Bjornsti, M.A.; Caron, P.R.; Wang, J.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:3559-3563 !$#title Peptide sequencing and site-directed mutagenesis identify !1tyrosine-727 as the active site tyrosine of Saccharomyces !1cerevisiae DNA topoisomerase I. !$#cross-references MUID:89264463; PMID:2542938 !$#accession S05792 !'##molecule_type protein !'##residues 725-731 ##label LYN REFERENCE S66685 !$#authors Hughes, B.; Pohl, T.M. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S66688 !'##molecule_type DNA !'##residues 1-769 ##label HUG !'##cross-references EMBL:Z74748; NID:g1419770; PIDN:CAA99005.1; !1PID:g1419771; GSPDB:GN00015; MIPS:YOL006c !'##experimental_source strain S288C COMMENT The type I DNA topoisomerase catalyzes the ATP-independent !1transient breakage of DNA phosphodiester bonds (one strand !1at a time), and the subsequent passage of a single strand !1across the break in another, followed by rejoining. This !1reaction will lead to the conversion of one topological !1isomer of DNA to another. GENETICS !$#gene SGD:TOP1; MAK1; MIPS:YOL006c !'##cross-references SGD:S0005366; MIPS:YOL006c !$#map_position 15L CLASSIFICATION #superfamily eukaryotic type I DNA topoisomerase KEYWORDS DNA binding; DNA replication; heterotetramer; isomerase FEATURE !$727 #active_site Tyr #status experimental SUMMARY #length 769 #molecular-weight 89995 #checksum 4734 SEQUENCE /// ENTRY ISZPT1 #type complete TITLE DNA topoisomerase (EC 5.99.1.2) - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES nicking-closing enzyme; omega-protein; relaxing enzyme; swivelase; type I DNA topoisomerase; untwisting enzyme ORGANISM #formal_name Schizosaccharomyces pombe DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS S03329 REFERENCE S03329 !$#authors Uemura, T.; Morino, K.; Uzawa, S.; Shiozaki, K.; Yanagida, !1M. !$#journal Nucleic Acids Res. (1987) 15:9727-9739 !$#title Cloning and sequencing of Schizosaccharomyces pombe DNA !1topoisomerase I gene, and effect of gene disruption. !$#cross-references MUID:88096534; PMID:2827111 !$#accession S03329 !'##molecule_type DNA !'##residues 1-812 ##label UEM !'##cross-references EMBL:X06201; NID:g5118; PIDN:CAA29559.1; PID:g5119 COMMENT Type I DNA topoisomerase catalyzes the ATP-independent !1transient breakage of DNA phosphodiester bonds (one strand !1at a time), and the subsequent passage of a single strand !1across the break in another, followed by rejoining. This !1reaction will lead to the conversion of one topological !1isomer of DNA to another. GENETICS !$#introns 5/1; 36/3 CLASSIFICATION #superfamily eukaryotic type I DNA topoisomerase KEYWORDS DNA binding; DNA replication; heterotetramer; isomerase FEATURE !$771 #active_site Tyr #status predicted SUMMARY #length 812 #molecular-weight 93838 #checksum 2468 SEQUENCE /// ENTRY ISBYT2 #type complete TITLE DNA topoisomerase (ATP-hydrolyzing) (EC 5.99.1.3) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES DNA gyrase; DNA topoisomerase II; protein N2244; protein YNL088w ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1992 #sequence_revision 10-Nov-1995 #text_change 16-Jun-2000 ACCESSIONS S57534; A25630; S63027; S30866; S65093 REFERENCE S57533 !$#authors Soler-Mira, A.; Saiz, J.E.; Ballesta, J.P.G.; Remacha, M. !$#submission submitted to the EMBL Data Library, June 1995 !$#accession S57534 !'##molecule_type DNA !'##residues 1-1428 ##label SOL !'##cross-references EMBL:X89016; NID:g887621; PIDN:CAA61422.1; !1PID:g887623 REFERENCE A25630 !$#authors Giaever, G.; Lynn, R.; Goto, T.; Wang, J.C. !$#journal J. Biol. Chem. (1986) 261:12448-12454 !$#title The complete nucleotide sequence of the structural gene TOP2 !1of yeast DNA topoisomerase II. !$#cross-references MUID:86304413; PMID:3017975 !$#accession A25630 !'##molecule_type DNA !'##residues 1-74,'N',75-546,'L',548-836,'R',838-1428 ##label GIA !'##cross-references GB:M13814; NID:g172997; PIDN:AAB36610.1; !1PID:g172998 REFERENCE S63018 !$#authors Soler-Mira, A.; Saiz, J.E.; Ballesta, J.P.G.; Remacha, M. !$#submission submitted to the Protein Sequence Database, April 1996 !$#accession S63027 !'##molecule_type DNA !'##residues 1-1428 ##label SOW !'##cross-references EMBL:Z71364; NID:g1301988; PIDN:CAA95964.1; !1PID:g1301989; GSPDB:GN00014; MIPS:YNL088w !'##experimental_source strain S288C REFERENCE S30866 !$#authors Jannatipour, M.; Liu, Y.X.; Nitiss, J.L. !$#submission submitted to the EMBL Data Library, January 1993 !$#description The top2-5 mutant of yeast topoisomerase II encodes an !1enzyme resistant to etoposide and amsacrine. !$#accession S30866 !'##molecule_type DNA !'##residues 812-836,'R',838-882,'P',884,'II',887-977 ##label JAN !'##cross-references EMBL:L08968; NID:g172999; PIDN:AAB59328.1; !1PID:g173000 REFERENCE S65092 !$#authors Soler-Mira, A.; Saiz, J.E.; Ballesta, J.P.G.; Remacha, M. !$#journal Yeast (1996) 12:485-491 !$#title The sequence of a 17 933 bp segment of Saccharomyces !1cerevisiae chromosome XIV contains the RHO2, TOP2, MKT1 and !1END3 genes and five new open reading frames. !$#cross-references MUID:96310628; PMID:8740422 !$#accession S65093 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-1428 ##label SOF !'##cross-references EMBL:X89016; NID:g887621; PIDN:CAA61422.1; !1PID:g887623 COMMENT Type II DNA topoisomerase catalyzes the ATP-dependent !1transient breakage, passage, and rejoining of !1double-stranded DNA. GENETICS !$#gene SGD:TOP2; TOR3; TRF3; TOP2-5; MIPS:YNL088w !'##cross-references SGD:S0005032; MIPS:YNL088w !$#map_position 14L CLASSIFICATION #superfamily eukaryotic type II DNA topoisomerase; phage T4 !1DNA topoisomerase (ATP-hydrolyzing) medium chain homology KEYWORDS ATP; DNA binding; DNA replication; heterotetramer; !1isomerase; phosphoprotein SUMMARY #length 1428 #molecular-weight 164213 #checksum 815 SEQUENCE /// ENTRY ISZPT2 #type complete TITLE DNA topoisomerase (ATP-hydrolyzing) (EC 5.99.1.3) - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES DNA-gyrase; type II DNA topoisomerase ORGANISM #formal_name Schizosaccharomyces pombe DATE 30-Sep-1992 #sequence_revision 01-Dec-2000 #text_change 01-Dec-2000 ACCESSIONS T39851; A24897 REFERENCE Z21885 !$#authors Wood, V.; Rajandream, M.A.; Barrell, B.G.; Volckaert, G. !$#submission submitted to the EMBL Data Library, July 1998 !$#accession T39851 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-1485 ##label WOO !'##cross-references EMBL:AL031174; PIDN:CAA20107.1; GSPDB:GN00067 !'##experimental_source strain 972h-; cosmid c1A4 REFERENCE A24897 !$#authors Uemura, T.; Morikawa, K.; Yanagida, M. !$#journal EMBO J. (1986) 5:2355-2361 !$#title The nucleotide sequence of the fission yeast DNA !1topoisomerase II gene: structural and functional !1relationships to other DNA topoisomerases. !$#cross-references MUID:87053875; PMID:3023070 !$#accession A24897 !'##molecule_type DNA !'##residues 55-993,'I',995-1485 ##label UEM !'##cross-references GB:X04326; NID:g5120; PIDN:CAA27857.1; PID:g5121 COMMENT Type II DNA topoisomerase catalyzes the ATP-dependent !1transient breakage, passage, and rejoining og !1double-stranded DNA. GENETICS !$#gene top2 !$#map_position 2 !$#introns 28/3 CLASSIFICATION #superfamily eukaryotic type II DNA topoisomerase; phage T4 !1DNA topoisomerase (ATP-hydrolyzing) medium chain homology KEYWORDS ATP; DNA binding; DNA replication; heterotetramer; isomerase SUMMARY #length 1485 #molecular-weight 167891 #checksum 2132 SEQUENCE /// ENTRY ISXFAS #type complete TITLE DNA topoisomerase (ATP-hydrolyzing) (EC 5.99.1.3) - African swine fever virus ALTERNATE_NAMES DNA-gyrase; type II DNA topoisomerase ORGANISM #formal_name African swine fever virus, ASFV DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 18-Jun-1999 ACCESSIONS B42549 REFERENCE A42549 !$#authors Garcia-Beato, R.; Freije, J.M.P.; Lopez-Otin, C.; Blasco, !1R.; Vinuela, E.; Salas, M.L. !$#journal Virology (1992) 188:938-947 !$#title A gene homologous to topoisomerase II in African swine fever !1virus. !$#cross-references MUID:92263807; PMID:1316688 !$#accession B42549 !'##molecule_type DNA !'##residues 1-1192 ##label GAR !'##cross-references GB:M88699; NID:g210652; PIDN:AAA42735.1; !1PID:g210654 CLASSIFICATION #superfamily eukaryotic type II DNA topoisomerase; phage T4 !1DNA topoisomerase (ATP-hydrolyzing) medium chain homology KEYWORDS ATP; DNA binding; DNA replication; heterotetramer; isomerase FEATURE !$800 #active_site Tyr #status predicted SUMMARY #length 1192 #molecular-weight 135543 #checksum 1858 SEQUENCE /// ENTRY ISECTB #type complete TITLE DNA topoisomerase (ATP-hydrolyzing) (EC 5.99.1.3) chain B - Escherichia coli (strain K-12) ALTERNATE_NAMES DNA gyrase B chain; type II DNA topoisomerase B chain ORGANISM #formal_name Escherichia coli DATE 30-Sep-1988 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS D65172; A26444; A26953; C22168; A38344 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65172 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-804 ##label BLAT !'##cross-references GB:AE000447; GB:U00096; NID:g2367266; !1PIDN:AAC76722.1; PID:g1790134; UWGP:b3699 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A93674 !$#authors Adachi, T.; Mizuuchi, M.; Robinson, E.A.; Appella, E.; !1O'Dea, M.H.; Gellert, M.; Mizuuchi, K. !$#journal Nucleic Acids Res. (1987) 15:771-784 !$#title DNA sequence of the E. coli gyrB gene: application of a new !1sequencing strategy. !$#cross-references MUID:87146392; PMID:3029692 !$#accession A26444 !'##molecule_type DNA !'##residues 1-384,'A',386-804 ##label ADA !'##cross-references GB:X04341; GB:X00870; NID:g41643; PIDN:CAA27871.1; !1PID:g41646 REFERENCE A26953 !$#authors Menzel, R.; Gellert, M. !$#journal J. Bacteriol. (1987) 169:1272-1278 !$#title Fusions of the Escherichia coli gyrA and gyrB control !1regions to the galactokinase gene are inducible by !1coumermycin treatment. !$#cross-references MUID:87137287; PMID:3029031 !$#accession A26953 !'##molecule_type DNA !'##residues 1-23 ##label MEN !'##cross-references GB:M15548; NID:g146307; PIDN:AAA23949.1; !1PID:g146308 REFERENCE A22168 !$#authors Adachi, T.; Mizuuchi, K.; Menzel, R.; Gellert, M. !$#journal Nucleic Acids Res. (1984) 12:6389-6395 !$#title DNA sequence and transcription of the region upstream of the !1E. coli gyrB gene. !$#cross-references MUID:84297235; PMID:6089112 !$#accession C22168 !'##molecule_type DNA !'##residues 1-50,'R',52-55,'L',57-106 ##label AD2 REFERENCE A38344 !$#authors Tamura, J.K.; Gellert, M. !$#journal J. Biol. Chem. (1990) 265:21342-21349 !$#title Characterization of the ATP binding site on Escherichia coli !1DNA gyrase. Affinity labeling of Lys-103 and Lys-110 of the !1B subunit by pyridoxal 5'-diphospho-5'-adenosine. !$#cross-references MUID:91065955; PMID:2174443 !$#accession A38344 !'##molecule_type protein !'##residues 93-126,'X',128-129 ##label TAM !'##note Lys-103 and Lys-110 were shown to bind covalently to the ATP !1analog and DNA gyrase inhibitor pyridoxal !15'-diphospho-5'-adenosine (PLP-AMP) COMMENT DNA gyrase, which catalyzes DNA supercoiling and relaxing, !1is made up of two chains. The A chain is responsible for DNA !1breakage and rejoining; the B chain catalyzes ATP !1hydrolysis. GENETICS !$#gene gyrB !$#map_position 83 min CLASSIFICATION #superfamily DNA topoisomerase (ATP-hydrolyzing) chain B KEYWORDS antibiotic resistance; ATP; DNA supercoiling; isomerase FEATURE !$93-129 #region ATP-binding SUMMARY #length 804 #molecular-weight 89975 #checksum 2976 SEQUENCE /// ENTRY A64078 #type complete TITLE DNA topoisomerase (ATP-hydrolyzing) (EC 5.99.1.3) chain B - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A64078 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession A64078 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-806 ##label TIGR !'##cross-references GB:U32738; GB:L42023; NID:g1573548; !1PIDN:AAC22225.1; PID:g1573554; TIGR:HI0567 CLASSIFICATION #superfamily DNA topoisomerase (ATP-hydrolyzing) chain B KEYWORDS antibiotic resistance; ATP; DNA supercoiling; isomerase SUMMARY #length 806 #molecular-weight 89884 #checksum 6120 SEQUENCE /// ENTRY S12608 #type complete TITLE DNA topoisomerase (ATP-hydrolyzing) (EC 5.99.1.3) chain B - Pseudomonas putida ALTERNATE_NAMES DNA gyrase chain gyrB; type II DNA topoisomerase chain B ORGANISM #formal_name Pseudomonas putida DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S12608; PV0002 REFERENCE S12608 !$#authors Parales, R.E.; Harwood, C.S. !$#journal Nucleic Acids Res. (1990) 18:5880 !$#title Nucleotide sequence of the gyrB gene of Pseudomonas putida. !$#cross-references MUID:91016930; PMID:2170947 !$#accession S12608 !'##molecule_type DNA !'##residues 1-806 ##label PAR !'##cross-references EMBL:X54631; NID:g45693; PIDN:CAA38447.1; !1PID:g45694 REFERENCE JV0002 !$#authors Fujita, M.Q.; Yoshikawa, H.; Ogasawara, N. !$#journal Mol. Gen. Genet. (1989) 215:381-387 !$#title Structure of the dnaA region of Pseudomonas putida: !1conservation among three bacteria, Bacillus subtilis, !1Escherichia coli and P. putida. !$#cross-references MUID:89218947; PMID:2540413 !$#accession PV0002 !'##molecule_type DNA !'##residues 1-47 ##label FUJ !'##cross-references GB:X14792; NID:g45724; PIDN:CAA32897.1; PID:g45725 GENETICS !$#gene gyrB CLASSIFICATION #superfamily DNA topoisomerase (ATP-hydrolyzing) chain B KEYWORDS antibiotic resistance; isomerase SUMMARY #length 806 #molecular-weight 90077 #checksum 7647 SEQUENCE /// ENTRY A49794 #type complete TITLE DNA topoisomerase (ATP-hydrolyzing) (EC 5.99.1.3) chain B, nalidixic acid-resistant - Neisseria gonorrhoeae (strain MUG116) ORGANISM #formal_name Neisseria gonorrhoeae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A49794 REFERENCE A49794 !$#authors Stein, D.C.; Danaher, R.J.; Cook, T.M. !$#journal Antimicrob. Agents Chemother. (1991) 35:622-626 !$#title Characterization of a gyrB mutation responsible for !1low-level nalidixic acid resistance in Neisseria !1gonorrhoeae. !$#cross-references MUID:91298684; PMID:1906260 !$#accession A49794 !'##status preliminary !'##molecule_type DNA !'##residues 1-781 ##label STE !'##cross-references GB:M59981 CLASSIFICATION #superfamily DNA topoisomerase (ATP-hydrolyzing) chain B KEYWORDS isomerase SUMMARY #length 781 #molecular-weight 86575 #checksum 431 SEQUENCE /// ENTRY ISYMBP #type complete TITLE DNA topoisomerase (ATP-hydrolyzing) (EC 5.99.1.3) chain B - Mycoplasma pneumoniae ALTERNATE_NAMES DNA topoisomerase type II chain B; DNA-gyrase chain B ORGANISM #formal_name Mycoplasma pneumoniae DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 21-Jan-2000 ACCESSIONS S11767; S62834; S73477; S14630 REFERENCE S11767 !$#authors Colman, S.D.; Hu, P.C.; Bott, K.F. !$#journal Mol. Microbiol. (1990) 4:1129-1134 !$#title Mycoplasma pneumoniae DNA gyrase genes. !$#cross-references MUID:91041721; PMID:2172693 !$#accession S11767 !'##molecule_type DNA !'##residues 1-650 ##label COL !'##cross-references EMBL:X53555; NID:g44483; PIDN:CAA37622.1; !1PID:g44484 !'##experimental_source ATCC 29342; clone MP202 REFERENCE S62797 !$#authors Hilbert, H.; Himmelreich, R.; Plagens, H.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:628-639 !$#title Sequence analysis of 56 kb from the genome of the bacterium !1Mycoplasma pneumoniae comprising the dnaA region, the atp !1operon and a cluster of ribosomal protein genes. !$#cross-references MUID:96177562; PMID:8604303 !$#accession S62834 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-637 ##label HIL !'##cross-references EMBL:U34816; NID:g1209514; PIDN:AAC43643.1; !1PID:g1209515 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1995 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73477 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-650 ##label HIM !'##cross-references EMBL:AE000016; GB:U00089; NID:g1673796; !1PIDN:AAB95799.1; PID:g1673811 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#gene gyrB !$#genetic_code SGC3 CLASSIFICATION #superfamily DNA topoisomerase (ATP-hydrolyzing) chain B KEYWORDS antibiotic resistance; ATP; heterotetramer; isomerase SUMMARY #length 650 #molecular-weight 73809 #checksum 2458 SEQUENCE /// ENTRY A39135 #type complete TITLE DNA topoisomerase chain B homolog - Haloferax sp. ORGANISM #formal_name Haloferax sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A39135 REFERENCE A39135 !$#authors Holmes, M.L.; Dyall-Smith, M.L. !$#journal J. Bacteriol. (1991) 173:642-648 !$#title Mutations in DNA gyrase result in novobiocin resistance in !1halophilic archaebacteria. !$#cross-references MUID:91100352; PMID:1846146 !$#accession A39135 !'##status preliminary !'##molecule_type DNA !'##residues 1-639 ##label HOL !'##cross-references GB:M38373; NID:g149022; PIDN:AAB09605.1; !1PID:g149024 CLASSIFICATION #superfamily DNA topoisomerase (ATP-hydrolyzing) chain B SUMMARY #length 639 #molecular-weight 71137 #checksum 3953 SEQUENCE /// ENTRY E22930 #type complete TITLE DNA topoisomerase (ATP-hydrolyzing) (EC 5.99.1.3) chain B (gyrB) - Bacillus subtilis ALTERNATE_NAMES DNA gyrase chain B ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS E22930; S66036; H69638 REFERENCE A94702 !$#authors Moriya, S.; Ogasawara, N.; Yoshikawa, H. !$#journal Nucleic Acids Res. (1985) 13:2251-2265 !$#title Structure and function of the region of the replication !1origin of the Bacillus subtilis chromosome. III. Nucleotide !1sequence of some 10,000 base pairs in the origin region. !$#cross-references MUID:85215612; PMID:2987847 !$#accession E22930 !'##molecule_type DNA !'##residues 1-638 ##label MOR !'##cross-references GB:D26185; NID:g467326; PIDN:BAA05242.1; !1PID:g467396 !'##note the authors translated the codon GAG for residue 131 as Gly, !1CCG for residue 449 as Arg, CTT for residue 450 as Gly, AGA !1for residue 451 as Lys, and GGT for residue 452 as Ile REFERENCE S65967 !$#authors Ogasawara, N.; Nakai, S.; Yoshikawa, H. !$#journal DNA Res. (1994) 1:1-14 !$#title Systematic sequencing of the 180 kilobase region of the !1Bacillus subtilis chromosome containing the replication !1origin. !$#cross-references MUID:96051385; PMID:7584024 !$#accession S66036 !'##status preliminary !'##molecule_type DNA !'##residues 1-638 ##label OGA !'##cross-references EMBL:D26185; NID:g467326; PIDN:BAA05242.1; !1PID:g467396 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69638 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-638 ##label KUN !'##cross-references GB:Z99104; GB:AL009126; NID:g2632267; !1PIDN:CAB11782.1; PID:g2632273 !'##experimental_source strain 168 GENETICS !$#gene gyrB !$#map_position 0 CLASSIFICATION #superfamily DNA topoisomerase (ATP-hydrolyzing) chain B KEYWORDS isomerase SUMMARY #length 638 #molecular-weight 71503 #checksum 6653 SEQUENCE /// ENTRY A40585 #type complete TITLE DNA topoisomerase (ATP-hydrolyzing) (EC 5.99.1.3) chain B - Staphylococcus aureus ORGANISM #formal_name Staphylococcus aureus DATE 07-Apr-1994 #sequence_revision 10-May-1996 #text_change 18-Feb-2000 ACCESSIONS A40585; A35406; S54711; A42295; S36024 REFERENCE A40585 !$#authors Brockbank, S.M.V.; Barth, P.T. !$#journal J. Bacteriol. (1993) 175:3269-3277 !$#title Cloning, sequencing, and expression of the DNA gyrase genes !1from Staphylococcus aureus. !$#cross-references MUID:93273692; PMID:8388872 !$#accession A40585 !'##status preliminary !'##molecule_type DNA !'##residues 1-644 ##label BRO !'##cross-references EMBL:X71437; NID:g296393; PIDN:CAA50570.1; !1PID:g296395 !'##note part of this sequence was confirmed by protein sequencing REFERENCE A35406 !$#authors Hopewell, R.; Oram, M.; Briesewitz, R.; Fisher, L.M. !$#journal J. Bacteriol. (1990) 172:3481-3484 !$#title DNA cloning and organization of the Staphylococcus aureus !1gyrA and gyrB genes: close homology among gyrase proteins !1and implications for 4-quinolone action and resistance. !$#cross-references MUID:90264350; PMID:2160946 !$#accession A35406 !'##status preliminary !'##molecule_type DNA !'##residues 593-644 ##label HOP !'##cross-references GB:M37915; NID:g153023; PIDN:AAA26635.1; !1PID:g153024 REFERENCE S54707 !$#authors Alonso, J.C.; Fisher, L.M. !$#journal Mol. Gen. Genet. (1995) 246:680-686 !$#title Nucleotide sequence of the recF gene cluster from !1Staphylococcus aureus and complementation analysis in !1Bacillus subtilis recF mutants. !$#cross-references MUID:95206242; PMID:7898435 !$#accession S54711 !'##status preliminary !'##molecule_type DNA !'##residues 1-30 ##label ALO REFERENCE A42295 !$#authors Margerrison, E.E.C.; Hopewell, R.; Fisher, L.M. !$#journal J. Bacteriol. (1992) 174:1596-1603 !$#title Nucleotide sequence of the Staphylococcus aureus gyrB-gyrA !1locus encoding the DNA gyrase A and B proteins. !$#cross-references MUID:92165734; PMID:1311298 !$#accession A42295 !'##status preliminary !'##molecule_type DNA !'##residues 1-39,'QRE','L',46,'ISV',50-65,'K',67-311,'RY',316-317, !1'EKIA',322-423,'Q',425-521,'I',523-578,'L',580-644 ##label !1MAR !'##cross-references GB:M86227; NID:g153083; PIDN:AAA73951.1; !1PID:g153085 GENETICS !$#gene gyrB CLASSIFICATION #superfamily DNA topoisomerase (ATP-hydrolyzing) chain B KEYWORDS antibiotic resistance; isomerase SUMMARY #length 644 #molecular-weight 72539 #checksum 1348 SEQUENCE /// ENTRY S44198 #type complete TITLE DNA topoisomerase (ATP-hydrolyzing) (EC 5.99.1.3) - Mycobacterium tuberculosis (strain H37RV) ALTERNATE_NAMES DNA gyrase chain B ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S44198; C70698 REFERENCE S44198 !$#authors Madhusudan, K.; Ramesh, V.; Nagaraja, V. !$#submission submitted to the EMBL Data Library, April 1994 !$#description DNA gyrase genes from Mycobacterium tuberculosis: Cloning !1and nucleic seqeunce analysis of gyrB. !$#accession S44198 !'##molecule_type DNA !'##residues 1-714 ##label MAD !'##cross-references EMBL:X78888; NID:g474434; PIDN:CAA55486.1; !1PID:g474435 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession C70698 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-714 ##label COL !'##cross-references GB:Z80233; GB:AL123456; NID:g3261645; !1PIDN:CAB02426.1; PID:g1552558 !'##experimental_source strain H37Rv GENETICS !$#gene gyrB CLASSIFICATION #superfamily DNA topoisomerase (ATP-hydrolyzing) chain B KEYWORDS isomerase SUMMARY #length 714 #molecular-weight 78439 #checksum 1358 SEQUENCE /// ENTRY ISBPT4 #type complete TITLE DNA topoisomerase (ATP-hydrolyzing) (EC 5.99.1.3) large chain - phage T4 ALTERNATE_NAMES DNA topoisomerase II; DNA-gyrase; gp 39 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Feb-1997 ACCESSIONS A25763; B25763; S01755 REFERENCE A25763 !$#authors Huang, W.M. !$#journal Nucleic Acids Res. (1986) 14:7751-7765 !$#title Nucleotide sequence of a type II DNA topoisomerase gene. !1Bacteriophage T4 gene 39. !$#cross-references MUID:87040739; PMID:3022233 !$#accession A25763 !'##molecule_type DNA !'##residues 1-520 ##label HUA !$#accession B25763 !'##molecule_type protein !'##residues 1-15 ##label HU2 COMMENT This protein differs from the other prokaryotic type II DNA !1topoisomerase, DNA gyrase, in that it can only remove !1superhelical twists in an ATP-dependent reaction rather than !1introducing supercoils. GENETICS !$#gene 39 !$#map_position 3.772-5.332 COMPLEX The enzyme consists of three polypeptide chains, the !1products of genes 39, 52, and gp 60. FUNCTION !$#description the topoisomerase exhibits the following multiple activities !1in vitro: the DNA strand passage reaction, which results in !1the relaxation of superhelical DNA; the related reactions of !1knotting, unknotting, catenation, and decatenation of !1circular DNA; DNA-dependent ATPase activity; DNA binding; !1the induced double-stranded DNA cleavage reaction and the !1covalent transfer of one of the protein chains to the !15'-ends of the cleaved DNA !$#pathway T4 DNA replication; initiation of chromosomal DNA !1replication !$#note large chain regulates specificity of T even phage DNA !1replication and has ATPase activity CLASSIFICATION #superfamily DNA topoisomerase (ATP-hydrolyzing) chain B KEYWORDS DNA binding; DNA replication; isomerase SUMMARY #length 520 #molecular-weight 58471 #checksum 4282 SEQUENCE /// ENTRY ITECAP #type complete TITLE DNA topoisomerase (ATP-hydrolyzing) (EC 5.99.1.3) chain A [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES DNA gyrase chain A; type II DNA topoisomerase chain A ORGANISM #formal_name Escherichia coli DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 01-Mar-2002 ACCESSIONS S02340; S01344; S03758; S29538; A60453; B26953; E64993 REFERENCE S02340 !$#authors Swanberg, S.L.; Wang, J.C. !$#journal J. Mol. Biol. (1987) 197:729-736 !$#title Cloning and sequencing of the Escherichia coli gyrA gene !1coding for the A subunit of DNA gyrase. !$#cross-references MUID:88118900; PMID:2828631 !$#accession S02340 !'##molecule_type DNA !'##residues 1-875 ##label SWA !'##cross-references EMBL:X06373; NID:g41635; PIDN:CAA29676.1; !1PID:g41636 REFERENCE S01344 !$#authors Yoshida, H.; Kojima, T.; Yamagishi, J.; Nakamura, S. !$#journal Mol. Gen. Genet. (1988) 211:1-7 !$#title Quinolone-resistant mutations of the gyrA gene of !1Escherichia coli. !$#cross-references MUID:88142556; PMID:2830458 !$#accession S01344 !'##molecule_type DNA !'##residues 1-875 ##label YOS !'##cross-references EMBL:X06744; NID:g41633; PIDN:CAA29919.1; !1PID:g41634 REFERENCE S03757 !$#authors Hussain, K.; Elliott, E.J.; Salmond, G.P.C. !$#journal Mol. Microbiol. (1987) 1:259-273 !$#title The ParD(-) mutant of Escherichia coli also carries a gyrA !1(am) mutation. The complete sequence of gyrA. !$#cross-references MUID:88201664; PMID:2834621 !$#accession S03758 !'##molecule_type DNA !'##residues 1-794,'IMM',795-875 ##label HUS !'##cross-references EMBL:Y00544 REFERENCE S29538 !$#authors Miki, T.; Park, J.R.; Nagao, K.; Horiuchi, T. !$#submission submitted to the EMBL Data Library, January 1991 !$#accession S29538 !'##molecule_type DNA !'##residues 1-213,'E',215-875 ##label MIK !'##cross-references EMBL:X57174; NID:g41641; PIDN:CAA40461.1; !1PID:g41642 REFERENCE A60453 !$#authors Cullen, M.E.; Wyke, A.W.; Kuroda, R.; Fisher, L.M. !$#journal Antimicrob. Agents Chemother. (1989) 33:886-894 !$#title Cloning and characterization of a DNA gyrase A gene from !1Escherichia coli that confers clinical resistance to !14-quinolones. !$#cross-references MUID:89350134; PMID:2548439 !$#accession A60453 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-82,'W',84-677,'E',679-827,'S',829-875 ##label CUL !'##note this sequence is from a quinolone-resistant uropathogenic !1strain of Escherichia coli (clinical isolate 227) REFERENCE A26953 !$#authors Menzel, R.; Gellert, M. !$#journal J. Bacteriol. (1987) 169:1272-1278 !$#title Fusions of the Escherichia coli gyrA and gyrB control !1regions to the galactokinase gene are inducible by !1coumermycin treatment. !$#cross-references MUID:87137287; PMID:3029031 !$#accession B26953 !'##molecule_type DNA !'##residues 1-88 ##label MEN !'##cross-references GB:M15631; NID:g146305; PIDN:AAA23948.1; !1PID:g146306 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64993 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-875 ##label BLAT !'##cross-references GB:AE000312; GB:U00096; NID:g1788555; !1PIDN:AAC75291.1; PID:g1788562; UWGP:b2231 !'##experimental_source strain K-12, substrain MG1655 COMMENT The A chain is the target of quinolone antibiotics such as !1nalidixic acid and enoxacin. COMMENT Substitution of Trp for Ser at position 83 confers !1resistance to a variety of quinolone antibiotics. GENETICS !$#gene gyrA !$#map_position 48 min FUNCTION !$#description EC 5.99.1.3 [validated, MUID:89350134] CLASSIFICATION #superfamily DNA topoisomerase (ATP-hydrolyzing) chain A; !1phage T4 DNA topoisomerase (ATP-hydrolyzing) medium chain !1homology KEYWORDS ATP; DNA binding; DNA replication; heterotetramer; isomerase FEATURE !$1-238 #domain phage T4 DNA topoisomerase (ATP-hydrolyzing) !8medium chain homology #label T4T\ !$122 #active_site Tyr #status predicted SUMMARY #length 875 #molecular-weight 96963 #checksum 9191 SEQUENCE /// ENTRY E64113 #type complete TITLE DNA topoisomerase (ATP-hydrolyzing) (EC 5.99.1.3) chain A - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES DNA gyrase chain A; type II DNA topoisomerase chain A ORGANISM #formal_name Haemophilus influenzae DATE 18-Aug-1995 #sequence_revision 16-Aug-1996 #text_change 18-Jun-1999 ACCESSIONS E64113 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession E64113 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-880 ##label TIGR !'##cross-references GB:U32806; GB:L42023; NID:g1574717; !1PIDN:AAC22917.1; PID:g1574722; TIGR:HI1264 GENETICS !$#gene gyrA CLASSIFICATION #superfamily DNA topoisomerase (ATP-hydrolyzing) chain A; !1phage T4 DNA topoisomerase (ATP-hydrolyzing) medium chain !1homology KEYWORDS ATP; isomerase FEATURE !$1-239 #domain phage T4 DNA topoisomerase (ATP-hydrolyzing) !8medium chain homology #label T4T SUMMARY #length 880 #molecular-weight 97817 #checksum 9938 SEQUENCE /// ENTRY B40585 #type complete TITLE DNA topoisomerase (ATP-hydrolyzing) (EC 5.99.1.3) chain A - Staphylococcus aureus ALTERNATE_NAMES DNA gyrase ORGANISM #formal_name Staphylococcus aureus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B40585; B42295; B35406; A37856; S36025 REFERENCE A40585 !$#authors Brockbank, S.M.V.; Barth, P.T. !$#journal J. Bacteriol. (1993) 175:3269-3277 !$#title Cloning, sequencing, and expression of the DNA gyrase genes !1from Staphylococcus aureus. !$#cross-references MUID:93273692; PMID:8388872 !$#accession B40585 !'##status preliminary !'##molecule_type DNA !'##residues 1-886 ##label BRO !'##cross-references GB:X71437; NID:g296393; PIDN:CAA50571.1; !1PID:g296396 REFERENCE A42295 !$#authors Margerrison, E.E.C.; Hopewell, R.; Fisher, L.M. !$#journal J. Bacteriol. (1992) 174:1596-1603 !$#title Nucleotide sequence of the Staphylococcus aureus gyrB-gyrA !1locus encoding the DNA gyrase A and B proteins. !$#cross-references MUID:92165734; PMID:1311298 !$#accession B42295 !'##status preliminary !'##molecule_type DNA !'##residues 1-438,'D',440-482,'D',484-593,'E',595-708,'E',710-814,'E', !1815-816,'T',818-824,'ST',825-852,'E',854-856,'T',858,'D', !1860-880,'L',882-886 ##label MAR !'##cross-references GB:M86227; NID:g153083; PIDN:AAA73952.1; !1PID:g153086 REFERENCE A35406 !$#authors Hopewell, R.; Oram, M.; Briesewitz, R.; Fisher, L.M. !$#journal J. Bacteriol. (1990) 172:3481-3484 !$#title DNA cloning and organization of the Staphylococcus aureus !1gyrA and gyrB genes: close homology among gyrase proteins !1and implications for 4-quinolone action and resistance. !$#cross-references MUID:90264350; PMID:2160946 !$#accession B35406 !'##status preliminary !'##molecule_type DNA !'##residues 1-146 ##label HOP !'##cross-references GB:M37915; NID:g153023; PIDN:AAA26636.1; !1PID:g153025 REFERENCE A37856 !$#authors Sreedharan, S.; Oram, M.; Jensen, B.; Peterson, L.R.; !1Fisher, L.M. !$#journal J. Bacteriol. (1990) 172:7260-7262 !$#title DNA gyrase gyrA mutations in ciprofloxacin-resistant strains !1of Staphylococcus aureus: close similarity with quinolone !1resistance mutations in Escherichia coli. !$#cross-references MUID:91072282; PMID:2174869 !$#accession A37856 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 81-91 ##label SRE GENETICS !$#gene gyrA CLASSIFICATION #superfamily DNA topoisomerase (ATP-hydrolyzing) chain A; !1phage T4 DNA topoisomerase (ATP-hydrolyzing) medium chain !1homology KEYWORDS ATP; DNA binding; DNA replication; isomerase FEATURE !$1-239 #domain phage T4 DNA topoisomerase (ATP-hydrolyzing) !8medium chain homology #label T4T\ !$123 #active_site Tyr #status predicted SUMMARY #length 886 #molecular-weight 99216 #checksum 5010 SEQUENCE /// ENTRY S73476 #type complete TITLE DNA topoisomerase (ATP-hydrolyzing) (EC 5.99.1.3) chain A - Mycoplasma pneumoniae (strain ATCC 29342) ALTERNATE_NAMES DNA gyrase chain A; DNA topoisomerase type II chain A; hypothetical protein D12_orf839o ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S73476; S11768; S14631 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73476 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-839 ##label HIM !'##cross-references EMBL:AE000016; GB:U00089; NID:g1673796; !1PIDN:AAB95798.1; PID:g1673810 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 REFERENCE S11767 !$#authors Colman, S.D.; Hu, P.C.; Bott, K.F. !$#journal Mol. Microbiol. (1990) 4:1129-1134 !$#title Mycoplasma pneumoniae DNA gyrase genes. !$#cross-references MUID:91041721; PMID:2172693 !$#accession S11768 !'##molecule_type DNA !'##residues 1-156 ##label COL !'##cross-references EMBL:X53555; NID:g44483; PIDN:CAA37623.1; !1PID:g44485 GENETICS !$#gene serS; gyrA !$#genetic_code SGC3 CLASSIFICATION #superfamily DNA topoisomerase (ATP-hydrolyzing) chain A; !1phage T4 DNA topoisomerase (ATP-hydrolyzing) medium chain !1homology KEYWORDS ATP; DNA binding; DNA recombination; DNA repair; DNA !1replication; heterotetramer; isomerase; nucleotide binding; !1P-loop FEATURE !$12-250 #domain phage T4 DNA topoisomerase (ATP-hydrolyzing) !8medium chain homology #label T4T\ !$724-731 #region nucleotide-binding motif A (P-loop)\ !$134 #active_site Tyr #status predicted SUMMARY #length 839 #molecular-weight 93356 #checksum 2751 SEQUENCE /// ENTRY F22930 #type complete TITLE DNA topoisomerase (ATP-hydrolyzing) (EC 5.99.1.3) chain A (gyrA) - Bacillus subtilis ALTERNATE_NAMES DNA gyrase chain A ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS F22930; S66037; G69638 REFERENCE A94702 !$#authors Moriya, S.; Ogasawara, N.; Yoshikawa, H. !$#journal Nucleic Acids Res. (1985) 13:2251-2265 !$#title Structure and function of the region of the replication !1origin of the Bacillus subtilis chromosome. III. Nucleotide !1sequence of some 10,000 base pairs in the origin region. !$#cross-references MUID:85215612; PMID:2987847 !$#accession F22930 !'##molecule_type DNA !'##residues 1-821 ##label MOR !'##cross-references GB:D26185; NID:g467326; PIDN:BAA05243.1; !1PID:g467397 REFERENCE S65967 !$#authors Ogasawara, N.; Nakai, S.; Yoshikawa, H. !$#journal DNA Res. (1994) 1:1-14 !$#title Systematic sequencing of the 180 kilobase region of the !1Bacillus subtilis chromosome containing the replication !1origin. !$#cross-references MUID:96051385; PMID:7584024 !$#accession S66037 !'##status preliminary !'##molecule_type DNA !'##residues 1-821 ##label OGA !'##cross-references EMBL:D26185; NID:g467326; PIDN:BAA05243.1; !1PID:g467397 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69638 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-821 ##label KUN !'##cross-references GB:Z99104; GB:AL009126; NID:g2632267; !1PIDN:CAB11783.1; PID:g2632274 !'##experimental_source strain 168 GENETICS !$#gene gyrA !$#map_position 0 CLASSIFICATION #superfamily DNA topoisomerase (ATP-hydrolyzing) chain A; !1phage T4 DNA topoisomerase (ATP-hydrolyzing) medium chain !1homology KEYWORDS ATP; DNA binding; DNA replication; isomerase FEATURE !$1-239 #domain phage T4 DNA topoisomerase (ATP-hydrolyzing) !8medium chain homology #label T4T\ !$123 #active_site Tyr #status predicted SUMMARY #length 821 #molecular-weight 92098 #checksum 3504 SEQUENCE /// ENTRY ITKBAP #type complete TITLE DNA topoisomerase (ATP-hydrolyzing) (EC 5.99.1.3) chain A - Klebsiella pneumoniae ALTERNATE_NAMES gyrase chain A ORGANISM #formal_name Klebsiella pneumoniae DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 18-Jun-1999 ACCESSIONS S07722; S12489 REFERENCE S07722 !$#authors Dimri, G.P.; Das, H.K. !$#journal Nucleic Acids Res. (1990) 18:151-156 !$#title Cloning and sequence analysis of gyrA gene of Klebsiella !1pneumoniae. !$#cross-references MUID:90174909; PMID:2155395 !$#accession S07722 !'##molecule_type DNA !'##residues 1-876 ##label DIM !'##cross-references EMBL:X16817 !'##note the authors translated the codon GAG for residue 545 as Gln and !1CCG for residue 569 as Ala REFERENCE S12489 !$#authors Das, H.K. !$#submission submitted to the EMBL Data Library, October 1989 !$#accession S12489 !'##molecule_type DNA !'##residues 1-282,'E',284-876 ##label DAS !'##cross-references EMBL:X16817; NID:g43807; PIDN:CAA34724.1; !1PID:g43808 GENETICS !$#gene gyrA CLASSIFICATION #superfamily DNA topoisomerase (ATP-hydrolyzing) chain A; !1phage T4 DNA topoisomerase (ATP-hydrolyzing) medium chain !1homology KEYWORDS ATP; DNA binding; DNA replication; heterotetramer; isomerase FEATURE !$1-238 #domain phage T4 DNA topoisomerase (ATP-hydrolyzing) !8medium chain homology #label T4T\ !$122 #active_site Tyr #status predicted SUMMARY #length 876 #molecular-weight 97140 #checksum 9506 SEQUENCE /// ENTRY ISBP24 #type complete TITLE DNA topoisomerase (ATP-hydrolyzing) (EC 5.99.1.3) small chain - phage T4 ALTERNATE_NAMES DNA topoisomerase II; DNA-gyrase; gp 60 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 18-Jun-1999 ACCESSIONS JT0209; PS0194; PS0461 REFERENCE JT0209 !$#authors Huang, W.M.; Ao, S.Z.; Casjens, S.; Orlandi, R.; Zeikus, R.; !1Weiss, R.; Winge, D.; Fang, M. !$#journal Science (1988) 239:1005-1012 !$#title A persistent untranslated sequence within bacteriophage T4 !1DNA topoisomerase gene 60. !$#cross-references MUID:88145641; PMID:2830666 !$#accession JT0209 !'##molecule_type DNA !'##residues 1-160 ##label HUA !'##cross-references EMBL:M19728; NID:g215845; PIDN:AAA32490.1; !1PID:g215846 REFERENCE PS0194 !$#authors Daegelen, P.; Brody, E. !$#journal Genetics (1990) 125:237-248 !$#title The rIIA gene of bacteriophage T4. I. Its DNA sequence and !1discovery of a new open reading frame between genes 60 and !1rIIA. !$#cross-references MUID:90337270; PMID:2379817 !$#accession PS0194 !'##molecule_type DNA !'##residues 70-160 ##label DAE !'##cross-references GB:X52686; GB:X00905; NID:g15177; PIDN:CAA36909.1; !1PID:g836601 !$#accession PS0461 !'##molecule_type protein !'##residues 1-15 ##label HU2 COMMENT This protein differs from the other prokaryotic type II DNA !1topoisomerase, DNA gyrase, in that it can only remove !1superhelical twists in an ATP-dependent reaction rather than !1introducing supercoils. COMMENT In the translation of gene 60 mRNA, fifty nucleotides are !1skipped at the 46th residue by the ribosome because of the !1formation of an RNA hairpin structure. GENETICS !$#gene 60 !$#map_position 2.460-2.802/2.852-2.990 COMPLEX The enzyme consists of three polypeptide chains, the !1products of genes 39, 52, and gp 60. FUNCTION !$#description the topoisomerase exhibits the following multiple activities !1in vitro: the DNA strand passage reaction, which results in !1the relaxation of superhelical DNA; the related reactions of !1knotting, unknotting, catenation, and decatenation of !1circular DNA; DNA-dependent ATPase activity; DNA binding; !1the induced double-stranded DNA cleavage reaction and the !1covalent transfer of one of the protein chains to the !15'-ends of the cleaved DNA !$#pathway T4 DNA replication; initiation of chromosomal DNA !1replication CLASSIFICATION #superfamily phage T4 DNA topoisomerase small chain KEYWORDS DNA binding; DNA replication; isomerase SUMMARY #length 160 #molecular-weight 18630 #checksum 4836 SEQUENCE /// ENTRY ITBPT4 #type complete TITLE DNA topoisomerase (ATP-hydrolyzing) (EC 5.99.1.3) medium chain - phage T4 ALTERNATE_NAMES DNA topoisomerase II; DNA-gyrase ORGANISM #formal_name phage T4 DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 05-Jun-1998 ACCESSIONS B24705; S01872 REFERENCE A24705 !$#authors Huang, W.M. !$#journal Nucleic Acids Res. (1986) 14:7379-7390 !$#title The 52-protein subunit of T4 DNA topoisomerase is homologous !1to the gyrA-protein of gyrase. !$#cross-references MUID:87016377; PMID:3020513 !$#accession B24705 !'##molecule_type DNA !'##residues 1-441 ##label HUA REFERENCE S01711 !$#authors Chapman, D.; Morad, I.; Kaufmann, G.; Gait, M.J.; Jorissen, !1L.; Snyder, L. !$#journal J. Mol. Biol. (1988) 199:373-377 !$#title Nucleotide and deduced amino acid sequence of stp: the !1bacteriophage T4 anticodon nuclease gene. !$#cross-references MUID:88172481; PMID:3280805 !$#accession S01872 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-46 ##label CHA GENETICS !$#gene 52 !$#map_position 162-164 kb COMPLEX this is the middle-sized of the three subunits of T4 DNA !1topoisomerase CLASSIFICATION #superfamily phage T4 DNA topoisomerase (ATP-hydrolyzing) !1medium chain; phage T4 DNA topoisomerase (ATP-hydrolyzing) !1medium chain homology KEYWORDS DNA binding; DNA replication; isomerase FEATURE !$1-225 #domain phage T4 DNA topoisomerase (ATP-hydrolyzing) !8medium chain homology #label TOP SUMMARY #length 441 #molecular-weight 50576 #checksum 2141 SEQUENCE /// ENTRY QQVZH7 #type complete TITLE poxvirus DNA topoisomerase 1 (EC 5.99.1.-) - vaccinia virus ALTERNATE_NAMES H6R protein ORGANISM #formal_name vaccinia virus DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 18-Feb-2000 ACCESSIONS G24481; F42514; A39886; T37372 REFERENCE A93022 !$#authors Rosel, J.L.; Earl, P.L.; Weir, J.P.; Moss, B. !$#journal J. Virol. (1986) 60:436-449 !$#title Conserved TAAATG sequence at the transcriptional and !1translational initiation sites of vaccinia virus late genes !1deduced by structural and functional analysis of the HindIII !1H genome fragment. !$#cross-references MUID:87036903; PMID:3021979 !$#accession G24481 !'##molecule_type DNA !'##residues 1-314 ##label ROS !'##cross-references GB:M13209; NID:g335739; PIDN:AAB59842.1; !1PID:g893338 !'##experimental_source strain WR REFERENCE A33172 !$#authors Johnson, G.P. !$#submission submitted to GenBank, June 1990 !$#accession F42514 !'##molecule_type DNA !'##residues 1-314 ##label JOH !'##experimental_source strain Copenhagen REFERENCE A39886 !$#authors Shuman, S.; Moss, B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:7478-7482 !$#title Identification of a vaccinia virus gene encoding a type I !1DNA topoisomerase. !$#cross-references MUID:88041129; PMID:2823264 !$#accession A39886 !'##status preliminary !'##molecule_type protein !'##residues 1-22 ##label SHU REFERENCE Z20877 !$#authors Antoine, G.; Scheiflinger, F.; Falkner, F.G.; Dorner, F. !$#submission submitted to the EMBL Data Library, March 1997 !$#description The complete genomic sequence of the Modified Vaccinia !1Ankara (MVA) strain. !$#accession T37372 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-314 ##label ANT !'##cross-references EMBL:U94848; PIDN:AAB96509.1 !'##experimental_source strain Ankara GENETICS !$#note MVA096R CLASSIFICATION #superfamily vaccinia virus DNA topoisomerase KEYWORDS DNA binding; DNA replication; isomerase SUMMARY #length 314 #molecular-weight 36665 #checksum 368 SEQUENCE /// ENTRY E36846 #type complete TITLE poxvirus DNA topoisomerase (EC 5.99.1.-) - variola virus ALTERNATE_NAMES I6R protein ORGANISM #formal_name variola virus DATE 30-Sep-1993 #sequence_revision 08-Feb-1996 #text_change 23-Mar-2001 ACCESSIONS E36846; S33103 REFERENCE A36859 !$#authors Blinov, V.M. !$#submission submitted to GenBank, November 1992 !$#accession E36846 !'##status preliminary !'##molecule_type DNA !'##residues 1-314 ##label BLI !'##cross-references GB:X69198; NID:g456758; PIDN:CAA49030.1; !1PID:g297269 !'##experimental_source strain India-1967 REFERENCE S33069 !$#authors Shchelkunov, S.N.; Blinov, V.M.; Totmenin, A.V.; !1Marennikova, S.S.; Kolykhalov, A.A.; Frolov, I.V.; !1Chizhikov, V.E.; Gytorov, V.V.; Gashikov, P.V.; Belanov, !1E.F.; Belavin, P.A.; Resenchuk, S.M.; Andzhaparidze, O.G.; !1Sandakhchiev, L.S. !$#journal Virus Res. (1993) 27:25-35 !$#title Nucleotide sequence analysis of variola virus HindIII M, L, !1I genome fragments. !$#cross-references MUID:93190624; PMID:8383392 !$#accession S33103 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-314 ##label SHC !'##cross-references EMBL:X67119; NID:g62330; PIDN:CAA47588.1; !1PID:g62365 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1992 CLASSIFICATION #superfamily vaccinia virus DNA topoisomerase KEYWORDS DNA binding; DNA replication; isomerase SUMMARY #length 314 #molecular-weight 36591 #checksum 972 SEQUENCE /// ENTRY ITVZKA #type complete TITLE poxvirus DNA topoisomerase (EC 5.99.1.-) - rabbit fibroma virus (strain Kazsa) ORGANISM #formal_name rabbit fibroma virus, Shope fibroma virus DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 18-Jun-1999 ACCESSIONS A34769 REFERENCE A34769 !$#authors Upton, C.; Opgenorth, A.; Traktman, P.; McFadden, G. !$#journal Virology (1990) 176:439-447 !$#title Identification and DNA sequence of the Shope fibroma virus !1DNA topoisomerase gene. !$#cross-references MUID:90266459; PMID:2161144 !$#accession A34769 !'##molecule_type DNA !'##residues 1-314 ##label UPT !'##cross-references EMBL:M31723; NID:g333617; PIDN:AAA47228.1; !1PID:g333618 CLASSIFICATION #superfamily vaccinia virus DNA topoisomerase KEYWORDS DNA binding; DNA replication; isomerase SUMMARY #length 314 #molecular-weight 36999 #checksum 9642 SEQUENCE /// ENTRY ISECFI #type complete TITLE L-fuculose isomerase (EC 5.3.1.-) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 01-Mar-2002 ACCESSIONS JS0185; F65062; S49564 REFERENCE S04702 !$#authors Lu, Z.; Lin, E.C.C. !$#journal Nucleic Acids Res. (1989) 17:4883-4884 !$#title The nucleotide sequence of Escherichia coli genes for !1L-fucose dissimilation. !$#cross-references MUID:89315234; PMID:2664711 !$#accession JS0185 !'##molecule_type DNA !'##residues 1-591 ##label LUZ !'##cross-references GB:X15025; NID:g41501; PIDN:CAA33127.1; PID:g41505 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65062 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-591 ##label BLAT !'##cross-references GB:AE000364; GB:U00096; NID:g2367162; !1PIDN:AAC75844.1; PID:g1789167; UWGP:b2802 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S49564 !$#authors Gunn, F.J.; Tate, C.G.; Henderson, P.J.F. !$#journal Mol. Microbiol. (1994) 12:799-809 !$#title Identification of a novel sugar-H(+) symport protein, FucP, !1for transport of L-fucose into Escherichia coli. !$#cross-references MUID:94328931; PMID:8052131 !$#accession S49564 !'##molecule_type protein !'##residues 1-7,'P',9 ##label GUN COMMENT This protein is an isomerase involved in an inducible !1catabolic pathway for L-fucose. GENETICS !$#gene fucI !$#map_position 60 min CLASSIFICATION #superfamily isomerase fucI KEYWORDS intramolecular oxidoreductase; isomerase; L-fucose !1catabolism; L-fucose utilization SUMMARY #length 591 #molecular-weight 64976 #checksum 6283 SEQUENCE /// ENTRY SYECYT #type complete TITLE tyrosine-tRNA ligase (EC 6.1.1.1) - Escherichia coli (strain K-12) ALTERNATE_NAMES tyrosyl-tRNA synthetase ORGANISM #formal_name Escherichia coli DATE 13-Jun-1983 #sequence_revision 04-Oct-1996 #text_change 03-Jun-2002 ACCESSIONS A01178; C43261; G64920 REFERENCE A01178 !$#authors Barker, D.G.; Bruton, C.J.; Winter, G. !$#journal FEBS Lett. (1982) 150:419-423 !$#title The tyrosyl-tRNA synthetase from Escherichia coli: complete !1nucleotide sequence of the structural gene. !$#cross-references MUID:83132295; PMID:6761148 !$#accession A01178 !'##molecule_type DNA !'##residues 2-424 ##label BAR !'##cross-references GB:J01719; NID:g148093; PIDN:AAA24707.1; !1PID:g148094 !'##note the initiator Met, which is removed after translation, is not !1shown REFERENCE A43261 !$#authors Lam, H.M.; Winkler, M.E. !$#journal J. Bacteriol. (1992) 174:6033-6045 !$#title Characterization of the complex pdxH-tyrS operon of !1Escherichia coli K-12 and pleiotropic phenotypes caused by !1pdxH insertion mutations. !$#cross-references MUID:93015640; PMID:1356963 !$#accession C43261 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-16 ##label LAM !'##cross-references GB:M92351; NID:g148095; PIDN:AAA24710.1; !1PID:g148098 !'##note sequence extracted from NCBI backbone (NCBIP:115107) REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64920 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-424 ##label BLAT !'##cross-references GB:AE000259; GB:U00096; NID:g1787921; !1PIDN:AAC74709.1; PID:g1787925; UWGP:b1637 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene tyrS !$#map_position 36 min COMPLEX homodimer FUNCTION !$#description catalyzes the ATP-dependent ligation of L-tyrosine to tRNA !1(tyr) CLASSIFICATION #superfamily tyrosine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; homodimer; ligase; protein !1biosynthesis SUMMARY #length 424 #molecular-weight 47527 #checksum 9815 SEQUENCE /// ENTRY SYBSYF #type complete TITLE tyrosine-tRNA ligase (EC 6.1.1.1) - Bacillus stearothermophilus ALTERNATE_NAMES tyrosyl-tRNA synthetase ORGANISM #formal_name Bacillus stearothermophilus DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 03-Jun-2002 ACCESSIONS A01179; I40506 REFERENCE A01179 !$#authors Winter, G.; Koch, G.L.E.; Hartley, B.S.; Barker, D.G. !$#journal Eur. J. Biochem. (1983) 132:383-387 !$#title The amino acid sequence of the tyrosyl-tRNA synthetase from !1Bacillus stearothermophilus. !$#cross-references MUID:83182471; PMID:6840095 !$#accession A01179 !'##molecule_type DNA !'##residues 1-419 ##label WIN !'##cross-references GB:J01546 REFERENCE I40503 !$#authors Waye, M.M.; Winter, G. !$#journal Eur. J. Biochem. (1986) 158:505-510 !$#title A transcription terminator in the 5' non-coding region of !1the tyrosyl tRNA synthetase gene from Bacillus !1stearothermophilus. !$#cross-references MUID:86274732; PMID:3525162 !$#accession I40506 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-11 ##label RES !'##cross-references EMBL:X04193; NID:g40233; PIDN:CAA27784.1; !1PID:g40235 FUNCTION !$#description catalyzes the ATP-dependent ligation of L-tyrosine to tRNA !1(tyr) CLASSIFICATION #superfamily tyrosine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; homodimer; ligase; protein !1biosynthesis SUMMARY #length 419 #molecular-weight 47302 #checksum 8288 SEQUENCE /// ENTRY SYBSYX #type complete TITLE tyrosine-tRNA ligase (EC 6.1.1.1) - Bacillus caldotenax ALTERNATE_NAMES tyrosyl-tRNA synthetase ORGANISM #formal_name Bacillus caldotenax DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 03-Jun-2002 ACCESSIONS A01180 REFERENCE A01180 !$#authors Jones, M.D.; Lowe, D.M.; Borgford, T.; Fersht, A.R. !$#journal Biochemistry (1986) 25:1887-1891 !$#title Natural variation of tyrosyl-tRNA synthetase and comparison !1with engineered mutants. !$#cross-references MUID:86216102; PMID:3011073 !$#accession A01180 !'##molecule_type DNA !'##residues 1-419 ##label JON !'##cross-references GB:M13148; NID:g143792; PIDN:AAA22877.1; !1PID:g143793 FUNCTION !$#description catalyzes the ATP-dependent ligation of L-tyrosine to tRNA !1(tyr) CLASSIFICATION #superfamily tyrosine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; homodimer; ligase; protein !1biosynthesis SUMMARY #length 419 #molecular-weight 47201 #checksum 7324 SEQUENCE /// ENTRY A42648 #type complete TITLE tyrosine-tRNA ligase (EC 6.1.1.1) tyrS, major - Bacillus subtilis ALTERNATE_NAMES tyrosyl-tRNA synthetase tyrS ORGANISM #formal_name Bacillus subtilis DATE 31-Dec-1993 #sequence_revision 06-Feb-1995 #text_change 03-Jun-2002 ACCESSIONS A42648; S39647; E69728 REFERENCE A42648 !$#authors Henkin, T.M.; Glass, B.L.; Grundy, F.J. !$#journal J. Bacteriol. (1992) 174:1299-1306 !$#title Analysis of the Bacillus subtilis tyrS gene: conservation of !1a regulatory sequence in multiple tRNA synthetase genes. !$#cross-references MUID:92138624; PMID:1735721 !$#accession A42648 !'##molecule_type DNA !'##residues 1-422 ##label HEN !'##cross-references GB:M77668; NID:g143794; PIDN:AAA22878.1; !1PID:g143795 REFERENCE S39641 !$#authors Grundy, F.J.; Waters, D.A.; Takova, T.Y.; Henkin, T.M. !$#journal Mol. Microbiol. (1993) 10:259-271 !$#title Identification of genes involved in utilization of acetate !1and acetoin in Bacillus subtilis. !$#cross-references MUID:95020526; PMID:7934817 !$#accession S39647 !'##molecule_type DNA !'##residues 1-13 ##label GRU !'##cross-references GB:L17309; NID:g861173; PIDN:AAA68288.1; !1PID:g861176 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69728 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-422 ##label KUN !'##cross-references GB:Z99119; GB:AL009126; NID:g2635411; !1PIDN:CAB14945.1; PID:g2635451 !'##experimental_source strain 168 COMMENT This protein, unlike a second tyrosine-tRNA ligase !1designated TyrZ, is expressed well in vegetative cells. GENETICS !$#gene tyrS FUNCTION !$#description catalyzes the ATP-dependent ligation of L-tyrosine to tRNA !1(tyr) CLASSIFICATION #superfamily tyrosine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; ligase; protein biosynthesis SUMMARY #length 422 #molecular-weight 47737 #checksum 350 SEQUENCE /// ENTRY A55515 #type complete TITLE tyrosine-tRNA ligase (EC 6.1.1.1) - Thiobacillus ferrooxidans ALTERNATE_NAMES tyrosyl-tRNA synthetase ORGANISM #formal_name Thiobacillus ferrooxidans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS A55515; S12872 REFERENCE A55515 !$#authors Salazar, O.; Sagredo, B.; Jedlicki, E.; Soell, D.; !1Weygand-Durasevic, I.; Orellana, O. !$#journal J. Bacteriol. (1994) 176:4409-4415 !$#title Thiobacillus ferrooxidans tyrosyl-tRNA synthetase functions !1in vivo in Escherichia coli. !$#cross-references MUID:94292471; PMID:7517395 !$#accession A55515 !'##molecule_type DNA !'##residues 1-407 ##label SAL !'##cross-references GB:X79010; NID:g505365; PIDN:CAA55643.1; !1PID:g505366 REFERENCE S12872 !$#authors Takamiya, M.; Salazar, O.; Vargas, D.; Jedlicki, E.; !1Orellana, O. !$#journal FEBS Lett. (1990) 272:50-54 !$#title Identification and structural analysis of a ribosomal RNA !1gene promoter from Thiobacillus ferrooxidans. !$#cross-references MUID:91032140; PMID:2172018 !$#accession S12872 !'##molecule_type DNA !'##residues 279-292,'M',294-309,'RL',311-360,'IVR' ##label TAK !'##note this sequence diverges from that in reference A55515 by a frame !1shift after the amino acid at position 360 GENETICS !$#gene tyrZ CLASSIFICATION #superfamily tyrosine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; ligase; protein biosynthesis SUMMARY #length 407 #molecular-weight 45860 #checksum 7042 SEQUENCE /// ENTRY D64132 #type complete TITLE tyrosine-tRNA ligase (EC 6.1.1.1) - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES tyrosyl-tRNA synthetase ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS D64132 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession D64132 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-401 ##label TIGR !'##cross-references GB:U32834; GB:L42023; NID:g1574444; !1PIDN:AAC23254.1; PID:g1574452; TIGR:HI1610 CLASSIFICATION #superfamily tyrosine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; ligase; protein biosynthesis SUMMARY #length 401 #molecular-weight 44774 #checksum 8633 SEQUENCE /// ENTRY S16426 #type complete TITLE tyrosine-tRNA ligase (EC 6.1.1.1) TyrZ - Bacillus subtilis ALTERNATE_NAMES tyrosyl-tRNA synthetase (minor) tyrZ ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S16426; S39664; F69728 REFERENCE S16421 !$#authors Glaser, P.; Kunst, F.; Debarbouille, M.; Vertes, A.; !1Danchin, A.; Dedonder, R. !$#journal DNA Seq. (1991) 1:251-261 !$#title A gene encoding a tyrosine tRNA synthetase is located near !1sacS in Bacillus subtilis. !$#cross-references MUID:92216127; PMID:1806041 !$#accession S16426 !'##status preliminary !'##molecule_type DNA !'##residues 1-413 ##label GLA !'##cross-references EMBL:X52480; NID:g40236; PIDN:CAA36724.1; !1PID:g40242 REFERENCE S39655 !$#authors Glaser, P.; Kunst, F.; Arnaud, M.; Coudart, M.P.; Gonzales, !1W.; Hullo, M.F.; Ionescu, M.; Lubochinsky, B.; Marcelino, !1L.; Moszer, I.; Presecan, E.; Santana, M.; Schneider, E.; !1Schweizer, J.; Vertes, A.; Rapoport, G.; Danchin, A. !$#journal Mol. Microbiol. (1993) 10:371-384 !$#title Bacillus subtilis genome project: cloning and sequencing of !1the 97 kb region from 325 degrees to 333 degrees. !$#cross-references MUID:95020537; PMID:7934828 !$#accession S39664 !'##status preliminary !'##molecule_type DNA !'##residues 1-413 ##label GL2 !'##cross-references EMBL:X73124; NID:g413923; PIDN:CAA51565.1; !1PID:g413933 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69728 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-413 ##label KUN !'##cross-references GB:Z99123; GB:AL009126; NID:g2636240; !1PIDN:CAB15872.1; PID:g2636381 !'##experimental_source strain 168 GENETICS !$#gene tyrZ CLASSIFICATION #superfamily tyrosine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; ligase; protein biosynthesis SUMMARY #length 413 #molecular-weight 47100 #checksum 3163 SEQUENCE /// ENTRY SYNCYT #type complete TITLE tyrosine-tRNA ligase (EC 6.1.1.1) precursor, mitochondrial - Neurospora crassa ALTERNATE_NAMES tyrosyl-tRNA synthetase ORGANISM #formal_name Neurospora crassa DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 03-Jun-2002 ACCESSIONS A27158 REFERENCE A27158 !$#authors Akins, R.A.; Lambowitz, A.M. !$#journal Cell (1987) 50:331-345 !$#title A protein required for splicing group I introns in !1Neurospora mitochondria is mitochondrial tyrosyl-tRNA !1synthetase or a derivative thereof. !$#cross-references MUID:87273496; PMID:3607872 !$#accession A27158 !'##molecule_type DNA !'##residues 1-531 ##label AKI !'##cross-references GB:M17118 COMMENT In addition to tyrosyl-tRNA synthetase activity, this enzyme !1is involved in the splicing of the large mitochondrial rRNA !1intron and possibly other group I introns. GENETICS !$#gene cyt-18 !$#introns 82/2 CLASSIFICATION #superfamily tyrosine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; homodimer; ligase; !1mitochondrion; protein biosynthesis FEATURE !$1-32 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$33-531 #product tyrosine-tRNA ligase #status predicted !8#label MAT SUMMARY #length 531 #molecular-weight 59904 #checksum 798 SEQUENCE /// ENTRY YWBYM #type complete TITLE tryptophan-tRNA ligase (EC 6.1.1.2), mitochondrial - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein D9954.7; protein YDR268w; tryptophanyl-tRNA synthetase ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1992 #sequence_revision 07-Feb-1997 #text_change 03-Jun-2002 ACCESSIONS S70128; S26867; A25436 REFERENCE S70124 !$#authors Le, T. !$#submission submitted to the EMBL Data Library, May 1996 !$#description The sequence of S. cerevisiae cosmid 9954. !$#accession S70128 !'##molecule_type DNA !'##residues 1-379 ##label LET !'##cross-references EMBL:U51030; NID:g1332633; PIDN:AAB64452.1; !1PID:g1230641; GSPDB:GN00004; MIPS:YDR268w REFERENCE S26867 !$#authors Entrup, R.; Langgut, W.; Lisowsky, T.; Schweizer, E. !$#journal Curr. Genet. (1992) 21:281-283 !$#title An yeast nuclear mutation conferring temperature-sensitivity !1to the mitochondrial tryptophanyl-tRNA synthetase. !$#cross-references MUID:92405222; PMID:1525855 !$#accession S26867 !'##molecule_type DNA !'##residues 1-293,'S',295-379 ##label ENT !'##cross-references EMBL:X66165 REFERENCE A25436 !$#authors Myers, A.M.; Tzagoloff, A. !$#journal J. Biol. Chem. (1985) 260:15371-15377 !$#title MSW, a yeast gene coding for mitochondrial tryptophanyl-tRNA !1synthetase. !$#cross-references MUID:86059396; PMID:2999114 !$#accession A25436 !'##molecule_type DNA !'##residues 1-267,'RLE',272-370,'PTFI',375 ##label MYE !'##cross-references GB:M12081; NID:g172013; PIDN:AAA34809.1; !1PID:g172014 GENETICS !$#gene SGD:MSW1; MIPS:YDR268w !'##cross-references SGD:S0002676; MIPS:YDR268w !$#map_position 4R !$#genome nuclear CLASSIFICATION #superfamily tryptophan-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; ligase; mitochondrion; !1protein biosynthesis SUMMARY #length 379 #molecular-weight 43015 #checksum 9962 SEQUENCE /// ENTRY YWBSF #type complete TITLE tryptophan-tRNA ligase (EC 6.1.1.2) - Bacillus stearothermophilus ALTERNATE_NAMES tryptophanyl-tRNA synthetase ORGANISM #formal_name Bacillus stearothermophilus DATE 30-Nov-1980 #sequence_revision 30-Sep-1992 #text_change 03-Jun-2002 ACCESSIONS A26055; A01181 REFERENCE A26055 !$#authors Barstow, D.A.; Sharman, A.F.; Atkinson, T.; Minton, N.P. !$#journal Gene (1986) 46:37-45 !$#title Cloning and complete nucleotide sequence of the Bacillus !1stearothermophilus tryptophanyl tRNA synthetase gene. !$#cross-references MUID:87106841; PMID:3026925 !$#accession A26055 !'##molecule_type DNA !'##residues 1-328 ##label BAR !'##cross-references GB:M14742 REFERENCE A01181 !$#authors Winter, G.P.; Hartley, B.S. !$#journal FEBS Lett. (1977) 80:340-342 !$#title The amino acid sequence of tryptophanyl tRNA synthetase from !1Bacillus stearothermophilus. !$#cross-references MUID:77246821; PMID:891985 !$#accession A01181 !'##molecule_type protein !'##residues 1-31,'Z',33-40,'BZ',43-327 ##label WIN GENETICS !$#gene trpS CLASSIFICATION #superfamily tryptophan-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; ligase; protein biosynthesis SUMMARY #length 328 #molecular-weight 37177 #checksum 9481 SEQUENCE /// ENTRY YWEC #type complete TITLE tryptophan-tRNA ligase (EC 6.1.1.2) - Escherichia coli (strain K-12) ALTERNATE_NAMES tryptophanyl-tRNA synthetase ORGANISM #formal_name Escherichia coli DATE 13-Jun-1983 #sequence_revision 05-Dec-1997 #text_change 03-Jun-2002 ACCESSIONS C65133; A01182; S31745; S55290; I69352; I54844 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65133 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-334 ##label BLAT !'##cross-references GB:AE000414; GB:U00096; NID:g1789783; !1PIDN:AAC76409.1; PID:g1789786; UWGP:b3384 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A92373 !$#authors Hall, C.V.; van Cleemput, M.; Muench, K.H.; Yanofsky, C. !$#journal J. Biol. Chem. (1982) 257:6132-6136 !$#title The nucleotide sequence of the structural gene for !1Escherichia coli tryptophanyl-tRNA synthetase. !$#cross-references MUID:82189977; PMID:7042706 !$#accession A01182 !'##molecule_type DNA !'##residues 1-29,'K',31-325,'Q',327-333,'R' ##label HAL !'##cross-references GB:V00371; NID:g463199; PIDN:CAA23670.1; !1PID:g43200; GB:J01716; GB:V00370 REFERENCE A91445 !$#authors Winter, G.P.; Hartley, B.S.; McLachlan, A.D.; Lee, M.; !1Muench, K.H. !$#journal FEBS Lett. (1977) 82:348-350 !$#title Sequence homology between the tryptophanyl tRNA synthetase !1of Bacillus stearothermophilus and Escherichia coli. !$#cross-references MUID:78024293; PMID:334569 !$#contents annotation !$#note this work confirms parts of the above sequence by amino acid !1analysis REFERENCE S31739 !$#authors Lyngstadaas, A.; Boye, E. !$#submission submitted to the EMBL Data Library, January 1993 !$#description dam operon. !$#accession S31745 !'##molecule_type DNA !'##residues 1-29,'K',31-325,'Q',327-333,'R' ##label LYN !'##cross-references EMBL:Z19601; NID:g41221; PIDN:CAA79669.1; !1PID:g41228 REFERENCE S55287 !$#authors Lyngstadaas, A.; Lobner-Olesen, A.; Boye, E. !$#journal Mol. Gen. Genet. (1995) 247:546-554 !$#title Characterization of three genes in the dam-containing operon !1of Escherichia coli. !$#cross-references MUID:95327050; PMID:7603433 !$#accession S55290 !'##status preliminary !'##molecule_type DNA !'##residues 1-29,'K',31-55 ##label LY2 !'##cross-references EMBL:Z19601 REFERENCE I54844 !$#authors Hall, C.V.; Yanofsky, C. !$#journal J. Bacteriol. (1981) 148:941-949 !$#title Cloning and characterization of the gene for Escherichia !1coli tryptophanyl-transfer ribonucleic acid synthetase. !$#cross-references MUID:82075662; PMID:6171561 !$#accession I69352 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-11 ##label RES !'##cross-references EMBL:Z28371; NID:g433091; PIDN:CAA82220.1; !1PID:g433092 !$#accession I54844 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 152-171 ##label RE2 !'##cross-references EMBL:V00370; NID:g43198; PIDN:CAA23669.1; !1PID:g929580 GENETICS !$#gene trpS !$#map_position 74 min CLASSIFICATION #superfamily tryptophan-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; ligase; protein biosynthesis SUMMARY #length 334 #molecular-weight 37438 #checksum 789 SEQUENCE /// ENTRY YWBS #type complete TITLE tryptophan-tRNA ligase (EC 6.1.1.2) - Bacillus subtilis ALTERNATE_NAMES tryptophanyl-tRNA synthetase ORGANISM #formal_name Bacillus subtilis DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 03-Jun-2002 ACCESSIONS JT0481; A32452; E69726 REFERENCE JT0481 !$#authors Chow, K.C.; Wong, T.F. !$#journal Gene (1988) 73:537-574 !$#title Cloning and nucleotide sequence of the structural gene !1coding for Bacillus subtilis tryptophanyl-tRNA synthetase. !$#cross-references MUID:89211991; PMID:3149612 !$#accession JT0481 !'##molecule_type DNA !'##residues 1-330 ##label CHO !'##cross-references GB:M24068; NID:g143785; PIDN:AAA22874.1; !1PID:g143786 REFERENCE A32452 !$#authors Xu, Z.J.; Love, M.L.; Ma, L.Y.Y.; Blum, M.; Bronskill, P.M.; !1Bernstein, J.; Grey, A.A.; Hofmann, T.; Camerman, N.; Wong, !1J.T.F. !$#journal J. Biol. Chem. (1989) 264:4304-4311 !$#title Tryptophanyl-tRNA synthetase from Bacillus subtilis. !1Characterization and role of hydrophobicity in substrate !1recognition. !$#cross-references MUID:89174673; PMID:2494170 !$#accession A32452 !'##molecule_type protein !'##residues 1-32 ##label XUZ REFERENCE A40192 !$#authors Chow, K.C.; Xue, H.; Shi, W.; Wong, J.T.F. !$#journal J. Biol. Chem. (1992) 267:9146-9149 !$#title Mutational identification of an essential tryptophan in !1tryptophanyl-tRNA synthetase of Bacillus subtilis. !$#cross-references MUID:92250512; PMID:1577751 !$#contents annotation !$#note site-directed mutagenesis of the unique Trp residue to Phe, !1Ala, or Gln eliminates activity; the role of this Trp !1residue has not been determined REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69726 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-330 ##label KUN !'##cross-references GB:Z99110; GB:AL009126; NID:g2633472; !1PIDN:CAB12999.1; PID:g2633496 !'##experimental_source strain 168 GENETICS !$#gene trpS CLASSIFICATION #superfamily tryptophan-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; ligase; protein biosynthesis SUMMARY #length 330 #molecular-weight 37197 #checksum 4991 SEQUENCE /// ENTRY A41706 #type complete TITLE tryptophan-tRNA ligase (EC 6.1.1.2) [similarity] - human ALTERNATE_NAMES interferon-inducible protein IFP53; peptide-chain release factor homolog; tryptophanyl-tRNA synthetase ORGANISM #formal_name Homo sapiens #common_name man DATE 19-May-2000 #sequence_revision 19-May-2000 #text_change 03-Jun-2002 ACCESSIONS A41633; A41706; S19246; JN0676; JH0533; S26287 REFERENCE A41633 !$#authors Fleckner, J.; Rasmussen, H.H.; Justesen, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:11520-11524 !$#title Human interferon gamma potently induces the synthesis of a !155-kDa protein (gamma2) highly homologous to rabbit peptide !1chain release factor and bovine tryptophanyl-tRNA !1synthetase. !$#cross-references MUID:92107982; PMID:1763065 !$#accession A41633 !'##status preliminary !'##molecule_type mRNA !'##residues 1-471 ##label FLE !'##cross-references GB:X59892; NID:g30820; PIDN:CAA42545.1; PID:g30821 REFERENCE A41706 !$#authors Rubin, B.Y.; Anderson, S.L.; Xing, L.; Powell, R.J.; Tate, !1W.P. !$#journal J. Biol. Chem. (1991) 266:24245-24248 !$#title Interferon induces tryptophanyl-tRNA synthetase expression !1in human fibroblasts. !$#cross-references MUID:92105071; PMID:1761529 !$#accession A41706 !'##status preliminary !'##molecule_type mRNA !'##residues 1-471 ##label RUB !'##cross-references GB:M77804; NID:g184656; PIDN:AAA67324.1; !1PID:g184657 REFERENCE S19246 !$#authors Buwitt, U.; Flohr, T.; Boettger, E.C. !$#journal EMBO J. (1992) 11:489-496 !$#title Molecular cloning and characterization of an interferon !1induced human cDNA with sequence homology to a mammalian !1peptide chain release factor. !$#cross-references MUID:92164636; PMID:1537332 !$#accession S19246 !'##status preliminary !'##molecule_type mRNA !'##residues 1-423,'R',425-471 ##label BUW !'##cross-references EMBL:X62570; NID:g32708; PIDN:CAA44450.1; !1PID:g32709 !'##note 213-Ser and 214-Tyr were also found REFERENCE JN0676 !$#authors Frolova, L.Y.; Grigorieva, A.Y.; Sudomoina, M.A.; Kisselev, !1L.L. !$#journal Gene (1993) 128:237-245 !$#title The human gene encoding tryptophanyl-tRNA synthetase: !1Interferon-response elements and exon-intron organization. !$#cross-references MUID:93292992; PMID:7685728 !$#accession JN0676 !'##molecule_type DNA !'##residues 1-141;182-471 ##label FRO1 !'##cross-references GB:X67918; GB:S62837; NID:g37968; GB:X67919; !1NID:g37969; GB:X67920; NID:g37970; GB:X67921; GB:S62842; !1NID:g37971; GB:X67922; GB:S62843; NID:g37972; GB:X67923; !1NID:g37973; GB:X67924; NID:g37974; GB:X67925; GB:S62855; !1NID:g37975; GB:X67926; GB:S62856; NID:g37976; GB:X67927; !1NID:g37966; GB:X67928; NID:g37967 !'##note the authors translated the codon GGG for residue 55 as Cys and !1GAG for residue 346 as Ser !'##note this translation is not annotated in GenBank entries HSWRSX1A, !1HSWRSX1B, HSWRSX2, HSWRSX3, HSWRSX4, HSWRSX6, HSWRSX7, !1HSWRSX8, HSWRSX9, HSWRSX10, and HSWRSX11, release 113.0 REFERENCE JH0533 !$#authors Frolova, L.Y.; Sudomoina, M.A.; Grigorieva, A.Y.; Zinovieva, !1O.L.; Kisselev, L.L. !$#journal Gene (1991) 109:291-296 !$#title Cloning and nucleotide sequence of the structural gene !1encoding for human tryptophanyl-tRNA synthetase. !$#cross-references MUID:92112058; PMID:1765274 !$#accession JH0533 !'##molecule_type mRNA !'##residues 1-212,'GD',215-471 ##label FRO2 !'##cross-references GB:M61715; NID:g340367; PIDN:AAA61298.1; !1PID:g340368 !'##experimental_source fibroblast GENETICS !$#gene GDB:WARS; IFP53 !'##cross-references GDB:119632; OMIM:191050 !$#map_position 14q23-14q31 !$#introns 33/3; 105/1; 141/2; 181/2; 242/2; 276/1; 313/3; 371/3; 418/3 CLASSIFICATION #superfamily mammalian tryptophan-tRNA ligase; amino !1acid-tRNA ligase repeat homology KEYWORDS aminoacyl-tRNA synthetase; ATP; ligase; protein biosynthesis FEATURE !$19-64 #domain amino acid-tRNA ligase repeat homology #label !8ATL SUMMARY #length 471 #molecular-weight 53165 #checksum 7082 SEQUENCE /// ENTRY YWBO #type complete TITLE tryptophan-tRNA ligase (EC 6.1.1.2) [validated] - bovine ALTERNATE_NAMES tryptophanyl-tRNA synthetase ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 03-Jun-2002 ACCESSIONS A40279; JN0354; S10460; S14540 REFERENCE A40279 !$#authors Garret, M.; Pajot, B.; Trezeguet, V.; Labouesse, J.; Merle, !1M.; Gandar, J.C.; Benedetto, J.P.; Sallafranque, M.L.; !1Alterio, J.; Gueguen, M.; Sarger, C.; Labouesse, B.; Bonnet, !1J. !$#journal Biochemistry (1991) 30:7809-7817 !$#title A mammalian tryptophanyl-tRNA synthetase shows little !1homology to prokaryotic synthetases but near identity with !1mammalian peptide chain release factor. !$#cross-references MUID:91329348; PMID:1907847 !$#accession A40279 !'##molecule_type mRNA !'##residues 1-475 ##label GAR !'##cross-references GB:M74074; EMBL:X53918; NID:g163798; !1PIDN:AAA30799.1; PID:g163799 !'##experimental_source pancreas !'##note the authors translated the codon CTG for residue 347 as Ala and !1CAG for residue 348 as Leu !'##note part of this sequence was confirmed by protein sequencing REFERENCE JN0354 !$#authors Zargarova, T.A.; Kovaleva, G.K.; Favorova, O.O.; Aevina, !1H.B.; Telezhinskaya, I.H. !$#journal Bioorg. Khim. (1989) 15:1307-1311 !$#title Amino acid sequence of several peptides of tryptophanyl-tRNA !1synthetase from cattle pancreas. !$#cross-references MUID:90211408; PMID:2631684 !$#accession JN0354 !'##molecule_type protein !'##residues 112-124;282-287,'N',288,'F',289-292,'Q',293-294, !1'IR';336-353;423-441,443-449,'ES',452,454-456,'DM',459-465, !1'PR',468-475 ##label ZAR !'##experimental_source liver !'##note this paper is in Russian CLASSIFICATION #superfamily mammalian tryptophan-tRNA ligase; amino !1acid-tRNA ligase repeat homology KEYWORDS aminoacyl-tRNA synthetase; ATP; ligase; protein biosynthesis FEATURE !$24-69 #domain amino acid-tRNA ligase repeat homology #label !8ATL SUMMARY #length 475 #molecular-weight 53728 #checksum 8127 SEQUENCE /// ENTRY YWRBPR #type complete TITLE tryptophan-tRNA ligase (EC 6.1.1.2) [validated] - rabbit ALTERNATE_NAMES tryptophanyl-tRNA synthetase ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 30-Sep-1992 #sequence_revision 13-Feb-1998 #text_change 03-Jun-2002 ACCESSIONS A35904; S37396 REFERENCE A35904 !$#authors Lee, C.C.; Craigen, W.J.; Muzny, D.M.; Harlow, E.; Caskey, !1C.T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:3508-3512 !$#title Cloning and expression of a mammalian peptide chain release !1factor with sequence similarity to tryptophanyl-tRNA !1synthetases. !$#cross-references MUID:90239043; PMID:2185472 !$#accession A35904 !'##molecule_type mRNA !'##residues 1-475 ##label LEE !'##cross-references GB:M33460 REFERENCE S37396 !$#authors Frolova, L.Y.; Dalphin, M.E.; Justesen, J.; Powell, R.J.; !1Drugeon, G.; McCaughan, K.K.; Kisselev, L.L.; Tate, W.P.; !1Haenni, A.L. !$#journal EMBO J. (1993) 12:4013-4019 !$#title Mammalian polypeptide chain release factor and !1tryptophanyl-tRNA synthetase are distinct proteins. !$#cross-references MUID:94009008; PMID:8404867 !$#accession S37396 !'##molecule_type mRNA !'##residues 166-177 ##label FRO GENETICS !$#gene WRS COMPLEX homodimer [validated, MUID:94009008] FUNCTION !$#description EC 6.1.1.2 [validated, MUID:94009008]; catalyzes the !1ATP-dependent formation of tryptophanyl-tRNA !$#note mammalian WRS (tryptophanyl-tRNA synthetases) and eRF !1(polypeptide chain release factor) are different proteins CLASSIFICATION #superfamily mammalian tryptophan-tRNA ligase; amino !1acid-tRNA ligase repeat homology KEYWORDS aminoacyl-tRNA synthetase; ATP; homodimer; ligase; !1metalloprotein; protein biosynthesis; zinc FEATURE !$23-68 #domain amino acid-tRNA ligase repeat homology #label !8ATL\ !$174-177 #region ATP-binding motif (HXGH) SUMMARY #length 475 #molecular-weight 53901 #checksum 483 SEQUENCE /// ENTRY YSHUT #type complete TITLE threonine-tRNA ligase (EC 6.1.1.3) - human ALTERNATE_NAMES threonyl-tRNA synthetase ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1992 #sequence_revision 30-Jun-1993 #text_change 03-Jun-2002 ACCESSIONS A38867; A40017 REFERENCE A38867 !$#authors Cruzen, M.E.; Arfin, S.M. !$#submission submitted to the EMBL Data Library, June 1991 !$#accession A38867 !'##molecule_type mRNA !'##residues 1-712 ##label CRU !'##cross-references EMBL:M63180; NID:g339679; PIDN:AAB04939.1; !1PID:g1464742 REFERENCE A40017 !$#authors Cruzen, M.E.; Arfin, S.M. !$#journal J. Biol. Chem. (1991) 266:9919-9923 !$#title Nucleotide and deduced amino acid sequence of human !1threonyl-tRNA synthetase reveals extensive homology to the !1Escherichia coli and yeast enzymes. !$#cross-references MUID:91236775; PMID:2033077 !$#accession A40017 !'##molecule_type mRNA !'##residues 1-66,'EC',69-274,'A',276-385,'F',387-454,'F',456-506,'R', !1508-527,'C',529-535,'S',537-602,'L',604-712 ##label CR2 !'##cross-references GB:M63180 !'##note the authors translated the codon GGC for residue 152 as Ala GENETICS !$#gene GDB:TARS !'##cross-references GDB:120397; OMIM:187790 !$#map_position 5p13-5cen CLASSIFICATION #superfamily threonine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; ligase; protein biosynthesis SUMMARY #length 712 #molecular-weight 82123 #checksum 6602 SEQUENCE /// ENTRY YSBYTC #type complete TITLE threonine-tRNA ligase (EC 6.1.1.3), cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YIL078w; threonyl-tRNA synthetase ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1992 #sequence_revision 02-Dec-1994 #text_change 03-Jun-2002 ACCESSIONS S48366; A23782 REFERENCE S48364 !$#authors Brown, D.; Bowman, S. !$#submission submitted to the EMBL Data Library, September 1994 !$#accession S48366 !'##molecule_type DNA !'##residues 1-734 ##label BRO !'##cross-references GB:Z47047; EMBL:Z37997; NID:g603997; PID:g763268; !1GSPDB:GN00009; MIPS:YIL078w REFERENCE A23782 !$#authors Pape, L.K.; Tzagoloff, A. !$#journal Nucleic Acids Res. (1985) 13:6171-6183 !$#title Cloning and characterization of the gene for the yeast !1cytoplasmic threonyl-tRNA synthetase. !$#cross-references MUID:86016080; PMID:2995918 !$#accession A23782 !'##molecule_type DNA !'##residues 1-8,'A',10-17,'N',19-501,'E',503-734 ##label PAP !'##cross-references EMBL:X02906; NID:g4618; PIDN:CAA26666.1; PID:g4619 GENETICS !$#gene SGD:THS1; MIPS:YIL078w !'##cross-references SGD:S0001340; MIPS:YIL078w !$#map_position 9L CLASSIFICATION #superfamily threonine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; ligase; protein biosynthesis SUMMARY #length 734 #molecular-weight 84520 #checksum 1773 SEQUENCE /// ENTRY YSBYTM #type complete TITLE threonine-tRNA ligase (EC 6.1.1.3) precursor, mitochondrial - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YKL194c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1992 #sequence_revision 02-May-1994 #text_change 03-Jun-2002 ACCESSIONS S38031; A24240; S51091 REFERENCE S38024 !$#authors Maia e Silva, A.; Bossier, P.; Vilela, C.; Fernandes, L.; !1Soares, H.; Guerreiro, P.; Rodrigues-Pousada, C. !$#submission submitted to the Protein Sequence Database, March 1994 !$#accession S38031 !'##molecule_type DNA !'##residues 1-462 ##label MAI !'##cross-references EMBL:Z28194; NID:g486344; PIDN:CAA82038.1; !1PID:g486345; GSPDB:GN00011; MIPS:YKL194c !'##experimental_source strain S288C REFERENCE A24240 !$#authors Pape, L.K.; Koerner, T.J.; Tzagoloff, A. !$#journal J. Biol. Chem. (1985) 260:15362-15370 !$#title Characterization of a yeast nuclear gene (MST1) coding for !1the mitochondrial threonyl-tRNA(1) synthetase. !$#cross-references MUID:86059395; PMID:2999113 !$#accession A24240 !'##molecule_type DNA !'##residues 1-264,'S',266-462 ##label PAP !'##cross-references EMBL:M12087; NID:g172011; PIDN:AAA34808.1; !1PID:g172012 REFERENCE S51090 !$#authors Mackelvie, S.H.; Andrews, P.D.; Stark, M.J.R. !$#submission submitted to the EMBL Data Library, December 1994 !$#description The Saccharomyces cerevisiae gene SDS22 encodes a potential !1regulator of the mitotic function of yeast type 1 protein !1phosphatase. !$#accession S51091 !'##molecule_type DNA !'##residues 1-14 ##label MAC !'##cross-references EMBL:X83609; NID:g619515; PIDN:CAA58589.1; !1PID:g619517 GENETICS !$#gene SGD:MST1; MIPS:YKL194c !'##cross-references SGD:S0001677; MIPS:YKL194c !$#map_position 11L !$#genome nuclear CLASSIFICATION #superfamily threonine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; ligase; mitochondrion; !1protein biosynthesis FEATURE !$1-45 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$46-462 #product threonine-tRNA ligase #status predicted !8#label MAT SUMMARY #length 462 #molecular-weight 54092 #checksum 7051 SEQUENCE /// ENTRY SYECTT #type complete TITLE threonine-tRNA ligase (EC 6.1.1.3) - Escherichia coli (strain K-12) ALTERNATE_NAMES threonyl-tRNA synthetase ORGANISM #formal_name Escherichia coli DATE 28-May-1986 #sequence_revision 31-Oct-1997 #text_change 03-Jun-2002 ACCESSIONS G64930; A01183; I59072 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64930 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-642 ##label BLAT !'##cross-references GB:AE000267; GB:U00096; NID:g1788011; !1PIDN:AAC74789.1; PID:g1788013; UWGP:b1719 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A01183 !$#authors Mayaux, J.F.; Fayat, G.; Fromant, M.; Springer, M.; !1Grunberg-Manago, M.; Blanquet, S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:6152-6156 !$#title Structural and transcriptional evidence for related thrS and !1infC expression. !$#cross-references MUID:84016012; PMID:6353409 !$#accession A01183 !'##molecule_type DNA !'##residues 1-194,'R',196-642 ##label MAY !'##cross-references GB:V00291; NID:g43065; PIDN:CAA23560.1; PID:g43066 REFERENCE I59072 !$#authors Springer, M.; Graffe, M.; Butler, J.S.; Grunberg-Manago, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:4384-4388 !$#title Genetic definition of the translational operator of the !1threonine-tRNA ligase gene in Escherichia coli. !$#cross-references MUID:86233434; PMID:3086882 !$#accession I59072 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-47 ##label RES !'##cross-references GB:M13549; NID:g147984; PIDN:AAA24674.1; !1PID:g147985 COMMENT This is also a translational repressor protein; it controls !1the translation of its own gene by binding to its mRNA. GENETICS !$#gene thrS !$#map_position 38 min FUNCTION !$#description activates L-threonine and transfers it to the specific tRNA !$#pathway protein biosynthesis !$#note belongs to class-II synthetases CLASSIFICATION #superfamily threonine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; homodimer; ligase; protein !1biosynthesis; translation regulation SUMMARY #length 642 #molecular-weight 74014 #checksum 7250 SEQUENCE /// ENTRY YSBST2 #type complete TITLE threonine-tRNA ligase (EC 6.1.1.3) thrZ [validated] - Bacillus subtilis ALTERNATE_NAMES threonine-tRNA ligase, minor; threonyl-tRNA synthetase ORGANISM #formal_name Bacillus subtilis DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 03-Jun-2002 ACCESSIONS A37770; C69723 REFERENCE A37770 !$#authors Putzer, H.; Brakhage, A.A.; Grunberg-Manago, M. !$#journal J. Bacteriol. (1990) 172:4593-4602 !$#title Independent genes for two threonyl-tRNA synthetases in !1Bacillus subtilis. !$#cross-references MUID:90330571; PMID:2115870 !$#accession A37770 !'##molecule_type DNA !'##residues 1-638 ##label PUT !'##cross-references GB:M36593; NID:g143763; PIDN:AAA22863.1; !1PID:g143764 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69723 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-638 ##label KUN !'##cross-references GB:Z99123; GB:AL009126; NID:g2636240; !1PIDN:CAB15783.1; PID:g2636292 !'##experimental_source strain 168 COMMENT This threonine-tRNA ligase is not expressed during !1vegetative growth. GENETICS !$#gene thrZ; thrS2 !$#map_position 344 (degrees) FUNCTION !$#description EC 6.1.1.3 [validated, MUID:90330571] CLASSIFICATION #superfamily threonine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; ligase; protein biosynthesis SUMMARY #length 638 #molecular-weight 73373 #checksum 3728 SEQUENCE /// ENTRY YSBST1 #type complete TITLE threonine-tRNA ligase (EC 6.1.1.3) thrS [validated] - Bacillus subtilis ALTERNATE_NAMES threonine-tRNA ligase, major; threonyl-tRNA synthetase ORGANISM #formal_name Bacillus subtilis DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 03-Jun-2002 ACCESSIONS B37770; E24720; B69723 REFERENCE A37770 !$#authors Putzer, H.; Brakhage, A.A.; Grunberg-Manago, M. !$#journal J. Bacteriol. (1990) 172:4593-4602 !$#title Independent genes for two threonyl-tRNA synthetases in !1Bacillus subtilis. !$#cross-references MUID:90330571; PMID:2115870 !$#accession B37770 !'##molecule_type DNA !'##residues 1-643 ##label PUT !'##cross-references GB:M36594; NID:g143765; PIDN:AAA22864.1; !1PID:g143766 REFERENCE A93650 !$#authors Ogasawara, N.; Moriya, S.; Mazza, P.G.; Yoshikawa, H. !$#journal Nucleic Acids Res. (1986) 14:9989-9999 !$#title Nucleotide sequence and organization of dnaB gene and !1neighbouring genes on the Bacillus subtilis chromosome. !$#cross-references MUID:87117549; PMID:3027671 !$#accession E24720 !'##molecule_type DNA !'##residues 1-180 ##label OGA !'##cross-references GB:X04963; NID:g39880; PIDN:CAA28636.1; PID:g39884 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69723 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-643 ##label KUN !'##cross-references GB:Z99118; GB:AL009126; NID:g2635200; !1PIDN:CAB14855.1; PID:g2635360 !'##experimental_source strain 168 COMMENT This threonine-tRNA ligase, unlike the product of the thrS2 !1gene, is expressed during vegetative growth. GENETICS !$#gene thrS; thrSv !$#map_position 250 (degrees) FUNCTION !$#description EC 6.1.1.3 [validated, MUID:90330571] CLASSIFICATION #superfamily threonine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; ligase; protein biosynthesis SUMMARY #length 643 #molecular-weight 73514 #checksum 7022 SEQUENCE /// ENTRY SYNCLC #type complete TITLE leucine-tRNA ligase (EC 6.1.1.4), cytosolic - Neurospora crassa ALTERNATE_NAMES leucyl-tRNA synthetase ORGANISM #formal_name Neurospora crassa DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 03-Jun-2002 ACCESSIONS A33475; S04532 REFERENCE A33475 !$#authors Chow, C.M.; Rajbhandary, U.L. !$#journal Mol. Cell. Biol. (1989) 9:4645-4652 !$#title Regulation of the nuclear genes encoding the cytoplasmic and !1mitochondrial leucyl-tRNA synthetases of Neurospora crassa. !$#cross-references MUID:90097875; PMID:2532300 !$#accession A33475 !'##molecule_type DNA !'##residues 1-1123 ##label CHO !'##cross-references GB:X13021 REFERENCE S04532 !$#authors Benarous, R.; Chow, C.M.; RajBhandary, U.L. !$#journal Genetics (1988) 119:805-814 !$#title Cytoplasmic leucyl-tRNA synthetase of Neurospora crassa is !1not specified by the leu-5 locus. !$#cross-references MUID:88313637; PMID:2842224 !$#accession S04532 !'##molecule_type DNA !'##residues 1-116 ##label BEN !'##cross-references EMBL:X13021; NID:g3020; PIDN:CAA31439.1; PID:g3021 GENETICS !$#gene leu-5 CLASSIFICATION #superfamily Neurospora cytosolic leucine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; ligase; protein biosynthesis SUMMARY #length 1123 #molecular-weight 126398 #checksum 6708 SEQUENCE /// ENTRY B28255 #type complete TITLE hypothetical 34K protein (pgtA 3' region) - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B28255 REFERENCE A91556 !$#authors Yu, G.; Hong, J. !$#journal Gene (1986) 45:51-57 !$#title Identification and nucleotide sequence of the activator gene !1of the externally induced phosphoglycerate transport system !1of Salmonella typhimurium. !$#cross-references MUID:87055265; PMID:3023201 !$#accession B28255 !'##molecule_type mRNA !'##residues 1-296 ##label YUG !'##cross-references GB:M13923; NID:g154254; PIDN:AAA27185.1; !1PID:g154256 !'##note the authors translated the codon GGG for residue 92 as Gln, TCT !1for residue 184 as Phe, and GAG for residue 226 as Gln CLASSIFICATION #superfamily Escherichia coli proteinase VII SUMMARY #length 296 #molecular-weight 33631 #checksum 596 SEQUENCE /// ENTRY A30916 #type complete TITLE coagulase/fibrinolysin precursor - Yersinia pestis plasmid pKYP1 ORGANISM #formal_name Yersinia pestis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S06979; A30916 REFERENCE S06979 !$#authors McDonough, K.A.; Falkow, S. !$#journal Mol. Microbiol. (1989) 3:767-775 !$#title A Yersinia pestis-specific DNA fragment encodes !1temperature-dependent coagulase and fibrinolysin-associated !1phenotypes. !$#cross-references MUID:89313306; PMID:2526282 !$#accession S06979 !'##molecule_type DNA !'##residues 1-312 ##label MCD !'##cross-references EMBL:X15136; NID:g48629; PIDN:CAA33235.1; !1PID:g48630 GENETICS !$#gene pla !$#genome plasmid CLASSIFICATION #superfamily Escherichia coli proteinase VII KEYWORDS periplasmic space FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-312 #product coagulase/fibrinolysin #status predicted !8#label MAT SUMMARY #length 312 #molecular-weight 34611 #checksum 1826 SEQUENCE /// ENTRY SYBYLM #type complete TITLE leucine-tRNA ligase (EC 6.1.1.4) precursor, mitochondrial - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES leucyl-tRNA synthetase; protein L3502.6; protein YLR382c ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 03-Jun-2002 ACCESSIONS A28521; S05842; S20165; S51469; A26635; S15581 REFERENCE A92722 !$#authors Tzagoloff, A.; Akai, A.; Kurkulos, M.; Repetto, B. !$#journal J. Biol. Chem. (1988) 263:850-856 !$#title Homology of yeast mitochondrial leucyl-tRNA synthetase and !1isoleucyl- and methionyl-tRNA synthetases of Escherichia !1coli. !$#cross-references MUID:88087210; PMID:2826465 !$#accession A28521 !'##molecule_type DNA !'##residues 1-894 ##label TZA !'##cross-references EMBL:J03495; NID:g172007; PIDN:AAA34805.1; !1PID:g172008 REFERENCE A91079 !$#authors Labouesse, M.; Herbert, C.J.; Dujardin, G.; Slonimski, P.P. !$#journal EMBO J. (1987) 6:713-721 !$#title Three suppressor mutations which cure a mitochondrial RNA !1maturase deficiency occur at the same codon in the open !1reading frame of the nuclear NAM2 gene. !$#cross-references MUID:87218532; PMID:3034607 !$#accession S05842 !'##molecule_type DNA !'##residues 1-894 ##label LAB !'##cross-references EMBL:X05843 !'##note the sequences of mutants having 240-Ser or 240-Cys were also !1determined REFERENCE S18752 !$#authors Herbert, C.J.; Dujardin, G.; Labouesse, M.; Slonimski, P.P. !$#journal Mol. Gen. Genet. (1988) 213:297-309 !$#title Divergence of the mitochondrial leucyl tRNA synthetase genes !1in two closely related yeasts Saccharomyces cerevisiae and !1Saccharomyces douglasii: a paradigm of incipient evolution. !$#cross-references MUID:89039717; PMID:3054483 !$#accession S20165 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-894 ##label HER REFERENCE S51466 !$#authors Du, Z. !$#submission submitted to the EMBL Data Library, December 1994 !$#description The sequence of S. cerevisiae cosmid L3502. !$#accession S51469 !'##molecule_type DNA !'##residues 1-894 ##label DUZ !'##cross-references EMBL:U19104; NID:g609423; PIDN:AAB67277.1; !1PID:g609429; GSPDB:GN00012; MIPS:YLR382c COMMENT This protein is capable of compensating for mutations in !1mRNA maturase encoded by the fourth intron of the !1mitochondrial cytochrome b gene. GENETICS !$#gene SGD:NAM2; MSL1; MIPS:YLR382c !'##cross-references SGD:S0004374; MIPS:YLR382c !$#map_position 12R !$#genome nuclear CLASSIFICATION #superfamily leucine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; ligase; mitochondrion; !1protein biosynthesis; zinc finger FEATURE !$1-25 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$26-894 #product leucine-tRNA ligase #status predicted #label !8MAT\ !$63-66 #region ATP binding #status predicted\ !$350-369 #region zinc finger CHCH motif\ !$462-506 #region zinc finger CCCC motif\ !$628-632 #region tRNA binding #status predicted SUMMARY #length 894 #molecular-weight 101920 #checksum 3980 SEQUENCE /// ENTRY SYBYMX #type complete TITLE leucine-tRNA ligase (EC 6.1.1.4) precursor, mitochondrial - yeast (Saccharomyces sp.) ALTERNATE_NAMES leucyl-tRNA synthetase ORGANISM #formal_name Saccharomyces sp. DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 03-Jun-2002 ACCESSIONS S18754; S00341 REFERENCE S18752 !$#authors Herbert, C.J.; Dujardin, G.; Labouesse, M.; Slonimski, P.P. !$#journal Mol. Gen. Genet. (1988) 213:297-309 !$#title Divergence of the mitochondrial leucyl tRNA synthetase genes !1in two closely related yeasts Saccharomyces cerevisiae and !1Saccharomyces douglasii: a paradigm of incipient evolution. !$#cross-references MUID:89039717; PMID:3054483 !$#accession S18754 !'##molecule_type DNA !'##residues 1-894 ##label HER1 !'##cross-references GB:X12864; NID:g4839; PIDN:CAA31343.1; PID:g4842 !'##note the source is designated as Saccharomyces douglasii REFERENCE S00341 !$#authors Herbert, C.J.; Labouesse, M.; Dujardin, G.; Slonimski, P.P. !$#journal EMBO J. (1988) 7:473-483 !$#title The NAM2 proteins from S.cerevisiae and S.douglasii are !1mitochondrial leucyl-tRNA synthetases, and are involved in !1mRNA splicing. !$#cross-references MUID:88211560; PMID:3284745 !$#accession S00341 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 26-894 ##label HER2 !'##note the source is designated as Saccharomyces douglasii GENETICS !$#gene NAM2 CLASSIFICATION #superfamily leucine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; ligase; mitochondrion; !1protein biosynthesis; zinc finger FEATURE !$1-48 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$49-894 #product leucine-tRNA ligase #status predicted #label !8MAT\ !$63-66 #region ATP binding #status predicted\ !$350-369 #region zinc finger CHCH motif\ !$462-506 #region zinc finger CCCC motif\ !$628-632 #region tRNA binding #status predicted SUMMARY #length 894 #molecular-weight 102193 #checksum 816 SEQUENCE /// ENTRY SYNCLM #type complete TITLE leucine-tRNA ligase (EC 6.1.1.4) precursor, mitochondrial - Neurospora crassa ALTERNATE_NAMES leucyl-tRNA synthetase ORGANISM #formal_name Neurospora crassa DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 03-Jun-2002 ACCESSIONS A33474 REFERENCE A33474 !$#authors Chow, C.M.; Metzenberg, R.L.; Rajbhandary, U.L. !$#journal Mol. Cell. Biol. (1989) 9:4631-4644 !$#title Nuclear gene for mitochondrial leucyl-tRNA synthetase of !1Neurospora crassa: isolation, sequence, chromosomal mapping, !1and evidence that the leu-5 locus specifies structural !1information. !$#cross-references MUID:90097874; PMID:2574823 !$#accession A33474 !'##molecule_type DNA !'##residues 1-994 ##label CHO !'##cross-references GB:M30472; NID:g168829; PIDN:AAA33599.1; !1PID:g168830 GENETICS !$#gene leu-5 CLASSIFICATION #superfamily leucine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; ligase; mitochondrion; !1protein biosynthesis; zinc finger FEATURE !$1-52 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$53-994 #product leucine-tRNA ligase #status predicted #label !8MAT\ !$100-103 #region ATP binding #status predicted\ !$503-550 #region zinc finger CCCC motif SUMMARY #length 994 #molecular-weight 109853 #checksum 1063 SEQUENCE /// ENTRY SYECL #type complete TITLE leucine-tRNA ligase (EC 6.1.1.4) [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES leucyl-tRNA synthetase ORGANISM #formal_name Escherichia coli DATE 31-Mar-1989 #sequence_revision 21-Nov-1997 #text_change 03-Jun-2002 ACCESSIONS H64798; A30290 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64798 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-860 ##label BLAT !'##cross-references GB:AE000168; GB:U00096; NID:g1786849; !1PIDN:AAC73743.1; PID:g1786861; UWGP:b0642 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A30290 !$#authors Haertlein, M.; Madern, D. !$#journal Nucleic Acids Res. (1987) 15:10199-10210 !$#title Molecular cloning and nucleotide sequence of the gene for !1Escherichia coli leucyl-tRNA synthetase. !$#cross-references MUID:88096562; PMID:3320963 !$#accession A30290 !'##molecule_type DNA !'##residues 1-66,'H',68-195,'N',197-261,'R',263-860 ##label HAE !'##cross-references EMBL:X06331; NID:g41915; PIDN:CAA29642.1; !1PID:g41916 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing GENETICS !$#gene leuS !$#map_position 15 min FUNCTION !$#description EC 6.1.1.4 [validated, MUID:88096562] !$#pathway protein biosynthesis CLASSIFICATION #superfamily leucine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; ligase; protein biosynthesis FEATURE !$49-52 #region ATP binding #status predicted SUMMARY #length 860 #molecular-weight 97233 #checksum 7927 SEQUENCE /// ENTRY SYECIT #type complete TITLE isoleucine-tRNA ligase (EC 6.1.1.5) - Escherichia coli (strain K-12) ALTERNATE_NAMES isoleucyl-tRNA synthetase ORGANISM #formal_name Escherichia coli DATE 25-Feb-1985 #sequence_revision 31-Oct-1997 #text_change 03-Jun-2002 ACCESSIONS B64723; S40549; A94277; A91325; A93991; A01184 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64723 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-938 ##label BLAT !'##cross-references GB:AE000113; GB:U00096; NID:g2367095; !1PIDN:AAC73137.1; PID:g2367096; UWGP:b0026 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40549 !'##molecule_type DNA !'##residues 1-157,'GLQNWK',163-196,'KRKLSITT',205,'LLRPSTLLSR',216-289, !1'SR','HG',297,'RCGAGAAA',306-383,'A',385-650,'T',652-677, !1'RR',680-689,'VVR',693,'RHRKTSSRRTKHTISTKWYK',714-736,'Y', !1738-739,'GH',742-938 ##label YUR !'##cross-references EMBL:D10483; NID:g216434; PIDN:BAA01304.1; !1PID:g216453 REFERENCE A94277 !$#authors Webster, T.; Tsai, H.; Kula, M.; Mackie, G.A.; Schimmel, P. !$#journal Science (1984) 226:1315-1317 !$#title Specific sequence homology and three-dimensional structure !1of an aminoacyl transfer RNA synthetase. !$#cross-references MUID:85065774; PMID:6390679 !$#accession A94277 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-242,'RRGLCLPTAQSLLHQISTMRWW',265-299,'DV',302-586,'C', !1588-636,'Q',638-723,'V',725-737,'P',739,'RTVW',744-786,'L', !1788-829,'N',831-866,'DRRY',870-938 ##label WEB !'##note most of this sequence was confirmed by amino acid analysis REFERENCE A91325 !$#authors Yu, F.; Yamada, H.; Daishima, K.; Mizushima, S. !$#journal FEBS Lett. (1984) 173:264-268 !$#title Nucleotide sequence of the lspA gene, the structural gene !1for lipoprotein signal peptidase of Escherichia coli. !$#cross-references MUID:84261953; PMID:6378662 !$#accession A91325 !'##molecule_type DNA !'##residues 794-938 ##label YUF !'##cross-references GB:X00776; NID:g41921; PIDN:CAA25352.1; PID:g757839 REFERENCE A93991 !$#authors Innis, M.A.; Tokunaga, M.; Williams, M.E.; Loranger, J.M.; !1Chang, S.Y.; Chang, S.; Wu, H.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:3708-3712 !$#title Nucleotide sequence of the Escherichia coli prolipoprotein !1signal peptidase (lsp) gene. !$#cross-references MUID:84222028; PMID:6374664 !$#accession A93991 !'##molecule_type DNA !'##residues 795-938 ##label INN !'##cross-references GB:K01990; NID:g146668; PIDN:AAA24091.1; !1PID:g146669 GENETICS !$#gene ileS !$#map_position 1 min FUNCTION !$#description aminoacyl-tRNA biosynthesis !$#pathway protein biosynthesis CLASSIFICATION #superfamily isoleucine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; ligase; metal binding; !1monomer; protein biosynthesis; zinc FEATURE !$65-68 #region aminoacyl-tRNA synthetase HIGH motif\ !$602-606 #region KMSKS motif\ !$605 #binding_site ATP (Lys) #status predicted SUMMARY #length 938 #molecular-weight 104296 #checksum 6626 SEQUENCE /// ENTRY SYBYI4 #type complete TITLE isoleucine-tRNA ligase (EC 6.1.1.5) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES isoleucyl-tRNA synthetase; protein YBL0734; protein YBL076c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 03-Jun-2002 ACCESSIONS S14459; S45434; S45812; S45817; S05761; A38786; S59231 REFERENCE S14459 !$#authors Martindale, D.W.; Gu, Z.M.; Csank, C. !$#journal Curr. Genet. (1989) 15:99-106 !$#title Isolation and complete sequence of the yeast isoleucyl-tRNA !1synthetase gene (ILS1). !$#cross-references MUID:89304140; PMID:2663194 !$#accession S14459 !'##molecule_type DNA !'##residues 1-1072 ##label MAR !'##cross-references GB:X07886; NID:g3818; PIDN:CAA30733.1; PID:g3820 !'##experimental_source strain A364A REFERENCE S45387 !$#authors Obermaier, B.; Gassenhuber, J.; Piravandi, E.; Domdey, H. !$#submission submitted to the EMBL Data Library, May 1994 !$#description Sequence analysis of a 78,6 kb segment of the left end of !1Saccaromyces cerevisiae chromosome II. !$#accession S45434 !'##molecule_type DNA !'##residues 1-1072 ##label OBE !'##cross-references EMBL:X79489; NID:g496661; PIDN:CAA56034.1; !1PID:g498991 !'##experimental_source strain S288C REFERENCE S45802 !$#authors Contreras, R.; Fiers, W.; Logghe, M.; Molemans, F. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S45812 !'##molecule_type DNA !'##residues 1-1072 ##label CON !'##cross-references EMBL:Z35838; NID:g536121; PIDN:CAA84898.1; !1PID:g536123; GSPDB:GN00002; MIPS:YBL076c REFERENCE S45816 !$#authors Domdey, H.; Gassenhuber, H.; Obermaier, B.; Piravandi, E. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S45817 !'##molecule_type DNA !'##residues 1-1072 ##label DOM !'##cross-references EMBL:Z35838; NID:g536121; PIDN:CAA84898.1; !1PID:g536123; GSPDB:GN00002; MIPS:YBL076c REFERENCE S05761 !$#authors Englisch, U.; Englisch, S.; Markmeyer, P.; Schischkoff, J.; !1Sternbach, H.; Kratzin, H.; Cramer, F. !$#journal Biol. Chem. Hoppe-Seyler (1987) 368:971-979 !$#title Structure of the yeast isoleucyl-tRNA synthetase gene !1(ILS1). DNA-sequence, amino-acid sequence of proteolytic !1peptides of the enzyme and comparison of the structure to !1those of other known aminoacyl-tRNA synthetases. !$#cross-references MUID:88024443; PMID:3311074 !$#accession S05761 !'##molecule_type DNA !'##residues 1-550,'E',552-587,'KS',589-692,'AEM',696-705,'V',707-746, !1'V',748-1072 ##label ENG !'##cross-references EMBL:M19992; NID:g171767; PIDN:AAA34712.1; !1PID:g171768 !'##experimental_source strain S288C !'##note the authors translated the codon GAT for residue 252 as Glu, !1ACG for residue 572 as Gly, and ACA for residue 764 as Tyr !$#accession A38786 !'##molecule_type protein !'##residues 36-57;140-148;412-419;422-443;463,'X',465-470,'X',472,'X', !1474-477;554-567;654-661;723-736;851-862,'X',864-867 ##label !1ENG2 REFERENCE S59184 !$#authors Obermaier, B.; Gassenhuber, J.; Piravandi, E.; Domdey, H. !$#journal Yeast (1995) 11:1103-1112 !$#title Sequence analysis of a 78.6 kb segment of the left end of !1Saccharomyces cerevisiae chromosome II. !$#cross-references MUID:96076635; PMID:7502586 !$#accession S59231 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1072 ##label OBW !'##cross-references EMBL:X79489; NID:g496661; PIDN:CAA56034.1; !1PID:g498991 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1May 1994 GENETICS !$#gene SGD:ILS1; MIPS:YBL076c !'##cross-references SGD:S0000172; MIPS:YBL076c !$#map_position 2L FUNCTION !$#description catalyzes the ligation of isoleucine to tRNA with the !1hydrolysis of ATP to AMP and pyrophosphate !$#pathway protein biosynthesis CLASSIFICATION #superfamily isoleucine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; blocked amino end; ligase; !1protein biosynthesis FEATURE !$54-57 #region ATP binding #status predicted\ !$602-606 #region tRNA binding #status predicted SUMMARY #length 1072 #molecular-weight 122982 #checksum 1749 SEQUENCE /// ENTRY A42399 #type complete TITLE isoleucine-tRNA ligase (EC 6.1.1.5) - Tetrahymena thermophila ORGANISM #formal_name Tetrahymena thermophila DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS A42399 REFERENCE A42399 !$#authors Csank, C.; Martindale, D.W. !$#journal J. Biol. Chem. (1992) 267:4592-4599 !$#title Isoleucyl-tRNA synthetase from the ciliated protozoan !1Tetrahymena thermophila. DNA sequence, gene regulation, and !1leucine zipper motifs. !$#cross-references MUID:92165815; PMID:1371507 !$#accession A42399 !'##status preliminary !'##molecule_type DNA !'##residues 1-1081 ##label CSA !'##cross-references GB:M30942; NID:g161800; PIDN:AAA30122.1; !1PID:g161801 !'##note sequence extracted from NCBI backbone (NCBIN:83878, !1NCBIP:83880) GENETICS !$#genetic_code SGC5 CLASSIFICATION #superfamily isoleucine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ligase; protein biosynthesis SUMMARY #length 1081 #molecular-weight 124850 #checksum 2917 SEQUENCE /// ENTRY SYEXI #type complete TITLE isoleucine-tRNA ligase (EC 6.1.1.5) [validated] - Methanobacterium thermoautotrophicum (strain Marburg) ALTERNATE_NAMES isoleucyl-tRNA synthetase ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 03-Jun-2002 ACCESSIONS A40398 REFERENCE A40398 !$#authors Jenal, U.; Rechsteiner, T.; Tan, P.Y.; Buehlmann, E.; Meile, !1L.; Leisinger, T. !$#journal J. Biol. Chem. (1991) 266:10570-10577 !$#title Isoleucyl-tRNA synthetase of Methanobacterium !1thermoautotrophicum Marburg. Cloning of the gene, nucleotide !1sequence, and localization of a base change conferring !1resistance to pseudomonic acid. !$#cross-references MUID:91244836; PMID:2037598 !$#accession A40398 !'##molecule_type DNA !'##residues 1-1045 ##label JEN !'##cross-references GB:M59245; NID:g149726; PIDN:AAA72950.1; !1PID:g149728 FUNCTION !$#description EC 6.1.1.5 [validated, MUID:91244836] CLASSIFICATION #superfamily isoleucine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; ligase; protein biosynthesis SUMMARY #length 1045 #molecular-weight 121361 #checksum 7139 SEQUENCE /// ENTRY SYECKT #type complete TITLE lysine-tRNA ligase (EC 6.1.1.6) - Escherichia coli (strain K-12) ALTERNATE_NAMES lysyl-tRNA synthetase I ORGANISM #formal_name Escherichia coli DATE 30-Jun-1991 #sequence_revision 21-Nov-1997 #text_change 03-Jun-2002 ACCESSIONS B65073; JS0401; A38066; B31325 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65073 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-505 ##label BLAT !'##cross-references GB:AE000372; GB:U00096; NID:g2367171; !1PIDN:AAC75928.1; PID:g1789256; UWGP:b2890 !'##experimental_source strain K-12, substrain MG1655 REFERENCE JS0401 !$#authors Leveque, F.; Plateau, P.; Dessen, P.; Blanquet, S. !$#journal Nucleic Acids Res. (1990) 18:305-312 !$#title Homology of lysS and lysU, the two Escherichia coli genes !1encoding distinct lysyl-tRNA synthetase species. !$#cross-references MUID:90221811; PMID:2183178 !$#accession JS0401 !'##molecule_type DNA !'##residues 1-396,398-444,'V',445-505 ##label LE1 !'##cross-references GB:X16542 !'##experimental_source strain EM20031 !$#accession A38066 !'##molecule_type protein !'##residues 1-28 ##label LE2 REFERENCE A32651 !$#authors Kawakami, K.; Joensson, Y.H.; Bjoerk, G.R.; Ikeda, H.; !1Nakamura, Y. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:5620-5624 !$#title Chromosomal location and structure of the operon encoding !1peptide-chain-release factor 2 of Escherichia coli. !$#cross-references MUID:88289768; PMID:2456575 !$#accession B31325 !'##molecule_type DNA !'##residues 1-505 ##label KAW !'##cross-references GB:J03795; NID:g146339; PIDN:AAA23959.1; !1PID:g146341 COMMENT In E. coli, lysine is activated and transferred to tRNA by !1two distinct forms of lysyl-tRNA synthetase. The !1constitutive form is encoded by the lysS gene and the !1thermoinducible form is encoded by the lysU gene. GENETICS !$#gene lysS; herC !$#map_position 62 min CLASSIFICATION #superfamily lysine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; homodimer; ligase; protein !1biosynthesis FEATURE !$2-505 #product lysine-tRNA ligase #status predicted #label !8MAT SUMMARY #length 505 #molecular-weight 57603 #checksum 779 SEQUENCE /// ENTRY SYECKU #type complete TITLE lysine-tRNA ligase (EC 6.1.1.6), thermoinducible - Escherichia coli (strain K-12) ALTERNATE_NAMES lysyl-tRNA synthetase II; lysyl-tRNA synthetase, thermoinducible ORGANISM #formal_name Escherichia coli DATE 30-Jun-1991 #sequence_revision 31-Oct-1997 #text_change 03-Jun-2002 ACCESSIONS S56358; H65222; JS0400; JV0093 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56358 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-505 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97029.1; !1PID:g536974 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65222 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-505 ##label BLAT !'##cross-references GB:AE000485; GB:U00096; NID:g1790563; !1PIDN:AAC77090.1; PID:g1790571; UWGP:b4129 !'##experimental_source strain K-12, substrain MG1655 REFERENCE JS0401 !$#authors Leveque, F.; Plateau, P.; Dessen, P.; Blanquet, S. !$#journal Nucleic Acids Res. (1990) 18:305-312 !$#title Homology of lysS and lysU, the two Escherichia coli genes !1encoding distinct lysyl-tRNA synthetase species. !$#cross-references MUID:90221811; PMID:2183178 !$#accession JS0400 !'##molecule_type DNA !'##residues 1-445,'R',447-505 ##label LEV !'##cross-references GB:X16542 REFERENCE JV0093 !$#authors Clark, R.L.; Neidhardt, F.C. !$#journal J. Bacteriol. (1990) 172:3237-3243 !$#title Roles of the two lysyl-tRNA synthetases of Escherichia coli: !1analysis of nucleotide sequences and mutant behavior. !$#cross-references MUID:90264318; PMID:2188953 !$#accession JV0093 !'##molecule_type DNA !'##residues 1-124,126-235,'A',237-257,'HVT',263-267,'R',270-350,'R', !1352-370,'S',372-379,'V',381,'G',383,'V',385-387,'S',389-505 !1##label CLA !'##cross-references GB:M30630; NID:g146688; PIDN:AAA24096.1; !1PID:g146689 COMMENT In E. coli, lysine is activated and transferred to tRNA by !1two distinct forms of lysyl-tRNA synthetase. The !1constitutive form is encoded by the lysS gene and the !1thermoinducible form is encoded by the lysU gene. GENETICS !$#gene lysU !$#map_position 94 min CLASSIFICATION #superfamily lysine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; homodimer; ligase; protein !1biosynthesis FEATURE !$2-505 #product lysine-tRNA ligase #status predicted #label !8MAT SUMMARY #length 505 #molecular-weight 57826 #checksum 2982 SEQUENCE /// ENTRY D64110 #type complete TITLE lysine-tRNA ligase (EC 6.1.1.6) - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES lysyl-tRNA synthetase ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS D64110 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession D64110 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-502 ##label TIGR !'##cross-references GB:U32800; GB:L42023; NID:g1574133; !1PIDN:AAC22865.1; PID:g1574141; TIGR:HI1211 CLASSIFICATION #superfamily lysine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; ligase; protein biosynthesis SUMMARY #length 502 #molecular-weight 56935 #checksum 5980 SEQUENCE /// ENTRY SYBYKT #type complete TITLE lysine-tRNA ligase (EC 6.1.1.6) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES lysyl-tRNA synthetase; protein D3457; protein YD9673.09; protein YDR037w ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 03-Jun-2002 ACCESSIONS A92695; S61592; S20176; S67851; A31899; S17011 REFERENCE A92695 !$#authors Mirande, M.; Waller, J.P. !$#journal J. Biol. Chem. (1988) 263:18443-18451 !$#title The yeast lysyl-tRNA synthetase gene. Evidence for general !1amino acid control of its expression and domain structure of !1the encoded protein. !$#cross-references MUID:89054027; PMID:2903861 !$#accession A92695 !'##molecule_type DNA !'##residues 1-591 ##label MIR !'##cross-references GB:J04186; NID:g171798; PIDN:AAA66916.1; !1PID:g171799 !'##experimental_source strain X2180 REFERENCE S61584 !$#authors Connor, R.; Churcher, C.M. !$#submission submitted to the EMBL Data Library, December 1995 !$#accession S61592 !'##molecule_type DNA !'##residues 1-591 ##label CON !'##cross-references EMBL:Z68196; NID:g1301809; PIDN:CAA92376.1; !1PID:g1122359; GSPDB:GN00004; MIPS:YDR037w !'##experimental_source strain AB972 REFERENCE S20176 !$#authors Martinez, R.; Latreille, M.T.; Mirande, M. !$#journal Mol. Gen. Genet. (1991) 227:149-154 !$#title A PMR2 tandem repeat with a modified C-terminus is located !1downstream from the KRS1 gene encoding lysyl-tRNA synthetase !1in Saccharomyces cerevisiae. !$#cross-references MUID:91260670; PMID:2046655 !$#accession S20176 !'##status translation not shown !'##molecule_type DNA !'##residues 1-21,'V',23-50,'T',52-110,'V',112-161,'H',163-164,'E', !1166-258,'K',260-429,'V',431,'A',433-590,'H' ##label MAR !'##cross-references EMBL:X56259; NID:g3863; PIDN:CAA39699.1; PID:g3864 REFERENCE S67842 !$#authors Arnold, W.; Becker, A.; Jaeger, W.; Kuester, H.; Nussbaumer, !1B. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67851 !'##molecule_type DNA !'##residues 1-591 ##label ARN !'##cross-references EMBL:Z74333; NID:g1431483; PIDN:CAA98863.1; !1PID:g1431484; GSPDB:GN00004; MIPS:YDR037w !'##experimental_source strain S288C GENETICS !$#gene SGD:KRS1; GCD5; MIPS:YDR037w !'##cross-references SGD:S0002444; MIPS:YDR037w !$#map_position 4R CLASSIFICATION #superfamily lysine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; homodimer; ligase; protein !1biosynthesis FEATURE !$2-591 #product lysine-tRNA ligase #status predicted #label !8MAT SUMMARY #length 591 #molecular-weight 67958 #checksum 6349 SEQUENCE /// ENTRY SYECNT #type complete TITLE asparagine-tRNA ligase (EC 6.1.1.22) - Escherichia coli (strain K-12) ALTERNATE_NAMES asparaginyl-tRNA synthetase ORGANISM #formal_name Escherichia coli DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 03-Jun-2002 ACCESSIONS JS0396; S29297; A64833 REFERENCE JS0396 !$#authors Anselme, J.; Haertlein, M. !$#journal Gene (1989) 84:481-485 !$#title Asparaginyl-tRNA synthetase from Escherichia coli has !1significant sequence homologies with yeast aspartyl-tRNA !1synthetase. !$#cross-references MUID:90128294; PMID:2693216 !$#accession JS0396 !'##molecule_type DNA !'##residues 1-466 ##label ANS !'##cross-references GB:M33145; NID:g147934; PIDN:AAA24666.1; !1PID:g147935 !'##experimental_source strain CE1215 !'##note residues 1-11 and 243-256 were confirmed by protein sequencing REFERENCE S29297 !$#authors Aoki, H.; Yaworsky, P.J.; Patel, S.D.; Margolin-Brzezinski, !1D.; Park, K.S.; Ganoza, C. !$#journal Eur. J. Biochem. (1992) 209:511-521 !$#title The asparaginyl-tRNA synthetase gene encodes one of the !1complementing factors for thermosensitive translation in the !1Escherichia coli mutant strain, N4316. !$#cross-references MUID:93049293; PMID:1425658 !$#accession S29297 !'##status preliminary !'##molecule_type DNA !'##residues 1-466 ##label AOK !'##cross-references EMBL:X68192; NID:g40999; PIDN:CAA48274.1; !1PID:g41000 !'##experimental_source strain K-12 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64833 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-466 ##label BLAT !'##cross-references GB:AE000195; GB:U00096; NID:g1787156; !1PIDN:AAC74016.1; PID:g1787161; UWGP:b0930 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene asnS; tss !$#map_position 21 min FUNCTION !$#description charges tRNA(Asn) with L-asparagine by forming !1L-asparaginyl-tRNA and releasing AMP !$#pathway protein biosynthesis CLASSIFICATION #superfamily lysine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; ligase; protein biosynthesis FEATURE !$2-466 #product asparagine-tRNA ligase #status predicted !8#label MAT SUMMARY #length 466 #molecular-weight 52570 #checksum 9774 SEQUENCE /// ENTRY SYHUDT #type complete TITLE aspartate-tRNA ligase (EC 6.1.1.12) [similarity] - human ALTERNATE_NAMES aspartyl-tRNA synthetase ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 03-Jun-2002 ACCESSIONS A34393 REFERENCE A34393 !$#authors Jacobo-Molina, A.; Peterson, R.; Yang, D.C.H. !$#journal J. Biol. Chem. (1989) 264:16608-16612 !$#title cDNA sequence, predicted primary structure, and evolving !1amphiphilic helix of human aspartyl-tRNA synthetase. !$#cross-references MUID:89380283; PMID:2674137 !$#accession A34393 !'##molecule_type mRNA !'##residues 1-500 ##label JAC !'##cross-references GB:J05032; NID:g179101; PIDN:AAA35567.1; !1PID:g179102 COMMENT In mammals, aspartate-tRNA ligase occurs in two distinct !1forms: a dimeric enzyme and a component of a multienzyme !1complex comprising the nine aminoacetyl-tRNA synthetases !1specific for arginine, aspartate, glutamate, glutamine, !1isoleucine, leucine, lysine, methionine, and proline. GENETICS !$#gene GDB:DARS !'##cross-references GDB:9622412 CLASSIFICATION #superfamily lysine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; homodimer; ligase; !1phosphoprotein; protein biosynthesis SUMMARY #length 500 #molecular-weight 57192 #checksum 6887 SEQUENCE /// ENTRY SYRTDT #type complete TITLE aspartate-tRNA ligase (EC 6.1.1.12) - rat ALTERNATE_NAMES aspartyl-tRNA synthetase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 03-Jun-2002 ACCESSIONS A32197 REFERENCE A32197 !$#authors Mirande, M.; Waller, J.P. !$#journal J. Biol. Chem. (1989) 264:842-847 !$#title Molecular cloning and primary structure of cDNA encoding the !1catalytic domain of rat liver aspartyl-tRNA synthetase. !$#cross-references MUID:89093153; PMID:2642907 !$#accession A32197 !'##molecule_type mRNA !'##residues 1-501 ##label MIR !'##cross-references GB:J04487; NID:g203065; PIDN:AAA40789.1; !1PID:g203066 COMMENT In mammals, aspartate-tRNA ligase occurs in two distinct !1forms: a dimeric enzyme and a component of a multienzyme !1complex comprising the nine aminoacetyl-tRNA synthetases !1specific for arginine, aspartate, glutamate, glutamine, !1isoleucine, leucine, lysine, methionine, and proline. GENETICS !$#gene DRS1 CLASSIFICATION #superfamily lysine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; homodimer; ligase; protein !1biosynthesis SUMMARY #length 501 #molecular-weight 57126 #checksum 1449 SEQUENCE /// ENTRY SYBYDC #type complete TITLE aspartate-tRNA ligase (EC 6.1.1.12), cytosolic [validated] - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES aspartyl-tRNA synthetase, cytosolic; protein L1295; protein YLL018c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 03-Jun-2002 ACCESSIONS A23508; A24503; S25391; S64766; S64760; S69388; S70557; !1S13357 REFERENCE A23508 !$#authors Sellami, M.; Fasiolo, F.; Dirheimer, G.; Ebel, J.P.; !1Gangloff, J. !$#journal Nucleic Acids Res. (1986) 14:1657-1666 !$#title Nucleotide sequence of the gene coding for yeast cytoplasmic !1aspartyl-tRNA synthetase (APS); mapping of the 5' and 3' !1termini of AspRS mRNA. !$#cross-references MUID:86148499; PMID:3513127 !$#accession A23508 !'##molecule_type DNA !'##residues 1-557 ##label SEL !'##cross-references GB:X03606; NID:g3369; PIDN:CAA27269.1; PID:g3370 REFERENCE A24503 !$#authors Amiri, I.; Mejdoub, H.; Hounwanou, N.; Boulanger, Y.; !1Reinbolt, J. !$#journal Biochimie (1985) 67:607-613 !$#title The complete amino acid sequence of cytoplasmic !1aspartyl-tRNA synthetase from Saccharomyces cerevisiae. !$#cross-references MUID:86026492; PMID:3902099 !$#accession A24503 !'##molecule_type protein !'##residues 1-557 ##label AMI REFERENCE S25391 !$#authors Reid, G.A. !$#journal Nucleic Acids Res. (1988) 16:1212 !$#title Sequence polymorphisms in the yeast gene encoding aspartyl !1tRNA synthase. !$#cross-references MUID:88144005; PMID:3278298 !$#accession S25391 !'##molecule_type DNA !'##residues 1-557 ##label REI !'##cross-references EMBL:X06665; NID:g3410; PIDN:CAA29865.1; PID:g3411 REFERENCE S64761 !$#authors Goffeau, A.; Purnelle, B. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64766 !'##molecule_type DNA !'##residues 1-557 ##label GOF !'##cross-references EMBL:Z73123; NID:g1360190; PIDN:CAA97464.1; !1PID:g1360191; GSPDB:GN00012; MIPS:YLL018c !'##note experimental_source strain S288C REFERENCE S64743 !$#authors Miosga, T.; Zimmermann, F.K. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64760 !'##molecule_type DNA !'##residues 1-81 ##label MIO !'##cross-references EMBL:Z73123; GSPDB:GN00012; MIPS:YLL018c !'##note experimental_source strain S288C REFERENCE S69380 !$#authors Purnelle, B.; Goffeau, A. !$#submission submitted to the EMBL Data Library, April 1996 !$#description The sequence of 32 kb on the left arm of yeast chromosome !1XII reveals 14 open reading frames among which HSP104, SSA2, !1SPA2, KNS1, DPS1/APS, SDC25, a new member of the !1seripauperins family and a new ABC transporter homologous to !1the human multidrug resistance protein. !$#accession S69388 !'##molecule_type DNA !'##residues 1-557 ##label PUR !'##cross-references EMBL:X97560; NID:g1297003; PIDN:CAA66172.1; !1PID:g1297012 REFERENCE S70557 !$#authors Miosga, T.; Zimmermann, F.K. !$#journal Yeast (1996) 12:693-708 !$#title Sequence analysis of the CEN12 region of Saccharomyces !1cerevisiae on a 43.7 kb fragment of chromosome XII including !1an open reading frame homologous to the human cystic !1fibrosis transmembrane conductance regulator protein CFTR. !$#cross-references MUID:96405918; PMID:8810043 !$#accession S70557 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-81 ##label MIW !'##cross-references EMBL:X91488; NID:g1495203; PIDN:CAA62772.1; !1PID:g1495204 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1September 1995 GENETICS !$#gene SGD:DPS1; APS1; MIPS:YLL018c !'##cross-references SGD:S0003941; MIPS:YLL018c !$#map_position 12L COMPLEX homodimer [validated, MUID:86026492] FUNCTION !$#description EC 6.1.1.12 [validated, MUID:86026492] !$#pathway protein biosynthesis CLASSIFICATION #superfamily lysine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; homodimer; ligase; protein !1biosynthesis SUMMARY #length 557 #molecular-weight 63515 #checksum 8347 SEQUENCE /// ENTRY SYBYDM #type complete TITLE aspartate-tRNA ligase (EC 6.1.1.12), mitochondrial - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES aspartyl-tRNA synthetase, mitochondrial; protein LPG5w; protein YPL104w ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1992 #sequence_revision 10-May-1996 #text_change 03-Jun-2002 ACCESSIONS S61963; A33279 REFERENCE S61959 !$#authors Wang, Y.; Ahmed, A.; Bussey, H.; Fortin, N.; Friesen, J.D.; !1Hall, J.; Storms, R.K.; Vo, D.H.; Winnett, E. !$#submission submitted to the EMBL Data Library, December 1995 !$#description The sequence of Saccharomyces cerevisiae chromosome XVI left !1arm. !$#accession S61963 !'##molecule_type DNA !'##residues 1-658 ##label WAN !'##cross-references EMBL:U43281; NID:g1151218; PIDN:AAB68196.1; !1PID:g1151223; GSPDB:GN00016; MIPS:YPL104w REFERENCE A33279 !$#authors Gampel, A.; Tzagoloff, A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:6023-6027 !$#title Homology of aspartyl- and lysyl-tRNA synthetases. !$#cross-references MUID:89345597; PMID:2668951 !$#accession A33279 !'##molecule_type DNA !'##residues 1-32,'L',34-290,'W',292-658 ##label GAM !'##cross-references GB:M26020; GB:M24418 GENETICS !$#gene SGD:MSD1; MIPS:YPL104w !'##cross-references SGD:S0006025; MIPS:YPL104w !$#map_position 16L CLASSIFICATION #superfamily lysine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; homodimer; ligase; !1mitochondrion; protein biosynthesis SUMMARY #length 658 #molecular-weight 75460 #checksum 5379 SEQUENCE /// ENTRY SYECD #type complete TITLE aspartate-tRNA ligase (EC 6.1.1.12) - Escherichia coli (strain K-12) ALTERNATE_NAMES aspartyl-tRNA synthetase ORGANISM #formal_name Escherichia coli DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 03-Jun-2002 ACCESSIONS JT0942; S23761; A38113; B64949 REFERENCE JT0942 !$#authors Eriani, G.; Dirheimer, G.; Gangloff, J. !$#journal Nucleic Acids Res. (1990) 18:7109-7118 !$#title Aspartyl-tRNA synthetase from Escherichia coli: cloning and !1characterisation of the gene, homologies of its translated !1amino acid sequence with asparaginyl- and lysyl-tRNA !1synthetases. !$#cross-references MUID:91088291; PMID:2129559 !$#accession JT0942 !'##molecule_type DNA !'##residues 1-590 ##label ERI !'##cross-references GB:X53863; NID:g41014; PIDN:CAA37856.1; PID:g41015 !'##experimental_source strain K-12 REFERENCE S23761 !$#authors Sharples, G.J.; Lloyd, R.G. !$#journal Mutat. Res. (1991) 264:93-96 !$#title Location of a mutation in the aspartyl-tRNA synthetase gene !1of Escherichia coli K 12. !$#cross-references MUID:92049526; PMID:1944398 !$#accession S23761 !'##molecule_type DNA !'##residues 382-590 ##label SHA !'##cross-references EMBL:X53984; NID:g43084; PIDN:CAA37932.1; !1PID:g43085 !'##experimental_source strain K-12 REFERENCE A38113 !$#authors Takahagi, M.; Iwasaki, H.; Nakata, A.; Shinagawa, H. !$#journal J. Bacteriol. (1991) 173:5747-5753 !$#title Molecular analysis of the Escherichia coli ruvC gene, which !1encodes a Holliday junction-specific endonuclease. !$#cross-references MUID:91358366; PMID:1885548 !$#accession A38113 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 461-590 ##label TAK !'##cross-references GB:D90392 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64949 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-590 ##label BLAT !'##cross-references GB:AE000280; GB:U00096; NID:g1788163; !1PIDN:AAC74936.1; PID:g1788173; UWGP:b1866 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene aspS; tls COMPLEX homodimer FUNCTION !$#description activates amino acid and transfers it to specific tRNA !1molecule !$#pathway protein biosynthesis CLASSIFICATION #superfamily lysine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; homodimer; ligase; protein !1biosynthesis SUMMARY #length 590 #molecular-weight 65913 #checksum 9019 SEQUENCE /// ENTRY E64061 #type complete TITLE aspartate-tRNA ligase (EC 6.1.1.12) - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES aspartyl-tRNA synthetase ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS E64061 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession E64061 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-588 ##label TIGR !'##cross-references GB:U32717; GB:L42023; NID:g1573283; !1PIDN:AAC21981.1; PID:g1573287; TIGR:HI0317 GENETICS !$#gene aspS FUNCTION !$#description activates amino acid and transfers it to specific tRNA !1molecule !$#pathway protein biosynthesis CLASSIFICATION #superfamily lysine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; ligase; protein biosynthesis SUMMARY #length 588 #molecular-weight 66639 #checksum 3996 SEQUENCE /// ENTRY S42047 #type complete TITLE aspartate-tRNA ligase (EC 6.1.1.12) - Mycobacterium leprae ALTERNATE_NAMES aspartyl-tRNA synthetase ORGANISM #formal_name Mycobacterium leprae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S42047 REFERENCE S42047 !$#authors Spierings, E.H.T.; Wieles, B.; Thole, J.E.R. !$#submission submitted to the EMBL Data Library, February 1994 !$#accession S42047 !'##status preliminary !'##molecule_type DNA !'##residues 1-589 ##label SPI !'##cross-references EMBL:X77655; NID:g454973; PIDN:CAA54735.1; !1PID:g581332 GENETICS !$#gene ASPS !$#start_codon GTG FUNCTION !$#description activates amino acid and transfers it to specific tRNA !1molecule !$#pathway protein biosynthesis CLASSIFICATION #superfamily lysine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; ligase; protein biosynthesis SUMMARY #length 589 #molecular-weight 64630 #checksum 93 SEQUENCE /// ENTRY S33743 #type complete TITLE aspartate-tRNA ligase (EC 6.1.1.12) - Thermus aquaticus ALTERNATE_NAMES aspartyl-tRNA synthetase ORGANISM #formal_name Thermus aquaticus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S33743 REFERENCE S33743 !$#authors Poterszman, A.; Plateau, P.; Moras, D.; Blanquet, S.; !1Mazauric, M.H.; Kreutzer, R.; Kern, D. !$#journal FEBS Lett. (1993) 325:183-186 !$#title Sequence, overproduction and crystallization of !1aspartyl-tRNA synthetase from Thermus thermophilus. !1Implications for the structure of prokaryotic aspartyl-tRNA !1synthetases. !$#cross-references MUID:93307491; PMID:8319804 !$#accession S33743 !'##molecule_type DNA !'##residues 1-580 ##label POT !'##cross-references EMBL:X70943; NID:g396500; PIDN:CAA50282.1; !1PID:g396501 !'##experimental_source strain VK-1 GENETICS !$#gene aspS FUNCTION !$#description activates amino acid and transfers it to specific tRNA !1molecule !$#pathway protein biosynthesis CLASSIFICATION #superfamily lysine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; ligase; protein biosynthesis SUMMARY #length 580 #molecular-weight 66029 #checksum 2986 SEQUENCE /// ENTRY SYMTAT #type complete TITLE alanine-tRNA ligase (EC 6.1.1.7) - silkworm ORGANISM #formal_name Bombyx mori #common_name silkworm DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 03-Jun-2002 ACCESSIONS A38327; S16072 REFERENCE A38327 !$#authors Chang, P.K.; Dignam, J.D. !$#journal J. Biol. Chem. (1990) 265:20898-20906 !$#title Primary structure of alanyl-tRNA synthetase and the !1regulation of its mRNA levels in Bombyx mori. !$#cross-references MUID:91065890; PMID:1701172 !$#accession A38327 !'##molecule_type DNA !'##residues 1-967 ##label CHA !'##cross-references GB:M55993; GB:J05684; NID:g155954; PIDN:AAA27821.1; !1PID:g155955 REFERENCE S16072 !$#authors Dignam, J.D.; Dignam, S.S.; Brumley, L.L. !$#journal Eur. J. Biochem. (1991) 198:201-210 !$#title Alanyl-tRNA synthetase from Escherichia coli, Bombyx mori !1and Ratus ratus. Existence of common structural features. !$#cross-references MUID:91249799; PMID:2040280 !$#accession S16072 !'##molecule_type DNA !'##residues 456-488 ##label DIG !'##cross-references GB:J05684 CLASSIFICATION #superfamily alanine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; ligase; protein biosynthesis SUMMARY #length 967 #molecular-weight 108177 #checksum 6136 SEQUENCE /// ENTRY SYECAT #type complete TITLE alanine-tRNA ligase (EC 6.1.1.7) [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES alanyl-tRNA synthetase ORGANISM #formal_name Escherichia coli DATE 31-Mar-1981 #sequence_revision 31-Oct-1997 #text_change 03-Jun-2002 ACCESSIONS E65049; A01185; A94258; A40608; I40988; A54217 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65049 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-876 ##label BLAT !'##cross-references GB:AE000353; GB:U00096; NID:g1789037; !1PIDN:AAC75739.1; PID:g1789048; UWGP:b2697 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A93864 !$#authors Herlihy, W.C.; Royal, N.J.; Biemann, K.; Putney, S.D.; !1Schimmel, P.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1980) 77:6531-6535 !$#title Mass spectra of partial protein hydrolysates as a multiple !1phase check for long polypeptides deduced from DNA !1sequences: NH-2-terminal segment of alanine tRNA synthetase. !$#cross-references MUID:81101084; PMID:7005898 !$#accession A01185 !'##molecule_type DNA !'##residues 1-28,'RY',31,'IT',34-157,'N',159-166 ##label HER REFERENCE A94258 !$#authors Putney, S.D.; Royal, N.J.; de Vegvar, H.N.; Herlihy, W.C.; !1Biemann, K.; Schimmel, P. !$#journal Science (1981) 213:1497-1501 !$#title Primary structure of a large aminoacyl-tRNA synthetase. !$#cross-references MUID:82017165; PMID:7025207 !$#accession A94258 !'##molecule_type DNA !'##residues 2-28,'RY',31,'IT',34-157,'N',159-167,'G',169-171,'R', !1173-174,'G',176-179,'D',181-583,'H',585-618,'L',620-876 !1##label PUT !'##cross-references GB:J01581; GB:J01582; NID:g414793; PIDN:AAA03208.1; !1PID:g145220 REFERENCE A40608 !$#authors Romeo, T.; Gong, M.; Liu, M.Y.; Brun-Zinkernagel, A.M. !$#journal J. Bacteriol. (1993) 175:4744-4755 !$#title Identification and molecular characterization of csrA, a !1pleiotropic gene from Escherichia coli that affects glycogen !1biosynthesis, gluconeogenesis, cell size, and surface !1properties. !$#cross-references MUID:93328679; PMID:8393005 !$#accession A40608 !'##molecule_type DNA !'##residues 866-876 ##label ROM !'##cross-references GB:L07596 REFERENCE I40988 !$#authors Putney, S.D.; Melendez, D.L.; Schimmel, P.R. !$#journal J. Biol. Chem. (1981) 256:205-211 !$#title Cloning, partial sequencing, and in vitro transcription of !1the gene for alanine tRNA synthetase. !$#cross-references MUID:81093926; PMID:6256345 !$#accession I40988 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-13 ##label RES !'##cross-references EMBL:Z28405; NID:g433884; PIDN:CAA82247.1; !1PID:g433885 REFERENCE A54217 !$#authors Musier-Forsyth, K.; Schimmel, P. !$#journal Biochemistry (1994) 33:773-779 !$#title Acceptor helix interactions in a class II tRNA synthetase: !1photoaffinity cross-linking of an RNA miniduplex substrate. !$#cross-references MUID:94122190; PMID:8292605 !$#accession A54217 !'##status preliminary !'##molecule_type protein !'##residues 'X',163-170,'X',172-173 ##label MUS GENETICS !$#gene alaS !$#map_position 58 min COMPLEX homodimer; predominant form at 25 degrees [validated, !1MUID:96213879] FUNCTION !$#description EC 6.1.1.7 [validated, MUID:96213879] !$#note catalytic core is not required for oligomer assembly CLASSIFICATION #superfamily alanine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; homodimer; ligase; protein !1biosynthesis SUMMARY #length 876 #molecular-weight 96032 #checksum 9257 SEQUENCE /// ENTRY SYECVT #type complete TITLE valine-tRNA ligase (EC 6.1.1.9) - Escherichia coli (strain K-12) ALTERNATE_NAMES valyl-tRNA synthetase ORGANISM #formal_name Escherichia coli DATE 31-Mar-1989 #sequence_revision 10-Oct-1997 #text_change 03-Jun-2002 ACCESSIONS E65238; A27302; B27302; A28522; S56484 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65238 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-951 ##label BLAT !'##cross-references GB:AE000496; GB:U00096; NID:g2367366; !1PIDN:AAC77215.1; PID:g1790708; UWGP:b4258 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A27302 !$#authors Haertlein, M.; Frank, R.; Madern, D. !$#journal Nucleic Acids Res. (1987) 15:9081-9082 !$#title Nucleotide sequence of Escherichia coli valyl-tRNA !1synthetase gene valS. !$#cross-references MUID:88067721; PMID:3317277 !$#accession A27302 !'##molecule_type DNA !'##residues 1-693,'T',695-951 ##label HA1 !'##cross-references GB:X05891; NID:g43301; PIDN:CAA29322.1; PID:g43302 !$#accession B27302 !'##molecule_type protein !'##residues 1-16 ##label HA2 REFERENCE A28522 !$#authors Heck, J.D.; Hatfield, G.W. !$#journal J. Biol. Chem. (1988) 263:868-877 !$#title Valyl-tRNA synthetase gene of Escherichia coli K12. Primary !1structure and homology within a family of aminoacyl-tRNA !1synthetases. !$#cross-references MUID:88087212; PMID:3275660 !$#accession A28522 !'##molecule_type DNA !'##residues 1-106,'A',108-832,'R',834-951 ##label HEC !'##cross-references GB:J03497; NID:g147905; PIDN:AAA24657.1; !1PID:g147906; GB:M18739 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56484 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-693,'X',695-951 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97155.1; !1PID:g537100 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 GENETICS !$#gene valS !$#map_position 97 min CLASSIFICATION #superfamily valine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; ligase; protein biosynthesis SUMMARY #length 951 #molecular-weight 108192 #checksum 1846 SEQUENCE /// ENTRY SYBSVS #type complete TITLE valine-tRNA ligase (EC 6.1.1.9) - Bacillus stearothermophilus ALTERNATE_NAMES valyl-tRNA synthetase ORGANISM #formal_name Bacillus stearothermophilus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 03-Jun-2002 ACCESSIONS A26738 REFERENCE A26738 !$#authors Borgford, T.J.; Brand, N.J.; Gray, T.E.; Fersht, A.R. !$#journal Biochemistry (1987) 26:2480-2486 !$#title The valyl-tRNA synthetase from Bacillus stearothermophilus !1has considerable sequence homology with the isoleucyl-tRNA !1synthetase from Escherichia coli. !$#cross-references MUID:87271643; PMID:3300774 !$#accession A26738 !'##molecule_type DNA !'##residues 1-880 ##label BOR !'##cross-references GB:M16318 GENETICS !$#gene valS CLASSIFICATION #superfamily valine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; ligase; protein biosynthesis SUMMARY #length 880 #molecular-weight 102025 #checksum 2823 SEQUENCE /// ENTRY S41420 #type complete TITLE valine-tRNA ligase (EC 6.1.1.9) valS - Bacillus subtilis ALTERNATE_NAMES valyl-tRNA synthetase valS ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S41420; A40646; B69730 REFERENCE S41420 !$#authors Putzer, H.; Leautey, J. !$#submission submitted to the EMBL Data Library, January 1994 !$#accession S41420 !'##molecule_type DNA !'##residues 1-880 ##label PUT !'##cross-references EMBL:X77239; NID:g452308; PIDN:CAA54458.1; !1PID:g452309 REFERENCE A40646 !$#authors Margolis, P.S.; Driks, A.; Losick, R. !$#journal J. Bacteriol. (1993) 175:528-540 !$#title Sporulation gene spoIIB from Bacillus subtilis. !$#cross-references MUID:93123172; PMID:8419299 !$#accession A40646 !'##molecule_type DNA !'##residues 825-880 ##label MAR !'##cross-references GB:L04520; NID:g142934; PIDN:AAB59020.1; !1PID:g142935 !'##note sequence extracted from NCBI backbone (NCBIN:122728, !1NCBIP:122729) REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69730 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-880 ##label KUN !'##cross-references GB:Z99118; GB:AL009126; NID:g2635200; !1PIDN:CAB14769.1; PID:g2635274 !'##experimental_source strain 168 GENETICS !$#gene valS CLASSIFICATION #superfamily valine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; ligase; protein biosynthesis SUMMARY #length 880 #molecular-weight 101746 #checksum 71 SEQUENCE /// ENTRY A49856 #type complete TITLE valine-tRNA ligase (EC 6.1.1.9) - Lactobacillus casei ALTERNATE_NAMES valyl-tRNA synthetase ORGANISM #formal_name Lactobacillus casei DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS A49856 REFERENCE A49856 !$#authors Taylor, B.V.; Toy, J.; Sit, T.L.; Bognar, A.L. !$#journal J. Bacteriol. (1993) 175:2475-2478 !$#title Cloning and sequence determination of the valS gene, !1encoding valyl-tRNA synthetase in Lactobacillus casei. !$#cross-references MUID:93224476; PMID:8468307 !$#accession A49856 !'##status preliminary !'##molecule_type DNA !'##residues 1-901 ##label TAY !'##cross-references GB:L08854; NID:g409359; PIDN:AAA57558.1; !1PID:g409360 !'##note sequence extracted from NCBI backbone (NCBIN:129327, !1NCBIP:129328) CLASSIFICATION #superfamily valine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ligase; protein biosynthesis SUMMARY #length 901 #molecular-weight 103143 #checksum 8061 SEQUENCE /// ENTRY SYBYVT #type complete TITLE valine-tRNA ligase (EC 6.1.1.9) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein G4647; protein YGR094w; valyl-tRNA synthetase ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1992 #sequence_revision 19-Jul-1996 #text_change 03-Jun-2002 ACCESSIONS S64389; S64399; A29871 REFERENCE S64356 !$#authors Wedler, H.; Scharfe, M.; Wedler, E.; Wambutt, R. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64389 !'##molecule_type DNA !'##residues 1-1104 ##label WED !'##cross-references EMBL:Z72879; NID:g1323140; PIDN:CAA97097.1; !1PID:g1323141; GSPDB:GN00007; MIPS:YGR094w !'##experimental_source strain S288C REFERENCE S64392 !$#authors Hernandez, K.; Weber, N.; Wipfli, P.; Schmidheini, T. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64399 !'##molecule_type DNA !'##residues 1-1104 ##label HER !'##cross-references EMBL:Z72879; NID:g1323140; PIDN:CAA97097.1; !1PID:g1323141; GSPDB:GN00007; MIPS:YGR094w !'##experimental_source strain S288C REFERENCE A29871 !$#authors Jordana, X.; Chatton, B.; Paz-Weisshaar, M.; Buhler, J.M.; !1Cramer, F.; Ebel, J.P.; Fasiolo, F. !$#journal J. Biol. Chem. (1987) 262:7189-7194 !$#title Structure of the yeast valyl-tRNA synthetase gene (VASI) and !1the homology of its translated amino acid sequence with !1Escherichia coli isoleucyl-tRNA synthetase. !$#cross-references MUID:87222321; PMID:3294828 !$#accession A29871 !'##molecule_type DNA !'##residues 1-146,'G',148-539,'K',541-1104 ##label JOR !'##cross-references GB:J02719; NID:g173163; PIDN:AAA35207.1; !1PID:g173164 GENETICS !$#gene SGD:VAS1; MIPS:YGR094w !'##cross-references SGD:S0003326; MIPS:YGR094w !$#map_position 7R CLASSIFICATION #superfamily valine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; ligase; protein biosynthesis SUMMARY #length 1104 #molecular-weight 125769 #checksum 6116 SEQUENCE /// ENTRY SYECMT #type complete TITLE methionine-tRNA ligase (EC 6.1.1.10) [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES methionyl-tRNA synthetase ORGANISM #formal_name Escherichia coli DATE 13-Jun-1983 #sequence_revision 30-Jun-1992 #text_change 23-Dec-2002 ACCESSIONS S14427; A91797; A91123; S11949; A64979; A01187; A35821 REFERENCE S14427 !$#authors Dardel, F. !$#submission submitted to the EMBL Data Library, October 1990 !$#accession S14427 !'##molecule_type DNA !'##residues 1-677 ##label DAR1 !'##cross-references EMBL:X55791; NID:g42015; PIDN:CAA39315.1; !1PID:g42016 REFERENCE A91797 !$#authors Dardel, F.; Fayat, G.; Blanquet, S. !$#journal J. Bacteriol. (1984) 160:1115-1122 !$#title Molecular cloning and primary structure of the Escherichia !1coli methionyl-tRNA synthetase gene. !$#cross-references MUID:85054627; PMID:6094501 !$#accession A91797 !'##molecule_type DNA !'##residues 2-677 ##label DAR2 !'##cross-references GB:K02671; NID:g146828; PIDN:AAA24161.1; !1PID:g146829; GB:J01649; GB:J01650 REFERENCE A91123 !$#authors Barker, D.G.; Ebel, J.P.; Jakes, R.; Bruton, C.J. !$#journal Eur. J. Biochem. (1982) 127:449-457 !$#title Methionyl-tRNA synthetase from E. coli: primary structure of !1the active crystallised tryptic fragment. !$#cross-references MUID:83079258; PMID:6756915 !$#accession A91123 !'##molecule_type DNA !'##residues 2-15,'V',17-149,'L',151-435,'A',437-564 ##label BAR !'##cross-references GB:K02671; GB:J01649; GB:J01650 !'##note most of this sequence was confirmed by protein sequencing REFERENCE S11948 !$#authors Dardel, F.; Panvert, M.; Fayat, G. !$#journal Mol. Gen. Genet. (1990) 223:121-133 !$#title Transcription and regulation of expression of the !1Escherichia coli methionyl-tRNA synthetase gene. !$#cross-references MUID:91080852; PMID:2259334 !$#accession S11949 !'##molecule_type DNA !'##residues 1-51;661-677 ##label DAR !'##cross-references EMBL:X55791 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64979 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-677 ##label BLAT !'##cross-references GB:AE000300; GB:U00096; NID:g1788425; !1PIDN:AAC75175.1; PID:g1788432; UWGP:b2114 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A92880 !$#authors Zelwer, C.; Risler, J.L.; Brunie, S. !$#journal J. Mol. Biol. (1982) 155:63-81 !$#title Crystal structure of Escherichia coli methionyl-tRNA !1synthetase at 2.5 A resolution. !$#cross-references MUID:82192427; PMID:7042987 !$#contents annotation; X-ray crystallography, 2.5 angstroms REFERENCE A35821 !$#authors Hountondji, C.; Schmitter, J.M.; Beauvallet, C.; Blanquet, !1S. !$#journal Biochemistry (1990) 29:8190-8198 !$#title Mapping of the active site of Escherichia coli !1methionyl-tRNA synthetase: identification of amino acid !1residues labeled by periodate-oxidized tRNA(fMet) molecules !1having modified lengths at the 3'-acceptor end. !$#cross-references MUID:91084494; PMID:1702021 !$#contents annotation; active site REFERENCE A51298 !$#authors Fourmy, D.; Dardel, F. !$#submission submitted to the Brookhaven Protein Data Bank, November 1992 !$#cross-references PDB:1MEA !$#contents annotation; conformation by (1)H-NMR, residues 'GS',139-164 REFERENCE A58691 !$#authors Fourmy, D.; Dardel, F.; Blanquet, S. !$#journal J. Mol. Biol. (1993) 231:1078-1089 !$#title Methionyl-tRNA synthetase zinc binding domain. !1Three-dimensional structure and homology with rubredoxin and !1gag retroviral proteins. !$#cross-references MUID:93294859; PMID:8515466 !$#contents annotation; conformation by (1)H-NMR REFERENCE A58692 !$#authors Brunie, S.; Zelwer, C.; Risler, J.L. !$#journal J. Mol. Biol. (1990) 216:411-424 !$#title Crystallographic study at 2.5 Angstroms resolution of the !1interaction of methionyl-tRNA synthetase from Escherichia !1coli with ATP. !$#cross-references MUID:91073404; PMID:2254937 !$#contents annotation; X-ray crystallography, 2.5 angstroms GENETICS !$#gene metG !$#map_position 46 min FUNCTION !$#description EC 6.1.1.10 [validated, MUID:83079258]; catalyzes the !1ligation of methionine to tRNA with the hydrolysis of ATP to !1AMP and pyrophosphate !$#pathway protein biosynthesis CLASSIFICATION #superfamily methionyl-tRNA synthetase, dimer-forming KEYWORDS aminoacyl-tRNA synthetase; ATP; homodimer; ligase; !1metalloprotein; protein biosynthesis; zinc FEATURE !$2-677 #product methionine-tRNA ligase #status predicted !8#label MAT\ !$62-66,137-157, !$335-341,434-438 #region tRNA 3'-acceptor end binding\ !$452-468 #region anticodon recognition\ !$16,22,53,336 #active_site Tyr, His, Asp, Lys #status predicted\ !$146,149,159,162 #binding_site zinc (Cys) #status experimental SUMMARY #length 677 #molecular-weight 76254 #checksum 6231 SEQUENCE /// ENTRY SYTWMT #type complete TITLE methionine-tRNA ligase (EC 6.1.1.10) - Thermus aquaticus ALTERNATE_NAMES methionyl-tRNA synthetase ORGANISM #formal_name Thermus aquaticus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 23-Dec-2002 ACCESSIONS A39517 REFERENCE A39517 !$#authors Nureki, O.; Muramatsu, T.; Suzuki, K.; Kohda, D.; Matsuzawa, !1H.; Ohta, T.; Miyazawa, T.; Yokoyama, S. !$#journal J. Biol. Chem. (1991) 266:3268-3277 !$#title Methionyl-tRNA synthetase gene from an extreme thermophile, !1Thermus thermophilus HB8. Molecular cloning, !1primary-structure analysis, expression in Escherichia coli, !1and site-directed mutagenesis. !$#cross-references MUID:91131636; PMID:1993699 !$#accession A39517 !'##molecule_type DNA !'##residues 1-616 ##label NUR !'##cross-references GB:M64273; GB:J05744; NID:g155135; PIDN:AAA27510.1; !1PID:g155136 !'##experimental_source strain HB8, ATCC 27634 !'##note the authors translated the codon TAC for residue 323 as Thr GENETICS !$#gene metS CLASSIFICATION #superfamily methionyl-tRNA synthetase, dimer-forming KEYWORDS aminoacyl-tRNA synthetase; ATP; homodimer; ligase; protein !1biosynthesis FEATURE !$13,19,50,300 #active_site Tyr, His, Asp, Lys #status predicted SUMMARY #length 616 #molecular-weight 70638 #checksum 4201 SEQUENCE /// ENTRY SYBYMM #type complete TITLE methionine-tRNA ligase (EC 6.1.1.10), mitochondrial - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES methionyl-tRNA synthetase; protein G7104; protein YGR171c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1992 #sequence_revision 19-Jul-1996 #text_change 23-Dec-2002 ACCESSIONS S64485; S07854 REFERENCE S64003 !$#authors Hebling, U.; Hofmann, B.; Delius, H. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64485 !'##molecule_type DNA !'##residues 1-575 ##label HEB !'##cross-references EMBL:Z72956; NID:g1323301; PIDN:CAA97197.1; !1PID:g1323302; GSPDB:GN00007; MIPS:YGR171c !'##experimental_source strain S288C REFERENCE S07854 !$#authors Tzagoloff, A.; Vambutas, A.; Akai, A. !$#journal Eur. J. Biochem. (1989) 179:365-371 !$#title Characterization of MSM1, the structural gene for yeast !1mitochondrial methionyl-tRNA synthetase. !$#cross-references MUID:89137113; PMID:2645139 !$#accession S07854 !'##molecule_type DNA !'##residues 1-13,'I',15-575 ##label TZA !'##cross-references EMBL:X14629; NID:g3997; PIDN:CAA32778.1; PID:g3998 GENETICS !$#gene SGD:MSM1; MIPS:YGR171c !'##cross-references SGD:S0003403; MIPS:YGR171c !$#map_position 7R !$#genome nuclear CLASSIFICATION #superfamily Mycobacterium tuberculosis methionine-tRNA !1ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; ligase; mitochondrion; !1protein biosynthesis SUMMARY #length 575 #molecular-weight 66734 #checksum 9298 SEQUENCE /// ENTRY SYBYMT #type complete TITLE methionine-tRNA ligase (EC 6.1.1.10), cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES methionyl-tRNA synthetase; protein G9340; protein YGR264c ORGANISM #formal_name Saccharomyces cerevisiae DATE 17-May-1985 #sequence_revision 19-Jul-1996 #text_change 23-Dec-2002 ACCESSIONS S64597; A25424; A01186; A21179 REFERENCE S64591 !$#authors Panzeri, L.; Agostoni Carbone, M.L.; Melchioretto, P.; !1Plevani, P.; Martegani, E.; Vanoni, M.; Carignani, G.; !1Clemente, M.L.; Frontali, L.; Fabiani, L.; Marconi, A.; !1Ruzzi, M.; Saliola, M. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64597 !'##molecule_type DNA !'##residues 1-751 ##label PAN !'##cross-references EMBL:Z73049; NID:g1323480; PIDN:CAA97293.1; !1PID:g1323481; GSPDB:GN00007; MIPS:YGR264c !'##experimental_source strain S288C REFERENCE A25424 !$#authors Fasiolo, F.; Gibson, B.W.; Walter, P.; Chatton, B.; Biemann, !1K.; Boulanger, Y. !$#journal J. Biol. Chem. (1985) 260:15571-15576 !$#title Cytoplasmic methionyl-tRNA synthetase from bakers' yeast. A !1monomer with a post-translationally modified N terminus. !$#cross-references MUID:86059432; PMID:3905796 !$#accession A25424 !'##molecule_type protein !'##residues 1-121,'A',123-568,'N',570-751 ##label FAS REFERENCE A01186 !$#authors Walter, P.; Gangloff, J.; Bonnet, J.; Boulanger, Y.; Ebel, !1J.P.; Fasiolo, F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:2437-2441 !$#title Primary structure of the Saccharomyces cerevisiae gene for !1methionyl-tRNA synthetase. !$#cross-references MUID:83195073; PMID:6341994 !$#accession A01186 !'##molecule_type DNA !'##residues 1-121,'A',123-306,'C',308-462,'I',464-751 ##label WAL !'##cross-references EMBL:V01316 !'##note the authors translated the codon TGC for residue 307 as Ser and !1ATT for residue 463 as Asn REFERENCE A21179 !$#authors Gibson, B.W.; Biemann, K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:1956-1960 !$#title Strategy for the mass spectrometric verification and !1correction of the primary structures of proteins deduced !1from their DNA sequences. !$#cross-references MUID:84193935; PMID:6371805 !$#accession A21179 !'##molecule_type protein !'##residues 10-70,72-90 ##label GIB GENETICS !$#gene SGD:MES1; MIPS:YGR264c !'##cross-references SGD:S0003496; MIPS:YGR264c !$#map_position 7R CLASSIFICATION #superfamily Mycobacterium tuberculosis methionine-tRNA !1ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; ligase; protein !1biosynthesis; zinc FEATURE !$206,212,244,528 #active_site Tyr, His, Asp, Lys #status predicted\ !$337,340,350,353 #binding_site zinc (Cys) #status predicted SUMMARY #length 751 #molecular-weight 85677 #checksum 6045 SEQUENCE /// ENTRY YSBYC #type complete TITLE serine-tRNA ligase (EC 6.1.1.11), cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein D3270; protein PZA462; protein YD9813.01; protein YDR023w; seryl-tRNA synthetase ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1992 #sequence_revision 12-May-1995 #text_change 03-Jun-2002 ACCESSIONS S50930; A26565; S44601; S63431; S67836; S72122 REFERENCE S50930 !$#authors Bowman, S. !$#submission submitted to the EMBL Data Library, January 1994 !$#accession S50930 !'##molecule_type DNA !'##residues 1-462 ##label BOW !'##cross-references EMBL:Z47814; NID:g642294; PIDN:CAA87802.1; !1PID:g642295; GSPDB:GN00004; MIPS:YDR023w REFERENCE A26565 !$#authors Weygand-Durasevic, I.; Johnson-Burke, D.; Soell, D. !$#journal Nucleic Acids Res. (1987) 15:1887-1904 !$#title Cloning and characterization of the gene coding for !1cytoplasmic seryl-tRNA synthetase from Saccharomyces !1cerevisiae. !$#cross-references MUID:87174725; PMID:3031581 !$#accession A26565 !'##molecule_type DNA !'##residues 1-223,'P',225-462 ##label WEY !'##cross-references GB:X04884; NID:g4457; PIDN:CAA28572.1; PID:g4458 REFERENCE S44600 !$#authors Folley, L.S.; Fox, T.D. !$#submission submitted to the EMBL Data Library, November 1993 !$#accession S44601 !'##molecule_type DNA !'##residues 451-462 ##label FOL !'##cross-references EMBL:L15408; NID:g295652; PIDN:AAC37412.1; !1PID:g295654 REFERENCE S63416 !$#authors Eide, L.G.; Sander, C.; Prydz, H. !$#submission submitted to the EMBL Data Library, February 1996 !$#description Sequencing and analysis of a 35.4 kb region on the left arm !1of chromosome IV for Saccharomyces cerevisiae reveal 23 open !1reading frames. !$#accession S63431 !'##molecule_type DNA !'##residues 1-462 ##label EID !'##cross-references EMBL:X95966; NID:g1216215; PIDN:CAA65216.1; !1PID:g1216231 REFERENCE S67822 !$#authors Prydz, H.; Eide, L.G. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67836 !'##molecule_type DNA !'##residues 1-462 ##label PRY !'##cross-references EMBL:Z74319; NID:g1431453; PIDN:CAA98844.1; !1PID:g1431454; GSPDB:GN00004; MIPS:YDR023w !'##experimental_source strain S288C REFERENCE S72107 !$#authors Eide, L.G.; Sander, C.; Prydz, H. !$#journal Yeast (1996) 12:1085-1090 !$#title Sequencing and analysis of a 35.4 kb region on the left arm !1of chromosome IV from Saccharomyces cerevisiae reveal 23 !1open reading frames. !$#cross-references MUID:97051598; PMID:8896275 !$#accession S72122 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-462 ##label EIW !'##cross-references EMBL:X95966; NID:g1216215; PIDN:CAA65216.1; !1PID:g1216231 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1February 1996 GENETICS !$#gene SGD:SES1; MIPS:YDR023w !'##cross-references MIPS:YDR023w; SGD:S0002430 !$#map_position 4R CLASSIFICATION #superfamily serine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; homodimer; ligase; protein !1biosynthesis SUMMARY #length 462 #molecular-weight 53309 #checksum 182 SEQUENCE /// ENTRY YSEC #type complete TITLE serine-tRNA ligase (EC 6.1.1.11) - Escherichia coli (strain K-12) ALTERNATE_NAMES seryl-tRNA synthetase ORGANISM #formal_name Escherichia coli DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 03-Jun-2002 ACCESSIONS A26400; S03784; D64828 REFERENCE A26400 !$#authors Hartlein, M.; Madern, D.; Leberman, R. !$#journal Nucleic Acids Res. (1987) 15:1005-1017 !$#title Cloning and characterization of the gene for Escherichia !1coli seryl-tRNA synthetase. !$#cross-references MUID:87146412; PMID:3029694 !$#accession A26400 !'##molecule_type DNA !'##residues 1-430 ##label HAR !'##cross-references GB:X05017; NID:g42949; PIDN:CAA28673.1; PID:g42950 !'##experimental_source strain K-12/1100 REFERENCE S03784 !$#authors Bilous, P.T.; Cole, S.T.; Anderson, W.F.; Weiner, J.H. !$#journal Mol. Microbiol. (1988) 2:785-795 !$#title Nucleotide sequence of the dmsABC operon encoding the !1anaerobic dimethylsulphoxide reductase of Escherichia coli. !$#cross-references MUID:89096500; PMID:3062312 !$#accession S03784 !'##molecule_type DNA !'##residues 251-430 ##label BIL !'##cross-references GB:J03412; NID:g145754; PIDN:AAA83842.1; !1PID:g1128947 !'##experimental_source strain C600 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64828 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-430 ##label BLAT !'##cross-references GB:AE000191; GB:U00096; NID:g1787115; !1PIDN:AAC73979.1; PID:g1787120; UWGP:b0893 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene serS !$#map_position 20 min FUNCTION !$#description charges tRNA(Ser) with serine !$#pathway protein biosynthesis CLASSIFICATION #superfamily serine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; homodimer; ligase; protein !1biosynthesis SUMMARY #length 430 #molecular-weight 48414 #checksum 3712 SEQUENCE /// ENTRY SYECGA #type complete TITLE glycine-tRNA ligase (EC 6.1.1.14) alpha chain - Escherichia coli (strain K-12) ALTERNATE_NAMES glycyl-tRNA synthetase alpha chain ORGANISM #formal_name Escherichia coli DATE 17-May-1985 #sequence_revision 05-Dec-1997 #text_change 03-Jun-2002 ACCESSIONS B65155; A01188; S47781; I41241 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65155 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-303 ##label BLAT !'##cross-references GB:AE000433; GB:U00096; NID:g1789977; !1PIDN:AAC76584.1; PID:g1789983; UWGP:b3560 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A92392 !$#authors Webster, T.A.; Gibson, B.W.; Keng, T.; Biemann, K.; !1Schimmel, P. !$#journal J. Biol. Chem. (1983) 258:10637-10641 !$#title Primary structures of both subunits of Escherichia coli !1glycyl-tRNA synthetse. !$#cross-references MUID:83290996; PMID:6309809 !$#accession A01188 !'##molecule_type DNA !'##residues 1-47,'A',49-64,'A',66-303 ##label WEB !'##cross-references GB:J01622; NID:g146221; PIDN:AAA23914.1; !1PID:g146222 REFERENCE S47666 !$#authors Plunkett, G. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S47781 !'##molecule_type DNA !'##residues 1-303 ##label PLU !'##cross-references EMBL:U00039; NID:g466582; PIDN:AAB18537.1; !1PID:g466698 REFERENCE I41241 !$#authors Keng, T.; Webster, T.A.; Sauer, R.T.; Schimmel, P.R. !$#journal J. Biol. Chem. (1982) 257:12503-12508 !$#title Gene for Escherichia coli glycyl-tRNA synthetase has tandem !1subunit coding regions in the same reading frame. !$#cross-references MUID:83030764; PMID:6290471 !$#accession I41241 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 268-303 ##label RES !'##cross-references GB:J01623; NID:g146224; PIDN:AAA23916.1; !1PID:g146225 COMMENT The active enzyme is composed of two alpha and two beta !1chains. GENETICS !$#gene glyQ; glyS(a) !$#map_position 80 min CLASSIFICATION #superfamily glycine-tRNA ligase alpha chain KEYWORDS aminoacyl-tRNA synthetase; ligase; protein biosynthesis SUMMARY #length 303 #molecular-weight 34774 #checksum 2489 SEQUENCE /// ENTRY G64227 #type complete TITLE glycine-tRNA ligase (EC 6.1.1.14) - Mycoplasma genitalium ALTERNATE_NAMES glycyl-tRNA synthetase ORGANISM #formal_name Mycoplasma genitalium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS G64227 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession G64227 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-446 ##label TIGR !'##cross-references GB:U39703; GB:L43967; NID:g1045933; PID:g1045942; !1TIGR:MG251 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily Mycoplasma genitalium glycine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ligase; protein biosynthesis SUMMARY #length 446 #molecular-weight 52295 #checksum 795 SEQUENCE /// ENTRY S73808 #type complete TITLE glycine-tRNA ligase (EC 6.1.1.14) grs1 - Mycoplasma pneumoniae (strain ATCC 29342) ALTERNATE_NAMES glycyl-tRNA synthetase grs1; hypothetical protein H91_orf449 ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S73808 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73808 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-449 ##label HIM !'##cross-references EMBL:AE000047; GB:U00089; NID:g1674162; !1PIDN:AAB96130.1; PID:g1674173 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#gene grs1 !$#genetic_code SGC3 CLASSIFICATION #superfamily Mycoplasma genitalium glycine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ligase; protein biosynthesis SUMMARY #length 449 #molecular-weight 52303 #checksum 7157 SEQUENCE /// ENTRY C71296 #type complete TITLE glycine-tRNA ligase (EC 6.1.1.14) (glyS) - syphilis spirochete ORGANISM #formal_name Treponema pallidum subsp. pallidum #common_name syphilis spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS C71296 REFERENCE A71250 !$#authors Fraser, C.M.; Norris, S.J.; Weinstock, G.M.; White, O.; !1Sutton, G.G.; Dodson, R.; Gwinn, M.; Hickey, E.K.; Clayton, !1R.; Ketchum, K.A.; Sodergren, E.; Hardham, J.M.; McLeod, !1M.P.; Salzberg, S.; Peterson, J.; Khalak, H.; Richardson, !1D.; Howell, J.K.; Chidambaram, M.; Utterback, T.; McDonald, !1L.; Artiach, P.; Bowman, C.; Cotton, M.D.; Fujii, C.; !1Garland, S.; Hatch, B.; Horst, K.; Roberts, K.; Watthey, L.; !1Weidman, J.; Smith, H.O.; Venter, J.C. !$#journal Science (1998) 281:375-388 !$#title Complete genome sequence of Treponema pallidum, the syphilis !1spirochete. !$#cross-references MUID:98332770; PMID:9665876 !$#accession C71296 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-462 ##label COL !'##cross-references GB:AE001241; GB:AE000520; NID:g3322969; !1PIDN:AAC26570.1; PID:g3322974 !'##experimental_source strain Nichols GENETICS !$#gene TP0672 CLASSIFICATION #superfamily Mycoplasma genitalium glycine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ligase; protein biosynthesis SUMMARY #length 462 #molecular-weight 52677 #checksum 5011 SEQUENCE /// ENTRY B70146 #type complete TITLE glycine-tRNA ligase (EC 6.1.1.14) glyS - Lyme disease spirochete ALTERNATE_NAMES glycyl-tRNA synthetase ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS B70146 REFERENCE A70100 !$#authors Fraser, C.M.; Casjens, S.; Huang, W.M.; Sutton, G.G.; !1Clayton, R.; Lathigra, R.; White, O.; Ketchum, K.A.; Dodson, !1R.; Hickey, E.K.; Gwinn, M.; Dougherty, B.; Tomb, J.F.; !1Fleischmann, R.D.; Richardson, D.; Peterson, J.; Kerlavage, !1A.R.; Quackenbush, J.; Salzberg, S.; Hanson, M.; Vugt, R.V.; !1Palmer, N.; Adams, M.D.; Gocayne, J.; Weidman, J.; !1Utterback, T.; Watthey, L.; McDonald, L.; Artiach, P.; !1Bowman, C.; Garland, S.; Fujii, C.; Cotton, M.D.; Horst, K.; !1Roberts, K.; Hatch, B.; Smith, H.O.; Venter, J.C. !$#journal Nature (1997) 390:580-586 !$#title Genomic sequence of a Lyme disease spirochaete, Borrelia !1burgdorferi. !$#cross-references MUID:98065943; PMID:9403685 !$#accession B70146 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-445 ##label KLE !'##cross-references GB:AE001142; GB:AE000783; NID:g2688264; !1PIDN:AAC66743.1; PID:g2688266; TIGR:BB0371 !'##experimental_source strain B31 CLASSIFICATION #superfamily Mycoplasma genitalium glycine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ligase; protein biosynthesis SUMMARY #length 445 #molecular-weight 52209 #checksum 3364 SEQUENCE /// ENTRY D70585 #type complete TITLE probable glyS protein - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS D70585 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession D70585 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-463 ##label COL !'##cross-references GB:Z95208; GB:AL123456; NID:g3261747; !1PIDN:CAB08466.1; PID:g2078043 !'##experimental_source strain H37Rv GENETICS !$#gene glyS CLASSIFICATION #superfamily Mycoplasma genitalium glycine-tRNA ligase SUMMARY #length 463 #molecular-weight 52937 #checksum 9033 SEQUENCE /// ENTRY S58522 #type complete TITLE glycine-tRNA ligase (EC 6.1.1.14) - Thermus aquaticus ALTERNATE_NAMES glycyl-tRNA synthetase ORGANISM #formal_name Thermus aquaticus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S58522 REFERENCE S58522 !$#authors Logan, D.T.; Mazauric, M.H.; Kern, D.; Moras, D. !$#journal EMBO J. (1995) 14:4156-4167 !$#title Crystal structure of glycyl-tRNA synthetase from Thermus !1thermophilus. !$#cross-references MUID:96016187; PMID:7556056 !$#accession S58522 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-506 ##label LOG !'##experimental_source strain HB8 !'##note the source is designated as Thermus thermophilus CLASSIFICATION #superfamily Mycoplasma genitalium glycine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; ligase; protein biosynthesis SUMMARY #length 506 #molecular-weight 58224 #checksum 8438 SEQUENCE /// ENTRY A46636 #type complete TITLE glycine-tRNA ligase (EC 6.1.1.14) - silkworm ALTERNATE_NAMES glycyl-tRNA synthetase ORGANISM #formal_name Bombyx mori #common_name silkworm DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS A46636 REFERENCE A46636 !$#authors Nada, S.; Chang, P.K.; Dignam, J.D. !$#journal J. Biol. Chem. (1993) 268:7660-7667 !$#title Primary structure of the gene for glycyl-tRNA synthetase !1from Bombyx mori. !$#cross-references MUID:93216727; PMID:8463296 !$#accession A46636 !'##status preliminary !'##molecule_type DNA; protein !'##residues 1-687 ##label NAD !'##note sequence inconsistent with the nucleotide translation !'##note sequence extracted from NCBI backbone (NCBIN:128985, !1NCBIP:128987) CLASSIFICATION #superfamily human glycine-tRNA ligase; amino acid-tRNA !1ligase repeat homology KEYWORDS aminoacyl-tRNA synthetase; ligase; protein biosynthesis FEATURE !$20-65 #domain amino acid-tRNA ligase repeat homology #label !8ATL SUMMARY #length 687 #molecular-weight 77668 #checksum 1674 SEQUENCE /// ENTRY SYECGB #type complete TITLE glycine-tRNA ligase (EC 6.1.1.14) beta chain - Escherichia coli (strain K-12) ALTERNATE_NAMES glycyl-tRNA synthetase beta chain ORGANISM #formal_name Escherichia coli DATE 28-Aug-1985 #sequence_revision 17-May-1996 #text_change 03-Jun-2002 ACCESSIONS S47780; I41242; A01189; A65155 REFERENCE S47666 !$#authors Plunkett, G. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S47780 !'##molecule_type DNA !'##residues 1-689 ##label PLU !'##cross-references EMBL:U00039; NID:g466582; PIDN:AAB18536.1; !1PID:g466697 REFERENCE I41241 !$#authors Keng, T.; Webster, T.A.; Sauer, R.T.; Schimmel, P.R. !$#journal J. Biol. Chem. (1982) 257:12503-12508 !$#title Gene for Escherichia coli glycyl-tRNA synthetase has tandem !1subunit coding regions in the same reading frame. !$#cross-references MUID:83030764; PMID:6290471 !$#accession I41242 !'##status preliminary !'##molecule_type DNA !'##residues 1-20 ##label RES !'##cross-references GB:J01623; NID:g146224; PIDN:AAA23917.1; !1PID:g146226 REFERENCE A92392 !$#authors Webster, T.A.; Gibson, B.W.; Keng, T.; Biemann, K.; !1Schimmel, P. !$#journal J. Biol. Chem. (1983) 258:10637-10641 !$#title Primary structures of both subunits of Escherichia coli !1glycyl-tRNA synthetse. !$#cross-references MUID:83290996; PMID:6309809 !$#accession A01189 !'##molecule_type DNA !'##residues 1,'Q',3-90,'P',92-153,'AAA',157-210,'DG',213-341,'D', !1343-360,'V',362-689 ##label WEB !'##cross-references GB:J01622; NID:g146221; PIDN:AAA23915.1; !1PID:g146223 !'##note the authors translated the codons GAC and GTC for residues 342 !1and 361 as Leu REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65155 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-689 ##label BLAT !'##cross-references GB:AE000433; GB:U00096; NID:g1789977; !1PIDN:AAC76583.1; PID:g1789982; UWGP:b3559 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene glyS; glyS(b) !$#map_position 80 min COMPLEX tetramer of two alpha and two beta chains CLASSIFICATION #superfamily glycine-tRNA ligase beta chain KEYWORDS aminoacyl-tRNA synthetase; ligase; protein biosynthesis SUMMARY #length 689 #molecular-weight 76812 #checksum 2533 SEQUENCE /// ENTRY YPEC #type complete TITLE proline-tRNA ligase (EC 6.1.1.15) - Escherichia coli (strain K-12) ALTERNATE_NAMES global RNA synthesis factor; prolyl-tRNA synthetase ORGANISM #formal_name Escherichia coli DATE 30-Sep-1992 #sequence_revision 31-Oct-1997 #text_change 03-Jun-2002 ACCESSIONS B64744; JV0110; JV0061 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64744 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-572 ##label BLAT !'##cross-references GB:AE000128; GB:U00096; NID:g1786383; !1PIDN:AAC73305.1; PID:g1786392; UWGP:b0194 !'##experimental_source strain K-12, substrain MG1655 REFERENCE JV0110 !$#authors Eriani, G.; Delarue, M.; Poch, O.; Gangloff, J.; Moras, D. !$#journal Nature (1990) 347:203-206 !$#title Partition of tRNA synthetases into two classes based on !1mutually exclusive sets of sequence motifs. !$#cross-references MUID:90370122; PMID:2203971 !$#accession JV0110 !'##molecule_type DNA !'##residues 1-25,'IV',28-204,'Q',206-572 ##label ERI !'##cross-references GB:M97858; NID:g147361; PIDN:AAA24420.1; !1PID:g147362 !'##note the sequence from Fig. 2 is inconsistent with that from Fig. 1 !1in having 205-Ser, 213-Cys, 238-Leu, 405-Tyr and in lacking !1248-Ala REFERENCE JV0061 !$#authors Zhou, Z.; Syvanen, M. !$#journal J. Bacteriol. (1990) 172:281-286 !$#title Identification and sequence of the drpA gene from !1Escherichia coli. !$#cross-references MUID:90094229; PMID:1688424 !$#accession JV0061 !'##molecule_type DNA !'##residues 1-126,'HV',129-204,'RPLTNSRCWRR',217-515,'RA' ##label ZHO !'##cross-references GB:M32357; NID:g145802; PIDN:AAA23710.1; !1PID:g145803 !'##note the authors identified this protein as global RNA synthesis !1factor (encoded by drpA gene), which is involved in general !1RNA synthesis GENETICS !$#gene proS; drpA !$#map_position 5 min CLASSIFICATION #superfamily proline-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; homodimer; ligase; protein !1biosynthesis SUMMARY #length 572 #molecular-weight 63692 #checksum 34 SEQUENCE /// ENTRY YYEC #type complete TITLE cysteine-tRNA ligase (EC 6.1.1.16) - Escherichia coli (strain K-12) ALTERNATE_NAMES cysteinyl-tRNA synthetase ORGANISM #formal_name Escherichia coli DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 03-Jun-2002 ACCESSIONS A37868; S17186; JN0109; S20221; S14075; S20219; E64784 REFERENCE A37868 !$#authors Hou, Y.M.; Shiba, K.; Mottes, C.; Schimmel, P. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:976-980 !$#title Sequence determination and modeling of structural motifs for !1the smallest monomeric aminoacyl-tRNA synthetase. !$#cross-references MUID:91126117; PMID:1992490 !$#accession A37868 !'##molecule_type DNA !'##residues 1-461 ##label HOU !'##cross-references GB:M59381; NID:g145691; PIDN:AAA23658.1; !1PID:g145692 REFERENCE S17186 !$#authors Avalos, J.; Corrochano, L.M.; Brenner, S. !$#journal FEBS Lett. (1991) 286:176-180 !$#title Cysteinyl-tRNA synthetase is a direct descendant of the !1first aminoacyl-tRNA synthetase. !$#cross-references MUID:91323511; PMID:1864365 !$#accession S17186 !'##molecule_type DNA !'##residues 1-461 ##label AVA !'##cross-references EMBL:X59293; NID:g41204; PIDN:CAA41983.1; !1PID:g41206 REFERENCE JN0109 !$#authors Eriani, G.; Dirheimer, G.; Gangloff, J. !$#journal Nucleic Acids Res. (1991) 19:265-269 !$#title Cysteinyl-tRNA synthetase: determination of the last E. coli !1aminoacyl-tRNA synthetase primary structure. !$#cross-references MUID:91195046; PMID:2014166 !$#accession JN0109 !'##molecule_type DNA !'##residues 1-336,'R',338-461 ##label ERI1 !'##cross-references EMBL:X56234 !$#accession S20221 !'##molecule_type protein !'##residues 1-10 ##label ERI2 REFERENCE S14075 !$#authors Eriani, G. !$#submission submitted to the EMBL Data Library, December 1990 !$#accession S14075 !'##molecule_type DNA !'##residues 1-315,'V',317-336,'R',338-461 ##label ERIW !'##cross-references EMBL:X56234 !'##note this sequence has been revised in reference S20219 REFERENCE S20219 !$#authors Eriani, G. !$#submission submitted to the EMBL Data Library, January 1991 !$#accession S20219 !'##molecule_type DNA !'##residues 1-315,'V',317-461 ##label ERI !'##cross-references EMBL:X56234; NID:g41202; PIDN:CAA39691.1; !1PID:g41203 !'##note this is a revision to the sequence from reference S14075 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64784 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-461 ##label BLAT !'##cross-references GB:AE000158; GB:U00096; NID:g1786728; !1PIDN:AAC73628.1; PID:g1786737; UWGP:b0526 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene cysS !$#map_position 12 min CLASSIFICATION #superfamily cysteine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; ligase; protein biosynthesis SUMMARY #length 461 #molecular-weight 52202 #checksum 5884 SEQUENCE /// ENTRY F64630 #type complete TITLE cysteine-tRNA ligase (EC 6.1.1.16) - Helicobacter pylori (strain 26695) ALTERNATE_NAMES cysteinyl-tRNA synthetase ORGANISM #formal_name Helicobacter pylori DATE 09-Aug-1997 #sequence_revision 09-Aug-1997 #text_change 03-Jun-2002 ACCESSIONS F64630; C53739 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession F64630 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-465 ##label TOM !'##cross-references GB:AE000511; NID:g2314019; PIDN:AAD07934.1; !1PID:g2314022; TIGR:HP0886 !'##experimental_source strain 26695 REFERENCE A53739 !$#authors Cover, T.L.; Tummuru, M.K.R.; Cao, P.; Thompson, S.A.; !1Blaser, M.J. !$#journal J. Biol. Chem. (1994) 269:10566-10573 !$#title Divergence of genetic sequences for the vacuolating !1cytotoxin among Helicobacter pylori strains. !$#cross-references MUID:94193753; PMID:8144644 !$#accession C53739 !'##molecule_type DNA !'##residues 278-279,'I',281-331,'N',333-391,'V',393-431,'Q',433-439, !1'H',441-465 ##label COV !'##cross-references GB:U05676; NID:g471727; PIDN:AAA17656.1; !1PID:g471728 !'##experimental_source strain ATCC 49503 CLASSIFICATION #superfamily cysteine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; ligase; protein biosynthesis SUMMARY #length 465 #molecular-weight 53131 #checksum 4766 SEQUENCE /// ENTRY I64227 #type complete TITLE cysteine-tRNA ligase (EC 6.1.1.16) - Mycoplasma genitalium ALTERNATE_NAMES cysteinyl-tRNA synthetase ORGANISM #formal_name Mycoplasma genitalium DATE 17-Nov-1995 #sequence_revision 17-Nov-1995 #text_change 03-Jun-2002 ACCESSIONS I64227 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession I64227 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-428 ##label TIGR !'##cross-references GB:U39703; GB:L43967; NID:g1045933; PID:g1045944; !1TIGR:MG253 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily cysteine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ligase; protein biosynthesis SUMMARY #length 428 #molecular-weight 49905 #checksum 9436 SEQUENCE /// ENTRY S73806 #type complete TITLE cysteine-tRNA ligase (EC 6.1.1.16) cysS - Mycoplasma pneumoniae (strain ATCC 29342) ALTERNATE_NAMES cysteinyl-tRNA synthetase cysS; hypothetical protein H91_orf473 ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 27-Feb-1997 #sequence_revision 25-Apr-1997 #text_change 03-Jun-2002 ACCESSIONS S73806 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73806 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-437 ##label HIM !'##cross-references EMBL:AE000047; GB:U00089; NID:g1674162; !1PIDN:AAB96128.1; PID:g1674171 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#gene cysS !$#genetic_code SGC3 CLASSIFICATION #superfamily cysteine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ligase; protein biosynthesis SUMMARY #length 437 #molecular-weight 50665 #checksum 8624 SEQUENCE /// ENTRY C53402 #type complete TITLE cysteine-tRNA ligase (EC 6.1.1.16) cysS - Bacillus subtilis ALTERNATE_NAMES cysteinyl-tRNA synthetase cysS ORGANISM #formal_name Bacillus subtilis DATE 27-Jun-1994 #sequence_revision 27-Jun-1994 #text_change 03-Jun-2002 ACCESSIONS C53402; S44447; S66123; B69612 REFERENCE A53402 !$#authors Gagnon, Y.; Breton, R.; Putzer, H.; Pelchat, M.; !1Grunberg-Manago, M.; Lapointe, J. !$#journal J. Biol. Chem. (1994) 269:7473-7482 !$#title Clustering and co-transcription of the Bacillus subtilis !1genes encoding the aminoacyl-tRNA synthetases specific for !1glutamate and for cysteine and the first enzyme for cysteine !1biosynthesis. !$#cross-references MUID:94171772; PMID:7510287 !$#accession C53402 !'##molecule_type DNA !'##residues 1-466 ##label GAG !'##cross-references GB:L14580; NID:g289278; PIDN:AAA21798.1; !1PID:g289284 REFERENCE S44447 !$#authors Seror, S.J.; Casaregola, S.; Vannier, F.; Zouari, N.; Dahl, !1M.; Boye, E. !$#journal EMBO J. (1994) 13:2472-2480 !$#title A mutant cysteinyl-tRNA synthetase affecting timing of !1chromosomal replication initiation in B.subtilis and !1conferring resistance to a protein kinase C inhibitor. !$#cross-references MUID:94252334; PMID:8194536 !$#accession S44447 !'##molecule_type DNA !'##residues 1-466 ##label SER !'##cross-references GB:X73989; NID:g499302; PIDN:CAA52167.1; !1PID:g499303 REFERENCE S65967 !$#authors Ogasawara, N.; Nakai, S.; Yoshikawa, H. !$#journal DNA Res. (1994) 1:1-14 !$#title Systematic sequencing of the 180 kilobase region of the !1Bacillus subtilis chromosome containing the replication !1origin. !$#cross-references MUID:96051385; PMID:7584024 !$#accession S66123 !'##molecule_type DNA !'##residues 1-466 ##label OGA !'##cross-references EMBL:D26185; NID:g467326; PIDN:BAA05328.1; !1PID:g467482 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69612 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-466 ##label KUN !'##cross-references GB:Z99104; GB:AL009126; NID:g2632267; !1PIDN:CAB11870.1; PID:g2632361 !'##experimental_source strain 168 GENETICS !$#gene cysS CLASSIFICATION #superfamily cysteine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ligase; protein biosynthesis SUMMARY #length 466 #molecular-weight 53907 #checksum 5354 SEQUENCE /// ENTRY F53402 #type fragment TITLE cysteine-tRNA ligase (EC 6.1.1.16) - Bacillus stearothermophilus (fragment) ORGANISM #formal_name Bacillus stearothermophilus DATE 27-Jun-1994 #sequence_revision 27-Jun-1994 #text_change 03-Jun-2002 ACCESSIONS F53402 REFERENCE A53402 !$#authors Gagnon, Y.; Breton, R.; Putzer, H.; Pelchat, M.; !1Grunberg-Manago, M.; Lapointe, J. !$#journal J. Biol. Chem. (1994) 269:7473-7482 !$#title Clustering and co-transcription of the Bacillus subtilis !1genes encoding the aminoacyl-tRNA synthetases specific for !1glutamate and for cysteine and the first enzyme for cysteine !1biosynthesis. !$#cross-references MUID:94171772; PMID:7510287 !$#accession F53402 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-221 ##label GAG CLASSIFICATION #superfamily cysteine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ligase; protein biosynthesis SUMMARY #length 221 #checksum 9248 SEQUENCE /// ENTRY F70174 #type complete TITLE cysteine-tRNA ligase (EC 6.1.1.16) cysS - Lyme disease spirochete ALTERNATE_NAMES cysteinyl-tRNA synthetase ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 13-Feb-1998 #sequence_revision 13-Feb-1998 #text_change 03-Jun-2002 ACCESSIONS F70174 REFERENCE A70100 !$#authors Fraser, C.M.; Casjens, S.; Huang, W.M.; Sutton, G.G.; !1Clayton, R.; Lathigra, R.; White, O.; Ketchum, K.A.; Dodson, !1R.; Hickey, E.K.; Gwinn, M.; Dougherty, B.; Tomb, J.F.; !1Fleischmann, R.D.; Richardson, D.; Peterson, J.; Kerlavage, !1A.R.; Quackenbush, J.; Salzberg, S.; Hanson, M.; Vugt, R.V.; !1Palmer, N.; Adams, M.D.; Gocayne, J.; Weidman, J.; !1Utterback, T.; Watthey, L.; McDonald, L.; Artiach, P.; !1Bowman, C.; Garland, S.; Fujii, C.; Cotton, M.D.; Horst, K.; !1Roberts, K.; Hatch, B.; Smith, H.O.; Venter, J.C. !$#journal Nature (1997) 390:580-586 !$#title Genomic sequence of a Lyme disease spirochaete, Borrelia !1burgdorferi. !$#cross-references MUID:98065943; PMID:9403685 !$#accession F70174 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-480 ##label KLE !'##cross-references GB:AE001161; GB:AE000783; NID:g2688515; !1PIDN:AAC66952.1; PID:g2688519; TIGR:BB0599 !'##experimental_source strain B31 CLASSIFICATION #superfamily cysteine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ligase; protein biosynthesis SUMMARY #length 480 #molecular-weight 56022 #checksum 1185 SEQUENCE /// ENTRY S76165 #type complete TITLE cysteine-tRNA ligase (EC 6.1.1.16) - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 25-Apr-1997 #sequence_revision 25-Apr-1997 #text_change 03-Jun-2002 ACCESSIONS S76165 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76165 !'##molecule_type DNA !'##residues 1-483 ##label KAN !'##cross-references EMBL:D90914; GB:AB001339; NID:g1653477; !1PIDN:BAA18424.1; PID:g1653511 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily cysteine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ligase; protein biosynthesis SUMMARY #length 483 #molecular-weight 53967 #checksum 502 SEQUENCE /// ENTRY C69301 #type complete TITLE cysteine-tRNA ligase (EC 6.1.1.16) - Archaeoglobus fulgidus ALTERNATE_NAMES cysteinyl-tRNA synthetase (cysS) ORGANISM #formal_name Archaeoglobus fulgidus DATE 05-Dec-1997 #sequence_revision 05-Dec-1997 #text_change 03-Jun-2002 ACCESSIONS C69301 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession C69301 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-467 ##label KLE !'##cross-references GB:AE001076; GB:AE000782; NID:g2689399; !1PIDN:AAB90823.1; PID:g2650218; TIGR:AF0411 CLASSIFICATION #superfamily cysteine-tRNA ligase KEYWORDS ligase SUMMARY #length 467 #molecular-weight 54790 #checksum 4677 SEQUENCE /// ENTRY SYECET #type complete TITLE glutamate-tRNA ligase (EC 6.1.1.17) - Escherichia coli (strain K-12) ALTERNATE_NAMES glutamyl-tRNA synthetase ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 03-Jun-2002 ACCESSIONS A25956; I41069; C65014 REFERENCE A25956 !$#authors Breton, R.; Sanfacon, H.; Papayannopoulos, I.; Biemann, K.; !1Lapointe, J. !$#journal J. Biol. Chem. (1986) 261:10610-10617 !$#title Glutamyl-tRNA synthetase of Escherichia coli. Isolation and !1primary structure of the gltX gene and homology with other !1aminoacyl-tRNA synthetases. !$#cross-references MUID:86278132; PMID:3015933 !$#accession A25956 !'##molecule_type DNA !'##residues 1-471 ##label BRE !'##cross-references GB:M13687; NID:g148254; PIDN:AAA65715.1; !1PID:g148256 REFERENCE I41069 !$#authors Brun, Y.V.; Sanfacon, H.; Breton, R.; Lapointe, J. !$#journal J. Mol. Biol. (1990) 214:845-864 !$#title Closely spaced and divergent promoters for an aminoacyl-tRNA !1synthetase gene and a tRNA operon in Escherichia coli. !1Transcriptional and post-transcriptional regulation of gltX, !1valU and alaW. !$#cross-references MUID:90355200; PMID:2201777 !$#accession I41069 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-57 ##label RES !'##cross-references EMBL:X55737; NID:g288085; PIDN:CAA39269.1; !1PID:g288086 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65014 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-471 ##label BLAT !'##cross-references GB:AE000328; GB:U00096; NID:g2367135; !1PIDN:AAC75457.1; PID:g1788743; UWGP:b2400 !'##experimental_source strain K-12, substrain MG1655 COMMENT The active enzyme, a monomer, is the smallest aminoacyl-tRNA !1synthetase of E. coli; it does not bind glutamate in the !1absence of cognate tRNA, which is therefore required for !1activation of the amino acid substrate. GENETICS !$#gene gltX !$#map_position 52 min CLASSIFICATION #superfamily glutamate-tRNA ligase; glutamine-tRNA ligase !1homology KEYWORDS aminoacyl-tRNA synthetase; ATP; ligase; protein biosynthesis FEATURE !$3-276 #domain glutamine-tRNA ligase homology #label EGL\ !$240 #binding_site ATP (Lys) #status predicted SUMMARY #length 471 #molecular-weight 53815 #checksum 9917 SEQUENCE /// ENTRY SYRZET #type complete TITLE glutamate-tRNA ligase (EC 6.1.1.17) - Rhizobium meliloti ALTERNATE_NAMES glutamyl-tRNA synthetase ORGANISM #formal_name Rhizobium meliloti DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 03-Jun-2002 ACCESSIONS A32888 REFERENCE A32888 !$#authors Laberge, S.; Gagnon, Y.; Bordeleau, L.M.; Lapointe, J. !$#journal J. Bacteriol. (1989) 171:3926-3932 !$#title Cloning and sequencing of the gltX gene, encoding the !1glutamyl-tRNA synthetase of Rhizobium meliloti A2. !$#cross-references MUID:89291743; PMID:2661539 !$#accession A32888 !'##molecule_type DNA !'##residues 1-484 ##label LAB !'##cross-references GB:M27221; NID:g341649; PIDN:AAC35209.1; !1PID:g717082 !'##experimental_source strain A2 CLASSIFICATION #superfamily glutamate-tRNA ligase; glutamine-tRNA ligase !1homology KEYWORDS aminoacyl-tRNA synthetase; ATP; ligase; protein biosynthesis FEATURE !$6-320 #domain glutamine-tRNA ligase homology #label EGL\ !$256 #binding_site ATP (Lys) #status predicted SUMMARY #length 484 #molecular-weight 54228 #checksum 7829 SEQUENCE /// ENTRY SYBSET #type complete TITLE glutamate-tRNA ligase (EC 6.1.1.17) gltX - Bacillus subtilis ALTERNATE_NAMES glutamyl-tRNA synthetase gltX ORGANISM #formal_name Bacillus subtilis DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 03-Jun-2002 ACCESSIONS A36090; S66121; E69635 REFERENCE A36090 !$#authors Breton, R.; Watson, D.; Yaguchi, M.; Lapointe, J. !$#journal J. Biol. Chem. (1990) 265:18248-18255 !$#title Glutamyl-tRNA synthetases of Bacillus subtilis 168T and of !1Bacillus stearothermophilus. Cloning and sequencing of the !1gltX genes and comparison with other aminoacyl-tRNA !1synthetases. !$#cross-references MUID:91009314; PMID:2120226 !$#accession A36090 !'##molecule_type DNA !'##residues 1-483 ##label BRE !'##cross-references GB:M55073; NID:g143005; PIDN:AAA22495.1; !1PID:g143006; GB:J05647 !'##experimental_source strain 168T !'##note the authors translated the codon CCT for residue 194 as Phe REFERENCE S65967 !$#authors Ogasawara, N.; Nakai, S.; Yoshikawa, H. !$#journal DNA Res. (1994) 1:1-14 !$#title Systematic sequencing of the 180 kilobase region of the !1Bacillus subtilis chromosome containing the replication !1origin. !$#cross-references MUID:96051385; PMID:7584024 !$#accession S66121 !'##status preliminary !'##molecule_type DNA !'##residues 1-483 ##label OGA !'##cross-references EMBL:D26185; NID:g467326; PIDN:BAA05326.1; !1PID:g467480 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69635 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-483 ##label KUN !'##cross-references GB:Z99104; GB:AL009126; NID:g2632267; !1PIDN:CAB11868.1; PID:g2632359 !'##experimental_source strain 168 GENETICS !$#gene gltX CLASSIFICATION #superfamily glutamate-tRNA ligase; glutamine-tRNA ligase !1homology KEYWORDS aminoacyl-tRNA synthetase; ATP; ligase; protein biosynthesis FEATURE !$5-293 #domain glutamine-tRNA ligase homology #label EGL\ !$255 #binding_site ATP (Lys) #status predicted SUMMARY #length 483 #molecular-weight 55722 #checksum 300 SEQUENCE /// ENTRY SYBSES #type complete TITLE glutamate-tRNA ligase (EC 6.1.1.17) - Bacillus stearothermophilus ALTERNATE_NAMES glutamyl-tRNA synthetase ORGANISM #formal_name Bacillus stearothermophilus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 03-Jun-2002 ACCESSIONS B36090 REFERENCE A36090 !$#authors Breton, R.; Watson, D.; Yaguchi, M.; Lapointe, J. !$#journal J. Biol. Chem. (1990) 265:18248-18255 !$#title Glutamyl-tRNA synthetases of Bacillus subtilis 168T and of !1Bacillus stearothermophilus. Cloning and sequencing of the !1gltX genes and comparison with other aminoacyl-tRNA !1synthetases. !$#cross-references MUID:91009314; PMID:2120226 !$#accession B36090 !'##molecule_type DNA !'##residues 1-489 ##label BRE !'##cross-references GB:M55072; NID:g143003; PIDN:AAA22494.1; !1PID:g143004; GB:J05647 !'##note the authors translated the codon AAC for residue 62 as Asp and !1CCG for residue 195 as Phe GENETICS !$#gene gltX CLASSIFICATION #superfamily glutamate-tRNA ligase; glutamine-tRNA ligase !1homology KEYWORDS aminoacyl-tRNA synthetase; ATP; ligase; protein biosynthesis FEATURE !$5-289 #domain glutamine-tRNA ligase homology #label EGL\ !$256 #binding_site ATP (Lys) #status predicted SUMMARY #length 489 #molecular-weight 56183 #checksum 959 SEQUENCE /// ENTRY SYHUQT #type complete TITLE multifunctional aminoacyl-tRNA synthetase - human ALTERNATE_NAMES gluproyl-tRNA synthase; glutaminyl-tRNA synthetase CONTAINS glutamate-tRNA ligase (EC 6.1.1.17); proline-tRNA ligase (EC 6.1.1.15) ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 19-Jul-2002 ACCESSIONS A38663; S03424; S00969; S38809 REFERENCE A38663 !$#authors Fett, R.; Knippers, R. !$#journal J. Biol. Chem. (1991) 266:1448-1455 !$#title The primary structure of human glutaminyl-tRNA synthetase. A !1highly conserved core, amino acid repeat regions, and !1homologies with translation elongation factors. !$#cross-references MUID:91107633; PMID:1988429 !$#accession A38663 !'##molecule_type mRNA !'##residues 1-1440 ##label FET !'##cross-references GB:X54326; NID:g31957; PIDN:CAA38224.1; PID:g31958 !'##note the cited Genbank accession number, X54327, is not in release !1101.0 REFERENCE S03424 !$#authors Knippers, R. !$#submission submitted to the EMBL Data Library, April 1988 !$#accession S03424 !'##molecule_type mRNA !'##residues 96-382,'L',384-497,'IGATSTLQ',506,'YT',509,'MQME',514, !1'SYL',518,'MQSLIWKT',527,'TTR',531,'PLRSLG',538,'QRLHML', !1545-555,'Q',557-887 ##label KNI !'##cross-references EMBL:X07466; NID:g31769; PIDN:CAA30354.1; !1PID:g825664 REFERENCE S00969 !$#authors Thoemmes, P.; Fett, R.; Schray, B.; Kunze, N.; Knippers, R. !$#journal Nucleic Acids Res. (1988) 16:5391-5406 !$#title The core region of human glutaminyl-tRNA synthetase !1homologies with the Escherichia coli and yeast enzymes. !$#cross-references MUID:88262551; PMID:3290852 !$#accession S00969 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 96-146,'I',148-191,'T',193-382,'L',384-416,'G',418-497, !1'IGATSTLQ',506,'YT',509,'MQME',514,'SYLIMQSLIWKT',527,'TTR', !1531,'PLRSLG',538,'QRLHML',545-555,'Q',557-566,'F',568-637, !1'N',639-662 ##label THO !'##cross-references EMBL:X07466 REFERENCE S18644 !$#authors Cerini, C.; Kerjan, P.; Astier, M.; Gratecos, D.; Mirande, !1M.; Semeriva, M. !$#journal EMBO J. (1991) 10:4267-4277 !$#title A component of the multisynthetase complex is a !1multifunctional aminoacyl-tRNA synthetase. !$#cross-references MUID:92097547; PMID:1756734 !$#contents annotation; demonstration of glutamyl- and prolyl- tRNA !1synthase activities in the Drosophila homolog REFERENCE S38809 !$#authors Kaiser, E.; Eberhard, D.; Knippers, R. !$#journal J. Mol. Evol. (1992) 34:45-53 !$#title Exons encoding the highly conserved part of human !1glutaminyl-tRNA synthetase. !$#cross-references MUID:92211721; PMID:1556743 !$#accession S38809 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type DNA !'##residues 96-382,'L',384-463 ##label KAI GENETICS !$#gene GDB:EPRS; QPRS; QARS !'##cross-references GDB:126609; OMIM:138295 !$#map_position 1q32-1q42 CLASSIFICATION #superfamily human multifunctional amino acid-tRNA ligase; !1amino acid-tRNA ligase repeat homology; glutamine-tRNA !1ligase homology KEYWORDS aminoacyl-tRNA synthetase; ATP; duplication; ligase; protein !1biosynthesis FEATURE !$125-485 #domain tRNA-charging #label GLN\ !$126-402 #domain glutamine-tRNA ligase homology #label EGL\ !$677-733 #region 57-residue repeat\ !$688-733 #domain amino acid-tRNA ligase repeat homology #label !8ATL1\ !$750-806 #region 57-residue repeat\ !$761-806 #domain amino acid-tRNA ligase repeat homology #label !8ATL2\ !$828-884 #region 57-residue repeat\ !$839-884 #domain amino acid-tRNA ligase repeat homology #label !8ATL3 SUMMARY #length 1440 #molecular-weight 163025 #checksum 8932 SEQUENCE /// ENTRY S18644 #type complete TITLE multifunctional amino acid-tRNA ligase (EC 6.1.1.-) - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES multifunctional aminoacyl-tRNA synthetase ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S18644 REFERENCE S18644 !$#authors Cerini, C.; Kerjan, P.; Astier, M.; Gratecos, D.; Mirande, !1M.; Semeriva, M. !$#journal EMBO J. (1991) 10:4267-4277 !$#title A component of the multisynthetase complex is a !1multifunctional aminoacyl-tRNA synthetase. !$#cross-references MUID:92097547; PMID:1756734 !$#accession S18644 !'##status preliminary !'##molecule_type mRNA !'##residues 1-1714 ##label CER !'##cross-references GB:M74104; NID:g157563; PIDN:AAA28594.1; !1PID:g157564 GENETICS !$#gene FlyBase:Aats-glupro !'##cross-references FlyBase:FBgn0005674 CLASSIFICATION #superfamily Drosophila multifunctional amino acid-tRNA !1ligase; amino acid-tRNA ligase repeat homology; !1glutamine-tRNA ligase homology KEYWORDS aminoacyl-tRNA synthetase; ATP; ligase; multifunctional !1enzyme; protein biosynthesis FEATURE !$204-480 #domain glutamine-tRNA ligase homology #label EGL\ !$755-800 #domain amino acid-tRNA ligase repeat homology #label !8ATL1\ !$827-872 #domain amino acid-tRNA ligase repeat homology #label !8ATL2\ !$901-946 #domain amino acid-tRNA ligase repeat homology #label !8ATL3\ !$980-1025 #domain amino acid-tRNA ligase repeat homology #label !8ATL4\ !$1055-1100 #domain amino acid-tRNA ligase repeat homology #label !8ATL5\ !$1129-1173 #domain amino acid-tRNA ligase repeat homology #label !8ATL6 SUMMARY #length 1714 #molecular-weight 189197 #checksum 490 SEQUENCE /// ENTRY S53934 #type complete TITLE glutamate-tRNA ligase (EC 6.1.1.17) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein G0583; protein HRB724; protein NRC145; protein YGL245w ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S53934; S59351; S60484; S61616; S64270; S64271 REFERENCE S53934 !$#authors Vandenbol, M.; Durand, P.; Portetelle, D.; Hilger, F. !$#submission submitted to the EMBL Data Library, April 1995 !$#description The sequence of a 11.1 kb DNA fragment between ADH4 and ADE5 !1on the left arm of chromosome VII, reveals the presence of !1eight open reading frames. !$#accession S53934 !'##molecule_type DNA !'##residues 1-724 ##label VAN !'##cross-references EMBL:Z49149; NID:g793865; PIDN:CAA89009.1; !1PID:g793866 REFERENCE S59351 !$#authors Frantz, J.D.; Gilbert, W. !$#submission submitted to the EMBL Data Library, July 1995 !$#description Isolation and sequence characterization of the gene encoding !1the yeast cytosolic glutamyl-tRNA synthetase. !$#accession S59351 !'##molecule_type DNA !'##residues 1-224,'D',226-488,'A',490-525,'S',527-561,'M',563-713, !1'VNLSTSMVQRNKHHISNVYTYLCYFSTSTF' ##label FRA !'##cross-references EMBL:U32265; NID:g1008482; PIDN:AAA78905.1; !1PID:g1008483 REFERENCE S60484 !$#authors Vandenbol, M.; Durand, P.; Portetelle, D.; Hilger, F. !$#journal Yeast (1995) 11:1519-1523 !$#title The sequence of an 11.1 kb DNA fragment between ADH4 and !1ADE5 on the left arm of chromosome VII reveals the presence !1of eight open reading frames. !$#cross-references MUID:96353434; PMID:8750240 !$#accession S60484 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 57-724 ##label VAW !'##cross-references EMBL:Z49149 REFERENCE S61598 !$#authors Coissac, E.; Maillier, E.; Robineau, S.; Netter, P. !$#submission submitted to the EMBL Data Library, December 1995 !$#accession S61616 !'##molecule_type DNA !'##residues 1-145 ##label COI !'##cross-references EMBL:X94357; NID:g1150575; PIDN:CAA64142.1; !1PID:g1150594 REFERENCE S64263 !$#authors Vandenbol, M.; Durand, P.; Portetelle, D.; Hilger, F. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64270 !'##molecule_type DNA !'##residues 1-724 ##label VAF !'##cross-references EMBL:Z72767; NID:g1945311; PIDN:CAA96964.1; !1PID:g1322915; GSPDB:GN00007; MIPS:YGL245w !'##experimental_source strain S288C REFERENCE S64271 !$#authors Coissac, E.; Maillier, E.; Netter, P. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64271 !'##molecule_type DNA !'##residues 1-145 ##label COW !'##cross-references EMBL:Z72767; GSPDB:GN00007; MIPS:YGL245w !'##experimental_source strain S288C GENETICS !$#gene MIPS:YGL245w !'##cross-references SGD:S0003214 !$#map_position 7L CLASSIFICATION #superfamily yeast glutamate-tRNA ligase; glutamine-tRNA !1ligase homology KEYWORDS aminoacyl-tRNA synthetase; ligase; protein biosynthesis FEATURE !$218-495 #domain glutamine-tRNA ligase homology #label EGL SUMMARY #length 724 #molecular-weight 82662 #checksum 199 SEQUENCE /// ENTRY SYECQT #type complete TITLE glutamine-tRNA ligase (EC 6.1.1.18) [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES glutaminyl-tRNA synthetase ORGANISM #formal_name Escherichia coli DATE 13-Jun-1983 #sequence_revision 05-Dec-1997 #text_change 03-Jun-2002 ACCESSIONS G64802; A92346; S03376; A01190; A31223 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64802 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-554 ##label BLAT !'##cross-references GB:AE000171; GB:U00096; NID:g1786888; !1PIDN:AAC73774.1; PID:g1786895; UWGP:b0680 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A92346 !$#authors Yamao, F.; Inokuchi, H.; Cheung, A.; Ozeki, H.; Soll, D. !$#journal J. Biol. Chem. (1982) 257:11639-11643 !$#title Escherichia coli glutaminyl-tRNA synthetase. !$#cross-references MUID:83007236; PMID:6288695 !$#accession A92346 !'##molecule_type DNA !'##residues 2-548,'GR',551 ##label YAM !'##cross-references GB:M10187; NID:g146174; PIDN:AAA23884.1; !1PID:g146175 REFERENCE S03376 !$#authors Uemura, H.; Conley, J.; Yamao, F.; Rogers, J.; Soell, D. !$#journal Protein Seq. Data Anal. (1988) 1:479-485 !$#title Escherichia coli glutaminyl-tRNA synthetase: a single amino !1acid replacement relaxes tRNA specificity. !$#cross-references MUID:89113343; PMID:2464170 !$#accession S03376 !'##molecule_type DNA !'##residues 2-554 ##label UEM REFERENCE A92347 !$#authors Hoben, P.; Royal, N.; Cheung, A.; Yamao, F.; Biemann, K.; !1Soll, D. !$#journal J. Biol. Chem. (1982) 257:11644-11650 !$#title Escherichia coli glutaminyl-tRNA synthetase. II. !1Characterization of the glnS gene product. !$#cross-references MUID:83007237; PMID:6749844 !$#contents annotation; confirmation of amino and carboxyl ends by amino !1acid analysis; strain JA221[pYY105] GENETICS !$#gene glnS !$#map_position 15 min FUNCTION !$#description EC 6.1.1.18 [validated, MUID:89113343] !$#pathway protein biosynthesis CLASSIFICATION #superfamily glutamine-tRNA ligase; glutamine-tRNA ligase !1homology KEYWORDS aminoacyl-tRNA synthetase; ATP; ligase; protein biosynthesis FEATURE !$28-310 #domain glutamine-tRNA ligase homology #label EGL SUMMARY #length 554 #molecular-weight 63477 #checksum 820 SEQUENCE /// ENTRY H64471 #type complete TITLE glutamate-tRNA ligase (EC 6.1.1.17) - Methanococcus jannaschii ALTERNATE_NAMES glutamyl-tRNA synthetase ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS H64471 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession H64471 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-553 ##label BUL !'##cross-references GB:U67577; GB:L77117; NID:g2826400; !1PIDN:AAB99384.1; PID:g1592022; TIGR:MJ1377 GENETICS !$#map_position REV1326696-1325035 !$#start_codon GTG CLASSIFICATION #superfamily glutamine-tRNA ligase; glutamine-tRNA ligase !1homology KEYWORDS aminoacyl-tRNA synthetase; ligase; protein biosynthesis FEATURE !$92-366 #domain glutamine-tRNA ligase homology #label EGL SUMMARY #length 553 #molecular-weight 64577 #checksum 558 SEQUENCE /// ENTRY I37422 #type complete TITLE glutamine-tRNA ligase (EC 6.1.1.18) - human ALTERNATE_NAMES glutaminyl-tRNA synthetase ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS I37422 REFERENCE I37422 !$#authors Lamour, V.; Quevillon, S.; Diriong, S.; N'Guyen, V.C.; !1Lipinski, M.; Mirande, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1994) 91:8670-8674 !$#title Evolution of the Glx-tRNA synthetase family: the glutaminyl !1enzyme as a case of horizontal gene transfer. !$#cross-references MUID:94359993; PMID:8078941 !$#accession I37422 !'##status preliminary !'##molecule_type mRNA !'##residues 1-775 ##label RES !'##cross-references EMBL:X76013; NID:g531595; PIDN:CAA53600.1; !1PID:g558586 GENETICS !$#gene GDB:QARS !'##cross-references GDB:386453 !$#map_position 3pter-3qter CLASSIFICATION #superfamily human glutamine-tRNA ligase; glutamine-tRNA !1ligase homology KEYWORDS aminoacyl-tRNA synthetase; ligase; protein biosynthesis FEATURE !$264-535 #domain glutamine-tRNA ligase homology #label EGL SUMMARY #length 775 #molecular-weight 87798 #checksum 1903 SEQUENCE /// ENTRY SYBYQT #type complete TITLE glutamine-tRNA ligase (EC 6.1.1.18) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES glutaminyl-tRNA synthetase; protein O3601; protein YOR168w ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1992 #sequence_revision 02-Aug-1996 #text_change 03-Jun-2002 ACCESSIONS S67056; A28494 REFERENCE S67032 !$#authors Bordonne, R.; Camasses, A.; Madania, A.; Martin, R.P.; Poch, !1O.; Tarassov, I.A.; Winsor, B. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67056 !'##molecule_type DNA !'##residues 1-809 ##label BOR !'##cross-references EMBL:Z75076; NID:g1420412; PIDN:CAA99374.1; !1PID:g1420413; GSPDB:GN00015; MIPS:YOR168w !'##experimental_source strain S288C REFERENCE A28494 !$#authors Ludmerer, S.W.; Schimmel, P. !$#journal J. Biol. Chem. (1987) 262:10801-10806 !$#title Gene for yeast glutamine tRNA synthetase encodes a large !1amino-terminal extension and provides a strong confirmation !1of the signature sequence for a group of the aminoacyl-tRNA !1synthetases. !$#cross-references MUID:87280149; PMID:3301841 !$#accession A28494 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-178,'Q',180-809 ##label LUD !'##cross-references EMBL:M29184 GENETICS !$#gene SGD:GLN4; MIPS:YOR168w !'##cross-references SGD:S0005694; MIPS:YOR168w !$#map_position 15R CLASSIFICATION #superfamily human glutamine-tRNA ligase; glutamine-tRNA !1ligase homology KEYWORDS aminoacyl-tRNA synthetase; ATP; ligase; protein biosynthesis FEATURE !$252-537 #domain glutamine-tRNA ligase homology #label EGL SUMMARY #length 809 #molecular-weight 93132 #checksum 1573 SEQUENCE /// ENTRY SYECRT #type complete TITLE arginine-tRNA ligase (EC 6.1.1.19) [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES arginyl-tRNA synthetase ORGANISM #formal_name Escherichia coli DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 03-Jun-2002 ACCESSIONS JS0267; D64950; S06050 REFERENCE JS0267 !$#authors Eriani, G.; Dirheimer, G.; Gangloff, J. !$#journal Nucleic Acids Res. (1989) 17:5725-5736 !$#title Isolation and characterization of the gene coding for !1Escherichia coli arginyl-tRNA synthetase. !$#cross-references MUID:89345164; PMID:2668891 !$#accession JS0267 !'##molecule_type DNA !'##residues 1-577 ##label ERI !'##cross-references GB:X15320; NID:g40963; PIDN:CAA33384.1; PID:g581040 !'##experimental_source K-12 !'##note the sequence of residues 1-19 was confirmed by protein !1sequencing REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64950 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-577 ##label BLAT !'##cross-references GB:AE000281; GB:U00096; NID:g1788179; !1PIDN:AAC74946.1; PID:g1788184; UWGP:b1876 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene argS !$#map_position 40 min !$#start_codon GTG FUNCTION !$#description EC 6.1.1.19 [validated, MUID:89345164]; activates amino acid !1and transfers it to specific tRNA molecule !$#pathway protein biosynthesis CLASSIFICATION #superfamily arginine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ATP; ligase; protein biosynthesis FEATURE !$129-132 #region ATP binding #status predicted SUMMARY #length 577 #molecular-weight 64682 #checksum 7436 SEQUENCE /// ENTRY JC4365 #type complete TITLE arginine-tRNA ligase (EC 6.1.1.19) - human ALTERNATE_NAMES arginyl-tRNA synthetase ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS JC4365 REFERENCE JC4365 !$#authors Girjes, A.A.; Hobson, K.; Chen, P.; Lavin, M.F. !$#journal Gene (1995) 164:347-350 !$#title Cloning and characterization of cDNA encoding a human !1arginyl-tRNA synthetase. !$#cross-references MUID:96069607; PMID:7590355 !$#accession JC4365 !'##molecule_type mRNA !'##residues 1-659 ##label GIR !'##cross-references GB:S80343; NID:g1217667; PIDN:AAB35627.1; !1PID:g1217668 GENETICS !$#gene GDB:RARS; ArgRS !'##cross-references GDB:1313718; OMIM:107820 !$#map_position 5pter-5q11 CLASSIFICATION #superfamily arginine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ligase; protein biosynthesis SUMMARY #length 659 #molecular-weight 74977 #checksum 5790 SEQUENCE /// ENTRY JN0870 #type complete TITLE arginine-tRNA ligase (EC 6.1.1.19) - Chinese hamster ALTERNATE_NAMES arginyl-tRNA synthetase ORGANISM #formal_name Cricetulus griseus #common_name Chinese hamster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS JN0870; PN0668 REFERENCE JN0870 !$#authors Lazard, M.; Mirande, M. !$#journal Gene (1993) 132:237-245 !$#title Cloning and analysis of a cDNA encoding mammalian !1arginyl-tRNA synthetase, a component of the multisynthetase !1complex with a hydrophobic N-terminal extension. !$#cross-references MUID:94040767; PMID:8224869 !$#accession JN0870 !'##molecule_type mRNA !'##residues 1-661 ##label LAZ !'##cross-references GB:X63415; NID:g433543; PIDN:CAA45012.1; !1PID:g433544 !'##experimental_source ovary !'##note in Genbank entry CLRRS1, release 109, the source is designated !1as Cricetulus longicaudatus !$#accession PN0668 !'##molecule_type protein !'##residues 74-93 ##label LA1 COMMENT This enzyme is one of the components of a ubiquitous !1multienzyme complex. CLASSIFICATION #superfamily arginine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ligase; protein biosynthesis SUMMARY #length 661 #molecular-weight 75601 #checksum 2162 SEQUENCE /// ENTRY F64329 #type complete TITLE arginine-tRNA ligase (EC 6.1.1.19) - Methanococcus jannaschii ALTERNATE_NAMES arginyl-tRNA synthetase ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS F64329 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession F64329 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-566 ##label BUL !'##cross-references GB:U67479; GB:L77117; NID:g1590965; !1PIDN:AAB98223.1; PID:g1590971; TIGR:MJ0237 GENETICS !$#map_position FOR228023-229723 CLASSIFICATION #superfamily Bacillus arginine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ligase; protein biosynthesis SUMMARY #length 566 #molecular-weight 64979 #checksum 7179 SEQUENCE /// ENTRY F69361 #type complete TITLE arginyl-tRNA synthetase (argS) homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS F69361 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession F69361 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-549 ##label KLE !'##cross-references GB:AE001042; GB:AE000782; NID:g2689365; !1PIDN:AAB90346.1; PID:g2649707; TIGR:AF0894 CLASSIFICATION #superfamily Bacillus arginine-tRNA ligase SUMMARY #length 549 #molecular-weight 62861 #checksum 8871 SEQUENCE /// ENTRY F69059 #type complete TITLE arginine-tRNA ligase (EC 6.1.1.19) - Methanobacterium thermoautotrophicum (strain Delta H) ALTERNATE_NAMES arginyl-tRNA synthetase ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS F69059 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession F69059 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-560 ##label MTH !'##cross-references GB:AE000906; GB:AE000666; NID:g2622557; !1PIDN:AAB85922.1; PID:g2622560 !'##experimental_source strain Delta H GENETICS !$#gene MTH1447 CLASSIFICATION #superfamily Bacillus arginine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ligase; protein biosynthesis SUMMARY #length 560 #molecular-weight 63647 #checksum 3308 SEQUENCE /// ENTRY A49936 #type complete TITLE arginine-tRNA ligase (EC 6.1.1.19) - Corynebacterium glutamicum ALTERNATE_NAMES arginyl-tRNA synthetase ORGANISM #formal_name Corynebacterium glutamicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS A49936; S42850 REFERENCE A49936 !$#authors Oguiza, J.A.; Malumbres, M.; Eriani, G.; Pisabarro, A.; !1Mateos, L.M.; Martin, F.; Martin, J.F. !$#journal J. Bacteriol. (1993) 175:7356-7362 !$#title A gene encoding arginyl-tRNA synthetase is located in the !1upstream region of the lysA gene in Brevibacterium !1lactofermentum: regulation of argS-lysA cluster expression !1by arginine. !$#cross-references MUID:94042911; PMID:8226683 !$#accession A49936 !'##molecule_type DNA !'##residues 1-550 ##label OGU !'##cross-references EMBL:Z21501; NID:g433533; PIDN:CAA79710.1; !1PID:g433534 !'##note nucleotide sequence not given; conceptual translation not !1complete GENETICS !$#gene argS CLASSIFICATION #superfamily Bacillus arginine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ligase; protein biosynthesis SUMMARY #length 550 #molecular-weight 59789 #checksum 8922 SEQUENCE /// ENTRY E69589 #type complete TITLE arginine-tRNA ligase (EC 6.1.1.19) argS - Bacillus subtilis ALTERNATE_NAMES arginyl-tRNA synthetase ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS E69589; S60082 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69589 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-556 ##label KUN !'##cross-references GB:Z99123; GB:AL009126; NID:g2636240; !1PIDN:CAB15761.1; PID:g2636270 !'##experimental_source strain 168 REFERENCE S60080 !$#authors Cruz Ramos, H.; Boursier, L.; Moszer, I.; Kunst, F.; !1Danchin, A.; Glaser, P. !$#journal EMBO J. (1995) 14:5984-5994 !$#title Anaerobic transcription activation in Bacillus subtilis: !1identification of distinct FNR-dependent and -independent !1regulatory mechanisms. !$#cross-references MUID:96112813; PMID:8846791 !$#accession S60082 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 442-556 ##label CRU !'##cross-references EMBL:Z49884; NID:g971335; PIDN:CAA90040.1; !1PID:g971336 !'##experimental_source strain 168 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 2995 GENETICS !$#gene argS CLASSIFICATION #superfamily Bacillus arginine-tRNA ligase KEYWORDS aminoacyl-tRNA synthetase; ligase; protein biosynthesis SUMMARY #length 556 #molecular-weight 62722 #checksum 6960 SEQUENCE /// ENTRY YFBYAM #type complete TITLE phenylalanine-tRNA ligase (EC 6.1.1.20) alpha chain precursor, mitochondrial - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES phenylalanyl-tRNA synthetase alpha chain; protein YP9499.05; protein YPR047w ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1992 #sequence_revision 01-Dec-1995 #text_change 03-Jun-2002 ACCESSIONS S54071; A26554; A41294 REFERENCE S54059 !$#authors Badcock, K.; Churcher, C.M. !$#submission submitted to the EMBL Data Library, May 1995 !$#accession S54071 !'##molecule_type DNA !'##residues 1-474 ##label BAD !'##cross-references EMBL:Z49219; NID:g805025; PIDN:CAA89167.1; !1PID:g805030; GSPDB:GN00016; MIPS:YPR047w !'##experimental_source strain AB972 REFERENCE A26554 !$#authors Koerner, T.J.; Myers, A.M.; Lee, S.; Tzagoloff, A. !$#journal J. Biol. Chem. (1987) 262:3690-3696 !$#title Isolation and characterization of the yeast gene coding for !1the alpha-subunit of mitochondrial phenylalanyl-tRNA !1synthetase. !$#cross-references MUID:87137670; PMID:3029120 !$#accession A26554 !'##molecule_type DNA !'##residues 1-90,'E',92-474 ##label KOE !'##cross-references GB:J02691 REFERENCE A41294 !$#authors Sanni, A.; Walter, P.; Boulanger, Y.; Ebel, J.P.; Fasiolo, !1F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:8387-8391 !$#title Evolution of aminoacyl-tRNA synthetase quaternary structure !1and activity: Saccharomyces cerevisiae mitochondrial !1phenylalanyl-tRNA synthetase. !$#cross-references MUID:92020858; PMID:1924298 !$#accession A41294 !'##molecule_type protein !'##residues 11-17;21-27 ##label SAN GENETICS !$#gene SGD:MSF1; MIPS:YPR047w !'##cross-references SGD:S0006251; MIPS:YPR047w !$#map_position 16R !$#genome nuclear CLASSIFICATION #superfamily phenylalanine-tRNA ligase alpha chain KEYWORDS aminoacyl-tRNA synthetase; ATP; heterotetramer; ligase; !1mitochondrion; protein biosynthesis FEATURE !$1-10 #domain transit peptide (mitochondrion) #status !8experimental #label TPN\ !$11-474 #product phenylalanine-tRNA ligase alpha chain !8#status experimental #label MAT SUMMARY #length 474 #molecular-weight 55376 #checksum 7046 SEQUENCE /// ENTRY SYECFA #type complete TITLE phenylalanine-tRNA ligase (EC 6.1.1.20) alpha chain - Escherichia coli (strain K-12) ALTERNATE_NAMES phenylalanyl-tRNA synthetase alpha chain ORGANISM #formal_name Escherichia coli DATE 31-Mar-1990 #sequence_revision 17-Oct-1997 #text_change 03-Jun-2002 ACCESSIONS B64930; A30391; A30392; I41283; A23099; Q00250 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64930 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-327 ##label BLAT !'##cross-references GB:AE000266; GB:U00096; NID:g1787997; !1PIDN:AAC74784.1; PID:g1788007; UWGP:b1714 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A30391 !$#authors Fayat, G.; Mayaux, J.F.; Sacerdot, C.; Fromant, M.; !1Springer, M.; Grunberg-Manago, M.; Blanquet, S. !$#journal J. Mol. Biol. (1983) 171:239-261 !$#title Escherichia coli phenylalanyl-tRNA synthetase operon region. !1Evidence for an attenuation mechanism. Identification of the !1gene for the ribosomal protein L20. !$#cross-references MUID:84090239; PMID:6317865 !$#accession A30391 !'##molecule_type DNA !'##residues 'MRKT',1-73,'A',75-327 ##label FAY !'##cross-references GB:V00291; NID:g43065; PIDN:CAA23564.1; PID:g43070; !1GB:M10430 REFERENCE A30392 !$#authors Mechulam, Y.; Fayat, G.; Blanquet, S. !$#journal J. Bacteriol. (1985) 163:787-791 !$#title Sequence of the Escherichia coli pheST operon and !1identification of the himA gene. !$#cross-references MUID:85261100; PMID:2991205 !$#accession A30392 !'##molecule_type DNA !'##residues 253-327 ##label MEC !'##cross-references GB:V00291; GB:M10430 REFERENCE I41281 !$#authors Miller, H.I. !$#journal Cold Spring Harb. Symp. Quant. Biol. (1984) 49:691-698 !$#title Primary structure of the himA gene of Escherichia coli: !1homology with DNA-binding protein HU and association with !1the phenylalanyl-tRNA synthetase operon. !$#cross-references MUID:85153048; PMID:6397321 !$#accession I41283 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-73,'A',75-327 ##label RES !'##cross-references GB:K02844; NID:g146342; PIDN:AAA51469.1; !1PID:g146345 GENETICS !$#gene pheS !$#map_position 37 min COMPLEX heterotetramer; two alpha and two beta chains FUNCTION !$#description catalyzes transfer of activated phenylalanine to !1phenylalanyl-tRNA CLASSIFICATION #superfamily phenylalanine-tRNA ligase alpha chain KEYWORDS aminoacyl-tRNA synthetase; ATP; heterotetramer; ligase; !1protein biosynthesis SUMMARY #length 327 #molecular-weight 36832 #checksum 8081 SEQUENCE /// ENTRY YFBSA #type complete TITLE phenylalanine-tRNA ligase (EC 6.1.1.20) alpha chain - Bacillus subtilis ALTERNATE_NAMES phenylalanyl-tRNA synthetase alpha chain ORGANISM #formal_name Bacillus subtilis DATE 30-Sep-1992 #sequence_revision 02-Jul-1998 #text_change 03-Jun-2002 ACCESSIONS H69675; I40459; S11730 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69675 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-344 ##label KUN !'##cross-references GB:Z99118; GB:AL009126; NID:g2635200; !1PIDN:CAB14824.1; PID:g2635329 !'##experimental_source strain 168 REFERENCE I40459 !$#authors Brakhage, A.A.; Wozny, M.; Putzer, H. !$#journal Biochimie (1990) 72:725-734 !$#title Structure and nucleotide sequence of the Bacillus subtilis !1phenylalanyl-tRNA synthetase genes. !$#cross-references MUID:91175935; PMID:2127701 !$#accession I40459 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-89,'DRQLTSRCREPCCSR',106-344 ##label BRA !'##cross-references EMBL:X53057; NID:g40052; PIDN:CAA37224.1; !1PID:g40053 GENETICS !$#gene pheS COMPLEX heterotetramer; two alpha and two beta chains; (see !1PIR:YFBSB) FUNCTION !$#description catalyzes transfer of activated phenylalanine to !1phenylalanyl-tRNA CLASSIFICATION #superfamily phenylalanine-tRNA ligase alpha chain KEYWORDS aminoacyl-tRNA synthetase; ATP; heterotetramer; ligase; !1protein biosynthesis SUMMARY #length 344 #molecular-weight 38675 #checksum 5505 SEQUENCE /// ENTRY YFBYBC #type complete TITLE phenylalanine-tRNA ligase (EC 6.1.1.20) alpha chain, cytosolic [validated] - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES phenylalanyl-tRNA synthetase large chain; protein L2165; protein YLR060w ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1992 #sequence_revision 12-Apr-1996 #text_change 03-Jun-2002 ACCESSIONS S61634; A31990; S64888 REFERENCE S61618 !$#authors Urrestarazu, L.A. !$#submission submitted to the EMBL Data Library, December 1995 !$#accession S61634 !'##molecule_type DNA !'##residues 1-595 ##label URR !'##cross-references EMBL:X94607; NID:g1181264; PIDN:CAA64307.1; !1PID:g1181281 REFERENCE A92675 !$#authors Sanni, A.; Mirande, M.; Ebel, J.P.; Boulanger, Y.; Waller, !1J.P.; Fasiolo, F. !$#journal J. Biol. Chem. (1988) 263:15407-15415 !$#title Structure and expression of the genes encoding the alpha-and !1beta-subunits of yeast phenylalanyl-tRNA synthetase. !$#cross-references MUID:89008440; PMID:3049607 !$#accession A31990 !'##molecule_type DNA !'##residues 1-17,'D',19-425,'D',427-595 ##label SAN !'##cross-references GB:J03964 !'##note part of this sequence was confirmed by protein sequencing REFERENCE S64872 !$#authors Andre, B.; Urrestarazu, L.A. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64888 !'##molecule_type DNA !'##residues 1-595 ##label AND !'##cross-references EMBL:Z73232; NID:g1360405; PIDN:CAA97591.1; !1PID:g1360406; GSPDB:GN00012; MIPS:YLR060w !'##note experimental_source strain S288C GENETICS !$#gene SGD:FRS1; MIPS:YLR060w !'##cross-references SGD:S0004050; MIPS:YLR060w !$#map_position 12R COMPLEX heterotetramer; two alpha and two beta chains FUNCTION !$#description EC 6.1.1.20 [validated, MUID:89008440] !$#pathway protein biosynthesis CLASSIFICATION #superfamily yeast cytosolic phenylalanine-tRNA ligase alpha !1chain KEYWORDS aminoacyl-tRNA synthetase; ATP; heterotetramer; ligase; !1protein biosynthesis SUMMARY #length 595 #molecular-weight 67364 #checksum 8045 SEQUENCE /// ENTRY SYECFB #type complete TITLE phenylalanine-tRNA ligase (EC 6.1.1.20) beta chain - Escherichia coli (strain K-12) ALTERNATE_NAMES phenylalanyl-tRNA synthetase beta chain ORGANISM #formal_name Escherichia coli DATE 28-Dec-1987 #sequence_revision 05-Dec-1997 #text_change 03-Jun-2002 ACCESSIONS I41284; A64930; B23099 REFERENCE I41281 !$#authors Miller, H.I. !$#journal Cold Spring Harb. Symp. Quant. Biol. (1984) 49:691-698 !$#title Primary structure of the himA gene of Escherichia coli: !1homology with DNA-binding protein HU and association with !1the phenylalanyl-tRNA synthetase operon. !$#cross-references MUID:85153048; PMID:6397321 !$#accession I41284 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-795 ##label RES !'##cross-references GB:K02844; NID:g146342; PIDN:AAA51470.1; !1PID:g146346 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64930 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-795 ##label BLAT !'##cross-references GB:AE000266; GB:U00096; NID:g1787997; !1PIDN:AAC74783.1; PID:g1788006; UWGP:b1713 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A30392 !$#authors Mechulam, Y.; Fayat, G.; Blanquet, S. !$#journal J. Bacteriol. (1985) 163:787-791 !$#title Sequence of the Escherichia coli pheST operon and !1identification of the himA gene. !$#cross-references MUID:85261100; PMID:2991205 !$#accession B23099 !'##molecule_type DNA !'##residues 1-92,'T',94-140,'VR',143-185,'AAGN',190-480,'R',482-697, !1'G',699-795 ##label MEC !'##cross-references GB:V00291; NID:g43065; PIDN:CAA23565.1; PID:g43071; !1GB:M10430 GENETICS !$#gene pheT !$#map_position 38 min COMPLEX heterotetramer; two alpha and two beta chains FUNCTION !$#description catalyzes transfer of activated phenylalanine to !1phenylalanyl-tRNA CLASSIFICATION #superfamily phenylalanine-tRNA ligase beta chain KEYWORDS aminoacyl-tRNA synthetase; ATP; heterotetramer; ligase; !1protein biosynthesis SUMMARY #length 795 #molecular-weight 87377 #checksum 8595 SEQUENCE /// ENTRY YFBSB #type complete TITLE phenylalanine-tRNA ligase (EC 6.1.1.20) beta chain - Bacillus subtilis ALTERNATE_NAMES phenylalanyl-tRNA synthetase beta chain ORGANISM #formal_name Bacillus subtilis DATE 30-Sep-1992 #sequence_revision 02-Jul-1998 #text_change 03-Jun-2002 ACCESSIONS A69676; I40460; S11731 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69676 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-804 ##label KUN !'##cross-references GB:Z99118; GB:AL009126; NID:g2635200; !1PIDN:CAB14823.1; PID:g2635328 !'##experimental_source strain 168 REFERENCE I40459 !$#authors Brakhage, A.A.; Wozny, M.; Putzer, H. !$#journal Biochimie (1990) 72:725-734 !$#title Structure and nucleotide sequence of the Bacillus subtilis !1phenylalanyl-tRNA synthetase genes. !$#cross-references MUID:91175935; PMID:2127701 !$#accession I40460 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-109,'NV',112-804 ##label BRA !'##cross-references EMBL:X53057; NID:g40052; PIDN:CAA37225.1; !1PID:g40054 GENETICS !$#gene pheT COMPLEX heterotetramer of two alpha (see PIR:YFBSA) and two beta !1chains CLASSIFICATION #superfamily phenylalanine-tRNA ligase beta chain KEYWORDS aminoacyl-tRNA synthetase; ATP; heterotetramer; ligase; !1protein biosynthesis SUMMARY #length 804 #molecular-weight 87945 #checksum 6551 SEQUENCE /// ENTRY YFBYAC #type complete TITLE phenylalanine-tRNA ligase (EC 6.1.1.20) beta chain, cytosolic [validated] - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES phenylalanyl-tRNA synthetase small chain, cytosolic; protein YFL022c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1992 #sequence_revision 19-Oct-1995 #text_change 03-Jun-2002 ACCESSIONS S56232; B31990 REFERENCE S56186 !$#authors Murakami, Y.; Naitou, M.; Hagiwara, H.; Shibata, T.; Ozawa, !1M.; Sasanuma, S.I.; Sasanuma, M.; Tsuchiya, Y.; Soeda, E.; !1Yokoyama, K.; Yamazaki, M.; Tashiro, H.; Eki, T. !$#submission submitted to the EMBL Data Library, May 1995 !$#description Analysis of the nucleotide sequence of chromosome VI from !1Saccaromyces cerevisiae. !$#accession S56232 !'##molecule_type DNA !'##residues 1-503 ##label MUR !'##cross-references EMBL:D50617; NID:g836685; PIDN:BAA09216.1; !1PID:g836732; GSPDB:GN00006; MIPS:YFL022c REFERENCE A92675 !$#authors Sanni, A.; Mirande, M.; Ebel, J.P.; Boulanger, Y.; Waller, !1J.P.; Fasiolo, F. !$#journal J. Biol. Chem. (1988) 263:15407-15415 !$#title Structure and expression of the genes encoding the alpha-and !1beta-subunits of yeast phenylalanyl-tRNA synthetase. !$#cross-references MUID:89008440; PMID:3049607 !$#accession B31990 !'##molecule_type DNA !'##residues 1-176,'S',178-288,'E',290-503 ##label SAN !'##cross-references GB:J03964 !'##note most of this sequence was confirmed by protein sequencing REFERENCE A40139 !$#authors Fasiolo, F.; Sanni, A.; Potier, S.; Ebel, J.P.; Boulanger, !1Y. !$#journal FEBS Lett. (1989) 242:351-356 !$#title Identification of the major tRNA(Phe) binding domain in the !1tetrameric structure of cytoplasmic phenylalanyl-tRNA !1synthetase from baker's yeast. !$#cross-references MUID:89121098; PMID:2644133 !$#contents annotation; tRNA[Phe] binding domain GENETICS !$#gene SGD:FRS2; MIPS:YFL022c !'##cross-references MIPS:YFL022c; SGD:S0001872 !$#map_position 6L FUNCTION !$#description EC 6.1.1.20 [validated, MUID:89008440] !$#pathway protein biosynthesis CLASSIFICATION #superfamily yeast cytosolic phenylalanine-tRNA ligase beta !1chain KEYWORDS aminoacyl-tRNA synthetase; ATP; heterotetramer; ligase; !1protein biosynthesis FEATURE !$1-172 #domain tRNA binding #status predicted #label PHE SUMMARY #length 503 #molecular-weight 57511 #checksum 73 SEQUENCE /// ENTRY SYECH #type complete TITLE histidine-tRNA ligase (EC 6.1.1.21) [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES histidyl-tRNA synthetase ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 03-Jun-2002 ACCESSIONS A23890; A65028 REFERENCE A23890 !$#authors Freedman, R.; Gibson, B.; Donovan, D.; Biemann, K.; !1Eisenbeis, S.; Parker, J.; Schimmel, P. !$#journal J. Biol. Chem. (1985) 260:10063-10068 !$#title Primary structure of histidine-tRNA synthetase and !1characterization of hisS transcripts. !$#cross-references MUID:85261421; PMID:2991272 !$#accession A23890 !'##molecule_type DNA !'##residues 1-424 ##label FRE !'##cross-references GB:M11843; NID:g415626; PIDN:AAA03226.1; !1PID:g146372 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65028 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-424 ##label BLAT !'##cross-references GB:AE000337; GB:U00096; NID:g1788850; !1PIDN:AAC75567.1; PID:g1788861; UWGP:b2514 !'##experimental_source strain K-12, substrain MG1655 COMMENT This enzyme is one of the smallest bacterial aminoacyl-tRNA !1synthetases. GENETICS !$#gene hisS !$#map_position 54 min !$#start_codon GTG FUNCTION !$#description EC 6.1.1.21 [validated, MUID:85261421] CLASSIFICATION #superfamily histidine-tRNA ligase; histidine-tRNA ligase !1homology KEYWORDS aminoacyl-tRNA synthetase; ATP; homodimer; ligase; protein !1biosynthesis FEATURE !$1-391 #domain histidine-tRNA ligase homology #label HTL SUMMARY #length 424 #molecular-weight 47029 #checksum 8187 SEQUENCE /// ENTRY H64203 #type complete TITLE histidine-tRNA ligase (EC 6.1.1.21) - Mycoplasma genitalium ALTERNATE_NAMES histidyl-tRNA synthetase ORGANISM #formal_name Mycoplasma genitalium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS H64203 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession H64203 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-414 ##label TIGR !'##cross-references GB:U39682; GB:L43967; NID:g1045702; PID:g1045706; !1TIGR:MG035 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily histidine-tRNA ligase; histidine-tRNA ligase !1homology KEYWORDS aminoacyl-tRNA synthetase; ligase; protein biosynthesis SUMMARY #length 414 #molecular-weight 48323 #checksum 7263 SEQUENCE /// ENTRY C70725 #type complete TITLE probable hisS protein - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS C70725 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession C70725 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-423 ##label COL !'##cross-references GB:Z77724; GB:AL123456; NID:g3261620; !1PIDN:CAB01263.1; PID:g1478232 !'##experimental_source strain H37Rv GENETICS !$#gene hisS CLASSIFICATION #superfamily histidine-tRNA ligase; histidine-tRNA ligase !1homology SUMMARY #length 423 #molecular-weight 45149 #checksum 7314 SEQUENCE /// ENTRY E69130 #type complete TITLE histidine-tRNA ligase (EC 6.1.1.21) - Methanobacterium thermoautotrophicum (strain Delta H) ALTERNATE_NAMES histidyl-tRNA synthetase ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS E69130 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession E69130 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-444 ##label MTH !'##cross-references GB:AE000811; GB:AE000666; NID:g2621287; !1PIDN:AAB84750.1; PID:g2621293 !'##experimental_source strain Delta H GENETICS !$#gene MTH244 CLASSIFICATION #superfamily histidine-tRNA ligase; histidine-tRNA ligase !1homology KEYWORDS aminoacyl-tRNA synthetase; ligase; protein biosynthesis FEATURE !$26-412 #domain histidine-tRNA ligase homology #label HTL SUMMARY #length 444 #molecular-weight 50062 #checksum 1718 SEQUENCE /// ENTRY G69641 #type complete TITLE histidine-tRNA ligase (EC 6.1.1.21) hisS - Bacillus subtilis ALTERNATE_NAMES histidyl-tRNA synthetase ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS G69641 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69641 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-424 ##label KUN !'##cross-references GB:Z99118; GB:AL009126; NID:g2635200; !1PIDN:CAB14715.1; PID:g2635220 !'##experimental_source strain 168 GENETICS !$#gene hisS CLASSIFICATION #superfamily histidine-tRNA ligase; histidine-tRNA ligase !1homology KEYWORDS aminoacyl-tRNA synthetase; ligase; protein biosynthesis SUMMARY #length 424 #molecular-weight 48131 #checksum 6948 SEQUENCE /// ENTRY G70311 #type complete TITLE histidine-tRNA ligase (EC 6.1.1.21) - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS G70311 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession G70311 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-403 ##label AQF !'##cross-references GB:AE000674; NID:g2982850; PIDN:AAC06477.1; !1PID:g2982856; GB:AE000657 !'##experimental_source strain VF5 GENETICS !$#gene hisS1 CLASSIFICATION #superfamily histidine-tRNA ligase; histidine-tRNA ligase !1homology KEYWORDS aminoacyl-tRNA synthetase; ligase; protein biosynthesis SUMMARY #length 403 #molecular-weight 46410 #checksum 7739 SEQUENCE /// ENTRY G64424 #type complete TITLE histidine-tRNA ligase (EC 6.1.1.21) - Methanococcus jannaschii ALTERNATE_NAMES histidyl-tRNA synthetase ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS G64424 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession G64424 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-416 ##label BUL !'##cross-references GB:U67542; GB:L77117; NID:g2826356; !1PIDN:AAB99003.1; PID:g1591660; TIGR:MJ1000 GENETICS !$#map_position FOR928720-929970 CLASSIFICATION #superfamily histidine-tRNA ligase; histidine-tRNA ligase !1homology KEYWORDS aminoacyl-tRNA synthetase; ligase; protein biosynthesis FEATURE !$1-389 #domain histidine-tRNA ligase homology #label HTL SUMMARY #length 416 #molecular-weight 48322 #checksum 2740 SEQUENCE /// ENTRY A69455 #type complete TITLE histidyl-tRNA synthetase (hisS) homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS A69455 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession A69455 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-409 ##label KLE !'##cross-references GB:AE000989; GB:AE000782; NID:g2689312; !1PIDN:AAB89600.1; PID:g2648908; TIGR:AF1642 CLASSIFICATION #superfamily histidine-tRNA ligase; histidine-tRNA ligase !1homology SUMMARY #length 409 #molecular-weight 46217 #checksum 1599 SEQUENCE /// ENTRY F64668 #type complete TITLE histidine-tRNA ligase (EC 6.1.1.21) - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS F64668 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession F64668 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-442 ##label TOM !'##cross-references GB:AE000625; GB:AE000511; NID:g2314349; !1PIDN:AAD08236.1; PID:g2314351; TIGR:HP1190 CLASSIFICATION #superfamily histidine-tRNA ligase; histidine-tRNA ligase !1homology KEYWORDS ligase FEATURE !$8-406 #domain histidine-tRNA ligase homology #label HTL SUMMARY #length 442 #molecular-weight 50172 #checksum 5089 SEQUENCE /// ENTRY G70116 #type complete TITLE histidine-tRNA ligase (EC 6.1.1.21) hisS - Lyme disease spirochete ALTERNATE_NAMES histidyl-tRNA synthetase ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS G70116 REFERENCE A70100 !$#authors Fraser, C.M.; Casjens, S.; Huang, W.M.; Sutton, G.G.; !1Clayton, R.; Lathigra, R.; White, O.; Ketchum, K.A.; Dodson, !1R.; Hickey, E.K.; Gwinn, M.; Dougherty, B.; Tomb, J.F.; !1Fleischmann, R.D.; Richardson, D.; Peterson, J.; Kerlavage, !1A.R.; Quackenbush, J.; Salzberg, S.; Hanson, M.; Vugt, R.V.; !1Palmer, N.; Adams, M.D.; Gocayne, J.; Weidman, J.; !1Utterback, T.; Watthey, L.; McDonald, L.; Artiach, P.; !1Bowman, C.; Garland, S.; Fujii, C.; Cotton, M.D.; Horst, K.; !1Roberts, K.; Hatch, B.; Smith, H.O.; Venter, J.C. !$#journal Nature (1997) 390:580-586 !$#title Genomic sequence of a Lyme disease spirochaete, Borrelia !1burgdorferi. !$#cross-references MUID:98065943; PMID:9403685 !$#accession G70116 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-457 ##label KLE !'##cross-references GB:AE001125; GB:AE000783; NID:g2688021; !1PIDN:AAC66531.1; PID:g2688030; TIGR:BB0135 !'##experimental_source strain B31 CLASSIFICATION #superfamily histidine-tRNA ligase; histidine-tRNA ligase !1homology KEYWORDS aminoacyl-tRNA synthetase; ligase; protein biosynthesis FEATURE !$8-418 #domain histidine-tRNA ligase homology #label HTL SUMMARY #length 457 #molecular-weight 52848 #checksum 4898 SEQUENCE /// ENTRY SYHUHT #type complete TITLE histidine-tRNA ligase (EC 6.1.1.21) - human ALTERNATE_NAMES histidyl-tRNA synthetase ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1992 #sequence_revision 02-Jul-1996 #text_change 03-Jun-2002 ACCESSIONS I37559; B27516; I53670; I38914; S18985 REFERENCE I37559 !$#authors Raben, N.; Borriello, F.; Amin, J.; Horwitz, R.; Fraser, D.; !1Plotz, P. !$#journal Nucleic Acids Res. (1992) 20:1075-1081 !$#title Human histidyl-tRNA synthetase: recognition of amino acid !1signature regions in class 2a aminoacyl-tRNA synthetases. !$#cross-references MUID:92195807; PMID:1549469 !$#accession I37559 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-509 ##label RES !'##cross-references EMBL:Z11518; NID:g32459; PIDN:CAA77607.1; !1PID:g32460 !'##note authors discuss differences between their sequence and that !1from reference A93663 and describe further experimental !1confirmation of theirs as the correct sequence REFERENCE A93663 !$#authors Tsui, F.W.L.; Siminovitch, L. !$#journal Nucleic Acids Res. (1987) 15:3349-3367 !$#title Isolation, structure and expression of mammalian genes for !1histidyl-tRNA synthetase. !$#cross-references MUID:87203366; PMID:3554142 !$#accession B27516 !'##molecule_type mRNA !'##residues 1-5,'P',7-164,'G',166-168,'PNSITV',175-180,'Q',182-185,'N', !1187-190,'S',192-205,'N',207-222,'V',224-226,'P',228-283,'V', !1285-346,'E',348-351,'W','C',355,'QCGCWR',362-372,'QR', !1375-377,'AMC',381,'AQHWGG',388-420,'ARGKT',426,'ACLR', !1431-492,'E',494-509 ##label TSU !'##cross-references GB:X05345; NID:g32457; PIDN:CAA28956.1; PID:g32458 !'##note the authors translated the codon GAT for residue 433 as Phe REFERENCE I53670 !$#authors Tsui, H.W.; Mok, S.; de Souza, L.; Martin, A.; Tsui, F.W. !$#journal Gene (1993) 131:201-208 !$#title Transcriptional analyses of the gene region that encodes !1human histidyl-tRNA synthetase: identification of a novel !1bidirectional regulatory element. !$#cross-references MUID:94010309; PMID:8406012 !$#accession I53670 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-30 ##label TS2 !'##cross-references GB:M96646; NID:g431311; PIDN:AAA58668.1; !1PID:g431312 REFERENCE I38913 !$#authors O'Hanlon, T.P.; Raben, N.; Miller, F.W. !$#journal Biochem. Biophys. Res. Commun. (1995) 210:556-566 !$#title A novel gene oriented in a head-to-head configuration with !1the human histidyl-tRNA synthetase (HRS) gene encodes an !1mRNA that predicts a polypeptide homologous to HRS. !$#cross-references MUID:95275311; PMID:7755634 !$#accession I38914 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-30 ##label RE2 !'##cross-references EMBL:U18936; NID:g899105; PIDN:AAA73973.1; !1PID:g899107 GENETICS !$#gene GDB:HARS; HRS !'##cross-references GDB:120034; OMIM:142810 !$#map_position 5q31.1-5q33.2 CLASSIFICATION #superfamily human histidine-tRNA ligase; amino acid-tRNA !1ligase repeat homology; histidine-tRNA ligase homology KEYWORDS aminoacyl-tRNA synthetase; ATP; homodimer; ligase; protein !1biosynthesis FEATURE !$14-59 #domain amino acid-tRNA ligase repeat homology #label !8ATL\ !$60-470 #domain histidine-tRNA ligase homology #label HTL SUMMARY #length 509 #molecular-weight 57410 #checksum 2360 SEQUENCE /// ENTRY SYHYHT #type complete TITLE histidine-tRNA ligase (EC 6.1.1.21) - Chinese hamster ALTERNATE_NAMES histidyl-tRNA synthetase ORGANISM #formal_name Cricetulus griseus #common_name Chinese hamster DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 19-Jul-2002 ACCESSIONS A27516 REFERENCE A93663 !$#authors Tsui, F.W.L.; Siminovitch, L. !$#journal Nucleic Acids Res. (1987) 15:3349-3367 !$#title Isolation, structure and expression of mammalian genes for !1histidyl-tRNA synthetase. !$#cross-references MUID:87203366; PMID:3554142 !$#accession A27516 !'##molecule_type mRNA !'##residues 1-508 ##label TSU !'##cross-references GB:X05346; NID:g49631; PIDN:CAA28957.1; PID:g49632 !'##note the authors translated the codon GAC for residue 115 as Asn, !1AAA for residue 117 as Glu, CTG for residue 125 as Cys, GGA !1for residue 136 as Ala, CTG for residue 139 as Val, TTG for !1residue 144 as Ile, ACC for residue 145 as Gln, AAC for !1residue 146 as Ser, and GAG for residue 276 as Gly CLASSIFICATION #superfamily human histidine-tRNA ligase; amino acid-tRNA !1ligase repeat homology; histidine-tRNA ligase homology KEYWORDS aminoacyl-tRNA synthetase; ATP; homodimer; ligase; protein !1biosynthesis FEATURE !$14-59 #domain amino acid-tRNA ligase repeat homology #label !8ATL\ !$60-469 #domain histidine-tRNA ligase homology #label HTL SUMMARY #length 508 #molecular-weight 57425 #checksum 815 SEQUENCE /// ENTRY JC5223 #type complete TITLE histidine-tRNA ligase (EC 6.1.1.21) - mouse ALTERNATE_NAMES histidyl-tRNA synthetase ORGANISM #formal_name Mus musculus #common_name house mouse DATE 13-Mar-1997 #sequence_revision 13-Mar-1997 #text_change 19-Jul-2002 ACCESSIONS JC5223 REFERENCE JC5223 !$#authors Blechynden, L.M.; Lawson, C.M.; Garlepp, M.J. !$#journal Gene (1996) 178:151-156 !$#title Sequence and polymorphism analysis of the murine gene !1encoding histidyl-tRNA synthetase. !$#cross-references MUID:97080562; PMID:8921907 !$#accession JC5223 !'##status preliminary !'##molecule_type mRNA !'##residues 1-509 ##label BLE !'##cross-references GB:U39473; NID:g1209682; PIDN:AAC52914.1; !1PID:g1209683 COMMENT This enzyme plays a role in the development of inflammatory !1muscle disease. GENETICS !$#gene mmhrs CLASSIFICATION #superfamily human histidine-tRNA ligase; amino acid-tRNA !1ligase repeat homology; histidine-tRNA ligase homology KEYWORDS aminoacyl-tRNA synthetase; ATP; ligase; protein biosynthesis FEATURE !$14-59 #domain amino acid-tRNA ligase repeat homology #label !8ATL\ !$60-470 #domain histidine-tRNA ligase homology #label HTL SUMMARY #length 509 #molecular-weight 57416 #checksum 4109 SEQUENCE /// ENTRY T40151 #type complete TITLE histidine-tRNA ligase precursor, mitochondrial - fission yeast (Schizosaccharomyces pombe) ORGANISM #formal_name Schizosaccharomyces pombe DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 19-Jul-2002 ACCESSIONS T40151 REFERENCE Z21842 !$#authors Wood, V.; Rajandream, M.A.; Barrell, B.G.; Devlin, K.; !1Churcher, C.M. !$#submission submitted to the EMBL Data Library, March 1998 !$#accession T40151 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-538 ##label WOO !'##cross-references EMBL:AL022103; PIDN:CAA17892.1; GSPDB:GN00067; !1SPDB:SPBC2G2.12 !'##experimental_source strain 972h-; cosmid c2G2 GENETICS !$#gene SPDB:SPBC2G2.12 !$#map_position 2 !$#genome nuclear CLASSIFICATION #superfamily human histidine-tRNA ligase; amino acid-tRNA !1ligase repeat homology; histidine-tRNA ligase homology KEYWORDS mitochondrion FEATURE !$15-65 #domain amino acid-tRNA ligase repeat homology #label !8ATL\ !$66-526 #domain histidine-tRNA ligase homology #label HTL SUMMARY #length 538 #molecular-weight 60237 #checksum 9393 SEQUENCE /// ENTRY SYBYHM #type complete TITLE histidine-tRNA ligase (EC 6.1.1.21) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES histidyl-tRNA synthetase; protein YP9367.13c; protein YPR033c CONTAINS histidine-tRNA ligase (EC 6.1.1.21) precursor, mitochondrial; histidine-tRNA ligase (EC 6.1.1.21), cytosolic ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1992 #sequence_revision 12-Apr-1996 #text_change 02-Aug-2002 ACCESSIONS S54507; B23946; A23946 REFERENCE S54059 !$#authors Badcock, K.; Churcher, C.M. !$#submission submitted to the EMBL Data Library, May 1995 !$#accession S54507 !'##molecule_type DNA !'##residues 1-546 ##label BAD !'##cross-references EMBL:Z49274; NID:g809585; PIDN:CAA89287.1; !1PID:g809598; GSPDB:GN00016; MIPS:YPR033c !'##experimental_source strain AB972 REFERENCE A90882 !$#authors Natsoulis, G.; Hilger, F.; Fink, G.R. !$#journal Cell (1986) 46:235-243 !$#title The HTS1 gene encodes both the cytoplasmic and mitochondrial !1histidine tRNA synthetases of S. cerevisiae. !$#cross-references MUID:86245069; PMID:3521891 !$#accession B23946 !'##molecule_type DNA !'##residues 1-475,'TTK',479-546 ##label NAT !'##cross-references GB:M14048; NID:g171731; PIDN:AAA34695.1; !1PID:g171732 !'##note mitochondrial form !$#accession A23946 !'##molecule_type DNA !'##residues 21-475,'TTK',479-546 ##label NAF !'##cross-references GB:M14048; NID:g171731; PIDN:AAA34696.1; !1PID:g171733 !'##note cytosolic form COMMENT In S. cerevisiae, the gene encoding the histidine-tRNA !1ligase has two in-frame transcription start sites. The !1longer mRNA encodes the mitochondrial ligase and the shorter !1mRNA encodes the cytosolic ligase. GENETICS !$#gene SGD:HTS1; MIPS:YPR033c !'##cross-references SGD:S0006237; MIPS:YPR033c !$#map_position 16R !$#genome nuclear CLASSIFICATION #superfamily human histidine-tRNA ligase; amino acid-tRNA !1ligase repeat homology; histidine-tRNA ligase homology KEYWORDS alternative initiators; aminoacyl-tRNA synthetase; ATP; !1homodimer; ligase; mitochondrion; protein biosynthesis FEATURE !$1-20 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$21-546 #product histidine-tRNA ligase, mitochondrial #status !8predicted #label MAT1\ !$21-546 #product histidine-tRNA ligase, cytosolic #status !8predicted #label MAT2\ !$59-492 #domain histidine-tRNA ligase homology #label HTL SUMMARY #length 546 #molecular-weight 59952 #checksum 7769 SEQUENCE /// ENTRY SYNCAA #type complete TITLE acetate-CoA ligase (EC 6.2.1.1) - Neurospora crassa ALTERNATE_NAMES acetyl-CoA synthetase ORGANISM #formal_name Neurospora crassa DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 03-Jun-2002 ACCESSIONS S09244 REFERENCE S09244 !$#authors Connerton, I.F.; Fincham, J.R.S.; Sandeman, R.A.; Hynes, !1M.J. !$#journal Mol. Microbiol. (1990) 4:451-460 !$#title Comparison and cross-species expression of the acetyl-CoA !1synthetase genes of the ascomycete fungi, Aspergillus !1nidulans and Neurospora crassa. !$#cross-references MUID:90286921; PMID:1972535 !$#accession S09244 !'##molecule_type DNA !'##residues 1-626 ##label CON !'##cross-references EMBL:X16989; NID:g2972; PIDN:CAA34857.1; PID:g2973 !'##note the authors translated the codon CAC for residue 140 as Thr !'##note it is uncertain whether Met-1 or Met-21 is the initiator GENETICS !$#gene acu-5 !$#introns 608/3 CLASSIFICATION #superfamily acetate-CoA ligase; acetate-CoA ligase homology KEYWORDS acid-thiol ligase; coenzyme A FEATURE !$109-592 #domain acetate-CoA ligase homology #label ACL SUMMARY #length 626 #molecular-weight 69117 #checksum 1002 SEQUENCE /// ENTRY JN0781 #type complete TITLE acetate-CoA ligase (EC 6.2.1.1) - Penicillium chrysogenum ALTERNATE_NAMES acetate-coenzyme A synthetase ORGANISM #formal_name Penicillium chrysogenum DATE 03-Feb-1994 #sequence_revision 03-Feb-1994 #text_change 03-Jun-2002 ACCESSIONS JN0781; A48379 REFERENCE JN0781 !$#authors Martinez-Blanco, H.; Orejas, M.; Reglero, A.; Luengo, J.M.; !1Penalva, M.A. !$#journal Gene (1993) 130:265-270 !$#title Characterisation of the gene encoding acetyl-CoA synthetase !1in Penicillium chrysogenum: Conservation of intron position !1in plectomycetes. !$#cross-references MUID:93366184; PMID:8103029 !$#accession JN0781 !'##molecule_type DNA !'##residues 1-669 ##label MAR !'##cross-references GB:L09598; NID:g397804; PIDN:AAA02921.1; !1PID:g397805 REFERENCE A48379 !$#authors Gouka, R.J.; van Hartingsveldt, W.; Bovenberg, R.A.; van !1Zeijl, C.M.; van den Hondel, C.A.; van Gorcom, R.F. !$#journal Appl. Microbiol. Biotechnol. (1993) 38:514-519 !$#title Development of a new transformant selection system for !1Penicillium chrysogenum: isolation and characterization of !1the P. chrysogenum acetyl-coenzyme A synthetase gene (facA) !1and its use as a homologous selection marker. !$#cross-references MUID:93159753; PMID:7765289 !$#accession A48379 !'##molecule_type DNA !'##residues 1-669 ##label GOU !'##cross-references GB:S54801; NID:g265228; PIDN:AAC60546.1; !1PID:g265229 !'##note sequence extracted from NCBI backbone (NCBIN:124674, !1NCBIP:124675) COMMENT This enzyme is involved in an accesory step of penicillin !1biosynthesis, in addition to its role in primary metabolism. GENETICS !$#gene facA; acuA !$#introns 13/3; 428/3; 515/3; 559/1; 649/3 CLASSIFICATION #superfamily acetate-CoA ligase; acetate-CoA ligase homology KEYWORDS acid-thiol ligase; coenzyme A FEATURE !$148-633 #domain acetate-CoA ligase homology #label ACL SUMMARY #length 669 #molecular-weight 74287 #checksum 3135 SEQUENCE /// ENTRY SYASAA #type complete TITLE acetate-CoA ligase (EC 6.2.1.1) - Emericella nidulans ALTERNATE_NAMES acetyl-CoA synthetase ORGANISM #formal_name Emericella nidulans, Aspergillus nidulans DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 03-Jun-2002 ACCESSIONS S09245 REFERENCE S09244 !$#authors Connerton, I.F.; Fincham, J.R.S.; Sandeman, R.A.; Hynes, !1M.J. !$#journal Mol. Microbiol. (1990) 4:451-460 !$#title Comparison and cross-species expression of the acetyl-CoA !1synthetase genes of the ascomycete fungi, Aspergillus !1nidulans and Neurospora crassa. !$#cross-references MUID:90286921; PMID:1972535 !$#accession S09245 !'##molecule_type DNA !'##residues 1-670 ##label CON !'##cross-references EMBL:X16990; NID:g2340; PIDN:CAA34858.1; PID:g2341 GENETICS !$#gene facA !$#introns 13/3; 428/3; 515/3; 559/1; 650/3 CLASSIFICATION #superfamily acetate-CoA ligase; acetate-CoA ligase homology KEYWORDS acid-thiol ligase; coenzyme A FEATURE !$148-634 #domain acetate-CoA ligase homology #label ACL SUMMARY #length 670 #molecular-weight 74262 #checksum 9086 SEQUENCE /// ENTRY S30019 #type complete TITLE acetate-CoA ligase (EC 6.2.1.1) ACS1, aerobic form [validated] - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES acetate thiokinase; acetyl-activating enzyme; acetyl-CoA synthetase; acyl-activating enzyme; protein YAL054c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1993 #sequence_revision 08-Sep-1995 #text_change 03-Jun-2002 ACCESSIONS S51967; S30019; S41883; S24608 REFERENCE S51956 !$#authors Bussey, H.; Kaback, D.B.; Zhong, W.; Vo, D.T.; Clark, M.W.; !1Fortin, N.; Hall, J.; Ouellette, B.F.F.; Keng, T.; Barton, !1A.B.; Su, Y.; Davies, C.K.; Storms, R.K. !$#submission submitted to the EMBL Data Library, August 1994 !$#description The sequence of chromosome 1 of Saccharomyces cerevisiae. !$#accession S51967 !'##molecule_type DNA !'##residues 1-713 ##label BUS !'##cross-references EMBL:U12980; NID:g1326053; PIDN:AAC04979.1; !1PID:g595532; GSPDB:GN00001; MIPS:YAL054c REFERENCE S30019 !$#authors de Virgilio, C.; Buerckert, N.; Barth, G.; Neuhaus, J.M.; !1Boller, T.; Wiemken, A. !$#journal Yeast (1992) 8:1043-1051 !$#title Cloning and disruption of a gene required for growth on !1acetate but not on ethanol: the acetyl-coenzyme A synthetase !1gene of Saccharomyces cerevisiae. !$#cross-references MUID:93190633; PMID:1363452 !$#accession S30019 !'##molecule_type DNA !'##residues 1-33,'R',35-713 ##label DEV !'##cross-references EMBL:X66425; NID:g3323; PIDN:CAA47054.1; PID:g3324 !'##note it is uncertain whether Met-1 or Met-24 is the initiator REFERENCE S41882 !$#authors Kratzer, S.; Schueller, W.J. !$#submission submitted to the EMBL Data Library, January 1994 !$#accession S41883 !'##molecule_type DNA !'##residues 1-33,'R',35-59 ##label KRA !'##cross-references EMBL:X76891; NID:g452678; PIDN:CAA54220.1; !1PID:g452680 GENETICS !$#gene SGD:ACS1; FUN44; MIPS:YAL054c !'##cross-references SGD:S0000050; MIPS:YAL054c !$#map_position 1L FUNCTION !$#description EC 6.2.1.1 [validated, MUID:93190633] !$#note ACS1 is glucose repressible and required for the !1assimilation of ethanol and acetate [validated, !1MUID:95377302] CLASSIFICATION #superfamily acetate-CoA ligase; acetate-CoA ligase homology KEYWORDS acid-thiol ligase; coenzyme A; transmembrane protein FEATURE !$185-681 #domain acetate-CoA ligase homology #label ACL\ !$203-219 #domain transmembrane #status predicted #label TMM SUMMARY #length 713 #molecular-weight 79140 #checksum 9921 SEQUENCE /// ENTRY A41043 #type complete TITLE acetate-CoA ligase (EC 6.2.1.1) [validated] - Methanothrix soehngenii ALTERNATE_NAMES acetate thiokinase; acetyl-activating enzyme; acetyl-CoA synthetase; acyl-activating enzyme ORGANISM #formal_name Methanothrix soehngenii DATE 27-Mar-1992 #sequence_revision 20-Aug-1994 #text_change 03-Jun-2002 ACCESSIONS A41043 REFERENCE A41043 !$#authors Eggen, R.I.L.; Geerling, A.C.M.; Boshoven, A.B.P.; de Vos, !1W.M. !$#journal J. Bacteriol. (1991) 173:6383-6389 !$#title Cloning, sequence analysis, and functional expression of the !1acetyl coenzyme A synthetase gene from Methanothrix !1soehngenii in Escherichia coli. !$#cross-references MUID:92011409; PMID:1680850 !$#accession A41043 !'##molecule_type DNA !'##residues 1-672 ##label EGG !'##cross-references GB:M63968; NID:g150031; PIDN:AAA73007.1; !1PID:g150032 GENETICS !$#gene acs !$#start_codon GTG FUNCTION !$#description EC 6.2.1.1 [validated, MUID:92011409] CLASSIFICATION #superfamily acetate-CoA ligase; acetate-CoA ligase homology KEYWORDS acid-thiol ligase; coenzyme A FEATURE !$154-644 #domain acetate-CoA ligase homology #label ACL SUMMARY #length 672 #molecular-weight 75526 #checksum 8929 SEQUENCE /// ENTRY A45736 #type complete TITLE acetate-CoA ligase (EC 6.2.1.1) - Alcaligenes eutrophus ALTERNATE_NAMES acetate thiokinase; acetyl activating enzyme; acetyl-CoA synthetase; acyl-activating enzyme ORGANISM #formal_name Alcaligenes eutrophus DATE 07-Apr-1994 #sequence_revision 20-Aug-1994 #text_change 03-Jun-2002 ACCESSIONS A45736 REFERENCE A45736 !$#authors Priefert, H.; Steinbuechel, A. !$#journal J. Bacteriol. (1992) 174:6590-6599 !$#title Identification and molecular characterization of the acetyl !1coenzyme A synthetase gene (acoE) of Alcaligenes eutrophus. !$#cross-references MUID:93015711; PMID:1356967 !$#accession A45736 !'##molecule_type DNA !'##residues 1-660 ##label PRI !'##cross-references GB:M97217; NID:g141889; PIDN:AAA21945.1; !1PID:g141890 GENETICS !$#gene acoE CLASSIFICATION #superfamily acetate-CoA ligase; acetate-CoA ligase homology KEYWORDS acid-thiol ligase; coenzyme A FEATURE !$134-631 #domain acetate-CoA ligase homology #label ACL SUMMARY #length 660 #molecular-weight 72601 #checksum 1465 SEQUENCE /// ENTRY JX0202 #type complete TITLE long-chain-fatty-acid-CoA ligase (EC 6.2.1.3) - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS JX0202 REFERENCE JX0202 !$#authors Abe, T.; Fujino, T.; Fukuyama, R.; Minoshima, S.; Shimizu, !1N.; Toh, H.; Suzuki, H.; Yamamoto, T. !$#journal J. Biochem. (1992) 111:123-128 !$#title Human long-chain acyl-CoA synthetase: Structure and !1chromosomal location. !$#cross-references MUID:92299644; PMID:1607358 !$#accession JX0202 !'##molecule_type mRNA !'##residues 1-698 ##label ABE !'##cross-references GB:D10040; NID:g219899; PIDN:BAA00931.1; !1PID:g219900 !'##experimental_source liver GENETICS !$#gene GDB:FACL2 !'##cross-references GDB:127357; OMIM:152426 !$#map_position 4q34-4q35 CLASSIFICATION #superfamily human long-chain-fatty-acid-CoA ligase; !1acetate-CoA ligase homology KEYWORDS acid-thiol ligase; coenzyme A; hydrolase FEATURE !$143-681 #domain acetate-CoA ligase homology #label ACL SUMMARY #length 698 #molecular-weight 77943 #checksum 615 SEQUENCE /// ENTRY A39827 #type complete TITLE 4-coumarate-CoA ligase (EC 6.2.1.12) 1 - potato ALTERNATE_NAMES 4-coumaroyl-CoA synthetase ORGANISM #formal_name Solanum tuberosum #common_name potato DATE 20-Mar-1992 #sequence_revision 20-Aug-1994 #text_change 03-Jun-2002 ACCESSIONS A39827 REFERENCE A39827 !$#authors Becker-Andre, M.; Schulze-Lefert, P.; Hahlbrock, K. !$#journal J. Biol. Chem. (1991) 266:8551-8559 !$#title Structural comparison, modes of expression, and putative !1cis-acting elements of the two 4-coumarate:CoA ligase genes !1in potato. !$#cross-references MUID:91217100; PMID:2022667 !$#accession A39827 !'##molecule_type DNA !'##residues 1-545 ##label BEC !'##cross-references GB:M62755; NID:g169573; PIDN:AAA33842.1; !1PID:g169574 CLASSIFICATION #superfamily 4-coumarate-CoA ligase; acetate-CoA ligase !1homology KEYWORDS acid-thiol ligase; coenzyme A; flavonoid biosynthesis FEATURE !$76-535 #domain acetate-CoA ligase homology #label ACL SUMMARY #length 545 #molecular-weight 59619 #checksum 3892 SEQUENCE /// ENTRY B39827 #type complete TITLE 4-coumarate-CoA ligase (EC 6.2.1.12) 2a - potato ALTERNATE_NAMES 4-coumaroyl-CoA synthetase ORGANISM #formal_name Solanum tuberosum #common_name potato DATE 20-Mar-1992 #sequence_revision 20-Aug-1994 #text_change 03-Jun-2002 ACCESSIONS B39827 REFERENCE A39827 !$#authors Becker-Andre, M.; Schulze-Lefert, P.; Hahlbrock, K. !$#journal J. Biol. Chem. (1991) 266:8551-8559 !$#title Structural comparison, modes of expression, and putative !1cis-acting elements of the two 4-coumarate:CoA ligase genes !1in potato. !$#cross-references MUID:91217100; PMID:2022667 !$#accession B39827 !'##molecule_type DNA !'##residues 1-545 ##label BEC CLASSIFICATION #superfamily 4-coumarate-CoA ligase; acetate-CoA ligase !1homology KEYWORDS acid-thiol ligase; coenzyme A; flavonoid biosynthesis FEATURE !$76-535 #domain acetate-CoA ligase homology #label ACL SUMMARY #length 545 #molecular-weight 59625 #checksum 2965 SEQUENCE /// ENTRY T02074 #type complete TITLE 4-coumarate-CoA ligase (EC 6.2.1.12) - common tobacco ALTERNATE_NAMES 4-coumaroyl-CoA synthetase ORGANISM #formal_name Nicotiana tabacum #common_name common tobacco DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS T02074 REFERENCE Z14545 !$#authors Katayama, Y.; Kawai, S.; Morohoshi, N.; Kajita, S. !$#submission submitted to the EMBL Data Library, December 1994 !$#description Cloning and nucleotide sequence of 4-coumarate:coenzyme A !1ligase gene from tobacco. !$#accession T02074 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-542 ##label KAT !'##cross-references EMBL:D43773; PIDN:BAA07828.1 CLASSIFICATION #superfamily 4-coumarate-CoA ligase; acetate-CoA ligase !1homology KEYWORDS acid-thiol ligase; coenzyme A; flavonoid biosynthesis FEATURE !$73-532 #domain acetate-CoA ligase homology #label ACL SUMMARY #length 542 #molecular-weight 59450 #checksum 1780 SEQUENCE /// ENTRY S01667 #type complete TITLE 4-coumarate-CoA ligase (EC 6.2.1.12) (clone pc4CL-1) - parsley ALTERNATE_NAMES 4-coumaroyl-CoA synthetase ORGANISM #formal_name Petroselinum crispum #common_name parsley DATE 30-Sep-1989 #sequence_revision 20-Aug-1994 #text_change 03-Jun-2002 ACCESSIONS S01667 REFERENCE S01667 !$#authors Lozoya, E.; Hoffmann, H.; Douglas, C.; Schulz, W.; Scheel, !1D.; Hahlbrock, K. !$#journal Eur. J. Biochem. (1988) 176:661-667 !$#title Primary structures and catalytic properties of isoenzymes !1encoded by the two 4-coumarate:CoA ligase genes in parsley. !$#cross-references MUID:89005119; PMID:3169018 !$#accession S01667 !'##molecule_type mRNA !'##residues 1-544 ##label LOZ !'##cross-references EMBL:X13324; NID:g20431; PIDN:CAA31696.1; !1PID:g20432 GENETICS !$#gene 4CL-1 CLASSIFICATION #superfamily 4-coumarate-CoA ligase; acetate-CoA ligase !1homology KEYWORDS acid-thiol ligase; coenzyme A; flavonoid biosynthesis FEATURE !$74-533 #domain acetate-CoA ligase homology #label ACL SUMMARY #length 544 #molecular-weight 59825 #checksum 3381 SEQUENCE /// ENTRY JU0311 #type complete TITLE 4-coumarate-CoA ligase (EC 6.2.1.12) - rice ALTERNATE_NAMES 4-coumaroyl-CoA synthetase ORGANISM #formal_name Oryza sativa #common_name rice DATE 30-Jun-1992 #sequence_revision 20-Aug-1994 #text_change 03-Jun-2002 ACCESSIONS JU0311 REFERENCE JU0311 !$#authors Zhao, Y.; Kung, S.D.; Dube, S.K. !$#journal Nucleic Acids Res. (1990) 18:6144 !$#title Nucleotide sequence of rice 4-coumarate:CoA ligase gene, !14-CL.1. !$#cross-references MUID:91045096; PMID:2235510 !$#accession JU0311 !'##status translation not shown !'##molecule_type DNA !'##residues 1-563 ##label ZHA !'##cross-references EMBL:X52623; NID:g20160; PIDN:CAA36850.1; !1PID:g20161 !'##experimental_source strain Japonica GENETICS !$#gene 4-CL.1 !$#introns 351/3; 418/1; 489/2; 520/3 CLASSIFICATION #superfamily 4-coumarate-CoA ligase; acetate-CoA ligase !1homology KEYWORDS acid-thiol ligase; coenzyme A; flavonoid biosynthesis FEATURE !$87-549 #domain acetate-CoA ligase homology #label ACL SUMMARY #length 563 #molecular-weight 60840 #checksum 7783 SEQUENCE /// ENTRY S23437 #type complete TITLE Photinus-luciferin 4-monooxygenase (ATP-hydrolysing) (EC 1.13.12.7) [similarity] - Japanese firefly ALTERNATE_NAMES firefly luciferase ORGANISM #formal_name Luciola lateralis #common_name Japanese firefly DATE 22-Jan-1993 #sequence_revision 20-Aug-1994 #text_change 02-Aug-2002 ACCESSIONS S23437; S57417 REFERENCE S23437 !$#authors Tatsumi, H.; Kajiyama, N.; Nakano, E. !$#journal Biochim. Biophys. Acta (1992) 1131:161-165 !$#title Molecular cloning and expression in Escherichia coli of a !1cDNA clone encoding luciferase of a firefly, Luciola !1lateralis. !$#cross-references MUID:92305054; PMID:1610896 !$#accession S23437 !'##molecule_type mRNA !'##residues 1-548 ##label TAT !'##cross-references EMBL:X66919; NID:g9526; PIDN:CAA47358.1; PID:g9527 REFERENCE S57417 !$#authors Cho, K.; Choi, Y.; Boo, K. !$#submission submitted to the EMBL Data Library, June 1995 !$#description Molecular cloning of gene for luciferase in Luciola !1lateralis. !$#accession S57417 !'##molecule_type DNA !'##residues 1-4,'D',6-14,'K',16-145,'N',147-175,'P',177-505,'G',507-548 !1##label CHO !'##cross-references EMBL:Z49891; NID:g871400; PIDN:CAA90072.1; !1PID:g871401 GENETICS !$#introns 44/3; 114/1; 225/2; 332/2; 450/3; 506/1 FUNCTION !$#description catalyzes the irreversible reaction of luciferin with oxygen !1and ATP to produce oxidized luciferin, AMP, pyrophosphate, !1carbon dioxide, and light !$#note magnesium is required; color of emitted light varies among !1species from green to yellow CLASSIFICATION #superfamily 4-coumarate-CoA ligase; acetate-CoA ligase !1homology KEYWORDS ATP; luminescence; magnesium; monooxygenase; oxidoreductase; !1peroxisome FEATURE !$73-537 #domain acetate-CoA ligase homology #label ACL SUMMARY #length 548 #molecular-weight 60125 #checksum 2707 SEQUENCE /// ENTRY JS0181 #type complete TITLE Photinus-luciferin 4-monooxygenase (ATP-hydrolysing) (EC 1.13.12.7) [similarity] - Genji firefly ALTERNATE_NAMES firefly luciferase ORGANISM #formal_name Luciola cruciata #common_name Genji firefly DATE 07-Jun-1990 #sequence_revision 20-Aug-1994 #text_change 02-Aug-2002 ACCESSIONS JS0181 REFERENCE JS0181 !$#authors Masuda, T.; Tatsumi, H.; Nakano, E. !$#journal Gene (1989) 77:265-270 !$#title Cloning and sequence analysis of cDNA for luciferase of a !1Japanese firefly, Luciola cruciata. !$#cross-references MUID:89326143; PMID:2473944 !$#accession JS0181 !'##molecule_type mRNA !'##residues 1-548 ##label MAS !'##cross-references GB:M26194; NID:g159050; PIDN:AAA29135.1; !1PID:g159051 COMMENT This protein catalyzes the oxidation of luciferin in the !1presence of ATP, oxygen, and magnesium ion. This oxidation !1results in the production of light; the colors of the light !1vary among species from green to yellow. CLASSIFICATION #superfamily 4-coumarate-CoA ligase; acetate-CoA ligase !1homology KEYWORDS ATP; luminescence; monooxygenase; oxidoreductase FEATURE !$73-537 #domain acetate-CoA ligase homology #label ACL SUMMARY #length 548 #molecular-weight 60017 #checksum 6022 SEQUENCE /// ENTRY A26772 #type complete TITLE Photinus-luciferin 4-monooxygenase (ATP-hydrolysing) (EC 1.13.12.7) [similarity] - common eastern firefly ALTERNATE_NAMES firefly luciferase ORGANISM #formal_name Photinus pyralis #common_name common eastern firefly DATE 19-Nov-1988 #sequence_revision 20-Aug-1994 #text_change 02-Aug-2002 ACCESSIONS A26772 REFERENCE A26772 !$#authors de Wet, J.R.; Wood, K.V.; DeLuca, M.; Helinski, D.R.; !1Subramani, S. !$#journal Mol. Cell. Biol. (1987) 7:725-737 !$#title Firefly luciferase gene: structure and expression in !1mammalian cells. !$#cross-references MUID:87144243; PMID:3821727 !$#accession A26772 !'##molecule_type DNA !'##residues 1-550 ##label DEW !'##cross-references GB:M15077; NID:g160793; PIDN:AAA29795.1; !1PID:g160794 !'##note the authors translated the codon CAA for residue 134 as Glu COMMENT This protein catalyzes the oxidation of luciferin in the !1presence of ATP, oxygen, and magnesium ion. This oxidation !1results in the production of light; the colors of the light !1vary among species from green to yellow. GENETICS !$#introns 42/3; 112/1; 223/2; 330/2; 448/3; 504/1 CLASSIFICATION #superfamily 4-coumarate-CoA ligase; acetate-CoA ligase !1homology KEYWORDS ATP; luminescence; monooxygenase; oxidoreductase FEATURE !$71-535 #domain acetate-CoA ligase homology #label ACL\ !$548-550 #region peroxisome/glyoxysome location signal !8(S-[RKH]-L) motif SUMMARY #length 550 #molecular-weight 60745 #checksum 3361 SEQUENCE /// ENTRY SYECEB #type complete TITLE 2,3-dihydroxybenzoate-[carrier protein] ligase (EC 6.2.1.-) entE - Escherichia coli (strain K-12) ALTERNATE_NAMES 2,3-dihydroxybenzoate-AMP ligase [misnomer]; dihydroxybenzoic acid-activating enzyme component E; enterobactin synthetase component E; enterochelin synthetase component E ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 21-Nov-1997 #text_change 01-Mar-2002 ACCESSIONS H64792; A48308; A32047; I41058; S08076 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64792 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-536 ##label BLAT !'##cross-references GB:AE000165; GB:U00096; NID:g1786808; !1PIDN:AAC73695.1; PID:g1786810; UWGP:b0594 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A48308 !$#authors Staab, J.F.; Elkins, M.F.; Earhart, C.F. !$#journal FEMS Microbiol. Lett. (1989) 59:15-19 !$#title Nucleotide sequence of the Escherichia coli entE gene. !$#cross-references MUID:89290355; PMID:2525505 !$#note in MedLine 89290355 this citation is erroneously given as !1volume 50 rather than volume 59 !$#accession A48308 !'##molecule_type DNA !'##residues 1-368,'ECRRKSTAAR',379-536 ##label STA !'##cross-references GB:M27490; EMBL:X15058; NID:g41345; !1PIDN:CAA33158.1; PID:g41346 REFERENCE A91904 !$#authors Liu, J.; Duncan, K.; Walsh, C.T. !$#journal J. Bacteriol. (1989) 171:791-798 !$#title Nucleotide sequence of a cluster of Escherichia coli !1enterobactin biosynthesis genes: identification of entA and !1purification of its product 2,3-dihydro-2, !13-dihydroxybenzoate dehydrogenase. !$#cross-references MUID:89123155; PMID:2521622 !$#accession A32047 !'##molecule_type DNA !'##residues 393-536 ##label LIU !'##cross-references GB:M24148; NID:g304949; PIDN:AAA16101.1; !1PID:g450380 COMMENT The enzymatic steps in the condensation of L-serine and 2, !13-dihydroxybenzoic acid to form enterobactin are not !1completely characterized chemically. The identification of !1this enzyme activity is based on its recognized homology !1with 4-coumarate-CoA ligase and by analogy with the enzyme !1activities of gramicidin S synthetase. COMMENT The formation of 2,3-dihydroxybenzoyl-AMP has been observed. !1The rapid reaction of this intermediate either with a thiol !1or with a serine (presumably attached to phosphopantetheine !1on the carrier protein) to release AMP, has also been !1observed. GENETICS !$#gene entE !$#map_position 14 min FUNCTION !$#description catalyzes the formation of 2,3-dihydroxybenzoyl-[carrier !1protein], AMP and pyrophosphate from 2,3-dihydroxybenzoic !1acid and ATP !$#pathway enterobactin biosynthesis !$#note this is one component of a membrane-bound multienzyme !1complex that catalyzes the condensation of L-serine and 2, !13-dihydroxybenzoate to form enterobactin (or enterochelin) !1used to chelate iron for transport into the cell CLASSIFICATION #superfamily 4-coumarate-CoA ligase; acetate-CoA ligase !1homology KEYWORDS acid-thiol ligase; enterobactin biosynthesis; !1membrane-associated complex FEATURE !$69-526 #domain acetate-CoA ligase homology #label ACL SUMMARY #length 536 #molecular-weight 59112 #checksum 5363 SEQUENCE /// ENTRY D69615 #type complete TITLE 2,3-dihydroxybenzoate-[carrier protein] ligase (EC 6.2.1.-) dhbE - Bacillus subtilis ALTERNATE_NAMES 2,3-dihydroxybenzoate-AMP ligase [misnomer]; dihydroxybenzoic acid-activating enzyme component E; EntE protein homolog; enterobactin synthetase component E; enterochelin synthetase component E ORGANISM #formal_name Bacillus subtilis DATE 05-Dec-1997 #sequence_revision 10-Jul-1998 #text_change 16-Jun-2000 ACCESSIONS D69615; PN0684 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D69615 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-539 ##label KUN !'##cross-references GB:Z99120; GB:AL009126; NID:g2635613; !1PIDN:CAB15188.1; PID:g2635695 !'##experimental_source strain 168 REFERENCE PN0683 !$#authors Adams, R.; Schumann, W. !$#journal Gene (1993) 133:119-121 !$#title Cloning and mapping of the Bacillus subtilis locus !1homologous to Escherichia coli ent genes. !$#cross-references MUID:94040785; PMID:8224884 !$#accession PN0684 !'##molecule_type DNA !'##residues 341-359,'I',361-533 ##label ADA !'##cross-references GB:L08645; NID:g348059; PIDN:AAA79759.1; !1PID:g1030072 COMMENT For discussion of the enzyme activity see PIR:SYECEB. GENETICS !$#gene dhbE FUNCTION !$#description catalyzes the formation of 2,3-dihydroxybenzoyl-[carrier !1protein], AMP and pyrophosphate from 2,3-dihydroxybenzoic !1acid and ATP !$#pathway enterobactin biosynthesis CLASSIFICATION #superfamily 4-coumarate-CoA ligase; acetate-CoA ligase !1homology KEYWORDS acid-thiol ligase; enterobactin biosynthesis; !1membrane-associated complex FEATURE !$71-525 #domain acetate-CoA ligase homology #label ACL SUMMARY #length 539 #molecular-weight 59928 #checksum 5040 SEQUENCE /// ENTRY S41589 #type complete TITLE long-chain-fatty-acid-CoA ligase (EC 6.2.1.3) [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES acyl coenzyme A synthetase ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS E64941; S41589; A45062; S42848 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64941 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-561 ##label BLAT !'##cross-references GB:AE000275; GB:U00096; NID:g1788106; !1PIDN:AAC74875.1; PID:g1788107; UWGP:b1805 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S41588 !$#authors Fulda, M.; Heinz, E.; Wolter, F.P. !$#journal Mol. Gen. Genet. (1994) 242:241-249 !$#title The fadD gene of Escherichia coli K12 is located close to !1rnd at 39.6 min of the chromosomal map and is a new member !1of the AMP-binding protein family. !$#cross-references MUID:94150456; PMID:8107670 !$#accession S41589 !'##molecule_type DNA !'##residues 1-561 ##label FUL !'##cross-references GB:X70994; NID:g433478; PIDN:CAA50321.1; !1PID:g581070 REFERENCE A45062 !$#authors Black, P.N.; DiRusso, C.C.; Metzger, A.K.; Heimert, T.L. !$#journal J. Biol. Chem. (1992) 267:25513-25520 !$#title Cloning, sequencing, and expression of the fadD gene of !1Escherichia coli encoding acyl coenzyme A synthetase. !$#cross-references MUID:93094273; PMID:1460045 !$#accession A45062 !'##status preliminary !'##molecule_type DNA; protein !'##residues 1-33,'GALRRSTCVCEY',46,'GGNDL',52-467, !1'TRLKMSSCSMVAYRKSRLLAYLP',491-495,'G',497-554,'QSGQ' ##label !1BLA !'##cross-references GB:L02649; NID:g145905; PIDN:AAA23752.1; !1PID:g145906 !'##note sequence extracted from NCBI backbone (NCBIN:120300, !1NCBIP:120301) GENETICS !$#gene fadD !$#start_codon TTG FUNCTION !$#description EC 6.2.1.3 [validated, MUID:94150456]; catalyzes the !1formation of fatty acyl-CoA by a two-step process, in the !1first step fatty acid and ATP form an acyl adenylate bound !1to the protein, while pyrophosphate is released, in the !1second step the acyl group is transferred to the sulfhydryl !1group of CoA and AMP is released !$#pathway lipid metabolism CLASSIFICATION #superfamily 4-coumarate-CoA ligase; acetate-CoA ligase !1homology KEYWORDS acid-thiol ligase; ATP; coenzyme A; lipid metabolism FEATURE !$1-561 #product long-chain-fatty-acid-CoA-ligase #status !8experimental #label MAT\ !$70-549 #domain acetate-CoA ligase homology #label ACL SUMMARY #length 561 #molecular-weight 62332 #checksum 7132 SEQUENCE /// ENTRY SYECSA #type complete TITLE succinate-CoA ligase (ADP-forming) (EC 6.2.1.5) alpha chain - Escherichia coli (strain K-12) ALTERNATE_NAMES succinyl-CoA synthetase (ADP-forming) alpha chain ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 03-Jun-2002 ACCESSIONS A90499; S61287; H64808; B24090 REFERENCE A90499 !$#authors Buck, D.; Spencer, M.E.; Guest, J.R. !$#journal Biochemistry (1985) 24:6245-6252 !$#title Primary structure of the succinyl-CoA synthetase of !1Escherichia coli. !$#cross-references MUID:86104124; PMID:3002435 !$#accession A90499 !'##molecule_type DNA !'##residues 1-289 ##label BUC !'##cross-references GB:J01619; NID:g146195; PIDN:AAA23900.1; !1PID:g146204 REFERENCE S61284 !$#authors Freestone, P.; Grant, S.; Toth, I.; Norris, V. !$#journal Mol. Microbiol. (1995) 15:573-580 !$#title Identification of phosphoproteins in Escherichia coli. !$#cross-references MUID:95302968; PMID:7783627 !$#accession S61287 !'##status preliminary !'##molecule_type protein !'##residues 1-11 ##label FRE REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64808 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-289 ##label BLAT !'##cross-references GB:AE000176; GB:U00096; NID:g1786947; !1PIDN:AAC73823.1; PID:g1786949; UWGP:b0729 !'##experimental_source strain K-12, substrain MG1655 COMMENT The alpha chain binds ATP and catalyzes the transfer of a !1phosphate group to one of its histidine residues. GENETICS !$#gene sucD !$#map_position 17 min COMPLEX heterotetramer; two alpha chains and two beta chains FUNCTION !$#description catalyzes the stepwise ATP-driven synthesis of succinyl-CoA !1from succinate and CoA !$#note phosphoryl enzyme and enzyme-bound succinyl phosphate !1intermediates are involved !$#note magnesium required CLASSIFICATION #superfamily succinate-CoA ligase (ADP-forming) alpha chain KEYWORDS acid-thiol ligase; ATP; coenzyme A; heterotetramer; !1phosphohistidine; phosphoprotein; tricarboxylic acid cycle FEATURE !$247 #active_site His (phosphohistidine intermediate) !8#status experimental SUMMARY #length 289 #molecular-weight 29777 #checksum 2100 SEQUENCE /// ENTRY SYRTSA #type complete TITLE succinate-CoA ligase (GDP-forming) (EC 6.2.1.4) alpha chain precursor - rat ALTERNATE_NAMES succinyl-CoA synthetase (GDP-forming) alpha chain ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 03-Jun-2002 ACCESSIONS A28962 REFERENCE A28962 !$#authors Henning, W.D.; Upton, C.; McFadden, G.; Majumdar, R.; !1Bridger, W.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:1432-1436 !$#title Cloning and sequencing of the cytoplasmic precursor to the !1alpha-subunit of rat liver mitochondrial succinyl-CoA !1synthetase. !$#cross-references MUID:88144451; PMID:3422742 !$#accession A28962 !'##molecule_type mRNA !'##residues 1-333 ##label HEN !'##cross-references GB:J03621; NID:g204355; PIDN:AAA41233.1; !1PID:g204356 !'##experimental_source liver COMMENT This enzyme catalyzes the stepwise synthesis of succinyl-CoA !1from succinate, CoA, and GTP in the presence of magnesium !1ion, involving phosphoryl enzyme and enzyme-bound succinyl !1phosphate as intermediates. The active enzyme is an !1alpha-beta dimer. CLASSIFICATION #superfamily succinate-CoA ligase (ADP-forming) alpha chain KEYWORDS acid-thiol ligase; ATP; coenzyme A; heterodimer; !1mitochondrion; phosphohistidine; phosphoprotein; !1tricarboxylic acid cycle FEATURE !$1-27 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$28-333 #product succinate-CoA ligase alpha chain #status !8experimental #label MAT\ !$286 #active_site His (phosphohistidine intermediate) !8#status experimental SUMMARY #length 333 #molecular-weight 35031 #checksum 2657 SEQUENCE /// ENTRY SYTWSA #type complete TITLE succinate-CoA ligase (ADP-forming) (EC 6.2.1.5) alpha chain [validated] - Thermus aquaticus ALTERNATE_NAMES succinyl-CoA synthetase alpha chain ORGANISM #formal_name Thermus aquaticus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 03-Jun-2002 ACCESSIONS S15951; S12138; S03675 REFERENCE S15948 !$#authors Nishiyama, M.; Horinouchi, S.; Beppu, T. !$#journal Mol. Gen. Genet. (1991) 226:1-9 !$#title Characterization of an operon encoding succinyl-CoA !1synthetase and malate dehydrogenase from Thermus flavus !1AT-62 and its expression in Escherichia coli. !$#cross-references MUID:91238680; PMID:2034208 !$#accession S15951 !'##molecule_type DNA !'##residues 1-288 ##label NIS !'##cross-references EMBL:X54073; NID:g48174; PIDN:CAA38007.1; !1PID:g48178 !'##experimental_source strain AT-62 REFERENCE S12137 !$#authors Nicholls, D.J.; Sundaram, T.K.; Atkinson, T.; Minton, N.P. !$#journal FEMS Microbiol. Lett. (1990) 70:7-14 !$#title Cloning and nucleotide sequences of the mdh and sucD genes !1from Thermus aquaticus B. !$#accession S12138 !'##molecule_type DNA !'##residues 1-288 ##label NIC1 !'##cross-references EMBL:X56033; NID:g48077; PIDN:CAA39507.1; !1PID:g581794 REFERENCE S03675 !$#authors Nicholls, D.J.; Sundaram, T.K.; Atkinson, T.; Minton, N.P. !$#journal Nucleic Acids Res. (1988) 16:9858 !$#title Nucleotide sequence of the succinyl-CoA synthetase !1alpha-subunit from Thermus aquaticus B. !$#cross-references MUID:89041573; PMID:3186449 !$#accession S03675 !'##molecule_type DNA !'##residues 1-183,'TG',186-288 ##label NIC2 !'##cross-references GB:M35832 !'##note the authors translated the codon CAC for residue 130 as Glu, !1CTA for residue 131 as Glu, CCC for residue 132 as Thr, CGG !1for residue 157 as Thr, CAC for residue 158 as Tyr, AGG for !1residue 183 as Ile, CGG for residue 184 as Thr, and CTA for !1residue 185 as Gly; the sequence shown follows the authors' !1translation GENETICS !$#gene sucD; scsA !$#start_codon GTG FUNCTION !$#description EC 6.2.1.5 [validated, MUID:91238680]; catalyzes the !1ATP-driven synthesis of succinyl-CoA from succinate and CoA CLASSIFICATION #superfamily succinate-CoA ligase (ADP-forming) alpha chain KEYWORDS acid-thiol ligase; ATP; coenzyme A; phosphohistidine; !1phosphoprotein FEATURE !$246 #active_site His (phosphohistidine intermediate) !8#status predicted SUMMARY #length 288 #molecular-weight 29822 #checksum 980 SEQUENCE /// ENTRY SYECSB #type complete TITLE succinate-CoA ligase (ADP-forming) (EC 6.2.1.5) beta chain - Escherichia coli (strain K-12) ALTERNATE_NAMES succinyl-CoA synthetase (ADP-forming) beta chain ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 03-Jun-2002 ACCESSIONS A24090; G64808 REFERENCE A90499 !$#authors Buck, D.; Spencer, M.E.; Guest, J.R. !$#journal Biochemistry (1985) 24:6245-6252 !$#title Primary structure of the succinyl-CoA synthetase of !1Escherichia coli. !$#cross-references MUID:86104124; PMID:3002435 !$#accession A24090 !'##molecule_type DNA !'##residues 1-388 ##label BUC !'##cross-references GB:J01619; GB:K00542; GB:M11121; NID:g146195; !1PIDN:AAA23899.1; PID:g146203 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64808 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-388 ##label BLAT !'##cross-references GB:AE000176; GB:U00096; NID:g1786947; !1PIDN:AAC73822.1; PID:g1786948; UWGP:b0728 !'##experimental_source strain K-12, substrain MG1655 COMMENT The beta chain contains the attachment sites for succinate !1and CoA. GENETICS !$#gene sucC !$#map_position 17 min COMPLEX heterotetramer; two alpha chains and two beta chains FUNCTION !$#description catalyzes the stepwise ATP-driven synthesis of succinyl-CoA !1from succinate and CoA !$#note phosphoryl enzyme and enzyme-bound succinyl phosphate !1intermediates are involved !$#note magnesium required CLASSIFICATION #superfamily succinate-CoA ligase (ADP-forming) beta chain KEYWORDS acid-thiol ligase; coenzyme A; tricarboxylic acid cycle SUMMARY #length 388 #molecular-weight 41392 #checksum 925 SEQUENCE /// ENTRY AJECNA #type complete TITLE aspartate-ammonia ligase (EC 6.3.1.1) - Escherichia coli (strain K-12) ALTERNATE_NAMES asparagine synthetase A ORGANISM #formal_name Escherichia coli DATE 02-Apr-1982 #sequence_revision 02-Apr-1982 #text_change 03-Jun-2002 ACCESSIONS A01191; A91504; PS0346; I52886; A65178 REFERENCE A01191 !$#authors Nakamura, M.; Yamada, M.; Hirota, Y.; Sugimoto, K.; Oka, A.; !1Takanami, M. !$#journal Nucleic Acids Res. (1981) 9:4669-4676 !$#title Nucleotide sequence of the asnA gene coding for asparagine !1synthetase of E.coli K-12. !$#cross-references MUID:82059491; PMID:6117826 !$#accession A01191 !'##molecule_type DNA !'##residues 1-330 ##label NAK !'##cross-references GB:J01657; GB:X02820; NID:g147023; PIDN:AAA24248.1; !1PID:g147026 !'##experimental_source strain K12 REFERENCE A91504 !$#authors Buhk, H.J.; Messer, W. !$#journal Gene (1983) 24:265-279 !$#title The replication origin region of Escherichia coli: !1nucleotide sequence and functional units. !$#cross-references MUID:84059088; PMID:6357950 !$#accession A91504 !'##molecule_type DNA !'##residues 1-330 ##label BUH !'##cross-references GB:K00826; NID:g147029; PIDN:AAA24253.1; !1PID:g147033 REFERENCE PS0346 !$#authors Sugiyama, A.; Kato, H.; Nishioka, T.; Oda, J. !$#journal Biosci. Biotechnol. Biochem. (1992) 56:376-379 !$#title Overexpression and purification of asparagine synthetase !1from Escherichia coli. !$#cross-references MUID:92330004; PMID:1369484 !$#accession PS0346 !'##molecule_type protein !'##residues 1-5 ##label SUG REFERENCE I52886 !$#authors Hirota, Y.; Yasuda, S.; Yamada, M.; Nishimura, A.; Sugimoto, !1K.; Sugisaki, H.; Oka, A.; Takanami, M. !$#journal Cold Spring Harb. Symp. Quant. Biol. (1979) 43:129-138 !$#title Structural and functional properties of the Escherichia coli !1origin of DNA replication. !$#cross-references MUID:80002740; PMID:383377 !$#accession I52886 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-253 ##label RES !'##cross-references GB:M10679; NID:g147027; PIDN:AAA24249.1; !1PID:g147028 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65178 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-330 ##label BLAT !'##cross-references GB:AE000451; GB:U00096; NID:g2367272; !1PIDN:AAC76767.1; PID:g1790183; UWGP:b3744 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene asnA !$#map_position 84 min FUNCTION !$#description catalyzes the transfer of ammonium to aspartic acid, in the !1presence of ATP, to form asparagine CLASSIFICATION #superfamily aspartate-ammonia ligase KEYWORDS ligase SUMMARY #length 330 #molecular-weight 36650 #checksum 6080 SEQUENCE /// ENTRY AJHUQ #type complete TITLE glutamate-ammonia ligase (EC 6.3.1.2) - human ALTERNATE_NAMES glutamine synthetase ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1991 #sequence_revision 01-Dec-2000 #text_change 03-Jun-2002 ACCESSIONS S18455; S00673; I53634; T47179; S15485 REFERENCE S18455 !$#authors van den Hoff, M.J.B.; Geerts, W.J.C.; Das, A.T.; Moorman, !1A.F.M.; Lamers, W.H. !$#journal Biochim. Biophys. Acta (1991) 1090:249-251 !$#title cDNA sequence of the long mRNA for human glutamine synthase. !$#cross-references MUID:92031701; PMID:1681907 !$#accession S18455 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-373 ##label HOF !'##cross-references EMBL:X59834; NID:g31830; PIDN:CAA42495.1; !1PID:g31831 REFERENCE S00673 !$#authors Gibbs, C.S.; Campbell, K.E.; Wilson, R.H. !$#journal Nucleic Acids Res. (1987) 15:6293 !$#title Sequence of a human glutamine synthetase cDNA. !$#cross-references MUID:87316885; PMID:2888076 !$#accession S00673 !'##molecule_type mRNA !'##residues 1-313,'G',315-321,'SI',324-346,'D',348-373 ##label GIB !'##cross-references EMBL:Y00387; NID:g31832; PIDN:CAA68457.1; !1PID:g31833 REFERENCE I53634 !$#authors Christa, L.; Simon, M.T.; Flinois, J.P.; Gebhardt, R.; !1Brechot, C.; Lasserre, C. !$#journal Gastroenterology (1994) 106:1312-1320 !$#title Overexpression of glutamine synthetase in human primary !1liver cancer. !$#cross-references MUID:94229472; PMID:7909780 !$#accession I53634 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-321,'SI',324-346,'D',348-373 ##label RES !'##cross-references GB:S70290; NID:g546602; PIDN:AAB30693.1; !1PID:g546603 REFERENCE Z24378 !$#authors Koehrer, K.; Beyer, A.; Mewes, H.W.; Weil, B.; Wiemann, S. !$#submission submitted to the Protein Sequence Database, March 2000 !$#accession T47179 !'##status preliminary !'##molecule_type mRNA !'##residues 1-109,'GVL' ##label AAA !'##cross-references EMBL:AL161952 !'##experimental_source adult testis; clone DKFZp434M0813 GENETICS !$#gene GDB:GLUL; GLNS !'##cross-references GDB:120626; OMIM:138290 !$#map_position 1q31-1q31 !$#note DKFZp434M0813.1 CLASSIFICATION #superfamily glutamate-ammonia ligase KEYWORDS ligase SUMMARY #length 373 #molecular-weight 42165 #checksum 2536 SEQUENCE /// ENTRY AJHYQ #type complete TITLE glutamate-ammonia ligase (EC 6.3.1.2) - Chinese hamster ALTERNATE_NAMES glutamine synthetase ORGANISM #formal_name Cricetulus griseus #common_name Chinese hamster DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Jun-2002 ACCESSIONS A23524 REFERENCE A23524 !$#authors Hayward, B.E.; Hussain, A.; Wilson, R.H.; Lyons, A.; !1Woodcock, V.; McIntosh, B.; Harris, T.J.R. !$#journal Nucleic Acids Res. (1986) 14:999-1008 !$#title The cloning and nucleotide sequence of cDNA for an amplified !1glutamine synthetase gene from the Chinese hamster. !$#cross-references MUID:86120385; PMID:2868445 !$#accession A23524 !'##molecule_type mRNA !'##residues 1-373 ##label HAY !'##cross-references GB:X03459 CLASSIFICATION #superfamily glutamate-ammonia ligase KEYWORDS ligase SUMMARY #length 373 #molecular-weight 42137 #checksum 855 SEQUENCE /// ENTRY AJRTQ #type complete TITLE glutamate-ammonia ligase (EC 6.3.1.2) - rat ALTERNATE_NAMES glutamine synthetase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Jun-2002 ACCESSIONS S01242; JN0040; A43754 REFERENCE S01242 !$#authors van de Zande, L.; Labruyere, W.T.; Smaling, M.M.; Moorman, !1A.F.M.; Wilson, R.H.; Charles, R.; Lamers, W.H. !$#journal Nucleic Acids Res. (1988) 16:7726 !$#title Nucleotide sequence of rat glutamine synthetase mRNA. !$#cross-references MUID:88319964; PMID:2901064 !$#accession S01242 !'##molecule_type mRNA !'##residues 1-373 ##label VAN !'##cross-references GB:X07921; NID:g57576; PIDN:CAA30754.1; PID:g57577 REFERENCE JN0040 !$#authors van de Zande, L.; Labruyere, W.T.; Arnberg, A.C.; Wilson, !1R.H.; van den Bogaert, A.J.W.; Das, A.T.; van Oorschot, !1D.A.J.; Frijters, C.; Charles, R.; Moorman, A.F.M.; Lamers, !1W.H. !$#journal Gene (1990) 87:225-232 !$#title Isolation and characterization of the rat glutamine !1synthetase-encoding gene. !$#cross-references MUID:90236314; PMID:1970548 !$#accession JN0040 !'##molecule_type mRNA !'##residues 1-373 ##label VA2 !'##cross-references GB:M29579; GB:M28542; NID:g204401; PIDN:AAA65095.1; !1PID:g204402 REFERENCE A43754 !$#authors Mill, J.F.; Mearow, K.M.; Purohit, H.J.; Haleem-Smith, H.; !1King, R.; Freese, E. !$#journal Brain Res. Mol. Brain Res. (1991) 9:197-207 !$#title Cloning and functional characterization of the rat glutamine !1synthetase gene. !$#cross-references MUID:91232386; PMID:1674354 !$#accession A43754 !'##status preliminary !'##molecule_type mRNA !'##residues 1-127,'R',129-373 ##label MIL !'##cross-references GB:M91652; NID:g204348; PIDN:AAC42038.1; !1PID:g204349 COMMENT This enzyme catalyzes the synthesis of glutamine from !1glutamate and ammonia at the expense of hydrolysis of ATP to !1ADP. CLASSIFICATION #superfamily glutamate-ammonia ligase KEYWORDS ligase SUMMARY #length 373 #molecular-weight 42267 #checksum 292 SEQUENCE /// ENTRY AJMSQ #type complete TITLE glutamate-ammonia ligase (EC 6.3.1.2) - mouse ALTERNATE_NAMES glutamine synthetase ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Jun-2002 ACCESSIONS S04991 REFERENCE S04991 !$#authors Kuo, C.F.; Darnell Jr., J.E. !$#journal J. Mol. Biol. (1989) 208:45-56 !$#title Mouse glutamine synthetase is encoded by a single gene that !1can be expressed in a localized fashion. !$#cross-references MUID:89362463; PMID:2475638 !$#accession S04991 !'##molecule_type DNA !'##residues 1-373 ##label KUO !'##cross-references GB:X16314; NID:g758149; PIDN:CAA34381.1; !1PID:g758150 CLASSIFICATION #superfamily glutamate-ammonia ligase KEYWORDS ligase SUMMARY #length 373 #molecular-weight 42190 #checksum 9838 SEQUENCE /// ENTRY AJMSQ3 #type complete TITLE glutamate-ammonia ligase (EC 6.3.1.2) - mouse ALTERNATE_NAMES glutamine synthetase ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Sep-1991 #sequence_revision 13-Mar-1997 #text_change 03-Jun-2002 ACCESSIONS I49706; A35579 REFERENCE I49706 !$#authors Bhandari, B.; Roesler, W.J.; DeLisio, K.D.; Klemm, D.J.; !1Ross, N.S.; Miller, R.E. !$#journal J. Biol. Chem. (1991) 266:7784-7792 !$#title A functional promoter flanks in intronless glutamine !1synthetase gene. !$#cross-references MUID:91210303; PMID:1673462 !$#accession I49706 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-371 ##label RES !'##cross-references GB:M60803; NID:g193654; PIDN:AAA37746.1; !1PID:g193655 REFERENCE A35579 !$#authors Bhandari, B.; Beckwith, K.D.; Miller, R.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:5789-5793 !$#title Cloning, nucleotide sequence, and potential regulatory !1elements of the glutamine synthetase gene from murine 3T3-L1 !1adipocytes. !$#cross-references MUID:88320329; PMID:2901089 !$#accession A35579 !'##molecule_type DNA !'##residues 1-33,'N',35-200 ##label BHA !'##cross-references GB:J03820 !'##experimental_source 3T3-L1 adipocytes CLASSIFICATION #superfamily glutamate-ammonia ligase KEYWORDS ligase SUMMARY #length 371 #molecular-weight 42018 #checksum 3883 SEQUENCE /// ENTRY AJCHQ #type complete TITLE glutamate-ammonia ligase (EC 6.3.1.2) - chicken ALTERNATE_NAMES glutamine synthetase ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Jun-2002 ACCESSIONS JQ0025; A44095 REFERENCE JQ0025 !$#authors Pu, H.; Young, A.P. !$#journal Gene (1989) 81:169-175 !$#title The structure of the chicken glutamine synthetase-encoding !1gene. !$#cross-references MUID:90034178; PMID:2572512 !$#accession JQ0025 !'##molecule_type mRNA !'##residues 1-373 ##label PUH !'##cross-references GB:M29076; NID:g211814; PIDN:AAA48783.1; !1PID:g211815 REFERENCE A44095 !$#authors Campbell, J.W.; Smith Jr., D.D. !$#journal Mol. Biol. Evol. (1992) 9:787-805 !$#title Metabolic compartmentation of vertebrate glutamine !1synthetase: putative mitochondrial targeting signal in avian !1liver glutamine synthetase. !$#cross-references MUID:92408449; PMID:1356223 !$#accession A44095 !'##molecule_type mRNA !'##residues 1-373 ##label CAM !'##cross-references GB:S45408; NID:g255851; PIDN:AAC69361.1; !1PID:g255852 !'##experimental_source liver !'##note sequence extracted from NCBI backbone (NCBIP:113559) CLASSIFICATION #superfamily glutamate-ammonia ligase KEYWORDS ligase SUMMARY #length 373 #molecular-weight 42146 #checksum 7876 SEQUENCE /// ENTRY AJFF1M #type complete TITLE glutamate-ammonia ligase (EC 6.3.1.2) 1, mitochondrial - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES glutamine synthetase ORGANISM #formal_name Drosophila melanogaster DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Jun-2002 ACCESSIONS S09109 REFERENCE S09108 !$#authors Caizzi, R.; Bozzetti, M.P.; Caggese, C. !$#journal J. Mol. Biol. (1990) 212:17-26 !$#title Homologous nuclear genes encode cytoplasmic and !1mitochondrial glutamine synthetase in Drosophila !1melanogaster. !$#cross-references MUID:90204539; PMID:1969491 !$#accession S09109 !'##molecule_type DNA !'##residues 1-399 ##label CAI GENETICS !$#gene FlyBase:Gs1 !'##cross-references FlyBase:FBgn0001142 CLASSIFICATION #superfamily glutamate-ammonia ligase KEYWORDS ligase; mitochondrion SUMMARY #length 399 #molecular-weight 44518 #checksum 1496 SEQUENCE /// ENTRY AJFF2C #type complete TITLE glutamate-ammonia ligase (EC 6.3.1.2) 2, cytosolic - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES glutamine synthetase 2, cytosolic ORGANISM #formal_name Drosophila melanogaster DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Jun-2002 ACCESSIONS S09108 REFERENCE S09108 !$#authors Caizzi, R.; Bozzetti, M.P.; Caggese, C. !$#journal J. Mol. Biol. (1990) 212:17-26 !$#title Homologous nuclear genes encode cytoplasmic and !1mitochondrial glutamine synthetase in Drosophila !1melanogaster. !$#cross-references MUID:90204539; PMID:1969491 !$#accession S09108 !'##molecule_type DNA !'##residues 1-365 ##label CAI GENETICS !$#gene FlyBase:Gs2 !'##cross-references FlyBase:FBgn0001145 CLASSIFICATION #superfamily glutamate-ammonia ligase KEYWORDS ligase SUMMARY #length 365 #molecular-weight 40868 #checksum 553 SEQUENCE /// ENTRY AJAAQ #type complete TITLE glutamate-ammonia ligase (EC 6.3.1.2) beta - alfalfa ALTERNATE_NAMES glutamine synthetase ORGANISM #formal_name Medicago sativa #common_name alfalfa DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 03-Jun-2002 ACCESSIONS A26025; A05079; A05097 REFERENCE A93126 !$#authors Tischer, E.; DasSarma, S.; Goodman, H.M. !$#journal Mol. Gen. Genet. (1986) 203:221-229 !$#title Nucleotide sequence of an alfalfa glutamine synthetase gene. !$#accession A26025 !'##molecule_type DNA !'##residues 1-356 ##label TIS REFERENCE A05079 !$#authors Donn, G.; Tischer, E.; Smith, J.A.; Goodman, H.M. !$#journal J. Mol. Appl. Genet. (1984) 2:621-635 !$#title Herbicide-resistant alfalfa cells: an example of gene !1amplification in plants. !$#cross-references MUID:85159408; PMID:6152283 !$#accession A05079 !'##molecule_type protein !'##residues 266-356 ##label DON COMMENT This enzyme catalyzes the formation of glutamine from !1ammonia and glutamic acid in the presence of ATP. GENETICS !$#introns 25/2; 38/3; 73/2; 89/3; 125/2; 154/3; 197/3; 222/3; 240/3; !1253/2; 306/3 CLASSIFICATION #superfamily glutamate-ammonia ligase KEYWORDS ligase SUMMARY #length 356 #molecular-weight 39107 #checksum 9291 SEQUENCE /// ENTRY AJFBQB #type complete TITLE glutamate-ammonia ligase (EC 6.3.1.2) beta, cytosolic - kidney bean ALTERNATE_NAMES glutamine synthetase ORGANISM #formal_name Phaseolus vulgaris #common_name kidney bean DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Jun-2002 ACCESSIONS A26308 REFERENCE A91042 !$#authors Gebhardt, C.; Oliver, J.E.; Forde, B.G.; Saarelainen, R.; !1Miflin, B.J. !$#journal EMBO J. (1986) 5:1429-1435 !$#title Primary structure and differential expression of glutamine !1synthetase genes in nodules, roots and leaves of Phaseolus !1vulgaris. !$#accession A26308 !'##molecule_type mRNA !'##residues 1-356 ##label GEB !'##cross-references GB:X04001; NID:g21010; PIDN:CAA27631.1; PID:g21011 GENETICS !$#gene R1 CLASSIFICATION #superfamily glutamate-ammonia ligase KEYWORDS ligase SUMMARY #length 356 #molecular-weight 39118 #checksum 698 SEQUENCE /// ENTRY AJPMQ1 #type complete TITLE glutamate-ammonia ligase (EC 6.3.1.2) beta, cytosolic - garden pea ALTERNATE_NAMES glutamine synthetase GS1 ORGANISM #formal_name Pisum sativum #common_name garden pea DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 03-Jun-2002 ACCESSIONS B28089; C26171 REFERENCE A92728 !$#authors Tingey, S.V.; Tsai, F.Y.; Edwards, J.W.; Walker, E.L.; !1Coruzzi, G.M. !$#journal J. Biol. Chem. (1988) 263:9651-9657 !$#title Chloroplast and cytosolic glutamine synthetase are encoded !1by homologous nuclear genes which are differentially !1expressed in vivo. !$#cross-references MUID:88257087; PMID:2898472 !$#accession B28089 !'##molecule_type mRNA !'##residues 1-355 ##label TIN !'##cross-references GB:M20663; GB:J03878; NID:g169095; PIDN:AAA33669.1; !1PID:g169096 COMMENT Glutamate-ammonia ligase catalyzes the formation of !1glutamine from glutamate and ammonia with ATP converting to !1ADP and phosphate. In higher plants, there are several !1distinct isoforms that are targeted to subcellular !1compartments. The cytosolic enzyme, gamma, is predominantly !1in the root and is responsible for the assimilation of !1ammonia fixed by bacteroids. CLASSIFICATION #superfamily glutamate-ammonia ligase KEYWORDS ligase SUMMARY #length 355 #molecular-weight 38928 #checksum 1757 SEQUENCE /// ENTRY AJLCQB #type complete TITLE glutamate-ammonia ligase (EC 6.3.1.2) beta, cytosolic - garden lettuce ALTERNATE_NAMES glutamine synthetase ORGANISM #formal_name Lactuca sativa #common_name garden lettuce DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Jun-2002 ACCESSIONS S11965 REFERENCE S11965 !$#authors Sakamoto, A.; Takeba, G.; Shibata, D.; Tanaka, K. !$#journal Plant Mol. Biol. (1990) 15:317-323 !$#title Phytochrome-mediated activation of the gene for cytosolic !1glutamine-synthetase (GS(1)) during imbibition of !1photosensitive lettuce seeds. !$#cross-references MUID:91355878; PMID:1983300 !$#accession S11965 !'##molecule_type DNA !'##residues 1-358 ##label SAK !'##note the sequence from Fig. 3 is inconsistent with that from Fig. 2 !1in having 40-Leu, 42-Gly, 83-Arg, 121-Ala, and 173-Asp CLASSIFICATION #superfamily glutamate-ammonia ligase KEYWORDS ligase SUMMARY #length 358 #molecular-weight 39576 #checksum 1210 SEQUENCE /// ENTRY AJRZQB #type complete TITLE glutamate-ammonia ligase (EC 6.3.1.2) beta, cytosolic - rice ALTERNATE_NAMES glutamine synthetase ORGANISM #formal_name Oryza sativa #common_name rice DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Jun-2002 ACCESSIONS S07469 REFERENCE S07469 !$#authors Sakamoto, A.; Ogawa, M.; Masumura, T.; Shibata, D.; Takeba, !1G.; Tanaka, K.; Fujii, S. !$#journal Plant Mol. Biol. (1989) 13:611-614 !$#title Three cDNA sequences coding for glutamine synthetase !1polypeptides in Oryza sativa L. !$#cross-references MUID:91370845; PMID:2577497 !$#accession S07469 !'##molecule_type DNA !'##residues 1-357 ##label SAK !'##cross-references GB:X14244; NID:g20357; PIDN:CAA32460.1; PID:g20358 CLASSIFICATION #superfamily glutamate-ammonia ligase KEYWORDS ligase SUMMARY #length 357 #molecular-weight 39258 #checksum 2065 SEQUENCE /// ENTRY AJFBQ #type complete TITLE glutamate-ammonia ligase (EC 6.3.1.2) gamma, cytosolic - kidney bean ALTERNATE_NAMES glutamine synthetase ORGANISM #formal_name Phaseolus vulgaris #common_name kidney bean DATE 28-Aug-1985 #sequence_revision 30-Sep-1991 #text_change 03-Jun-2002 ACCESSIONS S04727; A01193; PQ0141 REFERENCE S04727 !$#authors Bennett, M.J.; Lightfoot, D.A.; Cullimore, J.V. !$#journal Plant Mol. Biol. (1989) 12:553-565 !$#title cDNA sequence and differential expression of the gene !1encoding the glutamine synthetase gamma polypeptide of !1Phaseolus vulgaris L. !$#accession S04727 !'##molecule_type mRNA !'##residues 1-356 ##label BEN REFERENCE A01193 !$#authors Cullimore, J.V.; Gebhardt, C.; Saarelainen, R.; Miflin, !1B.J.; Idler, K.B.; Barker, R.F. !$#journal J. Mol. Appl. Genet. (1984) 2:589-599 !$#title Glutamine synthetase of Phaseolus vulgaris L.: !1organ-specific expression of a multigene family. !$#cross-references MUID:85159406; PMID:6152282 !$#accession A01193 !'##molecule_type mRNA !'##residues 216-356 ##label CUL !'##cross-references GB:M10159; NID:g169342; PIDN:AAA33762.1; !1PID:g169343 REFERENCE PQ0141 !$#authors Forde, B.G.; Freeman, J.; Oliver, J.E.; Pineda, M. !$#journal Plant Cell (1990) 2:925-939 !$#title Nuclear factors interact with conserved A/T-rich elements !1upstream of a nodule-enhanced glutamine synthetase gene from !1French bean. !$#cross-references MUID:93005681; PMID:1983793 !$#accession PQ0141 !'##molecule_type DNA !'##residues 1-38 ##label FOR !'##cross-references GB:M92095; NID:g169340; PIDN:AAA33761.1; !1PID:g169341 CLASSIFICATION #superfamily glutamate-ammonia ligase KEYWORDS ligase SUMMARY #length 356 #molecular-weight 39341 #checksum 1563 SEQUENCE /// ENTRY AJRZQG #type complete TITLE glutamate-ammonia ligase (EC 6.3.1.2), cytosolic (clone GS28) - rice ALTERNATE_NAMES glutamine synthetase ORGANISM #formal_name Oryza sativa #common_name rice DATE 30-Sep-1991 #sequence_revision 24-Apr-1998 #text_change 03-Jun-2002 ACCESSIONS S07470 REFERENCE S07469 !$#authors Sakamoto, A.; Ogawa, M.; Masumura, T.; Shibata, D.; Takeba, !1G.; Tanaka, K.; Fujii, S. !$#journal Plant Mol. Biol. (1989) 13:611-614 !$#title Three cDNA sequences coding for glutamine synthetase !1polypeptides in Oryza sativa L. !$#cross-references MUID:91370845; PMID:2577497 !$#accession S07470 !'##molecule_type mRNA !'##residues 1-356 ##label SAK !'##cross-references GB:X14245; NID:g20367; PIDN:CAA32461.1; PID:g20368 CLASSIFICATION #superfamily glutamate-ammonia ligase KEYWORDS cytosol; ligase SUMMARY #length 356 #molecular-weight 39201 #checksum 2818 SEQUENCE /// ENTRY AJFBQA #type complete TITLE glutamate-ammonia ligase (EC 6.3.1.2) alpha, cytosolic - kidney bean ALTERNATE_NAMES glutamine synthetase ORGANISM #formal_name Phaseolus vulgaris #common_name kidney bean DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Jun-2002 ACCESSIONS B26308 REFERENCE A91042 !$#authors Gebhardt, C.; Oliver, J.E.; Forde, B.G.; Saarelainen, R.; !1Miflin, B.J. !$#journal EMBO J. (1986) 5:1429-1435 !$#title Primary structure and differential expression of glutamine !1synthetase genes in nodules, roots and leaves of Phaseolus !1vulgaris. !$#accession B26308 !'##molecule_type mRNA !'##residues 1-356 ##label GEB !'##cross-references GB:X04002; NID:g21012; PIDN:CAA27632.1; PID:g21013 GENETICS !$#gene R2 CLASSIFICATION #superfamily glutamate-ammonia ligase KEYWORDS ligase SUMMARY #length 356 #molecular-weight 39205 #checksum 2646 SEQUENCE /// ENTRY AJPMQA #type complete TITLE glutamate-ammonia ligase (EC 6.3.1.2) alpha, cytosolic - garden pea ALTERNATE_NAMES glutamine synthetase ORGANISM #formal_name Pisum sativum #common_name garden pea DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Jun-2002 ACCESSIONS B26171 REFERENCE A91062 !$#authors Tingey, S.V.; Walker, E.L.; Coruzzi, G.M. !$#journal EMBO J. (1987) 6:1-9 !$#title Glutamine synthetase genes of pea encode distinct !1polypeptides which are differentially expressed in leaves, !1roots and nodules. !$#cross-references MUID:87218452; PMID:2884100 !$#accession B26171 !'##molecule_type mRNA !'##residues 1-357 ##label TIN !'##cross-references GB:X04763; NID:g20750; PIDN:CAA28456.1; PID:g20751 !'##experimental_source clone pGS341 CLASSIFICATION #superfamily glutamate-ammonia ligase KEYWORDS ligase SUMMARY #length 357 #molecular-weight 39288 #checksum 976 SEQUENCE /// ENTRY AJYLNB #type fragment TITLE glutamate-ammonia ligase (EC 6.3.1.2), cytosolic - narrow-leaved blue lupine (fragment) ALTERNATE_NAMES glutamine synthetase ORGANISM #formal_name Lupinus angustifolius #common_name narrow-leaved blue lupine DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Jun-2002 ACCESSIONS S07462 REFERENCE S07462 !$#authors Grant, M.R.; Carne, A.; Hill, D.F.; Farnden, K.J.F. !$#journal Plant Mol. Biol. (1989) 13:481-490 !$#title The isolation and characterization of a cDNA clone encoding !1Lupinus angustifolius root nodule glutamine synthetase. !$#cross-references MUID:91370830; PMID:2577495 !$#accession S07462 !'##molecule_type DNA !'##residues 1-315 ##label GRA !'##cross-references GB:X15578; NID:g19142; PIDN:CAA33605.1; PID:g579367 CLASSIFICATION #superfamily glutamate-ammonia ligase KEYWORDS ligase SUMMARY #length 315 #checksum 151 SEQUENCE /// ENTRY AJFBQD #type complete TITLE glutamate-ammonia ligase (EC 6.3.1.2) delta precursor, chloroplast - kidney bean ALTERNATE_NAMES glutamine synthetase delta; plasmid-located glutamine synthetase ORGANISM #formal_name Phaseolus vulgaris #common_name kidney bean DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Jun-2002 ACCESSIONS S04031; S24245 REFERENCE S04031 !$#authors Lightfoot, D.A.; Green, N.K.; Cullimore, J.V. !$#journal Plant Mol. Biol. (1988) 11:191-202 !$#title The chloroplast-located glutamine synthetase of Phaseolus !1vulgaris L.: nucleotide sequence, expression in different !1organs and uptake into isolated chloroplasts. !$#accession S04031 !'##molecule_type mRNA !'##residues 1-429 ##label LIG !'##cross-references GB:X12738; NID:g21004; PIDN:CAA31234.1; PID:g21005 REFERENCE S24245 !$#authors Cock, J.M. !$#submission submitted to the EMBL Data Library, July 1991 !$#accession S24245 !'##molecule_type DNA !'##residues 396-429 ##label COC !'##cross-references EMBL:X61292; NID:g20998; PIDN:CAA43591.1; !1PID:g805011 CLASSIFICATION #superfamily glutamate-ammonia ligase KEYWORDS chloroplast; ligase FEATURE !$1-57 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$58-429 #product glutamate-ammonia ligase delta #status !8predicted #label MAT SUMMARY #length 429 #molecular-weight 47246 #checksum 9923 SEQUENCE /// ENTRY AJPMQ2 #type complete TITLE glutamate-ammonia ligase (EC 6.3.1.2) delta precursor, chloroplast - garden pea ALTERNATE_NAMES glutamine synthetase GS2 ORGANISM #formal_name Pisum sativum #common_name garden pea DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 03-Jun-2002 ACCESSIONS A28089; A26171 REFERENCE A92728 !$#authors Tingey, S.V.; Tsai, F.Y.; Edwards, J.W.; Walker, E.L.; !1Coruzzi, G.M. !$#journal J. Biol. Chem. (1988) 263:9651-9657 !$#title Chloroplast and cytosolic glutamine synthetase are encoded !1by homologous nuclear genes which are differentially !1expressed in vivo. !$#cross-references MUID:88257087; PMID:2898472 !$#accession A28089 !'##molecule_type DNA !'##residues 1-430 ##label TIN !'##cross-references GB:M20664; GB:J03878; NID:g169058; PIDN:AAA33653.1; !1PID:g169059 !'##experimental_source clone pGS185 REFERENCE A91062 !$#authors Tingey, S.V.; Walker, E.L.; Coruzzi, G.M. !$#journal EMBO J. (1987) 6:1-9 !$#title Glutamine synthetase genes of pea encode distinct !1polypeptides which are differentially expressed in leaves, !1roots and nodules. !$#cross-references MUID:87218452; PMID:2884100 !$#accession A26171 !'##molecule_type mRNA !'##residues 58-430 ##label TIN2 !'##cross-references GB:X05514; NID:g20752; PIDN:CAA29057.1; PID:g829285 !'##experimental_source clone pGS197 !'##note the authors translated the codon GAG for residue 23 as Gly and !1TAT for residue 201 as Trp COMMENT Glutamate-ammonia ligase catalyzes the formation of !1glutamine from glutamate and ammonia with ATP converting to !1ADP and phosphate. In higher plants, there are several !1distinct isoforms that are targeted to subcellular !1compartments. The light-modulated chloroplast enzyme, !1encoded by a nuclear gene and expressed primarily in leaves, !1is responsible for the reassimilation of the ammonia !1generated by photorespiration. CLASSIFICATION #superfamily glutamate-ammonia ligase KEYWORDS chloroplast; ligase FEATURE !$1-49 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$50-430 #product glutamate-ammonia ligase #status predicted !8#label MAT SUMMARY #length 430 #molecular-weight 47345 #checksum 1726 SEQUENCE /// ENTRY AJRZQD #type complete TITLE glutamate-ammonia ligase (EC 6.3.1.2) delta precursor, chloroplast - rice ALTERNATE_NAMES glutamine synthetase delta ORGANISM #formal_name Oryza sativa #common_name rice DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Jun-2002 ACCESSIONS S07471 REFERENCE S07469 !$#authors Sakamoto, A.; Ogawa, M.; Masumura, T.; Shibata, D.; Takeba, !1G.; Tanaka, K.; Fujii, S. !$#journal Plant Mol. Biol. (1989) 13:611-614 !$#title Three cDNA sequences coding for glutamine synthetase !1polypeptides in Oryza sativa L. !$#cross-references MUID:91370845; PMID:2577497 !$#accession S07471 !'##molecule_type mRNA !'##residues 1-428 ##label SAK !'##cross-references GB:X14246; NID:g20369; PIDN:CAA32462.1; PID:g20370 CLASSIFICATION #superfamily glutamate-ammonia ligase KEYWORDS chloroplast; ligase SUMMARY #length 428 #molecular-weight 46642 #checksum 566 SEQUENCE /// ENTRY AJBHQ #type complete TITLE glutamate-ammonia ligase (EC 6.3.1.2) 2 precursor, chloroplast - barley ALTERNATE_NAMES glutamine synthetase 2 ORGANISM #formal_name Hordeum vulgare #common_name barley DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Jun-2002 ACCESSIONS S11865; S12687; S14893; A30468; A32363; S05971 REFERENCE S11865 !$#authors Stroman, P.; Baima, S.; Casadoro, G. !$#journal Plant Mol. Biol. (1990) 15:161-163 !$#title A cDNA sequence coding for glutamine synthetase in Hordeum !1vulgare L. !$#cross-references MUID:91355850; PMID:1983297 !$#accession S11865 !'##molecule_type mRNA !'##residues 1-434 ##label STR !'##cross-references EMBL:X53580 REFERENCE S12687 !$#authors Casadoro, G. !$#submission submitted to the EMBL Data Library, June 1990 !$#accession S12687 !'##molecule_type mRNA !'##residues 1-185,'P',187-434 ##label CAS !'##cross-references EMBL:X53580; NID:g18987; PIDN:CAA37643.1; !1PID:g18988 REFERENCE S14893 !$#authors Freeman, J.; Marquez, A.J.; Wallsgrove, R.M.; Saarelainen, !1R.; Forde, B.G. !$#journal Plant Mol. Biol. (1990) 14:297-311 !$#title Molecular analysis of barley mutants deficient in !1chloroplast glutamine synthetase. !$#cross-references MUID:91346618; PMID:1983286 !$#accession S14893 !'##molecule_type mRNA !'##residues 'AQAVVQAMQCQV',21,'VR',24,'RTA',28-40,'R',42-185,'P', !1187-434 ##label FRE !'##cross-references EMBL:X16000; NID:g18985; PIDN:CAA34131.1; !1PID:g755762 !$#accession A30468 !'##molecule_type protein !'##residues 'X',55-68 ##label FRE2 !'##note a large fraction of the protein has a blocked amino end. In the !1small fraction with a free amino end, 54-Ala and 55-Leu were !1found as amino-terminal residues in equal amount REFERENCE A32363 !$#authors Baima, S.; Haegi, A.; Stroman, P.; Casadoro, G. !$#journal Carlsberg Res. Commun. (1989) 54:1-9 !$#title Characterization of a cDNA clone for barley leaf glutamine !1synthetase. !$#cross-references MUID:89322552; PMID:2473765 !$#accession A32363 !'##molecule_type mRNA !'##residues 48-434 ##label BAI GENETICS !$#map_position 2 CLASSIFICATION #superfamily glutamate-ammonia ligase KEYWORDS chloroplast; ligase FEATURE !$1-53 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$54-434 #product glutamate-ammonia ligase #status !8experimental #label MAT SUMMARY #length 434 #molecular-weight 47125 #checksum 694 SEQUENCE /// ENTRY AJDHQ #type fragment TITLE glutamate-ammonia ligase (EC 6.3.1.2) - green alga (Dunaliella salina) (fragment) ALTERNATE_NAMES glutamine synthetase ORGANISM #formal_name Dunaliella salina DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Jun-2002 ACCESSIONS S04888 REFERENCE S04888 !$#authors Long, Z.; Nelson, N. !$#submission submitted to the EMBL Data Library, May 1989 !$#accession S04888 !'##molecule_type mRNA !'##residues 1-234 ##label LON !'##cross-references EMBL:X15280; NID:g18384; PIDN:CAA33353.1; !1PID:g1360726 CLASSIFICATION #superfamily glutamate-ammonia ligase KEYWORDS ligase SUMMARY #length 234 #checksum 4319 SEQUENCE /// ENTRY AJECQ #type complete TITLE glutamate-ammonia ligase (EC 6.3.1.2) - Escherichia coli (strain K-12) ALTERNATE_NAMES glutamine synthetase ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 24-Feb-1995 #text_change 03-Jun-2002 ACCESSIONS S40815; A25957; A23970; A44678; A33702; A22947; I41068; !1I41234; A65192 REFERENCE S40802 !$#authors Plunkett III, G.; Burland, V.; Daniels, D.L.; Blattner, F.R. !$#journal Nucleic Acids Res. (1993) 21:3391-3398 !$#title Analysis of the Escherichia coli genome. III. DNA sequence !1of the region from 87.2 to 89.2 minutes. !$#cross-references MUID:93347969; PMID:8346018 !$#accession S40815 !'##molecule_type DNA !'##residues 1-469 ##label PLU !'##cross-references EMBL:L19201; NID:g304961; PIDN:AAB03004.1; !1PID:g304975 !'##experimental_source strain MG1655 REFERENCE A25957 !$#authors Colombo, G.; Villafranca, J.J. !$#journal J. Biol. Chem. (1986) 261:10587-10591 !$#title Amino acid sequence of Escherichia coli glutamine synthetase !1deduced from the DNA nucleotide sequence. !$#cross-references MUID:86278128; PMID:2874141 !$#accession A25957 !'##molecule_type DNA !'##residues 1-89,'S',91-107,'MS',110-196,'S',198-469 ##label COL !'##cross-references GB:M13746; NID:g146156; PIDN:AAA23879.1; !1PID:g146157 !'##note the authors translated the codons TCG for residue 90 and TCT !1for residue 197 as Cys REFERENCE A91533 !$#authors Rocha, M.; Vazquez, M.; Garciarrubio, A.; Covarrubias, A.A. !$#journal Gene (1985) 37:91-99 !$#title Nucleotide sequence of the glnA-glnL intercistronic region !1of Escherichia coli. !$#cross-references MUID:86031370; PMID:2865194 !$#accession A23970 !'##molecule_type DNA !'##residues 363-469 ##label ROC !'##cross-references GB:K02176; NID:g146160; PIDN:AAA23880.1; !1PID:g146161; GB:M11581 REFERENCE A44678 !$#authors Heinrikson, R.L.; Kingdon, H.S. !$#journal J. Biol. Chem. (1971) 246:1099-1106 !$#title Primary structure of Escherichia coli glutamine synthetase. !1II. The complete amino acid sequence of a tryptic !1heneicosapeptide containing covalently bound adenylic acid. !$#cross-references MUID:71111416; PMID:5543675 !$#accession A44678 !'##molecule_type protein !'##residues 387-393,'KD',396-403,'G',404-406 ##label HEI REFERENCE A33702 !$#authors Di Ianni, C.L.; Villafranca, J.J. !$#journal J. Biol. Chem. (1989) 264:8686-8691 !$#title Identification of amino acid residues modified by pyridoxal !15'-phosphate in Escherichia coli glutamine synthetase. !$#cross-references MUID:89255329; PMID:2566607 !$#accession A33702 !'##status preliminary !'##molecule_type protein !'##residues 2-9,336-360,377-393 ##label DIT REFERENCE A22947 !$#authors Reitzer, L.J.; Magasanik, B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:1979-1983 !$#title Expression of glnA in Escherichia coli is regulated at !1tandem promoters. !$#cross-references MUID:85166256; PMID:2858855 !$#accession A22947 !'##molecule_type DNA !'##residues 1-9 ##label REI !'##cross-references GB:M10421; NID:g146163; PIDN:AAA23882.1; !1PID:g146164 REFERENCE I41068 !$#authors Covarrubias, A.A.; Bastarrachea, F. !$#journal Mol. Gen. Genet. (1983) 190:171-175 !$#title Nucleotide sequence of the glnA control region of !1Escherichia coli. !$#cross-references MUID:83218556; PMID:6134228 !$#accession I41068 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-43 ##label RES !'##cross-references EMBL:V00282; NID:g41566; PIDN:CAA23546.1; !1PID:g41567 REFERENCE I41234 !$#authors Ow, D.W.; Sundaresan, V.; Rothstein, D.M.; Brown, S.E.; !1Ausubel, F.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:2524-2528 !$#title Promoters regulated by the glnG (ntrC) and nifA gene !1products share a heptameric consensus sequence in the -15 !1region. !$#cross-references MUID:83195090; PMID:6133280 !$#accession I41234 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-7 ##label RE2 !'##cross-references GB:K01475; NID:g146152; PIDN:AAA23877.1; !1PID:g146153 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65192 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-469 ##label BLAT !'##cross-references GB:AE000462; GB:U00096; NID:g1790295; !1PIDN:AAC76867.1; PID:g1790301; UWGP:b3870 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene glnA !$#map_position 87 min FUNCTION !$#description catalyzes the formation of glutamine from ammonia and !1glutamic acid using ATP CLASSIFICATION #superfamily glutamate-ammonia ligase KEYWORDS ligase; phosphoprotein FEATURE !$398 #binding_site AMP (Tyr) (covalent) #status !8experimental SUMMARY #length 469 #molecular-weight 51903 #checksum 506 SEQUENCE /// ENTRY AJEBQT #type fragment TITLE glutamate-ammonia ligase (EC 6.3.1.2) - Salmonella typhimurium (fragment) ALTERNATE_NAMES glutamine synthetase ORGANISM #formal_name Salmonella typhimurium DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 03-Jun-2002 ACCESSIONS A25818; S53022 REFERENCE A25818 !$#authors Janson, C.A.; Kayne, P.S.; Almassy, R.J.; Grunstein, M.; !1Eisenberg, D. !$#journal Gene (1986) 46:297-300 !$#title Sequence of glutamine synthetase from Salmonella typhimurium !1and implications for the protein structure. !$#cross-references MUID:87106866; PMID:2879772 !$#accession A25818 !'##molecule_type DNA !'##residues 1-469 ##label JAN !'##cross-references GB:M14536; NID:g154089; PIDN:AAA27134.1; !1PID:g154090 REFERENCE S53022 !$#authors Kustu, S.G. !$#submission submitted to the EMBL Data Library, March 1995 !$#accession S53022 !'##status preliminary !'##molecule_type DNA !'##residues 133-222,'R',224-447,'R',449-469 ##label KUS !'##cross-references EMBL:X85104; NID:g728721; PIDN:CAA59423.1; !1PID:g728722 COMMENT This enzyme catalyzes the formation of glutamine from !1ammonia and glutamic acid in the presence of ATP. GENETICS !$#gene glnA !$#map_position 85 min CLASSIFICATION #superfamily glutamate-ammonia ligase KEYWORDS ligase; phosphoprotein FEATURE !$398 #binding_site AMP (Tyr) (covalent) #status predicted SUMMARY #length 469 #checksum 96 SEQUENCE /// ENTRY AJAIQ #type complete TITLE glutamate-ammonia ligase (EC 6.3.1.2) - Anabaena sp. ALTERNATE_NAMES glutamine synthetase ORGANISM #formal_name Anabaena sp. DATE 18-Apr-1984 #sequence_revision 18-Apr-1984 #text_change 03-Jun-2002 ACCESSIONS A01192 REFERENCE A01192 !$#authors Tumer, N.E.; Robinson, S.J.; Haselkorn, R. !$#journal Nature (1983) 306:337-342 !$#title Different promoters for the Anabaena glutamine synthetase !1gene during growth usine molecular or fixed nitrogen. !$#accession A01192 !'##molecule_type DNA !'##residues 1-474 ##label TUM !'##cross-references GB:X00147 !'##experimental_source PCC 7120 COMMENT This enzyme catalyzes the formation of glutamine from !1ammonia and glutamic acid in the presence of ATP. In !1Anabaena, it is present in ammonia-grown vegetative cells as !1well as in heterocysts (for nitrogen fixation). GENETICS !$#gene glnA !$#map_position 87 CLASSIFICATION #superfamily glutamate-ammonia ligase KEYWORDS ligase; phosphoprotein FEATURE !$402 #binding_site AMP (Tyr) (covalent) #status predicted SUMMARY #length 474 #molecular-weight 53136 #checksum 4261 SEQUENCE /// ENTRY AJAVQ #type complete TITLE glutamate-ammonia ligase (EC 6.3.1.2) - Azotobacter vinelandii ALTERNATE_NAMES glutamine synthetase ORGANISM #formal_name Azotobacter vinelandii DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 03-Jun-2002 ACCESSIONS A37153 REFERENCE A37153 !$#authors Toukdarian, A.; Saunders, G.; Selman-Sosa, G.; Santero, E.; !1Woodley, P.; Kennedy, C. !$#journal J. Bacteriol. (1990) 172:6529-6539 !$#title Molecular analysis of the Azotobacter vinelandii glnA gene !1encoding glutamine synthetase. !$#cross-references MUID:91035268; PMID:1977737 !$#accession A37153 !'##molecule_type DNA !'##residues 1-467 ##label TOU !'##cross-references EMBL:M57275; NID:g142308; PIDN:AAA62673.1; !1PID:g142309 COMMENT This enzyme catalyzes the formation of glutamine from !1ammonia and glutamic acid in the presence of ATP. GENETICS !$#gene glnA CLASSIFICATION #superfamily glutamate-ammonia ligase KEYWORDS ligase; phosphoprotein FEATURE !$396 #binding_site AMP (Tyr) (covalent) #status predicted SUMMARY #length 467 #molecular-weight 51746 #checksum 8851 SEQUENCE /// ENTRY AJKCQB #type complete TITLE glutamate-ammonia ligase (EC 6.3.1.2) - Azospirillum brasilense (strain Sp7) ALTERNATE_NAMES glutamine synthetase ORGANISM #formal_name Azospirillum brasilense DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 03-Jun-2002 ACCESSIONS A24714 REFERENCE A24714 !$#authors Bozouklian, H.; Elmerich, C. !$#journal Biochimie (1986) 68:1181-1187 !$#title Nucleotide sequence of the Azospirillum brasilense Sp 7 !1glutamine synthetase structural gene. !$#cross-references MUID:87076765; PMID:2878685 !$#accession A24714 !'##molecule_type DNA !'##residues 1-468 ##label BOZ !'##cross-references GB:M26107; NID:g142421; PIDN:AAA22183.1; !1PID:g142422 COMMENT This enzyme catalyzes the formation of glutamine from !1ammonia and glutamic acid in the presence of ATP. GENETICS !$#gene glnA CLASSIFICATION #superfamily glutamate-ammonia ligase KEYWORDS ligase; phosphoprotein FEATURE !$398 #binding_site AMP (Tyr) (covalent) #status predicted SUMMARY #length 468 #molecular-weight 51975 #checksum 2207 SEQUENCE /// ENTRY AJVCQA #type complete TITLE glutamate-ammonia ligase (EC 6.3.1.2) - Vibrio alginolyticus ALTERNATE_NAMES glutamine synthetase ORGANISM #formal_name Vibrio alginolyticus DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 03-Jun-2002 ACCESSIONS JL0113 REFERENCE JL0113 !$#authors Maharaj, R.; Rumbak, E.; Jones, W.A.; Robb, S.M.; Robb, !1F.T.; Woods, D.R. !$#journal Arch. Microbiol. (1989) 152:542-549 !$#title Nucleotide sequence of the Vibrio alginolyticus glnA region. !$#cross-references MUID:90073138; PMID:2574025 !$#accession JL0113 !'##molecule_type DNA !'##residues 1-468 ##label MAH !'##cross-references GB:M23257 !'##note the authors translated the codon TAC for residue 412 as Thr COMMENT This enzyme catalyzes the formation of glutamine from !1ammonia and glutamic acid in the presence of ATP. GENETICS !$#gene glnA CLASSIFICATION #superfamily glutamate-ammonia ligase KEYWORDS ligase; phosphoprotein FEATURE !$397 #binding_site AMP (Tyr) (covalent) #status predicted SUMMARY #length 468 #molecular-weight 51556 #checksum 6978 SEQUENCE /// ENTRY AJZRQL #type complete TITLE glutamate-ammonia ligase (EC 6.3.1.2) I - Rhizobium leguminosarum ALTERNATE_NAMES glutamine synthetase I ORGANISM #formal_name Rhizobium leguminosarum DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 03-Jun-2002 ACCESSIONS A26567 REFERENCE A93656 !$#authors Colonna-Romano, S.; Riccio, A.; Guida, M.; Defez, R.; !1Lamberti, A.; Iaccarino, M.; Arnold, W.; Priefer, U.; !1Puhler, A. !$#journal Nucleic Acids Res. (1987) 15:1951-1964 !$#title Tight linkage of glnA and a putative regulatory gene in !1Rhizobium leguminosarum. !$#cross-references MUID:87174729; PMID:2882467 !$#accession A26567 !'##molecule_type DNA !'##residues 1-469 ##label COL !'##cross-references GB:M16626 !'##note the authors translated the codon TTC for residue 54 as Ser, CGG !1for residues 106 and 130 as Pro, and TTC for residue 323 as !1Leu COMMENT This enzyme catalyzes the formation of glutamine from !1ammonia and glutamic acid in the presence of ATP. GENETICS !$#gene glnA CLASSIFICATION #superfamily glutamate-ammonia ligase KEYWORDS ligase; phosphoprotein FEATURE !$398 #binding_site AMP (Tyr) (covalent) #status predicted SUMMARY #length 469 #molecular-weight 52232 #checksum 3184 SEQUENCE /// ENTRY AJBCQF #type complete TITLE glutamate-ammonia ligase (EC 6.3.1.2) - Thiobacillus ferrooxidans ALTERNATE_NAMES glutamine synthetase ORGANISM #formal_name Thiobacillus ferrooxidans DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 03-Jun-2002 ACCESSIONS A29460 REFERENCE A29460 !$#authors Rawlings, D.E.; Jones, W.A.; O'Neill, E.G.; Woods, D.R. !$#journal Gene (1987) 53:211-217 !$#title Nucleotide sequence of the glutamine synthetase gene and its !1controlling region from the acidophilic autotroph !1Thiobacillus ferrooxidans. !$#cross-references MUID:87277411; PMID:2886400 !$#accession A29460 !'##molecule_type DNA !'##residues 1-468 ##label RAW !'##cross-references GB:M16626; NID:g154629; PIDN:AAA27370.1; !1PID:g154630 GENETICS !$#gene glnA CLASSIFICATION #superfamily glutamate-ammonia ligase KEYWORDS ligase; phosphoprotein FEATURE !$397 #binding_site AMP (Tyr) (covalent) #status predicted SUMMARY #length 468 #molecular-weight 51613 #checksum 5769 SEQUENCE /// ENTRY AJSMQC #type complete TITLE glutamate-ammonia ligase (EC 6.3.1.2) - Streptomyces coelicolor ALTERNATE_NAMES glutamine synthetase ORGANISM #formal_name Streptomyces coelicolor DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 03-Jun-2002 ACCESSIONS JT0389; T35314 REFERENCE JT0389 !$#authors Wray Jr., L.V.; Fisher, S.H. !$#journal Gene (1988) 71:247-256 !$#title Cloning and nucleotide sequence of the Streptomyces !1coelicolor gene encoding glutamine synthetase. !$#cross-references MUID:89138000; PMID:2906310 !$#accession JT0389 !'##molecule_type DNA !'##residues 1-469 ##label WRA !'##cross-references GB:M23172; NID:g295173; PIDN:AAA72717.1; !1PID:g295174 REFERENCE Z21574 !$#authors Seeger, K.; Harris, D.; Bentley, S.D.; Parkhill, J.; !1Barrell, B.G.; Rajandream, M.A. !$#submission submitted to the EMBL Data Library, July 1999 !$#accession T35314 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-469 ##label SEE !'##cross-references EMBL:AL096872; PIDN:CAB51282.1; GSPDB:GN00070; !1SCOEDB:glnA !'##experimental_source strain A3(2) COMMENT This enzyme catalyzes the formation of glutamine from !1ammonia and glutamic acid in the presence of ATP. GENETICS !$#gene glnA CLASSIFICATION #superfamily glutamate-ammonia ligase KEYWORDS ligase; phosphoprotein FEATURE !$397 #binding_site AMP (Tyr) (covalent) #status predicted SUMMARY #length 469 #molecular-weight 52567 #checksum 3870 SEQUENCE /// ENTRY AJBSQU #type complete TITLE glutamate-ammonia ligase (EC 6.3.1.2) - Bacillus cereus ALTERNATE_NAMES glutamine synthetase ORGANISM #formal_name Bacillus cereus DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 03-Jun-2002 ACCESSIONS JU0075; A38060 REFERENCE A91912 !$#authors Nakano, Y.; Kato, C.; Tanaka, E.; Kimura, K.; Horikoshi, K. !$#journal J. Biochem. (1989) 106:209-215 !$#title Nucleotide sequence of the glutamine synthetase gene (glnA) !1and its upstream region from Bacillus cereus. !$#cross-references MUID:90036764; PMID:2572584 !$#accession JU0075 !'##molecule_type DNA !'##residues 1-444 ##label NAK !'##cross-references GB:D00513; NID:g216271; PIDN:BAA00403.1; !1PID:g216273 !$#accession A38060 !'##molecule_type protein !'##residues 1-20 ##label NA2 COMMENT This enzyme catalyzes the formation of glutamine from !1ammonia and glutamic acid in the presence of ATP. It !1requires both Mn2+ and Mg2+ ions for high activity. GENETICS !$#gene glnA CLASSIFICATION #superfamily glutamate-ammonia ligase KEYWORDS ligase SUMMARY #length 444 #molecular-weight 50195 #checksum 2505 SEQUENCE /// ENTRY AJBSQS #type complete TITLE glutamate-ammonia ligase (EC 6.3.1.2) [validated] - Bacillus subtilis ALTERNATE_NAMES glutamine synthetase ORGANISM #formal_name Bacillus subtilis DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 03-Jun-2002 ACCESSIONS JT0392; A48312; C69633 REFERENCE JT0392 !$#authors Strauch, M.A.; Aronson, A.I.; Brown, S.W.; Schreier, H.J.; !1Sonenshein, A.L. !$#journal Gene (1988) 71:257-265 !$#title Sequence of the Bacillus subtilis glutamine synthetase gene !1region. !$#cross-references MUID:89138001; PMID:2906311 !$#accession JT0392 !'##molecule_type DNA !'##residues 1-444 ##label STR !'##cross-references GB:M22811; NID:g142985; PIDN:AAA83376.1; !1PID:g142986 !'##experimental_source strain JH642, Marburg REFERENCE A48312 !$#authors Nakano, Y.; Tanaka, E.; Kato, C.; Kimura, K.; Horikoshi, K. !$#journal FEMS Microbiol. Lett. (1989) 57:81-86 !$#title The complete nucleotide sequence of the glutamine synthetase !1gene (glnA) of Bacillus subtilis. !$#accession A48312 !'##molecule_type DNA !'##residues 1-9,'V',11-42,'E',44-252,'D',254-258,'Y',260-444 ##label !1NAK !'##cross-references GB:D00854; NID:g216394; PIDN:BAA00730.1; !1PID:g216396 !'##experimental_source strain PC1219 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69633 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-444 ##label KUN !'##cross-references GB:Z99113; GB:AL009126; NID:g2634090; !1PIDN:CAB13630.1; PID:g2634130 !'##experimental_source strain 168 GENETICS !$#gene glnA FUNCTION !$#description EC 6.3.2.1 [validated, MUID:89138001]; catalyzes the !1formation of glutamine from ammonia and glutamic acid in the !1presence of ATP !$#note requires both Mn2+ and Mg2+ ions for high activity CLASSIFICATION #superfamily glutamate-ammonia ligase KEYWORDS ligase SUMMARY #length 444 #molecular-weight 50278 #checksum 711 SEQUENCE /// ENTRY AJCLQA #type complete TITLE glutamate-ammonia ligase (EC 6.3.1.2) - Clostridium acetobutylicum ALTERNATE_NAMES glutamine synthetase ORGANISM #formal_name Clostridium acetobutylicum DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 03-Jun-2002 ACCESSIONS A28676; S11994 REFERENCE A28676 !$#authors Janssen, P.J.; Jones, W.A.; Jones, D.T.; Woods, D.R. !$#journal J. Bacteriol. (1988) 170:400-408 !$#title Molecular analysis and regulation of the glnA gene of the !1gram-positive anaerobe Clostridium acetobutylicum. !$#cross-references MUID:88086901; PMID:2891680 !$#accession A28676 !'##molecule_type DNA !'##residues 1-443 ##label JAN !'##cross-references GB:X54158 REFERENCE S11994 !$#authors Janssen, P.J.; Jones, D.T.; Woods, D.R. !$#journal Mol. Microbiol. (1990) 4:1575-1583 !$#title Studies on Clostridium acetobutylicum glnA promoters and !1antisense RNA. !$#cross-references MUID:91141310; PMID:1981087 !$#accession S11994 !'##status preliminary !'##molecule_type DNA !'##residues 1-38 ##label JA2 COMMENT This enzyme catalyzes the formation of glutamine from !1ammonia and glutamic acid in the presence of ATP. GENETICS !$#gene glnA CLASSIFICATION #superfamily glutamate-ammonia ligase KEYWORDS ligase SUMMARY #length 443 #molecular-weight 49682 #checksum 8514 SEQUENCE /// ENTRY AJZJQ2 #type complete TITLE glutamate-ammonia ligase (EC 6.3.1.2) II - Bradyrhizobium japonicum ALTERNATE_NAMES glutamine synthetase II ORGANISM #formal_name Bradyrhizobium japonicum DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 03-Jun-2002 ACCESSIONS A24155 REFERENCE A24155 !$#authors Carlson, T.A.; Chelm, B.K. !$#journal Nature (1986) 322:568-570 !$#title Apparent eukaryotic origin of glutamine synthetase II from !1the bacterium Bradyrhizobium japonicum. !$#accession A24155 !'##molecule_type DNA !'##residues 1-329 ##label CAR COMMENT Two forms of glutamine synthetase (GSI and GSII) can be !1found in B. japonicum, a soybean symbiont that belongs to !1the Rhizobiaceae family of bacteria. GSI is a typical !1prokaryotic glutamine synthetase whereas GSII is similar to !1the eukaryotic enzyme. GENETICS !$#gene glnII CLASSIFICATION #superfamily glutamate-ammonia ligase KEYWORDS ligase SUMMARY #length 329 #molecular-weight 36906 #checksum 8065 SEQUENCE /// ENTRY AJKXQ #type complete TITLE glutamate-ammonia ligase (EC 6.3.1.2) II - Frankia sp. ALTERNATE_NAMES glutamine synthetase ORGANISM #formal_name Frankia sp. DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Jun-2002 ACCESSIONS A36725 REFERENCE A36725 !$#authors Rochefort, D.A.; Benson, D.R. !$#journal J. Bacteriol. (1990) 172:5335-5342 !$#title Molecular cloning, sequencing, and expression of the !1glutamine synthetase II (glnII) gene from the actinomycete !1root nodule symbiont Frankia sp. strain CpI1. !$#cross-references MUID:90368593; PMID:1975584 !$#accession A36725 !'##molecule_type DNA !'##residues 1-352 ##label ROC !'##cross-references GB:M58415; GB:M35050; NID:g148664; PIDN:AAA62803.1; !1PID:g148665 GENETICS !$#gene glnII CLASSIFICATION #superfamily glutamate-ammonia ligase KEYWORDS ligase SUMMARY #length 352 #molecular-weight 38665 #checksum 5910 SEQUENCE /// ENTRY AJSM2H #type complete TITLE glutamate-ammonia ligase (EC 6.3.1.2) II - Streptomyces hygroscopicus ALTERNATE_NAMES glutamine synthetase ORGANISM #formal_name Streptomyces hygroscopicus DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Jun-2002 ACCESSIONS A36726 REFERENCE A36726 !$#authors Kumada, Y.; Takano, E.; Nagaoka, K.; Thompson, C.J. !$#journal J. Bacteriol. (1990) 172:5343-5351 !$#title Streptomyces hygroscopicus has two glutamine synthetase !1genes. !$#cross-references MUID:90368594; PMID:1975585 !$#accession A36726 !'##molecule_type DNA !'##residues 1-340 ##label KUM !'##cross-references GB:M33783; NID:g153285; PIDN:AAA26749.1; !1PID:g153286 CLASSIFICATION #superfamily glutamate-ammonia ligase KEYWORDS ligase SUMMARY #length 340 #molecular-weight 37417 #checksum 9121 SEQUENCE /// ENTRY AJSM2V #type complete TITLE glutamate-ammonia ligase (EC 6.3.1.2) II - Streptomyces viridochromogenes ALTERNATE_NAMES glutamine synthetase II ORGANISM #formal_name Streptomyces viridochromogenes DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Jun-2002 ACCESSIONS C36724; S09195; S11635 REFERENCE A36724 !$#authors Behrmann, I.; Hillemann, D.; Puehler, A.; Strauch, E.; !1Wohlleben, W. !$#journal J. Bacteriol. (1990) 172:5326-5334 !$#title Overexpression of a Streptomyces viridochromogenes gene !1(glnII) encoding a glutamine synthetase similar to those of !1eucaryotes confers resistance against the antibiotic !1phosphinothricyl-alanyl-alanine. !$#cross-references MUID:90368592; PMID:1975583 !$#accession C36724 !'##molecule_type DNA !'##residues 1-343 ##label BEH !'##cross-references EMBL:X52842; NID:g47983; PIDN:CAA37028.1; !1PID:g581783 GENETICS !$#gene glnII !$#start_codon GTG CLASSIFICATION #superfamily glutamate-ammonia ligase KEYWORDS ligase SUMMARY #length 343 #molecular-weight 37258 #checksum 4274 SEQUENCE /// ENTRY SYECEC #type complete TITLE glutamate-cysteine ligase (EC 6.3.2.2) - Escherichia coli (strain K-12) ALTERNATE_NAMES gamma-glutamylcysteine synthetase ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 17-Oct-1997 #text_change 03-Jun-2002 ACCESSIONS A65049; A24136 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65049 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-518 ##label BLAT !'##cross-references GB:AE000353; GB:U00096; NID:g1789037; !1PIDN:AAC75735.1; PID:g1789044; UWGP:b2688 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A24136 !$#authors Watanabe, K.; Yamano, Y.; Murata, K.; Kimura, A. !$#journal Nucleic Acids Res. (1986) 14:4393-4400 !$#title The nucleotide sequence of the gene for !1gamma-glutamylcysteine synthetase of Escherichia coli. !$#cross-references MUID:86232579; PMID:2872655 !$#accession A24136 !'##molecule_type DNA !'##residues 1-99,'L',101-493,'GF',496-518 ##label WAT !'##cross-references GB:X03954; NID:g41622; PIDN:CAA27583.1; PID:g581100 COMMENT This enzyme catalyzes the formation of !1gamma-glutamylcysteine from glutamate and cysteine in the !1presence of ATP, a step in glutathione biosynthesis. GENETICS !$#gene gshA (gshI) !$#map_position 58 min CLASSIFICATION #superfamily glutamate-cysteine ligase KEYWORDS glutathione biosynthesis; ligase SUMMARY #length 518 #molecular-weight 58269 #checksum 6982 SEQUENCE /// ENTRY SYECGS #type complete TITLE glutathione synthase (EC 6.3.2.3) - Escherichia coli (strain K-12) ALTERNATE_NAMES glutathione synthetase ORGANISM #formal_name Escherichia coli DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 01-Mar-2002 ACCESSIONS A01194; B65080 REFERENCE A01194 !$#authors Gushima, H.; Yasuda, S.; Soeda, E.; Yokota, M.; Kondo, M.; !1Kimura, A. !$#journal Nucleic Acids Res. (1984) 12:9299-9307 !$#title Complete nucleotide sequence of the Escherichia coli !1glutathione synthetase gsh-II. !$#cross-references MUID:85087938; PMID:6393055 !$#accession A01194 !'##molecule_type DNA !'##residues 1-316 ##label GUS !'##cross-references GB:X01666; NID:g41624; PIDN:CAA25826.1; PID:g41625 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65080 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-316 ##label BLAT !'##cross-references GB:AE000377; GB:U00096; NID:g2367178; !1PIDN:AAC75984.1; PID:g1789316; UWGP:b2947 !'##experimental_source strain K-12, substrain MG1655 COMMENT This enzyme catalyzes the formation of glutathione by !1condensing gamma-glutamylcysteine and glycine in the !1presence of ATP. GENETICS !$#gene gshB; gsh-II CLASSIFICATION #superfamily Escherichia coli glutathione synthase KEYWORDS ATP; glutathione biosynthesis; homotetramer; ligase SUMMARY #length 316 #molecular-weight 35561 #checksum 2303 SEQUENCE /// ENTRY S77430 #type complete TITLE glutathione synthase (EC 6.3.2.3) - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES glutathione synthetase; protein slr1238 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 11-Jan-2000 #sequence_revision 11-Jan-2000 #text_change 16-Jun-2000 ACCESSIONS S77430 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S77430 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-320 ##label KAN !'##cross-references EMBL:D90906; GB:AB001339; NID:g1652492; !1PIDN:BAA17533.1; PID:g1652612 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 COMMENT This enzyme catalyzes the formation of glutathione by !1condensing gamma-glutamylcysteine and glycine in the !1presence of ATP. GENETICS !$#gene gshB !$#start_codon GTG CLASSIFICATION #superfamily Escherichia coli glutathione synthase KEYWORDS ATP; glutathione biosynthesis; ligase SUMMARY #length 320 #molecular-weight 35069 #checksum 2693 SEQUENCE /// ENTRY JC4291 #type complete TITLE glutathione synthase (EC 6.3.2.3) - Anabaena sp. ALTERNATE_NAMES glutathione synthetase ORGANISM #formal_name Anabaena sp. DATE 11-Jan-2000 #sequence_revision 11-Jan-2000 #text_change 11-Jan-2000 ACCESSIONS JC4291 REFERENCE JC4289 !$#authors Doherty, H.M.; Adams, D.G. !$#journal Gene (1995) 163:93-96 !$#title Cloning and sequence of ftsZ and flanking regions from the !1cyanobacterium Anabaena PCC7120. !$#cross-references MUID:96001250; PMID:7557485 !$#accession JC4291 !'##molecule_type DNA !'##residues 1-324 ##label DOH !'##cross-references GB:U14408; NID:g555913; PIDN:AAA85527.1; !1PID:g555916 !'##experimental_source PCC7120 COMMENT This enzyme catalyzes the formation of glutathione by !1condensing gamma-glutamylcysteine and glycine in the !1presence of ATP. GENETICS !$#gene gsh-II CLASSIFICATION #superfamily Escherichia coli glutathione synthase KEYWORDS ATP; glutathione biosynthesis; ligase SUMMARY #length 324 #molecular-weight 35870 #checksum 9695 SEQUENCE /// ENTRY JQ1401 #type complete TITLE glutathione synthase (EC 6.3.2.3) - Anaplasma centrale ALTERNATE_NAMES glutathione synthetase ORGANISM #formal_name Anaplasma centrale DATE 11-Jan-2000 #sequence_revision 11-Jan-2000 #text_change 11-Jan-2000 ACCESSIONS JQ1401 REFERENCE JQ1401 !$#authors Peters, J.M.; Dalrymple, B.P.; Jorgensen, W.K. !$#journal Biochem. Biophys. Res. Commun. (1992) 182:1040-1046 !$#title Sequence of a putative glutathione synthetase II gene and !1flanking regions from Anaplasma centrale. !$#cross-references MUID:92171906; PMID:1540152 !$#accession JQ1401 !'##molecule_type DNA !'##residues 1-308 ##label PET !'##cross-references GB:M80425; NID:g142168; PIDN:AAA22064.1; !1PID:g142170 !'##note the authors translated the initiation codon GTG for residue 1 !1as Val COMMENT This enzyme catalyzes the formation of glutathione by !1condensing gamma-glutamylcysteine and glycine in the !1presence of ATP. GENETICS !$#gene gsh II !$#start_codon GTG CLASSIFICATION #superfamily Escherichia coli glutathione synthase KEYWORDS ATP; glutathione biosynthesis; ligase SUMMARY #length 308 #molecular-weight 34511 #checksum 1388 SEQUENCE /// ENTRY CEECDL #type complete TITLE D-alanine-D-alanine ligase (EC 6.3.2.4) B - Escherichia coli (strain K-12) ALTERNATE_NAMES alanylalanine synthetase ORGANISM #formal_name Escherichia coli DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 03-Jun-2002 ACCESSIONS A30289; S40602; C37155; D64731 REFERENCE A30289 !$#authors Robinson, A.C.; Kenan, D.J.; Sweeney, J.; Donachie, W.D. !$#journal J. Bacteriol. (1986) 167:809-817 !$#title Further evidence for overlapping transcriptional units in an !1Escherichia coli cell envelope-cell division gene cluster: !1DNA sequence and transcriptional organization of the ddl !1ftsQ region. !$#cross-references MUID:86304170; PMID:3528126 !$#accession A30289 !'##molecule_type DNA !'##residues 1-306 ##label ROB !'##cross-references GB:X55034; NID:g40841; PIDN:CAA38869.1; PID:g40860 !'##experimental_source strain K-12, substrain W3110 REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40602 !'##molecule_type DNA !'##residues 1-306 ##label YUR !'##cross-references EMBL:D10483; NID:g216434; PIDN:BAA01357.1; !1PID:g216506 REFERENCE A37155 !$#authors Dewar, S.J.; Donachie, W.D. !$#journal J. Bacteriol. (1990) 172:6611-6614 !$#title Regulation of expression of the ftsA cell division gene by !1sequences in upstream genes. !$#cross-references MUID:91035283; PMID:2228979 !$#accession C37155 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 300-306 ##label DEW REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64731 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-306 ##label BLAT !'##cross-references GB:AE000118; GB:U00096; NID:g1786262; !1PIDN:AAC73203.1; PID:g1786280; UWGP:b0092 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ddlB; ddl !$#map_position 2 min !$#note gene is located in a large cluster of genes that are !1involved in cell division and cell wall formation FUNCTION !$#description catalyzes ATP-driven formation of alanyl-D-alanine from 2 !1alanine molecules !$#pathway cell wall synthesis !$#note two D-alanine-D-alanine ligases in E. coli (and S. !1typhimurium) encoded by two distinct genes; the different !1cellular roles and relative expression of these genes are !1not yet clear; however, the two enzymes display remarkably !1similar catalytic efficiencies and substrate specificities !1in spite of their differences in size and amino acid !1sequence CLASSIFICATION #superfamily D-alanine-D-alanine ligase KEYWORDS cell wall synthesis; dimer; ligase; magnesium FEATURE !$63-74 #region D-alanine-D-alanine ligase motif 1\ !$245-276 #region D-alanine-D-alanine ligase motif 2 SUMMARY #length 306 #molecular-weight 32839 #checksum 7617 SEQUENCE /// ENTRY CEECDA #type complete TITLE D-alanine-D-alanine ligase (EC 6.3.2.4) A - Escherichia coli (strain K-12) ALTERNATE_NAMES D-alanylalanine synthetase A ORGANISM #formal_name Escherichia coli DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 03-Jun-2002 ACCESSIONS A39182; E64766 REFERENCE A39182 !$#authors Zawadzke, L.E.; Bugg, T.D.H.; Walsh, C.T. !$#journal Biochemistry (1991) 30:1673-1682 !$#title Existence of two D-alanine:D-alanine ligases in Escherichia !1coli: cloning and sequencing of the ddlA gene and !1purification and characterization of the DdlA and DdlB !1enzymes. !$#cross-references MUID:91129242; PMID:1993184 !$#accession A39182 !'##molecule_type DNA !'##residues 1-364 ##label ZAW !'##cross-references GB:J05319; GB:M58467; NID:g145721; PIDN:AAA23671.1; !1PID:g145722 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64766 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-364 ##label BLAT !'##cross-references GB:AE000144; GB:U00096; NID:g1786568; !1PIDN:AAC73484.1; PID:g1786579; UWGP:b0381 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ddlA FUNCTION !$#description catalyzes ATP-driven formation of alanyl-D-alanine from 2 !1alanine molecules !$#pathway cell wall synthesis !$#note two D-alanine-D-alanine ligases in E. coli (and S. !1typhimurium) encoded by two distinct genes; the different !1cellular roles and relative expression of these genes are !1not yet clear; however, the two enzymes display remarkably !1similar catalytic efficiencies and substrate specificities !1in spite of their differences in size and amino acid !1sequence !$#note along with alanine racemase, it makes up the D-alanine !1branch of the peptidoglycan biosynthetic route CLASSIFICATION #superfamily D-alanine-D-alanine ligase KEYWORDS ATP; cell wall synthesis; ligase; nucleotide binding; !1P-loop; peptidoglycan biosynthesis FEATURE !$7-14 #region nucleotide-binding motif A (P-loop)\ !$107-118 #region D-alanine-D-alanine ligase motif 1\ !$293-321 #region D-alanine-D-alanine ligase motif 2 SUMMARY #length 364 #molecular-weight 39315 #checksum 103 SEQUENCE /// ENTRY CEEBDT #type complete TITLE D-alanine-D-alanine ligase (EC 6.3.2.4) A - Salmonella typhimurium ALTERNATE_NAMES D-alanylalanine synthetase ORGANISM #formal_name Salmonella typhimurium DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 03-Jun-2002 ACCESSIONS A28642; B28642 REFERENCE A28642 !$#authors Daub, E.; Zawadzke, L.E.; Botstein, D.; Walsh, C.T. !$#journal Biochemistry (1988) 27:3701-3708 !$#title Isolation, cloning, and sequencing of the Salmonella !1typhimurium ddlA gene with purification and characterization !1of its product, D-alanine:D-alanine ligase (ADP forming). !$#cross-references MUID:88309774; PMID:2841972 !$#accession A28642 !'##molecule_type DNA !'##residues 1-364 ##label DAU !'##cross-references GB:M20793; NID:g153942; PIDN:AAA27056.1; !1PID:g153943 !$#accession B28642 !'##molecule_type protein !'##residues 2-36 ##label DAU2 !'##note 17-Ala was also found COMMENT This enzyme catalyzes the synthesis of D-alanyl-D-alanine !1from L-alanine, which leads to cell wall formation. Along !1with alanine racemase, it makes up the D-alanine branch of !1the peptidoglycan biosynthetic route. COMMENT There are two D-alanine-D-alanine ligases in S. typhimurium !1(and E. coli) encoded by two distinct genes. The different !1cellular roles and relative expression of these genes are !1not yet clear. GENETICS !$#gene ddlA CLASSIFICATION #superfamily D-alanine-D-alanine ligase KEYWORDS cell wall synthesis; ligase SUMMARY #length 364 #molecular-weight 39356 #checksum 1964 SEQUENCE /// ENTRY CESOVM #type complete TITLE vancomycin resistance protein vanA - Enterococcus faecium plasmid pIP816 ORGANISM #formal_name Enterococcus faecium DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 18-Jun-1999 ACCESSIONS S12254; A38812 REFERENCE S12254 !$#authors Dutka-Malen, S.; Molinas, C.; Arthur, M.; Courvalin, P. !$#journal Mol. Gen. Genet. (1990) 224:364-372 !$#title The VANA glycopeptide resistance protein is related to !1D-alanyl-D-alanine ligase cell wall biosynthesis enzymes. !$#cross-references MUID:91094773; PMID:2266943 !$#accession S12254 !'##molecule_type DNA !'##residues 1-343 ##label DU1 !'##cross-references EMBL:X56895; NID:g43335; PIDN:CAA40215.1; !1PID:g43336 !$#accession A38812 !'##molecule_type protein !'##residues 1-9 ##label DU2 COMMENT This protein can complement mutations of D-alanine-D-alanine !1ligase. GENETICS !$#gene vanA !$#genome plasmid CLASSIFICATION #superfamily D-alanine-D-alanine ligase KEYWORDS antibiotic resistance FEATURE !$1-343 #product vanA glycopeptide resistance protein #status !8experimental #label MAT SUMMARY #length 343 #molecular-weight 37443 #checksum 7581 SEQUENCE /// ENTRY CEBSSC #type complete TITLE phosphoribosylaminoimidazolesuccinocarboxamide synthase (EC 6.3.2.6) - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jun-2000 ACCESSIONS D29326; B69684 REFERENCE A29326 !$#authors Ebbole, D.J.; Zalkin, H. !$#journal J. Biol. Chem. (1987) 262:8274-8287 !$#title Cloning and characterization of a 12-gene cluster from !1Bacillus subtilis encoding nine enzymes for de novo purine !1nucleotide synthesis. !$#cross-references MUID:87250425; PMID:3036807 !$#accession D29326 !'##molecule_type DNA !'##residues 1-241 ##label EBB !'##cross-references EMBL:J02732; NID:g143363; PIDN:AAA22677.1; !1PID:g143367 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69684 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-241 ##label KUN !'##cross-references GB:Z99107; GB:AL009126; NID:g2632866; !1PIDN:CAB12465.1; PID:g2632959 !'##experimental_source strain 168 GENETICS !$#gene purC !$#map_position 18 min CLASSIFICATION #superfamily phosphoribosylaminoimidazolesuccinocarboxamide !1synthase KEYWORDS ligase; purine nucleotide biosynthesis SUMMARY #length 241 #molecular-weight 27460 #checksum 8302 SEQUENCE /// ENTRY C36146 #type complete TITLE phosphoribosylaminoimidazolesuccinocarboxamide synthase (EC 6.3.2.6) - Escherichia coli (strain K-12) ALTERNATE_NAMES SAICAR synthetase ORGANISM #formal_name Escherichia coli DATE 30-Nov-1990 #sequence_revision 26-May-1994 #text_change 01-Mar-2002 ACCESSIONS C36146; S25427; C65023 REFERENCE A36146 !$#authors Tiedeman, A.A.; DeMarini, D.J.; Parker, J.; Smith, J.M. !$#journal J. Bacteriol. (1990) 172:6035-6041 !$#title DNA sequence of the purC gene encoding !15'-phosphoribosyl-5-aminoimidazole-4-N-succinocarboxamide !1synthetase and organization of the dapA-purC region of !1Escherichia coli K-12. !$#cross-references MUID:91008982; PMID:2120198 !$#accession C36146 !'##molecule_type DNA !'##residues 1-237 ##label TIE !'##cross-references GB:M33928; NID:g147407; PIDN:AAA24448.1; !1PID:g147410 REFERENCE S25426 !$#authors Bouvier, J.; Pugsley, A.P.; Stragier, P. !$#journal J. Bacteriol. (1991) 173:5523-5531 !$#title A gene for a new lipoprotein in the dapA-purC interval of !1the Escherichia coli chromosome. !$#cross-references MUID:91358331; PMID:1885529 !$#accession S25427 !'##status preliminary !'##molecule_type DNA !'##residues 1-28 ##label BOU !'##cross-references EMBL:X57402; NID:g42125; PIDN:CAA40662.1; !1PID:g42127 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65023 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-237 ##label BLAT !'##cross-references GB:AE000334; GB:U00096; NID:g1788813; !1PIDN:AAC75529.1; PID:g1788820; UWGP:b2476 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene purC CLASSIFICATION #superfamily phosphoribosylaminoimidazolesuccinocarboxamide !1synthase KEYWORDS ligase; purine nucleotide biosynthesis SUMMARY #length 237 #molecular-weight 26995 #checksum 1397 SEQUENCE /// ENTRY JH0489 #type complete TITLE phosphoribosylaminoimidazolesuccinocarboxamide synthase (EC 6.3.2.6) - yeast (Candida maltosa) ALTERNATE_NAMES C-ADE1 protein; SAICAR synthetase ORGANISM #formal_name Candida maltosa DATE 31-Mar-1992 #sequence_revision 26-May-1994 #text_change 16-Jun-2000 ACCESSIONS JH0489; JQ0850 REFERENCE JH0489 !$#authors Sasnauskas, K.; Jomantiene, R.; Geneviciute, E.; Januska, !1A.; Lebedys, J. !$#journal Gene (1991) 107:161-164 !$#title Molecular cloning of the Candida maltosa ADE1 gene. !$#cross-references MUID:92077428; PMID:1743515 !$#accession JH0489 !'##molecule_type DNA !'##residues 1-291 ##label SAS !'##cross-references GB:M58322; NID:g170815; PIDN:AAA34318.1; !1PID:g170816 REFERENCE JQ0850 !$#authors Kawai, S.; Hikiji, T.; Murao, S.; Takagi, M.; Yano, K. !$#journal Agric. Biol. Chem. (1991) 55:59-65 !$#title Isolation and sequencing of a gene, C-ADE1, and its use for !1a host-vector system in Candida maltosa with two genetic !1markers. !$#cross-references MUID:91248497; PMID:1368674 !$#accession JQ0850 !'##molecule_type DNA !'##residues 1-291 ##label KAW !'##cross-references GB:D00855; NID:g218520; PIDN:BAA00731.1; !1PID:g218521 !'##experimental_source strain CH1 GENETICS !$#gene ADE1 CLASSIFICATION #superfamily phosphoribosylaminoimidazolesuccinocarboxamide !1synthase KEYWORDS ligase; purine nucleotide biosynthesis SUMMARY #length 291 #molecular-weight 32941 #checksum 2251 SEQUENCE /// ENTRY JQ1395 #type complete TITLE phosphoribosylaminoimidazolesuccinocarboxamide synthase (EC 6.3.2.6) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YAR015w; SAICAR synthetase ORGANISM #formal_name Saccharomyces cerevisiae DATE 17-Jul-1992 #sequence_revision 03-Nov-1995 #text_change 05-Nov-1999 ACCESSIONS S20122; S40905; S25679; JQ1395 REFERENCE S20121 !$#authors Davies, C.J.; Hutchison III, C.A. !$#journal Nucleic Acids Res. (1991) 19:5731-5738 !$#title A directed DNA sequencing strategy based upon Tn3 transposon !1mutagenesis: application to the ADE1 locus on Saccharomyces !1cerevisiae chromosome I. !$#cross-references MUID:92051323; PMID:1658741 !$#accession S20122 !'##molecule_type DNA !'##residues 1-306 ##label DAV !'##cross-references EMBL:M67445; NID:g170997; PIDN:AAA34398.1; !1PID:g170999 REFERENCE S40891 !$#authors Clark, M.W.; Keng, T.; Storms, R.K.; Zhong, W.; Fortin, N.; !1Zeng, B.; Delaney, S.; Ouellette, F.B.; Barton, A.B.; !1Kaback, D.B.; Bussey, H. !$#submission submitted to the EMBL Data Library, November 1993 !$#description Sequencing of chromosome I of Saccharomyces cerevisiae: !1Analysis of the 42 Kbp SP07-CENI-CDC15 REGION. !$#accession S40905 !'##molecule_type DNA !'##residues 1-306 ##label CLA !'##cross-references EMBL:L22015; NID:g1339990; PIDN:AAC04963.1; !1PID:g349755; GSPDB:GN00001; MIPS:YAR015w REFERENCE S23580 !$#authors Schweitzer, B.; Philippsen, P. !$#journal Mol. Gen. Genet. (1992) 234:164-167 !$#title NPK1, a nonessential protein kinase gene in Saccharomyces !1cerevisiae with similarity to Aspergillus nidulans nimA. !$#cross-references MUID:92357012; PMID:1495480 !$#accession S25679 !'##molecule_type DNA !'##residues 285-306 ##label SCH !'##cross-references EMBL:X60549; NID:g298024; PIDN:CAA43043.1; !1PID:g4043 REFERENCE JQ1395 !$#authors Myasnikov, A.N.; Sasnauskas, K.V.; Janulaitis, A.A.; !1Smirnov, M.N. !$#journal Gene (1991) 109:143-147 !$#title The Saccharomyces cerevisiae ADE1 gene: structure, !1overexpression and possible regulation by general amino acid !1control. !$#cross-references MUID:92097943; PMID:1756975 !$#accession JQ1395 !'##molecule_type DNA !'##residues 1-184,'G',186-306 ##label MYA !'##cross-references GB:M61209; NID:g170995; PIDN:AAA34396.1; !1PID:g170996 !'##experimental_source strain FH4C !'##note the authors translated the codon TAC for residue 98 as Asp GENETICS !$#gene SGD:ADE1; MIPS:YAR015w !'##cross-references SGD:S0000070; MIPS:YAR015w !$#map_position 1R FUNCTION !$#description catalyzes formation of !1N-succinyl-5-aminoimidazole-4-carboxamide ribotide from !14-carboxy-5-aminoimidazole ribotide and aspartic acid !$#pathway purine biosynthesis CLASSIFICATION #superfamily phosphoribosylaminoimidazolesuccinocarboxamide !1synthase KEYWORDS ligase; purine nucleotide biosynthesis SUMMARY #length 306 #molecular-weight 34603 #checksum 4488 SEQUENCE /// ENTRY CEECAM #type complete TITLE UDP-N-acetylmuramate-alanine ligase (EC 6.3.2.8) murC [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES UDP-N-acetylmuramoyl-L-alanine synthetase ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Jun-2002 ACCESSIONS JQ0545; S40601; S65354; C64731 REFERENCE JQ0544 !$#authors Ikeda, M.; Wachi, M.; Jung, H.K.; Ishino, F.; Matsuhashi, M. !$#journal Nucleic Acids Res. (1990) 18:4014 !$#title Nucleotide sequence involving murG and murC in the mra gene !1cluster region of Escherichia coli. !$#cross-references MUID:90326550; PMID:2197603 !$#accession JQ0545 !'##molecule_type DNA !'##residues 1-491 ##label IKE !'##cross-references EMBL:X52644; NID:g42053; PIDN:CAA36868.1; !1PID:g42056 REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40601 !'##molecule_type DNA !'##residues 1-491 ##label YUR !'##cross-references EMBL:D10483; NID:g216434; PIDN:BAA01356.1; !1PID:g216505 REFERENCE S65354 !$#authors Liger, D.; Masson, A.; Blanot, D.; van Heijenoort, J.; !1Parquet, C. !$#journal Eur. J. Biochem. (1995) 230:80-87 !$#title Over-production, purification and properties of the !1uridine-diphosphate-N-acetylmuramate:L-alanine ligase from !1Escherichia coli. !$#cross-references MUID:95324553; PMID:7601127 !$#accession S65354 !'##status preliminary !'##molecule_type protein !'##residues 1-14 ##label LIG REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64731 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-491 ##label BLAT !'##cross-references GB:AE000118; GB:U00096; NID:g1786262; !1PIDN:AAC73202.1; PID:g1786279; UWGP:b0091 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene murC !$#map_position 2 min FUNCTION !$#description one of the ligases responsible for the synthesis of !1UPD-N-acetylmuramyl pentapeptide, an intermediate in !1cell-wall biosynthesis !$#pathway peptidoglycan biosynthesis CLASSIFICATION #superfamily UDP-N-acetylmuramate-alanine ligase KEYWORDS ATP; cell division; cell wall; ligase; peptidoglycan !1biosynthesis SUMMARY #length 491 #molecular-weight 53626 #checksum 8296 SEQUENCE /// ENTRY CEECME #type complete TITLE UDP-N-acetylmuramoylalanine-D-glutamate ligase (EC 6.3.2.9) - Escherichia coli (strain K-12) ALTERNATE_NAMES UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase ORGANISM #formal_name Escherichia coli DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 03-Jun-2002 ACCESSIONS S08396; S07581; S40598; S19573; B32581; H64730 REFERENCE S08395 !$#authors Ikeda, M.; Wachi, M.; Ishino, F.; Matsuhashi, M. !$#journal Nucleic Acids Res. (1990) 18:1058 !$#title Nucleotide sequence involving murD and an open reading frame !1ORF-Y spacing murF and ftsW in Escherichia coli. !$#cross-references MUID:90192099; PMID:2179861 !$#accession S08396 !'##molecule_type DNA !'##residues 1-438 ##label IKE !'##cross-references EMBL:X51584; NID:g42058; PIDN:CAA35933.1; !1PID:g42060 REFERENCE S07581 !$#authors Mengin-Lecreulx, D.; van Heijenoort, J. !$#journal Nucleic Acids Res. (1990) 18:183 !$#title Nucleotide sequence of the murD gene encoding the !1UDP-MurNAc-L-Ala-D-Glu synthetase of Escherichia coli. !$#cross-references MUID:90174916; PMID:2129548 !$#accession S07581 !'##molecule_type DNA !'##residues 1-27,'A',29-72,84-173,'T',175-275,'RV',278-438 ##label MEN !'##cross-references EMBL:X17609; NID:g42045; PIDN:CAA35611.1; !1PID:g42046 !'##experimental_source strain K-12 REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40598 !'##molecule_type DNA !'##residues 1-438 ##label YUR !'##cross-references EMBL:D10483; NID:g216434; PIDN:BAA01353.1; !1PID:g216502 REFERENCE S19573 !$#authors Pratviel-Sosa, F.; Mengin-Lecreulx, D.; van Heijenoort, J. !$#journal Eur. J. Biochem. (1991) 202:1169-1176 !$#title Over-production, purification and properties of the uridine !1diphosphate N-acetylmuramoyl-L-alanine: D-glutamate ligase !1from Escherichia coli. !$#cross-references MUID:92111492; PMID:1765076 !$#accession S19573 !'##molecule_type protein !'##residues 2-20 ##label PRA REFERENCE A32581 !$#authors Ikeda, M.; Sato, T.; Wachi, M.; Jung, H.K.; Ishino, F.; !1Kobayashi, Y.; Matsuhashi, M. !$#journal J. Bacteriol. (1989) 171:6375-6378 !$#title Structural similarity among Escherichia coli FtsW and RodA !1proteins and Bacillus subtilis SpoVE protein, which function !1in cell division, cell elongation, and spore formation, !1respectively. !$#cross-references MUID:90036736; PMID:2509435 !$#accession B32581 !'##molecule_type DNA !'##residues 376-438 ##label IK2 !'##cross-references GB:M30807; NID:g146038; PIDN:AAA83858.1; !1PID:g1128955 !'##experimental_source strain JLB17 !'##note the authors translated the codon ATG for residue 407 as Trp REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64730 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-438 ##label BLAT !'##cross-references GB:AE000118; GB:U00096; NID:g1786262; !1PIDN:AAC73199.1; PID:g1786276; UWGP:b0088 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene murD !$#map_position 2 min FUNCTION !$#pathway peptidoglycan biosynthesis CLASSIFICATION #superfamily UDP-N-acetylmuramate-alanine ligase KEYWORDS ATP; cell division; cell wall; ligase; peptidoglycan !1biosynthesis SUMMARY #length 438 #molecular-weight 46973 #checksum 8510 SEQUENCE /// ENTRY SYECFG #type complete TITLE tetrahydrofolylpolyglutamate synthase (EC 6.3.2.17) / dihydrofolate synthase (EC 6.3.2.12) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS A65004; A29805; D29803; I41213 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65004 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-422 ##label BLAT !'##cross-references GB:AE000320; GB:U00096; NID:g1788647; !1PIDN:AAC75375.1; PID:g1788654; UWGP:b2315 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A29805 !$#authors Bognar, A.L.; Osborne, C.; Shane, B. !$#journal J. Biol. Chem. (1987) 262:12337-12343 !$#title Primary structure of the Escherichia coli folC gene and its !1folylpolyglutamate synthetase-dihydrofolate synthetase !1product and regulation of expression by an upstream gene. !$#cross-references MUID:87308246; PMID:3040739 !$#accession A29805 !'##molecule_type DNA !'##residues 1-325,'M',327-422 ##label BOG !'##cross-references GB:M32445; NID:g146018; PIDN:AAA23808.1; !1PID:g146020 REFERENCE A29803 !$#authors Nonet, M.L.; Marvel, C.C.; Tolan, D.R. !$#journal J. Biol. Chem. (1987) 262:12209-12217 !$#title The hisT-purF region of the Escherichia coli K-12 !1chromosome. Identification of additional genes of the hisT !1and purF operons. !$#cross-references MUID:87308226; PMID:3040734 !$#accession D29803 !'##molecule_type DNA !'##residues 1-328,'A',329-390,'EP',393-422 ##label NON !'##cross-references GB:M68934; GB:J02800; NID:g146359; PIDN:AAA23966.1; !1PID:g146365 REFERENCE I41212 !$#authors Bogner, A.L.; Osborne, C.; Shane, B. !$#journal J. Biol. Chem. (1987) 262:12334-12343 !$#title Primary structure of the Escherichia coli folC gene and its !1folylpolyglutamate synthetase-dihydrofolate synthetase !1product and regulation of expression by an upstream gene. !$#accession I41213 !'##status preliminary !'##molecule_type DNA !'##residues 1-325,'M',327-422 ##label RES !'##cross-references GB:J02808; NID:g146007; PIDN:AAA23802.1; !1PID:g146009 COMMENT This enzyme catalyzes the conversion of folates to folate !1polyglutamate derivatives, the major cellular forms of !1folate coenzymes involved in one-carbon metabolism. This !1enzyme has dihydrofolate synthetase activity; it catalyzes !1the formation of dihydrofolate dihydropteroate and !1glutamate. GENETICS !$#gene folC; dedC !$#map_position 50 min CLASSIFICATION #superfamily folylpolyglutamate synthase KEYWORDS ligase; multifunctional enzyme; one-carbon metabolism SUMMARY #length 422 #molecular-weight 45405 #checksum 2848 SEQUENCE /// ENTRY UQXFAS #type complete TITLE ubiquitin-protein ligase (EC 6.3.2.19) E2 - African swine fever virus (strain BA71V) ORGANISM #formal_name African swine fever virus, ASFV DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 03-Jun-2002 ACCESSIONS F39448 REFERENCE A39448 !$#authors Rodriguez, J.M.; Salas, M.L.; Vinuela, E. !$#journal Virology (1992) 186:40-52 !$#title Genes homologous to ubiquitin-conjugating proteins and !1eukaryotic transcription factor SII in African swine fever !1virus. !$#cross-references MUID:92087485; PMID:1309282 !$#accession F39448 !'##molecule_type DNA !'##residues 1-215 ##label ROD !'##cross-references GB:M77121; NID:g210618; PIDN:AAA42704.1; !1PID:g210624 CLASSIFICATION #superfamily African swine fever virus ubiquitin-protein !1ligase E2 KEYWORDS ligase; protein degradation SUMMARY #length 215 #molecular-weight 24737 #checksum 9157 SEQUENCE /// ENTRY S19158 #type complete TITLE ubiquitin-protein ligase (EC 6.3.2.19) E2 - African swine fever virus (isolate Malawi LIL20/1) ORGANISM #formal_name African swine fever virus, ASFV DATE 20-Feb-1995 #sequence_revision 20-Feb-1995 #text_change 03-Jun-2002 ACCESSIONS S19158 REFERENCE S19158 !$#authors Hingamp, P.M.; Arnold, J.E.; Mayer, R.J.; Dixon, L.K. !$#journal EMBO J. (1992) 11:361-366 !$#title A ubiquitin conjugating enzyme encoded by African swine !1fever virus. !$#cross-references MUID:92155177; PMID:1310934 !$#accession S19158 !'##status preliminary !'##molecule_type DNA !'##residues 1-213 ##label HIN !'##cross-references EMBL:X62440; NID:g58649; PIDN:CAA44305.1; !1PID:g58650 CLASSIFICATION #superfamily African swine fever virus ubiquitin-protein !1ligase E2 KEYWORDS ligase; protein degradation SUMMARY #length 213 #molecular-weight 24468 #checksum 3131 SEQUENCE /// ENTRY S12493 #type complete TITLE ubiquitin-protein ligase (EC 6.3.2.19) UBC1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YD9395.10; protein YDR177w; ubiquitin-conjugating enzyme UBC1 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S12493; S49773 REFERENCE S12493 !$#authors Seufert, W.; McGrath, J.P.; Jentsch, S. !$#journal EMBO J. (1990) 9:4535-4541 !$#title UBC1 encodes a novel member of an essential subfamily of !1yeast ubiquitin-conjugating enzymes involved in protein !1degradation. !$#cross-references MUID:91092279; PMID:2265617 !$#accession S12493 !'##molecule_type DNA !'##residues 1-215 ##label SEU !'##cross-references EMBL:X56402; NID:g4716; PIDN:CAA39812.1; PID:g4717 REFERENCE S49764 !$#authors Murphy, L.; Harris, D.E. !$#submission submitted to the EMBL Data Library, November 1994 !$#accession S49773 !'##molecule_type DNA !'##residues 1-215 ##label MUR !'##cross-references EMBL:Z46727; NID:g1289283; PIDN:CAA86682.1; !1PID:g1289292; GSPDB:GN00004; MIPS:YDR177w GENETICS !$#gene SGD:UBC1; MIPS:YDR177w !'##cross-references SGD:S0002584; MIPS:YDR177w !$#map_position 4R FUNCTION !$#description cell cycle control; DNA repair; ligase; protein degradation CLASSIFICATION #superfamily yeast ubiquitin-protein ligase UBC1 KEYWORDS cell cycle control; DNA repair; ligase; protein degradation SUMMARY #length 215 #molecular-weight 24178 #checksum 1205 SEQUENCE /// ENTRY S43217 #type complete TITLE ubiquitin-protein ligase (EC 6.3.2.19) RSP5 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES E6-AP-like protein ubiquitin ligase; protein YER125w; PUB1 protein ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S43217; S50628; S70050 REFERENCE S30812 !$#authors Mulligan, J.T.; Dietrich, F.S.; Hennessey, K.M.; Sehl, P.; !1Komp, C.; Wei, Y.; Taylor, P.; Nakahara, K.; Roberts, D.; !1Davis, R.W. !$#submission submitted to the EMBL Data Library, February 1993 !$#accession S43217 !'##molecule_type DNA !'##residues 1-809 ##label MUL !'##cross-references GB:U18916; EMBL:L11119; NID:g1384128; !1PIDN:AAC03223.1; PID:g603364 REFERENCE S50628 !$#authors Dietrich, F.S. !$#submission submitted to the EMBL Data Library, December 1994 !$#description The sequence of S. cerevisiae cosmids 9781, 8198, 9115, !19981, and lambda clones 3955 and 6052. !$#accession S50628 !'##molecule_type DNA !'##residues 1-809 ##label DIE !'##cross-references EMBL:U18916; NID:g1384128; PIDN:AAC03223.1; !1PID:g603364; GSPDB:GN00005; MIPS:YER125w REFERENCE S70050 !$#authors Hein, C.; Springael, J.Y.; Volland, C.; Haguenauer-Tsapis, !1R.; Andre, B. !$#journal Mol. Microbiol. (1995) 18:77-87 !$#title NPI1, an essential yeast gene involved in induced !1degradation of Gap1 and Fur4 permeases, encodes the Rsp5 !1ubiquitin-protein ligase. !$#cross-references MUID:96154942; PMID:8596462 !$#accession S70050 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type DNA !'##residues 1-101 ##label HEI GENETICS !$#gene SGD:RSP5; PUB1; NPI1; MIPS:YER125w !'##cross-references MIPS:YER125w; SGD:S0000927 !$#map_position 5R FUNCTION !$#description involved in endocytosis of GAP1 protein and FUR4 protein; !1binds and ubiquinates RBP1 protein CLASSIFICATION #superfamily yeast ubiquitin-protein ligase; WW repeat !1homology KEYWORDS ligase FEATURE !$229-266 #domain WW repeat homology #label WW1\ !$331-368 #domain WW repeat homology #label WW2\ !$387-424 #domain WW repeat homology #label WW3 SUMMARY #length 809 #molecular-weight 91816 #checksum 9023 SEQUENCE /// ENTRY S66562 #type complete TITLE ubiquitin-protein ligase (EC 6.3.2.19) - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES E6-AP-like protein ubiquitin ligase ORGANISM #formal_name Schizosaccharomyces pombe DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S66562; T45159 REFERENCE S66562 !$#authors Nefsky, B.; Beach, D. !$#journal EMBO J. (1996) 15:1301-1312 !$#title Pub1 acts as an E6-AP-like protein ubiquitin ligase in the !1degradation of cdc25. !$#cross-references MUID:96205868; PMID:8635463 !$#accession S66562 !'##status preliminary; nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-766 ##label NEF !'##cross-references GB:U66716; NID:g1519443; PIDN:AAB07514.1; !1PID:g1519444 REFERENCE Z22935 !$#authors Nefsky, B.S.; Beach, D. !$#submission submitted to the EMBL Data Library, August 1996 !$#description Pub1 acts as an E6-AP-like protein ubiquitin ligase in the !1degradation of cdc25. !$#accession T45159 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-766 ##label NE2 !'##cross-references EMBL:Y07592; PIDN:CAA68867.1 GENETICS !$#gene pub1 CLASSIFICATION #superfamily yeast ubiquitin-protein ligase; WW repeat !1homology KEYWORDS ligase FEATURE !$205-242 #domain WW repeat homology #label WW1\ !$288-325 #domain WW repeat homology #label WW2\ !$345-382 #domain WW repeat homology #label WW3 SUMMARY #length 766 #molecular-weight 87138 #checksum 7931 SEQUENCE /// ENTRY D64823 #type complete TITLE ribosomal protein S6-glutamic acid ligase (EC 6.3.2.-) - Escherichia coli (strain K-12) ALTERNATE_NAMES ribosomal protein S6 modification protein ORGANISM #formal_name Escherichia coli DATE 06-Nov-1998 #sequence_revision 06-Nov-1998 #text_change 01-Mar-2002 ACCESSIONS D64823; S04775 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64823 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-300 ##label BLAT !'##cross-references GB:AE000187; GB:U00096; NID:g1787070; !1PIDN:AAC73939.1; PID:g1787076; UWGP:b0852 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S04774 !$#authors Kang, W.K.; Icho, T.; Isono, S.; Kitakawa, M.; Isono, K. !$#journal Mol. Gen. Genet. (1989) 217:281-288 !$#title Characterization of the gene rimK responsible for the !1addition of glutamic acid residues to the C-terminus of !1ribosomal protein S6 in Escherichia coli K12. !$#cross-references MUID:89364710; PMID:2570347 !$#accession S04775 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 'MERSIRVSGW',19-300 ##label KAN !'##cross-references GB:X15859; NID:g42745; PIDN:CAA33868.1; PID:g42747 COMMENT For ribosomal protein S6, see PIR:R3EC6. GENETICS !$#gene rimK !$#map_position 18.7-19.0 min FUNCTION !$#description catalyzes the addition of glutamic acids to the carboxyl end !1of ribosomal protein S6 CLASSIFICATION #superfamily ribosomal protein S6-glutamic acid ligase KEYWORDS ligase SUMMARY #length 300 #molecular-weight 32436 #checksum 3104 SEQUENCE /// ENTRY H64127 #type complete TITLE ribosomal protein S6-glutamic acid ligase (EC 6.3.2.-) - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES rimK protein homolog ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS H64127 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession H64127 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-302 ##label TIGR !'##cross-references GB:U32828; GB:L42023; NID:g1574362; !1PIDN:AAC23177.1; PID:g1574372; TIGR:HI1531 CLASSIFICATION #superfamily ribosomal protein S6-glutamic acid ligase KEYWORDS ligase SUMMARY #length 302 #molecular-weight 33262 #checksum 6695 SEQUENCE /// ENTRY H64424 #type complete TITLE probable ribosomal protein S6-glutamic acid ligase (EC 6.3.2.-) II - Methanococcus jannaschii ALTERNATE_NAMES ribosomal protein S6 modification protein II ORGANISM #formal_name Methanococcus jannaschii DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 21-Jul-2000 ACCESSIONS H64424 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession H64424 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-290 ##label BUL !'##cross-references GB:U67542; GB:L77117; NID:g2826356; !1PIDN:AAB99004.1; PID:g1591661; TIGR:MJ1001 GENETICS !$#map_position FOR930007-930879 FUNCTION !$#description catalyzes the addition of glutamic acids to the carboxyl end !1of ribosomal protein S6 CLASSIFICATION #superfamily ribosomal protein S6-glutamic acid ligase KEYWORDS ligase SUMMARY #length 290 #molecular-weight 33390 #checksum 6929 SEQUENCE /// ENTRY AJECPC #type complete TITLE phosphoribosylformylglycinamidine cyclo-ligase (EC 6.3.3.1) - Escherichia coli (strain K-12) ALTERNATE_NAMES 5'-phosphoribosyl-5-aminoimidazole synthetase ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 01-Mar-2002 ACCESSIONS A25955; B65026 REFERENCE A25955 !$#authors Smith, J.M.; Daum III, H.A. !$#journal J. Biol. Chem. (1986) 261:10632-10636 !$#title Nucleotide sequence of the purM gene encoding !15'-phosphoribosyl-5-aminoimidazole synthetase of Escherichia !1coli K12. !$#cross-references MUID:86278135; PMID:3015935 !$#accession A25955 !'##molecule_type DNA !'##residues 1-345 ##label SMI !'##cross-references GB:M13747; GB:M17287; NID:g147424; PIDN:AAA83898.1; !1PID:g147425 !'##experimental_source strain K12 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65026 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-345 ##label BLAT !'##cross-references GB:AE000336; GB:U00096; NID:g1788839; !1PIDN:AAC75552.1; PID:g1788845; UWGP:b2499 !'##experimental_source strain K-12, substrain MG1655 COMMENT This enzyme catalyzes the fifth step, the ATP-dependent !1synthesis of 5'-phosphoribosyl-5-aminoimidazole from !15'-phosphoribosylformylglycinamide, in the de novo synthesis !1of purine nucleotides. GENETICS !$#gene purM !$#map_position 54 min !$#start_codon GTG CLASSIFICATION #superfamily phosphoribosylformylglycinamidine cyclo-ligase; !1phosphoribosylformylglycinamidine cyclo-ligase homology KEYWORDS cyclo-ligase; purine nucleotide biosynthesis FEATURE !$9-333 #domain phosphoribosylformylglycinamidine !8cyclo-ligase homology #label PFCL SUMMARY #length 345 #molecular-weight 36854 #checksum 946 SEQUENCE /// ENTRY AJBSCL #type complete TITLE phosphoribosylformylglycinamidine cyclo-ligase (EC 6.3.3.1) [validated] - Bacillus subtilis ALTERNATE_NAMES phosphoribosylaminoimidazole synthetase ORGANISM #formal_name Bacillus subtilis DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jun-2000 ACCESSIONS H29326; A69685 REFERENCE A29326 !$#authors Ebbole, D.J.; Zalkin, H. !$#journal J. Biol. Chem. (1987) 262:8274-8287 !$#title Cloning and characterization of a 12-gene cluster from !1Bacillus subtilis encoding nine enzymes for de novo purine !1nucleotide synthesis. !$#cross-references MUID:87250425; PMID:3036807 !$#accession H29326 !'##molecule_type DNA !'##residues 1-346 ##label EBB !'##cross-references EMBL:J02732; NID:g143363; PIDN:AAA22681.1; !1PID:g143371 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69685 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-346 ##label KUN !'##cross-references GB:Z99107; GB:AL009126; NID:g2632866; !1PIDN:CAB12470.1; PID:g2632964 !'##experimental_source strain 168 GENETICS !$#gene purM !$#map_position 18 min FUNCTION !$#description EC 6.3.3.1 [validated, MUID:87250425] CLASSIFICATION #superfamily phosphoribosylformylglycinamidine cyclo-ligase; !1phosphoribosylformylglycinamidine cyclo-ligase homology KEYWORDS cyclo-ligase; purine nucleotide biosynthesis FEATURE !$5-332 #domain phosphoribosylformylglycinamidine !8cyclo-ligase homology #label PFCL SUMMARY #length 346 #molecular-weight 37052 #checksum 9956 SEQUENCE /// ENTRY JQ2256 #type complete TITLE phosphoribosylformylglycinamidine cyclo-ligase (EC 6.3.3.1) precursor - Arabidopsis thaliana ALTERNATE_NAMES 5'-phosphoribosyl-5-aminoimidazole synthetase; protein F28P10.10 ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 30-Sep-1993 #sequence_revision 28-Oct-1994 #text_change 15-Oct-1999 ACCESSIONS JQ2256; T06719 REFERENCE JQ2256 !$#authors Senecoff, J.F.; Meagher, R.B. !$#journal Plant Physiol. (1993) 102:387-399 !$#title Isolating the Arabidopsis thaliana genes for de novo purine !1synthesis by suppression of Escherichia coli mutants. I. !15'-phosphoribosyl-5-aminoimidazole synthetase. !$#cross-references MUID:94151435; PMID:8108507 !$#accession JQ2256 !'##molecule_type DNA !'##residues 1-355 ##label SEN !'##cross-references GB:L12457; NID:g289187; PIDN:AAC37341.1; !1PID:g289188 REFERENCE Z15793 !$#authors Quetier, F.; Choisne, N.; Robert, C.; Brottier, P.; Wincker, !1P.; Cattolico, L.; Artiguenave, F.; Saurin, W.; Weissenbach, !1J.; Salanoubat, M.; Mewes, H.W.; Mayer, K.F.X.; Schueller, !1C. !$#submission submitted to the Protein Sequence Database, April 1999 !$#accession T06719 !'##molecule_type DNA !'##residues 1-125 ##label QUE !'##cross-references EMBL:AL049655; ATSP:F28P10.10; GSPDB:GN00061 !'##experimental_source cultivar Columbia; BAC clone F28P10 COMMENT This enzyme is involved in the fifth step of the purine !1biosynthetic pathway, converting !15'-phosphoribosyl-N-formylglycinamidine into 5'- !1phosphoribosyl-5-aminoimidazole. GENETICS !$#gene ATSP:F28P10.10 !$#map_position 3 !$#introns 102/1 CLASSIFICATION #superfamily phosphoribosylformylglycinamidine cyclo-ligase; !1phosphoribosylformylglycinamidine cyclo-ligase homology KEYWORDS cyclo-ligase; purine nucleotide biosynthesis FEATURE !$1-58 #domain signal sequence #status predicted #label SIG\ !$59-355 #product phosphoribosylformylglycinamidine !8cyclo-ligase #status predicted #label MAT\ !$68-355 #domain phosphoribosylformylglycinamidine !8cyclo-ligase homology #label PFCL SUMMARY #length 355 #molecular-weight 37750 #checksum 2318 SEQUENCE /// ENTRY S75786 #type complete TITLE phosphoribosylformylglycinamidine cyclo-ligase (EC 6.3.3.1) - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES 5'-phosphoribosyl-5-aminoimidazole synthetase; protein slr0838 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S75786 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75786 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-341 ##label KAN !'##cross-references EMBL:D64003; GB:AB001339; NID:g1001200; !1PIDN:BAA10521.1; PID:g1001275 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene purM CLASSIFICATION #superfamily phosphoribosylformylglycinamidine cyclo-ligase; !1phosphoribosylformylglycinamidine cyclo-ligase homology KEYWORDS cyclo-ligase; purine nucleotide biosynthesis FEATURE !$3-330 #domain phosphoribosylformylglycinamidine !8cyclo-ligase homology #label PFCL SUMMARY #length 341 #molecular-weight 36164 #checksum 7998 SEQUENCE /// ENTRY B64462 #type complete TITLE dethiobiotin synthase (EC 6.3.3.3) - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B64462 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession B64462 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-248 ##label BUL !'##cross-references GB:U67570; GB:L77117; NID:g2826392; !1PIDN:AAB99306.1; PID:g1591937; TIGR:MJ1299 GENETICS !$#map_position FOR1246520-1247266 !$#start_codon TTG CLASSIFICATION #superfamily dethiobiotin synthase KEYWORDS cyclo-ligase SUMMARY #length 248 #molecular-weight 28006 #checksum 7208 SEQUENCE /// ENTRY E64523 #type complete TITLE dethiobiotin synthetase - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS E64523 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession E64523 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-218 ##label TOM !'##cross-references GB:AE000525; GB:AE000511; NID:g2313102; !1PIDN:AAD07100.1; PID:g2313106; TIGR:HP0029 CLASSIFICATION #superfamily dethiobiotin synthase SUMMARY #length 218 #molecular-weight 24407 #checksum 1048 SEQUENCE /// ENTRY B64129 #type complete TITLE dethiobiotin synthase homolog HI1550 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B64129 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession B64129 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-191 ##label TIGR !'##cross-references GB:U32830; GB:L42023; NID:g1574389; !1PIDN:AAC23200.1; PID:g1574395; TIGR:HI1550 CLASSIFICATION #superfamily dethiobiotin synthase SUMMARY #length 191 #molecular-weight 21096 #checksum 3564 SEQUENCE /// ENTRY G69830 #type complete TITLE lipoate-protein ligase homolog yhfJ - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS G69830 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69830 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-331 ##label KUN !'##cross-references GB:Z99109; GB:AL009126; NID:g2633260; !1PIDN:CAB12865.1; PID:g2633361 !'##experimental_source strain 168 GENETICS !$#gene yhfJ CLASSIFICATION #superfamily lipoate-protein ligase SUMMARY #length 331 #molecular-weight 38020 #checksum 7034 SEQUENCE /// ENTRY S73775 #type complete TITLE lipoate protein ligase lplA - Mycoplasma pneumoniae (strain ATCC 29342) ALTERNATE_NAMES hypothetical protein F11_orf339 ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Dec-1999 ACCESSIONS S73775 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73775 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-339 ##label HIM !'##cross-references EMBL:AE000044; GB:U00089; NID:g1674130; !1PIDN:AAB96097.1; PID:g1674137 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#gene lplA !$#genetic_code SGC3 CLASSIFICATION #superfamily lipoate-protein ligase SUMMARY #length 339 #molecular-weight 39194 #checksum 1655 SEQUENCE /// ENTRY A54035 #type complete TITLE lipoate-protein ligase (EC 6.3.4.-) A [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 28-May-1999 #sequence_revision 28-May-1999 #text_change 01-Mar-2002 ACCESSIONS A54035; S56610; PQ0014; A65254; S56124 REFERENCE A54035 !$#authors Morris, T.W.; Reed, K.E.; Cronan Jr., J.E. !$#journal J. Biol. Chem. (1994) 269:16091-16100 !$#title Identification of the gene encoding lipoate-protein ligase A !1of Escherichia coli. Molecular cloning and characterization !1of the lplA gene and gene product. !$#cross-references MUID:94266793; PMID:8206909 !$#accession A54035 !'##status preliminary !'##molecule_type DNA !'##residues 1-338 ##label MOR !'##cross-references GB:L27665; NID:g504494; PIDN:AAA21740.1; !1PID:g504496 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56610 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-338 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97282.1; !1PID:g537226 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A26227 !$#authors Neuwald, A.F.; Stauffer, G.V. !$#journal Gene (1989) 82:219-228 !$#title An Escherichia coli membrane protein with a unique signal !1sequence. !$#cross-references MUID:90060811; PMID:2684780 !$#accession PQ0014 !'##molecule_type DNA !'##residues 1-68 ##label NEU !'##cross-references GB:X03046; GB:M30784; NID:g432632; PIDN:CAA26854.1; !1PID:g432634 !'##experimental_source strain K12 !'##note the gene encoding this protein is located downstream of the smp !1gene REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65254 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-338 ##label BLAT !'##cross-references GB:AE000508; GB:U00096; NID:g2367382; !1PIDN:AAC77339.1; PID:g1790846; UWGP:b4386 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S56124 !$#authors Green, D.E.; Morris, T.W.; Green, J.; Cronan Jr., J.E.; !1Guest, J.R. !$#journal Biochem. J. (1995) 309:853-862 !$#title Purification and properties of the lipoate protein ligase of !1Escherichia coli. !$#cross-references MUID:95366962; PMID:7639702 !$#accession S56124 !'##status preliminary !'##molecule_type protein !'##residues 'RS',170-176;180-184 ##label GRE GENETICS !$#gene lplA; yjjF !$#map_position 100 min FUNCTION !$#description EC 6.3.4.-; lipoate-protein ligase [validated, !1MUID:94266793]; catalyzes first the reaction of lipoic acid !1and ATP to form lipoyl-AMP and pyrophosphate, then the !1formation N6-lipoyl-lysine from a specific lysine residue in !1lipoate-dependent enzymes CLASSIFICATION #superfamily lipoate-protein ligase KEYWORDS ligase SUMMARY #length 338 #molecular-weight 37926 #checksum 4113 SEQUENCE /// ENTRY S56818 #type complete TITLE hypothetical protein YJL046w - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein J1171 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S56818 REFERENCE S56793 !$#authors Pohl, T.M.; Aljinovic, G. !$#submission submitted to the Protein Sequence Database, September 1995 !$#accession S56818 !'##molecule_type DNA !'##residues 1-451 ##label TOV !'##cross-references EMBL:Z49321; NID:g1008176; PIDN:CAA89337.1; !1PID:g1008177; GSPDB:GN00010; MIPS:YJL046w GENETICS !$#gene MIPS:YJL046w !'##cross-references SGD:S0003582 !$#map_position 10L CLASSIFICATION #superfamily lipoate-protein ligase SUMMARY #length 451 #molecular-weight 52085 #checksum 224 SEQUENCE /// ENTRY SYHUTP #type complete TITLE CTP synthase (EC 6.3.4.2) - human ALTERNATE_NAMES CTP-synthetase; UTP-ammonia ligase ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 18-Jun-1999 ACCESSIONS S12791 REFERENCE S12791 !$#authors Yamauchi, M.; Yamauchi, N.; Meuth, M. !$#journal EMBO J. (1990) 9:2095-2099 !$#title Molecular cloning of the human CTP synthetase gene by !1functional complementation with purified human metaphase !1chromosomes. !$#cross-references MUID:90291972; PMID:2113467 !$#accession S12791 !'##molecule_type mRNA !'##residues 1-591 ##label YAM !'##cross-references GB:X52142; NID:g30292; PIDN:CAA36386.1; PID:g30293 COMMENT This enzyme is a glutamine amidotransferase that catalyzes !1the terminal reaction in the de novo pathway for pyrimidine !1nucleotide synthesis; ammonia can replace glutamine. GENETICS !$#gene GDB:CTPS !'##cross-references GDB:126729; OMIM:123860 !$#map_position 1p34.3-1p34.1 CLASSIFICATION #superfamily CTP synthase KEYWORDS ligase; pyrimidine nucleotide biosynthesis SUMMARY #length 591 #molecular-weight 66705 #checksum 3171 SEQUENCE /// ENTRY SYECTP #type complete TITLE CTP synthase (EC 6.3.4.2) [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES CTP-synthetase; UTP-ammonia ligase ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 21-Nov-1997 #text_change 01-Mar-2002 ACCESSIONS H65059; A25608 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65059 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-545 ##label BLAT !'##cross-references GB:AE000361; GB:U00096; NID:g2367160; !1PIDN:AAC75822.1; PID:g1789142; UWGP:b2780 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A92584 !$#authors Weng, M.; Makaroff, C.A.; Zalkin, H. !$#journal J. Biol. Chem. (1986) 261:5568-5574 !$#title Nucleotide sequence of Escherichia coli pyrG encoding CTP !1synthetase. !$#cross-references MUID:86168304; PMID:3514618 !$#accession A25608 !'##molecule_type DNA !'##residues 1-337,'L',339-475,'S',477-488,'RA',491-545 ##label WEN !'##cross-references GB:M12843 GENETICS !$#gene pyrG !$#map_position 60 min COMPLEX homodimer; aggregates to a tetramer FUNCTION !$#description this glutamine amidotransferase catalyzes the terminal !1reaction in the de novo pathway for pyrimidine nucleotide !1synthesis; ammonia can replace glutamine [validated, !1MUID:86168304] CLASSIFICATION #superfamily CTP synthase KEYWORDS homodimer; ligase; pyrimidine nucleotide biosynthesis FEATURE !$2-545 #product CTP synthase #status experimental #label MAT SUMMARY #length 545 #molecular-weight 60374 #checksum 8117 SEQUENCE /// ENTRY SYBSTP #type complete TITLE CTP synthase (EC 6.3.4.2) - Bacillus subtilis ALTERNATE_NAMES CTP-synthetase; UTP-ammonia ligase ORGANISM #formal_name Bacillus subtilis DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jun-2000 ACCESSIONS A32354; S55423; C69610 REFERENCE A91883 !$#authors Trach, K.; Chapman, J.W.; Piggot, P.; LeCoq, D.; Hoch, J.A. !$#journal J. Bacteriol. (1988) 170:4194-4208 !$#title Complete sequence and transcriptional analysis of the spo0F !1region of the Bacillus subtilis chromosome. !$#cross-references MUID:88314920; PMID:2457578 !$#accession A32354 !'##molecule_type DNA !'##residues 1-535 ##label TRA !'##cross-references GB:M22039; NID:g460910; PIDN:AAA16801.1; !1PID:g143597 REFERENCE S55414 !$#authors Glaser, P.; Danchin, A. !$#submission submitted to the EMBL Data Library, May 1995 !$#description Cloning and sequencing of the Bacillus subtilis chromosomal !1region from 320 degrees to 321 degrees. !$#accession S55423 !'##molecule_type DNA !'##residues 1-535 ##label GLA !'##cross-references EMBL:Z49782; NID:g853752; PIDN:CAA89870.1; !1PID:g853762 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69610 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-535 ##label KUN !'##cross-references GB:Z99123; GB:AL009126; NID:g2636240; !1PIDN:CAB15743.1; PID:g2636252 !'##experimental_source strain 168 COMMENT This enzyme is a glutamine amidotransferase that catalyzes !1the terminal reaction in the de novo pathway for pyrimidine !1nucleotide synthesis; ammonia can replace glutamine. GENETICS !$#gene ctrA; pyrG !$#map_position 37 min CLASSIFICATION #superfamily CTP synthase KEYWORDS ligase; pyrimidine nucleotide biosynthesis SUMMARY #length 535 #molecular-weight 59718 #checksum 3338 SEQUENCE /// ENTRY A31903 #type complete TITLE methylenetetrahydrofolate dehydrogenase (NADP) (EC 1.5.1.5) - human CONTAINS formate-tetrahydrofolate ligase (EC 6.3.4.3); methylenetetrahydrofolate dehydrogenase (NADP) (EC 1.5.1.5) / methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9) ORGANISM #formal_name Homo sapiens #common_name man DATE 21-May-1990 #sequence_revision 05-Apr-1995 #text_change 19-Jul-2002 ACCESSIONS A31903 REFERENCE A31903 !$#authors Hum, D.W.; Bell, A.W.; Rozen, R.; MacKenzie, R.E. !$#journal J. Biol. Chem. (1988) 263:15946-15950 !$#title Primary structure of a human trifunctional enzyme. Isolation !1of a cDNA encoding methylenetetrahydrofolate !1dehydrogenase-methenyltetrahydrofolate !1cyclohydrolase-formyltetrahydrofolate synthetase. !$#cross-references MUID:89034046; PMID:3053686 !$#accession A31903 !'##molecule_type mRNA !'##residues 1-935 ##label HUM !'##cross-references GB:J04031; NID:g187464; PIDN:AAA59574.1; !1PID:g307178 GENETICS !$#gene GDB:MTHFD1; MTHFD; MTHFC !'##cross-references GDB:120704; OMIM:172460 !$#map_position 14q24-14q24 CLASSIFICATION #superfamily C1-tetrahydrofolate synthase; !1formate-tetrahydrofolate ligase homology; !1methylenetetrahydrofolate dehydrogenase (NAD+) homology KEYWORDS hydrolase; ligase; multifunctional enzyme; NADP; one-carbon !1metabolism; oxidoreductase FEATURE !$6-292 #domain methylenetetrahydrofolate dehydrogenase !8(NAD+) homology #label MTFD\ !$318-935 #domain formate-tetrahydrofolate ligase homology !8#label FTL SUMMARY #length 935 #molecular-weight 101558 #checksum 9026 SEQUENCE /// ENTRY A35367 #type complete TITLE methylenetetrahydrofolate dehydrogenase (NADP) (EC 1.5.1.5) - rat CONTAINS formate-tetrahydrofolate ligase (EC 6.3.4.3); methylenetetrahydrofolate dehydrogenase (NADP) (EC 1.5.1.5) / methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9) ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 17-Aug-1990 #sequence_revision 05-Apr-1995 #text_change 19-Jul-2002 ACCESSIONS A35367 REFERENCE A35367 !$#authors Thigpen, A.E.; West, M.G.; Appling, D.R. !$#journal J. Biol. Chem. (1990) 265:7907-7913 !$#title Rat C-1-tetrahydrofolate synthase. cDNA isolation, !1tissue-specific levels of the mRNA, and expression of the !1protein in yeast. !$#cross-references MUID:90243660; PMID:2186031 !$#accession A35367 !'##molecule_type mRNA !'##residues 1-935 ##label THI !'##cross-references GB:J05519 CLASSIFICATION #superfamily C1-tetrahydrofolate synthase; !1formate-tetrahydrofolate ligase homology; !1methylenetetrahydrofolate dehydrogenase (NAD+) homology KEYWORDS hydrolase; ligase; multifunctional enzyme; NADP; one-carbon !1metabolism; oxidoreductase FEATURE !$6-292 #domain methylenetetrahydrofolate dehydrogenase !8(NAD+) homology #label MTFD\ !$318-935 #domain formate-tetrahydrofolate ligase homology !8#label FTL SUMMARY #length 935 #molecular-weight 101098 #checksum 5611 SEQUENCE /// ENTRY A29550 #type complete TITLE methylenetetrahydrofolate dehydrogenase (NADP) (EC 1.5.1.5) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES C1-tetrahydrofolate synthase; protein G7733; protein YGR204w CONTAINS formate-tetrahydrofolate ligase (EC 6.3.4.3); methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9); methylenetetrahydrofolate dehydrogenase (NADP) (EC 1.5.1.5) ORGANISM #formal_name Saccharomyces cerevisiae DATE 21-May-1988 #sequence_revision 05-Apr-1995 #text_change 19-Jul-2002 ACCESSIONS A29550; S53927; S64526; S63853 REFERENCE A92580 !$#authors Staben, C.; Rabinowitz, J.C. !$#journal J. Biol. Chem. (1986) 261:4629-4637 !$#title Nucleotide sequence of the Saccharomyces cerevisiae ADE3 !1gene encoding C1-tetrahydrofolate synthase. !$#cross-references MUID:86168166; PMID:3514599 !$#accession A29550 !'##molecule_type DNA !'##residues 1-946 ##label STA !'##cross-references EMBL:M12878; NID:g171004; PIDN:AAA66316.1; !1PID:g171005 REFERENCE S53922 !$#authors Guerreiro, P.; Barreiros, T.; Soares, H.; Cyrne, L.; Maia e !1Silva, A.; Rodrigues-Pousada, C. !$#submission submitted to the EMBL Data Library, April 1995 !$#description Sequencing of a 17.6 kb segment on the right arm of yeast !1chromosome VII reveals 12 open reading frames, including !1CCT, ADE3 and TR-I genes, homologous to the yeast YAL023 and !1EF1G genes, of the human. !$#accession S53927 !'##molecule_type DNA !'##residues 1-946 ##label GUE !'##cross-references EMBL:Z49133; NID:g790489; PIDN:CAA88997.1; !1PID:g790495 !'##experimental_source strain S228C REFERENCE S64517 !$#authors Guerreiro, P.; Barreiros, T.; Cyrne, L.; Soares, H.; Maia e !1Silva, A.; Rodrigues-Pousada, C. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64526 !'##molecule_type DNA !'##residues 1-946 ##label GUW !'##cross-references EMBL:Z72989; NID:g1323364; PIDN:CAA97231.1; !1PID:g1323365; GSPDB:GN00007; MIPS:YGR204w !'##experimental_source strain S288C REFERENCE S63848 !$#authors Guerreiro, P.; Barreiros, T.; Soares, H.; Cyrne, L.; Maia e !1Silva, A.; Rodrigues-Pousada, C. !$#journal Yeast (1996) 12:273-280 !$#title Sequencing of a 17.6 kb segment on the right arm of yeast !1chromosome VII reveals 12 ORFs, including CCT, ADE3 and TR-I !1genes, homologues of the yeast PMT and EF1G genes, of the !1human and bacterial electron-transferring flavoproteins !1(beta-chain) and of the Escherichia coli phosphoserine !1phosphohydrolase, and five new ORFs. !$#cross-references MUID:97060019; PMID:8904340 !$#accession S63853 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-946 ##label GUF !'##cross-references EMBL:Z49133; NID:g790489; PIDN:CAA88997.1; !1PID:g790495 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1995 GENETICS !$#gene SGD:ADE3; MIPS:YGR204w !'##cross-references SGD:S0003436; MIPS:YGR204w !$#map_position 7R CLASSIFICATION #superfamily C1-tetrahydrofolate synthase; !1formate-tetrahydrofolate ligase homology; !1methylenetetrahydrofolate dehydrogenase (NAD+) homology KEYWORDS hydrolase; ligase; multifunctional enzyme; NADP; one-carbon !1metabolism; oxidoreductase FEATURE !$5-297 #domain methylenetetrahydrofolate dehydrogenase !8(NAD+) homology #label MTFD\ !$322-946 #domain formate-tetrahydrofolate ligase homology !8#label FTL SUMMARY #length 946 #molecular-weight 102204 #checksum 8079 SEQUENCE /// ENTRY A28174 #type complete TITLE methylenetetrahydrofolate dehydrogenase (NADP) (EC 1.5.1.5) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YBR0751; protein YBR084w CONTAINS formate-tetrahydrofolate ligase (EC 6.3.4.3); methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9); methylenetetrahydrofolate dehydrogenase (NADP) (EC 1.5.1.5) ORGANISM #formal_name Saccharomyces cerevisiae DATE 20-Jun-1989 #sequence_revision 05-Apr-1995 #text_change 19-Jul-2002 ACCESSIONS A28174; S45951 REFERENCE A28174 !$#authors Shannon, K.W.; Rabinowitz, J.C. !$#journal J. Biol. Chem. (1988) 263:7717-7725 !$#title Isolation and characterization of the Saccharomyces !1cerevisiae MIS1 gene encoding mitochondrial !1C-1-tetrahydrofolate synthase. !$#cross-references MUID:88227973; PMID:2836393 !$#accession A28174 !'##molecule_type DNA !'##residues 1-975 ##label SHA !'##cross-references EMBL:J03724; NID:g171952; PIDN:AAA34781.1; !1PID:g171953 REFERENCE S45893 !$#authors Andre, B.; Cziepluch, C.; Hein, C.; Jauniaux, J.C.; !1Urrestarazu, A.; Vissers, S. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S45951 !'##molecule_type DNA !'##residues 1-975 ##label AND !'##cross-references EMBL:Z35953; NID:g536347; PIDN:CAA85029.1; !1PID:g536348; GSPDB:GN00002; MIPS:YBR084w GENETICS !$#gene SGD:MIS1; MIPS:YBR084w !'##cross-references SGD:S0000288; MIPS:YBR084w !$#map_position 2R CLASSIFICATION #superfamily C1-tetrahydrofolate synthase; !1formate-tetrahydrofolate ligase homology; !1methylenetetrahydrofolate dehydrogenase (NAD+) homology KEYWORDS hydrolase; ligase; mitochondrion; multifunctional enzyme; !1NADP; one-carbon metabolism; oxidoreductase; transmembrane !1protein FEATURE !$1-34 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$35-975 #product C1-tetrahydrofolate synthase #status !8predicted #label MAT\ !$37-321 #domain methylenetetrahydrofolate dehydrogenase !8(NAD+) homology #label MTFD\ !$198-214 #domain transmembrane #status predicted #label TM1\ !$231-247 #domain transmembrane #status predicted #label TM2\ !$303-320 #domain transmembrane #status predicted #label TM3\ !$346-975 #domain formate-tetrahydrofolate ligase homology !8#label FTL\ !$592-608 #domain transmembrane #status predicted #label TM4\ !$673-689 #domain transmembrane #status predicted #label TM5\ !$729-745 #domain transmembrane #status predicted #label TM6 SUMMARY #length 975 #molecular-weight 106216 #checksum 2080 SEQUENCE /// ENTRY S53523 #type complete TITLE methylenetetrahydrofolate dehydrogenase (NADP) (EC 1.5.1.5) - fall armyworm ALTERNATE_NAMES C1-tetrahydrofolate synthase; folate-dependent trifunctional enzyme CONTAINS formate-tetrahydrofolate ligase (EC 6.3.4.3); methylenetetrahydrofolate dehydrogenase (NADP) (EC 1.5.1.5) / methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9) ORGANISM #formal_name Spodoptera frugiperda #common_name fall armyworm DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jul-2002 ACCESSIONS S53523; S71063 REFERENCE S53523 !$#authors Tremblay, G.B.; MacKenzie, R.E. !$#journal Biochim. Biophys. Acta (1995) 1261:129-133 !$#title Primary structure of a folate-dependent trifunctional enzyme !1from Spodoptera frugiperda. !$#cross-references MUID:95200961; PMID:7893749 !$#accession S53523 !'##status preliminary !'##molecule_type mRNA !'##residues 1-933 ##label TRE !'##cross-references EMBL:L36189 REFERENCE S71063 !$#authors Tremblay, G.B.; MacKenzie, R.E. !$#submission submitted to the EMBL Data Library, September 1994 !$#accession S71063 !'##status preliminary !'##molecule_type mRNA !'##residues 1-33,'DA',36-933 ##label TR2 !'##cross-references EMBL:L36189; NID:g537594; PIDN:AAA74302.1; !1PID:g537595 CLASSIFICATION #superfamily C1-tetrahydrofolate synthase; !1formate-tetrahydrofolate ligase homology; !1methylenetetrahydrofolate dehydrogenase (NAD+) homology KEYWORDS hydrolase; ligase; oxidoreductase FEATURE !$5-290 #domain methylenetetrahydrofolate dehydrogenase !8(NAD+) homology #label MTFD\ !$316-933 #domain formate-tetrahydrofolate ligase homology !8#label FTL SUMMARY #length 933 #molecular-weight 100657 #checksum 3486 SEQUENCE /// ENTRY A43350 #type complete TITLE formate-tetrahydrofolate ligase (EC 6.3.4.3) - spinach ALTERNATE_NAMES formyltetrahydrofolate synthetase ORGANISM #formal_name Spinacia oleracea #common_name spinach DATE 31-Dec-1993 #sequence_revision 05-Apr-1995 #text_change 03-Jun-2002 ACCESSIONS A43350 REFERENCE A43350 !$#authors Nour, J.M.; Rabinowitz, J.C. !$#journal J. Biol. Chem. (1992) 267:16292-16296 !$#title Isolation and sequencing of the cDNA coding for spinach !110-formyltetrahydrofolate synthetase. Comparisons with the !1yeast, mammalian, and bacterial proteins. !$#cross-references MUID:92355589; PMID:1644815 !$#accession A43350 !'##molecule_type mRNA !'##residues 1-637 ##label NOU !'##cross-references GB:M83940; NID:g170144; PIDN:AAA34046.1; !1PID:g170145 !'##note sequence extracted from NCBI backbone (NCBIN:110596, !1NCBIP:110597) CLASSIFICATION #superfamily formate-tetrahydrofolate ligase; !1formate-tetrahydrofolate ligase homology KEYWORDS ligase; one-carbon metabolism FEATURE !$19-637 #domain formate-tetrahydrofolate ligase homology !8#label FTL SUMMARY #length 637 #molecular-weight 67855 #checksum 7293 SEQUENCE /// ENTRY A28185 #type complete TITLE formate-tetrahydrofolate ligase (EC 6.3.4.3) - Clostridium acidiurici ALTERNATE_NAMES formyltetrahydrofolate synthetase ORGANISM #formal_name Clostridium acidiurici DATE 08-Mar-1991 #sequence_revision 05-Apr-1995 #text_change 03-Jun-2002 ACCESSIONS A28185 REFERENCE A28185 !$#authors Whitehead, T.R.; Rabinowitz, J.C. !$#journal J. Bacteriol. (1988) 170:3255-3261 !$#title Nucleotide sequence of the Clostridium acidiurici !1("Clostridium acidi-urici") gene for !110-formyltetrahydrofolate synthetase shows extensive amino !1acid homology with the trifunctional enzyme !1C-1-tetrahydrofolate synthase from Saccharomyces cerevisiae. !$#cross-references MUID:88257049; PMID:2838464 !$#accession A28185 !'##molecule_type DNA !'##residues 1-556 ##label WHI !'##cross-references GB:M21507; NID:g144809; PIDN:AAA53187.1; !1PID:g144810 CLASSIFICATION #superfamily formate-tetrahydrofolate ligase; !1formate-tetrahydrofolate ligase homology KEYWORDS ligase; one-carbon metabolism FEATURE !$3-556 #domain formate-tetrahydrofolate ligase homology !8#label FTL SUMMARY #length 556 #molecular-weight 59588 #checksum 6376 SEQUENCE /// ENTRY A35942 #type complete TITLE formate-tetrahydrofolate ligase (EC 6.3.4.3) - Clostridium thermaceticum ALTERNATE_NAMES formyltetrahydrofolate synthetase ORGANISM #formal_name Clostridium thermaceticum DATE 08-Mar-1991 #sequence_revision 05-Apr-1995 #text_change 03-Jun-2002 ACCESSIONS A35942 REFERENCE A35942 !$#authors Lovell, C.R.; Przybyla, A.; Ljungdahl, L.G. !$#journal Biochemistry (1990) 29:5687-5694 !$#title Primary structure of the thermostable formyltetrahydrofolate !1synthetase from Clostridium thermoaceticum. !$#cross-references MUID:90344789; PMID:2200509 !$#accession A35942 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-559 ##label LOV CLASSIFICATION #superfamily formate-tetrahydrofolate ligase; !1formate-tetrahydrofolate ligase homology KEYWORDS ligase; one-carbon metabolism FEATURE !$6-559 #domain formate-tetrahydrofolate ligase homology !8#label FTL SUMMARY #length 559 #molecular-weight 59993 #checksum 3748 SEQUENCE /// ENTRY AJMSDS #type complete TITLE adenylosuccinate synthase (EC 6.3.4.4), muscle - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 30-Jun-1993 ACCESSIONS A39317 REFERENCE A39317 !$#authors Guicherit, O.M.; Rudolph, F.B.; Kellems, R.E.; Cooper, B.F. !$#journal J. Biol. Chem. (1991) 266:22582-22587 !$#title Molecular cloning and expression of a mouse muscle cDNA !1encoding adenylosuccinate synthetase. !$#cross-references MUID:92042206; PMID:1939273 !$#accession A39317 !'##molecule_type mRNA !'##residues 1-452 ##label GUI !'##cross-references GB:M74495 COMMENT This cytosolic enzyme has a central regulatory role in the !1de novo pathway of purine biosynthesis and is the first !1enzyme in the AMP-specific branch. It has intrinsic GTPase !1activity. CLASSIFICATION #superfamily adenylosuccinate synthase KEYWORDS AMP biosynthesis; GTP binding; ligase; purine nucleotide !1biosynthesis FEATURE !$174 #binding_site GTP (Lys) #status predicted SUMMARY #length 452 #molecular-weight 49472 #checksum 8252 SEQUENCE /// ENTRY S21166 #type complete TITLE adenylosuccinate synthase (EC 6.3.4.4) - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 24-Sep-1999 ACCESSIONS S21166 REFERENCE S21166 !$#authors Powell, S.M.; Zalkin, H.; Dixon, J.E. !$#journal FEBS Lett. (1992) 303:4-10 !$#title Cloning and characterization of the cDNA encoding human !1adenylosuccinate synthetase. !$#cross-references MUID:92275078; PMID:1592113 !$#accession S21166 !'##status preliminary !'##molecule_type mRNA !'##residues 1-455 ##label POW !'##cross-references EMBL:X66503 GENETICS !$#gene GDB:ADSS !'##cross-references GDB:119656; OMIM:103060 !$#map_position 1pter-1qter CLASSIFICATION #superfamily adenylosuccinate synthase KEYWORDS ligase SUMMARY #length 455 #molecular-weight 49919 #checksum 9388 SEQUENCE /// ENTRY S48515 #type complete TITLE adenylosuccinate synthase (EC 6.3.4.4) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein N1290; protein YNL220w ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S48515; S53085; S63178 REFERENCE S48515 !$#authors Shabes, A.V.; Andreichuk, Y.V.; Holmes, W.M.; Domkin, V.D. !$#submission submitted to the EMBL Data Library, July 1993 !$#accession S48515 !'##molecule_type DNA !'##residues 1-433 ##label SHA !'##cross-references EMBL:L22185; NID:g347862; PIDN:AAA91338.1; !1PID:g347863 REFERENCE S53085 !$#authors Ohanjan, T.; Daignan-Fornier, B.; Krauss, G. !$#submission submitted to the EMBL Data Library, March 1995 !$#description Adenylosuccinate synthetase from Saccharomyces cereviseae. !$#accession S53085 !'##molecule_type DNA !'##residues 1-433 ##label OHA !'##cross-references EMBL:Z48671; NID:g732938; PIDN:CAA88590.1; !1PID:g732939 REFERENCE S62944 !$#authors Duesterhoeft, A.; Floeth, M.; Fritz, C.; Heuss-Neitzel, D.; !1Hilbert, H.; Moestl, D. !$#submission submitted to the Protein Sequence Database, April 1996 !$#accession S63178 !'##molecule_type DNA !'##residues 1-433 ##label DUE !'##cross-references EMBL:Z71496; NID:g1302236; PIDN:CAA96123.1; !1PID:g1302237; GSPDB:GN00014; MIPS:YNL220w !'##experimental_source strain S288C GENETICS !$#gene SGD:ADE12; MIPS:YNL220w !'##cross-references SGD:S0005164; MIPS:YNL220w !$#map_position 14L CLASSIFICATION #superfamily adenylosuccinate synthase KEYWORDS ligase; purine nucleotide biosynthesis SUMMARY #length 433 #molecular-weight 48279 #checksum 508 SEQUENCE /// ENTRY A45027 #type complete TITLE adenylosuccinate synthase (EC 6.3.4.4) - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES IMP-aspartate ligase ORGANISM #formal_name Schizosaccharomyces pombe DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A45027 REFERENCE A45027 !$#authors Speiser, D.M.; Ortiz, D.F.; Kreppel, L.; Scheel, G.; !1McDonald, G.; Ow, D.W. !$#journal Mol. Cell. Biol. (1992) 12:5301-5310 !$#title Purine biosynthetic genes are required for cadmium tolerance !1in Schizosaccharomyces pombe. !$#cross-references MUID:93078729; PMID:1448066 !$#accession A45027 !'##status preliminary !'##molecule_type DNA !'##residues 1-434 ##label SPE !'##note this sequence is inconsistent with the nucleotide translation !'##note sequence extracted from NCBI backbone (NCBIP:119048) CLASSIFICATION #superfamily adenylosuccinate synthase KEYWORDS AMP biosynthesis; GTP binding; ligase; purine nucleotide !1biosynthesis SUMMARY #length 434 #molecular-weight 47901 #checksum 2247 SEQUENCE /// ENTRY AJDODS #type complete TITLE adenylosuccinate synthase (EC 6.3.4.4) - slime mold (Dictyostelium discoideum) ALTERNATE_NAMES IMP-aspartate ligase ORGANISM #formal_name Dictyostelium discoideum DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 18-Jun-1999 ACCESSIONS A38617 REFERENCE A38617 !$#authors Wiesmueller, L.; Wittbrodt, J.; Noegel, A.A.; Schleicher, M. !$#journal J. Biol. Chem. (1991) 266:2480-2485 !$#title Purification and cDNA-derived sequence of adenylosuccinate !1synthetase from Dictyostelium discoideum. !$#cross-references MUID:91115872; PMID:1989999 !$#accession A38617 !'##molecule_type mRNA !'##residues 1-427 ##label WIE !'##cross-references GB:M58471; NID:g167667; PIDN:AAA33167.1; !1PID:g167668 COMMENT This cytosolic enzyme has a central regulatory role in the !1de novo pathway of purine biosynthesis and is the first !1enzyme in the AMP-specific branch. It has intrinsic GTPase !1activity. CLASSIFICATION #superfamily adenylosuccinate synthase KEYWORDS AMP biosynthesis; GTP binding; ligase; purine nucleotide !1biosynthesis FEATURE !$143 #binding_site GTP (Lys) #status predicted SUMMARY #length 427 #molecular-weight 47285 #checksum 3617 SEQUENCE /// ENTRY AJECDS #type complete TITLE adenylosuccinate synthase (EC 6.3.4.4) purA [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES IMP-aspartate ligase ORGANISM #formal_name Escherichia coli DATE 31-Dec-1991 #sequence_revision 14-Feb-1997 #text_change 01-Mar-2002 ACCESSIONS S56402; A31965; A61592; D65228 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56402 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-432 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97073.1; !1PID:g537018 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A31965 !$#authors Wolfe, S.A.; Smith, J.M. !$#journal J. Biol. Chem. (1988) 263:19147-19153 !$#title Nucleotide sequence and analysis of the purA gene encoding !1adenylosuccinate synthetase of Escherichia coli K12. !$#cross-references MUID:89066719; PMID:3058695 !$#accession A31965 !'##molecule_type DNA !'##residues 1-416,'D',418-432 ##label WOL !'##cross-references GB:J04199; NID:g147405; PIDN:AAA24446.1; !1PID:g147406 !'##experimental_source strain K12 REFERENCE A61592 !$#authors Bass, M.B.; Fromm, H.J.; Stayton, M.M. !$#journal Arch. Biochem. Biophys. (1987) 256:335-342 !$#title Overproduction, purification, and characterization of !1adenylosuccinate synthetase from Escherichia coli. !$#cross-references MUID:87269643; PMID:3038024 !$#accession A61592 !'##molecule_type protein !'##residues 2-11 ##label BAS REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65228 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-432 ##label BLAT !'##cross-references GB:AE000490; GB:U00096; NID:g2367356; !1PIDN:AAC77134.1; PID:g1790620; UWGP:b4177 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene purA !$#map_position 95 min COMPLEX homodimer [validated, MUID:96095802] FUNCTION !$#description EC 6.3.4.4 [validated, MUID:90202896]; adenylosuccinate !1synthase; catalyzes the formation of AMP (with GDP and !1phosphate) from GTP, IMP, and aspartate !$#pathway AMP biosynthesis; purine nucleotide biosynthesis !$#note has intrinsic GTPase activity !$#note inactivation of the enzyme by pyridoxal 5'-phosphate !$#note first enzyme in the AMP-specific branch of purine nucleotide !1biosynthesis CLASSIFICATION #superfamily adenylosuccinate synthase KEYWORDS AMP biosynthesis; GTP binding; homodimer; ligase; purine !1nucleotide biosynthesis FEATURE !$2-432 #product adenylosuccinate synthase #status !8experimental #label MAT\ !$141 #binding_site GTP (Lys) #status experimental\ !$148 #active_site Arg #status predicted SUMMARY #length 432 #molecular-weight 47345 #checksum 3003 SEQUENCE /// ENTRY AJHURS #type complete TITLE argininosuccinate synthase (EC 6.3.4.5) - human ALTERNATE_NAMES citrulline-aspartate ligase ORGANISM #formal_name Homo sapiens #common_name man DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 18-Jun-1999 ACCESSIONS A01195; S06104; I56310 REFERENCE A01195 !$#authors Bock, H.G.O.; Su, T.S.; O'Brien, W.E.; Beaudet, A.L. !$#journal Nucleic Acids Res. (1983) 11:6505-6512 !$#title Sequence for human argininosuccinate synthetase cDNA. !$#cross-references MUID:84015388; PMID:6194510 !$#accession A01195 !'##molecule_type mRNA !'##residues 1-412 ##label BOC !'##cross-references GB:X01630; NID:g28871; PIDN:CAA25771.1; PID:g28872 REFERENCE S06104 !$#authors Isashiki, Y.; Noda, T.; Kobayashi, K.; Sase, M.; Saheki, T.; !1Titani, K. !$#journal Protein Seq. Data Anal. (1989) 2:283-287 !$#title Identification of essential arginine residue(s) for Mg-ATP !1binding of human argininosuccinate synthetase. !$#cross-references MUID:89367258; PMID:2788888 !$#accession S06104 !'##molecule_type protein !'##residues 148-161 ##label ISA REFERENCE I56310 !$#authors Jinno, Y.; Nomiyama, H.; Matuo, S.; Shimada, K.; Matsuda, !1I.; Saheki, T. !$#journal J. Inherit. Metab. Dis. (1985) 8:157-159 !$#title Structure of the 5' end region of the human !1argininosuccinate synthetase gene. !$#cross-references MUID:87113889; PMID:3027451 !$#accession I56310 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-24 ##label RES !'##cross-references GB:M34903; NID:g179045; PIDN:AAA51782.1; !1PID:g179047 GENETICS !$#gene GDB:ASS !'##cross-references GDB:119010; OMIM:215700 !$#map_position 9q34.1-9q34.1 !$#note defects in this gene may cause citrullinemia FUNCTION !$#description catalyzes the formation of argininosuccinate from citrulline !1and aspartate coupled with the irreversible hydrolysis of !1ATP to AMP and diphosphate !$#pathway urea cycle CLASSIFICATION #superfamily argininosuccinate synthase KEYWORDS arginine biosynthesis; ATP; homotetramer; ligase; urea cycle FEATURE !$148-161 #region ATP binding #status experimental\ !$149,153 #binding_site Mg-ATP (Glu, Arg) #status predicted SUMMARY #length 412 #molecular-weight 46426 #checksum 4629 SEQUENCE /// ENTRY AJRTRS #type complete TITLE argininosuccinate synthase (EC 6.3.4.5) - rat ALTERNATE_NAMES citrulline-aspartate ligase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 18-Jun-1999 ACCESSIONS S01440 REFERENCE S01440 !$#authors Surh, L.C.; Morris, S.M.; O'Brien, W.E.; Beaudet, A.L. !$#journal Nucleic Acids Res. (1988) 16:9352 !$#title Nucleotide sequence of the cDNA encoding the rat !1argininosuccinate synthetase. !$#cross-references MUID:89016648; PMID:3174461 !$#accession S01440 !'##molecule_type mRNA !'##residues 1-412 ##label SUR !'##cross-references EMBL:X12459; NID:g55766; PIDN:CAA30999.1; !1PID:g55767 COMMENT This enzyme catalyzes the formation of argininosuccinate !1from citrulline and aspartate in the urea cycle. CLASSIFICATION #superfamily argininosuccinate synthase KEYWORDS arginine biosynthesis; homotetramer; ligase; urea cycle FEATURE !$149,153 #binding_site Mg-ATP (Glu, Arg) #status predicted SUMMARY #length 412 #molecular-weight 46496 #checksum 4784 SEQUENCE /// ENTRY AJMSRS #type complete TITLE argininosuccinate synthase (EC 6.3.4.5) - mouse ALTERNATE_NAMES citrulline-aspartate ligase ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 18-Jun-1999 ACCESSIONS JU0463 REFERENCE JU0463 !$#authors Surh, L.C.; Beaudet, A.L.; O'Brien, W.E. !$#journal Gene (1991) 99:181-189 !$#title Molecular characterization of the murine argininosuccinate !1synthetase locus. !$#cross-references MUID:91216457; PMID:1708740 !$#accession JU0463 !'##molecule_type mRNA !'##residues 1-412 ##label SUR !'##cross-references GB:M31690; NID:g192068; PIDN:AAA37266.1; !1PID:g309111 COMMENT This enzyme catalyzes the formation of argininosuccinate !1from citrulline and aspartate in the urea cycle. GENETICS !$#gene ASS !$#introns 35/3; 58/3; 121/3; 142/3; 495/3; 189/2; 199/3; 230/1; 258/2; !1280/1; 324/1; 376/2; 391/2 CLASSIFICATION #superfamily argininosuccinate synthase KEYWORDS arginine biosynthesis; homotetramer; ligase; urea cycle FEATURE !$149,153 #binding_site Mg-ATP (Glu, Arg) #status predicted SUMMARY #length 412 #molecular-weight 46584 #checksum 5814 SEQUENCE /// ENTRY AJBORS #type complete TITLE argininosuccinate synthase (EC 6.3.4.5) - bovine ALTERNATE_NAMES citrulline-aspartate ligase ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 23-Feb-1997 ACCESSIONS A33986 REFERENCE A33986 !$#authors Dennis, J.A.; Healy, P.J.; Beaudet, A.L.; O'Brien, W.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:7947-7951 !$#title Molecular definition of bovine argininosuccinate synthase !1deficiency. !$#cross-references MUID:90046714; PMID:2813370 !$#accession A33986 !'##molecule_type mRNA !'##residues 1-412 ##label DEN !'##cross-references GB:M26198 COMMENT This enzyme catalyzes the formation of argininosuccinate !1from citrulline and aspartate in the urea cycle. CLASSIFICATION #superfamily argininosuccinate synthase KEYWORDS arginine biosynthesis; homotetramer; ligase; urea cycle FEATURE !$149,153 #binding_site Mg-ATP (Glu, Arg) #status predicted SUMMARY #length 412 #molecular-weight 46404 #checksum 4201 SEQUENCE /// ENTRY AJBYRS #type complete TITLE argininosuccinate synthase (EC 6.3.4.5) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES citrulline-aspartate ligase; protein O1228; protein YOL058w ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1992 #sequence_revision 08-Mar-1996 #text_change 23-Mar-2001 ACCESSIONS S59291; JQ0779; S61721; S66750; S41983 REFERENCE S59285 !$#authors Mannhaupt, G.; Vetter, I.; Schwarzlose, C.; Mitzel, S.; !1Feldmann, H. !$#submission submitted to the EMBL Data Library, August 1995 !$#description Analysis of a 26kb region on the left arm of yeast !1chromosome XV. !$#accession S59291 !'##molecule_type DNA !'##residues 1-420 ##label FEL !'##cross-references EMBL:X91067; NID:g984177; PIDN:CAA62528.1; !1PID:g984184 REFERENCE JQ0778 !$#authors Van Vliet, F.; Crabeel, M.; Boyen, A.; Tricot, C.; Stalon, !1V.; Falmagne, P.; Nakamura, Y.; Baumberg, S.; Glansdorff, N. !$#journal Gene (1990) 95:99-104 !$#title Sequences of the genes encoding argininosuccinate synthetase !1in Escherichia coli and Saccharomyces cerevisiae: comparison !1with methanogenic archaebacteria and mammals. !$#cross-references MUID:91071613; PMID:2123815 !$#accession JQ0779 !'##molecule_type DNA !'##residues 1-26,'AT',29-47,'VL',50-60,'GGLS',65-168,'F',170-315,'L', !1317-420 ##label VAN !'##cross-references GB:M35237; NID:g171084; PIDN:AAA34437.1; !1PID:g171085 REFERENCE S61715 !$#authors Mannhaupt, G.; Vetter, I.; Schwarzlose, C.; Mitzel, S.; !1Feldmann, H. !$#journal Yeast (1996) 12:67-76 !$#title Analysis of a 26 kb region on the left arm of yeast !1chromosome XV. !$#cross-references MUID:96381248; PMID:8789261 !$#accession S61721 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-420 ##label MAN !'##cross-references EMBL:X91067; NID:g984177; PIDN:CAA62528.1; !1PID:g984184 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1995 REFERENCE S66743 !$#authors Feldmann, H.; Mannhaupt, G.; Vetter, I. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S66750 !'##molecule_type DNA !'##residues 1-420 ##label FEW !'##cross-references EMBL:Z74800; NID:g1419870; PIDN:CAA99067.1; !1PID:g1419871; GSPDB:GN00015; MIPS:YOL058w !'##experimental_source strain S288C REFERENCE S41983 !$#authors Crabeel, M.; Seneca, S.; Devos, K.; Glansdorff, N. !$#journal Curr. Genet. (1988) 13:113-124 !$#title Arginine repression of the Saccharomyces cerevisiae ARG1 !1gene. !$#cross-references MUID:88223481; PMID:2897249 !$#accession S41983 !'##molecule_type DNA !'##residues 1-26,'AT',29-47,'VL',50-57 ##label CRA !'##cross-references EMBL:X07070; NID:g3371; PIDN:CAA30106.1; PID:g3372 GENETICS !$#gene SGD:ARG1; MIPS:YOL058w !'##cross-references SGD:S0005419; MIPS:YOL058w !$#map_position 15L CLASSIFICATION #superfamily argininosuccinate synthase KEYWORDS arginine biosynthesis; homotetramer; ligase FEATURE !$148,152 #binding_site Mg-ATP (Glu, Arg) #status predicted SUMMARY #length 420 #molecular-weight 46939 #checksum 1572 SEQUENCE /// ENTRY AJSMRC #type complete TITLE argininosuccinate synthase (EC 6.3.4.5) - Streptomyces coelicolor ALTERNATE_NAMES citrulline-aspartate ligase ORGANISM #formal_name Streptomyces coelicolor DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jun-2000 ACCESSIONS JQ1057 REFERENCE JQ1057 !$#authors Ishihara, H.; Urabe, H.; Kasama, H.; Ogawara, H. !$#journal Actinomycetol. (1991) 5:14-17 !$#title Sequence of the gene encoding argininosuccinate synthetase !1in Streptomyces coelicolor A3(2). !$#accession JQ1057 !'##molecule_type DNA !'##residues 1-487 ##label ISH !'##cross-references GB:D00799; NID:g216987; PIDN:BAA00691.1; !1PID:g216988 !'##experimental_source strain A3[2]M130 COMMENT This enzyme catalyzes the formation of argininosuccinate !1from citrulline and aspartate. GENETICS !$#gene argG CLASSIFICATION #superfamily argininosuccinate synthase KEYWORDS ligase SUMMARY #length 487 #molecular-weight 53340 #checksum 8652 SEQUENCE /// ENTRY F64138 #type complete TITLE argininosuccinate synthase (EC 6.3.4.5) - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES citrulline-aspartate ligase ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS F64138 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession F64138 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-444 ##label TIGR !'##cross-references GB:U32845; GB:L42023; NID:g3212236; !1PIDN:AAC23373.1; PID:g1574583; TIGR:HI1727 CLASSIFICATION #superfamily argininosuccinate synthase KEYWORDS ligase SUMMARY #length 444 #molecular-weight 49289 #checksum 5005 SEQUENCE /// ENTRY JN0506 #type complete TITLE argininosuccinate synthase (EC 6.3.4.5) - Streptomyces lavendulae ALTERNATE_NAMES citrulline-aspartate ligase ORGANISM #formal_name Streptomyces lavendulae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS JN0506 REFERENCE JN0506 !$#authors Ogawara, H.; Kasama, H.; Nashimoto, K.; Ohtsubo, M.; !1Higashi, K.; Urabe, H. !$#journal Gene (1993) 125:91-96 !$#title Cloning, sequencing and expression of the argG gene from !1Streptomyces lavendulae. !$#cross-references MUID:93194084; PMID:8449418 !$#accession JN0506 !'##molecule_type DNA !'##residues 1-482 ##label OGA !'##cross-references DDBJ:D10691; NID:g287451; PIDN:BAA01533.1; !1PID:g287452 COMMENT This enzyme catalyzes the formation of argininosuccinate !1from citrulline and aspartate. GENETICS !$#gene argG CLASSIFICATION #superfamily argininosuccinate synthase KEYWORDS ligase SUMMARY #length 482 #molecular-weight 52382 #checksum 3283 SEQUENCE /// ENTRY AJECRS #type complete TITLE argininosuccinate synthase (EC 6.3.4.5) - Escherichia coli (strain K-12) ALTERNATE_NAMES citrulline-aspartate ligase ORGANISM #formal_name Escherichia coli DATE 30-Jun-1992 #sequence_revision 21-Nov-1997 #text_change 01-Mar-2002 ACCESSIONS G65107; JQ0778 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65107 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-447 ##label BLAT !'##cross-references GB:AE000398; GB:U00096; NID:g1789562; !1PIDN:AAC76205.1; PID:g1789563; UWGP:b3172 !'##experimental_source strain K-12, substrain MG1655 REFERENCE JQ0778 !$#authors Van Vliet, F.; Crabeel, M.; Boyen, A.; Tricot, C.; Stalon, !1V.; Falmagne, P.; Nakamura, Y.; Baumberg, S.; Glansdorff, N. !$#journal Gene (1990) 95:99-104 !$#title Sequences of the genes encoding argininosuccinate synthetase !1in Escherichia coli and Saccharomyces cerevisiae: comparison !1with methanogenic archaebacteria and mammals. !$#cross-references MUID:91071613; PMID:2123815 !$#accession JQ0778 !'##molecule_type DNA !'##residues 1-219,'N',221-327,'D',329-447 ##label VAN !'##cross-references GB:M35236; NID:g145341; PIDN:AAA23482.1; !1PID:g145342 GENETICS !$#gene argG CLASSIFICATION #superfamily argininosuccinate synthase KEYWORDS ligase SUMMARY #length 447 #molecular-weight 49898 #checksum 8702 SEQUENCE /// ENTRY AJMXRV #type complete TITLE argininosuccinate synthase (EC 6.3.4.5) - Methanococcus vannielii ALTERNATE_NAMES citrulline-aspartate ligase ORGANISM #formal_name Methanococcus vannielii DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 18-Jun-1999 ACCESSIONS C28180 REFERENCE A91873 !$#authors Morris, C.J.; Reeve, J.N. !$#journal J. Bacteriol. (1988) 170:3125-3130 !$#title Conservation of structure in the human gene encoding !1argininosuccinate synthetase and the argG genes of the !1archaebacteria Methanosarcina barkeri MS and Methanococcus !1vannielii. !$#cross-references MUID:88257029; PMID:3133361 !$#accession C28180 !'##molecule_type DNA !'##residues 1-397 ##label MOR !'##cross-references GB:M21315; NID:g150045; PIDN:AAA88322.1; !1PID:g150046 GENETICS !$#gene argG CLASSIFICATION #superfamily argininosuccinate synthase KEYWORDS ligase SUMMARY #length 397 #molecular-weight 44695 #checksum 8220 SEQUENCE /// ENTRY AJMZRB #type complete TITLE argininosuccinate synthase (EC 6.3.4.5) - Methanosarcina barkeri ALTERNATE_NAMES citrulline-aspartate ligase ORGANISM #formal_name Methanosarcina barkeri DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 18-Jun-1999 ACCESSIONS B28180 REFERENCE A91873 !$#authors Morris, C.J.; Reeve, J.N. !$#journal J. Bacteriol. (1988) 170:3125-3130 !$#title Conservation of structure in the human gene encoding !1argininosuccinate synthetase and the argG genes of the !1archaebacteria Methanosarcina barkeri MS and Methanococcus !1vannielii. !$#cross-references MUID:88257029; PMID:3133361 !$#accession B28180 !'##molecule_type DNA !'##residues 1-396 ##label MOR !'##cross-references GB:M21314; NID:g149816; PIDN:AAA72677.1; !1PID:g149818 !'##experimental_source strain MS GENETICS !$#gene argG CLASSIFICATION #superfamily argininosuccinate synthase KEYWORDS ligase SUMMARY #length 396 #molecular-weight 44441 #checksum 8557 SEQUENCE /// ENTRY AJBSAG #type complete TITLE phosphoribosylamine-glycine ligase (EC 6.3.4.13) [validated] - Bacillus subtilis ALTERNATE_NAMES phosphoribosylglycinamide synthetase ORGANISM #formal_name Bacillus subtilis DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 03-Jun-2002 ACCESSIONS B29183; C69684 REFERENCE A29326 !$#authors Ebbole, D.J.; Zalkin, H. !$#journal J. Biol. Chem. (1987) 262:8274-8287 !$#title Cloning and characterization of a 12-gene cluster from !1Bacillus subtilis encoding nine enzymes for de novo purine !1nucleotide synthesis. !$#cross-references MUID:87250425; PMID:3036807 !$#accession B29183 !'##molecule_type DNA !'##residues 1-422 ##label EBB !'##cross-references EMBL:J02732; NID:g143363; PIDN:AAA22684.1; !1PID:g143374 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69684 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-422 ##label KUN !'##cross-references GB:Z99107; GB:AL009126; NID:g2632866; !1PIDN:CAB12473.1; PID:g2632967 !'##experimental_source strain 168 GENETICS !$#gene purD !$#map_position 18 min FUNCTION !$#description EC 6.3.4.13 [validated, MUID:87250425] !$#pathway purine nucleotide biosynthesis CLASSIFICATION #superfamily phosphoribosylamine-glycine ligase; !1phosphoribosylamine-glycine ligase homology KEYWORDS ligase; purine nucleotide biosynthesis FEATURE !$2-415 #domain phosphoribosylamine-glycine ligase homology !8#label PGL SUMMARY #length 422 #molecular-weight 45280 #checksum 6513 SEQUENCE /// ENTRY AJECQG #type complete TITLE phosphoribosylamine-glycine ligase (EC 6.3.4.13) - Escherichia coli (strain K-12) ALTERNATE_NAMES glycinamide ribonucleotide synthetase ORGANISM #formal_name Escherichia coli DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Jun-2002 ACCESSIONS A33771; A34193; H65207 REFERENCE A33771 !$#authors Shen, Y.; Rudolph, J.; Stern, M.; Stubbe, J.; Flannigan, !1K.A.; Smith, J.M. !$#journal Biochemistry (1990) 29:218-227 !$#title Glycinamide ribonucleotide synthetase from Escherichia coli: !1cloning, overproduction, sequencing, isolation, and !1characterization. !$#cross-references MUID:90212572; PMID:2182115 !$#accession A33771 !'##molecule_type DNA !'##residues 1-429 ##label SHE !'##cross-references GB:X51950; NID:g42594; PIDN:CAA36213.1; PID:g42596 REFERENCE A92739 !$#authors Aiba, A.; Mizobuchi, K. !$#journal J. Biol. Chem. (1989) 264:21239-21246 !$#title Nucleotide sequence analysis of genes purH and purD involved !1in the de novo purine nucleotide biosynthesis of Escherichia !1coli. !$#cross-references MUID:90078227; PMID:2687276 !$#accession A34193 !'##molecule_type DNA !'##residues 1-14,'WR',17-96,'V',98-429 ##label AIB !'##cross-references EMBL:J05126; NID:g147419; PIDN:AAA24455.1; !1PID:g147421 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65207 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-429 ##label BLAT !'##cross-references GB:AE000473; GB:U00096; NID:g2367336; !1PIDN:AAC76979.1; PID:g1790438; UWGP:b4005 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene purD !$#map_position 90 min CLASSIFICATION #superfamily phosphoribosylamine-glycine ligase; !1phosphoribosylamine-glycine ligase homology KEYWORDS ligase; purine nucleotide biosynthesis FEATURE !$2-422 #domain phosphoribosylamine-glycine ligase homology !8#label PGL SUMMARY #length 429 #molecular-weight 45940 #checksum 1586 SEQUENCE /// ENTRY S18489 #type complete TITLE phosphoribosylamine-glycine ligase (EC 6.3.4.13) - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S18489 REFERENCE S18488 !$#authors Chopra, A.K.; Peterson, J.W.; Prasad, R. !$#journal Biochim. Biophys. Acta (1991) 1090:351-354 !$#title Nucleotide sequence analysis of purH and purD genes from !1Salmonella typhimurium. !$#cross-references MUID:92062738; PMID:1954258 !$#accession S18489 !'##status preliminary !'##molecule_type DNA !'##residues 1-429 ##label CHO !'##cross-references EMBL:M66160; NID:g154286; PIDN:AAA27198.1; !1PID:g154288 CLASSIFICATION #superfamily phosphoribosylamine-glycine ligase; !1phosphoribosylamine-glycine ligase homology KEYWORDS ligase FEATURE !$2-422 #domain phosphoribosylamine-glycine ligase homology !8#label PGL SUMMARY #length 429 #molecular-weight 45692 #checksum 56 SEQUENCE /// ENTRY C64100 #type complete TITLE phosphoribosylamine-glycine ligase (EC 6.3.4.13) - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES phosphoribosylglycinamide synthetase ORGANISM #formal_name Haemophilus influenzae DATE 18-Aug-1995 #sequence_revision 04-Oct-1996 #text_change 03-Jun-2002 ACCESSIONS C64100 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession C64100 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-429 ##label TIGR !'##cross-references GB:U32770; GB:L42023; NID:g1573898; !1PIDN:AAC22545.1; PID:g1573905; TIGR:HI0888 CLASSIFICATION #superfamily phosphoribosylamine-glycine ligase; !1phosphoribosylamine-glycine ligase homology KEYWORDS ligase; purine nucleotide biosynthesis FEATURE !$2-421 #domain phosphoribosylamine-glycine ligase homology !8#label PGL SUMMARY #length 429 #molecular-weight 46248 #checksum 6168 SEQUENCE /// ENTRY A64417 #type complete TITLE phosphoribosylamine-glycine ligase (EC 6.3.4.13) - Methanococcus jannaschii ALTERNATE_NAMES glycinamide ribonucleotide synthetase ORGANISM #formal_name Methanococcus jannaschii DATE 13-Sep-1996 #sequence_revision 04-Oct-1996 #text_change 03-Jun-2002 ACCESSIONS A64417 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession A64417 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-444 ##label BUL !'##cross-references GB:U67537; GB:L77117; NID:g2826351; !1PIDN:AAB98942.1; PID:g1499772; TIGR:MJ0937 GENETICS !$#map_position FOR866111-867445 CLASSIFICATION #superfamily phosphoribosylamine-glycine ligase; !1phosphoribosylamine-glycine ligase homology KEYWORDS ligase; purine nucleotide biosynthesis FEATURE !$2-429 #domain phosphoribosylamine-glycine ligase homology !8#label PGL SUMMARY #length 444 #molecular-weight 49097 #checksum 5218 SEQUENCE /// ENTRY S75867 #type complete TITLE phosphoribosylamine-glycine ligase (EC 6.3.4.13) - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein slr1159 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S75867 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75867 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-419 ##label KAN !'##cross-references EMBL:D90913; GB:AB001339; NID:g1653348; !1PIDN:BAA18326.1; PID:g1653412 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene purD CLASSIFICATION #superfamily phosphoribosylamine-glycine ligase; !1phosphoribosylamine-glycine ligase homology KEYWORDS ligase; purine nucleotide biosynthesis FEATURE !$2-417 #domain phosphoribosylamine-glycine ligase homology !8#label PGL SUMMARY #length 419 #molecular-weight 44016 #checksum 253 SEQUENCE /// ENTRY A26343 #type complete TITLE phosphoribosylamine-glycine ligase (EC 6.3.4.13) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES AIRSase; aminoimidazole ribotide synthetase; GARSase; glycinamide ribonucleotide synthetase; glycinamide ribotide synthetase; phosphoribosylaminoimidazole synthetase; protein G0930; protein YGL234w CONTAINS phosphoribosylamine-glycine ligase (EC 6.3.4.13); phosphoribosylformylglycinamidine cyclo-ligase (EC 6.3.3.1) ORGANISM #formal_name Saccharomyces cerevisiae DATE 19-Nov-1988 #sequence_revision 28-Oct-1994 #text_change 03-Jun-2002 ACCESSIONS A26343; S64256; S55759 REFERENCE A26343 !$#authors Henikoff, S. !$#journal J. Mol. Biol. (1986) 190:519-528 !$#title The Saccharomyces cerevisiae ADE5,7 protein is homologous to !1overlapping Drosophila melanogaster Gart polypeptides. !$#cross-references MUID:87061006; PMID:3097325 !$#accession A26343 !'##molecule_type DNA !'##residues 1-802 ##label HEN !'##cross-references EMBL:X04337; NID:g3334; PIDN:CAA27867.1; PID:g3335 REFERENCE S64248 !$#authors Fartmann, B.; Kramer, B.; Kramer, W. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64256 !'##molecule_type DNA !'##residues 1-802 ##label FAR !'##cross-references EMBL:Z72756; NID:g1322894; PIDN:CAA96952.1; !1PID:g1322895; GSPDB:GN00007; MIPS:YGL234w !'##experimental_source strain S288C REFERENCE S55757 !$#authors Boucherie, H.; Dujardin, G.; Kermorgant, M.; Monribot, C.; !1Slonimski, P.; Perrot, M. !$#journal Yeast (1995) 11:601-613 !$#title Two-dimensional protein map of Saccharomyces cerevisiae: !1construction of a gene-protein index. !$#cross-references MUID:96093904; PMID:7483834 !$#accession S55759 !'##molecule_type protein !'##residues 1-6,'XX',9,'X',11,'X',13 ##label BOU GENETICS !$#gene SGD:ADE5.7; MIPS:YGL234w !'##cross-references SGD:S0003203; MIPS:YGL234w !$#map_position 7L CLASSIFICATION #superfamily Saccharomyces cerevisiae ADE5 multifunctional !1protein; phosphoribosylamine-glycine ligase homology; !1phosphoribosylformylglycinamidine cyclo-ligase homology KEYWORDS cyclo-ligase; purine nucleotide biosynthesis FEATURE !$3-438 #domain phosphoribosylamine-glycine ligase homology !8#label PGL\ !$452-783 #domain phosphoribosylformylglycinamidine !8cyclo-ligase homology #label PFCL SUMMARY #length 802 #molecular-weight 86067 #checksum 3759 SEQUENCE /// ENTRY S00652 #type complete TITLE phosphoribosylamine-glycine ligase (EC 6.3.4.13) - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES AIRSase; aminoimidazole ribotide synthetase; GARSase; glycinamide ribonucleotide synthetase; glycinamide ribotide synthetase; phosphoribosylaminoimidazole synthetase CONTAINS phosphoribosylamine-glycine ligase (EC 6.3.4.13); phosphoribosylformylglycinamidine cyclo-ligase (EC 6.3.3.1) ORGANISM #formal_name Schizosaccharomyces pombe DATE 07-Sep-1990 #sequence_revision 28-Oct-1994 #text_change 03-Jun-2002 ACCESSIONS S00652; T40496; T40422 REFERENCE S00652 !$#authors McKenzie, R.; Schuchert, P.; Kilbey, B. !$#journal Curr. Genet. (1987) 12:591-597 !$#title Sequence of the bifunctional ade1 gene in the purine !1biosynthetic pathway of the fission yeast !1Schizosaccharomyces pombe. !$#cross-references MUID:89003164; PMID:3502942 !$#accession S00652 !'##molecule_type DNA !'##residues 1-788 ##label MCK !'##cross-references EMBL:X06601; NID:g4903; PIDN:CAA29820.1; PID:g4904 REFERENCE Z21910 !$#authors Wood, V.; Rajandream, M.A.; Barrell, B.G.; Lauber, J.; !1Hilbert, H.; Duesterhoeft, A. !$#submission submitted to the EMBL Data Library, February 1998 !$#accession T40496 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-788 ##label WOO !'##cross-references EMBL:AL021730; PIDN:CAA16823.1; GSPDB:GN00067; !1SPDB:SPBC4C3.02c !'##experimental_source strain 972h-; cosmid c4C3 REFERENCE Z21928 !$#authors Seeger, K.; Harris, D.; Wood, V.; Rajandream, M.A.; Barrell, !1B.G. !$#submission submitted to the EMBL Data Library, March 1999 !$#accession T40422 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 604-788 ##label SEE !'##cross-references EMBL:AL035655; PIDN:CAB38600.1; GSPDB:GN00067; !1SPDB:SPBC405.01 !'##experimental_source strain 972h-; cosmid c405 GENETICS !$#gene ADE1; SPDB:SPBC405.01 !$#map_position 2 CLASSIFICATION #superfamily Saccharomyces cerevisiae ADE5 multifunctional !1protein; phosphoribosylamine-glycine ligase homology; !1phosphoribosylformylglycinamidine cyclo-ligase homology KEYWORDS cyclo-ligase; purine nucleotide biosynthesis FEATURE !$5-425 #domain phosphoribosylamine-glycine ligase homology !8#label PGL\ !$439-767 #domain phosphoribosylformylglycinamidine !8cyclo-ligase homology #label PFCL SUMMARY #length 788 #molecular-weight 85231 #checksum 4919 SEQUENCE /// ENTRY BVECBF #type complete TITLE biotin-[acetyl-CoA-carboxylase] ligase (EC 6.3.4.15) - Escherichia coli (strain K-12) CONTAINS biotin operon repressor; biotin-[acetyl-CoA-carboxylase] ligase (EC 6.3.4.15) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Dec-1988 #text_change 03-Jun-2002 ACCESSIONS B24029; B45727; D65204; A24989 REFERENCE A91525 !$#authors Howard, P.K.; Shaw, J.; Otsuka, A.J. !$#journal Gene (1985) 35:321-331 !$#title Nucleotide sequence of the birA gene encoding the biotin !1operon repressor and biotin holoenzyme synthetase functions !1of Escherichia coli. !$#cross-references MUID:86006282; PMID:3899863 !$#accession B24029 !'##molecule_type DNA !'##residues 1-321 ##label HOW !'##cross-references GB:M10123; NID:g145430; PIDN:AAA23520.1; !1PID:g145432 REFERENCE A24989 !$#authors Buoncristiani, M.R.; Howard, P.K.; Otsuka, A.J. !$#journal Gene (1986) 44:255-261 !$#title DNA-binding and enzymatic domains of the bifunctional biotin !1operon repressor (BirA) of Escherichia coli. !$#cross-references MUID:87055242; PMID:3536662 !$#contents annotation; domain information !$#note this paper reports mutational studies done to understand !1DNA-binding and enzymatic functions of BirA protein REFERENCE A45727 !$#authors Song, W.J.; Jackowski, S. !$#journal J. Bacteriol. (1992) 174:6411-6417 !$#title Cloning, sequencing, and expression of the pantothenate !1kinase (coaA) gene of Escherichia coli. !$#cross-references MUID:93015690; PMID:1328157 !$#accession B45727 !'##status preliminary !'##molecule_type DNA !'##residues 226-321 ##label SON !'##cross-references GB:M90071 !'##note residues 246-247 are correct to paper REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65204 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-321 ##label BLAT !'##cross-references GB:AE000471; GB:U00096; NID:g1790404; !1PIDN:AAC76951.1; PID:g1790408; UWGP:b3973 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene birA !$#map_position 89 min FUNCTION ENZ !$#description EC 6.3.4.15 [validated; MUID:99400973]; !1biotin-[acetyl-CoA-carboxylase] ligase; activates biotin to !1form biotinyl-5'-adenylate and catalyzes covalent linkage of !1the biotin moiety to biotin-accepting proteins FUNCTION REP !$#description acts as a biotin operon repressor [validated; MUID:99400973] !1; the reaction intermediate biotinoyl-5'-AMP triggers !1binding of birA to the biotin operon repressor and thus !1functions as corepressor !$#note the switch of birA from a biotin ligase to a repressor !1reflects competition between biotin-accepting protein !1substrate and operator DNA for the birA-biotinoyl-5'-AMP !1complex CLASSIFICATION #superfamily birA bifunctional protein KEYWORDS ATP; biotin metabolism; DNA binding; ligase; repressor; !1transcription regulation FEATURE !$1-26 #domain DNA binding #status predicted #label DNA\ !$83-119,189-235 #domain biotin activation #status predicted #label !8BIO SUMMARY #length 321 #molecular-weight 35312 #checksum 5591 SEQUENCE /// ENTRY AJHUPR #type complete TITLE phosphoribosylamine-glycine ligase (EC 6.3.4.13) - human ALTERNATE_NAMES glycinamide ribonucleotide synthetase (GARSase); glycinamide ribonucleotide transformylase (GARTase); phosphoribosyl-aminoimidazole synthetase (AIRSase) CONTAINS phosphoribosylamine-glycine ligase (EC 6.3.4.13); phosphoribosylformylglycinamidine cyclo-ligase (EC 6.3.3.1); phosphoribosylglycinamide formyltransferase (EC 2.1.2.2) ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Jun-2002 ACCESSIONS S12616; A35632; B33097 REFERENCE S12616 !$#authors Aimi, J.; Qiu, H.; Williams, J.; Zalkin, H.; Dixon, J.E. !$#journal Nucleic Acids Res. (1990) 18:6665-6672 !$#title De novo purine nucleotide biosynthesis: cloning of human and !1avian cDNAs encoding the trifunctional glycinamide !1ribonucleotide synthetase-aminoimidazole ribonucleotide !1synthetase-glycinamide ribonucleotide transformylase by !1functional complementation in E. coli. !$#cross-references MUID:91067455; PMID:2147474 !$#accession S12616 !'##molecule_type mRNA !'##residues 1-1010 ##label AIM !'##cross-references EMBL:X54199; NID:g31641; PIDN:CAA38119.1; !1PID:g31642 REFERENCE A35632 !$#authors Schild, D.; Brake, A.J.; Kiefer, M.C.; Young, D.; Barr, P.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:2916-2920 !$#title Cloning of three human multifunctional de novo purine !1biosynthetic genes by functional complementation of yeast !1mutations. !$#cross-references MUID:90222141; PMID:2183217 !$#accession A35632 !'##molecule_type mRNA !'##residues 1-38;709-715,'G',753-1010 ##label SCH !'##cross-references GB:M32082 GENETICS !$#gene GDB:GART; PGFT !'##cross-references GDB:119487; OMIM:138440 !$#map_position 21q22.1-21q22.1 CLASSIFICATION #superfamily purine synthesis multifunctional protein; !1phosphoribosylamine-glycine ligase homology; !1phosphoribosylformylglycinamidine cyclo-ligase homology; !1phosphoribosylglycinamide formyltransferase homology KEYWORDS alternative splicing; cyclo-ligase; methyltransferase; !1multifunctional enzyme; purine nucleotide biosynthesis FEATURE !$4-424 #domain phosphoribosylamine-glycine ligase homology !8#label PGL\ !$437-766 #domain phosphoribosylformylglycinamidine !8cyclo-ligase homology #label PFCL\ !$810-1001 #domain phosphoribosylglycinamide formyltransferase !8homology #label PRGF SUMMARY #length 1010 #molecular-weight 107766 #checksum 5272 SEQUENCE /// ENTRY I67805 #type complete TITLE phosphoribosylamine-glycine ligase (EC 6.3.4.13) - mouse ALTERNATE_NAMES glycinamide ribonucleotide synthetase (GARSase); glycinamide ribonucleotide transformylase (GARTase); phosphoribosyl-aminoimidazole synthetase (AIRSase) CONTAINS phosphoribosylamine-glycine ligase (EC 6.3.4.13); phosphoribosylformylglycinamidine cyclo-ligase (EC 6.3.3.1); phosphoribosylglycinamide formyltransferase (EC 2.1.2.2) ORGANISM #formal_name Mus musculus #common_name house mouse DATE 02-Aug-1996 #sequence_revision 27-Feb-1997 #text_change 03-Jun-2002 ACCESSIONS I67805; I53700; T46882 REFERENCE I53700 !$#authors Kan, J.L.; Jannatipour, M.; Taylor, S.M.; Moran, R.G. !$#journal Gene (1993) 137:195-202 !$#title Mouse cDNAs encoding a trifunctional protein of de novo !1purine synthesis and a related single-domain glycinamide !1ribonucleotide synthetase. !$#cross-references MUID:94131283; PMID:8299947 !$#accession I67805 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-1010 ##label KAN1 !'##cross-references EMBL:U01024; NID:g403492; PIDN:AAA19013.1; !1PID:g403493 !$#accession I53700 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-433 ##label KAN2 !'##cross-references EMBL:U01023; NID:g403490; PIDN:AAA19012.1; !1PID:g403491 !'##experimental_source cell line EL4 FUNCTION GARS !$#description as phosphoribosylamine-glycine ligase, catalyzes the !1condensation of phosphoribosylamine, glycine, and ATP to !1form glycinamide ribonucleotide, ADP, and phosphate !$#pathway purine nucleotide biosynthesis FUNCTION AIRS !$#description as phosphoribosylformylglycinamidine cyclo-ligase, catalyzes !1the cyclization of N-formylglycinamidine ribonucleotide with !1ATP to form 5-aminoimdazole ribonucleotide, ADP, and !1phosphate !$#pathway purine nucleotide biosynthesis FUNCTION GART !$#description as phosphoribosylglycinamide formyltransferase, catalyzes !1the reaction of glycinamide ribonucleotide, N5, !1N10-methenyltetrahydrofolate, and water to form !1N-formylglycinamide ribonucleotide, tetrahydrofolate, and !1hydrogen ion !$#pathway purine nucleotide biosynthesis CLASSIFICATION #superfamily purine synthesis multifunctional protein; !1phosphoribosylamine-glycine ligase homology; !1phosphoribosylformylglycinamidine cyclo-ligase homology; !1phosphoribosylglycinamide formyltransferase homology KEYWORDS alternative splicing; cyclo-ligase; methyltransferase; !1multifunctional enzyme; purine nucleotide biosynthesis FEATURE !$1-433 #product phosphoribosylamine-glycine ligase, !8single-domain form #link GARS #status predicted !8#label MATL\ !$4-424 #domain phosphoribosylamine-glycine ligase homology !8#label PGL\ !$437-766 #domain phosphoribosylformylglycinamidine !8cyclo-ligase homology #label PFCL\ !$810-1001 #domain phosphoribosylglycinamide formyltransferase !8homology #label PRGF\ !$915,951 #active_site His, Asp #link GART #status predicted SUMMARY #length 1010 #molecular-weight 107382 #checksum 4261 SEQUENCE /// ENTRY AJCHPR #type complete TITLE phosphoribosylamine-glycine ligase (EC 6.3.4.13) - chicken ALTERNATE_NAMES glycinamide ribonucleotide synthetase; glycinamide ribonucleotide transformylase; phosphoribosyl-aminoimidazole synthetase CONTAINS phosphoribosylamine-glycine ligase (EC 6.3.4.13); phosphoribosylformylglycinamidine cyclo-ligase (EC 6.3.3.1); phosphoribosylglycinamide formyltransferase (EC 2.1.2.2) ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Jun-2002 ACCESSIONS S12617; A33097 REFERENCE S12616 !$#authors Aimi, J.; Qiu, H.; Williams, J.; Zalkin, H.; Dixon, J.E. !$#journal Nucleic Acids Res. (1990) 18:6665-6672 !$#title De novo purine nucleotide biosynthesis: cloning of human and !1avian cDNAs encoding the trifunctional glycinamide !1ribonucleotide synthetase-aminoimidazole ribonucleotide !1synthetase-glycinamide ribonucleotide transformylase by !1functional complementation in E. coli. !$#cross-references MUID:91067455; PMID:2147474 !$#accession S12617 !'##molecule_type mRNA !'##residues 1-1003 ##label AIM !'##cross-references EMBL:X54200; NID:g62898; PIDN:CAA38120.1; !1PID:g62899 CLASSIFICATION #superfamily purine synthesis multifunctional protein; !1phosphoribosylamine-glycine ligase homology; !1phosphoribosylformylglycinamidine cyclo-ligase homology; !1phosphoribosylglycinamide formyltransferase homology KEYWORDS alternative splicing; cyclo-ligase; methyltransferase; !1multifunctional enzyme; purine nucleotide biosynthesis FEATURE !$4-424 #domain phosphoribosylamine-glycine ligase homology !8#label PGL\ !$437-764 #domain phosphoribosylformylglycinamidine !8cyclo-ligase homology #label PFCL\ !$806-997 #domain phosphoribosylglycinamide formyltransferase !8homology #label PRGF SUMMARY #length 1003 #molecular-weight 106543 #checksum 8419 SEQUENCE /// ENTRY AJFFPM #type complete TITLE phosphoribosylamine-glycine ligase (EC 6.3.4.13) - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES glycinamide ribonucleotide synthetase (GARSase); glycinamide ribonucleotide transformylase (GARTase); phosphoribosyl-aminoimidazole synthetase (AIRSase) CONTAINS phosphoribosylamine-glycine ligase (EC 6.3.4.13); phosphoribosylformylglycinamidine cyclo-ligase (EC 6.3.3.1); phosphoribosylglycinamide formyltransferase (EC 2.1.2.2) ORGANISM #formal_name Drosophila melanogaster DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Jun-2002 ACCESSIONS S01206; A24787; A01196; A21201 REFERENCE S01204 !$#authors Henikoff, S.; Eghtedarzadeh, M.K. !$#journal Genetics (1987) 117:711-725 !$#title Conserved arrangement of nested genes at the Drosophila Gart !1locus. !$#cross-references MUID:88112752; PMID:3123310 !$#accession S01206 !'##molecule_type DNA !'##residues 1-1353 ##label HEN1 !'##cross-references EMBL:X06286; NID:g7995; PIDN:CAA29612.1; !1PID:g295747 REFERENCE A90876 !$#authors Henikoff, S.; Keene, M.A.; Fechtel, K.; Fristrom, J.W. !$#journal Cell (1986) 44:33-42 !$#title Gene within a gene: nested Drosophila genes encode unrelated !1proteins on opposite DNA strands. !$#cross-references MUID:86079579; PMID:3079672 !$#accession A24787 !'##molecule_type DNA !'##residues 1-141 ##label HEN2 !'##cross-references GB:J02527 REFERENCE A01196 !$#authors Henikoff, S.; Furlong, C.E. !$#journal Nucleic Acids Res. (1983) 11:789-800 !$#title Sequence of a Drosophila DNA segment that functions in !1Saccharomyces cerevisiae and its regulation by a yeast !1promoter. !$#cross-references MUID:83168902; PMID:6300768 !$#accession A01196 !'##molecule_type DNA !'##residues 1148-1353 ##label HEN3 !'##cross-references GB:K02461 !'##note the authors translated the codon GAG for residue 1317 as Ala REFERENCE A21201 !$#authors Henikoff, S.; Sloan, J.S.; Kelly, J.D. !$#journal Cell (1983) 34:405-414 !$#title A Drosophila metabolic gene transcript is alternatively !1processed. !$#cross-references MUID:84002248; PMID:6413075 !$#accession A21201 !'##molecule_type DNA !'##residues 60-1147 ##label HEN4 !'##cross-references GB:X00041 GENETICS !$#gene Gart !'##cross-references FlyBase:FBgn0000053 !$#map_position 2L 27C !$#introns 59/3; 142/2; 359/1; 434/2; 575/1; 925/1 CLASSIFICATION #superfamily Drosophila purine synthesis multifunctional !1protein; phosphoribosylamine-glycine ligase homology; !1phosphoribosylformylglycinamidine cyclo-ligase homology; !1phosphoribosylglycinamide formyltransferase homology KEYWORDS alternative splicing; cyclo-ligase; methyltransferase; !1multifunctional enzyme; purine nucleotide biosynthesis FEATURE !$4-430 #domain phosphoribosylamine-glycine ligase homology !8#label PGL\ !$444-775 #domain phosphoribosylformylglycinamidine !8cyclo-ligase homology #label PFC\ !$792-1122 #domain phosphoribosylformylglycinamidine !8cyclo-ligase homology #label PFCL\ !$1148-1353 #domain phosphoribosylglycinamide formyltransferase !8#status experimental #label GART\ !$1156-1349 #domain phosphoribosylglycinamide formyltransferase !8homology #label PRGF SUMMARY #length 1353 #molecular-weight 144447 #checksum 1822 SEQUENCE /// ENTRY AJFFPP #type complete TITLE phosphoribosylamine-glycine ligase (EC 6.3.4.13) - fruit fly (Drosophila pseudoobscura) ALTERNATE_NAMES glycinamide ribonucleotide synthetase (GARSase); glycinamide ribonucleotide transformylase (GARTase); phosphoribosyl-aminoimidazole synthetase (AIRSase) CONTAINS phosphoribosylamine-glycine ligase (EC 6.3.4.13); phosphoribosylformylglycinamidine cyclo-ligase (EC 6.3.3.1); phosphoribosylglycinamide formyltransferase (EC 2.1.2.2) ORGANISM #formal_name Drosophila pseudoobscura DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Jun-2002 ACCESSIONS S01204 REFERENCE S01204 !$#authors Henikoff, S.; Eghtedarzadeh, M.K. !$#journal Genetics (1987) 117:711-725 !$#title Conserved arrangement of nested genes at the Drosophila Gart !1locus. !$#cross-references MUID:88112752; PMID:3123310 !$#accession S01204 !'##molecule_type DNA !'##residues 1-1364 ##label HEN !'##cross-references EMBL:X06285; NID:g9055; PIDN:CAA29611.1; !1PID:g295787 !'##note monofunctional phosphoribosylamine-glycine ligase, prepared by !1alternative splicing, corresponds to residues 1-433 and !1contains an additional 434-Met GENETICS !$#gene Gart !'##cross-references FlyBase:FBgn0000053 !$#map_position 4 88 !$#introns 59/3; 142/2; 359/1; 434/2; 575/1; 927/1 CLASSIFICATION #superfamily Drosophila purine synthesis multifunctional !1protein; phosphoribosylamine-glycine ligase homology; !1phosphoribosylformylglycinamidine cyclo-ligase homology; !1phosphoribosylglycinamide formyltransferase homology KEYWORDS alternative splicing; cyclo-ligase; methyltransferase; !1multifunctional enzyme; purine nucleotide biosynthesis FEATURE !$4-430 #domain phosphoribosylamine-glycine ligase homology !8#label PGL\ !$444-775 #domain phosphoribosylformylglycinamidine !8cyclo-ligase homology #label PFC\ !$794-1124 #domain phosphoribosylformylglycinamidine !8cyclo-ligase homology #label PFCL\ !$1158-1351 #domain phosphoribosylglycinamide formyltransferase !8homology #label PRGF SUMMARY #length 1364 #molecular-weight 145692 #checksum 5275 SEQUENCE /// ENTRY SYECGU #type complete TITLE GMP synthase (glutamine-hydrolyzing) (EC 6.3.5.2) [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 17-Mar-1987 #sequence_revision 30-Sep-1987 #text_change 01-Mar-2002 ACCESSIONS A24640; B65027; A01197 REFERENCE A92546 !$#authors Tiedeman, A.A.; Smith, J.M.; Zalkin, H. !$#journal J. Biol. Chem. (1985) 260:8676-8679 !$#title Nucleotide sequence of the guaA gene encoding GMP synthetase !1of Escherichia coli K23. !$#cross-references MUID:85261223; PMID:3894345 !$#accession A24640 !'##molecule_type DNA !'##residues 1-525 ##label TIE !'##cross-references GB:M10101; GB:M10102; NID:g146274; PIDN:AAB18619.1; !1PID:g146276 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65027 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-525 ##label BLAT !'##cross-references GB:AE000337; GB:U00096; NID:g1788850; !1PIDN:AAC75560.1; PID:g1788854; UWGP:b2507 !'##experimental_source strain K-12, substrain MG1655 COMMENT The active enzyme catalyzes the formation of GMP by !1transferring the amide group from glutamine to XMP in the !1presence of ATP. GENETICS !$#gene guaA !$#map_position 54 min FUNCTION !$#description EC 6.3.5.2 [validated, MUID:85261223] CLASSIFICATION #superfamily GMP synthase (glutamine-hydrolyzing); trpG !1homology KEYWORDS homodimer; ligase; purine nucleotide biosynthesis FEATURE !$10-198 #domain trpG homology #label TRG\ !$239-401 #domain GMP binding #status predicted #label GMP\ !$86 #active_site Cys #status predicted SUMMARY #length 525 #molecular-weight 58679 #checksum 3240 SEQUENCE /// ENTRY I64055 #type complete TITLE GMP synthase (glutamine-hydrolyzing) (EC 6.3.5.2) - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS I64055 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession I64055 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-523 ##label TIGR !'##cross-references GB:U32708; GB:L42023; NID:g3212186; !1PIDN:AAC21891.1; PID:g1573186; TIGR:HI0222 !'##note named as homolog to a protein from Escherichia coli CLASSIFICATION #superfamily GMP synthase (glutamine-hydrolyzing); trpG !1homology KEYWORDS ligase; purine nucleotide biosynthesis FEATURE !$9-196 #domain trpG homology #label TRG\ !$237-399 #domain GMP binding #status predicted #label GMP\ !$85 #active_site Cys #status predicted SUMMARY #length 523 #molecular-weight 58185 #checksum 7081 SEQUENCE /// ENTRY C69638 #type complete TITLE GMP synthase (glutamine-hydrolyzing) (EC 6.3.5.2) guaA - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS C69638; B42280 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69638 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-513 ##label KUN !'##cross-references GB:Z99107; GB:AL009126; NID:g2632866; !1PIDN:CAB12455.1; PID:g2632949 !'##experimental_source strain 168 REFERENCE A42280 !$#authors Mantsala, P.; Zalkin, H. !$#journal J. Bacteriol. (1992) 174:1883-1890 !$#title Cloning and sequence of Bacillus subtilis purA and guaA, !1involved in the conversion of IMP to AMP and GMP. !$#cross-references MUID:92193275; PMID:1312531 !$#accession B42280 !'##status preliminary !'##molecule_type DNA !'##residues 1-102,'T',104-127,'G',129-162,'G',164-167,'H',169-195,'S', !1197-215,'Q',217-224,'G',226-261,'R',263-513 ##label MAN !'##note sequence inconsistent with the nucleotide translation !'##note sequence extracted from NCBI backbone (NCBIN:88687, !1NCBIP:88689) GENETICS !$#gene guaA CLASSIFICATION #superfamily GMP synthase (glutamine-hydrolyzing); trpG !1homology KEYWORDS ligase; purine nucleotide biosynthesis FEATURE !$9-190 #domain trpG homology #label TRG\ !$231-390 #domain GMP binding #status predicted #label GMP\ !$85 #active_site Cys #status predicted SUMMARY #length 513 #molecular-weight 57952 #checksum 9234 SEQUENCE /// ENTRY SYBS1G #type complete TITLE phosphoribosylformylglycinamidine synthase (EC 6.3.5.3) component I [validated] - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jun-2000 ACCESSIONS F29326; H69684 REFERENCE A29326 !$#authors Ebbole, D.J.; Zalkin, H. !$#journal J. Biol. Chem. (1987) 262:8274-8287 !$#title Cloning and characterization of a 12-gene cluster from !1Bacillus subtilis encoding nine enzymes for de novo purine !1nucleotide synthesis. !$#cross-references MUID:87250425; PMID:3036807 !$#accession F29326 !'##molecule_type DNA !'##residues 1-227 ##label EBB !'##cross-references EMBL:J02732; NID:g143363; PIDN:AAA22678.1; !1PID:g143368 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69684 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-227 ##label KUN !'##cross-references GB:Z99107; GB:AL009126; NID:g2632866; !1PIDN:CAB12467.1; PID:g2632961 !'##experimental_source strain 168 GENETICS !$#gene purQ !$#map_position 18 min !$#note this gene is designated purL by the SubtiList Web Server COMPLEX heterodimer; component I (PIR:SYBS1G) and component II !1(PIR:SYBS2G) FUNCTION !$#description EC 6.3.5.3 [validated, MUID:87250425]; catalyzes the !1condensation of 5'-phosphoribosylformylglycinamide with ATP, !1L-glutamine and water to form !15'-phosphoribosylformylglycinamidine, ADP, phosphate and !1L-glutamate !$#pathway purine nucleotide biosynthesis CLASSIFICATION #superfamily phosphoribosylformylglycinamidine synthase !1component I KEYWORDS heterodimer; ligase; purine nucleotide biosynthesis FEATURE !$86 #active_site Cys #status predicted SUMMARY #length 227 #molecular-weight 24784 #checksum 5742 SEQUENCE /// ENTRY SYBS2G #type complete TITLE phosphoribosylformylglycinamidine synthase (EC 6.3.5.3) component II - Bacillus subtilis ALTERNATE_NAMES formylglycinamide ribotide amidotransferase ORGANISM #formal_name Bacillus subtilis DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jun-2000 ACCESSIONS G29326; C69685 REFERENCE A29326 !$#authors Ebbole, D.J.; Zalkin, H. !$#journal J. Biol. Chem. (1987) 262:8274-8287 !$#title Cloning and characterization of a 12-gene cluster from !1Bacillus subtilis encoding nine enzymes for de novo purine !1nucleotide synthesis. !$#cross-references MUID:87250425; PMID:3036807 !$#accession G29326 !'##molecule_type DNA !'##residues 1-742 ##label EBB !'##cross-references EMBL:J02732; NID:g143363; PIDN:AAA22679.1; !1PID:g143369 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69685 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-742 ##label KUN !'##cross-references GB:Z99107; GB:AL009126; NID:g2632866; !1PIDN:CAB12468.1; PID:g2632962 !'##experimental_source strain 168 GENETICS !$#gene purL !$#map_position 18 min !$#note this gene is designated purQ by the SubtiList Web Server COMPLEX heterodimer with component I (see PIR:SYBS1G) FUNCTION !$#description catalyzes the condensation of !15'-phosphoribosylformylglycinamide with ATP, L-glutamine and !1water to form 5'-phosphoribosylformylglycinamidine, ADP, !1phosphate and L-glutamate !$#pathway purine nucleotide biosynthesis CLASSIFICATION #superfamily phosphoribosylformylglycinamidine synthase !1component II KEYWORDS heterodimer; ligase; purine nucleotide biosynthesis SUMMARY #length 742 #molecular-weight 80291 #checksum 8002 SEQUENCE /// ENTRY JC1290 #type complete TITLE phosphoribosylformylglycinamidine synthase (EC 6.3.5.3) component II - Lactobacillus casei ORGANISM #formal_name Lactobacillus casei DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JC1290; JC2024 REFERENCE JC1290 !$#authors Gu, Z.M.; Martindale, D.W.; Lee, B.H. !$#journal Gene (1992) 119:123-126 !$#title Isolation and complete sequence of the purL gene encoding !1FGAM synthase II in Lactobacillus casei. !$#cross-references MUID:93012962; PMID:1398079 !$#accession JC1290 !'##molecule_type DNA !'##residues 1-741 ##label GUZ REFERENCE JC2024 !$#authors Gu, Z.M.; Martindale, D.W.; Lee, B.H. !$#journal Gene (1993) 133:147 !$#cross-references MUID:94040790; PMID:8224889 !$#contents erratum !$#accession JC2024 !'##molecule_type DNA !'##residues 1-738,'KA' ##label GU2 !'##cross-references GB:M85265; NID:g308865; PIDN:AAC36947.1; !1PID:g308866 !'##note this sequence corrected phosphoribosylformylglycinamidine !1synthase chain II carboxyl-terminal sequencing errors in !1JC1290 COMMENT This enzyme catalyzes the conversion of !1phosphoribosylformylglycinamide to !1phosphoribosylformylglycinamidine. GENETICS !$#gene purL CLASSIFICATION #superfamily phosphoribosylformylglycinamidine synthase !1component II KEYWORDS ligase; purine nucleotide biosynthesis SUMMARY #length 741 #molecular-weight 79580 #checksum 6340 SEQUENCE /// ENTRY S74494 #type complete TITLE phosphoribosylformylglycinamidine synthase (EC 6.3.5.3) component II - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES formylglycinamide ribotide amidotransferase; phosphoribosylformylglycinamidine synthetase; protein sll1056 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 30-Oct-1998 #sequence_revision 30-Oct-1998 #text_change 16-Jun-2000 ACCESSIONS S74494 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74494 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-777 ##label KAN !'##cross-references EMBL:D90899; GB:AB001339; NID:g1651650; !1PIDN:BAA16646.1; PID:g1651718 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene purL FUNCTION !$#description catalyzes the condensation of !15'-phosphoribosylformylglycinamide with ATP, L-glutamine and !1water to form 5'-phosphoribosylformylglycinamidine, ADP, !1phosphate and L-glutamate !$#pathway purine nucleotide biosynthesis CLASSIFICATION #superfamily phosphoribosylformylglycinamidine synthase !1component II KEYWORDS ligase; purine nucleotide biosynthesis SUMMARY #length 777 #molecular-weight 82818 #checksum 8005 SEQUENCE /// ENTRY A70458 #type complete TITLE phosphoribosylformylglycinamidine synthase (EC 6.3.5.3) component II - Aquifex aeolicus ALTERNATE_NAMES formylglycinamide ribotide amidotransferase; phosphoribosylformylglycinamidine synthetase ORGANISM #formal_name Aquifex aeolicus DATE 30-Oct-1998 #sequence_revision 30-Oct-1998 #text_change 18-Jun-1999 ACCESSIONS A70458 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession A70458 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-745 ##label AQF !'##cross-references GB:AE000758; NID:g2984111; PIDN:AAC07653.1; !1PID:g2984116; GB:AE000657 !'##experimental_source strain VF5 GENETICS !$#gene purL FUNCTION !$#description catalyzes the condensation of !15'-phosphoribosylformylglycinamide with ATP, L-glutamine and !1water to form 5'-phosphoribosylformylglycinamidine, ADP, !1phosphate and L-glutamate !$#pathway purine nucleotide biosynthesis CLASSIFICATION #superfamily phosphoribosylformylglycinamidine synthase !1component II KEYWORDS ligase; purine nucleotide biosynthesis SUMMARY #length 745 #molecular-weight 83213 #checksum 6225 SEQUENCE /// ENTRY G64457 #type complete TITLE phosphoribosylformylglycinamidine synthase (EC 6.3.5.3) component II - Methanococcus jannaschii ALTERNATE_NAMES formylglycinamide ribotide amidotransferase; phosphoribosylformylglycinamidine synthetase ORGANISM #formal_name Methanococcus jannaschii DATE 30-Oct-1998 #sequence_revision 30-Oct-1998 #text_change 21-Jul-2000 ACCESSIONS G64457 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession G64457 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-733 ##label BUL !'##cross-references GB:U67567; GB:L77117; NID:g1591897; !1PIDN:AAB99270.1; PID:g1591899; TIGR:MJ1264 GENETICS !$#map_position REV1209847-1207646 FUNCTION !$#description catalyzes the condensation of !15'-phosphoribosylformylglycinamide with ATP, L-glutamine and !1water to form 5'-phosphoribosylformylglycinamidine, ADP, !1phosphate and L-glutamate !$#pathway purine nucleotide biosynthesis CLASSIFICATION #superfamily phosphoribosylformylglycinamidine synthase !1component II KEYWORDS ligase; purine nucleotide biosynthesis SUMMARY #length 733 #molecular-weight 80865 #checksum 7729 SEQUENCE /// ENTRY G69049 #type complete TITLE phosphoribosylformylglycinamidine synthase (EC 6.3.5.3) component II - Methanobacterium thermoautotrophicum (strain Delta H) ALTERNATE_NAMES formylglycinamide ribotide amidotransferase; phosphoribosylformylglycinamidine synthetase ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 30-Oct-1998 #sequence_revision 30-Oct-1998 #text_change 18-Jun-1999 ACCESSIONS G69049 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession G69049 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-714 ##label MTH !'##cross-references GB:AE000900; GB:AE000666; NID:g2622478; !1PIDN:AAB85851.1; PID:g2622483 !'##experimental_source strain Delta H GENETICS !$#gene MTH1374 FUNCTION !$#description catalyzes the condensation of !15'-phosphoribosylformylglycinamide with ATP, L-glutamine and !1water to form 5'-phosphoribosylformylglycinamidine, ADP, !1phosphate and L-glutamate !$#pathway purine nucleotide biosynthesis CLASSIFICATION #superfamily phosphoribosylformylglycinamidine synthase !1component II KEYWORDS ligase; purine nucleotide biosynthesis SUMMARY #length 714 #molecular-weight 76823 #checksum 5563 SEQUENCE /// ENTRY C69492 #type complete TITLE phosphoribosylformylglycinamidine synthase (EC 6.3.5.3) component II - Archaeoglobus fulgidus ALTERNATE_NAMES formylglycinamide ribotide amidotransferase; phosphoribosylformylglycinamidine synthetase ORGANISM #formal_name Archaeoglobus fulgidus DATE 30-Oct-1998 #sequence_revision 30-Oct-1998 #text_change 18-Jun-1999 ACCESSIONS C69492 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession C69492 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-765 ##label KLE !'##cross-references GB:AE000969; GB:AE000782; NID:g2689292; !1PIDN:AAB89311.1; PID:g2648599; TIGR:AF1940 FUNCTION !$#description catalyzes the condensation of !15'-phosphoribosylformylglycinamide with ATP, L-glutamine and !1water to form 5'-phosphoribosylformylglycinamidine, ADP, !1phosphate and L-glutamate !$#pathway purine nucleotide biosynthesis CLASSIFICATION #superfamily phosphoribosylformylglycinamidine synthase !1component II KEYWORDS ligase; purine nucleotide biosynthesis SUMMARY #length 765 #molecular-weight 84763 #checksum 227 SEQUENCE /// ENTRY SYECPG #type complete TITLE phosphoribosylformylglycinamidine synthase (EC 6.3.5.3) [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES formylglycinamide ribonucleotide synthetase; phosphoribosylformylglycinamidine synthetase ORGANISM #formal_name Escherichia coli DATE 30-Jun-1991 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS D65033; A31862; A34192 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65033 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1295 ##label BLAT !'##cross-references GB:AE000342; GB:U00096; NID:g1788907; !1PIDN:AAC75610.1; PID:g1788909; UWGP:b2557 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A31862 !$#authors Schendel, F.J.; Mueller, E.; Stubbe, J. !$#journal Biochemistry (1989) 28:2459-2471 !$#title Formylglycinamide ribonucleotide synthetase from Escherichia !1coli: cloning, sequencing, overproduction, isolation, and !1characterization. !$#cross-references MUID:89274173; PMID:2659070 !$#accession A31862 !'##molecule_type DNA !'##residues 1-846,'Y',848-1295 ##label SCH !'##cross-references EMBL:M19501; NID:g147422; PIDN:AAA24456.1; !1PID:g147423 REFERENCE A34192 !$#authors Sampei, G.; Mizobuchi, K. !$#journal J. Biol. Chem. (1989) 264:21230-21238 !$#title The organization of the purL gene encoding !15'-phosphoribosylformylglycinamide amidotransferase of !1Escherichia coli. !$#cross-references MUID:90078226; PMID:2531746 !$#contents annotation GENETICS !$#gene purL !$#map_position 55 min FUNCTION !$#description EC 6.3.5.3 [validated, MUID:89274173] CLASSIFICATION #superfamily phosphoribosylformylglycinamidine synthase KEYWORDS ligase; purine nucleotide biosynthesis FEATURE !$1-791 #domain domain I #label DOM1\ !$791-1040 #domain domain II, alpha/beta barrel-like #label !8DOM2\ !$1041-1295 #domain domain III, glutamine amidotransferase-like !8#label DOM3 SUMMARY #length 1295 #molecular-weight 141386 #checksum 9385 SEQUENCE /// ENTRY AJHUN1 #type complete TITLE aspartate-ammonia ligase (EC 6.3.1.1) - human ALTERNATE_NAMES asparagine synthetase (glutamine-hydrolyzing); cell division control protein ts11 CONTAINS aspartate-ammonia ligase (EC 6.3.1.1) ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 03-Jun-2002 ACCESSIONS A27062; I57649; A27443; A34479 REFERENCE A27062 !$#authors Andrulis, I.L.; Chen, J.; Ray, P.N. !$#journal Mol. Cell. Biol. (1987) 7:2435-2443 !$#title Isolation of human cDNAs for asparagine synthetase and !1expression in Jensen rat sarcoma cells. !$#cross-references MUID:87286877; PMID:2886907 !$#accession A27062 !'##molecule_type mRNA !'##residues 1-561 ##label AND !'##cross-references GB:M27396; GB:M16763; NID:g179099; PIDN:AAA51789.1; !1PID:g179100 REFERENCE A34479 !$#authors Van Heeke, G.; Schuster, S.M. !$#journal J. Biol. Chem. (1989) 264:19475-19477 !$#title The N-terminal cysteine of human asparagine synthetase is !1essential for glutamine-dependent activity. !$#cross-references MUID:90062038; PMID:2573597 !$#contents annotation; site-directed mutagenesis !$#note mutation of Cys-2 to Ala-2 abolished glutamine-dependent !1activity (EC 6.3.5.4) but not ammonia-dependent activity (EC !16.3.1.1) REFERENCE I57649 !$#authors Greco, A.; Gong, S.S.; Ittmann, M.; Basilico, C. !$#journal Mol. Cell. Biol. (1989) 9:2350-2359 !$#title Organization and expression of the cell cycle gene, ts11, !1that encodes asparagine synthetase. !$#cross-references MUID:89343953; PMID:2569668 !$#accession I57649 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-83 ##label GRE1 !'##cross-references GB:M27054; NID:g341608; PIDN:AAA63266.1; !1PID:g703119 !'##note identified by the authors as cell division control protein !1ts11, essential for progression through the cell cycle G1 !1phase in which the cell is committed to division REFERENCE A27443 !$#authors Greco, A.; Ittmann, M.; Basilico, C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:1565-1569 !$#title Molecular cloning of a gene that is necessary for G-1 !1progression in mammalian cells. !$#cross-references MUID:87175518; PMID:3470743 !$#accession A27443 !'##molecule_type mRNA !'##residues 22-332,'LMTLQQFVLRI',344-352,'GRTQIAWL',361-425,'S',427-561 !1##label GRE2 !'##cross-references GB:M15798; NID:g339986; PIDN:AAA36781.1; !1PID:g339987 GENETICS !$#gene GDB:ASNS; TS11 !'##cross-references GDB:119706; OMIM:108370 !$#map_position 7q21-7q31 FUNCTION !$#description catalyzes the formation of asparagine from aspartic acid and !1glutamine, coupled with the cleavage of ATP into AMP and !1pyrophosphate !$#note also capable of using ammonia as the nitrogen donor (EC !16.3.1.1) rather than glutamine CLASSIFICATION #superfamily asparagine synthase (glutamine-hydrolyzing) KEYWORDS asparagine biosynthesis; ligase FEATURE !$2-561 #product asparagine synthase (glutamine-hydrolyzing) !8#status predicted #label MAT\ !$2 #active_site Cys #status predicted SUMMARY #length 561 #molecular-weight 64429 #checksum 8855 SEQUENCE /// ENTRY S53447 #type complete TITLE aspartate-ammonia ligase (EC 6.3.1.1) [validated] - rat ALTERNATE_NAMES asparagine synthetase (glutamine-hydrolyzing) CONTAINS aspartate-ammonia ligase (EC 6.3.1.1) ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 18-Aug-2000 #sequence_revision 18-Aug-2000 #text_change 03-Jun-2002 ACCESSIONS S53447; S21704 REFERENCE S53447 !$#authors Hutson, R.G.; Kilberg, M.S. !$#journal Biochem. J. (1994) 304:745-750 !$#title Cloning of rat asparagine synthetase and specificity of the !1amino acid-dependent control of its mRNA content. !$#cross-references MUID:95118289; PMID:7818476 !$#accession S53447 !'##status preliminary !'##molecule_type mRNA !'##residues 1-561 ##label HUT !'##cross-references GB:U07201; NID:g460630; PIDN:AAA77671.1; !1PID:g460631 REFERENCE S21704 !$#authors Hongo, S.; Fujimori, M.; Shioda, S.; Nakai, Y.; Takeda, M.; !1Sato, T. !$#journal Arch. Biochem. Biophys. (1992) 295:120-125 !$#title Immunochemical characterization of rat testicular asparagine !1synthetase. !$#cross-references MUID:92246530; PMID:1349469 !$#accession S21704 !'##molecule_type protein !'##residues 2-9,'X',11-12 ##label HON FUNCTION !$#description catalyzes the formation of asparagine from aspartic acid and !1glutamine, coupled with the cleavage of ATP into AMP and !1pyrophosphate !$#note also capable of using ammonia as the nitrogen donor (EC !16.3.1.1) rather than glutamine CLASSIFICATION #superfamily asparagine synthase (glutamine-hydrolyzing) KEYWORDS asparagine biosynthesis; ligase FEATURE !$2-561 #product asparagine synthase (glutamine-hydrolyzing) !8#status experimental #label DUM\ !$2 #active_site Cys #status predicted SUMMARY #length 561 #molecular-weight 64282 #checksum 9381 SEQUENCE /// ENTRY AJHYNC #type complete TITLE asparagine synthase (glutamine-hydrolysing) (EC 6.3.5.4) [similarity] - Chinese hamster ALTERNATE_NAMES asparagine synthetase (glutamine-hydrolyzing) ORGANISM #formal_name Cricetulus griseus #common_name Chinese hamster DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 02-Aug-2002 ACCESSIONS JS0273 REFERENCE A91619 !$#authors Andrulis, I.L.; Shotwell, M.; Evans-Blackler, S.; Zalkin, !1H.; Siminovitch, L.; Ray, P.N. !$#journal Gene (1989) 80:75-85 !$#title Fine structure analysis of the Chinese hamster AS gene !1encoding asparagine synthetase. !$#cross-references MUID:90006788; PMID:2477309 !$#accession JS0273 !'##molecule_type mRNA !'##residues 1-561 ##label AND !'##cross-references GB:M27838; NID:g191063; PIDN:AAA36977.1; !1PID:g191064 !'##experimental_source ovary COMMENT This protein is one of a family of glutamine !1amidotransferases that have dual specificity to utilize !1either glutamine or ammonia as a substrate. Two functional !1domains have been identified: an aminator domain, which !1catalyzes the ammonia-dependent reaction, and a glutamine !1amide transfer domain, which binds glutamine and transfers !1the amide to the aminator domain. GENETICS !$#gene AS CLASSIFICATION #superfamily asparagine synthase (glutamine-hydrolyzing) KEYWORDS asparagine biosynthesis; ligase FEATURE !$2-561 #product asparagine synthase (glutamine-hydrolyzing) !8#status predicted #label MAT\ !$181-561 #domain aminator #label AMN\ !$2 #active_site Cys #status predicted SUMMARY #length 561 #molecular-weight 64326 #checksum 9138 SEQUENCE /// ENTRY AJHYNG #type complete TITLE asparagine synthase (glutamine-hydrolysing) (EC 6.3.5.4) [similarity] - golden hamster ALTERNATE_NAMES asparagine synthetase (glutamine-hydrolyzing) ORGANISM #formal_name Mesocricetus auratus #common_name golden hamster DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 02-Aug-2002 ACCESSIONS S12740 REFERENCE S12740 !$#authors Gong, S.S.; Basilico, C. !$#journal Nucleic Acids Res. (1990) 18:3509-3513 !$#title A mammalian temperature-sensitive mutation affecting G1 !1progression results from a single amino acid substitution in !1asparagine synthetase. !$#cross-references MUID:90301465; PMID:1972978 !$#accession S12740 !'##molecule_type DNA !'##residues 1-561 ##label GON !'##cross-references EMBL:X52130; NID:g49613; PIDN:CAA36375.1; !1PID:g49614 COMMENT This protein is one of a family of glutamine !1amidotransferases that have dual specificity to utilize !1either glutamine or ammonia as a substrate. Two functional !1domains have been identified: an aminator domain, which !1catalyzes the ammonia-dependent reaction, and a glutamine !1amide transfer domain, which binds glutamine and transfers !1the amide to the aminator domain. CLASSIFICATION #superfamily asparagine synthase (glutamine-hydrolyzing) KEYWORDS asparagine biosynthesis; ligase FEATURE !$2-561 #product asparagine synthase (glutamine-hydrolyzing) !8#status predicted #label MAT\ !$181-561 #domain aminator #label AMN\ !$2 #active_site Cys #status predicted SUMMARY #length 561 #molecular-weight 64273 #checksum 291 SEQUENCE /// ENTRY AJECN #type complete TITLE asparagine synthase (glutamine-hydrolysing) (EC 6.3.5.4) [similarity] - Escherichia coli (strain K-12) ALTERNATE_NAMES asparagine synthetase B ORGANISM #formal_name Escherichia coli DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 02-Aug-2002 ACCESSIONS A36616; A64802 REFERENCE A36616 !$#authors Scofield, M.A.; Lewis, W.S.; Schuster, S.M. !$#journal J. Biol. Chem. (1990) 265:12895-12902 !$#title Nucleotide sequence of Escherichia coli asnB and deduced !1amino acid sequence of asparagine synthetase B. !$#cross-references MUID:90330624; PMID:1973930 !$#accession A36616 !'##molecule_type DNA !'##residues 1-554 ##label SCO !'##cross-references GB:J05554; NID:g145392; PIDN:AAA23498.1; !1PID:g145393 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64802 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-554 ##label BLAT !'##cross-references GB:AE000171; GB:U00096; NID:g1786888; !1PIDN:AAC73768.1; PID:g1786889; UWGP:b0674 !'##experimental_source strain K-12, substrain MG1655 COMMENT This protein is one of a family of glutamine !1amidotransferases that have dual specificity to utilize !1either glutamine or ammonia as a substrate. Two functional !1domains have been identified: an aminator domain, which !1catalyzes the ammonia-dependent reaction, and a glutamine !1amide transfer domain, which binds glutamine and transfers !1the amide to the aminator domain. GENETICS !$#gene asnB CLASSIFICATION #superfamily asparagine synthase (glutamine-hydrolyzing) KEYWORDS asparagine biosynthesis; ligase FEATURE !$2-554 #product asparagine synthase (glutamine-hydrolyzing) !8#status predicted #label MAT\ !$176-554 #domain aminator #status predicted #label AMN\ !$2 #active_site Cys #status experimental SUMMARY #length 554 #molecular-weight 62658 #checksum 3652 SEQUENCE /// ENTRY AJPMN2 #type complete TITLE asparagine synthase (glutamine-hydrolysing) (EC 6.3.5.4) [similarity] - garden pea ALTERNATE_NAMES asparagine synthetase (glutamine-hydrolyzing) ORGANISM #formal_name Pisum sativum #common_name garden pea DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 02-Aug-2002 ACCESSIONS S11443 REFERENCE S11443 !$#authors Tsai, F.Y.; Coruzzi, G.M. !$#journal EMBO J. (1990) 9:323-332 !$#title Dark-induced and organ-specific expression of two asparagine !1synthetase genes in Pisum sativum. !$#cross-references MUID:90151604; PMID:1968003 !$#accession S11443 !'##molecule_type DNA !'##residues 1-583 ##label TSA !'##cross-references EMBL:X52180; NID:g20651; PIDN:CAA36430.1; !1PID:g20652 GENETICS !$#gene AS2 CLASSIFICATION #superfamily asparagine synthase (glutamine-hydrolyzing) KEYWORDS asparagine biosynthesis; ligase FEATURE !$2-583 #product asparagine synthase (glutamine-hydrolyzing) !8#status predicted #label MAT\ !$2 #active_site Cys #status predicted SUMMARY #length 583 #molecular-weight 65649 #checksum 2836 SEQUENCE /// ENTRY AJPMN1 #type complete TITLE asparagine synthase (glutamine-hydrolysing) (EC 6.3.5.4) [similarity] - garden pea ALTERNATE_NAMES asparagine synthetase (glutamine-hydrolyzing) ORGANISM #formal_name Pisum sativum #common_name garden pea DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 02-Aug-2002 ACCESSIONS S11444 REFERENCE S11443 !$#authors Tsai, F.Y.; Coruzzi, G.M. !$#journal EMBO J. (1990) 9:323-332 !$#title Dark-induced and organ-specific expression of two asparagine !1synthetase genes in Pisum sativum. !$#cross-references MUID:90151604; PMID:1968003 !$#accession S11444 !'##molecule_type DNA !'##residues 1-586 ##label TSA !'##cross-references EMBL:X52179; NID:g20649; PIDN:CAA36429.1; !1PID:g20650 COMMENT This protein is one of a family of glutamine !1amidotransferases that have dual specificity to utilize !1either glutamine or ammonia as a substrate. Two functional !1domains have been identified: an aminator domain, which !1catalyzes the ammonia-dependent reaction, and a glutamine !1amide transfer domain, which binds glutamine and transfers !1the amide to the aminator domain. GENETICS !$#gene AS1 CLASSIFICATION #superfamily asparagine synthase (glutamine-hydrolyzing) KEYWORDS asparagine biosynthesis; ligase FEATURE !$2-586 #product asparagine synthase (glutamine-hydrolyzing) !8#status predicted #label MAT\ !$175-586 #domain aminator #label AMN\ !$2 #active_site Cys #status predicted SUMMARY #length 586 #molecular-weight 66353 #checksum 3350 SEQUENCE /// ENTRY SYBYCP #type complete TITLE carbamoyl-phosphate synthase (glutamine-hydrolyzing) (EC 6.3.5.5) arginine-specific large chain - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES arginine-specific carbamoyl-phosphate synthetase ammonia chain; protein J2002; protein YJR109c ORGANISM #formal_name Saccharomyces cerevisiae DATE 13-Aug-1986 #sequence_revision 13-Aug-1986 #text_change 01-Sep-2000 ACCESSIONS A01199; A33478; S57130; S57132 REFERENCE A01199 !$#authors Lusty, C.J.; Widgren, E.E.; Broglie, K.E.; Nyunoya, H. !$#journal J. Biol. Chem. (1983) 258:14466-14477 !$#title Yeast carbamyl phosphate synthetase. Structure of the yeast !1gene and homology to Escherichia coli carbamyl phosphate !1synthetase. !$#cross-references MUID:84061899; PMID:6358221 !$#accession A01199 !'##molecule_type DNA !'##residues 1-1118 ##label LUS !'##cross-references GB:K01178; NID:g171309; PIDN:AAA66902.1; !1PID:g171310 REFERENCE A33478 !$#authors Kinney, D.M.; Lusty, C.J. !$#journal Mol. Cell. Biol. (1989) 9:4882-4888 !$#title Arginine restriction induced by delta-N- !1(Phosphonacetyl)-L-ornithine signals increased expression of !1HIS3, TRP5, CPA1, and CPA2 in Saccharomyces cerevisiae. !$#cross-references MUID:90097903; PMID:2689869 !$#accession A33478 !'##molecule_type DNA !'##residues 1-7 ##label KIN !'##cross-references GB:M30466 REFERENCE S57111 !$#authors Ramezani Rad, M.; Kirchrath, L.; Hollenberg, C.P. !$#submission submitted to the Protein Sequence Database, September 1995 !$#accession S57130 !'##molecule_type DNA !'##residues 1-1118 ##label RAM !'##cross-references EMBL:Z49609; NID:g1015821; PIDN:CAA89639.1; !1PID:g1015822; GSPDB:GN00010; MIPS:YJR109c REFERENCE S56848 !$#authors Rose, M.; Koetter, P.; Entian, K.D. !$#submission submitted to the Protein Sequence Database, September 1995 !$#accession S57132 !'##molecule_type DNA !'##residues 1-839 ##label ROS !'##cross-references EMBL:Z49609; GSPDB:GN00010; MIPS:YJR109c COMMENT This cytosolic enzyme catalyzes formation of carbamoyl !1phosphate to be used in the arginine biosynthetic pathway. !1It is composed of two chains; the small chain promotes the !1hydrolysis of glutamine to ammonia, which is used by the !1large chain to synthesize carbamoyl phosphate. GENETICS !$#gene SGD:CPA2; MIPS:YJR109c !'##cross-references SGD:S0003870; MIPS:YJR109c !$#map_position 10R CLASSIFICATION #superfamily carbamoyl-phosphate synthase !1(glutamine-hydrolyzing) large chain; biotin carboxylase !1homology; carbamoyl-phosphate synthase !1(glutamine-hydrolyzing) large chain homology KEYWORDS arginine biosynthesis; duplication; heterodimer; ligase; !1pyrimidine nucleotide biosynthesis FEATURE !$30-1083 #domain carbamoyl-phosphate synthase !8(glutamine-hydrolyzing) large chain homology #label !8CPL\ !$30-484 #domain biotin carboxylase homology #label BC1\ !$580-1032 #domain biotin carboxylase homology #label BC2 SUMMARY #length 1118 #molecular-weight 123914 #checksum 9818 SEQUENCE /// ENTRY SYECCP #type complete TITLE carbamoyl-phosphate synthase (glutamine-hydrolyzing) (EC 6.3.5.5) large chain [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES carbamoyl-phosphate synthetase (glutamine-hydrolyzing) ammonia chain ORGANISM #formal_name Escherichia coli DATE 19-Feb-1984 #sequence_revision 31-Dec-1991 #text_change 01-Mar-2002 ACCESSIONS A01198; S40556; A64724 REFERENCE A01198 !$#authors Nyunoya, H.; Lusty, C.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:4629-4633 !$#title The carB gene of Escherichia coli: a duplicated gene coding !1for the large subunit of carbamoyl-phosphate synthetase. !$#cross-references MUID:83273669; PMID:6308632 !$#accession A01198 !'##molecule_type DNA !'##residues 1-1073 ##label NYU !'##cross-references GB:J01597; NID:g145461; PIDN:AAA23539.1; !1PID:g145464 REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40556 !'##molecule_type DNA !'##residues 1-1073 ##label YUR !'##cross-references EMBL:D10483; NID:g216434; PIDN:BAA01311.1; !1PID:g216460 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64724 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1073 ##label BLAT !'##cross-references GB:AE000113; GB:U00096; NID:g2367095; !1PIDN:AAC73144.1; PID:g1786216; UWGP:b0033 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene carB !$#map_position 1 min COMPLEX heterodimer; large chain (PIR:SYECCP) and small chain !1(PIR:SYECCS) [validated, MUID:99190825] FUNCTION !$#description EC 6.3.5.5 [validated, MUID:83273669]; catalyzes formation !1of carbamoyl-phosphate using glutamine; the small chain !1promotes hydrolysis of glutamine to ammonia, which is used !1to synthesize carbamoyl-phosphate by the large chain !$#pathway glutamate metabolism; pyrimidine nucleotide biosynthesis CLASSIFICATION #superfamily carbamoyl-phosphate synthase !1(glutamine-hydrolyzing) large chain; biotin carboxylase !1homology; carbamoyl-phosphate synthase !1(glutamine-hydrolyzing) large chain homology KEYWORDS arginine biosynthesis; ATP; duplication; heterodimer; !1ligase; nucleotide binding; P-loop; pyrimidine nucleotide !1biosynthesis FEATURE !$2-1073 #product carbamoyl-phosphate synthase !8(glutamine-hydrolyzing) large chain #status predicted !8#label MAT\ !$9-1053 #domain carbamoyl-phosphate synthase !8(glutamine-hydrolyzing) large chain homology #label !8CPL\ !$9-471 #domain biotin carboxylase homology #label BC1\ !$561-992 #domain biotin carboxylase homology #label BC2\ !$866-873 #region nucleotide-binding motif A (P-loop) SUMMARY #length 1073 #molecular-weight 117841 #checksum 5486 SEQUENCE /// ENTRY I40169 #type complete TITLE carbamoyl-phosphate synthase (glutamine-hydrolyzing) (EC 6.3.5.5) - Bacillus caldolyticus ORGANISM #formal_name Bacillus caldolyticus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Sep-2000 ACCESSIONS I40169; S34321 REFERENCE I40166 !$#authors Ghim, S.Y.; Neuhard, J. !$#journal J. Bacteriol. (1994) 176:3698-3707 !$#title The pyrimidine biosynthesis operon of the thermophile !1Bacillus caldolyticus includes genes for uracil !1phosphoribosyltransferase and uracil permease. !$#cross-references MUID:94266723; PMID:8206848 !$#accession I40169 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-1065 ##label RES !'##cross-references EMBL:X73308; NID:g312439; PIDN:CAA51739.1; !1PID:g312443 GENETICS !$#gene pyrAb FUNCTION !$#pathway glutamate metabolism; pyrimidine nucleotide biosynthesis CLASSIFICATION #superfamily carbamoyl-phosphate synthase !1(glutamine-hydrolyzing) large chain; biotin carboxylase !1homology; carbamoyl-phosphate synthase !1(glutamine-hydrolyzing) large chain homology KEYWORDS ligase; pyrimidine nucleotide biosynthesis FEATURE !$9-1047 #domain carbamoyl-phosphate synthase !8(glutamine-hydrolyzing) large chain homology #label !8CPL\ !$9-467 #domain biotin carboxylase homology #label BC1\ !$553-985 #domain biotin carboxylase homology #label BC2 SUMMARY #length 1065 #molecular-weight 116482 #checksum 595 SEQUENCE /// ENTRY A29924 #type complete TITLE acetyl-CoA carboxylase (EC 6.4.1.2), hepatic - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Feb-2002 ACCESSIONS A29924; A29337; A27903 REFERENCE A29924 !$#authors Takai, T.; Yokoyama, C.; Wada, K.; Tanabe, T. !$#journal J. Biol. Chem. (1988) 263:2651-2657 !$#title Primary structure of chicken liver acetyl-CoA carboxylase !1deduced from cDNA sequence. !$#cross-references MUID:88139305; PMID:2893793 !$#accession A29924 !'##molecule_type mRNA !'##residues 1-2324 ##label TAK1 !'##cross-references GB:J03541; NID:g211567; PIDN:AAA48701.1; !1PID:g211568 REFERENCE A91375 !$#authors Takai, T.; Wada, K.; Tanabe, T. !$#journal FEBS Lett. (1987) 212:98-102 !$#title Primary structure of the biotin-binding site of chicken !1liver acetyl-CoA carboxylase. !$#cross-references MUID:87106011; PMID:2879745 !$#accession A29337 !'##molecule_type mRNA !'##residues 493-820 ##label TAK2 !'##cross-references GB:X05019; NID:g63021; PIDN:CAA28675.1; !1PID:g1334694 !$#accession A27903 !'##molecule_type mRNA !'##residues 493-552,554-783,'RSPS',789-820 ##label TAK3 CLASSIFICATION #superfamily human acetyl-CoA carboxylase; biotin !1carboxylase homology; lipoyl/biotin-binding homology KEYWORDS biotin binding; ligase; liver FEATURE !$120-620 #domain biotin carboxylase homology #label BCH\ !$747-819 #domain lipoyl/biotin-binding homology #label LPB\ !$786 #binding_site biotin (Lys) (covalent) #status !8predicted SUMMARY #length 2324 #molecular-weight 262718 #checksum 6146 SEQUENCE /// ENTRY A35578 #type complete TITLE acetyl-CoA carboxylase (EC 6.4.1.2) - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Feb-2002 ACCESSIONS A35578; A37119; I59145; I70069; I70070; I55305 REFERENCE A35578 !$#authors Lopez-Casillas, F.; Bai, D.H.; Luo, X.; Kong, I.S.; !1Hermodson, M.A.; Kim, K.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:5784-5788 !$#title Structure of the coding sequence and primary amino acid !1sequence of acetyl-coenzyme A carboxylase. !$#cross-references MUID:88320328; PMID:2901088 !$#accession A35578 !'##molecule_type mRNA !'##residues 1-2345 ##label LOP !'##cross-references GB:J03808; NID:g202644; PIDN:AAA40653.1; !1PID:g202645 REFERENCE A37119 !$#authors Kong, I.S.; Lopez-Casillas, F.; Kim, K.H. !$#journal J. Biol. Chem. (1990) 265:13695-13701 !$#title Acetyl-CoA carboxylase mRNA species with or without !1inhibitory coding sequence for Ser-1200 phosphorylation. !$#cross-references MUID:90337981; PMID:1974251 !$#accession A37119 !'##status preliminary !'##molecule_type mRNA !'##residues 1167-1200 ##label KON !'##cross-references GB:M55315 !'##experimental_source clone lambdaDHN121 REFERENCE I59145 !$#authors Luo, X. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:4042-4046 !$#title Structural features of the acetyl-CoA carboxylase gene: !1Mechanism for the generation of mRNAs with 5' end !1heterogeneity. !$#cross-references MUID:89264558; PMID:2566999 !$#accession I59145 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-74 ##label RES !'##cross-references GB:M26731; NID:g202641; PIDN:AAA40652.1; !1PID:g554406 !'##experimental_source hepatic REFERENCE I55305 !$#authors Lopez-Casillas, F.; Kim, K. !$#journal J. Biol. Chem. (1989) 264:7176-7184 !$#title Heterogeneity at the 5' end of rat acetyl-coenzyme A !1carboxylase mRNA: Lipogenic conditions enhance synthesis of !1a unique mRNA in liver. !$#cross-references MUID:89214151; PMID:2565337 !$#accession I70069 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-33 ##label RE2 !'##cross-references GB:M26196; NID:g202649; PIDN:AAA40655.1; !1PID:g554408 !$#accession I70070 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-33 ##label RE3 !'##cross-references GB:M26197; NID:g202651; PIDN:AAA40656.1; !1PID:g554409 !$#accession I55305 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-33 ##label RE4 !'##cross-references GB:M26195; NID:g202647; PIDN:AAA40654.1; !1PID:g554407 !'##experimental_source hepatic COMMENT This enzyme catalyzes the carboxylation of acetyl CoA to !1malonyl CoA and is the rate-limiting enzyme for long-chain !1fatty acid synthesis. CLASSIFICATION #superfamily human acetyl-CoA carboxylase; biotin !1carboxylase homology; lipoyl/biotin-binding homology KEYWORDS biotin binding; ligase FEATURE !$119-619 #domain biotin carboxylase homology #label BCH\ !$746-818 #domain lipoyl/biotin-binding homology #label LPB\ !$785 #binding_site biotin (Lys) (covalent) #status !8predicted SUMMARY #length 2345 #molecular-weight 265191 #checksum 6851 SEQUENCE /// ENTRY S60200 #type complete TITLE acetyl-CoA carboxylase (EC 6.4.1.2) - smut fungus (Ustilago maydis) ORGANISM #formal_name Ustilago maydis #common_name corn smut DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Feb-2002 ACCESSIONS S60200; S49991 REFERENCE S60200 !$#authors Bailey, A.; Keon, J.; Owen, J.; Hargreaves, J. !$#journal Mol. Gen. Genet. (1995) 249:191-201 !$#title The ACC1 gene, encoding acetyl-CoA carboxylase, is essential !1for growth in Ustilago maydis. !$#cross-references MUID:96086936; PMID:7500941 !$#accession S60200 !'##molecule_type DNA !'##residues 1-2185 ##label BAI !'##cross-references EMBL:Z46886; NID:g600097; PIDN:CAA86983.1; !1PID:g600098 GENETICS !$#gene ACC1 !$#introns 14/1 CLASSIFICATION #superfamily human acetyl-CoA carboxylase; biotin !1carboxylase homology; lipoyl/biotin-binding homology KEYWORDS biotin binding; ligase FEATURE !$41-548 #domain biotin carboxylase homology #label BCH\ !$675-747 #domain lipoyl/biotin-binding homology #label LPB\ !$714 #binding_site biotin (Lys) (covalent) #status !8predicted SUMMARY #length 2185 #molecular-weight 240029 #checksum 9283 SEQUENCE /// ENTRY A57710 #type complete TITLE acetyl-CoA carboxylase (EC 6.4.1.2) - wheat ORGANISM #formal_name Triticum aestivum #common_name common wheat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Sep-2000 ACCESSIONS A57710 REFERENCE A57710 !$#authors Gornicki, P.; Podkowinski, J.; Scappino, L.A.; DiMaio, J.; !1Ward, E.; Haselkorn, R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1994) 91:6860-6864 !$#title Wheat acetyl-Coenzyme A carboxylase: cDNA and protein !1structure. !$#cross-references MUID:94316597; PMID:7913745 !$#accession A57710 !'##status preliminary !'##molecule_type mRNA !'##residues 1-2257 ##label GOR !'##cross-references GB:U10187; NID:g514305; PIDN:AAA19970.1; !1PID:g514306 CLASSIFICATION #superfamily human acetyl-CoA carboxylase; biotin !1carboxylase homology; lipoyl/biotin-binding homology KEYWORDS ligase FEATURE !$29-534 #domain biotin carboxylase homology #label BCH\ !$661-733 #domain lipoyl/biotin-binding homology #label LPB\ !$700 #binding_site biotin (Lys) (covalent) #status !8predicted SUMMARY #length 2257 #molecular-weight 250953 #checksum 4993 SEQUENCE /// ENTRY A48757 #type complete TITLE acetyl-CoA carboxylase (EC 6.4.1.2) - Cyclotella cryptica ORGANISM #formal_name Cyclotella cryptica DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Feb-2002 ACCESSIONS A48757 REFERENCE A48757 !$#authors Roessler, P.G.; Ohlrogge, J.B. !$#journal J. Biol. Chem. (1993) 268:19254-19259 !$#title Cloning and characterization of the gene that encodes !1acetyl-coenzyme A carboxylase in the alga Cyclotella !1cryptica. !$#cross-references MUID:93374903; PMID:8103514 !$#accession A48757 !'##status preliminary; nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-2089 ##label ROE !'##cross-references GB:L20784; NID:g1065903; PIDN:AAA81471.1; !1PID:g409450 !'##note authors translated the codon GGC for residue 1834 as Ala GENETICS !$#introns 25/1; 729/1 CLASSIFICATION #superfamily human acetyl-CoA carboxylase; biotin !1carboxylase homology; lipoyl/biotin-binding homology KEYWORDS biotin binding; ligase FEATURE !$99-603 #domain biotin carboxylase homology #label BCH\ !$731-803 #domain lipoyl/biotin-binding homology #label LPB\ !$770 #binding_site biotin (Lys) (covalent) #status !8predicted SUMMARY #length 2089 #molecular-weight 229795 #checksum 4001 SEQUENCE /// ENTRY A27883 #type complete TITLE propionyl-CoA carboxylase (EC 6.4.1.3) alpha chain precursor [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 19-Nov-1988 #sequence_revision 03-Oct-1995 #text_change 01-Feb-2002 ACCESSIONS S04613; A27883; A45448; A24151 REFERENCE S04613 !$#authors Lamhonwah, A.M.; Mahuran, D.; Gravel, R.A. !$#journal Nucleic Acids Res. (1989) 17:4396 !$#title Human mitochondrial propionyl-CoA carboxylase: localization !1of the N-terminus of the pro- and mature alpha chains in the !1deduced primary sequence of a full-length cDNA. !$#cross-references MUID:89296507; PMID:2740237 !$#accession S04613 !'##molecule_type mRNA !'##residues 1-339,'HWPGPSPGKTVLQEHLSGTNKLIFAF',367-703 ##label LAM1 !'##cross-references EMBL:X14608; NID:g296365 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE A27883 !$#authors Lamhonwah, A.M.; Quan, F.; Gravel, R.A. !$#journal Arch. Biochem. Biophys. (1987) 254:631-636 !$#title Sequence homology around the biotin-binding site of human !1propionyl-CoA carboxylase and pyruvate carboxylase. !$#cross-references MUID:87212051; PMID:3555348 !$#accession A27883 !'##molecule_type mRNA !'##residues 608-703 ##label LAM2 !'##cross-references GB:X14608; NID:g296365 !'##note the complete translation is not shown REFERENCE A45448 !$#authors Stankovics, J.; Ledley, F.D. !$#journal Am. J. Hum. Genet. (1993) 52:144-151 !$#title Cloning of functional alpha propionyl CoA carboxylase and !1correction of enzyme deficiency in pccA fibroblasts. !$#cross-references MUID:93167265; PMID:8434582 !$#accession A45448 !'##molecule_type mRNA !'##residues 339-367 ##label STA !'##cross-references GB:S55656; NID:g265481; PIDN:AAB25345.1; !1PID:g265482 !'##experimental_source liver !'##note sequence extracted from NCBI backbone (NCBIN:124961, !1NCBIP:124962); corrects a region with frameshift errors from !1S04613 REFERENCE A94105 !$#authors Lamhonwah, A.M.; Barankiewicz, T.J.; Willard, H.F.; Mahuran, !1D.J.; Quan, F.; Gravel, R.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:4864-4868 !$#title Isolation of cDNA clones coding for the alpha and beta !1chains of human propionyl-CoA carboxylase: chromosomal !1assignments and DNA polymorphisms associated with PCCA and !1PCCB genes. !$#cross-references MUID:86259695; PMID:3460076 !$#accession A24151 !'##molecule_type mRNA !'##residues 'GPSPGKTVLQEHLSGTNKLIFAF',367-532,'H',534-536 ##label LAM3 !'##cross-references GB:M13572; NID:g189661; PIDN:AAA60035.1; !1PID:g189662 GENETICS !$#gene GDB:PCCA !'##cross-references GDB:119473; OMIM:232000 !$#map_position 13q32-13q32 CLASSIFICATION #superfamily propionyl-CoA carboxylase alpha chain; biotin !1carboxylase homology; lipoyl/biotin-binding homology KEYWORDS biotin binding; heterododecamer; ligase; mitochondrion FEATURE !$1-26 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$27-703 #product propionyl-CoA carboxylase alpha chain !8#status experimental #label MAT\ !$40-491 #domain biotin carboxylase homology #label BCH\ !$630-703 #domain lipoyl/biotin-binding homology #label LPB\ !$669 #binding_site biotin (Lys) (covalent) #status !8predicted SUMMARY #length 703 #molecular-weight 77353 #checksum 3412 SEQUENCE /// ENTRY S71008 #type complete TITLE propionyl-CoA carboxylase beta chain homolog - Saccharopolyspora erythraea ORGANISM #formal_name Saccharopolyspora erythraea DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S71008 REFERENCE S71005 !$#authors Donadio, S.; Staver, M.J.; Katz, L. !$#journal Mol. Microbiol. (1996) 19:977-984 !$#title Erythromycin production in Saccharopolyspora erythraea does !1not require a functional propionyl-CoA carboxylase. !$#cross-references MUID:96249691; PMID:8830278 !$#accession S71008 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-546 ##label DON !'##cross-references EMBL:X92557; NID:g1177651; PIDN:CAA63310.1; !1PID:g1177652 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1995 GENETICS !$#gene pccB CLASSIFICATION #superfamily propionyl-CoA carboxylase beta chain SUMMARY #length 546 #molecular-weight 58526 #checksum 7671 SEQUENCE /// ENTRY A48665 #type complete TITLE methylmalonyl-CoA carboxyltransferase (EC 2.1.3.1) 12S chain - Propionibacterium freudenreichii subsp. shermanii ORGANISM #formal_name Propionibacterium freudenreichii subsp. shermanii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A48665 REFERENCE A48665 !$#authors Thornton, C.G.; Kumar, G.K.; Haase, F.C.; Phillips, N.F.B.; !1Woo, S.B.; Park, V.M.; Magner, W.J.; Shenoy, B.C.; Wood, !1H.G.; Samols, D. !$#journal J. Bacteriol. (1993) 175:5301-5308 !$#title Primary structure of the monomer of the 12S subunit of !1transcarboxylase as deduced from DNA and characterization of !1the product expressed in Escherichia coli. !$#cross-references MUID:93374821; PMID:8366018 !$#accession A48665 !'##status preliminary !'##molecule_type DNA !'##residues 1-605 ##label THO !'##cross-references GB:L04196; NID:g150932; PIDN:AAA25676.1; !1PID:g150933 CLASSIFICATION #superfamily propionyl-CoA carboxylase beta chain KEYWORDS transferase SUMMARY #length 605 #molecular-weight 65699 #checksum 5947 SEQUENCE /// ENTRY B69893 #type complete TITLE propionyl-CoA carboxylase homolog yngE - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS B69893 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69893 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-595 ##label KUN !'##cross-references GB:Z99113; GB:AL009126; NID:g2634090; !1PIDN:CAB13704.1; PID:g2634204 !'##experimental_source strain 168 GENETICS !$#gene yngE CLASSIFICATION #superfamily propionyl-CoA carboxylase beta chain SUMMARY #length 595 #molecular-weight 66306 #checksum 6546 SEQUENCE /// ENTRY S28313 #type complete TITLE hypothetical protein F02A9.5 - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S28313 REFERENCE S28296 !$#authors Berks, M. !$#submission submitted to the EMBL Data Library, December 1992 !$#accession S28313 !'##molecule_type DNA !'##residues 1-608 ##label BER !'##cross-references EMBL:Z19555; NID:g6705; PID:g6711 GENETICS !$#introns 19/1; 55/2; 152/3; 352/1; 453/3; 505/2; 584/3 CLASSIFICATION #superfamily propionyl-CoA carboxylase beta chain SUMMARY #length 608 #molecular-weight 66523 #checksum 2475 SEQUENCE /// ENTRY QYBYP #type complete TITLE pyruvate carboxylase (EC 6.4.1.1) 1 [validated] - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein G3428; protein YGL062w; pyruvic carboxylase ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Dec-1991 #sequence_revision 19-Jul-1996 #text_change 01-Feb-2002 ACCESSIONS S64066; A29233; S05760; A29722 REFERENCE S64044 !$#authors Feuermann, M.; Potier, S.; Souciet, J.L. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64066 !'##molecule_type DNA !'##residues 1-1178 ##label FEU !'##cross-references EMBL:Z72584; NID:g1322565; PIDN:CAA96765.1; !1PID:g1322566; GSPDB:GN00007; MIPS:YGL062w !'##experimental_source strain S288C REFERENCE A92662 !$#authors Lim, F.; Morris, C.P.; Occhiodoro, F.; Wallace, J.C. !$#journal J. Biol. Chem. (1988) 263:11493-11497 !$#title Sequence and domain structure of yeast pyruvate carboxylase. !$#cross-references MUID:88298805; PMID:3042770 !$#accession A29233 !'##molecule_type DNA !'##residues 1-461,'G',463-492,'D',494-594,'A',596-618,'Q',620-663,'S', !1665-771,'R',773-878,'Q',880-908,'K',910-1178 ##label LIM !'##cross-references EMBL:J03889; NID:g172101; PIDN:AAA34843.1; !1PID:g172102 REFERENCE S05760 !$#authors Morris, C.P.; Lim, F.; Wallace, J.C. !$#journal Biochem. Biophys. Res. Commun. (1987) 145:390-396 !$#title Yeast pyruvate carboxylase: gene isolation. !$#cross-references MUID:87241529; PMID:3036126 !$#accession S05760 !'##molecule_type DNA !'##residues 1003-1178 ##label MOR !'##cross-references EMBL:J03889 !$#accession A29722 !'##molecule_type protein !'##residues 1124-1149 ##label MOR2 GENETICS !$#gene SGD:PYC1; PYV; MIPS:YGL062w !'##cross-references SGD:S0003030; MIPS:YGL062w !$#map_position 7L CLASSIFICATION #superfamily pyruvate carboxylase; biotin carboxylase !1homology; lipoyl/biotin-binding homology KEYWORDS biotin binding; gluconeogenesis; homotetramer; ligase; zinc FEATURE !$21-478 #domain biotin carboxylase homology #label BCH\ !$157-331 #domain ATP/bicarbonate binding #status predicted !8#label ATB1\ !$353-468 #domain ATP/bicarbonate binding #status predicted !8#label ATB2\ !$569-908 #domain pyruvate binding #status predicted #label !8PYR\ !$1096-1169 #domain lipoyl/biotin-binding homology #label LPB\ !$1135 #binding_site biotin (Lys) (covalent) #status !8experimental SUMMARY #length 1178 #molecular-weight 130098 #checksum 6277 SEQUENCE /// ENTRY A47255 #type complete TITLE pyruvate carboxylase (EC 6.4.1.1) precursor [similarity] - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Feb-2002 ACCESSIONS A47255 REFERENCE A47255 !$#authors Zhang, J.; Xia, W.L.; Brew, K.; Ahmad, F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:1766-1770 !$#title Adipose pyruvate carboxylase: amino acid sequence and domain !1structure deduced from cDNA sequencing. !$#cross-references MUID:93189578; PMID:8446588 !$#accession A47255 !'##status preliminary !'##molecule_type mRNA !'##residues 1-1178 ##label ZHA !'##cross-references GB:L09192; NID:g293743; PIDN:AAA39737.1; !1PID:g293744 !'##experimental_source 3T3-L1 adipocytes !'##note sequence extracted from NCBI backbone (NCBIN:126874, !1NCBIP:126875) CLASSIFICATION #superfamily pyruvate carboxylase; biotin carboxylase !1homology; lipoyl/biotin-binding homology KEYWORDS biotin binding; ligase; mitochondrion FEATURE !$1-20 #domain transit peptide (mitochondrion) #status !8predicted #label TRP\ !$21-1178 #product pyruvate carboxylase #status predicted !8#label MAT\ !$39-494 #domain biotin carboxylase homology #label BCH\ !$1105-1178 #domain lipoyl/biotin-binding homology #label LPB\ !$1144 #binding_site biotin (Lys) (covalent) #status !8predicted SUMMARY #length 1178 #molecular-weight 129684 #checksum 1003 SEQUENCE /// ENTRY JC2460 #type complete TITLE pyruvate carboxylase (EC 6.4.1.1) precursor - human ALTERNATE_NAMES pyruvate:carbon dioxide ligase (ADP-forming) ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 18-Aug-2000 #text_change 01-Feb-2002 ACCESSIONS G01933; JC2460; B27883; S01469 REFERENCE H00708 !$#authors Walker, M.E.; Jitrapakdee, S.; Val, D.L.; Wallace, J.C. !$#submission submitted to the EMBL Data Library, July 1995 !$#accession G01933 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-1178 ##label WAL !'##cross-references EMBL:U30891; NID:g1101028; PIDN:AAA82937.1; !1PID:g1101029 REFERENCE JC2460 !$#authors MacKay, N.; Rigat, B.; Douglas, C.; Chen, H.S.; Robinson, !1B.H. !$#journal Biochem. Biophys. Res. Commun. (1994) 202:1009-1014 !$#title cDNA cloning of human kidney pyruvate carboxylase. !$#cross-references MUID:94324922; PMID:8048912 !$#accession JC2460 !'##molecule_type mRNA !'##residues 1-224,'WP',227-351,'A',353-384,'PT',387-485,'DV',488-637, !1'R',639-728,'A',730-773,'AP',776-1178 ##label MAC !'##cross-references GB:S72370; NID:g632807; PIDN:AAB31500.1; !1PID:g632808 REFERENCE A27883 !$#authors Lamhonwah, A.M.; Quan, F.; Gravel, R.A. !$#journal Arch. Biochem. Biophys. (1987) 254:631-636 !$#title Sequence homology around the biotin-binding site of human !1propionyl-CoA carboxylase and pyruvate carboxylase. !$#cross-references MUID:87212051; PMID:3555348 !$#accession B27883 !'##molecule_type mRNA !'##residues 1083-1178 ##label LAM !'##cross-references GB:M26122; NID:g189657; PIDN:AAA36423.1; !1PID:g387003 REFERENCE S01469 !$#authors Freytag, S.O.; Collier, K.J. !$#journal J. Biol. Chem. (1984) 259:12831-12837 !$#title Molecular cloning of a cDNA for human pyruvate carboxylase. !1Structural relationship to other biotin-containing !1carboxylases and regulation of mRNA content in !1differentiating preadipocytes. !$#cross-references MUID:85030380; PMID:6548474 !$#accession S01469 !'##status preliminary !'##molecule_type mRNA !'##residues 1135-1178 ##label FRE !'##cross-references EMBL:K02282; NID:g189655; PIDN:AAA60033.1; !1PID:g189656 GENETICS !$#gene GDB:PC !'##cross-references GDB:119472; OMIM:266150 !$#map_position 11q11-11q13.1 CLASSIFICATION #superfamily pyruvate carboxylase; biotin carboxylase !1homology; lipoyl/biotin-binding homology KEYWORDS biotin binding; gluconeogenesis; ligase; mitochondrion FEATURE !$1-20 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$21-1178 #product pyruvate carboxylase #status predicted !8#label MAT\ !$39-494 #domain biotin carboxylase homology #label BCH\ !$1105-1178 #domain lipoyl/biotin-binding homology #label LPB\ !$1144 #binding_site biotin (Lys) (covalent) #status !8predicted SUMMARY #length 1178 #molecular-weight 129649 #checksum 760 SEQUENCE /// ENTRY JS0632 #type complete TITLE acetyl-CoA carboxylase (EC 6.4.1.2) biotin carboxylase chain [validated] - Escherichia coli (strain K-12) CONTAINS biotin carboxylase (EC 6.3.4.14) ORGANISM #formal_name Escherichia coli DATE 17-Jul-1992 #sequence_revision 26-May-1994 #text_change 01-Mar-2002 ACCESSIONS JS0632; PS0271; JS0687; PS0358; B33643; B65118 REFERENCE JS0632 !$#authors Kondo, H.; Shiratsuchi, K.; Yoshimoto, T.; Masuda, T.; !1Kitazono, A.; Tsuru, D.; Anai, M.; Sekiguchi, M.; Tanabe, T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:9730-9733 !$#title Acetyl-CoA carboxylase from Escherichia coli: gene !1organization and nucleotide sequence of the biotin !1carboxylase subunit. !$#cross-references MUID:92052166; PMID:1682920 !$#accession JS0632 !'##molecule_type DNA !'##residues 1-449 ##label KON !'##cross-references GB:M79446 !$#accession PS0271 !'##molecule_type protein !'##residues 1-20,'X', !122-39;59-88;126-144;151-159;191-222;263-282;354-363;388-399 !1##label KON1 REFERENCE JS0686 !$#authors Li, S.J.; Cronan Jr., J.E. !$#journal J. Biol. Chem. (1992) 267:855-863 !$#title The gene encoding the biotin carboxylase subunit of !1Escherichia coli acetyl-CoA carboxylase. !$#cross-references MUID:92112819; PMID:1370469 !$#accession JS0687 !'##molecule_type DNA !'##residues 1-259,'SR',262-449 ##label LIS !'##cross-references GB:M80458 !'##experimental_source strain K12 !$#accession PS0358 !'##molecule_type protein !'##residues 1-15,'X',17-18,'X',20,'X',22-31 ##label LIS1 REFERENCE A33643 !$#authors Alix, J.H. !$#journal DNA (1989) 8:779-789 !$#title A rapid procedure for cloning genes from lambda libraries by !1complementation of E. coli defective mutants: application to !1the fabE region of the E. coli chromosome. !$#cross-references MUID:90126231; PMID:2575489 !$#accession B33643 !'##status preliminary !'##molecule_type DNA !'##residues 1-135,'A',137-159,'P' ##label ALI !'##cross-references GB:M32214 !'##note the authors translated the codon GAA for residue 108 as Gln REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65118 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-449 ##label BLAT !'##cross-references GB:AE000404; GB:U00096; NID:g2367207; !1PIDN:AAC76288.1; PID:g1789654; UWGP:b3256 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene accC; fabG !$#map_position 72 min COMPLEX in E. coli, acetyl-CoA carboxylase is composed of biotin !1carboxylase (EC 6.3.4.14) (PIR:JS0362), carboxyltransferase !1(heterodimer of alpha (PIR:A43452) and beta (PIR:XMECBD) !1chains), and biotin carboxyl carrier protein (BCCP, !1homodimer) (PIR:BKEC9) FUNCTION ACC !$#description EC 6.4.1.2 [validated; MUID:75035569]; the acetyl-CoA !1carboxylase complex catalyzes the synthesis of malonyl-CoA !1from acetyl-CoA !$#pathway fatty acid biosynthesis FUNCTION BIC !$#description EC 6.3.4.14 [validated; MUID:20011362]; biotin carboxylase; !1catalyzes the carboxylation of biotin bound to biotin !1carboxyl carrier protein with bicarbonate CLASSIFICATION #superfamily biotin carboxylase; biotin carboxylase homology KEYWORDS ATP; biotin metabolism; fatty acid biosynthesis; ligase FEATURE !$4-449 #domain biotin carboxylase homology #label BCH SUMMARY #length 449 #molecular-weight 49320 #checksum 5648 SEQUENCE /// ENTRY F64105 #type complete TITLE biotin carboxylase (EC 6.3.4.14) - Haemophilus influenzae (strain Rd KW20) CONTAINS acetyl-CoA carboxylase (EC 6.4.1.2), biotin carboxylase chain ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS F64105 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession F64105 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-448 ##label TIGR !'##cross-references GB:U32778; GB:L42023; NID:g1573997; !1PIDN:AAC22632.1; PID:g1573999; TIGR:HI0972 CLASSIFICATION #superfamily biotin carboxylase; biotin carboxylase homology KEYWORDS ATP; fatty acid biosynthesis; ligase FEATURE !$4-448 #domain biotin carboxylase homology #label BCH SUMMARY #length 448 #molecular-weight 49108 #checksum 1153 SEQUENCE /// ENTRY B49342 #type complete TITLE acetyl-CoA carboxylase (EC 6.4.1.2), biotin carboxylase - Pseudomonas aeruginosa ALTERNATE_NAMES biotin carboxylase (EC 6.3.4.14) ORGANISM #formal_name Pseudomonas aeruginosa DATE 07-Apr-1994 #sequence_revision 26-May-1994 #text_change 31-Dec-2000 ACCESSIONS B49342; H83039 REFERENCE A49342 !$#authors Best, E.A.; Knauf, V.C. !$#journal J. Bacteriol. (1993) 175:6881-6889 !$#title Organization and nucleotide sequences of the genes encoding !1the biotin carboxyl carrier protein and biotin carboxylase !1protein of Pseudomonas aeruginosa acetyl coenzyme A !1carboxylase. !$#cross-references MUID:94042851; PMID:7693652 !$#accession B49342 !'##molecule_type DNA !'##residues 1-449 ##label BES !'##cross-references GB:L14612; NID:g405539; PIDN:AAA16041.1; !1PID:g405541 REFERENCE A82950 !$#authors Stover, C.K.; Pham, X.Q.; Erwin, A.L.; Mizoguchi, S.D.; !1Warrener, P.; Hickey, M.J.; Brinkman, F.S.L.; Hufnagle, !1W.O.; Kowalik, D.J.; Lagrou, M.; Garber, R.L.; Goltry, L.; !1Tolentino, E.; Westbrook-Wadman, S.; Yuan, Y.; Brody, L.L.; !1Coulter, S.N.; Folger, K.R.; Kas, A.; Larbig, K.; Lim, R.M.; !1Smith, K.A.; Spencer, D.H.; Wong, G.K.S.; Wu, Z.; Paulsen, !1I.T.; Reizer, J.; Saier, M.H.; Hancock, R.E.W.; Lory, S.; !1Olson, M.V. !$#journal Nature (2000) 406:959-964 !$#title Complete genome sequence of Pseudomonas aeruginosa PA01, an !1opportunistic pathogen. !$#cross-references MUID:20437337; PMID:10984043 !$#accession H83039 !'##status preliminary !'##molecule_type DNA !'##residues 1-449 ##label STO !'##cross-references GB:AE004898; GB:AE004091; NID:g9951115; !1PIDN:AAG08233.1; GSPDB:GN00131; PASP:PA4848 !'##experimental_source strain PAO1 GENETICS !$#gene accC; fabG; PA4848 COMPLEX in P. aeruginosa, acetyl-CoA carboxylase is composed of !1biotin carboxylase (EC 6.3.4.14), carboxyltransferase !1(heterodimer of alpha and beta chains), and biotin carboxyl !1carrier protein (BCCP, homodimer) FUNCTION !$#description the enzyme complex catalyzes the synthesis of malonyl-CoA; !1the overall reaction consists two distinct half-reactions: !1biotin carboxylase catalyzes the carboxylation of biotin !1bound to BCCP with bicarbonate; carboxyltransferase !1catalyzes the transfer of the carboxyl group from the !1carboxyl-biotin to acetyl-CoA to form malonyl-CoA !$#pathway fatty acid biosynthesis CLASSIFICATION #superfamily biotin carboxylase; biotin carboxylase homology KEYWORDS ATP; fatty acid biosynthesis; ligase FEATURE !$4-449 #domain biotin carboxylase homology #label BCH SUMMARY #length 449 #molecular-weight 48888 #checksum 5487 SEQUENCE /// ENTRY A43452 #type complete TITLE acetyl-CoA carboxylase (EC 6.4.1.2) carboxyltransferase alpha chain [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 04-Mar-1993 #sequence_revision 08-Feb-1996 #text_change 01-Mar-2002 ACCESSIONS A43452; D28390; A64743 REFERENCE A43452 !$#authors Li, S.J.; Cronan Jr., J.E. !$#journal J. Biol. Chem. (1992) 267:16841-16847 !$#title The genes encoding the two carboxyltransferase subunits of !1Escherichia coli acetyl-CoA carboxylase. !$#cross-references MUID:92380982; PMID:1355089 !$#accession A43452 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA; protein !'##residues 1-319 ##label LI1 !'##cross-references GB:M96394; NID:g147321; PIDN:AAA70370.1; !1PID:g147322 !'##note sequence extracted from NCBI backbone (NCBIP:111872) REFERENCE A91855 !$#authors Tomasiewicz, H.G.; McHenry, C.S. !$#journal J. Bacteriol. (1987) 169:5735-5744 !$#title Sequence analysis of the Escherichia coli dnaE gene. !$#cross-references MUID:88058791; PMID:3316192 !$#accession D28390 !'##molecule_type DNA !'##residues 1-20 ##label TOM !'##cross-references GB:M19334; GB:M18265; GB:M18266; NID:g450760 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64743 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-319 ##label BLAT !'##cross-references GB:AE000127; GB:U00096; NID:g1786370; !1PIDN:AAC73296.1; PID:g1786382; UWGP:b0185 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene accA !$#map_position 4.3 min COMPLEX in E. coli, acetyl-CoA carboxylase is composed of biotin !1carboxylase (EC 6.3.4.14) (PIR:JS0362), carboxyltransferase !1(heterodimer of alpha (PIR:A43452) and beta (PIR:XMECBD) !1chains), and biotin carboxyl carrier protein (BCCP, !1homodimer) (PIR:BKEC9) FUNCTION ACC !$#description EC 6.4.1.2 [validated, MUID:75035569]; the acetyl-CoA !1carboxylase complex catalyzes the synthesis of malonyl-CoA !1from acetyl-CoA !$#pathway fatty acid biosynthesis FUNCTION CTRA !$#description catalyzes the transfer of the carboxyl group from the !1carboxyl-biotin to acetyl-CoA to form malonyl-CoA !1[validated, MUID:20011362] CLASSIFICATION #superfamily acetyl-CoA carboxylase, carboxyltransferase !1alpha chain KEYWORDS fatty acid biosynthesis; ligase FEATURE !$84-119 #region acyl-CoA binding #status predicted SUMMARY #length 319 #molecular-weight 35241 #checksum 7843 SEQUENCE /// ENTRY XMECBD #type complete TITLE acetyl-CoA carboxylase (EC 6.4.1.2), carboxyltransferase beta chain [validated] - Escherichia coli (strain K-12) CONTAINS carboxyltransferase beta chain ORGANISM #formal_name Escherichia coli DATE 31-Dec-1988 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS B65004; C29803; B29805; E40637; I41212 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65004 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-304 ##label BLAT !'##cross-references GB:AE000320; GB:U00096; NID:g1788647; !1PIDN:AAC75376.1; PID:g1788655; UWGP:b2316 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A29803 !$#authors Nonet, M.L.; Marvel, C.C.; Tolan, D.R. !$#journal J. Biol. Chem. (1987) 262:12209-12217 !$#title The hisT-purF region of the Escherichia coli K-12 !1chromosome. Identification of additional genes of the hisT !1and purF operons. !$#cross-references MUID:87308226; PMID:3040734 !$#accession C29803 !'##molecule_type DNA !'##residues 1-75,'SV',78-225,'ALPVRVLSNR',236-304 ##label NON !'##cross-references GB:M68934; GB:J02800; NID:g146359; PIDN:AAA23965.1; !1PID:g146364 !'##experimental_source strain K12 REFERENCE A29805 !$#authors Bognar, A.L.; Osborne, C.; Shane, B. !$#journal J. Biol. Chem. (1987) 262:12337-12343 !$#title Primary structure of the Escherichia coli folC gene and its !1folylpolyglutamate synthetase-dihydrofolate synthetase !1product and regulation of expression by an upstream gene. !$#cross-references MUID:87308246; PMID:3040739 !$#accession B29805 !'##molecule_type DNA !'##residues 1-224,'MALPVRVLSNRPFAK',240-304 ##label BOG !'##cross-references GB:M32445; NID:g146018; PIDN:AAA23807.1; !1PID:g146019 REFERENCE A40637 !$#authors Li, S.J.; Cronan Jr., J.E. !$#journal J. Bacteriol. (1993) 175:332-340 !$#title Growth rate regulation of Escherichia coli acetyl coenzyme A !1carboxylase, which catalyzes the first committed step of !1lipid biosynthesis. !$#cross-references MUID:93123150; PMID:7678242 !$#accession E40637 !'##status preliminary !'##molecule_type DNA !'##residues 1-32 ##label LI1 !'##cross-references GB:S53037; NID:g263402; PIDN:AAB24894.1; !1PID:g263404 !'##note sequence extracted from NCBI backbone (NCBIN:122320, !1NCBIP:122322) REFERENCE I41212 !$#authors Bogner, A.L.; Osborne, C.; Shane, B. !$#journal J. Biol. Chem. (1987) 262:12334-12343 !$#title Primary structure of the Escherichia coli folC gene and its !1folylpolyglutamate synthetase-dihydrofolate synthetase !1product and regulation of expression by an upstream gene. !$#accession I41212 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-224,'MALPVRVLSNRPFAK',240-304 ##label RES !'##cross-references GB:J02808; NID:g146007; PIDN:AAA23801.1; !1PID:g146008 GENETICS !$#gene accD; dedB; usg !$#map_position 50 min COMPLEX in E. coli, acetyl-CoA carboxylase is composed of biotin !1carboxylase (EC 6.3.4.14) (PIR:JS0362), carboxyltransferase !1(heterodimer of alpha (PIR:A43452) and beta (PIR:XMECBD) !1chains), and biotin carboxyl carrier protein (BCCP, !1homodimer) (PIR:BKEC9) FUNCTION ACC !$#description EC 6.4.1.2 [validated, MUID:75035569]; the acetyl-CoA !1carboxylase complex catalyzes the synthesis of malonyl-CoA !1from acetyl-CoA !$#pathway fatty acid biosynthesis FUNCTION CTRB !$#description catalyzes the transfer of the carboxyl group from the !1carboxyl-biotin to acetyl-CoA to form malonyl-CoA !1[validated, MUID:20011362] CLASSIFICATION #superfamily acetyl-CoA carboxylase, carboxyltransferase !1beta chain KEYWORDS fatty acid biosynthesis; ligase; zinc finger FEATURE !$27-49 #region zinc finger CCCC motif SUMMARY #length 304 #molecular-weight 33322 #checksum 4584 SEQUENCE /// ENTRY B64113 #type complete TITLE acetyl-CoA carboxylase (EC 6.4.1.2) carboxyltransferase beta chain - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 18-Aug-1995 #sequence_revision 23-Feb-1996 #text_change 18-Jun-1999 ACCESSIONS B64113 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession B64113 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-296 ##label TIGR !'##cross-references GB:U32806; GB:L42023; NID:g1574717; !1PIDN:AAC22913.1; PID:g1574718; TIGR:HI1260 !'##note named as homolog to a protein from Escherichia coli FUNCTION !$#description the enzyme complex catalyzes the synthesis of malonyl-CoA; !1the overall reaction consists two distinct half-reactions: !1biotin carboxylase (see JS0632) catalyzes the carboxylation !1of biotin bound to BCCP (see BKEC9) with bicarbonate; !1carboxyltransferase catalyzes the transfer of the carboxyl !1group from the carboxyl-biotin to acetyl-CoA to form !1malonyl-CoA !$#pathway fatty acid biosynthesis !$#note first committed step CLASSIFICATION #superfamily acetyl-CoA carboxylase, carboxyltransferase !1beta chain KEYWORDS fatty acid biosynthesis; ligase; zinc finger FEATURE !$29-51 #region zinc finger CCCC motif SUMMARY #length 296 #molecular-weight 32635 #checksum 8644 SEQUENCE /// ENTRY JQ1238 #type complete TITLE zinc finger protein - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 30-Jun-1992 #sequence_revision 23-Feb-1996 #text_change 16-Jun-2000 ACCESSIONS JQ1238; S76114 REFERENCE JQ1233 !$#authors Ogura, Y.; Yoshida, T.; Nakamura, Y.; Takemura, M.; Oda, K.; !1Ohyama, K. !$#journal Agric. Biol. Chem. (1991) 55:2259-2264 !$#title Gene encoding a putative zinc finger protein in !1Synechocystis PCC6803. !$#cross-references MUID:92118327; PMID:1368738 !$#accession JQ1238 !'##molecule_type DNA !'##residues 1-326 ##label OGU !'##cross-references GB:S77740; NID:g243471; PIDN:AAC60398.1; !1PID:g243477; GB:D10004; NID:g217103; PID:g217109 !'##experimental_source strain PCC 6803 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76114 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-326 ##label KAN !'##cross-references EMBL:D63999; GB:AB001339; NID:g1001396; !1PIDN:BAA10092.1; PID:g1001466 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily acetyl-CoA carboxylase, carboxyltransferase !1beta chain KEYWORDS zinc finger FEATURE !$36-58 #region zinc finger CCCC motif SUMMARY #length 326 #molecular-weight 36396 #checksum 7129 SEQUENCE /// ENTRY BWFNZT #type complete TITLE zinc finger protein zfpA - turnip fern chloroplast ORGANISM #formal_name chloroplast Angiopteris lygodiifolia #common_name turnip fern DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 18-Jun-1999 ACCESSIONS S19230 REFERENCE S19228 !$#authors Yoshinaga, K.; Kubota, Y.; Ishii, T.; Wada, K. !$#journal Plant Mol. Biol. (1992) 18:79-82 !$#title Nucleotide sequence of atpB, rbcL, trnR, dedB and psaI !1chloroplast genes from a fern Angiopteris lygodiifolia: a !1possible emergence of Spermatophyta lineage before the !1separation of Bryophyta and Pteridophyta. !$#cross-references MUID:92119238; PMID:1731980 !$#accession S19230 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-314 ##label YOS !'##cross-references EMBL:X58429; NID:g11189; PIDN:CAA41333.1; !1PID:g11192 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1March 1991 GENETICS !$#gene zfpA; dedB !$#genome chloroplast CLASSIFICATION #superfamily acetyl-CoA carboxylase, carboxyltransferase !1beta chain KEYWORDS chloroplast; zinc finger FEATURE !$51-73 #region zinc finger CCCC motif SUMMARY #length 314 #molecular-weight 35098 #checksum 2941 SEQUENCE /// ENTRY LQBYPX #type complete TITLE DNA ligase (ATP) (EC 6.5.1.1) [validated] - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES cell division control protein CDC9; DNA ligase I; polydeoxyribonucleotide synthase (ATP); protein D1497; protein YDL164c CONTAINS DNA ligase (ATP) (EC 6.5.1.1) precursor, mitochondrial; DNA ligase (ATP) (EC 6.5.1.1), nuclear ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1991 #sequence_revision 12-Apr-1996 #text_change 19-Jan-2001 ACCESSIONS S61049; S05830; S67716; S31138; S74315 REFERENCE S61010 !$#authors Pohl, T.M. !$#submission submitted to the EMBL Data Library, November 1995 !$#accession S61049 !'##molecule_type DNA !'##residues 1-755 ##label POH !'##cross-references EMBL:Z67750; NID:g1061256; PIDN:CAA91582.1; !1PID:g1061275 REFERENCE S05830 !$#authors Barker, D.G.; White, J.H.M.; Johnston, L.H. !$#journal Nucleic Acids Res. (1985) 13:8323-8337 !$#title The nucleotide sequence of the DNA ligase gene (CDC9) from !1Saccharomyces cerevisiae: a gene which is cell-cycle !1regulated and induced in response to DNA damage. !$#cross-references MUID:86093646; PMID:3909103 !$#accession S05830 !'##molecule_type DNA !'##residues 1-68,'E',70-185,'V',187-755 ##label BAR !'##cross-references EMBL:X03246; NID:g3514; PIDN:CAA27005.1; PID:g3515 REFERENCE S67708 !$#authors Pohl, T.M. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67716 !'##molecule_type DNA !'##residues 1-755 ##label POW !'##cross-references EMBL:Z74212; EMBL:Z71256; NID:g1431258; !1PIDN:CAA98737.1; PID:g1431259; GSPDB:GN00004; MIPS:YDL164c !'##experimental_source strain S288C REFERENCE S31138 !$#authors Wehner, E.P.; Rao, E.; Brendel, M. !$#journal Mol. Gen. Genet. (1993) 237:351-358 !$#title Molecular structure and genetic regulation of SFA, a gene !1responsible for resistance to formaldehyde in Saccharomyces !1cerevisiae, and characterization of its protein product. !$#cross-references MUID:93247548; PMID:8483449 !$#accession S31138 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 'AGTCPTS',507,'MIKKTVISAATIVMPRAHRKELTG',533, !1'KALKGIGRRSPLCDSC',550,'RKQPSSR',558,'RPLSTAAARNGA',570, !1'KEMAPNSPPATAC',584,'HTHAET',591, !1'AHEPEVASPIFPIGDVGDIGATNRTCGAGDAGHDASGVE',610-755 ##label !1WEH !'##cross-references EMBL:X68020 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1992 !'##note this sequence has been revised in reference S74315 REFERENCE S74315 !$#authors Wehner, E. !$#submission submitted to the EMBL Data Library, November 1994 !$#accession S74315 !'##molecule_type DNA !'##residues 610-670,'E',672-723,'I',725-755 ##label WEW !'##cross-references EMBL:X68020; NID:g577609; PIDN:CAA48158.1; !1PID:g600039 GENETICS !$#gene SGD:CDC9; MIPS:YDL164c !'##cross-references SGD:S0002323; MIPS:YDL164c !$#map_position 4L FUNCTION MIT !$#description EC 6.5.1.1 [validated, MUID:20003237]; DNA ligase (ATP); !1required for propagation and maintenance of mitochondrial !1DNA FUNCTION NUC !$#description EC 6.5.1.1 [validated, MUID:20003237]; DNA ligase (ATP); !1involved in nuclear DNA replication; required for ligation !1of Okazaki fragments CLASSIFICATION #superfamily yeast polydeoxyribonucleotide synthase (ATP) KEYWORDS alternative initiators; DNA repair; ligase; mitochondrion; !1nucleus; phosphoprotein FEATURE !$1-44 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$24-755 #product DNA ligase (ATP), nuclear #status predicted !8#label MAT2\ !$45-755 #product DNA ligase (ATP), mitochondrial #status !8predicted #label MAT1\ !$419 #active_site Lys (covalent AMP-binding) #status !8predicted\ !$576 #binding_site ATP (Lys) #status predicted SUMMARY #length 755 #molecular-weight 84827 #checksum 7303 SEQUENCE /// ENTRY LQBP37 #type complete TITLE DNA ligase (ATP) (EC 6.5.1.1) - phage T7 ALTERNATE_NAMES polydeoxyribonucleotide synthase (ATP) ORGANISM #formal_name phage T7 DATE 01-Sep-1981 #sequence_revision 01-Sep-1981 #text_change 18-Jun-1999 ACCESSIONS E94615; F92866; S42292; A01200 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession E94615 !'##molecule_type DNA !'##residues 1-359 ##label DU1 REFERENCE A92866 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1981) 148:303-330 !$#title Nucleotide sequence from the genetic left end of !1bacteriophage T7 DNA to the beginning of gene 4. !$#cross-references MUID:82078034; PMID:7310871 !$#accession F92866 !'##molecule_type DNA !'##residues 1-359 ##label DU2 !'##cross-references GB:V01127; NID:g15498; PIDN:CAA24336.1; PID:g15508 REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42292 !'##molecule_type DNA !'##residues 1-359 ##label DUN !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24393.1; !1PID:g15572 COMMENT Polydeoxyribonucleotide synthase (ATP), which is expressed !1in the early stage of lytic development, has been implicated !1in T7 DNA synthesis and genetic recombination. It may also !1play a role in T7 DNA repair. GENETICS !$#gene 1.3 !$#map_position 16.19-18.88 CLASSIFICATION #superfamily phage T7 polydeoxyribonucleotide synthase (ATP) KEYWORDS ligase; phosphoprotein FEATURE !$34 #active_site Lys (covalent AMP-binding) #status !8predicted SUMMARY #length 359 #molecular-weight 41133 #checksum 6982 SEQUENCE /// ENTRY LQBP34 #type complete TITLE DNA ligase (ATP) (EC 6.5.1.1) - phage T4 ALTERNATE_NAMES polydeoxyribonucleotide synthase (ATP) ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 18-Jun-1999 ACCESSIONS A01201 REFERENCE A01201 !$#authors Armstrong, J.; Brown, R.S.; Tsugita, A. !$#journal Nucleic Acids Res. (1983) 11:7145-7156 !$#title Primary structure and genetic organization of phage T4 DNA !1ligase. !$#cross-references MUID:84041510; PMID:6314278 !$#accession A01201 !'##molecule_type DNA !'##residues 1-487 ##label ARM !'##cross-references GB:X00039; GB:M32518; NID:g15338; PIDN:CAA24921.1; !1PID:g15340 COMMENT Polydeoxyribonucleotide synthase (ATP), which is expressed !1in the early stage of lytic development, has been implicated !1in T4 DNA synthesis and genetic recombination. It may also !1play a role in T4 DNA repair. GENETICS !$#gene 30 CLASSIFICATION #superfamily phage T4 polydeoxyribonucleotide synthase (ATP) KEYWORDS DNA recombination; DNA repair; DNA replication; ligase; !1phosphoprotein FEATURE !$159 #active_site Lys (covalent AMP-binding) #status !8predicted SUMMARY #length 487 #molecular-weight 55292 #checksum 165 SEQUENCE /// ENTRY WMVZ7W #type complete TITLE DNA ligase (ATP) (EC 6.5.1.1) - vaccinia virus (strain Copenhagen) ALTERNATE_NAMES A50R protein; polydeoxyribonucleotide synthase (ATP) ORGANISM #formal_name vaccinia virus #note host Homo sapiens (man) DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 18-Jun-1999 ACCESSIONS G42522 REFERENCE A42501 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:517-563 !$#title Appendix to "The complete DNA sequence of vaccinia virus". !$#accession G42522 !'##molecule_type DNA !'##residues 1-552 ##label GOE !'##cross-references GB:M35027; NID:g335317; PIDN:AAA48182.1; !1PID:g335530 !'##experimental_source strain Copenhagen REFERENCE A42531 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:247-266 !$#title The complete DNA sequence of vaccinia virus. !$#cross-references MUID:91021027; PMID:2219722 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given CLASSIFICATION #superfamily vaccinia virus DNA ligase KEYWORDS ATP; DNA recombination; DNA repair; ligase; phosphoprotein FEATURE !$231 #active_site Lys (covalent AMP-binding) #status !8predicted\ !$382 #binding_site ATP (Lys) #status predicted SUMMARY #length 552 #molecular-weight 63389 #checksum 525 SEQUENCE /// ENTRY JQ1788 #type complete TITLE DNA ligase (ATP) (EC 6.5.1.1) - vaccinia virus (strain WR) ALTERNATE_NAMES polydeoxyribonucleotide synthase (ATP); SalF13R protein ORGANISM #formal_name vaccinia virus #note host Homo sapiens (man) DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jun-2000 ACCESSIONS JQ1788; S07629 REFERENCE JQ1767 !$#authors Smith, G.L.; Chan, Y.S.; Howard, S.T. !$#journal J. Gen. Virol. (1991) 72:1349-1376 !$#title Nucleotide sequence of 42kbp of vaccinia virus strain WR !1from near the right inverted terminal repeat. !$#cross-references MUID:91259063; PMID:2045793 !$#accession JQ1788 !'##molecule_type DNA !'##residues 1-552 ##label SMI !'##cross-references DDBJ:D11079; NID:g222717; PIDN:BAA01824.1; !1PID:g222739 REFERENCE S07629 !$#authors Smith, G.L.; Chan, Y.S.; Kerr, S.M. !$#journal Nucleic Acids Res. (1989) 17:9051-9062 !$#title Transcriptional mapping and nucleotide sequence of a !1vaccinia virus gene encoding a polypeptide with extensive !1homology to DNA ligases. !$#cross-references MUID:90067909; PMID:2555782 !$#accession S07629 !'##molecule_type DNA !'##residues 1-552 ##label SM2 !'##cross-references EMBL:X16512; NID:g62229; PIDN:CAA34519.1; !1PID:g62230 CLASSIFICATION #superfamily vaccinia virus DNA ligase KEYWORDS ATP; DNA recombination; DNA repair; ligase; phosphoprotein FEATURE !$231 #active_site Lys (covalent AMP-binding) #status !8predicted\ !$382 #binding_site ATP (Lys) #status predicted SUMMARY #length 552 #molecular-weight 63359 #checksum 388 SEQUENCE /// ENTRY JQ1857 #type complete TITLE DNA ligase (ATP) (EC 6.5.1.1) - variola major virus (strains India-1967 and Harvey) ALTERNATE_NAMES 26R protein; J4R protein ORGANISM #formal_name variola major virus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 24-May-2001 ACCESSIONS C36854; S46844; JQ1857 REFERENCE A36859 !$#authors Blinov, V.M. !$#submission submitted to GenBank, November 1992 !$#accession C36854 !'##molecule_type DNA !'##residues 1-552 ##label BLI !'##cross-references GB:X69198; NID:g456758; PIDN:CAA49103.1; !1PID:g457053 !'##experimental_source strain India-1967, ssp. major, isolate Ind3 REFERENCE S46842 !$#authors Kolykhalov, A.A.; Blinov, V.M.; Frolov, I.V.; Totmenin, !1A.V.; Shchelkunov, S.N.; Sandakhchiev, L.S. !$#submission submitted to the EMBL Data Library, April 1992 !$#description Nucleotide sequence analysis of the region of variola virus !1HindIII-J genome fragment. !$#accession S46844 !'##molecule_type DNA !'##residues 1-552 ##label KOL !'##cross-references EMBL:X67118; NID:g516399; PIDN:CAA47545.1; !1PID:g516403 !'##experimental_source strain India-1967, isolate Ind3 REFERENCE JQ1832 !$#authors Aguado, B.; Selmes, I.P.; Smith, G.L. !$#journal J. Gen. Virol. (1992) 73:2887-2902 !$#title Nucleotide sequence of 21.8 kbp of variola major virus !1strain Harvey and comparison with vaccinia virus. !$#cross-references MUID:93057361; PMID:1331292 !$#accession JQ1857 !'##molecule_type DNA !'##residues 1-552 ##label AGU !'##experimental_source strain Harvey CLASSIFICATION #superfamily vaccinia virus DNA ligase KEYWORDS ligase; phosphoprotein FEATURE !$231 #active_site Lys (covalent AMP-binding) #status !8predicted SUMMARY #length 552 #molecular-weight 63382 #checksum 1730 SEQUENCE /// ENTRY A45397 #type complete TITLE DNA ligase (ATP) (EC 6.5.1.1) - African swine fever virus (strain BA71V) ALTERNATE_NAMES polydeoxyribonucleotide synthase (ATP) ORGANISM #formal_name African swine fever virus, ASFV DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 18-Jun-1999 ACCESSIONS A45397 REFERENCE A45397 !$#authors Yanez, R.J.; Vinuela, E. !$#journal Virology (1993) 193:531-536 !$#title African swine fever virus encodes a DNA ligase. !$#cross-references MUID:93174976; PMID:8438592 !$#accession A45397 !'##molecule_type DNA !'##residues 1-419 ##label YAN !'##cross-references GB:X65373; NID:g288060; PIDN:CAA46445.1; !1PID:g288061 CLASSIFICATION #superfamily African swine fever virus DNA ligase KEYWORDS ATP; DNA recombination; DNA repair; ligase; phosphoprotein FEATURE !$151 #active_site Lys (covalent AMP-binding) #status !8predicted\ !$316 #binding_site ATP (Lys) #status predicted SUMMARY #length 419 #molecular-weight 48163 #checksum 5484 SEQUENCE /// ENTRY LQECC6 #type complete TITLE DNA ligase (NAD) (EC 6.5.1.2) - Escherichia coli (strain K-12) ALTERNATE_NAMES polydeoxyribonucleotide synthase (NAD+) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 21-Nov-1997 #text_change 03-Jun-2002 ACCESSIONS B65015; JS0139 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65015 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-671 ##label BLAT !'##cross-references GB:AE000328; GB:U00096; NID:g2367135; !1PIDN:AAC75464.1; PID:g1788750; UWGP:b2411 !'##experimental_source strain K-12, substrain MG1655 REFERENCE JS0139 !$#authors Ishino, Y.; Shinagawa, H.; Makino, K.; Tsunasawa, S.; !1Sakiyama, F.; Nakata, A. !$#journal Mol. Gen. Genet. (1986) 204:1-7 !$#title Nucleotide sequence of the lig gene and primary structure of !1DNA ligase of Escherichia coli. !$#cross-references MUID:86310292; PMID:3018436 !$#accession JS0139 !'##molecule_type DNA !'##residues 1-68,'R',70-671 ##label ISH !'##cross-references GB:M30255; NID:g146614; PIDN:AAA24071.1; !1PID:g146615 !'##experimental_source strain C600 !'##note residues 1-13 and 666-671 were confirmed by direct protein !1sequencing COMMENT This protein catalyzes the formation of phosphodiester !1linkages between 5'-phosphoryl and 3'-hydroxyl groups in !1double-stranded DNA using NAD as a coenzyme and as the !1energy source for the reaction. It is essential for DNA !1replication and repair of damaged DNA. GENETICS !$#gene lig !$#map_position 52 min CLASSIFICATION #superfamily polydeoxyribonucleotide synthase (NAD+) KEYWORDS DNA repair; DNA replication; ligase; NAD SUMMARY #length 671 #molecular-weight 73605 #checksum 9920 SEQUENCE /// ENTRY F69794 #type complete TITLE DNA ligase (NAD) (EC 6.5.1.2) - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 05-Dec-1997 #sequence_revision 05-Dec-1997 #text_change 03-Jun-2002 ACCESSIONS F69794 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69794 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-668 ##label KUN !'##cross-references GB:Z99107; GB:AL009126; NID:g2632866; !1PIDN:CAB12482.1; PID:g2632976 !'##experimental_source strain 168 GENETICS !$#gene yerG CLASSIFICATION #superfamily polydeoxyribonucleotide synthase (NAD+) KEYWORDS ligase; NAD SUMMARY #length 668 #molecular-weight 74875 #checksum 5968 SEQUENCE /// ENTRY G70168 #type complete TITLE DNA ligase (NAD) (EC 6.5.1.2) - Lyme disease spirochete ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 13-Feb-1998 #sequence_revision 13-Feb-1998 #text_change 03-Jun-2002 ACCESSIONS G70168 REFERENCE A70100 !$#authors Fraser, C.M.; Casjens, S.; Huang, W.M.; Sutton, G.G.; !1Clayton, R.; Lathigra, R.; White, O.; Ketchum, K.A.; Dodson, !1R.; Hickey, E.K.; Gwinn, M.; Dougherty, B.; Tomb, J.F.; !1Fleischmann, R.D.; Richardson, D.; Peterson, J.; Kerlavage, !1A.R.; Quackenbush, J.; Salzberg, S.; Hanson, M.; Vugt, R.V.; !1Palmer, N.; Adams, M.D.; Gocayne, J.; Weidman, J.; !1Utterback, T.; Watthey, L.; McDonald, L.; Artiach, P.; !1Bowman, C.; Garland, S.; Fujii, C.; Cotton, M.D.; Horst, K.; !1Roberts, K.; Hatch, B.; Smith, H.O.; Venter, J.C. !$#journal Nature (1997) 390:580-586 !$#title Genomic sequence of a Lyme disease spirochaete, Borrelia !1burgdorferi. !$#cross-references MUID:98065943; PMID:9403685 !$#accession G70168 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-660 ##label KLE !'##cross-references GB:AE001157; GB:AE000783; NID:g2688471; !1PIDN:AAC66923.1; PID:g2688477; TIGR:BB0552 !'##experimental_source strain B31 CLASSIFICATION #superfamily polydeoxyribonucleotide synthase (NAD+) KEYWORDS ligase; NAD SUMMARY #length 660 #molecular-weight 75316 #checksum 9505 SEQUENCE /// ENTRY G64596 #type complete TITLE DNA ligase (NAD) (EC 6.5.1.2) - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 09-Aug-1997 #sequence_revision 09-Aug-1997 #text_change 03-Jun-2002 ACCESSIONS G64596 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession G64596 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-656 ##label TOM !'##cross-references GB:AE000576; GB:AE000511; NID:g2313736; !1PIDN:AAD07680.1; PID:g2313737; TIGR:HP0615 CLASSIFICATION #superfamily polydeoxyribonucleotide synthase (NAD+) KEYWORDS ligase; NAD SUMMARY #length 656 #molecular-weight 73899 #checksum 7606 SEQUENCE /// ENTRY S20687 #type complete TITLE DNA ligase (NAD) (EC 6.5.1.2) - Zymomonas mobilis ORGANISM #formal_name Zymomonas mobilis DATE 20-Feb-1995 #sequence_revision 20-Feb-1995 #text_change 03-Jun-2002 ACCESSIONS S20687 REFERENCE S20687 !$#authors Shark, K.B.; Conway, T. !$#submission submitted to the EMBL Data Library, April 1992 !$#description Cloning and characterization of the DNA ligase gene (lig) !1from Zymomonas mobilis. !$#accession S20687 !'##molecule_type DNA !'##residues 1-731 ##label SHA !'##cross-references EMBL:Z11910; NID:g49283; PIDN:CAA77966.1; !1PID:g49284 CLASSIFICATION #superfamily polydeoxyribonucleotide synthase (NAD+) KEYWORDS ligase; NAD SUMMARY #length 731 #molecular-weight 82089 #checksum 6031 SEQUENCE /// ENTRY S74436 #type complete TITLE DNA ligase (NAD) (EC 6.5.1.2) - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein sll1209 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 25-Apr-1997 #sequence_revision 25-Apr-1997 #text_change 03-Jun-2002 ACCESSIONS S74436 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74436 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-669 ##label KAN !'##cross-references EMBL:D90899; GB:AB001339; NID:g1651650; !1PIDN:BAA16588.1; PID:g1651660 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene lig CLASSIFICATION #superfamily polydeoxyribonucleotide synthase (NAD+) KEYWORDS ligase; NAD SUMMARY #length 669 #molecular-weight 74602 #checksum 9660 SEQUENCE /// ENTRY A64228 #type complete TITLE DNA ligase (NAD) (EC 6.5.1.2) - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 17-Nov-1995 #sequence_revision 17-Nov-1995 #text_change 03-Jun-2002 ACCESSIONS A64228 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession A64228 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-659 ##label TIGR !'##cross-references GB:U39703; GB:L43967; NID:g1045933; PID:g1045945; !1TIGR:MG254 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 !$#start_codon GTG CLASSIFICATION #superfamily polydeoxyribonucleotide synthase (NAD+) KEYWORDS ligase; NAD SUMMARY #length 659 #molecular-weight 75388 #checksum 5929 SEQUENCE /// ENTRY S73805 #type complete TITLE DNA ligase (NAD) (EC 6.5.1.2) - Mycoplasma pneumoniae (strain ATCC 29342) ALTERNATE_NAMES hypothetical protein H91_orf658 ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 27-Feb-1997 #sequence_revision 25-Apr-1997 #text_change 03-Jun-2002 ACCESSIONS S73805 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73805 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-658 ##label HIM !'##cross-references EMBL:AE000047; GB:U00089; NID:g1674162; !1PIDN:AAB96127.1; PID:g1674170 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#gene lig !$#genetic_code SGC3 CLASSIFICATION #superfamily polydeoxyribonucleotide synthase (NAD+) KEYWORDS ligase; NAD SUMMARY #length 658 #molecular-weight 73969 #checksum 6864 SEQUENCE /// ENTRY LQBPR4 #type complete TITLE RNA ligase (ATP) (EC 6.5.1.3) - phage T4 ALTERNATE_NAMES polyribonucleotide synthase (ATP) ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 18-Jun-1999 ACCESSIONS A01202; S08604 REFERENCE A01202 !$#authors Rand, K.N.; Gait, M.J. !$#journal EMBO J. (1984) 3:397-402 !$#title Sequence and cloning of bacteriophage T4 gene 63 encoding !1RNA ligase and tail fibre attachment activities. !$#cross-references MUID:84182503; PMID:6370680 !$#accession A01202 !'##molecule_type mRNA !'##residues 1-374 ##label RAN !'##cross-references GB:X00365; NID:g15366; PIDN:CAA25107.1; PID:g15367 REFERENCE S07190 !$#authors Sjoeberg, B.M.; Hahne, S.; Mathews, C.Z.; Mathews, C.K.; !1Rand, K.N.; Gait, M.J. !$#journal EMBO J. (1986) 5:2031-2036 !$#title The bacteriophage T4 gene for the small subunit of !1ribonucleotide reductase contains an intron. !$#cross-references MUID:87004574; PMID:3530746 !$#accession S08604 !'##status preliminary !'##molecule_type DNA !'##residues 1-89 ##label SJO !'##cross-references EMBL:X04140; NID:g15341; PIDN:CAA27760.1; !1PID:g15345 REFERENCE A30612 !$#authors Thogersen, H.C.; Morris, H.R.; Rand, K.N.; Gait, M.J. !$#journal Eur. J. Biochem. (1985) 147:325-329 !$#title Location of the adenylylation site in T4 RNA ligase. !$#cross-references MUID:85127046; PMID:3882425 !$#contents annotation; determination of active site covalent !1intermediate GENETICS !$#gene 63 FUNCTION !$#description catalyzes the ligation of the 5'-phosphate of a strand of !1RNA to a 3'-phosphate of a strand of RNA using ATP and !1producing AMP and pyrophosphate !$#note can circularize linear RNA CLASSIFICATION #superfamily phage T4 RNA ligase KEYWORDS ligase; phosphoprotein; RNA biosynthesis; RNA repair FEATURE !$99 #active_site Lys (covalent AMP-binding) #status !8experimental SUMMARY #length 374 #molecular-weight 43509 #checksum 8072 SEQUENCE /// ENTRY SYRTPP #type complete TITLE erythrodihydroneopterin triphosphate synthetase (EC 6.-.-.-) - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Nov-1980 #sequence_revision 30-Nov-1980 #text_change 18-Mar-1994 ACCESSIONS A01203 REFERENCE A91463 !$#authors Gal, E.M.; Sherman, A.D. !$#journal Fed. Proc. (1979) 38:324 !$#title Sequence of the amino-terminal region of pig kidney fructure !11,6-bisphosphatase. !$#accession A01203 !'##molecule_type protein !'##residues 1-68 ##label GAL !'##note the sequence shown corresponds to the enzyme isolated from rat !1liver; the enzyme isolated from rat brain differs in having !1an additional residue, Asp, after 7-Tyr REFERENCE A90210 !$#authors Gal, E.M.; Sherman, A.D. !$#journal Biochem. Biophys. Res. Commun. (1978) 83:593-598 !$#title Phosphorylation, a factor controlling the synthesis of !1L-erythrodihydrobiopterin (BH-2). !$#cross-references MUID:79021006; PMID:697844 !$#contents annotation; phosphorylation site CLASSIFICATION #superfamily erythrodihydroneopterin triphosphate synthetase KEYWORDS ligase; phosphoprotein FEATURE !$66 #binding_site phosphate (Ser) (covalent) #status !8experimental SUMMARY #length 68 #molecular-weight 7837 #checksum 9883 SEQUENCE /// ENTRY SYGPPP #type complete TITLE erythrodihydroneopterin triphosphate synthetase (EC 6.-.-.-) - guinea pig ORGANISM #formal_name Cavia porcellus #common_name guinea pig DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 18-Mar-1994 ACCESSIONS A91463; A01203 REFERENCE A91463 !$#authors Gal, E.M.; Sherman, A.D. !$#journal Fed. Proc. (1979) 38:324 !$#title Sequence of the amino-terminal region of pig kidney fructure !11,6-bisphosphatase. !$#accession A91463 !'##molecule_type protein !'##residues 1-68 ##label GAL REFERENCE A90210 !$#authors Gal, E.M.; Sherman, A.D. !$#journal Biochem. Biophys. Res. Commun. (1978) 83:593-598 !$#title Phosphorylation, a factor controlling the synthesis of !1L-erythrodihydrobiopterin (BH-2). !$#cross-references MUID:79021006; PMID:697844 !$#contents annotation; phosphorylation site CLASSIFICATION #superfamily erythrodihydroneopterin triphosphate synthetase KEYWORDS ligase; phosphoprotein FEATURE !$66 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 68 #molecular-weight 7837 #checksum 9883 SEQUENCE /// ENTRY SYBOPP #type complete TITLE erythrodihydroneopterin triphosphate synthetase (EC 6.-.-.-) - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 18-Mar-1994 ACCESSIONS B91463; A01203 REFERENCE A91463 !$#authors Gal, E.M.; Sherman, A.D. !$#journal Fed. Proc. (1979) 38:324 !$#title Sequence of the amino-terminal region of pig kidney fructure !11,6-bisphosphatase. !$#accession B91463 !'##molecule_type protein !'##residues 1-68 ##label GAL REFERENCE A90210 !$#authors Gal, E.M.; Sherman, A.D. !$#journal Biochem. Biophys. Res. Commun. (1978) 83:593-598 !$#title Phosphorylation, a factor controlling the synthesis of !1L-erythrodihydrobiopterin (BH-2). !$#cross-references MUID:79021006; PMID:697844 !$#contents annotation; phosphorylation site CLASSIFICATION #superfamily erythrodihydroneopterin triphosphate synthetase KEYWORDS ligase; phosphoprotein FEATURE !$66 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 68 #molecular-weight 7837 #checksum 9883 SEQUENCE /// ENTRY SYHU18 #type complete TITLE (2'-5')oligo(A) synthetase (EC 2.7.7.-), splice form E18 - human ALTERNATE_NAMES oligoadenylate synthetase ORGANISM #formal_name Homo sapiens #common_name man DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 20-Apr-2000 ACCESSIONS B24359; I57630; I37997 REFERENCE A91013 !$#authors Benech, P.; Mory, Y.; Revel, M.; Chebath, J. !$#journal EMBO J. (1985) 4:2249-2256 !$#title Structure of two forms of the interferon-induced (2'-5') !1oligo A synthetase of human cells based on cDNAs and gene !1sequences. !$#cross-references MUID:86081732; PMID:2416561 !$#accession B24359 !'##molecule_type mRNA !'##residues 1-400 ##label BEN !'##cross-references GB:M11810; GB:K00006; GB:X02875; NID:g189322; !1PIDN:AAB59553.1; PID:g386986 REFERENCE I57630 !$#authors Benech, P.; Vigneron, M.; Peretz, D.; Revel, M.; Chebath, J. !$#journal Mol. Cell. Biol. (1987) 7:4498-4504 !$#title Interferon-responsive regulatory elements in the promoter of !1the human 2',5'-oligo(A) synthetase gene. !$#cross-references MUID:88142842; PMID:2830497 !$#accession I57630 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 2-28 ##label RES !'##cross-references GB:M18099; NID:g189326; PIDN:AAA59955.1; !1PID:g553604 REFERENCE I37997 !$#authors Wathelet, M.G.; Clauss, I.M.; Nols, C.B.; Content, J.; Huez, !1G.A. !$#journal Eur. J. Biochem. (1987) 169:313-321 !$#title New inducers revealed by the promoter sequence analysis of !1two interferon-activated human genes. !$#cross-references MUID:88082760; PMID:3121313 !$#accession I37997 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-28 ##label RE2 !'##cross-references EMBL:X06560; NID:g34393; PIDN:CAA29803.1; !1PID:g34394 COMMENT For alternate splice forms, see PIR:SYHU16 and PIR:A22842. GENETICS !$#gene GDB:OIAS !'##cross-references GDB:119465; OMIM:164350 !$#map_position 12pter-12qter CLASSIFICATION #superfamily oligo(A) synthetase KEYWORDS alternative splicing; nucleotidyltransferase SUMMARY #length 400 #molecular-weight 46000 #checksum 7015 SEQUENCE /// ENTRY SYHU16 #type complete TITLE (2'-5')oligo(A) synthetase (EC 2.7.7.-), splice form E16 - human ALTERNATE_NAMES oligoadenylate synthetase ORGANISM #formal_name Homo sapiens #common_name man DATE 14-Nov-1983 #sequence_revision 28-Dec-1987 #text_change 21-Jul-2000 ACCESSIONS A91013; JS0012; A23623; A01204; A24359 REFERENCE A91013 !$#authors Benech, P.; Mory, Y.; Revel, M.; Chebath, J. !$#journal EMBO J. (1985) 4:2249-2256 !$#title Structure of two forms of the interferon-induced (2'-5') !1oligo A synthetase of human cells based on cDNAs and gene !1sequences. !$#cross-references MUID:86081732; PMID:2416561 !$#accession A91013 !'##molecule_type mRNA !'##residues 1-364 ##label BEN !'##cross-references GB:X02874; GB:K00006; NID:g35122; PIDN:CAA26633.1; !1PID:g35123 REFERENCE A92003 !$#authors Shiojiri, S.; Fukunaga, R.; Ichii, Y.; Sokawa, Y. !$#journal J. Biochem. (1986) 99:1455-1464 !$#title Structure and expression of a cloned cDNA for human !1(2'-5')oligoadenylate synthetase. !$#cross-references MUID:86223945; PMID:3754863 !$#accession JS0012 !'##molecule_type mRNA !'##residues 1-30,'N',32-114,'F',116-364 ##label SHI !'##cross-references GB:D00068; GB:N00068; NID:g220080; PIDN:BAA00047.1; !1PID:g220081 REFERENCE A23623 !$#authors Wathelet, M.; Moutschen, S.; Cravador, A.; DeWit, L.; !1Defilippi, P.; Huez, G.; Content, J. !$#journal FEBS Lett. (1986) 196:113-120 !$#title Full-length sequence and expression of the 42 kDa 2-5A !1synthetase induced by human interferon. !$#cross-references MUID:86108911; PMID:3753689 !$#accession A23623 !'##molecule_type mRNA !'##residues 1-30,'N',32-114,'F',116-294,'T',296-314,'R',316-364 ##label !1WAT !'##cross-references GB:X04371; GB:M25352; NID:g23792; PIDN:CAB51602.1; !1PID:g5650578 COMMENT This enzyme, one of those induced by interferons, binds !1double-stranded RNA and polymerizes ATP into ppp(A2'p)nA !1oligomers, which activate the latent RNase F and inhibit !1protein synthesis. COMMENT For alternate splice forms, see PIR:SYHU18 and PIR:A22842. GENETICS !$#gene GDB:OIAS !'##cross-references GDB:119465; OMIM:164350 !$#map_position 12pter-12qter CLASSIFICATION #superfamily oligo(A) synthetase KEYWORDS alternative splicing; nucleotidyltransferase SUMMARY #length 364 #molecular-weight 41737 #checksum 8814 SEQUENCE /// ENTRY SYMSO2 #type complete TITLE (2'-5')oligo(A) synthetase (EC 2.7.7.-) 2 - mouse ALTERNATE_NAMES 2'-5'-oligoadenylate synthetase 2 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 11-Sep-1998 ACCESSIONS A39417 REFERENCE A39417 !$#authors Ghosh, S.K.; Kusari, J.; Bandyopadhyay, S.K.; Samanta, H.; !1Kumar, R.; Sen, G.C. !$#journal J. Biol. Chem. (1991) 266:15293-15299 !$#title Cloning, sequencing, and expression of two murine !12'-5'-oligoadenylate synthetases. Structure-function !1relationships. !$#cross-references MUID:91332052; PMID:1651324 !$#accession A39417 !'##molecule_type mRNA !'##residues 1-363 ##label GHO !'##cross-references GB:M63849 !'##note the authors translated the codon TTG for residue 259 as Arg COMMENT This enzyme, one of those induced by interferons, binds !1double-stranded RNA and polymerizes ATP into ppp(A2'p)nA !1oligomers, which activate the latent RNase F and inhibit !1protein synthesis. CLASSIFICATION #superfamily oligo(A) synthetase KEYWORDS nucleotidyltransferase SUMMARY #length 363 #molecular-weight 41697 #checksum 8938 SEQUENCE /// ENTRY SYMSO3 #type complete TITLE (2'-5')oligo(A) synthetase (EC 2.7.7.-) 3 - mouse ALTERNATE_NAMES 2'-5'-oligoadenylate synthetase 3 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS B39417 REFERENCE A39417 !$#authors Ghosh, S.K.; Kusari, J.; Bandyopadhyay, S.K.; Samanta, H.; !1Kumar, R.; Sen, G.C. !$#journal J. Biol. Chem. (1991) 266:15293-15299 !$#title Cloning, sequencing, and expression of two murine !12'-5'-oligoadenylate synthetases. Structure-function !1relationships. !$#cross-references MUID:91332052; PMID:1651324 !$#accession B39417 !'##molecule_type mRNA !'##residues 1-414 ##label GHO !'##cross-references GB:M63850; NID:g200136; PIDN:AAA39858.1; !1PID:g200137 !'##note the authors translated the codon TTG for residue 259 as Arg COMMENT This enzyme, one of those induced by interferons, binds !1double-stranded RNA and polymerizes ATP into ppp(A2'p)nA !1oligomers, which activate the latent RNase F and inhibit !1protein synthesis. CLASSIFICATION #superfamily oligo(A) synthetase KEYWORDS nucleotidyltransferase SUMMARY #length 414 #molecular-weight 47520 #checksum 6950 SEQUENCE /// ENTRY SYMSO1 #type complete TITLE (2'-5')oligo(A) synthetase (EC 2.7.7.-) 1 - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS A24725; A45349 REFERENCE A24725 !$#authors Ichii, Y.; Fukunaga, R.; Shiojiri, S.; Sokawa, Y. !$#journal Nucleic Acids Res. (1986) 14:10117 !$#title Mouse 2-5A synthetase cDNA: nucleotide sequence and !1comparison to human 2-5A synthetase. !$#cross-references MUID:87117515; PMID:3808949 !$#accession A24725 !'##molecule_type mRNA !'##residues 1-367 ##label ICH !'##cross-references EMBL:X04958; NID:g54214; PIDN:CAA28620.1; !1PID:g54215 REFERENCE A45349 !$#authors Coccia, E.M.; Romeo, G.; Nissim, A.; Marziali, G.; !1Albertini, R.; Affabris, E.; Battistini, A.; Fiorucci, G.; !1Orsatti, R.; Rossi, G.B.; Chebath, J. !$#journal Virology (1990) 179:228-233 !$#title A full-length murine 2-5A synthetase cDNA transfected in !1NIH-3T3 cells impairs EMCV but not VSV replication. !$#cross-references MUID:91021025; PMID:2171206 !$#accession A45349 !'##molecule_type mRNA !'##residues 1-367 ##label COC !'##cross-references GB:M33863; NID:g191502; PIDN:AAA37116.1; !1PID:g309075 COMMENT This enzyme, one of those induced by interferons, binds !1double-stranded RNA and polymerizes ATP into ppp(A2'p)nA !1oligomers, which activate the latent RNase F and inhibit !1protein synthesis. CLASSIFICATION #superfamily oligo(A) synthetase KEYWORDS nucleotidyltransferase SUMMARY #length 367 #molecular-weight 42456 #checksum 5922 SEQUENCE /// ENTRY S01913 #type complete TITLE diaminopimelate epimerase (EC 5.1.1.7) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Sep-1989 #sequence_revision 10-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS B65185; S30699; S01913; A37841; S24977 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65185 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-275 ##label BLAT !'##cross-references GB:AE000457; GB:U00096; NID:g2367294; !1PIDN:AAC76812.1; PID:g1790242; UWGP:b3809 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S30660 !$#authors Daniels, D.L.; Plunkett III, G.; Burland, V.; Blattner, F.R. !$#journal Science (1992) 257:771-778 !$#title Analysis of the Escherichia coli genome: DNA sequence of the !1region from 84.5 to 86.5 minutes. !$#cross-references MUID:92358234; PMID:1379743 !$#accession S30699 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-98,'X',100-275 ##label DAN !'##cross-references EMBL:M87049; NID:g836656; PIDN:AAA67605.1; !1PID:g148208 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1992 REFERENCE S01913 !$#authors Richaud, C.; Printz, C. !$#journal Nucleic Acids Res. (1988) 16:10367 !$#title Nucleotide sequence of the dapF gene and flanking regions !1from Escherichia coli K12. !$#cross-references MUID:89057481; PMID:3057443 !$#accession S01913 !'##molecule_type DNA !'##residues 1-98,'T',100-160,'WL',163-200,'DD',203-275 ##label RIC !'##cross-references EMBL:X12968; NID:g41236; PIDN:CAA31413.1; !1PID:g41237 !'##experimental_source strain K12 REFERENCE A37841 !$#authors Colloms, S.D.; Sykora, P.; Szatmari, G.; Sherratt, D.J. !$#journal J. Bacteriol. (1990) 172:6973-6980 !$#title Recombination at ColE1 cer requires the Escherichia coli !1xerC gene product, a member of the lambda integrase family !1of site-specific recombinases. !$#cross-references MUID:91072248; PMID:2254268 !$#accession A37841 !'##status preliminary !'##molecule_type DNA !'##residues 260-275 ##label COL !'##cross-references GB:M38257; NID:g148267; PIDN:AAA24761.1; !1PID:g148268 REFERENCE S24974 !$#authors Glaser, P.; Sismeiro, O.; Danchin, A. !$#submission submitted to the EMBL Data Library, June 1992 !$#description Phylogeny of enterobacterial cya locus. !$#accession S24977 !'##status preliminary !'##molecule_type DNA !'##residues 2-9,'HWQR',14,'YGR' ##label GLA !'##cross-references EMBL:X66782; NID:g41185; PIDN:CAA47282.1; !1PID:g41189 GENETICS !$#gene dapF !$#map_position 85 min FUNCTION !$#description catalyzes the isomerization between ll-2, !16-diaminoheptanedioate and meso-diaminoheptanedioate !$#pathway lysine biosynthesis from aspartate semialdehyde CLASSIFICATION #superfamily diaminopimelate epimerase KEYWORDS isomerase; lysine biosynthesis SUMMARY #length 275 #molecular-weight 30340 #checksum 7094 SEQUENCE /// ENTRY YGBSG1 #type complete TITLE phenylalanine racemase (ATP-hydrolyzing) (EC 5.1.1.11) - Bacillus brevis ALTERNATE_NAMES gramicidin S synthetase component I; gramicidin S synthetase I ORGANISM #formal_name Bacillus brevis DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 03-Nov-2000 ACCESSIONS JU0122; C33593; A56320 REFERENCE JU0122 !$#authors Hori, K.; Yamamoto, Y.; Minetoki, T.; Kurotsu, T.; Kanda, !1M.; Miura, S.; Okamura, K.; Furuyama, J.; Saito, Y. !$#journal J. Biochem. (1989) 106:639-645 !$#title Molecular cloning and nucleotide sequence of the gramicidin !1S synthetase 1 gene. !$#cross-references MUID:90110062; PMID:2691508 !$#accession JU0122 !'##molecule_type DNA !'##residues 1-1098 ##label HOR !'##cross-references EMBL:M29703 !'##experimental_source strain Nagano REFERENCE A33593 !$#authors Kraetzschmar, J.; Krause, M.; Marahiel, M.A. !$#journal J. Bacteriol. (1989) 171:5422-5429 !$#title Gramicidin S biosynthesis operon containing the structural !1genes grsA and grsB has an open reading frame encoding a !1protein homologous to fatty acid thioesterases. !$#cross-references MUID:90008776; PMID:2477357 !$#accession C33593 !'##molecule_type DNA !'##residues 1-341,'I',343-418,'S',420-474,'Y',476-820,'E',822-1098 !1##label KRA !'##cross-references EMBL:M29703 !'##experimental_source ATCC 9999 REFERENCE A56320 !$#authors Stein, T.; Kluge, B.; Vater, J.; Franke, P.; Otto, A.; !1Wittmann-Liebold, B. !$#journal Biochemistry (1995) 34:4633-4642 !$#title Gramicidin S synthetase 1 (phenylalanine racemase), a !1prototype of amino acid racemases containing the cofactor !14'-phosphopantetheine. !$#cross-references MUID:95234688; PMID:7718566 !$#accession A56320 !'##status preliminary !'##molecule_type protein !'##residues 564-575 ##label STE !'##experimental_source ATCC 9999 GENETICS !$#gene grsA FUNCTION !$#description catalyzes the synthesis of gramicidin S, a cyclic !1decapeptide antibiotic; component I activates and racemizes !1the first amino acid, phenylalanine, to the D-isomer. !1Component II activates the other constituent amino acids, !1Pro, Val, Orn, and Leu; it also catalyzes the pentapeptide !1formation; two identical pentapeptides cyclize to form !1gramicidin S CLASSIFICATION #superfamily gramicidin S synthetase I; acetate-CoA ligase !1homology; acyl carrier protein homology KEYWORDS antibiotic biosynthesis; carrier protein; isomerase; !1phosphopantetheine; phosphoprotein FEATURE !$85-523 #domain acetate-CoA ligase homology #label ACL\ !$541-608 #domain acyl carrier protein homology #label ACP\ !$573 #binding_site phosphopantetheine (Ser) (covalent) !8#status experimental SUMMARY #length 1098 #molecular-weight 126565 #checksum 3484 SEQUENCE /// ENTRY YGBSTB #type complete TITLE phenylalanine racemase (ATP-hydrolyzing) (EC 5.1.1.11) tycA - Bacillus brevis ALTERNATE_NAMES tyrocidine synthetase component I; tyrocidine synthetase 1 ORGANISM #formal_name Bacillus brevis DATE 31-Dec-1991 #sequence_revision 03-Nov-2000 #text_change 17-Nov-2000 ACCESSIONS T31074; S02039; A33956; A54110 REFERENCE Z20969 !$#authors Mootz, H.D.; Marahiel, M.A. !$#journal J. Bacteriol. (1997) 179:6843-6850 !$#title The tyrocidine biosynthesis operon of Bacillus brevis: !1Complete nucleotide sequence and biochemical !1characterization of functional internal adenylation domains. !$#cross-references MUID:98012987; PMID:9352938 !$#accession T31074 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-1088 ##label MOO !'##cross-references EMBL:AF004835; NID:g2623770; PID:g2623771; !1PIDN:AAC45928.1 !'##experimental_source ATCC 8185 REFERENCE S02039 !$#authors Weckermann, R.; Fuerbass, R.; Marahiel, M.A. !$#journal Nucleic Acids Res. (1988) 16:11841 !$#title Complete nucleotide sequence of the tycA gene coding the !1tyrocidine synthetase 1 from Bacillus brevis. !$#cross-references MUID:89098354; PMID:3267240 !$#accession S02039 !'##status translation not shown !'##molecule_type DNA !'##residues 1-196,'ICNPFSKIRLASPSKTGSGFLPACRSTHPFGKCSWLCCLAPRVHP', !1243-358,'AD',361-664,'V',666-736,'F',738-755, !1'KIWQPDTRRHLQGKRSVCPKKRILFKAGHNGCKNN',791-875, !1'KSSFIWRGTGARTSSNRQT',895-1088 ##label WEC !'##cross-references EMBL:X13237; NID:g39400; PIDN:CAA31623.1; !1PID:g39401 !'##experimental_source ATCC 8185 REFERENCE A33956 !$#authors Mittenhuber, G.; Weckermann, R.; Marahiel, M.A. !$#journal J. Bacteriol. (1989) 171:4881-4887 !$#title Gene cluster containing the genes for tyrocidine synthetases !11 and 2 from Bacillus brevis: evidence for an operon. !$#cross-references MUID:89359123; PMID:2768192 !$#accession A33956 !'##molecule_type DNA !'##residues 1018-1088 ##label MIT !'##experimental_source ATCC 8185 REFERENCE A54110 !$#authors Pavela-Vrancic, M.; Pfeifer, E.; van Liempt, H.; Schaefer, !1H.J.; von Doehren, H.; Kleinkauf, H. !$#journal Biochemistry (1994) 33:6276-6283 !$#title ATP binding in peptide synthetases: determination of contact !1sites of the adenine moiety by photoaffinity labeling of !1tyrocidine synthetase 1 with 2-azidoadenosine triphosphate. !$#cross-references MUID:94250669; PMID:8193142 !$#accession A54110 !'##status preliminary !'##molecule_type protein !'##residues 374-385;406-417;484-495,'I' ##label PAV COMMENT This enzyme is one of three components of the enzyme complex !1that catalyzes the synthesis of tyrocidine, a cyclic !1decapeptide antibiotic. GENETICS !$#gene tycA FUNCTION !$#description activates and racemizes phenylalanine, the first amino acid !1of tyrocidine, to the D-isomer !$#pathway tyrocidine biosynthesis CLASSIFICATION #superfamily gramicidin S synthetase I; acetate-CoA ligase !1homology; acyl carrier protein homology KEYWORDS antibiotic biosynthesis; carrier protein; isomerase; !1phosphopantetheine; phosphoprotein FEATURE !$73-512 #domain acetate-CoA ligase homology #label ACL\ !$531-598 #domain acyl carrier protein homology #label ACP\ !$563 #binding_site phosphopantetheine (Ser) (covalent) !8#status predicted SUMMARY #length 1088 #molecular-weight 122671 #checksum 107 SEQUENCE /// ENTRY YGPLV8 #type complete TITLE alpha-aminoadipyl-cysteinyl-valine synthetase (EC 6.-.-.-) - Penicillium chrysogenum (strain AS-P-78) ALTERNATE_NAMES ACV synthetase ORGANISM #formal_name Penicillium chrysogenum DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 03-Nov-2000 ACCESSIONS A37886 REFERENCE A37886 !$#authors Diez, B.; Gutierrez, S.; Barredo, J.L.; van Solingen, P.; !1van der Voort, L.H.M.; Martin, J.F. !$#journal J. Biol. Chem. (1990) 265:16358-16365 !$#title The cluster of penicillin biosynthetic genes. Identification !1and characterization of the pcbAB gene encoding the !1alpha-aminoadipyl-cysteinyl-valine synthetase and linkage to !1the pcbC and penDE genes. !$#cross-references MUID:90375501; PMID:2129535 !$#accession A37886 !'##molecule_type DNA !'##residues 1-3791 ##label DIE !'##cross-references GB:M57425; GB:J05604; NID:g169183; PIDN:AAA63415.1; !1PID:g169184 COMMENT This multifunctional enzyme catalyzes the formation of !1alpha-aminoadipyl-cysteinyl-valine by activating the three !1precursor amino acids in the L form, racemizing the L to !1D-valine, and carrying out the polymerization steps to form !1the tripeptide, which is the first common intermediate of !1penicillins and cephalosporin. GENETICS !$#gene pcbAB CLASSIFICATION #superfamily alpha-aminoadipyl-cysteinyl-valine synthetase; !1acetate-CoA ligase homology; acyl carrier protein homology KEYWORDS carrier protein; cephalosporin biosynthesis; duplication; !1ligase; penicillin biosynthesis; phosphopantetheine; !1phosphoprotein FEATURE !$368-834 #domain acetate-CoA ligase homology #label ACL1\ !$851-923 #domain acyl carrier protein homology #label ACP1\ !$1464-1921 #domain acetate-CoA ligase homology #label ACL2\ !$1937-2007 #domain acyl carrier protein homology #label ACP2\ !$2547-3009 #domain acetate-CoA ligase homology #label ACL3\ !$3026-3094 #domain acyl carrier protein homology #label ACP3\ !$885,1971,3058 #binding_site phosphopantetheine (Ser) (covalent) !8#status predicted SUMMARY #length 3791 #molecular-weight 425918 #checksum 3817 SEQUENCE /// ENTRY YGPLV3 #type complete TITLE alpha-aminoadipyl-cysteinyl-valine synthetase (EC 6.-.-.-) - Penicillium chrysogenum (strain Oli13) ALTERNATE_NAMES ACV synthetase ORGANISM #formal_name Penicillium chrysogenum DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 03-Nov-2000 ACCESSIONS S13134 REFERENCE S13134 !$#authors Smith, D.J.; Earl, A.J.; Turner, G. !$#journal EMBO J. (1990) 9:2743-2750 !$#title The multifunctional peptide synthetase performing the first !1step of penicillin biosynthesis in Penicillium chrysogenum !1is a 421 073 dalton protein similar to Bacillus brevis !1peptide antibiotic synthetases. !$#cross-references MUID:90360984; PMID:2118102 !$#accession S13134 !'##molecule_type DNA !'##residues 1-3746 ##label SMI !'##cross-references GB:X54296; NID:g3117; PIDN:CAA38195.1; PID:g3118 COMMENT This multifunctional enzyme catalyzes the formation of !1alpha-aminoadipyl-cysteinyl-valine by activating the three !1precursor amino acids in the L form, racemizing the L to !1D-valine, and carrying out the polymerization steps to form !1the tripeptide, which is the first common intermediate of !1penicillins and cephalosporin. GENETICS !$#gene pcbAB CLASSIFICATION #superfamily alpha-aminoadipyl-cysteinyl-valine synthetase; !1acetate-CoA ligase homology; acyl carrier protein homology KEYWORDS carrier protein; cephalosporin biosynthesis; duplication; !1ligase; penicillin biosynthesis; phosphopantetheine; !1phosphoprotein FEATURE !$338-804 #domain acetate-CoA ligase homology #label ACL1\ !$821-891 #domain acyl carrier protein homology #label ACP1\ !$1432-1889 #domain acetate-CoA ligase homology #label ACL2\ !$1905-1975 #domain acyl carrier protein homology #label ACP2\ !$2515-2977 #domain acetate-CoA ligase homology #label ACL3\ !$2994-3062 #domain acyl carrier protein homology #label ACP3\ !$855,1939,3026 #binding_site phosphopantetheine (Ser) (covalent) !8#status predicted SUMMARY #length 3746 #molecular-weight 421073 #checksum 9188 SEQUENCE /// ENTRY YGCEVC #type complete TITLE alpha-aminoadipyl-cysteinyl-valine synthetase (EC 6.-.-.-) - fungus (Acremonium chrysogenum) ALTERNATE_NAMES ACV synthetase ORGANISM #formal_name Acremonium chrysogenum DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 03-Nov-2000 ACCESSIONS A38531 REFERENCE A38531 !$#authors Gutierrez, S.; Diez, B.; Montenegro, E.; Martin, J.F. !$#journal J. Bacteriol. (1991) 173:2354-2365 !$#title Characterization of the Cephalosporium acremonium pcbAB gene !1encoding alpha-aminoadipyl-cysteinyl-valine synthetase, a !1large multidomain peptide synthetase: linkage to the pcbC !1gene as a cluster of early cephalosporin biosynthetic genes !1and evidence of multiple functional domains. !$#cross-references MUID:91177827; PMID:1706706 !$#accession A38531 !'##molecule_type DNA !'##residues 1-3712 ##label GUT COMMENT This multifunctional enzyme catalyzes the formation of !1alpha-aminoadipyl-cysteinyl-valine by activating the three !1precursor amino acids in the L form, racemizing the L to !1D-valine, and carrying out the polymerization steps to form !1the tripeptide, which is the first common intermediate of !1penicillins and cephalosporin. GENETICS !$#gene pcbAB CLASSIFICATION #superfamily alpha-aminoadipyl-cysteinyl-valine synthetase; !1acetate-CoA ligase homology; acyl carrier protein homology KEYWORDS carrier protein; cephalosporin biosynthesis; duplication; !1ligase; penicillin biosynthesis; phosphopantetheine; !1phosphoprotein FEATURE !$306-774 #domain acetate-CoA ligase homology #label ACL1\ !$793-863 #domain acyl carrier protein homology #label ACP1\ !$1408-1866 #domain acetate-CoA ligase homology #label ACL2\ !$1882-1952 #domain acyl carrier protein homology #label ACP2\ !$2482-2942 #domain acetate-CoA ligase homology #label ACL3\ !$2958-3026 #domain acyl carrier protein homology #label ACP3\ !$827,1916,2990 #binding_site phosphopantetheine (Ser) (covalent) !8#status predicted SUMMARY #length 3712 #molecular-weight 414771 #checksum 3975 SEQUENCE /// ENTRY YGBSG2 #type complete TITLE gramicidin S synthetase (EC 6.-.-.-) component II - Bacillus brevis ALTERNATE_NAMES gramicidin S synthetase 2 ORGANISM #formal_name Bacillus brevis DATE 31-Dec-1991 #sequence_revision 31-Dec-1992 #text_change 03-Nov-2000 ACCESSIONS S20542; PS0225; PS0182; D33593; PS0183 REFERENCE S20542 !$#authors Turgay, K.; Krause, M.; Marahiel, M.A. !$#journal Mol. Microbiol. (1992) 6:529-546 !$#title Four homologous domains in the primary structure of GrsB are !1related to domains in a superfamily of adenylate-forming !1enzymes. !$#cross-references MUID:92219998; PMID:1560782 !$#accession S20542 !'##molecule_type DNA !'##residues 1-4452 ##label TUR !'##cross-references EMBL:X61658; NID:g39371; PIDN:CAA43838.1; !1PID:g39372 REFERENCE PS0225 !$#authors Hori, K.; Yamamoto, Y.; Tokita, K.; Saito, F.; Kurotsu, T.; !1Kanda, M.; Okamura, K.; Furuyama, J.; Saito, Y. !$#journal J. Biochem. (1991) 110:111-119 !$#title The nucleotide sequence for a proline-activating domain of !1gramicidin S synthetase 2 gene from Bacillus brevis. !$#cross-references MUID:92041751; PMID:1939016 !$#accession PS0225 !'##molecule_type DNA !'##residues 1-274,'D',276-418,'R',420-654,659-660,'SFD',661,'CYQEI', !1666-941,'Q',945,'P',947,'TP',948-959 ##label HOR REFERENCE PS0182 !$#authors Kurotsu, T.; Hori, K.; Kanda, M.; Saito, Y. !$#journal J. Biochem. (1991) 109:763-769 !$#title Characterization and location of the L-proline activating !1fragment from the multifunctional gramicidin S synthetase 2. !$#cross-references MUID:92011463; PMID:1917901 !$#accession PS0182 !'##molecule_type protein !'##residues 2-16 ##label KUR REFERENCE A33593 !$#authors Kraetzschmar, J.; Krause, M.; Marahiel, M.A. !$#journal J. Bacteriol. (1989) 171:5422-5429 !$#title Gramicidin S biosynthesis operon containing the structural !1genes grsA and grsB has an open reading frame encoding a !1protein homologous to fatty acid thioesterases. !$#cross-references MUID:90008776; PMID:2477357 !$#accession D33593 !'##molecule_type DNA !'##residues 1-244 ##label KRA !'##cross-references EMBL:M29703; NID:g143028; PIDN:AAA58719.1; !1PID:g143031 GENETICS !$#gene grsB CLASSIFICATION #superfamily alpha-aminoadipyl-cysteinyl-valine synthetase; !1acetate-CoA ligase homology; acyl carrier protein homology KEYWORDS antibiotic biosynthesis; carrier protein; duplication; !1ligase; multifunctional enzyme; phosphopantetheine; !1phosphoprotein FEATURE !$2-4452 #product gramicidin S synthetase component II #status !8experimental #label MAT\ !$514-956 #domain acetate-CoA ligase homology #label ACL1\ !$974-1042 #domain acyl carrier protein homology #label ACP1\ !$1553-1992 #domain acetate-CoA ligase homology #label ACL2\ !$2010-2078 #domain acyl carrier protein homology #label ACP2\ !$2589-3038 #domain acetate-CoA ligase homology #label ACL3\ !$3056-3124 #domain acyl carrier protein homology #label ACP3\ !$3636-4076 #domain acetate-CoA ligase homology #label ACL4\ !$4094-4162 #domain acyl carrier protein homology #label ACP4\ !$1006,2042,3088,4126 #binding_site phosphopantetheine (Ser) (covalent) !8#status predicted SUMMARY #length 4452 #molecular-weight 510174 #checksum 2478 SEQUENCE /// ENTRY S18268 #type complete TITLE delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase - Streptomyces lactamdurans ORGANISM #formal_name Streptomyces lactamdurans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Nov-2000 ACCESSIONS S18268; S15283; B38171 REFERENCE S18268 !$#authors Martin, J.F. !$#submission submitted to the EMBL Data Library, January 1991 !$#accession S18268 !'##molecule_type DNA !'##residues 1-3649 ##label MAR !'##cross-references EMBL:X57310; NID:g45005; PIDN:CAA40561.1; !1PID:g45006 REFERENCE S15283 !$#authors Coque, J.J.R.; Martin, J.F.; Calzada, J.G.; Liras, P. !$#journal Mol. Microbiol. (1991) 5:1125-1133 !$#title The cephamycin biosynthetic genes pcbAB, encoding a large !1multidomain peptide synthetase, and pcbC of Nocardia !1lactamdurans are clustered together in an organization !1different from the same genes in Acremonium chrysogenum and !1Penicillium chrysogenum. !$#cross-references MUID:92065808; PMID:1956290 !$#accession S15283 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 224-940;1319-2010;2373-3307 ##label COQ !'##cross-references EMBL:X57310 !'##note the source is designated as Nocardia lactamdurans REFERENCE A38171 !$#authors Coque, J.J.R.; Liras, P.; Laiz, L.; Martin, J.F. !$#journal J. Bacteriol. (1991) 173:6258-6264 !$#title A gene encoding lysine 6-aminotransferase, which forms the !1beta-lactam precursor alpha-aminoadipic acid, is located in !1the cluster of cephamycin biosynthetic genes in Nocardia !1lactamdurans. !$#cross-references MUID:92011390; PMID:1917857 !$#accession B38171 !'##status preliminary !'##molecule_type DNA !'##residues 1-23 ##label CO2 !'##cross-references GB:S57006 GENETICS !$#gene pcbAB CLASSIFICATION #superfamily alpha-aminoadipyl-cysteinyl-valine synthetase; !1acetate-CoA ligase homology; acyl carrier protein homology KEYWORDS carrier protein; cephamycin biosynthesis; !1phosphopantetheine; phosphoprotein FEATURE !$298-758 #domain acetate-CoA ligase homology #label ACL1\ !$786-856 #domain acyl carrier protein homology #label ACP1\ !$1392-1844 #domain acetate-CoA ligase homology #label ACL2\ !$1862-1932 #domain acyl carrier protein homology #label ACP2\ !$2446-2895 #domain acetate-CoA ligase homology #label ACL3\ !$2912-2980 #domain acyl carrier protein homology #label ACP3\ !$820,1896,2944 #binding_site phosphopantetheine (Ser) (covalent) !8#status predicted SUMMARY #length 3649 #molecular-weight 404084 #checksum 2296 SEQUENCE /// ENTRY I40457 #type complete TITLE peptide synthetase ppsB - Bacillus subtilis ALTERNATE_NAMES pps2 ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Nov-2000 ACCESSIONS I40457; B69681; S49134 REFERENCE I40454 !$#authors Tognoni, A.; Franchi, E.; Magistrelli, C.; Colombo, E.; !1Cosmina, P.; Grandi, G. !$#journal Microbiology (1995) 141:645-648 !$#title A putative new peptide synthase operon in Bacillus subtilis: !1partial characterization. !$#cross-references MUID:95227362; PMID:7711903 !$#accession I40457 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-2560 ##label RES !'##cross-references EMBL:Z34883; NID:g1805667; PIDN:CAA84361.1; !1PID:g509469 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69681 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-2560 ##label KUN !'##cross-references GB:Z99113; GB:AL009126; NID:g2634090; !1PIDN:CAB13716.1; PID:g2634216 !'##experimental_source strain 168 GENETICS !$#gene ppsB; pps2 CLASSIFICATION #superfamily peptide synthetase ppsD; acetate-CoA ligase !1homology; acyl carrier protein homology KEYWORDS carrier protein; phosphopantetheine; phosphoprotein FEATURE !$515-952 #domain acetate-CoA ligase homology #label ACL1\ !$968-1036 #domain acyl carrier protein homology #label ACP1\ !$1546-1992 #domain acetate-CoA ligase homology #label ACL2\ !$2009-2076 #domain acyl carrier protein homology #label ACP2\ !$1000,2041 #binding_site phosphopantetheine (Ser) (covalent) !8#status predicted SUMMARY #length 2560 #molecular-weight 290162 #checksum 9702 SEQUENCE /// ENTRY I40456 #type complete TITLE peptide synthetase ppsA - Bacillus subtilis ALTERNATE_NAMES pps1 ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Nov-2000 ACCESSIONS I40456; A69681; S49133 REFERENCE I40454 !$#authors Tognoni, A.; Franchi, E.; Magistrelli, C.; Colombo, E.; !1Cosmina, P.; Grandi, G. !$#journal Microbiology (1995) 141:645-648 !$#title A putative new peptide synthase operon in Bacillus subtilis: !1partial characterization. !$#cross-references MUID:95227362; PMID:7711903 !$#accession I40456 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-2561 ##label RES !'##cross-references EMBL:Z34883; NID:g1805667; PIDN:CAA84360.1; !1PID:g580910 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69681 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-2561 ##label KUN !'##cross-references GB:Z99113; GB:AL009126; NID:g2634090; !1PIDN:CAB13717.1; PID:g2634217 !'##experimental_source strain 168 GENETICS !$#gene ppsA; pps1 !$#start_codon TTG CLASSIFICATION #superfamily peptide synthetase ppsD; acetate-CoA ligase !1homology; acyl carrier protein homology KEYWORDS carrier protein; phosphopantetheine; phosphoprotein FEATURE !$504-947 #domain acetate-CoA ligase homology #label ACL1\ !$964-1032 #domain acyl carrier protein homology #label ACP1\ !$1543-1994 #domain acetate-CoA ligase homology #label ACL2\ !$2010-2077 #domain acyl carrier protein homology #label ACP2\ !$996,2042 #binding_site phosphopantetheine (Ser) (covalent) !8#status predicted SUMMARY #length 2561 #molecular-weight 289181 #checksum 9798 SEQUENCE /// ENTRY JW0087 #type complete TITLE adenylyl-sulfate kinase (EC 2.7.1.25) - human ALTERNATE_NAMES adenosine 5'-phosphosulfate kinase; PAPS CONTAINS adenylylsulfate kinase (EC 2.7.1.25); sulfate adenylyltransferase (EC 2.7.7.4) ORGANISM #formal_name Homo sapiens #common_name man DATE 23-Apr-1999 #sequence_revision 23-Apr-1999 #text_change 03-Jun-2002 ACCESSIONS JW0087 REFERENCE JW0087 !$#authors Yanagisawa, K.; Sakakibara, Y.; Suiko, M.; Takami, Y.; !1Nakayama, T.; Nakajima, H.; Takayanagi, K.; Natori, Y.; Liu, !1M.C. !$#journal Biosci. Biotechnol. Biochem. (1998) 62:1037-1040 !$#title cDNA cloning, expression, and characterization of the human !1bifunctional ATP sulfurylase/adenosine 5'-phosphosulfate !1kinase enzyme. !$#cross-references MUID:98312048; PMID:9648242 !$#accession JW0087 !'##molecule_type mRNA !'##residues 1-624 ##label YAN !'##cross-references GB:AF033026; NID:g3378100; PIDN:AAC28429.1; !1PID:g3378101 !'##experimental_source Brain FUNCTION ASKF !$#description as adenylylsulfate kinase catalyzes the phosphorylation of !1adenylylsulfate by ATP to form 3'-phosphoadenylylsulfate and !1ADP FUNCTION SATF !$#description as sulfate adenylyltransferase catalyzes the reaction of !1sulfate and ATP to form adenylylsulfate and pyrophosphate CLASSIFICATION #superfamily animal 3'-phosphoadenosine-5'-phosphosulfate !1synthetase; adenylylsulfate kinase homology; sulfate !1adenylyltransferase homology KEYWORDS multifunctional enzyme; nucleotide binding; !1nucleotidyltransferase; P-loop; phosphoprotein; !1phosphotransferase FEATURE !$52-215 #domain adenylylsulfate kinase homology #label ASK\ !$59-66 #region nucleotide-binding motif A (P-loop)\ !$226-620 #domain sulfate adenylyltransferase homology #label !8SAT\ !$133 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 624 #molecular-weight 70833 #checksum 6801 SEQUENCE /// ENTRY JC4383 #type complete TITLE adenylyl-sulfate kinase (EC 2.7.1.25) - spoonworm (Urechis caupo) ALTERNATE_NAMES adenosine 5'-phosphosulfate kinase; PAPS CONTAINS adenylylsulfate kinase (EC 2.7.1.25); sulfate adenylyltransferase (EC 2.7.7.4) ORGANISM #formal_name Urechis caupo DATE 17-Jan-1996 #sequence_revision 19-Apr-1996 #text_change 03-Jun-2002 ACCESSIONS JC4383 REFERENCE JC4383 !$#authors Rosenthal, E.; Leustek, T. !$#journal Gene (1995) 165:243-248 !$#title A multifunctional Urechis caupo protein, PAPS synthetase, !1has both ATP sulfurylase and APS kinase activities. !$#cross-references MUID:96096529; PMID:8522184 !$#accession JC4383 !'##molecule_type mRNA !'##residues 1-610 ##label ROS !'##cross-references GB:L39001; NID:g705384; PIDN:AAB00139.1; !1PID:g705385 GENETICS !$#gene papss FUNCTION ASKF !$#description as adenylylsulfate kinase catalyzes the phosphorylation of !1adenylylsulfate by ATP to form 3'-phosphoadenylylsulfate and !1ADP FUNCTION SATF !$#description as sulfate adenylyltransferase catalyzes the reaction of !1sulfate and ATP to form adenylylsulfate and pyrophosphate CLASSIFICATION #superfamily animal 3'-phosphoadenosine-5'-phosphosulfate !1synthetase; adenylylsulfate kinase homology; sulfate !1adenylyltransferase homology KEYWORDS multifunctional enzyme; nucleotide binding; !1nucleotidyltransferase; P-loop; phosphoprotein; !1phosphotransferase FEATURE !$37-200 #domain adenylylsulfate kinase homology #label ASK\ !$44-51 #region nucleotide-binding motif A (P-loop)\ !$161-171 #domain 3'-phosphoadenosine-5'-phosphosulfate binding !8#status predicted #label PAB\ !$211-605 #domain sulfate adenylyltransferase homology #label !8SAT\ !$118 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 610 #molecular-weight 68475 #checksum 7175 SEQUENCE /// ENTRY T24918 #type complete TITLE 3'-phosphoadenosine-5'-phosphosulfate synthetase - Caenorhabditis elegans ALTERNATE_NAMES protein T14G10.1 ORGANISM #formal_name Caenorhabditis elegans DATE 22-Oct-1999 #sequence_revision 22-Oct-1999 #text_change 19-Jan-2001 ACCESSIONS T24918 REFERENCE Z19954 !$#authors Wild, A. !$#submission submitted to the EMBL Data Library, January 1996 !$#accession T24918 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-652 ##label WIL !'##cross-references EMBL:Z68880; PIDN:CAA93098.1; GSPDB:GN00022; !1CESP:T14G10.1 !'##experimental_source clone T14G10 GENETICS !$#gene CESP:T14G10.1 !$#map_position 4 !$#introns 23/3; 82/3; 176/1; 535/2; 623/2 FUNCTION ASKF !$#description as adenylylsulfate kinase catalyzes the phosphorylation of !1adenylylsulfate by ATP to form 3'-phosphoadenylylsulfate and !1ADP FUNCTION SATF !$#description as sulfate adenylyltransferase catalyzes the reaction of !1sulfate and ATP to form adenylylsulfate and pyrophosphate CLASSIFICATION #superfamily animal 3'-phosphoadenosine-5'-phosphosulfate !1synthetase; adenylylsulfate kinase homology; sulfate !1adenylyltransferase homology KEYWORDS multifunctional enzyme; nucleotide binding; !1nucleotidyltransferase; P-loop; phosphoprotein; !1phosphotransferase FEATURE !$56-219 #domain adenylylsulfate kinase homology #label ASK\ !$63-70 #region nucleotide-binding motif A (P-loop)\ !$180-190 #domain 3'-phosphoadenosine-5'-phosphosulfate binding !8#status predicted #label PAB\ !$230-647 #domain sulfate adenylyltransferase homology #label !8SAT\ !$137 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 652 #molecular-weight 72986 #checksum 8178 SEQUENCE /// ENTRY T01204 #type complete TITLE sulfate adenylyltransferase (EC 2.7.7.4) - maize ALTERNATE_NAMES ATP sulfurylase ORGANISM #formal_name Zea mays #common_name maize DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 23-Mar-2001 ACCESSIONS T01204 REFERENCE Z14260 !$#authors Bolchi, A.; Petrucco, S.; Foroni, C.; Tenca, G.L.; !1Ottonello, S. !$#submission submitted to the EMBL Data Library, July 1997 !$#description Sulfate permease and ATP sulfurylase mRNA are coordinately !1modulated in maize roots according to the sulfur-status: !1stereospecific downregulation by L-cysteine. !$#accession T01204 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-489 ##label BOL !'##cross-references EMBL:AF016305; NID:g2738749; PIDN:AAB94542.1; !1PID:g2738750 !'##experimental_source cultivar Paulo; root FUNCTION !$#description catalyzes activation of sulfate to adenylylsulfate CLASSIFICATION #superfamily sulfate adenylyltransferase met3-1; sulfate !1adenylyltransferase homology KEYWORDS nucleotidyltransferase FEATURE !$70-473 #domain sulfate adenylyltransferase homology #label !8SAT SUMMARY #length 489 #molecular-weight 53786 #checksum 4137 SEQUENCE /// ENTRY S75876 #type complete TITLE sulfate adenylyltransferase (EC 2.7.7.4) - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein slr1165 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S75876 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75876 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-390 ##label KAN !'##cross-references EMBL:D90913; GB:AB001339; NID:g1653348; !1PIDN:BAA18335.1; PID:g1653421 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene met3 CLASSIFICATION #superfamily sulfate adenylyltransferase met3-1; sulfate !1adenylyltransferase homology KEYWORDS nucleotidyltransferase FEATURE !$7-388 #domain sulfate adenylyltransferase homology #label !8SAT SUMMARY #length 390 #molecular-weight 43696 #checksum 462 SEQUENCE /// ENTRY A53651 #type complete TITLE sulfate adenylyltransferase (EC 2.7.7.4) [validated] - Penicillium chrysogenum ORGANISM #formal_name Penicillium chrysogenum DATE 23-Apr-1999 #sequence_revision 02-Jun-2000 #text_change 16-Jun-2000 ACCESSIONS A59274; A53651 REFERENCE A59274 !$#authors Segel, I.H. !$#submission submitted to the Protein Sequence Database, May 2000 !$#accession A59274 !'##molecule_type DNA !'##residues 1-573 ##label SEG REFERENCE A53651 !$#authors Foster, B.A.; Thomas, S.M.; Mahr, J.A.; Renosto, F.; Patel, !1H.C.; Segel, I.H. !$#journal J. Biol. Chem. (1994) 269:19777-19786 !$#title Cloning and sequencing of ATP sulfurylase from Penicillium !1chrysogenum. Identification of a likely allosteric domain. !$#cross-references MUID:94327520; PMID:8051058 !$#accession A53651 !'##molecule_type DNA !'##residues 1-368,370-573 ##label FOS !'##cross-references GB:U07353; NID:g460636; PIDN:AAA20839.1; !1PID:g460637 !'##note parts of this sequence were determined by protein sequencing !'##note lacks disulfide bonds COMMENT The enzymatically inactive adenylylsulfate kinase domain !1mediates allosteric feedback inhibition by !13'-phosphoadenosine-5'-phosphosulfate (PAPS). GENETICS !$#gene aps !$#introns 57/1; 66/2; 127/2; 176/1 COMPLEX homohexamer FUNCTION !$#description catalyzes the reaction of sulfate and ATP to form !1adenylylsulfate and pyrophosphate CLASSIFICATION #superfamily Penicillium chrysogenum sulfate !1adenylyltransferase; adenylylsulfate kinase homology; !1sulfate adenylyltransferase homology KEYWORDS cysteine biosynthesis; nucleotidyltransferase FEATURE !$2-391 #domain sulfate adenylyltransferase homology #label !8SAT\ !$396-559 #domain adenylylsulfate kinase homology #label ASK\ !$509 #binding_site 3'-phosphoadenosine-5'-phosphosulfate, !8allosteric (Cys) #status predicted SUMMARY #length 573 #molecular-weight 63973 #checksum 6665 SEQUENCE /// ENTRY S55034 #type complete TITLE sulfate adenylyltransferase (EC 2.7.7.4) - Emericella nidulans ORGANISM #formal_name Emericella nidulans, Aspergillus nidulans DATE 23-Apr-1999 #sequence_revision 23-Apr-1999 #text_change 16-Jun-2000 ACCESSIONS S55034 REFERENCE S55034 !$#authors Borges-Walmsley, M.I.; Turner, G.; Bailey, A.M.; Brown, J.; !1Lehmbeck, J.; Clausen, I.G. !$#journal Mol. Gen. Genet. (1995) 247:423-429 !$#title Isolation and characterisation of genes for sulphate !1activation and reduction in Aspergillus nidulans: !1implications for evolution of an allosteric control region !1by gene duplication. !$#cross-references MUID:95287864; PMID:7770049 !$#accession S55034 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-574 ##label BOR !'##cross-references EMBL:X82541; NID:g572512; PIDN:CAA57891.1; !1PID:g572513 COMMENT The enzymatically inactive adenylylsulfate kinase domain !1mediates allosteric feedback inhibition by !13'-phosphoadenosine-5'-phosphosulfate (PAPS). GENETICS !$#introns 57/1; 66/2; 127/2; 176/1; 199/2 FUNCTION !$#description catalyzes the reaction of sulfate and ATP to form !1adenylylsulfate and pyrophosphate CLASSIFICATION #superfamily Penicillium chrysogenum sulfate !1adenylyltransferase; adenylylsulfate kinase homology; !1sulfate adenylyltransferase homology KEYWORDS cysteine biosynthesis; nucleotidyltransferase FEATURE !$2-391 #domain sulfate adenylyltransferase homology #label !8SAT\ !$396-560 #domain adenylylsulfate kinase homology #label ASK\ !$510 #binding_site 3'-phosphoadenosine-5'-phosphosulfate, !8allosteric (Cys) #status predicted SUMMARY #length 574 #molecular-weight 63922 #checksum 528 SEQUENCE /// ENTRY C70393 #type complete TITLE probable adenylyl-sulfate kinase (EC 2.7.1.25) - Aquifex aeolicus ALTERNATE_NAMES probable PAPS synthetase CONTAINS adenylylsulfate kinase (EC 2.7.1.25); sulfate adenylyltransferase (EC 2.7.7.4) ORGANISM #formal_name Aquifex aeolicus DATE 23-Apr-1999 #sequence_revision 23-Apr-1999 #text_change 03-Jun-2002 ACCESSIONS C70393 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession C70393 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-546 ##label AQF !'##cross-references GB:AE000722; NID:g2983559; PIDN:AAC07134.1; !1PID:g2983561; GB:AE000657 !'##experimental_source strain VF5 COMMENT This protein contains two enzyme homology domains and, in !1contrast to fungal homologs, may have both activities. !1Aquifex retains the P-loop and proposed active site serine !1in the same relative positions as E. coli adenylylsulfate !1kinase. The animal 3'-phosphoadenosine-5'-phosphosulfate !1(PAPS) synthetase superfamily contains the same homology !1domains in the reverse order. GENETICS !$#gene cysD FUNCTION ASKF !$#description as adenylylsulfate kinase catalyzes the phosphorylation of !1adenylylsulfate by ATP to form 3'-phosphoadenylylsulfate and !1ADP FUNCTION SATF !$#description as sulfate adenylyltransferase catalyzes the reaction of !1sulfate and ATP to form adenylylsulfate and pyrophosphate CLASSIFICATION #superfamily Penicillium chrysogenum sulfate !1adenylyltransferase; adenylylsulfate kinase homology; !1sulfate adenylyltransferase homology KEYWORDS multifunctional enzyme; nucleotide binding; !1nucleotidyltransferase; P-loop; phosphoprotein; !1phosphotransferase FEATURE !$2-367 #domain sulfate adenylyltransferase homology #label !8SAT\ !$372-533 #domain adenylylsulfate kinase homology #label ASK\ !$379-386 #region nucleotide-binding motif A (P-loop)\ !$453 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$483 #binding_site 3'-phosphoadenosine-5'-phosphosulfate, !8allosteric (Cys) #status predicted SUMMARY #length 546 #molecular-weight 62787 #checksum 413 SEQUENCE /// ENTRY S55198 #type complete TITLE sulfate adenylyltransferase (EC 2.7.7.4) YJR010w - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES ATP sulfurylase; protein J1436 ORGANISM #formal_name Saccharomyces cerevisiae DATE 19-May-2000 #sequence_revision 19-May-2000 #text_change 21-Jul-2000 ACCESSIONS S55198; S57025; S00906; S40916; S17013 REFERENCE S55183 !$#authors de Haan, M.; Smits, P.H.M.; Grivell, L.A. !$#submission submitted to the EMBL Data Library, May 1995 !$#accession S55198 !'##molecule_type DNA !'##residues 1-511 ##label DEH !'##cross-references EMBL:X87611; NID:g854567; PIDN:CAA60932.1; !1PID:g854583 REFERENCE S56771 !$#authors de Haan, M.; Grivell, L.A.; Smits, P.H.M. !$#submission submitted to the Protein Sequence Database, September 1995 !$#accession S57025 !'##molecule_type DNA !'##residues 1-511 ##label ZAG !'##cross-references EMBL:Z49510; NID:g1015637; PIDN:CAA89532.1; !1PID:g1015638; GSPDB:GN00010; MIPS:YJR010w REFERENCE S00906 !$#authors Cherest, H.; Kerjan, P.; Surdin-Kerjan, Y. !$#journal Mol. Gen. Genet. (1987) 210:307-313 !$#title The Saccharomyces cerevisiae MET3 gene: nucleotide sequence !1and relationship of the 5' non-coding region to that of !1MET25. !$#cross-references MUID:88142548; PMID:3325778 !$#accession S00906 !'##molecule_type DNA !'##residues 1-491,'FHTLYK',498,'LSYSWKTMA',508,'LY',511,'NRHKMLPSQK' !1##label CHE !'##cross-references EMBL:X06413; NID:g3927; PIDN:CAA29702.1; PID:g3928 REFERENCE S40915 !$#authors Mountain, H.A.; Korch, C. !$#journal Yeast (1991) 7:873-880 !$#title TDH2 is linked to MET3 on chromosome X of Saccharomyces !1cerevisiae. !$#cross-references MUID:92160396; PMID:1789010 !$#accession S40916 !'##molecule_type DNA !'##residues 1-491,'FHTLYK',498,'LSYSWKTMA',508,'LY',511,'NRHKMLPSQK' !1##label MOU !'##cross-references EMBL:X60157; NID:g3935; PIDN:CAA42726.1; PID:g3937 GENETICS !$#gene SGD:MET3; MIPS:YJR010w !'##cross-references SGD:S0003771; MIPS:YJR010w !$#map_position 10R FUNCTION !$#description catalyzes the reaction of sulfate and ATP to form !1adenylylsulfate and pyrophosphate !$#pathway sulfur metabolism CLASSIFICATION #superfamily yeast sulfate adenylyltransferase; sulfate !1adenylyltransferase homology KEYWORDS cysteine biosynthesis; nucleotidyltransferase FEATURE !$1-390 #domain sulfate adenylyltransferase homology #label !8SAT SUMMARY #length 511 #molecular-weight 57724 #checksum 5637 SEQUENCE /// ENTRY YGECEF #type complete TITLE enterobactin synthetase component F - Escherichia coli (strain K-12) ALTERNATE_NAMES enterochelin synthetase component F CONTAINS (2,3-dihydroxybenzoyl)serine O-[(2,3-dihydroxybenzoyl)seryl] transferase (EC 2.3.1.-) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1991 #sequence_revision 14-Nov-1997 #text_change 01-Mar-2002 ACCESSIONS H64791; B38408; C31958; I41195 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64791 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1293 ##label BLAT !'##cross-references GB:AE000164; GB:U00096; NID:g1786800; !1PIDN:AAC73687.1; PID:g1786801; UWGP:b0586 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A38408 !$#authors Rusnak, F.; Sakaitani, M.; Drueckhammer, D.; Reichert, J.; !1Walsh, C.T. !$#journal Biochemistry (1991) 30:2916-2927 !$#title Biosynthesis of the Escherichia coli siderophore !1enterobactin: sequence of the entF gene, expression and !1purification of EntF, and analysis of covalent !1phosphopantetheine. !$#cross-references MUID:91175738; PMID:1826089 !$#accession B38408 !'##molecule_type DNA !'##residues 1-440,'HV',443-1293 ##label RUS !'##cross-references GB:M60177; GB:J05325; NID:g145842; PIDN:AAA92015.1; !1PID:g145843 REFERENCE A31958 !$#authors Pettis, G.S.; Brickman, T.J.; McIntosh, M.A. !$#journal J. Biol. Chem. (1988) 263:18857-18863 !$#title Transcriptional mapping and nucleotide sequence of the !1Escherichia coli fepA-fes enterobactin region. !1Identification of a unique iron-regulated bidirectional !1promoter. !$#cross-references MUID:89066678; PMID:2974033 !$#accession C31958 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-34 ##label PET1 !'##cross-references GB:J04216; NID:g145916; PIDN:AAA23759.1; !1PID:g551803 REFERENCE I41195 !$#authors Pettis, G.S.; McIntosh, M.A. !$#journal J. Bacteriol. (1987) 169:4154-4162 !$#title Molecular characterization of the Escherichia coli !1enterobactin cistron entF and coupled expression of entF and !1the fes gene. !$#cross-references MUID:87307997; PMID:3040679 !$#accession I41195 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-34 ##label PET2 !'##cross-references GB:M17354; NID:g145844; PIDN:AAA23727.1; !1PID:g551801 COMMENT Enterobactin is a catechol-containing siderophore that binds !1iron(III) ion for transport. GENETICS !$#gene entF !$#map_position 14 min FUNCTION !$#description forms enteroabactin from three molecules of (2, !13-dihydroxybenzoyl)serine by catalyzing the !1O3-esterification of (2,3-dihydroxybenzoyl)serine groups by !1(2,3-dihydroxybenzoyl)seryl-carrier protein !$#pathway enterobactin biosynthesis CLASSIFICATION #superfamily enterobactin synthetase component F; !1acetate-CoA ligase homology; acyl carrier protein homology KEYWORDS acyltransferase; carrier protein; enterobactin biosynthesis; !1iron transport; phosphopantetheine; phosphoprotein FEATURE !$501-958 #domain acetate-CoA ligase homology #label ACL\ !$974-1042 #domain acyl carrier protein homology #label ACP\ !$1006 #binding_site phosphopantetheine (Ser) (covalent) !8#status predicted SUMMARY #length 1293 #molecular-weight 141989 #checksum 5088 SEQUENCE /// ENTRY E69615 #type complete TITLE enterobactin synthetase component dhbF - Bacillus subtilis ALTERNATE_NAMES enterochelin synthetase component F CONTAINS (2,3-dihydroxybenzoyl)serine O-[(2,3-dihydroxybenzoyl)seryl] transferase (EC 2.3.1.-) ORGANISM #formal_name Bacillus subtilis DATE 05-Dec-1997 #sequence_revision 10-Jul-1998 #text_change 03-Nov-2000 ACCESSIONS E69615 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69615 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1278 ##label KUN !'##cross-references GB:Z99120; GB:AL009126; NID:g2635613; !1PIDN:CAB15186.1; PID:g2635693 !'##experimental_source strain 168 GENETICS !$#gene dhbF FUNCTION !$#description forms enteroabactin from three molecules of (2, !13-dihydroxybenzoyl)serine by catalyzing the !1O3-esterification of (2,3-dihydroxybenzoyl)serine groups by !1(2,3-dihydroxybenzoyl)seryl-carrier protein !$#pathway enterobactin biosynthesis CLASSIFICATION #superfamily enterobactin synthetase component F; !1acetate-CoA ligase homology; acyl carrier protein homology KEYWORDS acyltransferase; carrier protein; enterobactin biosynthesis; !1iron transport; phosphopantetheine; phosphoprotein; !1transmembrane protein FEATURE !$504-948 #domain acetate-CoA ligase homology #label ACL\ !$964-1032 #domain acyl carrier protein homology #label ACP\ !$996 #binding_site phosphopantetheine (Ser) (covalent) !8#status predicted SUMMARY #length 1278 #molecular-weight 142067 #checksum 2747 SEQUENCE /// ENTRY YGVCAR #type complete TITLE angR protein - Vibrio anguillarum ORGANISM #formal_name Vibrio anguillarum DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 03-Nov-2000 ACCESSIONS JQ0416; S26421 REFERENCE JQ0416 !$#authors Farrell, D.H.; Mikesell, P.; Actis, L.A.; Crosa, J.H. !$#journal Gene (1990) 86:45-51 !$#title A regulatory gene, angR, of the iron uptake system of Vibrio !1anguillarum: similarity with phage P22 cro and regulation by !1iron. !$#cross-references MUID:90185247; PMID:2311935 !$#accession JQ0416 !'##molecule_type DNA !'##residues 1-1048 ##label FAR !'##cross-references GB:M34504; NID:g155150; PIDN:AAA79860.1; !1PID:g155152 REFERENCE S26421 !$#authors Tolmasky, M.E.; Actis, L.A.; Waldbeser, L.S.; Crosa, J.H. !$#submission submitted to the EMBL Data Library, April 1992 !$#description Genetic characterization of the regulatory protein AngR: !1presence of leucine zippers and evidence for a biosynthetic !1function. !$#accession S26421 !'##status preliminary !'##molecule_type DNA !'##residues 1-266,'N',268-1048 ##label TOL !'##cross-references EMBL:Z12000; NID:g48322; PIDN:CAA78044.1; !1PID:g48323 COMMENT Vibrio anguillarum, a pathogenic bacterium, causes !1vibriosis, a widespread septicemic disease in marine fish. COMMENT This protein functions as a trans-acting transcriptional !1activator. It may be an enzyme involved in the biosynthesis !1of anguibactin, an iron-binding siderophore. GENETICS !$#gene angR CLASSIFICATION #superfamily Vibrio angR protein; acetate-CoA ligase !1homology; acyl carrier protein homology KEYWORDS carrier protein; DNA binding; iron transport; transcription !1regulation FEATURE !$499-948 #domain acetate-CoA ligase homology #label ACL\ !$968-1035 #domain acyl carrier protein homology #label ACP SUMMARY #length 1048 #molecular-weight 118420 #checksum 7053 SEQUENCE /// ENTRY YGBYAD #type complete TITLE L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES alpha-aminoadipate reductase; protein YBR0910; protein YBR115c ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 03-Nov-2000 ACCESSIONS JU0448; S48279; S45983; A25815; S37810; S25367; S34171; !1S44694 REFERENCE JU0448 !$#authors Morris, M.E.; Jinks-Robertson, S. !$#journal Gene (1991) 98:141-145 !$#title Nucleotide sequence of the LYS2 gene of Saccharomyces !1cerevisiae: homology to Bacillus brevis tyrocidine !1synthetase 1. !$#cross-references MUID:91192607; PMID:2013406 !$#accession JU0448 !'##molecule_type DNA !'##residues 1-1392 ##label MOR !'##cross-references GB:M36287; NID:g171866; PIDN:AAA34747.1; !1PID:g171867 REFERENCE S48255 !$#authors Mannhaupt, G.; Stucka, R.; Ehnle, S.; Vetter, I.; Feldmann, !1H. !$#journal Yeast (1994) 10:1363-1381 !$#title Analysis of a 70 kb region on the right arm of yeast !1chromosome II. !$#cross-references MUID:95208357; PMID:7900426 !$#accession S48279 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1392 ##label MAW !'##cross-references EMBL:X78993; NID:g476045; PIDN:CAA55617.1; !1PID:g476070 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1994 REFERENCE S45927 !$#authors Feldmann, H.; Mannhaupt, G.; Schwarzlose, C.; Vetter, I. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S45983 !'##molecule_type DNA !'##residues 1-1392 ##label FE2 !'##cross-references EMBL:Z35984; NID:g536454; PIDN:CAA85072.1; !1PID:g536455; GSPDB:GN00002; MIPS:YBR115c REFERENCE A25815 !$#authors Fleig, U.N.; Pridmore, R.D.; Philippsen, P. !$#journal Gene (1986) 46:237-245 !$#title Construction of LYS2 cartridges for use in manipulations of !1Saccharomyces cerevisiae. !$#cross-references MUID:87106859; PMID:3542721 !$#accession A25815 !'##molecule_type DNA !'##residues 1-151;1210-1392 ##label FLE !'##cross-references EMBL:M14967; EMBL:M14968 REFERENCE S37808 !$#authors Schaaff-Gerstenschlaeger, I.; Mannhaupt, G.; Vetter, I.; !1Zimmermann, F.K.; Feldmann, H. !$#journal Eur. J. Biochem. (1993) 217:487-492 !$#title TKL2, a second transketolase gene of Saccharomyces !1cerevisiae. Cloning, sequence and deletion analysis of the !1gene. !$#cross-references MUID:94039074; PMID:7916691 !$#accession S37810 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-130 ##label SCH !'##cross-references EMBL:X73532; NID:g313260; PIDN:CAA51938.1; !1PID:g313263 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1993 REFERENCE S25364 !$#authors Mannhaupt, G.; Stucka, R.; Ehnle, S.; Vetter, I.; Feldmann, !1H. !$#journal Yeast (1992) 8:397-408 !$#title Molecular analysis of yeast chromosome II between CMD1 and !1LYS2: the excision repair gene RAD16 located in this region !1belongs to a novel group of double-finger proteins. !$#cross-references MUID:92327848; PMID:1626431 !$#accession S25367 !'##molecule_type DNA !'##residues 1083-1392 ##label MAN !'##cross-references EMBL:X66247; NID:g3548; PIDN:CAA46975.1; PID:g3552 COMMENT This enzyme catalyzes the activation of 2-aminoadipate by !1ATP-dependent adenylation, and the reduction of activated !12-aminoadipate. Together with lys5 protein, it catalyzes the !1overall interconversion of 2-aminoadipate and !12-aminoadipic-2-semialdehyde. It may be a component of the !1enzyme complex L-aminoadipate-semialdehyde dehydrogenase (EC !11.2.1.31). GENETICS !$#gene SGD:LYS2; MIPS:YBR115c !'##cross-references SGD:S0000319; MIPS:YBR115c !$#map_position 2R CLASSIFICATION #superfamily Saccharomyces lys2 protein; acetate-CoA ligase !1homology; acyl carrier protein homology KEYWORDS carrier protein; lysine biosynthesis; oxidoreductase; !1phosphopantetheine; phosphoprotein; transmembrane protein FEATURE !$55-71 #domain transmembrane #status predicted #label TM1\ !$290-821 #domain acetate-CoA ligase homology #label ACL\ !$307-324 #domain transmembrane #status predicted #label TM2\ !$846-916 #domain acyl carrier protein homology #label ACP2\ !$971-987 #domain transmembrane #status predicted #label TM3\ !$880 #binding_site phosphopantetheine (Ser) (covalent) !8#status predicted SUMMARY #length 1392 #molecular-weight 155344 #checksum 5237 SEQUENCE /// ENTRY SYECQA #type complete TITLE quinolinate synthetase nadA [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS F64810; S01131 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64810 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-347 ##label BLAT !'##cross-references GB:AE000177; GB:U00096; NID:g1786955; !1PIDN:AAC73837.1; PID:g1786964; UWGP:b0750 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S01131 !$#authors Flachmann, R.; Kunz, N.; Seifert, J.; Guetlich, M.; !1Wientjes, F.J.; Laeufer, A.; Gassen, H.G. !$#journal Eur. J. Biochem. (1988) 175:221-228 !$#title Molecular biology of pyridine nucleotide biosynthesis in !1Escherichia coli: cloning and characterization of !1quinolinate synthesis genes nadA and nadB. !$#cross-references MUID:88296484; PMID:2841129 !$#accession S01131 !'##molecule_type DNA !'##residues 'M',44-152,'G',154-169,'C',171-303,'A',305,'GHR',346-347, !1'IRTGRKQSRGSC' ##label FLA !'##cross-references GB:X12713; NID:g42074; PIDN:CAA31216.1; PID:g581137 GENETICS !$#gene nadA; nicA !$#map_position 17 min COMPLEX heterodimer FUNCTION !$#description catalyzes condensation of the intermediate iminoaspartate, !1the reaction product of nadB (PIR:OXECLD), with !1dihydroxyacetone phosphate to quinolinate [validated, !1MUID:88296484] !$#note one of two components of the quinolinate synthetase complex, !1consisting of nadA and nadB !$#note quinolinate (pyridine-2,3-dicarboxylate) is the biosynthetic !1precursor of the pyridine ring of NAD CLASSIFICATION #superfamily quinolinate synthetase A KEYWORDS cytosol; pyridine nucleotide biosynthesis SUMMARY #length 347 #molecular-weight 38240 #checksum 456 SEQUENCE /// ENTRY SYECBB #type complete TITLE biotin synthase (EC 2.8.1.6) bioB [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES bioB protein ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS JC2517; G64813; C32025; S78778 REFERENCE JC2517 !$#authors Ifuku, O.; Koga, N.; Haze, S.; Kishimoto, J.; Arai, T.; !1Wachi, Y. !$#journal Biosci. Biotechnol. Biochem. (1995) 59:184-189 !$#title Molecular analysis of growth inhibition caused by !1overexpression of the biotin operon in Escherichia coli. !$#cross-references MUID:95218259; PMID:7766016 !$#accession JC2517 !'##molecule_type DNA !'##residues 1-346 ##label IFU !'##experimental_source DRK 3323 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64813 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-346 ##label BLAT !'##cross-references GB:AE000180; GB:U00096; NID:g1786988; !1PIDN:AAC73862.1; PID:g1786992; UWGP:b0775 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A32025 !$#authors Otsuka, A.J.; Buoncristiani, M.R.; Howard, P.K.; Flamm, J.; !1Johnson, C.; Yamamoto, R.; Uchida, K.; Cook, C.; Ruppert, !1J.; Matsuzaki, J. !$#journal J. Biol. Chem. (1988) 263:19577-19585 !$#title The Escherichia coli biotin biosynthetic enzyme sequences !1predicted from the nucleotide sequence of the bio operon. !$#cross-references MUID:89066784; PMID:3058702 !$#accession C32025 !'##molecule_type DNA !'##residues 1-62,'T',64-346 ##label OTS !'##cross-references GB:J04423; NID:g145422; PIDN:AAA23515.1; !1PID:g145425 REFERENCE S78778 !$#authors Sanyal, I.; Cohen, G.; Flint, D.H. !$#journal Biochemistry (1994) 33:3625-3631 !$#title Biotin synthase: purification, characterization as a !1[2Fe-2S]cluster protein, and in vitro activity of the !1Escherichia coli bioB gene product. !$#cross-references MUID:94190882; PMID:8142361 !$#accession S78778 !'##molecule_type protein !'##residues 1-17 ##label SAN GENETICS !$#gene bioB !$#map_position 17 min FUNCTION !$#description catalyzes conversion of dethiobiotin to biotin !$#pathway biotin biosynthesis !$#note last step CLASSIFICATION #superfamily biotin synthetase KEYWORDS 2Fe-2S; biotin biosynthesis; iron-sulfur protein; !1metalloprotein; sulfurtransferase FEATURE !$1-346 #product biotin synthetase #status experimental !8#label MAT\ !$53,57,60,188 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 346 #molecular-weight 38648 #checksum 7197 SEQUENCE /// ENTRY JC5006 #type complete TITLE biotin synthase (EC 2.8.1.6) bioB [similarity] - Erwinia herbicola ORGANISM #formal_name Erwinia herbicola DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 20-Oct-2000 ACCESSIONS JC5006 REFERENCE JC5005 !$#authors Wu, C.H.; Chen, H.Y.; Shiuan, D. !$#journal Gene (1996) 174:251-258 !$#title Isolation and characterization of the Erwinia herbicola bio !1operon and the sequences of the bioA and bioB genes. !$#cross-references MUID:97045821; PMID:8890743 !$#accession JC5006 !'##molecule_type DNA !'##residues 1-346 ##label WUA !'##cross-references GB:U38648; NID:g1228112; PIDN:AAC44534.1; !1PID:g1228114 !'##note the authors translated the codon ACC for residue 50 as Ile and !1ACG for residue 198 as Ile GENETICS !$#gene bioB FUNCTION !$#description catalyzes the conversion of dethiobiotin to biotin !$#pathway biotin biosynthesis CLASSIFICATION #superfamily biotin synthetase KEYWORDS 2Fe-2S; biotin biosynthesis; iron-sulfur protein; !1metalloprotein; sulfurtransferase FEATURE !$53,57,60,188 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 346 #molecular-weight 38714 #checksum 5657 SEQUENCE /// ENTRY JC5083 #type complete TITLE biotin synthase (EC 2.8.1.6) bioB [validated] - Methylobacillus sp. (strain flagellatum) ORGANISM #formal_name Methylobacillus sp. #variety strain flagellatum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 20-Oct-2000 ACCESSIONS JC5083 REFERENCE JC5083 !$#authors Serebriiskii, I.G.; Vassin, V.M.; Tsygankov, Y.D. !$#journal Gene (1996) 175:15-22 !$#title Two new members of the BioB superfamily: Cloning, sequencing !1and expression of bioB genes of Methylobacillus flagellatum !1and Corynebacterium glutamicum. !$#cross-references MUID:97074643; PMID:8917070 !$#accession JC5083 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-332 ##label SER !'##cross-references GB:U31280 !'##experimental_source Methylobacillus flagellatum !'##note the source is designated as Methylobacillus flagellatum GENETICS !$#gene bioB FUNCTION !$#description catalyzes conversion of dethiobiotin to biotin !$#pathway biotin biosynthesis !$#note last step CLASSIFICATION #superfamily biotin synthetase KEYWORDS 2Fe-2S; biotin biosynthesis; iron-sulfur protein; !1metalloprotein; sulfurtransferase FEATURE !$75,79,82,207 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 332 #molecular-weight 37261 #checksum 1727 SEQUENCE /// ENTRY I40338 #type complete TITLE biotin synthase (EC 2.8.1.6) bioB [similarity] - Corynebacterium glutamicum ORGANISM #formal_name Corynebacterium glutamicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 20-Oct-2000 ACCESSIONS I40338 REFERENCE I40338 !$#authors Hatakeyama, K.; Kohama, K.; Vertes, A.A.; Kobayashi, M.; !1Kurusu, Y.; Yukawa, H. !$#journal DNA Seq. (1993) 4:87-93 !$#title Analysis of the biotin biosynthesis pathway in coryneform !1bacteria: cloning and sequencing of the bioB gene from !1Brevibacterium flavum. !$#cross-references MUID:94227249; PMID:8173080 !$#accession I40338 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-334 ##label RES !'##cross-references GB:D14084; NID:g505064; PIDN:BAA03169.1; !1PID:g538222 GENETICS !$#gene bioB CLASSIFICATION #superfamily biotin synthetase KEYWORDS 2Fe-2S; biotin biosynthesis; iron-sulfur protein; !1metalloprotein; sulfurtransferase FEATURE !$70,74,77,205 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 334 #molecular-weight 36724 #checksum 2911 SEQUENCE /// ENTRY JS0274 #type complete TITLE biotin synthase (EC 2.8.1.6) bioB [validated] - Bacillus sphaericus ORGANISM #formal_name Bacillus sphaericus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 20-Oct-2000 ACCESSIONS JS0274 REFERENCE A91617 !$#authors Ohsawa, I.; Speck, D.; Kisou, T.; Hayakawa, K.; Zinsius, M.; !1Gloeckler, R.; Lemoine, Y.; Kamogawa, K. !$#journal Gene (1989) 80:39-48 !$#title Cloning of the biotin synthetase gene from Bacillus !1sphaericus and expression in Escherichia coli and Bacilli. !$#cross-references MUID:90006784; PMID:2507401 !$#accession JS0274 !'##molecule_type DNA !'##residues 1-332 ##label OHS !'##cross-references GB:M27867; NID:g341784; PIDN:AAA22268.1; !1PID:g520750 !'##experimental_source strain T-178-367 !'##note the sequence of the amino end was confirmed by protein !1sequencing COMMENT This protein catalyzes the biotransformation of dethiobiotin !1to biotin. GENETICS !$#gene bioB !$#start_codon GTG CLASSIFICATION #superfamily biotin synthetase KEYWORDS 2Fe-2S; biotin biosynthesis; iron-sulfur protein; !1metalloprotein; sulfurtransferase FEATURE !$64,68,71,200 #binding_site 2Fe-2S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 332 #molecular-weight 37015 #checksum 7088 SEQUENCE /// ENTRY TIHUGK #type complete TITLE tissue factor pathway inhibitor precursor [validated] - human ALTERNATE_NAMES extrinsic pathway inhibitor; lipoprotein-associated coagulation inhibitor ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 08-Dec-2000 ACCESSIONS A23712; A39176; A28650; A60433; B60433; S13034; A34315; !1A38294; S03903 REFERENCE A23712 !$#authors Girard, T.J.; Eddy, R.; Wesselschmidt, R.L.; MacPhail, L.A.; !1Likert, K.M.; Byers, M.G.; Shows, T.B.; Broze Jr., G.J. !$#journal J. Biol. Chem. (1991) 266:5036-5041 !$#title Structure of the human lipoprotein-associated coagulation !1inhibitor gene. Intro/exon gene organization and !1localization of the gene to chromosome 2. !$#cross-references MUID:91161593; PMID:2002045 !$#accession A23712 !'##molecule_type DNA !'##residues 1-304 ##label GIR !'##cross-references GB:M59493; GB:M59499; NID:g187204; PIDN:AAA59526.1; !1PID:g187206 REFERENCE A39176 !$#authors van der Logt, C.P.E.; Reitsma, P.H.; Bertina, R.M. !$#journal Biochemistry (1991) 30:1571-1577 !$#title Intron-exon organization of the human gene coding for the !1lipoprotein-associated coagulation inhibitor: the factor Xa !1dependent inhibitor of the extrinsic pathway of coagulation. !$#cross-references MUID:91129227; PMID:1993173 !$#accession A39176 !'##molecule_type DNA !'##residues 1-304 ##label VAN !'##cross-references GB:M58650; GB:J05312; NID:g186827; PIDN:AAA59480.1; !1PID:g186829 REFERENCE A28650 !$#authors Wun, T.C.; Kretzmer, K.K.; Girard, T.J.; Miletich, J.P.; !1Broze Jr., G.J. !$#journal J. Biol. Chem. (1988) 263:6001-6004 !$#title Cloning and characterization of a cDNA coding for the !1lipoprotein-associated coagulation inhibitor shows that it !1consists of three tandem kunitz-type inhibitory domains. !$#cross-references MUID:88198127; PMID:2452157 !$#accession A28650 !'##molecule_type mRNA !'##residues 1-304 ##label WUN !'##cross-references GB:J03225; NID:g180545; PIDN:AAA52022.1; !1PID:g180546 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE A60433 !$#authors Girard, T.J.; Warren, L.A.; Novotny, W.F.; Bejcek, B.E.; !1Miletich, J.P.; Broze Jr., G.J. !$#journal Thromb. Res. (1989) 55:37-50 !$#title Identification of the 1.4 KB and 4.0 KB messages for the !1lipoprotein associated coagulation inhibitor and expression !1of the encoded protein. !$#cross-references MUID:89388722; PMID:2781520 !$#accession A60433 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-304 ##label GI2 !'##experimental_source endothelial cells !$#accession B60433 !'##molecule_type protein !'##residues 'XX',31-53,'X',55-56 ##label GI3 !'##experimental_source recombinant material from mouse C137 cells REFERENCE S13034 !$#authors Girard, T.J.; McCourt, D.; Novotny, W.F.; MacPhail, L.A.; !1Likert, K.M.; Broze Jr., G.J. !$#journal Biochem. J. (1990) 270:621-625 !$#title Endogenous phosphorylation of the lipoprotein-associated !1coagulation inhibitor at serine-2. !$#cross-references MUID:91054349; PMID:2122883 !$#accession S13034 !'##molecule_type protein !'##residues 29-35 ##label GI4 REFERENCE A34315 !$#authors Novotny, W.F.; Girard, T.J.; Miletich, J.P.; Broze Jr., G.J. !$#journal J. Biol. Chem. (1989) 264:18832-18837 !$#title Purification and characterization of the !1lipoprotein-associated coagulation inhibitor from human !1plasma. !$#cross-references MUID:90036996; PMID:2553722 !$#accession A34315 !'##molecule_type protein !'##residues 'XX',31-33,'L',35-50 ##label NOV !'##experimental_source plasma REFERENCE A38294 !$#authors Pedersen, A.H.; Nordfang, O.; Norris, F.; Wiberg, F.C.; !1Christensen, P.M.; Moeller, K.B.; Meidahl-Pedersen, J.; !1Beck, T.C.; Norris, K.; Hedner, U.; Kisiel, W. !$#journal J. Biol. Chem. (1990) 265:16786-16793 !$#title Recombinant human extrinsic pathway inhibitor. Production, !1isolation, and characterization of its inhibitory activity !1on tissue factor-initiated coagulation reactions. !$#cross-references MUID:91009092; PMID:2211593 !$#accession A38294 !'##molecule_type protein !'##residues 29-41 ##label PED REFERENCE S03903 !$#authors Girard, T.J.; Warren, L.A.; Novotny, W.F.; Likert, K.M.; !1Brown, S.G.; Miletich, J.P.; Broze Jr., G.J. !$#journal Nature (1989) 338:518-520 !$#title Functional significance of the Kunitz-type inhibitory !1domains of lipoprotein-associated coagulation inhibitor. !$#cross-references MUID:89181950; PMID:2927510 !$#contents annotation; site-directed mutagenesis COMMENT The first Kunitz-type domain binds the factor VIIa/tissue !1factor complex; the second binds factor Xa. GENETICS !$#gene GDB:TFPI !'##cross-references GDB:127364; OMIM:152310 !$#map_position 2q32-2q32 !$#introns 41/1; 107/1; 120/1; 179/1; 210/1; 270/1 FUNCTION !$#description regulates clotting by factor Xa-dependent inhibition of the !1coagulation factor VIIa/tissue factor complex !$#pathway blood coagulation CLASSIFICATION #superfamily tissue factor pathway inhibitor; animal !1Kunitz-type proteinase inhibitor homology KEYWORDS anticoagulant; blood coagulation; duplication; glycoprotein; !1heparin binding; phosphoprotein; serine proteinase inhibitor FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-304 #product tissue factor pathway inhibitor #status !8experimental #label MAT\ !$54-104 #domain animal Kunitz-type proteinase inhibitor !8homology #label BP1\ !$125-175 #domain animal Kunitz-type proteinase inhibitor !8homology #label BP2\ !$217-267 #domain animal Kunitz-type proteinase inhibitor !8homology #label BP3\ !$284-289 #region heparin binding #status predicted\ !$30 #binding_site phosphate (Ser) (covalent) #status !8experimental\ !$54-104,63-87, !$79-100,125-175, !$134-158,150-171, !$217-267,226-250, !$242-263 #disulfide_bonds #status predicted\ !$64 #inhibitory_site Lys (coagulation factor VII/tissue !8factor complex) #status experimental\ !$135 #inhibitory_site Arg (coagulation factor X) #status !8experimental\ !$145,195,256 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$227 #inhibitory_site Arg (unidentified proteinase) !8#status predicted SUMMARY #length 304 #molecular-weight 35015 #checksum 5312 SEQUENCE /// ENTRY JC2264 #type complete TITLE tissue factor pathway inhibitor precursor - rhesus macaque ALTERNATE_NAMES extrinsic pathway inhibitor; lipoprotein-associated coagulation inhibitor ORGANISM #formal_name Macaca mulatta #common_name rhesus macaque DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS JC2264 REFERENCE JC2264 !$#authors Kamei, S.; Kamikubo, Y.; Hamuro, T.; Fujimoto, H.; Ishihara, !1M.; Yonemura, H.; Miyamoto, S.; Funatsu, A.; Enjyoji, K.; !1Abumiya, T.; Miyata, T.; Kato, H. !$#journal J. Biochem. (1994) 115:708-714 !$#title Amino acid sequence and inhibitory activity of rhesus monkey !1tissue factor pathway inhibitor (TFPI): comparison with !1human TFPI. !$#cross-references MUID:94375417; PMID:8089087 !$#accession JC2264 !'##molecule_type mRNA !'##residues 1-304 ##label KAM !'##cross-references GB:S73337; NID:g685016; PIDN:AAB31955.1; !1PID:g685017 !'##experimental_source liver COMMENT This protein inhibits the activities of factor Xa and tissue !1factor-factor VIIa complex. CLASSIFICATION #superfamily tissue factor pathway inhibitor; animal !1Kunitz-type proteinase inhibitor homology KEYWORDS anticoagulant; glycoprotein; serine proteinase inhibitor FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-304 #product tissue factor pathway inhibitor #status !8predicted #label MAT\ !$54-104 #domain animal Kunitz-type proteinase inhibitor !8homology #label BP1\ !$125-175 #domain animal Kunitz-type proteinase inhibitor !8homology #label BP2\ !$217-267 #domain animal Kunitz-type proteinase inhibitor !8homology #label BP3\ !$54-104,63-87, !$79-100,125-175, !$134-158,150-171, !$217-267,226-250, !$242-263 #disulfide_bonds #status predicted\ !$64 #inhibitory_site Lys (coagulation factor VII/tissue !8factor complex) #status predicted\ !$135 #inhibitory_site Arg (coagulation factor X) #status !8predicted\ !$145,195,256 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$227 #inhibitory_site Arg (unidentified proteinase) !8#status predicted SUMMARY #length 304 #molecular-weight 35085 #checksum 6813 SEQUENCE /// ENTRY TIRTGK #type complete TITLE tissue factor pathway inhibitor precursor - rat ALTERNATE_NAMES extrinsic pathway inhibitor; lipoprotein-associated coagulation inhibitor ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jun-2000 ACCESSIONS JX0213 REFERENCE JX0213 !$#authors Enjyoji, K.; Emi, M.; Mukai, T.; Kato, H. !$#journal J. Biochem. (1992) 111:681-687 !$#title cDNA cloning and expression of rat tissue factor pathway !1inhibitor (TFPI). !$#cross-references MUID:92348361; PMID:1639767 !$#accession JX0213 !'##molecule_type mRNA !'##residues 1-302 ##label ENJ !'##cross-references DDBJ:D10926; NID:g220916; PIDN:BAA01724.1; !1PID:g220917 !'##experimental_source liver COMMENT This serine proteinase inhibitor regulates clotting by !1factor Xa-dependent inhibition of the coagulation factor !1VIIa/tissue factor complex. COMMENT The first Kunitz-type domain binds the factor VIIa/tissue !1factor complex; the second binds factor Xa. CLASSIFICATION #superfamily tissue factor pathway inhibitor; animal !1Kunitz-type proteinase inhibitor homology KEYWORDS anticoagulant; blood coagulation; duplication; glycoprotein; !1heparin binding; serine proteinase inhibitor FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-302 #product tissue factor pathway inhibitor #status !8predicted #label MAT\ !$53-103 #domain animal Kunitz-type proteinase inhibitor !8homology #label BP1\ !$124-174 #domain animal Kunitz-type proteinase inhibitor !8homology #label BP2\ !$222-272 #domain animal Kunitz-type proteinase inhibitor !8homology #label BP3\ !$288-291 #region heparin binding #status predicted\ !$53-103,62-86,78-99, !$124-174,133-157, !$149-170,222-272, !$231-255,247-268 #disulfide_bonds #status predicted\ !$63 #inhibitory_site Lys (coagulation factor VII/tissue !8factor complex) #status predicted\ !$134 #inhibitory_site Arg (coagulation factor X) #status !8predicted\ !$144,251,261 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$232 #inhibitory_site Lys (unidentified proteinase) !8#status predicted SUMMARY #length 302 #molecular-weight 34554 #checksum 9138 SEQUENCE /// ENTRY TIBO #type complete TITLE basic proteinase inhibitor precursor - bovine ALTERNATE_NAMES aprotinin; basic pancreatic trypsin inhibitor; BPTI; cationic kallikrein inhibitor; inhibitor IV ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 24-Apr-1984 #sequence_revision 22-Jul-1994 #text_change 16-Jun-2000 ACCESSIONS S00277; A30333; S10546; S02486; S28197; A90162; A92023; !1A90736; A90927; A34658; A93977; S10062; A01205 REFERENCE S00274 !$#authors Creighton, T.E.; Charles, I.G. !$#journal J. Mol. Biol. (1987) 194:11-22 !$#title Sequences of the genes and polypeptide precursors for two !1bovine protease inhibitors. !$#cross-references MUID:87283904; PMID:2441071 !$#accession S00277 !'##molecule_type DNA; mRNA !'##residues 1-100 ##label CR2 !'##cross-references GB:M20934; GB:X05274; NID:g162767; PIDN:AAD13685.1; !1PID:g162769 REFERENCE A90926 !$#authors Creighton, T.E.; Charles, I.G. !$#journal Cold Spring Harb. Symp. Quant. Biol. (1987) 52:511-519 !$#title Biosynthesis, processing, and evolution of bovine pancreatic !1trypsin inhibitor. !$#cross-references MUID:88295740; PMID:2456884 !$#accession A30333 !'##molecule_type DNA !'##residues 1-100 ##label CRE !'##cross-references GB:M20934; GB:X05274; NID:g162767; PIDN:AAD13685.1; !1PID:g162769 REFERENCE S10546 !$#authors Kingston, I.B.; Anderson, S. !$#journal Biochem. J. (1986) 233:443-450 !$#title Sequences encoding two trypsin inhibitors occur in !1strikingly similar genomic environments. !$#cross-references MUID:86158754; PMID:2420326 !$#accession S10546 !'##molecule_type DNA !'##residues 34-97 ##label KIN REFERENCE S02485 !$#authors Fioretti, E.; Angeletti, M.; Fiorucci, L.; Barra, D.; Bossa, !1F.; Ascoli, F. !$#journal Biol. Chem. Hoppe-Seyler (1988) 369(Suppl.):37-42 !$#title Aprotinin-like isoinhibitors in bovine organs. !$#cross-references MUID:89076531; PMID:2462435 !$#accession S02486 !'##molecule_type protein !'##residues 36-93 ##label FIO REFERENCE S28197 !$#authors Ikekita, M.; Jone, C.S.; Kamo, M.; Tsugita, A.; Kizuki, K.; !1Moriya, H. !$#journal Protein Seq. Data Anal. (1992) 5:7-11 !$#title Purification and characterization of the major cationic !1kallikrein inhibitor in bovine pituitary gland. !$#cross-references MUID:93150003; PMID:1283464 !$#accession S28197 !'##molecule_type protein !'##residues 36-93 ##label IKE REFERENCE A90162 !$#authors Kassell, B.; Laskowski, M. !$#journal Biochem. Biophys. Res. Commun. (1965) 20:463-468 !$#title The basic trypsin inhibitor of bovine pancreas. V. The !1disulfide linkages. !$#cross-references MUID:66083012; PMID:5860161 !$#contents annotation; disulfide bonds !$#accession A90162 !'##molecule_type protein !'##residues 36-93 ##label KAS REFERENCE A92023 !$#authors Anderer, F.A.; Hornle, S. !$#journal J. Biol. Chem. (1966) 241:1568-1572 !$#title The disulfide linkages in kallikrein inactivator of bovine !1lung. !$#cross-references MUID:66171231; PMID:5296424 !$#contents annotation; disulfide bonds !$#accession A92023 !'##molecule_type protein !'##residues 36-93 ##label AN2 REFERENCE A90736 !$#authors Chauvet, J.; Acher, R. !$#journal Bull. Soc. Chim. Biol. (1967) 49:985-1000 !$#title La structure covalente d'un inhibiteur polypeptidique de la !1trypsine (inhibiteur de Kunitz et Northrop). !$#cross-references MUID:68012003; PMID:6053284 !$#contents annotation; disulfide bonds !$#accession A90736 !'##molecule_type protein !'##residues 36-93 ##label CHA REFERENCE A90927 !$#authors Dlouha, V.; Pospisilova, D.; Meloun, B.; Sorm, F. !$#journal Collect. Czech. Chem. Commun. (1968) 33:1363-1365 !$#title Sequence of residues 18-20 in pancreatic trypsin inhibitor. !$#accession A90927 !'##molecule_type protein !'##residues 36-93 ##label DLO REFERENCE A93410 !$#authors Huber, R.; Kukla, D.; Ruhlmann, A.; Epp, O.; Formanek, H. !$#journal Naturwissenschaften (1970) 57:389-392 !$#title The basic trypsin inhibitor of bovine pancreas. I. Structure !1analysis and conformation of the polypeptide chain. !$#cross-references MUID:70255230; PMID:5447861 !$#contents annotation; X-ray crystallography of basic protease !1inhibitor, 2.5 angstroms REFERENCE A34658 !$#authors Lewis, R.V.; Ray, P.; Coguill, R.; Kruggel, W. !$#journal Biochem. Biophys. Res. Commun. (1990) 167:543-547 !$#title Presence of pancreatic trypsin inhibitor in adrenal !1medullary chromaffin cells. !$#cross-references MUID:90211226; PMID:2322242 !$#accession A34658 !'##molecule_type protein !'##residues 36-53,55-81 ##label LEW REFERENCE A93977 !$#authors Anderson, S.; Kingston, I.B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:6838-6842 !$#title Isolation of a genomic clone for bovine pancreatic trypsin !1inhibitor by using a unique-sequence synthetic DNA probe. !$#cross-references MUID:84070725; PMID:6580617 !$#accession A93977 !'##molecule_type DNA !'##residues 'PSLFNRDPPIPA',34-97,'GKTGGRAEGEGKG' ##label AND !'##cross-references GB:X03365; GB:K00966; NID:g142; PIDN:CAA27062.1; !1PID:g1364183 REFERENCE S00371 !$#authors Siekmann, J.; Wenzel, H.R.; Schroeder, W.; Tschesche, H. !$#journal Biol. Chem. Hoppe-Seyler (1988) 369:157-163 !$#title Characterization and sequence determination of six aprotinin !1homologues from bovine lungs. !$#cross-references MUID:88221840; PMID:2453200 !$#accession S10062 !'##molecule_type protein !'##residues 36-66,'P',68-82,'S',84-93 ##label SIE !'##experimental_source lung !'##note the authors designated this protein as isoaprotinin 2 COMMENT Basic proteinase inhibitor is an intracellular polypeptide !1found in many tissues, probably located in granules of !1connective tissue mast cells. GENETICS !$#introns 34/1; 98/1 CLASSIFICATION #superfamily basic proteinase inhibitor; animal Kunitz-type !1proteinase inhibitor homology KEYWORDS serine proteinase inhibitor FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-35 #domain propeptide #status predicted #label PRO\ !$36-100 #product basic proteinase inhibitor #status !8experimental #label MAT\ !$40-90 #domain animal Kunitz-type proteinase inhibitor !8homology #label BPI\ !$40-90,49-73,65-86 #disulfide_bonds #status experimental\ !$50 #inhibitory_site Lys (trypsin, chymotrypsin, !8kallikrein, plasmin) #status experimental SUMMARY #length 100 #molecular-weight 10903 #checksum 5865 SEQUENCE /// ENTRY TIBOSP #type complete TITLE spleen basic proteinase inhibitor precursor - bovine ALTERNATE_NAMES isoaprotinin 1 ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 07-Sep-1990 #sequence_revision 22-Jul-1994 #text_change 21-Jul-2000 ACCESSIONS S00274; B30333; A27417; S02487; S10547; S13478; A23915; !1S10064 REFERENCE S00274 !$#authors Creighton, T.E.; Charles, I.G. !$#journal J. Mol. Biol. (1987) 194:11-22 !$#title Sequences of the genes and polypeptide precursors for two !1bovine protease inhibitors. !$#cross-references MUID:87283904; PMID:2441071 !$#accession S00274 !'##molecule_type DNA; mRNA !'##residues 1-100 ##label CR2 !'##cross-references EMBL:X05275; NID:g163718; PIDN:AAA51418.1; !1PID:g163720 REFERENCE A90926 !$#authors Creighton, T.E.; Charles, I.G. !$#journal Cold Spring Harb. Symp. Quant. Biol. (1987) 52:511-519 !$#title Biosynthesis, processing, and evolution of bovine pancreatic !1trypsin inhibitor. !$#cross-references MUID:88295740; PMID:2456884 !$#accession B30333 !'##molecule_type DNA !'##residues 1-100 ##label CRE !'##cross-references GB:M20935; GB:X05275; NID:g163718; PIDN:AAA51418.1; !1PID:g163720 REFERENCE A27417 !$#authors Barra, D.; Simmaco, M.; Bossa, F.; Fioretti, E.; Angeletti, !1M.; Ascoli, F. !$#journal J. Biol. Chem. (1987) 262:13916-13919 !$#title Primary structure of a protease isoinhibitor from bovine !1spleen. A possible intermediate in the processing of the !1primary gene product. !$#cross-references MUID:88007630; PMID:3654647 !$#accession A27417 !'##molecule_type protein !'##residues 34-99 ##label BAR !'##note the more abundant form of isoinhibitor I lacks 99-Asn REFERENCE S02485 !$#authors Fioretti, E.; Angeletti, M.; Fiorucci, L.; Barra, D.; Bossa, !1F.; Ascoli, F. !$#journal Biol. Chem. Hoppe-Seyler (1988) 369(Suppl.):37-42 !$#title Aprotinin-like isoinhibitors in bovine organs. !$#cross-references MUID:89076531; PMID:2462435 !$#accession S02487 !'##molecule_type protein !'##residues 34-99 ##label FIO REFERENCE S10546 !$#authors Kingston, I.B.; Anderson, S. !$#journal Biochem. J. (1986) 233:443-450 !$#title Sequences encoding two trypsin inhibitors occur in !1strikingly similar genomic environments. !$#cross-references MUID:86158754; PMID:2420326 !$#accession S10547 !'##molecule_type DNA !'##residues 34-97 ##label KIN REFERENCE S13478 !$#authors Barra, D.; Fioretti, E.; Angeletti, M.; Maras, B.; Bossa, !1F.; Ascoli, F. !$#journal Biochim. Biophys. Acta (1991) 1076:143-147 !$#title Proteinase isoinhibitors from bovine spleen: primary !1structure of an intermediate in the processing of the !1precursor. !$#cross-references MUID:91098258; PMID:1986787 !$#accession S13478 !'##molecule_type protein !'##residues 36-97 ##label BA2 REFERENCE A23915 !$#authors Fioretti, E.; Iacopino, G.; Angeletti, M.; Barra, D.; Bossa, !1F.; Ascoli, F. !$#journal J. Biol. Chem. (1985) 260:11451-11455 !$#cross-references MUID:86008178; PMID:2413011 !$#accession A23915 !'##molecule_type protein !'##residues 36-93 ##label FI2 !'##note three disulfide bonds are present REFERENCE S00371 !$#authors Siekmann, J.; Wenzel, H.R.; Schroeder, W.; Tschesche, H. !$#journal Biol. Chem. Hoppe-Seyler (1988) 369:157-163 !$#title Characterization and sequence determination of six aprotinin !1homologues from bovine lungs. !$#cross-references MUID:88221840; PMID:2453200 !$#accession S10064 !'##molecule_type protein !'##residues 36-93 ##label SIE !'##experimental_source lung COMMENT This inhibitor is found in many bovine organs. In spleen, it !1is located in vascular smooth muscle cells. COMMENT Compared with the basic proteinase inhibitor, affinity for !1trypsin and chymotrypsin is similar and for kallikrein is !1less. COMMENT Inhibitors I and III are intermediates in the processing of !1the precursor to the mature form, inhibitor II. GENETICS !$#introns 34/1; 98/1 CLASSIFICATION #superfamily basic proteinase inhibitor; animal Kunitz-type !1proteinase inhibitor homology KEYWORDS serine proteinase inhibitor FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-33 #domain propeptide #status predicted #label PRO\ !$34-98 #product spleen inhibitor I #status experimental !8#label SI1\ !$36-97 #product spleen inhibitor III #status experimental !8#label SI3\ !$36-93 #product spleen inhibitor II #status experimental !8#label SI2\ !$40-90 #domain animal Kunitz-type proteinase inhibitor !8homology #label BPI\ !$40-90,49-73,65-86 #disulfide_bonds #status predicted\ !$50 #inhibitory_site Lys (trypsin, chymotrypsin, !8kallikrein) #status predicted SUMMARY #length 100 #molecular-weight 10843 #checksum 5302 SEQUENCE /// ENTRY TIBOR #type complete TITLE serum basic proteinase inhibitor - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Oct-1980 #sequence_revision 31-Oct-1980 #text_change 31-Dec-1993 ACCESSIONS A01206 REFERENCE A01206 !$#authors Wachter, E.; Deppner, K.; Hochstrasser, K.; Lempart, K.; !1Geiger, R. !$#journal FEBS Lett. (1980) 119:58-62 !$#title A new Kunitz-type inhibitor from bovine serum amino acid !1sequence determination. !$#cross-references MUID:81044408; PMID:7428928 !$#accession A01206 !'##molecule_type protein !'##residues 1-60 ##label WAC COMMENT This inhibitor has activity very similar to that of the !1basic protease inhibitor from bovine tissues. CLASSIFICATION #superfamily basic proteinase inhibitor; animal Kunitz-type !1proteinase inhibitor homology KEYWORDS serine proteinase inhibitor FEATURE !$7-57 #domain animal Kunitz-type proteinase inhibitor !8homology #label BPI\ !$17 #inhibitory_site Lys (trypsin) #status experimental SUMMARY #length 60 #molecular-weight 6647 #checksum 3671 SEQUENCE /// ENTRY A55115 #type complete TITLE uterine plasmin/trypsin inhibitor - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A55115 REFERENCE A55115 !$#authors Stallings-Mann, M.L.; Burke, M.G.; Trout, W.E.; Roberts, !1R.M. !$#journal J. Biol. Chem. (1994) 269:24090-24094 !$#title Purification, characterization, and cDNA cloning of a !1Kunitz-type proteinase inhibitor secreted by the porcine !1uterus. !$#cross-references MUID:95014140; PMID:7929061 !$#accession A55115 !'##status preliminary !'##molecule_type mRNA !'##residues 1-122 ##label STA !'##cross-references GB:L14282; NID:g682652; PIDN:AAA62425.1; !1PID:g682653 !'##note authors translated the codon GGC for residue 36 as Ala, AGC for !1residue 48 as Arg, GTC for residue 52 as Ile, and AGC for !1residue 65 as Thr CLASSIFICATION #superfamily basic proteinase inhibitor; animal Kunitz-type !1proteinase inhibitor homology KEYWORDS serine proteinase inhibitor FEATURE !$38-88 #domain animal Kunitz-type proteinase inhibitor !8homology #label BPI SUMMARY #length 122 #molecular-weight 13109 #checksum 4219 SEQUENCE /// ENTRY TIHCBP #type complete TITLE proteinase inhibitor (BPI-type) - horseshoe crab (Tachypleus tridentatus) ORGANISM #formal_name Tachypleus tridentatus DATE 08-Mar-1989 #sequence_revision 22-Jul-1994 #text_change 24-Feb-1995 ACCESSIONS A26923 REFERENCE A26923 !$#authors Nakamura, T.; Hirai, T.; Tokunaga, F.; Kawabata, S.; !1Iwanaga, S. !$#journal J. Biochem. (1987) 101:1297-1306 !$#title Purification and amino acid sequence of Kunitz-type protease !1inhibitor found in the hemocytes of horseshoe crab !1(Tachypleus tridentatus). !$#cross-references MUID:88007472; PMID:3308864 !$#accession A26923 !'##molecule_type protein !'##residues 1-61 ##label NAK !'##experimental_source hemocytes COMMENT The inhibitory activity is similar to bovine basic !1proteinase inhibitor. CLASSIFICATION #superfamily basic proteinase inhibitor; animal Kunitz-type !1proteinase inhibitor homology KEYWORDS serine proteinase inhibitor FEATURE !$8-58 #domain animal Kunitz-type proteinase inhibitor !8homology #label BPI\ !$8-58,17-41,33-54 #disulfide_bonds #status predicted\ !$18 #inhibitory_site Arg (chymotrypsin, elastase, !8trypsin, plasmin, plasma kallikrein) #status !8predicted SUMMARY #length 61 #molecular-weight 6825 #checksum 5715 SEQUENCE /// ENTRY TIBOC #type complete TITLE trypsin inhibitor, colostrum (BPI type) - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 24-Apr-1984 #sequence_revision 31-Dec-1993 #text_change 06-Dec-1996 ACCESSIONS A01207 REFERENCE A90928 !$#authors Cechova, D.; Jonakova, V.; Sorm, F. !$#journal Collect. Czech. Chem. Commun. (1971) 36:3342-3357 !$#title Primary structure of trypsin inhibitor from cow colostrum !1(component B2). !$#accession A01207 !'##molecule_type protein !'##residues 1-26,'B',28-67 ##label CEC !'##note the residue identified as Asx is bound to carbohydrate; !1therefore, we have shown it as Asn REFERENCE A90929 !$#authors Cechova, D.; Ber, E. !$#journal Collect. Czech. Chem. Commun. (1974) 39:680-688 !$#title Disulfide bonds of trypsin inhibitor from cow colostrum. !$#contents annotation; disulfide bonds REFERENCE A91440 !$#authors Cechova, D.; Muszynska, G. !$#journal FEBS Lett. (1970) 8:84-86 !$#title Role of lysine 18 in active center of cow colostrum trypsin !1inhibitor. !$#contents annotation !$#note the inhibitory site was determined CLASSIFICATION #superfamily basic proteinase inhibitor; animal Kunitz-type !1proteinase inhibitor homology KEYWORDS colostrum; glycoprotein; serine proteinase inhibitor FEATURE !$8-58 #domain animal Kunitz-type proteinase inhibitor !8homology #label BPI\ !$8-58,17-41,33-54 #disulfide_bonds #status experimental\ !$18 #inhibitory_site Lys (trypsin) #status experimental\ !$27 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 67 #molecular-weight 7511 #checksum 9151 SEQUENCE /// ENTRY TIEPVI #type complete TITLE venom basic proteinase inhibitor I - black mamba (tentative sequence) ORGANISM #formal_name Dendroaspis polylepis polylepis #common_name black mamba DATE 30-Nov-1980 #sequence_revision 30-Nov-1980 #text_change 31-Mar-2000 ACCESSIONS A01211 REFERENCE A01211 !$#authors Strydom, D.J. !$#journal Nature New Biol. (1973) 243:88-89 !$#title Protease inhibitors as snake venom toxins. !$#cross-references MUID:73174607; PMID:4512962 !$#accession A01211 !'##molecule_type protein !'##residues 1-60 ##label STR COMMENT This protein, the main venom protein, is much less toxic to !1mice than is whole venom. It inhibits chymotrypsin slightly, !1but trypsin not at all. Its specific function has not yet !1been established. CLASSIFICATION #superfamily basic proteinase inhibitor; animal Kunitz-type !1proteinase inhibitor homology KEYWORDS serine proteinase inhibitor; venom FEATURE !$7-57 #domain animal Kunitz-type proteinase inhibitor !8homology #label BPI\ !$7-57,16-40,32-53 #disulfide_bonds #status predicted SUMMARY #length 60 #molecular-weight 7155 #checksum 6689 SEQUENCE /// ENTRY VIEPIA #type complete TITLE venom basic proteinase inhibitor I homolog - eastern green mamba ALTERNATE_NAMES alpha-dendrotoxin ORGANISM #formal_name Dendroaspis angusticeps #common_name eastern green mamba DATE 01-Sep-1981 #sequence_revision 01-Sep-1981 #text_change 24-Nov-1999 ACCESSIONS A01212 REFERENCE A91691 !$#authors Joubert, F.J.; Taljaard, N. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1980) 361:661-674 !$#title The amino acid sequences of two proteinase inhibitor !1homologues from Dendroaspis angusticeps venom. !$#cross-references MUID:81045446; PMID:7429422 !$#accession A01212 !'##molecule_type protein !'##residues 1-59 ##label JOU CLASSIFICATION #superfamily basic proteinase inhibitor; animal Kunitz-type !1proteinase inhibitor homology KEYWORDS blocked amino end; serine proteinase inhibitor; toxin; venom FEATURE !$7-57 #domain animal Kunitz-type proteinase inhibitor !8homology #label BPI\ !$1 #modified_site blocked amino end (Gln) (probably !8pyrrolidone carboxylic acid) #status experimental\ !$7-57,16-40,32-53 #disulfide_bonds #status experimental SUMMARY #length 59 #molecular-weight 7071 #checksum 5331 SEQUENCE /// ENTRY TIEPVK #type complete TITLE K+ channel blocker dendrotoxin K - black mamba ORGANISM #formal_name Dendroaspis polylepis polylepis #common_name black mamba DATE 30-Nov-1980 #sequence_revision 01-Dec-2000 #text_change 01-Dec-2000 ACCESSIONS A49291; A01213 REFERENCE A49291 !$#authors Smith, L.A.; Lafaye, P.J.; LaPenotiere, H.F.; Spain, T.; !1Dolly, J.O. !$#journal Biochemistry (1993) 32:5692-5697 !$#title Cloning and functional expression of dendrotoxin K from !1black mamba, a K+ channel blocker. !$#cross-references MUID:93277850; PMID:8504088 !$#accession A49291 !'##status preliminary !'##molecule_type mRNA; protein !'##residues 1-79 ##label SMI !'##cross-references GB:S61886; NID:g385317; PIDN:AAB26998.1; !1PID:g385318 !'##note sequence extracted from NCBI backbone (NCBIN:133053, !1NCBIP:133054) !'##note the source is designated as Dendroaspis polylepis REFERENCE A90617 !$#authors Strydom, D.J. !$#journal Biochim. Biophys. Acta (1977) 491:361-369 !$#title Snake venom toxins. The amino acid sequence of toxin Vi2, a !1homologue of pancreatic trypsin inhibitor, from Dndroaspis !1polylepis polylepis (black mamba) venom. !$#cross-references MUID:77158069; PMID:857902 !$#accession A01213 !'##molecule_type protein !'##residues 23-79 ##label STR COMMENT This protein is much less toxic to mice than is whole venom. !1It inhibits trypsin slightly, but chymotrypsin not at all. !1Its specific function has not yet been established. CLASSIFICATION #superfamily basic proteinase inhibitor; animal Kunitz-type !1proteinase inhibitor homology KEYWORDS serine proteinase inhibitor; venom FEATURE !$27-77 #domain animal Kunitz-type proteinase inhibitor !8homology #label BPI\ !$27-77,36-60,52-73 #disulfide_bonds #status predicted SUMMARY #length 79 #molecular-weight 8851 #checksum 5650 SEQUENCE /// ENTRY TIEPVA #type complete TITLE venom basic proteinase inhibitor K - eastern green mamba ALTERNATE_NAMES dendrotoxin delta-DaTX ORGANISM #formal_name Dendroaspis angusticeps #common_name eastern green mamba DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Feb-1997 ACCESSIONS A91691; C32508; A01213 REFERENCE A91691 !$#authors Joubert, F.J.; Taljaard, N. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1980) 361:661-674 !$#title The amino acid sequences of two proteinase inhibitor !1homologues from Dendroaspis angusticeps venom. !$#cross-references MUID:81045446; PMID:7429422 !$#accession A91691 !'##molecule_type protein !'##residues 1-57 ##label JOU REFERENCE A93137 !$#authors Benishin, C.G.; Sorensen, R.G.; Brown, W.E.; Krueger, B.K.; !1Blaustein, M.P. !$#journal Mol. Pharmacol. (1988) 34:152-159 !$#title Four polypeptide components of green mamba venom selectively !1block certain potassium channels in rat brain synaptosomes. !$#cross-references MUID:88318591; PMID:2457792 !$#accession C32508 !'##molecule_type protein !'##residues 1-21 ##label BEN !'##note the amino acid composition of the inhibitor is identical with !1that predicted from the sequence determined in reference !1A91691 COMMENT This proteinase inhibitor homolog has very low toxicity. Its !1physiological function is unknown. CLASSIFICATION #superfamily basic proteinase inhibitor; animal Kunitz-type !1proteinase inhibitor homology KEYWORDS venom FEATURE !$5-55 #domain animal Kunitz-type proteinase inhibitor !8homology #label BPI\ !$5-55,14-38,30-51 #disulfide_bonds #status predicted SUMMARY #length 57 #molecular-weight 6574 #checksum 5151 SEQUENCE /// ENTRY TIEPVB #type complete TITLE venom basic proteinase inhibitor B - black mamba ORGANISM #formal_name Dendroaspis polylepis polylepis #common_name black mamba DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 16-Feb-1997 ACCESSIONS A01214 REFERENCE A01214 !$#authors Strydom, D.J.; Joubert, F.J. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1981) 362:1377-1384 !$#title The amino acid sequence of a weak trypsin inhibitor B from !1Dendroaspis polylepis polylepis (black mamba) venom. !$#cross-references MUID:82074268; PMID:7309000 !$#accession A01214 !'##molecule_type protein !'##residues 1-57 ##label STR COMMENT This protease inhibits trypsin weakly. Met-15 and Phe-16 !1occupy the positions that are the trypsin-reactive site in !1homologous inhibitors. CLASSIFICATION #superfamily basic proteinase inhibitor; animal Kunitz-type !1proteinase inhibitor homology KEYWORDS serine proteinase inhibitor; venom FEATURE !$5-55 #domain animal Kunitz-type proteinase inhibitor !8homology #label BPI\ !$5-55,14-38,30-51 #disulfide_bonds #status predicted SUMMARY #length 57 #molecular-weight 6475 #checksum 6109 SEQUENCE /// ENTRY TIEPED #type complete TITLE venom basic proteinase inhibitor E - black mamba ORGANISM #formal_name Dendroaspis polylepis polylepis #common_name black mamba DATE 30-Nov-1980 #sequence_revision 30-Nov-1980 #text_change 16-Aug-1996 ACCESSIONS A01215 REFERENCE A01215 !$#authors Joubert, F.J.; Strydom, D.J. !$#journal Eur. J. Biochem. (1978) 87:191-198 !$#title Sanek venoms. The amino-acid sequence of trypsin inhibitor E !1of Dendroaspis polylepis polylepis (Black mamba) venom. !$#cross-references MUID:78214615; PMID:668688 !$#accession A01215 !'##molecule_type protein !'##residues 1-59 ##label JOU !'##note this protein inhibits trypsin and binds transition metal ions !1such as copper and cobalt CLASSIFICATION #superfamily basic proteinase inhibitor; animal Kunitz-type !1proteinase inhibitor homology KEYWORDS serine proteinase inhibitor; venom FEATURE !$7-57 #domain animal Kunitz-type proteinase inhibitor !8homology #label BPI\ !$7-57,16-40,32-53 #disulfide_bonds #status predicted SUMMARY #length 59 #molecular-weight 6620 #checksum 2765 SEQUENCE /// ENTRY TIRIV2 #type complete TITLE venom basic proteinase inhibitor II - ringhals ORGANISM #formal_name Hemachatus haemachatus, Sepedon haemachatus #common_name ringhals DATE 30-Nov-1980 #sequence_revision 30-Nov-1980 #text_change 16-Aug-1996 ACCESSIONS A01216 REFERENCE A91942 !$#authors Hokama, Y.; Iwanaga, S.; Tatsuki, T.; Suzuki, T. !$#journal J. Biochem. (1976) 79:559-578 !$#title Snake venom proteinase inhibitors. III. Isolation of five !1polypeptide inhibitors from the venoms of Hemachatus !1haemachatus (Ringhal's cobra) and Naja nivea (Cape cobra) !1and the complete amino acid sequences of two of them. !$#cross-references MUID:76237547; PMID:950337 !$#accession A01216 !'##molecule_type protein !'##residues 1-57 ##label HOK COMMENT The activity of this inhibitor is similar to that of bovine !1basic protease inhibitor. CLASSIFICATION #superfamily basic proteinase inhibitor; animal Kunitz-type !1proteinase inhibitor homology KEYWORDS serine proteinase inhibitor; venom FEATURE !$5-55 #domain animal Kunitz-type proteinase inhibitor !8homology #label BPI\ !$5-55,14-38,30-51 #disulfide_bonds #status predicted SUMMARY #length 57 #molecular-weight 6407 #checksum 3807 SEQUENCE /// ENTRY TINJVC #type complete TITLE venom basic proteinase inhibitor II - Cape cobra ORGANISM #formal_name Naja nivea #common_name Cape cobra DATE 30-Nov-1980 #sequence_revision 30-Nov-1980 #text_change 16-Aug-1996 ACCESSIONS A01217 REFERENCE A91942 !$#authors Hokama, Y.; Iwanaga, S.; Tatsuki, T.; Suzuki, T. !$#journal J. Biochem. (1976) 79:559-578 !$#title Snake venom proteinase inhibitors. III. Isolation of five !1polypeptide inhibitors from the venoms of Hemachatus !1haemachatus (Ringhal's cobra) and Naja nivea (Cape cobra) !1and the complete amino acid sequences of two of them. !$#cross-references MUID:76237547; PMID:950337 !$#accession A01217 !'##molecule_type protein !'##residues 1-57 ##label HOK COMMENT The activity of this inhibitor is probably similar to that !1of bovine basic protease inhibitor. CLASSIFICATION #superfamily basic proteinase inhibitor; animal Kunitz-type !1proteinase inhibitor homology KEYWORDS serine proteinase inhibitor; venom FEATURE !$5-55 #domain animal Kunitz-type proteinase inhibitor !8homology #label BPI\ !$5-55,14-38,30-51 #disulfide_bonds #status predicted SUMMARY #length 57 #molecular-weight 6466 #checksum 2976 SEQUENCE /// ENTRY TIKFBU #type complete TITLE beta-1 bungarotoxin chain B, major component - many-banded krait ORGANISM #formal_name Bungarus multicinctus #common_name many-banded krait DATE 30-Nov-1980 #sequence_revision 30-Nov-1980 #text_change 31-Dec-1993 ACCESSIONS A01218 REFERENCE A01218 !$#authors Kondo, K.; Narita, K.; Lee, C.Y. !$#journal J. Biochem. (1978) 83:101-115 !$#title Amino acid sequences of the two polypeptide chains in !1beta-1-bungarotoxin from the venom of Bungarus multicinctus. !$#cross-references MUID:78109400; PMID:624701 !$#accession A01218 !'##molecule_type protein !'##residues 1-60 ##label KON COMMENT Beta-1 bungarotoxin, a presynaptic neurotoxin of the venom, !1is a dimer of dissimilar chains linked by one or more !1disulfide bonds. The B chain is homologous to venom basic !1protease inhibitors. The sequences of the B chain minor !1component and the A chain, a phospholipase A2, are also !1known. CLASSIFICATION #superfamily basic proteinase inhibitor; animal Kunitz-type !1proteinase inhibitor homology KEYWORDS heterodimer; neurotoxin; venom FEATURE !$7-56 #domain animal Kunitz-type proteinase inhibitor !8homology #label BPI\ !$7-56,16-39,31-52 #disulfide_bonds #status predicted\ !$54 #disulfide_bonds interchain (to A chain) #status !8predicted SUMMARY #length 60 #molecular-weight 7034 #checksum 3589 SEQUENCE /// ENTRY TIKFBY #type complete TITLE beta-1 bungarotoxin chain B, minor component - many-banded krait ORGANISM #formal_name Bungarus multicinctus #common_name many-banded krait DATE 30-Nov-1980 #sequence_revision 30-Nov-1980 #text_change 31-Dec-1993 ACCESSIONS A01219 REFERENCE A01218 !$#authors Kondo, K.; Narita, K.; Lee, C.Y. !$#journal J. Biochem. (1978) 83:101-115 !$#title Amino acid sequences of the two polypeptide chains in !1beta-1-bungarotoxin from the venom of Bungarus multicinctus. !$#cross-references MUID:78109400; PMID:624701 !$#accession A01219 !'##molecule_type protein !'##residues 1-59 ##label KON COMMENT Beta-1 bungarotoxin, a presynaptic neurotoxin of the venom, !1is a dimer of dissimilar chains linked by one or more !1disulfide bonds. The B chain is homologous to venom basic !1protease inhibitors. The sequences of the B chain major !1component and the A chain, a phospholipase A2, are also !1known. CLASSIFICATION #superfamily basic proteinase inhibitor; animal Kunitz-type !1proteinase inhibitor homology KEYWORDS heterodimer; neurotoxin; venom FEATURE !$7-56 #domain animal Kunitz-type proteinase inhibitor !8homology #label BPI\ !$7-56,16-39,31-52 #disulfide_bonds #status predicted\ !$54 #disulfide_bonds interchain (to A chain) #status !8predicted SUMMARY #length 59 #molecular-weight 6975 #checksum 2243 SEQUENCE /// ENTRY TIKFB2 #type complete TITLE beta-2 bungarotoxin chain B [validated] - many-banded krait ORGANISM #formal_name Bungarus multicinctus #common_name many-banded krait DATE 14-Nov-1983 #sequence_revision 14-Feb-1997 #text_change 19-Jan-2001 ACCESSIONS A44550; A01220 REFERENCE A44550 !$#authors Gawinowicz, M.A. !$#citation unpublished results, cited by McDonald, N.Q., and Kwong, !1P.D., in Trends Biochem. Sci. 18, 209-210, 1993 !$#accession A44550 !'##molecule_type protein !'##residues 1-61 ##label GAW REFERENCE A01220 !$#authors Kondo, K.; Toda, H.; Narita, K.; Lee, C.Y. !$#journal J. Biochem. (1982) 91:1519-1530 !$#title Amino acid sequence of beta-2-bungarotoxin from Bungarus !1multicinctus venom. The amino acid substitutions in the B !1chains. !$#cross-references MUID:82239269; PMID:7096304 !$#accession A01220 !'##molecule_type protein !'##residues 1-19,21-40,'D',42,'DHGN',47-57,'EL',60-61 ##label KON COMMENT The B chain is homologous to venom basic protease inhibitors !1but has no protease inhibitor acitvity. The A chain has both !1phospholipase and neurotoxic activity. COMPLEX heterodimer of alpha and beta chains, disulfide linked CLASSIFICATION #superfamily basic proteinase inhibitor; animal Kunitz-type !1proteinase inhibitor homology KEYWORDS heterodimer; presynaptic neurotoxin; venom FEATURE !$7-57 #domain animal Kunitz-type proteinase inhibitor !8homology #label BPI\ !$7-57,16-40,32-53 #disulfide_bonds #status predicted\ !$55 #disulfide_bonds interchain (to A chain) #status !8predicted SUMMARY #length 61 #molecular-weight 7197 #checksum 4739 SEQUENCE /// ENTRY TIVRV2 #type complete TITLE venom basic proteinase inhibitor II - Russell's viper ORGANISM #formal_name Vipera russelli #common_name Russell's viper DATE 30-Nov-1980 #sequence_revision 30-Nov-1980 #text_change 16-Aug-1996 ACCESSIONS A01221 REFERENCE A01221 !$#authors Takahashi, H.; Iwanaga, S.; Kitagawa, T.; Hokama, Y.; !1Suzuki, T. !$#journal J. Biochem. (1974) 76:721-733 !$#title Snake venom proteinase inhibitors. II. Chemical structure of !1inhibitor II isolated from the venom of Russell's viper !1(Vipera russelli). !$#cross-references MUID:75060360; PMID:4436285 !$#accession A01221 !'##molecule_type protein !'##residues 1-60 ##label TAK COMMENT This inhibitor has activity similar to that of bovine basic !1protease inhibitor. CLASSIFICATION #superfamily basic proteinase inhibitor; animal Kunitz-type !1proteinase inhibitor homology KEYWORDS serine proteinase inhibitor; venom FEATURE !$7-57 #domain animal Kunitz-type proteinase inhibitor !8homology #label BPI\ !$7-57,16-40,32-53 #disulfide_bonds #status experimental SUMMARY #length 60 #molecular-weight 6850 #checksum 4101 SEQUENCE /// ENTRY TIVIT1 #type complete TITLE venom basic proteinase inhibitor I - western sand viper ALTERNATE_NAMES venom trypsin inhibitor I ORGANISM #formal_name Vipera ammodytes ammodytes #common_name western sand viper DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 16-Aug-1996 ACCESSIONS A01222 REFERENCE A01222 !$#authors Ritonja, A.; Meloun, B.; Gubensek, F. !$#journal Biochim. Biophys. Acta (1983) 748:429-435 !$#title The primary structure of Vipera ammodytes venom trypsin !1inhibitor I. !$#cross-references MUID:84053385; PMID:6639951 !$#accession A01222 !'##molecule_type protein !'##residues 1-61 ##label RIT COMMENT This protein inhibits trypsin and kallikrein. CLASSIFICATION #superfamily basic proteinase inhibitor; animal Kunitz-type !1proteinase inhibitor homology KEYWORDS pyroglutamic acid; serine proteinase inhibitor; venom FEATURE !$7-57 #domain animal Kunitz-type proteinase inhibitor !8homology #label BPI\ !$1 #modified_site pyrrolidone carboxylic acid (Gln) !8#status experimental\ !$7-57,16-40,32-53 #disulfide_bonds #status predicted\ !$17 #inhibitory_site Lys (trypsin) #status predicted SUMMARY #length 61 #molecular-weight 6865 #checksum 5148 SEQUENCE /// ENTRY TIVIVC #type complete TITLE venom basic proteinase inhibitor III - sand viper ALTERNATE_NAMES venom chymotrypsin inhibitor ORGANISM #formal_name Vipera ammodytes #common_name sand viper DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 16-Aug-1996 ACCESSIONS A01223 REFERENCE A01223 !$#authors Ritonja, A.; Meloun, B.; Gubensek, F. !$#journal Biochim. Biophys. Acta (1983) 746:138-145 !$#title The primary structure Of Vipera ammodytes venom chymotrypsin !1inhibitor. !$#accession A01223 !'##molecule_type protein !'##residues 1-65 ##label RIT CLASSIFICATION #superfamily basic proteinase inhibitor; animal Kunitz-type !1proteinase inhibitor homology KEYWORDS serine proteinase inhibitor; venom FEATURE !$7-57 #domain animal Kunitz-type proteinase inhibitor !8homology #label BPI\ !$7-57,16-40,32-53 #disulfide_bonds #status predicted\ !$17 #inhibitory_site Leu (chymotrypsin) #status predicted SUMMARY #length 65 #molecular-weight 7556 #checksum 7174 SEQUENCE /// ENTRY TIFFAF #type complete TITLE acrosin inhibitor - fruit fly (Drosophila funebris) ORGANISM #formal_name Drosophila funebris DATE 08-Dec-1989 #sequence_revision 22-Jul-1994 #text_change 21-Feb-1997 ACCESSIONS A33502 REFERENCE A33502 !$#authors Schmidt, T.; Stumm-Zollinger, E.; Chen, P.S.; Boehlen, P.; !1Stone, S.R. !$#journal J. Biol. Chem. (1989) 264:9745-9749 !$#title A male accessory gland peptide with protease inhibitory !1activity in Drosophila funebris. !$#cross-references MUID:89255538; PMID:2722874 !$#accession A33502 !'##molecule_type protein !'##residues 1-63 ##label SCH GENETICS !$#gene FlyBase:Dfun/PapD !'##cross-references FlyBase:FBgn0004113 CLASSIFICATION #superfamily basic proteinase inhibitor; animal Kunitz-type !1proteinase inhibitor homology KEYWORDS serine proteinase inhibitor FEATURE !$6-62 #domain animal Kunitz-type proteinase inhibitor !8homology #label BPI\ !$6-62,21-45,37-58 #disulfide_bonds #status predicted\ !$22 #inhibitory_site Arg (trypsin, acrosin, plasma !8kallikrein) #status predicted SUMMARY #length 63 #molecular-weight 6911 #checksum 8281 SEQUENCE /// ENTRY TIFHBP #type complete TITLE proteinase inhibitor - flesh fly (Sarcophaga bullata) ORGANISM #formal_name Sarcophaga bullata DATE 07-Feb-1992 #sequence_revision 22-Jul-1994 #text_change 07-May-1999 ACCESSIONS A37294 REFERENCE A37294 !$#authors Papayannopoulos, I.A.; Biemann, K. !$#journal Protein Sci. (1992) 1:278-288 !$#title Amino acid sequence of a protease inhibitor isolated from !1Sarcophaga bullata determined by mass spectrometry. !$#cross-references MUID:93284121; PMID:1304909 !$#accession A37294 !'##molecule_type protein !'##residues 1-57 ##label PAP !'##experimental_source hemolymph CLASSIFICATION #superfamily basic proteinase inhibitor; animal Kunitz-type !1proteinase inhibitor homology KEYWORDS serine proteinase inhibitor FEATURE !$6-56 #domain animal Kunitz-type proteinase inhibitor !8homology #label BPI\ !$6-56,15-39,31-52 #disulfide_bonds #status predicted\ !$16 #inhibitory_site Arg (chymotrypsin) #status predicted SUMMARY #length 57 #molecular-weight 6518 #checksum 2087 SEQUENCE /// ENTRY TIMTC3 #type complete TITLE chymotrypsin inhibitor III - silkworm ALTERNATE_NAMES SCI-III ORGANISM #formal_name Bombyx mori #common_name silkworm DATE 22-Jul-1987 #sequence_revision 22-Jul-1994 #text_change 22-Apr-1995 ACCESSIONS A25740 REFERENCE A25740 !$#authors Sasaki, T. !$#journal FEBS Lett. (1984) 168:227-230 !$#title Amino acid sequence of a novel Kunitz-type chymotrypsin !1inhibitor from hemolymph of silkworm larvae, Bombyx mori. !$#accession A25740 !'##molecule_type protein !'##residues 1-63 ##label SAS !'##experimental_source larval hemolymph COMMENT In contrast to chymotrypsin inhibitors I and II, which are !1basic, this inhibitor is acidic. CLASSIFICATION #superfamily basic proteinase inhibitor; animal Kunitz-type !1proteinase inhibitor homology KEYWORDS serine proteinase inhibitor FEATURE !$10-61 #domain animal Kunitz-type proteinase inhibitor !8homology #label BPI\ !$10-61,20-44,36-57 #disulfide_bonds #status predicted\ !$21 #inhibitory_site Phe (chymotrypsin) #status predicted SUMMARY #length 63 #molecular-weight 7118 #checksum 5071 SEQUENCE /// ENTRY TIHABK #type complete TITLE isoinhibitor K (BPI type) - Roman snail ORGANISM #formal_name Helix pomatia #common_name Roman snail DATE 23-Oct-1981 #sequence_revision 23-Oct-1981 #text_change 05-Aug-1994 ACCESSIONS A91232; A01225 REFERENCE A91232 !$#authors Tschesche, H.; Dietl, T. !$#journal Eur. J. Biochem. (1975) 58:439-451 !$#title The amino-acid sequence of isoinhibitor K from snails (Helix !1pomatia). A sequence determination by automated Edman !1degradation and mass-spectral identification of the !1phenylthiohydantoins. !$#cross-references MUID:76043680; PMID:1183446 !$#accession A91232 !'##molecule_type protein !'##residues 1-58 ##label TSC REFERENCE A91666 !$#authors Dietl, T.; Tschesche, H. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1976) 357:139-145 !$#title Die Disulfidbruecken des Trypsin-Kallikrein-Inhibitors K aus !1Weinbergschnecken (Helix pomatia). !$#cross-references MUID:76141310; PMID:3462 !$#contents annotation; disulfide bonds COMMENT This is one of several isoinhibitors of broad specificity !1that are secreted into the mucus of the snail. CLASSIFICATION #superfamily basic proteinase inhibitor; animal Kunitz-type !1proteinase inhibitor homology KEYWORDS pyroglutamic acid; serine proteinase inhibitor FEATURE !$7-57 #domain animal Kunitz-type proteinase inhibitor !8homology #label BPI\ !$1 #modified_site pyrrolidone carboxylic acid (Gln) !8#status experimental\ !$7-57,16-40,32-53 #disulfide_bonds #status predicted SUMMARY #length 58 #molecular-weight 6451 #checksum 6940 SEQUENCE /// ENTRY HCHU #type complete TITLE alpha-1-microglobulin/inter-alpha-trypsin inhibitor precursor [validated] - human ALTERNATE_NAMES bikunin; complex-forming glycoprotein heterogeneous in charge (HC) precursor; endothelial cell growth factor 2b; pre-alpha-inhibitor light chain; protein HC/HI-30 ITI; uronic acid-rich protein CONTAINS alpha-1-microglobulin (protein HC); inter-alpha-trypsin inhibitor ORGANISM #formal_name Homo sapiens #common_name man DATE 15-Oct-1982 #sequence_revision 30-Jun-1987 #text_change 08-Dec-2000 ACCESSIONS S13433; S10778; A93642; A90074; A90225; A90686; PN0450; !1B39079; A61580; B25604; C34245; A25303; A53110; S03552; !1S28930; S43466; A53642; S55688; I52208; S59509; S66434; !1S68728; S02431; A03217 REFERENCE S13433 !$#authors Vetr, H.; Gebhard, W. !$#journal Biol. Chem. Hoppe-Seyler (1990) 371:1185-1196 !$#title Structure of the human alpha(1)-microglobulin-bikunin gene. !$#cross-references MUID:91214554; PMID:1708673 !$#accession S13433 !'##status preliminary !'##molecule_type DNA !'##residues 1-352 ##label VET1 !'##cross-references EMBL:X54816; NID:g24475; PIDN:CAA38585.1; !1PID:g825614; EMBL:X54817; EMBL:X54818 REFERENCE S10778 !$#authors Diarra-Mehrpour, M.; Bourguignon, J.; Sesbouee, R.; Salier, !1J.P.; Leveillard, T.; Martin, J.P. !$#journal Eur. J. Biochem. (1990) 191:131-139 !$#title Structural analysis of the human inter-alpha-trypsin !1inhibitor light-chain gene. !$#cross-references MUID:90336621; PMID:1696200 !$#accession S10778 !'##status preliminary !'##molecule_type DNA !'##residues 1-202 ##label DIA REFERENCE A93642 !$#authors Kaumeyer, J.F.; Polazzi, J.O.; Kotick, M.P. !$#journal Nucleic Acids Res. (1986) 14:7839-7850 !$#title The mRNA for a proteinase inhibitor related to the HI-30 !1domain of inter-alpha-trypsin inhibitor also encodes !1alpha-1-microglobulin (protein HC). !$#cross-references MUID:87040757; PMID:2430261 !$#accession A93642 !'##molecule_type mRNA !'##residues 1-352 ##label KAU !'##cross-references GB:X04494; NID:g24478; PIDN:CAA28182.1; PID:g24479 REFERENCE A90074 !$#authors Lopez Otin, C.; Grubb, A.O.; Mendez, E. !$#journal Arch. Biochem. Biophys. (1984) 228:544-554 !$#title The complete amino acid sequence of human complex-forming !1glycoprotein heterogeneous in charge (protein HC) from one !1individiual. !$#cross-references MUID:84126849; PMID:6198962 !$#accession A90074 !'##molecule_type protein !'##residues 20-56,58-202 ##label LOP !'##experimental_source individual with tubular proteinuria !'##note no evidence of sequence heterogeneity could be found, in spite !1of persistent heterogeneity in charge REFERENCE A90225 !$#authors Takagi, T.; Takagi, K.; Kawai, T. !$#journal Biochem. Biophys. Res. Commun. (1981) 98:997-1001 !$#title Complete amino acid sequence of human !1alpha--1-microglobulin. !$#cross-references MUID:81184038; PMID:6164372 !$#accession A90225 !'##molecule_type protein !'##residues 20-47;58-136,138-141,'T',143-144,146-198 ##label TAK !'##experimental_source pooled urine of patients with tubular !1proteinuria REFERENCE A90686 !$#authors Reisinger, P.; Hochstrasser, K.; Albrecht, G.J.; Lempart, !1K.; Salier, J.P. !$#journal Biol. Chem. Hoppe-Seyler (1985) 366:479-483 !$#title Human inter-alpha-trypsin inhibitor: localization of the !1kunitz-type domains in the N-terminal part of the molecule !1and their release by a trypsin-like proteinase. !$#cross-references MUID:85225968; PMID:2408638 !$#accession A90686 !'##molecule_type protein !'##residues 206-290,'VI',293-342,'E',344-350 ##label REI REFERENCE PN0450 !$#authors Atmani, F.; Lacour, B.; Strecker, G.; Parvy, P.; Drueeke, !1T.; Daudon, M. !$#journal Biochem. Biophys. Res. Commun. (1993) 191:1158-1165 !$#title Molecular characteristics of uronic-acid-rich protein, a !1strong inhibitor of calcium oxalate crystallization in !1vitro. !$#cross-references MUID:93221481; PMID:8466493 !$#accession PN0450 !'##molecule_type protein !'##residues 206-214,'X' ##label ATM1 REFERENCE A39079 !$#authors Enghild, J.J.; Salvesen, G.; Hefta, S.A.; Thogersen, I.B.; !1Rutherfurd, S.; Pizzo, S.V. !$#journal J. Biol. Chem. (1991) 266:747-751 !$#title Chondroitin 4-sulfate covalently cross-links the chains of !1the human blood protein pre-alpha-inhibitor. !$#cross-references MUID:91093267; PMID:1898736 !$#accession B39079 !'##molecule_type protein !'##residues 206-225 ##label ENG1 REFERENCE A61580 !$#authors Chirat, F.; Balduyck, M.; Mizon, C.; Laroui, S.; Sautiere, !1P.; Mizon, J. !$#journal Int. J. Biochem. (1991) 23:1201-1203 !$#title A chondroitin-sulfate chain is located on serine-10 of the !1urinary trypsin inhibitor. !$#cross-references MUID:92175157; PMID:1794445 !$#accession A61580 !'##molecule_type protein !'##residues 214,'X',216-222,'X' ##label CHI REFERENCE A92583 !$#authors McKeehan, W.L.; Sakagami, Y.; Hoshi, H.; McKeehan, K.A. !$#journal J. Biol. Chem. (1986) 261:5378-5383 !$#title Two apparent human endothelial cell growth factors from !1human hepatoma cells are tumor-associated proteinase !1inhibitors. !$#cross-references MUID:86168278; PMID:3007499 !$#accession B25604 !'##molecule_type protein !'##residues 206-214,'X',216-230,'X',232-239,'X',241-248,'XX',251-252, !1'X',254 ##label MCK REFERENCE A92736 !$#authors Enghild, J.J.; Thogersen, I.B.; Pizzo, S.V.; Salvesen, G. !$#journal J. Biol. Chem. (1989) 264:15975-15981 !$#title Analysis of inter-alpha-trypsin inhibitor and a novel !1trypsin inhibitor, pre-alpha-trypsin inhibitor, from human !1plasma. Polypeptide chain stoichiometry and assembly by !1glycan. !$#cross-references MUID:89380192; PMID:2476436 !$#accession C34245 !'##molecule_type protein !'##residues 206-225 ##label ENG2 REFERENCE A25303 !$#authors Traboni, C.; Cortese, R. !$#journal Nucleic Acids Res. (1986) 14:6340 !$#title Sequence of a full length cDNA coding for human protein HC !1(alpha-1-microglobulin). !$#cross-references MUID:86312901; PMID:2428011 !$#accession A25303 !'##molecule_type mRNA !'##residues 1-218,'HW' ##label TRA !'##note this mRNA sequence appears to contain errors after residue 218 REFERENCE A53110 !$#authors Calero, M.; Escribano, J.; Grubb, A.; Mendez, E. !$#journal J. Biol. Chem. (1994) 269:384-389 !$#title Location of a novel type of interpolypeptide chain linkage !1in the human protein HC-IgA complex (HC-IgA) and !1identification of a heterogeneous chromophore associated !1with the complex. !$#cross-references MUID:94103241; PMID:7506257 !$#accession A53110 !'##molecule_type protein !'##residues 45-57 ##label CAL1 REFERENCE S03552 !$#authors Vetr, H.; Koegler, M.; Gebhard, W. !$#journal FEBS Lett. (1989) 245:137-140 !$#title The domain structure of the inhibitor subunit of human !1inter-alpha-trypsin inhibitor reflects the exon structure of !1its gene. !$#cross-references MUID:89171290; PMID:2466696 !$#accession S03552 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 206-352 ##label VET2 REFERENCE S28928 !$#authors Malki, N.; Balduyck, M.; Maes, P.; Capon, C.; Mizon, C.; !1Han, K.K.; Tartar, A.; Fournet, B.; Mizon, J. !$#journal Biol. Chem. Hoppe-Seyler (1992) 373:1009-1018 !$#title The heavy chains of human plasma inter-alpha-trypsin !1inhibitor: their isolation, their identification by !1electrophoresis and partial sequencing. Differential !1reactivity with Concanavalin A. !$#cross-references MUID:93039735; PMID:1384548 !$#accession S28930 !'##status preliminary !'##molecule_type protein !'##residues 206-215 ##label MAL REFERENCE S43466 !$#authors Morelle, W.; Capon, C.; Balduyck, M.; Sautiere, P.; Kouach, !1M.; Michalski, C.; Fournet, B.; Mizon, J. !$#journal Eur. J. Biochem. (1994) 221:881-888 !$#title Chondroitin sulphate covalently cross-links the three !1polypeptide chains of inter-alpha-trypsin inhibitor. !$#cross-references MUID:94229087; PMID:7513643 !$#accession S43466 !'##status preliminary !'##molecule_type protein !'##residues 206-221 ##label MOR REFERENCE A53642 !$#authors Wisniewski, H.G.; Burgess, W.H.; Oppenheim, J.D.; Vilcek, J. !$#journal Biochemistry (1994) 33:7423-7429 !$#title TSG-6, an arthritis-associated hyaluronan binding protein, !1forms a stable complex with the serum protein !1inter-alpha-inhibitor. !$#cross-references MUID:94271799; PMID:7516184 !$#accession A53642 !'##status preliminary !'##molecule_type protein !'##residues 206-217 ##label WIS REFERENCE S55688 !$#authors Calero, M.; Mendez, E.; Garcia, E. !$#journal Biochim. Biophys. Acta (1995) 1249:91-99 !$#title Expression of the human complex-forming glycoprotein HC !1(alpha-1-microglobulin) in Escherichia coli. !$#cross-references MUID:95284116; PMID:7539295 !$#accession S55688 !'##molecule_type protein !'##residues 20-24 ##label CAL2 REFERENCE I52208 !$#authors Bourguignon, J.; Diarra-Mehrpour, M.; Sesboue, R.; Frain, !1M.; Sala-Trepat, J.M.; Martin, J.P.; Salier, J.P. !$#journal Biochem. Biophys. Res. Commun. (1985) 131:1146-1153 !$#title Human inter-alpha-trypsin-inhibitor: characterization and !1partial nucleotide sequencing of a light chain-encoding !1cDNA. !$#cross-references MUID:86025577; PMID:2413856 !$#accession I52208 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 302-352 ##label BOU !'##cross-references GB:M11562; NID:g186587; PIDN:AAA59194.1; !1PID:g307077 REFERENCE S59509 !$#authors Wojcik, E.G.C.; van den Berg, M.; van der Linden, I.K.; !1Poort, S.R.; Cupers, R.; Bertina, R.M. !$#journal Biochem. J. (1995) 311:753-759 !$#title Factor IX Zutphen: a Cys(18) -> Arg mutation results in !1formation of a heterodimer with alpha(1)-microglobulin and !1the inability to form a calcium-induced conformation. !$#cross-references MUID:96067589; PMID:7487929 !$#accession S59509 !'##molecule_type protein !'##residues 27-35,'Y',37 ##label WOJ REFERENCE S66434 !$#authors Atmani, F.; Mizon, J.; Khan, S.R. !$#journal Eur. J. Biochem. (1996) 236:984-990 !$#title Identification of uronic-acid-rich protein as urinary !1bikunin, the light chain of inter-alpha-inhibitor. !$#cross-references MUID:96270753; PMID:8665922 !$#accession S66434 !'##molecule_type protein !'##residues 206-214,'X',216-230 ##label ATM2 REFERENCE S68728 !$#authors Akerstroem, B.; Bratt, T.; Enghild, J.J. !$#journal FEBS Lett. (1995) 362:50-54 !$#title Formation of the alpha(1)-microglobulin chromophore in !1mammalian and insect cells: a novel post-translational !1mechanism? !$#cross-references MUID:95212582; PMID:7535251 !$#accession S68728 !'##molecule_type protein !'##residues 89-100 ##label AKE REFERENCE S02431 !$#authors Jessen, T.E.; Faarvang, K.L.; Ploug, M. !$#journal FEBS Lett. (1988) 230:195-200 !$#title Carbohydrate as covalent crosslink in human !1inter-alpha-trypsin inhibitor: a novel plasma protein !1structure. !$#cross-references MUID:88167187; PMID:2450785 !$#accession S02431 !'##molecule_type protein !'##residues 206-214,'X',216-217 ##label JES REFERENCE A91304 !$#authors Lopez, C.; Grubb, A.; Mendez, E. !$#journal FEBS Lett. (1982) 144:349-353 !$#title Human protein HC displays variability in its !1carboxyl-terminal amino acid sequence. !$#contents annotation; variant of alpha-1-microglobulin !$#note pooled urine samples contained two forms of this protein, !1both lacking 57-Lys and one lacking residues 198-201 REFERENCE A91698 !$#authors Hochstrasser, K.; Schonberger, O.L.; Rossmanith, I.; !1Wachter, E. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1981) 362:1357-1362 !$#title Kunitz-type proteinase inhibitors derived by limited !1proteolysis of the inter-alpha-trypsin inhibitor, V([1-4]). !1Attachments of carbohydrates in the human urinary trypsin !1inhibitor isolated by affinity chromatography. !$#cross-references MUID:82074265; PMID:6171497 !$#contents annotation; carbohydrate binding sites REFERENCE A90682 !$#authors Morii, M.; Travis, J. !$#journal Biol. Chem. Hoppe-Seyler (1985) 366:19-21 !$#title The reactive site of human inter-alpha-trypsin inhibitor is !1in the amino-terminal half of the protein. !$#cross-references MUID:85225940; PMID:3890890 !$#contents annotation; inhibitory site !$#note in vitro, the first twelve residues of the amino end of the !1inhibitor appear to have a reactive site capable of !1inhibiting the activity of a number of enzymes; its in vivo !1function is not known COMMENT Alpha-1-microglobulin and inter-alpha-trypsin inhibitor are !1proteolytically processed from the precursor protein. COMMENT Alpha-1-microglobulin occurs in many physiological fluids !1including plasma, urine, and cerebrospinal fluid. It appears !1not only as a free monomer but also in complexes with IgA !1and albumin. It contains at least one brown-yellow !1chromophore. COMMENT As pre-alpha-inhibitor, this protein is covalently !1cross-linked by chondroitin sulfate to inter-alpha-trypsin !1inhibitor heavy chain 3 (see PIR:S30350). COMMENT Inter-alpha-trypsin inhibitor, present in plasma and urine, !1inhibits trypsin, plasmin, and lysosomal granulocytic !1elastase. Additional proteolytic processing in the kidney !1and/or urine can produce further amino- and carboxyl-end !1modifications in its sequence. COMMENT The inhibitor protein can also be derived from the amino-end !1of a larger (180kd) ITI plasma protein following in vitro !1treatment with trypsin. The complete sequence of the larger !1protein remains undetermined. GENETICS !$#gene GDB:AMBP; ITI; ITIL !'##cross-references GDB:120696; OMIM:176870 !$#map_position 9q32-9q33 !$#introns 39/3; 87/2; 113/1; 152/1; 186/1; 201/3; 229/1; 285/1; 343/1 CLASSIFICATION #superfamily protein HC; animal Kunitz-type proteinase !1inhibitor homology; lipocalin homology KEYWORDS chondroitin sulfate proteoglycan; chromoprotein; !1duplication; glycoprotein; plasma; serine proteinase !1inhibitor FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-203 #product alpha-1-microglobulin #status experimental !8#label A1G\ !$35-188 #domain lipocalin homology #label LIP\ !$206-352 #product inter-alpha-trypsin inhibitor #status !8experimental #label IAI\ !$206-226 #domain glycopeptide (secretory piece) #status !8experimental #label AMI\ !$231-281 #domain animal Kunitz-type proteinase inhibitor !8homology #label BP1\ !$287-337 #domain animal Kunitz-type proteinase inhibitor !8homology #label BP2\ !$24 #binding_site carbohydrate (Thr) (covalent) #status !8experimental\ !$36,115 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$53 #cross-link alpha-1-microglobulin-Ig alpha complex !8chromophore (Cys) (interchain to Cys-352 of Ig !8alpha-1 heavy chain) #status experimental\ !$91-188 #disulfide_bonds #status experimental\ !$215 #binding_site chondroitin sulfate (Ser) (covalent) !8#status experimental\ !$231-281,240-264, !$256-277,287-337, !$296-320,312-333 #disulfide_bonds #status predicted\ !$250 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$297 #inhibitory_site Arg (trypsin) #status predicted SUMMARY #length 352 #molecular-weight 38999 #checksum 1981 SEQUENCE /// ENTRY TIPGBI #type fragment TITLE alpha-1-microglobulin/inter-alpha-trypsin inhibitor precursor - pig (fragment) ALTERNATE_NAMES bikunin; ITI; PI-14 (inhibitory fragment of ITI) ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 30-Jun-1987 #sequence_revision 04-Feb-2000 #text_change 04-Feb-2000 ACCESSIONS S11066; S13493; A01208 REFERENCE S11066 !$#authors Gebhard, W.; Schreitmueller, T.; Vetr, H.; Wachter, E.; !1Hochstrasser, K. !$#journal FEBS Lett. (1990) 269:32-36 !$#title Complementary DNA and deduced amino acid sequences of !1porcine alpha1-microglobulin and bikunin. !$#cross-references MUID:90353595; PMID:1696914 !$#accession S11066 !'##status preliminary !'##molecule_type mRNA !'##residues 1-337 ##label GEB !'##cross-references EMBL:X53685; NID:g1877; PIDN:CAA37725.1; PID:g1878 REFERENCE S13493 !$#authors Tavakkol, A. !$#journal Biochim. Biophys. Acta (1991) 1088:47-56 !$#title Molecular cloning of porcine alpha(1)-microglobulin/HI-30 !1reveals developmental and tissue-specific expression of two !1variant messenger ribonucleic acids. !$#cross-references MUID:91113729; PMID:1703444 !$#accession S13493 !'##status preliminary !'##molecule_type mRNA !'##residues 'M',3-48,'M',50-337 ##label TAV !'##cross-references GB:X52087; NID:g1881; PIDN:CAA36306.1; PID:g1882 !'##note the authors translated the codon GTG for residue 2 as a Met !1initiation codon REFERENCE A90685 !$#authors Hochstrasser, K.; Wachter, E.; Albrecht, G.J.; Reisinger, P. !$#journal Biol. Chem. Hoppe-Seyler (1985) 366:473-478 !$#title Kunitz-type proteinase inhibitors derived by limited !1proteolysis of the inter-alpha-trypsin inhibitor, X[1]. !$#cross-references MUID:85225967; PMID:2408637 !$#accession A01208 !'##molecule_type protein !'##residues 212-258,'Q',260-269,'S',271-277,'Q',279-282,'A',284,'IR', !1287-292,'A',294-310,'K',312-314,'Q',316-334 ##label HOC COMMENT This inhibitory fragment, released from native ITI after !1limited proteolysis with trypsin, contains two homologous !1domains. Whereas the second domain is a strong inhibitor of !1trypsin, the first domain interacts weakly with !1PMN-granulocytic elastase and not at all with pancreatic !1elastase. COMMENT The amino acid at position P2' (228-Met) appears to !1determine the specificity of the inhibition of domain I. !1Inhibitors with methionine in this position interact weakly !1with chymotrypsin and elastase; those with leucine interact !1strongly. CLASSIFICATION #superfamily protein HC; animal Kunitz-type proteinase !1inhibitor homology; lipocalin homology KEYWORDS duplication; glycoprotein; plasma; serine proteinase !1inhibitor FEATURE !$20-173 #domain lipocalin homology #label LIP\ !$216-266 #domain animal Kunitz-type proteinase inhibitor !8homology #label BP1\ !$272-322 #domain animal Kunitz-type proteinase inhibitor !8homology #label BP2\ !$216-266,225-249, !$241-262,272-322, !$281-305,297-318 #disulfide_bonds #status predicted\ !$226 #inhibitory_site Leu (chymotrypsin, elastase) #status !8predicted\ !$235 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$282 #inhibitory_site Arg (trypsin) #status predicted SUMMARY #length 337 #checksum 3509 SEQUENCE /// ENTRY TIBOBI #type complete TITLE alpha-1-microglobulin / inter-alpha-trypsin inhibitor precursor [validated] - bovine ALTERNATE_NAMES BI-14 (inhibitory fragment of ITI); bikunin; ITI ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 25-Feb-1985 #sequence_revision 04-Feb-2000 #text_change 18-Aug-2000 ACCESSIONS S68149; A91717; A90685; S31219; A01209 REFERENCE S68149 !$#authors Lindqvist, A.; Akerstroem, B. !$#journal Biochim. Biophys. Acta (1996) 1306:98-106 !$#title Bovine alpha(1)-microglobulin/bikunin. Isolation and !1characterization of liver cDNA and urinary alpha !1(1)-microglobulin. !$#cross-references MUID:96201710; PMID:8611630 !$#accession S68149 !'##status preliminary !'##molecule_type mRNA !'##residues 1-352 ##label LIN !'##cross-references EMBL:U35642; NID:g1016297; PIDN:AAB07599.1; !1PID:g1016298 REFERENCE A91717 !$#authors Hochstrasser, K.; Wachter, E. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1983) 364:1679-1687 !$#title Kunitz-type proteinase inhibitors derived by limited !1proteolysis of the inter-alpha trypsin inhibitor, VII([1-6] !1). !$#cross-references MUID:84133807; PMID:6199275 !$#accession A91717 !'##molecule_type protein !'##residues 227-267,'L',269-273,'Q',275-297,'AF',300-329,'Q',331-345, !1'R',347-348 ##label HOC REFERENCE A90685 !$#authors Hochstrasser, K.; Wachter, E.; Albrecht, G.J.; Reisinger, P. !$#journal Biol. Chem. Hoppe-Seyler (1985) 366:473-478 !$#title Kunitz-type proteinase inhibitors derived by limited !1proteolysis of the inter-alpha-trypsin inhibitor, X[1]. !$#cross-references MUID:85225967; PMID:2408637 !$#accession A90685 !'##molecule_type protein !'##residues 347-349 ##label HOC2 REFERENCE A91718 !$#authors Hochstrasser, K.; Albrecht, G.J.; Schonberger, O.L.; !1Wachter, E. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1983) 364:1689-1696 !$#title Kunitz-type proteinase inhibitors derived by limited !1proteolysis of the inter-alpha-trypsin inhibitor, VIII([1-7] !1). !$#cross-references MUID:84133808; PMID:6199276 !$#contents annotation; reactive sites REFERENCE S31219 !$#authors Castillo, G.M.; Templeton, D.M. !$#journal FEBS Lett. (1993) 318:292-296 !$#title Subunit structure of bovine ESF (extracellular-matrix !1stabilizing factor(s)). A chondroitin sulfate proteoglycan !1with homology to human I-alpha-i (inter-alpha-trypsin !1inhibitors). !$#cross-references MUID:93178646; PMID:7680011 !$#accession S31219 !'##status preliminary !'##molecule_type protein !'##residues 206-214,'X',216,'X',218-220 ##label CAS CLASSIFICATION #superfamily protein HC; animal Kunitz-type proteinase !1inhibitor homology; lipocalin homology KEYWORDS duplication; glycoprotein; plasma; serine proteinase !1inhibitor FEATURE !$35-188 #domain lipocalin homology #label LIP\ !$231-281 #domain animal Kunitz-type proteinase inhibitor !8homology #label BP1\ !$287-337 #domain animal Kunitz-type proteinase inhibitor !8homology #label BP2\ !$241 #inhibitory_site Leu (chymotrypsin, elastase) #status !8experimental\ !$250 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$297 #inhibitory_site Arg (trypsin) #status experimental SUMMARY #length 352 #molecular-weight 39234 #checksum 118 SEQUENCE /// ENTRY TIHOBI #type fragment TITLE alpha-1-microglobulin/inter-alpha-trypsin inhibitor - horse (fragment) ALTERNATE_NAMES EI-14 (inhibitory fragment of ITI); ITI; trypsin inhibitor, E-UTI ORGANISM #formal_name Equus caballus #common_name domestic horse DATE 30-Jun-1987 #sequence_revision 04-Feb-2000 #text_change 05-May-2000 ACCESSIONS A01210; A45653 REFERENCE A90685 !$#authors Hochstrasser, K.; Wachter, E.; Albrecht, G.J.; Reisinger, P. !$#journal Biol. Chem. Hoppe-Seyler (1985) 366:473-478 !$#title Kunitz-type proteinase inhibitors derived by limited !1proteolysis of the inter-alpha-trypsin inhibitor, X[1]. !$#cross-references MUID:85225967; PMID:2408637 !$#accession A01210 !'##molecule_type protein !'##residues 3-125 ##label HOC REFERENCE A45653 !$#authors Veeraragavan, K.; Singh, K.; Wachter, E.; Hochstrasser, K. !$#journal Biochem. Int. (1992) 26:405-413 !$#title Characterization of a trypsin inhibitor from equine urine. !$#cross-references MUID:92328813; PMID:1627153 !$#accession A45653 !'##status preliminary !'##molecule_type protein !'##residues 1-12,'E',14-33 ##label VEE !'##cross-references PIDN:AAB22430.1; PID:g250858 !'##experimental_source urine !'##note sequence extracted from NCBI backbone (NCBIP:107966) COMMENT This inhibitory fragment, released from native ITI after !1limited proteolysis with trypsin, contains two homologous !1domains. Whereas the second domain is a strong inhibitor of !1trypsin, the first domain interacts weakly with !1PMN-granulocytic elastase and not at all with pancreatic !1elastase. COMMENT The amino acid at position P2' (19-Met) appears to determine !1the specificity of the inhibition of domain I. Inhibitors !1with methionine in this position interact weakly with !1chymotrypsin and elastase; those with leucine interact !1strongly. CLASSIFICATION #superfamily protein HC; animal Kunitz-type proteinase !1inhibitor homology; lipocalin homology KEYWORDS duplication; glycoprotein; plasma; serine proteinase !1inhibitor FEATURE !$7-57 #domain animal Kunitz-type proteinase inhibitor !8homology #label BP1\ !$63-113 #domain animal Kunitz-type proteinase inhibitor !8homology #label BP2\ !$7-57,16-40,32-53, !$63-113,72-96,88-109 #disulfide_bonds #status predicted\ !$17 #inhibitory_site Leu (chymotrypsin, elastase) #status !8predicted\ !$26 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$73 #inhibitory_site Arg (trypsin) #status predicted SUMMARY #length 125 #checksum 2963 SEQUENCE /// ENTRY S22181 #type complete TITLE gamma-1-microglobulin precursor - plaice ORGANISM #formal_name Pleuronectes platessa #common_name plaice DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S22181 REFERENCE S22181 !$#authors Leaver, M.J. !$#submission submitted to the EMBL Data Library, December 1991 !$#accession S22181 !'##status preliminary !'##molecule_type mRNA !'##residues 1-355 ##label LEA !'##cross-references EMBL:X63762; NID:g64233; PIDN:CAA45294.1; !1PID:g64234 CLASSIFICATION #superfamily protein HC; animal Kunitz-type proteinase !1inhibitor homology; lipocalin homology FEATURE !$37-189 #domain lipocalin homology #label LIP\ !$236-286 #domain animal Kunitz-type proteinase inhibitor !8homology #label BP1\ !$292-342 #domain animal Kunitz-type proteinase inhibitor !8homology #label BP2 SUMMARY #length 355 #molecular-weight 39669 #checksum 7920 SEQUENCE /// ENTRY TITTOR #type complete TITLE basic proteinase inhibitor - loggerhead ORGANISM #formal_name Caretta caretta #common_name loggerhead DATE 31-May-1979 #sequence_revision 23-Oct-1981 #text_change 05-Aug-1994 ACCESSIONS A01224 REFERENCE A01224 !$#authors Kato, I.; Tominaga, N. !$#journal Fed. Proc. (1979) 38:832 !$#title Trypsin--subtilisin inhibitor from red sea turtle eggwhite !1consists of two tandem domains -- one Kunitz -- one of a new !1family. !$#accession A01224 !'##molecule_type protein !'##residues 1-110 ##label KAT COMMENT This inhibitor, isolated from egg white, consists of two !1nonhomologous domains, the first inhibiting trypsin and the !1second inhibiting subtilisin. CLASSIFICATION #superfamily loggerhead basic proteinase inhibitor; animal !1Kunitz-type proteinase inhibitor homology; !1antileukoproteinase repeat homology KEYWORDS pyroglutamic acid; serine proteinase inhibitor FEATURE !$8-58 #domain animal Kunitz-type proteinase inhibitor !8homology #label BPI\ !$63-105 #domain antileukoproteinase repeat homology #label !8ALP\ !$1 #modified_site pyrrolidone carboxylic acid (Gln) !8#status experimental\ !$8-58,17-41,33-54, !$67-93,76-97,80-92, !$86-101 #disulfide_bonds #status predicted\ !$18 #inhibitory_site Lys (trypsin) #status predicted SUMMARY #length 110 #molecular-weight 11916 #checksum 1081 SEQUENCE /// ENTRY TIHUSP #type complete TITLE antileukoproteinase 1 precursor [validated] - human ALTERNATE_NAMES elastase inhibitor; HUSI-1; mucus proteinase inhibitor; secretory leukocyte proteinase inhibitor; seminal proteinase inhibitor ORGANISM #formal_name Homo sapiens #common_name man DATE 13-Aug-1986 #sequence_revision 07-Jul-1995 #text_change 08-Dec-2000 ACCESSIONS A25541; A25007; A25890; A01226; B01226; S13455; I55560; !1S14330; S21664; S50026 REFERENCE A25541 !$#authors Stetler, G.; Brewer, M.T.; Thompson, R.C. !$#journal Nucleic Acids Res. (1986) 14:7883-7896 !$#title Isolation and sequence of a human gene encoding a potent !1inhibitor of leukocyte proteases. !$#cross-references MUID:87040761; PMID:3640338 !$#accession A25541 !'##molecule_type DNA; mRNA !'##residues 1-132 ##label STE !'##cross-references GB:X04502; NID:g36485; PIDN:CAA28187.1; PID:g758101 REFERENCE A25007 !$#authors Heinzel, R.; Appelhans, H.; Gassen, G.; Seemuller, U.; !1Machleidt, W.; Fritz, H.; Steffens, G. !$#journal Eur. J. Biochem. (1986) 160:61-67 !$#title Molecular cloning and expression of cDNA for human !1antileukoprotease from cervix uterus. !$#cross-references MUID:87030258; PMID:3533531 !$#accession A25007 !'##molecule_type mRNA !'##residues 1-132 ##label HEI !'##cross-references GB:X04470; NID:g28638; PIDN:CAA28158.1; PID:g28639 REFERENCE A25890 !$#authors Thompson, R.C.; Ohlsson, K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:6692-6696 !$#title Isolation, properties, and complete amino acid sequence of !1human secretory leukocyte protease inhibitor, a potent !1inhibitor of leukocyte elastase. !$#cross-references MUID:86313644; PMID:3462719 !$#accession A25890 !'##molecule_type protein !'##residues 26-132 ##label THO REFERENCE A01226 !$#authors Seemuller, U.; Arnhold, M.; Fritz, H.; Wiedenmann, K.; !1Machleidt, W.; Heinzel, R.; Appelhans, H.; Gassen, H.G.; !1Lottspeich, F. !$#journal FEBS Lett. (1986) 199:43-48 !$#title The acid-stable proteinase inhibitor of human mucous !1secretions (HUSI-I, antileukoprotease). Complete amino acid !1sequence as revealed by protein and cDNA sequencing and !1structural homology to whey proteins and Red sea turtle !1proteinase inhibitor. !$#cross-references MUID:86164996; PMID:3485543 !$#accession A01226 !'##molecule_type protein !'##residues 26-132 ##label SEE !$#accession B01226 !'##molecule_type mRNA !'##residues 26-65 ##label SE2 REFERENCE S13455 !$#authors Sallenave, J.M.; Ryle, A.P. !$#journal Biol. Chem. Hoppe-Seyler (1991) 372:13-21 !$#title Purification and characterization of elastase-specific !1inhibitor. Sequence homology with mucus proteinase !1inhibitor. !$#cross-references MUID:91248412; PMID:2039600 !$#accession S13455 !'##molecule_type protein !'##residues 26-52 ##label SAL REFERENCE I55560 !$#authors Abe, T.; Kobayashi, N.; Yoshimura, K.; Trapnell, B.C.; Kim, !1H.; Hubbard, R.C.; Brewer, M.T.; Thompson, R.C.; Crystal, !1R.G. !$#journal J. Clin. Invest. (1991) 87:2207-2215 !$#title Expression of the secretory leukoprotease inhibitor gene in !1epithelial cells. !$#cross-references MUID:91250579; PMID:1674946 !$#accession I55560 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-26 ##label RES !'##cross-references GB:M74444; NID:g338232; PIDN:AAA60559.1; !1PID:g338233 REFERENCE S14330 !$#authors Boehm, B.; Deutzmann, R.; Burkhardt, H. !$#journal Biochem. J. (1991) 274:269-273 !$#title Purification of a serine-proteinase inhibitor from human !1articular cartilage. Identity with the acid-stable !1proteinase inhibitor of mucous secretions. !$#cross-references MUID:91158717; PMID:2001242 !$#accession S14330 !'##molecule_type protein !'##residues 26-34,'X',36-42,'X',44-50,'XE',53-55;103-104,'X',106-107 !1##label BOE REFERENCE S21664 !$#authors Andrews, J.L.; Melrose, J.; Ghosh, P. !$#journal Biol. Chem. Hoppe-Seyler (1992) 373:111-118 !$#title A comparative study of the low-molecular mass serine !1proteinase inhibitors of human connective tissues. !$#cross-references MUID:92265184; PMID:1586451 !$#accession S21664 !'##molecule_type protein !'##residues 26-34;36-42;46-50;52-54 ##label AND REFERENCE S50026 !$#authors Boudier, C.; Bieth, J.G. !$#journal Biochem. J. (1994) 303:61-68 !$#title Oxidized mucus proteinase inhibitor: a fairly potent !1neutrophil elastase inhibitor. !$#cross-references MUID:95031986; PMID:7945266 !$#accession S50026 !'##molecule_type protein !'##residues 26-34;99-106;108-116;123-132 ##label BOU COMMENT This protein contains a 'four-disulfide core,' a !1three-dimensional folding pattern of disulfide loops, within !1each domain. Although its functional significance is not yet !1known, this structure is also found in the related whey !1acidic proteins and chelonianin. COMMENT The sources of this protein include saliva, seminal plasma, !1and glandular tissue from the cervix. COMMENT Human mucous fluids contain acid-stable proteinase !1inhibitors with strong affinities for trypsin, chymotrypsin, !1elastase, and cathepsin G. Sequence similarities among the !1HUSI-1-type antileukoproteinases suggest that these !1inhibitors are encoded by a single gene expressed in all !1epithelial mucus cells. GENETICS !$#gene GDB:SLPI; HUSI-I !'##cross-references GDB:9836429; OMIM:107285 CLASSIFICATION #superfamily antileukoproteinase; antileukoproteinase repeat !1homology KEYWORDS duplication; glycoprotein; serine proteinase inhibitor FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-132 #product antileukoproteinase 1 #status experimental !8#label MAT\ !$31-76 #domain antileukoproteinase repeat homology #label !8ALP1\ !$85-130 #domain antileukoproteinase repeat homology #label !8ALP2\ !$35-64,43-68,51-63, !$57-72,89-118, !$96-122,105-117, !$111-126 #disulfide_bonds #status predicted\ !$45 #inhibitory_site Arg (trypsin) #status predicted\ !$80 #binding_site carbohydrate (Asn) (covalent) #status !8absent\ !$97,98 #inhibitory_site Leu, Met (elastase, chymotrypsin) !8#status predicted SUMMARY #length 132 #molecular-weight 14326 #checksum 3601 SEQUENCE /// ENTRY WYMS #type complete TITLE whey acidic protein precursor - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 16-Jun-2000 ACCESSIONS A93423; B23879; A01227; A92296 REFERENCE A93423 !$#authors Hennighausen, L.G.; Sippel, A.E. !$#journal Nucleic Acids Res. (1982) 10:2677-2684 !$#title Mouse whey acidic protein is a novel member of the family of !1'four-disulfide core' proteins. !$#cross-references MUID:82196900; PMID:6896234 !$#accession A93423 !'##molecule_type mRNA !'##residues 1-134 ##label HEN !'##note the cDNA codons given for residues 1 (AGT) and 63 (CGT) are !1inconsistent with the authors' translation and table of !1amino acid composition !'##note whey acidic protein and the neurophysins resemble each other in !1the number and pattern of distribution of the Cys residues, !1including the existence of two domains (duplicated region), !1but otherwise there is little detectable similarity between !1these proteins REFERENCE A92296 !$#authors Piletz, J.E.; Heinlen, M.; Ganschow, R.E. !$#journal J. Biol. Chem. (1981) 256:11509-11516 !$#title Biochemical characterization of a novel whey protein from !1murine milk. !$#cross-references MUID:82052974; PMID:6975276 !$#contents annotation; composition of tryptic peptides; strain YBR, !1variant !$#note the variant form appears to have one less Cys and one more !1Arg !$#note no phosphate or carbohydrate binding could be detected; !1however, both cholesterol and triglyceride are associated !1with the mouse protein REFERENCE A94701 !$#authors Campbell, S.M.; Rosen, J.M.; Hennighausen, L.G.; !1Strech-Jurk, U.; Sippel, A.E. !$#journal Nucleic Acids Res. (1984) 12:8685-8697 !$#title Comparison of the whey acidic protein genes of the rat and !1mouse. !$#cross-references MUID:85062841; PMID:6095207 !$#accession B23879 !'##molecule_type DNA !'##residues 1,'S',3-34,'Q',36-62,'V',64-86,'S',88-99,'K',101-134 !1##label CAM !'##cross-references GB:X01157; NID:g55423; PIDN:CAA25604.1; !1PID:g1213616 COMMENT This is one of the major protein components in the milk !1whey; although its function is unknown, sequence homologies !1with known proteinase inhibitors suggests that it may have !1an, as yet undescribed, inhibitory function. GENETICS !$#introns 30/1; 75/1; 130/1 CLASSIFICATION #superfamily antileukoproteinase; antileukoproteinase repeat !1homology KEYWORDS duplication; milk; proteinase inhibitor FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-134 #product whey acidic protein #status predicted #label !8MAT\ !$30-73 #domain antileukoproteinase repeat homology #label !8ALP1\ !$79-128 #domain antileukoproteinase repeat homology #label !8ALP2 SUMMARY #length 134 #molecular-weight 14392 #checksum 6533 SEQUENCE /// ENTRY WYRT #type complete TITLE whey acidic protein precursor - rat ALTERNATE_NAMES whey phosphoprotein ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 17-Jan-1983 #sequence_revision 17-Jan-1983 #text_change 21-Jul-2000 ACCESSIONS A93920; A93430; A23879; A01228 REFERENCE A93920 !$#authors Dandekar, A.M.; Robinson, E.A.; Appella, E.; Qasba, P.K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:3987-3991 !$#title Complete sequence analysis of cDNA clones encoding rat whey !1phosphoprotein: homology to a protease inhibitor. !$#cross-references MUID:82275050; PMID:6955785 !$#accession A93920 !'##molecule_type mRNA !'##residues 1-137 ##label DAN !'##cross-references GB:J00802; NID:g207682; PIDN:AAA42347.1; !1PID:g207683 !'##note partial sequencing of the precursor and of the mature protein !1have confirmed 27 of the first 41 residues !'##note this protein is called whey phosphoprotein by these authors REFERENCE A93430 !$#authors Hennighausen, L.G.; Sippel, A.E. !$#journal Nucleic Acids Res. (1982) 10:3733-3744 !$#title Comparative sequence analysis of the mRNAs coding for mouse !1and rat whey protein. !$#cross-references MUID:82274212; PMID:6896749 !$#accession A93430 !'##molecule_type mRNA !'##residues 1-3,'S',5-98,'G',100-126,'K',128,'D',130-133,'I',135-137 !1##label HEN REFERENCE A94701 !$#authors Campbell, S.M.; Rosen, J.M.; Hennighausen, L.G.; !1Strech-Jurk, U.; Sippel, A.E. !$#journal Nucleic Acids Res. (1984) 12:8685-8697 !$#title Comparison of the whey acidic protein genes of the rat and !1mouse. !$#cross-references MUID:85062841; PMID:6095207 !$#accession A23879 !'##molecule_type DNA !'##residues 1-3,'S',5-34,'S',36-38,'F',40-67,'S',69-115,'K',117-128, !1'K',130-133,'I',135-137 ##label CAM !'##cross-references GB:X01153; NID:g57492; PIDN:CAA25600.2; !1PID:g5679681 COMMENT Whey acidic protein and the neurophysins resemble each other !1in the number and pattern of distribution of the Cys !1residues, including the existence of two domains (duplicated !1region), but otherwise there is little detectable similarity !1between these proteins. COMMENT This is one of the major protein components in the milk !1whey; although its function is unknown, sequence homologies !1with known proteinase inhibitors suggests that it may have !1an, as yet undescribed, inhibitory function. GENETICS !$#introns 30/1; 75/1; 129/1 CLASSIFICATION #superfamily antileukoproteinase; antileukoproteinase repeat !1homology KEYWORDS duplication; milk; phosphoprotein; proteinase inhibitor FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-137 #product whey acidic protein #status predicted #label !8MAT\ !$30-73 #domain antileukoproteinase repeat homology #label !8ALP1\ !$79-127 #domain antileukoproteinase repeat homology #label !8ALP2\ !$34-61,45-65,48-60, !$54-69,83-115, !$96-119,102-114, !$108-123 #disulfide_bonds #status predicted\ !$39,40,103 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$50 #binding_site phosphate (Thr) (covalent) #status !8predicted SUMMARY #length 137 #molecular-weight 14820 #checksum 9613 SEQUENCE /// ENTRY S36658 #type complete TITLE proteinase inhibitors precursor [validated] - migratory locust ALTERNATE_NAMES deoxyhexose-linked peptide; pars intercerebralis major peptide C (PMP-C); pars intercerebralis major peptide D2 (PMP-D2) CONTAINS chymotrypsin inhibitor I; chymotrypsin inhibitor II ORGANISM #formal_name Locusta migratoria #common_name migratory locust DATE 06-Jan-1995 #sequence_revision 06-Jan-1995 #text_change 15-Sep-2000 ACCESSIONS S36658; S23076; S23074; JC1363; JC1364 REFERENCE S36658 !$#authors Lagueux, M.L. !$#submission submitted to the EMBL Data Library, May 1993 !$#accession S36658 !'##status preliminary !'##molecule_type mRNA !'##residues 1-92 ##label LAG !'##cross-references EMBL:Z22805; NID:g397613; PIDN:CAA80462.1; !1PID:g397614 REFERENCE S23074 !$#authors Nakakura, N.; Hietter, H.; van Dorsselaer, A.; Luu, B. !$#journal Eur. J. Biochem. (1992) 204:147-153 !$#title Isolation and structural determination of three peptides !1from the insect Locusta migratoria. Identification of a !1deoxyhexose-linked peptide. !$#cross-references MUID:92155197; PMID:1740125 !$#accession S23076 !'##molecule_type protein !'##residues 20-54 ##label NAK1 !$#accession S23074 !'##molecule_type protein !'##residues 57-92 ##label NAK2 !'##note the covalently bound sugar is identified as the deoxyhexose !1fucose REFERENCE JC1363 !$#authors Boigegrain, R.A.; Mattras, H.; Brehelin, M.; Paroutaud, P.; !1Coletti-Previero, M.A. !$#journal Biochem. Biophys. Res. Commun. (1992) 189:790-793 !$#title Insect immunity: Two proteinase inhibitors from hemolymph of !1Locusta migratoria. !$#cross-references MUID:93112047; PMID:1472051 !$#accession JC1363 !'##molecule_type protein !'##residues 20-54 ##label BOI1 !$#accession JC1364 !'##molecule_type protein !'##residues 57-92 ##label BOI2 REFERENCE A66384 !$#authors Mer, G.; Hietter, H.; Lefevre, J.F. !$#submission submitted to the Brookhaven Protein Data Bank, September !11995 !$#cross-references PDB:1PMC !$#contents annotation; conformation and disulfide bond assignments by !1(1)H-NMR, residues 57-92 REFERENCE A56290 !$#authors Mer, G.; Kellenberger, C.; Koehl, P.; Stote, R.; Sorokine, !1O.; Van Dorsselaer, A.; Luu, B.; Hietter, H.; Lefevre, J.F. !$#journal Biochemistry (1994) 33:15397-15407 !$#title Solution structure of PMP-D2, a 35-residue peptide isolated !1from the insect Locusta migratoria. !$#cross-references MUID:95101633; PMID:7803403 !$#contents annotation; conformation and disulfide bond assignments by !1(1)H-NMR; chemical disulfide bond assignment; residues 20-54 REFERENCE A58596 !$#authors Mer, G.; Hietter, H.; Kellenberger, C.; Renatus, M.; Luu, !1B.; Lefevre, J.F. !$#journal J. Mol. Biol. (1996) 258:158-171 !$#title Solution structure of PMP-C: a new fold in the group of !1small serine proteinase inhibitors. !$#cross-references MUID:96200987; PMID:8613985 !$#contents annotation; conformation and disulfide bond assignments by !1(1)H-NMR, residues 57-92 COMMENT These proteinase inhibitors probably act in the hemolymph to !1inhibit intermediate proteinases in the activation cascade !1for phenoloxidase. CLASSIFICATION #superfamily locust proteinase inhibitors precursor KEYWORDS duplication; glycoprotein; hemolymph; serine proteinase !1inhibitor FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-54 #product chymotrypsin inhibitor I #status !8experimental #label MAT1\ !$57-92 #product chymotrypsin inhibitor II #status !8experimental #label MAT2\ !$23-38,33-51,36-46, !$60-75,70-89,73-84 #disulfide_bonds #status experimental\ !$65 #binding_site carbohydrate (Thr) (covalent) #status !8experimental SUMMARY #length 92 #molecular-weight 9760 #checksum 2196 SEQUENCE /// ENTRY TIHUA #type complete TITLE pancreatic secretory trypsin inhibitor precursor [validated] - human ALTERNATE_NAMES endothelial cell growth factor 2a ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Nov-1980 #sequence_revision 17-Feb-1994 #text_change 08-Dec-2000 ACCESSIONS A27484; S02605; A90062; A92355; A25604; I52210; A01229 REFERENCE A27484 !$#authors Horii, A.; Kobayashi, T.; Tomita, N.; Yamamoto, T.; !1Fukushige, S.; Murotsu, T.; Ogawa, M.; Mori, T.; Matsubara, !1K. !$#journal Biochem. Biophys. Res. Commun. (1987) 149:635-641 !$#title Primary structure of human pancreatic secretory trypsin !1inhibitor (PSTI) gene. !$#cross-references MUID:88106485; PMID:3501289 !$#accession A27484 !'##molecule_type DNA !'##residues 1-79 ##label HOR !'##cross-references GB:M20530; GB:M18374; NID:g190692; PIDN:AAA36522.1; !1PID:g190694 REFERENCE S02605 !$#authors Tomita, N.; Horii, A.; Yamamoto, T.; Ogawa, M.; Mori, T.; !1Matsubara, K. !$#journal FEBS Lett. (1987) 225:113-119 !$#title Expression of pancreatic secretory trypsin inhibitor gene in !1neoplastic tissues. !$#cross-references MUID:88083571; PMID:2961612 !$#accession S02605 !'##molecule_type mRNA !'##residues 1-63,'G',65-79 ##label TOM !'##cross-references EMBL:Y00705; NID:g35765; PIDN:CAA68697.1; !1PID:g35766 !'##note the authors translated the codon TAC for residue 33 as Thr and !1GGT for residue 64 as Asn REFERENCE A90062 !$#authors Bartelt, D.C.; Shapanka, R.; Greene, L.J. !$#journal Arch. Biochem. Biophys. (1977) 179:189-199 !$#title The primary structure of the human pancreatic secretory !1trypsin inhibitor. Amino acid sequence of the reduced !1S-aminoethylated protein. !$#cross-references MUID:77133145; PMID:843082 !$#accession A90062 !'##molecule_type protein !'##residues 24-43,'N',45-51,'D',53-79 ##label BAR !'##note the inhibitor is present in multiple chromatographic forms !1differing in asparagine content; the sequence shown is the !1most highly amidated form REFERENCE A92355 !$#authors Huhtala, M.L.; Pesonen, K.; Kalkkinen, N.; Stenman, U.H. !$#journal J. Biol. Chem. (1982) 257:13713-13716 !$#title Purification and characterization of a tumor-associated !1trypsin inhibitor from the urine of a patient with ovarian !1cancer. !$#cross-references MUID:83056875; PMID:7142173 !$#accession A92355 !'##molecule_type protein !'##residues 24-31,'X',33-38,'X',40-43,'N',45-46 ##label HUH !'##note this peptide was isolated from the urine of a patient with !1ovarian cancer REFERENCE A92583 !$#authors McKeehan, W.L.; Sakagami, Y.; Hoshi, H.; McKeehan, K.A. !$#journal J. Biol. Chem. (1986) 261:5378-5383 !$#title Two apparent human endothelial cell growth factors from !1human hepatoma cells are tumor-associated proteinase !1inhibitors. !$#cross-references MUID:86168278; PMID:3007499 !$#accession A25604 !'##molecule_type protein !'##residues 24-31,'X',33-38,'X',40-46,'X',48 ##label MCK REFERENCE I52210 !$#authors Yamamoto, T.; Nakamura, Y.; Nishide, T.; Emi, M.; Ogawa, M.; !1Mori, T.; Matsubara, K. !$#journal Biochem. Biophys. Res. Commun. (1985) 132:605-612 !$#title Molecular cloning and nucleotide sequence of human !1pancreatic secretory trypsin inhibitor (PSTI) cDNA. !$#cross-references MUID:86050645; PMID:3877508 !$#accession I52210 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-79 ##label RES !'##cross-references GB:M11949; NID:g190687; PIDN:AAA36521.1; !1PID:g190688 GENETICS !$#gene GDB:SPINK1 !'##cross-references GDB:120383; OMIM:167790 !$#map_position 5q31-5q33 !$#introns 19/1; 29/3; 65/2 CLASSIFICATION #superfamily pancreatic secretory trypsin inhibitor; Kazal !1proteinase inhibitor homology KEYWORDS monomer; pancreas; serine proteinase inhibitor FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-79 #product pancreatic secretory trypsin inhibitor !8#status experimental #label MAT\ !$30-79 #domain Kazal proteinase inhibitor homology #label !8KPI\ !$32-61,39-58,47-79 #disulfide_bonds #status predicted\ !$41 #inhibitory_site Lys (trypsin) #status predicted SUMMARY #length 79 #molecular-weight 8507 #checksum 4966 SEQUENCE /// ENTRY TIBOA #type complete TITLE pancreatic secretory trypsin inhibitor - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 16-Jul-1999 ACCESSIONS A01230 REFERENCE A92046 !$#authors Greene, L.J.; Bartelt, D.C. !$#journal J. Biol. Chem. (1969) 244:2646-2657 !$#title The structure of the bovine pancreatic secretory trypsin !1inhibitor - Kazal's inhibitor. II. The order of the tryptic !1peptides. !$#cross-references MUID:69187206; PMID:5769997 !$#accession A01230 !'##molecule_type protein !'##residues 1-56 ##label GRE REFERENCE A92097 !$#authors Guy, O.; Shapanka, R.; Greene, L.J. !$#journal J. Biol. Chem. (1971) 246:7740-7747 !$#title The structure of the bovine pancreatic secretory trypsin !1inhibitor-Kazal's inhibitor. III. Determination of the !1disulfide bonds and proteolysis by thermolysin. !$#cross-references MUID:72086018; PMID:5135319 !$#contents annotation; disulfide bonds REFERENCE A92037 !$#authors Rigbi, M.; Greene, L.J. !$#journal J. Biol. Chem. (1968) 243:5457-5464 !$#title Limited proteolysis of the bovine pancreatic secretory !1trypsin inhibitor at acid pH. !$#cross-references MUID:69080142; PMID:5750336 !$#contents annotation; inhibitory site CLASSIFICATION #superfamily pancreatic secretory trypsin inhibitor; Kazal !1proteinase inhibitor homology KEYWORDS pancreas; serine proteinase inhibitor FEATURE !$7-56 #domain Kazal proteinase inhibitor homology #label !8KPI\ !$9-38,16-35,24-56 #disulfide_bonds #status experimental\ !$18 #inhibitory_site Arg (trypsin) #status experimental SUMMARY #length 56 #molecular-weight 6161 #checksum 2522 SEQUENCE /// ENTRY TISHA #type complete TITLE pancreatic secretory trypsin inhibitor - sheep (tentative sequence) ORGANISM #formal_name Ovis orientalis aries, Ovis ammon aries #common_name domestic sheep DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jul-1999 ACCESSIONS A94487; A01230 REFERENCE A94487 !$#authors Tschesche, H.; Obermeier, R.; Hochstrasser, K. !$#citation unpublished results, cited by Tschesche, H., Wachter, E., !1Kupfer, S., Obermeier, R., Reidel, G., Haenisch, G., and !1Schneider, M., in Proceedings of the International Research !1Conference on Proteinase Inhibitors, Fritz, H., and !1Tschesche, H., eds., pp.207-222, Walter de Gruyter, New !1York, 1971 !$#accession A94487 !'##molecule_type protein !'##residues 1-56 ##label TSC CLASSIFICATION #superfamily pancreatic secretory trypsin inhibitor; Kazal !1proteinase inhibitor homology KEYWORDS pancreas; serine proteinase inhibitor FEATURE !$7-56 #domain Kazal proteinase inhibitor homology #label !8KPI\ !$9-38,16-35,24-56 #disulfide_bonds #status predicted\ !$18 #inhibitory_site Arg (trypsin) #status predicted SUMMARY #length 56 #molecular-weight 6145 #checksum 1946 SEQUENCE /// ENTRY TIPG #type complete TITLE pancreatic secretory trypsin inhibitor - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 16-Jul-1999 ACCESSIONS A91174; A92079; A91647; A90646; A01231 REFERENCE A91174 !$#authors Tschesche, H.; Wachter, E. !$#journal Eur. J. Biochem. (1970) 16:187-198 !$#title The structure of the porcine pancreatic secretory trypsin !1inhibitor I. A sequence determination by Edman degradation !1and mass spectral identification of the !1p-bromophenyl-thiohydantoins. !$#cross-references MUID:70283430; PMID:5466061 !$#contents PSTI I !$#accession A91174 !'##molecule_type protein !'##residues 1-56 ##label TS1 REFERENCE A92079 !$#authors Bartelt, D.C.; Greene, L.J. !$#journal J. Biol. Chem. (1971) 246:2218-2229 !$#title The primary structure of the porcine pancreatic secretory !1trypsin inhibitor I. Amino acid sequence of the reduced !1s-aminoethylated protein. !$#cross-references MUID:71178430; PMID:5103069 !$#accession A92079 !'##molecule_type protein !'##residues 1-56 ##label BAR REFERENCE A91654 !$#authors Tschesche, H.; Schneider, M.; Reidel, G.; Klein, H. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1972) 353:763-764 !$#title Die Disulfidbruecken des sekretorischen !1Schweinepankreas-Trypsininhibitors und der Abbau der !1kovalenten Struktur waehrend der temporaeren Hemmung. !$#cross-references MUID:73001409; PMID:4672150 !$#contents annotation; disulfide bonds REFERENCE A91647 !$#authors Tschesche, H.; Wachter, E. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1970) 351:1449-1459 !$#title Die Primaerstrukltur des spezifischen Trypsininhibitors II !1(Kazal-Typ) aus Schweinepankreas. !$#cross-references MUID:71092915; PMID:5531651 !$#contents PSTI II !$#accession A91647 !'##molecule_type protein !'##residues 5-56 ##label TS2 REFERENCE A90646 !$#authors Menegatti, E.; Bortolotti, F.; Minchiotti, L.; de Marco, A. !$#journal Biochim. Biophys. Acta (1982) 707:50-58 !$#title Isolation and characterization of a new form of the porcine !1pancreatic secretory trypsin inhibitor. Biochemical studies !1and high-resolution (1)H-NMR. !$#cross-references MUID:83049107; PMID:7138878 !$#contents PSTI III !$#accession A90646 !'##molecule_type protein !'##residues 9-56 ##label MEN CLASSIFICATION #superfamily pancreatic secretory trypsin inhibitor; Kazal !1proteinase inhibitor homology KEYWORDS pancreas; serine proteinase inhibitor FEATURE !$7-56 #domain Kazal proteinase inhibitor homology #label !8KPI\ !$9-38,16-35,24-56 #disulfide_bonds #status experimental\ !$18 #inhibitory_site Lys (trypsin) #status experimental SUMMARY #length 56 #molecular-weight 6023 #checksum 3146 SEQUENCE /// ENTRY TIDGA #type complete TITLE pancreatic secretory trypsin inhibitor - dog ORGANISM #formal_name Canis lupus familiaris #common_name dog DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 16-Jul-1999 ACCESSIONS A01232 REFERENCE A01232 !$#authors Kikuchi, N.; Nagata, K.; Yoshida, N.; Tanaka, T.; Yamamoto, !1M.; Saitoh, Y. !$#journal FEBS Lett. (1985) 191:269-272 !$#title Purification and complete amino acid sequence of canine !1pancreatic secretory trypsin inhibitor. !$#cross-references MUID:86030679; PMID:4054311 !$#accession A01232 !'##molecule_type protein !'##residues 1-57 ##label KIK CLASSIFICATION #superfamily pancreatic secretory trypsin inhibitor; Kazal !1proteinase inhibitor homology KEYWORDS pancreas; serine proteinase inhibitor FEATURE !$8-57 #domain Kazal proteinase inhibitor homology #label !8KPI\ !$10-39,17-36,25-57 #disulfide_bonds #status predicted\ !$19 #inhibitory_site Lys (trypsin) #status predicted SUMMARY #length 57 #molecular-weight 6319 #checksum 5319 SEQUENCE /// ENTRY TIRT1 #type complete TITLE pancreatic secretory trypsin inhibitor I precursor - rat ALTERNATE_NAMES cholecystokinin-releasing peptide; monitor peptide ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jun-2000 ACCESSIONS S09602; A33292; A43972; S16223; S28946; S00633; A27111; !1I58414; I78898 REFERENCE S09602 !$#authors Fukuoka, S.I.; Scheele, G. !$#journal Nucleic Acids Res. (1989) 17:10111 !$#title Complementary nucleotide sequence for monitor peptide, a !1novel cholecystokinin-releasing peptide in the rat. !$#cross-references MUID:90098786; PMID:2602119 !$#accession S09602 !'##molecule_type mRNA !'##residues 1-79 ##label FUK !'##cross-references EMBL:M22162; NID:g205511; PIDN:AAA41629.1; !1PID:g205512 REFERENCE A33292 !$#authors Horii, A.; Tomita, N.; Yokouchi, H.; Doi, S.; Uda, K.; !1Ogawa, M.; Mori, T.; Matsubara, K. !$#journal Biochem. Biophys. Res. Commun. (1989) 162:151-159 !$#title On the cDNA's for two types of rat pancreatic secretory !1trypsin inhibitor. !$#cross-references MUID:89322236; PMID:2751646 !$#accession A33292 !'##molecule_type mRNA !'##residues 1-79 ##label HOR !'##cross-references GB:M27882; NID:g206464; PIDN:AAA41975.1; !1PID:g206465 REFERENCE A43972 !$#authors Fukuoka, S.I.; Scheele, G.A. !$#journal Pancreas (1990) 5:1-7 !$#title Rapid and selective cloning of monitor peptide, a novel !1cholecystokinin-releasing peptide, using minimal amino acid !1sequence and the polymerase chain reaction. !$#cross-references MUID:90083122; PMID:2293709 !$#accession A43972 !'##molecule_type mRNA !'##residues 1-79 ##label FU2 !'##cross-references GB:M35299; NID:g950097; PIDN:AAA74479.1; !1PID:g206467 !'##note a cDNA clone with a termination codon following residue 76 was !1also found REFERENCE S16223 !$#authors Tsuzuki, S.; Fushiki, T.; Kondo, A.; Murayama, H.; Sugimoto, !1E. !$#journal Eur. J. Biochem. (1991) 199:245-252 !$#title Effect of a high-protein diet on the gene expression of a !1trypsin-sensitive, cholecystokinin-releasing peptide !1(monitor peptide) in the pancreas. !$#cross-references MUID:91293130; PMID:2065678 !$#accession S16223 !'##molecule_type mRNA !'##residues 1-79 ##label TSU !'##cross-references EMBL:X59696; NID:g56694; PIDN:CAA42217.1; !1PID:g56695 REFERENCE S28946 !$#authors Tsuzuki, S.; Miura, Y.; Fushiki, T.; Oomori, T.; Satoh, T.; !1Natori, Y.; Sugimoto, E. !$#journal Biochim. Biophys. Acta (1992) 1132:199-202 !$#title Molecular cloning and characterization of genes encoding rat !1pancreatic cholecystokinin (CCK)-releasing peptide (monitor !1peptide) and pancreatic secretory trypsin inhibitor (PSTI). !$#cross-references MUID:93003324; PMID:1390891 !$#accession S28946 !'##molecule_type DNA !'##residues 1-79 ##label TS2 !'##cross-references DDBJ:D11321; NID:g220694; PIDN:BAA01944.1; !1PID:g220696 REFERENCE S00633 !$#authors Uda, K.I.; Ogawa, M.; Shibata, T.; Murata, A.; Mori, T.; !1Kikuchi, N.; Yoshida, N.; Tsunasawa, S.; Sakiyama, F. !$#journal Biol. Chem. Hoppe-Seyler (1988) 369(Suppl.):55-61 !$#title Purification, characterization and amino-acid sequencing of !1two pancreatic secretory trypsin inhibitors in rat !1pancreatic juice. !$#cross-references MUID:89076534; PMID:3202973 !$#accession S00633 !'##molecule_type protein !'##residues 19-79 ##label UDA REFERENCE A27111 !$#authors Iwai, K.; Fukuoka, S.I.; Fushiki, T.; Tsujikawa, M.; Hirose, !1M.; Tsunasawa, S.; Sakiyama, F. !$#journal J. Biol. Chem. (1987) 262:8956-8959 !$#title Purification and sequencing of a trypsin-sensitive !1cholecystokinin-releasing peptide from rat pancreatic juice. !1Its homology with pancreatic secretory trypsin inhibitor. !$#cross-references MUID:87250528; PMID:3597401 !$#accession A27111 !'##molecule_type protein !'##residues 19-56,'Z',58-77,'G',79 ##label IWA REFERENCE I58414 !$#authors Fukuoka, S. !$#journal Pancreas (1990) 4:1-7 !$#title Rapid and selective cloning of monitor peptide, a novel !1CCK-releasing peptide, using minimal amino acid sequence and !1the polymerase chain reaction (PCR). !$#accession I58414 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-79 ##label RES !'##cross-references GB:M35299; NID:g950097; PIDN:AAA74479.1; !1PID:g206467 !$#accession I78898 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 40-76 ##label RE2 !'##cross-references GB:M35300; NID:g206470; PIDN:AAA41977.1; !1PID:g206471 COMMENT This peptide stimulates cholecystokinin release from !1intestinal mucosal cells and DNA synthesis in fibroblasts. GENETICS !$#gene PSTI !$#introns 19/1; 29/3; 65/2 CLASSIFICATION #superfamily pancreatic secretory trypsin inhibitor; Kazal !1proteinase inhibitor homology KEYWORDS pancreas; serine proteinase inhibitor FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-79 #product pancreatic secretory trypsin inhibitor I !8#status experimental #label MAT\ !$30-79 #domain Kazal proteinase inhibitor homology #label !8KPI\ !$32-61,39-58,47-79 #disulfide_bonds #status predicted\ !$41 #inhibitory_site Arg (trypsin) #status predicted SUMMARY #length 79 #molecular-weight 8528 #checksum 6041 SEQUENCE /// ENTRY TIRT2 #type complete TITLE pancreatic secretory trypsin inhibitor II precursor - rat ALTERNATE_NAMES hepatic proteinase inhibitor ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jun-2000 ACCESSIONS B33292; S28947; S00634; S08982 REFERENCE A33292 !$#authors Horii, A.; Tomita, N.; Yokouchi, H.; Doi, S.; Uda, K.; !1Ogawa, M.; Mori, T.; Matsubara, K. !$#journal Biochem. Biophys. Res. Commun. (1989) 162:151-159 !$#title On the cDNA's for two types of rat pancreatic secretory !1trypsin inhibitor. !$#cross-references MUID:89322236; PMID:2751646 !$#accession B33292 !'##molecule_type mRNA !'##residues 1-79 ##label HOR !'##cross-references GB:M27883 REFERENCE S28946 !$#authors Tsuzuki, S.; Miura, Y.; Fushiki, T.; Oomori, T.; Satoh, T.; !1Natori, Y.; Sugimoto, E. !$#journal Biochim. Biophys. Acta (1992) 1132:199-202 !$#title Molecular cloning and characterization of genes encoding rat !1pancreatic cholecystokinin (CCK)-releasing peptide (monitor !1peptide) and pancreatic secretory trypsin inhibitor (PSTI). !$#cross-references MUID:93003324; PMID:1390891 !$#accession S28947 !'##molecule_type DNA !'##residues 1-79 ##label TSU !'##cross-references DDBJ:D11325; NID:g220885; PIDN:BAA01945.1; !1PID:g220887 REFERENCE S00633 !$#authors Uda, K.I.; Ogawa, M.; Shibata, T.; Murata, A.; Mori, T.; !1Kikuchi, N.; Yoshida, N.; Tsunasawa, S.; Sakiyama, F. !$#journal Biol. Chem. Hoppe-Seyler (1988) 369(Suppl.):55-61 !$#title Purification, characterization and amino-acid sequencing of !1two pancreatic secretory trypsin inhibitors in rat !1pancreatic juice. !$#cross-references MUID:89076534; PMID:3202973 !$#accession S00634 !'##molecule_type protein !'##residues 24-79 ##label UDA REFERENCE S08982 !$#authors Kido, H.; Yokogoshi, Y.; Katunuma, N. !$#journal Eur. J. Biochem. (1990) 188:501-506 !$#title A low-molecular-mass Kazal-type protease inhibitor isolated !1from rat hepatocytes is identical to rat pancreatic !1secretory trypsin inhibitor II. Purification and amino acid !1sequence. !$#cross-references MUID:90235819; PMID:2110056 !$#accession S08982 !'##molecule_type protein !'##residues 24-79 ##label KID GENETICS !$#introns 19/1; 29/3; 65/2 CLASSIFICATION #superfamily pancreatic secretory trypsin inhibitor; Kazal !1proteinase inhibitor homology KEYWORDS pancreas; serine proteinase inhibitor FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-79 #product pancreatic secretory trypsin inhibitor I !8#status experimental #label MAT\ !$30-79 #domain Kazal proteinase inhibitor homology #label !8KPI\ !$32-61,39-58,47-79 #disulfide_bonds #status predicted\ !$41 #inhibitory_site Arg (trypsin) #status predicted SUMMARY #length 79 #molecular-weight 8565 #checksum 4335 SEQUENCE /// ENTRY S01498 #type complete TITLE pancreatic secretory trypsin inhibitor precursor - mouse ALTERNATE_NAMES prostatic secretory glycoprotein p12 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS S01498; S18384 REFERENCE S01498 !$#authors Mills, J.S.; Needham, M.; Parker, M.G. !$#journal EMBO J. (1987) 6:3711-3717 !$#title A secretory protease inhibitor requires androgens for its !1expression in male sex accessory tissues but is expressed !1constitutively in pancreas. !$#cross-references MUID:88111560; PMID:3428272 !$#accession S01498 !'##molecule_type mRNA !'##residues 1-80 ##label MIL !'##cross-references EMBL:X06342; NID:g53686; PIDN:CAA29648.1; !1PID:g53687 !'##note the authors translated the codon ATA for residue 69 as Met REFERENCE S18384 !$#authors Lai, M.L.; Chen, S.W.; Chen, Y.H. !$#journal Arch. Biochem. Biophys. (1991) 290:265-271 !$#title Purification and characterization of a trypsin inhibitor !1from mouse seminal vesicle secretion. !$#cross-references MUID:92027737; PMID:1929395 !$#accession S18384 !'##molecule_type protein !'##residues 43-47;49-58;60-61;63-72 ##label LAI COMMENT The expression of this inhibitor is dependent upon !1testosterone in prostate gland, seminal vesicle, and !1coagulating gland. Expression is androgen-independent in !1pancreas. CLASSIFICATION #superfamily pancreatic secretory trypsin inhibitor; Kazal !1proteinase inhibitor homology KEYWORDS pancreas; prostate; seminal vesicle; serine proteinase !1inhibitor; testis FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-80 #product pancreatic secretory trypsin inhibitor !8#status predicted #label MAT\ !$31-80 #domain Kazal proteinase inhibitor homology #label !8KPI\ !$33-62,40-59,48-80 #disulfide_bonds #status predicted\ !$42 #inhibitory_site Arg (trypsin) #status predicted SUMMARY #length 80 #molecular-weight 8488 #checksum 4908 SEQUENCE /// ENTRY JU0152 #type complete TITLE acrosin/trypsin inhibitor precursor [validated] - human ALTERNATE_NAMES HUSI-II ORGANISM #formal_name Homo sapiens #common_name man DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 08-Dec-2000 ACCESSIONS JU0152; S13033; S11531 REFERENCE JU0152 !$#authors Moeritz, A.; Grzeschik, K.H.; Wingender, E.; Fink, E. !$#journal Gene (1993) 123:277-281 !$#title Organization and sequence of the gene encoding the human !1acrosin-trypsin inhibitor (HUSI-II). !$#cross-references MUID:93154598; PMID:8428671 !$#accession JU0152 !'##molecule_type DNA !'##residues 1-84 ##label MOE !'##cross-references GB:M91438; NID:g184478; PIDN:AAB59431.1; !1PID:g184479; GB:M84967 REFERENCE S13033 !$#authors Moeritz, A.; Lilja, H.; Fink, E. !$#journal FEBS Lett. (1991) 278:127-130 !$#title Molecular cloning and sequence analysis of the cDNA encoding !1the human acrosin-trypsin inhibitor (HUSI-II). !$#cross-references MUID:91130585; PMID:1704312 !$#accession S13033 !'##molecule_type mRNA !'##residues 1-84 ##label MO2 !'##cross-references GB:M91438; NID:g184478; PIDN:AAB59431.1; !1PID:g184479 REFERENCE S11531 !$#authors Fink, E.; Hehlein-Fink, C.; Eulitz, M. !$#journal FEBS Lett. (1990) 270:222-224 !$#title Amino acid sequence elucidation of human acrosin-trypsin !1inhibitor (HUSI-II) reveals that Kazal-type proteinase !1inhibitors are structurally related to beta-subunits of !1glycoprotein hormones. !$#cross-references MUID:91032019; PMID:2226783 !$#accession S11531 !'##molecule_type protein !'##residues 24-84 ##label FIN GENETICS !$#gene GDB:SPINK2 !'##cross-references GDB:138132 !$#map_position 4pter-4qter !$#introns 19/1; 33/3; 70/2 CLASSIFICATION #superfamily pancreatic secretory trypsin inhibitor; Kazal !1proteinase inhibitor homology KEYWORDS pyroglutamic acid; semen; serine proteinase inhibitor; !1sperm; testis FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-84 #product acrosin-trypsin inhibitor #status !8experimental #label MAT\ !$34-84 #domain Kazal proteinase inhibitor homology #label !8KPI\ !$24 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$36-66,44-63,52-84 #disulfide_bonds #status predicted\ !$46 #inhibitory_site Arg (acrosin, trypsin) #status !8predicted SUMMARY #length 84 #molecular-weight 9291 #checksum 5291 SEQUENCE /// ENTRY S29820 #type complete TITLE acrosin/trypsin inhibitor precursor - crab-eating macaque ORGANISM #formal_name Macaca fascicularis #common_name crab-eating macaque DATE 13-Jan-1995 #sequence_revision 14-Feb-1997 #text_change 16-Jul-1999 ACCESSIONS S29820 REFERENCE S29820 !$#authors Perry, A.C.F.; Jones, R.; Hall, L. !$#journal Biochim. Biophys. Acta (1993) 1172:159-160 !$#title Sequence analysis of monkey acrosin-trypsin inhibitor !1transcripts and their abundant expression in the epididymis. !$#cross-references MUID:93176800; PMID:8439554 !$#accession S29820 !'##molecule_type mRNA !'##residues 1-81 ##label PER !'##cross-references EMBL:X68331; NID:g296748; PIDN:CAA48408.1; !1PID:g296749 !'##experimental_source epididymis of adult COMMENT In this species, this protein occurs at high levels in !1epididymis and at low levels in testis. CLASSIFICATION #superfamily pancreatic secretory trypsin inhibitor; Kazal !1proteinase inhibitor homology KEYWORDS epididymis; semen; serine proteinase inhibitor FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-81 #product acrosin-trypsin inhibitor #status predicted !8#label MAT\ !$31-81 #domain Kazal proteinase inhibitor homology #label !8KPI\ !$33-63,41-60,49-81 #disulfide_bonds #status predicted\ !$43 #inhibitory_site Arg (acrosin, trypsin) #status !8predicted SUMMARY #length 81 #molecular-weight 9171 #checksum 9664 SEQUENCE /// ENTRY A34427 #type complete TITLE peptide PEC-60 precursor - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS A44041; A34427; S24956 REFERENCE A44041 !$#authors Metsis, M.; Cintra, A.; Solfrini, V.; Ernfors, P.; !1Bortolotti, F.; Morrasutti, D.G.; Ostenson, C.G.; Efendic, !1S.; Agerberth, B.; Mutt, V.; Persson, H.; Fuxe, K. !$#journal J. Biol. Chem. (1992) 267:19829-19832 !$#title Molecular cloning of PEC-60 and expression of its mRNA and !1peptide in the gastrointestinal tract and immune system. !$#cross-references MUID:93015834; PMID:1400298 !$#accession A44041 !'##molecule_type mRNA !'##residues 1-86 ##label MET !'##cross-references EMBL:X67109; NID:g2033; PIDN:CAA47482.1; PID:g2034 !'##note sequence extracted from NCBI backbone (NCBIP:115615) REFERENCE A34427 !$#authors Agerberth, B.; Soederling-Barros, J.; Joernvall, H.; Chen, !1Z.; Oestenson, C.G.; Efendic, S.; Mutt, V. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:8590-8594 !$#title Isolation and characterization of a 60-residue intestinal !1peptide structurally related to the pancreatic secretory !1type of trypsin inhibitor: influence on insulin secretion. !$#cross-references MUID:90046843; PMID:2573065 !$#accession A34427 !'##molecule_type protein !'##residues 27-86 ##label AGE COMMENT This peptide does not inhibit trypsin. Its biological !1function is unknown, although it inhibits glucose-induced !1insulin release from perfused pancreas. COMMENT This peptide is synthesized in duodenal goblet cells and in !1monocytes in bone marrow and blood. CLASSIFICATION #superfamily pancreatic secretory trypsin inhibitor; Kazal !1proteinase inhibitor homology KEYWORDS intestine; leukocyte; serine proteinase inhibitor FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-86 #product peptide PEC-60 #status experimental #label !8MAT\ !$35-86 #domain Kazal proteinase inhibitor homology #label !8KPI\ !$37-68,46-65 #disulfide_bonds #status predicted\ !$48 #inhibitory_site Arg (unidentified proteinase) !8#status predicted\ !$54-86 #disulfide_bonds #status experimental SUMMARY #length 86 #molecular-weight 9635 #checksum 7945 SEQUENCE /// ENTRY TIEEH #type complete TITLE proteinase inhibitor homolog - European eel ORGANISM #formal_name Anguilla anguilla #common_name European eel DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS S00630 REFERENCE S00630 !$#authors Conlon, J.M.; Thim, L. !$#journal Eur. J. Biochem. (1988) 174:149-153 !$#title A peptide from the eel pancreas with structural similarity !1to human pancreatic secretory trypsin inhibitor. !$#cross-references MUID:88225096; PMID:3371360 !$#accession S00630 !'##molecule_type protein !'##residues 1-61 ##label CON CLASSIFICATION #superfamily pancreatic secretory trypsin inhibitor; Kazal !1proteinase inhibitor homology KEYWORDS pancreas FEATURE !$10-61 #domain Kazal proteinase inhibitor homology #label !8KPI\ !$12-43,21-40,29-61 #disulfide_bonds #status predicted SUMMARY #length 61 #molecular-weight 6808 #checksum 6577 SEQUENCE /// ENTRY S00130 #type complete TITLE elastase inhibitor - snake-locks sea anemone ORGANISM #formal_name Anemonia sulcata #common_name snake-locks sea anemone DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS S00130 REFERENCE S00130 !$#authors Tschesche, H.; Kolkenbrock, H.; Bode, W. !$#journal Biol. Chem. Hoppe-Seyler (1987) 368:1297-1304 !$#title The covalent structure of the elastase inhibitor from !1Anemonia sulcata - a "non-classical" Kazal-type protein. !$#cross-references MUID:88106994; PMID:2892502 !$#accession S00130 !'##molecule_type protein !'##residues 1-48 ##label TSC CLASSIFICATION #superfamily pancreatic secretory trypsin inhibitor; Kazal !1proteinase inhibitor homology KEYWORDS serine proteinase inhibitor FEATURE !$2-48 #domain Kazal proteinase inhibitor homology #label !8KPI\ !$4-34,8-27,16-48 #disulfide_bonds #status experimental\ !$10 #inhibitory_site Met (elastase) #status predicted SUMMARY #length 48 #molecular-weight 5134 #checksum 8597 SEQUENCE /// ENTRY XTPG1 #type complete TITLE acrosin inhibitor A1 (PSTI type) - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 30-Nov-1980 #sequence_revision 30-Nov-1980 #text_change 16-Jul-1999 ACCESSIONS A01233 REFERENCE A94431 !$#authors Tschesche, H.; Kupfer, S.; Klauser, R.; Fink, E.; Fritz, H. !$#book Protides of the Biological Fluids, Proc. 23rd Colloq., !1Peeters, H., ed., pp.255-266, Pergamon Press, New York, 1976 !$#accession A01233 !'##molecule_type protein !'##residues 1-65 ##label TSC COMMENT Acrosin inhibitor A1 is one of several closely related !1inhibitors found in seminal plasma or spermatozoa. CLASSIFICATION #superfamily pancreatic secretory trypsin inhibitor; Kazal !1proteinase inhibitor homology KEYWORDS glycoprotein; semen; serine proteinase inhibitor; sperm; !1testis FEATURE !$5-57 #domain Kazal proteinase inhibitor homology #label !8KPI\ !$7-39,17-36,25-57 #disulfide_bonds #status experimental\ !$12,62 #binding_site carbohydrate (Ser) (covalent) #status !8predicted\ !$19 #inhibitory_site Arg (acrosin, trypsin) #status !8experimental SUMMARY #length 65 #molecular-weight 7595 #checksum 6319 SEQUENCE /// ENTRY XTBO1 #type complete TITLE acrosin inhibitor I (PSTI type) - bovine ALTERNATE_NAMES serine proteinase inhibitor ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 31-Mar-2000 ACCESSIONS A01234 REFERENCE A01234 !$#authors Meloun, B.; Cechova, D.; Jonakova, V. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1983) 364:1665-1670 !$#title Homologies in the structures of bull seminal plasma acrosin !1inhibitors and comparison with other homologous proteinase !1inhibitors of the Kazal type. !$#cross-references MUID:84133805; PMID:6365719 !$#accession A01234 !'##molecule_type protein !'##residues 1-63 ##label MEL CLASSIFICATION #superfamily pancreatic secretory trypsin inhibitor; Kazal !1proteinase inhibitor homology KEYWORDS semen; serine proteinase inhibitor; sperm; testis FEATURE !$12-61 #domain Kazal proteinase inhibitor homology #label !8KPI\ !$14-43,21-40,29-61 #disulfide_bonds #status predicted\ !$23 #inhibitory_site Arg (acrosin) #status predicted SUMMARY #length 63 #molecular-weight 7379 #checksum 4229 SEQUENCE /// ENTRY XTBO #type complete TITLE acrosin inhibitor II (PSTI type) - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Nov-1980 #sequence_revision 23-Oct-1981 #text_change 16-Jul-1999 ACCESSIONS A01235 REFERENCE A01235 !$#authors Cechova, D.; Meloun, B. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1979) 360:1497-1500 !$#title Differences in the evolution of seminal plasma acrosin !1inhibitors and pancreatic secretory trypsin inhibitors. !$#cross-references MUID:80048330; PMID:500016 !$#accession A01235 !'##molecule_type protein !'##residues 1-57 ##label CEC COMMENT This protein inhibits acrosin, trypsin, and chymotrypsin. CLASSIFICATION #superfamily pancreatic secretory trypsin inhibitor; Kazal !1proteinase inhibitor homology KEYWORDS pyroglutamic acid; semen; serine proteinase inhibitor; !1sperm; testis FEATURE !$5-56 #domain Kazal proteinase inhibitor homology #label !8KPI\ !$1 #modified_site pyrrolidone carboxylic acid (Gln) !8#status experimental\ !$7-39,17-36,25-56 #disulfide_bonds #status predicted\ !$19 #inhibitory_site Arg (acrosin, trypsin) #status !8predicted SUMMARY #length 57 #molecular-weight 6196 #checksum 3499 SEQUENCE /// ENTRY TIDGS #type complete TITLE proteinase inhibitor (PSTI type), submandibular - dog ORGANISM #formal_name Canis lupus familiaris #common_name dog DATE 30-Nov-1980 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS C29654; A01236 REFERENCE A94650 !$#authors Reisinger, P.W.M.; Hochstrasser, K.; Goettlicher, I.; !1Eulitz, M.; Wachter, E. !$#journal Biol. Chem. Hoppe-Seyler (1987) 368:717-726 !$#title The amino-acid sequences of the double-headed proteinase !1inhibitors from cat, lion and dog submandibular glands. !$#cross-references MUID:87299011; PMID:3304339 !$#accession C29654 !'##molecule_type protein !'##residues 1-115 ##label REI REFERENCE A91664 !$#authors Hochstrasser, K.; Bretzel, G.; Wachter, E.; Heindl, S. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1975) 356:1865-1877 !$#title The amino acid sequence of the double-headed proteinase !1inhibitor from canine submandibular glands, III. !$#cross-references MUID:76119551; PMID:1213682 !$#contents annotation !$#note sequence revised in reference A94650 !$#note three very similar inhibitors found in the submandibular !1glands are secreted into the saliva; the sequence shown is !1one of the two main inhibitors; the other differs from that !1shown in having 9-Lys CLASSIFICATION #superfamily submandibular proteinase inhibitor; Kazal !1proteinase inhibitor homology KEYWORDS duplication; saliva; serine proteinase inhibitor; !1submandibular gland FEATURE !$10-64 #domain Kazal proteinase inhibitor homology #label !8KP1\ !$66-115 #domain Kazal proteinase inhibitor homology #label !8KP2\ !$12-46,24-43,32-64, !$68-97,75-94,83-115 #disulfide_bonds #status predicted\ !$26 #inhibitory_site Arg (trypsin, plasmin) #status !8predicted\ !$77 #inhibitory_site Met (chymotrypsin, subtilisin, !8elastase) #status predicted SUMMARY #length 115 #molecular-weight 12774 #checksum 8955 SEQUENCE /// ENTRY S03371 #type complete TITLE proteinase inhibitor (PSTI type), submandibular - red fox ORGANISM #formal_name Vulpes vulpes #common_name red fox DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS S03371 REFERENCE S03371 !$#authors Reisinger, P.W.M.; Hochstrasser, K.; Wachter, E. !$#journal Protein Seq. Data Anal. (1988) 1:259-261 !$#title The amino-acid sequence of the double-headed proteinase !1inhibitor from fox (Vulpes vulpes) submandibular glands. !$#cross-references MUID:88276849; PMID:3393515 !$#accession S03371 !'##molecule_type protein !'##residues 1-115 ##label REI CLASSIFICATION #superfamily submandibular proteinase inhibitor; Kazal !1proteinase inhibitor homology KEYWORDS duplication; saliva; serine proteinase inhibitor; !1submandibular gland FEATURE !$10-64 #domain Kazal proteinase inhibitor homology #label !8KP1\ !$66-115 #domain Kazal proteinase inhibitor homology #label !8KP2\ !$12-46,24-43,32-64, !$68-97,75-94,83-115 #disulfide_bonds #status predicted\ !$26 #inhibitory_site Arg (trypsin, plasmin) #status !8predicted\ !$77 #inhibitory_site Met (chymotrypsin, subtilisin, !8elastase) #status predicted SUMMARY #length 115 #molecular-weight 12817 #checksum 9238 SEQUENCE /// ENTRY A29654 #type complete TITLE proteinase inhibitor (PSTI type), submandibular - cat ORGANISM #formal_name Felis silvestris catus #common_name domestic cat DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS A29654 REFERENCE A94650 !$#authors Reisinger, P.W.M.; Hochstrasser, K.; Goettlicher, I.; !1Eulitz, M.; Wachter, E. !$#journal Biol. Chem. Hoppe-Seyler (1987) 368:717-726 !$#title The amino-acid sequences of the double-headed proteinase !1inhibitors from cat, lion and dog submandibular glands. !$#cross-references MUID:87299011; PMID:3304339 !$#accession A29654 !'##molecule_type protein !'##residues 1-111 ##label REI CLASSIFICATION #superfamily submandibular proteinase inhibitor; Kazal !1proteinase inhibitor homology KEYWORDS duplication; saliva; serine proteinase inhibitor; !1submandibular gland FEATURE !$6-60 #domain Kazal proteinase inhibitor homology #label !8KP1\ !$62-111 #domain Kazal proteinase inhibitor homology #label !8KP2\ !$8-42,20-39,28-60, !$64-93,71-90,79-111 #disulfide_bonds #status predicted\ !$22 #inhibitory_site Lys (trypsin) #status predicted\ !$73 #inhibitory_site Met (chymotrypsin, elastase) #status !8predicted SUMMARY #length 111 #molecular-weight 12788 #checksum 8146 SEQUENCE /// ENTRY B29654 #type complete TITLE proteinase inhibitor (PSTI type), submandibular - lion ORGANISM #formal_name Panthera leo #common_name lion DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS B29654 REFERENCE A94650 !$#authors Reisinger, P.W.M.; Hochstrasser, K.; Goettlicher, I.; !1Eulitz, M.; Wachter, E. !$#journal Biol. Chem. Hoppe-Seyler (1987) 368:717-726 !$#title The amino-acid sequences of the double-headed proteinase !1inhibitors from cat, lion and dog submandibular glands. !$#cross-references MUID:87299011; PMID:3304339 !$#accession B29654 !'##molecule_type protein !'##residues 1-112 ##label REI CLASSIFICATION #superfamily submandibular proteinase inhibitor; Kazal !1proteinase inhibitor homology KEYWORDS duplication; saliva; serine proteinase inhibitor; !1submandibular gland FEATURE !$6-60 #domain Kazal proteinase inhibitor homology #label !8KP1\ !$62-111 #domain Kazal proteinase inhibitor homology #label !8KP2\ !$8-42,20-39,28-60, !$64-93,71-90,79-111 #disulfide_bonds #status predicted\ !$22 #inhibitory_site Lys (trypsin) #status predicted\ !$73 #inhibitory_site Met (chymotrypsin, elastase) #status !8predicted SUMMARY #length 112 #molecular-weight 12740 #checksum 2996 SEQUENCE /// ENTRY TICHM #type complete TITLE ovomucoid precursor - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Nov-1980 #sequence_revision 30-Nov-1980 #text_change 18-Jun-1999 ACCESSIONS A92754; A90514; B90514; A92242; A94438; I50401; A01239; !1A26475; A30218 REFERENCE A92754 !$#authors Catterall, J.F.; Stein, J.P.; Kristo, P.; Means, A.R.; !1O'Malley, B.W. !$#journal J. Cell Biol. (1980) 87:480-487 !$#title Primary sequence of ovomucoid messenger RNA as determined !1from cloned complementary DNA. !$#cross-references MUID:81047092; PMID:7430252 !$#accession A92754 !'##molecule_type mRNA !'##residues 1-210 ##label CAT REFERENCE A90514 !$#authors Kato, I.; Schrode, J.; Kohr, W.J.; Laskowski Jr., M. !$#journal Biochemistry (1987) 26:193-201 !$#title Chicken ovomucoid: determination of its amino acid sequence, !1determination of the trypsin reactive site, and preparation !1of all three of its domains. !$#cross-references MUID:87157614; PMID:3548816 !$#contents inhibitory site !$#accession A90514 !'##molecule_type protein !'##residues 1-210 ##label KAT1 !$#accession B90514 !'##molecule_type protein !'##residues 1-157,160-210 ##label KAT2 REFERENCE A92242 !$#authors Thibodeau, S.N.; Palmiter, R.D.; Walsh, K.A. !$#journal J. Biol. Chem. (1978) 253:9018-9023 !$#title Precursor of egg white ovomucoid. Amino acid sequence of an !1NH-2-terminal extension. !$#cross-references MUID:79067791; PMID:721826 !$#accession A92242 !'##molecule_type protein !'##residues 1-44 ##label THI !'##note this precursor was synthesized in a cell-free system directed !1by ovomucoid mRNA; the initiator methionine is cleaved !1during cell-free synthesis REFERENCE A94438 !$#authors Kato, I.; Kohr, W.J.; Laskowski Jr., M. !$#book Regulatory Proteolytic Enzymes and Their Inhibitors, !1Magnusson, S., Ottesen, M., Foltmann, B., Dano, K., and !1Neurath, H., eds., pp.197-206, Pergamon Press, New York, !11978 !$#title Evolution of avian ovomucoids. !$#accession A94438 !'##molecule_type protein !'##residues 25-61,'N',63,'E',65-107,'T',109-149,'E',151-210 ##label !1KAT3 REFERENCE A90292 !$#authors Beeley, J.G. !$#journal Biochem. J. (1976) 159:335-345 !$#title Location of the carbohydrate groups of ovomucoid. !$#cross-references MUID:77065162; PMID:999651 !$#contents annotation; carbohydrate binding sites REFERENCE I50377 !$#authors Buell, G.N.; Wickens, M.P.; Carbon, J.; Schimke, R.T. !$#journal J. Biol. Chem. (1979) 254:9277-9283 !$#title Isolation of recombinant plasmids bearing cDNA to hen !1ovomucoid and lysozyme mRNAs. !$#cross-references MUID:80006645; PMID:383714 !$#accession I50401 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 187-210 ##label BUE !'##cross-references GB:M10639; NID:g212487; PIDN:AAA48995.1; !1PID:g212488 CLASSIFICATION #superfamily ovomucoid; Kazal proteinase inhibitor homology KEYWORDS alternative splicing; egg white; glycoprotein; serine !1proteinase inhibitor FEATURE !$1-24 #domain signal sequence #status experimental #label !8SIG\ !$25-210 #product ovomucoid #status experimental #label MAT1\ !$25-157,160-210 #product ovomucoid short form #status experimental !8#label MAT2\ !$27-86 #domain Kazal proteinase inhibitor homology #label !8KPI1\ !$92-151 #domain Kazal proteinase inhibitor homology #label !8KPI2\ !$160-210 #domain Kazal proteinase inhibitor homology #label !8KPI3\ !$29-68,46-65,54-86, !$94-133,111-130, !$119-151,162-192, !$170-189,178-210 #disulfide_bonds #status predicted\ !$34,77,93,99 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$48 #inhibitory_site Lys (lysine endopeptidase C) #status !8predicted\ !$113 #inhibitory_site Arg (trypsin) #status experimental\ !$172 #inhibitory_site Ala (chymotrypsin, proteinase B) !8#status predicted\ !$182 #binding_site carbohydrate (Asn) (covalent) #status !8absent\ !$199 #binding_site carbohydrate (Asn) (covalent) (partial) !8#status experimental SUMMARY #length 210 #molecular-weight 22591 #checksum 1658 SEQUENCE /// ENTRY TIQJM #type complete TITLE ovomucoid - Japanese quail (tentative sequence) ORGANISM #formal_name Coturnix coturnix japonica #common_name Japanese quail DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 31-Mar-2000 ACCESSIONS B94430; A94430; B90515; A90515; B94438; A01237; C31442; !1D31442 REFERENCE A94430 !$#authors Kato, I.; Schrode, J.; Wilson, K.A.; Laskowski Jr., M. !$#book Protides of the Biological Fluids, Proc. 23rd Colloq., !1Peeters, H., ed., pp.235-243, Pergamon Press, New York, 1976 !$#contents active sites !$#note quail ovomucoid contains three homology regions, each !1related to pancreatic secretory trypsin inhibitor; the !1second and third regions inhibit trypsin; the first does not !1inhibit any tested proteinase !$#accession B94430 !'##molecule_type protein !'##residues 1-186 ##label KAT1 !$#accession A94430 !'##molecule_type protein !'##residues 1-161,'G',163-186 ##label KAT2 REFERENCE A90515 !$#authors Laskowski Jr., M.; Kato, I.; Ardelt, W.; Cook, J.; Denton, !1A.; Empie, M.W.; Kohr, W.J.; Park, S.J.; Parks, K.; !1Schatzley, B.L.; Schoenberger, O.L.; Tashiro, M.; Vichot, !1G.; Whatley, H.E.; Wieczorek, A.; Wieczorek, M. !$#journal Biochemistry (1987) 26:202-221 !$#title Ovomucoid third domains from 100 avian species: isolation, !1sequences, and hypervariability of enzyme-inhibitor contact !1residues. !$#cross-references MUID:87157615; PMID:3828298 !$#accession B90515 !'##molecule_type protein !'##residues 131-186 ##label LAS1 !'##note the authors designate this sequence with the code OMJPQS !$#accession A90515 !'##molecule_type protein !'##residues 131-161,'G',163-186 ##label LAS2 !'##note the authors designate this sequence with the code OMJPQG REFERENCE A94438 !$#authors Kato, I.; Kohr, W.J.; Laskowski Jr., M. !$#book Regulatory Proteolytic Enzymes and Their Inhibitors, !1Magnusson, S., Ottesen, M., Foltmann, B., Dano, K., and !1Neurath, H., eds., pp.197-206, Pergamon Press, New York, !11978 !$#title Evolution of avian ovomucoids. !$#accession B94438 !'##molecule_type protein !'##residues 1-186 ##label KA2 REFERENCE A92280 !$#authors Bogard Jr., W.C.; Kato, I.; Laskowski Jr., M. !$#journal J. Biol. Chem. (1980) 255:6569-6574 !$#title A Ser(162)/Gly(162) polymorphism in Japanese quail !1ovomucoid. !$#cross-references MUID:80227804; PMID:6771272 !$#contents annotation !$#note this polymorphism is the result of two allelic, autosomal !1genes at a single locus REFERENCE A92885 !$#authors Papamokos, E.; Weber, E.; Bode, W.; Huber, R.; Empie, M.W.; !1Kato, I.; Laskowski Jr., M. !$#journal J. Mol. Biol. (1982) 158:515-537 !$#title Crystallographic refinement of Japanese quail ovomucoid, a !1Kazal-type inhibitor, and model building studies of !1complexes with serine proteases. !$#cross-references MUID:83033622; PMID:6752426 !$#contents annotation; X-ray crystallography, 1.9 angstroms !$#note structure of the third domain was determined REFERENCE A90292 !$#authors Beeley, J.G. !$#journal Biochem. J. (1976) 159:335-345 !$#title Location of the carbohydrate groups of ovomucoid. !$#cross-references MUID:77065162; PMID:999651 !$#contents annotation; carbohydrate binding sites CLASSIFICATION #superfamily ovomucoid; Kazal proteinase inhibitor homology KEYWORDS egg white; glycoprotein; serine proteinase inhibitor FEATURE !$3-62 #domain Kazal proteinase inhibitor homology #label !8KPI1\ !$68-127 #domain Kazal proteinase inhibitor homology #label !8KPI2\ !$136-186 #domain Kazal proteinase inhibitor homology #label !8KPI3\ !$5-44,22-41,30-62, !$70-109,87-106, !$95-127 #disulfide_bonds #status predicted\ !$10,53,75 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$24 #inhibitory_site Asp (unidentified proteinase) !8#status predicted\ !$89 #inhibitory_site Lys (trypsin) #status predicted\ !$138-168,146-165, !$154-186 #disulfide_bonds #status experimental\ !$148 #inhibitory_site Lys (trypsin) #status experimental\ !$175 #binding_site carbohydrate (Asn) (covalent) (partial) !8#status experimental SUMMARY #length 186 #molecular-weight 20477 #checksum 5845 SEQUENCE /// ENTRY TITKM #type complete TITLE ovomucoid - turkey (tentative sequence) ORGANISM #formal_name Meleagris gallopavo #common_name common turkey DATE 30-Nov-1980 #sequence_revision 30-Nov-1980 #text_change 31-Mar-2000 ACCESSIONS A01238; A60786; G31447; A20337 REFERENCE A94438 !$#authors Kato, I.; Kohr, W.J.; Laskowski Jr., M. !$#book Regulatory Proteolytic Enzymes and Their Inhibitors, !1Magnusson, S., Ottesen, M., Foltmann, B., Dano, K., and !1Neurath, H., eds., pp.197-206, Pergamon Press, New York, !11978 !$#title Evolution of avian ovomucoids. !$#contents sequence and active sites !$#accession A01238 !'##molecule_type protein !'##residues 1-185 ##label KAT REFERENCE A60786 !$#authors Risley, J.M.; Van Etten, R.L. !$#journal Carbohydr. Res. (1986) 147:21-29 !$#title Structures of the carbohydrate moiety attached to one site !1in the first domain of turkey ovomucoid: elucidation by !1H-N.M.R. spectroscopy. !$#cross-references MUID:86189746; PMID:3698056 !$#accession A60786 !'##molecule_type protein !'##residues 49-56 ##label RIS REFERENCE A90515 !$#authors Laskowski Jr., M.; Kato, I.; Ardelt, W.; Cook, J.; Denton, !1A.; Empie, M.W.; Kohr, W.J.; Park, S.J.; Parks, K.; !1Schatzley, B.L.; Schoenberger, O.L.; Tashiro, M.; Vichot, !1G.; Whatley, H.E.; Wieczorek, A.; Wieczorek, M. !$#journal Biochemistry (1987) 26:202-221 !$#title Ovomucoid third domains from 100 avian species: isolation, !1sequences, and hypervariability of enzyme-inhibitor contact !1residues. !$#cross-references MUID:87157615; PMID:3828298 !$#accession G31447 !'##molecule_type protein !'##residues 130-185 ##label LAS !'##note the authors designate this sequence with the code OMTKY3 REFERENCE A90474 !$#authors Read, R.J.; Fujinaga, M.; Sielecki, A.R.; James, M.N.G. !$#journal Biochemistry (1983) 22:4420-4433 !$#title Structure of the complex of Streptomyces griseus protease B !1and the third domain of the turkey ovomucoid inhibitor at !11.8-angstrom resolution. !$#cross-references MUID:84024570; PMID:6414511 !$#contents annotation; X-ray crystallography, 1.8 angstroms !$#note structure of the third domain complexed with Streptomyces !1griseus protease B CLASSIFICATION #superfamily ovomucoid; Kazal proteinase inhibitor homology KEYWORDS egg white; glycoprotein; serine proteinase inhibitor FEATURE !$3-61 #domain Kazal proteinase inhibitor homology #label !8KPI1\ !$67-126 #domain Kazal proteinase inhibitor homology #label !8KPI2\ !$135-185 #domain Kazal proteinase inhibitor homology #label !8KPI3\ !$5-43,22-40,30-61, !$69-108,86-105, !$94-126 #disulfide_bonds #status predicted\ !$10,74 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$52,174 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$88 #inhibitory_site Lys (trypsin) #status experimental\ !$137-167,145-164, !$153-185 #disulfide_bonds #status experimental\ !$147 #inhibitory_site Leu (chymotrypsin, elastase, !8proteinase A, proteinase B, subtilisin) #status !8experimental\ !$157 #binding_site carbohydrate (Asn) (covalent) #status !8absent SUMMARY #length 185 #molecular-weight 20155 #checksum 3132 SEQUENCE /// ENTRY A26730 #type complete TITLE ovoinhibitor precursor [validated] - chicken CONTAINS serine proteinase inhibitor (Kazal type) ORGANISM #formal_name Gallus gallus #common_name chicken DATE 18-Aug-2000 #sequence_revision 18-Aug-2000 #text_change 01-Sep-2000 ACCESSIONS A26730 REFERENCE A26730 !$#authors Scott, M.J.; Huckaby, C.S.; Kato, I.; Kohr, W.J.; Laskowski !1Jr., M.; Tsai, M.J.; O'Malley, B.W. !$#journal J. Biol. Chem. (1987) 262:5899-5907 !$#title Ovoinhibitor introns specify functional domains as in the !1related and linked ovomucoid gene. !$#cross-references MUID:87194792; PMID:3571241 !$#accession A26730 !'##molecule_type mRNA; protein !'##residues 1-472 ##label SCO !'##cross-references GB:M16141; NID:g212483; PIDN:AAA48994.1; !1PID:g212485 !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing COMMENT This is a major inhibitor in blood plasma and also occurs in !1egg white. CLASSIFICATION #superfamily chicken ovoinhibitor; Kazal proteinase !1inhibitor homology KEYWORDS duplication; egg white; plasma; serine proteinase inhibitor FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-472 #product ovoinhibitor #status experimental #label !8MAT\ !$26-85 #domain Kazal proteinase inhibitor homology #label !8KPI1\ !$92-150 #domain Kazal proteinase inhibitor homology #label !8KPI2\ !$157-216 #domain Kazal proteinase inhibitor homology #label !8KPI3\ !$223-282 #domain Kazal proteinase inhibitor homology #label !8KPI4\ !$289-347 #domain Kazal proteinase inhibitor homology #label !8KPI5\ !$354-413 #domain Kazal proteinase inhibitor homology #label !8KPI6\ !$420-472 #domain Kazal proteinase inhibitor homology #label !8KPI7\ !$28-67,45-64,53-85, !$94-132,110-129, !$118-150,159-198, !$176-195,184-216, !$225-264,242-261, !$250-282,291-329, !$307-326,315-347, !$356-395,373-392, !$381-413,422-454, !$432-451,440-472 #disulfide_bonds #status predicted\ !$47 #inhibitory_site Arg (serine proteinase) #status !8predicted\ !$112 #inhibitory_site Arg (serine proteinase) #status !8predicted\ !$178 #inhibitory_site Arg (serine proteinase) #status !8predicted\ !$244 #inhibitory_site Arg (serine proteinase) #status !8predicted\ !$309 #inhibitory_site Phe (serine proteinase) #status !8predicted\ !$375 #inhibitory_site Met (serine proteinase) #status !8predicted\ !$434 #inhibitory_site Met (serine proteinase) #status !8predicted SUMMARY #length 472 #molecular-weight 51919 #checksum 9414 SEQUENCE /// ENTRY XSSMA #type complete TITLE subtilisin inhibitor precursor (PSTI type) - Streptomyces albogriseolus ORGANISM #formal_name Streptomyces albogriseolus DATE 24-Apr-1984 #sequence_revision 30-Jun-1992 #text_change 16-Jun-2000 ACCESSIONS JX0066; PC1264; A91934; A91957; A01240 REFERENCE JX0066 !$#authors Obata, S.; Taguchi, S.; Kumagai, I.; Miura, K. !$#journal J. Biochem. (1989) 105:367-371 !$#title Molecular cloning and nucleotide sequence determination of !1gene encoding Streptomyces subtilisin inhibitor (SSI). !$#cross-references MUID:89278057; PMID:2732212 !$#accession JX0066 !'##molecule_type mRNA !'##residues 1-144 ##label OBA !'##cross-references GB:D00402; NID:g217025; PIDN:BAA00305.1; !1PID:g217026 REFERENCE PC1260 !$#authors Taguchi, S.; Kikuchi, H.; Kojima, S.; Kumagai, I.; Nakase, !1T.; Miura, K.; Momose, H. !$#journal Biosci. Biotechnol. Biochem. (1993) 57:522-524 !$#title High frequency of SSI-like protease inhibitors among !1Streptomyces. !$#cross-references MUID:93222542; PMID:7763545 !$#accession PC1264 !'##molecule_type protein !'##residues 32-71 ##label TAG !'##experimental_source strain S-3253 REFERENCE A91934 !$#authors Ikenaka, T.; Odani, S.; Sakai, M.; Nabeshima, Y.; Sato, S.; !1Murao, S. !$#journal J. Biochem. (1974) 76:1191-1209 !$#title Amino acid sequence of an alkaline proteinase inhibitor !1(Streptomyces subtilisin inhibitor) from Streptomyces !1albogriseolus S-3253. !$#cross-references MUID:75133416; PMID:4376147 !$#accession A91934 !'##molecule_type protein !'##residues 32-141,'AF',144 ##label IKE !'##experimental_source strain S-3253 REFERENCE A91957 !$#authors Sakai, M.; Odani, S.; Ikenaka, T. !$#journal J. Biochem. (1980) 87:891-898 !$#title Importance of the carboxyl-terminal four amino acid residues !1in the inhibitory activity of Streptomyces subtilisin !1inhibitor (with a revision of its carboxyl-terminal !1sequence). !$#cross-references MUID:80227614; PMID:6993452 !$#accession A91957 !'##molecule_type protein !'##residues 141-144 ##label SAK REFERENCE A93205 !$#authors Mitsui, Y.; Satow, Y.; Watanabe, Y.; Hirono, S.; Iitaka, Y. !$#journal Nature (1979) 277:447-452 !$#title Crystal structures of Streptomyces subtilisin inhibitor and !1its complex with subtilisin BPN'. !$#cross-references MUID:79114456; PMID:763329 !$#contents annotation; X-ray crystallography, 2.6 angstroms COMMENT This inhibitor may be distantly related to the PSTI-type !1proteinase inhibitors. CLASSIFICATION #superfamily plasminostreptin KEYWORDS homodimer; serine proteinase inhibitor; tandem repeat FEATURE !$1-31 #domain signal sequence #status predicted #label SIG\ !$32-144 #product subtilisin inhibitor (PSTI type) #status !8experimental #label MAT\ !$33-43 #region 5-residue repeats\ !$66-81,102-132 #disulfide_bonds #status experimental\ !$104 #inhibitory_site Met (subtilisin) #status !8experimental SUMMARY #length 144 #molecular-weight 14312 #checksum 5140 SEQUENCE /// ENTRY XFSMF #type complete TITLE plasminostreptin (PSTI-type proteinase inhibitor) - Streptomyces "antifibrinolyticus" ORGANISM #formal_name Streptomyces "antifibrinolyticus" DATE 30-Nov-1980 #sequence_revision 30-Nov-1980 #text_change 07-May-1999 ACCESSIONS A01241; PC1260 REFERENCE A01241 !$#authors Sugino, H.; Kakinuma, A.; Iwanaga, S. !$#journal J. Biol. Chem. (1978) 253:1546-1555 !$#title Plasminostreptin, a protein proteinase inhibitor produced by !1Streptomyces antifibrinolyticus. !$#cross-references MUID:78109517; PMID:627554 !$#accession A01241 !'##molecule_type protein !'##residues 1-109 ##label SUG REFERENCE PC1260 !$#authors Taguchi, S.; Kikuchi, H.; Kojima, S.; Kumagai, I.; Nakase, !1T.; Miura, K.; Momose, H. !$#journal Biosci. Biotechnol. Biochem. (1993) 57:522-524 !$#title High frequency of SSI-like protease inhibitors among !1Streptomyces. !$#cross-references MUID:93222542; PMID:7763545 !$#accession PC1260 !'##molecule_type protein !'##residues 1-36 ##label TAG !'##experimental_source strain 7351 COMMENT Plasminostreptin inhibits plasmin, trypsin, subtilisin, and !1other microbial alkaline proteases. COMMENT This inhibitor may be distantly related to the PSTI-type !1proteinase inhibitors. CLASSIFICATION #superfamily plasminostreptin KEYWORDS serine proteinase inhibitor FEATURE !$31-46,67-97 #disulfide_bonds #status experimental\ !$69 #inhibitory_site Lys (trypsin) #status experimental SUMMARY #length 109 #molecular-weight 11399 #checksum 8843 SEQUENCE /// ENTRY XHHU3 #type complete TITLE antithrombin III precursor [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 05-Apr-1983 #sequence_revision 05-Apr-1983 #text_change 08-Dec-2000 ACCESSIONS A49494; A93453; A93943; A92431; A33305; A94445; A34190; !1S02530; S63600; I37191; A29371; I52399; I65277; I65278; !1I65279; S10716; A44935; B44935; I59610; I81229; A01242; !1I37192; S36128 REFERENCE A49494 !$#authors Olds, R.J.; Lane, D.A.; Chowdhury, V.; De Stefano, V.; !1Leone, G.; Thein, S.L. !$#journal Biochemistry (1993) 32:4216-4224 !$#title Complete nucleotide sequence of the antithrombin gene: !1evidence for homologous recombination causing thrombophilia. !$#cross-references MUID:93237227; PMID:8476848 !$#accession A49494 !'##molecule_type DNA !'##residues 1-464 ##label OLD !'##cross-references EMBL:X68793; NID:g28906; PIDN:CAA48690.1; !1PID:g28907 !'##note sequence extracted from NCBI backbone (NCBIN:130247, !1NCBIP:130248) REFERENCE A93453 !$#authors Bock, S.C.; Wion, K.L.; Vehar, G.A.; Lawn, R.M. !$#journal Nucleic Acids Res. (1982) 10:8113-8125 !$#title Cloning and expression of the cDNA for human antithrombin !1III. !$#cross-references MUID:83143280; PMID:6298709 !$#accession A93453 !'##molecule_type mRNA !'##residues 1-464 ##label BOC1 !'##cross-references GB:L00190; GB:J00102; GB:J00103; GB:J00104; !1NID:g179128; PIDN:AAB40025.1; PID:g179130 REFERENCE A93943 !$#authors Chandra, T.; Stackhouse, R.; Kidd, V.J.; Woo, S.L.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:1845-1848 !$#title Isolation and sequence characterization of a cDNA clone of !1human antithrombin III. !$#cross-references MUID:83169777; PMID:6572945 !$#accession A93943 !'##molecule_type mRNA !'##residues 1-464 ##label CHA !'##cross-references GB:L00190; GB:J00102; GB:J00103; GB:J00104; !1NID:g179128; PIDN:AAB40025.1; PID:g179130 REFERENCE A92431 !$#authors Prochownik, E.V.; Markham, A.F.; Orkin, S.H. !$#journal J. Biol. Chem. (1983) 258:8389-8394 !$#title Isolation of a cDNA clone for human antithrombin III. !$#cross-references MUID:83238456; PMID:6305982 !$#accession A92431 !'##molecule_type mRNA !'##residues 42-96,'R',98-464 ##label PRO !'##note the authors translated the codon GAC for residue 206 as Asn, !1GGC for residue 298 as Glu, and GGC for residue 411 as Glu REFERENCE A33305 !$#authors Chang, J.Y. !$#journal J. Biol. Chem. (1989) 264:3111-3115 !$#title Binding of heparin to human antithrombin III activates !1selective chemical modification at lysine 236. Lys-107, !1Lys-125, and Lys-136 are situated within the heparin-binding !1site of antithrombin III. !$#cross-references MUID:89123426; PMID:2492530 !$#accession A33305 !'##molecule_type protein !'##residues 90-105;124-143;147-161;165-171;268-273;381-402;446-457 !1##label CH2 REFERENCE A94445 !$#authors Petersen, T.E.; Dudek-Wojciechowska, G.; Sottrup-Jensen, L.; !1Magnusson, S. !$#book The Physiological Inhibitors of Blood Coagulation and !1Fibrinolysis, Collen, D., Wiman, B., and Verstraete, M., !1eds., pp.43-54, Elsevier/North Holland Biomedical Press, !1Amsterdam, 1979 !$#title Primary structure of antithrombin-III (heparin cofactor). !1Partial homology between alpha-1-antitrypsin and !1antithrombin-III. !$#accession A94445 !'##molecule_type protein !'##residues 33-68,'QE',71-242;243-245,248-250;254-464 ##label PET !'##note carbohydrate-binding site and disulfide bonds REFERENCE A34190 !$#authors Zettlmeissl, G.; Conradt, H.S.; Nimtz, M.; Karges, H.E. !$#journal J. Biol. Chem. (1989) 264:21153-21159 !$#title Characterization of recombinant human antithrombin III !1synthesized in Chinese hamster ovary cells. !$#cross-references MUID:90078215; PMID:2592368 !$#accession A34190 !'##molecule_type protein !'##residues 33-39 ##label ZET !'##experimental_source recombinant protein from Chinese hamster ovary !1(CHO) cells REFERENCE S02530 !$#authors Liu, C.S.; Chang, J.Y. !$#journal Eur. J. Biochem. (1987) 167:247-252 !$#title Probing the heparin-binding domain of human antithrombin III !1with V8 protease. !$#cross-references MUID:87304255; PMID:3305015 !$#accession S02530 !'##status preliminary !'##molecule_type protein !'##residues 33-39,'X',41-42;67-77,'XX',80-88,'X', !190-92;137-142;189-202;210-214,'X';265-266,'X', !1268-269;407-423 ##label LIU REFERENCE S63599 !$#authors Chang, W.S.W.; Wardell, M.R.; Lomas, D.A.; Carrell, R.W. !$#journal Biochem. J. (1996) 314:647-653 !$#title Probing serpin reactive-loop conformations by proteolytic !1cleavage. !$#cross-references MUID:96239126; PMID:8670081 !$#accession S63600 !'##status preliminary !'##molecule_type protein !'##residues 414-428 ##label CH3 REFERENCE I37191 !$#authors Bock, S.C.; Levitan, D.J. !$#journal Nucleic Acids Res. (1983) 11:8569-8582 !$#title Characterization of an unusual DNA length polymorphism 5' to !1the human antithrombin III gene. !$#cross-references MUID:84169500; PMID:6672771 !$#accession I37191 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-14 ##label BOC2 !'##cross-references EMBL:X00237; NID:g28917; PIDN:CAA25059.1; !1PID:g28918; EMBL:X00238; NID:g28919; PID:g28920 REFERENCE A29371 !$#authors Koide, T.; Odani, S.; Takahashi, K.; Ono, T.; Sakuragawa, N. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:289-293 !$#title Antithrombin III Toyama: replacement of arginine-47 by !1cysteine in hereditary abnormal antithrombin III that lacks !1heparin-binding ability. !$#cross-references MUID:84119472; PMID:6582486 !$#accession A29371 !'##molecule_type protein !'##residues 53-68,'QE',71-78,'C',80-135 ##label KOI !'##note variant Toyama with a substitution of Cys for Arg-79 and !1consequently cannot bind heparin REFERENCE I52399 !$#authors Bock, S.C.; Marrinan, J.A.; Radziejewska, E. !$#journal Biochemistry (1988) 27:6171-6178 !$#title Antithrombin III Utah: proline-407 to leucine mutation in a !1highly conserved region near the inhibitor reactive site. !$#cross-references MUID:89050967; PMID:3191114 !$#note a published erratum appears in Biochemistry 28, 3628 1989 !$#accession I52399 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 137-208 ##label BOC3 !'##cross-references GB:M21643; NID:g179147; PIDN:AAA51793.1; !1PID:g457132 !$#accession I65277 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 137-254 ##label BOC4 !'##cross-references GB:M21644; NID:g179148; PIDN:AAA51794.1; !1PID:g179151 !$#accession I65278 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 407-464 ##label BOC5 !'##cross-references GB:M21645; NID:g179149; PIDN:AAA51795.1; !1PID:g179152 !$#accession I65279 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-438,'L',440-464 ##label BOC6 !'##cross-references GB:M21642; NID:g179159; PIDN:AAA51796.1; !1PID:g179161 !'##note mutant Utah REFERENCE S10716 !$#authors Borg, J.Y.; Brennan, S.O.; Carrell, R.W.; George, P.; Perry, !1D.J.; Shaw, J. !$#journal FEBS Lett. (1990) 266:163-166 !$#title Antithrombin rouen-IV 24 Arg->Cys. The amino-terminal !1contribution to heparin binding. !$#cross-references MUID:90306344; PMID:2365065 !$#accession S10716 !'##molecule_type protein !'##residues 53-61 ##label BOR !'##note variant form Rouen-IV, 56-Cys, was also sequenced REFERENCE A44935 !$#authors Grundy, C.B.; Thomas, F.; Millar, D.S.; Krawczak, M.; !1Melissari, E.; Lindo, V.; Moffat, E.; Kakkar, V.V.; Cooper, !1D.N. !$#journal Blood (1991) 78:1027-1032 !$#title Recurrent deletion in the human antithrombin III gene. !$#cross-references MUID:91329813; PMID:1868237 !$#accession A44935 !'##molecule_type DNA !'##residues 271-276,'GRVQHL' ##label GR1 !'##cross-references GB:S49757; NID:g233568; PIDN:AAB19467.1; !1PID:g233569 !'##experimental_source antithrombin III deficiency patient 1 !'##note sequence extracted from NCBI backbone (NCBIN:49757, !1NCBIP:49758) !$#accession B44935 !'##molecule_type DNA !'##residues 271-276,'VVFSIYDVPGRQVPLSARG' ##label GR2 !'##cross-references GB:S49759; NID:g233570; PIDN:AAB19468.1; !1PID:g233571 !'##experimental_source antithrombin III deficiency patient 2 !'##note sequence extracted from NCBI backbone (NCBIN:49759, !1NCBIP:49760) !'##note different frameshift mutations at an identical site in !1unrelated patients suggests a mutational hot spot REFERENCE I59610 !$#authors Daly, M.; Perry, D.J.; Harper, P.L.; Daly, H.M.; Roques, !1A.W.; Carrell, R.W. !$#journal Thromb. Haemost. (1992) 67:521-525 !$#title Insertions/deletions in the antithrombin gene: 3 mutations !1associated with non-expression. !$#cross-references MUID:92390894; PMID:1325679 !$#accession I59610 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 79,'CLGTVQGQFPLCYHFLSAPGRFQE' ##label DAL1 !'##cross-references GB:S43612; NID:g254806; PIDN:AAB23132.1; !1PID:g254807 !'##note frameshift mutant, patient 1 !$#accession I81229 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 401,'RHFLR' ##label DAL2 !'##cross-references GB:S43621; NID:g254810; PIDN:AAB23134.1; !1PID:g254811 !'##note frameshift mutant, patient 3 REFERENCE A91287 !$#authors Bjork, I.; Danielsson, A.; Fenton II, J.W.; Jornvall, H. !$#journal FEBS Lett. (1981) 126:257-260 !$#title The site in human antithrombin for functional proteolytic !1cleavage by human thrombin. !$#cross-references MUID:81212814; PMID:7238875 !$#contents annotation; inhibitory site REFERENCE A92488 !$#authors Blackburn, M.N.; Smith, R.L.; Carson, J.; Sibley, C.C. !$#journal J. Biol. Chem. (1984) 259:939-941 !$#title The heparin-binding site of antithrombin III. Identification !1of a critical tryptophan in the amino acid sequence. !$#cross-references MUID:84111578; PMID:6693405 !$#contents annotation; heparin-binding site GENETICS !$#gene GDB:AT3 !'##cross-references GDB:119024; OMIM:107300 !$#map_position 1q23-1q25.1 !$#introns 14/2; 136/3; 208/3; 254/3; 385/1; 406/3 FUNCTION !$#description in blood plasma inhibits thrombin and activated coagulation !1factor X, either weakly alone or strongly in the presence of !1heparin CLASSIFICATION #superfamily antithrombin III KEYWORDS acute phase; glycoprotein; heparin binding; plasma; serine !1proteinase inhibitor FEATURE !$1-32 #domain signal sequence #status predicted #label SIG\ !$33-464 #product antithrombin III #status experimental #label !8MAT\ !$40-160,53-127, !$279-462 #disulfide_bonds #status experimental\ !$81 #binding_site heparin (Trp) #status experimental\ !$128,167,187,224 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$425-426 #cleavage_site Arg-Ser (thrombin) #status !8experimental\ !$425 #inhibitory_site Arg (thrombin, coagulation factor !8Xa) #status experimental SUMMARY #length 464 #molecular-weight 52602 #checksum 9504 SEQUENCE /// ENTRY S28219 #type complete TITLE antithrombin III precursor - sheep ORGANISM #formal_name Ovis orientalis aries, Ovis ammon aries #common_name domestic sheep DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S28219 REFERENCE S28219 !$#authors Niessen, R.W.L.M.; Sturk, A.; Hordijk, P.L.; Michiels, F.; !1Peters, M. !$#journal Biochim. Biophys. Acta (1992) 1171:207-210 !$#title Sequence characterization of a sheep cDNA for antithrombin !1III. !$#cross-references MUID:93129622; PMID:1482684 !$#accession S28219 !'##molecule_type mRNA !'##residues 1-465 ##label NIE !'##cross-references EMBL:X68287; NID:g1194; PIDN:CAA48347.1; PID:g1195 FUNCTION !$#description inhibits in blood plasma thrombin and activated coagulation !1factor X, either weakly alone or strongly in the presence of !1heparin CLASSIFICATION #superfamily antithrombin III KEYWORDS glycoprotein; plasma; serine proteinase inhibitor FEATURE !$1-32 #domain signal sequence #status predicted #label SIG\ !$33-465 #product antithrombin III #status predicted #label !8MAT\ !$129,168,188,225 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 465 #molecular-weight 52499 #checksum 1761 SEQUENCE /// ENTRY A61435 #type complete TITLE antithrombin III - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A61435 REFERENCE A61435 !$#authors Mejdoub, H.; Le Ret, M.; Boulanger, Y.; Maman, M.; Choay, !1J.; Reinbolt, J. !$#journal J. Protein Chem. (1991) 10:205-212 !$#title The complete amino acid sequence of bovine antithrombin !1(ATIII). !$#cross-references MUID:92029517; PMID:1930634 !$#accession A61435 !'##molecule_type protein !'##residues 1-433 ##label MEJ COMMENT This serpin inhibits thrombin and other clotting factors in !1the presence of heparin and is the principal inhibitor of !1the coagulation cascade. FUNCTION !$#description inhibits in blood plasma thrombin and activated coagulation !1factor X, either weakly alone or strongly in the presence of !1heparin CLASSIFICATION #superfamily antithrombin III KEYWORDS anticoagulant; glycoprotein; heparin binding; plasma; serine !1proteinase inhibitor FEATURE !$9-129,22-96,248-431 #disulfide_bonds #status predicted\ !$97,136,156,193 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$394 #inhibitory_site Arg (thrombin) #status experimental SUMMARY #length 433 #molecular-weight 49126 #checksum 9589 SEQUENCE /// ENTRY JX0364 #type complete TITLE antithrombin III - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JX0364 REFERENCE JX0364 !$#authors Tokunaga, F.; Goto, T.; Wakabayashi, S.; Koide, T. !$#journal J. Biochem. (1994) 116:1164-1170 !$#title Amino acid sequence of porcine antithrombin III. !$#cross-references MUID:95204393; PMID:7896748 !$#accession JX0364 !'##molecule_type protein !'##residues 1-431 ##label TOK FUNCTION !$#description inhibits in blood plasma thrombin and activated coagulation !1factor X, either weakly alone or strongly in the presence of !1heparin CLASSIFICATION #superfamily antithrombin III KEYWORDS glycoprotein; heparin binding FEATURE !$378-382 #region hinge #status predicted\ !$9-129,22-96,248-431 #disulfide_bonds #status predicted\ !$136,156,193 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$394 #inhibitory_site Arg (thrombin) #status predicted SUMMARY #length 431 #molecular-weight 48936 #checksum 362 SEQUENCE /// ENTRY ITHUP1 #type complete TITLE plasminogen activator inhibitor 1 precursor [validated] - human ALTERNATE_NAMES plasminogen activator inhibitor, endothelial ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 08-Dec-2000 ACCESSIONS A28107; S02551; A26996; I59126; JS0397; A25693; A26146; !1A29100; A25895; A25651; B25651; A60436; S74133; S70346 REFERENCE A28107 !$#authors Bosma, P.J.; van den Berg, E.A.; Kooistra, T.; Siemieniak, !1D.R.; Slightom, J.L. !$#journal J. Biol. Chem. (1988) 263:9129-9141 !$#title Human plasminogen activator inhibitor-1 gene. Promoter and !1structural gene nucleotide sequences. !$#cross-references MUID:88243790; PMID:3132455 !$#accession A28107 !'##molecule_type DNA !'##residues 1-402 ##label BOS !'##cross-references GB:J03764; NID:g189564; PIDN:AAA60007.1; !1PID:g386996 REFERENCE S02551 !$#authors Strandberg, L.; Lawrence, D.; Ny, T. !$#journal Eur. J. Biochem. (1988) 176:609-616 !$#title The organization of the !1human-plasminogen-activator-inhibitor-1 gene. Implications !1on the evolution of the serine-protease inhibitor family. !$#cross-references MUID:89005111; PMID:3262512 !$#accession S02551 !'##molecule_type DNA !'##residues 1-14,'T',16-402 ##label STR !'##cross-references EMBL:X13338; NID:g35244; PIDN:CAA31722.1; !1PID:g35245 !'##note the complete translation is not annotated in GenBank entries !1HSPAI11, HSPAI12, HSPAI13, HSPAI14, HSPAI15, HSPAI16, !1HSPAI17, HSPAI18, and HSPAI19, release 109.0 REFERENCE A26996 !$#authors Loskutoff, D.J.; Linders, M.; Keijer, J.; Veerman, H.; van !1Heerikhuizen, H.; Pannekoek, H. !$#journal Biochemistry (1987) 26:3763-3768 !$#title Structure of the human plasminogen activator inhibitor 1 !1gene: nonrandom distribution of introns. !$#cross-references MUID:88000586; PMID:2820474 !$#accession A26996 !'##molecule_type DNA !'##residues 1-402 ##label LOS !'##cross-references GB:M22321; GB:M17121; NID:g189576; PIDN:AAA60009.1; !1PID:g189578 !'##note the sequence in GenBank entry HUMPAIB2, release 109.0, !1(PID:g189578) has the codon CTG for 55-Val rather than the !1published GTG REFERENCE I59126 !$#authors van Zonneveld, A.J.; Curriden, S.A.; Loskutoff, D.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:5525-5529 !$#title Type 1 plasminogen activator inhibitor gene: functional !1analysis and glucocorticoid regulation of its promoter. !$#cross-references MUID:88289754; PMID:2840665 !$#accession I59126 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-9 ##label ZON !'##cross-references GB:J03836; NID:g189579; PIDN:AAA60010.1; !1PID:g189580 REFERENCE JS0397 !$#authors Follo, M.; Ginsburg, D. !$#journal Gene (1989) 84:447-453 !$#title Structure and expression of the human gene encoding !1plasminogen activator inhibitor, PAI-1. !$#cross-references MUID:90128289; PMID:2612914 !$#accession JS0397 !'##molecule_type DNA !'##residues 85-86;88-93;166-171;231-236;298-302;331-336;360-365;388-393 !1##label FOL !'##cross-references GB:M33136; NID:g189543 !'##note sequences of the intron/exon boundaries are shown REFERENCE A91052 !$#authors Pannekoek, H.; Veerman, H.; Lambers, H.; Diergaarde, P.; !1Verweij, C.L.; van Zonneveld, A.J.; van Mourik, J.A. !$#journal EMBO J. (1986) 5:2539-2544 !$#title Endothelial plasminogen activator inhibitor (PAI): a new !1member of the serpin gene family. !$#cross-references MUID:87053819; PMID:2430793 !$#accession A25693 !'##molecule_type mRNA !'##residues 1-402 ##label PAN !'##cross-references GB:X04429; NID:g35271; PIDN:CAA28025.1; PID:g35272 REFERENCE A92766 !$#authors Ginsburg, D.; Zeheb, R.; Yang, A.Y.; Rafferty, U.M.; !1Andreasen, P.A.; Nielsen, L.; Dano, K.; Lebo, R.V.; !1Gelehrter, T.D. !$#journal J. Clin. Invest. (1986) 78:1673-1680 !$#title cDNA cloning of human plasminogen activator-inhibitor from !1endothelial cells. !$#cross-references MUID:87058123; PMID:3097076 !$#accession A26146 !'##molecule_type mRNA !'##residues 1-402 ##label GIN !'##cross-references GB:M16006; NID:g189541; PIDN:AAA60003.1; !1PID:g189542 REFERENCE A29100 !$#authors Wun, T.C.; Kretzmer, K.K. !$#journal FEBS Lett. (1987) 210:11-16 !$#title cDNA cloning and expression in E. coli of a plasminogen !1activator inhibitor (PAI) related to a PAI produced by Hep !1G2 hepatoma cell. !$#cross-references MUID:87105925; PMID:3026837 !$#accession A29100 !'##molecule_type mRNA !'##residues 17-402 ##label WUN !'##cross-references GB:X04744; NID:g35275; PIDN:CAA28444.1; PID:g755747 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE A25895 !$#authors Ny, T.; Sawdey, M.; Lawrence, D.; Millan, J.L.; Loskutoff, !1D.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:6776-6780 !$#title Cloning and sequence of a cDNA coding for the human !1beta-migrating endothelial-cell-type plasminogen activator !1inhibitor. !$#cross-references MUID:86313660; PMID:3092219 !$#accession A25895 !'##molecule_type mRNA !'##residues 20-402 ##label NYT !'##cross-references GB:M14083; NID:g189566; PIDN:AAA60008.1; !1PID:g386997 REFERENCE A91371 !$#authors Andreasen, P.A.; Riccio, A.; Welinder, K.G.; Douglas, R.; !1Sartorio, R.; Nielsen, L.S.; Oppenheimer, C.; Blasi, F.; !1Dano, K. !$#journal FEBS Lett. (1986) 209:213-218 !$#title Plasminogen activator inhibitor type-1: reactive center and !1amino-terminal heterogeneity determined by protein and cDNA !1sequencing. !$#cross-references MUID:87080762; PMID:3025016 !$#accession A25651 !'##molecule_type mRNA !'##residues 1-14,'T',16-47 ##label AND1 !'##cross-references GB:X04729; NID:g35263; PIDN:CAA28438.1; PID:g35264 !$#accession B25651 !'##molecule_type mRNA !'##residues 364-402 ##label AND2 !'##cross-references GB:X04731; NID:g35260; PIDN:CAA28442.1; PID:g35261 REFERENCE A60436 !$#authors Laug, W.E.; Aebersold, R.; Jong, A.; Rideout, W.; Bergman, !1B.L.; Baker, J. !$#journal Thromb. Haemost. (1989) 61:517-521 !$#title Isolation of multiple types of plasminogen activator !1inhibitors from vascular smooth muscle cells. !$#cross-references MUID:90020174; PMID:2799763 !$#accession A60436 !'##molecule_type protein !'##residues 225-235 ##label LAU REFERENCE S74133 !$#authors Kjoller, L.; Martensen, P.M.; Sottrup-Jensen, L.; Justesen, !1J.; Rodenburg, K.W.; Andreasen, P.A. !$#journal Eur. J. Biochem. (1996) 241:38-46 !$#title Conformational changes of the reactive-centre loop and !1beta-strand 5A accompany temperature-dependent !1inhibitor-substrate transition of plasminogen-activator !1inhibitor 1. !$#cross-references MUID:97054589; PMID:8898886 !$#accession S74133 !'##molecule_type protein !'##residues 22-30;370-376 ##label KJO REFERENCE S70346 !$#authors Stroemqvist, M.; Karlsson, K.E.; Bjoerquist, P.; Andersson, !1J.O.; Bystroem, M.; Hansson, L.; Johansson, T.; Deinum, J. !$#journal Biochim. Biophys. Acta (1996) 1295:103-109 !$#title Characterization of the complex of plasminogen activator !1inhibitor type 1 with tissue-type plasminogen activator by !1mass spectrometry and size-exclusion chromatography. !$#cross-references MUID:96283799; PMID:8679667 !$#accession S70346 !'##status preliminary !'##molecule_type protein !'##residues 370-375 ##label STO COMMENT This inhibitor acts as "bait" for tissue plasminogen !1activator (see PIR:UKHUT), urokinase (see PIR:UKHU), and !1protein C (see PIR:KXHU). Its rapid interaction with tPA may !1serve to regulate fibrinolysis. High concentrations of this !1protein have been associated with human thromboembolic !1disease. COMMENT Three types of PAI have been identified (see also PIR:A32853 !1and PIR:A39339). PAI-1 is an acid-stable glycoprotein found !1in plasma and platelets and in endothelial, hepatoma, and !1fibrosarcoma cells. Vascular endothelial cells may be the !1primary site of synthesis of plasma PAI. COMMENT Glycosylation is not required for inhibitory activity. GENETICS !$#gene GDB:PAI1; PLANH1 !'##cross-references GDB:120297; OMIM:173360 !$#map_position 7q21.3-7q22 !$#introns 91/1; 169/1; 234/1; 300/2; 334/1; 363/1; 391/1 CLASSIFICATION #superfamily antithrombin III KEYWORDS glycoprotein; serine proteinase inhibitor FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-402 #product plasminogen activator inhibitor-1 #status !8experimental #label MAT\ !$232,288,352 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$369 #inhibitory_site Arg (plasminogen activator) #status !8predicted SUMMARY #length 402 #molecular-weight 45060 #checksum 7132 SEQUENCE /// ENTRY A35032 #type complete TITLE plasminogen activator inhibitor 1 precursor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A35032; JT0490; A60581; A39120 REFERENCE A35032 !$#authors Bruzdzinski, C.J.; Riordan-Johnson, M.; Nordby, E.C.; Suter, !1S.M.; Gelehrter, T.D. !$#journal J. Biol. Chem. (1990) 265:2078-2085 !$#title Isolation and characterization of the rat plasminogen !1activator inhibitor-1 gene. !$#cross-references MUID:90130456; PMID:2298740 !$#accession A35032 !'##molecule_type DNA !'##residues 1-402 ##label BRU !'##cross-references GB:J05206; NID:g205965; PIDN:AAA41796.1; !1PID:g205966 REFERENCE JT0490 !$#authors Zeheb, R.; Gelehrter, T.D. !$#journal Gene (1988) 73:459-468 !$#title Cloning and sequencing of cDNA for the rat plasminogen !1activator inhibitor-1. !$#cross-references MUID:89211983; PMID:3149611 !$#accession JT0490 !'##molecule_type mRNA !'##residues 1-402 ##label ZEH !'##cross-references GB:M24067; NID:g577500; PIDN:AAA56856.1; !1PID:g577501 REFERENCE A60581 !$#authors Newman, M.J.; Lane, E.A.; Iannotti, A.M.; Nugent, M.A.; !1Pepinsky, R.B.; Keski-Oja, J. !$#journal Endocrinology (1990) 126:2936-2946 !$#title Characterization and purification of a secreted plasminogen !1activator inhibitor (PAI-1) induced by transforming growth !1factor-beta1 in normal rat kidney (NRK) cells: decreased !1PAI-1 expression in transformed NRK cells. !$#cross-references MUID:90276328; PMID:2190800 !$#accession A60581 !'##molecule_type protein !'##residues 24-48 ##label NEW REFERENCE A39120 !$#authors Olson Jr., J.A.; Shiverick, K.T.; Ogilvie, S.; Buhi, W.C.; !1Raizada, M.K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:1928-1932 !$#title Angiotensin II induces secretion of plasminogen activator !1inhibitor 1 and a tissue metalloprotease inhibitor-related !1protein from rat brain astrocytes. !$#cross-references MUID:91156719; PMID:2000398 !$#accession A39120 !'##status preliminary !'##molecule_type protein !'##residues 24-43,'G' ##label OLS GENETICS !$#introns 91/1; 169/1; 234/1; 300/2; 334/1; 363/1; 391/1 CLASSIFICATION #superfamily antithrombin III KEYWORDS glycoprotein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-402 #product plasminogen activator inhibitor-1 #status !8experimental #label MAT\ !$88,232,288,352 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$369 #inhibitory_site Arg (plasminogen activator) #status !8predicted SUMMARY #length 402 #molecular-weight 45009 #checksum 5583 SEQUENCE /// ENTRY S06745 #type complete TITLE plasminogen activator inhibitor-1 precursor - bovine ALTERNATE_NAMES endothelial-cell plasminogen activator inhibitor; PAI-1 ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 28-Feb-1990 #sequence_revision 22-Apr-1995 #text_change 18-Jun-1999 ACCESSIONS S06745; A35855; S01324; S10906 REFERENCE S06745 !$#authors Mimuro, J.; Sawdey, M.; Hattori, M.; Luskutoff, D.J. !$#journal Nucleic Acids Res. (1989) 17:8872 !$#title cDNA for bovine type 1 plasminogen activator inhibitor !1(PAI-1). !$#cross-references MUID:90067867; PMID:2587231 !$#accession S06745 !'##molecule_type mRNA !'##residues 1-402 ##label MIM !'##cross-references EMBL:X16383; NID:g600; PIDN:CAA34419.1; PID:g601 REFERENCE A35855 !$#authors Pepper, M.S.; Belin, D.; Montesano, R.; Orci, L.; Vassalli, !1J.D. !$#journal J. Cell Biol. (1990) 111:743-755 !$#title Transforming growth factor-beta 1 modulates basic fibroblast !1growth factor-induced proteolytic and angiogenic properties !1of endothelial cells in vitro. !$#cross-references MUID:90338128; PMID:1696269 !$#accession A35855 !'##molecule_type mRNA !'##residues 153-235 ##label PEP !'##cross-references EMBL:X52906; NID:g598; PIDN:CAA37094.1; PID:g930005 REFERENCE S01324 !$#authors Katagiri, K.; Okada, K.; Hattori, H.; Yano, M. !$#journal Eur. J. Biochem. (1988) 176:81-87 !$#title Bovine endothelial cell plasminogen activator inhibitor. !1Purification and heat activation. !$#cross-references MUID:88329072; PMID:3262060 !$#accession S01324 !'##molecule_type protein !'##residues 24-49,'L',51-63 ##label KAT COMMENT Three types of PAI have been identified. PAI-1 is an !1acid-stable glycoprotein found in plasma and platelets and !1in endothelial, hepatoma, and fibrosarcoma cells. Vascular !1endothelial cells may be the primary site of synthesis of !1plasma PAI. COMMENT This inhibitor acts as "bait" for tissue plasminogen !1activator, urokinase, and protein C. Its rapid interaction !1with tPA may function as a major control point in the !1regulation of fibrinolysis. COMMENT Glycosylation is not a prerequisite for inhibitory activity. CLASSIFICATION #superfamily antithrombin III KEYWORDS glycoprotein; serine proteinase inhibitor FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-402 #product plasminogen activator inhibitor 1 #status !8predicted #label MAT\ !$232,288,352 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$369 #inhibitory_site Arg (plasminogen activator) #status !8predicted SUMMARY #length 402 #molecular-weight 45371 #checksum 7559 SEQUENCE /// ENTRY A34761 #type complete TITLE plasminogen activator inhibitor 1 homolog mr1 - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A34761; S48208 REFERENCE A34761 !$#authors Prendergast, G.C.; Diamond, L.E.; Dahl, D.; Cole, M.D. !$#journal Mol. Cell. Biol. (1990) 10:1265-1269 !$#title The c-myc-regulated gene mr1 encodes plasminogen activator !1inhibitor 1. !$#cross-references MUID:90158593; PMID:2406566 !$#accession A34761 !'##molecule_type mRNA !'##residues 1-402 ##label PRE !'##cross-references GB:M33960; NID:g200219; PIDN:AAA39887.1; !1PID:g200220 REFERENCE S48202 !$#authors Lijnen, H.R.; van Hoef, B.; Beelen, V.; Collen, D. !$#journal Eur. J. Biochem. (1994) 224:863-871 !$#title Characterization of the murine plasma fibrinolytic system. !$#cross-references MUID:95010076; PMID:7523120 !$#accession S48208 !'##molecule_type protein !'##residues 'M',24-29 ##label LIJ CLASSIFICATION #superfamily antithrombin III SUMMARY #length 402 #molecular-weight 45170 #checksum 6242 SEQUENCE /// ENTRY ITHUC1 #type complete TITLE complement C1 inhibitor precursor [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 08-Dec-2000 ACCESSIONS S15386; S00403; A38781; B38781; A24161; A38782; S03370; !1A34847; S15084; A24258; S15529; A23936; A38783; S15085; !1S15086; A36053; A05286 REFERENCE S15386 !$#authors Carter, P.E.; Duponchel, C.; Tosi, M.; Fothergill, J.E. !$#journal Eur. J. Biochem. (1991) 197:301-308 !$#title Complete nucleotide sequence of the gene for human C1 !1inhibitor with an unusually high density of Alu elements. !$#cross-references MUID:91224119; PMID:2026152 !$#accession S15386 !'##molecule_type DNA !'##residues 1-500 ##label CA2 !'##cross-references EMBL:X54486; NID:g29534; PIDN:CAA38358.1; !1PID:g29535 REFERENCE S00403 !$#authors Carter, P.E.; Dunbar, B.; Fothergill, J.E. !$#journal Eur. J. Biochem. (1988) 173:163-169 !$#title Genomic and cDNA cloning of the human C1 inhibitor. !1Intron-exon junctions and comparison with other serpins. !$#cross-references MUID:88185313; PMID:3267220 !$#accession S00403 !'##molecule_type DNA !'##residues 1-500 ##label CAR !'##cross-references EMBL:X07427; NID:g29520; PIDN:CAA30314.1; !1PID:g1197499 !$#accession A38781 !'##molecule_type mRNA !'##residues 178-500 ##label CA3 !'##cross-references GB:X07577; NID:g29536; PIDN:CAA30469.1; !1PID:g1340170 !$#accession B38781 !'##molecule_type protein !'##residues 173-237,'X',239-252,'X',254,'X',256-264,'X', !1266-268;277-286;330-333;335-340;344-351,'X', !1353-364;367-380;'X',404-408;467-499 ##label CA4 REFERENCE A24161 !$#authors Bock, S.C.; Skriver, K.; Nielsen, E.; Thogersen, H.C.; !1Wiman, B.; Donaldson, V.H.; Eddy, R.L.; Marrinan, J.; !1Radziejewska, E.; Huber, R.; Shows, T.B.; Magnusson, S. !$#journal Biochemistry (1986) 25:4292-4301 !$#title Human C1 inhibitor: primary structure, cDNA cloning, and !1chromosomal localization. !$#cross-references MUID:87000544; PMID:3756141 !$#accession A24161 !'##molecule_type mRNA !'##residues 1-186,'Q',188-500 ##label BOC !'##cross-references EMBL:M13656; NID:g179620; PIDN:AAB59387.1; !1PID:g179621 !$#accession A38782 !'##molecule_type protein !'##residues 23-500 ##label BO2 !'##note 480-Met was also found REFERENCE S03370 !$#authors Rauth, G.; Schumacher, G.; Buckel, P.; Mueller-Esterl, W. !$#journal Protein Seq. Data Anal. (1988) 1:251-257 !$#title Molecular cloning of the cDNA coding for human C1(-) !1inhibitor. !$#cross-references MUID:88276848; PMID:3393514 !$#accession S03370 !'##molecule_type mRNA !'##residues 'PPVQ',6-479,'M',481-500 ##label RAU REFERENCE A34847 !$#authors Stoppa-Lyonnet, D.; Carter, P.E.; Meo, T.; Tosi, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:1551-1555 !$#title Clusters of intragenic Alu repeats predispose the human C1 !1inhibitor locus to deleterious rearrangements. !$#cross-references MUID:90160364; PMID:2154751 !$#accession A34847 !'##molecule_type DNA !'##residues 33-228 ##label STO !'##cross-references GB:M30688 REFERENCE S15084 !$#authors Que, B.G. !$#submission submitted to the EMBL Data Library, November 1986 !$#accession S15084 !'##molecule_type mRNA !'##residues 1-305,'R',307-500 ##label QUE !'##cross-references EMBL:M13690; NID:g179618; PIDN:AAA35613.1; !1PID:g179619 REFERENCE A24258 !$#authors Que, B.G.; Petra, P.H. !$#journal Biochem. Biophys. Res. Commun. (1986) 137:620-625 !$#title Isolation and analysis of a cDNA coding for human C1 !1inhibitor. !$#cross-references MUID:86268965; PMID:3488058 !$#accession A24258 !'##molecule_type mRNA !'##residues 187,'K',189-408,413-500 ##label QU2 !'##cross-references EMBL:M13690 REFERENCE S15529 !$#authors Tosi, M.; Duponchel, C.; Bourgarel, P.; Colomb, M.; Meo, T. !$#journal Gene (1986) 42:265-272 !$#title Molecular cloning of human C1 inhibitor: sequence homologies !1with alpha(1)-antitrypsin and other members of the serpins !1superfamily. !$#cross-references MUID:86276001; PMID:3089875 !$#accession S15529 !'##molecule_type mRNA !'##residues 213-500 ##label TOS !'##cross-references EMBL:M14036; NID:g179616; PIDN:AAA51848.1; !1PID:g179617 REFERENCE A23936 !$#authors Davis III, A.E.; Whitehead, A.S.; Harrison, R.A.; !1Dauphinais, A.; Bruns, G.A.P.; Cicardi, M.; Rosen, F.S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:3161-3165 !$#title Human inhibitor of the first component of complement, C1: !1characterization of cDNA clones and localization of the gene !1to chromosome 11. !$#cross-references MUID:86205856; PMID:3458172 !$#accession A23936 !'##molecule_type mRNA !'##residues 241-314,'QLQKLSY',321,'M',323-331,'L',333-369,'TGTGSQ', !1376-416,'V',418-438,'F',440-458 ##label DA1 !'##cross-references EMBL:M13203 !'##note the authors translated the codon CTG for residue 332 as Val !$#accession A38783 !'##molecule_type protein !'##residues 23-24,'X',26-33;54-62,'XL';168-178,'X',180-186,'NAEAX',192, !1'X',194;326-351,'X',353-363,'XXX',367-368;384-399,'X', !1401-408;442-456 ##label DAV REFERENCE A05286 !$#authors Harrison, R.A. !$#journal Biochemistry (1983) 22:5001-5007 !$#title Human C1 inhibitor: improved isolation and preliminary !1structural characterization. !$#cross-references MUID:84053355; PMID:6416294 !$#accession S15085 !'##molecule_type protein !'##residues 23-24,'X',26-47,'X',48-62 ##label HAR REFERENCE S15086 !$#authors Salvesen, G.S.; Catanese, J.J.; Kress, L.F.; Travis, J. !$#journal J. Biol. Chem. (1985) 260:2432-2436 !$#title Primary structure of the reactive site of human !1C1-inhibitor. !$#cross-references MUID:85130986; PMID:3919001 !$#accession S15086 !'##molecule_type protein !'##residues 'I',61-62,'XX',65-68;464-475 ##label SAL REFERENCE A36053 !$#authors Parad, R.B.; Kramer, J.; Strunk, R.C.; Rosen, F.S.; Davis !1III, A.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:6786-6790 !$#title Dysfunctional C1 inhibitor Ta: deletion of Lys-251 results !1in acquisition of an N-glycosylation site. !$#cross-references MUID:90370868; PMID:2118657 !$#accession A36053 !'##molecule_type protein !'##residues 266-282 ##label PAR !'##note Lys-251 was deleted in protein isolated from a patient with !1type II hereditary angioneurotic edema COMMENT This protein inhibits the serine proteinase activity in !1complement factors C1r and C1s. COMMENT Defects in this protein result in hereditary angioneurotic !1edema. In type I disease, the protein is not expressed. In !1type II disease, a nonfunctional protein is produced. GENETICS !$#gene GDB:C1NH !'##cross-references GDB:119041; OMIM:106100 !$#map_position 11q12.1-11q13.1 !$#introns 17/3; 184/1; 229/1; 297/1; 343/3; 417/1 CLASSIFICATION #superfamily antithrombin III KEYWORDS glycoprotein; serine proteinase inhibitor; tandem repeat FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-500 #product complement C1 inhibitor #status experimental !8#label MAT\ !$23-119 #domain glycosylated #status predicted #label GLC\ !$65-119 #region 4-residue repeats\ !$120-500 #domain inhibitory #status predicted #label INH\ !$25,69,81,238,253, !$352 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$48,71,83,88,92,96 #binding_site carbohydrate (Thr) (covalent) #status !8experimental\ !$64 #binding_site carbohydrate (Ser) (covalent) #status !8experimental\ !$72,99,106,107,111, !$115,118,119 #binding_site carbohydrate (Thr) (covalent) #status !8predicted\ !$123-428,130-205 #disulfide_bonds #status experimental\ !$466 #inhibitory_site Arg (complement C1) #status !8experimental SUMMARY #length 500 #molecular-weight 55154 #checksum 6068 SEQUENCE /// ENTRY ITHUA2 #type complete TITLE alpha-2-antiplasmin precursor [validated] - human ALTERNATE_NAMES alpha-2-PI; alpha-2-plasmin inhibitor precursor ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Jul-1989 #sequence_revision 12-Apr-1996 #text_change 08-Dec-2000 ACCESSIONS A31402; A32163; A41504; A26684; A24708; PC2129; S00068; !1S32524; S32529 REFERENCE A31402 !$#authors Hirosawa, S.; Nakamura, Y.; Miura, O.; Sumi, Y.; Aoki, N. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:6836-6840 !$#title Organization of the human alpha-2-plasmin inhibitor gene. !$#cross-references MUID:88320531; PMID:3166140 !$#accession A31402 !'##molecule_type DNA !'##residues 1-491 ##label HIR1 !'##cross-references GB:M20786; GB:J03830; NID:g177884; PIDN:AAA51554.1; !1PID:g177886 REFERENCE A32163 !$#authors Hirosawa, S.; Nakamura, Y.; Miura, O.; Sumi, Y.; Aoki, N. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:1612-1613 !$#accession A32163 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-491 ##label HIR2 REFERENCE A41504 !$#authors Tone, M.; Kikuno, R.; Kume-Iwaki, A.; Hashimoto-Gotoh, T. !$#journal J. Biochem. (1987) 102:1033-1041 !$#title Structure of human alpha-2-plasmin inhibitor deduced from !1the cDNA sequence. !$#cross-references MUID:88139254; PMID:2830248 !$#accession A41504 !'##molecule_type mRNA !'##residues 1-32,'W',34-491 ##label TON !'##cross-references GB:D00174; NID:g219409; PIDN:BAA00124.1; !1PID:g219410 REFERENCE A26684 !$#authors Holmes, W.E.; Nelles, L.; Lijnen, H.R.; Collen, D. !$#journal J. Biol. Chem. (1987) 262:1659-1664 !$#title Primary structure of human alpha-2-antiplasmin, a serine !1protease inhibitor (serpin). !$#cross-references MUID:87109313; PMID:2433286 !$#accession A26684 !'##molecule_type mRNA !'##residues 4-288,'D',290-491 ##label HOL !'##cross-references GB:J02654; NID:g178750; PIDN:AAA35543.1; !1PID:g178751 !'##note the authors translated the codon GAT for residue 289 as His REFERENCE A24708 !$#authors Sumi, Y.; Nakamura, Y.; Aoki, N.; Sakai, M.; Muramatsu, M. !$#journal J. Biochem. (1986) 100:1399-1402 !$#title Structure of the carboxyl-terminal half of human !1alpha-2-plasmin inhibitor deduced from that of cDNA. !$#cross-references MUID:87137400; PMID:3818581 !$#accession A24708 !'##molecule_type mRNA !'##residues 218-491 ##label SUM !'##cross-references DDBJ:D00116; NID:g219407; PIDN:BAA00070.1; !1PID:g219408 REFERENCE PC2129 !$#authors Koyama, T.; Koike, Y.; Toyota, S.; Miyagi, F.; Suzuki, N.; !1Aoki, N. !$#journal Biochem. Biophys. Res. Commun. (1994) 200:417-422 !$#title Different NH2-terminal form with 12 additional residues of !1alpha2-plasmin inhibitor from human plasma and culture media !1of Hep G2 cells. !$#cross-references MUID:94220119; PMID:8166714 !$#accession PC2129 !'##molecule_type protein !'##residues 28-53 ##label KOY !'##experimental_source Hep G2 cells cultured in serum-free medium !'##note in the presence of serum, this material loses the first twelve !1residues and becomes more reactive to fibrin cross-linking REFERENCE S00068 !$#authors Lijnen, H.R.; Holmes, W.E.; Van Hoef, B.; Wiman, B.; !1Rodriguez, H.; Collen, D. !$#journal Eur. J. Biochem. (1987) 166:565-574 !$#title Amino-acid sequence of human alpha-2-antiplasmin. !$#cross-references MUID:87275946; PMID:2440681 !$#accession S00068 !'##molecule_type protein !'##residues 40-48,'G',50-104,'D',106-114,'X',116-327,'X',329-340, !1'XXXX',345-407,'G',409-415,'XX',418-454,'N',456-491 ##label !1LIJ !'##note 49-Gly and 408-Gly may represent heterogeneity; 2 disulfide !1bonds were determined; glycosylation sites were determined REFERENCE S32524 !$#authors Bangert, K.; Johnsen, A.H.; Christensen, U.; Thorsen, S. !$#journal Biochem. J. (1993) 291:623-625 !$#title Different N-terminal forms of alpha(2)-plasmin inhibitor in !1human plasma. !$#cross-references MUID:93249387; PMID:8484741 !$#accession S32524 !'##molecule_type protein !'##residues 28-58 ##label BAN REFERENCE S32529 !$#authors Enghild, J.J.; Valnickova, Z.; Thogersen, I.B.; Pizzo, S.V.; !1Salvesen, G. !$#journal Biochem. J. (1993) 291:933-938 !$#title An examination of the inhibitory mechanism of serpins by !1analysing the interaction of trypsin and chymotrypsin with !1alpha(2)-antiplasmin. !$#cross-references MUID:93256910; PMID:7683878 !$#accession S32529 !'##molecule_type protein !'##residues 28-43;64-69;405-409 ##label ENG !'##note determination of cleavage and inhibitory sites REFERENCE A57869 !$#authors Sumi, Y.; Ichikawa, Y.; Nakamura, Y.; Miura, O.; Aoki, N. !$#journal J. Biochem. (1989) 106:703-707 !$#title Expression and characterization of Pro alpha-2-plasmin !1inhibitor. !$#cross-references MUID:90110073; PMID:2606916 !$#contents annotation; role of propeptide REFERENCE A92565 !$#authors Kimura, S.; Aoki, N. !$#journal J. Biol. Chem. (1986) 261:15591-15595 !$#title Cross-linking site in fibrinogen for alpha-2-plasmin !1inhibitor. !$#cross-references MUID:87057190; PMID:2877981 !$#contents annotation; cross-linking site for fibrin COMMENT After synthesis in the liver, 30-50% of alpha-2-antiplasmin !1circulates in plasma with the propeptide uncleaved. The !1presence of the propeptide does not prevent plasmin !1inhibition, but does inhibit activated coagulation factor !1XIII from forming an isopeptide cross-link with fibrin. GENETICS !$#gene GDB:PLI !'##cross-references GDB:120301; OMIM:262850 !$#map_position 17pter-17p12 !$#introns 21/3; 34/3; 55/3; 123/1; 171/1; 239/1; 286/3; 355/1 FUNCTION !$#description moderates fibrinolysis by inhibiting plasmin CLASSIFICATION #superfamily antithrombin III KEYWORDS extracellular protein; fibrinolysis; glycoprotein; plasma; !1serine proteinase inhibitor FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-39 #domain propeptide #status experimental #label PRO\ !$40-491 #product alpha-2-antiplasmin #status experimental !8#label MAT\ !$454-465 #domain amphipathic helix #status predicted #label !8APH\ !$465-467 #region cell attachment (R-G-D) motif\ !$39-40 #cleavage_site Pro-Asn (unidentified plasma !8proteinase) #status experimental\ !$41 #cross-link isopeptide (Gln) (interchain to Lys-322 !8of fibrin alpha chain) #status experimental\ !$70-152,103-143 #disulfide_bonds #status experimental\ !$126,295,309,316 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$401-402 #cleavage_site Met-Ser (chymotrypsin) (partial) !8#status experimental\ !$403-404 #cleavage_site Arg-Met (plasmin, trypsin) #status !8experimental\ !$403 #inhibitory_site Arg (plasmin) #status predicted\ !$404-405 #cleavage_site Met-Ser (chymotrypsin) (partial) !8#status experimental\ !$404 #inhibitory_site Met (chymotrypsin) #status !8predicted\ !$437 #binding_site carbohydrate (Asn) (covalent) #status !8absent SUMMARY #length 491 #molecular-weight 54565 #checksum 2648 SEQUENCE /// ENTRY DXCH #type fragment TITLE ovalbumin-related X protein - chicken (fragment) ORGANISM #formal_name Gallus gallus #common_name chicken DATE 31-Dec-1980 #sequence_revision 31-Dec-1980 #text_change 18-Jun-1999 ACCESSIONS A01243 REFERENCE A01243 !$#authors Heilig, R.; Perrin, F.; Gannon, F.; Mandel, J.L.; Chambon, !1P. !$#journal Cell (1980) 20:625-637 !$#title The ovalbumin gene family: structure of the X gene and !1evolution of duplicated split genes. !$#cross-references MUID:81022623; PMID:7418002 !$#contents exons 6, 7, and 8 !$#accession A01243 !'##molecule_type DNA !'##residues 1-232 ##label HEI !'##cross-references GB:J00920; NID:g212895; PIDN:AAA68881.1; !1PID:g212897 CLASSIFICATION #superfamily antithrombin III KEYWORDS glycoprotein; phosphoprotein; serine proteinase inhibitor FEATURE !$137 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$189 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 232 #checksum 4831 SEQUENCE /// ENTRY DYCH #type complete TITLE ovalbumin-related Y protein - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 18-Jun-1999 ACCESSIONS A01244 REFERENCE A01244 !$#authors Heilig, R.; Muraskowsky, R.; Kloepfer, C.; Mandel, J.L. !$#journal Nucleic Acids Res. (1982) 10:4363-4382 !$#title The ovalbumin gene family: complete sequence and structure !1of the Y gene. !$#cross-references MUID:83014329; PMID:7122240 !$#accession A01244 !'##molecule_type DNA !'##residues 1-388 ##label HEI !'##cross-references GB:J00922; GB:V00439; NID:g212899; PIDN:AAA68882.1; !1PID:g212900 GENETICS !$#introns 56/3; 73/3; 116/3; 156/1; 203/3; 255/3 CLASSIFICATION #superfamily antithrombin III KEYWORDS glycoprotein; phosphoprotein; serine proteinase inhibitor FEATURE !$74-121 #disulfide_bonds #status predicted\ !$293 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$345 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 388 #molecular-weight 43772 #checksum 1055 SEQUENCE /// ENTRY OACH #type complete TITLE ovalbumin [validated] - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 31-Dec-1979 #sequence_revision 30-Jun-1993 #text_change 15-Sep-2000 ACCESSIONS A90455; I50402; I50605; A93197; A93827; A90093; A90092; !1A61297; A42793; A01245 REFERENCE A90455 !$#authors Woo, S.L.C.; Beattie, W.G.; Catterall, J.F.; Dugaiczyk, A.; !1Staden, R.; Brownlee, G.G.; O'Malley, B.W. !$#journal Biochemistry (1981) 20:6437-6446 !$#title Complete nucleotide sequence of the chicken chromosomal !1ovalbumin gene and its biological significance. !$#cross-references MUID:82069038; PMID:6272839 !$#accession A90455 !'##molecule_type DNA !'##residues 1-386 ##label WOO !'##cross-references EMBL:V00438; NID:g63719; PIDN:CAA23716.1; !1PID:g808974 !'##note a number of silent polymorphic sites are identified and !1discussed !'##note Thr-188 is also predicted REFERENCE I50402 !$#authors Catterall, J.F.; O'Malley, B.W.; Robertson, M.A.; Staden, !1R.; Tanaka, Y.; Brownlee, G.G. !$#journal Nature (1978) 275:510-513 !$#title Nucleotide sequence homology at 12 intron-exon junctions in !1the chick ovalbumin gene. !$#cross-references MUID:79010682; PMID:692731 !$#accession I50402 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-386 ##label CAT !'##cross-references GB:M34352; NID:g212501; PIDN:AAA48998.1; !1PID:g212503 REFERENCE I50605 !$#authors Robertson, M.A.; Staden, R.; Tanaka, Y.; Catterall, J.F.; !1O'Malley, B.W.; Brownlee, G.G. !$#journal Nature (1979) 278:370-372 !$#title Sequence of three introns in the chick ovalbumin gene. !$#cross-references MUID:79135070; PMID:423993 !$#accession I50605 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-4,'A',6-118,'F',120-155 ##label ROB !'##cross-references EMBL:V00382; NID:g63051; PIDN:CAA23681.1; !1PID:g63052 REFERENCE A93197 !$#authors McReynolds, L.; O'Malley, B.W.; Nisbet, A.D.; Fothergill, !1J.E.; Givol, D.; Fields, S.; Robertson, M.; Brownlee, G.G. !$#journal Nature (1978) 273:723-728 !$#title Sequence of chicken ovalbumin mRNA. !$#cross-references MUID:78199842; PMID:661981 !$#accession A93197 !'##molecule_type mRNA !'##residues 1-386 ##label MCR !'##cross-references EMBL:V00383; NID:g63053 !'##note a minor component has Asp-312 REFERENCE A93827 !$#authors Palmiter, R.D.; Gagnon, J.; Walsh, K.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1978) 75:94-98 !$#title Ovalbumin: a secreted protein without a transient !1hydrophobic leader sequence. !$#cross-references MUID:78116057; PMID:272676 !$#accession A93827 !'##molecule_type protein !'##residues 2-33,'X',35-36 ##label PAL REFERENCE A90093 !$#authors Thompson, E.O.P.; Fisher, W.K. !$#journal Aust. J. Biol. Sci. (1978) 31:443-446 !$#title A correction and extension of the acetylated amino terminal !1sequence of ovalbumin. !$#cross-references MUID:79186958; PMID:751625 !$#accession A90093 !'##molecule_type protein !'##residues 2-17 ##label TH1 REFERENCE A90092 !$#authors Thompson, E.O.P.; Fisher, W.K. !$#journal Aust. J. Biol. Sci. (1978) 31:433-442 !$#title Amino acid sequences containing half-cystine residues in !1ovalbumin. !$#cross-references MUID:79186957; PMID:751624 !$#accession A90092 !'##molecule_type protein !'##residues 6-17;30-36;61-79;116-124;367-374;380-386 ##label TH2 REFERENCE A61297 !$#authors Tsunasawa, S.; Narita, K. !$#journal J. Biochem. (1982) 92:607-613 !$#title Micro-identification of amino-terminal acetylamino acids in !1proteins. !$#cross-references MUID:83056735; PMID:6754709 !$#accession A61297 !'##molecule_type protein !'##residues 2-6 ##label TSU REFERENCE A42793 !$#authors Takahashi, N.; Hirose, M. !$#journal J. Biol. Chem. (1992) 267:11565-11572 !$#title Reversible denaturation of disulfide-reduced ovalbumin and !1its reoxidation generating the native cystine cross-link. !$#cross-references MUID:92283876; PMID:1597484 !$#accession A42793 !'##molecule_type protein !'##residues 60-73,'X',75-85;112-119,'EX',122-123 ##label TAK REFERENCE A50294 !$#authors Stein, P.E.; Leslie, A.G.W. !$#submission submitted to the Brookhaven Protein Data Bank, November 1990 !$#cross-references PDB:1OVA !$#contents annotation; X-ray crystallography, 1.95 angstroms, residues !12-386 REFERENCE A58761 !$#authors Stein, P.E.; Leslie, A.G.W.; Finch, J.T.; Carrell, R.W. !$#journal J. Mol. Biol. (1991) 221:941-959 !$#title Crystal structure of uncleaved ovalbumin at 1.95 Angstroms !1resolution. !$#cross-references MUID:92046044; PMID:1942038 !$#contents annotation; X-ray crystallography, 1.95 angstroms GENETICS !$#introns 56/3; 73/3; 116/3; 156/1; 203/3; 255/3 CLASSIFICATION #superfamily antithrombin III KEYWORDS acetylated amino end; glycoprotein; phosphoprotein FEATURE !$2-384 #product ovalbumin #status experimental #label MAT\ !$2 #modified_site acetylated amino end (Gly) (in mature !8form) #status experimental\ !$69,345 #binding_site phosphate (Ser) (covalent) #status !8experimental\ !$74-121 #disulfide_bonds #status experimental\ !$293 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 386 #molecular-weight 42881 #checksum 4753 SEQUENCE /// ENTRY A37924 #type complete TITLE heparin cofactor II precursor [validated] - human ALTERNATE_NAMES antithrombin; heparin cofactor A; leuserpin 2 ORGANISM #formal_name Homo sapiens #common_name man DATE 12-Jul-1991 #sequence_revision 07-Jul-1995 #text_change 08-Dec-2000 ACCESSIONS A37924; A28704; A26320; A23527; A31077; A39077; A25177; !1A24438 REFERENCE A37924 !$#authors Herzog, R.; Lutz, S.; Blin, N.; Marasa, J.C.; Blinder, M.A.; !1Tollefsen, D.M. !$#journal Biochemistry (1991) 30:1350-1357 !$#title Complete nucleotide sequence of the gene for human heparin !1cofactor II and mapping to chromosomal band 22q11. !$#cross-references MUID:91120782; PMID:1671335 !$#accession A37924 !'##molecule_type DNA !'##residues 1-499 ##label HER !'##cross-references GB:M58600; GB:J05309; NID:g183907; PIDN:AAA52641.1; !1PID:g183908 REFERENCE A28704 !$#authors Blinder, M.A.; Marasa, J.C.; Reynolds, C.H.; Deaven, L.L.; !1Tollefsen, D.M. !$#journal Biochemistry (1988) 27:752-759 !$#title Heparin cofactor II: cDNA sequence, chromosome localization, !1restriction fragment length polymorphism, and expression in !1Escherichia coli. !$#cross-references MUID:88163663; PMID:2894851 !$#accession A28704 !'##molecule_type mRNA !'##residues 1-236,'R',238-499 ##label BLI !'##cross-references GB:M12849; GB:M19241; NID:g183909; PIDN:AAA52642.1; !1PID:g183910 REFERENCE A26320 !$#authors Inhorn, R.C.; Tollefsen, D.M. !$#journal Biochem. Biophys. Res. Commun. (1986) 137:431-436 !$#title Isolation and characterization of a partial cDNA clone for !1heparin cofactor II. !$#cross-references MUID:86242236; PMID:3755044 !$#accession A26320 !'##molecule_type mRNA !'##residues 333-499 ##label INH !'##cross-references GB:M12849 !'##experimental_source fetal liver !'##note the authors translated the codon CAA for residue 430 as Asn and !1ACC for residue 465 as Ile REFERENCE A23527 !$#authors Ragg, H. !$#journal Nucleic Acids Res. (1986) 14:1073-1088 !$#title A new member of the plasma protease inhibitor gene family. !$#cross-references MUID:86120356; PMID:3003690 !$#accession A23527 !'##molecule_type mRNA !'##residues 20-499 ##label RAG !'##cross-references GB:X03498; NID:g32314; PIDN:CAA27218.1; !1PID:g1335104 REFERENCE A31077 !$#authors Ragg, H.; Preibisch, G. !$#journal J. Biol. Chem. (1988) 263:12129-12134 !$#title Structure and expression of the gene coding for the human !1serpin hLS2. !$#cross-references MUID:88298901; PMID:2841345 !$#accession A31077 !'##molecule_type DNA !'##residues 1-119;294-299;386-391;434-439 ##label RA2 !'##cross-references GB:J03921 REFERENCE A39077 !$#authors Church, F.C.; Pratt, C.W.; Hoffman, M. !$#journal J. Biol. Chem. (1991) 266:704-709 !$#title Leukocyte chemoattractant peptides from the serpin heparin !1cofactor II. !$#cross-references MUID:91093260; PMID:1985958 !$#accession A39077 !'##molecule_type protein !'##residues 58-65 ##label CHU !'##note proteolytic fragment 58-65, generated in vitro by neutrophil !1elastase digestion, and a synthetic peptide corresponding to !1residues 68-79 are potent chemotactic peptides for !1leukocytes REFERENCE A25177 !$#authors Church, F.C.; Noyes, C.M.; Griffith, M.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:6431-6434 !$#cross-references MUID:86016716; PMID:3863104 !$#accession A25177 !'##molecule_type protein !'##residues 463-482,'P',484-485,'TII',489-498,'Q' ##label CH2 REFERENCE A24438 !$#authors Griffith, M.J.; Noyes, C.M.; Tyndall, J.A.; Church, F.C. !$#journal Biochemistry (1985) 24:6777-6782 !$#cross-references MUID:86077723; PMID:3907702 !$#accession A24438 !'##molecule_type protein !'##residues 20-48,50-52;464-482,'P',484-485,'T',487-498,'Q' ##label GRI GENETICS !$#gene GDB:HCF2 !'##cross-references GDB:120038; OMIM:142360 !$#map_position 22q11.2-22q11.2 !$#introns 297/1; 388/2; 436/3 CLASSIFICATION #superfamily antithrombin III KEYWORDS anticoagulant; glycoprotein; plasma; serine proteinase !1inhibitor; sulfoprotein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-499 #product heparin cofactor II #status experimental !8#label MAT\ !$68-79 #region chemotactic\ !$182-214 #region heparin binding #status predicted\ !$49,188,387 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$79,92 #binding_site sulfate (Tyr) (covalent) #status !8predicted\ !$463 #inhibitory_site Leu (thrombin, chymotrypsin) #status !8predicted SUMMARY #length 499 #molecular-weight 57070 #checksum 1090 SEQUENCE /// ENTRY S41066 #type complete TITLE heparin cofactor II precursor - rat ALTERNATE_NAMES antithrombin; heparin cofactor A; leuserpin 2 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 13-Jan-1995 #sequence_revision 13-Jan-1995 #text_change 18-Jun-1999 ACCESSIONS S41066; S39205; S39204 REFERENCE S41066 !$#authors Westrup, D.; Ragg, H. !$#journal Biochim. Biophys. Acta (1994) 1217:93-96 !$#title Secondary thrombin-binding site, glycosaminoglycan binding !1domain and reactive center region of leuserpin-2 are !1strongly conserved in mammalian species. !$#cross-references MUID:94114579; PMID:8286422 !$#accession S41066 !'##status preliminary !'##molecule_type mRNA !'##residues 1-479 ##label WES1 !'##cross-references EMBL:X74549; NID:g433612; PIDN:CAA52643.1; !1PID:g433613 !'##note submitted to the EMBL Data Library, August 1993 !$#accession S39205 !'##status preliminary !'##molecule_type mRNA !'##residues 1-479 ##label WES2 !'##cross-references EMBL:X74550; NID:g433614; PIDN:CAA52644.1; !1PID:g433615 CLASSIFICATION #superfamily antithrombin III KEYWORDS anticoagulant; glycoprotein; plasma; serine proteinase !1inhibitor; sulfoprotein FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-479 #product heparin cofactor II #status predicted #label !8MAT\ !$50-61 #region chemotactic\ !$162-194 #region heparin binding #status predicted\ !$31,168,367,403 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$61,74 #binding_site sulfate (Tyr) (covalent) #status !8predicted\ !$443 #inhibitory_site Leu (thrombin, chymotrypsin) #status !8predicted SUMMARY #length 479 #molecular-weight 54551 #checksum 8502 SEQUENCE /// ENTRY A48681 #type complete TITLE placental thrombin inhibitor - human ALTERNATE_NAMES cytoplasmic antiproteinase; intracellular serine proteinase inhibitor, 38K ORGANISM #formal_name Homo sapiens #common_name man DATE 07-Apr-1994 #sequence_revision 07-Jul-1995 #text_change 18-Jun-1999 ACCESSIONS A48681; A54352; A46672; B46672; C46672; S35750 REFERENCE A48681 !$#authors Coughlin, P.; Sun, J.; Cerruti, L.; Salem, H.H.; Bird, P. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:9417-9421 !$#title Cloning and molecular characterization of a human !1intracellular serine proteinase inhibitor. !$#cross-references MUID:94022386; PMID:8415716 !$#accession A48681 !'##molecule_type mRNA !'##residues 1-376 ##label COU !'##cross-references GB:Z22658; NID:g297411; PIDN:CAA80373.1; !1PID:g297412 !'##experimental_source placenta !'##note authors translated the codon CAA for residue 198 as Gly REFERENCE A54352 !$#authors Morgenstern, K.A.; Sprecher, C.; Holth, L.; Foster, D.; !1Grant, F.J.; Ching, A.; Kisiel, W. !$#journal Biochemistry (1994) 33:3432-3441 !$#title Complementary DNA cloning and kinetic characterization of a !1novel intracellular serine proteinase inhibitor: mechanism !1of action with trypsin and factor Xa as model proteinases. !$#cross-references MUID:94183847; PMID:8136380 !$#accession A54352 !'##molecule_type mRNA !'##residues 1-174,'E',176-361,'S',363-376 ##label MOR !'##cross-references GB:S69272; NID:g546087; PIDN:AAB30320.1; !1PID:g546088 !'##experimental_source placenta !'##note sequence extracted from NCBI backbone (NCBIN:145231, !1NCBIP:145232) REFERENCE A46672 !$#authors Coughlin, P.B.; Tetaz, T.; Salem, H.H. !$#journal J. Biol. Chem. (1993) 268:9541-9547 !$#title Identification and purification of a novel serine proteinase !1inhibitor. !$#cross-references MUID:93252826; PMID:8486644 !$#accession A46672 !'##molecule_type protein !'##residues 47-60;63-81;91-98 ##label CO2 !'##experimental_source placenta, leukemic cell line K562 !'##note sequence modified after extraction from NCBI backbone GENETICS !$#gene GDB:PI6 !'##cross-references GDB:252025; OMIM:173321 !$#map_position 6p25-6p24.3 CLASSIFICATION #superfamily antithrombin III KEYWORDS blocked amino end; cytosol; serine proteinase inhibitor FEATURE !$341 #inhibitory_site Arg (thrombin) #status predicted SUMMARY #length 376 #molecular-weight 42587 #checksum 300 SEQUENCE /// ENTRY ITHUC #type complete TITLE alpha-1-antichymotrypsin precursor - human ORGANISM #formal_name Homo sapiens #common_name man DATE 19-Feb-1984 #sequence_revision 03-Oct-1995 #text_change 18-Jun-1999 ACCESSIONS A90475; A34934; I39380; B19893; A19893; S04975; S14806; !1S44458; A01246 REFERENCE A90475 !$#authors Chandra, T.; Stackhouse, R.; Kidd, V.J.; Robson, K.J.H.; !1Woo, S.L.C. !$#journal Biochemistry (1983) 22:5055-5061 !$#title Sequence homology between human alpha 1-antichymotrypsin, !1alpha 1-antitrypsin, and antithrombin III. !$#cross-references MUID:84080367; PMID:6606438 !$#accession A90475 !'##molecule_type mRNA !'##residues 1-101,'ASSSPHGDLLRQKFT',117-122,'RAPSIS',129-433 ##label !1CHA !'##cross-references GB:K01500; NID:g177808; PIDN:AAA51543.1; !1PID:g177809 !'##note it is uncertain whether Met-1 or Met-4 is the initiator !'##note the authors of reference A34934 propose a correction to this !1sequence REFERENCE A34934 !$#authors Rubin, H.; Wang, Z.; Nickbarg, E.B.; McLarney, S.; Naidoo, !1N.; Schoenberger, O.L.; Johnson, J.L.; Cooperman, B.S. !$#journal J. Biol. Chem. (1990) 265:1199-1207 !$#title Cloning, expression, purification, and biological activity !1of recombinant native and variant human !1alpha1-antichymotrypsins. !$#cross-references MUID:90110106; PMID:2404007 !$#accession A34934 !'##molecule_type mRNA !'##residues 87-129 ##label RUB !'##cross-references GB:J05176 REFERENCE I39380 !$#authors Abraham, C.R.; Selkoe, D.J.; Potter, H. !$#journal Cell (1988) 52:487-501 !$#title Immunochemical identification of the serine protease !1inhibitor alpha 1-antichymotrypsin in the brain amyloid !1deposits of Alzheimer's disease. !$#cross-references MUID:88135764; PMID:3257719 !$#accession I39380 !'##molecule_type mRNA !'##residues 1-46 ##label RES !'##cross-references GB:M18906; NID:g177928; PIDN:AAA51559.1; !1PID:g177931 REFERENCE A90110 !$#authors Morii, M.; Travis, J. !$#journal Biochem. Biophys. Res. Commun. (1983) 111:438-443 !$#title Structural alterations in alpha-1-antichymotrypsin from !1normal and acute phase human plasma. !$#cross-references MUID:83178256; PMID:6687683 !$#accession B19893 !'##molecule_type protein !'##residues 41-54,'S',56-60 ##label MOR !$#accession A19893 !'##molecule_type protein !'##residues 'DPN',29,'N',31,'DD',34-35,'EGDEN',41-45 ##label MO2 !'##note most of the discrepancies between this report and the canonical !1sequences are differences in amidation state REFERENCE S04975 !$#authors Lindmark, B.; Lilja, H.; Alm, R.; Eriksson, S. !$#journal Biochim. Biophys. Acta (1989) 997:90-95 !$#title The microheterogeneity of desialylated alpha !1(1)-antichymotrypsin: the occurrence of two amino-terminal !1isoforms, one lacking a His-Pro dipeptide. !$#cross-references MUID:89323223; PMID:2787670 !$#accession S04975 !'##molecule_type protein !'##residues 24-45 ##label LIN !'##note the His-Pro dipeptide may be found at position 24-25 REFERENCE S14806 !$#authors Baumann, U.; Huber, R.; Bode, W.; Grosse, D.; Lesjak, M.; !1Laurell, C.B. !$#journal J. Mol. Biol. (1991) 218:595-606 !$#title Crystal structure of cleaved human alpha(1)-antichymotrypsin !1at 2.7 A resolution and its comparison with other serpins. !$#cross-references MUID:91202538; PMID:2016749 !$#accession S14806 !'##molecule_type protein !'##residues 42-51,'R',53-54;388-396,'A',398 ##label BAU REFERENCE A92400 !$#authors Morii, M.; Travis, J. !$#journal J. Biol. Chem. (1983) 258:12749-12752 !$#title Amino acid sequence at the reactive site of human alpha-1- !1antichymotrypsin. !$#cross-references MUID:84032476; PMID:6556193 !$#contents annotation; inhibitory site REFERENCE S44458 !$#authors Korzus, E.; Luisetti, M.; Travis, J. !$#journal Biol. Chem. Hoppe-Seyler (1994) 375:335-341 !$#title Interactions of alpha-1-antichymotrypsin, alpha-1-proteinase !1inhibitor, and alpha-2-macroglobulin with the fungal enzyme, !1seaprose. !$#cross-references MUID:94354957; PMID:7521171 !$#accession S44458 !'##molecule_type protein !'##residues 36-45 ##label KOR COMMENT The concentration of this plasma protease inhibitor, which !1is synthesized in the liver, increases in the acute phase of !1inflammation or infection. It can inhibit neutrophil !1cathepsin G and mast cell chymase, both of which can convert !1angiotensin I to the active angiotensin II. GENETICS !$#gene GDB:AACT !'##cross-references GDB:118955; OMIM:107280 !$#map_position 14q32.1-14q32.1 CLASSIFICATION #superfamily antithrombin III KEYWORDS acute phase; Alzheimer's disease; amyloid; glycoprotein; !1inflammation; plasma; serine proteinase inhibitor FEATURE !$1-23 #domain (or 4-23) signal sequence #status predicted !8#label SIG\ !$24-433 #product alpha-1-antichymotrypsin #status predicted !8#label MAT\ !$33,93,106,127,186, !$271 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$383 #inhibitory_site Leu (chymotrypsin) #status !8experimental SUMMARY #length 433 #molecular-weight 48796 #checksum 888 SEQUENCE /// ENTRY S31507 #type complete TITLE serine proteinase inhibitor 2.4 - European woodmouse ORGANISM #formal_name Apodemus sylvaticus #common_name European woodmouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S31507 REFERENCE S31505 !$#authors Inglis, J.D.; Lee, M.; Hill, R.E. !$#submission submitted to the EMBL Data Library, December 1992 !$#accession S31507 !'##status preliminary !'##molecule_type mRNA !'##residues 1-418 ##label ING !'##cross-references EMBL:X69833; NID:g49418; PIDN:CAA49487.1; !1PID:g49419 CLASSIFICATION #superfamily antithrombin III SUMMARY #length 418 #molecular-weight 46918 #checksum 3628 SEQUENCE /// ENTRY ITHU #type complete TITLE alpha-1-antitrypsin precursor [validated] - human ALTERNATE_NAMES alpha-1-AT; alpha-1-proteinase inhibitor ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Nov-1980 #sequence_revision 31-Mar-1992 #text_change 15-Sep-2000 ACCESSIONS A21853; B21853; A93352; A90944; A58528; A23174; A93281; !1A32336; S14476; A24013; S13833; S23516; S23962; S55249; !1I39371; I39372; S63599; I39370; A35338; A01247 REFERENCE A21853 !$#authors Long, G.L.; Chandra, T.; Woo, S.L.C.; Davie, E.W.; Kurachi, !1K. !$#journal Biochemistry (1984) 23:4828-4837 !$#title Complete sequence of the cDNA for human alpha-1-antitrypsin !1and the gene for the S variant. !$#cross-references MUID:85047190; PMID:6093867 !$#accession A21853 !'##molecule_type mRNA !'##residues 1-418 ##label LON1 !'##cross-references GB:K02212; NID:g177830 !'##experimental_source M (normal) allele !$#accession B21853 !'##molecule_type DNA !'##residues 1-287,'V',289-418 ##label LON2 !'##cross-references GB:K02212; NID:g177830; PIDN:AAB59495.1; !1PID:g177831 !'##experimental_source S variant allele REFERENCE A93352 !$#authors Rosenberg, S.; Barr, P.J.; Najarian, R.C.; Hallewell, R.A. !$#journal Nature (1984) 312:77-80 !$#title Synthesis in yeast of a functional oxidation-resistant !1mutant of human alpha-1-antitrypsin. !$#cross-references MUID:85036645; PMID:6387509 !$#accession A93352 !'##molecule_type mRNA !'##residues 1-124,'H',126-325,'I',327-418 ##label ROS !'##cross-references EMBL:X01683; NID:g28965 REFERENCE A90944 !$#authors Bollen, A.; Herzog, A.; Cravador, A.; Herion, P.; Chuchana, !1P.; Vander Straten, A.; Loriau, R.; Jacobs, P.; Van Elsen, !1A. !$#journal DNA (1983) 2:255-264 !$#title Cloning and expression in Escherichia coli of full-length !1complementary DNA coding for human alpha-1-antitrypsin. !$#cross-references MUID:84107980; PMID:6319097 !$#accession A90944 !'##molecule_type mRNA !'##residues 1-138,'DG',141-272,'N',274-418 ##label BOL !'##cross-references GB:K01396; NID:g28965 !'##note this sequence has been corrected in reference A58528 REFERENCE A58528 !$#authors Colau, B.; Chuchana, P.; Bollen, A. !$#journal DNA (1984) 3:327-330 !$#title Revised sequence of full-length complementary DNA coding for !1human alpha-1-antitrypsin. !$#cross-references MUID:85026667; PMID:6333329 !$#contents corrections to sequence in A90944 !$#accession A58528 !'##molecule_type mRNA !'##residues 1-418 ##label COL !'##cross-references GB:K01396; NID:g28965; PIDN:CAA25838.1; PID:g28966 REFERENCE A23174 !$#authors Ciliberto, G.; Dente, L.; Cortese, R. !$#journal Cell (1985) 41:531-540 !$#title Cell-specific expression of a transfected human !1alpha-1-antitrypsin gene. !$#cross-references MUID:85176977; PMID:2985281 !$#accession A23174 !'##molecule_type mRNA !'##residues 1-11,13-173,'H',175-228,'D',230-418 ##label CIL !'##cross-references GB:M11465; NID:g177826; PIDN:AAA51546.1; !1PID:g177827 !'##note the authors state that this sequence corresponds to the M !1(normal) allele; 3 variants are described REFERENCE A93281 !$#authors Carrell, R.W.; Jeppsson, J.O.; Laurell, C.B.; Brennan, S.O.; !1Owen, M.C.; Vaughan, L.; Boswell, D.R. !$#journal Nature (1982) 298:329-334 !$#title Structure and variation of human alpha-1-antitrypsin. !$#cross-references MUID:82220135; PMID:7045697 !$#accession A93281 !'##molecule_type protein !'##residues 25-418 ##label CAR !'##note peptide sequence differences with A21853 (Leu-200 and the !1amidation states of residues 140, 182, and 183) are noted !1and explained REFERENCE A32336 !$#authors Zhu, X.J.; Kang, S.S.; Hargrove, K.; Shochat, D.; Jarrells, !1M.; Mojesky, M.; Chan, S.K. !$#journal Biochem. J. (1987) 246:25-36 !$#title The identification of epitopic sites in human !1alpha-1-proteinase inhibitor. !$#cross-references MUID:88049621; PMID:2445337 !$#accession A32336 !'##molecule_type protein !'##residues 25-418 ##label ZHU !'##note peptides were sequenced or partially sequenced and ordered by !1comparison with A21853 REFERENCE S14476 !$#authors Weiland, K.L.; Falany, C.N.; Dooley, T.P. !$#submission submitted to the EMBL Data Library, December 1989 !$#description Identification of a cDNA encoding a variant form of the !1human proteolytic enzyme inhibitor alpha-1 antitrypsin. !$#accession S14476 !'##molecule_type mRNA !'##residues 142-230,'Y',232-338 ##label WEI !'##cross-references EMBL:X17122; NID:g28636; PIDN:CAA34982.1; !1PID:g28637 !'##experimental_source a variant form REFERENCE A24013 !$#authors Riley, J.H.; Bathurst, I.C.; Edbrooke, M.R.; Carrell, R.W.; !1Craig, R.K. !$#journal FEBS Lett. (1985) 189:361-366 !$#title Alpha-1-antitrypsin and serum albumin mRNA accumulation in !1normal, acute phase and ZZ human liver. !$#cross-references MUID:86005469; PMID:3876243 !$#accession A24013 !'##molecule_type mRNA !'##residues 292-418 ##label RIL !'##cross-references EMBL:X02920; NID:g24437; PIDN:CAA26677.1; !1PID:g24438 REFERENCE S13833 !$#authors Schulze, A.J.; Baumann, U.; Knof, S.; Jaeger, E.; Huber, R.; !1Laurell, C.B. !$#journal Eur. J. Biochem. (1990) 194:51-56 !$#title Structural transition of alpha(1)-antitrypsin by a peptide !1sequentially similar to beta-strand s4A. !$#cross-references MUID:91071209; PMID:2253623 !$#accession S13833 !'##molecule_type protein !'##residues 25-41 ##label SCH REFERENCE S23516 !$#authors Niemann, M.A.; Narkates, A.J.; Miller, E.J. !$#journal Matrix (1992) 12:233-241 !$#title Isolation and serine protease inhibitory activity of the !144-residue, C-terminal fragment of alpha-1-antitrypsin from !1human placenta. !$#cross-references MUID:93024095; PMID:1406456 !$#accession S23516 !'##molecule_type protein !'##residues 375-409,'L',411-413,'S' ##label NIE REFERENCE S23962 !$#authors Dengler, R.; Eger, G.; Lottspeich, F.; Plewan, A.; Ogilvie, !1A.; Emmerich, B. !$#journal Biol. Chem. Hoppe-Seyler (1992) 373:581-588 !$#title Proteolytic inactivation of alpha(1)-proteinase inhibitor in !1vivo: detection, characterization and quantitation of the !1main fragment excreted in the urine of leukemia patients. !$#cross-references MUID:92384968; PMID:1515087 !$#accession S23962 !'##molecule_type protein !'##residues 44-53;384-392 ##label DEN REFERENCE S55249 !$#authors Dengler, R.; Lottspeich, F.; Oberthuer, W.; Mast, A.E.; !1Emmerich, B. !$#journal Biol. Chem. Hoppe-Seyler (1995) 376:165-172 !$#title Limited proteolysis of alpha(1)-proteinase inhibitor (alpha !1(1)-PI) in acute leukemia: studies on the resulting !1fragments and implication for the structure of the !1inactivated inhibitor. !$#cross-references MUID:95336645; PMID:7612193 !$#accession S55249 !'##molecule_type protein !'##residues 25-28;43-47;207-208;382-389;414-418 ##label DE2 REFERENCE I39371 !$#authors Leicht, M.; Long, G.L.; Chandra, T.; Kurachi, K.; Kidd, !1V.J.; Mace, M. !$#journal Nature (1982) 297:655-659 !$#title Sequence homology and structural comparison between the !1chromosomal human alpha 1-antitrypsin and chicken ovalbumin !1genes. !$#cross-references MUID:82220035; PMID:6979715 !$#accession I39371 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-67 ##label LEI1 !'##cross-references GB:J00064; NID:g177817; PIDN:AAB59369.1; !1PID:g177822 !$#accession I39372 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 196-225 ##label LEI2 !'##cross-references GB:J00066; NID:g177819; PIDN:AAB59370.1; !1PID:g177823 REFERENCE S63599 !$#authors Chang, W.S.W.; Wardell, M.R.; Lomas, D.A.; Carrell, R.W. !$#journal Biochem. J. (1996) 314:647-653 !$#title Probing serpin reactive-loop conformations by proteolytic !1cleavage. !$#cross-references MUID:96239126; PMID:8670081 !$#accession S63599 !'##molecule_type protein !'##residues 371-385 ##label CHA REFERENCE I39370 !$#authors Coutelle, C.; Speer, A.; Rogers, J.; Kalsheker, N.; !1Humphries, S.; Williamson, R. !$#journal Biomed. Biochim. Acta (1985) 44:421-431 !$#title Construction and partial characterization of a human liver !1cDNA library. !$#cross-references MUID:85225507; PMID:3873938 !$#accession I39370 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 387-399,'D',401-418 ##label COU !'##cross-references GB:M26123; NID:g177815; PIDN:AAA51545.1; !1PID:g177816 REFERENCE A35338 !$#authors Faber, J.P.; Weidinger, S.; Olek, K. !$#journal Am. J. Hum. Genet. (1990) 46:1158-1162 !$#title Sequence data of the rare deficient alpha-1-antitrypsin !1variant PI Zaugsburg. !$#cross-references MUID:90252805; PMID:2339709 !$#accession A35338 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type DNA !'##residues 122-124,'H',126-128;363-365,'K',367-369 ##label FAB !'##experimental_source mutant PI Zaugsberg !'##note this Z mutation with Lys-366 arose from the M2 variant with !1His-125 REFERENCE A50775 !$#authors Loebermann, H.; Tokuoka, R.; Deisenhofer, J.; Huber, R. !$#submission submitted to the Brookhaven Protein Data Bank, September !11988 !$#cross-references PDB:7API !$#contents annotation; X-ray crystallography, 3.0 angstroms, tetragonal !1form 1, residues 44-382;383-418 REFERENCE A50794 !$#authors Loebermann, H.; Tokuoka, R.; Deisenhofer, J.; Huber, R. !$#submission submitted to the Brookhaven Protein Data Bank, September !11988 !$#cross-references PDB:8API !$#contents annotation; X-ray crystallography, 3.1 angstroms, hexagonal !1form, residues 43-382;383-418 REFERENCE A50810 !$#authors Loebermann, H.; Tokuoka, R.; Deisenhofer, J.; Huber, R. !$#submission submitted to the Brookhaven Protein Data Bank, September !11988 !$#cross-references PDB:9API !$#contents annotation; X-ray crystallography, 3.0 angstroms, tetragonal !1form 2, residues 44-382;383-418 REFERENCE A58525 !$#authors Loebermann, H.; Tokuoka, R.; Deisenhofer, J.; Huber, R. !$#journal J. Mol. Biol. (1984) 177:531-556 !$#title Human alpha-1-proteinase inhibitor. Crystal structure !1analysis of two crystal modifications, molecular model and !1preliminary analysis of the implications for function. !$#cross-references MUID:84292309; PMID:6332197 !$#contents annotation; X-ray crystallography, 3.0 angstroms REFERENCE A58526 !$#authors Carrell, R.W.; Jeppsson, J.O.; Vaughan, L.; Brennan, S.O.; !1Owen, M.C.; Boswell, D.R. !$#journal FEBS Lett. (1981) 135:301-303 !$#title Human alpha-1-antitrypsin: carbohydrate attachment and !1sequence homology. !$#cross-references MUID:82095611; PMID:6976274 !$#contents annotation; carbohydrate attchment sites COMMENT The Z variant allele has Lys-366. Deficiency of the normal !1inhibitor in individuals homozygous for the Z allele can !1result in the development of chronic emphysema or infantile !1liver cirrhosis. GENETICS !$#gene GDB:PI !'##cross-references GDB:120289; OMIM:107400 !$#map_position 14q32.1-14q32.1 !$#introns 216/1; 306/2; 355/3 !$#note the first intron occurs before the initiator codon FUNCTION !$#description inhibitor of serine proteinases, primarily leukocyte !1elastase and collagenase !$#note it also inhibits plasmin, thrombin, kallikrein, trypsin, and !1chymotrypsin CLASSIFICATION #superfamily antithrombin III KEYWORDS acute phase; emphysema; glycoprotein; plasma; polymorphism; !1serine proteinase inhibitor FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-418 #product alpha-1-antitrypsin #status experimental !8#label MAT\ !$70,107,271 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$382 #inhibitory_site Met (elastase, collagenase) #status !8experimental SUMMARY #length 418 #molecular-weight 46736 #checksum 7644 SEQUENCE /// ENTRY ITBA #type fragment TITLE alpha-1-antitrypsin precursor - baboon (fragment) ALTERNATE_NAMES alpha-1-proteinase inhibitor ORGANISM #formal_name Papio sp. #common_name baboon DATE 02-Apr-1982 #sequence_revision 02-Apr-1982 #text_change 18-Jun-1999 ACCESSIONS A01248 REFERENCE A01248 !$#authors Kurachi, K.; Chandra, T.; Degen, S.J.F.; White, T.T.; !1Marchioro, T.L.; Woo, S.L.C.; Davie, E.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:6826-6830 !$#title Cloning and sequence of cDNA coding for alpha-1-antitrypsin. !$#cross-references MUID:82082539; PMID:7031661 !$#accession A01248 !'##molecule_type mRNA !'##residues 1-409 ##label KUR !'##cross-references GB:J00321; NID:g176561; PIDN:AAA35377.1; !1PID:g176562 COMMENT Alpha-1-antitrypsin is an inhibitor of serine proteinases. !1Its primary targets are leukocyte elastase and collagenase; !1it also inhibits plasmin, thrombin, kallikrein, trypsin, and !1chymotrypsin. CLASSIFICATION #superfamily antithrombin III KEYWORDS acute phase; glycoprotein; plasma; serine proteinase !1inhibitor FEATURE !$1-15 #domain signal sequence (fragment) #status predicted !8#label SIG\ !$16-409 #product alpha-1-antitrypsin #status predicted #label !8MAT\ !$61,98,262 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$373 #inhibitory_site Met (elastase, collagenase) #status !8predicted SUMMARY #length 409 #checksum 4799 SEQUENCE /// ENTRY ITSH #type complete TITLE alpha-1-antitrypsin precursor - sheep ALTERNATE_NAMES alpha-1-proteinase inhibitor ORGANISM #formal_name Ovis orientalis aries, Ovis ammon aries #common_name domestic sheep DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 18-Jun-1999 ACCESSIONS S05312 REFERENCE S05312 !$#authors Brown, W.M.; Dziegielewska, K.M.; Foreman, R.C.; Saunders, !1N.R.; Wu, Y. !$#journal Nucleic Acids Res. (1989) 17:6398 !$#title Nucleotide and deduced amino acid sequence of sheep alpha-1 !1antitrypsin. !$#cross-references MUID:89366677; PMID:2788872 !$#accession S05312 !'##molecule_type mRNA !'##residues 1-416 ##label BRO !'##cross-references EMBL:X15555; NID:g1369; PIDN:CAA33561.1; PID:g1370 !'##note the authors translated the codon ATC for residue 395 as Ala COMMENT Alpha-1-antitrypsin is an inhibitor of serine proteinases. !1Its primary targets are leukocyte elastase and collagenase; !1it also inhibits plasmin, thrombin, kallikrein, trypsin, and !1chymotrypsin. CLASSIFICATION #superfamily antithrombin III KEYWORDS acute phase; glycoprotein; plasma; serine proteinase !1inhibitor FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-416 #product alpha-1-antitrypsin #status predicted #label !8MAT\ !$68,105,269 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$380 #inhibitory_site Met (elastase, collagenase) #status !8predicted SUMMARY #length 416 #molecular-weight 45984 #checksum 236 SEQUENCE /// ENTRY ITRT #type complete TITLE alpha-1-antitrypsin precursor - rat ALTERNATE_NAMES alpha-1-proteinase inhibitor ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1992 #sequence_revision 31-Dec-1993 #text_change 16-Jun-2000 ACCESSIONS A33892; B33892; S08016; JX0123; A38823 REFERENCE A33892 !$#authors Chao, S.; Chai, K.X.; Chao, L.; Chao, J. !$#journal Biochemistry (1990) 29:323-329 !$#title Molecular cloning and primary structure of rat !1alpha-1-antitrypsin. !$#cross-references MUID:90148955; PMID:2302382 !$#accession A33892 !'##molecule_type mRNA !'##residues 4-411 ##label CHA !'##cross-references GB:M32247; NID:g203062; PIDN:AAA40788.1; !1PID:g203063 !$#accession B33892 !'##molecule_type protein !'##residues 25-57 ##label CH2 REFERENCE S08016 !$#authors Flink, I.L.; Bailey, T.; Morkin, E. !$#submission submitted to the EMBL Data Library, August 1989 !$#accession S08016 !'##molecule_type mRNA !'##residues 188-246,'I',248-321,'D',323-389 ##label FLI !'##cross-references EMBL:X16273; NID:g57299; PIDN:CAA34349.1; !1PID:g930263 REFERENCE JX0123 !$#authors Misumi, Y.; Sohda, M.; Ohkubo, K.; Takami, N.; Oda, K.; !1Ikehara, Y. !$#journal J. Biochem. (1990) 108:230-234 !$#title Molecular cloning and sequencing of the cDNA of rat !1alpha-1-protease inhibitor and its expression in COS-1 !1cells. !$#cross-references MUID:91035351; PMID:2229024 !$#accession JX0123 !'##molecule_type mRNA !'##residues 1-13,'G',15-83,'V',85-247,'Y',249-317,'N',319-411 ##label !1MIS !'##cross-references GB:D00675; NID:g220648; PIDN:BAA00579.1; !1PID:g220649 !'##experimental_source serum !$#accession A38823 !'##molecule_type protein !'##residues 25-45 ##label MI2 COMMENT Alpha-1-antitrypsin is an inhibitor of serine proteinases. !1Its primary targets are leukocyte elastase and collagenase; !1it also inhibits plasmin, thrombin, kallikrein, trypsin, and !1chymotrypsin. CLASSIFICATION #superfamily antithrombin III KEYWORDS acute phase; glycoprotein; plasma; serine proteinase !1inhibitor FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-411 #product alpha-1-antitrypsin #status experimental !8#label MAT\ !$64,101,265 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$376 #inhibitory_site Met (elastase, collagenase) #status !8predicted SUMMARY #length 411 #molecular-weight 46135 #checksum 2552 SEQUENCE /// ENTRY ITMSC #type complete TITLE alpha-1-antitrypsin precursor - ricefield mouse (Mus caroli) ALTERNATE_NAMES alpha-1-proteinase inhibitor ORGANISM #formal_name Mus caroli DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 18-Jun-1999 ACCESSIONS A34730 REFERENCE A34730 !$#authors Latimer, J.J.; Berger, F.G.; Baumann, H. !$#journal Mol. Cell. Biol. (1990) 10:760-769 !$#title Highly conserved upstream regions of the alpha-1-antitrypsin !1gene in two mouse species govern liver-specific expression !1by different mechanisms. !$#cross-references MUID:90136592; PMID:1689000 !$#accession A34730 !'##molecule_type mRNA !'##residues 1-412 ##label LAT !'##cross-references GB:M33567; NID:g191537; PIDN:AAA37128.1; !1PID:g309078 !'##note the authors translated the codon ACC for residue 63 as Asn and !1GTG for residue 235 as U. Residue 63 is included among the !1potential glycosylation sites COMMENT Alpha-1-antitrypsin is an inhibitor of serine proteinases. !1Its primary targets are leukocyte elastase and collagenase; !1it also inhibits plasmin, thrombin, kallikrein, trypsin, and !1chymotrypsin. COMMENT In Mus caroli, this protein is expressed not only in liver !1but also in kidney tubule cells, where it is regulated by !1androgens during development. CLASSIFICATION #superfamily antithrombin III KEYWORDS acute phase; glycoprotein; plasma; polymorphism; serine !1proteinase inhibitor FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-412 #product alpha-1-antitrypsin #status predicted #label !8MAT\ !$100,133,264,313 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$376 #inhibitory_site Met (elastase, collagenase) #status !8predicted SUMMARY #length 412 #molecular-weight 45872 #checksum 3579 SEQUENCE /// ENTRY S20608 #type complete TITLE heat shock protein Hsp47 precursor - human ALTERNATE_NAMES chaperonin; collagen-binding protein; colligin ORGANISM #formal_name Homo sapiens #common_name man DATE 22-Nov-1993 #sequence_revision 12-Apr-1996 #text_change 29-Oct-1999 ACCESSIONS S20608; S17329 REFERENCE S20608 !$#authors Clarke, E.P.; Sanwal, B.D. !$#journal Biochim. Biophys. Acta (1992) 1129:246-248 !$#title Cloning of a human collagen-binding protein, and its !1homology with rat gp46, chick hsp47 and mouse J6 proteins. !$#cross-references MUID:92110393; PMID:1309665 !$#accession S20608 !'##molecule_type mRNA !'##residues 1-417 ##label CLA !'##cross-references EMBL:X61598; NID:g30129; PIDN:CAA43795.1; !1PID:g30130 REFERENCE A57864 !$#authors Nagata, K. !$#journal Trends Biochem. Sci. (1996) 21:23-26 !$#title Hsp47: a collagen-specific molecular chaperone. !$#contents annotation; review article COMMENT This stress-induced glycoprotein of the ER lumen lacks !1protease inhibitor activity. GENETICS !$#gene GDB:CBP1 !'##cross-references GDB:129094; OMIM:600942 !$#map_position 3qcen-3qter FUNCTION !$#description Hsp47 associates transiently with procollagen to assist as a !1molecular chaperone in the pathway of collagen synthesis and !1secretion. It prevents secretion of improperly folded !1collagen and is induced by stresses such as heat shock. CLASSIFICATION #superfamily antithrombin III KEYWORDS collagen binding; endoplasmic reticulum; glycoprotein; heat !1shock; molecular chaperone; stress-induced protein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-417 #product heat shock protein Hsp47 #status predicted !8#label MAT\ !$414-417 #region endoplasmic reticulum retention signal\ !$119,124 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 417 #molecular-weight 46267 #checksum 33 SEQUENCE /// ENTRY A40968 #type complete TITLE heat shock protein 47 precursor - rat ALTERNATE_NAMES collagen-binding glycoprotein gp46; colligin; serine proteinase inhibitor homolog ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 17-Jul-1992 #sequence_revision 12-Apr-1996 #text_change 29-Oct-1999 ACCESSIONS A40968; S09313 REFERENCE A40968 !$#authors Clarke, E.P.; Cates, G.A.; Ball, E.H.; Sanwal, B.D. !$#journal J. Biol. Chem. (1991) 266:17230-17235 !$#title A collagen-binding protein in the endoplasmic reticulum of !1myoblasts exhibits relationship with serine protease !1inhibitors. !$#cross-references MUID:91373337; PMID:1654327 !$#accession A40968 !'##molecule_type mRNA !'##residues 1-417 ##label CLA !'##cross-references GB:M69246; NID:g204457; PIDN:AAA41270.1; !1PID:g204458 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE S09313 !$#authors Nandan, D.; Cates, G.A.; Ball, E.H.; Sanwal, B.D. !$#journal Arch. Biochem. Biophys. (1990) 278:291-296 !$#title Partial characterization of a collagen-binding, !1differentiation-related glycoprotein from skeletal !1myoblasts. !$#cross-references MUID:90225795; PMID:2158279 !$#accession S09313 !'##molecule_type protein !'##residues 18-32 ##label NAN REFERENCE A57864 !$#authors Nagata, K. !$#journal Trends Biochem. Sci. (1996) 21:23-26 !$#title Hsp47: a collagen-specific molecular chaperone. !$#contents annotation; review article COMMENT This stress-induced glycoprotein of the ER lumen lacks !1protease inhibitor activity. FUNCTION !$#description Hsp47 associates transiently with procollagen to assist as a !1molecular chaperone in the pathway of collagen synthesis and !1secretion. It prevents secretion of improperly folded !1collagen and is induced by stresses such as heat shock. CLASSIFICATION #superfamily antithrombin III KEYWORDS collagen binding; endoplasmic reticulum; glycoprotein; heat !1shock; molecular chaperone; stress-induced protein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-417 #product heat shock protein Hsp47 #status predicted !8#label MAT\ !$414-417 #region endoplasmic reticulum retention signal\ !$119,124,394 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 417 #molecular-weight 46517 #checksum 1345 SEQUENCE /// ENTRY A42843 #type complete TITLE heat shock protein Hsp47 precursor - mouse ALTERNATE_NAMES collagen-specific molecular chaperone, 47K; colligin; gp46; serine proteinase inhibitor homolog J6 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Sep-1993 #sequence_revision 12-Apr-1996 #text_change 16-Jun-2000 ACCESSIONS S23453; JQ2221; A39476; A38374; A42843 REFERENCE S23453 !$#authors Takechi, H.; Hirayoshi, K.; Nakai, A.; Kudo, H.; Saga, S.; !1Nagata, K. !$#journal Eur. J. Biochem. (1992) 206:323-329 !$#title Molecular cloning of a mouse 47-kDa heat-shock protein !1(HSP47), a collagen-binding stress protein, and its !1expression during the differentiation of F9 teratocarcinoma !1cells. !$#cross-references MUID:92283255; PMID:1317794 !$#accession S23453 !'##molecule_type mRNA !'##residues 1-417 ##label TAK !'##cross-references EMBL:X60676; NID:g51449; PIDN:CAA43091.1; !1PID:g51450 !'##experimental_source strain Balb/c REFERENCE JQ2221 !$#authors Hosokawa, N.; Takechi, H.; Yokota, S.; Hirayoshi, K.; !1Nagata, K. !$#journal Gene (1993) 126:187-193 !$#title Structure of the gene encoding the mouse 47-kDa heat-shock !1protein (HSP47). !$#cross-references MUID:93246243; PMID:8482533 !$#accession JQ2221 !'##molecule_type DNA !'##residues 1-211,'K',213-215,'K',217-417 ##label HOS !'##cross-references DDBJ:D12903; DDBJ:D12904; DDBJ:D12905; DDBJ:D12906; !1DDBJ:D12907; NID:g303676; PIDN:BAA02298.1; PID:g303678 !'##experimental_source liver REFERENCE A39476 !$#authors Wang, S.Y.; Gudas, L.J. !$#journal J. Biol. Chem. (1991) 266:14135 !$#cross-references MUID:91310706; PMID:1856236 !$#contents erratum !$#accession A39476 !'##molecule_type mRNA !'##residues 1-175,'P',177-269,'IA',272-276,'S',278-417 ##label WAN !'##cross-references GB:J05609 !'##experimental_source F9 teratocarcinoma cells REFERENCE A38374 !$#authors Wang, S.Y.; Gudas, L.J. !$#journal J. Biol. Chem. (1990) 265:15818-15822 !$#title A retinoic acid-inducible mRNA from F9 teratocarcinoma cells !1encodes a novel protease inhibitor homologue. !$#cross-references MUID:90368798; PMID:2394749 !$#accession A38374 !'##molecule_type mRNA !'##residues 'MPLGRGPGSRGEETPRGGSPWYCGEAKFQGDHTGRAQHRPG',53-175,'P', !1177-269,'IA',272-276,'S',278-417 ##label WA2 !'##cross-references GB:J05609; NID:g200965; PIDN:AAA03200.1; !1PID:g200966 !'##note this sequence has been revised REFERENCE A42843 !$#authors Wang, S.Y. !$#journal J. Biol. Chem. (1992) 267:15362-15366 !$#title Structure of the gene and its retinoic acid-regulatory !1region for murine J6 serpin. An F9 teratocarcinoma cell !1retinoic acid-inducible protein. !$#cross-references MUID:92348381; PMID:1639782 !$#contents annotation; splice junctions and 5'-flanking region REFERENCE A57864 !$#authors Nagata, K. !$#journal Trends Biochem. Sci. (1996) 21:23-26 !$#title Hsp47: a collagen-specific molecular chaperone. !$#contents annotation; review article COMMENT This stress-induced glycoprotein of the ER lumen lacks !1protease inhibitor activity. GENETICS !$#gene HSP47 !$#introns 207/1; 240/1; 317/3 !$#note alternatively spliced after heat shock in the 5' non-coding !1region FUNCTION !$#description Hsp47 associates transiently with procollagen to assist as a !1molecular chaperone in the pathway of collagen synthesis and !1secretion. It prevents secretion of improperly folded !1collagen and is induced by stresses such as heat shock. CLASSIFICATION #superfamily antithrombin III KEYWORDS collagen binding; endoplasmic reticulum; glycoprotein; heat !1shock; molecular chaperone; stress-induced protein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-417 #product heat shock protein Hsp47 #status predicted !8#label MAT\ !$414-417 #region endoplasmic reticulum retention signal\ !$119,124,394 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 417 #molecular-weight 46589 #checksum 1049 SEQUENCE /// ENTRY A41252 #type complete TITLE heat shock protein 47 precursor - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 03-Apr-1992 #sequence_revision 12-Apr-1996 #text_change 29-Oct-1999 ACCESSIONS A41252; A27656; S16673 REFERENCE A41252 !$#authors Hirayoshi, K.; Kudo, H.; Takechi, H.; Nakai, A.; Iwamatsu, !1A.; Yamada, K.M.; Nagata, K. !$#journal Mol. Cell. Biol. (1991) 11:4036-4044 !$#title HSP47: a tissue-specific, transformation-sensitive, !1collagen-binding heat shock protein of chicken embryo !1fibroblasts. !$#cross-references MUID:91304395; PMID:2072906 !$#accession A41252 !'##status preliminary !'##molecule_type mRNA !'##residues 1-405 ##label HIR !'##cross-references GB:X57157; NID:g63510; PIDN:CAA40444.1; PID:g63511 REFERENCE A27656 !$#authors Nagata, K.; Saga, S.; Yamada, K.M. !$#journal Biochem. Biophys. Res. Commun. (1988) 153:428-434 !$#title Characterization of a novel transformation-sensitive !1heat-shock protein (HSP47) that binds to collagen. !$#cross-references MUID:88240438; PMID:3377793 !$#accession A27656 !'##molecule_type protein !'##residues 16-51 ##label NAG REFERENCE A57864 !$#authors Nagata, K. !$#journal Trends Biochem. Sci. (1996) 21:23-26 !$#title Hsp47: a collagen-specific molecular chaperone. !$#contents annotation; review article COMMENT This stress-induced glycoprotein of the ER lumen lacks !1protease inhibitor activity. GENETICS !$#gene HSP47 FUNCTION !$#description Hsp47 associates transiently with procollagen to assist as a !1molecular chaperone in the pathway of collagen synthesis and !1secretion. It prevents secretion of improperly folded !1collagen and is induced by stresses such as heat shock. CLASSIFICATION #superfamily antithrombin III KEYWORDS collagen binding; endoplasmic reticulum; glycoprotein; heat !1shock; molecular chaperone; stress-induced protein FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-405 #product heat shock protein 47 #status predicted !8#label MAT\ !$402-405 #region endoplasmic reticulum retention signal\ !$107,112 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 405 #molecular-weight 45682 #checksum 2360 SEQUENCE /// ENTRY ANHU #type complete TITLE angiotensin precursor [validated] - human ALTERNATE_NAMES angiotensinogen CONTAINS angiotensin I; angiotensin II; angiotensin III ORGANISM #formal_name Homo sapiens #common_name man DATE 06-Jul-1982 #sequence_revision 19-Jan-1996 #text_change 08-Dec-2000 ACCESSIONS A35203; A31362; I37168; I37169; A60825; I39462; A90487; !1A90226; I54281; A01249 REFERENCE A35203 !$#authors Fukamizu, A.; Takahashi, S.; Seo, M.S.; Tada, M.; Tanimoto, !1K.; Uehara, S.; Murakami, K. !$#journal J. Biol. Chem. (1990) 265:7576-7582 !$#title Structure and expression of the human angiotensinogen gene. !1Identification of a unique and highly active promoter. !$#cross-references MUID:90237063; PMID:1692023 !$#accession A35203 !'##molecule_type DNA !'##residues 1-485 ##label FUK !'##cross-references GB:X15323; GB:X15324; GB:X15325; GB:X15326; !1GB:X15327 REFERENCE A31362 !$#authors Gaillard, I.; Clauser, E.; Corvol, P. !$#journal DNA (1989) 8:87-99 !$#title Structure of human angiotensinogen gene. !$#cross-references MUID:89170129; PMID:2924688 !$#accession A31362 !'##molecule_type DNA !'##residues 1-267,'M',269-332,'E',334-485 ##label GAI !'##cross-references GB:M24686; GB:M24687; GB:M24688 !'##note the authors translated the codon GAA for residue 333 as Gln REFERENCE I37168 !$#authors Nibu, Y.; Takahashi, S.; Tanimoto, K.; Murakami, K.; !1Fukamizu, A. !$#journal J. Biol. Chem. (1994) 269:28598-28605 !$#title Identification of cell type-dependent enhancer core element !1located in the 3'-downstream region of the human !1angiotensinogen gene. !$#cross-references MUID:95050659; PMID:7961807 !$#accession I37168 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-285 ##label NIB1 !'##cross-references EMBL:X15324; NID:g1197496; PIDN:CAA33385.1; !1PID:g1197497 !$#accession I37169 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 287-375 ##label NIB2 !'##cross-references EMBL:X15325; NID:g28695 REFERENCE A60825 !$#authors Kunapuli, S.P.; Benedict, C.R.; Kumar, A. !$#journal Arch. Biochem. Biophys. (1987) 254:642-646 !$#title Tissue specific hormonal regulation of the rat !1angiotensinogen gene expression. !$#cross-references MUID:87212053; PMID:3579322 !$#accession A60825 !'##molecule_type mRNA !'##residues 32-184 ##label KUN1 REFERENCE I39462 !$#authors Kunapuli, S.P.; Kumar, A. !$#journal Circ. Res. (1987) 60:786-790 !$#title Molecular cloning of human angiotensinogen cDNA and evidence !1for the presence of its mRNA in rat heart. !$#cross-references MUID:87244745; PMID:2885106 !$#accession I39462 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-267,'M',269-338 ##label KUN2 !'##cross-references GB:M69110; NID:g178643; PIDN:AAA52282.1; !1PID:g553181 REFERENCE A90487 !$#authors Kageyama, R.; Ohkubo, H.; Nakanishi, S. !$#journal Biochemistry (1984) 23:3603-3609 !$#title Primary structure of human preangiotensinogen deduced from !1the cloned cDNA sequence. !$#cross-references MUID:85000455; PMID:6089875 !$#accession A90487 !'##molecule_type mRNA !'##residues 1-267,'M',269-485 ##label KAG !'##cross-references GB:K02215; NID:g178639; PIDN:AAA51731.1; !1PID:g178640 !'##note it is uncertain whether Met-1 or Met-10 is the initiator REFERENCE A90226 !$#authors Tewksbury, D.A.; Dart, R.A.; Travis, J. !$#journal Biochem. Biophys. Res. Commun. (1981) 99:1311-1315 !$#title The amino terminal amino acid sequence of human !1angiotensinogen. !$#cross-references MUID:81255848; PMID:7259779 !$#accession A90226 !'##molecule_type protein !'##residues 34-46,'X',48-50,'S',52-57,'D' ##label TEW REFERENCE I54281 !$#authors Hixson, J.E.; Powers, P.K. !$#journal Hum. Genet. (1995) 96:110-112 !$#title Detection and characterization of new mutations in the human !1angiotensinogen gene (AGT). !$#cross-references MUID:95331754; PMID:7607642 !$#accession I54281 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 176-241,'I',243-267,'M',269-287,'ANLSAG' ##label HIX !'##cross-references GB:S78529; NID:g999316; PIDN:AAD14287.1; !1PID:g4261987 COMMENT Angiotensin I is released from angiotensinogen by renin, !1which is secreted in response to lowered blood pressure. !1Angiotensin I is converted to angiotensin II by dipeptidyl !1carboxypeptidase I (angiotensin-converting enzyme), !1primarily in the lungs. COMMENT The release of the amino-terminal residue (Asp-34) from !1angiotensin I and angiotensin II by aminopeptidases leads to !1[des-Asp-1]angiotensin I and angiotensin III, respectively. !1Also [des-Asp-1]angiotensin I is converted to angiotensin !1III by dipeptidyl carboxypeptidase I. COMMENT Angiotensin II causes vasoconstriction by direct action on !1blood vessels, by stimulating release of catecholamines and !1norepinephrine, and by direct action on the nervous system, !1which also induces thirst. COMMENT Angiotensin II and angiotensin III are equally potent in !1stimulating the synthesis of aldosterone, which increases !1the reabsorption of sodium ions by the renal tubules. COMMENT Angiotensinogen is synthesized in the liver and secreted !1into the plasma. The synthesis is increased by !1glucocorticoids and estrogens. GENETICS !$#gene GDB:AGT !'##cross-references GDB:118750; OMIM:106150 !$#map_position 1q42-1q43 !$#introns 286/1; 375/2; 423/3 CLASSIFICATION #superfamily antithrombin III KEYWORDS blood pressure control; glycoprotein; liver; plasma; !1vasoconstrictor FEATURE !$1-33 #domain (or 10-33) signal sequence #status predicted !8#label SIG\ !$34-485 #product angiotensinogen #status predicted #label !8MPT\ !$34-43 #product angiotensin I #status experimental #label !8PP1\ !$34-41 #product angiotensin II #status experimental #label !8PP2\ !$35-41 #product angiotensin III #status experimental #label !8PP3\ !$47,170,304,328 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 485 #molecular-weight 53124 #checksum 9394 SEQUENCE /// ENTRY ANRT #type complete TITLE angiotensin precursor - rat CONTAINS angiotensin I; angiotensin II; angiotensin III ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 18-Jun-1999 ACCESSIONS A93945; A90456; A01251 REFERENCE A93945 !$#authors Ohkubo, H.; Kageyama, R.; Ujihara, M.; Hirose, T.; Inayama, !1S.; Nakanishi, S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:2196-2200 !$#title Cloning and sequenc analysis of cDNA for rat !1angiotensinogen. !$#cross-references MUID:83169849; PMID:6572971 !$#accession A93945 !'##molecule_type mRNA !'##residues 1-477 ##label OHK !'##cross-references GB:L00094; GB:J00704; NID:g202912; PIDN:AAA98779.1; !1PID:g202914 REFERENCE A90456 !$#authors Bouhnik, J.; Clauser, E.; Strosberg, D.; Frenoy, J.P.; !1Menard, J.; Corvol, P. !$#journal Biochemistry (1981) 20:7010-7015 !$#title Rat angiotensinogen and Des(antiotensinI)angiotensinogen: !1purification, characterization, and partial sequencing. !$#cross-references MUID:82091819; PMID:6797467 !$#accession A90456 !'##molecule_type protein !'##residues 25-41 ##label BOU COMMENT Angiotensin I is released from angiotensinogen by renin, !1which is secreted in response to lowered blood pressure. !1Angiotensin I is converted to angiotensin II by dipeptidyl !1carboxypeptidase I (angiotensin-converting enzyme), !1primarily in the lungs. COMMENT The release of the amino-terminal residue (Asp-25) from !1angiotensin I and angiotensin II by aminopeptidases leads to !1[des-Asp-1]angiotensin I and angiotensin III, respectively. !1Also [des-Asp-1]angiotensin I is converted to angiotensin !1III by dipeptidyl carboxypeptidase I. COMMENT Angiotensinogen is synthesized in the liver and secreted !1into the plasma. The angiotensinogen mRNA has been found !1also in other tissues including brain, kidney, adrenal !1gland, ovary, and lung. CLASSIFICATION #superfamily antithrombin III KEYWORDS blood pressure control; glycoprotein; liver; plasma; !1vasoconstrictor FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-477 #product angiotensinogen #status predicted #label !8MPT\ !$25-34 #product angiotensin I #status experimental #label !8PP1\ !$25-32 #product angiotensin II #status experimental #label !8PP2\ !$26-32 #product angiotensin III #status experimental #label !8PP3\ !$295,319 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 477 #molecular-weight 51981 #checksum 3820 SEQUENCE /// ENTRY A29978 #type complete TITLE angiotensin precursor - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A29978 REFERENCE A29978 !$#authors Clouston, W.M.; Evans, B.A.; Haralambidis, J.; Richards, !1R.I. !$#journal Genomics (1988) 2:240-248 !$#title Molecular cloning of the mouse angiotensinogen gene. !$#cross-references MUID:88284703; PMID:3397061 !$#accession A29978 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-477 ##label CLO !'##cross-references GB:AF045887; GB:J03046; NID:g2842773; !1PIDN:AAC01765.1; PID:g2842775 GENETICS !$#introns 277/1; 366/2; 414/3 CLASSIFICATION #superfamily antithrombin III KEYWORDS blood pressure control FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-477 #product angiotensinogen #status predicted #label MAT SUMMARY #length 477 #molecular-weight 51990 #checksum 689 SEQUENCE /// ENTRY JC2318 #type complete TITLE angiotensin precursor - sheep ALTERNATE_NAMES angiotensinogen ORGANISM #formal_name Ovis orientalis aries, Ovis ammon aries #common_name domestic sheep DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS JC2318; A25406 REFERENCE JC2318 !$#authors Nagase, M.; Suzuki, F.; Fukamizu, A.; Takeda, N.; Takeuchi, !1K.; Murakami, K.; Nakamura, Y. !$#journal Biosci. Biotechnol. Biochem. (1994) 58:1884-1885 !$#title Sequencing and expression of sheep angiotensinogen cDNA. !$#cross-references MUID:95072318; PMID:7765514 !$#accession JC2318 !'##molecule_type mRNA !'##residues 1-476 ##label NAG !'##cross-references DDBJ:D17520; NID:g575593; PIDN:BAA04470.1; !1PID:g1197183 !'##experimental_source liver !'##note the authors translated the codon TTC for residue 465 as Leu REFERENCE A25406 !$#authors Fernley, R.T.; John, M.; Niall, H.D.; Coghlan, J.P. !$#journal Eur. J. Biochem. (1986) 154:597-601 !$#title Purification and characterization of ovine angiotensinogen. !$#cross-references MUID:86136099; PMID:3081342 !$#accession A25406 !'##molecule_type protein !'##residues 25-37,'X',39 ##label FER CLASSIFICATION #superfamily antithrombin III KEYWORDS blood pressure control; glycoprotein FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$24-476 #product angiotensinogen #status predicted #label !8MPT\ !$25-34 #product angiotensin #status predicted #label MAT\ !$295,362 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 476 #molecular-weight 51303 #checksum 5908 SEQUENCE /// ENTRY DXBHZ #type complete TITLE protein Z4 - barley ALTERNATE_NAMES major endosperm albumin ORGANISM #formal_name Hordeum vulgare #common_name barley DATE 30-Jun-1987 #sequence_revision 01-Dec-2000 #text_change 01-Dec-2000 ACCESSIONS S13822; A01252 REFERENCE S13822 !$#authors Brandt, A.; Svendsen, I.; Hejgaard, J. !$#journal Eur. J. Biochem. (1990) 194:499-505 !$#title A plant serpin gene. Structure, organization and expression !1of the gene encoding barley protein Z(4). !$#cross-references MUID:91099324; PMID:2269280 !$#accession S13822 !'##status preliminary !'##molecule_type DNA !'##residues 1-399 ##label BRA !'##cross-references GB:X51726; NID:g19067; PIDN:CAA36015.1; PID:g19068 REFERENCE A91332 !$#authors Hejgaard, J.; Rasmussen, S.K.; Brandt, A.; Svendsen, I. !$#journal FEBS Lett. (1985) 180:89-94 !$#title Sequence homology between barley endosperm protein Z and !1protease inhibitors of the alpha-1-antitrypsin family. !$#accession A01252 !'##molecule_type mRNA !'##residues 220-399 ##label HEJ !'##cross-references GB:X05902; NID:g19078; PIDN:CAA29331.1; PID:g19079 !'##note most of the sequence has been confirmed by amino acid !1sequencing REFERENCE A90095 !$#authors Nielsen, G.; Johansen, H.; Jensen, J.; Hejgaard, J. !$#journal Barley Genet. Newsl. (1983) 13:55-57 !$#title Localization on barley chromosome 4 of genes coding for !1beta-amylase (Bmyl) and protein Z (Pazl). !$#contents annotation; map position COMMENT A major component of the endosperm albumin, this protein !1acts as a storage protein during grain filling, contributing !1a substantial part of the grain's lysine. Sequence homology !1with proteins of the antithrombin-III superfamily suggests !1that it also has an inhibitory function during filling or !1germination. GENETICS !$#gene Pazl !$#map_position 4 CLASSIFICATION #superfamily antithrombin III KEYWORDS serine proteinase inhibitor; storage protein FEATURE !$357 #inhibitory_site Met (unidentified proteinase) !8#status predicted SUMMARY #length 399 #molecular-weight 43276 #checksum 1438 SEQUENCE /// ENTRY WMVZS3 #type complete TITLE antithrombin-III homolog - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jun-2000 ACCESSIONS JS0211 REFERENCE JS0211 !$#authors Boursnell, M.E.G.; Foulds, I.J.; Campbell, J.I.; Binns, M.M. !$#journal J. Gen. Virol. (1988) 69:2995-3003 !$#title Non-essential genes in the vaccinia virus HindIII K !1fragment: a gene related to serine protease inhibitors and a !1gene related to the 37K vaccinia virus major envelope !1antigen. !$#cross-references MUID:89067908; PMID:3264331 !$#accession JS0211 !'##molecule_type DNA !'##residues 1-369 ##label BOU !'##cross-references GB:D00382; NID:g222704; PIDN:BAA00287.1; !1PID:g222706 CLASSIFICATION #superfamily antithrombin III KEYWORDS glycoprotein; serine proteinase inhibitor FEATURE !$157,184,228,238,294 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$336 #inhibitory_site Arg (serine proteinase) #status !8predicted SUMMARY #length 369 #molecular-weight 42285 #checksum 1689 SEQUENCE /// ENTRY WMVZ1E #type complete TITLE antithrombin-III homolog - vaccinia virus (strain Copenhagen) ALTERNATE_NAMES K2L protein; serine proteinase inhibitor ORGANISM #formal_name vaccinia virus #note host Homo sapiens (man) DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 18-Jun-1999 ACCESSIONS A42505 REFERENCE A42501 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:517-563 !$#title Appendix to "The complete DNA sequence of vaccinia virus". !$#accession A42505 !'##molecule_type DNA !'##residues 1-369 ##label GOE !'##cross-references GB:M35027; NID:g335317; PIDN:AAA48006.1; !1PID:g335354 !'##experimental_source strain Copenhagen REFERENCE A42531 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:247-266 !$#title The complete DNA sequence of vaccinia virus. !$#cross-references MUID:91021027; PMID:2219722 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given CLASSIFICATION #superfamily antithrombin III KEYWORDS glycoprotein; serine proteinase inhibitor FEATURE !$157,184,228,238,294 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$336 #inhibitory_site Arg (serine proteinase) #status !8predicted SUMMARY #length 369 #molecular-weight 42299 #checksum 1308 SEQUENCE /// ENTRY WMVZHI #type complete TITLE antithrombin-III homolog 3 - cowpox virus ALTERNATE_NAMES hemorrhage-inducing 38K protein ORGANISM #formal_name cowpox virus DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 18-Jun-1999 ACCESSIONS A26477 REFERENCE A26477 !$#authors Pickup, D.J.; Ink, B.S.; Hu, W.; Ray, C.A.; Joklik, W.K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:7698-7702 !$#title Hemorrhage in lesions caused by cowpox virus is induced by a !1viral protein that is related to plasma protein inhibitors !1of serine proteases. !$#cross-references MUID:87017016; PMID:3532120 !$#accession A26477 !'##molecule_type DNA !'##residues 1-341 ##label PIC !'##cross-references GB:M14217; NID:g323401; PIDN:AAA42922.1; !1PID:g323402 COMMENT This viral protein may inhibit serine proteases involved in !1the blood coagulation process in the host. CLASSIFICATION #superfamily antithrombin III KEYWORDS glycoprotein; serine proteinase inhibitor FEATURE !$35,182,213 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 341 #molecular-weight 38077 #checksum 1134 SEQUENCE /// ENTRY WMVZB4 #type complete TITLE antithrombin-III homolog 3 - vaccinia virus (strain Copenhagen) ALTERNATE_NAMES B14R protein; serine proteinase inhibitor ORGANISM #formal_name vaccinia virus #note host Homo sapiens (man) DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 18-Jun-1999 ACCESSIONS D42527 REFERENCE A42501 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:517-563 !$#title Appendix to "The complete DNA sequence of vaccinia virus". !$#accession D42527 !'##molecule_type DNA !'##residues 1-222 ##label GOE !'##cross-references GB:M35027; NID:g335317; PIDN:AAA48211.1; !1PID:g335559 !'##experimental_source strain Copenhagen REFERENCE A42531 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:247-266 !$#title The complete DNA sequence of vaccinia virus. !$#cross-references MUID:91021027; PMID:2219722 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given CLASSIFICATION #superfamily antithrombin III KEYWORDS glycoprotein; serine proteinase inhibitor FEATURE !$62,93 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 222 #molecular-weight 24911 #checksum 2097 SEQUENCE /// ENTRY WMVZF3 #type complete TITLE antithrombin-III homolog - fowlpox virus (isolate HP-438[Munich]) ORGANISM #formal_name fowlpox virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jun-2000 ACCESSIONS C29963 REFERENCE JT0442 !$#authors Tomley, F.; Binns, M.; Campbell, J.; Boursnell, M. !$#journal J. Gen. Virol. (1988) 69:1025-1040 !$#title Sequence analysis of an 11.2 kilobase, near-terminal, BamHI !1fragment of fowlpox virus. !$#cross-references MUID:88229622; PMID:2836548 !$#accession C29963 !'##molecule_type DNA !'##residues 1-148 ##label TOM !'##cross-references GB:D00295; NID:g221380; PIDN:BAA00194.1; !1PID:g221385 CLASSIFICATION #superfamily antithrombin III KEYWORDS early protein SUMMARY #length 148 #molecular-weight 16464 #checksum 5912 SEQUENCE /// ENTRY WMVZS1 #type complete TITLE antithrombin-III homolog 1 - vaccinia virus (strain WR) ALTERNATE_NAMES B22R protein; serine proteinase inhibitor 1 ORGANISM #formal_name vaccinia virus DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jun-2000 ACCESSIONS A30175; B34035; JQ1816 REFERENCE A30175 !$#authors Kotwal, G.J.; Moss, B. !$#journal J. Virol. (1989) 63:600-606 !$#title Vaccinia virus encodes two proteins that are structurally !1related to members of the plasma serine protease inhibitor !1superfamily. !$#cross-references MUID:89094985; PMID:2783466 !$#accession A30175 !'##molecule_type DNA !'##residues 1-353 ##label KOT !'##cross-references EMBL:D00582; NID:g222702; PIDN:BAA00459.1; !1PID:g222703 REFERENCE A34035 !$#authors Smith, G.L.; Howard, S.T.; Chan, Y.S. !$#journal J. Gen. Virol. (1989) 70:2333-2343 !$#title Vaccinia virus encodes a family of genes with homology to !1serine proteinase inhibitors. !$#cross-references MUID:89381686; PMID:2778436 !$#accession B34035 !'##molecule_type DNA !'##residues 1-353 ##label SMI !'##cross-references EMBL:D00582; NID:g222702; PIDN:BAA00459.1; !1PID:g222703 REFERENCE JQ1767 !$#authors Smith, G.L.; Chan, Y.S.; Howard, S.T. !$#journal J. Gen. Virol. (1991) 72:1349-1376 !$#title Nucleotide sequence of 42kbp of vaccinia virus strain WR !1from near the right inverted terminal repeat. !$#cross-references MUID:91259063; PMID:2045793 !$#accession JQ1816 !'##molecule_type DNA !'##residues 1-353 ##label SM2 !'##cross-references DDBJ:D11079; NID:g222717; PIDN:BAA01852.1; !1PID:g222767 CLASSIFICATION #superfamily antithrombin III KEYWORDS glycoprotein; proteinase inhibitor FEATURE !$105,205,225,284,317 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$318 #inhibitory_site Phe (serine proteinase) #status !8predicted SUMMARY #length 353 #molecular-weight 40466 #checksum 5083 SEQUENCE /// ENTRY WMVZ2C #type complete TITLE antithrombin-III homolog 1 - vaccinia virus (strain Copenhagen) ALTERNATE_NAMES C12L protein; serine proteinase inhibitor ORGANISM #formal_name vaccinia virus #note host Homo sapiens (man) DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 18-Jun-1999 ACCESSIONS B42503 REFERENCE A42501 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:517-563 !$#title Appendix to "The complete DNA sequence of vaccinia virus". !$#accession B42503 !'##molecule_type DNA !'##residues 1-353 ##label GOE !'##cross-references GB:M35027; NID:g335317; PIDN:AAA47984.1; !1PID:g335332 !'##experimental_source strain Copenhagen REFERENCE A42531 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:247-266 !$#title The complete DNA sequence of vaccinia virus. !$#cross-references MUID:91021027; PMID:2219722 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given CLASSIFICATION #superfamily antithrombin III KEYWORDS glycoprotein; serine proteinase inhibitor FEATURE !$105,205,225,284,317 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$318 #inhibitory_site Phe (serine proteinase) #status !8predicted SUMMARY #length 353 #molecular-weight 40387 #checksum 5234 SEQUENCE /// ENTRY G36857 #type complete TITLE B25R protein - variola virus ALTERNATE_NAMES C12L protein (COP) ORGANISM #formal_name variola virus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 23-Mar-2001 ACCESSIONS G36857; S46882 REFERENCE A36859 !$#authors Blinov, V.M. !$#submission submitted to GenBank, November 1992 !$#accession G36857 !'##status preliminary !'##molecule_type DNA !'##residues 1-372 ##label BLI !'##cross-references GB:X69198; NID:g456758; PIDN:CAA49134.1; !1PID:g457084 !'##experimental_source strain India-1967, ssp. major, isolate Ind3 REFERENCE S46868 !$#authors Kolykhalov, A.A.; Blinov, V.M.; Gytorov, V.V.; Pozdnyakov, !1S.G.; Chizhikov, V.E.; Frolov, I.V.; Totmenin, A.V.; !1Shchelkunov, S.N.; Sandakhchiev, L.S. !$#submission submitted to the EMBL Data Library, April 1992 !$#description Nucleotide sequence analysis of the region of Variola virus !1XhoI F O H P Q genome fragment. !$#accession S46882 !'##status preliminary !'##molecule_type DNA !'##residues 1-372 ##label KOL !'##cross-references EMBL:X67117; NID:g516428; PIDN:CAA47534.1; !1PID:g516443 !'##experimental_source strain India-1967, isolate Ind3 CLASSIFICATION #superfamily antithrombin III SUMMARY #length 372 #molecular-weight 43135 #checksum 6299 SEQUENCE /// ENTRY S24676 #type complete TITLE serpin - Ectromelia virus ORGANISM #formal_name Ectromelia virus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S24676 REFERENCE S24675 !$#authors Senkevich, T. !$#submission submitted to the EMBL Data Library, August 1992 !$#accession S24676 !'##status preliminary !'##molecule_type DNA !'##residues 1-344 ##label SEN !'##cross-references EMBL:Z14256; NID:g59257; PIDN:CAA78623.1; !1PID:g59259 CLASSIFICATION #superfamily antithrombin III SUMMARY #length 344 #molecular-weight 39359 #checksum 918 SEQUENCE /// ENTRY WMVZW2 #type complete TITLE antithrombin-III homolog 2 - vaccinia virus ALTERNATE_NAMES B13R protein; serine proteinase inhibitor 2 ORGANISM #formal_name vaccinia virus DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jun-2000 ACCESSIONS A34035; JQ1807; B30175; C42527 REFERENCE A34035 !$#authors Smith, G.L.; Howard, S.T.; Chan, Y.S. !$#journal J. Gen. Virol. (1989) 70:2333-2343 !$#title Vaccinia virus encodes a family of genes with homology to !1serine proteinase inhibitors. !$#cross-references MUID:89381686; PMID:2778436 !$#accession A34035 !'##molecule_type DNA !'##residues 1-345 ##label SMI !'##cross-references EMBL:D00581; NID:g222694; PIDN:BAA00458.1; !1PID:g222695 !'##experimental_source strain WR REFERENCE JQ1767 !$#authors Smith, G.L.; Chan, Y.S.; Howard, S.T. !$#journal J. Gen. Virol. (1991) 72:1349-1376 !$#title Nucleotide sequence of 42kbp of vaccinia virus strain WR !1from near the right inverted terminal repeat. !$#cross-references MUID:91259063; PMID:2045793 !$#accession JQ1807 !'##molecule_type DNA !'##residues 1-345 ##label SM2 !'##cross-references DDBJ:D11079; NID:g222717; PIDN:BAA01843.1; !1PID:g222758 !'##experimental_source strain WR REFERENCE A30175 !$#authors Kotwal, G.J.; Moss, B. !$#journal J. Virol. (1989) 63:600-606 !$#title Vaccinia virus encodes two proteins that are structurally !1related to members of the plasma serine protease inhibitor !1superfamily. !$#cross-references MUID:89094985; PMID:2783466 !$#accession B30175 !'##molecule_type DNA !'##residues 1-56,'V',61-129,'S',131-133,'DV',136-164,'CI',167-171,'E', !1173-179,'T',181-199,'V',201-205,'N',207-228,'M',230-345 !1##label KOT REFERENCE A42501 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:517-563 !$#title Appendix to "The complete DNA sequence of vaccinia virus". !$#accession C42527 !'##molecule_type DNA !'##residues 11-47,'T',49-51,'T',53-78,'F',80-81,'G',83-124,'SN' ##label !1GOE !'##cross-references GB:M35027; NID:g335317; PIDN:AAA48210.1; !1PID:g335558 !'##experimental_source strain Copenhagen REFERENCE A42531 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:247-266 !$#title The complete DNA sequence of vaccinia virus. !$#cross-references MUID:91021027; PMID:2219722 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene SPI-2 CLASSIFICATION #superfamily antithrombin III KEYWORDS glycoprotein; serine proteinase inhibitor FEATURE !$35,59,185,216 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 345 #molecular-weight 38536 #checksum 9829 SEQUENCE /// ENTRY A39249 #type complete TITLE neutrophil cytosol factor 1 - human ALTERNATE_NAMES 47K autosomal chronic granulomatous disease protein; multicomponent microbicidal oxidase 47K cytosolic component; NCF-47K protein; p47-phox ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 18-Jun-1999 ACCESSIONS A35926; A39249; A54067; I59190; A32762; A41385 REFERENCE A35926 !$#authors Rodaway, A.R.F.; Teahan, C.G.; Casimir, C.M.; Segal, A.W.; !1Bentley, D.L. !$#journal Mol. Cell. Biol. (1990) 10:5388-5396 !$#title Characterization of the 47-kilodalton autosomal chronic !1granulomatous disease protein: tissue-specific expression !1and transcriptional control by retinoic acid. !$#cross-references MUID:90377229; PMID:2398896 !$#accession A35926 !'##molecule_type mRNA !'##residues 1-390 ##label ROD !'##cross-references GB:M55067; GB:M38755; NID:g189050; PIDN:AAA59901.1; !1PID:g189051 REFERENCE A39249 !$#authors Volpp, B.D.; Nauseef, W.M.; Donelson, J.E.; Moser, D.R.; !1Clark, R.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:9563 !$#contents erratum !$#accession A39249 !'##molecule_type mRNA !'##residues 1-390 ##label VOL !'##cross-references GB:M25665; GB:M26193; NID:g189107; PIDN:AAA57209.1; !1PID:g189108 REFERENCE A41385 !$#authors Volpp, B.D.; Nauseef, W.M.; Donelson, J.E.; Moser, D.R.; !1Clark, R.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:7195-7199 !$#title Cloning of the cDNA and functional expression of the !147-kilodalton cytosolic component of human neutrophil !1respiratory burst oxidase. !$#cross-references MUID:89386707; PMID:2550933 !$#contents annotation !$#note the sequence reported has been extensively revised in !1reference A39249 REFERENCE A32762 !$#authors Lomax, K.J.; Leto, T.L.; Nunoi, H.; Gallin, J.I.; Malech, !1H.L. !$#journal Science (1989) 245:409-412 !$#title Recombinant 47-kilodalton cytosol factor restores NADPH !1oxidase in chronic granulomatous disease. !$#cross-references MUID:89332501; PMID:2547247 !$#contents annotation !$#note the sequence reported has been extensively revised and now !1agrees with that shown REFERENCE A54067 !$#authors Finan, P.; Shimizu, Y.; Gout, I.; Hsuan, J.; Truong, O.; !1Butcher, C.; Bennett, P.; Waterfield, M.D.; Kellie, S. !$#journal J. Biol. Chem. (1994) 269:13752-13755 !$#title An SH3 domain and proline-rich sequence mediate an !1interaction between two components of the phagocyte NADPH !1oxidase complex. !$#cross-references MUID:94245680; PMID:8188650 !$#accession A54067 !'##molecule_type protein !'##residues 8-16;44-52;71-77 ##label FIN !'##experimental_source differentiated HL-60 cells REFERENCE I59190 !$#authors Casimir, C.M.; Bu-Ghanim, H.N.; Rodaway, A.R.F.; Bentley, !1D.L.; Rowe, P.; Segal, A.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:2753-2757 !$#title Autosomal recessive chronic granulomatous disease caused by !1deletion at a dinucleotide repeat. !$#cross-references MUID:91187870; PMID:2011585 !$#accession I59190 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 14-24 ##label CAS !'##cross-references GB:M60941; NID:g189948; PIDN:AAA60086.1; !1PID:g189949 !'##note a GT dinucleotide deletion at a GT-GT repeat causes a !1frameshift after residue 24 in three unrelated cases of !1autosomal recessive chronic granulomatous disease COMMENT This protein is required for activation of the latent NADPH !1oxidase, which is necessary for superoxide production. It is !1absent in most patients with autosomal recessive chronic !1granulomatous disease. GENETICS !$#gene GDB:NCF1 !'##cross-references GDB:120222; OMIM:233700 !$#map_position 7q11.23-7q11.23 !$#introns 24/3 !$#note the list of introns is incomplete CLASSIFICATION #superfamily neutrophil cytosol factor 1; SH3 homology KEYWORDS cytosol; neutrophil FEATURE !$163-210 #domain SH3 homology #label SH31\ !$233-280 #domain SH3 homology #label SH32 SUMMARY #length 390 #molecular-weight 44682 #checksum 4667 SEQUENCE /// ENTRY ANHU1 #type complete TITLE endothelin 1 precursor [validated] - human CONTAINS big endothelin 1; endothelin 1 ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 23-Mar-2001 ACCESSIONS A36517; A34108; A32111; S00563; I55582; A33399; S16966 REFERENCE A36517 !$#authors Inoue, A.; Yanagisawa, M.; Takuwa, Y.; Mitsui, Y.; !1Kobayashi, M.; Masaki, T. !$#journal J. Biol. Chem. (1989) 264:14954-14959 !$#title The human preproendothelin-1 gene. Complete nucleotide !1sequence and regulation of expression. !$#cross-references MUID:89359303; PMID:2670930 !$#accession A36517 !'##molecule_type DNA !'##residues 1-212 ##label INO !'##cross-references GB:J05008; NID:g340555; PIDN:AAA52339.1; !1PID:g556203 REFERENCE A34108 !$#authors Bloch, K.D.; Friedrich, S.P.; Lee, M.E.; Eddy, R.L.; Shows, !1T.B.; Quertermous, T. !$#journal J. Biol. Chem. (1989) 264:10851-10857 !$#title Structural organization and chromosomal assignment of the !1gene encoding endothelin. !$#cross-references MUID:89278161; PMID:2659594 !$#accession A34108 !'##molecule_type DNA !'##residues 1-212 ##label BLO !'##cross-references GB:M25380; GB:J04819; NID:g182257; PIDN:AAA52407.1; !1PID:g182259 REFERENCE A32111 !$#authors Inoue, A.; Yanagisawa, M.; Kimura, S.; Kasuya, Y.; Miyauchi, !1T.; Goto, K.; Masaki, T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:2863-2867 !$#title The human endothelin family: three structurally and !1pharmacologically distinct isopeptides predicted by three !1separate genes. !$#cross-references MUID:89202426; PMID:2649896 !$#accession A32111 !'##molecule_type DNA !'##residues 27-77 ##label IN2 !'##cross-references GB:M25549; DDBJ:J04522; NID:g556201; !1PIDN:AAA52338.1; PID:g556202 !'##note the authors translated the codon CTC for residue 47 as Lys REFERENCE S00563 !$#authors Itoh, Y.; Yanagisawa, M.; Ohkubo, S.; Kimura, C.; Kosaka, !1T.; Inoue, A.; Ishida, N.; Mitsui, Y.; Onda, H.; Fujino, M.; !1Masaki, T. !$#journal FEBS Lett. (1988) 231:440-444 !$#title Cloning and sequence analysis of cDNA encoding the precursor !1of a human endothelium-derived vasoconstrictor peptide, !1endothelin: identity of human and porcine endothelin. !$#cross-references MUID:88196441; PMID:3282927 !$#accession S00563 !'##molecule_type mRNA !'##residues 1-212 ##label ITO !'##cross-references EMBL:Y00749; NID:g31254; PIDN:CAA68718.1; !1PID:g31255 REFERENCE I55582 !$#authors Benatti, L.; Bonecchi, L.; Cozzi, L.; Sarmientos, P. !$#journal J. Clin. Invest. (1993) 91:1149-1156 !$#title Two preproendothelin 1 mRNAs transcribed by alternative !1promoters. !$#cross-references MUID:93195041; PMID:8450044 !$#accession I55582 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-212 ##label BEN !'##cross-references GB:S56805; NID:g298590; PIDN:AAB25760.1; !1PID:g298591 !'##note two forms of mRNA were found that differed in the !15'-untranslated region REFERENCE A33399 !$#authors Fleminger, G.; Bousso-Mittler, D.; Bdolah, A.; Kloog, Y.; !1Sokolovsky, M. !$#journal Biochem. Biophys. Res. Commun. (1989) 162:1317-1323 !$#title Immunological and structural characterization of !1sarafotoxin/endothelin family of peptides. !$#cross-references MUID:89350948; PMID:2475108 !$#accession A33399 !'##molecule_type protein !'##residues 60-62,'X',64 ##label FLE REFERENCE S16966 !$#authors Fabbrini, M.S.; Valsasina, B.; Nitti, G.; Benatti, L.; !1Vitale, A. !$#journal FEBS Lett. (1991) 286:91-94 !$#title The signal peptide of human preproendothelin-1. !$#cross-references MUID:91323544; PMID:1864385 !$#contents annotation !$#note the authors use genetically engineered variants of !1endothelin-1 mRNA to prove that the mechanism for secretion !1of this protein involves cleavage of a signal sequence in !1the endoplasmic reticulum rather than an alternate secretory !1mechanism REFERENCE A65502 !$#authors Wallace, B.A.; Janes, R.W. !$#submission submitted to the Brookhaven Protein Data Bank, September !11994 !$#cross-references PDB:1EDN !$#contents annotation; X-ray crystallography, 2.18 angstroms, residues !153-73 REFERENCE A53485 !$#authors Janes, R.W.; Peapus, D.H.; Wallace, B.A. !$#journal Nat. Struct. Biol. (1994) 1:311-319 !$#title The crystal structure of human endothelin. !$#cross-references MUID:95393150; PMID:7664037 !$#contents annotation; X-ray crystallography, 2.18 angstroms COMMENT Endothelin 1 is a powerful vasocontrictor produced by !1vascular endothelial cells. COMMENT Big endothelin 1 (ET-1) appears to be released by cleavage !1at paired basic residues flanking the sequence. Conversion !1of big ET-1 to mature ET-1 requires cleavage of a Trp-Ile !1bond. GENETICS !$#gene GDB:EDN1 !'##cross-references GDB:119861; OMIM:131240 !$#map_position 6p24.1-6p24.1 !$#introns 22/1; 78/2; 130/2; 178/2 CLASSIFICATION #superfamily endothelin KEYWORDS mitogen; vasoconstrictor FEATURE !$1-17 #domain signal sequence #status experimental #label !8SIG\ !$53-90 #product big endothelin 1 #status experimental #label !8BMAT\ !$53-73 #product endothelin 1 #status experimental #label !8MAT\ !$109-123 #product endothelin homolog #status predicted #label !8HOM\ !$53-67,55-63 #disulfide_bonds #status experimental\ !$109-123,111-119 #disulfide_bonds #status predicted SUMMARY #length 212 #molecular-weight 24425 #checksum 7022 SEQUENCE /// ENTRY S10488 #type complete TITLE endothelin 1 precursor - bovine CONTAINS big endothelin 1; endothelin 1; endothelin homolog ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 21-Nov-1993 #sequence_revision 30-Jan-1998 #text_change 18-Jun-1999 ACCESSIONS S10488; S12728; I46910 REFERENCE S10488 !$#authors Elshourbagy, N.A.; Kmetz, P.; Sathe, G.M. !$#journal Nucleic Acids Res. (1990) 18:4273 !$#title Nucleotide sequence of endothelin cDNA from bovine !1endothelial cells. !$#cross-references MUID:90332445; PMID:2198541 !$#accession S10488 !'##molecule_type mRNA !'##residues 1-131,'A',133-202 ##label ELS !'##cross-references EMBL:X52942; NID:g328; PIDN:CAA37117.1; PID:g329 REFERENCE S12728 !$#authors Price, G.J.; Malone, L. !$#journal Nucleic Acids Res. (1990) 18:3658 !$#title Cloning and sequencing of a bovine preproendothelin cDNA. !$#cross-references MUID:90301503; PMID:2362823 !$#accession S12728 !'##molecule_type mRNA !'##residues 1-202 ##label PRI !'##cross-references EMBL:X52740; NID:g326; PIDN:CAA36954.1; PID:g327 REFERENCE I46910 !$#authors Imai, T.; Hirata, Y.; Emori, T.; Yanagisawa, M.; Masaki, T.; !1Marumo, F. !$#journal Hypertension (1992) 19:753-757 !$#title Induction of endothelin-1 gene by angiotensin and !1vasopressin in endothelial cells. !$#cross-references MUID:92275763; PMID:1592477 !$#accession I46910 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-202 ##label IMA !'##cross-references GB:S37093; NID:g249739; PIDN:AAB22241.1; !1PID:g249740 COMMENT Endothelin 1 is a powerful vasocontrictor produced by !1vascular endothelial cells. CLASSIFICATION #superfamily endothelin KEYWORDS vasoconstrictor FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$53-91 #product big endothelin 1 #status predicted #label !8BMAT\ !$53-73 #product endothelin 1 #status predicted #label MAT\ !$110-124 #product endothelin homolog #status predicted #label !8HOM\ !$53-67,55-63, !$110-124,112-120 #disulfide_bonds #status predicted SUMMARY #length 202 #molecular-weight 22976 #checksum 5505 SEQUENCE /// ENTRY ANPG #type complete TITLE endothelin 1 precursor - pig CONTAINS big endothelin 1; endothelin 1; endothelin-like peptide 1 ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 18-Jun-1999 ACCESSIONS S03159; S18218; A33294; A33398; B33398; A61253; S11474; !1A37784 REFERENCE S03159 !$#authors Yanagisawa, M.; Kurihara, H.; Kimura, S.; Tomobe, Y.; !1Kobayashi, M.; Mitsui, Y.; Yazaki, Y.; Goto, K.; Masaki, T. !$#journal Nature (1988) 332:411-415 !$#title A novel potent vasoconstrictor peptide produced by vascular !1endothelial cells. !$#cross-references MUID:88175065; PMID:2451132 !$#accession S03159 !'##molecule_type mRNA !'##residues 1-203 ##label YAN !'##cross-references EMBL:X07383; NID:g1945; PIDN:CAA30296.1; PID:g1946 !$#accession S18218 !'##molecule_type protein !'##residues 53-73 ##label YA2 REFERENCE A33294 !$#authors Shinmi, O.; Kimura, S.; Yoshizawa, T.; Sawamura, T.; !1Uchiyama, Y.; Sugita, Y.; Kanazawa, I.; Yanagisawa, M.; !1Goto, K.; Masaki, T. !$#journal Biochem. Biophys. Res. Commun. (1989) 162:340-346 !$#title Presence of endothelin-1 in porcine spinal cord: isolation !1and sequence determination. !$#cross-references MUID:89322264; PMID:2665739 !$#accession A33294 !'##molecule_type protein !'##residues 'X',54,'X',56-62,'X',64-66,'X',68-73 ##label SHI !'##experimental_source spinal cord !'##note the authors suggest a possible role as a neuropeptide REFERENCE A33398 !$#authors Sawamura, T.; Kimura, S.; Shinmi, O.; Sugita, Y.; !1Yanagisawa, M.; Masaki, T. !$#journal Biochem. Biophys. Res. Commun. (1989) 162:1287-1294 !$#title Analysis of endothelin related peptides in culture !1supernatant of porcine aortic endothelial cells: evidence !1for biosynthetic pathway of endothelin-1. !$#cross-references MUID:89350944; PMID:2669747 !$#accession A33398 !'##molecule_type protein !'##residues 'X',54,'X',56-62,'X',64-66,'X',68-73 ##label SAW !'##note this sequence represents endothelin 1 !$#accession B33398 !'##molecule_type protein !'##residues 'X',54,'X',56-62,'X',64-66,'X',68-82 ##label SA2 !'##note this sequence represents a fragment of big endothelin 1 REFERENCE A61253 !$#authors Nakagawa, O.; Nakao, K.; Saito, Y.; Shirakami, G.; !1Jougasaki, M.; Mukoyama, M.; Hosoda, K.; Suga, S.; Ogawa, !1Y.; Kishimoto, I.; Komatsu, Y.; Hama, N.; Imura, H. !$#journal J. Cardiovasc. Pharmacol. (1991) 17(Suppl.7):S13-S16 !$#title Isolation and characterization of porcine endothelin-like !1peptide. !$#cross-references MUID:92219667; PMID:1725307 !$#accession A61253 !'##molecule_type protein !'##residues 94-109,'X',111,'X',113,'X',115-117 ##label NAK !'##experimental_source aortic endothelial cell-conditioned medium !'##note it was not determined if this peptide has biological activity REFERENCE A37784 !$#authors Takaoka, M.; Hukumori, Y.; Shiragami, K.; Ikegawa, R.; !1Matsumura, Y.; Morimoto, S. !$#journal Biochem. Biophys. Res. Commun. (1990) 173:1218-1223 !$#title Proteolytic processing of porcine big endothelin-1 catalyzed !1by cathepsin D. !$#cross-references MUID:91097552; PMID:2268325 !$#contents annotation REFERENCE S11474 !$#authors Takaoka, M.; Miyata, Y.; Takenobu, Y.; Ikegawa, R.; !1Matsumura, Y.; Morimoto, S. !$#journal Biochem. J. (1990) 270:541-544 !$#title Mode of cleavage of pig big endothelin-1 by chymotrypsin. !1Production and degradation of mature endothelin-1. !$#cross-references MUID:90380057; PMID:2205205 !$#accession S11474 !'##status preliminary !'##molecule_type protein !'##residues 'X',54,'X',56-62,'X',64-66,'X',68-83 ##label TAK CLASSIFICATION #superfamily endothelin KEYWORDS duplication; glycoprotein; vasoconstrictor FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$53-91 #product big endothelin 1 #status experimental #label !8BMAT\ !$53-73 #product endothelin 1 #status experimental #label !8MAT\ !$94-118 #product endothelin 1-related peptide #status !8experimental #label E1R\ !$110-124 #product endothelin homolog #status predicted #label !8HOM\ !$53-67,55-63 #disulfide_bonds #status experimental\ !$110-124,112-120 #disulfide_bonds #status predicted\ !$200 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 203 #molecular-weight 23259 #checksum 7898 SEQUENCE /// ENTRY S63538 #type complete TITLE endothelin 1 precursor - mouse ALTERNATE_NAMES preproendothelin 1 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 28-Oct-1996 #sequence_revision 13-Mar-1997 #text_change 18-Jun-1999 ACCESSIONS S63538; B36503; I51896; I49006 REFERENCE S63538 !$#authors Chan, T.S.K.; Lin, C.X.F.; Chan, W.Y.; Chung, S.S.M.; Chung, !1S.K. !$#journal Eur. J. Biochem. (1995) 234:819-826 !$#title Mouse preproendothelin-1 gene. cDNA cloning, sequence !1analysis and determination of sites of expression during !1embryonic development. !$#cross-references MUID:96163465; PMID:8575440 !$#accession S63538 !'##molecule_type mRNA !'##residues 1-202 ##label CHA !'##cross-references EMBL:U35233; NID:g1244501; PIDN:AAA97608.1; !1PID:g1244502 !'##experimental_source adult lung REFERENCE A36503 !$#authors Saida, K.; Mitsui, Y.; Ishida, N. !$#journal J. Biol. Chem. (1989) 264:14613-14616 !$#title A novel peptide, vasoactive intestinal contractor, of a new !1(endothelin) peptide family. Molecular cloning, expression, !1and biological activity. !$#cross-references MUID:89359247; PMID:2768235 !$#accession B36503 !'##molecule_type DNA !'##residues 48-77 ##label SAI !'##cross-references GB:M26497; NID:g193182 REFERENCE I51896 !$#authors Chen, M.; Todd-Turla, K.; Wang, W.H.; Cao, X.; Smart, A.; !1Brosius, F.C.; Killen, P.D.; Keiser, J.A.; Briggs, J.P.; !1Schnermann, J. !$#journal Am. J. Physiol. (1993) 265:F542-F550 !$#title Endothelin-1 mRNA in glomerular and epithelial cells of !1kidney. !$#cross-references MUID:94056808; PMID:8238383 !$#accession I51896 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 36-61,'X',63-76 ##label CHE !'##cross-references GB:S66650; NID:g435851 REFERENCE I49006 !$#authors Harats, D.; Kurihara, H.; Belloni, P.; Oakley, H.; Ziober, !1A.; Ackley, D.; Cain, G.; Kurihara, Y.; Lawn, R.; Sigal, E. !$#journal J. Clin. Invest. (1995) 95:1335-1344 !$#title Targeting gene expression to the vascular wall in transgenic !1mice using the murine preproendothelin-1 promoter. !$#cross-references MUID:95190032; PMID:7883980 !$#accession I49006 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-21,'GRRHLRIFLLQRSSYRFCFPLFFLSFLSFFPFYLFF' ##label HAR !'##cross-references EMBL:U07982; NID:g560542; PIDN:AAA74439.1; !1PID:g560543 !'##note the sequence in GenBank entry MMU07982, release 92.00, !1PID:g560543, includes conceptual translation of a portion of !1the first exon CLASSIFICATION #superfamily endothelin KEYWORDS vasoconstrictor FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$53-91 #product big endothelin 1 #status predicted #label !8BMAT\ !$53-73 #product endothelin 1 #status predicted #label MAT\ !$53-67,55-63, !$110-124,112-120 #disulfide_bonds #status predicted SUMMARY #length 202 #molecular-weight 22809 #checksum 8849 SEQUENCE /// ENTRY JN0125 #type complete TITLE endothelin 1 precursor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 05-Mar-1993 #sequence_revision 05-Mar-1993 #text_change 18-Jun-1999 ACCESSIONS JN0125; S15421 REFERENCE JN0125 !$#authors Sakurai, T.; Yanagisawa, M.; Inoue, A.; Ryan, U.S.; Kimura, !1S.; Mitsui, Y.; Goto, K.; Masaki, T. !$#journal Biochem. Biophys. Res. Commun. (1991) 175:44-47 !$#title cDNA cloning, sequence analysis and tissue distribution of !1rat preproendothelin-1 mRNA. !$#cross-references MUID:91151375; PMID:1840483 !$#accession JN0125 !'##molecule_type mRNA !'##residues 1-202 ##label SAK !'##cross-references GB:M64711; NID:g204067; PIDN:AAA41129.1; !1PID:g204068 REFERENCE S15421 !$#authors Nunez, D.J.R.; Taylor, E.A.; Oh, V.M.S.; Schofield, J.P.; !1Brown, M.J. !$#journal Biochem. J. (1991) 275:817-819 !$#title Endothelin-1 mRNA expression in the rat kidney. !$#cross-references MUID:91248125; PMID:2039460 !$#accession S15421 !'##molecule_type mRNA !'##residues 53-73 ##label NUN CLASSIFICATION #superfamily endothelin KEYWORDS vasoconstrictor FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$53-91 #product big endothelin 1 #status predicted #label !8BEN\ !$53-73 #product endothelin 1 #status predicted #label MAT\ !$53-67,55-63, !$110-124,112-120 #disulfide_bonds #status predicted SUMMARY #length 202 #molecular-weight 23135 #checksum 9363 SEQUENCE /// ENTRY A34378 #type complete TITLE endothelin 3 precursor - human CONTAINS big endothelin 3; endothelin 3; endothelin homolog ORGANISM #formal_name Homo sapiens #common_name man DATE 08-Jun-1990 #sequence_revision 26-May-1994 #text_change 18-Jun-1999 ACCESSIONS A34378; S08262 REFERENCE A34378 !$#authors Bloch, K.D.; Eddy, R.L.; Shows, T.B.; Quertermous, T. !$#journal J. Biol. Chem. (1989) 264:18156-18161 !$#title cDNA cloning and chromosomal assignment of the gene encoding !1endothelin 3. !$#cross-references MUID:90036893; PMID:2509452 !$#accession A34378 !'##molecule_type mRNA !'##residues 1-238 ##label BLO !'##cross-references GB:J05081; NID:g182248; PIDN:AAA52405.1; !1PID:g182249 !'##experimental_source hypothalamus REFERENCE S08262 !$#authors Onda, H.; Ohkubo, S.; Ogi, K.; Kosaka, T.; Kimura, C.; !1Matsumoto, H.; Suzuki, N.; Fujino, M. !$#journal FEBS Lett. (1990) 261:327-330 !$#title One of the endothelin gene family, endothelin 3 gene, is !1expressed in the placenta. !$#cross-references MUID:90184472; PMID:2178974 !$#accession S08262 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-180,'RQ',197-238 ##label OND !'##cross-references GB:X52001; NID:g31260; PIDN:CAA36252.1; PID:g31261 !'##experimental_source placenta GENETICS !$#gene GDB:EDN3 !'##cross-references GDB:119862; OMIM:131242 !$#map_position 20q13.2-20q13.3 CLASSIFICATION #superfamily endothelin KEYWORDS vasoconstrictor FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$97-138 #product big endothelin 3 #status predicted #label !8BMAT\ !$97-117 #product endothelin 3 #status predicted #label MAT\ !$159-179 #product endothelin homolog #status predicted #label !8HOM\ !$97-111,99-107, !$159-173,161-169 #disulfide_bonds #status predicted SUMMARY #length 238 #molecular-weight 25454 #checksum 2435 SEQUENCE /// ENTRY JC1102 #type complete TITLE endothelin 3 precursor - rat CONTAINS big endothelin 3; endothelin 3; endothelin homolog ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 09-Oct-1992 #sequence_revision 26-May-1994 #text_change 18-Jun-1999 ACCESSIONS JC1102; A31407 REFERENCE JC1102 !$#authors Shiba, R.; Sakurai, T.; Yamada, G.; Morimoto, H.; Saito, A.; !1Masaki, T.; Goto, K. !$#journal Biochem. Biophys. Res. Commun. (1992) 186:588-594 !$#title Cloning and expression of rat preproendothelin-3 cDNA. !$#cross-references MUID:92337657; PMID:1378731 !$#accession JC1102 !'##molecule_type mRNA !'##residues 1-167 ##label SHI !'##cross-references GB:S39779; NID:g251280; PIDN:AAB22502.1; !1PID:g251281 REFERENCE A31407 !$#authors Yanagisawa, M.; Inoue, A.; Ishikawa, T.; Kasuya, Y.; Kimura, !1S.; Kumagaye, S.I.; Nakajima, K.; Watanabe, T.X.; !1Sakakibara, S.; Goto, K.; Masaki, T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:6964-6967 !$#title Primary structure, synthesis, and biological activity of rat !1endothelin, an endothelium-derived vasoconstrictor peptide. !$#cross-references MUID:88320556; PMID:3045827 !$#accession A31407 !'##molecule_type DNA !'##residues 48-77 ##label YAN CLASSIFICATION #superfamily endothelin KEYWORDS vasoconstrictor FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-52 #domain propeptide #status predicted #label PRO\ !$53-94 #product big endothelin 3 #status predicted #label !8BET\ !$53-73 #product endothelin 3 #status predicted #label MAT\ !$115-135 #product endothelin homolog #status predicted #label !8HOM\ !$53-67,55-63, !$115-129,117-125 #disulfide_bonds #status predicted SUMMARY #length 167 #molecular-weight 18453 #checksum 5428 SEQUENCE /// ENTRY A39070 #type complete TITLE endothelin 2 precursor - human CONTAINS big endothelin 2; endothelin 2; endothelin homolog ORGANISM #formal_name Homo sapiens #common_name man DATE 20-Mar-1992 #sequence_revision 26-May-1994 #text_change 18-Jun-1999 ACCESSIONS A39070; S12912; A61252; B32111 REFERENCE A39070 !$#authors Bloch, K.D.; Hong, C.C.; Eddy, R.L.; Shows, T.B.; !1Quertermous, T. !$#journal Genomics (1991) 10:236-242 !$#title cDNA cloning and chromosomal assignment of the endothelin 2 !1gene: vasoactive intestinal contractor peptide is rat !1endothelin 2. !$#cross-references MUID:91257834; PMID:1840558 !$#accession A39070 !'##molecule_type mRNA !'##residues 1-178 ##label BLO !'##cross-references GB:M65200 REFERENCE S12912 !$#authors Ohkubo, S.; Ogi, K.; Hosoya, M.; Matsumoto, H.; Suzuki, N.; !1Kimura, C.; Onda, H.; Fujino, M. !$#journal FEBS Lett. (1990) 274:136-140 !$#title Specific expression of human endothelin-2 (ET-2) gene in a !1renal adenocarcinoma cell line. Molecular cloning of cDNA !1encoding the precursor of ET-2 and its characterization. !$#cross-references MUID:91071415; PMID:1701397 !$#accession S12912 !'##molecule_type mRNA !'##residues 1-178 ##label OHK !'##cross-references GB:X55177; NID:g31258; PIDN:CAA38962.1; PID:g31259 REFERENCE A61252 !$#authors Onda, H.; Ohkubo, S.; Kosaka, T.; Yasuhara, T.; Ogi, K.; !1Hosoya, M.; Matsumoto, H.; Suzuki, N.; Kitada, C.; !1Ishibashi, Y.; Kimura, C.; Kubo, K.; Fujino, M. !$#journal J. Cardiovasc. Pharmacol. (1991) 17(Suppl.7):S39-S43 !$#title Expression of endothelin-2 (ET-2) gene in a human renal !1adenocarcinoma cell line: purification and cDNA cloning of !1ET-2. !$#cross-references MUID:92219747; PMID:1725387 !$#accession A61252 !'##molecule_type mRNA !'##residues 1-178 ##label OND REFERENCE A32111 !$#authors Inoue, A.; Yanagisawa, M.; Kimura, S.; Kasuya, Y.; Miyauchi, !1T.; Goto, K.; Masaki, T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:2863-2867 !$#title The human endothelin family: three structurally and !1pharmacologically distinct isopeptides predicted by three !1separate genes. !$#cross-references MUID:89202426; PMID:2649896 !$#accession B32111 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 23-73 ##label INO !'##cross-references GB:M25550; GB:J04522; NID:g556204; PIDN:AAA52340.1; !1PID:g556205 GENETICS !$#gene GDB:EDN2 !'##cross-references GDB:125241; OMIM:131241 !$#map_position 1p34-1p34 CLASSIFICATION #superfamily endothelin KEYWORDS vasoconstrictor FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$49-85 #product big endothelin 2 #status predicted #label !8BMAT\ !$49-69 #product endothelin 2 #status predicted #label MAT\ !$96-110 #product endothelin homolog #status predicted #label !8HOM\ !$49-63,51-59,96-110, !$98-106 #disulfide_bonds #status predicted SUMMARY #length 178 #molecular-weight 19960 #checksum 2210 SEQUENCE /// ENTRY S17194 #type complete TITLE endothelin 2 precursor - mouse ALTERNATE_NAMES vasoactive intestinal contractor ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S17194; A36503 REFERENCE S17194 !$#authors Saida, K.; Mitsui, Y. !$#journal Biochim. Biophys. Acta (1991) 1089:404-406 !$#title cDNA cloning, sequence analysis and tissue distribution of a !1precursor for vasoactive intestinal contractor (VIC). !$#cross-references MUID:91316145; PMID:1859843 !$#accession S17194 !'##status preliminary !'##molecule_type mRNA !'##residues 1-160 ##label SAI !'##cross-references EMBL:X59556; NID:g55288; PIDN:CAA42155.1; !1PID:g55289 REFERENCE A36503 !$#authors Saida, K.; Mitsui, Y.; Ishida, N. !$#journal J. Biol. Chem. (1989) 264:14613-14616 !$#title A novel peptide, vasoactive intestinal contractor, of a new !1(endothelin) peptide family. Molecular cloning, expression, !1and biological activity. !$#cross-references MUID:89359247; PMID:2768235 !$#accession A36503 !'##status preliminary !'##molecule_type DNA !'##residues 41-70 ##label SA2 !'##cross-references GB:M26498 CLASSIFICATION #superfamily endothelin KEYWORDS intestine; neuropeptide SUMMARY #length 160 #molecular-weight 17637 #checksum 2878 SEQUENCE /// ENTRY A61339 #type complete TITLE vespulakinin 1 - eastern yellowjacket CONTAINS vespulakinin 2 ORGANISM #formal_name Vespula maculifrons #common_name eastern yellowjacket DATE 17-Jul-1994 #sequence_revision 07-Oct-1994 #text_change 07-May-1999 ACCESSIONS A61339 REFERENCE A61339 !$#authors Yoshida, H.; Geller, R.G.; Pisano, J.J. !$#journal Biochemistry (1976) 15:61-64 !$#title Vespulakinins: new carbohydrate-containing bradykinin !1derivatives. !$#cross-references MUID:76114777; PMID:1247511 !$#accession A61339 !'##molecule_type protein !'##residues 1-17 ##label YOS CLASSIFICATION #superfamily vespulakinin KEYWORDS antihypertensive; bradykinin; glycoprotein; venom FEATURE !$1-17 #product vespulakinin 1 #status experimental #label !8MAT1\ !$3-17 #product vespulakinin 2 #status experimental #label !8MAT2\ !$9-17 #region bradykinin-like\ !$3,4 #binding_site carbohydrate (Thr) (covalent) #status !8experimental SUMMARY #length 17 #molecular-weight 1960 #checksum 1902 SEQUENCE /// ENTRY XAVI9B #type complete TITLE angiotensin-converting enzyme inhibitor V-9 - jararaca ORGANISM #formal_name Bothrops jararaca #common_name jararaca DATE 13-Jul-1981 #sequence_revision 13-Jul-1981 #text_change 08-Dec-1995 ACCESSIONS A01253 REFERENCE A90356 !$#authors Ondetti, M.A.; Williams, N.J.; Sabo, E.F.; Pluscec, J.; !1Weaver, E.R.; Kocy, O. !$#journal Biochemistry (1971) 10:4033-4039 !$#title Angiotensin-converting enzyme inhibitors from the venom of !1Bothrops jararaca. Isolation, elucidation of structure, and !1synthesis. !$#cross-references MUID:72118526; PMID:4334402 !$#accession A01253 !'##molecule_type protein !'##residues 1-13 ##label OND !'##note the structure of the peptide was confirmed by synthesis COMMENT This peptide also potentiates bradykinin by inhibiting the !1kinases that inactivate it. CLASSIFICATION #superfamily bradykinin-potentiating peptide KEYWORDS angiotensin-converting enzyme inhibitor; pyroglutamic acid FEATURE !$1 #modified_site pyrrolidone carboxylic acid (Gln) !8#status experimental SUMMARY #length 13 #molecular-weight 1388 #checksum 7017 SEQUENCE /// ENTRY XAVIBH #type complete TITLE bradykinin-potentiating peptide - halys viper ALTERNATE_NAMES BPP ORGANISM #formal_name Agkistrodon halys #common_name halys viper DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 05-Aug-1994 ACCESSIONS JC0002 REFERENCE JC0002 !$#authors Chi, C.W.; Wang, S.Z.; Xu, L.G.; Wang, M.Y.; Lo, S.S.; !1Huang, W.D. !$#journal Peptides (1985) 6:339-342 !$#title Structure-function studies on the bradykinin potentiating !1peptide from Chinese snake venom (Agkistrodon halys Pallas). !$#cross-references MUID:86177022; PMID:3008123 !$#accession JC0002 !'##molecule_type protein !'##residues 1-11 ##label CHI COMMENT Because this peptide both inhibits the activity of the !1angiotensin-converting enzyme and enhances the action of !1bradykinin, it is an antihypertensive agent. CLASSIFICATION #superfamily bradykinin-potentiating peptide KEYWORDS angiotensin-converting enzyme inhibitor; antihypertensive; !1bradykinin; pyroglutamic acid; venom FEATURE !$1 #modified_site pyrrolidone carboxylic acid (Gln) !8#status experimental SUMMARY #length 11 #molecular-weight 1112 #checksum 5152 SEQUENCE /// ENTRY XASNBA #type complete TITLE bradykinin-potentiating peptide B - mamushi ORGANISM #formal_name Agkistrodon blomhoffi #common_name mamushi DATE 13-Jul-1981 #sequence_revision 13-Jul-1981 #text_change 08-Dec-1995 ACCESSIONS A01254 REFERENCE A01254 !$#authors Kato, H.; Suzuki, T. !$#journal Proc. Jpn. Acad. (1970) 46:176-181 !$#accession A01254 !'##molecule_type protein !'##residues 1-11 ##label KAT !'##note the sequence of the natural peptide was confirmed by the !1synthesis and analysis of a peptide having the identical !1structure and biological properties CLASSIFICATION #superfamily bradykinin-potentiating peptide KEYWORDS angiotensin-converting enzyme inhibitor; bradykinin; !1pyroglutamic acid; venom FEATURE !$1 #modified_site pyrrolidone carboxylic acid (Gln) !8#status experimental SUMMARY #length 11 #molecular-weight 1199 #checksum 5160 SEQUENCE /// ENTRY XAVI6B #type complete TITLE angiotensin-converting enzyme inhibitor V-6-II - jararaca ORGANISM #formal_name Bothrops jararaca #common_name jararaca DATE 13-Jul-1981 #sequence_revision 13-Jul-1981 #text_change 08-Dec-1995 ACCESSIONS A01255 REFERENCE A90356 !$#authors Ondetti, M.A.; Williams, N.J.; Sabo, E.F.; Pluscec, J.; !1Weaver, E.R.; Kocy, O. !$#journal Biochemistry (1971) 10:4033-4039 !$#title Angiotensin-converting enzyme inhibitors from the venom of !1Bothrops jararaca. Isolation, elucidation of structure, and !1synthesis. !$#cross-references MUID:72118526; PMID:4334402 !$#accession A01255 !'##molecule_type protein !'##residues 1-10 ##label OND !'##note the structure of the peptide was confirmed by synthesis COMMENT This peptide also potentiates bradykinin by inhibiting the !1kinases that inactivate it. CLASSIFICATION #superfamily bradykinin-potentiating peptide KEYWORDS angiotensin-converting enzyme inhibitor; pyroglutamic acid FEATURE !$1 #modified_site pyrrolidone carboxylic acid (Gln) !8#status experimental SUMMARY #length 10 #molecular-weight 1232 #checksum 4379 SEQUENCE /// ENTRY XASNPC #type complete TITLE angiotensin-converting enzyme inhibitor - aspic viper ORGANISM #formal_name Vipera aspis #common_name aspic viper DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 08-Dec-1995 ACCESSIONS A60377 REFERENCE A60377 !$#authors Komori, Y.; Sugihara, H. !$#journal Int. J. Biochem. (1990) 22:767-771 !$#title Characterization of a new inhibitor for angiotensin !1converting enzyme from the venom of Vipera aspis aspis. !$#cross-references MUID:90382616; PMID:2169439 !$#accession A60377 !'##molecule_type protein !'##residues 1-10 ##label KOM CLASSIFICATION #superfamily bradykinin-potentiating peptide KEYWORDS angiotensin-converting enzyme inhibitor; pyroglutamic acid FEATURE !$1 #modified_site pyrrolidone carboxylic acid (Gln) !8#status experimental SUMMARY #length 10 #molecular-weight 1062 #checksum 4372 SEQUENCE /// ENTRY MAHU #type complete TITLE alpha-2-macroglobulin precursor [validated] - human ALTERNATE_NAMES alpha-2M ORGANISM #formal_name Homo sapiens #common_name man DATE 05-Apr-1983 #sequence_revision 30-Jun-1987 #text_change 08-Dec-2000 ACCESSIONS A94033; I39375; S09107; JN0262; A92486; S66634; A01256 REFERENCE A94033 !$#authors Kan, C.C.; Solomon, E.; Belt, K.T.; Chain, A.C.; Hiorns, !1L.R.; Fey, G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:2282-2286 !$#title Nucleotide sequence of cDNA encoding human !1alpha-2-macroglobulin and assignment of the chromosomal !1locus. !$#cross-references MUID:85190481; PMID:2581245 !$#accession A94033 !'##molecule_type mRNA !'##residues 1-1474 ##label KAN !'##cross-references GB:M11313; NID:g177869; PIDN:AAA51551.1; !1PID:g177870 !'##note hydrolysis of the thiolester bond during amino acid sequencing !1of the mature protein converts 975-Gln into 975-Glu. !1Differences in amino acid composition at position 1000 may !1be due to DNA polymorphism REFERENCE I39375 !$#authors Bell, G.I.; Rall, L.B.; Sanchez-Pescador, R.; Merryweather, !1J.P.; Scott, J.; Eddy, R.L.; Shows, T.B. !$#journal Somat. Cell Mol. Genet. (1985) 11:285-289 !$#title Human alpha 2-macroglobulin gene is located on chromosome !112. !$#cross-references MUID:85219061; PMID:2408344 !$#accession I39375 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 832-999,'I',1001-1147,'D',1149-1194,'D',1196-1474 ##label !1BEL !'##cross-references GB:M36501; NID:g177871; PIDN:AAA51552.1; !1PID:g177872 REFERENCE S09106 !$#authors Marynen, P.; Devriendt, K.; van den Berghe, H.; Cassiman, !1J.J. !$#journal FEBS Lett. (1990) 262:349-352 !$#title A genetic polymorphism in a functional domain of human !1pregnancy zone protein: the bait region. Genomic structure !1of the bait domains of human pregnancy zone protein and !1alpha-2 macroglobulin. !$#cross-references MUID:90242963; PMID:1692292 !$#accession S09107 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 672-747 ##label MAR REFERENCE JN0262 !$#authors Matthijs, G.; Devriendt, K.; Cassiman, J.J.; Van Den Berghe, !1H.; Marynen, P. !$#journal Biochem. Biophys. Res. Commun. (1992) 184:596-603 !$#title Structure of the human alpha-2 macroglobulin gene and its !1promotor. !$#cross-references MUID:92246939; PMID:1374237 !$#accession JN0262 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-29 ##label MAT REFERENCE A92486 !$#authors Sottrup-Jensen, L.; Stepanik, T.M.; Kristensen, T.; !1Wierzbicki, D.M.; Jones, C.M.; Lonblad, P.B.; Magnusson, S.; !1Petersen, T.E. !$#journal J. Biol. Chem. (1984) 259:8318-8327 !$#title Primary structure of human alpha-2-macroglobulin. V. The !1complete structure. !$#cross-references MUID:84239807; PMID:6203908 !$#accession A92486 !'##molecule_type protein !'##residues 24-562,'E',564-974,'Z',976-999,'I',1001-1474 ##label SOT REFERENCE A92529 !$#authors Sottrup-Jensen, L.; Stepanik, T.M.; Kristensen, T.; !1Wierzbicki, D.M.; Jones, C.M.; Lonblad, P.B.; Magnusson, S.; !1Petersen, T.E. !$#journal J. Biol. Chem. (1985) 260:6500 !$#contents annotation; erratum REFERENCE A91713 !$#authors Virca, G.D.; Salvesen, G.S.; Travis, J. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1983) 364:1297-1302 !$#title Human neutrophil elastase and cathepsin G cleavage sites in !1the bait region of alpha-2-macroglobulin. Proposed !1structural limits of the bait region. !$#cross-references MUID:84030513; PMID:6195065 !$#contents annotation; inhibitory site REFERENCE A91290 !$#authors Sottrup-Jensen, L.; Lonblad, P.B.; Stepanik, T.M.; Petersen, !1T.E.; Magnusson, S.; Jornvall, H. !$#journal FEBS Lett. (1981) 127:167-173 !$#title Primary structure of the 'bait' region for proteinases in !1alpha-2-macroglobulin. Nature of the complex. !$#cross-references MUID:81212827; PMID:6165619 !$#contents annotation; inhibitory site REFERENCE A90099 !$#authors Hall, P.K.; Nelles, L.P.; Travis, J.; Roberts, R.C. !$#journal Biochem. Biophys. Res. Commun. (1981) 100:8-16 !$#title Proteolytic cleavage sites on alpha-2-macroglobulin !1resulting in proteinase binding are different for trypsin !1and Staphylococcus aureus V-8 proteinase. !$#cross-references MUID:81255805; PMID:6167263 !$#contents annotation; inhibitory site REFERENCE A91299 !$#authors Mortensen, S.B.; Sottrup-Jensen, L.; Hansen, H.F.; Petersen, !1T.E.; Magnusson, S. !$#journal FEBS Lett. (1981) 135:295-300 !$#title Primary and secondary cleavage sites in the bait region of !1alpha-2-macroglobulin. !$#cross-references MUID:82095610; PMID:6172288 !$#contents annotation; inhibitory site REFERENCE S66634 !$#authors Dolmer, K.; Jenner, L.B.; Jacobsen, L.; Andersen, G.R.; !1Koch, T.J.; Thirup, S.; Sottrup-Jensen, L.; Nyborg, J. !$#journal FEBS Lett. (1995) 372:93-95 !$#title Crystallisation and preliminary X-ray analysis of the !1receptor-binding domain of human and bovine alpha !1(2)-macroglobulin. !$#cross-references MUID:96032553; PMID:7556651 !$#accession S66634 !'##molecule_type protein !'##residues 1337-1343 ##label DOL COMMENT This inhibitor is able to inhibit all four classes (EC !13.4.21-3.4.24) of endopeptidases by a unique "trapping" !1mechanism. Enzymatic cleavage within the inhibitor's "bait !1region" changes its tertiary conformation, entrapping the !1proteinase. This results in hydrolysis of its thiolester !1bond which, although not necessary for inhibition, allows !1covalent bonding between inhibitor and enzyme and appears to !1unmask a receptor-specific binding site. COMMENT The entrapped enzyme remains active against low molecular !1weight substrates (activity against high molecular weight !1substrates is greatly reduced), but formation of the !1proteinase-inhibitor complex results in its rapid clearance !1from the circulation by receptor-mediated endocytosis. COMMENT The wide specificity of this inhibitor is attributed to the !1primary sequence of its "bait region." It contains three !1separate clusters of peptide bonds that, meeting the !1substrate specificities of a variety of plasma proteinases, !1form primary (residues 704-809) and secondary endopeptidase !1cleavage sites. GENETICS !$#gene GDB:A2M !'##cross-references GDB:119639; OMIM:103950 !$#map_position 12p13.3-12p12.3 COMPLEX homotetramer; dimer of disulfide linked dimers CLASSIFICATION #superfamily alpha-2-macroglobulin KEYWORDS glycoprotein; plasma; proteinase inhibitor; thiolester bond FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-1474 #product alpha-2-macroglobin #status experimental !8#label MA2\ !$693-694,704-709, !$719-723,730-735 #region inhibitory #status predicted\ !$698-742 #region bait region\ !$48-86,251-299, !$269-287,278-431, !$595-771,642-689, !$821-849,847-883, !$921-1321,1079-1127, !$1352-1467 #disulfide_bonds #status experimental\ !$55,70,247,396,410, !$869,991,1424 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$470,563 #disulfide_bonds interchain #status predicted\ !$972-975 #cross-link thiolester (Cys-Gln) #status experimental SUMMARY #length 1474 #molecular-weight 163277 #checksum 245 SEQUENCE /// ENTRY C3HU #type complete TITLE complement C3 precursor [validated] - human CONTAINS alternative-complement-pathway C3/C5 convertase (EC 3.4.21.47) C3b subunit; C3a anaphylatoxin ORGANISM #formal_name Homo sapiens #common_name man DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 08-Dec-2000 ACCESSIONS A94065; A37999; A92187; A27603; A23435; A45830; B45830; !1A01257; A01258 REFERENCE A94065 !$#authors de Bruijn, M.H.L.; Fey, G.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:708-712 !$#title Human complement component C3: cDNA coding sequence and !1derived primary structure. !$#cross-references MUID:85140166; PMID:2579379 !$#accession A94065 !'##molecule_type mRNA !'##residues 1-1663 ##label DEB !'##cross-references GB:K02765; NID:g179664; PIDN:AAA85332.1; !1PID:g179665 REFERENCE A37999 !$#authors Vik, D.P.; Amiguet, P.; Moffat, G.J.; Fey, M.; !1Amiguet-Barras, F.; Wetsel, R.A.; Tack, B.F. !$#journal Biochemistry (1991) 30:1080-1085 !$#title Structural features of the human C3 gene: intron/exon !1organization, transcriptional start site, and promoter !1region sequence. !$#cross-references MUID:91113687; PMID:1703437 !$#contents intron/exon structure of gene !$#accession A37999 !'##molecule_type DNA !'##residues 1-25 ##label VIK !'##cross-references GB:M63423 !'##note the authors translated the codon GGT for residue 6 as Leu, CCC !1for residue 7 as Leu, and AGC for residue 8 as Leu REFERENCE A92187 !$#authors Hugli, T.E. !$#journal J. Biol. Chem. (1975) 250:8293-8301 !$#title Human anaphylatoxin (C3a) from the third component of !1complement. !$#cross-references MUID:76069169; PMID:1238393 !$#accession A92187 !'##molecule_type protein !'##residues 672-680,'N',682-699,'Q',701-748 ##label HUG REFERENCE A27603 !$#authors Daoudaki, M.E.; Becherer, J.D.; Lambris, J.D. !$#journal J. Immunol. (1988) 140:1577-1580 !$#title A 34-amino acid peptide of the third component of complement !1mediates properdin binding. !$#cross-references MUID:88154452; PMID:3279119 !$#accession A27603 !'##molecule_type protein !'##residues 1409-1563 ##label DAO REFERENCE A23435 !$#authors Hellman, U.; Eggertsen, G.; Engstrom, A.; Sjoquist, J. !$#journal Biochem. J. (1985) 230:353-361 !$#title Amino acid sequence of the trypsin-generated C3d fragment !1from human complement factor C3. !$#cross-references MUID:86025442; PMID:3876831 !$#accession A23435 !'##molecule_type protein !'##residues 1002-1012,'E',1014-1303 ##label HEL !'##note sequence corresponding to residues 1072-1100 was not determined !1but was taken from de Bruijn & Fey (reference A94605) REFERENCE A45830 !$#authors Poznansky, M.C.; Clissold, P.M.; Lachmann, P.J. !$#journal J. Immunol. (1989) 143:1254-1258 !$#title The difference between human C3F and C3S results from a !1single amino acid change from an asparagine to an aspartate !1residue at position 1216 on the alpha-chain of the !1complement component, C3. !$#cross-references MUID:89309808; PMID:2473125 !$#accession A45830 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1212-1215,'N',1217-1223 ##label POZ !'##note this is the C3S allele !$#accession B45830 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1212-1223 ##label PO2 REFERENCE S27041 !$#authors Dolmer, K.; Sottrup-Jensen, L. !$#journal FEBS Lett. (1993) 315:85-90 !$#title Disulfide bridges in human complement component C3b. !$#cross-references MUID:93106233; PMID:8416818 !$#contents annotation; disulfide bonds COMMENT The sequence shown is the C3 fast (C3F) allele, which is !1found mainly in Caucasian populations and is associated with !1increased incidence of certain diseases. COMMENT Complement C3 contains two chains, formed by removal of four !1residues and linked by a disulfide bond. Its activation by a !1C3 convertase, which is the central reaction in both !1classical and alternative complement pathways, releases the !1C3a anaphylatoxin from the amino end of the alpha chain and !1generates C3b, which associates with the Bb fragment of !1complement factor B to form the !1alternative-complement-pathway C3/C5 convertase. COMMENT C3a anaphylatoxin is a vasoactive peptide and a mediator of !1inflammation. COMMENT C3b, with its highly reactive thiol group, binds to the !1surface of foreign particles and facilitates phagocytosis. !1It binds to complement C5 and renders it susceptible to !1proteolysis by the classical-complement-pathway C3/C5 !1convertase. The activity of C3b is regulated by proteolytic !1cleavage involving factors H and I. Its degradation products !1can also be biologically active. COMMENT The major site of synthesis of this plasma protein is the !1liver. GENETICS !$#gene GDB:C3 !'##cross-references GDB:119044; OMIM:120700 !$#map_position 19p13.3-19p13.3 !$#note contains 41 exons CLASSIFICATION #superfamily alpha-2-macroglobulin KEYWORDS acute phase; complement alternate pathway; complement !1pathway; glycoprotein; hydrolase; immune response; !1inflammation; plasma; serine proteinase; thiolester bond FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-667 #product complement C3 and C3b beta chain #status !8predicted #label C3BB\ !$23-667,672-1663 #product complement C3 #status predicted #label CC3\ !$23-667,749-1663 #product C3b #status predicted #label C3B\ !$672-1663 #product complement C3 alpha chain #status predicted !8#label CC3A\ !$672-748 #product C3a anaphylatoxin #status predicted #label !8C3T\ !$749-1663 #product C3b alpha' chain #status predicted #label !8C3BA\ !$946-1303 #product C3dk fragment #status predicted #label CDK\ !$955-1303 #product C3dg fragment #status predicted #label CDG\ !$955-1001 #product C3g fragment #status predicted #label C3G\ !$1002-1303 #product C3d fragment #status experimental #label !8C3D\ !$1424-1457 #region properdin binding\ !$85,939 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$559-816,627-662, !$693-720,694-727, !$707-728,873-1513, !$1101-1158, !$1358-1489, !$1389-1458, !$1506-1511, !$1518-1590, !$1537-1661,1637-1646 #disulfide_bonds #status experimental\ !$748-749 #cleavage_site Arg-Ser (C3 convertase) #status !8predicted\ !$954-955 #cleavage_site Arg-Glu (complement factor I) #status !8predicted\ !$1010-1013 #cross-link thiolester (Cys-Gln) #status !8experimental\ !$1303-1304 #cleavage_site Arg-Ser (complement factor I) #status !8predicted\ !$1320-1321 #cleavage_site Arg-Ser (complement factor I) #status !8predicted\ !$1617 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1663 #molecular-weight 187163 #checksum 38 SEQUENCE /// ENTRY C3MS #type complete TITLE complement C3 precursor - mouse CONTAINS alternative-complement-pathway C3/C5 convertase (EC 3.4.21.47) C3b subunit; C3a anaphylatoxin ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 18-Jun-1999 ACCESSIONS A92459; B92459; A92460; A93938; A21898; A54561; S16369; !1S16189; I49563; I49576; A01261; A05290; A29033 REFERENCE A92459 !$#authors Lundwall, A.; Wetsel, R.A.; Domdey, H.; Tack, B.F.; Fey, !1G.H. !$#journal J. Biol. Chem. (1984) 259:13851-13856 !$#title Structure of murine complement component C3: I. Nucleotide !1sequence of cloned complementary and genomic DNA coding for !1the beta chain. !$#cross-references MUID:85054818; PMID:6548745 !$#accession A92459 !'##molecule_type mRNA !'##residues 1-724 ##label LU1 !$#accession B92459 !'##molecule_type DNA !'##residues 1-124 ##label LU2 REFERENCE A92460 !$#authors Wetsel, R.A.; Lundwall, A.; Davidson, F.; Gibson, T.; Tack, !1B.F.; Fey, G.H. !$#journal J. Biol. Chem. (1984) 259:13857-13862 !$#title Structure of murine complement component C3: II. Nucleotide !1sequence of cloned complementary DNA coding for the alpha !1chain. !$#cross-references MUID:85054819; PMID:6094532 !$#accession A92460 !'##molecule_type mRNA !'##residues 671-1663 ##label WET REFERENCE A93938 !$#authors Domdey, H.; Wiebauer, K.; Kazmaier, M.; Muller, V.; Odink, !1K.; Fey, G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:7619-7623 !$#title Characterization of the mRNA and cloned cDNA specifying the !1third component of mouse complement. !$#cross-references MUID:83117730; PMID:6961437 !$#contents C3a !$#accession A93938 !'##molecule_type mRNA !'##residues 671-748 ##label DOM REFERENCE A21898 !$#authors Sottrup-Jensen, L.; Stepanik, T.M.; Kristensen, T.; Lonblad, !1P.B.; Jones, C.M.; Wierzbicki, D.M.; Magnusson, S.; Domdey, !1H.; Wetsel, R.A.; Lundwall, A.; Tack, B.F.; Fey, G.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:9-13 !$#title Common evolutionary origin of alpha2-macroglobulin and !1complement components C3 and C4. !$#cross-references MUID:85113177; PMID:2578664 !$#accession A21898 !'##molecule_type mRNA !'##residues 25-1663 ##label SOT REFERENCE A54561 !$#authors Hamada, J.; Cavanaugh, P.G.; Miki, K.; Nicolson, G.L. !$#journal Cancer Res. (1993) 53:4418-4423 !$#title A paracrine migration-stimulating factor for metastatic !1tumor cells secreted by mouse hepatic sinusoidal endothelial !1cells: identification as complement component C3b. !$#cross-references MUID:93373334; PMID:8364938 !$#accession A54561 !'##molecule_type protein !'##residues 25-41;749-760 ##label HAM !'##experimental_source migration-stimulating factor purified from !1medium conditioned by mouse hepatic sinusoidal endothelial !1cells REFERENCE S16189 !$#authors Sato, T.; Hong, M.H.; Jin, C.H.; Ishimi, Y.; Udagawa, N.; !1Shinki, T.; Abe, E.; Suda, T. !$#journal FEBS Lett. (1991) 285:21-24 !$#title The specific production of the third component of complement !1by osteoblastic cells treated with 1-alpha, !125-dihydroxyvitamin D(3). !$#cross-references MUID:91293304; PMID:2065778 !$#accession S16369 !'##molecule_type protein !'##residues 25-31 ##label SAT !$#accession S16189 !'##status preliminary !'##molecule_type protein !'##residues 671-677,'X',679-680 ##label SA2 REFERENCE I49563 !$#authors Fey, G.; Domdey, H.; Wiebauer, K.; Whitehead, A.S.; Odink, !1K. !$#journal Springer Semin. Immunopathol. (1983) 6:119-147 !$#title Structure and expression of the C3 gene. !$#cross-references MUID:84045280; PMID:6356427 !$#accession I49563 !'##status preliminary !'##molecule_type mRNA !'##residues 25-136,'Q',138-240 ##label FEY !'##cross-references GB:M35659; NID:g192280; PIDN:AAA37339.1; !1PID:g192281 REFERENCE I49576 !$#authors Fey, G.H.; Wiebauer, K.; Domdey, H. !$#journal Ann. N. Y. Acad. Sci. (1983) 421:307-312 !$#title Amino acid sequences of mouse complement C3 derived from !1nucleotide sequences of cloned cDNA. !$#cross-references MUID:84201365; PMID:6609661 !$#accession I49576 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 658-761 ##label RES !'##cross-references GB:M33032; NID:g192391; PIDN:AAA37378.1; !1PID:g192392 COMMENT Complement C3 contains two chains, formed by removal of four !1residues and linked by a disulfide bond. Its activation by a !1C3 convertase, which is the central reaction in both !1classical and alternative complement pathways, releases the !1C3a anaphylatoxin from the amino end of the alpha chain and !1generates C3b, which associates with the Bb fragment of !1complement factor B to form the !1alternative-complement-pathway C3/C5 convertase. COMMENT C3a anaphylatoxin is a vasoactive peptide and a mediator of !1inflammation. COMMENT C3b, with its highly reactive thiol group, binds to the !1surface of foreign particles and facilitates phagocytosis. !1It binds to complement C5 and renders it susceptible to !1proteolysis by the classical-complement-pathway C3/C5 !1convertase. The activity of C3b is regulated by proteolytic !1cleavage involving factors H and I. Its degradation products !1can also be biologically active. COMMENT The major site of synthesis of this plasma protein is the !1liver. GENETICS !$#introns 27/2; 90/3 !$#note the list of introns may be incomplete CLASSIFICATION #superfamily alpha-2-macroglobulin KEYWORDS acute phase; complement alternate pathway; complement !1pathway; glycoprotein; hydrolase; immune response; !1inflammation; plasma; serine proteinase; thiolester bond FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-666 #product complement C3 and C3b beta chain #status !8predicted #label C3BB\ !$25-666,671-1663 #product complement C3 #status predicted #label CC3\ !$25-666,749-1663 #product C3b #status predicted #label C3B\ !$671-1663 #product complement C3 alpha chain #status predicted !8#label CC3A\ !$671-748 #product C3a anaphylatoxin #status predicted #label !8C3T\ !$749-1663 #product C3b alpha' chain #status predicted #label !8C3BA\ !$946-1303 #product C3dk fragment #status predicted #label CDK\ !$1002-1303 #product C3d fragment #status predicted #label C3D\ !$1424-1457 #region properdin binding\ !$559-816,626-661, !$693-720,694-727, !$707-728,873-1513, !$1101-1158, !$1358-1489, !$1389-1458, !$1506-1511, !$1518-1590, !$1537-1661,1637-1646 #disulfide_bonds #status predicted\ !$748-749 #cleavage_site Arg-Ser (C3 convertase) #status !8predicted\ !$939,1617 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$1010-1013 #cross-link thiolester (Cys-Gln) #status predicted\ !$1303-1304 #cleavage_site Arg-Ser (complement factor I) #status !8predicted\ !$1320-1321 #cleavage_site Arg-Ser (complement factor I) #status !8predicted SUMMARY #length 1663 #molecular-weight 186482 #checksum 646 SEQUENCE /// ENTRY C3RT #type complete TITLE complement C3 precursor - rat ALTERNATE_NAMES 37K phospholipase A2 inhibitory protein CONTAINS alternative-complement-pathway C3/C5 convertase (EC 3.4.21.47) C3b subunit; C3a anaphylatoxin ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 04-Dec-1992 #sequence_revision 07-Oct-1994 #text_change 18-Jun-1999 ACCESSIONS S15764; A54562; A01260; B35979; A35979; PN0567; PN0566; !1A32281; S08692 REFERENCE S15764 !$#authors Misumi, Y.; Sohda, M.; Ikehara, Y. !$#journal Nucleic Acids Res. (1990) 18:2178 !$#title Nucleotide and deduced amino acid sequence of rat complement !1C3. !$#cross-references MUID:90245672; PMID:2336397 !$#accession S15764 !'##molecule_type mRNA !'##residues 1-1663 ##label MIS !'##cross-references EMBL:X52477; NID:g56953; PIDN:CAA36716.1; !1PID:g56954 REFERENCE A54562 !$#authors Sundstrom, S.A.; Komm, B.S.; Ponce-de-Leon, H.; Yi, Z.; !1Teuscher, C.; Lyttle, C.R. !$#journal J. Biol. Chem. (1989) 264:16941-16947 !$#title Estrogen regulation of tissue-specific expression of !1complement C3. !$#cross-references MUID:89380332; PMID:2674144 !$#accession A54562 !'##status translation not shown !'##molecule_type mRNA !'##residues 'P',1316-1595 ##label SUN !'##cross-references GB:M29866; NID:g203200; PIDN:AAA40837.1; !1PID:g554423 REFERENCE A01260 !$#authors Jacobs, J.W.; Rubin, J.S.; Hugli, T.E.; Bogardt, R.A.; !1Mariz, I.K.; Daniels, J.S.; Daughaday, W.H.; Bradshaw, R.A. !$#journal Biochemistry (1978) 17:5031-5038 !$#title Purification, characterization, and amino acid sequence of !1rat anaphylatoxin (C3a). !$#cross-references MUID:79062262; PMID:309768 !$#accession A01260 !'##molecule_type protein !'##residues 671-703,'K',705-720,'KL',723-748 ##label JAC !'##note three disulfide bonds are present REFERENCE A35979 !$#authors Suwa, Y.; Kudo, I.; Imaizumi, A.; Okada, M.; Kamimura, T.; !1Suzuki, Y.; Chang, H.W.; Hara, S.; Inoue, K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:2395-2399 !$#title Proteinaceous inhibitors of phospholipase A-2 purified from !1inflammatory sites in rats. !$#cross-references MUID:90207203; PMID:2320562 !$#accession B35979 !'##status preliminary !'##molecule_type protein !'##residues 'X',998-1005 ##label SUW !$#accession A35979 !'##molecule_type protein !'##residues 'X',961-962,'P',964-969 ##label SU2 REFERENCE PN0566 !$#authors Nakagawa, H.; Komorita, N. !$#journal Biochem. Biophys. Res. Commun. (1993) 194:1181-1187 !$#title Complement component C3-derived neutrophil chemotactic !1factors purified from exudate of rat carrageenin-induced !1inflammation. !$#cross-references MUID:93356786; PMID:8352775 !$#accession PN0567 !'##molecule_type protein !'##residues 568-592 ##label NAK !'##note amino end of a C3-derived peptide designated exudate neutrophil !1chemotactic factor 2, or C3-beta-c !$#accession PN0566 !'##molecule_type protein !'##residues 671-687 ##label NA2 !'##note amino end of peptide designated neutrophil chemotactic factor 1 !1and probably identical to C3a anaphylatoxin REFERENCE A32281 !$#authors Kuivanen, P.C.; Capulong, R.B.; Harkins, R.N.; DeSombre, !1E.R. !$#journal Biochem. Biophys. Res. Commun. (1989) 158:898-905 !$#title The estrogen-responsive 110K and 74K rat uterine secretory !1proteins are structurally related to complement component !1C3. !$#cross-references MUID:89149812; PMID:2645873 !$#accession A32281 !'##molecule_type protein !'##residues 25-41 ##label KUI !'##experimental_source 17beta-estradiol-stimulated uterus of immature !1rat !'##note the authors treat this 74K uterine secretory protein, identical !1as far as sequenced to complement C3, as a distinct, !1homologous protein rather than as an alternatively processed !1form or fragment COMMENT Complement C3 contains two chains, formed by removal of four !1residues and linked by a disulfide bond. Its activation by a !1C3 convertase, which is the central reaction in both !1classical and alternative complement pathways, releases the !1C3a anaphylatoxin from the amino end of the alpha chain and !1generates C3b, which associates with the Bb fragment of !1complement factor B to form the !1alternative-complement-pathway C3/C5 convertase. COMMENT C3a anaphylatoxin is a vasoactive peptide and a mediator of !1inflammation. COMMENT C3b, with its highly reactive thiol group, binds to the !1surface of foreign particles and facilitates phagocytosis. !1It binds to complement C5 and renders it susceptible to !1proteolysis by the classical-complement-pathway C3/C5 !1convertase. The activity of C3b is regulated by proteolytic !1cleavage involving factors H and I. Its degradation products !1can also be biologically active. COMMENT The major site of synthesis of this plasma protein is the !1liver. CLASSIFICATION #superfamily alpha-2-macroglobulin KEYWORDS acute phase; chemotaxis; complement alternate pathway; !1complement pathway; glycoprotein; hydrolase; immune !1response; inflammation; liver; plasma; serine proteinase; !1thiolester bond FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-666 #product complement C3 and C3b beta chain #status !8predicted #label C3BB\ !$25-666,671-1663 #product complement C3 #status predicted #label CC3\ !$25-666,749-1663 #product complement C3b #status predicted #label C3B\ !$671-1663 #product complement C3 alpha chain #status predicted !8#label CC3A\ !$671-748 #product C3a anaphylatoxin #status experimental !8#label C3T\ !$749-1663 #product complement C3b alpha' chain #status !8predicted #label C3BA\ !$946-1303 #product C3dk fragment #status predicted #label CDK\ !$1002-1303 #product C3d fragment #status predicted #label C3D\ !$1424-1457 #region properdin binding\ !$558-816,626-661, !$693-720,694-727, !$707-728,873-1513, !$1101-1158, !$1358-1489, !$1389-1458, !$1506-1511, !$1518-1590,1537-1661 #disulfide_bonds #status predicted\ !$748-749 #cleavage_site Arg-Ser (C3 convertase) #status !8predicted\ !$939,1617 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$1010-1013 #cross-link thiolester (Cys-Gln) #status predicted\ !$1303-1304 #cleavage_site Arg-Ser (complement factor I) #status !8predicted\ !$1320-1321 #cleavage_site Arg-Ser (complement factor I) #status !8predicted SUMMARY #length 1663 #molecular-weight 186459 #checksum 3009 SEQUENCE /// ENTRY C3GP #type complete TITLE complement C3 precursor - guinea pig CONTAINS alternative-complement-pathway C3/C5 convertase (EC 3.4.21.47) C3b subunit; C3a anaphylatoxin ORGANISM #formal_name Cavia porcellus #common_name guinea pig DATE 07-Feb-1992 #sequence_revision 07-Oct-1994 #text_change 18-Jun-1999 ACCESSIONS A37156; S03375; A20342; D20342; C20342; A31222 REFERENCE A37156 !$#authors Auerbach, H.S.; Burger, R.; Dodds, A.; Colten, H.R. !$#journal J. Clin. Invest. (1990) 86:96-106 !$#title Molecular basis of complement C3 deficiency in guinea pigs. !$#cross-references MUID:90307998; PMID:1973176 !$#accession A37156 !'##molecule_type mRNA !'##residues 1-1666 ##label AUE !'##cross-references GB:M34054; NID:g191262; PIDN:AAA37038.1; !1PID:g305335 REFERENCE S03375 !$#authors Gerard, N.P.; Lively, M.O.; Gerard, C. !$#journal Protein Seq. Data Anal. (1988) 1:473-478 !$#title Amino acid sequence of guinea pig C3a anaphylatoxin. !$#cross-references MUID:89113342; PMID:3064079 !$#accession S03375 !'##molecule_type protein !'##residues 676-730,'N',732-752 ##label GER !'##experimental_source complement-activated guinea pig serum !'##note form isolated is inactive C3a anaphylatoxin and is missing the !1carboxyl-terminal arginine REFERENCE A90479 !$#authors Thomas, M.L.; Tack, B.F. !$#journal Biochemistry (1983) 22:942-947 !$#title Identification and alignment of a thiol ester site in the !1third component of guinea pig complement. !$#cross-references MUID:83178889; PMID:6838833 !$#accession A20342 !'##molecule_type protein !'##residues 676-687 ##label TH1 !$#accession D20342 !'##molecule_type protein !'##residues 993-1012,1014-1017,'E',1019-1030,'Y' ##label TH2 REFERENCE A20342 !$#authors Goldberger, G.; Thomas, M.L.; Tack, B.F.; Williams, J.; !1Colten, H.R.; Abraham, G.N. !$#journal J. Biol. Chem. (1981) 256:12617-12619 !$#title NH2-terminal structure and cleavage of guinea pig pro-C3, !1the precursor of the third complement component. !$#cross-references MUID:82075767; PMID:6458605 !$#accession C20342 !'##molecule_type protein !'##residues 23-38 ##label GOL COMMENT Complement C3 contains two chains, formed by removal of four !1residues and linked by a disulfide bond. Its activation by a !1C3 convertase, which is the central reaction in both !1classical and alternative complement pathways, releases the !1C3a anaphylatoxin from the amino end of the alpha chain and !1generates C3b, which associates with the Bb fragment of !1complement factor B to form the !1alternative-complement-pathway C3/C5 convertase. COMMENT C3a anaphylatoxin is a vasoactive peptide and a mediator of !1inflammation. COMMENT C3b, with its highly reactive thiol group, binds to the !1surface of foreign particles and facilitates phagocytosis. !1It binds to complement C5 and renders it susceptible to !1proteolysis by the classical-complement-pathway C3/C5 !1convertase. The activity of C3b is regulated by proteolytic !1cleavage involving factors H and I. Its degradation products !1can also be biologically active. COMMENT The major site of synthesis of this plasma protein is the !1liver. CLASSIFICATION #superfamily alpha-2-macroglobulin KEYWORDS acute phase; complement alternate pathway; complement !1pathway; glycoprotein; hydrolase; immune response; !1inflammation; liver; plasma; serine proteinase; thiolester !1bond FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-671 #product complement C3 and C3b beta chain #status !8predicted #label C3BB\ !$23-671,676-1666 #product complement C3 #status predicted #label CC3\ !$23-671,754-1666 #product complement C3b #status predicted #label C3B\ !$676-1666 #product complement C3 alpha chain #status predicted !8#label CC3A\ !$676-753 #product C3a anaphylatoxin #status predicted #label !8C3T\ !$754-1666 #product complement C3b alpha' chain #status !8predicted #label C3BA\ !$951-1308 #product C3dk fragment #status predicted #label CDK\ !$1007-1308 #product C3d fragment #status predicted #label C3D\ !$1429-1461 #region properdin binding\ !$557-821,630-666, !$698-725,699-732, !$712-733,878-1517, !$1106-1163, !$1363-1493, !$1394-1462, !$1510-1515, !$1522-1593, !$1540-1664,1640-1649 #disulfide_bonds #status predicted\ !$753-754 #cleavage_site Arg-Ser (C3 convertase) #status !8predicted\ !$944,1620 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$1015-1018 #cross-link thiolester (Cys-Gln) #status !8experimental\ !$1308-1309 #cleavage_site Arg-Ser (complement factor I) #status !8predicted\ !$1325-1326 #cleavage_site Arg-Ser (complement factor I) #status !8predicted SUMMARY #length 1666 #molecular-weight 186487 #checksum 5419 SEQUENCE /// ENTRY C3NJ #type complete TITLE complement C3 precursor - monocled cobra CONTAINS alternative-complement-pathway C3/C5 convertase (EC 3.4.21.47) C3b subunit; C3a anaphylatoxin ORGANISM #formal_name Naja naja kaouthia, Naja naja siamensis #common_name monocled cobra DATE 18-Jun-1993 #sequence_revision 07-Oct-1994 #text_change 17-Mar-2000 ACCESSIONS A46513 REFERENCE A46513 !$#authors Fritzinger, D.C.; Petrella, E.C.; Connelly, M.B.; !1Bredehorst, R.; Vogel, C.W. !$#journal J. Immunol. (1992) 149:3554-3562 !$#title Primary structure of cobra complement component C3. !$#cross-references MUID:93056528; PMID:1431125 !$#accession A46513 !'##molecule_type mRNA !'##residues 1-1651 ##label FRI !'##cross-references GB:L02365; NID:g213372; PIDN:AAA49385.1; !1PID:g213373 !'##note authors' translation shows Arg-1408 after residue 1438 and, !1consequently, residues 1408-1438 are displaced one codon to !1the left !'##note sequence extracted from NCBI backbone (NCBIP:118403) and !1corrected to correspond with the translation of the !1nucleotide sequence COMMENT Complement C3 contains two chains, formed by removal of four !1residues and linked by a disulfide bond. Its activation by a !1C3 convertase, which is the central reaction in both !1classical and alternative complement pathways, releases the !1C3a anaphylatoxin from the amino end of the alpha chain and !1generates C3b, which associates with the Bb fragment of !1complement factor B to form the !1alternative-complement-pathway C3/C5 convertase. COMMENT C3a anaphylatoxin is a vasoactive peptide and a mediator of !1inflammation. COMMENT C3b, with its highly reactive thiol group, binds to the !1surface of foreign particles and facilitates phagocytosis. !1It binds to complement C5 and renders it susceptible to !1proteolysis by the classical-complement-pathway C3/C5 !1convertase. The activity of C3b is regulated by proteolytic !1cleavage involving factors H and I. Its degradation products !1can also be biologically active. COMMENT The major site of synthesis of this plasma protein is the !1liver. CLASSIFICATION #superfamily alpha-2-macroglobulin KEYWORDS acute phase; complement alternate pathway; complement !1pathway; glycoprotein; hydrolase; immune response; !1inflammation; liver; plasma; serine proteinase; thiolester !1bond FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-655 #product complement C3 and C3b beta chain #status !8predicted #label C3BB\ !$23-655,660-1651 #product complement C3 #status predicted #label CC3\ !$23-655,739-1651 #product complement C3b #status predicted #label C3B\ !$660-1651 #product complement C3 alpha chain #status predicted !8#label CC3A\ !$660-738 #product C3a anaphylatoxin #status predicted #label !8C3T\ !$739-1651 #product complement C3b alpha' chain #status !8predicted #label C3BA\ !$1412-1445 #region properdin binding\ !$546-807,615-650, !$683-710,684-717, !$697-718,863-1501, !$1091-1147, !$1346-1477, !$1377-1446, !$1494-1499, !$1506-1578, !$1525-1649,1625-1634 #disulfide_bonds #status predicted\ !$738-739 #cleavage_site Arg-Ser (C3 convertase) #status !8predicted\ !$999-1002 #cross-link thiolester (Cys-Gln) #status predicted SUMMARY #length 1651 #molecular-weight 184925 #checksum 3526 SEQUENCE /// ENTRY C4HU #type complete TITLE complement C4A precursor [validated] - human CONTAINS classical-complement-pathway C3/C5 convertase (EC 3.4.21.43) C4b subunit; complement C4a anaphylatoxin ORGANISM #formal_name Homo sapiens #common_name man DATE 25-Feb-1985 #sequence_revision 23-Aug-1996 #text_change 08-Dec-2000 ACCESSIONS I56095; A29177; B29177; A90845; A19311; A92337; S12866; !1A17265; A32335; A27600; I58991; I37399; A01262; A01263 REFERENCE I56095 !$#authors Yu, C.Y. !$#journal J. Immunol. (1991) 146:1057-1066 !$#title The complete exon-intron structure of a human complement !1component C4A gene. DNA sequences, polymorphism, and linkage !1to the 21-hydroxylase gene. !$#cross-references MUID:91108039; PMID:1988494 !$#accession I56095 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-1744 ##label RES !'##cross-references GB:M59815; NID:g179672; PIDN:AAA51855.1; !1PID:g179674 REFERENCE A29177 !$#authors Belt, K.T.; Yu, C.Y.; Carroll, M.C.; Porter, R.R. !$#journal Immunogenetics (1985) 21:173-180 !$#title Polymorphism of human complement component C4. !$#cross-references MUID:85156269; PMID:3838531 !$#accession A29177 !'##molecule_type DNA !'##residues 1-22 ##label BEL !'##cross-references GB:M14823 !$#accession B29177 !'##molecule_type DNA !'##residues 1056-1225 ##label BE3 !'##cross-references GB:M14824; NID:g179675; PIDN:AAA52292.1; !1PID:g553210 REFERENCE A90845 !$#authors Belt, K.T.; Carroll, M.C.; Porter, R.R. !$#journal Cell (1984) 36:907-914 !$#title The structural basis of the multiple forms of human !1complement component C4. !$#cross-references MUID:84156544; PMID:6546707 !$#accession A90845 !'##molecule_type mRNA !'##residues 20-346,'S',348-417,'A',419-725,'P',727-1200,'S',1202-1285, !1'S',1287-1418,1422-1744 ##label BE2 !'##cross-references GB:K02403 REFERENCE A19311 !$#authors Carroll, M.C.; Porter, R.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:264-267 !$#title Cloning of a human complement component C4 gene. !$#cross-references MUID:83117835; PMID:6572000 !$#accession A19311 !'##molecule_type mRNA !'##residues 1195-1285,'S',1287-1294 ##label CAR !'##cross-references GB:V00502; GB:J00080; NID:g30010; PIDN:CAA23760.1; !1PID:g1335030 REFERENCE A92337 !$#authors Moon, K.E.; Gorski, J.P.; Hugli, T.E. !$#journal J. Biol. Chem. (1981) 256:8685-8692 !$#title Complete primary structure of human C4a anaphylatoxin. !$#cross-references MUID:81264286; PMID:6167582 !$#accession A92337 !'##molecule_type protein !'##residues 680-725,'PN',728-756 ##label MOO REFERENCE S12866 !$#authors Hessing, M.; van't Veer, C.; Hackeng, T.M.; Bouma, B.N.; !1Iwanaga, S. !$#journal FEBS Lett. (1990) 271:131-136 !$#title Importance of the alpha(3)-fragment of complement C4 for the !1binding with C4b-binding protein. !$#cross-references MUID:91032049; PMID:1699796 !$#accession S12866 !'##molecule_type protein !'##residues 757,'X',759-771;980-990 ##label HES REFERENCE A17265 !$#authors Campbell, R.D.; Gagnon, J.; Porter, R.R. !$#journal Biochem. J. (1981) 199:359-370 !$#title Amino acid sequence around the thiol and reactive acyl !1groups of human complement component C4. !$#cross-references MUID:82182029; PMID:6978711 !$#accession A17265 !'##molecule_type protein !'##residues 957-1012,'E',1014-1044 ##label CAM REFERENCE A32335 !$#authors Chakravarti, D.N.; Campbell, R.D.; Porter, R.R. !$#journal Mol. Immunol. (1987) 24:1187-1197 !$#title The chemical structure of the C4d fragment of the human !1complement component C4. !$#cross-references MUID:88094444; PMID:3696167 !$#accession A32335 !'##molecule_type protein !'##residues 957-1012,'E',1014-1108,'I',1110-1175,'S',1177-1270,'V', !11272-1336 ##label CHA !'##note 1073-Gly, 1120-Leu, 1121-Ser, 1124-Ile, 1125-His, 1207-Ala, !11210-Arg were also found REFERENCE A27600 !$#authors Chakravarti, D.N.; Campbell, R.D.; Gagnon, J. !$#journal FEBS Lett. (1983) 154:387-390 !$#title Amino acid sequence of a polymorphic segment from fragment !1C4d of human complement component C4. !$#cross-references MUID:83158189; PMID:6832377 !$#accession A27600 !'##molecule_type protein !'##residues 1199-1270,'V',1272-1299,'V',1301-1304 ##label CH2 REFERENCE I58991 !$#authors Whitehead, A.S.; Goldberger, G.; Woods, D.E.; Markham, A.F.; !1Colten, H.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:5387-5391 !$#title Use of a cDNA clone for the fourth component of human !1complement (C4) for analysis of a genetic deficiency of C4 !1in guinea pig. !$#cross-references MUID:83299979; PMID:6577433 !$#accession I58991 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1448-1474 ##label RE2 !'##cross-references GB:K00830; NID:g187772; PIDN:AAA36229.1; !1PID:g187773 REFERENCE I37396 !$#authors Sargent, C.A.; Anderson, M.J.; Hsieh, S.L.; Kendall, E.; !1Gomez-Escobar, N.; Campbell, R.D. !$#journal Hum. Mol. Genet. (1994) 3:481-488 !$#title Characterisation of the novel gene G11 lying adjacent to the !1complement C4A gene in the human major histocompatibility !1complex. !$#cross-references MUID:94282044; PMID:8012361 !$#accession I37399 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-21 ##label RE3 !'##cross-references EMBL:X77491; NID:g453410; PIDN:CAA54627.1; !1PID:g453411 COMMENT This protein is synthesized as a single-chain precursor and, !1prior to secretion, is enzymatically cleaved to form a !1trimer of nonidentical chains (alpha, beta, and gamma) which !1are linked by disulfide bonds. COMMENT The activation of complement C4 by complement subcomponent !1C1s releases the C4a anaphylatoxin from the amino end of the !1alpha chain and generates C4b, which associates with the 2a !1fragment of complement factor 2 to form the !1classical-complement-pathway C3 convertase. The C4b,C2a !1fragment then associates with the 3b fragment of complement !1factor 3 to form the classical-complement-pathway C5 !1convertase. COMMENT C4a anaphylatoxin is a vasoactive peptide and a mediator of !1inflammation. COMMENT The activity of C4b is regulated by proteolytic cleavage !1involving C4b-binding protein and factor I. COMMENT Residues 1446 or 1449 may be the carboxyl end of the alpha !1chain. COMMENT There are at least two genes coding for C4, C4A and C4B. !1Each gene has many alleles. GENETICS !$#gene GDB:C4A !'##cross-references GDB:119732; OMIM:120810 !$#map_position 6p21.3-6p21.3 !$#introns 22/2; 88/3; 156/1; 179/3; 209/2; 237/1; 269/2; 304/3; 349/1; !1387/3; 447/3; 508/3; 570/3; 623/3; 666/1; 691/1; 757/1; 794/ !12; 818/1; 864/3; 934/3; 952/1; 982/1; 1052/1; 1077/2; 1129/ !13; 1168/3; 1226/1; 1303/3; 1359/3; 1379/3; 1411/1; 1473/2; !11503/3; 1528/3; 1563/1; 1593/1; 1626/1; 1654/1; 1698/2 CLASSIFICATION #superfamily alpha-2-macroglobulin KEYWORDS acute phase; complement classical pathway; glycoprotein; !1hydrolase; inflammation; plasma; polymorphism; serine !1proteinase; thiolester bond FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-675 #product complement C4 beta chain #status predicted !8#label BET\ !$20-675,757-1446, !$1454-1744 #product C4b #status predicted #label C4B\ !$680-1446 #product complement C4 alpha chain #status predicted !8#label ALP\ !$680-756 #product C4a anaphylatoxin #status experimental !8#label C4A\ !$757-845 #region C4b-binding protein binding\ !$957-1336 #product C4d fragment #status experimental #label !8C4D\ !$1454-1744 #product complement C4 gamma chain #status predicted !8#label GAM\ !$756-757 #cleavage_site Arg-Ala (complement subcomponent C1s) !8#status experimental\ !$1010-1013 #cross-link thiolester (Cys-Gln) #status !8experimental\ !$1328 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 1744 #molecular-weight 192860 #checksum 9431 SEQUENCE /// ENTRY A24558 #type complete TITLE complement C4 precursor - mouse CONTAINS classical-complement-pathway C3/C5 convertase (EC 3.4.21.43) C4b subunit; complement C4a anaphylatoxin ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Mar-1989 #sequence_revision 11-Nov-1994 #text_change 18-Jun-1999 ACCESSIONS A24558; A25371; A21692; A30520; A60227; A22039; A29059; !1A01264; B41195; I59084; I48274; I54567; I69023 REFERENCE A24558 !$#authors Sepich, D.S.; Noonan, D.J.; Ogata, R.T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:5895-5899 !$#title Complete cDNA sequence of the fourth component of murine !1complement. !$#cross-references MUID:85298264; PMID:3862104 !$#accession A24558 !'##molecule_type mRNA !'##residues 1-1738 ##label SEP !'##cross-references GB:M11729; NID:g199080; PIDN:AAA39506.1; !1PID:g387420 !'##experimental_source strain B10.WR REFERENCE A25371 !$#authors Nonaka, M.; Nakayama, K.; Yeul, Y.D.; Takahashi, M. !$#journal J. Biol. Chem. (1985) 260:10936-10943 !$#title Complete nucleotide and derived amino acid sequences of the !1fourth component of mouse complement (C4). Evolutionary !1aspects. !$#cross-references MUID:85289294; PMID:2993295 !$#accession A25371 !'##molecule_type mRNA !'##residues 1-131,'Y',133-326,'E',328-569,'E',571-1323,'N',1325-1441, !1'K',1443-1452,'V',1454-1738 ##label NON !'##cross-references GB:M11789 !'##experimental_source strain FM REFERENCE A94013 !$#authors Nonaka, M.; Takahashi, M.; Natsuume-Sakai, S.; Nonaka, M.; !1Tanaka, S.; Shimizu, A.; Honjo, T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:6822-6826 !$#title Isolation of cDNA clones specifying the fourth component of !1mouse complement and its isotype, sex-limited protein. !$#cross-references MUID:85038607; PMID:6208559 !$#accession A21692 !'##molecule_type mRNA !'##residues 651-719,'G',721-738,'AI',741-805 ##label NO2 !'##cross-references GB:M12970 !'##experimental_source strain FM REFERENCE A30520 !$#authors Taillon-Miller, P.A.; Shreffler, D.C. !$#journal J. Immunol. (1988) 141:2382-2387 !$#title Structural basis for the C4d.1/C4d.2 serologic allotypes of !1murine complement component C4. !$#cross-references MUID:89009745; PMID:2459207 !$#accession A30520 !'##molecule_type DNA !'##residues 961-1205,'Q',1207-1290 ##label TAI !'##cross-references GB:M23186; NID:g340821; PIDN:AAA40487.1; !1PID:g554392 !'##experimental_source strain B10.BR REFERENCE A60227 !$#authors Ogata, R.T.; Zepf, N.E. !$#journal Eur. J. Immunol. (1990) 20:1607-1610 !$#title C4 from C4-high and C4-low mouse strains have identical !1sequences in the region corresponding to the !1isotype-specific segment of human C4. !$#cross-references MUID:90353398; PMID:2387317 !$#accession A60227 !'##molecule_type DNA !'##residues 1099-1142 ##label OGA !'##cross-references GB:X55493; NID:g287729; PIDN:CAA39112.1; !1PID:g287730 REFERENCE A22039 !$#authors Levi-Strauss, M.; Tosi, M.; Steinmetz, M.; Klein, J.; Meo, !1T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:1746-1750 !$#title Multiple duplications of complement C4 gene correlate with !1H-2-controlled testosterone-independent expression of its !1sex-limited isoform, C4-Slp. !$#cross-references MUID:85166208; PMID:3856857 !$#accession A22039 !'##molecule_type mRNA !'##residues 1105-1118,'A',1120-1189,'T',1191-1449 ##label LEV !'##cross-references GB:K02798; NID:g199281; PIDN:AAC42021.1; !1PID:g199282 !'##experimental_source strain B10.W7R REFERENCE A93753 !$#authors Tosi, M.; Levi-Strauss, M.; Duponchel, C.; Meo, T. !$#journal Philos. Trans. R. Soc. Lond. (1984) 306:389-394 !$#title Sequence heterogeneity of murine complementary DNA clones !1related to the C4 and C4-Slp isoforms of the fourth !1complement component. !$#accession A29059 !'##molecule_type mRNA !'##residues 1258-1376 ##label TOS !'##cross-references GB:K02798 REFERENCE A01264 !$#authors Ogata, R.T.; Shreffler, D.C.; Sepich, D.S.; Lilly, S.P. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:5061-5065 !$#title cDNA clone spanning the alpha-gamma subunit junction in the !1precursor of the murine fourth complement component (C4). !$#cross-references MUID:83273751; PMID:6192448 !$#accession A01264 !'##molecule_type mRNA !'##residues 1360-1400,'S',1402-1511 ##label OG2 !'##cross-references GB:K00019; NID:g199259; PIDN:AAA39554.1; !1PID:g554209 !'##experimental_source strain B10.W7R REFERENCE A41195 !$#authors Ogata, R.T.; Sepich, D.S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:4908-4911 !$#title Genes for murine fourth complement component (C4) and !1sex-limited protein (Slp) identified by hybridization to C4- !1and Slp-specific cDNA. !$#cross-references MUID:84272739; PMID:6589636 !$#accession B41195 !'##molecule_type mRNA !'##residues 1360-1400,'S',1402-1511 ##label OG3 !'##cross-references GB:K00019; NID:g199259; PIDN:AAA39554.1; !1PID:g554209 !'##experimental_source strain B10.W7R REFERENCE I59084 !$#authors Nonaka, M.; Kimura, H.; Yeul, Y.D.; Yokoyama, S.; Nakayama, !1K.; Takahashi, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:7883-7887 !$#title Identification of the 5'-flanking regulatory region !1responsible for the difference in transcriptional control !1between mouse complement C4 and Slp genes. !$#cross-references MUID:87017050; PMID:3464002 !$#accession I59084 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-21 ##label RES !'##cross-references GB:M14225; NID:g199291; PIDN:AAA39563.1; !1PID:g554211 REFERENCE I48274 !$#authors Hemenway, C.; Kalff, M.; Stavenhagen, J.; Walthall, D.; !1Robins, D. !$#journal Nucleic Acids Res. (1986) 14:2539-2554 !$#title Sequence comparison of alleles of the fourth component of !1complement (C4) and sex-limited protein (Slp). !$#cross-references MUID:86176748; PMID:3008092 !$#accession I48274 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 591-603,'M',605-1323,'N',1325-1452,'V',1454-1585,'Q', !11587-1738 ##label RE2 !'##cross-references EMBL:X05314; NID:g50241; PIDN:CAA28936.1; !1PID:g50242 REFERENCE I54567 !$#authors Nonaka, M.; Nakayama, K.; Yeul, Y.D.; Shimizu, A.; !1Takahashi, M. !$#journal Immunol. Rev. (1985) 87:81-99 !$#title Molecular cloning and characterization of complementary and !1genomic DNA clones for mouse C4 and SLP. !$#cross-references MUID:86031969; PMID:2997024 !$#accession I54567 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-128 ##label RE3 !'##cross-references GB:M12968; NID:g199267; PIDN:AAA39558.1; !1PID:g199270 !$#accession I69023 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1724-1738 ##label RE4 !'##cross-references GB:M12969; NID:g199268; PIDN:AAA39559.1; !1PID:g387439 COMMENT This protein is synthesized as a single-chain precursor and, !1prior to secretion, is enzymatically cleaved to form a !1trimer of nonidentical chains (alpha, beta, and gamma) which !1are linked by disulfide bonds. COMMENT The activation of complement C4 by complement subcomponent !1C1s releases the C4a anaphylatoxin from the amino end of the !1alpha chain and generates C4b, which associates with the 2a !1fragment of complement factor 2 to form the !1classical-complement-pathway C3 convertase. The C4b,C2a !1fragment then associates with the 3b fragment of complement !1factor 3 to form the classical-complement-pathway C5 !1convertase. COMMENT C4a anaphylatoxin is a vasoactive peptide and a mediator of !1inflammation. COMMENT The activity of C4b is regulated by proteolytic cleavage !1involving C4b-binding protein and factor I. GENETICS !$#introns 22/2; 86/3; 977/3; 1047/3; 1073/3; 1125/3; 1164/3; 1221/3 !$#note the list of introns is incomplete CLASSIFICATION #superfamily alpha-2-macroglobulin KEYWORDS acute phase; complement classical pathway; glycoprotein; !1hydrolase; inflammation; plasma; polymorphism; serine !1proteinase; thiolester bond FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-673 #product complement C4 beta chain #status predicted !8#label BET\ !$20-673,754-1440, !$1448-1738 #product complement C4b #status predicted #label C4B\ !$678-1440 #product complement C4 alpha chain #status predicted !8#label ALP\ !$678-753 #product C4a anaphylatoxin #status predicted #label !8C4A\ !$754-843 #region C4b-binding protein binding\ !$953-1332 #product C4d fragment #status predicted #label C4D\ !$1448-1738 #product complement C4 gamma chain #status predicted !8#label GAM\ !$224,743,1387 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$753-754 #cleavage_site Arg-Asn (complement subcomponent C1s) !8#status predicted\ !$1006-1009 #cross-link thiolester (Cys-Gln) #status predicted SUMMARY #length 1738 #molecular-weight 192870 #checksum 4149 SEQUENCE /// ENTRY C5HU #type complete TITLE complement C5 precursor [validated] - human CONTAINS C5a anaphylatoxin; C5b ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 08-Dec-2000 ACCESSIONS A40075; A27689; A01267; A01266; S15121 REFERENCE A40075 !$#authors Haviland, D.L.; Haviland, J.C.; Fleischer, D.T.; Hunt, A.; !1Wetsel, R.A. !$#journal J. Immunol. (1991) 146:362-368 !$#title Complete cDNA sequence of human complement pro-C5. Evidence !1of truncated transcripts derived from a single copy gene. !$#cross-references MUID:91079575; PMID:1984448 !$#accession A40075 !'##molecule_type mRNA !'##residues 1-1676 ##label HAV !'##cross-references GB:M57729; NID:g179982; PIDN:AAA51925.1; !1PID:g179983 !'##note 518-Ser was also found REFERENCE A27689 !$#authors Wetsel, R.A.; Lemons, R.S.; Le Beau, M.M.; Barnum, S.R.; !1Noack, D.; Tack, B.F. !$#journal Biochemistry (1988) 27:1474-1482 !$#title Molecular analysis of human complement component C5: !1localization of the structural gene to chromosome 9. !$#cross-references MUID:88209511; PMID:3365401 !$#accession A27689 !'##molecule_type mRNA !'##residues 412-1676 ##label WET !'##cross-references GB:M65134; GB:M18879; NID:g179691; PIDN:AAA51856.1; !1PID:g179692 REFERENCE A01267 !$#authors Fernandez, H.N.; Hugli, T.E. !$#journal J. Biol. Chem. (1978) 253:6955-6964 !$#title Primary structural analysis of the polypeptide portion of !1human C5a anaphylatoxin. Polypeptide sequence determination !1and assignment of the oligosaccharide attachment site in !1C5a. !$#cross-references MUID:79005687; PMID:690134 !$#accession A01267 !'##molecule_type protein !'##residues 678-751 ##label FER REFERENCE A01266 !$#authors Lundwall, A.B.; Wetsel, R.A.; Kristensen, T.; Whitehead, !1A.S.; Woods, D.E.; Ogden, R.C.; Colten, H.R.; Tack, B.F. !$#journal J. Biol. Chem. (1985) 260:2108-2112 !$#title Isolation and sequence analysis of a cDNA clone encoding the !1fifth complement component. !$#cross-references MUID:85130937; PMID:2579066 !$#accession A01266 !'##molecule_type mRNA !'##residues 412-854,'SLALSPRLECNGKISGHCKLRLPGSSDSPASASQVAGITGTHHHAQPT' !1##label LUN !'##cross-references GB:K02874 !'##note the carboxyl-terminal part of the sequence in this report !1appears to be derived from translation of an ALU repeat !1sequence REFERENCE S15121 !$#authors Bohnsack, J.F.; Mollison, K.W.; Buko, A.M.; Ashworth, J.C.; !1Hill, H.R. !$#journal Biochem. J. (1991) 273:635-640 !$#title Group B streptococci inactivate complement component C5a by !1enzymic cleavage at the C-terminus. !$#cross-references MUID:91144547; PMID:1996961 !$#contents annotation COMMENT Complement C5 contains two disulfide-linked chains, formed !1by removal of four basic residues. C5 convertase releases !1C5a anaphylatoxin from the amino end of the alpha chain, !1generating C5b (beta and alpha' chains). COMMENT Activation of C5 initiates the spontaneous assembly of the !1late complement components, C5-C9, into the membrane attack !1complex. C5b has a transient binding site for C6. The C5b-C6 !1complex is the foundation upon which the membrane attack !1complex is assembled. COMMENT C5a has potent spasmogenic and chemotactic activity. GENETICS !$#gene GDB:C5 !'##cross-references GDB:119734; OMIM:120900 !$#map_position 9q34.1-9q34.1 CLASSIFICATION #superfamily alpha-2-macroglobulin KEYWORDS complement alternate pathway; complement pathway; cytolysis; !1glycoprotein; inflammation; membrane attack complex; plasma FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-673,678-1676 #product complement C5 #status predicted #label MAT\ !$19-673,752-1676 #product C5b #status predicted #label C5B\ !$19-673 #product complement C5 and C5b beta chain #status !8predicted #label C5BB\ !$678-1676 #product complement C5 alpha chain #status predicted !8#label C5A\ !$678-751 #product C5a anaphylatoxin #status experimental !8#label C5T\ !$752-1676 #product C5b alpha' chain #status predicted #label !8C5BA\ !$567-810,634-669, !$698-724,699-731, !$711-732,866-1527, !$1101-1159, !$1375-1505, !$1405-1474, !$1520-1525, !$1532-1606, !$1553-1676,1654-1657 #disulfide_bonds #status predicted\ !$741 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$751-752 #cleavage_site Arg-Leu (C5 convertase) #status !8experimental\ !$911,1115,1630 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1676 #molecular-weight 188330 #checksum 3858 SEQUENCE /// ENTRY C5MS #type complete TITLE complement C5 precursor - mouse CONTAINS C5a anaphylatoxin; C5b ORGANISM #formal_name Mus musculus #common_name house mouse DATE 19-Nov-1988 #sequence_revision 15-Oct-1994 #text_change 18-Jun-1999 ACCESSIONS A35530; A27538; A40429 REFERENCE A35530 !$#authors Wetsel, R.A.; Fleischer, D.T.; Haviland, D.L. !$#journal J. Biol. Chem. (1990) 265:2435-2440 !$#title Deficiency of the murine fifth complement component (C5). A !12-base pair gene deletion in a 5'-exon. !$#cross-references MUID:90153853; PMID:2303408 !$#accession A35530 !'##molecule_type mRNA !'##residues 1-215,'L' ##label WET !'##cross-references GB:M35526; GB:J05234; NID:g192302; PIDN:AAA37348.1; !1PID:g309123 REFERENCE A27538 !$#authors Wetsel, R.A.; Ogata, R.T.; Tack, B.F. !$#journal Biochemistry (1987) 26:737-743 !$#title Primary structure of the fifth component of murine !1complement. !$#cross-references MUID:87185363; PMID:2436653 !$#accession A27538 !'##molecule_type mRNA !'##residues 'PGL',44-1680 ##label WET2 REFERENCE A40429 !$#authors Haviland, D.L.; Haviland, J.C.; Fleischer, D.T.; Wetsel, !1R.A. !$#journal J. Biol. Chem. (1991) 266:11818-11825 !$#title Structure of the murine fifth complement component (C5) !1gene. A large, highly interrupted gene with a variant donor !1splice site and organizational homology with the third and !1fourth complement component genes. !$#cross-references MUID:91268053; PMID:1711041 !$#accession A40429 !'##molecule_type DNA !'##residues 1-15 ##label HAV !'##cross-references GB:M64852 COMMENT Complement C5 contains two disulfide-linked chains, formed !1by removal of four basic residues. C5 convertase releases !1C5a anaphylatoxin from the amino end of the alpha chain, !1generating C5b (beta and alpha' chains). COMMENT Activation of C5 initiates the spontaneous assembly of the !1late complement components, C5-C9, into the membrane attack !1complex. C5b has a transient binding site for C6. The C5b-C6 !1complex is the foundation upon which the membrane attack !1complex is assembled. COMMENT C5a has potent spasmogenic and chemotactic activity. GENETICS !$#map_position 2 !$#introns 22/3; 86/3; 140/3; 164/3; 195/2; 223/1; 253/2; 291/3; 334/1; !1372/3; 434/3; 502/3; 572/3; 622/3; 667/1; 691/1; 757/1; 787/ !12; 812/1; 858/3; 934/3; 955/1; 985/1; 1056/1; 1081/2; 1134/ !13; 1166/3; 1224/1; 1292/3; 1343/3; 1364/3; 1392/1; 1411/2; !11445/3; 1470/3; 1506/1; 1534/1; 1564/1; 1592/1; 1637/2 CLASSIFICATION #superfamily alpha-2-macroglobulin KEYWORDS complement alternate pathway; complement pathway; cytolysis; !1glycoprotein; inflammation; membrane attack complex; plasma FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-674,679-1679 #product complement C5 #status predicted #label MAT\ !$19-674,756-1679 #product C5b #status predicted #label C5B\ !$19-674 #product complement C5 and C5b beta chain #status !8predicted #label C5BB\ !$679-1679 #product complement C5 alpha chain #status predicted !8#label C5A\ !$679-755 #product C5a anaphylatoxin #status predicted #label !8C5T\ !$756-1679 #product C5b alpha' chain #status predicted #label !8C5BA\ !$567-814,635-670, !$702-728,703-735, !$715-736,870-1531, !$1105-1163, !$1379-1509, !$1409-1478, !$1524-1529, !$1536-1609, !$1557-1679,1657-1660 #disulfide_bonds #status predicted\ !$915,1119,1633 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1680 #molecular-weight 188876 #checksum 3888 SEQUENCE /// ENTRY ZYHUEP #type complete TITLE metalloproteinase tissue inhibitor 1 precursor [validated] - human ALTERNATE_NAMES erythroid potentiating activity (EPA); fibroblast collagenase inhibitor; tissue inhibitor of metalloproteinases (TIMP-1) ORGANISM #formal_name Homo sapiens #common_name man DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 08-Dec-2000 ACCESSIONS A93372; A93363; A23534; A20595; A35826; A48417; S20318; !1S15872; I52912; S66461; A01269 REFERENCE A93372 !$#authors Docherty, A.J.P.; Lyons, A.; Smith, B.J.; Wright, E.M.; !1Stephens, P.E.; Harris, T.J.R.; Murphy, G.; Reynolds, J.J. !$#journal Nature (1985) 318:66-69 !$#title Sequence of human tissue inhibitor of metalloproteinases and !1its identity to erythroid-potentiating activity. !$#cross-references MUID:86040463; PMID:3903517 !$#accession A93372 !'##molecule_type mRNA !'##residues 1-207 ##label DOC !'##cross-references GB:X03124; NID:g37182; PIDN:CAA26902.1; PID:g37183 REFERENCE A93363 !$#authors Gasson, J.C.; Golde, D.W.; Kaufman, S.E.; Westbrook, C.A.; !1Hewick, R.M.; Kaufman, R.J.; Wong, G.G.; Temple, P.A.; !1Leary, A.C.; Brown, E.L.; Orr, E.C.; Clark, S.C. !$#journal Nature (1985) 315:768-771 !$#title Molecular characterization and expression of the gene !1encoding human erythroid-potentiating activity. !$#cross-references MUID:85240567; PMID:3839290 !$#accession A93363 !'##molecule_type mRNA !'##residues 1-207 ##label GAS REFERENCE A23534 !$#authors Carmichael, D.F.; Sommer, A.; Thompson, R.C.; Anderson, !1D.C.; Smith, C.G.; Welgus, H.G.; Stricklin, G.P. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:2407-2411 !$#title Primary structure and cDNA cloning of human fibroblast !1collagenase inhibitor. !$#cross-references MUID:86205964; PMID:3010309 !$#accession A23534 !'##molecule_type mRNA !'##residues 1-207 ##label CAR !'##cross-references GB:M12670; NID:g182482; PIDN:AAA52436.1; !1PID:g182483 !'##note parts of this sequence were confirmed by protein sequencing !'##note carbohydrate binding sites were determined REFERENCE A20595 !$#authors Stricklin, G.P.; Welgus, H.G. !$#journal J. Biol. Chem. (1983) 258:12252-12258 !$#title Human skin fibroblast collagenase inhibitor. !$#cross-references MUID:84032401; PMID:6313647 !$#accession A20595 !'##molecule_type protein !'##residues 24-44,'L',46 ##label STR !'##note six disulfide bonds are present REFERENCE A35826 !$#authors Rapp, G.; Freudenstein, J.; Klaudiny, J.; Mucha, J.; Wempe, !1F.; Zimmer, M.; Scheit, K.H. !$#journal DNA Cell Biol. (1990) 9:479-485 !$#title Characterization of three abundant mRNAs from human ovarian !1granulosa cells. !$#cross-references MUID:91025550; PMID:2171551 !$#accession A35826 !'##molecule_type mRNA !'##residues 1-207 ##label RAP !'##cross-references GB:M38188 REFERENCE A48417 !$#authors Van Ranst, M.; Norga, K.; Masure, S.; Proost, P.; !1Vandekerckhove, F.; Auwerx, J.; Van Damme, J.; Opdenakker, !1G. !$#journal Cytokine (1991) 3:231-239 !$#title The cytokine-protease connection: identification of a 96-kD !1THP-1 gelatinase and regulation by interleukin-1 and !1cytokine inducers. !$#cross-references MUID:91355647; PMID:1653055 !$#accession A48417 !'##molecule_type protein !'##residues 'X',25,'X',27-35,'X',37-52 ##label VAN !'##experimental_source monocytic cell line THP-1 !'##note sequence modified after extraction from NCBI backbone !'##note sequence incorrectly identified as 96K gelatinase REFERENCE S20318 !$#authors Osthues, A.; Knaeuper, V.; Oberhoff, R.; Reinke, H.; !1Tschesche, H. !$#journal FEBS Lett. (1992) 296:16-20 !$#title Isolation and characterization of tissue inhibitors of !1metalloproteinases (TIMP-1 and TIMP-2) from human rheumatoid !1synovial fluid. !$#cross-references MUID:92111776; PMID:1730286 !$#accession S20318 !'##molecule_type protein !'##residues 'X',25,'X',27-35,'X',37-38 ##label OST !'##experimental_source rheumatoid synovial fluid REFERENCE S15872 !$#authors Opdenakker, G.; Masure, S.; Proost, P.; Billiau, A.; van !1Damme, J. !$#journal FEBS Lett. (1991) 284:73-78 !$#title Natural human monocyte gelatinase and its inhibitor. !$#cross-references MUID:91285112; PMID:1647974 !$#accession S15872 !'##molecule_type protein !'##residues 'X',25,'X',27-35,'X',37-42,'X',44,'X',46,'X',48-51 ##label !1FEB !'##experimental_source peripheral blood monocytes REFERENCE A38978 !$#authors Williamson, R.A.; Marston, F.A.O.; Angal, S.; Koklitis, P.; !1Panico, M.; Morris, H.R.; Carne, A.F.; Smith, B.J.; Harris, !1T.J.R.; Freedman, R.B. !$#journal Biochem. J. (1990) 268:267-274 !$#title Disulphide bond assignment in human tissue inhibitor of !1metalloproteinases (TIMP). !$#cross-references MUID:90303199; PMID:2163605 !$#contents annotation; disulfide bonds REFERENCE I52912 !$#authors Opbroek, A.; Kenney, M.C.; Brown, D. !$#journal Curr. Eye Res. (1993) 12:877-883 !$#title Characterization of a human corneal metalloproteinase !1inhibitor (TIMP-1). !$#cross-references MUID:94123576; PMID:7507419 !$#accession I52912 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-207 ##label RES !'##cross-references GB:S68252; NID:g545022; PIDN:AAD14009.1; !1PID:g4261709 REFERENCE S66461 !$#authors Triebel, S.; Blaeser, J.; Gote, T.; Pelz, G.; Schueren, E.; !1Schmitt, M.; Tschesche, H. !$#journal Eur. J. Biochem. (1995) 231:714-719 !$#title Evidence for the tissue inhibitor of metalloproteinases-1 !1(TIMP-1) in human polymorphonuclear leukocytes. !$#cross-references MUID:95377303; PMID:7649172 !$#accession S66461 !'##molecule_type protein !'##residues 24-38 ##label TRI !'##experimental_source polymorphonuclear leukocytes COMMENT This protein, found in a variety of body fluids, complexes !1with metalloproteinases, irreversibly inactivating them. It !1also mediates erythropoiesis in vitro; but, unlike IL-3, it !1is species-specific, stimulating the growth and !1differentiation of only human and murine erythroid !1progenitors. COMMENT The remarkable heat stability of this protein may be due to !1disulfide bond formation. GENETICS !$#gene GDB:TIMP1; CLGI; TIMP !'##cross-references GDB:119615; OMIM:305370 !$#map_position Xp11.3-Xp11.23 CLASSIFICATION #superfamily metalloproteinase inhibitor KEYWORDS erythropoiesis; glycoprotein; metalloproteinase inhibitor; !1mitogen FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-207 #product metalloproteinase inhibitor 1 #status !8experimental #label MAT\ !$24-93,26-122, !$36-147,150-197, !$155-160,168-189 #disulfide_bonds #status experimental\ !$53,101 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 207 #molecular-weight 23171 #checksum 9750 SEQUENCE /// ENTRY A35685 #type complete TITLE metalloproteinase inhibitor 1 precursor - bovine ALTERNATE_NAMES cartilage-derived neovascularization inhibitor; TIMP-1; tissue inhibitor of metalloproteinases 1 ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 21-Sep-1990 #sequence_revision 12-Apr-1996 #text_change 18-Jun-1999 ACCESSIONS A35685; B34468; B29712; A34833; I46979 REFERENCE A35685 !$#authors Freudenstein, J.; Wagner, S.; Luck, R.M.; Einspanier, R.; !1Scheit, K.H. !$#journal Biochem. Biophys. Res. Commun. (1990) 171:250-256 !$#title mRNA of bovine tissue inhibitor of metalloproteinase: !1sequence and expression in bovine ovarian tissue. !$#cross-references MUID:90365711; PMID:2393392 !$#accession A35685 !'##molecule_type mRNA !'##residues 1-207 ##label FRE !'##cross-references GB:M60073; NID:g163760; PIDN:AAA30784.1; !1PID:g163761 !'##experimental_source ovary cDNA library REFERENCE A34468 !$#authors De Clerck, Y.A.; Yean, T.D.; Ratzkin, B.J.; Lu, H.S.; !1Langley, K.E. !$#journal J. Biol. Chem. (1989) 264:17445-17453 !$#title Purification and characterization of two related but !1distinct metalloproteinase inhibitors secreted by bovine !1aortic endothelial cells. !$#cross-references MUID:90008914; PMID:2551903 !$#accession B34468 !'##molecule_type protein !'##residues 24-52,'X',54-57,'LY',60-61,'L',63-65,'L',67-68,'P' ##label !1DEC !'##experimental_source culture medium of aortic endothelial cells REFERENCE A29712 !$#authors Kaczorek, M.; Honore, N.; Ribes, V.; Dehoux, P.; Cornet, P.; !1Cartwright, T.; Streeck, R.E. !$#journal Bio/Technology (1987) 5:595-598 !$#title Molecular cloning and synthesis of biologically active human !1tissue inhibitor of metalloproteinases in yeast. !$#accession B29712 !'##molecule_type protein !'##residues 24-37 ##label KAC !'##experimental_source culture medium of fibroblastic BC 21 cells !'##note protein inhibits angiogenesis REFERENCE A34833 !$#authors Moses, M.A.; Sudhalter, J.; Langer, R. !$#journal Science (1990) 248:1408-1410 !$#title Identification of an inhibitor of neovascularization from !1cartilage. !$#cross-references MUID:90288433; PMID:1694043 !$#accession A34833 !'##molecule_type protein !'##residues 24-51 ##label MOS !'##experimental_source cartilage REFERENCE I46979 !$#authors Satoh, T.; Kobayashi, K.; Yamashita, S.; Kikuchi, M.; !1Sendai, Y.; Hoshi, H. !$#journal Biol. Reprod. (1994) 50:835-844 !$#title Tissue inhibitor of metalloproteinases (TIMP-1) produced by !1granulosa and oviduct cells enhances in vitro development of !1bovine embryo. !$#cross-references MUID:94257757; PMID:8199264 !$#accession I46979 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-207 ##label SAT !'##cross-references GB:S70841; NID:g546973; PIDN:AAB30892.1; !1PID:g546974 FUNCTION !$#description regulation of extracellular matrix remodeling by inhibition !1of matrix metalloproteinases; TIMP-1 and TIMP-2 complex !1specifically with progelatinase B and progelatinase A, !1respectively, possibly controlling their activation; TIMP-1 !1and TIMP-2 possess erythroid potentiating activity !$#note transcription induced by cytokines, tumor promoters, and !1anti-inflammatory agents !$#note TIMP-1 and TIMP-3 have distinct but overlapping !1tissue-specific expression patterns CLASSIFICATION #superfamily metalloproteinase inhibitor KEYWORDS erythropoiesis; extracellular matrix; glycoprotein; !1metalloproteinase inhibitor; mitogen FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-207 #product metalloproteinase inhibitor 1 #status !8experimental #label MAT\ !$24-93,26-122, !$36-147,150-197, !$155-160,168-189 #disulfide_bonds #status predicted\ !$53,101 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 207 #molecular-weight 23031 #checksum 7873 SEQUENCE /// ENTRY A33350 #type complete TITLE metalloproteinase inhibitor 1 precursor - rabbit ALTERNATE_NAMES TIMP-1; tissue inhibitor of metalloproteinases 1 ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 30-Jun-1992 #sequence_revision 12-Apr-1996 #text_change 18-Jun-1999 ACCESSIONS A33350; A30864 REFERENCE A33350 !$#authors Horowitz, S.; Dafni, N.; Shapiro, D.L.; Holm, B.A.; Notter, !1R.H.; Quible, D.J. !$#journal J. Biol. Chem. (1989) 264:7092-7095 !$#title Hyperoxic exposure alters gene expression in the lung. !1Induction of the tissue inhibitor of metalloproteinases mRNA !1and other mRNAs. !$#cross-references MUID:89214135; PMID:2708356 !$#accession A33350 !'##molecule_type mRNA !'##residues 1-206 ##label HOR !'##cross-references GB:J04712; NID:g165742; PIDN:AAA31478.1; !1PID:g165743 !'##experimental_source hyperoxi-exposed lung of New Zealand White !1rabbits COMMENT Expression of this protein in the lung is induced 6-fold by !1hyperoxia. FUNCTION !$#description regulation of extracellular matrix remodeling by inhibition !1of matrix metalloproteinases; TIMP-1 and TIMP-2 complex !1specifically with progelatinase B and progelatinase A, !1respectively, possibly controlling their activation; TIMP-1 !1and TIMP-2 possess erythroid potentiating activity !$#note transcription induced by cytokines, tumor promoters, and !1anti-inflammatory agents !$#note TIMP-1 and TIMP-3 have distinct but overlapping !1tissue-specific expression patterns CLASSIFICATION #superfamily metalloproteinase inhibitor KEYWORDS erythropoiesis; extracellular matrix; glycoprotein; !1metalloproteinase inhibitor; mitogen FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-206 #product metalloproteinase inhibitor 1 #status !8predicted #label MAT\ !$24-93,26-122, !$36-147,150-196, !$155-160,168-188 #disulfide_bonds #status predicted\ !$53,101 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 206 #molecular-weight 22758 #checksum 4434 SEQUENCE /// ENTRY A26106 #type complete TITLE metalloproteinase inhibitor 1 precursor - mouse ALTERNATE_NAMES erythroid potentiating activity (EPA); fibroblast collagenase inhibitor 16C8; tissue inhibitor of metalloproteinases 1 (TIMP-1); TPA-induced protein precursor; TPA-S1 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 05-Oct-1988 #sequence_revision 12-Apr-1996 #text_change 18-Jun-1999 ACCESSIONS A26917; A26106; A26633; A05276 REFERENCE A26917 !$#authors Johnson, M.D.; Housey, G.M.; Kirschmeier, P.T.; Weinstein, !1I.B. !$#journal Mol. Cell. Biol. (1987) 7:2821-2829 !$#title Molecular cloning of gene sequences regulated by tumor !1promoters and mitogens through protein kinase C. !$#cross-references MUID:88038821; PMID:3670294 !$#accession A26917 !'##molecule_type mRNA !'##residues 1-205 ##label JOH !'##cross-references GB:M17243; NID:g202111; PIDN:AAA40471.1; !1PID:g202112 !'##experimental_source embryonic fibroblast cDNA library REFERENCE A26106 !$#authors Edwards, D.R.; Waterhouse, P.; Holman, M.L.; Denhardt, D.T. !$#journal Nucleic Acids Res. (1986) 14:8863-8878 !$#title A growth-responsive gene (16C8) in normal mouse fibroblasts !1homologous to a human collagenase inhibitor with !1erythroid-potentiating activity: evidence for inducible and !1constitutive transcripts. !$#cross-references MUID:87066763; PMID:3024122 !$#accession A26106 !'##molecule_type mRNA !'##residues 1-205 ##label EDW !'##cross-references GB:X04684; NID:g49702; PIDN:CAA28387.1; PID:g49704 !'##experimental_source embryonic fibroblast cDNA library REFERENCE A26633 !$#authors Gewert, D.R.; Coulombe, B.; Castelino, M.; Skup, D.; !1Williams, B.R.G. !$#journal EMBO J. (1987) 6:651-657 !$#title Characterization and expression of a murine gene homologous !1to human EPA/TIMP: a virus-induced gene in the mouse. !$#cross-references MUID:87218524; PMID:3034603 !$#accession A26633 !'##molecule_type DNA !'##residues 1-51,'R',53-66,'M',67-116,'KF',119-120,'N',122-138,'V', !1140-142,'KN',144-193,'L',195-205 ##label GEW !'##cross-references GB:M28312; NID:g193040; PIDN:AAB42179.1; !1PID:g193042 REFERENCE A93424 !$#authors Skup, D.; Windass, J.D.; Sor, F.; George, H.; Williams, !1B.R.G.; Fukuhara, H.; De Maeyer-Guignard, J.; De Maeyer, E. !$#journal Nucleic Acids Res. (1982) 10:3069-3084 !$#title Molecular cloning of partial cDNA copies of two distinct !1mouse IFN-beta mRNAs. !$#cross-references MUID:82247191; PMID:6179042 !$#accession A05276 !'##molecule_type mRNA !'##residues 168-193,'L',195-205 ##label SKU !'##cross-references GB:V00755; GB:J00425; NID:g51554; PIDN:CAA24132.1; !1PID:g817965 !'##note authors thought this clone represented a form of interferon !1beta GENETICS !$#gene Timp !$#map_position X !$#introns 41/3; 68/3; 110/3; 152/3 FUNCTION !$#description regulation of extracellular matrix remodeling by inhibition !1of matrix metalloproteinases; TIMP-1 and TIMP-2 complex !1specifically with progelatinase B and progelatinase A, !1respectively, possibly controlling their activation; TIMP-1 !1and TIMP-2 possess erythroid potentiating activity !$#note transcription induced by cytokines, tumor promoters, and !1anti-inflammatory agents !$#note TIMP-1 and TIMP-3 have distinct but overlapping !1tissue-specific expression patterns CLASSIFICATION #superfamily metalloproteinase inhibitor KEYWORDS erythropoiesis; extracellular matrix; glycoprotein; !1metalloproteinase inhibitor; mitogen FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-205 #product metalloproteinase inhibitor 1 #status !8predicted #label MAT\ !$25-94,27-123, !$37-148,151-197, !$156-161,169-189 #disulfide_bonds #status predicted\ !$54,102 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 205 #molecular-weight 22628 #checksum 2718 SEQUENCE /// ENTRY JC2557 #type complete TITLE metalloproteinase inhibitor 1 precursor - rat ALTERNATE_NAMES TIMP-1 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JC2557; B39120; S20326 REFERENCE JC2557 !$#authors Okada, A.; Garnier, J.M.; Vicaire, S.; Basset, P. !$#journal Gene (1994) 147:301-302 !$#title Cloning of the cDNA encoding rat tissue inhibitor of !1metalloproteinase 1 (TIMP-1), amino acid comparison with !1other TIMPs, and gene expression in rat tissues. !$#cross-references MUID:95011636; PMID:7926820 !$#accession JC2557 !'##status preliminary !'##molecule_type mRNA !'##residues 1-217 ##label OKA !'##cross-references EMBL:U06179; NID:g468057; PIDN:AAA85780.1; !1PID:g468058 REFERENCE A39120 !$#authors Olson Jr., J.A.; Shiverick, K.T.; Ogilvie, S.; Buhi, W.C.; !1Raizada, M.K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:1928-1932 !$#title Angiotensin II induces secretion of plasminogen activator !1inhibitor 1 and a tissue metalloprotease inhibitor-related !1protein from rat brain astrocytes. !$#cross-references MUID:91156719; PMID:2000398 !$#accession B39120 !'##status preliminary !'##molecule_type protein !'##residues 24-36,'B',38,'B',40-42,'X',44 ##label OLS REFERENCE S20325 !$#authors Roswit, W.T.; McCourt, D.W.; Partridge, N.C.; Jeffrey, J.J. !$#journal Arch. Biochem. Biophys. (1992) 292:402-410 !$#title Purification and sequence analysis of two rat tissue !1inhibitors of metalloproteinases. !$#cross-references MUID:92117648; PMID:1309971 !$#accession S20326 !'##molecule_type protein !'##residues 24-45 ##label ROS FUNCTION !$#description regulation of extracellular matrix remodeling by inhibition !1of matrix metalloproteinases; TIMP-1 and TIMP-2 complex !1specifically with progelatinase B and progelatinase A, !1respectively, possibly controlling their activation; TIMP-1 !1and TIMP-2 possess erythroid potentiating activity !$#note transcription induced by cytokines, tumor promoters, and !1anti-inflammatory agents !$#note TIMP-1 and TIMP-3 have distinct but overlapping !1tissue-specific expression patterns CLASSIFICATION #superfamily metalloproteinase inhibitor KEYWORDS erythropoiesis; extracellular matrix; glycoprotein; !1metalloproteinase inhibitor; mitogen FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-217 #product metalloproteinase inhibitor 1 #status !8experimental #label MAT\ !$101,130 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 217 #molecular-weight 23793 #checksum 7859 SEQUENCE /// ENTRY A37128 #type complete TITLE metalloproteinase inhibitor 2 precursor [validated] - human ALTERNATE_NAMES chondrocyte-derived angiogenesis inhibitor; TIMP-2; tissue inhibitor of metalloproteinases 2 ORGANISM #formal_name Homo sapiens #common_name man DATE 08-Mar-1991 #sequence_revision 12-Apr-1996 #text_change 08-Dec-2000 ACCESSIONS A37128; B35996; A34464; A34415; S21303; S20319; S17165; !1S58794 REFERENCE A37128 !$#authors Stetler-Stevenson, W.G.; Brown, P.D.; Onisto, M.; Levy, !1A.T.; Liotta, L.A. !$#journal J. Biol. Chem. (1990) 265:13933-13938 !$#title Tissue inhibitor of metalloproteinases-2 (TIMP-2) mRNA !1expression in tumor cell lines and human tumor tissues. !$#cross-references MUID:90338014; PMID:2380196 !$#accession A37128 !'##molecule_type mRNA !'##residues 1-220 ##label STE !'##cross-references GB:J05593; NID:g339706; PIDN:AAA61186.1; !1PID:g339707 !'##experimental_source A2058 melanoma cell cDNA library REFERENCE A35996 !$#authors Boone, T.C.; Johnson, M.J.; De Clerck, Y.A.; Langley, K.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:2800-2804 !$#title cDNA cloning and expression of a metalloproteinase inhibitor !1related to tissue inhibitor of metalloproteinases. !$#cross-references MUID:90207285; PMID:2157214 !$#accession B35996 !'##molecule_type mRNA !'##residues 1-220 ##label BOO !'##cross-references GB:M32304; NID:g187522; PIDN:AAA59581.1; !1PID:g307195 !'##experimental_source fetal aorta cDNA library REFERENCE A34464 !$#authors Stetler-Stevenson, W.G.; Krutzsch, H.C.; Liotta, L.A. !$#journal J. Biol. Chem. (1989) 264:17374-17378 !$#title Tissue inhibitor of metalloproteinase (TIMP-2). A new member !1of the metalloproteinase inhibitor family. !$#cross-references MUID:90008902; PMID:2793861 !$#accession A34464 !'##molecule_type protein !'##residues 27-77,'K',79-81,'I',83-100,'E',102-117;119-121,'R',123-149, !1'Q',151-174,'T',176-219 ##label ST2 !'##experimental_source serum-free culture medium of A2058 cells REFERENCE A34415 !$#authors Goldberg, G.I.; Marmer, B.L.; Grant, G.A.; Eisen, A.Z.; !1Wilhelm, S.; He, C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:8207-8211 !$#title Human 72-kilodalton type IV collagenase forms a complex with !1a tissue inhibitor of metalloproteases designated TIMP-2. !$#cross-references MUID:90046765; PMID:2554304 !$#accession A34415 !'##molecule_type protein !'##residues 30-51;124-141;159-173 ##label GOL REFERENCE S21303 !$#authors Malik, K.; Sejima, H.; Aoki, T.; Iwata, K. !$#submission submitted to the EMBL Data Library, August 1990 !$#description Nucleotide sequence of a TIMP-II cDNA. !$#accession S21303 !'##molecule_type mRNA !'##residues 30-95,'V',97-214 ##label MAL !'##cross-references EMBL:X54533; NID:g37180; PIDN:CAA38400.1; !1PID:g37181 REFERENCE S20318 !$#authors Osthues, A.; Knaeuper, V.; Oberhoff, R.; Reinke, H.; !1Tschesche, H. !$#journal FEBS Lett. (1992) 296:16-20 !$#title Isolation and characterization of tissue inhibitors of !1metalloproteinases (TIMP-1 and TIMP-2) from human rheumatoid !1synovial fluid. !$#cross-references MUID:92111776; PMID:1730286 !$#accession S20319 !'##molecule_type protein !'##residues 'X',28,'X',30-38,'X',40-41 ##label OST !'##experimental_source rheumatoid synovial fluid REFERENCE S17165 !$#authors Ward, R.V.; Hembry, R.M.; Reynolds, J.J.; Murphy, G. !$#journal Biochem. J. (1991) 278:179-187 !$#title The purification of tissue inhibitor of metalloproteinases-2 !1from its 72 kDa progelatinase complex. !$#cross-references MUID:91354200; PMID:1909113 !$#accession S17165 !'##status preliminary !'##molecule_type protein !'##residues 27,'X',29,'X',31-38 ##label WAR REFERENCE S58794 !$#authors Ohba, Y.; Goto, Y.; Kimura, Y.; Suzuki, F.; Hisa, T.; !1Takahashi, K.; Takigawa, M. !$#journal Biochim. Biophys. Acta (1995) 1245:1-8 !$#title Purification of an angiogenesis inhibitor from culture !1medium conditioned by a human chondrosarcoma-derived !1chondrocytic cell line, HCS-2/8. !$#cross-references MUID:95383380; PMID:7544625 !$#accession S58794 !'##status preliminary !'##molecule_type protein !'##residues 27-37 ##label OHB GENETICS !$#gene GDB:TIMP2 !'##cross-references GDB:132612; OMIM:188825 !$#map_position 17q25-17q25 FUNCTION !$#description regulation of extracellular matrix remodeling by inhibition !1of matrix metalloproteinases; TIMP-1 and TIMP-2 complex !1specifically with progelatinase B and progelatinase A, !1respectively, possibly controlling their activation; TIMP-1 !1and TIMP-2 possess erythroid potentiating activity CLASSIFICATION #superfamily metalloproteinase inhibitor KEYWORDS erythropoiesis; extracellular matrix; metalloproteinase !1inhibitor; mitogen FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-220 #product metalloproteinase inhibitor 2 #status !8experimental #label MAT\ !$27-98,29-127, !$39-152,154-201, !$159-164,172-193 #disulfide_bonds #status predicted SUMMARY #length 220 #molecular-weight 24399 #checksum 6096 SEQUENCE /// ENTRY S38624 #type fragment TITLE metalloproteinase inhibitor 2 precursor - long-tailed hamster (fragment) ALTERNATE_NAMES TIMP-2; tissue inhibitor of metalloproteinases 2 ORGANISM #formal_name Cricetulus longicaudatus #common_name long-tailed hamster DATE 06-Jan-1995 #sequence_revision 12-Apr-1996 #text_change 18-Jun-1999 ACCESSIONS S38624 REFERENCE S38624 !$#authors Suzuki, Y. !$#submission submitted to the EMBL Data Library, November 1993 !$#accession S38624 !'##molecule_type mRNA !'##residues 1-196 ##label SUZ !'##cross-references EMBL:X75924; NID:g414876; PIDN:CAA53528.1; !1PID:g414877 FUNCTION !$#description regulation of extracellular matrix remodeling by inhibition !1of matrix metalloproteinases; TIMP-1 and TIMP-2 complex !1specifically with progelatinase B and progelatinase A, !1respectively, possibly controlling their activation; TIMP-1 !1and TIMP-2 possess erythroid potentiating activity CLASSIFICATION #superfamily metalloproteinase inhibitor KEYWORDS erythropoiesis; extracellular matrix; metalloproteinase !1inhibitor; mitogen FEATURE !$3-196 #product metalloproteinase inhibitor 2 #status !8predicted #label MAT\ !$3-74,5-103,15-128, !$130-177,135-140, !$148-169 #disulfide_bonds #status predicted SUMMARY #length 196 #checksum 7766 SEQUENCE /// ENTRY JH0683 #type complete TITLE metalloproteinase inhibitor 2 precursor - mouse ALTERNATE_NAMES TIMP-2; tissue inhibitor of metalloproteinases 2 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JH0683; JC1234; S18428; S15987; S26189 REFERENCE JH0683 !$#authors Shimizu, S.; Malik, K.; Sejima, H.; Kishi, J.; Hayakawa, T.; !1Koiwai, O. !$#journal Gene (1992) 114:291-292 !$#title Cloning and sequencing of the cDNA encoding a mouse tissue !1inhibitor of metalloproteinase-2. !$#cross-references MUID:92290292; PMID:1601312 !$#accession JH0683 !'##molecule_type mRNA !'##residues 1-220 ##label SHI !'##cross-references EMBL:X62622; NID:g54801; PIDN:CAA44491.1; !1PID:g54802 !'##experimental_source 3T3 fibroblast, strain Balb/c REFERENCE JC1234 !$#authors Leco, K.J.; Hayden, L.J.; Sharma, R.R.; Rocheleau, H.; !1Greenberg, A.H.; Edwards, D.R. !$#journal Gene (1992) 117:209-217 !$#title Differential regulation of TIMP-1 and TIMP-2 mRNA expression !1in normal and Ha-ras-transformed murine fibroblasts. !$#cross-references MUID:92347695; PMID:1639268 !$#accession JC1234 !'##molecule_type mRNA !'##residues 1-11,'H',13-20,'L',22-194,'E',196-220 ##label LEC !'##cross-references GB:M93954; NID:g202053; PIDN:AAA40446.1; !1PID:g202054 REFERENCE S18428 !$#authors Kishi, J. !$#journal Matrix (1991) 11:373 !$#title Correction. !$#cross-references MUID:92244125; PMID:1667327 !$#accession S18428 !'##molecule_type protein !'##residues 27-46,'H',48,50-53,'VD',56,'DY' ##label KIS REFERENCE S15987 !$#authors Kishi, J.I.; Ogawa, K.; Yamamoto, S.; Hayakawa, T. !$#journal Matrix (1991) 11:10-16 !$#title Purification and characterization of a new tissue inhibitor !1of metalloproteinases (TIMP-2) from mouse colon 26 tumor !1cells. !$#cross-references MUID:91226375; PMID:1851244 !$#accession S15987 !'##molecule_type protein !'##residues 27-46,'HLX',50-52,'LX',55-56,'DXX',60,'X',62 ##label KI2 !'##note this sequence has been revised in reference S18428 FUNCTION !$#description regulation of extracellular matrix remodeling by inhibition !1of matrix metalloproteinases; TIMP-1 and TIMP-2 complex !1specifically with progelatinase B and progelatinase A, !1respectively, possibly controlling their activation; TIMP-1 !1and TIMP-2 possess erythroid potentiating activity CLASSIFICATION #superfamily metalloproteinase inhibitor KEYWORDS erythropoiesis; extracellular matrix; metalloproteinase !1inhibitor; mitogen FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-220 #product metalloproteinase inhibitor 2 #status !8experimental #label MAT\ !$27-98,29-127, !$39-152,154-201, !$159-164,172-193 #disulfide_bonds #status predicted SUMMARY #length 220 #molecular-weight 24328 #checksum 6045 SEQUENCE /// ENTRY S45683 #type complete TITLE metalloproteinase inhibitor 2 precursor - rat ALTERNATE_NAMES TIMP-2; tissue inhibitor of metalloproteinases 2 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S45683; S20325; S60160 REFERENCE S45683 !$#authors Cook, T.F.; Burke, J.S.; Bergman, K.D.; Quinn, C.O.; !1Jeffrey, J.J.; Partridge, N.C. !$#journal Arch. Biochem. Biophys. (1994) 311:313-320 !$#title Cloning and regulation of rat tissue inhibitor of !1metalloproteinases-2 in osteoblastic cells. !$#cross-references MUID:94263207; PMID:8203893 !$#accession S45683 !'##molecule_type mRNA !'##residues 1-220 ##label COO !'##cross-references GB:U14526; NID:g540204; PIDN:AAA21553.1; !1PID:g540205 REFERENCE S20325 !$#authors Roswit, W.T.; McCourt, D.W.; Partridge, N.C.; Jeffrey, J.J. !$#journal Arch. Biochem. Biophys. (1992) 292:402-410 !$#title Purification and sequence analysis of two rat tissue !1inhibitors of metalloproteinases. !$#cross-references MUID:92117648; PMID:1309971 !$#accession S20325 !'##molecule_type protein !'##residues 27-48 ##label ROS REFERENCE S60160 !$#authors Gibbons, K.L.; O'Grady, R.L.; Piper, A.A. !$#submission submitted to the EMBL Data Library, June 1995 !$#description Rat tissue inhibitor of metalloproteinases-2: cDNA cloning !1and sequence analysis. !$#accession S60160 !'##status preliminary !'##molecule_type mRNA !'##residues 1-6,'S',8-20,'V',22-152,'E',154-220 ##label GIB !'##cross-references EMBL:L31884 GENETICS !$#gene TIMP-2 FUNCTION !$#description regulation of extracellular matrix remodeling by inhibition !1of matrix metalloproteinases; TIMP-1 and TIMP-2 complex !1specifically with progelatinase B and progelatinase A, !1respectively, possibly controlling their activation; TIMP-1 !1and TIMP-2 possess erythroid potentiating activity CLASSIFICATION #superfamily metalloproteinase inhibitor KEYWORDS erythropoiesis; extracellular matrix; metalloproteinase !1inhibitor; mitogen FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-220 #product metalloproteinase inhibitor 2 #status !8predicted #label MAT\ !$27-98,29-127, !$39-152,154-201, !$159-164,172-193 #disulfide_bonds #status predicted SUMMARY #length 220 #molecular-weight 24369 #checksum 6329 SEQUENCE /// ENTRY A35996 #type complete TITLE metalloproteinase inhibitor 2 precursor - bovine ALTERNATE_NAMES collagenase inhibitor; tissue inhibitor of metalloproteinases (TIMP-2) ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 16-Nov-1990 #sequence_revision 12-Apr-1996 #text_change 18-Jun-1999 ACCESSIONS A35996; A34468; A25322; S28151 REFERENCE A35996 !$#authors Boone, T.C.; Johnson, M.J.; De Clerck, Y.A.; Langley, K.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:2800-2804 !$#title cDNA cloning and expression of a metalloproteinase inhibitor !1related to tissue inhibitor of metalloproteinases. !$#cross-references MUID:90207285; PMID:2157214 !$#accession A35996 !'##molecule_type mRNA !'##residues 1-220 ##label BOO !'##cross-references GB:M32303; NID:g163341; PIDN:AAA30636.1; !1PID:g163342 !'##experimental_source aortic endothelial cDNA library REFERENCE A34468 !$#authors De Clerck, Y.A.; Yean, T.D.; Ratzkin, B.J.; Lu, H.S.; !1Langley, K.E. !$#journal J. Biol. Chem. (1989) 264:17445-17453 !$#title Purification and characterization of two related but !1distinct metalloproteinase inhibitors secreted by bovine !1aortic endothelial cells. !$#cross-references MUID:90008914; PMID:2551903 !$#accession A34468 !'##molecule_type protein !'##residues 27-71 ##label DEC !'##experimental_source culture medium of aortic endothelial cells REFERENCE A25322 !$#authors Murray, J.B.; Allison, K.; Sudhalter, J.; Langer, R. !$#journal J. Biol. Chem. (1986) 261:4154-4159 !$#title Purification and partial amino acid sequence of a bovine !1cartilage-derived collagenase inhibitor. !$#cross-references MUID:86140235; PMID:3005321 !$#accession A25322 !'##molecule_type protein !'##residues 27-41,'C',43-55,'EX',58-59,'X',61-66,'XS',69-71 ##label MUR !'##experimental_source cartilage REFERENCE S28151 !$#authors DeClerck, Y.A.; Yean, T.D.; Lee, Y.; Tomich, J.M.; Langley, !1K.E. !$#journal Biochem. J. (1993) 289:65-69 !$#title Characterization of the functional domain of tissue !1inhibitor of metalloproteinases-2 (TIMP-2). !$#cross-references MUID:93143691; PMID:8424773 !$#contents annotation; functional domain FUNCTION !$#description regulation of extracellular matrix remodeling by inhibition !1of matrix metalloproteinases; TIMP-1 and TIMP-2 complex !1specifically with progelatinase B and progelatinase A, !1respectively, possibly controlling their activation; TIMP-1 !1and TIMP-2 possess erythroid potentiating activity CLASSIFICATION #superfamily metalloproteinase inhibitor KEYWORDS erythropoiesis; extracellular matrix; metalloproteinase !1inhibitor; mitogen FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-220 #product metalloproteinase inhibitor 2 #status !8predicted #label MAT\ !$27-98,29-127, !$39-152,154-201, !$159-164,172-193 #disulfide_bonds #status predicted SUMMARY #length 220 #molecular-weight 24355 #checksum 3345 SEQUENCE /// ENTRY S45317 #type complete TITLE metalloproteinase inhibitor 3 precursor [validated] - human ALTERNATE_NAMES mig-5 protein; TIMP-3; tissue inhibitor of metalloproteinases 3 ORGANISM #formal_name Homo sapiens #common_name man DATE 06-Jan-1995 #sequence_revision 12-Apr-1996 #text_change 08-Dec-2000 ACCESSIONS S45317; S59515; S53870; I38023; A49614; C56937; I53025; !1S47041 REFERENCE S45317 !$#authors Uria, J.A.; Ferrando, A.A.; Velasco, G.; Freije, J.M.P.; !1Lopez-Otin, C. !$#journal Cancer Res. (1994) 54:2091-2094 !$#title Structure and expression in breast tumors of human TIMP-3, a !1new member of the metalloproteinase inhibitor family. !$#cross-references MUID:94228524; PMID:8174111 !$#accession S45317 !'##molecule_type mRNA !'##residues 1-211 ##label URI !'##cross-references EMBL:X76227; NID:g495251; PIDN:CAA53813.1; !1PID:g495252 !'##experimental_source breast tumor cDNA library REFERENCE S59515 !$#authors Silbiger, S.M.; Jacobsen, V.L.; Cupples, R.L.; Koski, R.A. !$#journal Gene (1994) 141:293-297 !$#title Cloning of cDNAs encoding human TIMP-3, a novel member of !1the tissue inhibitor of metalloproteinase family. !$#cross-references MUID:94215920; PMID:8163205 !$#accession S59515 !'##status preliminary !'##molecule_type mRNA !'##residues 1-211 ##label SIL !'##cross-references EMBL:U02571; NID:g472309; PIDN:AAA17672.1; !1PID:g472310 REFERENCE S53870 !$#authors Kishnani, N.S.; Staskus, P.W.; Yang, T.T.; Masiarz, F.R.; !1Hawkes, S.P. !$#journal Matrix Biol. (1994) 14:479-488 !$#title Identification and characterization of human tissue !1inhibitor of metalloproteinase-3 and detection of three !1additional metalloproteinase inhibitor activities in !1extracellular matrix. !$#accession S53870 !'##molecule_type protein !'##residues 'X',25,'XX',28,'X',30-35,'X',37,'X',39-41 ##label KIS REFERENCE I38023 !$#authors Wick, M.; Buerger, C.; Bruesselbach, S.; Lucibello, F.C.; !1Mueller, R. !$#journal J. Biol. Chem. (1994) 269:18953-18960 !$#title A novel member of human tissue inhibitor of !1metalloproteinases (TIMP) gene family is regulated during G1 !1progression, mitogenic stimulation, differentiation, and !1senescence. !$#cross-references MUID:94308155; PMID:8034652 !$#accession I38023 !'##molecule_type mRNA !'##residues 1-15,'W',17,'T',20-21,'PR',24-201,'X',203-211 ##label RES !'##cross-references EMBL:Z30183; NID:g520931; PIDN:CAA82918.1; !1PID:g520932 !'##experimental_source fibroblast cell line WI-38 REFERENCE A49614 !$#authors Apte, S.S.; Mattei, M.G.; Olsen, B.R. !$#journal Genomics (1994) 19:86-90 !$#title Cloning of the cDNA encoding human tissue inhibitor of !1metalloproteinases-3 (TIMP-3) and mapping of the TIMP3 gene !1to chromosome 22. !$#cross-references MUID:94245184; PMID:8188246 !$#accession A49614 !'##molecule_type mRNA !'##residues 14-20,'R',23-211 ##label APT !'##cross-references GB:L15078; NID:g407034; PIDN:AAA21815.1; !1PID:g407035 !'##experimental_source placenta cDNA library REFERENCE A56937 !$#authors Apte, S.S.; Olsen, B.R.; Murphy, G. !$#journal J. Biol. Chem. (1995) 270:14313-14318 !$#title The gene structure of tissue inhibitor of metalloproteinases !1(TIMP)-3 and its inhibitory activities define the distinct !1TIMP gene family. !$#cross-references MUID:95301511; PMID:7782289 !$#accession C56937 !'##molecule_type protein !'##residues 'X',25,'X',27-35,'X',37 ##label AP2 REFERENCE I53025 !$#authors Wilde, C.G.; Hawkins, P.R.; Coleman, R.T.; Levine, W.B.; !1Delegeane, A.M.; Okamoto, P.M.; Ito, L.Y.; Scott, R.W.; !1Seilhamer, J.J. !$#journal DNA Cell Biol. (1994) 13:711-718 !$#title Cloning and characterization of human tissue inhibitor of !1metalloproteinases-3. !$#cross-references MUID:95290091; PMID:7772252 !$#accession I53025 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-211 ##label RE2 !'##cross-references GB:S78453; NID:g998825; PIDN:AAB34532.1; !1PID:g998826 GENETICS !$#gene GDB:TIMP3 !'##cross-references GDB:138175; OMIM:188826 !$#map_position 22q12.1-22q13.2 FUNCTION !$#description regulation of extracellular matrix remodeling by inhibition !1of matrix metalloproteinases !$#note transcription induced by cytokines, tumor promoters, and !1anti-inflammatory agents !$#note TIMP-1 and TIMP-3 have distinct but overlapping !1tissue-specific expression patterns CLASSIFICATION #superfamily metalloproteinase inhibitor KEYWORDS extracellular matrix; metalloproteinase inhibitor FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-211 #product metalloproteinase inhibitor 3 #status !8experimental #label MAT\ !$24-91,26-118, !$36-143,145-192, !$150-155,163-184 #disulfide_bonds #status predicted SUMMARY #length 211 #molecular-weight 24145 #checksum 4550 SEQUENCE /// ENTRY A53532 #type complete TITLE metalloproteinase inhibitor 3 precursor - mouse ALTERNATE_NAMES TIMP-3; tissue inhibitor of metalloproteinases 3 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 27-Jun-1994 #sequence_revision 12-Apr-1996 #text_change 18-Jun-1999 ACCESSIONS A53532; S43053; A56937; B56937; I53108; S43052 REFERENCE A53532 !$#authors Leco, K.J.; Khokha, R.; Pavloff, N.; Hawkes, S.P.; Edwards, !1D.R. !$#journal J. Biol. Chem. (1994) 269:9352-9360 !$#title Tissue inhibitor of metalloproteinases-3 (TIMP-3) is an !1extracellular matrix-associated protein with a distinctive !1pattern of expression in mouse cells and tissues. !$#cross-references MUID:94179361; PMID:8132674 !$#accession A53532 !'##molecule_type mRNA !'##residues 1-211 ##label LEC !'##cross-references GB:L27424; NID:g439881; PIDN:AAA40447.1; !1PID:g439882 !'##note not glycosylated when expressed by monkey kidney COS-1 cells REFERENCE S43053 !$#authors Sun, Y.; Hegamyer, G.; Colburn, N.H. !$#journal Cancer Res. (1994) 54:1139-1144 !$#title Molecular cloning of five messenger RNAs differentially !1expressed in preneoplastic or neoplastic JB6 mouse epidermal !1cells: one is homologous to human tissue inhibitor of !1metalloproteinases-3. !$#cross-references MUID:94163596; PMID:8118794 !$#accession S43053 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 14-211 ##label SU2 !'##cross-references EMBL:Z30970 REFERENCE A56937 !$#authors Apte, S.S.; Olsen, B.R.; Murphy, G. !$#journal J. Biol. Chem. (1995) 270:14313-14318 !$#title The gene structure of tissue inhibitor of metalloproteinases !1(TIMP)-3 and its inhibitory activities define the distinct !1TIMP gene family. !$#cross-references MUID:95301511; PMID:7782289 !$#accession A56937 !'##molecule_type mRNA; DNA !'##residues 1-211 ##label APT !'##cross-references GB:L19622; NID:g438810; PIDN:AAC37669.1; !1PID:g438811; GB:U26433; GB:U26434; GB:U26435; GB:U26436; !1GB:U26437; NID:g1167532; PID:g1167534 !$#accession B56937 !'##molecule_type protein !'##residues 'X',25,'X',27-34 ##label AP2 !'##note a soluble recombinant form is N-glycosylated REFERENCE I53108 !$#authors Apte, S.S.; Hayashi, K.; Seldin, M.F.; Mattei, M.G.; !1Hayashi, M.; Olsen, B.R. !$#journal Dev. Dyn. (1994) 200:177-197 !$#title Gene encoding a novel murine tissue inhibitor of !1metalloproteinases (TIMP), TIMP-3, is expressed in !1developing mouse epithelia, cartilage, and muscle, and is !1located on mouse chromosome 10. !$#cross-references MUID:95036582; PMID:7949367 !$#accession I53108 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-211 ##label RES !'##cross-references GB:L19622; NID:g438810; PIDN:AAC37669.1; !1PID:g438811 GENETICS !$#gene timp3 !$#map_position 10 !$#introns 41/1; 68/3; 106/1; 146/3 FUNCTION !$#description regulation of extracellular matrix remodeling by inhibition !1of matrix metalloproteinases !$#note transcription induced by cytokines, tumor promoters, and !1anti-inflammatory agents !$#note TIMP-1 and TIMP-3 have distinct but overlapping !1tissue-specific expression patterns CLASSIFICATION #superfamily metalloproteinase inhibitor KEYWORDS extracellular matrix; metalloproteinase inhibitor FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-211 #product metalloproteinase inhibitor 3 #status !8experimental #label MAT\ !$24-91,26-118, !$36-143,145-192, !$150-155,163-184 #disulfide_bonds #status predicted SUMMARY #length 211 #molecular-weight 24182 #checksum 4940 SEQUENCE /// ENTRY A43429 #type complete TITLE metalloproteinase inhibitor 3 precursor - chicken ALTERNATE_NAMES 21K extracellular matrix protein; TIMP-3; tissue inhibitor of metalloproteinases 3 ORGANISM #formal_name Gallus gallus #common_name chicken DATE 04-Mar-1993 #sequence_revision 12-Apr-1996 #text_change 18-Jun-1999 ACCESSIONS A43429; A39043 REFERENCE A43429 !$#authors Pavloff, N.; Staskus, P.W.; Kishnani, N.S.; Hawkes, S.P. !$#journal J. Biol. Chem. (1992) 267:17321-17326 !$#title A new inhibitor of metalloproteinases from chicken: ChIMP-3. !1A third member of the TIMP family. !$#cross-references MUID:92381050; PMID:1512267 !$#accession A43429 !'##molecule_type mRNA !'##residues 1-212 ##label PAV !'##cross-references GB:M94531; NID:g211901; PIDN:AAA48813.1; !1PID:g211902 !'##experimental_source ten-day old embryo cDNA library !'##note sequence extracted from NCBI backbone (NCBIN:111960, !1NCBIP:111961) REFERENCE A39043 !$#authors Staskus, P.W.; Masiarz, F.R.; Pallanck, L.J.; Hawkes, S.P. !$#journal J. Biol. Chem. (1991) 266:449-454 !$#title The 21-kDa protein is a transformation-sensitive !1metalloproteinase inhibitor of chicken fibroblasts. !$#cross-references MUID:91093162; PMID:1845973 !$#accession A39043 !'##molecule_type protein !'##residues 26-51,'I',53 ##label STA !'##experimental_source cultured embryonic fibroblasts infected with !1Rous sarcoma virus !'##note contains disulfide bonds; not glycosylated; has inhibitory !1activity FUNCTION !$#description regulation of extracellular matrix remodeling by inhibition !1of matrix metalloproteinases !$#note transcription induced by cytokines, tumor promoters, and !1anti-inflammatory agents !$#note TIMP-1 and TIMP-3 have distinct but overlapping !1tissue-specific expression patterns CLASSIFICATION #superfamily metalloproteinase inhibitor KEYWORDS extracellular matrix; glycoprotein; metalloproteinase !1inhibitor FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-212 #product metalloproteinase inhibitor 3 #status !8experimental #label MAT\ !$25-92,27-119, !$37-144,146-193, !$151-156,164-185 #disulfide_bonds #status predicted\ !$208 #binding_site carbohydrate (Asn) (covalent) #status !8absent SUMMARY #length 212 #molecular-weight 24504 #checksum 6267 SEQUENCE /// ENTRY XKPGC #type complete TITLE cathelin - pig ALTERNATE_NAMES cysteine proteinase inhibitor ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 08-Dec-1995 ACCESSIONS S05660 REFERENCE S05660 !$#authors Ritonja, A.; Kopitar, M.; Jerala, R.; Turk, V. !$#journal FEBS Lett. (1989) 255:211-214 !$#title Primary structure of a new cysteine proteinase inhibitor !1from pig leucocytes. !$#cross-references MUID:90005979; PMID:2792375 !$#accession S05660 !'##molecule_type protein !'##residues 1-96 ##label RIT CLASSIFICATION #superfamily cathelin; cystatin homology KEYWORDS cysteine proteinase inhibitor; pyroglutamic acid FEATURE !$1 #modified_site pyrrolidone carboxylic acid (Gln) !8#status experimental SUMMARY #length 96 #molecular-weight 10850 #checksum 7428 SEQUENCE /// ENTRY JC1222 #type complete TITLE indolicidin precursor - bovine ALTERNATE_NAMES antimicrobial peptide ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JC1222; A42387; S25664 REFERENCE JC1222 !$#authors del Sal, G.; Storici, P.; Schneider, C.; Romeo, D.; Zanetti, !1M. !$#journal Biochem. Biophys. Res. Commun. (1992) 187:467-472 !$#title cDNA cloning of the neutrophil bactericidal peptide !1indolicidin. !$#cross-references MUID:92392368; PMID:1520337 !$#accession JC1222 !'##molecule_type mRNA !'##residues 1-144 ##label SAL !'##cross-references EMBL:X67340; NID:g462; PIDN:CAA47755.1; PID:g463 !'##experimental_source bone marrow REFERENCE A42387 !$#authors Selsted, M.E.; Novotny, M.J.; Morris, W.L.; Tang, Y.Q.; !1Smith, W.; Cullor, J.S. !$#journal J. Biol. Chem. (1992) 267:4292-4295 !$#title Indolicidin, a novel bactericidal tridecapeptide amide from !1neutrophils. !$#cross-references MUID:92165771; PMID:1537821 !$#accession A42387 !'##molecule_type protein !'##residues 131-143 ##label SEL !'##experimental_source neutrophils !'##note sequence extracted from NCBI backbone (NCBIP:83840) CLASSIFICATION #superfamily cathelin; cystatin homology KEYWORDS amidated carboxyl end FEATURE !$1-29 #domain signal sequence #status predicted #label SIG\ !$22-129 #domain cystatin homology #label CYS\ !$30-130 #domain propeptide #status predicted #label PRO\ !$131-143 #product indolicidin #status experimental #label MAT\ !$143 #modified_site amidated carboxyl end (Arg) (amide in !8mature form from following glycine) #status !8experimental SUMMARY #length 144 #molecular-weight 16479 #checksum 1637 SEQUENCE /// ENTRY UDHU #type complete TITLE cystatin C precursor [validated] - human ALTERNATE_NAMES gamma-CSF; gamma-trace; neuroendocrine basic polypeptide; post-gamma protein; post-gamma-globulin ORGANISM #formal_name Homo sapiens #common_name man DATE 06-Jul-1982 #sequence_revision 31-Mar-1991 #text_change 08-Dec-2000 ACCESSIONS S10216; S00004; JL0095; A33400; S02751; A01270; A25434; !1S12288; A32732; A60552; S10607; S55305; S10585; S14303 REFERENCE S10216 !$#authors Abrahamson, M.; Olafsson, I.; Palsdottir, A.; Ulvsbaeck, M.; !1Lundwall, A.; Jensson, O.; Grubb, A. !$#journal Biochem. J. (1990) 268:287-294 !$#title Structure and expression of the human cystatin C gene. !$#cross-references MUID:90303202; PMID:2363674 !$#accession S10216 !'##molecule_type DNA !'##residues 1-146 ##label AB1 !'##cross-references EMBL:X52255; NID:g30257; PIDN:CAA36497.1; !1PID:g296643 REFERENCE S00004 !$#authors Abrahamson, M.; Grubb, A.; Olafsson, I.; Lundwall, A. !$#journal FEBS Lett. (1987) 216:229-233 !$#title Molecular cloning and sequence analysis of cDNA coding for !1the precursor of the human cysteine proteinase inhibitor !1cystatin C. !$#cross-references MUID:87219149; PMID:3495457 !$#accession S00004 !'##molecule_type mRNA !'##residues 1-146 ##label AB2 !'##cross-references EMBL:X05607; NID:g30371; PIDN:CAA29096.1; !1PID:g755738 REFERENCE JL0095 !$#authors Levy, E.; Lopez-Otin, C.; Ghiso, J.; Geltner, D.; Frangione, !1B. !$#journal J. Exp. Med. (1989) 169:1771-1778 !$#title Stroke in Icelandic patients with hereditary amyloid !1angiopathy is related to a mutation in the cystatin C gene, !1an inhibitor of cysteine proteases. !$#cross-references MUID:89235594; PMID:2541223 !$#accession JL0095 !'##molecule_type DNA !'##residues 1-146 ##label LEV !'##cross-references GB:X61681; NID:g30367; PIDN:CAA43856.2; !1PID:g4490944 !'##note the cystatin C gene isolated from the brain of an Icelandic !1patient with hereditary cerebral hemorrhage with amyloidosis !1has a mutation of 94-Gln for Leu (CAG instead of CTG in the !1normal gene) REFERENCE A33400 !$#authors Saitoh, E.; Sabatini, L.M.; Eddy, R.L.; Shows, T.B.; Azen, !1E.A.; Isemura, S.; Sanada, K. !$#journal Biochem. Biophys. Res. Commun. (1989) 162:1324-1331 !$#title The human cystatin C gene (CST3) is a member of the cystatin !1gene family which is localized on chromosome 20. !$#cross-references MUID:89350949; PMID:2764935 !$#accession A33400 !'##molecule_type DNA !'##residues 1-24,'T',26-146 ##label SAI !'##cross-references GB:M27889; GB:M27890; GB:M27891; NID:g181385; !1PIDN:AAA52164.1; PID:g181387 REFERENCE S02751 !$#authors Ghiso, J.; Cowan, N.; Frangione, B. !$#journal Biol. Chem. Hoppe-Seyler (1988) 369:205-208 !$#title Isolation of a sequence encoding human cystatin C. !1Conservation of exon-intron structure between members of the !1cysteine proteinase inhibitors superfamily. !$#cross-references MUID:89076507; PMID:3264504 !$#accession S02751 !'##molecule_type DNA !'##residues 82-119 ##label GH2 !'##cross-references EMBL:M27769 !'##note the authors translated the codon ACC for residue 105 as Thr; !1the sequence shown follows the authors' translation REFERENCE A01270 !$#authors Grubb, A.; Lofberg, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:3024-3027 !$#title Human gamma-trace, a basic microprotein: amino acid sequence !1and presence in the adenohypophysis. !$#cross-references MUID:82222268; PMID:6283552 !$#accession A01270 !'##molecule_type protein !'##residues 27-131,'S',133-146 ##label GRU REFERENCE A25434 !$#authors Ghiso, J.; Jensson, O.; Frangione, B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:2974-2978 !$#title Amyloid fibrils in hereditary cerebral hemorrhage with !1amyloidosis of Iceland type is a variant of gamma-trace !1basic protein (cystatin C). !$#cross-references MUID:86206076; PMID:3517880 !$#accession A25434 !'##molecule_type protein !'##residues 37-93,'Q',95-146 ##label GHI REFERENCE S01461 !$#authors Turk, V.; Brzin, J.; Longer, M.; Ritonja, A.; Eropkin, M.; !1Borchart, U.; Machleidt, W. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1983) 364:1487-1496 !$#title Protein inhibitors of cysteine proteinases. III. Amino-acid !1sequence of cystatin from chicken egg white. !$#cross-references MUID:84110059; PMID:6662498 !$#accession S12288 !'##molecule_type protein !'##residues 27-73 ##label TUR REFERENCE A32732 !$#authors Brzin, J.; Popovic, T.; Turk, V. !$#journal Biochem. Biophys. Res. Commun. (1984) 118:103-109 !$#title Human cystatin, a new protein inhibitor of cysteine !1proteinases. !$#cross-references MUID:84128015; PMID:6365094 !$#accession A32732 !'##molecule_type protein !'##residues 27-76 ##label BRZ REFERENCE A60552 !$#authors Olafsson, I.; Gudmundsson, G.; Abrahamson, M.; Jensson, O.; !1Grubb, A. !$#journal Scand. J. Clin. Lab. Invest. (1990) 50:85-93 !$#title The amino terminal portion of cerebrospinal fluid cystatin C !1in hereditary cystatin C amyloid angiopathy is not !1truncated: direct sequence analysis from agarose gel !1electropherograms. !$#cross-references MUID:90193615; PMID:2315647 !$#accession A60552 !'##molecule_type protein !'##residues 27-49,'XX',52-64 ##label OLA !'##note this protein, purified from cerebrospinal fluid of patients !1with the autosomal dominant disease hereditary cystatin C !1amyloid angiopathy (HCCAA), represents the native form; the !1product of the defective gene is not present in CSF but is !1found instead in amyloid deposits REFERENCE S10607 !$#authors Popovic, T.; Brzin, J.; Ritonja, A.; Turk, V. !$#journal Biol. Chem. Hoppe-Seyler (1990) 371:575-580 !$#title Different forms of human cystatin C. !$#cross-references MUID:91025625; PMID:2222856 !$#accession S10607 !'##molecule_type protein !'##residues 27-53 ##label POP !'##experimental_source urine, kidney disease !'##note truncated forms with amino ends at positions 35 and 36 of the !1precursor were also found REFERENCE S01462 !$#authors Grubb, A.; Lofberg, H.; Barrett, A.J. !$#journal FEBS Lett. (1984) 170:370-374 !$#title The disulphide bridges of human cystatin C (gamma-trace) and !1chicken cystatin. !$#contents annotation; disulfide bonds REFERENCE S55305 !$#authors Berti, P.J.; Storer, A.C. !$#journal Biochem. J. (1994) 302:411-416 !$#title Local pH-dependent conformational changes leading to !1proteolytic susceptibility of cystatin C. !$#cross-references MUID:94379969; PMID:8092991 !$#accession S55305 !'##status preliminary !'##molecule_type protein !'##residues 27-49;106-146 ##label BER COMMENT This protein is found in the post-gamma-globulin fraction of !1cerebrospinal fluid, in high concentrations in !1neuroendocrine cells, semen, urine of patients with renal !1failure, and in sera of patients with certain autoimmune !1diseases. COMMENT This protein is an inhibitor of cysteine proteinases and may !1serve an important physiological role as a local regulator !1of this enzymatic activity. COMMENT A mutant cystatin C, with 94-Gln, is deposited in hereditary !1cerebral hermorrhage with amyloidosis. GENETICS !$#gene GDB:CST3 !'##cross-references GDB:119817; OMIM:105150 !$#map_position 20p11.2-20p11.2 !$#introns 81/3; 119/3 CLASSIFICATION #superfamily cystatin; cystatin homology KEYWORDS amyloid; cysteine proteinase inhibitor; extracellular !1protein; hydroxyproline FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-146 #product cystatin C #status experimental #label MAT\ !$35-146 #domain cystatin homology #label CYS\ !$81-85 #region inhibitory #status predicted\ !$29 #modified_site hydroxyproline (Pro) (partial) #status !8experimental\ !$99-109,123-143 #disulfide_bonds #status experimental SUMMARY #length 146 #molecular-weight 15799 #checksum 1457 SEQUENCE /// ENTRY UDBO #type complete TITLE cystatin - bovine ALTERNATE_NAMES thiol proteinase inhibitor ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 06-Dec-1996 ACCESSIONS A01271 REFERENCE A01271 !$#authors Hirado, M.; Tsunasawa, S.; Sakiyama, F.; Niinobe, M.; Fujii, !1S. !$#journal FEBS Lett. (1985) 186:41-45 !$#title Complete amino acid sequence of bovine colostrum low-M-r !1cysteine proteinase inhibitor. !$#cross-references MUID:85231205; PMID:3891407 !$#accession A01271 !'##molecule_type protein !'##residues 1-112 ##label HIR CLASSIFICATION #superfamily cystatin; cystatin homology KEYWORDS colostrum; cysteine proteinase inhibitor FEATURE !$2-112 #domain cystatin homology #label CYS\ !$48-52 #region inhibitory #status predicted\ !$66-76,90-110 #disulfide_bonds #status predicted SUMMARY #length 112 #molecular-weight 12789 #checksum 9113 SEQUENCE /// ENTRY UDHUP1 #type complete TITLE cystatin S precursor - human ALTERNATE_NAMES cystatin SA-III; salivary acidic protein-1 ORGANISM #formal_name Homo sapiens #common_name man DATE 25-Feb-1985 #sequence_revision 08-Feb-1996 #text_change 16-Jul-1999 ACCESSIONS S17667; S16500; A01272; A29603; S19280; A56608 REFERENCE S17667 !$#authors Bobek, L.A.; Aguirre, A.; Levine, M.J. !$#journal Biochem. J. (1991) 278:627-635 !$#title Human salivary cystatin S. Cloning, sequence analysis, !1hybridization in situ and immunocytochemistry. !$#cross-references MUID:91378918; PMID:1898352 !$#accession S17667 !'##molecule_type mRNA !'##residues 1-141 ##label BOB !'##cross-references EMBL:X54667; NID:g30365; PIDN:CAA38478.1; !1PID:g30366 REFERENCE S16500 !$#authors Lamkin, M.S.; Jensen, J.L.; Setayesh, M.R.; Troxler, R.F.; !1Oppenheim, F.G. !$#journal Arch. Biochem. Biophys. (1991) 288:664-670 !$#title Salivary cystatin SA-III, a potential precursor of the !1acquired enamel pellicle, is phosphorylated at both its !1amino- and carboxyl-terminal regions. !$#cross-references MUID:91378515; PMID:1898055 !$#accession S16500 !'##status preliminary !'##molecule_type protein !'##residues 21-134,'D',136-141 ##label IHU REFERENCE A91985 !$#authors Isemura, S.; Saitoh, E.; Sanada, K. !$#journal J. Biochem. (1984) 96:489-498 !$#title Isolation and amino acid sequence of SP-1, an acidic protein !1of human whole saliva, and sequence homology with human !1gamma-trace. !$#cross-references MUID:85054716; PMID:6501254 !$#accession A01272 !'##molecule_type protein !'##residues 29-134,'D',136-141 ##label ISE REFERENCE A91981 !$#authors Isemura, S.; Saitoh, E.; Ito, S.; Isemura, M.; Sanada, K. !$#journal J. Biochem. (1984) 96:1311-1314 !$#title Cystatin S: a cysteine proteinase inhibitor of human saliva. !$#cross-references MUID:85104877; PMID:6394600 !$#contents annotation; inhibitor specificity REFERENCE A29603 !$#authors Hawke, D.H.; Yuan, P.M.; Wilson, K.J.; Hunkapiller, M.W. !$#journal Biochem. Biophys. Res. Commun. (1987) 145:1248-1253 !$#title Identification of a long form of cystatin from human saliva !1by rapid microbore HPLC mapping. !$#cross-references MUID:87270697; PMID:3496880 !$#accession A29603 !'##molecule_type protein !'##residues 21-51 ##label HAW REFERENCE S19279 !$#authors Ramasubbu, N.; Reddy, M.S.; Bergey, E.J.; Haraszthy, G.G.; !1Soni, S.D.; Levine, M.J. !$#journal Biochem. J. (1991) 280:341-352 !$#title Large-scale purification and characterization of the major !1phosphoproteins and mucins of human submandibular-sublingual !1saliva. !$#cross-references MUID:92082469; PMID:1747107 !$#accession S19280 !'##status preliminary !'##molecule_type protein !'##residues 21-55 ##label RAM REFERENCE A56608 !$#authors Johnsson, M.; Richardson, C.F.; Bergey, E.J.; Levine, M.J.; !1Nancollas, G.H. !$#journal Arch. Oral Biol. (1991) 36:631-636 !$#title The effects of human salivary cystatins and statherin on !1hydroxyapatite crystallization. !$#cross-references MUID:92074898; PMID:1741693 !$#accession A56608 !'##molecule_type protein !'##residues 21-36 ##label JOH !'##note sequence extracted from NCBI backbone (NCBIP:67866) !'##note authors desigate form without phosphate as cystatin S and form !1containing one phosphoserine residue as cystatin S1 COMMENT This protein strongly inhibits papain and ficin, partially !1inhibits stem bromelain and bovine cathepsin C, but does not !1inhibit porcine cathepsin B or clostripain. Papain is !1inhibited noncompetitively. GENETICS !$#gene GDB:CST4 !'##cross-references GDB:136381 !$#map_position 20p11.2-20p11.2 CLASSIFICATION #superfamily cystatin; cystatin homology KEYWORDS cysteine proteinase inhibitor; phosphoprotein; saliva FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-141 #product cystatin S #status predicted #label MAT\ !$30-141 #domain cystatin homology #label CYS\ !$76-80 #region inhibitory #status predicted\ !$94-104,118-138 #disulfide_bonds #status predicted SUMMARY #length 141 #molecular-weight 16214 #checksum 8803 SEQUENCE /// ENTRY UDHUP2 #type complete TITLE cystatin SN precursor [validated] - human ALTERNATE_NAMES cystatin SA-I ORGANISM #formal_name Homo sapiens #common_name man DATE 28-May-1986 #sequence_revision 08-Feb-1996 #text_change 08-Dec-2000 ACCESSIONS A28110; S02489; A29632; A01273; S19279 REFERENCE A28110 !$#authors Al-Hashimi, I.; Dickinson, D.P.; Levine, M.J. !$#journal J. Biol. Chem. (1988) 263:9381-9387 !$#title Purification, molecular cloning, and sequencing of salivary !1cystatin SA-I. !$#cross-references MUID:88243825; PMID:2837486 !$#accession A28110 !'##molecule_type mRNA !'##residues 1-141 ##label ALH !'##cross-references GB:J03870; NID:g337751; PIDN:AAA60299.1; !1PID:g337752 REFERENCE S02489 !$#authors Saitoh, E.; Isemura, S.; Sanada, K.; Kim, H.S.; Smithies, !1O.; Maeda, N. !$#journal Biol. Chem. Hoppe-Seyler (1988) 369:191-197 !$#title Cystatin superfamily. Evidence that family II cystatin genes !1are evolutionarily related to family III cystatin genes. !$#cross-references MUID:89076505; PMID:3202964 !$#accession S02489 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 21-141 ##label SA2 REFERENCE A91589 !$#authors Saitoh, E.; Kim, H.S.; Smithies, O.; Maeda, N. !$#journal Gene (1987) 61:329-338 !$#title Human cysteine-proteinase inhibitors: nucleotide sequence !1analysis of three members of the cystatin gene family. !$#cross-references MUID:88185836; PMID:3446578 !$#accession A29632 !'##molecule_type DNA !'##residues 1-86,'I',88-141 ##label SAI REFERENCE A01273 !$#authors Isemura, S.; Saitoh, E.; Sanada, K. !$#journal FEBS Lett. (1986) 198:145-149 !$#title Characterization of a new cysteine proteinase inhibitor of !1human saliva, cystatin SN, which is immunologically related !1to cystatin S. !$#cross-references MUID:86164938; PMID:3514272 !$#accession A01273 !'##molecule_type protein !'##residues 29-141 ##label ISE REFERENCE S19279 !$#authors Ramasubbu, N.; Reddy, M.S.; Bergey, E.J.; Haraszthy, G.G.; !1Soni, S.D.; Levine, M.J. !$#journal Biochem. J. (1991) 280:341-352 !$#title Large-scale purification and characterization of the major !1phosphoproteins and mucins of human submandibular-sublingual !1saliva. !$#cross-references MUID:92082469; PMID:1747107 !$#accession S19279 !'##status preliminary !'##molecule_type protein !'##residues 21-55 ##label RAM COMMENT Human saliva appears to contain several cysteine proteinase !1inhibitors that are immunologically related to cystatin S !1but that differ in their specificity due to amino acid !1sequence differences. Cystatin SN, with a pI of 7.5, is a !1much better inhibitor of papain and dipeptidyl peptidase I !1than is cystatin S, although both inhibit ficin equally !1well. GENETICS !$#gene GDB:CST1 !'##cross-references GDB:119815; OMIM:123855 !$#map_position 20p11.2-20p11.2 CLASSIFICATION #superfamily cystatin; cystatin homology KEYWORDS cysteine proteinase inhibitor; extracellular protein; saliva FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-141 #product cystatin SA-I #status experimental #label !8MAT1\ !$29-141 #product cystatin SN #status experimental #label !8MAT2\ !$30-141 #domain cystatin homology #label CYS\ !$76-80 #region inhibitory #status predicted\ !$94-104,118-138 #disulfide_bonds #status predicted SUMMARY #length 141 #molecular-weight 16361 #checksum 447 SEQUENCE /// ENTRY JC2040 #type complete TITLE cystatin - chum salmon ALTERNATE_NAMES cysteine proteinase inhibitor ORGANISM #formal_name Oncorhynchus keta #common_name chum salmon DATE 14-Jul-1994 #sequence_revision 14-Jul-1994 #text_change 16-Jul-1999 ACCESSIONS JC2040 REFERENCE JC2040 !$#authors Koide, Y.; Noso, T. !$#journal Biosci. Biotechnol. Biochem. (1994) 58:164-169 !$#title The complete amino acid sequence of pituitary cystatin from !1chum salmon. !$#cross-references MUID:94162738; PMID:7764512 !$#accession JC2040 !'##molecule_type protein !'##residues 1-111 ##label KOI COMMENT The intracellular role of this protein is the inhibition of !1intralysosomal proteolysis by cysteine endoproteinases. CLASSIFICATION #superfamily cystatin; cystatin homology KEYWORDS cysteine proteinase inhibitor FEATURE !$2-111 #domain cystatin homology #label CYS\ !$48-52 #region inhibitory\ !$89-109 #disulfide_bonds #status experimental SUMMARY #length 111 #molecular-weight 12425 #checksum 2658 SEQUENCE /// ENTRY UDCH #type complete TITLE cystatin precursor - chicken ALTERNATE_NAMES cystatin 1; cysteine proteinase inhibitor; egg-white cystatin ORGANISM #formal_name Gallus gallus #common_name chicken DATE 03-Aug-1984 #sequence_revision 12-Apr-1996 #text_change 29-Oct-1999 ACCESSIONS A34456; A01274; S01461; S48159; S04008; JN0789 REFERENCE A34456 !$#authors Colella, R.; Sakaguchi, Y.; Nagase, H.; Bird, J.W.C. !$#journal J. Biol. Chem. (1989) 264:17164-17169 !$#title Chicken egg white cystatin. Molecular cloning, nucleotide !1sequence, and tissue distribution. !$#cross-references MUID:90008873; PMID:2793849 !$#accession A34456 !'##molecule_type mRNA !'##residues 1-139 ##label COL !'##cross-references GB:J05077; NID:g211714; PIDN:AAA48744.1; !1PID:g211715 REFERENCE A01274 !$#authors Schwabe, C.; Anastasi, A.; Crow, H.; McDonald, J.K.; !1Barrett, A.J. !$#journal Biochem. J. (1984) 217:813-817 !$#title Cystatin. Amino acid sequence and possible secondary !1structure. !$#cross-references MUID:84178305; PMID:6712597 !$#accession A01274 !'##molecule_type protein !'##residues 24-139 ##label SCH REFERENCE S01461 !$#authors Turk, V.; Brzin, J.; Longer, M.; Ritonja, A.; Eropkin, M.; !1Borchart, U.; Machleidt, W. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1983) 364:1487-1496 !$#title Protein inhibitors of cysteine proteinases. III. Amino-acid !1sequence of cystatin from chicken egg white. !$#cross-references MUID:84110059; PMID:6662498 !$#accession S01461 !'##molecule_type protein !'##residues 24-139 ##label TUR REFERENCE A37514 !$#authors Anastasi, A.; Brown, M.A.; Kembhavi, A.A.; Nicklin, M.J.H.; !1Sayers, C.A.; Sunter, D.C.; Barrett, A.J. !$#journal Biochem. J. (1983) 211:129-138 !$#title Cystatin, a protein inhibitor of cysteine proteinases. !1Improved purification from egg white, characterization, and !1detection in chicken serum. !$#cross-references MUID:83256421; PMID:6409085 !$#contents annotation; characterization of protein REFERENCE S01462 !$#authors Grubb, A.; Lofberg, H.; Barrett, A.J. !$#journal FEBS Lett. (1984) 170:370-374 !$#title The disulphide bridges of human cystatin C (gamma-trace) and !1chicken cystatin. !$#contents annotation; disulfide bonds REFERENCE S48159 !$#authors Auerswald, E.A.; Naegler, D.K.; Schulze, A.J.; Engh, R.A.; !1Genenger, G.; Machleidt, W.; Fritz, H. !$#journal Eur. J. Biochem. (1994) 224:407-415 !$#title Production, inhibitory activity, folding and conformational !1analysis of an N-terminal and an internal deletion variant !1of chicken cystatin. !$#cross-references MUID:95010016; PMID:7925354 !$#accession S48159 !'##status preliminary !'##molecule_type protein !'##residues 24-139 ##label AUE REFERENCE S04008 !$#authors Laber, B.; Krieglstein, K.; Henschen, A.; Kos, J.; Turk, V.; !1Huber, R.; Bode, W. !$#journal FEBS Lett. (1989) 248:162-168 !$#title The cysteine proteinase inhibitor chicken cystatin is a !1phosphoprotein. !$#cross-references MUID:89252033; PMID:2721673 !$#accession S04008 !'##molecule_type protein !'##residues 97-114 ##label LAB REFERENCE JN0789 !$#authors Colella, R.; Bird, J.W.C. !$#journal Gene (1993) 130:175-181 !$#title Isolation and characterization of the chicken !1cystatin-encoding gene: Mapping transcription start point !1and polyadenylation sites. !$#cross-references MUID:93366172; PMID:8359684 !$#accession JN0789 !'##molecule_type DNA !'##residues 1-139 ##label CO2 !'##cross-references GB:M95725 !'##note authors failed to translate the codon for residue 115-Tyr COMMENT This protein binds tightly to and inhibits a variety of !1cysteine proteinases including ficin, papain, and cathepsins !1B, C, H, and L. It is present in both egg white and serum. GENETICS !$#gene Csn !$#introns 76/3; 114/3 CLASSIFICATION #superfamily cystatin; cystatin homology KEYWORDS cysteine proteinase inhibitor; egg white; phosphoprotein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-139 #product cystatin, long form #status experimental !8#label CYLF\ !$30-139 #domain cystatin homology #label CYS\ !$32-139 #product cystatin, short form #status experimental !8#label CYSF\ !$76-80 #region inhibitory #status predicted\ !$94-104,118-138 #disulfide_bonds #status experimental\ !$103 #binding_site phosphate (Ser) (covalent) (partial) !8#status experimental SUMMARY #length 139 #molecular-weight 15287 #checksum 4441 SEQUENCE /// ENTRY UDRTS2 #type complete TITLE cystatin A [validated] - rat ALTERNATE_NAMES cystatin alpha; epidermal stefin; epidermal thiol proteinase inhibitor ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 18-Aug-2000 ACCESSIONS A01275; S10952 REFERENCE A01275 !$#authors Takio, K.; Kominami, E.; Bando, Y.; Katunuma, N.; Titani, K. !$#journal Biochem. Biophys. Res. Commun. (1984) 121:149-154 !$#title Amino acid sequence of rat epidermal thiol proteinase !1inhibitor. !$#cross-references MUID:84231334; PMID:6732797 !$#accession A01275 !'##molecule_type protein !'##residues 1-103 ##label TAK REFERENCE S10952 !$#authors Takeda, A.; Nakamura, Y.; Kaji, H.; Samejima, T. !$#journal Biol. Chem. Hoppe-Seyler (1990) 371:233-238 !$#title Evidence of protease activity producing NH(2)-terminal !1truncated form of rat cystatin A in newborn rat epidermis. !$#cross-references MUID:90380288; PMID:2205237 !$#accession S10952 !'##molecule_type protein !'##residues 7-10 ##label BIO CLASSIFICATION #superfamily cystatin; cystatin homology KEYWORDS acetylated amino end; cysteine proteinase inhibitor FEATURE !$8-103 #domain cystatin homology #label CYS\ !$52-56 #region inhibitory #status predicted\ !$1 #modified_site acetylated amino end (Met) #status !8experimental SUMMARY #length 103 #molecular-weight 11563 #checksum 9159 SEQUENCE /// ENTRY UDHUS #type complete TITLE cystatin A - human ALTERNATE_NAMES stefin A ORGANISM #formal_name Homo sapiens #common_name man DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 16-Jul-1999 ACCESSIONS A29139; A01276; JX0077; B54327; S51189 REFERENCE A29139 !$#authors Kartasova, T.; Cornelissen, B.J.C.; Belt, P.; van de Putte, !1P. !$#journal Nucleic Acids Res. (1987) 15:5945-5962 !$#title Effects of UV, 4-NQO and TPA on gene expression in cultured !1human epidermal keratinocytes. !$#cross-references MUID:87316861; PMID:2442723 !$#accession A29139 !'##molecule_type mRNA !'##residues 1-98 ##label KAR !'##cross-references GB:X05978; NID:g30374; PIDN:CAA29398.1; PID:g30375 REFERENCE A01276 !$#authors Machleidt, W.; Borchart, U.; Fritz, H.; Brzin, J.; Ritonja, !1A.; Turk, V. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1983) 364:1481-1486 !$#title Protein inhibitors of cysteine proteinases. II. Primary !1structure of stefin, a cytosolic protein inhibitor of !1cysteine proteinases from human polymorphonuclear !1granulocytes. !$#cross-references MUID:84110058; PMID:6689312 !$#accession A01276 !'##molecule_type protein !'##residues 1-98 ##label MAC REFERENCE JX0077 !$#authors Takeda, A.; Kaji, H.; Nakaya, K.; Nakamura, Y.; Samejima, T. !$#journal J. Biochem. (1989) 105:986-991 !$#title Comparative studies on the primary structure of human !1cystatin As from epidermis, liver, spleen, and leukocytes. !$#cross-references MUID:89359227; PMID:2768224 !$#accession JX0077 !'##molecule_type protein !'##residues 2-98 ##label TAK !'##note the sequence of epidermal cystatin A is identical with those !1isolated from liver, spleen, and leukocytes except for the !1lack of an amino-terminal methionine residue REFERENCE A54327 !$#authors Madsen, P.; Rasmussen, H.H.; Leffers, H.; Honore, B.; !1Dejgaard, K.; Olsen, E.; Kiil, J.; Walbum, E.; Andersen, !1A.H.; Basse, B.; Lauridsen, J.B.; Ratz, G.P.; Celis, A.; !1Vandekerckhove, J.; Celis, J.E. !$#journal J. Invest. Dermatol. (1991) 97:701-712 !$#title Molecular cloning, occurrence, and expression of a novel !1partially secreted protein "psoriasin" that is highly !1up-regulated in psoriatic skin. !$#cross-references MUID:92043866; PMID:1940442 !$#accession B54327 !'##molecule_type protein !'##residues 72-82,'XX',85 ##label MAD REFERENCE S51189 !$#authors Martin, J.R.; Jerala, R.; Kroon-Zitko, L.; Zerovnik, E.; !1Turk, V.; Waltho, J.P. !$#journal Eur. J. Biochem. (1994) 225:1181-1194 !$#title Structural characterisation of human stefin A in solution !1and implications for binding to cysteine proteinases. !$#cross-references MUID:95045548; PMID:7957209 !$#contents annotation; NMR structure COMMENT This intracellular thiol proteinase inhibitor, isolated from !1the cytosol of human granulocytes, is unusual in that it !1lacks cysteine residues. GENETICS !$#gene GDB:CSTA; STFA; STF1 !'##cross-references GDB:128150; OMIM:184600 !$#map_position 3q13-3q13 CLASSIFICATION #superfamily cystatin; cystatin homology KEYWORDS cysteine proteinase inhibitor FEATURE !$2-98 #domain cystatin homology #label CYS\ !$46-50 #region inhibitory #status predicted SUMMARY #length 98 #molecular-weight 11006 #checksum 4593 SEQUENCE /// ENTRY UDRTS #type complete TITLE cystatin beta - rat ALTERNATE_NAMES hepatic thiol proteinase inhibitor; stefin, hepatic ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 16-Jun-2000 ACCESSIONS JC1128; S12694; A01277 REFERENCE JC1128 !$#authors Sato, N.; Ishidoh, K.; Uchiyama, Y.; Kominami, E. !$#journal Gene (1992) 114:257-260 !$#title Structural organization of the gene encoding rat cystatin !1beta. !$#cross-references MUID:92290285; PMID:1601307 !$#accession JC1128 !'##molecule_type DNA !'##residues 1-98 ##label SAT1 !'##cross-references GB:D10607; DDBJ:D90542; NID:g220725; !1PIDN:BAA01462.1; PID:g220726 REFERENCE S12694 !$#authors Sato, N.; Ishidoh, K.; Uchiyama, Y.; Kominami, E. !$#journal Nucleic Acids Res. (1990) 18:6698 !$#title Molecular cloning and sequencing of cDNA for rat cystatin !1beta. !$#cross-references MUID:91067472; PMID:2251135 !$#accession S12694 !'##molecule_type mRNA !'##residues 1-98 ##label SAT2 !'##cross-references EMBL:X54737; NID:g55891; PIDN:CAA38534.1; !1PID:g55892 REFERENCE A01277 !$#authors Takio, K.; Kominami, E.; Wakamatsu, N.; Katunuma, N.; !1Titani, K. !$#journal Biochem. Biophys. Res. Commun. (1983) 115:902-908 !$#title Amino acid sequence of rat liver thiol proteinase inhibitor. !$#cross-references MUID:84023871; PMID:6626228 !$#accession A01277 !'##molecule_type protein !'##residues 1-98 ##label TAK GENETICS !$#gene cy-beta !$#introns 22/3; 56/3 CLASSIFICATION #superfamily cystatin; cystatin homology KEYWORDS acetylated amino end; cysteine proteinase inhibitor FEATURE !$2-98 #domain cystatin homology #label CYS\ !$46-50 #region inhibitory #status predicted\ !$1 #modified_site acetylated amino end (Met) #status !8experimental SUMMARY #length 98 #molecular-weight 11196 #checksum 1448 SEQUENCE /// ENTRY UDHUB #type complete TITLE cystatin B - human ALTERNATE_NAMES CPI-B; hepatic thiol proteinase inhibitor; stefin, hepatic ORGANISM #formal_name Homo sapiens #common_name man DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 24-Nov-1999 ACCESSIONS A01278 REFERENCE A01278 !$#authors Ritonja, A.; Machleidt, W.; Barrett, A.J. !$#journal Biochem. Biophys. Res. Commun. (1985) 131:1187-1192 !$#title Amino acid sequence of the intracellular cysteine proteinse !1inhibitor cystatin B from human liver. !$#cross-references MUID:86025583; PMID:3902020 !$#accession A01278 !'##molecule_type protein !'##residues 1-98 ##label RIT COMMENT This protein is able to form dimers stabilized by !1noncovalent forces. GENETICS !$#gene GDB:CSTB; STFB; EPM1; CST6; PME !'##cross-references GDB:5215249; OMIM:254800; OMIM:601145 !$#map_position 21q22.3-21q22.3 !$#note defects in this gene cause progressive myoclonic 1 !1(Unverricht-Lundborg type) epilepsy CLASSIFICATION #superfamily cystatin; cystatin homology KEYWORDS blocked amino end; cysteine proteinase inhibitor FEATURE !$2-98 #domain cystatin homology #label CYS\ !$46-50 #region inhibitory #status predicted\ !$1 #modified_site blocked amino end (Met) (probably !8acetylated) #status experimental SUMMARY #length 98 #molecular-weight 11174 #checksum 4066 SEQUENCE /// ENTRY TIAC #type complete TITLE trypsin inhibitor - common roundworm (tentative sequence) ORGANISM #formal_name Ascaris lumbricoides #common_name common roundworm DATE 23-Oct-1981 #sequence_revision 23-Oct-1981 #text_change 31-Mar-2000 ACCESSIONS A01288 REFERENCE A90573 !$#authors Fraefel, W.; Acher, R. !$#journal Biochim. Biophys. Acta (1968) 154:615-617 !$#title The amino acid sequence of a trypsin inhibitor isolated from !1ascaris (Ascaris lumbricoides var. suum). !$#cross-references MUID:68240446; PMID:5650426 !$#accession A01288 !'##molecule_type protein !'##residues 1-66 ##label FRA REFERENCE A94451 !$#authors Induni, A. !$#citation Ph.D. thesis, University of Freiburg, Switzerland, 1969, !1cited by Kassell, B., Methods Enzymol. 19, 872-883, 1970 !$#description [66e] proteolytic enzyme inhibitors from Ascaris !1lumbricoides. !$#contents annotation; disulfide bonds CLASSIFICATION #superfamily roundworm trypsin inhibitor KEYWORDS serine proteinase inhibitor FEATURE !$5-28,16-44,19-58, !$21-38,43-64 #disulfide_bonds #status experimental SUMMARY #length 66 #molecular-weight 7194 #checksum 7211 SEQUENCE /// ENTRY A42207 #type complete TITLE hirudin P6 - leech (Hirudinaria manillensis) ORGANISM #formal_name Hirudinaria manillensis DATE 31-Dec-1993 #sequence_revision 01-Dec-1995 #text_change 04-Oct-1996 ACCESSIONS A42207 REFERENCE A42207 !$#authors Steiner, V.; Knecht, R.; Bornsen, K.O.; Gassmann, E.; Stone, !1S.R.; Raschdorf, F.; Schlaeppi, J.M.; Maschler, R. !$#journal Biochemistry (1992) 31:2294-2298 !$#title Primary structure and function of novel O-glycosylated !1hirudins from the leech Hirudinaria manillensis. !$#cross-references MUID:92172851; PMID:1540584 !$#accession A42207 !'##molecule_type protein !'##residues 1-63 ##label STE !'##note sequence extracted from NCBI backbone (NCBIP:87044) CLASSIFICATION #superfamily thrombin inhibitor KEYWORDS anticoagulant; glycoprotein; salivary gland; serine !1proteinase inhibitor; sulfoprotein FEATURE !$43 #binding_site carbohydrate (Thr) (covalent) #status !8experimental\ !$61 #binding_site sulfate (Tyr) (covalent) #status !8experimental SUMMARY #length 63 #molecular-weight 6977 #checksum 5028 SEQUENCE /// ENTRY HULXH #type complete TITLE thrombin inhibitor (hirudin) - medicinal leech ORGANISM #formal_name Hirudo medicinalis #common_name medicinal leech DATE 30-Nov-1980 #sequence_revision 03-Aug-1984 #text_change 07-May-1999 ACCESSIONS A91318; A94429; A60811; A01289 REFERENCE A91318 !$#authors Dodt, J.; Muller, H.P.; Seemuller, U.; Chang, J.Y. !$#journal FEBS Lett. (1984) 165:180-183 !$#title The complete amino acid sequence of hirudin, a thrombin !1specific inhibitor. Application of colour !1carboxymethylation. !$#accession A91318 !'##molecule_type protein !'##residues 1-65 ##label DOD REFERENCE A94429 !$#authors Petersen, T.E.; Roberts, H.R.; Sottrup-Jensen, L.; !1Magnusson, S.; Bagdy, D. !$#book Protides of the Biological Fluids, Proc. 23rd Colloq., !1Peeters, H., ed., pp.145-149, Pergamon Press, New York, 1976 !$#accession A94429 !'##molecule_type protein !'##residues 1-65 ##label PET REFERENCE A60811 !$#authors Mao, S.J.T.; Yates, M.T.; Blankenship, D.T.; Cardin, A.D.; !1Krstenansky, J.L.; Lovenberg, W.; Jackson, R.L. !$#journal Anal. Biochem. (1987) 161:514-518 !$#title Rapid purification and revised amino-terminal sequence of !1hirudin: a specific thrombin inhibitor of the bloodsucking !1leech. !$#cross-references MUID:87211066; PMID:3578808 !$#accession A60811 !'##molecule_type protein !'##residues 1-32,'N',34-43 ##label MAO !'##note the authors suggest that their identification of 33-Asn is !1correct and that 33-Asp found in reference A91318 resulted !1from artifactual deamination during isolation; the !1difference may also represent a natural variant of hirudin COMMENT Hirudin is a potent thrombin-specific protease inhibitor. CLASSIFICATION #superfamily thrombin inhibitor KEYWORDS anticoagulant; sulfoprotein FEATURE !$6-14,16-28,22-39 #disulfide_bonds #status experimental\ !$63 #binding_site sulfate (Tyr) (covalent) #status !8experimental SUMMARY #length 65 #molecular-weight 6970 #checksum 6368 SEQUENCE /// ENTRY HULXLM #type complete TITLE hirullin P18 - leech (Hirudinaria manillensis) ALTERNATE_NAMES hirudin-related protein P18; thrombin inhibitor hirullin P18 ORGANISM #formal_name Hirudinaria manillensis DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 31-Mar-2000 ACCESSIONS S11341; S12991; B42207 REFERENCE S11341 !$#authors Krstenansky, J.L.; Owen, T.J.; Yates, M.T.; Mao, S.J.T. !$#journal FEBS Lett. (1990) 269:425-429 !$#title The C-terminal binding domain of hirullin P18. Antithrombin !1activity and comparison to hirudin peptides. !$#cross-references MUID:90382592; PMID:2401369 !$#accession S11341 !'##molecule_type protein !'##residues 1-29,31-62 ##label KRS1 !'##note this sequence has been revised in reference S12991 REFERENCE S12991 !$#authors Krstenansky, J.L.; Owen, T.J.; Yates, M.T.; Mao, S.J.T. !$#journal FEBS Lett. (1990) 276:232A !$#title Corrigendum. The C-terminal binding domain of hirullin P18: !1antithrombin activity and comparison to hirudin peptides. !$#accession S12991 !'##molecule_type protein !'##residues 30 ##label KRS2 REFERENCE A42207 !$#authors Steiner, V.; Knecht, R.; Bornsen, K.O.; Gassmann, E.; Stone, !1S.R.; Raschdorf, F.; Schlaeppi, J.M.; Maschler, R. !$#journal Biochemistry (1992) 31:2294-2298 !$#title Primary structure and function of novel O-glycosylated !1hirudins from the leech Hirudinaria manillensis. !$#cross-references MUID:92172851; PMID:1540584 !$#accession B42207 !'##molecule_type protein !'##residues 1-62 ##label STE !'##cross-references PIDN:AAB21616.1; PID:g246532 !'##note sequence extracted from NCBI backbone (NCBIP:87046) !'##note the single glycosylated residue was identified as !1Fuc-GalBeta1-3GalNAc-(O-threonine) at position 46; this !1protein does not contain a sulfated tyrosine residue CLASSIFICATION #superfamily thrombin inhibitor KEYWORDS anticoagulant; glycoprotein; salivary gland; serine !1proteinase inhibitor FEATURE !$6-13,15-26,20-35 #disulfide_bonds #status predicted\ !$46 #binding_site carbohydrate (Thr) (covalent) #status !8experimental SUMMARY #length 62 #molecular-weight 6693 #checksum 4705 SEQUENCE /// ENTRY EILXCH #type complete TITLE eglin C - medicinal leech ORGANISM #formal_name Hirudo medicinalis #common_name medicinal leech DATE 01-Sep-1981 #sequence_revision 02-Apr-1982 #text_change 16-Aug-1996 ACCESSIONS A94592; A01290 REFERENCE A94592 !$#authors Fritz, H.; Seemuller, U. !$#submission submitted to the Atlas, March 1982 !$#accession A94592 !'##molecule_type protein !'##residues 1-70 ##label FRI REFERENCE A91689 !$#authors Seemuller, U.; Eulitz, M.; Fritz, H.; Strobl, A. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1980) 361:1841-1846 !$#title Structure of the elastase-cathepsin G inhibitor of the leech !1Hirudo medicinalis. !$#cross-references MUID:81115825; PMID:6906312 !$#contents annotation; sequence COMMENT Eglins are protease inhibitors that form strong complexes !1with elastase and cathepsin G. CLASSIFICATION #superfamily eglin C KEYWORDS serine proteinase inhibitor FEATURE !$45 #inhibitory_site Leu (elastase, cathepsin G) #status !8experimental SUMMARY #length 70 #molecular-weight 8091 #checksum 8300 SEQUENCE /// ENTRY TIPO1A #type complete TITLE chymotrypsin inhibitor I chain A - potato ORGANISM #formal_name Solanum tuberosum #common_name potato DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 07-May-1999 ACCESSIONS A01291 REFERENCE A91417 !$#authors Richardson, M.; Cossins, L. !$#journal FEBS Lett. (1975) 52:161 !$#contents corrigendum !$#accession A01291 !'##molecule_type protein !'##residues 1-70 ##label RIC !'##note a 13-residue segment originally placed between positions 45 and !146 was found to be a slightly polymorphic form of residues !158-70 REFERENCE A90271 !$#authors Richardson, M. !$#journal Biochem. J. (1974) 137:101-112 !$#title Chymotryptic inhibitor I from potatoes. The amino acid !1sequence of subunit A. !$#cross-references MUID:74140203; PMID:4595280 !$#contents annotation !$#note this sequence has been revised in reference A91417 REFERENCE A94581 !$#authors Richardson, M. !$#submission submitted to the Atlas, June 1975 !$#contents annotation; microheterogeneity !$#note 46-Leu, 62-Asn, 66-Leu, 68-Val, 69-Leu, and 70-Gly are also !1found COMMENT The native inhibitor occurs as heterogeneous tetramers of !1similar chains. It inhibits both chymotrypsin and trypsin. CLASSIFICATION #superfamily eglin C KEYWORDS serine proteinase inhibitor SUMMARY #length 70 #molecular-weight 7905 #checksum 3748 SEQUENCE /// ENTRY EIBH2A #type complete TITLE subtilisin/chymotrypsin inhibitor 2A - barley ALTERNATE_NAMES subtilisin/chymotrypsin inhibitor CI-2 ORGANISM #formal_name Hordeum vulgare #common_name barley DATE 18-Dec-1981 #sequence_revision 05-Jan-1996 #text_change 24-Nov-1999 ACCESSIONS A01292; A29537 REFERENCE A90761 !$#authors Svendsen, I.; Martin, B.; Jonassen, I. !$#journal Carlsberg Res. Commun. (1980) 45:79-85 !$#title Characteristics of Hiproly barley III. Amino acid sequences !1of two lysine-rich proteins. !$#accession A01292 !'##molecule_type protein !'##residues 'ZVSS',6-84 ##label SVE REFERENCE A29537 !$#authors Williamson, M.S.; Forde, J.; Buxton, B.; Kreis, M. !$#journal Eur. J. Biochem. (1987) 165:99-106 !$#title Nucleotide sequence of barley chymotrypsin inhibitor-2 !1(CI-2) and its expression in normal and high-lysine barley. !$#cross-references MUID:87190479; PMID:3106042 !$#accession A29537 !'##molecule_type mRNA !'##residues 'MTVQDLTVTSAIXSVSQEASVTR',1-84 ##label WIL !'##cross-references EMBL:X05404 !'##experimental_source endosperm, cvs. Sundance and Hiproly !'##note the authors propose that the first initiation site is used, !1that the ochre stop codon (indicated by an 'X') is read !1through, and that a signal peptide is cleaved after 22-Thr !1in this alternative sequence REFERENCE A90764 !$#authors Jonassen, I.; Svendsen, I. !$#journal Carlsberg Res. Commun. (1982) 47:199-203 !$#title Identification of the reactive sites in two homologous !1serine proteinase inhibitors isolated from barley. !$#contents annotation; inhibitory site COMMENT This inhibitor is related to inhibitor CI-1 from barley, to !1chymotrypsin inhibitor I from potato, and to eglin C from !1leech. CLASSIFICATION #superfamily eglin C KEYWORDS blocked amino end; serine proteinase inhibitor FEATURE !$2 #modified_site blocked amino end (Ser) (in mature !8form) (probably acetylated) #status experimental\ !$60 #inhibitory_site Met (chymotrypsin, subtilisin) !8#status experimental SUMMARY #length 84 #molecular-weight 9381 #checksum 5172 SEQUENCE /// ENTRY S61830 #type complete TITLE subtilisin/chymotrypsin inhibitor - maize ALTERNATE_NAMES proteinase inhibitor ORGANISM #formal_name Zea mays #common_name maize DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S61830; S65863; S60458; S37493; S44238; S49477 REFERENCE S61830 !$#authors Cordero, M.J.; Raventos, D.; San Segundo, B. !$#journal Plant J. (1994) 6:141-150 !$#title Expression of a maize proteinase inhibitor gene is induced !1in response to wounding and fungal infection: systemic !1wound-response of a monocot gene. !$#cross-references MUID:95004658; PMID:7920708 !$#accession S61830 !'##molecule_type DNA !'##residues 1-73 ##label COR !'##cross-references EMBL:X78988; NID:g475252; PIDN:CAA55588.1; !1PID:g475253 !$#accession S65863 !'##molecule_type mRNA !'##residues 1-73 ##label COW !'##cross-references EMBL:X69972; NID:g474945; PIDN:CAA49593.1; !1PID:g475922 REFERENCE S60453 !$#authors Chevalier, C.; Bourgeois, E.; Pradet, A.; Raymond, P. !$#journal Plant Mol. Biol. (1995) 28:473-485 !$#title Molecular cloning and characterization of six cDNAs !1expressed during glucose starvation in excised maize (Zea !1mays L.) root tips. !$#cross-references MUID:95359405; PMID:7632917 !$#accession S60458 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type mRNA !'##residues 1-73 ##label CHE !'##cross-references EMBL:X82187; NID:g559537; PIDN:CAA57677.1; !1PID:g559538 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1994 CLASSIFICATION #superfamily eglin C KEYWORDS serine proteinase inhibitor SUMMARY #length 73 #molecular-weight 7605 #checksum 7995 SEQUENCE /// ENTRY EIBH1C #type complete TITLE subtilisin/chymotrypsin inhibitor CI-1 - barley (tentative sequence) ORGANISM #formal_name Hordeum vulgare #common_name barley DATE 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 31-Mar-2000 ACCESSIONS A01293 REFERENCE A90765 !$#authors Svendsen, I.; Boisen, S.; Hejgaard, J. !$#journal Carlsberg Res. Commun. (1982) 47:45-53 !$#title Amino acid sequence of serine protease inhibitor CI-1 from !1barley. Homology with barley inhibitor CI-2, potato !1inhibitor I, and leech eglin. !$#accession A01293 !'##molecule_type protein !'##residues 1-77 ##label SVE REFERENCE A90764 !$#authors Jonassen, I.; Svendsen, I. !$#journal Carlsberg Res. Commun. (1982) 47:199-203 !$#title Identification of the reactive sites in two homologous !1serine proteinase inhibitors isolated from barley. !$#contents annotation; reactive site !$#note Leu-53 is the site of interaction with chymotrypsin. Leu-53 !1and Met-24 are the sites of interaction with subtilisin COMMENT This inhibitor is related to inhibitor CI-2 from barley, to !1chymotrypsin inhibitor I from potato, and to eglin C from !1leech. CLASSIFICATION #superfamily eglin C KEYWORDS serine proteinase inhibitor SUMMARY #length 77 #molecular-weight 8258 #checksum 2117 SEQUENCE /// ENTRY TISYO #type complete TITLE proteinase inhibitor (Bowman-Birk) D-II precursor (clone pB2) - soybean ORGANISM #formal_name Glycine max #common_name soybean DATE 24-Apr-1984 #sequence_revision 12-Apr-1996 #text_change 18-Jun-1999 ACCESSIONS JC2226; A01294; B22636; S29607 REFERENCE JC2224 !$#authors Baek, J.M.; Song, J.C.; Choi, Y.D.; Kim, S.I. !$#journal Biosci. Biotechnol. Biochem. (1994) 58:843-846 !$#title Nucleotide sequence homology of cDNAs encoding soybean !1Bowman-Birk type proteinase inhibitor and its isoinhibitors. !$#cross-references MUID:94289861; PMID:7764974 !$#accession JC2226 !'##molecule_type mRNA !'##residues 1-110 ##label BAE !'##cross-references EMBL:X68704; NID:g18540; PIDN:CAA48655.1; !1PID:g18541 REFERENCE A91928 !$#authors Odani, S.; Ikenaka, T. !$#journal J. Biochem. (1972) 71:839-848 !$#title Studies on soybean trypsin inhibitors. IV. Complete amino !1acid sequence and the anti-proteinase sites of Bowman-Birk !1soybean proteinase inhibitor. !$#cross-references MUID:73009156; PMID:4672481 !$#accession A01294 !'##molecule_type protein !'##residues 40-110 ##label ODA REFERENCE A92489 !$#authors Hammond, R.W.; Foard, D.E.; Larkins, B.A. !$#journal J. Biol. Chem. (1984) 259:9883-9890 !$#title Molecular cloning and analysis of a gene coding for the !1Bowman-Birk protease inhibitor in soybean. !$#cross-references MUID:84264652; PMID:6086657 !$#contents annotation !$#note the sequence has been revised in reference A92540 REFERENCE A92540 !$#authors Hammond, R.W.; Foard, D.E.; Larkins, B.A. !$#journal J. Biol. Chem. (1985) 260:7806 !$#contents erratum !$#accession B22636 !'##molecule_type mRNA !'##residues 69-110 ##label HAM REFERENCE A91931 !$#authors Odani, S.; Ikenaka, T. !$#journal J. Biochem. (1973) 74:697-715 !$#title Studies on soybean trypsin inhibitors. VIII. Disulfide !1bridges in soybean Bowman-Birk proteinase inhibitor. !$#cross-references MUID:74055989; PMID:4797072 !$#contents annotation; disulfide bonds REFERENCE A91932 !$#authors Odani, S.; Ikenaka, T. !$#journal J. Biochem. (1973) 74:857-860 !$#title Scission of soybean Bowman-Birk proteinase inhibitor into !1two small fragments having either trypsin or chymotrypsin !1inhibitory activity. !$#cross-references MUID:74056007; PMID:4797073 !$#contents annotation !$#note the protein can be cleaved with pepsin and cyanogen bromide !1into a fragment consisting of residues 40-66 and 96-106 !1(held together by four disulfide bonds), which inhibits !1trypsin, and a second fragment consisting of residues 67-95, !1which inhibits chymotrypsin COMMENT This protein regulates endogeneous proteinase during !1germination, stores sulfur amino acids during dormancy, and !1protects the plant from insects and microorganisms. CLASSIFICATION #superfamily Bowman-Birk proteinase inhibitor; Bowman-Birk !1inhibitor repeat homology KEYWORDS duplication; seed; serine proteinase inhibitor FEATURE !$1-39 #domain signal sequence #status predicted #label SIG\ !$40-105 #product Bowman-Birk proteinase isoinhibitor D-II !8#status predicted #label MAT\ !$48-74 #domain Bowman-Birk inhibitor repeat homology #label !8BB1\ !$75-100 #domain Bowman-Birk inhibitor repeat homology #label !8BB2\ !$47-101,48-63,51-97, !$53-61,71-78,75-90, !$80-88 #disulfide_bonds #status experimental\ !$55 #inhibitory_site Lys (trypsin) #status experimental\ !$82 #inhibitory_site Leu (chymotrypsin) #status !8experimental SUMMARY #length 110 #molecular-weight 12092 #checksum 402 SEQUENCE /// ENTRY TILI #type complete TITLE proteinase inhibitor (Bowman-Birk) - lima bean (tentative sequence) ORGANISM #formal_name Phaseolus lunatus #common_name lima bean DATE 30-Nov-1980 #sequence_revision 30-Nov-1980 #text_change 31-Mar-2000 ACCESSIONS A01295 REFERENCE A01295 !$#authors Stevens, F.C.; Wuerz, S.; Krahn, J. !$#book Proteinase Inhibitors (Bayer-Symp. V), Fritz, H., Tschesche, !1H., Greene, L.J., and Truscheit, E., eds., pp.344-354, !1Springer-Verlag, Berlin, 1974 !$#title Structure-function relationships in lima bean protease !1inhibitor. !$#accession A01295 !'##molecule_type protein !'##residues 1-83 ##label STE !'##note several variants were isolated from a commercial lima bean !1preparation. Some lacked 8, 12, or 14 amino-terminal !1residues and 2 carboxyl-terminal residues. 23-Leu, 35-Ser, !137-Phe, 47-Glx, 53-Phe, 62-Thr, and 65-Thr were also found CLASSIFICATION #superfamily Bowman-Birk proteinase inhibitor; Bowman-Birk !1inhibitor repeat homology KEYWORDS duplication; serine proteinase inhibitor FEATURE !$19-45 #domain Bowman-Birk inhibitor repeat homology #label !8BB1\ !$46-71 #domain Bowman-Birk inhibitor repeat homology #label !8BB2\ !$18-72,19-34,22-68, !$24-32,42-49,46-61, !$51-59 #disulfide_bonds #status predicted\ !$26 #inhibitory_site Lys (trypsin) #status predicted\ !$53 #inhibitory_site Leu (chymotrypsin) #status predicted SUMMARY #length 83 #molecular-weight 9079 #checksum 9891 SEQUENCE /// ENTRY TIAM3 #type complete TITLE proteinase inhibitor (Bowman-Birk) DE-3 - Macrotyloma axillare ORGANISM #formal_name Macrotyloma axillare DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 31-Dec-1993 ACCESSIONS A01296 REFERENCE A91257 !$#authors Joubert, F.J.; Kruger, H.; Townshend, G.S.; Botes, D.P. !$#journal Eur. J. Biochem. (1979) 97:85-91 !$#title Purification, some properties and the complete primary !1structures of two protease inhibitors (DE-3 and DE-4) from !1Macrotyloma axillare seed. !$#cross-references MUID:80003636; PMID:477675 !$#accession A01296 !'##molecule_type protein !'##residues 1-76 ##label JOU CLASSIFICATION #superfamily Bowman-Birk proteinase inhibitor; Bowman-Birk !1inhibitor repeat homology KEYWORDS duplication; serine proteinase inhibitor FEATURE !$17-43 #domain Bowman-Birk inhibitor repeat homology #label !8BB1\ !$44-69 #domain Bowman-Birk inhibitor repeat homology #label !8BB2\ !$16-70,17-32,20-66, !$22-30,40-47,44-59, !$49-57 #disulfide_bonds #status predicted\ !$24 #inhibitory_site Lys (trypsin) #status predicted\ !$51 #inhibitory_site Phe (chymotrypsin) #status predicted SUMMARY #length 76 #molecular-weight 8292 #checksum 8633 SEQUENCE /// ENTRY TIZB1 #type complete TITLE proteinase inhibitor (Bowman-Birk) I - adzuki bean ORGANISM #formal_name Vigna angularis #common_name adzuki bean DATE 30-Nov-1980 #sequence_revision 30-Nov-1980 #text_change 07-May-1999 ACCESSIONS A91453; A01297 REFERENCE A91453 !$#authors Ishikawa, C.; Nakamura, S.; Watanabe, K.; Takahashi, K. !$#journal FEBS Lett. (1979) 99:97-100 !$#title The amino acid sequence of adzuki bean proteinase inhibitor !1I. !$#cross-references MUID:79169875; PMID:437138 !$#accession A91453 !'##molecule_type protein !'##residues 1-82 ##label ISH REFERENCE A48235 !$#authors Tsunogae, Y.; Tanaka, I.; Yamane, T.; Kikkawa, J.; Ashida, !1T.; Ishikawa, C.; Watanabe, K.; Nakamura, S.; Takahashi, K. !$#journal J. Biochem. (1986) 100:1637-1646 !$#title Structure of the trypsin-binding domain of Bowman-Birk type !1protease inhibitor and its interaction with trypsin. !$#cross-references MUID:87194674; PMID:3032921 !$#contents annotation: X-ray crystallography, 3.0 angstroms COMMENT Trypsin and chymotrypsin are inhibited simultaneously. CLASSIFICATION #superfamily Bowman-Birk proteinase inhibitor; Bowman-Birk !1inhibitor repeat homology KEYWORDS duplication; serine proteinase inhibitor FEATURE !$19-45 #domain Bowman-Birk inhibitor repeat homology #label !8BB1\ !$46-71 #domain Bowman-Birk inhibitor repeat homology #label !8BB2\ !$18-72,19-34,22-68, !$24-32 #disulfide_bonds #status experimental\ !$26 #inhibitory_site Lys (trypsin) #status experimental\ !$42-49,46-61,51-59 #disulfide_bonds #status predicted\ !$53 #inhibitory_site Tyr (chymotrypsin) #status predicted SUMMARY #length 82 #molecular-weight 9130 #checksum 8707 SEQUENCE /// ENTRY TIZB2 #type complete TITLE proteinase inhibitor (Bowman-Birk) II - adzuki bean CONTAINS proteinase inhibitor II' ORGANISM #formal_name Vigna angularis #common_name adzuki bean DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 19-Apr-1996 ACCESSIONS A90019; A01297 REFERENCE A90019 !$#authors Yoshikawa, M.; Kiyohara, T.; Iwasaki, T.; Ishii, Y.; Kimura, !1N. !$#journal Agric. Biol. Chem. (1979) 43:787-796 !$#title Amino acid sequences of proteinase inhibitors II and II' !1from adzuki beans. !$#accession A90019 !'##molecule_type protein !'##residues 1-81 ##label YOS COMMENT Separate reactive sites for trypsin and chymotrypsin do not !1inhibit simultaneously. CLASSIFICATION #superfamily Bowman-Birk proteinase inhibitor; Bowman-Birk !1inhibitor repeat homology KEYWORDS duplication; serine proteinase inhibitor FEATURE !$10-81 #product proteinase inhibitor II' #status !8experimental #label P2P\ !$19-44 #domain Bowman-Birk inhibitor repeat homology #label !8BB1\ !$45-70 #domain Bowman-Birk inhibitor repeat homology #label !8BB2\ !$18-71,19-33,22-67, !$23-31,41-48,45-60, !$50-58 #disulfide_bonds #status predicted\ !$25 #inhibitory_site Lys (trypsin) #status predicted\ !$52 #inhibitory_site Tyr (chymotrypsin) #status predicted SUMMARY #length 81 #molecular-weight 9044 #checksum 6265 SEQUENCE /// ENTRY TIAM4 #type complete TITLE proteinase inhibitor (Bowman-Birk) DE-4 - Macrotyloma axillare ORGANISM #formal_name Macrotyloma axillare DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 31-Dec-1993 ACCESSIONS A01298 REFERENCE A91257 !$#authors Joubert, F.J.; Kruger, H.; Townshend, G.S.; Botes, D.P. !$#journal Eur. J. Biochem. (1979) 97:85-91 !$#title Purification, some properties and the complete primary !1structures of two protease inhibitors (DE-3 and DE-4) from !1Macrotyloma axillare seed. !$#cross-references MUID:80003636; PMID:477675 !$#accession A01298 !'##molecule_type protein !'##residues 1-76 ##label JOU CLASSIFICATION #superfamily Bowman-Birk proteinase inhibitor; Bowman-Birk !1inhibitor repeat homology KEYWORDS duplication; serine proteinase inhibitor FEATURE !$16-42 #domain Bowman-Birk inhibitor repeat homology #label !8BB1\ !$43-68 #domain Bowman-Birk inhibitor repeat homology #label !8BB2\ !$15-69,16-31,19-65, !$21-29,39-46,43-58, !$48-56 #disulfide_bonds #status predicted\ !$23 #inhibitory_site Lys (trypsin) #status predicted\ !$50 #inhibitory_site Leu (chymotrypsin) #status predicted SUMMARY #length 76 #molecular-weight 8369 #checksum 6190 SEQUENCE /// ENTRY TIFB2 #type complete TITLE proteinase inhibitor (Bowman-Birk) II - kidney bean (tentative sequence) ORGANISM #formal_name Phaseolus vulgaris #common_name kidney bean DATE 30-Nov-1980 #sequence_revision 30-Nov-1980 #text_change 31-Mar-2000 ACCESSIONS A01299 REFERENCE A01299 !$#authors Wilson, K.A.; Laskowski Sr., M. !$#journal J. Biol. Chem. (1975) 250:4261-4267 !$#title The partial amino acid sequence of trypsin inhibitor II from !1garden bean, Phaseolus vulgaris, with location of the !1trypsin and elastase-reactive sites. !$#cross-references MUID:75151596; PMID:1126951 !$#accession A01299 !'##molecule_type protein !'##residues 1-79 ##label WIL !'##note two forms of the inhibitor were isolated; the amino end of the !1longer form is blocked; a shorter form, which lacks residues !11-8, is probably derived by proteolytic degradation. !1Residues 9-21 were sequenced only for the shorter form COMMENT This protein inhibits elastase and trypsin simultaneously !1and independently. CLASSIFICATION #superfamily Bowman-Birk proteinase inhibitor; Bowman-Birk !1inhibitor repeat homology KEYWORDS blocked amino end; duplication; serine proteinase inhibitor FEATURE !$18-44 #domain Bowman-Birk inhibitor repeat homology #label !8BB1\ !$45-70 #domain Bowman-Birk inhibitor repeat homology #label !8BB2\ !$17-71,18-33,21-67, !$23-31,41-48,45-60, !$50-58 #disulfide_bonds #status predicted\ !$25 #inhibitory_site Ala (elastase) #status experimental\ !$52 #inhibitory_site Arg (trypsin) #status experimental SUMMARY #length 79 #molecular-weight 8587 #checksum 4092 SEQUENCE /// ENTRY TIZB1A #type complete TITLE proteinase inhibitor (Bowman-Birk) I-A - adzuki bean ORGANISM #formal_name Vigna angularis #common_name adzuki bean DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 31-Dec-1993 ACCESSIONS A01300 REFERENCE A01300 !$#authors Kiyohara, T.; Yokota, K.; Masaki, Y.; Matsui, O.; Iwasaki, !1T.; Yoshikawa, M. !$#journal J. Biochem. (1981) 90:721-728 !$#title The amino acid sequences of proteinase inhibitors I-A and !1I-A' from adzuki beans. !$#cross-references MUID:82075699; PMID:7309695 !$#accession A01300 !'##molecule_type protein !'##residues 1-78 ##label KIY COMMENT This inhibitor strongly inhibits trypsin. CLASSIFICATION #superfamily Bowman-Birk proteinase inhibitor; Bowman-Birk !1inhibitor repeat homology KEYWORDS duplication; serine proteinase inhibitor FEATURE !$19-45 #domain Bowman-Birk inhibitor repeat homology #label !8BB1\ !$46-71 #domain Bowman-Birk inhibitor repeat homology #label !8BB2\ !$18-72,19-34,22-68, !$24-32,42-49,46-61, !$51-59 #disulfide_bonds #status predicted\ !$26 #inhibitory_site Lys (trypsin) #status experimental\ !$53 #inhibitory_site Arg (trypsin) #status experimental SUMMARY #length 78 #molecular-weight 8675 #checksum 951 SEQUENCE /// ENTRY TIZB1B #type complete TITLE proteinase inhibitor (Bowman-Birk) I-B - adzuki bean ORGANISM #formal_name Vigna angularis #common_name adzuki bean DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 31-Dec-1993 ACCESSIONS B01300; A01300 REFERENCE A01300 !$#authors Kiyohara, T.; Yokota, K.; Masaki, Y.; Matsui, O.; Iwasaki, !1T.; Yoshikawa, M. !$#journal J. Biochem. (1981) 90:721-728 !$#title The amino acid sequences of proteinase inhibitors I-A and !1I-A' from adzuki beans. !$#cross-references MUID:82075699; PMID:7309695 !$#accession B01300 !'##molecule_type protein !'##residues 1-78 ##label KIY COMMENT This inhibitor strongly inhibits trypsin. CLASSIFICATION #superfamily Bowman-Birk proteinase inhibitor; Bowman-Birk !1inhibitor repeat homology KEYWORDS duplication; serine proteinase inhibitor FEATURE !$19-45 #domain Bowman-Birk inhibitor repeat homology #label !8BB1\ !$46-71 #domain Bowman-Birk inhibitor repeat homology #label !8BB2\ !$18-72,19-34,22-68, !$24-32,42-49,46-61, !$51-59 #disulfide_bonds #status predicted\ !$26 #inhibitory_site Lys (trypsin) #status predicted\ !$53 #inhibitory_site Arg (trypsin) #status predicted SUMMARY #length 78 #molecular-weight 8656 #checksum 921 SEQUENCE /// ENTRY TIZB1P #type complete TITLE proteinase inhibitor (Bowman-Birk) I-A' - adzuki bean ORGANISM #formal_name Vigna angularis #common_name adzuki bean DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 31-Dec-1993 ACCESSIONS C01300; A01300 REFERENCE A01300 !$#authors Kiyohara, T.; Yokota, K.; Masaki, Y.; Matsui, O.; Iwasaki, !1T.; Yoshikawa, M. !$#journal J. Biochem. (1981) 90:721-728 !$#title The amino acid sequences of proteinase inhibitors I-A and !1I-A' from adzuki beans. !$#cross-references MUID:82075699; PMID:7309695 !$#accession C01300 !'##molecule_type protein !'##residues 1-72 ##label KIY COMMENT This inhibitor strongly inhibits trypsin. CLASSIFICATION #superfamily Bowman-Birk proteinase inhibitor; Bowman-Birk !1inhibitor repeat homology KEYWORDS duplication; serine proteinase inhibitor FEATURE !$13-39 #domain Bowman-Birk inhibitor repeat homology #label !8BB1\ !$40-65 #domain Bowman-Birk inhibitor repeat homology #label !8BB2\ !$12-66,13-28,16-62, !$18-26,36-43,40-55, !$45-53 #disulfide_bonds #status predicted\ !$20 #inhibitory_site Lys (trypsin) #status predicted\ !$47 #inhibitory_site Arg (trypsin) #status predicted SUMMARY #length 72 #molecular-weight 7970 #checksum 2612 SEQUENCE /// ENTRY TIMB #type complete TITLE trypsin inhibitor (Bowman-Birk) - mung bean ORGANISM #formal_name Vigna radiata #common_name mung bean DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 28-Oct-1994 ACCESSIONS A01301 REFERENCE A01301 !$#authors Zhang, Y.; Luo, S.; Tan, F.; Qi, Z.; Xu, L.; Zhang, A. !$#journal Sci. Sin. (1982) 25:268-277 !$#title Complete amino acid sequence of mung bean trypsin inhibitor. !$#accession A01301 !'##molecule_type protein !'##residues 1-72 ##label ZHA !'##note three isoinhibitors are also found whose amino ends differ !1slightly from that shown; the first differs in having Asp-2; !1the next two differ in lacking Ser-1 and His-2, instead !1having Asp-1 and Lys-1, respectively COMMENT This inhibitor stoichiometrically inhibits trypsin in a !1molar ratio of 1:2. CLASSIFICATION #superfamily Bowman-Birk proteinase inhibitor; Bowman-Birk !1inhibitor repeat homology KEYWORDS duplication; serine proteinase inhibitor FEATURE !$13-39 #domain Bowman-Birk inhibitor repeat homology #label !8BB1\ !$40-65 #domain Bowman-Birk inhibitor repeat homology #label !8BB2\ !$12-66,13-28,16-62, !$18-26,36-43,40-55, !$45-53 #disulfide_bonds #status predicted\ !$20 #inhibitory_site Lys (trypsin) #status predicted\ !$47 #inhibitory_site Arg (trypsin) #status predicted SUMMARY #length 72 #molecular-weight 7973 #checksum 2116 SEQUENCE /// ENTRY TISYC2 #type complete TITLE proteinase inhibitor (Bowman-Birk) C-II precursor - soybean ORGANISM #formal_name Glycine max #common_name soybean DATE 24-Apr-1984 #sequence_revision 31-Dec-1993 #text_change 18-Jun-1999 ACCESSIONS A22636; A01302 REFERENCE A92489 !$#authors Hammond, R.W.; Foard, D.E.; Larkins, B.A. !$#journal J. Biol. Chem. (1984) 259:9883-9890 !$#title Molecular cloning and analysis of a gene coding for the !1Bowman-Birk protease inhibitor in soybean. !$#cross-references MUID:84264652; PMID:6086657 !$#contents annotation !$#note the sequence has been revised in reference A92540 REFERENCE A92540 !$#authors Hammond, R.W.; Foard, D.E.; Larkins, B.A. !$#journal J. Biol. Chem. (1985) 260:7806 !$#contents erratum !$#accession A22636 !'##molecule_type DNA !'##residues 1-103 ##label HAM !'##cross-references GB:K01967; NID:g169942; PIDN:AAA33952.1; !1PID:g169943 REFERENCE A01302 !$#authors Odani, S.; Ikenaka, T. !$#journal J. Biochem. (1977) 82:1523-1531 !$#title Studies on soybean trypsin inhibitors. XI. Complete amino !1acid sequence of a soybean trypsin-chymotrypsin-elastase !1inhibitor, C-II. !$#cross-references MUID:78087480; PMID:599141 !$#accession A01302 !'##molecule_type protein !'##residues 28-103 ##label ODA COMMENT This protein inhibits trypsin, elastase, and chymotrypsin. !1The site of interaction with chymotrypsin has not been !1determined but is not independent of the trypsin-reactive !1site. CLASSIFICATION #superfamily Bowman-Birk proteinase inhibitor; Bowman-Birk !1inhibitor repeat homology KEYWORDS duplication; seed; serine proteinase inhibitor FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-103 #product proteinase inhibitor (Bowman-Birk) C-II !8#status experimental #label MAT\ !$42-68 #domain Bowman-Birk inhibitor repeat homology #label !8BB1\ !$69-94 #domain Bowman-Birk inhibitor repeat homology #label !8BB2\ !$41-95,42-57,45-91, !$47-55,65-72,69-84, !$74-82 #disulfide_bonds #status predicted\ !$49 #inhibitory_site Ala (elastase) #status predicted\ !$76 #inhibitory_site Arg (trypsin) #status experimental SUMMARY #length 103 #molecular-weight 11387 #checksum 3626 SEQUENCE /// ENTRY TISYD2 #type complete TITLE proteinase inhibitor (Bowman-Birk) D-II precursor - soybean CONTAINS proteinase inhibitor (Bowman-Birk) E-I (PI-II) ORGANISM #formal_name Glycine max #common_name soybean DATE 24-Apr-1984 #sequence_revision 12-Apr-1996 #text_change 18-Jun-1999 ACCESSIONS S32243; JC2224; A01303; B01303; S29559 REFERENCE S32243 !$#authors Song, J.C.; Baek, J.M.; Kim, S.I. !$#submission submitted to the EMBL Data Library, October 1992 !$#description Molecular cloning of a gemonic DNA encoding the soybean !1bowman-birk proteinase isoinhibitor D-II. !$#accession S32243 !'##status preliminary !'##molecule_type DNA !'##residues 1-102 ##label SON !'##cross-references EMBL:X68707; NID:g288618; PIDN:CAA48658.1; !1PID:g288619 REFERENCE JC2224 !$#authors Baek, J.M.; Song, J.C.; Choi, Y.D.; Kim, S.I. !$#journal Biosci. Biotechnol. Biochem. (1994) 58:843-846 !$#title Nucleotide sequence homology of cDNAs encoding soybean !1Bowman-Birk type proteinase inhibitor and its isoinhibitors. !$#cross-references MUID:94289861; PMID:7764974 !$#accession JC2224 !'##molecule_type mRNA !'##residues 1-102 ##label BA2 !'##cross-references EMBL:X68706; NID:g18571; PIDN:CAA48657.1; !1PID:g18572 !'##experimental_source clone pB26 REFERENCE A01303 !$#authors Odani, S.; Ikenaka, T. !$#journal J. Biochem. (1978) 83:737-745 !$#title Studies on soybean trypsin inhibitors. XII. Linear sequences !1of two soybean double-headed trypsin inhibitors, D-II and !1E-I. !$#cross-references MUID:78150870; PMID:641033 !$#accession A01303 !'##molecule_type protein !'##residues 28-102 ##label OD1 !$#accession B01303 !'##molecule_type protein !'##residues 37-57 ##label OD2 REFERENCE A42052 !$#authors Chen, P.; Rose, J.; Love, R.; Wei, C.H.; Wang, B.C. !$#journal J. Biol. Chem. (1992) 267:1990-1994 !$#title Reactive sites of an anticarcinogenic Bowman-Birk proteinase !1inhibitor are similar to other trypsin inhibitors. !$#cross-references MUID:92112932; PMID:1730730 !$#contents annotation; X-ray crystallography of inhibitor PI-II at 2.5 !1angstroms COMMENT This protein regulates endogeneous proteinase during !1germination, stores sulfur-containing amino acids during !1dormancy, and protects the plant from insects and !1microorganisms. CLASSIFICATION #superfamily Bowman-Birk proteinase inhibitor; Bowman-Birk !1inhibitor repeat homology KEYWORDS duplication; seed; serine proteinase inhibitor; storage !1protein FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-102 #product proteinase inhibitor (Bowman-Birk) D-II !8#status experimental #label MAT\ !$44-70 #domain Bowman-Birk inhibitor repeat homology #label !8BB1\ !$71-96 #domain Bowman-Birk inhibitor repeat homology #label !8BB2\ !$43-97,44-59,47-93, !$49-57,67-74,71-86, !$76-84 #disulfide_bonds #status experimental\ !$51 #inhibitory_site Arg (trypsin) #status predicted\ !$78 #inhibitory_site Arg (trypsin) #status predicted SUMMARY #length 102 #molecular-weight 11496 #checksum 3547 SEQUENCE /// ENTRY TIVTOA #type complete TITLE proteinase inhibitor (Bowman-Birk) - common vetch ORGANISM #formal_name Vicia sativa subsp. nigra #common_name common vetch DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 17-Feb-1995 ACCESSIONS A01304 REFERENCE A01304 !$#authors Shimokawa, Y.; Kuromizu, K.; Araki, T.; Ohata, J.; Abe, O. !$#journal Nat. Cult. (1983) 10:69-73 !$#title The complete amino acid sequence of Vicia angustifolia !1proteinase inhibitor. !$#accession A01304 !'##molecule_type protein !'##residues 1-72 ##label SHI !'##experimental_source var. segetalis COMMENT One mole of inhibitor inhibits either one mole of trypsin or !1two moles of chymotrypsin, stoichiometrically. CLASSIFICATION #superfamily Bowman-Birk proteinase inhibitor; Bowman-Birk !1inhibitor repeat homology KEYWORDS duplication; serine proteinase inhibitor FEATURE !$9-34 #domain Bowman-Birk inhibitor repeat homology #label !8BB1\ !$35-60 #domain Bowman-Birk inhibitor repeat homology #label !8BB2\ !$8-61,9-24,12-57, !$14-22,31-38,35-50, !$40-48 #disulfide_bonds #status predicted\ !$16 #inhibitory_site Arg (trypsin) #status predicted\ !$42 #inhibitory_site Tyr (chymotrypsin) #status predicted SUMMARY #length 72 #molecular-weight 8038 #checksum 3152 SEQUENCE /// ENTRY TIVF #type complete TITLE proteinase inhibitor (Bowman-Birk) - fava bean ORGANISM #formal_name Vicia faba #common_name fava bean DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 17-Feb-1995 ACCESSIONS JX0198 REFERENCE JX0198 !$#authors Asao, T.; Imai, F.; Tsuji, I.; Tashiro, M.; Iwami, K.; !1Ibuki, F. !$#journal J. Biochem. (1991) 110:951-955 !$#title The amino acid sequence of a Bowman-Birk type proteinase !1inhibitor from faba beans (Vicia faba L.). !$#cross-references MUID:92176172; PMID:1794984 !$#accession JX0198 !'##molecule_type protein !'##residues 1-63 ##label ASA !'##experimental_source seed CLASSIFICATION #superfamily Bowman-Birk proteinase inhibitor; Bowman-Birk !1inhibitor repeat homology KEYWORDS duplication; seed; serine proteinase inhibitor FEATURE !$9-34 #domain Bowman-Birk inhibitor repeat homology #label !8BB1\ !$35-60 #domain Bowman-Birk inhibitor repeat homology #label !8BB2\ !$8-61,9-24,12-57, !$14-22,31-38,35-50, !$40-48 #disulfide_bonds #status predicted\ !$16 #inhibitory_site Lys (trypsin) #status experimental\ !$42 #inhibitory_site Tyr (chymotrypsin) #status !8experimental SUMMARY #length 63 #molecular-weight 6989 #checksum 5679 SEQUENCE /// ENTRY TINPA2 #type complete TITLE proteinase inhibitor (Bowman-Birk) A-II - peanut ORGANISM #formal_name Arachis hypogaea #common_name peanut DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 07-May-1999 ACCESSIONS A91975; A91971; A01305 REFERENCE A91975 !$#authors Norioka, S.; Ikenaka, T. !$#journal J. Biochem. (1983) 94:589-599 !$#title Amino acid sequences of trypsin-chymotrypsin inhibitors !1(A-I, A-II, B-I, and B-II) from peanut (Arachis hypogaea): a !1discussion on the molecular evolution of legume Bowman-Birk !1type inhibitors. !$#cross-references MUID:84032360; PMID:6630176 !$#accession A91975 !'##molecule_type protein !'##residues 1-19 ##label NOR REFERENCE A91971 !$#authors Norioka, S.; Ikenaka, T. !$#journal J. Biochem. (1983) 93:479-485 !$#title Amino acid sequence of a trypsin-chymotrypsin inhibitor, !1B-III, of peanut (Arachis hypogaea). !$#cross-references MUID:83186120; PMID:6841347 !$#accession A91971 !'##molecule_type protein !'##residues 10-70 ##label NO2 REFERENCE A48236 !$#authors Suzuki, A.; Tsunogae, Y.; Tanaka, I.; Yamane, T.; Ashida, !1T.; Norioka, S.; Hara, S.; Ikenaka, T. !$#journal J. Biochem. (1987) 101:267-274 !$#title The structure of Bowman-Birk type protease inhibitor A-II !1from peanut (Arachis hypogaea) at 3.3 angstrom resolution. !$#cross-references MUID:87194702; PMID:3571206 !$#contents annotation; X-ray crystallography, 3.3 angstroms COMMENT Four inhibitors were found that are identical except at !1their amino ends and that probably arise by proteolytic !1degradation of a single gene product. Inhibitors A-I, B-I, !1and B-III comprise residues 4-70, 8-70, and 10-70, !1respectively. COMMENT These proteins inhibit trypsin and chymotrypsin, having two !1sites of interaction with trypsin. The site of interaction !1with chymotrypsin has not been determined but is not !1independent of the trypsin-reactive sites. CLASSIFICATION #superfamily Bowman-Birk proteinase inhibitor; Bowman-Birk !1inhibitor repeat homology KEYWORDS duplication; serine proteinase inhibitor FEATURE !$12-39 #domain Bowman-Birk inhibitor repeat homology #label !8BB1\ !$40-66 #domain Bowman-Birk inhibitor repeat homology #label !8BB2\ !$11-68,12-29,15-63, !$17-27,36-43,40-55, !$45-53 #disulfide_bonds #status experimental\ !$19 #inhibitory_site Arg (trypsin) #status experimental\ !$47 #inhibitory_site Arg (trypsin) #status experimental SUMMARY #length 70 #molecular-weight 7633 #checksum 2188 SEQUENCE /// ENTRY TINPB2 #type complete TITLE proteinase inhibitor (Bowman-Birk) B-II - peanut ORGANISM #formal_name Arachis hypogaea #common_name peanut DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 31-Dec-1993 ACCESSIONS A01306 REFERENCE A91975 !$#authors Norioka, S.; Ikenaka, T. !$#journal J. Biochem. (1983) 94:589-599 !$#title Amino acid sequences of trypsin-chymotrypsin inhibitors !1(A-I, A-II, B-I, and B-II) from peanut (Arachis hypogaea): a !1discussion on the molecular evolution of legume Bowman-Birk !1type inhibitors. !$#cross-references MUID:84032360; PMID:6630176 !$#accession A01306 !'##molecule_type protein !'##residues 1-63 ##label NOR COMMENT One of the trypsin inhibitory sites probably also interacts !1with chymotrypsin. CLASSIFICATION #superfamily Bowman-Birk proteinase inhibitor; Bowman-Birk !1inhibitor repeat homology KEYWORDS duplication; serine proteinase inhibitor FEATURE !$6-33 #domain Bowman-Birk inhibitor repeat homology #label !8BB1\ !$34-60 #domain Bowman-Birk inhibitor repeat homology #label !8BB2\ !$5-62,6-23,9-57, !$11-21,30-37,34-49, !$39-47 #disulfide_bonds #status predicted\ !$13 #inhibitory_site Arg (trypsin) #status experimental\ !$41 #inhibitory_site Arg (trypsin) #status experimental SUMMARY #length 63 #molecular-weight 6795 #checksum 5794 SEQUENCE /// ENTRY TIOAB #type complete TITLE trypsin inhibitor (Bowman-Birk) - Job's tears ORGANISM #formal_name Coix lachryma-jobi #common_name Job's tears DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 31-Dec-1993 ACCESSIONS S00349 REFERENCE S00349 !$#authors Ary, M.B.; Shewry, P.R.; Richardson, M. !$#journal FEBS Lett. (1988) 229:111-118 !$#title The amino acid sequence of a cereal Bowman-Birk type trypsin !1inhibitor from seeds of Jobs' tears (Coix lachryma-jobi L.). !$#cross-references MUID:88152203; PMID:3162215 !$#accession S00349 !'##molecule_type protein !'##residues 1-64 ##label ARY CLASSIFICATION #superfamily Bowman-Birk proteinase inhibitor; Bowman-Birk !1inhibitor repeat homology KEYWORDS duplication; proteinase inhibitor FEATURE !$10-35 #domain Bowman-Birk inhibitor repeat homology #label !8BB1\ !$36-59 #domain Bowman-Birk inhibitor repeat homology #status !8atypical #label BB2\ !$9-61,10-25,15-23, !$32-39,36-49 #disulfide_bonds #status predicted\ !$17 #inhibitory_site Arg (trypsin) #status predicted SUMMARY #length 64 #molecular-weight 7270 #checksum 4797 SEQUENCE /// ENTRY TIILF2 #type complete TITLE trypsin inhibitor (Bowman-Birk) II - foxtail millet ORGANISM #formal_name Setaria italica #common_name foxtail millet DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 31-Dec-1993 ACCESSIONS JX0136 REFERENCE JX0136 !$#authors Tashiro, M.; Asao, T.; Hirata, C.; Takahashi, K.; Kanamori, !1M. !$#journal J. Biochem. (1990) 108:669-672 !$#title The complete amino acid sequence of a major trypsin !1inhibitor from seeds of foxtail millet (Setaria italica). !$#cross-references MUID:91154179; PMID:2292595 !$#accession JX0136 !'##molecule_type protein !'##residues 1-67 ##label TAS CLASSIFICATION #superfamily Bowman-Birk proteinase inhibitor; Bowman-Birk !1inhibitor repeat homology KEYWORDS duplication; serine proteinase inhibitor FEATURE !$9-34 #domain Bowman-Birk inhibitor repeat homology #label !8BB1\ !$35-61 #domain Bowman-Birk inhibitor repeat homology #status !8atypical #label BB2\ !$8-63,9-24,14-22, !$31-38,35-51 #disulfide_bonds #status predicted\ !$16 #inhibitory_site Lys (trypsin) #status predicted SUMMARY #length 67 #molecular-weight 7679 #checksum 9289 SEQUENCE /// ENTRY TIILF3 #type complete TITLE trypsin inhibitor (Bowman-Birk) III - foxtail millet ORGANISM #formal_name Setaria italica #common_name foxtail millet DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 07-May-1999 ACCESSIONS JG0013 REFERENCE JG0013 !$#authors Tashiro, M.; Asao, T.; Hirata, C.; Takahashi, K. !$#journal Agric. Biol. Chem. (1991) 55:419-426 !$#title Purification, characterization, and amino acid sequence of !1foxtail millet trypsin inhibitor III. !$#cross-references MUID:91299279; PMID:1368693 !$#accession JG0013 !'##molecule_type protein !'##residues 1-67 ##label TAS CLASSIFICATION #superfamily Bowman-Birk proteinase inhibitor; Bowman-Birk !1inhibitor repeat homology KEYWORDS duplication; serine proteinase inhibitor FEATURE !$9-34 #domain Bowman-Birk inhibitor repeat homology #label !8BB1\ !$35-61 #domain Bowman-Birk inhibitor repeat homology #status !8atypical #label BB2\ !$8-63,9-24,14-22, !$31-38,35-51 #disulfide_bonds #status predicted\ !$16 #inhibitory_site Lys (trypsin) #status predicted SUMMARY #length 67 #molecular-weight 7680 #checksum 9169 SEQUENCE /// ENTRY XBPI #type complete TITLE bromelain inhibitor - pineapple ORGANISM #formal_name Ananas comosus #common_name pineapple DATE 30-Nov-1980 #sequence_revision 30-Nov-1980 #text_change 05-Jun-1998 ACCESSIONS A01307 REFERENCE A01307 !$#authors Reddy, M.N.; Keim, P.S.; Heinrikson, R.L.; Kezdy, F.J. !$#journal J. Biol. Chem. (1975) 250:1741-1750 !$#title Primary structural analysis of sulfhydryl protease !1inhibitors from pineapple stem. !$#cross-references MUID:75095654; PMID:1112827 !$#accession A01307 !'##molecule_type protein !'##residues 1-11;12-52 ##label RED !'##note the inhibitor is composed of two chains; the authors suggest !1that the inhibitor is generated by the excision of a bridge !1peptide from a single-chain precursor !'##note a number of similar inhibitors were found; they differ from the !1sequence shown in having 11-Arg, 12-Gln or 12-pyrrolidone !1carboxylic acid, and 19-Thr. Also, some B chains lack 1-Thr CLASSIFICATION #superfamily Bowman-Birk proteinase inhibitor; Bowman-Birk !1inhibitor repeat homology KEYWORDS cysteine proteinase inhibitor FEATURE !$1-11 #product bromelain inhibitor, chain B #status !8experimental #label MATB\ !$3-28 #domain Bowman-Birk inhibitor repeat homology !8(fragments) #label BB1\ !$12-52 #product bromelain inhibitor, chain A #status !8experimental #label MATA\ !$29-52 #domain Bowman-Birk inhibitor repeat homology #status !8atypical #label BB2\ !$3-18,6-50,8-16, !$25-32,29-41 #disulfide_bonds #status predicted SUMMARY #length 52 #molecular-weight 5817 #checksum 2300 SEQUENCE /// ENTRY TIBHB #type complete TITLE trypsin inhibitor (Bowman-Birk) - two-rowed barley ORGANISM #formal_name Hordeum vulgare var. distichum #common_name two-rowed barley DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 31-Dec-1993 ACCESSIONS JT0235 REFERENCE JT0235 !$#authors Nagasue, A.; Fukamachi, H.; Ikenaga, H.; Funatsu, G. !$#journal Agric. Biol. Chem. (1988) 52:1505-1514 !$#title The amino acid sequence of barley rootlet trypsin inhibitor. !$#accession JT0235 !'##molecule_type protein !'##residues 1-124 ##label NAG COMMENT This inhibitor interacts with two molecules of trypsin. CLASSIFICATION #superfamily barley rootlet proteinase inhibitor; !1Bowman-Birk inhibitor repeat homology KEYWORDS duplication; serine proteinase inhibitor FEATURE !$10-35 #domain Bowman-Birk inhibitor repeat homology #label !8BB1\ !$36-60 #domain Bowman-Birk inhibitor repeat homology #status !8atypical #label BB2\ !$68-93 #domain Bowman-Birk inhibitor repeat homology #label !8BB3\ !$94-119 #domain Bowman-Birk inhibitor repeat homology #status !8atypical #label BB4\ !$9-62,10-25,15-23, !$32-39,36-50,67-121, !$68-83,73-81,90-97, !$94-109 #disulfide_bonds #status predicted\ !$17 #inhibitory_site Arg (trypsin) #status predicted\ !$75 #inhibitory_site Arg (trypsin) #status predicted SUMMARY #length 124 #molecular-weight 13823 #checksum 7046 SEQUENCE /// ENTRY TIRZBR #type complete TITLE trypsin inhibitor (Bowman-Birk) - rice ORGANISM #formal_name Oryza sativa #common_name rice DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 21-Jan-1997 ACCESSIONS A27193 REFERENCE A27193 !$#authors Tashiro, M.; Hashino, K.; Shiozaki, M.; Ibuki, F.; Maki, Z. !$#journal J. Biochem. (1987) 102:297-306 !$#title The complete amino acid sequence of rice bran trypsin !1inhibitor. !$#cross-references MUID:88032948; PMID:3667571 !$#accession A27193 !'##molecule_type protein !'##residues 1-133 ##label TAS COMMENT This inhibitor interacts with two molecules of trypsin. CLASSIFICATION #superfamily barley rootlet proteinase inhibitor; !1Bowman-Birk inhibitor repeat homology KEYWORDS duplication; serine proteinase inhibitor FEATURE !$8-37 #domain Bowman-Birk inhibitor repeat homology #status !8atypical #label BB1\ !$38-65 #domain Bowman-Birk inhibitor repeat homology #status !8atypical #label BB2\ !$76-101 #domain Bowman-Birk inhibitor repeat homology #label !8BB3\ !$102-128 #domain Bowman-Birk inhibitor repeat homology #status !8atypical #label BB4\ !$7-67,8-25,34-41, !$38-54,75-130,76-91, !$81-89,98-105, !$102-118 #disulfide_bonds #status predicted\ !$17 #inhibitory_site Lys (trypsin) #status predicted\ !$83 #inhibitory_site Lys (trypsin) #status predicted SUMMARY #length 133 #molecular-weight 15074 #checksum 9770 SEQUENCE /// ENTRY TITZ #type complete TITLE trypsin inhibitor - Mongolian snake-gourd ORGANISM #formal_name Trichosanthes kirilowii #common_name Mongolian snake-gourd DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 31-Dec-1993 ACCESSIONS A01308 REFERENCE A01308 !$#authors Tan, F.; Zhang, G.; Mu, J.; Lin, N.; Chi, C. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1984) 365:1211-1217 !$#title Purification, characterization and sequence determination of !1a double-headed trypsin inhibitor peptide from Trichosanthes !1kirilowii (a Chinese medical herb). !$#cross-references MUID:85103287; PMID:6440850 !$#accession A01308 !'##molecule_type protein !'##residues 1-41 ##label TAN COMMENT This small inhibitor, isolated from a Chinese medicinal herb !1of the gourd (cucurbit) family, has two active sites that !1simultaneously bind trypsin. CLASSIFICATION #superfamily Trichosanthes trypsin inhibitor KEYWORDS serine proteinase inhibitor FEATURE !$15-26,17-24 #disulfide_bonds #status predicted\ !$20 #inhibitory_site Arg (trypsin) #status predicted\ !$29-37 #disulfide_bonds #status experimental\ !$30 #inhibitory_site Lys (trypsin) #status predicted SUMMARY #length 41 #molecular-weight 4531 #checksum 4248 SEQUENCE /// ENTRY TISYC #type complete TITLE trypsin inhibitor C (Kunitz) - soybean ORGANISM #formal_name Glycine max #common_name soybean DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 17-Mar-2000 ACCESSIONS A91998; C60808; A01309 REFERENCE A91998 !$#authors Kim, S.H.; Hara, S.; Hase, S.; Ikenaka, T.; Toda, H.; !1Kitamura, K.; Kaizuma, N. !$#journal J. Biochem. (1985) 98:435-448 !$#title Comparative study on amino acid sequences of Kunitz-type !1soybean trypsin inhibitors, Ti(a), Ti(b), and Ti(c). !$#cross-references MUID:86059307; PMID:3905784 !$#accession A91998 !'##molecule_type protein !'##residues 1-181 ##label KIM !'##experimental_source cv. Raiden REFERENCE A60808 !$#authors Hsieh, J.C.; Lin, F.P.; Tam, M.F. !$#journal Anal. Biochem. (1988) 170:1-8 !$#title Electroblotting onto glass-fiber filter from an analytical !1isoelectrofocusing gel: a preparative method for isolating !1proteins for N-terminal microsequencing. !$#cross-references MUID:88267456; PMID:3389500 !$#accession C60808 !'##molecule_type protein !'##residues 1-15,'X',17-20 ##label HSI REFERENCE A90382 !$#authors Sweet, R.M.; Wright, H.T.; Janin, J.; Chothia, C.H.; Blow, !1D.M. !$#journal Biochemistry (1974) 13:4212-4228 !$#title Crystal structure of the complex of porcine trypsin with !1soybean trypsin inhibitor (Kunitz) at 2.6-A resolution. !$#cross-references MUID:75008481; PMID:4472048 !$#contents annotation; X-ray crystallography, 2.6 angstroms !$#note the structure of the complex of soybean trypsin inhibitor !1and pig trypsin was determined REFERENCE A90163 !$#authors Brown, J.R.; Lerman, N.; Bohak, Z. !$#journal Biochem. Biophys. Res. Commun. (1966) 23:561-565 !$#title The amino acid sequences around the disulfide bonds of !1soybean trypsin inhibitor. !$#cross-references MUID:67120094; PMID:6006643 !$#contents annotation; disulfide bonds REFERENCE A92026 !$#authors Ozawa, K.; Laskowski Jr., M. !$#journal J. Biol. Chem. (1966) 241:3955-3961 !$#title The reactive site of trypsin inhibitors. !$#cross-references MUID:67020674; PMID:5950769 !$#contents annotation; inhibitory site COMMENT Electrophoresis identifies three genetically distinct !1variants, A, B, and C, that are inherited as codominant !1alleles. CLASSIFICATION #superfamily plant Kunitz-type proteinase inhibitor KEYWORDS serine proteinase inhibitor FEATURE !$39-86,136-145 #disulfide_bonds #status experimental\ !$63 #inhibitory_site Arg (trypsin) #status experimental SUMMARY #length 181 #molecular-weight 20167 #checksum 9936 SEQUENCE /// ENTRY TISY #type complete TITLE trypsin inhibitor A (Kunitz) precursor - soybean ORGANISM #formal_name Glycine max #common_name soybean DATE 30-Nov-1980 #sequence_revision 12-Apr-1996 #text_change 17-Mar-2000 ACCESSIONS S19189; B91998; A91203; A01309 REFERENCE S19189 !$#authors Song, S.I.; Kim, C.H.; Baek, S.J.; Choi, Y.D. !$#submission submitted to the EMBL Data Library, February 1992 !$#description Nucleotide sequence of a cDNA encoding the precursor for !1soybean trypsin inhibitor (Kunitz type A). !$#accession S19189 !'##molecule_type mRNA !'##residues 1-217 ##label SON !'##cross-references EMBL:X64447; NID:g18769; PIDN:CAA45777.1; !1PID:g18770 REFERENCE A91998 !$#authors Kim, S.H.; Hara, S.; Hase, S.; Ikenaka, T.; Toda, H.; !1Kitamura, K.; Kaizuma, N. !$#journal J. Biochem. (1985) 98:435-448 !$#title Comparative study on amino acid sequences of Kunitz-type !1soybean trypsin inhibitors, Ti(a), Ti(b), and Ti(c). !$#cross-references MUID:86059307; PMID:3905784 !$#accession B91998 !'##molecule_type protein !'##residues 26-206 ##label KIM REFERENCE A91203 !$#authors Koide, T.; Ikenaka, T. !$#journal Eur. J. Biochem. (1973) 32:417-431 !$#title Studies on soybean trypsin inhibitors. 3. Amino-acid !1sequence of the carboxyl-terminal region and the complete !1amino-acid sequence of soybean trypsin inhibitor (Kunitz). !$#cross-references MUID:73142321; PMID:4734969 !$#accession A91203 !'##molecule_type protein !'##residues 26-84,'PS',87-178,'D',180,'GH',183-206 ##label KOI !'##note this is the final paper in a series !'##note Leu-206 is missing from 75% of the molecules REFERENCE A90382 !$#authors Sweet, R.M.; Wright, H.T.; Janin, J.; Chothia, C.H.; Blow, !1D.M. !$#journal Biochemistry (1974) 13:4212-4228 !$#title Crystal structure of the complex of porcine trypsin with !1soybean trypsin inhibitor (Kunitz) at 2.6-A resolution. !$#cross-references MUID:75008481; PMID:4472048 !$#contents annotation; X-ray crystallography, 2.6 angstroms !$#note the structure of the complex of soybean trypsin inhibitor !1and pig trypsin was determined REFERENCE A90163 !$#authors Brown, J.R.; Lerman, N.; Bohak, Z. !$#journal Biochem. Biophys. Res. Commun. (1966) 23:561-565 !$#title The amino acid sequences around the disulfide bonds of !1soybean trypsin inhibitor. !$#cross-references MUID:67120094; PMID:6006643 !$#contents annotation; disulfide bonds REFERENCE A92026 !$#authors Ozawa, K.; Laskowski Jr., M. !$#journal J. Biol. Chem. (1966) 241:3955-3961 !$#title The reactive site of trypsin inhibitors. !$#cross-references MUID:67020674; PMID:5950769 !$#contents annotation; inhibitory site COMMENT Electrophoresis identifies three genetically distinct !1variants, A, B, and C, that are inherited as codominant !1alleles. CLASSIFICATION #superfamily plant Kunitz-type proteinase inhibitor KEYWORDS serine proteinase inhibitor FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-206 #product trypsin inhibitor A (Kunitz) #status !8experimental #label MAT\ !$64-111,161-170 #disulfide_bonds #status experimental\ !$88 #inhibitory_site Arg (trypsin) #status experimental SUMMARY #length 217 #molecular-weight 24076 #checksum 3720 SEQUENCE /// ENTRY TISYB #type complete TITLE trypsin inhibitor B (Kunitz) - soybean ORGANISM #formal_name Glycine max #common_name soybean DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 17-Mar-2000 ACCESSIONS A01310 REFERENCE A91998 !$#authors Kim, S.H.; Hara, S.; Hase, S.; Ikenaka, T.; Toda, H.; !1Kitamura, K.; Kaizuma, N. !$#journal J. Biochem. (1985) 98:435-448 !$#title Comparative study on amino acid sequences of Kunitz-type !1soybean trypsin inhibitors, Ti(a), Ti(b), and Ti(c). !$#cross-references MUID:86059307; PMID:3905784 !$#accession A01310 !'##molecule_type protein !'##residues 1-181 ##label KIM !'##experimental_source cv. Norin No. 2 COMMENT Electrophoresis identifies three genetically distinct !1variants, A, B, and C, that are inherited as codominant !1alleles. CLASSIFICATION #superfamily plant Kunitz-type proteinase inhibitor KEYWORDS proteinase inhibitor FEATURE !$39-86,136-145 #disulfide_bonds #status predicted\ !$63 #inhibitory_site Arg (trypsin) #status predicted SUMMARY #length 181 #molecular-weight 20040 #checksum 823 SEQUENCE /// ENTRY TIWDK #type complete TITLE trypsin inhibitor 1A (Kunitz) - winged bean ORGANISM #formal_name Psophocarpus tetragonolobus #common_name winged bean DATE 03-Aug-1984 #sequence_revision 31-Mar-1992 #text_change 17-Mar-2000 ACCESSIONS B01311; A01311 REFERENCE A01311 !$#authors Yamamoto, M.; Hara, S.; Ikenaka, T. !$#journal J. Biochem. (1983) 94:849-863 !$#title Amino acid sequences of two trypsin inhibitors from winged !1bean seed (Psophocarpus tetragonolobus (L)DC). !$#cross-references MUID:84061716; PMID:6643426 !$#accession B01311 !'##molecule_type protein !'##residues 1-172 ##label YAM COMMENT This protein inhibits trypsin stoichiometrically. COMMENT The protease inhibitors of legume seeds are separated into !1two groups depending upon their molecular weight and !1cysteine content. Kunitz inhibitors have high molecular !1weights (20,000) and four cysteine residues; Bowman-Birk !1inhibitors have low molecular weights (8,000) and 14 !1cysteine residues. All the cysteines in both groups form !1disulfide bonds. COMMENT By homology with the Kunitz trypsin inhibitor from soybean, !1Asn-13, Arg-64, and Phe-67 are thought to be important in !1the formation of the enzyme-inhibitor complex. CLASSIFICATION #superfamily plant Kunitz-type proteinase inhibitor KEYWORDS serine proteinase inhibitor FEATURE !$40-84,133-139 #disulfide_bonds #status predicted\ !$64 #inhibitory_site Arg (trypsin) #status experimental SUMMARY #length 172 #molecular-weight 19261 #checksum 4440 SEQUENCE /// ENTRY TIWDKB #type complete TITLE trypsin inhibitor 1B (Kunitz) - winged bean ORGANISM #formal_name Psophocarpus tetragonolobus #common_name winged bean DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 17-Mar-2000 ACCESSIONS A01311 REFERENCE A01311 !$#authors Yamamoto, M.; Hara, S.; Ikenaka, T. !$#journal J. Biochem. (1983) 94:849-863 !$#title Amino acid sequences of two trypsin inhibitors from winged !1bean seed (Psophocarpus tetragonolobus (L)DC). !$#cross-references MUID:84061716; PMID:6643426 !$#accession A01311 !'##molecule_type protein !'##residues 1-172 ##label YAM COMMENT This protein inhibits trypsin stoichiometrically. COMMENT The protease inhibitors of legume seeds are separated into !1two groups depending upon their molecular weight and !1cysteine content. Kunitz inhibitors have high molecular !1weights (20,000) and four cysteine residues; Bowman-Birk !1inhibitors have low molecular weights (8,000) and 14 !1cysteine residues. All the cysteines in both groups form !1disulfide bonds. COMMENT By homology with the Kunitz trypsin inhibitor from soybean, !1Asn-13, Arg-64, and Phe-67 are thought to be important in !1the formation of the enzyme-inhibitor complex. CLASSIFICATION #superfamily plant Kunitz-type proteinase inhibitor KEYWORDS serine proteinase inhibitor FEATURE !$40-84,133-139 #disulfide_bonds #status predicted\ !$64 #inhibitory_site Arg (trypsin) #status experimental SUMMARY #length 172 #molecular-weight 19217 #checksum 4128 SEQUENCE /// ENTRY A61433 #type complete TITLE trypsin inhibitor 2a (Kunitz) - winged bean ALTERNATE_NAMES acidic trypsin inhibitor 2a ORGANISM #formal_name Psophocarpus tetragonolobus #common_name winged bean DATE 07-Oct-1994 #sequence_revision 02-Dec-1994 #text_change 17-Mar-2000 ACCESSIONS A61433 REFERENCE A61433 !$#authors Kortt, A.A.; Burns, J.E.; Caldwell, J.B.; Ferro, T.; Strike, !1P.M. !$#journal J. Protein Chem. (1991) 10:183-188 !$#title Primary structure of kunitz-type trypsin inhibitor-2a !1(pI5.9) from Psophocarpus tetragonolobus (L.) DC seed. !$#cross-references MUID:92029514; PMID:1930632 !$#accession A61433 !'##molecule_type protein !'##residues 1-180 ##label KOR CLASSIFICATION #superfamily plant Kunitz-type proteinase inhibitor KEYWORDS pyroglutamic acid; seed; serine proteinase inhibitor FEATURE !$1 #modified_site pyrrolidone carboxylic acid (Gln) !8#status experimental\ !$40-84,136-147 #disulfide_bonds #status predicted\ !$64 #inhibitory_site Arg (trypsin) #status predicted SUMMARY #length 180 #molecular-weight 20386 #checksum 3516 SEQUENCE /// ENTRY A33872 #type complete TITLE miraculin precursor - sweet berry ALTERNATE_NAMES taste-modifying protein ORGANISM #formal_name Richardella dulcifica #common_name sweet berry DATE 27-Feb-1990 #sequence_revision 03-May-1996 #text_change 17-Mar-2000 ACCESSIONS JC4232; PC4066; A33872; A29237 REFERENCE JC4232 !$#authors Masuda, Y.; Nirasawa, S.; Nakaya, K.; Kurihara, Y. !$#journal Gene (1995) 161:175-177 !$#title Cloning and sequencing of a cDNA encoding a taste-modifying !1protein, miraculin. !$#cross-references MUID:95394351; PMID:7665074 !$#accession JC4232 !'##molecule_type mRNA !'##residues 1-220 ##label MAS !'##cross-references DDBJ:D38598 !$#accession PC4066 !'##molecule_type protein !'##residues 98-104;211-217 ##label MA2 !'##note The authors translated the codon GGA for residue 16 as Ala and !1CGT for residue 25 as Leu REFERENCE A33872 !$#authors Theerasilp, S.; Hitotsuya, H.; Nakajo, S.; Nakaya, K.; !1Nakamura, Y.; Kurihara, Y. !$#journal J. Biol. Chem. (1989) 264:6655-6659 !$#title Complete amino acid sequence and structure characterization !1of the taste-modifying protein, miraculin. !$#cross-references MUID:89214066; PMID:2708331 !$#accession A33872 !'##molecule_type protein !'##residues 30-128,'S',130-220 ##label THE REFERENCE A29237 !$#authors Theerasilp, S.; Kurihara, Y. !$#journal J. Biol. Chem. (1988) 263:11536-11539 !$#title Complete purification and characterization of the !1taste-modifying protein, miraculin, from miracle fruit. !$#cross-references MUID:88298812; PMID:3403544 !$#accession A29237 !'##molecule_type protein !'##residues 30-49 ##label TH2 COMMENT This protein has the unusual property of modifying a sour !1taste into a sweet taste. CLASSIFICATION #superfamily plant Kunitz-type proteinase inhibitor KEYWORDS glycoprotein; monomer; sweet taste FEATURE !$1-29 #domain signal sequence #status predicted #label SIG\ !$30-220 #product miraculin #status experimental #label MAT\ !$71,215 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$114 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 220 #molecular-weight 24396 #checksum 3536 SEQUENCE /// ENTRY TIZM #type complete TITLE trypsin inhibitor - maize (tentative sequence) ORGANISM #formal_name Zea mays #common_name maize DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 31-Mar-2000 ACCESSIONS A01312 REFERENCE A01312 !$#authors Hochstrasser, K.; Illchmann, K.; Werle, E. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1970) 351:721-728 !$#title Plant protease inhibitors, VII: The amino acid sequence of !1the specific trypsin inhibitor from maize seeds and the !1characterization of the polymer. !$#cross-references MUID:70226643; PMID:5425943 !$#accession A01312 !'##molecule_type protein !'##residues 1-65 ##label HOC !'##note after interaction with trypsin, the inhibitor consists of two !1chains linked by disulfide bonds COMPLEX homotrimer CLASSIFICATION #superfamily maize trypsin inhibitor KEYWORDS homotrimer; serine proteinase inhibitor FEATURE !$25-26 #cleavage_site Arg-Leu (trypsin) #status !8experimental\ !$25 #inhibitory_site Arg (trypsin) #status experimental SUMMARY #length 65 #molecular-weight 6981 #checksum 9405 SEQUENCE /// ENTRY TIPU #type complete TITLE trypsin inhibitor ITD I - winter squash ORGANISM #formal_name Cucurbita maxima #common_name winter squash DATE 18-Apr-1984 #sequence_revision 18-Apr-1984 #text_change 10-Mar-1994 ACCESSIONS A01313 REFERENCE A01313 !$#authors Wilusz, T.; Wieczorek, M.; Polanowski, A.; Denton, A.; Cook, !1J.; Laskowski Jr., M. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1983) 364:93-95 !$#title Amino-acid sequence of two trypsin isoinhibitors, ITD I and !1ITD III from squash seed (Cucurbita maxima). !$#cross-references MUID:83184077; PMID:6840699 !$#accession A01313 !'##molecule_type protein !'##residues 1-29 ##label WIL REFERENCE A37580 !$#authors Bode, W.; Greyling, H.J.; Huber, R.; Otlewski, J.; Wilusz, !1T. !$#journal FEBS Lett. (1989) 242:285-292 !$#title The refined 2.0 A X-ray crystal structure of the complex !1formed between bovine beta-trypsin and CMTI-I, a trypsin !1inhibitor from squash seeds (Cucurbita maxima). !$#cross-references MUID:89121085; PMID:2914611 !$#contents annotation; X-ray crystallography, 2.0 angstroms; disulfide !1bonds COMMENT In these references the terms pumpkin and squash are used !1synonymously for Cucurbita maxima. CLASSIFICATION #superfamily squash trypsin inhibitor ITD I KEYWORDS serine proteinase inhibitor FEATURE !$3-20,10-22,16-28 #disulfide_bonds #status experimental\ !$5 #inhibitory_site Arg (trypsin) #status experimental SUMMARY #length 29 #molecular-weight 3275 #checksum 1706 SEQUENCE /// ENTRY TIPU3 #type complete TITLE trypsin inhibitor ITD III - winter squash ORGANISM #formal_name Cucurbita maxima #common_name winter squash DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 05-May-1994 ACCESSIONS B01313; A01313 REFERENCE A01313 !$#authors Wilusz, T.; Wieczorek, M.; Polanowski, A.; Denton, A.; Cook, !1J.; Laskowski Jr., M. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1983) 364:93-95 !$#title Amino-acid sequence of two trypsin isoinhibitors, ITD I and !1ITD III from squash seed (Cucurbita maxima). !$#cross-references MUID:83184077; PMID:6840699 !$#accession B01313 !'##molecule_type protein !'##residues 1-29 ##label WIL !'##note iTD III and PHFI, an inhibitor of both trypsin and factor XII !1(Hageman factor), may be identical !'##note in this reference the terms pumpkin and squash are used !1synonymously for Cucurbita maxima CLASSIFICATION #superfamily squash trypsin inhibitor ITD I KEYWORDS serine proteinase inhibitor FEATURE !$3-20,10-22,16-28 #disulfide_bonds #status predicted\ !$5 #inhibitory_site Arg (trypsin) #status predicted SUMMARY #length 29 #molecular-weight 3274 #checksum 1760 SEQUENCE /// ENTRY TIPU1W #type complete TITLE trypsin inhibitor I - watermelon ORGANISM #formal_name Citrullus lanatus #common_name watermelon DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 31-Dec-1993 ACCESSIONS S00176 REFERENCE S00176 !$#authors Otlewski, J.; Whatley, H.; Polanowski, A.; Wilusz, T. !$#journal Biol. Chem. Hoppe-Seyler (1987) 368:1505-1507 !$#title Amino-acid sequences of trypsin inhibitors from watermelon !1(Citrullus vulgaris) and red bryony (Bryonia dioica) seeds. !$#cross-references MUID:88134580; PMID:3435645 !$#accession S00176 !'##molecule_type protein !'##residues 1-30 ##label OTL !'##note the source is designated as Citrullus vulgaris CLASSIFICATION #superfamily squash trypsin inhibitor ITD I KEYWORDS serine proteinase inhibitor FEATURE !$4-21,11-23,17-29 #disulfide_bonds #status predicted\ !$6 #inhibitory_site Arg (trypsin) #status predicted SUMMARY #length 30 #molecular-weight 3386 #checksum 3662 SEQUENCE /// ENTRY TIPU2B #type complete TITLE trypsin inhibitor II - red bryony ORGANISM #formal_name Bryonia dioica #common_name red bryony DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 31-Dec-1993 ACCESSIONS S00177 REFERENCE S00176 !$#authors Otlewski, J.; Whatley, H.; Polanowski, A.; Wilusz, T. !$#journal Biol. Chem. Hoppe-Seyler (1987) 368:1505-1507 !$#title Amino-acid sequences of trypsin inhibitors from watermelon !1(Citrullus vulgaris) and red bryony (Bryonia dioica) seeds. !$#cross-references MUID:88134580; PMID:3435645 !$#accession S00177 !'##molecule_type protein !'##residues 1-29 ##label OTL CLASSIFICATION #superfamily squash trypsin inhibitor ITD I KEYWORDS serine proteinase inhibitor FEATURE !$3-20,10-22,16-28 #disulfide_bonds #status predicted\ !$5 #inhibitory_site Arg (trypsin) #status predicted SUMMARY #length 29 #molecular-weight 3207 #checksum 2324 SEQUENCE /// ENTRY XKPO #type complete TITLE metallocarboxypeptidase inhibitor IIa precursor [validated] - potato ORGANISM #formal_name Solanum tuberosum #common_name potato DATE 23-Oct-1981 #sequence_revision 20-Apr-2000 #text_change 05-May-2000 ACCESSIONS T07003; A90386; A90032; A01314 REFERENCE Z15855 !$#authors Villanueva, J.; Canals, F.; Prat, S.; Ludevid, D.; Querol, !1E.; Aviles, F.X. !$#journal FEBS Lett. (1998) 440:175-182 !$#title Characterization of the wound-induced !1metallocarboxypeptidase inhibitor from potato. cDNA !1sequence, induction of gene expression, subcellular !1immunolocalization and potential roles of the C-terminal !1propeptide. !$#cross-references MUID:99077266; PMID:9862450 !$#accession T07003 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-102 ##label VIL !'##cross-references EMBL:AF060551; NID:g3091283; PIDN:AAC95130.1; !1PID:g3091284 !'##experimental_source cv. Berolina, ABA-induced leaf REFERENCE A90386 !$#authors Hass, G.M.; Nau, H.; Biemann, K.; Grahn, D.T.; Ericsson, !1L.H.; Neurath, H. !$#journal Biochemistry (1975) 14:1334-1342 !$#title The amino acid sequence of a carboxypeptidase inhibitor from !1potatoes. !$#cross-references MUID:75127965; PMID:1122280 !$#accession A90386 !'##molecule_type protein !'##residues 57-95 ##label HAS !'##note half of the molecules lack 58-Gln REFERENCE A90032 !$#authors Nau, H.; Biemann, K. !$#journal Anal. Biochem. (1976) 73:175-186 !$#title Amino acid sequencing by gas chromatography-mass !1spectrometry using trifluoro-dideuteroalkylated peptide !1derivatives. C. The primary structure of the !1carboxypeptidase inhibitor from potatoes. !$#cross-references MUID:76250864; PMID:942094 !$#accession A90032 !'##molecule_type protein !'##residues 57-95 ##label NAU !'##note this sequence was determined by gas chromatography-mass !1spectrometry REFERENCE A90428 !$#authors Leary, T.R.; Grahn, D.T.; Neurath, H.; Hass, G.M. !$#journal Biochemistry (1979) 18:2252-2256 !$#title Structure of potato carboxypeptidase inhibitor: disulfide !1pairing and exposure of aromatic residues. !$#cross-references MUID:79187807; PMID:444453 !$#contents annotation; disulfide bonds REFERENCE A50963 !$#authors Lipscomb, W.N.; Rees, D.C. !$#submission submitted to the Brookhaven Protein Data Bank, March 1982 !$#cross-references PDB:4CPA !$#contents annotation; X-ray crystallography, 2.5 angstroms, residues !1'Z',59-94 REFERENCE A92887 !$#authors Rees, D.C.; Lipscomb, W.N. !$#journal J. Mol. Biol. (1982) 160:475-498 !$#title Refined crystal structure of the potato inhibitor complex of !1carboxypeptidase A at 2.5 angstrom resolution. !$#cross-references MUID:83111930; PMID:7154070 !$#contents annotation; X-ray crystallography, 2.5 angstroms !$#note the structure of the complex of the inhibitor and !1carboxypeptidase A was determined. Val-94 is the site of !1interaction with carboxypeptidase REFERENCE A92902 !$#authors Rees, D.C.; Lewis, M.; Lipscomb, W.N. !$#journal J. Mol. Biol. (1983) 168:367-387 !$#title Refined crystal structure of carboxypeptidase A at 1.54 !1angstrom resolution. !$#cross-references MUID:83294519; PMID:6887246 !$#contents annotation; X-ray crystallography, 1.54 angstroms CLASSIFICATION #superfamily potato carboxypeptidase inhibitor KEYWORDS pyroglutamic acid; stress-induced protein FEATURE !$1-29 #domain signal sequence #status predicted #label SIG\ !$30-56 #domain propeptide #status predicted #label PRO\ !$57-95 #product carboxypeptidase inhibitor IIa #status !8experimental #label MAT\ !$96-102 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$57 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$64-80,68-83,74-90 #disulfide_bonds #status experimental\ !$94 #inhibitory_site Val (carboxypeptidase) #status !8experimental SUMMARY #length 102 #molecular-weight 11309 #checksum 5026 SEQUENCE /// ENTRY XKTO #type complete TITLE metallocarboxypeptidase inhibitor - tomato ORGANISM #formal_name Lycopersicon esculentum #common_name tomato DATE 06-Jul-1982 #sequence_revision 12-Apr-1996 #text_change 18-Jun-1999 ACCESSIONS S16558; A01315 REFERENCE S16558 !$#authors Martineau, B.; McBride, K.E.; Houck, C.M. !$#journal Mol. Gen. Genet. (1991) 228:281-286 !$#title Regulation of metallocarboxypeptidase inhibitor gene !1expression in tomato. !$#cross-references MUID:91360077; PMID:1715974 !$#accession S16558 !'##status preliminary !'##molecule_type mRNA !'##residues 1-77 ##label MAR !'##cross-references EMBL:X59282; NID:g19278; PIDN:CAA41973.1; !1PID:g19279 REFERENCE A01315 !$#authors Hass, G.M.; Hermodson, M.A. !$#journal Biochemistry (1981) 20:2256-2260 !$#title Amino acid sequence of a carboxypeptidase inhibitor from !1tomato fruit. !$#cross-references MUID:81208084; PMID:7236596 !$#accession A01315 !'##molecule_type protein !'##residues 33-69 ##label HAS CLASSIFICATION #superfamily potato carboxypeptidase inhibitor KEYWORDS pyroglutamic acid FEATURE !$33 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$39-55,43-58,49-65 #disulfide_bonds #status predicted SUMMARY #length 77 #molecular-weight 8354 #checksum 146 SEQUENCE /// ENTRY ZYSMN #type complete TITLE metalloproteinase inhibitor precursor - Streptomyces nigrescens (strain TK-24 and strain TK-23) ORGANISM #formal_name Streptomyces nigrescens #variety strain TK-24; strain TK-23 DATE 28-Feb-1986 #sequence_revision 12-Apr-1996 #text_change 16-Jun-2000 ACCESSIONS S12615; A01316 REFERENCE S12615 !$#authors Tanaka, K.; Aoki, H.; Oda, K.; Murao, S.; Saito, H.; !1Takahashi, H. !$#journal Nucleic Acids Res. (1990) 18:6433 !$#title Nucleotide sequence of the gene for a metalloproteinase !1inhibitor of Streptomyces nigrescens (SMPI). !$#cross-references MUID:91057139; PMID:2243793 !$#accession S12615 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-131 ##label TAN !'##cross-references GB:D00671; NID:g217027; PIDN:BAA00574.1; !1PID:g217028 !'##experimental_source strain TK-24 REFERENCE A01316 !$#authors Murai, H.; Hara, S.; Ikenaka, T.; Oda, K.; Murao, S. !$#journal J. Biochem. (1985) 97:173-180 !$#title Amino acid sequence of Streptomyces metallo-proteinase !1inhibitor from Streptomyces nigrescens TK-23. !$#cross-references MUID:85207510; PMID:3888972 !$#accession A01316 !'##molecule_type protein !'##residues 30-131 ##label MUR !'##experimental_source strain TK-23 !'##note thermolysin slowly cleaves only the peptide bond following !1Cys-64 FUNCTION !$#description inhibits microbial metalloproteinases, such as thermolysin !$#note does not inibit serine proteinases, cysteine proteinases, or !1aspartic proteinases CLASSIFICATION #superfamily microbial metalloproteinase inhibitor KEYWORDS metalloproteinase inhibitor FEATURE !$1-29 #domain signal sequence #status predicted #label SIG\ !$30-131 #product metalloproteinase inhibitor #status !8predicted #label MAT\ !$33-39,93-98 #disulfide_bonds #status experimental\ !$93 #inhibitory_site Cys (thermolysin) #status predicted SUMMARY #length 131 #molecular-weight 13186 #checksum 4327 SEQUENCE /// ENTRY XKPODC #type complete TITLE cathepsin D inhibitor pdi - potato ALTERNATE_NAMES aspartic proteinase inhibitor ORGANISM #formal_name Solanum tuberosum #common_name potato DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 23-Feb-1996 ACCESSIONS S05025; S24189 REFERENCE S05025 !$#authors Mares, M.; Meloun, B.; Pavlik, M.; Kostka, V.; Baudys, M. !$#journal FEBS Lett. (1989) 251:94-98 !$#title Primary structure of cathepsin D inhibitor from potatoes and !1its structure relationship to soybean trypsin inhibitor !1family. !$#cross-references MUID:89325696; PMID:2753167 !$#accession S05025 !'##molecule_type protein !'##residues 1-188 ##label MAR REFERENCE S23961 !$#authors Strukelj, B.; Pungercar, J.; Mesko, P.; Barlic-Maganja, D.; !1Gubensek, F.; Kregar, I.; Turk, V. !$#journal Biol. Chem. Hoppe-Seyler (1992) 373:477-482 !$#title Characterization of aspartic proteinase inhibitors from !1potato at the gene, cDNA and protein levels. !$#cross-references MUID:92384955; PMID:1515078 !$#accession S24189 !'##molecule_type protein !'##residues 1-188 ##label STR CLASSIFICATION #superfamily cathepsin D inhibitor KEYWORDS aspartic proteinase inhibitor; glycoprotein FEATURE !$19 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$48-93,142-153, !$150-159 #disulfide_bonds #status predicted\ !$67 #inhibitory_site Arg (cathepsin D) #status predicted SUMMARY #length 188 #molecular-weight 20589 #checksum 1952 SEQUENCE /// ENTRY XKPOD #type complete TITLE aspartic proteinase inhibitor precursor (clone PI8) - potato ORGANISM #formal_name Solanum tuberosum #common_name potato DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 18-Jun-1999 ACCESSIONS S10979; S24185 REFERENCE S10979 !$#authors Strukelj, B.; Pungercar, J.; Ritonja, A.; Krizaj, I.; !1Gubensek, F.; Kregar, I.; Turk, V. !$#journal Nucleic Acids Res. (1990) 18:4605 !$#title Nucleotide and deduced amino acid sequence of an aspartic !1proteinase inhibitor homologue from potato tubers (Solanum !1tuberosum L.). !$#cross-references MUID:90356412; PMID:2201952 !$#accession S10979 !'##molecule_type mRNA !'##residues 1-220 ##label STR !'##cross-references EMBL:X53470; NID:g21408; PIDN:CAA37566.1; !1PID:g21409 REFERENCE S23961 !$#authors Strukelj, B.; Pungercar, J.; Mesko, P.; Barlic-Maganja, D.; !1Gubensek, F.; Kregar, I.; Turk, V. !$#journal Biol. Chem. Hoppe-Seyler (1992) 373:477-482 !$#title Characterization of aspartic proteinase inhibitors from !1potato at the gene, cDNA and protein levels. !$#cross-references MUID:92384955; PMID:1515078 !$#accession S24185 !'##molecule_type mRNA !'##residues 1-220 ##label STW CLASSIFICATION #superfamily cathepsin D inhibitor KEYWORDS aspartic proteinase inhibitor FEATURE !$1-32 #domain signal sequence #status predicted #label SIG\ !$33-220 #product aspartic proteinase inhibitor #status !8predicted #label MAT SUMMARY #length 220 #molecular-weight 24190 #checksum 5393 SEQUENCE /// ENTRY XKACP3 #type complete TITLE pepsin inhibitor 3 - pig roundworm ALTERNATE_NAMES aspartyl proteinase inhibitor; major pepsin inhibitor ORGANISM #formal_name Ascaris suum #common_name pig roundworm DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 30-Jun-1993 ACCESSIONS A35701; A33107 REFERENCE A35701 !$#authors Martzen, M.R.; McMullen, B.A.; Smith, N.E.; Fujikawa, K.; !1Peanasky, R.J. !$#journal Biochemistry (1990) 29:7366-7372 !$#title Primary structure of the major pepsin inhibitor from the !1intestinal parasitic nematode Ascaris suum. !$#cross-references MUID:91027748; PMID:2223768 !$#accession A35701 !'##molecule_type protein !'##residues 1-149 ##label MAR CLASSIFICATION #superfamily roundworm pepsin inhibitor KEYWORDS aspartic proteinase inhibitor FEATURE !$13-59,48-66,79-146 #disulfide_bonds #status experimental SUMMARY #length 149 #molecular-weight 16397 #checksum 6108 SEQUENCE /// ENTRY TIEO1 #type complete TITLE proteinase inhibitor - eggplant ORGANISM #formal_name Solanum melongena #common_name eggplant, aubergine DATE 30-Nov-1980 #sequence_revision 30-Nov-1980 #text_change 05-Aug-1994 ACCESSIONS A01317 REFERENCE A01317 !$#authors Richardson, M. !$#journal FEBS Lett. (1979) 104:322-326 !$#title The complete amino acid sequence and the trypsin reactive !1(inhibitory) site of the major proteinase inhibitor from the !1fruits of aubergine (Solanum melongena L.). !$#cross-references MUID:80004163; PMID:477995 !$#accession A01317 !'##molecule_type protein !'##residues 1-52 ##label RIC !'##note 2-Leu and 6-Cys were also found CLASSIFICATION #superfamily potato proteinase inhibitor PTI KEYWORDS pyroglutamic acid FEATURE !$1 #modified_site pyrrolidone carboxylic acid (Gln) !8#status experimental\ !$38 #inhibitory_site Arg (trypsin) #status experimental SUMMARY #length 52 #molecular-weight 5590 #checksum 2914 SEQUENCE /// ENTRY XKPOT #type complete TITLE proteinase inhibitor PTI - potato ORGANISM #formal_name Solanum tuberosum #common_name potato DATE 06-Jul-1982 #sequence_revision 06-Jul-1982 #text_change 16-Aug-1996 ACCESSIONS A01318 REFERENCE A90465 !$#authors Hass, G.M.; Hermodson, M.A.; Ryan, C.A.; Gentry, L. !$#journal Biochemistry (1982) 21:752-756 !$#title Primary structures of two low molecular weight proteinase !1inhibitors from potatoes. !$#cross-references MUID:82182863; PMID:7074039 !$#accession A01318 !'##molecule_type protein !'##residues 1-51 ##label HAS !'##note Arg-38 is probably the site of interaction with trypsin CLASSIFICATION #superfamily potato proteinase inhibitor PTI KEYWORDS serine proteinase inhibitor SUMMARY #length 51 #molecular-weight 5602 #checksum 279 SEQUENCE /// ENTRY XKPOC1 #type complete TITLE proteinase inhibitor PCI-I precursor - potato ALTERNATE_NAMES potato chymotrypsin inhibitor I; protease inhibitor II ORGANISM #formal_name Solanum tuberosum #common_name potato DATE 06-Jul-1982 #sequence_revision 12-Apr-1996 #text_change 20-Apr-2000 ACCESSIONS A26584; A01319; A23591 REFERENCE A26584 !$#authors Thornburg, R.W.; An, G.; Cleveland, T.E.; Johnson, R.; Ryan, !1C.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:744-748 !$#title Wound-inducible expression of a potato inhibitor !1II-chloramphenicol acetyltransferase gene fusion in !1transgenic tobacco plants. !$#accession A26584 !'##molecule_type DNA !'##residues 1-153 ##label THO !'##cross-references GB:M15186; NID:g169488; PIDN:AAA33815.1; !1PID:g169489 REFERENCE A90465 !$#authors Hass, G.M.; Hermodson, M.A.; Ryan, C.A.; Gentry, L. !$#journal Biochemistry (1982) 21:752-756 !$#title Primary structures of two low molecular weight proteinase !1inhibitors from potatoes. !$#cross-references MUID:82182863; PMID:7074039 !$#accession A01319 !'##molecule_type protein !'##residues 55-106 ##label HAS !'##note Leu-92 is probably the site of interaction with chymotrypsin REFERENCE A23591 !$#authors Keil, M.; Sanchez-Serrano, J.; Schell, J.; Willmitzer, L. !$#journal Nucleic Acids Res. (1986) 14:5641-5650 !$#title Primary structure of a proteinase inhibitor II gene from !1potato (Solanum tuberosum). !$#cross-references MUID:86286579; PMID:3016659 !$#accession A23591 !'##molecule_type DNA !'##residues 1-26,'EH',28-33,'TL',36-54,'R',56-153 ##label KEI !'##cross-references GB:X04118; NID:g21521; PIDN:CAA27730.1; PID:g21522 GENETICS !$#gene IIK !$#introns 18/1 CLASSIFICATION #superfamily potato proteinase inhibitor PTI KEYWORDS serine proteinase inhibitor FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$55-106 #product proteinase inhibitor PCI-I #status !8experimental #label MAT SUMMARY #length 153 #molecular-weight 16505 #checksum 6807 SEQUENCE /// ENTRY XKPO2A #type fragment TITLE proteinase inhibitor IIa - potato (fragment) ORGANISM #formal_name Solanum tuberosum #common_name potato DATE 02-Apr-1982 #sequence_revision 02-Apr-1982 #text_change 16-Aug-1996 ACCESSIONS A01320 REFERENCE A01320 !$#authors Iwasaki, T.; Kiyohara, T.; Yoshikawa, M. !$#journal J. Biochem. (1976) 79:381-391 !$#title Amino acid sequence of an active fragment of potato !1proteinase inhibitor IIa. !$#cross-references MUID:76190064; PMID:1270410 !$#accession A01320 !'##molecule_type protein !'##residues 1-45 ##label IWA !'##note this active fragment inhibits trypsin strongly and chymotrypsin !1temporarily; the complete protein chain contains 97 residues CLASSIFICATION #superfamily potato proteinase inhibitor PTI KEYWORDS serine proteinase inhibitor FEATURE !$10-24,14-35,20-43 #disulfide_bonds #status experimental\ !$32 #inhibitory_site Lys (trypsin) #status experimental SUMMARY #length 45 #checksum 7686 SEQUENCE /// ENTRY XKPO2B #type fragment TITLE proteinase inhibitor IIb - potato (fragment) ORGANISM #formal_name Solanum tuberosum #common_name potato DATE 02-Apr-1982 #sequence_revision 02-Apr-1982 #text_change 16-Aug-1996 ACCESSIONS A01321 REFERENCE A01321 !$#authors Iwasaki, T.; Wada, J.; Kiyohara, T.; Yoshikawa, M. !$#journal J. Biochem. (1977) 82:991-1004 !$#title Amino acid sequence of an active fragment of potato !1proteinase inhibitor IIb. !$#cross-references MUID:78045944; PMID:924994 !$#accession A01321 !'##molecule_type protein !'##residues 1-40 ##label IWA !'##note this active fragment inhibits chymotrypsin and subtilisin !1strongly; the complete protein chain contains 97 residues CLASSIFICATION #superfamily potato proteinase inhibitor PTI KEYWORDS serine proteinase inhibitor FEATURE !$2-16,6-28,12-38 #disulfide_bonds #status experimental\ !$26 #inhibitory_site Lys (trypsin) #status experimental SUMMARY #length 40 #checksum 1210 SEQUENCE /// ENTRY XKARA #type complete TITLE proteinase inhibitor A - arrowhead ORGANISM #formal_name Sagittaria sagittifolia #common_name arrowhead DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 31-Mar-2000 ACCESSIONS A43809 REFERENCE A43809 !$#authors Yang, H.L.; Luo, R.S.; Wang, L.X.; Zhu, D.X.; Chi, C.W. !$#journal J. Biochem. (1992) 111:537-545 !$#title Primary structure and disulfide bridge location of arrowhead !1double-headed proteinase inhibitors. !$#cross-references MUID:92316904; PMID:1618743 !$#accession A43809 !'##molecule_type protein !'##residues 1-150 ##label YAN CLASSIFICATION #superfamily arrowhead proteinase inhibitor B KEYWORDS serine proteinase inhibitor FEATURE !$43-89,110-119, !$112-115 #disulfide_bonds #status predicted SUMMARY #length 150 #molecular-weight 16226 #checksum 9979 SEQUENCE /// ENTRY XKARB #type complete TITLE proteinase inhibitor B - arrowhead ALTERNATE_NAMES arrowhead proteinase inhibitor ORGANISM #formal_name Sagittaria sagittifolia #common_name arrowhead DATE 30-Sep-1988 #sequence_revision 31-Mar-1993 #text_change 31-Mar-2000 ACCESSIONS B43809; JC0004; JC1057; A24624 REFERENCE A43809 !$#authors Yang, H.L.; Luo, R.S.; Wang, L.X.; Zhu, D.X.; Chi, C.W. !$#journal J. Biochem. (1992) 111:537-545 !$#title Primary structure and disulfide bridge location of arrowhead !1double-headed proteinase inhibitors. !$#cross-references MUID:92316904; PMID:1618743 !$#accession B43809 !'##molecule_type protein !'##residues 1-150 ##label YAN REFERENCE A90695 !$#authors Chi, C.W.; Zhu, D.X.; Lin, N.Q.; Xu, L.X.; Tan, F.L.; Wang, !1L.X. !$#journal Biol. Chem. Hoppe-Seyler (1985) 366:879-885 !$#title The complete amino-acid sequence of the proteinase inhibitor !1B from the root of the arrowhead (Sagittaria sagittifolia !1L.). !$#cross-references MUID:86077291; PMID:3907662 !$#accession JC0004 !'##molecule_type protein !'##residues 1-62,'TQSAAMDVPGLGDFAEKVGSGEVDFGTFRGRGKFIAFE', !1'YAPTSVCISCAQYICPWLTNTSLKQDEHSMELGSRYKFSFL' ##label CHI !'##note this sequence has been revised in reference A43809 REFERENCE JC1057 !$#authors Chi, Z.W.; Zhu, D.X.; Lin, N.Q.; Xue, L.X.; Tan, F.L. !$#journal Acta Biochim. Biophys. Sin. (1986) 18:156-163 !$#title The complete amino acid sequence of the arrowhead proteinase !1inhibitor B. !$#accession JC1057 !'##molecule_type protein !'##residues 1-62, !1'TQSAAMDVPGLGDFAEKVGSGEVDFGTFRGRGKFIAFEYAPTSVCISCAQYICPWLTNT !1SLKQDEHSMELGSRYKFSFL' ##label CH2 !'##note this paper is in Chinese, with an English abstract CLASSIFICATION #superfamily arrowhead proteinase inhibitor B KEYWORDS serine proteinase inhibitor FEATURE !$43-89,110-119, !$112-115 #disulfide_bonds #status experimental SUMMARY #length 150 #molecular-weight 16152 #checksum 55 SEQUENCE /// ENTRY EPRZ #type complete TITLE phospholipid transfer protein homolog - rice ALTERNATE_NAMES amylase/proteinase inhibitor homolog ORGANISM #formal_name Oryza sativa #common_name rice DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 30-Jun-1993 ACCESSIONS S06427 REFERENCE S06427 !$#authors Yu, Y.G.; Chung, C.H.; Fowler, A.; Suh, S.W. !$#journal Arch. Biochem. Biophys. (1988) 265:466-475 !$#title Amino acid sequence of a probable amylase/protease inhibitor !1from rice seeds. !$#cross-references MUID:88339366; PMID:2458699 !$#accession S06427 !'##molecule_type protein !'##residues 1-91 ##label YUY COMMENT Four disulfide bonds are present. CLASSIFICATION #superfamily phospholipid transfer protein KEYWORDS disulfide bond SUMMARY #length 91 #molecular-weight 8909 #checksum 9022 SEQUENCE /// ENTRY S33459 #type complete TITLE lipid transfer protein - sorghum ORGANISM #formal_name Sorghum bicolor #common_name sorghum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 23-Mar-2001 ACCESSIONS S33459 REFERENCE S33459 !$#authors Plse, F.; Caelles, C.; Kader, J.C.; Delseny, M.; !1Puigdomnech, P. !$#submission submitted to the EMBL Data Library, April 1993 !$#description A tandem of genes coding for lipid transfer proteins in !1sorghum. !$#accession S33459 !'##status preliminary !'##molecule_type DNA !'##residues 1-118 ##label PLS !'##cross-references EMBL:X71667; NID:g311330; PIDN:CAA50660.1; !1PID:g311331 GENETICS !$#introns 116/3 CLASSIFICATION #superfamily phospholipid transfer protein SUMMARY #length 118 #molecular-weight 11570 #checksum 213 SEQUENCE /// ENTRY A31779 #type complete TITLE phospholipid transfer protein 9C2 precursor - maize ORGANISM #formal_name Zea mays #common_name maize DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A31779; JH0378 REFERENCE A31779 !$#authors Tchang, F.; This, P.; Stiefel, V.; Arondel, V.; Morch, M.D.; !1Pages, M.; Puigdomenech, P.; Grellet, F.; Delseny, M.; !1Bouillon, P.; Huet, J.C.; Guerbette, F.; Beauvais-Cante, F.; !1Duranton, H.; Pernollet, J.C.; Kader, J.C. !$#journal J. Biol. Chem. (1988) 263:16849-16855 !$#title Phospholipid transfer protein: full-length cDNA and amino !1acid sequence in maize. Amino acid sequence homologies !1between plant phospholipid transfer proteins. !$#cross-references MUID:89034179; PMID:3182817 !$#accession A31779 !'##molecule_type mRNA !'##residues 1-120 ##label TCH !'##cross-references GB:J04176; NID:g168575; PIDN:AAA33493.1; !1PID:g168576 REFERENCE JH0378 !$#authors Arondel, V.; Tchang, F.; Baillet, B.; Vignols, F.; Grellet, !1F.; Delseny, M.; Kader, J.C.; Puigdomenech, P. !$#journal Gene (1991) 99:133-136 !$#title Multiple mRNA coding for phospholipid-transfer protein from !1Zea mays arise from alternative splicing. !$#cross-references MUID:91216438; PMID:2022320 !$#accession JH0378 !'##molecule_type mRNA !'##residues 1-120 ##label ARO !'##note the authors translated the codon CAG for residue 5 as Glu CLASSIFICATION #superfamily phospholipid transfer protein KEYWORDS alternative splicing FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-120 #product phospholipid transfer protein #status !8predicted #label MAT SUMMARY #length 120 #molecular-weight 11705 #checksum 895 SEQUENCE /// ENTRY S20862 #type complete TITLE probable lipid transfer protein precursor - tomato ORGANISM #formal_name Lycopersicon esculentum #common_name tomato DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S20862 REFERENCE S20862 !$#authors Torres-Schumann, S.; Godoy, J.A.; Pintor-Toro, J.A. !$#journal Plant Mol. Biol. (1992) 18:749-757 !$#title A probable lipid transfer protein gene is induced by NaCl in !1stems of tomato plants. !$#cross-references MUID:92216050; PMID:1558948 !$#accession S20862 !'##molecule_type mRNA !'##residues 1-114 ##label TOR !'##cross-references EMBL:X56040; NID:g19391; PIDN:CAA39512.1; !1PID:g19392 CLASSIFICATION #superfamily phospholipid transfer protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-114 #product probable lipid transfer protein #status !8predicted #label MAT SUMMARY #length 114 #molecular-weight 11600 #checksum 804 SEQUENCE /// ENTRY S22168 #type complete TITLE lipid transfer protein - common tobacco ORGANISM #formal_name Nicotiana tabacum #common_name common tobacco DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S22168 REFERENCE S22168 !$#authors Fleming, A.; Mandel, T.; Hofmann, S.; Sterk, P.; de Vries, !1S.; Kuhlemeier, C. !$#submission submitted to the EMBL Data Library, December 1991 !$#accession S22168 !'##status preliminary !'##molecule_type DNA !'##residues 1-114 ##label FLE !'##cross-references EMBL:X62395; NID:g1679608; PIDN:CAA44267.1; !1PID:g19883 GENETICS !$#introns 112/2 CLASSIFICATION #superfamily phospholipid transfer protein SUMMARY #length 114 #molecular-weight 11523 #checksum 189 SEQUENCE /// ENTRY S00060 #type complete TITLE phospholipid transfer protein - spinach ORGANISM #formal_name Spinacia oleracea #common_name spinach DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S00060; S03359 REFERENCE S00060 !$#authors Bouillon, P.; Drischel, C.; Vergnolle, C.; Duranton, H.; !1Kader, J.C. !$#journal Eur. J. Biochem. (1987) 166:387-391 !$#title The primary structure of spinach-leaf phospholipid-transfer !1protein. !$#cross-references MUID:87275922; PMID:3609015 !$#accession S00060 !'##molecule_type protein !'##residues 1-91 ##label BOU REFERENCE S03359 !$#authors Bernhard, W.R.; Somerville, C.R. !$#journal Arch. Biochem. Biophys. (1989) 269:695-697 !$#title Coidentity of putative amylase inhibitors from barley and !1finger millet with phospholipid transfer proteins inferred !1from amino acid sequence homology. !$#cross-references MUID:89149117; PMID:2465737 !$#accession S03359 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-2,'Y',4-26,'CC',29-45,'Y',47-63,'QD',66-88,'R',90-91 !1##label BER COMMENT This protein binds also long-chain fatty acids. CLASSIFICATION #superfamily phospholipid transfer protein KEYWORDS lipid binding; lipid transport; phospholipid SUMMARY #length 91 #molecular-weight 8833 #checksum 6739 SEQUENCE /// ENTRY JQ1280 #type complete TITLE lipid transfer protein EP2 precursor - carrot ALTERNATE_NAMES extracellular protein 2 ORGANISM #formal_name Daucus carota #common_name carrot DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JQ1280 REFERENCE JQ1280 !$#authors Sterk, P.; Booij, H.; Schellekens, G.A.; Van Kammen, A.; De !1Vries, S.C. !$#journal Plant Cell (1991) 3:907-921 !$#title Cell-specific expression of the carrot EP2 lipid transfer !1protein gene. !$#cross-references MUID:92361243; PMID:1822991 !$#accession JQ1280 !'##molecule_type mRNA !'##residues 1-120 ##label STE !'##cross-references GB:M64746; NID:g167553; PIDN:AAB96834.1; !1PID:g167554 COMMENT This protein locates in cell walls. COMMENT The gene encoding for this protein is expressed in the !1embryogenic cell cultures, the shoot apex of seedlings and !1the flowers. CLASSIFICATION #superfamily phospholipid transfer protein FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-120 #product lipid transfer protein EP2 #status predicted !8#label LIP SUMMARY #length 120 #molecular-weight 12504 #checksum 5651 SEQUENCE /// ENTRY S51816 #type complete TITLE nonspecific lipid transfer protein - loblolly pine ORGANISM #formal_name Pinus taeda #common_name loblolly pine DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S51816 REFERENCE S51816 !$#authors Kinlaw, C.S.; Gerttula, S.M.; Carter, M.C. !$#journal Plant Mol. Biol. (1994) 26:1213-1216 !$#title Lipid transfer protein genes of loblolly pine are members of !1a complex gene family. !$#cross-references MUID:95111104; PMID:7811979 !$#accession S51816 !'##status preliminary; nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-123 ##label KIN !'##cross-references EMBL:U10432; NID:g600153; PIDN:AAA82182.1; !1PID:g600154 CLASSIFICATION #superfamily phospholipid transfer protein SUMMARY #length 123 #molecular-weight 12751 #checksum 5374 SEQUENCE /// ENTRY RZCS #type complete TITLE 2S seed storage protein precursor - castor bean ALTERNATE_NAMES 2S albumin precursor ORGANISM #formal_name Ricinus communis #common_name castor bean DATE 14-Nov-1983 #sequence_revision 08-Feb-1996 #text_change 18-Jun-1999 ACCESSIONS S11499; S11500; S11501; S11502; S27221; A01328; S27222 REFERENCE S11499 !$#authors Irwin, S.D.; Lord, J.M. !$#journal Nucleic Acids Res. (1990) 18:5890 !$#title Nucleotide sequence of a Ricinus communis 2S albumin !1precursor gene. !$#cross-references MUID:91016940; PMID:2216785 !$#accession S11499 !'##molecule_type DNA !'##residues 1-258 ##label IRW !'##cross-references EMBL:X54158; NID:g21067; PIDN:CAA38097.1; !1PID:g21068 !'##note the authors translated the codon CTC for residue 14 as Phe, CCA !1for residue 74 as Thr and CAA for residue 194 as Asp REFERENCE S11500 !$#authors Irwin, S.D.; Keen, J.N.; Findlay, J.B.C.; Lord, J.M. !$#journal Mol. Gen. Genet. (1990) 222:400-408 !$#title The Ricinus communis 2S albumin precursor: a single !1preproprotein may be processed into two different !1heterodimeric storage proteins. !$#cross-references MUID:91109729; PMID:2274038 !$#accession S11500 !'##molecule_type mRNA !'##residues 1-13,'F',15-73,'T',75-258 ##label IR2 !'##experimental_source clone 14g4 !$#accession S11501 !'##molecule_type mRNA !'##residues 'SFAIVTVF',15-73,'T',75-258 ##label IR3 !'##experimental_source clone 8g8 !$#accession S11502 !'##molecule_type mRNA !'##residues 'M',4,'LS',7-13,'F',15-21 ##label IRF !'##experimental_source clone 10a12 !$#accession S27221 !'##molecule_type protein !'##residues 'X',37,'X',39-45;'X',158-161,'X',163-174,'X' ##label IRA REFERENCE A92357 !$#authors Sharief, F.S.; Li, S.S.L. !$#journal J. Biol. Chem. (1982) 257:14753-14759 !$#title Amino acid sequence of small and large subunits of seed !1storage protein from Ricinus communis. !$#cross-references MUID:83082772; PMID:7174664 !$#accession A01328 !'##molecule_type protein !'##residues 157-190;194-221,'Q',223-225,230-233,'N',235-254,'Q',256-258 !1##label SHA !'##note 230-Ser was also found !'##note there is considerable similarity between residues 181-231 of !1this protein and residues 1-47 of the lima bean Bowman-Birk !1protease inhibitor REFERENCE A90322 !$#authors Odani, S.; Koide, T.; Ono, T.; Ohnishi, K. !$#journal Biochem. J. (1983) 213:543-545 !$#title Structural relationship between barley (Hordeum vulgare) !1trypsin inhibitor and castor-bean (Ricinus communis) storage !1protein. !$#cross-references MUID:83308577; PMID:6615448 !$#contents annotation !$#note this protein is homologous with trypsin inhibitor from !1barley COMPLEX consists of two chains linked by two disulfide bonds !1involving Cys-162 and Cys-175 CLASSIFICATION #superfamily 2S seed storage protein precursor KEYWORDS pyroglutamic acid; seed; storage protein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-35 #domain propeptide #status predicted #label PRO\ !$36-72 #product probable 2S seed storage protein small chain !82 #status experimental #label SCH1\ !$87-156 #product probable 2S seed storage protein chain large !82 #status predicted #label LCH1\ !$157-190 #product 2S seed storage protein small chain #status !8experimental #label SML\ !$194-258 #product 2S seed storage protein large chain #status !8experimental #label LRG\ !$194 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental SUMMARY #length 258 #molecular-weight 29290 #checksum 1269 SEQUENCE /// ENTRY T05710 #type complete TITLE 2S albumin precursor - soybean ALTERNATE_NAMES aspartic acid-rich peptide ORGANISM #formal_name Glycine max #common_name soybean DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS T05710; A28485 REFERENCE Z15424 !$#authors Wang, J.; Pichersky, E. !$#journal Plant Physiol. (1997) 114:1567 !$#title Nucleotide Sequence of S-Adenosyl-L-Methionine:Caffeic Acid !13-O-Methyltransferase from Clarkia breweri (Accession No. !1AF006009) (PGR97-104). !$#accession T05710 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-158 ##label WAN !'##cross-references EMBL:AF005030; NID:g2305019; PID:g2305020 !'##experimental_source cultivar Hodgson 78; cotyledon REFERENCE A28485 !$#authors Odani, S.; Koide, T.; Ono, T. !$#journal J. Biol. Chem. (1987) 262:10502-10505 !$#title Amino acid sequence of a soybean (Glycine max) seed !1polypeptide having a poly(L-aspartic acid) structure. !$#cross-references MUID:87280104; PMID:3611081 !$#accession A28485 !'##molecule_type protein !'##residues 22-64 ##label ODA CLASSIFICATION #superfamily soybean 2S albumin KEYWORDS glycoprotein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-64 #product 2S albumin small chain #status predicted !8#label MAT\ !$54-56 #region cell attachment (R-G-D) motif\ !$39 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 158 #molecular-weight 18460 #checksum 879 SEQUENCE /// ENTRY WIWTA #type complete TITLE alpha-amylase inhibitor CIII - wheat ORGANISM #formal_name Triticum aestivum #common_name common wheat DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 04-Sep-1998 ACCESSIONS A01322 REFERENCE A01322 !$#authors Kashlan, N.; Richardson, M. !$#journal Phytochemistry (1981) 20:1781-1784 !$#title The complete amino acid sequence of a major wheat protein !1inhibitor of alpha-amylase. !$#accession A01322 !'##molecule_type protein !'##residues 1-123 ##label KAS !'##note half of the molecules contained 65-Ser. Very small amounts of !167-Ala, 98-Gly, 99-Pro, and 118-Val were also found COMMENT This protein is one of a number of related alpha-amylase !1inhibitors found in the endosperm of wheat seeds. CLASSIFICATION #superfamily wheat alpha-amylase inhibitor KEYWORDS alpha-amylase inhibitor FEATURE !$7-54,21-42,29-82, !$43-98,56-113 #disulfide_bonds #status predicted SUMMARY #length 123 #molecular-weight 13342 #checksum 4689 SEQUENCE /// ENTRY WIWTA5 #type complete TITLE alpha-amylase inhibitor 0.53 - wheat ORGANISM #formal_name Triticum aestivum #common_name common wheat DATE 13-Jun-1983 #sequence_revision 28-Feb-1986 #text_change 04-Sep-1998 ACCESSIONS A90649; A90656; A01323 REFERENCE A90649 !$#authors Maeda, K.; Hase, T.; Matsubara, H. !$#journal Biochim. Biophys. Acta (1983) 743:52-57 !$#title Complete amino acid sequence of an alpha-amylase inhibitor !1in wheat kernel. !$#cross-references MUID:83127436; PMID:6186287 !$#accession A90649 !'##molecule_type protein !'##residues 1-119,'YPDAA' ##label MA1 !'##note this sequence has been revised in reference A90656 REFERENCE A90656 !$#authors Maeda, K.; Wakabayashi, S.; Matsubara, H. !$#journal Biochim. Biophys. Acta (1985) 828:213-221 !$#title Complete amino acid sequence of an alpha-amylase inhibitor !1in wheat kernel (0.19-inhibitor). !$#cross-references MUID:85175148; PMID:3872681 !$#accession A90656 !'##molecule_type protein !'##residues 1-124 ##label MA2 REFERENCE A91976 !$#authors Maeda, K.; Wakabayashi, S.; Matsubara, H. !$#journal J. Biochem. (1983) 94:865-870 !$#title Disulfide bridges in an alpha-amylase inhibitor from wheat !1kernel. !$#cross-references MUID:84061717; PMID:6605967 !$#contents annotation; disulfide bonds COMMENT This protein is a dimer of identical chains. CLASSIFICATION #superfamily wheat alpha-amylase inhibitor KEYWORDS alpha-amylase inhibitor FEATURE !$20-41,42-99,54-115 #disulfide_bonds #status predicted\ !$28-83 #disulfide_bonds #status experimental SUMMARY #length 124 #molecular-weight 13185 #checksum 4073 SEQUENCE /// ENTRY WIWTA1 #type complete TITLE alpha-amylase inhibitor 0.19 - wheat ORGANISM #formal_name Triticum aestivum #common_name common wheat DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 30-Sep-1998 ACCESSIONS A01324 REFERENCE A90656 !$#authors Maeda, K.; Wakabayashi, S.; Matsubara, H. !$#journal Biochim. Biophys. Acta (1985) 828:213-221 !$#title Complete amino acid sequence of an alpha-amylase inhibitor !1in wheat kernel (0.19-inhibitor). !$#cross-references MUID:85175148; PMID:3872681 !$#accession A01324 !'##molecule_type protein !'##residues 1-124 ##label MAE REFERENCE JC5705 !$#authors Okuda, M.; Satoh, T.; Sakurai, N.; Shibuya, K.; Kaji, H.; !1Samejima, T. !$#journal J. Biochem. (1997) 122:918-926 !$#title Overexpression in Escherichia coli of chemically synthesized !1gene for active 0.19 alpha-amylase inhibitor from wheat !1kernel. !$#cross-references MUID:98104043; PMID:9443806 !$#contents annotation COMMENT For the sequence from a synthetic DNA used for artificial !1protein production, see PIR:JC5705. COMPLEX homodimer CLASSIFICATION #superfamily wheat alpha-amylase inhibitor KEYWORDS alpha-amylase inhibitor; homodimer FEATURE !$6-52,20-41,28-83, !$42-99,54-115 #disulfide_bonds #status predicted SUMMARY #length 124 #molecular-weight 13337 #checksum 3320 SEQUENCE /// ENTRY WIILAI #type complete TITLE alpha-amylase/trypsin inhibitor - finger millet ORGANISM #formal_name Eleusine coracan #common_name finger millet DATE 18-Apr-1984 #sequence_revision 18-Apr-1984 #text_change 16-Feb-1997 ACCESSIONS A01326 REFERENCE A01326 !$#authors Campos, F.A.P.; Richardson, M. !$#journal FEBS Lett. (1983) 152:300-304 !$#title The complete amino acid sequence of the bifunctional !1alpha-amylase/trypsin inhibitor from seeds of ragi (Indian !1finger millet, Eleusine coracana Gaertn.). !$#accession A01326 !'##molecule_type protein !'##residues 1-122 ##label CAM !'##note 25-Ser, 26-Thr, 28-Thr, and 70-Ser were also found CLASSIFICATION #superfamily wheat alpha-amylase inhibitor KEYWORDS alpha-amylase inhibitor; serine proteinase inhibitor FEATURE !$34 #inhibitory_site Arg (trypsin) #status predicted SUMMARY #length 122 #molecular-weight 13119 #checksum 704 SEQUENCE /// ENTRY TIZM1 #type complete TITLE trypsin/factor XIIa inhibitor precursor - maize ALTERNATE_NAMES Hageman factor inhibitor ORGANISM #formal_name Zea mays #common_name maize DATE 28-Aug-1985 #sequence_revision 31-Dec-1992 #text_change 18-Jun-1999 ACCESSIONS S20850; A01327 REFERENCE S20850 !$#authors Wen, L.; Huang, J.K.; Zen, K.C.; Johnson, B.H.; !1Muthukrishnan, S.; MacKay, V.; Manney, T.R.; Manney, M.; !1Reeck, G.R. !$#journal Plant Mol. Biol. (1992) 18:813-814 !$#title Nucleotide sequence of a cDNA clone that encodes the maize !1inhibitor of trypsin and activated Hageman factor. !$#cross-references MUID:92216060; PMID:1558956 !$#accession S20850 !'##molecule_type mRNA !'##residues 1-155 ##label WEN !'##cross-references EMBL:X54064; NID:g22326; PIDN:CAA37998.1; !1PID:g22327 REFERENCE A01327 !$#authors Mahoney, W.C.; Hermodson, M.A.; Jones, B.; Powers, D.D.; !1Corfman, R.S.; Reeck, G.R. !$#journal J. Biol. Chem. (1984) 259:8412-8416 !$#title Amino acid sequence and secondary structural analysis of the !1corn inhibitor of trypsin and activated Hageman factor. !$#cross-references MUID:84239823; PMID:6610678 !$#accession A01327 !'##molecule_type protein !'##residues 29-48,'C',50-55,'R',57-60,'PR',61-106,'A',108-116,'A', !1118-119,'Q',121-134,'E',136-138 ##label MAH !'##note 117-Glu was also found COMMENT Five disulfide bonds are present. CLASSIFICATION #superfamily wheat alpha-amylase inhibitor KEYWORDS disulfide bond; serine proteinase inhibitor FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-138 #product trypsin/factor XIIa inhibitor #status !8experimental #label MAT\ !$139-155 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$62 #inhibitory_site Arg (trypsin) #status experimental SUMMARY #length 155 #molecular-weight 16302 #checksum 5547 SEQUENCE /// ENTRY TIBH #type complete TITLE trypsin inhibitor CMe precursor - barley ORGANISM #formal_name Hordeum vulgare #common_name barley DATE 14-Nov-1983 #sequence_revision 12-Apr-1996 #text_change 16-Jun-2000 ACCESSIONS S21451; A01325; JQ0342; S71590 REFERENCE S21451 !$#authors Royo, J. !$#submission submitted to the EMBL Data Library, April 1992 !$#accession S21451 !'##molecule_type DNA !'##residues 1-148 ##label ROY !'##cross-references EMBL:X65875; NID:g19008; PIDN:CAA46705.1; !1PID:g19009 REFERENCE A01325 !$#authors Odani, S.; Koide, T.; Ono, T. !$#journal J. Biol. Chem. (1983) 258:7998-8003 !$#title The complete amino acid sequence of barley trypsin !1inhibitor. !$#cross-references MUID:83238397; PMID:6345537 !$#accession A01325 !'##molecule_type protein !'##residues 25-145 ##label ODA !'##note residue 57 is tentatively assigned as the site of interaction !1with trypsin REFERENCE JQ0342 !$#authors Rodriguez-Palenzuela, P.; Royo, J.; Gomez, L.; !1Sanchez-Monge, R.; Salcedo, G.; Molina-Cano, J.L.; !1Garcia-Olmedo, F.; Carbonero, P. !$#journal Mol. Gen. Genet. (1989) 219:474-479 !$#title The gene for trypsin inhibitor CMe is regulated in trans by !1the lys 3a locus in the endosperm of barley (Hordeum vulgare !1L.). !$#cross-references MUID:90158508; PMID:2516240 !$#accession JQ0342 !'##molecule_type mRNA !'##residues 1-142,'A',144 ##label ROD !'##cross-references GB:X17302; NID:g18956; PIDN:CAA35188.1; !1PID:g1405736 !'##note the authors translated the codon GAG for residue 111 as Asp and !1GCA for residue 143 as Gly REFERENCE S71590 !$#authors Royo, J.; Diaz, I.; Rodriquez-Palenzuela, P.; Carbonero, P. !$#journal Plant Mol. Biol. (1996) 31:1051-1059 !$#title Isolation and promoter characterization of barley gene Itr1 !1encoding trypsin inhibitor BTI-CMe: differential activity in !1wild-type and mutant lys3a endosperm. !$#cross-references MUID:97000917; PMID:8843947 !$#accession S71590 !'##molecule_type DNA !'##residues 1-148 ##label RO2 !'##cross-references EMBL:X65875; NID:g19008; PIDN:CAA46705.1; !1PID:g19009 GENETICS !$#gene Itr1 CLASSIFICATION #superfamily wheat alpha-amylase inhibitor KEYWORDS serine proteinase inhibitor FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-144 #product trypsin inhibitor CMe #status predicted !8#label MAT\ !$57 #inhibitory_site Arg (trypsin) #status predicted SUMMARY #length 148 #molecular-weight 16135 #checksum 7837 SEQUENCE /// ENTRY S18241 #type complete TITLE alpha-amylase inhibitor, tetrameric, chain CM17 precursor - wheat ORGANISM #formal_name Triticum aestivum #common_name common wheat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S18241 REFERENCE S18241 !$#authors Lullien, V.; Alary, R.; Guirao, A.; Joudrier, P.; Gautier, !1M.F. !$#journal Plant Mol. Biol. (1991) 17:1081-1082 !$#title Isolation and nucleotide sequence of a cDNA clone encoding !1the bread wheat (Triticum aestivum L.) CM17 protein. !$#cross-references MUID:92032767; PMID:1932681 !$#accession S18241 !'##status preliminary !'##molecule_type mRNA !'##residues 1-143 ##label LUL !'##cross-references EMBL:X59791; NID:g21710; PIDN:CAA42453.1; !1PID:g21711 CLASSIFICATION #superfamily wheat alpha-amylase inhibitor KEYWORDS alpha-amylase inhibitor; tetramer SUMMARY #length 143 #molecular-weight 15989 #checksum 6711 SEQUENCE /// ENTRY NWRP2 #type complete TITLE napin 2 precursor - rape ALTERNATE_NAMES 1.7S seed storage protein ORGANISM #formal_name Brassica napus #common_name rape DATE 18-Apr-1984 #sequence_revision 18-Apr-1984 #text_change 18-Jun-1999 ACCESSIONS A01329 REFERENCE A92836 !$#authors Crouch, M.L.; Tenbarge, K.M.; Simon, A.E.; Ferl, R. !$#journal J. Mol. Appl. Genet. (1983) 2:273-283 !$#title cDNA clones for Brassica napus seed storage proteins: !1evidence from nucleotide sequence analysis that both !1subunits of napin are cleaved from a precursor polypeptide. !$#cross-references MUID:84113267; PMID:6689334 !$#accession A01329 !'##molecule_type mRNA !'##residues 1-178 ##label CRO !'##cross-references GB:K01545; NID:g167176; PIDN:AAA33006.1; !1PID:g167177 !'##experimental_source cv. Tower COMMENT The small, basic, water-soluble napins are one of the two !1major kinds of storage proteins synthesized in the seed !1during its maturation. The mature protein consists of a !1small and a large chain linked by disulfide bonds. CLASSIFICATION #superfamily wheat alpha-amylase inhibitor KEYWORDS seed; storage protein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-38 #domain propeptide #status predicted #label PRO\ !$39-74 #product napin 2 small chain #status predicted #label !8SCH\ !$95-175 #product napin 2 large chain #status predicted #label !8LCH SUMMARY #length 178 #molecular-weight 20130 #checksum 9882 SEQUENCE /// ENTRY NWRP1 #type fragment TITLE napin 1 precursor - rape (fragment) ALTERNATE_NAMES 1.7S seed storage protein ORGANISM #formal_name Brassica napus #common_name rape DATE 18-Apr-1984 #sequence_revision 18-Apr-1984 #text_change 18-Jun-1999 ACCESSIONS A01330 REFERENCE A92836 !$#authors Crouch, M.L.; Tenbarge, K.M.; Simon, A.E.; Ferl, R. !$#journal J. Mol. Appl. Genet. (1983) 2:273-283 !$#title cDNA clones for Brassica napus seed storage proteins: !1evidence from nucleotide sequence analysis that both !1subunits of napin are cleaved from a precursor polypeptide. !$#cross-references MUID:84113267; PMID:6689334 !$#accession A01330 !'##molecule_type mRNA !'##residues 1-133 ##label CRO !'##cross-references GB:K01544; NID:g167174; PIDN:AAA33005.1; !1PID:g167175 !'##experimental_source cv. Tower CLASSIFICATION #superfamily wheat alpha-amylase inhibitor KEYWORDS seed; storage protein FEATURE !$1-30 #product napin 1 small chain (fragment) #status !8predicted #label SCH\ !$50-130 #product napin 1 large chain #status predicted #label !8LCH SUMMARY #length 133 #checksum 8223 SEQUENCE /// ENTRY NWMU1 #type complete TITLE 2S albumin 1 precursor - Arabidopsis thaliana ALTERNATE_NAMES seed storage protein AT2S1 ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Dec-1999 ACCESSIONS JA0161; PS0282; S34676; T06044 REFERENCE JA0161 !$#authors Krebbers, E.; Herdies, L.; de Clercq, A.; Seurinck, J.; !1Leemans, J.; Van Damme, J.; Segura, M.; Gheysen, G.; Van !1Montagu, M.; Vandekerckhove, J. !$#journal Plant Physiol. (1988) 87:859-866 !$#title Determination of the processing sites of an Arabidopsis 2S !1albumin and characterization of the complete gene family. !$#accession JA0161 !'##molecule_type DNA !'##residues 1-164 ##label KRE !'##cross-references GB:M22032; NID:g166609; PIDN:AAA32743.1; !1PID:g166614 !$#accession PS0282 !'##molecule_type protein !'##residues 38-73;84-162 ##label KR2 REFERENCE S34674 !$#authors Conceicao, A.D.S.; Krebbers, E. !$#submission submitted to the EMBL Data Library, July 1993 !$#description Tentative title: a cotyledon regulatory region is !1responsible for the different spatial expression patterns of !1Arabidopsis 2S albumin genes. !$#accession S34676 !'##molecule_type DNA !'##residues 1-164 ##label CON !'##cross-references EMBL:Z24745; NID:g395203; PIDN:CAA80870.1; !1PID:g395204 REFERENCE Z15484 !$#authors Bevan, M.; Van Der Schueren, J.; Chuang, Y.J.; Voet, M.; !1Robben, J.; Volckaert, G.; Bancroft, I.; Mewes, H.W.; Mayer, !1K.F.X.; Schueller, C. !$#submission submitted to the Protein Sequence Database, March 1999 !$#accession T06044 !'##molecule_type DNA !'##residues 1-164 ##label BEV !'##cross-references EMBL:AL035680; GSPDB:GN00062; ATSP:T24A18.90 !'##experimental_source cultivar Columbia; BAC clone T24A18 GENETICS !$#gene T24A18.90 !$#map_position 4 CLASSIFICATION #superfamily wheat alpha-amylase inhibitor KEYWORDS seed; storage protein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-164 #product 2S albumin 1 proprotein #status predicted !8#label AT2\ !$38-73 #product 2S albumin 1 small chain #status !8experimental #label SMC\ !$84-162 #product 2S albumin 1 large chain #status !8experimental #label LAC SUMMARY #length 164 #molecular-weight 19014 #checksum 7503 SEQUENCE /// ENTRY NWMU2 #type complete TITLE 2S albumin 2 precursor - Arabidopsis thaliana ALTERNATE_NAMES seed storage protein AT2S2 ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Dec-1999 ACCESSIONS JA0162; S34677; T06045 REFERENCE JA0161 !$#authors Krebbers, E.; Herdies, L.; de Clercq, A.; Seurinck, J.; !1Leemans, J.; Van Damme, J.; Segura, M.; Gheysen, G.; Van !1Montagu, M.; Vandekerckhove, J. !$#journal Plant Physiol. (1988) 87:859-866 !$#title Determination of the processing sites of an Arabidopsis 2S !1albumin and characterization of the complete gene family. !$#accession JA0162 !'##molecule_type DNA !'##residues 1-170 ##label KRE !'##cross-references GB:M22034; NID:g166610; PIDN:AAA32744.1; !1PID:g166615 REFERENCE S34674 !$#authors Conceicao, A.D.S.; Krebbers, E. !$#submission submitted to the EMBL Data Library, July 1993 !$#description Tentative title: a cotyledon regulatory region is !1responsible for the different spatial expression patterns of !1Arabidopsis 2S albumin genes. !$#accession S34677 !'##molecule_type DNA !'##residues 1-170 ##label CON !'##cross-references EMBL:Z24745; NID:g395203; PIDN:CAA80871.1; !1PID:g395205 REFERENCE Z15484 !$#authors Bevan, M.; Van Der Schueren, J.; Chuang, Y.J.; Voet, M.; !1Robben, J.; Volckaert, G.; Bancroft, I.; Mewes, H.W.; Mayer, !1K.F.X.; Schueller, C. !$#submission submitted to the Protein Sequence Database, March 1999 !$#accession T06045 !'##molecule_type DNA !'##residues 1-170 ##label BEV !'##cross-references EMBL:AL035680; GSPDB:GN00062; ATSP:T24A18.100 !'##experimental_source cultivar Columbia; BAC clone T24A18 GENETICS !$#gene T24A18.100 !$#map_position 4 CLASSIFICATION #superfamily wheat alpha-amylase inhibitor KEYWORDS seed; storage protein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-170 #product 2S albumin 2 proprotein #status predicted !8#label AT2\ !$38-72 #product 2S albumin 2 small chain #status predicted !8#label SMC\ !$89-169 #product 2S albumin 2 large chain #status predicted !8#label LAC SUMMARY #length 170 #molecular-weight 19361 #checksum 3182 SEQUENCE /// ENTRY NWMU3 #type complete TITLE 2S albumin 3 precursor - Arabidopsis thaliana ALTERNATE_NAMES seed storage protein AT2S3 ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 10-May-2001 ACCESSIONS JA0163; S34674; PN0174; T06046 REFERENCE JA0161 !$#authors Krebbers, E.; Herdies, L.; de Clercq, A.; Seurinck, J.; !1Leemans, J.; Van Damme, J.; Segura, M.; Gheysen, G.; Van !1Montagu, M.; Vandekerckhove, J. !$#journal Plant Physiol. (1988) 87:859-866 !$#title Determination of the processing sites of an Arabidopsis 2S !1albumin and characterization of the complete gene family. !$#accession JA0163 !'##molecule_type DNA !'##residues 1-164 ##label KRE !'##cross-references GB:M22035; NID:g166611; PIDN:AAA32745.1; !1PID:g166616 REFERENCE S34674 !$#authors Conceicao, A.D.S.; Krebbers, E. !$#submission submitted to the EMBL Data Library, July 1993 !$#description Tentative title: a cotyledon regulatory region is !1responsible for the different spatial expression patterns of !1Arabidopsis 2S albumin genes. !$#accession S34674 !'##molecule_type DNA !'##residues 1-164 ##label CON !'##cross-references EMBL:Z24744; NID:g395200; PIDN:CAA80868.1; !1PID:g395201 REFERENCE PN0173 !$#authors Tsugita, A.; Kamo, M.; Kawakami, M.; Ohki, Y. !$#submission submitted to JIPID, December 1995 !$#description Two dimensional electrophoresis of plant proteins and !1standardization of the gel patterns. !$#accession PN0174 !'##molecule_type protein !'##residues 81-94 ##label TSU !'##experimental_source seeds REFERENCE Z15484 !$#authors Bevan, M.; Van Der Schueren, J.; Chuang, Y.J.; Voet, M.; !1Robben, J.; Volckaert, G.; Bancroft, I.; Mewes, H.W.; Mayer, !1K.F.X.; Schueller, C. !$#submission submitted to the Protein Sequence Database, March 1999 !$#accession T06046 !'##molecule_type DNA !'##residues 1-164 ##label BEV !'##cross-references EMBL:AL035680; GSPDB:GN00062; ATSP:T24A18.110 !'##experimental_source cultivar Columbia; BAC clone T24A18 GENETICS !$#gene T24A18.110 !$#map_position 4 CLASSIFICATION #superfamily wheat alpha-amylase inhibitor KEYWORDS seed; storage protein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-164 #product 2S albumin 3 proprotein #status predicted !8#label AT2\ !$38-72 #product 2S albumin 3 small chain #status predicted !8#label SMC\ !$82-162 #product 2S albumin 3 large chain #status predicted !8#label LAC SUMMARY #length 164 #molecular-weight 18762 #checksum 419 SEQUENCE /// ENTRY NWMU4 #type complete TITLE 2S albumin 4 precursor - Arabidopsis thaliana ALTERNATE_NAMES seed storage protein AT2S4 ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Dec-1999 ACCESSIONS JA0164; S34675; T06047 REFERENCE JA0161 !$#authors Krebbers, E.; Herdies, L.; de Clercq, A.; Seurinck, J.; !1Leemans, J.; Van Damme, J.; Segura, M.; Gheysen, G.; Van !1Montagu, M.; Vandekerckhove, J. !$#journal Plant Physiol. (1988) 87:859-866 !$#title Determination of the processing sites of an Arabidopsis 2S !1albumin and characterization of the complete gene family. !$#accession JA0164 !'##molecule_type DNA !'##residues 1-166 ##label KRE !'##cross-references GB:M22033; NID:g166612; PIDN:AAA32746.1; !1PID:g166617 REFERENCE S34674 !$#authors Conceicao, A.D.S.; Krebbers, E. !$#submission submitted to the EMBL Data Library, July 1993 !$#description Tentative title: a cotyledon regulatory region is !1responsible for the different spatial expression patterns of !1Arabidopsis 2S albumin genes. !$#accession S34675 !'##molecule_type DNA !'##residues 1-166 ##label CON !'##cross-references EMBL:Z24744; NID:g395200; PIDN:CAA80869.1; !1PID:g395202 REFERENCE Z15484 !$#authors Bevan, M.; Van Der Schueren, J.; Chuang, Y.J.; Voet, M.; !1Robben, J.; Volckaert, G.; Bancroft, I.; Mewes, H.W.; Mayer, !1K.F.X.; Schueller, C. !$#submission submitted to the Protein Sequence Database, March 1999 !$#accession T06047 !'##molecule_type DNA !'##residues 1-166 ##label BEV !'##cross-references EMBL:AL035680; GSPDB:GN00062; ATSP:T24A18.120 !'##experimental_source cultivar Columbia; BAC clone T24A18 GENETICS !$#gene T24A18.120 !$#map_position 4 CLASSIFICATION #superfamily wheat alpha-amylase inhibitor KEYWORDS seed; storage protein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-166 #product 2S albumin 4 proprotein #status predicted !8#label 2SA\ !$38-72 #product 2S albumin 4 small chain #status predicted !8#label SMC\ !$89-164 #product 2S albumin 4 large chain #status predicted !8#label LAC SUMMARY #length 166 #molecular-weight 19169 #checksum 7158 SEQUENCE /// ENTRY WMRZ19 #type complete TITLE 19K globulin precursor - rice ALTERNATE_NAMES alpha-globulin ORGANISM #formal_name Oryza sativa #common_name rice DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 18-Jun-1999 ACCESSIONS S20024; S25735; PN0497 REFERENCE S20024 !$#authors Shorrosh, B.S.; Wen, L.; Zen, K.C.; Huang, J.K.; Pan, J.S.; !1Hermodson, M.A.; Tanaka, K.; Muthukrishnan, S.; Reeck, G.R. !$#journal Plant Mol. Biol. (1992) 18:151-154 !$#title A novel cereal storage protein: molecular genetics of the 19 !1kDa globulin of rice. !$#cross-references MUID:92119226; PMID:1731968 !$#accession S20024 !'##molecule_type mRNA !'##residues 1-186 ##label SHO !'##cross-references EMBL:X63990; NID:g20158; PIDN:CAA45400.1; !1PID:g20159 !$#accession S25735 !'##molecule_type protein !'##residues 66-74;108-133;171-186 ##label SH2 REFERENCE PN0497 !$#authors Krishnan, H.B.; Pueppke, S.G. !$#journal Biochem. Biophys. Res. Commun. (1993) 193:460-466 !$#title Nucleotide sequence of an abundant rice seed globulin: !1homology with the high molecular weight glutelins of wheat, !1rye and triticale. !$#cross-references MUID:93277591; PMID:8503935 !$#accession PN0497 !'##molecule_type mRNA !'##residues 6-186 ##label KRI !'##cross-references GB:L12252 !'##experimental_source seed CLASSIFICATION #superfamily wheat alpha-amylase inhibitor KEYWORDS storage protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-186 #product 19K globulin #status predicted #label MAT SUMMARY #length 186 #molecular-weight 21050 #checksum 1252 SEQUENCE /// ENTRY WISMAA #type complete TITLE alpha-amylase inhibitor AI-3688 - Streptomyces aureofaciens ORGANISM #formal_name Streptomyces aureofaciens DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 17-Feb-1995 ACCESSIONS A01331 REFERENCE A01331 !$#authors Vertesy, L.; Tripier, D. !$#journal FEBS Lett. (1985) 185:187-190 !$#title Isolation and structure elucidation of an alpha-amylase !1inhibitor, AI-3688, from Streptomyces aureofaciens. !$#cross-references MUID:85204394; PMID:2581812 !$#accession A01331 !'##molecule_type protein !'##residues 1-36 ##label VER !'##experimental_source FH1656, strain DSM 2790 COMMENT This protein is an effective inhibitor of pancreatic !1alpha-amylase, forming a 1:1 stoichiometric complex with the !1enzyme. It is five times less effective against human !1salivary amylase and does not inhibit the B. subtilis !1enzyme. Inhibition is pH-independent but does require an !1intact disulfide bond. CLASSIFICATION #superfamily Streptomyces alpha-amylase inhibitor KEYWORDS alpha-amylase inhibitor FEATURE !$14-18 #region inhibitory #status predicted\ !$9-25 #disulfide_bonds #status experimental SUMMARY #length 36 #molecular-weight 3938 #checksum 2743 SEQUENCE /// ENTRY WISMAT #type complete TITLE alpha-amylase inhibitor precursor - Streptomyces tendae ALTERNATE_NAMES tendamistat ORGANISM #formal_name Streptomyces tendae DATE 18-Aug-1982 #sequence_revision 31-Mar-1993 #text_change 18-Jun-1999 ACCESSIONS A33961; A01332 REFERENCE A33961 !$#authors Koller, K.P.; Riess, G. !$#journal J. Bacteriol. (1989) 171:4953-4957 !$#title Heterologous expression of the alpha-amylase inhibitor gene !1cloned from an amplified genomic sequence of Streptomyces !1tendae. !$#cross-references MUID:89359132; PMID:2788646 !$#accession A33961 !'##molecule_type DNA !'##residues 1-104 ##label KOL !'##cross-references GB:M28478; NID:g153137; PIDN:AAA26686.1; !1PID:g153138 !'##note the authors translated the codon CAG for residue 59 as Glu REFERENCE A01332 !$#authors Aschauer, H.; Vertesy, L.; Nesemann, G.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1983) 364:1347-1356 !$#title The primary structure of the alpha-amylase inhibitor Hoe467A !1from Streptomyces tendae 4158. A new class of inhibitors. !$#cross-references MUID:84059634; PMID:6605909 !$#accession A01332 !'##molecule_type protein !'##residues 31-58,'E',60-104 ##label ASC !'##experimental_source strain 4158 CLASSIFICATION #superfamily Streptomyces alpha-amylase inhibitor KEYWORDS alpha-amylase inhibitor FEATURE !$1-30 #domain signal sequence #status predicted #label SIG\ !$31-104 #product alpha-amylase inhibitor #status predicted !8#label MAT\ !$46-50 #region inhibitory #status predicted\ !$41-57,75-103 #disulfide_bonds #status experimental SUMMARY #length 104 #molecular-weight 10759 #checksum 2159 SEQUENCE /// ENTRY WISMAG #type complete TITLE alpha-amylase inhibitor - Streptomyces griseosporeus ALTERNATE_NAMES haim II ORGANISM #formal_name Streptomyces griseosporeus DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 31-Dec-1993 ACCESSIONS A01333 REFERENCE A01333 !$#authors Murai, H.; Hara, S.; Ikenaka, T.; Goto, A.; Arai, M.; Murao, !1S. !$#journal J. Biochem. (1985) 97:1129-1133 !$#title Amino acid sequence of protein alpha-amylase inhibitor from !1Streptomyces griseosporeus YM-25. !$#cross-references MUID:85289094; PMID:3875608 !$#accession A01333 !'##molecule_type protein !'##residues 1-77 ##label MUR !'##experimental_source strain YM-25 CLASSIFICATION #superfamily Streptomyces alpha-amylase inhibitor KEYWORDS alpha-amylase inhibitor FEATURE !$11-15 #region inhibitory #status predicted\ !$6-22,40-67 #disulfide_bonds #status experimental SUMMARY #length 77 #molecular-weight 8033 #checksum 3169 SEQUENCE /// ENTRY IABY3 #type complete TITLE proteinase A inhibitor 3 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YM8010.04c; protein YMR174c ORGANISM #formal_name Saccharomyces cerevisiae DATE 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 21-Jul-2000 ACCESSIONS A01334; S16692; S55121 REFERENCE A01334 !$#authors Biedermann, K.; Montali, U.; Martin, B.; Svendsen, I.; !1Ottesen, M. !$#journal Carlsberg Res. Commun. (1980) 45:225-235 !$#title The amino acid sequence of proteinase A inhibitor 3 from !1baker's yeast. !$#accession A01334 !'##molecule_type protein !'##residues 1-68 ##label BIE !'##note nearly all of the inhibitory activity is present in the peptide !1consisting of residues 2-33 REFERENCE S16692 !$#authors Schu, P.; Wolf, D.H. !$#journal FEBS Lett. (1991) 283:78-84 !$#title The proteinase yscA-inhibitor, I(A)(3), gene. Studies of !1cytoplasmic proteinase inhibitor deficiency on yeast !1physiology. !$#cross-references MUID:91243884; PMID:2037077 !$#accession S16692 !'##molecule_type DNA !'##residues 1-68 ##label SCH !'##cross-references EMBL:X60050; NID:g4094; PIDN:CAA42650.1; PID:g4095 REFERENCE S55118 !$#authors Churcher, C.M. !$#submission submitted to the EMBL Data Library, June 1995 !$#accession S55121 !'##molecule_type DNA !'##residues 1-68 ##label CHU !'##cross-references EMBL:Z49808; NID:g854440; PIDN:CAA89907.1; !1PID:g854444; GSPDB:GN00013; MIPS:YMR174c !'##experimental_source strain AB972 GENETICS !$#gene SGD:PAI3; MIPS:YMR174c !'##cross-references SGD:S0004786; MIPS:YMR174c !$#map_position 13R CLASSIFICATION #superfamily proteinase A inhibitor 3 KEYWORDS acetylated amino end; blocked amino end; proteinase !1inhibitor FEATURE !$1 #modified_site acetylated amino end (Met) #status !8experimental SUMMARY #length 68 #molecular-weight 7707 #checksum 9740 SEQUENCE /// ENTRY YBBY2 #type complete TITLE proteinase B inhibitor 2 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein N2844; protein YNL015w; proteinase B inhibitor 1 ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Nov-1980 #sequence_revision 23-Feb-1996 #text_change 16-Jun-2000 ACCESSIONS S16882; A01335; S62927; A90215 REFERENCE S16882 !$#authors Schu, P.; Suarez Rendueles, P.; Wolf, D.H. !$#journal Eur. J. Biochem. (1991) 197:1-7 !$#title The proteinase yscB inhibitor (PBI2) gene of yeast and !1studies on the function of its protein product. !$#cross-references MUID:91200033; PMID:2015812 !$#accession S16882 !'##molecule_type DNA !'##residues 1-75 ##label SCH !'##cross-references EMBL:X60051; NID:g4104; PIDN:CAA42651.1; PID:g4105 REFERENCE A92246 !$#authors Maier, K.; Muller, H.; Tesch, R.; Trolp, R.; Witt, I.; !1Holzer, H. !$#journal J. Biol. Chem. (1979) 254:12555-12561 !$#title Primary structure of yeast proteinase B inhibitor 2. !$#accession A01335 !'##molecule_type protein !'##residues 2-32,'L',34-75 ##label MAI REFERENCE S62920 !$#authors Andre, B.; Iraqui Houssaini, I.; Urrestarazu, L.A.; Vissers, !1S. !$#submission submitted to the Protein Sequence Database, April 1996 !$#accession S62927 !'##molecule_type DNA !'##residues 1-75 ##label AND !'##cross-references EMBL:Z71291; NID:g1301838; PIDN:CAA95876.1; !1PID:g1301839; GSPDB:GN00014; MIPS:YNL015w !'##experimental_source strain S288C REFERENCE A90215 !$#authors Maier, K.; Muller, H.; Tesch, R.; Witt, I.; Holzer, H. !$#journal Biochem. Biophys. Res. Commun. (1979) 91:1390-1398 !$#title Amino acid sequence of yeast proteinse B inhibitor 1 !1comparison with inhibitor 2. !$#cross-references MUID:80109301; PMID:393265 !$#accession A90215 !'##molecule_type protein !'##residues 2-34,'K',36-75 ##label MAW COMMENT The proteinase B inhibitors are found in the cytosol, !1whereas proteinase B is in the vacuole. Probably these !1inhibitors regulate proteinase B activity during limited !1proteolysis. GENETICS !$#gene SGD:PBI2; MIPS:YNL015w !'##cross-references SGD:S0004960; MIPS:YNL015w !$#map_position 14L CLASSIFICATION #superfamily proteinase B inhibitor 2 KEYWORDS proteinase inhibitor SUMMARY #length 75 #molecular-weight 8590 #checksum 7772 SEQUENCE /// ENTRY C69973 #type complete TITLE ribonuclease inhibitor homolog yrdF - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69973; T44775 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69973 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-91 ##label KUN !'##cross-references GB:Z99117; GB:AL009126; NID:g2634966; !1PIDN:CAB14614.1; PID:g2635118 !'##experimental_source strain 168 REFERENCE Z22837 !$#authors Belitsky, B.R.; Gustafsson, M.C.U.; Sonenshein, A.L.; von !1Wachenfeldt, C. !$#journal J. Bacteriol. (1997) 179:5448-5457 !$#title An lrp-like gene of Bacillus subtilis involved in !1branched-chain amino acid transport. !$#cross-references MUID:97431495; PMID:9287000 !$#accession T44775 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-91 ##label BEL !'##cross-references EMBL:Y11043; NID:g1926275; PIDN:CAA71938.1; !1PID:g1926279 !'##experimental_source strain 1A1 GENETICS !$#gene yrdF CLASSIFICATION #superfamily Bacillus ribonuclease inhibitor SUMMARY #length 91 #molecular-weight 10728 #checksum 9299 SEQUENCE /// ENTRY S01373 #type complete TITLE ribonuclease inhibitor - Bacillus amyloliquefaciens ALTERNATE_NAMES barstar ORGANISM #formal_name Bacillus amyloliquefaciens DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S01373 REFERENCE S01372 !$#authors Hartley, R.W. !$#journal J. Mol. Biol. (1988) 202:913-915 !$#title Barnase and barstar. Expression of its cloned inhibitor !1permits expression of a cloned ribonuclease. !$#cross-references MUID:89012012; PMID:3050134 !$#accession S01373 !'##molecule_type DNA !'##residues 1-90 ##label HAR !'##cross-references EMBL:X15545; NID:g1155006; PIDN:CAA33551.1; !1PID:g39312 CLASSIFICATION #superfamily Bacillus ribonuclease inhibitor SUMMARY #length 90 #molecular-weight 10343 #checksum 9055 SEQUENCE /// ENTRY IWBO #type complete TITLE ATPase inhibitor precursor, mitochondrial - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 19-Feb-1984 #sequence_revision 28-Apr-1995 #text_change 18-Jun-1999 ACCESSIONS C27382; A01336 REFERENCE A90527 !$#authors Walker, J.E.; Gay, N.J.; Powell, S.J.; Kostina, M.; Dyer, !1M.R. !$#journal Biochemistry (1987) 26:8613-8619 !$#title ATP synthase from bovine mitochondria: sequences of imported !1precursors of oligomycin sensitivity conferral protein, !1factor 6, and adenosinetriphosphatase inhibitor protein. !$#cross-references MUID:88163536; PMID:2894843 !$#accession C27382 !'##molecule_type mRNA !'##residues 1-109 ##label WAL !'##cross-references GB:M22559; NID:g162712; PIDN:AAA30396.1; !1PID:g162713 REFERENCE A01336 !$#authors Frangione, B.; Rosenwasser, E.; Penefsky, H.S.; Pullman, !1M.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:7403-7407 !$#title Amino acid sequence of the protein inhibitor of !1mitochondrial adenosine triphosphatase. !$#cross-references MUID:82150878; PMID:6461003 !$#accession A01336 !'##molecule_type protein !'##residues 26-54,'Q',56-109 ##label FRA !'##note there are several internal duplications near the carboxyl end !1(residues 73-97) COMMENT This peptide is thought to be a regulatory component of the !1ATP-synthesizing complex in the mitochondria. CLASSIFICATION #superfamily ATPase inhibitor, mitochondrial KEYWORDS ATPase inhibitor; mitochondrion FEATURE !$1-25 #domain transit peptide (mitochondrion) #status !8predicted #label SIG\ !$26-109 #product ATPase inhibitor #status experimental #label !8MAT SUMMARY #length 109 #molecular-weight 12301 #checksum 4929 SEQUENCE /// ENTRY JS0738 #type complete TITLE ATPase inhibitor precursor, mitochondrial - rat ALTERNATE_NAMES H+-ATP synthase ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 23-Mar-2001 ACCESSIONS JS0738; S30182; S30387 REFERENCE JS0739 !$#authors Higuti, T.; Kuroiwa, K.; Kawamura, Y.; Tsujita, H. !$#submission submitted to JIPID, September 1992 !$#description Molecular cloning of cDNA for the import precursor of rat !1ATPase inhibitor protein of H+-ATP synthase in mitochondria. !$#accession JS0738 !'##molecule_type mRNA !'##residues 1-107 ##label HIG !'##cross-references DDBJ:D13122; NID:g286197; PIDN:BAA02424.1; !1PID:g286198 !'##experimental_source hepatocyte, cell line H4TG REFERENCE S30181 !$#authors Higuti, T.; Kuroiwa, K.; Kawamura, Y.; Morimoto, K.; !1Tsujita, H. !$#journal Biochim. Biophys. Acta (1993) 1172:311-314 !$#title Molecular cloning and sequence of cDNAs for the import !1precursors of oligomycin sensitivity conferring protein, !1ATPase inhibitor protein, and subunit c of H(+)-ATP synthase !1in rat mitochondria. !$#cross-references MUID:93192323; PMID:8448208 !$#accession S30182 !'##status preliminary !'##molecule_type mRNA !'##residues 1-107 ##label HIG2 !'##cross-references GB:D13122; NID:g286197; PIDN:BAA02424.1; !1PID:g286198 REFERENCE S30387 !$#authors Lebowitz, M.S.; Pedersen, P.L. !$#journal Arch. Biochem. Biophys. (1993) 301:64-70 !$#title Regulation of the mitochondrial ATP synthase/ATPase complex: !1cDNA cloning, sequence, overexpression, and secondary !1structural characterization of a functional protein !1inhibitor. !$#cross-references MUID:93183021; PMID:8442667 !$#accession S30387 !'##status preliminary !'##molecule_type mRNA !'##residues 1,'TK',4,'CRIEAST',12-107 ##label LEB !'##cross-references EMBL:L07806; NID:g204681; PIDN:AAA41360.1; !1PID:g204682 CLASSIFICATION #superfamily ATPase inhibitor, mitochondrial KEYWORDS ATPase inhibitor; mitochondrion FEATURE !$1-25 #domain transit peptide (mitochondrion) #status !8predicted #label TRP\ !$26-107 #product ATPase inhibitor #status predicted #label !8MAT SUMMARY #length 107 #molecular-weight 12248 #checksum 7928 SEQUENCE /// ENTRY IWBY #type complete TITLE H+-transporting ATP synthase inhibitor precursor, mitochondrial - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein D1305; protein YDL181w ORGANISM #formal_name Saccharomyces cerevisiae DATE 02-Apr-1982 #sequence_revision 31-Dec-1993 #text_change 21-Jul-2000 ACCESSIONS A35231; A01337; A19978; S58736; S67733; S67736 REFERENCE A35231 !$#authors Ichikawa, N.; Yoshida, Y.; Hashimoto, T.; Ogasawara, N.; !1Yoshikawa, H.; Imamoto, F.; Tagawa, K. !$#journal J. Biol. Chem. (1990) 265:6274-6278 !$#title Activation of ATP hydrolysis by an uncoupler in mutant !1mitochondria lacking an intrinsic ATPase inhibitor in yeast. !$#cross-references MUID:90202902; PMID:2138617 !$#accession A35231 !'##molecule_type DNA !'##residues 1-85 ##label ICH !'##cross-references GB:D00443; NID:g218434; PIDN:BAA00344.1; !1PID:g218435 REFERENCE A01337 !$#authors Matsubara, H.; Hase, T.; Hashimoto, T.; Tagawa, K. !$#journal J. Biochem. (1981) 90:1159-1165 !$#title A stabilizing factor of yeast mitochondrial F(1)F !1(0)-ATPase-inhibitor complex: common amino acid sequence !1with yeast ATPase inhibitor and E.coli epsilon and bovine !1gamma subunits. !$#cross-references MUID:82075741; PMID:6458601 !$#accession A01337 !'##molecule_type protein !'##residues 23-85 ##label MATS REFERENCE A19978 !$#authors Yoshida, Y.; Hashimoto, T.; Hase, T.; Matsubara, H.; Tagawa, !1K. !$#journal J. Biochem. (1983) 94:291-297 !$#title Partial amino terminal sequence of the precursor of !1mitochondrial ATPase inhibitor protein synthesized with mRNA !1partially purified by gel permeation chromatography. !$#cross-references MUID:84008110; PMID:6619114 !$#accession A19978 !'##molecule_type protein !'##residues 1-2,'SX',5,'X',7,'LX',10-11,'X',13,'XS',16,'XXXXX',23,'X', !125-26,'X',28 ##label YOS REFERENCE S58730 !$#authors Verhasselt, P.; Voet, M.; Volckaert, G. !$#journal Yeast (1995) 11:961-966 !$#title New open reading frames, one of which is similar to the nifV !1gene of Azotobacter vinelandii, found on a 12.5 kbp fragment !1of chromosome IV of Saccharomyces cerevisiae. !$#cross-references MUID:96021607; PMID:8533471 !$#accession S58736 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-85 ##label VER !'##cross-references EMBL:X83276; NID:g1004294; PIDN:CAA58265.1; !1PID:g1004313 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1994 REFERENCE S67708 !$#authors Pohl, T.M. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67733 !'##molecule_type DNA !'##residues 1-85 ##label POH !'##cross-references EMBL:Z74229; NID:g1431292; PIDN:CAA98755.1; !1PID:g1431293; GSPDB:GN00004; MIPS:YDL181w !'##experimental_source strain S288C REFERENCE S67735 !$#authors Volckaert, G.; Verhasselt, P.; Voet, M. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67736 !'##molecule_type DNA !'##residues 1-85 ##label VOL !'##cross-references EMBL:Z74229; NID:g1431292; PIDN:CAA98755.1; !1PID:g1431293; GSPDB:GN00004; MIPS:YDL181w !'##experimental_source strain S288C COMMENT This protein forms a one-to-one complex with ATP synthase to !1inhibit the enzyme activity completely. GENETICS !$#gene SGD:INH1; MIPS:YDL181w !'##cross-references SGD:S0002340; MIPS:YDL181w !$#map_position 4L !$#genome nuclear CLASSIFICATION #superfamily ATPase inhibitor, mitochondrial KEYWORDS mitochondrion FEATURE !$1-22 #domain transit peptide (mitochondrion) #status !8experimental #label TNP\ !$23-85 #product H+-transporting ATP synthase inhibitor !8#status experimental #label MAT SUMMARY #length 85 #molecular-weight 9870 #checksum 6684 SEQUENCE /// ENTRY IWBY9 #type complete TITLE ATPase-stabilizing factor 10K precursor, mitochondrial - yeast (Saccharomyces cerevisiae) ORGANISM #formal_name Saccharomyces cerevisiae DATE 19-Feb-1984 #sequence_revision 30-Jun-1992 #text_change 19-Apr-2002 ACCESSIONS JX0048; A01338; S25428 REFERENCE JX0048 !$#authors Akashi, A.; Yoshida, Y.; Nakagoshi, H.; Kuroki, K.; !1Hashimoto, T.; Tagawa, K.; Imamoto, F. !$#journal J. Biochem. (1988) 104:526-530 !$#title Molecular cloning and expression of a gene for a factor !1which stabilizes formation of inhibitor-mitochondrial ATPase !1complex from Saccharomyces cerevisiae. !$#cross-references MUID:89197851; PMID:2907329 !$#accession JX0048 !'##molecule_type DNA !'##residues 1-86 ##label AKA !'##cross-references GB:D00347; NID:g218387; PIDN:BAA00256.1; !1PID:g218388 REFERENCE A01338 !$#authors Matsubara, H.; Inoue, K.; Hashimoto, T.; Yoshida, Y.; !1Tagawa, K. !$#journal J. Biochem. (1983) 94:315-318 !$#title A stabilizing factor of yeast mitochondrial !1F1F0-ATPase-inhibitor complex: common amino acid sequence !1with yeast ATPase inhibitor and E. coli epsilon and bovine !1delta subunits. !$#cross-references MUID:84008115; PMID:6194151 !$#accession A01338 !'##molecule_type protein !'##residues 24-86 ##label MATS GENETICS !'##cross-references SGD:S0007232 CLASSIFICATION #superfamily ATPase inhibitor, mitochondrial KEYWORDS mitochondrion FEATURE !$1-23 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$24-86 #product ATPase stabilizing factor 10K #status !8experimental #label MAT SUMMARY #length 86 #molecular-weight 10062 #checksum 8361 SEQUENCE /// ENTRY S12201 #type complete TITLE ATP synthase regulatory factor, 15K - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein G3858; protein YGR008c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S12201; S64297 REFERENCE S12201 !$#authors Yoshida, Y.; Sato, T.; Hashimoto, T.; Ichikawa, N.; Nakai, !1S.; Yoshikawa, H.; Imamoto, F.; Tagawa, K. !$#journal Eur. J. Biochem. (1990) 192:49-53 !$#title Isolation of a gene for a regulatory 15-kDa subunit of !1mitochondrial F(1)F(0)-ATPase and construction of mutant !1yeast lacking the protein. !$#cross-references MUID:90382454; PMID:2169416 !$#accession S12201 !'##molecule_type DNA !'##residues 1-84 ##label YOS !'##cross-references EMBL:D00444; NID:g218497; PIDN:BAA00345.1; !1PID:g218498 REFERENCE S64003 !$#authors Hebling, U.; Hofmann, B.; Delius, H. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64297 !'##molecule_type DNA !'##residues 1-84 ##label HEB !'##cross-references EMBL:Z72793; NID:g1322966; PIDN:CAA96991.1; !1PID:g1322967; GSPDB:GN00007; MIPS:YGR008c !'##experimental_source strain S288C GENETICS !$#gene SGD:STF2; MIPS:YGR008c !'##cross-references SGD:S0003240; MIPS:YGR008c !$#map_position 7R CLASSIFICATION #superfamily ATP synthase regulatory factor, 15K KEYWORDS mitochondrion SUMMARY #length 84 #molecular-weight 9615 #checksum 1900 SEQUENCE /// ENTRY A40424 #type complete TITLE phospholamban - human ORGANISM #formal_name Homo sapiens #common_name man DATE 28-Feb-1992 #sequence_revision 27-Jun-1994 #text_change 18-Jun-1999 ACCESSIONS A40424 REFERENCE A40424 !$#authors Fujii, J.; Zarain-Herzberg, A.; Willard, H.F.; Tada, M.; !1MacLennan, D.H. !$#journal J. Biol. Chem. (1991) 266:11669-11675 !$#title Structure of the rabbit phospholamban gene, cloning of the !1human cDNA, and assignment of the gene to human chromosome !16. !$#cross-references MUID:91268032; PMID:1828805 !$#accession A40424 !'##molecule_type mRNA !'##residues 1-52 ##label FUJ !'##cross-references GB:M63603; NID:g189942; PIDN:AAA60083.1; !1PID:g189943 COMMENT Phospholamban is expressed in cardiac muscle, slow twitch !1skeletal muscle, and smooth muscle. COMMENT Phospholamban is the major phosphorylated protein in cardiac !1muscle sarcoplasmic reticulum after beta-adrenergic !1stimulation. The unphosphorylated form binds to and inhibits !1the Ca++-ATPase; after phosphorylation, the Ca++ pump is !1activated and the rate of muscle relaxation increases. COMMENT Helical transmembrane domains of five chains are thought to !1aggregate in the sarcoplamic membrane, with their !1amino-terminal polar regions extending into the sarcoplasm. GENETICS !$#gene GDB:PLN; PLB !'##cross-references GDB:128300; OMIM:172405 !$#map_position 6q22.1-6q22.1 CLASSIFICATION #superfamily phospholamban KEYWORDS acetylated amino end; ATPase inhibitor; muscle; pentamer; !1phosphoprotein; transmembrane protein FEATURE !$31-52 #domain transmembrane #status predicted #label TMM\ !$1 #modified_site acetylated amino end (Met) #status !8predicted\ !$16 #binding_site phosphate (Ser) (covalent) (by !8cAMP-dependent kinase) #status predicted\ !$17 #binding_site phosphate (Thr) (covalent) (by !8calmodulin-dependent kinase) #status predicted SUMMARY #length 52 #molecular-weight 6108 #checksum 3813 SEQUENCE /// ENTRY S37638 #type complete TITLE phospholamban - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 05-Mar-1994 #sequence_revision 27-Jun-1994 #text_change 18-Jun-1999 ACCESSIONS S37638; I52270; I64795; I51840 REFERENCE S37637 !$#authors Shanahan, C.M.; Weissberg, P.L.; Metcalfe, J.C. !$#journal Circ. Res. (1993) 73:193-204 !$#title Isolation of gene markers of differentiated and !1proliferating vascular smooth muscle cells. !$#cross-references MUID:93284726; PMID:8508530 !$#accession S37638 !'##molecule_type mRNA !'##residues 1-52 ##label SHA !'##cross-references EMBL:X71068; NID:g313809; PIDN:CAA50394.1; !1PID:g313810 REFERENCE I52270 !$#authors Johns, D.C.; Feldman, A.M. !$#journal Biochem. Biophys. Res. Commun. (1992) 188:927-933 !$#title Identification of a highly conserved region at the 5' flank !1of the phospholamban gene. !$#cross-references MUID:93075183; PMID:1445334 !$#accession I52270 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-52 ##label JOH !'##cross-references GB:L03382; NID:g206134; PIDN:AAA41849.1; !1PID:g206136 REFERENCE I51840 !$#authors Hwang, K.S.; Nadal-Ginard, B. !$#journal Adv. Exp. Med. Biol. (1991) 304:387-395 !$#title Cloning phospholamban cDNA from rat aortic smooth muscle. !$#cross-references MUID:92206263; PMID:1725098 !$#accession I64795 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-52 ##label HWA1 !'##cross-references GB:S95853; NID:g247932; PIDN:AAB21903.1; !1PID:g247933 !$#accession I51840 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-52 ##label HWA2 !'##cross-references GB:S95849; NID:g247934 COMMENT Phospholamban is expressed in cardiac muscle, slow twitch !1skeletal muscle, and smooth muscle. COMMENT Phospholamban is the major phosphorylated protein in cardiac !1muscle sarcoplasmic reticulum after beta-adrenergic !1stimulation. The unphosphorylated form binds to and inhibits !1the calcium-ATPase; after phosphorylation, the calcium pump !1is activated and the rate of muscle relaxation increases. CLASSIFICATION #superfamily phospholamban KEYWORDS acetylated amino end; ATPase inhibitor; cardiac muscle; !1heart; pentamer; phosphoprotein; smooth muscle; !1transmembrane protein FEATURE !$31-52 #domain transmembrane #status predicted #label TMM\ !$1 #modified_site acetylated amino end (Met) #status !8predicted\ !$16 #binding_site phosphate (Ser) (covalent) (by !8cAMP-dependent kinase) #status predicted\ !$17 #binding_site phosphate (Thr) (covalent) (by !8calmodulin-dependent kinase) #status predicted SUMMARY #length 52 #molecular-weight 6094 #checksum 3894 SEQUENCE /// ENTRY A49057 #type complete TITLE phospholamban - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 19-Dec-1993 #sequence_revision 27-Jun-1994 #text_change 18-Jun-1999 ACCESSIONS A49057 REFERENCE A49057 !$#authors Ganim, J.R.; Luo, W.; Ponniah, S.; Grupp, I.; Kim, H.W.; !1Ferguson, D.G.; Kadambi, V.; Neumann, J.C.; Doetschman, T.; !1Kranias, E.G. !$#journal Circ. Res. (1992) 71:1021-1030 !$#title Mouse phospholamban gene expression during development in !1vivo and in vitro. !$#cross-references MUID:93008802; PMID:1394867 !$#accession A49057 !'##molecule_type mRNA !'##residues 1-52 ##label GAN !'##cross-references GB:S46792; NID:g257745; PIDN:AAB23706.1; !1PID:g257746 !'##experimental_source cardiac muscle !'##note sequence extracted from NCBI backbone (NCBIN:116999, !1NCBIP:117001) COMMENT Phospholamban is expressed in cardiac muscle, slow twitch !1skeletal muscle, and smooth muscle. COMMENT Phospholamban is the major phosphorylated protein in cardiac !1muscle sarcoplasmic reticulum after beta-adrenergic !1stimulation. The unphosphorylated form binds to and inhibits !1the Ca++-ATPase; after phosphorylation, the Ca++ pump is !1activated and the rate of muscle relaxation increases. CLASSIFICATION #superfamily phospholamban KEYWORDS acetylated amino end; ATPase inhibitor; muscle; pentamer; !1phosphoprotein; transmembrane protein FEATURE !$31-52 #domain transmembrane #status predicted #label TMM\ !$1 #modified_site acetylated amino end (Met) #status !8predicted\ !$16 #binding_site phosphate (Ser) (covalent) (by !8cAMP-dependent kinase) #status predicted\ !$17 #binding_site phosphate (Thr) (covalent) (by !8calmodulin-dependent kinase) #status predicted SUMMARY #length 52 #molecular-weight 6094 #checksum 3894 SEQUENCE /// ENTRY B40424 #type complete TITLE phospholamban - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 28-Feb-1992 #sequence_revision 27-Jun-1994 #text_change 18-Jun-1999 ACCESSIONS B40424; S00249 REFERENCE A40424 !$#authors Fujii, J.; Zarain-Herzberg, A.; Willard, H.F.; Tada, M.; !1MacLennan, D.H. !$#journal J. Biol. Chem. (1991) 266:11669-11675 !$#title Structure of the rabbit phospholamban gene, cloning of the !1human cDNA, and assignment of the gene to human chromosome !16. !$#cross-references MUID:91268032; PMID:1828805 !$#accession B40424 !'##molecule_type DNA !'##residues 1-52 ##label FUJ !'##cross-references GB:M63601; NID:g165636; PIDN:AAA31445.1; !1PID:g165639 REFERENCE S00249 !$#authors Fujii, J.; Lytton, J.; Tada, M.; MacLennan, D.H. !$#journal FEBS Lett. (1988) 227:51-55 !$#title Rabbit cardiac and slow-twitch muscle express the same !1phospholamban gene. !$#cross-references MUID:88112222; PMID:2962883 !$#accession S00249 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-52 ##label FU2 !'##cross-references GB:Y00761; NID:g1661; PIDN:CAA68730.1; PID:g1662 COMMENT Phospholamban is expressed in cardiac muscle, slow twitch !1skeletal muscle, and smooth muscle. COMMENT Phospholamban is the major phosphorylated protein in cardiac !1muscle sarcoplasmic reticulum after beta-adrenergic !1stimulation. The unphosphorylated form binds to and inhibits !1the Ca++-ATPase; after phosphorylation, the Ca++ pump is !1activated and the rate of muscle relaxation increases. GENETICS !$#note only one gene was detected !$#note the single intron is upstream of the coding region CLASSIFICATION #superfamily phospholamban KEYWORDS acetylated amino end; ATPase inhibitor; muscle; pentamer; !1phosphoprotein; transmembrane protein FEATURE !$31-52 #domain transmembrane #status predicted #label TMM\ !$1 #modified_site acetylated amino end (Met) #status !8predicted\ !$16 #binding_site phosphate (Ser) (covalent) (by !8cAMP-dependent kinase) #status predicted\ !$17 #binding_site phosphate (Thr) (covalent) (by !8calmodulin-dependent kinase) #status predicted SUMMARY #length 52 #molecular-weight 6094 #checksum 3894 SEQUENCE /// ENTRY A29002 #type complete TITLE phospholamban - dog ORGANISM #formal_name Canis lupus familiaris #common_name dog DATE 23-Aug-1987 #sequence_revision 27-Jun-1994 #text_change 18-Jun-1999 ACCESSIONS A29002; A26805; A25307; A24818; I46227 REFERENCE A29002 !$#authors Fujii, J.; Ueno, A.; Kitano, K.; Tanaka, S.; Kadoma, M.; !1Tada, M. !$#journal J. Clin. Invest. (1987) 79:301-304 !$#title Complete complementary DNA-derived amino acid sequence of !1canine cardiac phospholamban. !$#cross-references MUID:87083954; PMID:3793929 !$#accession A29002 !'##molecule_type mRNA !'##residues 1-52 ##label FUJ !'##cross-references GB:M16012; NID:g164043; PIDN:AAA30884.1; !1PID:g164044 REFERENCE A26805 !$#authors Uyeda, A.; Kitano, K.; Fujii, J.; Kadoma, M.; Tada, M.; !1Tanaka, S. !$#journal Nucleic Acids Res. (1987) 15:6738 !$#title The cDNA sequence of the major phospholamban mRNA in canine !1cardiac ventricular muscle. !$#cross-references MUID:87316936; PMID:3628007 !$#accession A26805 !'##molecule_type mRNA !'##residues 1-52 ##label UYE !'##cross-references GB:Y00399; NID:g911; PIDN:CAA68461.1; PID:g912 REFERENCE A25307 !$#authors Simmerman, H.K.B.; Collins, J.H.; Theibert, J.L.; Wegener, !1A.D.; Jones, L.R. !$#journal J. Biol. Chem. (1986) 261:13333-13341 !$#title Sequence analysis of phospholamban. Identification of !1phosphorylation sites and two major structural domains. !$#cross-references MUID:87008549; PMID:3759968 !$#contents partial sequence and phosphorylation sites !$#accession A25307 !'##molecule_type protein !'##residues 10-45 ##label SIM REFERENCE A24818 !$#authors Fujii, J.; Kadoma, M.; Tada, M.; Toda, H.; Sakiyama, F. !$#journal Biochem. Biophys. Res. Commun. (1986) 138:1044-1050 !$#title Characterization of structural unit of phospholamban by !1amino acid sequencing and electrophoretic analysis. !$#cross-references MUID:86323152; PMID:3753485 !$#contents partial sequence and acetylation site !$#accession A24818 !'##molecule_type protein !'##residues 1-35,'X',37-40,'X',42-45 ##label FU2 REFERENCE I46227 !$#authors Uyeda, A.; Kitano, K.; Fujii, J.; Kadoma, M.; Tada, M.; !1Tanaka, S. !$#journal Nucleic Acids Symp. Ser. (1986) 17:121-124 !$#title Characterization of recombinant cDNA clones for canine !1cardiac phospholamban. !$#cross-references MUID:87174860; PMID:3562256 !$#accession I46227 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-52 ##label UY2 !'##cross-references GB:M35393; NID:g164045; PIDN:AAC41618.1; !1PID:g164046 COMMENT Phospholamban is expressed in cardiac muscle, slow twitch !1skeletal muscle, and smooth muscle. COMMENT Phospholamban is the major phosphorylated protein in cardiac !1muscle sarcoplasmic reticulum after beta-adrenergic !1stimulation. The unphosphorylated form binds to and inhibits !1the Ca++-ATPase; after phosphorylation, the Ca++ pump is !1activated and the rate of muscle relaxation increases. CLASSIFICATION #superfamily phospholamban KEYWORDS acetylated amino end; ATPase inhibitor; muscle; pentamer; !1phosphoprotein; transmembrane protein FEATURE !$31-52 #domain transmembrane #status predicted #label TMM\ !$1 #modified_site acetylated amino end (Met) #status !8experimental\ !$16 #binding_site phosphate (Ser) (covalent) (by !8cAMP-dependent kinase) #status experimental\ !$17 #binding_site phosphate (Thr) (covalent) (by !8calmodulin-dependent kinase) #status experimental SUMMARY #length 52 #molecular-weight 6080 #checksum 3892 SEQUENCE /// ENTRY S05540 #type complete TITLE phospholamban - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 21-Nov-1993 #sequence_revision 27-Jun-1994 #text_change 18-Jun-1999 ACCESSIONS S05540 REFERENCE S05540 !$#authors Verboomen, H.; Wuytack, F.; Eggermont, J.A.; de Jaegere, S.; !1Missiaen, L.; Raeymaekers, L.; Casteels, R. !$#journal Biochem. J. (1989) 262:353-356 !$#title cDNA cloning and sequencing of phospholamban from pig !1stomach smooth muscle. !$#cross-references MUID:90056437; PMID:2530978 !$#accession S05540 !'##molecule_type mRNA !'##residues 1-52 ##label VER !'##cross-references EMBL:X15075; NID:g2055; PIDN:CAA33171.1; PID:g2056 COMMENT Phospholamban is expressed in cardiac muscle, slow twitch !1skeletal muscle, and smooth muscle. COMMENT Phospholamban is the major phosphorylated protein in cardiac !1muscle sarcoplasmic reticulum after beta-adrenergic !1stimulation. The unphosphorylated form binds to and inhibits !1the Ca++-ATPase; after phosphorylation, the Ca++ pump is !1activated and the rate of muscle relaxation increases. CLASSIFICATION #superfamily phospholamban KEYWORDS acetylated amino end; ATPase inhibitor; muscle; pentamer; !1phosphoprotein; transmembrane protein FEATURE !$31-52 #domain transmembrane #status predicted #label TMM\ !$1 #modified_site acetylated amino end (Met) #status !8predicted\ !$16 #binding_site phosphate (Ser) (covalent) (by !8cAMP-dependent kinase) #status predicted\ !$17 #binding_site phosphate (Thr) (covalent) (by !8calmodulin-dependent kinase) #status predicted SUMMARY #length 52 #molecular-weight 6080 #checksum 3892 SEQUENCE /// ENTRY A39535 #type complete TITLE phospholamban - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 06-Mar-1992 #sequence_revision 27-Jun-1994 #text_change 18-Jun-1999 ACCESSIONS A39535; B39535; A44531 REFERENCE A39535 !$#authors Toyofuku, T.; Zak, R. !$#journal J. Biol. Chem. (1991) 266:5375-5383 !$#title Characterization of cDNA and genomic sequences encoding a !1chicken phospholamban. !$#cross-references MUID:91170195; PMID:1825996 !$#accession A39535 !'##molecule_type mRNA !'##residues 1-17,'L',19-52 ##label TOY !'##cross-references GB:M59039; NID:g212575; PIDN:AAA62738.1; !1PID:g212576 !'##note the authors translated the codon CTT for residue 18 as Ile !$#accession B39535 !'##molecule_type DNA !'##residues 1-52 ##label TO2 !'##cross-references GB:M59038 !'##note the sequence of residues 33-52 and the corresponding nucleotide !1sequence are not shown REFERENCE A44531 !$#authors Toyofuku, T.; Zak, R. !$#submission submitted to GenBank, April 1991 !$#accession A44531 !'##molecule_type DNA !'##residues 1-52 ##label TO3 !'##cross-references GB:M59038 COMMENT Phospholamban is expressed in cardiac muscle, slow twitch !1skeletal muscle, and smooth muscle. COMMENT Phospholamban is the major phosphorylated protein in cardiac !1muscle sarcoplasmic reticulum after beta-adrenergic !1stimulation. The unphosphorylated form binds to and inhibits !1the Ca++-ATPase; after phosphorylation, the Ca++ pump is !1activated and the rate of muscle relaxation increases. GENETICS !$#note only one gene was detected !$#note the single intron is upstream of the coding region CLASSIFICATION #superfamily phospholamban KEYWORDS acetylated amino end; ATPase inhibitor; muscle; pentamer; !1phosphoprotein; transmembrane protein FEATURE !$31-52 #domain transmembrane #status predicted #label TMM\ !$1 #modified_site acetylated amino end (Met) #status !8predicted\ !$16 #binding_site phosphate (Ser) (covalent) (by !8cAMP-dependent kinase) #status predicted\ !$17 #binding_site phosphate (Thr) (covalent) (by !8calmodulin-dependent kinase) #status predicted SUMMARY #length 52 #molecular-weight 6091 #checksum 4292 SEQUENCE /// ENTRY PZRB1 #type complete TITLE protein phosphatase inhibitor 1 - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 17-Dec-1982 #sequence_revision 31-Dec-1988 #text_change 09-Aug-1997 ACCESSIONS A91120; A94639; S02271; A01339; A30015 REFERENCE A91120 !$#authors Aitken, A.; Bilham, T.; Cohen, P. !$#journal Eur. J. Biochem. (1982) 126:235-246 !$#title Complete primary structure of protein phosphatase !1inhibitor-1 from rabbit skeletal muscle. !$#cross-references MUID:83027314; PMID:6290217 !$#accession A91120 !'##molecule_type protein !'##residues 1-163,165-166 ##label AIT !'##note residues 163 was the carboxyl end in 40% of the molecules !'##note the CNBr peptide comprising residues 2-66 retains the full !1inhibitory activity of this protein REFERENCE A94639 !$#authors Aitken, A. !$#submission submitted to the Protein Sequence Database, October 1988 !$#accession A94639 !'##molecule_type protein !'##residues 1-166 ##label AI2 REFERENCE A91305 !$#authors Aitken, A.; Cohen, P. !$#journal FEBS Lett. (1982) 147:54-58 !$#title Isolation and characterisation of active fragments of !1protein phosphatase inhibitor-1 from rabbit skeletal muscle. !$#cross-references MUID:83054004; PMID:7140990 !$#contents annotation; fragment activities !$#note a peptide comprising residues 9-54 retains the full activity !1of the protein; residues 9-22 are essential for activity; a !1region within residues 42-54 may be essential for activity REFERENCE S02271 !$#authors MacDougall, L.K.; Campbell, D.G.; Hubbard, M.J.; Cohen, P. !$#journal Biochim. Biophys. Acta (1989) 1010:218-226 !$#title Partial structure and hormonal regulation of rabbit liver !1inhibitor-1; distribution of inhibitor-1 and inhibitor-2 in !1rabbit and rat tissues. !$#cross-references MUID:89105609; PMID:2912504 !$#accession S02271 !'##molecule_type protein !'##residues 2-45;61-96;135-166 ##label MAC COMMENT This protein may be important in hormonal control of !1glycogen metabolism. Phosphorylation of Thr-35, which is !1required for inhibitor activity, increases in response to !1adrenalin and decreases in response to insulin. The !1phosphorylation of Ser-67 and one other Thr, possibly 75, !1are not required for inhibitor activity. CLASSIFICATION #superfamily protein phosphatase inhibitor 1 KEYWORDS acetylated amino end; phosphoprotein; protein phosphatase !1inhibitor FEATURE !$1 #modified_site acetylated amino end (Met) #status !8experimental\ !$35 #binding_site phosphate (Thr) (covalent) (by !8cAMP-dependent kinase) #status experimental\ !$67 #binding_site phosphate (Ser) (covalent) (by !8cAMP-dependent kinase) (partial) #status !8experimental\ !$75 #binding_site phosphate (Thr) (covalent) #status !8predicted SUMMARY #length 166 #molecular-weight 18032 #checksum 6736 SEQUENCE /// ENTRY A40468 #type complete TITLE cyclic AMP-dependent protein kinase inhibitor - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A40468 REFERENCE A40468 !$#authors Olsen, S.R.; Uhler, M.D. !$#journal Mol. Endocrinol. (1991) 5:1246-1256 !$#title Inhibition of protein kinase-A by overexpression of the !1cloned human protein kinase inhibitor. !$#cross-references MUID:92123220; PMID:1770951 !$#accession A40468 !'##status preliminary !'##molecule_type DNA !'##residues 1-76 ##label OLS !'##cross-references GB:S76765 CLASSIFICATION #superfamily cAMP-dependent protein kinase inhibitor SUMMARY #length 76 #molecular-weight 7988 #checksum 6380 SEQUENCE /// ENTRY OKRBCI #type complete TITLE cAMP-dependent protein kinase inhibitor - rabbit ALTERNATE_NAMES PKI ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 24-Nov-1999 ACCESSIONS A01340 REFERENCE A94057 !$#authors Scott, J.D.; Fischer, E.H.; Takio, K.; Demaille, J.G.; !1Krebs, E.G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:5732-5736 !$#title Amino acid sequence of the heat-stable inhibitor of the !1cAMP-dependent protein kinase from rabbit skeletal muscle. !$#cross-references MUID:85298234; PMID:3898070 !$#accession A01340 !'##molecule_type protein !'##residues 1-75 ##label SCO !'##experimental_source skeletal muscle REFERENCE A94050 !$#authors Scott, J.D.; Fischer, E.H.; Demaille, J.G.; Krebs, E.G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:4379-4383 !$#title Identification of an inhibitory region of the heat-stable !1protein inhibitor of the cAMP-dependent protein kinase. !$#cross-references MUID:85242688; PMID:2989819 !$#contents annotation; inhibitory site COMMENT An extremely potent competitive inhibitor of cAMP-dependent !1protein kinase activity, this protein interacts with the !1catalytic subunit of the enzyme after the cAMP-induced !1dissociation of its regulatory chains. COMMENT The inhibitory region contains sequences very similar to the !1hinge regions (sites that directly interact with the enzyme !1active site) and "pseudosubstrate site" of the regulatory !1chains but, unlike these chains, PKI does not contain !1cAMP-binding sites. The arginine residues within the !1inhibitory region are essential for inhibition and !1recognition of the enzyme active site. CLASSIFICATION #superfamily cAMP-dependent protein kinase inhibitor KEYWORDS blocked amino end; protein kinase inhibitor FEATURE !$11-30 #region inhibitory\ !$1 #modified_site blocked amino end (Thr) (probably !8acetylated) #status experimental SUMMARY #length 75 #molecular-weight 7857 #checksum 5352 SEQUENCE /// ENTRY A46224 #type complete TITLE 3',5'-cyclic adenosine monophosphate-dependent protein kinase inhibitor alpha isoform - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A46224 REFERENCE A46224 !$#authors Van Patten, S.M.; Howard, P.; Walsh, D.A.; Maurer, R.A. !$#journal Mol. Endocrinol. (1992) 6:2114-2122 !$#title The alpha- and beta-isoforms of the inhibitor protein of the !13',5'-cyclic adenosine monophosphate-dependent protein !1kinase: characteristics and tissue- and !1developmental-specific expression. !$#cross-references MUID:93149120; PMID:1491692 !$#accession A46224 !'##status preliminary !'##molecule_type mRNA !'##residues 1-76 ##label VAN !'##experimental_source brain !'##note sequence extracted from NCBI backbone (NCBIN:123680, !1NCBIP:123681) CLASSIFICATION #superfamily cAMP-dependent protein kinase inhibitor SUMMARY #length 76 #molecular-weight 7988 #checksum 6380 SEQUENCE /// ENTRY A40536 #type complete TITLE cAMP-dependent protein kinase inhibitor - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A40536 REFERENCE A40536 !$#authors Olsen, S.R.; Uhler, M.D. !$#journal J. Biol. Chem. (1991) 266:11158-11162 !$#title Isolation and characterization of cDNA clones for an !1inhibitor protein of cAMP-dependent protein kinase. !$#cross-references MUID:91250427; PMID:1710219 !$#accession A40536 !'##status preliminary !'##molecule_type mRNA !'##residues 1-76 ##label OLS !'##cross-references GB:M65554 CLASSIFICATION #superfamily cAMP-dependent protein kinase inhibitor SUMMARY #length 76 #molecular-weight 7960 #checksum 6662 SEQUENCE /// ENTRY JC4128 #type complete TITLE cAMP-dependent protein kinase inhibitor - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JC4128 REFERENCE JC4128 !$#authors Marchetto, G.S.; Henry, H.L. !$#journal Gene (1995) 158:303-304 !$#title Cloning and sequencing of the cDNA encoding the avian kidney !1cAMP-dependent protein kinase inhibitor protein. !$#cross-references MUID:95331636; PMID:7607559 !$#accession JC4128 !'##molecule_type mRNA !'##residues 1-76 ##label MAR !'##cross-references GB:U19496; NID:g632651; PIDN:AAA86697.1; !1PID:g632652 !'##experimental_source kidney COMMENT This protein is a specific and potent competitive inhibitor !1of the catalytic subunit of the cAMP-dependent protein !1kinase. It plays an important role in regulating !1cAMP-dependent protein kinase activity under physiological !1conditions. CLASSIFICATION #superfamily cAMP-dependent protein kinase inhibitor KEYWORDS kidney; protein kinase inhibitor FEATURE !$18-22 #region pseudosubstrate site #status predicted SUMMARY #length 76 #molecular-weight 8007 #checksum 6498 SEQUENCE /// ENTRY S52485 #type complete TITLE glucokinase regulator - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S52485 REFERENCE S52485 !$#authors Bonthron, D.T.; Intody, S.; Warner, J.P. !$#submission submitted to the EMBL Data Library, February 1995 !$#description Human glucokinase. !$#accession S52485 !'##status preliminary !'##molecule_type mRNA !'##residues 1-625 ##label BON !'##cross-references EMBL:Z48475; NID:g683571; PIDN:CAA88367.1; !1PID:g683572 GENETICS !$#gene GDB:GCKR !'##cross-references GDB:207312; OMIM:600842 !$#map_position 2p23.3-2p23.2 CLASSIFICATION #superfamily glucokinase regulator SUMMARY #length 625 #molecular-weight 68688 #checksum 5443 SEQUENCE /// ENTRY S41745 #type complete TITLE glucokinase regulator - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S41745 REFERENCE S41745 !$#authors Detheux, M.; Vandekerckhove, J.; van Schaftingen, E. !$#journal FEBS Lett. (1994) 339:312-315 !$#title Cloning and sequencing of rat liver cDNAs encoding the !1regulatory protein of glucokinase. !$#cross-references MUID:94156054; PMID:8112473 !$#accession S41745 !'##molecule_type mRNA !'##residues 1-627 ##label DET CLASSIFICATION #superfamily glucokinase regulator SUMMARY #length 627 #molecular-weight 68917 #checksum 3983 SEQUENCE /// ENTRY S48729 #type complete TITLE glucokinase regulator - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S48729; S49339 REFERENCE S48729 !$#authors Veiga-da-Cunha, M.; Detheux, M.; Watelet, N.; van !1Schaftingen, E. !$#journal Eur. J. Biochem. (1994) 225:43-51 !$#title Cloning and expression of a Xenopus liver cDNA encoding a !1fructose-phosphate-insensitive regulatory protein of !1glucokinase. !$#cross-references MUID:95010134; PMID:7925465 !$#accession S48729 !'##status preliminary !'##molecule_type mRNA !'##residues 1-619 ##label VEI !'##cross-references EMBL:X80901; NID:g556677; PIDN:CAA56863.1; !1PID:g556678 CLASSIFICATION #superfamily glucokinase regulator SUMMARY #length 619 #molecular-weight 68738 #checksum 8568 SEQUENCE /// ENTRY XEYDGD #type complete TITLE galactose oxidase inhibitor - fungus (Cladobotryum dendroides) ORGANISM #formal_name Cladobotryum dendroides DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 31-Dec-1993 ACCESSIONS A01341 REFERENCE A01341 !$#authors Avigad, G.; Markus, Z. !$#journal Fed. Proc. (1972) 31:447 !$#accession A01341 !'##molecule_type protein !'##residues 1-7 ##label AVI COMMENT The mycelia of this imperfect fungus produce the !1metalloenzyme galactose oxidase and its peptide inhibitor. !1The inhibitor, which can bind one copper ion per molecule !1and does not bind the apoenzyme, may inactivate the enzyme !1by binding to its prosthetic copper group. CLASSIFICATION #superfamily galactose oxidase inhibitor KEYWORDS copper SUMMARY #length 7 #molecular-weight 706 #checksum 2177 SEQUENCE /// ENTRY TVFVAF #type complete TITLE transforming protein maf - avian retrovirus AS42 ORGANISM #formal_name avian retrovirus AS42 DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 28-Feb-1997 ACCESSIONS B33975 REFERENCE A33975 !$#authors Nishizawa, M.; Kataoka, K.; Goto, N.; Fujiwara, K.T.; Kawai, !1S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:7711-7715 !$#title v-maf, a viral oncogene that encodes a "leucine zipper" !1motif. !$#cross-references MUID:90046665; PMID:2554284 !$#accession B33975 !'##molecule_type DNA !'##residues 1-369 ##label NIS GENETICS !$#gene maf CLASSIFICATION #superfamily maf transforming protein; maf homology KEYWORDS DNA binding; leucine zipper; nucleus; transcription !1regulation; transforming protein FEATURE !$248-337 #domain maf homology #label MAF\ !$302-323 #region leucine zipper motif SUMMARY #length 369 #molecular-weight 38892 #checksum 8250 SEQUENCE /// ENTRY TVHUMB #type complete TITLE transforming protein myb, splice form containing exon 9A - human CONTAINS transforming protein myb, normal splice form ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1990 #sequence_revision 15-Aug-1997 #text_change 21-Jul-2000 ACCESSIONS A26661; A41952; S11197; I59517; I80450; I58400; S08492 REFERENCE A26661 !$#authors Majello, B.; Kenyon, L.C.; Dalla-Favera, R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:9636-9640 !$#title Human c-myb protooncogene: nucleotide sequence of cDNA and !1organization of the genomic locus. !$#cross-references MUID:87092302; PMID:3540945 !$#accession A26661 !'##molecule_type mRNA !'##residues 1-401,523-631,'F',633-683,'R',685-761 ##label MAJ !'##cross-references GB:M15024; NID:g180659; PIDN:AAA52032.1; !1PID:g180660 REFERENCE A41952 !$#authors Nicolaides, N.C.; Gualdi, R.; Casadevall, C.; Manzella, L.; !1Calabretta, B. !$#journal Mol. Cell. Biol. (1991) 11:6166-6176 !$#title Positive autoregulation of c-myb expression via myb binding !1sites in the 5' flanking region of the human c-myb gene. !$#cross-references MUID:92049347; PMID:1944282 !$#accession A41952 !'##status translation not shown !'##molecule_type DNA !'##residues 1-7 ##label NIC !'##cross-references GB:S66422; NID:g238956; PIDN:AAD13983.1; !1PID:g4261683 REFERENCE S11197 !$#authors Westin, E.H.; Gorse, K.M.; Clarke, M.F. !$#journal Oncogene (1990) 5:1117-1124 !$#title Alternative splicing of the human c-myb gene. !$#cross-references MUID:90363543; PMID:2202948 !$#accession S11197 !'##status preliminary !'##molecule_type mRNA !'##residues 1-313,317-401,523-761 ##label WES !'##cross-references EMBL:X52125; NID:g29988; PIDN:CAA36371.1; !1PID:g29989 REFERENCE I59517 !$#authors Slamon, D.J.; Boone, T.C.; Murdock, D.C.; Keith, D.E.; !1Press, M.F.; Larson, R.A.; Souza, L.M. !$#journal Science (1986) 233:347-351 !$#title Studies of the human c-myb gene and its product in human !1acute leukemias. !$#cross-references MUID:86261774; PMID:3014652 !$#accession I59517 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 47-401,523-761 ##label RES !'##cross-references GB:M13665; NID:g180655; PIDN:AAA52030.1; !1PID:g180656 !$#accession I80450 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 47-316,'VRLSSCA' ##label RE3 !'##cross-references GB:M13666; NID:g180657; PIDN:AAA52031.1; !1PID:g180658 REFERENCE I58400 !$#authors Jacobs, S.M.; Gorse, K.M.; Westin, E.H. !$#journal Oncogene (1994) 9:227-235 !$#title Identification of a second promoter in the human c-myb !1proto-oncogene. !$#cross-references MUID:94134419; PMID:8302584 !$#accession I58400 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-47 ##label RE2 !'##cross-references GB:M95584; NID:g402703; PIDN:AAA72118.1; !1PID:g402704 REFERENCE S08492 !$#authors Dasgupta, P.; Reddy, E.P. !$#journal Oncogene (1989) 4:1419-1423 !$#title Identification of alternatively spliced transcripts for !1human c-myb: molecular cloning and sequence analysis of !1human c-myb exon 9A sequences. !$#cross-references MUID:90082412; PMID:2687764 !$#accession S08492 !'##status preliminary !'##molecule_type mRNA !'##residues 398-537 ##label DAS !'##cross-references EMBL:X17469; NID:g29987; PIDN:CAA35503.1; !1PID:g930049 !'##note the authors translated the codon TTT for residue 433 as Leu GENETICS !$#gene GDB:MYB !'##cross-references GDB:119441; OMIM:189990 !$#map_position 6q22-6q22 !$#introns 8/2 !$#note list of introns is incomplete !$#note expression is complex and can involve intermolecular !1recombination of coding sequences from different chromosomes FUNCTION !$#description transcription regulation; essential for hematopoiesis; !1probably has tissue-specific roles in cellular !1differentiation !$#note phosphorylation by casein kinase II reduces DNA binding !1activity; oncogenic forms are missing these phosphorylation !1sites CLASSIFICATION #superfamily myb transforming protein; myb DNA-binding !1repeat homology KEYWORDS alternative initiators; alternative splicing; DNA binding; !1duplication; nucleus; phosphoprotein; proto-oncogene; !1transcription regulation FEATURE !$1-401,523-761 #product transforming protein myb, normal splice form !8#status predicted #label MYB\ !$35-86 #domain myb DNA-binding repeat homology #label MYB1\ !$87-138 #domain myb DNA-binding repeat homology #label MYB2\ !$139-189 #domain myb DNA-binding repeat homology #label MYB3\ !$275-325 #region myb response element transcription !8activation\ !$11,12 #binding_site phosphate (Ser) (covalent) (by casein !8kinase II) #status predicted SUMMARY #length 761 #molecular-weight 85508 #checksum 5120 SEQUENCE /// ENTRY TVMSMB #type complete TITLE transforming protein myb, normal form - mouse ALTERNATE_NAMES C-myb protein ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Jun-2000 ACCESSIONS A25285; A23939; A93630; I59075; I53245; S07545; I49626 REFERENCE A25285 !$#authors Gonda, T.J.; Gough, N.M.; Dunn, A.R.; de Blaquiere, J. !$#journal EMBO J. (1985) 4:2003-2008 !$#title Nucleotide sequence of cDNA clones of the murine myb !1proto-oncogene. !$#cross-references MUID:86055758; PMID:2998780 !$#accession A25285 !'##molecule_type mRNA !'##residues 1-636 ##label GON !'##cross-references GB:X02774; NID:g50464; PIDN:CAA26552.1; PID:g50466 REFERENCE A23939 !$#authors Bender, T.P.; Kuehl, W.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:3204-3208 !$#title Murine myb protooncogene mRNA: cDNA sequence and evidence !1for 5' heterogeneity. !$#cross-references MUID:86205865; PMID:3010282 !$#accession A23939 !'##molecule_type mRNA !'##residues 1-104,'E',106-200,'E',202-266,'A',268-410,'S',412-499,'Q', !1501-524,'E',526-636 ##label BEN !'##cross-references GB:M12848; NID:g199934; PIDN:AAB59713.1; !1PID:g199935 REFERENCE A93630 !$#authors Lavu, S.; Reddy, E.P. !$#journal Nucleic Acids Res. (1986) 14:5309-5320 !$#title Structural organization and nucleotide sequence of mouse !1c-myb oncogene: activation in ABPL tumors is due to viral !1integration in an intron which results in the deletion of !1the 5' coding sequences. !$#cross-references MUID:86286545; PMID:3016644 !$#accession A93630 !'##molecule_type DNA !'##residues 72-104,'E',106-200,'E',202-401 ##label LAV !'##cross-references GB:X04099; NID:g50448; PIDN:CAA27724.1; !1PID:g1197517 !'##note the authors translated the codon CAG for residue 355 as Glu REFERENCE I59075 !$#authors Weinstein, Y.; Ihle, J.N.; Lavu, S.; Reddy, E.P. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:5010-5014 !$#title Truncation of the c-myb gene by a retroviral integration in !1an interleukin 3-dependent myeloid leukemia cell line. !$#cross-references MUID:86259723; PMID:3014527 !$#accession I59075 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 388-401,'V' ##label WEI !'##cross-references GB:K03547; NID:g199939; PIDN:AAA39786.1; !1PID:g554244 !'##note this sequence is referred to by the authors as the rearranged !1c-myb DNA (R-Locus); the complete translation is not shown REFERENCE I53245 !$#authors Watson, R.J.; Dyson, P.J.; McMahon, J. !$#journal EMBO J. (1987) 6:1643-1651 !$#title Multiple c-myb transcript cap sites are variously utilized !1in cells of mouse haemopoietic origin. !$#cross-references MUID:87275857; PMID:3608990 !$#accession I53245 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-7 ##label WAT !'##cross-references GB:M20210; NID:g199932; PIDN:AAA39783.1; !1PID:g554243 REFERENCE S07545 !$#authors Sobieszczuk, P.W.; Gonda, T.J.; Dunn, A.R. !$#journal Nucleic Acids Res. (1989) 17:9593-9611 !$#title Structure and biological activity of the transcriptional !1initiation sequences of the murine c-myb oncogene. !$#cross-references MUID:90098830; PMID:2481264 !$#accession S07545 !'##molecule_type DNA !'##residues 1-47 ##label SOB !'##cross-references EMBL:X16389; NID:g50460; PIDN:CAA34425.1; !1PID:g581950; EMBL:X16390; NID:g50461; PID:g1333883 REFERENCE I49626 !$#authors Reddy, C.D.; Reddy, E.P. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:7326-7330 !$#title Differential binding of nuclear factors to intron-1 !1containing the transcriptional pause site correlates with !1c-myb expression. !$#cross-references MUID:90017472; PMID:2678098 !$#accession I49626 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-8,'S',9-11 ##label RED !'##cross-references GB:M26185; NID:g192883; PIDN:AAA37505.1; !1PID:g553904 !'##note the authors show a different acceptor splice boundary for the !1first exon GENETICS !$#gene myb !$#introns 8/2; 102/3; 176/2; 254/3; 281/3; 316/3 !$#note list of introns is incomplete !$#note expression is complex and can involve intermolecular !1recombination of coding sequences from different chromosomes FUNCTION !$#description transcription regulation; essential for hematopoiesis; !1probably has various tissue-specific roles in cellular !1differentiation !$#note phosphorylation by casein kinase II reduces DNA binding !1activity; oncogenic forms are missing these phosphorylation !1sites CLASSIFICATION #superfamily myb transforming protein; myb DNA-binding !1repeat homology KEYWORDS alternative initiators; alternative splicing; DNA binding; !1duplication; leucine zipper; nucleus; phosphoprotein; !1proto-oncogene; transcription regulation FEATURE !$35-86 #domain myb DNA-binding repeat homology #label MYB1\ !$87-138 #domain myb DNA-binding repeat homology #label MYB2\ !$139-189 #domain myb DNA-binding repeat homology #label MYB3\ !$275-325 #region myb response element transcription !8activation\ !$383-403 #region leucine zipper motif\ !$11,12 #binding_site phosphate (Ser) (covalent) (by casein !8kinase II) #status predicted SUMMARY #length 636 #molecular-weight 71417 #checksum 5181 SEQUENCE /// ENTRY A55073 #type complete TITLE transforming protein myb, normal splice form - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 23-Mar-1995 #sequence_revision 23-Mar-1995 #text_change 16-Jun-2000 ACCESSIONS A55073; B55073; C55073 REFERENCE A55073 !$#authors Ishiguro, N.; Ohzono, T.; Shinagawa, T.; Horiuchi, M.; !1Shinagawa, M. !$#journal J. Biol. Chem. (1994) 269:26822-26829 !$#title A spontaneous internal deletion of the c-myb protooncogene !1enhances transcriptional activation in bovine T lymphoma !1cells. !$#cross-references MUID:95014544; PMID:7929419 !$#accession A55073 !'##molecule_type mRNA !'##residues 1-640 ##label ISH !'##cross-references GB:D26147; NID:g467488; PIDN:BAA05135.1; !1PID:g467489 !'##experimental_source cell line BLT2 from bovine lymphosarcoma !$#accession B55073 !'##molecule_type mRNA !'##residues 1-208,'P',210-316,402-461,'S',463-500,'V',502-570,'G', !1572-640 ##label IS2 !'##cross-references GB:D26148; NID:g442459; PIDN:BAA05136.1; !1PID:g442460 !'##experimental_source cell line BTL-PC3 from bovine lymphosarcoma !'##note deleted protein corresponds to exon 9 of human gene, which !1encodes a negative regulatory domain; this form has enhanced !1activity !$#accession C55073 !'##molecule_type mRNA !'##residues 211-362,'P',364-461,'S',463-500,'V',502-640 ##label IS3 !'##cross-references GB:D26149; NID:g442461; PIDN:BAA05137.1; !1PID:g442462 !'##experimental_source thymus GENETICS !$#note expression is complex and can involve intermolecular !1recombination of coding sequences from different chromosomes FUNCTION !$#description transcription regulation; essential for hematopoiesis; !1probably has various tissue-specific roles in cellular !1differentiation !$#note phosphorylation by casein kinase II reduces DNA binding !1activity; oncogenic forms are missing these phosphorylation !1sites CLASSIFICATION #superfamily myb transforming protein; myb DNA-binding !1repeat homology KEYWORDS alternative initiators; alternative splicing; DNA binding; !1duplication; nucleus; phosphoprotein; proto-oncogene; !1transcription regulation FEATURE !$35-86 #domain myb DNA-binding repeat homology #label MYB1\ !$87-138 #domain myb DNA-binding repeat homology #label MYB2\ !$139-189 #domain myb DNA-binding repeat homology #label MYB3\ !$275-325 #region myb response element transcription !8activation\ !$11,12 #binding_site phosphate (Ser) (covalent) (by casein !8kinase II) #status predicted SUMMARY #length 640 #molecular-weight 72511 #checksum 7769 SEQUENCE /// ENTRY TVCHM #type complete TITLE transforming protein myb, splice form containing exon 9A - chicken ALTERNATE_NAMES c-myb protein CONTAINS transforming protein myb, normal splice form ORGANISM #formal_name Gallus gallus #common_name chicken DATE 18-Apr-1984 #sequence_revision 18-Jul-1997 #text_change 18-Aug-2000 ACCESSIONS A25075; S06168; A24665; I50203; S38820; S78518; S02583; !1I50621; A01346 REFERENCE A25075 !$#authors Gerondakis, S.; Bishop, J.M. !$#journal Mol. Cell. Biol. (1986) 6:3677-3684 !$#title Structure of the protein encoded by the chicken !1proto-oncogene c-myb. !$#cross-references MUID:87089708; PMID:3025608 !$#accession A25075 !'##molecule_type mRNA !'##residues 1-402,523-761 ##label GER !'##cross-references GB:M14129; NID:g212352; PIDN:AAA48962.1; !1PID:g212353 REFERENCE S06168 !$#authors Dvorak, M.; Urbanek, P.; Bartunek, P.; Paces, V.; Vlach, J.; !1Pecenka, V.; Arnold, L.; Travnicek, M.; Riman, J. !$#journal Nucleic Acids Res. (1989) 17:5651-5664 !$#title Transcription of the chicken myb proto-oncogene starts !1within a CpG island. !$#cross-references MUID:89345158; PMID:2548166 !$#accession S06168 !'##status translation not shown !'##molecule_type DNA !'##residues 1-175 ##label DVO !'##cross-references GB:X14612; NID:g63627; PIDN:CAA32767.1; PID:g63628 REFERENCE A24665 !$#authors Rosson, D.; Reddy, P. !$#journal Nature (1986) 319:604-606 !$#title Nucleotide sequence of chicken c-myb complementary DNA and !1implications for myb oncogene activation. !$#cross-references MUID:86118729; PMID:3753748 !$#accession A24665 !'##molecule_type mRNA !'##residues 1-402,523-560,'T',562-721,'L',723-729,'G',731-734,'E', !1736-761 ##label ROS !'##cross-references GB:X03477; NID:g63245; PIDN:CAA27197.1; PID:g63246 REFERENCE I50203 !$#authors Hahn, S.L.; Hahn, M.; Hayward, W.S. !$#journal Mol. Cell. Biol. (1989) 9:837-843 !$#title Structural organization of upstream exons and distribution !1of transcription start sites in the chicken c-myb gene. !$#cross-references MUID:89219081; PMID:2710126 !$#accession I50203 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-7 ##label HAH !'##cross-references GB:M24373; NID:g211554; PIDN:AAA48697.1; !1PID:g555434 REFERENCE S38820 !$#authors Schuur, E.R.; Dasgupta, P.; Reddy, E.P.; Rabinovich, J.M.; !1Baluda, M.A. !$#journal Oncogene (1993) 8:1839-1847 !$#title Alternative splicing of the chicken c-myb exon 9A. !$#cross-references MUID:93288398; PMID:8510928 !$#accession S38820 !'##molecule_type mRNA !'##residues 403-522 ##label SCH !'##cross-references EMBL:X73660 REFERENCE S78518 !$#authors Soret, J.; Vellard, M.; Martinerie, C.; Perbal, B. !$#submission submitted to the EMBL Data Library, July 1990 !$#accession S78518 !'##molecule_type DNA !'##residues 1-79 ##label SOR !'##cross-references EMBL:M35508 !'##note Met-1 is the intitiator in thymus, Met-21 in yolk sac REFERENCE S02582 !$#authors Soret, J.; Vellard, M.; Martinerie, C.; Perbal, B. !$#journal FEBS Lett. (1988) 232:227-234 !$#title Organization of 5'-proximal c-myb exons in chicken DNA. !1Implications for c-myb tissue-specific transcription. !$#cross-references MUID:88211864; PMID:2452755 !$#accession S02583 !'##molecule_type mRNA !'##residues 'MASI';'PPAAAAR',1-13 ##label SOW !'##note the assignment of the initiator Met has been revised in S78518 REFERENCE I50621 !$#authors Urbanek, P.; Dvorak, M.; Bartunek, P.; Pecenka, V.; Paces, !1V.; Travnicek, M. !$#journal Nucleic Acids Res. (1988) 16:11521-11530 !$#title Nucleotide sequence of chicken myb proto-oncogene promoter !1region: detection of an evolutionarily conserved element. !$#cross-references MUID:89098307; PMID:3145493 !$#accession I50621 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-7,'R' ##label URB !'##cross-references EMBL:X12495; NID:g63244; PIDN:CAA31015.1; !1PID:g584468 GENETICS !$#gene myb !$#introns 8/2; 47/3; 71/3; 102/3 !$#note list of introns is incomplete !$#note expression is complex and can involve intermolecular !1recombination of coding sequences from different chromosomes FUNCTION !$#description transcription regulation; essential for hematopoiesis; !1probably has various tissue-specific roles in cellular !1differentiation !$#note phosphorylation by casein kinase II reduces DNA binding !1activity; oncogenic forms are missing these phosphorylation !1sites CLASSIFICATION #superfamily myb transforming protein; myb DNA-binding !1repeat homology KEYWORDS alternative initiators; alternative splicing; DNA binding; !1duplication; nucleus; phosphoprotein; proto-oncogene; !1transcription regulation FEATURE !$1-402,523-761 #product transforming protein myb, normal splice form !8#status predicted #label MYB\ !$35-86 #domain myb DNA-binding repeat homology #label MYB1\ !$87-138 #domain myb DNA-binding repeat homology #label MYB2\ !$139-189 #domain myb DNA-binding repeat homology #label MYB3\ !$275-325 #region myb response element transcription !8activation\ !$11,12 #binding_site phosphate (Ser) (covalent) (by casein !8kinase II) #status predicted SUMMARY #length 761 #molecular-weight 84625 #checksum 9907 SEQUENCE /// ENTRY QOYV #type complete TITLE transforming protein myb - avian myeloblastosis virus ORGANISM #formal_name avian myeloblastosis virus DATE 18-Aug-1982 #sequence_revision 11-Jul-1997 #text_change 18-Jun-1999 ACCESSIONS A36314; A90831; A94263; A01347 REFERENCE A36314 !$#authors Lane, T.; Ibanez, C.; Garcia, A.; Graf, T.; Lipsick, J. !$#journal Mol. Cell. Biol. (1990) 10:2591-2598 !$#title Transformation by v-myb correlates with trans-activation of !1gene expression. !$#cross-references MUID:90258844; PMID:2160580 !$#accession A36314 !'##status preliminary; nucleic acid sequence not shown; not compared !1with conceptual translation !'##molecule_type DNA !'##residues 1-388 ##label LAN REFERENCE A90831 !$#authors Klempnauer, K.H.; Gonda, T.J.; Bishop, J.M. !$#journal Cell (1982) 31:453-463 !$#title Nucleotide sequence of the retroviral leukemia gene v-myb !1and its cellular progenitor c-myb: the architecture of a !1transduced oncogene. !$#cross-references MUID:83129359; PMID:6297766 !$#accession A90831 !'##molecule_type DNA !'##residues 124-388 ##label KLE !'##cross-references GB:J02012; NID:g509584; PIDN:AAA42553.1; !1PID:g509585 REFERENCE A94263 !$#authors Rushlow, K.E.; Lautenberger, J.A.; Papas, T.S.; Baluda, !1M.A.; Perbal, B.; Chirikjian, J.G.; Reddy, E.P. !$#journal Science (1982) 216:1421-1423 !$#title Nucleotide sequence of the transforming gene of avian !1myeloblastosis virus. !$#cross-references MUID:82223743; PMID:6283631 !$#accession A94263 !'##molecule_type DNA !'##residues 124-388 ##label RUS !'##cross-references GB:J02013; GB:V00871; NID:g210094; PIDN:AAC15907.1; !1PID:g210096 GENETICS !$#gene myb CLASSIFICATION #superfamily myb transforming protein; myb DNA-binding !1repeat homology KEYWORDS DNA binding; transforming protein FEATURE !$22-73 #domain myb DNA-binding repeat homology #label MYB1\ !$74-124 #domain myb DNA-binding repeat homology #label MYB2 SUMMARY #length 388 #molecular-weight 43733 #checksum 7102 SEQUENCE /// ENTRY I51581 #type complete TITLE transforming protein myb - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 13-Sep-1996 #sequence_revision 13-Sep-1996 #text_change 18-Jun-1999 ACCESSIONS I51581 REFERENCE I51581 !$#authors Amaravadi, L.; King, M.W. !$#journal Oncogene (1994) 9:971-974 !$#title Characterization and expression of the Xenopus c-Myb !1homolog. !$#cross-references MUID:94151023; PMID:7509053 !$#accession I51581 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-624 ##label AMA !'##cross-references GB:L22741; NID:g460075; PIDN:AAC38011.1; !1PID:g460076 GENETICS !$#gene myb !$#note in human and chicken expression is complex and can involve !1intermolecular recombination of coding sequences from !1different chromosomes FUNCTION !$#description transcription regulation; essential for hematopoiesis; !1probably has various tissue-specific roles in cellular !1differentiation !$#note in mouse phosphorylation by casein kinase II reduces DNA !1binding activity; oncogenic forms are missing these !1phosphorylation sites CLASSIFICATION #superfamily myb transforming protein; myb DNA-binding !1repeat homology KEYWORDS alternative initiators; alternative splicing; DNA binding; !1duplication; leucine zipper; nucleus; phosphoprotein; !1proto-oncogene; transcription regulation FEATURE !$32-83 #domain myb DNA-binding repeat homology #label MYB1\ !$84-135 #domain myb DNA-binding repeat homology #label MYB2\ !$136-186 #domain myb DNA-binding repeat homology #label MYB3\ !$264-312 #region myb response element transcription !8activation\ !$9,10 #binding_site phosphate (Ser) (covalent) (by casein !8kinase II) #status predicted SUMMARY #length 624 #molecular-weight 72111 #checksum 2994 SEQUENCE /// ENTRY S03423 #type complete TITLE transforming protein A-myb - human ALTERNATE_NAMES myb-related protein A ORGANISM #formal_name Homo sapiens #common_name man DATE 28-Feb-1990 #sequence_revision 18-Jul-1997 #text_change 18-Jun-1999 ACCESSIONS S03423; S32751; I52715 REFERENCE S01991 !$#authors Nomura, N.; Takahashi, M.; Matsui, M.; Ishii, S.; Date, T.; !1Sasamoto, S.; Ishizaki, R. !$#journal Nucleic Acids Res. (1988) 16:11075-11089 !$#title Isolation of human cDNA clones of myb-related genes, A-myb !1and B-myb. !$#cross-references MUID:89083548; PMID:3060855 !$#accession S03423 !'##molecule_type mRNA !'##residues 1-745 ##label NOM !'##cross-references EMBL:X13294; NID:g28685; PIDN:CAA31656.1; !1PID:g28686 REFERENCE S32751 !$#authors Castellano, M.; Introna, M.; Golay, J. !$#submission submitted to the EMBL Data Library, May 1992 !$#accession S32751 !'##molecule_type mRNA !'##residues 398-752 ##label CAS !'##cross-references EMBL:X66087; NID:g296032; PIDN:CAA46886.1; !1PID:g825624 !'##experimental_source B cells REFERENCE I52715 !$#authors Ma, X.P.; Calabretta, B. !$#journal Cancer Res. (1994) 54:6512-6516 !$#title DNA binding and transactivation activity of A-myb, a !1c-myb-related gene. !$#cross-references MUID:95079434; PMID:7987850 !$#accession I52715 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 727-752 ##label RES !'##cross-references GB:S75881; NID:g861477; PIDN:AAB32716.1; !1PID:g861478 GENETICS !$#gene GDB:MYBL1; AMYB !'##cross-references GDB:128089; OMIM:159405 !$#map_position 8q22-8q22 FUNCTION !$#description transcription regulation; strong transcription activator; !1active in fibroblasts and spermatogonial cells CLASSIFICATION #superfamily myb transforming protein; myb DNA-binding !1repeat homology KEYWORDS DNA binding; duplication; nucleus; transcription regulation FEATURE !$30-81 #domain myb DNA-binding repeat homology #label MYB1\ !$82-133 #domain myb DNA-binding repeat homology #label MYB2\ !$134-184 #domain myb DNA-binding repeat homology #label MYB3\ !$283-286 #region nuclear location signal\ !$448-452 #region nuclear location signal\ !$692-695 #region nuclear location signal SUMMARY #length 752 #molecular-weight 85886 #checksum 1222 SEQUENCE /// ENTRY I49497 #type complete TITLE transforming protein A-myb - mouse ALTERNATE_NAMES myb-related protein A ORGANISM #formal_name Mus musculus #common_name house mouse DATE 02-Jul-1996 #sequence_revision 02-Jul-1996 #text_change 18-Jun-1999 ACCESSIONS I49497; S51794 REFERENCE I49497 !$#authors Mettus, R.V.; Litvin, J.; Wali, A.; Toscani, A.; Latham, K.; !1Hatton, K.; Reddy, E.P. !$#journal Oncogene (1994) 9:3077-3086 !$#title Murine A-myb: evidence for differential splicing and !1tissue-specific expression. !$#cross-references MUID:94366762; PMID:8084617 !$#accession I49497 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-751 ##label RES !'##cross-references GB:L35261; NID:g529726; PIDN:AAA62182.1; !1PID:g529058 REFERENCE S51794 !$#authors Trauth, K.; Mutschler, B.; Jenkins, N.A.; Gilbert, D.J.; !1Copeland, N.G.; Klempnauer, K.H. !$#journal EMBO J. (1994) 13:5994-6005 !$#title Mouse A-myb encodes a trans-activator and is expressed in !1mitotically active cells of the developing central nervous !1system, adult testis and B lymphocytes. !$#cross-references MUID:95112810; PMID:7813437 !$#accession S51794 !'##status preliminary !'##molecule_type mRNA !'##residues 1-357,'PR',360-445,'S',447-463,'SA',466-472,'RRI',476-751, !1'YCY' ##label TRA !'##cross-references EMBL:X82327; NID:g624027; PIDN:CAA57771.1; !1PID:g624028 GENETICS !$#gene A-myb FUNCTION !$#description transcription regulation; strong transcription activator; !1active in fibroblasts and spermatogonial cells CLASSIFICATION #superfamily myb transforming protein; myb DNA-binding !1repeat homology KEYWORDS DNA binding; duplication; nucleus; transcription regulation FEATURE !$30-81 #domain myb DNA-binding repeat homology #label MYB1\ !$82-133 #domain myb DNA-binding repeat homology #label MYB2\ !$134-184 #domain myb DNA-binding repeat homology #label MYB3\ !$282-285 #region nuclear location signal\ !$447-451 #region nuclear location signal\ !$691-694 #region nuclear location signal SUMMARY #length 751 #molecular-weight 85544 #checksum 2148 SEQUENCE /// ENTRY I50667 #type complete TITLE transforming protein A-myb - chicken ALTERNATE_NAMES myb-related protein A ORGANISM #formal_name Gallus gallus #common_name chicken DATE 13-Sep-1996 #sequence_revision 13-Sep-1996 #text_change 18-Jun-1999 ACCESSIONS I50667 REFERENCE I50667 !$#authors Foos, G.; Grimm, S.; Klempnauer, K.H. !$#journal Oncogene (1994) 9:2481-2488 !$#title The chicken A-myb protein is a transcriptional activator. !$#cross-references MUID:94336201; PMID:8058311 !$#accession I50667 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-757 ##label FOO !'##cross-references EMBL:X79470; NID:g558575; PIDN:CAA55980.1; !1PID:g558576 GENETICS !$#gene A-myb FUNCTION !$#description transcription regulation; strong transcription activator; !1active in fibroblasts and spermatogonial cells CLASSIFICATION #superfamily myb transforming protein; myb DNA-binding !1repeat homology KEYWORDS DNA binding; duplication; nucleus; transcription regulation FEATURE !$30-81 #domain myb DNA-binding repeat homology #label MYB1\ !$82-133 #domain myb DNA-binding repeat homology #label MYB2\ !$134-184 #domain myb DNA-binding repeat homology #label MYB3\ !$288-291 #region nuclear location signal\ !$453-457 #region nuclear location signal\ !$697-700 #region nuclear location signal SUMMARY #length 757 #molecular-weight 86008 #checksum 5171 SEQUENCE /// ENTRY S36095 #type complete TITLE transforming protein A-myb - African clawed frog ALTERNATE_NAMES myb-related protein A; transforming protein myb2 ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 18-Jun-1999 ACCESSIONS S36095; S33644 REFERENCE S36095 !$#authors Sleeman, J.P. !$#submission submitted to the EMBL Data Library, March 1993 !$#accession S36095 !'##molecule_type mRNA !'##residues 1-728 ##label SLE !'##cross-references EMBL:X72620; NID:g288274; PIDN:CAA51196.1; !1PID:g288275 REFERENCE S33643 !$#authors Bouwmeester, T.; Gueehmann, S.; El-Baradi, T.; Kalkbrenner, !1F.; van Wijk, I.; Moelling, K.; Pieler, T. !$#journal Mech. Dev. (1992) 37:57-68 !$#title Molecular cloning, expression and in vitro functional !1characterization of Myb-related proteins in Xenopus. !$#cross-references MUID:92297434; PMID:1606020 !$#accession S33644 !'##status preliminary !'##molecule_type mRNA !'##residues 1-180 ##label BOU !'##cross-references GB:X72620; NID:g288274; PIDN:CAA51196.1; !1PID:g288275 !'##note the authors translated the codon GAT for residue 146 as Val, !1CGC for residue 147 as Asp, and ATC for residue 148 as Arg GENETICS !$#gene amyb FUNCTION !$#description transcription regulation; strong transcription activator; !1active in fibroblasts and spermatogonial cells CLASSIFICATION #superfamily myb transforming protein; myb DNA-binding !1repeat homology KEYWORDS DNA binding; duplication; nucleus; transcription regulation FEATURE !$30-80 #domain myb DNA-binding repeat homology #label MYB1\ !$81-132 #domain myb DNA-binding repeat homology #label MYB2\ !$133-183 #domain myb DNA-binding repeat homology #label MYB3\ !$283-286 #region nuclear location signal\ !$436-439 #region nuclear location signal\ !$667-670 #region nuclear location signal SUMMARY #length 728 #molecular-weight 83576 #checksum 3907 SEQUENCE /// ENTRY S01991 #type complete TITLE transforming protein B-myb - human ORGANISM #formal_name Homo sapiens #common_name man DATE 28-Feb-1990 #sequence_revision 28-Feb-1990 #text_change 18-Jun-1999 ACCESSIONS S01991; S48661 REFERENCE S01991 !$#authors Nomura, N.; Takahashi, M.; Matsui, M.; Ishii, S.; Date, T.; !1Sasamoto, S.; Ishizaki, R. !$#journal Nucleic Acids Res. (1988) 16:11075-11089 !$#title Isolation of human cDNA clones of myb-related genes, A-myb !1and B-myb. !$#cross-references MUID:89083548; PMID:3060855 !$#accession S01991 !'##molecule_type mRNA !'##residues 1-700 ##label NOM !'##cross-references EMBL:X13293; NID:g29471; PIDN:CAA31655.1; !1PID:g29472 REFERENCE S48661 !$#authors Takemoto, Y.; Tashiro, S.; Handa, H.; Ishii, S. !$#journal FEBS Lett. (1994) 350:55-60 !$#title Multiple nuclear localization signals of the B-myb gene !1product. !$#cross-references MUID:94341374; PMID:8062924 !$#contents annotation; identification of nuclear location signal !1regions by mutational analysis GENETICS !$#gene GDB:MYBL2; BMYB !'##cross-references GDB:128109; OMIM:310305; OMIM:601415 !$#map_position Xq13-Xq13 FUNCTION !$#description transcription regulation; widespread activator of cell cycle !1genes; represses by inhibiting activating activity of other !1myb proteins CLASSIFICATION #superfamily myb transforming protein; myb DNA-binding !1repeat homology KEYWORDS DNA binding; duplication; nucleus; transcription regulation FEATURE !$26-77 #domain myb DNA-binding repeat homology #label MYB1\ !$78-129 #domain myb DNA-binding repeat homology #label MYB2\ !$130-180 #domain myb DNA-binding repeat homology #label MYB3\ !$411-417 #region nuclear location signal\ !$569-584 #region nuclear location signal SUMMARY #length 700 #molecular-weight 78763 #checksum 6926 SEQUENCE /// ENTRY S33704 #type complete TITLE transforming protein B-myb - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 13-Jan-1995 #sequence_revision 13-Jan-1995 #text_change 18-Jun-1999 ACCESSIONS S33704; I48269 REFERENCE S33704 !$#authors Lam, E.W.F.; Robinson, C.; Watson, R.J. !$#journal Oncogene (1992) 7:1885-1890 !$#title Characterization and cell cycle-regulated expression of !1mouse B-myb. !$#cross-references MUID:92366176; PMID:1501895 !$#accession S33704 !'##status preliminary !'##molecule_type mRNA !'##residues 1-704 ##label LAM !'##cross-references EMBL:X70472; NID:g312825; PIDN:CAA49898.1; !1PID:g312826 REFERENCE I48269 !$#authors Lam, E.W.; Watson, R.J. !$#journal EMBO J. (1993) 12:2705-2713 !$#title An E2F-binding site mediates cell-cycle regulated repression !1of mouse B-myb transcription. !$#cross-references MUID:93327760; PMID:8334989 !$#accession I48269 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-6 ##label RES !'##cross-references EMBL:X73028; NID:g297153; PIDN:CAA51511.1; !1PID:g581921 GENETICS !$#gene B-myb FUNCTION !$#description transcription regulation; widespread activator of cell cycle !1genes; represses by inhibiting activating activity of other !1myb proteins CLASSIFICATION #superfamily myb transforming protein; myb DNA-binding !1repeat homology KEYWORDS DNA binding; duplication; nucleus; transcription regulation FEATURE !$26-77 #domain myb DNA-binding repeat homology #label MYB1\ !$78-129 #domain myb DNA-binding repeat homology #label MYB2\ !$130-180 #domain myb DNA-binding repeat homology #label MYB3\ !$414-420 #region nuclear location signal\ !$573-588 #region nuclear location signal SUMMARY #length 704 #molecular-weight 79102 #checksum 9390 SEQUENCE /// ENTRY S28050 #type complete TITLE transforming protein B-myb - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 17-Apr-1993 #sequence_revision 17-Apr-1993 #text_change 18-Jun-1999 ACCESSIONS S28050 REFERENCE S28050 !$#authors Foos, G.; Grimm, S.; Klempnauer, K.H. !$#journal EMBO J. (1992) 11:4619-4629 !$#title Functional antagonism between members of the myb family: !1B-myb inhibits v-myb-induced gene activation. !$#cross-references MUID:93049214; PMID:1425593 !$#accession S28050 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-686 ##label FOO !'##cross-references EMBL:X67505; NID:g63098; PIDN:CAA47839.1; !1PID:g63099 GENETICS !$#gene B-myb FUNCTION !$#description transcription regulation; widespread activator of cell cycle !1genes; represses by inhibiting activating activity of other !1myb proteins CLASSIFICATION #superfamily myb transforming protein; myb DNA-binding !1repeat homology KEYWORDS DNA binding; duplication; nucleus; transcription regulation FEATURE !$26-77 #domain myb DNA-binding repeat homology #label MYB1\ !$78-129 #domain myb DNA-binding repeat homology #label MYB2\ !$130-180 #domain myb DNA-binding repeat homology #label MYB3\ !$392-398 #region nuclear location signal\ !$552-567 #region nuclear location signal SUMMARY #length 686 #molecular-weight 77736 #checksum 8075 SEQUENCE /// ENTRY S33643 #type complete TITLE transforming protein B-myb - African clawed frog ALTERNATE_NAMES transforming protein myb1 ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 05-Mar-1994 #sequence_revision 01-Sep-1995 #text_change 07-May-1999 ACCESSIONS S33643; S27942 REFERENCE S33643 !$#authors Bouwmeester, T.; Gueehmann, S.; El-Baradi, T.; Kalkbrenner, !1F.; van Wijk, I.; Moelling, K.; Pieler, T. !$#journal Mech. Dev. (1992) 37:57-68 !$#title Molecular cloning, expression and in vitro functional !1characterization of Myb-related proteins in Xenopus. !$#cross-references MUID:92297434; PMID:1606020 !$#accession S33643 !'##status preliminary !'##molecule_type mRNA !'##residues 1-733 ##label BOU !'##cross-references EMBL:M75870; NID:g214597; PID:g214598 GENETICS !$#gene myb1; B-myb FUNCTION !$#description transcription regulation; widespread activator of cell cycle !1genes; represses by inhibiting activating activity of other !1myb proteins CLASSIFICATION #superfamily myb transforming protein; myb DNA-binding !1repeat homology KEYWORDS DNA binding; duplication; nucleus; transcription regulation FEATURE !$26-77 #domain myb DNA-binding repeat homology #label MYB1\ !$78-129 #domain myb DNA-binding repeat homology #label MYB2\ !$130-180 #domain myb DNA-binding repeat homology #label MYB3\ !$372-375 #region nuclear location signal\ !$528-531 #region nuclear location signal SUMMARY #length 733 #molecular-weight 81791 #checksum 8565 SEQUENCE /// ENTRY TVFFMA #type complete TITLE transforming protein myb - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 18-Jun-1999 ACCESSIONS S00578; A01345 REFERENCE S00578 !$#authors Peters, C.W.B.; Sippel, A.E.; Vingron, M.; Klempnauer, K.H. !$#journal EMBO J. (1987) 6:3085-3090 !$#title Drosophila and vertebrate myb proteins share two conserved !1regions, one of which functions as a DNA-binding domain. !$#cross-references MUID:88082681; PMID:3121304 !$#accession S00578 !'##molecule_type mRNA !'##residues 1-657 ##label PET !'##cross-references GB:X05939; NID:g8276; PIDN:CAA29373.1; PID:g8277 REFERENCE A01345 !$#authors Katzen, A.L.; Kornberg, T.B.; Bishop, J.M. !$#journal Cell (1985) 41:449-456 !$#title Isolation of the proto-oncogene c-myb from Drosophila !1melanogaster. !$#cross-references MUID:85176969; PMID:3921261 !$#accession A01345 !'##molecule_type DNA !'##residues 1-369,'A',371-439,'KY' ##label KAT !'##cross-references GB:M11281; NID:g157933; PIDN:AAA70367.1; !1PID:g904102 GENETICS !$#gene myb !'##cross-references FlyBase:FBgn0002914 !$#map_position X (13E-F) CLASSIFICATION #superfamily myb transforming protein; myb DNA-binding !1repeat homology KEYWORDS DNA binding; duplication; nucleus; transcription regulation FEATURE !$80-130 #domain myb DNA-binding repeat homology #label MYB1\ !$131-182 #domain myb DNA-binding repeat homology #label MYB2\ !$183-233 #domain myb DNA-binding repeat homology #label MYB3 SUMMARY #length 657 #molecular-weight 74072 #checksum 2042 SEQUENCE /// ENTRY A40083 #type complete TITLE transcription factor BAS1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YKR099w ORGANISM #formal_name Saccharomyces cerevisiae DATE 22-Jan-1993 #sequence_revision 22-Jan-1993 #text_change 21-Jul-2000 ACCESSIONS A40083; S38178 REFERENCE A40083 !$#authors Tice-Baldwin, K.; Fink, G.R.; Arndt, K.T. !$#journal Science (1989) 246:931-935 !$#title BAS1 has a myb motif and activates HIS4 transcription only !1in combination with BAS2. !$#cross-references MUID:90049230; PMID:2683089 !$#accession A40083 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-811 ##label TIC !'##cross-references GB:M58057; NID:g1435185; PIDN:AAB04030.1; !1PID:g172020 REFERENCE S38175 !$#authors Gaillon, L.; Dujon, B. !$#submission submitted to the Protein Sequence Database, March 1994 !$#accession S38178 !'##molecule_type DNA !'##residues 1-811 ##label GAI !'##cross-references EMBL:Z28324; NID:g486594; PIDN:CAA82179.1; !1PID:g486595; GSPDB:GN00011; MIPS:YKR099w !'##experimental_source strain S288C REFERENCE A43094 !$#authors Hovring, I.; Bostad, A.; Ording, E.; Myrset, A.H.; !1Gabrielsen, O.S. !$#journal J. Biol. Chem. (1994) 269:17663-17669 !$#title DNA-binding domain and recognition sequence of the yeast !1BAS1 protein, a divergent member of the Myb family of !1transcription factors. !$#cross-references MUID:94292530; PMID:8021277 !$#contents annotation; DNA binding !$#note all three myb repeats plus up to 55 residues !1carboxyl-terminal to the third myb repeat are required for !1specific binding to DNA GENETICS !$#gene SGD:BAS1; MIPS:YKR099w !'##cross-references SGD:S0001807; MIPS:YKR099w !$#map_position 11R FUNCTION !$#description transcription activator; activates transcription of HIS4 !1(with other transcription factors) !$#note BAS2/PHO2 is also required for basal transcription, GCN4 is !1required for transcription in response to amino acid !1starvation, and RAP1 is also required CLASSIFICATION #superfamily transcription factor BAS1; myb DNA-binding !1repeat homology KEYWORDS DNA binding; duplication; nucleus; transcription regulation FEATURE !$34-110 #domain myb DNA-binding repeat homology #status !8atypical #label MYB1\ !$111-161 #domain myb DNA-binding repeat homology #label MYB2\ !$164-214 #domain myb DNA-binding repeat homology #label MYB3 SUMMARY #length 811 #molecular-weight 89603 #checksum 2429 SEQUENCE /// ENTRY S45907 #type complete TITLE myb-related protein REB1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YBR049c; protein YBR0502 ORGANISM #formal_name Saccharomyces cerevisiae DATE 26-Aug-1994 #sequence_revision 09-Sep-1994 #text_change 05-Nov-1999 ACCESSIONS S45907; S49504; A35924; S55847 REFERENCE S45906 !$#authors Aljinovic, G.; Pohl, F.M.; Pohl, T.M. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S45907 !'##molecule_type DNA !'##residues 1-810 ##label ALJ !'##cross-references EMBL:Z35918; NID:g536279; PIDN:CAA84992.1; !1PID:g536280; GSPDB:GN00002; MIPS:YBR049c !'##experimental_source strain S288C REFERENCE S49503 !$#authors Aljinovic, G. !$#submission submitted to the EMBL Data Library, October 1994 !$#description Sequence and analysis of 24 kb on chromosome II of !1Saccharomyces cerevisiae. !$#accession S49504 !'##molecule_type DNA !'##residues 1-810 ##label AL2 !'##cross-references EMBL:Z46260; NID:g559942; PIDN:CAA86391.1; !1PID:g559944 !'##experimental_source strain S288C REFERENCE A35924 !$#authors Ju, Q.; Morrow, B.E.; Warner, J.R. !$#journal Mol. Cell. Biol. (1990) 10:5226-5234 !$#title REB1, a yeast DNA-binding protein with many targets, is !1essential for cell growth and bears some resemblance to the !1oncogene myb. !$#cross-references MUID:90377212; PMID:2204808 !$#accession A35924 !'##molecule_type DNA !'##residues 1-55,'N',57-591,'RAVVFKNNNNFFNKSSKMMTMLLRSC',619-626,'E', !1628-635,'E',637-810 ##label JUA !'##cross-references EMBL:M58728; NID:g172371; PIDN:AAA34963.1; !1PID:g172372 REFERENCE S55846 !$#authors Aljinovic, G.; Pohl, T.M. !$#journal Yeast (1995) 11:475-479 !$#title Sequence and analysis of 24 kb on chromosome II of !1Saccharomyces cerevisiae. !$#cross-references MUID:95321020; PMID:7597852 !$#accession S55847 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-810 ##label ALW !'##cross-references EMBL:Z46260; NID:g559942; PIDN:CAA86391.1; !1PID:g559944 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1994 GENETICS !$#gene SGD:REB1; MIPS:YBR049c !'##cross-references SGD:S0000253; MIPS:YBR049c !$#map_position 2R CLASSIFICATION #superfamily myb-related protein REB1; myb DNA-binding !1repeat homology KEYWORDS DNA binding; nucleus; transcription regulation FEATURE !$470-519 #domain myb DNA-binding repeat homology #label MYB SUMMARY #length 810 #molecular-weight 91874 #checksum 2973 SEQUENCE /// ENTRY A48077 #type complete TITLE myb-related protein REB1 - yeast (Kluyveromyces marxianus var. lactis) ORGANISM #formal_name Kluyveromyces marxianus var. lactis, Candida sphaerica DATE 21-Jan-1994 #sequence_revision 18-Nov-1994 #text_change 18-Jun-1999 ACCESSIONS A48077 REFERENCE A48077 !$#authors Morrow, B.E.; Ju, Q.; Warner, J.R. !$#journal Mol. Cell. Biol. (1993) 13:1173-1182 !$#title A bipartite DNA-binding domain in yeast Reb1p. !$#cross-references MUID:93140755; PMID:8423784 !$#accession A48077 !'##status preliminary !'##molecule_type DNA !'##residues 1-595 ##label MOR !'##cross-references GB:L03789; NID:g173313; PIDN:AAA61343.1; !1PID:g173314 !'##note sequence extracted from NCBI backbone (NCBIN:123574, !1NCBIP:123576) CLASSIFICATION #superfamily myb-related protein REB1; myb DNA-binding !1repeat homology KEYWORDS DNA binding; nucleus; transcription regulation FEATURE !$333-382 #domain myb DNA-binding repeat homology #label MYB SUMMARY #length 595 #molecular-weight 68050 #checksum 6133 SEQUENCE /// ENTRY S50933 #type complete TITLE myb-related protein YDR026c - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein D3283; hypothetical protein PZE570; hypothetical protein YD9813.04c; REB1-related protein ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Feb-1995 #sequence_revision 12-May-1995 #text_change 19-Apr-2002 ACCESSIONS S50933; S63434; S67839; S72125 REFERENCE S50930 !$#authors Bowman, S. !$#submission submitted to the EMBL Data Library, January 1994 !$#accession S50933 !'##molecule_type DNA !'##residues 1-570 ##label BOW !'##cross-references EMBL:Z47814; NID:g642294; PIDN:CAA87805.1; !1PID:g642298; GSPDB:GN00004; MIPS:YDR026c REFERENCE S63416 !$#authors Eide, L.G.; Sander, C.; Prydz, H. !$#submission submitted to the EMBL Data Library, February 1996 !$#description Sequencing and analysis of a 35.4 kb region on the left arm !1of chromosome IV for Saccharomyces cerevisiae reveal 23 open !1reading frames. !$#accession S63434 !'##molecule_type DNA !'##residues 1-570 ##label EID !'##cross-references EMBL:X95966; NID:g1216215; PIDN:CAA65219.1; !1PID:g1216234 REFERENCE S67822 !$#authors Prydz, H.; Eide, L.G. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67839 !'##molecule_type DNA !'##residues 1-570 ##label PRY !'##cross-references EMBL:Z74322; NID:g1431459; PIDN:CAA98848.1; !1PID:g1431460; GSPDB:GN00004; MIPS:YDR026c !'##experimental_source strain S288C REFERENCE S72107 !$#authors Eide, L.G.; Sander, C.; Prydz, H. !$#journal Yeast (1996) 12:1085-1090 !$#title Sequencing and analysis of a 35.4 kb region on the left arm !1of chromosome IV from Saccharomyces cerevisiae reveal 23 !1open reading frames. !$#cross-references MUID:97051598; PMID:8896275 !$#accession S72125 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-570 ##label EIW !'##cross-references EMBL:X95966; NID:g1216215; PIDN:CAA65219.1; !1PID:g1216234 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1February 1996 GENETICS !$#gene MIPS:YDR026c !'##cross-references SGD:S0002433 !$#map_position 4R CLASSIFICATION #superfamily myb-related protein REB1; myb DNA-binding !1repeat homology KEYWORDS DNA binding; nucleus; transcription regulation FEATURE !$340-389 #domain myb DNA-binding repeat homology #label MYB SUMMARY #length 570 #molecular-weight 66352 #checksum 2753 SEQUENCE /// ENTRY S50591 #type complete TITLE myb-related protein YER088c - yeast (Saccharomyces cerevisiae) ORGANISM #formal_name Saccharomyces cerevisiae DATE 28-May-1993 #sequence_revision 24-Feb-1995 #text_change 19-Apr-2002 ACCESSIONS S50591 REFERENCE S50436 !$#authors Dietrich, F.S. !$#submission submitted to the EMBL Data Library, December 1994 !$#description The sequence of S. cerevisiae cosmids 9747, 8198, 9781, and !1lambda clones 3612 and 6052. !$#accession S50591 !'##molecule_type DNA !'##residues 1-670 ##label DIE !'##cross-references EMBL:U18839; NID:g603313; PIDN:AAB64643.1; !1PID:g603326; GSPDB:GN00005; MIPS:YER088c GENETICS !$#gene SGD:DOT6; MIPS:YER088c !'##cross-references SGD:S0000890 !$#map_position 5R CLASSIFICATION #superfamily myb-related hypothetical protein YER088c; myb !1DNA-binding repeat homology FEATURE !$67-117 #domain myb DNA-binding repeat homology #label MYB SUMMARY #length 670 #molecular-weight 73048 #checksum 5269 SEQUENCE /// ENTRY S39834 #type complete TITLE myb-related protein YBL054w - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein YBL0509; hypothetical protein YBL0513 ORGANISM #formal_name Saccharomyces cerevisiae DATE 16-Dec-1993 #sequence_revision 09-Sep-1994 #text_change 19-Apr-2002 ACCESSIONS S39834; S45789; S37335 REFERENCE S39824 !$#authors Scherens, B.; el Bakkoury, M.; Vierendeels, F.; Dubois, E.; !1Messenguy, F. !$#journal Yeast (1993) 9:1355-1371 !$#title Sequencing and functional analysis of a 32 560 bp segment on !1the left arm of yeast chromosome II. Identification of 26 !1open reading frames, including the KIP1 and SEC17 genes. !$#cross-references MUID:94205266; PMID:8154187 !$#accession S39834 !'##molecule_type DNA !'##residues 1-525 ##label SCH !'##cross-references EMBL:Z23261; NID:g313733; PIDN:CAA80793.1; !1PID:g313744 !'##experimental_source strain S288C REFERENCE S45782 !$#authors Dubois, E.; El Bakkoury, M.; Glansdorff, N.; Messenguy, F.; !1Pierard, A.; Scherens, B.; Vierendeels, F. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S45789 !'##molecule_type DNA !'##residues 1-525 ##label DUB !'##cross-references EMBL:Z35815; NID:g536081; PIDN:CAA84874.1; !1PID:g536082; GSPDB:GN00002; MIPS:YBL054w !'##experimental_source strain S288C GENETICS !$#gene MIPS:YBL054w !'##cross-references SGD:S0000150 !$#map_position 2L CLASSIFICATION #superfamily myb-related hypothetical protein YER088c; myb !1DNA-binding repeat homology FEATURE !$70-120 #domain myb DNA-binding repeat homology #label MYB SUMMARY #length 525 #molecular-weight 59225 #checksum 9282 SEQUENCE /// ENTRY S41712 #type complete TITLE myb-related protein cdc5 - fission yeast (Schizosaccharomyces pombe) ORGANISM #formal_name Schizosaccharomyces pombe DATE 13-Jan-1995 #sequence_revision 27-Jan-1995 #text_change 16-Jul-1999 ACCESSIONS S41712 REFERENCE S41712 !$#authors Ohi, R.; McCollum, D.; Hirani, B.; den Haese, G.J.; Zhang, !1X.; Burke, J.D.; Turner, K.; Gould, K.L. !$#journal EMBO J. (1994) 13:471-483 !$#title The Schizosaccharomyces pombe cdc5(+) gene encodes an !1essential protein with homology to c-Myb. !$#cross-references MUID:94147994; PMID:8313892 !$#accession S41712 !'##molecule_type DNA !'##residues 1-757 ##label OHI !'##cross-references EMBL:L19525; NID:g439121; PIDN:AAA17515.1; !1PID:g469226 GENETICS !$#gene cdc5 FUNCTION !$#description probably a transcription factor required for cell cycle !1progression and growth during G2 CLASSIFICATION #superfamily myb-related protein cdc5; myb DNA-binding !1repeat homology KEYWORDS DNA binding; duplication; nucleus; transcription regulation FEATURE !$1-52 #domain myb DNA-binding repeat homology #label MYB1\ !$53-102 #domain myb DNA-binding repeat homology #label MYB2 SUMMARY #length 757 #molecular-weight 86843 #checksum 4478 SEQUENCE /// ENTRY S55095 #type complete TITLE myb-related protein YMR213w - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein YM8261.07 ORGANISM #formal_name Saccharomyces cerevisiae DATE 08-Jul-1995 #sequence_revision 01-Sep-1995 #text_change 19-Apr-2002 ACCESSIONS S55095 REFERENCE S55089 !$#authors Dedman, K.; Brown, D.; Bowman, S. !$#submission submitted to the EMBL Data Library, June 1995 !$#accession S55095 !'##molecule_type DNA !'##residues 1-590 ##label DED !'##cross-references EMBL:Z49809; NID:g854459; PIDN:CAA89928.1; !1PID:g854465; GSPDB:GN00013; MIPS:YMR213w !'##experimental_source strain AB972 GENETICS !$#gene SGD:CEF1; MIPS:YMR213w !'##cross-references SGD:S0004826 !$#map_position 13R CLASSIFICATION #superfamily myb-related protein cdc5; myb DNA-binding !1repeat homology FEATURE !$5-56 #domain myb DNA-binding repeat homology #label MYB1\ !$57-106 #domain myb DNA-binding repeat homology #label MYB2 SUMMARY #length 590 #molecular-weight 67730 #checksum 2493 SEQUENCE /// ENTRY S71287 #type complete TITLE myb-related 24.7K transcription factor - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 28-Oct-1996 #sequence_revision 27-Feb-1997 #text_change 16-Jun-2000 ACCESSIONS S71287; JC5729 REFERENCE S71287 !$#authors Kirik, V.; Baumlein, H. !$#submission submitted to the EMBL Data Library, December 1995 !$#description Isolation and chromosomal localization of leaf-specific cDNA !1encoding for a new member of Arabidopsis myb family which !1has one MYB domain. !$#accession S71287 !'##molecule_type mRNA !'##residues 1-213 ##label KIR !'##cross-references EMBL:Z68157; NID:g1197189; PIDN:CAA92280.1; !1PID:g1197190 REFERENCE JC5729 !$#authors Kirik, V.; Baeumlein, H. !$#journal Gene (1996) 183:109-113 !$#title A novel leaf-specific myb-related protein with a single !1binding repeat. !$#cross-references MUID:97149286; PMID:8996094 !$#accession JC5729 !'##molecule_type mRNA !'##residues 1-213 ##label KI2 !'##cross-references EMBL:Z68157; NID:g1197189; PIDN:CAA92280.1; !1PID:g1197190 COMMENT This protein is involved in the control of anthocyanin !1biosysthesis and the regulation cell differentiation. GENETICS !$#gene AtmybL2 !$#map_position I CLASSIFICATION #superfamily Arabidopsis myb-related 24.7K protein; myb !1DNA-binding repeat homology KEYWORDS DNA binding; nucleus; transcription regulation FEATURE !$30-80 #domain myb DNA-binding repeat homology #label MYB2\ !$54-80 #region helix-turn-helix SUMMARY #length 213 #molecular-weight 24693 #checksum 916 SEQUENCE /// ENTRY S71285 #type complete TITLE myb-related protein, 33.2K - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 28-Oct-1996 #sequence_revision 27-Feb-1997 #text_change 16-Jun-2000 ACCESSIONS S71285 REFERENCE S71285 !$#authors Kirik, V.; Baumlein, H. !$#submission submitted to the EMBL Data Library, September 1995 !$#description Characterization of two cDNAs encoding MYB-related proteins !1in Arabidopsis thaliana. !$#accession S71285 !'##molecule_type mRNA !'##residues 1-304 ##label KIR !'##cross-references EMBL:Z54137; NID:g1263096; PIDN:CAA90810.1; !1PID:g1263097 CLASSIFICATION #superfamily Arabidopsis myb-related 33.2K protein; myb !1DNA-binding repeat homology KEYWORDS DNA binding; duplication FEATURE !$1-52 #domain myb DNA-binding repeat homology #label MYB1\ !$53-103 #domain myb DNA-binding repeat homology #label MYB2 SUMMARY #length 304 #molecular-weight 33292 #checksum 3562 SEQUENCE /// ENTRY S71284 #type complete TITLE myb-related protein, 33.3K - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 28-Oct-1996 #sequence_revision 27-Feb-1997 #text_change 16-Jun-2000 ACCESSIONS S71284 REFERENCE S71284 !$#authors Kirik, V.; Baumlein, H. !$#submission submitted to the EMBL Data Library, September 1995 !$#description Characterization of two cDNAs encoding MYB-related proteins !1in Arabidopsis thaliana. !$#accession S71284 !'##molecule_type mRNA !'##residues 1-305 ##label KIR !'##cross-references EMBL:Z54136; NID:g1263094; PIDN:CAA90809.1; !1PID:g1263095 CLASSIFICATION #superfamily Arabidopsis myb-related 33.2K protein; myb !1DNA-binding repeat homology KEYWORDS DNA binding; duplication FEATURE !$1-52 #domain myb DNA-binding repeat homology #label MYB1\ !$53-103 #domain myb DNA-binding repeat homology #label MYB2 SUMMARY #length 305 #molecular-weight 33328 #checksum 5943 SEQUENCE /// ENTRY A39697 #type complete TITLE maize myb-related protein P, long splice form - maize ORGANISM #formal_name Zea mays #common_name maize DATE 08-Nov-1991 #sequence_revision 08-Nov-1991 #text_change 18-Jun-1999 ACCESSIONS A39697; S26150 REFERENCE A39697 !$#authors Grotewold, E.; Athma, P.; Peterson, T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:4587-4591 !$#title Alternatively spliced products of the maize P gene encode !1proteins with homology to the DNA-binding domain of myb-like !1transcription factors. !$#cross-references MUID:91271238; PMID:2052542 !$#accession A39697 !'##status preliminary !'##molecule_type mRNA !'##residues 1-399 ##label GRO !'##cross-references GB:M73028; GB:M62878; NID:g168589; PIDN:AAA33500.1; !1PID:g168590 REFERENCE S26150 !$#authors Athma, P.; Grotewold, E.; Peterson, T. !$#journal Genetics (1992) 131:199-209 !$#title Insertional mutagenesis of the maize P gene by intragenic !1transposition of Ac. !$#cross-references MUID:92275319; PMID:1317315 !$#accession S26150 !'##status preliminary; translation not shown !'##molecule_type DNA !'##residues 1-399 ##label ATH !'##cross-references EMBL:Z11879; NID:g22176; PIDN:CAA77939.1; !1PID:g22177 GENETICS !$#gene P !$#introns 45/1; 88/2 CLASSIFICATION #superfamily maize myb-related protein P; myb DNA-binding !1repeat homology KEYWORDS alternative splicing; DNA binding; duplication; nucleus; !1transcription regulation FEATURE !$9-61 #domain myb DNA-binding repeat homology #label MYB1\ !$62-112 #domain myb DNA-binding repeat homology #label MYB2 SUMMARY #length 399 #molecular-weight 43756 #checksum 6001 SEQUENCE /// ENTRY B39697 #type complete TITLE myb-related protein P, short splice form - maize ORGANISM #formal_name Zea mays #common_name maize DATE 08-Nov-1991 #sequence_revision 08-Nov-1991 #text_change 18-Jun-1999 ACCESSIONS B39697 REFERENCE A39697 !$#authors Grotewold, E.; Athma, P.; Peterson, T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:4587-4591 !$#title Alternatively spliced products of the maize P gene encode !1proteins with homology to the DNA-binding domain of myb-like !1transcription factors. !$#cross-references MUID:91271238; PMID:2052542 !$#accession B39697 !'##status preliminary !'##molecule_type mRNA !'##residues 1-151 ##label GRO !'##cross-references GB:M73029; GB:M62879; NID:g168591; PIDN:AAA33501.1; !1PID:g168592 CLASSIFICATION #superfamily maize myb-related protein P, short splice form; !1myb DNA-binding repeat homology KEYWORDS alternative splicing; DNA binding; nucleus; transcription !1regulation FEATURE !$9-61 #domain myb DNA-binding repeat homology #label MYB1\ !$62-88 #domain myb DNA-binding repeat homology #status !8atypical #label MYB2 SUMMARY #length 151 #molecular-weight 17332 #checksum 6389 SEQUENCE /// ENTRY S58293 #type complete TITLE myb-related protein M4 - Arabidopsis thaliana ALTERNATE_NAMES protein F18E5.60; protein T6K22.170 CONTAINS myb-related protein cM4 ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 14-Jan-1996 #sequence_revision 23-Jul-1999 #text_change 20-Aug-1999 ACCESSIONS T05152; T05186; S58293; S58280 REFERENCE Z15400 !$#authors Bevan, M.; Peters, S.A.; van Staveren, M.; Dirkse, W.; !1Stiekema, W.; Bancroft, I.; Mewes, H.W.; Mayer, K.F.X.; !1Schueller, C. !$#submission submitted to the Protein Sequence Database, August 1998 !$#accession T05152 !'##molecule_type DNA !'##residues 1-352 ##label BEV !'##cross-references EMBL:ALO22603 !'##experimental_source cultivar Columbia; BAC clone F18E5 !$#accession T05186 !'##molecule_type DNA !'##residues 1-352 ##label BEW !'##cross-references EMBL:AL031187 !'##experimental_source cultivar Columbia; BAC clone T6K22 REFERENCE S58280 !$#authors Quaedvlieg, N.E.M.; Dockx, J.; Keultjes, G.G.M.; Smeekens, !1J.C.M. !$#submission submitted to the EMBL Data Library, July 1995 !$#accession S58293 !'##molecule_type DNA !'##residues 1-78,'A',80-166,'Q',168-183,'I',185-192,'HNQNQNQNQN', !1193-197,'EKQ',201,'VYHHHDVN',210-218,'D',220-224,'A', !1226-241,'H',243-245,'D',247-286,'H',288-352 ##label QUA !'##cross-references EMBL:X90381; NID:g928941; PIDN:CAA62029.1; !1PID:g928942 !'##genetics M4P !$#accession S58280 !'##molecule_type DNA !'##residues 1-45,48-78,'A',80-166,'Q',168-183,'I',185-192,'HNQNQNQNQN', !1193-197,'EKQ',201,'VYHHHDVN',210-218,'D',220-224,'A', !1226-241,'H',243-245,'D',247-286,'H',288-352 ##label QUW !'##cross-references EMBL:X90382; NID:g928927; PIDN:CAA62030.1; !1PID:g928928 !'##note variant cM4 !'##note though labeled as the sequence of a gene, cM4, the nucleotide !1sequence has a poly-A tail and no introns GENETICS !$#gene M4 !$#map_position 4 !$#introns 47/1; 90/2 !$#note F18E5.60; T6K22.170 CLASSIFICATION #superfamily Arabidopsis myb-related protein M4; myb !1DNA-binding repeat homology KEYWORDS DNA binding; duplication FEATURE !$1-352 #product gene M4 protein #status predicted #label !8M4P\ !$1-45,48-352 #product myb-related protein cM4 #status predicted !8#label CM4\ !$9-63 #domain myb DNA-binding repeat homology #label MYB1\ !$64-114 #domain myb DNA-binding repeat homology #label MYB2 SUMMARY #length 352 #molecular-weight 40371 #checksum 3013 SEQUENCE /// ENTRY S58283 #type complete TITLE myb-related protein Y13 - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 13-Jan-1996 #sequence_revision 12-Apr-1996 #text_change 18-Jun-1999 ACCESSIONS S58283; S58281 REFERENCE S58280 !$#authors Quaedvlieg, N.E.M.; Dockx, J.; Keultjes, G.G.M.; Smeekens, !1J.C.M. !$#submission submitted to the EMBL Data Library, July 1995 !$#accession S58283 !'##molecule_type DNA !'##residues 1-332 ##label QUA !'##cross-references EMBL:X90383; NID:g928964; PIDN:CAA62031.1; !1PID:g928965 !$#accession S58281 !'##molecule_type mRNA !'##residues 1-332 ##label QUW !'##cross-references EMBL:X90387; NID:g928929; PIDN:CAA62034.1; !1PID:g928930 GENETICS !$#introns 44/3; 88/3 CLASSIFICATION #superfamily Arabidopsis myb-related protein Y13; myb !1DNA-binding repeat homology KEYWORDS DNA binding; duplication FEATURE !$9-61 #domain myb DNA-binding repeat homology #label MYB1\ !$62-112 #domain myb DNA-binding repeat homology #label MYB2 SUMMARY #length 332 #molecular-weight 37171 #checksum 1263 SEQUENCE /// ENTRY JQ0956 #type complete TITLE myb-related protein 306 - garden snapdragon ORGANISM #formal_name Antirrhinum majus #common_name garden snapdragon DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 24-Jul-1997 ACCESSIONS JQ0956 REFERENCE JQ0956 !$#authors Jackson, D.; Culianez-Macia, F.; Prescott, A.G.; Roberts, !1K.; Martin, C. !$#journal Plant Cell (1991) 3:115-125 !$#title Expression patterns of myb genes from Antirrhinum flowers. !$#cross-references MUID:93005689; PMID:1840903 !$#accession JQ0956 !'##molecule_type mRNA !'##residues 1-316 ##label JAC !'##experimental_source strain JI:522 CLASSIFICATION #superfamily Arabidopsis myb-related protein Y13; myb !1DNA-binding repeat homology KEYWORDS DNA binding; duplication FEATURE !$9-61 #domain myb DNA-binding repeat homology #label MYB1\ !$62-112 #domain myb DNA-binding repeat homology #label MYB2 SUMMARY #length 316 #molecular-weight 35142 #checksum 9769 SEQUENCE /// ENTRY S71283 #type complete TITLE myb-related protein, 28K, leaf-specific - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 28-Oct-1996 #sequence_revision 27-Feb-1997 #text_change 16-Jun-2000 ACCESSIONS S71283 REFERENCE S71283 !$#authors Kirik, V.; Koelle, K.; Misera, S.; Baeumlein, H. !$#submission submitted to the EMBL Data Library, August 1995 !$#description The expression of a new leaf-specific myb gene is shifted to !1late embryogenesis in the fus3 mutant of Arabidopsis. !$#accession S71283 !'##molecule_type DNA !'##residues 1-246 ##label KIR !'##cross-references EMBL:Z50869; NID:g1263092; PIDN:CAA90748.1; !1PID:g1263093 !'##experimental_source strain Columbia GENETICS !$#introns 45/1; 88/2 CLASSIFICATION #superfamily Arabidopsis 28K leaf-specific myb-related !1protein; myb DNA-binding repeat homology KEYWORDS DNA binding; duplication; nucleus; transcription regulation FEATURE !$9-61 #domain myb DNA-binding repeat homology #label MYB1\ !$62-112 #domain myb DNA-binding repeat homology #label MYB2 SUMMARY #length 246 #molecular-weight 27921 #checksum 4794 SEQUENCE /// ENTRY S26604 #type complete TITLE myb-related protein Ph2 - garden petunia ORGANISM #formal_name Petunia x hybrida #common_name garden petunia DATE 25-Feb-1994 #sequence_revision 03-Nov-1995 #text_change 18-Jun-1999 ACCESSIONS S26604 REFERENCE S26604 !$#authors Avila, J.; Nieto, C.; Canas, L.; Benito, M.; Paz-Ares, J. !$#submission submitted to the EMBL Data Library, July 1992 !$#description Petunia hybrida genes related to the maize regulatory C1 !1gene and to animal myb proto-oncogenes. !$#accession S26604 !'##status preliminary !'##molecule_type DNA !'##residues 1-280 ##label AVI !'##cross-references EMBL:Z13997; NID:g20560; PIDN:CAA78387.1; !1PID:g20561 !'##experimental_source strain v26, developing flowers CLASSIFICATION #superfamily Arabidopsis 28K leaf-specific myb-related !1protein; myb DNA-binding repeat homology KEYWORDS DNA binding; duplication; nucleus; transcription regulation FEATURE !$9-61 #domain myb DNA-binding repeat homology #label MYB1\ !$62-112 #domain myb DNA-binding repeat homology #label MYB2 SUMMARY #length 280 #molecular-weight 32178 #checksum 6555 SEQUENCE /// ENTRY S31818 #type complete TITLE myb-related protein 3 - barley ALTERNATE_NAMES myb3 protein; MybHv33 protein ORGANISM #formal_name Hordeum vulgare #common_name barley DATE 22-Nov-1993 #sequence_revision 26-May-1995 #text_change 18-Jun-1999 ACCESSIONS S31818; S35419; S61508; S04897 REFERENCE S31813 !$#authors Wissenbach, M.; Ueberlacker, B.; Vogt, F.; Backer, D.; !1Salamini, F.; Rohde, W. !$#submission submitted to the EMBL Data Library, January 1993 !$#description Myb gene from hordeum vulgare: tissue-specific expression of !1chimeric Myb promoter/Gus genes in transgenic tobacco. !$#accession S31818 !'##status preliminary !'##molecule_type DNA !'##residues 1-302 ##label WIS !'##cross-references EMBL:X70881; NID:g456213; PIDN:CAA50226.1; !1PID:g456214 REFERENCE S35419 !$#authors Rohde, W. !$#submission submitted to the EMBL Data Library, January 1993 !$#accession S35419 !'##molecule_type mRNA !'##residues 1-258,'P',260-302 ##label ROH !'##cross-references EMBL:X70878; NID:g19058; PIDN:CAA50223.1; !1PID:g19059 REFERENCE S61506 !$#authors Wissenbach, M.; Ueberlacker, B.; Vogt, F.; Becker, D.; !1Salamini, F.; Rohde, W. !$#journal Plant J. (1993) 4:411-422 !$#title Myb genes from Hordeum vulgare: tissue-specific expression !1of chimeric Myb promoter/Gus genes in transgenic tobacco. !$#cross-references MUID:94035190; PMID:8220488 !$#accession S61508 !'##status preliminary; nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-119 ##label WI2 !'##cross-references EMBL:X70881 REFERENCE S04896 !$#authors Marocco, A.; Wissenbach, M.; Becker, D.; Paz-Ares, J.; !1Saedler, H.; Salamini, F.; Rohde, W. !$#journal Mol. Gen. Genet. (1989) 216:183-187 !$#title Multiple genes are transcribed in Hordeum vulgare and Zea !1mays that carry the DNA binding domain of the myb !1oncoproteins. !$#cross-references MUID:89313655; PMID:2664447 !$#accession S04897 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 35-258, !1'RSRPSRRWRGSSSTHRRSRSFAALPRTEPPRKFRFQPGIGTILLKFPPLF', !1'SLHFSPS' ##label MAR GENETICS !$#gene myb3 !$#introns 90/2 CLASSIFICATION #superfamily barley myb-related protein 3; myb DNA-binding !1repeat homology KEYWORDS DNA binding; duplication; nucleus; transcription regulation FEATURE !$11-63 #domain myb DNA-binding repeat homology #label MYB1\ !$64-114 #domain myb DNA-binding repeat homology #label MYB2 SUMMARY #length 302 #molecular-weight 33003 #checksum 1506 SEQUENCE /// ENTRY JQ2390 #type complete TITLE MYB transcription factor (Atmyb2) [imported] - Arabidopsis thaliana ALTERNATE_NAMES myb-related protein 2; ATMYB2 protein ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 28-Aug-1985 #sequence_revision 07-Oct-1994 #text_change 23-Mar-2001 ACCESSIONS JQ2390; B84912 REFERENCE JQ2390 !$#authors Urao, T.; Yamaguchi-Shinozaki, K.; Urao, S.; Shinozaki, K. !$#journal Plant Cell (1993) 5:1529-1539 !$#title An arabidopsis myb homolog is induced by dehydration stress !1and its gene product binds to the conserved MYB recognition !1sequence. !$#cross-references MUID:94146551; PMID:8312738 !$#accession JQ2390 !'##molecule_type mRNA !'##residues 1-273 ##label URA !'##cross-references DDBJ:D14712; NID:g455462; PIDN:BAA03534.1; !1PID:g506189 REFERENCE A84420 !$#authors Lin, X.; Kaul, S.; Rounsley, S.D.; Shea, T.P.; Benito, M.I.; !1Town, C.D.; Fujii, C.Y.; Mason, T.M.; Bowman, C.L.; !1Barnstead, M.E.; Feldblyum, T.V.; Buell, C.R.; Ketchum, !1K.A.; Lee, J.J.; Ronning, C.M.; Koo, H.; Moffat, K.S.; !1Cronin, L.A.; Shen, M.; VanAken, S.E.; Umayam, L.; Tallon, !1L.J.; Gill, J.E.; Adams, M.D.; Carrera, A.J.; Creasy, T.H.; !1Goodman, H.M.; Somerville, C.R.; Copenhaver, G.P.; Preuss, !1D.; Nierman, W.C.; White, O.; Eisen, J.A.; Salzberg, S.L.; !1Fraser, C.M.; Venter, J.C. !$#journal Nature (1999) 402:761-768 !$#title Sequence and analysis of chromosome 2 of the plant !1Arabidopsis thaliana. !$#cross-references MUID:20083487; PMID:10617197 !$#accession B84912 !'##status preliminary !'##molecule_type DNA !'##residues 1-273 ##label STO !'##cross-references GB:AE002093; NID:g2275197; PIDN:AAB63819.1; !1GSPDB:GN00139 COMMENT The expression of the gene encoding for this protein is !1induced by dehydration stress, high-salt conditions, and !1treatment with the plant hormone abscisic acid at the !1transcriptional level. GENETICS !$#gene Atmyb2; At2g47190 !$#map_position 2 !$#introns 53/1; 96/2 CLASSIFICATION #superfamily Arabidopsis myb-related protein 2; myb !1DNA-binding repeat homology KEYWORDS DNA binding; duplication FEATURE !$17-69 #domain myb DNA-binding repeat homology #label MYB1\ !$70-120 #domain myb DNA-binding repeat homology #label MYB2 SUMMARY #length 273 #molecular-weight 31448 #checksum 9758 SEQUENCE /// ENTRY JQ0958 #type complete TITLE myb-related protein 305 - garden snapdragon ORGANISM #formal_name Antirrhinum majus #common_name garden snapdragon DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 24-Jul-1997 ACCESSIONS JQ0958 REFERENCE JQ0956 !$#authors Jackson, D.; Culianez-Macia, F.; Prescott, A.G.; Roberts, !1K.; Martin, C. !$#journal Plant Cell (1991) 3:115-125 !$#title Expression patterns of myb genes from Antirrhinum flowers. !$#cross-references MUID:93005689; PMID:1840903 !$#accession JQ0958 !'##molecule_type mRNA !'##residues 1-205 ##label JAC !'##experimental_source strain JI:522 COMMENT This protein is specifically expressed in flowers. CLASSIFICATION #superfamily Arabidopsis myb-related protein 2; myb !1DNA-binding repeat homology KEYWORDS DNA binding; duplication FEATURE !$10-62 #domain myb DNA-binding repeat homology #label MYB1\ !$63-113 #domain myb DNA-binding repeat homology #label MYB2 SUMMARY #length 205 #molecular-weight 23507 #checksum 8074 SEQUENCE /// ENTRY JQ0959 #type complete TITLE myb-related protein 340 - garden snapdragon ORGANISM #formal_name Antirrhinum majus #common_name garden snapdragon DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 02-Sep-1997 ACCESSIONS JQ0959 REFERENCE JQ0956 !$#authors Jackson, D.; Culianez-Macia, F.; Prescott, A.G.; Roberts, !1K.; Martin, C. !$#journal Plant Cell (1991) 3:115-125 !$#title Expression patterns of myb genes from Antirrhinum flowers. !$#cross-references MUID:93005689; PMID:1840903 !$#accession JQ0959 !'##molecule_type mRNA !'##residues 1-198 ##label JAC !'##experimental_source strain JI:522 COMMENT This protein is specifically expressed in flowers. CLASSIFICATION #superfamily Arabidopsis myb-related protein 2; myb !1DNA-binding repeat homology KEYWORDS DNA binding; duplication FEATURE !$10-62 #domain myb DNA-binding repeat homology #label MYB1\ !$63-113 #domain myb DNA-binding repeat homology #label MYB2 SUMMARY #length 198 #molecular-weight 22846 #checksum 816 SEQUENCE /// ENTRY S61506 #type complete TITLE myb-related protein 1 - barley ALTERNATE_NAMES myb1 protein ORGANISM #formal_name Hordeum vulgare #common_name barley DATE 20-Jul-1996 #sequence_revision 27-Feb-1997 #text_change 18-Jun-1999 ACCESSIONS S61506; S04896; S31817 REFERENCE S61506 !$#authors Wissenbach, M.; Ueberlacker, B.; Vogt, F.; Becker, D.; !1Salamini, F.; Rohde, W. !$#journal Plant J. (1993) 4:411-422 !$#title Myb genes from Hordeum vulgare: tissue-specific expression !1of chimeric Myb promoter/Gus genes in transgenic tobacco. !$#cross-references MUID:94035190; PMID:8220488 !$#accession S61506 !'##status preliminary !'##molecule_type DNA !'##residues 1-267 ##label WIS !'##cross-references EMBL:X70879; NID:g19052; PIDN:CAA50224.1; !1PID:g19053 !'##experimental_source var. Abessynian 2231 REFERENCE S04896 !$#authors Marocco, A.; Wissenbach, M.; Becker, D.; Paz-Ares, J.; !1Saedler, H.; Salamini, F.; Rohde, W. !$#journal Mol. Gen. Genet. (1989) 216:183-187 !$#title Multiple genes are transcribed in Hordeum vulgare and Zea !1mays that carry the DNA binding domain of the myb !1oncoproteins. !$#cross-references MUID:89313655; PMID:2664447 !$#accession S04896 !'##molecule_type mRNA !'##residues 1-267 ##label MAR !'##cross-references EMBL:X70877; NID:g19050; PIDN:CAA50222.1; !1PID:g19051 !'##experimental_source var. Abessynian 2231 GENETICS !$#introns 88/2 CLASSIFICATION #superfamily barley myb-related protein 1; myb DNA-binding !1repeat homology KEYWORDS DNA binding; duplication; nucleus; transcription regulation FEATURE !$9-61 #domain myb DNA-binding repeat homology #label MYB1\ !$62-112 #domain myb DNA-binding repeat homology #label MYB2 SUMMARY #length 267 #molecular-weight 29740 #checksum 5702 SEQUENCE /// ENTRY S04899 #type complete TITLE myb-related protein Zm38 - maize ORGANISM #formal_name Zea mays #common_name maize DATE 28-Feb-1990 #sequence_revision 28-Feb-1990 #text_change 24-Jul-1997 ACCESSIONS S04899 REFERENCE S04896 !$#authors Marocco, A.; Wissenbach, M.; Becker, D.; Paz-Ares, J.; !1Saedler, H.; Salamini, F.; Rohde, W. !$#journal Mol. Gen. Genet. (1989) 216:183-187 !$#title Multiple genes are transcribed in Hordeum vulgare and Zea !1mays that carry the DNA binding domain of the myb !1oncoproteins. !$#cross-references MUID:89313655; PMID:2664447 !$#accession S04899 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-255 ##label MAR CLASSIFICATION #superfamily barley myb-related protein 1; myb DNA-binding !1repeat homology KEYWORDS DNA binding; duplication; nucleus; transcription regulation FEATURE !$9-61 #domain myb DNA-binding repeat homology #label MYB1\ !$62-112 #domain myb DNA-binding repeat homology #label MYB2 SUMMARY #length 255 #molecular-weight 27568 #checksum 4202 SEQUENCE /// ENTRY JQ0960 #type complete TITLE myb-related protein 308 - garden snapdragon ORGANISM #formal_name Antirrhinum majus #common_name garden snapdragon DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 24-Jul-1997 ACCESSIONS JQ0960 REFERENCE JQ0956 !$#authors Jackson, D.; Culianez-Macia, F.; Prescott, A.G.; Roberts, !1K.; Martin, C. !$#journal Plant Cell (1991) 3:115-125 !$#title Expression patterns of myb genes from Antirrhinum flowers. !$#cross-references MUID:93005689; PMID:1840903 !$#accession JQ0960 !'##molecule_type mRNA !'##residues 1-232 ##label JAC !'##experimental_source strain JI:522 COMMENT The gene encoding for this protein is expressed in all plant !1organs. CLASSIFICATION #superfamily barley myb-related protein 1; myb DNA-binding !1repeat homology KEYWORDS DNA binding; duplication; nucleus; transcription regulation FEATURE !$9-61 #domain myb DNA-binding repeat homology #label MYB1\ !$62-112 #domain myb DNA-binding repeat homology #label MYB2 SUMMARY #length 232 #molecular-weight 26164 #checksum 4148 SEQUENCE /// ENTRY S69189 #type complete TITLE myb-related protein TMH27 - tomato ORGANISM #formal_name Lycopersicon esculentum #common_name tomato DATE 06-Dec-1996 #sequence_revision 13-Mar-1997 #text_change 16-Jun-2000 ACCESSIONS S69189 REFERENCE S69189 !$#authors Lin, Q.; Hamilton, W.D.O.; Merryweather, A. !$#journal Plant Mol. Biol. (1996) 30:1009-1020 !$#title Cloning and initial characterization of 14 myb-related cDNAs !1from tomato (Lycopersicon esculentum cv. Ailsa Craig). !$#cross-references MUID:96270378; PMID:8639738 !$#accession S69189 !'##status preliminary !'##molecule_type mRNA !'##residues 1-273 ##label LIN !'##cross-references EMBL:X95296; NID:g1167483; PIDN:CAA64614.1; !1PID:g1167484 GENETICS !$#gene TMH27 CLASSIFICATION #superfamily barley myb-related protein 1; myb DNA-binding !1repeat homology KEYWORDS DNA binding; duplication; nucleus; transcription regulation FEATURE !$9-61 #domain myb DNA-binding repeat homology #label MYB1\ !$62-112 #domain myb DNA-binding repeat homology #label MYB2 SUMMARY #length 273 #molecular-weight 31100 #checksum 1733 SEQUENCE /// ENTRY S58292 #type complete TITLE probable MYB family transcription factor At2g16720 [imported] - Arabidopsis thaliana ALTERNATE_NAMES myb-related protein Y49 ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 13-Jan-1996 #sequence_revision 19-Apr-1996 #text_change 02-Mar-2001 ACCESSIONS S58292; D84543 REFERENCE S58280 !$#authors Quaedvlieg, N.E.M.; Dockx, J.; Keultjes, G.G.M.; Smeekens, !1J.C.M. !$#submission submitted to the EMBL Data Library, July 1995 !$#accession S58292 !'##molecule_type DNA !'##residues 1-269 ##label QUA !'##cross-references EMBL:X90385; NID:g928968; PIDN:CAA62033.1; !1PID:g928969 REFERENCE A84420 !$#authors Lin, X.; Kaul, S.; Rounsley, S.D.; Shea, T.P.; Benito, M.I.; !1Town, C.D.; Fujii, C.Y.; Mason, T.M.; Bowman, C.L.; !1Barnstead, M.E.; Feldblyum, T.V.; Buell, C.R.; Ketchum, !1K.A.; Lee, J.J.; Ronning, C.M.; Koo, H.; Moffat, K.S.; !1Cronin, L.A.; Shen, M.; VanAken, S.E.; Umayam, L.; Tallon, !1L.J.; Gill, J.E.; Adams, M.D.; Carrera, A.J.; Creasy, T.H.; !1Goodman, H.M.; Somerville, C.R.; Copenhaver, G.P.; Preuss, !1D.; Nierman, W.C.; White, O.; Eisen, J.A.; Salzberg, S.L.; !1Fraser, C.M.; Venter, J.C. !$#journal Nature (1999) 402:761-768 !$#title Sequence and analysis of chromosome 2 of the plant !1Arabidopsis thaliana. !$#cross-references MUID:20083487; PMID:10617197 !$#accession D84543 !'##status preliminary !'##molecule_type DNA !'##residues 1-269 ##label STO !'##cross-references GB:AE002093; NID:g4581115; PIDN:AAD24605.1; !1GSPDB:GN00139 GENETICS !$#gene At2g16720 !$#map_position 2 !$#introns 88/2 CLASSIFICATION #superfamily barley myb-related protein 1; myb DNA-binding !1repeat homology KEYWORDS DNA binding; duplication; nucleus; transcription regulation FEATURE !$9-61 #domain myb DNA-binding repeat homology #label MYB1\ !$62-112 #domain myb DNA-binding repeat homology #label MYB2 SUMMARY #length 269 #molecular-weight 31009 #checksum 1868 SEQUENCE /// ENTRY S35729 #type complete TITLE myb-related protein 2 - barley ALTERNATE_NAMES myb2 protein; MybHv5 protein ORGANISM #formal_name Hordeum vulgare #common_name barley DATE 03-Mar-1994 #sequence_revision 26-May-1995 #text_change 18-Jun-1999 ACCESSIONS S35729; S31813; S61507 REFERENCE S35419 !$#authors Rohde, W. !$#submission submitted to the EMBL Data Library, January 1993 !$#accession S35729 !'##molecule_type mRNA !'##residues 1-251 ##label ROH !'##cross-references EMBL:X70876; NID:g19054; PIDN:CAA50221.1; !1PID:g19055 REFERENCE S31813 !$#authors Wissenbach, M.; Ueberlacker, B.; Vogt, F.; Backer, D.; !1Salamini, F.; Rohde, W. !$#submission submitted to the EMBL Data Library, January 1993 !$#description Myb gene from hordeum vulgare: tissue-specific expression of !1chimeric Myb promoter/Gus genes in transgenic tobacco. !$#accession S31813 !'##molecule_type DNA !'##residues 1-104 ##label WIS !'##cross-references EMBL:X70880; NID:g19056; PIDN:CAA50225.1; !1PID:g19057 REFERENCE S61506 !$#authors Wissenbach, M.; Ueberlacker, B.; Vogt, F.; Becker, D.; !1Salamini, F.; Rohde, W. !$#journal Plant J. (1993) 4:411-422 !$#title Myb genes from Hordeum vulgare: tissue-specific expression !1of chimeric Myb promoter/Gus genes in transgenic tobacco. !$#cross-references MUID:94035190; PMID:8220488 !$#accession S61507 !'##status preliminary; nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-117 ##label WI2 !'##cross-references EMBL:X70880 GENETICS !$#gene myb2 !$#introns 88/2 CLASSIFICATION #superfamily barley myb-related protein 1; myb DNA-binding !1repeat homology KEYWORDS DNA binding; duplication; nucleus; transcription regulation FEATURE !$9-61 #domain myb DNA-binding repeat homology #label MYB1\ !$62-112 #domain myb DNA-binding repeat homology #label MYB2 SUMMARY #length 251 #molecular-weight 27602 #checksum 3997 SEQUENCE /// ENTRY JQ0957 #type complete TITLE myb-related protein 330 - garden snapdragon ORGANISM #formal_name Antirrhinum majus #common_name garden snapdragon DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 24-Jul-1997 ACCESSIONS JQ0957 REFERENCE JQ0956 !$#authors Jackson, D.; Culianez-Macia, F.; Prescott, A.G.; Roberts, !1K.; Martin, C. !$#journal Plant Cell (1991) 3:115-125 !$#title Expression patterns of myb genes from Antirrhinum flowers. !$#cross-references MUID:93005689; PMID:1840903 !$#accession JQ0957 !'##molecule_type mRNA !'##residues 1-274 ##label JAC !'##experimental_source strain JI:522 CLASSIFICATION #superfamily barley myb-related protein 1; myb DNA-binding !1repeat homology KEYWORDS DNA binding; duplication; nucleus; transcription regulation FEATURE !$9-61 #domain myb DNA-binding repeat homology #label MYB1\ !$62-112 #domain myb DNA-binding repeat homology #label MYB2 SUMMARY #length 274 #molecular-weight 30679 #checksum 1860 SEQUENCE /// ENTRY S45338 #type complete TITLE myb-related protein MIXTA - garden snapdragon ORGANISM #formal_name Antirrhinum majus #common_name garden snapdragon DATE 06-Jan-1995 #sequence_revision 06-Jan-1995 #text_change 18-Jun-1999 ACCESSIONS S45338; S44926 REFERENCE S45338 !$#authors Noda, K.; Glover, B.J.; Linstead, P.; Martin, C. !$#journal Nature (1994) 369:661-664 !$#title Flower colour intensity depends on specialized cell shape !1controlled by a Myb-related transcription factor. !$#cross-references MUID:94268554; PMID:8208293 !$#accession S45338 !'##status preliminary !'##molecule_type mRNA !'##residues 1-321 ##label NOD !'##cross-references EMBL:X79108; NID:g485866; PIDN:CAA55725.1; !1PID:g485867 CLASSIFICATION #superfamily myb-related protein MIXTA; myb DNA-binding !1repeat homology KEYWORDS DNA binding; duplication; nucleus; transcription regulation FEATURE !$9-61 #domain myb DNA-binding repeat homology #label MYB1\ !$62-112 #domain myb DNA-binding repeat homology #label MYB2 SUMMARY #length 321 #molecular-weight 36315 #checksum 8535 SEQUENCE /// ENTRY TVZMMB #type complete TITLE anthocyanin biosynthesis regulatory protein - maize ALTERNATE_NAMES transforming protein myb homolog ORGANISM #formal_name Zea mays #common_name maize DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 18-Jun-1999 ACCESSIONS S06215; S12369 REFERENCE S06215 !$#authors Paz-Ares, J.; Ghosal, D.; Wienand, U.; Peterson, P.A.; !1Saedler, H. !$#journal EMBO J. (1987) 6:3553-3558 !$#title The regulatory c1 locus of Zea mays encodes a protein with !1homology to myb proto-oncogene products and with structural !1similarities to transcriptional activators. !$#cross-references MUID:88111545; PMID:3428265 !$#accession S06215 !'##molecule_type DNA !'##residues 1-273 ##label PAZ !'##cross-references EMBL:M37153; NID:g168514; PIDN:AAA33482.1; !1PID:g168515 REFERENCE S12369 !$#authors Paz-Ares, J.; Ghosal, D.; Saedler, H. !$#journal EMBO J. (1990) 9:315-321 !$#title Molecular analysis of the C1-I allele from Zea mays: a !1dominant mutant of the regulatory C1 locus. !$#cross-references MUID:90151603; PMID:2303027 !$#accession S12369 !'##status preliminary !'##molecule_type DNA !'##residues 1-100,'E',102-121,124-125,'R',127-144,'SS',147-150,'KG', !1153-154,'P',156-181,'S',183-208,'VG',209-227,'P',229-248, !1'SWTT' ##label PA2 !'##cross-references GB:X52201; NID:g22213; PIDN:CAA36456.1; PID:g22214 !'##experimental_source C1-I allele GENETICS !$#gene C1 !$#introns 45/1; 88/2 FUNCTION !$#description transcription regulation; stimulates expression of genes !1involved in anthocyanin biosynthesis, including !1naringenin-chalcone synthase, dihydroflavonol 4-reductase, !1and flavonol 3-O-glucosyltransferase CLASSIFICATION #superfamily anthocyanin biosynthesis regulatory protein; !1myb DNA-binding repeat homology KEYWORDS DNA binding; duplication; nucleus; transcription regulation FEATURE !$9-61 #domain myb DNA-binding repeat homology #label MYB1\ !$62-112 #domain myb DNA-binding repeat homology #label MYB2 SUMMARY #length 273 #molecular-weight 28750 #checksum 5469 SEQUENCE /// ENTRY TVMUG1 #type complete TITLE trichome differentiation protein GL1 - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 18-Jun-1999 ACCESSIONS A39289; S42641 REFERENCE A39289 !$#authors Oppenheimer, D.G.; Herman, P.L.; Sivakumaran, S.; Esch, J.; !1Marks, M.D. !$#journal Cell (1991) 67:483-493 !$#title A myb gene required for leaf trichome differentiation in !1Arabidopsis is expressed in stipules. !$#cross-references MUID:92034971; PMID:1934056 !$#accession A39289 !'##molecule_type DNA !'##residues 1-228 ##label OPP !'##cross-references GB:M79448; NID:g166779; PIDN:AAC97387.1; !1PID:g166780 REFERENCE S42641 !$#authors Esch, J.J.; Oppenheimer, D.G.; Marks, M.D. !$#journal Plant Mol. Biol. (1994) 24:203-207 !$#title Characterization of a weak allele of the GL1 gene of !1Arabidopsis thaliana. !$#cross-references MUID:94154232; PMID:8111017 !$#accession S42641 !'##molecule_type DNA !'##residues 1-148,'C',150-201 ##label ESC !'##cross-references EMBL:L22786; NID:g438452; PIDN:AAC97388.1; !1PID:g438453 !'##experimental_source gl1-2 allele !'##note mutant allele of GL1; results in a reduction in leaf trichome !1initiation GENETICS !$#gene GL1 !$#introns 47/1; 90/2 FUNCTION !$#description transcription regulation; required for initiation of !1differentiation of hair cells (trichomes) on leaf primordia CLASSIFICATION #superfamily trichome differentiation protein GL1; myb !1DNA-binding repeat homology KEYWORDS DNA binding; duplication; nucleus; transcription regulation FEATURE !$11-63 #domain myb DNA-binding repeat homology #label MYB1\ !$64-114 #domain myb DNA-binding repeat homology #label MYB2 SUMMARY #length 228 #molecular-weight 26435 #checksum 8466 SEQUENCE /// ENTRY JQ0961 #type complete TITLE myb-related protein 315 - garden snapdragon ORGANISM #formal_name Antirrhinum majus #common_name garden snapdragon DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 01-Aug-1997 ACCESSIONS JQ0961 REFERENCE JQ0956 !$#authors Jackson, D.; Culianez-Macia, F.; Prescott, A.G.; Roberts, !1K.; Martin, C. !$#journal Plant Cell (1991) 3:115-125 !$#title Expression patterns of myb genes from Antirrhinum flowers. !$#cross-references MUID:93005689; PMID:1840903 !$#accession JQ0961 !'##molecule_type mRNA !'##residues 1-268 ##label JAC !'##experimental_source strain JI:522 COMMENT The gene encoding for this protein is expressed in all plant !1organs. CLASSIFICATION #superfamily Antirrhinum myb-related protein 315; myb !1DNA-binding repeat homology KEYWORDS DNA binding; duplication; nucleus; transcription regulation FEATURE !$9-61 #domain myb DNA-binding repeat homology #label MYB1\ !$62-112 #domain myb DNA-binding repeat homology #label MYB2 SUMMARY #length 268 #molecular-weight 31110 #checksum 4591 SEQUENCE /// ENTRY S69190 #type complete TITLE myb-related protein 1 - tomato ALTERNATE_NAMES TMH1 protein ORGANISM #formal_name Lycopersicon esculentum #common_name tomato DATE 06-Dec-1996 #sequence_revision 13-Mar-1997 #text_change 16-Jun-2000 ACCESSIONS S69190 REFERENCE S69189 !$#authors Lin, Q.; Hamilton, W.D.O.; Merryweather, A. !$#journal Plant Mol. Biol. (1996) 30:1009-1020 !$#title Cloning and initial characterization of 14 myb-related cDNAs !1from tomato (Lycopersicon esculentum cv. Ailsa Craig). !$#cross-references MUID:96270378; PMID:8639738 !$#accession S69190 !'##molecule_type mRNA !'##residues 1-331 ##label LIN !'##cross-references EMBL:X95297; NID:g1167485; PIDN:CAA64615.1; !1PID:g1167486 !'##experimental_source cv. Ailsa Craig, three-week old seedlings GENETICS !$#gene TMH1 CLASSIFICATION #superfamily tomato myb-related protein 1; myb DNA-binding !1repeat homology KEYWORDS DNA binding; duplication; nucleus; transcription regulation FEATURE !$9-61 #domain myb DNA-binding repeat homology #label MYB1\ !$62-112 #domain myb DNA-binding repeat homology #label MYB2 SUMMARY #length 331 #molecular-weight 37826 #checksum 622 SEQUENCE /// ENTRY S68688 #type complete TITLE myb-related protein 5 - Arabidopsis thaliana ALTERNATE_NAMES protein Atmyb5 ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 15-Nov-1996 #sequence_revision 27-Feb-1997 #text_change 18-Jun-1999 ACCESSIONS S68688 REFERENCE S68688 !$#authors Li, S.F.; Santini, J.M.; Nicolaou, O.; Parish, R.W. !$#journal FEBS Lett. (1996) 379:117-121 !$#title A novel myb-related gene from Arabidopsis thaliana. !$#cross-references MUID:96225952; PMID:8635574 !$#accession S68688 !'##molecule_type DNA !'##residues 1-249 ##label LIS !'##cross-references EMBL:U26935; NID:g1254994; PIDN:AAC49311.1; !1PID:g1218000 !'##experimental_source strain Landsberg erecta GENETICS !$#gene myb5 !$#introns 99/3 CLASSIFICATION #superfamily Arabidopsis myb-related protein 5; myb !1DNA-binding repeat homology KEYWORDS DNA binding; duplication; nucleus; transcription regulation FEATURE !$20-72 #domain myb DNA-binding repeat homology #label MYB1\ !$73-123 #domain myb DNA-binding repeat homology #label MYB2 SUMMARY #length 249 #molecular-weight 27793 #checksum 343 SEQUENCE /// ENTRY S04898 #type complete TITLE myb-related protein 1 - maize ALTERNATE_NAMES myb-related protein Zm1 ORGANISM #formal_name Zea mays #common_name maize DATE 28-Feb-1990 #sequence_revision 28-Feb-1990 #text_change 01-Aug-1997 ACCESSIONS S04898 REFERENCE S04896 !$#authors Marocco, A.; Wissenbach, M.; Becker, D.; Paz-Ares, J.; !1Saedler, H.; Salamini, F.; Rohde, W. !$#journal Mol. Gen. Genet. (1989) 216:183-187 !$#title Multiple genes are transcribed in Hordeum vulgare and Zea !1mays that carry the DNA binding domain of the myb !1oncoproteins. !$#cross-references MUID:89313655; PMID:2664447 !$#accession S04898 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-340 ##label MAR CLASSIFICATION #superfamily maize myb-related protein 1; myb DNA-binding !1repeat homology KEYWORDS DNA binding; duplication; nucleus; transcription regulation FEATURE !$11-63 #domain myb DNA-binding repeat homology #label MYB1\ !$64-114 #domain myb DNA-binding repeat homology #label MYB2 SUMMARY #length 340 #molecular-weight 36239 #checksum 3322 SEQUENCE /// ENTRY S26606 #type complete TITLE myb-related protein 3 - garden petunia ORGANISM #formal_name Petunia x hybrida #common_name garden petunia DATE 25-Feb-1994 #sequence_revision 03-Nov-1995 #text_change 22-Oct-1999 ACCESSIONS S26606 REFERENCE S26604 !$#authors Avila, J.; Nieto, C.; Canas, L.; Benito, M.; Paz-Ares, J. !$#submission submitted to the EMBL Data Library, July 1992 !$#description Petunia hybrida genes related to the maize regulatory C1 !1gene and to animal myb proto-oncogenes. !$#accession S26606 !'##molecule_type DNA !'##residues 1-517 ##label AVI !'##cross-references EMBL:Z13998; NID:g20564; PIDN:CAA78388.1; !1PID:g20565 !'##experimental_source strain v26, developing flowers CLASSIFICATION #superfamily petunia myb-related protein 3; myb DNA-binding !1repeat homology KEYWORDS DNA binding; duplication; nucleus; transcription regulation FEATURE !$25-77 #domain myb DNA-binding repeat homology #label MYB1\ !$78-128 #domain myb DNA-binding repeat homology #label MYB2 SUMMARY #length 517 #molecular-weight 57260 #checksum 5915 SEQUENCE /// ENTRY S26605 #type complete TITLE myb-related protein 1 - garden petunia ORGANISM #formal_name Petunia x hybrida #common_name garden petunia DATE 25-Feb-1994 #sequence_revision 03-Nov-1995 #text_change 22-Oct-1999 ACCESSIONS S26605 REFERENCE S26604 !$#authors Avila, J.; Nieto, C.; Canas, L.; Benito, M.; Paz-Ares, J. !$#submission submitted to the EMBL Data Library, July 1992 !$#description Petunia hybrida genes related to the maize regulatory C1 !1gene and to animal myb proto-oncogenes. !$#accession S26605 !'##molecule_type DNA !'##residues 1-421 ##label AVI !'##cross-references EMBL:Z13996; NID:g20562; PIDN:CAA78386.1; !1PID:g20563 !'##experimental_source strain v26, developing flowers CLASSIFICATION #superfamily petunia myb-related protein 1; myb DNA-binding !1repeat homology KEYWORDS DNA binding; duplication; nucleus; transcription regulation FEATURE !$9-61 #domain myb DNA-binding repeat homology #label MYB1\ !$62-112 #domain myb DNA-binding repeat homology #label MYB2 SUMMARY #length 421 #molecular-weight 46080 #checksum 5792 SEQUENCE /// ENTRY S58294 #type complete TITLE myb-related protein Y19 - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 14-Jan-1996 #sequence_revision 19-Apr-1996 #text_change 18-Jun-1999 ACCESSIONS S58294 REFERENCE S58280 !$#authors Quaedvlieg, N.E.M.; Dockx, J.; Keultjes, G.G.M.; Smeekens, !1J.C.M. !$#submission submitted to the EMBL Data Library, July 1995 !$#accession S58294 !'##molecule_type DNA !'##residues 1-122 ##label QUA !'##cross-references EMBL:X90384; NID:g928966; PIDN:CAA62032.1; !1PID:g928967 GENETICS !$#introns 44/3; 88/3 CLASSIFICATION #superfamily Arabidopsis myb-related protein Y19; myb !1DNA-binding repeat homology KEYWORDS DNA binding; duplication; nucleus; transcription regulation FEATURE !$9-61 #domain myb DNA-binding repeat homology #label MYB1\ !$62-112 #domain myb DNA-binding repeat homology #label MYB2 SUMMARY #length 122 #molecular-weight 14058 #checksum 4064 SEQUENCE /// ENTRY S22520 #type complete TITLE myb-related protein 1 - Arabidopsis thaliana ALTERNATE_NAMES protein Atmyb1 ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 03-Feb-1994 #sequence_revision 03-Feb-1994 #text_change 16-Jun-2000 ACCESSIONS S22520 REFERENCE S22520 !$#authors Shinozaki, K.; Yamaguchi-Shinozaki, K.; Urao, T.; Koizumi, !1M. !$#journal Plant Mol. Biol. (1992) 19:493-499 !$#title Nucleotide sequence of a gene from Arabidopsis thaliana !1encoding a myb homologue. !$#cross-references MUID:92322982; PMID:1623193 !$#accession S22520 !'##molecule_type DNA !'##residues 1-393 ##label SHI !'##cross-references EMBL:D10936; NID:g217858; PIDN:BAA01730.1; !1PID:g217859 !'##experimental_source strain Columbia GENETICS !$#gene myb1 !$#introns 112/1 CLASSIFICATION #superfamily Arabidopsis myb-related protein 1; myb !1DNA-binding repeat homology KEYWORDS DNA binding; duplication; nucleus; transcription regulation FEATURE !$50-101 #domain myb DNA-binding repeat homology #label MYB1\ !$102-152 #domain myb DNA-binding repeat homology #label MYB2 SUMMARY #length 393 #molecular-weight 42811 #checksum 6250 SEQUENCE /// ENTRY S24244 #type complete TITLE myb-related protein 2 - moss (Physcomitrella patens) ALTERNATE_NAMES myb-related protein Pp2 ORGANISM #formal_name Physcomitrella patens DATE 19-Feb-1994 #sequence_revision 26-May-1995 #text_change 18-Jun-1999 ACCESSIONS S24244 REFERENCE S24244 !$#authors Leech, M.J.; Martin, C.M.; Wang, T.L. !$#submission submitted to the EMBL Data Library, April 1992 !$#description Regulation of myb-related genes in the moss, Physcomitrella !1patens. !$#accession S24244 !'##molecule_type mRNA !'##residues 1-421 ##label LEE !'##cross-references EMBL:X67050; NID:g22637; PIDN:CAA47435.1; !1PID:g22638 CLASSIFICATION #superfamily Physcomitrella myb-related protein 2; myb !1DNA-binding repeat homology KEYWORDS DNA binding; duplication; nucleus; transcription regulation FEATURE !$9-61 #domain myb DNA-binding repeat homology #label MYB1\ !$62-112 #domain myb DNA-binding repeat homology #label MYB2 SUMMARY #length 421 #molecular-weight 46695 #checksum 5267 SEQUENCE /// ENTRY TVHUET #type complete TITLE transcription factor ets-1, splice form a - human ALTERNATE_NAMES transcription factor p54; transforming protein ets-1a ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jul-1999 ACCESSIONS A32066; S10086; S22952; I56994; I59051 REFERENCE A94208 !$#authors Watson, D.K.; McWilliams, M.J.; Lapis, P.; Lautenberger, !1J.A.; Schweinfest, C.W.; Papas, T.S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:7862-7866 !$#title Mammalian ets-1 and ets-2 genes encode highly conserved !1proteins. !$#cross-references MUID:89042086; PMID:2847145 !$#accession A32066 !'##molecule_type mRNA !'##residues 1-441 ##label WAT !'##cross-references GB:J04101; NID:g182268; PIDN:AAA52410.1; !1PID:g182269 REFERENCE S10086 !$#authors Reddy, E.S.P.; Rao, V.N. !$#journal Oncogene Res. (1988) 3:239-246 !$#title Structure, expression and alternative splicing of the human !1c-ets-1 proto-oncogene. !$#cross-references MUID:89083219; PMID:3060801 !$#accession S10086 !'##status preliminary !'##molecule_type mRNA !'##residues 1-441 ##label RED !'##cross-references EMBL:X14798; NID:g29881; PIDN:CAA32904.1; !1PID:g29882 REFERENCE S22952 !$#authors Majerus, M.A.; Bibollet-Ruche, F.; Telliez, J.B.; Wasylyk, !1B.; Bailleul, B. !$#journal Nucleic Acids Res. (1992) 20:2699-2703 !$#title Serum, AP-1 and Ets-1 stimulate the human ets-1 promoter. !$#cross-references MUID:92310964; PMID:1614856 !$#accession S22952 !'##status translation not shown !'##molecule_type DNA !'##residues 1-27 ##label MAJ !'##cross-references EMBL:X65469 REFERENCE I56994 !$#authors Collyn d'Hooghe, M.; Galiegue-Zouitina, S.; Szymiczek, D.; !1Lantoine, D.; Quief, S.; Loucheux-Lefebvre, M.H.; Kerckaert, !1J.P. !$#journal Leukemia (1993) 7:1777-1785 !$#title Quantitative and qualitative variation of ETS-1 transcripts !1in hematologic malignancies. !$#cross-references MUID:94048220; PMID:8231246 !$#accession I56994 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 146-161,'C',163-174 ##label RES !'##cross-references GB:S67063; NID:g452904; PIDN:AAB28747.1; !1PID:g452905 REFERENCE I59051 !$#authors Watson, D.K.; McWilliams-Smith, M.J.; Nunn, M.F.; Duesberg, !1P.H.; O'Brien, S.J.; Papas, T.S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:7294-7298 !$#title The ets sequence from the transforming gene of avian !1erythroblastosis virus, E26, has unique domains on human !1chromosomes 11 and 21: both loci are transcriptionally !1active. !$#cross-references MUID:86042652; PMID:2997781 !$#accession I59051 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 'FLPPPLPP',244-331,'RR',334,'PAA' ##label RE2 !'##cross-references GB:M11921; NID:g182266; PIDN:AAA52409.1; !1PID:g182267 GENETICS !$#gene GDB:ETS1 !'##cross-references GDB:119122; OMIM:164720 !$#map_position 11q23.3-11q23.3 CLASSIFICATION #superfamily transcription factor ets; ets DNA-binding !1domain homology; ets RII regulatory region homology KEYWORDS alternative splicing; DNA binding; nucleus; phosphoprotein; !1proto-oncogene; transcription factor FEATURE !$57-130 #domain ets RII regulatory region homology #label !8ETR\ !$97-130 #region helix-loop-helix #status predicted\ !$337-415 #domain ets DNA-binding domain homology #label ETS\ !$377-383 #region nuclear location signal SUMMARY #length 441 #molecular-weight 50407 #checksum 5545 SEQUENCE /// ENTRY A53988 #type complete TITLE transcription factor ets-1, splice form a - rat ALTERNATE_NAMES transcription factor p54; transforming protein ets-1a; transforming protein Tpl-1 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 09-Oct-1994 #sequence_revision 23-May-1997 #text_change 16-Jul-1999 ACCESSIONS A53988 REFERENCE A53988 !$#authors Bellacosa, A.; Datta, K.; Bear, S.E.; Patriotis, C.; Lazo, !1P.A.; Copeland, N.G.; Jenkins, N.A.; Tsichlis, P.N. !$#journal J. Virol. (1994) 68:2320-2330 !$#title Effects of provirus integration in the Tpl-1/Ets-1 locus in !1Moloney murine leukemia virus-induced rat T-cell lymphomas: !1levels of expression, polyadenylation, transcriptional !1initiation, and differential splicing of the Ets-1 mRNA. !$#cross-references MUID:94187072; PMID:8139017 !$#accession A53988 !'##status preliminary !'##molecule_type mRNA !'##residues 1-441 ##label BEL !'##cross-references GB:L20681; NID:g404781; PIDN:AAA21093.1; !1PID:g404782 GENETICS !$#gene ets-1 CLASSIFICATION #superfamily transcription factor ets; ets DNA-binding !1domain homology; ets RII regulatory region homology KEYWORDS alternative splicing; DNA binding; nucleus; phosphoprotein; !1proto-oncogene FEATURE !$57-130 #domain ets RII regulatory region homology #label !8ETR\ !$97-130 #region helix-loop-helix #status predicted\ !$337-415 #domain ets DNA-binding domain homology #label ETS\ !$377-383 #region nuclear location signal SUMMARY #length 441 #molecular-weight 50422 #checksum 6268 SEQUENCE /// ENTRY A35875 #type complete TITLE transcription factor ets-1, splice form a - mouse ALTERNATE_NAMES transcription factor p54; transforming protein ets-1a ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Mar-1992 #sequence_revision 23-May-1997 #text_change 16-Jul-1999 ACCESSIONS A30487; A35875 REFERENCE A30487 !$#authors Graves, B.J. !$#submission submitted to the EMBL Data Library, July 1990 !$#accession A30487 !'##molecule_type mRNA !'##residues 1-440 ##label GRA !'##cross-references EMBL:X53953; NID:g50870; PIDN:CAA37904.1; !1PID:g50871 !'##experimental_source strain BALB/C, thymus tissue REFERENCE A35875 !$#authors Gunther, C.V.; Nye, J.A.; Bryner, R.S.; Graves, B.J. !$#journal Genes Dev. (1990) 4:667-679 !$#title Sequence-specific DNA binding of the proto-oncoprotein ets-1 !1defines a transcriptional activator sequence within the long !1terminal repeat of the Moloney murine sarcoma virus. !$#cross-references MUID:90299137; PMID:2163347 !$#accession A35875 !'##molecule_type mRNA !'##residues 170-440 ##label GUN !'##cross-references EMBL:X53953 GENETICS !$#gene Ets1 !$#map_position 9 15.0 CLASSIFICATION #superfamily transcription factor ets; ets DNA-binding !1domain homology; ets RII regulatory region homology KEYWORDS alternative splicing; DNA binding; nucleus; phosphoprotein; !1proto-oncogene FEATURE !$57-130 #domain ets RII regulatory region homology #label !8ETR\ !$97-130 #region helix-loop-helix #status predicted\ !$337-415 #domain ets DNA-binding domain homology #label ETS\ !$377-383 #region nuclear location signal SUMMARY #length 440 #molecular-weight 50201 #checksum 2673 SEQUENCE /// ENTRY TVCHTE #type complete TITLE transcription factor ets-1, splice form a - chicken ALTERNATE_NAMES transcription factor p54; transforming protein ets-1a ORGANISM #formal_name Gallus gallus #common_name chicken DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jul-1999 ACCESSIONS A31285; S07625; S29132; I51223 REFERENCE A31285 !$#authors Watson, D.K.; McWilliams, M.J.; Papas, T.S. !$#journal Virology (1988) 167:1-7 !$#title A unique amino-terminal sequence predicted for the chicken !1proto-ets protein. !$#cross-references MUID:89045631; PMID:2847407 !$#accession A31285 !'##molecule_type mRNA !'##residues 1-441 ##label WAT !'##cross-references GB:M22462; NID:g211752; PIDN:AAA48764.1; !1PID:g211753 REFERENCE S07625 !$#authors Duterque-Coquillaud, M.; Leprince, D.; Flourens, A.; Henry, !1C.; Ghysdael, J.; Debuire, B.; Stehelin, D. !$#journal Oncogene Res. (1988) 2:335-344 !$#title Cloning and expression of chicken p54(c-ets) cDNA(s): the !1first p54(c-ets) coding exon is located into the 40.0 kbp !1genomic domain unrelated to v-ets. !$#cross-references MUID:88289026; PMID:3041344 !$#accession S07625 !'##molecule_type mRNA !'##residues 1-116,'R',118-441 ##label DUT !'##cross-references EMBL:X13026; NID:g63179; PIDN:CAA31441.1; !1PID:g63180 !'##note the authors translated the codon AGC for residue 26 as Phe and !1CGG for residue 117 as Ala REFERENCE S29132 !$#authors Chen, J.H. !$#journal Oncogene Res. (1988) 2:371-384 !$#title Complementary DNA clones of chicken proto-oncogene c-ets: !1sequence divergence from the viral oncogene v-ets. !$#cross-references MUID:88289029; PMID:3041346 !$#accession S29132 !'##molecule_type mRNA !'##residues 1-116,'R',118-441 ##label CHE !'##cross-references EMBL:X13027; NID:g63382; PIDN:CAA31442.1; !1PID:g63383 !'##experimental_source spleen REFERENCE I51223 !$#authors Crepieux, P.; Leprince, D.; Flourens, A.; Albagli, O.; !1Ferreira, E.; Stehelin, D. !$#journal Gene Expr. (1993) 3:215-225 !$#title The two functionally distinct amino termini of chicken !1c-ets-1 products arise from alternative promoter usage. !$#cross-references MUID:94093304; PMID:8268721 !$#accession I51223 !'##status preliminary !'##molecule_type DNA !'##residues 1-22 ##label CRE !'##cross-references GB:S68254; NID:g471777; PIDN:AAB29406.1; !1PID:g471778 GENETICS !$#gene ets-1 CLASSIFICATION #superfamily transcription factor ets; ets DNA-binding !1domain homology; ets RII regulatory region homology KEYWORDS alternative splicing; DNA binding; nucleus; phosphoprotein; !1proto-oncogene; transcription regulation FEATURE !$57-130 #domain ets RII regulatory region homology #label !8ETR\ !$97-130 #region helix-loop-helix #status predicted\ !$337-415 #domain ets DNA-binding domain homology #label ETS\ !$377-383 #region nuclear location signal SUMMARY #length 441 #molecular-weight 50241 #checksum 4479 SEQUENCE /// ENTRY TVFVES #type complete TITLE transcription factor ets - avian erythroblastosis virus (strain E26) ORGANISM #formal_name avian erythroblastosis virus DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jul-1999 ACCESSIONS B01348; A01348 REFERENCE A93319 !$#authors Nunn, M.F.; Seeburg, P.H.; Moscovici, C.; Duesberg, P.H. !$#journal Nature (1983) 306:391-395 !$#title Tripartite structure of the avian erythroblastosis virus E26 !1transforming gene. !$#cross-references MUID:84068165; PMID:6316155 !$#accession B01348 !'##molecule_type DNA !'##residues 1-488 ##label NUN !'##cross-references GB:X00144 COMMENT This protein is translated as a myb-ets polyprotein; only !1the ets part is shown. GENETICS !$#gene ets CLASSIFICATION #superfamily transcription factor ets; ets DNA-binding !1domain homology; ets RII regulatory region homology KEYWORDS DNA binding; oncogene; transforming protein FEATURE !$101-174 #domain ets RII regulatory region homology #label !8ETR\ !$141-174 #region helix-loop-helix #status predicted\ !$381-459 #domain ets DNA-binding domain homology #label ETS\ !$421-427 #region nuclear location signal SUMMARY #length 488 #molecular-weight 55142 #checksum 916 SEQUENCE /// ENTRY TVCHET #type complete TITLE transcription factor ets-1, splice form b - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jul-1999 ACCESSIONS A28875; A28610 REFERENCE A28875 !$#authors Leprince, D.; Duterque-Coquillaud, M.; Li, R.P.; Henry, C.; !1Flourens, A.; Debuire, B.; Stehelin, D. !$#journal J. Virol. (1988) 62:3233-3241 !$#title Alternative splicing within the chicken c-ets-1 locus: !1implications for transduction within the E26 retrovirus of !1the c-ets proto-oncogene. !$#cross-references MUID:88300873; PMID:2841475 !$#accession A28875 !'##molecule_type mRNA !'##residues 1-485 ##label LEP !'##cross-references GB:M21823; NID:g211465; PIDN:AAA48669.1; !1PID:g211466 REFERENCE A28610 !$#authors Watson, D.K.; McWilliams, M.J.; Papas, T.S. !$#journal Virology (1988) 164:99-105 !$#title Molecular organization of the chicken ets locus. !$#cross-references MUID:88206088; PMID:3284179 !$#accession A28610 !'##molecule_type DNA !'##residues 1-485 ##label WAT !'##cross-references GB:M20507; GB:M20508; GB:M20509; GB:M20510; !1GB:M20511; GB:M20512; GB:M20513; GB:M20514; GB:M20515 GENETICS !$#gene ets-1 CLASSIFICATION #superfamily transcription factor ets; ets DNA-binding !1domain homology; ets RII regulatory region homology KEYWORDS alternative splicing; DNA binding; nucleus; proto-oncogene; !1transcription factor; transforming protein FEATURE !$101-174 #domain ets RII regulatory region homology #label !8ETR\ !$141-174 #region helix-loop-helix #status predicted\ !$381-459 #domain ets DNA-binding domain homology #label ETS\ !$421-427 #region nuclear location signal SUMMARY #length 485 #molecular-weight 55020 #checksum 1040 SEQUENCE /// ENTRY S11225 #type complete TITLE transcription factor ets-1, splice form a - African clawed frog ALTERNATE_NAMES transcription factor p54; transforming protein ets-1a ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 18-Feb-1994 #sequence_revision 23-May-1997 #text_change 16-Jul-1999 ACCESSIONS S11225 REFERENCE S11224 !$#authors Stiegler, P.; Wolff, C.M.; Baltzinger, M.; Hirtzlin, J.; !1Senan, F.; Meyer, D.; Ghysdael, J.; Stehelin, D.; Befort, !1N.; Remy, P. !$#journal Nucleic Acids Res. (1990) 18:5298 !$#title Characterization of Xenopus laevis cDNA clones of the !1c-ets-1 proto-oncogene. !$#cross-references MUID:90384849; PMID:2205841 !$#accession S11225 !'##molecule_type mRNA !'##residues 1-438 ##label STI !'##cross-references EMBL:X52692; NID:g64614; PIDN:CAA36919.1; !1PID:g64615 !'##experimental_source oocytes GENETICS !$#gene ets-1 CLASSIFICATION #superfamily transcription factor ets; ets DNA-binding !1domain homology; ets RII regulatory region homology KEYWORDS alternative splicing; DNA binding; nucleus; phosphoprotein; !1proto-oncogene FEATURE !$55-128 #domain ets RII regulatory region homology #label !8ETR\ !$95-128 #region helix-loop-helix #status predicted\ !$334-412 #domain ets DNA-binding domain homology #label ETS\ !$374-380 #region nuclear location signal SUMMARY #length 438 #molecular-weight 50267 #checksum 6611 SEQUENCE /// ENTRY TVHUE2 #type complete TITLE transcription factor ets-2 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1989 #sequence_revision 23-May-1997 #text_change 16-Jul-1999 ACCESSIONS B32066; I79404; I37377 REFERENCE A94208 !$#authors Watson, D.K.; McWilliams, M.J.; Lapis, P.; Lautenberger, !1J.A.; Schweinfest, C.W.; Papas, T.S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:7862-7866 !$#title Mammalian ets-1 and ets-2 genes encode highly conserved !1proteins. !$#cross-references MUID:89042086; PMID:2847145 !$#accession B32066 !'##molecule_type mRNA !'##residues 1-469 ##label WAT !'##cross-references GB:J04102; NID:g182272; PIDN:AAA52412.1; !1PID:g182273 REFERENCE I59051 !$#authors Watson, D.K.; McWilliams-Smith, M.J.; Nunn, M.F.; Duesberg, !1P.H.; O'Brien, S.J.; Papas, T.S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:7294-7298 !$#title The ets sequence from the transforming gene of avian !1erythroblastosis virus, E26, has unique domains on human !1chromosomes 11 and 21: both loci are transcriptionally !1active. !$#cross-references MUID:86042652; PMID:2997781 !$#accession I79404 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 324-469 ##label RES !'##cross-references GB:M11922; NID:g182270; PIDN:AAA52411.1; !1PID:g182271 REFERENCE I37377 !$#authors Watson, D.K.; Mavrothalassitis, G.J.; Jorcyk, C.L.; Smyth, !1F.E.; Papas, T.S. !$#journal Oncogene (1990) 5:1521-1527 !$#title Molecular organization and differential polyadenylation !1sites of the human ETS2 gene. !$#cross-references MUID:91067187; PMID:2250910 !$#accession I37377 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 399-469 ##label RE2 !'##cross-references EMBL:X55181; NID:g31265; PIDN:CAA38966.1; !1PID:g31266 GENETICS !$#gene GDB:ETS2 !'##cross-references GDB:119888; OMIM:164740 !$#map_position 21q22.3-21q22.3 CLASSIFICATION #superfamily transcription factor ets; ets DNA-binding !1domain homology; ets RII regulatory region homology KEYWORDS DNA binding; nucleus; proto-oncogene; transcription factor; !1transforming protein FEATURE !$91-164 #domain ets RII regulatory region homology #label !8ETR\ !$131-164 #region helix-loop-helix #status predicted\ !$365-443 #domain ets DNA-binding domain homology #label ETS\ !$405-411 #region nuclear location signal SUMMARY #length 469 #molecular-weight 53001 #checksum 9832 SEQUENCE /// ENTRY TVMSE2 #type complete TITLE transcription factor ets-2 - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1989 #sequence_revision 23-May-1997 #text_change 16-Jul-1999 ACCESSIONS C32066 REFERENCE A94208 !$#authors Watson, D.K.; McWilliams, M.J.; Lapis, P.; Lautenberger, !1J.A.; Schweinfest, C.W.; Papas, T.S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:7862-7866 !$#title Mammalian ets-1 and ets-2 genes encode highly conserved !1proteins. !$#cross-references MUID:89042086; PMID:2847145 !$#accession C32066 !'##molecule_type mRNA !'##residues 1-468 ##label WAT !'##cross-references GB:J04103; NID:g193193; PIDN:AAA37581.1; !1PID:g309221 GENETICS !$#gene Ets2 !$#map_position 16 68.5 CLASSIFICATION #superfamily transcription factor ets; ets DNA-binding !1domain homology; ets RII regulatory region homology KEYWORDS DNA binding; nucleus; proto-oncogene; transcription factor; !1transforming protein FEATURE !$91-164 #domain ets RII regulatory region homology #label !8ETR\ !$131-164 #region helix-loop-helix #status predicted\ !$364-442 #domain ets DNA-binding domain homology #label ETS\ !$404-410 #region nuclear location signal SUMMARY #length 468 #molecular-weight 52827 #checksum 6346 SEQUENCE /// ENTRY TVCHE2 #type complete TITLE transcription factor ets-2 - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Jul-1999 ACCESSIONS S00386 REFERENCE S00386 !$#authors Boulukos, K.E.; Pognonec, P.; Begue, A.; Galibert, F.; !1Gesquiere, J.C.; Stehelin, D.; Ghysdael, J. !$#journal EMBO J. (1988) 7:697-705 !$#title Identification in chickens of an evolutionarily conserved !1cellular ets-2 gene (c-ets-2) encoding nuclear proteins !1related to the products of the c-ets proto-oncogene. !$#cross-references MUID:88283637; PMID:3293999 !$#accession S00386 !'##molecule_type mRNA !'##residues 1-479 ##label BOU !'##cross-references EMBL:X07202; NID:g63181; PIDN:CAA30178.1; !1PID:g63182 !'##note it is uncertain whether 1-Met, 9-Met, 18-Met, or 22-Met is the !1initiator codon GENETICS !$#gene ets-2 CLASSIFICATION #superfamily transcription factor ets; ets DNA-binding !1domain homology; ets RII regulatory region homology KEYWORDS DNA binding; nucleus; phosphoprotein; proto-oncogene; !1transcription factor; transforming protein FEATURE !$94-167 #domain ets RII regulatory region homology #label !8ETR\ !$134-167 #region helix-loop-helix #status predicted\ !$375-453 #domain ets DNA-binding domain homology #label ETS\ !$415-421 #region nuclear location signal SUMMARY #length 479 #molecular-weight 54540 #checksum 1969 SEQUENCE /// ENTRY A53236 #type complete TITLE transcription factor ets-2b - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 02-May-1994 #sequence_revision 23-May-1997 #text_change 16-Jul-1999 ACCESSIONS A53236; S16517; I51415 REFERENCE A53236 !$#authors Wolff, C.M.; Stiegler, P.; Baltzinger, M.; Meyer, D.; !1Ghysdael, J.; Stehelin, D.; Befort, N.; Remy, P. !$#journal Cell Growth Differ. (1991) 2:447-456 !$#title Cloning, sequencing, and expression of two Xenopus laevis !1c-ets-2 protooncogenes. !$#cross-references MUID:92088972; PMID:1751411 !$#accession A53236 !'##status preliminary !'##molecule_type mRNA !'##residues 1-472 ##label WOL !'##cross-references GB:X52635; NID:g64620; PIDN:CAA36860.1; PID:g64621 !'##note sequence extracted from NCBI backbone (NCBIN:71222, !1NCBIP:71224) REFERENCE S10994 !$#authors Wolff, C.M.; Stiegler, P.; Baltzinger, M.; Meyer, D.; !1Ghysdael, J.; Stehelin, D.; Befort, N.; Remy, P. !$#journal Nucleic Acids Res. (1990) 18:4603-4604 !$#title Isolation of two different c-ets-2 proto-oncogenes in !1Xenopus laevis. !$#cross-references MUID:90356411; PMID:2201951 !$#accession S16517 !'##molecule_type mRNA !'##residues 121-472 ##label WO2 !'##cross-references EMBL:X52635 REFERENCE S28824 !$#authors Burdett, L.A.; Qi, S.M.; Chen, Z. !$#journal Nucleic Acids Res. (1992) 20:371 !$#title Characterization of the cDNA sequences of two Xenopus cis-2 !1proto-oncogenes. !$#cross-references MUID:92158632; PMID:1741266 !$#accession I51415 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-146 ##label BUR !'##cross-references GB:M81684; NID:g214131; PIDN:AAA49706.1; !1PID:g214132 GENETICS !$#gene ets-2b CLASSIFICATION #superfamily transcription factor ets; ets DNA-binding !1domain homology; ets RII regulatory region homology KEYWORDS DNA binding; nucleus; proto-oncogene; transcription factor; !1transforming protein FEATURE !$91-164 #domain ets RII regulatory region homology #label !8ETR\ !$131-164 #region helix-loop-helix #status predicted\ !$368-446 #domain ets DNA-binding domain homology #label ETS\ !$408-414 #region nuclear location signal SUMMARY #length 472 #molecular-weight 53928 #checksum 1916 SEQUENCE /// ENTRY B53236 #type complete TITLE transcription factor ets-2a - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 02-May-1994 #sequence_revision 23-May-1997 #text_change 16-Jul-1999 ACCESSIONS S28824; S10994; B53236; I51414 REFERENCE S28824 !$#authors Burdett, L.A.; Qi, S.M.; Chen, Z. !$#journal Nucleic Acids Res. (1992) 20:371 !$#title Characterization of the cDNA sequences of two Xenopus cis-2 !1proto-oncogenes. !$#cross-references MUID:92158632; PMID:1741266 !$#accession S28824 !'##status preliminary !'##molecule_type mRNA !'##residues 1-472 ##label BUR !'##cross-references EMBL:M81683; NID:g214129; PIDN:AAA49705.1; !1PID:g214130 REFERENCE S10994 !$#authors Wolff, C.M.; Stiegler, P.; Baltzinger, M.; Meyer, D.; !1Ghysdael, J.; Stehelin, D.; Befort, N.; Remy, P. !$#journal Nucleic Acids Res. (1990) 18:4603-4604 !$#title Isolation of two different c-ets-2 proto-oncogenes in !1Xenopus laevis. !$#cross-references MUID:90356411; PMID:2201951 !$#accession S10994 !'##molecule_type mRNA !'##residues 121-472 ##label WOL !'##cross-references EMBL:X51826; NID:g64618; PIDN:CAA36124.1; !1PID:g64619 REFERENCE A53236 !$#authors Wolff, C.M.; Stiegler, P.; Baltzinger, M.; Meyer, D.; !1Ghysdael, J.; Stehelin, D.; Befort, N.; Remy, P. !$#journal Cell Growth Differ. (1991) 2:447-456 !$#title Cloning, sequencing, and expression of two Xenopus laevis !1c-ets-2 protooncogenes. !$#cross-references MUID:92088972; PMID:1751411 !$#accession B53236 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 121-472 ##label WO2 !'##cross-references EMBL:X52635; NID:g64620 !'##note sequence extracted from NCBI backbone (NCBIP:71225) GENETICS !$#gene ets-2a CLASSIFICATION #superfamily transcription factor ets; ets DNA-binding !1domain homology; ets RII regulatory region homology KEYWORDS DNA binding; nucleus; proto-oncogene; transcription factor; !1transforming protein FEATURE !$91-164 #domain ets RII regulatory region homology #label !8ETR\ !$131-164 #region helix-loop-helix #status predicted\ !$368-446 #domain ets DNA-binding domain homology #label ETS\ !$408-414 #region nuclear location signal SUMMARY #length 472 #molecular-weight 53894 #checksum 1457 SEQUENCE /// ENTRY TVHUEG #type complete TITLE transforming protein erg-3 - human CONTAINS transforming protein erg-1; transforming protein erg-2 ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1989 #sequence_revision 30-May-1997 #text_change 16-Jul-1999 ACCESSIONS A94294; A94178; I58410; A28041; A29515 REFERENCE A94294 !$#authors Rao, V.N.; Papas, T.S.; Shyam, E.; Reddy, P. !$#journal Science (1987) 237:635-639 !$#title erg, a human ets-related gene on chromosome 21: alternative !1splicing, polyadenylation, and translation. !$#cross-references MUID:87263429; PMID:3299708 !$#accession A94294 !'##molecule_type mRNA !'##residues 1-231,256-486 ##label REA !'##cross-references GB:M17254; NID:g182186; PIDN:AAA52398.1; !1PID:g182187 REFERENCE A94178 !$#authors Reddy, E.S.P.; Rao, V.N.; Papas, T.S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:6131-6135 !$#title The erg gene: a human gene related to the ets oncogene. !$#cross-references MUID:87317608; PMID:3476934 !$#accession A94178 !'##molecule_type mRNA !'##residues 100-231,256-486 ##label REB !'##cross-references GB:M21535; NID:g182182; PIDN:AAA35811.1; !1PID:g182185 REFERENCE I58410 !$#authors Prasad, D.D.; Rao, V.N.; Lee, L.; Reddy, E.S. !$#journal Oncogene (1994) 9:669-673 !$#title Differentially spliced erg-3 product functions as a !1transcriptional activator. !$#cross-references MUID:94119611; PMID:8290279 !$#accession I58410 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 230-259 ##label RES !'##cross-references GB:S68130; NID:g544960; PIDN:AAB29724.1; !1PID:g544961 GENETICS !$#gene GDB:ERG !'##cross-references GDB:119884; OMIM:165080 !$#map_position 21q22.2-21q22.2 CLASSIFICATION #superfamily transcription factor erg; ets DNA-binding !1domain homology; ets RII regulatory region homology KEYWORDS alternative splicing; DNA binding; nucleus; proto-oncogene; !1transcription factor; transforming protein FEATURE !$1-231,256-486 #product transforming proitein erg-2 #status !8predicted #label EG2\ !$100-231,256-486 #product transforming protein erg-1 #status predicted !8#label EG1\ !$126-200 #domain ets RII regulatory region homology #label !8ETR\ !$320-398 #domain ets DNA-binding domain homology #label ETS SUMMARY #length 486 #molecular-weight 54608 #checksum 9577 SEQUENCE /// ENTRY S60754 #type complete TITLE transcription factor erg - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 27-Apr-1996 #sequence_revision 23-May-1997 #text_change 16-Jul-1999 ACCESSIONS S60754 REFERENCE S60754 !$#authors Dhordain, P.; Dewitte, F.; Desbiens, X.; Stehelin, D.; !1Duterque-Coquillaud, M. !$#journal Mech. Dev. (1995) 50:17-28 !$#title Mesodermal expression of the chicken erg gene associated !1with precartilaginous condensation and cartilage !1differentiation. !$#cross-references MUID:95329425; PMID:7605748 !$#accession S60754 !'##status preliminary !'##molecule_type mRNA !'##residues 1-478 ##label DHO !'##cross-references EMBL:X77159; NID:g790439; PIDN:CAA54404.1; !1PID:g790440 GENETICS !$#gene erg CLASSIFICATION #superfamily transcription factor erg; ets DNA-binding !1domain homology; ets RII regulatory region homology KEYWORDS DNA binding; phosphoprotein; proto-oncogene; transcription !1factor; transforming protein FEATURE !$119-193 #domain ets RII regulatory region homology #label !8ETR\ !$312-390 #domain ets DNA-binding domain homology #label ETS SUMMARY #length 478 #molecular-weight 53913 #checksum 547 SEQUENCE /// ENTRY I37565 #type complete TITLE transforming protein fli, long splice form - human ALTERNATE_NAMES Friend leukemia integration protein 1; transcription factor ERGB ORGANISM #formal_name Homo sapiens #common_name man DATE 04-Oct-1996 #sequence_revision 30-May-1997 #text_change 03-Mar-2000 ACCESSIONS I37565; S29843; S35506; A49000; A49015; I54170 REFERENCE S28257 !$#authors Delattre, O.; Zucman, J.; Plougastel, B.; Desmaze, C.; !1Melot, T.; Peter, M.; Kovar, H.; Joubert, I.; de Jong, P.; !1Rouleau, G.; Aurias, A.; Thomas, G. !$#journal Nature (1992) 359:162-165 !$#title Gene fusion with an ETS DNA-binding domain caused by !1chromosome translocation in human tumours. !$#cross-references MUID:92396239; PMID:1522903 !$#accession I37565 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-452 ##label DEL !'##cross-references EMBL:X67001; NID:g32529; PIDN:CAA47399.1; !1PID:g32530 REFERENCE S29843 !$#authors Hromas, R.; May, W.; Denny, C.; Raskind, W.; Moore, J.; !1Maki, R.A.; Beck, E.; Klemsz, M.J. !$#journal Biochim. Biophys. Acta (1993) 1172:155-158 !$#title Human FLI-1 localizes to chromosome 11Q24 and has an !1aberrant transcript in neuroepithelioma. !$#cross-references MUID:93176799; PMID:8439553 !$#accession S29843 !'##molecule_type mRNA !'##residues 1-68,'V',70-129,'A',131-132,'V',134-322,'Q',324-425,427-452 !1##label HRO1 !'##cross-references EMBL:M93255; NID:g182659 !'##note the authors translated the codon GTG for residue 69 as Glu REFERENCE S35506 !$#authors Hromas, R.A.; May, W.; Denny, C.; Raskind, W.; Moore, J.; !1Maki, R.A.; Beck, E.; Klemsz, M.J. !$#submission submitted to the EMBL Data Library, May 1993 !$#description Human FLI-1, an ETS oncogene family member preferentially !1expressed in hematopoetic cells, is a sequence-specific DNA !1binding protein. !$#accession S35506 !'##molecule_type mRNA !'##residues 1-68,'V',70-76,78-129,'A',131-132,'V',134-322,'Q',324-425, !1427-452 ##label HRO2 !'##cross-references EMBL:M93255; NID:g182659; PIDN:AAA58479.1; !1PID:g182660 REFERENCE A49000 !$#authors Prasad, D.D.; Rao, V.N.; Reddy, E.S. !$#journal Cancer Res. (1992) 52:5833-5837 !$#title Structure and expression of human Fli-1 gene. !$#cross-references MUID:93007976; PMID:1394211 !$#accession A49000 !'##status preliminary !'##molecule_type mRNA !'##residues 1-322,'Q',324-452 ##label PRA !'##cross-references GB:S45205; NID:g257353; PIDN:AAB23637.1; !1PID:g257354 !'##note sequence extracted from NCBI backbone (NCBIN:115336, !1NCBIP:115337) REFERENCE A49015 !$#authors Watson, D.K.; Smyth, F.E.; Thompson, D.M.; Cheng, J.Q.; !1Testa, J.R.; Papas, T.S.; Seth, A. !$#journal Cell Growth Differ. (1992) 3:705-713 !$#title The ERGB/Fli-1 gene: isolation and characterization of a new !1member of the family of human ETS transcription factors. !$#cross-references MUID:93075640; PMID:1445800 !$#accession A49015 !'##status preliminary !'##molecule_type mRNA !'##residues 1-390,'Q',392-425,427-452 ##label WAT !'##cross-references GB:M98833; NID:g182188; PIDN:AAA35812.1; !1PID:g182189 !'##note sequence extracted from NCBI backbone (NCBIN:119390, !1NCBIP:119392) REFERENCE I54170 !$#authors Baud, V.; Lipinski, M.; Rassart, E.; Poliquin, L.; Bergeron, !1D. !$#journal Genomics (1991) 11:223-224 !$#title The human homolog of the mouse common viral integration !1region, FLI1, maps to 11q23-q24. !$#cross-references MUID:92112219; PMID:1765382 !$#accession I54170 !'##status preliminary; nucleic acid sequence not shown; translated from !1GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-6 ##label BAU !'##cross-references GB:L47616; NID:g1000863; PIDN:AAA76854.1; !1PID:g1000864 GENETICS !$#gene GDB:FLI1 !'##cross-references GDB:127565; OMIM:193067 !$#map_position 11q24.1-11q24.3 !$#introns 77/3 CLASSIFICATION #superfamily transcription factor erg; ets DNA-binding !1domain homology; ets RII regulatory region homology KEYWORDS alternative splicing; DNA binding; nucleus; proto-oncogene; !1transcription factor; transforming protein FEATURE !$118-192 #domain ets RII regulatory region homology #label !8ETR\ !$283-361 #domain ets DNA-binding domain homology #label ETS SUMMARY #length 452 #molecular-weight 50982 #checksum 389 SEQUENCE /// ENTRY S29844 #type complete TITLE transforming protein fli, short splice form - human ALTERNATE_NAMES Friend leukemia integration protein 1; transcription factor ERGB ORGANISM #formal_name Homo sapiens #common_name man DATE 02-Dec-1993 #sequence_revision 23-May-1997 #text_change 16-Jul-1999 ACCESSIONS S29844 REFERENCE S29843 !$#authors Hromas, R.; May, W.; Denny, C.; Raskind, W.; Moore, J.; !1Maki, R.A.; Beck, E.; Klemsz, M.J. !$#journal Biochim. Biophys. Acta (1993) 1172:155-158 !$#title Human FLI-1 localizes to chromosome 11Q24 and has an !1aberrant transcript in neuroepithelioma. !$#cross-references MUID:93176799; PMID:8439553 !$#accession S29844 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type mRNA !'##residues 1-385 ##label HRO !'##cross-references EMBL:M93255; NID:g18265; PIDN:AAA58480.1; !1PID:g182661 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1May 1992 GENETICS !$#gene GDB:FLI1 !'##cross-references GDB:127565; OMIM:193067 !$#map_position 11q24.1-11q24.3 CLASSIFICATION #superfamily transcription factor erg; ets DNA-binding !1domain homology; ets RII regulatory region homology KEYWORDS alternative splicing; DNA binding; nucleus; proto-oncogene; !1transcription factor; transforming protein FEATURE !$52-126 #domain ets RII regulatory region homology #label !8ETR\ !$217-295 #domain ets DNA-binding domain homology #label ETS SUMMARY #length 385 #molecular-weight 43437 #checksum 4889 SEQUENCE /// ENTRY S17403 #type complete TITLE transforming protein fli - mouse ALTERNATE_NAMES Friend leukemia integration protein 1; transcription factor ERGB ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS S17403 REFERENCE S17403 !$#authors Ben-David, Y.; Giddens, E.B.; Letwin, K.; Bernstein, A. !$#journal Genes Dev. (1991) 5:908-918 !$#title Erythroleukemia induction by Friend murine leukemia virus: !1insertional activation of a new member of the ets gene !1family, Fli-1, closely linked to c-ets-1. !$#cross-references MUID:91257578; PMID:2044959 !$#accession S17403 !'##molecule_type mRNA !'##residues 1-452 ##label BEN !'##cross-references GB:X59421; NID:g50974; PIDN:CAA42055.1; PID:g50975 GENETICS !$#gene Fli CLASSIFICATION #superfamily transcription factor erg; ets DNA-binding !1domain homology; ets RII regulatory region homology KEYWORDS DNA binding; nucleus; proto-oncogene; transcription factor; !1transforming protein FEATURE !$118-192 #domain ets RII regulatory region homology #label !8ETR\ !$283-361 #domain ets DNA-binding domain homology #label ETS SUMMARY #length 452 #molecular-weight 51002 #checksum 8905 SEQUENCE /// ENTRY S49013 #type complete TITLE transforming protein fli - African clawed frog ALTERNATE_NAMES Friend leukemia integration protein 1; transcription factor ERGB ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 07-May-1995 #sequence_revision 23-May-1997 #text_change 16-Jul-1999 ACCESSIONS S49013 REFERENCE S49013 !$#authors Meyer, D.; Wolff, C.M.; Stiegler, P.; Senan, F.; Befort, N.; !1Befort, J.J.; Remy, P. !$#journal Mech. Dev. (1993) 44:109-121 !$#title Xl-fli, the Xenopus homologue of the fli-1 gene, is !1expressed during embryogenesis in a restricted pattern !1evocative of neural crest cell distribution. !$#cross-references MUID:94206844; PMID:8155576 !$#accession S49013 !'##status preliminary !'##molecule_type mRNA !'##residues 1-453 ##label MEY !'##cross-references EMBL:X66979; NID:g505486; PIDN:CAA47389.1; !1PID:g505487 GENETICS !$#gene fli CLASSIFICATION #superfamily transcription factor erg; ets DNA-binding !1domain homology; ets RII regulatory region homology KEYWORDS DNA binding; nucleus; proto-oncogene; transcription factor; !1transforming protein FEATURE !$117-191 #domain ets RII regulatory region homology #label !8ETR\ !$284-362 #domain ets DNA-binding domain homology #label ETS SUMMARY #length 453 #molecular-weight 51015 #checksum 774 SEQUENCE /// ENTRY I38893 #type complete TITLE transcription factor ER81 - human ALTERNATE_NAMES ets translocation variant 1 ORGANISM #formal_name Homo sapiens #common_name man DATE 01-Nov-1996 #sequence_revision 23-May-1997 #text_change 18-Jun-1999 ACCESSIONS I38893; S61541 REFERENCE I38893 !$#authors Jeon, I.S.; Davis, J.N.; Braun, B.S.; Sublett, J.E.; !1Roussel, M.F.; Denny, C.T.; Shapiro, D.N. !$#journal Oncogene (1995) 10:1229-1234 !$#title A variant Ewing's sarcoma translocation (7;22) fuses the EWS !1gene to the ETS gene ETV1. !$#cross-references MUID:95215084; PMID:7700648 !$#accession I38893 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-477 ##label RES !'##cross-references EMBL:U17163; NID:g596005; PIDN:AAA79844.1; !1PID:g596006 REFERENCE S61541 !$#authors Monte, D.; Coutte, L.; Baert, J.L.; Angeli, I.; Stehelin, !1D.; de Launoit, Y. !$#journal Oncogene (1995) 11:771-779 !$#title Molecular characterization of the ets-related human !1transcription factor ER81. !$#cross-references MUID:95380185; PMID:7651741 !$#accession S61541 !'##status preliminary !'##molecule_type mRNA !'##residues 1-38,'V',40-60,'V',80-116,'C',118-126,'K',128-252,254-348, !1'A',350-477 ##label MON !'##cross-references EMBL:X87175; NID:g1045060; PIDN:CAA60642.1; !1PID:g1045061 GENETICS !$#gene GDB:ETV1 !'##cross-references GDB:335229; OMIM:600541 !$#map_position 21q22.3-21q22.3 CLASSIFICATION #superfamily transcription factor ER81; ets DNA-binding !1domain homology KEYWORDS DNA binding; nucleus; transcription factor FEATURE !$337-415 #domain ets DNA-binding domain homology #label ETS SUMMARY #length 477 #molecular-weight 55100 #checksum 3669 SEQUENCE /// ENTRY B46396 #type complete TITLE transcription factor ER81 - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 19-May-1994 #sequence_revision 23-May-1997 #text_change 18-Jun-1999 ACCESSIONS B46396 REFERENCE A46396 !$#authors Brown, T.A.; McKnight, S.L. !$#journal Genes Dev. (1992) 6:2502-2512 !$#title Specificities of protein-protein and protein-DNA interaction !1of GABPalpha and two newly defined ets-related proteins. !$#cross-references MUID:94040714; PMID:1340465 !$#accession B46396 !'##molecule_type mRNA !'##residues 1-477 ##label BRO !'##cross-references GB:L10426; NID:g193195; PIDN:AAA20075.1; !1PID:g515964 CLASSIFICATION #superfamily transcription factor ER81; ets DNA-binding !1domain homology KEYWORDS DNA binding; nucleus; transcription factor FEATURE !$337-415 #domain ets DNA-binding domain homology #label ETS SUMMARY #length 477 #molecular-weight 55040 #checksum 2601 SEQUENCE /// ENTRY S43692 #type complete TITLE transcription factor erm - human ALTERNATE_NAMES ets variant gene 5; ets-related molecule ORGANISM #formal_name Homo sapiens #common_name man DATE 13-Jan-1995 #sequence_revision 23-May-1997 #text_change 18-Jun-1999 ACCESSIONS S43692 REFERENCE S43692 !$#authors Monte, D.; Baert, J.L.; Defossez, P.A.; de Launoit, Y.; !1Stehelin, D. !$#journal Oncogene (1994) 9:1397-1406 !$#title Molecular cloning and characterization of human ERM, a new !1member of the Ets family closely related to mouse PEA3 and !1ER81 transcription factors. !$#cross-references MUID:94203669; PMID:8152800 !$#accession S43692 !'##status preliminary !'##molecule_type mRNA !'##residues 1-510 ##label MON !'##cross-references EMBL:X76184; NID:g479166; PIDN:CAA53778.1; !1PID:g479167 GENETICS !$#gene GDB:ETV5; ERM; ETV2L1 !'##cross-references GDB:361087; OMIM:601600 !$#map_position 3q27-3q29 CLASSIFICATION #superfamily transcription factor ER81; ets DNA-binding !1domain homology KEYWORDS DNA binding; nucleus; transcription factor FEATURE !$370-448 #domain ets DNA-binding domain homology #label ETS SUMMARY #length 510 #molecular-weight 57838 #checksum 3278 SEQUENCE /// ENTRY S35534 #type fragment TITLE adenovirus E1A enhancer-binding protein E1AF - human (fragment) ALTERNATE_NAMES ets translocation variant 4 ORGANISM #formal_name Homo sapiens #common_name man DATE 09-Dec-1993 #sequence_revision 23-May-1997 #text_change 16-Jun-2000 ACCESSIONS S35534 REFERENCE S35534 !$#authors Higashino, F.; Yoshida, K.; Fujinaga, Y.; Kamio, K.; !1Fujinaga, K. !$#journal Nucleic Acids Res. (1993) 21:547-553 !$#title Isolation of a cDNA encoding the adenovirus E1A enhancer !1binding protein: a new human member of the ets oncogene !1family. !$#cross-references MUID:93181246; PMID:8441666 !$#accession S35534 !'##status preliminary !'##molecule_type mRNA !'##residues 1-462 ##label HIG !'##cross-references GB:D12765; NID:g219610; PIDN:BAA02234.1; !1PID:g219611 GENETICS !$#gene GDB:ETV4; E1A-F !'##cross-references GDB:512230; OMIM:600711 !$#map_position 17q21-17q21 CLASSIFICATION #superfamily transcription factor ER81; ets DNA-binding !1domain homology KEYWORDS DNA binding; nucleus; transcription factor FEATURE !$321-399 #domain ets DNA-binding domain homology #label ETS SUMMARY #length 462 #checksum 1665 SEQUENCE /// ENTRY S24061 #type complete TITLE transcription factor PEA3 - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 19-Feb-1994 #sequence_revision 23-May-1997 #text_change 18-Jun-1999 ACCESSIONS S24061 REFERENCE S24061 !$#authors Xin, J.H.; Cowie, A.; Lachance, P.; Hassell, J.A. !$#journal Genes Dev. (1992) 6:481-496 !$#title Molecular cloning and characterization of PEA3, a new member !1of the Ets oncogene family that is differentially expressed !1in mouse embryonic cells. !$#cross-references MUID:92192459; PMID:1547944 !$#accession S24061 !'##status preliminary !'##molecule_type mRNA !'##residues 1-555 ##label XIN !'##cross-references EMBL:X63190; NID:g53627; PIDN:CAA44872.1; !1PID:g53628 CLASSIFICATION #superfamily transcription factor ER81; ets DNA-binding !1domain homology KEYWORDS DNA binding; nucleus; transcription factor FEATURE !$414-492 #domain ets DNA-binding domain homology #label ETS SUMMARY #length 555 #molecular-weight 60846 #checksum 535 SEQUENCE /// ENTRY S33167 #type complete TITLE gene pointed protein splice form 1 - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES ETS-like protein ORGANISM #formal_name Drosophila melanogaster DATE 13-Jan-1995 #sequence_revision 30-May-1997 #text_change 15-Oct-1999 ACCESSIONS S33167; S28819; S28818 REFERENCE S33167 !$#authors Klaembt, C. !$#journal Development (1993) 117:163-176 !$#title The Drosophila gene pointed encodes two ETS-like proteins !1which are involved in the development of the midline glial !1cells. !$#cross-references MUID:94038653; PMID:8223245 !$#accession S33167 !'##status preliminary !'##molecule_type mRNA !'##residues 1-623 ##label KLA !'##cross-references EMBL:X69166; NID:g288079; PIDN:CAA48916.1; !1PID:g288080 REFERENCE S28819 !$#authors Chen, T.; Bunting, M.; Karim, F.D.; Thummel, C.S. !$#journal Dev. Biol. (1992) 151:176-191 !$#title Isolation and characterization of five Drosophila genes that !1encode an ets-related DNA binding domain. !$#cross-references MUID:92249640; PMID:1577186 !$#accession S28819 !'##molecule_type mRNA !'##residues 456-613 ##label CHE !'##cross-references EMBL:M88472; NID:g157191; PIDN:AAC34200.1; !1PID:g157192 REFERENCE S28818 !$#authors Pribyl, L.J.; Watson, D.K.; McWilliams, M.J.; Ascione, R.; !1Papas, T.S. !$#journal Dev. Biol. (1988) 127:45-53 !$#title The Drosophila ets-2 gene: molecular structure, chromosomal !1localization, and developmental expression. !$#cross-references MUID:88196618; PMID:2834248 !$#accession S28818 !'##status preliminary !'##molecule_type DNA !'##residues 445-466,'R',468-603 ##label PRI !'##cross-references EMBL:M20408; NID:g157384; PIDN:AAA28521.1; !1PID:g157385 !'##note the authors translated the codon AGA for residue 467 as Gln GENETICS !$#gene FlyBase:pnt !'##cross-references FlyBase:FBgn0003118 !$#introns 550/3 CLASSIFICATION #superfamily pointed protein, splice form 1; ets DNA-binding !1domain homology KEYWORDS alternative splicing; DNA binding; nucleus; transcription !1factor FEATURE !$517-595 #domain ets DNA-binding domain homology #label ETS SUMMARY #length 623 #molecular-weight 66866 #checksum 3179 SEQUENCE /// ENTRY S33168 #type complete TITLE gene pointed protein splice form 2 - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES pointed-P2 protein; transforming protein D-ets-2 ORGANISM #formal_name Drosophila melanogaster DATE 13-Jan-1995 #sequence_revision 30-May-1997 #text_change 15-Oct-1999 ACCESSIONS S33168; S28819; S28818 REFERENCE S33167 !$#authors Klaembt, C. !$#journal Development (1993) 117:163-176 !$#title The Drosophila gene pointed encodes two ETS-like proteins !1which are involved in the development of the midline glial !1cells. !$#cross-references MUID:94038653; PMID:8223245 !$#accession S33168 !'##status preliminary !'##molecule_type mRNA !'##residues 1-718 ##label KLA !'##cross-references EMBL:X69167; NID:g393375; PIDN:CAA48917.1; !1PID:g393376 REFERENCE S28819 !$#authors Chen, T.; Bunting, M.; Karim, F.D.; Thummel, C.S. !$#journal Dev. Biol. (1992) 151:176-191 !$#title Isolation and characterization of five Drosophila genes that !1encode an ets-related DNA binding domain. !$#cross-references MUID:92249640; PMID:1577186 !$#accession S28819 !'##molecule_type mRNA !'##residues 551-708 ##label CHE !'##cross-references EMBL:M88472; NID:g157191; PIDN:AAC34200.1; !1PID:g157192 REFERENCE S28818 !$#authors Pribyl, L.J.; Watson, D.K.; McWilliams, M.J.; Ascione, R.; !1Papas, T.S. !$#journal Dev. Biol. (1988) 127:45-53 !$#title The Drosophila ets-2 gene: molecular structure, chromosomal !1localization, and developmental expression. !$#cross-references MUID:88196618; PMID:2834248 !$#accession S28818 !'##status preliminary !'##molecule_type DNA !'##residues 540-561,'R',563-698 ##label PRI !'##cross-references EMBL:M20408; NID:g157384; PIDN:AAA28521.1; !1PID:g157385 !'##note the authors translated the codon AGA for residue 562 as Gln GENETICS !$#gene FlyBase:pnt !'##cross-references FlyBase:FBgn0003118 !$#introns 645/3 CLASSIFICATION #superfamily pointed protein, splice form 2; ets DNA-binding !1domain homology; ets RII regulatory region homology KEYWORDS alternative splicing; DNA binding; nucleus; transcription !1factor FEATURE !$170-244 #domain ets RII regulatory region homology #label !8ETR\ !$612-690 #domain ets DNA-binding domain homology #label ETS SUMMARY #length 718 #molecular-weight 77727 #checksum 6266 SEQUENCE /// ENTRY S37616 #type complete TITLE transcription factor elg - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES transcription factor ets-97D ORGANISM #formal_name Drosophila melanogaster DATE 13-Jan-1995 #sequence_revision 23-May-1997 #text_change 16-Jul-1999 ACCESSIONS S37616; S28822 REFERENCE S37616 !$#authors The, S.M.; Xie, X.; Smyth, F.; Papas, T.S.; Watson, D.K.; !1Schulz, R.A. !$#journal Oncogene (1992) 7:2471-2478 !$#title Molecular characterization and structural organization of !1D-elg, an ets proto-oncogene-related gene of Drosophila. !$#cross-references MUID:93096481; PMID:1461651 !$#accession S37616 !'##status preliminary !'##molecule_type DNA !'##residues 1-464 ##label THE !'##cross-references EMBL:X68259; NID:g7942; PIDN:CAA48327.1; PID:g7943 REFERENCE S28819 !$#authors Chen, T.; Bunting, M.; Karim, F.D.; Thummel, C.S. !$#journal Dev. Biol. (1992) 151:176-191 !$#title Isolation and characterization of five Drosophila genes that !1encode an ets-related DNA binding domain. !$#cross-references MUID:92249640; PMID:1577186 !$#accession S28822 !'##molecule_type mRNA !'##residues 298-449 ##label CHE !'##cross-references EMBL:M88471; NID:g157189; PIDN:AAC34199.1; !1PID:g552088 !'##note the authors translated the codon AGC for residue 302 as Thr GENETICS !$#gene FlyBase:Ets97D !'##cross-references FlyBase:FBgn0004510 !$#introns 22/1; 60/2; 83/3; 322/1 CLASSIFICATION #superfamily transcription factor elg; ets DNA-binding !1domain homology; ets RII regulatory region homology KEYWORDS DNA binding; nucleus; transcription factor FEATURE !$190-263 #domain ets RII regulatory region homology #label !8ETR\ !$348-426 #domain ets DNA-binding domain homology #label ETS SUMMARY #length 464 #molecular-weight 52658 #checksum 2714 SEQUENCE /// ENTRY A48146 #type complete TITLE GA-binding protein alpha chain - human ALTERNATE_NAMES GABPA; nuclear respiratory factor-2 alpha chain; transcription factor E4TF1 60K chain ORGANISM #formal_name Homo sapiens #common_name man DATE 21-Jan-1994 #sequence_revision 23-May-1997 #text_change 16-Jul-1999 ACCESSIONS A48146; A46303; A55903 REFERENCE A48146 !$#authors Watanabe, H.; Sawada, J.; Yano, K.; Yamaguchi, K.; Goto, M.; !1Handa, H. !$#journal Mol. Cell. Biol. (1993) 13:1385-1391 !$#title cDNA cloning of transcription factor E4TF1 subunits with Ets !1and notch motifs. !$#cross-references MUID:93180783; PMID:8441384 !$#accession A48146 !'##status not compared with conceptual translation !'##molecule_type mRNA; protein !'##residues 1-454 ##label WAT !'##note sequence extracted from NCBI backbone (NCBIP:125762) !'##note parts of this sequence were determined by protein sequencing REFERENCE A46303 !$#authors Virbasius, J.V.; Virbasius, C.A.; Scarpulla, R.C. !$#journal Genes Dev. (1993) 7:380-392 !$#title Identity of GABP with NRF-2, a multisubunit activator of !1cytochrome oxidase expression, reveals a cellular role for !1an ETS domain activator of viral promoters. !$#cross-references MUID:93194058; PMID:8383622 !$#accession A46303 !'##molecule_type protein !'##residues 237-248;429-448 ##label VIR REFERENCE A55903 !$#authors Cardot, P.; Pastier, D.; Lacorte, J.M.; Mangeney, M.; !1Zannis, V.I.; Chambaz, J. !$#journal Biochemistry (1994) 33:12139-12148 !$#title Purification and characterization of nuclear factors binding !1to the negative regulatory element D of human apolipoprotein !1A-II promoter: a negative regulatory effect is reversed by !1GABP, an ets-related protein. !$#cross-references MUID:95001929; PMID:7918435 !$#accession A55903 !'##molecule_type protein !'##residues 26-34,'A',36,'X',38,'X',40-46;151-165;167-174;350-359 !1##label CAR GENETICS !$#gene GDB:GABPA; E4TF1-60; E4TF1A !'##cross-references GDB:138476; OMIM:600609 !$#map_position 21q21-21q22.1 COMPLEX GA-binding protein is a heterotetramer of two alpha and two !1beta-type chains. FUNCTION !$#description a transcription factor that binds (via the alpha chain) to !1GA-rich promoters !$#pathway known to promote transcription of apolipoprotein A-II, !1cytochrom c oxidase chain IV, ATPase beta chain, and !1adenovirus E4 genes CLASSIFICATION #superfamily transcription factor elg; ets DNA-binding !1domain homology; ets RII regulatory region homology KEYWORDS DNA binding; nucleus; transcription factor FEATURE !$174-245 #domain ets RII regulatory region homology #label !8ETR\ !$322-400 #domain ets DNA-binding domain homology #label ETS SUMMARY #length 454 #molecular-weight 51311 #checksum 3079 SEQUENCE /// ENTRY A40858 #type complete TITLE GA-binding protein alpha chain - mouse ALTERNATE_NAMES GABPA; nuclear respiratory factor-2 alpha chain; transcription factor E4TF1 60K chain ORGANISM #formal_name Mus musculus #common_name house mouse DATE 28-Feb-1992 #sequence_revision 23-May-1997 #text_change 16-Jul-1999 ACCESSIONS A40858 REFERENCE A40858 !$#authors LaMarco, K.; Thompson, C.C.; Byers, B.P.; Walton, E.M.; !1McKnight, S.L. !$#journal Science (1991) 253:789-792 !$#title Identification of ets- and notch-related subunits in GA !1binding protein. !$#cross-references MUID:91343912; PMID:1876836 !$#accession A40858 !'##molecule_type mRNA; protein !'##residues 1-454 ##label LAM !'##cross-references GB:M74515; NID:g193382; PIDN:AAA53030.1; !1PID:g193383 !'##note parts of this sequence were determined by protein sequencing GENETICS !$#gene Gabpa !$#map_position 16 47.0 COMPLEX GA-binding protein is a heterotetramer of two alpha and two !1beta-type chains. FUNCTION !$#description a transcription factor that binds (via the alpha chain) to !1GA-rich promoters !$#pathway known to promote transcription of apolipoprotein A-II, !1cytochrom c oxidase chain IV, ATPase beta chain, and !1adenovirus E4 genes CLASSIFICATION #superfamily transcription factor elg; ets DNA-binding !1domain homology; ets RII regulatory region homology KEYWORDS DNA binding; nucleus; transcription factor FEATURE !$174-245 #domain ets RII regulatory region homology #label !8ETR\ !$322-400 #domain ets DNA-binding domain homology #label ETS SUMMARY #length 454 #molecular-weight 51363 #checksum 1760 SEQUENCE /// ENTRY TVHUEK #type complete TITLE transforming protein elk-1 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 18-Jun-1999 ACCESSIONS A41354; S54721 REFERENCE A41354 !$#authors Rao, V.N.; Huebner, K.; Isobe, M.; ar-Rushdi, A.; Croce, !1C.M.; Reddy, E.S.P. !$#journal Science (1989) 244:66-70 !$#title elk, tissue-specific ets-related genes on chromosomes X and !114 near translocation breakpoints. !$#cross-references MUID:89203250; PMID:2539641 !$#accession A41354 !'##molecule_type mRNA !'##residues 1-428 ##label RAO !'##cross-references GB:M25269; NID:g538208; PIDN:AAA52384.1; !1PID:g538209 REFERENCE S54721 !$#authors Gille, H.; Kortenjann, M.; Thomae, O.; Moomaw, C.; !1Slaughter, C.; Cobb, M.H.; Shaw, P.E. !$#journal EMBO J. (1995) 14:951-962 !$#title ERK phosphorylation potentiates Elk-1-mediated ternary !1complex formation and transactivation. !$#cross-references MUID:95196758; PMID:7889942 !$#accession S54721 !'##status preliminary !'##molecule_type protein !'##residues 318-328,'XX',331;336-364;380-388,'X',390-392,'X',394-400, !1'XX',403-405,'X',407-408 ##label GIL GENETICS !$#gene GDB:ELK1 !'##cross-references GDB:119867; OMIM:311040 !$#map_position Xp11.2-Xp11.2 CLASSIFICATION #superfamily elk-1 transforming protein; ets DNA-binding !1domain homology KEYWORDS DNA binding; oncogene; transforming protein FEATURE !$7-86 #domain ets DNA-binding domain homology #label ETS SUMMARY #length 428 #molecular-weight 44915 #checksum 5428 SEQUENCE /// ENTRY TVHUM #type complete TITLE transforming protein C-myc - human ALTERNATE_NAMES p64 myc oncogene ORGANISM #formal_name Homo sapiens #common_name man DATE 14-Nov-1983 #sequence_revision 31-Mar-1992 #text_change 24-Nov-1999 ACCESSIONS A01349; A26245; A26246; A21061; I67315; I53224; I61947; !1I38052; I57605; I37244; I38075; I57633 REFERENCE A01349 !$#authors Watson, D.K.; Psallidopoulos, M.C.; Samuel, K.P.; !1Dalla-Favera, R.; Papas, T.S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:3642-3645 !$#title Nucleotide sequence analysis of human c-myc locus, chicken !1homologue, and myelocytomatosis virus MC29 transforming gene !1reveals a highly conserved gene product. !$#cross-references MUID:83221652; PMID:6304729 !$#accession A01349 !'##molecule_type DNA !'##residues 1-439 ##label WATS !'##cross-references GB:K01906; NID:g188937; PIDN:AAA59881.1; !1PID:g386968 REFERENCE A26245 !$#authors Colby, W.W.; Chen, E.Y.; Smith, D.H.; Levinson, A.D. !$#journal Nature (1983) 301:722-725 !$#title Identification and nucleotide sequence of a human locus !1homologous to the v-myc oncogene of avian myelocytomatosis !1virus MC29. !$#cross-references MUID:83141777; PMID:6298632 !$#accession A26245 !'##molecule_type DNA !'##residues 1-439 ##label COL !'##cross-references GB:J00120; GB:K01908; GB:M23541; GB:V00501; !1GB:X00364; NID:g515632; PIDN:AAA20042.1; PID:g386965 REFERENCE A26246 !$#authors Watt, R.; Stanton, L.W.; Marcu, K.B.; Gallo, R.C.; Croce, !1C.M.; Rovera, G. !$#journal Nature (1983) 303:725-728 !$#title Nucleotide sequence of cloned cDNA of human c-myc oncogene. !$#cross-references MUID:83219310; PMID:6304538 !$#accession A26246 !'##molecule_type mRNA !'##residues 1-439 ##label WATT !'##cross-references GB:V00568; NID:g34815; PIDN:CAA23831.1; PID:g34816 REFERENCE A21061 !$#authors Battey, J.; Moulding, C.; Taub, R.; Murphy, W.; Stewart, T.; !1Potter, H.; Lenoir, G.; Leder, P. !$#journal Cell (1983) 34:779-787 !$#title The human c-myc oncogene: structural consequences of !1translocation into the IgH locus in Burkitt lymphoma. !$#cross-references MUID:84026482; PMID:6414718 !$#accession A21061 !'##molecule_type DNA !'##residues 1-439 ##label BAT !'##cross-references GB:K00535; NID:g188917; PIDN:AAA59880.1; !1PID:g188919 REFERENCE I53224 !$#authors Gazin, C.; De Dinechin, S.D.; Hampe, A.; Masson, J. !$#journal EMBO J. (1984) 3:383-387 !$#title Nucleotide sequence of the human c-myc locus: provocative !1open reading frame within the first exon. !$#cross-references MUID:84182501; PMID:6714223 !$#accession I67315 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-439 ##label GAZ1 !'##cross-references GB:D10493; NID:g219932; PIDN:BAA01375.1; !1PID:g219934 !$#accession I53224 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 'LNFFREVENQQPPAT',1-439 ##label GAZ2 !'##cross-references GB:D10493; NID:g219932; PID:g219933 REFERENCE I38052 !$#authors Bernard, O.; Cory, S.; Gerondakis, S.; Webb, E.; Adams, J.M. !$#journal EMBO J. (1983) 2:2375-2383 !$#title Sequence of the murine and human cellular myc oncogenes and !1two modes of myc transcription resulting from chromosome !1translocation in B lymphoid tumours. !$#cross-references MUID:84131953; PMID:6321164 !$#accession I61947 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-439 ##label BER1 !'##cross-references GB:K01904; NID:g188931; PIDN:AAA36341.1; !1PID:g386967 !$#accession I38052 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-252 ##label BER2 !'##cross-references EMBL:X00196; NID:g34822; PIDN:CAA25015.1; !1PID:g34823 REFERENCE I57605 !$#authors Bentley, D.L.; Groudine, M. !$#journal Mol. Cell. Biol. (1986) 6:3481-3489 !$#title Novel promoter upstream of the human c-myc gene and !1regulation of c-myc expression in B-cell lymphomas. !$#cross-references MUID:87089682; PMID:3540591 !$#accession I57605 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-170 ##label BEN !'##cross-references GB:M13929; NID:g188963; PIDN:AAA88092.1; !1PID:g188964 REFERENCE I37244 !$#authors Rabbitts, T.H.; Forster, A.; Hamlyn, P.; Baer, R. !$#journal Nature (1984) 309:592-597 !$#title Effect of somatic mutation within translocated c-myc genes !1in Burkitt's lymphoma. !$#cross-references MUID:84219769; PMID:6547209 !$#accession I37244 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-61,'P',63-252 ##label RAB !'##cross-references EMBL:X00676; NID:g29996; PIDN:CAA25288.1; !1PID:g29997 REFERENCE I38075 !$#authors Hayday, A.C.; Gillies, S.D.; Saito, H.; Wood, C.; Wiman, K.; !1Hayward, W.S.; Tonegawa, S. !$#journal Nature (1984) 307:334-340 !$#title Activation of a translocated human c-myc gene by an enhancer !1in the immunoglobulin heavy-chain locus. !$#cross-references MUID:84117466; PMID:6420706 !$#accession I38075 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-7 ##label HAY !'##cross-references EMBL:X00344; NID:g35146; PIDN:CAA25095.1; !1PID:g580340 REFERENCE I57633 !$#authors Hollis, G.F.; Gazdar, A.F.; Bertness, V.L.; Kirsch, I.R. !$#journal Mol. Cell. Biol. (1988) 8:124-129 !$#title Complex translocation disrupts c-myc regulation in a human !1plasma cell myeloma. !$#cross-references MUID:88094377; PMID:3275865 !$#accession I57633 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 437-439 ##label HOL !'##cross-references GB:M19724; NID:g190971 !'##note this translation is not annotated in GenBank entry HUMRCMYC3, !1release 112.0 GENETICS !$#gene GDB:MYC !'##cross-references GDB:120208; OMIM:190080 !$#map_position 8q24.12-8q24.13 !$#introns 253/1 CLASSIFICATION #superfamily myc transforming protein; myc transforming !1protein homology KEYWORDS DNA binding; glycoprotein; leucine zipper; transcription !1regulation; transforming protein FEATURE !$14-437 #domain myc transforming protein homology #label MYC\ !$406-434 #region leucine zipper motif\ !$58 #binding_site carbohydrate (Thr) (covalent) #status !8predicted SUMMARY #length 439 #molecular-weight 48804 #checksum 7695 SEQUENCE /// ENTRY TVCTMC #type complete TITLE transforming protein myc - cat ORGANISM #formal_name Felis silvestris catus #common_name domestic cat DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 28-Feb-1997 ACCESSIONS A24295 REFERENCE A24295 !$#authors Stewart, M.A.; Forrest, D.; McFarlane, R.; Onions, D.; !1Wilkie, N.; Neil, J.C. !$#journal Virology (1986) 154:121-134 !$#title Conservation of the c-myc coding sequence in transduced !1feline v-myc genes. !$#cross-references MUID:86317706; PMID:3018999 !$#accession A24295 !'##molecule_type DNA !'##residues 1-439 ##label STE GENETICS !$#gene myc !$#introns 253/1 CLASSIFICATION #superfamily myc transforming protein; myc transforming !1protein homology KEYWORDS DNA binding; leucine zipper; transcription regulation; !1transforming protein FEATURE !$14-437 #domain myc transforming protein homology #label MYC\ !$406-434 #region leucine zipper motif SUMMARY #length 439 #molecular-weight 48535 #checksum 2819 SEQUENCE /// ENTRY TVMVFT #type complete TITLE gag-myc polyprotein - feline leukemia virus (provirus) CONTAINS fragment of core protein p30; transforming protein myc ORGANISM #formal_name feline leukemia virus DATE 31-Dec-1990 #sequence_revision 01-Dec-2000 #text_change 01-Dec-2000 ACCESSIONS A26268; A31477 REFERENCE A26268 !$#authors Braun, M.J.; Deininger, P.L.; Casey, J.W. !$#journal J. Virol. (1985) 55:177-183 !$#title Nucleotide sequence of a transduced myc gene from a !1defective leukemia provirus. !$#cross-references MUID:85237695; PMID:2989554 !$#accession A26268 !'##molecule_type DNA !'##residues 1-484 ##label BRA !'##cross-references GB:M10973; NID:g323922; PIDN:AAA43059.1; !1PID:g323923 REFERENCE A31477 !$#authors Doggett, D.L.; Drake, A.L.; Hirsch, V.; Rowe, M.E.; !1Stallard, V.; Mullins, J.I. !$#journal J. Virol. (1989) 63:2108-2117 !$#title Structure, origin, and transforming activity of feline !1leukemia virus-myc recombinant provirus FTT. !$#cross-references MUID:89199767; PMID:2539507 !$#accession A31477 !'##molecule_type mRNA !'##residues 46-280,'K',282-403,'D',405-482 ##label DOG COMMENT This protein is synthesized as a gag-myc polyprotein. GENETICS !$#gene gag-myc CLASSIFICATION #superfamily myc transforming protein; myc transforming !1protein homology KEYWORDS core protein; DNA binding; leucine zipper; polyprotein; !1transforming protein FEATURE !$59-482 #domain myc transforming protein homology #label MYC\ !$451-479 #region leucine zipper motif SUMMARY #length 484 #molecular-weight 53406 #checksum 1243 SEQUENCE /// ENTRY TVMS #type complete TITLE transforming protein myc - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 18-Apr-1984 #sequence_revision 28-Aug-1985 #text_change 18-Jun-1999 ACCESSIONS A93337; A93314; A01351 REFERENCE A93337 !$#authors Stanton, L.W.; Fahrlander, P.D.; Tesser, P.M.; Marcu, K.B. !$#journal Nature (1984) 310:423-425 !$#title Nucleotide sequence comparison of normal and translocated !1murine c-myc genes. !$#cross-references MUID:84270712; PMID:6462227 !$#accession A93337 !'##molecule_type mRNA !'##residues 1-439 ##label STA !'##cross-references GB:X01023; NID:g50467; PIDN:CAA25508.1; PID:g50468 REFERENCE A93314 !$#authors Neuberger, M.S.; Calabi, F. !$#journal Nature (1983) 305:240-243 !$#title Reciprocal chromosome translocation between c-myc and !1immunoglobulin gamma2b genes. !$#cross-references MUID:83297726; PMID:6412145 !$#accession A93314 !'##molecule_type DNA !'##residues 1-38,'D',40-252 ##label NEU GENETICS !$#gene myc CLASSIFICATION #superfamily myc transforming protein; myc transforming !1protein homology KEYWORDS DNA binding; leucine zipper; proto-oncogene; transcription !1regulation FEATURE !$14-437 #domain myc transforming protein homology #label MYC\ !$406-434 #region leucine zipper motif SUMMARY #length 439 #molecular-weight 48971 #checksum 7500 SEQUENCE /// ENTRY TVRTMC #type complete TITLE transforming protein myc - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 21-Jul-2000 ACCESSIONS A26801 REFERENCE A26801 !$#authors Hayashi, K.; Makino, R.; Kawamura, H.; Arisawa, A.; Yoneda, !1K. !$#journal Nucleic Acids Res. (1987) 15:6419-6436 !$#title Characterization of rat c-myc and adjacent regions. !$#cross-references MUID:87316910; PMID:3306601 !$#accession A26801 !'##molecule_type DNA !'##residues 1-439 ##label HAY !'##cross-references GB:Y00396; NID:g55967; PIDN:CAA68459.2; !1PID:g5327227 GENETICS !$#gene myc CLASSIFICATION #superfamily myc transforming protein; myc transforming !1protein homology KEYWORDS DNA binding; leucine zipper; transcription regulation; !1transforming protein FEATURE !$14-437 #domain myc transforming protein homology #label MYC\ !$406-434 #region leucine zipper motif SUMMARY #length 439 #molecular-weight 48898 #checksum 7249 SEQUENCE /// ENTRY FOCH #type complete TITLE transforming protein myc - chicken ALTERNATE_NAMES c-myc ORGANISM #formal_name Gallus gallus #common_name chicken DATE 18-Apr-1984 #sequence_revision 28-Aug-1985 #text_change 18-Jun-1999 ACCESSIONS A93944; A93998; I50205; A01352 REFERENCE A93944 !$#authors Watson, D.K.; Reddy, E.P.; Duesberg, P.H.; Papas, T.S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:2146-2150 !$#title Nucleotide sequence analysis of the chicken c-myc gene !1reveals homologous and unique coding regions by comparison !1with the transforming gene of avian myelocytomatosis virus !1MC29, deltagag-myc. !$#cross-references MUID:83169838; PMID:6300896 !$#accession A93944 !'##molecule_type DNA !'##residues 1-416 ##label WAT !'##cross-references GB:J00889; NID:g212354; PIDN:AAA48963.1; !1PID:g212355 REFERENCE A93998 !$#authors Shih, C.K.; Linial, M.; Goodenow, M.M.; Hayward, W.S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:4697-4701 !$#title Nucleotide sequence 5' of the chicken cc-myc coding region: !1localization of a noncoding exon that is absent from myc !1transcripts in most avian leukosis virus-induced lymphomas. !$#cross-references MUID:84272700; PMID:6087343 !$#accession A93998 !'##molecule_type DNA !'##residues 1-44 ##label SHI REFERENCE I50205 !$#authors Hahn, M.; Hayward, W. !$#journal Mol. Cell. Biol. (1988) 8:2659-2662 !$#title Absence of missense mutations in activated c-myc genes in !1avian leukosis virus-induced B-cell lymphomas. !$#cross-references MUID:88302180; PMID:2841585 !$#accession I50205 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-416 ##label HAH !'##cross-references GB:M20006; NID:g211565; PIDN:AAA48700.1; !1PID:g211566 GENETICS !$#gene myc !$#introns 230/1 CLASSIFICATION #superfamily myc transforming protein; myc transforming !1protein homology KEYWORDS DNA binding; leucine zipper; proto-oncogene; transcription !1regulation; transforming protein FEATURE !$14-414 #domain myc transforming protein homology #label MYC\ !$383-411 #region leucine zipper motif SUMMARY #length 416 #molecular-weight 46040 #checksum 1702 SEQUENCE /// ENTRY TVFVAC #type complete TITLE transforming protein myc - avian myelocytomatosis virus OK10 (provirus) ORGANISM #formal_name avian myelocytomatosis virus OK10 #note host Gallus gallus DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 18-Jun-1999 ACCESSIONS A22669 REFERENCE A22669 !$#authors Hayflick, J.; Seeburg, P.H.; Ohlsson, R.; Pfeifer-Ohlsson, !1S.; Watson, D.; Papas, T.; Duesberg, P.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:2718-2722 !$#title Nucleotide sequence of two overlapping myc-related genes in !1avian carcinoma virus ok10 and their relation to the myc !1genes of other viruses and the cell. !$#cross-references MUID:85190568; PMID:2986131 !$#accession A22669 !'##molecule_type genomic RNA !'##residues 1-416 ##label HAY !'##cross-references GB:M11352; NID:g209656; PIDN:AAA42391.1; !1PID:g209657 GENETICS !$#gene myc CLASSIFICATION #superfamily myc transforming protein; myc transforming !1protein homology KEYWORDS DNA binding; leucine zipper; transforming protein FEATURE !$14-414 #domain myc transforming protein homology #label MYC\ !$383-411 #region leucine zipper motif SUMMARY #length 416 #molecular-weight 46040 #checksum 1276 SEQUENCE /// ENTRY TVFV2E #type complete TITLE transforming protein myc - avian myelocytomatosis virus MH2 (provirus) ORGANISM #formal_name avian myelocytomatosis virus MH2 #note host Gallus gallus (chicken) DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 18-Jun-1999 ACCESSIONS A29285; B21137 REFERENCE A29285 !$#authors Patschinsky, T.; Jansen, H.W.; Blocker, H.; Frank, R.; !1Bister, K. !$#journal J. Virol. (1986) 59:341-353 !$#title Structure and transforming function of transduced mutant !1alleles of the chicken c-myc gene. !$#cross-references MUID:86281833; PMID:3016301 !$#accession A29285 !'##molecule_type DNA !'##residues 1-423 ##label PAT !'##cross-references GB:M14008; NID:g209645; PIDN:AAA42389.1; !1PID:g209646 REFERENCE A21137 !$#authors Kan, N.C.; Flordellis, C.S.; Mark, G.E.; Duesberg, P.H.; !1Papas, T.S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:3000-3004 !$#title Nucleotide sequence of avian carcinoma virus MH2: two !1potential onc genes, one related to avian virus MC29 and the !1other related to murine sarcoma virus 3611. !$#cross-references MUID:84221892; PMID:6328485 !$#accession B21137 !'##molecule_type DNA !'##residues 7-44,'S',46-231,'V',233-263,'G',265-423 ##label KAN !'##cross-references GB:K02082; NID:g209649; PIDN:AAB59930.1; !1PID:g209651 GENETICS !$#gene myc CLASSIFICATION #superfamily myc transforming protein; myc transforming !1protein homology KEYWORDS DNA binding; leucine zipper; oncogene; transforming protein FEATURE !$25-421 #domain myc transforming protein homology #label MYC\ !$390-418 #region leucine zipper motif SUMMARY #length 423 #molecular-weight 46188 #checksum 1905 SEQUENCE /// ENTRY TVXLMC #type complete TITLE transforming protein myc I - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 01-Dec-2000 ACCESSIONS A25392; S22574; S12483; S07555; S22547; I51545 REFERENCE A25392 !$#authors King, M.W.; Roberts, J.M.; Eisenman, R.N. !$#journal Mol. Cell. Biol. (1986) 6:4499-4508 !$#title Expression of the c-myc proto-oncogene during development of !1Xenopus laevis. !$#cross-references MUID:87089810; PMID:3540613 !$#accession A25392 !'##molecule_type mRNA !'##residues 1-419 ##label KIN !'##cross-references GB:M14455; NID:g214601; PIDN:AAA49905.1; !1PID:g214602 REFERENCE S22574 !$#authors King, M.W. !$#journal Nucleic Acids Res. (1991) 19:5777-5783 !$#title Developmentally regulated alternative splicing in the !1Xenopus laevis c-Myc gene creates an intron-1 containing !1c-Myc RNA present only in post-midblastula embryos. !$#cross-references MUID:92051330; PMID:1945855 !$#accession S22574 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-227,'G',229-419 ##label KI2 !'##cross-references EMBL:X53717; NID:g64633; PIDN:CAA37753.1; !1PID:g64634 !'##note nucleotide sequence submitted to the EMBL Data Library, June !11990 REFERENCE S12483 !$#authors Mechali, M. !$#submission submitted to the EMBL Data Library, March 1989 !$#accession S12483 !'##molecule_type mRNA !'##residues 1-146,'R',148-419 ##label MEC !'##cross-references EMBL:X14806; NID:g64902; PIDN:CAA32911.1; !1PID:g64903 REFERENCE S07555 !$#authors Vriz, S.; Taylor, M.; Mechali, M. !$#journal EMBO J. (1989) 8:4091-4097 !$#title Differential expression of two Xenopus c-myc proto-oncogenes !1during development. !$#cross-references MUID:90076130; PMID:2686981 !$#accession S07555 !'##molecule_type mRNA !'##residues 1-90,'EFLGGDMVN',91-146,'R',148-419 ##label VRI !'##cross-references EMBL:X14806 !'##note sequence in Fig. 1 repeats amino acids 91-99 and the !1corresponding nucleotides; these amino acids do not appear !1in the sequence presented in Fig. 2 REFERENCE S22545 !$#authors Principaud, E.; Spohr, G. !$#journal Nucleic Acids Res. (1991) 19:3081-3088 !$#title Xenopus laevis c-myc I and II genes: molecular structure and !1developmental expression. !$#cross-references MUID:91279466; PMID:2057364 !$#accession S22547 !'##molecule_type DNA !'##residues 1-83 ##label PRI !'##cross-references EMBL:X56871; NID:g64635; PIDN:CAA40195.1; !1PID:g64636 REFERENCE I51545 !$#authors Taylor, M.V.; Gusse, M.; Evan, G.I.; Dathan, N.; Mechali, M. !$#journal EMBO J. (1986) 5:3563-3570 !$#title Xenopus myc proto-oncogene during development: Expression as !1a stable maternal mRNA uncoupled from cell division. !$#cross-references MUID:87161766; PMID:3549280 !$#accession I51545 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 'R',91-146,'R',148-419 ##label TAY !'##cross-references GB:M26285; NID:g214603; PIDN:AAA49906.1; !1PID:g214604 GENETICS !$#gene myc I; c-myc !$#introns 228/2 CLASSIFICATION #superfamily myc transforming protein; myc transforming !1protein homology KEYWORDS DNA binding; embryo; leucine zipper; nucleus; oocyte; !1proto-oncogene; transcription regulation; transforming !1protein FEATURE !$14-418 #domain myc transforming protein homology #label MYC\ !$387-415 #region leucine zipper motif SUMMARY #length 419 #molecular-weight 47360 #checksum 6303 SEQUENCE /// ENTRY TVTRMC #type fragment TITLE transforming protein myc - rainbow trout (fragment) ORGANISM #formal_name Oncorhynchus mykiss #common_name rainbow trout DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 18-Jun-1999 ACCESSIONS A25272 REFERENCE A25272 !$#authors Van Beneden, R.J.; Watson, D.K.; Chen, T.T.; Lautenberger, !1J.A.; Papas, T.S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:3698-3702 !$#title Cellular myc (c-myc) in fish (rainbow trout): its !1relationship to other vertebrate myc genes and to the !1transforming genes of the MC29 family of viruses. !$#cross-references MUID:86233301; PMID:3520551 !$#accession A25272 !'##molecule_type DNA !'##residues 1-414 ##label VAN !'##cross-references GB:M13048; NID:g213826; PIDN:AAA49604.1; !1PID:g213827 GENETICS !$#gene myc !$#introns 222/1 CLASSIFICATION #superfamily myc transforming protein; myc transforming !1protein homology KEYWORDS DNA binding; leucine zipper; nucleus; transcription !1regulation; transforming protein FEATURE !$11-407 #domain myc transforming protein homology #label MYC\ !$376-404 #region leucine zipper motif SUMMARY #length 414 #checksum 6559 SEQUENCE /// ENTRY TVHUMC #type complete TITLE transforming protein N-myc (version 1) - human ORGANISM #formal_name Homo sapiens #common_name man DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 15-Oct-1999 ACCESSIONS A01355; I59514; S02249 REFERENCE A01355 !$#authors Stanton, L.W.; Schwab, M.; Bishop, J.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:1772-1776 !$#title Nucleotide sequence of the human N-myc gene. !$#cross-references MUID:86149381; PMID:2869488 !$#accession A01355 !'##molecule_type DNA !'##residues 1-456 ##label STA !'##cross-references GB:M13241; NID:g189247; PIDN:AAA36371.1; !1PID:g386983 REFERENCE I59514 !$#authors Slamon, D.J.; Boone, T.C.; Seeger, R.C.; Keith, D.E.; !1Chazin, V.; Lee, H.C.; Souza, L.M. !$#journal Science (1986) 232:768-772 !$#title Identification and characterization of the protein encoded !1by the human N-myc oncogene. !$#cross-references MUID:86179901; PMID:3008339 !$#accession I59514 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 63-456 ##label RES !'##cross-references GB:M13228; NID:g189243; PIDN:AAA36370.1; !1PID:g386982 REFERENCE S00945 !$#authors Ibson, J.M.; Rabbitts, P.H. !$#journal Oncogene (1988) 2:399-402 !$#title Sequence of a germ-line N-myc gene and amplification as a !1mechanism of activation. !$#cross-references MUID:88202932; PMID:2834684 !$#accession S02249 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-354,'V',356-456 ##label IBS !'##cross-references EMBL:Y00664; NID:g35074; PIDN:CAA68678.1; !1PID:g35076 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1988 GENETICS !$#gene GDB:MYCN; NMYC !'##cross-references GDB:120527; OMIM:164840 !$#map_position 2p24.3-2p24.3 !$#introns 256/1 CLASSIFICATION #superfamily myc transforming protein; myc transforming !1protein homology KEYWORDS DNA binding; leucine zipper; nucleus; phosphoprotein; !1proto-oncogene; transforming protein FEATURE !$11-456 #domain myc transforming protein homology #label MYC\ !$425-453 #region leucine zipper motif SUMMARY #length 456 #molecular-weight 48766 #checksum 4352 SEQUENCE /// ENTRY TVHUM2 #type complete TITLE transforming protein N-myc (version 2) - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 18-Jun-1999 ACCESSIONS A25744; B25744; I57628 REFERENCE A25744 !$#authors Kohl, N.E.; Legouy, E.; DePinho, R.A.; Nisen, P.D.; Smith, !1R.K.; Gee, C.E.; Alt, F.W. !$#journal Nature (1986) 319:73-77 !$#title Human N-myc is closely related in organization and !1nucleotide sequence to c-myc. !$#cross-references MUID:86092232; PMID:3510398 !$#accession A25744 !'##molecule_type DNA !'##residues 1-464 ##label KOH !$#accession B25744 !'##molecule_type mRNA !'##residues 1-464 ##label KOH2 REFERENCE I57628 !$#authors Stanton, L.W.; Bishop, J.M. !$#journal Mol. Cell. Biol. (1987) 7:4266-4272 !$#title Alternative processing of RNA transcribed from NMYC. !$#cross-references MUID:88142816; PMID:3437890 !$#accession I57628 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-40 ##label RES !'##cross-references GB:M18090; NID:g188960; PIDN:AAA59885.1; !1PID:g188962 GENETICS !$#gene GDB:MYCN; NMYC !'##cross-references GDB:120527; OMIM:164840 !$#map_position 2p24.3-2p24.3 CLASSIFICATION #superfamily myc transforming protein; myc transforming !1protein homology KEYWORDS DNA binding; nucleus; phosphoprotein; proto-oncogene; !1transforming protein FEATURE !$19-464 #domain myc transforming protein homology #label MYC SUMMARY #length 464 #molecular-weight 49587 #checksum 7857 SEQUENCE /// ENTRY TVMSMC #type complete TITLE transforming protein N-myc (version 1) - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 13-Aug-1986 #sequence_revision 13-Aug-1986 #text_change 18-Jun-1999 ACCESSIONS A01356; I57657 REFERENCE A01356 !$#authors DePinho, R.A.; Legouy, E.; Feldman, L.B.; Kohl, N.E.; !1Yancopoulos, G.D.; Alt, F.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:1827-1831 !$#title Structure and expression of the murine N-myc gene. !$#cross-references MUID:86149392; PMID:3513190 !$#accession A01356 !'##molecule_type DNA !'##residues 1-462 ##label DEP !'##cross-references GB:M12731; NID:g199965; PIDN:AAA39788.1; !1PID:g387488 REFERENCE I57657 !$#authors Setoguchi, M.; Higuchi, Y.; Yoshida, S.; Nasu, N.; Miyazaki, !1Y.; Akizuki, S.; Yamamoto, S. !$#journal Mol. Cell. Biol. (1989) 9:4515-4522 !$#title Insertional activation of N-myc by endogenous Moloney-like !1murine retrovirus sequences in macrophage cell lines derived !1from myeloma cell line-macrophage hybrids. !$#cross-references MUID:90066462; PMID:2555695 !$#accession I57657 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 327-456 ##label RES !'##cross-references GB:M29208; NID:g200085; PIDN:AAA39830.1; !1PID:g387497 GENETICS !$#gene N-myc !$#introns 262/1 CLASSIFICATION #superfamily myc transforming protein; myc transforming !1protein homology KEYWORDS DNA binding; leucine zipper; nucleus; phosphoprotein; !1proto-oncogene; transforming protein FEATURE !$19-462 #domain myc transforming protein homology #label MYC\ !$431-459 #region leucine zipper motif SUMMARY #length 462 #molecular-weight 49460 #checksum 4226 SEQUENCE /// ENTRY TVMSM2 #type complete TITLE transforming protein N-myc (version 2) - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 18-Jun-1999 ACCESSIONS A01357; S02126 REFERENCE A01357 !$#authors Taya, Y.; Mizusawa, S.; Nishimura, S. !$#journal EMBO J. (1986) 5:1215-1219 !$#title Nucleotide sequence of the coding region of the mouse N-myc !1gene. !$#cross-references MUID:86274623; PMID:3015591 !$#accession A01357 !'##molecule_type DNA !'##residues 1-462 ##label TAY !'##cross-references GB:X03919; NID:g53426; PIDN:CAA27557.1; PID:g53427 REFERENCE S02126 !$#authors Katoh, K.; Sawai, S.; Ueno, K.; Kondoh, H. !$#journal Nucleic Acids Res. (1988) 16:3589 !$#title Complete nucleotide sequence and exon-intron boundaries of !1the 5' non-coding region of the mouse N-myc gene. !$#cross-references MUID:88233958; PMID:3287334 !$#accession S02126 !'##status preliminary; translation not shown !'##molecule_type DNA !'##residues 1-39 ##label KAT !'##cross-references EMBL:X06993 GENETICS !$#gene N-myc !$#introns 261/3 CLASSIFICATION #superfamily myc transforming protein; myc transforming !1protein homology KEYWORDS DNA binding; nucleus; phosphoprotein; proto-oncogene; !1transforming protein FEATURE !$19-462 #domain myc transforming protein homology #label MYC SUMMARY #length 462 #molecular-weight 49573 #checksum 4302 SEQUENCE /// ENTRY TVCHMC #type complete TITLE transforming protein N-myc - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jun-2000 ACCESSIONS A34703; JT0545 REFERENCE A34703 !$#authors Sawai, S.; Kato, K.; Wakamatsu, Y.; Kondoh, H. !$#journal Mol. Cell. Biol. (1990) 10:2017-2026 !$#title Organization and expression of the chicken N-myc gene. !$#cross-references MUID:90220586; PMID:2183017 !$#accession A34703 !'##molecule_type DNA !'##residues 1-441 ##label SAW !'##cross-references GB:D90071; NID:g222842; PIDN:BAA14112.1; !1PID:g222843 GENETICS !$#gene N-myc !$#introns 243/1 CLASSIFICATION #superfamily myc transforming protein; myc transforming !1protein homology KEYWORDS DNA binding; leucine zipper; nucleus; phosphoprotein; !1transforming protein FEATURE !$11-441 #domain myc transforming protein homology #label MYC\ !$410-438 #region leucine zipper motif SUMMARY #length 441 #molecular-weight 48696 #checksum 3131 SEQUENCE /// ENTRY TVMSML #type complete TITLE transforming protein L-myc - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 18-Jun-1999 ACCESSIONS S03017 REFERENCE S03017 !$#authors Legouy, E.; DePinho, R.; Zimmerman, K.; Collum, R.; !1Yancopoulos, G.; Mitsock, L.; Kriz, R.; Alt, F.W. !$#journal EMBO J. (1987) 6:3359-3366 !$#title Structure and expression of the murine L-myc gene. !$#cross-references MUID:88111523; PMID:2828024 !$#accession S03017 !'##molecule_type DNA !'##residues 1-368 ##label LEG !'##cross-references GB:X13945; GB:X06183; GB:X13949; GB:Y00082; !1NID:g53287; PIDN:CAA32128.1; PID:g53288 GENETICS !$#gene L-myc CLASSIFICATION #superfamily myc transforming protein; myc transforming !1protein homology KEYWORDS DNA binding; leucine zipper; nucleus; transforming protein FEATURE !$1-368 #domain myc transforming protein homology #label MYC\ !$337-365 #region leucine zipper motif SUMMARY #length 368 #molecular-weight 40848 #checksum 5 SEQUENCE /// ENTRY TVHUML #type complete TITLE transforming protein L-myc-1 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 18-Jun-1999 ACCESSIONS A27675; S01200; S09390 REFERENCE A27675 !$#authors Kaye, F.; Battey, J.; Nau, M.; Brooks, B.; Seifter, E.; De !1Greve, J.; Birrer, M.; Sausville, E.; Minna, J. !$#journal Mol. Cell. Biol. (1988) 8:186-195 !$#title Structure and expression of the human L-myc gene reveal a !1complex pattern of alternative mRNA processing. !$#cross-references MUID:88094386; PMID:2827002 !$#accession A27675 !'##molecule_type DNA !'##residues 1-364 ##label KAY !'##cross-references GB:M19720; NID:g188906; PIDN:AAA59879.1; !1PID:g386964 REFERENCE S01200 !$#authors DePinho, R.A.; Hatton, K.S.; Tesfaye, A.; Yancopoulos, G.D.; !1Alt, F.W. !$#journal Genes Dev. (1987) 1:1311-1326 !$#title The human myc gene family: structure and activity of L-myc !1and an L-myc pseudogene. !$#cross-references MUID:88112807; PMID:3322939 !$#accession S01200 !'##molecule_type DNA !'##residues 1-364 ##label DEP REFERENCE S09390 !$#authors Ikegaki, N.; Minna, J.; Kennett, R.H. !$#journal EMBO J. (1989) 8:1793-1799 !$#title The human L-myc gene is expressed as two forms of protein in !1small cell lung carcinoma cell lines: detection by !1monoclonal antibodies specific to two myc homology box !1sequences. !$#cross-references MUID:89356654; PMID:2548855 !$#accession S09390 !'##status preliminary !'##molecule_type protein !'##residues 165-179 ##label IKE GENETICS !$#gene GDB:MYCL1 !'##cross-references GDB:120706; OMIM:164850 !$#map_position 1p32-1p32 !$#introns 166/1 CLASSIFICATION #superfamily myc transforming protein; myc transforming !1protein homology KEYWORDS DNA binding; nucleus; transforming protein FEATURE !$1-364 #domain myc transforming protein homology #label MYC SUMMARY #length 364 #molecular-weight 40312 #checksum 9684 SEQUENCE /// ENTRY TVHUL2 #type complete TITLE transforming protein L-myc-2 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 18-Jun-1999 ACCESSIONS A30146; S40641 REFERENCE A30146 !$#authors Morton, C.C.; Nussenzweig, M.C.; Sousa, R.; Sorenson, G.D.; !1Pettengill, O.S.; Shows, T.B. !$#journal Genomics (1989) 4:367-375 !$#title Mapping and characterization of an X-linked processed gene !1related to MYCL1. !$#cross-references MUID:89233129; PMID:2541066 !$#accession A30146 !'##molecule_type DNA !'##residues 1-357 ##label MOR !'##cross-references GB:J03069; NID:g188952; PIDN:AAA59883.1; !1PID:g188953 REFERENCE S40641 !$#authors Robertson, N.G.; Pomponio, R.J.; Mutter, G.L.; Morton, C.C. !$#journal Nucleic Acids Res. (1991) 19:3129-3137 !$#title Testis-specific expression of the human MYCL2 gene. !$#cross-references MUID:91279473; PMID:1711681 !$#accession S40641 !'##status preliminary !'##molecule_type mRNA !'##residues 273-354 ##label ROB GENETICS !$#gene GDB:MYCL2 !'##cross-references GDB:120209; OMIM:310310 !$#map_position Xq22-Xq28 CLASSIFICATION #superfamily myc transforming protein; myc transforming !1protein homology KEYWORDS DNA binding; leucine zipper; nucleus; transforming protein FEATURE !$1-357 #domain myc transforming protein homology #label MYC\ !$326-354 #region leucine zipper motif SUMMARY #length 357 #molecular-weight 41113 #checksum 7519 SEQUENCE /// ENTRY TVRTBM #type complete TITLE transforming protein B-myc - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1989 #sequence_revision 22-Apr-1995 #text_change 28-May-1999 ACCESSIONS A45502; A31198 REFERENCE A45502 !$#authors Asker, C.; Steinitz, M.; Andersson, K.; Suemegi, J.; Klein, !1G.; Ingvarsson, S. !$#journal Oncogene (1989) 4:1523-1527 !$#title Nucleotide sequence of the rat B-myc gene. !$#cross-references MUID:90082428; PMID:2687773 !$#accession A45502 !'##molecule_type DNA !'##residues 1-178 ##label ASK !'##cross-references GB:X17455; NID:g55830; PIDN:CAA35499.1; PID:g55831 !'##note the authors translated the codon CAC for residue 173 as Gln REFERENCE A31198 !$#authors Ingvarsson, S.; Asker, C.; Axelson, H.; Klein, G.; Suemegi, !1J. !$#journal Mol. Cell. Biol. (1988) 8:3168-3174 !$#title Structure and expression of B-myc, a new member of the myc !1gene family. !$#cross-references MUID:89096904; PMID:2850482 !$#accession A31198 !'##molecule_type mRNA !'##residues 1-120 ##label ING COMMENT The sequence is related to the amino end of the myc protein. !1It is missing the region thought to be important for nuclear !1localization, DNA binding, transforming activity, and !1oligomerization. GENETICS !$#gene B-myc CLASSIFICATION #superfamily transforming protein B-myc; myc transforming !1protein homology KEYWORDS DNA binding; transforming protein FEATURE !$14-178 #domain myc transforming protein homology #status !8atypical #label MYC SUMMARY #length 178 #molecular-weight 19463 #checksum 5965 SEQUENCE /// ENTRY FOFV29 #type complete TITLE gag-myc polyprotein - avian myelocytomatosis virus MC29 (provirus) CONTAINS amino end of core protein p27; core protein p10; core protein p19; transforming protein myc ORGANISM #formal_name avian myelocytomatosis virus MC29 #note host Gallus gallus (chicken) DATE 14-Nov-1983 #sequence_revision 09-Sep-1994 #text_change 28-Jul-2000 ACCESSIONS A03923; A93939; A01353; A93947 REFERENCE A93947 !$#authors Reddy, E.P.; Reynolds, R.K.; Watson, D.K.; Schultz, R.A.; !1Lautenberger, J.; Papas, T.S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:2500-2504 !$#title Nucleotide sequence analysis of the proviral genome of avian !1myelocytomatosis virus (MC29). !$#cross-references MUID:83195085; PMID:6302688 !$#accession A03923 !'##molecule_type DNA !'##residues 1-875 ##label RED !'##cross-references GB:J02247; NID:g61608; PIDN:CAA24499.1; PID:g61609 !'##note mC29 is a replication-defective, integrated provirus REFERENCE A93939 !$#authors Alitalo, K.; Bishop, J.M.; Smith, D.H.; Chen, E.Y.; Colby, !1W.W.; Levinson, A.D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:100-104 !$#title Nucleotide sequence of the v-myc oncogene of avian !1retrovirus MC29. !$#cross-references MUID:83117796; PMID:6296857 !$#accession A93939 !'##molecule_type DNA !'##residues 454-604,'R',606-847,'R',849-875 ##label ALI COMMENT Transformed cell lines produce a 110K gag-myc hybrid !1protein. GENETICS !$#gene gag-myc CLASSIFICATION #superfamily avian myelocytomatosis virus gag-myc !1polyprotein; myc transforming protein homology KEYWORDS core protein; DNA binding; nucleus; oncogene; polyprotein; !1transforming protein FEATURE !$1-452 #region virus gene-derived\ !$1-175 #product core protein p19 #status predicted #label !8C19\ !$178-239 #product core protein p10 #status predicted #label !8C10\ !$240-453 #product core protein p27 #status predicted #label !8C27\ !$453-875 #region host gene-derived\ !$473-873 #domain myc transforming protein homology #label MYC SUMMARY #length 875 #molecular-weight 94259 #checksum 5011 SEQUENCE /// ENTRY FOFVHB #type complete TITLE gag-myc polyprotein - avian myelocytomatosis virus (strain HBI) CONTAINS core protein p10; core protein p19; core protein p27; transforming protein myc ORGANISM #formal_name avian myelocytomatosis virus DATE 30-Jun-1987 #sequence_revision 09-Sep-1994 #text_change 18-Jun-1999 ACCESSIONS A03924; A01354 REFERENCE A93014 !$#authors Smith, D.R.; Vennstrom, B.; Hayman, M.J.; Enrietto, P.J. !$#journal J. Virol. (1985) 56:969-977 !$#title Nucleotide sequence of HBI, a novel recombinant MC29 !1derivative with altered pathogenic properties. !$#cross-references MUID:86062930; PMID:2999450 !$#accession A03924 !'##molecule_type DNA !'##residues 1-875 ##label SMI !'##cross-references GB:M11784; NID:g209694; PIDN:AAA42406.1; !1PID:g209695 GENETICS !$#gene gag-myc CLASSIFICATION #superfamily avian myelocytomatosis virus gag-myc !1polyprotein; myc transforming protein homology KEYWORDS core protein; DNA binding; nucleus; oncogene; polyprotein; !1transforming protein FEATURE !$1-452 #region virus gene-derived\ !$1-175 #product core protein p19 #status predicted #label !8P19\ !$178-239 #product core protein p10 #status predicted #label !8P10\ !$240-453 #product core protein p27 #status predicted #label !8P27\ !$453-875 #region host gene-derived\ !$473-873 #domain myc transforming protein homology #label MYC SUMMARY #length 875 #molecular-weight 94100 #checksum 4931 SEQUENCE /// ENTRY TVFV2C #type fragment TITLE gag-myc polyprotein - avian myelocytomatosis virus CMII (fragment) ORGANISM #formal_name avian myelocytomatosis virus CMII DATE 31-Dec-1988 #sequence_revision 09-Sep-1994 #text_change 18-Jun-1999 ACCESSIONS A24297 REFERENCE A24297 !$#authors Walther, N.; Jansen, H.W.; Trachmann, C.; Bister, K. !$#journal Virology (1986) 154:219-223 !$#title Nucleotide sequence of the CMII v-myc allele. !$#cross-references MUID:86317715; PMID:3019003 !$#accession A24297 !'##molecule_type DNA !'##residues 1-451 ##label WAL !'##cross-references GB:M15241; NID:g209697; PIDN:AAA42408.1; !1PID:g209698 GENETICS !$#gene gag-myc CLASSIFICATION #superfamily avian myelocytomatosis virus gag-myc !1polyprotein; myc transforming protein homology KEYWORDS DNA binding; transforming protein FEATURE !$49-449 #domain myc transforming protein homology #label MYC SUMMARY #length 451 #checksum 1081 SEQUENCE /// ENTRY B37953 #type complete TITLE transcription regulator PAN-2 - golden hamster ORGANISM #formal_name Mesocricetus auratus #common_name golden hamster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B37953 REFERENCE A37953 !$#authors German, M.S.; Blanar, M.A.; Nelson, C.; Moss, L.G.; Rutter, !1W.J. !$#journal Mol. Endocrinol. (1991) 5:292-299 !$#title Two related helix-loop-helix proteins participate in !1separate cell-specific complexes that bind the insulin !1enhancer. !$#cross-references MUID:91246228; PMID:1710033 !$#accession B37953 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-649 ##label GER CLASSIFICATION #superfamily human transcription factor 3 SUMMARY #length 649 #molecular-weight 67322 #checksum 2623 SEQUENCE /// ENTRY S23391 #type complete TITLE transcription factor E12 - African clawed frog ALTERNATE_NAMES DNA-binding protein E12 ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S23391 REFERENCE S23391 !$#authors Rashbass, J.; Taylor, M.V.; Gurdon, J.B. !$#journal EMBO J. (1992) 11:2981-2990 !$#title The DNA-binding protein E12 co-operates with XMyoD in the !1activation of muscle-specific gene expression in Xenopus !1embryos. !$#cross-references MUID:92347333; PMID:1322293 !$#accession S23391 !'##molecule_type mRNA !'##residues 1-658 ##label RAS !'##cross-references EMBL:X66959; NID:g65223; PIDN:CAA47381.1; !1PID:g65224 CLASSIFICATION #superfamily human transcription factor 3 KEYWORDS transcription factor SUMMARY #length 658 #molecular-weight 70090 #checksum 602 SEQUENCE /// ENTRY S34416 #type complete TITLE transcription factor ITF-2 - dog ORGANISM #formal_name Canis lupus familiaris #common_name dog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S34416; S08433 REFERENCE S34416 !$#authors Javaux, F.; Donda, A.; Vassart, G.; Christophe, D. !$#journal Nucleic Acids Res. (1991) 19:1121-1127 !$#title Cloning and sequence analysis of TFE, a helix-loop-helix !1transcription factor able to recognize the thyroglobulin !1gene promoter in vitro. !$#cross-references MUID:91212194; PMID:1840650 !$#accession S34416 !'##status preliminary !'##molecule_type mRNA !'##residues 1-642 ##label JAV !'##cross-references EMBL:X51448; NID:g938; PIDN:CAA35812.1; PID:g940 REFERENCE S08432 !$#authors Javaux, F.; Vassart, G.; Christophe, D. !$#journal Nucleic Acids Res. (1990) 18:1301 !$#title Nucleotide sequence of a putative transcription factor !1recognizing the thyroglobulin promoter. !$#cross-references MUID:90206807; PMID:2320428 !$#accession S08433 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-551,'PRHQRGFQGARPHGAAPPQE' ##label JA2 !'##cross-references EMBL:X51448 CLASSIFICATION #superfamily human transcription factor 3 KEYWORDS DNA binding; transcription regulation SUMMARY #length 642 #molecular-weight 68354 #checksum 9239 SEQUENCE /// ENTRY TVFVSK #type complete TITLE transforming protein ski - avian erythroblastosis virus (strain Sloan-Kettering) ORGANISM #formal_name avian erythroblastosis virus DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 02-Jun-1994 ACCESSIONS A32574 REFERENCE A32574 !$#authors Stavnezer, E.; Brodeur, D.; Brennan, L.A. !$#journal Mol. Cell. Biol. (1989) 9:4038-4045 !$#title The v-ski oncogene encodes a truncated set of c-ski coding !1exons with limited sequence and structural relatedness to !1v-myc. !$#cross-references MUID:89384634; PMID:2674685 !$#accession A32574 !'##molecule_type DNA !'##residues 1-437 ##label STA GENETICS !$#gene v-ski CLASSIFICATION #superfamily ski transforming protein KEYWORDS transforming protein SUMMARY #length 437 #molecular-weight 48867 #checksum 931 SEQUENCE /// ENTRY TVHUSK #type complete TITLE transforming protein ski - human ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 18-Jun-1999 ACCESSIONS S06053 REFERENCE S06052 !$#authors Nomura, N.; Sasamoto, S.; Ishii, S.; Date, T.; Matsui, M.; !1Ishizaki, R. !$#journal Nucleic Acids Res. (1989) 17:5489-5500 !$#title Isolation of human cDNA clones of ski and the ski-related !1gene, sno. !$#cross-references MUID:89345144; PMID:2762147 !$#accession S06053 !'##molecule_type mRNA !'##residues 1-728 ##label NOM !'##cross-references GB:X15218; NID:g36483; PIDN:CAA33288.1; PID:g36484 COMMENT Transforming proteins ski may function as a transcription !1factor regulating muscle gene expression. GENETICS !$#gene GDB:SKI !'##cross-references GDB:119595; OMIM:164780 !$#map_position 1q22-1q24 CLASSIFICATION #superfamily ski transforming protein KEYWORDS proto-oncogene; tandem repeat; transforming protein FEATURE !$61-93 #region proline-rich\ !$494-509 #region serine-rich\ !$558-582,583-607, !$608-633 #region 25-residue repeats SUMMARY #length 728 #molecular-weight 80004 #checksum 4247 SEQUENCE /// ENTRY S29923 #type complete TITLE transforming protein c-ski - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS I51644; S29923 REFERENCE I51644 !$#authors Sleeman, J.P.; Laskey, R.A. !$#journal Oncogene (1993) 8:67-77 !$#title Xenopus c-ski contains a novel coiled-coil protein domain, !1and is maternally expressed during development. !$#cross-references MUID:93141278; PMID:8423997 !$#accession I51644 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-717 ##label SL2 !'##cross-references EMBL:X68683; NID:g65100; PIDN:CAA48642.1; !1PID:g65101 GENETICS !$#gene c-ski CLASSIFICATION #superfamily ski transforming protein KEYWORDS nucleus SUMMARY #length 717 #molecular-weight 80739 #checksum 8318 SEQUENCE /// ENTRY TVHUSN #type complete TITLE transforming protein sno-N - human ALTERNATE_NAMES ski-related novel gene, non-Alu-containing CONTAINS transforming protein sno-I ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 18-Jun-1999 ACCESSIONS S06052; S42108; S33508 REFERENCE S06052 !$#authors Nomura, N.; Sasamoto, S.; Ishii, S.; Date, T.; Matsui, M.; !1Ishizaki, R. !$#journal Nucleic Acids Res. (1989) 17:5489-5500 !$#title Isolation of human cDNA clones of ski and the ski-related !1gene, sno. !$#cross-references MUID:89345144; PMID:2762147 !$#accession S06052 !'##molecule_type mRNA !'##residues 1-684 ##label NOM !'##cross-references EMBL:X15219; NID:g36510; PIDN:CAA33289.1; !1PID:g36511 !'##note the sequence from clone lambda-sno3 differs from that shown in !1having 38-Ala REFERENCE S42108 !$#authors Pearson-White, S. !$#journal Nucleic Acids Res. (1993) 21:4632-4638 !$#title SnoI, a novel alternatively spliced isoform of the ski !1proto-oncogene homolog, sno. !$#cross-references MUID:94051573; PMID:8233802 !$#accession S42108 !'##molecule_type mRNA !'##residues 'R',14-37,'A',39-399 ##label PEA !'##cross-references EMBL:Z19588; NID:g311623; PIDN:CAA79636.1; !1PID:g460982 !'##experimental_source myoblasts !'##note the authors translated the codon GCA for residue 38 as Val; !1this splice form has a termination codon after residue 399 COMMENT Transforming proteins sno-N and sno-I may function as !1transcription factors regulating muscle gene expression. !1Transforming protein sno-I appears to be expressed !1exclusively in myoblasts and myofibers. See PIR:TVHUSA. GENETICS !$#gene GDB:SNO !'##cross-references GDB:204117 CLASSIFICATION #superfamily ski transforming protein KEYWORDS alternative splicing; proto-oncogene; transforming protein FEATURE !$1-684 #product transforming protein sno-N #status predicted !8#label MATN\ !$1-399 #product transforming protein sno-I #status predicted !8#label MATI SUMMARY #length 684 #molecular-weight 77003 #checksum 3812 SEQUENCE /// ENTRY TVHUSA #type complete TITLE transforming protein sno-A - human ALTERNATE_NAMES ski-related novel gene, Alu-containing ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 18-Jun-1999 ACCESSIONS S06054 REFERENCE S06052 !$#authors Nomura, N.; Sasamoto, S.; Ishii, S.; Date, T.; Matsui, M.; !1Ishizaki, R. !$#journal Nucleic Acids Res. (1989) 17:5489-5500 !$#title Isolation of human cDNA clones of ski and the ski-related !1gene, sno. !$#cross-references MUID:89345144; PMID:2762147 !$#accession S06054 !'##molecule_type mRNA !'##residues 1-415 ##label NOM !'##cross-references EMBL:X15217; NID:g36508; PIDN:CAA33287.1; !1PID:g36509 !'##note the sequence from clone lambda-sno3 differs from that shown in !1having 38-Ala COMMENT Transforming protein sno-A may function as a transcription !1factor regulating muscle gene expression. See PIR:TVHUSN. GENETICS !$#gene GDB:SNO !'##cross-references GDB:204117 CLASSIFICATION #superfamily ski transforming protein KEYWORDS alternative splicing; proto-oncogene; transforming protein FEATURE !$369-381 #region hydrophobic SUMMARY #length 415 #molecular-weight 46362 #checksum 2462 SEQUENCE /// ENTRY TVHURA #type complete TITLE GTP-binding protein N-ras - human ALTERNATE_NAMES p21 transforming protein; transforming protein N-ras ORGANISM #formal_name Homo sapiens #common_name man DATE 18-Apr-1984 #sequence_revision 18-Apr-1984 #text_change 19-Jan-2001 ACCESSIONS A90839; B90839; A21700; B21700; A93575; S02328; A60193; !1I59056; I52559; A01359; A23790 REFERENCE A90839 !$#authors Taparowsky, E.; Shimizu, K.; Goldfarb, M.; Wigler, M. !$#journal Cell (1983) 34:581-586 !$#title Structure and activation of the human N-ras gene. !$#cross-references MUID:84002264; PMID:6616621 !$#accession A90839 !'##molecule_type DNA !'##residues 1-189 ##label TA1 !'##cross-references GB:L00040 !'##experimental_source normal cells !$#accession B90839 !'##molecule_type DNA !'##residues 1-60,'K',62-189 ##label TA2 !'##experimental_source neuroblastoma cell line SK-N-SH REFERENCE A21700 !$#authors Brown, R.; Marshall, C.J.; Pennie, S.G.; Hall, A. !$#journal EMBO J. (1984) 3:1321-1326 !$#title Mechanism of activation of an N-ras gene in the human !1fibrosarcoma cell line HT1080. !$#cross-references MUID:84261421; PMID:6086315 !$#accession A21700 !'##molecule_type DNA !'##residues 1-189 ##label BR1 !'##cross-references GB:X00642 !'##experimental_source normal cells !$#accession B21700 !'##molecule_type DNA !'##residues 1-60,'K',62-189 ##label BR2 !'##experimental_source fibrosarcoma cell line HT1080 REFERENCE A93575 !$#authors Hall, A.; Brown, R. !$#journal Nucleic Acids Res. (1985) 13:5255-5268 !$#title Human N-ras: cDNA cloning and gene structure. !$#cross-references MUID:85269641; PMID:2991860 !$#accession A93575 !'##molecule_type mRNA !'##residues 1-189 ##label HAL !'##cross-references GB:X02751; NID:g35102; PIDN:CAA26529.1; PID:g35103 !'##experimental_source cell line FLOW 2002 REFERENCE S02328 !$#authors Raybaud, F.; Noguchi, T.; Marics, I.; Adelaide, J.; Planche, !1J.; Batoz, M.; Aubert, C.; de Lapeyriere, O.; Birnbaum, D. !$#journal Cancer Res. (1988) 48:950-953 !$#title Detection of a low frequency of activated ras genes in human !1melanomas using a tumorigenicity assay. !$#cross-references MUID:88109371; PMID:3276402 !$#accession S02328 !'##molecule_type DNA !'##residues 60,'R',62-96 ##label RAY !'##cross-references EMBL:X07440; NID:g35301; PIDN:CAA30320.1; !1PID:g929658 REFERENCE A60193 !$#authors Yuasa, Y.; Kamiyama, T.; Kato, M.; Iwama, T.; Ikeuchi, T.; !1Tonomura, A. !$#journal Oncogene (1990) 5:589-596 !$#title Transforming genes from familial adenomatous polyposis !1patient cells detected by a tumorigenicity assay. !$#cross-references MUID:90221601; PMID:1970154 !$#accession A60193 !'##molecule_type DNA !'##residues 1-29;43-78 ##label YUA !'##cross-references GB:X53291; NID:g35098; PIDN:CAA37384.1; !1PID:g825697; GB:X53292 !'##experimental_source cells from familial adenomatous polyposis !1patient REFERENCE I59056 !$#authors Gambke, C.; Hall, A.; Moroni, C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:879-882 !$#title Activation of an N-ras gene in acute myeloblastic leukemia !1through somatic mutation in the first exon. !$#cross-references MUID:85140199; PMID:3856237 !$#accession I59056 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-96 ##label RES !'##cross-references GB:K03211; NID:g190930; PIDN:AAA36556.1; !1PID:g553638 REFERENCE I52559 !$#authors Hirai, H.; Tanaka, S.; Azuma, M.; Anraku, Y.; Kobayashi, Y.; !1Fujisawa, M.; Okabe, T.; Urabe, A.; Takaku, F. !$#journal Blood (1985) 66:1371-1378 !$#title Transforming genes in human leukemia cells. !$#cross-references MUID:86051910; PMID:2998510 !$#accession I52559 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-11,'C',13-96 ##label RE2 !'##cross-references GB:M25898; NID:g190882; PIDN:AAA36548.1; !1PID:g553633 !'##experimental_source CML-1 and ALL-1 human leukemia cells !'##note a mutation of Gly to Cys in the GTP-binding site was found as !1the lesion in a number of independent leukemic cells GENETICS !$#gene GDB:NRAS !'##cross-references GDB:119457; OMIM:164790 !$#map_position 1p13.2-1p13.2 !$#introns 37/3; 97/2; 150/3 CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS GTP binding; lipoprotein; membrane protein; methylated !1carboxyl end; nucleotide binding; P-loop; prenylated !1cysteine; proto-oncogene; thiolester bond; transforming !1protein FEATURE !$2-186 #product GTP-binding protein N-ras #status predicted !8#label MAT\ !$4-119 #domain translation elongation factor Tu homology !8#label ETU\ !$10-17 #region nucleotide-binding motif A (P-loop)\ !$116-119 #region GTP-binding NKXD motif\ !$145-147 #region GTP-binding SAK/L motif\ !$16,17,35,116,117, !$119,145 #binding_site Mg-GTP (Lys, Ser, Thr, Asn, Lys, Asp, !8Ser) #status predicted\ !$181 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$186 #binding_site farnesyl (Cys) (covalent) #status !8predicted\ !$186 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted SUMMARY #length 189 #molecular-weight 21229 #checksum 2905 SEQUENCE /// ENTRY TVMSNS #type complete TITLE transforming protein N-ras - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 19-Jan-2001 ACCESSIONS A23560; PQ0095; S02054 REFERENCE A23560 !$#authors Guerrero, I.; Villasante, A.; Corces, V.; Pellicer, A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:7810-7814 !$#title Loss of the normal N-ras allele in a mouse thymic lymphoma !1induced by a chemical carcinogen. !$#cross-references MUID:86067993; PMID:3865197 !$#accession A23560 !'##molecule_type DNA !'##residues 1-189 ##label GUE !'##cross-references GB:M12124; NID:g200104; PIDN:AAA39839.1; !1PID:g387498 REFERENCE PQ0095 !$#authors Yuasa, Y.; Yamazaki, H.; Maruo, K.; Ueyama, Y.; Shibuya, M.; !1Tamaoki, N. !$#journal Jpn. J. Cancer Res. (1990) 81:333-339 !$#title Alterations of mouse proto-oncogenes in sarcomas induced !1after transplantation of human tumors in athymic nude mice. !$#cross-references MUID:90307554; PMID:2114387 !$#accession PQ0095 !'##molecule_type DNA !'##residues 1-11,'D',13-29;43-78 ##label YUA !'##cross-references DDBJ:D00640; NID:g220381; PIDN:BAA25127.1; !1PID:g2959437; DDBJ:D00836; NID:g220382; PIDN:BAA28218.1; !1PID:g3135097 !'##experimental_source strain BALB/c nu/nu !'##note this sequence was determined from the activated gene in tumor REFERENCE S02054 !$#authors Chang, H.Y.; Guerrero, I.; Lake, R.; Pellicer, A.; !1d'Eustachio, P. !$#journal Oncogene Res. (1987) 1:129-136 !$#title Mouse N-ras genes: organization of the functional locus and !1of a truncated cDNA-like pseudogene. !$#cross-references MUID:88217314; PMID:2835730 !$#accession S02054 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-189,'CKTL' ##label CHA !'##cross-references EMBL:X13664; NID:g53447; PIDN:CAA31958.1; !1PID:g53448 GENETICS !$#gene N-ras !$#map_position 3 !$#introns 37/3; 97/2; 150/3 CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS GTP binding; lipoprotein; membrane protein; methylated !1carboxyl end; nucleotide binding; P-loop; prenylated !1cysteine; transforming protein FEATURE !$4-119 #domain translation elongation factor Tu homology !8#label ETU\ !$10-17 #region nucleotide-binding motif A (P-loop)\ !$116-119 #region GTP-binding NKXD motif\ !$145-147 #region GTP-binding SAK/L motif\ !$16,17,35,116,117, !$119,145 #binding_site Mg-GTP (Lys, Ser, Thr, Asn, Lys, Asp, !8Ser) #status predicted\ !$186 #binding_site farnesyl (Cys) (covalent) #status !8predicted\ !$186 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted SUMMARY #length 189 #molecular-weight 21199 #checksum 2772 SEQUENCE /// ENTRY TVGPRS #type complete TITLE GTP-binding protein N-ras - guinea pig ALTERNATE_NAMES p21 transforming protein; transforming protein N-ras ORGANISM #formal_name Cavia porcellus #common_name guinea pig DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 19-Jan-2001 ACCESSIONS A26552; S25431 REFERENCE A26552 !$#authors Doniger, J.; Notario, V.; DiPaolo, J.A. !$#journal J. Biol. Chem. (1987) 262:3813-3819 !$#title Carcinogens with diverse mutagenic activities initiate !1neoplastic guinea pig cells that acquire the same N-ras !1point mutation. !$#cross-references MUID:87137688; PMID:3029126 !$#accession A26552 !'##molecule_type mRNA !'##residues 1-189 ##label DON !'##cross-references GB:M15808; NID:g191290; PIDN:AAA37050.1; !1PID:g387062 REFERENCE S25431 !$#authors Doniger, J. !$#journal Oncogene (1987) 1:331-334 !$#title Differential conservation of non-coding regions within human !1and guinea pig N-ras genes. !$#cross-references MUID:88262225; PMID:3133626 !$#accession S25431 !'##status preliminary !'##molecule_type DNA !'##residues 1-189 ##label DO2 !'##cross-references EMBL:X60130 GENETICS !$#gene N-ras !$#introns 37/3; 97/2; 150/3 CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS alternative splicing; GTP binding; lipoprotein; membrane !1protein; methylated carboxyl end; nucleotide binding; !1P-loop; prenylated cysteine; proto-oncogene; thiolester !1bond; transforming protein FEATURE !$4-119 #domain translation elongation factor Tu homology !8#label ETU\ !$10-17 #region nucleotide-binding motif A (P-loop)\ !$116-119 #region GTP-binding NKXD motif\ !$145-147 #region GTP-binding SAK/L motif\ !$16,17,35,116,117, !$119,145 #binding_site Mg-GTP (Lys, Ser, Thr, Asn, Lys, Asp, !8Ser) #status predicted\ !$181 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$186 #binding_site farnesyl (Cys) (covalent) #status !8predicted\ !$186 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted SUMMARY #length 189 #molecular-weight 21256 #checksum 2890 SEQUENCE /// ENTRY TVGPRT #type complete TITLE GTP-binding protein N-ras, short splice form - guinea pig ALTERNATE_NAMES transforming protein N-ras ORGANISM #formal_name Cavia porcellus #common_name guinea pig DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 19-Jan-2001 ACCESSIONS A23652 REFERENCE A23652 !$#authors Doniger, J. !$#journal Oncogene (1988) 2:293-294 !$#title Alternative splicing results in a truncated N-ras protein. !$#cross-references MUID:88176040; PMID:3281097 !$#accession A23652 !'##molecule_type mRNA !'##residues 1-106 ##label DON !'##cross-references GB:X60128; GB:Y00663; NID:g49556; PIDN:CAA42716.1; !1PID:g49557 GENETICS !$#gene N-ras CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS alternative splicing; GTP binding; nucleotide binding; !1P-loop; transforming protein FEATURE !$10-17 #region nucleotide-binding motif A (P-loop) SUMMARY #length 106 #molecular-weight 11976 #checksum 8707 SEQUENCE /// ENTRY TVHUH #type complete TITLE transforming protein p21 (H-ras-1) [validated] - human ALTERNATE_NAMES c-bas/has oncogene; c-H-ras protein; c-Ha-ras protein; c-Harvey-ras protein; H-ras oncogene CONTAINS GTPase (EC 3.6.1.-) ORGANISM #formal_name Homo sapiens #common_name man DATE 18-Apr-1984 #sequence_revision 18-Apr-1984 #text_change 19-Jan-2001 ACCESSIONS A93299; A94270; A93292; I37096; A94000; I56950; I52688; !1I57624; I59121; S34768; S07800; I38148; I51857; A01360 REFERENCE A93299 !$#authors Capon, D.J.; Chen, E.Y.; Levinson, A.D.; Seeburg, P.H.; !1Goeddel, D.V. !$#journal Nature (1983) 302:33-37 !$#title Complete nucleotide sequences of the T24 human bladder !1carcinoma oncogene and its normal homologue. !$#cross-references MUID:83141783; PMID:6298635 !$#accession A93299 !'##molecule_type DNA !'##residues 1-189 ##label CAP !'##cross-references GB:V00574; GB:J00206; GB:J00276; GB:J00277; !1GB:K00954; NID:g35886; PIDN:CAA23837.1; PID:g35887 !'##experimental_source normal and T24 bladder carcinoma REFERENCE A94270 !$#authors Reddy, E.P. !$#journal Science (1983) 220:1061-1063 !$#title Nucleotide sequence analysis of the T24 human bladder !1carcinoma oncogene. !$#cross-references MUID:83197392; PMID:6844927 !$#accession A94270 !'##molecule_type DNA !'##residues 1-189 ##label RED !'##cross-references GB:J00277; GB:J00206; GB:J00276; GB:K00954; !1NID:g190890; PIDN:AAB02605.1; PID:g190891 !'##experimental_source normal and T24 bladder carcinoma REFERENCE A93292 !$#authors Tabin, C.J.; Bradley, S.M.; Bargmann, C.I.; Weinberg, R.A.; !1Papageorge, A.G.; Scolnick, E.M.; Dhar, R.; Lowy, D.R.; !1Chang, E.H. !$#journal Nature (1982) 300:143-149 !$#title Mechanism of activation of a human oncogene. !$#cross-references MUID:83036978; PMID:6290897 !$#accession A93292 !'##molecule_type DNA !'##residues 1-37 ##label TAB !'##cross-references GB:J00277; GB:J00206; GB:J00276; GB:K00954; !1NID:g190890 !'##experimental_source normal and EJ bladder carcinoma REFERENCE I37096 !$#authors Yuasa, Y.; Srivastava, S.K.; Dunn, C.Y.; Rhim, J.S.; Reddy, !1E.P.; Aaronson, S.A. !$#journal Nature (1983) 303:775-779 !$#title Acquisition of transforming properties by alternative point !1mutations within c-bas/has human proto-oncogene. !$#cross-references MUID:83244961; PMID:6866079 !$#accession I37096 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-37 ##label YUA !'##cross-references EMBL:X01227; NID:g23713; PID:g23714 REFERENCE A94000 !$#authors Sekiya, T.; Fushimi, M.; Hori, H.; Hirohashi, S.; Nishimura, !1S.; Sugimura, T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:4771-4775 !$#title Molecular cloning and the total nucleotide sequence of the !1human c-Ha-ras-1 gene activated in a melanoma from a !1Japanese patient. !$#cross-references MUID:84272715; PMID:6087347 !$#accession A94000 !'##molecule_type DNA !'##residues 1-189 ##label SEK1 !'##cross-references GB:J00277; GB:J00206; GB:J00276; GB:K00954; !1NID:g190890; PIDN:AAB02605.1; PID:g190891 !'##experimental_source normal and melanoma tissues !'##note T24 and EJ bladder carcinoma sequences differ from the normal !1sequence in having 12-Val; the melanoma sequence differs !1from from the normal sequence in having 61-Leu REFERENCE I56950 !$#authors Sekiya, T.; Tokunaga, A.; Fushimi, M. !$#journal Jpn. J. Cancer Res. (1985) 76:787-791 !$#title Essential region for transforming activity of human !1c-Ha-ras-1. !$#cross-references MUID:86033277; PMID:3932274 !$#accession I56950 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-37 ##label SEK2 !'##cross-references GB:M30539; NID:g190937; PIDN:AAA36557.1; !1PID:g190938 REFERENCE I52688 !$#authors Deng, G.; Lu, Y.; Chen, S.; Miao, J.; Lu, G.; Li, H.; Cai, !1H.; Xu, X.; Zheng, E.; Liu, P. !$#journal Cancer Res. (1987) 47:3195-3198 !$#title Activated c-Ha-ras oncogene with a guanine to thymine !1transversion at the twelfth codon in a human stomach cancer !1cell line. !$#cross-references MUID:87215620; PMID:3034404 !$#accession I52688 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-11,'V',13-37 ##label DEN !'##cross-references GB:M25876; NID:g180474; PIDN:AAA35683.1; !1PID:g180475 !'##note this sequence represents the translation of an activated !1oncogene with a transversion mutation REFERENCE I57624 !$#authors Honkawa, H.; Masahashi, W.; Hashimoto, S.; Hashimoto-Gotoh, !1T. !$#journal Mol. Cell. Biol. (1987) 7:2933-2940 !$#title Identification of the principal promoter sequence of the !1c-H-ras transforming oncogene: deletion analysis of the !15'-flanking region by focus formation assay. !$#cross-references MUID:88038834; PMID:3670300 !$#accession I57624 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-11,'V',13-16 ##label HON !'##cross-references GB:M17232; NID:g180531; PIDN:AAA35685.1; !1PID:g180533 !'##note this sequence represents the translation of an activated !1oncogene REFERENCE I59121 !$#authors Stevens, C.W.; Manoharan, T.H.; Fahl, W.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:3875-3879 !$#title Characterization of mutagen-activated cellular oncogenes !1that confer anchorage independence to human fibroblasts and !1tumorigenicity to NIH 3T3 cells: sequence analysis of an !1enzymatically amplified mutant HRAS allele. !$#cross-references MUID:88234524; PMID:3131765 !$#accession I59121 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-30 ##label STE !'##cross-references GB:M19990; NID:g184387; PIDN:AAA52693.1; !1PID:g465130 REFERENCE S34768 !$#authors Loew, A.; Sprinzl, M.; Faulhammer, H.G. !$#journal Eur. J. Biochem. (1993) 215:473-479 !$#title Affinity labeling of c-H-ras p21 consensus elements with !1periodate-oxidized GDP and GTP. !$#cross-references MUID:93345536; PMID:8393791 !$#accession S34768 !'##molecule_type protein !'##residues 108-117;132-153 ##label LOE !'##note peptides labeled by cross-linking to activated GTP analogs REFERENCE S07800 !$#authors Tadokoro, K.; Ueda, M.; Ohshima, T.; Fujita, K.; Rikimaru, !1K.; Takahashi, N.; Enomoto, S.; Tsuchida, N. !$#journal Oncogene (1989) 4:499-505 !$#title Activation of oncogenes in human oral cancer cells: a novel !1codon 13 mutation of c-H-ras-1 and concurrent amplifications !1of c-erbB-1 and c-myc. !$#cross-references MUID:89239477; PMID:2654810 !$#accession S07800 !'##molecule_type DNA !'##residues 1-12,'R',14-37 ##label TAD !'##cross-references EMBL:X16438; NID:g29944; PIDN:CAA34461.1; !1PID:g29945 !'##experimental_source oral carcinoma !'##note the authors translated the codon TAC for residue 32 as Thr !'##note this sequence represents the translation of an activated !1oncogene with point mutations REFERENCE I38148 !$#authors Hirai, H.; Kobayashi, Y.; Mano, H.; Hagiwara, K.; Maru, Y.; !1Omine, M.; Mizoguchi, H.; Nishida, J.; Takaku, F. !$#journal Nature (1987) 327:430-432 !$#title A point mutation at codon 13 of the N-ras oncogene in !1myelodysplastic syndrome. !$#cross-references MUID:87229039; PMID:3295562 !$#accession I38148 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-12,'R',14-37 ##label RES !'##cross-references EMBL:X05564; NID:g35890; PIDN:CAA29078.1; !1PID:g35891 !'##note this sequence represents the translation of an activated !1oncogene with point mutations REFERENCE I51857 !$#authors Imamura, N.; Kuramoto, A.; Ishihara, H.; Shimizu, S. !$#journal Am. J. Hematol. (1993) 43:151-153 !$#title Detection of high incidence of H-RAS oncogene point !1mutations in acute myelogenous leukemia. !$#cross-references MUID:93343137; PMID:7916576 !$#accession I51857 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-4,'N',6-9,'APA',13-14,'A',16-37 ##label RE2 !'##cross-references GB:S64238; NID:g402829; PIDN:AAD13952.1; !1PID:g4261652 !'##note this sequence represents the translation of an activated !1oncogene with point mutations REFERENCE A51570 !$#authors Krengel, U.; Scheffzek, K.; Scherer, A.; Kabsch, W.; !1Wittinghofer, A.; Pai, E.F. !$#submission submitted to the Brookhaven Protein Data Bank, June 1991 !$#cross-references PDB:121P !$#contents annotation; X-ray crystallography, 1.54 angstroms, residues !11-166 REFERENCE A58854 !$#authors Pai, E.F.; Krengel, U.; Petsko, G.A.; Goody, R.S.; Kabsch, !1W.; Wittinghofer, A. !$#journal EMBO J. (1990) 9:2351-2359 !$#title Refined crystal structure of the triphosphate conformation !1of H-ras p21 at 1.35 angstroms resolution: implications for !1the mechanism of GTP hydrolysis. !$#cross-references MUID:90316087; PMID:2196171 !$#contents annotation; X-ray crystallography, 1.35 angstroms COMMENT Ras transforming proteins are guanine nucleotide binding !1proteins that couple cell-surface receptors to intracellular !1signalling pathways involved in cell poliferation and !1differentiation. GENETICS !$#gene GDB:HRAS; H-ras !'##cross-references GDB:120684; OMIM:190020 !$#map_position 11p15.5-11p15.5 !$#introns 37/3; 97/2; 150/3 CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS GTP binding; hydrolase; lipoprotein; membrane protein; !1methylated carboxyl end; nucleotide binding; P-loop; !1prenylated cysteine; proto-oncogene; thiolester bond; !1transforming protein FEATURE !$4-119 #domain translation elongation factor Tu homology !8#label ETU\ !$10-17 #region nucleotide-binding motif A (P-loop)\ !$25-40 #region switch 1 region\ !$57-75 #region switch 2 region\ !$116-119 #region GTP-binding NKXD motif\ !$145-147 #region GTP-binding SAK motif\ !$16,17,35,116,117, !$119,145 #binding_site Mg-GTP (Lys, Ser, Thr, Asn, Lys, Asp, !8Ser) #status experimental\ !$181,184 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$186 #binding_site farnesyl (Cys) (covalent) #status !8predicted\ !$186 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted SUMMARY #length 189 #molecular-weight 21298 #checksum 2608 SEQUENCE /// ENTRY TVMVB #type complete TITLE transforming protein H-ras - BALB murine sarcoma virus ORGANISM #formal_name BALB murine sarcoma virus DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 19-Jan-2001 ACCESSIONS A01361 REFERENCE A01361 !$#authors Reddy, E.P.; Lipman, D.; Andersen, P.R.; Tronick, S.R.; !1Aaronson, S.A. !$#journal J. Virol. (1985) 53:984-987 !$#title Nucleotide sequence analysis of the BALB/c murine sarcoma !1virus transforming gene. !$#cross-references MUID:85135050; PMID:2983103 !$#accession A01361 !'##molecule_type DNA !'##residues 1-189 ##label RED !'##cross-references GB:M10035; NID:g332199; PIDN:AAA46575.1; !1PID:g332200 !'##note the authors translated the codon GAG for residues 31 and 63 as !1Gly GENETICS !$#gene H-ras CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS GTP binding; lipoprotein; membrane protein; methylated !1carboxyl end; nucleotide binding; P-loop; prenylated !1cysteine; thiolester bond; transforming protein FEATURE !$4-119 #domain translation elongation factor Tu homology !8#label ETU\ !$10-17 #region nucleotide-binding motif A (P-loop)\ !$116-119 #region GTP-binding NKXD motif\ !$145-147 #region GTP-binding SAK/L motif\ !$16,17,35,116,117, !$119,145 #binding_site Mg-GTP (Lys, Ser, Thr, Asn, Lys, Asp, !8Ser) #status predicted\ !$181,184 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$186 #binding_site farnesyl (Cys) (covalent) #status !8predicted\ !$186 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted SUMMARY #length 189 #molecular-weight 21368 #checksum 2830 SEQUENCE /// ENTRY TVCHRS #type complete TITLE transforming protein H-ras-1 - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 19-Jan-2001 ACCESSIONS A24617 REFERENCE A24617 !$#authors Westaway, D.; Papkoff, J.; Moscovici, C.; Varmus, H.E. !$#journal EMBO J. (1986) 5:301-309 !$#title Identification of a provirally activated c-Ha-ras oncogene !1in an avian nephroblastoma via a novel procedure: cDNA !1cloning of a chimaeric viral-host transcript. !$#cross-references MUID:86220108; PMID:3011401 !$#accession A24617 !'##molecule_type mRNA !'##residues 1-189 ##label WES !'##cross-references GB:X03578; NID:g63506; PIDN:CAA27258.1; PID:g63507 GENETICS !$#gene H-ras-1 CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS GTP binding; lipoprotein; membrane protein; methylated !1carboxyl end; nucleotide binding; P-loop; prenylated !1cysteine; transforming protein FEATURE !$4-119 #domain translation elongation factor Tu homology !8#label ETU\ !$10-17 #region nucleotide-binding motif A (P-loop)\ !$116-119 #region GTP-binding NKXD motif\ !$145-147 #region GTP-binding SAK/L motif\ !$16,17,35,116,117, !$119,145 #binding_site Mg-GTP (Lys, Ser, Thr, Asn, Lys, Asp, !8Ser) #status predicted\ !$186 #binding_site farnesyl (Cys) (covalent) #status !8predicted\ !$186 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted SUMMARY #length 189 #molecular-weight 21365 #checksum 2615 SEQUENCE /// ENTRY TVMVRS #type complete TITLE transforming protein p29 (ras) - Rasheed rat sarcoma virus ORGANISM #formal_name Rasheed rat sarcoma virus DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 19-Jan-2001 ACCESSIONS A01362 REFERENCE A01362 !$#authors Rasheed, S.; Norman, G.L.; Heidecker, G. !$#journal Science (1983) 221:155-157 !$#title Nucleotide sequence of the Rasheed rat sarcoma virus !1oncogene: new mutations. !$#cross-references MUID:83223613; PMID:6344220 !$#accession A01362 !'##molecule_type DNA !'##residues 1-248 ##label RAS !'##cross-references GB:J02294; NID:g333963; PIDN:AAA47420.1; !1PID:g333964 GENETICS !$#gene ras CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS glycoprotein; GTP binding; lipoprotein; membrane protein; !1methylated carboxyl end; nucleotide binding; P-loop; !1prenylated cysteine; thiolester bond; transforming protein FEATURE !$63-178 #domain translation elongation factor Tu homology !8#label ETU\ !$69-76 #region nucleotide-binding motif A (P-loop)\ !$175-178 #region GTP-binding NKXD motif\ !$204-206 #region GTP-binding SAK/L motif\ !$75,76,94,175,176, !$178,204 #binding_site Mg-GTP (Lys, Ser, Thr, Asn, Lys, Asp, !8Ser) #status predicted\ !$144 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$240,243 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$245 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted\ !$245 #binding_site farnesyl (Cys) (covalent) #status !8predicted SUMMARY #length 248 #molecular-weight 27424 #checksum 137 SEQUENCE /// ENTRY TVMV3H #type complete TITLE transforming protein H-ras - Harvey murine sarcoma virus ORGANISM #formal_name Harvey murine sarcoma virus DATE 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 19-Jan-2001 ACCESSIONS A01363 REFERENCE A01363 !$#authors Dhar, R.; Ellis, R.W.; Shih, T.Y.; Oroszlan, S.; Shapiro, !1B.; Maizel, J.; Lowy, D.; Scolnick, E. !$#journal Science (1982) 217:934-937 !$#title Nucleotide sequence of the p21 transforming protein of !1Harvey murine sarcoma virus. !$#cross-references MUID:82277118; PMID:6287572 !$#accession A01363 !'##molecule_type genomic RNA !'##residues 1-241 ##label DHA !'##cross-references GB:M24154; NID:g332184; PIDN:AAA46568.1; !1PID:g332185; GB:J02207; NID:g332187; PID:g332188 COMMENT Residues 14 and 53 are two potential initiators that would !1produce proteins p29 (residues 14-241) and p21 (residues !153-241), respectively. Studies of transformed cells have !1indicated that p21 is the transforming protein. COMMENT Gene H-ras is also known as has and has/bas-1. GENETICS !$#gene H-ras CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS glycoprotein; GTP binding; lipoprotein; membrane protein; !1methylated carboxyl end; nucleotide binding; P-loop; !1prenylated cysteine; thiolester bond; transforming protein FEATURE !$56-171 #domain translation elongation factor Tu homology !8#label ETU\ !$62-69 #region nucleotide-binding motif A (P-loop)\ !$168-171 #region GTP-binding NKXD motif\ !$197-199 #region GTP-binding SAK/L motif\ !$68,69,87,168,169, !$171,197 #binding_site Mg-GTP (Lys, Ser, Thr, Asn, Lys, Asp, !8Ser) #status predicted\ !$137 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$233,236 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$238 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted\ !$238 #binding_site farnesyl (Cys) (covalent) #status !8predicted SUMMARY #length 241 #molecular-weight 26328 #checksum 8457 SEQUENCE /// ENTRY TVMVNS #type complete TITLE transforming protein ras - NS.C58 murine sarcoma virus ALTERNATE_NAMES p21 transforming protein ORGANISM #formal_name NS.C58 murine sarcoma virus DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 19-Jan-2001 ACCESSIONS A27839 REFERENCE A27839 !$#authors Fredrickson, T.N.; O'Neill, R.R.; Rutledge, R.A.; Theodore, !1T.S.; Martin, M.A.; Ruscetti, S.K.; Austin, J.B.; Hartley, !1J.W. !$#journal J. Virol. (1987) 61:2109-2119 !$#title Biologic and molecular characterization of two newly !1isolated ras-containing murine leukemia viruses. !$#cross-references MUID:87226391; PMID:3035212 !$#accession A27839 !'##molecule_type DNA !'##residues 1-189 ##label FRE !'##cross-references GB:M30733; NID:g332197; PIDN:AAA46574.1; !1PID:g332198 GENETICS !$#gene ras CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS GTP binding; lipoprotein; membrane protein; methylated !1carboxyl end; nucleotide binding; P-loop; prenylated !1cysteine; thiolester bond; transforming protein FEATURE !$4-119 #domain translation elongation factor Tu homology !8#label ETU\ !$10-17 #region nucleotide-binding motif A (P-loop)\ !$116-119 #region GTP-binding NKXD motif\ !$145-147 #region GTP-binding SAK/L motif\ !$16,17,35,116,117, !$119,145 #binding_site Mg-GTP (Lys, Ser, Thr, Asn, Lys, Asp, !8Ser) #status predicted\ !$181,184 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$186 #binding_site farnesyl (Cys) (covalent) #status !8predicted\ !$186 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted SUMMARY #length 189 #molecular-weight 21397 #checksum 2740 SEQUENCE /// ENTRY TVHU2K #type complete TITLE transforming protein K-ras-2, major splice form - human ALTERNATE_NAMES c-K-ras protein; c-Ki-ras protein; c-Kirsten-ras protein; p21 protein; PR310 c-K-ras oncogene ORGANISM #formal_name Homo sapiens #common_name man DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 19-Jan-2001 ACCESSIONS B93311; B93310; I59498; I52205; I51971; A01367 REFERENCE A93311 !$#authors McGrath, J.P.; Capon, D.J.; Smith, D.H.; Chen, E.Y.; !1Seeburg, P.H.; Goeddel, D.V.; Levinson, A.D. !$#journal Nature (1983) 304:501-506 !$#title Structure and organization of the human Ki-ras !1proto-oncogene and a related processed pseudogene. !$#cross-references MUID:83271513; PMID:6308466 !$#accession B93311 !'##molecule_type DNA !'##residues 1-188 ##label MCG !'##cross-references GB:L00045; GB:L00046; GB:L00047; GB:L00049; !1NID:g190907; PIDN:AAB59444.1; PID:g190910 REFERENCE A93310 !$#authors Shimizu, K.; Birnbaum, D.; Ruley, M.A.; Fasano, O.; Suard, !1Y.; Edlund, L.; Taparowsky, E.; Goldfarb, M.; Wigler, M. !$#journal Nature (1983) 304:497-500 !$#title Structure of the Ki-ras gene of the human lung carcinoma !1cell line Calu-1. !$#cross-references MUID:83271512; PMID:6308465 !$#accession B93310 !'##molecule_type DNA !'##residues 1-11,'C',13-30,'G',32-188 ##label SHI !'##cross-references GB:L00049; GB:K00652; GB:K00653; NID:g190907 REFERENCE I59498 !$#authors Santos, E.; Martin-Zanca, D.; Reddy, E.P.; Pierotti, M.A.; !1Della Porta, G.; Barbacid, M. !$#journal Science (1984) 223:661-664 !$#title Malignant activation of a K-ras oncogene in lung carcinoma !1but not in normal tissue of the same patient. !$#cross-references MUID:84121280; PMID:6695174 !$#accession I59498 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-36 ##label SAN !'##cross-references GB:M34904; NID:g186765; PIDN:AAA36149.1; !1PID:g553520 REFERENCE I52205 !$#authors Hirai, H.; Okabe, T.; Anraku, Y.; Fujisawa, M.; Urabe, A.; !1Takaku, F. !$#journal Biochem. Biophys. Res. Commun. (1985) 127:168-174 !$#title Activation of the c-K-ras oncogene in a human pancreas !1carcimoma. !$#cross-references MUID:85149400; PMID:3855240 !$#accession I52205 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-60,'H',62-96 ##label HIR !'##cross-references GB:K03210; NID:g190899; PIDN:AAA36554.1; !1PID:g553635 !'##note the sequence with a point mutation found in T3M-4 primary !1pancreatic exocrine adenocarcinoma cells REFERENCE I51971 !$#authors Kahn, S.; Yamamoto, F. !$#journal Anticancer Res. (1987) 7:639-652 !$#title The c-K-ras gene and human cancer (review). !$#cross-references MUID:88022525; PMID:3310850 !$#accession I51971 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-11,'C',13-188 ##label KAH !'##cross-references GB:M54968; NID:g1815608; PIDN:AAB41942.1; !1PID:g186764 COMMENT This splice form, approximately 99% of the transcripts in !1colon carcinoma SW480 cells, uses exon 4b. For the !1alternative splice form, see PIR:TVHUK. GENETICS !$#gene GDB:KRAS2; K-ras !'##cross-references GDB:120120; OMIM:190070 !$#map_position 12p12.1-12p12.1 !$#introns 37/3; 97/2; 150/3 !$#note the first intron occurs before the initiator codon CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS alternative splicing; GTP binding; lipoprotein; membrane !1protein; methylated carboxyl end; nucleotide binding; !1P-loop; prenylated cysteine; proto-oncogene; transforming !1protein FEATURE !$4-119 #domain translation elongation factor Tu homology !8#label ETU\ !$10-17 #region nucleotide-binding motif A (P-loop)\ !$116-119 #region GTP-binding NKXD motif\ !$145-147 #region GTP-binding SAK/L motif\ !$16,17,35,116,117, !$119,145 #binding_site Mg-GTP (Lys, Ser, Thr, Asn, Lys, Asp, !8Ser) #status predicted\ !$185 #binding_site farnesyl (Cys) (covalent) #status !8predicted\ !$185 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted SUMMARY #length 188 #molecular-weight 21424 #checksum 80 SEQUENCE /// ENTRY TVHUK #type complete TITLE transforming protein K-ras-2, minor splice form - human ALTERNATE_NAMES c-K-ras protein; c-Ki-ras protein; c-Kirsten-ras protein; transforming protein K-ras-1 [misnomer] ORGANISM #formal_name Homo sapiens #common_name man DATE 18-Apr-1984 #sequence_revision 18-Apr-1984 #text_change 19-Jan-2001 ACCESSIONS A93311; A93310; A93312; A01364 REFERENCE A93311 !$#authors McGrath, J.P.; Capon, D.J.; Smith, D.H.; Chen, E.Y.; !1Seeburg, P.H.; Goeddel, D.V.; Levinson, A.D. !$#journal Nature (1983) 304:501-506 !$#title Structure and organization of the human Ki-ras !1proto-oncogene and a related processed pseudogene. !$#cross-references MUID:83271513; PMID:6308466 !$#accession A93311 !'##molecule_type DNA !'##residues 1-189 ##label MCG !'##cross-references GB:L00045; GB:L00046; GB:L00047; GB:L00048; !1NID:g190906; PIDN:AAB59445.1; PID:g190909 REFERENCE A93310 !$#authors Shimizu, K.; Birnbaum, D.; Ruley, M.A.; Fasano, O.; Suard, !1Y.; Edlund, L.; Taparowsky, E.; Goldfarb, M.; Wigler, M. !$#journal Nature (1983) 304:497-500 !$#title Structure of the Ki-ras gene of the human lung carcinoma !1cell line Calu-1. !$#cross-references MUID:83271512; PMID:6308465 !$#accession A93310 !'##molecule_type DNA !'##residues 1-11,'C',13-30,'G',32-189 ##label SHI !'##cross-references GB:L00048; GB:K00652; GB:K00653; NID:g190906 !'##experimental_source lung carcinoma cell REFERENCE A93312 !$#authors Capon, D.J.; Seeburg, P.H.; McGrath, J.P.; Hayflick, J.S.; !1Edman, U.; Levinson, A.D.; Goeddel, D.V. !$#journal Nature (1983) 304:507-513 !$#title Activation of Ki-ras 2 gene in human colon and lung !1carcinomas by two different point mutations. !$#cross-references MUID:83271514; PMID:6308467 !$#accession A93312 !'##molecule_type DNA !'##residues 1-11,'C',13-189 ##label CAP !'##cross-references GB:L00048; GB:K00652; GB:K00653; NID:g190906 !'##experimental_source lung and colon carcinoma cells !'##note colon carcinoma SW480 cell sequence differs from that shown in !1having 12-Val COMMENT This splice form, approximately 1% of the transcripts in !1colon carcinoma SW480 cells, uses exon 4a. For the !1alternative splice form, see PIR:TVHU2K. COMMENT The name transforming protein K-ras-1 is a misnomer. That !1name properly refers to a processed pseudogene. GENETICS !$#gene GDB:KRAS2 !'##cross-references GDB:120120; OMIM:190070 !$#map_position 12p12.1-12p12.1 !$#introns 37/3; 97/2; 150/3 !$#note the first intron occurs before the initiator codon CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS alternative splicing; GTP binding; lipoprotein; membrane !1protein; methylated carboxyl end; nucleotide binding; !1P-loop; prenylated cysteine; proto-oncogene; thiolester !1bond; transforming protein FEATURE !$4-119 #domain translation elongation factor Tu homology !8#label ETU\ !$10-17 #region nucleotide-binding motif A (P-loop)\ !$116-119 #region GTP-binding NKXD motif\ !$145-147 #region GTP-binding SAK/L motif\ !$16,17,35,116,117, !$119,145 #binding_site Mg-GTP (Lys, Ser, Thr, Asn, Lys, Asp, !8Ser) #status predicted\ !$180 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$186 #binding_site farnesyl (Cys) (covalent) #status !8predicted\ !$186 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted SUMMARY #length 189 #molecular-weight 21656 #checksum 2803 SEQUENCE /// ENTRY TVMS2K #type complete TITLE transforming protein K-ras, splice form 2 - mouse ALTERNATE_NAMES c-Ki-ras transforming protein ORGANISM #formal_name Mus musculus #common_name house mouse DATE 04-Dec-1986 #sequence_revision 09-Apr-1998 #text_change 19-Jan-2001 ACCESSIONS B01365; I59500; A46134; I48307 REFERENCE A01365 !$#authors George, D.L.; Scott, A.F.; Trusko, S.; Glick, B.; Ford, E.; !1Dorney, D.J. !$#journal EMBO J. (1985) 4:1199-1203 !$#title Structure and expression of amplified cKi-ras gene sequences !1in Y1 mouse adrenal tumor cells. !$#cross-references MUID:85230570; PMID:4006913 !$#accession B01365 !'##molecule_type DNA !'##residues 1-188 ##label GEO !'##cross-references GB:X02452; NID:g52798; PIDN:CAA26295.1; !1PID:g1213018 !'##experimental_source adrenal tumor Y1 REFERENCE I59500 !$#authors Guerrero, I.; Villasante, A.; Corces, V.; Pellicer, A. !$#journal Science (1984) 225:1159-1162 !$#title Activation of a c-K-ras oncogene by somatic mutation in !1mouse lymphomas induced by gamma radiation. !$#cross-references MUID:84300296; PMID:6474169 !$#accession I59500 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-37 ##label GUE !'##cross-references GB:K01927; NID:g200673; PIDN:AAA40037.1; !1PID:g200674 REFERENCE A46134 !$#authors You, M.; Wang, Y.; Stoner, G.; You, L.; Maronpot, R.; !1Reynolds, S.H.; Anderson, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:5804-5808 !$#title Parental bias of Ki-ras oncogenes detected in lung tumors !1from mouse hybrids. !$#cross-references MUID:92335186; PMID:1352876 !$#accession A46134 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-37 ##label YOU !'##cross-references GB:S39586; NID:g251108 !'##experimental_source strains C3A and AC3 F1 !'##note the parental inbred strains, C3H/HeJ and A/J, are both Mus !1musculus REFERENCE I48307 !$#authors George, D.L.; Scott, A.F.; de Martinville, B.; Francke, U. !$#journal Nucleic Acids Res. (1984) 12:2731-2743 !$#title Amplified DNA in Y1 mouse adrenal tumor cells: isolation of !1cDNAs complementary to an amplified c-Ki-ras gene and !1localization of homologous sequences to mouse chromosome 6. !$#cross-references MUID:84169569; PMID:6546797 !$#accession I48307 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 109-173 ##label RES !'##cross-references EMBL:X00485; NID:g50546; PIDN:CAA25160.1; !1PID:g929681 GENETICS !$#gene K-ras; Ki-ras !$#introns 37/3; 97/2; 150/3 !$#note this gene is amplified in adrenal tumor Y1 cells CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS alternative splicing; GTP binding; lipoprotein; membrane !1protein; methylated carboxyl end; nucleotide binding; !1oncogene; P-loop; prenylated cysteine; transforming protein FEATURE !$4-119 #domain translation elongation factor Tu homology !8#label ETU\ !$10-17 #region nucleotide-binding motif A (P-loop)\ !$116-119 #region GTP-binding NKXD motif\ !$145-147 #region GTP-binding SAK/L motif\ !$16,17,35,116,117, !$119,145 #binding_site Mg-GTP (Lys, Ser, Thr, Asn, Lys, Asp, !8Ser) #status predicted\ !$185 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted\ !$185 #binding_site farnesyl (Cys) (covalent) #status !8predicted SUMMARY #length 188 #molecular-weight 21482 #checksum 444 SEQUENCE /// ENTRY TVMSK #type complete TITLE transforming protein K-ras, splice form 1 - mouse ALTERNATE_NAMES c-Ki-ras transforming protein ORGANISM #formal_name Mus musculus #common_name house mouse DATE 04-Dec-1986 #sequence_revision 09-Apr-1998 #text_change 19-Jan-2001 ACCESSIONS A01365; I48293 REFERENCE A01365 !$#authors George, D.L.; Scott, A.F.; Trusko, S.; Glick, B.; Ford, E.; !1Dorney, D.J. !$#journal EMBO J. (1985) 4:1199-1203 !$#title Structure and expression of amplified cKi-ras gene sequences !1in Y1 mouse adrenal tumor cells. !$#cross-references MUID:85230570; PMID:4006913 !$#accession A01365 !'##molecule_type DNA !'##residues 1-189 ##label GEO !'##cross-references GB:X02455; NID:g52804 !'##experimental_source adrenal tumor Y1 REFERENCE I48293 !$#authors Trusko, S.P.; Hoffman, E.K.; George, D.L. !$#journal Nucleic Acids Res. (1989) 17:9259-9265 !$#title Transcriptional activation of cKi-ras proto-oncogene !1resulting from retroviral promoter insertion. !$#cross-references MUID:90067925; PMID:2555789 !$#accession I48293 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-7 ##label RES !'##cross-references EMBL:X15888; NID:g50415; PIDN:CAA33898.1; !1PID:g581942 GENETICS !$#gene K-ras !$#introns 37/3; 97/2; 150/3 !$#note this gene is amplified in adrenal tumor Y1 cells CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS alternative splicing; GTP binding; lipoprotein; membrane !1protein; methylated carboxyl end; nucleotide binding; !1oncogene; P-loop; prenylated cysteine; thiolester bond; !1transforming protein FEATURE !$4-119 #domain translation elongation factor Tu homology !8#label ETU\ !$10-17 #region nucleotide-binding motif A (P-loop)\ !$116-119 #region GTP-binding NKXD motif\ !$145-147 #region GTP-binding SAK/L motif\ !$16,17,35,116,117, !$119,145 #binding_site Mg-GTP (Lys, Ser, Thr, Asn, Lys, Asp, !8Ser) #status predicted\ !$180 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$186 #binding_site farnesyl (Cys) (covalent) #status !8predicted\ !$186 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted SUMMARY #length 189 #molecular-weight 21656 #checksum 3029 SEQUENCE /// ENTRY TVMV2K #type complete TITLE transforming protein K-ras-1 - Kirsten murine sarcoma virus ORGANISM #formal_name Kirsten murine sarcoma virus DATE 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 19-Jan-2001 ACCESSIONS A01366 REFERENCE A01366 !$#authors Tsuchida, N.; Ryder, T.; Ohtsubo, E. !$#journal Science (1982) 217:937-939 !$#title Nucleotide sequence of the oncogene encoding the p21 !1transforming protein of Kirsten murine sarcoma virus. !$#cross-references MUID:82277119; PMID:6287573 !$#accession A01366 !'##molecule_type genomic RNA !'##residues 1-189 ##label TSU !'##cross-references GB:J02228; NID:g332192; PIDN:AAA46572.1; !1PID:g332193 COMMENT Gene K-ras is also known as kis. GENETICS !$#gene K-ras CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS glycoprotein; GTP binding; lipoprotein; membrane protein; !1methylated carboxyl end; nucleotide binding; P-loop; !1prenylated cysteine; thiolester bond; transforming protein FEATURE !$4-119 #domain translation elongation factor Tu homology !8#label ETU\ !$10-17 #region nucleotide-binding motif A (P-loop)\ !$116-119 #region GTP-binding NKXD motif\ !$145-147 #region GTP-binding SAK/L motif\ !$16,17,35,116,117, !$119,145 #binding_site Mg-GTP (Lys, Ser, Thr, Asn, Lys, Asp, !8Ser) #status predicted\ !$85 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$180 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$186 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted\ !$186 #binding_site farnesyl (Cys) (covalent) #status !8predicted SUMMARY #length 189 #molecular-weight 21715 #checksum 3784 SEQUENCE /// ENTRY TVBYR1 #type complete TITLE GTP-binding protein RAS1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein O3205; protein YOR101w; protein YOR3205w; transforming protein homolog H-ras-1 ORGANISM #formal_name Saccharomyces cerevisiae DATE 03-Aug-1984 #sequence_revision 12-Apr-1996 #text_change 19-Jan-2001 ACCESSIONS S61661; A01368; S14171; S62143; S66986 REFERENCE S61643 !$#authors Benes, V.; Andrade, M.A.; Rechmann, S.; Teodoru, C.; !1Banrevi, A.; Sander, C.; Valencia, A.; Ansorge, W.; Voss, H. !$#submission submitted to the EMBL Data Library, December 1995 !$#description Nucleotide sequence and analysis of a 130 kb fragment of !1yeast chromosome XV. !$#accession S61661 !'##molecule_type DNA !'##residues 1-309 ##label BEN !'##cross-references EMBL:X94335; NID:g1262139; PIDN:CAA64023.1; !1PID:g1164948 REFERENCE A01368 !$#authors Powers, S.; Kataoka, T.; Fasano, O.; Goldfarb, M.; !1Strathern, J.; Broach, J.; Wigler, M. !$#journal Cell (1984) 36:607-612 !$#title Genes in S. cerevisiae encoding proteins with domains !1homologous to the mammalian ras proteins. !$#cross-references MUID:84130171; PMID:6365329 !$#accession A01368 !'##molecule_type DNA !'##residues 1-203,'I',205-309 ##label POW !'##cross-references GB:K01970; NID:g172360; PIDN:AAA34958.1; !1PID:g172361 !'##note the authors translated the codon GAA for residue 38 as Gly and !1TCT for residue 301 as Tyr REFERENCE S05732 !$#authors Dhar, R.; Nieto, A.; Koller, R.; DeFeo-Jones, D.; Scolnick, !1E.M. !$#journal Nucleic Acids Res. (1984) 12:3611-3618 !$#title Nucleotide sequence of two ras(H) related-genes isolated !1from the yeast Saccharomyces cerevisiae. !$#cross-references MUID:84221383; PMID:6328429 !$#accession S14171 !'##molecule_type DNA !'##residues 1-309 ##label DHA !'##cross-references EMBL:X00527; NID:g4288; PIDN:CAA25206.1; PID:g4289 REFERENCE S62142 !$#authors Silberstein, S.; Collins, P.G.; Kelleher, D.J.; Gilmore, R. !$#journal J. Cell Biol. (1995) 131:371-383 !$#title The essential OST2 gene encodes the 16-kD subunit of the !1yeast oligosaccharyltransferase, a highly conserved protein !1expressed in diverse eukaryotic organisms. !$#cross-references MUID:96017708; PMID:7593165 !$#accession S62143 !'##status translation not shown !'##molecule_type DNA !'##residues 245-309 ##label SIL !'##cross-references EMBL:U32307; NID:g1041719; PIDN:AAC49087.1; !1PID:g1041721 REFERENCE S66965 !$#authors Voss, H.; Benes, V.; Rechmann, S.; Teodoru, C.; Schwager, !1C.; Paces, V.; Ansorge, W. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S66986 !'##molecule_type DNA !'##residues 1-309 ##label VOS !'##cross-references EMBL:Z75009; NID:g1420280; PIDN:CAA99298.1; !1PID:g1420281; GSPDB:GN00015; MIPS:YOR101w !'##experimental_source strain S288C GENETICS !$#gene SGD:RAS1; MIPS:YOR101w !'##cross-references SGD:S0005627; MIPS:YOR101w !$#map_position 15R CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS GTP binding; lipoprotein; membrane protein; nucleotide !1binding; P-loop; prenylated cysteine; thiolester bond FEATURE !$11-126 #domain translation elongation factor Tu homology !8#label ETU\ !$17-24 #region nucleotide-binding motif A (P-loop)\ !$123-126 #region GTP-binding NKXD motif\ !$153-155 #region GTP-binding SAK/L motif\ !$23,24,42,123,124, !$126,153 #binding_site Mg-GTP (Lys, Ser, Thr, Asn, Lys, Asp, !8Ser) #status predicted\ !$305 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$306 #binding_site farnesyl (Cys) (covalent) #status !8predicted SUMMARY #length 309 #molecular-weight 34346 #checksum 1809 SEQUENCE /// ENTRY TVBYR2 #type complete TITLE GTP-binding protein RAS2 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein N2198; protein YNL098c; transforming protein homolog H-ras-2 ORGANISM #formal_name Saccharomyces cerevisiae DATE 03-Aug-1984 #sequence_revision 23-Feb-1996 #text_change 19-Jan-2001 ACCESSIONS S58254; A01369; S05732; S63038; S63956 REFERENCE S58246 !$#authors Saiz, J.E.; Buitrago, M.J.; Soler, A.; del Rey, F.; !1Revuelta, J.L. !$#submission submitted to the EMBL Data Library, July 1995 !$#description The sequence of a 21.3 kb fragment from the left arm of !1yeast chromosome XIV reveals LEU4, MET4, POL1, RAS2 and four !1new open reading frames. !$#accession S58254 !'##molecule_type DNA !'##residues 1-322 ##label SAI !'##cross-references EMBL:Z50161; NID:g929846; PIDN:CAA90528.1; !1PID:g929855 REFERENCE A01368 !$#authors Powers, S.; Kataoka, T.; Fasano, O.; Goldfarb, M.; !1Strathern, J.; Broach, J.; Wigler, M. !$#journal Cell (1984) 36:607-612 !$#title Genes in S. cerevisiae encoding proteins with domains !1homologous to the mammalian ras proteins. !$#cross-references MUID:84130171; PMID:6365329 !$#accession A01369 !'##molecule_type DNA !'##residues 1-254,'V',256-322 ##label POW !'##cross-references GB:K01971; NID:g172362; PIDN:AAA34959.1; !1PID:g172363 !'##note the authors translated the codon CTG for residue 100 as Ser REFERENCE S05732 !$#authors Dhar, R.; Nieto, A.; Koller, R.; DeFeo-Jones, D.; Scolnick, !1E.M. !$#journal Nucleic Acids Res. (1984) 12:3611-3618 !$#title Nucleotide sequence of two ras(H) related-genes isolated !1from the yeast Saccharomyces cerevisiae. !$#cross-references MUID:84221383; PMID:6328429 !$#accession S05732 !'##molecule_type DNA !'##residues 1-107,'P',109-209,'L',211-297,'SK',300-322 ##label DHA !'##cross-references EMBL:X00528; NID:g4290; PIDN:CAA25207.1; PID:g4291 !'##note the authors translated the codon CTG for residue 100 as Ser REFERENCE A44327 !$#authors Kuroda, Y.; Suzuki, N.; Kataoka, T. !$#journal Science (1993) 259:683-686 !$#title The effect of posttranslational modifications on the !1interaction of Ras2 with adenylyl cyclase. !$#cross-references MUID:93157832; PMID:8430318 !$#contents annotation REFERENCE S63037 !$#authors Saiz, J.E.; Buitrago, M.J.; Soler-Mira, A.; Del Rey, F.; !1Revuelta, J.L. !$#submission submitted to the Protein Sequence Database, April 1996 !$#accession S63038 !'##molecule_type DNA !'##residues 1-322 ##label SAW !'##cross-references EMBL:Z71374; NID:g1302007; PIDN:CAA95974.1; !1PID:g1302008; GSPDB:GN00014; MIPS:YNL098c !'##experimental_source strain S288C REFERENCE S63948 !$#authors Saiz, J.E.; Buitrago, M.J.; Soler-Mira, A.; del Rey, F.; !1Revuelta, J.L. !$#journal Yeast (1996) 12:403-409 !$#title The sequence of a 21.3 kb DNA fragment from the left arm of !1yeast chromosome XIV reveals LEU4, MET4, POL1, RAS2, and six !1new open reading frames. !$#cross-references MUID:96267765; PMID:8701612 !$#accession S63956 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-322 ##label SAF !'##cross-references EMBL:Z50161; NID:g929846; PIDN:CAA90528.1; !1PID:g929855 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1995 GENETICS !$#gene SGD:RAS2; CTN5; GLC5; MIPS:YNL098c !'##cross-references SGD:S0005042; MIPS:YNL098c !$#map_position 14L CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS GTP binding; lipoprotein; membrane protein; methylated !1carboxyl end; nucleotide binding; P-loop; prenylated !1cysteine; thiolester bond FEATURE !$1-319 #product GTP-binding protein RAS2 #status predicted !8#label MAT\ !$11-126 #domain translation elongation factor Tu homology !8#label ETU\ !$17-24 #region nucleotide-binding motif A (P-loop)\ !$123-126 #region GTP-binding NKXD motif\ !$153-155 #region GTP-binding SAK/L motif\ !$23,24,42,123,124, !$126,153 #binding_site Mg-GTP (Lys, Ser, Thr, Asn, Lys, Asp, !8Ser) #status predicted\ !$318 #binding_site palmitate (Cys) (covalent) #status !8experimental\ !$319 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status experimental\ !$319 #binding_site farnesyl (Cys) (covalent) #status !8experimental SUMMARY #length 322 #molecular-weight 34705 #checksum 1543 SEQUENCE /// ENTRY TVBYPR #type complete TITLE ras-like protein 1 - fission yeast (Schizosaccharomyces pombe) ORGANISM #formal_name Schizosaccharomyces pombe DATE 31-Dec-1988 #sequence_revision 01-Dec-2000 #text_change 19-Jan-2001 ACCESSIONS T37875; A25820 REFERENCE Z21751 !$#authors Skelton, J.; Churcher, C.M.; Barrell, B.G.; Rajandream, !1M.A.; Wood, V. !$#submission submitted to the EMBL Data Library, August 1997 !$#accession T37875 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-219 ##label SKE !'##cross-references EMBL:Z98597; PIDN:CAB11218.1; GSPDB:GN00066; !1SPDB:SPAC17H9.09c !'##experimental_source strain 972h-; cosmid c17H9 REFERENCE A25820 !$#authors Nadin-Davis, S.A.; Yang, R.C.A.; Narang, S.A.; Nasim, A. !$#journal J. Mol. Evol. (1986) 23:41-51 !$#title The cloning and characterization of a RAS gene from !1Schizosaccharomyces pombe. !$#cross-references MUID:86200236; PMID:3084798 !$#accession A25820 !'##molecule_type DNA !'##residues 'M',7-219 ##label NAD !'##cross-references GB:X03771; NID:g5035; PIDN:CAA27399.1; PID:g5036 GENETICS !$#gene SPDB:SPAC17H9.09c; ras !$#map_position 1 !$#introns 2/3; 7/2 CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS GTP binding; lipoprotein; membrane protein; methylated !1carboxyl end; nucleotide binding; P-loop; prenylated !1cysteine; thiolester bond; transforming protein FEATURE !$9-124 #domain translation elongation factor Tu homology !8#label ETU\ !$15-22 #region nucleotide-binding motif A (P-loop)\ !$121-124 #region GTP-binding NKXD motif\ !$151-153 #region GTP-binding SAK/L motif\ !$21,22,40,121,122, !$124,151 #binding_site Mg-GTP (Lys, Ser, Thr, Asn, Lys, Asp, !8Ser) #status predicted\ !$215 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$216 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted\ !$216 #binding_site farnesyl (Cys) (covalent) #status !8predicted SUMMARY #length 219 #molecular-weight 24734 #checksum 8699 SEQUENCE /// ENTRY TVBYSR #type complete TITLE transforming protein ras - fission yeast (Schizosaccharomyces pombe) (strain JY282) ORGANISM #formal_name Schizosaccharomyces pombe DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 19-Jan-2001 ACCESSIONS A22715 REFERENCE A22715 !$#authors Fukui, Y.; Kaziro, Y. !$#journal EMBO J. (1985) 4:687-691 !$#title Molecular cloning and sequence analysis of a ras gene from !1Schizosaccharomyces pombe. !$#cross-references MUID:85230537; PMID:4006903 !$#accession A22715 !'##molecule_type DNA !'##residues 1-219 ##label FUK !'##note the authors translated the codon TTC for residue 11 as Leu, GTT !1for residue 57 as Leu, CTA for residue 60 as Val, CAG for !1residue 81 as Glu, CGC for residue 136 as Gly, and CAT for !1residue 181 as Gln GENETICS !$#gene ras !$#introns 2/3 CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS GTP binding; lipoprotein; membrane protein; methylated !1carboxyl end; nucleotide binding; P-loop; prenylated !1cysteine; thiolester bond; transforming protein FEATURE !$9-124 #domain translation elongation factor Tu homology !8#label ETU\ !$15-22 #region nucleotide-binding motif A (P-loop)\ !$121-124 #region GTP-binding NKXD motif\ !$151-153 #region GTP-binding SAK/L motif\ !$21,22,40,121,122, !$124,151 #binding_site Mg-GTP (Lys, Ser, Thr, Asn, Lys, Asp, !8Ser) #status predicted\ !$215 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$216 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted\ !$216 #binding_site farnesyl (Cys) (covalent) #status !8predicted SUMMARY #length 219 #molecular-weight 24972 #checksum 9766 SEQUENCE /// ENTRY TVWYRS #type complete TITLE transforming protein ras - shiitake mushroom ORGANISM #formal_name Lentinula edodes #common_name shiitake mushroom DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 19-Jan-2001 ACCESSIONS JS0619; JQ1296 REFERENCE JQ1296 !$#authors Hori, K.; Kajiwara, S.; Saito, T.; Miyazawa, H.; Katayose, !1Y.; Shishido, K. !$#journal Gene (1991) 105:91-96 !$#title Cloning, sequence analysis and transcriptional expression of !1a ras gene of the edible basidiomycete Lentinus edodes. !$#cross-references MUID:92039023; PMID:1937010 !$#accession JS0619 !'##molecule_type DNA !'##residues 1-217 ##label HOR !'##cross-references GB:D00742; NID:g217947; PIDN:BAA00642.1; !1PID:g217948 !'##note the source was designated as Lentinus edodes GENETICS !$#gene ras !$#introns 4/3; 20/1; 45/1; 72/2; 137/1; 176/3 CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS GTP binding; lipoprotein; membrane protein; methylated !1carboxyl end; nucleotide binding; P-loop; prenylated !1cysteine; transforming protein FEATURE !$11-126 #domain translation elongation factor Tu homology !8#label ETU\ !$17-24 #region nucleotide-binding motif A (P-loop)\ !$123-126 #region GTP-binding NKXD motif\ !$153-155 #region GTP-binding SAK/L motif\ !$23,24,42,123,124, !$126,153 #binding_site Mg-GTP (Lys, Ser, Thr, Asn, Lys, Asp, !8Ser) #status predicted\ !$214 #binding_site geranyl-geranyl (Cys) (covalent) !8#status predicted\ !$214 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted SUMMARY #length 217 #molecular-weight 24007 #checksum 8227 SEQUENCE /// ENTRY TVFFR #type complete TITLE transforming protein homolog ras-64B - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 19-Jan-2001 ACCESSIONS A01370; B29048 REFERENCE A01370 !$#authors Mozer, B.; Marlor, R.; Parkhurst, S.; Corces, V. !$#journal Mol. Cell. Biol. (1985) 5:885-889 !$#title Characterization and developmental expression of a !1Drosophila ras oncogene. !$#cross-references MUID:85187987; PMID:3921827 !$#accession A01370 !'##molecule_type DNA !'##residues 1-195 ##label MOZ !'##cross-references GB:M10804; NID:g158217; PIDN:AAA99202.1; !1PID:g158219 REFERENCE A29048 !$#authors Brock, H.W. !$#journal Gene (1987) 51:129-137 !$#title Sequence and genomic structure of ras homologues Dmras85D !1and Dmras64B of Drosophila melanogaster. !$#cross-references MUID:87248071; PMID:3110012 !$#accession B29048 !'##molecule_type DNA !'##residues 1-195 ##label BRO !'##cross-references GB:M16431; NID:g158212; PIDN:AAA28849.1; !1PID:g158214 GENETICS !$#gene ras-64B !'##cross-references FlyBase:FBgn0003206 !$#introns 27/3; 50/3 CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS GTP binding; lipoprotein; membrane protein; methylated !1carboxyl end; nucleotide binding; P-loop; prenylated !1cysteine; transforming protein FEATURE !$6-124 #domain translation elongation factor Tu homology !8#label ETU\ !$12-19 #region nucleotide-binding motif A (P-loop)\ !$121-124 #region GTP-binding NKXD motif\ !$151-153 #region GTP-binding SAK/L motif\ !$18,19,37,121,122, !$124,151 #binding_site Mg-GTP (Lys, Ser, Thr, Asn, Lys, Asp, !8Ser) #status predicted\ !$192 #binding_site farnesyl (Cys) (covalent) #status !8predicted\ !$192 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted SUMMARY #length 195 #molecular-weight 22726 #checksum 9578 SEQUENCE /// ENTRY TVFF85 #type complete TITLE transforming protein homolog ras-85D - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 19-Jan-2001 ACCESSIONS A29048 REFERENCE A29048 !$#authors Brock, H.W. !$#journal Gene (1987) 51:129-137 !$#title Sequence and genomic structure of ras homologues Dmras85D !1and Dmras64B of Drosophila melanogaster. !$#cross-references MUID:87248071; PMID:3110012 !$#accession A29048 !'##molecule_type DNA !'##residues 1-189 ##label BRO !'##cross-references GB:M16429; NID:g158203; PIDN:AAA28847.1; !1PID:g158205 !'##note the author translated the codon GCA for residue 155 as Pro GENETICS !$#gene ras-85D !'##cross-references FlyBase:FBgn0003205 !$#introns 47/1; 132/3 CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS GTP binding; lipoprotein; membrane protein; methylated !1carboxyl end; nucleotide binding; P-loop; prenylated !1cysteine; transforming protein FEATURE !$4-119 #domain translation elongation factor Tu homology !8#label ETU\ !$10-17 #region nucleotide-binding motif A (P-loop)\ !$116-119 #region GTP-binding NKXD motif\ !$145-147 #region GTP-binding SAK/L motif\ !$16,17,35,116,117, !$119,145 #binding_site Mg-GTP (Lys, Ser, Thr, Asn, Lys, Asp, !8Ser) #status predicted\ !$186 #binding_site geranyl-geranyl (Cys) (covalent) !8#status predicted\ !$186 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted SUMMARY #length 189 #molecular-weight 21594 #checksum 455 SEQUENCE /// ENTRY TVHURR #type complete TITLE transforming protein R-ras - human ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 19-Jan-2001 ACCESSIONS A26159 REFERENCE A26159 !$#authors Lowe, D.G.; Capon, D.J.; Delwart, E.; Sakaguchi, A.Y.; !1Naylor, S.L.; Goeddel, D.V. !$#journal Cell (1987) 48:137-146 !$#title Structure of the human and murine R-ras genes, novel genes !1closely related to ras proto-oncogenes. !$#cross-references MUID:87078390; PMID:3098437 !$#accession A26159 !'##molecule_type DNA !'##residues 1-218 ##label LOW !'##cross-references GB:M14949; NID:g190934; PIDN:AAA60256.1; !1PID:g190936 GENETICS !$#gene GDB:RRAS !'##cross-references GDB:120356; OMIM:165090 !$#map_position 19q13.3-19qter !$#introns 51/3; 81/1; 115/2; 151/3; 191/2 CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS GTP binding; lipoprotein; membrane protein; methylated !1carboxyl end; nucleotide binding; P-loop; prenylated !1cysteine; transforming protein FEATURE !$30-145 #domain translation elongation factor Tu homology !8#label ETU\ !$36-43 #region nucleotide-binding motif A (P-loop)\ !$142-145 #region GTP-binding NKXD motif\ !$172-174 #region GTP-binding SAK/L motif\ !$42,43,61,142,143, !$145,172 #binding_site Mg-GTP (Lys, Ser, Thr, Asn, Lys, Asp, !8Ser) #status predicted\ !$215 #binding_site geranyl-geranyl (Cys) (covalent) !8#status predicted\ !$215 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted SUMMARY #length 218 #molecular-weight 23480 #checksum 1140 SEQUENCE /// ENTRY TVHUC2 #type complete TITLE GTP-binding protein RAS/TC21 - human ALTERNATE_NAMES transforming protein RAS/TC21 ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 19-Jan-2001 ACCESSIONS B34788 REFERENCE A34788 !$#authors Drivas, G.T.; Shih, A.; Coutavas, E.; Rush, M.G.; !1D'Eustachio, P. !$#journal Mol. Cell. Biol. (1990) 10:1793-1798 !$#title Characterization of four novel ras-like genes expressed in a !1human teratocarcinoma cell line. !$#cross-references MUID:90205863; PMID:2108320 !$#accession B34788 !'##molecule_type mRNA !'##residues 1-203 ##label DRI !'##cross-references GB:M31468; NID:g190876; PIDN:AAA36545.1; !1PID:g190877 GENETICS !$#gene GDB:TC21 !'##cross-references GDB:5573831; OMIM:600098 !$#map_position 7q34-7q35 CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS GTP binding; lipoprotein; membrane protein; methylated !1carboxyl end; nucleotide binding; P-loop; prenylated !1cysteine; transforming protein FEATURE !$14-129 #domain translation elongation factor Tu homology !8#label ETU\ !$20-27 #region nucleotide-binding motif A (P-loop)\ !$126-129 #region GTP-binding NKXD motif\ !$156-158 #region GTP-binding SAK/L motif\ !$26,27,45,126,127, !$129,156 #binding_site Mg-GTP (Lys, Ser, Thr, Asn, Lys, Asp, !8Ser) #status predicted\ !$200 #binding_site geranyl-geranyl (Cys) (covalent) !8#status predicted\ !$200 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted SUMMARY #length 203 #molecular-weight 23294 #checksum 9420 SEQUENCE /// ENTRY TVDORS #type complete TITLE transforming protein ras - slime mold (Dictyostelium discoideum) ORGANISM #formal_name Dictyostelium discoideum DATE 13-Aug-1986 #sequence_revision 13-Aug-1986 #text_change 19-Jan-2001 ACCESSIONS A01371 REFERENCE A01371 !$#authors Reymond, C.D.; Gomer, R.H.; Mehdy, M.C.; Firtel, R.A. !$#journal Cell (1984) 39:141-148 !$#title Developmental regulation of a Dictyostelium gene encoding a !1protein homologous to mammalian ras protein. !$#cross-references MUID:85024887; PMID:6091907 !$#accession A01371 !'##molecule_type DNA !'##residues 1-186 ##label REY !'##cross-references GB:K02114; NID:g167864; PIDN:AAA33243.1; !1PID:g167865 GENETICS !$#gene ras !$#introns 25/3; 30/1; 47/1 CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS GTP binding; lipoprotein; membrane protein; methylated !1carboxyl end; nucleotide binding; P-loop; prenylated !1cysteine; proto-oncogene; transforming protein FEATURE !$4-119 #domain translation elongation factor Tu homology !8#label ETU\ !$10-17 #region nucleotide-binding motif A (P-loop)\ !$116-119 #region GTP-binding NKXD motif\ !$145-147 #region GTP-binding SAK/L motif\ !$16,17,35,116,117, !$119,145 #binding_site Mg-GTP (Lys, Ser, Thr, Asn, Lys, Asp, !8Ser) #status predicted\ !$183 #binding_site geranyl-geranyl (Cys) (covalent) !8#status predicted\ !$183 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted SUMMARY #length 186 #molecular-weight 21092 #checksum 6804 SEQUENCE /// ENTRY TVDORA #type complete TITLE transforming protein rasG - slime mold (Dictyostelium discoideum) ORGANISM #formal_name Dictyostelium discoideum DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 19-Jan-2001 ACCESSIONS A31456; S21090; S22129 REFERENCE A31456 !$#authors Robbins, S.M.; Williams, J.G.; Jermyn, K.A.; Spiegelman, !1G.B.; Weeks, G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:938-942 !$#title Growing and developing Dictyostelium cells express different !1ras genes. !$#cross-references MUID:89128893; PMID:2644652 !$#accession A31456 !'##molecule_type mRNA !'##residues 1-189 ##label ROB1 !'##cross-references GB:J04160; NID:g167866; PIDN:AAA33244.1; !1PID:g167867 REFERENCE S21090 !$#authors Robbins, S.M.; Williams, J.G.; Spiegelman, G.B.; Weeks, G. !$#journal Biochim. Biophys. Acta (1992) 1130:85-89 !$#title Cloning and characterization of the Dictyostelium discoideum !1rasG genomic sequences. !$#cross-references MUID:92182019; PMID:1339294 !$#accession S21090 !'##status translation not shown !'##molecule_type DNA !'##residues 1-189 ##label ROB2 !'##cross-references EMBL:Z11533; NID:g7342; PIDN:CAA77632.1; PID:g7343 GENETICS !$#gene rasG !$#introns 25/3 CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS GTP binding; lipoprotein; membrane protein; methylated !1carboxyl end; nucleotide binding; P-loop; prenylated !1cysteine; transforming protein FEATURE !$4-119 #domain translation elongation factor Tu homology !8#label ETU\ !$10-17 #region nucleotide-binding motif A (P-loop)\ !$116-119 #region GTP-binding NKXD motif\ !$146-148 #region GTP-binding SAK/L motif\ !$16,17,35,116,117, !$119,146 #binding_site Mg-GTP (Lys, Ser, Thr, Asn, Lys, Asp, !8Ser) #status predicted\ !$186 #binding_site geranyl-geranyl (Cys) (covalent) !8#status predicted\ !$186 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted SUMMARY #length 189 #molecular-weight 21333 #checksum 669 SEQUENCE /// ENTRY TVHUR2 #type complete TITLE transforming protein rap2b - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 19-Jan-2001 ACCESSIONS A33121; A36039 REFERENCE A33121 !$#authors Farrell, F.X.; Ohmstede, C.A.; Reep, B.R.; Lapetina, E.G. !$#journal Nucleic Acids Res. (1990) 18:4281 !$#title cDNA sequence of a new ras-related gene (rap2b) isolated !1from human platelets with sequence homology to rap2. !$#cross-references MUID:90332453; PMID:2115998 !$#accession A33121 !'##molecule_type mRNA !'##residues 1-183 ##label FAR !'##cross-references GB:X52987; NID:g35862; PIDN:CAA37178.1; PID:g35863 !'##note the authors translated the codon UUC for residue 90 as Ser REFERENCE A36039 !$#authors Ohmstede, C.A.; Farrell, F.X.; Reep, B.R.; Clemetson, K.J.; !1Lapetina, E.G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:6527-6531 !$#title RAP2B: a RAS-related GTP-binding protein from platelets. !$#cross-references MUID:90370818; PMID:2118648 !$#accession A36039 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type mRNA !'##residues 1-89,'S',91-183 ##label OHM GENETICS !$#gene GDB:RAP2B !'##cross-references GDB:126960; OMIM:179541 !$#map_position 13q34-13q34 CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS GTP binding; lipoprotein; methylated carboxyl end; !1nucleotide binding; P-loop; prenylated cysteine; !1transforming protein FEATURE !$2-180 #product transforming protein rap2b #status predicted !8#label MAT\ !$4-119 #domain translation elongation factor Tu homology !8#label ETU\ !$10-17 #region nucleotide-binding motif A (P-loop)\ !$116-119 #region GTP-binding NKXD motif\ !$146-148 #region GTP-binding SAK/L motif\ !$16,17,35,116,117, !$119,146 #binding_site Mg-GTP (Lys, Ser, Thr, Asn, Lys, Asp, !8Ser) #status predicted\ !$180 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted\ !$180 #binding_site geranyl-geranyl (Cys) (covalent) !8#status predicted SUMMARY #length 183 #molecular-weight 20494 #checksum 6421 SEQUENCE /// ENTRY TVHUR1 #type complete TITLE transforming protein rap1b [validated] - human ALTERNATE_NAMES GTP-binding protein G-22K ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 19-Jan-2001 ACCESSIONS S01952; S15829; A35421; A31777; T12553 REFERENCE S01952 !$#authors Pizon, V.; Lerosey, I.; Chardin, P.; Tavitian, A. !$#journal Nucleic Acids Res. (1988) 16:7719 !$#title Nucleotide sequence of a human cDNA encoding a ras-related !1protein (rap1B). !$#cross-references MUID:88319957; PMID:3137530 !$#accession S01952 !'##molecule_type mRNA !'##residues 1-184 ##label PIZ !'##cross-references EMBL:X08004; NID:g35872; PIDN:CAB46488.1; !1PID:g5419893 REFERENCE S15829 !$#authors Fischer, T.H.; Collins, J.H.; Gatling, M.N.; White II, G.C. !$#journal FEBS Lett. (1991) 283:173-176 !$#title The localization of the cAMP-dependent protein kinase !1phosphorylation site in the platelet rat protein, rap 1B. !$#cross-references MUID:91257295; PMID:1904369 !$#accession S15829 !'##molecule_type protein !'##residues 'XX',3-25,'X',27-29,'X',31-36;177-180 ##label FIS REFERENCE A35421 !$#authors Siess, W.; Winegar, D.A.; Lapetina, E.G. !$#journal Biochem. Biophys. Res. Commun. (1990) 170:944-950 !$#title RAP1-B is phosphorylated by protein kinase A in intact human !1platelets. !$#cross-references MUID:90343822; PMID:1696481 !$#accession A35421 !'##status preliminary !'##molecule_type protein !'##residues 146-180 ##label SIE REFERENCE A31777 !$#authors Bokoch, G.M.; Parkos, C.A.; Mumby, S.M. !$#journal J. Biol. Chem. (1988) 263:16744-16749 !$#title Purification and characterization of the 22,000-Dalton !1GTP-binding protein substrate for ADP-ribosylation by !1botulinum toxin, G-22K. !$#cross-references MUID:89034164; PMID:3141412 !$#accession A31777 !'##molecule_type protein !'##residues 1-35 ##label BOK REFERENCE Z17527 !$#authors Ansorge, W.; Wirkner, U.; Mewes, H.W.; Gassenhuber, J.; !1Wiemann, S. !$#submission submitted to the Protein Sequence Database, June 1999 !$#accession T12553 !'##status preliminary !'##molecule_type mRNA !'##residues 1-184 ##label ANS !'##cross-references EMBL:AL080212 !'##experimental_source adult uterus; clone DKFZp586H0723 GENETICS !$#gene GDB:RAP1B !'##cross-references GDB:120336; OMIM:179530 !$#map_position 12q14-12q14 !$#note DKFZp586H0723.1 CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS GTP binding; lipoprotein; membrane protein; methylated !1carboxyl end; nucleotide binding; P-loop; phosphoprotein; !1prenylated cysteine; transforming protein FEATURE !$1-181 #product transforming protein rap1b #status !8experimental #label MAT\ !$4-119 #domain translation elongation factor Tu homology !8#label ETU\ !$10-17 #region nucleotide-binding motif A (P-loop)\ !$116-119 #region GTP-binding NKXD motif\ !$147-149 #region GTP-binding SAK/L motif\ !$16,17,35,116,117, !$119,147 #binding_site Mg-GTP (Lys, Ser, Thr, Asn, Lys, Asp, !8Ser) #status predicted\ !$39 #modified_site ADP-ribosylserine (Ser) (by botulinum !8exoenzyme C3) #status predicted\ !$181 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted\ !$181 #binding_site geranyl-geranyl (Cys) (covalent) !8#status predicted SUMMARY #length 184 #molecular-weight 20825 #checksum 7714 SEQUENCE /// ENTRY A34655 #type complete TITLE transforming protein rap1b - bovine ALTERNATE_NAMES GTP-binding protein smg p21B ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 06-Jul-1990 #sequence_revision 05-Apr-1995 #text_change 19-Jan-2001 ACCESSIONS A34655; B60346 REFERENCE A34655 !$#authors Matsui, Y.; Kikuchi, A.; Kawata, M.; Kondo, J.; Teranishi, !1Y.; Takai, Y. !$#journal Biochem. Biophys. Res. Commun. (1990) 166:1010-1016 !$#title Molecular cloning of smg p21B and identification of smg p21 !1purified from bovine brain and human platelets as smg p21B. !$#cross-references MUID:90147747; PMID:2105724 !$#accession A34655 !'##molecule_type mRNA !'##residues 1-184 ##label MAT !'##cross-references GB:M33141; NID:g163721; PIDN:AAA30763.1; !1PID:g163722 REFERENCE A60346 !$#authors Kawata, M.; Kawahara, Y.; Sunako, M.; Araki, S.; Koide, M.; !1Tsuda, T.; Fukuzaki, H.; Takai, Y. !$#journal Oncogene (1991) 6:841-848 !$#title The molecular heterogeneity of the smg-21/Krev-1/rap1 !1proteins, a GTP-binding protein having the same effector !1domain as ras p21s, in bovine aortic smooth muscle !1membranes. !$#cross-references MUID:91270903; PMID:1646988 !$#accession B60346 !'##molecule_type protein !'##residues 130-140;169-174 ##label KAW CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS GTP binding; lipoprotein; membrane protein; methylated !1carboxyl end; nucleotide binding; P-loop; phosphoprotein; !1prenylated cysteine; transforming protein FEATURE !$1-181 #product transforming protein rap1b #status predicted !8#label MTR\ !$4-119 #domain translation elongation factor Tu homology !8#label ETU\ !$10-17 #region nucleotide-binding motif A (P-loop)\ !$116-119 #region GTP-binding NKXD motif\ !$147-149 #region GTP-binding SAK/L motif\ !$16,17,35,116,117, !$119,147 #binding_site Mg-GTP (Lys, Ser, Thr, Asn, Lys, Asp, !8Ser) #status predicted\ !$16 #binding_site ATP (Lys) #status predicted\ !$181 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted\ !$181 #binding_site geranyl-geranyl (Cys) (covalent) !8#status predicted SUMMARY #length 184 #molecular-weight 20825 #checksum 7714 SEQUENCE /// ENTRY A31961 #type complete TITLE transforming protein rap1A - bovine ALTERNATE_NAMES GTP-binding protein smg p21A ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Mar-1990 #sequence_revision 05-Apr-1995 #text_change 19-Jan-2001 ACCESSIONS A31961; A60346 REFERENCE A31961 !$#authors Kawata, M.; Matsui, Y.; Kondo, J.; Hishida, T.; Teranishi, !1Y.; Takai, Y. !$#journal J. Biol. Chem. (1988) 263:18965-18971 !$#title A novel small molecular weight GTP-binding protein with the !1same putative effector domain as the ras proteins in bovine !1brain membranes. Purification, determination of primary !1structure, and characterization. !$#cross-references MUID:89066693; PMID:3143720 !$#accession A31961 !'##molecule_type mRNA !'##residues 1-184 ##label KAW !'##cross-references GB:J04196; NID:g162757; PIDN:AAA30415.1; !1PID:g162758 REFERENCE A60346 !$#authors Kawata, M.; Kawahara, Y.; Sunako, M.; Araki, S.; Koide, M.; !1Tsuda, T.; Fukuzaki, H.; Takai, Y. !$#journal Oncogene (1991) 6:841-848 !$#title The molecular heterogeneity of the smg-21/Krev-1/rap1 !1proteins, a GTP-binding protein having the same effector !1domain as ras p21s, in bovine aortic smooth muscle !1membranes. !$#cross-references MUID:91270903; PMID:1646988 !$#accession A60346 !'##molecule_type protein !'##residues 130-138,'X',140,'X',142-145;169-173 ##label KA2 CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS GTP binding; lipoprotein; membrane protein; methylated !1carboxyl end; nucleotide binding; P-loop; prenylated !1cysteine; transforming protein FEATURE !$4-119 #domain translation elongation factor Tu homology !8#label ETU\ !$10-17 #region nucleotide-binding motif A (P-loop)\ !$116-119 #region GTP-binding NKXD motif\ !$147-149 #region GTP-binding SAK/L motif\ !$16,17,35,116,117, !$119,147 #binding_site Mg-GTP (Lys, Ser, Thr, Asn, Lys, Asp, !8Ser) #status predicted\ !$16 #binding_site ATP (Lys) #status predicted\ !$181 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted\ !$181 #binding_site geranyl-geranyl (Cys) (covalent) !8#status predicted SUMMARY #length 184 #molecular-weight 20987 #checksum 7493 SEQUENCE /// ENTRY TVFFR3 #type complete TITLE transforming protein ras3 - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES transforming protein, 21K ORGANISM #formal_name Drosophila melanogaster DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 19-Jan-2001 ACCESSIONS S07187 REFERENCE S07187 !$#authors Schejter, E.D.; Shilo, B.Z. !$#journal EMBO J. (1985) 4:407-412 !$#title Characterization of functional domains of p21 ras by use of !1chimeric genes. !$#cross-references MUID:85257468; PMID:3926484 !$#accession S07187 !'##molecule_type DNA !'##residues 1-182 ##label SCH !'##cross-references EMBL:X02200; NID:g8407; PIDN:CAA26131.1; PID:g8408 GENETICS !$#gene ras3 !'##cross-references FlyBase:FBgn0004636 !$#map_position 62B CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS GTP binding; lipoprotein; membrane protein; methylated !1carboxyl end; nucleotide binding; P-loop; prenylated !1cysteine; transforming protein FEATURE !$1-179 #product transforming protein ras3 #status predicted !8#label MAT\ !$4-118 #domain translation elongation factor Tu homology !8#label ETU\ !$10-17 #region nucleotide-binding motif A (P-loop)\ !$115-118 #region GTP-binding NKXD motif\ !$145-147 #region GTP-binding SAK/L motif\ !$16,17,35,115,116, !$118,145 #binding_site Mg-GTP (Lys, Ser, Thr, Asn, Lys, Asp, !8Ser) #status predicted\ !$179 #binding_site geranyl-geranyl (Cys) (covalent) !8#status predicted\ !$179 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted SUMMARY #length 182 #molecular-weight 21030 #checksum 666 SEQUENCE /// ENTRY TVCJRA #type complete TITLE transforming protein ral - cotton-top tamarin ORGANISM #formal_name Saguinus oedipus #common_name cotton-top tamarin DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 19-Jan-2001 ACCESSIONS A25261; A24893 REFERENCE A91050 !$#authors Chardin, P.; Tavitian, A. !$#journal EMBO J. (1986) 5:2203-2208 !$#title The ral gene: a new ras related gene isolated by the use of !1a synthetic probe. !$#cross-references MUID:87053859; PMID:3023062 !$#accession A25261 !'##molecule_type mRNA !'##residues 1-206 ##label CHA !'##cross-references EMBL:X04328; NID:g38256; PIDN:CAA27859.1; !1PID:g38257 GENETICS !$#gene ral CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS GTP binding; lipoprotein; membrane protein; methylated !1carboxyl end; nucleotide binding; P-loop; prenylated !1cysteine; proto-oncogene; transforming protein FEATURE !$15-130 #domain translation elongation factor Tu homology !8#label ETU\ !$21-28 #region nucleotide-binding motif A (P-loop)\ !$127-130 #region GTP-binding NKXD motif\ !$157-159 #region GTP-binding SAK/L motif\ !$27,28,46,127,128, !$130,157 #binding_site Mg-GTP (Lys, Ser, Thr, Asn, Lys, Asp, !8Ser) #status predicted\ !$203 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted\ !$203 #binding_site geranyl-geranyl (Cys) (covalent) !8#status predicted SUMMARY #length 206 #molecular-weight 23553 #checksum 4767 SEQUENCE /// ENTRY TVHUAA #type complete TITLE transforming protein ralA - human ALTERNATE_NAMES GTP-binding protein ral ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 19-Jan-2001 ACCESSIONS S04596; A34387 REFERENCE S04596 !$#authors Chardin, P.; Tavitian, A. !$#journal Nucleic Acids Res. (1989) 17:4380 !$#title Coding sequences of human ralA and ralB cDNAs. !$#cross-references MUID:89296492; PMID:2662142 !$#accession S04596 !'##molecule_type mRNA !'##residues 1-206 ##label CHA !'##cross-references GB:X15014; NID:g35845; PIDN:CAA33118.1; PID:g35846 REFERENCE A34387 !$#authors Polakis, P.G.; Weber, R.F.; Nevins, B.; Didsbury, J.R.; !1Evans, T.; Snyderman, R. !$#journal J. Biol. Chem. (1989) 264:16383-16389 !$#title Identification of the ral and rac1 gene products, low !1molecular mass GTP-binding proteins from human platelets. !$#cross-references MUID:89380251; PMID:2550440 !$#accession A34387 !'##molecule_type mRNA !'##residues 1,'VDYL',3-206 ##label POL !'##cross-references GB:M29893; NID:g190849; PIDN:AAA36542.1; !1PID:g190850 !'##note parts of this sequence were confirmed by peptide sequencing GENETICS !$#gene GDB:RALA !'##cross-references GDB:120723; OMIM:179550 !$#map_position 7pter-7cen CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS GTP binding; lipoprotein; membrane protein; methylated !1carboxyl end; nucleotide binding; P-loop; prenylated !1cysteine; proto-oncogene; transforming protein FEATURE !$15-130 #domain translation elongation factor Tu homology !8#label ETU\ !$21-28 #region nucleotide-binding motif A (P-loop)\ !$127-130 #region GTP-binding NKXD motif\ !$157-159 #region GTP-binding SAK/L motif\ !$27,28,46,127,128, !$130,157 #binding_site Mg-GTP (Lys, Ser, Thr, Asn, Lys, Asp, !8Ser) #status predicted\ !$203 #binding_site geranyl-geranyl (Cys) (covalent) !8#status predicted\ !$203 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted SUMMARY #length 206 #molecular-weight 23567 #checksum 4800 SEQUENCE /// ENTRY TVHUAB #type complete TITLE transforming protein ralB - human ALTERNATE_NAMES GTP-binding protein ralB ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 19-Jan-2001 ACCESSIONS S04597; A43973 REFERENCE S04596 !$#authors Chardin, P.; Tavitian, A. !$#journal Nucleic Acids Res. (1989) 17:4380 !$#title Coding sequences of human ralA and ralB cDNAs. !$#cross-references MUID:89296492; PMID:2662142 !$#accession S04597 !'##molecule_type mRNA !'##residues 1-206 ##label CHA !'##cross-references GB:X15015; NID:g35847; PIDN:CAA33119.1; PID:g35848 REFERENCE A43973 !$#authors Hsieh, C.L.; Swaroop, A.; Francke, U. !$#journal Somat. Cell Mol. Genet. (1990) 16:407-410 !$#title Chromosomal localization and cDNA sequence of human ralB, a !1GTP binding protein. !$#cross-references MUID:91019694; PMID:2120779 !$#accession A43973 !'##molecule_type mRNA !'##residues 1-206 ##label HSI !'##cross-references EMBL:M35416; NID:g190851; PIDN:AAA60250.1; !1PID:g190852 GENETICS !$#gene GDB:RALB !'##cross-references GDB:125273; OMIM:179551 !$#map_position 2cen-2q13 CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS GTP binding; lipoprotein; membrane protein; methylated !1carboxyl end; nucleotide binding; P-loop; prenylated !1cysteine; proto-oncogene; transforming protein FEATURE !$15-131 #domain translation elongation factor Tu homology !8#label ETU\ !$21-28 #region nucleotide-binding motif A (P-loop)\ !$128-131 #region GTP-binding NKXD motif\ !$158-160 #region GTP-binding SAK/L motif\ !$27,28,46,128,129, !$131,158 #binding_site Mg-GTP (Lys, Ser, Thr, Asn, Lys, Asp, !8Ser) #status predicted\ !$203 #binding_site geranyl-geranyl (Cys) (covalent) !8#status predicted\ !$203 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted SUMMARY #length 206 #molecular-weight 23408 #checksum 5912 SEQUENCE /// ENTRY RGECGT #type complete TITLE GTP-binding protein era - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Sep-1988 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS S44713; E65034; A25927 REFERENCE S44713 !$#authors Sood, P.; Lerner, C.G.; Shimamoto, T.; Lu, Q.; Inouye, M. !$#journal Mol. Microbiol. (1994) 12:201-208 !$#title Characterization of the autophosphorylation of Era, an !1essential Escherichia coli GTPase. !$#cross-references MUID:94335640; PMID:8057845 !$#accession S44713 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-301 ##label SOO !'##cross-references EMBL:M14658; NID:g416294; PIDN:AAA03242.1; !1PID:g416295 !'##note this is a revision to the sequence from reference A25927 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65034 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-301 ##label BLAT !'##cross-references GB:AE000343; GB:U00096; NID:g2367139; !1PIDN:AAC75619.1; PID:g1788919; UWGP:b2566 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A25927 !$#authors Ahnn, J.; March, P.E.; Takiff, H.E.; Inouye, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:8849-8853 !$#title A GTP-binding protein of Escherichia coli has homology to !1yeast RAS proteins. !$#cross-references MUID:87067411; PMID:3097637 !$#accession A25927 !'##molecule_type DNA !'##residues 1-289,'AHCAVSVTLTIFKSNSDGRLAARICPA' ##label AHN GENETICS !$#gene era CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS autophosphorylation; GTP binding; nucleotide binding; !1P-loop; phosphoprotein FEATURE !$9-127 #domain translation elongation factor Tu homology !8#label ETU\ !$15-22 #region nucleotide-binding motif A (P-loop)\ !$124-127 #region GTP-binding NKXD motif\ !$155-157 #region GTP-binding SAL/K motif #status atypical SUMMARY #length 301 #molecular-weight 33810 #checksum 1182 SEQUENCE /// ENTRY TVBYQ4 #type complete TITLE GTP-binding protein SEC4 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein F002; protein YFL005w ORGANISM #formal_name Saccharomyces cerevisiae DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 19-Jan-2001 ACCESSIONS A25959; S56249; S62289; S61732 REFERENCE A25959 !$#authors Salminen, A.; Novick, P.J. !$#journal Cell (1987) 49:527-538 !$#title A ras-like protein is required for a post-Golgi event in !1yeast secretion. !$#cross-references MUID:87187650; PMID:3552249 !$#accession A25959 !'##molecule_type DNA !'##residues 1-215 ##label SAL !'##cross-references EMBL:M16507; NID:g172565; PIDN:AAA35032.1; !1PID:g172566 !'##note the authors translated the codon CGT for residue 91 as Thr REFERENCE S56186 !$#authors Murakami, Y.; Naitou, M.; Hagiwara, H.; Shibata, T.; Ozawa, !1M.; Sasanuma, S.I.; Sasanuma, M.; Tsuchiya, Y.; Soeda, E.; !1Yokoyama, K.; Yamazaki, M.; Tashiro, H.; Eki, T. !$#submission submitted to the EMBL Data Library, May 1995 !$#description Analysis of the nucleotide sequence of chromosome VI from !1Saccaromyces cerevisiae. !$#accession S56249 !'##molecule_type DNA !'##residues 1-215 ##label MUR !'##cross-references EMBL:D50617; NID:g836685; PIDN:BAA09233.1; !1PID:g836749; GSPDB:GN00006; MIPS:YFL005w REFERENCE S62230 !$#authors Murakami, Y. !$#submission submitted to the EMBL Data Library, December 1994 !$#accession S62289 !'##molecule_type DNA !'##residues 1-215 ##label MUW !'##cross-references EMBL:D44604; NID:g870821; PIDN:BAA08071.1; !1PID:g870823 REFERENCE S61731 !$#authors Naitou, M.; Ozawa, M.; Sasanuma, S.; Kobayashi, M.; !1Hagiwara, H.; Shibata, T.; Hanaoka, F.; Watanabe, K.; Ono, !1A.; Yamazaki, M.; Tashiro, H.; Eki, T.; Murakami, Y. !$#journal Yeast (1996) 12:77-84 !$#title Sequencing of a 23 kb fragment from Saccharomyces cerevisiae !1chromosome VI. !$#cross-references MUID:96381249; PMID:8789262 !$#accession S61732 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-215 ##label NAI !'##cross-references EMBL:D44604; NID:g870821; PIDN:BAA08071.1; !1PID:g870823 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1994 GENETICS !$#gene SGD:SEC4; MIPS:YFL005w !'##cross-references SGD:S0001889; MIPS:YFL005w !$#map_position 6L CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS GTP binding; lipoprotein; membrane protein; membrane !1trafficking; nucleotide binding; P-loop; prenylated cysteine FEATURE !$21-136 #domain translation elongation factor Tu homology !8#label ETU\ !$27-34 #region nucleotide-binding motif A (P-loop)\ !$133-136 #region GTP-binding NKXD motif\ !$162-164 #region GTP-binding SAK/L motif\ !$214,215 #binding_site geranyl-geranyl (Cys) (covalent) !8#status predicted SUMMARY #length 215 #molecular-weight 23506 #checksum 2046 SEQUENCE /// ENTRY TVHUC1 #type complete TITLE GTP-binding protein rac1 - human ALTERNATE_NAMES ras-related C3 botulimum toxin substrate 1 ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 19-Jan-2001 ACCESSIONS A34788; A34386; B34387 REFERENCE A34788 !$#authors Drivas, G.T.; Shih, A.; Coutavas, E.; Rush, M.G.; !1D'Eustachio, P. !$#journal Mol. Cell. Biol. (1990) 10:1793-1798 !$#title Characterization of four novel ras-like genes expressed in a !1human teratocarcinoma cell line. !$#cross-references MUID:90205863; PMID:2108320 !$#accession A34788 !'##molecule_type mRNA !'##residues 1-192 ##label DRI !'##cross-references GB:M31467 !'##experimental_source teratocarcinoma clone TC25 REFERENCE A34386 !$#authors Didsbury, J.; Weber, R.F.; Bokoch, G.M.; Evans, T.; !1Snyderman, R. !$#journal J. Biol. Chem. (1989) 264:16378-16382 !$#title rac, a novel ras-related family of proteins that are !1botulinum toxin substrates. !$#cross-references MUID:89380250; PMID:2674130 !$#accession A34386 !'##molecule_type mRNA !'##residues 1-192 ##label DID !'##cross-references GB:M29870; NID:g190823; PIDN:AAA36537.1; !1PID:g190824; GB:J05038 REFERENCE A34387 !$#authors Polakis, P.G.; Weber, R.F.; Nevins, B.; Didsbury, J.R.; !1Evans, T.; Snyderman, R. !$#journal J. Biol. Chem. (1989) 264:16383-16389 !$#title Identification of the ral and rac1 gene products, low !1molecular mass GTP-binding proteins from human platelets. !$#cross-references MUID:89380251; PMID:2550440 !$#accession B34387 !'##molecule_type protein !'##residues 48-55,'X',57-65;136-142,'X',144;147-156,'X',158-162,'X', !1164-167,'X',169,'X',171-173 ##label POL GENETICS !$#gene GDB:RAC1 !'##cross-references GDB:134410 !$#map_position 17q21.2-17q21.2 CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS GTP binding; lipoprotein; membrane protein; methylated !1carboxyl end; nucleotide binding; P-loop; prenylated !1cysteine; proto-oncogene; transforming protein FEATURE !$2-189 #product GTP-binding protein rac1 #status predicted !8#label MAT\ !$10-17 #region nucleotide-binding motif A (P-loop)\ !$115-118 #region GTP-binding NKXD motif\ !$158-160 #region GTP-binding SAK/L motif\ !$39 #modified_site ADP-ribosylasparagine (Asn) (by !8botulinum exoenzyme C3) #status predicted\ !$189 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted\ !$189 #binding_site geranyl-geranyl (Cys) (covalent) !8#status predicted SUMMARY #length 192 #molecular-weight 21450 #checksum 7938 SEQUENCE /// ENTRY B34386 #type complete TITLE GTP-binding protein rac2 - human ALTERNATE_NAMES GTP binding protein Gx; ras-related C3 botulinum toxin substrate ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1991 #sequence_revision 31-May-1996 #text_change 19-Jan-2001 ACCESSIONS B34386; JT0574; B38126; C49292 REFERENCE A34386 !$#authors Didsbury, J.; Weber, R.F.; Bokoch, G.M.; Evans, T.; !1Snyderman, R. !$#journal J. Biol. Chem. (1989) 264:16378-16382 !$#title rac, a novel ras-related family of proteins that are !1botulinum toxin substrates. !$#cross-references MUID:89380250; PMID:2674130 !$#accession B34386 !'##molecule_type mRNA !'##residues 1-192 ##label DID !'##cross-references GB:M29871; NID:g190825; PIDN:AAA36538.1; !1PID:g190826; GB:J05038 REFERENCE JT0574 !$#authors Reibel, L.; Dorseuil, O.; Stancou, R.; Bertoglio, J.; Gacon, !1G. !$#journal Biochem. Biophys. Res. Commun. (1991) 175:451-458 !$#title A hemopoietic specific gene encoding a small GTP binding !1protein is overexpressed during T cell activation. !$#cross-references MUID:91207334; PMID:1902092 !$#accession JT0574 !'##molecule_type mRNA !'##residues 13-192 ##label REI !'##cross-references GB:M64595; NID:g183708; PIDN:AAA35941.1; !1PID:g183709 !'##experimental_source B cell REFERENCE A38126 !$#authors Mizuno, T.; Kaibuchi, K.; Ando, S.; Musha, T.; Hiraoka, K.; !1Takaishi, K.; Asada, M.; Nunoi, H.; Matsuda, I.; Takai, Y. !$#journal J. Biol. Chem. (1992) 267:10215-10218 !$#title Regulation of the superoxide-generating NADPH oxidase by a !1small GTP-binding protein and its stimulatory and inhibitory !1GDP/GTP exchange proteins. !$#cross-references MUID:92268051; PMID:1316893 !$#accession B38126 !'##molecule_type protein !'##residues 6-15;97-107;134-165 ##label MIZ !'##experimental_source HL60 REFERENCE A49292 !$#authors Kwong, C.H.; Malech, H.L.; Rotrosen, D.; Leto, T.L. !$#journal Biochemistry (1993) 32:5711-5717 !$#title Regulation of the human neutrophil NADPH oxidase by !1rho-related G-proteins. !$#cross-references MUID:93277853; PMID:8504089 !$#accession C49292 !'##molecule_type protein !'##residues 97-102;167-174 ##label KWO GENETICS !$#gene GDB:RAC2; EN-7 !'##cross-references GDB:134411; GDB:5952562 !$#map_position 22q12.3-22q13.2 CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS GTP binding; lipoprotein; membrane protein; methylated !1carboxyl end; nucleotide binding; P-loop; prenylated !1cysteine; proto-oncogene; signal transduction; transforming !1protein FEATURE !$2-189 #product GTP-binding protein rac2 #status predicted !8#label MAT\ !$10-17 #region nucleotide-binding motif A (P-loop)\ !$57-62 #region GTP binding #status predicted\ !$111-118 #region GTP binding #status predicted\ !$140-146 #region GTP binding #status predicted\ !$158-160 #region GTP-binding SAK/L motif\ !$39 #modified_site ADP-ribosylasparagine (Asn) (by !8botulinum exoenzyme C3) #status predicted\ !$189 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted\ !$189 #binding_site geranyl-geranyl (Cys) (covalent) !8#status predicted SUMMARY #length 192 #molecular-weight 21429 #checksum 8838 SEQUENCE /// ENTRY TVHURG #type complete TITLE GTP-binding protein rhoG - human ALTERNATE_NAMES ras homolog G; transforming protein rhoG ORGANISM #formal_name Homo sapiens #common_name man DATE 13-Jan-1995 #sequence_revision 24-May-1996 #text_change 19-Jan-2001 ACCESSIONS S25722 REFERENCE S25722 !$#authors Vincent, S.; Jeanteur, P.; Fort, P. !$#journal Mol. Cell. Biol. (1992) 12:3138-3148 !$#title Growth-regulated expression of rhoG, a new member of the ras !1homolog gene family. !$#cross-references MUID:92318931; PMID:1620121 !$#accession S25722 !'##molecule_type mRNA !'##residues 1-191 ##label VIN !'##cross-references EMBL:X61587; NID:g36035; PIDN:CAA43784.1; !1PID:g36036 GENETICS !$#gene GDB:ARHG; rhoG !'##cross-references GDB:136404; OMIM:179505 !$#map_position 11p15.5-11p15.4 CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS GTP binding; lipoprotein; membrane protein; methylated !1carboxyl end; nucleotide binding; P-loop; prenylated !1cysteine; proto-oncogene; transforming protein FEATURE !$2-188 #product GTP-binding protein rhoG #status predicted !8#label MAT\ !$10-17 #region nucleotide-binding motif A (P-loop)\ !$115-118 #region GTP-binding NKXD motif\ !$158-160 #region GTP-binding SAK/L motif\ !$39 #modified_site ADP-ribosylasparagine (Asn) (by !8botulinum exoenzyme C3) #status predicted\ !$188 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted\ !$188 #binding_site geranyl-geranyl (Cys) (covalent) !8#status predicted SUMMARY #length 191 #molecular-weight 21338 #checksum 5854 SEQUENCE /// ENTRY TVHUC4 #type complete TITLE transforming protein ras (teratocarcinoma clone TC10) - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 19-Jan-2001 ACCESSIONS D34788 REFERENCE A34788 !$#authors Drivas, G.T.; Shih, A.; Coutavas, E.; Rush, M.G.; !1D'Eustachio, P. !$#journal Mol. Cell. Biol. (1990) 10:1793-1798 !$#title Characterization of four novel ras-like genes expressed in a !1human teratocarcinoma cell line. !$#cross-references MUID:90205863; PMID:2108320 !$#accession D34788 !'##molecule_type mRNA !'##residues 1-213 ##label DRI !'##cross-references GB:M31470; NID:g190880; PIDN:AAA36547.1; !1PID:g190881 GENETICS !$#gene GDB:TC10 !'##cross-references GDB:9956554 CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS GTP binding; lipoprotein; membrane protein; methylated !1carboxyl end; nucleotide binding; P-loop; prenylated !1cysteine; thiolester bond; transforming protein FEATURE !$24-31 #region nucleotide-binding motif A (P-loop)\ !$129-132 #region GTP-binding NKXD motif\ !$172-174 #region GTP-binding SAK/L motif\ !$209 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$210 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted\ !$210 #binding_site farnesyl (Cys) (covalent) #status !8predicted SUMMARY #length 213 #molecular-weight 23403 #checksum 4993 SEQUENCE /// ENTRY TVHU12 #type complete TITLE GTP-binding protein rhoA - human ALTERNATE_NAMES Gb; ras-related homolog 12; transforming protein rhoA ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 19-Jan-2001 ACCESSIONS A26675; I53800 REFERENCE A26675 !$#authors Yeramian, P.; Chardin, P.; Madaule, P.; Tavitian, A. !$#journal Nucleic Acids Res. (1987) 15:1869 !$#title Nucleotide sequence of human rho cDNA clone 12. !$#cross-references MUID:87146500; PMID:3822842 !$#accession A26675 !'##molecule_type mRNA !'##residues 1-193 ##label YER !'##cross-references EMBL:X05026; NID:g36029; PIDN:CAA28690.1; !1PID:g36030 REFERENCE I53800 !$#authors Moscow, J.A.; He, R.; Gudas, J.M.; Cowan, K.H. !$#journal Gene (1994) 144:229-236 !$#title Utilization of multiple polyadenylation signals in the human !1RHOA protooncogene. !$#cross-references MUID:94314221; PMID:8039707 !$#accession I53800 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 5-193 ##label RES !'##cross-references GB:L09159; NID:g307374; PIDN:AAA50612.1; !1PID:g307375 GENETICS !$#gene GDB:ARH12; rhoA !'##cross-references GDB:119698; OMIM:165390 !$#map_position 3p21-3p21 CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS acetylated amino end; GTP binding; lipoprotein; membrane !1protein; methylated carboxyl end; nucleotide binding; !1P-loop; prenylated cysteine; proto-oncogene; transforming !1protein FEATURE !$2-190 #product GTP-binding protein rhoA #status predicted !8#label MAT\ !$12-19 #region nucleotide-binding motif A (P-loop)\ !$117-120 #region GTP-binding NKXD motif\ !$160-162 #region GTP-binding SAK/L motif\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status predicted\ !$18,19,37,117,118, !$120,160 #binding_site Mg-GTP (Lys, Thr, Thr, Asn, Lys, Asp, !8Ser) #status predicted\ !$41 #modified_site ADP-ribosylasparagine (Asn) (by !8botulinum exoenzyme C3) #status predicted\ !$190 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted\ !$190 #binding_site geranyl-geranyl (Cys) (covalent) !8#status predicted SUMMARY #length 193 #molecular-weight 21768 #checksum 5051 SEQUENCE /// ENTRY TVBO12 #type complete TITLE GTP-binding protein rhoA - bovine ALTERNATE_NAMES Gb; ras-related homolog A; transforming protein rhoA ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 15-Jan-1993 #sequence_revision 24-May-1996 #text_change 19-Jan-2001 ACCESSIONS A33518; A60050; A32119; A38324 REFERENCE A33518 !$#authors Ogorochi, T.; Nemoto, Y.; Nakajima, M.; Nakamura, E.; !1Fujiwara, M.; Narumiya, S. !$#journal Biochem. Biophys. Res. Commun. (1989) 163:1175-1181 !$#title cDNA cloning of Gb, the substrate for botulinum !1ADP-ribosyltransferase from bovine adrenal gland and its !1identification as a rho gene product. !$#cross-references MUID:89391974; PMID:2506852 !$#accession A33518 !'##molecule_type mRNA !'##residues 1-193 ##label OGO !'##cross-references GB:M27278; NID:g162742; PIDN:AAA30409.1; !1PID:g162743 REFERENCE A60050 !$#authors Hoshijima, M.; Kondo, J.; Kikuchi, A.; Yamamoto, K.; Takai, !1Y. !$#journal Brain Res. Mol. Brain Res. (1990) 7:9-16 !$#title Purification and characterization from bovine brain !1membranes of a GTP-binding protein with a M-r of 21,000, !1ADP-ribosylated by an ADP-ribosyltransferase contaminated in !1botulinum toxin type C1 - identification as the rhoA gene !1product. !$#cross-references MUID:90135940; PMID:2153899 !$#accession A60050 !'##molecule_type protein !'##residues 8-15;28-43;52-58;100-104;169-181 ##label HOS REFERENCE A32119 !$#authors Narumiya, S.; Sekine, A.; Fujiwara, M. !$#journal J. Biol. Chem. (1988) 263:17255-17257 !$#title Substrate for botulinum ADP-ribosyltransferase, Gb, has an !1amino acid sequence homologous to a putative rho gene !1product. !$#cross-references MUID:89034241; PMID:3141419 !$#accession A32119 !'##molecule_type protein !'##residues 19,'X',21-25;'X',42-50;52-57;59-82,'X',84-97;99-104;'M', !1133-158,'X',160-162;169-176 ##label NAR !'##note the amino end of the mature protein is blocked REFERENCE A38324 !$#authors Williamson, K.C.; Smith, L.A.; Moss, J.; Vaughan, M. !$#journal J. Biol. Chem. (1990) 265:20807-20812 !$#title Guanine nucleotide-dependent ADP-ribosylation of soluble rho !1catalyzed by Clostridium botulinum C3 !1ADP-ribosyltransferase. Isolation and characterization of a !1newly recognized form of rhoA. !$#cross-references MUID:91065876; PMID:2174426 !$#accession A38324 !'##molecule_type protein !'##residues 28-70;99-104 ##label WIL REFERENCE A33190 !$#authors Sekine, A.; Fujiwara, M.; Narumiya, S. !$#journal J. Biol. Chem. (1989) 264:8602-8605 !$#title Asparagine residue in the rho gene product is the !1modification site for botulinum ADP-ribosyltransferase. !$#cross-references MUID:89255316; PMID:2498316 !$#contents annotation; identification of ADP-ribosylation site CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS acetylated amino end; GTP binding; lipoprotein; membrane !1protein; methylated carboxyl end; nucleotide binding; !1P-loop; prenylated cysteine; proto-oncogene; transforming !1protein FEATURE !$2-190 #product GTP-binding protein rhoA #status predicted !8#label MAT\ !$12-19 #region nucleotide-binding motif A (P-loop)\ !$117-120 #region GTP-binding NKXD motif\ !$160-162 #region GTP-binding SAK/L motif\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status predicted\ !$18,19,37,117,118, !$120,160 #binding_site Mg-GTP (Lys, Thr, Thr, Asn, Lys, Asp, !8Ser) #status predicted\ !$41 #modified_site ADP-ribosylasparagine (Asn) (by !8botulinum exoenzyme C3) #status experimental\ !$190 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted\ !$190 #binding_site geranyl-geranyl (Cys) (covalent) !8#status predicted SUMMARY #length 193 #molecular-weight 21768 #checksum 5051 SEQUENCE /// ENTRY TVHURH #type complete TITLE GTP-binding protein rhoB - human ALTERNATE_NAMES Gb; ras-related homolog 6; transforming protein rhoB ORGANISM #formal_name Homo sapiens #common_name man DATE 27-Nov-1985 #sequence_revision 31-Mar-1991 #text_change 19-Jan-2001 ACCESSIONS A01372; S00744 REFERENCE A01372 !$#authors Madaule, P.; Axel, R. !$#journal Cell (1985) 41:31-40 !$#title A novel ras-related gene family. !$#cross-references MUID:85201682; PMID:3888408 !$#accession A01372 !'##molecule_type mRNA !'##residues 29-196 ##label MAD !'##cross-references GB:M12174; NID:g337392; PIDN:AAA36565.1; !1PID:g337393 REFERENCE S00744 !$#authors Chardin, P.; Madaule, P.; Tavitian, A. !$#journal Nucleic Acids Res. (1988) 16:2717 !$#title Coding sequence of human rho cDNAs clone 6 and clone 9. !$#cross-references MUID:88203210; PMID:3283705 !$#accession S00744 !'##molecule_type mRNA !'##residues 1-196 ##label CHA !'##cross-references EMBL:X06820; NID:g36031; PIDN:CAA29968.1; !1PID:g36032 GENETICS !$#gene GDB:ARH6 !'##cross-references GDB:119699; OMIM:165370 !$#map_position 2pter-2p12 CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS acetylated amino end; GTP binding; lipoprotein; membrane !1protein; methylated carboxyl end; nucleotide binding; !1P-loop; prenylated cysteine; proto-oncogene; thiolester !1bond; transforming protein FEATURE !$2-193 #product GTP-binding protein rhoB #status predicted !8#label MAT\ !$12-19 #region nucleotide-binding motif A (P-loop)\ !$117-120 #region GTP-binding NKXD motif\ !$160-162 #region GTP-binding SAK/L motif\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status predicted\ !$18,19,37,117,118, !$120,160 #binding_site Mg-GTP (Lys, Thr, Thr, Asn, Lys, Asp, !8Ser) #status predicted\ !$41 #modified_site ADP-ribosylasparagine (Asn) (by !8botulinum exoenzyme C3) #status predicted\ !$192 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$193 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted\ !$193 #binding_site geranyl-geranyl (Cys) (covalent) !8#status predicted SUMMARY #length 196 #molecular-weight 22123 #checksum 2378 SEQUENCE /// ENTRY TVRTRH #type complete TITLE GTP-binding protein rhoB - rat ALTERNATE_NAMES transforming protein rhoB ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 19-Jan-2001 ACCESSIONS A39727 REFERENCE A39727 !$#authors Jaehner, D.; Hunter, T. !$#journal Mol. Cell. Biol. (1991) 11:3682-3690 !$#title The ras-related gene rhoB is an immediate-early gene !1inducible by v-Fps, epidermal growth factor, and !1platelet-derived growth factor in rat fibroblasts. !$#cross-references MUID:91260717; PMID:1710770 !$#accession A39727 !'##molecule_type mRNA !'##residues 1-196 ##label JAH !'##cross-references GB:M74295; NID:g206655; PIDN:AAA42040.1; !1PID:g206656 GENETICS !$#gene rhoB CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS GTP binding; immediate-early protein; lipoprotein; membrane !1protein; methylated carboxyl end; nucleotide binding; !1P-loop; prenylated cysteine; proto-oncogene; thiolester !1bond; transforming protein FEATURE !$2-193 #product GTP-binding protein rhoB #status predicted !8#label MAT\ !$12-19 #region nucleotide-binding motif A (P-loop)\ !$117-120 #region GTP-binding NKXD motif\ !$160-162 #region GTP-binding SAK/L motif\ !$18,19,37,117,118, !$120,160 #binding_site Mg-GTP (Lys, Thr, Thr, Asn, Lys, Asp, !8Ser) #status predicted\ !$41 #modified_site ADP-ribosylasparagine (Asn) (by !8botulinum exoenzyme C3) #status predicted\ !$192 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$193 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted\ !$193 #binding_site geranyl-geranyl (Cys) (covalent) !8#status predicted SUMMARY #length 196 #molecular-weight 22123 #checksum 2378 SEQUENCE /// ENTRY TVHURC #type complete TITLE GTP-binding protein rhoC - human ALTERNATE_NAMES Gb; ras-related homolog 9; transforming protein rhoC ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 19-Jan-2001 ACCESSIONS S01029 REFERENCE S00744 !$#authors Chardin, P.; Madaule, P.; Tavitian, A. !$#journal Nucleic Acids Res. (1988) 16:2717 !$#title Coding sequence of human rho cDNAs clone 6 and clone 9. !$#cross-references MUID:88203210; PMID:3283705 !$#accession S01029 !'##molecule_type mRNA !'##residues 1-193 ##label CHA !'##cross-references EMBL:X06821; NID:g36033; PIDN:CAA29969.1; !1PID:g36034 GENETICS !$#gene GDB:ARH9; rhoC !'##cross-references GDB:119700; OMIM:165380 !$#map_position 1p21-1p13 CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS acetylated amino end; GTP binding; lipoprotein; membrane !1protein; methylated carboxyl end; nucleotide binding; !1P-loop; prenylated cysteine; proto-oncogene; transforming !1protein FEATURE !$2-190 #product GTP-binding protein rhoC #status predicted !8#label MAT\ !$12-19 #region nucleotide-binding motif A (P-loop)\ !$117-120 #region GTP-binding NKXD motif\ !$160-162 #region GTP-binding SAK/L motif\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status predicted\ !$18,19,37,117,118, !$120,160 #binding_site Mg-GTP (Lys, Thr, Thr, Asn, Lys, Asp, !8Ser) #status predicted\ !$41 #modified_site ADP-ribosylasparagine (Asn) (by !8botulinum exoenzyme C3) #status predicted\ !$190 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted\ !$190 #binding_site geranyl-geranyl (Cys) (covalent) !8#status predicted SUMMARY #length 193 #molecular-weight 22006 #checksum 5512 SEQUENCE /// ENTRY TVGAAC #type complete TITLE transforming protein rho - California sea hare ORGANISM #formal_name Aplysia californica #common_name California sea hare DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 19-Jan-2001 ACCESSIONS A01373 REFERENCE A01372 !$#authors Madaule, P.; Axel, R. !$#journal Cell (1985) 41:31-40 !$#title A novel ras-related gene family. !$#cross-references MUID:85201682; PMID:3888408 !$#accession A01373 !'##molecule_type mRNA !'##residues 1-192 ##label MAD !'##cross-references GB:M10078; NID:g155803; PIDN:AAA27776.1; !1PID:g155804 COMMENT This protein is homologous with the ras transforming !1proteins. GENETICS !$#gene rho CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS GTP binding; lipoprotein; membrane protein; methylated !1carboxyl end; nucleotide binding; P-loop; prenylated !1cysteine; proto-oncogene; transforming protein FEATURE !$12-19 #region nucleotide-binding motif A (P-loop)\ !$117-120 #region GTP-binding NKXD motif\ !$160-162 #region GTP-binding SAK/L motif\ !$18,19,37,117,118, !$120,160 #binding_site Mg-GTP (Lys, Thr, Thr, Asn, Lys, Asp, !8Ser) #status predicted\ !$189 #binding_site geranyl-geranyl (Cys) (covalent) !8#status predicted\ !$189 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted SUMMARY #length 192 #molecular-weight 21661 #checksum 5045 SEQUENCE /// ENTRY TVBYH1 #type complete TITLE transforming protein RHO1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein P9325.3; protein YPR165w ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 19-Jan-2001 ACCESSIONS A26587; S59824 REFERENCE A94186 !$#authors Madaule, P.; Axel, R.; Myers, A.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:779-783 !$#title Characterization of two members of the rho gene family from !1the yeast Saccharomyces cerevisiae. !$#cross-references MUID:87118248; PMID:3543936 !$#accession A26587 !'##molecule_type DNA !'##residues 1-209 ##label MAD !'##cross-references EMBL:M15189; NID:g172419; PIDN:AAA34977.1; !1PID:g172420 REFERENCE S59821 !$#authors Hallsworth, K. !$#submission submitted to the EMBL Data Library, April 1995 !$#description The sequence of S. cerevisiae cosmid 9325. !$#accession S59824 !'##molecule_type DNA !'##residues 1-209 ##label HAL !'##cross-references EMBL:U25840; NID:g786286; PIDN:AAB68152.1; !1PID:g786290; GSPDB:GN00016; MIPS:YPR165w GENETICS !$#gene SGD:RHO1; MIPS:YPR165w !'##cross-references SGD:S0006369; MIPS:YPR165w !$#map_position 16R CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS GTP binding; lipoprotein; membrane protein; methylated !1carboxyl end; nucleotide binding; P-loop; prenylated !1cysteine; transmembrane protein FEATURE !$17-24 #region nucleotide-binding motif A (P-loop)\ !$108-124 #domain transmembrane #status predicted #label TM2\ !$122-125 #region GTP-binding NKXD motif\ !$165-167 #region GTP-binding SAK/L motif\ !$206 #binding_site geranyl-geranyl (Cys) (covalent) !8#status predicted\ !$206 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted SUMMARY #length 209 #molecular-weight 23152 #checksum 6070 SEQUENCE /// ENTRY TVBYH2 #type complete TITLE GTP-binding protein RHO2 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein N2237; protein YNL090w; transforming protein RHO2 ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Dec-1988 #sequence_revision 10-Nov-1995 #text_change 19-Jan-2001 ACCESSIONS S57533; B26587; S63029; S65092 REFERENCE S57533 !$#authors Soler-Mira, A.; Saiz, J.E.; Ballesta, J.P.G.; Remacha, M. !$#submission submitted to the EMBL Data Library, June 1995 !$#accession S57533 !'##molecule_type DNA !'##residues 1-192 ##label SOL !'##cross-references EMBL:X89016; NID:g887621; PIDN:CAA61421.1; !1PID:g887622 REFERENCE A94186 !$#authors Madaule, P.; Axel, R.; Myers, A.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:779-783 !$#title Characterization of two members of the rho gene family from !1the yeast Saccharomyces cerevisiae. !$#cross-references MUID:87118248; PMID:3543936 !$#accession B26587 !'##molecule_type DNA !'##residues 1-47,'S',49-192 ##label MAD !'##cross-references EMBL:M15190; NID:g172421; PIDN:AAA34978.1; !1PID:g172422 !'##note the authors translated the codon TCG for residue 48 as Cys REFERENCE S63018 !$#authors Soler-Mira, A.; Saiz, J.E.; Ballesta, J.P.G.; Remacha, M. !$#submission submitted to the Protein Sequence Database, April 1996 !$#accession S63029 !'##molecule_type DNA !'##residues 1-192 ##label SOW !'##cross-references EMBL:Z71366; NID:g1301990; PIDN:CAA95965.1; !1PID:g1301991; GSPDB:GN00014; MIPS:YNL090w !'##experimental_source strain S288C REFERENCE S65092 !$#authors Soler-Mira, A.; Saiz, J.E.; Ballesta, J.P.G.; Remacha, M. !$#journal Yeast (1996) 12:485-491 !$#title The sequence of a 17 933 bp segment of Saccharomyces !1cerevisiae chromosome XIV contains the RHO2, TOP2, MKT1 and !1END3 genes and five new open reading frames. !$#cross-references MUID:96310628; PMID:8740422 !$#accession S65092 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-192 ##label SOF !'##cross-references EMBL:X89016; NID:g887621; PIDN:CAA61421.1; !1PID:g887622 GENETICS !$#gene SGD:RHO2; MIPS:YNL090w !'##cross-references SGD:S0005034; MIPS:YNL090w !$#map_position 14L CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS GTP binding; lipoprotein; membrane protein; methylated !1carboxyl end; nucleotide binding; P-loop; prenylated !1cysteine; thiolester bond; transforming protein FEATURE !$14-21 #region nucleotide-binding motif A (P-loop)\ !$119-122 #region GTP-binding NKXD motif\ !$159-161 #region GTP-binding SAK/L motif\ !$188 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$189 #binding_site geranyl-geranyl (Cys) (covalent) !8#status predicted\ !$189 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted SUMMARY #length 192 #molecular-weight 21479 #checksum 378 SEQUENCE /// ENTRY TVBYQ2 #type complete TITLE GTP-binding protein YPT1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein F011; protein YFL038c; transforming protein homolog YP2 ORGANISM #formal_name Saccharomyces cerevisiae DATE 03-Aug-1984 #sequence_revision 19-Oct-1995 #text_change 19-Jan-2001 ACCESSIONS S56216; A01374; S60498 REFERENCE S56186 !$#authors Murakami, Y.; Naitou, M.; Hagiwara, H.; Shibata, T.; Ozawa, !1M.; Sasanuma, S.I.; Sasanuma, M.; Tsuchiya, Y.; Soeda, E.; !1Yokoyama, K.; Yamazaki, M.; Tashiro, H.; Eki, T. !$#submission submitted to the EMBL Data Library, May 1995 !$#description Analysis of the nucleotide sequence of chromosome VI from !1Saccaromyces cerevisiae. !$#accession S56216 !'##molecule_type DNA !'##residues 1-206 ##label MUR !'##cross-references EMBL:D50617; NID:g836685; PIDN:BAA09201.1; !1PID:g836716; GSPDB:GN00006; MIPS:YFL038c REFERENCE A01374 !$#authors Gallwitz, D.; Donath, C.; Sander, C. !$#journal Nature (1983) 306:704-707 !$#title A gene encoding a protein homologous to the human c-has/bas !1proto-oncogene product. !$#cross-references MUID:84093563; PMID:6318115 !$#accession A01374 !'##molecule_type DNA !'##residues 1-170,'Q',172-206 ##label GAL !'##cross-references EMBL:X00209; NID:g4292; PIDN:CAA25036.1; PID:g4293 REFERENCE S60495 !$#authors Naitou, M.; Ozawa, M.; Sasanuma, S.I.; Kobayashi, M.; !1Hagiwara, H.; Shibata, T.; Hanaoka, F.; Watanabe, K.; Ono, !1A.; Yamazaki, M.; Tashiro, H.; Eki, T.; Murakami, Y. !$#journal Yeast (1995) 11:1525-1532 !$#title Sequencing of an 18.8 kb fragment from Saccharomyces !1cerevisiae chromosome VI. !$#cross-references MUID:96353435; PMID:8750241 !$#accession S60498 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-206 ##label NAI !'##cross-references EMBL:D44598; NID:g871933; PIDN:BAA08026.1; !1PID:g871935 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1994 GENETICS !$#gene SGD:YPT1; YP2; MIPS:YFL038c !'##cross-references SGD:S0001856; MIPS:YFL038c !$#map_position 6L CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS GTP binding; lipoprotein; nucleotide binding; P-loop; !1prenylated cysteine; thiolester bond FEATURE !$9-124 #domain translation elongation factor Tu homology !8#label ETU\ !$15-22 #region nucleotide-binding motif A (P-loop)\ !$121-124 #region GTP-binding NKXD motif\ !$151-153 #region GTP-binding SAK/L motif\ !$21,22,40,121,122, !$124,151 #binding_site Mg-GTP (Lys, Ser, Thr, Asn, Lys, Asp, !8Ser) #status predicted\ !$205 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$206 #binding_site geranyl-geranyl (Cys) (covalent) !8#status predicted SUMMARY #length 206 #molecular-weight 23214 #checksum 7761 SEQUENCE /// ENTRY TVHUYP #type complete TITLE GTP-binding protein Rab1 - human ALTERNATE_NAMES protein DKFZp564B163.1 ORGANISM #formal_name Homo sapiens #common_name man DATE 29-Jun-1990 #sequence_revision 06-Dec-1996 #text_change 19-Jan-2001 ACCESSIONS A34323; T08698 REFERENCE A34323 !$#authors Zahraoui, A.; Touchot, N.; Chardin, P.; Tavitian, A. !$#journal J. Biol. Chem. (1989) 264:12394-12401 !$#title The human Rab genes encode a family of GTP-binding proteins !1related to yeast YPT1 and SEC4 products involved in !1secretion. !$#cross-references MUID:89308668; PMID:2501306 !$#accession A34323 !'##molecule_type mRNA !'##residues 1-205 ##label ZAH !'##cross-references GB:J04941; GB:M28209; NID:g550059; PIDN:AAA60240.1; !1PID:g550060 !'##experimental_source pheochromocytoma REFERENCE Z16471 !$#authors Wambutt, R.; Heubner, D.; Mewes, H.W.; Gassenhuber, J.; !1Wiemann, S. !$#submission submitted to the Protein Sequence Database, March 1999 !$#accession T08698 !'##molecule_type mRNA !'##residues 1-64,141-205 ##label WAM !'##cross-references EMBL:AL050268 !'##experimental_source fetal brain; clone DKFZp564B163 GENETICS !$#gene GDB:RAB1 !'##cross-references GDB:118857; OMIM:179508 !$#map_position 4p15.31-4p15.31 !$#note DKFZp564B163.1 FUNCTION !$#description probably involved in protein transport from the endoplasmic !1reticulum through the Golgi apparatus CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS endoplasmic reticulum; Golgi apparatus; GTP binding; !1lipoprotein; membrane protein; membrane trafficking; !1nucleotide binding; P-loop; phosphoprotein; prenylated !1cysteine; transforming protein FEATURE !$1-205 #product GTP-binding protein Rab1 #status predicted !8#label MAT1\ !$1-64,141-205 #product GTP-binding protein Rab1, splice variant !8#status predicted #label MAT2\ !$12-127 #domain translation elongation factor Tu homology !8#label ETU\ !$18-25 #region nucleotide-binding motif A (P-loop)\ !$62-67 #region nucleotide-binding motif B\ !$124-127 #region GTP-binding NKXD motif\ !$154-156 #region GTP-binding SAK/L motif\ !$24,25,43,124,125, !$127,154 #binding_site Mg-GTP (Lys, Ser, Thr, Asn, Lys, Asp, !8Ser) #status predicted\ !$194 #binding_site phosphate (Ser) (covalent) (by cdc2 !8kinase) #status predicted\ !$204,205 #binding_site geranyl-geranyl (Cys) (covalent) !8#status experimental SUMMARY #length 205 #molecular-weight 22678 #checksum 3483 SEQUENCE /// ENTRY TVDGYP #type complete TITLE GTP-binding protein Rab1 - dog ORGANISM #formal_name Canis lupus familiaris #common_name dog DATE 19-Feb-1994 #sequence_revision 06-Dec-1996 #text_change 19-Jan-2001 ACCESSIONS S19104; A36364; S15600 REFERENCE S19104 !$#authors Zerial, M. !$#submission submitted to the EMBL Data Library, August 1990 !$#accession S19104 !'##molecule_type mRNA !'##residues 1-205 ##label ZER !'##cross-references EMBL:X56384 REFERENCE A36364 !$#authors Chavrier, P.; Vingron, M.; Sander, C.; Simons, K.; Zerial, !1M. !$#journal Mol. Cell. Biol. (1990) 10:6578-6585 !$#title Molecular cloning of YPT1/SEC4-related cDNAs from an !1epithelial cell line. !$#cross-references MUID:91061765; PMID:2123294 !$#accession A36364 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-157,'EK',160-205 ##label CHA !'##cross-references GB:X56384; NID:g913 FUNCTION !$#description probably involved in protein transport from the endoplasmic !1reticulum through the Golgi apparatus CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS endoplasmic reticulum; Golgi apparatus; GTP binding; !1lipoprotein; membrane protein; membrane trafficking; !1nucleotide binding; P-loop; phosphoprotein; prenylated !1cysteine; transforming protein FEATURE !$12-127 #domain translation elongation factor Tu homology !8#label ETU\ !$18-25 #region nucleotide-binding motif A (P-loop)\ !$62-67 #region nucleotide-binding motif B\ !$124-127 #region GTP-binding NKXD motif\ !$154-156 #region GTP-binding SAK/L motif\ !$24,25,43,124,125, !$127,154 #binding_site Mg-GTP (Lys, Ser, Thr, Asn, Lys, Asp, !8Ser) #status predicted\ !$194 #binding_site phosphate (Ser) (covalent) (by cdc2 !8kinase) #status predicted\ !$204,205 #binding_site geranyl-geranyl (Cys) (covalent) !8#status predicted SUMMARY #length 205 #molecular-weight 22678 #checksum 3483 SEQUENCE /// ENTRY TVMSYP #type complete TITLE GTP-binding protein ypt1 - mouse ALTERNATE_NAMES GTP-binding protein Rab1; ras-related protein ypt1; transforming protein ypt1 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 19-Jan-2001 ACCESSIONS S05551; S06285 REFERENCE S05551 !$#authors Wichmann, H.; Disela, C.; Haubruck, H.; Gallwitz, D. !$#journal Nucleic Acids Res. (1989) 17:6737-6738 !$#title Nucleotide sequence of the mouse ypt1 gene encoding a !1ras-related GTP-binding protein. !$#cross-references MUID:89386011; PMID:2506528 !$#accession S05551 !'##molecule_type DNA !'##residues 1-205 ##label WIC !'##cross-references EMBL:X15744; NID:g55458; PIDN:CAA33760.1; !1PID:g763158 REFERENCE S06285 !$#authors Haubruck, H.; Disela, C.; Wagner, P.; Gallwitz, D. !$#journal EMBO J. (1987) 6:4049-4053 !$#title The ras-related ypt protein is an ubiquitous eukaryotic !1protein: isolation and sequence analysis of mouse cDNA !1clones highly homologous to the yeast YPT1 gene. !$#cross-references MUID:88166649; PMID:3127202 !$#accession S06285 !'##molecule_type mRNA !'##residues 1-205 ##label HAU GENETICS !$#gene ypt1 !$#introns 8/2; 32/3; 64/3; 96/3; 140/3 FUNCTION !$#description probably involved in protein transport from the endoplasmic !1reticulum through the Golgi apparatus CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS endoplasmic reticulum; Golgi apparatus; GTP binding; !1lipoprotein; membrane protein; membrane trafficking; !1nucleotide binding; P-loop; phosphoprotein; prenylated !1cysteine; transforming protein FEATURE !$12-127 #domain translation elongation factor Tu homology !8#label ETU\ !$18-25 #region nucleotide-binding motif A (P-loop)\ !$62-67 #region nucleotide-binding motif B\ !$124-127 #region GTP-binding NKXD motif\ !$154-156 #region GTP-binding SAK/L motif\ !$24,25,43,124,125, !$127,154 #binding_site Mg-GTP (Lys, Ser, Thr, Asn, Lys, Asp, !8Ser) #status predicted\ !$194 #binding_site phosphate (Ser) (covalent) (by cdc2 !8kinase) #status predicted\ !$204,205 #binding_site geranyl-geranyl (Cys) (covalent) !8#status predicted SUMMARY #length 205 #molecular-weight 22678 #checksum 3483 SEQUENCE /// ENTRY TVRTYP #type complete TITLE GTP-binding protein Rab1 - rat ALTERNATE_NAMES transforming protein ypt1 homolog ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 03-Aug-1992 #sequence_revision 06-Dec-1996 #text_change 19-Jan-2001 ACCESSIONS A39963 REFERENCE A39963 !$#authors Touchot, N.; Chardin, P.; Tavitian, A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:8210-8214 !$#title Four additional members of the ras gene superfamily isolated !1by an oligonucleotide strategy: molecular cloning of !1YPT-related cDNAs from a rat brain library. !$#cross-references MUID:88068563; PMID:3317403 !$#accession A39963 !'##molecule_type mRNA !'##residues 1-205 ##label TOU !'##cross-references GB:J02998; NID:g206552; PIDN:AAA42006.1; !1PID:g206553 FUNCTION !$#description probably involved in protein transport from the endoplasmic !1reticulum through the Golgi apparatus CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS endoplasmic reticulum; Golgi apparatus; GTP binding; !1lipoprotein; membrane protein; membrane trafficking; !1nucleotide binding; P-loop; phosphoprotein; prenylated !1cysteine; transforming protein FEATURE !$12-127 #domain translation elongation factor Tu homology !8#label ETU\ !$18-25 #region nucleotide-binding motif A (P-loop)\ !$62-67 #region nucleotide-binding motif B\ !$124-127 #region GTP-binding NKXD motif\ !$154-156 #region GTP-binding SAK/L motif\ !$24,25,43,124,125, !$127,154 #binding_site Mg-GTP (Lys, Ser, Thr, Asn, Lys, Asp, !8Ser) #status predicted\ !$194 #binding_site phosphate (Ser) (covalent) (by cdc2 !8kinase) #status predicted\ !$204,205 #binding_site geranyl-geranyl (Cys) (covalent) !8#status predicted SUMMARY #length 205 #molecular-weight 22763 #checksum 3254 SEQUENCE /// ENTRY TVHUC3 #type complete TITLE GTP-binding protein Ran/TC4 - human ALTERNATE_NAMES 25K nuclear protein ras homolog; ras-related nuclear protein Ran; transforming protein ras (teratocarcinoma clone TC4) ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1991 #sequence_revision 23-Feb-1996 #text_change 19-Jan-2001 ACCESSIONS A44393; A41613; C34788 REFERENCE A44393 !$#authors Ren, M.; Drivas, G.; D'Eustachio, P.; Rush, M.G. !$#journal J. Cell Biol. (1993) 120:313-323 !$#title Ran/TC4: a small nuclear GTP-binding protein that regulates !1DNA synthesis. !$#cross-references MUID:93132064; PMID:8421051 !$#accession A44393 !'##molecule_type mRNA !'##residues 1-216 ##label REN !'##cross-references GB:M31469; NID:g190878; PIDN:AAA36546.1; !1PID:g190879 !'##note sequence extracted from NCBI backbone (NCBIP:122658) REFERENCE A41613 !$#authors Bischoff, F.R.; Ponstingl, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:10830-10834 !$#title Mitotic regulator protein RCC1 is complexed with a nuclear !1ras-related polypeptide. !$#cross-references MUID:92073381; PMID:1961752 !$#accession A41613 !'##molecule_type protein !'##residues 65-76;90-103;105-119;121-122;124-125;128,'S', !1130-139;141-147;154-158;160-162;164-216 ##label BIS REFERENCE A34788 !$#authors Drivas, G.T.; Shih, A.; Coutavas, E.; Rush, M.G.; !1D'Eustachio, P. !$#journal Mol. Cell. Biol. (1990) 10:1793-1798 !$#title Characterization of four novel ras-like genes expressed in a !1human teratocarcinoma cell line. !$#cross-references MUID:90205863; PMID:2108320 !$#accession C34788 !'##status significant sequence differences !'##molecule_type mRNA !'##cross-references GB:M31469 !'##note this sequence has been revised in reference A44393 GENETICS !$#gene GDB:RAN !'##cross-references GDB:4642521; OMIM:601179 !$#map_position 2cen-2q13 CLASSIFICATION #superfamily ras transforming protein; translation !1elongation factor Tu homology KEYWORDS cell cycle control; GTP binding; nucleotide binding; P-loop; !1signal transduction; transforming protein FEATURE !$17-24 #region nucleotide-binding motif A (P-loop)\ !$122-125 #region GTP-binding NKXD motif\ !$150-152 #region GTP-binding SAK/L motif SUMMARY #length 216 #molecular-weight 24423 #checksum 7677 SEQUENCE /// ENTRY S37599 #type complete TITLE ADP-ribosylation factor 1 - fission yeast (Schizosaccharomyces pombe) ORGANISM #formal_name Schizosaccharomyces pombe DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S37599; T40515 REFERENCE S37599 !$#authors Erickson, F.L.; Hannig, E.M.; Krasinskas, A.; Kahn, R.A. !$#journal Yeast (1993) 9:923-927 !$#title Yeast sequencing reports. Cloning and sequence of !1ADP-ribosylation factor 1 (ARF1) from Schizosaccharomyces !1pombe. !$#cross-references MUID:94025983; PMID:8212899 !$#accession S37599 !'##molecule_type mRNA !'##residues 1-180 ##label ERI !'##cross-references EMBL:L09551; NID:g173344; PIDN:AAC37347.1; !1PID:g173345 REFERENCE Z21933 !$#authors Gwilliam, R.; Rajandream, M.A.; Barrell, B.G.; Skelton, J.; !1Churcher, C.M. !$#submission submitted to the EMBL Data Library, September 1998 !$#accession T40515 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-180 ##label GWI !'##cross-references EMBL:AL031534; PIDN:CAA20738.1; GSPDB:GN00067; !1SPDB:SPBC4F6.18c !'##experimental_source strain 972h-; cosmid c4F6 GENETICS !$#gene ARF1; SPBC4F6.18c !$#map_position 2 !$#introns 17/3 CLASSIFICATION #superfamily ADP-ribosylation factor KEYWORDS blocked amino end; GTP binding; lipoprotein; myristylation; !1nucleotide binding; P-loop FEATURE !$24-31 #region nucleotide-binding motif A (P-loop)\ !$89-94 #region nucleotide-binding motif B\ !$126-129 #region GTP-binding NKXD motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted SUMMARY #length 180 #molecular-weight 20618 #checksum 15 SEQUENCE /// ENTRY TVHUAS #type complete TITLE transforming protein mas - human ORGANISM #formal_name Homo sapiens #common_name man DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 18-Jun-1999 ACCESSIONS A01375 REFERENCE A01375 !$#authors Young, D.; Waitches, G.; Birchmeier, C.; Fasano, O.; Wigler, !1M. !$#journal Cell (1986) 45:711-719 !$#title Isolation and characterization of a new cellular oncogene !1encoding a protein with multiple potential transmembrane !1domains. !$#cross-references MUID:86218084; PMID:3708691 !$#accession A01375 !'##molecule_type DNA !'##residues 1-325 ##label YOU !'##cross-references GB:M13150; NID:g187388; PIDN:AAA36199.1; !1PID:g307158 GENETICS !$#gene GDB:MAS1 !'##cross-references GDB:120166; OMIM:165180 !$#map_position 6q24-6q27 CLASSIFICATION #superfamily mas transforming protein KEYWORDS G protein-coupled receptor; glycoprotein; proto-oncogene; !1transforming protein; transmembrane protein FEATURE !$31-61 #domain transmembrane #status predicted #label TM1\ !$66-97 #domain transmembrane #status predicted #label TM2\ !$105-135 #domain transmembrane #status predicted #label TM3\ !$150-172 #domain transmembrane #status predicted #label TM4\ !$186-214 #domain transmembrane #status predicted #label TM5\ !$225-250 #domain transmembrane #status predicted #label TM6\ !$258-286 #domain transmembrane #status predicted #label TM7\ !$5,16,22,272 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 325 #molecular-weight 37465 #checksum 6267 SEQUENCE /// ENTRY TVRTAS #type complete TITLE transforming protein mas - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 18-Jun-1999 ACCESSIONS A31816 REFERENCE A31816 !$#authors Young, D.; O'Neill, K.; Jessell, T.; Wigler, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:5339-5342 !$#title Characterization of the rat mas oncogene and its high-level !1expression in the hippocampus and cerebral cortex of rat !1brain. !$#cross-references MUID:88276953; PMID:2455902 !$#accession A31816 !'##molecule_type mRNA !'##residues 1-324 ##label YOU !'##cross-references GB:J03823; NID:g205313; PIDN:AAA41573.1; !1PID:g205314 GENETICS !$#gene mas CLASSIFICATION #superfamily mas transforming protein KEYWORDS G protein-coupled receptor; transforming protein; !1transmembrane protein FEATURE !$31-47 #domain transmembrane #status predicted #label TM1\ !$72-88 #domain transmembrane #status predicted #label TM2\ !$149-165 #domain transmembrane #status predicted #label TM3\ !$185-204 #domain transmembrane #status predicted #label TM4\ !$225-243 #domain transmembrane #status predicted #label TM5 SUMMARY #length 324 #molecular-weight 37130 #checksum 1531 SEQUENCE /// ENTRY TVHUB #type complete TITLE transforming protein Blym-1 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 20-Sep-1984 #sequence_revision 20-Sep-1984 #text_change 18-Jun-1999 ACCESSIONS A01376 REFERENCE A01376 !$#authors Diamond, A.; Devine, J.M.; Cooper, G.M. !$#journal Science (1984) 225:516-519 !$#title Nucleotide sequence of a human Blym transforming gene !1activated in a Burkitt's lymphoma. !$#cross-references MUID:84250206; PMID:6330897 !$#accession A01376 !'##molecule_type DNA !'##residues 1-58 ##label DIA !'##cross-references GB:K01884; NID:g179497; PIDN:AAA51832.1; !1PID:g179498 GENETICS !$#gene GDB:BLYM !'##cross-references GDB:119038; OMIM:164830 !$#map_position 1p32-1p32 CLASSIFICATION #superfamily Blym-1 transforming protein KEYWORDS transforming protein SUMMARY #length 58 #molecular-weight 6727 #checksum 5783 SEQUENCE /// ENTRY TVHUA1 #type complete TITLE transforming protein bcl-2, splice form alpha - human ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1988 #sequence_revision 07-Jun-1996 #text_change 15-Oct-1999 ACCESSIONS C37332; A29409; S02452; A24428; A27622; B27622 REFERENCE A37332 !$#authors Eguchi, Y.; Ewert, D.L.; Tsujimoto, Y. !$#journal Nucleic Acids Res. (1992) 20:4187-4192 !$#title Isolation and characterization of the chicken bcl-2 gene: !1expression in a variety of tissues including lymphoid and !1neuronal organs in adult and embryo. !$#cross-references MUID:92375724; PMID:1508712 !$#accession C37332 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type DNA !'##residues 1-239 ##label EGU !'##note this report is a correction REFERENCE A29409 !$#authors Tsujimoto, Y.; Croce, C.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:5214-5218 !$#title Analysis of the structure, transcripts, and protein products !1of bcl-2, the gene involved in human follicular lymphoma. !$#cross-references MUID:86259760; PMID:3523487 !$#accession A29409 !'##molecule_type mRNA !'##residues 1-95,'A',97-109,'G',111-236,'S',238-239 ##label TSU !'##cross-references GB:M13994; NID:g179366; PIDN:AAA51813.1; !1PID:g179367 !'##note this sequence has been corrected in reference A37332 REFERENCE S02452 !$#authors Seto, M.; Jaeger, U.; Hockett, R.D.; Graninger, W.; Bennett, !1S.; Goldman, P.; Korsmeyer, S.J. !$#journal EMBO J. (1988) 7:123-131 !$#title Alternative promoters and exons, somatic mutation and !1deregulation of the Bcl-2--Ig fusion gene in lymphoma. !$#cross-references MUID:88196071; PMID:2834197 !$#accession S02452 !'##molecule_type mRNA !'##residues 1-239 ##label SET REFERENCE A24428 !$#authors Cleary, M.L.; Smith, S.D.; Sklar, J. !$#journal Cell (1986) 47:19-28 !$#title Cloning and structural analysis of cDNAs for bcl-2 and a !1hybrid bcl-2/immunoglobulin transcript resulting from the t !1(14;18) translocation. !$#cross-references MUID:87002488; PMID:2875799 !$#accession A24428 !'##molecule_type mRNA !'##residues 1-58,'T',60-116,'R',118-239 ##label CLE !'##cross-references GB:M14745; NID:g179370; PIDN:AAA35591.1; !1PID:g179371 REFERENCE A27622 !$#authors Hua, C.; Zorn, S.; Jensen, J.P.; Coupland, R.W.; Ko, H.S.; !1Wright, J.J.; Bakhshi, A. !$#journal Oncogene Res. (1988) 2:263-275 !$#title Consequences of the t(14;18) chromosomal translocation in !1follicular lymphoma: deregulated expression of a chimeric !1and mutated BCL-2 gene. !$#cross-references MUID:88217344; PMID:3285301 !$#accession A27622 !'##molecule_type mRNA !'##residues 1-58,'T',60-239 ##label HUA !$#accession B27622 !'##molecule_type DNA !'##residues 1-6,'S',8-58,'T',60-128,'C',130-239 ##label HUA2 !'##note the sequence was determined from the germline gene COMMENT Constitutive expression of BCL2 following t(14:18) !1chromosomal translocation is typically found in follicular !1lymphoma. GENETICS !$#gene GDB:BCL2 !'##cross-references GDB:119031; OMIM:151430 !$#map_position 18q21.3-18q21.3 FUNCTION !$#description blocks apoptosis in hematopoietic cells CLASSIFICATION #superfamily bcl transforming protein KEYWORDS alternative splicing; apoptosis; B-cell lymphoma; follicular !1lymphoma; proto-oncogene; transforming protein; !1transmembrane protein SUMMARY #length 239 #molecular-weight 26266 #checksum 8323 SEQUENCE /// ENTRY TVHUB1 #type complete TITLE transforming protein bcl-2, splice form beta - human ALTERNATE_NAMES apoptosis regulator bcl-2 ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 15-Oct-1999 ACCESSIONS B29409; I52566; D37332 REFERENCE A29409 !$#authors Tsujimoto, Y.; Croce, C.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:5214-5218 !$#title Analysis of the structure, transcripts, and protein products !1of bcl-2, the gene involved in human follicular lymphoma. !$#cross-references MUID:86259760; PMID:3523487 !$#accession B29409 !'##molecule_type mRNA !'##residues 1-205 ##label TSU !'##cross-references GB:M13995; NID:g179368; PIDN:AAA51814.1; !1PID:g179369 REFERENCE I52566 !$#authors Tanaka, S.; Louie, D.C.; Kant, J.A.; Reed, J.C. !$#journal Blood (1992) 79:229-237 !$#title Frequent incidence of somatic mutations in translocated BCL2 !1oncogenes of non-Hodgkin's lymphomas. !$#cross-references MUID:92096610; PMID:1339299 !$#accession I52566 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-131 ##label TAN !'##cross-references GB:S72602; NID:g241046; PIDN:AAD14111.1; !1PID:g4261811 REFERENCE A37332 !$#authors Eguchi, Y.; Ewert, D.L.; Tsujimoto, Y. !$#journal Nucleic Acids Res. (1992) 20:4187-4192 !$#title Isolation and characterization of the chicken bcl-2 gene: !1expression in a variety of tissues including lymphoid and !1neuronal organs in adult and embryo. !$#cross-references MUID:92375724; PMID:1508712 !$#accession D37332 !'##status preliminary; nucleic acid sequence not shown; not compared !1with conceptual translation !'##molecule_type DNA !'##residues 1-33,'E',34-95,'T',97-109,'R',111-205 ##label EGU GENETICS !$#gene GDB:BCL2 !'##cross-references GDB:119031; OMIM:151430 !$#map_position 18q21.3-18q21.3 FUNCTION !$#description blocks apoptosis in hematopoietic cells CLASSIFICATION #superfamily bcl transforming protein KEYWORDS alternative splicing; apoptosis; B-cell lymphoma; follicular !1lymphoma; proto-oncogene; transforming protein SUMMARY #length 205 #molecular-weight 22182 #checksum 1183 SEQUENCE /// ENTRY TVMSA1 #type complete TITLE transforming protein bcl-2-alpha - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 18-Jun-1999 ACCESSIONS A25960; E37332 REFERENCE A90893 !$#authors Negrini, M.; Silini, E.; Kozak, C.; Tsujimoto, Y.; Croce, !1C.M. !$#journal Cell (1987) 49:455-463 !$#title Molecular analysis of mbcl-2: structure and expression of !1the murine gene homologous to the human gene involved in !1follicular lymphoma. !$#cross-references MUID:87187643; PMID:3032455 !$#accession A25960 !'##molecule_type DNA !'##residues 1-236 ##label NEG !'##cross-references GB:L31532; GB:M16506; NID:g468336; PIDN:AAA37282.1; !1PID:g387109 REFERENCE A37332 !$#authors Eguchi, Y.; Ewert, D.L.; Tsujimoto, Y. !$#journal Nucleic Acids Res. (1992) 20:4187-4192 !$#title Isolation and characterization of the chicken bcl-2 gene: !1expression in a variety of tissues including lymphoid and !1neuronal organs in adult and embryo. !$#cross-references MUID:92375724; PMID:1508712 !$#accession E37332 !'##status preliminary; nucleic acid sequence not shown; not compared !1with conceptual translation !'##molecule_type DNA !'##residues 1-33,'E',34-220,'AL',223-236 ##label EGU GENETICS !$#gene BCL2 !$#introns 192/3 CLASSIFICATION #superfamily bcl transforming protein KEYWORDS alternative splicing; mitochondrion; transforming protein; !1transmembrane protein SUMMARY #length 236 #molecular-weight 26524 #checksum 6709 SEQUENCE /// ENTRY TVMSB1 #type complete TITLE transforming protein bcl-2-beta - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 18-Jun-1999 ACCESSIONS B25960 REFERENCE A90893 !$#authors Negrini, M.; Silini, E.; Kozak, C.; Tsujimoto, Y.; Croce, !1C.M. !$#journal Cell (1987) 49:455-463 !$#title Molecular analysis of mbcl-2: structure and expression of !1the murine gene homologous to the human gene involved in !1follicular lymphoma. !$#cross-references MUID:87187643; PMID:3032455 !$#accession B25960 !'##molecule_type DNA !'##residues 1-199 ##label NEG !'##cross-references GB:M16506; NID:g468335; PIDN:AAA37281.1; !1PID:g387110 GENETICS !$#gene BCL2 CLASSIFICATION #superfamily bcl transforming protein KEYWORDS alternative splicing; transforming protein SUMMARY #length 199 #molecular-weight 22299 #checksum 7397 SEQUENCE /// ENTRY TVTK #type fragment TITLE transforming protein rel - turkey (fragment) ORGANISM #formal_name Meleagris gallopavo #common_name common turkey DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 02-Jun-1994 ACCESSIONS A01377 REFERENCE A93003 !$#authors Wilhelmsen, K.C.; Eggleton, K.; Temin, H.M. !$#journal J. Virol. (1984) 52:172-182 !$#title Nucleotide acid sequences of the oncogene v-rel in !1reticuloendotheliosis virus strain T and its cellular !1homolog, the proto-oncogene c-rel. !$#cross-references MUID:85009850; PMID:6090694 !$#accession A01377 !'##molecule_type DNA !'##residues 1-530 ##label WIL !'##note the authors translated the codon GAA for residue 267 as Asp and !1AGT for residues 487 and 524 as Met GENETICS !$#gene rel CLASSIFICATION #superfamily rel transforming protein; rel homology KEYWORDS DNA binding; nucleus; phosphoprotein; proto-oncogene; !1transcription regulation; transforming protein FEATURE !$5-293 #domain rel homology #label REL\ !$289-292 #region nuclear location signal\ !$264 #binding_site phosphate (Ser) (covalent) (by !8cAMP-dependent kinase) #status predicted SUMMARY #length 530 #checksum 128 SEQUENCE /// ENTRY TVCHRL #type complete TITLE transforming protein rel - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 18-Jun-1999 ACCESSIONS A34098 REFERENCE A34098 !$#authors Hannink, M.; Temin, H.M. !$#journal Mol. Cell. Biol. (1989) 9:4323-4336 !$#title Transactivation of gene expression by nuclear and !1cytoplasmic rel proteins. !$#cross-references MUID:90066439; PMID:2555689 !$#accession A34098 !'##molecule_type mRNA !'##residues 1-595 ##label HAN !'##cross-references GB:M26381; NID:g211658; PIDN:AAA48721.1; !1PID:g211659 GENETICS !$#gene rel CLASSIFICATION #superfamily rel transforming protein; rel homology KEYWORDS DNA binding; nucleus; phosphoprotein; proto-oncogene; !1transcription regulation; transforming protein FEATURE !$4-292 #domain rel homology #label REL\ !$288-291 #region nuclear location signal\ !$263 #binding_site phosphate (Ser) (covalent) (by !8cAMP-dependent kinase) #status predicted SUMMARY #length 595 #molecular-weight 66650 #checksum 9823 SEQUENCE /// ENTRY VCVDA #type complete TITLE transforming protein rel - avian reticuloendotheliosis virus ORGANISM #formal_name avian reticuloendotheliosis virus DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 24-Sep-1999 ACCESSIONS A93974; A93003; A01378 REFERENCE A93974 !$#authors Stephens, R.M.; Rice, N.R.; Hiebsch, R.R.; Bose Jr., H.R.; !1Gilden, R.V. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:6229-6233 !$#title Nucleotide sequence of v-rel: the oncogene of !1reticuloendotheliosis virus. !$#cross-references MUID:84016028; PMID:6312449 !$#accession A93974 !'##molecule_type DNA !'##residues 1-503 ##label STE !'##cross-references GB:K00555; GB:X02759; NID:g209713; PIDN:AAA99199.1; !1PID:g209714 REFERENCE A93003 !$#authors Wilhelmsen, K.C.; Eggleton, K.; Temin, H.M. !$#journal J. Virol. (1984) 52:172-182 !$#title Nucleotide acid sequences of the oncogene v-rel in !1reticuloendotheliosis virus strain T and its cellular !1homolog, the proto-oncogene c-rel. !$#cross-references MUID:85009850; PMID:6090694 !$#accession A93003 !'##molecule_type DNA !'##residues 1-503 ##label WIL !'##cross-references GB:K00555; GB:X02759; NID:g209713; PIDN:AAA99199.1; !1PID:g209714 !'##experimental_source strain T GENETICS !$#gene env-rel-env CLASSIFICATION #superfamily rel transforming protein; rel homology KEYWORDS DNA binding; nucleus; oncogene; phosphoprotein; !1transcription regulation; transforming protein FEATURE !$1-12 #region env polyprotein gene-derived\ !$16-304 #domain rel homology #label REL\ !$300-303 #region nuclear location signal\ !$485-503 #region env polyprotein gene-derived\ !$275 #binding_site phosphate (Ser) (covalent) (by !8cAMP-dependent kinase) #status predicted SUMMARY #length 503 #molecular-weight 55910 #checksum 335 SEQUENCE /// ENTRY A30350 #type complete TITLE dorsal protein - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A30350; A33757 REFERENCE A30350 !$#authors Steward, R. !$#journal Science (1987) 238:692-694 !$#title Dorsal, an embryonic polarity gene in Drosophila, is !1homologous to the vertebrate proto-oncogene, c-rel. !$#cross-references MUID:88042799; PMID:3118464 !$#accession A30350 !'##molecule_type mRNA !'##residues 1-392,'LGFLIGRLLSSHPRRSRCRHRATTTTTARPRPTTWPPRSA',434-678 !1##label STE !'##cross-references GB:M23702 !'##note this sequence has been revised in reference A33757 REFERENCE A33757 !$#authors Steward, R. !$#journal Cell (1989) 59:1179-1188 !$#title Relocalization of the dorsal protein from the cytoplasm to !1the nucleus correlates with its function. !$#cross-references MUID:90090617; PMID:2598266 !$#accession A33757 !'##molecule_type DNA !'##residues 390-440 ##label ST2 GENETICS !$#gene FlyBase:dl !'##cross-references FlyBase:FBgn0000462 CLASSIFICATION #superfamily dorsal protein; rel homology KEYWORDS DNA binding; nucleus; phosphoprotein; transcription !1regulation FEATURE !$47-341 #domain rel homology #label REL\ !$335-340 #region nuclear location signal\ !$312 #binding_site phosphate (Ser) (covalent) (by !8cAMP-dependent kinase) #status predicted SUMMARY #length 678 #molecular-weight 75475 #checksum 5412 SEQUENCE /// ENTRY TVHUDB #type complete TITLE transforming protein dbl precursor - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 02-Sep-1997 ACCESSIONS A30040 REFERENCE A30040 !$#authors Ron, D.; Tronick, S.R.; Aaronson, S.A.; Eva, A. !$#journal EMBO J. (1988) 7:2465-2473 !$#title Molecular cloning and characterization of the human dbl !1proto-oncogene: evidence that its overexpression is !1sufficient to transform NIH/3T3 cells. !$#cross-references MUID:89052660; PMID:3056717 !$#accession A30040 !'##molecule_type mRNA !'##residues 1-925 ##label RON !'##cross-references EMBL:X12556 GENETICS !$#gene GDB:MCF2 !'##cross-references GDB:120168; OMIM:311030 !$#map_position Xq26.3-Xq27.1 CLASSIFICATION #superfamily dbl transforming protein; CDC24 homology; !1pleckstrin repeat homology KEYWORDS oncogene; phosphoprotein; transforming protein FEATURE !$495-675 #domain CDC24 homology #label CD24\ !$498-925 #product transforming protein dbl #status predicted !8#label DBL\ !$703-807 #domain pleckstrin repeat homology #label PLK SUMMARY #length 925 #molecular-weight 107640 #checksum 7016 SEQUENCE /// ENTRY TVFVJN #type complete TITLE transforming protein jun - avian sarcoma virus 17 ORGANISM #formal_name avian sarcoma virus 17 DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Feb-1997 ACCESSIONS A29870 REFERENCE A29870 !$#authors Maki, Y.; Bos, T.J.; Davis, C.; Starbuck, M.; Vogt, P.K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:2848-2852 !$#title Avian sarcoma virus 17 carries the jun oncogene. !$#cross-references MUID:87204225; PMID:3033666 !$#accession A29870 !'##molecule_type DNA !'##residues 1-296 ##label MAK COMMENT This protein is translated as a gag-jun polyprotein. GENETICS !$#gene jun CLASSIFICATION #superfamily jun transforming protein; fos/jun DNA-binding !1domain homology KEYWORDS DNA binding; leucine zipper; oncogene; transcription !1regulation; transforming protein FEATURE !$212-252 #domain fos/jun DNA-binding domain homology #label !8FJD\ !$245-273 #region leucine zipper motif SUMMARY #length 296 #molecular-weight 32477 #checksum 7209 SEQUENCE /// ENTRY TVQJUN #type complete TITLE transforming protein jun - Japanese quail ORGANISM #formal_name Coturnix coturnix japonica #common_name Japanese quail DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 18-Jun-1999 ACCESSIONS S05963 REFERENCE S05963 !$#authors Brun, G.; La Vista, N.; Dangy, J.P.; Castellazzi, M. !$#journal Nucleic Acids Res. (1989) 17:6393 !$#title Nucleotide sequence of the quail c-jun protooncogene. !$#cross-references MUID:89366673; PMID:2505235 !$#accession S05963 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-313 ##label BRU !'##cross-references EMBL:X15547; NID:g62639; PIDN:CAA33553.1; !1PID:g62640 GENETICS !$#gene jun CLASSIFICATION #superfamily jun transforming protein; fos/jun DNA-binding !1domain homology KEYWORDS DNA binding; leucine zipper; oncogene; transcription !1regulation; transforming protein FEATURE !$229-269 #domain fos/jun DNA-binding domain homology #label !8FJD\ !$262-290 #region leucine zipper motif SUMMARY #length 313 #molecular-weight 34341 #checksum 3736 SEQUENCE /// ENTRY TVHUJN #type complete TITLE transcription factor AP-1 - human ALTERNATE_NAMES transforming protein jun ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1989 #sequence_revision 31-Dec-1989 #text_change 02-Sep-1997 ACCESSIONS A31264; A30009; A38441 REFERENCE A94218 !$#authors Hattori, K.; Angel, P.; Le Beau, M.M.; Karin, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:9148-9152 !$#title Structure and chromosomal localization of the functional !1intronless human JUN protooncogene. !$#cross-references MUID:89057892; PMID:3194415 !$#accession A31264 !'##molecule_type DNA !'##residues 1-331 ##label HAT REFERENCE A94296 !$#authors Bohmann, D.; Bos, T.J.; Admon, A.; Nishimura, T.; Vogt, !1P.K.; Tjian, R. !$#journal Science (1987) 238:1386-1392 !$#title Human proto-oncogene c-jun encodes a DNA binding protein !1with structural and functional properties of transcription !1factor AP-1. !$#cross-references MUID:88070595; PMID:2825349 !$#accession A30009 !'##molecule_type mRNA !'##residues 1-10,'G',12-13,'F',15-331 ##label SAA REFERENCE A38441 !$#authors Boyle, W.J.; Smeal, T.; Defize, L.H.K.; Angel, P.; Woodgett, !1J.R.; Karin, M.; Hunter, T. !$#journal Cell (1991) 64:573-584 !$#title Activation of protein kinase C decreases phosphorylation of !1c-Jun at sites that negatively regulate its DNA-binding !1activity. !$#cross-references MUID:91121514; PMID:1846781 !$#accession A38441 !'##molecule_type protein !'##residues 226-252 ##label BOY GENETICS !$#gene GDB:JUN !'##cross-references GDB:120114; OMIM:165160 !$#map_position 1p32-1p31 CLASSIFICATION #superfamily jun transforming protein; fos/jun DNA-binding !1domain homology KEYWORDS DNA binding; leucine zipper; phosphoprotein; proto-oncogene; !1transcription factor; transforming protein FEATURE !$247-287 #domain fos/jun DNA-binding domain homology #label !8FJD\ !$280-308 #region leucine zipper motif\ !$239 #binding_site phosphate (Thr) (covalent) (by glycogen !8synthase kinase 3) #status experimental\ !$243,249 #binding_site phosphate (Ser) (covalent) (by glycogen !8synthase kinase 3) #status experimental SUMMARY #length 331 #molecular-weight 35661 #checksum 2881 SEQUENCE /// ENTRY TVMSJA #type complete TITLE transcription factor AP-1 - mouse ALTERNATE_NAMES fos-associated 39K protein; protein PEA1; transcription factor, TGACTCA-binding; transforming protein jun-A ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 18-Jun-1999 ACCESSIONS A31345; S04683; S04537 REFERENCE A31345 !$#authors Ryder, K.; Nathans, D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:8464-8467 !$#title Induction of protooncogene c-jun by serum growth factors. !$#cross-references MUID:89042204; PMID:3186736 !$#accession A31345 !'##molecule_type mRNA !'##residues 1-334 ##label RYD !'##cross-references GB:J04115; NID:g192577; PIDN:AAA37419.1; !1PID:g309169 REFERENCE S04683 !$#authors Lamph, W.W.; Wamsley, P.; Sassone-Corsi, P.; Verma, I.M. !$#journal Nature (1988) 334:629-631 !$#title Induction of proto-oncogene JUN/AP-1 by serum and TPA. !$#cross-references MUID:88302467; PMID:2457172 !$#accession S04683 !'##molecule_type mRNA !'##residues 1-334 ##label LAM !'##cross-references EMBL:X12740; NID:g52762; PIDN:CAA31236.1; !1PID:g52763 REFERENCE S04537 !$#authors Ryseck, R.P.; Hirai, S.I.; Yaniv, M.; Bravo, R. !$#journal Nature (1988) 334:535-537 !$#title Transcriptional activation of c-jun during the G(0)/G(1) !1transition in mouse fibroblasts. !$#cross-references MUID:88302446; PMID:3136397 !$#accession S04537 !'##molecule_type mRNA !'##residues 1-182,'C',184-334 ##label RYS !'##cross-references EMBL:X12761; NID:g52758; PIDN:CAA31252.1; !1PID:g52759 GENETICS !$#gene jun-A CLASSIFICATION #superfamily jun transforming protein; fos/jun DNA-binding !1domain homology KEYWORDS DNA binding; leucine zipper; phosphoprotein; proto-oncogene; !1transcription factor; transforming protein FEATURE !$250-290 #domain fos/jun DNA-binding domain homology #label !8FJD\ !$283-311 #region leucine zipper motif SUMMARY #length 334 #molecular-weight 35944 #checksum 4374 SEQUENCE /// ENTRY TVMSJD #type complete TITLE transforming protein jun-D - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 18-Jun-1999 ACCESSIONS A32158; S04461; A35013 REFERENCE A32158 !$#authors Ryder, K.; Lanahan, A.; Perez-Albuerne, E.; Nathans, D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:1500-1503 !$#title Jun-D: a third member of the Jun gene family. !$#cross-references MUID:89160806; PMID:2493644 !$#accession A32158 !'##molecule_type mRNA !'##residues 1-341 ##label RYD !'##cross-references GB:J04509; NID:g198486; PIDN:AAA39344.1; !1PID:g293680 REFERENCE S04461 !$#authors Hirai, S.I.; Ryseck, R.P.; Mechta, F.; Bravo, R.; Yaniv, M. !$#journal EMBO J. (1989) 8:1433-1439 !$#title Characterization of junD: a new member of the jun !1proto-oncogene family. !$#cross-references MUID:89356612; PMID:2504580 !$#accession S04461 !'##molecule_type mRNA !'##residues 1-341 ##label HIR !'##cross-references EMBL:X15358; NID:g52765; PIDN:CAA33418.1; !1PID:g52766 REFERENCE A35013 !$#authors Li, L.; Hu, J.S.; Olson, E.N. !$#journal J. Biol. Chem. (1990) 265:1556-1562 !$#title Different members of the jun proto-oncogene family exhibit !1distinct patterns of expression in response to type beta !1transforming growth factor. !$#cross-references MUID:90110219; PMID:2104845 !$#accession A35013 !'##status preliminary !'##molecule_type mRNA !'##residues 1-4,'L',6-60,'DE',63-316,'HV',319-341 ##label LIL !'##cross-references GB:J05205; NID:g198488; PIDN:AAA39345.1; !1PID:g293681 GENETICS !$#gene jun-D CLASSIFICATION #superfamily jun transforming protein; fos/jun DNA-binding !1domain homology KEYWORDS DNA binding; leucine zipper; transcription regulation; !1transforming protein FEATURE !$257-297 #domain fos/jun DNA-binding domain homology #label !8FJD\ !$290-318 #region leucine zipper motif SUMMARY #length 341 #molecular-weight 34904 #checksum 3375 SEQUENCE /// ENTRY TVHUJD #type complete TITLE transforming protein jun-D - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 18-Jun-1999 ACCESSIONS S10184 REFERENCE S10183 !$#authors Nomura, N.; Ide, M.; Sasamoto, S.; Matsui, M.; Date, T.; !1Ishizaki, R. !$#journal Nucleic Acids Res. (1990) 18:3047-3048 !$#title Isolation of human cDNA clones of jun-related genes, jun-B !1and jun-D. !$#cross-references MUID:90272414; PMID:2112242 !$#accession S10184 !'##molecule_type mRNA !'##residues 1-303 ##label NOM !'##cross-references EMBL:X51346; NID:g34016; PIDN:CAA35739.1; !1PID:g34017 GENETICS !$#gene GDB:JUND !'##cross-references GDB:125380; OMIM:165162 !$#map_position 19p13.1-19p13.1 CLASSIFICATION #superfamily jun transforming protein; fos/jun DNA-binding !1domain homology KEYWORDS DNA binding; leucine zipper; proto-oncogene; transcription !1regulation; transforming protein FEATURE !$219-259 #domain fos/jun DNA-binding domain homology #label !8FJD\ !$252-280 #region leucine zipper motif SUMMARY #length 303 #molecular-weight 31102 #checksum 2198 SEQUENCE /// ENTRY TVFFJD #type complete TITLE transforming protein jun-D - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 18-Jun-1999 ACCESSIONS A36011; B35847 REFERENCE A36011 !$#authors Zhang, K.; Chaillet, J.R.; Perkins, L.A.; Halazonetis, T.D.; !1Perrimon, N. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:6281-6285 !$#title Drosophila homolog of the mammalian jun oncogene is !1expressed during embryonic development and activates !1transcription in mammalian cells. !$#cross-references MUID:90349599; PMID:1696724 !$#accession A36011 !'##molecule_type DNA !'##residues 1-289 ##label ZHA !'##cross-references GB:M36181; NID:g157773; PIDN:AAA28650.1; !1PID:g157774 REFERENCE A35847 !$#authors Perkins, K.K.; Admon, A.; Patel, N.; Tjian, R. !$#journal Genes Dev. (1990) 4:822-834 !$#title The Drosophila Fos-related AP-1 protein is a developmentally !1regulated transcription factor. !$#cross-references MUID:90337318; PMID:2116361 !$#accession B35847 !'##status preliminary !'##molecule_type mRNA !'##residues 1-266,'QL',269-289 ##label PER !'##cross-references GB:X54144; NID:g9120; PIDN:CAA38083.1; PID:g9121 GENETICS !$#gene jun-D !'##cross-references FlyBase:FBgn0001291 CLASSIFICATION #superfamily jun transforming protein; fos/jun DNA-binding !1domain homology KEYWORDS DNA binding; leucine zipper; oncogene; transcription !1regulation; transforming protein FEATURE !$207-247 #domain fos/jun DNA-binding domain homology #label !8FJD\ !$240-261 #region leucine zipper motif SUMMARY #length 289 #molecular-weight 31016 #checksum 1900 SEQUENCE /// ENTRY TVMSJB #type complete TITLE transforming protein jun-B - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 18-Jun-1999 ACCESSIONS A28963 REFERENCE A28963 !$#authors Ryder, K.; Lau, L.F.; Nathans, D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:1487-1491 !$#title A gene activated by growth factors is related to the !1oncogene v-jun. !$#cross-references MUID:88144462; PMID:3422745 !$#accession A28963 !'##molecule_type mRNA !'##residues 1-344 ##label RYD !'##cross-references GB:J03236; NID:g198484; PIDN:AAA39343.1; !1PID:g293679 GENETICS !$#gene jun-B CLASSIFICATION #superfamily jun transforming protein; fos/jun DNA-binding !1domain homology KEYWORDS DNA binding; leucine zipper; transcription regulation; !1transforming protein FEATURE !$260-300 #domain fos/jun DNA-binding domain homology #label !8FJD\ !$293-321 #region leucine zipper motif SUMMARY #length 344 #molecular-weight 35765 #checksum 8248 SEQUENCE /// ENTRY TVHUJB #type complete TITLE transforming protein jun-B - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 18-Jun-1999 ACCESSIONS S10183; A33753 REFERENCE S10183 !$#authors Nomura, N.; Ide, M.; Sasamoto, S.; Matsui, M.; Date, T.; !1Ishizaki, R. !$#journal Nucleic Acids Res. (1990) 18:3047-3048 !$#title Isolation of human cDNA clones of jun-related genes, jun-B !1and jun-D. !$#cross-references MUID:90272414; PMID:2112242 !$#accession S10183 !'##molecule_type mRNA !'##residues 1-347 ##label NOM !'##cross-references EMBL:X51345; NID:g34014; PIDN:CAA35738.1; !1PID:g34015 REFERENCE A33753 !$#authors Schuette, J.; Viallet, J.; Nau, M.; Segal, S.; Fedorko, J.; !1Minna, J. !$#journal Cell (1989) 59:987-997 !$#title jun-B inhibits and c-fos stimulates the transforming and !1trans-activating activities of c-jun. !$#cross-references MUID:90090625; PMID:2513129 !$#accession A33753 !'##molecule_type DNA !'##residues 1-347 ##label SCH !'##cross-references EMBL:M29039; NID:g186626; PIDN:AAA59198.1; !1PID:g386840 GENETICS !$#gene GDB:JUNB !'##cross-references GDB:125379; OMIM:165161 !$#map_position 19p13.2-19p13.2 CLASSIFICATION #superfamily jun transforming protein; fos/jun DNA-binding !1domain homology KEYWORDS DNA binding; leucine zipper; transcription factor; !1transforming protein FEATURE !$263-303 #domain fos/jun DNA-binding domain homology #label !8FJD\ !$296-324 #region leucine zipper motif SUMMARY #length 347 #molecular-weight 35879 #checksum 9081 SEQUENCE /// ENTRY TVHUF1 #type complete TITLE transforming protein fos - human ORGANISM #formal_name Homo sapiens #common_name man DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 24-Sep-1999 ACCESSIONS A01342; I58359; S09375 REFERENCE A01342 !$#authors van Straaten, F.; Muller, R.; Curran, T.; Van Beveren, C.; !1Verma, I.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:3183-3187 !$#title Complete nucleotide sequence of a human c-onc gene: deduced !1amino acid sequence of the human c-fos protein. !$#cross-references MUID:83221560; PMID:6574479 !$#accession A01342 !'##molecule_type DNA !'##residues 1-380 ##label VAN !'##cross-references GB:V01512; NID:g29903; PIDN:CAA24756.1; PID:g29904 REFERENCE S09374 !$#authors Nakabeppu, Y.; Nathans, D. !$#journal EMBO J. (1989) 8:3833-3841 !$#title The basic region of Fos mediates specific DNA binding. !$#cross-references MUID:90059986; PMID:2511004 !$#contents annotation !$#note engineered chimeric forms including residues 121-207 REFERENCE I58359 !$#authors Roux, P.; Verrier, B.; Klein, B.; Niccolino, M.; Marty, L.; !1Alexandre, C.; Piechaczyk, M. !$#journal Oncogene (1991) 6:2155-2160 !$#title Retrovirus-mediated gene transfer of a human c-fos cDNA into !1mouse bone marrow stromal cells. !$#cross-references MUID:92050815; PMID:1658710 !$#accession I58359 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-6 ##label RES !'##cross-references GB:S65138; NID:g238776; PIDN:AAB20306.1; !1PID:g238778 GENETICS !$#gene GDB:FOS !'##cross-references GDB:119917; OMIM:164810 !$#map_position 14q24.3-14q24.3 !$#introns 47/3; 131/3; 167/3 CLASSIFICATION #superfamily fos transforming protein; fos/jun DNA-binding !1domain homology KEYWORDS DNA binding; heterodimer; leucine zipper FEATURE !$132-172 #domain fos/jun DNA-binding domain homology #label !8FJD\ !$165-193 #region leucine zipper motif SUMMARY #length 380 #molecular-weight 40695 #checksum 4677 SEQUENCE /// ENTRY TVMSF #type complete TITLE transforming protein fos - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 24-Sep-1999 ACCESSIONS A01343 REFERENCE A03986 !$#authors Van Beveren, C.; van Straaten, F.; Curran, T.; Mueller, R.; !1Verma, I.M. !$#journal Cell (1983) 32:1241-1255 !$#title Analysis of FBJ-MuSV provirus and c-fos (mouse) gene reveals !1that viral and cellular fos gene products have different !1carboxy termini. !$#cross-references MUID:83180421; PMID:6301687 !$#accession A01343 !'##molecule_type DNA !'##residues 1-380 ##label VAN !'##cross-references GB:V00727; NID:g50399; PIDN:CAA24105.1; PID:g50400 GENETICS !$#gene c-fos !$#introns 47/3; 131/3; 167/3 CLASSIFICATION #superfamily fos transforming protein; fos/jun DNA-binding !1domain homology KEYWORDS DNA binding; leucine zipper FEATURE !$132-172 #domain fos/jun DNA-binding domain homology #label !8FJD\ !$165-193 #region leucine zipper motif SUMMARY #length 380 #molecular-weight 40838 #checksum 6299 SEQUENCE /// ENTRY TVRTFS #type complete TITLE transforming protein fos - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 18-Jun-1999 ACCESSIONS A28263; I59159 REFERENCE A28263 !$#authors Curran, T.; Gordon, M.B.; Rubino, K.L.; Sambucetti, L.C. !$#journal Oncogene (1987) 2:79-84 !$#title Isolation and characterization of the c-fos(rat) cDNA and !1analysis of post-translational modification in vitro. !$#cross-references MUID:88143713; PMID:3325886 !$#accession A28263 !'##molecule_type mRNA !'##residues 1-380 ##label CUR !'##cross-references GB:X06769; NID:g55933; PIDN:CAA29937.1; PID:g55934 REFERENCE I59159 !$#authors Abate, C.; Luk, D.; Gentz, R.; Rauscher, F.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:1032-1036 !$#title Expression and purification of the leucine zipper and !1DNA-binding domains of Fos and Jun: Both Fos and Jun contact !1DNA directly. !$#cross-references MUID:90138931; PMID:2105492 !$#accession I59159 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 'S',118-211 ##label RES !'##cross-references GB:M34001; NID:g207684; PIDN:AAA42348.1; !1PID:g207685 GENETICS !$#gene fos CLASSIFICATION #superfamily fos transforming protein; fos/jun DNA-binding !1domain homology KEYWORDS DNA binding; leucine zipper; transforming protein FEATURE !$132-172 #domain fos/jun DNA-binding domain homology #label !8FJD\ !$165-193 #region leucine zipper motif SUMMARY #length 380 #molecular-weight 40926 #checksum 9113 SEQUENCE /// ENTRY TVMVFB #type fragment TITLE transforming protein fos-fox - FBR murine osteosarcoma virus (provirus) (fragment) CONTAINS fragment of transforming protein fos; fragment of transforming protein fox ORGANISM #formal_name FBR murine osteosarcoma virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Feb-1997 ACCESSIONS B23244 REFERENCE A23244 !$#authors Van Beveren, C.; Enami, S.; Curran, T.; Verma, I.M. !$#journal Virology (1984) 135:229-243 !$#title FBR murine osteosarcoma virus. II. Nucleotide sequence of !1the provirus reveals that the genome contains sequences !1acquired from two cellular genes. !$#cross-references MUID:84225828; PMID:6203215 !$#accession B23244 !'##molecule_type mRNA !'##residues 1-244 ##label VAN !'##cross-references EMBL:K02712 COMMENT This protein is synthesized as a gag-fos-fox polyprotein. GENETICS !$#gene fos-fox CLASSIFICATION #superfamily fos transforming protein; fos/jun DNA-binding !1domain homology KEYWORDS DNA binding; leucine zipper; transforming protein FEATURE !$1-236 #product transforming protein fos (fragment) #status !8predicted #label FOS\ !$108-148 #domain fos/jun DNA-binding domain homology #label !8FJD\ !$141-169 #region leucine zipper motif\ !$237-244 #product transforming protein fox (fragment) #status !8predicted #label FOX SUMMARY #length 244 #checksum 3011 SEQUENCE /// ENTRY TVMVJ #type complete TITLE transforming protein fos - FBJ murine osteosarcoma virus ORGANISM #formal_name FBJ murine osteosarcoma virus DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 28-May-1999 ACCESSIONS A01344 REFERENCE A03986 !$#authors Van Beveren, C.; van Straaten, F.; Curran, T.; Mueller, R.; !1Verma, I.M. !$#journal Cell (1983) 32:1241-1255 !$#title Analysis of FBJ-MuSV provirus and c-fos (mouse) gene reveals !1that viral and cellular fos gene products have different !1carboxy termini. !$#cross-references MUID:83180421; PMID:6301687 !$#accession A01344 !'##molecule_type DNA !'##residues 1-381 ##label VAN !'##cross-references GB:V01184; GB:J02084; NID:g61642; PIDN:CAA24505.1; !1PID:g61643 GENETICS !$#gene fos CLASSIFICATION #superfamily fos transforming protein; fos/jun DNA-binding !1domain homology KEYWORDS DNA binding; leucine zipper; transforming protein FEATURE !$132-172 #domain fos/jun DNA-binding domain homology #label !8FJD\ !$165-193 #region leucine zipper motif SUMMARY #length 381 #molecular-weight 41647 #checksum 7743 SEQUENCE /// ENTRY TVCHFS #type complete TITLE transforming protein fos - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 18-Jun-1999 ACCESSIONS A28368; A34073 REFERENCE A28368 !$#authors Moelders, H.; Jenuwein, T.; Adamkiewicz, J.; Mueller, R. !$#journal Oncogene (1987) 1:377-385 !$#title Isolation and structural analysis of a biologically active !1chicken c-fos cDNA: identification of evolutionarily !1conserved domains in fos protein. !$#cross-references MUID:88262231; PMID:3330781 !$#accession A28368 !'##molecule_type mRNA !'##residues 1-367 ##label MOE !'##cross-references GB:M37000; NID:g211469; PIDN:AAA48670.1; !1PID:g211470 REFERENCE A34073 !$#authors Fujiwara, K.T.; Ashida, K.; Nishina, H.; Iba, H.; Miyajima, !1N.; Nishizawa, M.; Kawai, S. !$#journal J. Virol. (1987) 61:4012-4018 !$#title The chicken c-fos gene: cloning and nucleotide sequence !1analysis. !$#cross-references MUID:88062957; PMID:3316710 !$#accession A34073 !'##molecule_type DNA !'##residues 1-367 ##label FUJ !'##cross-references GB:M18043; NID:g211467; PIDN:AAA76823.1; !1PID:g211468 !'##note the authors translated the codon AAC for residue 90 as Asp GENETICS !$#gene fos !$#introns 47/3; 130/3; 166/3 CLASSIFICATION #superfamily fos transforming protein; fos/jun DNA-binding !1domain homology KEYWORDS DNA binding; leucine zipper; transforming protein FEATURE !$131-171 #domain fos/jun DNA-binding domain homology #label !8FJD\ !$164-192 #region leucine zipper motif SUMMARY #length 367 #molecular-weight 39004 #checksum 7007 SEQUENCE /// ENTRY TVFVF4 #type complete TITLE transforming protein fos - avian retrovirus NK24 ORGANISM #formal_name avian retrovirus NK24 DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 26-May-1995 ACCESSIONS B34071 REFERENCE A34071 !$#authors Nishizawa, M.; Goto, N.; Kawai, S. !$#journal J. Virol. (1987) 61:3733-3740 !$#title An avian transforming retrovirus isolated from a !1nephroblastoma that carries the fos gene as the oncogene. !$#cross-references MUID:88062920; PMID:2824811 !$#accession B34071 !'##molecule_type DNA !'##residues 1-322 ##label NIS GENETICS !$#gene fos CLASSIFICATION #superfamily fos transforming protein; fos/jun DNA-binding !1domain homology KEYWORDS DNA binding; leucine zipper; transforming protein FEATURE !$86-126 #domain fos/jun DNA-binding domain homology #label !8FJD\ !$119-147 #region leucine zipper motif SUMMARY #length 322 #molecular-weight 34333 #checksum 9324 SEQUENCE /// ENTRY TVMSFB #type complete TITLE transforming protein fos-B - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 21-Jul-2000 ACCESSIONS S35477; S04108 REFERENCE S35477 !$#authors Lazo, P.S.; Dorfman, K.; Noguchi, T.; Mattei, M.G.; Bravo, !1R. !$#journal Nucleic Acids Res. (1992) 20:343-350 !$#title Structure and mapping of the fosB gene. FosB downregulates !1the activity of the fosB promoter. !$#cross-references MUID:92158623; PMID:1741260 !$#accession S35477 !'##status preliminary !'##molecule_type DNA !'##residues 1-338 ##label LAZ !'##cross-references EMBL:M77748; NID:g4235385; PIDN:AAD13196.1; !1PID:g4235387 REFERENCE S04108 !$#authors Zerial, M.; Toschi, L.; Ryseck, R.P.; Schuermann, M.; !1Mueller, R.; Bravo, R. !$#journal EMBO J. (1989) 8:805-813 !$#title The product of a novel growth factor activated gene, fos B, !1interacts with JUN proteins enhancing their DNA binding !1activity. !$#cross-references MUID:89251612; PMID:2498083 !$#accession S04108 !'##molecule_type mRNA !'##residues 1-338 ##label ZER !'##cross-references GB:X14897; NID:g50991; PIDN:CAA33026.1; PID:g50992 GENETICS !$#gene fos-B !$#introns 42/3; 149/3; 185/3 CLASSIFICATION #superfamily fos transforming protein; fos/jun DNA-binding !1domain homology KEYWORDS DNA binding; leucine zipper; nucleus; transforming protein FEATURE !$150-190 #domain fos/jun DNA-binding domain homology #label !8FJD\ !$183-211 #region leucine zipper motif SUMMARY #length 338 #molecular-weight 35976 #checksum 2324 SEQUENCE /// ENTRY TVRTFR #type complete TITLE transforming protein fra-1 - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 01-Dec-2000 ACCESSIONS A27722; I57559 REFERENCE A27722 !$#authors Cohen, D.R.; Curran, T. !$#journal Mol. Cell. Biol. (1988) 8:2063-2069 !$#title fra-1: a serum-inducible, cellular immediate-early gene that !1encodes a fos-related antigen. !$#cross-references MUID:88261282; PMID:3133553 !$#accession A27722 !'##molecule_type mRNA !'##residues 1-275 ##label COH !'##cross-references GB:M19651; NID:g204174; PIDN:AAA41171.1; !1PID:g204175 !'##experimental_source Fischer F2408 embryo fibroblast cell line 208F REFERENCE I57559 !$#authors Bergers, G.; Graninger, P.; Braselmann, S.; Wrighton, C.; !1Busslinger, M. !$#journal Mol. Cell. Biol. (1995) 15:3748-3758 !$#title Transcriptional activation of the fra-1 gene by AP-1 is !1mediated by regulatory sequences in the first intron. !$#cross-references MUID:95311973; PMID:7791782 !$#accession I57559 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-43 ##label RES !'##cross-references EMBL:U24154; NID:g1079522; PIDN:AAA82045.1; !1PID:g1079523 COMMENT This protein is a fos-related antigen (fra) that may bind to !1DNA. GENETICS !$#gene fra-1 !$#introns 35/3 CLASSIFICATION #superfamily fos transforming protein; fos/jun DNA-binding !1domain homology KEYWORDS DNA binding; leucine zipper; transforming protein FEATURE !$102-142 #domain fos/jun DNA-binding domain homology #label !8FJD\ !$135-163 #region leucine zipper motif SUMMARY #length 275 #molecular-weight 30115 #checksum 7844 SEQUENCE /// ENTRY A36299 #type complete TITLE transcription factor hXBP-1 - human ALTERNATE_NAMES DNA-binding protein TREB5 ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A36299; S12559; A47490 REFERENCE A36299 !$#authors Liou, H.C.; Boothby, M.R.; Finn, P.W.; Davidon, R.; Nabavi, !1N.; Zeleznik-Le, N.J.; Ting, J.P.Y.; Glimcher, L.H. !$#journal Science (1990) 247:1581-1583 !$#title A new member of the leucine zipper class of proteins that !1binds to the HLA DRalpha promoter. !$#cross-references MUID:90208323; PMID:2321018 !$#accession A36299 !'##status preliminary !'##molecule_type mRNA !'##residues 1-260 ##label LIO !'##cross-references GB:M31627; NID:g184485; PIDN:AAA36031.1; !1PID:g306893 REFERENCE S12559 !$#authors Yoshimura, T.; Fujisawa, J.I.; Yoshida, M. !$#journal EMBO J. (1990) 9:2537-2542 !$#title Multiple cDNA clones encoding nuclear proteins that bind to !1the tax-dependent enhancer of HTLV-1: all contain a leucine !1zipper structure and basic amino acid domain. !$#cross-references MUID:90316112; PMID:2196176 !$#accession S12559 !'##molecule_type DNA !'##residues 1-32,'GQA',35-260 ##label YOS !'##cross-references EMBL:X55543; NID:g287644; PIDN:CAA39149.1; !1PID:g287645 REFERENCE A47490 !$#authors Ponath, P.D.; Fass, D.; Liou, H.C.; Glimcher, L.H.; !1Strominger, J.L. !$#journal J. Biol. Chem. (1993) 268:17074-17082 !$#title The regulatory gene, hXBP-1, and its target, HLA-DRA, !1utilize both common and distinct regulatory elements and !1protein complexes. !$#cross-references MUID:93352484; PMID:8349596 !$#accession A47490 !'##status preliminary !'##molecule_type DNA !'##residues 1-32,'GQA',35-128,'T',130-192,'F',194-198,'R',200-260 !1##label PON !'##cross-references GB:L13850 !'##note authors translated the codon ACC for residue 130 as Asn, AAG !1for residue 151 as Leu, TTC for residue 194 as Leu, and AGG !1for residue 200 as Ser GENETICS !$#gene GDB:XBP1; XBP2 !'##cross-references GDB:131393; OMIM:194355 !$#map_position 22pter-22qter !$#introns 76/3; 108/3; 151/3; 200/3 CLASSIFICATION #superfamily X box-binding protein 1; fos/jun DNA-binding !1domain homology KEYWORDS DNA binding; leucine zipper; nucleus; transcription !1regulation FEATURE !$64-104 #domain fos/jun DNA-binding domain homology #label !8FJD SUMMARY #length 260 #molecular-weight 28666 #checksum 2791 SEQUENCE /// ENTRY RGBYA2 #type complete TITLE amino acid biosynthesis regulatory protein - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YEL009c ORGANISM #formal_name Saccharomyces cerevisiae DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 21-Jul-2000 ACCESSIONS A03605; S50450; A03604 REFERENCE A03605 !$#authors Hinnebusch, A.G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:6442-6446 !$#title Evidence for translational regulation of the activator of !1general amino acid control in yeast. !$#cross-references MUID:85038531; PMID:6387704 !$#accession A03605 !'##molecule_type DNA !'##residues 1-281 ##label HIN !'##cross-references EMBL:K02205; NID:g171581; PIDN:AAA34640.1; !1PID:g171584 REFERENCE S50428 !$#authors Dietrich, F.S. !$#submission submitted to the EMBL Data Library, December 1994 !$#description Saccharomyces cerevisiae chromosome V cosmids 9871, 8199, !19867, 9495 and lambda clones 6693 and 5898. !$#accession S50450 !'##molecule_type DNA !'##residues 1-281 ##label DIE !'##cross-references EMBL:U18530; NID:g602367; PIDN:AAB64486.1; !1PID:g602376; GSPDB:GN00005; MIPS:YEL009c REFERENCE A03604 !$#authors Thireos, G.; Penn, M.D.; Greer, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:5096-5100 !$#title 5' untranslated sequences are required for the translational !1control of a yeast regulatory gene. !$#cross-references MUID:84298088; PMID:6433345 !$#accession A03604 !'##molecule_type DNA !'##residues 1-238,'PGVLVRESCKE' ##label THI !'##cross-references EMBL:K02649; NID:g171585; PIDN:AAA65521.1; !1PID:g171586 GENETICS !$#gene SGD:GCN4; MIPS:YEL009c !'##cross-references SGD:S0000735; MIPS:YEL009c !$#map_position 5L FUNCTION !$#description transcription regulation !$#note required under amino acid starvation conditions for !1increasing the transcription of many genes that are subject !1to a common regulatory system CLASSIFICATION #superfamily amino-acid biosynthesis regulatory protein; !1fos/jun DNA-binding domain homology KEYWORDS DNA binding; leucine zipper; transcription regulation FEATURE !$220-260 #domain fos/jun DNA-binding domain homology #label !8FJD\ !$253-281 #region leucine zipper motif SUMMARY #length 281 #molecular-weight 31310 #checksum 5404 SEQUENCE /// ENTRY A30208 #type complete TITLE cross-pathway control protein 1 - Neurospora crassa ALTERNATE_NAMES cpc-1 protein ORGANISM #formal_name Neurospora crassa DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A30208 REFERENCE A30208 !$#authors Paluh, J.L.; Orbach, M.J.; Legerton, T.L.; Yanofsky, C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:3728-3732 !$#title The cross-pathway control gene of Neurospora crassa, cpc-1, !1encodes a protein similar to GCN4 of yeast and the !1DNA-binding domain of the oncogene v-jun-encoded protein. !$#cross-references MUID:88234499; PMID:2967496 !$#accession A30208 !'##molecule_type DNA !'##residues 1-269 ##label PAL !'##cross-references GB:J03262 GENETICS !$#introns 4/1 CLASSIFICATION #superfamily cross-pathway control protein 1; fos/jun !1DNA-binding domain homology KEYWORDS DNA binding; nucleus; transcription regulation FEATURE !$210-250 #domain fos/jun DNA-binding domain homology #label !8FJD SUMMARY #length 269 #molecular-weight 29269 #checksum 5399 SEQUENCE /// ENTRY A30225 #type complete TITLE regulatory protein cys-3 - Neurospora crassa ORGANISM #formal_name Neurospora crassa DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A30225; A37066 REFERENCE A30225 !$#authors Fu, Y.H.; Paietta, J.V.; Mannix, D.G.; Marzluf, G.A. !$#journal Mol. Cell. Biol. (1989) 9:1120-1127 !$#title cys-3, the positive-acting sulfur regulatory gene of !1Neurospora crassa, encodes a protein with a putative leucine !1zipper DNA-binding element. !$#cross-references MUID:89261715; PMID:2524646 !$#accession A30225 !'##molecule_type DNA !'##residues 1-236 ##label FUX !'##cross-references GB:M26008; NID:g168807; PIDN:AAA33585.1; !1PID:g168808 REFERENCE A37066 !$#authors Fu, Y.H.; Marzluf, G.A. !$#journal J. Biol. Chem. (1990) 265:11942-11947 !$#title cys-3, the positive-acting sulfur regulatory gene of !1Neurospora crassa, encodes a sequence-specific DNA-binding !1protein. !$#cross-references MUID:90307725; PMID:2142156 !$#accession A37066 !'##status preliminary !'##molecule_type DNA !'##residues 98-155 ##label FUA !'##cross-references GB:M26008 CLASSIFICATION #superfamily regulatory protein cys-3; fos/jun DNA-binding !1domain homology KEYWORDS DNA binding; nucleus; transcription regulation FEATURE !$93-134 #domain fos/jun DNA-binding domain homology #label !8FJD SUMMARY #length 236 #molecular-weight 25895 #checksum 2577 SEQUENCE /// ENTRY A36749 #type complete TITLE transcription factor HNF-1A - human ALTERNATE_NAMES hepatic nuclear factor 1-alpha; transcription factor 1, hepatic; transcription factor LF-B1 ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A36749 REFERENCE A36749 !$#authors Bach, I.; Galcheva-Gargova, Z.; Mattei, M.G.; !1Simon-Chazottes, D.; Guenet, J.L.; Cereghini, S.; Yaniv, M. !$#journal Genomics (1990) 8:155-164 !$#title Cloning of human hepatic nuclear factor 1 (HNF1) and !1chromosomal localization of its gene in man and mouse. !$#cross-references MUID:91184801; PMID:1707031 !$#accession A36749 !'##molecule_type mRNA !'##residues 1-631 ##label BAC !'##cross-references GB:M57732; NID:g184264; PIDN:AAA88077.1; !1PID:g184265 GENETICS !$#gene GDB:TCF1; HNF1; LFB1 !'##cross-references GDB:125297; OMIM:142410; OMIM:600496 !$#map_position 12q24.3-12q24.3 COMPLEX homodimer; can also form heterodimers with, for example, !1HNF-1B FUNCTION !$#description transcription activator required for the expression of a !1number of liver-specific genes !$#note also expressed in some other tissues, where it may play !1other roles CLASSIFICATION #superfamily transcription factor HNF-1; homeobox homology KEYWORDS DNA binding; heterodimer; homeobox; homodimer; liver; !1nucleus; transcription regulation FEATURE !$1-33 #region dimerization\ !$222-277 #domain homeobox homology #label HOX SUMMARY #length 631 #molecular-weight 67356 #checksum 2931 SEQUENCE /// ENTRY A39262 #type complete TITLE transcription factor HNF-1A - mouse ALTERNATE_NAMES hepatic nuclear factor 1-alpha; transcription factor APF; transcription factor HP-1; transcription factor LF-B1 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A39262; S70436 REFERENCE A39262 !$#authors Kuo, C.J.; Conley, P.B.; Hsieh, C.L.; Francke, U.; Crabtree, !1G.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:9838-9842 !$#title Molecular cloning, functional expression, and chromosomal !1localization of mouse hepatocyte nuclear factor 1. !$#cross-references MUID:91088607; PMID:2263635 !$#accession A39262 !'##status preliminary !'##molecule_type mRNA !'##residues 1-628 ##label KUO !'##cross-references GB:M57966; NID:g193885; PIDN:AAA37821.1; !1PID:g193886 REFERENCE S70435 !$#authors Bach, I.; Pontoglio, M.; Yaniv, M. !$#journal Nucleic Acids Res. (1992) 20:4199-4204 !$#title Structure of the gene encoding hepatocyte nuclear factor 1 !1(HNF1). !$#cross-references MUID:92375726; PMID:1354855 !$#accession S70436 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 199-279 ##label BAC !'##note only a part of the nucleic acid sequence is shown GENETICS !$#gene Hnf-1 !$#introns 238/2 !$#note the list of introns is incomplete COMPLEX homodimer; can also form heterodimers with, for example, !1HNF-1B FUNCTION !$#description transcription activator required for the expression of a !1number of liver-specific genes, for example albumin !$#note also expressed in other tissues (kidney, stomach, !1intestine), where it may play other roles CLASSIFICATION #superfamily transcription factor HNF-1; homeobox homology KEYWORDS DNA binding; heterodimer; homeobox; homodimer; liver; !1nucleus; transcription regulation FEATURE !$1-33 #region dimerization\ !$222-277 #domain homeobox homology #label HOX SUMMARY #length 628 #molecular-weight 67237 #checksum 2887 SEQUENCE /// ENTRY A33333 #type complete TITLE transcription factor HNF-1A - rat ALTERNATE_NAMES hepatic nuclear factor 1-alpha; transcription factor APF; transcription factor HP-1; transcription factor LF-B1 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A33333; A34590; S11568; S70435 REFERENCE A33333 !$#authors Frain, M.; Swart, G.; Monaci, P.; Nicosia, A.; Staempfli, !1S.; Frank, R.; Cortese, R. !$#journal Cell (1989) 59:145-157 !$#title The liver-specific transcription factor LF-B1 contains a !1highly diverged homeobox DNA binding domain. !$#cross-references MUID:90003224; PMID:2571419 !$#accession A33333 !'##status preliminary !'##molecule_type mRNA !'##residues 1-628 ##label FRA !'##cross-references GB:J03170; NID:g205164; PIDN:AAA41524.1; !1PID:g205165 REFERENCE A34590 !$#authors Baumhueter, S.; Mendel, D.B.; Conley, P.B.; Kuo, C.J.; Turk, !1C.; Graves, M.K.; Edwards, C.A.; Courtois, G.; Crabtree, !1G.R. !$#journal Genes Dev. (1990) 4:372-379 !$#title HNF-1 shares three sequence motifs with the POU domain !1proteins and is identical to LF-B1 and APF. !$#cross-references MUID:90249741; PMID:1970973 !$#accession A34590 !'##status preliminary !'##molecule_type mRNA !'##residues 'R',166-628 ##label BAU !'##cross-references GB:X53297; NID:g57867; PIDN:CAA37387.1; PID:g57868 !'##note the authors translated the codon GAG for residue 616 as Asp REFERENCE S11568 !$#authors Chouard, T.; Blumenfeld, M.; Bach, I.; Vandekerckhove, J.; !1Cereghini, S.; Yaniv, M. !$#journal Nucleic Acids Res. (1990) 18:5853-5863 !$#title A distal dimerization domain is essential for DNA-binding by !1the atypical HNF1 homeodomain. !$#cross-references MUID:91016926; PMID:2216777 !$#accession S11568 !'##molecule_type mRNA !'##residues 1-628 ##label CHO !'##cross-references EMBL:X54423; NID:g56367; PIDN:CAA38295.1; !1PID:g56368 REFERENCE S70435 !$#authors Bach, I.; Pontoglio, M.; Yaniv, M. !$#journal Nucleic Acids Res. (1992) 20:4199-4204 !$#title Structure of the gene encoding hepatocyte nuclear factor 1 !1(HNF1). !$#cross-references MUID:92375726; PMID:1354855 !$#accession S70435 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 199-279 ##label BAC !'##note only a part of the nucleic acid sequence is shown GENETICS !$#gene Hnf-1 !$#introns 238/2 !$#note the list of introns is incomplete COMPLEX homodimer; can also form heterodimers with, for example, !1HNF-1B FUNCTION !$#description transcription activator required for the expression of a !1number of liver-specific genes, for example albumin !$#note also expressed in other tissues (kidney, stomach, !1intestine), where it may play other roles CLASSIFICATION #superfamily transcription factor HNF-1; homeobox homology KEYWORDS DNA binding; heterodimer; homeobox; homodimer; liver; !1nucleus; transcription regulation FEATURE !$1-33 #region dimerization\ !$222-277 #domain homeobox homology #label HOX SUMMARY #length 628 #molecular-weight 67213 #checksum 2387 SEQUENCE /// ENTRY A46149 #type complete TITLE transcription factor HNF-1A - hamster ALTERNATE_NAMES hepatic nuclear factor 1-alpha; transcription factor LF-B1 ORGANISM #formal_name Cricetinae gen. sp. #common_name hamster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A46149 REFERENCE A46149 !$#authors Emens, L.A.; Landers, D.W.; Moss, L.G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:7300-7304 !$#title Hepatocyte nuclear factor 1 alpha is expressed in a hamster !1insulinoma line and transactivates the rat insulin I gene. !$#cross-references MUID:92366449; PMID:1380153 !$#accession A46149 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-630 ##label EME !'##experimental_source HIT-T15 M.2.2.2 insulinoma cell line !'##note sequence extracted from NCBI backbone (NCBIP:110643) COMPLEX homodimer; can also form heterodimers with, for example, !1HNF-1B FUNCTION !$#description transcription activator required for the expression of a !1number of liver-specific genes !$#note also expressed in some other tissues, where it may play !1other roles CLASSIFICATION #superfamily transcription factor HNF-1; homeobox homology KEYWORDS DNA binding; homeobox; liver; nucleus; transcription !1regulation FEATURE !$1-33 #region dimerization\ !$222-277 #domain homeobox homology #label HOX SUMMARY #length 630 #molecular-weight 67468 #checksum 1732 SEQUENCE /// ENTRY S35574 #type complete TITLE transcription factor HNF-1A - chicken ALTERNATE_NAMES hepatic nuclear factor 1-alpha; transcription factor LF-B1 ORGANISM #formal_name Gallus gallus #common_name chicken DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S35574; S33229 REFERENCE S35574 !$#authors Hoerlein, A.; Grajer, K.H.; Igo-Kemenes, T. !$#journal Biol. Chem. Hoppe-Seyler (1993) 374:419-425 !$#title Genomic structure of the POU-related hepatic transcription !1factor HNF-1-alpha. !$#cross-references MUID:94030658; PMID:8105803 !$#accession S35574 !'##status preliminary !'##molecule_type DNA !'##residues 1-634 ##label HOE !'##cross-references EMBL:X67690 REFERENCE S33229 !$#authors Grajer, K.H.; Hoerlein, A.; Igo-Kemenes, T. !$#journal Biol. Chem. Hoppe-Seyler (1993) 374:319-326 !$#title Hepatic nuclear factor 1alpha (HNF-1alpha) is expressed in !1the oviduct of hens and interacts with regulatory elements !1of the lysozyme gene. !$#cross-references MUID:93332647; PMID:7687846 !$#accession S33229 !'##status preliminary !'##molecule_type mRNA !'##residues 375-411 ##label GRA GENETICS !$#introns 179/1; 241/2; 321/1; 373/3; 441/1; 505/1; 545/3; 593/1 COMPLEX homodimer; can also form heterodimers with, for example, !1HNF-1B FUNCTION !$#description transcription activator required for the expression of a !1number of liver-specific genes !$#note also expressed in some other tissues, where it may play !1other roles CLASSIFICATION #superfamily transcription factor HNF-1; homeobox homology KEYWORDS DNA binding; homeobox; liver; nucleus; transcription !1regulation FEATURE !$1-33 #region dimerization\ !$225-280 #domain homeobox homology #label HOX SUMMARY #length 634 #molecular-weight 69189 #checksum 5384 SEQUENCE /// ENTRY S34412 #type complete TITLE transcription factor HNF-1B - human ALTERNATE_NAMES hepatic nuclear factor 1-beta; transcription factor 2, hepatic; transcription factor LF-B3; variant hepatic nuclear factor 1; vHNF-1 ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S34412 REFERENCE S34412 !$#authors Bach, I.; Mattei, M.G.; Cereghini, S.; Yaniv, M. !$#journal Nucleic Acids Res. (1991) 19:3553-3559 !$#title Two members of an HNF1 homeoprotein family are expressed in !1human liver. !$#cross-references MUID:91305097; PMID:1677179 !$#accession S34412 !'##status preliminary !'##molecule_type mRNA !'##residues 1-557 ##label BAC !'##cross-references GB:X58840; NID:g414047; PIDN:CAA41652.1; !1PID:g414048 GENETICS !$#gene GDB:TCF2; LFB3; VHNF1 !'##cross-references GDB:125298; OMIM:189907 !$#map_position 17q11.2-17q12 CLASSIFICATION #superfamily transcription factor HNF-1; homeobox homology KEYWORDS DNA binding; homeobox; liver; nucleus; transcription !1regulation FEATURE !$1-33 #region dimerization\ !$254-309 #domain homeobox homology #label HOX SUMMARY #length 557 #molecular-weight 61323 #checksum 2250 SEQUENCE /// ENTRY S15342 #type complete TITLE transcription factor HNF-1B - rat ALTERNATE_NAMES hepatic nuclear factor 1-beta; transcription factor LF-B3; variant hepatic nuclear factor 1; vHNF-1 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S15342 REFERENCE S15342 !$#authors Rey-Campos, J.; Chouard, T.; Yaniv, M.; Cereghini, S. !$#journal EMBO J. (1991) 10:1445-1457 !$#title vHNF1 is a homeoprotein that activates transcription and !1forms heterodimers with HNF1. !$#cross-references MUID:91224096; PMID:1673926 !$#accession S15342 !'##status preliminary !'##molecule_type mRNA !'##residues 1-557 ##label EMB !'##cross-references GB:X56546; NID:g57477; PIDN:CAA39886.1; PID:g57478 CLASSIFICATION #superfamily transcription factor HNF-1; homeobox homology KEYWORDS DNA binding; homeobox; liver; nucleus; transcription !1regulation FEATURE !$1-33 #region dimerization\ !$254-309 #domain homeobox homology #label HOX SUMMARY #length 557 #molecular-weight 61370 #checksum 1629 SEQUENCE /// ENTRY A39633 #type complete TITLE transcription factor HNF-1B - mouse ALTERNATE_NAMES hepatic nuclear factor 1-beta; transcription factor LF-B3; variant hepatic nuclear factor 1; vHNF-1 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A39633; S15341 REFERENCE A39633 !$#authors Mendel, D.B.; Hansen, L.P.; Graves, M.K.; Conley, P.B.; !1Crabtree, G.R. !$#journal Genes Dev. (1991) 5:1042-1056 !$#title HNF-1alpha and HNF-1beta (vHNF-1) share dimerization and !1homeo domains, but not activation domains, and form !1heterodimers in vitro. !$#cross-references MUID:91257571; PMID:2044952 !$#accession A39633 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-183,210-558 ##label MEN REFERENCE S15341 !$#authors de Simone, V.; de Magistris, L.; Lazzaro, D.; Gerstner, J.; !1Monaci, P.; Nicosia, A.; Cortese, R. !$#journal EMBO J. (1991) 10:1435-1443 !$#title LFB3, a heterodimer-forming homeoprotein of the LFB1 family, !1is expressed in specialized epithelia. !$#cross-references MUID:91224095; PMID:1673925 !$#accession S15341 !'##status preliminary !'##molecule_type mRNA !'##residues 1-422,'TH',424,'PPQSP',430-519,'HT',522-558 ##label PNI !'##cross-references GB:X55842; NID:g52896; PIDN:CAA39358.1; PID:g52897 CLASSIFICATION #superfamily transcription factor HNF-1; homeobox homology KEYWORDS DNA binding; homeobox; liver; nucleus; transcription !1regulation FEATURE !$1-33 #region dimerization\ !$254-309 #domain homeobox homology #label HOX SUMMARY #length 558 #molecular-weight 61588 #checksum 5016 SEQUENCE /// ENTRY I51704 #type complete TITLE transcription factor HNF-1B - African clawed frog ALTERNATE_NAMES hepatic nuclear factor 1-beta; transcription factor LF-B3; variant hepatic nuclear factor 1; vHNF-1 ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS I51704 REFERENCE I51704 !$#authors Demartis, A.; Maffei, M.; Vignali, R.; Barsacchi, G.; De !1Simone, V. !$#journal Mech. Dev. (1994) 47:19-28 !$#title Cloning and developmental expression of LFB3/HNF1 beta !1transcription factor in Xenopus laevis. !$#cross-references MUID:95034304; PMID:7524626 !$#accession I51704 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-561 ##label DEM !'##cross-references EMBL:X76052; NID:g515328; PIDN:CAA53637.1; !1PID:g515329 GENETICS !$#gene LFB3 CLASSIFICATION #superfamily transcription factor HNF-1; homeobox homology KEYWORDS DNA binding; homeobox; liver; nucleus; transcription !1regulation FEATURE !$1-33 #region dimerization\ !$253-308 #domain homeobox homology #label HOX SUMMARY #length 561 #molecular-weight 62343 #checksum 5969 SEQUENCE /// ENTRY S15031 #type complete TITLE paired box transcription factor Pax-3 - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 21-Nov-1993 #sequence_revision 21-Jul-1995 #text_change 18-Jun-1999 ACCESSIONS S15031; I52812; I65737 REFERENCE S15031 !$#authors Goulding, M.D.; Chalepakis, G.; Deutsch, U.; Erselius, J.R.; !1Gruss, P. !$#journal EMBO J. (1991) 10:1135-1147 !$#title Pax-3, a novel murine DNA binding protein expressed during !1early neurogenesis. !$#cross-references MUID:91216108; PMID:2022185 !$#accession S15031 !'##molecule_type mRNA !'##residues 1-479 ##label GOU !'##cross-references GB:X59358; NID:g53591; PIDN:CAA42008.1; PID:g53592 REFERENCE I52812 !$#authors Epstein, D.J.; Vekemans, M.; Gros, P. !$#journal Cell (1991) 67:767-774 !$#title Splotch (Sp2H), a mutation affecting development of the !1mouse neural tube, shows a deletion within the paired !1homeodomain of Pax-3. !$#cross-references MUID:92034997; PMID:1682057 !$#accession I52812 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 219-260 ##label RES !'##cross-references GB:S66429; NID:g239200; PIDN:AAB20359.1; !1PID:g239201 !$#accession I65737 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 219-237 ##label RE2 !'##cross-references GB:S66433; NID:g239202; PIDN:AAB20360.1; !1PID:g239203 GENETICS !$#gene Pax-3 CLASSIFICATION #superfamily paired box transcription factor Pax-3; homeobox !1homology; paired box homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$34-159 #domain paired box homology #label PBH\ !$220-276 #domain homeobox homology #label HOX SUMMARY #length 479 #molecular-weight 52984 #checksum 6402 SEQUENCE /// ENTRY B43698 #type complete TITLE paired box transcription factor BSH4 - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 03-Mar-1993 #sequence_revision 03-Mar-1993 #text_change 07-May-1999 ACCESSIONS B43698 REFERENCE A43698 !$#authors Baumgartner, S.; Bopp, D.; Burri, M.; Noll, M. !$#journal Genes Dev. (1987) 1:1247-1267 !$#title Structure of two genes at the gooseberry locus related to !1the paired gene and their spatial expression during !1Drosophila embryogenesis. !$#cross-references MUID:88112802; PMID:3123319 !$#accession B43698 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-449 ##label BAU GENETICS !$#gene FlyBase:gsb-p !'##cross-references FlyBase:FBgn0001147 CLASSIFICATION #superfamily paired box transcription factor BSH4; homeobox !1homology; paired box homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$20-141 #domain paired box homology #label PBH\ !$183-239 #domain homeobox homology #label HOX SUMMARY #length 449 #molecular-weight 48272 #checksum 1890 SEQUENCE /// ENTRY A43698 #type complete TITLE paired box transcription factor BSH9 - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 03-Mar-1993 #sequence_revision 03-Mar-1993 #text_change 18-Jun-1999 ACCESSIONS A43698; B26332 REFERENCE A43698 !$#authors Baumgartner, S.; Bopp, D.; Burri, M.; Noll, M. !$#journal Genes Dev. (1987) 1:1247-1267 !$#title Structure of two genes at the gooseberry locus related to !1the paired gene and their spatial expression during !1Drosophila embryogenesis. !$#cross-references MUID:88112802; PMID:3123319 !$#accession A43698 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-427 ##label BAU REFERENCE A90884 !$#authors Bopp, D.; Burri, M.; Baumgartner, S.; Frigerio, G.; Noll, M. !$#journal Cell (1986) 47:1033-1040 !$#title Conservation of a large protein domain in the segmentation !1gene paired and in functionally related genes of Drosophila. !$#cross-references MUID:87051758; PMID:2877747 !$#accession B26332 !'##molecule_type DNA !'##residues 165-244 ##label BOP !'##cross-references GB:M14942; NID:g158167; PIDN:AAA28837.1; !1PID:g158170 GENETICS !$#gene FlyBase:gsb-d !'##cross-references FlyBase:FBgn0001148 CLASSIFICATION #superfamily paired box transcription factor BSH9; homeobox !1homology; paired box homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$19-143 #domain paired box homology #label PBH\ !$186-242 #domain homeobox homology #label HOX SUMMARY #length 427 #molecular-weight 45515 #checksum 1165 SEQUENCE /// ENTRY A56674 #type complete TITLE paired box transcription factor Pax-6 - human ALTERNATE_NAMES homeotic protein aniridia ORGANISM #formal_name Homo sapiens #common_name man DATE 08-Jul-1995 #sequence_revision 03-Aug-1995 #text_change 18-Jun-1999 ACCESSIONS A56674; A41644 REFERENCE A56674 !$#authors Glaser, T.; Walton, D.S.; Maas, R.L. !$#journal Nature Genet. (1992) 2:232-239 !$#title Genomic structure, evolutionary conservation and aniridia !1mutations in the human PAX6 gene. !$#cross-references MUID:94258210; PMID:1345175 !$#accession A56674 !'##status preliminary !'##molecule_type mRNA !'##residues 1-422 ##label GLA !'##cross-references GB:M93650; NID:g189632; PIDN:AAA36416.1; !1PID:g189633 REFERENCE A41644 !$#authors Ton, C.C.T.; Hirvonen, H.; Miwa, H.; Weil, M.M.; Monaghan, !1P.; Jordan, T.; van Heyningen, V.; Hastie, N.D.; !1Meijers-Heijboer, H.; Drechsler, M.; Royer-Pokora, B.; !1Collins, F.; Swaroop, A.; Strong, L.C.; Saunders, G.F. !$#journal Cell (1991) 67:1059-1074 !$#title Positional cloning and characterization of a paired box- and !1homeobox-containing gene from the aniridia region. !$#cross-references MUID:92103673; PMID:1684738 !$#accession A41644 !'##molecule_type mRNA !'##residues 'MDRHPRFQSPIFEPRGIPRPPARAS',1-316,'L',318-422 ##label TON !'##cross-references GB:M77844 !'##note authors were uncertain whether Met-1 was the initiator or !1whether an upstream GTG codon was used as initiator COMMENT Deletion of the gene for this protein leads to aniridia, a !1congenital absence of the iris. GENETICS !$#gene GDB:PAX6; AN; AN2; D11S812E; WAGR !'##cross-references GDB:118997; OMIM:106210 !$#map_position 11p13-11p13 CLASSIFICATION #superfamily paired box transcription factor Pax-6; homeobox !1homology; paired box homology KEYWORDS alternative splicing; DNA binding; homeobox; nucleus; !1transcription regulation FEATURE !$4-128 #domain paired box homology #label PBH\ !$211-267 #domain homeobox homology #label HOX SUMMARY #length 422 #molecular-weight 46683 #checksum 9466 SEQUENCE /// ENTRY S42234 #type complete TITLE paired box transcription factor Pax-6 - mouse ALTERNATE_NAMES aniridia homolog; homeotic protein small eye (sey); oculorhombin ORGANISM #formal_name Mus musculus #common_name house mouse DATE 13-Jan-1995 #sequence_revision 13-Jan-1995 #text_change 16-Jun-2000 ACCESSIONS S42234; A42001; S19602; C41061 REFERENCE S42234 !$#authors Walther, C.; Gruss, P. !$#journal Development (1991) 113:1435-1449 !$#title Pax-6, a murine paired box gene, is expressed in the !1developing CNS. !$#cross-references MUID:92249187; PMID:1687460 !$#accession S42234 !'##status preliminary !'##molecule_type mRNA !'##residues 1-436 ##label WAL1 !'##cross-references EMBL:X63963; NID:g460050; PIDN:CAA45379.1; !1PID:g1405744 REFERENCE A42001 !$#authors Ton, C.C.T.; Miwa, H.; Saunders, G.F. !$#journal Genomics (1992) 13:251-256 !$#title Small eye (Sey): cloning and characterization of the murine !1homolog of the human aniridia gene. !$#cross-references MUID:92307655; PMID:1612585 !$#accession A42001 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 45-47,62-300,'T',302-434 ##label TON !'##cross-references GB:M77842; NID:g498021; PIDN:AAA40109.1; !1PID:g498022 !'##note the translated sequence in GenBank entry MUSSEYA, release !1111.0, differs from the published sequence in beginning !1incorrectly at the internal 151-Met AUG codon REFERENCE S19602 !$#authors Hill, R.E.; Favor, J.; Hogan, B.L.M.; Ton, C.C.T.; Saunders, !1G.F.; Hanson, I.M.; Prosser, J.; Jordan, T.; Hastie, N.D.; !1van Heyningen, V. !$#journal Nature (1991) 354:522-525 !$#title Mouse small eye results from mutations in a paired-like !1homeobox-containing gene. !$#cross-references MUID:92100191; PMID:1684639 !$#accession S19602 !'##status preliminary !'##molecule_type DNA !'##residues 310-327 ##label HIL REFERENCE A41061 !$#authors Walther, C.; Guenet, J.L.; Simon, D.; Deutsch, U.; Jostes, !1B.; Goulding, M.D.; Plachov, D.; Balling, R.; Gruss, P. !$#journal Genomics (1991) 11:424-434 !$#title Pax: a murine multigene family of paired box-containing !1genes. !$#cross-references MUID:92120664; PMID:1685142 !$#accession C41061 !'##molecule_type DNA !'##residues 4-47,62-145 ##label WAL2 !'##cross-references GB:X63963; NID:g460050 !'##note the complete translation is not shown CLASSIFICATION #superfamily paired box transcription factor Pax-6; homeobox !1homology; paired box homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$4-142 #domain paired box homology #label PBH\ !$225-281 #domain homeobox homology #label HOX SUMMARY #length 436 #molecular-weight 48219 #checksum 2666 SEQUENCE /// ENTRY I50108 #type complete TITLE paired box transcription factor Pax-6 - zebra fish ALTERNATE_NAMES small eye (sey) / aniridia homolog Pax-6 ORGANISM #formal_name Brachydanio rerio #common_name zebra fish DATE 13-Mar-1997 #sequence_revision 13-Mar-1997 #text_change 18-Jun-1999 ACCESSIONS I50108; S18558; S17876 REFERENCE I50108 !$#authors Pueschel, A.W.; Gruss, P.; Westerfield, M. !$#journal Development (1992) 114:643-651 !$#title Sequence and expression pattern of pax-6 are highly !1conserved between zebrafish and mice. !$#cross-references MUID:92315909; PMID:1352238 !$#accession I50108 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-451 ##label PUS !'##cross-references EMBL:X63183; NID:g62546; PIDN:CAA44867.1; !1PID:g62547 REFERENCE S18558 !$#authors Krauss, S.; Johansen, T.; Korzh, V.; Moens, U.; Ericson, !1J.U.; Fjose, A. !$#journal EMBO J. (1991) 10:3609-3619 !$#title Zebrafish pax[zf-a]: a paired box-containing gene expressed !1in the neural tube. !$#cross-references MUID:92037521; PMID:1718739 !$#accession S18558 !'##molecule_type mRNA !'##residues 1-66,81-451 ##label KRA !'##cross-references EMBL:X61389; NID:g62548; PIDN:CAA43661.1; !1PID:g62549 REFERENCE S17876 !$#authors Krauss, S.; Johansen, T.; Korzh, V.; Fjose, A. !$#journal Nature (1991) 353:267-270 !$#title Expression pattern of zebrafish pax genes suggests a role in !1early brain regionalization. !$#cross-references MUID:91375540; PMID:1680220 !$#accession S17876 !'##molecule_type mRNA !'##residues 'ILQ',81-451 ##label KR2 !'##cross-references GB:X61389; NID:g62548; PIDN:CAA43661.1; PID:g62549 GENETICS !$#gene pax-6 CLASSIFICATION #superfamily paired box transcription factor Pax-6; homeobox !1homology; paired box homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$23-161 #domain paired box homology #label PBH\ !$244-300 #domain homeobox homology #label HOX SUMMARY #length 451 #molecular-weight 49961 #checksum 6422 SEQUENCE /// ENTRY S60252 #type complete TITLE paired box transcription factor vab-3 - Caenorhabditis elegans ALTERNATE_NAMES small eye (sey) / aniridia / Pax-6 homolog vab-3 ORGANISM #formal_name Caenorhabditis elegans DATE 10-Apr-1996 #sequence_revision 01-Dec-2000 #text_change 01-Dec-2000 ACCESSIONS T20900; S60252 REFERENCE Z19343 !$#authors Kershaw, J. !$#submission submitted to the EMBL Data Library, June 1995 !$#accession T20900 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-491 ##label WIL !'##cross-references EMBL:Z49937; PIDN:CAA90186.1; GSPDB:GN00028; !1CESP:F14F3.1 !'##experimental_source clone F14F3 REFERENCE S60252 !$#authors Chisholm, A.D.; Horvitz, H.R. !$#journal Nature (1995) 377:52-55 !$#title Patterning of the Caenorhabditis elegans head region by the !1Pax-6 family member vab-3. !$#cross-references MUID:95388138; PMID:7659159 !$#accession S60252 !'##status preliminary !'##molecule_type mRNA !'##residues 'MSD',40-491 ##label CHI !'##cross-references EMBL:U31537; NID:g965065; PIDN:AAA82991.1; !1PID:g965066 GENETICS !$#gene CESP:F14F3.1 !$#map_position X !$#introns 39/1; 88/2; 114/2; 156/3; 191/2; 230/1; 271/1; 298/3; 391/2; !1448/1 CLASSIFICATION #superfamily paired box transcription factor Pax-6; homeobox !1homology; paired box homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$41-165 #domain paired box homology #label PBH\ !$254-310 #domain homeobox homology #label HOX SUMMARY #length 491 #molecular-weight 55314 #checksum 7689 SEQUENCE /// ENTRY A26062 #type complete TITLE paired box segmentation protein prd - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 25-Oct-1987 #sequence_revision 25-Oct-1987 #text_change 18-Jun-1999 ACCESSIONS A26062 REFERENCE A26062 !$#authors Frigerio, G.; Burri, M.; Bopp, D.; Baumgartner, S.; Noll, M. !$#journal Cell (1986) 47:735-746 !$#title Structure of the segmentation gene paired and the Drosophila !1PRD gene set as part of a gene network. !$#cross-references MUID:87051745; PMID:2877746 !$#accession A26062 !'##molecule_type DNA; mRNA !'##residues 1-613 ##label FRI !'##cross-references GB:M14548; NID:g158159; PIDN:AAB59221.1; !1PID:g158160 !'##note 164-Thr and 220-Ile were also found GENETICS !$#gene prd (paired) !'##cross-references FlyBase:FBgn0003145 !$#introns 23/1 CLASSIFICATION #superfamily paired box segmentation protein prd; homeobox !1homology; paired box homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$27-151 #domain paired box homology #label PBH\ !$214-270 #domain homeobox homology #label HOX\ !$545-576 #region histidine/proline-rich SUMMARY #length 613 #molecular-weight 65497 #checksum 9800 SEQUENCE /// ENTRY A54258 #type complete TITLE transcription factor HNF-3 alpha - mouse ALTERNATE_NAMES hepatocyte nuclear factor 3 alpha ORGANISM #formal_name Mus musculus #common_name house mouse DATE 18-Aug-1995 #sequence_revision 19-Oct-1995 #text_change 18-Jun-1999 ACCESSIONS A54258; I49675; S37187 REFERENCE A54258 !$#authors Kaestner, K.H.; Hiemisch, H.; Luckow, B.; Schutz, G. !$#journal Genomics (1994) 20:377-385 !$#title The HNF-3 gene family of transcription factors in mice: gene !1structure, cDNA sequence, and mRNA distribution. !$#cross-references MUID:94307723; PMID:8034310 !$#accession A54258 !'##molecule_type mRNA !'##residues 1-468 ##label KAE !'##cross-references EMBL:X74936; NID:g402194; PIDN:CAA52890.1; !1PID:g402195 REFERENCE I49674 !$#authors Sasaki, H.; Hogan, B.L. !$#journal Development (1993) 118:47-59 !$#title Differential expression of multiple fork head related genes !1during gastrulation and axial pattern formation in the mouse !1embryo. !$#cross-references MUID:93387221; PMID:8375339 !$#accession I49675 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 'XX',161-269 ##label RES !'##cross-references GB:L10408; NID:g404761; PIDN:AAA03160.1; !1PID:g404762 GENETICS !$#introns 24/3 FUNCTION !$#description regulation of gene expression, especially in liver and lung !$#note expressed in embryonic endoderm and endoderm-derived adult !1tissues, most strongly in large intestine and stomach, less !1in liver, lung, and small intestine CLASSIFICATION #superfamily transcription factor HNF-3; fork head !1DNA-binding domain homology KEYWORDS DNA binding; transcription factor FEATURE !$170-261 #domain fork head DNA-binding domain homology #label !8FHD SUMMARY #length 468 #molecular-weight 48911 #checksum 4707 SEQUENCE /// ENTRY B54258 #type complete TITLE transcription factor HNF-3 beta - mouse ALTERNATE_NAMES hepatocyte nuclear factor 3 beta ORGANISM #formal_name Mus musculus #common_name house mouse DATE 18-Aug-1995 #sequence_revision 19-Oct-1995 #text_change 18-Jun-1999 ACCESSIONS B54258; I49676; S37185 REFERENCE A54258 !$#authors Kaestner, K.H.; Hiemisch, H.; Luckow, B.; Schutz, G. !$#journal Genomics (1994) 20:377-385 !$#title The HNF-3 gene family of transcription factors in mice: gene !1structure, cDNA sequence, and mRNA distribution. !$#cross-references MUID:94307723; PMID:8034310 !$#accession B54258 !'##molecule_type mRNA !'##residues 1-459 ##label KAE !'##cross-references EMBL:X74937; NID:g402190; PIDN:CAA52891.1; !1PID:g402191 REFERENCE I49674 !$#authors Sasaki, H.; Hogan, B.L. !$#journal Development (1993) 118:47-59 !$#title Differential expression of multiple fork head related genes !1during gastrulation and axial pattern formation in the mouse !1embryo. !$#cross-references MUID:93387221; PMID:8375339 !$#accession I49676 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-9,'H',11-459 ##label RES !'##cross-references GB:L10409; NID:g404763; PIDN:AAA03161.1; !1PID:g404764 GENETICS !$#gene HNF-3beta !$#introns 23/3 FUNCTION !$#description regulation of gene expression, especially in liver and lung !$#note expressed in embryonic endoderm and endoderm-derived adult !1tissues, most strongly in large intestine and stomach, less !1in liver, lung, and small intestine CLASSIFICATION #superfamily transcription factor HNF-3; fork head !1DNA-binding domain homology KEYWORDS DNA binding; transcription factor FEATURE !$159-250 #domain fork head DNA-binding domain homology #label !8FHD SUMMARY #length 459 #molecular-weight 48474 #checksum 9278 SEQUENCE /// ENTRY A47527 #type complete TITLE transcription factor HNF-3 beta - zebra fish ALTERNATE_NAMES axial protein; hepatocyte nuclear factor 3 beta ORGANISM #formal_name Brachydanio rerio #common_name zebra fish DATE 11-Nov-1994 #sequence_revision 19-Oct-1995 #text_change 18-Jun-1999 ACCESSIONS A47527; S36040 REFERENCE A47527 !$#authors Straehle, U.; Blader, P.; Henrique, D.; Ingham, P.W. !$#journal Genes Dev. (1993) 7:1436-1446 !$#title Axial, a zebra fish gene expressed along the developing body !1axis, shows altered expression in cyclops mutant embryos. !$#cross-references MUID:93321871; PMID:7687227 !$#accession A47527 !'##molecule_type mRNA !'##residues 1-409 ##label STR !'##cross-references EMBL:Z22762; NID:g311267; PIDN:CAA80443.1; !1PID:g311268 FUNCTION !$#description required for induction of axial mesoendoderm and of ventral !1central nervous system; regulation of gene expression in !1adults, especially in liver !$#note expressed in all three layers of the developing embryonic !1axis and in adult liver and gut CLASSIFICATION #superfamily transcription factor HNF-3; fork head !1DNA-binding domain homology KEYWORDS DNA binding; transcription factor FEATURE !$151-242 #domain fork head DNA-binding domain homology #label !8FHD SUMMARY #length 409 #molecular-weight 45075 #checksum 8977 SEQUENCE /// ENTRY S35090 #type complete TITLE transcription factor HNF-3 gamma - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S35090; A39533 REFERENCE S35090 !$#authors Lai, E.; Prezioso, V.R.; Tao, W.; Chen, W.S.; Darnell, J.E. !$#submission submitted to the EMBL Data Library, January 1993 !$#description Hepatocyte nuclear factor 3a belongs to a gene family in !1mammals that is homologous to the Drosophila homeotic gene !1fork head (correction). !$#accession S35090 !'##status preliminary !'##molecule_type mRNA !'##residues 1-354 ##label LAI !'##cross-references EMBL:L09648; NID:g204624; PIDN:AAA41339.1; !1PID:g204625 REFERENCE A39533 !$#authors Lai, E.; Prezioso, V.R.; Tao, W.; Chen, W.S.; Darnell Jr., !1J.E. !$#journal Genes Dev. (1991) 5:416-427 !$#title Hepatocyte nuclear factor 3alpha belongs to a gene family in !1mammals that is homologous to the Drosophila homeotic gene !1fork head. !$#cross-references MUID:91160974; PMID:1672118 !$#accession A39533 !'##status preliminary !'##molecule_type mRNA !'##residues 'M',23,'GQEDRTT',31,'RQEDRAYAVLF',43-44,'T',57-115,'A', !1117-354 ##label LA2 !'##cross-references GB:L09647 CLASSIFICATION #superfamily transcription factor HNF-3; fork head !1DNA-binding domain homology KEYWORDS DNA binding; nucleus; transcription regulation FEATURE !$119-210 #domain fork head DNA-binding domain homology #label !8FHD SUMMARY #length 354 #molecular-weight 37652 #checksum 9015 SEQUENCE /// ENTRY C54258 #type complete TITLE transcription factor HNF-3 gamma - mouse ALTERNATE_NAMES hepatocyte nuclear factor 3 gamma ORGANISM #formal_name Mus musculus #common_name house mouse DATE 18-Aug-1995 #sequence_revision 19-Oct-1995 #text_change 18-Jun-1999 ACCESSIONS C54258; S37186 REFERENCE A54258 !$#authors Kaestner, K.H.; Hiemisch, H.; Luckow, B.; Schutz, G. !$#journal Genomics (1994) 20:377-385 !$#title The HNF-3 gene family of transcription factors in mice: gene !1structure, cDNA sequence, and mRNA distribution. !$#cross-references MUID:94307723; PMID:8034310 !$#accession C54258 !'##molecule_type mRNA !'##residues 1-353 ##label KAE !'##cross-references EMBL:X74938; NID:g402192; PIDN:CAA52892.1; !1PID:g402193 GENETICS !$#introns 23/3 FUNCTION !$#description regulation of gene expression !$#note embryonic expression is later that HNF-3 alpha and beta, and !1tissue distribution in adults is broader, though it is not !1found in lung CLASSIFICATION #superfamily transcription factor HNF-3; fork head !1DNA-binding domain homology KEYWORDS DNA binding; transcription factor FEATURE !$119-210 #domain fork head DNA-binding domain homology #label !8FHD SUMMARY #length 353 #molecular-weight 37601 #checksum 1137 SEQUENCE /// ENTRY S35719 #type complete TITLE transcription factor pintallavis - African clawed frog ALTERNATE_NAMES XFD-1 protein ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 09-Dec-1993 #sequence_revision 19-Oct-1995 #text_change 18-Jun-1999 ACCESSIONS S35719; A56556; S25490 REFERENCE S35719 !$#authors Ruiz i Altaba, A.; Jessell, T.M. !$#journal Development (1992) 116:81-93 !$#title Pintallavis, a gene expressed in the organizer and midline !1cells of frog embryos: involvement in the development of the !1neural axis. !$#cross-references MUID:93130781; PMID:1483397 !$#accession S35719 !'##molecule_type mRNA !'##residues 1-399 ##label RUI !'##cross-references EMBL:X65171; NID:g64983; PIDN:CAA46290.1; !1PID:g64984 REFERENCE A56556 !$#authors Knochel, S.; Lef, J.; Clement, J.; Klocke, B.; Hille, S.; !1Koster, M.; Knochel, W. !$#journal Mech. Dev. (1992) 38:157-165 !$#title Activin A induced expression of a fork head related gene in !1posterior chordamesoderm (notochord) of Xenopus laevis !1embryos. !$#cross-references MUID:93041288; PMID:1358174 !$#accession A56556 !'##status preliminary !'##molecule_type DNA; mRNA !'##residues 1-361,'N',363-399 ##label KNO !'##experimental_source gastrula !'##note sequence extracted from NCBI backbone (NCBIN:118172, !1NCBIN:118174, NCBIP:118176) FUNCTION !$#description may have a role in neural induction; binds to the HNF-3 !1alpha target sequence !$#note transiently expressed by midline cells of gastrula and !1neurula stage embryos CLASSIFICATION #superfamily transcription factor HNF-3; fork head !1DNA-binding domain homology KEYWORDS DNA binding; transcription factor FEATURE !$119-210 #domain fork head DNA-binding domain homology #label !8FHD SUMMARY #length 399 #molecular-weight 44511 #checksum 634 SEQUENCE /// ENTRY TVHURF #type complete TITLE ret finger protein - human ALTERNATE_NAMES transforming protein rfp ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 19-Jan-2001 ACCESSIONS A28101 REFERENCE A28101 !$#authors Takahashi, M.; Inaguma, Y.; Hiai, H.; Hirose, F. !$#journal Mol. Cell. Biol. (1988) 8:1853-1856 !$#title Developmentally regulated expression of a human !1"finger"-containing gene encoded by the 5' half of the ret !1transforming gene. !$#cross-references MUID:88246464; PMID:3380101 !$#accession A28101 !'##molecule_type mRNA !'##residues 1-513 ##label TAK !'##cross-references DDBJ:J03407; NID:g337371; PIDN:AAA36564.1; !1PID:g337372 GENETICS !$#gene GDB:RFP !'##cross-references GDB:511359; GDB:1391662 !$#map_position 6p22-6p21.3 CLASSIFICATION #superfamily rfp transforming protein; RING finger homology KEYWORDS DNA binding; transforming protein; zinc finger FEATURE !$1-315 #product transforming protein rfp (fragment) #status !8predicted #label RET\ !$12-62 #domain RING finger homology #label RNG\ !$16-127 #domain metal and nucleic acid binding #status !8predicted #label TMN\ !$16-56 #region zinc finger C3HC4 motif SUMMARY #length 513 #molecular-weight 58489 #checksum 1712 SEQUENCE /// ENTRY A37241 #type complete TITLE 52K autoantigen Ro/SS-A - human ALTERNATE_NAMES Sjogren syndrome antigen A ORGANISM #formal_name Homo sapiens #common_name man DATE 07-Feb-1992 #sequence_revision 26-May-1995 #text_change 17-Mar-2000 ACCESSIONS A55642; A37241; A37240 REFERENCE A55642 !$#authors Tsugu, H.; Horowitz, R.; Gibson, N.; Frank, M.B. !$#journal Genomics (1994) 24:541-548 !$#title The location of a disease-associated polymorphism and !1genomic structure of the human 52-kDa Ro/SSA locus (SSA1). !$#cross-references MUID:95229155; PMID:7713506 !$#accession A55642 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-475 ##label TSU !'##cross-references GB:U13657 REFERENCE A37241 !$#authors Itoh, K.; Itoh, Y.; Frank, M.B. !$#journal J. Clin. Invest. (1991) 87:177-186 !$#title Protein heterogeneity in the human Ro/SSA !1ribonucleoproteins. The 52- and 60-kD Ro/SSA autoantigens !1are encoded by separate genes. !$#cross-references MUID:91086445; PMID:1985094 !$#accession A37241 !'##molecule_type mRNA !'##residues 1-475 ##label ITO !'##cross-references GB:M34551; NID:g337484; PIDN:AAA36581.1; !1PID:g337485 REFERENCE A37240 !$#authors Chan, E.K.L.; Hamel, J.C.; Buyon, J.P.; Tan, E.M. !$#journal J. Clin. Invest. (1991) 87:68-76 !$#title Molecular definition and sequence motifs of the 52-kD !1component of human SS-A/Ro autoantigen. !$#cross-references MUID:91086480; PMID:1985112 !$#accession A37240 !'##molecule_type mRNA !'##residues 1-51,'A',53-475 ##label CHA !'##cross-references GB:M62800; NID:g338489; PIDN:AAA36651.1; !1PID:g338490; GB:M35041 GENETICS !$#gene GDB:SSA1 !'##cross-references GDB:133758; OMIM:109092 !$#map_position 11p15.5-11p15.5 !$#introns 136/3; 168/3; 245/3; 253/2; 287/1 CLASSIFICATION #superfamily rfp transforming protein; RING finger homology KEYWORDS DNA binding; nucleus; zinc finger FEATURE !$12-60 #domain RING finger homology #label RNG\ !$16-54 #region zinc finger C3HC4 motif SUMMARY #length 475 #molecular-weight 54169 #checksum 7482 SEQUENCE /// ENTRY A58881 #type complete TITLE breast/ovarian cancer susceptibility protein BRCA1 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 16-Oct-1998 #sequence_revision 16-Oct-1998 #text_change 18-Jun-1999 ACCESSIONS A58881; A54652; I58130 REFERENCE A58881 !$#authors Skolnick, M.H. !$#submission submitted to GenBank, September 1994 !$#description Human breast and ovarian cancer susceptibility (BRCA1) mRNA, !1complete cds. !$#accession A58881 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-1863 ##label SKO !'##cross-references GB:U14680; NID:g555931; PIDN:AAA73985.1; !1PID:g555932 REFERENCE A54652 !$#authors Miki, Y.; Swensen, J.; Shattuck-Eidens, D.; Futreal, P.A.; !1Harshman, K.; Tavtigian, S.; Liu, Q.; Cochran, C.; Bennett, !1L.M.; Ding, W.; Bell, R.; Rosenthal, J.; Hussey, C.; Tran, !1T.; McClure, M.; Frye, C.; Hattier, T.; Phelps, R.; !1Haugen-Strano, A.; Katcher, H.; Yakumo, K.; Gholami, Z.; !1Shaffer, D.; Stone, S.; Bayer, S.; Wray, C.; Bogden, R.; !1Dayananth, P.; Ward, J.; Tonin, P.; Narod, S.; Bristow, !1P.K.; Norris, F.H.; Helvering, L.; Morrison, P.; Rosteck, !1P.; Lai, M.; Barrett, J.C.; Lewis, C.; Neuhausen, S.; !1Cannon-Albright, L.; Goldgar, D.; Wiseman, R.; Kamb, A.; !1Skolnick, M.H. !$#journal Science (1994) 266:66-71 !$#title A strong candidate for the breast and ovarian cancer !1susceptibility gene BRCA1. !$#cross-references MUID:95025896; PMID:7545954 !$#accession A54652 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-444,'D',446-487,'S',489-593,595-600,'M',601-1452,'VLQ', !11456-1471,'X',1473-1523,'P',1525-1863 ##label MIK !'##cross-references GB:U14680 REFERENCE I58130 !$#authors Hosking, L.; Trowsdale, J.; Nicolai, H.; Solomon, E.; !1Foulkes, W.; Stamp, G.; Signer, E.; Jeffreys, A. !$#journal Nature Genet. (1995) 9:343-344 !$#title A somatic BRCA1 mutation in an ovarian tumour. !$#cross-references MUID:95315980; PMID:7795636 !$#accession I58130 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1812-1813,'PGQRTMASMQLGRCVRHLW' ##label HOS !'##cross-references GB:S78558; NID:g1000568; PIDN:AAB34725.1; !1PID:g1000569 !'##note frame shift mutation from an ovarian tumor GENETICS !$#gene GDB:BRCA1 !'##cross-references GDB:126611; OMIM:113705 !$#map_position 17q21-17q21 CLASSIFICATION #superfamily breast/ovarian cancer susceptibility protein !1BRCA1; RING finger homology KEYWORDS mammary gland; nucleus; ovary; tumor suppressor; zinc finger FEATURE !$20-70 #domain RING finger homology #label RNG\ !$24-64 #region zinc finger C3HC4 motif\ !$607-621 #region nuclear location signal\ !$651-664 #region nuclear location signal\ !$679-692 #region nuclear location signal\ !$24,27,44,47 #binding_site zinc (Cys) #status predicted\ !$39,41,61,64 #binding_site zinc (Cys, His, Cys, Cys) #status !8predicted SUMMARY #length 1863 #molecular-weight 207719 #checksum 851 SEQUENCE /// ENTRY A38637 #type complete TITLE Ras interactor RIN1 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 14-Feb-1992 #sequence_revision 17-Oct-1997 #text_change 20-Apr-2000 ACCESSIONS A58613; A38637 REFERENCE A58613 !$#authors Han, L.; Wong, D.; Dhaka, A.; Afar, D.; White, M.; Xie, W.; !1Herschman, H.; Witte, O.; Colicelli, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1997) 94:4954-4959 !$#title Protein binding and signaling properties of RIN1 suggest a !1unique effector function. !$#cross-references MUID:97289700; PMID:9144171 !$#accession A58613 !'##molecule_type mRNA !'##residues 1-783 ##label HAN !'##cross-references GB:L36463; NID:g1695232; PIDN:AAB67270.1; !1PID:g1695233 !'##experimental_source glioblastoma cell line U118-MG !'##note this report extends and revises the sequence from reference !1A38637 REFERENCE A38637 !$#authors Colicelli, J.; Nicolette, C.; Birchmeier, C.; Rodgers, L.; !1Riggs, M.; Wigler, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:2913-2917 !$#title Expression of three mammalian cDNAs that interfere with RAS !1function in Saccharomyces cerevisiae. !$#cross-references MUID:91187901; PMID:1849280 !$#accession A38637 !'##molecule_type mRNA !'##residues 'I',294-687,'PWPTGCPPLATSSTAGQSGLRPRGL' ##label COL !'##cross-references GB:M37192; NID:g190894; PIDN:AAA36552.1; !1PID:g190895 !'##note this sequence has been entended and revised; later functional !1studies using the full-length clone probably better reflect !1the biology of the protein REFERENCE A59017 !$#authors Han, L.; Colicelli, J. !$#journal Mol. Cell. Biol. (1995) 15:1318-1323 !$#title A human protein selected for interference with Ras function !1interacts directly with Ras and competes with Raf1. !$#cross-references MUID:95166216; PMID:7862125 !$#contents annotation COMMENT The RIN1 protein has both RAS and ABL binding domains and is !1a potential effector for both proteins. RIN1 also binds !1several 14-3-3 isoforms. In biological assays, RIN1 can !1enhance the transformation properties of the BCR/ABL !1oncogene. GENETICS !$#gene GDB:RIN1 !'##cross-references GDB:9957793 CLASSIFICATION #superfamily Ras interactor RIN1 KEYWORDS alternative splicing SUMMARY #length 783 #molecular-weight 84117 #checksum 8941 SEQUENCE /// ENTRY S00755 #type complete TITLE pleckstrin - human ALTERNATE_NAMES p47; platelet/leukocyte C kinase substrate (pleckstrin) ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 20-Apr-2000 ACCESSIONS S00755; A45762 REFERENCE S00755 !$#authors Tyers, M.; Rachubinski, R.A.; Stewart, M.I.; Varrichio, !1A.M.; Shorr, R.G.L.; Haslam, R.J.; Harley, C.B. !$#journal Nature (1988) 333:470-473 !$#title Molecular cloning and expression of the major protein kinase !1C substrate of platelets. !$#cross-references MUID:88232910; PMID:2897630 !$#accession S00755 !'##molecule_type mRNA !'##residues 1-350 ##label TYE !'##cross-references EMBL:X07743; NID:g35517; PIDN:CAA30564.1; !1PID:g35518 REFERENCE A45762 !$#authors Tyers, M.; Haslam, R.J.; Rachubinski, R.A.; Harley, C.B. !$#journal J. Cell. Biochem. (1989) 40:133-145 !$#title Molecular analysis of pleckstrin: the major protein kinase C !1substrate of platelets. !$#cross-references MUID:89359547; PMID:2768345 !$#accession A45762 !'##molecule_type mRNA !'##residues 1-350 ##label TY2 !'##cross-references GB:X07743; NID:g35517; PIDN:CAA30564.1; PID:g35518 !'##note 92-Arg was also found GENETICS !$#gene GDB:PLEK; p47 !'##cross-references GDB:9836816; OMIM:173570 !$#map_position 2pter-2qter CLASSIFICATION #superfamily pleckstrin; pleckstrin repeat homology KEYWORDS phosphoprotein; signal transduction FEATURE !$3-99 #domain pleckstrin repeat homology #label PLK1\ !$243-345 #domain pleckstrin repeat homology #label PLK2 SUMMARY #length 350 #molecular-weight 40082 #checksum 1536 SEQUENCE /// ENTRY S16948 #type complete TITLE insulin receptor substrate IRS-1 - rat ALTERNATE_NAMES insulin receptor substrate pp185 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 13-Jan-1995 #sequence_revision 13-Jan-1995 #text_change 18-Jun-1999 ACCESSIONS S16948; A39811 REFERENCE S16948 !$#authors Sun, X.J.; Rothenberg, P.; Kahn, C.R.; Backer, J.M.; Araki, !1E.; Wilden, P.A.; Cahill, D.A.; Goldstein, B.J.; White, M.F. !$#journal Nature (1991) 352:73-77 !$#title Structure of the insulin receptor substrate IRS-1 defines a !1unique signal transduction protein. !$#cross-references MUID:91287824; PMID:1648180 !$#accession S16948 !'##molecule_type mRNA !'##residues 1-1235 ##label SUN !'##cross-references EMBL:X58375; NID:g56503; PIDN:CAA41264.1; !1PID:g56504 REFERENCE A39811 !$#authors Rothenberg, P.L.; Lane, W.S.; Karasik, A.; Backer, J.; !1White, M.; Kahn, C.R. !$#journal J. Biol. Chem. (1991) 266:8302-8311 !$#title Purification and partial sequence analysis of pp185, the !1major cellular substrate of the insulin receptor tyrosine !1kinase. !$#cross-references MUID:91217066; PMID:2022647 !$#accession A39811 !'##molecule_type protein !'##residues 44-51;173-178;223-243;489-506;635-646;871-882,'I',884,'X', !1886-888;932-936,'XX',939-947;'L',1099-1106,'XP' ##label ROT !'##note the phosphotyrosine residue was not identified COMMENT This protein and the beta chain of the insulin receptor !1itself are the major targets of insulin-induced insulin !1receptor tyrosine kinase activity. COMMENT Phosphorylation of this protein in response to insulin is !1maximal at 30 seconds and is followed by almost complete !1dephosphorylation within three minutes, even in the !1continued presence of insulin. CLASSIFICATION #superfamily insulin receptor substrate IRS-1; pleckstrin !1repeat homology KEYWORDS phosphoprotein; signal transduction FEATURE !$11-113 #domain pleckstrin repeat homology #label PLK\ !$872-891 #region glutamine-rich SUMMARY #length 1235 #molecular-weight 131177 #checksum 315 SEQUENCE /// ENTRY S45444 #type complete TITLE BEM1 protein-binding protein BOB1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YBL0717; protein YBL085w ORGANISM #formal_name Saccharomyces cerevisiae DATE 09-Aug-1994 #sequence_revision 09-Sep-1994 #text_change 21-Jul-2000 ACCESSIONS S45444; S45421; S45826; S59218 REFERENCE S45444 !$#authors Bender, A.; Bender, L.; Kokojan, V. !$#submission submitted to the EMBL Data Library, April 1994 !$#description Yeast Bob1p (Bem1p-binding protein) binds to the SH3 !1domain-containing protein Bem1p. !$#accession S45444 !'##molecule_type DNA !'##residues 1-980 ##label BEN !'##cross-references EMBL:L31406; NID:g829041; PIDN:AAB08439.1; !1PID:g466436 REFERENCE S45387 !$#authors Obermaier, B.; Gassenhuber, J.; Piravandi, E.; Domdey, H. !$#submission submitted to the EMBL Data Library, May 1994 !$#description Sequence analysis of a 78,6 kb segment of the left end of !1Saccaromyces cerevisiae chromosome II. !$#accession S45421 !'##molecule_type DNA !'##residues 1-980 ##label OBE !'##cross-references EMBL:X79489; NID:g496661; PIDN:CAA56021.1; !1PID:g496694 REFERENCE S45816 !$#authors Domdey, H.; Gassenhuber, H.; Obermaier, B.; Piravandi, E. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S45826 !'##molecule_type DNA !'##residues 1-980 ##label DOM !'##cross-references EMBL:Z35846; NID:g536137; PIDN:CAA84906.1; !1PID:g536138; GSPDB:GN00002; MIPS:YBL085w REFERENCE S59184 !$#authors Obermaier, B.; Gassenhuber, J.; Piravandi, E.; Domdey, H. !$#journal Yeast (1995) 11:1103-1112 !$#title Sequence analysis of a 78.6 kb segment of the left end of !1Saccharomyces cerevisiae chromosome II. !$#cross-references MUID:96076635; PMID:7502586 !$#accession S59218 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-980 ##label OBW !'##cross-references EMBL:X79489; NID:g496661; PIDN:CAA56021.1; !1PID:g496694 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1May 1994 GENETICS !$#gene SGD:BOI1; BOB1; MIPS:YBL085w !'##cross-references MIPS:YBL085w; SGD:S0000181 !$#map_position 2L CLASSIFICATION #superfamily BEM1 protein-binding protein BOB1; pleckstrin !1repeat homology; SAM homology; SH3 homology FEATURE !$20-72 #domain SH3 homology #label SH3\ !$225-291 #domain SAM homology #label SAM SUMMARY #length 980 #molecular-weight 109294 #checksum 8660 SEQUENCE /// ENTRY TVHUVV #type fragments TITLE transforming protein vav - human (fragments) ALTERNATE_NAMES finger protein vav ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1991 #sequence_revision 03-May-1996 #text_change 18-Jun-1999 ACCESSIONS B39576; S05382 REFERENCE A39576 !$#authors Katzav, S.; Cleveland, J.L.; Heslop, H.E.; Pulido, D. !$#journal Mol. Cell. Biol. (1991) 11:1912-1920 !$#title Loss of the amino-terminal helix-loop-helix domain of the !1vav proto-oncogene activates its transforming potential. !$#cross-references MUID:91172176; PMID:2005887 !$#accession B39576 !'##molecule_type mRNA !'##residues 1-61 ##label KAT !'##cross-references GB:M59834; NID:g340189; PIDN:AAA63267.1; !1PID:g340190 !'##note the authors translated the codon CAA for residue 6 as Glu, CAG !1for residue 13 as Glu, CAG for residue 29 as Glu, CAG for !1residue 35 as Glu, and CAG for residue 45 as Glu REFERENCE S05382 !$#authors Katzav, S.; Martin-Zanca, D.; Barbacid, M. !$#journal EMBO J. (1989) 8:2283-2290 !$#title vav, a novel human oncogene derived from a locus !1ubiquitously expressed in hematopoietic cells. !$#cross-references MUID:90005432; PMID:2477241 !$#accession S05382 !'##molecule_type mRNA !'##residues 62-839 ##label KAT2 !'##cross-references EMBL:X16316 REFERENCE S23669 !$#authors Adams, J.M.; Houston, H.; Allen, J.; Lints, T.; Harvey, R. !$#journal Oncogene (1992) 7:611-618 !$#title The hematopoietically expressed vav proto-oncogene shares !1homology with the dbl GDP-GTP exchange factor, the bcr gene !1and a yeast gene (CDC24) involved in cytoskeletal !1organization. !$#cross-references MUID:92228488; PMID:1565462 !$#contents annotation !$#note in the sequence from mouse the authors find three additional !1nucleotides that produce a frameshift in the positions !1corresponding to 322-348 in the human, and suggest a similar !1misreading has occurred in the published human sequences COMMENT In comparing these sequences with the mouse (see !1PIR:TVMSVV), there appear to be six residues, 'LRPQMS', !1missing between the fragments after position 61. GENETICS !$#gene GDB:VAV1; VAV !'##cross-references GDB:127112; OMIM:164875 !$#map_position 19p13.3-19p13.3 CLASSIFICATION #superfamily vav transforming protein; CDC24 homology; !1protein kinase C zinc-binding repeat homology; SH2 homology; !1SH3 homology KEYWORDS phosphoprotein; transforming protein; zinc finger FEATURE !$126-170 #region acidic\ !$188-452 #domain CDC24 homology #label CD24\ !$509-557 #domain protein kinase C zinc-binding repeat homology !8#label KZ2\ !$522-542 #region zinc finger CCCC motif\ !$547-560 #region zinc finger HCCH motif\ !$598-648 #domain SH3 homology #label SH3A\ !$664-756 #domain SH2 homology #label SH2\ !$783-831 #domain SH3 homology #label SH3B\ !$433 #binding_site phosphate (Ser) (covalent) (by protein !8kinase A) #status predicted SUMMARY #length 839 #checksum 7065 SEQUENCE /// ENTRY TVMSVV #type complete TITLE transforming protein vav - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 03-May-1994 #sequence_revision 16-Feb-1996 #text_change 18-Jun-1999 ACCESSIONS A61187; A39576; S36941; S23669 REFERENCE A61187 !$#authors Coppola, J.; Bryant, S.; Koda, T.; Conway, D.; Barbacid, M. !$#journal Cell Growth Differ. (1991) 2:95-105 !$#title Mechanism of activation of the vav protooncogene. !$#cross-references MUID:91299578; PMID:2069873 !$#accession A61187 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-844 ##label COP REFERENCE A39576 !$#authors Katzav, S.; Cleveland, J.L.; Heslop, H.E.; Pulido, D. !$#journal Mol. Cell. Biol. (1991) 11:1912-1920 !$#title Loss of the amino-terminal helix-loop-helix domain of the !1vav proto-oncogene activates its transforming potential. !$#cross-references MUID:91172176; PMID:2005887 !$#accession A39576 !'##molecule_type mRNA !'##residues 1-28,'E',30-93 ##label KAT !'##cross-references GB:M59833; NID:g202343; PIDN:AAA63402.1; !1PID:g202344 REFERENCE S36941 !$#authors Adams, J.M. !$#submission submitted to the EMBL Data Library, January 1992 !$#accession S36941 !'##molecule_type mRNA !'##residues 1-323,'DLLMVPMQRVLKYHLLLQELVK',346-347,'QDAT',352,'K',354, !1'N',355-453,'R',455-844 ##label ADA !'##cross-references EMBL:X64361; NID:g55220; PIDN:CAA45713.1; !1PID:g55221 REFERENCE S23669 !$#authors Adams, J.M.; Houston, H.; Allen, J.; Lints, T.; Harvey, R. !$#journal Oncogene (1992) 7:611-618 !$#title The hematopoietically expressed vav proto-oncogene shares !1homology with the dbl GDP-GTP exchange factor, the bcr gene !1and a yeast gene (CDC24) involved in cytoskeletal !1organization. !$#cross-references MUID:92228488; PMID:1565462 !$#contents annotation; the authors note the frameshift difference with !1sequence in A61187 !$#note the complete sequence was submitted to Genbank; see S36941 GENETICS !$#gene vav CLASSIFICATION #superfamily vav transforming protein; CDC24 homology; !1protein kinase C zinc-binding repeat homology; SH2 homology; !1SH3 homology KEYWORDS phosphoprotein; transforming protein; zinc finger FEATURE !$32-102 #region leucine-rich\ !$132-176 #region acidic\ !$194-458 #domain CDC24 homology #label CD24\ !$336-340 #region proline-rich\ !$486-493 #region nuclear location signal\ !$515-563 #domain protein kinase C zinc-binding repeat homology !8#label KZ1\ !$528-548 #region zinc finger CCCC motif\ !$553-566 #region zinc finger HCCH motif\ !$575-582 #region nuclear location signal\ !$604-654 #domain SH3 homology #label SH3A\ !$606-609 #region proline-rich\ !$670-761 #domain SH2 homology #label SH2\ !$788-836 #domain SH3 homology #label SH3B\ !$439 #binding_site phosphate (Ser) (covalent) (by protein !8kinase A) #status predicted SUMMARY #length 844 #molecular-weight 97298 #checksum 5962 SEQUENCE /// ENTRY TVFV10 #type complete TITLE transforming protein crk - avian sarcoma virus CT10 ORGANISM #formal_name avian sarcoma virus CT10 DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 03-Mar-1995 ACCESSIONS B29851 REFERENCE S00872 !$#authors Mayer, B.J.; Hamaguchi, M.; Hanafusa, H. !$#journal Nature (1988) 332:272-275 !$#title A novel viral oncogene with structural similarity to !1phospholipase C. !$#cross-references MUID:88156964; PMID:2450282 !$#accession B29851 !'##molecule_type genomic RNA !'##residues 1-232 ##label MAY !'##cross-references EMBL:Y00302 GENETICS !$#gene crk CLASSIFICATION #superfamily crk transforming protein; SH2 homology; SH3 !1homology KEYWORDS transforming protein FEATURE !$40-146 #domain SH2 homology #status atypical #label SH2\ !$167-215 #domain SH3 homology #label SH3 SUMMARY #length 232 #molecular-weight 25343 #checksum 8901 SEQUENCE /// ENTRY A49011 #type complete TITLE c-Crk - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A49011 REFERENCE A49011 !$#authors Reichman, C.T.; Mayer, B.J.; Keshav, S.; Hanafusa, H. !$#journal Cell Growth Differ. (1992) 3:451-460 !$#title The product of the cellular crk gene consists primarily of !1SH2 and SH3 regions. !$#cross-references MUID:93041379; PMID:1329926 !$#accession A49011 !'##status preliminary !'##molecule_type mRNA !'##residues 1-305 ##label REI !'##cross-references GB:L08168; GB:M32398; NID:g212527; PIDN:AAA49001.1; !1PID:g212528 !'##experimental_source embryo, brain !'##note sequence extracted from NCBI backbone (NCBIN:117106, !1NCBIP:117107) CLASSIFICATION #superfamily crk transforming protein; SH2 homology; SH3 !1homology FEATURE !$13-119 #domain SH2 homology #label SH2\ !$140-188 #domain SH3 homology #label SH3 SUMMARY #length 305 #molecular-weight 33805 #checksum 9452 SEQUENCE /// ENTRY A39651 #type complete TITLE discs-large tumor suppressor - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A39651 REFERENCE A39651 !$#authors Woods, D.F.; Bryant, P.J. !$#journal Cell (1991) 66:451-464 !$#title The discs-large tumor suppressor gene of Drosophila encodes !1a guanylate kinase homolog localized at septate junctions. !$#cross-references MUID:91330294; PMID:1651169 !$#accession A39651 !'##molecule_type mRNA !'##residues 1-960 ##label WOO !'##cross-references GB:M73529; NID:g157243; PIDN:AAA28468.1; !1PID:g157244 COMMENT Loss of this protein causes large imaginal disks by allowing !1neoplastic overgrowth. The presence of a guanylate kinase !1domain suggests that function of this protein involves !1signal transduction to control cellular proliferation. GENETICS !$#gene FlyBase:dlg1 !'##cross-references FlyBase:FBgn0001624 CLASSIFICATION #superfamily discs-large tumor suppressor; GLGF domain !1homology; guanylate kinase homology; SH3 homology KEYWORDS signal transduction FEATURE !$45-123 #domain GLGF domain homology #label GLG1\ !$159-241 #domain GLGF domain homology #label GLG2\ !$491-563 #domain GLGF domain homology #label GLG3\ !$607-665 #domain SH3 homology #label SH3\ !$771-948 #domain guanylate kinase homology #label GKI SUMMARY #length 960 #molecular-weight 102468 #checksum 8684 SEQUENCE /// ENTRY TWBYA1 #type complete TITLE protein N-acetyltransferase (EC 2.3.1.-) chain ARD1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES arrest-defective protein 1; protein YHR013c ORGANISM #formal_name Saccharomyces cerevisiae DATE 28-Dec-1987 #sequence_revision 10-Feb-1995 #text_change 23-Mar-2001 ACCESSIONS S46783; A23640 REFERENCE S46774 !$#authors Du, Z. !$#submission submitted to the EMBL Data Library, June 1994 !$#description The sequence of S. cerevisiae cosmid L2825. !$#accession S46783 !'##molecule_type DNA !'##residues 1-238 ##label DUZ !'##cross-references EMBL:U10400; NID:g500701; PIDN:AAB68937.1; !1PID:g500702; GSPDB:GN00008; MIPS:YHR013c REFERENCE A23640 !$#authors Whiteway, M.; Szostak, J.W. !$#journal Cell (1985) 43:483-492 !$#title The ARD1 gene of yeast functions in the switch between the !1mitotic cell cycle and alternative developmental pathways. !$#cross-references MUID:86079530; PMID:3907857 !$#accession A23640 !'##molecule_type DNA !'##residues 1-36,'T',38-238 ##label WHI !'##cross-references EMBL:M11621; NID:g171069; PIDN:AAA66323.1; !1PID:g806323 GENETICS !$#gene SGD:ARD1; MIPS:YHR013c !'##cross-references SGD:S0001055; MIPS:YHR013c !$#map_position 8R FUNCTION !$#description catalyzes the acetylation of the amino terminal of proteins !$#pathway protein maturation !$#note in this organism may be required for transcription of genes !1involved in execution of alternatives to the mitotic cell !1cycle such as a-mating, stationary phase, and sporulation CLASSIFICATION #superfamily arrest-defective protein 1 KEYWORDS acyltransferase SUMMARY #length 238 #molecular-weight 27603 #checksum 6369 SEQUENCE /// ENTRY COZPME #type complete TITLE mei2 protein - fission yeast (Schizosaccharomyces pombe) ORGANISM #formal_name Schizosaccharomyces pombe DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 10-Dec-1999 ACCESSIONS S00391; T38436 REFERENCE S00391 !$#authors Watanabe, Y.; Iino, Y.; Furuhata, K.; Shimoda, C.; Yamamoto, !1M. !$#journal EMBO J. (1988) 7:761-767 !$#title The S. pombe mei2 gene encoding a crucial molecule for !1commitment to meiosis is under the regulation of cAMP. !$#cross-references MUID:88283645; PMID:2840284 !$#accession S00391 !'##molecule_type DNA !'##residues 1-750 ##label WAT !'##cross-references EMBL:X07180; NID:g4990; PIDN:CAA30165.1; PID:g4991 REFERENCE Z21793 !$#authors McDougall, R.; Wood, V.; Barrell, B.G.; Rajandream, M.A. !$#submission submitted to the EMBL Data Library, December 1997 !$#accession T38436 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-750 ##label MCD !'##cross-references EMBL:AL009227; PIDN:CAA15822.1; GSPDB:GN00066; !1SPDB:SPAC27D7.03c !'##experimental_source strain 972h-; cosmid c27D7 COMMENT This protein is required for the initiation of meiosis. GENETICS !$#gene mei2 !$#map_position 1 CLASSIFICATION #superfamily mei2 protein KEYWORDS meiosis SUMMARY #length 750 #molecular-weight 82676 #checksum 4523 SEQUENCE /// ENTRY COBYW2 #type complete TITLE WHI2 protein - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES growth regulator protein; protein O2766; protein YOR043w ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1992 #sequence_revision 02-Aug-1996 #text_change 16-Jun-2000 ACCESSIONS S66917; JT0319 REFERENCE S66907 !$#authors Landt, O.; Hiesel, R.; Unseld, M. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S66917 !'##molecule_type DNA !'##residues 1-486 ##label LAN !'##cross-references EMBL:Z74951; NID:g1420168; PIDN:CAA99234.1; !1PID:g1420169; GSPDB:GN00015; MIPS:YOR043w !'##experimental_source strain S288C REFERENCE JT0319 !$#authors Kelly, D.E.; Trevethick, J.; Mountain, H.; Sudbery, P.E. !$#journal Gene (1988) 66:205-213 !$#title Transcript characterisation, gene disruption and nucleotide !1sequence of the Saccharomyces cerevisiae WHI2 gene. !$#cross-references MUID:89006262; PMID:3049245 !$#accession JT0319 !'##molecule_type DNA !'##residues 1-215,'L',217-486 ##label KEL !'##cross-references GB:M21089; NID:g173188; PIDN:AAA35218.1; !1PID:g173189 GENETICS !$#gene SGD:WHI2; MIPS:YOR043w !'##cross-references SGD:S0005569; MIPS:YOR043w !$#map_position 15R CLASSIFICATION #superfamily Saccharomyces cerevisiae WHI2 protein KEYWORDS cell cycle control SUMMARY #length 486 #molecular-weight 55346 #checksum 209 SEQUENCE /// ENTRY BVBYK5 #type complete TITLE killer toxin resistance protein KRE5 precursor - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein O6254; protein YOR336w ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1991 #sequence_revision 10-May-1996 #text_change 16-Jun-2000 ACCESSIONS S62066; A36327; S67243; S71974; S12202 REFERENCE S62058 !$#authors Parle, A.G.; Hand, N.J.; Goulding, S.G.; Wolfe, K.H. !$#submission submitted to the EMBL Data Library, June 1995 !$#description Sequence of 29 kilobases around the PDR10 locus on the right !1arm of Saccharomyces cerevisiae chromosome XV: similarity to !1part of chromosome I. !$#accession S62066 !'##molecule_type DNA !'##residues 1-1365 ##label PAR !'##cross-references EMBL:Z49821; NID:g1163062; PIDN:CAA89981.1; !1PID:g1163070 REFERENCE A36327 !$#authors Meaden, P.; Hill, K.; Wagner, J.; Slipetz, D.; Sommer, S.S.; !1Bussey, H. !$#journal Mol. Cell. Biol. (1990) 10:3013-3019 !$#title The yeast KRE5 gene encodes a probable endoplasmic reticulum !1protein required for (1->6)-beta-D-glucan synthesis and !1normal cell growth. !$#cross-references MUID:90258892; PMID:2188106 !$#accession A36327 !'##molecule_type DNA !'##residues 1-581,583-779,'I',781,'IKMKCQKQNISK',794,'K',795-1365 !1##label MEA !'##cross-references EMBL:M33556; NID:g171794; PIDN:AAA34725.1; !1PID:g171795 REFERENCE S67233 !$#authors Goulding, S.E.; Hand, N.J.; Parle-McDermott, A.G.; Wolfe, !1K.H. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67243 !'##molecule_type DNA !'##residues 1-1365 ##label GOU !'##cross-references EMBL:Z75244; NID:g1420730; PIDN:CAA99659.1; !1PID:g1420731; GSPDB:GN00015; MIPS:YOR336w !'##experimental_source strain S288C REFERENCE S71966 !$#authors Parle-McDermott, A.G.; Hand, N.J.; Goulding, S.E.; Wolfe, !1K.H. !$#journal Yeast (1996) 12:999-1004 !$#title Sequence of 29 kb around the PDR10 locus on the right arm of !1Saccharomyces cerevisiae chromosome XV: similarity to part !1of chromosome I. !$#cross-references MUID:97051586; PMID:8896263 !$#accession S71974 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1365 ##label PAW !'##cross-references EMBL:Z49821; NID:g1163062; PIDN:CAA89981.1; !1PID:g1163070 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1995 GENETICS !$#gene SGD:KRE5; MIPS:YOR336w !'##cross-references SGD:S0005863; MIPS:YOR336w !$#map_position 15R FUNCTION !$#description required for normal cell growth !$#pathway (1->6)-beta-D-glucan biosynthesis CLASSIFICATION #superfamily KRE5 protein KEYWORDS endoplasmic reticulum; glycoprotein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-1365 #product killer toxin resistance protein KRE5 #status !8predicted #label MAT\ !$1362-1365 #region endoplasmic reticulum retention signal !8#status predicted\ !$115,228,293,457, !$519,523,604,644, !$870,1091,1150,1195 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1365 #molecular-weight 156476 #checksum 1235 SEQUENCE /// ENTRY BVBYL1 #type complete TITLE guanine nucleotide-releasing factor LTE1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YAL024c ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1991 #sequence_revision 03-Nov-1995 #text_change 16-Jun-2000 ACCESSIONS S51997; S45454; S43456; S05869; S46646 REFERENCE S51956 !$#authors Bussey, H.; Kaback, D.B.; Zhong, W.; Vo, D.T.; Clark, M.W.; !1Fortin, N.; Hall, J.; Ouellette, B.F.F.; Keng, T.; Barton, !1A.B.; Su, Y.; Davies, C.K.; Storms, R.K. !$#submission submitted to the EMBL Data Library, August 1994 !$#description The sequence of chromosome 1 of Saccharomyces cerevisiae. !$#accession S51997 !'##molecule_type DNA !'##residues 1-1435 ##label BUS !'##cross-references EMBL:U12980; NID:g1326053; PIDN:AAC05008.1; !1PID:g595562; GSPDB:GN00001; MIPS:YAL024c REFERENCE S45454 !$#authors Keng, T.; Clark, M.W.; Storms, R.K.; Fortin, N.; Zhong, W.; !1Ouellette, B.F.F.; Barton, A.B.; Kaback, D.B.; Bussey, H. !$#journal Yeast (1994) 10:953-958 !$#title LTE1 of Saccharomyces cerevisiae is a 1435 codon open !1reading frame that has sequence similarities to guanine !1nucleotide releasing factors. !$#cross-references MUID:95076714; PMID:7985422 !$#accession S45454 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-301,'C',303-1435 ##label KEN !'##cross-references EMBL:L20125 REFERENCE S43456 !$#authors Shirayama, M.; Matsui, Y.; Tanaka, K.; Toh-E, A. !$#journal Yeast (1994) 10:451-461 !$#title Isolation of a CDC25 family gene, MSI2/LTE1, as a multicopy !1suppressor of iral. !$#cross-references MUID:95028143; PMID:7941731 !$#accession S43456 !'##molecule_type DNA !'##residues 1-997,'LIVH',1002,'RKCIDN',1010-1435 ##label SHI !'##cross-references GB:D21354; NID:g426455; PIDN:BAA04820.1; !1PID:g452242 REFERENCE S05869 !$#authors Wickner, R.B.; Koh, T.J.; Crowley, J.C.; O'Neil, J.; Kaback, !1D.B. !$#journal Yeast (1987) 3:51-57 !$#title Molecular cloning of chromosome I DNA from Saccharomyces !1cerevisiae: isolation of the MAK16 gene and analysis of an !1adjacent gene essential for growth at low temperatures. !$#cross-references MUID:89073921; PMID:3332963 !$#accession S05869 !'##molecule_type DNA !'##residues 1127-1160,'GE',1164-1435 ##label WIC !'##cross-references EMBL:M16076; NID:g171849; PIDN:AAA34746.1; !1PID:g171850 REFERENCE S46646 !$#authors Keng, T.; Clark, M.W.; Storms, R.K.; Fortin, N.; Zhong, W.; !1Ouellette, F.B.F.; Barton, A.B.; Kaback, D.B.; Bussey, H. !$#submission submitted to the EMBL Data Library, December 1993 !$#description LTE1 of Saccharomyces cerevisiae is a 1435 codon open !1reading frame that has sequence similarities to guanine !1nucleotide releasing factors. !$#accession S46646 !'##molecule_type DNA !'##residues 1-1435 ##label KEW !'##cross-references EMBL:L20125; NID:g437022; PIDN:AAA50468.1; !1PID:g437023 GENETICS !$#gene SGD:LTE1; MSI2; MIPS:YAL024c !'##cross-references SGD:S0000022; MIPS:YAL024c !$#map_position 1L CLASSIFICATION #superfamily guanine nucleotide-releasing factor LTE1; !1CDC25-type guanine nucleotide exchange activator homology FEATURE !$1190-1430 #domain CDC25-type guanine nucleotide exchange !8activator homology #label SOS SUMMARY #length 1435 #molecular-weight 163149 #checksum 8478 SEQUENCE /// ENTRY COBYD1 #type complete TITLE RED1 protein - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein L8479.6; protein YLR263w ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 21-Jul-2000 ACCESSIONS JQ0308; S51400; S05784 REFERENCE JQ0308 !$#authors Thompson, E.A.; Roeder, G.S. !$#journal Mol. Gen. Genet. (1989) 218:293-301 !$#title Expression and DNA sequence of RED1, a gene required for !1meiosis I chromosome segregation in yeast. !$#cross-references MUID:89384455; PMID:2550770 !$#accession JQ0308 !'##molecule_type DNA !'##residues 1-827 ##label THO !'##cross-references EMBL:X16183; NID:g4300; PIDN:CAA34306.1; PID:g4301 REFERENCE S51395 !$#authors Miller, N. !$#submission submitted to the EMBL Data Library, November 1994 !$#description The sequence of S. cerevisiae cosmid 8479. !$#accession S51400 !'##molecule_type DNA !'##residues 1-827 ##label MIL !'##cross-references EMBL:U17244; NID:g577171; PIDN:AAB67376.1; !1PID:g577177; GSPDB:GN00012; MIPS:YLR263w COMMENT This protein is required for chromosome segregation at the !1first meiotic division. GENETICS !$#gene SGD:RED1; MIPS:YLR263w !'##cross-references SGD:S0004253; MIPS:YLR263w !$#map_position 12R CLASSIFICATION #superfamily RED1 protein KEYWORDS meiosis SUMMARY #length 827 #molecular-weight 95538 #checksum 2480 SEQUENCE /// ENTRY RGBYI2 #type complete TITLE probable GTPase-activating protein IRA2 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES GLC4 protein; protein O0985; protein YOL081w; protein YOL0951 ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1991 #sequence_revision 16-Aug-1996 #text_change 03-Dec-1999 ACCESSIONS S66775; S66774; A35656; S48254; S50426; S11190; S38505 REFERENCE S66775 !$#authors Zumstein, E.; Pearson, B.M.; Kalogeropoulos, A.; Schweizer, !1M. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S66775 !'##molecule_type DNA !'##residues 1-2423 ##label ZUM !'##cross-references EMBL:Z74823; GSPDB:GN00015; MIPS:YOL081w !'##experimental_source strain S288C REFERENCE S66756 !$#authors Alexandraki, D.; Katsoulou, C.; Tzermia, M. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S66774 !'##molecule_type DNA !'##residues 1983-3079 ##label ALE !'##cross-references EMBL:Z74823; GSPDB:GN00015; MIPS:YOL081w !'##experimental_source strain S288C REFERENCE A35656 !$#authors Tanaka, K.; Nakafuku, M.; Tamanoi, F.; Kaziro, Y.; !1Matsumoto, K.; Toh-e, A. !$#journal Mol. Cell. Biol. (1990) 10:4303-4313 !$#title IRA2, a second gene of Saccharomyces cerevisiae that encodes !1a protein with a domain homologous to mammalian ras !1GTPase-activating protein. !$#cross-references MUID:90318397; PMID:2164637 !$#accession A35656 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-2308,'V',2310-2316,'I',2318-3079 ##label TAN !'##cross-references EMBL:M33779; NID:g171761; PIDN:AAA34710.1; !1PID:g171762 REFERENCE S48253 !$#authors Zumstein, E.; Griffin, H.; Schweizer, M. !$#journal Yeast (1994) 10:1383-1387 !$#title Sequence of a 10.27 kb segment on the left arm of chromosome !1XV from Saccharomyces cerevisiae includes part of the IRA2 !1gene and a putative new gene. !$#cross-references MUID:95208358; PMID:7900427 !$#accession S48254 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-2423 ##label ZU2 !'##cross-references EMBL:X75449; NID:g414079; PIDN:CAA53202.1; !1PID:g414081 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1993 REFERENCE S50410 !$#authors Zumstein, E.; Pearson, B.M.; Kalogeropoulos, A.; Schweizer, !1M. !$#submission submitted to the EMBL Data Library, December 1994 !$#accession S50426 !'##molecule_type DNA !'##residues 1-2423 ##label ZU3 !'##cross-references EMBL:X83121; NID:g600461; PIDN:CAA58201.1; !1PID:g600480 GENETICS !$#gene SGD:IRA2; MIPS:YOL081w !'##cross-references SGD:S0005441; MIPS:YOL081w !$#map_position 15L CLASSIFICATION #superfamily regulatory protein IRA2; ras-specific GAP !1catalytic domain homology KEYWORDS transmembrane protein FEATURE !$693-709 #domain transmembrane #status predicted #label TM1\ !$1135-1151 #domain transmembrane #status predicted #label TM2\ !$1701-1910 #domain ras-specific GAP catalytic domain homology !8#label GAP\ !$1842-1858 #domain transmembrane #status predicted #label TM3\ !$2318-2334 #domain transmembrane #status predicted #label TM4\ !$2562-2578 #domain transmembrane #status predicted #label TM5 SUMMARY #length 3079 #molecular-weight 351665 #checksum 471 SEQUENCE /// ENTRY RGBYW6 #type complete TITLE regulatory protein SWI6 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein L9470.8; protein YLR182w ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 12-Nov-1999 ACCESSIONS S03161; S51427 REFERENCE S03161 !$#authors Breeden, L.; Nasmyth, K. !$#journal Nature (1987) 329:651-654 !$#title Similarity between cell-cycle genes of budding yeast and !1fission yeast and the Notch gene of Drosophila. !$#cross-references MUID:88014241; PMID:2821408 !$#accession S03161 !'##molecule_type DNA !'##residues 1-803 ##label BRE !'##cross-references EMBL:X06238; NID:g4597; PIDN:CAA29581.1; PID:g4598 REFERENCE S51414 !$#authors Wohldmann, P. !$#submission submitted to the EMBL Data Library, November 1994 !$#description The sequence of S. cerevisiae cosmid 9470. !$#accession S51427 !'##molecule_type DNA !'##residues 1-803 ##label WOH !'##cross-references EMBL:U17246; NID:g577192; PIDN:AAB67460.1; !1PID:g577200; GSPDB:GN00012; MIPS:YLR182w GENETICS !$#gene SGD:SWI6; SDS11; PSL8; MIPS:YLR182w !'##cross-references SGD:S0004172; MIPS:YLR182w !$#map_position 12R CLASSIFICATION #superfamily regulatory protein SWI6; ankyrin repeat !1homology KEYWORDS DNA binding; transcription regulation FEATURE !$317-349 #domain ankyrin repeat homology #label AN1\ !$469-501 #domain ankyrin repeat homology #label AN2 SUMMARY #length 803 #molecular-weight 90559 #checksum 7241 SEQUENCE /// ENTRY S27421 #type complete TITLE cell division control protein CDC13 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein D0859; protein YDL220c ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Dec-1993 #sequence_revision 06-Sep-1996 #text_change 16-Jun-2000 ACCESSIONS S67783; S27421 REFERENCE S67778 !$#authors Rasmussen, S.W. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67783 !'##molecule_type DNA !'##residues 1-924 ##label RAS !'##cross-references EMBL:Z74269; NID:g1431369; PIDN:CAA98800.1; !1PID:g1431371; GSPDB:GN00004; MIPS:YDL220c !'##experimental_source strain S288C REFERENCE S27421 !$#authors Hartwell, L.; Carson, M.J.; Garvik, B.M. !$#submission submitted to the EMBL Data Library, September 1991 !$#accession S27421 !'##molecule_type DNA !'##residues 1-39,'A',41-924 ##label HAR !'##cross-references EMBL:M76550; NID:g171180; PIDN:AAA99990.1; !1PID:g171181 GENETICS !$#gene SGD:CDC13; MIPS:YDL220c !'##cross-references SGD:S0002379; MIPS:YDL220c !$#map_position 4L CLASSIFICATION #superfamily cell division control protein CDC13 KEYWORDS transmembrane protein FEATURE !$31-47 #domain transmembrane #status predicted #label TMM SUMMARY #length 924 #molecular-weight 104903 #checksum 9374 SEQUENCE /// ENTRY RGBY23 #type complete TITLE cell division control protein CDC23 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YHR166c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 23-Mar-2001 ACCESSIONS S12330; A32697; S48906; JS0435 REFERENCE S12330 !$#authors Doi, A.; Doi, K. !$#journal Gene (1990) 91:123-126 !$#title Cloning and nucleotide sequence of the CDC23 gene of !1Saccharomyces cerevisiae. !$#cross-references MUID:90382687; PMID:2205535 !$#accession S12330 !'##molecule_type DNA !'##residues 1-626 ##label DOI !'##cross-references EMBL:D00610; NID:g218407; PIDN:BAA00485.1; !1PID:g218408 REFERENCE A32697 !$#authors Sikorski, R.S.; Boguski, M.S.; Goebl, M.; Hieter, P. !$#journal Cell (1990) 60:307-317 !$#title A repeating amino acid motif in CDC23 defines a family of !1proteins and a new relationship among genes required for !1mitosis and RNA synthesis. !$#cross-references MUID:90124639; PMID:2404612 !$#accession A32697 !'##molecule_type DNA !'##residues 1-626 ##label SIK !'##cross-references GB:D00610; EMBL:M31040; NID:g218407; !1PIDN:BAA00485.1; PID:g218408 REFERENCE S46673 !$#authors Macri, C. !$#submission submitted to the EMBL Data Library, February 1994 !$#description The sequence of S. cerevisiae cosmid 9986. !$#accession S48906 !'##molecule_type DNA !'##residues 1-626 ##label MAC !'##cross-references EMBL:U00027; NID:g551319; PIDN:AAB68012.1; !1PID:g458908; GSPDB:GN00008; MIPS:YHR166c GENETICS !$#gene SGD:CDC23; MIPS:YHR166c !'##cross-references SGD:S0001209; MIPS:YHR166c !$#map_position 8R CLASSIFICATION #superfamily cell division control protein CDC23; !1tetratricopeptide repeat homology KEYWORDS calcium binding; cell cycle control FEATURE !$153-161 #domain calcium binding #status predicted #label CAB\ !$215-248 #domain tetratricopeptide repeat homology #label TT1\ !$295-328 #domain tetratricopeptide repeat homology #label TT2\ !$329-362 #domain tetratricopeptide repeat homology #label TT3\ !$363-396 #domain tetratricopeptide repeat homology #label TT4\ !$397-430 #domain tetratricopeptide repeat homology #label TT5\ !$431-464 #domain tetratricopeptide repeat homology #label TT6\ !$465-498 #domain tetratricopeptide repeat homology #label TT7\ !$499-532 #domain tetratricopeptide repeat homology #label TT8\ !$536-569 #domain tetratricopeptide repeat homology #label TT9 SUMMARY #length 626 #molecular-weight 73113 #checksum 5818 SEQUENCE /// ENTRY RGBYC5 #type complete TITLE cell division control protein CDC25 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein L2142.6; protein YLR310c ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1988 #sequence_revision 31-Mar-1993 #text_change 21-Jul-2000 ACCESSIONS A26596; S51442; A23444; S43051; S47990 REFERENCE A26596 !$#authors Broek, D.; Toda, T.; Michaeli, T.; Levin, L.; Birchmeier, !1C.; Zoller, M.; Powers, S.; Wigler, M. !$#journal Cell (1987) 48:789-799 !$#title The S. cerevisiae CDC25 gene product regulates the RAS/ !1adenylate cyclase pathway. !$#cross-references MUID:87131091; PMID:3545497 !$#accession A26596 !'##molecule_type DNA !'##residues 1-1589 ##label BRO !'##cross-references EMBL:M15458; NID:g171184; PIDN:AAA34478.1; !1PID:g171185 REFERENCE S51437 !$#authors Pauley, A. !$#submission submitted to the EMBL Data Library, November 1994 !$#description The sequence of S. cerevisiae cosmid L2142. !$#accession S51442 !'##molecule_type DNA !'##residues 1-1589 ##label PAU !'##cross-references EMBL:U17247; NID:g577216; PIDN:AAB67360.1; !1PID:g577222; GSPDB:GN00012; MIPS:YLR310c REFERENCE A23444 !$#authors Camonis, J.H.; Kalekine, M.; Gondre, B.; Garreau, H.; !1Boy-Marcotte, E.; Jacquet, M. !$#journal EMBO J. (1986) 5:375-380 !$#title Characterization, cloning and sequence analysis of the CDC25 !1gene which controls the cyclic AMP level of Saccharomyces !1cerevisiae. !$#cross-references MUID:86220116; PMID:3011405 !$#accession A23444 !'##molecule_type DNA !'##residues 1-496,'Y',498-953,'LSVIMNLSR',964-1589 ##label CAM !'##cross-references EMBL:X03579; NID:g3483; PIDN:CAA27259.1; PID:g3484 REFERENCE S43051 !$#authors Daniel, J.H. !$#journal Curr. Genet. (1986) 10:879-885 !$#title The CDC25 "Start" gene of Saccharomyces cerevisiae: !1sequencing of the active C-terminal fragment and regional !1homologies with rhodopsin and cytochrome P450. !$#cross-references MUID:88194639; PMID:3329037 !$#accession S43051 !'##molecule_type DNA !'##residues 877-1589 ##label DAN !'##cross-references EMBL:X03579 GENETICS !$#gene SGD:CDC25; CTN1; MIPS:YLR310c !'##cross-references SGD:S0004301; MIPS:YLR310c !$#map_position 12R FUNCTION !$#description positive control of level of cellular cAMP at the stage at !1which the cell division cycle is triggered CLASSIFICATION #superfamily budding yeast CDC25; CDC25-type guanine !1nucleotide exchange activator homology; SH3 homology KEYWORDS cell cycle control; transmembrane protein FEATURE !$65-123 #domain SH3 homology #label SH3\ !$1301-1542 #domain CDC25-type guanine nucleotide exchange !8activator homology #label SOS SUMMARY #length 1589 #molecular-weight 179090 #checksum 7509 SEQUENCE /// ENTRY RGBY36 #type complete TITLE cell division control protein CDC36 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein D1492; protein YDL165w; start protein CDC36 ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jun-2000 ACCESSIONS S12304; A26372; S61048; S67717 REFERENCE S05830 !$#authors Barker, D.G.; White, J.H.M.; Johnston, L.H. !$#journal Nucleic Acids Res. (1985) 13:8323-8337 !$#title The nucleotide sequence of the DNA ligase gene (CDC9) from !1Saccharomyces cerevisiae: a gene which is cell-cycle !1regulated and induced in response to DNA damage. !$#cross-references MUID:86093646; PMID:3909103 !$#accession S12304 !'##molecule_type DNA !'##residues 1-191 ##label BAR !'##cross-references EMBL:X03246; NID:g3514; PIDN:CAA27006.1; PID:g3516 REFERENCE A93635 !$#authors Ferguson, J.; Ho, J.Y.; Peterson, T.A.; Reed, S.I. !$#journal Nucleic Acids Res. (1986) 14:6681-6697 !$#title Nucleotide sequence of the yeast cell division cycle start !1genes CDC28, CDC36, CDC37, and CDC39, and a structural !1analysis of the predicted products. !$#cross-references MUID:86312926; PMID:3018676 !$#accession A26372 !'##molecule_type DNA !'##residues 1-191 ##label FER !'##cross-references GB:X04287; NID:g3490; PIDN:CAA27835.1; PID:g3491 REFERENCE S61010 !$#authors Pohl, T.M. !$#submission submitted to the EMBL Data Library, November 1995 !$#accession S61048 !'##molecule_type DNA !'##residues 1-191 ##label POH !'##cross-references EMBL:Z67750; NID:g1061256; PIDN:CAA91581.1; !1PID:g1061274 REFERENCE S67708 !$#authors Pohl, T.M. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67717 !'##molecule_type DNA !'##residues 1-191 ##label POW !'##cross-references EMBL:Z74213; NID:g1431261; PIDN:CAA98739.1; !1PID:g1431262; GSPDB:GN00004; MIPS:YDL165w !'##experimental_source strain S288C GENETICS !$#gene SGD:CDC36; MIPS:YDL165w !'##cross-references SGD:S0002324; MIPS:YDL165w !$#map_position 4L CLASSIFICATION #superfamily cell division control protein CDC36 KEYWORDS cell cycle control; transcription regulation SUMMARY #length 191 #molecular-weight 22362 #checksum 7370 SEQUENCE /// ENTRY S42228 #type complete TITLE replication licensing factor MCM2 - human ALTERNATE_NAMES CDCL1; minichromosome maintenance protein MCM2 homolog; protein BM28 ORGANISM #formal_name Homo sapiens #common_name man DATE 13-Aug-1999 #sequence_revision 13-Aug-1999 #text_change 20-Aug-1999 ACCESSIONS S42228 REFERENCE S42228 !$#authors Todorov, I.T.; Pepperkok, R.; Philipova, R.N.; Kearsey, !1S.E.; Ansorge, W.; Werner, D. !$#journal J. Cell Sci. (1994) 107:253-265 !$#title A human nuclear protein with sequence homology to a family !1of early S phase proteins is required for entry into S phase !1and for cell division. !$#cross-references MUID:94230605; PMID:8175912 !$#accession S42228 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-892 ##label TOD !'##cross-references EMBL:X67334; NID:g468703; PIDN:CAA47749.1; !1PID:g468704 COMMENT The complex of six MCM proteins is one of several proteins !1that must be bound at the origins of replication for the !1initiation of DNA replication. As replication proceeds, MCM !1proteins are phosphorylated and dissociate from the !1chromatin. GENETICS !$#gene GDB:MCM2; CDCL1; D3S3194; cdc19 !'##cross-references GDB:224876; OMIM:116945 !$#map_position 3q21-3q21 COMPLEX The predominant form is a heterohexamer of MCM2, MCM3, MCM4, !1MCM5, MCM6, and MCM7, sometimes called the RLF-M component !1of replication licensing factor. FUNCTION !$#description part of the replication licensing system that permits DNA !1replication to occur once and only once within a single cell !1division cycle CLASSIFICATION #superfamily replication licensing factor MCM2; MCM homology KEYWORDS cell cycle control; DNA replication initiation; !1heterohexamer; nucleus; phosphoprotein; zinc finger FEATURE !$283-786 #domain MCM homology #label MCM\ !$318-344 #region zinc finger CCCC motif SUMMARY #length 892 #molecular-weight 99235 #checksum 329 SEQUENCE /// ENTRY T10067 #type complete TITLE replication licensing factor MCM2 - mouse ALTERNATE_NAMES minichromosome maintenance protein MCM2 homolog ORGANISM #formal_name Mus musculus #common_name house mouse DATE 13-Aug-1999 #sequence_revision 13-Aug-1999 #text_change 21-Jul-2000 ACCESSIONS T10067 REFERENCE Z16934 !$#authors Kimura, H.; Ohtomo, T.; Yamaguchi, M.; Ishii, A.; Sugimoto, !1K. !$#journal Genes Cells (1996) 1:977-993 !$#title Mouse MCM proteins: complex formation and transportation to !1the nucleus. !$#cross-references MUID:97224213; PMID:9077461 !$#accession T10067 !'##molecule_type mRNA !'##residues 1-904 ##label KIM !'##cross-references EMBL:D86725; NID:g2381484; PIDN:BAA22148.1; !1PID:g2381485 COMMENT The complex of six MCM proteins is one of several proteins !1that must be bound at the origins of replication for the !1initiation of DNA replication. As replication proceeds, MCM !1proteins are phosphorylated and dissociate from the !1chromatin. COMPLEX The predominant form is a heterohexamer of MCM2, MCM3, MCM4, !1MCM5, MCM6, and MCM7, sometimes called the RLF-M component !1of replication licensing factor. FUNCTION !$#description part of the replication licensing system that permits DNA !1replication to occur once and only once within a single cell !1division cycle CLASSIFICATION #superfamily replication licensing factor MCM2; MCM homology KEYWORDS cell cycle control; DNA replication initiation; !1heterohexamer; nucleus; phosphoprotein; zinc finger FEATURE !$294-797 #domain MCM homology #label MCM\ !$329-355 #region zinc finger CCCC motif SUMMARY #length 904 #molecular-weight 102047 #checksum 6356 SEQUENCE /// ENTRY JC5085 #type complete TITLE replication licensing factor MCM2 [validated] - African clawed frog ALTERNATE_NAMES MCM2p; minichromosome maintenance protein MCM2 homolog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 13-Aug-1999 #sequence_revision 13-Aug-1999 #text_change 01-Dec-2000 ACCESSIONS JC5085; T47225 REFERENCE JC5085 !$#authors Miyake, S.; Saito, I.; Kobayashi, H.; Yamashita, S. !$#journal Gene (1996) 175:71-75 !$#title Identification of two Xenopus laevis genes, xMCM2 and !1xCDC46, with sequence homology to MCM genes involved in DNA !1replication. !$#cross-references MUID:97074651; PMID:8917078 !$#contents oocyte !$#accession JC5085 !'##molecule_type mRNA !'##residues 1-886 ##label MIY !'##cross-references DDBJ:D63919; NID:g1753192; PIDN:BAA09948.1; !1PID:g1753193 REFERENCE Z24400 !$#authors Kubota, Y.; Mimura, S.; Nishimoto, S.; Masuda, T.; Nojima, !1H.; Takisawa, H. !$#journal EMBO J. (1997) 16:3320-3331 !$#title Licensing of DNA replication by a multi-protein complex of !1MCM/P1 proteins in Xenopus eggs. !$#cross-references MUID:97357318; PMID:9214647 !$#accession T47225 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-168,'K',170-438,'G',440-562,'L',564-727,'M',729-886 !1##label KUB !'##cross-references EMBL:U44047; NID:g2231168; PIDN:AAC60223.1; !1PID:g2231169 COMMENT The complex of six MCM proteins is one of several proteins !1that must be bound at the origins of replication for the !1initiation of DNA replication. As replication proceeds, MCM !1proteins are phosphorylated and dissociate from the !1chromatin. GENETICS !$#gene MCM2 COMPLEX The predominant form is a heterohexamer; the complex !1consists of MCM2 (PIR:T47225), MCM3 (PIR:T47226), MCM4 !1(PIR:T47223), MCM5 (PIR:T47224), MCM6 (PIR:T47222), and MCM7 !1(PIR:T47221) [validated, MUID:97357318], sometimes called !1the RLF-M component of replication licensing factor. FUNCTION !$#description MCM2 is a component of the replication licensing factor that !1permits DNA replication to occur once and only once within a !1single cell division cycle [validated, MUID:97357318] CLASSIFICATION #superfamily replication licensing factor MCM2; MCM homology KEYWORDS cell cycle control; DNA replication initiation; !1heterohexamer; nucleus; phosphoprotein; zinc finger FEATURE !$279-779 #domain MCM homology #label MCM\ !$314-340 #region zinc finger CCCC motif SUMMARY #length 886 #molecular-weight 100376 #checksum 1615 SEQUENCE /// ENTRY B48723 #type complete TITLE replication licensing factor MCM2 homolog nda1 - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES cell division cycle protein cdc19 ORGANISM #formal_name Schizosaccharomyces pombe DATE 13-Aug-1999 #sequence_revision 13-Aug-1999 #text_change 18-Jul-2001 ACCESSIONS B48723; T40418; T52476 REFERENCE A48723 !$#authors Miyake, S.; Okishio, N.; Samejima, I.; Hiraoka, Y.; Toda, !1T.; Saitoh, I.; Yanagida, M. !$#journal Mol. Biol. Cell (1993) 4:1003-1015 !$#title Fission yeast genes nda1(+) and nda4(+), mutations of which !1lead to S-phase block, chromatin alteration and Ca(2+) !1suppression, are members of the CDC46/MCM2 family. !$#cross-references MUID:94129084; PMID:8298187 !$#accession B48723 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-830 ##label MIY !'##cross-references GB:S68468; NID:g545212; PIDN:AAC60569.1; !1PID:g545213 REFERENCE Z21927 !$#authors McDougall, R.C.; Rajandream, M.A.; Barrell, B.G.; Brown, S.; !1Harris, D. !$#submission submitted to the EMBL Data Library, October 1999 !$#accession T40418 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-830 ##label MCD !'##cross-references EMBL:AL121863; PIDN:CAB58403.1; GSPDB:GN00067; !1SPDB:SPBC4.04c !'##experimental_source strain 972h-; cosmid c4 REFERENCE Z26087 !$#authors Forsburg, S.L.; Nurse, P. !$#journal J. Cell Sci. (1994) 107:2779-2788 !$#title The fission yeast cdc19+ gene encodes a member of the MCM !1family of replication proteins. !$#cross-references MUID:95181580; PMID:7876346 !$#accession T52476 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-830 ##label FOR !'##cross-references EMBL:U08048; PIDN:AAC48930.1 COMMENT The complex of six MCM proteins is one of several proteins !1that must be bound at the origins of replication for the !1initiation of DNA replication. As replication proceeds, MCM !1proteins are phosphorylated and dissociate from the !1chromatin. GENETICS !$#gene nda1+ !$#map_position 2 !$#introns 78/2 !$#note cdc19+ COMPLEX The predominant form is a heterohexamer of MCM2, MCM3, MCM4, !1MCM5, MCM6, and MCM7, sometimes called the RLF-M component !1of replication licensing factor. FUNCTION !$#description part of the replication licensing system that permits DNA !1replication to occur once and only once within a single cell !1division cycle, plays a potentially conserved role in S !1phase [validated, MUID:95181580] CLASSIFICATION #superfamily replication licensing factor MCM2; MCM homology KEYWORDS cell cycle control; DNA replication initiation; !1heterohexamer; nucleus; phosphoprotein; zinc finger FEATURE !$299-804 #domain MCM homology #label MCM\ !$334-360 #region zinc finger CCCC motif SUMMARY #length 830 #molecular-weight 92830 #checksum 2624 SEQUENCE /// ENTRY S45757 #type complete TITLE replication licensing factor MCM2 [validated] - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES minichromosome maintenance protein MCM2; protein YBL023c; protein YBL0438 ORGANISM #formal_name Saccharomyces cerevisiae DATE 13-Aug-1999 #sequence_revision 13-Aug-1999 #text_change 21-Jul-2000 ACCESSIONS S45757; S50306; S43939; B39630; A39630 REFERENCE S45745 !$#authors Goffeau, A.; Jonniaux, J.L.; Purnelle, B.; Skala, J.; de !1Wergifosse, P.; van Dyck, L. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S45757 !'##molecule_type DNA !'##residues 1-868 ##label GOF !'##cross-references EMBL:Z35784; NID:g536020; PIDN:CAA84842.1; !1PID:g536021; GSPDB:GN00002; MIPS:YBL023c REFERENCE S50299 !$#authors van Dyck, L.; Jonniaux, J.L.; de Melo Barreiros, T.; Kleine, !1K.; Goffeau, A. !$#journal Yeast (1994) 10:1663-1673 !$#title Analysis of a 17.4 kb DNA segment of yeast chromosome II !1encompassing the ribosomal protein L19 as well as proteins !1with homologies to components of the hnRNP and snRNP !1complexes and to the human proliferation-associated p120 !1antigen. !$#cross-references MUID:95242843; PMID:7725803 !$#accession S50306 !'##molecule_type DNA !'##residues 1-868 ##label VAW !'##cross-references EMBL:X77291; NID:g602888; PIDN:CAA54503.1; !1PID:g602896 REFERENCE S43937 !$#authors van Dyck, L.; Pearce, D.A.; Sherman, F. !$#journal J. Biol. Chem. (1994) 269:238-242 !$#title PIM1 encodes a mitochondrial ATP-dependent protease that is !1required for mitochondrial function in the yeast !1Saccharomyces cerevisiae. !$#cross-references MUID:94103216; PMID:8276800 !$#accession S43939 !'##molecule_type DNA !'##residues 1-85 ##label VAN !'##cross-references EMBL:X74544; NID:g453234; PIDN:CAA52635.1; !1PID:g453237 REFERENCE A39632 !$#authors Tye, B.K. !$#submission submitted to GenBank, June 1990 !$#accession B39630 !'##molecule_type DNA !'##residues 1-163,'T',165-171,'IH',174-528,'P',530-577,'R',579-582,'H', !1584-711,'Q',713-732,748-858, !1'SLSQFIPWVTKTLLFLRISGYEDKKFSVSIHVLAILFSIYKFPLFFV' ##label !1TYE !'##cross-references GB:X53539; NID:g3911; PIDN:CAA37615.1; PID:g3912 REFERENCE A39630 !$#authors Yan, H.; Gibson, S.; Tye, B.K. !$#journal Genes Dev. (1991) 5:944-957 !$#title Mcm2 and Mcm3, two proteins important for ARS activity, are !1related in structure and function. !$#cross-references MUID:91257581; PMID:2044961 !$#accession A39630 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-79,'Y',81-163,'T',165-171,'IH',174-319,'R',321-528,'P', !1530-577,'R',579-582,'H',584-711,'Q',713-732,748-858, !1'SLSQFIPWVTKTLLFLRISGYEDKKFSVSIHVLAILFSIYKFPLFFV' ##label !1YAN !'##cross-references GB:X53539 COMMENT The complex of six MCM proteins is one of several proteins !1that must be bound at the origins of replication for the !1initiation of DNA replication. As replication proceeds, MCM !1proteins are phosphorylated and dissociate from the !1chromatin. GENETICS !$#gene SGD:MCM2; MIPS:YBL023c !'##cross-references SGD:S0000119; MIPS:YBL023c !$#map_position 2L FUNCTION !$#description MCM2 is a component of the replication licensing factor that !1permits DNA replication to occur once and only once within a !1single cell division cycle [validated, MUID:98001511] CLASSIFICATION #superfamily replication licensing factor MCM2; MCM homology KEYWORDS cell cycle control; DNA replication initiation; !1heterohexamer; nucleus; phosphoprotein; zinc finger FEATURE !$306-840 #domain MCM homology #label MCM\ !$341-367 #region zinc finger CCCC motif SUMMARY #length 868 #molecular-weight 98779 #checksum 7206 SEQUENCE /// ENTRY S62594 #type complete TITLE replication licensing factor MCM3 - human ALTERNATE_NAMES DNA polymerase alpha-associated protein P1; minichromosome maintenance protein MCM3 homolog; replication origin activator ORGANISM #formal_name Homo sapiens #common_name man DATE 13-Aug-1999 #sequence_revision 13-Aug-1999 #text_change 20-Aug-1999 ACCESSIONS S62594; S22803; S17098 REFERENCE S62594 !$#authors Schulte, D. !$#submission submitted to the EMBL Data Library, September 1993 !$#accession S62594 !'##molecule_type mRNA !'##residues 1-808 ##label SCH !'##cross-references EMBL:X62153; NID:g397871; PIDN:CAA44078.1; !1PID:g397872 REFERENCE S22803 !$#authors Thoemmes, P.; Fett, R.; Schray, B.; Burkhart, R.; Barnes, !1M.; Kennedy, C.; Brown, N.C.; Knippers, R. !$#journal Nucleic Acids Res. (1992) 20:1069-1074 !$#title Properties of the nuclear P1 protein, a mammalian homologue !1of the yeast Mcm3 replication protein. !$#cross-references MUID:92195806; PMID:1549468 !$#accession S22803 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 563-808 ##label THO !'##cross-references EMBL:X62153 COMMENT The complex of six MCM proteins is one of several proteins !1that must be bound at the origins of replication for the !1initiation of DNA replication. As replication proceeds, MCM !1proteins are phosphorylated and dissociate from the !1chromatin. GENETICS !$#gene GDB:MCM3 !'##cross-references GDB:433797 !$#map_position 6p21.1-6p11 COMPLEX The predominant form is a heterohexamer of MCM2, MCM3, MCM4, !1MCM5, MCM6, and MCM7, sometimes called the RLF-M component !1of replication licensing factor. FUNCTION !$#description part of the replication licensing system that permits DNA !1replication to occur once and only once within a single cell !1division cycle CLASSIFICATION #superfamily human replication licensing factor MCM3; MCM !1homology KEYWORDS cell cycle control; DNA replication initiation; nucleus; !1phosphoprotein FEATURE !$113-648 #domain MCM homology #label MCM SUMMARY #length 808 #molecular-weight 90951 #checksum 4500 SEQUENCE /// ENTRY S22804 #type fragment TITLE replication licensing factor MCM3 - mouse (fragment) ALTERNATE_NAMES DNA polymerase alpha-associated protein P1; minichromosome maintenance protein MCM3 homolog; replication origin activator ORGANISM #formal_name Mus musculus #common_name house mouse DATE 13-Aug-1999 #sequence_revision 13-Aug-1999 #text_change 21-Jan-2000 ACCESSIONS S22804; S17100 REFERENCE S22803 !$#authors Thoemmes, P.; Fett, R.; Schray, B.; Burkhart, R.; Barnes, !1M.; Kennedy, C.; Brown, N.C.; Knippers, R. !$#journal Nucleic Acids Res. (1992) 20:1069-1074 !$#title Properties of the nuclear P1 protein, a mammalian homologue !1of the yeast Mcm3 replication protein. !$#cross-references MUID:92195806; PMID:1549468 !$#accession S22804 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-795 ##label THO !'##cross-references EMBL:X62154 REFERENCE S17098 !$#authors Knippers, R. !$#submission submitted to the EMBL Data Library, September 1991 !$#accession S17100 !'##molecule_type mRNA !'##residues 1-163,'N',165-300,'L',302-795 ##label KNI !'##cross-references EMBL:X62154; NID:g53550; PIDN:CAA44079.1; !1PID:g53551 COMMENT The complex of six MCM proteins is one of several proteins !1that must be bound at the origins of replication for the !1initiation of DNA replication. As replication proceeds, MCM !1proteins are phosphorylated and dissociate from the !1chromatin. COMPLEX The predominant form is a heterohexamer of MCM2, MCM3, MCM4, !1MCM5, MCM6, and MCM7, sometimes called the RLF-M component !1of replication licensing factor. FUNCTION !$#description part of the replication licensing system that permits DNA !1replication to occur once and only once within a single cell !1division cycle CLASSIFICATION #superfamily human replication licensing factor MCM3; MCM !1homology KEYWORDS cell cycle control; DNA replication initiation; nucleus; !1phosphoprotein FEATURE !$96-631 #domain MCM homology #label MCM SUMMARY #length 795 #checksum 6808 SEQUENCE /// ENTRY I51685 #type complete TITLE replication licensing factor MCM3 [validated] - African clawed frog ALTERNATE_NAMES DNA polymerase alpha-associated protein P1; minichromosome maintenance protein MCM3 homolog; replication origin activator ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 13-Aug-1999 #sequence_revision 13-Aug-1999 #text_change 21-Jul-2000 ACCESSIONS I51685; T47226; I51589 REFERENCE I51685 !$#authors Madine, M.A.; Khoo, C.Y.; Mills, A.D.; Laskey, R.A. !$#journal Nature (1995) 375:421-424 !$#title MCM3 complex required for cell cycle regulation of DNA !1replication in vertebrate cells. !$#cross-references MUID:95281058; PMID:7760938 !$#accession I51685 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-807 ##label MAD !'##cross-references EMBL:U26057; NID:g829620; PIDN:AAA80227.1; !1PID:g829621 !$#accession T47226 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-807 ##label MA2 !'##cross-references EMBL:U26057; NID:g829620; PIDN:AAA80227.1; !1PID:g829621 REFERENCE A56915 !$#authors Kubota, Y.; Mimura, S.; Nishimoto, S.; Takisawa, H.; Nojima, !1H. !$#journal Cell (1995) 81:601-609 !$#title Identification of the yeast MCM3-related protein as a !1component of Xenopus DNA replication licensing factor. !$#cross-references MUID:95277847; PMID:7758114 !$#accession I51589 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 2-205,'D',207-605,'D',607-700,'S',702-793,'G',795-807 !1##label KUB !'##cross-references GB:D38074; NID:g868011; PIDN:BAA07268.1; !1PID:g868012 COMMENT The complex of six MCM proteins is one of several proteins !1that must be bound at the origins of replication for the !1initiation of DNA replication. As replication proceeds, MCM !1proteins are phosphorylated and dissociate from the !1chromatin. GENETICS !$#gene Xmcm3 COMPLEX the replication licensing complex consists of at least six !1proteins; MCM2 (PIR:T47225), MCM3 (PIR:T47226), MCM4 !1(PIR:T47223), MCM5 (PIR:T47224), MCM6 (PIR:T47222), and MCM7 !1(PIR:T47221), sometimes called the RLF-M component of !1replication licensing factor [validated, MUID:97357318] FUNCTION !$#description MCM3 is a component of the replication licensing factor that !1permits DNA replication to occur once and only once within a !1single cell division cycle [validated, MUID:95281058] CLASSIFICATION #superfamily human replication licensing factor MCM3; MCM !1homology KEYWORDS cell cycle control; DNA replication initiation; nucleus; !1phosphoprotein FEATURE !$113-648 #domain MCM homology #label MCM SUMMARY #length 807 #molecular-weight 90357 #checksum 3404 SEQUENCE /// ENTRY I51022 #type fragment TITLE replication licensing factor MCM3 - eastern newt (fragment) ALTERNATE_NAMES B24 protein; DNA polymerase alpha-associated protein P1; minichromosome maintenance protein MCM3 homolog; replication origin activator ORGANISM #formal_name Notophthalmus viridescens, Triturus viridescens #common_name eastern newt DATE 13-Aug-1999 #sequence_revision 13-Aug-1999 #text_change 21-Jan-2000 ACCESSIONS I51022 REFERENCE I51022 !$#authors Bucci, S.; Ragghianti, M.; Nardi, I.; Bellini, M.; Mancino, !1G.; Lacroix, J.C. !$#journal Int. J. Dev. Biol. (1993) 37:509-517 !$#title Identification of an amphibian oocyte nuclear protein as a !1candidate for a role in embryonic DNA replication. !$#cross-references MUID:94235414; PMID:8179995 !$#accession I51022 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-744 ##label BUC !'##cross-references EMBL:X78322; NID:g467690; PIDN:CAA55125.1; !1PID:g467691 COMMENT The complex of six MCM proteins is one of several proteins !1that must be bound at the origins of replication for the !1initiation of DNA replication. As replication proceeds, MCM !1proteins are phosphorylated and dissociate from the !1chromatin. GENETICS !$#gene B24 COMPLEX The predominant form is a heterohexamer of MCM2, MCM3, MCM4, !1MCM5, MCM6, and MCM7, sometimes called the RLF-M component !1of replication licensing factor. FUNCTION !$#description part of the replication licensing system that permits DNA !1replication to occur once and only once within a single cell !1division cycle CLASSIFICATION #superfamily human replication licensing factor MCM3; MCM !1homology KEYWORDS cell cycle control; DNA replication initiation; nucleus; !1phosphoprotein FEATURE !$111-646 #domain MCM homology #label MCM SUMMARY #length 744 #checksum 5392 SEQUENCE /// ENTRY A36376 #type complete TITLE replication licensing factor MCM3 [validated] - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES minichromosome maintenance protein MCM3; protein YEL032w ORGANISM #formal_name Saccharomyces cerevisiae DATE 13-Aug-1999 #sequence_revision 13-Aug-1999 #text_change 02-Aug-2002 ACCESSIONS A36376; S50512; S30851 REFERENCE A36376 !$#authors Gibson, S.I.; Surosky, R.T.; Tye, B.K. !$#journal Mol. Cell. Biol. (1990) 10:5707-5720 !$#title The phenotype of the minichromosome maintenance mutant mcm3 !1is characteristic of mutants defective in DNA replication. !$#cross-references MUID:91042499; PMID:2233713 !$#accession A36376 !'##molecule_type DNA !'##residues 1-971 ##label GIB !'##cross-references GB:X53540; NID:g3913; PIDN:CAA37616.1; PID:g3914 REFERENCE S50491 !$#authors Dietrich, F.S. !$#submission submitted to the EMBL Data Library, December 1994 !$#description The sequence of S. cerevisiae cosmids 8199, 8334, and 9871. !$#accession S50512 !'##molecule_type DNA !'##residues 1-971 ##label DIE !'##cross-references EMBL:U18779; NID:g603625; PIDN:AAB65010.1; !1PID:g603647; GSPDB:GN00005; MIPS:YEL032w REFERENCE S30812 !$#authors Mulligan, J.T.; Dietrich, F.S.; Hennessey, K.M.; Sehl, P.; !1Komp, C.; Wei, Y.; Taylor, P.; Nakahara, K.; Roberts, D.; !1Davis, R.W. !$#submission submitted to the EMBL Data Library, February 1993 !$#accession S30851 !'##molecule_type DNA !'##residues 1-954 ##label MUL !'##cross-references EMBL:L10830 COMMENT The complex of six MCM proteins is one of several proteins !1that must be bound at the origins of replication for the !1initiation of DNA replication. As replication proceeds, MCM !1proteins are phosphorylated and dissociate from the !1chromatin. GENETICS !$#gene SGD:MCM3; MIPS:YEL032w !'##cross-references SGD:S0000758; MIPS:YEL032w !$#map_position 5L COMPLEX The predominant form is a heterohexamer of MCM2 !1(PIR:S45757), MCM3 (PIR:A36376), MCM4 (PIR:S56050), MCM5 !1(PIR:A39631), MCM6 (PIR:S64219), and MCM7 (PIR:S34027); !1sometimes called the RLF-M component of replication !1licensing factor. FUNCTION !$#description MCM3 is a component of the replication licensing factor that !1permits DNA replication to occur once and only once within a !1single cell division cycle [validated, MUID:98001511] CLASSIFICATION #superfamily human replication licensing factor MCM3; MCM !1homology KEYWORDS cell cycle control; DNA replication initiation; nucleus; !1phosphoprotein FEATURE !$168-732 #domain MCM homology #label MCM SUMMARY #length 971 #molecular-weight 107516 #checksum 6724 SEQUENCE /// ENTRY S65954 #type complete TITLE replication licensing factor MCM4 - human ALTERNATE_NAMES cell division cycle control protein CDC21/CDC54; S. cerevisiae minichromosome maintenance deficient 4 homolog ORGANISM #formal_name Homo sapiens #common_name man DATE 13-Aug-1999 #sequence_revision 13-Aug-1999 #text_change 21-Jan-2000 ACCESSIONS S65954; S43198; S41622 REFERENCE S65954 !$#authors Musahl, C.; Schulte, D.; Burkhart, R.; Knippers, R. !$#journal Eur. J. Biochem. (1995) 230:1096-1101 !$#title A human homologue of the yeast replication protein Cdc21. !1Interactions with other Mcm proteins. !$#cross-references MUID:95324568; PMID:7601140 !$#accession S65954 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues !1'IRHERVATSSASGRLPRNARRRGRALARSRRERPRCGAGQGSREAGPARACPCRAGTPS !1T',1-863 ##label MUS !'##cross-references EMBL:X74794; NID:g683749; PIDN:CAA52801.1; !1PID:g940536 REFERENCE S43198 !$#authors Hu, B. !$#submission submitted to the EMBL Data Library, August 1993 !$#accession S43198 !'##molecule_type mRNA !'##residues 'ARE',440-702 ##label HUB1 !'##cross-references EMBL:X74794 REFERENCE S41622 !$#authors Hu, B.; Burkhart, R.; Schulte, D.; Musahl, C.; Knippers, R. !$#journal Nucleic Acids Res. (1993) 21:5289-5293 !$#title The P1 family: a new class of nuclear mammalian proteins !1related to the yeast Mcm replication proteins. !$#cross-references MUID:94089373; PMID:8265339 !$#accession S41622 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 'ARE',440-636 ##label HUB2 !'##cross-references EMBL:X74794 COMMENT The complex of six MCM proteins is one of several proteins !1that must be bound at the origins of replication for the !1initiation of DNA replication. As replication proceeds, MCM !1proteins are phosphorylated and dissociate from the !1chromatin. GENETICS !$#gene GDB:MCM4; CDC21; CDC54 !'##cross-references GDB:433798 COMPLEX The predominant form is a heterohexamer of MCM2, MCM3, MCM4, !1MCM5, MCM6, and MCM7, sometimes called the RLF-M component !1of replication licensing factor. FUNCTION !$#description part of the replication licensing system that permits DNA !1replication to occur once and only once within a single cell !1division cycle CLASSIFICATION #superfamily replication licensing factor MCM4; MCM homology KEYWORDS cell cycle control; DNA replication initiation; !1heterohexamer; nucleus; phosphoprotein; zinc finger FEATURE !$271-764 #domain MCM homology #label MCM SUMMARY #length 863 #molecular-weight 96610 #checksum 4427 SEQUENCE /// ENTRY S56766 #type complete TITLE replication licensing factor MCM4 - mouse ALTERNATE_NAMES cell division cycle control protein CDC21/CDC54 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 13-Aug-1999 #sequence_revision 13-Aug-1999 #text_change 16-Jun-2000 ACCESSIONS S56766 REFERENCE S56766 !$#authors Kimura, H.; Takizawa, N.; Nozaki, N.; Sugimoto, K. !$#journal Nucleic Acids Res. (1995) 23:2097-2104 !$#title Molecular cloning of cDNA encoding mouse Cdc21 and CDC46 !1homologs and characterization of the products: physical !1interaction between P1(MCM3) and CDC46 proteins. !$#cross-references MUID:95334361; PMID:7610039 !$#accession S56766 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type mRNA !'##residues 1-862 ##label KIM !'##cross-references EMBL:D26089; NID:g940405; PIDN:BAA05082.1; !1PID:g940406 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1993 COMMENT The complex of six MCM proteins is one of several proteins !1that must be bound at the origins of replication for the !1initiation of DNA replication. As replication proceeds, MCM !1proteins are phosphorylated and dissociate from the !1chromatin. COMPLEX The predominant form is a heterohexamer of MCM2, MCM3, MCM4, !1MCM5, MCM6, and MCM7, sometimes called the RLF-M component !1of replication licensing factor. FUNCTION !$#description part of the replication licensing system that permits DNA !1replication to occur once and only once within a single cell !1division cycle CLASSIFICATION #superfamily replication licensing factor MCM4; MCM homology KEYWORDS cell cycle control; DNA replication initiation; !1heterohexamer; nucleus; phosphoprotein; zinc finger FEATURE !$270-763 #domain MCM homology #label MCM SUMMARY #length 862 #molecular-weight 96735 #checksum 6623 SEQUENCE /// ENTRY S64720 #type complete TITLE replication licensing factor MCM4 - African clawed frog ALTERNATE_NAMES cell division cycle control protein CDC21/CDC54 ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 13-Aug-1999 #sequence_revision 13-Aug-1999 #text_change 21-Jul-2000 ACCESSIONS S64720; S26643; S25529 REFERENCE S64720 !$#authors Coue, M.; Kearsey, S.E.; Mechali, M. !$#journal EMBO J. (1996) 15:1085-1097 !$#title Chromatin binding, nuclear localization and phosphorylation !1of Xenopus cdc21 are cell-cycle dependent and associated !1with the control of initiation of DNA replication. !$#cross-references MUID:96183193; PMID:8605878 !$#accession S64720 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type mRNA !'##residues 1-863 ##label COU !'##cross-references EMBL:U29178; NID:g1002597; PIDN:AAB01680.1; !1PID:g1002598 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1995 REFERENCE S26640 !$#authors Coxon, A.; Maundrell, K.; Kearsey, S.E. !$#journal Nucleic Acids Res. (1992) 20:5571-5577 !$#title Fission yeast cdc21(+) belongs to a family of proteins !1involved in an early step of chromosome replication. !$#cross-references MUID:93087163; PMID:1454522 !$#accession S26643 !'##molecule_type DNA !'##residues 513-523,'Y',525-538,'G',540-553,'G',555-588 ##label COX !'##cross-references EMBL:Z15033; NID:g64612; PIDN:CAA78751.1; !1PID:g64613 COMMENT The complex of six MCM proteins is one of several proteins !1that must be bound at the origins of replication for the !1initiation of DNA replication. As replication proceeds, MCM !1proteins are phosphorylated and dissociate from the !1chromatin. GENETICS !$#gene cdc21 COMPLEX The predominant form is a heterohexamer of MCM2, MCM3, MCM4, !1MCM5, MCM6, and MCM7, sometimes called the RLF-M component !1of replication licensing factor. FUNCTION !$#description part of the replication licensing system that permits DNA !1replication to occur once and only once within a single cell !1division cycle CLASSIFICATION #superfamily replication licensing factor MCM4; MCM homology KEYWORDS cell cycle control; DNA replication initiation; !1heterohexamer; nucleus; phosphoprotein; zinc finger FEATURE !$271-764 #domain MCM homology #label MCM SUMMARY #length 863 #molecular-weight 97178 #checksum 6655 SEQUENCE /// ENTRY S59872 #type complete TITLE replication licensing factor MCM4 - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES cell division cycle control protein CDC21/CDC54; gene disc proliferation abnormal protein ORGANISM #formal_name Drosophila melanogaster DATE 13-Aug-1999 #sequence_revision 13-Aug-1999 #text_change 21-Jan-2000 ACCESSIONS S59872 REFERENCE S59872 !$#authors Feger, G.; Vaessin, H.; Su, T.T.; Wolff, E.; Jan, L.Y.; Jan, !1Y.N. !$#journal EMBO J. (1995) 14:5387-5398 !$#title dpa, a member of the MCM family, is required for mitotic DNA !1replication but not endoreplication in Drosophila. !$#cross-references MUID:96080174; PMID:7489728 !$#accession S59872 !'##molecule_type mRNA !'##residues 1-866 ##label FEG !'##cross-references GB:S80255; NID:g1245869; PIDN:AAB35644.1; !1PID:g1245870 COMMENT The complex of six MCM proteins is one of several proteins !1that must be bound at the origins of replication for the !1initiation of DNA replication. As replication proceeds, MCM !1proteins are phosphorylated and dissociate from the !1chromatin. GENETICS !$#gene dpa; disc proliferation abnormal !'##cross-references FlyBase:FBgn0015929 COMPLEX The predominant form is a heterohexamer of MCM2, MCM3, MCM4, !1MCM5, MCM6, and MCM7, sometimes called the RLF-M component !1of replication licensing factor. FUNCTION !$#description part of the replication licensing system that permits DNA !1replication to occur once and only once within a single cell !1division cycle CLASSIFICATION #superfamily replication licensing factor MCM4; MCM homology KEYWORDS cell cycle control; DNA replication initiation; !1heterohexamer; nucleus; phosphoprotein; zinc finger FEATURE !$274-766 #domain MCM homology #label MCM SUMMARY #length 866 #molecular-weight 96623 #checksum 649 SEQUENCE /// ENTRY S56050 #type complete TITLE replication licensing factor MCM4 [validated] - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES cell division control protein CDC21/CDC54; protein YP9531.13; protein YPR019w ORGANISM #formal_name Saccharomyces cerevisiae DATE 13-Aug-1999 #sequence_revision 13-Aug-1999 #text_change 26-May-2000 ACCESSIONS S56050; S57553; S26641; S25527 REFERENCE S56049 !$#authors Dalton, S. !$#submission submitted to the EMBL Data Library, September 1994 !$#description Cdc47 and Cdc54 belong to a family of proteins essential for !1initiation of eukaryotic DNA replication. !$#accession S56050 !'##molecule_type DNA !'##residues 1-933 ##label DAL !'##cross-references EMBL:U14731; NID:g608170; PIDN:AAA86310.1; !1PID:g608171 REFERENCE S57541 !$#authors Bowman, S. !$#submission submitted to the EMBL Data Library, June 1995 !$#accession S57553 !'##molecule_type DNA !'##residues 1-933 ##label BOW !'##cross-references EMBL:Z49919; NID:g887584; PIDN:CAA90164.1; !1PID:g887597; GSPDB:GN00016; MIPS:YPR019w !'##experimental_source strain AB972 REFERENCE S26640 !$#authors Coxon, A.; Maundrell, K.; Kearsey, S.E. !$#journal Nucleic Acids Res. (1992) 20:5571-5577 !$#title Fission yeast cdc21(+) belongs to a family of proteins !1involved in an early step of chromosome replication. !$#cross-references MUID:93087163; PMID:1454522 !$#accession S26641 !'##molecule_type DNA !'##residues 571-646 ##label COX !'##cross-references EMBL:Z15032; NID:g3481; PIDN:CAA78750.1; PID:g3482 COMMENT The complex of six MCM proteins is one of several proteins !1that must be bound at the origins of replication for the !1initiation of DNA replication. As replication proceeds, MCM !1proteins are phosphorylated and dissociate from the !1chromatin. GENETICS !$#gene SGD:CDC54; HCD21; MIPS:YPR019w !'##cross-references SGD:S0006223; MIPS:YPR019w !$#map_position 16R COMPLEX The predominant form is a heterohexamer of MCM2 !1(PIR:S45757), MCM3 (PIR:A36376), MCM4 (PIR:S56050), MCM5 !1(PIR:A39631), MCM6 (PIR:S64219), and MCM7 (PIR:S34027); !1sometimes called the RLF-M component of replication !1licensing factor. FUNCTION !$#description MCM4 is a component of the replication licensing factor that !1permits DNA replication to occur once and only once within a !1single cell division cycle [validated, MUID:98001511] CLASSIFICATION #superfamily replication licensing factor MCM4; MCM homology KEYWORDS cell cycle control; DNA replication initiation; !1heterohexamer; nucleus; phosphoprotein; zinc finger FEATURE !$314-828 #domain MCM homology #label MCM SUMMARY #length 933 #molecular-weight 105002 #checksum 809 SEQUENCE /// ENTRY S26640 #type complete TITLE replication licensing factor MCM4 - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES cell division cycle control protein CDC21/CDC54 ORGANISM #formal_name Schizosaccharomyces pombe DATE 13-Aug-1999 #sequence_revision 13-Aug-1999 #text_change 03-Nov-2000 ACCESSIONS S26640; T41090; S21829 REFERENCE S26640 !$#authors Coxon, A.; Maundrell, K.; Kearsey, S.E. !$#journal Nucleic Acids Res. (1992) 20:5571-5577 !$#title Fission yeast cdc21(+) belongs to a family of proteins !1involved in an early step of chromosome replication. !$#cross-references MUID:93087163; PMID:1454522 !$#accession S26640 !'##molecule_type DNA !'##residues 1-909 ##label COX !'##cross-references EMBL:X58824; NID:g4926; PID:g4927 REFERENCE Z21822 !$#authors McDougall, R.C.; Rajandream, M.A.; Barrell, B.G.; !1Zimmermann, W.; Wambutt, R. !$#submission submitted to the EMBL Data Library, August 1999 !$#accession T41090 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-546 ##label MCD !'##cross-references EMBL:AL109957; PIDN:CAB53089.1; GSPDB:GN00068; !1SPDB:SPCC16A11.17 !'##experimental_source strain 972h(-); cosmid c16A11 COMMENT The complex of six MCM proteins is one of several proteins !1that must be bound at the origins of replication for the !1initiation of DNA replication. As replication proceeds, MCM !1proteins are phosphorylated and dissociate from the !1chromatin. GENETICS !$#gene cdc21; SPDB:SPCC16A11.17 !$#map_position 3 COMPLEX predominant form is a heterohexamer of MCM2, MCM3, MCM4, !1MCM5, MCM6, and MCM7, sometimes called the RLF-M component !1of replication licensing factor FUNCTION !$#description part of the replication licensing system that permits DNA !1replication to occur once and only once within a single cell !1division cycle CLASSIFICATION #superfamily replication licensing factor MCM4; MCM homology KEYWORDS cell cycle control; DNA replication initiation; !1heterohexamer; nucleus; phosphoprotein; zinc finger FEATURE !$291-805 #domain MCM homology #label MCM SUMMARY #length 909 #molecular-weight 101388 #checksum 9334 SEQUENCE /// ENTRY I38080 #type complete TITLE replication licensing factor MCM5 - human ALTERNATE_NAMES cell division control protein CDC46; minichromosome maintenance protein MCM5 homolog ORGANISM #formal_name Homo sapiens #common_name man DATE 13-Aug-1999 #sequence_revision 13-Aug-1999 #text_change 20-Apr-2001 ACCESSIONS I38080; S43199; S41623 REFERENCE I38080 !$#authors Hu, B.; Burkhart, R.; Schulte, D.; Musahl, C.; Knippers, R. !$#journal Nucleic Acids Res. (1993) 21:5289-5293 !$#title The P1 family: a new class of nuclear mammalian proteins !1related to the yeast Mcm replication proteins. !$#cross-references MUID:94089373; PMID:8265339 !$#accession I38080 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-734 ##label RES !'##cross-references EMBL:X74795; NID:g895842; PIDN:CAA52802.1; !1PID:g895843 REFERENCE S43198 !$#authors Hu, B. !$#submission submitted to the EMBL Data Library, August 1993 !$#accession S43199 !'##molecule_type mRNA !'##residues 'AR',352-590 ##label HUB1 !'##cross-references EMBL:X74795 COMMENT The complex of six MCM proteins is one of several proteins !1that must be bound at the origins of replication for the !1initiation of DNA replication. As replication proceeds, MCM !1proteins are phosphorylated and dissociate from the !1chromatin. GENETICS !$#gene GDB:MCM5; CDC46 !'##cross-references GDB:433799 !$#map_position 22q13.1-22q13.2 COMPLEX The predominant form is a heterohexamer of MCM2, MCM3, MCM4, !1MCM5, MCM6, and MCM7, sometimes called the RLF-M component !1of replication licensing factor. FUNCTION !$#description part of the replication licensing system that permits DNA !1replication to occur once and only once within a single cell !1division cycle CLASSIFICATION #superfamily replication licensing factor MCM5; MCM homology KEYWORDS cell cycle control; DNA replication initiation; nucleus FEATURE !$137-643 #domain MCM homology #label MCM SUMMARY #length 734 #molecular-weight 82244 #checksum 3875 SEQUENCE /// ENTRY S56767 #type complete TITLE replication licensing factor MCM5 - mouse ALTERNATE_NAMES cell division control protein CDC46; minichromosome maintenance protein MCM5 homolog ORGANISM #formal_name Mus musculus #common_name house mouse DATE 13-Aug-1999 #sequence_revision 13-Aug-1999 #text_change 16-Jun-2000 ACCESSIONS S56767 REFERENCE S56766 !$#authors Kimura, H.; Takizawa, N.; Nozaki, N.; Sugimoto, K. !$#journal Nucleic Acids Res. (1995) 23:2097-2104 !$#title Molecular cloning of cDNA encoding mouse Cdc21 and CDC46 !1homologs and characterization of the products: physical !1interaction between P1(MCM3) and CDC46 proteins. !$#cross-references MUID:95334361; PMID:7610039 !$#accession S56767 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type mRNA !'##residues 1-733 ##label KIM !'##cross-references EMBL:D26090; NID:g940403; PIDN:BAA05083.1; !1PID:g940404 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1993 COMMENT The complex of six MCM proteins is one of several proteins !1that must be bound at the origins of replication for the !1initiation of DNA replication. As replication proceeds, MCM !1proteins are phosphorylated and dissociate from the !1chromatin. COMPLEX The predominant form is a heterohexamer of MCM2, MCM3, MCM4, !1MCM5, MCM6, and MCM7, sometimes called the RLF-M component !1of replication licensing factor. FUNCTION !$#description part of the replication licensing system that permits DNA !1replication to occur once and only once within a single cell !1division cycle CLASSIFICATION #superfamily replication licensing factor MCM5; MCM homology KEYWORDS cell cycle control; DNA replication initiation; nucleus FEATURE !$137-642 #domain MCM homology #label MCM SUMMARY #length 733 #molecular-weight 82342 #checksum 6080 SEQUENCE /// ENTRY PC4225 #type complete TITLE replication licensing factor MCM5 [validated] - African clawed frog ALTERNATE_NAMES cell division control protein CDC46; MCM5/CDC46p; minichromosome maintenance protein MCM5 homolog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 13-Aug-1999 #sequence_revision 18-Aug-2000 #text_change 18-Aug-2000 ACCESSIONS T47224; PC4225 REFERENCE Z24400 !$#authors Kubota, Y.; Mimura, S.; Nishimoto, S.; Masuda, T.; Nojima, !1H.; Takisawa, H. !$#journal EMBO J. (1997) 16:3320-3331 !$#title Licensing of DNA replication by a multi-protein complex of !1MCM/P1 proteins in Xenopus eggs. !$#cross-references MUID:97357318; PMID:9214647 !$#accession T47224 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-735 ##label KUB !'##cross-references EMBL:U44048; NID:g2231170; PIDN:AAC60224.1; !1PID:g2231171 REFERENCE JC5085 !$#authors Miyake, S.; Saito, I.; Kobayashi, H.; Yamashita, S. !$#journal Gene (1996) 175:71-75 !$#title Identification of two Xenopus laevis genes, xMCM2 and !1xCDC46, with sequence homology to MCM genes involved in DNA !1replication. !$#cross-references MUID:97074651; PMID:8917078 !$#contents oocyte !$#accession PC4225 !'##molecule_type mRNA !'##residues 20-735 ##label MIY !'##cross-references DDBJ:D63920; NID:g1753194; PIDN:BAA09949.1; !1PID:g1753195 COMMENT The complex of six MCM proteins is one of several proteins !1that must be bound at the origins of replication for the !1initiation of DNA replication. As replication proceeds, MCM !1proteins are phosphorylated and dissociate from the !1chromatin. GENETICS !$#gene MCM5 COMPLEX the replication licensing complex consists of at least six !1proteins; MCM2 (PIR:T47225), MCM3 (PIR:T47226), MCM4 !1(PIR:T47223), MCM5 (PIR:T47224), MCM6 (PIR:T47222), and MCM7 !1(PIR:T47221) [validated, MUID:97357318] FUNCTION !$#description MCM5 is a component of the replication licensing factor that !1permits DNA replication to occur once and only once within a !1single cell division cycle [validated, MUID:97357318] CLASSIFICATION #superfamily replication licensing factor MCM5; MCM homology KEYWORDS cell cycle control; DNA replication initiation; nucleus FEATURE !$138-644 #domain MCM homology #label MCM SUMMARY #length 735 #molecular-weight 82435 #checksum 9547 SEQUENCE /// ENTRY A39631 #type complete TITLE replication licensing factor MCM5 [validated] - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES cell division control protein CDC46; minichromosome maintenance protein MCM5; protein L9328.1; protein YLR274w ORGANISM #formal_name Saccharomyces cerevisiae DATE 13-Aug-1999 #sequence_revision 13-Aug-1999 #text_change 21-Jul-2000 ACCESSIONS A39631; S51410 REFERENCE A39631 !$#authors Hennessy, K.M.; Lee, A.; Chen, E.; Botstein, D. !$#journal Genes Dev. (1991) 5:958-969 !$#title A group of interacting yeast DNA replication genes. !$#cross-references MUID:91257582; PMID:2044962 !$#accession A39631 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-775 ##label HEN !'##cross-references GB:U09242; NID:g485272; PIDN:AAA18027.1; !1PID:g485273 REFERENCE S51409 !$#authors Miller, N. !$#submission submitted to the EMBL Data Library, November 1994 !$#description The sequence of S. cerevisiae cosmid 9328. !$#accession S51410 !'##molecule_type DNA !'##residues 1-775 ##label MIL !'##cross-references EMBL:U17245; NID:g577186; PIDN:AAB67364.1; !1PID:g577187; GSPDB:GN00012; MIPS:YLR274w COMMENT The complex of six MCM proteins is one of several proteins !1that must be bound at the origins of replication for the !1initiation of DNA replication. As replication proceeds, MCM !1proteins are phosphorylated and dissociate from the !1chromatin. GENETICS !$#gene SGD:CDC46; MCM1; MIPS:YLR274w !'##cross-references SGD:S0004264; MIPS:YLR274w !$#map_position 12R COMPLEX The predominant form is a heterohexamer of MCM2 !1(PIR:S45757), MCM3 (PIR:A36376), MCM4 (PIR:S56050), MCM5 !1(PIR:A39631), MCM6 (PIR:S64219), and MCM7 (PIR:S34027); !1sometimes called the RLF-M component of replication !1licensing factor. FUNCTION !$#description MCM5 is a component of the replication licensing factor that !1permits DNA replication to occur once and only once within a !1single cell division cycle [validated, MUID:98001511] CLASSIFICATION #superfamily replication licensing factor MCM5; MCM homology KEYWORDS cell cycle control; DNA replication initiation; nucleus FEATURE !$148-683 #domain MCM homology #label MCM SUMMARY #length 775 #molecular-weight 86410 #checksum 5474 SEQUENCE /// ENTRY A48723 #type complete TITLE replication licensing factor MCM5 - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES cell division control protein CDC46; cell division control protein nda4; minichromosome maintenance protein MCM5 homolog ORGANISM #formal_name Schizosaccharomyces pombe DATE 13-Aug-1999 #sequence_revision 13-Aug-1999 #text_change 18-Aug-2000 ACCESSIONS A48723; T38702 REFERENCE A48723 !$#authors Miyake, S.; Okishio, N.; Samejima, I.; Hiraoka, Y.; Toda, !1T.; Saitoh, I.; Yanagida, M. !$#journal Mol. Biol. Cell (1993) 4:1003-1015 !$#title Fission yeast genes nda1(+) and nda4(+), mutations of which !1lead to S-phase block, chromatin alteration and Ca(2+) !1suppression, are members of the CDC46/MCM2 family. !$#cross-references MUID:94129084; PMID:8298187 !$#accession A48723 !'##molecule_type DNA !'##residues 1-720 ##label MIY !'##cross-references GB:S68467; NID:g545210; PIDN:AAC60568.1; !1PID:g545211 REFERENCE Z21807 !$#authors Murphy, L.; Harris, D.; Barrell, B.G.; Rajandream, M.A.; !1Walsh, S.V. !$#submission submitted to the EMBL Data Library, February 1996 !$#accession T38702 !'##molecule_type DNA !'##residues 72-460,'A',462-584,'R',586-699,'L',701-720 ##label MUR !'##cross-references EMBL:Z69369; PIDN:CAA93299.1; GSPDB:GN00066; !1SPDB:SPAC3F10.01 COMMENT The complex of six MCM proteins is one of several proteins !1that must be bound at the origins of replication for the !1initiation of DNA replication. As replication proceeds, MCM !1proteins are phosphorylated and dissociate from the !1chromatin. GENETICS !$#gene nda4+ COMPLEX The predominant form is a heterohexamer of MCM2, MCM3, MCM4, !1MCM5, MCM6, and MCM7, sometimes called the RLF-M component !1of replication licensing factor. FUNCTION !$#description part of the replication licensing system that permits DNA !1replication to occur once and only once within a single cell !1division cycle CLASSIFICATION #superfamily replication licensing factor MCM5; MCM homology KEYWORDS cell cycle control; DNA replication initiation; nucleus FEATURE !$132-636 #domain MCM homology #label MCM SUMMARY #length 720 #molecular-weight 80184 #checksum 1029 SEQUENCE /// ENTRY S64219 #type complete TITLE replication licensing factor MCM6 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein G1256; hypothetical protein YGL201c; minichromosome maintenance protein MCM6 ORGANISM #formal_name Saccharomyces cerevisiae DATE 13-Aug-1999 #sequence_revision 13-Aug-1999 #text_change 21-Jul-2000 ACCESSIONS S64219 REFERENCE S64218 !$#authors Bjourson, A.J.; McReynolds, A.D.K.; Wright, L.F. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64219 !'##molecule_type DNA !'##residues 1-1017 ##label BJO !'##cross-references EMBL:Z72723; NID:g1322831; PIDN:CAA96913.1; !1PID:g1322832; GSPDB:GN00007; MIPS:YGL201c !'##experimental_source strain S288C GENETICS !$#gene SGD:MCM6; MIPS:YGL201c !'##cross-references SGD:S0003169; MIPS:YGL201c !$#map_position 7L CLASSIFICATION #superfamily yeast replication licensing factor MCM6; MCM !1homology KEYWORDS cell cycle control; DNA replication; nucleus FEATURE !$276-830 #domain MCM homology #label MCM SUMMARY #length 1017 #molecular-weight 112951 #checksum 8085 SEQUENCE /// ENTRY S70583 #type complete TITLE replication licensing factor MCM7 - human ALTERNATE_NAMES cell division control protein CDC47 ORGANISM #formal_name Homo sapiens #common_name man DATE 13-Aug-1999 #sequence_revision 13-Aug-1999 #text_change 16-Jun-2000 ACCESSIONS S70583; S62607; S43200; S41624 REFERENCE S70583 !$#authors Kiyono, T.; Fujita, M.; Hayashi, Y.; Ishibashi, M. !$#journal Biochim. Biophys. Acta (1996) 1307:31-34 !$#title Cloning of a cDNA encoding a human homologue of CDC47, a !1member of the MCM family. !$#cross-references MUID:96254060; PMID:8652665 !$#accession S70583 !'##molecule_type mRNA !'##residues 1-719 ##label KIY !'##cross-references EMBL:D55716; NID:g1255616; PIDN:BAA09534.1; !1PID:g1255617 REFERENCE S62607 !$#authors Schulte, D.; Richter, A.; Burkhart, R.; Musahl, C.; !1Knippers, R. !$#journal Eur. J. Biochem. (1996) 235:144-151 !$#title Properties of the human nuclear protein p85Mcm. Expression, !1nuclear localization and interaction with other Mcm !1proteins. !$#cross-references MUID:96202928; PMID:8631321 !$#accession S62607 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type mRNA !'##residues 'L',104-143,'N',145-719 ##label SCH !'##cross-references EMBL:X74796; NID:g683751; PIDN:CAA52803.1; !1PID:g755746 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1993 REFERENCE S43198 !$#authors Hu, B. !$#submission submitted to the EMBL Data Library, August 1993 !$#accession S43200 !'##molecule_type mRNA !'##residues 261-557 ##label HUB1 !'##cross-references EMBL:X74796 REFERENCE S41622 !$#authors Hu, B.; Burkhart, R.; Schulte, D.; Musahl, C.; Knippers, R. !$#journal Nucleic Acids Res. (1993) 21:5289-5293 !$#title The P1 family: a new class of nuclear mammalian proteins !1related to the yeast Mcm replication proteins. !$#cross-references MUID:94089373; PMID:8265339 !$#accession S41624 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 311-507 ##label HUB2 !'##cross-references EMBL:X74796 COMMENT The complex of six MCM proteins is one of several proteins !1that must be bound at the origins of replication for the !1initiation of DNA replication. As replication proceeds, MCM !1proteins are phosphorylated and dissociate from the !1chromatin. GENETICS !$#gene GDB:MCM7; MCM2; CDC47 !'##cross-references GDB:433796; OMIM:600592 !$#map_position 7q21.3-7q22.1 COMPLEX The predominant form is a heterohexamer of MCM2, MCM3, MCM4, !1MCM5, MCM6, and MCM7, sometimes called the RLF-M component !1of replication licensing factor. FUNCTION !$#description part of the replication licensing system that permits DNA !1replication to occur once and only once within a single cell !1division cycle CLASSIFICATION #superfamily replication licensing factor MCM7; MCM homology KEYWORDS cell cycle control; DNA replication initiation; !1heterohexamer; nucleus; phosphoprotein; zinc finger FEATURE !$149-636 #domain MCM homology #label MCM SUMMARY #length 719 #molecular-weight 81280 #checksum 4414 SEQUENCE /// ENTRY JC4580 #type complete TITLE replication licensing factor MCM7 - mouse ALTERNATE_NAMES cell division control protein CDC47 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 13-Aug-1999 #sequence_revision 13-Aug-1999 #text_change 16-Jun-2000 ACCESSIONS JC4580 REFERENCE JC4580 !$#authors Takizawa, N.; Kimura, H.; Sugimoto, K. !$#journal Gene (1995) 167:343-344 !$#title Sequence of mouse CDC47, a member of the minichromosome !1maintenance (Mcm) family involved in the DNA replication !1licensing system. !$#cross-references MUID:96144303; PMID:8566808 !$#accession JC4580 !'##molecule_type mRNA !'##residues 1-719 ##label TAK !'##cross-references DDBJ:D26091; NID:g1136746; PIDN:BAA05084.1; !1PID:g1136747 COMMENT The complex of six MCM proteins is one of several proteins !1that must be bound at the origins of replication for the !1initiation of DNA replication. As replication proceeds, MCM !1proteins are phosphorylated and dissociate from the !1chromatin. GENETICS !$#gene cdc47 COMPLEX The predominant form is a heterohexamer of MCM2, MCM3, MCM4, !1MCM5, MCM6, and MCM7, sometimes called the RLF-M component !1of replication licensing factor. FUNCTION !$#description part of the replication licensing system that permits DNA !1replication to occur once and only once within a single cell !1division cycle CLASSIFICATION #superfamily replication licensing factor MCM7; MCM homology KEYWORDS cell cycle control; DNA replication initiation; !1heterohexamer; nucleus; phosphoprotein; zinc finger FEATURE !$149-636 #domain MCM homology #label MCM SUMMARY #length 719 #molecular-weight 81210 #checksum 3401 SEQUENCE /// ENTRY T03920 #type complete TITLE replication licensing factor MCM7 - Caenorhabditis elegans ALTERNATE_NAMES cell division control protein CDC47 ORGANISM #formal_name Caenorhabditis elegans DATE 13-Aug-1999 #sequence_revision 13-Aug-1999 #text_change 10-Sep-1999 ACCESSIONS T03920 REFERENCE Z15134 !$#authors Becker, M.; Bradshaw, H.; Kramer, J. !$#submission submitted to the EMBL Data Library, July 1997 !$#description The sequence of C. elegans cosmid F32D1. !$#accession T03920 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-730 ##label BEC !'##cross-references EMBL:AF016427; NID:g2291228; PIDN:AAB65356.1; !1PID:g2291237 COMMENT The complex of six MCM proteins is one of several proteins !1that must be bound at the origins of replication for the !1initiation of DNA replication. As replication proceeds, MCM !1proteins are phosphorylated and dissociate from the !1chromatin. GENETICS !$#map_position V !$#introns 34/3; 313/3; 663/2 !$#note F32D1.10 COMPLEX The predominant form is a heterohexamer of MCM2, MCM3, MCM4, !1MCM5, MCM6, and MCM7, sometimes called the RLF-M component !1of replication licensing factor. FUNCTION !$#description part of the replication licensing system that permits DNA !1replication to occur once and only once within a single cell !1division cycle CLASSIFICATION #superfamily replication licensing factor MCM7; MCM homology KEYWORDS cell cycle control; DNA replication initiation; !1heterohexamer; nucleus; phosphoprotein; zinc finger FEATURE !$162-646 #domain MCM homology #label MCM SUMMARY #length 730 #molecular-weight 81617 #checksum 6831 SEQUENCE /// ENTRY T01507 #type complete TITLE replication licensing factor MCM7 - Arabidopsis thaliana ALTERNATE_NAMES cell division control protein CDC47 ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 13-Aug-1999 #sequence_revision 13-Aug-1999 #text_change 21-Jan-2000 ACCESSIONS T01507 REFERENCE Z14346 !$#authors Johnson, A.F.; de la Bastide, M.; Lodhi, M.; Hoffman, J.; !1Hasegawa, A.; Gnoj, L.; Gottesman, T.; Granat, S.; Hameed, !1A.; Kaplan, N.; Schutz, K.; Shohdy, N.; van Keuren, K.; !1Parnell, L.; Dedhia, N.; Martienssen, R.; McCombie, W. !$#submission submitted to the EMBL Data Library, May 1997 !$#description The sequence of the Arabidopsis thaliana T10M13 BAC. !$#accession T01507 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-716 ##label JOH !'##cross-references EMBL:AF001308; NID:g2104523; PIDN:AAC78698.1; !1PID:g2104530 !'##experimental_source cultivar Columbia COMMENT The complex of six MCM proteins is one of several proteins !1that must be bound at the origins of replication for the !1initiation of DNA replication. As replication proceeds, MCM !1proteins are phosphorylated and dissociate from the !1chromatin. GENETICS !$#map_position 4S !$#introns 11/1; 33/3; 53/3; 128/2; 187/3; 228/3; 258/3; 306/2; 365/3; !1429/3; 487/2; 555/2; 610/3; 684/3 !$#note T10M13.7 COMPLEX The predominant form is a heterohexamer of MCM2, MCM3, MCM4, !1MCM5, MCM6, and MCM7, sometimes called the RLF-M component !1of replication licensing factor. FUNCTION !$#description part of the replication licensing system that permits DNA !1replication to occur once and only once within a single cell !1division cycle CLASSIFICATION #superfamily replication licensing factor MCM7; MCM homology KEYWORDS cell cycle control; DNA replication initiation; !1heterohexamer; nucleus; phosphoprotein; zinc finger FEATURE !$143-632 #domain MCM homology #label MCM SUMMARY #length 716 #molecular-weight 80332 #checksum 4717 SEQUENCE /// ENTRY S34027 #type complete TITLE replication licensing factor MCM7 [validated] - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES cell division control protein CDC47; protein YBR1441; protein YBR202w ORGANISM #formal_name Saccharomyces cerevisiae DATE 13-Aug-1999 #sequence_revision 13-Aug-1999 #text_change 21-Jul-2000 ACCESSIONS S34027; S46074; S34925; S56049 REFERENCE S34022 !$#authors Jacquet, M. !$#submission submitted to the EMBL Data Library, January 1993 !$#accession S34027 !'##molecule_type DNA !'##residues 1-845 ##label JAC !'##cross-references EMBL:Z21487; NID:g311665; PIDN:CAA79689.1; !1PID:g311678 REFERENCE S46054 !$#authors Bussereau, F.; Demolis, N.; Jacquet, M.; Mallet, L. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S46074 !'##molecule_type DNA !'##residues 1-845 ##label BUS !'##cross-references EMBL:Z36071; NID:g536576; PIDN:CAA85166.1; !1PID:g536577; GSPDB:GN00002; MIPS:YBR202w REFERENCE S34925 !$#authors Bussereau, F.; Mallet, L.; Gaillon, L.; Jacquet, M. !$#journal Yeast (1993) 9:797-806 !$#title Yeast Sequencing Reports. A 12.8 kb segment, on the right !1arm of chromosome II from Saccharomyces cerevisiae including !1part of the DUR1,2 gene, contains five putative new genes. !$#cross-references MUID:93377417; PMID:8368014 !$#accession S34925 !'##molecule_type DNA !'##residues 407-620 ##label BU2 !'##cross-references EMBL:Z21487 REFERENCE S56049 !$#authors Dalton, S. !$#submission submitted to the EMBL Data Library, September 1994 !$#description Cdc47 and Cdc54 belong to a family of proteins essential for !1initiation of eukaryotic DNA replication. !$#accession S56049 !'##molecule_type DNA !'##residues 1-551,'G',553-555,'TLN',559-573,'Y',575-845 ##label DAL !'##cross-references EMBL:U14730; NID:g608168; PIDN:AAA86309.1; !1PID:g608169 COMMENT The complex of six MCM proteins is one of several proteins !1that must be bound at the origins of replication for the !1initiation of DNA replication. As replication proceeds, MCM !1proteins are phosphorylated and dissociate from the !1chromatin. GENETICS !$#gene SGD:CDC47; MIPS:YBR202w !'##cross-references SGD:S0000406; MIPS:YBR202w !$#map_position 2R COMPLEX The predominant form is a heterohexamer of MCM2 !1(PIR:S45757), MCM3 (PIR:A36376), MCM4 (PIR:S56050), MCM5 !1(PIR:A39631), MCM6 (PIR:S64219), and MCM7 (PIR:S34027); !1sometimes called the RLF-M component of replication !1licensing factor. FUNCTION !$#description MCM7 is a component of the replication licensing factor that !1permits DNA replication to occur once and only once within a !1single cell division cycle [validated, MUID:98001511] CLASSIFICATION #superfamily replication licensing factor MCM7; MCM homology KEYWORDS cell cycle control; DNA replication initiation; !1heterohexamer; nucleus; phosphoprotein; zinc finger FEATURE !$227-719 #domain MCM homology #label MCM SUMMARY #length 845 #molecular-weight 94874 #checksum 3856 SEQUENCE /// ENTRY E69314 #type complete TITLE replication licensing factor MCM-type homolog AF0517 - Archaeoglobus fulgidus ALTERNATE_NAMES cell division cycle control protein CDC21/CDC54 homolog ORGANISM #formal_name Archaeoglobus fulgidus DATE 13-Aug-1999 #sequence_revision 13-Aug-1999 #text_change 20-Aug-1999 ACCESSIONS E69314 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession E69314 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-586 ##label KLE !'##cross-references GB:AE001068; GB:AE000782; NID:g2689391; !1PIDN:AAB90715.1; PID:g2650102; TIGR:AF0517 CLASSIFICATION #superfamily Archaeoglobus replication licensing factor !1MCM-type homolog; MCM homology KEYWORDS cell cycle control; DNA replication initiation FEATURE !$1-488 #domain MCM homology #status atypical #label MCM SUMMARY #length 586 #molecular-weight 65975 #checksum 8757 SEQUENCE /// ENTRY D69103 #type complete TITLE DNA helicase (EC 3.6.1.-) MTH1770 [validated] - Methanobacterium thermoautotrophicum (strain Delta H) ALTERNATE_NAMES cell division control protein CDC21/CDC54 homolog; replication licensing factor MCM-type homolog MTH1770 CONTAINS adenosinetriphosphatase (EC 3.6.1.3) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 13-Aug-1999 #sequence_revision 13-Aug-1999 #text_change 26-May-2000 ACCESSIONS D69103 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession D69103 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-666 ##label MTH !'##cross-references GB:AE000932; GB:AE000666; NID:g2622894; !1PIDN:AAB86236.1; PID:g2622900 !'##experimental_source strain Delta H GENETICS !$#gene MTH1770 COMPLEX dodecamer; double hexamer [validated, MUID:20144074] FUNCTION HEL !$#description EC 3.6.1.-; DNA helicase; ATP-dependent DNA unwinding !1activity [validated, MUID:20144074] FUNCTION ATP !$#description EC 3.6.1.3 [validated, MUID:20144074]; !1adenosinetriphosphatase, DNA-dependent FUNCTION DNA !$#description ATP-independent single-stranded DNA-binding; ATP-dependent !1double-stranded DNA-binding [validated, MUID:20144074] CLASSIFICATION #superfamily Archaeoglobus replication licensing factor !1MCM-type homolog; MCM homology KEYWORDS cell cycle control; DNA replication initiation; hydrolase FEATURE !$98-570 #domain MCM homology #label MCM SUMMARY #length 666 #molecular-weight 75552 #checksum 2215 SEQUENCE /// ENTRY H64485 #type complete TITLE replication licensing factor MCM-type homolog MJ1489 - Methanococcus jannaschii ALTERNATE_NAMES cell division cycle control protein CDC21/CDC54 homolog ORGANISM #formal_name Methanococcus jannaschii DATE 20-Aug-1999 #sequence_revision 20-Aug-1999 #text_change 21-Jul-2000 ACCESSIONS H64485 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession H64485 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-682 ##label BUL !'##cross-references GB:U67590; GB:L77117; NID:g1592126; !1PIDN:AAB99502.1; PID:g1592127; TIGR:MJ1489 GENETICS !$#map_position FOR1461597-1463645 !$#start_codon TTG CLASSIFICATION #superfamily Methanococcus replication licensing factor !1MCM-type homolog MJ1489; MCM homology KEYWORDS cell cycle control; DNA replication initiation FEATURE !$116-589 #domain MCM homology #label MCM SUMMARY #length 682 #molecular-weight 77706 #checksum 1883 SEQUENCE /// ENTRY C64345 #type complete TITLE replication licensing factor MCM-type homolog MJ0363 - Methanococcus jannaschii ALTERNATE_NAMES cell division cycle control protein CDC21/CDC54 homolog ORGANISM #formal_name Methanococcus jannaschii DATE 20-Aug-1999 #sequence_revision 20-Aug-1999 #text_change 21-Jul-2000 ACCESSIONS C64345 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession C64345 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-759 ##label BUL !'##cross-references GB:U67489; GB:L77117; NID:g1591063; !1PIDN:AAB98345.1; PID:g1591071; TIGR:MJ0363 GENETICS !$#map_position FOR329865-332144 CLASSIFICATION #superfamily Methanococcus replication licensing factor !1MCM-type homolog MJ0363; MCM homology KEYWORDS cell cycle control; DNA replication initiation FEATURE !$174-663 #domain MCM homology #label MCM SUMMARY #length 759 #molecular-weight 86166 #checksum 7216 SEQUENCE /// ENTRY A64420 #type complete TITLE replication licensing factor MCM-type homolog MJ0961 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 20-Aug-1999 #sequence_revision 20-Aug-1999 #text_change 21-Jul-2000 ACCESSIONS A64420 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession A64420 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-762 ##label BUL !'##cross-references GB:U67539; GB:L77117; NID:g1591619; !1PIDN:AAB98963.1; PID:g1591625; TIGR:MJ0961 GENETICS !$#map_position FOR892654-894942 CLASSIFICATION #superfamily Methanococcus replication licensing factor !1MCM-type homolog MJ0363; MCM homology KEYWORDS cell cycle control; DNA replication initiation FEATURE !$102-667 #domain MCM homology #label MCM SUMMARY #length 762 #molecular-weight 87525 #checksum 9447 SEQUENCE /// ENTRY E64511 #type complete TITLE replication licensing factor MCM-type homolog MJECL13 - Methanococcus jannaschii plasmid pURB800 ORGANISM #formal_name Methanococcus jannaschii DATE 26-Aug-1999 #sequence_revision 26-Aug-1999 #text_change 21-Jul-2000 ACCESSIONS E64511 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession E64511 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-602 ##label BUL !'##cross-references GB:L77118; NID:g1500644; TIGR:MJECL13; !1PIDN:AAC37086.1; PID:g1522653 GENETICS !$#map_position ECLFOR10678-12486 !$#genome plasmid !$#start_codon GTG !$#note this stable 58-kilobase pair plasmid is also designated ECL !1(large extrachromosomal element) and contains 44 predicted !1coding regions CLASSIFICATION #superfamily replication licensing factor MCM-type homolog !1MJECL13; MCM homology KEYWORDS cell cycle control; DNA replication initiation FEATURE !$105-575 #domain MCM homology #label MCM SUMMARY #length 602 #molecular-weight 69322 #checksum 2919 SEQUENCE /// ENTRY COZPCD #type complete TITLE cdc10 start control protein - fission yeast (Schizosaccharomyces pombe) ORGANISM #formal_name Schizosaccharomyces pombe DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 10-Dec-1999 ACCESSIONS A01382; T40250 REFERENCE A01382 !$#authors Aves, S.J.; Durkacz, B.W.; Carr, A.; Nurse, P. !$#journal EMBO J. (1985) 4:457-463 !$#title Cloning, sequencing and transcriptional control of the !1Schizosaccharomyces pombe cdc 10 'start' gene. !$#cross-references MUID:85257476; PMID:4018034 !$#accession A01382 !'##molecule_type DNA !'##residues 1-767 ##label AVE !'##cross-references GB:X02175; NID:g4920; PIDN:CAA26116.1; PID:g4921 REFERENCE Z21916 !$#authors Borzym, K.; Beck, A.; Reinhardt, R.; McDougall, R.C.; !1Rajandream, M.A.; Barrell, B.G. !$#submission submitted to the EMBL Data Library, October 1999 !$#accession T40250 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-767 ##label BOR !'##cross-references EMBL:AL121815; PIDN:CAB58164.1; GSPDB:GN00067; !1SPDB:SPBC336.12c !'##experimental_source strain 972h-; cosmid c336 COMMENT In fission yeast, two genes, cdc10 and cdc2, are required !1for the cell cycle control called start, the point early in !1the G1 phase at which cells become committed to the mitotic !1cycle. GENETICS !$#gene SPBC336.12c !$#map_position 2 CLASSIFICATION #superfamily cdc10 start control protein; ankyrin repeat !1homology KEYWORDS cell cycle control; mitosis FEATURE !$356-388 #domain ankyrin repeat homology #label AN1\ !$483-515 #domain ankyrin repeat homology #label AN2 SUMMARY #length 767 #molecular-weight 85512 #checksum 4206 SEQUENCE /// ENTRY RGBY43 #type complete TITLE cell division control protein CDC43 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES CAL1 protein; DPR1 protein; protein G1864; protein YGL155w ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1991 #sequence_revision 12-Apr-1996 #text_change 21-Jul-2000 ACCESSIONS A40875; S11186; S60429; S64171; JU0326 REFERENCE A40875 !$#authors Ohya, Y.; Goebl, M.; Goodman, L.E.; Petersen-Bjorn, S.; !1Friesen, J.D.; Tamanoi, F.; Anraku, Y. !$#journal J. Biol. Chem. (1991) 266:12356-12360 !$#title Yeast CAL1 is a structural and functional homologue to the !1DPR1 (RAM) gene involved in ras processing. !$#cross-references MUID:91286255; PMID:2061313 !$#accession A40875 !'##molecule_type DNA !'##residues 1-376 ##label OHY !'##cross-references GB:M74109; GB:M29471; NID:g171146; PIDN:AAA34464.1; !1PID:g171147 REFERENCE JU0326 !$#authors Johnson, D.I.; O'Brien, J.M.; Jacobs, C.W. !$#journal Gene (1990) 90:93-98 !$#title Isolation and sequence analysis of CDC43, a gene involved in !1the control of cell polarity in Saccharomyces cerevisiae. !$#cross-references MUID:90337353; PMID:2199333 !$#accession S11186 !'##molecule_type DNA !'##residues 1-212,'Q' ##label JOH !'##cross-references EMBL:M31114 REFERENCE S60417 !$#authors James, C.M.; Indge, K.J.; Oliver, S.G. !$#journal Yeast (1995) 11:1413-1419 !$#title DNA sequence analysis of a 35 kb segment from Saccharomyces !1cerevisiae chromosome VII reveals 19 open reading frames !1including RAD54, ACE1/CUP2, PMR1, RCK1, AMS1 and CAL1/CDC43. !$#cross-references MUID:96158061; PMID:8585324 !$#accession S60429 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-376 ##label JAM !'##cross-references EMBL:Z48618 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1March 1995 REFERENCE S64165 !$#authors James, C.M.; Indge, K.J.; Oliver, S.G. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64171 !'##molecule_type DNA !'##residues 1-376 ##label JAW !'##cross-references EMBL:Z72677; NID:g1322743; PIDN:CAA96867.1; !1PID:g1322744; GSPDB:GN00007; MIPS:YGL155w !'##experimental_source strain S288C GENETICS !$#gene SGD:CDC43; CAL1; MIPS:YGL155w !'##cross-references SGD:S0003123; MIPS:YGL155w !$#map_position 7L FUNCTION !$#description involved in cell polarity control CLASSIFICATION #superfamily cell division control protein CDC43 KEYWORDS cell cycle control SUMMARY #length 376 #molecular-weight 42689 #checksum 7999 SEQUENCE /// ENTRY RGBYC6 #type complete TITLE cell division control protein CDC6 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein J0347; protein YJL194w ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1991 #sequence_revision 10-Feb-1995 #text_change 12-Nov-1999 ACCESSIONS S46640; S28236; S05737; S11954; S20156; S37746; S56981; !1A33711 REFERENCE S46621 !$#authors Purnelle, B.; Coster, F.; Goffeau, A. !$#journal Yeast (1994) 10:1235-1249 !$#title The sequence of a 36 kb segment on the left arm of yeast !1chromosome X identifies 24 open reading frames including !1NUC1, PRP21 (SPP91), CDC6, CRY2, the gene for S24, a !1homologue to the aconitase gene ACO1 and two homologues to !1chromosome III genes. !$#cross-references MUID:95274326; PMID:7754713 !$#accession S46640 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-513 ##label PUR !'##cross-references EMBL:X77688; NID:g1183992; PIDN:CAA54766.1; !1PID:g547601 REFERENCE S28236 !$#authors Bueno, A.A. !$#submission submitted to the EMBL Data Library, March 1992 !$#accession S28236 !'##molecule_type DNA !'##residues 1-513 ##label BUE !'##cross-references EMBL:X65299; NID:g3509; PIDN:CAA46392.1; PID:g3510 REFERENCE A33711 !$#authors Zhou, C.; Huang, S.H.; Jong, A.Y. !$#journal J. Biol. Chem. (1989) 264:9022-9029 !$#title Molecular cloning of Saccharomyces cerevisiae CDC6 gene. !1Isolation, identification, and sequence analysis. !$#cross-references MUID:89255379; PMID:2656692 !$#accession S05737 !'##molecule_type DNA !'##residues 1-2,'G',4-513 ##label ZHO !'##cross-references EMBL:J04734 !'##note the authors translated the codon GGT for residue 3 as Ala REFERENCE S11954 !$#authors Jong, A.Y. !$#submission submitted to the EMBL Data Library, August 1989 !$#accession S11954 !'##molecule_type DNA !'##residues 1-2,'G',4-201,'I',203-224,'I',226-276,'F',278-338,'S', !1340-513 ##label JON !'##cross-references EMBL:J04734; NID:g171199; PIDN:AAA34484.1; !1PID:g171200 REFERENCE S20156 !$#authors Lisziewicz, J.; Godany, A.; Agoston, D.V.; Kuentzel, H. !$#journal Nucleic Acids Res. (1988) 16:11507-11520 !$#title Cloning and characterization of the Saccharomyces cerevisiae !1CDC6 gene. !$#cross-references MUID:89098306; PMID:3062576 !$#accession S20156 !'##molecule_type DNA !'##residues 89-271,'P',273-394,'LQN',397-401,'L',403-409,'S',411-435, !1'L',437-513 ##label LIS !'##cross-references EMBL:X13118; NID:g3505; PIDN:CAA31510.1; PID:g3506 REFERENCE S37746 !$#authors Zhou, C.; Jong, A. !$#journal J. Biol. Chem. (1990) 265:19904-19909 !$#title CDC6 mRNA fluctuates periodically in the yeast cell cycle. !$#cross-references MUID:91060609; PMID:2246267 !$#accession S37746 !'##status translation not shown !'##molecule_type DNA !'##residues 1-48 ##label ZH2 !'##cross-references EMBL:M61183; NID:g171205; PIDN:AAA34488.1; !1PID:g171206 REFERENCE S56977 !$#authors Purnelle, B.; Coster, F.; Goffeau, A. !$#submission submitted to the Protein Sequence Database, September 1995 !$#accession S56981 !'##molecule_type DNA !'##residues 1-513 ##label PUW !'##cross-references EMBL:Z49470; NID:g1008407; PIDN:CAA89490.1; !1PID:g1008409; GSPDB:GN00010; MIPS:YJL194w GENETICS !$#gene SGD:CDC6; MIPS:YJL194w !'##cross-references SGD:S0003730; MIPS:YJL194w !$#map_position 10L FUNCTION !$#description cell cycle control CLASSIFICATION #superfamily cell division control protein CDC6 KEYWORDS cell cycle control SUMMARY #length 513 #molecular-weight 58036 #checksum 9042 SEQUENCE /// ENTRY A39654 #type complete TITLE cell cycle arrest protein BUB2 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YM9796.08c; protein YMR055c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 21-Jul-2000 ACCESSIONS A39654; S54555; S19034 REFERENCE A39654 !$#authors Hoyt, M.A.; Totis, L.; Roberts, B.T. !$#journal Cell (1991) 66:507-517 !$#title Saccharomyces cerevisiae genes required for cell cycle !1arrest in response to loss of microtubule function. !$#cross-references MUID:91330299; PMID:1651171 !$#accession A39654 !'##molecule_type DNA !'##residues 1-306 ##label HOY !'##cross-references GB:M64706; NID:g171133; PIDN:AAA16885.1; !1PID:g171135 REFERENCE S54548 !$#authors Devlin, K.; Churcher, C.M. !$#submission submitted to the EMBL Data Library, May 1995 !$#accession S54555 !'##molecule_type DNA !'##residues 1-306 ##label DEV !'##cross-references EMBL:Z49703; NID:g817880; PIDN:CAA89765.1; !1PID:g817888; GSPDB:GN00013; MIPS:YMR055c GENETICS !$#gene SGD:BUB2; MIPS:YMR055c !'##cross-references SGD:S0004659; MIPS:YMR055c !$#map_position 13R CLASSIFICATION #superfamily cell cycle arrest protein BUB2 KEYWORDS transmembrane protein FEATURE !$232-248 #domain transmembrane #status predicted #label TMM SUMMARY #length 306 #molecular-weight 35027 #checksum 4878 SEQUENCE /// ENTRY B39654 #type complete TITLE cell cycle arrest protein BUB3 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein O2654; protein YOR026w ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 21-Jul-2000 ACCESSIONS B39654; S54632; S66892; S19036 REFERENCE A39654 !$#authors Hoyt, M.A.; Totis, L.; Roberts, B.T. !$#journal Cell (1991) 66:507-517 !$#title Saccharomyces cerevisiae genes required for cell cycle !1arrest in response to loss of microtubule function. !$#cross-references MUID:91330299; PMID:1651171 !$#accession B39654 !'##molecule_type DNA !'##residues 1-341 ##label HOY !'##cross-references GB:M64707; NID:g171136; PIDN:AAA34459.1; !1PID:g171137 REFERENCE S54617 !$#authors de Haan, M.; Maarse, A.C.; Grivell, L.A. !$#submission submitted to the EMBL Data Library, May 1995 !$#accession S54632 !'##molecule_type DNA !'##residues 1-341 ##label DEH !'##cross-references EMBL:X87331; NID:g1041652; PIDN:CAA60742.1; !1PID:g829136 !'##experimental_source strain S288C REFERENCE S66877 !$#authors de Haan, M.; Grivell, L.A.; Maarse, A.C. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S66892 !'##molecule_type DNA !'##residues 1-341 ##label DEW !'##cross-references EMBL:Z74934; NID:g1420136; PIDN:CAA99216.1; !1PID:g1420137; GSPDB:GN00015; MIPS:YOR026w !'##experimental_source strain S288C GENETICS !$#gene SGD:BUB3; MIPS:YOR026w !'##cross-references SGD:S0005552; MIPS:YOR026w !$#map_position 15R FUNCTION !$#description cell cycle arrest CLASSIFICATION #superfamily cell cycle arrest protein BUB3 KEYWORDS cell cycle control SUMMARY #length 341 #molecular-weight 38444 #checksum 394 SEQUENCE /// ENTRY COBYC1 #type complete TITLE cyclin 1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YM9646.13; protein YMR199w ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1992 #sequence_revision 12-May-1995 #text_change 12-Nov-1999 ACCESSIONS S50929; A33289; S12306 REFERENCE S50917 !$#authors Pearson, D.; Bowman, S. !$#submission submitted to the EMBL Data Library, January 1995 !$#accession S50929 !'##molecule_type DNA !'##residues 1-546 ##label PEA !'##cross-references EMBL:Z47815; NID:g642280; PIDN:CAA87822.1; !1PID:g642293; GSPDB:GN00013; MIPS:YMR199w REFERENCE A33289 !$#authors Hadwiger, J.A.; Wittenberg, C.; Richardson, H.E.; de Barros !1Lopes, M.; Reed, S.I. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:6255-6259 !$#title A family of cyclin homologs that control the G-1 phase in !1yeast. !$#cross-references MUID:89345642; PMID:2569741 !$#accession A33289 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-12,'H',14-95,'S',97-250,'R',252-255,'S',257-517,'S', !1519-546 ##label HAD1 REFERENCE S12306 !$#authors Hadwiger, J.A.; Reed, S.I. !$#journal Nucleic Acids Res. (1990) 18:4025 !$#title Nucleotide sequence of the Saccharomyces cerevisiae CLN1 and !1CLN2 genes. !$#cross-references MUID:90326560; PMID:2197605 !$#accession S12306 !'##status translation not shown !'##molecule_type DNA !'##residues 1-12,'H',14-95,'S',97-250,'R',252-255,'S',257-517,'S', !1519-546 ##label HAD2 !'##cross-references EMBL:M33264 GENETICS !$#gene SGD:CLN1; MIPS:YMR199w !'##cross-references SGD:S0004812; MIPS:YMR199w !$#map_position 13R CLASSIFICATION #superfamily yeast cyclin KEYWORDS cell cycle control SUMMARY #length 546 #molecular-weight 62049 #checksum 3434 SEQUENCE /// ENTRY COBYC2 #type complete TITLE cyclin 2 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein P0741; protein YPL256c ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 21-Jul-2000 ACCESSIONS B33289; S12307; S65287 REFERENCE A33289 !$#authors Hadwiger, J.A.; Wittenberg, C.; Richardson, H.E.; de Barros !1Lopes, M.; Reed, S.I. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:6255-6259 !$#title A family of cyclin homologs that control the G-1 phase in !1yeast. !$#cross-references MUID:89345642; PMID:2569741 !$#accession B33289 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-545 ##label HAD1 !'##cross-references GB:M33265; NID:g171243; PIDN:AAA65725.1; !1PID:g171244 REFERENCE S12306 !$#authors Hadwiger, J.A.; Reed, S.I. !$#journal Nucleic Acids Res. (1990) 18:4025 !$#title Nucleotide sequence of the Saccharomyces cerevisiae CLN1 and !1CLN2 genes. !$#cross-references MUID:90326560; PMID:2197605 !$#accession S12307 !'##status translation not shown !'##molecule_type DNA !'##residues 1-545 ##label HAD2 !'##cross-references EMBL:M33265; NID:g171243; PIDN:AAA65725.1; !1PID:g171244 REFERENCE S64935 !$#authors Messenguy, F.; Dubois, E.; Vierendeels, F.; Scherens, B. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S65287 !'##molecule_type DNA !'##residues 1-545 ##label MES !'##cross-references EMBL:Z73612; NID:g1370525; PIDN:CAA97982.1; !1PID:g1370526; GSPDB:GN00016; MIPS:YPL256c !'##experimental_source strain S288C (AB972) GENETICS !$#gene SGD:CLN2; MIPS:YPL256c !'##cross-references SGD:S0006177; MIPS:YPL256c !$#map_position 16L CLASSIFICATION #superfamily yeast cyclin KEYWORDS cell cycle control SUMMARY #length 545 #molecular-weight 61696 #checksum 1666 SEQUENCE /// ENTRY COBEQ2 #type complete TITLE cyclin homolog ECLF2 - saimiriine herpesvirus 1 (strain 11) ORGANISM #formal_name saimiriine herpesvirus 1 #note host Saimiri sciureus (common squirrel monkey) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 18-Jun-1999 ACCESSIONS S20243; F36813 REFERENCE S20243 !$#authors Nicholas, J.; Cameron, K.R.; Honess, R.W. !$#journal Nature (1992) 355:362-365 !$#title Herpesvirus saimiri encodes homologues of G protein-coupled !1receptors and cyclins. !$#cross-references MUID:92115001; PMID:1309943 !$#accession S20243 !'##molecule_type DNA !'##residues 1-254 ##label NIC !'##cross-references GB:S76368; NID:g243351; PIDN:AAB21115.1; !1PID:g243352 REFERENCE A36806 !$#authors Albrecht, J. !$#submission submitted to the EMBL Data Library, January 1992 !$#description Primary structure of the herpesvirus saimiri genome. !$#accession F36813 !'##molecule_type DNA !'##residues 1-254 ##label ALB !'##cross-references GB:X64346; NID:g60320; PIDN:CAA45695.1; PID:g60393 REFERENCE A37309 !$#authors Albrecht, J.C.; Nicholas, J.; Biller, D.; Cameron, K.R.; !1Biesinger, B.; Newman, C.; Wittmann, S.; Craxton, M.A.; !1Coleman, H.; Fleckenstein, B.; Honess, R.W. !$#journal J. Virol. (1992) 66:5047-5058 !$#title Primary structure of the herpesvirus saimiri genome. !$#cross-references MUID:92333688; PMID:1321287 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene ECLF2; 72 CLASSIFICATION #superfamily cyclin KEYWORDS cell cycle control SUMMARY #length 254 #molecular-weight 28637 #checksum 1899 SEQUENCE /// ENTRY COBY26 #type complete TITLE cell division control protein CDC26 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein F017; protein YFR036w ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1991 #sequence_revision 03-Nov-1995 #text_change 16-Jun-2000 ACCESSIONS S56291; S07680; S62247; S63841 REFERENCE S56186 !$#authors Murakami, Y.; Naitou, M.; Hagiwara, H.; Shibata, T.; Ozawa, !1M.; Sasanuma, S.I.; Sasanuma, M.; Tsuchiya, Y.; Soeda, E.; !1Yokoyama, K.; Yamazaki, M.; Tashiro, H.; Eki, T. !$#submission submitted to the EMBL Data Library, May 1995 !$#description Analysis of the nucleotide sequence of chromosome VI from !1Saccaromyces cerevisiae. !$#accession S56291 !'##molecule_type DNA !'##residues 1-124 ##label MUR !'##cross-references EMBL:D50617; NID:g836685; PIDN:BAA09275.1; !1PID:g836791; GSPDB:GN00006; MIPS:YFR036w REFERENCE S07680 !$#authors Dascher, C.; Kuentzel, H. !$#journal Nucleic Acids Res. (1989) 17:10491 !$#title Nucleotide sequence of yeast SCD26, a dosage-dependent !1suppressor of the cell cycle mutation cdc26. !$#cross-references MUID:90098884; PMID:2690018 !$#accession S07680 !'##molecule_type DNA !'##residues 1-49,'F',51-120,'TARNNSISAYAHAHAHAHASTFTFTYKISSL' ##label !1DAS !'##cross-references EMBL:X17118; NID:g4423; PIDN:CAA34978.1; PID:g4424 REFERENCE S62230 !$#authors Murakami, Y. !$#submission submitted to the EMBL Data Library, December 1994 !$#accession S62247 !'##molecule_type DNA !'##residues 1-124 ##label MUW !'##cross-references EMBL:D44602; NID:g893419; PIDN:BAA08047.1; !1PID:g893431 REFERENCE S63830 !$#authors Eki, T.; Naitou, M.; Hagiwara, H.; Abe, M.; Ozawa, M.; !1Sasanuma, S.I.; Sasanuma, M.; Tsuchiya, Y.; Shibata, T.; !1Watanabe, K.; Ono, A.; Yamazaki, M.A.; Tashiro, H.; Hanaoka, !1F.; Murakami, Y. !$#journal Yeast (1996) 12:177-190 !$#title Fifteen open reading frames in a 30.8 kb region of the right !1arm of chromosome VI from Saccharomyces cerevisiae. !$#cross-references MUID:96287654; PMID:8686381 !$#accession S63841 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-124 ##label EKI !'##cross-references EMBL:D44602; NID:g893419; PIDN:BAA08047.1; !1PID:g893431 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1995 GENETICS !$#gene SGD:CDC26; SCD26; HIT3; MIPS:YFR036w !'##cross-references SGD:S0001932; MIPS:YFR036w !$#map_position 6R CLASSIFICATION #superfamily SDC26 protein KEYWORDS cell cycle control SUMMARY #length 124 #molecular-weight 14081 #checksum 5799 SEQUENCE /// ENTRY COBY10 #type complete TITLE COX10 protein precursor - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein P2287; protein YPL172c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 21-Jul-2000 ACCESSIONS A37812; B55569; S51872; S65184; S11193 REFERENCE A37812 !$#authors Nobrega, M.P.; Nobrega, F.G.; Tzagoloff, A. !$#journal J. Biol. Chem. (1990) 265:14220-14226 !$#title COX10 codes for a protein homologous to the ORF1 product of !1Paracoccus denitrificans and is required for the synthesis !1of yeast cytochrome oxidase. !$#cross-references MUID:90354402; PMID:2167310 !$#accession A37812 !'##molecule_type DNA !'##residues 1-462 ##label NOB !'##cross-references GB:M55566; GB:J05566; NID:g171264; PIDN:AAA34509.1; !1PID:g171265 REFERENCE A55569 !$#authors Niino, Y.S.; Chakraborty, S.; Brown, B.J.; Massey, V. !$#journal J. Biol. Chem. (1995) 270:1983-1991 !$#title A new Old Yellow enzyme of Saccharomyces cerevisiae. !$#cross-references MUID:95138156; PMID:7836424 !$#accession B55569 !'##status preliminary !'##molecule_type DNA !'##residues 1-30 ##label NII !'##cross-references GB:L29279; NID:g460038; PIDN:AAA64523.1; !1PID:g460040 REFERENCE S51871 !$#authors Niino, Y.S.; Chakraborty, S.; Massey, V. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S51872 !'##molecule_type DNA !'##residues 1-30 ##label NIW !'##cross-references EMBL:L29279; NID:g460038; PIDN:AAA64523.1; !1PID:g460040 REFERENCE S65183 !$#authors Benes, V.; Rechmann, S.; Nentwich, U.; Voss, H.; Ansorge, W. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S65184 !'##molecule_type DNA !'##residues 1-462 ##label BEN !'##cross-references EMBL:Z73528; NID:g1370362; PIDN:CAA97879.1; !1PID:g1370363; GSPDB:GN00016; MIPS:YPL172c !'##experimental_source strain S288C (AB972) GENETICS !$#gene SGD:COX10; MIPS:YPL172c !'##cross-references SGD:S0006093; MIPS:YPL172c !$#map_position 16L !$#genome nuclear CLASSIFICATION #superfamily COX10 protein KEYWORDS mitochondrial inner membrane; mitochondrion; transmembrane !1protein FEATURE !$1-30 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$31-462 #product COX10 protein #status predicted #label MAT\ !$157-173 #domain transmembrane #status predicted #label TM1\ !$231-247 #domain transmembrane #status predicted #label TM2\ !$425-441 #domain transmembrane #status predicted #label TM3 SUMMARY #length 462 #molecular-weight 52147 #checksum 9564 SEQUENCE /// ENTRY PFHUG1 #type complete TITLE platelet-derived growth factor chain A precursor - human ALTERNATE_NAMES PDGF A-chain; PDGF-1; PDGF-A; platelet-derived growth factor 1 ORGANISM #formal_name Homo sapiens #common_name man DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 18-Feb-2000 ACCESSIONS A28964; S47564; A42002; A01379; S00173; A28122 REFERENCE A28964 !$#authors Bonthron, D.T.; Morton, C.C.; Orkin, S.H.; Collins, T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:1492-1496 !$#title Platelet-derived growth factor A chain: gene structure, !1chromosomal location, and basis for alternative mRNA !1splicing. !$#cross-references MUID:88144463; PMID:3422746 !$#accession A28964 !'##molecule_type DNA !'##residues 1-211 ##label BON !'##cross-references GB:M21571; GB:J03638; GB:M19984; GB:M19985; !1GB:M19986; GB:M19987; GB:M19988; NID:g189718; !1PIDN:AAA60046.1; PID:g387007 REFERENCE S47564 !$#authors Takimoto, Y.; Kuramoto, A. !$#journal Biochim. Biophys. Acta (1994) 1222:511-514 !$#title Gene regulation by the 5'-untranslated region of the !1platelet-derived growth factor A-chain. !$#cross-references MUID:94312450; PMID:7518695 !$#accession S47564 !'##status preliminary !'##molecule_type DNA !'##residues 1-21 ##label TAK REFERENCE A42002 !$#authors Bonthron, D.; Collins, T.; Grzeschik, K.H.; van Roy, N.; !1Speleman, F. !$#journal Genomics (1992) 13:257-263 !$#title Platelet-derived growth factor A chain: confirmation of !1localization of PDGFA to chromosome 7p22 and description of !1an unusual minisatellite. !$#cross-references MUID:92307656; PMID:1612586 !$#accession A42002 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 152-211 ##label BO2 REFERENCE A01379 !$#authors Betsholtz, C.; Johnsson, A.; Heldin, C.H.; Westermark, B.; !1Lind, P.; Urdea, M.S.; Eddy, R.; Shows, T.B.; Philpott, K.; !1Mellor, A.L.; Knott, T.J.; Scott, J. !$#journal Nature (1986) 320:695-699 !$#title cDNA sequence and chromosomal localization of human !1platelet-derived growth factor A-chain and its expression in !1tumour cell lines. !$#cross-references MUID:86203630; PMID:3754619 !$#accession A01379 !'##molecule_type mRNA !'##residues 1-211 ##label BET !'##cross-references GB:X03795; NID:g35365; PIDN:CAA27421.1; PID:g35366 !'##experimental_source clonal glioma cell line U-343 MGaC12:6, a tumor !1cell line REFERENCE S00173 !$#authors Hoppe, J.; Schumacher, L.; Eichner, W.; Weich, H.A. !$#journal FEBS Lett. (1987) 223:243-246 !$#title The long 3'-untranslated regions of the PDGF-A and -B mRNAs !1are only distantly related. !$#cross-references MUID:88030061; PMID:3666150 !$#accession S00173 !'##molecule_type mRNA !'##residues 1-193,'DVR' ##label HOP !'##cross-references EMBL:X06374; NID:g35363; PIDN:CAA29677.1; !1PID:g35364 REFERENCE A28122 !$#authors Rorsman, F.; Bywater, M.; Knott, T.J.; Scott, J.; Betsholtz, !1C. !$#journal Mol. Cell. Biol. (1988) 8:571-577 !$#title Structural characterization of the human platelet-derived !1growth factor A-chain cDNA and gene: alternative exon usage !1predicts two different precursor proteins. !$#cross-references MUID:88174698; PMID:2832727 !$#accession A28122 !'##molecule_type mRNA !'##residues 1-63,'TRD',67-211 ##label ROR !'##cross-references GB:M20488 !'##note the authors translated the codon ACA for residue 64 as Arg, CGT !1for residue 65 as Ala, and GAC for residue 66 as His COMMENT Platelet-derived growth factor, a potent mitogen for cells !1of mesenchymal origin, induces a variety of cellular !1responses. Different receptors bind preferentially to A and !1B homodimers. COMMENT A carboxyl-terminal propeptide may be removed from the !1precursor by proteolysis. GENETICS !$#gene GDB:PDGFA !'##cross-references GDB:120266; OMIM:173430 !$#map_position 7p22-7p22 !$#introns 21/3; 54/1; 89/1; 151/3; 194/1 COMPLEX homodimer; heterodimer (see PIR:PFHUG2) CLASSIFICATION #superfamily platelet-derived growth factor KEYWORDS alternative splicing; glycoprotein; growth factor; mitogen; !1platelet FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-86 #domain propeptide #status predicted #label PRO\ !$87-211 #product platelet-derived growth factor chain A !8#status predicted #label MAT\ !$158-162 #region receptor binding #status predicted\ !$96-140,129-177, !$133-179 #disulfide_bonds #status predicted\ !$123 #disulfide_bonds interchain (to chain B-133 in !8heterodimeric form) #status predicted\ !$123 #disulfide_bonds interchain (to 132 in homodimeric !8form) #status predicted\ !$132 #disulfide_bonds interchain (to chain B-124 in !8heterodimeric form) #status predicted\ !$132 #disulfide_bonds interchain (to 123 in homodimeric !8form) #status predicted\ !$134 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 211 #molecular-weight 24043 #checksum 7074 SEQUENCE /// ENTRY PFHUG2 #type complete TITLE platelet-derived growth factor chain B precursor [validated] - human ALTERNATE_NAMES PDGF B-chain; PDGF-B; PDGF-II; PDGF-related transforming protein (sis) ORGANISM #formal_name Homo sapiens #common_name man DATE 18-Apr-1984 #sequence_revision 20-Sep-1984 #text_change 08-Dec-2000 ACCESSIONS A94276; A21024; A23532; A93366; A25141; A94271; A93308; !1A43499; S56115; I57635; I37266; A55030; S58383; I38108; !1A01380; A94622 REFERENCE A94276 !$#authors Josephs, S.F.; Ratner, L.; Clarke, M.F.; Westin, E.H.; !1Reitz, M.S.; Wong-Staal, F. !$#journal Science (1984) 225:636-639 !$#title Transforming potential of human c-sis nucleotide sequences !1encoding platelet-derived growth factor. !$#cross-references MUID:84250225; PMID:6740330 !$#accession A94276 !'##molecule_type DNA !'##residues 1-241 ##label JOS1 !'##cross-references GB:K01401; NID:g338206; PIDN:AAA60552.1; !1PID:g338209 REFERENCE A21024 !$#authors Chiu, I.M.; Reddy, E.P.; Givol, D.; Robbins, K.C.; Tronick, !1S.R.; Aaronson, S.A. !$#journal Cell (1984) 37:123-129 !$#title Nucleotide sequence analysis identifies the human c-sis !1proto-oncogene as a structural gene for platelet-derived !1growth factor. !$#cross-references MUID:84205633; PMID:6327048 !$#accession A21024 !'##molecule_type DNA !'##residues 17-20,'RQ',22-241 ##label CHI !'##cross-references GB:K01917; NID:g338197 REFERENCE A23532 !$#authors Rao, C.D.; Igarashi, H.; Chiu, I.M.; Robbins, K.C.; !1Aaronson, S.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:2392-2396 !$#title Structure and sequence of the human c-sis/platelet-derived !1growth factor 2 (SIS/PDGF2) transcriptional unit. !$#cross-references MUID:86205961; PMID:3517869 !$#accession A23532 !'##molecule_type mRNA !'##residues 1-241 ##label RAO1 !'##cross-references GB:M12783; GB:M16288; NID:g338210; PIDN:AAA60553.1; !1PID:g338211 REFERENCE A93366 !$#authors Collins, T.; Ginsburg, D.; Boss, J.M.; Orkin, S.H.; Pober, !1J.S. !$#journal Nature (1985) 316:748-750 !$#title Cultured human endothelial cells express platelet-derived !1growth factor B chain: cDNA cloning and structural analysis. !$#cross-references MUID:85296313; PMID:4033772 !$#accession A93366 !'##molecule_type mRNA !'##residues 1-241 ##label COL !'##cross-references GB:X02811; NID:g35371; PIDN:CAA26579.1; PID:g35372 REFERENCE A25141 !$#authors Weich, H.A.; Sebald, W.; Schairer, H.U.; Hoppe, J. !$#journal FEBS Lett. (1986) 198:344-348 !$#title The human osteosarcoma cell line U-2 OS expresses a 3.8 !1kilobase mRNA which codes for the sequence of the PDGF-B !1chain. !$#cross-references MUID:86164981; PMID:3456904 !$#accession A25141 !'##molecule_type mRNA !'##residues 26-241 ##label WEI !'##cross-references GB:X03702; NID:g35374; PIDN:CAA27333.1; PID:g35375 REFERENCE A94271 !$#authors Antoniades, H.N.; Hunkapiller, M.W. !$#journal Science (1983) 220:963-965 !$#title Human platelet-derived growth factor (PDGF): amino-terminal !1amino acid sequence. !$#cross-references MUID:83197379; PMID:6844921 !$#accession A94271 !'##molecule_type protein !'##residues 82-100,'E',102-104,'C',106,'C',108-110 ##label ANT REFERENCE A93308 !$#authors Waterfield, M.D.; Scrace, G.T.; Whittle, N.; Stroobant, P.; !1Johnsson, A.; Wasteson, A.; Westermark, B.; Heldin, C.H.; !1Huang, J.S.; Deuel, T.F. !$#journal Nature (1983) 304:35-39 !$#title Platelet-derived growth factor is structurally related to !1the putative transforming protein p28(sis) of simian sarcoma !1virus. !$#cross-references MUID:83244981; PMID:6306471 !$#accession A93308 !'##molecule_type protein !'##residues 82-112 ##label WAT REFERENCE A43499 !$#authors Josephs, S.F.; Guo, C.; Ratner, L.; Wong-Staal, F. !$#journal Science (1984) 223:487-491 !$#title Human proto-oncogene nucleotide sequences corresponding to !1the transforming region of simian sarcoma virus. !$#cross-references MUID:84097555; PMID:6318322 !$#accession A43499 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 'Q',22-241 ##label JOS2 REFERENCE S56115 !$#authors Lu, K.V.; Rohde, M.F.; Thomason, A.R.; Kenney, W.C.; Lu, !1H.S. !$#journal Biochem. J. (1995) 309:411-417 !$#title Mistranslation of a TGA termination codon as tryptophan in !1recombinant platelet-derived growth factor expressed in !1Escherichia coli. !$#cross-references MUID:95351967; PMID:7626004 !$#accession S56115 !'##status preliminary !'##molecule_type protein !'##residues 82-93 ##label LUK REFERENCE I57635 !$#authors Rao, C.D.; Pech, M.; Robbins, K.C.; Aaronson, S.A. !$#journal Mol. Cell. Biol. (1988) 8:284-292 !$#title The 5' untranslated sequence of the c-sis/platelet-derived !1growth factor 2 transcript is a potent translational !1inhibitor. !$#cross-references MUID:88094398; PMID:3275870 !$#accession I57635 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-20 ##label RAO2 !'##cross-references GB:M19719; NID:g189727; PIDN:AAA60349.1; !1PID:g553608 REFERENCE I37266 !$#authors Ratner, L.; Josephs, S.F.; Jarrett, R.; Reitz, M.S. !$#journal Nucleic Acids Res. (1985) 13:5007-5018 !$#title Nucleotide sequence of transforming human c-sis cDNA clones !1with homology to platelet-derived growth factor. !$#cross-references MUID:85269623; PMID:2991848 !$#accession I37266 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-241 ##label RAT !'##cross-references EMBL:X02744; NID:g30246; PIDN:CAA26524.1; !1PID:g30247 REFERENCE A55030 !$#authors Johnsson, A.; Heldin, C.H.; Wasteson, A.; Westermark, B.; !1Deuel, T.F.; Huang, J.S.; Seeburg, P.H.; Gray, A.; Ullrich, !1A.; Scrace, G.; Stroobant, P.; Waterfield, M.D. !$#journal EMBO J. (1984) 3:921-928 !$#title The c-sis gene encodes a precursor of the B chain of !1platelet-derived growth factor. !$#cross-references MUID:84236121; PMID:6329745 !$#accession A55030 !'##status preliminary !'##molecule_type DNA !'##residues 'SLSL',17-20,'RQ',22-241 ##label JOH !'##cross-references GB:X00556; GB:X00559; GB:X00560; GB:X00561; !1GB:X00562 REFERENCE S58382 !$#authors Dirks, R.P.H.; Onnekink, C.; Jansen, H.J.; de Jong, A.; !1Bloemers, H.P.J. !$#journal Nucleic Acids Res. (1995) 23:2815-2822 !$#title A novel human c-sis mRNA species is transcribed from a !1promoter in c-sis intron 1 and contains the code for an !1alternative PDGF B-like protein. !$#cross-references MUID:95388493; PMID:7659502 !$#accession S58383 !'##status preliminary !'##molecule_type mRNA !'##residues 'MFIMGL',22-200 ##label DIR !'##cross-references EMBL:X83705; NID:g951023; PIDN:CAA58679.1; !1PID:g951025 REFERENCE I38108 !$#authors Cook, A.L.; Kirwin, P.M.; Craig, S.; Bawden, L.J.; Green, !1D.R.; Price, M.J.; Richardson, S.J.; Fallon, A.; Drummond, !1A.H.; Edwards, R.M.; Clements, J.M. !$#journal Biochem. J. (1992) 281:57-65 !$#title Purification and analysis of proteinase-resistant mutants of !1recombinant platelet-derived growth factor-BB exhibiting !1improved biological activity. !$#cross-references MUID:92117992; PMID:1731768 !$#accession I38108 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 'M',82-241 ##label COO !'##cross-references EMBL:X63966; NID:g311378; PIDN:CAA45383.1; !1PID:g35377 !'##note mutagenized recombinant sequence COMMENT Platelet-derived growth factor, a potent mitogen for cells !1of mesenchymal origin, induces a variety of cellular !1responses. Different receptors bind preferentially to A and !1B homodimers. GENETICS !$#gene GDB:PDGFB !'##cross-references GDB:120709; OMIM:190040 !$#map_position 22q12.3-22q13.1 !$#introns 57/3; 94/1; 192/3; 241/1 COMPLEX homodimer; heterodimer (see PIR:PFHUG1) CLASSIFICATION #superfamily platelet-derived growth factor KEYWORDS growth factor; mitogen FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-81 #domain amino-terminal propeptide #status predicted !8#label PRO\ !$82-190 #product platelet-derived growth factor chain B !8#status experimental #label MAT\ !$159-163 #region receptor binding #status predicted\ !$191-241 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$97-141,130-178, !$134-180 #disulfide_bonds #status experimental\ !$124 #disulfide_bonds interchain (to 133 in homodimeric !8form) #status experimental\ !$124 #disulfide_bonds interchain (to chain A-132 in !8heterodimeric form) #status predicted\ !$133 #disulfide_bonds interchain (to 124 in homodimeric !8form) #status experimental\ !$133 #disulfide_bonds interchain (to chain A-124 in !8heterodimeric form) #status predicted SUMMARY #length 241 #molecular-weight 27283 #checksum 3348 SEQUENCE /// ENTRY PFMSGB #type complete TITLE platelet-derived growth factor chain B precursor (sis) - mouse ALTERNATE_NAMES PDGF-related transforming protein ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1992 #sequence_revision 31-Mar-1993 #text_change 18-Jun-1999 ACCESSIONS A39073 REFERENCE A39073 !$#authors Bonthron, D.T.; Sultan, P.; Collins, T. !$#journal Genomics (1991) 10:287-292 !$#title Structure of the murine c-sis proto-oncogene (Sis, PDGFB) !1encoding the B chain of platelet-derived growth factor. !$#cross-references MUID:91257844; PMID:2045107 !$#accession A39073 !'##molecule_type DNA !'##residues 1-241 ##label BON !'##cross-references GB:M64849; GB:M55394; NID:g192818; PIDN:AAA37485.1; !1PID:g192820 GENETICS !$#gene sis CLASSIFICATION #superfamily platelet-derived growth factor KEYWORDS glycoprotein; growth factor; platelet; proto-oncogene; !1transforming protein FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-81 #domain propeptide #status predicted #label PRO\ !$82-190 #product platelet-derived growth factor chain B !8#status predicted #label MAT\ !$159-163 #region receptor binding #status predicted\ !$63 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 241 #molecular-weight 27381 #checksum 4345 SEQUENCE /// ENTRY TVCTSS #type complete TITLE platelet-derived growth factor chain B precursor - cat ALTERNATE_NAMES PDGF-related transforming protein ORGANISM #formal_name Felis silvestris catus #common_name domestic cat DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 31-Mar-1996 ACCESSIONS A26402 REFERENCE A26402 !$#authors Van den Ouweland, A.M.W.; Van Groningen, J.J.M.; Schalken, !1J.A.; Van Neck, H.W.; Bloemers, H.P.J.; Van de Ven, W.J.M. !$#journal Nucleic Acids Res. (1987) 15:959-970 !$#title Genetic organization of the c-sis transcription unit. !$#cross-references MUID:87146463; PMID:3822831 !$#accession A26402 !'##molecule_type mRNA !'##residues 1-245 ##label VAN GENETICS !$#gene sis CLASSIFICATION #superfamily platelet-derived growth factor KEYWORDS glycoprotein; growth factor; platelet; proto-oncogene; !1transforming protein FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-81 #domain propeptide #status predicted #label PRO\ !$82-194 #product platelet-derived growth factor chain B !8#status predicted #label MAT\ !$163-167 #region receptor binding #status predicted\ !$63 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 245 #molecular-weight 27787 #checksum 2148 SEQUENCE /// ENTRY TVMVSS #type complete TITLE PDGF-related transforming protein (sis) - simian sarcoma virus ALTERNATE_NAMES p28-sis ORGANISM #formal_name simian sarcoma virus DATE 23-Jul-1983 #sequence_revision 20-Sep-1984 #text_change 31-Oct-1997 ACCESSIONS A01381 REFERENCE A03982 !$#authors Devare, S.G.; Reddy, E.P.; Law, J.D.; Robbins, K.C.; !1Aaronson, S.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:731-735 !$#title Nucleotide sequence of the simian sarcoma virus genome: !1demonstration that its acquired cellular sequences encode !1the transforming gene product p28(sis). !$#cross-references MUID:83144004; PMID:6298772 !$#accession A01381 !'##molecule_type genomic RNA !'##residues 1-226 ##label DEV GENETICS !$#gene sis CLASSIFICATION #superfamily platelet-derived growth factor KEYWORDS growth factor; transforming protein FEATURE !$6-226 #domain platelet-derived growth factor chain B !8similarity #label PDG SUMMARY #length 226 #molecular-weight 25411 #checksum 2886 SEQUENCE /// ENTRY THHUB #type complete TITLE thrombomodulin precursor [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1988 #sequence_revision 12-May-1995 #text_change 15-Sep-2000 ACCESSIONS A41442; A28307; A29680; A27073; JX0264; S38954 REFERENCE A41442 !$#authors Shirai, T.; Shiojiri, S.; Ito, H.; Yamamoto, S.; Kusumoto, !1H.; Deyashiki, Y.; Maruyama, I.; Suzuki, K. !$#journal J. Biochem. (1988) 103:281-285 !$#title Gene structure of human thrombomodulin, a cofactor for !1thrombin-catalyzed activation of protein C. !$#cross-references MUID:88227901; PMID:2836377 !$#accession A41442 !'##molecule_type DNA !'##residues 1-575 ##label SHI !'##cross-references DDBJ:D00210; NID:g220126; PIDN:BAA00149.1; !1PID:g220127 REFERENCE A28307 !$#authors Jackman, R.W.; Beeler, D.L.; Fritze, L.; Soff, G.; !1Rosenberg, R.D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:6425-6429 !$#title Human thrombomodulin gene is intron depleted: nucleic acid !1sequences of the cDNA and gene predict protein structure and !1suggest sites of regulatory control. !$#cross-references MUID:87317665; PMID:2819876 !$#accession A28307 !'##molecule_type DNA; mRNA !'##residues 1-472,'A',474-575 ##label JAC !'##cross-references GB:J02973; NID:g339658; PIDN:AAA61175.1; !1PID:g339659 REFERENCE A29680 !$#authors Suzuki, K.; Kusumoto, H.; Deyashiki, Y.; Nishioka, J.; !1Maruyama, I.; Zushi, M.; Kawahara, S.; Honda, G.; Yamamoto, !1S.; Horiguchi, S. !$#journal EMBO J. (1987) 6:1891-1897 !$#title Structure and expression of human thrombomodulin, a thrombin !1receptor on endothelium acting as a cofactor for protein C !1activation. !$#cross-references MUID:88004395; PMID:2820710 !$#accession A29680 !'##molecule_type mRNA !'##residues 1-575 ##label SUZ !'##cross-references GB:X05495; NID:g37123; PIDN:CAA29045.1; PID:g736251 !'##experimental_source lung endothelium !'##note part of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing REFERENCE A27073 !$#authors Wen, D.; Dittman, W.A.; Ye, R.D.; Deaven, L.L.; Majerus, !1P.W.; Sadler, J.E. !$#journal Biochemistry (1987) 26:4350-4357 !$#title Human thrombomodulin: complete cDNA sequence and chromosome !1localization of the gene. !$#cross-references MUID:88024950; PMID:2822087 !$#accession A27073 !'##molecule_type mRNA !'##residues 1-472,'A',474-575 ##label WEN !'##cross-references GB:M16552; NID:g339656; PIDN:AAB59508.1; !1PID:g339657 !'##experimental_source placenta !'##note parts of this sequence were determined by protein sequencing REFERENCE JX0264 !$#authors Yamamoto, S.; Mizoguchi, T.; Tamaki, T.; Ohkuchi, M.; !1Kimura, S.; Aoki, N. !$#journal J. Biochem. (1993) 113:433-440 !$#title Urinary thrombomodulin, its isolation and characterization. !$#cross-references MUID:93293792; PMID:8390446 !$#accession JX0264 !'##molecule_type protein; mRNA !'##residues 19-472,'A',474-486 ##label YAM !'##experimental_source urine !'##note the urinary form appears to be identical with that circulating !1in plasma REFERENCE S38954 !$#authors Gerlitz, B.; Hassell, T.; Vlahos, C.J.; Parkinson, J.F.; !1Bang, N.U.; Grinnell, B.W. !$#journal Biochem. J. (1993) 295:131-140 !$#title Identification of the predominant !1glycosaminoglycan-attachment site in soluble recombinant !1human thrombomodulin: potential regulation of functionality !1by glycosyltransferase competition for serine. !$#cross-references MUID:94029900; PMID:8216207 !$#accession S38954 !'##molecule_type protein !'##residues 475-491,'X',493-494 ##label GER !'##note the residue designated 'X' was determined to be a Ser with !1covalently bound chondroitin sulfate REFERENCE A67369 !$#authors Meininger, D.P.; Komives, E.A. !$#submission submitted to the Brookhaven Protein Data Bank, September !11995 !$#cross-references PDB:1ZAQ !$#contents annotation; conformation and disulfide bond assignments by !1(1)H-NMR, residues 364-407 REFERENCE A52804 !$#authors Tulinsky, A.; Mathews, I.I. !$#submission submitted to the Brookhaven Protein Data Bank, August 1994 !$#cross-references PDB:1HLT !$#contents annotation; X-ray crystallography, 3.0 angstroms, residues !1426-442 REFERENCE A65583 !$#authors Hrabal, R.; Komives, E.A.; Ni, F. !$#submission submitted to the Brookhaven Protein Data Bank, November 1995 !$#cross-references PDB:1FGD !$#contents annotation; conformation by (1)H-NMR, residues 427-444 REFERENCE A58595 !$#authors Hrabal, R.; Komives, E.A.; Ni, F. !$#journal Protein Sci. (1996) 5:195-203 !$#title Structural resiliency of an EGF-like subdomain bound to its !1target protein, thrombin. !$#cross-references MUID:96276211; PMID:8745396 !$#contents annotation; conformation by (1)H-NMR GENETICS !$#gene GDB:THBD !'##cross-references GDB:119613; OMIM:188040 !$#map_position 20p11.2-20p11.2 !$#introns #status absent COMPLEX homodimer, urinary form FUNCTION !$#description inhibits thrombin activation of fibrinogen; cofactor for !1thrombin activation of protein C !$#pathway blood coagulation moderation !$#note the membrane-bound form is located on the endothelium !1luminal surface of arteries, capillaries, veins and !1lymphatics and the syncytiotrophoblast of placenta !$#note thrombin complexed with the membrane-bound form is subject !1to endocytosis CLASSIFICATION #superfamily thrombomodulin; C-type lectin homology; EGF !1homology KEYWORDS anticoagulant; beta-hydroxyasparagine; beta-hydroxyaspartic !1acid; blood coagulation; chondroitin sulfate proteoglycan; !1endocytosis; glycoprotein; homodimer; thrombin binding; !1transmembrane protein FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-575 #product thrombomodulin, membrane-bound form #status !8predicted #label MAT\ !$19-513 #domain extracellular #status predicted #label EXT\ !$19-486 #product thrombomodulin, urinary form #status !8experimental #label MAU\ !$24-167 #domain C-type lectin homology #label LCH\ !$177-199 #region PEST sequence\ !$201-233 #region PEST sequence\ !$245-280 #domain EGF homology #label EG1\ !$288-323 #domain EGF homology #label EG2\ !$329-362 #domain EGF homology #label EG3\ !$369-404 #domain EGF homology #label EG4\ !$408-439 #domain EGF homology #label EG5\ !$445-480 #domain EGF homology #label EG6\ !$485-513 #region PEST sequence\ !$517-539 #domain transmembrane #status predicted #label TMN\ !$540-575 #domain intracellular #status predicted #label INT\ !$47,115,116,382,409 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$174,225,411,504 #binding_site carbohydrate (Thr) (covalent) #status !8predicted\ !$245-256,252-265, !$267-280,288-296, !$292-308,310-323, !$329-340,336-349, !$351-362,369-378, !$374-388,390-404, !$408-417,413-425, !$427-439,445-455, !$451-464,466-480 #disulfide_bonds #status predicted\ !$334,498 #binding_site carbohydrate (Ser) (covalent) #status !8predicted\ !$342 #modified_site erythro-beta-hydroxyasparagine (Asn) !8#status experimental\ !$490,492 #binding_site chondroitin sulfate (Ser) (covalent) !8(partial) #status experimental SUMMARY #length 575 #molecular-weight 60357 #checksum 9072 SEQUENCE /// ENTRY KXHUS #type complete TITLE plasma protein S precursor - human ALTERNATE_NAMES vitamin K-dependent protein S ORGANISM #formal_name Homo sapiens #common_name man DATE 21-Sep-1990 #sequence_revision 26-Jan-1996 #text_change 16-Jul-1999 ACCESSIONS A35610; A35611; A26157; A25891; A35612; A60903; S02424; !1S09519 REFERENCE A35610 !$#authors Schmidel, D.K.; Tatro, A.V.; Phelps, L.G.; Tomczak, J.A.; !1Long, G.L. !$#journal Biochemistry (1990) 29:7845-7852 !$#title Organization of the human protein S genes. !$#cross-references MUID:91084444; PMID:2148110 !$#accession A35610 !'##molecule_type DNA !'##residues 1-676 ##label SCH !'##cross-references GB:M57853; NID:g190547; PIDN:AAA60357.1; !1PID:g190549; GB:J02917 !'##note the authors translated the codon TTT for residue 26 as Leu REFERENCE A35611 !$#authors Ploos van Amstel, H.K.; Reitsma, P.H.; van der Logt, C.P.E.; !1Bertina, R.M. !$#journal Biochemistry (1990) 29:7853-7861 !$#title Intron-exon organization of the active human protein S gene !1PSalpha and its pseudogene PSbeta: duplication and silencing !1during primate evolution. !$#cross-references MUID:91084445; PMID:2148111 !$#accession A35611 !'##molecule_type DNA !'##residues 1-25 ##label PL3 !'##cross-references GB:J02918 REFERENCE A26157 !$#authors Hoskins, J.; Norman, D.K.; Beckmann, R.J.; Long, G.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:349-353 !$#title Cloning and characterization of human liver cDNA encoding a !1protein S precursor. !$#cross-references MUID:87092407; PMID:3467362 !$#accession A26157 !'##molecule_type mRNA !'##residues 1-10,'P',12-25,'L',27-676 ##label HOS !'##cross-references GB:M15036; NID:g190288; PIDN:AAA36479.1; !1PID:g190289 REFERENCE A25891 !$#authors Lundwall, A.; Dackowski, W.; Cohen, E.; Shaffer, M.; Mahr, !1A.; Dahlback, B.; Stenflo, J.; Wydro, R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:6716-6720 !$#title Isolation and sequence of the cDNA for human protein S, a !1regulator of blood coagulation. !$#cross-references MUID:86313649; PMID:2944113 !$#accession A25891 !'##molecule_type mRNA !'##residues 27-220,'L',222-262,'H',264-344,'Y',346-676 ##label LUN !'##cross-references GB:M14338; NID:g190448; PIDN:AAA60181.1; !1PID:g190449 !'##note part of this sequence, including the amino end of the mature !1protein, was determined by protein sequencing REFERENCE A35612 !$#authors Edenbrandt, C.M.; Lundwall, A.; Wydro, R.; Stenflo, J. !$#journal Biochemistry (1990) 29:7861-7868 !$#title Molecular analysis of the gene for vitamin K dependent !1protein S and its pseudogene. Cloning and partial gene !1organization. !$#cross-references MUID:91084446; PMID:2148112 !$#accession A35612 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 284-676 ##label EDE !'##cross-references GB:J02919 REFERENCE A60903 !$#authors Ploos van Amstel, J.K.; van der Zanden, A.L.; Bakker, E.; !1Reitsma, P.H.; Bertina, R.M. !$#journal Thromb. Haemost. (1987) 58:982-987 !$#title Two genes homologous with human protein S cDNA are located !1on chromosome 3. !$#cross-references MUID:88178564; PMID:2895503 !$#accession A60903 !'##molecule_type mRNA !'##residues 351-676 ##label PLO REFERENCE S02424 !$#authors Ploos van Amstel, H.K.; van der Zanden, A.L.; Reitsma, P.H.; !1Bertina, R.M. !$#journal FEBS Lett. (1987) 222:186-190 !$#title Human protein S cDNA encodes Phe-16 and Tyr 222 in consensus !1sequences for the posttranslational processing. !$#cross-references MUID:88005138; PMID:2820795 !$#accession S02424 !'##molecule_type mRNA !'##residues 1-676 ##label PL2 !'##cross-references EMBL:Y00692; NID:g36578; PIDN:CAA68687.1; !1PID:g36579 GENETICS !$#gene GDB:PROS1; PROS !'##cross-references GDB:120721; OMIM:176880 !$#map_position 3p11.1-3q11.2 !$#introns 26/1; 78/3; 87/1; 116/1; 157/1; 201/1; 243/1; 283/3; 322/2; !1385/3; 441/3; 498/1; 548/3; 624/1 COMPLEX in plasma forms a complex with C4b binding protein FUNCTION !$#description a cofactor for activated protein C (EC 3.4.21.69); thrombin !1cleavage destroys the cofactor activity of plasma protein S CLASSIFICATION #superfamily plasma protein S; EGF homology; Gla domain !1homology; laminin G repeat homology; sex hormone-binding !1globulin homology KEYWORDS beta-hydroxyasparagine; beta-hydroxyaspartic acid; blood !1coagulation; carboxyglutamic acid; glycoprotein; vitamin K FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-41 #domain propeptide #status predicted #label PRO\ !$26-85 #domain Gla domain homology #label GLA\ !$42-676 #product plasma protein S #status predicted #label !8MAT\ !$121-154 #domain EGF homology #label EG1\ !$161-199 #domain EGF homology #label EG2\ !$205-241 #domain EGF homology #label EG3\ !$247-282 #domain EGF homology #label EG4\ !$315-667 #domain sex hormone-binding globulin homology #label !8SHB\ !$325-478 #domain laminin G repeat homology #label LGR\ !$47,48,55,57,60,61, !$66,67,70,73,77 #modified_site gamma-carboxyglutamic acid (Glu) !8#status predicted\ !$58-63,88-113, !$121-134,126-143, !$145-154,161-175, !$171-184,186-199, !$205-217,212-226, !$228-241,247-256, !$252-265,267-282, !$288-568,449-475, !$639-666 #disulfide_bonds #status predicted\ !$111-112 #cleavage_site Arg-Ser (thrombin) #status predicted\ !$136 #modified_site erythro-beta-hydroxyaspartic acid !8(Asp) #status predicted\ !$177,219,258 #modified_site erythro-beta-hydroxyasparagine (Asn) !8#status predicted\ !$499,509,530 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 676 #molecular-weight 75122 #checksum 5771 SEQUENCE /// ENTRY KXBOS #type complete TITLE plasma protein S precursor - bovine ALTERNATE_NAMES vitamin K-dependent protein S ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 08-Aug-1987 #sequence_revision 26-Jan-1996 #text_change 16-Jul-1999 ACCESSIONS A24759; A23888 REFERENCE A24759 !$#authors Dahlback, B.; Lundwall, A.; Stenflo, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:4199-4203 !$#title Primary structure of bovine vitamin K-dependent protein S. !$#cross-references MUID:86233400; PMID:2940598 !$#accession A24759 !'##molecule_type mRNA !'##residues 1-675 ##label DAH !'##cross-references GB:M13044; NID:g163697; PIDN:AAA30757.1; !1PID:g163698 !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing REFERENCE A23888 !$#authors Dahlback, B.; Lundwall, A.; Stenflo, J. !$#journal J. Biol. Chem. (1986) 261:5111-5115 !$#title Localization of thrombin cleavage sites in the !1amino-terminal region of bovine protein S. !$#cross-references MUID:86168236; PMID:2937785 !$#accession A23888 !'##molecule_type protein !'##residues 42-141 ##label DA2 COMPLEX in plasma forms a complex with C4b binding protein FUNCTION !$#description a cofactor for activated protein C (EC 3.4.21.69); thrombin !1cleavage destroys the cofactor activity of plasma protein S CLASSIFICATION #superfamily plasma protein S; EGF homology; Gla domain !1homology; laminin G repeat homology; sex hormone-binding !1globulin homology KEYWORDS beta-hydroxyasparagine; beta-hydroxyaspartic acid; blood !1coagulation; carboxyglutamic acid; glycoprotein; vitamin K FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-41 #domain propeptide #status predicted #label PRO\ !$26-85 #domain Gla domain homology #label GLA\ !$42-675 #product plasma protein S #status experimental #label !8MAT\ !$121-154 #domain EGF homology #label EG1\ !$161-199 #domain EGF homology #label EG2\ !$205-241 #domain EGF homology #label EG3\ !$247-282 #domain EGF homology #label EG4\ !$315-666 #domain sex hormone-binding globulin homology #label !8SHB\ !$325-478 #domain laminin G repeat homology #label LGR\ !$47,48,55,57,60,61, !$66,67,70,73,77 #modified_site gamma-carboxyglutamic acid (Glu) !8#status experimental\ !$58-63,88-113, !$121-134,126-143, !$145-154,161-175, !$171-184,186-199, !$205-217,212-226, !$228-241,247-256, !$252-265,267-282 #disulfide_bonds #status predicted\ !$93-94 #cleavage_site Arg-Ala (thrombin) #status !8experimental\ !$111-112 #cleavage_site Arg-Ser (thrombin) #status !8experimental\ !$136 #modified_site erythro-beta-hydroxyaspartic acid !8(Asp) #status experimental\ !$177,219,258 #modified_site erythro-beta-hydroxyasparagine (Asn) !8#status experimental\ !$288-567,449-475, !$638-665 #disulfide_bonds #status experimental\ !$499 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$509 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 675 #molecular-weight 75132 #checksum 9382 SEQUENCE /// ENTRY KXMSS #type complete TITLE plasma protein S precursor - mouse ALTERNATE_NAMES vitamin K-dependent glycoprotein S ORGANISM #formal_name Mus musculus #common_name house mouse DATE 13-Jan-1995 #sequence_revision 26-Jan-1996 #text_change 16-Jul-1999 ACCESSIONS S43504; I59616; S35962 REFERENCE S43504 !$#authors Chu, M.D.; Sun, J.; Bird, P. !$#journal Biochim. Biophys. Acta (1994) 1217:325-328 !$#title Cloning and sequencing of a cDNA encoding the murine vitamin !1K-dependent protein S. !$#cross-references MUID:94198297; PMID:8148380 !$#accession S43504 !'##molecule_type mRNA !'##residues 1-675 ##label CHU !'##cross-references EMBL:Z25469; NID:g396426; PIDN:CAA80961.1; !1PID:g396427 REFERENCE I59616 !$#authors Lu, D.; Schmidel, D.K.; Long, G.L. !$#journal Thromb. Res. (1994) 74:135-142 !$#title Structure of mouse protein S as determined by PCR !1amplification and DNA sequencing of cDNA. !$#cross-references MUID:94302659; PMID:8029814 !$#accession I59616 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 33-492,'L',494-675 ##label RES !'##cross-references GB:L27439; NID:g487866; PIDN:AAA40006.1; !1PID:g487867 COMPLEX in plasma forms a complex with C4b binding protein FUNCTION !$#description a cofactor for activated protein C (EC 3.4.21.69); thrombin !1cleavage destroys the cofactor activity of plasma protein S CLASSIFICATION #superfamily plasma protein S; EGF homology; Gla domain !1homology; laminin G repeat homology; sex hormone-binding !1globulin homology KEYWORDS beta-hydroxyasparagine; beta-hydroxyaspartic acid; blood !1coagulation; carboxyglutamic acid; glycoprotein; vitamin K FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-41 #domain propeptide #status predicted #label PRO\ !$26-85 #domain Gla domain homology #label GLA\ !$42-675 #product plasma protein S #status predicted #label !8MAT\ !$121-154 #domain EGF homology #label EG1\ !$161-199 #domain EGF homology #label EG2\ !$205-241 #domain EGF homology #label EG3\ !$247-282 #domain EGF homology #label EG4\ !$315-666 #domain sex hormone-binding globulin homology #label !8SHB\ !$325-478 #domain laminin G repeat homology #label LGR\ !$47,48,55,57,60,61, !$66,67,70,73,77 #modified_site gamma-carboxyglutamic acid (Glu) !8#status predicted\ !$58-63,88-113, !$121-134,126-143, !$145-154,161-175, !$171-184,186-199, !$205-217,212-226, !$228-241,247-256, !$252-265,267-282, !$288-567,449-475, !$638-665 #disulfide_bonds #status predicted\ !$111-112 #cleavage_site Arg-Ser (thrombin) #status predicted\ !$136 #modified_site erythro-beta-hydroxyaspartic acid !8(Asp) #status predicted\ !$177,219,258 #modified_site erythro-beta-hydroxyasparagine (Asn) !8#status predicted\ !$499,509 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 675 #molecular-weight 74934 #checksum 7404 SEQUENCE /// ENTRY KXRTS #type complete TITLE plasma protein S precursor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 04-Oct-1995 #sequence_revision 26-Jan-1996 #text_change 16-Jul-1999 ACCESSIONS JC4180 REFERENCE JC4180 !$#authors Yasuda, F.; Hayashi, T.; Tanitame, K.; Nishioka, J.; Suzuki, !1K. !$#journal J. Biochem. (1995) 117:374-383 !$#title Molecular cloning and functional characterization of rat !1plasma protein S. !$#cross-references MUID:95332263; PMID:7608128 !$#accession JC4180 !'##molecule_type mRNA !'##residues 1-675 ##label YAS !'##cross-references GB:S78744; NID:g1041903; PIDN:AAC60704.1; !1PID:g1041904 COMMENT This protein is a vitamin K-dependent plasma glycoprotein !1that has an anticoagulant activity in the blood coagulation !1system by acting as a cofactor in the activated protein !1C-catalyzed inactivation of coagulation factors Va and !1VIIIa. This protein also binds to factor Va and Xa. CLASSIFICATION #superfamily plasma protein S; EGF homology; Gla domain !1homology; laminin G repeat homology; sex hormone-binding !1globulin homology KEYWORDS beta-hydroxyasparagine; beta-hydroxyaspartic acid; blood !1coagulation; carboxyglutamic acid; glycoprotein; vitamin K FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-41 #domain propeptide #status predicted #label PRO\ !$26-85 #domain Gla domain homology #label GLA\ !$42-675 #product plasma protein S #status predicted #label !8MAT\ !$88-116 #domain thrombin-sensitive #status predicted #label !8THS\ !$121-154 #domain EGF homology #label EG1\ !$161-199 #domain EGF homology #label EG2\ !$205-241 #domain EGF homology #label EG3\ !$247-282 #domain EGF homology #label EG4\ !$315-666 #domain sex hormone-binding globulin homology #label !8SHB\ !$325-478 #domain laminin G repeat homology #label LGR\ !$47,48,55,57,60,61, !$66,67,70,73,77 #modified_site gamma-carboxyglutamic acid (Glu) !8#status predicted\ !$58-63,88-113, !$121-134,126-143, !$145-154,161-175, !$171-184,186-199, !$205-217,212-226, !$228-241,247-256, !$252-265,267-282, !$288-567,449-475, !$638-665 #disulfide_bonds #status predicted\ !$111-112 #cleavage_site Arg-Ser (thrombin) #status predicted\ !$136 #modified_site erythro-beta-hydroxyaspartic acid !8(Asp) #status predicted\ !$177,219,258 #modified_site erythro-beta-hydroxyasparagine (Asn) !8#status predicted\ !$499,509 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 675 #molecular-weight 74626 #checksum 5581 SEQUENCE /// ENTRY A34702 #type complete TITLE amphiregulin precursor [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 08-Dec-2000 ACCESSIONS A34702; B34702; A30057; A31230; A39788; A30056 REFERENCE A34702 !$#authors Plowman, G.D.; Green, J.M.; McDonald, V.L.; Neubauer, M.G.; !1Disteche, C.M.; Todaro, G.J.; Shoyab, M. !$#journal Mol. Cell. Biol. (1990) 10:1969-1981 !$#title The amphiregulin gene encodes a novel epidermal growth !1factor-related protein with tumor-inhibitory activity. !$#cross-references MUID:90220581; PMID:2325643 !$#accession A34702 !'##molecule_type DNA !'##residues 1-252 ##label PL1 !'##cross-references GB:M30698 !$#accession B34702 !'##molecule_type mRNA !'##residues 1-252 ##label PL2 !'##cross-references GB:M30704; NID:g179039; PIDN:AAA51781.1; !1PID:g179040 REFERENCE A30057 !$#authors Shoyab, M.; Plowman, G.D.; McDonald, V.L.; Bradley, J.G.; !1Todaro, G.J. !$#journal Science (1989) 243:1074-1076 !$#title Structure and function of human amphiregulin: a member of !1the epidermal growth factor family. !$#cross-references MUID:89162036; PMID:2466334 !$#accession A30057 !'##molecule_type protein !'##residues 101-112,'D',114-184 ##label SH1 REFERENCE A94205 !$#authors Shoyab, M.; McDonald, V.L.; Bradley, J.G.; Todaro, G.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:6528-6532 !$#title Amphiregulin: a bifunctional growth-modulating glycoprotein !1produced by the phorbol 12-myristate 13-acetate-treated !1human breast adenocarcinoma cell line MCF-7. !$#cross-references MUID:88320474; PMID:3413110 !$#accession A31230 !'##molecule_type protein !'##residues 101-112,'D',114-131 ##label SH2 REFERENCE A39788 !$#authors Cook, P.W.; Mattox, P.A.; Keeble, W.W.; Pittelkow, M.R.; !1Plowman, G.D.; Shoyab, M.; Adelman, J.P.; Shipley, G.D. !$#journal Mol. Cell. Biol. (1991) 11:2547-2557 !$#title A heparin sulfate-regulated human keratinocyte autocrine !1factor is similar or identical to amphiregulin. !$#cross-references MUID:91203875; PMID:2017164 !$#accession A39788 !'##molecule_type protein !'##residues 101-126 ##label COO COMMENT Amphiregulin is a secreted protein that is released from the !1transmembrane precursor by proteolytic cleavage. GENETICS !$#gene GDB:AREG !'##cross-references GDB:119697; OMIM:104640 !$#map_position 4q13-4q21 !$#introns 21/1; 104/1; 171/1; 222/2 CLASSIFICATION #superfamily amphiregulin; EGF homology KEYWORDS extracellular protein; glycoprotein; growth factor; !1transmembrane protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-100 #domain propeptide #status predicted #label PRO\ !$101-184 #product amphiregulin long form #status experimental !8#label MAL\ !$107-184 #product amphiregulin short form #status experimental !8#label MAS\ !$146-181 #domain EGF homology #label EGF\ !$199-221 #domain transmembrane #status predicted #label TM1\ !$222-252 #domain intracellular #status predicted #label INT\ !$30,113,119 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$146-159,154-170, !$172-181 #disulfide_bonds #status predicted SUMMARY #length 252 #molecular-weight 27895 #checksum 7174 SEQUENCE /// ENTRY JH0612 #type complete TITLE amphiregulin precursor - mouse ALTERNATE_NAMES Schwannoma-derived growth factor precursor ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jun-2000 ACCESSIONS JH0612; A56830 REFERENCE JH0612 !$#authors Sonoda, H.; Yamaguchi, T.; Watanabe, S. !$#journal Biochem. Biophys. Res. Commun. (1992) 185:103-109 !$#title Androgen-responsive expression and mitogenic activity of !1schwannoma-derived growth factor on an androgen-dependent !1Shionogi mouse mammary carcinoma cell line. !$#cross-references MUID:92287078; PMID:1318038 !$#accession JH0612 !'##molecule_type mRNA !'##residues 1-248 ##label SON !'##cross-references GB:D12648; DDBJ:D01182; NID:g220599; !1PIDN:BAA02169.1; PID:g220600 !'##experimental_source SC2G cell REFERENCE A56830 !$#authors Das, S.K.; Chakraborty, I.; Paria, B.C.; Wang, X.N.; !1Plowman, G.; Dey, S.K. !$#journal Mol. Endocrinol. (1995) 9:691-705 !$#title Amphiregulin is an implantation-specific and !1progesterone-regulated gene in the mouse uterus. !$#cross-references MUID:96174905; PMID:8592515 !$#accession A56830 !'##molecule_type mRNA !'##residues 1-248 ##label DAS !'##cross-references GB:L41352; NID:g845598; PIDN:AAB00472.1; !1PID:g845599 !'##note authors translated the codon CCA for residue 84 as Glu COMMENT Amphiregulin is a secreted protein that is released from the !1transmembrane precursor by proteolytic cleavage. CLASSIFICATION #superfamily amphiregulin; EGF homology KEYWORDS extracellular protein; glycoprotein; growth factor; !1transmembrane protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-93 #domain propeptide #status predicted #label PRO\ !$94-177 #product amphiregulin long form #status predicted !8#label MAL\ !$100-177 #product amphiregulin short form #status predicted !8#label MAS\ !$139-174 #domain EGF homology #label EGF\ !$192-217 #domain transmembrane #status predicted #label TM1\ !$218-248 #domain intracellular #status predicted #label INT\ !$106 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$139-152,147-163, !$165-174 #disulfide_bonds #status predicted SUMMARY #length 248 #molecular-weight 27549 #checksum 8496 SEQUENCE /// ENTRY EGHU #type complete TITLE epidermal growth factor precursor [validated] - human ALTERNATE_NAMES urogastrone precursor ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Nov-1980 #sequence_revision 14-Aug-1998 #text_change 08-Dec-2000 ACCESSIONS A25531; A01388; A33517; A29721; S45282; S45283 REFERENCE A25531 !$#authors Bell, G.I.; Fong, N.M.; Stempien, M.M.; Wormsted, M.A.; !1Caput, D.; Ku, L.; Urdea, M.S.; Rall, L.B.; !1Sanchez-Pescador, R. !$#journal Nucleic Acids Res. (1986) 14:8427-8446 !$#title Human epidermal growth factor precursor: cDNA sequence, !1expression in vitro and gene organization. !$#cross-references MUID:87066721; PMID:3491360 !$#accession A25531 !'##molecule_type mRNA !'##residues 1-1207 ##label BEL !'##cross-references EMBL:X04571; NID:g31120; PIDN:CAA28240.1; !1PID:g31121 !'##note 708-Met was also found !'##note intron positions were also determined REFERENCE A01388 !$#authors Gregory, H.; Preston, B.M. !$#journal Int. J. Pept. Protein Res. (1977) 9:107-118 !$#title The primary structure of human urogastrone. !$#cross-references MUID:77117897; PMID:300079 !$#accession A01388 !'##molecule_type protein !'##residues 971-1023 ##label GRE !'##note some of the molecules lack Arg-1023 REFERENCE A33517 !$#authors Furuya, M.; Akashi, S.; Hirayama, K. !$#journal Biochem. Biophys. Res. Commun. (1989) 163:1100-1106 !$#title The primary structure of human EGF produced by genetic !1engineering, studied by high-performance tandem mass !1spectrometry. !$#cross-references MUID:89391964; PMID:2789514 !$#accession A33517 !'##molecule_type protein !'##residues 971-1023 ##label FUR REFERENCE A29721 !$#authors Tsukumo, K.; Nakamura, H.; Sakamoto, S. !$#journal Biochem. Biophys. Res. Commun. (1987) 145:126-133 !$#title Purification and characterization of high molecular weight !1human epidermal growth factor from human urine. !$#cross-references MUID:87241488; PMID:3297054 !$#accession A29721 !'##molecule_type protein !'##residues 829-834,'X',836-839,'X',841-845,'X',847-848 ##label TSU !'##note this is the amino-terminal sequence of a high molecular weight !1form of EGF, isolated from urine, from which EGF can be !1released in vitro REFERENCE S45282 !$#authors Svoboda, M.; Bauhofer, A.; Schwind, P.; Bade, E.; Rasched, !1I.; Przybylski, M. !$#journal Biochim. Biophys. Acta (1994) 1206:35-41 !$#title Structural characterization and biological activity of !1recombinant human epidermal growth factor proteins with !1different N-terminal sequences. !$#cross-references MUID:94242778; PMID:8186248 !$#accession S45282 !'##molecule_type protein !'##residues 'M',971-1023 ##label SVO !'##note expressed recombinant protein !$#accession S45283 !'##molecule_type protein !'##residues 'MKKYP',970-1023 ##label SV2 !'##note expressed recombinant protein COMMENT Epidermal growth factor (EGF) stimulates the proliferation !1and differentiation of skin and some other epithelial !1tissues. It also inhibits gastric acid and pepsin secretion !1and stimulates gastrointestinal cell proliferation. COMMENT EGF is released in the pancreas, small intestine, mammary !1gland, and (in some species) submaxillary gland. COMMENT The EGF precursor is found in kidney as a receptor-like !1membrane-bound protein. GENETICS !$#gene GDB:EGF !'##cross-references GDB:119105; OMIM:131530 !$#map_position 4q25-4q25 !$#introns 43/1; 109/3; 170/2; 246/2; 314/1; 356/3; 397/1; 438/1; 480/ !11; 525/3; 575/2; 610/2; 685/1; 741/1; 791/3; 831/1; 870/1; !1912/1; 953/1; 1002/2; 1058/2; 1097/3; 1124/1 CLASSIFICATION #superfamily epidermal growth factor precursor; EGF !1homology; LDL receptor YWTD-containing repeat homology KEYWORDS duplication; growth factor; tandem repeat; transmembrane !1protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-1207 #product epidermal growth factor proprotein, !8membrane-bound form #status predicted #label PRE\ !$23-1032 #domain extracellular #status predicted #label EXT\ !$43-479 #region EGF precursor long repeat #label LR1\ !$46-85 #domain LDL receptor YWTD-containing repeat homology !8#label YW01\ !$86-127 #domain LDL receptor YWTD-containing repeat homology !8#label YW02\ !$128-169 #domain LDL receptor YWTD-containing repeat homology !8#label YW03\ !$170-211 #domain LDL receptor YWTD-containing repeat homology !8#label YW04\ !$212-256 #domain LDL receptor YWTD-containing repeat homology !8#label YW05\ !$257-301 #domain LDL receptor YWTD-containing repeat homology !8#label YW06\ !$318-354 #domain EGF homology #label EG1\ !$360-395 #domain EGF homology #label EG2\ !$401-436 #domain EGF homology #label EG3\ !$439-476 #domain EGF homology #label EG4\ !$480-954 #region EGF precursor long repeat #label LR2\ !$483-523 #domain LDL receptor YWTD-containing repeat homology !8#label YW07\ !$524-566 #domain LDL receptor YWTD-containing repeat homology !8#label YW08\ !$567-609 #domain LDL receptor YWTD-containing repeat homology !8#label YW09\ !$610-653 #domain LDL receptor YWTD-containing repeat homology !8#label YW10\ !$654-694 #domain LDL receptor YWTD-containing repeat homology !8#label YW11\ !$695-737 #domain LDL receptor YWTD-containing repeat homology !8#label YW12\ !$745-780 #domain EGF homology #label EG5\ !$835-868 #domain EGF homology #label EG6\ !$874-910 #domain EGF homology #label EG7\ !$916-951 #domain EGF homology #label EG8\ !$971-1023 #product epidermal growth factor #status experimental !8#label EGF\ !$976-1012 #domain EGF homology #label EG9\ !$1033-1057 #domain transmembrane #status predicted #label TMM\ !$1058-1207 #domain intracellular #status predicted #label INT\ !$318-330,325-339, !$341-354,360-371, !$367-380,382-395, !$401-412,408-421, !$423-436,439-451, !$447-461,463-476, !$745-756,752-765, !$767-780,835-846, !$840-855,857-868, !$874-888,881-897, !$899-910,916-929, !$923-938,940-951 #disulfide_bonds #status predicted\ !$976-990,984-1001, !$1003-1012 #disulfide_bonds #status experimental SUMMARY #length 1207 #molecular-weight 133945 #checksum 2144 SEQUENCE /// ENTRY EGMSMG #type complete TITLE epidermal growth factor precursor - mouse ALTERNATE_NAMES urogastrone precursor ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Nov-1980 #sequence_revision 11-Aug-1983 #text_change 19-Jan-2001 ACCESSIONS A94272; A93304; A92118; A01387 REFERENCE A94272 !$#authors Scott, J.; Urdea, M.; Quiroga, M.; Sanchez-Pescador, R.; !1Fong, N.; Selby, M.; Rutter, W.J.; Bell, G.I. !$#journal Science (1983) 221:236-240 !$#title Structure of a mouse submaxillary messenger RNA encoding !1epidermal growth factor and seven related proteins. !$#cross-references MUID:83223630; PMID:6602382 !$#accession A94272 !'##molecule_type mRNA !'##residues 1-1217 ##label SCO !'##cross-references GB:J00380; NID:g192993; PIDN:AAA37539.1; !1PID:g309210 REFERENCE A93304 !$#authors Gray, A.; Dull, T.; Ullrich, A. !$#journal Nature (1983) 303:722-725 !$#title Nucleotide sequence of epidermal growth factor cDNA predicts !1a 128,000-molecular weight protein precursor. !$#cross-references MUID:83219309; PMID:6304537 !$#accession A93304 !'##molecule_type mRNA !'##residues 1-789,'Y',791-1047,'S',1049-1168 ##label GRA !'##cross-references GB:J00380 !'##note the sequence shown by these authors differs from residues !11134-1168 due to an insertion of one base in the nucleotide !1sequence; (we translated this region in the same reading !1frame as the sequence of Scott et al.) REFERENCE A92118 !$#authors Savage Jr., C.R.; Inagami, T.; Cohen, S. !$#journal J. Biol. Chem. (1972) 247:7612-7621 !$#title The primary structure of epidermal growth factor. !$#cross-references MUID:73048516; PMID:4636327 !$#accession A92118 !'##molecule_type protein !'##residues 977-1029 ##label SAV !'##note residues 1024-1029 are not required for full biological !1activity in vivo REFERENCE A92144 !$#authors Savage Jr., C.R.; Hash, J.H.; Cohen, S. !$#journal J. Biol. Chem. (1973) 248:7669-7672 !$#title Epidermal growth factor. Location of disulfide bonds. !$#cross-references MUID:74025498; PMID:4750422 !$#contents annotation; disulfide bonds COMMENT Epidermal growth factor (EGF) stimulates the proliferation !1and differentiation of skin and some other epithelial !1tissues. It also inhibits gastric acid and pepsin secretion !1and stimulates gastrointestinal cell proliferation. COMMENT EGF is released in the pancreas, small intestine, mammary !1gland, and (in some species) submaxillary gland. COMMENT The EGF precursor is found in kidney as a receptor-like !1membrane-bound protein. COMMENT The active growth factor from this submaxillary gland !1protein stimulates the growth of various epidermal and !1epithelial tissues in vivo and in vitro and of some !1fibroblasts in cell culture. CLASSIFICATION #superfamily epidermal growth factor precursor; EGF !1homology; LDL receptor YWTD-containing repeat homology KEYWORDS duplication; growth factor; tandem repeat; transmembrane !1protein FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-1217 #product epidermal growth factor proprotein, !8membrane-bound form #status predicted #label PRE\ !$29-1038 #domain extracellular #status predicted #label EXT\ !$50-485 #region EGF precursor long repeat\ !$53-92 #domain LDL receptor YWTD-containing repeat homology !8#label YW01\ !$93-134 #domain LDL receptor YWTD-containing repeat homology !8#label YW02\ !$135-176 #domain LDL receptor YWTD-containing repeat homology !8#label YW03\ !$177-217 #domain LDL receptor YWTD-containing repeat homology !8#label YW04\ !$218-262 #domain LDL receptor YWTD-containing repeat homology !8#label YW05\ !$263-307 #domain LDL receptor YWTD-containing repeat homology !8#label YW06\ !$324-360 #domain EGF homology #status atypical #label EG1\ !$366-401 #domain EGF homology #label EG2\ !$407-442 #domain EGF homology #label EG3\ !$445-482 #domain EGF homology #label EG4\ !$486-961 #region EGF precursor long repeat\ !$489-529 #domain LDL receptor YWTD-containing repeat homology !8#label YW07\ !$530-572 #domain LDL receptor YWTD-containing repeat homology !8#label YW08\ !$573-615 #domain LDL receptor YWTD-containing repeat homology !8#label YW09\ !$616-659 #domain LDL receptor YWTD-containing repeat homology !8#label YW10\ !$660-700 #domain LDL receptor YWTD-containing repeat homology !8#label YW11\ !$701-743 #domain LDL receptor YWTD-containing repeat homology !8#label YW12\ !$751-786 #domain EGF homology #label EG5\ !$842-875 #domain EGF homology #label EG6\ !$881-917 #domain EGF homology #label EG7\ !$923-958 #domain EGF homology #label EG8\ !$977-1029 #product epidermal growth factor #status experimental !8#label EGF\ !$982-1018 #domain EGF homology #label EG9\ !$1039-1063 #domain transmembrane #status predicted #label TMM\ !$1064-1217 #domain intracellular #status predicted #label INT\ !$347-360,366-377, !$373-386,388-401, !$407-418,414-427, !$429-442,445-457, !$453-467,469-482, !$751-762,758-771, !$773-786,842-853, !$847-862,864-875, !$881-895,888-904, !$906-917,923-936, !$930-945,947-958 #disulfide_bonds #status predicted\ !$982-996,990-1007, !$1009-1018 #disulfide_bonds #status experimental SUMMARY #length 1217 #molecular-weight 133143 #checksum 9280 SEQUENCE /// ENTRY EGRT #type complete TITLE epidermal growth factor precursor - rat ALTERNATE_NAMES urogastrone precursor ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1988 #sequence_revision 14-Aug-1998 #text_change 18-Jun-1999 ACCESSIONS I52995; S05074; S01974; A25425; S18419; S08288 REFERENCE I52995 !$#authors Saggi, S.J.; Safirstein, R.; Price, P.M. !$#journal DNA Cell Biol. (1992) 11:481-487 !$#title Cloning and Sequencing of the Rat Preproepidermal Growth !1Factor cDNA: Comparison with Mouse and Human Sequences. !$#cross-references MUID:92398779; PMID:1524680 !$#accession I52995 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-1133 ##label RES !'##cross-references EMBL:U04842; NID:g440236; PIDN:AAB60436.1; !1PID:g440237 REFERENCE S05074 !$#authors Simpson, R. !$#submission submitted to the EMBL Data Library, August 1988 !$#accession S05074 !'##molecule_type mRNA !'##residues 'W',966,'RWL',970-1023,'NW',1026-1108,'SGAGVSSGPQPWFVVLE', !11126,'HQ' ##label SIM !'##cross-references EMBL:X12748 REFERENCE S01974 !$#authors Dorow, D.S.; Simpson, R.J. !$#journal Nucleic Acids Res. (1988) 16:9338 !$#title Cloning and sequence analysis of a cDNA for rat epidermal !1growth factor. !$#cross-references MUID:89016634; PMID:3262867 !$#accession S01974 !'##molecule_type mRNA !'##residues 'W',966,'RWL',970-1023,'NW',1026-1108 ##label DOR !'##cross-references EMBL:X12748 REFERENCE A25425 !$#authors Simpson, R.J.; Smith, J.A.; Moritz, R.L.; O'Hare, M.J.; !1Rudland, P.S.; Morrison, J.R.; Lloyd, C.J.; Grego, B.; !1Burgess, A.W.; Nice, E.C. !$#journal Eur. J. Biochem. (1985) 153:629-637 !$#title Rat epidermal growth factor: complete amino acid sequence. !$#cross-references MUID:86081810; PMID:3000782 !$#accession A25425 !'##molecule_type protein !'##residues 974-1021 ##label SI2 REFERENCE S18419 !$#authors Nishi, N.; Shimizu, C.; Okutani, T.; Kagawa, Y.; Takasuga, !1H.; Suno, M.; Wada, F. !$#journal Biochim. Biophys. Acta (1991) 1095:268-275 !$#title Rat prostatic growth factors: purification and !1characterization of high and low molecular weight epidermal !1growth factors from rat dorsolateral prostate. !$#cross-references MUID:92069070; PMID:1958699 !$#accession S18419 !'##status preliminary !'##molecule_type protein !'##residues 974-1021 ##label NIS REFERENCE S08288 !$#authors Nexo, E.; Jorgensen, P.E.; Thim, L.; Roepstorff, P. !$#journal Biochim. Biophys. Acta (1990) 1037:388-393 !$#title Purification and characterization of a low and a high !1molecular weight form of epidermal growth factor from rat !1urine. !$#cross-references MUID:90181442; PMID:2310752 !$#accession S08288 !'##molecule_type protein !'##residues 974-1024 ##label NEX COMMENT Epidermal growth factor (EGF) stimulates the proliferation !1and differentiation of skin and some other epithelial !1tissues. It also inhibits gastric acid and pepsin secretion !1and stimulates gastrointestinal cell proliferation. COMMENT EGF is released in the pancreas, small intestine, mammary !1gland, and (in some species) submaxillary gland. COMMENT The EGF precursor is found in kidney as a receptor-like !1membrane-bound protein. CLASSIFICATION #superfamily epidermal growth factor precursor; EGF !1homology; LDL receptor YWTD-containing repeat homology KEYWORDS duplication; growth factor; mitogen; tandem repeat; !1transmembrane protein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-1133 #product epidermal growth factor proprotein, !8membrane-bound form #status predicted #label PRE\ !$22-1035 #domain extracellular #status predicted #label EXT\ !$44-480 #region EGF precursor long repeat #label LR1\ !$47-86 #domain LDL receptor YWTD-containing repeat homology !8#label YW01\ !$87-128 #domain LDL receptor YWTD-containing repeat homology !8#label YW02\ !$129-170 #domain LDL receptor YWTD-containing repeat homology !8#label YW03\ !$171-212 #domain LDL receptor YWTD-containing repeat homology !8#label YW04\ !$213-257 #domain LDL receptor YWTD-containing repeat homology !8#label YW05\ !$258-302 #domain LDL receptor YWTD-containing repeat homology !8#label YW06\ !$319-355 #domain EGF homology #status atypical #label EG1\ !$361-396 #domain EGF homology #label EG2\ !$402-437 #domain EGF homology #label EG3\ !$440-477 #domain EGF homology #label EG4\ !$482-958 #region EGF precursor long repeat #label LR2\ !$485-525 #domain LDL receptor YWTD-containing repeat homology !8#label YW07\ !$526-568 #domain LDL receptor YWTD-containing repeat homology !8#label YW08\ !$569-611 #domain LDL receptor YWTD-containing repeat homology !8#label YW09\ !$612-655 #domain LDL receptor YWTD-containing repeat homology !8#label YW10\ !$656-696 #domain LDL receptor YWTD-containing repeat homology !8#label YW11\ !$697-739 #domain LDL receptor YWTD-containing repeat homology !8#label YW12\ !$747-782 #domain EGF homology #label EG5\ !$839-872 #domain EGF homology #label EG6\ !$878-914 #domain EGF homology #label EG7\ !$920-955 #domain EGF homology #label EG8\ !$974-1024 #product epidermal growth factor #status experimental !8#label MAT\ !$979-1015 #domain EGF homology #label EG9\ !$1036-1060 #domain transmembrane #status predicted #label TMM\ !$1061-1133 #domain intracellular #status predicted #label INT\ !$342-355,361-372, !$368-381,383-396, !$402-413,409-422, !$424-437,440-452, !$448-462,464-477, !$747-758,754-767, !$769-782,839-850, !$844-859,861-872, !$878-892,885-901, !$903-914,920-933, !$927-942,944-955, !$979-993,987-1004, !$1006-1015 #disulfide_bonds #status predicted SUMMARY #length 1133 #molecular-weight 124125 #checksum 1478 SEQUENCE /// ENTRY WFRT1 #type complete TITLE transforming growth factor alpha precursor - rat ALTERNATE_NAMES EGF-like TGF; eTGF; TGF type 1; TGF-alpha ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 15-Nov-1984 #sequence_revision 30-Oct-1998 #text_change 18-Jun-1999 ACCESSIONS A93356; B93356; I77379; A94273; B94273; A92405; B92405; !1A01389; A05285; A21639 REFERENCE A93356 !$#authors Lee, D.C.; Rose, T.M.; Webb, N.R.; Todaro, G.J. !$#journal Nature (1985) 313:489-491 !$#title Cloning and sequence analysis of a cDNA for rat transforming !1growth factor-alpha. !$#cross-references MUID:85111164; PMID:3855503 !$#accession A93356 !'##molecule_type mRNA !'##residues 'PGRRGRPSARAPGAGPVACAFFPRAHRGGARHSPTAKSAVAAAPCARK',1-159 !1##label LEE1 !'##cross-references GB:X02004; NID:g57337 !'##note the size of the initial translation product was not known; !1homology with the human TGF-alpha sequence indicated Met-1 !1as the initiator !$#accession B93356 !'##molecule_type mRNA !'##residues 1-159 ##label LEE2 !'##cross-references GB:X02004; NID:g57337; PIDN:CAA26036.1; PID:g57338 REFERENCE I57497 !$#authors Blasband, A.J.; Rogers, K.T.; Chen, X.; Azizkhan, J.C.; Lee, !1D.C. !$#journal Mol. Cell. Biol. (1990) 10:2111-2121 !$#title Characterization of the rat transforming growth factor alpha !1gene and identification of promoter sequences. !$#cross-references MUID:90220597; PMID:2325647 !$#accession I77379 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-13 ##label BLA !'##cross-references GB:M31075; NID:g207283; PIDN:AAA42234.1; !1PID:g554526 !'##note Met-1 shown to be the initiator REFERENCE A94273 !$#authors Marquardt, H.; Hunkapiller, M.W.; Hood, L.E.; Todaro, G.J. !$#journal Science (1984) 223:1079-1082 !$#title Rat transforming growth factor type 1: structure and !1relation to epidermal growth factor. !$#cross-references MUID:84121322; PMID:6320373 !$#accession A94273 !'##molecule_type protein !'##residues 39-88 ##label MAR1 !$#accession B94273 !'##molecule_type protein !'##residues 39-88 ##label MAR2 REFERENCE A92405 !$#authors Massague, J. !$#journal J. Biol. Chem. (1983) 258:13606-13613 !$#title Epidermal growth factor-like transforming growth factor. I. !1Isolation, chemical characterization, and potentiation by !1other transforming factors from feline sarcoma !1virus-transformed rat cells. !$#cross-references MUID:84061765; PMID:6605968 !$#accession A92405 !'##molecule_type protein !'##residues 39-67 ##label MAS1 !$#accession B92405 !'##molecule_type protein !'##residues 39-67 ##label MAS2 COMMENT TGF alpha is a mitogenic polypeptide that is able to bind to !1the EGF receptor and to act synergistically with TGF beta to !1promote anchorage-independent cell proliferation in soft !1agar. Its mRNA is found in transformed cells and, at lower !1concentrations, in normal rat kidney, liver, and brain !1tissue, and its sequence suggests that it is derived from a !1transmembrane precursor having biologically active !1polypeptides on both sides of the membrane. COMMENT Both hydrophobic regions of this precursor are associated !1with pairs of basic residues, recognition sites for !1proteolysis, and release of active peptides; however, !1cleavage of TGF alpha from this precursor requires a !1protease specific for alanine-valine bonds. COMMENT This polypeptide is produced by transformed cells. It is !1able to bind to normal EGF receptor and could have a role in !1growth of neoplastic cells. COMMENT Type I and type II transforming growth factors act !1synergistically to promote anchorage-independent cell !1proliferation in soft agar. CLASSIFICATION #superfamily transforming growth factor alpha precursor; EGF !1homology KEYWORDS carcinogenesis; glycoprotein; growth factor; mitogen; !1transformation; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-38 #domain propeptide #status predicted #label PRO\ !$39-88 #product transforming growth factor alpha #status !8experimental #label MAT\ !$46-81 #domain EGF homology #label EGF\ !$98-124 #domain transmembrane #status predicted #label TMM\ !$25 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$46-59,54-70,72-81 #disulfide_bonds #status predicted SUMMARY #length 159 #molecular-weight 16970 #checksum 9453 SEQUENCE /// ENTRY WFHU1 #type complete TITLE transforming growth factor alpha precursor - human ALTERNATE_NAMES EGF-like TGF; eTGF; TGF type 1; TGF-alpha ORGANISM #formal_name Homo sapiens #common_name man DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 18-Jun-1999 ACCESSIONS JN0876; A01390; I57646; I57694; S31858 REFERENCE JN0876 !$#authors Qian, J.F.; Lazar-Wesley, E.; Breugnot, C.; May, E. !$#journal Gene (1993) 132:291-296 !$#title Human transforming growth factor alpha: Sequence analysis of !1the 4.5-kb and 1.6-kb mRNA species. !$#cross-references MUID:94040776; PMID:8224876 !$#accession JN0876 !'##molecule_type mRNA !'##residues 1-160 ##label QIA !'##cross-references EMBL:X70340; NID:g37089; PIDN:CAA49806.1; !1PID:g37090 REFERENCE A01390 !$#authors Derynck, R.; Roberts, A.B.; Winkler, M.E.; Chen, E.Y.; !1Goeddel, D.V. !$#journal Cell (1984) 38:287-297 !$#title Human transforming growth factor-alpha: precursor structure !1and expression in Escherichia coli. !$#cross-references MUID:84282712; PMID:6088071 !$#accession A01390 !'##molecule_type mRNA !'##residues 1-160 ##label DER !'##cross-references GB:K03222; NID:g339545; PIDN:AAA61159.1; !1PID:g339546 REFERENCE I57646 !$#authors Jakobovits, E.B.; Schlokat, U.; Vannice, J.L.; Derynck, R.; !1Levinson, A.D. !$#journal Mol. Cell. Biol. (1988) 8:5549-5554 !$#title The human transforming growth factor alpha promoter directs !1transcription initiation from a single site in the absence !1of a TATA sequence. !$#cross-references MUID:89219018; PMID:2907605 !$#accession I57646 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-58 ##label RES !'##cross-references GB:M22440; NID:g183079; PIDN:AAA52530.1; !1PID:g183080 REFERENCE I57694 !$#authors Jakowlew, S.B.; Kondaiah, P.; Dillard, P.J.; Sporn, M.B.; !1Roberts, A.B. !$#journal Mol. Endocrinol. (1988) 2:1056-1063 !$#title A novel low molecular weight ribonucleic acid (RNA) related !1to transforming growth factor alpha messenger RNA. !$#cross-references MUID:89127251; PMID:2464748 !$#accession I57694 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-57,'A',59-64,'H',66-158,'L',160 ##label RE2 !'##cross-references GB:M31172; NID:g339537; PIDN:AAA61157.1; !1PID:g339538 COMMENT This protein is involved in neoplasia and also contributes !1to growth regulation of normal cells. GENETICS !$#gene GDB:TGFA !'##cross-references GDB:120435; OMIM:190170 !$#map_position 2p13-2p13 CLASSIFICATION #superfamily transforming growth factor alpha precursor; EGF !1homology KEYWORDS carcinogenesis; glycoprotein; growth factor; mitogen; !1transformation; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$40-89 #product transforming growth factor alpha #status !8predicted #label TGF\ !$47-82 #domain EGF homology #label EGF\ !$99-124 #domain transmembrane #status predicted #label TMS\ !$25 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$47-60,55-71,73-82 #disulfide_bonds #status predicted SUMMARY #length 160 #molecular-weight 17006 #checksum 449 SEQUENCE /// ENTRY S27195 #type complete TITLE transforming growth factor alpha - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S27195; I52198 REFERENCE S27195 !$#authors Vaughan, T.J.; Pascall, J.C.; Brown, K.D. !$#journal Biochim. Biophys. Acta (1992) 1132:322-324 !$#title Nucleotide sequence and tissue distribution of mouse !1transforming growth factor-alpha. !$#cross-references MUID:93041937; PMID:1420315 !$#accession S27195 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-159 ##label VAU !'##cross-references GB:M92420; NID:g202155; PIDN:AAA40481.1; !1PID:g202156 CLASSIFICATION #superfamily transforming growth factor alpha precursor; EGF !1homology FEATURE !$46-81 #domain EGF homology #label EGF SUMMARY #length 159 #molecular-weight 17018 #checksum 9352 SEQUENCE /// ENTRY WMVZ9 #type complete TITLE growth factor - vaccinia virus ORGANISM #formal_name vaccinia virus DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 07-Aug-1998 ACCESSIONS A01391 REFERENCE A92988 !$#authors Venkatesan, S.; Gershowitz, A.; Moss, B. !$#journal J. Virol. (1982) 44:637-646 !$#title Complete nucleotide sequences of two adjacent early vaccinia !1virus genes located within the inverted terminal repetition. !$#cross-references MUID:83059924; PMID:7143577 !$#accession A01391 !'##molecule_type DNA !'##residues 1-140 ##label VEN CLASSIFICATION #superfamily transforming growth factor alpha precursor; EGF !1homology KEYWORDS growth factor FEATURE !$45-80 #domain EGF homology #label EGF SUMMARY #length 140 #molecular-weight 15524 #checksum 59 SEQUENCE /// ENTRY WMVZ3C #type complete TITLE growth factor - vaccinia virus (strain Copenhagen) ALTERNATE_NAMES C11R protein ORGANISM #formal_name vaccinia virus #note host Homo sapiens (man) DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 18-Jun-1999 ACCESSIONS C42503 REFERENCE A42501 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:517-563 !$#title Appendix to "The complete DNA sequence of vaccinia virus". !$#accession C42503 !'##molecule_type DNA !'##residues 1-142 ##label GOE !'##cross-references GB:M35027; NID:g335317; PIDN:AAA47985.1; !1PID:g335333 !'##experimental_source strain Copenhagen REFERENCE A42531 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:247-266 !$#title The complete DNA sequence of vaccinia virus. !$#cross-references MUID:91021027; PMID:2219722 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given CLASSIFICATION #superfamily transforming growth factor alpha precursor; EGF !1homology KEYWORDS growth factor FEATURE !$45-80 #domain EGF homology #label EGF SUMMARY #length 142 #molecular-weight 15777 #checksum 4221 SEQUENCE /// ENTRY EGVZM1 #type complete TITLE growth factor - myxoma virus ORGANISM #formal_name myxoma virus DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 18-Jun-1999 ACCESSIONS A26131 REFERENCE A93024 !$#authors Upton, C.; Macen, J.L.; McFadden, G. !$#journal J. Virol. (1987) 61:1271-1275 !$#title Mapping and sequencing of a gene from myxoma virus that is !1related to those encoding epidermal growth factor and !1transforming growth factor alpha. !$#cross-references MUID:87141350; PMID:3029424 !$#accession A26131 !'##molecule_type DNA !'##residues 1-85 ##label UPT !'##cross-references GB:M15806; GB:M35234; NID:g332299; PIDN:AAA46626.1; !1PID:g332300 CLASSIFICATION #superfamily transforming growth factor alpha precursor; EGF !1homology KEYWORDS glycoprotein; growth factor FEATURE !$37-76 #domain EGF homology #label EGF\ !$48,58 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 85 #molecular-weight 9629 #checksum 6950 SEQUENCE /// ENTRY EGVZSF #type complete TITLE growth factor - rabbit fibroma virus ORGANISM #formal_name rabbit fibroma virus, Shope fibroma virus DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 13-Aug-1999 ACCESSIONS A26723 REFERENCE A26723 !$#authors Chang, W.; Upton, C.; Hu, S.L.; Purchio, A.F.; McFadden, G. !$#journal Mol. Cell. Biol. (1987) 7:535-540 !$#title The genome of Shope fibroma virus, a tumorigenic poxvirus, !1contains a growth factor gene with sequence similarity to !1those encoding epidermal growth factor and transforming !1growth factor alpha. !$#cross-references MUID:87172751; PMID:3031480 !$#accession A26723 !'##molecule_type DNA !'##residues 1-80 ##label CHA !'##cross-references GB:M15921; NID:g333600; PIDN:AAA66873.1; !1PID:g333601 !'##experimental_source strain Kasza CLASSIFICATION #superfamily transforming growth factor alpha precursor; EGF !1homology KEYWORDS glycoprotein; growth factor FEATURE !$33-72 #domain EGF homology #label EGF\ !$44,54 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 80 #molecular-weight 9210 #checksum 7811 SEQUENCE /// ENTRY A38432 #type complete TITLE heparin-binding EGF-like growth factor precursor - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 29-Sep-1999 ACCESSIONS A38432; A37300 REFERENCE A38432 !$#authors Higashiyama, S.; Abraham, J.A.; Miller, J.; Fiddes, J.C.; !1Klagsbrun, M. !$#journal Science (1991) 251:936-939 !$#title A heparin-binding growth factor secreted by macrophage-like !1cells that is related to EGF. !$#cross-references MUID:91157008; PMID:1840698 !$#accession A38432 !'##molecule_type mRNA !'##residues 1-208 ##label HIG !'##cross-references GB:M60278; NID:g183866; PIDN:AAA35956.1; !1PID:g183867 REFERENCE A37300 !$#authors Higashiyama, S.; Lau, K.; Besner, G.E.; Abraham, J.A.; !1Klagsbrun, M. !$#journal J. Biol. Chem. (1992) 267:6205-6212 !$#title Structure of heparin-binding EGF-like growth factor. !1Multiple forms, primary structure, and glycosylation of the !1mature protein. !$#cross-references MUID:92210596; PMID:1556128 !$#accession A37300 !'##molecule_type protein !'##residues 63-74,'X',76-84,'X',86-148 ##label HI2 GENETICS !$#gene GDB:DTR; DTS; HEGFL !'##cross-references GDB:119853; OMIM:126150 !$#map_position 5q23-5q23 CLASSIFICATION #superfamily heparin-binding EGF-like growth factor; EGF !1homology KEYWORDS heparin binding; transmembrane protein FEATURE !$108-143 #domain EGF homology #label EGF SUMMARY #length 208 #molecular-weight 23067 #checksum 3973 SEQUENCE /// ENTRY A41914 #type complete TITLE diptheria toxin receptor precursor - green monkey ORGANISM #formal_name Cercopithecus aethiops #common_name green monkey, grivet DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A41914; JC4687 REFERENCE A41914 !$#authors Naglich, J.G.; Metherall, J.E.; Russell, D.W.; Eidels, L. !$#journal Cell (1992) 69:1051-1061 !$#title Expression cloning of a diphtheria toxin receptor: identity !1with a heparin-binding EGF-like growth factor precursor. !$#cross-references MUID:92298386; PMID:1606612 !$#accession A41914 !'##status preliminary !'##molecule_type mRNA !'##residues 1-208 ##label NAG !'##cross-references GB:M93012 REFERENCE JC4687 !$#authors Hooper, K.P.; Eidels, L. !$#journal Biochem. Biophys. Res. Commun. (1996) 220:675-680 !$#title Glutamic acid 141 of the diptheria toxin receptor (HB-EGF !1precursor) is critical for toxin binding and toxin !1sensitivity. !$#cross-references MUID:96183008; PMID:8607824 !$#accession JC4687 !'##molecule_type mRNA !'##residues 1-208 ##label HOO COMMENT This precursor is a transmembrane glycoprotein which is !1cleaved at th e cell surface to release the mature !1heparin-binding-epidermal growth factor. CLASSIFICATION #superfamily heparin-binding EGF-like growth factor; EGF !1homology KEYWORDS receptor; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$63-150 #product diptheria toxin receptor precursor #status !8predicted #label MAT\ !$108-143 #domain EGF homology #label EGF\ !$160-184 #domain transmembrane #status predicted #label TRN SUMMARY #length 208 #molecular-weight 22985 #checksum 3725 SEQUENCE /// ENTRY JC1409 #type complete TITLE heparin-binding EGF-like growth factor precursor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JC1409 REFERENCE JC1409 !$#authors Abraham, J.A.; Damm, D.; Bajardi, A.; Miller, J.; Klagsbrun, !1M.; Ezekowitz, R.A.B. !$#journal Biochem. Biophys. Res. Commun. (1993) 190:125-133 !$#title Heparin-binding EGF-like growth factor: Characterization of !1rat and mouse cDNA clones, protein domain conservation !1across species, and transcript expression in tissues. !$#cross-references MUID:93135756; PMID:7678488 !$#accession JC1409 !'##molecule_type mRNA !'##residues 1-208 ##label ABR !'##cross-references GB:L05489; NID:g204289; PIDN:AAA81780.1; !1PID:g204290 CLASSIFICATION #superfamily heparin-binding EGF-like growth factor; EGF !1homology KEYWORDS growth factor; heparin binding; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-208 #product heparin-binding EGF-like growth factor !8#status predicted #label MAT\ !$108-143 #domain EGF homology #label EGF\ !$161-184 #domain transmembrane #status predicted #label TMM SUMMARY #length 208 #molecular-weight 22842 #checksum 3282 SEQUENCE /// ENTRY JC1410 #type complete TITLE heparin-binding EGF-like growth factor precursor - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JC1410; JC4659 REFERENCE JC1409 !$#authors Abraham, J.A.; Damm, D.; Bajardi, A.; Miller, J.; Klagsbrun, !1M.; Ezekowitz, R.A.B. !$#journal Biochem. Biophys. Res. Commun. (1993) 190:125-133 !$#title Heparin-binding EGF-like growth factor: Characterization of !1rat and mouse cDNA clones, protein domain conservation !1across species, and transcript expression in tissues. !$#cross-references MUID:93135756; PMID:7678488 !$#accession JC1410 !'##molecule_type mRNA !'##residues 1-208 ##label ABR !'##cross-references GB:L07264; NID:g192999; PIDN:AAA37542.1; !1PID:g193000 REFERENCE JC4659 !$#authors Harding, P.A.; Brigstock, D.R.; Shen, L.; Crissman-Combs, !1M.A.; Besner, G.E. !$#journal Gene (1996) 169:291-292 !$#title Characterization of the gene encoding murine heparin-binding !1epidermal growth factor-like growth factor. !$#cross-references MUID:96194822; PMID:8647467 !$#accession JC4659 !'##molecule_type DNA !'##residues 1-208 ##label HAR !'##cross-references GB:U39189 COMMENT This factor is a member of the epidermal growth factor !1family. Its binding activity is heparin-dependent. GENETICS !$#gene mHB-EGF !$#introns 16/1; 74/1; 133/2; 185/2 CLASSIFICATION #superfamily heparin-binding EGF-like growth factor; EGF !1homology KEYWORDS growth factor; heparin binding; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-208 #product heparin-binding EGF-like growth factor !8#status predicted #label MAT\ !$108-143 #domain EGF homology #label EGF\ !$161-184 #domain transmembrane #status predicted #label TMM SUMMARY #length 208 #molecular-weight 22807 #checksum 4733 SEQUENCE /// ENTRY TVHUSE #type complete TITLE transforming protein sec - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 18-Jun-1999 ACCESSIONS A36751 REFERENCE A36751 !$#authors Lane, M.A.; Wong, S.K.; Daugherty, K.; Roskey, M.; Sousa, !1D.; Sainten, A.C.; Macoska, J. !$#journal Nucleic Acids Res. (1990) 18:3068 !$#title Nucleotide sequence of a human oncogene active in tumors of !1secretory epithelium. !$#cross-references MUID:90272432; PMID:2349114 !$#accession A36751 !'##molecule_type DNA !'##residues 1-109 ##label LAN !'##cross-references EMBL:X52259; NID:g36423; PIDN:CAA36502.1; !1PID:g36424 GENETICS !$#introns #status absent CLASSIFICATION #superfamily sec transforming protein KEYWORDS oncogene; transforming protein SUMMARY #length 109 #molecular-weight 12209 #checksum 9972 SEQUENCE /// ENTRY TVMVT3 #type complete TITLE transforming protein int-3 - mouse mammary tumor virus ORGANISM #formal_name mouse mammary tumor virus, MMTV DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 10-Jul-1998 ACCESSIONS A38072 REFERENCE A38072 !$#authors Robbins, J.; Blondel, B.J.; Gallahan, D.; Callahan, R. !$#journal J. Virol. (1992) 66:2594-2599 !$#title Mouse mammary tumor gene int-3: a member of the notch gene !1family transforms mammary epithelial cells. !$#cross-references MUID:92194507; PMID:1312643 !$#accession A38072 !'##molecule_type mRNA !'##residues 1-552 ##label ROB !'##cross-references GB:M80456 GENETICS !$#gene int-3 CLASSIFICATION #superfamily int-3 transforming protein; ankyrin repeat !1homology KEYWORDS duplication; oncogene; transforming protein FEATURE !$217-248 #domain ankyrin repeat homology #label AN1\ !$249-281 #domain ankyrin repeat homology #label AN2\ !$283-315 #domain ankyrin repeat homology #label AN3\ !$316-348 #domain ankyrin repeat homology #label AN4 SUMMARY #length 552 #molecular-weight 57516 #checksum 8493 SEQUENCE /// ENTRY GKBOA #type complete TITLE acidic fibroblast growth factor precursor - bovine ALTERNATE_NAMES aFGF; eye-derived growth factor II; heparin-binding growth factor I; prostatropin ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 13-Aug-1986 #sequence_revision 03-Feb-1994 #text_change 19-Jan-2001 ACCESSIONS JH0613; S02102; S02661; S22065; B24663; A94281; S03953; !1A91010; A24477; B25043; C25043; A25043; A24539; A60884; !1A37892; B37892; A61198; I46024; A34477; A01385 REFERENCE JH0613 !$#authors Renaud, F.; Desset, S.; Bugra, K.; Halley, C.; Philippe, !1J.M.; Courtois, Y.; Laurent, M. !$#journal Biochem. Biophys. Res. Commun. (1992) 184:945-952 !$#title Heterogeneity of 3' untranslated region of bovine acidic FGF !1transcripts. !$#cross-references MUID:92246990; PMID:1374244 !$#accession JH0613 !'##molecule_type DNA !'##residues 58-155 ##label REN REFERENCE S02102 !$#authors Halley, C.; Courtois, Y.; Laurent, M. !$#journal Nucleic Acids Res. (1988) 16:10913 !$#title Nucleotide sequence of bovine acidic fibroblast growth !1factor cDNA. !$#cross-references MUID:89083506; PMID:3205724 !$#accession S02102 !'##molecule_type mRNA !'##residues 1-155 ##label HAL !'##cross-references EMBL:X13221; NID:g347; PIDN:CAA31610.1; PID:g348 REFERENCE S02661 !$#authors Alterio, J.; Halley, C.; Brou, C.; Soussi, T.; Courtois, Y.; !1Laurent, M. !$#journal FEBS Lett. (1988) 242:41-46 !$#title Characterization of a bovine acidic FGF cDNA clone and its !1expression in brain and retina. !$#cross-references MUID:89078619; PMID:2849564 !$#accession S02661 !'##molecule_type mRNA !'##residues 1-155 ##label ALT !'##cross-references EMBL:X14032; NID:g322; PIDN:CAA32192.1; PID:g323 REFERENCE S22065 !$#authors Philippe, J.M. !$#submission submitted to the EMBL Data Library, May 1992 !$#accession S22065 !'##molecule_type mRNA !'##residues 1-18 ##label PHI !'##cross-references EMBL:X66446; NID:g411; PIDN:CAA47063.1; PID:g412 REFERENCE A94290 !$#authors Abraham, J.A.; Mergia, A.; Whang, J.L.; Tumolo, A.; !1Friedman, J.; Hjerrild, K.A.; Gospodarowicz, D.; Fiddes, !1J.C. !$#journal Science (1986) 233:545-548 !$#title Nucleotide sequence of a bovine clone encoding the !1angiogenic protein, basic fibroblast growth factor. !$#cross-references MUID:86261806; PMID:2425435 !$#accession B24663 !'##molecule_type mRNA !'##residues 16-56 ##label ABR REFERENCE A94281 !$#authors Gimenez-Gallego, G.; Rodkey, J.; Bennett, C.; !1Rios-Candelore, M.; DiSalvo, J.; Thomas, K. !$#journal Science (1985) 230:1385-1388 !$#title Brain-derived acidic fibroblast growth factor: complete !1amino acid sequence and homologies. !$#cross-references MUID:86070224; PMID:4071057 !$#accession A94281 !'##molecule_type protein !'##residues 16-155 ##label GIM REFERENCE S03953 !$#authors Quinkler, W.; Maasberg, M.; Bernotat-Danielowski, S.; !1Luethe, N.; Sharma, H.S.; Schaper, W. !$#journal Eur. J. Biochem. (1989) 181:67-73 !$#title Isolation of heparin-binding growth factors from bovine, !1porcine and canine hearts. !$#cross-references MUID:89231704; PMID:2714282 !$#accession S03953 !'##molecule_type protein !'##residues 16-45 ##label QUI REFERENCE A91010 !$#authors Bohlen, P.; Esch, F.; Baird, A.; Gospodarowicz, D. !$#journal EMBO J. (1985) 4:1951-1956 !$#title Acidic fibroblast growth factor (FGF) from bovine brain: !1amino-terminal sequence and comparison with basic FMF. !$#cross-references MUID:86055750; PMID:4065099 !$#accession A91010 !'##molecule_type protein !'##residues 16-30,'X',32-34,'X',36-44 ##label BOH REFERENCE A24477 !$#authors Crabb, J.W.; Armes, L.G.; Carr, S.A.; Johnson, C.M.; !1Roberts, G.D.; Bordoli, R.S.; McKeehan, W.L. !$#journal Biochemistry (1986) 25:4988-4993 !$#title Complete primary structure of prostatropin, a prostate !1epithelial cell growth factor. !$#cross-references MUID:87026586; PMID:3768327 !$#accession A24477 !'##molecule_type protein !'##residues 2,'GE',5-155 ##label CRA REFERENCE A94127 !$#authors Burgess, W.H.; Mehlman, T.; Marshak, D.R.; Fraser, B.A.; !1Maciag, T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:7216-7220 !$#title Structural evidence that endothelial cell growth factor beta !1is the precursor of both endothelial cell growth factor !1alpha and acidic fibroblast growth factor. !$#cross-references MUID:87016918; PMID:3532107 !$#accession B25043 !'##molecule_type protein !'##residues 2-155 ##label BUR !'##note this form was designated beta endothelial cell growth factor !$#accession C25043 !'##molecule_type protein !'##residues 16-155 ##label BU2 !'##note this form was designated acidic fibroblast growth factor !$#accession A25043 !'##molecule_type protein !'##residues 22-155 ##label BU3 !'##note this form was designated alpha endothelial cell growth factor REFERENCE A24539 !$#authors Strydom, D.J.; Harper, J.W.; Lobb, R.R. !$#journal Biochemistry (1986) 25:945-951 !$#title Amino acid sequence of bovine brain derived class 1 !1heparin-binding growth factor. !$#cross-references MUID:86187766; PMID:2421762 !$#accession A24539 !'##molecule_type protein !'##residues 16-155 ##label STR REFERENCE A60884 !$#authors Thomas, K.A.; Gimenez-Gallego, G.; Rios-Candelore, M.; !1DiSalvo, J. !$#journal J. Protein Chem. (1987) 6:163-171 !$#title Primary structure and mitogenic and angiogenic activities of !1brain-derived acidic fibroblast growth factor. !$#accession A60884 !'##molecule_type protein !'##residues 16-155 ##label THO REFERENCE A37892 !$#authors Kuo, M.D.; Huang, S.S.; Huang, J.S. !$#journal J. Biol. Chem. (1990) 265:16455-16463 !$#title Acidic fibroblast growth factor receptor purified from !1bovine liver is a novel protein tyrosine kinase. !$#cross-references MUID:90375514; PMID:2168890 !$#accession A37892 !'##molecule_type protein !'##residues 22-30,'X',32-38 ##label KU2 !'##note this form was designated brain-derived growth factor A !$#accession B37892 !'##molecule_type protein !'##residues 16-30,'X',32-40 ##label KUO !'##note this sequence is an amino-terminal fragment of a form !1designated as brain-derived growth factor B REFERENCE A61198 !$#authors Hill, C.E.; Belford, D.A.; Godovac-Zimmermann, J.; Hendry, !1I.A. !$#journal Brain Res. Dev. Brain Res. (1991) 63:13-19 !$#title Class 1 heparin binding growth factor promotes the !1differentiation but not the survival of ciliary neurones in !1vivo. !$#cross-references MUID:92164087; PMID:1724209 !$#accession A61198 !'##molecule_type protein !'##residues 11-26;28-50;53-110,'H',112,'NTY';134-155 ##label HIL REFERENCE I46024 !$#authors Philippe, J.M.; Renaud, F.; Desset, S.; Laurent, M.; Mallet, !1J.; Courtois, Y.; Edwards, J.B. !$#journal Biochem. Biophys. Res. Commun. (1992) 188:843-850 !$#title Cloning of two different 5' untranslated exons of bovine !1acidic fibroblast growth factor by the single strand !1ligation to single-stranded cDNA methodology. !$#cross-references MUID:93075172; PMID:1280126 !$#accession I46024 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-18 ##label PH2 !'##cross-references EMBL:X66446; NID:g411; PIDN:CAA47063.1; PID:g412 REFERENCE A34477 !$#authors Sasaki, H.; Hoshi, H.; Hong, Y.M.; Suzuki, T.; Kato, T.; !1Sasaki, H.; Saito, M.; Youki, H.; Karube, K.; Konno, S.; !1Onodera, M.; Saito, T.; Aoyagi, S. !$#journal J. Biol. Chem. (1989) 264:17606-17612 !$#title Purification of acidic fibroblast growth factor from bovine !1heart and its localization in the cardiac myocytes. !$#cross-references MUID:90008933; PMID:2677012 !$#accession A34477 !'##status preliminary !'##molecule_type protein !'##residues 16-24;121-127;134-143 ##label SAS !'##experimental_source heart COMMENT The acidic and basic fibroblast growth factors are the major !1endothelial-cell growth factors. Both are angiogenic agents !1in vivo and are potent mitogens for a variety of !1mesoderm-derived cell types in vitro (although bFGF is !130-100 times more potent than aFGF in stimulating the !1proliferation of normal diploid cells). There are !1differences in the tissue distribution and concentration of !1these two growth factors. COMMENT This protein binds heparin, although less strongly than does !1bFGF. COMMENT There are some sequence similarities between residues !1117-126 (a region flanked by Lys-Lys dipeptides) and a !1number of neuropeptides, including a gastrin-releasing !1peptide from the pig (residues 18-27) and bovine substance P !1beta (residues 98-107). GENETICS !$#gene HBGF-1 !$#introns 57/1; 91/3 CLASSIFICATION #superfamily fibroblast growth factor KEYWORDS acetylated amino end; angiogenesis; growth factor; heparin !1binding; mitogen FEATURE !$2-155 #product beta endothelial cell growth factor #status !8experimental #label ECB\ !$16-155 #product acidic fibroblast growth factor #status !8experimental #label MAT\ !$22-155 #product alpha endothelial cell growth factor #status !8experimental #label ECA\ !$24-28,113-116 #region heparin binding #status predicted\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental SUMMARY #length 155 #molecular-weight 17493 #checksum 8491 SEQUENCE /// ENTRY A60721 #type complete TITLE acidic fibroblast growth factor - golden hamster ALTERNATE_NAMES heparin-binding growth factor 1 ORGANISM #formal_name Mesocricetus auratus #common_name golden hamster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A60721 REFERENCE A60721 !$#authors Hall, J.A.; Harris, M.A.; Malark, M.; Mansson, P.E.; Zhou, !1H.; Harris, S.E. !$#journal J. Cell. Biochem. (1990) 43:17-26 !$#title Characterization of the hamster DDT-1 cell aFGF/HGBF-I gene !1and cDNA and its modulation by steroids. !$#cross-references MUID:90270291; PMID:1693366 !$#accession A60721 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-155 ##label HAL CLASSIFICATION #superfamily fibroblast growth factor KEYWORDS growth factor; heparin binding SUMMARY #length 155 #molecular-weight 17403 #checksum 9573 SEQUENCE /// ENTRY A33665 #type complete TITLE acidic fibroblast growth factor 1 precursor [validated] - human ALTERNATE_NAMES beta-ECGF; endothelial cell growth factor beta; heparin-binding growth factor 1 ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 08-Dec-2000 ACCESSIONS A33665; A32316; S18217; A43804; A24662; JH0707; S35535; !1S35536; I39413; A23553; A24820; A24243; A24301; A26386; !1A53639 REFERENCE A33665 !$#authors Mergia, A.; Tischer, E.; Graves, D.; Tumolo, A.; Miller, J.; !1Gospodarowicz, D.; Abraham, J.A.; Shipley, G.D.; Fiddes, !1J.C. !$#journal Biochem. Biophys. Res. Commun. (1989) 164:1121-1129 !$#title Structural analysis of the gene for human acidic fibroblast !1growth factor. !$#cross-references MUID:90073637; PMID:2590193 !$#accession A33665 !'##molecule_type DNA !'##residues 1-155 ##label MER !'##cross-references GB:M30491 REFERENCE A32316 !$#authors Wang, W.P.; Lehtoma, K.; Varban, M.L.; Krishnan, I.; Chiu, !1I.M. !$#journal Mol. Cell. Biol. (1989) 9:2387-2395 !$#title Cloning of the gene coding for human class 1 heparin-binding !1growth factor and its expression in fetal tissues. !$#cross-references MUID:89343957; PMID:2474753 !$#accession A32316 !'##molecule_type DNA !'##residues 1-155 ##label WAN !'##cross-references GB:M23087; NID:g183875; PIDN:AAA52638.1; !1PID:g386768 REFERENCE S18217 !$#authors Wang, W.P.; Quick, D.; Balcerzak, S.P.; Needleman, S.W.; !1Chiu, I.M. !$#journal Oncogene (1991) 6:1521-1529 !$#title Cloning and sequence analysis of the human acidic fibroblast !1growth factor gene and its preservation in leukemia !1patients. !$#cross-references MUID:92019819; PMID:1717925 !$#accession S18217 !'##molecule_type DNA !'##residues 1-155 ##label WA2 !'##cross-references EMBL:M23086 REFERENCE A43804 !$#authors Chiu, I.M.; Wang, W.P.; Lehtoma, K. !$#journal Oncogene (1990) 5:755-762 !$#title Alternative splicing generates two forms of mRNA coding for !1human heparin-binding growth factor 1. !$#cross-references MUID:90265618; PMID:1693186 !$#accession A43804 !'##molecule_type mRNA !'##residues 1-155 ##label CHI !'##cross-references EMBL:X51943; NID:g32435; PIDN:CAA36206.1; !1PID:g32436 REFERENCE A24662 !$#authors Jaye, M.; Howk, R.; Burgess, W.; Ricca, G.A.; Chiu, I.M.; !1Ravera, M.W.; O'Brien, S.J.; Modi, W.S.; Maciag, T.; Drohan, !1W.N. !$#journal Science (1986) 233:541-545 !$#title Human endothelial cell growth factor: cloning, nucleotide !1sequence, and chromosome localization. !$#cross-references MUID:86261805; PMID:3523756 !$#accession A24662 !'##molecule_type mRNA !'##residues 1-155 ##label JAY !'##cross-references GB:M13361; NID:g181941; PIDN:AAA79245.1; !1PID:g181942 REFERENCE JH0707 !$#authors Yu, Y.L.; Kha, H.; Golden, J.A.; Migchielsen, A.A.J.; !1Goetzl, E.J.; Turck, C.W. !$#journal J. Exp. Med. (1992) 175:1073-1080 !$#title An acidic fibroblast growth factor protein generated by !1alternate splicing acts like an antagonist. !$#cross-references MUID:92202857; PMID:1372643 !$#accession JH0707 !'##molecule_type mRNA !'##residues 1-155 ##label YUY !'##cross-references GB:X65778; NID:g396163; PIDN:CAA46661.1; !1PID:g396164 REFERENCE S35535 !$#authors Payson, R.A.; Canatan, H.; Chotani, M.A.; Wang, W.P.; !1Harris, S.E.; Myers, R.L.; Chiu, I.M. !$#journal Nucleic Acids Res. (1993) 21:489-495 !$#title Cloning of two novel forms of human acidic fibroblast growth !1factor (aFGF) mRNA. !$#cross-references MUID:93181239; PMID:7680120 !$#accession S35535 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-58 ##label PAY !'##cross-references GB:L01485 !$#accession S35536 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-58 ##label PA2 !'##cross-references GB:L01487 REFERENCE I39412 !$#authors Crumley, G.; Dionne, C.A.; Jaye, M. !$#journal Biochem. Biophys. Res. Commun. (1990) 171:7-13 !$#title The gene for human acidic fibroblast growth factor encodes !1two upstream exons alternatively spliced to the first coding !1exon. !$#cross-references MUID:90365758; PMID:2393407 !$#accession I39413 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-40 ##label RES !'##cross-references GB:M60515; NID:g178226; PIDN:AAA51672.1; !1PID:g553170; GB:M60516; NID:g178232; PID:g553171 REFERENCE A23553 !$#authors Harper, J.W.; Strydom, D.J.; Lobb, R.R. !$#journal Biochemistry (1986) 25:4097-4103 !$#cross-references MUID:86296647; PMID:2427112 !$#accession A23553 !'##molecule_type protein !'##residues 16-155 ##label HAR REFERENCE A24820 !$#authors Gimenez-Gallego, G.; Conn, G.; Hatcher, V.B.; Thomas, K.A. !$#journal Biochem. Biophys. Res. Commun. (1986) 138:611-617 !$#title The complete amino acid sequence of human brain-derived !1acidic fibroblast growth factor. !$#cross-references MUID:86295741; PMID:3527167 !$#accession A24820 !'##molecule_type protein !'##residues 16-155 ##label GIM REFERENCE A90122 !$#authors Gimenez-Gallego, G.; Conn, G.; Hatcher, V.B.; Thomas, K.A. !$#journal Biochem. Biophys. Res. Commun. (1986) 135:541-548 !$#title Human brain-derived acidic and basic fibroblast growth !1factors: amino terminal sequences and specific mitogenic !1activities. !$#cross-references MUID:86186784; PMID:3964259 !$#accession A24243 !'##molecule_type protein !'##residues 16-47 ##label GI2 !'##experimental_source brain REFERENCE A91364 !$#authors Gautschi, P.; Frater-Schroder, M.; Bohlen, P. !$#journal FEBS Lett. (1986) 204:203-207 !$#title Partial molecular characterization of endothelial cell !1mitogens from human brain: acidic and basic fibroblast !1growth factors. !$#cross-references MUID:86275260; PMID:3732516 !$#accession A24301 !'##molecule_type protein !'##residues 16-30,'X',32-49 ##label GAU REFERENCE A26386 !$#authors Gautschi-Sova, P.; Muller, T.; Bohlen, P. !$#journal Biochem. Biophys. Res. Commun. (1986) 140:874-880 !$#title Amino acid sequence of human acidic fibroblast growth !1factor. !$#cross-references MUID:87048871; PMID:3778488 !$#accession A26386 !'##molecule_type protein !'##residues 16-155 ##label GA2 !'##experimental_source brain REFERENCE A53639 !$#authors Chavan, A.J.; Haley, B.E.; Volkin, D.B.; Marfia, K.E.; !1Verticelli, A.M.; Bruner, M.W.; Draper, J.P.; Burke, C.J.; !1Middaugh, C.R. !$#journal Biochemistry (1994) 33:7193-7202 !$#title Interaction of nucleotides with acidic fibroblast growth !1factor (FGF-1). !$#cross-references MUID:94271773; PMID:7516183 !$#accession A53639 !'##molecule_type protein !'##residues 16-30,'X',32-38;73-75,'X',77-97,'X',99-101;128-131,'X', !1133-140,'X',142-152 ##label CHA GENETICS !$#gene GDB:FGF1; FGFA !'##cross-references GDB:119909; OMIM:131220 !$#map_position 5q31.3-5q33.2 !$#introns 57/1; 91/3 CLASSIFICATION #superfamily fibroblast growth factor KEYWORDS alternative splicing; growth factor; heparin binding FEATURE !$16-155 #product fibroblast growth factor 1 #status !8experimental #label MAT\ !$129 #binding_site carbohydrate (Asn) (covalent) #status !8absent SUMMARY #length 155 #molecular-weight 17460 #checksum 9243 SEQUENCE /// ENTRY GKBOB #type fragment TITLE basic fibroblast growth factor precursor - bovine (fragment) ALTERNATE_NAMES bFGF; kidney-derived growth factor; prostatropin ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 13-Aug-1986 #sequence_revision 02-Jun-1995 #text_change 24-Nov-1999 ACCESSIONS A24663; A32878; A33784; A61550; A61551; A60310; A61094; !1A01386; A60316; A22054; A24819 REFERENCE A94290 !$#authors Abraham, J.A.; Mergia, A.; Whang, J.L.; Tumolo, A.; !1Friedman, J.; Hjerrild, K.A.; Gospodarowicz, D.; Fiddes, !1J.C. !$#journal Science (1986) 233:545-548 !$#title Nucleotide sequence of a bovine clone encoding the !1angiogenic protein, basic fibroblast growth factor. !$#cross-references MUID:86261806; PMID:2425435 !$#accession A24663 !'##molecule_type mRNA !'##residues 3-157 ##label ABR !'##cross-references GB:M13440; NID:g163049; PIDN:AAA30518.1; !1PID:g163050 !'##experimental_source pituitary gland REFERENCE A90924 !$#authors Abraham, J.A.; Whang, J.L.; Tumolo, A.; Mergia, A.; Fiddes, !1J.C. !$#journal Cold Spring Harb. Symp. Quant. Biol. (1986) 51:657-668 !$#title Human basic fibroblast growth factor: nucleotide sequence, !1genomic organization, and expression in mammalian cells. !$#cross-references MUID:87217066; PMID:3472745 !$#accession A32878 !'##molecule_type mRNA !'##residues 3-157 ##label AB2 REFERENCE A33784 !$#authors Milner, P.G.; Li, Y.S.; Hoffman, R.M.; Kodner, C.M.; Siegel, !1N.R.; Deuel, T.F. !$#journal Biochem. Biophys. Res. Commun. (1989) 165:1096-1103 !$#title A novel 17 kD heparin-binding growth factor (HBGF-8) in !1bovine uterus: purification and N-terminal amino acid !1sequence. !$#cross-references MUID:90121211; PMID:2610682 !$#accession A33784 !'##molecule_type protein !'##residues 1-14 ##label MIL !'##note demonstration of a possible alternative initiator or splice !1junction REFERENCE A61550 !$#authors Bertolini, J.; Hearn, M.T.W. !$#journal Mol. Cell. Endocrinol. (1987) 51:187-199 !$#title Isolation, characterisation and tissue localisation of an !1N-terminal-truncated variant of fibroblast growth factor. !$#cross-references MUID:87247652; PMID:3596000 !$#accession A61550 !'##molecule_type protein !'##residues 16-35 ##label BER REFERENCE A61551 !$#authors Ueno, N.; Baird, A.; Esch, F.; Ling, N.; Guillemin, R. !$#journal Mol. Cell. Endocrinol. (1987) 49:189-194 !$#title Isolation and partial characterization of basic fibroblast !1growth factor from bovine testis. !$#cross-references MUID:87162856; PMID:3556754 !$#accession A61551 !'##molecule_type protein !'##residues 27-35,'X',37-41 ##label UE3 !'##experimental_source testes !'##note this form appears to be identical to the renal form REFERENCE A60310 !$#authors Ueno, N.; Baird, A.; Esch, F.; Shimasaki, S.; Ling, N.; !1Guillemin, R. !$#journal Regul. Pept. (1986) 16:135-145 !$#title Purification and partial characterization of a mitogenic !1factor from bovine liver: structural homology with basic !1fibroblast growth factor. !$#cross-references MUID:87119165; PMID:3809608 !$#accession A60310 !'##molecule_type protein !'##residues 23-35,'X',37-42 ##label UEN !'##experimental_source liver REFERENCE A24819 !$#authors Ueno, N.; Baird, A.; Esch, F.; Ling, N.; Guillemin, R. !$#journal Biochem. Biophys. Res. Commun. (1986) 138:580-588 !$#title Isolation of an amino terminal extended form of basic !1fibroblast growth factor. !$#cross-references MUID:86295737; PMID:3741423 !$#contents annotation !$#note the amino end of this form was blocked; the peptide !1composition matched what was thought to be the signal !1sequence REFERENCE A61094 !$#authors Gospodarowicz, D.; Baird, A.; Cheng, J.; Lui, G.M.; Esch, !1F.; Bohlen, P. !$#journal Endocrinology (1986) 118:82-90 !$#title Isolation of fibroblast growth factor from bovine adrenal !1gland: physicochemical and biological characterization. !$#cross-references MUID:86081530; PMID:3940857 !$#accession A61094 !'##molecule_type protein !'##residues 12-25,27-35,'X',37-40 ##label GOS !'##experimental_source adrenal gland REFERENCE A01386 !$#authors Esch, F.; Baird, A.; Ling, N.; Ueno, N.; Hill, F.; Denoroy, !1L.; Klepper, R.; Gospodarowicz, D.; Bohlen, P.; Guillemin, !1R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:6507-6511 !$#title Primary structure of bovine pituitary basic fibroblast !1growth factor (FGF) and comparison with the amino-terminal !1sequence of bovine brain acidic FMF. !$#cross-references MUID:86016731; PMID:3863109 !$#accession A01386 !'##molecule_type protein !'##residues 12-157 ##label ESC !'##experimental_source pituitary gland REFERENCE A60316 !$#authors Baird, A.; Esch, F.; Boehlen, P.; Ling, N.; Gospodarowicz, !1D. !$#journal Regul. Pept. (1985) 12:201-213 !$#title Isolation and partial characterization of an endothelial !1cell growth factor from the bovine kidney: homology with !1basic fibroblast growth factor. !$#cross-references MUID:86095426; PMID:4081126 !$#accession A60316 !'##molecule_type protein !'##residues 27-35,'X',37-43 ##label BAI !'##experimental_source kidney REFERENCE A22054 !$#authors Bohlen, P.; Baird, A.; Esch, F.; Ling, N.; Gospodarowicz, D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:5364-5368 !$#title Isolation and partial molecular characterization of !1pituitary fibroblast growth factor. !$#cross-references MUID:84298139; PMID:6591194 !$#accession A22054 !'##molecule_type protein !'##residues 12-26 ##label BOH COMMENT The acidic and basic fibroblast growth factors are the major !1endothelial-cell growth factors. Both are angiogenic agents !1in vivo and are potent mitogens for a variety of !1mesoderm-derived cell types in vitro (although bFGF is !130-100 times more potent than aFGF in stimulating the !1proliferation of normal diploid cells). COMMENT This protein binds heparin more strongly than does aFGF. CLASSIFICATION #superfamily fibroblast growth factor KEYWORDS alternative splicing; angiogenesis; blocked amino end; !1growth factor; heparin binding; mitogen FEATURE !$1-157 #product basic fibroblast growth factor, uterine form !8#status predicted #label MAT1\ !$4-157 #product basic fibroblast growth factor, pituitary !8gamma form #status experimental #label MAT2\ !$12-157 #product basic fibroblast growth factor, pituitary !8alpha form #status experimental #label MAT3\ !$16-157 #product basic fibroblast growth factor, pituitary !8short form #status predicted #label MAT4\ !$23-157 #product basic fibroblast growth factor, hepatic form !8#status experimental #label MAT5\ !$27-157 #product basic fibroblast growth factor, renal form !8#status experimental #label MAT6\ !$29-33,118-121 #region heparin binding #status predicted\ !$4 #modified_site blocked amino end (Ala) (in mature !8form pituitary gamma) (probably acetylated) #status !8experimental SUMMARY #length 157 #checksum 1115 SEQUENCE /// ENTRY S00185 #type complete TITLE basic fibroblast growth factor - sheep ALTERNATE_NAMES prostatropin ORGANISM #formal_name Ovis orientalis aries, Ovis ammon aries #common_name domestic sheep DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S00185 REFERENCE S00185 !$#authors Simpson, R.J.; Moritz, R.L.; Lloyd, C.J.; Fabri, L.J.; Nice, !1E.C.; Rubira, M.R.; Burgess, A.W. !$#journal FEBS Lett. (1987) 224:128-132 !$#title Primary structure of ovine pituitary basic fibroblast growth !1factor. !$#cross-references MUID:88055577; PMID:3678486 !$#accession S00185 !'##molecule_type protein !'##residues 1-146 ##label SIM CLASSIFICATION #superfamily fibroblast growth factor KEYWORDS growth factor; heparin binding; mitogen FEATURE !$18-22 #region heparin binding #status predicted\ !$107-110 #region heparin binding #status predicted SUMMARY #length 146 #molecular-weight 16434 #checksum 3560 SEQUENCE /// ENTRY A40117 #type complete TITLE basic fibroblast growth factor - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A40117; A29618 REFERENCE A40117 !$#authors Kimelman, D.; Abraham, J.A.; Haaparanta, T.; Palisi, T.M.; !1Kirschner, M.W. !$#journal Science (1988) 242:1053-1056 !$#title The presence of fibroblast growth factor in the frog egg: !1its role as a natural mesoderm inducer. !$#cross-references MUID:89058621; PMID:3194757 !$#accession A40117 !'##status preliminary !'##molecule_type mRNA !'##residues 1-155 ##label KIM !'##cross-references GB:M18067; NID:g214177; PIDN:AAA49726.1; !1PID:g214178; GB:M21092 REFERENCE A29618 !$#authors Kimelman, D.; Kirschner, M. !$#journal Cell (1987) 51:869-877 !$#title Synergistic induction of mesoderm by FGF and TGF-beta and !1the identification of an mRNA coding for FGF in the early !1Xenopus embryo. !$#cross-references MUID:88052890; PMID:3479265 !$#accession A29618 !'##molecule_type mRNA !'##residues 95-110,112-155 ##label KI2 CLASSIFICATION #superfamily fibroblast growth factor KEYWORDS growth factor SUMMARY #length 155 #molecular-weight 17241 #checksum 6402 SEQUENCE /// ENTRY A36301 #type complete TITLE fibroblast growth factor 7 precursor [validated] - human ALTERNATE_NAMES keratinocyte growth factor ORGANISM #formal_name Homo sapiens #common_name man DATE 28-Mar-1991 #sequence_revision 07-Jul-1995 #text_change 08-Dec-2000 ACCESSIONS A36301; A31453; A46289; I51958 REFERENCE A36301 !$#authors Finch, P.W.; Rubin, J.S.; Miki, T.; Ron, D.; Aaronson, S.A. !$#journal Science (1989) 245:752-755 !$#title Human KGF is FGF-related with properties of a paracrine !1effector of epithelial cell growth. !$#cross-references MUID:89368897; PMID:2475908 !$#accession A36301 !'##molecule_type mRNA !'##residues 1-194 ##label FIN !'##cross-references GB:M60828; NID:g186738; PIDN:AAA63210.1; !1PID:g186739; GB:M25295 REFERENCE A31453 !$#authors Rubin, J.S.; Osada, H.; Finch, P.W.; Taylor, W.G.; Rudikoff, !1S.; Aaronson, S.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:802-806 !$#title Purification and characterization of a newly identified !1growth factor specific for epithelial cells. !$#cross-references MUID:89128865; PMID:2915979 !$#accession A31453 !'##molecule_type protein !'##residues 'X',33-44 ##label RUB !'##experimental_source embryonic lung cell fibroblast line M426 REFERENCE A46289 !$#authors Kelley, M.J.; Pech, M.; Seuanez, H.N.; Rubin, J.S.; O'Brien, !1S.J.; Aaronson, S.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:9287-9291 !$#title Emergence of the keratinocyte growth factor multigene family !1during the great ape radiation. !$#cross-references MUID:93028449; PMID:1409637 !$#accession A46289 !'##molecule_type DNA !'##residues 97-194 ##label KEL !'##note sequence extracted from NCBI backbone (NCBIN:115887, !1NCBIP:115889) REFERENCE I51958 !$#authors Aaronson, S.A.; Bottaro, D.P.; Miki, T.; Ron, D.; Finch, !1P.W.; Fleming, T.P.; Ahn, J.; Taylor, W.G.; Rubin, J.S. !$#journal Ann. N. Y. Acad. Sci. (1991) 638:62-77 !$#title Keratinocyte growth factor. A fibroblast growth factor !1family member with unusual target cell specificity. !$#cross-references MUID:92152720; PMID:1664700 !$#accession I51958 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-194 ##label AAR !'##cross-references GB:S81661; NID:g245438; PIDN:AAB21431.1; !1PID:g245439 GENETICS !$#gene GDB:FGF7 !'##cross-references GDB:131444; OMIM:148180 !$#map_position 15q13-15q22 !$#note the human genome contains about 16, intron-containing, !1partial copies of this gene; these copies lack exon 1, are !1dispersed to different chromosomes, and are !1transcriptionally active CLASSIFICATION #superfamily fibroblast growth factor KEYWORDS extracellular protein; growth factor; heparin binding; !1mitogen FEATURE !$1-31 #domain signal sequence #status predicted #label SIG\ !$32-194 #product fibroblast growth factor 7 #status !8experimental #label MAT SUMMARY #length 194 #molecular-weight 22509 #checksum 9753 SEQUENCE /// ENTRY TVMST2 #type complete TITLE transforming protein (int-2) - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 18-Jun-1999 ACCESSIONS A23930; S08157 REFERENCE A23930 !$#authors Moore, R.; Casey, G.; Brookes, S.; Dixon, M.; Peters, G.; !1Dickson, C. !$#journal EMBO J. (1986) 5:919-924 !$#title Sequence, topography and protein coding potential of mouse !1int-2: a putative oncogene activated by mouse mammary tumour !1virus. !$#cross-references MUID:86247582; PMID:3013624 !$#accession A23930 !'##molecule_type DNA; mRNA !'##residues 1-245 ##label MOO !'##cross-references GB:Y00848; GB:M26284; GB:X68450; NID:g52716; !1PIDN:CAA68767.1; PID:g599879 REFERENCE S08157 !$#authors Acland, P.; Dixon, M.; Peters, G.; Dickson, C. !$#journal Nature (1990) 343:662-665 !$#title Subcellular fate of the Int-2 oncoprotein is determined by !1choice of initiation codon. !$#cross-references MUID:90158795; PMID:2406607 !$#accession S08157 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 'HSRAGLARGRVLPAPRLRETRAGAAAAAGGRDAGM',3-17 ##label ACL GENETICS !$#gene int-2 !$#map_position 7 !$#introns 74/1; 108/3 CLASSIFICATION #superfamily fibroblast growth factor KEYWORDS growth factor; transforming protein SUMMARY #length 245 #molecular-weight 27214 #checksum 2365 SEQUENCE /// ENTRY S39582 #type complete TITLE transforming protein int-2 - African clawed frog ALTERNATE_NAMES FGF-3 protein; fibroblast growth factor 3 ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S39582; S25713 REFERENCE S39582 !$#authors Kiefer, P.; Mathieu, M.; Close, M.J.; Peters, G.; Dickson, !1C. !$#journal EMBO J. (1993) 12:4159-4168 !$#title FGF3 from Xenopus laevis. !$#cross-references MUID:94038898; PMID:8223431 !$#accession S39582 !'##status preliminary !'##molecule_type mRNA !'##residues 1-237 ##label KIE !'##cross-references EMBL:Z25539; NID:g396830; PIDN:CAA80987.1; !1PID:g396831 REFERENCE S25713 !$#authors Tannahill, D.; Isaacs, H.V.; Close, M.J.; Peters, G.; Slack, !1J.M.W. !$#journal Development (1992) 115:695-702 !$#title Developmental expression of the Xenopus int-2 (FGF-3) gene: !1activation by mesodermal and neural induction. !$#cross-references MUID:93048831; PMID:1425349 !$#accession S25713 !'##status preliminary !'##molecule_type mRNA !'##residues 39-137 ##label TAN !'##cross-references EMBL:X65237; NID:g64855; PIDN:CAA46341.1; !1PID:g64856 CLASSIFICATION #superfamily fibroblast growth factor SUMMARY #length 237 #molecular-weight 26984 #checksum 9430 SEQUENCE /// ENTRY S04742 #type complete TITLE fibroblast growth factor 3 precursor - human ALTERNATE_NAMES transforming protein int-2 ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 29-Sep-1999 ACCESSIONS S04742 REFERENCE S04742 !$#authors Brookes, S.; Smith, R.; Casey, G.; Dickson, C.; Peters, G. !$#journal Oncogene (1989) 4:429-436 !$#title Sequence organization of the human int-2 gene and its !1expression in teratocarcinoma cells. !$#cross-references MUID:89239468; PMID:2470007 !$#accession S04742 !'##molecule_type DNA !'##residues 1-239 ##label BRO !'##cross-references EMBL:X14445; NID:g33937; PIDN:CAA32615.1; !1PID:g312409 GENETICS !$#gene GDB:FGF3; INT2 !'##cross-references GDB:120103; OMIM:164950 !$#map_position 11q13.3-11q13.3 !$#introns 74/1; 108/3 CLASSIFICATION #superfamily fibroblast growth factor KEYWORDS growth factor FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-239 #product transforming protein (int-2) #status !8predicted #label MAT SUMMARY #length 239 #molecular-weight 26886 #checksum 6563 SEQUENCE /// ENTRY TVHUHS #type complete TITLE fibroblast growth factor 4 - human ALTERNATE_NAMES heparin secretory transforming protein 1; Kaposi sarcoma oncogene; transforming protein hst ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 18-Jun-1999 ACCESSIONS A28417; A29876; A29649 REFERENCE A28417 !$#authors Yoshida, T.; Miyagawa, K.; Odagiri, H.; Sakamoto, H.; !1Little, P.F.R.; Terada, M.; Sugimura, T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:7305-7309 !$#title Genomic sequence of hst, a transforming gene encoding a !1protein homologous to fibroblast growth factors and the !1int-2-encoded protein. !$#cross-references MUID:88041096; PMID:2959959 !$#accession A28417 !'##molecule_type DNA !'##residues 1-206 ##label YOS !'##cross-references DDBJ:J02986; NID:g184430; PIDN:AAB59555.1; !1PID:g386788 REFERENCE A29876 !$#authors Taira, M.; Yoshida, T.; Miyagawa, K.; Sakamoto, H.; Terada, !1M.; Sugimura, T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:2980-2984 !$#title cDNA sequence of human transforming gene hst and !1identification of the coding sequence required for !1transforming activity. !$#cross-references MUID:87204251; PMID:2953031 !$#accession A29876 !'##molecule_type mRNA !'##residues 1-206 ##label TAI !'##cross-references GB:J02986; GB:M16338; NID:g184430; PIDN:AAB59555.1; !1PID:g386788 REFERENCE A29649 !$#authors Delli Bovi, P.; Curatola, A.M.; Kern, F.G.; Greco, A.; !1Ittmann, M.; Basilico, C. !$#journal Cell (1987) 50:729-737 !$#title An oncogene isolated by transfection of Kaposi's sarcoma DNA !1encodes a growth factor that is a member of the FGF family. !$#cross-references MUID:87301716; PMID:2957062 !$#accession A29649 !'##molecule_type mRNA !'##residues 1-206 ##label BOV !'##cross-references GB:M17446; NID:g186785; PIDN:AAA59473.1; !1PID:g307092 COMMENT This protein is an oncogene for Kaposi's sarcoma. It is !1homologous to the mouse int-2-encoded protein, which has !1been implicated in murine mammary carcinogenesis. GENETICS !$#gene GDB:FGF4; HSTF1 !'##cross-references GDB:120066; OMIM:164980 !$#map_position 11q13.3-11q13.3 !$#introns 114/1; 148/3 CLASSIFICATION #superfamily fibroblast growth factor KEYWORDS growth factor; Kaposi sarcoma; transforming protein SUMMARY #length 206 #molecular-weight 22047 #checksum 2847 SEQUENCE /// ENTRY TVMSHS #type complete TITLE fibroblast growth factor 4 - mouse ALTERNATE_NAMES transforming protein hstf1; transforming protein k-FGF; transforming protein KS3 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 17-Mar-2000 ACCESSIONS S04741; A37360 REFERENCE S04741 !$#authors Brookes, S.; Smith, R.; Thurlow, J.; Dickson, C.; Peters, G. !$#journal Nucleic Acids Res. (1989) 17:4037-4045 !$#title The mouse homologue of hst/k-FGF: sequence, genome !1organization and location relative to int-2. !$#cross-references MUID:89296455; PMID:2740210 !$#accession S04741 !'##molecule_type DNA !'##residues 1-202 ##label BRO !'##cross-references GB:X14849; GB:M28516; NID:g52791; PIDN:CAA32967.1; !1PID:g52792 REFERENCE A37360 !$#authors Hebert, J.M.; Basilico, C.; Goldfarb, M.; Haub, O.; Martin, !1G.R. !$#journal Dev. Biol. (1990) 138:454-463 !$#title Isolation of cDNAs encoding four mouse FGF family members !1and characterization of their expression patterns during !1embryogenesis. !$#cross-references MUID:90201563; PMID:2318343 !$#accession A37360 !'##status preliminary !'##molecule_type mRNA !'##residues 1-166,'S',168-202 ##label HEB !'##cross-references GB:M30642; NID:g193290; PIDN:AAA37619.1; !1PID:g309237 GENETICS !$#gene hst CLASSIFICATION #superfamily fibroblast growth factor KEYWORDS growth factor; transforming protein SUMMARY #length 202 #molecular-weight 21902 #checksum 4302 SEQUENCE /// ENTRY TVHUF5 #type complete TITLE fibroblast growth factor 5 - human ALTERNATE_NAMES transforming protein FGF5 ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 17-Mar-2000 ACCESSIONS A31194 REFERENCE A31194 !$#authors Zhan, X.; Bates, B.; Hu, X.; Goldfarb, M. !$#journal Mol. Cell. Biol. (1988) 8:3487-3495 !$#title The human FGF-5 oncogene encodes a novel protein related to !1fibroblast growth factors. !$#cross-references MUID:89096942; PMID:3211147 !$#accession A31194 !'##molecule_type mRNA !'##residues 1-267 ##label ZHA !'##cross-references GB:M23536; GB:M21617; NID:g182539; PIDN:AAB60699.1; !1PID:g182542 GENETICS !$#gene GDB:FGF5 !'##cross-references GDB:119907; OMIM:165190 !$#map_position 4q21-4q21 CLASSIFICATION #superfamily fibroblast growth factor KEYWORDS growth factor; transforming protein SUMMARY #length 267 #molecular-weight 29370 #checksum 6413 SEQUENCE /// ENTRY TVHUT1 #type complete TITLE transforming protein int-1 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 18-Jun-1999 ACCESSIONS A24674 REFERENCE A24674 !$#authors van Ooyen, A.; Kwee, V.; Nusse, R. !$#journal EMBO J. (1985) 4:2905-2909 !$#title The nucleotide sequence of the human int-1 mammary oncogene; !1evolutionary conservation of coding and non-coding !1sequences. !$#cross-references MUID:86055728; PMID:2998762 !$#accession A24674 !'##molecule_type DNA !'##residues 1-370 ##label VAN !'##cross-references GB:X03072; NID:g33935; PIDN:CAA26874.1; PID:g33936 GENETICS !$#gene GDB:WNT1; INT1 !'##cross-references GDB:120101; OMIM:164820 !$#map_position 12q13-12q13 !$#introns 35/2; 120/1; 208/3 CLASSIFICATION #superfamily int-1 transforming protein KEYWORDS proto-oncogene; transforming protein; transmembrane protein FEATURE !$1-48 #domain transmembrane #status predicted #label TMM SUMMARY #length 370 #molecular-weight 40981 #checksum 8314 SEQUENCE /// ENTRY TVMST1 #type complete TITLE transforming protein int-1 - mouse ALTERNATE_NAMES Wnt-1 protein ORGANISM #formal_name Mus musculus #common_name house mouse DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 18-Jun-1999 ACCESSIONS A23447; A36470; A01358 REFERENCE A93068 !$#authors Fung, Y.K.T.; Shackleford, G.M.; Brown, A.M.C.; Sanders, !1G.S.; Varmus, H.E. !$#journal Mol. Cell. Biol. (1985) 5:3337-3344 !$#title Nucleotide sequence and expression in vitro of cDNA derived !1from mRNA of int-1, a provirally activated mouse mammary !1oncogene. !$#cross-references MUID:86310810; PMID:3018519 !$#accession A23447 !'##molecule_type mRNA !'##residues 1-370 ##label FUN !'##cross-references GB:M11943; NID:g198423; PIDN:AAA39322.1; !1PID:g293671 !'##note the authors translated the codon GTG for residue 242 as Gly and !1GGC for codon 243 as Val REFERENCE A36470 !$#authors Gavin, B.J.; McMahon, J.A.; McMahon, A.P. !$#journal Genes Dev. (1990) 4:2319-2332 !$#title Expression of multiple novel Wnt-1/int-1-related genes !1during fetal and adult mouse development. !$#cross-references MUID:91122634; PMID:2279700 !$#accession A36470 !'##status preliminary; nucleic acid sequence not shown; not compared !1with conceptual translation !'##molecule_type mRNA !'##residues 1-370 ##label GAV GENETICS !$#gene int-1 !$#introns 35/2; 120/1; 208/3 CLASSIFICATION #superfamily int-1 transforming protein KEYWORDS proto-oncogene; transforming protein; transmembrane protein FEATURE !$1-48 #domain transmembrane #status predicted #label TMM SUMMARY #length 370 #molecular-weight 41085 #checksum 8529 SEQUENCE /// ENTRY TVMVT1 #type complete TITLE transforming protein int-1 - mouse mammary tumor virus ORGANISM #formal_name mouse mammary tumor virus, MMTV DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 18-Jun-1999 ACCESSIONS B23447; A01358; A23447 REFERENCE A90855 !$#authors Ooyen, A.V.; Nusse, R. !$#journal Cell (1984) 39:233-240 !$#title Structure and nucleotide sequence of the putative mammary !1oncogene int-1; proviral insertions leave the !1protein-encoding domain intact. !$#cross-references MUID:85024897; PMID:6091914 !$#accession B23447 !'##molecule_type DNA !'##residues 1-370 ##label OOY !'##cross-references EMBL:K02593; NID:g198421; PIDN:AAA39321.1; !1PID:g387388 !'##note the authors translated the codon GTG for residue 242 as Gly and !1GGC for codon 243 as Val GENETICS !$#gene int-1 !$#introns 35/2; 120/1; 208/3 CLASSIFICATION #superfamily int-1 transforming protein KEYWORDS oncogene; transforming protein; transmembrane protein FEATURE !$10-28 #domain transmembrane #status predicted #label TMM SUMMARY #length 370 #molecular-weight 41085 #checksum 8529 SEQUENCE /// ENTRY TVXLT1 #type complete TITLE transforming protein int-1 precursor - African clawed frog ALTERNATE_NAMES pxwnt-1 protein ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 18-Jun-1999 ACCESSIONS S02113; S41630 REFERENCE S02113 !$#authors Noordermeer, J.; Meijlink, F.; Verrijzer, P.; Rijsewijk, F.; !1Destree, O. !$#journal Nucleic Acids Res. (1989) 17:11-18 !$#title Isolation of the Xenopus homolog of int-1/wingless and !1expression during neurula stages of early development. !$#cross-references MUID:89098373; PMID:2911462 !$#accession S02113 !'##molecule_type mRNA !'##residues 1-371 ##label NOO !'##cross-references EMBL:X13138; NID:g65235; PIDN:CAA31528.1; !1PID:g65236 REFERENCE S41630 !$#authors Gao, X.; Kuiken, G.A.; Baarends, W.M.; Koster, J.G.; !1Destree, O.H.J. !$#journal Oncogene (1994) 9:573-581 !$#title Characterization of a functional promoter for the Xenopus !1wnt-1 gene in vivo. !$#cross-references MUID:94119599; PMID:8290268 !$#accession S41630 !'##molecule_type DNA !'##residues 1-37 ##label GAO !'##cross-references EMBL:X56845 GENETICS !$#gene int-1 CLASSIFICATION #superfamily int-1 transforming protein KEYWORDS glycoprotein; oncogene; transforming protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-371 #product transforming protein int-1 #status predicted !8#label MAT\ !$28,261,279,306,317, !$360 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 371 #molecular-weight 41125 #checksum 3277 SEQUENCE /// ENTRY TVFFT1 #type complete TITLE transforming protein int-1 - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Feb-1997 ACCESSIONS A31337 REFERENCE A31337 !$#authors Uzvoelgyi, E.; Kiss, I.; Pitt, A.; Arsenian, S.; Ingvarsson, !1S.; Udvardy, A.; Hamada, M.; Klein, G.; Suemegi, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:3034-3038 !$#title Drosophila homolog of the murine Int-1 protooncogene. !$#cross-references MUID:88203634; PMID:3129722 !$#accession A31337 !'##molecule_type mRNA !'##residues 1-469 ##label UZV GENETICS !$#gene int-1 !'##cross-references FlyBase:FBgn0004009 CLASSIFICATION #superfamily int-1 transforming protein KEYWORDS glycoprotein; oncogene; transforming protein FEATURE !$49,103,108,415 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 469 #molecular-weight 51963 #checksum 2575 SEQUENCE /// ENTRY TVMVCB #type complete TITLE transforming protein cb1 - Cas-NS-1 murine sarcoma virus ORGANISM #formal_name Cas-NS-1 murine sarcoma virus DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 02-Jun-1994 ACCESSIONS B32325 REFERENCE A32325 !$#authors Langdon, W.Y.; Hartley, J.W.; Klinken, S.P.; Ruscetti, S.K.; !1Morse III, H.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:1168-1172 !$#title v-cbl, an oncogene from a dual-recombinant murine retrovirus !1that induces early B-lineage lymphomas. !$#cross-references MUID:89145204; PMID:2784003 !$#accession B32325 !'##molecule_type DNA !'##residues 1-390 ##label LAN GENETICS !$#gene cbl CLASSIFICATION #superfamily cbl transforming protein KEYWORDS transforming protein SUMMARY #length 390 #molecular-weight 43692 #checksum 1598 SEQUENCE /// ENTRY TVBE11 #type complete TITLE transforming protein stp - saimiriine herpesvirus 1 (strain 11) ORGANISM #formal_name saimiriine herpesvirus 1 #note host Saimiri sciureus (common squirrel monkey) DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 18-Jun-1999 ACCESSIONS A32389; A36806 REFERENCE A32389 !$#authors Murthy, S.C.S.; Trimble, J.J.; Desrosiers, R.C. !$#journal J. Virol. (1989) 63:3307-3314 !$#title Deletion mutants of herpesvirus saimiri define an open !1reading frame necessary for transformation. !$#cross-references MUID:89311619; PMID:2545905 !$#accession A32389 !'##molecule_type DNA !'##residues 1-164 ##label MUR !'##cross-references GB:M28071; NID:g341821; PIDN:AAA58725.1; !1PID:g609445 REFERENCE A36806 !$#authors Albrecht, J. !$#submission submitted to the EMBL Data Library, January 1992 !$#description Primary structure of the herpesvirus saimiri genome. !$#accession A36806 !'##molecule_type DNA !'##residues 1-164 ##label ALB !'##cross-references GB:X64346; NID:g60320; PIDN:CAA45623.1; PID:g60321 REFERENCE A37309 !$#authors Albrecht, J.C.; Nicholas, J.; Biller, D.; Cameron, K.R.; !1Biesinger, B.; Newman, C.; Wittmann, S.; Craxton, M.A.; !1Coleman, H.; Fleckenstein, B.; Honess, R.W. !$#journal J. Virol. (1992) 66:5047-5058 !$#title Primary structure of the herpesvirus saimiri genome. !$#cross-references MUID:92333688; PMID:1321287 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 1 CLASSIFICATION #superfamily stp transforming protein KEYWORDS transforming protein; transmembrane protein; zinc finger FEATURE !$122-135 #region zinc finger HHCC motif\ !$137-161 #domain transmembrane #status predicted #label TRM SUMMARY #length 164 #molecular-weight 17061 #checksum 315 SEQUENCE /// ENTRY WFPGA #type complete TITLE inhibin alpha chain precursor - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 18-Jun-1999 ACCESSIONS A01392; A25947 REFERENCE A93371 !$#authors Mason, A.J.; Hayflick, J.S.; Ling, N.; Esch, F.; Ueno, N.; !1Ying, S.Y.; Guillemin, R.; Niall, H.; Seeburg, P.H. !$#journal Nature (1985) 318:659-663 !$#title Complementary DNA sequences of ovarian follicular fluid !1inhibin show precursor structure and homology with !1transforming growth factor-beta. !$#cross-references MUID:86092207; PMID:2417121 !$#accession A01392 !'##molecule_type mRNA !'##residues 1-364 ##label MAS !'##cross-references GB:X03265; NID:g1999; PIDN:CAA27019.1; PID:g2000 REFERENCE A94116 !$#authors Mayo, K.E.; Cerelli, G.M.; Spiess, J.; Rivier, J.; !1Rosenfeld, M.G.; Evans, R.M.; Vale, W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:5849-5853 !$#title Inhibin A-subunit cDNAs from porcine ovary and human !1placenta. !$#cross-references MUID:86287350; PMID:3016724 !$#accession A25947 !'##molecule_type mRNA !'##residues 1-119,'R',121-124,'A',126-364 ##label MAY !'##cross-references GB:M13980; NID:g164518; PIDN:AAA31057.1; !1PID:g164519 COMMENT The mature protein is the carboxyl-terminal segment of a !1precursor polypeptide; the active molecule is a dimer of one !1beta and one alpha chain, linked by one or more disulfide !1bonds. Two different forms of inhibin have been isolated (A !1and B) that differ in the amino-terminal sequence of their !1beta chains. COMMENT Inhibin is secreted by ovaries or testes and inhibits the !1secretion of follitropin by the pituitary gland. CLASSIFICATION #superfamily inhibin KEYWORDS contraceptive; follitropin inhibitor; glycoprotein; gonad FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-230 #domain propeptide #status predicted #label PRO\ !$231-364 #product inhibin alpha chain #status predicted #label !8MAT\ !$144,266 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 364 #molecular-weight 39171 #checksum 1835 SEQUENCE /// ENTRY A25732 #type complete TITLE inhibin alpha chain precursor - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A25732; S50897; A30161; A61548 REFERENCE A94097 !$#authors Forage, R.G.; Ring, J.M.; Brown, R.W.; McInerney, B.V.; !1Cobon, G.S.; Gregson, R.P.; Robertson, D.M.; Morgan, F.J.; !1Hearn, M.T.W.; Findlay, J.K.; Wettenhall, R.E.H.; Burger, !1H.G.; De Kretser, D.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:3091-3095 !$#title Cloning and sequence analysis of cDNA species coding for the !1two subunits of inhibin from bovine follicular fluid. !$#cross-references MUID:86205842; PMID:3458167 !$#accession A25732 !'##molecule_type mRNA !'##residues 1-360 ##label FOR !'##cross-references GB:M13273; NID:g163194; PIDN:AAA97414.1; !1PID:g163195 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE S50897 !$#authors Thompson, D.A.; Cronin, C.N.; Martin, F. !$#journal Eur. J. Biochem. (1994) 226:751-764 !$#title Genomic cloning and sequence analyses of the bovine alpha-, !1beta(A)- and beta(B)-inhibin/activin genes. Identification !1of transcription factor AP-2-binding sites in the !15'-flanking regions by DNase I footprinting. !$#cross-references MUID:95112839; PMID:7813465 !$#accession S50897 !'##status preliminary !'##molecule_type DNA !'##residues 1-87 ##label THO !'##cross-references EMBL:U16237; NID:g563744; PIDN:AAB60262.1; !1PID:g563745 REFERENCE A30161 !$#authors Sugino, K.; Nakamura, T.; Takio, K.; Titani, K.; Miyamoto, !1K.; Hasegawa, Y.; Igarashi, M.; Sugino, H. !$#journal Biochem. Biophys. Res. Commun. (1989) 159:1323-1329 !$#title Inhibin alpha-subunit monomer is present in bovine !1follicular fluid. !$#cross-references MUID:89193729; PMID:2930562 !$#accession A30161 !'##molecule_type protein !'##residues 18-37;227-246 ##label SUG REFERENCE A61548 !$#authors Fukuda, M.; Miyamoto, K.; Hasegawa, Y.; Nomura, M.; !1Igarashi, M.; Kangawa, K.; Matsuo, H. !$#journal Mol. Cell. Endocrinol. (1986) 44:55-60 !$#title Isolation of bovine follicular fluid inhibin of about 32 !1kDa. !$#cross-references MUID:86136989; PMID:3081385 !$#accession A61548 !'##molecule_type protein !'##residues 227-230 ##label FUK COMMENT Inhibin suppresses follicle-stimulating hormone secretion. CLASSIFICATION #superfamily inhibin KEYWORDS disulfide bond; glycoprotein; gonad; heterodimer; hormone FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-226 #domain propeptide #status predicted #label PRO\ !$227-360 #product inhibin alpha chain #status predicted #label !8MAT\ !$140,262 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 360 #molecular-weight 38809 #checksum 8036 SEQUENCE /// ENTRY A24248 #type complete TITLE inhibin alpha chain precursor - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Dec-2000 ACCESSIONS A23556; B25947; A24248 REFERENCE A91366 !$#authors Stewart, A.G.; Milborrow, H.M.; Ring, J.M.; Crowther, C.E.; !1Forage, R.G. !$#journal FEBS Lett. (1986) 206:329-334 !$#title Human inhibin genes. Genomic characterisation and !1sequencing. !$#cross-references MUID:87005283; PMID:3758355 !$#accession A23556 !'##molecule_type DNA !'##residues 1-366 ##label STE !'##cross-references GB:X04445; NID:g33921; PIDN:CAA28040.1; !1PID:g1204105 REFERENCE A94116 !$#authors Mayo, K.E.; Cerelli, G.M.; Spiess, J.; Rivier, J.; !1Rosenfeld, M.G.; Evans, R.M.; Vale, W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:5849-5853 !$#title Inhibin A-subunit cDNAs from porcine ovary and human !1placenta. !$#cross-references MUID:86287350; PMID:3016724 !$#accession B25947 !'##molecule_type mRNA !'##residues 1-366 ##label MAY !'##cross-references GB:M13981; NID:g186410; PIDN:AAA59166.1; !1PID:g307068 REFERENCE A90123 !$#authors Mason, A.J.; Niall, H.D.; Seeburg, P.H. !$#journal Biochem. Biophys. Res. Commun. (1986) 135:957-964 !$#title Structure of two human ovarian inhibins. !$#cross-references MUID:86186863; PMID:3754442 !$#accession A24248 !'##molecule_type mRNA !'##residues 16,'V',18,'S',20-366 ##label MAS !'##cross-references GB:M13144; NID:g186412; PIDN:AAA59167.1; !1PID:g186413 COMMENT Activins A and B are homodimers of inhibin beta-A or inhibin !1beta-B, respectively, while activin AB is a heterodimer. !1Inhibins A and B are heterodimers of the inhibin alpha chain !1with inhibin beta-A and beta-B, respectively. GENETICS !$#gene GDB:INHA !'##cross-references GDB:120100; OMIM:147380 !$#map_position 2q33-2q36 !$#introns 90/1 CLASSIFICATION #superfamily inhibin KEYWORDS glycoprotein; gonad; heterodimer; hormone FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-232 #domain propeptide #status predicted #label PRO\ !$233-366 #product inhibin alpha chain #status predicted #label !8MAT\ !$146,268,302 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 366 #molecular-weight 39669 #checksum 7076 SEQUENCE /// ENTRY JC1106 #type complete TITLE inhibin alpha chain precursor - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 01-Dec-2000 #text_change 01-Dec-2000 ACCESSIONS JC1106; A60490; I48243; S31439 REFERENCE JC1106 !$#authors Su, J.G.W.; Hsueh, A.J.W. !$#journal Biochem. Biophys. Res. Commun. (1992) 186:293-300 !$#title Characterization of mouse inhibin alpha gene and its !1promoter. !$#cross-references MUID:92337610; PMID:1632772 !$#accession JC1106 !'##molecule_type DNA !'##residues 1-164,'R',166-366 ##label SUJ !'##cross-references GB:M95525; NID:g198404; PIDN:AAA39314.1; !1PID:g459875; GB:M95526 REFERENCE A60490 !$#authors Tone, S.; Katoh, Y.; Fujimoto, H.; Togashi, S.; Yanazawa, !1M.; Kato, Y.; Higashinakagawa, T. !$#journal Differentiation (1990) 44:62-68 !$#title Expression of inhibin alpha-subunit gene during mouse !1gametogenesis. !$#cross-references MUID:91071531; PMID:2253839 !$#accession A60490 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 49-366 ##label TON !'##cross-references GB:X55957; NID:g296837; PIDN:CAA39424.1; !1PID:g296838 !'##experimental_source Swiss Webster REFERENCE I48243 !$#authors Albano, R.M.; Groome, N.; Smith, J.C. !$#journal Development (1993) 117:711-723 !$#title Activins are expressed in preimplantation mouse embryos and !1in ES and EC cells and are regulated on their !1differentiation. !$#cross-references MUID:93321614; PMID:8330535 !$#accession I48243 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-170,'V',172-335,'T',337-366 ##label ALB !'##cross-references EMBL:X69618; NID:g49936; PIDN:CAA49324.1; !1PID:g49937 COMMENT This protein inhibits the secretion and synthesis of !1follicle-stimulating hormone. COMMENT This alpha chain is linked by two disulfide bonds to the !1beta-A chain in inhibin A, or to the beta-B chain in inhibin !1B. GENETICS !$#introns 91/1 CLASSIFICATION #superfamily inhibin KEYWORDS glycoprotein; gonad; heterodimer FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-233 #domain propeptide #status predicted #label PRO\ !$234-366 #product inhibin alpha chain #status predicted #label !8MAT\ !$147,269 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 366 #molecular-weight 39549 #checksum 2800 SEQUENCE /// ENTRY A40056 #type complete TITLE inhibin alpha chain precursor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 08-Dec-2000 ACCESSIONS A41398; A40056; A40905 REFERENCE A41398 !$#authors Feng, Z.M.; Li, Y.P.; Chen, C.L.C. !$#journal Mol. Endocrinol. (1989) 3:1914-1925 !$#title Analysis of the 5'-flanking regions of rat inhibin alpha- !1and beta-B-subunit genes suggests two different regulatory !1mechanisms. !$#cross-references MUID:90190649; PMID:2628729 !$#accession A41398 !'##status preliminary !'##molecule_type DNA !'##residues 1-366 ##label FEN !'##cross-references GB:M32754; GB:M32755; NID:g204939; PIDN:AAA41437.1; !1PID:g204941 REFERENCE A40056 !$#authors Woodruff, T.K.; Meunier, H.; Jones, P.B.C.; Hsueh, A.J.W.; !1Mayo, K.E. !$#journal Mol. Endocrinol. (1987) 1:561-568 !$#title Rat inhibin: molecular cloning of alpha- and beta-subunit !1complementary deoxyribonucleic acids and expression in the !1ovary. !$#cross-references MUID:91042598; PMID:3153478 !$#accession A40056 !'##status preliminary !'##molecule_type mRNA !'##residues 1-366 ##label WOO !'##cross-references GB:M36453; NID:g204934; PIDN:AAA41435.1; !1PID:g204935 REFERENCE A40905 !$#authors Esch, F.S.; Shimasaki, S.; Cooksey, K.; Mercado, M.; Mason, !1A.J.; Ying, S.Y.; Ueno, N.; Ling, N. !$#journal Mol. Endocrinol. (1987) 1:388-396 !$#title Complementary deoxyribonucleic acid (cDNA) cloning and DNA !1sequence analysis of rat ovarian inhibins. !$#cross-references MUID:90331931; PMID:2484214 !$#accession A40905 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-366 ##label ESC CLASSIFICATION #superfamily inhibin KEYWORDS glycoprotein FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-233 #domain propeptide #status predicted #label PRO\ !$234-366 #product inhibin alpha chain #status predicted #label !8MAT\ !$147,269 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 366 #molecular-weight 39496 #checksum 2766 SEQUENCE /// ENTRY B24248 #type complete TITLE inhibin beta-A chain precursor [validated] - human ALTERNATE_NAMES activin A; activin AB chain A; erythroid differentiation factor; megakaryocyte differentiation active protein ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 08-Dec-2000 ACCESSIONS S30488; B23556; B24248; A30884; S33351; PN0010 REFERENCE S30488 !$#authors Tanimoto, K.; Handa, S.I.; Ueno, N.; Murakami, K.; Fukamizu, !1A. !$#journal DNA Seq. (1991) 2:103-110 !$#title Structure and sequence analysis of the human activin beta(A) !1subunit gene. !$#cross-references MUID:92135888; PMID:1777673 !$#accession S30488 !'##status preliminary !'##molecule_type DNA !'##residues 1-426 ##label TAN !'##cross-references EMBL:X57578; NID:g28351; PIDN:CAA40805.1; !1PID:g825621 !'##note the authors translated the codon GAG for residue 53 as Gly and !1GAG for residue 56 as Gly REFERENCE A91366 !$#authors Stewart, A.G.; Milborrow, H.M.; Ring, J.M.; Crowther, C.E.; !1Forage, R.G. !$#journal FEBS Lett. (1986) 206:329-334 !$#title Human inhibin genes. Genomic characterisation and !1sequencing. !$#cross-references MUID:87005283; PMID:3758355 !$#accession B23556 !'##molecule_type DNA !'##residues 311-426 ##label STE !'##cross-references GB:X04447; NID:g33928; PIDN:CAA28041.1; PID:g33929 REFERENCE A90123 !$#authors Mason, A.J.; Niall, H.D.; Seeburg, P.H. !$#journal Biochem. Biophys. Res. Commun. (1986) 135:957-964 !$#title Structure of two human ovarian inhibins. !$#cross-references MUID:86186863; PMID:3754442 !$#accession B24248 !'##molecule_type mRNA !'##residues 1-426 ##label MAS !'##cross-references GB:M13436; NID:g186414; PIDN:AAA59168.1; !1PID:g307069 REFERENCE A30884 !$#authors Murata, M.; Eto, Y.; Shibai, H.; Sakai, M.; Muramatsu, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:2434-2438 !$#title Erythroid differentiation factor is encoded by the same mRNA !1as that of the inhibin beta-A chain. !$#cross-references MUID:88190086; PMID:3267209 !$#accession A30884 !'##molecule_type mRNA !'##residues 1-426 ##label MUR !'##cross-references GB:J03634; NID:g181946; PIDN:AAA35787.1; !1PID:g181947 REFERENCE S33351 !$#authors Berg, H.; Walter, M.; Northemann, W. !$#submission submitted to the EMBL Data Library, April 1993 !$#description Nucleotide sequence coding for the mature subunit beta(A) of !1human inhibin in testis. !$#accession S33351 !'##status preliminary !'##molecule_type mRNA !'##residues 311-376,'AC',380-426 ##label BER !'##cross-references EMBL:X72498; NID:g297786; PIDN:CAA51163.1; !1PID:g755740 REFERENCE PN0010 !$#authors Fujimoto, K.; Kawakita, M.; Kato, K.; Yonemura, Y.; Masuda, !1T.; Matsuzaki, H.; Hirose, J.; Isaji, M.; Sasaki, H.; Inoue, !1T.; Takatsuki, K. !$#journal Biochem. Biophys. Res. Commun. (1991) 174:1163-1168 !$#title Purification of megakaryocyte differentiation activity from !1a human fibrous histiocytoma cell line: N-terminal sequence !1homology with activin A. !$#cross-references MUID:91144591; PMID:1847627 !$#accession PN0010 !'##molecule_type protein !'##residues 311-313,'X',315-320,'XX',323-328,'X',330-334 ##label FUJ COMMENT Activins A and B are homodimers of inhibin beta-A or inhibin !1beta-B, respectively, while activin AB is a heterodimer. !1Inhibins A and B are heterodimers of the inhibin alpha chain !1with inhibin beta-A and beta-B, respectively. GENETICS !$#gene GDB:INHBA !'##cross-references GDB:119346; OMIM:147290 !$#map_position 7p15-7p13 !$#introns 129/3 CLASSIFICATION #superfamily inhibin KEYWORDS glycoprotein; gonad; heterodimer; homodimer; hormone FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-310 #domain propeptide #status predicted #label PRO\ !$311-426 #product inhibin beta A chain #status experimental !8#label MAT\ !$165 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 426 #molecular-weight 47442 #checksum 3853 SEQUENCE /// ENTRY WFPGBA #type complete TITLE inhibin beta-A chain precursor - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 13-Aug-1986 #sequence_revision 13-Aug-1986 #text_change 18-Jun-1999 ACCESSIONS A01393 REFERENCE A93371 !$#authors Mason, A.J.; Hayflick, J.S.; Ling, N.; Esch, F.; Ueno, N.; !1Ying, S.Y.; Guillemin, R.; Niall, H.; Seeburg, P.H. !$#journal Nature (1985) 318:659-663 !$#title Complementary DNA sequences of ovarian follicular fluid !1inhibin show precursor structure and homology with !1transforming growth factor-beta. !$#cross-references MUID:86092207; PMID:2417121 !$#accession A01393 !'##molecule_type mRNA !'##residues 1-424 ##label MAS !'##cross-references GB:X03266; NID:g2002; PIDN:CAA27020.1; PID:g2003 COMMENT The source of this protein is ovarian follicular fluid. COMMENT The mature protein is the carboxyl-terminal segment of a !1precursor polypeptide; the active molecule is a dimer of one !1beta and one alpha chain, linked by one or more disulfide !1bonds. Two different forms of inhibin have been isolated (A !1and B) that differ in the amino-terminal sequence of their !1beta chains. COMMENT Inhibin is secreted by ovaries or testes and inhibits the !1secretion of follitropin by the pituitary gland. CLASSIFICATION #superfamily inhibin KEYWORDS contraceptive; follitropin inhibitor; glycoprotein; gonad FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-308 #domain propeptide #status predicted #label PRO\ !$309-424 #product inhibin beta-A chain #status predicted !8#label MAT\ !$165 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 424 #molecular-weight 47476 #checksum 1246 SEQUENCE /// ENTRY S31440 #type complete TITLE inhibin beta-A chain - mouse ALTERNATE_NAMES activin A; mesoderm-inducing factor WEHI-MIF ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A60087; I48265; S31440 REFERENCE A60087 !$#authors Albano, R.M.; Godsave, S.F.; Huylebroeck, D.; Van Nimmen, !1K.; Isaacs, H.V.; Slack, J.M.W.; Smith, J.C. !$#journal Development (1990) 110:435-443 !$#title A mesoderm-inducing factor produced by WEHI-3 murine !1myelomonocytic leukemia cells is activin A. !$#cross-references MUID:92155098; PMID:2133547 !$#accession A60087 !'##molecule_type protein !'##residues 309-311,'X',313-318,'XX',321-325 ##label AL2 REFERENCE I48243 !$#authors Albano, R.M.; Groome, N.; Smith, J.C. !$#journal Development (1993) 117:711-723 !$#title Activins are expressed in preimplantation mouse embryos and !1in ES and EC cells and are regulated on their !1differentiation. !$#cross-references MUID:93321614; PMID:8330535 !$#accession I48265 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-424 ##label RES !'##cross-references EMBL:X69619; NID:g50145; PIDN:CAA49325.1; !1PID:g50146 CLASSIFICATION #superfamily inhibin SUMMARY #length 424 #molecular-weight 47392 #checksum 2136 SEQUENCE /// ENTRY S50898 #type complete TITLE inhibin beta-A chain precursor - bovine ALTERNATE_NAMES activin; mesoderm inducing factor ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S50898; B25732; A60960; B61548 REFERENCE S50897 !$#authors Thompson, D.A.; Cronin, C.N.; Martin, F. !$#journal Eur. J. Biochem. (1994) 226:751-764 !$#title Genomic cloning and sequence analyses of the bovine alpha-, !1beta(A)- and beta(B)-inhibin/activin genes. Identification !1of transcription factor AP-2-binding sites in the !15'-flanking regions by DNase I footprinting. !$#cross-references MUID:95112839; PMID:7813465 !$#accession S50898 !'##status preliminary !'##molecule_type DNA !'##residues 1-425 ##label THO !'##cross-references EMBL:U16238 REFERENCE A94097 !$#authors Forage, R.G.; Ring, J.M.; Brown, R.W.; McInerney, B.V.; !1Cobon, G.S.; Gregson, R.P.; Robertson, D.M.; Morgan, F.J.; !1Hearn, M.T.W.; Findlay, J.K.; Wettenhall, R.E.H.; Burger, !1H.G.; De Kretser, D.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:3091-3095 !$#title Cloning and sequence analysis of cDNA species coding for the !1two subunits of inhibin from bovine follicular fluid. !$#cross-references MUID:86205842; PMID:3458167 !$#accession B25732 !'##molecule_type mRNA !'##residues 258-425 ##label FOR !'##cross-references GB:M13274; NID:g163196; PIDN:AAA97415.1; !1PID:g163197 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE A60960 !$#authors Chertov, O.Y.; Krasnosel'skii, A.L.; Bogdanov, M.E.; !1Hoperskaya, O.A. !$#journal Biomed. Sci. (1990) 1:499-506 !$#title Mesoderm-inducing factor from bovine amniotic fluid: !1purification and N-terminal amino acid sequence !1determination. !$#cross-references MUID:92126853; PMID:2133067 !$#accession A60960 !'##molecule_type protein !'##residues 310-312,'X',314-319,'XX',322-328,'P' ##label CHE REFERENCE A61548 !$#authors Fukuda, M.; Miyamoto, K.; Hasegawa, Y.; Nomura, M.; !1Igarashi, M.; Kangawa, K.; Matsuo, H. !$#journal Mol. Cell. Endocrinol. (1986) 44:55-60 !$#title Isolation of bovine follicular fluid inhibin of about 32 !1kDa. !$#cross-references MUID:86136989; PMID:3081385 !$#accession B61548 !'##molecule_type protein !'##residues 310-313 ##label FUK GENETICS !$#introns 130/1 CLASSIFICATION #superfamily inhibin KEYWORDS disulfide bond; glycoprotein; gonad; heterodimer; homodimer; !1hormone FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-309 #domain propeptide #status predicted #label PRO\ !$310-425 #product beta-A inhibin/activin #status experimental !8#label MAT\ !$165 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 425 #molecular-weight 47521 #checksum 898 SEQUENCE /// ENTRY B40905 #type complete TITLE inhibin beta-A chain precursor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B40905; B40056 REFERENCE A40905 !$#authors Esch, F.S.; Shimasaki, S.; Cooksey, K.; Mercado, M.; Mason, !1A.J.; Ying, S.Y.; Ueno, N.; Ling, N. !$#journal Mol. Endocrinol. (1987) 1:388-396 !$#title Complementary deoxyribonucleic acid (cDNA) cloning and DNA !1sequence analysis of rat ovarian inhibins. !$#cross-references MUID:90331931; PMID:2484214 !$#accession B40905 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-424 ##label ESC REFERENCE A40056 !$#authors Woodruff, T.K.; Meunier, H.; Jones, P.B.C.; Hsueh, A.J.W.; !1Mayo, K.E. !$#journal Mol. Endocrinol. (1987) 1:561-568 !$#title Rat inhibin: molecular cloning of alpha- and beta-subunit !1complementary deoxyribonucleic acids and expression in the !1ovary. !$#cross-references MUID:91042598; PMID:3153478 !$#accession B40056 !'##status preliminary !'##molecule_type mRNA !'##residues 1-366,'H',368-424 ##label WOO !'##cross-references GB:M37482; NID:g204936; PIDN:AAA41436.1; !1PID:g204937 CLASSIFICATION #superfamily inhibin SUMMARY #length 424 #molecular-weight 47356 #checksum 1734 SEQUENCE /// ENTRY A40150 #type complete TITLE inhibin beta-B chain precursor - human ALTERNATE_NAMES activin AB chain B ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Dec-2000 ACCESSIONS A40150; C24248; A40156; S10751 REFERENCE A40150 !$#authors Mason, A.J.; Berkemeier, L.M.; Schmelzer, C.H.; Schwall, !1R.H. !$#journal Mol. Endocrinol. (1989) 3:1352-1358 !$#title Activin B: precursor sequences, genomic structure and in !1vitro activities. !$#cross-references MUID:90114200; PMID:2575216 !$#accession A40150 !'##molecule_type DNA !'##residues 1-407 ##label MAS !'##cross-references GB:M31668; GB:M31669; NID:g186419; PIDN:AAA59451.1; !1PID:g386827 REFERENCE A90123 !$#authors Mason, A.J.; Niall, H.D.; Seeburg, P.H. !$#journal Biochem. Biophys. Res. Commun. (1986) 135:957-964 !$#title Structure of two human ovarian inhibins. !$#cross-references MUID:86186863; PMID:3754442 !$#accession C24248 !'##molecule_type mRNA !'##residues 55-407 ##label MA2 !'##cross-references GB:M13437; NID:g186416; PIDN:AAA59169.1; !1PID:g186417 REFERENCE A40156 !$#authors Feng, Z.M.; Bardin, C.W.; Chen, C.L.C. !$#journal Mol. Endocrinol. (1989) 3:939-948 !$#title Characterization and regulation of testicular inhibin !1beta-subunit mRNA. !$#cross-references MUID:89295443; PMID:2739657 !$#accession A40156 !'##molecule_type mRNA !'##residues 22-46,'A',48-407 ##label FEN !'##cross-references GB:M31632 !'##experimental_source testis REFERENCE S10751 !$#authors Schmelzer, C.H.; Burton, L.E.; Tamony, C.M.; Schwall, R.H.; !1Mason, A.J.; Liegeois, N. !$#journal Biochim. Biophys. Acta (1990) 1039:135-141 !$#title Purification and characterization of recombinant human !1activin B. !$#cross-references MUID:90304183; PMID:2364091 !$#accession S10751 !'##molecule_type protein !'##residues 293-294,'GX',297-302,'XX',305-307 ##label SCH COMMENT Activins A and B are homodimers of inhibin beta-A or inhibin !1beta-B, respectively, while activin AB is a heterodimer. !1Inhibins A and B are heterodimers of the inhibin alpha chain !1with inhibin beta-A and beta-B, respectively. GENETICS !$#gene GDB:INHBB !'##cross-references GDB:119347; OMIM:147390 !$#map_position 2cen-2q13 CLASSIFICATION #superfamily inhibin KEYWORDS glycoprotein; gonad; heterodimer; homodimer; hormone FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-292 #domain propeptide #status predicted #label PRO\ !$293 #product inhibin beta-B chain #status predicted !8#label MAT\ !$93 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 407 #molecular-weight 45121 #checksum 9126 SEQUENCE /// ENTRY WFPGBB #type fragment TITLE inhibin beta-B chain precursor - pig (fragment) ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 01-Dec-2000 ACCESSIONS A01394 REFERENCE A93371 !$#authors Mason, A.J.; Hayflick, J.S.; Ling, N.; Esch, F.; Ueno, N.; !1Ying, S.Y.; Guillemin, R.; Niall, H.; Seeburg, P.H. !$#journal Nature (1985) 318:659-663 !$#title Complementary DNA sequences of ovarian follicular fluid !1inhibin show precursor structure and homology with !1transforming growth factor-beta. !$#cross-references MUID:86092207; PMID:2417121 !$#accession A01394 !'##molecule_type mRNA !'##residues 1-349 ##label MAS !'##cross-references GB:X03267; NID:g2005; PIDN:CAA27021.1; PID:g2006 COMMENT The source of this protein is ovarian follicular fluid. COMMENT The mature protein is the carboxyl-terminal segment of a !1precursor polypeptide; the active molecule is a dimer of one !1beta and one alpha chain, linked by one or more disulfide !1bonds. Two different forms of inhibin have been isolated (A !1and B) that differ in the amino-terminal sequence of their !1beta chains. COMMENT Inhibin is secreted by ovaries or testes and inhibits the !1secretion of follitropin by the pituitary gland. CLASSIFICATION #superfamily inhibin KEYWORDS contraceptive; follitropin inhibitor; glycoprotein; gonad FEATURE !$1-234 #domain propeptide (fragment) #status predicted !8#label PRO\ !$235-349 #product inhibin beta-B chain #status predicted !8#label MAT\ !$35 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 349 #checksum 1666 SEQUENCE /// ENTRY WFHU2 #type complete TITLE transforming growth factor beta-1 precursor [validated] - human ALTERNATE_NAMES growth-inhibitory factor; TGF type 2; TGF-beta ORGANISM #formal_name Homo sapiens #common_name man DATE 28-Feb-1986 #sequence_revision 19-Oct-1995 #text_change 08-Dec-2000 ACCESSIONS A27513; A01395; A22290; I59664; S53444 REFERENCE A27513 !$#authors Derynck, R.; Rhee, L.; Chen, E.Y.; Van Tilburg, A. !$#journal Nucleic Acids Res. (1987) 15:3188-3189 !$#title Intron-exon structure of the human transforming growth !1factor-beta precursor gene. !$#cross-references MUID:87174845; PMID:3470709 !$#accession A27513 !'##molecule_type DNA !'##residues 1-390 ##label DER !'##cross-references GB:X05839; GB:Y00112; NID:g37097; PIDN:CAA29283.1; !1PID:g1212989 REFERENCE A01395 !$#authors Derynck, R.; Jarrett, J.A.; Chen, E.Y.; Eaton, D.H.; Bell, !1J.R.; Assoian, R.K.; Roberts, A.B.; Sporn, M.B.; Goeddel, !1D.V. !$#journal Nature (1985) 316:701-705 !$#title Human transforming growth factor-beta complementary DNA !1sequence and expression in normal and transformed cells. !$#cross-references MUID:85296301; PMID:3861940 !$#accession A01395 !'##molecule_type mRNA !'##residues 1-9,'P',11-24,'P',26-159,'R',160-390 ##label DE2 !'##cross-references GB:X02812; GB:J05114; NID:g37092; PIDN:CAA26580.1; !1PID:g37093 !'##note the authors suggest that residues 8-23 could represent the !1hydrophobic core of an amino-terminal signal peptide REFERENCE A22290 !$#authors Massague, J.; Like, B. !$#journal J. Biol. Chem. (1985) 260:2636-2645 !$#title Cellular receptors for type beta transforming growth factor. !1Ligand binding and affinity labeling in human and rodent !1cell lines. !$#cross-references MUID:85131019; PMID:2982829 !$#accession A22290 !'##molecule_type protein !'##residues 279-295,'XX',298-301 ##label MAS REFERENCE I59664 !$#authors Urushizaki, Y.; Niitsu, Y.; Terui, T.; Koshida, Y.; Mahara, !1K.; Kohgo, Y.; Urushizaki, I.; Takahashi, Y.; Ito, H. !$#journal Tumor Res. (1987) 22:41-55 !$#title Cloning and expression of the gene for human transforming !1growth factor-beta in Escherichia coli. !$#accession I59664 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 279-390 ##label RES !'##cross-references GB:M38449; NID:g339557; PIDN:AAA36735.1; !1PID:g339558 REFERENCE S53444 !$#authors Stam, K.; Stewart, A.A.; Qu, G.Y.; Iwata, K.K.; Fenyoe, D.; !1Chait, B.T.; Marshak, D.R.; Haley, J.D. !$#journal Biochem. J. (1995) 305:87-92 !$#title Physical and biological characterization of a !1growth-inhibitory activity purified from the !1neuroepithelioma cell line A673. !$#cross-references MUID:95126934; PMID:7826358 !$#accession S53444 !'##status preliminary !'##molecule_type protein !'##residues 279-297 ##label STA COMMENT The mature protein is the carboxyl-terminal segment of a !1precursor polypeptide; the active molecule is a dimer of !1identical polypeptide chains linked by an interchain !1disulfide bond. GENETICS !$#gene GDB:TGFB1; TGFB !'##cross-references GDB:120729; OMIM:190180 !$#map_position 19q13.2-19q13.2 CLASSIFICATION #superfamily inhibin KEYWORDS glycoprotein; growth factor; homodimer; mitogen; !1transformation FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-278 #domain propeptide #status predicted #label PRO\ !$244-246 #region cell attachment (R-G-D) motif\ !$279-390 #product transforming growth factor beta-1 #status !8experimental #label MAT\ !$82,136,176 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 390 #molecular-weight 44341 #checksum 1750 SEQUENCE /// ENTRY WFMS2 #type complete TITLE transforming growth factor beta-1 precursor - mouse ALTERNATE_NAMES TGF type 2; TGF-beta ORGANISM #formal_name Mus musculus #common_name house mouse DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 24-Nov-1999 ACCESSIONS A01396 REFERENCE A01396 !$#authors Derynck, R.; Jarrett, J.A.; Chen, E.Y.; Goeddel, D.V. !$#journal J. Biol. Chem. (1986) 261:4377-4379 !$#title The murine transforming growth factor-beta precursor. !$#cross-references MUID:86168129; PMID:3007454 !$#accession A01396 !'##molecule_type mRNA !'##residues 1-390 ##label DER !'##cross-references GB:M13177; NID:g201952; PIDN:AAA40423.1; !1PID:g201953 !'##note the authors suggest that residues 8-23 could represent the !1hydrophobic core of an amino-terminal signal peptide COMMENT The mature protein is the carboxyl-terminal segment of a !1precursor polypeptide; the active molecule is a dimer of !1identical polypeptide chains linked by an interchain !1disulfide bond. CLASSIFICATION #superfamily inhibin KEYWORDS glycoprotein; growth factor; growth regulation; homodimer; !1mitogen; transformation FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-278 #domain propeptide #status predicted #label PRO\ !$244-246 #region cell attachment (R-G-D) motif\ !$279-390 #product transforming growth factor beta-1 #status !8predicted #label MAT\ !$82,136,176 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 390 #molecular-weight 44310 #checksum 1901 SEQUENCE /// ENTRY WFMKB2 #type complete TITLE transforming growth factor beta-2 precursor, short form - green monkey ALTERNATE_NAMES BSC-1 cell growth inhibitor; cartilage-inducing factor B; polyergin ORGANISM #formal_name Cercopithecus aethiops #common_name green monkey, grivet DATE 23-Mar-1990 #sequence_revision 19-Oct-1995 #text_change 18-Jun-1999 ACCESSIONS A34005 REFERENCE A34005 !$#authors Hanks, S.K.; Armour, R.; Baldwin, J.H.; Maldonado, F.; !1Spiess, J.; Holley, R.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:79-82 !$#title Amino acid sequence of the BSC-1 cell growth inhibitor !1(polyergin) deduced from the nucleotide sequence of the !1cDNA. !$#cross-references MUID:88124824; PMID:3277172 !$#accession A34005 !'##molecule_type mRNA !'##residues 1-414 ##label HAN !'##cross-references GB:J03585; NID:g176495; PIDN:AAA35358.1; !1PID:g176496 !'##note part of this sequence, including the amino end of the active !1peptide, confirmed by protein sequencing REFERENCE A90960 !$#authors Webb, N.R.; Madisen, L.; Rose, T.M.; Purchio, A.F. !$#journal DNA (1988) 7:493-497 !$#title Structural and sequence analysis of TGF-beta-2 cDNA clones !1predicts two different precursor proteins produced by !1alternative mRNA splicing. !$#cross-references MUID:89090808; PMID:2850146 !$#contents annotation !$#note although they do not show the sequences, a clone identical !1yielding a sequence identical with A34005 was sequenced; !1another clone was partially sequenced and found to have an !1insert identical with that in the long form of the human !1sequence CLASSIFICATION #superfamily inhibin KEYWORDS alternative splicing; glycoprotein; growth factor; growth !1regulation; homodimer; mitogen FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-302 #domain propeptide #status predicted #label PRO\ !$303-414 #product transforming growth factor beta-2 #status !8predicted #label MAT\ !$72,140,241 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 414 #molecular-weight 47747 #checksum 5111 SEQUENCE /// ENTRY WFMSB2 #type complete TITLE transforming growth factor beta-2 precursor - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Jun-1999 ACCESSIONS A40148 REFERENCE A40148 !$#authors Miller, D.A.; Lee, A.; Pelton, R.W.; Chen, E.Y.; Moses, !1H.L.; Derynck, R. !$#journal Mol. Endocrinol. (1989) 3:1108-1114 !$#title Murine transforming growth factor-beta2 cDNA sequence and !1expression in adult tissues and embryos. !$#cross-references MUID:90014832; PMID:2797004 !$#accession A40148 !'##molecule_type mRNA !'##residues 1-414 ##label MIL !'##cross-references EMBL:X57413; NID:g54772; PIDN:CAA40672.1; !1PID:g54773 COMMENT None of the three predicted glycosylation sites is in the !1mature protein. CLASSIFICATION #superfamily inhibin KEYWORDS glycoprotein; growth factor; growth regulation; homodimer; !1mitogen FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-302 #domain propeptide #status predicted #label PRO\ !$303-414 #product transforming growth factor beta-2 #status !8predicted #label MAT\ !$72,140,241 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 414 #molecular-weight 47601 #checksum 6120 SEQUENCE /// ENTRY WFXLB2 #type complete TITLE transforming growth factor beta-2 precursor - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 12-Feb-1993 #sequence_revision 19-Oct-1995 #text_change 18-Jun-1999 ACCESSIONS S09510; A61036 REFERENCE S09510 !$#authors Rebbert, M.L.; Bhatia-Dey, N.; Dawid, I.B. !$#journal Nucleic Acids Res. (1990) 18:2185 !$#title The sequence of TGF-beta2 from Xenopus laevis. !$#cross-references MUID:90245678; PMID:2336403 !$#accession S09510 !'##molecule_type mRNA !'##residues 1-413 ##label REB !'##cross-references EMBL:X51817; NID:g414789; PIDN:CAA36116.1; !1PID:g65137 REFERENCE A61036 !$#authors Roberts, A.B.; Rosa, F.; Roche, N.S.; Coligan, J.E.; !1Garfield, M.; Rebbert, M.L.; Kondaiah, P.; Danielpour, D.; !1Kehrl, J.H.; Wahl, S.M.; Dawid, I.B.; Sporn, M.B. !$#journal Growth Factors (1990) 2:135-147 !$#title Isolation and characterization of TGF-beta2 and TGF-beta5 !1from medium conditioned by Xenopus XTC cells. !$#cross-references MUID:90253806; PMID:2340184 !$#accession A61036 !'##molecule_type protein !'##residues 302-307,'X',309-315,'XX',318-319 ##label ROB CLASSIFICATION #superfamily inhibin KEYWORDS glycoprotein; growth factor; growth regulation; homodimer; !1mitogen FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-301 #domain propeptide #status predicted #label PRO\ !$302-413 #product transforming growth factor beta-2 #status !8predicted #label MAT\ !$72,140,241 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 413 #molecular-weight 47639 #checksum 3655 SEQUENCE /// ENTRY WFHUM #type complete TITLE mullerian inhibiting factor precursor - human ALTERNATE_NAMES anti-Mullerian hormone; mullerian inhibiting substance (MIS) ORGANISM #formal_name Homo sapiens #common_name man DATE 13-Aug-1986 #sequence_revision 13-Aug-1986 #text_change 18-Jun-1999 ACCESSIONS A01397 REFERENCE A90879 !$#authors Cate, R.L.; Mattaliano, R.J.; Hession, C.; Tizard, R.; !1Farber, N.M.; Cheung, A.; Ninfa, E.G.; Frey, A.Z.; Gash, !1D.J.; Chow, E.P.; Fisher, R.A.; Bertonis, J.M.; Torres, G.; !1Wallner, B.P.; Ramachandran, K.L.; Ragin, R.C.; Manganaro, !1T.F.; MacLaughlin, D.T.; Donahoe, P.K. !$#journal Cell (1986) 45:685-698 !$#title Isolation of the bovine and human genes for Muellerian !1inhibiting substance and expression of the human gene in !1animal cells. !$#cross-references MUID:86218082; PMID:3754790 !$#accession A01397 !'##molecule_type DNA !'##residues 1-560 ##label CAT !'##cross-references GB:K03474; NID:g188560; PIDN:AAA98805.1; !1PID:g386953 COMMENT Although it does not compete with EGF for receptor binding !1sites, MIS can inhibit the autophosphorylation of the EGF !1receptor in vitro. COMMENT For anti-Mullerian hormone type II receptor, see PIR:JC4335. GENETICS !$#gene GDB:AMH !'##cross-references GDB:118996; OMIM:261550; OMIM:600957 !$#map_position 19p13.3-19p13.3 !$#introns 138/1; 185/3; 222/1; 275/2 CLASSIFICATION #superfamily inhibin KEYWORDS cytotoxin; glycoprotein; gonadal differentiation; hormone; !1testis FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-25 #domain propeptide #status predicted #label PRO\ !$26-560 #product mullerian inhibiting factor #status !8predicted #label MAT\ !$64,329 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$462-526,488-557, !$492-559 #disulfide_bonds #status predicted\ !$525 #disulfide_bonds interchain #status predicted SUMMARY #length 560 #molecular-weight 59192 #checksum 3812 SEQUENCE /// ENTRY WFBOM #type complete TITLE mullerian inhibiting factor precursor - bovine ALTERNATE_NAMES Mullerian inhibiting substance (MIS) ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 13-Aug-1986 #sequence_revision 13-Aug-1986 #text_change 01-Dec-2000 ACCESSIONS A01398; B01398 REFERENCE A90879 !$#authors Cate, R.L.; Mattaliano, R.J.; Hession, C.; Tizard, R.; !1Farber, N.M.; Cheung, A.; Ninfa, E.G.; Frey, A.Z.; Gash, !1D.J.; Chow, E.P.; Fisher, R.A.; Bertonis, J.M.; Torres, G.; !1Wallner, B.P.; Ramachandran, K.L.; Ragin, R.C.; Manganaro, !1T.F.; MacLaughlin, D.T.; Donahoe, P.K. !$#journal Cell (1986) 45:685-698 !$#title Isolation of the bovine and human genes for Muellerian !1inhibiting substance and expression of the human gene in !1animal cells. !$#cross-references MUID:86218082; PMID:3754790 !$#accession A01398 !'##molecule_type DNA !'##residues 1-14 ##label CA1 !'##experimental_source newborn calf testis, clones cbmis15 and pS21 !$#accession B01398 !'##molecule_type mRNA !'##residues 15-575 ##label CA2 COMMENT This glycoprotein, produced by the Sertoli cells of the !1testis, causes regression of the Mullerian duct. It also is !1able, in vivo and in vitro, to inhibit the growth of tumors !1derived from tissues of Mullerian duct origin. Other roles !1for this protein in gonadal differentiation, meiosis !1inhibition, and testicle descent are suggested by the low !1MIS concentrations found in the testis after duct regression !1and in the adult ovary. COMMENT This protein is homologous to the beta transforming growth !1factor, inhibin alpha chain, and inhibin beta A and B !1chains. The best area of homology corresponds to the mature !1protein of all these sequences. All of these proteins are !1biologically active as disulfide-linked dimers. COMMENT Although it does not compete with EGF for receptor binding !1sites, MIS can inhibit the autophosphorylation of the EGF !1receptor in vitro. CLASSIFICATION #superfamily inhibin KEYWORDS cytotoxin; glycoprotein; gonadal differentiation; testis FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-24 #domain propeptide #status predicted #label PRO\ !$25-575 #product mullerian inhibiting factor #status !8predicted #label MAT\ !$78,344 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 575 #molecular-weight 60623 #checksum 8089 SEQUENCE /// ENTRY A42499 #type complete TITLE mullerian inhibiting factor precursor - rat ALTERNATE_NAMES anti-mullerian hormone; mullerian inhibiting substance (MIS) ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A42499 REFERENCE A42499 !$#authors Haqq, C.; Lee, M.M.; Tizard, R.; Wysk, M.; DeMarinis, J.; !1Donahoe, P.K.; Cate, R.L. !$#journal Genomics (1992) 12:665-669 !$#title Isolation of the rat gene for Mullerian inhibiting !1substance. !$#cross-references MUID:92241861; PMID:1572639 !$#accession A42499 !'##molecule_type DNA !'##residues 1-553 ##label HAQ !'##cross-references GB:S98336; NID:g248896; PIDN:AAB22104.1; !1PID:g248897 !'##note sequence extracted from NCBI backbone (NCBIN:98336, !1NCBIP:98343) CLASSIFICATION #superfamily inhibin KEYWORDS cytotoxin; glycoprotein; gonadal differentiation; testis SUMMARY #length 553 #molecular-weight 58888 #checksum 5359 SEQUENCE /// ENTRY S20100 #type complete TITLE mullerian inhibiting factor - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Dec-2000 ACCESSIONS S20100; S51159 REFERENCE S20100 !$#authors Muensterberg, A.; Lovell-Badge, R. !$#journal Development (1991) 113:613-624 !$#title Expression of the mouse anti-Muellerian hormone gene !1suggests a role in both male and female sexual !1differentiation. !$#cross-references MUID:92146272; PMID:1782869 !$#accession S20100 !'##molecule_type DNA !'##residues 1-555 ##label MUE !'##cross-references EMBL:X63240; NID:g49945; PIDN:CAA44912.1; !1PID:g49946 REFERENCE S51159 !$#authors Dresser, D.W.; Hacker, A.; Lovell-Badge, R.; Guerrier, D. !$#submission submitted to the EMBL Data Library, January 1995 !$#description The genes for anti-Muellerian hormone (AMH) and a !1spliceosome protein (SAP62) are contiguous. !$#accession S51159 !'##status preliminary !'##molecule_type DNA !'##residues 1-41 ##label DRE !'##cross-references EMBL:X83733 GENETICS !$#introns 135/1; 182/3; 219/1; 272/2 CLASSIFICATION #superfamily inhibin SUMMARY #length 555 #molecular-weight 59778 #checksum 3223 SEQUENCE /// ENTRY BMHU6 #type complete TITLE bone morphogenetic protein 6 precursor - human ORGANISM #formal_name Homo sapiens #common_name man DATE 18-Oct-1991 #sequence_revision 03-Aug-1995 #text_change 18-Jun-1999 ACCESSIONS B39263 REFERENCE A39263 !$#authors Celeste, A.J.; Iannazzi, J.A.; Taylor, R.C.; Hewick, R.M.; !1Rosen, V.; Wang, E.A.; Wozney, J.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:9843-9847 !$#title Identification of transforming growth factor beta family !1members present in bone-inductive protein purified from !1bovine bone. !$#cross-references MUID:91088608; PMID:2263636 !$#accession B39263 !'##molecule_type mRNA !'##residues 1-513 ##label CEL !'##cross-references GB:M60315; GB:M38694; NID:g339561; PIDN:AAA36737.1; !1PID:g339562 GENETICS !$#gene GDB:BMP6 !'##cross-references GDB:127596; OMIM:112266 !$#map_position 6pter-6qter CLASSIFICATION #superfamily inhibin KEYWORDS bone; glycoprotein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-374 #domain propeptide #status predicted #label PRO\ !$375-513 #product bone morphogenetic protein 6 #status !8predicted #label MAT\ !$241,269,386,404,454 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 513 #molecular-weight 57225 #checksum 183 SEQUENCE /// ENTRY BMHU5 #type complete TITLE bone morphogenetic protein 5 precursor - human ORGANISM #formal_name Homo sapiens #common_name man DATE 18-Oct-1991 #sequence_revision 03-Aug-1995 #text_change 18-Jun-1999 ACCESSIONS A39263 REFERENCE A39263 !$#authors Celeste, A.J.; Iannazzi, J.A.; Taylor, R.C.; Hewick, R.M.; !1Rosen, V.; Wang, E.A.; Wozney, J.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:9843-9847 !$#title Identification of transforming growth factor beta family !1members present in bone-inductive protein purified from !1bovine bone. !$#cross-references MUID:91088608; PMID:2263636 !$#accession A39263 !'##molecule_type mRNA !'##residues 1-454 ##label CEL !'##cross-references GB:M60314; GB:M38693; NID:g339559; PIDN:AAA36736.1; !1PID:g339560 GENETICS !$#gene GDB:BMP5 !'##cross-references GDB:127595; OMIM:112265 !$#map_position 6pter-6qter CLASSIFICATION #superfamily inhibin KEYWORDS bone; glycoprotein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-316 #domain propeptide #status predicted #label PRO\ !$317-454 #product bone morphogenetic protein 5 #status !8predicted #label MAT\ !$211,327,345,395 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 454 #molecular-weight 51736 #checksum 4416 SEQUENCE /// ENTRY BMHU7 #type complete TITLE bone morphogenetic protein 7 precursor - human ALTERNATE_NAMES osteogenic protein 1 ORGANISM #formal_name Homo sapiens #common_name man DATE 18-Oct-1991 #sequence_revision 03-Aug-1995 #text_change 18-Jun-1999 ACCESSIONS C39263; S10529 REFERENCE A39263 !$#authors Celeste, A.J.; Iannazzi, J.A.; Taylor, R.C.; Hewick, R.M.; !1Rosen, V.; Wang, E.A.; Wozney, J.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:9843-9847 !$#title Identification of transforming growth factor beta family !1members present in bone-inductive protein purified from !1bovine bone. !$#cross-references MUID:91088608; PMID:2263636 !$#accession C39263 !'##molecule_type mRNA !'##residues 1-431 ##label CEL !'##cross-references GB:M60316; GB:M38695; NID:g339563; PIDN:AAA36738.1; !1PID:g339564 REFERENCE S10529 !$#authors Oezkaynak, E.; Rueger, D.C.; Drier, E.A.; Corbett, C.; !1Ridge, R.J.; Sampath, T.K.; Oppermann, H. !$#journal EMBO J. (1990) 9:2085-2093 !$#title OP-1 cDNA encodes an osteogenic protein in the TGF-beta !1family. !$#cross-references MUID:90291971; PMID:2357959 !$#accession S10529 !'##molecule_type mRNA !'##residues 1-431 ##label OEZ !'##cross-references EMBL:X51801; NID:g35151; PIDN:CAA36100.1; !1PID:g35152 GENETICS !$#gene GDB:BMP7 !'##cross-references GDB:127597; OMIM:112267 !$#map_position 20pter-20qter CLASSIFICATION #superfamily inhibin KEYWORDS bone; dimer; glycoprotein FEATURE !$1-29 #domain signal sequence #status predicted #label SIG\ !$30-299 #domain propeptide #status predicted #label PRO\ !$300-431 #product bone morphogenetic protein 7 #status !8predicted #label MAT\ !$187,302,321,372 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 431 #molecular-weight 49313 #checksum 128 SEQUENCE /// ENTRY BMHU4 #type complete TITLE bone morphogenetic protein 4 precursor - human ALTERNATE_NAMES bone morphogenetic protein 2B ORGANISM #formal_name Homo sapiens #common_name man DATE 16-Sep-1992 #sequence_revision 03-Aug-1995 #text_change 18-Jun-1999 ACCESSIONS C37278 REFERENCE A37278 !$#authors Wozney, J.M.; Rosen, V.; Celeste, A.J.; Mitsock, L.M.; !1Whitters, M.J.; Kriz, R.W.; Hewick, R.M.; Wang, E.A. !$#journal Science (1988) 242:1528-1534 !$#title Novel regulators of bone formation: molecular clones and !1activities. !$#cross-references MUID:89072730; PMID:3201241 !$#accession C37278 !'##molecule_type mRNA !'##residues 1-408 ##label WO3 !'##cross-references GB:M22490; NID:g179503; PIDN:AAA51835.1; !1PID:g179504 GENETICS !$#gene GDB:BMP4; BMP2B !'##cross-references GDB:125205; OMIM:112262 !$#map_position 14q22-14q23 CLASSIFICATION #superfamily inhibin KEYWORDS bone; glycoprotein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-292 #domain propeptide #status predicted #label PRO\ !$293-408 #product bone morphogenetic protein 4 #status !8predicted #label MAT\ !$143,208,350,365 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 408 #molecular-weight 46555 #checksum 48 SEQUENCE /// ENTRY BMHU2 #type complete TITLE bone morphogenetic protein 2 precursor - human ALTERNATE_NAMES bone morphogenetic protein 2A; rhBMP2 ORGANISM #formal_name Homo sapiens #common_name man DATE 16-Sep-1992 #sequence_revision 03-Aug-1995 #text_change 18-Jun-1999 ACCESSIONS B37278; PC2178 REFERENCE A37278 !$#authors Wozney, J.M.; Rosen, V.; Celeste, A.J.; Mitsock, L.M.; !1Whitters, M.J.; Kriz, R.W.; Hewick, R.M.; Wang, E.A. !$#journal Science (1988) 242:1528-1534 !$#title Novel regulators of bone formation: molecular clones and !1activities. !$#cross-references MUID:89072730; PMID:3201241 !$#accession B37278 !'##molecule_type mRNA !'##residues 1-396 ##label WO2 !'##cross-references GB:M22489; NID:g179501; PIDN:AAA51834.1; !1PID:g179502 REFERENCE PC2178 !$#authors Ishida, N.; Tsujimoto, M.; Kanaya, T.; Shimamura, A.; !1Tsuruoka, N.; Kodama, S.; Katayama, T.; Oikawa, S.; Matsui, !1M.; Nakanishi, T.; Kobayashi, J.; Nakazato, H. !$#journal J. Biochem. (1994) 115:279-285 !$#title Expression and characterization of human bone morphogenetic !1protein-2 in silkworm larvae infected with recombinant !1Bombyx mori nuclear polyhedrosis virus. !$#cross-references MUID:94266754; PMID:8206877 !$#accession PC2178 !'##molecule_type protein !'##residues 290-295,'X',297-304 ##label ISH !'##experimental_source cell line BoMo-15AIIc REFERENCE A56729 !$#authors Rathore, S.; Hammerstone, K.M.; Dansereau, S.; Porter, T.J. !$#journal Protein Sci. (1995) 4(Suppl.2):443S !$#title N-terminal isoforms of recombinant human bone morphogenetic !1protein (rhBMP-2) are active in vitro and in vivo. !$#contents annotation !$#note determination of amino ends of mature forms; dimers with !1long form chains have reduced activity COMMENT This hormone is capable of inducing bone formation at !1ectopic morphological locations. GENETICS !$#gene GDB:BMP2; BMP2A !'##cross-references GDB:125204; OMIM:112261 !$#map_position 20p12-20p12 COMPLEX homodimer, disulfide linked CLASSIFICATION #superfamily inhibin KEYWORDS bone; dimer; glycoprotein; pyroglutamic acid FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-265 #domain propeptide #status predicted #label PRO\ !$266-396 #product bone morphogenetic protein 2, long form !8#status predicted #label MATL\ !$283-396 #product bone morphogenetic protein 2 #status !8predicted #label MAT\ !$135,163,164,200 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$283 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$338 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 396 #molecular-weight 44702 #checksum 9850 SEQUENCE /// ENTRY BMHU3 #type complete TITLE bone morphogenetic protein 3 precursor - human ALTERNATE_NAMES osteogenin ORGANISM #formal_name Homo sapiens #common_name man DATE 16-Sep-1992 #sequence_revision 03-Aug-1995 #text_change 18-Jun-1999 ACCESSIONS D37278 REFERENCE A37278 !$#authors Wozney, J.M.; Rosen, V.; Celeste, A.J.; Mitsock, L.M.; !1Whitters, M.J.; Kriz, R.W.; Hewick, R.M.; Wang, E.A. !$#journal Science (1988) 242:1528-1534 !$#title Novel regulators of bone formation: molecular clones and !1activities. !$#cross-references MUID:89072730; PMID:3201241 !$#accession D37278 !'##molecule_type mRNA !'##residues 1-472 ##label WO4 !'##cross-references GB:M22491; NID:g179505; PIDN:AAA51836.1; !1PID:g179506 GENETICS !$#gene GDB:BMP3 !'##cross-references GDB:125206; OMIM:112263 !$#map_position 4p14-4q21 CLASSIFICATION #superfamily inhibin KEYWORDS bone; glycoprotein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-345 #domain propeptide #status predicted #label PRO\ !$346-472 #product bone morphogenetic protein 3 #status !8predicted #label MAT\ !$117,141,175,220,463 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 472 #molecular-weight 53406 #checksum 9364 SEQUENCE /// ENTRY JDBOB #type complete TITLE glia maturation factor beta - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 05-Aug-1994 ACCESSIONS A33102; A33066; A60210 REFERENCE A33102 !$#authors Lim, R.; Zaheer, A.; Lane, W.S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:5233-5237 !$#title Complete amino acid sequence of bovine glia maturation !1factor beta. !$#cross-references MUID:90319086; PMID:2196564 !$#accession A33102 !'##molecule_type protein !'##residues 1-141 ##label LIM COMMENT This protein causes differentiation of brain cells, !1stimulation of neural regeneration, and inhibition of !1proliferation of tumor cells. CLASSIFICATION #superfamily glia maturation factor beta KEYWORDS acetylated amino end; growth factor FEATURE !$1 #modified_site acetylated amino end (Ser) #status !8experimental SUMMARY #length 141 #molecular-weight 16582 #checksum 9151 SEQUENCE /// ENTRY PT0410 #type complete TITLE glia maturation factor beta - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 29-Sep-1999 ACCESSIONS PT0410 REFERENCE PT0410 !$#authors Kaplan, R.; Zaheer, A.; Jaye, M.; Lim, R. !$#journal J. Neurochem. (1991) 57:483-490 !$#title Molecular cloning and expression of biologically active !1human glia maturation factor-beta. !$#cross-references MUID:91303115; PMID:1712830 !$#accession PT0410 !'##molecule_type mRNA !'##residues 1-142 ##label KAP !'##cross-references GB:M86492; GB:M31742; NID:g183369; PIDN:AAA58614.1; !1PID:g183370 COMMENT This protein promotes the differentiation of normal neurons !1and glial cells, and inhibits the proliferation of their !1derived tumor cells in vitro. GENETICS !$#gene GDB:GMFB !'##cross-references GDB:134671 CLASSIFICATION #superfamily glia maturation factor beta SUMMARY #length 142 #molecular-weight 16713 #checksum 1964 SEQUENCE /// ENTRY S22149 #type complete TITLE glia maturation factor beta - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S22149 REFERENCE S22149 !$#authors Zaheer, A. !$#submission submitted to the EMBL Data Library, December 1991 !$#accession S22149 !'##status preliminary !'##molecule_type mRNA !'##residues 1-141 ##label ZAH !'##cross-references EMBL:Z11558; NID:g56294; PID:g1334282 CLASSIFICATION #superfamily glia maturation factor beta SUMMARY #length 141 #molecular-weight 16605 #checksum 9292 SEQUENCE /// ENTRY NGHUBM #type fragment TITLE nerve growth factor beta chain precursor - human (fragment) ORGANISM #formal_name Homo sapiens #common_name man DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 18-Jun-1999 ACCESSIONS A01399; S10253 REFERENCE A93305 !$#authors Ullrich, A.; Gray, A.; Berman, C.; Dull, T.J. !$#journal Nature (1983) 303:821-825 !$#title Human beta-nerve growth factor gene sequence highly !1homologous to that of mouse. !$#cross-references MUID:83244969; PMID:6688123 !$#accession A01399 !'##molecule_type DNA !'##residues 1-286 ##label ULL REFERENCE S10253 !$#authors Borsani, G.; Pizzuti, A.; Rugarli, E.I.; Falini, A.; Silani, !1V.; Sidoli, A.; Scarlato, G.; Baralle, F.E. !$#journal Nucleic Acids Res. (1990) 18:4020 !$#title cDNA sequence of human beta-NGF. !$#cross-references MUID:90326556; PMID:2374737 !$#accession S10253 !'##status translation not shown !'##molecule_type mRNA !'##residues 46-286 ##label BOR !'##cross-references EMBL:X52599; NID:g29476; PIDN:CAA36832.1; !1PID:g29477 COMMENT Nerve growth factor is found in submaxillary gland in large !1quantities and in other tissues in trace amounts. Its !1abilities to stimulate rapid neurite outgrowth from !1sympathetic and embryonic sensory ganglia in vivo and in !1vitro and to increase cellular neurotubule levels may be !1closely connected. GENETICS !$#gene GDB:NGFB !'##cross-references GDB:120233; OMIM:162030 !$#map_position 1p13.1-1p13.1 !$#introns 41/3 COMPLEX nerve growth factor is composed of two alpha chains, two !1beta chains, and two gamma chains; beta chains associate to !1form homodimers CLASSIFICATION #superfamily nerve growth factor beta chain KEYWORDS glycoprotein; growth factor; submandibular gland FEATURE !$1-166 #domain signal sequence and propeptide (fragment) !8#status predicted #label SIG\ !$167-284 #product nerve growth factor beta chain #status !8predicted #label MAT\ !$26,114,159,211 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$181-246,224-274, !$234-276 #disulfide_bonds #status predicted SUMMARY #length 286 #checksum 1929 SEQUENCE /// ENTRY NGMSMG #type complete TITLE nerve growth factor beta chain precursor - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Nov-1980 #sequence_revision 19-Feb-1984 #text_change 21-Jul-2000 ACCESSIONS A93301; A93305; A90366; I49689; I52891; A01400; I49690 REFERENCE A93301 !$#authors Scott, J.; Selby, M.; Urdea, M.; Quiroga, M.; Bell, G.I.; !1Rutter, W.J. !$#journal Nature (1983) 302:538-540 !$#title Isolation and nucleotide sequence of a cDNA encoding the !1precursor of mouse nerve growth factor. !$#cross-references MUID:83167518; PMID:6336309 !$#accession A93301 !'##molecule_type mRNA !'##residues 1-307 ##label SCO !'##cross-references GB:V00836; NID:g53364; PIDN:CAA24221.1; PID:g53365 REFERENCE A93305 !$#authors Ullrich, A.; Gray, A.; Berman, C.; Dull, T.J. !$#journal Nature (1983) 303:821-825 !$#title Human beta-nerve growth factor gene sequence highly !1homologous to that of mouse. !$#cross-references MUID:83244969; PMID:6688123 !$#accession A93305 !'##molecule_type mRNA !'##residues 1-307 ##label ULL !'##cross-references GB:K01759; NID:g200051; PIDN:AAA39820.1; !1PID:g387495 !'##note these authors believe that Met-67 is probably the !1amino-terminal residue and that residues 67-84 are the !1signal sequence REFERENCE A90366 !$#authors Angeletti, R.H.; Hermodson, M.A.; Bradshaw, R.A. !$#journal Biochemistry (1973) 12:100-115 !$#title Amino acid sequences of mouse 2.5S nerve growth factor. II. !1Isolation and characterization of the thermolytic and peptic !1peptides and the complete covalent structure. !$#cross-references MUID:73075048; PMID:4566923 !$#accession A90366 !'##molecule_type protein !'##residues 188-216,'N',218-305 ##label ANG REFERENCE I49689 !$#authors Selby, M.J.; Edwards, R.; Sharp, F.; Rutter, W.J. !$#journal Mol. Cell. Biol. (1987) 7:3057-3064 !$#title Mouse nerve growth factor gene: Structure and expression. !$#cross-references MUID:88038855; PMID:3670305 !$#accession I49689 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-307 ##label RES !'##cross-references GB:M17298; NID:g193493; PIDN:AAA37687.1; !1PID:g467311 REFERENCE I52891 !$#authors Ullrich, A.; Gray, A.; Berman, C.H.; Coussens, L.; Dull, !1T.J. !$#journal Cold Spring Harb. Symp. Quant. Biol. (1983) 48:435-442 !$#title Sequence homology of human and mouse beta-NGF subunit genes. !$#cross-references MUID:84206565; PMID:6327169 !$#accession I52891 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-307 ##label RE3 !'##cross-references GB:M14805; NID:g200053; PIDN:AAA39821.1; !1PID:g200054 COMMENT The active molecule is a dimer of identical chains !1associated by noncovalent forces. COMMENT Nerve growth factor is found in submaxillary gland in large !1quantities and in other tissues in trace amounts. Its !1abilities to stimulate rapid neurite outgrowth from !1sympathetic and embryonic sensory ganglia in vivo and in !1vitro and to increase cellular neurotubule levels may be !1closely connected. GENETICS !$#gene NGFB !$#introns 21/2; 62/3 CLASSIFICATION #superfamily nerve growth factor beta chain KEYWORDS glycoprotein; growth factor; homodimer FEATURE !$1-187 #domain signal sequence and propeptide #status !8predicted #label SIG\ !$188-305 #product nerve growth factor beta chain #status !8experimental #label MAT\ !$135,180 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$202-267,245-295, !$255-297 #disulfide_bonds #status experimental\ !$232 #binding_site carbohydrate (Asn) (covalent) #status !8absent SUMMARY #length 307 #molecular-weight 33787 #checksum 1085 SEQUENCE /// ENTRY NGRTBA #type complete TITLE nerve growth factor beta chain precursor - multimammate rat (Mastomys natalensis) ORGANISM #formal_name Mastomys natalensis DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 18-Jun-1999 ACCESSIONS JT0343 REFERENCE JT0343 !$#authors Fahnestock, M.; Bell, R.A. !$#journal Gene (1988) 69:257-264 !$#title Molecular cloning of a cDNA encoding the nerve growth factor !1precursor from Mastomys natalensis. !$#cross-references MUID:89172070; PMID:3234767 !$#accession JT0343 !'##molecule_type mRNA !'##residues 1-303 ##label FAH !'##cross-references GB:M22748; NID:g202514; PIDN:AAA40599.1; !1PID:g202515 !'##note it is uncertain whether Met-1 or Met-63 is the initiator CLASSIFICATION #superfamily nerve growth factor beta chain KEYWORDS glycoprotein; growth factor; homodimer; submaxillary gland FEATURE !$184-301 #product nerve growth factor beta chain #status !8predicted #label MAT\ !$131,176,228 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$198-263,241-291, !$251-293 #disulfide_bonds #status predicted SUMMARY #length 303 #molecular-weight 33462 #checksum 5721 SEQUENCE /// ENTRY NGNJXI #type complete TITLE nerve growth factor - Indian cobra ORGANISM #formal_name Naja naja naja #common_name Indian cobra DATE 30-Nov-1980 #sequence_revision 25-Apr-1997 #text_change 17-Mar-2000 ACCESSIONS S13927; A01401 REFERENCE S13927 !$#authors Inoue, S.; Oda, T.; Koyama, J.; Ikeda, K.; Hayashi, K. !$#journal FEBS Lett. (1991) 279:38-40 !$#title Amino acid sequences of nerve growth factors derived from !1cobra venoms. !$#cross-references MUID:91138755; PMID:1995338 !$#accession S13927 !'##molecule_type protein !'##residues 1-116 ##label INO !'##experimental_source venom !'##note the source is designated as Naja naja and referred to as Indian !1cobra, so we have assigned it to the most probable !1subspecies REFERENCE A01401 !$#authors Hogue-Angeletti, R.A.; Frazier, W.A.; Jacobs, J.W.; Niall, !1H.D.; Bradshaw, R.A. !$#journal Biochemistry (1976) 15:26-34 !$#title Purification, characterization, and partial amino acid !1sequence of nerve growth factor from cobra venom. !$#cross-references MUID:76114772; PMID:1247508 !$#accession A01401 !'##molecule_type protein !'##residues 1-11,'P',13-14,'B',16,'TBT';20-21,'GV';23-27,'N', !129-31;'AS',34,'S';36-48,'E',50-55;56,'RBSB',61,'PZP',65-66, !1'K';68-69,'BTZ',73-74,'B',76-79,'TSNS',84-90,'BZG',94,'SA', !197-102,'Z',104-113,115-116 ##label HOG !'##experimental_source venom !'##note the source is designated as Naja naja and referred to as Indian !1cobra, so we have assigned it to the most probable !1subspecies COMMENT Nerve growth factor is necessary for the development of !1embryonic sympathetic and sensory neurons. Its role in snake !1venom is unclear. COMPLEX homodimer CLASSIFICATION #superfamily nerve growth factor beta chain KEYWORDS growth factor; homodimer; venom FEATURE !$14-78,56-106,66-108 #disulfide_bonds #status predicted SUMMARY #length 116 #molecular-weight 13021 #checksum 4634 SEQUENCE /// ENTRY GQVZML #type complete TITLE T2 protein - myxoma virus (strain Lausanne) ORGANISM #formal_name myxoma virus DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 18-Jun-1999 ACCESSIONS A40566 REFERENCE A40566 !$#authors Upton, C.; Macen, J.L.; Schreiber, M.; Mcfadden, G. !$#journal Virology (1991) 184:370-382 !$#title Myxoma virus expresses a secreted protein with homology to !1the tumor necrosis factor receptor gene family that !1contributes to viral virulence. !$#cross-references MUID:91335768; PMID:1651597 !$#accession A40566 !'##molecule_type DNA !'##residues 1-326 ##label UPT !'##cross-references GB:M95181; GB:M37976; NID:g332309; PIDN:AAA46632.1; !1PID:g332310 CLASSIFICATION #superfamily myxoma virus T2 protein; NGF receptor repeat !1homology KEYWORDS glycoprotein FEATURE !$64-105 #domain NGF receptor repeat homology #label NG2\ !$106-147 #domain NGF receptor repeat homology #label NG3\ !$66,181,205,238 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 326 #molecular-weight 35208 #checksum 9255 SEQUENCE /// ENTRY SWWOD #type complete TITLE diuretic hormone precursor - tobacco hornworm ALTERNATE_NAMES diuretic hormone Mas-DH ORGANISM #formal_name Manduca sexta #common_name tobacco hornworm DATE 31-Dec-1991 #sequence_revision 12-Apr-1996 #text_change 18-Jun-1999 ACCESSIONS A46377; A32113 REFERENCE A46377 !$#authors Digan, M.E.; Roberts, D.N.; Enderlin, F.E.; Woodworth, A.R.; !1Kramer, S.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:11074-11078 !$#title Characterization of the precursor for Manduca sexta diuretic !1hormone Mas-DH. !$#cross-references MUID:93066387; PMID:1279702 !$#accession A46377 !'##molecule_type mRNA !'##residues 1-138 ##label DIG !'##cross-references GB:L04628; GB:L04624; GB:L04625; GB:L04626; !1GB:L04627; NID:g159500; PIDN:AAB59200.1; PID:g159501 !'##note sequence extracted from NCBI backbone (NCBIN:118881, !1NCBIP:118883) REFERENCE A32113 !$#authors Kataoka, H.; Troetschler, R.G.; Li, J.P.; Kramer, S.J.; !1Carney, R.L.; Schooley, D.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:2976-2980 !$#title Isolation and identification of a diuretic hormone from the !1tobacco hornworm, Manduca sexta. !$#accession A32113 !'##molecule_type protein !'##residues 81-121 ##label KAT CLASSIFICATION #superfamily diuretic hormone precursor; diuretic hormone !1homology KEYWORDS amidated carboxyl end; diuretic; hormone; osmoregulation FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$80-121 #domain diuretic hormone homology #label DHH\ !$81-121 #product diuretic hormone #status experimental #label !8MAT\ !$121 #modified_site amidated carboxyl end (Ile) (amide in !8mature form from following glycine) #status !8experimental SUMMARY #length 138 #molecular-weight 15296 #checksum 3695 SEQUENCE /// ENTRY SWLQDA #type complete TITLE diuretic hormone - African migratory locust ORGANISM #formal_name Locusta migratoria migratorioides #common_name African migratory locust DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 17-May-1996 ACCESSIONS JH0243; S17864; A23702 REFERENCE JH0243 !$#authors Lehmberg, E.; Ota, R.B.; Furuya, K.; King, D.S.; Applebaum, !1S.W.; Ferenz, H.J.; Schooley, D.A. !$#journal Biochem. Biophys. Res. Commun. (1991) 179:1036-1041 !$#title Identification of a diuretic hormone of Locusta migratoria. !$#cross-references MUID:91378968; PMID:1654896 !$#accession JH0243 !'##molecule_type protein !'##residues 1-46 ##label LE2 !'##experimental_source brain and corpora cardiaca REFERENCE S17864 !$#authors Kay, I.; Wheeler, C.H.; Coast, G.M.; Totty, N.F.; Cusinato, !1O.; Patel, M.; Goldsworthy, G.J. !$#journal Biol. Chem. Hoppe-Seyler (1991) 372:929-934 !$#title Characterization of a diuretic peptide from Locusta !1migratoria. !$#cross-references MUID:92126231; PMID:1663363 !$#accession S17864 !'##molecule_type protein !'##residues 1-46 ##label KAY !'##note species designated as Locusta migratoria COMMENT This hormone stimulates urine production by Malpighian !1tubules and elevates levels of cAMP concentration in !1tubules. CLASSIFICATION #superfamily diuretic hormone precursor; diuretic hormone !1homology KEYWORDS amidated carboxyl end; diuretic; hormone; osmoregulation FEATURE !$2-46 #domain diuretic hormone homology #label DHH\ !$46 #modified_site amidated carboxyl end (Ile) #status !8experimental SUMMARY #length 46 #molecular-weight 5364 #checksum 1214 SEQUENCE /// ENTRY RHRTCE #type complete TITLE corticoliberin precursor - rat ALTERNATE_NAMES corticotropin-releasing factor; prepro-CRF CONTAINS corticoliberin ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 14-Nov-1983 #sequence_revision 30-Sep-1987 #text_change 18-Jun-1999 ACCESSIONS A40906; A91351; A93965; A01405; A24009 REFERENCE A40906 !$#authors Thompson, R.C.; Seasholtz, A.F.; Herbert, E. !$#journal Mol. Endocrinol. (1987) 1:363-370 !$#title Rat corticotropin-releasing hormone gene: sequence and !1tissue-specific expression. !$#cross-references MUID:90331928; PMID:3274895 !$#accession A40906 !'##molecule_type DNA !'##residues 1-187 ##label THO !'##cross-references GB:M54987; NID:g203593; PIDN:AAA40965.1; !1PID:g203594 REFERENCE A91351 !$#authors Jingami, H.; Mizuno, N.; Takahashi, H.; Shibahara, S.; !1Furutani, Y.; Imura, H.; Numa, S. !$#journal FEBS Lett. (1985) 191:63-66 !$#title Cloning and sequence analysis of cDNA for rat !1corticotropin-releasing factor precursor. !$#cross-references MUID:86030658; PMID:3876950 !$#accession A91351 !'##molecule_type mRNA !'##residues 1-187 ##label JIN !'##cross-references GB:X03036; NID:g56008; PIDN:CAA26838.1; PID:g56009 REFERENCE A93965 !$#authors Rivier, J.; Spiess, J.; Vale, W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:4851-4855 !$#title Characterization of rat hypothalamic corticotropin-releasing !1factor. !$#cross-references MUID:83273710; PMID:6603620 !$#accession A93965 !'##molecule_type protein !'##residues 145-185 ##label RIV COMMENT Corticoliberin from hypothalamus stimulates the release of !1corticotropin (ACTH) from the anterior pituitary gland. This !1hormone is also synthesized in various areas of the brain, !1the pituitary gland, testis, spinal cord, and adrenal gland. GENETICS !$#gene CRH !$#introns #status absent !$#note one intron is in 5' noncoding region CLASSIFICATION #superfamily corticoliberin-endorpholiberin; diuretic !1hormone homology KEYWORDS amidated carboxyl end; hormone; hypothalamus FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-187 #product procorticoliberin #status predicted #label !8MAT\ !$145-185 #product corticoliberin #status experimental #label !8CLN\ !$145-184 #domain diuretic hormone homology #label DHH\ !$185 #modified_site amidated carboxyl end (Ile) (amide in !8mature form from following glycine) #status !8experimental SUMMARY #length 187 #molecular-weight 20680 #checksum 8137 SEQUENCE /// ENTRY RHPGCE #type complete TITLE corticoliberin - pig ALTERNATE_NAMES corticotropin-releasing factor; CRF; endorpholiberin ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 11-Apr-1997 ACCESSIONS A01404 REFERENCE A01404 !$#authors Patthy, M.; Horvath, J.; Mason-Garcia, M.; Szoke, B.; !1Schlesinger, D.H.; Schally, A.V. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:8762-8766 !$#title Isolation and amino acid sequence of corticotropin-releasing !1factor from pig hypothalami. !$#cross-references MUID:86094305; PMID:3878520 !$#accession A01404 !'##molecule_type protein !'##residues 1-41 ##label PAT !'##note 40-Ile was also found COMMENT This hormone from hypothalamus regulates the release of !1corticotropin from pituitary gland. CLASSIFICATION #superfamily corticoliberin-endorpholiberin; diuretic !1hormone homology KEYWORDS amidated carboxyl end; hormone; hypothalamus FEATURE !$41 #modified_site amidated carboxyl end (Phe) #status !8experimental SUMMARY #length 41 #molecular-weight 4793 #checksum 4582 SEQUENCE /// ENTRY RHSHCE #type complete TITLE corticoliberin precursor - sheep ALTERNATE_NAMES corticotropin-releasing factor; endorpholiberin ORGANISM #formal_name Ovis orientalis aries, Ovis ammon aries #common_name domestic sheep DATE 24-Sep-1981 #sequence_revision 31-Dec-1992 #text_change 18-Jun-1999 ACCESSIONS JS0030; A38853; B38853; A93895; A94257; S03406; A01403 REFERENCE JS0030 !$#authors Roche, P.J.; Crawford, R.J.; Fernley, R.T.; Tregear, G.W.; !1Coghlan, J.P. !$#journal Gene (1988) 71:421-431 !$#title Nucleotide sequence of the gene coding for ovine !1corticotropin-releasing factor and regulation of its mRNA !1levels by glucocorticoids. !$#cross-references MUID:89138018; PMID:3265687 !$#accession JS0030 !'##molecule_type DNA !'##residues 1-190 ##label ROC !'##cross-references GB:M22853; NID:g165847; PIDN:AAA31513.1; !1PID:g165848 REFERENCE A38853 !$#authors Furutani, Y.; Morimoto, Y.; Shibahara, S.; Noda, M.; !1Takahashi, H.; Hirose, T.; Asai, M.; Inayama, S.; Hayashida, !1H.; Miyata, T.; Numa, S. !$#journal Nature (1983) 301:537-540 !$#title Cloning and sequence analysis of cDNA for ovine !1corticotropin-releasing factor precursor. !$#cross-references MUID:83115325; PMID:6600512 !$#accession A38853 !'##molecule_type mRNA !'##residues 1-126,'K',128-190 ##label FUR !'##cross-references GB:J00803; NID:g165845; PIDN:AAA31512.1; !1PID:g165846 !$#accession B38853 !'##molecule_type mRNA !'##residues 1-190 ##label FU2 REFERENCE A93895 !$#authors Spiess, J.; Rivier, J.; Rivier, C.; Vale, W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:6517-6521 !$#title Primary structure of corticotropin-releasing factor from !1ovine hypothalamus. !$#cross-references MUID:82082489; PMID:6273874 !$#accession A93895 !'##molecule_type protein !'##residues 148-188 ##label SPI REFERENCE A94257 !$#authors Vale, W.; Spiess, J.; Rivier, C.; Rivier, J. !$#journal Science (1981) 213:1394-1397 !$#title Characterization of a 41-residue ovine hypothalamic peptide !1that stimulates secretion of corticotropin and !1beta-endorphin. !$#cross-references MUID:81274815; PMID:6267699 !$#accession A94257 !'##molecule_type protein !'##residues 148-188 ##label VAL REFERENCE S03406 !$#authors Audhya, T.; Hollander, C.S.; Schlesinger, D.H.; Hutchinson, !1B. !$#journal Biochim. Biophys. Acta (1989) 995:10-16 !$#title Structural characterization and localization of !1corticotropin-releasing factor in testis. !$#cross-references MUID:89166626; PMID:2647152 !$#accession S03406 !'##molecule_type protein !'##residues 148-188 ##label AUD !'##note 186-Glu was also found COMMENT Corticoliberin stimulates the synthesis and release of !1adrenocorticotropic hormone from the anterior pituitary !1gland. GENETICS !$#gene CRF CLASSIFICATION #superfamily corticoliberin-endorpholiberin; diuretic !1hormone homology KEYWORDS amidated carboxyl end; hormone; hypothalamus FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-147 #domain propeptide #status predicted #label PRO\ !$148-188 #product corticoliberin #status experimental #label !8MCF\ !$148-188 #domain diuretic hormone homology #label DHH\ !$188 #modified_site amidated carboxyl end (Ala) (amide in !8mature form from following glycine) #status !8experimental SUMMARY #length 190 #molecular-weight 20673 #checksum 2463 SEQUENCE /// ENTRY SWFGS #type complete TITLE sauvagine - Sauvage's leaf frog ORGANISM #formal_name Phyllomedusa sauvagei #common_name Sauvage's leaf frog DATE 24-Sep-1981 #sequence_revision 24-Sep-1981 #text_change 07-May-1999 ACCESSIONS A01406; A61325 REFERENCE A01406 !$#authors Montecucchi, P.C.; Henschen, A.; Erspamer, V. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1979) 360:1178 !$#title Structure of sauvagine, a vasoactive peptide from the skin !1of a frog. !$#accession A01406 !'##molecule_type protein !'##residues 1-40 ##label MON REFERENCE A61325 !$#authors Montecucchi, P.C.; Henschen, A. !$#journal Int. J. Pept. Protein Res. (1981) 18:113-120 !$#title Amino acid composition and sequence analysis of sauvagine, a !1new active peptide from the skin of Phyllomedusa sauvagei. !$#cross-references MUID:82075075; PMID:7309372 !$#accession A61325 !'##molecule_type protein !'##residues 1-40 ##label MO2 COMMENT This hypotensive peptide is obtained from the cutaneous !1tissue of the frog. CLASSIFICATION #superfamily corticoliberin-endorpholiberin; diuretic !1hormone homology KEYWORDS amidated carboxyl end; antihypertensive; pyroglutamic acid; !1skin FEATURE !$1 #modified_site pyrrolidone carboxylic acid (Gln) !8#status experimental\ !$40 #modified_site amidated carboxyl end (Ile) #status !8experimental SUMMARY #length 40 #molecular-weight 4617 #checksum 1495 SEQUENCE /// ENTRY UOCC1M #type complete TITLE urotensin I - white sucker ORGANISM #formal_name Catostomus commersoni #common_name white sucker DATE 05-Apr-1983 #sequence_revision 05-Apr-1983 #text_change 21-Jan-2000 ACCESSIONS A94267; A90754; A01407 REFERENCE A94267 !$#authors Lederis, K.; Letter, A.; McMaster, D.; Moore, G.; !1Schlesinger, D. !$#journal Science (1982) 218:162-164 !$#title Complete amino acid sequence of urotensin I, a hypotensive !1and corticotropin-releasing neuropeptide from Catostomus. !$#cross-references MUID:83016606; PMID:6981844 !$#accession A94267 !'##molecule_type protein !'##residues 1-41 ##label LE1 REFERENCE A90754 !$#authors Lederis, K.; Letter, A.; McMaster, D.; Ichikawa, T.; !1MacCannell, K.L.; Rivier, J.; Rivier, C.; Vale, W.; Fryer, !1J.; Kobayashi, Y. !$#journal Can. J. Biochem. Cell Biol. (1983) 61:602-614 !$#title Isolation, analysis of structure, synthesis, and biological !1actions of urotensin I neuropeptides. !$#cross-references MUID:84025881; PMID:6313156 !$#accession A90754 !'##molecule_type protein !'##residues 1-41 ##label LE2 COMMENT Urotensin I is found in the teleost caudal neurosecretory !1system and is involved in hypotensive, vasodilatory !1activities. CLASSIFICATION #superfamily corticoliberin-endorpholiberin; diuretic !1hormone homology KEYWORDS amidated carboxyl end; hormone; osmoregulation FEATURE !$1-41 #domain diuretic hormone homology #label DHH\ !$41 #modified_site amidated carboxyl end (Val) #status !8experimental SUMMARY #length 41 #molecular-weight 4870 #checksum 4972 SEQUENCE /// ENTRY UOCA1 #type complete TITLE urotensin I precursor - common carp CONTAINS urotensin I ORGANISM #formal_name Cyprinus carpio #common_name common carp DATE 05-Apr-1983 #sequence_revision 31-Mar-1988 #text_change 20-Apr-2001 ACCESSIONS A94096; A93752; A01408; A25966 REFERENCE A94096 !$#authors Ishida, I.; Ichikawa, T.; Deguchi, T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:308-312 !$#title Cloning and sequence analysis of cDNA encoding urotensin I !1precursor. !$#cross-references MUID:86094380; PMID:3484550 !$#accession A94096 !'##molecule_type mRNA !'##residues 1-145 ##label ISH !'##cross-references GB:M11671; NID:g213064; PIDN:AAA49214.1; !1PID:g213065 !'##experimental_source spinal cord REFERENCE A93752 !$#authors Ichikawa, T.; McMaster, D.; Lederis, K.; Kobayashi, H. !$#journal Peptides (1982) 3:859-867 !$#title Isolation and amino acid sequence of urotensin I, a !1vasoactive and ACTH-releasing neuropeptide, from the carp !1(Cyprinus carpio) urophysis. !$#cross-references MUID:83090718; PMID:6757895 !$#accession A93752 !'##molecule_type protein !'##residues 103-143 ##label ICH COMMENT Urotensin I is found in the teleost caudal neurosecretory !1system. It has a suggested role in osmoregulation and as a !1corticotropin-releasing factor. COMMENT The nonhormonal portion of this precursor may be a urotensin !1binding protein, urophysin. CLASSIFICATION #superfamily corticoliberin-endorpholiberin; diuretic !1hormone homology KEYWORDS amidated carboxyl end; hormone; osmoregulation FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-145 #product prourotensin I #status predicted #label PRO\ !$103-143 #product urotensin I #status experimental #label MAT\ !$103-143 #domain diuretic hormone homology #label DHH\ !$143 #modified_site amidated carboxyl end (Val) (amide in !8mature form from following glycine) #status !8experimental SUMMARY #length 145 #molecular-weight 16249 #checksum 8207 SEQUENCE /// ENTRY UOGM2 #type complete TITLE urotensin II - long-jawed mudsucker ORGANISM #formal_name Gillichthys mirabilis #common_name long-jawed mudsucker DATE 23-Oct-1981 #sequence_revision 23-Oct-1981 #text_change 15-Oct-1996 ACCESSIONS A01409 REFERENCE A01409 !$#authors Pearson, D.; Shively, J.E.; Clark, B.R.; Geschwind, I.I.; !1Barkley, M.; Nishioka, R.; Bern, H.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1980) 77:5021-5024 !$#title Urotensin II: a somatostatin-like peptide in the caudal !1neurosecretory system of fishes. !$#cross-references MUID:81054904; PMID:6107911 !$#accession A01409 !'##molecule_type protein !'##residues 1-12 ##label PEA !'##note the proposed sequence was confirmed by synthesis of a peptide !1with the same structure, physical properties, and !1substantial biological activity COMMENT Urotensin II is found in the teleost caudal neurosecretory !1system and is involved in osmoregulatory and hypertensive !1activities. CLASSIFICATION #superfamily urotensin II KEYWORDS neuropeptide; osmoregulation FEATURE !$6-11 #disulfide_bonds #status experimental SUMMARY #length 12 #molecular-weight 1364 #checksum 5981 SEQUENCE /// ENTRY RHHUG #type complete TITLE gonadoliberin precursor [validated] - human ALTERNATE_NAMES gonadotropin releasing hormone (GnRH); luteinizing hormone releasing hormone (LHRH) CONTAINS gonadoliberin-associated protein (GAP); progonadoliberin ORGANISM #formal_name Homo sapiens #common_name man DATE 17-Mar-1987 #sequence_revision 21-Jul-1995 #text_change 08-Dec-2000 ACCESSIONS S05308; A26173; A93342; A90108; A01410; S45718 REFERENCE S05308 !$#authors Hayflick, J.S.; Adelman, J.P.; Seeburg, P.H. !$#journal Nucleic Acids Res. (1989) 17:6403-6404 !$#title The complete nucleotide sequence of the human !1gonadotropin-releasing hormone gene. !$#cross-references MUID:89366682; PMID:2671939 !$#accession S05308 !'##status translation not shown !'##molecule_type DNA !'##residues 1-92 ##label HAY !'##cross-references EMBL:X15215; NID:g31955; PIDN:CAA33285.1; !1PID:g31956 REFERENCE A94090 !$#authors Adelman, J.P.; Mason, A.J.; Hayflick, J.S.; Seeburg, P.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:179-183 !$#title Isolation of the gene and hypothalamic cDNA for the common !1precursor of gonadotropin-releasing hormone and prolactin !1release-inhibiting factor in human and rat. !$#cross-references MUID:86094338; PMID:2867548 !$#accession A26173 !'##molecule_type mRNA !'##residues 1-92 ##label ADE !'##cross-references GB:M12578; NID:g183418; PIDN:AAA35916.1; !1PID:g386749 !'##experimental_source hypothalamus REFERENCE A93342 !$#authors Seeburg, P.H.; Adelman, J.P. !$#journal Nature (1984) 311:666-668 !$#title Characterization of cDNA for precursor of human luteinizing !1hormone releasing hormone. !$#cross-references MUID:85012739; PMID:6090951 !$#accession A93342 !'##molecule_type mRNA !'##residues 1-15,'S',17-92 ##label SEE !'##cross-references GB:X01059; NID:g34356; PIDN:CAA25526.1; PID:g34357 !'##experimental_source placenta REFERENCE A90108 !$#authors Tan, L.; Rousseau, P. !$#journal Biochem. Biophys. Res. Commun. (1982) 109:1061-1071 !$#title The chemical identity of the immunoreactive LHRH-like !1peptide biosynthesized in the human placenta. !$#cross-references MUID:83126573; PMID:6760865 !$#accession A90108 !'##molecule_type protein !'##residues 24-33 ##label TAN !'##experimental_source placental trophoblasts REFERENCE S45718 !$#authors Leibovitz, D.; Koch, Y.; Pitzer, F.; Fridkin, M.; Dantes, !1A.; Baumeister, W.; Amsterdam, A. !$#journal FEBS Lett. (1994) 346:203-206 !$#title Sequential degradation of the neuropeptide !1gonadotropin-releasing hormone by the 20 S granulosa cell !1proteasomes. !$#cross-references MUID:94283597; PMID:8013634 !$#contents annotation; degradation pathway of synthetic hormone GENETICS !$#gene GDB:GNRH; LHRH; GRH !'##cross-references GDB:133746; OMIM:227200; OMIM:152760 !$#map_position 8p21-8p11.2 !$#introns 47/3; 79/3 FUNCTION !$#description gonadoliberin stimulates pituitary secretion of lutropin and !1follitropin !$#note gonadoliberin-associated protein may have prolactin release !1inhibiting activiy CLASSIFICATION #superfamily gonadoliberin KEYWORDS amidated carboxyl end; hormone; hypothalamus; placenta; !1pyroglutamic acid FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-92 #product progonadoliberin #status predicted #label !8PGN\ !$24-33 #product gonadoliberin #status experimental #label !8MAT\ !$37-92 #product gonadoliberin-associated protein #status !8predicted #label GAP\ !$24 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$33 #modified_site amidated carboxyl end (Gly) (amide in !8mature form from following glycine) #status !8experimental SUMMARY #length 92 #molecular-weight 10380 #checksum 1786 SEQUENCE /// ENTRY RHPGG #type complete TITLE gonadoliberin - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 13-Jul-1981 #sequence_revision 13-Jul-1981 #text_change 18-Mar-1997 ACCESSIONS A01411 REFERENCE A90172 !$#authors Baba, Y.; Matsuo, H.; Schally, A.V. !$#journal Biochem. Biophys. Res. Commun. (1971) 44:459-463 !$#title Structure of the porcine LH- and FSH-releasing hormone. II. !1Confirmation of the proposed structure by conventional !1sequential analyses. !$#cross-references MUID:72114303; PMID:4946067 !$#accession A01411 !'##molecule_type protein !'##residues 1-10 ##label BAB REFERENCE A90176 !$#authors Matsuo, H.; Arimura, A.; Nair, R.M.G.; Schally, A.V. !$#journal Biochem. Biophys. Res. Commun. (1971) 45:822-827 !$#title Synthesis of the porcine LH- and FSH-releasing hormone by !1the solid-phase method. !$#cross-references MUID:72065376; PMID:4942726 !$#contents annotation; synthesis !$#note the synthetic and natural hormones have the same !1physicochemical and biological properties REFERENCE A90175 !$#authors Baba, Y.; Arimura, A.; Schally, A.V. !$#journal Biochem. Biophys. Res. Commun. (1971) 45:483-487 !$#title On the tryptophan residue in porcine LH and FSH-releasing !1hormone. !$#cross-references MUID:72117544; PMID:4946275 !$#contents annotation !$#note Trp-3 appears to be essential for biological activity COMMENT This hypothalamic hormone stimulates the secretion of both !1luteinizing and follicle-stimulating hormones. CLASSIFICATION #superfamily gonadoliberin KEYWORDS amidated carboxyl end; hormone; hypothalamus; pyroglutamic !1acid FEATURE !$1 #modified_site pyrrolidone carboxylic acid (Gln) !8#status experimental\ !$10 #modified_site amidated carboxyl end (Gly) #status !8experimental SUMMARY #length 10 #molecular-weight 1200 #checksum 4307 SEQUENCE /// ENTRY RHSHG #type complete TITLE gonadoliberin - sheep ORGANISM #formal_name Ovis orientalis aries, Ovis ammon aries #common_name domestic sheep DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 18-Mar-1997 ACCESSIONS A93780; A01411 REFERENCE A93780 !$#authors Burgus, R.; Butcher, M.; Amoss, M.; Ling, N.; Monahan, M.; !1Rivier, J.; Fellows, R.; Blackwell, R.; Vale, W.; Guillemin, !1R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1972) 69:278-282 !$#title Primary structure of the ovine hypothalamic luteinizing !1hormone-releasing factor (LRF). !$#cross-references MUID:72094314; PMID:4550508 !$#accession A93780 !'##molecule_type protein !'##residues 1-10 ##label BUR !'##note the natural and synthetic hormones have the same biological !1activity COMMENT This hypothalamic hormone stimulates the secretion of both !1luteinizing and follicle-stimulating hormones. CLASSIFICATION #superfamily gonadoliberin KEYWORDS amidated carboxyl end; hormone; hypothalamus; pyroglutamic !1acid FEATURE !$1 #modified_site pyrrolidone carboxylic acid (Gln) !8#status experimental\ !$10 #modified_site amidated carboxyl end (Gly) #status !8experimental SUMMARY #length 10 #molecular-weight 1200 #checksum 4307 SEQUENCE /// ENTRY RHMSG #type complete TITLE gonadoliberin precursor - mouse ALTERNATE_NAMES gonadotropin-releasing hormone (GnRH); luteinizing hormone releasing hormone (LHRH) CONTAINS gonadoliberin; gonadoliberin-associated protein (GAP) ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1993 #sequence_revision 18-Mar-1997 #text_change 18-Jun-1999 ACCESSIONS A47578 REFERENCE A47578 !$#authors Mason, A.J.; Hayflick, J.S.; Zoeller, R.T.; Young III, W.S.; !1Phillips, H.S.; Nikolics, K.; Seeburg, P.H. !$#journal Science (1986) 234:1366-1371 !$#title A deletion truncating the gonadotropin-releasing hormone !1gene is responsible for hypogonadism in the hpg mouse. !$#cross-references MUID:87069928; PMID:3024317 !$#accession A47578 !'##molecule_type DNA !'##residues 1-90 ##label MAS !'##cross-references EMBL:M14872; NID:g193576; PIDN:AAA37717.1; !1PID:g387175 GENETICS !$#introns 45/3; 77/3 FUNCTION !$#description gonadoliberin stimulates pituitary secretion of lutropin and !1follitropin !$#note gonadoliberin-associated protein may have prolactin release !1inhibiting activity CLASSIFICATION #superfamily gonadoliberin KEYWORDS amidated carboxyl end; hormone; hypothalamus; pyroglutamic !1acid FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$22-31 #product gonadoliberin #status predicted #label GLB\ !$35-90 #product gonadoliberin-associated protein #status !8predicted #label GAP\ !$22 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status predicted\ !$31 #modified_site amidated carboxyl end (Gly) (amide in !8mature form from following glycine) #status predicted SUMMARY #length 90 #molecular-weight 10337 #checksum 7749 SEQUENCE /// ENTRY RHRTG #type complete TITLE gonadoliberin precursor - rat ALTERNATE_NAMES gonadoliberin-associated protein (GAP); gonadotropin releasing hormone (GnRH); luteinizing hormone releasing hormone (LHRH) CONTAINS gonadoliberin; prolactin release-inhibiting factor ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 18-Jun-1999 ACCESSIONS A40147; B26173; A48410 REFERENCE A40147 !$#authors Bond, C.T.; Hayflick, J.S.; Seeburg, P.H.; Adelman, J.P. !$#journal Mol. Endocrinol. (1989) 3:1257-1262 !$#title The rat gonadotropin-releasing hormone: SH locus: structure !1and hypothalamic expression. !$#cross-references MUID:89384661; PMID:2476669 !$#accession A40147 !'##molecule_type DNA !'##residues 1-92 ##label BON !'##cross-references GB:M31670; NID:g204447; PIDN:AAA41264.1; !1PID:g204448 REFERENCE A94090 !$#authors Adelman, J.P.; Mason, A.J.; Hayflick, J.S.; Seeburg, P.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:179-183 !$#title Isolation of the gene and hypothalamic cDNA for the common !1precursor of gonadotropin-releasing hormone and prolactin !1release-inhibiting factor in human and rat. !$#cross-references MUID:86094338; PMID:2867548 !$#accession B26173 !'##molecule_type mRNA !'##residues 1-92 ##label ADE !'##cross-references GB:M12579; NID:g204445; PIDN:AAA41263.1; !1PID:g204446 REFERENCE A48410 !$#authors Maier, C.C.; Marchetti, B.; LeBoeuf, R.D.; Blalock, J.E. !$#journal Cell. Mol. Neurobiol. (1992) 12:447-454 !$#title Thymocytes express a mRNA that is identical to hypothalamic !1luteinizing hormone-releasing hormone mRNA. !$#cross-references MUID:93105480; PMID:1468115 !$#accession A48410 !'##status preliminary !'##molecule_type mRNA !'##residues 1-92 ##label MAI !'##cross-references GB:S50870; NID:g262059; PIDN:AAB24572.1; !1PID:g262060 !'##experimental_source thymus !'##note sequence extracted from NCBI backbone (NCBIN:121082, !1NCBIP:121083) GENETICS !$#introns 47/3; 79/3 FUNCTION !$#description stimulates pituitary secretion of lutropin and follitropin !$#note gonadoliberin-associated protein may have prolactin release !1inhibiting activiy CLASSIFICATION #superfamily gonadoliberin KEYWORDS amidated carboxyl end; hormone; hypothalamus; placenta; !1pyroglutamic acid; reproduction FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-92 #product progonadoliberin #status predicted #label !8PGN\ !$24-33 #product gonadoliberin #status predicted #label GLN\ !$37-92 #product prolactin release-inhibiting factor #status !8predicted #label PIF\ !$24 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status predicted\ !$33 #modified_site amidated carboxyl end (Gly) (amide in !8mature form from following glycine) #status predicted SUMMARY #length 92 #molecular-weight 10500 #checksum 1405 SEQUENCE /// ENTRY RHAQ1 #type complete TITLE gonadoliberin I - American alligator ALTERNATE_NAMES gonadotropin-releasing hormone I ORGANISM #formal_name Alligator mississippiensis #common_name American alligator DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 18-Mar-1997 ACCESSIONS A60066 REFERENCE A60066 !$#authors Lovejoy, D.A.; Fischer, W.H.; Parker, D.B.; McRory, J.E.; !1Park, M.; Lance, V.; Swanson, P.; Rivier, J.E.; Sherwood, !1N.M. !$#journal Regul. Pept. (1991) 33:105-116 !$#title Primary structure of two forms of gonadotropin-releasing !1hormone from brains of the American alligator (Alligator !1mississippiensis). !$#cross-references MUID:91352338; PMID:1882082 !$#accession A60066 !'##molecule_type protein !'##residues 1-10 ##label LOV CLASSIFICATION #superfamily gonadoliberin KEYWORDS amidated carboxyl end; hormone; hypothalamus; pyroglutamic !1acid FEATURE !$1 #modified_site pyrrolidone carboxylic acid (Gln) !8#status experimental\ !$10 #modified_site amidated carboxyl end (Gly) #status !8experimental SUMMARY #length 10 #molecular-weight 1172 #checksum 4299 SEQUENCE /// ENTRY RHAQ2 #type complete TITLE gonadoliberin II - American alligator ALTERNATE_NAMES gonadotropin-releasing hormone II ORGANISM #formal_name Alligator mississippiensis #common_name American alligator DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 18-Mar-1997 ACCESSIONS B60066 REFERENCE A60066 !$#authors Lovejoy, D.A.; Fischer, W.H.; Parker, D.B.; McRory, J.E.; !1Park, M.; Lance, V.; Swanson, P.; Rivier, J.E.; Sherwood, !1N.M. !$#journal Regul. Pept. (1991) 33:105-116 !$#title Primary structure of two forms of gonadotropin-releasing !1hormone from brains of the American alligator (Alligator !1mississippiensis). !$#cross-references MUID:91352338; PMID:1882082 !$#accession B60066 !'##molecule_type protein !'##residues 1-10 ##label LOV CLASSIFICATION #superfamily gonadoliberin KEYWORDS amidated carboxyl end; hormone; hypothalamus; pyroglutamic !1acid FEATURE !$1 #modified_site pyrrolidone carboxylic acid (Gln) !8#status experimental\ !$10 #modified_site amidated carboxyl end (Gly) #status !8experimental SUMMARY #length 10 #molecular-weight 1254 #checksum 4355 SEQUENCE /// ENTRY A61126 #type complete TITLE gonadoliberin - spotted ratfish ALTERNATE_NAMES gonadotropin-releasing hormone ORGANISM #formal_name Hydrolagus colliei #common_name spotted ratfish DATE 26-May-1994 #sequence_revision 26-May-1994 #text_change 18-Mar-1997 ACCESSIONS A61126 REFERENCE A61126 !$#authors Lovejoy, D.A.; Sherwood, N.M.; Fischer, W.H.; Jackson, B.C.; !1Rivier, J.E.; Lee, T. !$#journal Gen. Comp. Endocrinol. (1991) 82:152-161 !$#title Primary structure of gonadotropin-releasing hormone from the !1brain of a holocephalan (ratfish: Hydrolagus colliei). !$#cross-references MUID:91340067; PMID:1678723 !$#accession A61126 !'##molecule_type protein !'##residues 1-10 ##label LOV !'##experimental_source brain CLASSIFICATION #superfamily gonadoliberin KEYWORDS amidated carboxyl end; brain; hormone; pyroglutamic acid FEATURE !$1 #modified_site pyrrolidone carboxylic acid (Gln) !8#status experimental\ !$10 #modified_site amidated carboxyl end (Gly) #status !8experimental SUMMARY #length 10 #molecular-weight 1254 #checksum 4355 SEQUENCE /// ENTRY RHLMGS #type complete TITLE gonadoliberin - sea lamprey ALTERNATE_NAMES gonadotropin releasing hormone (GnRH) ORGANISM #formal_name Petromyzon marinus #common_name sea lamprey DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 18-Mar-1997 ACCESSIONS A01412 REFERENCE A01412 !$#authors Sherwood, N.M.; Sower, S.A.; Marshak, D.R.; Fraser, B.A.; !1Brownstein, M.J. !$#journal J. Biol. Chem. (1986) 261:4812-4819 !$#title Primary structure of gonadotropin-releasing hormone from !1lamprey brain. !$#cross-references MUID:86168192; PMID:3514603 !$#accession A01412 !'##molecule_type protein !'##residues 1-10 ##label SHE COMMENT This hormone was isolated from the brain. CLASSIFICATION #superfamily gonadoliberin KEYWORDS amidated carboxyl end; hormone; pyroglutamic acid FEATURE !$1 #modified_site pyrrolidone carboxylic acid (Gln) !8#status experimental\ !$10 #modified_site amidated carboxyl end (Gly) #status !8experimental SUMMARY #length 10 #molecular-weight 1244 #checksum 4257 SEQUENCE /// ENTRY RHID2S #type complete TITLE gonadoliberin II precursor - sharptooth catfish ALTERNATE_NAMES gonadoliberin, chicken-type; gonadotropin-releasing hormone II (GnRH-II); gonadotropin-releasing hormone, chicken-type; preprogonadotropin-releasing hormone CONTAINS gonadoliberin II; gonadoliberin II-associated protein ORGANISM #formal_name Clarias gariepinus #common_name sharptooth catfish DATE 30-Sep-1993 #sequence_revision 18-Mar-1997 #text_change 18-Jun-1999 ACCESSIONS S45600; JC1243; S42935 REFERENCE S45600 !$#authors Bogerd, J.; Zandbergen, T.; Andersson, E.; Goos, H. !$#journal Eur. J. Biochem. (1994) 222:541-549 !$#title Isolation, characterization and expression of cDNAs encoding !1the catfish-type and chicken-II-type !1gonadotropin-releasing-hormone precursors in the African !1catfish. !$#cross-references MUID:94291651; PMID:8020492 !$#accession S45600 !'##molecule_type mRNA !'##residues 1-86 ##label BOG1 !'##cross-references EMBL:X78047; NID:g459429; PIDN:CAA54969.1; !1PID:g459430 REFERENCE JC1242 !$#authors Bogerd, J.; Li, K.W.; Janssen-Dommerholt, C.; Goos, H. !$#journal Biochem. Biophys. Res. Commun. (1992) 187:127-134 !$#title Two gonadotropin-releasing hormones from African catfish !1(Clarias gariepinus). !$#cross-references MUID:92392313; PMID:1520292 !$#accession JC1243 !'##molecule_type protein !'##residues 25-34 ##label BOG2 !'##experimental_source brain CLASSIFICATION #superfamily gonadoliberin KEYWORDS amidated carboxyl end; hormone; hypothalamus; pyroglutamic !1acid FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-34 #product gonadoliberin II #status experimental #label !8MAT1\ !$38-86 #product gonadoliberin II-associated protein #status !8predicted #label MAT2\ !$25 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$34 #modified_site amidated carboxyl end (Gly) (amide in !8mature form from following glycine) #status !8experimental SUMMARY #length 86 #molecular-weight 9766 #checksum 8020 SEQUENCE /// ENTRY RHID1S #type complete TITLE gonadoliberin I precursor - sharptooth catfish ALTERNATE_NAMES gonadoliberin, catfish-type; gonadotropin-releasing hormone I (GnRH-I); gonadotropin-releasing hormone, catfish-type; preprogonadotropin-releasing hormone CONTAINS gonadoliberin I; gonadoliberin I-associated protein form I; gonadoliberin I-associated protein form II ORGANISM #formal_name Clarias gariepinus #common_name sharptooth catfish DATE 30-Sep-1993 #sequence_revision 18-Mar-1997 #text_change 18-Jun-1999 ACCESSIONS S45602; S45601; JC1242; S42936; S42937 REFERENCE S45600 !$#authors Bogerd, J.; Zandbergen, T.; Andersson, E.; Goos, H. !$#journal Eur. J. Biochem. (1994) 222:541-549 !$#title Isolation, characterization and expression of cDNAs encoding !1the catfish-type and chicken-II-type !1gonadotropin-releasing-hormone precursors in the African !1catfish. !$#cross-references MUID:94291651; PMID:8020492 !$#accession S45602 !'##molecule_type mRNA !'##residues 1-80 ##label BOG1 !'##cross-references EMBL:X78049; NID:g459433; PIDN:CAA54971.1; !1PID:g459434 !'##note gonadoliberin I-associated protein form I !$#accession S45601 !'##molecule_type mRNA !'##residues 1-46,'S',48-59,'G',61-80 ##label BOG2 !'##cross-references EMBL:X78048; NID:g459431; PIDN:CAA54970.1; !1PID:g459432 !'##note gonadoliberin I-associated protein form II, presumed to be a !1polymorphic form REFERENCE JC1242 !$#authors Bogerd, J.; Li, K.W.; Janssen-Dommerholt, C.; Goos, H. !$#journal Biochem. Biophys. Res. Commun. (1992) 187:127-134 !$#title Two gonadotropin-releasing hormones from African catfish !1(Clarias gariepinus). !$#cross-references MUID:92392313; PMID:1520292 !$#accession JC1242 !'##molecule_type protein !'##residues 22-31 ##label BOG3 !'##experimental_source brain CLASSIFICATION #superfamily gonadoliberin KEYWORDS amidated carboxyl end; hormone; hypothalamus; pyroglutamic !1acid FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-31 #product gonadoliberin I #status experimental #label !8MAT1\ !$35-80 #product gonadoliberin I-associated protein #status !8predicted #label MAT2\ !$22 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$31 #modified_site amidated carboxyl end (Gly) (amide in !8mature form from following glycine) #status !8experimental SUMMARY #length 80 #molecular-weight 9062 #checksum 8190 SEQUENCE /// ENTRY RHHUT #type complete TITLE thyroliberin precursor [validated] - human ALTERNATE_NAMES prothyrotropin; thyrotropin-releasing hormone precursor; TRH CONTAINS prothyroliberin; thyroliberin ORGANISM #formal_name Homo sapiens #common_name man DATE 22-Jun-1990 #sequence_revision 12-May-1995 #text_change 08-Dec-2000 ACCESSIONS A34550 REFERENCE A34550 !$#authors Yamada, M.; Radovick, S.; Wondisford, F.E.; Nakayama, Y.; !1Weintraub, B.D.; Wilber, J.F. !$#journal Mol. Endocrinol. (1990) 4:551-556 !$#title Cloning and structure of human genomic DNA and hypothalamic !1cDNA encoding human preproThyrotropin-releasing hormone. !$#cross-references MUID:91125361; PMID:2126343 !$#accession A34550 !'##molecule_type DNA; mRNA !'##residues 1-242 ##label YAM !'##cross-references GB:M63581; GB:M63582; NID:g190296; PIDN:AAA36480.1; !1PID:g190298; GB:M58043; GB:M58044; GB:M60723; GB:M63393 COMMENT The peptide hormone is released from the hypothalamus. GENETICS !$#gene GDB:TRH !'##cross-references GDB:128072; OMIM:275120 !$#map_position 3pter-3qter !$#introns 71/1 !$#note the first intron occurs before the initiator codon FUNCTION !$#description stimulates synthesis and secretion of thyrotropin from the !1anterior pituitary CLASSIFICATION #superfamily thyroliberin precursor KEYWORDS amidated carboxyl end; hormone; hypothalamus; polyprotein; !1pyroglutamic acid FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-242 #product prothyroliberin #status predicted #label !8PTL\ !$84-86 #product thyroliberin #status experimental #label !8TL1\ !$114-116 #product thyroliberin #status experimental #label !8TL2\ !$135-137 #product thyroliberin #status experimental #label !8TL3\ !$152-154 #product thyroliberin #status experimental #label !8TL4\ !$186-188 #product thyroliberin #status experimental #label !8TL5\ !$227-229 #product thyroliberin #status experimental #label !8TL6\ !$84,114,135,152,186, !$227 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$86,116,137,154,188, !$229 #modified_site amidated carboxyl end (Pro) (amide in !8mature form from following glycine) #status !8experimental SUMMARY #length 242 #molecular-weight 27404 #checksum 4193 SEQUENCE /// ENTRY RTMST #type complete TITLE thyroliberin precursor - mouse ALTERNATE_NAMES prothyrotropin; thyrotropin-releasing hormone precursor; TRH CONTAINS prothyroliberin; thyroliberin ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1993 #sequence_revision 12-May-1995 #text_change 18-Jun-1999 ACCESSIONS A43955 REFERENCE A43955 !$#authors Satoh, T.; Yamada, M.; Monden, T.; Iizuka, M.; Mori, M. !$#journal Brain Res. Mol. Brain Res. (1992) 14:131-135 !$#title Cloning of the mouse hypothalamic !1preprothyrotropin-releasing hormone (TRH) cDNA and tissue !1distribution of its mRNA. !$#cross-references MUID:92356787; PMID:1323011 !$#accession A43955 !'##molecule_type mRNA !'##residues 1-256 ##label SAT !'##cross-references GB:X59387; NID:g425251; PIDN:CAA42030.1; !1PID:g425252; GB:S42180 !'##experimental_source hypothalamus !'##note sequence extracted from NCBI backbone (NCBIN:110500, !1NCBIP:110501) !'##note the mRNA was found to be expressed only in hypothalamus and !1testis COMMENT The peptide hormone is released from the hypothalamus. FUNCTION !$#description stimulates synthesis and secretion of thyrotropin from the !1anterior pituitary CLASSIFICATION #superfamily thyroliberin precursor KEYWORDS amidated carboxyl end; hormone; hypothalamus; polyprotein; !1pyroglutamic acid FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-255 #product prothyroliberin #status predicted #label !8PTL\ !$77-79 #product thyroliberin #status experimental #label !8TL1\ !$109-111 #product thyroliberin #status experimental #label !8TL2\ !$154-156 #product thyroliberin #status experimental #label !8TL3\ !$172-174 #product thyroliberin #status experimental #label !8TL4\ !$203-205 #product thyroliberin #status experimental #label !8TL5\ !$77,109,154,172,203 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$79,111,156,174,205 #modified_site amidated carboxyl end (Pro) (amide in !8mature form from following glycine) #status !8experimental SUMMARY #length 256 #molecular-weight 29181 #checksum 3766 SEQUENCE /// ENTRY RHRTT #type complete TITLE thyroliberin precursor - rat ALTERNATE_NAMES prothyrotropin; thyrotropin-releasing hormone (TRH) CONTAINS prothyroliberin ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 18-Jun-1999 ACCESSIONS A31773; A43630; I59662; A01414; A34155 REFERENCE A31773 !$#authors Lee, S.L.; Stewart, K.; Goodman, R.H. !$#journal J. Biol. Chem. (1988) 263:16604-16609 !$#title Structure of the gene encoding rat thyrotropin releasing !1hormone. !$#cross-references MUID:89034143; PMID:2903153 !$#accession A31773 !'##molecule_type DNA !'##residues 1-255 ##label LEE1 !'##cross-references GB:M12138; NID:g207467; PIDN:AAA42275.1; !1PID:g207468 REFERENCE A43630 !$#authors Lee, S.L.; Sevarino, K.; Roos, B.A.; Goodman, R.H. !$#journal Ann. N. Y. Acad. Sci. (1989) 553:14-28 !$#title Characterization and expression of the gene-encoding rat !1thyrotropin-releasing hormone (TRH). !$#cross-references MUID:89245682; PMID:2497670 !$#accession A43630 !'##molecule_type DNA !'##residues 1-255 ##label LEE2 !'##cross-references GB:M27463; GB:M27464; GB:M27465; NID:g532640; !1PIDN:AAA42239.1; PID:g532642 REFERENCE I59662 !$#authors Mandel, G.; Goodman, R.H. !$#journal Trends Neurosci. (1987) 10:101-104 !$#title Using the brain to screen cloned genes. !$#accession I59662 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-255 ##label MAN !'##cross-references GB:M36317; NID:g207469; PIDN:AAA42276.1; !1PID:g207470 REFERENCE A01414 !$#authors Lechan, R.M.; Wu, P.; Jackson, I.M.D.; Wolf, H.; Cooperman, !1S.; Mandel, G.; Goodman, R.H. !$#journal Science (1986) 231:159-161 !$#title Thyrotropin-releasing hormone precursor: characterization in !1rat brain. !$#cross-references MUID:86096758; PMID:3079917 !$#accession A01414 !'##molecule_type mRNA !'##residues 1-255 ##label LEC !'##cross-references GB:M12138; NID:g207467; PIDN:AAA42275.1; !1PID:g207468 REFERENCE A34155 !$#authors Sevarino, K.A.; Goodman, R.H.; Spiess, J.; Jackson, I.M.D.; !1Wu, P. !$#journal J. Biol. Chem. (1989) 264:21529-21535 !$#title Thyrotropin-releasing hormone (TRH) precursor processing. !1Characterization of mature TRH and non-TRH peptides !1synthesized by transfected mammalian cells. !$#cross-references MUID:90094321; PMID:2513321 !$#accession A34155 !'##molecule_type protein !'##residues !125-50;53-54;58-59;61;63;65-67;208-218;221-224;226-228; !1230-232 ##label SEV !'##note examination of peptides released during processing COMMENT The peptide hormone thyroliberin is released from the !1hypothalamus. GENETICS !$#gene Trh !$#introns 70/1 !$#note the first intron occurs before the initiator codon FUNCTION !$#description stimulates synthesis and secretion of thyrotropin from the !1anterior pituitary CLASSIFICATION #superfamily thyroliberin precursor KEYWORDS amidated carboxyl end; hormone; hypothalamus; polyprotein; !1pyroglutamic acid FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-255 #product prothyroliberin #status predicted #label !8PTL\ !$77-79 #product thyroliberin #status experimental #label !8TL1\ !$109-111 #product thyroliberin #status experimental #label !8TL2\ !$154-156 #product thyroliberin #status experimental #label !8TL3\ !$172-174 #product thyroliberin #status experimental #label !8TL4\ !$202-204 #product thyroliberin #status experimental #label !8TL5\ !$77,109,154,172,202 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$79,111,156,174,204 #modified_site amidated carboxyl end (Pro) (amide in !8mature form from following glycine) #status !8experimental SUMMARY #length 255 #molecular-weight 29284 #checksum 1922 SEQUENCE /// ENTRY RHXLT #type complete TITLE thyroliberin precursor - African clawed frog ALTERNATE_NAMES thyrotropin-releasing hormone; TRH CONTAINS thyroliberin ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 28-May-1986 #sequence_revision 12-May-1995 #text_change 18-Jun-1999 ACCESSIONS A37061; A01416; T00997 REFERENCE A37061 !$#authors Kuchler, K.; Richter, K.; Trnovsky, J.; Egger, R.; Kreil, G. !$#journal J. Biol. Chem. (1990) 265:11731-11733 !$#title Two precursors of thyrotropin-releasing hormone from skin of !1Xenopus laevis. Each contains seven copies of the end !1product. !$#cross-references MUID:90307692; PMID:1694847 !$#accession A37061 !'##molecule_type mRNA !'##residues 1-227 ##label KUC !'##cross-references GB:M34699; GB:J05514; NID:g214839; PIDN:AAA49973.1; !1PID:g214840 !'##experimental_source skin; clone TRH-L4 REFERENCE A01416 !$#authors Richter, K.; Kawashima, E.; Egger, R.; Kreil, G. !$#journal EMBO J. (1984) 3:617-621 !$#title Biosynthesis of thyrotropin releasing hormone in the skin of !1Xenopus laevis: partial sequence of the precursor deduced !1from cloned cDNA. !$#cross-references MUID:84182535; PMID:6425056 !$#accession A01416 !'##molecule_type mRNA !'##residues 1-35,'S',37-69,'I',71-123 ##label RIC !'##experimental_source skin !$#accession T00997 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-35,'S',37-69,'I',71-123,'PP' ##label RIH !'##cross-references EMBL:X00770; NID:g65150; PIDN:CAA25345.1; !1PID:g65151 COMMENT The peptide hormone thyroliberin is released from the skin. CLASSIFICATION #superfamily thyroliberin precursor KEYWORDS amidated carboxyl end; hormone; polyprotein; pyroglutamic !1acid; skin FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-227 #product prothyroliberin #status predicted #label !8PTL\ !$75-77 #product thyroliberin #status experimental #label !8TL1\ !$89-91 #product thyroliberin #status experimental #label !8TL2\ !$107-109 #product thyroliberin #status experimental #label !8TL3\ !$121-123 #product thyroliberin #status experimental #label !8TL4\ !$153-156 #product thyroliberin #status experimental #label !8TL5\ !$168-170 #product thyroliberin #status experimental #label !8TL6\ !$193-195 #product thyroliberin #status experimental #label !8TL7\ !$75,89,107,121,153, !$168,193 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$77,91,109,123,155, !$170,195 #modified_site amidated carboxyl end (Pro) (amide in !8mature form from following glycine) #status !8experimental SUMMARY #length 227 #molecular-weight 26336 #checksum 7957 SEQUENCE /// ENTRY NYPG7 #type complete TITLE hypothalamic heptapeptide - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 01-Sep-1981 #sequence_revision 01-Sep-1981 #text_change 23-Aug-1996 ACCESSIONS A01417 REFERENCE A01417 !$#authors Chang, R.C.C.; Huang, W.Y.; Arimura, A.; Redding, T.W.; Coy, !1D.H.; Saffran, M.; Kong, A.; Hamilton, J.W.; Cohn, D.V.; !1Schally, A.V. !$#journal Horm. Metab. Res. (1981) 13:228-232 !$#title Isolation, structure and synthesis of a heptapeptide with in !1vitro ACTH-releasing activity from porcine hypothalamus. !$#cross-references MUID:81213980; PMID:6263778 !$#accession A01417 !'##molecule_type protein !'##residues 1-7 ##label CHA CLASSIFICATION #superfamily hypothalamic heptapeptide KEYWORDS hypothalamus SUMMARY #length 7 #molecular-weight 957 #checksum 2245 SEQUENCE /// ENTRY POBO #type complete TITLE posterior pituitary peptide - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 22-Jun-1981 #sequence_revision 22-Jun-1981 #text_change 23-Aug-1996 ACCESSIONS A01418 REFERENCE A01418 !$#authors Preddie, E.C. !$#journal J. Biol. Chem. (1965) 240:4194-4203 !$#title Structure of a large polypeptide of bovine posterior !1pituitary tissue. !$#cross-references MUID:66045180; PMID:5845822 !$#accession A01418 !'##molecule_type protein !'##residues 1-48 ##label PRE CLASSIFICATION #superfamily posterior pituitary peptide KEYWORDS pituitary FEATURE !$34-37,40-45 #disulfide_bonds #status experimental SUMMARY #length 48 #molecular-weight 5080 #checksum 9061 SEQUENCE /// ENTRY NYPG14 #type complete TITLE hypothalamic tetradecapeptide - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 13-Jul-1981 #sequence_revision 13-Jul-1981 #text_change 23-Aug-1996 ACCESSIONS A01419 REFERENCE A01419 !$#authors Schlesinger, D.H.; Niall, H.D.; Linthicum, G.L.; Dupont, A.; !1Schally, A.V. !$#submission submitted to the Atlas, November 1976 !$#accession A01419 !'##molecule_type protein !'##residues 1-14 ##label SCH CLASSIFICATION #superfamily hypothalamic tetradecapeptide KEYWORDS amidated carboxyl end; hypothalamus FEATURE !$14 #modified_site amidated carboxyl end (Tyr) #status !8experimental SUMMARY #length 14 #molecular-weight 1648 #checksum 8460 SEQUENCE /// ENTRY UNHUCF #type complete TITLE ciliary neurotrophic factor - human ALTERNATE_NAMES CNTF; survival factor ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 18-Jun-1999 ACCESSIONS JH0455; JH0567; S17846; S17658; I58125 REFERENCE JH0455 !$#authors Masiakowski, P.; Liu, H.; Radziejewski, C.; Lottspeich, F.; !1Oberthuer, W.; Wong, V.; Lindsay, R.M.; Furth, M.E.; !1Panayotatos, N. !$#journal J. Neurochem. (1991) 57:1003-1012 !$#title Recombinant human and rat ciliary neurotrophic factors. !$#cross-references MUID:91318259; PMID:1861138 !$#accession JH0455 !'##molecule_type DNA !'##residues 1-200 ##label MAS REFERENCE JH0567 !$#authors Lam, A.; Fuller, F.; Miller, J.; Kloss, J.; Manthorpe, M.; !1Varon, S.; Cordell, B. !$#journal Gene (1991) 102:271-276 !$#title Sequence and structural organization of the human gene !1encoding ciliary neurotrophic factor. !$#cross-references MUID:91340164; PMID:1840538 !$#accession JH0567 !'##molecule_type DNA !'##residues 1-200 ##label LAM !'##cross-references EMBL:X55889; NID:g30004; PIDN:CAA39374.1; !1PID:g825644; EMBL:X55890 REFERENCE S17846 !$#authors Negro, A.; Tolosano, E.; Skaper, S.D.; Martini, I.; !1Callegaro, L.; Silengo, L.; Fiorini, F.; Altruda, F. !$#journal Eur. J. Biochem. (1991) 201:289-294 !$#title Cloning and expression of human ciliary neurotrophic factor. !$#cross-references MUID:92007888; PMID:1915374 !$#accession S17846 !'##molecule_type DNA !'##residues 1-200 ##label NEG !'##cross-references EMBL:X60477; NID:g29999; PIDN:CAA43009.1; !1PID:g825643; EMBL:X60478 REFERENCE S17658 !$#authors McDonald, J.R.; Ko, C.; Mismer, D.; Smith, D.J.; Collins, F. !$#journal Biochim. Biophys. Acta (1991) 1090:70-80 !$#title Expression and characterization of recombinant human ciliary !1neurotrophic factor from Escherichia coli. !$#cross-references MUID:91355232; PMID:1883844 !$#accession S17658 !'##molecule_type DNA !'##residues 1-200 ##label MCD !'##cross-references EMBL:X60542; NID:g30002; PIDN:CAA43032.1; !1PID:g30003 REFERENCE I58125 !$#authors Takahashi, R.; Yokoji, H.; Misawa, H.; Hayashi, M.; Hu, J.; !1Deguchi, T. !$#journal Nature Genet. (1994) 7:79-84 !$#title A null mutation in the human CNTF gene is not causally !1related to neurological diseases. !$#cross-references MUID:94355982; PMID:8075647 !$#accession I58125 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-38,'PGEASGPEQEHQPGLCGWDASGKH' ##label RES !'##cross-references GB:S72921; NID:g633829; PIDN:AAB31818.1; !1PID:g633830 COMMENT A 25-residue segment having the characteristics of a PEST !1region appears in the first third of the protein. COMMENT The middle half bears a distinct resemblance to a !1113-residue segment of human brain-derived neurotrophic !1factor precursor. COMMENT CNTF has the characteristics of a nonsecreted, cytoplasmic !1protein; however, a receptor for this protein is found !1exclusively in nervous and skeletal muscle tissues (see !1ciliary neurotrophic factor receptor, PIR:UHHUCN). COMMENT CNTF promotes survival, neurotransmitter synthesis, and !1neurite outgrowth in certain neuronal populations. COMMENT Although CNTF was first thought to affect only ciliary or !1parasympathetic neurons, it has been found to prevent death !1of peripheral neurons in vitro and in vivo in chickens and !1rodents. COMMENT CNTF is being tested for treatment of human motor neuron !1diseases, such as amyotrophic lateral sclerosis. GENETICS !$#gene GDB:CNTF !'##cross-references GDB:125919; OMIM:118945 !$#map_position 11q12.2-11q12.2 !$#introns 38/3 CLASSIFICATION #superfamily ciliary neurotrophic factor KEYWORDS growth factor; peripheral neuron SUMMARY #length 200 #molecular-weight 22931 #checksum 1179 SEQUENCE /// ENTRY UNRTCF #type complete TITLE ciliary neurotrophic factor - rat ALTERNATE_NAMES CNTF; survival factor ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 18-Jun-1999 ACCESSIONS S08144; A43007 REFERENCE S08144 !$#authors Stoeckli, K.A.; Lottspeich, F.; Sendtner, M.; Masiakowski, !1P.; Carroll, P.; Goetz, R.; Lindholm, D.; Thoenen, H. !$#journal Nature (1989) 342:920-923 !$#title Molecular cloning, expression and regional distribution of !1rat ciliary neurotrophic factor. !$#cross-references MUID:90081871; PMID:2594085 !$#accession S08144 !'##molecule_type mRNA !'##residues 1-200 ##label ST1 !'##cross-references EMBL:X17457; NID:g55968; PIDN:CAA35500.1; !1PID:g55969 !$#accession A43007 !'##molecule_type protein !'##residues 20-25;29-40;47-60;65-92;113-154;161-166;184-200 ##label ST2 COMMENT CNTF has the characteristics of a nonsecreted, cytoplasmic !1protein; however, a receptor for this protein is found !1exclusively in nervous and skeletal muscle tissues (see !1ciliary neurotrophic factor receptor, PIR:I58141). COMMENT CNTF promotes survival, neurotransmitter synthesis, and !1neurite outgrowth in certain neuronal populations. CLASSIFICATION #superfamily ciliary neurotrophic factor KEYWORDS growth factor; peripheral neuron SUMMARY #length 200 #molecular-weight 22854 #checksum 2308 SEQUENCE /// ENTRY UNRBCF #type complete TITLE ciliary neurotrophic factor - rabbit ALTERNATE_NAMES CNTF; survival factor ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 30-Jun-1993 ACCESSIONS A40082; B40082; C40082; A36286 REFERENCE A40082 !$#authors Lin, L.F.H.; Mismer, D.; Lile, J.D.; Armes, L.G.; Butler !1III, E.T.; Vannice, J.L.; Collins, F. !$#journal Science (1989) 246:1023-1025 !$#title Purification, cloning, and expression of ciliary !1neurotrophic factor (CNTF). !$#cross-references MUID:90069557; PMID:2587985 !$#accession A40082 !'##molecule_type mRNA !'##residues 1-199 ##label LI1 !'##cross-references GB:M29828 !$#accession B40082 !'##molecule_type DNA !'##residues 44-159 ##label LI2 !$#accession C40082 !'##molecule_type protein !'##residues 6-15;23-59;93-103;148-170;174-178 ##label LI3 REFERENCE A36286 !$#authors Lin, L.F.H.; Armes, L.G.; Sommer, A.; Smith, D.J.; Collins, !1F. !$#journal J. Biol. Chem. (1990) 265:8942-8947 !$#title Isolation and characterization of ciliary neurotrophic !1factor from rabbit sciatic nerves. !$#cross-references MUID:90256829; PMID:2341413 !$#accession A36286 !'##molecule_type protein !'##residues 6-15;23-59;93-103;140-147;148-169;174-178 ##label LI4 COMMENT CNTF has the characteristics of a nonsecreted, cytoplasmic !1protein; however, a receptor for this protein is found !1exclusively in nervous and skeletal muscle tissues (see !1ciliary neurotrophic factor receptor). COMMENT CNTF promotes survival, neurotransmitter synthesis, and !1neurite outgrowth in certain neuronal populations. CLASSIFICATION #superfamily ciliary neurotrophic factor KEYWORDS growth factor; peripheral neuron SUMMARY #length 199 #molecular-weight 22662 #checksum 8387 SEQUENCE /// ENTRY UNDG #type complete TITLE neurotensin precursor - dog CONTAINS neuromedin N; neuromedin N-125; neurotensin ORGANISM #formal_name Canis lupus familiaris #common_name dog DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 18-Jun-1999 ACCESSIONS A28025; B60319; A60319; A60324; JN0293; A36272 REFERENCE A28025 !$#authors Dobner, P.R.; Barber, D.L.; Villa-Komaroff, L.; McKiernan, !1C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:3516-3520 !$#title Cloning and sequence analysis of cDNA for the canine !1neurotensin/neuromedin N precursor. !$#cross-references MUID:87204168; PMID:3472221 !$#accession A28025 !'##molecule_type mRNA !'##residues 1-170 ##label DOB !'##cross-references GB:M16443; NID:g164033; PIDN:AAA30878.1; !1PID:g164034 REFERENCE A60319 !$#authors Mitra, S.P.; Muraki, K.; Brown, D.R.; Parsons, A.M.; !1Carraway, R.E. !$#journal Regul. Pept. (1990) 28:11-22 !$#title Canine neurotensin, neurotensin(6-13) and neuromedin N: !1primary structures and receptor activity. !$#cross-references MUID:90222594; PMID:2158127 !$#accession B60319 !'##molecule_type protein !'##residues 143-148 ##label MIT !$#accession A60319 !'##molecule_type protein !'##residues 'E',152-163 ##label MI2 REFERENCE A60324 !$#authors Mogard, M.H.; Reeve Jr., J.R.; Shively, J.E.; Ben-Avram, !1C.M.; Eysselein, V.E.; Walsh, J.H. !$#journal Regul. Pept. (1986) 14:313-321 !$#title Isolation and characterization of a neurotensin-like !1decapeptide from a canine upper small intestinal extract. !$#cross-references MUID:86314883; PMID:3749527 !$#accession A60324 !'##molecule_type protein !'##residues 154-163 ##label MOG REFERENCE JN0293 !$#authors Carraway, R.E.; Mitra, S.P. !$#journal Biochem. Biophys. Res. Commun. (1991) 179:301-308 !$#title Purification of large neuromedin N (NMN) from canine !1intestine and its identification as NMN-125. !$#cross-references MUID:91354266; PMID:1883359 !$#accession JN0293 !'##molecule_type protein !'##residues 24-43 ##label CAR !'##experimental_source small intestine REFERENCE A36272 !$#authors Carraway, R.E.; Mitra, S.P. !$#journal J. Biol. Chem. (1990) 265:8627-8631 !$#title Differential processing of neurotensin/neuromedin N !1precursor(s) in canine brain and intestine. !$#cross-references MUID:90256783; PMID:2341398 !$#accession A36272 !'##molecule_type protein !'##residues 128-147 ##label CA2 CLASSIFICATION #superfamily neurotensin KEYWORDS hormone; neuropeptide; pyroglutamic acid FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-148 #product large neuromedin N-125 #status experimental !8#label LNM\ !$143-148 #product neuromedin N #status experimental #label !8NMN\ !$151-163 #product neurotensin #status experimental #label NTS\ !$151 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental SUMMARY #length 170 #molecular-weight 19863 #checksum 7873 SEQUENCE /// ENTRY UNBO #type complete TITLE neurotensin - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 18-Dec-1981 #sequence_revision 18-Dec-1981 #text_change 24-Feb-1995 ACCESSIONS A01420 REFERENCE A92172 !$#authors Carraway, R.; Leeman, S.E. !$#journal J. Biol. Chem. (1975) 250:1907-1911 !$#title The amino acid sequence of a hypothalamic peptide, !1neurotensin. !$#cross-references MUID:75095678; PMID:1167549 !$#accession A01420 !'##molecule_type protein !'##residues 1-13 ##label CAR !'##experimental_source hypothalamus REFERENCE A92173 !$#authors Carraway, R.; Leeman, S.E. !$#journal J. Biol. Chem. (1975) 250:1912-1918 !$#title The synthesis of neurotensin. !$#cross-references MUID:75095679; PMID:1112838 !$#contents annotation; synthesis !$#note a tridecapeptide chemically and pharmacologically identical !1with the natural peptide was synthesized CLASSIFICATION #superfamily neurotensin KEYWORDS neuropeptide; pyroglutamic acid FEATURE !$1 #modified_site pyrrolidone carboxylic acid (Gln) !8#status experimental SUMMARY #length 13 #molecular-weight 1690 #checksum 7213 SEQUENCE /// ENTRY UNOPBT #type complete TITLE neurotensin - brush-tailed possum ORGANISM #formal_name Trichosurus vulpecula #common_name brush-tailed possum DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 05-Aug-1994 ACCESSIONS A60064 REFERENCE A60064 !$#authors Shaw, C.; Murphy, R.; Thim, L.; Furness, J.B.; Buchanan, !1K.D. !$#journal Regul. Pept. (1991) 35:49-57 !$#title Marsupial possum neurotensin: a unique mammalian regulatory !1peptide exhibiting structural homology to the avian !1analogue. !$#cross-references MUID:92021617; PMID:1924896 !$#accession A60064 !'##molecule_type protein !'##residues 1-13 ##label SHA CLASSIFICATION #superfamily neurotensin KEYWORDS hypothalamus; intestine; neuropeptide; pyroglutamic acid FEATURE !$1 #modified_site pyrrolidone carboxylic acid (Gln) !8#status experimental SUMMARY #length 13 #molecular-weight 1610 #checksum 7185 SEQUENCE /// ENTRY SFRT #type complete TITLE scotophobin - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 23-Oct-1981 #sequence_revision 23-Oct-1981 #text_change 07-May-1999 ACCESSIONS A93164; A92757; A01423 REFERENCE A93164 !$#authors Ungar, G.; Desiderio, D.M.; Parr, W. !$#journal Nature (1972) 238:198-202 !$#title Isolation, identification and synthesis of a !1specific-behaviour-inducing brain peptide. !$#cross-references MUID:72240741; PMID:4558348 !$#accession A93164 !'##molecule_type protein !'##residues 1-15 ##label UNG !'##note chemical synthesis REFERENCE A92757 !$#authors Desiderio, D.M.; Ungar, G.; White, P.A. !$#journal J. Chem. Soc. D Chem. Commun. (1971) 1971:432-433 !$#title The use of mass spectrometry in the structural elucidation !1of scotophobin -- a specific behaviour-inducing brain !1peptide. !$#accession A92757 !'##molecule_type protein !'##residues 1-15 ##label DES !'##experimental_source brain !'##note the sequence was determined by mass spectrometry REFERENCE A93165 !$#authors Stewart, W.W. !$#journal Nature (1972) 238:202-209 !$#title Comments on the chemistry of scotophobin. !$#cross-references MUID:72240742; PMID:4558349 !$#contents annotation; referee's comments on first reference above REFERENCE A93166 !$#authors Ungar, G.; Desiderio, D.M.; Parr, W. !$#journal Nature (1972) 238:209-210 !$#contents annotation !$#note reply to referee's comments REFERENCE A43076 !$#authors Wilson, D. !$#journal Nature (1986) 320:313-314 !$#title Scotophobin resurrected as a neuropeptide. !$#cross-references MUID:86175024; PMID:3960116 !$#contents annotation !$#note comparison with other neuropeptides; author presents !1scotophobin sequence in the reverse direction in Table 1, !1apparently because the carboxyl-terminal amide group was !1misinterpreted as indicating the amino end CLASSIFICATION #superfamily scotophobin KEYWORDS amidated carboxyl end FEATURE !$15 #modified_site amidated carboxyl end (Tyr) #status !8experimental SUMMARY #length 15 #molecular-weight 1582 #checksum 9265 SEQUENCE /// ENTRY AWHU #type complete TITLE natriuretic peptide A precursor [validated] - human ALTERNATE_NAMES ANF; atrial natriuretic factor; atrial natriuretic protein; prepronatriodilatin (PND) CONTAINS atrial alpha natriuretic peptide (ANP); cardiodilatin (atrial gamma natriuretic factor) ORGANISM #formal_name Homo sapiens #common_name man DATE 15-Nov-1984 #sequence_revision 15-Nov-1984 #text_change 08-Dec-2000 ACCESSIONS A22693; B22693; A01424; B29370; A32733; I58054; S14097; !1I39458; I39459; I39460; I37167 REFERENCE A22693 !$#authors Nemer, M.; Chamberland, M.; Sirois, D.; Argentin, S.; !1Drouin, J.; Dixon, R.A.F.; Zivin, R.A.; Condra, J.H. !$#journal Nature (1984) 312:654-656 !$#title Gene structure of human cardiac hormone precursor, !1pronatriodilatin. !$#cross-references MUID:85061626; PMID:6095118 !$#accession A22693 !'##molecule_type DNA !'##residues 1-151 ##label NEM !'##cross-references GB:X01470; NID:g28687; PIDN:CAA25699.1; PID:g825625 !$#accession B22693 !'##molecule_type DNA !'##residues 1-151,'RR' ##label NE2 !'##note allelic variant with UGA termination codon replaced by CGA !1arginine codon REFERENCE A01424 !$#authors Oikawa, S.; Imai, M.; Ueno, A.; Tanaka, S.; Noguchi, T.; !1Nakazato, H.; Kangawa, K.; Fukuda, A.; Matsuo, H. !$#journal Nature (1984) 309:724-726 !$#title Cloning and sequence analysis of cDNA encoding a precursor !1for human atrial natriuretic polypeptide. !$#cross-references MUID:84219799; PMID:6203042 !$#accession A01424 !'##molecule_type mRNA !'##residues 1-151 ##label OIK !'##cross-references GB:K02043; NID:g178629; PIDN:AAB59379.1; !1PID:g178630 REFERENCE A29370 !$#authors Seidman, C.E.; Bloch, K.D.; Klein, K.A.; Smith, J.A.; !1Seidman, J.G. !$#journal Science (1984) 226:1206-1209 !$#title Nucleotide sequences of the human and mouse atrial !1natriuretic factor genes. !$#cross-references MUID:85065766; PMID:6542248 !$#accession B29370 !'##molecule_type DNA !'##residues 1-64,'D',66-151 ##label SEI !'##cross-references GB:K02043 REFERENCE A32733 !$#authors Kangawa, K.; Matsuo, H. !$#journal Biochem. Biophys. Res. Commun. (1984) 118:131-139 !$#title Purification and complete amino acid sequence of alpha-human !1atrial natriuretic polypeptide (alpha-hANP). !$#cross-references MUID:84128019; PMID:6230082 !$#accession A32733 !'##molecule_type protein !'##residues 124-151 ##label KAN REFERENCE I58054 !$#authors Nakayama, K.; Ohkubo, H.; Hirose, T.; Inayama, S.; !1Nakanishi, S. !$#journal Nature (1984) 310:699-701 !$#title mRNA sequence for human cardiodilatin-atrial natriuretic !1factor precursor and regulation of precursor mRNA in rat !1atria. !$#cross-references MUID:84295577; PMID:6547996 !$#accession I58054 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-151 ##label RES !'##cross-references GB:M30262; NID:g180181; PIDN:AAA35669.1; !1PID:g180182 REFERENCE S14097 !$#authors Vanneste, Y.; Michel, A.; Deschodt-Lanckman, M. !$#journal Eur. J. Biochem. (1991) 196:281-286 !$#title Hydrolysis of intact and Cys-Phe-cleaved human atrial !1natriuretic peptide in vitro by human tissue kallikrein. !$#cross-references MUID:91176998; PMID:1826098 !$#accession S14097 !'##molecule_type protein !'##residues 124-151 ##label VAN !'##note natural and synthetic peptide sujected to kallikrein !1proteolysis REFERENCE I39458 !$#authors Zivin, R.A.; Condra, J.H.; Dixon, R.A.; Seidah, N.G.; !1Chretien, M.; Nemer, M.; Chamberland, M.; Drouin, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:6325-6329 !$#title Molecular cloning and characterization of DNA sequences !1encoding rat and human atrial natriuretic factors. !$#cross-references MUID:85038509; PMID:6238331 !$#accession I39458 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 119-151,'RR' ##label RE2 !'##cross-references GB:K02044; NID:g178631; PIDN:AAA51730.1; !1PID:g178632 REFERENCE I39459 !$#authors Maki, M.; Parmentier, M.; Inagami, T. !$#journal Biochem. Biophys. Res. Commun. (1984) 125:797-802 !$#title Cloning of genomic DNA for human atrial natriuretic factor. !$#cross-references MUID:85096983; PMID:6097248 !$#accession I39459 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-75 ##label RE3 !'##cross-references GB:K02399; NID:g178633; PIDN:AAA35528.1; !1PID:g178634 REFERENCE I39460 !$#authors Seidman, C.E.; Bloch, K.D.; Zisfein, J.; Smit, J.; Haber, !1E.; Homcy, C.J.; Duby, A.D.; Choi, E.; Graham, R.M.; !1Seidman, J.G. !$#journal Hypertension (1985) 7:31-34 !$#title Molecular studies of the atrial natriuretic factor gene. !$#accession I39460 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-64,'D',66-151 ##label RE4 !'##cross-references GB:M54951; NID:g178636; PIDN:AAA35529.1; !1PID:g178638 REFERENCE I37167 !$#authors Greenberg, B.D.; Bencen, G.H.; Seilhamer, J.J.; Lewicki, !1J.A.; Fiddes, J.C. !$#journal Nature (1984) 312:656-658 !$#title Nucleotide sequence of the gene encoding human atrial !1natriuretic factor precursor. !$#cross-references MUID:85061627; PMID:6095119 !$#accession I37167 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 26-151 ##label RE5 !'##cross-references EMBL:X01471; NID:g28690; PIDN:CAA25700.1; !1PID:g1340150 COMMENT Cardiodilantin is a vasoconstrictor but not a diuretic or !1natriuretic. GENETICS !$#gene GDB:NPPA; ANP; PND !'##cross-references GDB:118727; OMIM:108780 !$#map_position 1p36-1p36 !$#introns 41/3; 150/3 CLASSIFICATION #superfamily natriuretic peptide A precursor KEYWORDS atrium; diuretic; hormone; natriuretic; osmoregulation FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-151 #product cardiodilantin #status predicted #label CDD\ !$124-151 #product atrial alpha natriuretic peptide #status !8experimental #label ANP\ !$130-146 #disulfide_bonds #status experimental SUMMARY #length 151 #molecular-weight 16395 #checksum 3644 SEQUENCE /// ENTRY JQ0947 #type complete TITLE atrial natriuretic peptide precursor - bullfrog ALTERNATE_NAMES ANP; atrial natriuretic factor (ANF) CONTAINS atrial natriuretic peptide-21; atrial natriuretic peptide-24 ORGANISM #formal_name Rana catesbeiana #common_name bullfrog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JQ0947; A31510 REFERENCE JQ0947 !$#authors Kojima, M. !$#submission submitted to JIPID, May 1991 !$#accession JQ0947 !'##molecule_type mRNA !'##residues 1-145 ##label KOJ REFERENCE A31510 !$#authors Sakata, J.; Kangawa, K.; Matsuo, H. !$#journal Biochem. Biophys. Res. Commun. (1988) 155:1338-1345 !$#title Identification of new atrial natriuretic peptides in frog !1heart. !$#cross-references MUID:89025806; PMID:2972279 !$#accession A31510 !'##molecule_type protein !'##residues 122-145 ##label SAK COMMENT In mammals, several active peptides may be derived from the !1prohormone. CLASSIFICATION #superfamily natriuretic peptide A precursor KEYWORDS atrium; diuretic; hormone; natriuretic; osmoregulation FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-121 #domain propeptide #status predicted #label PRO\ !$122-145 #product atrial natriuretic peptide-24 #status !8experimental #label M24\ !$125-145 #product atrial natriuretic peptide-21 #status !8experimental #label M21\ !$125-141 #disulfide_bonds #status predicted SUMMARY #length 145 #molecular-weight 15934 #checksum 1892 SEQUENCE /// ENTRY AWRB #type complete TITLE atrial natriuretic peptide precursor - rabbit ALTERNATE_NAMES ANP; atrial natriuretic polypeptide ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 18-Jun-1999 ACCESSIONS B25302 REFERENCE A90119 !$#authors Oikawa, S.; Imai, M.; Inuzuka, C.; Tawaragi, Y.; Nakazato, !1H.; Matsuo, H. !$#journal Biochem. Biophys. Res. Commun. (1985) 132:892-899 !$#title Structure of dog and rabbit precursors of atrial natriuretic !1polypeptides deduced from nucleotide sequence of cloned !1cDNA. !$#cross-references MUID:86076957; PMID:2934062 !$#accession B25302 !'##molecule_type mRNA !'##residues 1-153 ##label OIK !'##cross-references GB:M12046; NID:g164770; PIDN:AAA31162.1; !1PID:g164771 CLASSIFICATION #superfamily natriuretic peptide A precursor KEYWORDS atrium; diuretic; hormone; natriuretic; osmoregulation FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-151 #product gamma atrial natriuretic factor #status !8predicted #label ANF\ !$124-151 #product alpha atrial natriuretic peptide #status !8predicted #label ANP\ !$130-146 #disulfide_bonds #status predicted SUMMARY #length 153 #molecular-weight 16843 #checksum 7650 SEQUENCE /// ENTRY AWBO #type complete TITLE atrial natriuretic peptide precursor - bovine ALTERNATE_NAMES ANP; atrial natriuretic polypeptide ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 18-Jun-1999 ACCESSIONS A90124; A93049; A24247; A26090 REFERENCE A90124 !$#authors Vlasuk, G.P.; Miller, J.; Bencen, G.H.; Lewicki, J.A. !$#journal Biochem. Biophys. Res. Commun. (1986) 136:396-403 !$#title Structure and analysis of the bovine atrial natriuretic !1peptide precursor gene. !$#cross-references MUID:86215205; PMID:2939830 !$#accession A90124 !'##molecule_type DNA !'##residues 1-152 ##label VLA !'##cross-references GB:M13145; NID:g162665; PIDN:AAA30375.1; !1PID:g162666 REFERENCE A93049 !$#authors Ong, H.; McNicoll, N.; Lazure, C.; Seidah, N.; Chretien, M.; !1Cantin, M.; De Lean, A. !$#journal Life Sci. (1986) 38:1309-1315 !$#title Purification and sequence determination of bovine atrial !1natriuretic factor. !$#cross-references MUID:86173941; PMID:3007908 !$#accession A93049 !'##molecule_type protein !'##residues 123-150 ##label ONG GENETICS !$#introns 40/3; 149/3 CLASSIFICATION #superfamily natriuretic peptide A precursor KEYWORDS atrium; diuretic; hormone; natriuretic; osmoregulation FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-152 #product gamma atrial natriuretic factor #status !8predicted #label ANF\ !$123-150 #product alpha atrial natriuretic peptide #status !8experimental #label ANP\ !$129-145 #disulfide_bonds #status predicted SUMMARY #length 152 #molecular-weight 16518 #checksum 7552 SEQUENCE /// ENTRY S13107 #type complete TITLE atrial natriuretic peptide precursor - pig CONTAINS alpha atrial natriuretic peptide; gamma atrial natriuretic factor (cardiodilatin) ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 21-Nov-1993 #sequence_revision 14-Jul-1994 #text_change 11-May-2000 ACCESSIONS S13107; A60899 REFERENCE S13107 !$#authors Maegert, H.J.; Appelhans, H.; Gassen, H.G.; Forssmann, W.G. !$#journal Nucleic Acids Res. (1990) 18:6704 !$#title Nucleotide sequence of a porcine prepro atrial natriuretic !1peptide (ANP) cDNA. !$#cross-references MUID:91067478; PMID:2147477 !$#accession S13107 !'##molecule_type mRNA !'##residues 1-150 ##label MAE !'##cross-references EMBL:X54669; NID:g1883; PIDN:CAA38480.1; PID:g1884 REFERENCE A60899 !$#authors Forssmann, W.G.; Hock, D.; Lottspeich, A.; Henschen, A.; !1Kreye, V.; Christmann, M.; Reinecke, M.; Metz, J.; !1Carlquist, M.; Mutt, V. !$#journal Anat. Embryol. (1983) 168:307-313 !$#title The right auricle of the heart is an endocrine organ. !1Cardiodilatin as a peptide hormone candidate. !$#cross-references MUID:84176555; PMID:6689515 !$#accession A60899 !'##molecule_type protein !'##residues 25-54 ##label FOR CLASSIFICATION #superfamily natriuretic peptide A precursor KEYWORDS atrium; diuretic; hormone; natriuretic; osmoregulation FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-150 #product gamma atrial natriuretic factor #status !8predicted #label ANF\ !$123-150 #product alpha atrial natriuretic peptide #status !8predicted #label ANP\ !$129-145 #disulfide_bonds #status predicted SUMMARY #length 150 #molecular-weight 16351 #checksum 9859 SEQUENCE /// ENTRY AWDG #type complete TITLE atrial natriuretic peptide precursor - dog ALTERNATE_NAMES ANP; atrial natriuretic polypeptide ORGANISM #formal_name Canis lupus familiaris #common_name dog DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 18-Jun-1999 ACCESSIONS A25302 REFERENCE A90119 !$#authors Oikawa, S.; Imai, M.; Inuzuka, C.; Tawaragi, Y.; Nakazato, !1H.; Matsuo, H. !$#journal Biochem. Biophys. Res. Commun. (1985) 132:892-899 !$#title Structure of dog and rabbit precursors of atrial natriuretic !1polypeptides deduced from nucleotide sequence of cloned !1cDNA. !$#cross-references MUID:86076957; PMID:2934062 !$#accession A25302 !'##molecule_type mRNA !'##residues 1-149 ##label OIK !'##cross-references GB:M12045; NID:g163900; PIDN:AAA30828.1; !1PID:g163901 CLASSIFICATION #superfamily natriuretic peptide A precursor KEYWORDS atrium; diuretic; hormone; natriuretic; osmoregulation FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-149 #product gamma atrial natriuretic factor #status !8predicted #label ANF\ !$122-149 #product alpha atrial natriuretic peptide #status !8predicted #label ANP\ !$128-144 #disulfide_bonds #status predicted SUMMARY #length 149 #molecular-weight 15819 #checksum 8040 SEQUENCE /// ENTRY AWRT #type complete TITLE atrial natriuretic factor precursor - rat CONTAINS ANF(1-33); ANF(2-33); ANF(3-33); ANF(8-33); atrial natriuretic peptide; atriopeptin I; atriopeptin II; auriculin A; auriculin B; preprocardionatrin ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 19-Feb-1984 #sequence_revision 15-Nov-1984 #text_change 18-Jun-1999 ACCESSIONS A22570; A01425; A93332; A43617; A93330; A94275; PT0061; !1A20973; A44190; A60390; I59094; I58057; I52678 REFERENCE A22570 !$#authors Argentin, S.; Nemer, M.; Drouin, J.; Scott, G.K.; Kennedy, !1B.P.; Davies, P.L. !$#journal J. Biol. Chem. (1985) 260:4568-4571 !$#title The gene for rat atrial natriuretic factor. !$#cross-references MUID:85182558; PMID:2985557 !$#accession A22570 !'##molecule_type DNA !'##residues 1-152 ##label ARG !'##cross-references GB:K02062; NID:g202899; PIDN:AAA40735.1; !1PID:g202900 REFERENCE A93331 !$#authors Yamanaka, M.; Greenberg, B.; Johnson, L.; Seilhamer, J.; !1Brewer, M.; Friedemann, T.; Miller, J.; Atlas, S.; Laragh, !1J.; Lewicki, J.; Fiddes, J. !$#journal Nature (1984) 309:719-722 !$#title Cloning and sequence analysis of the cDNA for the rat atrial !1natriuretic factor precursor. !$#cross-references MUID:84219797; PMID:6547210 !$#accession A01425 !'##molecule_type mRNA !'##residues 1-152 ##label YAM !'##cross-references EMBL:X00665; NID:g55711; PIDN:CAA25285.1; !1PID:g55712 REFERENCE A93332 !$#authors Maki, M.; Takayanagi, R.; Misono, K.S.; Pandey, K.N.; !1Tibbetts, C.; Inagami, T. !$#journal Nature (1984) 309:722-724 !$#title Structure of rat atrial natriuretic factor precursor deduced !1from cDNA sequence. !$#cross-references MUID:84219798; PMID:6328328 !$#accession A93332 !'##molecule_type mRNA !'##residues 1-152 ##label MAK !'##cross-references GB:X00665; EMBL:X00658; NID:g55711; !1PIDN:CAA25285.1; PID:g55712 REFERENCE A43617 !$#authors Seidman, C.E.; Duby, A.D.; Choi, E.; Graham, R.M.; Haber, !1E.; Homcy, C.; Smith, J.A.; Seidman, J.G. !$#journal Science (1984) 225:324-326 !$#title The structure of rat preproatrial natriuretic factor as !1defined by a complementary DNA clone. !$#cross-references MUID:84250178; PMID:6234658 !$#accession A43617 !'##molecule_type mRNA !'##residues 1-152 ##label SEI !'##cross-references GB:K02062; GB:K02063; NID:g202899; PIDN:AAA40735.1; !1PID:g202900 REFERENCE A93330 !$#authors Atlas, S.A.; Kleinert, H.D.; Camargo, M.J.; Januszewicz, A.; !1Sealey, J.E.; Laragh, J.H.; Schilling, J.W.; Lewicki, J.A.; !1Johnson, L.K.; Maack, T. !$#journal Nature (1984) 309:717-719 !$#title Purification, sequencing and synthesis of natriuretic and !1vasoactive rat atrial peptide. !$#cross-references MUID:84219796; PMID:6233494 !$#accession A93330 !'##molecule_type protein !'##residues 126-149 ##label ATL REFERENCE A94275 !$#authors Currie, M.G.; Geller, D.M.; Cole, B.R.; Siegel, N.R.; Fok, !1K.F.; Adams, S.P.; Eubanks, S.R.; Galluppi, G.R.; Needleman, !1P. !$#journal Science (1984) 223:67-69 !$#title Purification and sequence analysis of bioactive atrial !1peptides (atriopeptins). !$#cross-references MUID:84097513; PMID:6419347 !$#accession A94275 !'##molecule_type protein !'##residues 127-149 ##label CUR REFERENCE PT0061 !$#authors Thibault, G.; Murthy, K.K.; Gutkowska, J.; Seidah, N.G.; !1Lazure, C.; Chretien, M.; Cantin, M. !$#journal Peptides (1988) 9:47-53 !$#title NH2-terminal fragment of rat pro-atrial natriuretic factor !1in the circulation: identification, radioimmunoassay and !1half-life. !$#cross-references MUID:88203350; PMID:2966345 !$#accession PT0061 !'##molecule_type protein !'##residues 25-28,'X',30-31,'X',33,'X',35-38 ##label THI REFERENCE A20973 !$#authors Seidah, N.G.; Lazure, C.; Chretien, M.; Thibault, G.; !1Garcia, R.; Cantin, M.; Genest, J.; Nutt, R.F.; Brady, S.F.; !1Lyle, T.A.; Paleveda, W.J.; Colton, C.D.; Ciccarone, T.M.; !1Veber, D.F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:2640-2644 !$#title Amino acid sequence of homologous rat atrial peptides: !1natriuretic activity of native and synthetic forms. !$#cross-references MUID:84194062; PMID:6232612 !$#accession A20973 !'##molecule_type protein !'##residues 118-150 ##label SE2 REFERENCE A44190 !$#authors Flynn, T.G.; Davies, P.L.; Kennedy, B.P.; de Bold, M.L.; de !1Bold, A.J. !$#journal Science (1985) 228:323-325 !$#title Alignment of rat cardionatrin sequences with the !1preprocardionatrin sequence from complementary DNA. !$#cross-references MUID:85168263; PMID:3157217 !$#accession A44190 !'##molecule_type mRNA !'##residues 1-152 ##label FLY !'##cross-references GB:K02062; NID:g202899; PIDN:AAA40735.1; !1PID:g202900 !'##note part of this sequence, including the amino ends of three mature !1peptides, was confirmed by protein sequencing REFERENCE A60390 !$#authors Belcourt, D.; Varma, D.R.; Toney, K.; Bennett, H.P.J. !$#journal Protein Expr. Purif. (1990) 1:28-32 !$#title Purification of rat pro-atrial natriuretic factor: a !1simplified scheme using reversed-phase high-performance !1liquid chromatography. !$#cross-references MUID:93044510; PMID:2152180 !$#accession A60390 !'##molecule_type protein !'##residues 25-39 ##label BEL REFERENCE I59094 !$#authors Gardner, D.G.; Vlasuk, G.P.; Baxter, J.D.; Fiddes, J.C.; !1Lewicki, J.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:2175-2179 !$#title Identification of atrial natriuretic factor gene transcripts !1in the central nervous system of the rat. !$#cross-references MUID:87175636; PMID:2951736 !$#accession I59094 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 38-152 ##label RES !'##cross-references GB:M15868; NID:g202903; PIDN:AAA40736.1; !1PID:g202904 REFERENCE I58057 !$#authors Kangawa, K.; Tawaragi, Y.; Oikawa, S.; Mizuno, A.; !1Sakuragawa, Y.; Nakazato, H.; Fukuda, A.; Minamino, N.; !1Matsuo, H. !$#journal Nature (1984) 312:152-155 !$#title Identification of rat gamma atrial natriuretic polypeptide !1and characterization of the cDNA encoding its precursor. !$#cross-references MUID:85061500; PMID:6239103 !$#accession I58057 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-152 ##label RE2 !'##cross-references EMBL:X01118; NID:g55716; PIDN:CAA25586.1; !1PID:g55717 REFERENCE I52678 !$#authors Flynn, T.G. !$#journal Can. J. Physiol. Pharmacol. (1987) 65:2013-2020 !$#title the elucidation of the structure of atrial natriuretic !1factor, a new peptide hormone. !$#cross-references MUID:88109092; PMID:2962707 !$#accession I52678 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-51,'X',53-85,'X',87-152 ##label RE3 !'##cross-references GB:M27498; NID:g202905; PIDN:AAA40737.1; !1PID:g202906 COMMENT A disulfide bond is required for full activity of !1atriopeptins. COMMENT Several active peptides may be derived from the carboxyl !1region of this precursor. GENETICS !$#gene ANF !$#introns 40/3; 149/3 CLASSIFICATION #superfamily natriuretic peptide A precursor KEYWORDS atrium; diuretic; hormone; natriuretic; osmoregulation FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-152 #product pro-atrial natriuretic factor #status !8experimental #label PRO\ !$25-150 #product cardionatrin IV #status experimental #label !8CN4\ !$73-150 #product cardionatrin III #status experimental #label !8CN3\ !$118-150 #product ANF(1-33) #status experimental #label ANF1\ !$119-150 #product ANF(2-33) #status experimental #label ANF2\ !$120-150 #product ANF(3-33) #status experimental #label ANF3\ !$123-150 #product cardionatrin I #status experimental #label !8CN1\ !$125-150 #product ANF(8-33) #status experimental #label ANF4\ !$126-150 #product auriculin B #status experimental #label AUB\ !$126-149 #product auriculin A #status experimental #label AUA\ !$127-150 #product atrial natriuretic factor #status predicted !8#label MAT\ !$127-149 #product atriopeptin I #status experimental #label !8AT1\ !$127-147 #product atriopeptin II #status experimental #label !8AT2\ !$129-145 #disulfide_bonds #status experimental SUMMARY #length 152 #molecular-weight 16556 #checksum 7818 SEQUENCE /// ENTRY AWMS #type complete TITLE atrial natriuretic peptide precursor - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 18-Jun-1999 ACCESSIONS A29370; B43619 REFERENCE A29370 !$#authors Seidman, C.E.; Bloch, K.D.; Klein, K.A.; Smith, J.A.; !1Seidman, J.G. !$#journal Science (1984) 226:1206-1209 !$#title Nucleotide sequences of the human and mouse atrial !1natriuretic factor genes. !$#cross-references MUID:85065766; PMID:6542248 !$#accession A29370 !'##molecule_type DNA !'##residues 1-152 ##label SEI !'##cross-references GB:K02781; NID:g191937; PIDN:AAA37235.1; !1PID:g387099 GENETICS !$#introns 40/3; 149/3 CLASSIFICATION #superfamily natriuretic peptide A precursor KEYWORDS atrium; diuretic; hormone; natriuretic; osmoregulation FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-150 #product gamma atrial natriuretic factor #status !8predicted #label ANF\ !$123-150 #product alpha atrial natriuretic peptide #status !8predicted #label ANP\ !$129-145 #disulfide_bonds #status predicted SUMMARY #length 152 #molecular-weight 16645 #checksum 9384 SEQUENCE /// ENTRY AWHUB #type complete TITLE natriuretic peptide B precursor [validated] - human ALTERNATE_NAMES brain natriuretic factor-32 (BNF-32); brain natriuretic protein precursor CONTAINS brain alpha natriuretic peptide; brain gamma natriuretic factor ORGANISM #formal_name Homo sapiens #common_name man DATE 07-Sep-1990 #sequence_revision 02-Dec-1994 #text_change 08-Dec-2000 ACCESSIONS A36736; A30163; A34143; A34661; B34661 REFERENCE A36736 !$#authors Seilhamer, J.J.; Arfsten, A.; Miller, J.A.; Lundquist, P.; !1Scarborough, R.M.; Lewicki, J.A.; Porter, J.G. !$#journal Biochem. Biophys. Res. Commun. (1989) 165:650-658 !$#title Human and canine gene homologs of porcine brain natriuretic !1peptide. !$#cross-references MUID:90088474; PMID:2597152 !$#accession A36736 !'##molecule_type DNA !'##residues 1-134 ##label SEI !'##cross-references GB:M31776; NID:g179514; PIDN:AAA35603.1; !1PID:g179515 REFERENCE A30163 !$#authors Sudoh, T.; Maekawa, K.; Kojima, M.; Minamino, N.; Kangawa, !1K.; Matsuo, H. !$#journal Biochem. Biophys. Res. Commun. (1989) 159:1427-1434 !$#title Cloning and sequence analysis of cDNA encoding a precursor !1for human brain natriuretic peptide. !$#cross-references MUID:89193743; PMID:2522777 !$#accession A30163 !'##molecule_type mRNA !'##residues 1-134 ##label SUD !'##cross-references GB:M31776; NID:g179514; PIDN:AAA35603.1; !1PID:g179515 REFERENCE A34143 !$#authors Kambayashi, Y.; Nakao, K.; Mukoyama, M.; Saito, Y.; Ogawa, !1Y.; Shiono, S.; Inouye, K.; Yoshida, N.; Imura, H. !$#journal FEBS Lett. (1990) 259:341-345 !$#title Isolation and sequence determination of human brain !1natriuretic peptide in human atrium. !$#cross-references MUID:90092577; PMID:2136732 !$#accession A34143 !'##molecule_type protein !'##residues 103-134 ##label KAM REFERENCE A90161 !$#authors Hino, J.; Tateyama, H.; Minamino, N.; Kangawa, K.; Matsuo, !1H. !$#journal Biochem. Biophys. Res. Commun. (1990) 167:693-700 !$#title Isolation and identification of human brain natriuretic !1peptides in cardiac atrium. !$#cross-references MUID:90211249; PMID:2138890 !$#accession A34661 !'##molecule_type protein !'##residues 27-58 ##label HIN !$#accession B34661 !'##molecule_type protein !'##residues 103-134 ##label HI2 GENETICS !$#gene GDB:NPPB !'##cross-references GDB:127884; OMIM:600295 !$#map_position 1p36-1p36 !$#introns 44/3; 130/1 CLASSIFICATION #superfamily natriuretic peptide A precursor KEYWORDS brain; diuretic; hormone; natriuretic; osmoregulation FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-134 #product brain gamma natriuretic factor #status !8experimental #label GNF\ !$103-134 #product brain alpha natriuretic peptide #status !8experimental #label ANF\ !$112-128 #disulfide_bonds #status predicted SUMMARY #length 134 #molecular-weight 14726 #checksum 9481 SEQUENCE /// ENTRY A54119 #type complete TITLE c-type natriuretic peptide I precursor - bullfrog ALTERNATE_NAMES CNP I ORGANISM #formal_name Rana catesbeiana #common_name bullfrog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A54119 REFERENCE A54119 !$#authors Kojima, M.; Ohyama, Y.; Miyamoto, K.; Minamino, N.; Kangawa, !1K.; Matsuo, H. !$#journal J. Biol. Chem. (1994) 269:13136-13140 !$#title Cloning and characterization of a novel natriuretic peptide !1in frog (Rana catesbeiana). !$#cross-references MUID:94230409; PMID:8175740 !$#accession A54119 !'##status preliminary !'##molecule_type mRNA !'##residues 1-129 ##label KOJ !'##cross-references GB:D17413; NID:g397837; PIDN:BAA04235.1; !1PID:g397838 CLASSIFICATION #superfamily natriuretic peptide A precursor SUMMARY #length 129 #molecular-weight 14655 #checksum 3902 SEQUENCE /// ENTRY S15822 #type complete TITLE natriuretic peptide type C - smaller spotted catshark ORGANISM #formal_name Scyliorhinus canicula #common_name smaller spotted catshark, smaller spotted dogfish DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S15822 REFERENCE S15822 !$#authors Suzuki, R.; Takahashi, A.; Hazon, N.; Takei, Y. !$#journal FEBS Lett. (1991) 282:321-325 !$#title Isolation of high-molecular-weight C-type natriuretic !1peptide from the heart of a cartilaginous fish (European !1dogfish, Scyliorhinus canicula). !$#cross-references MUID:91243822; PMID:1828036 !$#accession S15822 !'##molecule_type protein !'##residues 1-115 ##label FEB CLASSIFICATION #superfamily natriuretic peptide A precursor SUMMARY #length 115 #molecular-weight 12885 #checksum 9179 SEQUENCE /// ENTRY A61244 #type complete TITLE natriuretic peptide type C precursor - spiny dogfish ORGANISM #formal_name Squalus acanthias #common_name spiny dogfish DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A61244; I51329 REFERENCE A61244 !$#authors Schofield, J.P.; Jones, D.S.C.; Forrest Jr., J.N. !$#journal Am. J. Physiol. (1991) 261:F734-F739 !$#title Identification of C-type natriuretic peptide in heart of !1spiny dogfish shark (Squalus acanthias). !$#cross-references MUID:92026459; PMID:1928383 !$#accession A61244 !'##molecule_type mRNA !'##residues 1-135 ##label SCH !'##cross-references EMBL:X59991; NID:g556803; PIDN:CAA42608.1; !1PID:g556804 GENETICS !$#introns 30/3 CLASSIFICATION #superfamily natriuretic peptide A precursor KEYWORDS disulfide bond; diuretic; hormone; natriuretic; !1osmoregulation FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$114-135 #product natriuretic peptide C #status predicted !8#label NPC\ !$119-135 #disulfide_bonds #status predicted SUMMARY #length 135 #molecular-weight 15062 #checksum 7540 SEQUENCE /// ENTRY A30162 #type complete TITLE brain natriuretic factor precursor - rat ALTERNATE_NAMES brain natriuretic peptide; cardiac natriuretic factor; iso-atrial natriuretic factor CONTAINS brain natriuretic factor BNP-45 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A30162; A35691; A54893; A32918; A32919; A33253; A60735; !1I57704; A33252 REFERENCE A30162 !$#authors Kojima, M.; Minamino, N.; Kangawa, K.; Matsuo, H. !$#journal Biochem. Biophys. Res. Commun. (1989) 159:1420-1426 !$#title Cloning and sequence analysis of cDNA encoding a precursor !1for rat brain natriuretic peptide. !$#cross-references MUID:89193742; PMID:2522776 !$#accession A30162 !'##molecule_type mRNA !'##residues 1-121 ##label KOJ !'##cross-references GB:M25297; NID:g602483; PIDN:AAA57269.1; !1PID:g602484 REFERENCE A35691 !$#authors Roy, R.N.; Flynn, T.G. !$#journal Biochem. Biophys. Res. Commun. (1990) 171:416-423 !$#title Organization of the gene for iso-rANP, a rat B-type !1natriuretic peptide. !$#cross-references MUID:90365739; PMID:2144113 !$#accession A35691 !'##molecule_type DNA !'##residues 1-14,'V',16-121 ##label ROY !'##cross-references GB:M60731; NID:g204985; PIDN:AAA41456.1; !1PID:g204986 !'##note the authors translated the codon GTT for residue 15 as Leu REFERENCE A54893 !$#authors Thuerauf, D.J.; Hanford, D.S.; Glembotski, C.C. !$#journal J. Biol. Chem. (1994) 269:17772-17775 !$#title Regulation of rat brain natriuretic peptide transcription. A !1potential role for GATA-related transcription factors in !1myocardial cell gene expression. !$#cross-references MUID:94299479; PMID:8027030 !$#accession A54893 !'##molecule_type DNA !'##residues 1-19 ##label THU !'##cross-references GB:U02972; NID:g458021; PIDN:AAA21648.1; !1PID:g458022 REFERENCE A32918 !$#authors Aburaya, M.; Hino, J.; Minamino, N.; Kangawa, K.; Matsuo, H. !$#journal Biochem. Biophys. Res. Commun. (1989) 163:226-232 !$#title Isolation and identification of rat brain natriuretic !1peptides in cardiac atrium. !$#cross-references MUID:89374230; PMID:2673236 !$#accession A32918 !'##molecule_type protein !'##residues 27-121 ##label ABU REFERENCE A32919 !$#authors Kambayashi, Y.; Nakao, K.; Itoh, H.; Hosoda, K.; Saito, Y.; !1Yamada, T.; Mukoyama, M.; Arai, H.; Shirakami, G.; Suga, S.; !1Ogawa, Y.; Jougasaki, M.; Minamino, N.; Kangawa, K.; Matsuo, !1H.; Inouye, K.; Imura, H. !$#journal Biochem. Biophys. Res. Commun. (1989) 163:233-240 !$#title Isolation and sequence determination of rat cardiac !1natriuretic peptide. !$#cross-references MUID:89374231; PMID:2528349 !$#accession A32919 !'##molecule_type protein !'##residues 77-121 ##label KAM REFERENCE A33253 !$#authors Flynn, T.G.; Brar, A.; Tremblay, L.; Sarda, I.; Lyons, C.; !1Jennings, D.B. !$#journal Biochem. Biophys. Res. Commun. (1989) 161:830-837 !$#title Isolation and characterization of iso-rANP, a new !1natriuretic peptide from rat atria. !$#cross-references MUID:89286593; PMID:2525380 !$#accession A33253 !'##molecule_type protein !'##residues 77-119,'Q',121 ##label FLY REFERENCE A60735 !$#authors Nakao, K.; Itoh, H.; Kambayashi, Y.; Hosoda, K.; Saito, Y.; !1Yamada, T.; Mukoyama, M.; Arai, H.; Shirakami, G.; Suga, S.; !1Jougasaki, M.; Ogawa, Y.; Inouye, K.; Imura, H. !$#journal Hypertension (1990) 15:774-778 !$#title Rat brain natriuretic peptide. Isolation from rat heart and !1tissue distribution. !$#cross-references MUID:90277148; PMID:2351430 !$#accession A60735 !'##molecule_type protein !'##residues 77-121 ##label NAK REFERENCE I57704 !$#authors Dagnino, L.; Drouin, J.; Nemer, M. !$#journal Mol. Endocrinol. (1991) 5:1292-1300 !$#title Differential expression of natriuretic peptide genes in !1cardiac and extracardiac tissues. !$#cross-references MUID:92123224; PMID:1837590 !$#accession I57704 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-121 ##label RES !'##cross-references GB:M60266; NID:g204983; PIDN:AAA41455.1; !1PID:g204984 GENETICS !$#introns 42/3; 117/1 CLASSIFICATION #superfamily natriuretic peptide A precursor KEYWORDS cardiac muscle; heart FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-121 #product brain natriuretic factor #status !8experimental #label MAT1\ !$77-121 #product brain natriuretic factor BNP-45 #status !8experimental #label MAT2 SUMMARY #length 121 #molecular-weight 13656 #checksum 4170 SEQUENCE /// ENTRY S14320 #type complete TITLE alpha-atrial natriuretic peptide precursor - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S14320; A31509 REFERENCE S14320 !$#authors Akizuki, N.; Kangawa, K.; Minamino, N.; Matsuo, H. !$#journal FEBS Lett. (1991) 280:357-362 !$#title Cloning and sequence analysis of complementary DNA encoding !1a precursor for chicken natriuretic peptide. !$#cross-references MUID:91192169; PMID:1826483 !$#accession S14320 !'##status preliminary !'##molecule_type mRNA !'##residues 1-140 ##label AKI !'##cross-references GB:X57702; NID:g63648; PIDN:CAA40879.1; !1PID:g3805902 REFERENCE A31509 !$#authors Miyata, A.; Minamino, N.; Kangawa, K.; Matsuo, H. !$#journal Biochem. Biophys. Res. Commun. (1988) 155:1330-1337 !$#title Identification of a 29-amino acid natriuretic peptide in !1chicken heart. !$#cross-references MUID:89025805; PMID:2972278 !$#accession A31509 !'##molecule_type protein !'##residues 112-140 ##label MIY CLASSIFICATION #superfamily natriuretic peptide A precursor FEATURE !$118-134 #disulfide_bonds #status experimental SUMMARY #length 140 #molecular-weight 15714 #checksum 6924 SEQUENCE /// ENTRY AWHUC #type complete TITLE natriuretic peptide C precursor [validated] - human ALTERNATE_NAMES natriuretic factor C CONTAINS natriuretic peptide C-22; natriuretic peptide C-29; natriuretic peptide C-53 ORGANISM #formal_name Homo sapiens #common_name man DATE 17-Apr-1993 #sequence_revision 02-Dec-1994 #text_change 08-Dec-2000 ACCESSIONS JT0567; JC1361; I54400 REFERENCE JT0567 !$#authors Tawaragi, Y.; Fuchimura, K.; Tanaka, S.; Minamino, N.; !1Kangawa, K.; Matsuo, H. !$#journal Biochem. Biophys. Res. Commun. (1991) 175:645-651 !$#title Gene and precursor structures of human C-type natriuretic !1peptide. !$#cross-references MUID:91207363; PMID:2018508 !$#accession JT0567 !'##molecule_type DNA !'##residues 1-126 ##label TAW !'##cross-references GB:M64710; NID:g180676; PIDN:AAA35703.1; !1PID:g180677 REFERENCE JC1361 !$#authors Ishizaka, Y.; Kangawa, K.; Minamino, N.; Ishii, K.; Takano, !1S.; Eto, T.; Matsuo, H. !$#journal Biochem. Biophys. Res. Commun. (1992) 189:697-704 !$#title Isolation and identification of C-type natriuretic peptide !1in human monocytic cell line, THP-1. !$#cross-references MUID:93112033; PMID:1472040 !$#accession JC1361 !'##molecule_type protein !'##residues 98-109,'X',111-118 ##label ISH REFERENCE I54400 !$#authors Ogawa, Y.; Nakao, K.; Nakagawa, O.; Komatsu, Y.; Hosoda, K.; !1Suga, S.; Arai, H.; Nagata, K.; Yoshida, N.; Imura, H. !$#journal Hypertension (1992) 19:809-813 !$#title Human C-type natriuretic peptide, Characterization of the !1gene and peptide. !$#cross-references MUID:92275775; PMID:1339402 !$#accession I54400 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-126 ##label RES !'##cross-references GB:D90337; NID:g219542; PIDN:BAA14351.1; !1PID:g219543 GENETICS !$#gene GDB:NPPC !'##cross-references GDB:250346; OMIM:600296 !$#map_position 2pter-2qter !$#introns 30/3 CLASSIFICATION #superfamily natriuretic peptide C precursor KEYWORDS brain; diuretic; hormone; natriuretic; neuropeptide; !1osmoregulation FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$74-126 #product natriuretic peptide C-53 #status predicted !8#label C53\ !$98-126 #product natriuretic peptide C-29 #status !8experimental #label C29\ !$105-126 #product natriuretic peptide C-22 #status predicted !8#label C22\ !$110-126 #disulfide_bonds #status predicted SUMMARY #length 126 #molecular-weight 13246 #checksum 2405 SEQUENCE /// ENTRY A36155 #type complete TITLE natriuretic peptide C precursor - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A36155; A35423; A34642 REFERENCE A36155 !$#authors Tawaragi, Y.; Fuchimura, K.; Nakazato, H.; Tanaka, S.; !1Minamino, N.; Kangawa, K.; Matsuo, H. !$#journal Biochem. Biophys. Res. Commun. (1990) 172:627-632 !$#title Gene and precursor structure of porcine C-type natriuretic !1peptide. !$#cross-references MUID:91054475; PMID:2146957 !$#accession A36155 !'##status preliminary !'##molecule_type DNA !'##residues 1-126 ##label TAW !'##cross-references EMBL:M64758; NID:g309789; PIDN:AAA31018.1; !1PID:g309790 REFERENCE A35423 !$#authors Minamino, N.; Kangawa, K.; Matsuo, H. !$#journal Biochem. Biophys. Res. Commun. (1990) 170:973-979 !$#title N-terminally extended form of C-type natriuretic peptide !1(CNP-53) identified in porcine brain. !$#cross-references MUID:90343827; PMID:2383278 !$#accession A35423 !'##status preliminary !'##molecule_type protein !'##residues 74-126 ##label MIN REFERENCE A34642 !$#authors Sudoh, T.; Minamino, N.; Kangawa, K.; Matsuo, H. !$#journal Biochem. Biophys. Res. Commun. (1990) 168:863-870 !$#title C-type natriuretic peptide (CNP): a new member of !1natriuretic peptide family identified in porcine brain. !$#cross-references MUID:90241265; PMID:2139780 !$#accession A34642 !'##status preliminary !'##molecule_type protein !'##residues 105-126 ##label SUD CLASSIFICATION #superfamily natriuretic peptide C precursor KEYWORDS disulfide bond; diuretic; hormone; natriuretic; !1osmoregulation FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$74-126 #product natriuretic peptide C-53 #status !8experimental #label C53\ !$98-126 #product natriuretic peptide C-29 #status predicted !8#label C29\ !$105-126 #product natriuretic peptide C-22 #status !8experimental #label C22\ !$110-126 #disulfide_bonds #status predicted SUMMARY #length 126 #molecular-weight 13243 #checksum 4058 SEQUENCE /// ENTRY ECXAA #type complete TITLE antho-RFamide neuropeptide - sea anemone (Anthopleura elegantissima) ORGANISM #formal_name Anthopleura elegantissima DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 08-Dec-1995 ACCESSIONS A26666 REFERENCE A26666 !$#authors Grimmelikhuijzen, C.J.P.; Graff, D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:9817-9821 !$#title Isolation of Asp). !$#cross-references MUID:69004666; PMID:5680274 !$#contents alpha-D allele; composition !$#accession A90574 !'##molecule_type protein !'##residues 1-14,'D',16-141 ##label HUI CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15047 #checksum 9202 SEQUENCE /// ENTRY HAEKN #type complete TITLE hemoglobin alpha chain - European moose ORGANISM #formal_name Alces alces alces #common_name European moose, elk DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 03-Mar-2000 ACCESSIONS A02295 REFERENCE A91729 !$#authors Aschauer, H.; Wiesner, H.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1984) 365:1323-1330 !$#title Zur intrinsischen Sauerstoffaffinitaet: die Primaerstruktur !1eines weiteren Ruminantia-Haemoglobins: Methionin in betaNA2 !1eines Stirnwaffentraegers, des Nordland-Elches (Alces alces !1alces). !$#cross-references MUID:85078042; PMID:6510898 !$#accession A02295 !'##molecule_type protein !'##residues 1-141 ##label ASC CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15115 #checksum 256 SEQUENCE /// ENTRY HADE1V #type complete TITLE hemoglobin alpha chains - Virginia white-tailed deer (tentative sequence) ORGANISM #formal_name Odocoileus virginianus virginianus #common_name Virginia white-tailed deer DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 31-Mar-2000 ACCESSIONS A02296 REFERENCE A02296 !$#authors Harris, M.J.; Wilson, J.B.; Huisman, T.H.J. !$#journal Arch. Biochem. Biophys. (1972) 151:540-548 !$#title Structural studies of hemoglobin alpha chains from Virginia !1white-tailed deer. !$#cross-references MUID:72239057; PMID:5045934 !$#accession A02296 !'##molecule_type protein !'##residues 1-141 ##label HAR !'##note the compositions or partial sequences of all tryptic peptides !1from three allelic alpha-1 chains and a nonallelic alpha-2 !1chain were determined !'##note the sequences of the other two allelic alpha-1 chains differ !1from that shown in having either 5-Thr or 24-Phe; the !1sequence of the nonallelic alpha-2 chain differs from that !1shown in having 20-Lys and 24-Phe COMMENT The sequence shown is one allele of the alpha-1 chain. CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15125 #checksum 1624 SEQUENCE /// ENTRY HALL #type complete TITLE hemoglobin alpha chain - llama ORGANISM #formal_name Lama guanicoe glama #common_name llama DATE 30-Apr-1980 #sequence_revision 31-Dec-1991 #text_change 03-Mar-2000 ACCESSIONS A02297 REFERENCE A91672 !$#authors Braunitzer, G.; Schrank, B.; Stangl, A. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1977) 358:409-412 !$#title Die Sequenz der alpha-Ketten der Haemoglobine des Schweines !1und des Lamas (Aspekte zur Atmung im Hochland). !$#cross-references MUID:77163922; PMID:852824 !$#accession A02297 !'##molecule_type protein !'##residues 1-141 ##label BRA CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15104 #checksum 7858 SEQUENCE /// ENTRY HAGW #type complete TITLE hemoglobin alpha chain - guanaco ORGANISM #formal_name Lama guanicoe #common_name guanaco DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 03-Mar-2000 ACCESSIONS S10615 REFERENCE S10615 !$#authors Piccinini, M.; Kleinschmidt, T.; Juergens, K.D.; Braunitzer, !1G. !$#journal Biol. Chem. Hoppe-Seyler (1990) 371:641-648 !$#title Primary structure and oxygen-binding properties of the !1hemoglobin from guanaco (Lama guanacoe, Tylopoda). !$#cross-references MUID:91025635; PMID:2222863 !$#accession S10615 !'##molecule_type protein !'##residues 1-141 ##label PIC !'##note the source is designated as Lama guanacoe CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15126 #checksum 7890 SEQUENCE /// ENTRY HACMA #type complete TITLE hemoglobin alpha chain - Arabian camel ORGANISM #formal_name Camelus dromedarius #common_name Arabian camel DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Mar-2000 ACCESSIONS B91685 REFERENCE A91685 !$#authors Braunitzer, G.; Schrank, B.; Stangl, A.; Wiesner, H. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1979) 360:1941-1946 !$#title Hoehenatmung, Phosphat-Protein-Wechselwirkung: die Sequenz !1der Haemoglobine des Meerschweinchens und des Dromedars. !$#cross-references MUID:80114125; PMID:527943 !$#accession B91685 !'##molecule_type protein !'##residues 1-141 ##label BRA !'##note article in German with English abstract CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15172 #checksum 8303 SEQUENCE /// ENTRY HACMB #type complete TITLE hemoglobin alpha chain - Bactrian camel ORGANISM #formal_name Camelus bactrianus #common_name Bactrian camel DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Mar-2000 ACCESSIONS B92758 REFERENCE A92758 !$#authors Braunitzer, G.; Schrank, B.; Stangl, A.; Wiesner, H. !$#journal J. Chem. Soc. Pak. (1980) 2:1-7 !$#title Respiration at high altitudes, !1phosphate-protein-interaction: sequence of the hemoglobins !1of the hamster (Mesocricetus aureatus) and the camel !1(Camelus ferus, Camelidae). !$#accession B92758 !'##molecule_type protein !'##residues 1-141 ##label BRA !'##note the source is designated as Camelus ferus !'##note article in German with English abstract CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15172 #checksum 8303 SEQUENCE /// ENTRY HAGP #type complete TITLE hemoglobin alpha chain - guinea pig (tentative sequence) ORGANISM #formal_name Cavia porcellus #common_name guinea pig DATE 30-Apr-1980 #sequence_revision 30-Apr-1980 #text_change 31-Mar-2000 ACCESSIONS A02269 REFERENCE A91685 !$#authors Braunitzer, G.; Schrank, B.; Stangl, A.; Wiesner, H. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1979) 360:1941-1946 !$#title Hoehenatmung, Phosphat-Protein-Wechselwirkung: die Sequenz !1der Haemoglobine des Meerschweinchens und des Dromedars. !$#cross-references MUID:80114125; PMID:527943 !$#accession A02269 !'##molecule_type protein !'##residues 1-141 ##label BRA CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15229 #checksum 9595 SEQUENCE /// ENTRY HTHU #type complete TITLE hemoglobin theta-1 chain - human ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1988 #sequence_revision 12-Jul-1996 #text_change 03-Mar-2000 ACCESSIONS I52337; A29346 REFERENCE I52337 !$#authors Gonzalez-Redondo, J.M.; Han, I.S.; Gu, Y.C.; Huisman, T.H.J. !$#journal Biochem. Genet. (1988) 26:207-211 !$#title Nucleotide sequence of the human theta-1-globin gene. !$#cross-references MUID:88309052; PMID:3408475 !$#accession I52337 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-142 ##label RES !'##cross-references GB:M33022; NID:g183895; PIDN:AAA52640.1; !1PID:g386769 REFERENCE A29346 !$#authors Hsu, S.L.; Marks, J.; Shaw, J.P.; Tam, M.; Higgs, D.R.; !1Shen, C.C.; Shen, C.K.J. !$#journal Nature (1988) 331:94-96 !$#title Structure and expression of the human theta-1-globin gene. !$#cross-references MUID:88122547; PMID:3422341 !$#accession A29346 !'##molecule_type DNA !'##residues 2-142 ##label HSU !'##cross-references GB:X06482; NID:g31775; PIDN:CAA29776.1; PID:g31776 !'##note initiator Met not shown COMMENT It has not been established whether this alpha-type !1hemoglobin is transcribed or functional. GENETICS !$#gene GDB:HBQ1 !'##cross-references GDB:120036; OMIM:142240 !$#map_position 16p13.3-16p13.3 !$#introns 33/2; 101/3 FUNCTION !$#description in erythrocytes binds and transports molecular oxygen from !1placenta to tissues CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; embryo; erythrocyte; heme; !1heterotetramer; iron; metalloprotein; oxygen carrier FEATURE !$3-142 #domain globin homology #label GLB\ !$59 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$88 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 142 #molecular-weight 15508 #checksum 4591 SEQUENCE /// ENTRY HTOR #type complete TITLE hemoglobin theta-1 chain - orangutan ORGANISM #formal_name Pongo pygmaeus #common_name orangutan DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 03-Mar-2000 ACCESSIONS A26397 REFERENCE A26397 !$#authors Marks, J.; Shaw, J.P.; Shen, C.K.J. !$#journal Nature (1986) 321:785-788 !$#title Sequence organization and genomic complexity of primate !1theta1 globin gene, a novel alpha-globin-like gene. !$#cross-references MUID:86230953; PMID:3012370 !$#accession A26397 !'##molecule_type DNA !'##residues 1-141 ##label MAR !'##cross-references GB:X03950; NID:g38150; PIDN:CAA27579.1; PID:g38151 GENETICS !$#introns 31/2; 99/3 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15348 #checksum 1597 SEQUENCE /// ENTRY HAKGG #type complete TITLE hemoglobin alpha chain - eastern gray kangaroo ORGANISM #formal_name Macropus giganteus #common_name eastern gray kangaroo DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 03-Mar-2000 ACCESSIONS A02298 REFERENCE A02298 !$#authors Beard, J.M.; Thompson, E.O.P. !$#journal Aust. J. Biol. Sci. (1971) 24:765-786 !$#title Studies on marsupial proteins. V. Amino acid sequence of the !1alpha-chain of haemoglobin from the grey kangaroo, Macropus !1giganteus. !$#cross-references MUID:72041397; PMID:5119242 !$#accession A02298 !'##molecule_type protein !'##residues 1-141 ##label BEA CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15219 #checksum 7692 SEQUENCE /// ENTRY HAOPV #type complete TITLE hemoglobin alpha chain - North American opossum ORGANISM #formal_name Didelphis virginiana, Didelphis marsupialis virginiana #common_name North American opossum DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 03-Mar-2000 ACCESSIONS A02299 REFERENCE A02299 !$#authors Stenzel, P. !$#journal Nature (1974) 252:62-63 !$#title Opossum Hb chain sequence and neutral mutation theory. !$#cross-references MUID:75045345; PMID:4427683 !$#accession A02299 !'##molecule_type protein !'##residues 1-141 ##label STE COMMENT The opossum hemoglobin alpha chain is exceptional in !1appearing to have glutamine rather than histidine as the !1distal axial ligand binding oxygen. CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (Gln) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15257 #checksum 1053 SEQUENCE /// ENTRY HATG #type complete TITLE hemoglobin alpha-1 chains - Australian echidna (tentative sequence) ORGANISM #formal_name Tachyglossus aculeatus #common_name Australian echidna DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 31-Mar-2000 ACCESSIONS A90089; A90090; A02300 REFERENCE A90089 !$#authors Whittaker, R.G.; Fisher, W.K.; Thompson, E.O.P. !$#journal Aust. J. Biol. Sci. (1973) 26:877-888 !$#title Studies on monotreme proteins. II. Amino acid sequence of !1the alpha-chain in haemoglobin from the echidna, !1Tachyglossus aculeatus aculeatus. !$#cross-references MUID:74021288; PMID:4748330 !$#contents T. a. aculeatus, sequence of B variant !$#accession A90089 !'##molecule_type protein !'##residues 1-141 ##label WHI REFERENCE A90090 !$#authors Dodgson, S.J.; Fisher, W.K.; Thompson, E.O.P. !$#journal Aust. J. Biol. Sci. (1974) 27:111-115 !$#title Studies on monotreme proteins. IV. Amino acid sequence of !1haemoglobin-IA of the echidna; a comparison of major !1haemoglobins from two geographical groups of echidnas. !$#cross-references MUID:75015353; PMID:4415942 !$#contents T. a. aculeatus, sequence of A variant !$#accession A90090 !'##molecule_type protein !'##residues 1-11,'G',13-77,'N',79-101,'S',103-114,'E',116-141 ##label !1DOD COMMENT The alpha-1 B variant sequence is shown. COMMENT Echidnas have a major hemoglobin I (with alpha-1 chain !1variants A, B, and C) and a minor hemoglobin II (with !1alpha-2 chain variants A and B). All hemoglobins may have !1the same beta chain. The sequences of both alpha-1 A and B !1variants differ from that of the alpha-2 A variant at nine !1positions. CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15461 #checksum 8759 SEQUENCE /// ENTRY HATG2 #type complete TITLE hemoglobin alpha-2 chain - Australian echidna (tentative sequence) ORGANISM #formal_name Tachyglossus aculeatus #common_name Australian echidna DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 31-Mar-2000 ACCESSIONS A02301 REFERENCE A90088 !$#authors Thompson, E.O.P.; Fisher, W.K.; Whittaker, R.G. !$#journal Aust. J. Biol. Sci. (1973) 26:1327-1335 !$#title Studies on monotreme protein. III. Amino acid sequence of !1the alpha- and beta-globin chains of the minor haemoglobin !1from the echidna, Tachyglossus aculeatus aculeatus. !$#cross-references MUID:74097602; PMID:4798231 !$#contents T. a. aculeatus !$#accession A02301 !'##molecule_type protein !'##residues 1-141 ##label THO COMMENT This alpha chain is the A variant from the minor hemoglobin !1II. Its sequence differs from those of the alpha-1 chain !1variants A and B at nine positions each. CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15585 #checksum 8763 SEQUENCE /// ENTRY HAOR #type complete TITLE hemoglobin alpha chain - duckbill platypus (tentative sequence) ORGANISM #formal_name Ornithorhynchus anatinus #common_name duckbill platypus DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 31-Mar-2000 ACCESSIONS A02302 REFERENCE A02302 !$#authors Whittaker, R.G.; Thompson, E.O.P. !$#journal Aust. J. Biol. Sci. (1974) 27:591-605 !$#title Studies on monotreme proteins. V. Amino acid sequence of the !1alpha-chain of haemoglobin from the platypus, !1Ornithorhynchus anatinus. !$#cross-references MUID:75224271; PMID:4464824 !$#accession A02302 !'##molecule_type protein !'##residues 1-141 ##label WHI CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15334 #checksum 6232 SEQUENCE /// ENTRY HAOS #type complete TITLE hemoglobin alpha-A chain - ostrich ORGANISM #formal_name Struthio camelus #common_name ostrich DATE 01-Sep-1981 #sequence_revision 20-Sep-1984 #text_change 19-May-2000 ACCESSIONS A91712; A91693; A02304 REFERENCE A91712 !$#authors Oberthur, W.; Braunitzer, G.; Baumann, R.; Wright, P.G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1983) 364:119-134 !$#title Die Primaerstruktur der alpha- und beta-Ketten der !1Hauptkomponenten der Haemoglobine des Straubes (Struthio !1camelus) und des Nandus (Rhea americana) (Struthioformes). !$#cross-references MUID:83184081; PMID:6840701 !$#contents major chain !$#accession A91712 !'##molecule_type protein !'##residues 1-141 ##label OBE !'##note tryptic peptides and the prolyl peptide (residues 95-141) were !1sequenced and ordered by homology REFERENCE A91693 !$#authors Oberthur, W.; Voelter, W.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1980) 361:969-975 !$#title Die Sequenz der Haemoglobine von Streifengans (Anser !1indicus) und Strauss (Struthio camelus). Inositpentaphosphat !1als Modulator Der Evolutionsgeschwindigkeit: die !1ueberraschende Sequenz alpha-63 (E12) Valin. !$#cross-references MUID:80247760; PMID:7399417 !$#contents alpha-A chain !$#accession A91693 !'##molecule_type protein !'##residues 1-108,'A',110-141 ##label OB2 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15446 #checksum 8504 SEQUENCE /// ENTRY HAPN #type complete TITLE hemoglobin alpha-A chain - emperor penguin ORGANISM #formal_name Aptenodytes forsteri #common_name emperor penguin DATE 28-Feb-1986 #sequence_revision 12-Sep-1997 #text_change 19-May-2000 ACCESSIONS S46402; A94411; A91400; A02303 REFERENCE S46402 !$#authors Tamburrini, M.; Condo, S.G.; di Prisco, G.; Giardina, B. !$#journal J. Mol. Biol. (1994) 237:615-621 !$#title Adaptation to extreme environments: structure-function !1relationships in Emperor penguin haemoglobin. !$#cross-references MUID:94210485; PMID:8158641 !$#accession S46402 !'##status preliminary !'##molecule_type protein !'##residues 1-141 ##label TAM REFERENCE A94411 !$#authors Schnek, A.G.; Paul, C.; Vandecasserie, C. !$#book Chemical Zoology, vol.10, Brush, A.H., ed., pp.359-381, !1Academic Press, New York, San Francisco, and London, 1978 !$#accession A94411 !'##molecule_type protein !'##residues 1-4,'D',6-16,'LHT',20-21,'CG',24-27,'P',29-33,'Z',35-37, !1'T',39-48,'S',50-53,'Z',55-63,'BZIGK',69,'IAZLBB',76-84,'B', !186-88,'Z',90-93,'B',95-96,'B',98-101,'SHGLZ',107,'AB',110, !1'KBLVRZF',118-119,'GVT',123-125,'B',127,'IHKS',132,'SAAHQA', !1139-141 ##label SCH REFERENCE A91400 !$#authors Monier, C.; Schnek, A.G.; Dirkx, J.; Leonis, J. !$#journal FEBS Lett. (1973) 36:93-95 !$#title Penguin hemoglobin (Aptenodytes forsteri). A 45 residue !1N-terminal sequence. !$#cross-references MUID:74015990; PMID:4747605 !$#accession A91400 !'##molecule_type protein !'##residues 1-4,'D',6-16,'LHT',20-21,'C',23-27,'P',29-33,'Z',35-37,'T', !139-45 ##label MON CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15468 #checksum 9217 SEQUENCE /// ENTRY HAPNR #type complete TITLE hemoglobin alpha-A chain - rock-hopper penguin ORGANISM #formal_name Eudyptes crestatus #common_name rock-hopper penguin DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 19-May-2000 ACCESSIONS S00822 REFERENCE S00822 !$#authors Huber, K.; Braunitzer, G.; Schneeganss, D.; Koesters, J.; !1Grimm, F. !$#journal Biol. Chem. Hoppe-Seyler (1988) 369:513-519 !$#title The primary structure of the hemoglobin of the rock-hopper !1penguin (Eudyptes crestatus, Sphenisciformes). !$#cross-references MUID:89076486; PMID:3202958 !$#accession S00822 !'##molecule_type protein !'##residues 1-141 ##label HUB CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15471 #checksum 9373 SEQUENCE /// ENTRY HAEH #type complete TITLE hemoglobin alpha-A chain - greater rhea ORGANISM #formal_name Rhea americana #common_name greater rhea, common rhea DATE 20-Sep-1984 #sequence_revision 20-Sep-1984 #text_change 03-Mar-2000 ACCESSIONS A02305 REFERENCE A91712 !$#authors Oberthur, W.; Braunitzer, G.; Baumann, R.; Wright, P.G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1983) 364:119-134 !$#title Die Primaerstruktur der alpha- und beta-Ketten der !1Hauptkomponenten der Haemoglobine des Straubes (Struthio !1camelus) und des Nandus (Rhea americana) (Struthioformes). !$#cross-references MUID:83184081; PMID:6840701 !$#accession A02305 !'##molecule_type protein !'##residues 1-141 ##label OBE !'##note tryptic peptides and the prolyl peptide (residues 95-141) were !1sequenced and ordered by homology CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15409 #checksum 9475 SEQUENCE /// ENTRY HAKOAW #type complete TITLE hemoglobin alpha-A chain - white stork ORGANISM #formal_name Ciconia ciconia #common_name white stork DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 03-Mar-2000 ACCESSIONS A02306 REFERENCE A91728 !$#authors Godovac-Zimmermann, J.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1984) 365:1107-1113 !$#title Hemoglobin of the adult white stork (Ciconia ciconia, !1Ciconiiformes). The primary structure of alpha (A)- and !1beta-chains from the only present hemoglobin component. !$#cross-references MUID:85053022; PMID:6500517 !$#accession A02306 !'##molecule_type protein !'##residues 1-141 ##label GOD CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15467 #checksum 9798 SEQUENCE /// ENTRY HAGDA #type complete TITLE hemoglobin alpha-A chain - American flamingo ORGANISM #formal_name Phoenicopterus ruber #common_name American flamingo DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 03-Mar-2000 ACCESSIONS A02307 REFERENCE A91733 !$#authors Godovac-Zimmermann, J.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1984) 365:437-443 !$#title The amino-acid sequence of alpha(A)- and beta-chains from !1the major hemoglobin component of American flamingo !1(Phoenicopterus ruber ruber). !$#cross-references MUID:84238000; PMID:6735355 !$#accession A02307 !'##molecule_type protein !'##residues 1-141 ##label GOD CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15368 #checksum 8168 SEQUENCE /// ENTRY HAGSM #type complete TITLE hemoglobin alpha-A chain - magpie goose ORGANISM #formal_name Anseranas semipalmata #common_name magpie goose DATE 20-Sep-1984 #sequence_revision 20-Sep-1984 #text_change 03-Mar-2000 ACCESSIONS A02308 REFERENCE A91720 !$#authors Oberthur, W.; Wiesner, H.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1983) 364:51-59 !$#title Die Primaerstruktur der alpha- und beta-Ketten der !1Hauptkomponente der Haemoglobine der Spaltfussgans !1(Anseranas semipalmata, Anatidae). !$#cross-references MUID:83184073; PMID:6840695 !$#accession A02308 !'##molecule_type protein !'##residues 1-141 ##label OBE !'##note tryptic peptides and the prolyl peptide (residues 95-141) were !1sequenced and ordered by homology CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15335 #checksum 7284 SEQUENCE /// ENTRY HADK #type complete TITLE hemoglobin alpha-A chain - duck ORGANISM #formal_name Anas platyrhynchos #common_name domestic duck DATE 18-Aug-1982 #sequence_revision 31-Dec-1991 #text_change 16-Jun-2000 ACCESSIONS A02309 REFERENCE A91111 !$#authors Paddock, G.V.; Gaubatz, J. !$#journal Eur. J. Biochem. (1981) 117:269-273 !$#title Nucleotide seuence for a novel duck alpha-globin gene. !$#cross-references MUID:82004164; PMID:6895064 !$#accession A02309 !'##molecule_type mRNA !'##residues 1-142 ##label PAD !'##cross-references GB:X02008; NID:g62457; PIDN:CAA26039.1; !1PID:g1334620 !'##experimental_source Pekin breed !'##note the authors translated the codon ACC for residue 9 as Ala GENETICS !$#introns 32/2; 100/3 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$2-142 #product hemoglobin alpha-A chain #status predicted !8#label MAT\ !$3-142 #domain globin homology #label GLB\ !$59 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$88 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 142 #molecular-weight 15365 #checksum 9577 SEQUENCE /// ENTRY HADKAM #type complete TITLE hemoglobin alpha-A chain - common mallard ORGANISM #formal_name Anas platyrhynchos platyrhynchos #common_name common mallard DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Mar-2000 ACCESSIONS A91721 REFERENCE A91721 !$#authors Godovac-Zimmermann, J.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1983) 364:665-674 !$#title The amino-acid sequence of northern mallard (Anas !1platyrhynchos platyrhynchos) hemoglobin. !$#cross-references MUID:83289128; PMID:6884992 !$#accession A91721 !'##molecule_type protein !'##residues 1-141 ##label GOD CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15248 #checksum 6988 SEQUENCE /// ENTRY HADKAW #type complete TITLE hemoglobin alpha-A chain - European wigeon ORGANISM #formal_name Anas penelope #common_name European wigeon DATE 03-Feb-1994 #sequence_revision 03-Feb-1994 #text_change 03-Mar-2000 ACCESSIONS JU0336 REFERENCE JU0336 !$#authors Abbasi, A.; Zaidi, Z.H. !$#submission submitted to JIPID, March 1991 !$#accession JU0336 !'##molecule_type protein !'##residues 1-141 ##label ABB CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15229 #checksum 6973 SEQUENCE /// ENTRY HADKAY #type complete TITLE hemoglobin alpha-A chain - muscovy duck ORGANISM #formal_name Cairina moschata #common_name muscovy duck DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Mar-2000 ACCESSIONS A91496 REFERENCE A91496 !$#authors Erbil, C.; Niessing, J. !$#journal Gene (1982) 20:211-217 !$#title The complete nucleotide sequence of the duck alpha(A)-globin !1gene. !$#cross-references MUID:83158759; PMID:7166233 !$#accession A91496 !'##molecule_type DNA !'##residues 1-142 ##label ERB !'##cross-references GB:J00923; GB:J00924; NID:g212911; PIDN:AAA49148.1; !1PID:g212914 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$2-142 #product hemoglobin alpha-A chain #status predicted !8#label MAT\ !$3-142 #domain globin homology #label GLB\ !$59 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$88 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 142 #molecular-weight 15420 #checksum 9256 SEQUENCE /// ENTRY HAGS #type complete TITLE hemoglobin alpha-A chain - western graylag goose ORGANISM #formal_name Anser anser anser #common_name western graylag goose DATE 31-Jan-1980 #sequence_revision 31-Jan-1980 #text_change 03-Mar-2000 ACCESSIONS A02310 REFERENCE A91694 !$#authors Oberthur, W.; Braunitzer, G.; Kalas, S. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1981) 362:1101-1112 !$#title Untersuchungen am Haemoglobin der Graugans (Anser anser). !1Die Primaerstruktur der alpha- und beta-Ketten der !1Hauptkomponente. !$#cross-references MUID:82263308; PMID:7346378 !$#accession A02310 !'##molecule_type protein !'##residues 1-141 ##label OBE CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15305 #checksum 7647 SEQUENCE /// ENTRY HAGSI #type complete TITLE hemoglobin alpha-A chain - bar-headed goose ORGANISM #formal_name Anser indicus #common_name bar-headed goose DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 03-Mar-2000 ACCESSIONS A02311 REFERENCE A91705 !$#authors Oberthur, W.; Braunitzer, G.; Wurdinger, I. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1982) 363:581-590 !$#title Das Haemoglobin der Streifengans (Anser indicus). !1Primaerstruktur und Physiologie der Atmung, Systematik und !1Evolution. !$#cross-references MUID:82263336; PMID:7106705 !$#accession A02311 !'##molecule_type protein !'##residues 1-141 ##label OBE CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15337 #checksum 7914 SEQUENCE /// ENTRY HAGSC #type complete TITLE hemoglobin alpha-A chain - Canada goose ORGANISM #formal_name Branta canadensis #common_name Canada goose DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 03-Mar-2000 ACCESSIONS A02312 REFERENCE A91709 !$#authors Oberthur, W.; Godovac-Zimmermann, J.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1982) 363:777-787 !$#title The amino acid sequence of Canada goose (Branta canadensis) !1and mute swan (Cygnus olor) hemoglobins. !$#cross-references MUID:83005405; PMID:7118073 !$#accession A02312 !'##molecule_type protein !'##residues 1-141 ##label OBE CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15289 #checksum 7693 SEQUENCE /// ENTRY HAWS #type complete TITLE hemoglobin alpha-A chain - mute swan ORGANISM #formal_name Cygnus olor #common_name mute swan DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 03-Mar-2000 ACCESSIONS A02313 REFERENCE A91709 !$#authors Oberthur, W.; Godovac-Zimmermann, J.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1982) 363:777-787 !$#title The amino acid sequence of Canada goose (Branta canadensis) !1and mute swan (Cygnus olor) hemoglobins. !$#cross-references MUID:83005405; PMID:7118073 !$#accession A02313 !'##molecule_type protein !'##residues 1-141 ##label OBE CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15258 #checksum 6848 SEQUENCE /// ENTRY HAGSAA #type complete TITLE hemoglobin alpha-A chain - Andean goose ORGANISM #formal_name Chloephaga melanoptera #common_name Andean goose DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS S00568 REFERENCE S00523 !$#authors Hiebl, I.; Braunitzer, G.; Schneeganss, D. !$#journal Biol. Chem. Hoppe-Seyler (1987) 368:1559-1569 !$#title High-altitude respiration of geese. The primary structures !1of the major and minor hemoglobin-components of adult Andean !1goose (Chloephaga melanoptera, Anatidae): the mutation !1Leu-Ser in position 55 of the beta-chains. !$#cross-references MUID:88163076; PMID:3442599 !$#accession S00568 !'##molecule_type protein !'##residues 1-141 ##label HIE CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15270 #checksum 6632 SEQUENCE /// ENTRY HASIA #type complete TITLE hemoglobin alpha-A chain - swift ORGANISM #formal_name Apus apus #common_name swift DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS S07479 REFERENCE S07479 !$#authors Nothum, R.; Weber, R.E.; Koesters, J.; Schneeganss, D.; !1Braunitzer, G. !$#journal Biol. Chem. Hoppe-Seyler (1989) 370:1197-1207 !$#title Amino-acid sequences and functional differentiation of !1hemoglobins A and D from swift (Apus apus, Apodiformes). !$#cross-references MUID:90121756; PMID:2610936 !$#accession S07479 !'##molecule_type protein !'##residues 1-141 ##label NOT CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 14886 #checksum 7315 SEQUENCE /// ENTRY HACOAG #type complete TITLE hemoglobin alpha-A chain - great cormorant ORGANISM #formal_name Phalacrocorax carbo #common_name great cormorant DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS S01804 REFERENCE S01804 !$#authors Huber, K.; Braunitzer, G.; Schneeganss, D.; Koesters, J.; !1Grimm, F. !$#journal Biol. Chem. Hoppe-Seyler (1988) 369:1251-1258 !$#title The primary structure of the hemoglobin of the cormorant !1(Phalacrocorax carbo, Pelecaniformes). !$#cross-references MUID:89228540; PMID:3245897 !$#accession S01804 !'##molecule_type protein !'##residues 1-141 ##label HUB CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15275 #checksum 6747 SEQUENCE /// ENTRY HAGLAB #type complete TITLE hemoglobin alpha-A chain - black-headed gull ORGANISM #formal_name Larus ridibundus #common_name black-headed gull DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 03-Mar-2000 ACCESSIONS S00814 REFERENCE S00814 !$#authors Godovac-Zimmermann, J.; Koesters, J.; Braunitzer, G.; !1Goeltenboth, R. !$#journal Biol. Chem. Hoppe-Seyler (1988) 369:341-348 !$#title Structural adaptation of bird hemoglobins to high-altitude !1respiration and the primary sequences of black-headed gull !1(Larus ridibundus, Charadriiformes) alpha(A)- and beta/ !1beta'-chains. !$#cross-references MUID:89000193; PMID:3166738 !$#accession S00814 !'##molecule_type protein !'##residues 1-141 ##label GOD CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15232 #checksum 8636 SEQUENCE /// ENTRY HAQC #type complete TITLE hemoglobin alpha-A chain - golden eagle ORGANISM #formal_name Aquila chrysaetos #common_name golden eagle DATE 20-Sep-1984 #sequence_revision 20-Sep-1984 #text_change 03-Mar-2000 ACCESSIONS A02314 REFERENCE A91724 !$#authors Oberthur, W.; Braunitzer, G.; Grimm, F.; Kosters, J. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1983) 364:851-858 !$#title Haemoglobine des steinadlers (Aquila chrysaetos, !1Accipitriformes): die Aminosaeure-Sequenz der alpha(A)- und !1beta-Ketten der Hauptkomponente. !$#cross-references MUID:84006435; PMID:6618445 !$#accession A02314 !'##molecule_type protein !'##residues 1-141 ##label OBE !'##note tryptic peptides and the prolyl peptide (residues 95-141) were !1sequenced and ordered by homology COMMENT This chain occurs in hemoglobin A, which is the major !1component (60%) of adult hemoglobin molecules. CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15457 #checksum 8366 SEQUENCE /// ENTRY HAGRAW #type complete TITLE hemoglobin alpha-A chain - white-headed vulture ORGANISM #formal_name Trigonoceps occipitalis #common_name white-headed vulture DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS S04949 REFERENCE S04948 !$#authors Hiebl, I.; Weber, R.E.; Schneeganss, D.; Braunitzer, G. !$#journal Biol. Chem. Hoppe-Seyler (1989) 370:699-706 !$#title High-altitude respiration of Falconiformes. The primary !1structures and functional properties of the major and minor !1hemoglobin components of the adult white-headed vulture !1(Trigonoceps occipitalis, Aegypiinae). !$#cross-references MUID:89374815; PMID:2775491 !$#accession S04949 !'##molecule_type protein !'##residues 1-141 ##label HIE CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15468 #checksum 8515 SEQUENCE /// ENTRY HAGRAR #type complete TITLE hemoglobin alpha-A chain - Rueppell's griffon ORGANISM #formal_name Gyps rueppellii #common_name Rueppell's griffon DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 03-Mar-2000 ACCESSIONS S00527 REFERENCE S00527 !$#authors Hiebl, I.; Weber, R.E.; Schneeganss, D.; Koesters, J.; !1Braunitzer, G. !$#journal Biol. Chem. Hoppe-Seyler (1988) 369:217-232 !$#title High-altitude respiration of birds. Structural adaptations !1in the major and minor hemoglobin components of adult !1Rueppell's griffon (Gyps rueppellii, Aegypiinae): a new !1molecular pattern for hypoxic tolerance. !$#cross-references MUID:88293711; PMID:3401327 !$#accession S00527 !'##molecule_type protein !'##residues 1-141 ##label HIE !'##note the sequence of the alpha-A' chain differs from that shown in !1having 34-Ile CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15483 #checksum 8840 SEQUENCE /// ENTRY HACH2 #type complete TITLE hemoglobin alpha-A chain - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 24-Apr-1984 #sequence_revision 12-Apr-1996 #text_change 03-Mar-2000 ACCESSIONS S18673; A93277; B93277; A92421; A93892; A92290; A91482; !1A93696; A91765; I50155; A02315 REFERENCE S18672 !$#authors Lewis, W.; Lee, J.D.; Dodgson, J.B. !$#journal Nucleic Acids Res. (1991) 19:5321-5329 !$#title Adult chicken alpha-globin gene expression in transfected !1QT6 quail cells: evidence for a negative regulatory element !1in the alpha-D gene region. !$#cross-references MUID:92020223; PMID:1656392 !$#accession S18673 !'##status translation not shown !'##molecule_type DNA !'##residues 1-142 ##label LEW !'##cross-references EMBL:X59989; NID:g63012; PIDN:CAA42606.1; !1PID:g63014 REFERENCE A93277 !$#authors Knochel, W.; Wittig, B.; Wittig, S.; John, M.E.; Grundmann, !1U.; Oberthur, W.; Godovac, J.; Braunitzer, G. !$#journal Nature (1982) 295:710-712 !$#title No evidence for 'stress' alpha-globin genes in chicken. !$#cross-references MUID:82125524; PMID:7057930 !$#accession A93277 !'##molecule_type protein !'##residues 2-142 ##label KNO !$#accession B93277 !'##molecule_type mRNA !'##residues 2-142 ##label KN2 !'##cross-references GB:J00852; NID:g211864; PIDN:AAA48799.1; !1PID:g211865 !'##experimental_source adult chicken; phenylhydrazine-stressed chicken !'##note the stress-induced alpha chain is shown to be identical with !1the major adult alpha chain, the sequence of which was !1redetermined and extensively revised REFERENCE A92421 !$#authors Dodgson, J.B.; Engel, J.D. !$#journal J. Biol. Chem. (1983) 258:4623-4629 !$#title The nucleotide sequence of the adult chicken alpha-globin !1genes. !$#cross-references MUID:83161047; PMID:6300093 !$#accession A92421 !'##molecule_type DNA !'##residues 2-142 ##label DOD !'##cross-references GB:J00854; NID:g211867; PIDN:AAA48801.1; !1PID:g211870 REFERENCE A93892 !$#authors Dodgson, J.B.; McCune, K.C.; Rusling, D.J.; Krust, A.; !1Engel, J.D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:5998-6002 !$#title Adult chicken alpha-globin genes, alpha(A) and alpha(D): no !1anemic shock alpha-globin exists in domestic chickens. !$#cross-references MUID:82082384; PMID:6273837 !$#accession A93892 !'##molecule_type DNA; mRNA !'##residues 2-142 ##label DO2 !'##experimental_source nonanemic chicken REFERENCE A92290 !$#authors Richards, R.I.; Wells, J.R.E. !$#journal J. Biol. Chem. (1980) 255:9306-9311 !$#title Chicken globin genes. Nucleotide sequence of cDNA clones !1coding for the alpha-globin expressed during hemolytic !1anemia. !$#cross-references MUID:81007015; PMID:6251083 !$#accession A92290 !'##molecule_type mRNA !'##residues 2-142 ##label RIC !'##cross-references GB:J00852; NID:g211864; PIDN:AAA48799.1; !1PID:g211865 !'##experimental_source phenylhydrazine-stressed chicken REFERENCE A91482 !$#authors Liu, A.Y.; Salser, W. !$#journal Gene (1981) 13:409-415 !$#title Complete nucleotide sequence of a chicken alpha-globin cDNA. !$#cross-references MUID:81261951; PMID:6894907 !$#accession A91482 !'##molecule_type mRNA !'##residues 2-110,'T',112-121,'I',123-142 ##label LIU !'##experimental_source phenylhydrazine-stressed chicken REFERENCE A93696 !$#authors Deacon, N.J.; Shine, J.; Naora, H. !$#journal Nucleic Acids Res. (1980) 8:1187-1199 !$#title Complete nucleotide sequence of a cloned chicken !1alpha-globin cDNA. !$#cross-references MUID:81053805; PMID:6253930 !$#accession A93696 !'##molecule_type mRNA !'##residues 2-92,'TGG',96-120,'K',122-142 ##label DEA !'##experimental_source phenylhydrazine-stressed chicken REFERENCE A91765 !$#authors Matsuda, G.; Takei, H.; Wu, K.C.; Shiozawa, T.; Ota, Y. !$#journal Int. J. Pept. Protein Res. (1972) 4:291-302 !$#title Sequence studies on the tryptic peptides and the !1chymotryptic peptides from the alpha polypeptide chain of !1aII component of the chicken hemoglobin. !$#cross-references MUID:73086012; PMID:4567660 !$#accession A91765 !'##molecule_type protein !'##residues 2-4,'N',6-34,'IGF',38,'T',40-63,'AL',66,'ITN',70,'IE',73, !1'A',75-77,'S',79,'A',81-109,'LVA',113,'L',115-116,'E',118, !1'A',120,'K',122-142 ##label MAT REFERENCE I50155 !$#authors Cummings, I.W.; Liu, A.Y.; Salser, W.A. !$#journal Nature (1978) 276:418-419 !$#title Identification of a new chicken alpha-globin structural gene !1by complementary DNA cloning. !$#cross-references MUID:79053299; PMID:714170 !$#accession I50155 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 61-84 ##label CUM !'##cross-references GB:M35068; NID:g211115; PIDN:AAA48583.1; !1PID:g211116 COMMENT This alpha chain is from the adult major tetrameric !1component, which has been called hemoglobin A or AII. GENETICS !$#gene alpha-A !$#introns 32/2; 100/3 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-142 #domain globin homology #label GLB\ !$59 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$88 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 142 #molecular-weight 15429 #checksum 978 SEQUENCE /// ENTRY HAFEA #type complete TITLE hemoglobin alpha-A chain - ring-necked pheasant ORGANISM #formal_name Phasianus colchicus #common_name ring-necked pheasant DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 03-Mar-2000 ACCESSIONS A02316 REFERENCE A91704 !$#authors Braunitzer, G.; Godovac, J. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1982) 363:229-238 !$#title The amino acid sequence of pheasant (Phasianus colchicus !1colchicus) hemoglobins. !$#cross-references MUID:82188254; PMID:7076123 !$#accession A02316 !'##molecule_type protein !'##residues 1-141 ##label BRA COMMENT This alpha chain is from the adult major tetrameric !1component, which has been called hemoglobin A or AII. GENETICS !$#gene alpha-A CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15344 #checksum 8790 SEQUENCE /// ENTRY HAQJAF #type complete TITLE hemoglobin alpha-A chain - gray francolin ORGANISM #formal_name Francolinus pondicerianus #common_name gray francolin DATE 03-Feb-1994 #sequence_revision 03-Feb-1994 #text_change 03-Mar-2000 ACCESSIONS JU0338; A37012 REFERENCE JU0336 !$#authors Abbasi, A.; Zaidi, Z.H. !$#submission submitted to JIPID, March 1991 !$#accession JU0338 !'##molecule_type protein !'##residues 1-141 ##label ABB REFERENCE A37012 !$#authors Abbasi, A.; Zaidi, Z.H. !$#journal J. Protein Chem. (1989) 8:647-652 !$#title Primary structure of hemoglobin from gray partridge !1(Francolinus pondacerianus, Galliformes). !$#cross-references MUID:90121574; PMID:2610858 !$#accession A37012 !'##molecule_type protein !'##residues 1-72,'H',73-141 ##label AB2 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15272 #checksum 9066 SEQUENCE /// ENTRY HADLA #type complete TITLE hemoglobin alpha-A chain - blue-and-yellow macaw ORGANISM #formal_name Ara ararauna #common_name blue-and-yellow macaw DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 03-Mar-2000 ACCESSIONS A02317 REFERENCE A90687 !$#authors Godovac-Zimmermann, J.; Braunitzer, G. !$#journal Biol. Chem. Hoppe-Seyler (1985) 366:503-508 !$#title The primary structure of alpha(A)- and beta-chains from !1blue-and-yellow macaw (Ara arauna, Psittaci) hemoglobin. !$#cross-references MUID:85225971; PMID:4005049 !$#accession A02317 !'##molecule_type protein !'##residues 1-141 ##label GOD CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15105 #checksum 9133 SEQUENCE /// ENTRY HAJSA #type complete TITLE hemoglobin alpha-A chain - common starling ORGANISM #formal_name Sturnus vulgaris #common_name common starling DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 03-Mar-2000 ACCESSIONS A02318 REFERENCE A91731 !$#authors Oberthur, W.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1984) 365:159-173 !$#title Hemoglobins of starling (Sturnus vulgaris, Passeriformes). !1The primary structures of alpha(A)-, alpha (D)- and !1beta-chains. !$#cross-references MUID:84184202; PMID:6714943 !$#accession A02318 !'##molecule_type protein !'##residues 1-141 ##label OBE CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15033 #checksum 9280 SEQUENCE /// ENTRY HAHTAB #type complete TITLE hemoglobin alpha-A chain - blackbird ORGANISM #formal_name Turdus merula #common_name blackbird DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS S04000 REFERENCE S04000 !$#authors Nothum, R.; Braunitzer, G.; Hiebl, I.; Koesters, J.; !1Schneeganss, D. !$#journal Biol. Chem. Hoppe-Seyler (1989) 370:309-316 !$#title The hemoglobins of the adult blackbird (Turdus merula, !1Passeriformes). The sequence of the major (HbA) and minor !1component (HbD). !$#cross-references MUID:89335259; PMID:2757791 !$#accession S04000 !'##molecule_type protein !'##residues 1-141 ##label NOT CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15047 #checksum 9422 SEQUENCE /// ENTRY HATJA #type complete TITLE hemoglobin alpha-A chain - tuatara ORGANISM #formal_name Sphenodon punctatus #common_name tuatara DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS S01136 REFERENCE S01136 !$#authors Abbasi, A.; Wells, R.M.G.; Brittain, T.; Braunitzer, G. !$#journal Biol. Chem. Hoppe-Seyler (1988) 369:755-764 !$#title Primary structure of the hemoglobins from sphenodon !1(Sphenodon punctatus, tuatara, Rynchocephalia). Evidence for !1the expression of alpha(D)-gene. !$#cross-references MUID:89105321; PMID:3214555 !$#accession S01136 !'##molecule_type protein !'##residues 1-141 ##label ABB CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15454 #checksum 436 SEQUENCE /// ENTRY HAIG1 #type complete TITLE hemoglobin alpha-I chain - common iguana ORGANISM #formal_name Iguana iguana #common_name common iguana DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS S01664 REFERENCE S01664 !$#authors Ruecknagel, K.P.; Braunitzer, G.; Wiesner, H. !$#journal Biol. Chem. Hoppe-Seyler (1988) 369:1143-1150 !$#title Hemoglobins of reptiles. The primary structures of the alpha !1(I)- and beta(I)-chains of common iguana (Iguana iguana) !1hemoglobin. !$#cross-references MUID:89207099; PMID:3242545 !$#accession S01664 !'##molecule_type protein !'##residues 1-141 ##label RUE CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15439 #checksum 4895 SEQUENCE /// ENTRY HALZC #type complete TITLE hemoglobin alpha-II chain - Cape monitor ORGANISM #formal_name Varanus exanthematicus albigularis #common_name Cape monitor DATE 31-Dec-1990 #sequence_revision 13-Feb-1998 #text_change 03-Mar-2000 ACCESSIONS S16196; S06093 REFERENCE S16196 !$#authors Abbasi, A.; Braunitzer, G. !$#journal Biol. Chem. Hoppe-Seyler (1991) 372:473-479 !$#title Primary structure of hemoglobin from monitor lizard (Varanus !1exanthematicus albigularis-Squamata). !$#cross-references MUID:92029675; PMID:1930730 !$#accession S16196 !'##molecule_type protein !'##residues 1-141 ##label ABB1 REFERENCE S06093 !$#authors Abbasi, A.; Braunitzer, G. !$#book Protein structure-function relationship, Zaidi, Z.H., ed., !1pp.1-13, Elsevier, Amsterdam, 1988 !$#title Hemoglobin - structure, physiology and evolution. !$#accession S06093 !'##molecule_type protein !'##residues 1-84,'D',86-141 ##label ABB2 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15785 #checksum 4693 SEQUENCE /// ENTRY HATTAP #type complete TITLE hemoglobin alpha-A chain - western painted turtle ORGANISM #formal_name Chrysemys picta bellii #common_name western painted turtle DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 03-Mar-2000 ACCESSIONS S00525 REFERENCE S00525 !$#authors Ruecknagel, K.P.; Braunitzer, G. !$#journal Biol. Chem. Hoppe-Seyler (1988) 369:123-131 !$#title Hemoglobins of reptiles. The primary structure of the major !1and minor hemoglobin component of adult Western painted !1turtle (Chrysemys picta bellii). !$#cross-references MUID:88209274; PMID:3365328 !$#accession S00525 !'##molecule_type protein !'##residues 1-141 ##label RUE CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15642 #checksum 2116 SEQUENCE /// ENTRY HAAK #type complete TITLE hemoglobin alpha chain - Nile crocodile ORGANISM #formal_name Crocodylus niloticus #common_name Nile crocodile DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 03-Mar-2000 ACCESSIONS A02319 REFERENCE A91695 !$#authors Leclercq, F.; Schnek, A.G.; Braunitzer, G.; Stangl, A.; !1Schrank, B. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1981) 362:1151-1158 !$#title Direct reciprocal allosteric interaction of oxygen and !1hydrogen carbonate sequence of the haemoglobins of the !1caiman (Caiman crocodylus), the Nile crocodile (Crocodylus !1niloticus) and the Mississippi crocodile (Alligator !1mississippiensis). !$#cross-references MUID:82263313; PMID:6286445 !$#accession A02319 !'##molecule_type protein !'##residues 1-141 ##label LEC CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15574 #checksum 8655 SEQUENCE /// ENTRY HAAQ #type complete TITLE hemoglobin alpha chain - American alligator ORGANISM #formal_name Alligator mississippiensis #common_name American alligator DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 03-Mar-2000 ACCESSIONS A02320 REFERENCE A91695 !$#authors Leclercq, F.; Schnek, A.G.; Braunitzer, G.; Stangl, A.; !1Schrank, B. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1981) 362:1151-1158 !$#title Direct reciprocal allosteric interaction of oxygen and !1hydrogen carbonate sequence of the haemoglobins of the !1caiman (Caiman crocodylus), the Nile crocodile (Crocodylus !1niloticus) and the Mississippi crocodile (Alligator !1mississippiensis). !$#cross-references MUID:82263313; PMID:6286445 !$#accession A02320 !'##molecule_type protein !'##residues 1-141 ##label LEC CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15734 #checksum 7188 SEQUENCE /// ENTRY HACQ #type complete TITLE hemoglobin alpha chain - spectacled caiman ORGANISM #formal_name Caiman crocodilus, Caiman sclerops #common_name spectacled caiman DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 03-Mar-2000 ACCESSIONS A02321 REFERENCE A91695 !$#authors Leclercq, F.; Schnek, A.G.; Braunitzer, G.; Stangl, A.; !1Schrank, B. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1981) 362:1151-1158 !$#title Direct reciprocal allosteric interaction of oxygen and !1hydrogen carbonate sequence of the haemoglobins of the !1caiman (Caiman crocodylus), the Nile crocodile (Crocodylus !1niloticus) and the Mississippi crocodile (Alligator !1mississippiensis). !$#cross-references MUID:82263313; PMID:6286445 !$#accession A02321 !'##molecule_type protein !'##residues 1-141 ##label LEC CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15767 #checksum 8393 SEQUENCE /// ENTRY HACH1 #type complete TITLE hemoglobin alpha-D chain - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 24-Apr-1984 #sequence_revision 20-Sep-1984 #text_change 03-Mar-2000 ACCESSIONS B92421; B93892; A91937; B92377; S18672; A02322 REFERENCE A92421 !$#authors Dodgson, J.B.; Engel, J.D. !$#journal J. Biol. Chem. (1983) 258:4623-4629 !$#title The nucleotide sequence of the adult chicken alpha-globin !1genes. !$#cross-references MUID:83161047; PMID:6300093 !$#accession B92421 !'##molecule_type DNA !'##residues 1-141 ##label DOD !'##cross-references GB:J00853; NID:g211866; PIDN:AAA48800.1; !1PID:g211869 !'##note the gene from which this sequence was translated is unusual in !1that the second intron begins with 'GC' rather than the !1usual 'GT' REFERENCE A93892 !$#authors Dodgson, J.B.; McCune, K.C.; Rusling, D.J.; Krust, A.; !1Engel, J.D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:5998-6002 !$#title Adult chicken alpha-globin genes, alpha(A) and alpha(D): no !1anemic shock alpha-globin exists in domestic chickens. !$#cross-references MUID:82082384; PMID:6273837 !$#accession B93892 !'##molecule_type mRNA !'##residues 1-106,'C',108,'RL',111-141 ##label DO2 REFERENCE A91937 !$#authors Takei, H.; Ota, Y.; Wu, K.C.; Kiyohara, T.; Matsuda, G. !$#journal J. Biochem. (1975) 77:1345-1347 !$#title Amino acid sequence of the alpha chain of chicken AI !1hemoglobin. !$#cross-references MUID:76189993; PMID:1225908 !$#accession A91937 !'##molecule_type protein !'##residues 1-21,'Q',23-37,'E',39-52,'NE',55-106,'Q',108-141 ##label !1TAK !'##note this alpha chain is from the adult minor tetrameric component, !1which has been called hemoglobin D or AI REFERENCE A92377 !$#authors Chapman, B.S.; Hood, L.E.; Tobin, A.J. !$#journal J. Biol. Chem. (1982) 257:651-658 !$#title Minor early embryonic chick hemoglobin M. Amino acid !1sequences of the epsilon and alpha(D) chains. !$#cross-references MUID:82098109; PMID:7054172 !$#accession B92377 !'##molecule_type protein !'##residues 1-63;94-106,'C',108-110,'A',112-122 ##label CHA !'##experimental_source embryo !'##note this chain was isolated from HbM, the least abundant of the !1four early chick hemoglobins REFERENCE S18672 !$#authors Lewis, W.; Lee, J.D.; Dodgson, J.B. !$#journal Nucleic Acids Res. (1991) 19:5321-5329 !$#title Adult chicken alpha-globin gene expression in transfected !1QT6 quail cells: evidence for a negative regulatory element !1in the alpha-D gene region. !$#cross-references MUID:92020223; PMID:1656392 !$#accession S18672 !'##status preliminary; translation not shown !'##molecule_type DNA !'##residues 1-15,'R',17-141 ##label LEW !'##cross-references EMBL:X59989; NID:g63012; PIDN:CAA42605.1; !1PID:g63013 GENETICS !$#gene alpha-D !$#introns 31/2; 99/3 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15695 #checksum 2235 SEQUENCE /// ENTRY HAFEDR #type complete TITLE hemoglobin alpha-D chain - ring-necked pheasant ORGANISM #formal_name Phasianus colchicus #common_name ring-necked pheasant DATE 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 03-Mar-2000 ACCESSIONS A02323 REFERENCE A91704 !$#authors Braunitzer, G.; Godovac, J. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1982) 363:229-238 !$#title The amino acid sequence of pheasant (Phasianus colchicus !1colchicus) hemoglobins. !$#cross-references MUID:82188254; PMID:7076123 !$#accession A02323 !'##molecule_type protein !'##residues 1-141 ##label BRA COMMENT The minor adult hemoglobin, HbD, contains alpha-D chains. CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15736 #checksum 1125 SEQUENCE /// ENTRY HADKDD #type complete TITLE hemoglobin alpha-D chain - duck ORGANISM #formal_name Anas platyrhynchos #common_name domestic duck DATE 17-Mar-1987 #sequence_revision 12-Apr-1996 #text_change 03-Mar-2000 ACCESSIONS S13971; A02324 REFERENCE S13971 !$#authors Frankis, R.C.; Paddock, G.V. !$#journal J. Mol. Appl. Genet. (1984) 2:381-391 !$#title Nucleotide sequences for the duck globin mRNAs. !$#cross-references MUID:84241515; PMID:6547470 !$#accession S13971 !'##status preliminary !'##molecule_type mRNA !'##residues 1-141 ##label FRA !'##cross-references EMBL:K01942; NID:g213094; PIDN:AAA49220.1; !1PID:g213095 REFERENCE A02324 !$#authors Ben Tahar, S.; Scherrer, K. !$#journal Mol. Biol. Rep. (1983) 9:101-113 !$#title Determination of the primary sequence of the duck alpha(D) !1globin mRNA and comparison of all adult duck and chick !1globin mRNA sequences. !$#cross-references MUID:83297271; PMID:6888376 !$#accession A02324 !'##molecule_type mRNA !'##residues 7-141 ##label BEN !'##experimental_source Pekin breed COMMENT The alpha-D chain occurs in the minor hemoglobin D molecule, !1which has the beta chain identical with that of the major !1hemoglobin A. Hemoglobin D is expressed in late embryonic !1and adult life. CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15746 #checksum 9173 SEQUENCE /// ENTRY HADKMD #type complete TITLE hemoglobin alpha-D chain - muscovy duck ORGANISM #formal_name Cairina moschata #common_name muscovy duck DATE 20-Sep-1984 #sequence_revision 20-Sep-1984 #text_change 03-Mar-2000 ACCESSIONS A02325; I50443 REFERENCE A02325 !$#authors Erbil, C.; Niessing, J. !$#journal EMBO J. (1983) 2:1339-1343 !$#title The primary structure of the duck alpha(D)-globin gene: an !1unusual 5' splice junction sequence. !$#accession A02325 !'##molecule_type DNA !'##residues 1-141 ##label ERB REFERENCE I50443 !$#authors Niessing, J.; Erbil, C.; Neubauer, V. !$#journal Gene (1982) 18:187-191 !$#title The isolation and partial characterization of linked !1alpha-A- and alpha-D-globin genes from a duck DNA !1recombinant library. !$#cross-references MUID:83028533; PMID:6290322 !$#accession I50443 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-29 ##label NIE !'##cross-references GB:J00925; NID:g212910; PIDN:AAA49147.1; !1PID:g555478 COMMENT The alpha-D chain occurs in the minor hemoglobin D molecule, !1which has the beta chain identical with that of the major !1hemoglobin A. Hemoglobin D is expressed in late embryonic !1and adult life. GENETICS !$#gene alpha-D !$#introns 31/2; 99/3 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15712 #checksum 9310 SEQUENCE /// ENTRY HAGSDA #type complete TITLE hemoglobin alpha-D chain - Andean goose ORGANISM #formal_name Chloephaga melanoptera #common_name Andean goose DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS S00523 REFERENCE S00523 !$#authors Hiebl, I.; Braunitzer, G.; Schneeganss, D. !$#journal Biol. Chem. Hoppe-Seyler (1987) 368:1559-1569 !$#title High-altitude respiration of geese. The primary structures !1of the major and minor hemoglobin-components of adult Andean !1goose (Chloephaga melanoptera, Anatidae): the mutation !1Leu-Ser in position 55 of the beta-chains. !$#cross-references MUID:88163076; PMID:3442599 !$#accession S00523 !'##molecule_type protein !'##residues 1-141 ##label HIE CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15746 #checksum 55 SEQUENCE /// ENTRY HAGSD #type complete TITLE hemoglobin alpha-D chain - graylag goose ORGANISM #formal_name Anser anser #common_name graylag goose DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 03-Mar-2000 ACCESSIONS A02326 REFERENCE A90710 !$#authors Hiebl, I.; Schneeganss, D.; Braunitzer, G. !$#journal Biol. Chem. Hoppe-Seyler (1986) 367:591-599 !$#title The primary structures of the alpha(D)-chains of the !1bar-headed boose (Anser indicus), the greylag goose (Anser) !1and the Canada goose (Branta canadensis). !$#cross-references MUID:87000166; PMID:3755960 !$#accession A02326 !'##molecule_type protein !'##residues 1-141 ##label HIE CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15773 #checksum 1583 SEQUENCE /// ENTRY HAGSDI #type complete TITLE hemoglobin alpha-D chain - bar-headed goose ORGANISM #formal_name Anser indicus #common_name bar-headed goose DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 03-Mar-2000 ACCESSIONS A02327 REFERENCE A90710 !$#authors Hiebl, I.; Schneeganss, D.; Braunitzer, G. !$#journal Biol. Chem. Hoppe-Seyler (1986) 367:591-599 !$#title The primary structures of the alpha(D)-chains of the !1bar-headed boose (Anser indicus), the greylag goose (Anser) !1and the Canada goose (Branta canadensis). !$#cross-references MUID:87000166; PMID:3755960 !$#accession A02327 !'##molecule_type protein !'##residues 1-141 ##label HIE CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15745 #checksum 2003 SEQUENCE /// ENTRY HAGSDC #type complete TITLE hemoglobin alpha-D chain - Canada goose ORGANISM #formal_name Branta canadensis #common_name Canada goose DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 03-Mar-2000 ACCESSIONS A02328 REFERENCE A90710 !$#authors Hiebl, I.; Schneeganss, D.; Braunitzer, G. !$#journal Biol. Chem. Hoppe-Seyler (1986) 367:591-599 !$#title The primary structures of the alpha(D)-chains of the !1bar-headed boose (Anser indicus), the greylag goose (Anser) !1and the Canada goose (Branta canadensis). !$#cross-references MUID:87000166; PMID:3755960 !$#accession A02328 !'##molecule_type protein !'##residues 1-141 ##label HIE CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15804 #checksum 1325 SEQUENCE /// ENTRY HAEHD #type complete TITLE hemoglobin alpha-D chain - greater rhea ORGANISM #formal_name Rhea americana #common_name greater rhea, common rhea DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 03-Mar-2000 ACCESSIONS A02329 REFERENCE A90707 !$#authors Oberthur, W.; Godovac-Zimmermann, J.; Braunitzer, G. !$#journal Biol. Chem. Hoppe-Seyler (1986) 367:507-514 !$#title The expression of alpha(D)-chains in the hemoglobin of adult !1ostrich (Struthio camelus) and American rhea (Rhea !1americana). The different evolution of adult bird alpha(A), !1alpha(D)- and beta-chains. !$#cross-references MUID:86296189; PMID:3741627 !$#accession A02329 !'##molecule_type protein !'##residues 1-141 ##label OBE CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15788 #checksum 1727 SEQUENCE /// ENTRY HAOSD #type complete TITLE hemoglobin alpha-D chain - ostrich ORGANISM #formal_name Struthio camelus #common_name ostrich DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 03-Mar-2000 ACCESSIONS A02330 REFERENCE A90707 !$#authors Oberthur, W.; Godovac-Zimmermann, J.; Braunitzer, G. !$#journal Biol. Chem. Hoppe-Seyler (1986) 367:507-514 !$#title The expression of alpha(D)-chains in the hemoglobin of adult !1ostrich (Struthio camelus) and American rhea (Rhea !1americana). The different evolution of adult bird alpha(A), !1alpha(D)- and beta-chains. !$#cross-references MUID:86296189; PMID:3741627 !$#accession A02330 !'##molecule_type protein !'##residues 1-141 ##label OBE CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15874 #checksum 692 SEQUENCE /// ENTRY HASID #type complete TITLE hemoglobin alpha-D chain - swift ORGANISM #formal_name Apus apus #common_name swift DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS S07481 REFERENCE S07479 !$#authors Nothum, R.; Weber, R.E.; Koesters, J.; Schneeganss, D.; !1Braunitzer, G. !$#journal Biol. Chem. Hoppe-Seyler (1989) 370:1197-1207 !$#title Amino-acid sequences and functional differentiation of !1hemoglobins A and D from swift (Apus apus, Apodiformes). !$#cross-references MUID:90121756; PMID:2610936 !$#accession S07481 !'##molecule_type protein !'##residues 1-141 ##label NOT CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15767 #checksum 2693 SEQUENCE /// ENTRY HAGRDW #type complete TITLE hemoglobin alpha-D chain - white-headed vulture ORGANISM #formal_name Trigonoceps occipitalis #common_name white-headed vulture DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS S04948 REFERENCE S04948 !$#authors Hiebl, I.; Weber, R.E.; Schneeganss, D.; Braunitzer, G. !$#journal Biol. Chem. Hoppe-Seyler (1989) 370:699-706 !$#title High-altitude respiration of Falconiformes. The primary !1structures and functional properties of the major and minor !1hemoglobin components of the adult white-headed vulture !1(Trigonoceps occipitalis, Aegypiinae). !$#cross-references MUID:89374815; PMID:2775491 !$#accession S04948 !'##molecule_type protein !'##residues 1-141 ##label HIE CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15749 #checksum 2071 SEQUENCE /// ENTRY HAGRDR #type complete TITLE hemoglobin alpha-D chain - Rueppell's griffon ORGANISM #formal_name Gyps rueppellii #common_name Rueppell's griffon DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 03-Mar-2000 ACCESSIONS S01195 REFERENCE S00527 !$#authors Hiebl, I.; Weber, R.E.; Schneeganss, D.; Koesters, J.; !1Braunitzer, G. !$#journal Biol. Chem. Hoppe-Seyler (1988) 369:217-232 !$#title High-altitude respiration of birds. Structural adaptations !1in the major and minor hemoglobin components of adult !1Rueppell's griffon (Gyps rueppellii, Aegypiinae): a new !1molecular pattern for hypoxic tolerance. !$#cross-references MUID:88293711; PMID:3401327 !$#accession S01195 !'##molecule_type protein !'##residues 1-141 ##label HIE !'##note the sequence of the alpha-D' chain differs from that shown in !1having 104-Asn CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15826 #checksum 2499 SEQUENCE /// ENTRY HACODG #type complete TITLE hemoglobin alpha-D chain - great cormorant ORGANISM #formal_name Phalacrocorax carbo #common_name great cormorant DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS S01806 REFERENCE S01804 !$#authors Huber, K.; Braunitzer, G.; Schneeganss, D.; Koesters, J.; !1Grimm, F. !$#journal Biol. Chem. Hoppe-Seyler (1988) 369:1251-1258 !$#title The primary structure of the hemoglobin of the cormorant !1(Phalacrocorax carbo, Pelecaniformes). !$#cross-references MUID:89228540; PMID:3245897 !$#accession S01806 !'##molecule_type protein !'##residues 1-141 ##label HUB CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15979 #checksum 1089 SEQUENCE /// ENTRY HAJSB #type complete TITLE hemoglobin alpha-D chain - common starling ORGANISM #formal_name Sturnus vulgaris #common_name common starling DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 03-Mar-2000 ACCESSIONS A02331 REFERENCE A91731 !$#authors Oberthur, W.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1984) 365:159-173 !$#title Hemoglobins of starling (Sturnus vulgaris, Passeriformes). !1The primary structures of alpha(A)-, alpha (D)- and !1beta-chains. !$#cross-references MUID:84184202; PMID:6714943 !$#accession A02331 !'##molecule_type protein !'##residues 1-141 ##label OBE CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15660 #checksum 859 SEQUENCE /// ENTRY HAHTDB #type complete TITLE hemoglobin alpha-D chain - blackbird ORGANISM #formal_name Turdus merula #common_name blackbird DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS S04002 REFERENCE S04000 !$#authors Nothum, R.; Braunitzer, G.; Hiebl, I.; Koesters, J.; !1Schneeganss, D. !$#journal Biol. Chem. Hoppe-Seyler (1989) 370:309-316 !$#title The hemoglobins of the adult blackbird (Turdus merula, !1Passeriformes). The sequence of the major (HbA) and minor !1component (HbD). !$#cross-references MUID:89335259; PMID:2757791 !$#accession S04002 !'##molecule_type protein !'##residues 1-141 ##label NOT CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15680 #checksum 1085 SEQUENCE /// ENTRY HATJD #type complete TITLE hemoglobin alpha-D chain - tuatara ORGANISM #formal_name Sphenodon punctatus #common_name tuatara DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS S01137 REFERENCE S01136 !$#authors Abbasi, A.; Wells, R.M.G.; Brittain, T.; Braunitzer, G. !$#journal Biol. Chem. Hoppe-Seyler (1988) 369:755-764 !$#title Primary structure of the hemoglobins from sphenodon !1(Sphenodon punctatus, tuatara, Rynchocephalia). Evidence for !1the expression of alpha(D)-gene. !$#cross-references MUID:89105321; PMID:3214555 !$#accession S01137 !'##molecule_type protein !'##residues 1-141 ##label ABB CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 16272 #checksum 9772 SEQUENCE /// ENTRY HATTDP #type complete TITLE hemoglobin alpha-D chain - western painted turtle ORGANISM #formal_name Chrysemys picta bellii #common_name western painted turtle DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 03-Mar-2000 ACCESSIONS A02332; S00537 REFERENCE A02332 !$#authors Ruecknagel, K.P.; Reischl, E.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1984) 365:1163-1171 !$#title Hemoglobins of reptiles: expression of alpha(D)-genes in the !1turtles Chrysemys pica bellii and Phrynops hilarii !1(Testudines). !$#cross-references MUID:85103281; PMID:6519642 !$#accession A02332 !'##molecule_type protein !'##residues 1-141 ##label RU1 REFERENCE S00525 !$#authors Ruecknagel, K.P.; Braunitzer, G. !$#journal Biol. Chem. Hoppe-Seyler (1988) 369:123-131 !$#title Hemoglobins of reptiles. The primary structure of the major !1and minor hemoglobin component of adult Western painted !1turtle (Chrysemys picta bellii). !$#cross-references MUID:88209274; PMID:3365328 !$#accession S00537 !'##molecule_type protein !'##residues 1-141 ##label RUE CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 16241 #checksum 8984 SEQUENCE /// ENTRY HATTD #type complete TITLE hemoglobin alpha-D chain - snake-necked turtle ALTERNATE_NAMES component CII ORGANISM #formal_name Phrynops hilarii DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 03-Mar-2000 ACCESSIONS A02333 REFERENCE A02332 !$#authors Ruecknagel, K.P.; Reischl, E.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1984) 365:1163-1171 !$#title Hemoglobins of reptiles: expression of alpha(D)-genes in the !1turtles Chrysemys pica bellii and Phrynops hilarii !1(Testudines). !$#cross-references MUID:85103281; PMID:6519642 !$#accession A02333 !'##molecule_type protein !'##residues 1-141 ##label RUC CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 16237 #checksum 8688 SEQUENCE /// ENTRY HACHPE #type complete TITLE hemoglobin pi' chain - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 31-Oct-1979 #sequence_revision 04-Dec-1986 #text_change 16-Jun-2000 ACCESSIONS A93941; A92289; A02334 REFERENCE A93941 !$#authors Engel, J.D.; Rusling, D.J.; McCune, K.C.; Dodgson, J.B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:1392-1396 !$#title Unusual structure of the chicken embryonic alpha-globin !1gene, pi'. !$#cross-references MUID:83144082; PMID:6572397 !$#accession A93941 !'##molecule_type DNA !'##residues 1-141 ##label ENG !'##cross-references GB:V00408; GB:J00856; NID:g63410; PIDN:CAA23699.1; !1PID:g1628382 !'##note only one chromosomal pi locus was found !'##note initiator Met not shown REFERENCE A92289 !$#authors Chapman, B.S.; Tobin, A.J.; Hood, L.E. !$#journal J. Biol. Chem. (1980) 255:9051-9059 !$#title Complete amino acid sequences of the major early embryonic !1alpha-like globins of the chicken. !$#cross-references MUID:81006979; PMID:6157691 !$#contents chains pi and pi' !$#accession A92289 !'##molecule_type protein !'##residues 1-141 ##label CHA !'##note the sequence shown was designated as chain pi'; the sequence !1having 124-Glu was designated as chain pi COMMENT The pi' chain is the counterpart of the alpha chain in the !1major early embryonic hemoglobin P. GENETICS !$#map_position alpha-globin gene cluster !$#introns 32/2; 100/3 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; embryo; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15578 #checksum 3028 SEQUENCE /// ENTRY HADKP #type complete TITLE hemoglobin pi' chain - muscovy duck ORGANISM #formal_name Cairina moschata #common_name muscovy duck DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 03-Mar-2000 ACCESSIONS A02335 REFERENCE A02335 !$#authors Erbil, C.; Niessing, J. !$#journal Gene (1984) 32:161-170 !$#title Chromosomal arrangement of the duck alpha-globin genes and !1primary structure of the embryonic alpha-globin gene pi'. !$#cross-references MUID:85155473; PMID:6530142 !$#accession A02335 !'##molecule_type DNA !'##residues 1-141 ##label ERB !'##cross-references GB:M10141; NID:g212921; PIDN:AAA49150.1; !1PID:g212922 COMMENT The initiator Met is not shown. GENETICS !$#map_position alpha globin gene cluster, 5' end !$#introns 31/2; 99/3 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; embryo; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15588 #checksum 1867 SEQUENCE /// ENTRY HZHU #type complete TITLE hemoglobin zeta chain [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 18-Aug-1982 #sequence_revision 06-Feb-1998 #text_change 08-Dec-2000 ACCESSIONS A90832; A90938; A91696; A93894; A02336 REFERENCE A90832 !$#authors Proudfoot, N.J.; Gil, A.; Maniatis, T. !$#journal Cell (1982) 31:553-563 !$#title The structure of the human zeta-globin gene and a closely !1linked, nearly identical pseudogene. !$#cross-references MUID:83129370; PMID:6297773 !$#accession A90832 !'##molecule_type DNA !'##residues 1-142 ##label PRO !'##cross-references GB:J00182; GB:J00181; NID:g183790; PIDN:AAB59406.1; !1PID:g386763 !'##note translation of initiator Met is not shown REFERENCE A90938 !$#authors Cohen-Solal, M.M.; Authier, B.; deRiel, J.K.; Murnane, M.J.; !1Forget, B.G. !$#journal DNA (1982) 1:355-363 !$#title Cloning and nucleotide sequence analysis of human embryonic !1zeta-globin cDNA. !$#cross-references MUID:83182021; PMID:6963223 !$#accession A90938 !'##molecule_type mRNA !'##residues 2-142 ##label COH !'##cross-references GB:M24173; NID:g340391; PIDN:AAA61306.1; !1PID:g340392 !'##note translation of initiator Met is not shown REFERENCE A91696 !$#authors Aschauer, H.; Sanguansermsri, T.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1981) 362:1159-1162 !$#title Embryonale Haemoglobine des Menschen: die Primaerstruktur !1der zeta-Ketten. !$#cross-references MUID:82263314; PMID:6179844 !$#accession A91696 !'##molecule_type protein !'##residues 2-142 ##label ASC REFERENCE A91700 !$#authors Aschauer, H.; Schafer, W.; Sanguansermsri, T.; Braunitzer, !1G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1981) 362:1657-1659 !$#title Embryonale Haemoglobine des Menschen: Ac-Ser-Leu-Thr-, die !1N-terminal Sequenz der zeta-Ketten. !$#cross-references MUID:82096755; PMID:6172357 !$#contents annotation; amino-terminal residue REFERENCE A93894 !$#authors Clegg, J.B.; Gagnon, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:6076-6080 !$#title Structure of the zeta chain of human embryonic hemoglobin. !$#cross-references MUID:82082400; PMID:6171809 !$#accession A93894 !'##molecule_type protein !'##residues 2-142 ##label CLE GENETICS !$#gene GDB:HBZ !'##cross-references GDB:119302; OMIM:142310 !$#map_position 16p13.3-16p13.3 COMPLEX two zeta chains combine in heterotetramers with two epsilon !1chains (see PIR:HEHU) to form hemoglobin Gower 1 FUNCTION !$#description in erythrocytes binds and transports molecular oxygen from !1placenta to tissues !$#note an embryonic alpha-type chain synthesized mainly in the yolk !1sac CLASSIFICATION #superfamily globin; globin homology KEYWORDS acetylated amino end; blood; chromoprotein; embryo; !1erythrocyte; heme; heterotetramer; iron; metalloprotein; !1oxygen carrier FEATURE !$2-142 #product hemoglobin zeta chain #status experimental !8#label MAT\ !$3-142 #domain globin homology #label GLB\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental\ !$59 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$88 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 142 #molecular-weight 15637 #checksum 3239 SEQUENCE /// ENTRY HZCZ #type complete TITLE hemoglobin zeta-1 chain - chimpanzee ORGANISM #formal_name Pan troglodytes #common_name chimpanzee DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 03-Mar-2000 ACCESSIONS A02337 REFERENCE A02337 !$#authors Willard, C.; Wong, E.; Hess, J.F.; Shen, C.K.J.; Chapman, !1B.; Wilson, A.C.; Schmid, C.W. !$#journal J. Mol. Evol. (1985) 22:309-315 !$#title Comparison of human and chimpanzee zeta1 globin genes. !$#cross-references MUID:86115299; PMID:3003369 !$#accession A02337 !'##molecule_type DNA !'##residues 1-142 ##label WIL !'##cross-references GB:X03234; NID:g38202; PIDN:CAA26980.1; PID:g38203 COMMENT The zeta chain is an alpha-type chain of the mammalian !1embryonic (early embryonic) hemoglobins. COMMENT The zeta chain is synthesized in the yolk sac tissues. GENETICS !$#gene HBZ1 !$#introns 32/2; 100/3 CLASSIFICATION #superfamily globin; globin homology KEYWORDS acetylated amino end; blood; chromoprotein; egg yolk; !1embryo; erythrocyte; heme; iron; metalloprotein; oxygen !1carrier FEATURE !$3-142 #domain globin homology #label GLB\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status predicted\ !$59 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$88 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 142 #molecular-weight 15537 #checksum 3341 SEQUENCE /// ENTRY A25555 #type complete TITLE hemoglobin zeta chain - goat ORGANISM #formal_name Capra aegagrus hircus #common_name domestic goat DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 16-Jun-2000 ACCESSIONS A25555 REFERENCE A25555 !$#authors Wernke, S.M.; Lingrel, J.B. !$#journal J. Mol. Biol. (1986) 192:457-471 !$#title Nucleotide sequence of the goat embryonic alpha-globin gene !1(zeta) and linkage and evolutionary analysis of the complete !1alpha-globin cluster. !$#cross-references MUID:87169733; PMID:3560223 !$#accession A25555 !'##molecule_type DNA !'##residues 1-141 ##label WER !'##cross-references GB:X04726; NID:g946; PIDN:CAA28435.1; PID:g1234893 !'##note translation of initiator Met is not shown GENETICS !$#gene hbz1 !$#introns 32/2; 100/3 FUNCTION !$#description in erythrocytes binds and transports molecular oxygen from !1placenta to tissues !$#note an embryonic alpha-type chain synthesized mainly in the yolk !1sac CLASSIFICATION #superfamily globin; globin homology KEYWORDS acetylated amino end; blood; chromoprotein; embryo; !1erythrocyte; heme; heterotetramer; iron; metalloprotein; !1oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$1 #modified_site acetylated amino end (Ser) #status !8predicted\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15566 #checksum 1685 SEQUENCE /// ENTRY HZPG #type complete TITLE hemoglobin zeta chain - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 03-Mar-2000 ACCESSIONS A02338 REFERENCE A91732 !$#authors Bieber, F.A.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1984) 365:321-334 !$#title Pre- and perinatal oxygen-transport in mammals: the !1embryonic hemoglobins of the pig (Sus scrofa domestica). !$#cross-references MUID:84210428; PMID:6724525 !$#accession A02338 !'##molecule_type protein !'##residues 1-141 ##label BIE COMMENT Hemoglobin zeta chain is an embryonic alpha-type chain. CLASSIFICATION #superfamily globin; globin homology KEYWORDS acetylated amino end; blood; chromoprotein; embryo; !1erythrocyte; heme; iron; metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$1 #modified_site acetylated amino end (Ser) #status !8experimental\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15402 #checksum 723 SEQUENCE /// ENTRY S01714 #type complete TITLE hemoglobin zeta chain - horse ORGANISM #formal_name Equus caballus #common_name domestic horse DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 03-Mar-2000 ACCESSIONS S01714 REFERENCE S01714 !$#authors Flint, J.; Taylor, A.M.; Clegg, J.B. !$#journal J. Mol. Biol. (1988) 199:427-437 !$#title Structure and evolution of the horse zeta globin locus. !$#cross-references MUID:88172490; PMID:3351936 !$#accession S01714 !'##molecule_type DNA !'##residues 1-142 ##label FLI !'##cross-references EMBL:X07051; NID:g1069; PIDN:CAA30095.1; PID:g1070 GENETICS !$#introns 32/2; 100/3 FUNCTION !$#description in erythrocytes binds and transports molecular oxygen from !1placenta to tissues !$#note an embryonic alpha-type chain synthesized mainly in the yolk !1sac CLASSIFICATION #superfamily globin; globin homology KEYWORDS acetylated amino end; blood; chromoprotein; embryo; !1erythrocyte; heme; heterotetramer; iron; metalloprotein; !1oxygen carrier FEATURE !$2-142 #product hemoglobin zeta chain #status predicted !8#label MAT\ !$3-142 #domain globin homology #label GLB\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status predicted\ !$59 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$88 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 142 #molecular-weight 15563 #checksum 4575 SEQUENCE /// ENTRY A23283 #type complete TITLE hemoglobin zeta chain - mouse ALTERNATE_NAMES hemoglobin alpha embryonic chain x; x protein ORGANISM #formal_name Mus musculus #common_name house mouse DATE 08-Aug-1987 #sequence_revision 08-Aug-1987 #text_change 03-Mar-2000 ACCESSIONS A23283; D43560; A05252 REFERENCE A23283 !$#authors Leder, A.; Weir, L.; Leder, P. !$#journal Mol. Cell. Biol. (1985) 5:1025-1033 !$#title Characterization, expression, and evolution of the mouse !1embryonic zeta-globin gene. !$#cross-references MUID:85213471; PMID:4000117 !$#accession A23283 !'##molecule_type DNA !'##residues 1-142 ##label LED !'##cross-references GB:X62302; GB:M11238; GB:X02645; NID:g50878; !1PIDN:CAA44187.1; PID:g50879 REFERENCE A43560 !$#authors Wilkinson, D.G.; Bailes, J.A.; Champion, J.E.; McMahon, A.P. !$#journal Development (1987) 99:493-500 !$#title A molecular analysis of mouse development from 8 to 10 days !1post coitum detects changes only in embryonic globin !1expression. !$#cross-references MUID:88029090; PMID:2444404 !$#accession D43560 !'##molecule_type mRNA !'##residues 1-117,'N',119-142 ##label WIL !'##cross-references GB:M26898; NID:g193536 !'##note the sequence in GenBank entry MUSGLOBZ, release 103.0, !1(PID:g309259) has the codon CTC for 108-Val rather than the !1published GTC REFERENCE A05252 !$#authors Farace, M.G.; Hill, A.; Tripodi, M.; Padgett, R.W.; !1Raschella, G.; Gambari, R.; Fantoni, A.; Hutchison III, !1C.A.; Edgell, M.H. !$#journal Gene (1984) 31:241-245 !$#cross-references MUID:85128441; PMID:6084630 !$#accession A05252 !'##molecule_type mRNA !'##residues 'L',45-142 ##label FAR !'##cross-references GB:M13125; NID:g193801; PIDN:AAA37794.1; !1PID:g193802 GENETICS !$#introns 32/2; 100/3 FUNCTION !$#description in erythrocytes binds and transports molecular oxygen from !1placenta to tissues !$#note an embryonic alpha-type chain synthesized mainly in the yolk !1sac CLASSIFICATION #superfamily globin; globin homology KEYWORDS acetylated amino end; blood; chromoprotein; embryo; !1erythrocyte; heme; heterotetramer; iron; metalloprotein; !1oxygen carrier FEATURE !$2-142 #product hemoglobin zeta chain #status predicted !8#label MAT\ !$3-142 #domain globin homology #label GLB\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status predicted\ !$59 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$88 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 142 #molecular-weight 16235 #checksum 3414 SEQUENCE /// ENTRY HASNV #type complete TITLE hemoglobin alpha chain - aspic viper ORGANISM #formal_name Vipera aspis #common_name aspic viper DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 03-Mar-2000 ACCESSIONS A02339 REFERENCE A02339 !$#authors Duguet, M.; Chauvet, J.P.; Acher, R. !$#journal FEBS Lett. (1974) 47:333-337 !$#title Phylogeny of hemoglobins: the complete amino acid sequence !1of an alpha-chain of viper (Vipera aspis) hemoglobin. !$#cross-references MUID:75039165; PMID:4430360 !$#accession A02339 !'##molecule_type protein !'##residues 1-141 ##label DUG COMMENT This is one of two types of alpha chains found in viper !1hemoglobin. CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15437 #checksum 1012 SEQUENCE /// ENTRY HAFG3T #type complete TITLE hemoglobin alpha chain, tadpole - bullfrog ORGANISM #formal_name Rana catesbeiana #common_name bullfrog DATE 31-Jul-1980 #sequence_revision 31-Jul-1980 #text_change 03-Mar-2000 ACCESSIONS A02340 REFERENCE A02340 !$#authors Maruyama, T.; Watt, K.W.K.; Riggs, A. !$#journal J. Biol. Chem. (1980) 255:3285-3293 !$#title Hemoglobins of the tadpole of the bullfrog, Rana !1catesbeiana. Amino acid sequence of the alpha chain of a !1major component. !$#cross-references MUID:80159937; PMID:6965939 !$#accession A02340 !'##molecule_type protein !'##residues 1-141 ##label MAR COMMENT This alpha chain is a component of hemoglobin III. CLASSIFICATION #superfamily globin; globin homology KEYWORDS acetylated amino end; blood; chromoprotein; erythrocyte; !1heme; iron; metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$1 #modified_site acetylated amino end (Ser) #status !8experimental\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 14874 #checksum 370 SEQUENCE /// ENTRY HAXL1 #type complete TITLE hemoglobin alpha chain, major - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 03-Mar-2000 ACCESSIONS A93456; A92863; A90964; S02731; I51428; A02341 REFERENCE A93456 !$#authors Kay, R.M.; Harris, R.; Patient, R.K.; Williams, J.G. !$#journal Nucleic Acids Res. (1983) 11:1537-1542 !$#title Complete nucleotide sequence of a cloned cDNA derived from !1the major adult alpha-globin mRNA of Xenopus laevis. !$#cross-references MUID:83143364; PMID:6298747 !$#accession A93456 !'##molecule_type mRNA !'##residues 1-142 ##label KAY REFERENCE A92863 !$#authors Partington, G.A.; Baralle, F.E. !$#journal J. Mol. Biol. (1981) 145:463-470 !$#title Isolation of a Xenopus laevis alpha-globin gene. !$#cross-references MUID:81267326; PMID:7265209 !$#accession A92863 !'##molecule_type DNA !'##residues 'S',30-45,'N',47-100;127-142 ##label PAR REFERENCE A90964 !$#authors Richardson, C.; Cappello, J.; Cochran, M.D.; Armentrout, !1R.W.; Brown, R.D. !$#journal Dev. Biol. (1980) 78:161-172 !$#title Partial sequence analysis of Xenopus alpha- and beta-globin !1mRNA as determined from recombinant DNA plasmids. !$#cross-references MUID:80247171; PMID:6249685 !$#accession A90964 !'##molecule_type mRNA !'##residues 'KLH',72-96,'S',98-113,'L',115-142 ##label RIC !'##cross-references GB:M15381; NID:g213995; PIDN:AAA49662.1; !1PID:g213996 REFERENCE S02731 !$#authors Stalder, J.; Wirthmueller, U.; Beck, J.; Gruber, A.; !1Meyerhof, W.; Knoechel, W.; Weber, R. !$#journal J. Mol. Evol. (1988) 28:64-71 !$#title Primary structure and evolutionary relationship between the !1adult alpha-globin genes and their 5'-flanking regions of !1Xenopus laevis and Xenopus tropicalis. !$#cross-references MUID:89178739; PMID:3148743 !$#accession S02731 !'##status translation not shown !'##molecule_type DNA !'##residues 1-142 ##label STA !'##cross-references EMBL:X14259; NID:g64722; PIDN:CAA32472.1; !1PID:g64723 REFERENCE I51428 !$#authors Kay, R.M.; Harris, R.; Patient, R.K.; Williams, J.G. !$#journal Nucleic Acids Res. (1980) 8:2691-2707 !$#title Molecular cloning of cDNA sequences coding for the major !1alpha- and beta-globin polypeptides of adult Xenopus laevis. !$#cross-references MUID:81053706; PMID:7001356 !$#accession I51428 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 129-142 ##label KA2 !'##cross-references GB:M10577; NID:g214201; PIDN:AAA49732.1; !1PID:g214202 GENETICS !$#introns 32/2; 100/3 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-142 #domain globin homology #label GLB\ !$59 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$88 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 142 #molecular-weight 15747 #checksum 2278 SEQUENCE /// ENTRY HAXL2 #type complete TITLE hemoglobin alpha chain, minor - African clawed frog ALTERNATE_NAMES hemoglobin alpha-II chain ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 03-Mar-2000 ACCESSIONS A02342; S02733 REFERENCE A93457 !$#authors Knochel, W.; Meyerhof, W.; Hummel, S.; Grundmann, U. !$#journal Nucleic Acids Res. (1983) 11:1543-1553 !$#title Molecular cloning and sequencing of mRNAs coding for minor !1adult globin polypeptides of Xenopus laevis. !$#cross-references MUID:83143365; PMID:6298748 !$#accession A02342 !'##molecule_type mRNA !'##residues 1-142 ##label KNO !'##cross-references GB:X01559; NID:g64536; PIDN:CAA25712.1; PID:g64537 REFERENCE S02731 !$#authors Stalder, J.; Wirthmueller, U.; Beck, J.; Gruber, A.; !1Meyerhof, W.; Knoechel, W.; Weber, R. !$#journal J. Mol. Evol. (1988) 28:64-71 !$#title Primary structure and evolutionary relationship between the !1adult alpha-globin genes and their 5'-flanking regions of !1Xenopus laevis and Xenopus tropicalis. !$#cross-references MUID:89178739; PMID:3148743 !$#accession S02733 !'##status translation not shown !'##molecule_type DNA !'##residues 1-23,'T',25-29,'L',31-142 ##label STA !'##cross-references EMBL:X14261; NID:g64724; PIDN:CAA32474.1; !1PID:g64725 GENETICS !$#introns 32/2; 100/3 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-142 #domain globin homology #label GLB\ !$59 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$88 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 142 #molecular-weight 15774 #checksum 2533 SEQUENCE /// ENTRY HAXLWA #type complete TITLE hemoglobin alpha chain - western clawed frog ORGANISM #formal_name Xenopus tropicalis #common_name western clawed frog DATE 25-Oct-1987 #sequence_revision 19-Oct-1995 #text_change 03-Mar-2000 ACCESSIONS S02732; A25929 REFERENCE S02731 !$#authors Stalder, J.; Wirthmueller, U.; Beck, J.; Gruber, A.; !1Meyerhof, W.; Knoechel, W.; Weber, R. !$#journal J. Mol. Evol. (1988) 28:64-71 !$#title Primary structure and evolutionary relationship between the !1adult alpha-globin genes and their 5'-flanking regions of !1Xenopus laevis and Xenopus tropicalis. !$#cross-references MUID:89178739; PMID:3148743 !$#accession S02732 !'##status translation not shown !'##molecule_type DNA !'##residues 1-142 ##label STA !'##cross-references EMBL:X14260; NID:g65297; PIDN:CAA32473.1; !1PID:g65298 REFERENCE A92964 !$#authors Knochel, W.; Korge, E.; Basner, A.; Meyerhof, W. !$#journal J. Mol. Evol. (1986) 23:211-223 !$#title Globin evolution in the genus Xenopus: comparative analysis !1of cDNAs coding for adult globin polypeptides of Xenopus !1borealis and Xenopus tropicalis. !$#cross-references MUID:87112760; PMID:3100812 !$#accession A25929 !'##molecule_type mRNA !'##residues 2-142 ##label KNO !'##cross-references GB:M32454; NID:g213943; PIDN:AAA49644.1; !1PID:g213944 !'##note initiator Met shown but not translated GENETICS !$#introns 32/2; 100/3 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-142 #domain globin homology #label GLB\ !$59 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$88 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 142 #molecular-weight 15887 #checksum 9552 SEQUENCE /// ENTRY HANERM #type fragment TITLE hemoglobin alpha chain, minor - Iberian ribbed newt (fragment) ORGANISM #formal_name Pleurodeles waltlii #common_name Iberian ribbed newt DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 03-Mar-2000 ACCESSIONS B25640 REFERENCE A91546 !$#authors Flavin, M.; Romeo, P.H.; Cohen-Solal, M.; Duprat, A.M.; !1Valentin, C.; Rosa, J. !$#journal Gene (1986) 42:159-168 !$#title Cloning and sequencing of mRNAs coding for two adult alpha !1globin chains of the salamander Pleurodeles waltlii. !$#cross-references MUID:86275988; PMID:3015729 !$#accession B25640 !'##molecule_type mRNA !'##residues 1-133 ##label FLA !'##cross-references GB:M13691; NID:g213865; PIDN:AAA49613.1; !1PID:g213866 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$1-133 #domain globin homology (fragment) #label GLB\ !$50 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$79 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 133 #checksum 1789 SEQUENCE /// ENTRY HANER #type complete TITLE hemoglobin alpha chain, major - Iberian ribbed newt ORGANISM #formal_name Pleurodeles waltlii #common_name Iberian ribbed newt DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 03-Mar-2000 ACCESSIONS A25640 REFERENCE A91546 !$#authors Flavin, M.; Romeo, P.H.; Cohen-Solal, M.; Duprat, A.M.; !1Valentin, C.; Rosa, J. !$#journal Gene (1986) 42:159-168 !$#title Cloning and sequencing of mRNAs coding for two adult alpha !1globin chains of the salamander Pleurodeles waltlii. !$#cross-references MUID:86275988; PMID:3015729 !$#accession A25640 !'##molecule_type mRNA !'##residues 1-141 ##label FLA !'##cross-references GB:M13365; NID:g213863; PIDN:AAA49612.1; !1PID:g213864 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15886 #checksum 9245 SEQUENCE /// ENTRY HANE #type complete TITLE hemoglobin alpha chain - roughskin newt ORGANISM #formal_name Taricha granulosa #common_name roughskin newt DATE 29-Jul-1981 #sequence_revision 29-Jul-1981 #text_change 03-Mar-2000 ACCESSIONS A02343 REFERENCE A02343 !$#authors Coates, M.; Brimhall, B.; Stenzel, P.; Hermodson, M.; !1Gibson, D.; Jones, R.T.; Vedvick, T. !$#journal Aust. J. Biol. Sci. (1977) 30:1-19 !$#title Alpha-chain sequence of newt haemoglobin (Taricha !1granulosa). !$#cross-references MUID:77266268; PMID:901300 !$#accession A02343 !'##molecule_type protein !'##residues 1-142 ##label COA CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-142 #domain globin homology #label GLB\ !$59 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$88 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 142 #molecular-weight 15712 #checksum 9362 SEQUENCE /// ENTRY HAXM #type complete TITLE hemoglobin alpha chain - axolotl ORGANISM #formal_name Ambystoma mexicanum #common_name axolotl DATE 02-Apr-1982 #sequence_revision 02-Apr-1982 #text_change 03-Mar-2000 ACCESSIONS A02344 REFERENCE A02344 !$#authors Boissel, J.P.; Wajcman, H.; Labie, D. !$#journal Eur. J. Biochem. (1980) 103:613-621 !$#title Hemoglobins of an amphibian, the neotenous Ambystoma !1mexicanum. Complete amino-acid sequence of the alpha chain !1of the major component using automatic solid-phase Edman !1degradation. !$#cross-references MUID:80134253; PMID:7358052 !$#accession A02344 !'##molecule_type protein !'##residues 1-142 ##label BOI CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-142 #domain globin homology #label GLB\ !$59 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$88 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 142 #molecular-weight 15900 #checksum 6823 SEQUENCE /// ENTRY HACA #type complete TITLE hemoglobin alpha chain - common carp ORGANISM #formal_name Cyprinus carpio #common_name common carp DATE 24-Apr-1984 #sequence_revision 09-Apr-1999 #text_change 03-Mar-2000 ACCESSIONS I50491; A02345 REFERENCE I50491 !$#authors Takeshita, S.; Aoki, T.; Fukumaki, Y.; Takagi, Y. !$#journal Biochim. Biophys. Acta (1984) 783:265-271 !$#title Cloning and sequence analysis of a cDNA for the alpha-globin !1mRNA of carp, Cyprinus carpio. !$#cross-references MUID:85072917; PMID:6548931 !$#accession I50491 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-143 ##label TAK !'##cross-references GB:M25643; NID:g213043; PIDN:AAA49202.1; !1PID:g213044 REFERENCE A02345 !$#authors Hilse, K.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1968) 349:433-450 !$#title Haemoglobine, XVI. Die Aminosaeuresequenz der alpha-Ketten !1der beiden Hauptkomponenten des Karpfenhaemoglobins. !$#cross-references MUID:68361093; PMID:4875309 !$#accession A02345 !'##molecule_type protein !'##residues 2-12,'IA',15-58,'HGK',62-83,'S',85-90,'S',92-104,'NHIV', !1109,'G',111,'MFYL',116-143 ##label HIL CLASSIFICATION #superfamily globin; globin homology KEYWORDS acetylated amino end; blood; chromoprotein; erythrocyte; !1heme; iron; metalloprotein; oxygen carrier FEATURE !$3-143 #domain globin homology #label GLB\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental\ !$60 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$89 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 143 #molecular-weight 15447 #checksum 3388 SEQUENCE /// ENTRY HAGY #type complete TITLE hemoglobin alpha chain - goldfish ORGANISM #formal_name Carassius auratus #common_name goldfish DATE 02-Apr-1982 #sequence_revision 17-May-1985 #text_change 03-Mar-2000 ACCESSIONS A02347 REFERENCE A91739 !$#authors Rodewald, K.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1984) 365:95-104 !$#title The primary structure of the hemoglobin from goldfish !1(Carassius auratus). !$#cross-references MUID:84184196; PMID:6714939 !$#accession A02347 !'##molecule_type protein !'##residues 1-142 ##label ROD CLASSIFICATION #superfamily globin; globin homology KEYWORDS acetylated amino end; blood; chromoprotein; erythrocyte; !1heme; iron; metalloprotein; oxygen carrier FEATURE !$2-142 #domain globin homology #label GLB\ !$1 #modified_site acetylated amino end (Ser) #status !8experimental\ !$59 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$88 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 142 #molecular-weight 15426 #checksum 2477 SEQUENCE /// ENTRY HACC1 #type complete TITLE hemoglobin alpha chain - desert sucker (tentative sequence) ORGANISM #formal_name Catostomus clarki #common_name desert sucker DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 31-Mar-2000 ACCESSIONS A92116; A02346 REFERENCE A92116 !$#authors Powers, D.A.; Edmundson, A.B. !$#journal J. Biol. Chem. (1972) 247:6694-6707 !$#title Multiple hemoglobins of catostomid fish. II. The amino acid !1sequence of the major alpha chain from Catostomus clarkii !1hemoglobins. !$#cross-references MUID:73015892; PMID:4672861 !$#accession A92116 !'##molecule_type protein !'##residues 1-142 ##label POW !'##note this sequence has the same insertions and deletions compared !1with mammalian alpha chains as does that of carp REFERENCE A92115 !$#authors Powers, D.A.; Edmundson, A.B. !$#journal J. Biol. Chem. (1972) 247:6686-6693 !$#title Multiple hemoglobins of catostomid fish. I. Isolation and !1characterization of the isohemoglobins from Catostomus !1clarkii. !$#cross-references MUID:73015891; PMID:5076774 !$#contents annotation !$#note this species of catostomid fish possesses six types of !1hemoglobin chains, including a major alpha chain, a minor !1alpha chain, two major beta chains, and two minor beta !1chains !$#note ten different tetramers are resolved by chromatography and !1electrophoresis, eight of which are anodal and two, !1cathodal; the cathodal tetramers do not exhibit the Bohr !1effect, due to lack of the carboxyl-terminal His in the beta !1chains and to blocking of the alpha-amino group on the !1amino-terminal residue of the alpha chains !$#note the possession of both major types of tetramers may be a !1physiological advantage for fishes living in fast-moving !1water habitats, as does this species CLASSIFICATION #superfamily globin; globin homology KEYWORDS blocked amino end; blood; chromoprotein; erythrocyte; heme; !1iron; metalloprotein; oxygen carrier FEATURE !$2-142 #domain globin homology #label GLB\ !$1 #modified_site blocked amino end (Ser) (probably !8acetylated) #status experimental\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$88 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 142 #molecular-weight 15431 #checksum 2764 SEQUENCE /// ENTRY S03399 #type complete TITLE hemoglobin alpha chain - electric eel ORGANISM #formal_name Electrophorus electricus #common_name electric eel DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-May-2000 ACCESSIONS S03399 REFERENCE S03399 !$#authors Huber, F.; Braunitzer, G. !$#journal Biol. Chem. Hoppe-Seyler (1989) 370:245-250 !$#title The primary structure of the hemoglobin of the electric eel !1(Electrophorus electricus). !$#cross-references MUID:89228561; PMID:2713104 !$#accession S03399 !'##molecule_type protein !'##residues 1-142 ##label HUB CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; heme; iron; metalloprotein; oxygen !1carrier FEATURE !$2-142 #domain globin homology #label GLB\ !$88 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 142 #molecular-weight 15344 #checksum 9816 SEQUENCE /// ENTRY HATR1 #type complete TITLE hemoglobin I alpha chain - rainbow trout (tentative sequence) ORGANISM #formal_name Oncorhynchus mykiss #common_name rainbow trout DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 19-May-2000 ACCESSIONS A02348 REFERENCE A02348 !$#authors Bossa, F.; Barra, D.; Petruzzelli, R.; Martini, F.; Brunori, !1M. !$#journal Biochim. Biophys. Acta (1978) 536:298-305 !$#title Primary structure of hemoglobin from trout (Salmo irideus). !1Amino acid sequence of alpha chain of Hb trout I. !$#cross-references MUID:79042280; PMID:708770 !$#accession A02348 !'##molecule_type protein !'##residues 1-144 ##label BOS !'##note this hemoglobin has two more residues, 32-Asp and 33-Lys, than !1other fish hemoglobins; this difference could be due to a !1minor component CLASSIFICATION #superfamily globin; globin homology KEYWORDS acetylated amino end; blood; chromoprotein; erythrocyte; !1heme; iron; metalloprotein; oxygen carrier FEATURE !$2-144 #domain globin homology #label GLB\ !$1 #modified_site acetylated amino end (Ser) #status !8experimental\ !$61 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$90 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 144 #molecular-weight 15306 #checksum 5197 SEQUENCE /// ENTRY S04589 #type complete TITLE hemoglobin alpha chain - Atlantic salmon ORGANISM #formal_name Salmo salar #common_name Atlantic salmon DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-May-2000 ACCESSIONS S04589 REFERENCE S04589 !$#authors Wolff, J.P.; Gannon, F. !$#journal Nucleic Acids Res. (1989) 17:4369 !$#title cDNA and deduced amino acid sequence of the Salmo salar !1(Atlantic salmon) adult hemoglobin alpha chain. !$#cross-references MUID:89296481; PMID:2740221 !$#accession S04589 !'##molecule_type mRNA !'##residues 1-143 ##label WOL !'##cross-references EMBL:X14431; NID:g64359; PIDN:CAA32596.1; !1PID:g64360 !'##note the authors translated the codon ATT for residue 18 as Glu CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; heme; iron; metalloprotein; oxygen !1carrier FEATURE !$3-143 #domain globin homology #label GLB\ !$89 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 143 #molecular-weight 15219 #checksum 3222 SEQUENCE /// ENTRY HALUA #type complete TITLE hemoglobin alpha chain - South American lungfish (tentative sequence) ORGANISM #formal_name Lepidosiren paradoxus #common_name South American lungfish DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 31-Mar-2000 ACCESSIONS A02349 REFERENCE A91735 !$#authors Rodewald, K.; Stangl, A.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1984) 365:639-649 !$#title Primary structure, biochemical and physiological aspects of !1hemoglobin from South American lungfish (Lepidosiren !1paradoxus, Dipnoi). !$#cross-references MUID:85005237; PMID:6090299 !$#accession A02349 !'##molecule_type protein !'##residues 1-143 ##label ROD !'##note compositions of tryptic peptides and sequences of residues 1-77 !1and 97-136 were determined; the unsequenced residues were !1positioned by homology with the carp sequence CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-143 #domain globin homology #label GLB\ !$60 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$89 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 143 #molecular-weight 16092 #checksum 1081 SEQUENCE /// ENTRY HARYM #type complete TITLE hemoglobin alpha chain - marbled electric ray ORGANISM #formal_name Torpedo marmorata #common_name marbled electric ray DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 03-Mar-2000 ACCESSIONS S05418; S05419 REFERENCE S05418 !$#authors Huber, F.; Braunitzer, G. !$#journal Biol. Chem. Hoppe-Seyler (1989) 370:831-838 !$#title The primary structure of electric ray hemoglobin (Torpedo !1marmorata). Bohr effect and phosphate interaction. !$#cross-references MUID:90074179; PMID:2590465 !$#accession S05418 !'##molecule_type protein !'##residues 1-141 ##label HUB !'##note 9-Ile, 61-Asp, 72-Asp, 82-His, 91-Asp, and 117-Lys were also !1found CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$2-141 #domain globin homology #label GLB\ !$59 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$88 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15866 #checksum 6868 SEQUENCE /// ENTRY HARKJ #type complete TITLE hemoglobin alpha chain - Port Jackson shark ORGANISM #formal_name Heterodontus portusjacksoni #common_name Port Jackson shark DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 03-Mar-2000 ACCESSIONS A02350 REFERENCE A02350 !$#authors Nash, A.R.; Fisher, W.K.; Thompson, E.O.P. !$#journal Aust. J. Biol. Sci. (1976) 29:73-97 !$#title Haemoglobins of the shark, Heterodontus portusjacksoni II. !1Amino acid sequence of the alpha-chain. !$#cross-references MUID:76277354; PMID:962723 !$#accession A02350 !'##molecule_type protein !'##residues 1-148 ##label NAS CLASSIFICATION #superfamily globin; globin homology KEYWORDS acetylated amino end; blood; chromoprotein; erythrocyte; !1heme; iron; metalloprotein; oxygen carrier FEATURE !$9-148 #domain globin homology #label GLB\ !$1 #modified_site acetylated amino end (Ser) #status !8experimental\ !$66 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$95 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 148 #molecular-weight 16166 #checksum 3708 SEQUENCE /// ENTRY HAFGH #type complete TITLE hemoglobin alpha-type chain, cardiac muscle - bullfrog ORGANISM #formal_name Rana catesbeiana #common_name bullfrog DATE 06-Jul-1982 #sequence_revision 06-Jul-1982 #text_change 03-Mar-2000 ACCESSIONS A02351 REFERENCE A02351 !$#authors Maeda, N.; Fitch, W.M. !$#journal J. Biol. Chem. (1982) 257:2806-2815 !$#title Isolation and amino acid sequence of a monomeric hemoglobin !1in heart muscle of the bullfrog, Rana catesbeiana. !$#cross-references MUID:82142402; PMID:7037772 !$#accession A02351 !'##molecule_type protein !'##residues 1-132 ##label MAE !'##note this chain appears to have diverged from the line leading to !1alpha-type hemoglobin chains close to the divergence of !1alpha and beta chains COMMENT Functionally, this monomeric hemoglobin may replace !1myocardial myoglobin in this amphibian species. CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; cardiac muscle; chromoprotein; erythrocyte; heart; !1heme; iron; metalloprotein; oxygen carrier FEATURE !$2-132 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$83 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 132 #molecular-weight 14391 #checksum 2370 SEQUENCE /// ENTRY HBHU #type complete TITLE hemoglobin beta chain [validated] - human ALTERNATE_NAMES hemoglobin-derived opioid peptide CONTAINS LVV-hemorphin-6; LVV-hemorphin-7 ORGANISM #formal_name Homo sapiens #common_name man DATE 24-Apr-1984 #sequence_revision 31-May-1996 #text_change 15-Sep-2000 ACCESSIONS A53136; A90805; B91637; I59432; I37204; I54148; A60062; !1JQ1518; S68371; A02352; I61222; I61223; I61224; I61225; !1I61226; I61227; I61228; I61229; I61230; I61231; I61232; !1I61233; I61234; I61235; I61236; I61237 REFERENCE A53136 !$#authors Fullerton, S.M.; Harding, R.M.; Boyce, A.J.; Clegg, J.B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1994) 91:1805-1809 !$#title Molecular and population genetic analysis of allelic !1sequence diversity at the human beta-globin locus. !$#cross-references MUID:94173918; PMID:7907422 !$#accession A53136 !'##status nucleic acid sequence not shown; translation not shown; !1translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-147 ##label FUL !'##cross-references GB:L26462; PIDN:AAA21100.1; PID:g532506; GB:L26463; !1PID:g532507; GB:L26464; PID:g532514; GB:L26465; PID:g532508; !1GB:L26466; PID:g532509; GB:L26467; PID:g532510; GB:L26468; !1PID:g532511; GB:L26469; PID:g532512; GB:L26470; PID:g532513; !1GB:L26471; PID:g532515; GB:L26472; PID:g532516; GB:L26473; !1PID:g532517; GB:L26474; PID:g532518; GB:L26475; PID:g532519; !1GB:L26476; PID:g532520; GB:L26477; PID:g532521; GB:L26478; !1PID:g532522 !'##note 60 normal and 12 thalassemia mutant sequences were determined REFERENCE A90805 !$#authors Lawn, R.M.; Efstratiadis, A.; O'Connell, C.; Maniatis, T. !$#journal Cell (1980) 21:647-651 !$#title The nucleotide sequence of the human beta-globin gene. !$#cross-references MUID:81064667; PMID:6254664 !$#accession A90805 !'##molecule_type DNA !'##residues 2-147 ##label LAW !'##cross-references EMBL:V00499; NID:g29440; PIDN:CAA23758.1; !1PID:g29441 !'##note initiator Met not shown REFERENCE A91637 !$#authors Braunitzer, G.; Gehring-Muller, R.; Hilschmann, N.; Hilse, !1K.; Hobom, G.; Rudloff, V.; Wittmann-Liebold, B. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1961) 325:283-286 !$#title Die Konstitution des normalen adulten Humanhaemoglobins. !$#accession B91637 !'##molecule_type protein !'##residues 2-147 ##label BRA !'##note article in German with English abstract REFERENCE I59432 !$#authors Marotta, C.A.; Forget, B.G.; Cohen-Solal, M.M.; Weissman, !1S.M. !$#journal Prog. Nucleic Acid Res. Mol. Biol. (1976) 19:165-175 !$#title Nucleotide sequence analysis of coding and noncoding regions !1of human beta-globin mRNA. !$#cross-references MUID:77126403; PMID:1019344 !$#accession I59432 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-3,'X',5-6,'V',8-23,'X',25-30,'X',32-42,'XX',45-49,'X', !151-52,'X',54-110,'X',112-127,'X',129-147 ##label MAR !'##cross-references GB:M25079; NID:g179408; PIDN:AAA35597.1; !1PID:g179409 !'##note mutant sickle cell hemoglobin beta chain REFERENCE I37204 !$#authors Marotta, C.A.; Wilson, J.T.; Forget, B.G.; Weissman, S.M. !$#journal J. Biol. Chem. (1977) 252:5040-5053 !$#title Human beta-globin messenger RNA. III. Nucleotide sequences !1derived from complementary DNA. !$#cross-references MUID:77207124; PMID:68958 !$#accession I37204 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-6,'V',8-14,'X',16-147 ##label MA2 !'##cross-references EMBL:V00500; NID:g29445; PIDN:CAA23759.1; !1PID:g29446 !'##note mutant sickle cell hemoglobin beta chain REFERENCE I54148 !$#authors Limborskaya, S.A.; Bukhman, V.L.; Prosnyak, M.I.; Fedorov, !1A.N.; Slominskii, P.A.; Ninkina, N.N.; Ryskov, A.P. !$#journal Genetika (1987) 23:152-159 !$#title Molecular causes of thalassemia: IV. Cloning of the !1beta-globin gene of a beta-thalassemia patient from !1Azerbaidzhan and determination of a point mutation in a !1minor intron. !$#accession I54148 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-147 ##label LIM !'##cross-references GB:M36640; NID:g183829; PIDN:AAA52634.1; !1PID:g183830 REFERENCE A60062 !$#authors Glaemsta, E.L.; Marklund, A.; Hellman, U.; Wernstedt, C.; !1Terenius, L.; Nyberg, F. !$#journal Regul. Pept. (1991) 34:169-179 !$#title Isolation and characterization of a hemoglobin-derived !1opioid peptide from the human pituitary gland. !$#cross-references MUID:92021602; PMID:1924887 !$#accession A60062 !'##molecule_type protein !'##residues 33-41 ##label GLA !'##note this sequence corresponds to residues 33-41 of hemoglobin beta, !1gamma, delta and epsilon chains REFERENCE JQ1518 !$#authors Glaemsta, E.L.; Meyerson, B.; Silberring, J.; Terenins, L.; !1Nyberg, F. !$#journal Biochem. Biophys. Res. Commun. (1992) 184:1060-1066 !$#title Isolation of a hemoglobin-derived opioid peptide from !1cerebrospinal fluid of patients with cerebrovascular !1bleedings. !$#cross-references MUID:92246921; PMID:1575724 !$#accession JQ1518 !'##molecule_type protein !'##residues 33-42 ##label GL2 !'##experimental_source ventricular cerebrospinal fluid !'##note this sequence corresponds to residues 33-42 of hemoglobin beta, !1gamma, delta and epsilon chains REFERENCE A50669 !$#authors Fermi, G.; Perutz, M.F. !$#submission submitted to the Brookhaven Protein Data Bank, March 1984 !$#cross-references PDB:4HHB !$#contents annotation; X-ray crystallography, 1.74 angstroms, residues !12-146 REFERENCE A92953 !$#authors Fermi, G. !$#journal J. Mol. Biol. (1975) 97:237-256 !$#title Three-dimensional Fourier synthesis of human !1deoxyhaemoglobin at 2.5 angstrom resolution: refinement of !1the atomic model. !$#cross-references MUID:76027820; PMID:1177322 !$#contents annotation; X-ray crystallography, 2.5 angstroms REFERENCE A44527 !$#authors Arnone, A. !$#journal Nature (1972) 237:146-149 !$#title X-ray diffraction study of binding of 2,3-diphosphoglycerate !1to human deoxyhaemoglobin. !$#cross-references MUID:72200594; PMID:4555506 !$#contents annotation; X-ray crystallography, 3.5 angstroms !$#note one molecule of 2,3-diphosphoglycerate binds per hemoglobin !1tetramer; in mammalian erythrocytes it occurs in !1approximately equimolar concentrations with hemoglobin and !1helps regulate the oxygen affinity of hemoglobin REFERENCE A57978 !$#authors Jia, L.; Bonaventura, C.; Bonaventura, J.; Stamler, J.S. !$#journal Nature (1996) 380:221-226 !$#title S-nitrosohaemoglobin: a dynamic activity of blood involved !1in vascular control. !$#cross-references MUID:96207749; PMID:8637569 !$#contents annotation; nitrosonium binding !$#note evidence for the binding of nitrosonium to form !1S-nitrosocysteine in lung and its release during capillary !1transit, possibly mediated by exogenous nitrosothiols REFERENCE A58579 !$#authors Stamler, J.S.; Jia, L.; Eu, J.P.; McMahon, T.J.; Demchenko, !1I.T.; Bonaventura, J.; Gernert, K.; Piantadosi, C.A. !$#journal Science (1997) 276:2034-2037 !$#title Blood flow regulation by S-nitrosohemoglobin in the !1physiological gradient. !$#cross-references MUID:97342849; PMID:9197264 !$#contents annotation; nitrosonium binding !$#note evidence for the physiological consequences of nitric oxide !1binding to form S-nitrosocysteine REFERENCE S68371 !$#authors Razynska, A.; Matheson-Urbaitis, B.; Fronticelli, C.; !1Collins, J.H.; Bucci, E. !$#journal Arch. Biochem. Biophys. (1996) 326:119-125 !$#title Stabilization of the tetrameric structure of human and !1bovine hemoglobins by pseudocrosslinking with muconic acid. !$#cross-references MUID:96154256; PMID:8579359 !$#accession S68371 !'##molecule_type protein !'##residues 2-7;10-39,'G',41-65;67-121;123-144,'L',146-147 ##label RAZ REFERENCE A39865 !$#authors Prome, D.; Blouquit, Y.; Ponthus, C.; Prome, J.C.; Rosa, J. !$#journal J. Biol. Chem. (1991) 266:13050-13054 !$#title Structure of the human adult hemoglobin minor fraction A1b !1by electrospray and secondary ion mass spectrometry. Pyruvic !1acid as amino-terminal blocking group. !$#cross-references MUID:91302324; PMID:2071591 !$#contents annotation; post-translational modification !$#note the modification producing the minor (less than 0.5%) A1b !1form is identified as a pyruvic acid ketimine blocked amino !1end GENETICS !$#gene GDB:HBB !'##cross-references GDB:119297; OMIM:141900 !$#map_position 11p15.5-11p15.5 !$#introns 31/2; 105/3 COMPLEX Two beta chains combine to form heterotetramers with two !1alpha chains (see PIR:HAHU) to form adult hemoglobin A; at !1low alpha chain concentrations, beta chains can combine in !1homotetramers to form hemoglobin H. FUNCTION !$#description in erythrocytes binds and transports molecular oxygen from !1lung to tissues CLASSIFICATION #superfamily globin; globin homology KEYWORDS blocked amino end; blood; chromoprotein; erythrocyte; heme; !1heterotetramer; homotetramer; iron; metalloprotein; opioid !1peptide; oxygen carrier FEATURE !$2-147 #product hemoglobin beta chain #status experimental !8#label MAT\ !$4-147 #domain globin homology #label GLB\ !$33-42 #product LVV-hemorphin-7 #status experimental #label !8OPI7\ !$33-41 #product LVV-hemorphin-6 #status experimental #label !8OPI6\ !$2,3,83,144 #binding_site 2,3-diphosphoglycerate (Val, His, Lys, !8His) #status experimental\ !$2 #modified_site pyruvate 2-iminyl amino end (Val) (in !8mature form A1b) #status experimental\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status experimental\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status experimental\ !$94 #binding_site nitrosonium (Cys) (covalent) #status !8experimental SUMMARY #length 147 #molecular-weight 15998 #checksum 3588 SEQUENCE /// ENTRY HBCZ #type complete TITLE hemoglobin beta chain - chimpanzee ORGANISM #formal_name Pan troglodytes #common_name chimpanzee DATE 30-Jun-1993 #sequence_revision 10-Oct-1997 #text_change 03-Mar-2000 ACCESSIONS B93303; B90569; I56395 REFERENCE A93303 !$#authors Goodman, M.; Braunitzer, G.; Stangl, A.; Schrank, B. !$#journal Nature (1983) 303:546-548 !$#title Evidence on human origins from haemoglobins of African apes. !$#cross-references MUID:83219265; PMID:6406908 !$#accession B93303 !'##molecule_type protein !'##residues 2-147 ##label GOO REFERENCE A90569 !$#authors Rifkin, D.B.; Konigsberg, W. !$#journal Biochim. Biophys. Acta (1965) 104:457-461 !$#title The characterization of the tryptic peptides from the !1hemoglobin of the chimpanzee (Pan troglodytes). !$#cross-references MUID:66071496; PMID:5855051 !$#contents compositions and mobilities of tryptic peptides !$#accession B90569 !'##molecule_type protein !'##residues 2-147 ##label RIF REFERENCE I56395 !$#authors Savatier, P.; Trabuchet, G.; Faure, C.; Chebloune, Y.; Gouy, !1M.; Verdier, G.; Nigon, V.M. !$#journal J. Mol. Biol. (1985) 182:21-29 !$#title Evolution of the primate beta-globin gene region. High rate !1of variation in CpG dinucleotides and in short repeated !1sequences between man and chimpanzee. !$#cross-references MUID:85210896; PMID:3999143 !$#accession I56395 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-32,'VSRL',33-121 ##label RES !'##cross-references EMBL:X02345; NID:g38226; PIDN:CAA26204.1; !1PID:g38227 !'##note the insert in this sequence probably represents an incorrect !1specification of exon boundaries GENETICS !$#introns 32/3; 105/3 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$4-147 #domain globin homology #label GLB\ !$2,3,83,144 #binding_site 2,3-diphosphoglycerate (Val, His, Lys, !8His) #status predicted\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 147 #molecular-weight 15998 #checksum 3588 SEQUENCE /// ENTRY HBCZP #type complete TITLE hemoglobin beta chain - pygmy chimpanzee ORGANISM #formal_name Pan paniscus #common_name pygmy chimpanzee, bonobo DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 03-Mar-2000 ACCESSIONS D93303 REFERENCE A93303 !$#authors Goodman, M.; Braunitzer, G.; Stangl, A.; Schrank, B. !$#journal Nature (1983) 303:546-548 !$#title Evidence on human origins from haemoglobins of African apes. !$#cross-references MUID:83219265; PMID:6406908 !$#accession D93303 !'##molecule_type protein !'##residues 1-146 ##label GOO CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$1,2,82,143 #binding_site 2,3-diphosphoglycerate (Val, His, Lys, !8His) #status predicted\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15867 #checksum 1242 SEQUENCE /// ENTRY HBGO #type complete TITLE hemoglobin beta chain - gorilla ORGANISM #formal_name Gorilla gorilla #common_name gorilla DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 03-Mar-2000 ACCESSIONS S24304; F93303; A94571 REFERENCE S24304 !$#authors Perrin-Pecontal, P.; Gouy, M.; Nigon, V.M.; Trabuchet, G. !$#journal J. Mol. Evol. (1992) 34:17-30 !$#title Evolution of the primate beta-globin gene region: nucleotide !1sequence of the delta-beta-globin intergenic region of !1gorilla and phylogenetic relationships between African apes !1and man. !$#cross-references MUID:92211718; PMID:1556740 !$#accession S24304 !'##molecule_type DNA !'##residues 1-121 ##label PER !'##cross-references EMBL:X61109; NID:g22873; PIDN:CAA43421.1; !1PID:g22874 REFERENCE A93303 !$#authors Goodman, M.; Braunitzer, G.; Stangl, A.; Schrank, B. !$#journal Nature (1983) 303:546-548 !$#title Evidence on human origins from haemoglobins of African apes. !$#cross-references MUID:83219265; PMID:6406908 !$#accession F93303 !'##molecule_type protein !'##residues 2-147 ##label GOO REFERENCE A94571 !$#authors Zuckerkandl, E. !$#submission submitted to the Atlas, July 1966 !$#contents compositions and mobilities of tryptic peptides !$#accession A94571 !'##molecule_type protein !'##residues 2-147 ##label ZUC CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-147 #product hemoglobin beta chain #status experimental !8#label MAT\ !$4-147 #domain globin homology #label GLB\ !$2,3,83,144 #binding_site 2,3-diphosphoglycerate (Val, His, Lys, !8His) #status predicted\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 147 #molecular-weight 15970 #checksum 3252 SEQUENCE /// ENTRY HBGI #type complete TITLE hemoglobin beta chain - common gibbon (tentative sequence) ORGANISM #formal_name Hylobates lar #common_name common gibbon, white-handed gibbon DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 03-Mar-2000 ACCESSIONS A02353 REFERENCE A90233 !$#authors Boyer, S.H.; Crosby, E.F.; Noyes, A.N.; Fuller, G.F.; !1Leslie, S.E.; Donaldson, L.J.; Vrablik, G.R.; Schaefer Jr., !1E.W.; Thurmon, T.F. !$#journal Biochem. Genet. (1971) 5:405-448 !$#title Primate hemoglobins: some sequences and some proposals !1concerning the character of evolution and mutation. !$#cross-references MUID:72020149; PMID:4999925 !$#accession A02353 !'##molecule_type protein !'##residues 1-146 ##label BOY COMMENT A common allelic sequence has 80-Asp and 87-Lys, and an !1uncommon allelic sequence has 80-Asn and 87-Lys. CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15925 #checksum 1163 SEQUENCE /// ENTRY HBMQP #type complete TITLE hemoglobin beta chain - hanuman langur ORGANISM #formal_name Presbytis entellus #common_name hanuman langur DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS B02250; A02354 REFERENCE A02250 !$#authors Matsuda, G.; Maita, T.; Nakashima, Y.; Barnabas, J.; !1Ranjekar, P.K.; Gandhi, N.S. !$#journal Int. J. Pept. Protein Res. (1973) 5:423-425 !$#title The primary structures of the alpha and beta poly-peptide !1chains of adult hemoglobin of the hanuman langur (Presbytis !1entellus). !$#cross-references MUID:74115166; PMID:4205760 !$#accession B02250 !'##molecule_type protein !'##residues 1-146 ##label MAT CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15895 #checksum 951 SEQUENCE /// ENTRY HBMQR #type complete TITLE hemoglobin beta chain - rhesus macaque ORGANISM #formal_name Macaca mulatta #common_name rhesus macaque DATE 29-Jul-1981 #sequence_revision 29-Jul-1981 #text_change 03-Mar-2000 ACCESSIONS A02354 REFERENCE A02251 !$#authors Matsuda, G.; Maita, T.; Ota, H.; Takei, H. !$#journal Int. J. Protein Res. (1970) 2:99-108 !$#title The primary structure of the alpha and beta polypeptide !1chains of adult hemoglobin of the Rhesus monkey (Macaca !1mulatta). Biochemical studies on hemoglobins and myoglobins. !1IV. !$#cross-references MUID:75150973; PMID:4950988 !$#accession A02354 !'##molecule_type protein !'##residues 1-146 ##label MAT CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15997 #checksum 903 SEQUENCE /// ENTRY HBMQJ #type complete TITLE hemoglobin beta chain - Japanese macaque ORGANISM #formal_name Macaca fuscata fuscata #common_name Japanese macaque DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS A04622; A02354 REFERENCE A04622 !$#authors Matsuda, G.; Maita, T.; Ota, H.; Tachikawa, I.; Tanaka, Y.; !1Araya, A.; Nakashima, Y. !$#journal Int. J. Protein Res. (1971) 3:53-55 !$#title The primary structure of the beta polypeptide chain of adult !1hemoglobin of the Japanese monkey (Macaca fuscata fuscata). !$#cross-references MUID:72030553; PMID:5000512 !$#accession A04622 !'##molecule_type protein !'##residues 1-146 ##label MAT CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15983 #checksum 1233 SEQUENCE /// ENTRY HBMQPM #type complete TITLE hemoglobin beta chain - pig-tailed macaque ORGANISM #formal_name Macaca nemestrina #common_name pig-tailed macaque DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Mar-2000 ACCESSIONS S10689; S04300 REFERENCE S10689 !$#authors Nute, P.E.; Pataryas, H.A. !$#journal Am. J. Phys. Anthropol. (1974) 40:75-82 !$#title Amino acid compositions of the tryptic peptides comprising !1the beta-hemoglobin chain of Macaca nemestrina. !$#cross-references MUID:74126665; PMID:4206326 !$#accession S10689 !'##molecule_type protein !'##residues 1-146 ##label NUT CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15983 #checksum 1233 SEQUENCE /// ENTRY HBMQC #type complete TITLE hemoglobin beta chain - crab-eating macaque ORGANISM #formal_name Macaca fascicularis #common_name crab-eating macaque DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS A29665; A04623; A02354 REFERENCE A29665 !$#authors Savatier, P.; Trabuchet, G.; Chebloune, Y.; Faure, C.; !1Verdier, G.; Nigon, V.M. !$#journal J. Mol. Evol. (1987) 24:309-318 !$#title Nucleotide sequence of the beta-globin genes in gorilla and !1macaque: the origin of nucleotide polymorphisms in human. !$#cross-references MUID:87254238; PMID:3110424 !$#accession A29665 !'##status translation not shown !'##molecule_type DNA !'##residues 1-120 ##label SAV !'##cross-references EMBL:X05665; NID:g38042; PIDN:CAA29153.1; !1PID:g1333691 !'##experimental_source species designated as Macaca cynomolgus !'##note initiator Met not translated REFERENCE A04623 !$#authors Wade, P.T.; Barnicot, N.A.; Huehns, E.R. !$#journal Biochim. Biophys. Acta (1970) 221:450-466 !$#title Structural studies on the major and minor haemoglobin of the !1monkey Macaca-irus. !$#cross-references MUID:71108403; PMID:5499429 !$#accession A04623 !'##molecule_type protein !'##residues 1-146 ##label WAD GENETICS !$#introns 30/3; 104/3 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15983 #checksum 1233 SEQUENCE /// ENTRY HBMKG #type complete TITLE hemoglobin beta chain - green monkey ORGANISM #formal_name Cercopithecus aethiops #common_name green monkey, grivet DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS B02252; A02354 REFERENCE A02252 !$#authors Matsuda, G.; Maita, T.; Watanabe, B.; Araya, A.; Morokuma, !1K.; Goodman, M.; Prychodko, W. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1973) 354:1153-1155 !$#title The amino acid sequences of the alpha and beta polypeptide !1chains of adult hemoglobin of the Savannah monkey !1(Cercopithecus aethiops). !$#cross-references MUID:75040050; PMID:4214754 !$#accession B02252 !'##molecule_type protein !'##residues 1-146 ##label MAT CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15927 #checksum 1040 SEQUENCE /// ENTRY HBBAM #type complete TITLE hemoglobin beta chain - mandrill ORGANISM #formal_name Papio sphinx, Mandrillus sphinx #common_name mandrill DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 03-Mar-2000 ACCESSIONS S00540 REFERENCE S00526 !$#authors Lin, H.X.; Kleinschmidt, T.; Braunitzer, G.; Goeltenboth, R. !$#journal Biol. Chem. Hoppe-Seyler (1988) 369:209-216 !$#title The primary structure of the mandrill (Mandrillus sphinx, !1Primates) hemoglobin. !$#cross-references MUID:88293710; PMID:3401326 !$#accession S00540 !'##molecule_type protein !'##residues 1-146 ##label LIN CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15956 #checksum 1244 SEQUENCE /// ENTRY HBBAG #type complete TITLE hemoglobin beta chain - gelada baboon ORGANISM #formal_name Theropithecus gelada #common_name gelada baboon DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS A04620; A02354 REFERENCE A04620 !$#authors Hewett-Emmett, D.; Barnicot, N.A. !$#citation unpublished results, cited in Hewett-Emmett, D., Ph.D. !1thesis, University of London, 1973, cited by Yasunobu, K.T., !1and Tanaka, M., in Handbook of Biochemistry and Molecular !1Biology, 3rd ed., vol.3, Fasman, G.D., ed., pp.441-460, !1Chemical Rubber Co., Cleveland, 1976 !$#accession A04620 !'##molecule_type protein !'##residues 1-146 ##label HEW CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15925 #checksum 1034 SEQUENCE /// ENTRY HBBAY #type complete TITLE hemoglobin beta chain - yellow baboon ORGANISM #formal_name Papio cynocephalus, Papio hamadryas cynocephalus #common_name yellow baboon DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS A04624; A02354 REFERENCE A04624 !$#authors Nute, P.E.; Mahoney, W.C. !$#journal Hemoglobin (1980) 4:109-123 !$#title Complete primary structure of the beta chain from the !1hemoglobin of a baboon, Papio cynocephalus. !$#cross-references MUID:80227364; PMID:7390858 !$#accession A04624 !'##molecule_type protein !'##residues 1-146 ##label NUT CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15895 #checksum 787 SEQUENCE /// ENTRY HBMKB #type complete TITLE hemoglobin beta chain - red-crowned mangabey ORGANISM #formal_name Cercocebus torquatus #common_name red-crowned mangabey, white-collared mangabey DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS A04621; A02354 REFERENCE A04621 !$#authors Cook, C.N.; Barnicot, N.A. !$#citation unpublished results, cited in Hewett-Emmett, D., Ph.D. !1thesis, University of London, 1973, cited by Yasunobu, K.T., !1and Tanaka, M., in Handbook of Biochemistry and Molecular !1Biology, 3rd ed., vol.3, Fasman, G.D., ed., pp.441-460, !1Chemical Rubber Co., Cleveland, 1976 !$#accession A04621 !'##molecule_type protein !'##residues 1-146 ##label COO CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15995 #checksum 1055 SEQUENCE /// ENTRY HBMQB #type complete TITLE hemoglobin beta chain - red colobus ORGANISM #formal_name Colobus badius #common_name red colobus DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS B04620; A02354 REFERENCE A04620 !$#authors Hewett-Emmett, D.; Barnicot, N.A. !$#citation unpublished results, cited in Hewett-Emmett, D., Ph.D. !1thesis, University of London, 1973, cited by Yasunobu, K.T., !1and Tanaka, M., in Handbook of Biochemistry and Molecular !1Biology, 3rd ed., vol.3, Fasman, G.D., ed., pp.441-460, !1Chemical Rubber Co., Cleveland, 1976 !$#accession B04620 !'##molecule_type protein !'##residues 1-146 ##label HEW CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15870 #checksum 9975 SEQUENCE /// ENTRY HBMQF #type complete TITLE hemoglobin beta chain - brown-headed tamarin ORGANISM #formal_name Saguinus fuscicollis #common_name brown-headed tamarin, saddle-backed tamarin DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 03-Mar-2000 ACCESSIONS A02360 REFERENCE A90230 !$#authors Lin, K.D.; Kim, Y.K.; Chernoff, A.I. !$#journal Biochem. Genet. (1976) 14:427-440 !$#title Primary structure of the marmoset (Saguinus fuscicollis) !1hemoglobin. I. Use of tryptic maleylated peptides in the !1solubilization and sequence elucidation of the alpha- and !1beta-chains. !$#cross-references MUID:77021459; PMID:823937 !$#accession A02360 !'##molecule_type protein !'##residues 1-146 ##label LIN CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15914 #checksum 1706 SEQUENCE /// ENTRY HBMQN #type complete TITLE hemoglobin beta chain - black-and-red tamarin (tentative sequence) ORGANISM #formal_name Saguinus nigricollis #common_name black-and-red tamarin DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 03-Mar-2000 ACCESSIONS A02358 REFERENCE A90233 !$#authors Boyer, S.H.; Crosby, E.F.; Noyes, A.N.; Fuller, G.F.; !1Leslie, S.E.; Donaldson, L.J.; Vrablik, G.R.; Schaefer Jr., !1E.W.; Thurmon, T.F. !$#journal Biochem. Genet. (1971) 5:405-448 !$#title Primate hemoglobins: some sequences and some proposals !1concerning the character of evolution and mutation. !$#cross-references MUID:72020149; PMID:4999925 !$#accession A02358 !'##molecule_type protein !'##residues 1-146 ##label BOY CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15972 #checksum 1728 SEQUENCE /// ENTRY HBMKM #type complete TITLE hemoglobin beta chain - moustached tamarin (tentative sequence) ORGANISM #formal_name Saguinus mystax #common_name moustached tamarin DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 03-Mar-2000 ACCESSIONS A02359 REFERENCE A90233 !$#authors Boyer, S.H.; Crosby, E.F.; Noyes, A.N.; Fuller, G.F.; !1Leslie, S.E.; Donaldson, L.J.; Vrablik, G.R.; Schaefer Jr., !1E.W.; Thurmon, T.F. !$#journal Biochem. Genet. (1971) 5:405-448 !$#title Primate hemoglobins: some sequences and some proposals !1concerning the character of evolution and mutation. !$#cross-references MUID:72020149; PMID:4999925 !$#accession A02359 !'##molecule_type protein !'##residues 1-146 ##label BOY CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15958 #checksum 1685 SEQUENCE /// ENTRY HBCJB #type complete TITLE hemoglobin beta chain - black-tailed marmoset ORGANISM #formal_name Callithrix argentata #common_name black-tailed marmoset DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS S06513 REFERENCE S06512 !$#authors Maita, T.; Hayashida, M.; Matsuda, G. !$#journal J. Biochem. (1984) 95:805-813 !$#title Primary structures of adult hemoglobins of silvery marmoset, !1Callithrix argentatus, and cotton-headed tamarin, Saguinus !1oedipus. !$#cross-references MUID:84212383; PMID:6427202 !$#accession S06513 !'##molecule_type protein !'##residues 1-146 ##label MAI CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15952 #checksum 1656 SEQUENCE /// ENTRY HBMQAA #type complete TITLE hemoglobin beta chain - white-fronted capuchin ORGANISM #formal_name Cebus albifrons #common_name white-fronted capuchin, pale-fronted capuchin DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 11-May-2000 ACCESSIONS A02361 REFERENCE A02361 !$#authors Nute, P.E.; Sullivan, B. !$#journal Comp. Biochem. Physiol. B (1971) 39:797-814 !$#title Primate hemoglobins: their structure, function and !1evolution. I. Amino acid compositions of the tryptic !1peptides from the beta chain of Cebus albifrons. !$#cross-references MUID:72076589; PMID:5002362 !$#accession A02361 !'##molecule_type protein !'##residues 1-146 ##label NUT !'##note 13-Thr was found in half of the beta chains from one monkey CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15959 #checksum 1948 SEQUENCE /// ENTRY HBMQA #type complete TITLE hemoglobin beta chain - brown capuchin ORGANISM #formal_name Cebus apella #common_name brown capuchin, black-capped capuchin DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 03-Mar-2000 ACCESSIONS A02362 REFERENCE A02362 !$#authors Watanabe, B. !$#journal Seikagaku (1974) 46:255-267 !$#title Amino acid sequences of the tryptic peptides from the beta !1chain of hemoglobin of tufted capuchin monkey (Cebus !1apella). !$#cross-references MUID:75042140; PMID:4214886 !$#accession A02362 !'##molecule_type protein !'##residues 1-146 ##label WAT CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15989 #checksum 2195 SEQUENCE /// ENTRY HBMKN #type complete TITLE hemoglobin beta chain - douroucouli (tentative sequence) ORGANISM #formal_name Aotus trivirgatus #common_name douroucouli, night monkey, owl monkey DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 03-Mar-2000 ACCESSIONS A02356 REFERENCE A90233 !$#authors Boyer, S.H.; Crosby, E.F.; Noyes, A.N.; Fuller, G.F.; !1Leslie, S.E.; Donaldson, L.J.; Vrablik, G.R.; Schaefer Jr., !1E.W.; Thurmon, T.F. !$#journal Biochem. Genet. (1971) 5:405-448 !$#title Primate hemoglobins: some sequences and some proposals !1concerning the character of evolution and mutation. !$#cross-references MUID:72020149; PMID:4999925 !$#accession A02356 !'##molecule_type protein !'##residues 1-146 ##label BOY CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15898 #checksum 1255 SEQUENCE /// ENTRY HBMKP #type complete TITLE hemoglobin beta chain - black-handed spider monkey ORGANISM #formal_name Ateles geoffroyi #common_name black-handed spider monkey DATE 24-Apr-1984 #sequence_revision 28-May-1986 #text_change 03-Mar-2000 ACCESSIONS A90233; A02355 REFERENCE A90233 !$#authors Boyer, S.H.; Crosby, E.F.; Noyes, A.N.; Fuller, G.F.; !1Leslie, S.E.; Donaldson, L.J.; Vrablik, G.R.; Schaefer Jr., !1E.W.; Thurmon, T.F. !$#journal Biochem. Genet. (1971) 5:405-448 !$#title Primate hemoglobins: some sequences and some proposals !1concerning the character of evolution and mutation. !$#cross-references MUID:72020149; PMID:4999925 !$#accession A90233 !'##molecule_type protein !'##residues 1-146 ##label BOY CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15913 #checksum 1508 SEQUENCE /// ENTRY HBMKH #type complete TITLE hemoglobin beta chain - long-haired spider monkey ORGANISM #formal_name Ateles belzebuth #common_name long-haired spider monkey DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 03-Mar-2000 ACCESSIONS B90233; A02355 REFERENCE A90233 !$#authors Boyer, S.H.; Crosby, E.F.; Noyes, A.N.; Fuller, G.F.; !1Leslie, S.E.; Donaldson, L.J.; Vrablik, G.R.; Schaefer Jr., !1E.W.; Thurmon, T.F. !$#journal Biochem. Genet. (1971) 5:405-448 !$#title Primate hemoglobins: some sequences and some proposals !1concerning the character of evolution and mutation. !$#cross-references MUID:72020149; PMID:4999925 !$#accession B90233 !'##molecule_type protein !'##residues 1-146 ##label BOY CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15913 #checksum 1508 SEQUENCE /// ENTRY HBMKK #type complete TITLE hemoglobin beta chain - black spider monkey ORGANISM #formal_name Ateles paniscus #common_name black spider monkey DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 03-Mar-2000 ACCESSIONS A90034; A02355 REFERENCE A90034 !$#authors Boyer, S.H.; Crosby, E.F.; Fuller, G.F.; Noyes, A.N.; Adams, !1J.G. !$#journal Ann. N. Y. Acad. Sci. (1969) 165:360-377 !$#title The structure and biosynthesis of hemoglobins A and A-2 in !1the new world primate Ateles paniscus: a preliminary !1account. !$#cross-references MUID:70031568; PMID:4981734 !$#accession A90034 !'##molecule_type protein !'##residues 1-146 ##label BOY CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15913 #checksum 1508 SEQUENCE /// ENTRY HBMKS #type complete TITLE hemoglobin beta chain - common squirrel monkey (tentative sequence) ORGANISM #formal_name Saimiri sciureus #common_name common squirrel monkey DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 03-Mar-2000 ACCESSIONS A02357 REFERENCE A90233 !$#authors Boyer, S.H.; Crosby, E.F.; Noyes, A.N.; Fuller, G.F.; !1Leslie, S.E.; Donaldson, L.J.; Vrablik, G.R.; Schaefer Jr., !1E.W.; Thurmon, T.F. !$#journal Biochem. Genet. (1971) 5:405-448 !$#title Primate hemoglobins: some sequences and some proposals !1concerning the character of evolution and mutation. !$#cross-references MUID:72020149; PMID:4999925 !$#accession A02357 !'##molecule_type protein !'##residues 1-146 ##label BOY !'##note an allelic sequence has 76-Thr CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15912 #checksum 1341 SEQUENCE /// ENTRY HBEMA #type complete TITLE hemoglobin beta chain - Amazon manatee ORGANISM #formal_name Trichechus inunguis #common_name Amazon manatee, Brazilian manatee DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 03-Mar-2000 ACCESSIONS S00821; B24929 REFERENCE S00820 !$#authors Kleinschmidt, T.; Braunitzer, G.; Best, R. !$#journal Biol. Chem. Hoppe-Seyler (1988) 369:507-512 !$#title The primary structure of the hemoglobin of the Brazilian !1manatee (Trichechus inunguis, Sirenia). !$#cross-references MUID:89076485; PMID:3202957 !$#accession S00821 !'##molecule_type protein !'##residues 1-146 ##label KL1 REFERENCE A93060 !$#authors Kleinschmidt, T.; Czelusniak, J.; Goodman, M.; Braunitzer, !1G. !$#journal Mol. Biol. Evol. (1986) 3:427-435 !$#title Paenungulata: a comparison of the hemoglobin sequences from !1elephant, hyrax, and manatee. !$#cross-references MUID:88174362; PMID:3444412 !$#accession B24929 !'##molecule_type protein !'##residues 1-146 ##label KL2 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16179 #checksum 9180 SEQUENCE /// ENTRY HDHU #type complete TITLE hemoglobin delta chain - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Apr-1980 #sequence_revision 30-Apr-1980 #text_change 03-Mar-2000 ACCESSIONS A90804; A91678; A02363 REFERENCE A90804 !$#authors Spritz, R.A.; DeRiel, J.K.; Forget, B.G.; Weissman, S.M. !$#journal Cell (1980) 21:639-646 !$#title Complete nucleotide sequence of the human delta-globin gene. !$#cross-references MUID:81064666; PMID:7438204 !$#accession A90804 !'##molecule_type DNA !'##residues 1-146 ##label SPR !'##cross-references GB:V00505; NID:g30510; PIDN:CAA23763.1; PID:g30511 REFERENCE A91678 !$#authors Braunitzer, G.; Schrank, B.; Stangl, A.; Grillemeier, M. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1978) 359:777-783 !$#title Notiz zur Sequenz der delta Ketten der menschlichen !1Haemoglobine (Hb A-2 = alpha-2/delta-2). !$#cross-references MUID:78240319; PMID:680638 !$#accession A91678 !'##molecule_type protein !'##residues 1-146 ##label BRA GENETICS !$#gene GDB:HBD !'##cross-references GDB:119298; OMIM:142000 !$#map_position 11p15.5-11p15.5 COMPLEX two delta chains combine in heterotetramers with two alpha !1chains (see PIR:HAHU) to form adult hemoglobin A2 FUNCTION !$#description in erythrocytes binds and transports molecular oxygen from !1lung to tissues CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15924 #checksum 1414 SEQUENCE /// ENTRY HDCZ #type complete TITLE hemoglobin delta chain - chimpanzee (tentative sequence) ORGANISM #formal_name Pan troglodytes #common_name chimpanzee DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 03-Mar-2000 ACCESSIONS C90233; A93402; A02364 REFERENCE A90233 !$#authors Boyer, S.H.; Crosby, E.F.; Noyes, A.N.; Fuller, G.F.; !1Leslie, S.E.; Donaldson, L.J.; Vrablik, G.R.; Schaefer Jr., !1E.W.; Thurmon, T.F. !$#journal Biochem. Genet. (1971) 5:405-448 !$#title Primate hemoglobins: some sequences and some proposals !1concerning the character of evolution and mutation. !$#cross-references MUID:72020149; PMID:4999925 !$#accession C90233 !'##molecule_type protein !'##residues 1-146 ##label BOY REFERENCE A93402 !$#authors de Jong, W.W.W. !$#journal Nature New Biol. (1971) 234:176-177 !$#title Structure of the delta-chain of chimpanzee haemoglobin A-2. !$#cross-references MUID:72089100; PMID:5002785 !$#accession A93402 !'##molecule_type protein !'##residues 1-146 ##label DEJ CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15892 #checksum 1522 SEQUENCE /// ENTRY HDGO #type complete TITLE hemoglobin delta chain - gorilla (tentative sequence) ORGANISM #formal_name Gorilla gorilla #common_name gorilla DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 03-Mar-2000 ACCESSIONS D90233; A02364 REFERENCE A90233 !$#authors Boyer, S.H.; Crosby, E.F.; Noyes, A.N.; Fuller, G.F.; !1Leslie, S.E.; Donaldson, L.J.; Vrablik, G.R.; Schaefer Jr., !1E.W.; Thurmon, T.F. !$#journal Biochem. Genet. (1971) 5:405-448 !$#title Primate hemoglobins: some sequences and some proposals !1concerning the character of evolution and mutation. !$#cross-references MUID:72020149; PMID:4999925 !$#accession D90233 !'##molecule_type protein !'##residues 1-146 ##label BOY !'##note an allele of the gorilla sequence has 126-Ala CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15892 #checksum 1522 SEQUENCE /// ENTRY HDGI #type complete TITLE hemoglobin delta chain - gibbon (tentative sequence) ORGANISM #formal_name Hylobates sp. #common_name gibbon DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 03-Mar-2000 ACCESSIONS E90233; A02364 REFERENCE A90233 !$#authors Boyer, S.H.; Crosby, E.F.; Noyes, A.N.; Fuller, G.F.; !1Leslie, S.E.; Donaldson, L.J.; Vrablik, G.R.; Schaefer Jr., !1E.W.; Thurmon, T.F. !$#journal Biochem. Genet. (1971) 5:405-448 !$#title Primate hemoglobins: some sequences and some proposals !1concerning the character of evolution and mutation. !$#cross-references MUID:72020149; PMID:4999925 !$#accession E90233 !'##molecule_type protein !'##residues 1-146 ##label BOY !'##note a common allele of the gibbon sequence has 6- or 7-Gly CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15892 #checksum 1522 SEQUENCE /// ENTRY HDMKP #type complete TITLE hemoglobin delta chain - black-handed spider monkey ORGANISM #formal_name Ateles geoffroyi #common_name black-handed spider monkey DATE 24-Apr-1984 #sequence_revision 30-Sep-1993 #text_change 03-Mar-2000 ACCESSIONS A31523; B02365; A02365 REFERENCE A31523 !$#authors Spritz, R.A.; Giebel, L.B. !$#journal Mol. Biol. Evol. (1988) 5:21-29 !$#title The structure and evolution of the spider monkey !1delta-globin gene. !$#cross-references MUID:88189005; PMID:2833675 !$#accession A31523 !'##molecule_type DNA !'##residues 1-146 ##label SPR !'##cross-references GB:M19061; NID:g342379; PIDN:AAB00793.1; !1PID:g342380 !'##note the authors translated the codon AAG for residue 132 as Glu REFERENCE A90233 !$#authors Boyer, S.H.; Crosby, E.F.; Noyes, A.N.; Fuller, G.F.; !1Leslie, S.E.; Donaldson, L.J.; Vrablik, G.R.; Schaefer Jr., !1E.W.; Thurmon, T.F. !$#journal Biochem. Genet. (1971) 5:405-448 !$#title Primate hemoglobins: some sequences and some proposals !1concerning the character of evolution and mutation. !$#cross-references MUID:72020149; PMID:4999925 !$#accession B02365 !'##molecule_type protein !'##residues 1-4,'G',6-8,'S',10-46,'A',48-51,'D',53-146 ##label BOY !'##note three alleles of the sequence shown have 6-Lys, 9-Ala, and !169-Asp, respectively GENETICS !$#introns 30/2; 104/3 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15802 #checksum 501 SEQUENCE /// ENTRY HDMKH #type complete TITLE hemoglobin delta chain - brown-headed spider monkey (tentative sequence) ORGANISM #formal_name Ateles fusciceps #common_name brown-headed spider monkey DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 03-Mar-2000 ACCESSIONS C02365; A02365 REFERENCE A90233 !$#authors Boyer, S.H.; Crosby, E.F.; Noyes, A.N.; Fuller, G.F.; !1Leslie, S.E.; Donaldson, L.J.; Vrablik, G.R.; Schaefer Jr., !1E.W.; Thurmon, T.F. !$#journal Biochem. Genet. (1971) 5:405-448 !$#title Primate hemoglobins: some sequences and some proposals !1concerning the character of evolution and mutation. !$#cross-references MUID:72020149; PMID:4999925 !$#accession C02365 !'##molecule_type protein !'##residues 1-146 ##label BOY !'##note three alleles of the sequence shown have 6-Lys, 9-Ala, and !169-Asp, respectively CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15778 #checksum 633 SEQUENCE /// ENTRY HDMKTM #type complete TITLE hemoglobin delta chain - moustached tamarin (tentative sequence) ORGANISM #formal_name Saguinus mystax #common_name moustached tamarin DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 03-Mar-2000 ACCESSIONS D02365; A02365 REFERENCE A90233 !$#authors Boyer, S.H.; Crosby, E.F.; Noyes, A.N.; Fuller, G.F.; !1Leslie, S.E.; Donaldson, L.J.; Vrablik, G.R.; Schaefer Jr., !1E.W.; Thurmon, T.F. !$#journal Biochem. Genet. (1971) 5:405-448 !$#title Primate hemoglobins: some sequences and some proposals !1concerning the character of evolution and mutation. !$#cross-references MUID:72020149; PMID:4999925 !$#accession D02365 !'##molecule_type protein !'##residues 1-146 ##label BOY !'##note residues 16 and 12 may be Gly and Ser, respectively CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15808 #checksum 780 SEQUENCE /// ENTRY HDMKTB #type complete TITLE hemoglobin delta chain - black-and-red tamarin (tentative sequence) ORGANISM #formal_name Saguinus nigricollis #common_name black-and-red tamarin DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 03-Mar-2000 ACCESSIONS E02365; A02365 REFERENCE A90233 !$#authors Boyer, S.H.; Crosby, E.F.; Noyes, A.N.; Fuller, G.F.; !1Leslie, S.E.; Donaldson, L.J.; Vrablik, G.R.; Schaefer Jr., !1E.W.; Thurmon, T.F. !$#journal Biochem. Genet. (1971) 5:405-448 !$#title Primate hemoglobins: some sequences and some proposals !1concerning the character of evolution and mutation. !$#cross-references MUID:72020149; PMID:4999925 !$#accession E02365 !'##molecule_type protein !'##residues 1-146 ##label BOY !'##note residues 16 and 12 may be Gly and Ser, respectively CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15822 #checksum 786 SEQUENCE /// ENTRY HDMKDU #type complete TITLE hemoglobin delta chain - douroucouli (tentative sequence) ORGANISM #formal_name Aotus trivirgatus #common_name douroucouli, night monkey, owl monkey DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 03-Mar-2000 ACCESSIONS F02365; A02365 REFERENCE A90233 !$#authors Boyer, S.H.; Crosby, E.F.; Noyes, A.N.; Fuller, G.F.; !1Leslie, S.E.; Donaldson, L.J.; Vrablik, G.R.; Schaefer Jr., !1E.W.; Thurmon, T.F. !$#journal Biochem. Genet. (1971) 5:405-448 !$#title Primate hemoglobins: some sequences and some proposals !1concerning the character of evolution and mutation. !$#cross-references MUID:72020149; PMID:4999925 !$#accession F02365 !'##molecule_type protein !'##residues 1-146 ##label BOY !'##note residue 125 may be Gln and residue 127 or 131 may be Leu !'##note an allelic sequence has 120-Asn CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15721 #checksum 291 SEQUENCE /// ENTRY HDMKSQ #type complete TITLE hemoglobin delta chain - common squirrel monkey (tentative sequence) ORGANISM #formal_name Saimiri sciureus #common_name common squirrel monkey DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 03-Mar-2000 ACCESSIONS G02365; A02365 REFERENCE A90233 !$#authors Boyer, S.H.; Crosby, E.F.; Noyes, A.N.; Fuller, G.F.; !1Leslie, S.E.; Donaldson, L.J.; Vrablik, G.R.; Schaefer Jr., !1E.W.; Thurmon, T.F. !$#journal Biochem. Genet. (1971) 5:405-448 !$#title Primate hemoglobins: some sequences and some proposals !1concerning the character of evolution and mutation. !$#cross-references MUID:72020149; PMID:4999925 !$#accession G02365 !'##molecule_type protein !'##residues 1-146 ##label BOY !'##note residues 16 and 12 may be Gly and Ser, respectively. Residues !151 and 58 may be Pro and Ala, respectively !'##note an allelic sequence has 121-Gln CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15754 #checksum 4 SEQUENCE /// ENTRY HBLRS #type complete TITLE hemoglobin beta chain - slow loris ORGANISM #formal_name Nycticebus coucang #common_name slow loris DATE 24-Apr-1984 #sequence_revision 31-Dec-1991 #text_change 03-Mar-2000 ACCESSIONS A02366 REFERENCE A91767 !$#authors Matsuda, G.; Maita, T.; Watanabe, B.; Ota, H.; Araya, A.; !1Goodman, M.; Prychodko, W. !$#journal Int. J. Pept. Protein Res. (1973) 5:419-421 !$#title The primary structures of the alpha and beta polypeptide !1chains of adult hemoglobin of the slow loris (Nycticebus !1coucang). !$#cross-references MUID:74115165; PMID:4782642 !$#accession A02366 !'##molecule_type protein !'##residues 1-146 ##label MAT CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15900 #checksum 3327 SEQUENCE /// ENTRY HBLRN #type complete TITLE hemoglobin beta chain - slender loris ORGANISM #formal_name Loris tardigradus #common_name slender loris DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Mar-2000 ACCESSIONS B91949 REFERENCE A91949 !$#authors Maita, T.; Goodman, M.; Matsuda, G. !$#journal J. Biochem. (1978) 84:377-383 !$#title Amino acid sequences of the alpha and beta chains of adult !1hemoglobin of the slender loris, Loris tardigradus. !$#cross-references MUID:79027141; PMID:100490 !$#accession B91949 !'##molecule_type protein !'##residues 1-146 ##label MAI CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15900 #checksum 3426 SEQUENCE /// ENTRY HBGC #type complete TITLE hemoglobin beta-I chain - thick-tailed bush baby ORGANISM #formal_name Galago crassicaudatus, Otolemur crassicaudatus #common_name thick-tailed bush baby DATE 28-Aug-1985 #sequence_revision 31-Dec-1991 #text_change 03-Mar-2000 ACCESSIONS A02367 REFERENCE A90683 !$#authors Watanabe, B.; Fujii, T.; Nakashima, Y.; Maita, T.; Matsuda, !1G. !$#journal Biol. Chem. Hoppe-Seyler (1985) 366:265-269 !$#title Amino-acid sequences of the alpha and beta chains of adult !1hemoglobins of the grand galago, Galago crassicaudatus. !$#cross-references MUID:85225956; PMID:4005042 !$#accession A02367 !'##molecule_type protein !'##residues 1-146 ##label WAT CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15934 #checksum 1911 SEQUENCE /// ENTRY HBGC2 #type complete TITLE hemoglobin beta-II chain - thick-tailed bush baby ORGANISM #formal_name Galago crassicaudatus, Otolemur crassicaudatus #common_name thick-tailed bush baby DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Mar-2000 ACCESSIONS A90683 REFERENCE A90683 !$#authors Watanabe, B.; Fujii, T.; Nakashima, Y.; Maita, T.; Matsuda, !1G. !$#journal Biol. Chem. Hoppe-Seyler (1985) 366:265-269 !$#title Amino-acid sequences of the alpha and beta chains of adult !1hemoglobins of the grand galago, Galago crassicaudatus. !$#cross-references MUID:85225956; PMID:4005042 !$#accession A90683 !'##molecule_type protein !'##residues 1-146 ##label WAT CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15933 #checksum 2043 SEQUENCE /// ENTRY HBTB #type complete TITLE hemoglobin beta chain - western tarsier (tentative sequence) ORGANISM #formal_name Tarsius bancanus #common_name western tarsier DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 31-Mar-2000 ACCESSIONS A02368 REFERENCE A93178 !$#authors Beard, J.M.; Barnicot, N.A.; Hewett-Emmett, D. !$#journal Nature (1976) 259:338-341 !$#title Alpha and beta chains of the major haemoglobin and a note on !1the minor component of Tarsius. !$#cross-references MUID:76126211; PMID:1250373 !$#accession A02368 !'##molecule_type protein !'##residues 1-146 ##label BEA CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15862 #checksum 603 SEQUENCE /// ENTRY HBTS #type complete TITLE hemoglobin beta chain - common tree shrew (tentative sequence) ORGANISM #formal_name Tupaia glis #common_name common tree shrew DATE 31-May-1979 #sequence_revision 31-May-1979 #text_change 31-Mar-2000 ACCESSIONS A02369 REFERENCE A91944 !$#authors Maita, T.; Tanaka, E.; Goodman, M.; Matsuda, G. !$#journal J. Biochem. (1977) 82:603-605 !$#title Amino acid sequences of the alpha and beta chains of adult !1hemoglobin of the Tupai, Tupaia glis. !$#cross-references MUID:78026432; PMID:410801 !$#accession A02369 !'##molecule_type protein !'##residues 1-146 ##label MAI CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15855 #checksum 3567 SEQUENCE /// ENTRY HBLEF #type complete TITLE hemoglobin beta chain - brown lemur (tentative sequence) ORGANISM #formal_name Lemur fulvus fulvus #common_name brown lemur DATE 30-Sep-1979 #sequence_revision 30-Sep-1979 #text_change 31-Mar-2000 ACCESSIONS A02370 REFERENCE A91952 !$#authors Maita, T.; Setoguchi, M.; Matsuda, G.; Goodman, M. !$#journal J. Biochem. (1979) 85:755-764 !$#title Amino acid sequences of the alpha and beta chains of adult !1hemoglobin of the brown lemur, Lemur fulvus fulvus. !$#cross-references MUID:79150872; PMID:107155 !$#accession A02370 !'##molecule_type protein !'##residues 1-146 ##label MAI CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15770 #checksum 3404 SEQUENCE /// ENTRY HBLEC #type complete TITLE hemoglobin beta chain - ring-tailed lemur ORGANISM #formal_name Lemur catta #common_name ring-tailed lemur DATE 18-Aug-1982 #sequence_revision 17-Mar-1987 #text_change 03-Mar-2000 ACCESSIONS A02371 REFERENCE A02371 !$#authors Coppenhaver, D.H.; Dixon, J.D.; Duffy, L.K. !$#journal Hemoglobin (1983) 7:1-14 !$#title Prosimian hemoglobins I. The primary structure of the !1beta-globin chain of Lemur catta. !$#cross-references MUID:83185437; PMID:6841124 !$#accession A02371 !'##molecule_type protein !'##residues 1-146 ##label COP !'##note residues 125-131 were positioned by homology CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15981 #checksum 1431 SEQUENCE /// ENTRY S06511 #type complete TITLE hemoglobin beta chain - ruffed lemur ORGANISM #formal_name Varecia variegata #common_name ruffed lemur DATE 30-Sep-1991 #sequence_revision 03-Oct-1995 #text_change 03-Mar-2000 ACCESSIONS S06511 REFERENCE S06511 !$#authors Duffy, L.K.; Coppenhaver, D.H. !$#book Brussels hemoglobin symposium, Schneck, A.G., and Paul, C., !1eds., pp.377-392, Editions de l'Universite de Bruxelles, !1Brussels, 1984 !$#title Prosimian hemoglobins II. Comparison of hemoglobin !1beta-chain primary structures in the genus Lemur. !$#accession S06511 !'##molecule_type protein !'##residues 1-146 ##label DUF !'##note the source is designated as Lemur variegatus CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16124 #checksum 1748 SEQUENCE /// ENTRY HBRTNG #type complete TITLE hemoglobin beta chain - northern gundi ORGANISM #formal_name Ctenodactylus gundi #common_name northern gundi DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Mar-2000 ACCESSIONS S13283; C33082 REFERENCE S13282 !$#authors Beintema, J.J.; Rodewald, K.; Braunitzer, G. !$#journal Biol. Chem. Hoppe-Seyler (1990) 371:1089-1099 !$#title The primary structures of gundi (Ctenodactylus gundi, !1Rodentia) hemoglobin and myoglobin. !$#cross-references MUID:91197427; PMID:2085415 !$#accession S13283 !'##molecule_type protein !'##residues 1-146 ##label BEI CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15846 #checksum 9870 SEQUENCE /// ENTRY HBRR #type complete TITLE hemoglobin beta chain - raccoon ORGANISM #formal_name Procyon lotor #common_name raccoon DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS S06525 REFERENCE S06524 !$#authors Brimhall, B.; Stangland, K.; Jones, R.T.; Becker, R.R.; !1Bailey, T.J. !$#journal Hemoglobin (1978) 2:351-370 !$#title Amino acid sequence of the hemoglobin of raccoon (Procyon !1lotor). !$#cross-references MUID:79026831; PMID:701090 !$#accession S06525 !'##molecule_type protein !'##residues 1-146 ##label BRI CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16007 #checksum 295 SEQUENCE /// ENTRY HBBRT #type complete TITLE hemoglobin beta chain - Asiatic black bear ORGANISM #formal_name Ursus tibetanus #common_name Asiatic black bear DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Mar-2000 ACCESSIONS A90709 REFERENCE A90709 !$#authors Hofmann, O.; Schreitmuller, T.; Braunitzer, G.; Wiesner, !1M.V.H. !$#journal Biol. Chem. Hoppe-Seyler (1986) 367:53-59 !$#title The primary structure of polar bear (Ursus maritimus, !1Carnivora) and Asiatic black bear (Ursus tibetanus, !1Carnivora) hemoglobin. !$#cross-references MUID:86159301; PMID:3954890 !$#accession A90709 !'##molecule_type protein !'##residues 1-146 ##label HOF !'##note article in German with English abstract CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16009 #checksum 257 SEQUENCE /// ENTRY HBBRM #type complete TITLE hemoglobin beta chain - polar bear ORGANISM #formal_name Ursus maritimus #common_name polar bear DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Mar-2000 ACCESSIONS B25880 REFERENCE A90709 !$#authors Hofmann, O.; Schreitmuller, T.; Braunitzer, G.; Wiesner, !1M.V.H. !$#journal Biol. Chem. Hoppe-Seyler (1986) 367:53-59 !$#title The primary structure of polar bear (Ursus maritimus, !1Carnivora) and Asiatic black bear (Ursus tibetanus, !1Carnivora) hemoglobin. !$#cross-references MUID:86159301; PMID:3954890 !$#accession B25880 !'##molecule_type protein !'##residues 1-146 ##label HOF !'##note article in German with English abstract CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16009 #checksum 257 SEQUENCE /// ENTRY HBBD #type complete TITLE hemoglobin beta chain - Eurasian badger (tentative sequence) ORGANISM #formal_name Meles meles #common_name Eurasian badger DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 31-Mar-2000 ACCESSIONS A02372 REFERENCE A02372 !$#authors Hombrados, I.; Ducastaing, S.; Iron, A.; Neuzil, E.; !1Debuire, B.; Han, K.K. !$#journal Biochim. Biophys. Acta (1976) 427:107-118 !$#title Primary sequence of the beta-chain of badger haemoglobin. !$#cross-references MUID:76161287; PMID:1259993 !$#accession A02372 !'##molecule_type protein !'##residues 1-146 ##label HOM CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16010 #checksum 2193 SEQUENCE /// ENTRY HBFQL #type complete TITLE hemoglobin beta chain - lesser panda ORGANISM #formal_name Ailurus fulgens #common_name lesser panda DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS S06527 REFERENCE S06526 !$#authors Tagle, D.A.; Miyamoto, M.M.; Goodman, M.; Hofmann, O.; !1Braunitzer, G.; Goeltenboth, R.; Jalanka, H. !$#journal Naturwissenschaften (1986) 73:512-514 !$#title Hemoglobin of pandas: phylogenetic relationships of !1carnivores as ascertained with protein sequence data. !$#cross-references MUID:87014854; PMID:3762727 !$#accession S06527 !'##molecule_type protein !'##residues 1-146 ##label TAG CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15950 #checksum 1268 SEQUENCE /// ENTRY HBFQG #type complete TITLE hemoglobin beta chain - giant panda ORGANISM #formal_name Ailuropoda melanoleuca #common_name giant panda DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS S06529 REFERENCE S06526 !$#authors Tagle, D.A.; Miyamoto, M.M.; Goodman, M.; Hofmann, O.; !1Braunitzer, G.; Goeltenboth, R.; Jalanka, H. !$#journal Naturwissenschaften (1986) 73:512-514 !$#title Hemoglobin of pandas: phylogenetic relationships of !1carnivores as ascertained with protein sequence data. !$#cross-references MUID:87014854; PMID:3762727 !$#accession S06529 !'##molecule_type protein !'##residues 1-146 ##label TAG CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16021 #checksum 1710 SEQUENCE /// ENTRY HBMN #type complete TITLE hemoglobin beta chain - domestic ferret ORGANISM #formal_name Mustela putorius furo #common_name domestic ferret DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 03-Mar-2000 ACCESSIONS S11534 REFERENCE S11534 !$#authors Pauplin, Y.; Hombrados, I.; Faure, F.; Han, K.K.; Neuzil, E. !$#journal Biochem. Soc. Trans. (1988) 16:608-609 !$#title The primary structure of the beta-chain of the haemoglobins !1of the ferret (Mustela putorius furo). !$#accession S11534 !'##molecule_type protein !'##residues 1-146 ##label PAU CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15994 #checksum 2183 SEQUENCE /// ENTRY HBOTE #type complete TITLE hemoglobin beta chain - Eurasian river otter ORGANISM #formal_name Lutra lutra #common_name Eurasian river otter DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 03-Mar-2000 ACCESSIONS S00817 REFERENCE S00816 !$#authors Lin, H.X.; Kleinschmidt, T.; Braunitzer, G.; Scheil, H.G. !$#journal Biol. Chem. Hoppe-Seyler (1988) 369:349-355 !$#title Carnivora: the primary structure of the common otter (Lutra !1lutra, Mustelidae) hemoglobin. !$#cross-references MUID:89000194; PMID:3166739 !$#accession S00817 !'##molecule_type protein !'##residues 1-146 ##label LIN CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15950 #checksum 1232 SEQUENCE /// ENTRY HBOTG #type complete TITLE hemoglobin beta chain - giant otter ORGANISM #formal_name Pteronura brasiliensis #common_name giant otter DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS S02081 REFERENCE S02080 !$#authors Kleinschmidt, T.; Braunitzer, G.; Scheil, H.G. !$#journal Biol. Chem. Hoppe-Seyler (1989) 370:35-40 !$#title Carnivora: the primary structure of the giant otter !1(Pteronura brasiliensis, Mustelidae) hemoglobin. !$#cross-references MUID:89228546; PMID:2713096 !$#accession S02081 !'##molecule_type protein !'##residues 1-146 ##label KLE CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15934 #checksum 998 SEQUENCE /// ENTRY HBMNE #type complete TITLE hemoglobin beta chain - European mink ORGANISM #formal_name Mustela lutreola #common_name European mink DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 11-May-2000 ACCESSIONS S10105 REFERENCE S10104 !$#authors Ahmed, A.; Jahan, M.; Braunitzer, G. !$#journal Z. Naturforsch. C (1990) 45:223-228 !$#title Carnivora: the amino acid sequence of the adult European !1mink (Mustela lutreola, Mustelidae) hemoglobins. !$#cross-references MUID:90303485; PMID:2363790 !$#accession S10105 !'##molecule_type protein !'##residues 1-146 ##label AHM CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15935 #checksum 1118 SEQUENCE /// ENTRY HBUKE #type complete TITLE hemoglobin beta chain - European polecat ORGANISM #formal_name Mustela putorius #common_name European polecat DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 03-Mar-2000 ACCESSIONS S10103 REFERENCE S10102 !$#authors Ahmed, A.; Jahan, M.; Braunitzer, G.; Pechlaner, H. !$#journal Z. Naturforsch. B (1989) 44:817-824 !$#title Carnivora: the amino acid sequence of the adult European !1polecat (Mustela putorius, Mustelidae) hemoglobins. !$#accession S10103 !'##molecule_type protein !'##residues 1-146 ##label AHM CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15994 #checksum 1910 SEQUENCE /// ENTRY HBBDR #type complete TITLE hemoglobin beta chain - ratel ORGANISM #formal_name Mellivora capensis #common_name ratel DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS S01663 REFERENCE S01662 !$#authors Rodewald, K.; Braunitzer, G.; Goeltenboth, R. !$#journal Biol. Chem. Hoppe-Seyler (1988) 369:1137-1142 !$#title Carnivora: primary structure of the hemoglobins from ratel !1(Mellivora capensis). !$#cross-references MUID:89207098; PMID:3242544 !$#accession S01663 !'##molecule_type protein !'##residues 1-146 ##label ROD CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15948 #checksum 968 SEQUENCE /// ENTRY HBBDBM #type complete TITLE hemoglobin beta chain - beech marten ORGANISM #formal_name Martes foina #common_name beech marten DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 03-Mar-2000 ACCESSIONS S10599 REFERENCE S10598 !$#authors Ruecknagel, K.P.; Wiesner, H.; Braunitzer, G. !$#journal Biol. Chem. Hoppe-Seyler (1990) 371:503-509 !$#title Carnivora: the primary structure of the beech marten (Martes !1foina, Mustelidae) hemoglobin. !$#cross-references MUID:90359058; PMID:2390216 !$#accession S10599 !'##molecule_type protein !'##residues 1-146 ##label BIO CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15934 #checksum 998 SEQUENCE /// ENTRY HBUW #type complete TITLE hemoglobin beta chain - Pacific walrus ORGANISM #formal_name Odobenus rosmarus divergens #common_name Pacific walrus DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS S02820 REFERENCE S02819 !$#authors Lin, H.X.; Kleinschmidt, T.; Johnson, M.L.; Braunitzer, G. !$#journal Biol. Chem. Hoppe-Seyler (1989) 370:135-140 !$#title Carnivora: the primary structure of the Pacific walrus !1(Odobenus rosmarus divergens, Pinnipedia) hemoglobin. !$#cross-references MUID:89207123; PMID:2706084 !$#accession S02820 !'##molecule_type protein !'##residues 1-146 ##label LIN CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15920 #checksum 946 SEQUENCE /// ENTRY B61434 #type complete TITLE hemoglobin beta chain - Galapagos fur seal ORGANISM #formal_name Arctocephalus galapagoensis #common_name Galapagos fur seal DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS B61434 REFERENCE A61434 !$#authors Jahan, M.; Ahmed, A.; Trillmich, F.; Braunitzer, G. !$#journal J. Protein Chem. (1991) 10:257-263 !$#title The complete primary structure of the marine carnivora, !1Galapagoes fur seal (Arctocephalus galapagoensis, Otariidae) !1hemoglobins. !$#cross-references MUID:92000163; PMID:1910457 !$#accession B61434 !'##molecule_type protein !'##residues 1-146 ##label JAH CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15920 #checksum 946 SEQUENCE /// ENTRY HBSLW #type complete TITLE hemoglobin beta chain - Weddell seal ORGANISM #formal_name Leptonychotes weddelli #common_name Weddell seal DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS S04952 REFERENCE S04951 !$#authors Lin, H.; Kleinschmidt, T.; Braunitzer, G.; Scheil, H.G. !$#journal Biol. Chem. Hoppe-Seyler (1989) 370:707-713 !$#title Carnivora: the primary structure of Weddell seal !1(Leptonychotes weddelli, Pinnipedia) hemoglobin. !$#cross-references MUID:89374816; PMID:2775492 !$#accession S04952 !'##molecule_type protein !'##residues 1-146 ##label LIN CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15993 #checksum 1832 SEQUENCE /// ENTRY HBDD #type complete TITLE hemoglobin beta chain - bottle-nosed dolphin ORGANISM #formal_name Tursiops truncatus #common_name bottle-nosed dolphin DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS S06523 REFERENCE S06522 !$#authors Kleinschmidt, T.; Braunitzer, G. !$#journal Biomed. Biochim. Acta (1983) 42:685-695 !$#title The primary structure of the bottlenosed dolphin (Tursiops !1truncatus, Cetacea) hemoglobin. !$#cross-references MUID:84052510; PMID:6639644 !$#accession S06523 !'##molecule_type protein !'##residues 1-146 ##label KLE !'##note article in German with English abstract CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16035 #checksum 1395 SEQUENCE /// ENTRY HBWHK #type complete TITLE hemoglobin beta chain - minke whale ORGANISM #formal_name Balaenoptera acutorostrata #common_name minke whale, lesser rorqual DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS S06521 REFERENCE S06520 !$#authors Abbasi, A.; Rucknagel, P.; Matsuda, G.; Zaidi, Z.H.; !1Braunitzer, G. !$#journal J. Chem. Soc. Pak. (1984) 6:253-256 !$#title The primary structure of Minke-whale (Balenoptera !1acutorosterata - Cetacea) hemoglobin. !$#accession S06521 !'##molecule_type protein !'##residues 1-146 ##label ABB !'##note 72-Ala, 87-Ala, 123-Leu, and 128-Ser were also found CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16061 #checksum 9990 SEQUENCE /// ENTRY HBBTV #type complete TITLE hemoglobin beta chain - false vampire bat (Megaderma lyra) ORGANISM #formal_name Megaderma lyra DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS S00541 REFERENCE S00524 !$#authors Sgouros, J.G.; Kleinschmidt, T.; Braunitzer, G. !$#journal Biol. Chem. Hoppe-Seyler (1988) 369:47-53 !$#title The primary structure of the hemoglobin of the Indian false !1vampire (Megaderma lyra, Microchiroptera). !$#cross-references MUID:88163088; PMID:3348887 !$#accession S00541 !'##molecule_type protein !'##residues 1-146 ##label SGO CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16145 #checksum 1136 SEQUENCE /// ENTRY HBHZS #type complete TITLE hemoglobin beta chain - spotted hyena ORGANISM #formal_name Crocuta crocuta #common_name spotted hyena DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS S04221 REFERENCE S04220 !$#authors He, C.; Rodewald, K.; Braunitzer, G.; Goeltenboth, R. !$#journal Biol. Chem. Hoppe-Seyler (1989) 370:417-423 !$#title Carnivora: primary structure of the hemoglobin from the !1spotted hyena (Crocuta crocuta, Hyenidae). !$#cross-references MUID:89302684; PMID:2742752 !$#accession S04221 !'##molecule_type protein !'##residues 1-146 ##label HEC CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16017 #checksum 53 SEQUENCE /// ENTRY HBPD #type complete TITLE hemoglobin beta chain - Amur leopard ORGANISM #formal_name Panthera pardus orientalis #common_name Amur leopard DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 03-Mar-2000 ACCESSIONS A02373 REFERENCE A92977 !$#authors Abbasi, A.; Braunitzer, G. !$#journal J. Protein Chem. (1985) 4:57-67 !$#title The primary structure of haemoglobin from amur-leopard !1(Panthera pardus orientalis). !$#accession A02373 !'##molecule_type protein !'##residues 1-146 ##label ABB COMMENT In the cat family (Felidae), the oxygen affinity of !1hemoglobin depends little or not at all on the association !1with diphosphoglycerate (DPG). CLASSIFICATION #superfamily globin; globin homology KEYWORDS acetylated amino end; blood; chromoprotein; erythrocyte; !1heme; iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$1 #modified_site acetylated amino end (Ser) #status !8experimental\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15986 #checksum 465 SEQUENCE /// ENTRY HBPD2P #type complete TITLE hemoglobin beta-II chain - northern Persian leopard ORGANISM #formal_name Panthera pardus saxicolor #common_name northern Persian leopard DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS S03929 REFERENCE S03927 !$#authors Ahmed, A.; Jahan, M.; Braunitzer, G.; Goeltenboth, R. !$#journal Z. Naturforsch. B (1988) 43:1341-1346 !$#title Carnivora: the primary structure of the major and minor !1hemoglobin components of adult north Persian leopard !1(Panthera pardus sexicolor). !$#accession S03929 !'##molecule_type protein !'##residues 1-146 ##label AHM CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15928 #checksum 312 SEQUENCE /// ENTRY HBJL2 #type complete TITLE hemoglobin beta-II chain - lion ORGANISM #formal_name Panthera leo #common_name lion DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS S03926 REFERENCE S03924 !$#authors Jahan, M.; Ahmed, A.; Braunitzer, G.; Zaidi, Z.H.; !1Goeltenboth, R. !$#journal Z. Naturforsch. B (1987) 42:1465-1470 !$#title Carnivora: the primary structures of adult lion (Panthera !1leo) hemoglobins. !$#accession S03926 !'##molecule_type protein !'##residues 1-146 ##label JAH CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15928 #checksum 312 SEQUENCE /// ENTRY HBJU #type complete TITLE hemoglobin beta-I chain - jaguar ORGANISM #formal_name Panthera onca #common_name jaguar DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 03-Mar-2000 ACCESSIONS S00522 REFERENCE S00521 !$#authors Ahmed, A.; Jahan, M.; Zaidi, Z.H.; Braunitzer, G.; !1Goeltenboth, R. !$#journal Biol. Chem. Hoppe-Seyler (1987) 368:1385-1390 !$#title The primary structure of the hemoglobins of the adult jaguar !1(Panthera onco, Carnivora). !$#cross-references MUID:88107004; PMID:3426807 !$#accession S00522 !'##molecule_type protein !'##residues 1-146 ##label AHM !'##note the sequence of the beta-II chain differs from that shown in !1having 1-Gly and 139-Lys CLASSIFICATION #superfamily globin; globin homology KEYWORDS acetylated amino end; blood; chromoprotein; erythrocyte; !1heme; heterotetramer; iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$1 #modified_site acetylated amino end (Ser) #status !8experimental\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15986 #checksum 534 SEQUENCE /// ENTRY HBTX1 #type complete TITLE hemoglobin beta-I chain - tiger ORGANISM #formal_name Panthera tigris sumatrae #common_name Sumatran tiger DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS S02079 REFERENCE S02078 !$#authors Jahan, M.; Ahmed, A.; Braunitzer, G.; Goeltenboth, R. !$#journal Biol. Chem. Hoppe-Seyler (1989) 370:27-33 !$#title Carnivora: the amino-acid sequence of the adult Sumatran !1tiger (Panthera tigris sumatrae) hemoglobins. !$#cross-references MUID:89228545; PMID:2713095 !$#accession S02079 !'##molecule_type protein !'##residues 1-146 ##label JAH CLASSIFICATION #superfamily globin; globin homology KEYWORDS acetylated amino end; blood; chromoprotein; erythrocyte; !1heme; heterotetramer; iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$1 #modified_site acetylated amino end (Ser) #status !8experimental\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15986 #checksum 534 SEQUENCE /// ENTRY HBJL1 #type complete TITLE hemoglobin beta-I chain - lion ORGANISM #formal_name Panthera leo #common_name lion DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS S03925 REFERENCE S03924 !$#authors Jahan, M.; Ahmed, A.; Braunitzer, G.; Zaidi, Z.H.; !1Goeltenboth, R. !$#journal Z. Naturforsch. B (1987) 42:1465-1470 !$#title Carnivora: the primary structures of adult lion (Panthera !1leo) hemoglobins. !$#accession S03925 !'##molecule_type protein !'##residues 1-146 ##label JAH CLASSIFICATION #superfamily globin; globin homology KEYWORDS acetylated amino end; blood; chromoprotein; erythrocyte; !1heme; heterotetramer; iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$1 #modified_site acetylated amino end (Ser) #status !8experimental\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15986 #checksum 534 SEQUENCE /// ENTRY HBPD1P #type complete TITLE hemoglobin beta-I chain - northern Persian leopard ORGANISM #formal_name Panthera pardus saxicolor #common_name northern Persian leopard DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS S03928 REFERENCE S03927 !$#authors Ahmed, A.; Jahan, M.; Braunitzer, G.; Goeltenboth, R. !$#journal Z. Naturforsch. B (1988) 43:1341-1346 !$#title Carnivora: the primary structure of the major and minor !1hemoglobin components of adult north Persian leopard !1(Panthera pardus sexicolor). !$#accession S03928 !'##molecule_type protein !'##residues 1-146 ##label AHM CLASSIFICATION #superfamily globin; globin homology KEYWORDS acetylated amino end; blood; chromoprotein; erythrocyte; !1heme; heterotetramer; iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$1 #modified_site acetylated amino end (Ser) #status !8experimental\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15986 #checksum 534 SEQUENCE /// ENTRY HBTX2 #type complete TITLE hemoglobin beta-II chain - tiger ORGANISM #formal_name Panthera tigris sumatrae #common_name Sumatran tiger DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS S11301 REFERENCE S02078 !$#authors Jahan, M.; Ahmed, A.; Braunitzer, G.; Goeltenboth, R. !$#journal Biol. Chem. Hoppe-Seyler (1989) 370:27-33 !$#title Carnivora: the amino-acid sequence of the adult Sumatran !1tiger (Panthera tigris sumatrae) hemoglobins. !$#cross-references MUID:89228545; PMID:2713095 !$#accession S11301 !'##molecule_type protein !'##residues 1-146 ##label JAH CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15928 #checksum 312 SEQUENCE /// ENTRY HBDG #type complete TITLE hemoglobin beta chain - dog ORGANISM #formal_name Canis lupus familiaris #common_name dog DATE 24-Apr-1984 #sequence_revision 31-Dec-1991 #text_change 03-Mar-2000 ACCESSIONS A02374 REFERENCE A92970 !$#authors Brimhall, B.; Duerst, M.; Jones, R.T. !$#journal J. Mol. Evol. (1977) 9:231-235 !$#title The amino acid sequence of dog (Canis familiaris) !1hemoglobin. !$#cross-references MUID:77190158; PMID:864726 !$#accession A02374 !'##molecule_type protein !'##residues 1-146 ##label BRI CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15996 #checksum 1568 SEQUENCE /// ENTRY HBDGY #type complete TITLE hemoglobin beta chain - coyote (tentative sequence) ORGANISM #formal_name Canis latrans #common_name coyote DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Mar-2000 ACCESSIONS B90227 REFERENCE A90227 !$#authors Runkel, D.; Dresler, S.L.; Brimhall, B.; Jones, R.T. !$#journal Biochem. Genet. (1974) 12:467-473 !$#title The tryptic peptide of coyote (Canis latrans) hemoglobin. !$#cross-references MUID:75145794; PMID:4458658 !$#accession B90227 !'##molecule_type protein !'##residues 1-146 ##label RUN CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15996 #checksum 1568 SEQUENCE /// ENTRY HBRB #type complete TITLE hemoglobin beta chain - rabbit CONTAINS hemoglobin beta chain, allele 1; hemoglobin beta chain, allele 2 ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 24-Apr-1984 #sequence_revision 13-Mar-1997 #text_change 16-Jun-2000 ACCESSIONS I46476; A90774; I46723; I46724; A94249; A90785; I46728; !1S03090; I46721; I46725; I46726; I46722; I46720; A91646; !1A02375 REFERENCE I46476 !$#authors Kafatos, F.C.; Efstratiadis, A.; Forget, B.G.; Weissman, !1S.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1977) 74:5618-5622 !$#title Molecular evolution of human and rabbit beta-globin mRNAs. !$#cross-references MUID:78094461; PMID:271989 !$#accession I46476 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-147 ##label KAF !'##cross-references EMBL:V00879; NID:g1484; PIDN:CAA24248.1; PID:g1485 REFERENCE A90774 !$#authors Efstratiadis, A.; Kafatos, F.C.; Maniatis, T. !$#journal Cell (1977) 10:571-585 !$#title The primary structure of rabbit beta-globin mRNA as !1determined from cloned DNA. !$#cross-references MUID:77183599; PMID:558827 !$#accession A90774 !'##molecule_type DNA !'##residues 2-147 ##label EFS !'##cross-references GB:J00659; NID:g165074; PIDN:AAA31273.1; !1PID:g165075 !'##experimental_source allele 1 !'##note translation of initiator Met is not shown REFERENCE I46723 !$#authors van den Berg, J.; van Ooyen, A.; Mantei, N.; Schamboeck, A.; !1Grosveld, G.; Flavell, R.A.; Weissmann, C. !$#journal Nature (1978) 276:37-44 !$#title Comparison of cloned rabbit and mouse beta-globin genes !1showing strong evolutionary divergence of two homologous !1pairs of introns. !$#cross-references MUID:79114395; PMID:264241 !$#accession I46723 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 28-42 ##label VAN1 !'##cross-references GB:M10831; NID:g165068; PIDN:AAA31271.1; !1PID:g552376 !$#accession I46724 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 100-115 ##label VAN2 !'##cross-references GB:M10833; NID:g165070; PIDN:AAA31272.1; !1PID:g165073 REFERENCE A94249 !$#authors van Ooyen, A.; van den Berg, J.; Mantei, N.; Weissmann, C. !$#journal Science (1979) 206:337-344 !$#title Comparison of total sequence of a cloned rabbit beta-globin !1gene and its flanking regions with a homologous mouse !1sequence. !$#cross-references MUID:80014491; PMID:482942 !$#accession A94249 !'##molecule_type DNA !'##residues 2-147 ##label VANO !'##cross-references GB:V00882; NID:g1489; PIDN:CAA24251.1; PID:g1632820 !'##experimental_source allele 1 !'##note translation of initiator Met is not shown REFERENCE A90785 !$#authors Hardison, R.C.; Butler III, E.T.; Lacy, E.; Maniatis, T.; !1Rosenthal, N.; Efstratiadis, A. !$#journal Cell (1979) 18:1285-1297 !$#title The structure and transcription of four linked rabbit !1beta-like globin genes. !$#cross-references MUID:80090069; PMID:519769 !$#accession A90785 !'##molecule_type DNA !'##residues 2-52,'H',54-56,'S',58-76,'N',78-112,'V',114-147 ##label HAR !'##cross-references GB:V00878; NID:g1482; PIDN:CAA24247.1; PID:g1483 !'##experimental_source allele 2 !'##note translation of initiator Met is not shown; this sequence !1represents the second most common allelic variant REFERENCE I46718 !$#authors Vary, C.P.H.; Vournakis, J.N. !$#journal J. Biol. Chem. (1984) 259:3299-3307 !$#title RNase H-catalyzed site-specific deadenylylation of rabbit !1alpha- and beta-globin mRNAs: Secondary structure of !13'-noncoding regions. !$#cross-references MUID:84135843; PMID:6321504 !$#accession I46728 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 106-112,'V',114-147 ##label VAR !'##cross-references GB:M12540; NID:g165089; PIDN:AAA72520.1; !1PID:g165090 REFERENCE S03088 !$#authors Margot, J.B.; Demers, G.W.; Hardison, R.C. !$#journal J. Mol. Biol. (1989) 205:15-40 !$#title Complete nucleotide sequence of the rabbit beta-like globin !1gene cluster. Analysis of intergenic sequences and !1comparison with the human beta-like globin gene cluster. !$#cross-references MUID:89178632; PMID:2486295 !$#accession S03090 !'##status translation not shown !'##molecule_type DNA !'##residues 1-52,'H',54-56,'S',58-76,'N',78-112,'V',114-147 ##label MAR !'##cross-references GB:M18818; GB:X07786; GB:X07787; GB:X07788; !1NID:g164790; PIDN:AAA02985.1; PID:g164793 !'##experimental_source allele 2 REFERENCE I46721 !$#authors Proudfoot, N.J.; Brownlee, G.G. !$#journal Br. Med. Bull. (1976) 32:251-256 !$#title Nucleotide sequences of globin messenger RNA. !$#cross-references MUID:77022845; PMID:788834 !$#accession I46721 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 108-112,'V',114-138 ##label PRO1 !'##cross-references GB:M24885; NID:g165059; PIDN:AAA31269.1; !1PID:g165062 !'##note 113-Ile was also seen REFERENCE I46725 !$#authors Proudfoot, N.J. !$#journal Nucleic Acids Res. (1976) 3:1811-1821 !$#title Nucleotide sequence from the coding region of rabbit !1beta-globin messenger RNA. !$#cross-references MUID:77012983; PMID:61580 !$#accession I46725 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 109-112,'V',114-137 ##label PRO2 !'##cross-references GB:M10885; NID:g165078; PIDN:AAA31275.1; !1PID:g552377 !'##note 113-Ile was also seen REFERENCE I46726 !$#authors Browne, J.K.; Paddock, G.V.; Liu, A.; Clarke, P.; Heindell, !1H.C.; Salser, W. !$#journal Science (1977) 195:389-391 !$#title Nucleotide sequences from the rabbit beta globin gene !1inserted into Escherichia coli plasmids. !$#cross-references MUID:77081055; PMID:318762 !$#accession I46726 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 94-112,'V',114-121,'NSLLRCRLPIRRWWLVWPMPWPQIP' ##label BRO !'##cross-references GB:M10847; NID:g165080; PIDN:AAA31276.1; !1PID:g552378 !'##note the sequence in GenBank entry RABHBBB, release 103, !1(PID:g552378) inserts a G (meant as an observed !1heterogeneous nucleotide) in the published sequence after !1nucleotide 83, corresponding to peptide position 121; the !1translation of the published sequence agrees with that shown !1for 94-147 except for 113 REFERENCE I41430 !$#authors Sim, G.K.; Efstratiadis, A.; Jones, C.W.; Kafatos, F.C.; !1Koehler, M.; Kronenberg, H.M.; Maniatis, T.; Regier, J.C.; !1Roberts, B.F.; Rosenthal, N. !$#journal Cold Spring Harb. Symp. Quant. Biol. (1978) 42:933-945 !$#title Studies on the structure of genes expressed during !1development. !$#cross-references MUID:78237860; PMID:277327 !$#accession I46722 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-147 ##label SIM !'##cross-references GB:M10843; NID:g165066; PIDN:AAA31270.1; !1PID:g165067 REFERENCE I46716 !$#authors Pavlakis, G.N.; Lockard, R.E.; Vamvakopoulos, N.; Rieser, !1L.; RajBhandary, U.L.; Vournakis, J.N. !$#journal Cell (1980) 19:91-102 !$#title Secondary structure of mouse and rabbit alpha- and !1beta-globin mRNAs: Differential accessibility of alpha and !1beta initiator AUG codons towards nucleases. !$#cross-references MUID:80132479; PMID:7357610 !$#accession I46720 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-62 ##label PAV !'##cross-references GB:M10525; NID:g165057; PIDN:AAA31268.1; !1PID:g552375 REFERENCE A91646 !$#authors Best, J.S.; Flamm, U.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1969) 350:563-580 !$#title The primary structure of the beta-chain of rabbit !1haemoglobin. !$#cross-references MUID:69219353; PMID:5789874 !$#accession A91646 !'##molecule_type protein !'##residues 2-147 ##label BES !'##experimental_source allele 1 REFERENCE A90035 !$#authors Garrick, M.D.; Hafner, R.; Bricker, J.; Garrick, L.M. !$#journal Ann. N. Y. Acad. Sci. (1974) 241:436-438 !$#title Discussion paper: genetic variation in the primary structure !1of the beta chain of rabbit hemoglobin. !$#cross-references MUID:75053122; PMID:4530669 !$#contents annotation !$#note these authors investigated the occurrence and frequency of !1allelic chains; the most common type of beta chain found !1corresponded to that shown; the second common type had !153-His, 57-Ser, 77-Asn, and 113-Val GENETICS !$#introns 31/2; 105/3 COMPLEX Two beta chains combine to form heterotetramers with two !1alpha chains FUNCTION !$#description in erythrocytes binds and transports molecular oxygen from !1lung to tissues CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-147 #product hemoglobin beta chain, allele 1 #status !8experimental #label MAT1\ !$2-52,'H',54-56,'S', !$58-76,'N',78-112, !$'V',114-147 #product hemoglobin beta chain, allele 2 #status !8experimental #label MAT2\ !$4-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 147 #molecular-weight 16132 #checksum 4125 SEQUENCE /// ENTRY HBBTF #type complete TITLE hemoglobin beta chain - Egyptian rousette (tentative sequence) ORGANISM #formal_name Rousettus aegyptiacus #common_name Egyptian rousette DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 31-Mar-2000 ACCESSIONS A02376 REFERENCE A91702 !$#authors Kleinschmidt, T.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1982) 363:1209-1215 !$#title Die Primaerstruktur des Haemoglobins vom Aegyptischen !1Flughund (Rousettus aegyptiacus, Chiroptera). !$#cross-references MUID:83055089; PMID:7141404 !$#accession A02376 !'##molecule_type protein !'##residues 1-146 ##label KLE CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15955 #checksum 2133 SEQUENCE /// ENTRY HBFXB #type complete TITLE hemoglobin beta chain - black flying fox ORGANISM #formal_name Pteropus alecto #common_name black flying fox DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS S01309 REFERENCE S01308 !$#authors Kleinschmidt, T.; Sgouros, J.G.; Pettigrew, J.D.; !1Braunitzer, G. !$#journal Biol. Chem. Hoppe-Seyler (1988) 369:975-984 !$#title The primary structure of the hemoglobin from the grey-headed !1flying fox (Pteropus poliocephalus) and the black flying fox !1(P. alecto, Megachiroptera). !$#cross-references MUID:89149963; PMID:3228493 !$#accession S01309 !'##molecule_type protein !'##residues 1-146 ##label KLE !'##note 139-Thr was also found CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15937 #checksum 1253 SEQUENCE /// ENTRY HBFXG #type complete TITLE hemoglobin beta chain - gray-headed flying fox ORGANISM #formal_name Pteropus poliocephalus #common_name gray-headed flying fox DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS S01311 REFERENCE S01308 !$#authors Kleinschmidt, T.; Sgouros, J.G.; Pettigrew, J.D.; !1Braunitzer, G. !$#journal Biol. Chem. Hoppe-Seyler (1988) 369:975-984 !$#title The primary structure of the hemoglobin from the grey-headed !1flying fox (Pteropus poliocephalus) and the black flying fox !1(P. alecto, Megachiroptera). !$#cross-references MUID:89149963; PMID:3228493 !$#accession S01311 !'##molecule_type protein !'##residues 1-146 ##label KLE !'##note 139-Thr was also found CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15947 #checksum 1097 SEQUENCE /// ENTRY HBHH #type complete TITLE hemoglobin beta chain - western European hedgehog (tentative sequence) ORGANISM #formal_name Erinaceus europaeus #common_name western European hedgehog DATE 30-Jun-1979 #sequence_revision 30-Jun-1979 #text_change 31-Mar-2000 ACCESSIONS A02377 REFERENCE A91950 !$#authors Maita, T.; Araya, A.; Matsuda, G.; Goodman, M. !$#journal J. Biochem. (1979) 85:259-269 !$#title Amino acid sequences of the alpha and beta chains of adult !1hemoglobin of the European hedgehog, Erinaceus europaeus. !$#cross-references MUID:79109529; PMID:762046 !$#accession A02377 !'##molecule_type protein !'##residues 1-146 ##label MAI CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15805 #checksum 9720 SEQUENCE /// ENTRY HBTSM #type complete TITLE hemoglobin beta chain - house shrew (tentative sequence) ORGANISM #formal_name Suncus murinus #common_name house shrew DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 31-Mar-2000 ACCESSIONS A02378 REFERENCE A91699 !$#authors Maita, T.; Matsuda, G.; Takenaka, O.; Takahashi, K. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1981) 362:1465-1474 !$#title The primary structure of adult hemoglobin of musk shrew !1(Suncus murinus). !$#cross-references MUID:82074278; PMID:7309005 !$#accession A02378 !'##molecule_type protein !'##residues 1-146 ##label MAI CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15734 #checksum 1529 SEQUENCE /// ENTRY HBOEE #type complete TITLE hemoglobin beta chain - European mole (tentative sequence) ORGANISM #formal_name Talpa europaea #common_name European mole DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 31-Mar-2000 ACCESSIONS A02379 REFERENCE A91697 !$#authors Kleinschmidt, T.; Jelkmann, W.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1981) 362:1263-1272 !$#title Die Primaerstruktur des Haemoglobins des Maulwurfs (Talpa !1europaea). !$#cross-references MUID:82263326; PMID:7346384 !$#accession A02379 !'##molecule_type protein !'##residues 1-146 ##label KLE CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15787 #checksum 1396 SEQUENCE /// ENTRY HBHO #type complete TITLE hemoglobin beta chain [validated] - horse ORGANISM #formal_name Equus caballus #common_name domestic horse DATE 24-Apr-1984 #sequence_revision 04-Dec-1986 #text_change 15-Sep-2000 ACCESSIONS B91688; A90744; A90745; A02380 REFERENCE A91688 !$#authors Matsuda, G.; Maita, T.; Braunitzer, G.; Schrank, B. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1980) 361:1107-1116 !$#title Notiz zur Sequenz der Haemoglobine des Pferdes. !$#cross-references MUID:81005583; PMID:7409745 !$#accession B91688 !'##molecule_type protein !'##residues 1-146 ##label MAT REFERENCE A90744 !$#authors Smith, D.B. !$#journal Can. J. Biochem. (1968) 46:825-843 !$#title Amino acid sequences of some tryptic peptides from the !1beta-chain of horse hemoglobin. !$#cross-references MUID:68397920; PMID:4876811 !$#accession A90744 !'##molecule_type protein !'##residues 1-82;117-146 ##label SM1 REFERENCE A90745 !$#authors Smith, D.B.; Chung, W.P. !$#journal Can. J. Biochem. (1970) 48:1160-1164 !$#title Amide groups of some tryptic peptides from the beta-chain of !1horse hemoglobin. !$#cross-references MUID:71027939; PMID:5529282 !$#contents determination of amides !$#accession A90745 !'##molecule_type protein !'##residues 52-54 ##label SM2 REFERENCE A50429 !$#authors Perutz, M.F. !$#submission submitted to the Brookhaven Protein Data Bank, November 1973 !$#cross-references PDB:2DHB !$#contents annotation; X-ray crystallography, 2.8 angstroms, deoxy !1form, residues 1-110,'AL',113,'V',115-146 REFERENCE A30628 !$#authors Bolton, W.; Perutz, M.F. !$#journal Nature (1970) 228:551-552 !$#title Three dimensional Fourier synthesis of horse !1deoxyhaemoglobin at 2.8 angstroms resolution. !$#cross-references MUID:71011555; PMID:5472471 !$#contents annotation; X-ray crystallography, 2.8 angstroms, deoxy form REFERENCE A30627 !$#authors Perutz, M.F.; Muirhead, H.; Cox, J.M.; Goaman, L.C.G. !$#journal Nature (1968) 219:131-139 !$#title Three-dimensional Fourier synthesis of horse oxyhaemoglobin !1at 2.8 angstroms resolution: the atomic model. !$#cross-references MUID:68317028; PMID:5659637 !$#contents annotation; X-ray crystallography, 2.8 angstroms, oxy form REFERENCE A50493 !$#authors Ladner, R.C.; Heidner, E.G.; Perutz, M.F. !$#submission submitted to the Brookhaven Protein Data Bank, February 1977 !$#cross-references PDB:2MHB !$#contents annotation; X-ray crystallography, 2.0 angstroms, aquo met !1form, residues 1-146 REFERENCE A92848 !$#authors Ladner, R.C.; Heidner, E.J.; Perutz, M.F. !$#journal J. Mol. Biol. (1977) 114:385-414 !$#title The structure of horse methaemoglobin at 2.0 angstrom !1resolution. !$#cross-references MUID:78007980; PMID:561852 !$#contents annotation; sequence correction; X-ray crystallography, 2.0 !1angstroms, 2.0 angstroms, aquo met form !$#note discusses incorrect beta chain sequence used in X-ray !1structure refinement COMPLEX Two beta chains combine to form heterotetramers with two !1alpha chains to form hemoglobin A. FUNCTION !$#description in erythrocytes binds and transports molecular oxygen from !1lung to tissues CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status experimental\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status experimental SUMMARY #length 146 #molecular-weight 16008 #checksum 1311 SEQUENCE /// ENTRY HBHOZ #type complete TITLE hemoglobin beta chain - mountain zebra ORGANISM #formal_name Equus zebra #common_name mountain zebra DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 03-Mar-2000 ACCESSIONS A02381 REFERENCE A91706 !$#authors Mazur, G.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1982) 363:59-71 !$#title Perissodactyla: die Sequenz der Haemoglobine von Wildsel !1(Equus hemionus kulan) und Zebra (Equus zebra). !$#cross-references MUID:82140509; PMID:7061044 !$#accession A02381 !'##molecule_type protein !'##residues 1-146 ##label MAZ CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16079 #checksum 1479 SEQUENCE /// ENTRY HBHOK #type complete TITLE hemoglobin beta chain - kulan ORGANISM #formal_name Equus hemionus kulan #common_name kulan DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Mar-2000 ACCESSIONS A91706 REFERENCE A91706 !$#authors Mazur, G.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1982) 363:59-71 !$#title Perissodactyla: die Sequenz der Haemoglobine von Wildsel !1(Equus hemionus kulan) und Zebra (Equus zebra). !$#cross-references MUID:82140509; PMID:7061044 !$#accession A91706 !'##molecule_type protein !'##residues 1-146 ##label MAZ !'##note article in German with English abstract CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16079 #checksum 1479 SEQUENCE /// ENTRY HBTPJ #type complete TITLE hemoglobin beta chain, major - Brazilian tapir ORGANISM #formal_name Tapirus terrestris #common_name Brazilian tapir, lowland tapir DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 03-Mar-2000 ACCESSIONS A02382 REFERENCE A91727 !$#authors Mazur, G.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1984) 365:1097-1106 !$#title Perissodactyla: die Primaerstruktur der Haemoglobine eines !1Flachlandtapirs (Tapirus terrestris): Glutaminsaeure in !1Position 2 der beta-Ketten. !$#cross-references MUID:85053021; PMID:6149994 !$#accession A02382 !'##molecule_type protein !'##residues 1-146 ##label MAZ CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15973 #checksum 793 SEQUENCE /// ENTRY HBTPN #type complete TITLE hemoglobin beta chain, minor - Brazilian tapir ORGANISM #formal_name Tapirus terrestris #common_name Brazilian tapir, lowland tapir DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 03-Mar-2000 ACCESSIONS A02383 REFERENCE A91727 !$#authors Mazur, G.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1984) 365:1097-1106 !$#title Perissodactyla: die Primaerstruktur der Haemoglobine eines !1Flachlandtapirs (Tapirus terrestris): Glutaminsaeure in !1Position 2 der beta-Ketten. !$#cross-references MUID:85053021; PMID:6149994 !$#accession A02383 !'##molecule_type protein !'##residues 1-146 ##label MAZ CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16004 #checksum 907 SEQUENCE /// ENTRY HBRNW #type complete TITLE hemoglobin beta chains - white rhinoceros ORGANISM #formal_name Ceratotherium simum #common_name white rhinoceros, square-lipped rhinoceros DATE 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 03-Mar-2000 ACCESSIONS A02384 REFERENCE A91701 !$#authors Mazur, G.; Braunitzer, G.; Wright, P.G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1982) 363:1077-1085 !$#title Die Primaerstruktur des Haemoglobins vom Breitmaulnashorn !1(Ceratotherium simum, Perissodactyla): beta-2 Glu. !$#cross-references MUID:83055102; PMID:7141412 !$#accession A02384 !'##molecule_type protein !'##residues 1-146 ##label MAZ !'##note 62-Thr, 62-Ser, and 116-Gln were also found in this sample from !1a single animal, suggesting the presence of at least two !1beta chain loci CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15967 #checksum 947 SEQUENCE /// ENTRY HBPG #type complete TITLE hemoglobin beta chain [validated] - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 30-Apr-1980 #sequence_revision 19-May-2000 #text_change 15-Sep-2000 ACCESSIONS S54269; A02385 REFERENCE S54269 !$#authors Sharma, A.; Parson, C.T.; Midha, S.; Okabe, J.; Yerle, M.; !1Pinton, P.; Logan, J.; Kumar, L.R. !$#submission submitted to the EMBL Data Library, May 1995 !$#description Molecular characterization of porcine beta globin locus. !$#accession S54269 !'##molecule_type DNA !'##residues 1-147 ##label SHA !'##cross-references EMBL:X86791; NID:g806380; PIDN:CAA60490.1; !1PID:g806381 REFERENCE A91676 !$#authors Braunitzer, G.; Schrank, B.; Stangl, A.; Scheithauer, U. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1978) 359:137-146 !$#title Die Sequenzanalyse des Haemoglobins des Schweines. !$#cross-references MUID:78170269; PMID:565742 !$#accession A02385 !'##molecule_type protein !'##residues 2-125,'D',127-147 ##label BRA REFERENCE A52890 !$#authors Katz, D.S.; White, S.P.; Huang, W.; Kumar, R.; Christianson, !1D.W. !$#submission submitted to the Brookhaven Protein Data Bank, September !11994 !$#cross-references PDB:2PGH !$#contents annotation; X-ray crystallography, 2.8 angstroms, residues !11-141 REFERENCE A58466 !$#authors Katz, D.S.; White, S.P.; Huang, W.; Kumar, R.; Christianson, !1D.W. !$#journal J. Mol. Biol. (1994) 244:541-553 !$#title Structure determination of aquomet porcine hemoglobin at 2.8 !1Angstroms resolution. !$#cross-references MUID:95082021; PMID:7990139 !$#contents annotation; X-ray crystallography, 2.8 angstroms GENETICS !$#introns 31/2; 105/3 COMPLEX two beta chains combine in heterotetramers with two alpha !1chains (see PIR:HAPG) FUNCTION !$#description in erythrocytes binds and transports molecular oxygen from !1lung to tissues CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$4-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status experimental\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status experimental SUMMARY #length 147 #molecular-weight 16165 #checksum 3350 SEQUENCE /// ENTRY HBLL #type complete TITLE hemoglobin beta chain - llama ORGANISM #formal_name Lama guanicoe glama #common_name llama DATE 30-Jun-1980 #sequence_revision 31-Dec-1991 #text_change 03-Mar-2000 ACCESSIONS A91677; A02386 REFERENCE A91677 !$#authors Braunitzer, G.; Schrank, B.; Stangl, A.; Bauer, C. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1978) 359:547-558 !$#title Phosphat/protein-Wechselwirkung und die Atmung des Lamas, !1des menschlichen Foetus und die des Pferdes. !$#cross-references MUID:78216692; PMID:669574 !$#accession A91677 !'##molecule_type protein !'##residues 1-146 ##label BR2 REFERENCE A91673 !$#authors Braunitzer, G.; Schrank, B.; Stangl, A.; Bauer, C. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1977) 358:921-925 !$#title Die Regulation der Hoehenatmung und ihre molekulare Deutung: !1die Sequenz der beta-Ketten der Haemoglobine des Schweines !1und des Lamas. !$#cross-references MUID:77248104; PMID:892715 !$#accession A02386 !'##molecule_type protein !'##residues 1-18,'N',20-146 ##label BR1 !'##note this sequence has been revised in reference A91677 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16064 #checksum 2718 SEQUENCE /// ENTRY HBGW #type complete TITLE hemoglobin beta chain - guanaco ORGANISM #formal_name Lama guanicoe #common_name guanaco DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 03-Mar-2000 ACCESSIONS S10616 REFERENCE S10615 !$#authors Piccinini, M.; Kleinschmidt, T.; Juergens, K.D.; Braunitzer, !1G. !$#journal Biol. Chem. Hoppe-Seyler (1990) 371:641-648 !$#title Primary structure and oxygen-binding properties of the !1hemoglobin from guanaco (Lama guanacoe, Tylopoda). !$#cross-references MUID:91025635; PMID:2222863 !$#accession S10616 !'##molecule_type protein !'##residues 1-146 ##label PIC !'##note the source is designated as Lama guanacoe CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16064 #checksum 2718 SEQUENCE /// ENTRY HBCMA #type complete TITLE hemoglobin beta chain - Arabian camel ORGANISM #formal_name Camelus dromedarius #common_name Arabian camel DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Mar-2000 ACCESSIONS A91685 REFERENCE A91685 !$#authors Braunitzer, G.; Schrank, B.; Stangl, A.; Wiesner, H. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1979) 360:1941-1946 !$#title Hoehenatmung, Phosphat-Protein-Wechselwirkung: die Sequenz !1der Haemoglobine des Meerschweinchens und des Dromedars. !$#cross-references MUID:80114125; PMID:527943 !$#accession A91685 !'##molecule_type protein !'##residues 1-146 ##label BRA !'##note article in German with English abstract CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16114 #checksum 2611 SEQUENCE /// ENTRY HBCMB #type complete TITLE hemoglobin beta chain - Bactrian camel ORGANISM #formal_name Camelus bactrianus #common_name Bactrian camel DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Mar-2000 ACCESSIONS A92758 REFERENCE A92758 !$#authors Braunitzer, G.; Schrank, B.; Stangl, A.; Wiesner, H. !$#journal J. Chem. Soc. Pak. (1980) 2:1-7 !$#title Respiration at high altitudes, !1phosphate-protein-interaction: sequence of the hemoglobins !1of the hamster (Mesocricetus aureatus) and the camel !1(Camelus ferus, Camelidae). !$#accession A92758 !'##molecule_type protein !'##residues 1-146 ##label BRA !'##note article in German with English abstract CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16114 #checksum 2611 SEQUENCE /// ENTRY HBBOB #type complete TITLE hemoglobin beta chain [validated] - bovine ALTERNATE_NAMES hemoglobin-derived opioid peptide CONTAINS LVV-hemorphin-7; VV-hemorphin-7 ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 24-Apr-1984 #sequence_revision 25-Feb-1985 #text_change 15-Sep-2000 ACCESSIONS B93504; A90046; B90046; A90052; B90052; S35696; S65609; !1A02387 REFERENCE A93504 !$#authors Schimenti, J.C.; Duncan, C.H. !$#journal Nucleic Acids Res. (1984) 12:1641-1655 !$#title Ruminant globin gene structures suggest an evolutionary role !1for Alu-type repeats. !$#cross-references MUID:84144058; PMID:6322113 !$#accession B93504 !'##molecule_type DNA !'##residues 1-145 ##label SCI !'##cross-references EMBL:X00376; NID:g394; PIDN:CAA25111.1; PID:g395 !'##experimental_source beta A allele, Jersey cattle REFERENCE A90046 !$#authors Schroeder, W.A.; Shelton, J.R.; Shelton, J.B.; Robberson, !1B.; Babin, D.R. !$#journal Arch. Biochem. Biophys. (1967) 120:124-135 !$#title A comparison of amino acid sequences in the beta-chains of !1adult bovine hemoglobins A and B. !$#cross-references MUID:68001834; PMID:6048711 !$#accession A90046 !'##molecule_type protein !'##residues 1-145 ##label SCR1 !'##experimental_source beta A allele, Jersey cattle !$#accession B90046 !'##molecule_type protein !'##residues 1-14,'S',16-17,'H',19-118,'N',120-145 ##label SCR2 !'##experimental_source beta B allele, Jersey cattle REFERENCE A90052 !$#authors Schroeder, W.A.; Shelton, J.R.; Shelton, J.B.; Apell, G.; !1Huisman, T.H.J.; Smith, L.L.; Carr, W.R. !$#journal Arch. Biochem. Biophys. (1972) 152:222-232 !$#title Amino acid sequences in the beta-chains of adult bovine !1hemoglobins C-Rhodesia and D-Zambia. !$#cross-references MUID:73007895; PMID:4561255 !$#accession A90052 !'##molecule_type protein !'##residues 1-130,'Q',132-145 ##label SCR3 !'##experimental_source C-Rhodesia allele, Angoni cattle (East African !1short-horn zebu) !$#accession B90052 !'##molecule_type protein !'##residues 1-19,'G',21-42,'T',44-145 ##label SCR4 !'##experimental_source D-Zambia allele, Angoni cattle (East African !1short-horn zebu) REFERENCE S35696 !$#authors Barkhudaryan, N.; Kellermann, J.; Galoyan, A.; Lottspeich, !1F. !$#journal FEBS Lett. (1993) 329:215-218 !$#title High molecular weight aspartic endopeptidase generates a !1coronaro-constrictory peptide from the beta-chain of !1hemoglobin. !$#cross-references MUID:93359052; PMID:8354398 !$#accession S35696 !'##molecule_type protein !'##residues 31-40 ##label BAR !'##note LVV-hemorphin-7 acts as a vasoconstrictor REFERENCE S65609 !$#authors Aubes-Dufau, I.; Capdevielle, J.; Seris, J.L.; Combes, D. !$#journal FEBS Lett. (1995) 364:115-119 !$#title Bitter peptide from hemoglobin hydrolysate: isolation and !1characterization. !$#cross-references MUID:95269781; PMID:7750554 !$#accession S65609 !'##molecule_type protein !'##residues 32-40 ##label AUB !'##note VV-hemorphin-7 isolated from a hydrolysate has a bitter taste REFERENCE A52353 !$#authors Fermi, G. !$#submission submitted to the Brookhaven Protein Data Bank, May 1993 !$#cross-references PDB:1HDA !$#contents annotation; X-ray crystallography, 2.2 angstroms, residues !11-145 REFERENCE A58463 !$#authors Perutz, M.F.; Fermi, G.; Poyart, C.; Pagnier, J.; Kister, J. !$#journal J. Mol. Biol. (1993) 233:536-545 !$#title A novel allosteric mechanism in haemoglobin. Structure of !1bovine deoxyhaemoglobin, absence of specific !1chloride-binding sites and origin of the chloride-linked !1Bohr effect in bovine and human haemoglobin. !$#cross-references MUID:94016570; PMID:8411160 !$#contents annotation; X-ray crystallography, 2.2 angstroms GENETICS !$#introns 28/2; 102/3 COMPLEX Two beta chains combine to form heterotetramers with two !1alpha chains to form adult hemoglobin A. FUNCTION !$#description in erythrocytes binds and transports molecular oxygen from !1lung to tissues CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; opioid peptide; oxygen carrier FEATURE !$2-145 #domain globin homology #label GLB\ !$31-40 #product LVV-hemorphin-7 #status experimental #label !8OPIA\ !$32-40 #product VV-hemorphin-7 #status experimental #label !8OPI9\ !$62 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$91 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 145 #molecular-weight 15954 #checksum 8159 SEQUENCE /// ENTRY HBBOBB #type complete TITLE hemoglobin beta-A chain - banteng (tentative sequence) ORGANISM #formal_name Bos javanicus #common_name banteng DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 03-Mar-2000 ACCESSIONS A02388 REFERENCE A02388 !$#authors Namikawa, T.; Takenaka, O.; Takahashi, K. !$#journal Biochem. Genet. (1983) 21:787-796 !$#title Hemoglobin Bali (bovine): beta(A)18(Bl)Lys -> His: one of !1the "missing links" between beta(A) and beta(B) of domestic !1cattle exists in the Bali cattle (Bovinae, Bos banteng). !$#cross-references MUID:84023669; PMID:6626147 !$#accession A02388 !'##molecule_type protein !'##residues 1-145 ##label NAM !'##experimental_source Hereford breed !'##note tryptic peptides were positioned by homology with the bovine !1sequence CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-145 #domain globin homology #label GLB\ !$62 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$91 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 145 #molecular-weight 15964 #checksum 7955 SEQUENCE /// ENTRY HBBOG #type complete TITLE hemoglobin beta chain - gayal ORGANISM #formal_name Bos gaurus frontalis #common_name gayal DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 03-Mar-2000 ACCESSIONS A02389 REFERENCE A91737 !$#authors Lalthantluanga, R.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1984) 365:737-741 !$#title Amino-acid sequence of gayal hemoglobin (Bos gaurus !1frontalis, Bovidae). !$#cross-references MUID:85005246; PMID:6479895 !$#accession A02389 !'##molecule_type protein !'##residues 1-145 ##label LAL CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-145 #domain globin homology #label GLB\ !$62 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$91 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 145 #molecular-weight 15986 #checksum 8093 SEQUENCE /// ENTRY HBYA2 #type complete TITLE hemoglobin beta chain - yak ORGANISM #formal_name Bos mutus grunniens #common_name yak DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 03-Mar-2000 ACCESSIONS A02390 REFERENCE A90689 !$#authors Lalthantluanga, R.; Wiesner, H.; Braunitzer, G. !$#journal Biol. Chem. Hoppe-Seyler (1985) 366:63-68 !$#title Studies on yak hemoglobin (Bos grunniens, Bovidae): !1structural basis for high intrinsic oxygen affinity? !$#cross-references MUID:85225945; PMID:4005038 !$#contents beta-I and beta-II alleles !$#accession A02390 !'##molecule_type protein !'##residues 1-145 ##label THE !'##note the sequence from the beta-I allele differs from that shown in !1having 49-Thr, 116-Asn, and 134-Ala COMMENT The beta-II allele is shown. COMMENT The beta-II allele occurs much more frequently than the !1beta-I allele. CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-145 #domain globin homology #label GLB\ !$62 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$91 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 145 #molecular-weight 15991 #checksum 8518 SEQUENCE /// ENTRY HBBOKA #type complete TITLE hemoglobin beta chain - greater kudu ORGANISM #formal_name Tragelaphus strepsiceros #common_name greater kudu DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 03-Mar-2000 ACCESSIONS A02391 REFERENCE A90684 !$#authors Rodewald, K.; Wiesner, H.; Braunitzer, G. !$#journal Biol. Chem. Hoppe-Seyler (1985) 366:395-402 !$#title Primary structure of the hemoglobins from the greater Kudu !1antelope (Tragelaphus strepsiceros). !$#cross-references MUID:85279893; PMID:4026993 !$#accession A02391 !'##molecule_type protein !'##residues 1-145 ##label ROD !'##note there are two alleles for the beta chain, one having the !1sequence shown and the other having 16-Ser CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier; polymorphism FEATURE !$2-145 #domain globin homology #label GLB\ !$62 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$91 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 145 #molecular-weight 16053 #checksum 8642 SEQUENCE /// ENTRY HBEKN #type complete TITLE hemoglobin beta chain - European moose ORGANISM #formal_name Alces alces alces #common_name European moose, elk DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 03-Mar-2000 ACCESSIONS A02392 REFERENCE A91729 !$#authors Aschauer, H.; Wiesner, H.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1984) 365:1323-1330 !$#title Zur intrinsischen Sauerstoffaffinitaet: die Primaerstruktur !1eines weiteren Ruminantia-Haemoglobins: Methionin in betaNA2 !1eines Stirnwaffentraegers, des Nordland-Elches (Alces alces !1alces). !$#cross-references MUID:85078042; PMID:6510898 !$#accession A02392 !'##molecule_type protein !'##residues 1-145 ##label ASC CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-145 #domain globin homology #label GLB\ !$62 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$91 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 145 #molecular-weight 16223 #checksum 6806 SEQUENCE /// ENTRY HBDE3 #type complete TITLE hemoglobin beta-III chain - Virginia white-tailed deer ORGANISM #formal_name Odocoileus virginianus virginianus #common_name Virginia white-tailed deer DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 03-Mar-2000 ACCESSIONS A02393 REFERENCE A02393 !$#authors Shimizu, K.; Wong, S.C.; Wilson, J.B.; Lam, H.; Reynolds, !1A.E.; Singh, P.; Huisman, T.H.J.; Charles, N.G.; Amma, E.L. !$#journal Hemoglobin (1983) 7:15-45 !$#title The primary sequence of the beta chain of Hb type III of the !1Virginia white-tailed deer (Odocoilus virginianus), a !1comparison with putative sequences of the beta chains from !1four additional deer hemoglobins, types II, IV, V, and VII, !1and relationships between intermolecular contacts, primary !1sequence and sickling of deer hemoglobins. !$#cross-references MUID:83185439; PMID:6841126 !$#accession A02393 !'##molecule_type protein !'##residues 1-145 ##label SHI COMMENT This chain is one of five beta chain alleles. CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-145 #domain globin homology #label GLB\ !$62 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$91 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 145 #molecular-weight 15824 #checksum 7726 SEQUENCE /// ENTRY HBSHB #type complete TITLE hemoglobin beta-B chain - sheep ORGANISM #formal_name Ovis orientalis aries, Ovis ammon aries #common_name domestic sheep DATE 24-Apr-1984 #sequence_revision 30-Jan-1998 #text_change 19-May-2000 ACCESSIONS S10073; A92027; I47082; A02394 REFERENCE S10073 !$#authors Garner, K.J.; Lingrel, J.B. !$#journal J. Mol. Evol. (1989) 28:175-184 !$#title A comparison of the beta(A)- and beta(B)-globin gene !1clusters of sheep. !$#cross-references MUID:89178744; PMID:2494347 !$#accession S10073 !'##molecule_type DNA !'##residues 1-145 ##label GAR1 !'##cross-references EMBL:X14727; NID:g1208; PIDN:CAA32849.1; PID:g1209 !'##note the sequence of codons and residues 44-63 is repeated twice in !1the authors' translation REFERENCE A92027 !$#authors Boyer, S.H.; Hathaway, P.; Pascasio, F.; Bordley, J.; Orton, !1C.; Naughton, M.A. !$#journal J. Biol. Chem. (1967) 242:2211-2232 !$#title Differences in the amino acid sequences of tryptic peptides !1from three sheep hemoglobin beta chains. !$#cross-references MUID:67134347; PMID:6022868 !$#accession A92027 !'##molecule_type protein !'##residues 1-48,'B',50-67,'B',69-97,'B',99,'ZB',102-145 ##label BOY REFERENCE I47082 !$#authors Garner, K.J.; Lingrel, J.B. !$#journal Mol. Biol. Evol. (1988) 5:134-140 !$#title Structural organization of the beta-globin locus of !1beta-haplotype sheep. !$#cross-references MUID:88216150; PMID:3367782 !$#accession I47082 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-28 ##label GAR2 !'##cross-references GB:M19754; NID:g165890; PIDN:AAA31528.1; !1PID:g552420 GENETICS !$#introns 29/2; 103/3 COMPLEX two beta chains combine in heterotetramers with two alpha !1chains (see PIR:HASH) to form adult hemoglobin A FUNCTION !$#description in erythrocytes binds and transports molecular oxygen from !1lung to tissues CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$1-145 #product hemoglobin beta-B chain #status experimental !8#label MAT\ !$2-145 #domain globin homology #label GLB\ !$62 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$91 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 145 #molecular-weight 16073 #checksum 7912 SEQUENCE /// ENTRY HBSHA #type complete TITLE hemoglobin beta-A chain - sheep (tentative sequence) ORGANISM #formal_name Ovis orientalis aries, Ovis ammon aries #common_name domestic sheep DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 31-Mar-2000 ACCESSIONS A94556; A90237; A92306; A02394 REFERENCE A94556 !$#authors Beale, D. !$#submission submitted to the Atlas, August 1967 !$#accession A94556 !'##molecule_type protein !'##residues 1-145 ##label BEA1 REFERENCE A90237 !$#authors Beale, D. !$#journal Biochem. J. (1967) 103:129-140 !$#title A partial amino acid sequence for sheep haemoglobin A. !$#cross-references MUID:67209244; PMID:6033754 !$#accession A90237 !'##molecule_type protein !'##residues 1-145 ##label BEA2 REFERENCE A92306 !$#authors Kretschmer, P.J.; Coon, H.C.; Davis, A.; Harrison, M.; !1Nienhuis, A.W. !$#journal J. Biol. Chem. (1981) 256:1975-1982 !$#title Hemoglobin switching in sheep. Isolation of the fetal !1gamma-globin gene and demonstration that the fetal gamma- !1and adult beta(A)-globin genes lie within eight kilobase !1segments of homologous DNA. !$#cross-references MUID:81117290; PMID:6161931 !$#accession A92306 !'##molecule_type DNA !'##residues 1-29;39-56,'P',58-59;72-85;104-145 ##label KRE !'##cross-references GB:K02820 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$2-145 #domain globin homology #label GLB\ !$62 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$91 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 145 #molecular-weight 15917 #checksum 7131 SEQUENCE /// ENTRY HBGTA #type complete TITLE hemoglobin beta-A chain - goat ORGANISM #formal_name Capra aegagrus hircus #common_name domestic goat DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 03-Mar-2000 ACCESSIONS A90817; I46170; I46171; I46273; I46274; A92028; A90047; !1A90049; A02395 REFERENCE A90817 !$#authors Schon, E.A.; Cleary, M.L.; Haynes, J.R.; Lingrel, J.B. !$#journal Cell (1981) 27:359-369 !$#title Structure and evolution of goat gamma-, beta(c)- and beta !1(A)-globin genes: three developmentally regulated genes !1contain inserted elements. !$#cross-references MUID:82137075; PMID:6277503 !$#accession A90817 !'##molecule_type DNA !'##residues 1-145 ##label SCH !'##cross-references GB:M15387; NID:g164133; PIDN:AAA30913.1; !1PID:g164134 REFERENCE I46169 !$#authors Cleary, M.L.; Haynes, J.R.; Schon, E.A.; Lingrel, J.B. !$#journal Nucleic Acids Res. (1980) 8:4791-4802 !$#title Identification by nucleotide sequence analysis of a goat !1pseudoglobin gene. !$#cross-references MUID:81076616; PMID:6255432 !$#accession I46170 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-29 ##label CLE1 !'##cross-references EMBL:V00152; NID:g961; PIDN:CAA23467.1; PID:g962 !$#accession I46171 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 64-99 ##label CLE2 !'##cross-references EMBL:V00153; NID:g963; PIDN:CAA23468.1; PID:g669075 REFERENCE I46273 !$#authors Haynes, J.R.; Rosteck, P.R.; Schon, E.A.; Gallagher, P.M.; !1Burks, D.J.; Smith, K.; Lingrel, J.B. !$#journal J. Biol. Chem. (1980) 255:6355-6367 !$#title The isolation of the beta-a-, beta-c-, and gamma-globin !1genes and a presumptive embryonic globin gene from a goat !1DNA recombinant library. !$#cross-references MUID:80227766; PMID:6248519 !$#accession I46273 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 64-97 ##label HAY1 !'##cross-references GB:K00657; NID:g164128; PIDN:AAA30911.1; !1PID:g552351 !$#accession I46274 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 114-119 ##label HAY2 !'##cross-references GB:K00658; NID:g164129; PIDN:AAA30912.1; !1PID:g552352 REFERENCE A92028 !$#authors Huisman, T.H.J.; Adams, H.R.; Dimmock, M.O.; Edwards, W.E.; !1Wilson, J.B. !$#journal J. Biol. Chem. (1967) 242:2534-2541 !$#title The structure of goat hemoglobins. I. Structural studies of !1the beta chains of the hemoglobins of normal and anemic !1goats. !$#cross-references MUID:67165362; PMID:6026247 !$#accession A92028 !'##molecule_type protein !'##residues 1-145 ##label HUI !'##experimental_source A allele, partial sequence REFERENCE A90047 !$#authors Adams, H.R.; Boyd, E.M.; Wilson, J.B.; Miller, A.; Huisman, !1T.H.J. !$#journal Arch. Biochem. Biophys. (1968) 127:398-405 !$#title The structure of goat hemoglobins. III. Hemoglobin D, a beta !1chain variant with one apparent amino acid substitution (21 !1Asp-->His). !$#cross-references MUID:69036192; PMID:5697993 !$#accession A90047 !'##molecule_type protein !'##residues 1-19,'H',21-145 ##label ADA !'##experimental_source D allele, partial sequence REFERENCE A90049 !$#authors Wrightstone, R.N.; Wilson, J.B.; Miller, A.; Huisman, T.H.J. !$#journal Arch. Biochem. Biophys. (1970) 138:451-456 !$#title The structure of goat hemoglobins. IV. A third beta chain !1variant (beta-E) with three apparent amino acid !1substitutions. !$#cross-references MUID:70252721; PMID:5433580 !$#accession A90049 !'##molecule_type protein !'##residues 1-85,'H',87-102,'R',104-123,'V',125-145 ##label WRI !'##experimental_source E allele, partial sequence COMMENT The A allele sequence is shown. GENETICS !$#introns 29/2; 103/3 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-145 #domain globin homology #label GLB\ !$62 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$91 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 145 #molecular-weight 16021 #checksum 7122 SEQUENCE /// ENTRY HBGTC #type complete TITLE hemoglobin beta-C chain - goat ORGANISM #formal_name Capra aegagrus hircus #common_name domestic goat DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 03-Mar-2000 ACCESSIONS B02396; I46277; A02396 REFERENCE A90817 !$#authors Schon, E.A.; Cleary, M.L.; Haynes, J.R.; Lingrel, J.B. !$#journal Cell (1981) 27:359-369 !$#title Structure and evolution of goat gamma-, beta(c)- and beta !1(A)-globin genes: three developmentally regulated genes !1contain inserted elements. !$#cross-references MUID:82137075; PMID:6277503 !$#accession B02396 !'##molecule_type DNA !'##residues 1-141 ##label SCH !'##cross-references GB:M15389 !'##note initiator Met not shown REFERENCE I46273 !$#authors Haynes, J.R.; Rosteck, P.R.; Schon, E.A.; Gallagher, P.M.; !1Burks, D.J.; Smith, K.; Lingrel, J.B. !$#journal J. Biol. Chem. (1980) 255:6355-6367 !$#title The isolation of the beta-a-, beta-c-, and gamma-globin !1genes and a presumptive embryonic globin gene from a goat !1DNA recombinant library. !$#cross-references MUID:80227766; PMID:6248519 !$#accession I46277 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 66-93,'XX',96-115,'XX',118-134 ##label HAY !'##cross-references GB:K00662; NID:g164154; PID:g164158 COMMENT This type of beta-C chain is found when anemia has been !1experimentally produced. GENETICS !$#introns 26/2; 100/3 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$1-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15620 #checksum 7201 SEQUENCE /// ENTRY HBSHC #type complete TITLE hemoglobin beta-C chain - sheep ORGANISM #formal_name Ovis orientalis aries, Ovis ammon aries #common_name domestic sheep DATE 30-Sep-1993 #sequence_revision 30-Jan-1998 #text_change 03-Mar-2000 ACCESSIONS S10074; B92027; A90045; A02396 REFERENCE S10073 !$#authors Garner, K.J.; Lingrel, J.B. !$#journal J. Mol. Evol. (1989) 28:175-184 !$#title A comparison of the beta(A)- and beta(B)-globin gene !1clusters of sheep. !$#cross-references MUID:89178744; PMID:2494347 !$#accession S10074 !'##molecule_type DNA !'##residues 1-142 ##label GAR !'##cross-references EMBL:X14728; NID:g1212; PIDN:CAA32850.1; PID:g1213 !'##note the authors translated the codon GTC for residue 30 as Ala !'##note the sequence of codons and residues 41-60 is repeated twice in !1the authors' translation REFERENCE A92027 !$#authors Boyer, S.H.; Hathaway, P.; Pascasio, F.; Bordley, J.; Orton, !1C.; Naughton, M.A. !$#journal J. Biol. Chem. (1967) 242:2211-2232 !$#title Differences in the amino acid sequences of tryptic peptides !1from three sheep hemoglobin beta chains. !$#cross-references MUID:67134347; PMID:6022868 !$#accession B92027 !'##molecule_type protein !'##residues 2-64,'B',66-68,'B',70-71,'Z',73-74,'BB',77-82,'Z',84-85, !1'Z',87-94,'B',96,'ZB',99-103,'B',105-142 ##label BOY !'##experimental_source Dorset breed REFERENCE A90045 !$#authors Wilson, J.B.; Edwards, W.C.; McDaniel, M.; Dobbs, M.M.; !1Huisman, T.H.J. !$#journal Arch. Biochem. Biophys. (1966) 115:385-400 !$#title The structure of sheep hemoglobins. II. The amino acid !1composition of the tryptic peptides of the non-alpha chains !1of hemoglobins A, B, C, and F. !$#accession A90045 !'##molecule_type protein !'##residues 2-64,'B',66-68,'B',70-71,'Z',73-74,'BB',77-82,'Z',84-85, !1'Z',87-94,'B',96,'ZB',99-103,'B',105-142 ##label WIL !'##experimental_source Rambouillet breed !'##note there are several discrepancies between the sequence in this !1paper and that given by Boyer's group; the groups agreed to !1accept Boyer's sequence COMMENT This beta-C chain is produced when anemia is experimentally !1induced. GENETICS !$#introns 26/2; 100/3 COMPLEX Two beta chains combine to form heterotetramers with two !1alpha chains to form adult hemoglobin A FUNCTION !$#description in erythrocytes binds and transports molecular oxygen from !1lung to tissues CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$1-142 #domain globin homology #label GLB\ !$2-142 #product hemoglobin beta-C chain #status experimental !8#label MAT\ !$59 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$88 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 142 #molecular-weight 15750 #checksum 1174 SEQUENCE /// ENTRY HBMFC #type complete TITLE hemoglobin beta-C chain - mouflon (tentative sequence) ORGANISM #formal_name Ovis orientalis musimon, Ovis ammon musimon #common_name mouflon DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 03-Mar-2000 ACCESSIONS A90232; A02396 REFERENCE A90232 !$#authors Wilson, J.B.; Miller, A.; Huisman, T.H.J. !$#journal Biochem. Genet. (1970) 4:677-688 !$#title Production of hemoglobin C in the moufflon (Ovis musimon !1pallas, 1811) and the barbary sheep (Ammotragus lervia !1pallas, 1777) during experimental anemia: amino acid !1composition of tryptic peptides from the beta(B) and beta !1(C) chains. !$#cross-references MUID:71089262; PMID:5496230 !$#accession A90232 !'##molecule_type protein !'##residues 1-141 ##label WIL !'##note compositions of tryptic peptides were determined; positions !1100-111 were sequenced COMMENT This type of beta-C chain is found when anemia has been !1experimentally produced. CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$1-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15618 #checksum 8632 SEQUENCE /// ENTRY HBSHCR #type complete TITLE hemoglobin beta-C chain - aoudad (tentative sequence) ORGANISM #formal_name Ammotragus lervia #common_name aoudad, Barbary sheep DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 03-Mar-2000 ACCESSIONS B90232; A02396 REFERENCE A90232 !$#authors Wilson, J.B.; Miller, A.; Huisman, T.H.J. !$#journal Biochem. Genet. (1970) 4:677-688 !$#title Production of hemoglobin C in the moufflon (Ovis musimon !1pallas, 1811) and the barbary sheep (Ammotragus lervia !1pallas, 1777) during experimental anemia: amino acid !1composition of tryptic peptides from the beta(B) and beta !1(C) chains. !$#cross-references MUID:71089262; PMID:5496230 !$#accession B90232 !'##molecule_type protein !'##residues 1-141 ##label WIL !'##note compositions of tryptic peptides were determined; positions !1100-111 were sequenced COMMENT This type of beta-C chain is found when anemia has been !1experimentally produced. CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$1-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15632 #checksum 8896 SEQUENCE /// ENTRY HBSHBC #type complete TITLE hemoglobin beta C(NA) chain - aoudad (tentative sequence) ORGANISM #formal_name Ammotragus lervia #common_name aoudad, Barbary sheep DATE 24-Apr-1984 #sequence_revision 30-Sep-1988 #text_change 31-Mar-2000 ACCESSIONS A90239; A02397 REFERENCE A90239 !$#authors Huisman, T.H.J.; Dasher, G.A.; Moretz Jr., W.H.; Dozy, A.M.; !1Wilson, J.B.; Vliet, G.V. !$#journal Biochem. J. (1968) 107:745-751 !$#title Studies of haemoglobin types in Barbary sheep (Ammotragus !1lervia). !$#contents composition of tryptic peptides !$#accession A90239 !'##molecule_type protein !'##residues 1-141 ##label HUI REFERENCE A94566 !$#authors Huisman, T.H.J. !$#submission submitted to the Atlas, January 1969 !$#contents annotation; revision to residue 103 COMMENT This type of beta C chain is found in nonanemic Barbary !1sheep, whereas the other type of beta C chain is found in !1anemic Barbary sheep. CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$1-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 15633 #checksum 8915 SEQUENCE /// ENTRY HBBOF #type complete TITLE hemoglobin beta chain, fetal - bovine ALTERNATE_NAMES hemoglobin gamma chain ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 03-Mar-2000 ACCESSIONS A93504; A90549; A02398 REFERENCE A93504 !$#authors Schimenti, J.C.; Duncan, C.H. !$#journal Nucleic Acids Res. (1984) 12:1641-1655 !$#title Ruminant globin gene structures suggest an evolutionary role !1for Alu-type repeats. !$#cross-references MUID:84144058; PMID:6322113 !$#accession A93504 !'##molecule_type DNA !'##residues 1-145 ##label SCH !'##cross-references GB:X00354; NID:g392; PIDN:CAA25101.1; PID:g393 REFERENCE A90549 !$#authors Babin, D.R.; Schroeder, W.A.; Shelton, J.R.; Shelton, J.B.; !1Robberson, B. !$#journal Biochemistry (1966) 5:1297-1310 !$#title The amino acid sequence of the gamma chain of bovine fetal !1hemoglobin. !$#cross-references MUID:67089183; PMID:5958205 !$#accession A90549 !'##molecule_type protein !'##residues 1-145 ##label BAB GENETICS !$#introns 29/2; 103/3 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-145 #domain globin homology #label GLB\ !$62 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$91 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 145 #molecular-weight 15859 #checksum 7550 SEQUENCE /// ENTRY HBGTF #type complete TITLE hemoglobin beta chain, fetal - goat ALTERNATE_NAMES hemoglobin gamma chain [misnomer] ORGANISM #formal_name Capra aegagrus hircus #common_name domestic goat DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 03-Mar-2000 ACCESSIONS A02399; A91710; I46279; I46280 REFERENCE A90817 !$#authors Schon, E.A.; Cleary, M.L.; Haynes, J.R.; Lingrel, J.B. !$#journal Cell (1981) 27:359-369 !$#title Structure and evolution of goat gamma-, beta(c)- and beta !1(A)-globin genes: three developmentally regulated genes !1contain inserted elements. !$#cross-references MUID:82137075; PMID:6277503 !$#accession A02399 !'##molecule_type DNA !'##residues 1-145 ##label SCH !'##cross-references GB:M15388; NID:g164169; PIDN:AAA30925.1; !1PID:g164170 REFERENCE A91710 !$#authors Kleinschmidt, T.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1982) 363:789-796 !$#title Die Primaerstruktur der gamma-Ketten der foetalen !1Haemoglobine von Schaf (Ovis ammon) und Ziege (Capra !1aegagrus), Artiodactyla. !$#cross-references MUID:83005406; PMID:7118074 !$#accession A91710 !'##molecule_type protein !'##residues 1-145 ##label KLE REFERENCE I46273 !$#authors Haynes, J.R.; Rosteck, P.R.; Schon, E.A.; Gallagher, P.M.; !1Burks, D.J.; Smith, K.; Lingrel, J.B. !$#journal J. Biol. Chem. (1980) 255:6355-6367 !$#title The isolation of the beta-a-, beta-c-, and gamma-globin !1genes and a presumptive embryonic globin gene from a goat !1DNA recombinant library. !$#cross-references MUID:80227766; PMID:6248519 !$#accession I46279 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 52-97 ##label HAY1 !'##cross-references GB:K00663; NID:g164164; PIDN:AAA30923.1; !1PID:g164167 !$#accession I46280 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 104-118,'XXX',122-123,'G',125-139 ##label HAY2 !'##cross-references GB:K00664; NID:g164165; PIDN:AAA30924.1; !1PID:g552354 COMMENT This is regarded as a beta chain produced by the fetus, not !1as a gamma chain. CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$1-145 #product hemoglobin beta chain, fetal #status !8experimental #label MAT\ !$2-145 #domain globin homology #label GLB\ !$62 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$91 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 145 #molecular-weight 15946 #checksum 7339 SEQUENCE /// ENTRY HGSH #type complete TITLE hemoglobin beta chain, fetal - sheep ALTERNATE_NAMES hemoglobin gamma chain [misnomer] ORGANISM #formal_name Ovis orientalis aries, Ovis ammon aries #common_name domestic sheep DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Mar-2000 ACCESSIONS B92306; S45297; A90610; A92306 REFERENCE A92306 !$#authors Kretschmer, P.J.; Coon, H.C.; Davis, A.; Harrison, M.; !1Nienhuis, A.W. !$#journal J. Biol. Chem. (1981) 256:1975-1982 !$#title Hemoglobin switching in sheep. Isolation of the fetal !1gamma-globin gene and demonstration that the fetal gamma- !1and adult beta(A)-globin genes lie within eight kilobase !1segments of homologous DNA. !$#cross-references MUID:81117290; PMID:6161931 !$#accession B92306 !'##molecule_type DNA !'##residues 1-29;52-96;104-145 ##label KRE !'##cross-references GB:K02824; NID:g165901; PIDN:AAA31533.1; !1PID:g552423; GB:K02825; NID:g165902; PID:g165906; GB:K02826; !1NID:g165903; PID:g165907 REFERENCE S45297 !$#authors Saban, J.; King, D. !$#journal Biochim. Biophys. Acta (1994) 1218:87-90 !$#title Sequence of the sheep fetal beta globin gene and flanking !1region. !$#cross-references MUID:94250699; PMID:8193169 !$#accession S45297 !'##molecule_type DNA !'##residues 1-17,30-47,'F',49-145 ##label SAB !'##cross-references EMBL:U01378; NID:g437113; PIDN:AAA19218.1; !1PID:g437114 REFERENCE A90610 !$#authors Darbre, P.D.; Lehmann, H. !$#journal Biochim. Biophys. Acta (1976) 446:10-18 !$#title The gamma chain of the lamb. !$#cross-references MUID:77022158; PMID:974104 !$#accession A90610 !'##molecule_type protein !'##residues 1-118,'EG',121-145 ##label DAR COMMENT This is regarded as a beta chain produced by the fetus, not !1as a gamma chain. GENETICS !$#introns 17/2; 103/3 COMPLEX Two gamma chains combine in heterotetramers with two alpha !1chains to form fetal hemoglobin F. FUNCTION !$#description in erythrocytes binds and transports molecular oxygen from !1placenta to tissues CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$1-145 #product hemoglobin beta chain, fetal #status !8experimental #label MAT\ !$2-145 #domain globin homology #label GLB\ !$62 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$91 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 145 #molecular-weight 15931 #checksum 7431 SEQUENCE /// ENTRY HBELI #type complete TITLE hemoglobin beta chain - Indian elephant ORGANISM #formal_name Elephas maximus #common_name Indian elephant DATE 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 03-Mar-2000 ACCESSIONS A02400 REFERENCE A91708 !$#authors Braunitzer, G.; Jelkmann, W.; Stangl, A.; Schrank, B.; !1Krombach, C. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1982) 363:683-691 !$#title Die primaere Struktur des Haemoglobins des indischen !1Elefanten (Elephas maximus, Proboscidea): beta-2 = Asn. !$#cross-references MUID:83029110; PMID:7129359 !$#accession A02400 !'##molecule_type protein !'##residues 1-146 ##label BRA CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16168 #checksum 440 SEQUENCE /// ENTRY HBELA #type complete TITLE hemoglobin beta chain - African elephant ORGANISM #formal_name Loxodonta africana #common_name African elephant DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 03-Mar-2000 ACCESSIONS A02401 REFERENCE A91738 !$#authors Braunitzer, G.; Stangl, A.; Schrank, B.; Krombach, C.; !1Wiesner, H. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1984) 365:743-749 !$#title The primary structure of the haemoglobin of the African !1elephant (Loxodonta africana, Proboscidea): asparagine !1position 2 of the beta-chain. !$#cross-references MUID:85005247; PMID:6479896 !$#accession A02401 !'##molecule_type protein !'##residues 1-146 ##label BRA CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16182 #checksum 492 SEQUENCE /// ENTRY HBHXR #type complete TITLE hemoglobin beta chain - Abyssinian hyrax ORGANISM #formal_name Procavia capensis habessinica #common_name Abyssinian hyrax DATE 20-Sep-1984 #sequence_revision 20-Sep-1984 #text_change 03-Mar-2000 ACCESSIONS A02402 REFERENCE A91714 !$#authors Kleinschmidt, T.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1983) 364:1303-1313 !$#title The primary structure of the rock hyrax (Procavia !1habessinica, Hyracoidea) hemoglobin: insertion of glutamine !1in the alpha chain. !$#cross-references MUID:84030514; PMID:6629339 !$#accession A02402 !'##molecule_type protein !'##residues 1-146 ##label KLE !'##note tryptic peptides were sequenced and were positioned by homology CLASSIFICATION #superfamily globin; globin homology KEYWORDS acetylated amino end; blood; chromoprotein; erythrocyte; !1heme; iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$1 #modified_site acetylated amino end (Val) (partial) !8#status experimental\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16205 #checksum 247 SEQUENCE /// ENTRY HBDN #type complete TITLE hemoglobin beta chain - nine-banded armadillo (tentative sequence) ORGANISM #formal_name Dasypus novemcinctus #common_name nine-banded armadillo DATE 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 31-Mar-2000 ACCESSIONS A02403 REFERENCE A02403 !$#authors de Jong, W.W.; Leunissen, J.A.M.; Cuijpers, H.T. !$#journal Biochim. Biophys. Acta (1981) 668:57-62 !$#title Primary structure of the major beta-chain of armadillo !1(Dasypus novemcinctus) haemoglobin. !$#cross-references MUID:81208315; PMID:7236709 !$#accession A02403 !'##molecule_type protein !'##residues 1-146 ##label DEJ CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16326 #checksum 1143 SEQUENCE /// ENTRY HBOWP #type complete TITLE hemoglobin beta chain - pale-throated sloth ORGANISM #formal_name Bradypus tridactylus #common_name pale-throated sloth DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS S03999 REFERENCE S03998 !$#authors Kleinschmidt, T.; Maerz, J.; Braunitzer, G. !$#journal Biol. Chem. Hoppe-Seyler (1989) 370:303-308 !$#title The primary structure of pale-throated three-toed sloth !1(Bradypus tridactylus, Xenarthra) hemoglobin. !$#cross-references MUID:89335258; PMID:2757790 !$#accession S03999 !'##molecule_type protein !'##residues 1-146 ##label KLE CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16143 #checksum 1593 SEQUENCE /// ENTRY HBMS #type complete TITLE hemoglobin beta major chain - mouse CONTAINS hemoglobin beta major chain, d allele; hemoglobin beta major chain, s allele ORGANISM #formal_name Mus musculus #common_name house mouse DATE 29-Jul-1981 #sequence_revision 06-Feb-1998 #text_change 03-Mar-2000 ACCESSIONS A90790; I49724; I49725; I49727; B94249; I48267; A22333; !1I49726; I49723; A02404 REFERENCE A90790 !$#authors Konkel, D.A.; Maizel Jr., J.V.; Leder, P. !$#journal Cell (1979) 18:865-873 !$#title The evolution and sequence comparison of two recently !1diverged mouse chromosomal beta-globin genes. !$#cross-references MUID:80090038; PMID:519759 !$#accession A90790 !'##molecule_type DNA !'##residues 2-147 ##label KON !'##cross-references GB:J00413; GB:K01748; GB:K03545; GB:X00624; !1NID:g193793; PIDN:AAA37791.1; PID:g387188 !'##experimental_source strain BALB/c !'##note inbred mouse strains possess one of three alleles at the Hbb !1locus: d (diffuse), s (single), and p; the d and p alleles !1are actually closely linked doublets that coordinately !1express a major and a minor chain, the minor chain being !1slightly different in the two alleles; the s allele produces !1only one chain REFERENCE I46723 !$#authors van den Berg, J.; van Ooyen, A.; Mantei, N.; Schamboeck, A.; !1Grosveld, G.; Flavell, R.A.; Weissmann, C. !$#journal Nature (1978) 276:37-44 !$#title Comparison of cloned rabbit and mouse beta-globin genes !1showing strong evolutionary divergence of two homologous !1pairs of introns. !$#cross-references MUID:79114395; PMID:264241 !$#accession I49724 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 28-43 ##label VAN2 !'##cross-references GB:M10828; NID:g193768; PIDN:AAA37786.1; !1PID:g193772 !$#accession I49725 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 100-115 ##label VAN3 !'##cross-references GB:M10830; NID:g193770; PIDN:AAA37787.1; !1PID:g193773 REFERENCE I49727 !$#authors Tilghman, S.M.; Tiemeier, D.C.; Seidman, J.G.; Peterlin, !1B.M.; Sullivan, M.; Maizel, J.V.; Leder, P. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1978) 75:725-729 !$#title Intervening sequence of DNA identified in the structural !1portion of a mouse beta-globin gene. !$#cross-references MUID:78137024; PMID:273235 !$#accession I49727 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 94-104 ##label TIL !'##cross-references GB:M10688; NID:g193791; PIDN:AAA37790.1; !1PID:g553925 REFERENCE A94249 !$#authors van Ooyen, A.; van den Berg, J.; Mantei, N.; Weissmann, C. !$#journal Science (1979) 206:337-344 !$#title Comparison of total sequence of a cloned rabbit beta-globin !1gene and its flanking regions with a homologous mouse !1sequence. !$#cross-references MUID:80014491; PMID:482942 !$#accession B94249 !'##molecule_type DNA !'##residues 2-90,'Q',92-147 ##label VAN1 !'##cross-references GB:J00413; GB:K01748; GB:K03545; GB:X00624; !1NID:g193793 REFERENCE I48267 !$#authors Gilmour, R.S.; Spandidos, D.A.; Vass, J.K.; Gow, J.W.; Paul, !1J. !$#journal EMBO J. (1984) 3:1263-1272 !$#title A negative regulatory sequence near the mouse beta-maj !1globin gene associated with a region of potential Z-DNA. !$#cross-references MUID:84261412; PMID:6086313 !$#accession I48267 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-31 ##label GIL !'##cross-references EMBL:X00624; NID:g50164; PIDN:CAA25258.1; !1PID:g50165 REFERENCE A22333 !$#authors Erhart, M.A.; Simons, K.S.; Weaver, S. !$#journal Mol. Biol. Evol. (1985) 2:304-320 !$#title Evolution of the mouse beta-globin genes: a recent gene !1conversion in the Hbb-s haplotype. !$#cross-references MUID:88216120; PMID:3870864 !$#accession A22333 !'##molecule_type DNA !'##residues 2-13,'G',15-20,'A',22-139,'A',141-147 ##label ERH !'##experimental_source strain C57BL/10 REFERENCE I49722 !$#authors Curtis, P.J.; Mantei, N.; Weissmann, C. !$#journal Cold Spring Harb. Symp. Quant. Biol. (1978) 42:971-984 !$#title Characterization and kinetics of sythesis of 15S beta-globin !1RNA, a putative precursor of beta-globin mRNA. !$#cross-references MUID:78237863; PMID:277329 !$#accession I49726 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 87-109 ##label CUR !'##cross-references GB:M19236; NID:g193774; PIDN:AAA37788.1; !1PID:g193775 REFERENCE I46716 !$#authors Pavlakis, G.N.; Lockard, R.E.; Vamvakopoulos, N.; Rieser, !1L.; RajBhandary, U.L.; Vournakis, J.N. !$#journal Cell (1980) 19:91-102 !$#title Secondary structure of mouse and rabbit alpha- and !1beta-globin mRNAs: Differential accessibility of alpha and !1beta initiator AUG codons towards nucleases. !$#cross-references MUID:80132479; PMID:7357610 !$#accession I49723 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-52 ##label PAV !'##cross-references GB:M10524; NID:g193766; PIDN:AAA37785.1; !1PID:g193767 REFERENCE A90293 !$#authors Gilman, J.G. !$#journal Biochem. J. (1976) 159:43-53 !$#title Mouse haemoblogin beta chains. Comparative sequence data on !1adult major and minor beta chains from two species, Mus !1musculus and Mus cervicolor. !$#cross-references MUID:77065139; PMID:999642 !$#contents annotation; allelic variants !$#note this paper summarizes and revises the work from various !1authors on the differences between the beta chain alleles !1found in the laboratory mouse, Mus musculus; the beta chain !1s allele, characteristic of North American wild mice, !1differs from that shown in having 14-Gly, 21-Ala, and !1140-Ala COMMENT The hemoglobin beta major d allele sequence is shown. See !1also the entry for the hemoglobin beta minor chain, !1PIR:HBMSN1. GENETICS !$#gene Hbb1 !$#introns 31/2; 105/3 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-147 #product hemoglobin beta major chain, d allele !8#status experimental #label MAD\ !$2-13,'G',15-20,'A', !$22-139,'A',141-147 #product hemoglobin beta major chain, s allele !8#status predicted #label MAS\ !$4-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 147 #molecular-weight 15840 #checksum 2746 SEQUENCE /// ENTRY HBMSN1 #type complete TITLE hemoglobin beta minor chain - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 29-Jul-1981 #sequence_revision 29-Jul-1981 #text_change 03-Mar-2000 ACCESSIONS B90790; A02405 REFERENCE A90790 !$#authors Konkel, D.A.; Maizel Jr., J.V.; Leder, P. !$#journal Cell (1979) 18:865-873 !$#title The evolution and sequence comparison of two recently !1diverged mouse chromosomal beta-globin genes. !$#cross-references MUID:80090038; PMID:519759 !$#accession B90790 !'##molecule_type DNA !'##residues 1-146 ##label KON !'##cross-references GB:V00722; NID:g50155; PIDN:CAA24101.1; PID:g50156 !'##experimental_source strain BALB/c REFERENCE A90293 !$#authors Gilman, J.G. !$#journal Biochem. J. (1976) 159:43-53 !$#title Mouse haemoblogin beta chains. Comparative sequence data on !1adult major and minor beta chains from two species, Mus !1musculus and Mus cervicolor. !$#cross-references MUID:77065139; PMID:999642 !$#contents annotation; allelic variants !$#note the p-minor sequence differs from that shown at least in !1having 22-Ala and 23-Ile COMMENT The hemoglobin beta minor d allele sequence is shown. See !1also the entry for the hemoglobin beta major chain, !1PIR:HBMS. GENETICS !$#gene Hbb2 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15747 #checksum 9830 SEQUENCE /// ENTRY HBOL #type complete TITLE hemoglobin beta chain - Ehrenberg's mole-rat ORGANISM #formal_name Spalax leucodon ehrenbergi #common_name Ehrenberg's mole-rat DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 03-Mar-2000 ACCESSIONS A02406; B24658 REFERENCE A91734 !$#authors Kleinschmidt, T.; Nevo, E.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1984) 365:531-537 !$#title The primary structure of the hemoglobin of the mole rat !1(Spalax ehrenbergi, Rodentia, chromosome species 60). !$#cross-references MUID:84287390; PMID:6469215 !$#accession A02406 !'##molecule_type protein !'##residues 1-146 ##label KLE !'##note peptides were positioned by homology with the human sequence CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15784 #checksum 3333 SEQUENCE /// ENTRY HBRT #type complete TITLE hemoglobin beta-II chain - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 24-Apr-1984 #sequence_revision 01-Dec-1995 #text_change 03-Mar-2000 ACCESSIONS S06748; A94602; A91460; B26903; S34720; A02407 REFERENCE S06748 !$#authors Woo, C.; Lam, V.M.S.; Tam, J.W.O. !$#journal Nucleic Acids Res. (1989) 17:8870 !$#title cDNA sequences of two beta-globin genes in a Sprague-Dawley !1rat. !$#cross-references MUID:90067865; PMID:2587229 !$#accession S06748 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-147 ##label WOO !'##cross-references EMBL:X16417; NID:g55822; PIDN:CAA34439.1; !1PID:g55823 !'##experimental_source clone RBGM1 REFERENCE A94602 !$#authors Garrick, L.M.; Sloan, R.L.; Ryan, T.W.; Klonowski, T.J.; !1Garrick, M.D. !$#submission submitted to the Atlas, October 1977 !$#accession A94602 !'##molecule_type protein !'##residues 2-123,'S',125-147 ##label GA1 !'##note the residues at positions 94 and 125 were identified as Asp and !1Cys, respectively !'##note a variant of the sequence shown has 58-Ala, 87-Asn, 89-Thr, and !1123-Thr REFERENCE A91460 !$#authors Garrick, L.M.; Klonowski, T.J.; Sloan, R.L.; Ryan, T.W.; !1Garrick, M.D. !$#journal Fed. Proc. (1977) 36:758 !$#accession A91460 !'##molecule_type protein !'##residues 2-123,'S',125-147 ##label GA2 REFERENCE A90135 !$#authors Satoh, H.; Fujii, H.; Okazaki, T. !$#journal Biochem. Biophys. Res. Commun. (1987) 146:618-624 !$#title Molecular cloning and sequence analysis of two rat major !1globin cDNAs. !$#cross-references MUID:87298485; PMID:3619896 !$#accession B26903 !'##molecule_type mRNA !'##residues 1-13,'A',15-147 ##label SAT !'##cross-references GB:M17084; NID:g204569; PIDN:AAA41309.1; !1PID:g204570 !'##note the authors translated the codon GCC for residue 14 as Gly REFERENCE S34719 !$#authors Inokuchi, N.; Iwahara, S.I.; Satoh, H.; Nagoe, Y.; Okazaki, !1T. !$#submission submitted to the EMBL Data Library, July 1992 !$#description Organization structure and expression of rat beta-globin !1genes. !$#accession S34720 !'##status preliminary !'##molecule_type DNA !'##residues 1-147 ##label INO !'##cross-references EMBL:X67613; NID:g395938; PIDN:CAA47873.1; !1PID:g395939 GENETICS !$#introns 31/2; 105/3 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-147 #product hemoglobin beta-II chain #status predicted !8#label MAT\ !$4-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 147 #molecular-weight 15979 #checksum 2088 SEQUENCE /// ENTRY HBVOY #type complete TITLE hemoglobin beta chain - yellow-cheeked vole (tentative sequence) ORGANISM #formal_name Microtus xanthognathus #common_name yellow-cheeked vole DATE 29-Jul-1981 #sequence_revision 29-Jul-1981 #text_change 11-May-2000 ACCESSIONS A02408 REFERENCE A02408 !$#authors Duffy, L.K.; Genaux, C.T. !$#journal Comp. Biochem. Physiol. B (1977) 56:143-146 !$#title The primary structure of the hemoglobin beta-chain of !1Microtus xanthognathus. !$#cross-references MUID:77067724; PMID:318611 !$#accession A02408 !'##molecule_type protein !'##residues 1-146 ##label DUF CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15672 #checksum 184 SEQUENCE /// ENTRY HBOZ #type complete TITLE hemoglobin beta chain - muskrat ORGANISM #formal_name Ondatra zibethicus #common_name muskrat DATE 20-Sep-1984 #sequence_revision 20-Sep-1984 #text_change 03-Mar-2000 ACCESSIONS A02409 REFERENCE A91716 !$#authors Bieber, F.A.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1983) 364:1527-1536 !$#title The primary structure of the hemoglobin of the musk-rat !1(Ondatra zibethica). !$#cross-references MUID:84110063; PMID:6363267 !$#accession A02409 !'##molecule_type protein !'##residues 1-146 ##label BIE !'##note the tryptic peptides and the prolyl peptide (residues 100-146) !1were sequenced and ordered by homology CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15724 #checksum 72 SEQUENCE /// ENTRY HBHY #type complete TITLE hemoglobin beta chain - golden hamster ORGANISM #formal_name Mesocricetus auratus #common_name golden hamster DATE 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 03-Mar-2000 ACCESSIONS A02410 REFERENCE A92758 !$#authors Braunitzer, G.; Schrank, B.; Stangl, A.; Wiesner, H. !$#journal J. Chem. Soc. Pak. (1980) 2:1-7 !$#title Respiration at high altitudes, !1phosphate-protein-interaction: sequence of the hemoglobins !1of the hamster (Mesocricetus aureatus) and the camel !1(Camelus ferus, Camelidae). !$#accession A02410 !'##molecule_type protein !'##residues 1-146 ##label BRA CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15860 #checksum 8794 SEQUENCE /// ENTRY HBGP #type complete TITLE hemoglobin beta chain - guinea pig (tentative sequence) ORGANISM #formal_name Cavia porcellus #common_name guinea pig DATE 30-Apr-1980 #sequence_revision 30-Apr-1980 #text_change 31-Mar-2000 ACCESSIONS A02411 REFERENCE A91685 !$#authors Braunitzer, G.; Schrank, B.; Stangl, A.; Wiesner, H. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1979) 360:1941-1946 !$#title Hoehenatmung, Phosphat-Protein-Wechselwirkung: die Sequenz !1der Haemoglobine des Meerschweinchens und des Dromedars. !$#cross-references MUID:80114125; PMID:527943 !$#accession A02411 !'##molecule_type protein !'##residues 1-146 ##label BRA CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15921 #checksum 8400 SEQUENCE /// ENTRY HGHUA #type complete TITLE hemoglobin gamma-A chain [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1980 #sequence_revision 30-Jun-1993 #text_change 23-Mar-2001 ACCESSIONS A90803; I37420; A93770; I37413; I59428; S07669; S21402; !1A02412 REFERENCE A90803 !$#authors Slightom, J.L.; Blechl, A.E.; Smithies, O. !$#journal Cell (1980) 21:627-638 !$#title Human fetal G-gamma- and A-gamma globin genes: complete !1nucleotide sequences suggest that DNA can be exchanged !1between these duplicated genes. !$#cross-references MUID:81064665; PMID:7438203 !$#accession A90803 !'##molecule_type DNA !'##residues 1-147 ##label SLI !'##cross-references EMBL:V00513; NID:g31728; PIDN:CAA23771.1; !1PID:g31729; EMBL:V00514; NID:g31730; PID:g31731 !'##note nucleotide sequences of two allelic gamma-A genes and the !1nonallelic gamma-G gene are given. Protein chains coded by !1the gamma-A alleles are identical REFERENCE I37419 !$#authors Shen, S.H.; Slightom, J.L.; Smithies, O. !$#journal Cell (1981) 26:191-203 !$#title A history of the human fetal globin gene duplication. !$#cross-references MUID:82137053; PMID:7332928 !$#accession I37420 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-147 ##label SHE !'##cross-references EMBL:V00517; NID:g31759; PIDN:CAA23776.1; !1PID:g31761 REFERENCE A93770 !$#authors Schroeder, W.A.; Huisman, T.H.J.; Shelton, J.R.; Shelton, !1J.B.; Kleihauer, E.F.; Dozy, A.M.; Robberson, B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1968) 60:537-544 !$#title Evidence for multiple structural genes for the gamma chain !1of human fetal hemoglobin. !$#cross-references MUID:69076676; PMID:5248810 !$#accession A93770 !'##molecule_type protein !'##residues 135-144 ##label SCH !'##note the nonallelic gamma chains differ from each other in having !1137-Ala or 137-Gly REFERENCE I37413 !$#authors Poon, R.; Kan, Y.W.; Boyer, H.W. !$#journal Nucleic Acids Res. (1978) 5:4625-4630 !$#title Sequence of the 3'-noncoding and adjacent coding regions of !1human gamma-globin mRNA. !$#cross-references MUID:79136489; PMID:318163 !$#accession I37413 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 129-147 ##label POO !'##cross-references EMBL:V00512; NID:g31726; PIDN:CAA23770.1; !1PID:g31727 REFERENCE I59428 !$#authors Gelinas, R.; Yagi, M.; Endlich, B.; Lotshaw, C.; Kazazian, !1H.H. !$#journal Prog. Clin. Biol. Res. (1985) 191:125-139 !$#title Sequences of G-gamma, A-gamma, and beta genes of the Greek !1(A-gamma) HPFH mutant: evidence for a distal CCAAT box !1mutation in the A-gamma gene. !$#cross-references MUID:86017015; PMID:2413469 !$#accession I59428 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-123 ##label GEL !'##cross-references GB:M32724; NID:g183831; PIDN:AAA35953.1; !1PID:g183832 REFERENCE S03522 !$#authors Powers, P.A.; Smithies, O. !$#journal Genetics (1986) 112:343-358 !$#title Short gene conversions in the human fetal globin gene !1region: a by-product of chromosome pairing during meiosis? !$#cross-references MUID:86083145; PMID:2416635 !$#accession S07669 !'##molecule_type DNA !'##residues 100-147 ##label POW !'##cross-references GB:M27553; EMBL:X06490; NID:g31765; !1PIDN:CAA29779.1; PID:g1335077; PID:g1335078 REFERENCE S21402 !$#authors Dmitrenko, V.V.; Kavsan, V.M. !$#submission submitted to the EMBL Data Library, September 1990 !$#description Nucleotide sequence of mitochondrial cytochrome C oxydase II !1from human fetal liver. !$#accession S21402 !'##molecule_type mRNA !'##residues 123-147 ##label DMI !'##cross-references EMBL:X55655; NID:g31639; PIDN:CAA39188.1; !1PID:g31640 REFERENCE A92082 !$#authors Stegink, L.D.; Meyer, P.D.; Brummel, M.C. !$#journal J. Biol. Chem. (1971) 246:3001-3007 !$#title Human fetal hemoglobin F1. !$#cross-references MUID:71166470; PMID:5554303 !$#contents annotation !$#note the amino ends of both gamma chains are acetylated in the !1minor hemoglobin F1 tetramer GENETICS !$#gene GDB:HBG1 !'##cross-references GDB:119300; OMIM:142200 !$#map_position 11p15.5-11p15.5 !$#introns 31/2; 105/3 COMPLEX two gamma chains (see also PIR:HGHUG) combine in !1heterotetramers with two alpha chains to form fetal !1hemoglobin F; at low alpha chain concentrations, gamma !1chains can combine in homotetramers to form hemoglobin Barts FUNCTION !$#description in erythrocytes binds and transports molecular oxygen from !1placenta to tissues CLASSIFICATION #superfamily globin; globin homology KEYWORDS acetylated amino end; blood; chromoprotein; erythrocyte; !1fetus; heme; heterotetramer; homotetramer; iron; !1metalloprotein; oxygen carrier FEATURE !$2-147 #product hemoglobin gamma-A chain #status !8experimental #label MAT\ !$4-147 #domain globin homology #label GLB\ !$2 #modified_site acetylated amino end (Gly) (in mature !8form) (partial) #status experimental\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 147 #molecular-weight 16140 #checksum 5358 SEQUENCE /// ENTRY HGCZA #type complete TITLE hemoglobin gamma-A chain - chimpanzee ALTERNATE_NAMES hemoglobin gamma-2 chain ORGANISM #formal_name Pan troglodytes #common_name chimpanzee DATE 30-Jun-1993 #sequence_revision 21-Jan-1997 #text_change 03-Mar-2000 ACCESSIONS I36940; I84427; A90581; A02412 REFERENCE I36939 !$#authors Slightom, J.L.; Chang, L.Y.; Koop, B.F.; Goodman, M. !$#journal Mol. Biol. Evol. (1985) 2:370-389 !$#title Chimpanzee fetal G-gamma and A-gamma globin gene nucleotide !1sequences provide further evidence of gene conversions in !1hominine evolution. !$#cross-references MUID:88216125; PMID:3870867 !$#accession I36940 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-147 ##label RES !'##cross-references GB:M92294; NID:g176778; PIDN:AAA35410.1; !1PID:g176779 !$#accession I84427 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-147 ##label RE2 !'##cross-references EMBL:X03110; NID:g38162; PIDN:CAA26892.1; !1PID:g38163 REFERENCE A90581 !$#authors De Jong, W.W.W. !$#journal Biochim. Biophys. Acta (1971) 251:217-226 !$#title Chimpanzee foetal haemoglobin: structure and heterogeneity !1of the gamma chain. !$#contents composition of tryptic, chymotryptic and cyanogen bromide !1peptides !$#accession A90581 !'##molecule_type protein !'##residues 2-147 ##label DEJ !'##note chimpanzee has two nonallelic gamma chains identical with the !1human gamma chains COMMENT Gamma chains normally combine in heterotetramers with two !1alpha chains to form fetal hemoglobin F, but in low alpha !1chain concentration conditions gamma chains can combine in !1homotetramers to form hemoglobin Barts. GENETICS !$#introns 31/2; 105/3 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-147 #product hemoglobin gamma-A chain #status !8experimental #label MAT\ !$4-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 147 #molecular-weight 16140 #checksum 5358 SEQUENCE /// ENTRY HGHUG #type complete TITLE hemoglobin gamma-G chain [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 23-Mar-2001 ACCESSIONS B90803; I37419; I80323; S03522; S21413; A24980; A91474; !1A90445; B93770; A02412 REFERENCE A90803 !$#authors Slightom, J.L.; Blechl, A.E.; Smithies, O. !$#journal Cell (1980) 21:627-638 !$#title Human fetal G-gamma- and A-gamma globin genes: complete !1nucleotide sequences suggest that DNA can be exchanged !1between these duplicated genes. !$#cross-references MUID:81064665; PMID:7438203 !$#accession B90803 !'##molecule_type DNA !'##residues 1-147 ##label SLI !'##cross-references EMBL:V00515; NID:g31732; PIDN:CAA23773.1; !1PID:g31733 !'##note nucleotide sequences of two allelic gamma-A genes and the !1nonallelic gamma-G gene are given. Protein chains coded by !1the gamma-A alleles are identical REFERENCE I37419 !$#authors Shen, S.H.; Slightom, J.L.; Smithies, O. !$#journal Cell (1981) 26:191-203 !$#title A history of the human fetal globin gene duplication. !$#cross-references MUID:82137053; PMID:7332928 !$#accession I37419 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-147 ##label SHE !'##cross-references EMBL:V00517; NID:g31759; PIDN:CAA23775.1; !1PID:g31760 REFERENCE I59428 !$#authors Gelinas, R.; Yagi, M.; Endlich, B.; Lotshaw, C.; Kazazian, !1H.H. !$#journal Prog. Clin. Biol. Res. (1985) 191:125-139 !$#title Sequences of G-gamma, A-gamma, and beta genes of the Greek !1(A-gamma) HPFH mutant: evidence for a distal CCAAT box !1mutation in the A-gamma gene. !$#cross-references MUID:86017015; PMID:2413469 !$#accession I80323 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-101 ##label GEL !'##cross-references GB:M32723; NID:g183850; PIDN:AAA35955.1; !1PID:g183851 REFERENCE S03522 !$#authors Powers, P.A.; Smithies, O. !$#journal Genetics (1986) 112:343-358 !$#title Short gene conversions in the human fetal globin gene !1region: a by-product of chromosome pairing during meiosis? !$#cross-references MUID:86083145; PMID:2416635 !$#accession S03522 !'##molecule_type DNA !'##residues 100-147 ##label POW !'##cross-references GB:M27553; EMBL:X06490; NID:g31765; !1PIDN:CAB58151.1; PID:g6048259 REFERENCE S21402 !$#authors Dmitrenko, V.V.; Kavsan, V.M. !$#submission submitted to the EMBL Data Library, September 1990 !$#description Nucleotide sequence of mitochondrial cytochrome C oxydase II !1from human fetal liver. !$#accession S21413 !'##molecule_type mRNA !'##residues 123-147 ##label DMI !'##cross-references EMBL:X55657; NID:g31722; PIDN:CAA39190.1; !1PID:g31723 REFERENCE A24980 !$#authors Lang, K.M.; Spritz, R.A. !$#journal Gene (1985) 33:191-196 !$#title Cloning specific complete polyadenylated 3'-terminal cDNA !1segments. !$#cross-references MUID:85205333; PMID:2581851 !$#accession A24980 !'##molecule_type mRNA !'##residues 122-147 ##label LAN !'##cross-references GB:M11427; NID:g183868; PIDN:AAA35957.1; !1PID:g386767 REFERENCE A91474 !$#authors Cavallesco, C.; Forget, B.G.; deRiel, J.K.; Wilson, L.B.; !1Wilson, J.T.; Weissman, S.M. !$#journal Gene (1980) 12:215-221 !$#title Nucleotide sequence of human G-gamma globin messenger RNA. !$#cross-references MUID:81237783; PMID:7250702 !$#accession A91474 !'##molecule_type mRNA !'##residues 2-147 ##label CAV !'##cross-references GB:M15386; NID:g183884; PIDN:AAB50159.1; !1PID:g183885 REFERENCE A90445 !$#authors Schroeder, W.A.; Shelton, J.R.; Shelton, J.B.; Cormick, J.; !1Jones, R.T. !$#journal Biochemistry (1963) 2:992-1008 !$#title The amino acid sequence of the gamma chain of human fetal !1hemoglobin. !$#accession A90445 !'##molecule_type protein !'##residues 2-147 ##label SC1 REFERENCE A93770 !$#authors Schroeder, W.A.; Huisman, T.H.J.; Shelton, J.R.; Shelton, !1J.B.; Kleihauer, E.F.; Dozy, A.M.; Robberson, B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1968) 60:537-544 !$#title Evidence for multiple structural genes for the gamma chain !1of human fetal hemoglobin. !$#cross-references MUID:69076676; PMID:5248810 !$#accession B93770 !'##molecule_type protein !'##residues 135-144 ##label SC2 !'##note the nonallelic gamma chains differ from each other in having !1137-Ala or 137-Gly REFERENCE A92082 !$#authors Stegink, L.D.; Meyer, P.D.; Brummel, M.C. !$#journal J. Biol. Chem. (1971) 246:3001-3007 !$#title Human fetal hemoglobin F1. !$#cross-references MUID:71166470; PMID:5554303 !$#contents annotation !$#note the amino ends of both gamma chains are acetylated in the !1minor hemoglobin F1 tetramer REFERENCE A50125 !$#authors Frier Jr., J.A. !$#submission submitted to the Brookhaven Protein Data Bank, August 1976 !$#cross-references PDB:1FDH !$#contents annotation; X-ray crystallography, 2.5 angstroms, residues !12-147 REFERENCE A45926 !$#authors Frier, J.A.; Perutz, M.F. !$#journal J. Mol. Biol. (1977) 112:97-112 !$#title Structure of human foetal deoxyhaemoglobin. !$#cross-references MUID:77230464; PMID:881729 !$#contents annotation; X-ray crystallography, 2.5 angstroms GENETICS !$#gene GDB:HBG2 !'##cross-references GDB:119301; OMIM:142250 !$#map_position 11p15.5-11p15.5 !$#introns 31/2; 105/3 COMPLEX two gamma chains (see also PIR:HGHUA) combine in !1heterotetramers with two alpha chains to form fetal !1hemoglobin F; at low alpha chain concentrations, gamma !1chains can combine in homotetramers to form hemoglobin Barts FUNCTION !$#description in erythrocytes binds and transports molecular oxygen from !1placenta to tissues CLASSIFICATION #superfamily globin; globin homology KEYWORDS acetylated amino end; blood; chromoprotein; erythrocyte; !1fetus; heme; heterotetramer; homotetramer; iron; !1metalloprotein; oxygen carrier FEATURE !$2-147 #product hemoglobin gamma-G chain #status !8experimental #label MAT\ !$4-147 #domain globin homology #label GLB\ !$2 #modified_site acetylated amino end (Gly) (in mature !8form) (partial) #status experimental\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status experimental\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status experimental SUMMARY #length 147 #molecular-weight 16126 #checksum 5496 SEQUENCE /// ENTRY HGCZG #type complete TITLE hemoglobin gamma-G chain - chimpanzee ALTERNATE_NAMES hemoglobin gamma-1 chain ORGANISM #formal_name Pan troglodytes #common_name chimpanzee DATE 31-May-1996 #sequence_revision 21-Jan-1997 #text_change 03-Mar-2000 ACCESSIONS I36939; I61853 REFERENCE I36939 !$#authors Slightom, J.L.; Chang, L.Y.; Koop, B.F.; Goodman, M. !$#journal Mol. Biol. Evol. (1985) 2:370-389 !$#title Chimpanzee fetal G-gamma and A-gamma globin gene nucleotide !1sequences provide further evidence of gene conversions in !1hominine evolution. !$#cross-references MUID:88216125; PMID:3870867 !$#accession I36939 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-147 ##label RES !'##cross-references GB:M92294; NID:g176778; PIDN:AAA35411.1; !1PID:g176780 !$#accession I61853 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-147 ##label RE2 !'##cross-references EMBL:X03109; NID:g38219; PIDN:CAA26891.1; !1PID:g38220 REFERENCE A90581 !$#authors De Jong, W.W.W. !$#journal Biochim. Biophys. Acta (1971) 251:217-226 !$#title Chimpanzee foetal haemoglobin: structure and heterogeneity !1of the gamma chain. !$#contents annotation; composition of tryptic, chymotryptic and !1cyanogen bromide peptides !$#note chimpanzee has two nonallelic gamma chains identical with !1the human gamma chains COMMENT Gamma chains normally combine in heterotetramers with two !1alpha chains to form fetal hemoglobin F, but in low alpha !1chain concentration conditions gamma chains can combine in !1homotetramers to form hemoglobin Barts. GENETICS !$#introns 31/2; 105/3 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; heme; iron; metalloprotein; oxygen !1carrier FEATURE !$2-147 #product hemoglobin gamma-G chain #status !8experimental #label MAT\ !$4-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 147 #molecular-weight 16126 #checksum 5496 SEQUENCE /// ENTRY I37025 #type complete TITLE hemoglobin gamma-G chain - gorilla ALTERNATE_NAMES hemoglobin gamma-1 chain ORGANISM #formal_name Gorilla gorilla #common_name gorilla DATE 31-May-1996 #sequence_revision 31-May-1996 #text_change 03-Mar-2000 ACCESSIONS I37025; I37055 REFERENCE I37022 !$#authors Scott, A.F.; Heath, P.; Trusko, S.; Boyer, S.H.; Prass, W.; !1Goodman, M.; Czelusniak, J.; Chang, L.Y.; Slightom, J.L. !$#journal Mol. Biol. Evol. (1984) 1:371-389 !$#title The sequence of the gorilla fetal globin genes: evidence for !1multiple gene conversions in human evolution. !$#cross-references MUID:88174320; PMID:6599972 !$#accession I37025 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-147 ##label SCO !'##cross-references EMBL:X03111; GB:M23863; NID:g22887; !1PIDN:CAA26893.1; PID:g22888; GB:M92295; NID:g177052; !1PID:g177054 GENETICS !$#gene HBG1 !$#introns 31/2; 105/3 COMPLEX Two gamma chains combine in heterotetramers with two alpha !1chains to form fetal hemoglobin F; at low alpha chain !1concentrations, gamma chains can combine in homotetramers to !1form hemoglobin Barts. FUNCTION !$#description in erythrocytes binds and transports molecular oxygen from !1placenta to tissues CLASSIFICATION #superfamily globin; globin homology KEYWORDS acetylated amino end; blood; chromoprotein; erythrocyte; !1fetus; heme; heterotetramer; homotetramer; iron; !1metalloprotein; oxygen carrier FEATURE !$2-147 #product hemoglobin gamma-A chain #status predicted !8#label MAT\ !$4-147 #domain globin homology #label GLB\ !$2 #modified_site acetylated amino end (Gly) (in mature !8form) #status predicted\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 147 #molecular-weight 16126 #checksum 5496 SEQUENCE /// ENTRY I37022 #type complete TITLE hemoglobin gamma-A chain - gorilla ALTERNATE_NAMES hemoglobin gamma-2 chain ORGANISM #formal_name Gorilla gorilla #common_name gorilla DATE 31-May-1996 #sequence_revision 31-May-1996 #text_change 03-Mar-2000 ACCESSIONS I37022; I37056 REFERENCE I37022 !$#authors Scott, A.F.; Heath, P.; Trusko, S.; Boyer, S.H.; Prass, W.; !1Goodman, M.; Czelusniak, J.; Chang, L.Y.; Slightom, J.L. !$#journal Mol. Biol. Evol. (1984) 1:371-389 !$#title The sequence of the gorilla fetal globin genes: evidence for !1multiple gene conversions in human evolution. !$#cross-references MUID:88174320; PMID:6599972 !$#accession I37022 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-147 ##label SCO !'##cross-references EMBL:X03112; GB:M23864; NID:g22861; !1PIDN:CAA26894.1; PID:g22862; GB:M92295; NID:g177052; !1PID:g177053 GENETICS !$#gene HBG2 !$#introns 31/2; 105/3 COMPLEX Two gamma chains combine in heterotetramers with two alpha !1chains to form fetal hemoglobin F; at low alpha chain !1concentrations, gamma chains can combine in homotetramers to !1form hemoglobin Barts. FUNCTION !$#description in erythrocytes binds and transports molecular oxygen from !1placenta to tissues CLASSIFICATION #superfamily globin; globin homology KEYWORDS acetylated amino end; blood; chromoprotein; erythrocyte; !1fetus; heme; heterotetramer; homotetramer; iron; !1metalloprotein; oxygen carrier FEATURE !$2-147 #product hemoglobin gamma-A chain #status predicted !8#label MAT\ !$4-147 #domain globin homology #label GLB\ !$2 #modified_site acetylated amino end (Gly) (in mature !8form) #status predicted\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 147 #molecular-weight 16110 #checksum 5745 SEQUENCE /// ENTRY HGMQR #type complete TITLE hemoglobin gamma-1 chain - rhesus macaque ORGANISM #formal_name Macaca mulatta #common_name rhesus macaque DATE 17-Mar-1987 #sequence_revision 19-Oct-1995 #text_change 03-Mar-2000 ACCESSIONS A31109; A02414 REFERENCE A31109 !$#authors Slightom, J.L.; Koop, B.F.; Xu, P.; Goodman, M. !$#journal J. Biol. Chem. (1988) 263:12427-12438 !$#title Rhesus fetal globin genes. Concerted gene evolution in the !1descent of higher primates. !$#cross-references MUID:88315036; PMID:3410846 !$#accession A31109 !'##molecule_type DNA !'##residues 1-147 ##label SLI !'##cross-references GB:M19434; GB:J03938; NID:g342107; PIDN:AAA36846.1; !1PID:g342110 !'##note the authors translated the codon AAT for residue 20 as Asp REFERENCE A02414 !$#authors Mahoney, W.C.; Nute, P.E. !$#journal Biochemistry (1980) 19:4436-4442 !$#title Fetal hemoglobin of the Rhesus monkey, Macaca mulatta: !1complete primary structure of the gamma chain. !$#cross-references MUID:81000303; PMID:6157408 !$#accession A02414 !'##molecule_type protein !'##residues 2-147 ##label MAH GENETICS !$#gene gamma-1 !$#introns 31/2; 105/3 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; embryo; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-147 #product hemoglobin gamma-1 chain #status !8experimental #label MAT\ !$4-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 147 #molecular-weight 16101 #checksum 5540 SEQUENCE /// ENTRY HGMQJ #type complete TITLE hemoglobin gamma chain - Japanese macaque ORGANISM #formal_name Macaca fuscata #common_name Japanese macaque DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 03-Mar-2000 ACCESSIONS A02415 REFERENCE A02415 !$#authors Takenaka, A.; Takenaka, O.; Ohuchi, M.; Nakamura, S.; !1Takahashi, K. !$#journal Hemoglobin (1986) 10:1-13 !$#title Complete amino acid sequence of gamma chain of fetal !1hemoglobin of Japanese macaque (Macaca fuscata). !$#cross-references MUID:86167516; PMID:2420747 !$#accession A02415 !'##molecule_type protein !'##residues 1-146 ##label TAK CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; embryo; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15970 #checksum 3154 SEQUENCE /// ENTRY HGBAY #type complete TITLE hemoglobin gamma chain - yellow baboon ORGANISM #formal_name Papio cynocephalus, Papio hamadryas cynocephalus #common_name yellow baboon DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 03-Mar-2000 ACCESSIONS A02416 REFERENCE A02416 !$#authors Nute, P.E.; Mahoney, W.C. !$#journal Hemoglobin (1979) 3:399-410 !$#title Complete sequence of the gamma chain from the fetal !1hemoglobin of the baboon, Papio cynocephalus. !$#cross-references MUID:80071586; PMID:511581 !$#accession A02416 !'##molecule_type protein !'##residues 1-146 ##label NUT !'##note both Ile and Val were found at position 75 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; embryo; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15970 #checksum 3154 SEQUENCE /// ENTRY HGMQP #type complete TITLE hemoglobin gamma chain - pig-tailed macaque ORGANISM #formal_name Macaca nemestrina #common_name pig-tailed macaque DATE 30-Jun-1979 #sequence_revision 29-Jul-1981 #text_change 03-Mar-2000 ACCESSIONS A02413 REFERENCE A02413 !$#authors Nute, P.E.; Mahoney, W.C. !$#journal Biochemistry (1979) 18:467-472 !$#title Complete amino acid sequence of the gamma chain from the !1major fetal hemoglobin of the pig-tailed macaque, Macaca !1nemestrina. !$#cross-references MUID:79124683; PMID:105752 !$#accession A02413 !'##molecule_type protein !'##residues 1-146 ##label NUT !'##note the residues responsible for the gamma-fast sequence are not !1known COMMENT The gamma-slow sequence is shown. CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; embryo; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15989 #checksum 3184 SEQUENCE /// ENTRY HGMQR2 #type complete TITLE hemoglobin gamma-2 chain - rhesus macaque ORGANISM #formal_name Macaca mulatta #common_name rhesus macaque DATE 28-Feb-1992 #sequence_revision 19-Oct-1995 #text_change 03-Mar-2000 ACCESSIONS B31109; S21893 REFERENCE A31109 !$#authors Slightom, J.L.; Koop, B.F.; Xu, P.; Goodman, M. !$#journal J. Biol. Chem. (1988) 263:12427-12438 !$#title Rhesus fetal globin genes. Concerted gene evolution in the !1descent of higher primates. !$#cross-references MUID:88315036; PMID:3410846 !$#accession B31109 !'##molecule_type DNA !'##residues 1-147 ##label SLI !'##cross-references GB:M19433; GB:J03938; NID:g342106; PIDN:AAA36845.1; !1PID:g342109 !'##note the authors translated the codon AAT for residue 20 as Asp REFERENCE S21892 !$#authors Fitch, D.H.A.; Bailey, W.J.; Tagle, D.A.; Goodman, M.; !1Slightom, J.L. !$#submission submitted to the EMBL Data Library, June 1990 !$#description Duplication of the gamma-globin gene mediated by repetitive !1L1 LINE sequences in an early ancestor of simian primates. !$#accession S21893 !'##molecule_type DNA !'##residues 1-147 ##label FIT !'##cross-references EMBL:X53419; NID:g38087; PIDN:CAA37498.1; !1PID:g38088 GENETICS !$#gene gamma-2 !$#introns 31/2; 105/3 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; embryo; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-147 #product hemoglobin gamma-1 chain #status predicted !8#label MAT\ !$4-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 147 #molecular-weight 16127 #checksum 5608 SEQUENCE /// ENTRY HGGC #type complete TITLE hemoglobin gamma chain - thick-tailed bush baby ORGANISM #formal_name Galago crassicaudatus, Otolemur crassicaudatus #common_name thick-tailed bush baby DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 03-Mar-2000 ACCESSIONS S01376; S20204 REFERENCE S01375 !$#authors Tagle, D.A.; Koop, B.F.; Goodman, M.; Slightom, J.L.; Hess, !1D.L.; Jones, R.T. !$#journal J. Mol. Biol. (1988) 203:439-455 !$#title Embryonic epsilon and gamma globin genes of a prosimian !1primate (Galago crassicaudatus). Nucleotide and amino acid !1sequences, developmental regulation and phylogenetic !1footprints. !$#cross-references MUID:89068695; PMID:3199442 !$#accession S01376 !'##molecule_type DNA !'##residues 1-147 ##label TAG !'##cross-references EMBL:M36305; NID:g176979; PIDN:AAA35447.1; !1PID:g176980 !$#accession S20204 !'##molecule_type protein !'##residues 2-8,'L',10-120,'R',122;135-144,'L',146-147 ##label TAG2 !'##note the authors translated the codon TCG for residue 131 as Cys GENETICS !$#introns 31/2; 105/3 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$2-147 #product hemoglobin gamma chain #status experimental !8#label MAT\ !$4-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 147 #molecular-weight 16170 #checksum 3567 SEQUENCE /// ENTRY HGMKS #type complete TITLE hemoglobin gamma chain - black-handed spider monkey ORGANISM #formal_name Ateles geoffroyi #common_name black-handed spider monkey DATE 30-Sep-1987 #sequence_revision 19-Oct-1995 #text_change 03-Mar-2000 ACCESSIONS S21892; A24729 REFERENCE S21892 !$#authors Fitch, D.H.A.; Bailey, W.J.; Tagle, D.A.; Goodman, M.; !1Slightom, J.L. !$#submission submitted to the EMBL Data Library, June 1990 !$#description Duplication of the gamma-globin gene mediated by repetitive !1L1 LINE sequences in an early ancestor of simian primates. !$#accession S21892 !'##molecule_type DNA !'##residues 1-147 ##label FIT !'##cross-references EMBL:X53420; NID:g22769; PIDN:CAA37499.1; !1PID:g22770 REFERENCE A57081 !$#authors Fitch, D.H.A.; Bailey, W.J.; Tagle, D.A.; Goodman, M.; Sieu, !1L.; Slightom, J.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:7396-7400 !$#title Duplication of the gamma-globin gene mediated by L1 long !1interspersed repetitive elements in an early ancestor of !1simian primates. !$#cross-references MUID:91334472; PMID:1908094 !$#contents annotation; identification of genes REFERENCE A24729 !$#authors Giebel, L.B.; van Santen, V.L.; Slightom, J.L.; Spritz, R.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:6985-6989 !$#title Nucleotide sequence, evolution, and expression of the fetal !1globin gene of the spider monkey Ateles geoffroyi. !$#cross-references MUID:86016820; PMID:2413451 !$#accession A24729 !'##molecule_type DNA !'##residues 2-147 ##label GIE !'##cross-references GB:M36773; NID:g342382; PIDN:AAA36926.1; !1PID:g342383 !'##note the authors translated the codon AAT for residue 19 as Asp; the !1sequence reported includes the initiator Met GENETICS !$#introns 31/2; 105/3 !$#note contrary to early reports, there are two gamma globin genes, !1only one of which is functional COMPLEX Fetal hemoglobin F consists of two gamma and two alpha !1chains. CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; fetus; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$4-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 147 #molecular-weight 15940 #checksum 6169 SEQUENCE /// ENTRY HBRB3 #type complete TITLE hemoglobin gamma chain - rabbit ALTERNATE_NAMES hemoglobin beta-3 chain ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 03-Mar-2000 ACCESSIONS A02417 REFERENCE A02417 !$#authors Hardison, R.C. !$#journal J. Biol. Chem. (1981) 256:11780-11786 !$#title The nucleotide sequence of rabbit embryonic globin gene !1beta3. !$#cross-references MUID:82053017; PMID:6271761 !$#accession A02417 !'##molecule_type DNA !'##residues 1-147 ##label HAR !'##cross-references GB:V00883; GB:J00663; NID:g1493; PIDN:CAA24252.1; !1PID:g1494 COMMENT This protein functions as an embryonic globin, but the gene !1structure and chromosomal location resemble more closely the !1human gamma chain gene, which codes for a fetal globin. GENETICS !$#introns 31/2; 105/3 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-147 #product hemoglobin gamma chain #status predicted !8#label MAT\ !$4-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 147 #molecular-weight 16225 #checksum 4092 SEQUENCE /// ENTRY HBMSH0 #type complete TITLE hemoglobin beta-h0 chain - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 03-Mar-2000 ACCESSIONS A02418; S10115 REFERENCE A92472 !$#authors Hill, A.; Hardies, S.C.; Phillips, S.J.; Davis, M.G.; !1Hutchison III, C.A.; Edgell, M.H. !$#journal J. Biol. Chem. (1984) 259:3739-3747 !$#title Two mouse early embryonic beta-globin gene sequences. !1Evolution of the nonadult beta-globins. !$#cross-references MUID:84162046; PMID:6323438 !$#accession A02418 !'##molecule_type DNA !'##residues 1-147 ##label HIL !'##cross-references GB:J00416; NID:g193785; PIDN:AAB59637.1; !1PID:g387186 REFERENCE S10115 !$#authors Jahn, C.L.; Hutchison III, C.A.; Phillips, S.J.; Weaver, S.; !1Haigwood, N.L.; Voliva, C.F.; Edgell, M.H. !$#journal Cell (1980) 21:159-168 !$#title DNA sequence organization of the beta-globin complex in the !1BALB/c mouse. !$#cross-references MUID:81001851; PMID:6250710 !$#accession S10115 !'##molecule_type DNA !'##residues 59-60,'N',62,'T',64-79,'N',81-105 ##label JAH !'##cross-references EMBL:V00723; NID:g50157; PIDN:CAA24102.1; !1PID:g50158 COMMENT This is the minor, early embryonic beta chain. GENETICS !$#introns 31/2; 105/3 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; embryo; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$4-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 147 #molecular-weight 16406 #checksum 1987 SEQUENCE /// ENTRY HBMSH1 #type complete TITLE hemoglobin beta-h1 chain - mouse ALTERNATE_NAMES z protein ORGANISM #formal_name Mus musculus #common_name house mouse DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 03-Mar-2000 ACCESSIONS A02419; S10116; A43560 REFERENCE A92472 !$#authors Hill, A.; Hardies, S.C.; Phillips, S.J.; Davis, M.G.; !1Hutchison III, C.A.; Edgell, M.H. !$#journal J. Biol. Chem. (1984) 259:3739-3747 !$#title Two mouse early embryonic beta-globin gene sequences. !1Evolution of the nonadult beta-globins. !$#cross-references MUID:84162046; PMID:6323438 !$#accession A02419 !'##molecule_type DNA !'##residues 1-147 ##label HIL !'##cross-references GB:J00417; NID:g193787; PIDN:AAB59638.1; !1PID:g387187 REFERENCE S10115 !$#authors Jahn, C.L.; Hutchison III, C.A.; Phillips, S.J.; Weaver, S.; !1Haigwood, N.L.; Voliva, C.F.; Edgell, M.H. !$#journal Cell (1980) 21:159-168 !$#title DNA sequence organization of the beta-globin complex in the !1BALB/c mouse. !$#cross-references MUID:81001851; PMID:6250710 !$#accession S10116 !'##molecule_type DNA !'##residues 60-65,'X',67-105 ##label JAH !'##cross-references EMBL:V00724; NID:g50159; PIDN:CAA24103.1; !1PID:g50160 REFERENCE A43560 !$#authors Wilkinson, D.G.; Bailes, J.A.; Champion, J.E.; McMahon, A.P. !$#journal Development (1987) 99:493-500 !$#title A molecular analysis of mouse development from 8 to 10 days !1post coitum detects changes only in embryonic globin !1expression. !$#cross-references MUID:88029090; PMID:2444404 !$#accession A43560 !'##molecule_type mRNA !'##residues 8-85,'I',87-147 ##label WIL !'##cross-references GB:M26894; NID:g193520; PIDN:AAA37695.1; !1PID:g387174 COMMENT This gene codes for the early z protein, which is an !1embryonic beta-type chain. GENETICS !$#introns 31/2; 105/3 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; embryo; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$4-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 147 #molecular-weight 16494 #checksum 2550 SEQUENCE /// ENTRY HEHU #type complete TITLE hemoglobin epsilon chain [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 28-Feb-1980 #sequence_revision 14-Sep-1994 #text_change 08-Dec-2000 ACCESSIONS A90802; A15673; A94303; I51946; A02420 REFERENCE A90802 !$#authors Baralle, F.E.; Shoulders, C.C.; Proudfoot, N.J. !$#journal Cell (1980) 21:621-626 !$#title The primary structure of the human epsilon-globin gene. !$#cross-references MUID:81064664; PMID:6254663 !$#accession A90802 !'##molecule_type DNA !'##residues 2-147 ##label BAR !'##cross-references GB:U01317; GB:J00179; GB:J00093; GB:J00094; !1GB:J00096; GB:J00158; GB:J00159; GB:J00160; GB:J00161; !1GB:J00162; GB:J00163; GB:J00164; GB:J00165; GB:J00166; !1GB:J00167; GB:J00168; GB:J00169; GB:J00170; GB:J00171; !1GB:J00172; GB:J00173; GB:J00174; GB:J00175; GB:J00177; !1GB:J00178; GB:K01239; GB:K01890; GB:K02544; GB:M18047; !1GB:M19067; GB:M24868; GB:M24886; GB:X00423; GB:X00424; !1GB:X00672; NID:g455025; PIDN:AAA16330.1; PID:g455993 !'##note initiator Met not shown REFERENCE A15673 !$#authors Baralle, F.E.; Shoulders, C.C.; Goodbourn, S.; Jeffreys, A.; !1Proudfoot, N.J. !$#journal Nucleic Acids Res. (1980) 8:4393-4404 !$#title The 5' flanking region of human epsilon-globin gene. !$#cross-references MUID:81053776; PMID:6253916 !$#accession A15673 !'##molecule_type DNA !'##residues 1-28 ##label BA2 !'##cross-references GB:V00508 REFERENCE A94303 !$#authors Clegg, J.B. !$#journal Tex. Rep. Biol. Med. (1981) 40:23-28 !$#title Embryonic hemoglobin: sequence of the epsilon and zeta !1chains. !$#cross-references MUID:82108309; PMID:6172865 !$#accession A94303 !'##molecule_type protein !'##residues 2-142,'G',144-147 ##label CLE REFERENCE I51946 !$#authors Baralle, F.E.; Proudfoot, N.J.; Clegg, J.B. !$#journal Ann. N. Y. Acad. Sci. (1980) 344:76-82 !$#title The structural analysis of the human epsilon-globin gene and !1its products. !$#cross-references MUID:80240425; PMID:6930885 !$#accession I51946 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 63-68,'X',70-97,'XX',100-101 ##label RES !'##cross-references GB:M25037; NID:g183846; PIDN:AAA35954.1; !1PID:g183847 GENETICS !$#gene GDB:HBE1 !'##cross-references GDB:119299; OMIM:142100 !$#map_position 11p15.5-11p15.5 !$#introns 32/2; 106/3 COMPLEX two epsilon chains combine in heterotetramers with two alpha !1chains (see PIR:HAHU) to form hemoglobin Gower 2, or with !1two zeta chains (see PIR:HZHU) to form hemoglobin Gower 1 FUNCTION !$#description in erythrocytes binds and transports molecular oxygen from !1placenta to tissues !$#note a beta-type chain found in early embryos CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; embryo; erythrocyte; heme; !1heterotetramer; iron; metalloprotein; oxygen carrier FEATURE !$2-147 #product hemoglobin epsilon #status experimental !8#label MAT\ !$4-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 147 #molecular-weight 16203 #checksum 2461 SEQUENCE /// ENTRY HEGC #type complete TITLE hemoglobin epsilon chain - thick-tailed bush baby ORGANISM #formal_name Galago crassicaudatus, Otolemur crassicaudatus #common_name thick-tailed bush baby DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 03-Mar-2000 ACCESSIONS S01375; S20203 REFERENCE S01375 !$#authors Tagle, D.A.; Koop, B.F.; Goodman, M.; Slightom, J.L.; Hess, !1D.L.; Jones, R.T. !$#journal J. Mol. Biol. (1988) 203:439-455 !$#title Embryonic epsilon and gamma globin genes of a prosimian !1primate (Galago crassicaudatus). Nucleotide and amino acid !1sequences, developmental regulation and phylogenetic !1footprints. !$#cross-references MUID:89068695; PMID:3199442 !$#accession S01375 !'##molecule_type DNA !'##residues 1-147 ##label TAG !'##cross-references EMBL:M36304; NID:g176977; PIDN:AAA35446.1; !1PID:g176978 !$#accession S20203 !'##molecule_type protein !'##residues 2-43,'D',45-48;80-93,'E',95-111 ##label TAG2 GENETICS !$#introns 31/2; 105/3 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$2-147 #product hemoglobin epsilon chain #status !8experimental #label MAT\ !$4-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 147 #molecular-weight 16181 #checksum 1794 SEQUENCE /// ENTRY HEPG #type complete TITLE hemoglobin epsilon chain - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 03-Mar-2000 ACCESSIONS A02421 REFERENCE A91732 !$#authors Bieber, F.A.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1984) 365:321-334 !$#title Pre- and perinatal oxygen-transport in mammals: the !1embryonic hemoglobins of the pig (Sus scrofa domestica). !$#cross-references MUID:84210428; PMID:6724525 !$#accession A02421 !'##molecule_type protein !'##residues 1-146 ##label BIE COMMENT Hemoglobin epsilon chain is an embryonic beta-type chain. CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; embryo; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16122 #checksum 1396 SEQUENCE /// ENTRY HTPG #type complete TITLE hemoglobin theta chain - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 03-Mar-2000 ACCESSIONS A02422 REFERENCE A91732 !$#authors Bieber, F.A.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1984) 365:321-334 !$#title Pre- and perinatal oxygen-transport in mammals: the !1embryonic hemoglobins of the pig (Sus scrofa domestica). !$#cross-references MUID:84210428; PMID:6724525 !$#accession A02422 !'##molecule_type protein !'##residues 1-146 ##label BIE COMMENT Hemoglobin theta chain is an embryonic beta-type chain. CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; embryo; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15980 #checksum 1181 SEQUENCE /// ENTRY HEGT1 #type complete TITLE hemoglobin epsilon-I chain - goat ORGANISM #formal_name Capra aegagrus hircus #common_name domestic goat DATE 20-Sep-1984 #sequence_revision 20-Sep-1984 #text_change 03-Mar-2000 ACCESSIONS A02423; I46278 REFERENCE A92905 !$#authors Shapiro, S.G.; Schon, E.A.; Townes, T.M.; Lingrel, J.B. !$#journal J. Mol. Biol. (1983) 169:31-52 !$#title Sequence and linkage of the goat epsilon(I) and epsilon(II) !1beta-globin genes. !$#cross-references MUID:84010860; PMID:6312053 !$#accession A02423 !'##molecule_type DNA !'##residues 1-147 ##label SHA REFERENCE I46273 !$#authors Haynes, J.R.; Rosteck, P.R.; Schon, E.A.; Gallagher, P.M.; !1Burks, D.J.; Smith, K.; Lingrel, J.B. !$#journal J. Biol. Chem. (1980) 255:6355-6367 !$#title The isolation of the beta-a-, beta-c-, and gamma-globin !1genes and a presumptive embryonic globin gene from a goat !1DNA recombinant library. !$#cross-references MUID:80227766; PMID:6248519 !$#accession I46278 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 66-71,'X',73,'X',75-87,'E',89-97,'PXXXLD',104-105,'A', !1107-108,'QCDCDYSGYSFWQ' ##label HAY !'##cross-references GB:K00666; NID:g164160; PIDN:AAA30922.1; !1PID:g552353 COMMENT Epsilon chains are found in embryonic hemoglobins. GENETICS !$#gene epsilon-I !$#introns 31/2; 105/3 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; embryo; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$4-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 147 #molecular-weight 16070 #checksum 1713 SEQUENCE /// ENTRY HBRB4 #type complete TITLE hemoglobin epsilon chain - rabbit ALTERNATE_NAMES hemoglobin beta-4 chain ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 15-Nov-1984 #sequence_revision 06-Jun-1997 #text_change 03-Mar-2000 ACCESSIONS A02424; S03088 REFERENCE A02424 !$#authors Hardison, R.C. !$#journal J. Biol. Chem. (1983) 258:8739-8744 !$#title The nucleotide sequence of the rabbit embryonic globin gene !1beta4. !$#cross-references MUID:83238509; PMID:6305998 !$#accession A02424 !'##molecule_type DNA !'##residues 1-147 ##label HAR GENETICS !$#introns 31/2; 105/3 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; embryo; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$4-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 147 #molecular-weight 16290 #checksum 2708 SEQUENCE /// ENTRY HEMSY2 #type complete TITLE hemoglobin epsilon-y2 chain - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 18-Aug-1982 #sequence_revision 06-Feb-1998 #text_change 03-Mar-2000 ACCESSIONS A92342; S10117; C43560; A90291; A02425 REFERENCE A92342 !$#authors Hansen, J.N.; Konkel, D.A.; Leder, P. !$#journal J. Biol. Chem. (1982) 257:1048-1052 !$#title The sequence of a mouse embryonic beta-globin gene. !1Evolution of the gene and its signal region. !$#cross-references MUID:82098088; PMID:6274852 !$#accession A92342 !'##molecule_type DNA !'##residues 2-147 ##label HAN !'##cross-references GB:V00726; NID:g50176; PIDN:CAA24104.1; PID:g50177; !1GB:J00419; NID:g193797; PID:g387189 !'##experimental_source strain BALB/c !'##note translation of initiator Met is not shown REFERENCE S10115 !$#authors Jahn, C.L.; Hutchison III, C.A.; Phillips, S.J.; Weaver, S.; !1Haigwood, N.L.; Voliva, C.F.; Edgell, M.H. !$#journal Cell (1980) 21:159-168 !$#title DNA sequence organization of the beta-globin complex in the !1BALB/c mouse. !$#cross-references MUID:81001851; PMID:6250710 !$#accession S10117 !'##molecule_type DNA !'##residues 32-105 ##label JAH !'##cross-references EMBL:V00742; NID:g50807; PIDN:CAA24117.1; !1PID:g763135 REFERENCE A43560 !$#authors Wilkinson, D.G.; Bailes, J.A.; Champion, J.E.; McMahon, A.P. !$#journal Development (1987) 99:493-500 !$#title A molecular analysis of mouse development from 8 to 10 days !1post coitum detects changes only in embryonic globin !1expression. !$#cross-references MUID:88029090; PMID:2444404 !$#accession C43560 !'##molecule_type mRNA !'##residues 1-39,'H',41-147 ##label WIL !'##cross-references GB:M26897; NID:g193532; PIDN:AAA37701.1; !1PID:g309258 REFERENCE A90291 !$#authors Gilman, J.G. !$#journal Biochem. J. (1976) 155:231-241 !$#title Mouse haemoglobin beta chains. Sequence data on embryonic y !1chain and genetic linkage of the y-chain locus to the adult !1beta-chain locus Hbb. !$#cross-references MUID:76231500; PMID:938477 !$#accession A90291 !'##molecule_type protein !'##residues 2-40 ##label GIL GENETICS !$#introns 31/2; 105/3 FUNCTION !$#description in erythrocytes binds and transports molecular oxygen from !1placenta to tissues !$#note a beta-type chain found in early embryos CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; embryo; erythrocyte; heme; !1heterotetramer; iron; metalloprotein; oxygen carrier FEATURE !$2-147 #product hemoglobin epsilon-y2 chain #status !8predicted #label MAT\ !$4-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 147 #molecular-weight 16137 #checksum 3655 SEQUENCE /// ENTRY HEBO2 #type complete TITLE hemoglobin epsilon-2 chain - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 03-Mar-2000 ACCESSIONS A25754 REFERENCE A93058 !$#authors Schimenti, J.C.; Duncan, C.H. !$#journal Mol. Biol. Evol. (1985) 2:505-513 !$#title Concerted evolution of the cow epsilon(2) and epsilon(4) !1beta-globin genes. !$#cross-references MUID:88216137; PMID:3870873 !$#accession A25754 !'##molecule_type DNA !'##residues 1-146 ##label SCH !'##cross-references GB:X03248; GB:M13996; NID:g318; PIDN:CAA27007.1; !1PID:g319 COMMENT The bovine hemoglobin epsilon-2 chain is exceptional in !1appearing to have tyrosine rather than histidine as the !1distal axial ligand binding oxygen. GENETICS !$#gene HBE2 !$#introns 30/2; 104/3 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; embryo; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (Tyr) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16404 #checksum 368 SEQUENCE /// ENTRY HEBO4 #type complete TITLE hemoglobin epsilon-4 chain - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 03-Mar-2000 ACCESSIONS B25754 REFERENCE A93058 !$#authors Schimenti, J.C.; Duncan, C.H. !$#journal Mol. Biol. Evol. (1985) 2:505-513 !$#title Concerted evolution of the cow epsilon(2) and epsilon(4) !1beta-globin genes. !$#cross-references MUID:88216137; PMID:3870873 !$#accession B25754 !'##molecule_type DNA !'##residues 1-146 ##label SCH !'##cross-references GB:X03249; GB:M13997; NID:g320; PIDN:CAA27008.1; !1PID:g321 GENETICS !$#gene HBE4 !$#introns 30/2; 104/3 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; embryo; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16383 #checksum 342 SEQUENCE /// ENTRY HEGT2 #type complete TITLE hemoglobin epsilon-II chain - goat ORGANISM #formal_name Capra aegagrus hircus #common_name domestic goat DATE 20-Sep-1984 #sequence_revision 20-Sep-1984 #text_change 03-Mar-2000 ACCESSIONS A02426 REFERENCE A92905 !$#authors Shapiro, S.G.; Schon, E.A.; Townes, T.M.; Lingrel, J.B. !$#journal J. Mol. Biol. (1983) 169:31-52 !$#title Sequence and linkage of the goat epsilon(I) and epsilon(II) !1beta-globin genes. !$#cross-references MUID:84010860; PMID:6312053 !$#accession A02426 !'##molecule_type DNA !'##residues 1-147 ##label SHA !'##cross-references GB:K01714; NID:g164145; PIDN:AAA30918.1; !1PID:g164146 !'##note the authors translated the codon GCA for residue 30 as Gly COMMENT Epsilon chains are found in embryonic hemoglobins. GENETICS !$#gene epsilon-II !$#introns 31/2; 105/3 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; embryo; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$4-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 147 #molecular-weight 16405 #checksum 1921 SEQUENCE /// ENTRY HBKG2G #type complete TITLE hemoglobin beta chain - eastern gray kangaroo ORGANISM #formal_name Macropus giganteus #common_name eastern gray kangaroo DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 03-Mar-2000 ACCESSIONS A02427 REFERENCE A90085 !$#authors Air, G.M.; Thompson, E.O.P. !$#journal Aust. J. Biol. Sci. (1969) 22:1437-1454 !$#title Studies on marsupial proteins. II. Amino acid sequence of !1the beta-chain of haemoglobin from the grey kangaroo, !1Macropus giganteus. !$#accession A02427 !'##molecule_type protein !'##residues 1-146 ##label AIR !'##note an allele of the sequence shown has 2-Gln CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16015 #checksum 6780 SEQUENCE /// ENTRY HBKGR #type complete TITLE hemoglobin beta chain - red kangaroo (tentative sequence) ORGANISM #formal_name Macropus rufus, Megaleia rufa #common_name red kangaroo DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Mar-2000 ACCESSIONS A90086 REFERENCE A90086 !$#authors Thompson, E.O.P.; Air, G.M. !$#journal Aust. J. Biol. Sci. (1971) 24:1199-1217 !$#title Studies on marsupial proteins. VI. Evolutionary changes in !1beta-globins of the Macropodidae and the amino acid sequence !1of beta-globin from Potorous tridactylus. !$#cross-references MUID:74096089; PMID:5005884 !$#accession A90086 !'##molecule_type protein !'##residues 1-146 ##label THO CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16001 #checksum 7116 SEQUENCE /// ENTRY HBPT #type complete TITLE hemoglobin beta chain - potoroo (tentative sequence) ORGANISM #formal_name Potorous tridactylus #common_name potoroo, long-nosed rat kangaroo DATE 24-Apr-1984 #sequence_revision 30-Sep-1988 #text_change 31-Mar-2000 ACCESSIONS A02428 REFERENCE A90086 !$#authors Thompson, E.O.P.; Air, G.M. !$#journal Aust. J. Biol. Sci. (1971) 24:1199-1217 !$#title Studies on marsupial proteins. VI. Evolutionary changes in !1beta-globins of the Macropodidae and the amino acid sequence !1of beta-globin from Potorous tridactylus. !$#cross-references MUID:74096089; PMID:5005884 !$#accession A02428 !'##molecule_type protein !'##residues 1-146 ##label THO CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15933 #checksum 8086 SEQUENCE /// ENTRY HBOP #type complete TITLE hemoglobin beta chain - North American opossum ORGANISM #formal_name Didelphis virginiana, Didelphis marsupialis virginiana #common_name North American opossum DATE 31-May-1979 #sequence_revision 09-Apr-1999 #text_change 03-Mar-2000 ACCESSIONS B30213; A02429 REFERENCE A30213 !$#authors Koop, B.F.; Goodman, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:3893-3897 !$#title Evolutionary and developmental aspects of two hemoglobin !1beta-chain genes (epsilon(M) and beta(M)) of opossum. !$#cross-references MUID:88234526; PMID:3375246 !$#accession B30213 !'##molecule_type DNA !'##residues 1-147 ##label KOO !'##cross-references GB:J03643; NID:g164284; PIDN:AAA30976.1; !1PID:g164285 REFERENCE A02429 !$#authors Stenzel, P.; Brimhall, B.; Jones, R.T.; Black, J.A.; !1McLachlan, A.; Gibson, D. !$#journal J. Biol. Chem. (1979) 254:2071-2076 !$#title Opossum hemoglobin. The amino acid sequences of the alpha !1and beta chains. !$#cross-references MUID:79130456; PMID:422568 !$#accession A02429 !'##molecule_type protein !'##residues 2-80,'D',82-108,'B',110-127,'Z',129-131,'Z',133-147 ##label !1STE GENETICS !$#introns 31/2; 105/3 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$4-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 147 #molecular-weight 16211 #checksum 3557 SEQUENCE /// ENTRY HBTG #type complete TITLE hemoglobin beta chain - Australian echidna ORGANISM #formal_name Tachyglossus aculeatus #common_name Australian echidna DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 03-Mar-2000 ACCESSIONS A90087; A90088; A02430 REFERENCE A90087 !$#authors Whittaker, R.G.; Fisher, W.K.; Thompson, E.O.P. !$#journal Aust. J. Biol. Sci. (1972) 25:989-1004 !$#title Studies on monotreme proteins. I. Amino acid sequence of the !1beta-chain of haemoglobin from the echidna, Tachyglossus !1aculeatus aculeatus. !$#cross-references MUID:73201997; PMID:4663350 !$#contents T. a. aculeatus !$#accession A90087 !'##molecule_type protein !'##residues 1-146 ##label WHI REFERENCE A90088 !$#authors Thompson, E.O.P.; Fisher, W.K.; Whittaker, R.G. !$#journal Aust. J. Biol. Sci. (1973) 26:1327-1335 !$#title Studies on monotreme protein. III. Amino acid sequence of !1the alpha- and beta-globin chains of the minor haemoglobin !1from the echidna, Tachyglossus aculeatus aculeatus. !$#cross-references MUID:74097602; PMID:4798231 !$#contents T. a. aculeatus, variant chain !$#accession A90088 !'##molecule_type protein !'##residues 1-146 ##label THO !'##note in a single animal, two types of beta chains were obtained from !1hemoglobin I having the alpha-1 B chain variant; the !1sequence of the second type of beta chain differs from that !1shown in having 5-Glu and 138-Ala and is most likely an !1allelic chain CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15974 #checksum 1912 SEQUENCE /// ENTRY HBOR #type complete TITLE hemoglobin beta chain - duckbill platypus (tentative sequence) ORGANISM #formal_name Ornithorhynchus anatinus #common_name duckbill platypus DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 31-Mar-2000 ACCESSIONS A02431 REFERENCE A02431 !$#authors Whittaker, R.G.; Thompson, E.O.P. !$#journal Aust. J. Biol. Sci. (1975) 28:353-365 !$#title Studies of monotreme proteins. VI. Amino acid sequence of !1the beta-chain of haemoglobin from the platypus, !1Ornithorhynchus anatinus. !$#cross-references MUID:76061123; PMID:1191127 !$#accession A02431 !'##molecule_type protein !'##residues 1-146 ##label WHI CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15872 #checksum 41 SEQUENCE /// ENTRY HBTJ1 #type complete TITLE hemoglobin beta-I chain - tuatara (tentative sequence) ORGANISM #formal_name Sphenodon punctatus #common_name tuatara DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 31-Mar-2000 ACCESSIONS S01138 REFERENCE S01136 !$#authors Abbasi, A.; Wells, R.M.G.; Brittain, T.; Braunitzer, G. !$#journal Biol. Chem. Hoppe-Seyler (1988) 369:755-764 !$#title Primary structure of the hemoglobins from sphenodon !1(Sphenodon punctatus, tuatara, Rynchocephalia). Evidence for !1the expression of alpha(D)-gene. !$#cross-references MUID:89105321; PMID:3214555 !$#accession S01138 !'##molecule_type protein !'##residues 1-146 ##label ABB CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16191 #checksum 8945 SEQUENCE /// ENTRY HBTJ2 #type complete TITLE hemoglobin beta-II chain - tuatara ORGANISM #formal_name Sphenodon punctatus #common_name tuatara DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS S01139 REFERENCE S01136 !$#authors Abbasi, A.; Wells, R.M.G.; Brittain, T.; Braunitzer, G. !$#journal Biol. Chem. Hoppe-Seyler (1988) 369:755-764 !$#title Primary structure of the hemoglobins from sphenodon !1(Sphenodon punctatus, tuatara, Rynchocephalia). Evidence for !1the expression of alpha(D)-gene. !$#cross-references MUID:89105321; PMID:3214555 !$#accession S01139 !'##molecule_type protein !'##residues 1-146 ##label ABB CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16342 #checksum 1024 SEQUENCE /// ENTRY HBCH #type complete TITLE hemoglobin beta chain - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Apr-1981 #sequence_revision 13-Mar-1997 #text_change 21-Jul-2000 ACCESSIONS I50249; A92420; A93692; A91939; I50246; A02432 REFERENCE A49359 !$#authors Reitman, M.; Grasso, J.A.; Blumenthal, R.; Lewit, P. !$#journal Genomics (1993) 18:616-626 !$#title Primary sequence, evolution, and repetitive elements of the !1Gallus gallus (chicken) beta-globin cluster. !$#cross-references MUID:94140361; PMID:8307571 !$#accession I50249 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-147 ##label REI !'##cross-references GB:L17432; NID:g3927807; PIDN:AAD03347.1; !1PID:g408498 REFERENCE A92420 !$#authors Dolan, M.; Dodgson, J.B.; Engel, J.D. !$#journal J. Biol. Chem. (1983) 258:3983-3990 !$#title Analysis of the adult chicken beta-globin gene: nucleotide !1sequence of the locus, microheterogeneity at the 5'-end of !1beta-globin mRNA, and aberrant nuclear RNA species. !$#cross-references MUID:83160946; PMID:6833240 !$#accession A92420 !'##molecule_type DNA !'##residues 2-147 ##label DOL !'##cross-references GB:V00409; GB:J00858; NID:g63412; PIDN:CAA23700.1; !1PID:g63413 !'##note initiator Met not shown REFERENCE A93692 !$#authors Richards, R.I.; Shine, J.; Ullrich, A.; Wells, J.R.E.; !1Goodman, H.M. !$#journal Nucleic Acids Res. (1979) 7:1137-1146 !$#title Molecular cloning and sequence analysis of adult chicken !1beta globin cDNA. !$#cross-references MUID:80079280; PMID:514809 !$#accession A93692 !'##molecule_type mRNA !'##residues 2-147 ##label RIC !'##cross-references GB:J00860; NID:g211881; PIDN:AAA48805.1; !1PID:g211882 REFERENCE A91939 !$#authors Maita, T.; Mizuno, K.; Matsuda, G. !$#journal J. Biochem. (1975) 78:1311-1319 !$#title Peptic peptides from the beta polypeptide chain of AII !1component of chicken hemoglobin. !$#cross-references MUID:76190041; PMID:773926 !$#accession A91939 !'##molecule_type protein !'##residues 2-147 ##label MAI !'##note this is the final paper in a series REFERENCE I50246 !$#authors Padayatty, J.; Cummings, I.; Manske, C.L.; Higuchi, R.; Woo, !1S.; Salser, W. !$#journal Gene (1981) 13:417-422 !$#title Cloning of chicken globin cDNA in bacterial plasmids. !$#cross-references MUID:81261952; PMID:6266925 !$#accession I50246 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 30-44 ##label PAD !'##cross-references GB:M10380; NID:g211874; PIDN:AAA48803.1; !1PID:g211875 GENETICS !$#introns 31/2; 105/3 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$4-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 147 #molecular-weight 16466 #checksum 2545 SEQUENCE /// ENTRY HBQJF #type complete TITLE hemoglobin beta chain - gray francolin ORGANISM #formal_name Francolinus pondicerianus #common_name gray francolin DATE 03-Feb-1994 #sequence_revision 03-Feb-1994 #text_change 03-Mar-2000 ACCESSIONS JU0339 REFERENCE JU0336 !$#authors Abbasi, A.; Zaidi, Z.H. !$#submission submitted to JIPID, March 1991 !$#accession JU0339 !'##molecule_type protein !'##residues 1-146 ##label ABB CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16321 #checksum 195 SEQUENCE /// ENTRY HBFER #type complete TITLE hemoglobin beta chain - ring-necked pheasant ORGANISM #formal_name Phasianus colchicus #common_name ring-necked pheasant DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 03-Mar-2000 ACCESSIONS A02433 REFERENCE A91704 !$#authors Braunitzer, G.; Godovac, J. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1982) 363:229-238 !$#title The amino acid sequence of pheasant (Phasianus colchicus !1colchicus) hemoglobins. !$#cross-references MUID:82188254; PMID:7076123 !$#accession A02433 !'##molecule_type protein !'##residues 1-146 ##label BRA CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16307 #checksum 180 SEQUENCE /// ENTRY HBGSA #type complete TITLE hemoglobin beta chain - Andean goose ORGANISM #formal_name Chloephaga melanoptera #common_name Andean goose DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS S00569 REFERENCE S00523 !$#authors Hiebl, I.; Braunitzer, G.; Schneeganss, D. !$#journal Biol. Chem. Hoppe-Seyler (1987) 368:1559-1569 !$#title High-altitude respiration of geese. The primary structures !1of the major and minor hemoglobin-components of adult Andean !1goose (Chloephaga melanoptera, Anatidae): the mutation !1Leu-Ser in position 55 of the beta-chains. !$#cross-references MUID:88163076; PMID:3442599 !$#accession S00569 !'##molecule_type protein !'##residues 1-146 ##label HIE CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16295 #checksum 563 SEQUENCE /// ENTRY HBDK #type complete TITLE hemoglobin beta chain - duck ORGANISM #formal_name Anas platyrhynchos #common_name domestic duck DATE 20-Sep-1984 #sequence_revision 20-Sep-1984 #text_change 03-Mar-2000 ACCESSIONS A02434 REFERENCE A02434 !$#authors Hampe, A.; Therwath, A.; Soriano, P.; Galibert, F. !$#journal Gene (1981) 14:11-21 !$#title Nucleotide sequence analysis of a cloned duck beta-globin !1cDNA. !$#cross-references MUID:81261956; PMID:6894908 !$#accession A02434 !'##molecule_type mRNA !'##residues 1-146 ##label HAM !'##note the authors translated the codon CAG for residues 87, 127, and !1131 as Glu CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16319 #checksum 9667 SEQUENCE /// ENTRY HBDKM #type complete TITLE hemoglobin beta chain - muscovy duck ORGANISM #formal_name Cairina moschata #common_name muscovy duck DATE 28-Feb-1986 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS S07635 REFERENCE S07635 !$#authors Mathieu-Kolling, C.; Niessing, J. !$#journal Nucleic Acids Res. (1989) 17:9472 !$#title Nucleotide sequence and deduced amino acid sequence of the !1duck beta-globin gene. !$#cross-references MUID:90067945; PMID:2587266 !$#accession S07635 !'##molecule_type DNA !'##residues 1-147 ##label MAT !'##cross-references EMBL:X15739; NID:g62719; PIDN:CAA33756.1; !1PID:g62720 GENETICS !$#introns 31/2; 105/3 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$4-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 147 #molecular-weight 16436 #checksum 1976 SEQUENCE /// ENTRY HBDL #type complete TITLE hemoglobin beta chain - blue-and-yellow macaw ORGANISM #formal_name Ara ararauna #common_name blue-and-yellow macaw DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 03-Mar-2000 ACCESSIONS A02436 REFERENCE A90687 !$#authors Godovac-Zimmermann, J.; Braunitzer, G. !$#journal Biol. Chem. Hoppe-Seyler (1985) 366:503-508 !$#title The primary structure of alpha(A)- and beta-chains from !1blue-and-yellow macaw (Ara arauna, Psittaci) hemoglobin. !$#cross-references MUID:85225971; PMID:4005049 !$#accession A02436 !'##molecule_type protein !'##residues 1-146 ##label GOD CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16216 #checksum 9442 SEQUENCE /// ENTRY HBGS #type complete TITLE hemoglobin beta chain - western graylag goose ORGANISM #formal_name Anser anser anser #common_name western graylag goose DATE 31-Jan-1980 #sequence_revision 02-Apr-1982 #text_change 03-Mar-2000 ACCESSIONS A02437 REFERENCE A91694 !$#authors Oberthur, W.; Braunitzer, G.; Kalas, S. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1981) 362:1101-1112 !$#title Untersuchungen am Haemoglobin der Graugans (Anser anser). !1Die Primaerstruktur der alpha- und beta-Ketten der !1Hauptkomponente. !$#cross-references MUID:82263308; PMID:7346378 !$#accession A02437 !'##molecule_type protein !'##residues 1-146 ##label OBE CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16305 #checksum 349 SEQUENCE /// ENTRY HBGSI #type complete TITLE hemoglobin beta chain - bar-headed goose ORGANISM #formal_name Anser indicus #common_name bar-headed goose DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 03-Mar-2000 ACCESSIONS A02438 REFERENCE A91705 !$#authors Oberthur, W.; Braunitzer, G.; Wurdinger, I. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1982) 363:581-590 !$#title Das Haemoglobin der Streifengans (Anser indicus). !1Primaerstruktur und Physiologie der Atmung, Systematik und !1Evolution. !$#cross-references MUID:82263336; PMID:7106705 !$#accession A02438 !'##molecule_type protein !'##residues 1-146 ##label OBE CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16291 #checksum 338 SEQUENCE /// ENTRY HBGSC #type complete TITLE hemoglobin beta chain - Canada goose ORGANISM #formal_name Branta canadensis #common_name Canada goose DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 03-Mar-2000 ACCESSIONS A02439 REFERENCE A91709 !$#authors Oberthur, W.; Godovac-Zimmermann, J.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1982) 363:777-787 !$#title The amino acid sequence of Canada goose (Branta canadensis) !1and mute swan (Cygnus olor) hemoglobins. !$#cross-references MUID:83005405; PMID:7118073 !$#accession A02439 !'##molecule_type protein !'##residues 1-146 ##label OBE CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16291 #checksum 335 SEQUENCE /// ENTRY HBWS #type complete TITLE hemoglobin beta chain - mute swan ORGANISM #formal_name Cygnus olor #common_name mute swan DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Mar-2000 ACCESSIONS A91709 REFERENCE A91709 !$#authors Oberthur, W.; Godovac-Zimmermann, J.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1982) 363:777-787 !$#title The amino acid sequence of Canada goose (Branta canadensis) !1and mute swan (Cygnus olor) hemoglobins. !$#cross-references MUID:83005405; PMID:7118073 !$#accession A91709 !'##molecule_type protein !'##residues 1-146 ##label OBE CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16291 #checksum 335 SEQUENCE /// ENTRY HBGD #type complete TITLE hemoglobin beta chain - American flamingo ORGANISM #formal_name Phoenicopterus ruber #common_name American flamingo DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 03-Mar-2000 ACCESSIONS A02441 REFERENCE A91733 !$#authors Godovac-Zimmermann, J.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1984) 365:437-443 !$#title The amino-acid sequence of alpha(A)- and beta-chains from !1the major hemoglobin component of American flamingo !1(Phoenicopterus ruber ruber). !$#cross-references MUID:84238000; PMID:6735355 !$#accession A02441 !'##molecule_type protein !'##residues 1-146 ##label GOD CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16319 #checksum 9740 SEQUENCE /// ENTRY HBGSS #type complete TITLE hemoglobin beta chain - magpie goose ORGANISM #formal_name Anseranas semipalmata #common_name magpie goose DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 03-Mar-2000 ACCESSIONS A02440 REFERENCE A91720 !$#authors Oberthur, W.; Wiesner, H.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1983) 364:51-59 !$#title Die Primaerstruktur der alpha- und beta-Ketten der !1Hauptkomponente der Haemoglobine der Spaltfussgans !1(Anseranas semipalmata, Anatidae). !$#cross-references MUID:83184073; PMID:6840695 !$#accession A02440 !'##molecule_type protein !'##residues 1-146 ##label OBE !'##note tryptic peptides and the prolyl peptide (residues 100-146) were !1sequenced and were positioned by homology with the graylag !1goose sequence CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16308 #checksum 9804 SEQUENCE /// ENTRY HBOS #type complete TITLE hemoglobin beta chain - ostrich ORGANISM #formal_name Struthio camelus #common_name ostrich DATE 20-Sep-1984 #sequence_revision 20-Sep-1984 #text_change 03-Mar-2000 ACCESSIONS A02443 REFERENCE A91693 !$#authors Oberthur, W.; Voelter, W.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1980) 361:969-975 !$#title Die Sequenz der Haemoglobine von Streifengans (Anser !1indicus) und Strauss (Struthio camelus). Inositpentaphosphat !1als Modulator Der Evolutionsgeschwindigkeit: die !1ueberraschende Sequenz alpha-63 (E12) Valin. !$#cross-references MUID:80247760; PMID:7399417 !$#accession A02443 !'##molecule_type protein !'##residues 1-146 ##label OBE CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16296 #checksum 9676 SEQUENCE /// ENTRY HBEH #type complete TITLE hemoglobin beta chain - greater rhea ORGANISM #formal_name Rhea americana #common_name greater rhea, common rhea DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 03-Mar-2000 ACCESSIONS A02444 REFERENCE A91712 !$#authors Oberthur, W.; Braunitzer, G.; Baumann, R.; Wright, P.G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1983) 364:119-134 !$#title Die Primaerstruktur der alpha- und beta-Ketten der !1Hauptkomponenten der Haemoglobine des Straubes (Struthio !1camelus) und des Nandus (Rhea americana) (Struthioformes). !$#cross-references MUID:83184081; PMID:6840701 !$#accession A02444 !'##molecule_type protein !'##residues 1-146 ##label OBE CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16280 #checksum 9590 SEQUENCE /// ENTRY HBQC #type complete TITLE hemoglobin beta chain - golden eagle ORGANISM #formal_name Aquila chrysaetos #common_name golden eagle DATE 20-Sep-1984 #sequence_revision 20-Sep-1984 #text_change 03-Mar-2000 ACCESSIONS A02442 REFERENCE A91724 !$#authors Oberthur, W.; Braunitzer, G.; Grimm, F.; Kosters, J. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1983) 364:851-858 !$#title Haemoglobine des steinadlers (Aquila chrysaetos, !1Accipitriformes): die Aminosaeure-Sequenz der alpha(A)- und !1beta-Ketten der Hauptkomponente. !$#cross-references MUID:84006435; PMID:6618445 !$#accession A02442 !'##molecule_type protein !'##residues 1-146 ##label OBE !'##note tryptic peptides and the prolyl peptide (residues 100-146) were !1sequenced and ordered by homology CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16277 #checksum 9036 SEQUENCE /// ENTRY HBGRW #type complete TITLE hemoglobin beta chain - white-headed vulture ORGANISM #formal_name Trigonoceps occipitalis #common_name white-headed vulture DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS S04950 REFERENCE S04948 !$#authors Hiebl, I.; Weber, R.E.; Schneeganss, D.; Braunitzer, G. !$#journal Biol. Chem. Hoppe-Seyler (1989) 370:699-706 !$#title High-altitude respiration of Falconiformes. The primary !1structures and functional properties of the major and minor !1hemoglobin components of the adult white-headed vulture !1(Trigonoceps occipitalis, Aegypiinae). !$#cross-references MUID:89374815; PMID:2775491 !$#accession S04950 !'##molecule_type protein !'##residues 1-146 ##label HIE CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16233 #checksum 8971 SEQUENCE /// ENTRY HBGRR #type complete TITLE hemoglobin beta chain - Rueppell's griffon ORGANISM #formal_name Gyps rueppellii #common_name Rueppell's griffon DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 03-Mar-2000 ACCESSIONS S00539 REFERENCE S00527 !$#authors Hiebl, I.; Weber, R.E.; Schneeganss, D.; Koesters, J.; !1Braunitzer, G. !$#journal Biol. Chem. Hoppe-Seyler (1988) 369:217-232 !$#title High-altitude respiration of birds. Structural adaptations !1in the major and minor hemoglobin components of adult !1Rueppell's griffon (Gyps rueppellii, Aegypiinae): a new !1molecular pattern for hypoxic tolerance. !$#cross-references MUID:88293711; PMID:3401327 !$#accession S00539 !'##molecule_type protein !'##residues 1-146 ##label HIE CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16233 #checksum 8971 SEQUENCE /// ENTRY HBGLB #type complete TITLE hemoglobin beta chain - black-headed gull ORGANISM #formal_name Larus ridibundus #common_name black-headed gull DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 03-Mar-2000 ACCESSIONS S00815 REFERENCE S00814 !$#authors Godovac-Zimmermann, J.; Koesters, J.; Braunitzer, G.; !1Goeltenboth, R. !$#journal Biol. Chem. Hoppe-Seyler (1988) 369:341-348 !$#title Structural adaptation of bird hemoglobins to high-altitude !1respiration and the primary sequences of black-headed gull !1(Larus ridibundus, Charadriiformes) alpha(A)- and beta/ !1beta'-chains. !$#cross-references MUID:89000193; PMID:3166738 !$#accession S00815 !'##molecule_type protein !'##residues 1-146 ##label GOD !'##note 78-Ile was also found CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16260 #checksum 9875 SEQUENCE /// ENTRY HBPNR #type complete TITLE hemoglobin beta chain - rock-hopper penguin ORGANISM #formal_name Eudyptes crestatus #common_name rock-hopper penguin DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 03-Mar-2000 ACCESSIONS S00823 REFERENCE S00822 !$#authors Huber, K.; Braunitzer, G.; Schneeganss, D.; Koesters, J.; !1Grimm, F. !$#journal Biol. Chem. Hoppe-Seyler (1988) 369:513-519 !$#title The primary structure of the hemoglobin of the rock-hopper !1penguin (Eudyptes crestatus, Sphenisciformes). !$#cross-references MUID:89076486; PMID:3202958 !$#accession S00823 !'##molecule_type protein !'##residues 1-146 ##label HUB CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16295 #checksum 543 SEQUENCE /// ENTRY HBCOG #type complete TITLE hemoglobin beta chain - great cormorant ORGANISM #formal_name Phalacrocorax carbo #common_name great cormorant DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS S01805 REFERENCE S01804 !$#authors Huber, K.; Braunitzer, G.; Schneeganss, D.; Koesters, J.; !1Grimm, F. !$#journal Biol. Chem. Hoppe-Seyler (1988) 369:1251-1258 !$#title The primary structure of the hemoglobin of the cormorant !1(Phalacrocorax carbo, Pelecaniformes). !$#cross-references MUID:89228540; PMID:3245897 !$#accession S01805 !'##molecule_type protein !'##residues 1-146 ##label HUB CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16109 #checksum 8254 SEQUENCE /// ENTRY HBSI #type complete TITLE hemoglobin beta chain - swift ORGANISM #formal_name Apus apus #common_name swift DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS S07480 REFERENCE S07479 !$#authors Nothum, R.; Weber, R.E.; Koesters, J.; Schneeganss, D.; !1Braunitzer, G. !$#journal Biol. Chem. Hoppe-Seyler (1989) 370:1197-1207 !$#title Amino-acid sequences and functional differentiation of !1hemoglobins A and D from swift (Apus apus, Apodiformes). !$#cross-references MUID:90121756; PMID:2610936 !$#accession S07480 !'##molecule_type protein !'##residues 1-146 ##label NOT CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16156 #checksum 9179 SEQUENCE /// ENTRY HBPY #type complete TITLE hemoglobin beta chain - pigeon ORGANISM #formal_name Columba livia #common_name domestic pigeon DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 03-Mar-2000 ACCESSIONS A61432; A94542; JQ0340; JT0204 REFERENCE A61432 !$#authors Sultana, C.; Abbasi, A.; Zaidi, Z.H. !$#journal J. Protein Chem. (1991) 10:145-149 !$#title Primary structure of hemoglobin beta-chain from Columba !1livia (gray wild pigeon). !$#cross-references MUID:92029509; PMID:1930630 !$#accession A61432 !'##molecule_type protein !'##residues 1-146 ##label SUL CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterodimer; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16152 #checksum 9872 SEQUENCE /// ENTRY HBKOW #type complete TITLE hemoglobin beta chain - white stork ORGANISM #formal_name Ciconia ciconia #common_name white stork DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 03-Mar-2000 ACCESSIONS A02445 REFERENCE A91728 !$#authors Godovac-Zimmermann, J.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1984) 365:1107-1113 !$#title Hemoglobin of the adult white stork (Ciconia ciconia, !1Ciconiiformes). The primary structure of alpha (A)- and !1beta-chains from the only present hemoglobin component. !$#cross-references MUID:85053022; PMID:6500517 !$#accession A02445 !'##molecule_type protein !'##residues 1-146 ##label GOD CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16206 #checksum 7997 SEQUENCE /// ENTRY HBJS #type complete TITLE hemoglobin beta chain - common starling ORGANISM #formal_name Sturnus vulgaris #common_name common starling DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 03-Mar-2000 ACCESSIONS A02446 REFERENCE A91731 !$#authors Oberthur, W.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1984) 365:159-173 !$#title Hemoglobins of starling (Sturnus vulgaris, Passeriformes). !1The primary structures of alpha(A)-, alpha (D)- and !1beta-chains. !$#cross-references MUID:84184202; PMID:6714943 !$#accession A02446 !'##molecule_type protein !'##residues 1-146 ##label OBE CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16182 #checksum 2379 SEQUENCE /// ENTRY HBHTB #type complete TITLE hemoglobin beta chain - blackbird ORGANISM #formal_name Turdus merula #common_name blackbird DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS S04001 REFERENCE S04000 !$#authors Nothum, R.; Braunitzer, G.; Hiebl, I.; Koesters, J.; !1Schneeganss, D. !$#journal Biol. Chem. Hoppe-Seyler (1989) 370:309-316 !$#title The hemoglobins of the adult blackbird (Turdus merula, !1Passeriformes). The sequence of the major (HbA) and minor !1component (HbD). !$#cross-references MUID:89335259; PMID:2757791 !$#accession S04001 !'##molecule_type protein !'##residues 1-146 ##label NOT CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16109 #checksum 1841 SEQUENCE /// ENTRY HFCHR #type complete TITLE hemoglobin rho chain - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 29-Jul-1981 #sequence_revision 13-Mar-1997 #text_change 21-Jul-2000 ACCESSIONS I50247; A92399; A93884; A92323; A02447 REFERENCE A49359 !$#authors Reitman, M.; Grasso, J.A.; Blumenthal, R.; Lewit, P. !$#journal Genomics (1993) 18:616-626 !$#title Primary sequence, evolution, and repetitive elements of the !1Gallus gallus (chicken) beta-globin cluster. !$#cross-references MUID:94140361; PMID:8307571 !$#accession I50247 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-147 ##label REI !'##cross-references GB:L17432; NID:g3927807; PIDN:AAD03345.1; !1PID:g408499 REFERENCE A92399 !$#authors Dodgson, J.B.; Stadt, S.J.; Choi, O.R.; Dolan, M.; Fischer, !1H.D.; Engel, J.D. !$#journal J. Biol. Chem. (1983) 258:12685-12692 !$#title The nucleotide sequence of the embryonic chicken beta-type !1globin genes. !$#cross-references MUID:84032465; PMID:6313671 !$#accession A92399 !'##molecule_type DNA !'##residues 2-147 ##label DOD !'##cross-references GB:K00823; NID:g211885; PIDN:AAA48806.1; !1PID:g211888 REFERENCE A93884 !$#authors Roninson, I.B.; Ingram, V.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:4782-4785 !$#title cDNA sequence of a new chicken embryonic rho-globin. !$#cross-references MUID:82060137; PMID:6170981 !$#accession A93884 !'##molecule_type mRNA !'##residues 2-147 ##label RON !'##cross-references GB:J00862; NID:g211893; PIDN:AAA48809.1; !1PID:g211894 !'##note initiator Met not shown REFERENCE A92323 !$#authors Chapman, B.S.; Tobin, A.J.; Hood, L.E. !$#journal J. Biol. Chem. (1981) 256:5524-5531 !$#title Complete amino acid sequence of the major early embryonic !1beta-like globin in chickens. !$#cross-references MUID:81215454; PMID:7240154 !$#accession A92323 !'##molecule_type protein !'##residues 2-125,'E',127-129,'A',131-139,'K',141-143,'R',145-147 !1##label CHA COMMENT The rho chain is the beta-type chain of the major early !1embryonic hemoglobin P. GENETICS !$#map_position beta-globin gene cluster !$#introns 31/2; 105/3 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; embryo; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$4-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 147 #molecular-weight 16589 #checksum 4024 SEQUENCE /// ENTRY HECH #type complete TITLE hemoglobin epsilon chain - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 05-Apr-1983 #sequence_revision 13-Mar-1997 #text_change 21-Jul-2000 ACCESSIONS I50250; B92399; A92377; A92376; A02448 REFERENCE A49359 !$#authors Reitman, M.; Grasso, J.A.; Blumenthal, R.; Lewit, P. !$#journal Genomics (1993) 18:616-626 !$#title Primary sequence, evolution, and repetitive elements of the !1Gallus gallus (chicken) beta-globin cluster. !$#cross-references MUID:94140361; PMID:8307571 !$#accession I50250 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-147 ##label REI !'##cross-references GB:L17432; NID:g3927807; PIDN:AAD03348.1; !1PID:g408497 REFERENCE A92399 !$#authors Dodgson, J.B.; Stadt, S.J.; Choi, O.R.; Dolan, M.; Fischer, !1H.D.; Engel, J.D. !$#journal J. Biol. Chem. (1983) 258:12685-12692 !$#title The nucleotide sequence of the embryonic chicken beta-type !1globin genes. !$#cross-references MUID:84032465; PMID:6313671 !$#accession B92399 !'##molecule_type DNA !'##residues 2-147 ##label DOD !'##cross-references GB:K00824; NID:g211886; PIDN:AAA48807.1; !1PID:g211889 !'##note initiator Met not shown REFERENCE A92377 !$#authors Chapman, B.S.; Hood, L.E.; Tobin, A.J. !$#journal J. Biol. Chem. (1982) 257:651-658 !$#title Minor early embryonic chick hemoglobin M. Amino acid !1sequences of the epsilon and alpha(D) chains. !$#cross-references MUID:82098109; PMID:7054172 !$#accession A92377 !'##molecule_type protein !'##residues 2-59,'K',61-147 ##label CH1 !'##note this chain was isolated from HbM, the least abundant of the !1four early chick hemoglobins, which also contains alpha-D !1chains REFERENCE A92376 !$#authors Chapman, B.S.; Hood, L.E.; Tobin, A.J. !$#journal J. Biol. Chem. (1982) 257:643-650 !$#title Amino acid sequences of the epsilon and alpha E globins of !1HbE, a minor early embryonic hemoglobin of the chicken. !$#cross-references MUID:82098108; PMID:7054171 !$#accession A92376 !'##molecule_type protein !'##residues 2-59,'K',61-147 ##label CH2 !'##note this chain was isolated from HbE, one of the two minor !1hemoglobins in early chick embryos, which also contains !1alpha-A chains GENETICS !$#introns 31/2; 105/3 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; embryo; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$4-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 147 #molecular-weight 16603 #checksum 2984 SEQUENCE /// ENTRY HEDKM #type complete TITLE hemoglobin epsilon chain - muscovy duck ORGANISM #formal_name Cairina moschata #common_name muscovy duck DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS S14685; S08117 REFERENCE S14685 !$#authors Mathieu-Kolling, C.; Niessing, J. !$#journal Nucleic Acids Res. (1990) 18:3657 !$#title Nucleotide sequence of the gene encoding the duck embryonic !1epsilon-globin. !$#cross-references MUID:90301502; PMID:2362822 !$#accession S14685 !'##molecule_type DNA !'##residues 1-147 ##label MAT !'##cross-references EMBL:X15740; NID:g62721; PIDN:CAA33757.1; !1PID:g62722 GENETICS !$#introns 31/2; 105/3 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$4-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 147 #molecular-weight 16688 #checksum 4422 SEQUENCE /// ENTRY HBTTP #type complete TITLE hemoglobin beta chain - western painted turtle ORGANISM #formal_name Chrysemys picta bellii #common_name western painted turtle DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 03-Mar-2000 ACCESSIONS S00538 REFERENCE S00525 !$#authors Ruecknagel, K.P.; Braunitzer, G. !$#journal Biol. Chem. Hoppe-Seyler (1988) 369:123-131 !$#title Hemoglobins of reptiles. The primary structure of the major !1and minor hemoglobin component of adult Western painted !1turtle (Chrysemys picta bellii). !$#cross-references MUID:88209274; PMID:3365328 !$#accession S00538 !'##molecule_type protein !'##residues 1-146 ##label RUE CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16304 #checksum 9804 SEQUENCE /// ENTRY HBNJ2I #type complete TITLE hemoglobin beta-II chain - Indian cobra ORGANISM #formal_name Naja naja naja #common_name Indian cobra DATE 03-Feb-1994 #sequence_revision 03-Feb-1994 #text_change 03-Mar-2000 ACCESSIONS JU0337 REFERENCE JU0337 !$#authors Naqvi, S.; Abbasi, A.; Zaidi, Z.H. !$#submission submitted to JIPID, March 1991 !$#accession JU0337 !'##molecule_type protein !'##residues 1-146 ##label NAQ CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16290 #checksum 311 SEQUENCE /// ENTRY HBIG1 #type complete TITLE hemoglobin beta-I chain - common iguana ORGANISM #formal_name Iguana iguana #common_name common iguana DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS S01665 REFERENCE S01664 !$#authors Ruecknagel, K.P.; Braunitzer, G.; Wiesner, H. !$#journal Biol. Chem. Hoppe-Seyler (1988) 369:1143-1150 !$#title Hemoglobins of reptiles. The primary structures of the alpha !1(I)- and beta(I)-chains of common iguana (Iguana iguana) !1hemoglobin. !$#cross-references MUID:89207099; PMID:3242545 !$#accession S01665 !'##molecule_type protein !'##residues 1-146 ##label RUE CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16111 #checksum 8926 SEQUENCE /// ENTRY HBLZC #type complete TITLE hemoglobin beta-I chain - Cape monitor ORGANISM #formal_name Varanus exanthematicus albigularis #common_name Cape monitor DATE 31-Dec-1990 #sequence_revision 13-Feb-1998 #text_change 03-Mar-2000 ACCESSIONS S16367; S06094 REFERENCE S16196 !$#authors Abbasi, A.; Braunitzer, G. !$#journal Biol. Chem. Hoppe-Seyler (1991) 372:473-479 !$#title Primary structure of hemoglobin from monitor lizard (Varanus !1exanthematicus albigularis-Squamata). !$#cross-references MUID:92029675; PMID:1930730 !$#accession S16367 !'##molecule_type protein !'##residues 1-146 ##label ABB1 REFERENCE S06093 !$#authors Abbasi, A.; Braunitzer, G. !$#book Protein structure-function relationship, Zaidi, Z.H., ed., !1pp.1-13, Elsevier, Amsterdam, 1988 !$#title Hemoglobin - structure, physiology and evolution. !$#accession S06094 !'##molecule_type protein !'##residues 1-12,'T',14-26,'A',28-43,'T',45-49,'N',51-100,'E',102-103, !1'R',105-117,'L',119-146 ##label ABB2 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16193 #checksum 2531 SEQUENCE /// ENTRY HBAK #type complete TITLE hemoglobin beta chain - Nile crocodile ORGANISM #formal_name Crocodylus niloticus #common_name Nile crocodile DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 11-May-2000 ACCESSIONS A91695; A02449 REFERENCE A91695 !$#authors Leclercq, F.; Schnek, A.G.; Braunitzer, G.; Stangl, A.; !1Schrank, B. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1981) 362:1151-1158 !$#title Direct reciprocal allosteric interaction of oxygen and !1hydrogen carbonate sequence of the haemoglobins of the !1caiman (Caiman crocodylus), the Nile crocodile (Crocodylus !1niloticus) and the Mississippi crocodile (Alligator !1mississippiensis). !$#cross-references MUID:82263313; PMID:6286445 !$#accession A91695 !'##molecule_type protein !'##residues 1-146 ##label LEC REFERENCE A94406 !$#authors Schafer, W.; Braunitzer, G.; Stangl, A. !$#journal Z. Naturforsch. C (1981) 36:902-903 !$#title Direct allosteric interaction of oxygen and bicarbonate: !1N-acetyl-alanyl-seryl-phenylalanine, N-terminal sequence of !1the beta-chains of the haemoglobins of Nile crocodile !1(Crocodylus niloticus) and Mississippi crocodile (Alligator !1mississippiensis). !$#cross-references MUID:82064118; PMID:7303821 !$#contents annotation CLASSIFICATION #superfamily globin; globin homology KEYWORDS acetylated amino end; blood; chromoprotein; erythrocyte; !1heme; iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16437 #checksum 6184 SEQUENCE /// ENTRY HBAQ #type complete TITLE hemoglobin beta chain - American alligator ORGANISM #formal_name Alligator mississippiensis #common_name American alligator DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 11-May-2000 ACCESSIONS B91695; A02450 REFERENCE A91695 !$#authors Leclercq, F.; Schnek, A.G.; Braunitzer, G.; Stangl, A.; !1Schrank, B. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1981) 362:1151-1158 !$#title Direct reciprocal allosteric interaction of oxygen and !1hydrogen carbonate sequence of the haemoglobins of the !1caiman (Caiman crocodylus), the Nile crocodile (Crocodylus !1niloticus) and the Mississippi crocodile (Alligator !1mississippiensis). !$#cross-references MUID:82263313; PMID:6286445 !$#accession B91695 !'##molecule_type protein !'##residues 1-146 ##label LEC REFERENCE A94406 !$#authors Schafer, W.; Braunitzer, G.; Stangl, A. !$#journal Z. Naturforsch. C (1981) 36:902-903 !$#title Direct allosteric interaction of oxygen and bicarbonate: !1N-acetyl-alanyl-seryl-phenylalanine, N-terminal sequence of !1the beta-chains of the haemoglobins of Nile crocodile !1(Crocodylus niloticus) and Mississippi crocodile (Alligator !1mississippiensis). !$#cross-references MUID:82064118; PMID:7303821 !$#contents annotation CLASSIFICATION #superfamily globin; globin homology KEYWORDS acetylated amino end; blood; chromoprotein; erythrocyte; !1heme; iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16610 #checksum 5144 SEQUENCE /// ENTRY HBCQ #type complete TITLE hemoglobin beta chain - spectacled caiman ORGANISM #formal_name Caiman crocodilus, Caiman sclerops #common_name spectacled caiman DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 03-Mar-2000 ACCESSIONS A02451 REFERENCE A91695 !$#authors Leclercq, F.; Schnek, A.G.; Braunitzer, G.; Stangl, A.; !1Schrank, B. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1981) 362:1151-1158 !$#title Direct reciprocal allosteric interaction of oxygen and !1hydrogen carbonate sequence of the haemoglobins of the !1caiman (Caiman crocodylus), the Nile crocodile (Crocodylus !1niloticus) and the Mississippi crocodile (Alligator !1mississippiensis). !$#cross-references MUID:82263313; PMID:6286445 !$#accession A02451 !'##molecule_type protein !'##residues 1-146 ##label LEC CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16718 #checksum 7935 SEQUENCE /// ENTRY HBFGRE #type complete TITLE hemoglobin beta chain - edible frog ORGANISM #formal_name Rana esculenta #common_name edible frog DATE 29-Jul-1981 #sequence_revision 29-Jul-1981 #text_change 03-Mar-2000 ACCESSIONS A02454 REFERENCE A02454 !$#authors Chauvet, J.P.; Acher, R. !$#journal Biochemistry (1972) 11:916-927 !$#title Phylogeny of hemoglobins. Beta chain of frog (Rana !1esculenta) hemoglobin. !$#cross-references MUID:72111329; PMID:4536743 !$#accession A02454 !'##molecule_type protein !'##residues 1-140 ##label CHA CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$1-140 #domain globin homology #label GLB\ !$57 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$86 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 140 #molecular-weight 15423 #checksum 4818 SEQUENCE /// ENTRY HBFGC #type complete TITLE hemoglobin beta chain - bullfrog ORGANISM #formal_name Rana catesbeiana #common_name bullfrog DATE 24-Apr-1984 #sequence_revision 04-Dec-1986 #text_change 03-Mar-2000 ACCESSIONS A02455 REFERENCE A02455 !$#authors Tam, L.T.; Gray, G.P.; Riggs, A.F. !$#journal J. Biol. Chem. (1986) 261:8290-8294 !$#title The hemoglobins of the bullfrog Rana catesbeiana. The !1structure of the beta chain of component C and the role of !1the alpha chain in the formation of intermolecular disulfide !1bonds. !$#cross-references MUID:86250724; PMID:3487542 !$#accession A02455 !'##molecule_type protein !'##residues 1-140 ##label TAM !'##note this beta chain is from hemoglobin C COMMENT The beta chains of hemoglobins B and C appear to be !1identical. COMMENT Hemoglobin C tetramers polymerize by the formation of !1disulfide bonds. The deoxy tetramers of hemoglobin B and C !1associate to form molecules believed to be trimers (B+2C) of !1very low oxygen affinity. CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$1-140 #domain globin homology #label GLB\ !$57 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$86 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 140 #molecular-weight 15424 #checksum 7056 SEQUENCE /// ENTRY HBXL #type complete TITLE hemoglobin beta chain, major - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 30-Nov-1980 #sequence_revision 30-Nov-1980 #text_change 03-Mar-2000 ACCESSIONS A92432; A93709; B90964; A02452 REFERENCE A92432 !$#authors Patient, R.K.; Harris, R.; Walmsley, M.E.; Williams, J.G. !$#journal J. Biol. Chem. (1983) 258:8521-8523 !$#title The complete nucleotide sequence of the major adult beta !1globin gene of Xenopus laevis. !$#cross-references MUID:83238474; PMID:6305990 !$#accession A92432 !'##molecule_type DNA !'##residues 1-145 ##label PAT !'##cross-references GB:J00978; NID:g214209; PIDN:AAA49734.1; !1PID:g214210 !'##note initiator Met not shown REFERENCE A93709 !$#authors Williams, J.G.; Kay, R.M.; Patient, R.K. !$#journal Nucleic Acids Res. (1980) 8:4247-4258 !$#title The nucleotide sequence of the major beta-globin mRNA from !1Xenopus laevis. !$#cross-references MUID:81053765; PMID:7433108 !$#accession A93709 !'##molecule_type mRNA !'##residues 1-145 ##label WIL REFERENCE A90964 !$#authors Richardson, C.; Cappello, J.; Cochran, M.D.; Armentrout, !1R.W.; Brown, R.D. !$#journal Dev. Biol. (1980) 78:161-172 !$#title Partial sequence analysis of Xenopus alpha- and beta-globin !1mRNA as determined from recombinant DNA plasmids. !$#cross-references MUID:80247171; PMID:6249685 !$#accession B90964 !'##molecule_type mRNA !'##residues 38-99,'A',101-102,'G',104-145 ##label RIC !'##cross-references GB:M15382; NID:g213937; PIDN:AAA49641.1; !1PID:g213938 GENETICS !$#gene beta-1 !$#introns 29/2; 99/3 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-145 #domain globin homology #label GLB\ !$62 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$91 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 145 #molecular-weight 16290 #checksum 6488 SEQUENCE /// ENTRY HBXL2 #type fragment TITLE hemoglobin beta chain, minor - African clawed frog (fragment) ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 03-Mar-2000 ACCESSIONS A02453 REFERENCE A93457 !$#authors Knochel, W.; Meyerhof, W.; Hummel, S.; Grundmann, U. !$#journal Nucleic Acids Res. (1983) 11:1543-1553 !$#title Molecular cloning and sequencing of mRNAs coding for minor !1adult globin polypeptides of Xenopus laevis. !$#cross-references MUID:83143365; PMID:6298748 !$#accession A02453 !'##molecule_type mRNA !'##residues 1-124 ##label KNO !'##cross-references GB:X01560; NID:g64579; PIDN:CAA25713.1; PID:g64580 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$1-124 #domain globin homology (fragment) #label GLB\ !$41 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$70 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 124 #checksum 398 SEQUENCE /// ENTRY HBFG3T #type complete TITLE hemoglobin beta chain, tadpole - bullfrog ORGANISM #formal_name Rana catesbeiana #common_name bullfrog DATE 31-Jul-1980 #sequence_revision 31-Jul-1980 #text_change 03-Mar-2000 ACCESSIONS A02456 REFERENCE A02456 !$#authors Watt, K.W.K.; Maruyama, T.; Riggs, A. !$#journal J. Biol. Chem. (1980) 255:3294-3301 !$#title Hemoglobins of the tadpole of the bullfrog, Rana !1catesbeiana. Amino acid sequence of the beta chain of a !1major component. !$#cross-references MUID:80159938; PMID:6965940 !$#accession A02456 !'##molecule_type protein !'##residues 1-146 ##label WAT COMMENT This beta chain is a component of hemoglobin III. CLASSIFICATION #superfamily globin; globin homology KEYWORDS acetylated amino end; blood; chromoprotein; erythrocyte; !1heme; iron; metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$1 #modified_site acetylated amino end (Val) #status !8absent\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 16346 #checksum 1433 SEQUENCE /// ENTRY HBXLT1 #type complete TITLE hemoglobin beta-T1 chain, tadpole - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 20-Sep-1984 #sequence_revision 20-Sep-1984 #text_change 03-Mar-2000 ACCESSIONS A02457 REFERENCE A02457 !$#authors Banville, D.; Kay, R.M.; Harris, R.; Williams, J.G. !$#journal J. Biol. Chem. (1983) 258:7924-7927 !$#title The nucleotide sequence of the mRNA encoding a tadpole !1beta-globin polypeptide of Xenopus laevis. !$#cross-references MUID:83238385; PMID:6688076 !$#accession A02457 !'##molecule_type mRNA !'##residues 1-146 ##label BAN CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15902 #checksum 2166 SEQUENCE /// ENTRY HBXLLW #type complete TITLE hemoglobin beta chain, larval - western clawed frog ORGANISM #formal_name Xenopus tropicalis #common_name western clawed frog DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 03-Mar-2000 ACCESSIONS S06308 REFERENCE S06308 !$#authors Knoechel, W.; Beck, J.; Meyerhof, W. !$#journal Nucleic Acids Res. (1987) 15:10062 !$#title Nucleotide sequence of the Xenopus tropicalis larval beta !1globin gene. !$#cross-references MUID:88096508; PMID:3697074 !$#accession S06308 !'##molecule_type DNA !'##residues 1-147 ##label KNO !'##cross-references EMBL:Y00501; NID:g65299; PIDN:CAA68554.1; !1PID:g65300 !'##note the authors translated the codon GTC for residues 55, 59, and !168 as Ala, GAT for residues 80 and 81 as Asn, CGC for !1residue 106 as Asn, and CAA for residue 128 as Glu GENETICS !$#introns 31/2; 105/3 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$2-147 #product hemoglobin beta chain, larval #status !8predicted #label MAT\ !$4-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 147 #molecular-weight 16000 #checksum 7036 SEQUENCE /// ENTRY HBLUA #type complete TITLE hemoglobin beta chain - South American lungfish ORGANISM #formal_name Lepidosiren paradoxus #common_name South American lungfish DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 03-Mar-2000 ACCESSIONS A02458 REFERENCE A91735 !$#authors Rodewald, K.; Stangl, A.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1984) 365:639-649 !$#title Primary structure, biochemical and physiological aspects of !1hemoglobin from South American lungfish (Lepidosiren !1paradoxus, Dipnoi). !$#cross-references MUID:85005237; PMID:6090299 !$#accession A02458 !'##molecule_type protein !'##residues 1-147 ##label ROD CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-147 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 147 #molecular-weight 16817 #checksum 3681 SEQUENCE /// ENTRY HBCAA #type complete TITLE hemoglobin beta chains - common carp ORGANISM #formal_name Cyprinus carpio #common_name common carp DATE 30-Sep-1979 #sequence_revision 29-Jul-1981 #text_change 03-Mar-2000 ACCESSIONS A02459 REFERENCE A02459 !$#authors Grujic-Injac, B.; Braunitzer, G.; Stangl, A. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1980) 361:1629-1639 !$#title Hemoglobins, XXXV: the sequence of the beta-A and !1beta-b-chains of the hemoglobins of the carp (Cyprinus !1carpio L.). !$#cross-references MUID:81092283; PMID:7450680 !$#accession A02459 !'##molecule_type protein !'##residues 1-147 ##label GRU !'##note the sequence of the beta-B chain differs from that shown in !1having 13-Gly, 41-Tyr, 122-Ala, and 143-Cys COMMENT The beta-A sequence is shown. CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-147 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 147 #molecular-weight 16262 #checksum 3078 SEQUENCE /// ENTRY HBGY #type complete TITLE hemoglobin beta chain - goldfish ORGANISM #formal_name Carassius auratus #common_name goldfish DATE 02-Apr-1982 #sequence_revision 02-Apr-1982 #text_change 03-Mar-2000 ACCESSIONS A02460 REFERENCE A91739 !$#authors Rodewald, K.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1984) 365:95-104 !$#title The primary structure of the hemoglobin from goldfish !1(Carassius auratus). !$#cross-references MUID:84184196; PMID:6714939 !$#accession A02460 !'##molecule_type protein !'##residues 1-147 ##label ROD CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-147 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 147 #molecular-weight 16210 #checksum 3167 SEQUENCE /// ENTRY HBTR4 #type complete TITLE hemoglobin IV beta chain - rainbow trout (tentative sequence) ORGANISM #formal_name Oncorhynchus mykiss #common_name rainbow trout DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 19-May-2000 ACCESSIONS A02461; A61416 REFERENCE A02461 !$#authors Petruzzelli, R.; Barra, D.; Goffredo, B.M.; Bossa, F.; !1Coletta, M.; Brunori, M. !$#journal Biochim. Biophys. Acta (1984) 789:69-73 !$#title Amino-acid sequence of beta-chain of hemoglobin IV from !1trout (Salmo irideus). !$#accession A02461 !'##molecule_type protein !'##residues 1-147 ##label PET REFERENCE A61416 !$#authors Bossa, F.; Barra, D.; Coletta, M.; Martini, F.; Liverzani, !1A.; Petruzzelli, R.; Bonaventura, J.; Brunori, M. !$#journal FEBS Lett. (1976) 64:76-80 !$#title Primary structure of hemoglobins from trout (Salmo irideus). !1Partial determination of amino acid sequence of HB trout IV. !$#cross-references MUID:76188064; PMID:1269767 !$#accession A61416 !'##molecule_type protein !'##residues 1-42;46-76,'D',78,'BB',81-85 ##label BOS CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-147 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 147 #molecular-weight 15982 #checksum 4781 SEQUENCE /// ENTRY HBTR1 #type complete TITLE hemoglobin I beta chain - rainbow trout (tentative sequence) ORGANISM #formal_name Oncorhynchus mykiss #common_name rainbow trout DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 19-May-2000 ACCESSIONS A02462 REFERENCE A02462 !$#authors Barra, D.; Petruzzelli, R.; Bossa, F.; Brunori, M. !$#journal Biochim. Biophys. Acta (1983) 742:72-77 !$#title Primary structure of hemoglobin from trout (Salmo irideus) !1amino acid sequence of the beta chain of trout Hb I. !$#cross-references MUID:83127399; PMID:6824687 !$#accession A02462 !'##molecule_type protein !'##residues 1-146 ##label BAR !'##note this hemoglobin differs from other fish hemoglobins in lacking !1a residue between 121 and 122 CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15881 #checksum 3938 SEQUENCE /// ENTRY HBRKJ #type complete TITLE hemoglobin beta chain - Port Jackson shark ORGANISM #formal_name Heterodontus portusjacksoni #common_name Port Jackson shark DATE 31-Jul-1979 #sequence_revision 31-Jul-1979 #text_change 03-Mar-2000 ACCESSIONS A02463 REFERENCE A02463 !$#authors Fisher, W.K.; Nash, A.R.; Thompson, E.O.P. !$#journal Aust. J. Biol. Sci. (1977) 30:487-506 !$#title Haemoglobins of the shark, Heterodontus portusjacksoni. III. !1Amino acid sequence of the beta-chain. !$#cross-references MUID:78186393; PMID:614004 !$#accession A02463 !'##molecule_type protein !'##residues 1-141 ##label FIS CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$3-141 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 141 #molecular-weight 16011 #checksum 9641 SEQUENCE /// ENTRY HBRYM #type complete TITLE hemoglobin beta chain - marbled electric ray ORGANISM #formal_name Torpedo marmorata #common_name marbled electric ray DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 03-Mar-2000 ACCESSIONS S05421; S05420 REFERENCE S05418 !$#authors Huber, F.; Braunitzer, G. !$#journal Biol. Chem. Hoppe-Seyler (1989) 370:831-838 !$#title The primary structure of electric ray hemoglobin (Torpedo !1marmorata). Bohr effect and phosphate interaction. !$#cross-references MUID:90074179; PMID:2590465 !$#accession S05421 !'##molecule_type protein !'##residues 1-142 ##label HUB !'##note 8-Ile, 9-Arg, 55-Gln, 65-Asn, 67-Ile, 76-Asp, 77-Ile, and !1113-Leu were also found CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; heterotetramer; !1iron; metalloprotein; oxygen carrier FEATURE !$3-142 #domain globin homology #label GLB\ !$59 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$88 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 142 #molecular-weight 16089 #checksum 1864 SEQUENCE /// ENTRY MYHU #type complete TITLE myoglobin [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 24-Apr-1984 #sequence_revision 12-Jul-1996 #text_change 08-Dec-2000 ACCESSIONS I53991; A90999; A93398; A90582; A90584; A02464 REFERENCE I53991 !$#authors Akaboshi, E. !$#journal Gene (1985) 33:241-249 !$#title Cloning of the human myoglobin gene. !$#cross-references MUID:85232026; PMID:2989088 !$#accession I53991 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-128,'E',130-154 ##label RES !'##cross-references GB:M14603; NID:g187582; PIDN:AAA59595.1; !1PID:g386872 REFERENCE A90999 !$#authors Weller, P.; Jeffreys, A.J.; Wilson, V.; Blanchetot, A. !$#journal EMBO J. (1984) 3:439-446 !$#title Organization of the human myoglobin gene. !$#cross-references MUID:84182508; PMID:6571704 !$#accession A90999 !'##molecule_type DNA !'##residues 2-154 ##label WEL !'##cross-references GB:X00371; NID:g34607; PIDN:CAA25109.1; !1PID:g1235527 !'##note initiator Met not shown REFERENCE A93398 !$#authors Romero-Herrera, A.E.; Lehmann, H. !$#journal Nature New Biol. (1971) 232:149-152 !$#title Primary structure of human myoglobin. !$#cross-references MUID:71291923; PMID:5285572 !$#accession A93398 !'##molecule_type protein !'##residues 2-19,'IDPA',24-83,'Q',85-99,'VPI',103-154 ##label ROM !'##note this sequence has been revised in references A90582 and A90584 REFERENCE A90582 !$#authors Romero-Herrera, A.E.; Lehmann, H. !$#journal Biochim. Biophys. Acta (1971) 251:482-488 !$#title The myoglobin of primates. I. Hylobates agilis (gibbon). !$#accession A90582 !'##molecule_type protein !'##residues 20-23;84 ##label RO2 !'##note revision to human sequence REFERENCE A90584 !$#authors Romero-Herrera, A.E.; Lehmann, H. !$#journal Biochim. Biophys. Acta (1972) 278:62-67 !$#title The myoglobin of primates. II. Pan troglodytes (chimpanzee). !$#cross-references MUID:73002055; PMID:4627044 !$#accession A90584 !'##molecule_type protein !'##residues 100-102 ##label RO3 !'##note revision to human sequence REFERENCE A30619 !$#authors Hubbard, S.R.; Hendrickson, W.A.; Lambright, D.G.; Boxer, !1S.G. !$#journal J. Mol. Biol. (1990) 213:215-218 !$#title X-ray crystal structure of a recombinant human myoglobin !1mutant at 2.8 angstroms resolution. !$#cross-references MUID:90258028; PMID:2342104 !$#contents annotation; X-ray crystallography, 2.8 angstroms of !1engineered mutant with 46-Arg and 111-Ala expressed in !1Escherichia coli GENETICS !$#gene GDB:MB !'##cross-references GDB:119378; OMIM:160000 !$#map_position 22q12-22q12 !$#introns 32/2; 106/3 FUNCTION !$#description binds molecular oxygen for intracellular storage and !1transport, primarily in muscle CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; monomer; muscle; !1oxygen carrier FEATURE !$2-154 #product myoglobin #status experimental #label MAT\ !$3-148 #domain globin homology #label GLB\ !$65 #binding_site oxygen (His) (distal axial ligand) !8#status experimental\ !$94 #binding_site heme iron (His) (proximal axial ligand) !8#status experimental SUMMARY #length 154 #molecular-weight 17184 #checksum 7061 SEQUENCE /// ENTRY MYCZ #type complete TITLE myoglobin - chimpanzee (tentative sequence) ORGANISM #formal_name Pan troglodytes #common_name chimpanzee DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 03-Mar-2000 ACCESSIONS A02465 REFERENCE A90584 !$#authors Romero-Herrera, A.E.; Lehmann, H. !$#journal Biochim. Biophys. Acta (1972) 278:62-67 !$#title The myoglobin of primates. II. Pan troglodytes (chimpanzee). !$#cross-references MUID:73002055; PMID:4627044 !$#accession A02465 !'##molecule_type protein !'##residues 1-153 ##label ROM !'##note the tryptic, peptic, and thermolytic peptides were aligned by !1homology with the human sequence COMMENT This myoglobin was isolated from skeletal muscle. CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 17062 #checksum 4170 SEQUENCE /// ENTRY MYGI #type complete TITLE myoglobin - agile gibbon (tentative sequence) ORGANISM #formal_name Hylobates agilis #common_name agile gibbon DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 03-Mar-2000 ACCESSIONS A02466 REFERENCE A90582 !$#authors Romero-Herrera, A.E.; Lehmann, H. !$#journal Biochim. Biophys. Acta (1971) 251:482-488 !$#title The myoglobin of primates. I. Hylobates agilis (gibbon). !$#accession A02466 !'##molecule_type protein !'##residues 1-153 ##label ROM !'##note compositions of tryptic and chymotryptic peptides and the !1sequence of residues 19-23 were determined; the peptides !1were aligned by homology with the human sequence COMMENT This myoglobin was isolated from skeletal muscle. CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 17083 #checksum 4464 SEQUENCE /// ENTRY MYGO #type complete TITLE myoglobin - mountain gorilla (tentative sequence) ORGANISM #formal_name Gorilla gorilla beringei #common_name mountain gorilla, highland gorilla DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 03-Mar-2000 ACCESSIONS A02467 REFERENCE A02467 !$#authors Romero-Herrera, A.E.; Lehmann, H.; Fossey, D. !$#journal Biochim. Biophys. Acta (1975) 393:383-388 !$#title The myoglobin of primates. VIII. Gorilla gorilla beringei !1(Eastern highland gorilla). !$#cross-references MUID:75205685; PMID:1148222 !$#contents compositions of tryptic and thermolytic peptides and !1sequence of residues 21-22 !$#accession A02467 !'##molecule_type protein !'##residues 1-153 ##label ROM !'##note the peptides were positioned by homology with the human !1sequence COMMENT This myoglobin was isolated from skeletal muscle. CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 17042 #checksum 4254 SEQUENCE /// ENTRY MYOG #type complete TITLE myoglobin - Bornean orangutan (tentative sequence) ORGANISM #formal_name Pongo pygmaeus pygmaeus #common_name Bornean orangutan DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 03-Mar-2000 ACCESSIONS A02468 REFERENCE A02468 !$#authors Romero-Herrera, A.E.; Lehmann, H.; Castillo, O.; Joysey, !1K.A.; Friday, A.E. !$#journal Nature (1976) 261:162-164 !$#title Myoglobin of the orangutan as a phylogenetic enigma. !$#cross-references MUID:76196270; PMID:1272388 !$#contents compositions of tryptic and peptic peptides and sequences of !1residues 17-23 and 110 !$#accession A02468 !'##molecule_type protein !'##residues 1-153 ##label ROM !'##note the peptides were aligned by homology with the human sequence CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 17066 #checksum 5312 SEQUENCE /// ENTRY MYBAO #type complete TITLE myoglobin - olive baboon (tentative sequence) ORGANISM #formal_name Papio anubis, Papio hamadryas anubis #common_name olive baboon DATE 24-Apr-1984 #sequence_revision 27-Nov-1985 #text_change 03-Mar-2000 ACCESSIONS A90583; A02469 REFERENCE A90583 !$#authors Romero-Herrera, A.E.; Lehmann, H. !$#journal Biochim. Biophys. Acta (1972) 278:465-481 !$#title The myoglobin of primates. III. Cercopithecidae (Old World !1monkeys): Papio anubis (olive baboon) and Macaca !1fascicularis (=irus, crab-eating monkey. !$#cross-references MUID:73040318; PMID:4628632 !$#contents compositions of tryptic, peptic, and chymotryptic peptides !1and sequences of residues 25, 110-102, 140, and 143-145 !$#accession A90583 !'##molecule_type protein !'##residues 1-153 ##label ROM !'##note the peptides were aligned by homology with the human sequence COMMENT This myoglobin was isolated from skeletal muscle. CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 17016 #checksum 5051 SEQUENCE /// ENTRY MYMQRG #type complete TITLE myoglobin - red guenon (tentative sequence) ORGANISM #formal_name Erythrocebus patas #common_name red guenon, hussar DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 03-Mar-2000 ACCESSIONS A90633; A02469 REFERENCE A90633 !$#authors Dene, H.; Sazy, J.; Romero-Herrera, A.E. !$#journal Biochim. Biophys. Acta (1980) 625:133-145 !$#title The myoglobin of primates. X. !$#cross-references MUID:81021734; PMID:7417495 !$#contents compositions of tryptic and peptic peptides and sequences of !1residues 17-23, 103-105, 110, and 140-142 !$#accession A90633 !'##molecule_type protein !'##residues 1-153 ##label DEN !'##note the peptides were aligned by homology with the human sequence COMMENT This myoglobin was isolated from skeletal muscle. CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 17016 #checksum 5051 SEQUENCE /// ENTRY MYMQHL #type complete TITLE myoglobin - hanuman langur (tentative sequence) ORGANISM #formal_name Presbytis entellus #common_name hanuman langur DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 03-Mar-2000 ACCESSIONS B90633; A02469 REFERENCE A90633 !$#authors Dene, H.; Sazy, J.; Romero-Herrera, A.E. !$#journal Biochim. Biophys. Acta (1980) 625:133-145 !$#title The myoglobin of primates. X. !$#cross-references MUID:81021734; PMID:7417495 !$#contents compositions of tryptic and peptic peptides and sequences of !1residues 17-23, 103-105, 110, and 140-142 !$#accession B90633 !'##molecule_type protein !'##residues 1-153 ##label DEN !'##note the peptides were aligned by homology with the human sequence COMMENT This myoglobin was isolated from skeletal muscle. CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 17016 #checksum 5051 SEQUENCE /// ENTRY MYMQIM #type complete TITLE myoglobin - crab-eating macaque (tentative sequence) ORGANISM #formal_name Macaca fascicularis #common_name crab-eating macaque DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 03-Mar-2000 ACCESSIONS A02470 REFERENCE A90583 !$#authors Romero-Herrera, A.E.; Lehmann, H. !$#journal Biochim. Biophys. Acta (1972) 278:465-481 !$#title The myoglobin of primates. III. Cercopithecidae (Old World !1monkeys): Papio anubis (olive baboon) and Macaca !1fascicularis (=irus, crab-eating monkey. !$#cross-references MUID:73040318; PMID:4628632 !$#accession A02470 !'##molecule_type protein !'##residues 1-153 ##label ROM !'##note compositions of tryptic and peptic peptides and sequences of !1residues 25, 64-66, 110-112, and 140-144 were determined; !1the peptides were aligned by homology with the human !1sequence COMMENT This myoglobin was isolated from skeletal muscle. CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 17045 #checksum 5240 SEQUENCE /// ENTRY MYMQN #type complete TITLE myoglobin - douroucouli ORGANISM #formal_name Aotus trivirgatus #common_name douroucouli, night monkey, owl monkey DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 03-Mar-2000 ACCESSIONS A02471 REFERENCE A02471 !$#authors Heinbokel, N.; Lehmann, H. !$#journal FEBS Lett. (1984) 165:46-50 !$#title The myoglobin of primates: the night monkey, Aotes !1trivirgatus (Cebidae, Platyrrhini, Anthropoidea). !$#cross-references MUID:84108869; PMID:6692912 !$#accession A02471 !'##molecule_type protein !'##residues 1-153 ##label HEI COMMENT This myoglobin was isolated from skeletal muscle. CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 17030 #checksum 4467 SEQUENCE /// ENTRY MYCJ #type complete TITLE myoglobin - common marmoset (tentative sequence) ORGANISM #formal_name Callithrix jacchus #common_name common marmoset DATE 24-Apr-1984 #sequence_revision 27-Nov-1985 #text_change 03-Mar-2000 ACCESSIONS A90587; A91390; A02472 REFERENCE A90587 !$#authors Romero-Herrera, A.E.; Lehmann, H. !$#journal Biochim. Biophys. Acta (1973) 317:65-84 !$#title The myoglobin of primates. IV. New World monkeys: Cebidae: !1(1) Saimiri sciureus (squirrel monkey); (2) Lagothrix !1lagothricha (Humboldt's woolly monkey. Callitrichidae: !1Callithrix jacchus (common marmoset). !$#cross-references MUID:73231297; PMID:4198766 !$#contents compositions of tryptic and peptic peptides and sequences of !1residues 19-23, 30-31, 57-58, 107-109, 111-112, 118, and 140 !$#accession A90587 !'##molecule_type protein !'##residues 1-153 ##label ROM !'##note the peptides were positioned by homology with the human !1sequence !'##note 62-Arg was also found REFERENCE A91390 !$#authors Romero-Herrera, A.E.; Lehmann, H. !$#journal FEBS Lett. (1973) 31:175-180 !$#title N-terminal chain elongation as evidence for duplication of !1myoglobin in three South American monkeys. !$#contents minor component !$#accession A91390 !'##molecule_type protein !'##residues 'FK',1-153 ##label RO2 COMMENT This myoglobin was isolated from skeletal muscle. CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 17044 #checksum 4194 SEQUENCE /// ENTRY MYMQC #type complete TITLE myoglobin - brown capuchin (tentative sequence) ORGANISM #formal_name Cebus apella #common_name brown capuchin, black-capped capuchin DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 03-Mar-2000 ACCESSIONS A02473 REFERENCE A90633 !$#authors Dene, H.; Sazy, J.; Romero-Herrera, A.E. !$#journal Biochim. Biophys. Acta (1980) 625:133-145 !$#title The myoglobin of primates. X. !$#cross-references MUID:81021734; PMID:7417495 !$#accession A02473 !'##molecule_type protein !'##residues 1-153 ##label DEN !'##note compositions of tryptic and peptic peptides and sequences of !1residues 12-23, 30-31, 57-60, 80-86, 107-108, 110-113, and !1140-142 were determined; the peptides were aligned by !1homology with the human sequence COMMENT This myoglobin was isolated from skeletal muscle. CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 17007 #checksum 4221 SEQUENCE /// ENTRY MYMQW #type complete TITLE myoglobin - common woolly monkey (tentative sequence) ORGANISM #formal_name Lagothrix lagothricha #common_name common woolly monkey DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 03-Mar-2000 ACCESSIONS B90587; B91390; A02474 REFERENCE A90587 !$#authors Romero-Herrera, A.E.; Lehmann, H. !$#journal Biochim. Biophys. Acta (1973) 317:65-84 !$#title The myoglobin of primates. IV. New World monkeys: Cebidae: !1(1) Saimiri sciureus (squirrel monkey); (2) Lagothrix !1lagothricha (Humboldt's woolly monkey. Callitrichidae: !1Callithrix jacchus (common marmoset). !$#cross-references MUID:73231297; PMID:4198766 !$#contents compositions of tryptic and peptic peptides and sequences of !1residues 12-13, 25, 30-31, 57-60, 64-66, 79-81, 86, 107-113, !1118, 133, and 140 !$#accession B90587 !'##molecule_type protein !'##residues 1-153 ##label ROM !'##note the peptides were positioned by homology with the human !1sequence REFERENCE A91390 !$#authors Romero-Herrera, A.E.; Lehmann, H. !$#journal FEBS Lett. (1973) 31:175-180 !$#title N-terminal chain elongation as evidence for duplication of !1myoglobin in three South American monkeys. !$#contents minor component !$#accession B91390 !'##molecule_type protein !'##residues 'FK',1-153 ##label RO2 COMMENT This myoglobin was isolated from skeletal muscle. CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 17035 #checksum 2329 SEQUENCE /// ENTRY MYMQS #type complete TITLE myoglobin - common squirrel monkey (tentative sequence) ORGANISM #formal_name Saimiri sciureus #common_name common squirrel monkey DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 03-Mar-2000 ACCESSIONS C90587; C91390; A02475 REFERENCE A90587 !$#authors Romero-Herrera, A.E.; Lehmann, H. !$#journal Biochim. Biophys. Acta (1973) 317:65-84 !$#title The myoglobin of primates. IV. New World monkeys: Cebidae: !1(1) Saimiri sciureus (squirrel monkey); (2) Lagothrix !1lagothricha (Humboldt's woolly monkey. Callitrichidae: !1Callithrix jacchus (common marmoset). !$#cross-references MUID:73231297; PMID:4198766 !$#contents compositions of tryptic and peptic peptides and sequences of !1residues 12-13, 19, 64-66, 79-83, 86, 103-106, 110-116, 118, !1133, and 140 !$#accession C90587 !'##molecule_type protein !'##residues 1-153 ##label ROM !'##note the peptides were positioned by homology with the human !1sequence REFERENCE A91390 !$#authors Romero-Herrera, A.E.; Lehmann, H. !$#journal FEBS Lett. (1973) 31:175-180 !$#title N-terminal chain elongation as evidence for duplication of !1myoglobin in three South American monkeys. !$#contents minor component !$#accession C91390 !'##molecule_type protein !'##residues 'FK',1-153 ##label RO2 COMMENT This myoglobin was isolated from skeletal muscle. CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 17017 #checksum 4517 SEQUENCE /// ENTRY MYHH #type complete TITLE myoglobin - western European hedgehog ORGANISM #formal_name Erinaceus europaeus #common_name western European hedgehog DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 03-Mar-2000 ACCESSIONS A02476 REFERENCE A02476 !$#authors Romero-Herrera, A.E.; Lehmann, H.; Fakes, W. !$#journal Biochim. Biophys. Acta (1975) 379:13-21 !$#title The primary structure of the myoglobin of the insectivore !1Erinaceus europaeus (common European hedgehog). !$#cross-references MUID:75109311; PMID:1167790 !$#accession A02476 !'##molecule_type protein !'##residues 1-153 ##label ROM !'##experimental_source skeletal muscle CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 16983 #checksum 4606 SEQUENCE /// ENTRY MYBD #type complete TITLE myoglobin - Eurasian badger (tentative sequence) ORGANISM #formal_name Meles meles #common_name Eurasian badger DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 31-Mar-2000 ACCESSIONS A02477 REFERENCE A02477 !$#authors Tetaert, D.; Han, K.; Plancot, M.T.; Dautrevaux, M.; !1Ducastaing, S.; Hombrados, I.; Neuzil, E. !$#journal Biochim. Biophys. Acta (1974) 351:317-324 !$#title The primary sequence of badger myoglobin. !$#cross-references MUID:74269748; PMID:4407312 !$#accession A02477 !'##molecule_type protein !'##residues 1-153 ##label TET CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 16965 #checksum 3405 SEQUENCE /// ENTRY MYOT #type complete TITLE myoglobin - Eurasian river otter ORGANISM #formal_name Lutra lutra #common_name Eurasian river otter DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 03-Mar-2000 ACCESSIONS JT0156 REFERENCE JT0156 !$#authors Sukhomlinov, B.F.; Sergienko, L.M. !$#journal Bioorg. Khim. (1986) 58:6-12 !$#title The primary structure of myoglobin from Otter (Lutra lutra !1L.). II. Peptic peptides of the tryptic insoluble core. !1Reconstruction of otter myoglobin polypeptide chain. !$#accession JT0156 !'##molecule_type protein !'##residues 1-153 ##label SUK !'##note peptides were positioned by homology CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 17036 #checksum 3257 SEQUENCE /// ENTRY PN0126 #type complete TITLE myoglobin - muskrat ORGANISM #formal_name Ondatra zibethicus #common_name muskrat DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 03-Mar-2000 ACCESSIONS PN0126 REFERENCE PN0126 !$#authors Sukhomlinov, B.F.; Vasilyeva, V.A. !$#journal Biokhimiia (1989) 54:956-964 !$#title The primary structure of ondatra (Ondatra zibethica) !1myoglobin: some peculiarities of functional morphology of !1myoglobins of semiaquatic animals. !$#cross-references MUID:90001338; PMID:2675985 !$#accession PN0126 !'##molecule_type protein !'##residues 1-153 ##label SUK !'##note article in Russian with English abstract CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 17137 #checksum 2531 SEQUENCE /// ENTRY MYDG #type complete TITLE myoglobin - dog (tentative sequence) ORGANISM #formal_name Canis lupus familiaris #common_name dog DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 31-Mar-2000 ACCESSIONS A90606; A90609; A02478 REFERENCE A90606 !$#authors Dumur, V.; Dautrevaux, M.; Han, K. !$#journal Biochim. Biophys. Acta (1976) 420:376-386 !$#title The covalent structure of dog myoglobin. !$#cross-references MUID:76136443; PMID:1252463 !$#accession A90606 !'##molecule_type protein !'##residues 1-50,'S',52-153 ##label DU1 REFERENCE A90609 !$#authors Dumur, V.; Dautrevaux, M.; Han, K. !$#journal Biochim. Biophys. Acta (1976) 427:759-761 !$#contents erratum !$#accession A90609 !'##molecule_type protein !'##residues 1-153 ##label DU2 CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 17206 #checksum 4025 SEQUENCE /// ENTRY MYFXBE #type complete TITLE myoglobin - bat-eared fox (tentative sequence) ORGANISM #formal_name Otocyon megalotis #common_name bat-eared fox DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 31-Mar-2000 ACCESSIONS A90611; A02478 REFERENCE A90611 !$#authors Darbre, P.D.; Lehmann, H. !$#journal Biochim. Biophys. Acta (1976) 453:285-288 !$#title Comparison of the myoglobin of the bat-eared fox (Otocyon !1megalotis) with that of the domestic dog (Canis familiaris). !$#cross-references MUID:77065657; PMID:793619 !$#accession A90611 !'##molecule_type protein !'##residues 1-153 ##label DAR CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 17206 #checksum 4025 SEQUENCE /// ENTRY MYDGAH #type complete TITLE myoglobin - African hunting dog (tentative sequence) ORGANISM #formal_name Lycaon pictus #common_name African hunting dog DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 31-Mar-2000 ACCESSIONS A90605; A02478 REFERENCE A90605 !$#authors Romero-Herrera, A.E.; Darbre, P.D.; Lehmann, H. !$#journal Biochim. Biophys. Acta (1976) 420:350-357 !$#title The myoglobin of the cape hunting dog (Lycaon pictus). !$#cross-references MUID:76136441; PMID:1252462 !$#accession A90605 !'##molecule_type protein !'##residues 1-153 ##label ROM CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 17233 #checksum 4010 SEQUENCE /// ENTRY MYFXC #type complete TITLE myoglobin - Cape fox (tentative sequence) ORGANISM #formal_name Vulpes chama #common_name Cape fox DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 31-Mar-2000 ACCESSIONS A90625; A02478 REFERENCE A90625 !$#authors Jones, L.T.; Castillo, O.; Lehmann, H. !$#journal Biochim. Biophys. Acta (1977) 493:460-464 !$#title The myoglobin of the Cape fox (Vulpes chama). !$#cross-references MUID:77242510; PMID:889878 !$#accession A90625 !'##molecule_type protein !'##residues 1-153 ##label JON CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 17206 #checksum 4052 SEQUENCE /// ENTRY MYZC #type complete TITLE myoglobin - California sealion (tentative sequence) ORGANISM #formal_name Zalophus californianus #common_name California sealion DATE 24-Apr-1984 #sequence_revision 30-Sep-1988 #text_change 31-Mar-2000 ACCESSIONS A02479 REFERENCE A02479 !$#authors Vigna, R.A.; Gurd, L.J.; Gurd, F.R.N. !$#journal J. Biol. Chem. (1974) 249:4144-4148 !$#title California sea lion myoglobin. Complete covalent structure !1of the polypeptide chain. !$#cross-references MUID:74298946; PMID:4850855 !$#accession A02479 !'##molecule_type protein !'##residues 1-153 ##label VIG CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 17249 #checksum 3693 SEQUENCE /// ENTRY MYSLG #type complete TITLE myoglobin - gray seal ORGANISM #formal_name Halichoerus grypus #common_name gray seal DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 16-Jun-2000 ACCESSIONS A93295; A02480 REFERENCE A93295 !$#authors Blanchetot, A.; Wilson, V.; Wood, D.; Jeffreys, A.J. !$#journal Nature (1983) 301:732-734 !$#title The seal myoglobin gene: an unusually long globin gene. !$#cross-references MUID:83141779; PMID:6828156 !$#accession A93295 !'##molecule_type DNA !'##residues 1-153 ##label BLA !'##cross-references GB:V00471; NID:g1122; PIDN:CAA23743.1; PID:g1234901 !'##note initiator Met not shown COMMENT This myoglobin was isolated from skeletal muscle. GENETICS !$#introns 32/2; 106/3 CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 17297 #checksum 3789 SEQUENCE /// ENTRY MYSLH #type complete TITLE myoglobin [validated] - harbor seal ORGANISM #formal_name Phoca vitulina #common_name harbor seal DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 15-Sep-2000 ACCESSIONS A92045; A02480 REFERENCE A92045 !$#authors Bradshaw, R.A.; Gurd, F.R.N. !$#journal J. Biol. Chem. (1969) 244:2167-2181 !$#title Comparison of myoglobins from harbor seal, porpoise, and !1sperm whale. !$#cross-references MUID:69177451; PMID:5782005 !$#accession A92045 !'##molecule_type protein !'##residues 1-153 ##label BRA !'##experimental_source skeletal muscle REFERENCE A50275 !$#authors Scouloudi, H. !$#submission submitted to the Brookhaven Protein Data Bank, March 1979 !$#cross-references PDB:1MBS !$#contents annotation; X-ray crystallography, 2.5 angstroms, residues !11-153 REFERENCE A92855 !$#authors Scouloudi, H.; Baker, E.N. !$#journal J. Mol. Biol. (1978) 126:637-660 !$#title X-ray crystallographic studies of seal myoglobin. The !1molecule at 2.5 angstrom resolution. !$#cross-references MUID:79132579; PMID:745243 !$#contents annotation; X-ray crystallography, 2.5 angstroms FUNCTION !$#description binds molecular oxygen for intracellular storage and !1transport, primarily in muscle CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status experimental\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status experimental SUMMARY #length 153 #molecular-weight 17297 #checksum 3789 SEQUENCE /// ENTRY MYBTF #type complete TITLE myoglobin - Egyptian rousette (tentative sequence) ORGANISM #formal_name Rousettus aegyptiacus #common_name Egyptian rousette DATE 30-Jun-1979 #sequence_revision 30-Jun-1979 #text_change 31-Mar-2000 ACCESSIONS A02481 REFERENCE A02481 !$#authors Castillo, O.; Lehmann, H. !$#journal Biochim. Biophys. Acta (1977) 492:232-236 !$#title The myoglobin of the fruit-bat (Rousettus aegyptiacus). !$#cross-references MUID:77182228; PMID:861250 !$#accession A02481 !'##molecule_type protein !'##residues 1-153 ##label CAS CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 16947 #checksum 5041 SEQUENCE /// ENTRY MYOY #type complete TITLE myoglobin - aardvark ORGANISM #formal_name Orycteropus afer #common_name aardvark DATE 15-Nov-1984 #sequence_revision 15-Nov-1984 #text_change 03-Mar-2000 ACCESSIONS A02482 REFERENCE A02482 !$#authors Dene, H.; Goodman, M.; Walz, D.A.; Romero-Herrera, A.E. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1983) 364:1585-1595 !$#title The phylogenetic position of aardvark (Orycteropus afer) as !1suggested by its myoglobin. !$#cross-references MUID:84110069; PMID:6662504 !$#accession A02482 !'##molecule_type protein !'##residues 1-153 ##label DEN CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 17012 #checksum 4396 SEQUENCE /// ENTRY MYTS #type complete TITLE myoglobin - common tree shrew (tentative sequence) ORGANISM #formal_name Tupaia glis belangeri #common_name common tree shrew DATE 24-Apr-1984 #sequence_revision 30-Sep-1988 #text_change 31-Mar-2000 ACCESSIONS A02483 REFERENCE A02483 !$#authors Romero-Herrera, A.E.; Lehmann, H. !$#journal Biochim. Biophys. Acta (1974) 359:236-241 !$#title The myoglobin of primates. VI. Tupaia glis belangeri (common !1treeshrew). !$#cross-references MUID:74308940; PMID:4605302 !$#accession A02483 !'##molecule_type protein !'##residues 1-153 ##label ROM CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 16967 #checksum 3729 SEQUENCE /// ENTRY MYMS #type complete TITLE myoglobin - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 04-Dec-1986 #sequence_revision 19-Apr-1996 #text_change 21-Jul-2000 ACCESSIONS A25799; T01679; A02484 REFERENCE A25799 !$#authors Blanchetot, A.; Price, M.; Jeffreys, A.J. !$#journal Eur. J. Biochem. (1986) 159:469-474 !$#title The mouse myoglobin gene. Characterisation and sequence !1comparison with other mammalian myoglobin genes. !$#cross-references MUID:87004662; PMID:3758071 !$#accession A25799 !'##molecule_type DNA !'##residues 1-154 ##label BLA !'##cross-references GB:X04405; NID:g53305; PIDN:CAA27994.1; !1PID:g1279552 !$#accession T01679 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-154 ##label BL2 !'##cross-references EMBL:X04405; NID:g53305; PIDN:CAA27994.1; !1PID:g1279552 REFERENCE A91346 !$#authors Harris, D.E.; Gurnett, A.M.; Lehmann, H.; Joysey, K.A. !$#journal FEBS Lett. (1985) 190:288-292 !$#title The myoglobin of rodents Proechimys guairae (casiragua) and !1Mus musculus (house mouse). !$#cross-references MUID:86005515; PMID:4043406 !$#accession A02484 !'##molecule_type protein !'##residues 2-115,'K',117-154 ##label HAR GENETICS !$#introns 32/2; 106/3 CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$3-148 #domain globin homology #label GLB\ !$65 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$94 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 154 #molecular-weight 17070 #checksum 6764 SEQUENCE /// ENTRY MYOL #type complete TITLE myoglobin - Ehrenberg's mole-rat ORGANISM #formal_name Spalax leucodon ehrenbergi #common_name Ehrenberg's mole-rat DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 03-Mar-2000 ACCESSIONS A02485 REFERENCE A92976 !$#authors Gurnett, A.M.; O'Connell, J.P.; Harris, D.E.; Lehmann, H.; !1Joysey, K.A.; Nevo, E. !$#journal J. Protein Chem. (1984) 3:445-454 !$#title The myoglobin of rodents: Lagostomus maximus (viscacha) and !1Spalax ehenbergi (mole rat). !$#accession A02485 !'##molecule_type protein !'##residues 1-153 ##label GUR !'##note 127-Thr was also found CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier; polymorphism FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 16924 #checksum 3559 SEQUENCE /// ENTRY MYRTNG #type complete TITLE myoglobin - northern gundi ORGANISM #formal_name Ctenodactylus gundi #common_name northern gundi DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Mar-2000 ACCESSIONS S13387; A33082 REFERENCE S13282 !$#authors Beintema, J.J.; Rodewald, K.; Braunitzer, G. !$#journal Biol. Chem. Hoppe-Seyler (1990) 371:1089-1099 !$#title The primary structures of gundi (Ctenodactylus gundi, !1Rodentia) hemoglobin and myoglobin. !$#cross-references MUID:91197427; PMID:2085415 !$#accession S13387 !'##molecule_type protein !'##residues 1-153 ##label BEI CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 16943 #checksum 3664 SEQUENCE /// ENTRY MYKS #type complete TITLE myoglobin - casiragua ORGANISM #formal_name Proechimys guairae #common_name casiragua DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 03-Mar-2000 ACCESSIONS A02486 REFERENCE A91346 !$#authors Harris, D.E.; Gurnett, A.M.; Lehmann, H.; Joysey, K.A. !$#journal FEBS Lett. (1985) 190:288-292 !$#title The myoglobin of rodents Proechimys guairae (casiragua) and !1Mus musculus (house mouse). !$#cross-references MUID:86005515; PMID:4043406 !$#accession A02486 !'##molecule_type protein !'##residues 1-153 ##label HAR CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 16867 #checksum 3295 SEQUENCE /// ENTRY MYVJ #type complete TITLE myoglobin - plains viscacha ORGANISM #formal_name Lagostomus maximus #common_name plains viscacha DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 03-Mar-2000 ACCESSIONS A02487 REFERENCE A92976 !$#authors Gurnett, A.M.; O'Connell, J.P.; Harris, D.E.; Lehmann, H.; !1Joysey, K.A.; Nevo, E. !$#journal J. Protein Chem. (1984) 3:445-454 !$#title The myoglobin of rodents: Lagostomus maximus (viscacha) and !1Spalax ehenbergi (mole rat). !$#accession A02487 !'##molecule_type protein !'##residues 1-153 ##label GUR !'##note 77-Arg was also found CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier; polymorphism FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 16879 #checksum 2978 SEQUENCE /// ENTRY MYLP #type complete TITLE myoglobin - potto (tentative sequence) ORGANISM #formal_name Perodicticus potto #common_name potto DATE 24-Apr-1984 #sequence_revision 27-Nov-1985 #text_change 03-Mar-2000 ACCESSIONS A02488 REFERENCE A02488 !$#authors Romero-Herrera, A.E.; Lehmann, H. !$#journal Biochim. Biophys. Acta (1975) 393:205-214 !$#title The myoglobin of primates. VII. Perodicticus potto edwarsi !1(potto). !$#cross-references MUID:75184111; PMID:1095064 !$#contents P. p. edwardsi, compositions of tryptic, peptic, and !1chymotryptic peptides and sequences of residues 1-4, 9, !121-22, 28, 32-35, 43, 51-52, 64-66, 110-113, and 140-142 !$#accession A02488 !'##molecule_type protein !'##residues 1-153 ##label ROM !'##experimental_source skeletal muscle !'##note the peptides were positioned by homology with the human !1sequence CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 16931 #checksum 3539 SEQUENCE /// ENTRY MYLR #type complete TITLE myoglobin - slow loris (tentative sequence) ORGANISM #formal_name Nycticebus coucang #common_name slow loris DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 03-Mar-2000 ACCESSIONS A02489 REFERENCE A02489 !$#authors Romero-Herrera, A.E.; Lehmann, H.; Castillo, O. !$#journal Biochim. Biophys. Acta (1976) 420:387-396 !$#title The myoglobin of primates. VIII. Nycticebus coucang (slow !1loris). !$#cross-references MUID:76136444; PMID:814928 !$#contents compositions of tryptic, peptic, and thermolytic peptides !1and sequences of residues 8-9, 21-22, 28, 32-35, 48, 51-52, !164-66, 80-81, 107-108, 110-113, 131-132, and 140-142 !$#accession A02489 !'##molecule_type protein !'##residues 1-153 ##label ROM !'##note the peptides were positioned by homology with the human !1sequence COMMENT This myoglobin was isolated from skeletal muscle. CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 16823 #checksum 3949 SEQUENCE /// ENTRY MYGC #type complete TITLE myoglobin - thick-tailed bush baby (tentative sequence) ORGANISM #formal_name Galago crassicaudatus, Otolemur crassicaudatus #common_name thick-tailed bush baby DATE 24-Apr-1984 #sequence_revision 30-Sep-1988 #text_change 31-Mar-2000 ACCESSIONS A02490 REFERENCE A90589 !$#authors Romero-Herrera, A.E.; Lehmann, H. !$#journal Biochim. Biophys. Acta (1973) 322:10-22 !$#title The myoglobin of primates. V. Prosimians: Galago !1crassicaudatus (thick-tailed galago) and Lepilemur !1mustelinus (sportive lemur). !$#cross-references MUID:74008816; PMID:4582928 !$#accession A02490 !'##molecule_type protein !'##residues 1-153 ##label ROM !'##note some amides were assigned by electrophoretic mobility or by !1homology CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 16970 #checksum 3619 SEQUENCE /// ENTRY MYLEM #type complete TITLE myoglobin - weasel lemur (tentative sequence) ORGANISM #formal_name Lepilemur mustelinus #common_name weasel lemur DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 31-Mar-2000 ACCESSIONS A02491 REFERENCE A90589 !$#authors Romero-Herrera, A.E.; Lehmann, H. !$#journal Biochim. Biophys. Acta (1973) 322:10-22 !$#title The myoglobin of primates. V. Prosimians: Galago !1crassicaudatus (thick-tailed galago) and Lepilemur !1mustelinus (sportive lemur). !$#cross-references MUID:74008816; PMID:4582928 !$#accession A02491 !'##molecule_type protein !'##residues 1-153 ##label ROM !'##note some amides were assigned by electrophoretic mobility or by !1homology CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 16942 #checksum 3504 SEQUENCE /// ENTRY MYRB #type complete TITLE myoglobin - rabbit (tentative sequence) ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 31-Mar-2000 ACCESSIONS A02492 REFERENCE A02492 !$#authors Romero-Herrera, A.E.; Lehmann, H.; Castillo, O. !$#journal Biochim. Biophys. Acta (1976) 439:51-54 !$#title The primary structure of the myoglobin of rabbit !1(Oryctolagus cuniculus). !$#cross-references MUID:76253773; PMID:952958 !$#accession A02492 !'##molecule_type protein !'##residues 1-153 ##label ROM CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 17089 #checksum 3150 SEQUENCE /// ENTRY MYOI #type complete TITLE myoglobin - southern American pika ORGANISM #formal_name Ochotona princeps #common_name southern American pika DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 03-Mar-2000 ACCESSIONS A02493 REFERENCE A02493 !$#authors Dene, H.; Goodman, M.; McKenna, M.C.; Romero-Herrera, A.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:1917-1920 !$#title Ochotona princeps (pika) myoglobin: an appraisal of !1lagomorph phylogeny. !$#cross-references MUID:82197608; PMID:6952242 !$#accession A02493 !'##molecule_type protein !'##residues 1-153 ##label DEN COMMENT The pika is a small animal related to the rabbit. CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 16977 #checksum 4630 SEQUENCE /// ENTRY MYDD #type complete TITLE myoglobin - bottle-nosed dolphin ORGANISM #formal_name Tursiops truncatus #common_name bottle-nosed dolphin DATE 01-Sep-1981 #sequence_revision 01-Sep-1981 #text_change 03-Mar-2000 ACCESSIONS A02494 REFERENCE A02494 !$#authors Jones, B.N.; Vigna, R.A.; Dwulet, F.E.; Bogardt, R.A.; !1Lehman, L.D.; Gurd, F.R.N. !$#journal Biochemistry (1976) 15:4418-4422 !$#title Complete amino acid sequence of the myoglobin from the !1Atlantic bottlenosed dolphin, Tursiops truncatus. !$#cross-references MUID:77022063; PMID:974068 !$#accession A02494 !'##molecule_type protein !'##residues 1-153 ##label JON CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 17057 #checksum 1515 SEQUENCE /// ENTRY MYDDBS #type complete TITLE myoglobin - saddleback dolphin ORGANISM #formal_name Delphinus delphis #common_name saddleback dolphin #note the saddleback dolphin is also called Black Sea dolphin DATE 27-Nov-1985 #sequence_revision 31-Mar-1991 #text_change 03-Mar-2000 ACCESSIONS A26230; A02497; A37509; A37510; A02494 REFERENCE A26230 !$#authors Wang, C.C.; Avila, R.; Jones, B.N.; Gurd, F.R.N. !$#journal Biochemistry (1977) 16:4978-4981 !$#title Complete primary structure of the major component myoglobin !1of Pacific common dolphin (Delphinus delphis). !$#cross-references MUID:78020893; PMID:911808 !$#accession A26230 !'##molecule_type protein !'##residues 1-153 ##label WAN REFERENCE A02497 !$#authors Kluh, I.; Bakardjieva, A. !$#journal FEBS Lett. (1971) 17:31-34 !$#title Primary structure of N-terminal part of molecule of dolphin !1myoglobin. !$#accession A02497 !'##molecule_type protein !'##residues 1-20,'V',22-27,'I',29-31 ##label KLU REFERENCE A37509 !$#authors Karadjova, M.; Nedkov, P.; Bakardjieva, A.; Genov, N. !$#journal Biochim. Biophys. Acta (1970) 221:136-139 !$#title Difference in amino acid sequence between dolphin and sperm !1whale myoglobins. !$#cross-references MUID:71014229; PMID:5473803 !$#accession A37509 !'##molecule_type protein !'##residues 31-65,'D',67-121,'Q',123-153 ##label KAR !'##note the amidation states of residues 60, 85, and 132 were not !1determined and were assigned by homology with the sperm !1whale sequence REFERENCE A37510 !$#authors Kluh, I. !$#submission submitted to the Atlas, December 1977 !$#contents revision to residue 26 !$#accession A37510 !'##molecule_type protein !'##residues 26 ##label KL2 CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 17057 #checksum 1515 SEQUENCE /// ENTRY MYWHL #type complete TITLE myoglobin - killer whale ORGANISM #formal_name Orcinus orca #common_name killer whale DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 03-Mar-2000 ACCESSIONS A92956; A90614; A02495 REFERENCE A92956 !$#authors Meuth, J.L.; Jones, B.N.; Gurd, F.R.N. !$#journal J. Mol. Evol. (1981) 17:163-166 !$#title Reassignment of residue 122 in the myoglobin from the killer !1whale, Orcinus orca. !$#cross-references MUID:81267443; PMID:6115067 !$#accession A92956 !'##molecule_type protein !'##residues 1-153 ##label MEU REFERENCE A90614 !$#authors Castillo, O.; Lehmann, H.; Jones, L.T. !$#journal Biochim. Biophys. Acta (1977) 491:23-28 !$#title The myoglobin of the killer whale (Orcinus orca). !$#cross-references MUID:77134898; PMID:849459 !$#accession A90614 !'##molecule_type protein !'##residues 1-121,'Q',123-153 ##label CAS COMMENT This myoglobin was isolated from skeletal muscle. CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 17071 #checksum 1151 SEQUENCE /// ENTRY MYWHT #type complete TITLE myoglobin - pilot whale ORGANISM #formal_name Globicephala melaena #common_name pilot whale DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 03-Mar-2000 ACCESSIONS A02496 REFERENCE A02496 !$#authors Jones, B.N.; Dwulet, F.E.; Lehman, L.D.; Garner, M.H.; !1Bogardt Jr., R.A.; Garner, W.H.; Gurd, F.R.N. !$#journal Biochemistry (1978) 17:1971-1974 !$#title Complete amino acid sequence of myoglobin from the pilot !1whale, Globicephala melaena. !$#cross-references MUID:78187213; PMID:656376 !$#accession A02496 !'##molecule_type protein !'##residues 1-153 ##label JON COMMENT This myoglobin was isolated from skeletal muscle. CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 17085 #checksum 1177 SEQUENCE /// ENTRY MYPE #type complete TITLE myoglobin - harbor porpoise ORGANISM #formal_name Phocoena phocoena #common_name harbor porpoise DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 03-Mar-2000 ACCESSIONS B92045; A90415; A02498 REFERENCE A92045 !$#authors Bradshaw, R.A.; Gurd, F.R.N. !$#journal J. Biol. Chem. (1969) 244:2167-2181 !$#title Comparison of myoglobins from harbor seal, porpoise, and !1sperm whale. !$#cross-references MUID:69177451; PMID:5782005 !$#accession B92045 !'##molecule_type protein !'##residues 1-82,'EAN',86-153 ##label BRA !'##note this sequence has been revised in reference A90415 !'##note this is the final paper in a series REFERENCE A90415 !$#authors Meuth, J.L.; Jones, B.N.; Garner, W.H.; Gurd, F.R.N. !$#journal Biochemistry (1978) 17:3429-3431 !$#title Complete amino acid sequence of the myoglobin from the Dall !1porpoise (Phocoenoides dalli dalli) and reinvestigation of !1the primary structure of the myoglobin from common porpoise !1(Phocoena phocoena). !$#cross-references MUID:79000346; PMID:687594 !$#accession A90415 !'##molecule_type protein !'##residues 56-90 ##label MEU CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 17101 #checksum 2245 SEQUENCE /// ENTRY MYPED #type complete TITLE myoglobin - Dall's porpoise ORGANISM #formal_name Phocoenoides dalli #common_name Dall's porpoise DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 03-Mar-2000 ACCESSIONS B90415; A02498 REFERENCE A90415 !$#authors Meuth, J.L.; Jones, B.N.; Garner, W.H.; Gurd, F.R.N. !$#journal Biochemistry (1978) 17:3429-3431 !$#title Complete amino acid sequence of the myoglobin from the Dall !1porpoise (Phocoenoides dalli dalli) and reinvestigation of !1the primary structure of the myoglobin from common porpoise !1(Phocoena phocoena). !$#cross-references MUID:79000346; PMID:687594 !$#accession B90415 !'##molecule_type protein !'##residues 1-153 ##label MEU CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 17101 #checksum 2245 SEQUENCE /// ENTRY MYDDAR #type complete TITLE myoglobin - Amazon dolphin ORGANISM #formal_name Inia geoffrensis #common_name Amazon dolphin DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 03-Mar-2000 ACCESSIONS A02503 REFERENCE A02503 !$#authors Dwulet, F.E.; Bogardt, R.A.; Jones, B.N.; Lehman, L.D.; !1Gurd, F.R.N. !$#journal Biochemistry (1975) 14:5336-5343 !$#title The complete amino acid sequence of the major component !1myoglobin of Amazon river dolphin (Inia geoffrensis). !$#cross-references MUID:76062412; PMID:1191640 !$#accession A02503 !'##molecule_type protein !'##residues 1-153 ##label DWU COMMENT This myoglobin was isolated from skeletal muscle. CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 17071 #checksum 1472 SEQUENCE /// ENTRY MYWHC #type complete TITLE myoglobin - California gray whale ORGANISM #formal_name Eschrichtius robustus, Eschrichtius gibbosus #common_name California gray whale DATE 01-Sep-1981 #sequence_revision 01-Sep-1981 #text_change 03-Mar-2000 ACCESSIONS A02499 REFERENCE A02499 !$#authors Bogardt Jr., R.A.; Dwulet, F.E.; Lehman, L.D.; Jones, B.N.; !1Gurd, F.R.N. !$#journal Biochemistry (1976) 15:2597-2602 !$#title Complete primary structure of the major component myoglobin !1of California gray whale (Eschrichtius gibbosus). !$#cross-references MUID:76232191; PMID:938629 !$#accession A02499 !'##molecule_type protein !'##residues 1-153 ##label BOG COMMENT This myoglobin was isolated from skeletal muscle. CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 17118 #checksum 1503 SEQUENCE /// ENTRY MYWHH #type complete TITLE myoglobin - humpback whale ORGANISM #formal_name Megaptera novaeangliae #common_name humpback whale DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 03-Mar-2000 ACCESSIONS A90416; A91088; A02500 REFERENCE A90416 !$#authors Lehman, L.D.; Dwulet, F.E.; Jones, B.N.; Bogardt Jr., R.A.; !1Krueckeberg, S.T.; Visscher, R.B.; Gurd, F.R.N. !$#journal Biochemistry (1978) 17:3736-3739 !$#title Complete amino acid sequence of the major component !1myoglobin from the humpback whale, Megaptera novaeangliae. !$#cross-references MUID:79021601; PMID:698193 !$#accession A90416 !'##molecule_type protein !'##residues 1-153 ##label LEH REFERENCE A91088 !$#authors Edman, P.; Begg, G. !$#journal Eur. J. Biochem. (1967) 1:80-91 !$#title A protein sequenator. !$#cross-references MUID:68049168; PMID:6059350 !$#accession A91088 !'##molecule_type protein !'##residues 1-60 ##label EDM !'##note this was the first sequence determined using the modern !1sequenator COMMENT This myoglobin was isolated from skeletal muscle. CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 17132 #checksum 1461 SEQUENCE /// ENTRY MYWHK #type complete TITLE myoglobin - minke whale ORGANISM #formal_name Balaenoptera acutorostrata #common_name minke whale, lesser rorqual DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 03-Mar-2000 ACCESSIONS A02501 REFERENCE A02501 !$#authors Lehman, L.D.; Dwulet, F.E.; Bogardt Jr., R.A.; Jones, B.N.; !1Gurd, F.R.N. !$#journal Biochemistry (1977) 16:706-709 !$#title The complete amino acid sequence of the major component !1myoglobin from the Arctic minke whale, Balaenoptera !1acutorostrata. !$#cross-references MUID:77112438; PMID:836810 !$#accession A02501 !'##molecule_type protein !'##residues 1-153 ##label LEH COMMENT This myoglobin was isolated from skeletal muscle. CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 17155 #checksum 1397 SEQUENCE /// ENTRY MYWHF #type complete TITLE myoglobin - finback whale ORGANISM #formal_name Balaenoptera physalus #common_name finback whale, common rorqual DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 03-Mar-2000 ACCESSIONS A02502 REFERENCE A02502 !$#authors DiMarchi, R.D.; Wang, C.C.; Hemenway, J.B.; Gurd, F.R.N. !$#journal Biochemistry (1978) 17:1968-1970 !$#title Complete amino acid sequence of the major component !1myoglobin of finback whale (Balaenoptera physalus). !$#cross-references MUID:78187212; PMID:656375 !$#accession A02502 !'##molecule_type protein !'##residues 1-153 ##label DIM COMMENT This myoglobin was isolated from skeletal muscle. CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 17086 #checksum 1423 SEQUENCE /// ENTRY MYWHZ #type complete TITLE myoglobin - goose-beaked whale ORGANISM #formal_name Ziphius cavirostris #common_name goose-beaked whale DATE 01-Sep-1981 #sequence_revision 01-Sep-1981 #text_change 03-Mar-2000 ACCESSIONS A02504 REFERENCE A02504 !$#authors Lehman, L.D.; Jones, B.N.; Dwulet, F.E.; Bogardt Jr., R.A.; !1Gurd, F.R.N. !$#journal Biochim. Biophys. Acta (1980) 625:221-229 !$#title Complete amino acid sequence of the major component !1myoglobin from the goose-beaked whale, Ziphius cavirostris. !$#cross-references MUID:81063290; PMID:7437458 !$#accession A02504 !'##molecule_type protein !'##residues 1-153 ##label LEH COMMENT This myoglobin was isolated from skeletal muscle. CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 17178 #checksum 1547 SEQUENCE /// ENTRY MYWHU #type complete TITLE myoglobin - Hubbs' whale ORGANISM #formal_name Mesoplodon carlhubbsi #common_name Hubbs' whale DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 03-Mar-2000 ACCESSIONS A02505 REFERENCE A02505 !$#authors Dwulet, J.A.; Dwulet, F.E.; Gurd, F.R.N. !$#journal Biochim. Biophys. Acta (1980) 624:121-129 !$#title Complete amino acid sequence of the major component !1myoglobin from Hubb's beaked whale, Mesoplodon carlhubbsi. !$#cross-references MUID:81000592; PMID:7407230 !$#accession A02505 !'##molecule_type protein !'##residues 1-153 ##label DWU COMMENT This myoglobin was isolated from skeletal muscle. CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 17136 #checksum 1609 SEQUENCE /// ENTRY MYWHP #type complete TITLE myoglobin [validated] - sperm whale ORGANISM #formal_name Physeter catodon #common_name sperm whale DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 15-Sep-2000 ACCESSIONS A90591; A92844; A93150; A02506 REFERENCE A90591 !$#authors Romero-Herrera, A.E.; Lehmann, H. !$#journal Biochim. Biophys. Acta (1974) 336:318-323 !$#title Residue 122 of sperm whale and horse myoglobin. !$#accession A90591 !'##molecule_type protein !'##residues 1-153 ##label ROM !'##experimental_source skeletal muscle REFERENCE A92844 !$#authors Takano, T. !$#journal J. Mol. Biol. (1977) 110:537-568 !$#title Structure of myoglobin refined at 2.0 angstrom resolution. !1I. Crystallographic refinement of metmyoglobin from sperm !1whale. !$#cross-references MUID:77144097; PMID:845959 !$#contents X-ray crystallography of metmyoglobin, 2.0 angstroms !$#accession A92844 !'##molecule_type protein !'##residues 1-120,'A',122-153 ##label TAK REFERENCE A93150 !$#authors Edmundson, A.B. !$#journal Nature (1965) 205:883-887 !$#title Amino-acid sequence of sperm whale myoglobin. !$#accession A93150 !'##molecule_type protein !'##residues 1-121,'N',123-153 ##label EDM !'##experimental_source heart muscle REFERENCE A50272 !$#authors Watson, H.C.; Kendrew, J.C. !$#submission submitted to the Brookhaven Protein Data Bank, April 1973 !$#cross-references PDB:1MBN !$#contents annotation; X-ray crystallography, 2.0 angstroms, residues !11-153 REFERENCE A50732 !$#authors Takano, T. !$#submission submitted to the Brookhaven Protein Data Bank, January 1988 !$#cross-references PDB:5MBN !$#contents annotation; X-ray crystallography, 2.0 angstroms, residues !11-153 REFERENCE A92845 !$#authors Takano, T. !$#journal J. Mol. Biol. (1977) 110:569-584 !$#title Structure of myoglobin refined at 2.0 angstrom resolution. !1II. Structure of deoxymyoglobin from sperm whale. !$#cross-references MUID:77144098; PMID:845960 !$#contents annotation; X-ray crystallography of deoxymyoglobin, 2.0 !1angstroms FUNCTION !$#description binds molecular oxygen for intracellular storage and !1transport, primarily in muscle CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status experimental\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status experimental SUMMARY #length 153 #molecular-weight 17200 #checksum 3184 SEQUENCE /// ENTRY MYWHW #type complete TITLE myoglobin - dwarf sperm whale ORGANISM #formal_name Kogia simus #common_name dwarf sperm whale DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 03-Mar-2000 ACCESSIONS A90407; A02506 REFERENCE A90407 !$#authors Dwulet, F.E.; Jones, B.N.; Lehman, L.D.; Gurd, F.R.N. !$#journal Biochemistry (1977) 16:873-877 !$#title The complete amino acid sequence of the major component !1myoglobin of dwarf sperm whale (Kogia simus). !$#cross-references MUID:77134684; PMID:843520 !$#accession A90407 !'##molecule_type protein !'##residues 1-153 ##label DWU CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 17237 #checksum 2523 SEQUENCE /// ENTRY MYELI #type complete TITLE myoglobin - Indian elephant ORGANISM #formal_name Elephas maximus #common_name Indian elephant DATE 30-Sep-1980 #sequence_revision 27-Nov-1985 #text_change 03-Mar-2000 ACCESSIONS A94228; A02507 REFERENCE A94228 !$#authors Dene, H.; Goodman, M.; Romero-Herrera, A.E. !$#journal Proc. R. Soc. Lond. B Biol. Sci. (1980) 207:111-127 !$#title The amino acid sequence of elephant (Elephas maximus) !1myoglobin and the phylogeny of Proboscidea. !$#cross-references MUID:80145813; PMID:6102395 !$#accession A94228 !'##molecule_type protein !'##residues 1-153 ##label DEN COMMENT This myoglobin was isolated from skeletal muscle. COMMENT The elephant myoglobins are exceptional in appearing to have !1glutamine rather than histidine as the distal axial ligand !1binding oxygen. CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (Gln) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 17008 #checksum 3094 SEQUENCE /// ENTRY MYELA #type complete TITLE myoglobin - African elephant ORGANISM #formal_name Loxodonta africana #common_name African elephant DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 03-Mar-2000 ACCESSIONS A02508 REFERENCE A92955 !$#authors Romero-Herrera, A.E.; Goodman, M.; Dene, H.; Bartnicki, !1D.E.; Mizukami, H. !$#journal J. Mol. Evol. (1981) 17:140-147 !$#title An exceptional amino acid replacement on the distal side of !1the iron atom in proboscidean myoglobin. !$#cross-references MUID:81267440; PMID:7265266 !$#accession A02508 !'##molecule_type protein !'##residues 1-153 ##label ROM COMMENT The elephant myoglobins are exceptional in appearing to have !1glutamine rather than histidine as the distal axial ligand !1binding oxygen. CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (Gln) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 17022 #checksum 3004 SEQUENCE /// ENTRY MYHO #type complete TITLE myoglobin [validated] - horse ORGANISM #formal_name Equus caballus #common_name domestic horse DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 15-Sep-2000 ACCESSIONS A91098; B90591; A34047; A02509 REFERENCE A91098 !$#authors Dautrevaux, M.; Boulanger, Y.; Han, K.; Biserte, G. !$#journal Eur. J. Biochem. (1969) 11:267-277 !$#title Structure covalente de la myoglobine de cheval. !$#cross-references MUID:70064092; PMID:4902609 !$#accession A91098 !'##molecule_type protein !'##residues 1-153 ##label DAU !'##experimental_source heart muscle REFERENCE A90591 !$#authors Romero-Herrera, A.E.; Lehmann, H. !$#journal Biochim. Biophys. Acta (1974) 336:318-323 !$#title Residue 122 of sperm whale and horse myoglobin. !$#accession B90591 !'##molecule_type protein !'##residues 1-121,'D',123-153 ##label ROM !'##experimental_source skeletal muscle REFERENCE A90157 !$#authors Jahnen, W.; Ward, L.D.; Reid, G.E.; Moritz, R.L.; Simpson, !1R.J. !$#journal Biochem. Biophys. Res. Commun. (1990) 166:139-145 !$#title Internal amino acid sequencing of proteins by in situ !1cyanogen bromide cleavage in polyacrylamide gels. !$#cross-references MUID:90147691; PMID:2302197 !$#accession A34047 !'##molecule_type protein !'##residues 1-6,'X',8-13,'X',15-16;57-70 ##label JAH REFERENCE A52032 !$#authors Evans, S.V.; Brayer, G.D. !$#submission submitted to the Brookhaven Protein Data Bank, September !11993 !$#cross-references PDB:1YMB !$#contents annotation; X-ray crystallography, 1.9 angstroms, residues !11-121,'D',123-153 REFERENCE A58444 !$#authors Evans, S.V.; Brayer, G.D. !$#journal J. Mol. Biol. (1990) 213:885-897 !$#title High resolution study of the three-dimensional structure of !1horse heart metmyoglobin. !$#cross-references MUID:90294302; PMID:2359126 !$#contents annotation; X-ray crystallography, 1.9 angstroms FUNCTION !$#description binds molecular oxygen for intracellular storage and !1transport, primarily in muscle CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status experimental\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status experimental SUMMARY #length 153 #molecular-weight 16950 #checksum 2648 SEQUENCE /// ENTRY MYHOZ #type complete TITLE myoglobin - common zebra (tentative sequence) ORGANISM #formal_name Equus burchelli, Equus quagga #common_name common zebra, plains zebra DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 03-Mar-2000 ACCESSIONS A90603; A02509 REFERENCE A90603 !$#authors Darbre, P.D.; Romero-Herrera, A.E.; Lehmann, H. !$#journal Biochim. Biophys. Acta (1975) 393:201-204 !$#title Comparison of the myoglobin of the zebra (Equus burchelli) !1with that of the horse (Equus caballus). !$#cross-references MUID:75184110; PMID:1095063 !$#contents composition of tryptic and peptic peptides !$#accession A90603 !'##molecule_type protein !'##residues 1-153 ##label DAR CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 16950 #checksum 2648 SEQUENCE /// ENTRY MYPG #type complete TITLE myoglobin [validated] - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 24-Apr-1984 #sequence_revision 11-Nov-1994 #text_change 15-Sep-2000 ACCESSIONS A23988; A02510 REFERENCE A23988 !$#authors Akaboshi, E. !$#journal Gene (1985) 40:137-140 !$#title Cloning and sequence analysis of porcine myoglobin cDNA. !$#cross-references MUID:86137410; PMID:3005120 !$#accession A23988 !'##molecule_type mRNA !'##residues 1-153 ##label AKA !'##cross-references GB:M14433; NID:g164546; PIDN:AAA31073.1; !1PID:g164547 !'##note initiator Met not shown REFERENCE A02510 !$#authors Rousseaux, J.; Dautrevaux, M.; Han, K. !$#journal Biochim. Biophys. Acta (1976) 439:55-62 !$#title Comparison of the amino acid sequence of pig heart myoglobin !1with other ungulate myoglobins. !$#cross-references MUID:76253774; PMID:952959 !$#accession A02510 !'##molecule_type protein !'##residues 1-153 ##label ROU REFERENCE A50317 !$#authors Smerdon, S.J.; Oldfield, T.J.; Dodson, E.J.; Dodson, G.G.; !1Hubbard, R.E.; Wilkinson, A.J. !$#submission submitted to the Brookhaven Protein Data Bank, November 1989 !$#cross-references PDB:1PMB !$#contents annotation; X-ray crystallography, 2.5 angstroms, residues !11-153 !$#note native and recombinant form expressed in Escherichia coli REFERENCE A44662 !$#authors Dodson, G.; Hubbard, R.E.; Oldfield, T.J.; Smerdon, S.J.; !1Wilkinson, A.J. !$#journal Protein Eng. (1988) 2:233-237 !$#title Apomyoglobin as a molecular recognition surface: expression, !1reconstitution and crystallization of recombinant porcine !1myoglobin in Escherichia coli. !$#cross-references MUID:89184426; PMID:3070546 !$#contents annotation; X-ray crystallography, 2.5 angstroms !$#note native and recombinant form expressed in Escherichia coli FUNCTION !$#description binds molecular oxygen for intracellular storage and !1transport, primarily in muscle CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status experimental\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status experimental SUMMARY #length 153 #molecular-weight 16953 #checksum 4034 SEQUENCE /// ENTRY MYSH #type complete TITLE myoglobin - sheep ORGANISM #formal_name Ovis orientalis aries, Ovis ammon aries #common_name domestic sheep DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 03-Mar-2000 ACCESSIONS A91195; A94596; A92969; A02511 REFERENCE A91195 !$#authors Han, K.; Tetaert, D.; Moschetto, Y.; Dautrevaux, M.; !1Kopeyan, C. !$#journal Eur. J. Biochem. (1972) 27:585-592 !$#title The covalent structure of sheep-heart myoglobin. !$#cross-references MUID:72254487; PMID:5065743 !$#accession A91195 !'##molecule_type protein !'##residues 1-98,'V',100,'I',102-153 ##label HAN REFERENCE A94596 !$#authors Han, K. !$#submission submitted to the Atlas, November 1972 !$#accession A94596 !'##molecule_type protein !'##residues 1-153 ##label HA2 REFERENCE A92969 !$#authors Votsch, W.; Anderer, F.A. !$#journal J. Mol. Evol. (1975) 5:315-326 !$#title The amino acid sequence of myoglobin from skeletal muscles !1of red deer (Cervus elaphus). !$#cross-references MUID:76072125; PMID:1202228 !$#accession A92969 !'##molecule_type protein !'##residues 140-144,'Q',146-153 ##label VOT COMMENT This myoglobin was isolated from heart muscle. CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 16923 #checksum 3023 SEQUENCE /// ENTRY MYDE #type complete TITLE myoglobin - red deer ORGANISM #formal_name Cervus elaphus #common_name red deer DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 03-Mar-2000 ACCESSIONS A02512 REFERENCE A92969 !$#authors Votsch, W.; Anderer, F.A. !$#journal J. Mol. Evol. (1975) 5:315-326 !$#title The amino acid sequence of myoglobin from skeletal muscles !1of red deer (Cervus elaphus). !$#cross-references MUID:76072125; PMID:1202228 !$#accession A02512 !'##molecule_type protein !'##residues 1-153 ##label VOT COMMENT This myoglobin was isolated from skeletal muscle. CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 16922 #checksum 3395 SEQUENCE /// ENTRY MYBO #type complete TITLE myoglobin - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 24-Apr-1984 #sequence_revision 12-May-1995 #text_change 16-Jun-2000 ACCESSIONS JX0068; A38821; A02513 REFERENCE JX0068 !$#authors Shimada, H.; Fukasawa, T.; Ishimura, Y. !$#journal J. Biochem. (1989) 105:417-422 !$#title Expression of bovine myoglobin cDNA as a functionally active !1holoprotein in Saccharomyces cerevisiae. !$#cross-references MUID:89278066; PMID:2659586 !$#accession JX0068 !'##molecule_type mRNA !'##residues 1-154 ##label SHI !'##cross-references GB:D00409; NID:g217579; PIDN:BAA00311.1; !1PID:g217580 !'##experimental_source fetal skeletal muscle !$#accession A38821 !'##molecule_type protein !'##residues 2-5 ##label SH2 !'##experimental_source fetal skeletal muscle REFERENCE A02513 !$#authors Han, K.; Dautrevaux, M.; Chaila, X.; Biserte, G. !$#journal Eur. J. Biochem. (1970) 16:465-471 !$#title The covalent structure of beef heart myoglobin. !$#cross-references MUID:71028010; PMID:5477290 !$#accession A02513 !'##molecule_type protein !'##residues 2-9,'A',11-99,'V',101,'I',103-122,'N',124,'A',126-129,'G', !1131-142,'A',144,'EK',147-154 ##label HAN !'##experimental_source cardiac muscle !'##note some peptides and residues were positioned by homology with !1horse myoglobin CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-154 #product myoglobin #status experimental #label MAT\ !$3-148 #domain globin homology #label GLB\ !$65 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$94 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 154 #molecular-weight 17078 #checksum 5708 SEQUENCE /// ENTRY MYOP #type complete TITLE myoglobin - North American opossum ORGANISM #formal_name Didelphis virginiana, Didelphis marsupialis virginiana #common_name North American opossum DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 03-Mar-2000 ACCESSIONS A02514 REFERENCE A02514 !$#authors Romero-Herrera, A.E.; Lehmann, H. !$#journal Biochim. Biophys. Acta (1975) 400:387-398 !$#title The primary structure of the myoglobin of Didelphis !1marsupialis (Virginia opossum). !$#cross-references MUID:76019100; PMID:1164514 !$#accession A02514 !'##molecule_type protein !'##residues 1-153 ##label ROM CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 16927 #checksum 2976 SEQUENCE /// ENTRY MYKGR #type complete TITLE myoglobin - red kangaroo (tentative sequence) ORGANISM #formal_name Macropus rufus, Megaleia rufa #common_name red kangaroo DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 31-Mar-2000 ACCESSIONS A02515 REFERENCE A02515 !$#authors Air, G.M.; Thompson, E.O.P. !$#journal Aust. J. Biol. Sci. (1971) 24:75-95 !$#title Studies on marsupial proteins. IV. Amino acid sequence of !1myoglobin from the red kangaroo, Megaleia rufa. !$#cross-references MUID:71164315; PMID:5553675 !$#accession A02515 !'##molecule_type protein !'##residues 1-153 ##label AIR CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 17138 #checksum 2353 SEQUENCE /// ENTRY MYTG #type complete TITLE myoglobin - Australian echidna (tentative sequence) ORGANISM #formal_name Tachyglossus aculeatus #common_name Australian echidna DATE 30-Jun-1979 #sequence_revision 30-Jun-1979 #text_change 31-Mar-2000 ACCESSIONS A02516 REFERENCE A02516 !$#authors Castillo, O.; Jones, L.T.; Lehmann, H. !$#journal Biochim. Biophys. Acta (1978) 533:289-292 !$#title The myoglobin of an echidna (Tachyglossus aculeatus !1aculeatus). !$#cross-references MUID:78166046; PMID:647011 !$#contents T. a. aculeatus !$#accession A02516 !'##molecule_type protein !'##residues 1-153 ##label CAS CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 17066 #checksum 3291 SEQUENCE /// ENTRY MYOR #type complete TITLE myoglobin - duckbill platypus (tentative sequence) ORGANISM #formal_name Ornithorhynchus anatinus #common_name duckbill platypus DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 31-Mar-2000 ACCESSIONS A02517 REFERENCE A02517 !$#authors Fisher, W.K.; Thompson, E.O.P. !$#journal Aust. J. Biol. Sci. (1976) 29:57-72 !$#title Studies on monotreme proteins. VII. Amino acid sequence of !1myoglobin from the platypus, Ornithorhynchus anatinus. !$#cross-references MUID:76277353; PMID:962722 !$#accession A02517 !'##molecule_type protein !'##residues 1-153 ##label FIS CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 16966 #checksum 3254 SEQUENCE /// ENTRY MYCH #type complete TITLE myoglobin - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 24-Apr-1984 #sequence_revision 30-Sep-1993 #text_change 11-May-2000 ACCESSIONS A60792; A02519; A02518 REFERENCE A60792 !$#authors Matsuoka, A.; Iwaasa, H.; Takiguchi, K.; Arakawa, N.; Li, !1L.; Takagi, T.; Shikama, K. !$#journal Comp. Biochem. Physiol. B (1987) 88:783-789 !$#title Stability properties of oxymyoglobin from chicken gizzard !1smooth muscle. !$#cross-references MUID:88110469; PMID:3427916 !$#accession A60792 !'##molecule_type protein !'##residues 1-153 ##label MAT REFERENCE A02519 !$#authors Prass, W.A.; Berkley, D.S.; Romero-Herrera, A.E. !$#journal Biochim. Biophys. Acta (1983) 742:677-680 !$#title Chicken cardiac myoglobin revisited. !$#cross-references MUID:83179027; PMID:6838896 !$#contents compositions of tryptic, chymotryptic, and peptic peptides !1and sequences of residues 51-54, 64-66, 75-76, 78, 80-84, !1and 140-141 !$#accession A02519 !'##molecule_type protein !'##residues 1-52,'NE',55-80,'Q',82-84,'D',86-153 ##label PRA !'##note this reference reconsiders some sequence assignments made below !1in reference A02518 !'##note the unsequenced residues were positioned by homology with the !1chicken sequence in reference A02518 !'##note this myoglobin was isolated from cardiac muscle REFERENCE A02518 !$#authors Deconinck, M.; Peiffer, S.; Depreter, J.; Paul, C.; Schnek, !1A.G.; Leonis, J. !$#journal Biochim. Biophys. Acta (1975) 386:567-575 !$#title The primary sequence of chicken myoglobin (Gallus gallus). !$#cross-references MUID:75183995; PMID:1169972 !$#accession A02518 !'##molecule_type protein !'##residues 1-51,'EPD',55-65,'Q',67-70,'A',72-73,'AQ',76-77,'K',79-80, !1'H',82-83,'AD',86-139,'D',141-153 ##label DEC CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 17291 #checksum 6850 SEQUENCE /// ENTRY MYPN #type complete TITLE myoglobin - emperor penguin (tentative sequence) ORGANISM #formal_name Aptenodytes forsteri #common_name emperor penguin DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 31-Mar-2000 ACCESSIONS A94423; A91402; A02520 REFERENCE A94423 !$#authors Castillo, O.; Lehmann, H.; Joysey, K.A.; Friday, A.E. !$#book Myoglobin, Schnek, A.G., and Vandecasserie, C., eds., !1pp.130-141, Editions de l'Universite de Bruxelles, Brussels, !11977 !$#accession A94423 !'##molecule_type protein !'##residues 1-152 ##label CAS REFERENCE A91402 !$#authors Peiffer, S.; Deconinck, M.; Paul, C.; Depreter, J.; Schnek, !1A.G.; Leonis, J. !$#journal FEBS Lett. (1973) 37:295-297 !$#title Penguin (Aptenodytes forsteri) myoglobin. A 70 residue !1N-terminal sequence. !$#cross-references MUID:74055088; PMID:4763336 !$#accession A91402 !'##molecule_type protein !'##residues 1-70 ##label PEI CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-146 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 152 #molecular-weight 17305 #checksum 4702 SEQUENCE /// ENTRY MYAQ #type complete TITLE myoglobin - American alligator (tentative sequence) ORGANISM #formal_name Alligator mississippiensis #common_name American alligator DATE 30-Sep-1980 #sequence_revision 01-Sep-1981 #text_change 31-Mar-2000 ACCESSIONS A02521 REFERENCE A02521 !$#authors Dene, H.; Sazy, J.; Goodman, M.; Romero-Herrera, A.E. !$#journal Biochim. Biophys. Acta (1980) 624:397-408 !$#title The amino acid sequence of alligator (Alligator !1mississippiensis) myoglobin. Phylogenetic implications. !$#cross-references MUID:81021710; PMID:6774758 !$#accession A02521 !'##molecule_type protein !'##residues 1-154 ##label DEN CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$3-148 #domain globin homology #label GLB\ !$65 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$94 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 154 #molecular-weight 17874 #checksum 9649 SEQUENCE /// ENTRY MYTTM #type complete TITLE myoglobin - map turtle ORGANISM #formal_name Graptemys geographica #common_name map turtle DATE 02-Apr-1982 #sequence_revision 02-Apr-1982 #text_change 03-Mar-2000 ACCESSIONS A02522 REFERENCE A02522 !$#authors Maeda, N.; Fitch, W.M. !$#journal J. Biol. Chem. (1981) 256:4293-4300 !$#title Amino acid sequence of a myoglobin isolated from map turtle, !1Graptemys geographica. !$#cross-references MUID:81168226; PMID:6783658 !$#accession A02522 !'##molecule_type protein !'##residues 1-153 ##label MAE CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 17495 #checksum 7602 SEQUENCE /// ENTRY MYTTG #type complete TITLE myoglobin - green seaturtle (tentative sequence) ORGANISM #formal_name Chelonia mydas #common_name green seaturtle DATE 17-May-1985 #sequence_revision 30-Sep-1988 #text_change 31-Mar-2000 ACCESSIONS A02523 REFERENCE A02523 !$#authors Watts, D.A.; Angelides, T.; Brown, W.D. !$#journal Biochim. Biophys. Acta (1983) 742:310-317 !$#title The primary structure of myoglobin from Pacific green sea !1turtle (Chelonia mydas caranigra). !$#cross-references MUID:83127407; PMID:6824692 !$#contents C. m. caranigra !$#accession A02523 !'##molecule_type protein !'##residues 1-153 ##label WAT !'##experimental_source skeletal muscle CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 17390 #checksum 6980 SEQUENCE /// ENTRY MYLZM #type complete TITLE myoglobin - lace monitor ORGANISM #formal_name Varanus varius #common_name lace monitor DATE 02-Apr-1982 #sequence_revision 02-Apr-1982 #text_change 03-Mar-2000 ACCESSIONS A02524 REFERENCE A02524 !$#authors Maeda, N.; Fitch, W.M. !$#journal J. Biol. Chem. (1981) 256:4301-4309 !$#title Amino acid sequence of a myoglobin from lace monitor lizard, !1Varanus varius, and its evolutionary implications. !$#cross-references MUID:81168227; PMID:6260792 !$#accession A02524 !'##molecule_type protein !'##residues 1-153 ##label MAE CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$93 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 153 #molecular-weight 17435 #checksum 7218 SEQUENCE /// ENTRY MYCA #type complete TITLE myoglobin - common carp ORGANISM #formal_name Cyprinus carpio #common_name common carp DATE 30-Sep-1980 #sequence_revision 30-Sep-1980 #text_change 03-Mar-2000 ACCESSIONS A02525 REFERENCE A02525 !$#authors Romero-Herrera, A.E. !$#submission submitted to the Atlas, July 1980 !$#accession A02525 !'##molecule_type protein !'##residues 1-146 ##label ROM CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; muscle; oxygen !1carrier FEATURE !$1-140 #domain globin homology #label GLB\ !$59 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$88 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15645 #checksum 6821 SEQUENCE /// ENTRY MYTUY #type complete TITLE myoglobin [validated] - yellowfin tuna ORGANISM #formal_name Thunnus albacares #common_name yellowfin tuna DATE 02-Apr-1982 #sequence_revision 02-Apr-1982 #text_change 15-Sep-2000 ACCESSIONS A02526 REFERENCE A02526 !$#authors Watts, D.A.; Rice, R.H.; Brown, W.D. !$#journal J. Biol. Chem. (1980) 255:10916-10924 !$#title The primary structure of myoglobin from yellowfin tuna !1(Thunnus albacares). !$#cross-references MUID:81046956; PMID:7430163 !$#accession A02526 !'##molecule_type protein !'##residues 1-146 ##label WAT REFERENCE A51306 !$#authors Birnbaum, G.I.; Evans, S.V.; Przybylska, M.; Rose, D.R. !$#submission submitted to the Brookhaven Protein Data Bank, May 1991 !$#cross-references PDB:1MYT !$#contents annotation; X-ray crystallography, 1.74 angstroms, residues !11-146 REFERENCE A58455 !$#authors Lattman, E.E.; Nockolds, C.E.; Kretsinger, R.H.; Love, W.E. !$#journal J. Mol. Biol. (1971) 60:271-277 !$#title Structure of yellow fin tuna metmyoglobin at 6 angstroms !1resolution. !$#cross-references MUID:72014155; PMID:5107328 !$#contents annotation; X-ray crystallography, 6.0 angstroms FUNCTION !$#description binds molecular oxygen for intracellular storage and !1transport, primarily in muscle CLASSIFICATION #superfamily globin; globin homology KEYWORDS acetylated amino end; chromoprotein; heme; iron; !1metalloprotein; muscle; oxygen carrier FEATURE !$1-140 #domain globin homology #label GLB\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$59 #binding_site oxygen (His) (distal axial ligand) !8#status experimental\ !$88 #binding_site heme iron (His) (proximal axial ligand) !8#status experimental SUMMARY #length 146 #molecular-weight 15529 #checksum 5101 SEQUENCE /// ENTRY MYRKJ #type complete TITLE myoglobin - Port Jackson shark ORGANISM #formal_name Heterodontus portusjacksoni #common_name Port Jackson shark DATE 31-May-1980 #sequence_revision 31-May-1980 #text_change 03-Mar-2000 ACCESSIONS A02527 REFERENCE A02527 !$#authors Fisher, W.K.; Thompson, E.O.P. !$#journal Aust. J. Biol. Sci. (1979) 32:277-294 !$#title Myoglobin of the shark Heterodontus portusjacksoni isolation !1and amino acid sequence. !$#cross-references MUID:80064553; PMID:508202 !$#accession A02527 !'##molecule_type protein !'##residues 1-148 ##label FIS CLASSIFICATION #superfamily globin; globin homology KEYWORDS acetylated amino end; chromoprotein; heme; iron; !1metalloprotein; muscle; oxygen carrier FEATURE !$1-142 #domain globin homology #label GLB\ !$1 #modified_site acetylated amino end (Thr) #status !8experimental\ !$59 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$88 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 148 #molecular-weight 16846 #checksum 6679 SEQUENCE /// ENTRY GGLMF #type complete TITLE globin - river lamprey ORGANISM #formal_name Lampetra fluviatilis #common_name river lamprey DATE 30-Apr-1980 #sequence_revision 30-Apr-1980 #text_change 03-Mar-2000 ACCESSIONS A02528 REFERENCE A02528 !$#authors Zelenik, M.; Rudloff, V.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1979) 360:1879-1894 !$#title Hemoglobins, XXX. The amino acid sequence of the monomeric !1hemoglobin from Lampetra fluviatilis. !$#cross-references MUID:80114121; PMID:118914 !$#accession A02528 !'##molecule_type protein !'##residues 1-149 ##label ZEL !'##note a second component is formylated at the amino end, probably !1artifactually CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxygen carrier FEATURE !$11-149 #domain globin homology #label GLB\ !$73 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$105 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 149 #molecular-weight 16273 #checksum 7737 SEQUENCE /// ENTRY GGLMS #type complete TITLE globin V [validated] - sea lamprey ORGANISM #formal_name Petromyzon marinus #common_name sea lamprey DATE 19-Feb-1984 #sequence_revision 07-Nov-1997 #text_change 15-Sep-2000 ACCESSIONS A90676; A92070; A92948; A02529 REFERENCE A90676 !$#authors Hombrados, I.; Rodewald, K.; Neuzil, E.; Braunitzer, G. !$#journal Biochimie (1983) 65:247-257 !$#title Haemoglobins, LX. Primary structure of the major haemoglobin !1of the sea lamprey Petromyzon marinus (var. Garonne, Loire). !$#cross-references MUID:83257424; PMID:6409159 !$#accession A90676 !'##molecule_type protein !'##residues 1-149 ##label HOM REFERENCE A92070 !$#authors Li, S.L.; Riggs, A. !$#journal J. Biol. Chem. (1970) 245:6149-6169 !$#title The amino acid sequence of hemoglobin V from the lamprey, !1Petromyzon marinus. !$#cross-references MUID:71051151; PMID:5484471 !$#accession A92070 !'##molecule_type protein !'##residues 1-97,'N',101-137,'R',140-149 ##label LIS REFERENCE A50479 !$#authors Honzatko, R.B.; Hendrickson, W.A.; Love, W.E. !$#submission submitted to the Brookhaven Protein Data Bank, August 1985 !$#cross-references PDB:2LHB !$#contents annotation; X-ray crystallography, 2.0 angstroms residues !11-62,'E',64-81,'D',83-99,'N',101-113,'E',115-149 REFERENCE A58465 !$#authors Honzatko, R.B.; Hendrickson, W.A.; Love, W.E. !$#journal J. Mol. Biol. (1985) 184:147-164 !$#title Refinement of a molecular model for lamprey hemoglobin from !1Petromyzon marinus. !$#cross-references MUID:85293078; PMID:4032476 !$#contents annotation; X-ray crystallography, 2.0 angstroms REFERENCE A92948 !$#authors Hendrickson, W.A.; Love, W.E.; Karle, J. !$#journal J. Mol. Biol. (1973) 74:331-361 !$#title Crystal structure analysis of sea lamprey hemoglobin at 2 !1Angstrom resolution. !$#cross-references MUID:73143809; PMID:4692855 !$#contents X-ray crystallography, 2.0 angstroms !$#accession A92948 !'##molecule_type protein !'##residues 1-95,'S',96-97,100-137,'R',139-149 ##label HEN !'##note 29-Asn was also found COMMENT Globin V is the major component of the six globins found in !1the sea lamprey. COMMENT This protein exists in both monomeric and dimeric forms. The !1equilibrium between the two forms depends on oxygen tension !1and pH. FUNCTION !$#description in erythrocytes binds and transports molecular oxygen from !1lung to tissues CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; erythrocyte; heme; iron; metalloprotein; !1oxygen carrier FEATURE !$11-149 #domain globin homology #label GLB\ !$73 #binding_site oxygen (His) (distal axial ligand) !8#status experimental\ !$105 #binding_site heme iron (His) (proximal axial ligand) !8#status experimental SUMMARY #length 149 #molecular-weight 16270 #checksum 7918 SEQUENCE /// ENTRY GGHF3G #type complete TITLE globin III - Atlantic hagfish ORGANISM #formal_name Myxine glutinosa #common_name Atlantic hagfish DATE 31-Aug-1979 #sequence_revision 31-Aug-1979 #text_change 03-Mar-2000 ACCESSIONS A02530 REFERENCE A02530 !$#authors Liljeqvist, G.; Braunitzer, G.; Paleus, S. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1979) 360:125-135 !$#title The amino acid sequence of hemoglobin III from Myxine !1glutinosa L. A new heme complex: E7 glutamine, E11 !1isoleucine. !$#cross-references MUID:79129113; PMID:422122 !$#accession A02530 !'##molecule_type protein !'##residues 1-148 ##label LIL COMMENT This monomeric globin is the main component in hagfish !1blood. COMMENT The Atlantic hagfish globin III is exceptional in appearing !1to have glutamine rather than histidine as the distal axial !1ligand binding oxygen. CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxygen carrier FEATURE !$11-147 #domain globin homology #label GLB\ !$71 #binding_site oxygen (Gln) (distal axial ligand) !8#status predicted\ !$103 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 148 #molecular-weight 16648 #checksum 4827 SEQUENCE /// ENTRY GGGAA #type complete TITLE globin [validated] - slug sea hare ALTERNATE_NAMES myoglobin ORGANISM #formal_name Aplysia limacina #common_name slug sea hare DATE 24-Apr-1984 #sequence_revision 31-Oct-1997 #text_change 15-Sep-2000 ACCESSIONS S64703; A02531 REFERENCE S64703 !$#authors Cutruzzola, F.; Travaglini Allocatelli, C.; Brancaccio, A.; !1Brunori, M. !$#journal Biochem. J. (1996) 314:83-90 !$#title Aplysia limacina myoglobin cDNA cloning: an alternative !1mechanism of oxygen stabilization as studied by active-site !1mutagenesis. !$#cross-references MUID:96195114; PMID:8660313 !$#accession S64703 !'##status preliminary !'##molecule_type mRNA !'##residues 2-146 ##label CU2 !'##cross-references EMBL:X79304; NID:g586940 REFERENCE A02531 !$#authors Tentori, L.; Vivaldi, G.; Carta, S.; Marinucci, M.; Massa, !1A.; Antonini, E.; Brunori, M. !$#journal Int. J. Pept. Protein Res. (1973) 5:187-200 !$#title The amino acid sequence of myoglobin from the mollusc !1Aplysia limacina. !$#cross-references MUID:74046672; PMID:4759566 !$#accession A02531 !'##molecule_type protein !'##residues 1-21,'N',23-25,'AD',28-76,'D',78-79,'N',81-128;130-146 !1##label TEN !'##experimental_source buccal muscle REFERENCE A50268 !$#authors Bolognesi, M.; Onesti, S.; Gatti, G.; Coda, A.; Ascenzi, P.; !1Brunori, M. !$#submission submitted to the Brookhaven Protein Data Bank, February 1989 !$#cross-references PDB:1MBA !$#contents annotation; X-ray crystallography, 1.6 angstroms, residues !11-21,'N',23-25,'LD',28-79,'N',81-145,'A' !$#note crystallographic evidence for 77-Asn, sequence revision REFERENCE A44584 !$#authors Bolognesi, M.; Onesti, S.; Gatti, G.; Coda, A.; Ascenzi, P.; !1Brunori, M. !$#journal J. Mol. Biol. (1989) 205:529-544 !$#title Aplysia limacina myoglobin. Crystallographic analysis at 1.6 !1angstroms resolution. !$#cross-references MUID:89178672; PMID:2926816 !$#contents annotation; X-ray crystallography, 1.6 angstroms; sequence !1revision !$#note crystallographic evidence for 129-Ala; description of heme !1iron binding site COMMENT This globin lacks the histidine distal heme ligand found in !1most other globins. FUNCTION !$#description binds molecular oxygen for intracellular storage and !1transport, primarily in muscle CLASSIFICATION #superfamily globin; globin homology KEYWORDS acetylated amino end; chromoprotein; heme; iron; !1metalloprotein; muscle; oxygen carrier FEATURE !$2-146 #domain globin homology #label GLB\ !$1 #modified_site acetylated amino end (Ser) #status !8experimental\ !$95 #binding_site heme iron (His) (proximal axial ligand) !8#status experimental SUMMARY #length 146 #molecular-weight 15324 #checksum 3012 SEQUENCE /// ENTRY GGGA2A #type complete TITLE globin - Kuroda's sea hare (tentative sequence) ORGANISM #formal_name Aplysia kurodai #common_name Kuroda's sea hare DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 31-Mar-2000 ACCESSIONS A02532; S20308 REFERENCE A02532 !$#authors Suzuki, T.; Takagi, T.; Shikama, K. !$#journal Biochim. Biophys. Acta (1981) 669:79-83 !$#title Amino acid sequence of myoglobin from Aplysia kurodai. !$#cross-references MUID:82046799; PMID:7295773 !$#accession A02532 !'##molecule_type protein !'##residues 1-144 ##label SUZ REFERENCE S20308 !$#authors Matsuoka, A.; Shikama, K. !$#journal Biochim. Biophys. Acta (1992) 1118:123-129 !$#title Stability properties of Aplysia oxymyoglobin: effect of !1esterification of the heme propionates. !$#cross-references MUID:92110346; PMID:1730027 !$#accession S20308 !'##molecule_type protein !'##residues 1-144 ##label MAT COMMENT This globin, like that of the slug sea hare (Aplysia !1limacina), lacks the distal heme histidine residue found in !1most other globins. CLASSIFICATION #superfamily globin; globin homology KEYWORDS acetylated amino end; chromoprotein; heme; iron; !1metalloprotein; muscle; oxygen carrier FEATURE !$2-144 #domain globin homology #label GLB\ !$1 #modified_site acetylated amino end (Ser) #status !8experimental\ !$95 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 144 #molecular-weight 15328 #checksum 9895 SEQUENCE /// ENTRY GGGDA #type complete TITLE globin - sea hare (Dolabella auricularia) ORGANISM #formal_name Dolabella auricularia DATE 30-Jun-1988 #sequence_revision 27-Jun-1994 #text_change 03-Mar-2000 ACCESSIONS A25331 REFERENCE A25331 !$#authors Suzuki, T. !$#journal J. Biol. Chem. (1986) 261:3692-3699 !$#title Amino acid sequence of myoglobin from the mollusc Dolabella !1auricularia. !$#cross-references MUID:86140164; PMID:3949784 !$#accession A25331 !'##molecule_type protein !'##residues 1-146 ##label SUZ COMMENT This globin, like that of the sea hare Aplysia limacina, !1lacks the distal heme histidine residue found in most other !1globins. CLASSIFICATION #superfamily globin; globin homology KEYWORDS acetylated amino end; chromoprotein; heme; iron; !1metalloprotein; muscle; oxygen carrier FEATURE !$2-146 #domain globin homology #label GLB\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$95 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15319 #checksum 3632 SEQUENCE /// ENTRY GGNKT #type complete TITLE globin beta chain - ark shell (Anadara trapezia) ORGANISM #formal_name Anadara trapezia DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 03-Mar-2000 ACCESSIONS A02533 REFERENCE A02533 !$#authors Gilbert, A.T.; Thompson, E.O.P. !$#journal Aust. J. Biol. Sci. (1985) 38:221-236 !$#title Amino acid sequence of the beta-chain of the tetrameric !1haemoglobin of the bivalve mollusc, Anadara trapezia. !$#cross-references MUID:86130215; PMID:4091752 !$#accession A02533 !'##molecule_type protein !'##residues 1-151 ##label GIL CLASSIFICATION #superfamily globin; globin homology KEYWORDS acetylated amino end; chromoprotein; erythrocyte; heme; !1iron; metalloprotein; oxygen carrier FEATURE !$12-151 #domain globin homology #label GLB\ !$1 #modified_site acetylated amino end (Ser) #status !8experimental\ !$71 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$103 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 151 #molecular-weight 16393 #checksum 2765 SEQUENCE /// ENTRY HANK2 #type complete TITLE hemoglobin II - ark shell (Anadara trapezia) ORGANISM #formal_name Anadara trapezia DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Mar-2000 ACCESSIONS S06502; S06717 REFERENCE S06502 !$#authors Fisher, W.K.; Gilbert, A.T.; Thompson, E.O.P. !$#journal Aust. J. Biol. Sci. (1984) 37:191-203 !$#title Amino acid sequence of the globin IIB chain of the dimeric !1haemoglobin of the bivalve mollusc Andara trapezia. !$#accession S06502 !'##molecule_type protein !'##residues 1-146 ##label FIS !'##note 42-Asp and 139-Ser were also found !'##note this sequence was obtained from hemoglobin IIb REFERENCE S06717 !$#authors Mann, R.G.; Fisher, W.K.; Gilbert, A.T.; Thompson, E.O.P. !$#journal Aust. J. Biol. Sci. (1986) 39:109-115 !$#title Genetic variation of the dimeric haemoglobin of the bivalve !1mollusc Anadara trapezia. !$#accession S06717 !'##molecule_type protein !'##residues 54-63,'D',65-67 ##label MAN !'##note this sequence was obtained from hemoglobin IIa COMMENT Hemoglobins IIa and IIb are probably allelic variants. CLASSIFICATION #superfamily globin; globin homology KEYWORDS blood; chromoprotein; erythrocyte; heme; homodimer; iron; !1metalloprotein; oxygen carrier FEATURE !$10-146 #domain globin homology #label GLB\ !$69 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$101 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15995 #checksum 8305 SEQUENCE /// ENTRY GGNKIB #type complete TITLE globin I - ark shell (Anadara broughtonii) ORGANISM #formal_name Anadara broughtonii #common_name blood clam DATE 20-Sep-1984 #sequence_revision 20-Sep-1984 #text_change 03-Mar-2000 ACCESSIONS A02534 REFERENCE A02534 !$#authors Furuta, H.; Kajita, A. !$#journal Biochemistry (1983) 22:917-922 !$#title Dimeric hemoglobin of the bivalve mollusc Anadara !1broughtonii: complete amino acid sequence of the globin !1chain. !$#cross-references MUID:83178885; PMID:6838831 !$#accession A02534 !'##molecule_type protein !'##residues 1-146 ##label FUR COMMENT This chain is from the intracellular hemolymph globin HbI, !1which is a dimer of identical chains. CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; dimer; heme; iron; metalloprotein; oxygen !1carrier FEATURE !$10-146 #domain globin homology #label GLB\ !$69 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$101 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15856 #checksum 9103 SEQUENCE /// ENTRY GGNKID #type complete TITLE globin I - ark shell (Scapharca inaequivalvis) ALTERNATE_NAMES dimeric hemoglobin; hemoglobin I ORGANISM #formal_name Scapharca inaequivalvis DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 03-Mar-2000 ACCESSIONS A02535; S07100 REFERENCE A91339 !$#authors Petruzzelli, R.; Goffredo, B.M.; Barra, D.; Bossa, F.; !1Boffi, A.; Verzili, D.; Ascoli, F.; Chiancone, E. !$#journal FEBS Lett. (1985) 184:328-332 !$#title Amino acid sequence of the cooperative homodimeric !1hemoglobin from the mollusc Scapharca inaequivalvis and !1topology of the intersubunit contacts. !$#cross-references MUID:85204369; PMID:3996589 !$#accession A02535 !'##molecule_type protein !'##residues 1-146 ##label PET1 !'##experimental_source hemocytes REFERENCE A93364 !$#authors Royer, W.E.; Love, W.E.; Fenderson, F.F. !$#journal Nature (1985) 316:277-280 !$#title Cooperative dimeric and tetrameric clam haemoglobins are !1novel assemblages of myoglobin folds. !$#cross-references MUID:85268020; PMID:4022123 !$#contents annotation; X-ray crystallography, 5.5 angstroms REFERENCE S07100 !$#authors Petruzzelli, R.; Boffi, A.; Barra, D.; Bossa, F.; Ascoli, !1F.; Chiancone, E. !$#journal FEBS Lett. (1989) 259:133-136 !$#title Scapharca hemoglobins, type cases of a novel mode of chain !1assembly and heme-heme communication. Amino acid sequence !1and subunit interactions of the tetrameric component. !$#cross-references MUID:90092513; PMID:2599099 !$#accession S07100 !'##molecule_type protein !'##residues 1-146 ##label PET2 COMMENT The molecule is a dimer of identical chains; their assembly !1is quite different from that of vertebrate hemoglobin. CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; homodimer; iron; metalloprotein; oxygen !1carrier FEATURE !$10-146 #domain globin homology #label GLB\ !$69 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$101 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15945 #checksum 9000 SEQUENCE /// ENTRY GGGAB #type complete TITLE globin - channeled whelk ORGANISM #formal_name Busycon canaliculatum #common_name channeled whelk DATE 24-Apr-1984 #sequence_revision 18-Aug-1995 #text_change 03-Mar-2000 ACCESSIONS A02536; A44589 REFERENCE A02536 !$#authors Bonner, A.G.; Laursen, R.A. !$#journal FEBS Lett. (1977) 73:201-203 !$#title The amino acid sequence of a dimeric myoglobin from the !1gastropod mollusc, Busycon canaliculatum L. !$#cross-references MUID:77116159; PMID:838061 !$#accession A02536 !'##molecule_type protein !'##residues 1-116,'Z',118-123,'Q',125-147 ##label BON REFERENCE A44588 !$#authors Laursen, R.A. !$#submission submitted to the Protein Sequence Database, June 1994 !$#accession A44589 !'##molecule_type protein !'##residues 117-125 ##label LAU !'##note sequence correction with revised composition COMMENT This globin was isolated from the radular muscle of this !1gastropod mollusc. COMPLEX homodimer CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; homodimer; iron; metalloprotein; !1muscle; oxygen carrier FEATURE !$2-147 #domain globin homology #label GLB\ !$66 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$98 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 147 #molecular-weight 15736 #checksum 5974 SEQUENCE /// ENTRY GGGACR #type complete TITLE globin - horn shell (Cerithidea rhizophorarum) (tentative sequence) ALTERNATE_NAMES myoglobin ORGANISM #formal_name Cerithidea rhizophorarum DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 31-Mar-2000 ACCESSIONS A02537 REFERENCE A02537 !$#authors Takagi, T.; Tobita, M.; Shikama, K. !$#journal Biochim. Biophys. Acta (1983) 745:32-36 !$#title Amino acid sequence of dimeric myoglobin from Cerithidea !1rhizophorarum. !$#cross-references MUID:83204919; PMID:6849938 !$#accession A02537 !'##molecule_type protein !'##residues 1-151 ##label TAK COMMENT This globin was isolated from the radular muscle of this !1gastropod mollusc. CLASSIFICATION #superfamily globin; globin homology KEYWORDS acetylated amino end; chromoprotein; heme; iron; !1metalloprotein; muscle; oxygen carrier FEATURE !$2-151 #domain globin homology #label GLB\ !$1 #modified_site acetylated amino end (Ser) #status !8experimental\ !$66 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$98 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 151 #molecular-weight 16210 #checksum 918 SEQUENCE /// ENTRY JC1516 #type complete TITLE globin - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 14-Jul-1994 #sequence_revision 14-Jul-1994 #text_change 03-Mar-2000 ACCESSIONS JC1516; S32218; S15801 REFERENCE JC1516 !$#authors Kloek, A.P.; Sherman, D.R.; Goldberg, D.E. !$#journal Gene (1993) 129:215-221 !$#title Novel gene structure and evolutionary context of !1Caenorhabditis elegans globin. !$#cross-references MUID:93314965; PMID:8325507 !$#accession JC1516 !'##molecule_type DNA !'##residues 1-159 ##label KLO !'##cross-references GB:Z11115; NID:g6953; PID:g6965; GB:Z18264 REFERENCE S32218 !$#authors Kloek, A.P. !$#submission submitted to the EMBL Data Library, October 1992 !$#accession S32218 !'##molecule_type mRNA !'##residues 1-34,'Y',36-159 ##label KL2 !'##cross-references EMBL:Z18264; NID:g288467; PIDN:CAA79148.1; !1PID:g288468 COMMENT This globin lacks the distal heme histidine residue found in !1most other globins. GENETICS !$#gene Glo !$#introns 65/2 CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxygen carrier FEATURE !$9-152 #domain globin homology #label GLB\ !$69 #binding_site oxygen (Gln) (distal axial ligand) !8#status predicted\ !$101 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 159 #molecular-weight 18485 #checksum 9928 SEQUENCE /// ENTRY GGNW1B #type complete TITLE globin, major monomeric component - polychaete (Glycera dibranchiata) ORGANISM #formal_name Glycera dibranchiata #common_name bloodworm DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 03-Mar-2000 ACCESSIONS A02538 REFERENCE A92104 !$#authors Imamura, T.; Baldwin, T.O.; Riggs, A. !$#journal J. Biol. Chem. (1972) 247:2785-2797 !$#title The amino acid sequence of the monomeric hemoglobin !1component from the bloodworm, Glycera dibranchiata. !$#cross-references MUID:72181368; PMID:5063466 !$#accession A02538 !'##molecule_type protein !'##residues 1-147 ##label IMA !'##note experimental results indicate the possibility that some chains !1may have Gly instead of Asp at position 20 !'##note either Glx-65 or Glx-76 is amidated !'##note the sequence of the amino-terminal 35 residues of a minor !1monomeric component differs from that region of the major !1component only in lacking the first and second residues !'##note a second minor monomeric component has been partially sequenced REFERENCE A92151 !$#authors Padlan, E.A.; Love, W.E. !$#journal J. Biol. Chem. (1974) 249:4067-4078 !$#title Three-dimensional structure of hemoglobin from the !1polychaete annelid, Glycera dibranchiata, at 2.5 A !1resolution. !$#cross-references MUID:74309555; PMID:4855197 !$#contents annotation; X-ray crystallography, 2.5 angstroms !$#note X-ray crystallographic analysis indicates that the D helix !1is absent, Leu-58 replaces the distal His (of myoglobin E7), !1His-90 binds to the heme iron, the F helix has several more !1residues than in mammalian globins, and Pro-105 (G7) causes !1a bend in the G helix CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxygen carrier FEATURE !$90 #binding_site heme iron (His) (proximal axial ligand) !8#status experimental SUMMARY #length 147 #molecular-weight 14979 #checksum 8096 SEQUENCE /// ENTRY GGNW3B #type fragment TITLE globin, minor monomeric component - polychaete (Glycera dibranchiata) (fragment) ORGANISM #formal_name Glycera dibranchiata #common_name bloodworm DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 01-Aug-1997 ACCESSIONS A02539 REFERENCE A02539 !$#authors Li, S.L.; Riggs, A.F. !$#journal Biochim. Biophys. Acta (1971) 236:208-210 !$#title Partial sequence of the NH-2-terminal segment of Glycera !1hemoglobin. Homology with sperm whale myoglobin. !$#cross-references MUID:71201068; PMID:5577463 !$#accession A02539 !'##molecule_type protein !'##residues 1-45 ##label LIS !'##note the residue at position 13 is probably Cys !'##note the sequence of this fragment differs from the corresponding !1region of the major monomeric component at 9 of the 42 known !1positions CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; oxygen carrier FEATURE !$1-45 #product globin, minor monomeric component (fragment) !8#status experimental #label MAT SUMMARY #length 45 #checksum 6360 SEQUENCE /// ENTRY GGEWA3 #type complete TITLE globin AIII - earthworm (Lumbricus terrestris) ALTERNATE_NAMES erythrocruorin ORGANISM #formal_name Lumbricus terrestris #common_name common earthworm DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 03-Mar-2000 ACCESSIONS A02540 REFERENCE A02540 !$#authors Garlick, R.L.; Riggs, A.F. !$#journal J. Biol. Chem. (1982) 257:9005-9015 !$#title The amino acid sequence of a major polypeptide chain of !1earthworm hemoglobin. !$#cross-references MUID:82239392; PMID:7096348 !$#accession A02540 !'##molecule_type protein !'##residues 1-157 ##label GAR COMMENT The sequence shown is one heme-binding chain of an !1extracellular globin that is a polymer of many subunits. CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxygen carrier FEATURE !$55 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$96 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 157 #molecular-weight 17493 #checksum 9522 SEQUENCE /// ENTRY GGWNS #type complete TITLE globin small chain, extracellular - polychaete (Tylorrhynchus heterochaetus) ALTERNATE_NAMES erythrocruorin ORGANISM #formal_name Tylorrhynchus heterochaetus #common_name Japanese palolo DATE 20-Sep-1984 #sequence_revision 20-Sep-1984 #text_change 03-Mar-2000 ACCESSIONS A02541 REFERENCE A02541 !$#authors Suzuki, T.; Takagi, T.; Gotoh, T. !$#journal Biochim. Biophys. Acta (1982) 708:253-258 !$#title Amino acid sequence of the smallest polypeptide chain !1containing heme of extracellular hemoglobin from the !1polychaete Tylorrhynchus heterochaetus. !$#accession A02541 !'##molecule_type protein !'##residues 1-139 ##label SUZ COMMENT This sequence is shorter than the normal globin due to the !1absence of seven residues in the G-helical region. CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxygen carrier FEATURE !$62 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$94 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 139 #molecular-weight 15705 #checksum 6043 SEQUENCE /// ENTRY GGWN2C #type complete TITLE globin IIC, extracellular - polychaete (Tylorrhynchus heterochaetus) ORGANISM #formal_name Tylorrhynchus heterochaetus #common_name Japanese palolo DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 03-Mar-2000 ACCESSIONS A02542 REFERENCE A02542 !$#authors Suzuki, T.; Furukohri, T.; Gotoh, T. !$#journal J. Biol. Chem. (1985) 260:3145-3154 !$#title Subunit structure of extracellular hemoglobin from the !1polychaete Tylorrhynchus heterochaetus and amino acid !1sequence of the constituent polypeptide chain (IIC). !$#cross-references MUID:85131096; PMID:3972820 !$#accession A02542 !'##molecule_type protein !'##residues 1-149 ##label SUZ COMMENT Tylorrhynchus heterochaetus is a marine worm. CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxygen carrier FEATURE !$4-148 #domain globin homology #label GLB\ !$66 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$98 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 149 #molecular-weight 16795 #checksum 4842 SEQUENCE /// ENTRY GGICE1 #type complete TITLE globin CTT-I - midge (Chironomus thummi thummi) ALTERNATE_NAMES erythrocruorin ORGANISM #formal_name Chironomus thummi thummi DATE 30-Apr-1980 #sequence_revision 01-Sep-1981 #text_change 03-Mar-2000 ACCESSIONS A91690; A02543 REFERENCE A91690 !$#authors Kleinschmidt, T.; von der Mark-Neuwirth, H.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1980) 361:401-411 !$#title Analyse der Primaerstruktur des monomeren !1Insektenhaemoglobins CTT I (Erythrocruorin) aus Chironomus !1thummi thummi, Diptera. !$#cross-references MUID:80202931; PMID:7380386 !$#accession A91690 !'##molecule_type protein !'##residues 1-143 ##label KLE COMMENT The functional molecule is a monomer. CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxygen carrier FEATURE !$59 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$94 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 143 #molecular-weight 15463 #checksum 4073 SEQUENCE /// ENTRY GGIC1A #type complete TITLE globin CTT-IA - midge (Chironomus thummi thummi) ALTERNATE_NAMES erythrocruorin ORGANISM #formal_name Chironomus thummi thummi DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 03-Mar-2000 ACCESSIONS A91719; PQ0171; A02543 REFERENCE A91719 !$#authors Goodman, M.; Braunitzer, G.; Kleinschmidt, T.; Aschauer, H. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1983) 364:205-217 !$#title The analysis of a protein-polymorphism. Evolution of !1monomeric and homodimeric haemoglobins (erythrocruorins) of !1Chironomus thummi thummi (Insecta, Diptera). !$#cross-references MUID:83236193; PMID:6862374 !$#accession A91719 !'##molecule_type protein !'##residues 1-143 ##label GOO REFERENCE PQ0171 !$#authors Saffarini, D.A.; Trewitt, P.M.; Luhm, R.A.; Bergtrom, G. !$#journal Gene (1991) 101:215-222 !$#title Differential regulation of insect globin and actin mRNAs !1during larval development in Chironomus thummi. !$#cross-references MUID:91276274; PMID:2055487 !$#accession PQ0171 !'##molecule_type mRNA !'##residues 68-143 ##label SAF !'##cross-references GB:M57410; NID:g156580; PIDN:AAA62727.1; !1PID:g156581 !'##experimental_source larva COMMENT The functional molecule is a monomer. CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxygen carrier FEATURE !$59 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$94 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 143 #molecular-weight 15493 #checksum 4852 SEQUENCE /// ENTRY GGICE2 #type complete TITLE globin CTT-II beta - midge (Chironomus thummi thummi) ORGANISM #formal_name Chironomus thummi thummi DATE 30-Apr-1980 #sequence_revision 30-Apr-1980 #text_change 03-Mar-2000 ACCESSIONS A02544 REFERENCE A02544 !$#authors Kleinschmidt, T.; Braunitzer, G. !$#journal Justus Liebigs Ann. Chem. (1978) 1978:1060-1075 !$#title Haemoglobins, XXIV. Concerning the primary structure of a !1dimeric haemoglobin, erythrocruorin, from insects (component !1II beta of Chironomus thummi thummi, Diptera). !$#accession A02544 !'##molecule_type protein !'##residues 1-145 ##label KLE COMMENT The functional molecule is a dimer. CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxygen carrier FEATURE !$3-145 #domain globin homology #label GLB\ !$60 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$95 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 145 #molecular-weight 15923 #checksum 5899 SEQUENCE /// ENTRY S14574 #type complete TITLE globin C precursor - midge (Chironomus tentans) ORGANISM #formal_name Chironomus tentans DATE 12-Nov-1999 #sequence_revision 12-Nov-1999 #text_change 03-Mar-2000 ACCESSIONS S14574 REFERENCE S14572 !$#authors Rozynek, P.; Broeker, M.; Hankeln, T.; Schmidt, E.R. !$#submission submitted to the EMBL Data Library, September 1990 !$#description The primary structure of several hemoglobin genes from the !1genome of Chironomus tentans. !$#accession S14574 !'##molecule_type DNA !'##residues 1-160 ##label ROZ !'##cross-references EMBL:X56272; NID:g7090; PIDN:CAA39723.1; PID:g7092 CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxygen carrier FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-160 #product globin C #status predicted #label MAT\ !$18-160 #domain globin homology #label GLB\ !$75 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$110 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 160 #molecular-weight 17618 #checksum 8622 SEQUENCE /// ENTRY GGICE9 #type complete TITLE globin CTT-IX - midge (Chironomus thummi thummi) ORGANISM #formal_name Chironomus thummi thummi DATE 30-Apr-1980 #sequence_revision 18-Aug-1982 #text_change 03-Mar-2000 ACCESSIONS A02545 REFERENCE A02545 !$#authors Steer, W.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1981) 362:59-71 !$#title Hemoglobins, XXXVI: the primary structure of a dimeric !1insect hemoglobin (erythrocruorin), component IX from !1Chironomus thummi thummi. Studies on the quaternary !1structure of the dimeric CTT-hemoglobins. !$#cross-references MUID:81166258; PMID:7216162 !$#accession A02545 !'##molecule_type protein !'##residues 1-145 ##label STE !'##note the functional molecule is a dimer CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxygen carrier FEATURE !$3-145 #domain globin homology #label GLB\ !$60 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$95 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 145 #molecular-weight 15576 #checksum 4616 SEQUENCE /// ENTRY S14575 #type complete TITLE globin D precursor - midge (Chironomus tentans) ORGANISM #formal_name Chironomus tentans DATE 12-Nov-1999 #sequence_revision 12-Nov-1999 #text_change 03-Mar-2000 ACCESSIONS S14575 REFERENCE S14572 !$#authors Rozynek, P.; Broeker, M.; Hankeln, T.; Schmidt, E.R. !$#submission submitted to the EMBL Data Library, September 1990 !$#description The primary structure of several hemoglobin genes from the !1genome of Chironomus tentans. !$#accession S14575 !'##molecule_type DNA !'##residues 1-161 ##label ROZ !'##cross-references EMBL:X56272; NID:g7090; PIDN:CAA39724.1; PID:g7093 CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxygen carrier FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-161 #product globin C #status predicted #label MAT\ !$19-161 #domain globin homology #label GLB\ !$76 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$111 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 161 #molecular-weight 17553 #checksum 1223 SEQUENCE /// ENTRY GGICE6 #type complete TITLE globin CTT-VI - midge (Chironomus thummi thummi) (tentative sequence) ORGANISM #formal_name Chironomus thummi thummi DATE 28-Feb-1980 #sequence_revision 31-Dec-1991 #text_change 31-Mar-2000 ACCESSIONS A02546; PQ0172 REFERENCE A02546 !$#authors Aschauer, H.; Zaidi, Z.H.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1981) 362:261-273 !$#title Hemoglobins, XXXVIII. Amino acid sequence of a dimeric !1hemoglobin (erythrocruorin), component VI from Chironomus !1thummi thummi (CTT VI). !$#cross-references MUID:81190266; PMID:7227979 !$#accession A02546 !'##molecule_type protein !'##residues 1-147 ##label ASC REFERENCE PQ0171 !$#authors Saffarini, D.A.; Trewitt, P.M.; Luhm, R.A.; Bergtrom, G. !$#journal Gene (1991) 101:215-222 !$#title Differential regulation of insect globin and actin mRNAs !1during larval development in Chironomus thummi. !$#cross-references MUID:91276274; PMID:2055487 !$#accession PQ0172 !'##molecule_type mRNA !'##residues 109-147 ##label SAF !'##cross-references GB:M57411; NID:g156582; PIDN:AAA62728.1; !1PID:g156583 !'##experimental_source larva CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; homodimer; iron; metalloprotein; oxygen !1carrier FEATURE !$3-146 #domain globin homology #label GLB\ !$60 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$95 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 147 #molecular-weight 16205 #checksum 23 SEQUENCE /// ENTRY GGICE8 #type complete TITLE globin CTT-VIIB - midge (Chironomus thummi thummi) (tentative sequence) ORGANISM #formal_name Chironomus thummi thummi DATE 31-Aug-1979 #sequence_revision 31-Aug-1979 #text_change 31-Mar-2000 ACCESSIONS A02547 REFERENCE A02547 !$#authors Sladic-Simic, D.; Kleinschmidt, T.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1979) 360:115-124 !$#title Analysis of the primary structure of the dimeric insect !1haemoglobin CTT VIIB (erythrocruorin) from Chironomus thummi !1thummi, Diptera. !$#cross-references MUID:79129112; PMID:422121 !$#accession A02547 !'##molecule_type protein !'##residues 1-145 ##label SLA !'##note another component may exist, as 37-Met, 41-Ser, 75-Met, 78-Ala, !1110-Thr, and 138-Phe were also found in equal amounts CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxygen carrier FEATURE !$3-145 #domain globin homology #label GLB\ !$60 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$95 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 145 #molecular-weight 15326 #checksum 2173 SEQUENCE /// ENTRY JT0292 #type complete TITLE hemoglobin VIIB-5/VIIB-6 precursor - midge (Chironomus thummi piger) ORGANISM #formal_name Chironomus thummi piger DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jun-2000 ACCESSIONS JT0292; S21629; S21630 REFERENCE JT0292 !$#authors Hankeln, T.; Rozynek, P.; Schmidt, E.R. !$#journal Gene (1988) 64:297-304 !$#title The nucleotide sequence and in situ localization of a gene !1for a dimeric haemoglobin from the midge Chironomus thummi !1piger. !$#cross-references MUID:88297160; PMID:2841201 !$#accession JT0292 !'##molecule_type DNA !'##residues 1-161 ##label HAN !'##cross-references GB:M20918; NID:g156578; PIDN:AAA28259.1; !1PID:g156579 REFERENCE S21627 !$#authors Hankeln, T.; Rozynek, P.; Schmidt, E.R. !$#submission submitted to the EMBL Data Library, September 1990 !$#description Complete nucleotide sequence of a hemoglobin gene cluster !1from the midge Chironomus thummi piger. !$#accession S21629 !'##molecule_type DNA !'##residues 1-161 ##label HAW !'##cross-references EMBL:X56271; NID:g7069; PIDN:CAA39714.1; PID:g7072 !'##genetics 7B5 !$#accession S21630 !'##molecule_type DNA !'##residues 1-161 ##label HA2 !'##cross-references EMBL:X56271; NID:g7069; PIDN:CAA39714.1; PID:g7072 !'##genetics 7B6 GENETICS 7B5 !$#gene HbVIIB-5 !$#map_position II GENETICS 7B6 !$#gene HbVIIB-6 CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxygen carrier FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-161 #product hemoglobin #status predicted #label MAT\ !$19-161 #domain globin homology #label GLB\ !$111 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 161 #molecular-weight 16945 #checksum 4958 SEQUENCE /// ENTRY JT0349 #type complete TITLE hemoglobin VIIB-5 precursor - midge (Chironomus thummi thummi) ORGANISM #formal_name Chironomus thummi thummi DATE 12-Nov-1999 #sequence_revision 12-Nov-1999 #text_change 03-Mar-2000 ACCESSIONS JT0349 REFERENCE JT0349 !$#authors Trewitt, P.M.; Saffarini, D.A.; Bergtrom, G. !$#journal Gene (1988) 69:91-100 !$#title Multiple clustered genes of the haemoglobin VIIB subfamily !1of Chironomus thummi thummi (Diptera). !$#cross-references MUID:89137998; PMID:2852146 !$#accession JT0349 !'##molecule_type DNA !'##residues 1-161 ##label TRE !'##cross-references GB:U07703; GB:M22721; GB:Y00368; NID:g473362; !1PIDN:AAA85487.1; PID:g473368 GENETICS !$#gene GbVIIB-5 CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxygen carrier FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-161 #product hemoglobin VIIB-5 #status predicted #label !8MAT\ !$19-161 #domain globin homology #label GLB\ !$76 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$111 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 161 #molecular-weight 16945 #checksum 4958 SEQUENCE /// ENTRY A30477 #type complete TITLE hemoglobin VIIB-6 precursor - midge (Chironomus thummi thummi) ORGANISM #formal_name Chironomus thummi thummi DATE 12-Nov-1999 #sequence_revision 12-Nov-1999 #text_change 03-Mar-2000 ACCESSIONS A30477 REFERENCE JT0349 !$#authors Trewitt, P.M.; Saffarini, D.A.; Bergtrom, G. !$#journal Gene (1988) 69:91-100 !$#title Multiple clustered genes of the haemoglobin VIIB subfamily !1of Chironomus thummi thummi (Diptera). !$#cross-references MUID:89137998; PMID:2852146 !$#accession A30477 !'##molecule_type DNA !'##residues 1-161 ##label TRE !'##cross-references GB:U07703; GB:M22721; GB:Y00368; NID:g473362; !1PIDN:AAA85486.1; PID:g473367 GENETICS !$#gene GbVIIB-6 CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxygen carrier FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-161 #product hemoglobin VIIB-6 #status predicted #label !8MAT\ !$19-161 #domain globin homology #label GLB\ !$76 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$111 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 161 #molecular-weight 16959 #checksum 4366 SEQUENCE /// ENTRY S04499 #type complete TITLE hemoglobin VIIB-8 precursor - midge (Chironomus thummi piger) ORGANISM #formal_name Chironomus thummi piger DATE 12-Nov-1999 #sequence_revision 12-Nov-1999 #text_change 03-Mar-2000 ACCESSIONS S04499; S21628 REFERENCE S04498 !$#authors Rozynek, P.; Hankeln, T.; Schmidt, E.R. !$#journal Biol. Chem. Hoppe-Seyler (1989) 370:533-542 !$#title Structure of a hemoglobin gene cluster and nucleotide !1sequence of three hemoglobin genes from the midge Chironomus !1thummi piger (Diptera, Insecta). !$#cross-references MUID:89374801; PMID:2775480 !$#accession S04499 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-161 ##label ROZ REFERENCE S21627 !$#authors Hankeln, T.; Rozynek, P.; Schmidt, E.R. !$#submission submitted to the EMBL Data Library, September 1990 !$#description Complete nucleotide sequence of a hemoglobin gene cluster !1from the midge Chironomus thummi piger. !$#accession S21628 !'##molecule_type DNA !'##residues 1-161 ##label HAN !'##cross-references EMBL:X56271; NID:g7069; PIDN:CAA39713.1; PID:g7071 GENETICS !$#gene HbVIIB-8 !$#map_position arm D F2b3 CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxygen carrier FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-161 #product hemoglobin VIIB-8 #status predicted #label !8MAT\ !$19-161 #domain globin homology #label GLB\ !$76 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$111 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 161 #molecular-weight 16999 #checksum 4970 SEQUENCE /// ENTRY S04500 #type complete TITLE hemoglobin VIIB-9 precursor - midge (Chironomus thummi piger) ORGANISM #formal_name Chironomus thummi piger DATE 12-Nov-1999 #sequence_revision 12-Nov-1999 #text_change 03-Mar-2000 ACCESSIONS S04500; S21627 REFERENCE S04498 !$#authors Rozynek, P.; Hankeln, T.; Schmidt, E.R. !$#journal Biol. Chem. Hoppe-Seyler (1989) 370:533-542 !$#title Structure of a hemoglobin gene cluster and nucleotide !1sequence of three hemoglobin genes from the midge Chironomus !1thummi piger (Diptera, Insecta). !$#cross-references MUID:89374801; PMID:2775480 !$#accession S04500 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-161 ##label ROZ REFERENCE S21627 !$#authors Hankeln, T.; Rozynek, P.; Schmidt, E.R. !$#submission submitted to the EMBL Data Library, September 1990 !$#description Complete nucleotide sequence of a hemoglobin gene cluster !1from the midge Chironomus thummi piger. !$#accession S21627 !'##molecule_type DNA !'##residues 1-161 ##label HAN !'##cross-references EMBL:X56271; NID:g7069; PIDN:CAA39712.1; PID:g7070 GENETICS !$#gene HbVIIB-9 !$#map_position II arm D F2b3 CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxygen carrier FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-161 #product hemoglobin VIIB-9 #status predicted #label !8MAT\ !$19-161 #domain globin homology #label GLB\ !$76 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$111 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 161 #molecular-weight 16804 #checksum 1724 SEQUENCE /// ENTRY S21632 #type complete TITLE hemoglobin Z precursor - midge (Chironomus thummi piger) ORGANISM #formal_name Chironomus thummi piger DATE 12-Nov-1999 #sequence_revision 12-Nov-1999 #text_change 03-Mar-2000 ACCESSIONS S21632 REFERENCE S21627 !$#authors Hankeln, T.; Rozynek, P.; Schmidt, E.R. !$#submission submitted to the EMBL Data Library, September 1990 !$#description Complete nucleotide sequence of a hemoglobin gene cluster !1from the midge Chironomus thummi piger. !$#accession S21632 !'##molecule_type DNA !'##residues 1-163 ##label HAN !'##cross-references EMBL:X56271; NID:g7069; PIDN:CAA39717.1; PID:g7075 GENETICS !$#gene HbZ !$#map_position II CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxygen carrier FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-163 #product hemoglobin #status predicted #label MAT\ !$19-162 #domain globin homology #label GLB\ !$76 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$111 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 163 #molecular-weight 17826 #checksum 6252 SEQUENCE /// ENTRY S21633 #type complete TITLE hemoglobin V precursor - midge (Chironomus thummi piger) ORGANISM #formal_name Chironomus thummi piger DATE 12-Nov-1999 #sequence_revision 12-Nov-1999 #text_change 03-Mar-2000 ACCESSIONS S21633 REFERENCE S21627 !$#authors Hankeln, T.; Rozynek, P.; Schmidt, E.R. !$#submission submitted to the EMBL Data Library, September 1990 !$#description Complete nucleotide sequence of a hemoglobin gene cluster !1from the midge Chironomus thummi piger. !$#accession S21633 !'##molecule_type DNA !'##residues 1-163 ##label HAN !'##cross-references EMBL:X56271; NID:g7069; PIDN:CAA39718.1; PID:g7076 GENETICS !$#gene HbV !$#map_position II CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxygen carrier FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-163 #product hemoglobin V #status predicted #label MAT\ !$19-162 #domain globin homology #label GLB\ !$76 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$111 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 163 #molecular-weight 17782 #checksum 3163 SEQUENCE /// ENTRY S21631 #type complete TITLE hemoglobin VIIB-7 precursor - midge (Chironomus thummi piger) ORGANISM #formal_name Chironomus thummi piger DATE 20-Feb-1995 #sequence_revision 20-Feb-1995 #text_change 19-May-2000 ACCESSIONS S21631 REFERENCE S21627 !$#authors Hankeln, T.; Rozynek, P.; Schmidt, E.R. !$#submission submitted to the EMBL Data Library, September 1990 !$#description Complete nucleotide sequence of a hemoglobin gene cluster !1from the midge Chironomus thummi piger. !$#accession S21631 !'##molecule_type DNA !'##residues 1-162 ##label HAN !'##cross-references EMBL:X56271; NID:g7069; PIDN:CAA39716.1; PID:g7074 GENETICS !$#gene HbVIIB-7 !$#map_position II CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxygen carrier FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-162 #product hemoglobin #status predicted #label MAT\ !$19-162 #domain globin homology #label GLB\ !$111 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 162 #molecular-weight 17287 #checksum 8380 SEQUENCE /// ENTRY GGICE7 #type complete TITLE globin CTT-VIIA - midge (Chironomus thummi thummi) (tentative sequence) ORGANISM #formal_name Chironomus thummi thummi DATE 01-Sep-1981 #sequence_revision 01-Sep-1981 #text_change 31-Mar-2000 ACCESSIONS A02548 REFERENCE A02548 !$#authors Kleinschmidt, T.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1980) 361:933-942 !$#title Hemoglobins, XXXII. Analysis of the primary structure of the !1monomeric hemoglobin CTT VIIA (erythrocruorin) of Chironomus !1thummi thummi, Diptera. !$#cross-references MUID:80247756; PMID:7399413 !$#accession A02548 !'##molecule_type protein !'##residues 1-145 ##label KLE COMMENT The functional molecule is a dimer. CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxygen carrier FEATURE !$3-145 #domain globin homology #label GLB\ !$60 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$95 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 145 #molecular-weight 15181 #checksum 3951 SEQUENCE /// ENTRY S14576 #type complete TITLE globin E precursor - midge (Chironomus tentans) ORGANISM #formal_name Chironomus tentans DATE 12-Nov-1999 #sequence_revision 12-Nov-1999 #text_change 03-Mar-2000 ACCESSIONS S14576 REFERENCE S14572 !$#authors Rozynek, P.; Broeker, M.; Hankeln, T.; Schmidt, E.R. !$#submission submitted to the EMBL Data Library, September 1990 !$#description The primary structure of several hemoglobin genes from the !1genome of Chironomus tentans. !$#accession S14576 !'##molecule_type DNA !'##residues 1-161 ##label ROZ !'##cross-references EMBL:X56272; NID:g7090; PIDN:CAA39725.1; PID:g7094 CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxygen carrier FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-161 #product globin C #status predicted #label MAT\ !$19-161 #domain globin homology #label GLB\ !$76 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$111 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 161 #molecular-weight 16948 #checksum 3745 SEQUENCE /// ENTRY S14572 #type complete TITLE globin A precursor - midge (Chironomus tentans) ORGANISM #formal_name Chironomus tentans DATE 12-Nov-1999 #sequence_revision 12-Nov-1999 #text_change 03-Mar-2000 ACCESSIONS S14572 REFERENCE S14572 !$#authors Rozynek, P.; Broeker, M.; Hankeln, T.; Schmidt, E.R. !$#submission submitted to the EMBL Data Library, September 1990 !$#description The primary structure of several hemoglobin genes from the !1genome of Chironomus tentans. !$#accession S14572 !'##molecule_type DNA !'##residues 1-163 ##label ROZ !'##cross-references EMBL:X56272; NID:g7090; PIDN:CAA39721.1; PID:g7091 CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxygen carrier FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-163 #product globin C #status predicted #label MAT\ !$21-163 #domain globin homology #label GLB\ !$78 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$113 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 163 #molecular-weight 17156 #checksum 231 SEQUENCE /// ENTRY GGICEH #type complete TITLE globin CTT-VIII - midge (Chironomus thummi thummi) ORGANISM #formal_name Chironomus thummi thummi DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 03-Mar-2000 ACCESSIONS A02549 REFERENCE A02549 !$#authors Aschauer, H.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1981) 362:409-420 !$#title Haemoglobine, XXXIX. Aminosaeuresequenz eines dimeren !1Haemoglobins (Erythrocruorin) von Chironomus thummi thummi: !1Komponente CTT VIII. !$#cross-references MUID:81213990; PMID:7239440 !$#accession A02549 !'##molecule_type protein !'##residues 1-151 ##label ASC !'##note the functional molecule is a dimer of identical chains CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxygen carrier FEATURE !$5-148 #domain globin homology #label GLB\ !$62 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$97 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 151 #molecular-weight 16898 #checksum 8550 SEQUENCE /// ENTRY GGICEX #type complete TITLE globin CTT-X - midge (Chironomus thummi thummi) ORGANISM #formal_name Chironomus thummi thummi DATE 31-Aug-1979 #sequence_revision 31-Aug-1979 #text_change 03-Mar-2000 ACCESSIONS A02550 REFERENCE A02550 !$#authors Lalthantluanga, R.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1979) 360:99-101 !$#title The primary structure of one of the dimeric hemoglobin !1(erythrocruorin) components, CTT-X, of Chironomus thummi !1thummi (Diptera). !$#cross-references MUID:79108399; PMID:761850 !$#accession A02550 !'##molecule_type protein !'##residues 1-151 ##label LAL !'##note a second component differs from the above in having 48-Thr CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxygen carrier FEATURE !$7-150 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$99 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 151 #molecular-weight 17068 #checksum 8169 SEQUENCE /// ENTRY GGICE3 #type complete TITLE globin CTT-III - midge (Chironomus thummi thummi) ALTERNATE_NAMES erythrocruorin III ORGANISM #formal_name Chironomus thummi thummi DATE 30-Apr-1980 #sequence_revision 30-Apr-1980 #text_change 03-Mar-2000 ACCESSIONS A91687; A02551 REFERENCE A91687 !$#authors Buse, G.; Steffens, G.J.; Braunitzer, G.; Steer, W. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1979) 360:89-97 !$#title Haemoglobin (Erythrocruorin) CTT III aus Chironomus thummi !1thummi (Diptera). !$#cross-references MUID:79108397; PMID:761849 !$#accession A91687 !'##molecule_type protein !'##residues 1-136 ##label BUS !'##note 57-Thr and 57-Ile were found in a ratio of 2:1 REFERENCE A92947 !$#authors Huber, R.; Epp, O.; Formanek, H. !$#journal J. Mol. Biol. (1969) 42:591-594 !$#title The environment of the haem group in erythrocruorin !1(Chironomus thummi). !$#cross-references MUID:69266512; PMID:5804161 !$#contents annotation; heme binding REFERENCE A91649 !$#authors Glossmann, H.; Horst, J.; Plagens, U.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1970) 351:342-348 !$#title Isoelektrisches Fokussieren von Haemoglobinen !1(Erythrocrurinen) der Insekten (Chironomus thummi thummi, !1Diptera). !$#cross-references MUID:70206790; PMID:5420706 !$#contents annotation; heme binding REFERENCE A91184 !$#authors Huber, R.; Epp, O.; Steigemann, W.; Formanek, H. !$#journal Eur. J. Biochem. (1971) 19:42-50 !$#title The atomic structure of erythrocruorin in the light of the !1chemical sequence and its comparison with myoglobin. !$#cross-references MUID:71157305; PMID:5102553 !$#contents annotation; X-ray crystallography, 2.5 angstroms !$#note there are some discrepancies between the interpretation of !1the electron density map and the sequence shown here REFERENCE A44577 !$#authors Weber, E.; Steigemann, W.; Jones, T.A.; Huber, R. !$#journal J. Mol. Biol. (1978) 120:327-336 !$#title The structure of oxy-erythrocruorin at 1.4 angstroms !1resolution. !$#cross-references MUID:78153774; PMID:642012 !$#contents annotation; X-ray crystallography, 1.4 angstroms REFERENCE A48224 !$#authors Steigemann, W.; Weber, E. !$#journal J. Mol. Biol. (1979) 127:309-338 !$#title Structure of erythrocruorin in different ligand states !1refined at 1.4 angstroms resolution. !$#cross-references MUID:79153989; PMID:430568 !$#contents annotation; X-ray crystallography, 1.4 angstroms; sequence !1revision COMMENT The heme group is rotated by an angle of approximately 180 !1degrees as compared with myoglobin. COMMENT The His-58, expected to bind oxygen as the proximal axial !1ligand, instead forms a hydrogen bond with a heme propionic !1group. COMMENT The functional molecule is a monomer. CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxygen carrier FEATURE !$1-136 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status absent\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status experimental SUMMARY #length 136 #molecular-weight 14784 #checksum 7292 SEQUENCE /// ENTRY GGIC3 #type complete TITLE hemoglobin III - midge (Chironomus thummi piger) ALTERNATE_NAMES erythrocruorin III ORGANISM #formal_name Chironomus thummi piger DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 03-Mar-2000 ACCESSIONS S05422 REFERENCE S05422 !$#authors Kleinschmidt, T.; Keyl, H.G.; Braunitzer, G. !$#journal Biol. Chem. Hoppe-Seyler (1989) 370:839-845 !$#title Comparison of insect hemoglobins (erythrocruorins) from !1Chironomus thummi thummi and Chironomus thummi piger !1(Diptera). The primary structure of the monomeric hemoglobin !1CTP III. !$#cross-references MUID:90074180; PMID:2590466 !$#accession S05422 !'##molecule_type protein !'##residues 1-136 ##label KLE !'##note 57-Ile, 105-Ile, and 134-Ala were also found CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; hemolymph; heterotetramer; iron; !1metalloprotein; oxygen carrier FEATURE !$1-136 #domain globin homology #label GLB\ !$58 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$87 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 136 #molecular-weight 14784 #checksum 7292 SEQUENCE /// ENTRY GGICE4 #type complete TITLE globin CTT-IV precursor - midge (Chironomus thummi thummi) ORGANISM #formal_name Chironomus thummi thummi DATE 18-Aug-1982 #sequence_revision 30-Jun-1990 #text_change 03-Mar-2000 ACCESSIONS A21808; A02552 REFERENCE A21808 !$#authors Antoine, M.; Niessing, J. !$#journal Nature (1984) 310:795-798 !$#title Intron-less globin genes in the insect Chironomus thummi !1thummi. !$#accession A21808 !'##molecule_type DNA !'##residues 1-151 ##label ANT REFERENCE A02552 !$#authors Pfletschinger, J.; Plagens, H.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1981) 362:539-547 !$#title Hemoglobins, XL: sequence analysis of the monomeric !1hemoglobin CTT IV (erythrocruorin) of Chironomus thummi !1thummi, Diptera. !$#cross-references MUID:81238144; PMID:7250903 !$#accession A02552 !'##molecule_type protein !'##residues 16-151 ##label PFL COMMENT The functional molecule is a monomer. CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxygen carrier FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-151 #product globin CTT-IV #status experimental #label !8MAT\ !$16-151 #domain globin homology #label GLB\ !$73 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$102 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 151 #molecular-weight 15935 #checksum 433 SEQUENCE /// ENTRY GGICEA #type complete TITLE globin CTT-IIIa - midge (Chironomus thummi thummi) ORGANISM #formal_name Chironomus thummi thummi DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 03-Mar-2000 ACCESSIONS A02553 REFERENCE A02553 !$#authors Steer, W.; Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1981) 362:73-80 !$#title Hemoglobins, XXXVII. The primary structure of a monomeric !1insect hemoglobin (erythrocruorin), component CTT IIIa of !1Chironomus thummi thummi. An anomalous heme complex: E7 Gln, !1E11 Ile. !$#cross-references MUID:81166259; PMID:7216163 !$#accession A02553 !'##molecule_type protein !'##residues 1-151 ##label STE !'##note the functional molecule is a monomer COMMENT The midge globin CTT-IIIa is exceptional in appearing to !1have glutamine rather than histidine as the distal axial !1ligand binding oxygen. CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxygen carrier FEATURE !$9-147 #domain globin homology #label GLB\ !$65 #binding_site oxygen (Gln) (distal axial ligand) !8#status predicted\ !$98 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 151 #molecular-weight 16155 #checksum 8076 SEQUENCE /// ENTRY GPVF #type complete TITLE leghemoglobin I - fava bean ORGANISM #formal_name Vicia faba #common_name fava bean DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 03-Mar-2000 ACCESSIONS A02554 REFERENCE A02554 !$#authors Richardson, M.; Dilworth, M.J.; Scawen, M.D. !$#journal FEBS Lett. (1975) 51:33-37 !$#title The amino acid sequence of leghaemoglobin I from root !1nodules of broad bean (Vicia faba L.). !$#cross-references MUID:75131397; PMID:1123063 !$#accession A02554 !'##molecule_type protein !'##residues 1-143 ##label RIC !'##note 4-Asp, 5-Gln, 22-Gly, 23-Gly, 34-Lys, 41-Gly, 59-Gln, 64-Gln, !171-Glu, 74-Ile, 77-Gln, 126-Glu, 128-Ile, and 134-Glu were !1also found in this pooled preparation CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxygen carrier FEATURE !$2-143 #domain globin homology #label GLB\ !$61 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 143 #molecular-weight 15399 #checksum 3799 SEQUENCE /// ENTRY GPPMI #type complete TITLE leghemoglobin I - garden pea ORGANISM #formal_name Pisum sativum #common_name garden pea DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 03-Mar-2000 ACCESSIONS A02555 REFERENCE A02555 !$#authors Lehtovaara, P.; Lappalainen, A.; Ellfolk, N. !$#journal Biochim. Biophys. Acta (1980) 623:98-106 !$#title The amino acid sequence of pea (Pisum sativum) !1leghemoglobin. !$#cross-references MUID:80198537; PMID:7378476 !$#accession A02555 !'##molecule_type protein !'##residues 1-147 ##label LEH !'##experimental_source cv. Torstai !'##note 21-Gln, 23-Asn, 24-Ala, 25-Thr/Val, 31-Ile, 93-Ala, and 94-Gly !1were also found CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxygen carrier FEATURE !$2-145 #domain globin homology #label GLB\ !$60 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 147 #molecular-weight 15835 #checksum 2970 SEQUENCE /// ENTRY GPFJG2 #type complete TITLE leghemoglobin glb2 - Sesbania rostrata ALTERNATE_NAMES leghemoglobin II ORGANISM #formal_name Sesbania rostrata DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 17-Mar-2000 ACCESSIONS S08322; S21460; S02206 REFERENCE S08322 !$#authors Metz, B.A.; Welters, P.; Hoffmann, H.J.; Jensen, E.O.; !1Schell, J.; de Bruijn, F.J. !$#journal Mol. Gen. Genet. (1988) 214:181-191 !$#title Primary structure and promoter analysis of leghemoglobin !1genes of the stem-nodulated tropical legume Sesbania !1rostrata: conserved coding sequences, cis-elements and !1trans-acting factors. !$#cross-references MUID:89181515; PMID:3237206 !$#accession S08322 !'##molecule_type DNA !'##residues 1-148 ##label MET !'##cross-references EMBL:X13505; NID:g21381; PIDN:CAA31859.1; !1PID:g21382 REFERENCE S21460 !$#authors Welters, P.; Metz, B.; Schell, J.; de Bruijn, F.J. !$#submission submitted to the EMBL Data Library, December 1988 !$#description Nucleotide sequence of te sesbania rostrata leghemoglobin !1(Srglb3) gene. !$#accession S21460 !'##molecule_type DNA !'##residues 1-148 ##label WEL !'##cross-references EMBL:X13815; NID:g21374; PIDN:CAA32044.1; !1PID:g21375 REFERENCE S02206 !$#authors Kortt, A.A.; Strike, P.M.; Bogusz, D.; Appleby, C.A. !$#journal Biochem. Int. (1987) 15:509-516 !$#title The amino acid sequence of leghemoglobin II from Sesbania !1rostrata stem nodules. !$#accession S02206 !'##molecule_type protein !'##residues 2-4,'D',6-19,'K',21-24,'H',26-36,'E',38-42,'L',44-71,'H', !173,'A',75-100,'T',102-129,'I',131-139,'A',141-148 ##label !1KOR !'##note the sequence from Fig. 3 is inconsistent with that from Fig. 2 !1in having 76-Gly GENETICS !$#gene glb2 !$#introns 32/2; 70/3; 106/3 CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxygen carrier FEATURE !$2-148 #product leghemoglobin glb2 #status experimental !8#label MAT\ !$3-148 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$95 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 148 #molecular-weight 15800 #checksum 5446 SEQUENCE /// ENTRY GPFBA #type complete TITLE leghemoglobin a - kidney bean ORGANISM #formal_name Phaseolus vulgaris #common_name kidney bean DATE 08-Oct-1981 #sequence_revision 08-Oct-1981 #text_change 03-Mar-2000 ACCESSIONS A02556 REFERENCE A02556 !$#authors Lehtovaara, P.; Ellfolk, N. !$#journal Eur. J. Biochem. (1975) 54:577-584 !$#title The amino-acid sequence of leghemoglobin component a from !1Phaseolus vulgaris (kidney bean). !$#cross-references MUID:76022373; PMID:809270 !$#accession A02556 !'##molecule_type protein !'##residues 1-145 ##label LEH !'##experimental_source cv. Kaiser Wilhelm CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxygen carrier FEATURE !$3-145 #domain globin homology #label GLB\ !$61 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 145 #molecular-weight 15486 #checksum 7213 SEQUENCE /// ENTRY GPSYC1 #type complete TITLE leghemoglobin c1 - soybean ORGANISM #formal_name Glycine max #common_name soybean DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 16-Jun-2000 ACCESSIONS A02557 REFERENCE A93447 !$#authors Hyldig-Nielsen, J.J.; Jensen, E.O.; Paludan, K.; Wiborg, O.; !1Garrett, R.; Jorgensen, P.; Marcker, K.A. !$#journal Nucleic Acids Res. (1982) 10:689-701 !$#title The primary structures of two leghemoglobin genes from !1soybean. !$#cross-references MUID:82150225; PMID:6278428 !$#accession A02557 !'##molecule_type DNA !'##residues 1-143 ##label HYL !'##cross-references GB:V00452; GB:J01300; NID:g18593; PIDN:CAA23730.1; !1PID:g1628385 !'##note five leghemoglobin genes have been isolated; this sequence is !1tentatively identified as c1 !'##note initiator Met not shown GENETICS !$#introns 32/2; 68/3; 103/3 CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxygen carrier FEATURE !$3-143 #domain globin homology #label GLB\ !$61 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 143 #molecular-weight 15257 #checksum 2568 SEQUENCE /// ENTRY GPSYC2 #type complete TITLE leghemoglobin c2 - soybean ORGANISM #formal_name Glycine max #common_name soybean DATE 31-May-1980 #sequence_revision 27-Nov-1985 #text_change 03-Mar-2000 ACCESSIONS A90008; A91441; A02558 REFERENCE A90008 !$#authors Sievers, G.; Huhtala, M.L.; Ellfolk, N. !$#journal Acta Chem. Scand. B Org. Chem. Biochem. (1978) 32:380-386 !$#title The primary structure of soybean (Glycine max) leghemoglobin !1c. !$#accession A90008 !'##molecule_type protein !'##residues 1-143 ##label SIE REFERENCE A94598 !$#authors Ellfolk, N. !$#submission submitted to the Atlas, November 1982 !$#contents annotation !$#note 8-Glu, 20-Thr, 39-Val, 79-Asn, and 97-Ile were also found REFERENCE A91441 !$#authors Hurrell, J.G.R.; Leach, S.J. !$#journal FEBS Lett. (1977) 80:23-26 !$#title The amino acid sequence of soybean leghaemoglobin c-2. !$#cross-references MUID:77246779; PMID:561001 !$#accession A91441 !'##molecule_type protein !'##residues 1-30,'T',32-37,'F',39,'V',41-51,'N',53-66,'G',68-78,81-87, !1'S',89-143 ##label HUR CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxygen carrier FEATURE !$3-143 #domain globin homology #label GLB\ !$61 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 143 #molecular-weight 15264 #checksum 677 SEQUENCE /// ENTRY GPSYC3 #type complete TITLE leghemoglobin c3 - soybean ORGANISM #formal_name Glycine max #common_name soybean DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 03-Mar-2000 ACCESSIONS A93426; B93921; A32711; A02559 REFERENCE A93426 !$#authors Wiborg, O.; Hyldig-Nielsen, J.J.; Jensen, E.O.; Paludan, K.; !1Marcker, K.A. !$#journal Nucleic Acids Res. (1982) 10:3487-3494 !$#title The nucleotide sequences of two leghemoglobin genes from !1soybean. !$#cross-references MUID:82247221; PMID:6285303 !$#accession A93426 !'##molecule_type DNA !'##residues 1-144 ##label WIB REFERENCE A93921 !$#authors Brisson, N.; Verma, D.P.S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:4055-4059 !$#title Soybean leghemoglobin gene family: normal, pseudo, and !1truncated genes. !$#cross-references MUID:82275064; PMID:6287463 !$#accession B93921 !'##molecule_type DNA !'##residues 1-144 ##label BRI !'##cross-references GB:V00454; GB:J01303; NID:g18599; PIDN:CAA23732.1; !1PID:g313504 REFERENCE A32711 !$#authors Stougaard, J.; Petersen, T.E.; Marcker, K.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:5754-5757 !$#title Expression of a complete soybean leghemoglobin gene in root !1nodules of transgenic Lotus corniculatus. !$#accession A32711 !'##molecule_type protein !'##residues 1-23 ##label STO COMMENT The initiator Met is not shown. GENETICS !$#introns 32/2; 68/3; 103/3 CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxygen carrier FEATURE !$3-144 #domain globin homology #label GLB\ !$61 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 144 #molecular-weight 15450 #checksum 5002 SEQUENCE /// ENTRY GPSYS #type complete TITLE leghemoglobin a - soybean ORGANISM #formal_name Glycine max #common_name soybean DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 11-May-2000 ACCESSIONS A93447; A90006; A90007; A02560 REFERENCE A93447 !$#authors Hyldig-Nielsen, J.J.; Jensen, E.O.; Paludan, K.; Wiborg, O.; !1Garrett, R.; Jorgensen, P.; Marcker, K.A. !$#journal Nucleic Acids Res. (1982) 10:689-701 !$#title The primary structures of two leghemoglobin genes from !1soybean. !$#cross-references MUID:82150225; PMID:6278428 !$#accession A93447 !'##molecule_type DNA !'##residues 1-143 ##label HYL !'##cross-references GB:V00453; GB:J01299; NID:g18595; PIDN:CAA23731.1; !1PID:g313503 !'##note initiator Met not shown REFERENCE A90006 !$#authors Ellfolk, N.; Sievers, G. !$#journal Acta Chem. Scand. (1973) 27:3986-3992 !$#title The primary structure of soybean leghemoglobin. IV. !1Fractionation and sequence of thermolytic peptides of the !1apoprotein of the slow component (Lba). !$#cross-references MUID:74121196; PMID:4798828 !$#accession A90006 !'##molecule_type protein !'##residues 1-49,'PT',52,'GV',55-98,'N',100,'E',102-104,106-141,'AK' !1##label EL1 !'##note this is the final paper in a series REFERENCE A90007 !$#authors Ellfolk, N.; Sievers, G. !$#journal Acta Chem. Scand. B (1974) 28:1245-1246 !$#title Correction of the amino acid sequence of soybean !1leghemoglobin a. !$#cross-references MUID:75180648; PMID:4477921 !$#accession A90007 !'##molecule_type protein !'##residues 42-57 ##label EL2 GENETICS !$#introns 32/2; 68/3; 103/3 CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxygen carrier FEATURE !$3-143 #domain globin homology #label GLB\ !$61 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$92 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 143 #molecular-weight 15242 #checksum 2384 SEQUENCE /// ENTRY GPYL #type complete TITLE leghemoglobin I - yellow lupine ORGANISM #formal_name Lupinus luteus #common_name yellow lupine DATE 24-Apr-1984 #sequence_revision 26-May-1994 #text_change 03-Mar-2000 ACCESSIONS A26808; S41327; A02561; JN0241 REFERENCE A26808 !$#authors Konieczny, A. !$#journal Nucleic Acids Res. (1987) 15:6742 !$#title Nucleotide sequence of lupin leghemoglobin I cDNA. !$#cross-references MUID:87316940; PMID:3628011 !$#accession A26808 !'##molecule_type mRNA !'##residues 1-154 ##label KON !'##cross-references EMBL:Y00401 REFERENCE S41327 !$#authors Strozycki, P.S.P. !$#submission submitted to the EMBL Data Library, January 1994 !$#accession S41327 !'##status preliminary !'##molecule_type mRNA !'##residues 1-154 ##label STR !'##cross-references EMBL:X77043; NID:g441458; PIDN:CAA54332.1; !1PID:g441459 REFERENCE A90723 !$#authors Egorov, T.A.; Feigina, M.Y.; Kazakov, V.K.; Shakhparonov, !1M.I.; Mimaleva, S.I.; Ovchinnikov, Y.A. !$#journal Bioorg. Khim. (1976) 2:125-128 !$#title The complete amino acid sequence of the leghemoglobin I from !1yellow lupin root nodules. !$#accession A02561 !'##molecule_type protein !'##residues 2-79,'E',81-154 ##label EGO REFERENCE JN0241 !$#authors Egorov, T.A.; Kazakov, V.K.; Shakhparonov, M.I.; Feigina, !1M.Y. !$#journal Bioorg. Khim. (1980) 6:666-683 !$#title Amino acid sequence of leghemoglobins I and II from yellow !1lupine. !$#accession JN0241 !'##molecule_type protein !'##residues 2-79,'E',81-154 ##label EG2 !'##experimental_source root nodules !'##note article in Russian with English abstract CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxygen carrier FEATURE !$2-154 #product leghemoglobin I #status experimental #label !8MAT\ !$4-151 #domain globin homology #label GLB\ !$64 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$98 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 154 #molecular-weight 16753 #checksum 1300 SEQUENCE /// ENTRY GPYL2 #type complete TITLE leghemoglobin II - yellow lupine ORGANISM #formal_name Lupinus luteus #common_name yellow lupine DATE 31-May-1979 #sequence_revision 24-Oct-1997 #text_change 03-Mar-2000 ACCESSIONS S41328; A54493; A02562; JN0242 REFERENCE S41327 !$#authors Strozycki, P.S.P. !$#submission submitted to the EMBL Data Library, January 1994 !$#accession S41328 !'##molecule_type mRNA !'##residues 3-153 ##label STR !'##cross-references EMBL:X77042; NID:g441460; PIDN:CAA54331.1; !1PID:g441461 REFERENCE A54493 !$#authors Konieczny, A.; Jensen, E.O.; Marcker, K.A.; Legocki, A.B. !$#journal Mol. Biol. Rep. (1987) 12:61-66 !$#title Molecular cloning of lupin leghemoglobin cDNA. !$#cross-references MUID:87315070; PMID:2442601 !$#accession A54493 !'##molecule_type mRNA !'##residues 62-153 ##label KON !'##cross-references GB:M17893 REFERENCE A02562 !$#authors Egorov, T.A.; Kazakov, V.K.; Shakhparonov, M.I.; Feigina, !1M.Y.; Kostetsky, P.V. !$#journal Bioorg. Khim. (1978) 4:476-480 !$#accession A02562 !'##molecule_type protein !'##residues 1-78,'E',80-85,'S',87-149,'D',151-153 ##label EGO REFERENCE JN0241 !$#authors Egorov, T.A.; Kazakov, V.K.; Shakhparonov, M.I.; Feigina, !1M.Y. !$#journal Bioorg. Khim. (1980) 6:666-683 !$#title Amino acid sequence of leghemoglobins I and II from yellow !1lupine. !$#accession JN0242 !'##molecule_type protein !'##residues 1-78,'E',80-85,'S',87-149,'D',151-153 ##label EG2 !'##experimental_source root nodules !'##note article in Russian with English abstract REFERENCE A93172 !$#authors Vainshtein, B.K.; Harutyunyan, E.H.; Kuranova, I.P.; !1Borisov, V.V.; Sosfenov, N.I.; Pavlovsky, A.G.; Grebenko, !1A.I.; Konareva, N.V. !$#journal Nature (1975) 254:163-164 !$#title Structure of leghaemoglobin from lupin root nodules at 5 !1angstroms resolution. !$#cross-references MUID:75118996; PMID:1118009 !$#contents annotation; X-ray crystallography, 5.0 angstroms CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxygen carrier FEATURE !$3-150 #domain globin homology #label GLB\ !$63 #binding_site oxygen (His) (distal axial ligand) !8#status experimental\ !$97 #binding_site heme iron (His) (proximal axial ligand) !8#status experimental SUMMARY #length 153 #molecular-weight 16652 #checksum 8272 SEQUENCE /// ENTRY GPDRNL #type complete TITLE hemoglobin I - Parasponia andersonii ORGANISM #formal_name Parasponia andersonii DATE 17-Mar-1987 #sequence_revision 19-May-2000 #text_change 19-May-2000 ACCESSIONS S05541; A25054; A02563 REFERENCE S01019 !$#authors Kortt, A.A.; Trinick, M.J.; Appleby, C.A. !$#journal Eur. J. Biochem. (1988) 175:141-149 !$#title Amino acid sequences of hemoglobins I and II from root !1nodules of the non-leguminous Parasponia rigida-rhizobium !1symbiosis, and a correction of the sequence of hemoglobin I !1from Parasponia andersonii. !$#cross-references MUID:88296462; PMID:3402445 !$#accession S05541 !'##molecule_type protein !'##residues 2-162 ##label KOR1 !'##note 30-Asp was also found REFERENCE A25054 !$#authors Landsmann, J.; Dennis, E.S.; Higgins, T.J.V.; Appleby, C.A.; !1Kortt, A.A.; Peacock, W.J. !$#journal Nature (1986) 324:166-168 !$#title Common evolutionary origin of legume and non-legume plant !1haemoglobins. !$#accession A25054 !'##molecule_type DNA !'##residues 2-162 ##label LAN !'##cross-references GB:U27194; GB:M36509; NID:g862962; PIDN:AAB86653.1; !1PID:g862963 !'##note translation of initiator Met is not shown REFERENCE A02563 !$#authors Kortt, A.A.; Burns, J.E.; Trinick, M.J.; Appleby, C.A. !$#journal FEBS Lett. (1985) 180:55-60 !$#title The amino acid sequence of hemoglobin I from Parasponia !1andersonii, a nonleguminous plant. !$#accession A02563 !'##molecule_type protein !'##residues 6-36,38-73,75-78,'T',80-162 ##label KOR2 GENETICS !$#introns 39/2; 77/3; 116/3 CLASSIFICATION #superfamily globin; globin homology KEYWORDS acetylated amino end; chromoprotein; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$10-158 #domain globin homology #label GLB\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental\ !$70 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$105 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 162 #molecular-weight 18178 #checksum 9899 SEQUENCE /// ENTRY GPUGNI #type complete TITLE hemoglobin I - swamp oak ORGANISM #formal_name Casuarina glauca #common_name swamp oak DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 03-Mar-2000 ACCESSIONS S00560 REFERENCE S00560 !$#authors Kortt, A.A.; Inglis, A.S.; Fleming, A.I.; Appleby, C.A. !$#journal FEBS Lett. (1988) 231:341-346 !$#title Amino acid sequence of hemoglobin I from root nodules of the !1non-leguminous Casuarina glauca-Frankia symbiosis. !$#accession S00560 !'##molecule_type protein !'##residues 1-151 ##label KOR COMMENT This protein was isolated from the root nodules of Casuarina !1glauca after inoculation with an actinomycete, Frankia sp. CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxygen carrier FEATURE !$2-150 #domain globin homology #label GLB\ !$62 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$97 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 151 #molecular-weight 17112 #checksum 2020 SEQUENCE /// ENTRY GGZLB #type complete TITLE bacterial hemoglobin - Vitreoscilla sp. ALTERNATE_NAMES soluble cytochrome o ORGANISM #formal_name Vitreoscilla sp. #note Vitreoscilla is a genus of filamentous, obligate aerobic bacteria DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 03-Mar-2000 ACCESSIONS S08307; A02564; S06831 REFERENCE S08307 !$#authors Khosla, C.; Bailey, J.E. !$#journal Mol. Gen. Genet. (1988) 214:158-161 !$#title The Vitreoscilla hemoglobin gene: molecular cloning, !1nucleotide sequence and genetic expression in Escherichia !1coli. !$#cross-references MUID:89143453; PMID:3067078 !$#accession S08307 !'##molecule_type DNA !'##residues 1-146 ##label KHO !'##cross-references EMBL:X13516; NID:g48458; PIDN:CAA31866.1; !1PID:g48459 REFERENCE A02564 !$#authors Wakabayashi, S.; Matsubara, H.; Webster, D.A. !$#journal Nature (1986) 322:481-483 !$#title Primary sequence of a dimeric bacterial haemoglobin from !1Vitreoscilla. !$#cross-references MUID:86285002; PMID:3736670 !$#accession A02564 !'##molecule_type protein !'##residues 1-146 ##label WAK REFERENCE S06831 !$#authors Khosla, C.; Bailey, J.E. !$#journal J. Mol. Biol. (1989) 210:79-89 !$#title Evidence for partial export of Vitreoscilla hemoglobin into !1the periplasmic space in Escherichia coli. Implications for !1protein function. !$#cross-references MUID:90064558; PMID:2685332 !$#accession S06831 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-16 ##label KH2 FUNCTION !$#description this protein functions as a terminal oxidase CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; dimer; heme; iron; metalloprotein; oxygen !1carrier FEATURE !$2-138 #domain globin homology #label GLB\ !$53 #binding_site oxygen (Gln) (distal axial ligand) !8#status predicted\ !$85 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 146 #molecular-weight 15774 #checksum 6674 SEQUENCE /// ENTRY F70319 #type complete TITLE bacterial hemoglobin - Aquifex aeolicus ALTERNATE_NAMES flavohemoprotein [misnomer] ORGANISM #formal_name Aquifex aeolicus DATE 12-Nov-1999 #sequence_revision 12-Nov-1999 #text_change 03-Mar-2000 ACCESSIONS F70319 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession F70319 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-139 ##label AQF !'##cross-references GB:AE000678; NID:g2982921; PIDN:AAC06544.1; !1PID:g2982927; GB:AE000657 !'##experimental_source strain VF5 GENETICS !$#gene fhp CLASSIFICATION #superfamily globin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein; oxygen carrier FEATURE !$2-133 #domain globin homology #label GLB\ !$50 #binding_site oxygen (Gln) (distal axial ligand) !8#status predicted\ !$82 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 139 #molecular-weight 15964 #checksum 4660 SEQUENCE /// ENTRY A47183 #type complete TITLE hemoglobin precursor [validated] - pig roundworm ALTERNATE_NAMES high affinity, extracellular, octomeric hemoglobin ORGANISM #formal_name Ascaris suum #common_name pig roundworm DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 15-Sep-2000 ACCESSIONS A47183; A45289; A50001 REFERENCE A47183 !$#authors Sherman, D.R.; Kloek, A.P.; Krishnan, B.R.; Guinn, B.; !1Goldberg, D.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:11696-11700 !$#title Ascaris hemoglobin gene: plant-like structure reflects the !1ancestral globin gene. !$#cross-references MUID:93101593; PMID:1465385 !$#accession A47183 !'##molecule_type mRNA !'##residues 1-338 ##label SHE !'##cross-references GB:L03351; NID:g159662; PIDN:AAA29374.1; !1PID:g159663 !'##note sequence extracted from NCBI backbone (NCBIN:120541, !1NCBIP:120542) REFERENCE A52916 !$#authors Yang, J.; Mathews, F.S.; Kloek, A.P.; Goldberg, D.E. !$#submission submitted to the Brookhaven Protein Data Bank, January 1995 !$#cross-references PDB:1ASH !$#contents annotation; X-ray crystallography, 2.15 angstroms, residues !118-63,'S',65-164 !$#note recombinant form expressed in Escherichia coli, plasmid !1pet-8c REFERENCE A47403 !$#authors Kloek, A.P.; Yang, J.; Mathews, F.S.; Goldberg, D.E. !$#journal J. Biol. Chem. (1993) 268:17669-17671 !$#title Expression, characterization, and crystallization of !1oxygen-avid Ascaris hemoglobin domains. !$#cross-references MUID:93352567; PMID:8349648 !$#contents annotation; physical properties REFERENCE A45289 !$#authors De Baere, I.; Liu, L.; Moens, L.; Van Beeumen, J.; Gielens, !1C.; Richelle, J.; Trotman, C.; Finch, J.; Gerstein, M.; !1Perutz, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:4638-4642 !$#title Polar zipper sequence in the high-affinity hemoglobin of !1Ascaris suum: amino acid sequence and structural !1interpretation. !$#cross-references MUID:92262495; PMID:1584800 !$#accession A45289 !'##molecule_type protein !'##residues 19-116,'L',118-168,173-265,'D',267-333 ##label DEA COMMENT This extracellular hemoglobin is an octamer of identical !1chains. It has an extraordinarily high affinity for oxygen. COMPLEX homooctamer CLASSIFICATION #superfamily nematode hemoglobin; globin homology KEYWORDS chromoprotein; duplication; extracellular protein; !1glycoprotein; heme; homooctamer; iron; metalloprotein; !1oxygen carrier FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$22-167 #domain globin homology #label GLB1\ !$171-316 #domain globin homology #label GLB2\ !$317-336 #region 4-residue repeats (E-H-K-E)\ !$19,216 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$82 #binding_site oxygen (Gln) (distal axial ligand) !8#status predicted\ !$114 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted\ !$231 #binding_site oxygen (Gln) (distal axial ligand) !8#status predicted\ !$263 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 338 #molecular-weight 40648 #checksum 6980 SEQUENCE /// ENTRY A41099 #type complete TITLE hemoglobin precursor - codworm ORGANISM #formal_name Pseudoterranova decipiens #common_name codworm DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S24615; A41099 REFERENCE S24615 !$#authors Dixon, B. !$#submission submitted to the EMBL Data Library, February 1992 !$#accession S24615 !'##molecule_type DNA !'##residues 1-333 ##label DIX !'##cross-references EMBL:Z11681; NID:g9815; PIDN:CAA77743.1; PID:g9816 REFERENCE A41099 !$#authors Dixon, B.; Walker, B.; Kimmins, W.; Pohajdak, B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:5655-5659 !$#title Isolation and sequencing of a cDNA for an unusual hemoglobin !1from the parasitic nematode Pseudoterranova decipiens. !$#cross-references MUID:91288523; PMID:2062843 !$#accession A41099 !'##molecule_type mRNA !'##residues 1-8,'I',10-333 ##label DI2 !'##cross-references GB:M63298; NID:g160798; PIDN:AAA29797.1; !1PID:g160799 GENETICS !$#introns 21/1; 50/2; 83/1; 127/3; 170/1; 199/2 CLASSIFICATION #superfamily nematode hemoglobin; globin homology KEYWORDS duplication; extracellular protein; glycoprotein; heme FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-333 #product hemoglobin #status predicted #label MAT\ !$22-167 #domain globin homology #label GLB1\ !$171-318 #domain globin homology #label GLB2 SUMMARY #length 333 #molecular-weight 39440 #checksum 3244 SEQUENCE /// ENTRY A39601 #type complete TITLE hemoglobin 35K chain - ark shell (Barbatia reeveana) ORGANISM #formal_name Barbatia reeveana DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Mar-2000 ACCESSIONS A39601 REFERENCE A39601 !$#authors Naito, Y.; Riggs, C.K.; Vandergon, T.L.; Riggs, A.F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:6672-6676 !$#title Origin of a "bridge" intron in the gene for a two-domain !1globin. !$#cross-references MUID:91319746; PMID:1862092 !$#accession A39601 !'##molecule_type DNA !'##residues 1-309 ##label NAI !'##cross-references GB:M73327; GB:M73328 COMMENT This species also contains a hemoglobin of 16- to 17-kDa !1chains. CLASSIFICATION #superfamily Barbatia 35K hemoglobin; globin homology KEYWORDS chromoprotein; heme; iron; metalloprotein FEATURE !$11-155 #domain globin homology #label GLB1\ !$165-309 #domain globin homology #label GLB2\ !$71 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$103 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted\ !$225 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$257 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 309 #molecular-weight 35324 #checksum 7729 SEQUENCE /// ENTRY I38963 #type complete TITLE DAZ protein - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS I38963 REFERENCE I38963 !$#authors Reijo, R.; Lee, T. !$#journal Nature Genet. (1995) 10:383-393 !$#title Diverse spermatogenic defects in humans caused by Y !1chromosome deletions encompassing a novel RNA-binding !1protein gene. !$#cross-references MUID:95400318; PMID:7670487 !$#accession I38963 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-366 ##label RES !'##cross-references EMBL:U21663; NID:g1045307; PIDN:AAB02393.1; !1PID:g1045308 GENETICS !$#gene GDB:DAZ !'##cross-references GDB:635890; OMIM:400003 !$#map_position Yq11-Yq11 CLASSIFICATION #superfamily human DAZ protein; ribonucleoprotein repeat !1homology FEATURE !$41-106 #domain ribonucleoprotein repeat homology #label RRM1 SUMMARY #length 366 #molecular-weight 41283 #checksum 4069 SEQUENCE /// ENTRY S68988 #type complete TITLE boule protein - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S68988 REFERENCE S68988 !$#authors Eberhart, C.G.; Maines, J.Z.; Wasserman, S.A. !$#journal Nature (1996) 381:783-785 !$#title Meiotic cell cycle requirement for a fly homologue of human !1Deleted in Azoospermia. !$#cross-references MUID:96267004; PMID:8657280 !$#accession S68988 !'##status preliminary; nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-228 ##label EBE !'##cross-references EMBL:U51858; NID:g1395210; PIDN:AAC47133.1; !1PID:g1395211 CLASSIFICATION #superfamily fruit fly boule protein; ribonucleoprotein !1repeat homology FEATURE !$34-101 #domain ribonucleoprotein repeat homology #label RRM1 SUMMARY #length 228 #molecular-weight 24682 #checksum 8562 SEQUENCE /// ENTRY S75129 #type complete TITLE cyanoglobin - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein slr2097 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S75129 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75129 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-124 ##label KAN !'##cross-references EMBL:D90910; GB:AB001339; NID:g1652956; !1PIDN:BAA17991.1; PID:g1653074 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene glbN CLASSIFICATION #superfamily Tetrahymena globin KEYWORDS chromoprotein; heme; iron; metalloprotein; oxygen carrier FEATURE !$70 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 124 #molecular-weight 13868 #checksum 7433 SEQUENCE /// ENTRY A36270 #type complete TITLE hemoglobin - Tetrahymena pyriformis ORGANISM #formal_name Tetrahymena pyriformis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S32555; A36270 REFERENCE S32555 !$#authors Takagi, T.; Iwaasa, H.; Yuasa, H.; Shikama, K.; Takemasa, !1T.; Watanabe, Y. !$#journal Biochim. Biophys. Acta (1993) 1173:75-78 !$#title Primary structure of Tetrahymena hemoglobins. !$#cross-references MUID:93250050; PMID:8485156 !$#accession S32555 !'##molecule_type mRNA !'##residues 1-121 ##label TAK !'##cross-references EMBL:D13920; NID:g217409; PIDN:BAA03015.1; !1PID:g418106 REFERENCE A36270 !$#authors Iwaasa, H.; Takagi, T.; Shikama, K. !$#journal J. Biol. Chem. (1990) 265:8603-8609 !$#title Protozoan hemoglobin from Tetrahymena pyriformis. Isolation, !1characterization, and amino acid sequence. !$#cross-references MUID:90256780; PMID:2111321 !$#accession A36270 !'##molecule_type protein !'##residues 1-121 ##label IWA GENETICS !$#genetic_code SGC5 CLASSIFICATION #superfamily Tetrahymena globin KEYWORDS chromoprotein; heme; iron; metalloprotein; monomer FEATURE !$1-121 #product hemoglobin I #status experimental #label !8MAT1\ !$3-121 #product hemoglobin II #status experimental #label !8MAT2\ !$73 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 121 #molecular-weight 13684 #checksum 81 SEQUENCE /// ENTRY S32556 #type complete TITLE hemoglobin - Tetrahymena thermophila ORGANISM #formal_name Tetrahymena thermophila DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S32556 REFERENCE S32555 !$#authors Takagi, T.; Iwaasa, H.; Yuasa, H.; Shikama, K.; Takemasa, !1T.; Watanabe, Y. !$#journal Biochim. Biophys. Acta (1993) 1173:75-78 !$#title Primary structure of Tetrahymena hemoglobins. !$#cross-references MUID:93250050; PMID:8485156 !$#accession S32556 !'##status preliminary !'##molecule_type mRNA !'##residues 1-121 ##label TAK !'##cross-references EMBL:D13919; NID:g217410; PIDN:BAA03014.1; !1PID:g418107 GENETICS !$#genetic_code SGC5 CLASSIFICATION #superfamily Tetrahymena globin KEYWORDS chromoprotein; heme; iron; metalloprotein FEATURE !$73 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 121 #molecular-weight 13590 #checksum 9047 SEQUENCE /// ENTRY S27185 #type complete TITLE hemoglobin major component - Paramecium caudatum ALTERNATE_NAMES B-type hemoglobin; monomeric hemoglobin; myoglobin ORGANISM #formal_name Paramecium caudatum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S27185; S05230; JQ2009; JQ1316 REFERENCE S27185 !$#authors Yamauchi, K.; Ochiai, T.; Usuki, I. !$#journal Biochim. Biophys. Acta (1992) 1171:81-87 !$#title The unique structure of the Paramecium caudatum hemoglobin !1gene: the presence of one intron in the middle of the coding !1region. !$#cross-references MUID:93042011; PMID:1420365 !$#accession S27185 !'##molecule_type DNA !'##residues 1-116 ##label YAM !'##cross-references EMBL:M99047 !'##note the authors did not translate the codon for residue 1 REFERENCE S05230 !$#authors Iwaasa, H.; Takagi, T.; Shikama, K. !$#journal J. Mol. Biol. (1989) 208:355-358 !$#title Protozoan myoglobin from Paramecium caudatum. Its unusual !1amino acid sequence. !$#cross-references MUID:89362481; PMID:2769763 !$#accession S05230 !'##molecule_type protein !'##residues 2-117 ##label IWA !'##experimental_source strain syngen 3 stock StG1 REFERENCE JQ2009 !$#authors Yamauchi, K.; Tada, H.; Ochiai, T.; Usuki, I. !$#journal Gene (1993) 126:243-246 !$#title Structure of the Paramecium caudatum gene encoding the !1B-type of the major hemoglobin component. !$#cross-references MUID:93246250; PMID:8482540 !$#accession JQ2009 !'##molecule_type DNA !'##residues 1-117 ##label YAW !'##cross-references DDBJ:D12916; NID:g397832; PIDN:BAA02300.1; !1PID:g415308 !'##experimental_source stock K33 REFERENCE JQ1316 !$#authors Yamauchi, K.; Mukai, M.; Ochiai, T.; Usuki, I. !$#journal Biochem. Biophys. Res. Commun. (1992) 182:195-200 !$#title Molecular cloning of the cDNA for the major hemoglobin !1component from Paramecium caudatum. !$#cross-references MUID:92118012; PMID:1731779 !$#accession JQ1316 !'##molecule_type mRNA !'##residues 1-117 ##label YA2 !'##cross-references GB:M57542 GENETICS !$#gene Hb !$#genetic_code SGC5 !$#introns 63/3 CLASSIFICATION #superfamily Tetrahymena globin KEYWORDS acetylated amino end; chromoprotein; heme; iron; !1metalloprotein; oxygen carrier FEATURE !$2-117 #product hemoglobin major component #status !8experimental #label MAT\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental\ !$69 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 117 #molecular-weight 12039 #checksum 8619 SEQUENCE /// ENTRY S60030 #type complete TITLE hemoglobin - Paramecium jenningsi ORGANISM #formal_name Paramecium jenningsi DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S60030 REFERENCE S60030 !$#authors Yamauchi, K.; Tada, H.; Usuki, I. !$#journal Biochim. Biophys. Acta (1995) 1264:53-62 !$#title Structure and evolution of Paramecium hemoglobin genes. !$#cross-references MUID:96038820; PMID:7578257 !$#accession S60030 !'##molecule_type DNA !'##residues 1-117 ##label YAM !'##cross-references EMBL:D49689; NID:g1071656; PIDN:BAA08540.1; !1PID:g1384087 !'##note the authors did not translate the codon for residue 1 GENETICS !$#gene Hb !$#genetic_code SGC5 !$#introns 63/3 CLASSIFICATION #superfamily Tetrahymena globin KEYWORDS chromoprotein; heme; iron; metalloprotein FEATURE !$69 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 117 #molecular-weight 12090 #checksum 9370 SEQUENCE /// ENTRY S60032 #type complete TITLE hemoglobin - Paramecium triaurelia ORGANISM #formal_name Paramecium triaurelia DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S60032 REFERENCE S60030 !$#authors Yamauchi, K.; Tada, H.; Usuki, I. !$#journal Biochim. Biophys. Acta (1995) 1264:53-62 !$#title Structure and evolution of Paramecium hemoglobin genes. !$#cross-references MUID:96038820; PMID:7578257 !$#accession S60032 !'##molecule_type DNA !'##residues 1-117 ##label YAM !'##cross-references EMBL:D49688; NID:g1071655; PIDN:BAA08539.1; !1PID:g1384086 !'##note the authors did not translate the codon for residue 1 GENETICS !$#gene Hb !$#genetic_code SGC5 !$#introns 63/3 CLASSIFICATION #superfamily Tetrahymena globin KEYWORDS chromoprotein; heme; iron; metalloprotein FEATURE !$69 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 117 #molecular-weight 12090 #checksum 9370 SEQUENCE /// ENTRY S60031 #type complete TITLE hemoglobin - Paramecium multimicronucleatum ORGANISM #formal_name Paramecium multimicronucleatum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S60031 REFERENCE S60030 !$#authors Yamauchi, K.; Tada, H.; Usuki, I. !$#journal Biochim. Biophys. Acta (1995) 1264:53-62 !$#title Structure and evolution of Paramecium hemoglobin genes. !$#cross-references MUID:96038820; PMID:7578257 !$#accession S60031 !'##molecule_type DNA !'##residues 1-118 ##label YAM !'##cross-references EMBL:D49687; NID:g1071654; PIDN:BAA08538.1; !1PID:g1384085 !'##note the authors did not translate the codon for residue 1 GENETICS !$#gene Hb !$#genetic_code SGC5 !$#introns 63/3 CLASSIFICATION #superfamily Tetrahymena globin KEYWORDS chromoprotein; heme; iron; metalloprotein FEATURE !$69 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 118 #molecular-weight 12091 #checksum 8513 SEQUENCE /// ENTRY S13421 #type fragment TITLE polymeric globin alpha - brine shrimp (fragment) ORGANISM #formal_name Artemia sp. #common_name brine shrimp DATE 19-Mar-1997 #sequence_revision 14-Nov-1997 #text_change 03-Mar-2000 ACCESSIONS S13421 REFERENCE S13421 !$#authors Manning, A.M.; Trotman, C.N.A.; Tate, W.P. !$#journal Nature (1990) 348:653-656 !$#title Evolution of a polymeric globin in the brine shrimp Artemia. !$#cross-references MUID:91066953; PMID:2250721 !$#accession S13421 !'##molecule_type mRNA !'##residues 1-1405 ##label MAN COMMENT In this species, alpha and beta globin genes each encode !1many repeats of a myoglobin-like heme-binding domain !1separated by short linkers. Hemoglobin I is an alpha chain !1homodimer, II is a heterodimer, and III is a beta chain !1homodimer. All are approximately 260 kilodaltons. CLASSIFICATION #superfamily Artemia polymeric globin; globin homology KEYWORDS chromoprotein; heme; heterodimer; homodimer; iron; !1metalloprotein FEATURE !$1-139 #domain globin homology (fragment) #label GLB1\ !$150-293 #domain globin homology #label GLB2\ !$304-450 #domain globin homology #label GLB3\ !$461-607 #domain globin homology #label GLB4\ !$620-762 #domain globin homology #label GLB5\ !$772-918 #domain globin homology #label GLB6\ !$929-1075 #domain globin homology #label GLB7\ !$1086-1234 #domain globin homology #label GLB8\ !$1245-1390 #domain globin homology #label GLB9\ !$57 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$89 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted\ !$211 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$243 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted\ !$365 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$397 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted\ !$524 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$556 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted\ !$681 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$713 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted\ !$833 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$865 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted\ !$990 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$1022 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted\ !$1149 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$1181 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted\ !$1305 #binding_site oxygen (His) (distal axial ligand) !8#status predicted\ !$1337 #binding_site heme iron (His) (proximal axial ligand) !8#status predicted SUMMARY #length 1405 #checksum 648 SEQUENCE /// ENTRY BHTLD #type complete TITLE hemocyanin chain d - American tarantula (Eurypelma californica) ORGANISM #formal_name Eurypelma californica DATE 15-Nov-1984 #sequence_revision 15-Nov-1984 #text_change 01-Aug-1997 ACCESSIONS A02565 REFERENCE A02565 !$#authors Schartau, W.; Eyerle, F.; Reisinger, P.; Geisert, H.; Storz, !1H.; Linzen, B. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1983) 364:1383-1409 !$#title Hemocyanins in spiders, XIX[1]. Complete amino-acid sequence !1of subunit d from Eurypelma californicum hemocyanin, and !1comparison to chain e. !$#cross-references MUID:84059636; PMID:6642428 !$#accession A02565 !'##molecule_type protein !'##residues 1-627 ##label SCH COMMENT Residues 169-177 and 319-327 are thought to form the copper !1binding site. The two copper ions bound each have 3 nitrogen !1ligands (presumably contributed by histidine residues) and !1share a bridging ligand (possibly contributed by a tyrosine !1residue) in addition to binding oxygen. COMMENT The hemocyanins are copper-containing, oxygen transport !1proteins that are highly conserved but found only in !1arthropods and molluscs. These proteins have a complex and !1variable quaternary structure with homologous chains !1aggregating to form either simple hexamers or multihexamer !1configurations. The tarantula hemocyanin is a 24-chain !1polymer with seven different chains identified. CLASSIFICATION #superfamily hemocyanin KEYWORDS copper; glycoprotein; oxygen carrier FEATURE !$445 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 627 #molecular-weight 72178 #checksum 9707 SEQUENCE /// ENTRY BHTLE #type complete TITLE hemocyanin chain e - American tarantula (Eurypelma californica) ORGANISM #formal_name Eurypelma californica DATE 15-Nov-1984 #sequence_revision 31-Mar-1992 #text_change 22-Jun-1999 ACCESSIONS S06701; A35772; S13441; A02566; A24179; B37975; S08107 REFERENCE S06701 !$#authors Voll, W.M.M. !$#submission submitted to the EMBL Data Library, August 1989 !$#accession S06701 !'##molecule_type DNA !'##residues 1-624 ##label VOL !'##cross-references EMBL:X16650; NID:g9249; PIDN:CAA34643.1; !1PID:g829205 REFERENCE A35772 !$#authors Voll, W.; Voit, R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:5312-5316 !$#title Characterization of the gene encoding the hemocyanin subunit !1e from the tarantula Eurypelma californicum. !$#cross-references MUID:90319102; PMID:2371273 !$#accession A35772 !'##molecule_type DNA !'##residues 1-64;604-624 ##label VOL2 REFERENCE A37975 !$#authors Voit, R.; Feldmaier-Fuchs, G. !$#journal J. Biol. Chem. (1990) 265:19447-19452 !$#title Arthropod hemocyanins. Molecular cloning and sequencing of !1cDNAs encoding the tarantula hemocyanin subunits a and e. !$#cross-references MUID:91060544; PMID:2246235 !$#accession S13441 !'##molecule_type mRNA !'##residues 1-624 ##label VOI !'##cross-references EMBL:X16894; NID:g9268; PIDN:CAA34772.1; PID:g9269 REFERENCE A02566 !$#authors Schneider, H.J.; Drexel, R.; Feldmaier, G.; Linzen, B.; !1Lottspeich, F.; Henschen, A. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1983) 364:1357-1381 !$#title Hemocyanins in spiders, XVIII[1]. Complete amino-acid !1sequence of subunit e from Eurypelma californicum !1hemocyanin. !$#cross-references MUID:84059635; PMID:6357986 !$#accession A02566 !'##molecule_type protein !'##residues 2-29,'R',31-46,'D',48-79,'K',81-90,'H',92-110,112-159,'K', !1161-216,'H',218-254,'M',256-307,'H',309-326,'M',327-528,'D', !1530,'K',532-561,'D',565-602,'F',604-608,'V',610-624 ##label !1SCH GENETICS !$#introns 65/1; 137/3; 206/2; 338/3; 381/3; 426/3; 489/1; 560/3 CLASSIFICATION #superfamily hemocyanin KEYWORDS copper; hemolymph; oxygen carrier FEATURE !$2-624 #product hemocyanin chain e #status experimental !8#label MAT\ !$2-150 #domain 1 #label DO1\ !$151-374 #domain 2 #label DO2\ !$375-624 #domain 3 #label DO3\ !$169,173,200 #binding_site copper (His) #status predicted\ !$320,324,360 #binding_site copper (His) #status predicted SUMMARY #length 624 #molecular-weight 71668 #checksum 9799 SEQUENCE /// ENTRY BHTLA #type complete TITLE hemocyanin chain a - American tarantula (Eurypelma californica) ORGANISM #formal_name Eurypelma californica DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 01-Aug-1997 ACCESSIONS A37975; S10606; S08108; S13440 REFERENCE A37975 !$#authors Voit, R.; Feldmaier-Fuchs, G. !$#journal J. Biol. Chem. (1990) 265:19447-19452 !$#title Arthropod hemocyanins. Molecular cloning and sequencing of !1cDNAs encoding the tarantula hemocyanin subunits a and e. !$#cross-references MUID:91060544; PMID:2246235 !$#accession A37975 !'##molecule_type mRNA !'##residues 1-631 ##label VOI !'##cross-references EMBL:X16893 !'##note 29-Ala was also found REFERENCE S10606 !$#authors Schartau, W.; Metzger, W.; Sonner, P.; Geisert, H.; Storz, !1H. !$#journal Biol. Chem. Hoppe-Seyler (1990) 371:557-565 !$#title Hemocyanins in spiders, XXIII. Complete amino-acid sequence !1of subunit a of Eurypelma californicum hemocyanin. !$#cross-references MUID:91025623; PMID:2222854 !$#accession S10606 !'##molecule_type protein !'##residues 2-28,'A',30-44,'D',46-132,'I',134-148,'I',150-154,'L', !1156-262,'M',264-411,'L',413-539,'K',541-544,'T',546-547,'R', !1548-577,'V',579-631 ##label SCH CLASSIFICATION #superfamily hemocyanin KEYWORDS copper; hemolymph; oxygen carrier FEATURE !$2-631 #product hemocyanin chain a #status experimental !8#label MAT\ !$2-156 #domain 1 #label DO1\ !$157-380 #domain 2 #label DO2\ !$381-631 #domain 3 #label DO3\ !$175,179,206 #binding_site copper (His) #status predicted\ !$326,330,366 #binding_site copper (His) #status predicted SUMMARY #length 631 #molecular-weight 72360 #checksum 7728 SEQUENCE /// ENTRY BHHC2A #type complete TITLE hemocyanin subunit II - Atlantic horseshoe crab ORGANISM #formal_name Limulus polyphemus #common_name Atlantic horseshoe crab DATE 04-Dec-1986 #sequence_revision 14-Jul-1994 #text_change 26-Feb-1999 ACCESSIONS A26713; A02568; B20554 REFERENCE A26713 !$#authors Nakashima, H.; Behrens, P.Q.; Moore, M.D.; Yokota, E.; !1Riggs, A.F. !$#journal J. Biol. Chem. (1986) 261:10526-10533 !$#title Structure of hemocyanin II from the horseshoe crab, Limulus !1polyphemus. Sequences of the overlapping peptides, ordering !1the CNBr fragments, and the complete amino acid sequence. !$#cross-references MUID:86278119; PMID:3525550 !$#accession A26713 !'##molecule_type protein !'##residues 1-407,'FT',410-628 ##label NAK REFERENCE A02568 !$#authors Yokota, E.; Riggs, A.F. !$#journal J. Biol. Chem. (1984) 259:4739-4749 !$#title The structure of the hemocyanin from the horseshoe crab, !1Limulus polyphemus. The amino acid sequence of the largest !1cyanogen bromide fragment. !$#cross-references MUID:84185567; PMID:6715319 !$#accession A02568 !'##molecule_type protein !'##residues 1-203 ##label YOK REFERENCE A90478 !$#authors Lamy, J.; Lamy, J.; Sizaret, P.Y.; Billiald, P.; Jolles, P.; !1Jolles, J.; Feldmann, R.J.; Bonaventura, J. !$#journal Biochemistry (1983) 22:5573-5583 !$#title Quaternary structure of Limulus polyphemus hemocyanin. !$#accession B20554 !'##molecule_type protein !'##residues 1-9,'V',11-21,'FH' ##label LAM REFERENCE A47325 !$#authors Hazes, B.; Magnus, K.A.; Bonaventura, C.; Bonaventura, J.; !1Dauter, Z.; Kalk, K.H.; Hol, W.G.J. !$#journal Protein Sci. (1993) 2:597-619 !$#title Crystal structure of deoxygenated Limulus polyphemus subunit !1II hemocyacin at 2.18 angstroms resolution: clues for a !1mechanism for allosteric regulation. !$#cross-references MUID:93299372; PMID:8518732 !$#contents annotation; X-ray crystallography, 2.18 angstroms; sequence !1revision !$#note evidence for reordering of Thr-408, Phe-409; Ile was fit !1better than Val at position 9 COMMENT Limulus polyphemus hemocyanin is an association of eight !1different subunits within eight heterohexamers. !1Approximately 8 chains of subunit II are found in the !148-mer. COMMENT The homohexamer of subunit II by itself exhibits cooperative !1oxygen binding, reduced by chloride and enhanced by lower !1pH. COMMENT One molecule of oxygen is bound between the two copper !1atoms, which are separated by 4.61 angstroms in the !1deoxygenated form. COMMENT Alternative conformations of Glu-309 may regulate oxygen !1access to the binding site. COMMENT There are only 2 disulfide bonds. CLASSIFICATION #superfamily hemocyanin KEYWORDS blocked amino end; copper; oxygen carrier FEATURE !$1-154 #domain 1, amino-terminal #label DO1\ !$155-380 #domain 2, oxygen binding #label DO2\ !$381-628 #domain 3, carboxyl-terminal #label DO3\ !$1 #modified_site blocked amino end (Thr) (partial) !8#status experimental\ !$47,333 #binding_site chloride (Ser, Arg) #status !8experimental\ !$173,177,204 #binding_site copper (His) #status experimental\ !$208-213 #disulfide_bonds #status absent\ !$324,328,364 #binding_site copper (His) #status experimental\ !$507,510,578 #binding_site calcium (Ser, Thr, Asp) #status !8predicted\ !$534-576,536-583 #disulfide_bonds #status experimental SUMMARY #length 628 #molecular-weight 72628 #checksum 9112 SEQUENCE /// ENTRY BHLOA #type complete TITLE hemocyanin chain a - California spiny lobster ORGANISM #formal_name Panulirus interruptus #common_name California spiny lobster DATE 31-Dec-1988 #sequence_revision 30-Jun-1991 #text_change 07-May-1999 ACCESSIONS A24183; S06859; A02569; A25716 REFERENCE A24183 !$#authors Bak, H.J.; Neuteboom, B.; Jekel, P.A.; Soeter, N.M.; !1Vereijken, J.M.; Beintema, J.J. !$#journal FEBS Lett. (1986) 204:141-144 !$#title Structure of arthropod hemocyanin. !$#accession A24183 !'##molecule_type protein !'##residues 1-138,'Q',140-657 ##label BAK !'##note this sequence has been revised in reference S02707 REFERENCE S02707 !$#authors Jekel, P.A.; Bak, H.J.; Soeter, N.M.; Vereijken, J.M.; !1Beintema, J.J. !$#journal Eur. J. Biochem. (1988) 178:403-412 !$#title Panulirus interruptus hemocyanin. The amino acid sequence of !1subunit b and anomalous behaviour of subunits a and b on !1polyacrylamide gel electrophoresis in the presence of SDS. !$#cross-references MUID:89091175; PMID:3208765 !$#accession S06859 !'##molecule_type protein !'##residues 139 ##label JEK REFERENCE A02569 !$#authors Vereijken, J.M.; De Vlieg, J.; Beintema, J.J. !$#journal Biochim. Biophys. Acta (1984) 788:298-305 !$#title Panulirus interruptus hemocyanin. The amino-acid sequence of !1the region containing one copper-binding site and the sites !1susceptible to limited proteolysis. !$#accession A02569 !'##molecule_type protein !'##residues 160-230 ##label VER REFERENCE A26249 !$#authors Gaykema, W.P.J.; Hol, W.G.J.; Vereijken, J.M.; Soeter, N.M.; !1Bak, H.J.; Beintema, J.J. !$#journal Nature (1984) 309:23-29 !$#title 3.2 angstrom structure of the copper-containing, !1oxygen-carrying protein Panulirus interruptus haemocyanin. !$#contents annotation; X-ray crystallography, 3.2 angstroms REFERENCE A44600 !$#authors Volbeda, A.; Hol, W.G.J. !$#journal J. Mol. Biol. (1989) 209:249-279 !$#title Crystal structure of hexameric haemocyanin from Panulirus !1interruptus refined at 3.2 angstroms resolution. !$#cross-references MUID:90064489; PMID:2585484 !$#contents annotation; X-ray crystallography, 3.2 angstroms !$#note the crystals contained a mixture of a and b chains; the !1structure was fit to a sequence matching the a chain except !1at positions 32, 163, 458, and 574, where the b chain !1sequence was used COMMENT This hemocyanin is a hexamer of a number of different !1chains, of which a, b, and c have been identified. COMMENT One molecule of oxygen is bound between the two copper !1atoms, which are separated by 3.16 angstroms in the !1deoxygenated form. CLASSIFICATION #superfamily hemocyanin KEYWORDS copper; glycoprotein; hemolymph; oxygen carrier FEATURE !$1-175 #domain 1, amino-terminal #label DO1\ !$176-398 #domain 2, oxygen binding #label DO2\ !$399-657 #domain 3, carboxyl-terminal #label DO3\ !$93-98,483-502, !$562-609 #disulfide_bonds #status experimental\ !$167 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$194,198,224 #binding_site copper (His) #status experimental\ !$344,348,384 #binding_site copper (His) #status experimental SUMMARY #length 657 #molecular-weight 75696 #checksum 4043 SEQUENCE /// ENTRY BHLOB #type complete TITLE hemocyanin chain b - California spiny lobster ALTERNATE_NAMES hemocyanin 90K chain ORGANISM #formal_name Panulirus interruptus #common_name California spiny lobster DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 07-May-1999 ACCESSIONS S02707 REFERENCE S02707 !$#authors Jekel, P.A.; Bak, H.J.; Soeter, N.M.; Vereijken, J.M.; !1Beintema, J.J. !$#journal Eur. J. Biochem. (1988) 178:403-412 !$#title Panulirus interruptus hemocyanin. The amino acid sequence of !1subunit b and anomalous behaviour of subunits a and b on !1polyacrylamide gel electrophoresis in the presence of SDS. !$#cross-references MUID:89091175; PMID:3208765 !$#accession S02707 !'##molecule_type protein !'##residues 1-657 ##label JEK !'##note 32-Glu, 49-Gln, 122-Gly, 130-Lys, 132-Val, and 561-Ala were !1also found REFERENCE A26249 !$#authors Gaykema, W.P.J.; Hol, W.G.J.; Vereijken, J.M.; Soeter, N.M.; !1Bak, H.J.; Beintema, J.J. !$#journal Nature (1984) 309:23-29 !$#title 3.2 angstrom structure of the copper-containing, !1oxygen-carrying protein Panulirus interruptus haemocyanin. !$#contents annotation; X-ray crystallography, 3.2 angstroms REFERENCE A44600 !$#authors Volbeda, A.; Hol, W.G.J. !$#journal J. Mol. Biol. (1989) 209:249-279 !$#title Crystal structure of hexameric haemocyanin from Panulirus !1interruptus refined at 3.2 angstroms resolution. !$#cross-references MUID:90064489; PMID:2585484 !$#contents annotation; X-ray crystallography, 3.2 angstroms !$#note the crystals contained a mixture of a and b chains; the !1structure was fit to a sequence matching the a chain except !1at positions 32, 163, 458, and 574, where the b chain !1sequence was used COMMENT This hemocyanin is a hexamer of a number of different !1chains, of which a, b, and c have been identified. COMMENT One molecule of oxygen is bound between the two copper !1atoms, which are separated by 3.16 angstroms in the !1deoxygenated form. CLASSIFICATION #superfamily hemocyanin KEYWORDS copper; glycoprotein; hemolymph; oxygen carrier FEATURE !$1-175 #domain 1, amino-terminal #label DO1\ !$176-398 #domain 2, oxygen binding #label DO2\ !$399-657 #domain 3, carboxyl-terminal #label DO3\ !$93-98,483-502, !$562-609 #disulfide_bonds #status experimental\ !$167 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$194,198,224 #binding_site copper (His) #status experimental\ !$344,348,384 #binding_site copper (His) #status experimental SUMMARY #length 657 #molecular-weight 75388 #checksum 958 SEQUENCE /// ENTRY HRGG #type complete TITLE hemerythrin - sipunculid (Phascolopsis gouldii) ORGANISM #formal_name Phascolopsis gouldii DATE 18-Apr-1984 #sequence_revision 18-Apr-1984 #text_change 01-Aug-1997 ACCESSIONS A90553; A91281; A90211; A90361; A02570 REFERENCE A90553 !$#authors Klippenstein, G.L.; Holleman, J.W.; Klotz, I.M. !$#journal Biochemistry (1968) 7:3868-3878 !$#title The primary structure of Golfingia gouldii hemerythrin. !1Order of peptides in fragments produced by tryptic digestion !1of succinylated hemerythrin. Complete amino acid sequence. !$#cross-references MUID:69051123; PMID:5722254 !$#accession A90553 !'##molecule_type protein !'##residues 1-9,'DW',12-57,'QE',60-113 ##label KLI !'##note the other major variants have 79-Thr, 96-Ala, or 79-Thr and !196-Ala REFERENCE A91281 !$#authors Ferrell, R.E.; Kitto, G.B. !$#journal FEBS Lett. (1971) 12:322-324 !$#title The aminoterminal sequence of Dendrostomum pyroides !1hemerythrin. !$#accession A91281 !'##molecule_type protein !'##residues 1-12 ##label FER REFERENCE A90211 !$#authors Gormley, P.M.; Loehr, J.S.; Brimhall, B.; Hermodson, M.A. !$#journal Biochem. Biophys. Res. Commun. (1978) 85:1360-1366 !$#title New evidence for glutamic acid as an iron ligand in !1hemerythrin. !$#cross-references MUID:79124201; PMID:743303 !$#accession A90211 !'##molecule_type protein !'##residues 50-62 ##label GOR REFERENCE A90361 !$#authors Klippenstein, G.L. !$#journal Biochemistry (1972) 11:372-379 !$#title Molecular variants of Golfingia gouldii hemerythrin. The !1primary structure of the variants arising from five amino !1acid interchanges. !$#cross-references MUID:72108270; PMID:5059118 !$#contents minor component !$#accession A90361 !'##molecule_type protein !'##residues 1-62,'E',64-77,'D',79-81,'N',83-95,'A',97-113 ##label KL2 COMMENT The sequence from one of the four major component variants !1is shown. CLASSIFICATION #superfamily hemerythrin KEYWORDS iron; oxygen carrier FEATURE !$25,54,58,73,77,101, !$106 #binding_site 2Fe-O cluster (His, His, Glu, His, His, !8His, Asp) #status predicted SUMMARY #length 113 #molecular-weight 13430 #checksum 3343 SEQUENCE /// ENTRY HRTH #type complete TITLE hemerythrin - sipunculid (Themiste zostericola) (tentative sequence) ORGANISM #formal_name Themiste zostericola DATE 24-Apr-1984 #sequence_revision 17-May-1996 #text_change 01-Aug-1997 ACCESSIONS A02571 REFERENCE A02571 !$#authors Ferrell, R.E.; Kitto, G.B. !$#journal Biochemistry (1971) 10:2923-2929 !$#title Structural studies on Dendrostomum pyroides hemerythrin. !$#cross-references MUID:72028385; PMID:5114534 !$#accession A02571 !'##molecule_type protein !'##residues 1-57,'QE',60-113 ##label FER !'##note we have reversed the amidation of residues 58 and 59 to conform !1with structural predictions REFERENCE A93255 !$#authors Stenkamp, R.E.; Sieker, L.C.; Jensen, L.H.; Sanders-Loehr, !1J. !$#journal Nature (1981) 291:263-264 !$#title Structure of the binuclear iron complex in !1metazidohaemerythrin from Themiste dyscritum at 2.2 angstrom !1resolution. !$#contents annotation; X-ray crystallography, 2.2 angstroms, and iron !1ligands of Themiste dyscritum hemerythrin REFERENCE A92203 !$#authors Hendrickson, W.A.; Ward, K.B. !$#journal J. Biol. Chem. (1977) 252:3012-3018 !$#title Pseudosymmetry in the structure of myhemerythrin. !$#cross-references MUID:77165245; PMID:856811 !$#contents annotation !$#note this worm was misidentified as Themiste pyroides COMMENT Hemerythrin is a respiratory protein in blood cells of !1certain marine worms. COMPLEX homooctamer CLASSIFICATION #superfamily hemerythrin KEYWORDS homooctamer; iron; oxygen carrier FEATURE !$25,54,58,73,77,101, !$106 #binding_site 2Fe-O cluster (His, His, Glu, His, His, !8His, Asp) #status experimental SUMMARY #length 113 #molecular-weight 13421 #checksum 3338 SEQUENCE /// ENTRY HRTHBD #type complete TITLE hemerythrin - sipunculid (Themiste dyscritum) ORGANISM #formal_name Themiste dyscritum DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 01-Aug-1997 ACCESSIONS A92234; A02572 REFERENCE A92234 !$#authors Loehr, J.S.; Lammers, P.J.; Brimhall, B.; Hermodson, M.A. !$#journal J. Biol. Chem. (1978) 253:5726-5731 !$#title Amino acid sequence of hemerythrin from Themiste dyscritum. !$#cross-references MUID:78218273; PMID:670224 !$#accession A92234 !'##molecule_type protein !'##residues 1-113 ##label LOE !'##note composition data for tryptic peptide 50-73 suggests that both !1Ala and Ser may be found at position 64 REFERENCE A90413 !$#authors Stenkamp, R.E.; Sieker, L.C.; Jensen, L.H.; McQueen Jr., !1J.E. !$#journal Biochemistry (1978) 17:2499-2504 !$#title Structure of methemerythrin at 2.8-angstrom resolution: !1computer graphics fit of an averaged electron density map. !$#cross-references MUID:78235906; PMID:678527 !$#contents annotation; X-ray crystallography, 2.8 angstroms, and iron !1ligands REFERENCE A93255 !$#authors Stenkamp, R.E.; Sieker, L.C.; Jensen, L.H.; Sanders-Loehr, !1J. !$#journal Nature (1981) 291:263-264 !$#title Structure of the binuclear iron complex in !1metazidohaemerythrin from Themiste dyscritum at 2.2 angstrom !1resolution. !$#contents annotation; X-ray crystallography, 2.2 angstroms, and iron !1ligands COMMENT Hemerythrin is a respiratory protein in blood cells of !1certain marine worms. COMPLEX homooctamer CLASSIFICATION #superfamily hemerythrin KEYWORDS homooctamer; iron; oxygen carrier FEATURE !$25,54,58,73,77,101, !$106 #binding_site 2Fe-O cluster (His, His, Glu, His, His, !8His, Asp) #status experimental SUMMARY #length 113 #molecular-weight 13319 #checksum 4997 SEQUENCE /// ENTRY HRTHM #type complete TITLE myohemerythrin [validated] - sipunculid (Themiste zostericola) ORGANISM #formal_name Themiste zostericola DATE 24-Apr-1984 #sequence_revision 30-Jun-1993 #text_change 15-Sep-2000 ACCESSIONS A37369; A02573 REFERENCE A37369 !$#authors Sheriff, S.; Hendrickson, W.A.; Smith, J.L. !$#journal J. Mol. Biol. (1987) 197:273-296 !$#title Structure of myohemerythrin in the azidomet state at 1.7/1.3 !1angstrom resolution. !$#cross-references MUID:88062755; PMID:3681996 !$#contents sequence; X-ray crystallography, 1.7 angstroms !$#accession A37369 !'##molecule_type protein !'##residues 1-118 ##label SHE !'##note the modeled sequence at 34-35 was confirmed by sequencing REFERENCE A90394 !$#authors Klippenstein, G.L.; Cote, J.L.; Ludlam, S.E. !$#journal Biochemistry (1976) 15:1128-1136 !$#title The primary structure of myohemerythrin. !$#cross-references MUID:76136381; PMID:1252432 !$#accession A02573 !'##molecule_type protein !'##residues 1-33,'CD',36-118 ##label KLI REFERENCE A50494 !$#authors Sheriff, S.; Hendrickson, W.A. !$#submission submitted to the Brookhaven Protein Data Bank, April 1987 !$#cross-references PDB:2MHR !$#contents annotation; X-ray crystallography, 1.7 angstroms, residues !11-118 REFERENCE A93798 !$#authors Hendrickson, W.A.; Klippenstein, G.L.; Ward, K.B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1975) 72:2160-2164 !$#title Tertiary structure of myohemerythrin at low resolution. !$#cross-references MUID:75176901; PMID:1056020 !$#contents annotation; X-ray crystallography, 5.5 angstroms REFERENCE A92203 !$#authors Hendrickson, W.A.; Ward, K.B. !$#journal J. Biol. Chem. (1977) 252:3012-3018 !$#title Pseudosymmetry in the structure of myhemerythrin. !$#cross-references MUID:77165245; PMID:856811 !$#contents annotation !$#note this worm was misidentified as Themiste pyroides in !1reference A93798 COMPLEX monomer FUNCTION !$#description binds molecular oxygen for intracellular storage and !1transport, primarily in the retractor muscles CLASSIFICATION #superfamily hemerythrin KEYWORDS iron; metalloprotein; monomer; muscle; oxygen carrier FEATURE !$25,54,58,73,77,106, !$111 #binding_site 2Fe-O cluster (His, His, Glu, His, His, !8His, Asp) #status experimental SUMMARY #length 118 #molecular-weight 13778 #checksum 1326 SEQUENCE /// ENTRY HRIN #type complete TITLE hemerythrin - sipunculid (Siphonosoma cumanense) ORGANISM #formal_name Siphonosoma cumanense DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 01-Aug-1997 ACCESSIONS JT0556 REFERENCE JT0556 !$#authors Uchida, T.; Yano, H.; Satake, K.; Kubota, I.; Tsugita, A. !$#journal Protein Seq. Data Anal. (1990) 3:141-147 !$#title The amino acid sequence of hemerythrin from Siphonosoma !1cumanense. !$#cross-references MUID:90301732; PMID:2362933 !$#accession JT0556 !'##molecule_type protein !'##residues 1-113 ##label UCH !'##note 3-Glu, 10-Asp, 60-Gly, 66-Asn, and 83-Gln were also found COMMENT Hemerythrin is a respiratory protein found in several phyla !1of marine invertebrates. The functional molecule is a trimer !1composed of homologous chains, each of which contains a pair !1of nonheme iron atoms that reversibly bind molecular oxygen. CLASSIFICATION #superfamily hemerythrin KEYWORDS iron; oxygen carrier FEATURE !$25,54,58,73,77,101, !$106 #binding_site 2Fe-O cluster (His, His, Glu, His, His, !8His, Asp) #status predicted SUMMARY #length 113 #molecular-weight 12437 #checksum 1365 SEQUENCE /// ENTRY D70448 #type complete TITLE hemerythrin homolog aq_1719 - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 15-Oct-1999 ACCESSIONS D70448 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession D70448 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-131 ##label AQF !'##cross-references GB:AE000753; NID:g2984035; PIDN:AAC07584.1; !1PID:g2984042; GB:AE000657 !'##experimental_source strain VF5 GENETICS !$#gene aq_1719 CLASSIFICATION #superfamily hemerythrin KEYWORDS iron FEATURE !$20,56,60,75,79,117, !$122 #binding_site 2Fe-O cluster (His, His, Glu, His, His, !8His, Asp) #status predicted SUMMARY #length 131 #molecular-weight 15964 #checksum 1038 SEQUENCE /// ENTRY C64393 #type complete TITLE hemerythrin homolog MJ0747 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 21-Jul-2000 ACCESSIONS C64393 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession C64393 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-169 ##label BUL !'##cross-references GB:U67520; GB:L77117; NID:g1591447; !1PIDN:AAB98740.1; PID:g1591460; TIGR:MJ0747 GENETICS !$#map_position REV673469-672960 !$#start_codon GTG CLASSIFICATION #superfamily hemerythrin KEYWORDS iron FEATURE !$45,82,86,101,105, !$142,147 #binding_site 2Fe-O cluster (His, His, Glu, His, His, !8His, Asp) #status predicted SUMMARY #length 169 #molecular-weight 20055 #checksum 4154 SEQUENCE /// ENTRY UQHU #type complete TITLE ubiquitin - human (tentative sequence) ALTERNATE_NAMES ubiquitous immunopoietic polypeptide (UBIP) ORGANISM #formal_name Homo sapiens #common_name man DATE 24-Apr-1984 #sequence_revision 28-Apr-1995 #text_change 20-Oct-2000 ACCESSIONS A02574 REFERENCE A93174 !$#authors Schlesinger, D.H.; Goldstein, G. !$#journal Nature (1975) 255:423-424 !$#title Molecular conservation of 74 amino acid sequence of !1ubiquitin between cattle and man. !$#cross-references MUID:75156547; PMID:124018 !$#accession A02574 !'##molecule_type protein !'##residues 1-76 ##label SCH !'##experimental_source thymus REFERENCE A44701 !$#authors Vijay-Kumar, S.; Bugg, C.E.; Cook, W.J. !$#journal J. Mol. Biol. (1987) 194:531-544 !$#title Structure of ubiquitin refined at 1.8 angstroms resolution. !$#cross-references MUID:87311725; PMID:3041007 !$#contents annotation; X-ray crystallography, 1.8 angstroms !$#note source erythrocyte REFERENCE A44702 !$#authors Cook, W.J.; Jeffrey, L.C.; Kasperek, E.; Pickart, C.M. !$#journal J. Mol. Biol. (1994) 236:601-609 !$#title Structure of tetraubiquitin shows how multiubiquitin chains !1can be formed. !$#cross-references MUID:94149762; PMID:8107144 !$#contents annotation; X-ray crystallography, 2.4 angstroms !$#note structure of four cross-linked ubiquitin subunits COMMENT Ubiquitin appears to be present in all cells of all living !1organisms. COMMENT The carboxyl-terminal Gly-Gly residues are shown. CLASSIFICATION #superfamily ubiquitin; ubiquitin homology KEYWORDS protein degradation; thiolester bond FEATURE !$1-76 #product ubiquitin #status experimental #label MAT\ !$1-76 #domain ubiquitin homology #label UBH\ !$48 #cross-link isopeptide (Lys) (interchain to Gly-76) !8#status experimental\ !$76 #cross-link isopeptide carboxyl end (Gly) (interchain !8to Lys N6-amino of other proteins) #status !8experimental\ !$76 #cross-link thiolester carboxyl end (Gly) (interchain !8to Cys of conjugating enzyme) #status predicted SUMMARY #length 76 #molecular-weight 8565 #checksum 9473 SEQUENCE /// ENTRY UQBO #type complete TITLE ubiquitin - bovine (tentative sequence) ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Dec-1991 #sequence_revision 22-Apr-1995 #text_change 20-Oct-2000 ACCESSIONS A90388; A02577; S27064; S27065; A02574 REFERENCE A90388 !$#authors Schlesinger, D.H.; Goldstein, G.; Niall, H.D. !$#journal Biochemistry (1975) 14:2214-2218 !$#title The complete amino acid sequence of ubiquitin, an adenylate !1cyclase stimulating polypeptide probably universal in living !1cells. !$#cross-references MUID:75205496; PMID:1170880 !$#accession A90388 !'##molecule_type protein !'##residues 1-74 ##label SCH !'##experimental_source thymus REFERENCE A02577 !$#authors Hamilton, J.W.; Rouse, J.B. !$#journal Biochem. Biophys. Res. Commun. (1980) 96:114-120 !$#title The biosynthesis of ubiquitin by parathyroid gland. !$#cross-references MUID:81062406; PMID:6254502 !$#accession A02577 !'##molecule_type protein !'##residues 1-19,'X',21-33,'Q',35-40,'E',42-43,'G',45-48,'S',50 ##label !1HAM !'##experimental_source parathyroid REFERENCE A90203 !$#authors Hunt, L.T.; Dayhoff, M.O. !$#journal Biochem. Biophys. Res. Commun. (1977) 74:650-655 !$#title Amino-terminal sequence identity of ubiquitin and the !1nonhistone component of nuclear protein A24. !$#cross-references MUID:77112011; PMID:836318 !$#contents annotation !$#note first recognition of ubiquitin in both cytoplasmic and !1nuclear cellular compartments; nuclear protein p24 is now !1known to be ubiquitin conjugated by isopeptide linkage to !1histone 2A REFERENCE A38936 !$#authors Cook, W.J.; Jeffrey, L.C.; Carson, M.; Chen, Z.; Pickart, !1C.M. !$#journal J. Biol. Chem. (1992) 267:16467-16471 !$#title Structure of a diubiquitin conjugate and a model for !1interaction with ubiquitin conjugating enzyme (E2). !$#cross-references MUID:92355616; PMID:1322903 !$#contents annotation; X-ray crystallography, 2.3 angstroms !$#note structure of two cross-linked ubiquitin subunits REFERENCE S27064 !$#authors Zdebska, E.; Antoniewicz, J.; Nilsson, B.; Sandhoff, K.; !1Fuerst, W.; Janik, P.; Koscielak, J. !$#journal Eur. J. Biochem. (1992) 210:483-489 !$#title Ganglioside binding proteins of calf brain with !1ubiquitin-like N-terminals. !$#cross-references MUID:93092984; PMID:1333954 !$#accession S27064 !'##molecule_type protein !'##residues 1-12 ##label ZDE !'##note this sequence was obtained from ganglioside-binding protein I; !1identity of the sequence to ubiquitin was noted !$#accession S27065 !'##molecule_type protein !'##residues 1-15,'X',17-20 ##label JAN !'##note this sequence was obtained from ganglioside-binding protein II; !1identity of the sequence to ubiquitin was noted COMMENT Ubiquitin appears to be present in all cells of all living !1organisms. COMMENT The carboxyl-terminal Gly-Gly residues are shown. CLASSIFICATION #superfamily ubiquitin; ubiquitin homology KEYWORDS protein degradation FEATURE !$1-76 #product ubiquitin #status experimental #label MAT\ !$1-76 #domain ubiquitin homology #label UBH\ !$48 #cross-link isopeptide (Lys) (interchain to Gly-76) !8#status experimental\ !$76 #cross-link isopeptide carboxyl end (Gly) (interchain !8to Lys N6-amino of other proteins) #status !8experimental SUMMARY #length 76 #molecular-weight 8565 #checksum 9473 SEQUENCE /// ENTRY UQHY #type fragment TITLE ubiquitin precursor - Chinese hamster (fragment) ALTERNATE_NAMES polyubiquitin ORGANISM #formal_name Cricetulus griseus #common_name Chinese hamster DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Aug-1996 ACCESSIONS S02825 REFERENCE S02825 !$#authors Fornace Jr., A.J.; Alamo Jr., I.; Hollander, M.C.; !1Lamoreaux, E. !$#journal Nucleic Acids Res. (1989) 17:1215-1230 !$#title Ubiquitin mRNA is a major stress-induced transcript in !1mammalian cells. !$#cross-references MUID:89160248; PMID:2537950 !$#accession S02825 !'##molecule_type mRNA !'##residues 1-222 ##label FOR !'##cross-references EMBL:X08013 CLASSIFICATION #superfamily ubiquitin; ubiquitin homology KEYWORDS polyprotein; protein degradation FEATURE !$1-76 #product ubiquitin #status predicted #label UBI1\ !$1-76 #domain ubiquitin homology #label UBH1\ !$77-152 #product ubiquitin #status predicted #label UBI2\ !$77-152 #domain ubiquitin homology #label UBH2\ !$153-222 #domain ubiquitin homology (fragment) #label UBH3\ !$153-222 #product ubiquitin (fragment) #status predicted !8#label UBI3 SUMMARY #length 222 #checksum 9497 SEQUENCE /// ENTRY UQFFM #type complete TITLE ubiquitin - Mediterranean fruit fly ORGANISM #formal_name Ceratitis capitata #common_name Mediterranean fruit fly DATE 15-Oct-1982 #sequence_revision 15-Oct-1982 #text_change 16-Aug-1996 ACCESSIONS A02575 REFERENCE A02575 !$#authors Gavilanes, J.G.; Gonzalez de Buitrago, G.; Perez-Castells, !1R.; Rodriguez, R. !$#journal J. Biol. Chem. (1982) 257:10267-10270 !$#title Isolation, characterization, and amino acid sequence of a !1ubiquitin-like protein from insect eggs. !$#cross-references MUID:82265683; PMID:6286647 !$#accession A02575 !'##molecule_type protein !'##residues 1-74 ##label GAV CLASSIFICATION #superfamily ubiquitin; ubiquitin homology KEYWORDS protein degradation FEATURE !$1-74 #domain ubiquitin homology #label UBH SUMMARY #length 74 #molecular-weight 8451 #checksum 6846 SEQUENCE /// ENTRY UQUTC #type fragment TITLE ubiquitin precursor - Trypanosoma cruzi (fragment) ALTERNATE_NAMES polyubiquitin ORGANISM #formal_name Trypanosoma cruzi DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S00510 REFERENCE S00484 !$#authors Swindle, J.; Ajioka, J.; Eisen, H.; Sanwal, B.; Jacquemot, !1C.; Browder, Z.; Buck, G. !$#journal EMBO J. (1988) 7:1121-1127 !$#title The genomic organization and transcription of the ubiquitin !1genes of Trypanosoma cruzi. !$#cross-references MUID:88296415; PMID:2841110 !$#accession S00510 !'##molecule_type DNA !'##residues 1-78 ##label SWI !'##cross-references EMBL:X07451; NID:g10672; PIDN:CAA30334.1; !1PID:g10674 GENETICS !$#gene PUB12.5 CLASSIFICATION #superfamily ubiquitin; ubiquitin homology KEYWORDS polyprotein; protein degradation FEATURE !$1-76 #product ubiquitin #status predicted #label UBI1\ !$1-76 #domain ubiquitin homology #label UBH\ !$77-78 #product ubiquitin (fragment) #status predicted !8#label UBI2 SUMMARY #length 78 #checksum 1479 SEQUENCE /// ENTRY UQOA #type complete TITLE ubiquitin - oat ORGANISM #formal_name Avena sativa #common_name oat DATE 13-Aug-1986 #sequence_revision 13-Aug-1986 #text_change 16-Aug-1996 ACCESSIONS A02576 REFERENCE A02576 !$#authors Vierstra, R.D.; Langan, S.M.; Schaller, G.E. !$#journal Biochemistry (1986) 25:3105-3108 !$#title Complete amino acid sequence of ubiquitin from the higher !1plant Avena sativa. !$#accession A02576 !'##molecule_type protein !'##residues 1-76 ##label VIE CLASSIFICATION #superfamily ubiquitin; ubiquitin homology KEYWORDS protein degradation FEATURE !$1-76 #domain ubiquitin homology #label UBH\ !$76 #cross-link isopeptide carboxyl end (Gly) (interchain !8to Lys N6-amino of other proteins) #status !8experimental SUMMARY #length 76 #molecular-weight 8525 #checksum 8480 SEQUENCE /// ENTRY UQSY #type fragment TITLE ubiquitin precursor - soybean (fragment) ALTERNATE_NAMES polyubiquitin ORGANISM #formal_name Glycine max #common_name soybean DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Aug-1996 ACCESSIONS S02222 REFERENCE S02222 !$#authors Fortin, M.G.; Purohit, S.K.; Verma, D.P.S. !$#journal Nucleic Acids Res. (1988) 16:11377 !$#title The primary structure of soybean (Glycine max) ubiquitin is !1identical to other plant ubiquitins. !$#cross-references MUID:89083578; PMID:2849766 !$#accession S02222 !'##molecule_type mRNA !'##residues 1-88 ##label FOR !'##cross-references EMBL:X13251 CLASSIFICATION #superfamily ubiquitin; ubiquitin homology KEYWORDS polyprotein; protein degradation FEATURE !$1-11 #product ubiquitin (fragment) #status predicted !8#label UBI1\ !$12-87 #product ubiquitin #status predicted #label UBI2\ !$12-87 #domain ubiquitin homology #label UBH SUMMARY #length 88 #checksum 2690 SEQUENCE /// ENTRY UQFS #type fragment TITLE ubiquitin precursor - common sunflower (fragment) ALTERNATE_NAMES polyubiquitin ORGANISM #formal_name Helianthus annuus #common_name common sunflower DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Aug-1996 ACCESSIONS S03599 REFERENCE S03599 !$#authors Binet, M.N.; Steinmetz, A.; Tessier, L.H. !$#journal Nucleic Acids Res. (1989) 17:2119 !$#title The primary structure of sunflower (Helianthus annuus) !1ubiquitin. !$#cross-references MUID:89183614; PMID:2538802 !$#accession S03599 !'##molecule_type mRNA !'##residues 1-410 ##label BIN !'##cross-references EMBL:X14333 CLASSIFICATION #superfamily ubiquitin; ubiquitin homology KEYWORDS polyprotein; protein degradation FEATURE !$1-29 #product ubiquitin (fragment) #status predicted !8#label UBI1\ !$30-105 #product ubiquitin #status predicted #label UBI2\ !$30-105 #domain ubiquitin homology #label UBH1\ !$106-181 #domain ubiquitin homology #label UBH2\ !$106-181 #product ubiquitin #status predicted #label UBI3\ !$182-257 #product ubiquitin #status predicted #label UBI4\ !$182-257 #domain ubiquitin homology #label UBH3\ !$258-333 #domain ubiquitin homology #label UBH4\ !$258-333 #product ubiquitin #status predicted #label UBI5\ !$334-409 #product ubiquitin #status predicted #label UBI6\ !$334-409 #domain ubiquitin homology #label UBH5 SUMMARY #length 410 #checksum 7309 SEQUENCE /// ENTRY UQUYSF #type fragment TITLE ubiquitin - fall armyworm (fragment) ORGANISM #formal_name Spodoptera frugiperda #common_name fall armyworm DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Aug-1996 ACCESSIONS B34813 REFERENCE A34813 !$#authors Guarino, L.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:409-413 !$#title Identification of a viral gene encoding a ubiquitin-like !1protein. !$#cross-references MUID:90115886; PMID:2153300 !$#accession B34813 !'##molecule_type DNA !'##residues 1-76 ##label GUA !'##cross-references GB:M30306 CLASSIFICATION #superfamily ubiquitin; ubiquitin homology KEYWORDS polyprotein; protein degradation FEATURE !$1-76 #product ubiquitin #status predicted #label UBT\ !$1-76 #domain ubiquitin homology #label UBH SUMMARY #length 76 #checksum 9575 SEQUENCE /// ENTRY UQUT #type complete TITLE ubiquitin - Trypanosoma brucei ALTERNATE_NAMES polyubiquitin ORGANISM #formal_name Trypanosoma brucei DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS A44981; S07998 REFERENCE A44981 !$#authors Wong, S.; Campbell, D.A. !$#journal Mol. Biochem. Parasitol. (1989) 37:147-150 !$#title A polyubiquitin gene from Trypanosoma brucei. !$#cross-references MUID:90136711; PMID:2559328 !$#accession A44981 !'##molecule_type DNA !'##residues 1-77 ##label WON !'##cross-references EMBL:X14554; NID:g10570; PIDN:CAA32691.1; !1PID:g10571 CLASSIFICATION #superfamily ubiquitin; ubiquitin homology KEYWORDS protein degradation FEATURE !$1-76 #product ubiquitin #status predicted #label MAT\ !$1-76 #domain ubiquitin homology #label UBH SUMMARY #length 77 #molecular-weight 8620 #checksum 9468 SEQUENCE /// ENTRY UQNVAC #type complete TITLE ubiquitin - Autographa californica nuclear polyhedrosis virus ORGANISM #formal_name Autographa californica nuclear polyhedrosis virus, AcMNPV DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 29-Oct-1999 ACCESSIONS A34813; E45355 REFERENCE A34813 !$#authors Guarino, L.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:409-413 !$#title Identification of a viral gene encoding a ubiquitin-like !1protein. !$#cross-references MUID:90115886; PMID:2153300 !$#accession A34813 !'##molecule_type DNA !'##residues 1-77 ##label GUA !'##cross-references GB:M30305; NID:g332488; PIDN:AAA46751.1; !1PID:g332489 REFERENCE A45355 !$#authors Guarino, L.A.; Smith, M.W. !$#journal Virology (1990) 179:1-8 !$#title Nucleotide sequence and characterization of the 39K gene !1region of Autographa californica nuclear polyhedrosis virus. !$#cross-references MUID:91021010; PMID:2219715 !$#accession E45355 !'##status preliminary !'##molecule_type DNA !'##residues 1-19,'A',21-77 ##label GU2 !'##cross-references GB:M37122; NID:g332383; PIDN:AAA46685.1; !1PID:g332388 CLASSIFICATION #superfamily ubiquitin; ubiquitin homology KEYWORDS late protein; protein degradation FEATURE !$1-76 #domain ubiquitin homology #label UBH SUMMARY #length 77 #molecular-weight 8711 #checksum 371 SEQUENCE /// ENTRY S29853 #type complete TITLE polyubiquitin 4 - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 08-Dec-1993 #sequence_revision 22-Apr-1995 #text_change 16-Jul-1999 ACCESSIONS S29853; I45965 REFERENCE S29853 !$#authors Wempe, F.; Scheit, K.H. !$#journal Biochim. Biophys. Acta (1993) 1172:209-211 !$#title Characterization of a full-length cDNA encoding a bovine !1four tandem-repeat ubiquitin. !$#cross-references MUID:93176814; PMID:8382528 !$#accession S29853 !'##molecule_type mRNA !'##residues 1-305 ##label WEM !'##cross-references EMBL:Z18245; NID:g644; PIDN:CAA79146.1; PID:g645 REFERENCE I45964 !$#authors Meyers, G.; Tautz, N.; Dubovi, E.J.; Thiel, H. !$#journal Virology (1991) 180:602-616 !$#title Viral cytopathogenicity correlated with integration of !1Ubiquitin-Coding sequences. !$#cross-references MUID:91111979; PMID:1846490 !$#accession I45965 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 142-305 ##label MEY !'##cross-references GB:M62429; NID:g163574; PIDN:AAA30720.1; !1PID:g163575 COMMENT See entry PIR:UQBO. CLASSIFICATION #superfamily polyubiquitin 4; ubiquitin homology KEYWORDS duplication; polyprotein; protein degradation FEATURE !$1-76 #product ubiquitin #status predicted #label UB1\ !$1-76 #domain ubiquitin homology #label UBH1\ !$77-152 #product ubiquitin #status predicted #label UB2\ !$77-152 #domain ubiquitin homology #label UBH2\ !$153-228 #product ubiquitin #status predicted #label UB3\ !$153-228 #domain ubiquitin homology #label UBH3\ !$229-304 #product ubiquitin #status predicted #label UB4\ !$229-304 #domain ubiquitin homology #label UBH4 SUMMARY #length 305 #molecular-weight 34368 #checksum 4998 SEQUENCE /// ENTRY I50437 #type complete TITLE polyubiquitin 4 - chicken ALTERNATE_NAMES ubiquitin I ORGANISM #formal_name Gallus gallus #common_name chicken DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS I50437; I50728 REFERENCE I50437 !$#authors Bond, U.; Schlesinger, M.J. !$#journal Mol. Cell. Biol. (1986) 6:4602-4610 !$#title The chicken ubiquitin gene contains a heat shock promoter !1and expresses an unstable mRNA in heat-shocked cells. !$#cross-references MUID:87089821; PMID:3025663 !$#accession I50437 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-305 ##label BON !'##cross-references GB:M14693; NID:g212848; PIDN:AAA49128.1; !1PID:g212849 REFERENCE I50438 !$#authors Bond, U.; Schlesinger, M.J. !$#journal Mol. Cell. Biol. (1985) 5:949-956 !$#title Ubiquitin is a heat shock protein in chicken embryo !1fibroblasts. !$#cross-references MUID:85213498; PMID:2987683 !$#accession I50728 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 149-270,'W',272-305 ##label BO2 !'##cross-references EMBL:X02650; NID:g63864; PID:g1334750 CLASSIFICATION #superfamily polyubiquitin 4; ubiquitin homology KEYWORDS nucleus; polyprotein; protein degradation FEATURE !$1-76 #product ubiquitin #status predicted #label UB1\ !$1-76 #domain ubiquitin homology #label UBH1\ !$77-152 #product ubiquitin #status predicted #label UB2\ !$77-152 #domain ubiquitin homology #label UBH2\ !$153-228 #product ubiquitin #status predicted #label UB3\ !$153-228 #domain ubiquitin homology #label UBH3\ !$229-304 #product ubiquitin #status predicted #label UB4\ !$229-304 #domain ubiquitin homology #label UBH4 SUMMARY #length 305 #molecular-weight 34368 #checksum 5685 SEQUENCE /// ENTRY S12583 #type complete TITLE polyubiquitin 4 - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S12583 REFERENCE S12583 !$#authors Finch, J.S.; Bonham, K.; Krieg, P.; Bowden, G.T. !$#journal Nucleic Acids Res. (1990) 18:1907 !$#title Murine polyubiquitin mRNA sequence. !$#cross-references MUID:90245601; PMID:2159627 !$#accession S12583 !'##molecule_type mRNA !'##residues 1-305 ##label FIN !'##cross-references EMBL:X51703; NID:g55117; PIDN:CAA35999.1; !1PID:g55118 !'##note the authors translated the codon CTC for residues 56, 132, 208, !1and 284 as Ala and they did not translate the codon TAT for !1residue 305 CLASSIFICATION #superfamily polyubiquitin 4; ubiquitin homology KEYWORDS nucleus; polyprotein; protein degradation FEATURE !$1-76 #product ubiquitin #status predicted #label UB1\ !$1-76 #domain ubiquitin homology #label UBH1\ !$77-152 #product ubiquitin #status predicted #label UB2\ !$77-152 #domain ubiquitin homology #label UBH2\ !$153-228 #product ubiquitin #status predicted #label UB3\ !$153-228 #domain ubiquitin homology #label UBH3\ !$229-304 #product ubiquitin #status predicted #label UB4\ !$229-304 #domain ubiquitin homology #label UBH4 SUMMARY #length 305 #molecular-weight 34368 #checksum 5685 SEQUENCE /// ENTRY S28426 #type complete TITLE polyubiquitin 4 - wild oat ORGANISM #formal_name Avena fatua #common_name wild oat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S28426 REFERENCE S28426 !$#authors Reynolds, G.J.; Hooley, R. !$#journal Plant Mol. Biol. (1992) 20:753-758 !$#title cDNA cloning of a tetraubiquitin gene, and expression of !1ubiquitin-containing transcripts, in aleurone layers of !1Avena fatua. !$#cross-references MUID:93081737; PMID:1333296 !$#accession S28426 !'##molecule_type mRNA !'##residues 1-305 ##label REY !'##cross-references EMBL:X69422; NID:g15988; PIDN:CAA49200.1; !1PID:g15989 CLASSIFICATION #superfamily polyubiquitin 4; ubiquitin homology KEYWORDS nucleus; polyprotein FEATURE !$1-76 #product ubiquitin #status predicted #label UB1\ !$1-76 #domain ubiquitin homology #label UBH1\ !$77-152 #product ubiquitin #status predicted #label UB2\ !$77-152 #domain ubiquitin homology #label UBH2\ !$153-228 #product ubiquitin #status predicted #label UB3\ !$153-228 #domain ubiquitin homology #label UBH3\ !$229-304 #product ubiquitin #status predicted #label UB4\ !$229-304 #domain ubiquitin homology #label UBH4 SUMMARY #length 305 #molecular-weight 34173 #checksum 2750 SEQUENCE /// ENTRY S49332 #type complete TITLE polyubiquitin 4 - common sunflower ALTERNATE_NAMES seed tetraubiquitin ORGANISM #formal_name Helianthus annuus #common_name common sunflower DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S49332 REFERENCE S49332 !$#authors Almoguera, C.; Coca, M.A.; Jordano, J. !$#submission submitted to the EMBL Data Library, July 1994 !$#description Differential accumulation of sunflower tetraubiquitin mRNAs !1during zygotic embryogenesis and developmental regulation of !1their heat-shock response. !$#accession S49332 !'##status preliminary !'##molecule_type mRNA !'##residues 1-305 ##label ALM !'##cross-references EMBL:Z34988; NID:g556687; PIDN:CAA84440.1; !1PID:g556688 CLASSIFICATION #superfamily polyubiquitin 4; ubiquitin homology KEYWORDS nucleus; polyprotein; protein degradation FEATURE !$1-76 #product ubiquitin #status predicted #label UB1\ !$1-76 #domain ubiquitin homology #label UBH1\ !$77-152 #product ubiquitin #status predicted #label UB2\ !$77-152 #domain ubiquitin homology #label UBH2\ !$153-228 #product ubiquitin #status predicted #label UB3\ !$153-228 #domain ubiquitin homology #label UBH3\ !$229-304 #product ubiquitin #status predicted #label UB4\ !$229-304 #domain ubiquitin homology #label UBH4 SUMMARY #length 305 #molecular-weight 34192 #checksum 2530 SEQUENCE /// ENTRY UQNC #type complete TITLE polyubiquitin 4 - Neurospora crassa ORGANISM #formal_name Neurospora crassa DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S05323 REFERENCE S05323 !$#authors Taccioli, G.E.; Grotewold, E.; Aisemberg, G.O.; Judewicz, !1N.D. !$#journal Nucleic Acids Res. (1989) 17:6153-6165 !$#title Ubiquitin expression in Neurospora crassa: cloning and !1sequencing of a polyubiquitin gene. !$#cross-references MUID:89366647; PMID:2549509 !$#accession S05323 !'##molecule_type DNA !'##residues 1-305 ##label TAC !'##cross-references EMBL:X13140; NID:g3087; PIDN:CAA31530.1; !1PID:g295930 GENETICS !$#introns 8/1 CLASSIFICATION #superfamily polyubiquitin 4; ubiquitin homology KEYWORDS polyprotein; protein degradation FEATURE !$1-76 #product ubiquitin #status predicted #label UB1\ !$1-76 #domain ubiquitin homology #label UBH1\ !$77-152 #product ubiquitin #status predicted #label UB2\ !$77-152 #domain ubiquitin homology #label UBH2\ !$153-228 #product ubiquitin #status predicted #label UB3\ !$153-228 #domain ubiquitin homology #label UBH3\ !$229-304 #product ubiquitin #status predicted #label UB4\ !$229-304 #domain ubiquitin homology #label UBH4 SUMMARY #length 305 #molecular-weight 34465 #checksum 7620 SEQUENCE /// ENTRY S55244 #type complete TITLE polyubiquitin 4 - Arabidopsis thaliana ALTERNATE_NAMES ubiquitin-like protein 9 ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S55244; S61069 REFERENCE S55242 !$#authors Callis, J.; Carpenter, T.; Sun, C.W.; Vierstra, R.D. !$#journal Genetics (1995) 139:921-939 !$#title Structure and evolution of genes encoding polyubiquitin and !1ubiquitin-like proteins in Arabidopsis thaliana ecotype !1Columbia. !$#cross-references MUID:95229071; PMID:7713442 !$#accession S55244 !'##molecule_type DNA !'##residues 1-320 ##label CAL !'##cross-references EMBL:L05365 !'##experimental_source ecotype Columbia REFERENCE S61069 !$#authors Callis, J.; Carpenter, T.; Sun, C.W.; Vierstra, R.D. !$#submission submitted to the EMBL Data Library, June 1995 !$#accession S61069 !'##molecule_type DNA !'##residues 1-76,'I',78-111,'V',113-212,'M',214-320 ##label CAF !'##cross-references EMBL:L05365 CLASSIFICATION #superfamily polyubiquitin 4; ubiquitin homology KEYWORDS nucleus; polyprotein; protein degradation FEATURE !$1-76 #product ubiquitin #status predicted #label UB1\ !$1-76 #domain ubiquitin homology #label UBH1\ !$77-152 #product ubiquitin #status predicted #label UB2\ !$77-152 #domain ubiquitin homology #label UBH2\ !$153-228 #product ubiquitin #status predicted #label UB3\ !$153-228 #domain ubiquitin homology #label UBH3\ !$229-305 #product ubiquitin #status predicted #label UB4\ !$229-305 #domain ubiquitin homology #label UBH4 SUMMARY #length 320 #molecular-weight 36052 #checksum 4495 SEQUENCE /// ENTRY UQMUM #type complete TITLE polyubiquitin 5 - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S01425 REFERENCE S01425 !$#authors Burke, T.J.; Callis, J.; Vierstra, R.D. !$#journal Mol. Gen. Genet. (1988) 213:435-443 !$#title Characterization of a polyubiquitin gene from Arabidopsis !1thaliana. !$#cross-references MUID:89039731; PMID:2460733 !$#accession S01425 !'##molecule_type DNA !'##residues 1-382 ##label BUR !'##cross-references EMBL:X12853; NID:g17677; PIDN:CAA31331.1; !1PID:g17678 GENETICS !$#gene UBQ4 CLASSIFICATION #superfamily polyubiquitin 5; ubiquitin homology KEYWORDS polyprotein; protein degradation FEATURE !$1-76 #product ubiquitin #status predicted #label UBI1\ !$1-76 #domain ubiquitin homology #label UBH1\ !$77-152 #product ubiquitin #status predicted #label UBI2\ !$77-152 #domain ubiquitin homology #label UBH2\ !$153-228 #product ubiquitin #status predicted #label UBI3\ !$153-228 #domain ubiquitin homology #label UBH3\ !$229-304 #product ubiquitin #status predicted #label UBI4\ !$229-304 #domain ubiquitin homology #label UBH4\ !$305-380 #product ubiquitin #status predicted #label UBI5\ !$305-380 #domain ubiquitin homology #label UBH5 SUMMARY #length 382 #molecular-weight 42786 #checksum 4926 SEQUENCE /// ENTRY UQPM #type complete TITLE polyubiquitin 5 - garden pea ORGANISM #formal_name Pisum sativum #common_name garden pea DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S06921 REFERENCE S06921 !$#authors Watts, F.Z.; Moore, A.L. !$#journal Nucleic Acids Res. (1989) 17:10100 !$#title Nucleotide sequence of a full length cDNA clone encoding a !1polyubiquitin gene from Pisum sativum. !$#accession S06921 !'##molecule_type mRNA !'##residues 1-381 ##label WAT !'##cross-references EMBL:X17020; NID:g20588; PIDN:CAA34886.1; !1PID:g20589 CLASSIFICATION #superfamily polyubiquitin 5; ubiquitin homology KEYWORDS polyprotein; protein degradation FEATURE !$1-76 #product ubiquitin #status predicted #label UBI1\ !$1-76 #domain ubiquitin homology #label UBH1\ !$77-152 #product ubiquitin #status predicted #label UBI2\ !$77-152 #domain ubiquitin homology #label UBH2\ !$153-228 #product ubiquitin #status predicted #label UBI3\ !$153-228 #domain ubiquitin homology #label UBH3\ !$229-304 #product ubiquitin #status predicted #label UBI4\ !$229-304 #domain ubiquitin homology #label UBH4\ !$305-380 #product ubiquitin #status predicted #label UBI5\ !$305-380 #domain ubiquitin homology #label UBH5 SUMMARY #length 381 #molecular-weight 42699 #checksum 1619 SEQUENCE /// ENTRY UQBY #type complete TITLE polyubiquitin 5 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein L0904; protein YLL039c; ubiquitin precursor UBI4 ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1987 #sequence_revision 11-Sep-1998 #text_change 20-Oct-2000 ACCESSIONS D29456; S64790; B22696; A22696 REFERENCE A29456 !$#authors Oezkaynak, E.; Finley, D.; Solomon, M.J.; Varshavsky, A. !$#journal EMBO J. (1987) 6:1429-1439 !$#title The yeast ubiquitin genes: a family of natural gene fusions. !$#cross-references MUID:87275838; PMID:3038523 !$#accession D29456 !'##molecule_type DNA !'##residues 1-381 ##label OEZ !'##cross-references EMBL:X05731; NID:g4733; PIDN:CAA29198.1; PID:g4734 REFERENCE S64775 !$#authors Duesterhoeft, A.; Floeth, M.; Heuss-Neitzel, D.; Hilbert, !1H.; Moestl, D. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64790 !'##molecule_type DNA !'##residues 1-381 ##label DUE !'##cross-references EMBL:Z73144; NID:g1360230; PIDN:CAA97489.1; !1PID:g1360231; GSPDB:GN00012; MIPS:YLL039c !'##note experimental_source strain S288C REFERENCE A22696 !$#authors Oezkaynak, E.; Finley, D.; Varshavsky, A. !$#journal Nature (1984) 312:663-666 !$#title The yeast ubiquitin gene: head-to-tail repeats encoding a !1polyubiquitin precursor protein. !$#cross-references MUID:85061630; PMID:6095120 !$#accession B22696 !'##molecule_type DNA !'##residues 44-81,'N',83-123;191-351,'N',353-381 ##label OEY !'##cross-references GB:X01473; GB:X01474 !'##note authors translated the codon AAC for residue 82 as Lys, and AAC !1for residue 352 as Lys GENETICS !$#gene SGD:UBI4; MIPS:YLL039c !'##cross-references SGD:S0003962; MIPS:YLL039c !$#map_position 12L CLASSIFICATION #superfamily polyubiquitin 5; ubiquitin homology KEYWORDS nucleus; polyprotein; protein degradation; tandem repeat; !1thiolester bond FEATURE !$1-76 #product ubiquitin #status predicted #label UBI1\ !$1-76 #domain ubiquitin homology #label UBH1\ !$77-152 #product ubiquitin #status predicted #label UBI2\ !$77-152 #domain ubiquitin homology #label UBH2\ !$153-228 #product ubiquitin #status predicted #label UBI3\ !$153-228 #domain ubiquitin homology #label UBH3\ !$229-304 #product ubiquitin #status predicted #label UBI4\ !$229-304 #domain ubiquitin homology #label UBH4\ !$305-380 #product ubiquitin #status predicted #label UBI5\ !$305-380 #domain ubiquitin homology #label UBH5\ !$48 #cross-link isopeptide (Lys) (interchain to Gly-76 of !8mature ubiquitin) #status predicted\ !$76 #cross-link isopeptide carboxyl end (Gly) (interchain !8to Lys N6-amino of other proteins) #status predicted\ !$76 #cross-link thiolester carboxyl end (Gly) (interchain !8to Cys-88 of conjugating enzyme) #status predicted\ !$124 #cross-link isopeptide (Lys) (interchain to Gly-76 of !8mature ubiquitin) #status predicted\ !$152 #cross-link thiolester carboxyl end (Gly) (interchain !8to Cys-88 of conjugating enzyme) #status predicted\ !$152 #cross-link isopeptide carboxyl end (Gly) (interchain !8to Lys N6-amino of other proteins) #status predicted\ !$200 #cross-link isopeptide (Lys) (interchain to Gly-76 of !8mature ubiquitin) #status predicted\ !$228 #cross-link isopeptide carboxyl end (Gly) (interchain !8to Lys N6-amino of other proteins) #status predicted\ !$228 #cross-link thiolester carboxyl end (Gly) (interchain !8to Cys-88 of conjugating enzyme) #status predicted\ !$304 #cross-link isopeptide carboxyl end (Gly) (interchain !8to Lys N6-amino of other proteins) #status predicted\ !$304 #cross-link thiolester carboxyl end (Gly) (interchain !8to Cys-88 of conjugating enzyme) #status predicted\ !$352 #cross-link isopeptide (Lys) (interchain to Gly-76 of !8mature ubiquitin) #status predicted\ !$380 #cross-link isopeptide carboxyl end (Gly) (interchain !8to Lys N6-amino of other proteins) #status predicted\ !$380 #cross-link thiolester carboxyl end (Gly) (interchain !8to Cys-88 of conjugating enzyme) #status predicted SUMMARY #length 381 #molecular-weight 42826 #checksum 8213 SEQUENCE /// ENTRY S20925 #type complete TITLE polyubiquitin - maize ORGANISM #formal_name Zea mays #common_name maize DATE 30-Sep-1993 #sequence_revision 11-Apr-1997 #text_change 22-Jun-1999 ACCESSIONS S20925; S20926; S04863 REFERENCE S20925 !$#authors Christensen, A.H.; Sharrock, R.A.; Quail, P.H. !$#journal Plant Mol. Biol. (1992) 18:675-689 !$#title Maize polyubiquitin genes: structure, thermal perturbation !1of expression and transcript splicing, and promoter activity !1following transfer to protoplasts by electroporation. !$#cross-references MUID:92216044; PMID:1313711 !$#accession S20925 !'##molecule_type DNA !'##residues 1-533 ##label CHR1 !'##cross-references EMBL:S94464; NID:g248336; PIDN:AAB21993.1; !1PID:g248337 !'##genetics UBI1 !$#accession S20926 !'##molecule_type DNA !'##residues 1-533 ##label CHR2 !'##cross-references EMBL:S94466; NID:g248338; PIDN:AAB21994.1; !1PID:g248339 !'##genetics UBI2 REFERENCE S04863 !$#authors Christensen, A.H.; Quail, P.H. !$#journal Plant Mol. Biol. (1989) 12:619-632 !$#title Sequence analysis and transcriptional regulation by heat !1shock of polyubiquitin transcripts from maize. !$#accession S04863 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 'R',263-533 ##label CHR3 GENETICS UBI1 !$#gene Ubi-1 GENETICS UBI2 !$#gene Ubi-2 CLASSIFICATION #superfamily polyubiquitin 7; ubiquitin homology KEYWORDS nucleus; polyprotein; protein degradation FEATURE !$1-76 #product ubiquitin #status predicted #label UB1\ !$1-76 #domain ubiquitin homology #label UBH1\ !$77-152 #product ubiquitin #status predicted #label UB2\ !$77-152 #domain ubiquitin homology #label UBH2\ !$153-228 #product ubiquitin #status predicted #label UB3\ !$153-228 #domain ubiquitin homology #label UBH3\ !$229-304 #product ubiquitin #status predicted #label UB4\ !$229-304 #domain ubiquitin homology #label UBH4\ !$305-380 #product ubiquitin #status predicted #label UB5\ !$305-380 #domain ubiquitin homology #label UBH5\ !$381-456 #product ubiquitin #status predicted #label UB6\ !$381-456 #domain ubiquitin homology #label UBH6\ !$457-532 #product ubiquitin #status predicted #label UB7\ !$457-532 #domain ubiquitin homology #label UBH7 SUMMARY #length 533 #molecular-weight 59693 #checksum 5400 SEQUENCE /// ENTRY UQHUB #type complete TITLE polyubiquitin 3 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 05-Jun-1988 #sequence_revision 28-Apr-1995 #text_change 21-Jul-2000 ACCESSIONS A26437 REFERENCE A26437 !$#authors Baker, R.T.; Board, P.G. !$#journal Nucleic Acids Res. (1987) 15:443-463 !$#title The human ubiquitin gene family: structure of a gene and !1pseudogenes from the Ub B subfamily. !$#cross-references MUID:87146371; PMID:3029682 !$#accession A26437 !'##molecule_type DNA !'##residues 1-229 ##label BAK !'##cross-references EMBL:X04803; GB:U49869; NID:g6647297; !1PIDN:CAA28495.1; PID:g6647298 COMMENT See entry PIR:UQHU. GENETICS !$#gene GDB:UBB !'##cross-references GDB:120478; OMIM:191339 !$#map_position 17p12-17p11.2 CLASSIFICATION #superfamily polyubiquitin 3; ubiquitin homology KEYWORDS duplication; polyprotein; protein degradation FEATURE !$1-76 #domain ubiquitin homology #label UBH1\ !$77-152 #domain ubiquitin homology #label UBH2\ !$153-228 #domain ubiquitin homology #label UBH3 SUMMARY #length 229 #molecular-weight 25761 #checksum 4499 SEQUENCE /// ENTRY A31560 #type complete TITLE polyuciquitin - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A31560 REFERENCE A31560 !$#authors Lee, H.; Simon, J.A.; Lis, J.T. !$#journal Mol. Cell. Biol. (1988) 8:4727-4735 !$#title Structure and expression of ubiquitin genes of Drosophila !1melanogaster. !$#cross-references MUID:89096844; PMID:2463465 !$#accession A31560 !'##molecule_type DNA !'##residues 1-231 ##label LEE !'##cross-references GB:M22428; NID:g158752; PIDN:AAA28997.1; !1PID:g158753 GENETICS !$#gene FlyBase:Ubi-p63E !'##cross-references FlyBase:FBgn0003943 CLASSIFICATION #superfamily polyubiquitin 3; ubiquitin homology KEYWORDS duplication; nucleus; polyprotein; protein degradation FEATURE !$1-76 #domain ubiquitin homology #label UBH1\ !$77-152 #domain ubiquitin homology #label UBH2\ !$153-228 #domain ubiquitin homology #label UBH3 SUMMARY #length 231 #molecular-weight 25971 #checksum 4862 SEQUENCE /// ENTRY S13928 #type complete TITLE ubiquitin precursor - chicken ALTERNATE_NAMES polyubiquitin ORGANISM #formal_name Gallus gallus #common_name chicken DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S13928 REFERENCE S13928 !$#authors Mezquita, J.; Mezquita, C. !$#journal FEBS Lett. (1991) 279:69-72 !$#title Characterization of a chicken polyubiquitin gene !1preferentially expressed during spermatogenesis. !$#cross-references MUID:91138765; PMID:1704859 !$#accession S13928 !'##status preliminary !'##molecule_type DNA !'##residues 1-229 ##label MEZ CLASSIFICATION #superfamily polyubiquitin 3; ubiquitin homology KEYWORDS duplication; polyprotein; protein degradation FEATURE !$1-76 #domain ubiquitin homology #label UBH1\ !$77-152 #domain ubiquitin homology #label UBH2\ !$153-228 #domain ubiquitin homology #label UBH3 SUMMARY #length 229 #molecular-weight 25772 #checksum 4510 SEQUENCE /// ENTRY UQJNI #type complete TITLE ubiquitin precursor - Phytophthora infestans ORGANISM #formal_name Phytophthora infestans #common_name potato late blight agent DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 22-Jun-1999 ACCESSIONS S17740; S14579 REFERENCE S17740 !$#authors Pieterse, C.M.J.; Risseeuw, E.P.; Davidse, L.C. !$#journal Plant Mol. Biol. (1991) 17:799-811 !$#title An in planta induced gene of Phytophthora infestans codes !1for ubiquitin. !$#cross-references MUID:92003691; PMID:1655113 !$#accession S17740 !'##molecule_type DNA !'##residues 1-229 ##label PIE !'##cross-references EMBL:X55717; NID:g3175; PIDN:CAA39250.1; PID:g3176 GENETICS !$#gene ubi3R CLASSIFICATION #superfamily polyubiquitin 3; ubiquitin homology KEYWORDS polyprotein; protein degradation FEATURE !$1-76 #product ubiquitin #status predicted #label UBI1\ !$1-76 #domain ubiquitin homology #label UBH1\ !$77-152 #product ubiquitin #status predicted #label UBI2\ !$77-152 #domain ubiquitin homology #label UBH2\ !$153-228 #product ubiquitin #status predicted #label UBI3\ !$153-228 #domain ubiquitin homology #label UBH3 SUMMARY #length 229 #molecular-weight 25817 #checksum 5611 SEQUENCE /// ENTRY A56582 #type complete TITLE polyubiquitin - Euplotes eurystomus ORGANISM #formal_name Euplotes eurystomus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 07-Dec-1999 ACCESSIONS A56582 REFERENCE A56582 !$#authors Hauser, L.J.; Roberson, A.E.; Olins, D.E. !$#journal Chromosoma (1991) 100:386-394 !$#title Structure of the macronuclear polyubiquitin gene in !1Euplotes. !$#cross-references MUID:91372022; PMID:1654239 !$#accession A56582 !'##status preliminary !'##molecule_type DNA !'##residues 1-229 ##label HAU !'##cross-references GB:M57231; NID:g159037; PIDN:AAA62225.1; !1PID:g159038 !'##experimental_source macronucleus !'##note authors translated the codon AAG for residue 185 as Leu GENETICS !$#genetic_code SGC9 CLASSIFICATION #superfamily polyubiquitin 3; ubiquitin homology KEYWORDS duplication; polyprotein; protein degradation FEATURE !$1-76 #domain ubiquitin homology #label UBH1\ !$77-152 #domain ubiquitin homology #label UBH2\ !$153-228 #domain ubiquitin homology #label UBH3 SUMMARY #length 229 #molecular-weight 25856 #checksum 3983 SEQUENCE /// ENTRY UQHUC #type complete TITLE polyubiquitin 9 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1988 #sequence_revision 28-Apr-1995 #text_change 19-Jan-2001 ACCESSIONS A22005; I52220; T17283; JE0190; A59312 REFERENCE A22005 !$#authors Wiborg, O.; Pedersen, M.S.; Wind, A.; Berglund, L.E.; !1Marcker, K.A.; Vuust, J. !$#journal EMBO J. (1985) 4:755-759 !$#title The human ubiquitin multigene family: some genes contain !1multiple directly repeated ubiquitin coding sequences. !$#cross-references MUID:85230546; PMID:2988935 !$#accession A22005 !'##molecule_type DNA !'##residues 1-685 ##label WIB !'##cross-references GB:M26880; NID:g340067; PIDN:AAA36789.1; !1PID:g340068 REFERENCE I52220 !$#authors Einspanier, R.; Sharma, H.S.; Scheit, K.H. !$#journal Biochem. Biophys. Res. Commun. (1987) 147:581-587 !$#title Cloning and sequence analysis of a cDNA encoding !1poly-ubiquitin in human ovarian granulosa cells. !$#cross-references MUID:87326412; PMID:2820408 !$#accession I52220 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 417-685 ##label EIN !'##cross-references GB:M17597; NID:g340057; PIDN:AAA36787.1; !1PID:g340058 REFERENCE Z18723 !$#authors Poustka, A.; Klein, M.; Mewes, H.W.; Gassenhuber, J.; !1Wiemann, S. !$#submission submitted to the Protein Sequence Database, September 1999 !$#accession T17283 !'##molecule_type mRNA !'##residues 447-685 ##label POU !'##cross-references EMBL:AL117514; NID:g5912027; PIDN:CAB55973.1; !1PID:g5912028 !'##experimental_source adult testis; clone DKFZp434K0435 REFERENCE JE0190 !$#authors Kim, N.S.; Yamaguchi, T.; Sekine, S.; Saeki, M.; Iwamuro, !1S.; Kato, S. !$#journal J. Biochem. (1998) 124:35-39 !$#title Cloning of human polyubiquitin cDNAs and a ubiquitin-binding !1assay involving its in vitro translation product. !$#cross-references MUID:98309846; PMID:9644242 !$#accession JE0190 !'##molecule_type mRNA !'##residues 609-685 ##label KIM !'##cross-references DDBJ:AB009010; NID:g2647407 !'##note the sequence is revised in GenBank entry AB009010, release !1113.0 REFERENCE A59312 !$#authors Kato, S. !$#submission submitted to GenBank, November 1997 !$#accession A59312 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-685 ##label KAT !'##cross-references GB:AB009010; NID:g2647407; PIDN:BAA23632.1; !1PID:g2647408 !'##experimental_source clone HP00184; gene UbC2; note polymorphic !1variant; replace a COMMENT See PIR:UQHU. GENETICS !$#gene GDB:UBC; UbC1 !'##cross-references GDB:128730; OMIM:191340 !$#map_position 12q24.3-12q24.3 CLASSIFICATION #superfamily polyubiquitin 9; ubiquitin homology KEYWORDS duplication; polyprotein; protein degradation FEATURE !$1-76 #product ubiquitin #status predicted #label UB1\ !$1-76 #domain ubiquitin homology #label UBH1\ !$77-152 #product ubiquitin #status predicted #label UB2\ !$77-152 #domain ubiquitin homology #label UBH2\ !$153-228 #product ubiquitin #status predicted #label UB3\ !$153-228 #domain ubiquitin homology #label UBH3\ !$229-304 #product ubiquitin #status predicted #label UB4\ !$229-304 #domain ubiquitin homology #label UBH4\ !$305-380 #product ubiquitin #status predicted #label UB5\ !$305-380 #domain ubiquitin homology #label UBH5\ !$381-456 #product ubiquitin #status predicted #label UB6\ !$381-456 #domain ubiquitin homology #label UBH6\ !$457-532 #product ubiquitin #status predicted #label UB7\ !$457-532 #domain ubiquitin homology #label UBH7\ !$533-608 #product ubiquitin #status predicted #label UB8\ !$533-608 #domain ubiquitin homology #label UBH8\ !$609-684 #product ubiquitin #status predicted #label UB9\ !$609-684 #domain ubiquitin homology #label UBH9 SUMMARY #length 685 #molecular-weight 77038 #checksum 3382 SEQUENCE /// ENTRY UQHUR #type complete TITLE ubiquitin / ribosomal protein CEP52 - human ALTERNATE_NAMES ubiquitin fusion protein ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1990 #sequence_revision 28-Apr-1995 #text_change 22-Jun-1999 ACCESSIONS S34428; S34429; S34430; S11247 REFERENCE S34428 !$#authors Baker, R.T.; Board, P.G. !$#journal Nucleic Acids Res. (1991) 19:1035-1040 !$#title The human ubiquitin-52 amino acid fusion protein gene shares !1several structural features with mammalian ribosomal protein !1genes. !$#cross-references MUID:91212181; PMID:1850507 !$#accession S34428 !'##molecule_type DNA !'##residues 1-128 ##label BAK !'##cross-references EMBL:X56997; NID:g37566; PIDN:CAA40312.1; !1PID:g37567 !$#accession S34429 !'##molecule_type mRNA !'##residues 1-128 ##label BAF !'##cross-references EMBL:X56998; NID:g37564; PIDN:CAA40313.1; !1PID:g37565 !$#accession S34430 !'##molecule_type mRNA !'##residues 1-128 ##label BAW !'##cross-references EMBL:X56999; NID:g37568; PIDN:CAA40314.1; !1PID:g37569 REFERENCE S11247 !$#authors Salvesen, G.; Lloyd, C.; Farley, D. !$#journal Nucleic Acids Res. (1987) 15:5485 !$#title cDNA encoding a human homolog of yeast ubiquitin 1. !$#cross-references MUID:87260019; PMID:3037496 !$#accession S11247 !'##molecule_type mRNA !'##residues 40-128 ##label SAL !'##cross-references EMBL:Y00361; NID:g37575; PIDN:CAA68439.1; !1PID:g825728 !'##note the translation of codon 61 is not shown in the figure GENETICS !$#gene GDB:UBA52 !'##cross-references GDB:133775; OMIM:191321 !$#map_position 19p13.1-19p12 !$#introns 35/1; 64/1; 98/2 !$#note the first intron occurs before the initiator codon CLASSIFICATION #superfamily ubiquitin/ribosomal protein CEP52; ribosomal !1protein CEP52 homology; ubiquitin homology KEYWORDS protein biosynthesis; protein degradation; ribosome; RNA !1binding; zinc finger FEATURE !$1-76 #product ubiquitin #status predicted #label MAT1\ !$1-76 #domain ubiquitin homology #label UBH\ !$77-128 #product ribosomal protein CEP52 #status predicted !8#label MAT2\ !$77-128 #domain ribosomal protein CEP52 homology #label CPH\ !$96-115 #region zinc finger CCCC motif\ !$122-128 #region nuclear location signal SUMMARY #length 128 #molecular-weight 14728 #checksum 8544 SEQUENCE /// ENTRY I65237 #type complete TITLE ubiquitin / ribosomal protein L40, cytosolic [validated] - rat ALTERNATE_NAMES ubiquitin / ribosomal protein CEP52; ubiquitin fusion protein CONTAINS ribosomal protein L40; ubiquitin ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 21-Jul-2000 ACCESSIONS I65237; S66575 REFERENCE I52328 !$#authors Chan, Y.L.; Suzuki, K.; Wool, I.G. !$#journal Biochem. Biophys. Res. Commun. (1995) 215:682-690 !$#title The Carboxyl extensions of rat ubiquitin fusion proteins are !1ribosomal proteins S27a and L40. !$#cross-references MUID:96011832; PMID:7488009 !$#accession I65237 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-128 ##label RES !'##cross-references EMBL:X82636; NID:g1050757; PIDN:CAA57958.1; !1PID:g1050758 !'##note part of this sequence was confirmed by protein sequencing !'##note the proteins are designated ubiquitin and ribosomal protein L40 REFERENCE S66575 !$#authors Redman, K.L.; Burris, G.W. !$#journal Biochem. J. (1996) 315:315-321 !$#title The cDNA for the ubiquitin-52-amino-acid fusion protein from !1rat encodes a previously unidentified 60 S ribosomal subunit !1protein. !$#cross-references MUID:96207597; PMID:8670124 !$#accession S66575 !'##molecule_type mRNA !'##residues 1-52 ##label RED !'##cross-references EMBL:U25064; NID:g973177; PIDN:AAC52495.1; !1PID:g973178 CLASSIFICATION #superfamily ubiquitin/ribosomal protein CEP52; ribosomal !1protein CEP52 homology; ubiquitin homology KEYWORDS protein biosynthesis; ribosome; zinc finger FEATURE !$1-76 #product ubiquitin #status experimental #label MAT1\ !$1-76 #domain ubiquitin homology #label UBH\ !$77-128 #product ribosomal protein L40 #status experimental !8#label MAT2\ !$77-128 #domain ribosomal protein CEP52 homology #label CPH SUMMARY #length 128 #molecular-weight 14728 #checksum 8544 SEQUENCE /// ENTRY UQDOR #type complete TITLE ubiquitin / ribosomal protein CEP52 - slime mold (Dictyostelium discoideum) ALTERNATE_NAMES ubiquitin fusion protein ORGANISM #formal_name Dictyostelium discoideum DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S00357; A25863 REFERENCE S00357 !$#authors Mueller-Taubenberger, A.; Westphal, M.; Jaeger, E.; Noegel, !1A.; Gerisch, G. !$#journal FEBS Lett. (1988) 229:273-278 !$#title Complete cDNA sequence of a Dictyostelium ubiquitin with a !1carboxy-terminal tail and identification of the protein !1using an anti-peptide antibody. !$#cross-references MUID:88152253; PMID:2831095 !$#accession S00357 !'##molecule_type mRNA !'##residues 1-128 ##label MUE !'##cross-references EMBL:X07210; NID:g7381; PIDN:CAA30183.1; PID:g7382 !'##experimental_source strain AX2-214 GENETICS !$#gene DUB1 CLASSIFICATION #superfamily ubiquitin/ribosomal protein CEP52; ribosomal !1protein CEP52 homology; ubiquitin homology KEYWORDS DNA binding; protein biosynthesis; protein degradation; !1ribosome; zinc finger FEATURE !$1-76 #product ubiquitin #status predicted #label UBI\ !$1-76 #domain ubiquitin homology #label UBH\ !$77-128 #product ribosomal protein CEP52 #status predicted !8#label RIB\ !$77-128 #domain ribosomal protein CEP52 homology #label CPH\ !$95-114 #region zinc finger CCCC motif\ !$121-128 #region nuclear location signal SUMMARY #length 128 #molecular-weight 14671 #checksum 7483 SEQUENCE /// ENTRY UQKM #type complete TITLE ubiquitin / ribosomal protein CEP52 - Chlamydomonas reinhardtii ALTERNATE_NAMES ubiquitin fusion protein ORGANISM #formal_name Chlamydomonas reinhardtii DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 01-Dec-2000 ACCESSIONS S06598; S19543; S21687 REFERENCE S06598 !$#authors Callis, J.; Pollmann, L.; Shanklin, J.; Wettern, M.; !1Vierstra, R.D. !$#journal Nucleic Acids Res. (1989) 17:8377 !$#title Sequence of a cDNA from Chlamydomonas reinhardii encoding a !1ubiquitin 52 amino acid extension protein. !$#cross-references MUID:90045969; PMID:2554258 !$#accession S06598 !'##molecule_type mRNA !'##residues 1-128 ##label CAL !'##cross-references EMBL:X15427; NID:g18245; PIDN:CAA33466.1; !1PID:g18246 REFERENCE S19543 !$#authors Pollmann, L.; von Kampen, J.; Wettern, M. !$#journal Eur. J. Biochem. (1991) 202:197-204 !$#title Ubiquitin in a lower plant. Characterization of !1ubiquitin-encoding DNA and RNA from Chlamydomonas !1reinhardii. !$#cross-references MUID:92037644; PMID:1657605 !$#accession S19543 !'##molecule_type mRNA !'##residues 1-128 ##label POL !'##cross-references GB:X60826; GB:S65065; NID:g18243; PIDN:CAA43216.1; !1PID:g18244 REFERENCE S21687 !$#authors Shimogawara, K.; Muto, S. !$#journal Arch. Biochem. Biophys. (1992) 294:193-199 !$#title Purification of Chlamydomonas 28-kDa ubiquitinated protein !1and its identification as ubiquitinated histone H2B. !$#cross-references MUID:92198009; PMID:1312804 !$#accession S21687 !'##molecule_type protein !'##residues 1-64,'XX',67-70;75-76 ##label SHI !'##experimental_source strain CW-15 CLASSIFICATION #superfamily ubiquitin/ribosomal protein CEP52; ribosomal !1protein CEP52 homology; ubiquitin homology KEYWORDS DNA binding; protein biosynthesis; protein degradation; !1ribosome; zinc finger FEATURE !$1-76 #product ubiquitin #status experimental #label UBI\ !$1-76 #domain ubiquitin homology #label UBH\ !$77-128 #product ribosomal protein CEP52 #status predicted !8#label RIB\ !$77-128 #domain ribosomal protein CEP52 homology #label CPH\ !$96-115 #region zinc finger CCCC motif\ !$122-128 #region nuclear location signal\ !$76 #cross-link isopeptide carboxyl end (Gly) (interchain !8to Lys N6-amino of other proteins) #status !8experimental SUMMARY #length 128 #molecular-weight 14700 #checksum 7441 SEQUENCE /// ENTRY UQUTRC #type complete TITLE polyubiquitin / ribosomal protein CEP52 - Trypanosoma cruzi ALTERNATE_NAMES ubiquitin fusion protein ORGANISM #formal_name Trypanosoma cruzi DATE 31-Dec-1990 #sequence_revision 12-Apr-1996 #text_change 22-Jun-1999 ACCESSIONS A31115; S00484; A37581; S20558 REFERENCE A31115 !$#authors Kirchhoff, L.V.; Kim, K.S.; Engman, D.M.; Donelson, J.E. !$#journal J. Biol. Chem. (1988) 263:12698-12704 !$#title Ubiquitin genes in trypanosomatidae. !$#cross-references MUID:88315072; PMID:2457589 !$#accession A31115 !'##molecule_type mRNA !'##residues 1-356 ##label KIR !'##cross-references GB:J03945; NID:g162336; PIDN:AAA30271.1; !1PID:g162337 REFERENCE S00484 !$#authors Swindle, J.; Ajioka, J.; Eisen, H.; Sanwal, B.; Jacquemot, !1C.; Browder, Z.; Buck, G. !$#journal EMBO J. (1988) 7:1121-1127 !$#title The genomic organization and transcription of the ubiquitin !1genes of Trypanosoma cruzi. !$#cross-references MUID:88296415; PMID:2841110 !$#accession S00484 !'##molecule_type DNA !'##residues 229-356 ##label SWI !'##cross-references EMBL:X07451; NID:g10672; PIDN:CAA30333.1; !1PID:g10673 !$#accession A37581 !'##molecule_type mRNA !'##residues 229-356 ##label SWI2 !'##cross-references EMBL:X07452; NID:g10675; PIDN:CAA30335.1; !1PID:g10676 GENETICS !$#gene FUS1 CLASSIFICATION #superfamily polyubiquitin/ribosomal protein CEP52; !1ribosomal protein CEP52 homology; ubiquitin homology KEYWORDS DNA binding; nucleus; protein biosynthesis; protein !1degradation; ribosome; zinc finger FEATURE !$1-76 #product ubiquitin #status predicted #label UBI\ !$1-76 #domain ubiquitin homology #label UBH1\ !$77-152 #product ubiquitin #status predicted #label UB2\ !$77-152 #domain ubiquitin homology #label UBH2\ !$153-228 #product ubiquitin #status predicted #label UB3\ !$153-228 #domain ubiquitin homology #label UBH3\ !$229-304 #product ubiquitin #status predicted #label UB4\ !$229-304 #domain ubiquitin homology #label UBH4\ !$305-356 #product ribosomal protein CEP52 #status predicted !8#label RIB\ !$305-356 #domain ribosomal protein CEP52 homology #label CPH\ !$324-343 #region zinc finger CCCC motif\ !$350-356 #region nuclear location signal SUMMARY #length 356 #molecular-weight 40130 #checksum 8829 SEQUENCE /// ENTRY UQHUR7 #type complete TITLE ubiquitin / ribosomal protein S27a, cytosolic [validated] - human ALTERNATE_NAMES platelet activity suppressive lymphokine; ubiquitin carboxyl extension protein HUBCEP80 ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 21-Jul-2000 ACCESSIONS A22632; A49030; A56872; S68912; JC7257 REFERENCE A22632 !$#authors Lund, P.K.; Moats-Staats, B.M.; Simmons, J.G.; Hoyt, E.; !1D'Ercole, A.J.; Martin, F.; Van Wyk, J.J. !$#journal J. Biol. Chem. (1985) 260:7609-7613 !$#title Nucleotide sequence analysis of a cDNA encoding human !1ubiquitin reveals that ubiquitin is synthesized as a !1precursor. !$#cross-references MUID:85207809; PMID:2581967 !$#accession A22632 !'##molecule_type mRNA !'##residues 1-156 ##label LUN !'##cross-references GB:M10939 REFERENCE A49030 !$#authors Pancre, V.; Pierce, R.J.; Fournier, F.; Mehtali, M.; !1Delanoye, A.; Capron, A.; Auriault, C. !$#journal Eur. J. Immunol. (1991) 21:2735-2741 !$#title Effect of ubiquitin on platelet functions: possible identity !1with platelet activity suppressive lymphokine (PASL). !$#cross-references MUID:92037818; PMID:1657614 !$#accession A49030 !'##molecule_type mRNA !'##residues 1-156 ##label PAN !'##cross-references GB:X63237; NID:g37570; PIDN:CAA44911.1; PID:g37571 !'##experimental_source Jurkat cell line !'##note sequence extracted from NCBI backbone (NCBIN:63925, !1NCBIP:63927) REFERENCE A56872 !$#authors Adams, S.M.; Sharp, M.G.; Walker, R.A.; Brammar, W.J.; !1Varley, J.M. !$#journal Br. J. Cancer (1992) 65:65-71 !$#title Differential expression of translation-associated genes in !1benign and malignant human breast tumours. !$#cross-references MUID:92126503; PMID:1370760 !$#accession A56872 !'##status preliminary !'##molecule_type mRNA !'##residues 1-156 ##label ADA !'##cross-references GB:S79522; NID:g243887; PIDN:AAB21188.1; !1PID:g243888 !'##note sequence extracted from NCBI backbone (NCBIN:79522, !1NCBIP:79525) REFERENCE S68911 !$#authors Vladimirov, S.N.; Ivanov, A.V.; Karpova, G.G.; Musolyamov, !1A.K.; Egorov, T.A.; Thiede, B.; Wittmann-Liebold, B.; Otto, !1A. !$#journal Eur. J. Biochem. (1996) 239:144-149 !$#title Characterization of the human small-ribosomal-subunit !1proteins by N-terminal and internal sequencing, and mass !1spectrometry. !$#cross-references MUID:96305378; PMID:8706699 !$#accession S68912 !'##molecule_type protein !'##residues 77-92,'XXXX',97-98 ##label VLA REFERENCE JC7257 !$#authors Kirschner, L.S.; Stratakis, C.A. !$#journal Biochem. Biophys. Res. Commun. (2000) 270:1106-1110 !$#title Structure of the human ubiquitin fusion gene Uba80(RPS27a) !1and one of its pseudogenes. !$#accession JC7257 !'##status preliminary !'##molecule_type DNA !'##residues 1-156 ##label KIR COMMENT See entry PIR:UQHU. GENETICS !$#gene UbA80 CLASSIFICATION #superfamily ubiquitin / rat ribosomal protein S27a; !1ribosomal protein S27a homology; ubiquitin homology KEYWORDS protein biosynthesis; protein degradation; ribosome FEATURE !$1-76 #product ubiquitin #status predicted #label MAT1\ !$1-76 #domain ubiquitin homology #label UBH\ !$77-156 #product ribosomal protein S27a #status experimental !8#label MAT2\ !$101-151 #domain ribosomal protein S27a homology #label RIB SUMMARY #length 156 #molecular-weight 17965 #checksum 9250 SEQUENCE /// ENTRY I52328 #type complete TITLE ubiquitin / ribosomal protein S27a, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 28-Jul-2000 ACCESSIONS I52328 REFERENCE I52328 !$#authors Chan, Y.L.; Suzuki, K.; Wool, I.G. !$#journal Biochem. Biophys. Res. Commun. (1995) 215:682-690 !$#title The Carboxyl extensions of rat ubiquitin fusion proteins are !1ribosomal proteins S27a and L40. !$#cross-references MUID:96011832; PMID:7488009 !$#accession I52328 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-156 ##label RES !'##cross-references EMBL:X81839; NID:g1050755; PIDN:CAA57432.1; !1PID:g1050756 !'##note the proteins are designated as ubiquitin and ribosomal protein !1S27a; ribosomal protein S27a identified by comigration !1analysis after in vitro translation CLASSIFICATION #superfamily ubiquitin / rat ribosomal protein S27a; !1ribosomal protein S27a homology; ubiquitin homology KEYWORDS protein biosynthesis; ribosome; zinc finger FEATURE !$1-76 #product ubiquitin #status predicted #label MAT1\ !$1-76 #domain ubiquitin homology #label UBH\ !$77-156 #product ribosomal protein S27a #status predicted !8#label MAT2\ !$102-151 #domain ribosomal protein S27a homology #label RIB SUMMARY #length 156 #molecular-weight 17951 #checksum 9364 SEQUENCE /// ENTRY UQFFR7 #type complete TITLE ubiquitin / ribosomal protein S27a - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES ubiquitin-80-amino-acid fusion-protein ORGANISM #formal_name Drosophila melanogaster DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 21-Jul-2000 ACCESSIONS B31560; S46214 REFERENCE A31560 !$#authors Lee, H.; Simon, J.A.; Lis, J.T. !$#journal Mol. Cell. Biol. (1988) 8:4727-4735 !$#title Structure and expression of ubiquitin genes of Drosophila !1melanogaster. !$#cross-references MUID:89096844; PMID:2463465 !$#accession B31560 !'##molecule_type mRNA !'##residues 1-156 ##label LEE !'##cross-references GB:M22536; NID:g158754; PIDN:AAA28998.1; !1PID:g158755 REFERENCE S46214 !$#authors Barrio, R.; del Arco, A.; Cabrera, H.L.; Arribas, C. !$#journal Biochem. J. (1994) 302:237-244 !$#title Structure and expression of the Drosophila !1ubiquitin-80-amino-acid fusion-protein gene. !$#cross-references MUID:94347108; PMID:8068011 !$#accession S46214 !'##status preliminary !'##molecule_type DNA !'##residues 1-156 ##label BAR GENETICS !$#gene FlyBase:Ubi-f80 !'##cross-references FlyBase:FBgn0003942 CLASSIFICATION #superfamily ubiquitin / rat ribosomal protein S27a; !1ribosomal protein S27a homology; ubiquitin homology KEYWORDS protein biosynthesis; protein degradation; ribosome FEATURE !$1-76 #product ubiquitin #status predicted #label MAT1\ !$1-76 #domain ubiquitin homology #label UBH\ !$77-156 #product ribosomal protein S27a #status predicted !8#label MAT2\ !$101-151 #domain ribosomal protein S27a homology #label RIB SUMMARY #length 156 #molecular-weight 17940 #checksum 9110 SEQUENCE /// ENTRY UQWO7A #type complete TITLE ubiquitin / ribosomal protein S27a - tobacco hornworm CONTAINS ribosomal protein S27a; ubiquitin ORGANISM #formal_name Manduca sexta #common_name tobacco hornworm DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 21-Jul-2000 ACCESSIONS S13136 REFERENCE S13136 !$#authors Bishoff, S.T.; Schwartz, L.M. !$#journal Nucleic Acids Res. (1990) 18:6039-6043 !$#title Characterization of a ubiquitin-fusion gene from the tobacco !1hawkmoth, Manduca sexta. !$#cross-references MUID:91045065; PMID:1700368 !$#accession S13136 !'##molecule_type mRNA !'##residues 1-155 ##label BIS !'##cross-references EMBL:X53524; NID:g9724; PIDN:CAA37599.1; PID:g9725 CLASSIFICATION #superfamily ubiquitin / rat ribosomal protein S27a; !1ribosomal protein S27a homology; ubiquitin homology KEYWORDS protein biosynthesis; protein degradation; ribosome; zinc !1finger FEATURE !$1-76 #product ubiquitin #status predicted #label UBI\ !$1-76 #domain ubiquitin homology #label UBH\ !$77-155 #product ribosomal protein S27a #status predicted !8#label RIBP\ !$101-151 #domain ribosomal protein S27a homology #label RIB\ !$121-144 #region zinc finger CCCC motif SUMMARY #length 155 #molecular-weight 17848 #checksum 5153 SEQUENCE /// ENTRY UQBYR7 #type complete TITLE ubiquitin / ribosomal protein S31.e, cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein L9470.14; protein YLR167w; ubiquitin / ribosomal protein YS24; ubiquitin / ribosomal protein YS27a; ubiquitin fusion protein 3 ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 21-Jul-2000 ACCESSIONS C29456; S51414; S11252 REFERENCE A29456 !$#authors Oezkaynak, E.; Finley, D.; Solomon, M.J.; Varshavsky, A. !$#journal EMBO J. (1987) 6:1429-1439 !$#title The yeast ubiquitin genes: a family of natural gene fusions. !$#cross-references MUID:87275838; PMID:3038523 !$#accession C29456 !'##molecule_type DNA !'##residues 1-152 ##label OEZ !'##cross-references EMBL:X05730; NID:g4731; PIDN:CAA29197.1; PID:g4732 REFERENCE S51414 !$#authors Wohldmann, P. !$#submission submitted to the EMBL Data Library, November 1994 !$#description The sequence of S. cerevisiae cosmid 9470. !$#accession S51414 !'##molecule_type DNA !'##residues 1-152 ##label WOH !'##cross-references EMBL:U17246; NID:g577192; PIDN:AAB67466.1; !1PID:g577206; GSPDB:GN00012; MIPS:YLR167w REFERENCE S11249 !$#authors Otaka, E.; Higo, K.I.; Itoh, T. !$#journal Mol. Gen. Genet. (1984) 195:544-546 !$#title Yeast ribosomal proteins. VIII. Isolation of two proteins !1and sequence characterization of twenty-four proteins from !1cytoplasmic ribosomes. !$#accession S11252 !'##molecule_type protein !'##residues 77-95 ##label OTA GENETICS !$#gene SGD:UBI3; RPS37; MIPS:YLR167w !'##cross-references SGD:S0004157; MIPS:YLR167w !$#map_position 12R CLASSIFICATION #superfamily ubiquitin / rat ribosomal protein S27a; !1ribosomal protein S27a homology; ubiquitin homology KEYWORDS protein biosynthesis; ribosome FEATURE !$1-76 #product ubiquitin #status experimental #label MAT1\ !$1-76 #domain ubiquitin homology #label UBH\ !$77-152 #product ribosomal protein S27a #status experimental !8#label MAT2\ !$101-151 #domain ribosomal protein S27a homology #label RIB SUMMARY #length 152 #molecular-weight 17216 #checksum 9303 SEQUENCE /// ENTRY UQNCR #type fragment TITLE ubiquitin / ribosomal protein S27a - Neurospora crassa (fragment) ALTERNATE_NAMES ubiquitin fusion protein 3 ORGANISM #formal_name Neurospora crassa DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 21-Jul-2000 ACCESSIONS PQ0201; S05977 REFERENCE PQ0201 !$#authors Taccioli, G.E.; Grotewold, E.; Aisemberg, G.O.; Judewicz, !1N.D. !$#journal Gene (1991) 102:133-137 !$#title The cDNA sequence and expression of an ubiquitin-tail gene !1fusion in Neurospora crassa. !$#cross-references MUID:91323720; PMID:1650731 !$#accession PQ0201 !'##molecule_type mRNA !'##residues 1-149 ##label TAC !'##cross-references EMBL:X15338; NID:g3085; PIDN:CAA33390.1; PID:g3086 GENETICS !$#gene UBI CLASSIFICATION #superfamily ubiquitin / rat ribosomal protein S27a; !1ribosomal protein S27a homology; ubiquitin homology KEYWORDS DNA binding; protein biosynthesis; protein degradation; !1ribosome; zinc finger FEATURE !$1-71 #product ubiquitin (fragment) #status predicted !8#label UBI\ !$1-71 #domain ubiquitin homology (fragment) #label UBH\ !$72-149 #product ribosomal protein S27a #status predicted !8#label RIBP\ !$96-146 #domain ribosomal protein S27a homology #label RIB\ !$116-140 #region zinc finger CCCC motif SUMMARY #length 149 #checksum 1936 SEQUENCE /// ENTRY UQTO7A #type complete TITLE ubiquitin / ribosomal protein S27a - tomato ALTERNATE_NAMES ubiquitin fusion protein ubi3 CONTAINS ribosomal protein S27a; ubiquitin ORGANISM #formal_name Lycopersicon esculentum #common_name tomato DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 21-Jul-2000 ACCESSIONS S18351; S27280; S14656 REFERENCE S18351 !$#authors Hoffman, N.E.; Ko, K.; Milkowski, D.; Pichersky, E. !$#journal Plant Mol. Biol. (1991) 17:1189-1201 !$#title Isolation and characterization of tomato cDNA and genomic !1clones encoding the ubiquitin gene ubi3. !$#cross-references MUID:92032784; PMID:1657246 !$#accession S18351 !'##molecule_type DNA !'##residues 1-156 ##label HOF1 !'##cross-references EMBL:X58253; NID:g19396; PIDN:CAA41207.1; !1PID:g19397 !$#accession S27280 !'##molecule_type mRNA !'##residues 1-156 ##label HOF2 !'##cross-references GB:X58253; NID:g19396; PIDN:CAA41207.1; PID:g19397 GENETICS !$#gene UBI3 !$#map_position 1 CLASSIFICATION #superfamily ubiquitin / rat ribosomal protein S27a; !1ribosomal protein S27a homology; ubiquitin homology KEYWORDS protein biosynthesis; protein degradation; ribosome FEATURE !$1-76 #product ubiquitin #status predicted #label MAT1\ !$1-76 #domain ubiquitin homology #label UBH\ !$77-156 #product ribosomal protein S27a #status predicted !8#label MAT2\ !$101-151 #domain ribosomal protein S27a homology #label RIB SUMMARY #length 156 #molecular-weight 17702 #checksum 8513 SEQUENCE /// ENTRY UQDOR7 #type complete TITLE ubiquitin / ribosomal protein S27a - slime mold (Dictyostelium discoideum) ORGANISM #formal_name Dictyostelium discoideum DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 21-Jul-2000 ACCESSIONS E34080 REFERENCE A34080 !$#authors Ohmachi, T.; Giorda, R.; Shaw, D.R.; Ennis, H.L. !$#journal Biochemistry (1989) 28:5226-5231 !$#title Molecular organization of developmentally regulated !1Dictyostelium discoideum ubiquitin cDNAs. !$#cross-references MUID:89352609; PMID:2548604 !$#accession E34080 !'##molecule_type mRNA !'##residues 1-154 ##label OHM !'##cross-references GB:M23750; GB:J02858; NID:g167940; PIDN:AAA33264.1; !1PID:g167941 CLASSIFICATION #superfamily ubiquitin / rat ribosomal protein S27a; !1ribosomal protein S27a homology; ubiquitin homology KEYWORDS protein biosynthesis; protein degradation; ribosome FEATURE !$1-76 #product ubiquitin #status predicted #label MAT1\ !$1-76 #domain ubiquitin homology #label UBH\ !$77-154 #product ribosomal protein S27a #status predicted !8#label MAT2\ !$102-152 #domain ribosomal protein S27a homology #label RIB SUMMARY #length 154 #molecular-weight 17448 #checksum 3723 SEQUENCE /// ENTRY A64349 #type complete TITLE ribosomal protein S27A - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A64349 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession A64349 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-60 ##label BUL !'##cross-references GB:U67492; GB:L77117; NID:g1591096; !1PIDN:AAB98383.1; PID:g1591098; TIGR:MJ0393 GENETICS !$#map_position REV356992-356810 CLASSIFICATION #superfamily ribosomal protein S27a; ribosomal protein S27a !1homology FEATURE !$8-54 #domain ribosomal protein S27a homology #label RIB SUMMARY #length 60 #molecular-weight 7048 #checksum 6073 SEQUENCE /// ENTRY S27036 #type complete TITLE ribosomal protein S27a.eR [similarity] - Haloarcula marismortui ALTERNATE_NAMES ribosomal protein HSH ORGANISM #formal_name Haloarcula marismortui DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S27036 REFERENCE S27035 !$#authors Arndt, E.; Steffens, C. !$#journal FEBS Lett. (1992) 314:211-214 !$#title Nucleotide sequence of the genes for ribosomal proteins HS15 !1and HSH from Haloarcula marismortui: an archaeon-specific !1gene cluster. !$#cross-references MUID:93106152; PMID:1468549 !$#accession S27036 !'##molecule_type DNA !'##residues 1-44 ##label ARN !'##cross-references GB:X70117; GB:S51568; NID:g312778; PIDN:CAA49708.1; !1PID:g312780 CLASSIFICATION #superfamily ribosomal protein S27a; ribosomal protein S27a !1homology FEATURE !$2-44 #domain ribosomal protein S27a homology #label RIB SUMMARY #length 44 #molecular-weight 5203 #checksum 4167 SEQUENCE /// ENTRY HSHU1B #type complete TITLE histone H1-4 [validated] - human ALTERNATE_NAMES histone H1.4; histone H1b ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1988 #sequence_revision 12-Apr-1996 #text_change 17-Mar-2000 ACCESSIONS C40335; A24413 REFERENCE A40335 !$#authors Albig, W.; Kardalinou, E.; Drabent, B.; Zimmer, A.; !1Doenecke, D. !$#journal Genomics (1991) 10:940-948 !$#title Isolation and characterization of two human H1 histone genes !1within clusters of core histone genes. !$#cross-references MUID:92009931; PMID:1916825 !$#accession C40335 !'##status preliminary !'##molecule_type DNA !'##residues 1-219 ##label ALB !'##cross-references GB:M60748; NID:g184073; PIDN:AAA63187.1; !1PID:g184074 !'##experimental_source blood REFERENCE A24413 !$#authors Ohe, Y.; Hayashi, H.; Iwai, K. !$#journal J. Biochem. (1986) 100:359-368 !$#title Human spleen histone H1. Isolation and amino acid sequence !1of a main variant, H1b. !$#cross-references MUID:87057092; PMID:3782055 !$#accession A24413 !'##molecule_type protein !'##residues 2-219 ##label OHE !'##experimental_source spleen COMMENT This variant accounts for 60% of histone H1. GENETICS !$#gene GDB:H1F4 !'##cross-references GDB:120030; OMIM:142220 !$#map_position 12q11-12q21 CLASSIFICATION #superfamily histone H1 KEYWORDS acetylated amino end; chromosomal protein; DNA binding; !1methylated amino acid; nucleosome; spleen FEATURE !$2-219 #product histone H1-4 #status experimental #label !8MAT\ !$2-34 #domain amino-terminal #label ATD\ !$35-109 #domain globular #label GLB\ !$110-219 #domain carboxyl-terminal #label CTD\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental\ !$26 #modified_site N6-methyllysine (Lys) (partial) !8#status experimental SUMMARY #length 219 #molecular-weight 21865 #checksum 5512 SEQUENCE /// ENTRY B40335 #type complete TITLE histone H1-3 [validated] - human ALTERNATE_NAMES histone H1.3; histone H1.c ORGANISM #formal_name Homo sapiens #common_name man DATE 03-Mar-2000 #sequence_revision 03-Mar-2000 #text_change 03-Mar-2000 ACCESSIONS B40335; JX0086 REFERENCE A40335 !$#authors Albig, W.; Kardalinou, E.; Drabent, B.; Zimmer, A.; !1Doenecke, D. !$#journal Genomics (1991) 10:940-948 !$#title Isolation and characterization of two human H1 histone genes !1within clusters of core histone genes. !$#cross-references MUID:92009931; PMID:1916825 !$#accession B40335 !'##status preliminary !'##molecule_type DNA !'##residues 1-221 ##label ALB !'##cross-references GB:M60747; NID:g184071; PIDN:AAA63186.1; !1PID:g184072 REFERENCE JX0080 !$#authors Ohe, Y.; Hayashi, H.; Iwai, K. !$#journal J. Biochem. (1989) 106:844-857 !$#title Human spleen histone H1; isolation and amino acid sequences !1of three minor variants, H1a, H1c, and H1d. !$#cross-references MUID:90130391; PMID:2613692 !$#accession JX0086 !'##molecule_type protein !'##residues 2-221 ##label OHE GENETICS !$#gene GDB:H1F3; H1T !'##cross-references GDB:120029; OMIM:142210 !$#map_position 6p22.3-6p21.3 CLASSIFICATION #superfamily histone H1 KEYWORDS acetylated amino end; chromosomal protein; DNA binding; !1nucleosome; nucleus FEATURE !$2-221 #product histone H1-3 #status experimental #label !8MAT\ !$2-35 #domain amino-terminal #label ATD\ !$36-110 #domain globular #label GLB\ !$111-221 #domain carboxyl-terminal #label CTD\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental SUMMARY #length 221 #molecular-weight 22350 #checksum 9140 SEQUENCE /// ENTRY HSHU11 #type complete TITLE histone H1-2 [validated] - human ALTERNATE_NAMES histone H1-1; histone H1d ORGANISM #formal_name Homo sapiens #common_name man DATE 22-Nov-1993 #sequence_revision 12-Apr-1996 #text_change 17-Mar-2000 ACCESSIONS S26364; JX0080 REFERENCE S26363 !$#authors Eick, S.; Nicolai, M.; Mumberg, D.; Doenecke, D. !$#journal Eur. J. Cell Biol. (1989) 49:110-115 !$#title Human H1 histones: conserved and varied sequence elements in !1two H1 subtype genes. !$#cross-references MUID:89338424; PMID:2759094 !$#accession S26364 !'##molecule_type DNA !'##residues 1-213 ##label EIC !'##cross-references EMBL:X57129; NID:g31967; PIDN:CAA40408.1; !1PID:g31968 !'##note translation of initiator Met is not shown !'##note this sequence is called histone H1.2 by the authors REFERENCE JX0080 !$#authors Ohe, Y.; Hayashi, H.; Iwai, K. !$#journal J. Biochem. (1989) 106:844-857 !$#title Human spleen histone H1; isolation and amino acid sequences !1of three minor variants, H1a, H1c, and H1d. !$#cross-references MUID:90130391; PMID:2613692 !$#accession JX0080 !'##molecule_type protein !'##residues 2-213 ##label OHE !'##note 18-Val was also found COMMENT This histone, formerly H1-1, is reffered to as H1-2 in a !1revised nomenclature. GENETICS !$#gene GDB:H1F2 !'##cross-references GDB:120028; OMIM:142710 !$#map_position 1q21-1q21 CLASSIFICATION #superfamily histone H1 KEYWORDS acetylated amino end; chromosomal protein; nucleosome FEATURE !$2-213 #product histone H1-2 #status experimental #label !8MAT\ !$2-34 #domain amino-terminal #label ATD\ !$35-109 #domain globular #label GLB\ !$110-213 #domain carboxyl-terminal #label CTD\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental SUMMARY #length 213 #molecular-weight 21365 #checksum 929 SEQUENCE /// ENTRY HSBO11 #type fragment TITLE histone H1.1 - bovine (fragment) ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 29-Jun-1981 #sequence_revision 23-Mar-1995 #text_change 16-Feb-1997 ACCESSIONS A92316; S03027; A02580 REFERENCE A92316 !$#authors Liao, L.W.; Cole, R.D. !$#journal J. Biol. Chem. (1981) 256:3024-3029 !$#title The amino acid sequence of residues 1-104 of CTL-1, a bovine !1H1 histone. !$#cross-references MUID:81142290; PMID:7204387 !$#accession A92316 !'##molecule_type protein !'##residues 1-104 ##label LIA REFERENCE S03027 !$#authors Jakes, S.; Hastings, T.G.; Reimann, E.M.; Schlender, K.K. !$#journal FEBS Lett. (1988) 234:31-34 !$#title Identification of the phosphoserine residue in histone H1 !1phosphorylated by protein kinase C. !$#cross-references MUID:88271620; PMID:3134256 !$#accession S03027 !'##molecule_type protein !'##residues 97-105 ##label JAK REFERENCE A02578 !$#authors Rall, S.C.; Cole, R.D. !$#journal J. Biol. Chem. (1971) 246:7175-7190 !$#title Amino acid sequence and sequence variability of the !1amino-terminal regions of lysine-rich histones. !$#cross-references MUID:72068710; PMID:5167020 !$#contents annotation; composition of tryptic peptides CLASSIFICATION #superfamily histone H1 KEYWORDS acetylated amino end; DNA binding; nucleosome; !1phosphoprotein FEATURE !$1 #modified_site acetylated amino end (Ser) #status !8experimental\ !$35 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$103 #binding_site phosphate (Ser) (covalent) (by protein !8kinase C) #status experimental SUMMARY #length 105 #checksum 5344 SEQUENCE /// ENTRY S51660 #type complete TITLE histone H1-5 [validated] - human ALTERNATE_NAMES histone H1.5; histone H1a ORGANISM #formal_name Homo sapiens #common_name man DATE 03-Mar-2000 #sequence_revision 03-Mar-2000 #text_change 03-Mar-2000 ACCESSIONS S51660; JX0087; I59499 REFERENCE S51660 !$#authors Albig, W.; Doenecke, D. !$#submission submitted to the EMBL Data Library, December 1994 !$#description A human histone gene cluster containing a complete set of !1histone genes. !$#accession S51660 !'##molecule_type DNA !'##residues 1-226 ##label ALB !'##cross-references EMBL:X83509; NID:g603550; PIDN:CAA58498.1; !1PID:g603551 REFERENCE JX0080 !$#authors Ohe, Y.; Hayashi, H.; Iwai, K. !$#journal J. Biochem. (1989) 106:844-857 !$#title Human spleen histone H1; isolation and amino acid sequences !1of three minor variants, H1a, H1c, and H1d. !$#cross-references MUID:90130391; PMID:2613692 !$#accession JX0087 !'##molecule_type protein !'##residues 2-214,218-226 ##label OHE REFERENCE I59499 !$#authors Carozzi, N.; Marashi, F.; Plumb, M.; Zimmerman, S.; !1Zimmerman, A.; Coles, L.S.; Wells, J.R.E.; Stein, G.; Stein, !1J. !$#journal Science (1984) 224:1115-1117 !$#title Clustering of human H1 and core histone genes. !$#cross-references MUID:84196423; PMID:6719136 !$#accession I59499 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-36,'I',38,'A',40-51,'P',53-58,'A' ##label CAR !'##cross-references GB:K02570; NID:g183746; PIDN:AAA35943.1; !1PID:g553328 GENETICS !$#gene GDB:H1F5 !'##cross-references GDB:6261922; OMIM:142711 !$#map_position 6p22.2-6p21.1 CLASSIFICATION #superfamily histone H1 KEYWORDS acetylated amino end; chromosomal protein; DNA binding; !1nucleosome; nucleus FEATURE !$2-226 #product histone H1-5 #status experimental #label !8MAT\ !$2-37 #domain amino-terminal #label ATD\ !$38-112 #domain globular #label GLB\ !$113-226 #domain carboxyl-terminal #label CTD\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental SUMMARY #length 226 #molecular-weight 22580 #checksum 1199 SEQUENCE /// ENTRY HSRB13 #type complete TITLE histone H1.3 - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 31-Mar-1980 #sequence_revision 13-Jul-1981 #text_change 16-Feb-1997 ACCESSIONS A94467; A02578; A92149 REFERENCE A94467 !$#authors Hsiang, M.; Largman, C.R.; Cole, R.D. !$#citation unpublished results, cited by Cole, R.D., in The Molecular !1Biology of the Mammalian Genetic Apparatus, vol.1, Ts'o, !1P.O.P., ed., pp.93-104, Elsevier/North-Holland, Amsterdam, !1New York, and Oxford, 1977 !$#accession A94467 !'##molecule_type protein !'##residues 1-213 ##label HSI REFERENCE A02578 !$#authors Rall, S.C.; Cole, R.D. !$#journal J. Biol. Chem. (1971) 246:7175-7190 !$#title Amino acid sequence and sequence variability of the !1amino-terminal regions of lysine-rich histones. !$#cross-references MUID:72068710; PMID:5167020 !$#accession A02578 !'##molecule_type protein !'##residues 1-72 ##label RAL REFERENCE A92149 !$#authors Jones, G.M.T.; Rall, S.C.; Cole, R.D. !$#journal J. Biol. Chem. (1974) 249:2548-2553 !$#title Extension of the amino acid sequence of a lysine-rich !1histone. !$#cross-references MUID:74143498; PMID:4822503 !$#accession A92149 !'##molecule_type protein !'##residues 73-107 ##label JON CLASSIFICATION #superfamily histone H1 KEYWORDS acetylated amino end; DNA binding; nucleosome FEATURE !$1 #modified_site acetylated amino end (Ser) #status !8experimental SUMMARY #length 213 #molecular-weight 21423 #checksum 5443 SEQUENCE /// ENTRY HSCH1 #type complete TITLE histone H1.02 - chicken ALTERNATE_NAMES linker histone ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 03-Mar-2000 ACCESSIONS A29179 REFERENCE A92434 !$#authors Sugarman, B.J.; Dodgson, J.B.; Engel, J.D. !$#journal J. Biol. Chem. (1983) 258:9005-9016 !$#title Genomic organization, DNA sequence, and expression of !1chicken embryonic histone genes. !$#cross-references MUID:83238548; PMID:6190814 !$#accession A29179 !'##molecule_type DNA !'##residues 1-218 ##label SUG !'##note the authors translated the codon GCG for residue 117 as Glu CLASSIFICATION #superfamily histone H1 KEYWORDS acetylated amino end; chromosomal protein; DNA binding; !1nucleosome FEATURE !$2-218 #product histone H1 #status predicted #label MAT\ !$2-36 #domain amino-terminal #label ATD\ !$37-110 #domain globular #label GLB\ !$111-218 #domain carboxyl-terminal #label CTD\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status predicted SUMMARY #length 218 #molecular-weight 21881 #checksum 2895 SEQUENCE /// ENTRY HSRT1T #type complete TITLE histone H1t - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1987 #sequence_revision 01-Dec-1995 #text_change 22-Jun-1999 ACCESSIONS A27779; A02582; I55352 REFERENCE A27779 !$#authors Cole, K.D.; Kandala, J.C.; Kistler, W.S. !$#journal J. Biol. Chem. (1986) 261:7178-7183 !$#title Isolation of the gene for the testis-specific H1 histone !1variant H1t. !$#cross-references MUID:86223975; PMID:2423516 !$#accession A27779 !'##molecule_type DNA !'##residues 1-208 ##label COL !'##cross-references GB:M13170; NID:g204596; PIDN:AAA41328.1; !1PID:g204597 REFERENCE A02582 !$#authors Cole, K.D.; York, R.G.; Kistler, W.S. !$#journal Biochim. Biophys. Acta (1986) 869:223-229 !$#title Sequence of the amino terminal half of rat testis-specific !1histone variant H1t. !$#cross-references MUID:86131690; PMID:3947637 !$#accession A02582 !'##molecule_type protein !'##residues 2-109 ##label CO2 REFERENCE I55352 !$#authors Wolfe, S.A.; Grimes, S.R. !$#journal J. Biol. Chem. (1991) 266:6637-6643 !$#title Protein-DNa interactions within the rat histone h4t !1promoter. !$#cross-references MUID:91177927; PMID:1706721 !$#accession I55352 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-208 ##label RES !'##cross-references GB:M28409; NID:g204550; PIDN:AAA41305.1; !1PID:g204551 COMMENT This histone is a testis-specific H1 variant that appears !1during meiosis in spermatogenesis. GENETICS !$#gene H1t CLASSIFICATION #superfamily histone H1 KEYWORDS chromosomal protein; DNA binding; nucleosome; !1spermatogenesis; testis FEATURE !$2-208 #product histone H1t #status predicted #label MAT SUMMARY #length 208 #molecular-weight 21725 #checksum 2222 SEQUENCE /// ENTRY HSPG1T #type complete TITLE histone H1t - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 16-Feb-1997 ACCESSIONS A02581 REFERENCE A02581 !$#authors Cole, K.D.; York, R.G.; Kistler, W.S. !$#journal J. Biol. Chem. (1984) 259:13695-13702 !$#title The amino acid sequence of boar H1t, a testis-specific H1 !1histone variant. !$#cross-references MUID:85054795; PMID:6389534 !$#accession A02581 !'##molecule_type protein !'##residues 1-211 ##label COL COMMENT This histone is a testis-specific H1 variant that appears !1during meiosis in spermatogenesis. CLASSIFICATION #superfamily histone H1 KEYWORDS acetylated amino end; chromosomal protein; DNA binding; !1nucleosome; spermatogenesis; testis FEATURE !$1 #modified_site acetylated amino end (Ala) #status !8experimental SUMMARY #length 211 #molecular-weight 22059 #checksum 1979 SEQUENCE /// ENTRY HSTR1 #type complete TITLE histone H1 - trout ORGANISM #formal_name Salmo sp. #common_name trout DATE 31-May-1979 #sequence_revision 08-Oct-1981 #text_change 16-Feb-1997 ACCESSIONS A02583 REFERENCE A02583 !$#authors MacLeod, A.R.; Wong, N.C.W.; Dixon, G.H. !$#journal Eur. J. Biochem. (1977) 78:281-291 !$#title The amino-acid sequence of trout-testis histone H1. !$#cross-references MUID:78023898; PMID:913397 !$#accession A02583 !'##molecule_type protein !'##residues 1-194 ##label MAC !'##note a minor component has 35-Ile CLASSIFICATION #superfamily histone H1 KEYWORDS acetylated amino end; DNA binding; nucleosome; !1phosphoprotein FEATURE !$1 #modified_site acetylated amino end (Ala) (partial) !8#status experimental\ !$145,161,182 #binding_site phosphate (Ser) (covalent) #status !8experimental SUMMARY #length 194 #molecular-weight 19408 #checksum 8243 SEQUENCE /// ENTRY HSTR1R #type complete TITLE histone H1 - rainbow trout ORGANISM #formal_name Oncorhynchus mykiss #common_name rainbow trout DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 16-Jun-2000 ACCESSIONS A02584 REFERENCE A02584 !$#authors Mezquita, J.; Connor, W.; Winkfein, R.J.; Dixon, G.H. !$#journal J. Mol. Evol. (1985) 21:209-219 !$#title An H1 histone gene from rainbow trout (Salmo gairdnerii). !$#cross-references MUID:85264847; PMID:6443128 !$#accession A02584 !'##molecule_type DNA !'##residues 1-206 ##label MEZ !'##cross-references GB:X02624; NID:g64323; PIDN:CAB37646.1; !1PID:g4468016 CLASSIFICATION #superfamily histone H1 KEYWORDS chromosomal protein; DNA binding; nucleosome FEATURE !$1-44 #region flexible nose\ !$45-117 #region globular head\ !$118-206 #region flexible tail SUMMARY #length 206 #molecular-weight 20672 #checksum 5424 SEQUENCE /// ENTRY HSXL1A #type complete TITLE histone H1A - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 22-Jun-1999 ACCESSIONS F24510 REFERENCE A92918 !$#authors Perry, M.; Thomsen, G.H.; Roeder, R.G. !$#journal J. Mol. Biol. (1985) 185:479-499 !$#title Genomic organization and nucleotide sequence of two distinct !1histone gene clusters from Xenopus laevis. Identification of !1novel conserved upstream sequence elements. !$#cross-references MUID:86037224; PMID:3863963 !$#accession F24510 !'##molecule_type DNA !'##residues 1-209 ##label PER !'##cross-references GB:X03018; NID:g64774; PIDN:CAA26815.1; PID:g64775 !'##note initiator Met not shown !'##note one copy of the H1A gene, from the X1h3 gene cluster, was !1sequenced CLASSIFICATION #superfamily histone H1 KEYWORDS chromosomal protein; DNA binding; nucleosome SUMMARY #length 209 #molecular-weight 21242 #checksum 7795 SEQUENCE /// ENTRY HSXL1B #type complete TITLE histone H1B - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 22-Jun-1999 ACCESSIONS D24510 REFERENCE A92918 !$#authors Perry, M.; Thomsen, G.H.; Roeder, R.G. !$#journal J. Mol. Biol. (1985) 185:479-499 !$#title Genomic organization and nucleotide sequence of two distinct !1histone gene clusters from Xenopus laevis. Identification of !1novel conserved upstream sequence elements. !$#cross-references MUID:86037224; PMID:3863963 !$#accession D24510 !'##molecule_type DNA !'##residues 1-219 ##label PER !'##cross-references GB:X03017; NID:g64766; PIDN:CAA26812.1; PID:g64771 !'##note the authors translated the codon AGC for residue 102 as Thr !'##note initiator Met not shown !'##note one copy of the H1B gene, from the X1h1 gene cluster, was !1sequenced CLASSIFICATION #superfamily histone H1 KEYWORDS chromosomal protein; DNA binding; nucleosome SUMMARY #length 219 #molecular-weight 22309 #checksum 1801 SEQUENCE /// ENTRY HSFF1 #type fragments TITLE histone H1 - fruit fly (Drosophila melanogaster) (fragments) ORGANISM #formal_name Drosophila melanogaster DATE 31-Oct-1980 #sequence_revision 31-Oct-1980 #text_change 14-May-1999 ACCESSIONS A02585 REFERENCE A02630 !$#authors Goldberg, M.L. !$#citation Ph.D. thesis, Stanford Univ., 1979 !$#accession A02585 !'##molecule_type DNA !'##residues 1-187 ##label GOL !'##note the author translated the codon TTC for residue 87 as Leu and !1GGT for residue 123 as Trp GENETICS !$#gene FlyBase:His1 !'##cross-references FlyBase:FBgn0001195 CLASSIFICATION #superfamily histone H1 KEYWORDS DNA binding; nucleosome SUMMARY #length 187 #checksum 3047 SEQUENCE /// ENTRY HSUR1P #type complete TITLE histone H1, gonadal - sea urchin (Parechinus angulosus) ORGANISM #formal_name Parechinus angulosus #common_name angulate urchin DATE 31-Mar-1980 #sequence_revision 31-Mar-1980 #text_change 16-Feb-1997 ACCESSIONS A91090; A91091; A02586 REFERENCE A91090 !$#authors Strickland, W.N.; Strickland, M.; de Groot, P.C.; von Holt, !1C.; Wittmann-Liebold, B. !$#journal Eur. J. Biochem. (1980) 104:559-566 !$#title The primary structure of histone H1 from sperm of the sea !1urchin Parechinus angulosus. 1. Chemical and enzymatic !1fragmentation of the protein and the sequence of amino acids !1in the four N-terminal cyanogen bromide peptides. !$#cross-references MUID:80156831; PMID:6767609 !$#contents sequence of residues 1-84 !$#accession A91090 !'##molecule_type protein !'##residues 1-248 ##label STR REFERENCE A91091 !$#authors Strickland, W.N.; Strickland, M.; Brandt, W.F.; von Holt, !1C.; Lehmann, A.; Wittmann-Liebold, B. !$#journal Eur. J. Biochem. (1980) 104:567-578 !$#title The primary structure of histone H1 from sperm of the sea !1urchin Parechinus angulosus. 2. Sequence of the C-terminal !1CNBr peptide and the entire primary structure. !$#cross-references MUID:80156832; PMID:7363905 !$#accession A91091 !'##molecule_type protein !'##residues 80-248 ##label ST2 !'##note 144-Arg was also found CLASSIFICATION #superfamily histone H1 KEYWORDS DNA binding; nucleosome; sperm SUMMARY #length 248 #molecular-weight 26387 #checksum 7580 SEQUENCE /// ENTRY HSUR1E #type fragment TITLE histone H1, gonadal - sea urchin (Echinolampas crassa) (tentative sequence) (fragment) ORGANISM #formal_name Echinolampas crassa DATE 06-Jul-1982 #sequence_revision 30-Sep-1988 #text_change 31-Mar-2000 ACCESSIONS A02587 REFERENCE A02587 !$#authors Strickland, W.N.; Strickland, M.; von Holt, C. !$#journal Biochim. Biophys. Acta (1982) 700:127-129 !$#title A comparison of the amino acid sequences of histones H1 from !1the sperm of Echinolampas crassa and Parechinus angulosus. !$#accession A02587 !'##molecule_type protein !'##residues 1-171 ##label STR CLASSIFICATION #superfamily histone H1 KEYWORDS DNA binding; nucleosome; sperm SUMMARY #length 171 #checksum 20 SEQUENCE /// ENTRY HSDU1A #type complete TITLE histone H1a, sperm - polychaete (Platynereis dumerilii) ORGANISM #formal_name Platynereis dumerilii DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Feb-1997 ACCESSIONS A24560 REFERENCE A91148 !$#authors Kmiecik, D.; Sellos, D.; Belaiche, D.; Sautiere, P. !$#journal Eur. J. Biochem. (1985) 150:359-370 !$#title Primary structure of the two variants of a sperm-specific !1histone H1 from the annelid Platynereis dumerilii. !$#cross-references MUID:85257663; PMID:4018088 !$#accession A24560 !'##molecule_type protein !'##residues 1-121 ##label KMI CLASSIFICATION #superfamily histone H1 KEYWORDS chromosomal protein; DNA binding; nucleosome; sperm FEATURE !$9-79 #domain globular #label GLB SUMMARY #length 121 #molecular-weight 13318 #checksum 3272 SEQUENCE /// ENTRY HSDU1B #type complete TITLE histone H1b, sperm - polychaete (Platynereis dumerilii) ORGANISM #formal_name Platynereis dumerilii DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Feb-1997 ACCESSIONS B24560 REFERENCE A91148 !$#authors Kmiecik, D.; Sellos, D.; Belaiche, D.; Sautiere, P. !$#journal Eur. J. Biochem. (1985) 150:359-370 !$#title Primary structure of the two variants of a sperm-specific !1histone H1 from the annelid Platynereis dumerilii. !$#cross-references MUID:85257663; PMID:4018088 !$#accession B24560 !'##molecule_type protein !'##residues 1-119 ##label KMI CLASSIFICATION #superfamily histone H1 KEYWORDS chromosomal protein; DNA binding; nucleosome; sperm FEATURE !$7-77 #domain globular #label GLB SUMMARY #length 119 #molecular-weight 13099 #checksum 2435 SEQUENCE /// ENTRY HSGS5 #type complete TITLE histone H5 - goose ORGANISM #formal_name Anser anser #common_name domestic goose DATE 31-Dec-1979 #sequence_revision 31-Dec-1979 #text_change 16-Feb-1997 ACCESSIONS A02588 REFERENCE A02588 !$#authors Yaguchi, M.; Roy, C.; Seligy, V.L. !$#journal Biochem. Biophys. Res. Commun. (1979) 90:1400-1406 !$#title Complete amino acid sequence of goose erythrocyte H5 histone !1and the homology between H1 and H5 histones. !$#cross-references MUID:80087664; PMID:518607 !$#accession A02588 !'##molecule_type protein !'##residues 1-193 ##label YAG CLASSIFICATION #superfamily histone H1 KEYWORDS chromosomal protein; DNA binding; erythrocyte FEATURE !$1-21 #domain amino-terminal #label NH2\ !$22-99 #domain globular #label GLB\ !$100-193 #domain carboxyl-terminal #label END SUMMARY #length 193 #molecular-weight 20900 #checksum 7262 SEQUENCE /// ENTRY HSPY5 #type fragment TITLE histone H5 - pigeon (fragment) ORGANISM #formal_name Columba livia #common_name domestic pigeon DATE 31-May-1980 #sequence_revision 31-May-1980 #text_change 16-Feb-1997 ACCESSIONS A02590 REFERENCE A02590 !$#authors Yaguchi, M.; Roy, C.; Dove, M.; Seligy, V. !$#journal Biochem. Biophys. Res. Commun. (1977) 76:100-106 !$#title Amino acid sequence homologies between H1 and H5 histones. !$#cross-references MUID:77201524; PMID:559492 !$#accession A02590 !'##molecule_type protein !'##residues 1-38 ##label YAG CLASSIFICATION #superfamily histone H1 KEYWORDS chromosomal protein; DNA binding; erythrocyte FEATURE !$1-23 #domain amino-terminal #label NH2\ !$24-38 #domain globular (fragment) #label GLB SUMMARY #length 38 #checksum 5917 SEQUENCE /// ENTRY HSCH5 #type complete TITLE histone H5 - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 13-Jul-1981 #sequence_revision 13-Jul-1981 #text_change 22-Jun-1999 ACCESSIONS A93487; A91415; A91416; A91277; A02589 REFERENCE A93487 !$#authors Krieg, P.A.; Robins, A.J.; D'Andrea, R.; Wells, J.R.E. !$#journal Nucleic Acids Res. (1983) 11:619-627 !$#title The chicken H5 gene is unlinked to core and H1 histone !1genes. !$#cross-references MUID:83168890; PMID:6300759 !$#accession A93487 !'##molecule_type DNA !'##residues 1-189 ##label KRI !'##cross-references GB:J00870; NID:g211861; PIDN:AAA48798.1; !1PID:g211862 REFERENCE A91415 !$#authors Garel, A.; Mazen, A.; Champagne, M.; Sautiere, P.; Kmiecik, !1D.; Loy, O.; Biserte, G. !$#journal FEBS Lett. (1975) 50:195-199 !$#title Chicken erythrocyte histone H-5; I amino terminal sequence !1(70 residues). !$#cross-references MUID:75093662; PMID:1112411 !$#accession A91415 !'##molecule_type protein !'##residues 1-70 ##label GAR !'##note 15-Gln was also found REFERENCE A91416 !$#authors Sautiere, P.; Kmiecik, D.; Loy, O.; Briand, G.; Biserte, G.; !1Garel, A.; Champagne, M. !$#journal FEBS Lett. (1975) 50:200-203 !$#title Chicken erythrocyte histone H-5. II. Amino acid sequence !1adjacent to the phenylalanine residue. !$#cross-references MUID:75093663; PMID:1112412 !$#accession A91416 !'##molecule_type protein !'##residues 71-89,'GS',92-95 ##label SAU REFERENCE A91277 !$#authors Briand, G.; Kmiecik, D.; Sautiere, P.; Wouters, D.; !1Borie-Loy, O.; Biserte, G.; Mazen, A.; Champagne, M. !$#journal FEBS Lett. (1980) 112:147-151 !$#title Chicken erythrocyte histone H5. IV. Sequence of the !1carboxy-terminal half of the molecule (96 residues) and !1complete sequence. !$#cross-references MUID:80179171; PMID:7371850 !$#accession A91277 !'##molecule_type protein !'##residues 90-91;94-189 ##label BRI REFERENCE A94462 !$#authors Martinage, A. !$#citation unpublished results, cited by Briand, G., Kmiecik, D., !1Sautiere, P., Wouters, D., Borie-Loy, O., Biserte, G., !1Mazen, A., and Champagne, M., FEBS Lett. 112, 147-151, 1980 !$#contents annotation; phosphate binding sites CLASSIFICATION #superfamily histone H1 KEYWORDS chromosomal protein; DNA binding; erythrocyte; !1phosphoprotein FEATURE !$1-20 #domain amino-terminal #label NH2\ !$21-98 #domain globular #label GLB\ !$99-189 #domain carboxyl-terminal #label END\ !$145,166 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 189 #molecular-weight 20602 #checksum 1368 SEQUENCE /// ENTRY HSHU10 #type complete TITLE histone H1-0 - human ALTERNATE_NAMES histone H1'; histone H1(o); histone H1.0; linker histone ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 17-Mar-2000 ACCESSIONS A24850 REFERENCE A24850 !$#authors Doenecke, D.; Tonjes, R. !$#journal J. Mol. Biol. (1986) 187:461-464 !$#title Differential distribution of lysine and arginine residues in !1the closely related histones H1' and H5. Analysis of a human !1H1' gene. !$#cross-references MUID:86200226; PMID:3084796 !$#accession A24850 !'##molecule_type DNA !'##residues 1-194 ##label DOE !'##cross-references EMBL:X03473; NID:g32106; PIDN:CAA27190.1; !1PID:g32107 COMMENT The H1-0 histones are found in cells that are in terminal !1stages of differentiation or that have low rates of cell !1division. Structurally and functionally the H1-0 family !1appears intermediate with respect to the H1 and H5 families. COMMENT A three-domain organization is conserved throughout this !1superfamily, with a central globular domain sealing off two !1turns of DNA around the nucleosome and a carboxyl domain !1involved with chromatin condensation. GENETICS !$#gene GDB:H1F0; H1FV; H10 !'##cross-references GDB:118808; OMIM:142708 !$#map_position 22q13.1-22q13.1 CLASSIFICATION #superfamily histone H1 KEYWORDS chromosomal protein; DNA binding; nucleosome FEATURE !$2-194 #product histone H1-0 #status predicted #label MAT\ !$2-20 #domain amino-terminal #label NH2\ !$21-98 #domain globular #label GLB\ !$99-194 #domain carboxyl-terminal #label END SUMMARY #length 194 #molecular-weight 20863 #checksum 7654 SEQUENCE /// ENTRY HSXL5A #type complete TITLE histone H5A - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Feb-1997 ACCESSIONS JT0403 REFERENCE JT0403 !$#authors Rutledge, R.G.; Neelin, J.M.; Seligy, V.L. !$#journal Gene (1988) 70:117-126 !$#title Isolation and expression of cDNA clones coding for two !1sequence variants of Xenopus laevis histone H5. !$#cross-references MUID:89196903; PMID:2907322 !$#accession JT0403 !'##molecule_type mRNA !'##residues 1-196 ##label RUT !'##cross-references GB:M22834 CLASSIFICATION #superfamily histone H1 KEYWORDS chromosomal protein; DNA binding FEATURE !$2-196 #product histone H5A #status predicted #label MAT\ !$2-20 #domain amino-terminal #label NH2\ !$21-98 #domain globular #label GLB\ !$99-196 #domain carboxyl-terminal #label END SUMMARY #length 196 #molecular-weight 21062 #checksum 1473 SEQUENCE /// ENTRY HSMU11 #type complete TITLE histone H1.1 - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 31-Mar-1992 #sequence_revision 05-May-1995 #text_change 22-Jun-1999 ACCESSIONS S19698; S18053 REFERENCE S19698 !$#authors Gantt, J.S.; Lenvik, T.R. !$#journal Eur. J. Biochem. (1991) 202:1029-1039 !$#title Arabidopsis thaliana H1 histones. Analysis of two members of !1a small gene family. !$#cross-references MUID:92111474; PMID:1765064 !$#accession S19698 !'##molecule_type DNA !'##residues 1-274 ##label GAN1 !'##cross-references EMBL:X62458; NID:g16316; PIDN:CAA44314.1; !1PID:g16317 REFERENCE S18053 !$#authors Gantt, J.S.; Lenvik, T.R. !$#submission submitted to the EMBL Data Library, October 1991 !$#description Arabidopsis thaliana H1 histones: analysis of two members of !1a small gene family. !$#accession S18053 !'##molecule_type mRNA !'##residues 33-274 ##label GAN2 !'##cross-references EMBL:X62456; NID:g732560; PIDN:CAA44312.1; !1PID:g16314 GENETICS !$#introns 67/3 CLASSIFICATION #superfamily histone H1 KEYWORDS chromosomal protein; DNA binding; nucleosome SUMMARY #length 274 #molecular-weight 28946 #checksum 1028 SEQUENCE /// ENTRY HSMU12 #type complete TITLE histone H1, partial [imported] - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 02-Mar-2001 ACCESSIONS S19699; S18065; F84710 REFERENCE S19698 !$#authors Gantt, J.S.; Lenvik, T.R. !$#journal Eur. J. Biochem. (1991) 202:1029-1039 !$#title Arabidopsis thaliana H1 histones. Analysis of two members of !1a small gene family. !$#cross-references MUID:92111474; PMID:1765064 !$#accession S19699 !'##molecule_type mRNA !'##residues 1-273 ##label GAN !'##cross-references EMBL:X62459; NID:g16319; PIDN:CAA44316.1; !1PID:g16320 REFERENCE A84420 !$#authors Lin, X.; Kaul, S.; Rounsley, S.D.; Shea, T.P.; Benito, M.I.; !1Town, C.D.; Fujii, C.Y.; Mason, T.M.; Bowman, C.L.; !1Barnstead, M.E.; Feldblyum, T.V.; Buell, C.R.; Ketchum, !1K.A.; Lee, J.J.; Ronning, C.M.; Koo, H.; Moffat, K.S.; !1Cronin, L.A.; Shen, M.; VanAken, S.E.; Umayam, L.; Tallon, !1L.J.; Gill, J.E.; Adams, M.D.; Carrera, A.J.; Creasy, T.H.; !1Goodman, H.M.; Somerville, C.R.; Copenhaver, G.P.; Preuss, !1D.; Nierman, W.C.; White, O.; Eisen, J.A.; Salzberg, S.L.; !1Fraser, C.M.; Venter, J.C. !$#journal Nature (1999) 402:761-768 !$#title Sequence and analysis of chromosome 2 of the plant !1Arabidopsis thaliana. !$#cross-references MUID:20083487; PMID:10617197 !$#accession F84710 !'##status preliminary !'##molecule_type DNA !'##residues 1-273 ##label STO !'##cross-references GB:AE002093; NID:g6598353; PIDN:AAF18593.1; !1GSPDB:GN00139 GENETICS !$#gene At2g30620 !$#map_position 2 CLASSIFICATION #superfamily histone H1 KEYWORDS chromosomal protein; DNA binding; nucleosome SUMMARY #length 273 #molecular-weight 28487 #checksum 7081 SEQUENCE /// ENTRY HSHUA1 #type complete TITLE histone H2A.1 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1987 #sequence_revision 22-Nov-1996 #text_change 22-Jun-1999 ACCESSIONS B56624; S51661; A91959; A02591; A05257; S14528 REFERENCE A56624 !$#authors Dobner, T.; Wolf, I.; Mai, B.; Lipp, M. !$#journal DNA Seq. (1991) 1:409-413 !$#title A novel divergently transcribed human histone H2A/H2B gene !1pair. !$#cross-references MUID:92119332; PMID:1768865 !$#accession B56624 !'##molecule_type DNA !'##residues 1-130 ##label DOB !'##cross-references EMBL:X57138; NID:g31978; PIDN:CAA40417.1; !1PID:g31980 !'##note sequence extracted from NCBI backbone (NCBIP:77765) REFERENCE S51660 !$#authors Albig, W.; Doenecke, D. !$#submission submitted to the EMBL Data Library, December 1994 !$#description A human histone gene cluster containing a complete set of !1histone genes. !$#accession S51661 !'##status preliminary !'##molecule_type DNA !'##residues 1-130 ##label ALB !'##cross-references EMBL:X83549; NID:g603552; PIDN:CAA58539.1; !1PID:g603553 REFERENCE A91959 !$#authors Hayashi, T.; Ohe, Y.; Hayashi, H.; Iwai, K. !$#journal J. Biochem. (1980) 88:27-34 !$#title Human spleen histone H2A. Isolation and four variant !1sequences. !$#cross-references MUID:81006778; PMID:7410338 !$#contents compositions of tryptic peptides !$#accession A91959 !'##molecule_type protein !'##residues 2-130 ##label HAY !'##note four variants were found; the sequence of variant 1 is shown !'##note variant 2 appears to differ from that shown in having 100-Arg; !1variant 3, in having 17-Ser (or 77-Ser) and 52-Met; and !1variant 4, in having 17-Ser (or 77-Ser) and 52-Met and in !1lacking a His at position 124 or 125 GENETICS !$#gene GDB:H2A !'##cross-references GDB:134229 !$#map_position 1q21-1q23 CLASSIFICATION #superfamily histone H2A KEYWORDS acetylated amino end; chromosomal protein; DNA binding; !1nucleosome core; phosphoprotein FEATURE !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status predicted\ !$2 #binding_site phosphate (Ser) (covalent) (partial) !8#status experimental SUMMARY #length 130 #molecular-weight 14091 #checksum 205 SEQUENCE /// ENTRY HSBO2A #type complete TITLE histone H2A - bovine ALTERNATE_NAMES brain capillary plasma membrane 16K protein; peptide MB-35 ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 23-Oct-1981 #sequence_revision 23-Oct-1981 #text_change 16-Feb-1997 ACCESSIONS A91216; A93756; A92113; A92106; PL0132; A34289; A49741; !1A02591 REFERENCE A91216 !$#authors Sautiere, P.; Tyrou, D.; Laine, B.; Mizon, J.; Ruffin, P.; !1Biserte, G. !$#journal Eur. J. Biochem. (1974) 41:563-576 !$#title Covalent structure of calf-thymus ALK-histone. !$#cross-references MUID:74125866; PMID:4856314 !$#accession A91216 !'##molecule_type protein !'##residues 1-129 ##label SAU REFERENCE A93756 !$#authors Olson, M.O.J.; Sugano, N.; Yeoman, L.C.; Johnson, B.R.; !1Jordan, J.; Taylor, C.W.; Starbuck, W.C.; Busch, H. !$#journal Physiol. Chem. Phys. (1972) 4:10-16 !$#title Homology of the amino terminal sequences of the AL and GAR !1calf thymus histones. !$#cross-references MUID:74009494; PMID:4667695 !$#accession A93756 !'##molecule_type protein !'##residues 1-29 ##label OLS !'##experimental_source thymus REFERENCE A92113 !$#authors Yeoman, L.C.; Olson, M.O.J.; Sugano, N.; Jordan, J.J.; !1Taylor, C.W.; Starbuck, W.C.; Busch, H. !$#journal J. Biol. Chem. (1972) 247:6018-6023 !$#title Amino acid sequence of the center of the !1arginine-lysine-rich histone from calf thymus. The total !1sequence. !$#cross-references MUID:73094977; PMID:4568599 !$#accession A92113 !'##molecule_type protein !'##residues 30-81 ##label YEO !'##experimental_source thymus REFERENCE A92106 !$#authors Sugano, N.; Olson, M.O.J.; Yeoman, L.C.; Johnson, B.R.; !1Taylor, C.W.; Starbuck, W.C.; Busch, H. !$#journal J. Biol. Chem. (1972) 247:3589-3591 !$#title Amino acid sequence of the COOH-terminal portion of the !1arginine-lysine-rich histone of calf thymus. !$#cross-references MUID:72195544; PMID:4555425 !$#accession A92106 !'##molecule_type protein !'##residues 82-129 ##label SUG !'##experimental_source thymus REFERENCE PL0130 !$#authors Pardridge, W.M.; Nowlin, D.M.; Calaycay, J.; Shively, J.E. !$#journal J. Neurochem. (1989) 53:1014-1018 !$#title Predominant low-molecular-weight proteins in isolated brain !1capillaries are histones. !$#cross-references MUID:89361419; PMID:2769252 !$#accession PL0132 !'##molecule_type protein !'##residues 21-29;78-81 ##label PAR REFERENCE A34289 !$#authors Aten, R.F.; Behrman, H.R. !$#journal J. Biol. Chem. (1989) 264:11065-11071 !$#title A gonadotropin-releasing hormone-binding inhibitor from !1bovine ovaries. Purification and identification as histone !1H2A. !$#cross-references MUID:89291845; PMID:2661554 !$#accession A34289 !'##molecule_type protein !'##residues 95-98,'R',100-114 ##label ATE REFERENCE A49741 !$#authors Badamchian, M.; Spangelo, B.L.; Damavandy, T.; MacLeod, !1R.M.; Goldstein, A.L. !$#journal Endocrinology (1991) 128:1580-1588 !$#title Complete amino acid sequence analysis of a peptide isolated !1from the thymus that enhances release of growth hormone and !1prolactin. !$#cross-references MUID:91153254; PMID:1999173 !$#accession A49741 !'##molecule_type protein !'##residues 86-120 ##label BAD CLASSIFICATION #superfamily histone H2A KEYWORDS acetylated amino end; chromosomal protein; DNA binding; !1nucleosome core FEATURE !$1 #modified_site acetylated amino end (Ser) #status !8experimental SUMMARY #length 129 #molecular-weight 13960 #checksum 359 SEQUENCE /// ENTRY HSRT2A #type complete TITLE histone H2A - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1987 #sequence_revision 01-Dec-1995 #text_change 22-Jun-1999 ACCESSIONS S26186; A02591 REFERENCE S26185 !$#authors Huh, N.E.; Hwang, I.; Lim, K.; You, K.H.; Chae, C.B. !$#journal Nucleic Acids Res. (1991) 19:93-98 !$#title Presence of a bi-directional S phase-specific transcription !1regulatory element in the promoter shared by testis-specific !1TH2A and TH2B histone genes. !$#cross-references MUID:91187654; PMID:2011515 !$#accession S26186 !'##status preliminary !'##molecule_type DNA !'##residues 1-130 ##label HUH !'##cross-references EMBL:X59961; NID:g56345; PIDN:CAA42586.1; !1PID:g56347 REFERENCE A02591 !$#authors Laine, B.; Sautiere, P.; Biserte, G. !$#journal Biochemistry (1976) 15:1640-1645 !$#title Primary structure and microheterogeneities of rat !1chloroleukemia histone H-2A (histone ALK, II-b1, or F-2a2). !$#cross-references MUID:76184680; PMID:1268188 !$#accession A02591 !'##molecule_type protein !'##residues 2-16,'S',18-40,'A',42-67,'G',69-99,'K',101-126,'A',128-130 !1##label LAI !'##note three variants were found; the sequence of the major variant is !1shown. Variant 2 differs from that shown in having 99-Arg. !1Variant 3 differs in having 16-Thr and 99-Arg COMMENT This protein was isolated from chloroleukemic tumors. CLASSIFICATION #superfamily histone H2A KEYWORDS chromosomal protein; DNA binding; nucleosome core SUMMARY #length 130 #molecular-weight 14175 #checksum 1373 SEQUENCE /// ENTRY HSHUA5 #type complete TITLE histone H2A.5 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Feb-1997 ACCESSIONS B26318 REFERENCE A26318 !$#authors Zhong, R.; Roeder, R.G.; Heintz, N. !$#journal Nucleic Acids Res. (1983) 11:7409-7425 !$#title The primary structure and expression of four cloned human !1histone genes. !$#cross-references MUID:84069776; PMID:6647026 !$#accession B26318 !'##molecule_type DNA !'##residues 1-129 ##label ZHO !'##note initiator Met not shown CLASSIFICATION #superfamily histone H2A KEYWORDS chromosomal protein; DNA binding; nucleosome core SUMMARY #length 129 #molecular-weight 14053 #checksum 2382 SEQUENCE /// ENTRY HSCH2A #type complete TITLE histone H2A - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Sep-1987 #sequence_revision 03-Mar-2000 #text_change 16-Jun-2000 ACCESSIONS B93556; JC1523; I50657; I50653; I50651; I50655; I50647; !1I50649; A90674; A02591; A23025; S04565; S19236; S19238; !1S19239; S19241 REFERENCE A93556 !$#authors Wang, S.W.; Robins, A.J.; d'Andrea, R.; Wells, J.R.E. !$#journal Nucleic Acids Res. (1985) 13:1369-1387 !$#title Inverted duplication of histone genes in chicken and !1disposition of regulatory sequences. !$#cross-references MUID:85215552; PMID:4000938 !$#accession B93556 !'##molecule_type DNA !'##residues 2-129 ##label WAN !'##cross-references GB:X02218; NID:g63471; PIDN:CAA26139.1; PID:g63475 !'##note initiator Met not shown REFERENCE JC1523 !$#authors Ohshige, T.; Takechi, S.; Nakayama, T. !$#journal Gene (1993) 131:193-199 !$#title Presence of particular transcription regulatory elements in !1the 5'-intergenic region shared by the chicken H2A-III and !1H2B-V pair. !$#cross-references MUID:94010308; PMID:8406011 !$#accession JC1523 !'##molecule_type DNA !'##residues 1-69,'P',71-129 ##label OHS !'##cross-references DDBJ:D11054; NID:g220978; PIDN:BAA01797.1; !1PID:g285697 !'##experimental_source histone H2A-III REFERENCE I50657 !$#authors D'Andrea, R.; Harvey, R.; Wells, J.R. !$#journal Nucleic Acids Res. (1981) 9:3119-3128 !$#title Vertebrate histone genes: nucleotide sequence of a chicken !1H2A gene and regulatory flanking sequences. !$#cross-references MUID:82014895; PMID:6269072 !$#accession I50657 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-49,'L',51-129 ##label DXA !'##cross-references EMBL:V00413; NID:g63447; PIDN:CAA23704.1; !1PID:g63448 REFERENCE I50647 !$#authors Sturm, R.A.; Dalton, S.; Wells, J.R. !$#journal Nucleic Acids Res. (1988) 16:8571-8586 !$#title Conservation of histone H2A/H2B intergene regions: a role !1for the H2B specific element in divergent transcription. !$#cross-references MUID:88335608; PMID:3267232 !$#accession I50653 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-102 ##label STU1 !'##cross-references EMBL:X07763; NID:g63438; PIDN:CAA30589.1; !1PID:g63439 !'##experimental_source clone pCH3.5E !$#accession I50651 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-63 ##label STU2 !'##cross-references EMBL:X07762; NID:g63436; PIDN:CAA30587.1; !1PID:g63437 !'##experimental_source clone pCH22.0B !$#accession I50655 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-25 ##label STU3 !'##cross-references EMBL:X07764; NID:g63441; PIDN:CAA30591.1; !1PID:g63442 !'##experimental_source clone pCH11.0EL !$#accession I50647 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-25 ##label STU4 !'##cross-references EMBL:X07765; NID:g63429; PIDN:CAA30593.1; !1PID:g63430 !'##experimental_source clone pCH11.0ER !$#accession I50649 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-10,'V',12-51,'M',53-93,'HEF' ##label STU5 !'##cross-references EMBL:X07766; NID:g63432; PIDN:CAA30595.1; !1PID:g63433 !'##experimental_source clone CH1-10 REFERENCE A90674 !$#authors Laine, B.; Kmiecik, D.; Sautiere, P.; Biserte, G. !$#journal Biochimie (1978) 60:147-150 !$#title Primary structure of chicken erythrocyte histone H2A. !$#cross-references MUID:78211369; PMID:667168 !$#accession A90674 !'##molecule_type protein !'##residues 2-129 ##label LAI !'##experimental_source erythrocyte GENETICS !$#gene H2A CLASSIFICATION #superfamily histone H2A KEYWORDS acetylated amino end; chromosomal protein; DNA binding; !1nucleosome core; nucleus FEATURE !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental SUMMARY #length 129 #molecular-weight 13940 #checksum 8943 SEQUENCE /// ENTRY HSTR21 #type complete TITLE histone H2A, gonadal - rainbow trout ORGANISM #formal_name Oncorhynchus mykiss #common_name rainbow trout DATE 24-Apr-1984 #sequence_revision 30-Sep-1987 #text_change 22-Jun-1999 ACCESSIONS A92959; A92139; A92107; A02592; A23220 REFERENCE A92959 !$#authors Connor, W.; States, J.C.; Mezquita, J.; Dixon, G.H. !$#journal J. Mol. Evol. (1984) 20:236-250 !$#title Organization and nucleotide sequence of rainbow trout !1histone H2A and H3 genes. !$#cross-references MUID:85083109; PMID:6439879 !$#accession A92959 !'##molecule_type mRNA !'##residues 1-127 ##label CON !'##cross-references GB:X01064; NID:g64324; PIDN:CAA25528.1; PID:g64325 !'##note initiator Met not shown REFERENCE A92139 !$#authors Bailey, G.S.; Dixon, G.H. !$#journal J. Biol. Chem. (1973) 248:5463-5472 !$#title Histone IIb1 from rainbow trout. Comparison in amino acid !1sequence with calf thymus IIB1. !$#cross-references MUID:74071618; PMID:4768909 !$#accession A92139 !'##molecule_type protein !'##residues 1-56,58-78,80-127 ##label BAI REFERENCE A92107 !$#authors Candido, E.P.M.; Dixon, G.H. !$#journal J. Biol. Chem. (1972) 247:3868-3873 !$#title Acetylation of trout testis histones in vivo. Site of the !1modification in histone IIb-1. !$#cross-references MUID:72206029; PMID:5033394 !$#contents acetylation, phosphorylation !$#accession A92107 !'##molecule_type protein !'##residues 1-17 ##label CAN CLASSIFICATION #superfamily histone H2A KEYWORDS acetylated amino end; acetyllysine; chromosomal protein; DNA !1binding; nucleosome core; phosphoprotein; testis FEATURE !$1 #binding_site phosphate (Ser) (covalent) #status !8experimental\ !$1 #modified_site acetylated amino end (Ser) #status !8experimental\ !$5 #binding_site acetyl (Lys) (covalent) #status !8experimental SUMMARY #length 127 #molecular-weight 13600 #checksum 8493 SEQUENCE /// ENTRY HSXLA1 #type complete TITLE histone H2A.1 - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 30-Sep-1987 #sequence_revision 30-Jun-1989 #text_change 22-Jun-1999 ACCESSIONS H24510; A05259 REFERENCE A92918 !$#authors Perry, M.; Thomsen, G.H.; Roeder, R.G. !$#journal J. Mol. Biol. (1985) 185:479-499 !$#title Genomic organization and nucleotide sequence of two distinct !1histone gene clusters from Xenopus laevis. Identification of !1novel conserved upstream sequence elements. !$#cross-references MUID:86037224; PMID:3863963 !$#accession H24510 !'##molecule_type DNA !'##residues 1-130 ##label PER !'##cross-references GB:X03018; NID:g64774; PIDN:CAA26817.1; PID:g64777 !'##note the sequence shown in Figure 5 is incorrect; the correct !1sequence is shown in Figure 9 CLASSIFICATION #superfamily histone H2A KEYWORDS chromosomal protein; DNA binding; nucleosome core FEATURE !$2-130 #product histone H2A.1 #status predicted #label MAT SUMMARY #length 130 #molecular-weight 13966 #checksum 1910 SEQUENCE /// ENTRY HSXLA2 #type complete TITLE histone H2A.2 - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 30-Sep-1987 #sequence_revision 30-Jun-1989 #text_change 16-Feb-1997 ACCESSIONS I24510 REFERENCE A92918 !$#authors Perry, M.; Thomsen, G.H.; Roeder, R.G. !$#journal J. Mol. Biol. (1985) 185:479-499 !$#title Genomic organization and nucleotide sequence of two distinct !1histone gene clusters from Xenopus laevis. Identification of !1novel conserved upstream sequence elements. !$#cross-references MUID:86037224; PMID:3863963 !$#accession I24510 !'##molecule_type DNA !'##residues 1-131 ##label PER !'##note the sequence shown in Figure 5 is incorrect; the correct !1sequence is shown in Figure 9 CLASSIFICATION #superfamily histone H2A KEYWORDS chromosomal protein; DNA binding; nucleosome core FEATURE !$2-131 #product histone H2A.2 #status predicted #label MAT SUMMARY #length 131 #molecular-weight 14113 #checksum 3592 SEQUENCE /// ENTRY HSURA1 #type fragment TITLE histone H2A-beta, sperm - sea urchin (Strongylocentrotus purpuratus) (fragment) ORGANISM #formal_name Strongylocentrotus purpuratus #common_name purple urchin DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 22-Jun-1999 ACCESSIONS C25381 REFERENCE A93078 !$#authors Lieber, T.; Weisser, K.; Childs, G. !$#journal Mol. Cell. Biol. (1986) 6:2602-2612 !$#title Analysis of histone gene expression in adult tissues of the !1sea urchins Strongylocentrotus purpuratus and Lytechinus !1pictus: tissue-specific expression of sperm histone genes. !$#cross-references MUID:87064560; PMID:3785204 !$#accession C25381 !'##molecule_type mRNA !'##residues 1-88 ##label LIE !'##cross-references GB:M13636; NID:g161491; PIDN:AAA30057.1; !1PID:g161492 !'##experimental_source testis CLASSIFICATION #superfamily histone H2A KEYWORDS chromosomal protein; DNA binding; nucleosome core SUMMARY #length 88 #checksum 1521 SEQUENCE /// ENTRY HSURA2 #type fragment TITLE histone H2A, sperm - sea urchin (Lytechinus pictus) (fragment) ORGANISM #formal_name Lytechinus pictus #common_name painted urchin DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 22-Jun-1999 ACCESSIONS D25381 REFERENCE A93078 !$#authors Lieber, T.; Weisser, K.; Childs, G. !$#journal Mol. Cell. Biol. (1986) 6:2602-2612 !$#title Analysis of histone gene expression in adult tissues of the !1sea urchins Strongylocentrotus purpuratus and Lytechinus !1pictus: tissue-specific expression of sperm histone genes. !$#cross-references MUID:87064560; PMID:3785204 !$#accession D25381 !'##molecule_type mRNA !'##residues 1-112 ##label LIE !'##cross-references GB:M13637; NID:g161313; PIDN:AAA30000.1; !1PID:g161314 !'##experimental_source testis CLASSIFICATION #superfamily histone H2A KEYWORDS chromosomal protein; DNA binding; nucleosome core SUMMARY #length 112 #checksum 9798 SEQUENCE /// ENTRY HSUR9M #type complete TITLE histone H2A, gonadal - sea urchin (Psammechinus miliaris) ORGANISM #formal_name Psammechinus miliaris #common_name sand urchin DATE 30-Jun-1979 #sequence_revision 23-Oct-1981 #text_change 16-Feb-1997 ACCESSIONS A38054; A02593 REFERENCE A38054 !$#authors Wouters, D.; Sautiere, P.; Biserte, G. !$#journal Eur. J. Biochem. (1978) 90:231-239 !$#title Primary structure of histone H2A from gonad of the sea !1urchin Psammechinus miliaris. !$#cross-references MUID:79045320; PMID:710427 !$#accession A38054 !'##molecule_type protein !'##residues 1-125 ##label WOU CLASSIFICATION #superfamily histone H2A KEYWORDS acetylated amino end; chromosomal protein; DNA binding; !1nucleosome core FEATURE !$1 #modified_site acetylated amino end (Ser) #status !8experimental SUMMARY #length 125 #molecular-weight 13279 #checksum 6620 SEQUENCE /// ENTRY HSUR9P #type complete TITLE histone H2A, gonadal - sea urchin (Parechinus angulosus) ORGANISM #formal_name Parechinus angulosus #common_name angulate urchin DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Feb-1997 ACCESSIONS A37574; A02593 REFERENCE A37574 !$#authors Strickland, W.N.; Strickland, M.S.; de Groot, P.C.; von !1Holt, C. !$#journal Eur. J. Biochem. (1980) 109:151-158 !$#title The primary structure of histone H2A from the sperm cell of !1the sea urchin Parechinus angulosus. !$#cross-references MUID:81003893; PMID:6997045 !$#accession A37574 !'##molecule_type protein !'##residues 1-125 ##label STR CLASSIFICATION #superfamily histone H2A KEYWORDS acetylated amino end; chromosomal protein; DNA binding FEATURE !$1 #modified_site acetylated amino end (Ser) #status !8experimental SUMMARY #length 125 #molecular-weight 13279 #checksum 6632 SEQUENCE /// ENTRY HSSF2 #type complete TITLE histone H2A - starfish (Asterias rubens) ORGANISM #formal_name Asterias rubens #common_name common European starfish DATE 18-Apr-1984 #sequence_revision 18-Apr-1984 #text_change 16-Feb-1997 ACCESSIONS A02596 REFERENCE A02596 !$#authors Martinage, A.; Belaiche, D.; Dupressoir, T.; Sautiere, P. !$#journal Eur. J. Biochem. (1983) 130:465-472 !$#title Primary structure of histone H2A from gonads of the starfish !1Asterias rubens. !$#cross-references MUID:83131687; PMID:6825703 !$#accession A02596 !'##molecule_type protein !'##residues 1-124 ##label MAR !'##note 18-Ala, 40-Gln, and 50-Asn were also found CLASSIFICATION #superfamily histone H2A KEYWORDS acetylated amino end; chromosomal protein; DNA binding; !1nucleosome core FEATURE !$1 #modified_site acetylated amino end (Ser) #status !8experimental SUMMARY #length 124 #molecular-weight 13266 #checksum 5718 SEQUENCE /// ENTRY HSUR7M #type complete TITLE histone H2A, embryonic - sea urchin (Strongylocentrotus purpuratus) ORGANISM #formal_name Strongylocentrotus purpuratus #common_name purple urchin DATE 31-Jul-1980 #sequence_revision 31-Dec-1991 #text_change 22-Jun-1999 ACCESSIONS A02598 REFERENCE A90777 !$#authors Sures, I.; Lowry, J.; Kedes, L.H. !$#journal Cell (1978) 15:1033-1044 !$#title The DNA sequence of sea urchin (S. purpuratus) H2A, H2B and !1H3 histone coding and spacer regions. !$#cross-references MUID:79084134; PMID:728984 !$#accession A02598 !'##molecule_type DNA !'##residues 1-124 ##label SUR !'##cross-references GB:V01357; NID:g10254; PIDN:CAA24648.1; PID:g809111 CLASSIFICATION #superfamily histone H2A KEYWORDS chromosomal protein; DNA binding; nucleosome core FEATURE !$2-124 #product histone H2A, embryonic #status predicted !8#label MAT SUMMARY #length 124 #molecular-weight 13331 #checksum 6634 SEQUENCE /// ENTRY HSURH9 #type complete TITLE histone H2A, embryonic (clone h19) - sea urchin (Psammechinus miliaris) ORGANISM #formal_name Psammechinus miliaris #common_name sand urchin DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 22-Jun-1999 ACCESSIONS A93719; A02598 REFERENCE A93719 !$#authors Busslinger, M.; Portmann, R.; Irminger, J.C.; Birnstiel, !1M.L. !$#journal Nucleic Acids Res. (1980) 8:957-977 !$#title Ubiquitous and gene-specific regulatory 5' sequences in a !1sea urchin histone DNA clone coding for histone protein !1variants. !$#cross-references MUID:81076674; PMID:7443547 !$#accession A93719 !'##molecule_type DNA !'##residues 1-124 ##label BUS !'##cross-references GB:M10559; NID:g161382; PIDN:AAA30027.1; !1PID:g161388 CLASSIFICATION #superfamily histone H2A KEYWORDS chromosomal protein; DNA binding; nucleosome core FEATURE !$2-124 #product histone H2A, embryonic (clone h19) #status !8predicted #label MAT SUMMARY #length 124 #molecular-weight 13331 #checksum 6634 SEQUENCE /// ENTRY HSURH2 #type complete TITLE histone H2A, embryonic (clone h22) - sea urchin (Psammechinus miliaris) ORGANISM #formal_name Psammechinus miliaris #common_name sand urchin DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 21-Jul-2000 ACCESSIONS A90776; A02598 REFERENCE A90776 !$#authors Schaffner, W.; Kunz, G.; Daetwyler, H.; Telford, J.; Smith, !1H.O.; Birnstiel, M.L. !$#journal Cell (1978) 14:655-671 !$#title Genes and spacers of cloned sea urchin histone DNA analyzed !1by sequencing. !$#cross-references MUID:79001915; PMID:688387 !$#accession A90776 !'##molecule_type DNA !'##residues 1-124 ##label SCH !'##cross-references GB:V01141; NID:g161395; PIDN:AAB59207.1; !1PID:g161402 !'##note this is the major H2A component in this species CLASSIFICATION #superfamily histone H2A KEYWORDS chromosomal protein; DNA binding; nucleosome core FEATURE !$2-124 #product histone H2A, embryonic (clone h22) #status !8predicted #label MAT SUMMARY #length 124 #molecular-weight 13303 #checksum 6660 SEQUENCE /// ENTRY HSKW2A #type complete TITLE histone H2A - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 30-Sep-1988 #sequence_revision 19-Oct-1995 #text_change 17-Mar-2000 ACCESSIONS S04238; A27790; T16286; T18659; T20596; T22660; T23030; !1T24790; T25163; T27742; T27744; T28962; T29228; T30053; !1T30056; T33002 REFERENCE S04238 !$#authors Roberts, S.B.; Emmons, S.W.; Childs, G. !$#journal J. Mol. Biol. (1989) 206:567-577 !$#title Nucleotide sequences of Caenorhabditis elegans core histone !1genes. Genes for different histone classes share common !1flanking sequence elements. !$#cross-references MUID:89293823; PMID:2544730 !$#accession S04238 !'##molecule_type DNA !'##residues 1-127 ##label ROB !'##cross-references EMBL:X15633; NID:g6753; PIDN:CAA33641.1; PID:g6754 REFERENCE A27790 !$#authors Vanfleteren, J.R.; Van Bun, S.M.; Van Beeumen, J.J. !$#journal Biochem. J. (1987) 243:297-300 !$#title The primary structure of histone H2A from the nematode !1Caenorhabditis elegans. !$#cross-references MUID:87270639; PMID:3606579 !$#accession A27790 !'##molecule_type protein !'##residues 2-127 ##label VAN !'##experimental_source strain DR27 daf-17[m27] REFERENCE Z18490 !$#authors Woessner, J. !$#submission submitted to the EMBL Data Library, November 1995 !$#description The sequence of C. elegans cosmid F35H10. !$#accession T16286 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-127 ##label WOE !'##cross-references EMBL:U40934; NID:g1072149; PID:g1072158; !1PIDN:AAA81686.1; CESP:F35H10.1 REFERENCE Z19002 !$#authors White, S. !$#submission submitted to the EMBL Data Library, May 1996 !$#accession T18659 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-127 ##label WIL !'##cross-references EMBL:Z73102; PIDN:CAA97414.1; GSPDB:GN00022; !1CESP:B0035.7 !'##experimental_source clone B0035 REFERENCE Z19298 !$#authors Wallis, J. !$#submission submitted to the EMBL Data Library, November 1996 !$#accession T20596 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-127 ##label WI2 !'##cross-references EMBL:Z81495; PIDN:CAB04056.1; GSPDB:GN00020; !1CESP:F08G2.2 !'##experimental_source clone F08G2 REFERENCE Z19594 !$#authors White, S.; Mortimore, B. !$#submission submitted to the EMBL Data Library, November 1996 !$#accession T22660 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-127 ##label WI3 !'##cross-references EMBL:Z82271; PIDN:CAB05212.1; GSPDB:GN00022; !1CESP:F54E12.5 !'##experimental_source clone F54E12 REFERENCE Z19656 !$#authors McLay, K. !$#submission submitted to the EMBL Data Library, March 1997 !$#accession T23030 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-127 ##label WI4 !'##cross-references EMBL:Z92789; PIDN:CAB07221.1; GSPDB:GN00022; !1CESP:H02I12.7 !'##experimental_source clone H02I12 REFERENCE Z19936 !$#authors McMurray, A. !$#submission submitted to the EMBL Data Library, March 1997 !$#accession T24790 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-127 ##label WI5 !'##cross-references EMBL:Z93388; PIDN:CAB07656.1; GSPDB:GN00023; !1CESP:T10C6.12 !'##experimental_source clone T10C6 REFERENCE Z19989 !$#authors Wild, A. !$#submission submitted to the EMBL Data Library, October 1996 !$#accession T25163 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-127 ##label WI6 !'##cross-references EMBL:Z81128; PIDN:CAB03399.1; GSPDB:GN00019; !1CESP:T23D8.6 !'##experimental_source clone T23D8 REFERENCE Z20413 !$#authors Steward, C. !$#submission submitted to the EMBL Data Library, December 1996 !$#accession T27742 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-127 ##label WI7 !'##cross-references EMBL:Z83245; PIDN:CAB05836.1; GSPDB:GN00020; !1CESP:ZK131.6 !'##experimental_source clone ZK131 !$#accession T27744 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-127 ##label WI8 !'##cross-references EMBL:Z83245; PIDN:CAB05838.1; GSPDB:GN00020; !1CESP:ZK131.10 !'##experimental_source clone ZK131 REFERENCE Z20548 !$#authors Davidson, S.; Wohldmann, P. !$#submission submitted to the EMBL Data Library, July 1996 !$#description The sequence of C. elegans cosmid F45F2. !$#accession T28962 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-127 ##label DAV !'##cross-references EMBL:U64845; PIDN:AAC48024.1; GSPDB:GN00023; !1CESP:F45F2.4 !'##experimental_source strain Bristol N2; clone F45F2 REFERENCE Z20591 !$#authors Murray, J.; Le, T.T. !$#submission submitted to the EMBL Data Library, May 1996 !$#description The sequence of C. elegans cosmid F55G1. !$#accession T29228 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-127 ##label MUR !'##cross-references EMBL:U58750; PIDN:AAB00647.1; GSPDB:GN00022; !1CESP:F55G1.10 !'##experimental_source strain Bristol N2; clone F55G1 REFERENCE Z20728 !$#authors Miller, N.; Bradshaw, H. !$#submission submitted to the EMBL Data Library, July 1996 !$#description The sequence of C. elegans cosmid K06C4. !$#accession T30053 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-127 ##label MIL !'##cross-references EMBL:U64843; PIDN:AAB04853.1; GSPDB:GN00023; !1CESP:K06C4.11 !'##experimental_source strain Bristol N2; clone K06C4 !$#accession T30056 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-127 ##label MI2 !'##cross-references EMBL:U64843; PIDN:AAB04856.1; GSPDB:GN00023; !1CESP:K06C4.3 !'##experimental_source strain Bristol N2; clone K06C4 REFERENCE Z21262 !$#authors Woessner, J. !$#submission submitted to the EMBL Data Library, February 1998 !$#description The sequence of C. elegans cosmid F17E9. !$#accession T33002 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-127 ##label WO2 !'##cross-references EMBL:AF047656; PIDN:AAC05100.1; GSPDB:GN00022; !1CESP:F17E9.13 !'##experimental_source strain Bristol N2; clone F17E9 COMMENT 25%, 10%, and 15% of the lysine residues at positions 6, 9, !1and 11, respectively, are acetylated. GENETICS H01 !$#gene his-12 GENETICS H02 !$#gene CESP:B0035.7 !$#map_position 4 GENETICS H03 !$#gene CESP:F08G2.2 !$#map_position 2 GENETICS H04 !$#gene CESP:F54E12.5 !$#map_position 4 GENETICS H05 !$#gene CESP:H02I12.7 !$#map_position 4 GENETICS H06 !$#gene CESP:T10C6.12 !$#map_position 5 GENETICS H07 !$#gene CESP:T23D8.6 !$#map_position 1 GENETICS H08 !$#gene CESP:ZK131.6 !$#map_position 2 GENETICS H09 !$#gene CESP:ZK131.10 !$#map_position 2 !$#note ; Gene: CESP:F55G1.10; Map position: 4 !$#note ; Gene: CESP:K06C4.11; Map position: 5 !$#note ; Gene: CESP:F45F2.4; Map position: 4 !$#note ; Gene: CESP:K06C4.3; Map position: 5 !$#note ; Gene: CESP:F17E9.13; Map position: 4 !$#note histones exist in large multigene families; it is possible !1that some of the genes shown here represent the same gene CLASSIFICATION #superfamily histone H2A KEYWORDS acetyllysine; blocked amino end; chromosomal protein; DNA !1binding; nucleosome core FEATURE !$2 #modified_site blocked amino end (Ser) (in mature !8form) (probably acetylated) #status experimental\ !$6,9,11 #binding_site acetyl (Lys) (covalent) (partial) !8#status experimental SUMMARY #length 127 #molecular-weight 13404 #checksum 7735 SEQUENCE /// ENTRY HSFF2 #type complete TITLE histone H2A - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 31-Oct-1980 #sequence_revision 15-Oct-1996 #text_change 22-Jun-1999 ACCESSIONS S10094; A58168; A02594 REFERENCE S10094 !$#authors Matsuo, Y.; Yamazaki, T. !$#journal Nucleic Acids Res. (1989) 17:225-238 !$#title tRNA derived insertion element in histone gene repeating !1unit of Drosophila melanogaster. !$#cross-references MUID:89098383; PMID:2536150 !$#accession S10094 !'##molecule_type DNA !'##residues 1-63 ##label MAS !'##cross-references EMBL:X14215; NID:g8066; PIDN:CAA32431.1; PID:g8067 !'##note translation of initiator Met is not shown !$#accession A58168 !'##molecule_type DNA !'##residues 64-124 ##label MA2 !'##cross-references EMBL:X14215; NID:g8066; PIDN:CAA32436.1; PID:g8072 !'##note the complete nucleic acid sequence is shown split in two clone !1fragments; there is no intron REFERENCE A02630 !$#authors Goldberg, M.L. !$#citation Ph.D. thesis, Stanford Univ., 1979 !$#accession A02594 !'##molecule_type DNA !'##residues 2-122 ##label GOL GENETICS !$#gene FlyBase:His2A !'##cross-references FlyBase:FBgn0001196 !$#introns #status absent CLASSIFICATION #superfamily histone H2A KEYWORDS chromosomal protein; DNA binding; nucleosome core FEATURE !$2-124 #product histone H2A #status predicted #label MAT SUMMARY #length 124 #molecular-weight 13363 #checksum 5636 SEQUENCE /// ENTRY HSIN21 #type complete TITLE histone H2A - sipunculid (Sipunculus nudus) ORGANISM #formal_name Sipunculus nudus DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 16-Feb-1997 ACCESSIONS A02597 REFERENCE A02597 !$#authors Kmiecik, D.; Couppez, M.; Belaiche, D.; Sautiere, P. !$#journal Eur. J. Biochem. (1983) 135:113-121 !$#title Primary structure of histone H2A from nucleated erythrocyte !1of the marine worm Sipunculus nudus. Presence of two forms !1of H2A in the sipunculid chromatin. !$#cross-references MUID:83287386; PMID:6349995 !$#accession A02597 !'##molecule_type protein !'##residues 1-123 ##label KMI CLASSIFICATION #superfamily histone H2A KEYWORDS acetylated amino end; chromosomal protein; DNA binding; !1nucleosome core; phosphoprotein FEATURE !$1 #modified_site acetylated amino end (Ser) #status !8experimental\ !$1 #binding_site phosphate (Ser) (covalent) (partial) !8#status experimental SUMMARY #length 123 #molecular-weight 13221 #checksum 4744 SEQUENCE /// ENTRY HSOO2 #type complete TITLE histone H2A - common cuttlefish ORGANISM #formal_name Sepia officinalis #common_name common cuttlefish DATE 18-Apr-1984 #sequence_revision 18-Apr-1984 #text_change 16-Feb-1997 ACCESSIONS A02595 REFERENCE A02595 !$#authors Wouters-Tyrou, D.; Martin-Ponthieu, A.; Briand, G.; !1Sautiere, P.; Biserte, G. !$#journal Eur. J. Biochem. (1982) 124:489-498 !$#title The amino-acid sequence of histone H2A from cuttlefish Sepia !1officinalis. !$#cross-references MUID:82261665; PMID:7049696 !$#accession A02595 !'##molecule_type protein !'##residues 1-124 ##label WOU CLASSIFICATION #superfamily histone H2A KEYWORDS acetylated amino end; chromosomal protein; DNA binding; !1nucleosome core FEATURE !$1 #modified_site acetylated amino end (Ser) #status !8experimental SUMMARY #length 124 #molecular-weight 13289 #checksum 6472 SEQUENCE /// ENTRY HSZPA2 #type complete TITLE histone H2A.1 - fission yeast (Schizosaccharomyces pombe) ORGANISM #formal_name Schizosaccharomyces pombe DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 10-Dec-1999 ACCESSIONS B27399; T41488 REFERENCE A91027 !$#authors Matsumoto, S.; Yanagida, M. !$#journal EMBO J. (1985) 4:3531-3538 !$#title Histone gene organization of fission yeast: a common !1upstream sequence. !$#cross-references MUID:86135992; PMID:4092687 !$#accession B27399 !'##molecule_type DNA !'##residues 1-132 ##label MATS !'##cross-references GB:X05220; NID:g4957; PIDN:CAA28848.1; PID:g4959 REFERENCE Z21998 !$#authors Seeger, K.; Harris, D.; Lyne, M.; Rajandream, M.A.; Barrell, !1B.G. !$#submission submitted to the EMBL Data Library, October 1998 !$#accession T41488 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-132 ##label SEE !'##cross-references EMBL:AL033127; PIDN:CAA21864.1; GSPDB:GN00068; !1SPDB:SPCC622.08c !'##experimental_source strain 972h-; cosmid c622 GENETICS !$#gene SPCC622.08c !$#map_position 3 CLASSIFICATION #superfamily histone H2A KEYWORDS chromosomal protein; DNA binding; nucleosome core FEATURE !$2-132 #product histone H2A.1 #status predicted #label MAT SUMMARY #length 132 #molecular-weight 13878 #checksum 4241 SEQUENCE /// ENTRY HSZPA3 #type complete TITLE histone H2A.2 - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES histone H2A-beta ORGANISM #formal_name Schizosaccharomyces pombe DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 21-Jul-2000 ACCESSIONS C27399; T37993; T43332 REFERENCE A91027 !$#authors Matsumoto, S.; Yanagida, M. !$#journal EMBO J. (1985) 4:3531-3538 !$#title Histone gene organization of fission yeast: a common !1upstream sequence. !$#cross-references MUID:86135992; PMID:4092687 !$#accession C27399 !'##molecule_type DNA !'##residues 1-131 ##label MATS !'##cross-references GB:X05221; NID:g4960; PIDN:CAA28849.1; PID:g4961 REFERENCE Z21760 !$#authors Oliver, K.; Harris, D.; Wood, V.; Barrell, B.G.; Rajandream, !1M.A. !$#submission submitted to the EMBL Data Library, June 1997 !$#accession T37993 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-131 ##label OLI !'##cross-references EMBL:Z97209; PIDN:CAB10117.1; GSPDB:GN00066; !1SPDB:SPAC19G12.06c !'##experimental_source strain 972h-; cosmid c19G12 REFERENCE Z22433 !$#authors Choe, J.; Schuster, T.; Grunstein, M. !$#journal Mol. Cell. Biol. (1985) 5:3261-3269 !$#title Organization, primary structure, and evolution of histone !1H2A and H2B genes of the fission yeast Schizosaccharomyces !1pombe. !$#cross-references MUID:86310796; PMID:3018512 !$#accession T43332 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-131 ##label CHO !'##cross-references EMBL:M11500; NID:g173401; PIDN:AAA35310.1; !1PID:g173402 GENETICS !$#gene SPAC19G12.06c !$#map_position 1 CLASSIFICATION #superfamily histone H2A KEYWORDS chromosomal protein; DNA binding; nucleosome core; nucleus FEATURE !$2-131 #product histone H2A.2 #status predicted #label MAT SUMMARY #length 131 #molecular-weight 13776 #checksum 2691 SEQUENCE /// ENTRY HSBYA1 #type complete TITLE histone H2A.1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YD9934.10; protein YDR225w ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 21-Jul-2000 ACCESSIONS S05813; S47933; S53986; S59432; S47474; S47948 REFERENCE S05813 !$#authors Choe, J.; Kolodrubetz, D.; Grunstein, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:1484-1487 !$#title The two yeast histone H2A genes encode similar protein !1subtypes. !$#cross-references MUID:82174624; PMID:7041122 !$#accession S05813 !'##molecule_type DNA !'##residues 1-132 ##label CHO !'##cross-references EMBL:V01304; NID:g3750; PIDN:CAA24611.1; PID:g3751 REFERENCE S47932 !$#authors Davies, C.J.; Hutchison III, C.A. !$#submission submitted to the EMBL Data Library, September 1994 !$#description Tn3 transposon/deletion sequencing of a 9.4kb DNA fragment: !1Characterisation of Tn3 insertion-site specificity and !1analysis of transpositional 'hot' and 'cold' spots. !$#accession S47933 !'##molecule_type DNA !'##residues 1-132 ##label DAV !'##cross-references EMBL:L35344; EMBL:U13239; EMBL:Z36548 REFERENCE S53985 !$#authors Davies, C.J.; Hutchison III, C.A. !$#journal Nucleic Acids Res. (1995) 23:507-514 !$#title Insertion site specificity of the transposon Tn3. !$#cross-references MUID:95192063; PMID:7885847 !$#accession S53986 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-132 ##label DAW !'##cross-references EMBL:U13239; NID:g532747; PIDN:AAC33142.1; !1PID:g532749 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE S59423 !$#authors Murphy, L.; Harris, D. !$#submission submitted to the EMBL Data Library, March 1995 !$#accession S59432 !'##molecule_type DNA !'##residues 1-132 ##label MUR !'##cross-references EMBL:Z48612; NID:g728671; PIDN:CAA88505.1; !1PID:g728681; GSPDB:GN00004; MIPS:YDR225w !'##experimental_source strain AB972 GENETICS !$#gene SGD:HTA1; H2A1; MIPS:YDR225w !'##cross-references SGD:S0002633; MIPS:YDR225w !$#map_position 4R CLASSIFICATION #superfamily histone H2A KEYWORDS chromosomal protein; DNA binding; nucleosome core FEATURE !$2-132 #product histone H2A.1 #status predicted #label MAT SUMMARY #length 132 #molecular-weight 13989 #checksum 5116 SEQUENCE /// ENTRY HSBYA2 #type complete TITLE histone H2A.2 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein YBL003c; hypothetical protein YBL0103 ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 05-Nov-1999 ACCESSIONS S05814; S44557; S45732; S45268; S37319 REFERENCE S05813 !$#authors Choe, J.; Kolodrubetz, D.; Grunstein, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:1484-1487 !$#title The two yeast histone H2A genes encode similar protein !1subtypes. !$#cross-references MUID:82174624; PMID:7041122 !$#accession S05814 !'##molecule_type DNA !'##residues 1-132 ##label CHO !'##cross-references EMBL:V01305; NID:g3752; PIDN:CAA24612.1; PID:g3753 REFERENCE S44556 !$#authors Wolfe, K.H.; Lohan, A.J.E. !$#journal Yeast (1994) 10(Suppl.A):S41-S46 !$#title Sequence around the centromere of Saccharomyces cerevisiae !1chromosome II: similarity of CEN2 to CEN4. !$#cross-references MUID:94378721; PMID:8091860 !$#accession S44557 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-132 ##label WOL !'##cross-references EMBL:Z26494; NID:g403311; PIDN:CAA81267.1; !1PID:g403313 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1September 1993 REFERENCE S45730 !$#authors Lohan, A.J.E.; Wolfe, K.H. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S45732 !'##molecule_type DNA !'##residues 1-132 ##label LOH !'##cross-references EMBL:Z35764; NID:g535977; PIDN:CAA84818.1; !1PID:g535978; GSPDB:GN00002; MIPS:YBL003c REFERENCE A91100 !$#authors Brandt, W.F.; Patterson, K.; von Holt, C. !$#journal Eur. J. Biochem. (1980) 110:67-76 !$#title The histones of yeast. The isolation and partial structure !1of the core histones. !$#cross-references MUID:81066651; PMID:7002547 !$#accession S45268 !'##molecule_type protein !'##residues 45-46,'T',48-64 ##label BRA GENETICS !$#gene SGD:HTA2; H2A2; MIPS:YBL003c !'##cross-references SGD:S0000099; MIPS:YBL003c !$#map_position 2L CLASSIFICATION #superfamily histone H2A KEYWORDS chromosomal protein; DNA binding; nucleosome core FEATURE !$2-132 #product histone H2A.2 #status predicted #label MAT SUMMARY #length 132 #molecular-weight 13989 #checksum 5097 SEQUENCE /// ENTRY HSTE92 #type complete TITLE histone H2A.2 - Tetrahymena pyriformis ORGANISM #formal_name Tetrahymena pyriformis DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 07-Dec-1999 ACCESSIONS A02601 REFERENCE A91969 !$#authors Fusauchi, Y.; Iwai, K. !$#journal J. Biochem. (1983) 93:1487-1497 !$#title Tetrahymena histone II2A. Isolation and two variant !1sequences. !$#cross-references MUID:83290791; PMID:6885734 !$#accession A02601 !'##molecule_type protein !'##residues 1-132 ##label FUS GENETICS !$#genetic_code SGC5 CLASSIFICATION #superfamily histone H2A KEYWORDS chromosomal protein; DNA binding; nucleosome core SUMMARY #length 132 #molecular-weight 14126 #checksum 3514 SEQUENCE /// ENTRY HSTE91 #type complete TITLE histone H2A.1 - Tetrahymena pyriformis ORGANISM #formal_name Tetrahymena pyriformis DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 07-Dec-1999 ACCESSIONS A02600 REFERENCE A91969 !$#authors Fusauchi, Y.; Iwai, K. !$#journal J. Biochem. (1983) 93:1487-1497 !$#title Tetrahymena histone II2A. Isolation and two variant !1sequences. !$#cross-references MUID:83290791; PMID:6885734 !$#accession A02600 !'##molecule_type protein !'##residues 1-137 ##label FUS GENETICS !$#genetic_code SGC5 CLASSIFICATION #superfamily histone H2A KEYWORDS chromosomal protein; DNA binding; nucleosome core SUMMARY #length 137 #molecular-weight 14654 #checksum 1517 SEQUENCE /// ENTRY HSWT91 #type complete TITLE histone H2A.1 - wheat ORGANISM #formal_name Triticum aestivum #common_name common wheat DATE 31-May-1980 #sequence_revision 04-Dec-1986 #text_change 16-Feb-1997 ACCESSIONS A02602 REFERENCE A02602 !$#authors Rodrigues, J.A.; Brandt, W.F.; von Holt, C. !$#journal Eur. J. Biochem. (1985) 150:499-506 !$#title The amino acid sequence of wheat histone H2A-(1). A core !1histone with a C-terminal extension. !$#cross-references MUID:85257682; PMID:4018096 !$#accession A02602 !'##molecule_type protein !'##residues 1-145 ##label ROD !'##experimental_source germ CLASSIFICATION #superfamily histone H2A KEYWORDS chromosomal protein; DNA binding; nucleosome core; !1structural protein SUMMARY #length 145 #molecular-weight 15455 #checksum 9700 SEQUENCE /// ENTRY HSWT2A #type complete TITLE histone H2A.2 - wheat ORGANISM #formal_name Triticum aestivum #common_name common wheat DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 12-Apr-1996 ACCESSIONS S00623; A02603 REFERENCE S00623 !$#authors de Andrade Rodrigues, J.; Brandt, W.F.; von Holt, C. !$#journal Eur. J. Biochem. (1988) 173:555-560 !$#title The primary structure of the histone H2A(2) type from wheat !1germ. A core histone type with both, N-terminal and !1C-terminal extensions. !$#cross-references MUID:88225070; PMID:3371346 !$#accession S00623 !'##molecule_type protein !'##residues 1-151 ##label DE1 !'##note 3-Ala, 6-Leu, 11-Gly, 24-Arg, 83-Ser, and 94-Val were also !1found REFERENCE A90629 !$#authors Rodrigues, J.A.; Brandt, W.F.; von Holt, C. !$#journal Biochim. Biophys. Acta (1979) 578:196-206 !$#title Plant histone 2 from wheat germ, a family of histone H2A !1variants. !$#cross-references MUID:79209696; PMID:454665 !$#accession A02603 !'##molecule_type protein !'##residues 1-37 ##label ROD !'##experimental_source germ CLASSIFICATION #superfamily histone H2A KEYWORDS acetylated amino end; chromosomal protein; DNA binding; !1nucleosome core FEATURE !$1 #modified_site acetylated amino end (Met) #status !8experimental SUMMARY #length 151 #molecular-weight 16013 #checksum 5620 SEQUENCE /// ENTRY HSCH2F #type complete TITLE histone H2A.F, embryonic - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 03-Aug-1984 #sequence_revision 14-Nov-1997 #text_change 22-Jun-1999 ACCESSIONS S03282; A02599 REFERENCE S03282 !$#authors Dalton, S.; Robins, A.J.; Harvey, R.P.; Wells, J.R.E. !$#journal Nucleic Acids Res. (1989) 17:1745-1756 !$#title Transcription from the intron-containing chicken histone !1H2A.(F) gene is not S-phase regulated. !$#cross-references MUID:89160327; PMID:2493634 !$#accession S03282 !'##molecule_type DNA !'##residues 1-128 ##label DAL !'##cross-references EMBL:X13894 !'##note the authors translated the codon TAC for residue 54 as Thr and !1GGC for residue 71 as Glu REFERENCE A02599 !$#authors Harvey, R.P.; Whiting, J.A.; Coles, L.S.; Krieg, P.A.; !1Wells, J.R.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:2819-2823 !$#title H2A.F: an extremely variant histone H2A sequence expressed !1in the chicken embryo. !$#cross-references MUID:83221493; PMID:6574451 !$#accession A02599 !'##molecule_type DNA !'##residues 2-128 ##label HAR !'##cross-references GB:V00414; GB:J00868; NID:g63465; PIDN:CAA23705.1; !1PID:g63466 GENETICS !$#gene H2A.F !$#introns 1/3; 27/3; 65/3; 109/1 CLASSIFICATION #superfamily histone H2A KEYWORDS chromosomal protein; DNA binding; nucleosome core; nucleus SUMMARY #length 128 #molecular-weight 13509 #checksum 7249 SEQUENCE /// ENTRY HSWT93 #type fragment TITLE histone H2A.3 - wheat (fragment) ORGANISM #formal_name Triticum aestivum #common_name common wheat DATE 31-May-1980 #sequence_revision 31-May-1980 #text_change 16-Feb-1997 ACCESSIONS A02604 REFERENCE A90629 !$#authors Rodrigues, J.A.; Brandt, W.F.; von Holt, C. !$#journal Biochim. Biophys. Acta (1979) 578:196-206 !$#title Plant histone 2 from wheat germ, a family of histone H2A !1variants. !$#cross-references MUID:79209696; PMID:454665 !$#accession A02604 !'##molecule_type protein !'##residues 1-37 ##label ROD !'##experimental_source germ CLASSIFICATION #superfamily histone H2A KEYWORDS acetylated amino end; chromosomal protein; DNA binding; !1nucleosome core FEATURE !$1 #modified_site acetylated amino end (Met) #status !8experimental SUMMARY #length 37 #checksum 3863 SEQUENCE /// ENTRY HSHUB1 #type complete TITLE histone H2B.1 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1987 #sequence_revision 06-Jan-1995 #text_change 22-Jun-1999 ACCESSIONS A26318; A32955 REFERENCE A26318 !$#authors Zhong, R.; Roeder, R.G.; Heintz, N. !$#journal Nucleic Acids Res. (1983) 11:7409-7425 !$#title The primary structure and expression of four cloned human !1histone genes. !$#cross-references MUID:84069776; PMID:6647026 !$#accession A26318 !'##molecule_type DNA !'##residues 1-125 ##label ZHO !'##cross-references GB:X00088; NID:g32112; PIDN:CAA24950.1; PID:g32113 REFERENCE A32955 !$#authors Alnemri, E.S.; Litwack, G. !$#journal J. Biol. Chem. (1989) 264:4104-4111 !$#title Glucocorticoid-induced lymphocytolysis is not mediated by an !1induced endonuclease. !$#cross-references MUID:89139481; PMID:2917990 !$#accession A32955 !'##molecule_type protein !'##residues 2-27 ##label ALN CLASSIFICATION #superfamily histone H2B KEYWORDS chromosomal protein; DNA binding; nucleosome core FEATURE !$2-125 #product histone H2B.1 #status predicted #label MAT SUMMARY #length 125 #molecular-weight 13615 #checksum 8464 SEQUENCE /// ENTRY HSHUB2 #type complete TITLE histone H2B [validated] - human ALTERNATE_NAMES histone H2B.1(a); histone H2B.2 ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1987 #sequence_revision 15-Oct-1999 #text_change 08-Dec-2000 ACCESSIONS E40335; A91951; A02605 REFERENCE A40335 !$#authors Albig, W.; Kardalinou, E.; Drabent, B.; Zimmer, A.; !1Doenecke, D. !$#journal Genomics (1991) 10:940-948 !$#title Isolation and characterization of two human H1 histone genes !1within clusters of core histone genes. !$#cross-references MUID:92009931; PMID:1916825 !$#accession E40335 !'##status preliminary !'##molecule_type DNA !'##residues 1-126 ##label ALB !'##cross-references GB:M60750; NID:g184077; PIDN:AAA63189.1; !1PID:g184078 REFERENCE A91951 !$#authors Ohe, Y.; Hayashi, H.; Iwai, K. !$#journal J. Biochem. (1979) 85:615-624 !$#title Human spleen histone H2B. Isolation and amino acid sequence. !$#cross-references MUID:79130392; PMID:422550 !$#accession A91951 !'##molecule_type protein !'##residues 2-126 ##label OHE !'##note 40-Ile and 125-Ala were found in 25% and 30% of the molecules, !1respectively GENETICS !$#gene GDB:H2B; H2B.2 !'##cross-references GDB:126843 !$#map_position 1q21-1q23 CLASSIFICATION #superfamily histone H2B KEYWORDS chromosomal protein; DNA binding; nucleosome core; nucleus FEATURE !$2-126 #product histone H2B #status experimental #label MAT SUMMARY #length 126 #molecular-weight 13906 #checksum 1662 SEQUENCE /// ENTRY HSBO22 #type complete TITLE histone H2B - bovine ALTERNATE_NAMES bone morphogenetic protein; brain capillary plasma membrane 17K protein ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 28-Feb-1980 #sequence_revision 13-Jul-1981 #text_change 16-Feb-1997 ACCESSIONS A02605; A29374; PL0131 REFERENCE A91929 !$#authors Iwai, K.; Hayashi, H.; Ishikawa, K. !$#journal J. Biochem. (1972) 72:357-367 !$#title Calf thymus lysine- and serine-rich histone. III. Complete !1amino acid sequence and its implication for interactions of !1histones with DNA. !$#cross-references MUID:73069077; PMID:4644305 !$#accession A02605 !'##molecule_type protein !'##residues 1-125 ##label IWA !'##note this is the last paper in a series characterizing the complete !1sequence REFERENCE A29374 !$#authors Urist, M.R.; Huo, Y.K.; Brownell, A.G.; Hohl, W.M.; Buyske, !1J.; Lietze, A.; Tempst, P.; Hunkapiller, M.; DeLange, R.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:371-375 !$#title Purification of bovine bone morphogenetic protein by !1hydroxyapatite chromatography. !$#cross-references MUID:84119489; PMID:6320184 !$#accession A29374 !'##molecule_type protein !'##residues 1-19,'T',21-25 ##label URI REFERENCE PL0130 !$#authors Pardridge, W.M.; Nowlin, D.M.; Calaycay, J.; Shively, J.E. !$#journal J. Neurochem. (1989) 53:1014-1018 !$#title Predominant low-molecular-weight proteins in isolated brain !1capillaries are histones. !$#cross-references MUID:89361419; PMID:2769252 !$#accession PL0131 !'##molecule_type protein !'##residues 1-9 ##label PAR CLASSIFICATION #superfamily histone H2B KEYWORDS chromosomal protein; DNA binding; nucleosome core SUMMARY #length 125 #molecular-weight 13775 #checksum 308 SEQUENCE /// ENTRY HSXLB1 #type complete TITLE histone H2B.1 - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 30-Jun-1979 #sequence_revision 30-Sep-1987 #text_change 22-Jun-1999 ACCESSIONS B92918; A90626; A02608; A24510 REFERENCE A92918 !$#authors Perry, M.; Thomsen, G.H.; Roeder, R.G. !$#journal J. Mol. Biol. (1985) 185:479-499 !$#title Genomic organization and nucleotide sequence of two distinct !1histone gene clusters from Xenopus laevis. Identification of !1novel conserved upstream sequence elements. !$#cross-references MUID:86037224; PMID:3863963 !$#accession B92918 !'##molecule_type DNA !'##residues 1-125 ##label PER !'##cross-references GB:X03018; NID:g64774; PIDN:CAA26816.1; PID:g64776 !'##experimental_source clone X1h3 !'##note initiator Met not shown REFERENCE A90626 !$#authors Van Helden, P.; Strickland, W.N.; Brandt, W.F.; von Holt, C. !$#journal Biochim. Biophys. Acta (1978) 533:278-281 !$#title Histone H2B variants from the erythrocytes of an amphibian, !1a reptile and a bird. !$#cross-references MUID:78144893; PMID:638193 !$#accession A90626 !'##molecule_type protein !'##residues 1-29;62-84 ##label VAN !'##experimental_source erythrocyte CLASSIFICATION #superfamily histone H2B KEYWORDS chromosomal protein; DNA binding; nucleosome core SUMMARY #length 125 #molecular-weight 13803 #checksum 9521 SEQUENCE /// ENTRY HSXLB2 #type complete TITLE histone H2B.2 - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 22-Jun-1999 ACCESSIONS B24510; A02608 REFERENCE A92918 !$#authors Perry, M.; Thomsen, G.H.; Roeder, R.G. !$#journal J. Mol. Biol. (1985) 185:479-499 !$#title Genomic organization and nucleotide sequence of two distinct !1histone gene clusters from Xenopus laevis. Identification of !1novel conserved upstream sequence elements. !$#cross-references MUID:86037224; PMID:3863963 !$#accession B24510 !'##molecule_type DNA !'##residues 1-125 ##label PER !'##cross-references GB:X03017; NID:g64766; PIDN:CAA26811.1; PID:g64770 !'##experimental_source clone X1h1 !'##note initiator Met not shown CLASSIFICATION #superfamily histone H2B KEYWORDS chromosomal protein; DNA binding; nucleosome core SUMMARY #length 125 #molecular-weight 13774 #checksum 9352 SEQUENCE /// ENTRY HSSB22 #type complete TITLE histone H2B, gonadal - brown trout ORGANISM #formal_name Salmo trutta #common_name brown trout DATE 30-Jun-1979 #sequence_revision 13-Jul-1981 #text_change 16-Feb-1997 ACCESSIONS A02609 REFERENCE A02609 !$#authors Kootstra, A.; Bailey, G.S. !$#journal Biochemistry (1978) 17:2504-2510 !$#title Primary structure of histone H2B from trout (Salmo trutta) !1testes. !$#cross-references MUID:78235907; PMID:678528 !$#accession A02609 !'##molecule_type protein !'##residues 1-123 ##label KOO CLASSIFICATION #superfamily histone H2B KEYWORDS chromosomal protein; DNA binding; nucleosome core SUMMARY #length 123 #molecular-weight 13464 #checksum 7587 SEQUENCE /// ENTRY HSTR2B #type complete TITLE histone H2B - rainbow trout ORGANISM #formal_name Oncorhynchus mykiss #common_name rainbow trout DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 22-Jun-1999 ACCESSIONS A92961; A93779; A02609; B24552 REFERENCE A92961 !$#authors Winkfein, R.J.; Connor, W.; Mezquita, J.; Dixon, G.H. !$#journal J. Mol. Evol. (1985) 22:1-19 !$#title Histone H4 and H2B genes in rainbow trout (Salmo !1gairdnerii). !$#cross-references MUID:86037261; PMID:2997457 !$#accession A92961 !'##molecule_type DNA !'##residues 1-123 ##label WIN !'##cross-references GB:X02916; NID:g64320; PIDN:CAA26673.1; PID:g64322 !'##note the authors translated the codon GAG for residue 69 as Asp !'##note initiator Met not shown REFERENCE A93779 !$#authors Candido, E.P.M.; Dixon, G.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1972) 69:2015-2019 !$#title Amino-terminal sequences and sites of in vito acetylation of !1trout-testis histones III and IIb-2. !$#cross-references MUID:72259090; PMID:4506069 !$#contents acetylation !$#accession A93779 !'##molecule_type protein !'##residues 1-22 ##label CAN CLASSIFICATION #superfamily histone H2B KEYWORDS acetyllysine; chromosomal protein; DNA binding; nucleosome !1core FEATURE !$5,18 #binding_site acetyl (Lys) (covalent) (partial) !8#status experimental\ !$10,13 #binding_site acetyl (Lys) (covalent) #status !8experimental SUMMARY #length 123 #molecular-weight 13464 #checksum 7580 SEQUENCE /// ENTRY HSUR2M #type complete TITLE histone H2B.1, embryonic - sea urchin (Psammechinus miliaris) ORGANISM #formal_name Psammechinus miliaris #common_name sand urchin DATE 23-Oct-1981 #sequence_revision 23-Oct-1981 #text_change 16-Feb-1997 ACCESSIONS B93719; B90776; A02615 REFERENCE A93719 !$#authors Busslinger, M.; Portmann, R.; Irminger, J.C.; Birnstiel, !1M.L. !$#journal Nucleic Acids Res. (1980) 8:957-977 !$#title Ubiquitous and gene-specific regulatory 5' sequences in a !1sea urchin histone DNA clone coding for histone protein !1variants. !$#cross-references MUID:81076674; PMID:7443547 !$#accession B93719 !'##molecule_type DNA !'##residues 1-20 ##label BUS !'##experimental_source clone h22 REFERENCE A90776 !$#authors Schaffner, W.; Kunz, G.; Daetwyler, H.; Telford, J.; Smith, !1H.O.; Birnstiel, M.L. !$#journal Cell (1978) 14:655-671 !$#title Genes and spacers of cloned sea urchin histone DNA analyzed !1by sequencing. !$#cross-references MUID:79001915; PMID:688387 !$#accession B90776 !'##molecule_type DNA !'##residues 21-122 ##label SCH !'##experimental_source clone h22 CLASSIFICATION #superfamily histone H2B KEYWORDS chromosomal protein; DNA binding; nucleosome core SUMMARY #length 122 #molecular-weight 13430 #checksum 7328 SEQUENCE /// ENTRY HSUR6M #type complete TITLE histone H2B.2, embryonic - sea urchin (Psammechinus miliaris) ORGANISM #formal_name Psammechinus miliaris #common_name sand urchin DATE 23-Oct-1981 #sequence_revision 23-Oct-1981 #text_change 24-Sep-1999 ACCESSIONS A02616 REFERENCE A93719 !$#authors Busslinger, M.; Portmann, R.; Irminger, J.C.; Birnstiel, !1M.L. !$#journal Nucleic Acids Res. (1980) 8:957-977 !$#title Ubiquitous and gene-specific regulatory 5' sequences in a !1sea urchin histone DNA clone coding for histone protein !1variants. !$#cross-references MUID:81076674; PMID:7443547 !$#accession A02616 !'##molecule_type DNA !'##residues 1-122 ##label BUS !'##cross-references GB:X01344; NID:g10032; PIDN:CAA25631.1; PID:g10033 !'##experimental_source clone h19 CLASSIFICATION #superfamily histone H2B KEYWORDS chromosomal protein; DNA binding; nucleosome core SUMMARY #length 122 #molecular-weight 13450 #checksum 6131 SEQUENCE /// ENTRY HSUR2S #type complete TITLE histone H2B, embryonic - sea urchin (Strongylocentrotus purpuratus) (tentative sequence) ORGANISM #formal_name Strongylocentrotus purpuratus #common_name purple urchin DATE 30-Jun-1979 #sequence_revision 29-Jul-1981 #text_change 31-Mar-2000 ACCESSIONS A02617 REFERENCE A90777 !$#authors Sures, I.; Lowry, J.; Kedes, L.H. !$#journal Cell (1978) 15:1033-1044 !$#title The DNA sequence of sea urchin (S. purpuratus) H2A, H2B and !1H3 histone coding and spacer regions. !$#cross-references MUID:79084134; PMID:728984 !$#accession A02617 !'##molecule_type DNA !'##residues 1-123 ##label SUR !'##cross-references GB:V01356; NID:g10251; PIDN:CAA24646.1; PID:g10252 !'##note the codons were incompletely determined for the four residues !1in parentheses; however, the suggested residues are !1compatible with the partial evidence and with the three !1histone H2B sequences from Parechinus angulosus sperm CLASSIFICATION #superfamily histone H2B KEYWORDS chromosomal protein; DNA binding; nucleosome core SUMMARY #length 123 #molecular-weight 13496 #checksum 7740 SEQUENCE /// ENTRY S15721 #type complete TITLE histone H2B - Trypanosoma cruzi ORGANISM #formal_name Trypanosoma cruzi DATE 20-Feb-1995 #sequence_revision 11-Apr-1997 #text_change 22-Jun-1999 ACCESSIONS S54703; S15721 REFERENCE S54703 !$#authors Garcia-Salcedo, J.A.; Oliver, J.L.; Stock, R.P.; Gonzalez, !1A. !$#journal Mol. Microbiol. (1994) 13:1033-1043 !$#title Molecular characterization and transcription of the histone !1H2B gene from the protozoan parasite Trypanosoma cruzi. !$#cross-references MUID:95157247; PMID:7854118 !$#accession S54703 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-112 ##label GAR !'##cross-references EMBL:X60982; NID:g10612; PIDN:CAA43297.1; !1PID:g10613 !'##experimental_source strain Y GENETICS !$#note gene is tandemly repeated at 18 times in each of two !1clusters CLASSIFICATION #superfamily histone H2B KEYWORDS DNA binding; nucleus FEATURE !$19-23 #region nuclear location signal SUMMARY #length 112 #molecular-weight 12375 #checksum 5364 SEQUENCE /// ENTRY HSKW22 #type complete TITLE histone H2B [validated] - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 04-Dec-1986 #sequence_revision 09-Jun-2000 #text_change 09-Jun-2000 ACCESSIONS T30054; T30055; T28961; S04239; A02614; T20601; T27736; !1T27738; T33003; T18658; T22659; T23029; T29229; T20112 REFERENCE Z20728 !$#authors Miller, N.; Bradshaw, H. !$#submission submitted to the EMBL Data Library, July 1996 !$#description The sequence of C. elegans cosmid K06C4. !$#accession T30054 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-123 ##label MIL !'##cross-references EMBL:U64843; PIDN:AAB04854.1; GSPDB:GN00023; !1CESP:K06C4.4 !'##experimental_source strain Bristol N2; clone K06C4 !$#accession T30055 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-123 ##label MI2 !'##cross-references EMBL:U64843; PIDN:AAB04855.1; GSPDB:GN00023; !1CESP:K06C4.12 !'##experimental_source strain Bristol N2; clone K06C4 REFERENCE Z20548 !$#authors Davidson, S.; Wohldmann, P. !$#submission submitted to the EMBL Data Library, July 1996 !$#description The sequence of C. elegans cosmid F45F2. !$#accession T28961 !'##status preliminary !'##molecule_type DNA !'##residues 1-123 ##label DAV !'##cross-references EMBL:U64845; PIDN:AAC48023.1; GSPDB:GN00023; !1CESP:F45F2.12 REFERENCE S04238 !$#authors Roberts, S.B.; Emmons, S.W.; Childs, G. !$#journal J. Mol. Biol. (1989) 206:567-577 !$#title Nucleotide sequences of Caenorhabditis elegans core histone !1genes. Genes for different histone classes share common !1flanking sequence elements. !$#cross-references MUID:89293823; PMID:2544730 !$#accession S04239 !'##molecule_type DNA !'##residues 'M',3-123 ##label ROB !'##cross-references EMBL:X15633; NID:g6753; PIDN:CAA33642.1; PID:g6755 REFERENCE A02614 !$#authors Vanfleteren, J.R.; Van Bun, S.M.; Delcambe, L.L.; Van !1Beeumen, J.J. !$#journal Biochem. J. (1986) 235:769-773 !$#title Multiple forms of histone H2B from the nematode !1Caenorhabditis elegans. !$#cross-references MUID:86323051; PMID:3753445 !$#accession A02614 !'##molecule_type protein !'##residues 2-27,'KK',30-123 ##label VAN !'##note a minor variant lacks 2-Ala !'##note 8-Lys, 15-Lys, and 73-Ser were also found REFERENCE Z19298 !$#authors Wallis, J. !$#submission submitted to the EMBL Data Library, November 1996 !$#accession T20601 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 'M',3-123 ##label WIL !'##cross-references EMBL:Z81495; PIDN:CAB04061.1; GSPDB:GN00020; !1CESP:F08G2.1 !'##experimental_source clone F08G2 REFERENCE Z20413 !$#authors Steward, C. !$#submission submitted to the EMBL Data Library, December 1996 !$#accession T27736 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 'M',3-123 ##label WI2 !'##cross-references EMBL:Z83245; PIDN:CAB05830.1; GSPDB:GN00020; !1CESP:ZK131.9 !'##experimental_source clone ZK131 !$#accession T27738 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 'M',3-123 ##label WI3 !'##cross-references EMBL:Z83245; PIDN:CAB05832.1; GSPDB:GN00020; !1CESP:ZK131.5 !'##experimental_source clone ZK131 REFERENCE Z21262 !$#authors Woessner, J. !$#submission submitted to the EMBL Data Library, February 1998 !$#description The sequence of C. elegans cosmid F17E9. !$#accession T33003 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 'M',3-123 ##label WOE !'##cross-references EMBL:AF047656; PIDN:AAC05103.1; GSPDB:GN00022; !1CESP:F17E9.9 !'##experimental_source strain Bristol N2; clone F17E9 REFERENCE Z19002 !$#authors White, S. !$#submission submitted to the EMBL Data Library, May 1996 !$#accession T18658 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 'M',3-18,'VA',20-72,'S',74-123 ##label WI4 !'##cross-references EMBL:Z73102; PIDN:CAA97413.1; GSPDB:GN00022; !1CESP:B0035.8 !'##experimental_source clone B0035 REFERENCE Z19594 !$#authors White, S.; Mortimore, B. !$#submission submitted to the EMBL Data Library, November 1996 !$#accession T22659 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 'M',3-18,'VA',20-72,'S',74-123 ##label WI5 !'##cross-references EMBL:Z82271; PIDN:CAB05211.1; GSPDB:GN00022; !1CESP:F54E12.4 !'##experimental_source clone F54E12 REFERENCE Z19656 !$#authors McLay, K. !$#submission submitted to the EMBL Data Library, March 1997 !$#accession T23029 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 'M',3-18,'VA',20-72,'S',74-123 ##label WI6 !'##cross-references EMBL:Z92789; PIDN:CAB07220.1; GSPDB:GN00022; !1CESP:H02I12.6 !'##experimental_source clone H02I12 REFERENCE Z20591 !$#authors Murray, J.; Le, T.T. !$#submission submitted to the EMBL Data Library, May 1996 !$#description The sequence of C. elegans cosmid F55G1. !$#accession T29229 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 'M',3-18,'VA',20-72,'S',74-123 ##label MUR !'##cross-references EMBL:U58750; PIDN:AAB00648.1; GSPDB:GN00022; !1CESP:F55G1.3 !'##experimental_source strain Bristol N2; clone F55G1 REFERENCE Z19225 !$#authors McMurray, A. !$#submission submitted to the EMBL Data Library, April 1996 !$#accession T20112 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-18,'S',20-27,'K',29-72,'S',74-123 ##label WI7 !'##cross-references EMBL:Z70750; PIDN:CAA94740.1; GSPDB:GN00023; !1CESP:C50F4.5 !'##experimental_source clone C50F4 GENETICS H1 !$#gene his-11 GENETICS H2 !$#gene CESP:F08G2.1; CESP:ZK131.5; CESP:F17E9.9 !$#map_position 2 GENETICS H3 !$#gene CESP:F17E9.9; CESP:F54E12.4; CESP:B0035.8; CESP:F55G1.3; !1CESP:H02I12.6 !$#map_position 4 GENETICS H4 !$#gene CESP:K06C4.4; CESP:K06C4.12; CESP:F45F2.12 !$#map_position 5 GENETICS H5 !$#gene CESP:C50F4.5 !$#introns 45/3 CLASSIFICATION #superfamily histone H2B KEYWORDS chromosomal protein; DNA binding; nucleosome core SUMMARY #length 123 #molecular-weight 13572 #checksum 8140 SEQUENCE /// ENTRY HSFF22 #type complete TITLE histone H2B - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 28-Feb-1980 #sequence_revision 10-Oct-1997 #text_change 22-Jun-1999 ACCESSIONS S10095; A90434; B02630; A02610 REFERENCE S10094 !$#authors Matsuo, Y.; Yamazaki, T. !$#journal Nucleic Acids Res. (1989) 17:225-238 !$#title tRNA derived insertion element in histone gene repeating !1unit of Drosophila melanogaster. !$#cross-references MUID:89098383; PMID:2536150 !$#accession S10095 !'##status preliminary !'##molecule_type DNA !'##residues 1-123 ##label MAT !'##cross-references EMBL:X14215; NID:g8066; PIDN:CAA32432.1; PID:g8068 !'##note in the authors' translation 100-Leu is not shown and, !1consequently, residues 101-123 are displaced one codon to !1the left REFERENCE A90434 !$#authors Elgin, S.C.R.; Schilling, J.; Hood, L.E. !$#journal Biochemistry (1979) 18:5679-5685 !$#title Sequence of histone 2B of Drosophila melanogaster. !$#cross-references MUID:80088273; PMID:117830 !$#accession A90434 !'##molecule_type protein !'##residues 2-123 ##label ELG REFERENCE A02630 !$#authors Goldberg, M.L. !$#citation Ph.D. thesis, Stanford Univ., 1979 !$#accession B02630 !'##molecule_type DNA !'##residues 2-118 ##label GOL GENETICS !$#gene FlyBase:His2B !'##cross-references FlyBase:FBgn0001198 CLASSIFICATION #superfamily histone H2B KEYWORDS chromosomal protein; DNA binding; nucleosome core; nucleus SUMMARY #length 123 #molecular-weight 13696 #checksum 6230 SEQUENCE /// ENTRY HSKP22 #type complete TITLE histone H2B, gonadal - sandpaper limpet ORGANISM #formal_name Patella granatina #common_name sandpaper limpet DATE 30-Jun-1979 #sequence_revision 30-Jun-1979 #text_change 16-Feb-1997 ACCESSIONS A02611 REFERENCE A02611 !$#authors Van Helden, P.D.; Strickland, W.N.; Brandt, W.F.; von Holt, !1C. !$#journal Eur. J. Biochem. (1979) 93:71-78 !$#title The complete amino-acid sequence of histone H2B from the !1mollusc Patella granatina. !$#cross-references MUID:79169266; PMID:436833 !$#accession A02611 !'##molecule_type protein !'##residues 1-121 ##label VAN CLASSIFICATION #superfamily histone H2B KEYWORDS chromosomal protein; DNA binding; nucleosome core SUMMARY #length 121 #molecular-weight 13393 #checksum 6132 SEQUENCE /// ENTRY HSSF22 #type complete TITLE histone H2B, gonadal - starfish (Asterias rubens) ORGANISM #formal_name Asterias rubens #common_name common European starfish DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 16-Feb-1997 ACCESSIONS A02613 REFERENCE A02613 !$#authors Martinage, A.; Briand, G.; Van Dorsselaer, A.; Turner, C.H.; !1Sautiere, P. !$#journal Eur. J. Biochem. (1985) 147:351-359 !$#title Primary structure of histone H2B from gonads of the starfish !1Asterias rubens. Identification of an N-dimethylproline !1residue at the amino-terminal. !$#cross-references MUID:85127049; PMID:3882426 !$#accession A02613 !'##molecule_type protein !'##residues 1-121 ##label MAR CLASSIFICATION #superfamily histone H2B KEYWORDS blocked amino end; chromosomal protein; DNA binding; !1methylated amino end; nucleosome core FEATURE !$1 #modified_site dimethylated amino end (Pro) #status !8experimental SUMMARY #length 121 #molecular-weight 13461 #checksum 6096 SEQUENCE /// ENTRY HSSF2M #type complete TITLE histone H2B, sperm - starfish (Marthasterias glacialis) (tentative sequence) ORGANISM #formal_name Marthasterias glacialis #common_name spiny starfish DATE 30-Nov-1980 #sequence_revision 30-Sep-1988 #text_change 31-Mar-2000 ACCESSIONS A02612 REFERENCE A02612 !$#authors Strickland, M.S.; Strickland, W.N.; von Holt, C. !$#journal Eur. J. Biochem. (1980) 106:541-548 !$#title The histone H2B from the sperm cell of the starfish !1Marthasterias glacialis. !$#cross-references MUID:80245951; PMID:7398625 !$#accession A02612 !'##molecule_type protein !'##residues 1-120 ##label STR COMMENT The blocked amino end is not acetylated. CLASSIFICATION #superfamily histone H2B KEYWORDS blocked amino end; chromosomal protein; DNA binding; !1nucleosome core FEATURE !$1 #modified_site blocked amino end (Pro) #status !8experimental SUMMARY #length 120 #molecular-weight 13349 #checksum 5961 SEQUENCE /// ENTRY HSZPB2 #type complete TITLE histone H2B.1 - fission yeast (Schizosaccharomyces pombe) ORGANISM #formal_name Schizosaccharomyces pombe DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 10-Dec-1999 ACCESSIONS A27399; T41489 REFERENCE A91027 !$#authors Matsumoto, S.; Yanagida, M. !$#journal EMBO J. (1985) 4:3531-3538 !$#title Histone gene organization of fission yeast: a common !1upstream sequence. !$#cross-references MUID:86135992; PMID:4092687 !$#accession A27399 !'##molecule_type DNA !'##residues 1-126 ##label MATS !'##cross-references GB:X05220; NID:g4957; PIDN:CAA28847.1; PID:g4958 REFERENCE Z21998 !$#authors Seeger, K.; Harris, D.; Lyne, M.; Rajandream, M.A.; Barrell, !1B.G. !$#submission submitted to the EMBL Data Library, October 1998 !$#accession T41489 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-126 ##label SEE !'##cross-references EMBL:AL033127; PIDN:CAA21865.1; GSPDB:GN00068; !1SPDB:SPCC622.09 !'##experimental_source strain 972h-; cosmid c622 GENETICS !$#gene SPCC622.09 !$#map_position 3 CLASSIFICATION #superfamily histone H2B KEYWORDS chromosomal protein; DNA binding; nucleosome core FEATURE !$2-126 #product histone H2B.1 #status predicted #label MAT SUMMARY #length 126 #molecular-weight 13819 #checksum 9538 SEQUENCE /// ENTRY HSBY22 #type complete TITLE histone H2B.1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YD9934.09c; protein YDR224c ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1981 #sequence_revision 30-Jun-1992 #text_change 21-Jul-2000 ACCESSIONS A02621; S47932; S53985; S59431; S47473; S47947 REFERENCE A02621 !$#authors Wallis, J.W.; Hereford, L.; Grunstein, M. !$#journal Cell (1980) 22:799-805 !$#title Histone H2B genes of yeast encode two different proteins. !$#cross-references MUID:81112148; PMID:7006833 !$#accession A02621 !'##molecule_type DNA !'##residues 1-131 ##label WAL !'##cross-references GB:J01327; NID:g171632; PIDN:AAA88719.1; !1PID:g171633 REFERENCE S47932 !$#authors Davies, C.J.; Hutchison III, C.A. !$#submission submitted to the EMBL Data Library, September 1994 !$#description Tn3 transposon/deletion sequencing of a 9.4kb DNA fragment: !1Characterisation of Tn3 insertion-site specificity and !1analysis of transpositional 'hot' and 'cold' spots. !$#accession S47932 !'##molecule_type DNA !'##residues 1-131 ##label DAV2 !'##cross-references EMBL:L35344; EMBL:U13239; EMBL:Z36548 REFERENCE S53985 !$#authors Davies, C.J.; Hutchison III, C.A. !$#journal Nucleic Acids Res. (1995) 23:507-514 !$#title Insertion site specificity of the transposon Tn3. !$#cross-references MUID:95192063; PMID:7885847 !$#accession S53985 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-131 ##label DAV !'##cross-references EMBL:U13239; NID:g532747; PIDN:AAC33141.1; !1PID:g532748 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE S59423 !$#authors Murphy, L.; Harris, D. !$#submission submitted to the EMBL Data Library, March 1995 !$#accession S59431 !'##molecule_type DNA !'##residues 1-131 ##label MUR !'##cross-references EMBL:Z48612; NID:g728671; PIDN:CAA88504.1; !1PID:g728680; GSPDB:GN00004; MIPS:YDR224c !'##experimental_source strain AB972 GENETICS !$#gene SGD:HTB1; MIPS:YDR224c !'##cross-references SGD:S0002632; MIPS:YDR224c !$#map_position 4R CLASSIFICATION #superfamily histone H2B KEYWORDS chromosomal protein; DNA binding; nucleosome core SUMMARY #length 131 #molecular-weight 14252 #checksum 4371 SEQUENCE /// ENTRY HSBYB2 #type complete TITLE histone H2B - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein YBL002w; hypothetical protein YBL0104 ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1992 #sequence_revision 31-Dec-1993 #text_change 21-Jul-2000 ACCESSIONS S44558; S45731; B02621; S45269; S48891; A02621; S37320 REFERENCE S44556 !$#authors Wolfe, K.H.; Lohan, A.J.E. !$#journal Yeast (1994) 10(Suppl.A):S41-S46 !$#title Sequence around the centromere of Saccharomyces cerevisiae !1chromosome II: similarity of CEN2 to CEN4. !$#cross-references MUID:94378721; PMID:8091860 !$#accession S44558 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-131 ##label WOL !'##cross-references EMBL:Z26494; NID:g403311; PIDN:CAA81268.1; !1PID:g403314 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1September 1993 REFERENCE S45730 !$#authors Lohan, A.J.E.; Wolfe, K.H. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S45731 !'##molecule_type DNA !'##residues 1-131 ##label LOH !'##cross-references EMBL:Z35763; NID:g535975; PIDN:CAA84817.1; !1PID:g535976; GSPDB:GN00002; MIPS:YBL002w REFERENCE A02621 !$#authors Wallis, J.W.; Hereford, L.; Grunstein, M. !$#journal Cell (1980) 22:799-805 !$#title Histone H2B genes of yeast encode two different proteins. !$#cross-references MUID:81112148; PMID:7006833 !$#accession B02621 !'##molecule_type DNA !'##residues 2-131 ##label WAL !'##cross-references GB:J01328; NID:g3776; PIDN:CAA24615.1; PID:g3777 REFERENCE A91100 !$#authors Brandt, W.F.; Patterson, K.; von Holt, C. !$#journal Eur. J. Biochem. (1980) 110:67-76 !$#title The histones of yeast. The isolation and partial structure !1of the core histones. !$#cross-references MUID:81066651; PMID:7002547 !$#accession S45269 !'##molecule_type protein !'##residues 63-89 ##label BRA REFERENCE S48891 !$#authors Xu, H.; Johnson, L.; Grunstein, M. !$#journal Mol. Cell. Biol. (1990) 10:2687-2694 !$#title Coding and noncoding sequences at the 3' end of yeast !1histone H2B mRNA confer cell cycle regulation. !$#cross-references MUID:90258855; PMID:2188095 !$#accession S48891 !'##status translation not shown !'##molecule_type mRNA !'##residues 115-131 ##label XUH !'##cross-references EMBL:M37743 GENETICS !$#gene SGD:HTB2; H2B2; MIPS:YBL002w !'##cross-references SGD:S0000098; MIPS:YBL002w !$#map_position 2L CLASSIFICATION #superfamily histone H2B KEYWORDS chromosomal protein; DNA binding; nucleosome core SUMMARY #length 131 #molecular-weight 14237 #checksum 5197 SEQUENCE /// ENTRY HSWT2B #type complete TITLE histone H2B.2 - wheat ORGANISM #formal_name Triticum aestivum #common_name common wheat DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 24-Nov-1999 ACCESSIONS S00622 REFERENCE S00622 !$#authors Brandt, W.F.; de Andrade Rodrigues, J.; von Holt, C. !$#journal Eur. J. Biochem. (1988) 173:547-554 !$#title The amino acid sequence of wheat histone H2B(2). A core !1histone with a novel repetitive N-terminal extension. !$#cross-references MUID:88225069; PMID:3131141 !$#accession S00622 !'##molecule_type protein !'##residues 1-149 ##label BRA CLASSIFICATION #superfamily histone H2B KEYWORDS blocked amino end; chromosomal protein; DNA binding; !1nucleosome core FEATURE !$1 #modified_site blocked amino end (Pro) #status !8experimental SUMMARY #length 149 #molecular-weight 16095 #checksum 5817 SEQUENCE /// ENTRY HSURB2 #type complete TITLE histone H2B.2, sperm - sea urchin (Lytechinus pictus) ORGANISM #formal_name Lytechinus pictus #common_name painted urchin DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 22-Jun-1999 ACCESSIONS A24329; B25381 REFERENCE A93637 !$#authors Lai, Z.C.; Childs, G. !$#journal Nucleic Acids Res. (1986) 14:6845-6856 !$#title Isolation and characterization of the gene encoding the !1testis specific histone protein H2B-2 from the sea urchin !1Lytechinus pictus. !$#cross-references MUID:87016329; PMID:3763394 !$#accession A24329 !'##molecule_type DNA !'##residues 1-143 ##label LAI !'##cross-references GB:X04384; NID:g9618; PIDN:CAA27971.1; PID:g9619 !'##experimental_source testis REFERENCE A93078 !$#authors Lieber, T.; Weisser, K.; Childs, G. !$#journal Mol. Cell. Biol. (1986) 6:2602-2612 !$#title Analysis of histone gene expression in adult tissues of the !1sea urchins Strongylocentrotus purpuratus and Lytechinus !1pictus: tissue-specific expression of sperm histone genes. !$#cross-references MUID:87064560; PMID:3785204 !$#accession B25381 !'##molecule_type mRNA !'##residues 59-75,'A',77-137,'N',139-143 ##label LIE !'##cross-references GB:M13635; NID:g161315; PIDN:AAA30001.1; !1PID:g161316 !'##experimental_source testis !'##note this sequence most likely represents an alternative allele of !1the same gene CLASSIFICATION #superfamily histone H2B KEYWORDS chromosomal protein; DNA binding; nucleosome core FEATURE !$2-143 #product histone H2B.2, sperm #status predicted !8#label MAT SUMMARY #length 143 #molecular-weight 15936 #checksum 1021 SEQUENCE /// ENTRY HSUR6P #type complete TITLE histone H2B.2, sperm - sea urchin (Parechinus angulosus) ORGANISM #formal_name Parechinus angulosus #common_name angulate urchin DATE 30-Jun-1979 #sequence_revision 30-Jun-1979 #text_change 16-Feb-1997 ACCESSIONS A02619 REFERENCE A02619 !$#authors Strickland, W.N.; Strickland, M.; Brandt, W.F.; von Holt, C. !$#journal Eur. J. Biochem. (1977) 77:277-286 !$#title The complete amino-acid sequence of histone H2B-(2) from !1sperm of the sea urchin Parechinus angulosus. !$#cross-references MUID:77245960; PMID:891535 !$#accession A02619 !'##molecule_type protein !'##residues 1-143 ##label STR CLASSIFICATION #superfamily histone H2B KEYWORDS chromosomal protein; DNA binding; nucleosome core SUMMARY #length 143 #molecular-weight 15832 #checksum 1830 SEQUENCE /// ENTRY HSUR8P #type complete TITLE histone H2B.3, sperm - sea urchin (Parechinus angulosus) ORGANISM #formal_name Parechinus angulosus #common_name angulate urchin DATE 30-Jun-1979 #sequence_revision 30-Jun-1979 #text_change 16-Feb-1997 ACCESSIONS A02620 REFERENCE A02620 !$#authors Strickland, M.; Strickland, W.N.; Brandt, W.F.; von Holt, !1C.; Wittmann-Liebold, B.; Lehmann, A. !$#journal Eur. J. Biochem. (1978) 89:443-452 !$#title The complete amino-acid sequence of histone H2B-(3) from !1sperm of the sea urchin Parechinus angulosus. !$#cross-references MUID:79045272; PMID:710402 !$#accession A02620 !'##molecule_type protein !'##residues 1-148 ##label STR CLASSIFICATION #superfamily histone H2B KEYWORDS chromosomal protein; DNA binding; nucleosome core SUMMARY #length 148 #molecular-weight 16388 #checksum 4930 SEQUENCE /// ENTRY HSURB1 #type complete TITLE histone H2B.2, sperm - sea urchin (Strongylocentrotus purpuratus) ORGANISM #formal_name Strongylocentrotus purpuratus #common_name purple urchin DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 22-Jun-1999 ACCESSIONS A25381 REFERENCE A93078 !$#authors Lieber, T.; Weisser, K.; Childs, G. !$#journal Mol. Cell. Biol. (1986) 6:2602-2612 !$#title Analysis of histone gene expression in adult tissues of the !1sea urchins Strongylocentrotus purpuratus and Lytechinus !1pictus: tissue-specific expression of sperm histone genes. !$#cross-references MUID:87064560; PMID:3785204 !$#accession A25381 !'##molecule_type mRNA !'##residues 1-144 ##label LIE !'##cross-references GB:M13634; NID:g161514; PIDN:AAA30058.1; !1PID:g161515 !'##experimental_source testis CLASSIFICATION #superfamily histone H2B KEYWORDS chromosomal protein; DNA binding; nucleosome core FEATURE !$2-144 #product histone H2B.2, sperm #status predicted !8#label MAT SUMMARY #length 144 #molecular-weight 16004 #checksum 3532 SEQUENCE /// ENTRY HSUR2P #type complete TITLE histone H2B.1, sperm - sea urchin (Parechinus angulosus) ORGANISM #formal_name Parechinus angulosus #common_name angulate urchin DATE 30-Jun-1979 #sequence_revision 30-Jun-1979 #text_change 16-Feb-1997 ACCESSIONS A02618 REFERENCE A02618 !$#authors Strickland, M.; Strickland, W.N.; Brandt, W.F.; von Holt, C. !$#journal Eur. J. Biochem. (1977) 77:263-275 !$#title The complete amino-acid sequence of histone H2B-(1) from !1sperm of the sea urchin Parechinus angulosus. !$#cross-references MUID:77245959; PMID:891534 !$#accession A02618 !'##molecule_type protein !'##residues 1-144 ##label STR CLASSIFICATION #superfamily histone H2B KEYWORDS chromosomal protein; DNA binding; nucleosome core SUMMARY #length 144 #molecular-weight 16013 #checksum 4967 SEQUENCE /// ENTRY HSURBS #type complete TITLE histone H2B.1, sperm - sea urchin (Strongylocentrotus purpuratus) ORGANISM #formal_name Strongylocentrotus purpuratus #common_name purple urchin DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 22-Jun-1999 ACCESSIONS S07376 REFERENCE S07376 !$#authors Lai, Z.; Lieber, T.; Childs, G. !$#journal Nucleic Acids Res. (1986) 14:9218 !$#title The nucleotide sequence of the gene encoding the sperm !1specific histone subtype H2B-1 from the sea urchin !1Strongylocentrotus purpuratus. !$#cross-references MUID:87066789; PMID:3786151 !$#accession S07376 !'##molecule_type DNA !'##residues 1-140 ##label LAI !'##cross-references EMBL:X04681; NID:g10232; PIDN:CAA28385.1; !1PID:g10233 CLASSIFICATION #superfamily histone H2B KEYWORDS chromosomal protein; DNA binding; nucleosome core; sperm FEATURE !$2-140 #product histone H2B.1, sperm #status predicted !8#label MAT SUMMARY #length 140 #molecular-weight 15562 #checksum 5755 SEQUENCE /// ENTRY HSCH22 #type complete TITLE histone H2B.1 - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Jun-1979 #sequence_revision 03-Mar-2000 #text_change 21-Jul-2000 ACCESSIONS S14510; A26399; I50650; I50654; I50243; I50658; A02606; !1S04566; S19242 REFERENCE S14510 !$#authors Nakayama, T.; Setoguchi, Y. !$#submission submitted to the EMBL Data Library, January 1991 !$#description Nucleotide sequence of a member (H2B-IV) of the chicken H2B !1histone-encoding gene family. !$#accession S14510 !'##molecule_type DNA !'##residues 1-126 ##label NAK !'##cross-references EMBL:X57263; NID:g63457; PIDN:CAA40537.1; !1PID:g63458 REFERENCE A93651 !$#authors Grandy, D.K.; Dodgson, J.B. !$#journal Nucleic Acids Res. (1987) 15:1063-1080 !$#title Structure and organization of the chicken H2B histone gene !1family. !$#cross-references MUID:87146416; PMID:3822819 !$#accession A26399 !'##molecule_type DNA !'##residues 1-126 ##label GRA1 !'##cross-references GB:X05095; NID:g63451; PIDN:CAA28746.1; PID:g63452 !'##experimental_source clone pRR2e-3.5 REFERENCE I50647 !$#authors Sturm, R.A.; Dalton, S.; Wells, J.R. !$#journal Nucleic Acids Res. (1988) 16:8571-8586 !$#title Conservation of histone H2A/H2B intergene regions: a role !1for the H2B specific element in divergent transcription. !$#cross-references MUID:88335608; PMID:3267232 !$#accession I50650 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-126 ##label STU1 !'##cross-references EMBL:X07766; NID:g63432; PIDN:CAA30596.1; !1PID:g63434 !$#accession I50654 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-120 ##label STU2 !'##cross-references EMBL:X07763; NID:g63438; PIDN:CAA30590.1; !1PID:g63440 REFERENCE I50243 !$#authors Grandy, D.K.; Engel, J. !$#journal J. Biol. Chem. (1982) 257:8577-8580 !$#title Complete nucleotide sequence of a chicken H2B histone gene. !$#cross-references MUID:82239319; PMID:7096326 !$#accession I50243 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-126 ##label GRA2 !'##cross-references GB:J00871; NID:g63467; PIDN:CAA23706.1; PID:g63468 !$#accession I50658 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-126 ##label GRA3 !'##cross-references EMBL:V00415; NID:g63467; PIDN:CAA23706.1; !1PID:g63468 REFERENCE A90626 !$#authors Van Helden, P.; Strickland, W.N.; Brandt, W.F.; von Holt, C. !$#journal Biochim. Biophys. Acta (1978) 533:278-281 !$#title Histone H2B variants from the erythrocytes of an amphibian, !1a reptile and a bird. !$#cross-references MUID:78144893; PMID:638193 !$#accession A02606 !'##molecule_type protein !'##residues 2-30;63-90 ##label VAN !'##experimental_source erythrocyte CLASSIFICATION #superfamily histone H2B KEYWORDS chromosomal protein; DNA binding; nucleosome core; nucleus FEATURE !$2-126 #product histone H2B #status predicted #label MAT SUMMARY #length 126 #molecular-weight 13922 #checksum 1333 SEQUENCE /// ENTRY HSAK22 #type fragments TITLE histone H2B - Nile crocodile (tentative sequence) (fragments) ORGANISM #formal_name Crocodylus niloticus #common_name Nile crocodile DATE 30-Jun-1979 #sequence_revision 30-Jun-1979 #text_change 31-Mar-2000 ACCESSIONS A02607 REFERENCE A90626 !$#authors Van Helden, P.; Strickland, W.N.; Brandt, W.F.; von Holt, C. !$#journal Biochim. Biophys. Acta (1978) 533:278-281 !$#title Histone H2B variants from the erythrocytes of an amphibian, !1a reptile and a bird. !$#cross-references MUID:78144893; PMID:638193 !$#accession A02607 !'##molecule_type protein !'##residues 1-60 ##label VAN !'##experimental_source erythrocyte CLASSIFICATION #superfamily histone H2B KEYWORDS chromosomal protein; DNA binding; nucleosome core SUMMARY #length 60 #checksum 5966 SEQUENCE /// ENTRY HSHU33 #type complete TITLE histone H3.3 [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1987 #sequence_revision 03-Aug-1995 #text_change 08-Dec-2000 ACCESSIONS A27501; S52795; A94040; A91961; A02622 REFERENCE A27501 !$#authors Wells, D.; Hoffman, D.; Kedes, L. !$#journal Nucleic Acids Res. (1987) 15:2871-2889 !$#title Unusual structure, evolutionary conservation of non-coding !1sequences and numerous pseudogenes characterize the human !1H3.3 histone multigene family. !$#cross-references MUID:87174815; PMID:3031613 !$#accession A27501 !'##molecule_type DNA !'##residues 1-136 ##label WE2 !'##cross-references GB:X05854; GB:X05855; GB:X05856; GB:X05857; !1GB:Y00108 REFERENCE S52795 !$#authors Albig, W.; Bramlage, B.; Gruber, K.; Drabent, B.; Klobeck, !1H.; Kunz, J.; Doenecke, D. !$#submission submitted to the EMBL Data Library, March 1995 !$#description The human replacement histone gene variant H3.3B. !$#accession S52795 !'##molecule_type DNA !'##residues 1-136 ##label ALB !'##cross-references EMBL:Z48950; NID:g761715; PIDN:CAA88778.1; !1PID:g761716 REFERENCE A94040 !$#authors Wells, D.; Kedes, L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:2834-2838 !$#title Structure of a human histone cDNA: evidence that basally !1expressed histone genes have intervening sequences and !1encode polyadenylylated mRNAs. !$#cross-references MUID:85190590; PMID:2859593 !$#accession A94040 !'##molecule_type mRNA !'##residues 2-136 ##label WEL !'##cross-references GB:M11353; NID:g184092; PIDN:AAA52654.1; !1PID:g306849; GB:M11354; NID:g184090; PID:g306848 REFERENCE A91961 !$#authors Ohe, Y.; Iwai, K. !$#journal J. Biochem. (1981) 90:1205-1211 !$#title Human spleen histone H3. Isolation and amino acid sequence. !$#cross-references MUID:82075746; PMID:7309716 !$#accession A91961 !'##molecule_type protein !'##residues 2-136 ##label OHE !'##note 31-Ala, 87-Ser, 89-Val, and 90-Met were found in 50% of the !1chains COMMENT This histone is the predominant form in nondividing cells. GENETICS !$#gene GDB:H3F2 !'##cross-references GDB:120031; OMIM:142780 !$#map_position 1q21-1q21 !$#introns 43/2; 94/3 CLASSIFICATION #superfamily histone H3 KEYWORDS acetyllysine; chromosomal protein; DNA binding; methylated !1amino acid; nucleosome core FEATURE !$2-136 #product histone H3.3 #status experimental #label !8MAT\ !$10,37 #modified_site N6-methyllysine (Lys) (partial) !8#status experimental\ !$15,24 #binding_site acetyl (Lys) (covalent) (partial) !8#status experimental\ !$28 #modified_site N6-methyllysine (Lys) #status !8experimental SUMMARY #length 136 #molecular-weight 15328 #checksum 9585 SEQUENCE /// ENTRY HSCH3 #type complete TITLE histone H3 - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Jun-1987 #sequence_revision 13-Mar-1997 #text_change 22-Jun-1999 ACCESSIONS S18716; S18717; A93556; JS0690; A91223; S02627; A02625; !1S17359; S17360 REFERENCE S18716 !$#authors Setoguchi, Y.; Nakayama, T. !$#journal Nucleic Acids Res. (1991) 19:6327 !$#title Nucleotide sequences of new members (H3-IV and H3-V) of the !1chicken H3 histone-encoding gene family. !$#cross-references MUID:92066488; PMID:1956792 !$#accession S18716 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-136 ##label SET !'##cross-references EMBL:X62291; NID:g63481; PIDN:CAA44180.1; !1PID:g63482 !'##note histone H3-IV !'##note this sequence was submitted to the EMBL Data Library, August !11991 !$#accession S18717 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-136 ##label SEW !'##cross-references EMBL:X62292; NID:g63483; PIDN:CAA44181.1; !1PID:g63484 !'##note histone H3-V !'##note this sequence was submitted to the EMBL Data Library, August !11991 REFERENCE A93556 !$#authors Wang, S.W.; Robins, A.J.; d'Andrea, R.; Wells, J.R.E. !$#journal Nucleic Acids Res. (1985) 13:1369-1387 !$#title Inverted duplication of histone genes in chicken and !1disposition of regulatory sequences. !$#cross-references MUID:85215552; PMID:4000938 !$#accession A93556 !'##molecule_type mRNA !'##residues 2-136 ##label WAN !'##cross-references GB:X02218; NID:g63471; PIDN:CAA26138.1; PID:g63474 REFERENCE JS0690 !$#authors Nakayama, T. !$#journal Gene (1991) 102:289-290 !$#title Nucleotide sequences of two members of the chicken H3 !1histone-encoding gene family. !$#cross-references MUID:91340167; PMID:1874451 !$#accession JS0690 !'##molecule_type DNA !'##residues 1-136 ##label NAK !'##cross-references GB:M61154; NID:g211856; PIDN:AAA48796.1; !1PID:g211857; GB:M61155 !'##note histone H3-II and H3-III !'##note sequences of histone H3-II and histone H3-III are identical to !1that of histone H3-I; differences are found in the DNA !1sequences REFERENCE A91223 !$#authors Brandt, W.F.; von Holt, C. !$#journal Eur. J. Biochem. (1974) 46:419-429 !$#title The determination of the primary structure of histone F3 !1from chicken erythrocytes by automatic Edman degradation. 2. !1Sequence analysis of histone F3. !$#cross-references MUID:74308333; PMID:4859525 !$#accession A91223 !'##molecule_type protein !'##residues 2-136 ##label BRA REFERENCE S02627 !$#authors Lewis, P.N.; Guillemette, J.G.; Chan, S. !$#journal Eur. J. Biochem. (1988) 172:135-145 !$#title Histone accessibility determined by lysine-specific !1acetylation in chicken erythrocyte nuclei. !$#cross-references MUID:88151979; PMID:3126068 !$#accession S02627 !'##status preliminary !'##molecule_type protein !'##residues 2-26 ##label LEW !'##experimental_source strain leghorn GENETICS !$#gene H3-I; H3-II; H3-III; H3-IV; H3-V CLASSIFICATION #superfamily histone H3 KEYWORDS acetyllysine; chromosomal protein; DNA binding; methylated !1amino acid; nucleosome core; nucleus FEATURE !$10,28,37 #modified_site N6-methyllysine (Lys) #status !8predicted\ !$15,24 #binding_site acetyl (Lys) (covalent) #status !8predicted SUMMARY #length 136 #molecular-weight 15388 #checksum 200 SEQUENCE /// ENTRY HSRK3 #type complete TITLE histone H3 - striped catshark ORGANISM #formal_name Poroderma africanum #common_name striped catshark DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 16-Feb-1997 ACCESSIONS A02626 REFERENCE A02626 !$#authors Brandt, W.F.; Strickland, W.N.; von Holt, C. !$#journal FEBS Lett. (1974) 40:349-352 !$#title The primary structure of histone F3 from shark erythrocytes. !$#cross-references MUID:74309063; PMID:4855011 !$#accession A02626 !'##molecule_type protein !'##residues 1-135 ##label BRA !'##note Lys-9 (70%), Lys-27 (50%), and Lys-36 (20%) are methylated, !1mainly with the dimethyl derivative COMMENT The amount and position of acetylation was not precisely !1determined. Electrophoresis indicated that, when present, !1acetyl groups were located between residues 16 and 41. CLASSIFICATION #superfamily histone H3 KEYWORDS acetyllysine; chromosomal protein; DNA binding; methylated !1amino acid; nucleosome core FEATURE !$9,27,36 #modified_site N6-methyllysine or N6, !8N6-dimethyllysine (Lys) (partial) #status !8experimental SUMMARY #length 135 #molecular-weight 15257 #checksum 8291 SEQUENCE /// ENTRY HSTR3 #type complete TITLE histone H3, gonadal - rainbow trout ORGANISM #formal_name Oncorhynchus mykiss #common_name rainbow trout DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 22-Jun-1999 ACCESSIONS B92959; B93779; B23220 REFERENCE A92959 !$#authors Connor, W.; States, J.C.; Mezquita, J.; Dixon, G.H. !$#journal J. Mol. Evol. (1984) 20:236-250 !$#title Organization and nucleotide sequence of rainbow trout !1histone H2A and H3 genes. !$#cross-references MUID:85083109; PMID:6439879 !$#accession B92959 !'##molecule_type DNA !'##residues 1-135 ##label CON !'##cross-references GB:X01064; NID:g64324; PIDN:CAA25529.1; PID:g64326 !'##note initiator Met not shown REFERENCE A93779 !$#authors Candido, E.P.M.; Dixon, G.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1972) 69:2015-2019 !$#title Amino-terminal sequences and sites of in vito acetylation of !1trout-testis histones III and IIb-2. !$#cross-references MUID:72259090; PMID:4506069 !$#accession B93779 !'##molecule_type protein !'##residues 1-25 ##label CAN CLASSIFICATION #superfamily histone H3 KEYWORDS acetyllysine; chromosomal protein; DNA binding; nucleosome !1core; testis FEATURE !$9,18 #binding_site acetyl (Lys) (covalent) (partial) !8#status experimental\ !$14,23 #binding_site acetyl (Lys) (covalent) #status !8experimental SUMMARY #length 135 #molecular-weight 15257 #checksum 8291 SEQUENCE /// ENTRY HSFI3 #type complete TITLE histone H3 - smallmouth buffalo fish ORGANISM #formal_name Ictiobus bubalus #common_name smallmouth buffalo fish DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 16-Feb-1997 ACCESSIONS A02627 REFERENCE A02627 !$#authors Hooper, J.A.; Smith, E.L.; Sommer, K.R.; Chalkley, R. !$#journal J. Biol. Chem. (1973) 248:3275-3279 !$#title Histone III. IV. Amino acid sequence of histone III of the !1testes of the carp, Letiobus bubalus. !$#cross-references MUID:73166575; PMID:4700460 !$#accession A02627 !'##molecule_type protein !'##residues 1-135 ##label HOO !'##note Lys-9 is epsilon-N-monomethyllysine, epsilon-N-dimethyllysine, !1epsilon-N-trimethyllysine, or unmodified in 10, 13, 11, and !165% of the molecules, respectively !'##note Lys-27 is epsilon-N-monomethyllysine, epsilon-N-dimethyllysine, !1epsilon-N-trimethyllysine, or unmodified in 36, 40, 16, and !18% of the molecules, respectively CLASSIFICATION #superfamily histone H3 KEYWORDS chromosomal protein; DNA binding; methylated amino acid; !1nucleosome core FEATURE !$9,27 #modified_site N6-methyllysine, N6,N6-dimethyllysine !8or N6,N6,N6-trimethyllysine (Lys) (partial) #status !8experimental SUMMARY #length 135 #molecular-weight 15257 #checksum 8291 SEQUENCE /// ENTRY HSXL31 #type complete TITLE histone H3.1 - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 24-Sep-1999 ACCESSIONS A93596; A92918; A02634; A24279; E24510 REFERENCE A93596 !$#authors Old, R.W.; Sheikh, S.A.; Chambers, A.; Newton, C.A.; !1Mohammed, A.; Aldridge, T.C. !$#journal Nucleic Acids Res. (1985) 13:7341-7358 !$#title Individual Xenopus histone genes are replication-independent !1in oocytes and replication-dependent in Xenopus or mouse !1somatic cells. !$#cross-references MUID:86041919; PMID:4059058 !$#accession A93596 !'##molecule_type DNA !'##residues 1-135 ##label OLD !'##cross-references GB:X03104; NID:g64780; PIDN:CAA26890.1; PID:g64781 !'##experimental_source clone XLHW23 REFERENCE A92918 !$#authors Perry, M.; Thomsen, G.H.; Roeder, R.G. !$#journal J. Mol. Biol. (1985) 185:479-499 !$#title Genomic organization and nucleotide sequence of two distinct !1histone gene clusters from Xenopus laevis. Identification of !1novel conserved upstream sequence elements. !$#cross-references MUID:86037224; PMID:3863963 !$#accession A92918 !'##molecule_type DNA !'##residues 1-135 ##label PER !'##cross-references GB:X03017; NID:g64766; PIDN:CAA26813.1; PID:g64772 !'##experimental_source clones X1h1 and X1h3 COMMENT The initiator Met is not shown. CLASSIFICATION #superfamily histone H3 KEYWORDS chromosomal protein; DNA binding; nucleosome core SUMMARY #length 135 #molecular-weight 15257 #checksum 8291 SEQUENCE /// ENTRY HSUR3M #type complete TITLE histone H3, embryonic - sea urchin (Psammechinus miliaris) ORGANISM #formal_name Psammechinus miliaris #common_name sand urchin DATE 30-Jun-1979 #sequence_revision 23-Oct-1981 #text_change 24-Sep-1999 ACCESSIONS C90776; C93719; A02628 REFERENCE A90776 !$#authors Schaffner, W.; Kunz, G.; Daetwyler, H.; Telford, J.; Smith, !1H.O.; Birnstiel, M.L. !$#journal Cell (1978) 14:655-671 !$#title Genes and spacers of cloned sea urchin histone DNA analyzed !1by sequencing. !$#cross-references MUID:79001915; PMID:688387 !$#accession C90776 !'##molecule_type DNA !'##residues 1-135 ##label SCH !'##cross-references GB:J01181; GB:M10555; GB:V01140; NID:g161394; !1PIDN:AAB59206.1; PID:g161401 !'##experimental_source clone h22 REFERENCE A93719 !$#authors Busslinger, M.; Portmann, R.; Irminger, J.C.; Birnstiel, !1M.L. !$#journal Nucleic Acids Res. (1980) 8:957-977 !$#title Ubiquitous and gene-specific regulatory 5' sequences in a !1sea urchin histone DNA clone coding for histone protein !1variants. !$#cross-references MUID:81076674; PMID:7443547 !$#accession C93719 !'##molecule_type DNA !'##residues 1-135 ##label BUS !'##cross-references GB:X01345; NID:g10034; PIDN:CAA25632.1; PID:g10035 !'##experimental_source clone h19 CLASSIFICATION #superfamily histone H3 KEYWORDS chromosomal protein; DNA binding; embryo; nucleosome core SUMMARY #length 135 #molecular-weight 15271 #checksum 8315 SEQUENCE /// ENTRY HSUR3P #type complete TITLE histone H3, embryonic - sea urchin (Strongylocentrotus purpuratus) ORGANISM #formal_name Strongylocentrotus purpuratus #common_name purple urchin DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 22-Jun-1999 ACCESSIONS A02629 REFERENCE A93627 !$#authors Kaumeyer, J.F.; Weinberg, E.S. !$#journal Nucleic Acids Res. (1986) 14:4557-4576 !$#title Sequence, organization and expression of late embryonic H3 !1and H4 histone genes from the sea urchin, Strongylocentrotus !1purpuratus. !$#cross-references MUID:86232591; PMID:3714486 !$#accession A02629 !'##molecule_type DNA !'##residues 1-135 ##label KAU !'##cross-references GB:X03952; NID:g10256; PIDN:CAA27582.1; PID:g10258 !'##note the authors translated the codon AGC for residue 96 as Arg and !1CGT for residue 102 as Gly COMMENT This histone is expressed during late embryonic development. CLASSIFICATION #superfamily histone H3 KEYWORDS chromosomal protein; DNA binding; embryo; nucleosome core SUMMARY #length 135 #molecular-weight 15370 #checksum 8810 SEQUENCE /// ENTRY HSBO3 #type complete TITLE histone H3 - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 08-Oct-1981 #sequence_revision 08-Oct-1981 #text_change 07-May-1999 ACCESSIONS A02624; PL0130; A49978; S68319 REFERENCE A92132 !$#authors DeLange, R.J.; Hooper, J.A.; Smith, E.L. !$#journal J. Biol. Chem. (1973) 248:3261-3274 !$#title Histone III. III. Sequence studies on the cyanogen bromide !1peptides; complete amino acid sequence of calf thymus !1histone III. !$#cross-references MUID:73166574; PMID:4735580 !$#accession A02624 !'##molecule_type protein !'##residues 1-135 ##label DEL !'##note Cys-96 and Cys-110 can form an intrachain disulfide bond or !1interchain disulfide bonds resulting in the formation of !1dimers and higher polymers !'##note Lys-23 is acetylated in 43% of the molecules and Lys-14, in an !1unknown percent REFERENCE PL0130 !$#authors Pardridge, W.M.; Nowlin, D.M.; Calaycay, J.; Shively, J.E. !$#journal J. Neurochem. (1989) 53:1014-1018 !$#title Predominant low-molecular-weight proteins in isolated brain !1capillaries are histones. !$#cross-references MUID:89361419; PMID:2769252 !$#accession PL0130 !'##molecule_type protein !'##residues 1-16 ##label PAR !'##experimental_source brain REFERENCE A49978 !$#authors Wakim, B.T.; Aswad, G.D. !$#journal J. Biol. Chem. (1994) 269:2722-2727 !$#title Ca(2+)-calmodulin-dependent phosphorylation of arginine in !1histone 3 by a nuclear kinase from mouse leukemia cells. !$#cross-references MUID:94132040; PMID:8300603 !$#accession A49978 !'##molecule_type protein !'##residues 1-24;121-135 ##label WAK REFERENCE A92130 !$#authors DeLange, R.J.; Smith, E.L. !$#journal J. Biol. Chem. (1973) 248:3248-3254 !$#title Histone III. I. Isolation and sequences of the tryptic !1peptides from the maleylated calf thymus protein. !$#cross-references MUID:73166572; PMID:4735579 !$#contents annotation; tryptic peptides REFERENCE A92131 !$#authors Hooper, J.A.; Smith, E.L. !$#journal J. Biol. Chem. (1973) 248:3255-3260 !$#title Histone III. II. Isolation and sequences of chymotryptic !1peptides from calf thymus histone III. !$#cross-references MUID:73166573; PMID:4700459 !$#contents annotation; chymotryptic peptides REFERENCE A92102 !$#authors Marzluff Jr., W.F.; Sanders, L.A.; Miller, D.M.; McCarty, !1K.S. !$#journal J. Biol. Chem. (1972) 247:2026-2033 !$#title Two chemically and metabolically distinct forms of calf !1thymus histone F3. !$#cross-references MUID:72154496; PMID:5016641 !$#contents annotation; thymus, variant !$#note 20% of the histone H3 fraction consists of a minor form that !1differs from that shown at least in having only one Cys !1(Cys-110); the minor form is also acetylated more rapidly REFERENCE A92174 !$#authors Patthy, L.; Smith, E.L. !$#journal J. Biol. Chem. (1975) 250:1919-1920 !$#title Histone III. IV. Two forms of calf thymus histone III. !$#cross-references MUID:75095680; PMID:1167550 !$#contents annotation; variant !$#note analyses of two chymotryptic peptides, both corresponding to !1positions 91-99, indicated that both Cys and Ser are present !1at position 96 in a ratio of 2:1 REFERENCE S68319 !$#authors Couppez, M.; Belaiche, D. !$#journal Arch. Biochem. Biophys. (1996) 325:29-38 !$#title Successive elution by ion-exchange chromatography of H3-H4 !1histone complexes differing in their degree of acetylation. !$#cross-references MUID:96140594; PMID:8554340 !$#accession S68319 !'##molecule_type protein !'##residues 1-29 ##label COU CLASSIFICATION #superfamily histone H3 KEYWORDS acetyllysine; chromosomal protein; DNA binding; methylated !1amino acid; nucleosome core; phosphoprotein FEATURE !$2,128,129,131 #binding_site phosphate (Arg) (covalent) #status !8experimental\ !$9,27 #modified_site N6-methyllysine, N6,N6-dimethyllysine !8or N6,N6,N6-trimethyllysine (Lys) (partial) #status !8experimental\ !$14,23 #binding_site acetyl (Lys) (covalent) (partial) !8#status experimental\ !$96,110 #disulfide_bonds interchain (in polymeric form) !8#status experimental\ !$96-110 #disulfide_bonds (in monomeric form) #status !8experimental SUMMARY #length 135 #molecular-weight 15273 #checksum 7667 SEQUENCE /// ENTRY HSHU3 #type complete TITLE histone H3.1 - human ALTERNATE_NAMES histone H3; histone H3a ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1987 #sequence_revision 14-Jul-1995 #text_change 22-Jun-1999 ACCESSIONS I37446; A02623; S49502; A40335; C33178; A33290; S28528 REFERENCE I37445 !$#authors Kardalinou, E.; Eick, S.; Albig, W.; Doenecke, D. !$#journal J. Cell. Biochem. (1993) 52:375-383 !$#title Association of a human H1 histone gene with an H2A !1pseudogene and genes encoding H2B.1 and H3.1 histones. !$#cross-references MUID:94043505; PMID:8227173 !$#accession I37446 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-136 ##label RES !'##cross-references EMBL:X57128; NID:g31981; PIDN:CAA40407.1; !1PID:g31982 REFERENCE A02623 !$#authors Marashi, F.; Helms, S.; Shiels, A.; Silverstein, S.; !1Greenspan, D.S.; Stein, G.; Stein, J. !$#journal Biochem. Cell Biol. (1986) 64:277-289 !$#title Enhancer-facilitated expression of prokaryotic and !1eukaryotic genes using human histone gene 5' regulatory !1sequences. !$#cross-references MUID:86242753; PMID:3013246 !$#accession A02623 !'##molecule_type DNA !'##residues 2-134,'A' ##label MAR !'##cross-references GB:M26150; NID:g184061; PIDN:AAA52651.1; !1PID:g386772 REFERENCE S49502 !$#authors Runge, D.; Eick, S.; Doenecke, D. !$#submission submitted to the EMBL Data Library, October 1994 !$#description Expression of human histone h1.1 and the nearby core !1histones. !$#accession S49502 !'##status preliminary !'##molecule_type DNA !'##residues 1-136 ##label RUN !'##cross-references EMBL:Z46261; NID:g559901; PIDN:CAA86403.1; !1PID:g559902 REFERENCE A40335 !$#authors Albig, W.; Kardalinou, E.; Drabent, B.; Zimmer, A.; !1Doenecke, D. !$#journal Genomics (1991) 10:940-948 !$#title Isolation and characterization of two human H1 histone genes !1within clusters of core histone genes. !$#cross-references MUID:92009931; PMID:1916825 !$#accession A40335 !'##molecule_type DNA !'##residues 2-136 ##label ALB !'##cross-references GB:M60746; NID:g184069; PIDN:AAA63185.1; !1PID:g184070 !'##note the authors did not translate the codon for residue 1 REFERENCE A33178 !$#authors Ward, L.D.; Hong, J.; Whitehead, R.H.; Simpson, R.J. !$#journal Electrophoresis (1990) 11:883-891 !$#title Development of a database of amino acid sequences for human !1colon carcinoma proteins separated by two-dimensional !1polyacrylamide gel electrophoresis. !$#cross-references MUID:91176935; PMID:2079031 !$#accession C33178 !'##molecule_type protein !'##residues 2-25 ##label WAR REFERENCE A33290 !$#authors Baxter, G.D.; Smith, P.J.; Lavin, M.F. !$#journal Biochem. Biophys. Res. Commun. (1989) 162:30-37 !$#title Molecular changes associated with induction of cell death in !1a human T-cell leukaemia line: putative nucleases identified !1as histones. !$#cross-references MUID:89322258; PMID:2546549 !$#accession A33290 !'##molecule_type protein !'##residues 'X',3-11 ##label BAX GENETICS !$#gene H3.1 CLASSIFICATION #superfamily histone H3 KEYWORDS acetyllysine; chromosomal protein; DNA binding; methylated !1amino acid; nucleosome core FEATURE !$2-136 #product histone H3.1 #status predicted #label MAT\ !$10,37 #modified_site N6-methyllysine (Lys) (partial) !8#status experimental\ !$15,24 #binding_site acetyl (Lys) (covalent) (partial) !8#status experimental\ !$28 #modified_site N6-methyllysine (Lys) #status !8experimental SUMMARY #length 136 #molecular-weight 15404 #checksum 9560 SEQUENCE /// ENTRY HSEAH3 #type complete TITLE histone H3 - Altenstein's bread tree ORGANISM #formal_name Encephalartos altensteinii #common_name Altenstein's bread tree DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Feb-1997 ACCESSIONS A23604 REFERENCE A23604 !$#authors Brandt, W.F.; von Holt, C. !$#journal FEBS Lett. (1986) 194:278-281 !$#title The primary structure of histone H3 from cycad pollen. !$#accession A23604 !'##molecule_type protein !'##residues 1-135 ##label BRA !'##experimental_source pollen !'##note 53-Lys, 96-Ser, 107-Ser, and 124-Val were also found CLASSIFICATION #superfamily histone H3 KEYWORDS chromosomal protein; DNA binding; methylated amino acid; !1nucleosome core FEATURE !$4 #modified_site N6-methyllysine or N6, !8N6-dimethyllysine (Lys) (partial) #status !8experimental\ !$9,27 #modified_site N6-methyllysine or N6, !8N6-dimethyllysine (Lys) #status experimental SUMMARY #length 135 #molecular-weight 15165 #checksum 6414 SEQUENCE /// ENTRY HSKW3 #type complete TITLE histone H3 - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 30-Sep-1988 #sequence_revision 19-Oct-1995 #text_change 20-Oct-2000 ACCESSIONS S04241; A25842; T18656; T20597; T21228; T22657; T24787; !1T27737; T27739; T27740; T28963; T29231; T30052; T30057; !1T33001 REFERENCE S04238 !$#authors Roberts, S.B.; Emmons, S.W.; Childs, G. !$#journal J. Mol. Biol. (1989) 206:567-577 !$#title Nucleotide sequences of Caenorhabditis elegans core histone !1genes. Genes for different histone classes share common !1flanking sequence elements. !$#cross-references MUID:89293823; PMID:2544730 !$#accession S04241 !'##molecule_type DNA !'##residues 1-136 ##label ROB !'##cross-references EMBL:X15634; NID:g6750; PIDN:CAA33644.1; PID:g6752 REFERENCE A25842 !$#authors Vanfleteren, J.R.; Van Bun, S.M.; Van Beeumen, J.J. !$#journal FEBS Lett. (1987) 211:59-63 !$#title The primary structure of histone H3 from the nematode !1Caenorhabditis elegans. !$#cross-references MUID:87105951; PMID:3803587 !$#accession A25842 !'##molecule_type protein !'##residues 2-64,'K',66-96,'C',98-136 ##label VAN !'##experimental_source strain DR27 daf-17[m27] !'##note 97-Ala and 101-Ile were also found; artifactual S-carboxymethyl !1cysteine was found at position 97 after treatment with !1iodoacetic acid REFERENCE Z19002 !$#authors White, S. !$#submission submitted to the EMBL Data Library, May 1996 !$#accession T18656 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-136 ##label WIL !'##cross-references EMBL:Z73102; PIDN:CAA97411.1; GSPDB:GN00022; !1CESP:B0035.10 !'##experimental_source clone B0035 REFERENCE Z19298 !$#authors Wallis, J. !$#submission submitted to the EMBL Data Library, November 1996 !$#accession T20597 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-136 ##label WI2 !'##cross-references EMBL:Z81495; PIDN:CAB04057.1; GSPDB:GN00020; !1CESP:F08G2.3 !'##experimental_source clone F08G2 REFERENCE Z19394 !$#authors Cottage, A. !$#submission submitted to the EMBL Data Library, January 1996 !$#accession T21228 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-136 ##label WI3 !'##cross-references EMBL:Z68336; PIDN:CAA92733.1; GSPDB:GN00022; !1CESP:F22B3.2 !'##experimental_source clone F22B3 REFERENCE Z19594 !$#authors White, S.; Mortimore, B. !$#submission submitted to the EMBL Data Library, November 1996 !$#accession T22657 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-136 ##label WI4 !'##cross-references EMBL:Z82271; PIDN:CAB05209.1; GSPDB:GN00022; !1CESP:F54E12.1 !'##experimental_source clone F54E12 REFERENCE Z19936 !$#authors McMurray, A. !$#submission submitted to the EMBL Data Library, March 1997 !$#accession T24787 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-136 ##label WI5 !'##cross-references EMBL:Z93388; PIDN:CAB07653.1; GSPDB:GN00023; !1CESP:T10C6.13 !'##experimental_source clone T10C6 REFERENCE Z20413 !$#authors Steward, C. !$#submission submitted to the EMBL Data Library, December 1996 !$#accession T27737 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-136 ##label WI6 !'##cross-references EMBL:Z83245; PIDN:CAB05831.1; GSPDB:GN00020; !1CESP:ZK131.7 !'##experimental_source clone ZK131 !$#accession T27739 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-136 ##label WI7 !'##cross-references EMBL:Z83245; PIDN:CAB05833.1; GSPDB:GN00020; !1CESP:ZK131.3 !'##experimental_source clone ZK131 !$#accession T27740 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-136 ##label WI8 !'##cross-references EMBL:Z83245; PIDN:CAB05834.1; GSPDB:GN00020; !1CESP:ZK131.2 !'##experimental_source clone ZK131 REFERENCE Z20548 !$#authors Davidson, S.; Wohldmann, P. !$#submission submitted to the EMBL Data Library, July 1996 !$#description The sequence of C. elegans cosmid F45F2. !$#accession T28963 !'##status preliminary !'##molecule_type DNA !'##residues 1-136 ##label DAV !'##cross-references EMBL:U64845; PIDN:AAC48033.1; GSPDB:GN00023; !1CESP:F45F2.13 REFERENCE Z20591 !$#authors Murray, J.; Le, T.T. !$#submission submitted to the EMBL Data Library, May 1996 !$#description The sequence of C. elegans cosmid F55G1. !$#accession T29231 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-136 ##label MUR !'##cross-references EMBL:U58750; PIDN:AAB00650.1; GSPDB:GN00022; !1CESP:F55G1.2 !'##experimental_source strain Bristol N2; clone F55G1 REFERENCE Z20728 !$#authors Miller, N.; Bradshaw, H. !$#submission submitted to the EMBL Data Library, July 1996 !$#description The sequence of C. elegans cosmid K06C4. !$#accession T30052 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-136 ##label MIL !'##cross-references EMBL:U64843; PIDN:AAB04852.1; GSPDB:GN00023; !1CESP:K06C4.5 !'##experimental_source strain Bristol N2; clone K06C4 !$#accession T30057 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-136 ##label MI2 !'##cross-references EMBL:U64843; PIDN:AAB04857.1; GSPDB:GN00023; !1CESP:K06C4.13 !'##experimental_source strain Bristol N2; clone K06C4 REFERENCE Z21262 !$#authors Woessner, J. !$#submission submitted to the EMBL Data Library, February 1998 !$#description The sequence of C. elegans cosmid F17E9. !$#accession T33001 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-136 ##label WOE !'##cross-references EMBL:AF047656; PIDN:AAC05102.1; GSPDB:GN00022; !1CESP:F17E9.10 !'##experimental_source strain Bristol N2; clone F17E9 GENETICS H01 !$#gene his-9 GENETICS H02 !$#gene CESP:B0035.10 !$#map_position 4 GENETICS H03 !$#gene CESP:F08G2.3 !$#map_position 2 GENETICS H04 !$#gene CESP:F22B3.2 !$#map_position 4 GENETICS H05 !$#gene CESP:F54E12.1 !$#map_position 4 GENETICS H06 !$#gene CESP:T10C6.13 !$#map_position 5 GENETICS H07 !$#gene CESP:ZK131.7 !$#map_position 2 GENETICS H08 !$#gene CESP:ZK131.3 !$#map_position 2 GENETICS H09 !$#gene CESP:ZK131.2 !$#map_position 2 GENETICS H10 !$#gene CESP:F17E9.10 !$#map_position 4 !$#note ; Gene: CESP:F55G1.2; Map position: 4 !$#note ; Gene: CESP:K06C4.5; Map position: 5 !$#note ; Gene: CESP:K06C4.13 !$#note histones exist in large multigene families; it is possible !1that some of the genes shown here represent the same gene CLASSIFICATION #superfamily histone H3 KEYWORDS acetyllysine; chromosomal protein; DNA binding; methylated !1amino acid; nucleosome core FEATURE !$5,15,24 #binding_site acetyl (Lys) (covalent) (partial) !8#status experimental\ !$10 #modified_site N6-methyllysine or N6, !8N6-dimethyllysine (Lys) (partial) #status !8experimental\ !$28,37,80 #modified_site N6-methyllysine (Lys) (partial) !8#status experimental SUMMARY #length 136 #molecular-weight 15344 #checksum 9404 SEQUENCE /// ENTRY HSPM3 #type complete TITLE histone H3 - garden pea (tentative sequence) ORGANISM #formal_name Pisum sativum #common_name garden pea DATE 13-Jul-1981 #sequence_revision 13-Jul-1981 #text_change 31-Mar-2000 ACCESSIONS A02631 REFERENCE A02631 !$#authors Patthy, L.; Smith, E.L.; Johnson, J. !$#journal J. Biol. Chem. (1973) 248:6834-6840 !$#title Histone III. V. The amino acid sequence of pea embryo !1histone III. !$#cross-references MUID:74011270; PMID:4795661 !$#accession A02631 !'##molecule_type protein !'##residues 1-135 ##label PAT !'##experimental_source embryo !'##note Lys-9 and Lys-27 are mainly epsilon-N-monomethyllysine. In a !1small fraction of the chains the dimethyl derivative is !1present at either position !'##note 96-Ser was found in 40% of the molecules CLASSIFICATION #superfamily histone H3 KEYWORDS chromosomal protein; DNA binding; nucleosome core SUMMARY #length 135 #molecular-weight 15153 #checksum 6637 SEQUENCE /// ENTRY HSBH3 #type fragment TITLE histone H3 - barley (fragment) ORGANISM #formal_name Hordeum vulgare #common_name barley DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 16-Feb-1997 ACCESSIONS A02632 REFERENCE A02632 !$#authors Chojecki, J. !$#journal Carlsberg Res. Commun. (1986) 51:211-217 !$#title Identification and characterization of a cDNA clone for !1histone H3 in barley. !$#accession A02632 !'##molecule_type mRNA !'##residues 1-80 ##label CHO CLASSIFICATION #superfamily histone H3 KEYWORDS chromosomal protein; DNA binding; nucleosome core SUMMARY #length 80 #checksum 3200 SEQUENCE /// ENTRY HSXL32 #type complete TITLE histone H3.2 - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 16-Feb-1997 ACCESSIONS A02634 REFERENCE A91300 !$#authors Moorman, A.F.M.; De Boer, P.A.J.; De Laaf, R.T.M.; Van !1Dongen, W.M.A.M.; Destree, O.H.J. !$#journal FEBS Lett. (1981) 136:45-52 !$#title Primary structure of the histone H3 and H4 genes and their !1flanking sequences in a minor histone gene cluster of !1Xenopus laevis. !$#cross-references MUID:82095633; PMID:6274702 !$#accession A02634 !'##molecule_type DNA !'##residues 1-135 ##label MOR !'##experimental_source clone X1hi1 !'##note initiator Met not shown CLASSIFICATION #superfamily histone H3 KEYWORDS chromosomal protein; DNA binding; nucleosome core SUMMARY #length 135 #molecular-weight 15356 #checksum 7803 SEQUENCE /// ENTRY HSZP3 #type complete TITLE histone H3.1 [similarity] - fission yeast (Schizosaccharomyces pombe) ORGANISM #formal_name Schizosaccharomyces pombe DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 21-Jul-2000 ACCESSIONS E27399; T39288; T40749; T50115 REFERENCE A91027 !$#authors Matsumoto, S.; Yanagida, M. !$#journal EMBO J. (1985) 4:3531-3538 !$#title Histone gene organization of fission yeast: a common !1upstream sequence. !$#cross-references MUID:86135992; PMID:4092687 !$#accession E27399 !'##molecule_type DNA !'##residues 1-136 ##label MATS !'##cross-references GB:X05223; GB:M26378; NID:g4962; PIDN:CAA28852.1; !1PID:g4963 REFERENCE Z21841 !$#authors McDougall, R.C.; Rajandream, M.A.; Barrell, B.G.; !1Ramsperger, U.; Bothe, G.; Pohl, T. !$#submission submitted to the EMBL Data Library, July 1999 !$#accession T39288 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-136 ##label MCD !'##cross-references EMBL:AL096851; PIDN:CAB50974.1; GSPDB:GN00067; !1SPDB:SPBC1105.11c !'##experimental_source strain 972h-; cosmid c1105 !'##genetics MCD1 REFERENCE Z21948 !$#authors Lyne, M.; Rajandream, M.A.; Barrell, B.G.; Lauber, J.; !1Hilbert, H.; Duesterhoeft, A. !$#submission submitted to the EMBL Data Library, March 1998 !$#accession T40749 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-136 ##label LYN !'##cross-references EMBL:AL022072; PIDN:CAA17819.1; GSPDB:GN00067; !1SPDB:SPBC8D2.04 !'##experimental_source strain 972h-; cosmid c8D2 !'##genetics LYN2 REFERENCE Z25039 !$#authors Seeger, K.; Harris, D.; Wood, V.; Rajandream, M.A.; Barrell, !1B.G. !$#submission submitted to the EMBL Data Library, February 2000 !$#accession T50115 !'##molecule_type DNA !'##residues 1-136 ##label SEE !'##cross-references EMBL:AL157734; PIDN:CAB75772.1; GSPDB:GN00066; !1SPDB:SPAC1834.04 !'##experimental_source strain 972h-; cosmid c1834 !'##genetics SEE3 GENETICS MCD1 !$#gene SPBC1105.11c !$#map_position 2 GENETICS LYN2 !$#gene SPBC8D2.04 !$#map_position 2 GENETICS SEE3 !$#gene hht1; SPAC1834.04 !$#map_position 1 CLASSIFICATION #superfamily histone H3 KEYWORDS chromosomal protein; DNA binding; nucleosome core FEATURE !$2-136 #product histone H3.1 #status predicted #label MAT SUMMARY #length 136 #molecular-weight 15357 #checksum 219 SEQUENCE /// ENTRY HSBY3 #type complete TITLE histone H3 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein N2749; protein YBR010w; protein YBR0201; protein YNL031c ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Dec-1980 #sequence_revision 09-Sep-1994 #text_change 16-Jun-2000 ACCESSIONS S45265; S45267; S45863; A02635; S45270; A91431; S62953; !1S62943 REFERENCE A92906 !$#authors Smith, M.M.; Andresson, O.S. !$#journal J. Mol. Biol. (1983) 169:663-690 !$#title DNA sequences of yeast H3 and H4 histone genes from two !1non-allelic gene sets encode identical H3 and H4 proteins. !$#cross-references MUID:84036173; PMID:6355483 !$#accession S45265 !'##molecule_type DNA !'##residues 1-136 ##label SMI !'##cross-references EMBL:X00724; NID:g3754; PIDN:CAA25310.1; PID:g3755 !'##genetics HHT1 !$#accession S45267 !'##molecule_type DNA !'##residues 1-136 ##label SM2 !'##cross-references EMBL:X00725; NID:g3757; PIDN:CAA25312.1; PID:g3758 !'##genetics HHT2 REFERENCE S45862 !$#authors Entian, K.D.; Koetter, P.; Rose, M.; Li, Z.; Thermann, R.; !1Brendel, M.; Baur, A.; Boles, E.; Miosga, T.; !1Schaaff-Gerstenschlaeger, I.; Zimmermann, F.K. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S45863 !'##molecule_type DNA !'##residues 1-136 ##label ENT !'##cross-references EMBL:Z35879; GSPDB:GN00002; MIPS:YBR010w; !1NID:g536203; PIDN:CAA84948.1; PID:g536204 !'##genetics HHT1 REFERENCE A91113 !$#authors Brandt, W.F.; von Holt, C. !$#journal Eur. J. Biochem. (1982) 121:501-510 !$#title The primary structure of yeast histone H3. !$#cross-references MUID:82117063; PMID:7035169 !$#accession A02635 !'##molecule_type protein !'##residues 2-136 ##label BR1 REFERENCE A91100 !$#authors Brandt, W.F.; Patterson, K.; von Holt, C. !$#journal Eur. J. Biochem. (1980) 110:67-76 !$#title The histones of yeast. The isolation and partial structure !1of the core histones. !$#cross-references MUID:81066651; PMID:7002547 !$#accession S45270 !'##molecule_type protein !'##residues 2-43 ##label BR3 REFERENCE A91431 !$#authors Brandt, W.F.; von Holt, C. !$#journal FEBS Lett. (1976) 65:386-390 !$#title The occurrence of histone H3 and H4 in yeast. !$#cross-references MUID:76257804; PMID:782914 !$#accession A91431 !'##molecule_type protein !'##residues 2-16 ##label BR2 REFERENCE S62944 !$#authors Duesterhoeft, A.; Floeth, M.; Fritz, C.; Heuss-Neitzel, D.; !1Hilbert, H.; Moestl, D. !$#submission submitted to the Protein Sequence Database, April 1996 !$#accession S62953 !'##molecule_type DNA !'##residues 1-136 ##label DUE !'##cross-references EMBL:Z71307; GSPDB:GN00014; MIPS:YNL031c; !1NID:g1301869; PIDN:CAA95894.1; PID:g1301870 !'##experimental_source strain S288C !'##genetics HHT2 REFERENCE S62920 !$#authors Andre, B.; Iraqui Houssaini, I.; Urrestarazu, L.A.; Vissers, !1S. !$#submission submitted to the Protein Sequence Database, April 1996 !$#accession S62943 !'##molecule_type DNA !'##residues 1-63 ##label AND !'##cross-references EMBL:Z71307; GSPDB:GN00014; MIPS:YNL031c !'##experimental_source strain S288C !'##genetics HHT2 GENETICS HHT1 !$#gene SGD:HHT1; H3I; MIPS:YBR010w !'##cross-references MIPS:YBR010w; SGD:S0000214 !$#map_position 2R GENETICS HHT2 !$#gene SGD:HHT2; MIPS:YNL031c !'##cross-references MIPS:YNL031c; SGD:S0004976 !$#map_position 14L CLASSIFICATION #superfamily histone H3 KEYWORDS chromosomal protein; DNA binding; methylated amino acid; !1nucleosome core FEATURE !$2-136 #product histone H3 #status experimental #label MAT\ !$5 #modified_site N6-methyllysine or N6, !8N6-dimethyllysine (Lys) (partial) #status !8experimental SUMMARY #length 136 #molecular-weight 15356 #checksum 403 SEQUENCE /// ENTRY HSVK3L #type complete TITLE histone H3 - yeast (Kluyveromyces marxianus var. lactis) ORGANISM #formal_name Kluyveromyces marxianus var. lactis, Candida sphaerica DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 22-Jun-1999 ACCESSIONS S07892 REFERENCE S07892 !$#authors Stark, M.J.R.; Milner, J.S. !$#journal Yeast (1989) 5:35-50 !$#title Cloning and analysis of the Kluyveromyces lactis TRP1 gene: !1a chromosomal locus flanked by genes encoding inorganic !1pyrophosphatase and histone H3. !$#cross-references MUID:89189093; PMID:2538971 !$#accession S07892 !'##molecule_type DNA !'##residues 1-136 ##label STA !'##cross-references EMBL:X14230; NID:g2900; PIDN:CAA32444.1; PID:g2901 GENETICS !$#gene HHT1 CLASSIFICATION #superfamily histone H3 KEYWORDS chromosomal protein; DNA binding; nucleosome core SUMMARY #length 136 #molecular-weight 15356 #checksum 403 SEQUENCE /// ENTRY HSDK34 #type complete TITLE histone H3.4 - muscovy duck ALTERNATE_NAMES four-cysteine variant histone H3 ORGANISM #formal_name Cairina moschata #common_name muscovy duck DATE 30-Sep-1987 #sequence_revision 30-Jun-1989 #text_change 22-Jun-1999 ACCESSIONS A23981; A05256 REFERENCE A91540 !$#authors Tonjes, R.; Doenecke, D. !$#journal Gene (1985) 39:275-279 !$#title Structure of a duck H3 variant histone gene: a H3 subtype !1with four cysteine residues. !$#cross-references MUID:86137397; PMID:4092933 !$#accession A23981 !'##molecule_type DNA !'##residues 1-136 ##label TON !'##cross-references GB:M14396; NID:g212923; PIDN:AAA49151.1; !1PID:g212924 CLASSIFICATION #superfamily histone H3 KEYWORDS chromosomal protein; DNA binding; nucleosome core FEATURE !$2-136 #product histone H3.4 #status predicted #label MAT SUMMARY #length 136 #molecular-weight 15317 #checksum 8229 SEQUENCE /// ENTRY HSMS34 #type complete TITLE histone H3.4 - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 28-May-1999 ACCESSIONS A02633 REFERENCE A02633 !$#authors Sittman, D.B.; Chiu, I.M.; Pan, C.J.; Cohn, R.H.; Kedes, !1L.H.; Marzluff, W.F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:4078-4082 !$#title Isolation of two clusters of mouse histone genes. !$#cross-references MUID:82037786; PMID:6457299 !$#accession A02633 !'##molecule_type mRNA !'##residues 1-134 ##label SIT !'##cross-references GB:V00754; GB:J00421; NID:g51297; PIDN:CAA24131.1; !1PID:g51298 !'##experimental_source clone MM531 CLASSIFICATION #superfamily histone H3 KEYWORDS chromosomal protein; DNA binding; nucleosome core SUMMARY #length 134 #molecular-weight 14794 #checksum 5452 SEQUENCE /// ENTRY HSHU4 #type complete TITLE histone H4 [validated] - human CONTAINS osteogenic growth peptide (OGP) ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1987 #sequence_revision 03-Aug-1995 #text_change 08-Dec-2000 ACCESSIONS D40335; A93490; A90810; B32955; A61299; S17086; S17087; !1S17088; S17089; S17090; S17091; S23216; S51662; A57904; !1I59522; I37447; A02636 REFERENCE A40335 !$#authors Albig, W.; Kardalinou, E.; Drabent, B.; Zimmer, A.; !1Doenecke, D. !$#journal Genomics (1991) 10:940-948 !$#title Isolation and characterization of two human H1 histone genes !1within clusters of core histone genes. !$#cross-references MUID:92009931; PMID:1916825 !$#accession D40335 !'##molecule_type DNA !'##residues 1-103 ##label ALB !'##cross-references GB:M60749; NID:g184075; PIDN:AAA63188.1; !1PID:g184076 REFERENCE A93490 !$#authors Sierra, F.; Stein, G.; Stein, J. !$#journal Nucleic Acids Res. (1983) 11:7069-7086 !$#title Structure and in vitro transcription of a human H4 histone !1gene. !$#cross-references MUID:84041504; PMID:6314274 !$#accession A93490 !'##molecule_type DNA !'##residues 2-103 ##label SIE !'##cross-references EMBL:X00038 REFERENCE A90810 !$#authors Heintz, N.; Zernik, M.; Roeder, R.G. !$#journal Cell (1981) 24:661-668 !$#title The structure of the human histone genes: clustered but not !1tandemly repeated. !$#cross-references MUID:81234551; PMID:6265100 !$#accession A90810 !'##molecule_type DNA !'##residues 2-27,'H',29-32;69-71,'S',73-103 ##label HEI !'##cross-references GB:J00188; GB:J00189 REFERENCE A32955 !$#authors Alnemri, E.S.; Litwack, G. !$#journal J. Biol. Chem. (1989) 264:4104-4111 !$#title Glucocorticoid-induced lymphocytolysis is not mediated by an !1induced endonuclease. !$#cross-references MUID:89139481; PMID:2917990 !$#accession B32955 !'##molecule_type protein !'##residues 86-103 ##label ALN REFERENCE A61299 !$#authors Hayashi, T.; Ohe, Y.; Hayashi, H.; Iwai, K. !$#journal J. Biochem. (1982) 92:1995-2000 !$#title Human spleen histone H4. Isolation and amino acid sequence. !$#cross-references MUID:83135672; PMID:7161271 !$#accession A61299 !'##molecule_type protein !'##residues 2-4;14-18;21-36;41-45 ##label HAY REFERENCE S17086 !$#authors Doenecke, D.; Kardalinou, E. !$#submission submitted to the EMBL Data Library, July 1991 !$#accession S17086 !'##molecule_type DNA !'##residues 1-103 ##label DOE !'##cross-references EMBL:X60481; NID:g31994; PIDN:CAA43011.1; !1PID:g31995 !'##note gene a !$#accession S17087 !'##molecule_type DNA !'##residues 1-103 ##label DO1 !'##cross-references EMBL:X60482; NID:g31996; PIDN:CAA43012.1; !1PID:g31997 !'##note gene b !$#accession S17088 !'##molecule_type DNA !'##residues 1-103 ##label DO2 !'##cross-references EMBL:X60483; NID:g31998; PIDN:CAA43013.1; !1PID:g31999 !'##note gene d !$#accession S17089 !'##molecule_type DNA !'##residues 1-103 ##label DO3 !'##cross-references EMBL:X60484; NID:g32000; PIDN:CAA43014.1; !1PID:g32001 !'##note gene e !$#accession S17090 !'##molecule_type DNA !'##residues 1-103 ##label DO4 !'##cross-references EMBL:X60486; NID:g32003; PIDN:CAA43016.1; !1PID:g32004 !'##note gene g !$#accession S17091 !'##molecule_type DNA !'##residues 1-103 ##label DO5 !'##cross-references EMBL:X60487; NID:g32005; PIDN:CAA43017.1; !1PID:g32006 !'##note gene h REFERENCE S23216 !$#authors Runge, D.M.; Eick, S.; Doenecke, D. !$#submission submitted to the EMBL Data Library, June 1992 !$#accession S23216 !'##molecule_type DNA !'##residues 1-103 ##label RUN !'##cross-references EMBL:X67081; NID:g32007; PIDN:CAA47464.1; !1PID:g32008 !'##experimental_source leukocyte REFERENCE S51660 !$#authors Albig, W.; Doenecke, D. !$#submission submitted to the EMBL Data Library, December 1994 !$#description A human histone gene cluster containing a complete set of !1histone genes. !$#accession S51662 !'##molecule_type DNA !'##residues 1-103 ##label AL2 !'##cross-references EMBL:X83548; NID:g603555; PIDN:CAA58538.1; !1PID:g603556 !'##experimental_source leukocyte REFERENCE A57904 !$#authors Bab, I.; Gazit, D.; Chorev, M.; Muhlrad, A.; Shteyer, A.; !1Greenberg, Z.; Namdar, M.; Kahn, A. !$#journal EMBO J. (1992) 11:1867-1873 !$#title Histone H4-related osteogenic growth peptide (OGP): a novel !1circulating stimulator of osteoblastic activity. !$#cross-references MUID:92258396; PMID:1582415 !$#accession A57904 !'##molecule_type protein !'##residues 90-103 ##label BAB REFERENCE A44711 !$#authors Turner, B.M.; O'Neill, L.P.; Allan, I.M. !$#journal FEBS Lett. (1989) 253:141-145 !$#title Histone H4 acetylation in human cells. Frequency of !1acetylation at different sites defined by immunolabeling !1with site-specific antibodies. !$#cross-references MUID:89338730; PMID:2474456 !$#contents annotation; acetylation REFERENCE I59522 !$#authors Pauli, U.; Chrysogelos, S.; Stein, G.; Stein, J.; Nick, H. !$#journal Science (1987) 236:1308-1311 !$#title Protein-DNA interactions in vivo upstream of a cell !1cycle-regulated human H4 histone gene. !$#cross-references MUID:87234336; PMID:3035717 !$#accession I59522 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-103 ##label RES !'##cross-references GB:M16707; NID:g184063; PIDN:AAA52652.1; !1PID:g386773 !'##note cell cycle-regulated histone gene F0108 REFERENCE I37447 !$#authors Drabent, B.; Kardalinou, E.; Bode, C.; Doenecke, D. !$#journal DNA Cell Biol. (1995) 14:591-597 !$#title Association of histone H4 genes with the mammalian !1testis-specific H1t histone gene. !$#cross-references MUID:95352203; PMID:7626218 !$#accession I37447 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-103 ##label RE2 !'##cross-references EMBL:X60486; NID:g32003; PIDN:CAA43016.1; !1PID:g32004 GENETICS !$#gene GDB:H4F2; H4/g !'##cross-references GDB:120032; OMIM:142750 !$#map_position 1q21-1q21 !$#introns #status absent !$#note several gene clusters code for a number of identical protein !1sequences CLASSIFICATION #superfamily histone H4 KEYWORDS acetylated amino end; acetyllysine; chromosomal protein; DNA !1binding; methylated amino acid; nucleosome core FEATURE !$2-103 #product histone H4 #status experimental #label MAT\ !$90-103 #product osteogenic growth peptide #status !8experimental #label OGP\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental\ !$6,9,13,17 #binding_site acetyl (Lys) (covalent) (partial) !8#status experimental\ !$21 #modified_site N6,N6-dimethyllysine (Lys) #status !8experimental SUMMARY #length 103 #molecular-weight 11367 #checksum 9523 SEQUENCE /// ENTRY HSBO4 #type complete TITLE histone H4 - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 23-Oct-1981 #sequence_revision 23-Oct-1981 #text_change 16-Feb-1997 ACCESSIONS A92050; A92044; A02637; A43295 REFERENCE A92050 !$#authors Ogawa, Y.; Quagliarotti, G.; Jordan, J.; Taylor, C.W.; !1Starbuck, W.C.; Busch, H. !$#journal J. Biol. Chem. (1969) 244:4387-4392 !$#title Structural analysis of the glycine-rich, arginine-rich !1histone. III. Sequence of the amino-terminal half of the !1molecule containing the modified lysine residues and the !1total sequence. !$#cross-references MUID:69278585; PMID:5817359 !$#accession A92050 !'##molecule_type protein !'##residues 1-49 ##label OGA !'##experimental_source thymus REFERENCE A92044 !$#authors Quagliarotti, G.; Ogawa, Y.; Taylor, C.W.; Sautiere, P.; !1Jordan, J.; Starbuck, W.C.; Busch, H. !$#journal J. Biol. Chem. (1969) 244:1796-1802 !$#cross-references MUID:69167927; PMID:5780842 !$#accession A92044 !'##molecule_type protein !'##residues 50-102 ##label QUA !'##experimental_source thymus REFERENCE A90756 !$#authors Wilson, R.K.; Starbuck, W.C.; Taylor, C.W.; Jordan, J.; !1Busch, H. !$#journal Cancer Res. (1970) 30:2942-2951 !$#title Structure of the glycine-rich, arginine-rich histone of the !1Novikoff hepatoma. !$#cross-references MUID:71084062; PMID:4321977 !$#contents annotation; Novikoff hepatoma, partial sequence CLASSIFICATION #superfamily histone H4 KEYWORDS acetylated amino end; acetyllysine; chromosomal protein; DNA !1binding; methylated amino acid; nucleosome core FEATURE !$1 #modified_site acetylated amino end (Ser) #status !8experimental\ !$5,8,12 #binding_site acetyl (Lys) (covalent) #status !8predicted\ !$16 #binding_site acetyl (Lys) (covalent) (partial) !8#status experimental\ !$20 #modified_site N6-methyllysine or N6, !8N6-dimethyllysine (Lys) #status experimental SUMMARY #length 102 #molecular-weight 11236 #checksum 6544 SEQUENCE /// ENTRY HSPG4 #type complete TITLE histone H4 - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 16-Feb-1997 ACCESSIONS A02638 REFERENCE A02638 !$#authors Sautiere, P.; Lambelin-Breynaert, M.D.; Moschetto, Y.; !1Biserte, G. !$#journal Biochimie (1971) 53:711-715 !$#title Histone riche en glycine et en arginine du thymus de porc: !1etude des peptides tryptiques et sequence complete. !$#cross-references MUID:72052117; PMID:5123897 !$#accession A02638 !'##molecule_type protein !'##residues 1-102 ##label SAU !'##experimental_source thymus CLASSIFICATION #superfamily histone H4 KEYWORDS acetylated amino end; acetyllysine; chromosomal protein; DNA !1binding; methylated amino acid; nucleosome core FEATURE !$1 #modified_site acetylated amino end (Ser) #status !8experimental\ !$16 #binding_site acetyl (Lys) (covalent) (partial) !8#status experimental\ !$20 #modified_site N6-methyllysine (Lys) #status !8experimental SUMMARY #length 102 #molecular-weight 11236 #checksum 6544 SEQUENCE /// ENTRY HSRT4 #type complete TITLE histone H4 - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1987 #sequence_revision 01-Dec-1995 #text_change 22-Jun-1999 ACCESSIONS A91265; S02762; A02639; I70081; A27556; A30772; A94522 REFERENCE A91265 !$#authors Grimes, S.; Weisz-Carrington, P.; Daum III, H.; Smith, J.; !1Green, L.; Wright, K.; Stein, G.; Stein, J. !$#journal Exp. Cell Res. (1987) 173:534-545 !$#title A rat histone H4 gene closely associated with the !1testis-specific H1T gene. !$#cross-references MUID:88083222; PMID:3691674 !$#accession A91265 !'##molecule_type DNA !'##residues 1-103 ##label GRI !'##cross-references GB:M27433; GB:M24020; NID:g204600; PIDN:AAA60735.1; !1PID:g204601 REFERENCE S02762 !$#authors Wolfe, S.A.; Anderson, J.V.; Grimes, S.R.; Stein, G.S.; !1Stein, J.S. !$#journal Biochim. Biophys. Acta (1989) 1007:140-150 !$#title Comparison of the structural organization and expression of !1germinal and somatic rat histone H4 genes. !$#cross-references MUID:89150245; PMID:2920170 !$#accession S02762 !'##molecule_type DNA !'##residues 1-103 ##label WOL !'##cross-references EMBL:X13554; NID:g56348; PIDN:CAA31906.1; !1PID:g56349 REFERENCE A02639 !$#authors Sautiere, P.; Tyrou, D.; Moschetto, Y.; Biserte, G. !$#journal Biochimie (1971) 53:479-483 !$#title Structure primaire de l'histone riche en glycine et en !1arginine isolee de la tumeur de chloroleucemie du rat. !$#cross-references MUID:72055172; PMID:5171427 !$#accession A02639 !'##molecule_type protein !'##residues 2-103 ##label SAU !'##experimental_source chloroleukemic tumor REFERENCE I55352 !$#authors Wolfe, S.A.; Grimes, S.R. !$#journal J. Biol. Chem. (1991) 266:6637-6643 !$#title Protein-DNa interactions within the rat histone h4t !1promoter. !$#cross-references MUID:91177927; PMID:1706721 !$#accession I70081 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-103 ##label RES !'##cross-references GB:M28409; NID:g204550; PIDN:AAA41306.1; !1PID:g204552 GENETICS !$#gene H4t CLASSIFICATION #superfamily histone H4 KEYWORDS acetylated amino end; acetyllysine; chromosomal protein; DNA !1binding; methylated amino acid; nucleosome core FEATURE !$2-103 #product histone H4 #status experimental #label MAT\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental\ !$17 #binding_site acetyl (Lys) (covalent) (partial) !8#status experimental\ !$21 #modified_site N6-methyllysine (Lys) #status !8experimental SUMMARY #length 103 #molecular-weight 11367 #checksum 9523 SEQUENCE /// ENTRY HSCH4 #type complete TITLE histone H4 - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 22-Jun-1999 ACCESSIONS A02640; B29179 REFERENCE A93556 !$#authors Wang, S.W.; Robins, A.J.; d'Andrea, R.; Wells, J.R.E. !$#journal Nucleic Acids Res. (1985) 13:1369-1387 !$#title Inverted duplication of histone genes in chicken and !1disposition of regulatory sequences. !$#cross-references MUID:85215552; PMID:4000938 !$#accession A02640 !'##molecule_type DNA !'##residues 1-102 ##label WAN !'##cross-references GB:X02218; NID:g63471; PIDN:CAA26137.1; PID:g63472 REFERENCE A92434 !$#authors Sugarman, B.J.; Dodgson, J.B.; Engel, J.D. !$#journal J. Biol. Chem. (1983) 258:9005-9016 !$#title Genomic organization, DNA sequence, and expression of !1chicken embryonic histone genes. !$#cross-references MUID:83238548; PMID:6190814 !$#accession B29179 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-102 ##label SUG CLASSIFICATION #superfamily histone H4 KEYWORDS chromosomal protein; DNA binding; nucleosome core SUMMARY #length 102 #molecular-weight 11236 #checksum 6544 SEQUENCE /// ENTRY HSTR4 #type complete TITLE histone H4 - rainbow trout ORGANISM #formal_name Oncorhynchus mykiss #common_name rainbow trout DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 22-Jun-1999 ACCESSIONS A24552 REFERENCE A92961 !$#authors Winkfein, R.J.; Connor, W.; Mezquita, J.; Dixon, G.H. !$#journal J. Mol. Evol. (1985) 22:1-19 !$#title Histone H4 and H2B genes in rainbow trout (Salmo !1gairdnerii). !$#cross-references MUID:86037261; PMID:2997457 !$#accession A24552 !'##molecule_type DNA !'##residues 1-102 ##label WIN !'##cross-references GB:X02916; NID:g64320; PIDN:CAA26672.1; PID:g64321 !'##note initiator Met not shown REFERENCE A92085 !$#authors Candido, E.P.M.; Dixon, G.H. !$#journal J. Biol. Chem. (1971) 246:3182-3188 !$#title Sites of in vivo acetylation in trout testis histone IV. !$#cross-references MUID:71185689; PMID:5574393 !$#contents annotation; acetylation CLASSIFICATION #superfamily histone H4 KEYWORDS acetyllysine; chromosomal protein; DNA binding; nucleosome !1core FEATURE !$5,8,12,16 #binding_site acetyl (Lys) (covalent) (partial) !8#status experimental SUMMARY #length 102 #molecular-weight 11236 #checksum 6544 SEQUENCE /// ENTRY HSXL4 #type complete TITLE histone H4 - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 30-Jun-1987 #sequence_revision 31-Mar-1993 #text_change 22-Jun-1999 ACCESSIONS A02641; A20896; I51444; I51449 REFERENCE A91300 !$#authors Moorman, A.F.M.; De Boer, P.A.J.; De Laaf, R.T.M.; Van !1Dongen, W.M.A.M.; Destree, O.H.J. !$#journal FEBS Lett. (1981) 136:45-52 !$#title Primary structure of the histone H3 and H4 genes and their !1flanking sequences in a minor histone gene cluster of !1Xenopus laevis. !$#cross-references MUID:82095633; PMID:6274702 !$#accession A02641 !'##molecule_type DNA !'##residues 1-103 ##label MOO !'##cross-references GB:J00987 REFERENCE A20896 !$#authors Clerc, R.G.; Bucher, P.; Strub, K.; Birnstiel, M.L. !$#journal Nucleic Acids Res. (1983) 11:8641-8657 !$#title Transcription of a cloned Xenopus laevis H4 histone gene in !1the homologous frog oocyte system depends on an evolutionary !1conserved sequence motif in the -50 region. !$#cross-references MUID:84169505; PMID:6324093 !$#accession A20896 !'##molecule_type DNA !'##residues 1-103 ##label CLE !'##cross-references EMBL:X00224; NID:g64764; PIDN:CAA25042.1; !1PID:g64765 REFERENCE I51443 !$#authors Perry, M.; Thomsen, G.H.; Roeder, R.G. !$#journal J. Biol. Chem. (1985) 260:479-499 !$#title Genomic organization and nucleotide sequence of two distinct !1histone gene clusters from Xenopus laevis: Identification of !1novel conserved upstream sequence elements. !$#accession I51444 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-103 ##label PER !'##cross-references GB:M21286; NID:g214273; PIDN:AAA49761.1; !1PID:g214275 !'##note this sequence represents coding region 1429-1740 (NID:g214273) !$#accession I51449 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-103 ##label PE2 !'##cross-references GB:M21286; NID:g214273; PIDN:AAA49766.1; !1PID:g214280 !'##note this sequence represents coding region 14297-14608 !1(NID:g214273) CLASSIFICATION #superfamily histone H4 KEYWORDS chromosomal protein; DNA binding; nucleosome core FEATURE !$2-103 #product histone H4 #status predicted #label MAT SUMMARY #length 103 #molecular-weight 11367 #checksum 9523 SEQUENCE /// ENTRY HSUR4 #type complete TITLE histone H4 - sea urchin (Psammechinus miliaris) ORGANISM #formal_name Psammechinus miliaris #common_name sand urchin DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 24-Sep-1999 ACCESSIONS D93719; A91430; A02642 REFERENCE A93719 !$#authors Busslinger, M.; Portmann, R.; Irminger, J.C.; Birnstiel, !1M.L. !$#journal Nucleic Acids Res. (1980) 8:957-977 !$#title Ubiquitous and gene-specific regulatory 5' sequences in a !1sea urchin histone DNA clone coding for histone protein !1variants. !$#cross-references MUID:81076674; PMID:7443547 !$#accession D93719 !'##molecule_type DNA !'##residues 1-102 ##label BUS !'##cross-references GB:X01343; NID:g10036; PIDN:CAA25630.1; PID:g10037 REFERENCE A91430 !$#authors Wouters-Tyrou, D.; Sautiere, P.; Biserte, G. !$#journal FEBS Lett. (1976) 65:225-228 !$#title Covalent structure of the sea urchin histone H-4. !$#cross-references MUID:76210965; PMID:1278426 !$#accession A91430 !'##molecule_type protein !'##residues 1-102 ##label WOU COMMENT Lys-16 is acetylated in 20% of the molecules. CLASSIFICATION #superfamily histone H4 KEYWORDS acetylated amino end; acetyllysine; chromosomal protein; DNA !1binding; methylated amino acid; nucleosome core FEATURE !$1 #modified_site acetylated amino end (Ser) #status !8experimental\ !$16 #binding_site acetyl (Lys) (covalent) (partial) !8#status experimental\ !$20 #modified_site N6-methyllysine (Lys) #status !8experimental SUMMARY #length 102 #molecular-weight 11238 #checksum 6272 SEQUENCE /// ENTRY HSUR4P #type complete TITLE histone H4, embryonic - sea urchin (Strongylocentrotus purpuratus) ORGANISM #formal_name Strongylocentrotus purpuratus #common_name purple urchin DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 22-Jun-1999 ACCESSIONS A02643 REFERENCE A93627 !$#authors Kaumeyer, J.F.; Weinberg, E.S. !$#journal Nucleic Acids Res. (1986) 14:4557-4576 !$#title Sequence, organization and expression of late embryonic H3 !1and H4 histone genes from the sea urchin, Strongylocentrotus !1purpuratus. !$#cross-references MUID:86232591; PMID:3714486 !$#accession A02643 !'##molecule_type DNA !'##residues 1-102 ##label KAU !'##cross-references GB:X03952; NID:g10256; PIDN:CAA27581.1; PID:g10257 COMMENT This histone is expressed during late embryonic development. CLASSIFICATION #superfamily histone H4 KEYWORDS chromosomal protein; DNA binding; embryo; nucleosome core SUMMARY #length 102 #molecular-weight 11238 #checksum 6272 SEQUENCE /// ENTRY HSFF4 #type complete TITLE histone H4 - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 31-Oct-1980 #sequence_revision 10-Oct-1997 #text_change 16-Jun-2000 ACCESSIONS S10098; A02644; S71346; S71347 REFERENCE S10094 !$#authors Matsuo, Y.; Yamazaki, T. !$#journal Nucleic Acids Res. (1989) 17:225-238 !$#title tRNA derived insertion element in histone gene repeating !1unit of Drosophila melanogaster. !$#cross-references MUID:89098383; PMID:2536150 !$#accession S10098 !'##molecule_type DNA !'##residues 1-103 ##label MAT !'##cross-references EMBL:X14215; NID:g8066; PIDN:CAA32435.1; PID:g8071 !'##genetics CH1 REFERENCE A02630 !$#authors Goldberg, M.L. !$#citation Ph.D. thesis, Stanford Univ., 1979 !$#accession A02644 !'##molecule_type DNA !'##residues 2-72 ##label GOL REFERENCE S71345 !$#authors Akhmanova, A.; Miedema, K.; Hennig, W. !$#journal FEBS Lett. (1996) 388:219-222 !$#title Identification and characterization of the Drosophila !1histone H4 replacement gene. !$#cross-references MUID:96275536; PMID:8690091 !$#accession S71346 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type mRNA !'##residues 1-103 ##label AKH !'##cross-references EMBL:X97438; NID:g1419481; PIDN:CAA66068.1; !1PID:g1419482 !'##experimental_source strain Canton S !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1996 !$#accession S71347 !'##molecule_type DNA !'##residues 1-103 ##label AKW !'##cross-references EMBL:X97437; NID:g1419479; PIDN:CAA66067.1; !1PID:g1419480 !'##experimental_source strain Canton S !'##genetics CH2 GENETICS CH1 !$#gene FlyBase:His4 !'##cross-references FlyBase:FBgn0001200 GENETICS CH2 !$#gene H4r !$#map_position 3 !$#introns 60/3 CLASSIFICATION #superfamily histone H4 KEYWORDS chromosomal protein; DNA binding; methylated amino acid; !1nucleosome core; nucleus FEATURE !$6,9,13,17 #binding_site acetyl (Lys) (covalent) #status !8predicted\ !$21 #modified_site N6,N6-dimethyllysine (Lys) #status !8predicted SUMMARY #length 103 #molecular-weight 11381 #checksum 9525 SEQUENCE /// ENTRY HSZM4 #type complete TITLE histone H4 - maize ORGANISM #formal_name Zea mays #common_name maize DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 24-Sep-1999 ACCESSIONS A25642 REFERENCE A25642 !$#authors Philipps, G.; Chaubet, N.; Chaboute, M.E.; Ehling, M.; !1Gigot, C. !$#journal Gene (1986) 42:225-229 !$#title Genomic organization and nucleotide sequences of two corn !1histone H4 genes. !$#cross-references MUID:86275997; PMID:3015736 !$#accession A25642 !'##molecule_type DNA !'##residues 1-103 ##label PHI !'##cross-references GB:M13370; NID:g168500; PIDN:AAA33475.1; !1PID:g168501 CLASSIFICATION #superfamily histone H4 KEYWORDS chromosomal protein; DNA binding; nucleosome core FEATURE !$2-103 #product histone H4 #status predicted #label MAT SUMMARY #length 103 #molecular-weight 11409 #checksum 9618 SEQUENCE /// ENTRY HSWT4 #type complete TITLE histone H4 - wheat ORGANISM #formal_name Triticum aestivum #common_name common wheat DATE 15-Nov-1984 #sequence_revision 15-Nov-1984 #text_change 22-Jun-1999 ACCESSIONS A02645 REFERENCE A02645 !$#authors Tabata, T.; Sasaki, K.; Iwabuchi, M. !$#journal Nucleic Acids Res. (1983) 11:5865-5875 !$#title The structural organization and DNA sequence of a wheat !1histone H4 gene. !$#cross-references MUID:83299256; PMID:6310518 !$#accession A02645 !'##molecule_type DNA !'##residues 1-102 ##label TAB !'##cross-references GB:X00043; NID:g21794; PIDN:CAA24924.1; PID:g21795 CLASSIFICATION #superfamily histone H4 KEYWORDS acetylated amino end; chromosomal protein; DNA binding; !1nucleosome core FEATURE !$1 #modified_site acetylated amino end (Ser) #status !8predicted SUMMARY #length 102 #molecular-weight 11278 #checksum 6645 SEQUENCE /// ENTRY HSPM4 #type complete TITLE histone H4 - garden pea ORGANISM #formal_name Pisum sativum #common_name garden pea DATE 17-Mar-1987 #sequence_revision 10-Oct-1997 #text_change 22-Jun-1999 ACCESSIONS S60475; A02646 REFERENCE S60474 !$#authors Devitt, M.L.; Stafstrom, J.P. !$#journal Plant Mol. Biol. (1995) 29:255-265 !$#title Cell cycle regulation during growth-dormancy cycles in pea !1axillary buds. !$#cross-references MUID:96046745; PMID:7579177 !$#accession S60475 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-103 ##label DEV !'##cross-references EMBL:U10042; NID:g498897; PIDN:AAA86948.1; !1PID:g498898 !'##experimental_source cv. Alaska REFERENCE A02646 !$#authors DeLange, R.J.; Fambrough, D.M.; Smith, E.L.; Bonner, J. !$#journal J. Biol. Chem. (1969) 244:5669-5679 !$#title Calf and pea histone IV. III. Complete amino acid sequence !1of pea seedling histone IV; comparison with the homologous !1calf thymus histone. !$#cross-references MUID:70027325; PMID:5388597 !$#accession A02646 !'##molecule_type protein !'##residues 2-103 ##label DEL !'##experimental_source seedling COMMENT Lys residues in about 6% of molecules are acetylated, the !1acetyl groups being distributed between Lys-17 and one other !1Lys, probably Lys-9. CLASSIFICATION #superfamily histone H4 KEYWORDS acetylated amino end; acetyllysine; chromosomal protein; DNA !1binding; nucleosome core FEATURE !$2-103 #product histone H4 #status experimental #label MAT\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental\ !$9 #binding_site acetyl (Lys) (covalent) #status !8predicted\ !$17 #binding_site acetyl (Lys) (covalent) (partial) !8#status experimental SUMMARY #length 103 #molecular-weight 11409 #checksum 9618 SEQUENCE /// ENTRY HSWT41 #type complete TITLE histone H4 (TH091) - wheat ORGANISM #formal_name Triticum aestivum #common_name common wheat DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 22-Jun-1999 ACCESSIONS A24967 REFERENCE A24967 !$#authors Tabata, T.; Iwabuchi, M. !$#journal Gene (1984) 31:285-289 !$#title Molecular cloning and nucleotide sequence of a variant wheat !1histone H4 gene. !$#cross-references MUID:85128449; PMID:6526273 !$#accession A24967 !'##molecule_type DNA !'##residues 1-103 ##label TAB !'##cross-references GB:M12277; NID:g170746; PIDN:AAA34292.1; !1PID:g170747 !'##experimental_source cv. Horoshirikomugi CLASSIFICATION #superfamily histone H4 KEYWORDS chromosomal protein; DNA binding; nucleosome core FEATURE !$2-103 #product histone H4 (TH091) #status predicted #label !8MAT SUMMARY #length 103 #molecular-weight 11467 #checksum 9603 SEQUENCE /// ENTRY HSBY4 #type complete TITLE histone H4 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein N2752; protein YBR009c; protein YBR0122; protein YNL030w ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Dec-1980 #sequence_revision 30-Jun-1992 #text_change 21-Jul-2000 ACCESSIONS A02647; S45266; S07914; S45861; S45862; A91100; S62942; !1S62952 REFERENCE A92906 !$#authors Smith, M.M.; Andresson, O.S. !$#journal J. Mol. Biol. (1983) 169:663-690 !$#title DNA sequences of yeast H3 and H4 histone genes from two !1non-allelic gene sets encode identical H3 and H4 proteins. !$#cross-references MUID:84036173; PMID:6355483 !$#accession A02647 !'##molecule_type DNA !'##residues 1-103 ##label SMI !'##cross-references EMBL:X00724; NID:g3754; PIDN:CAA25311.1; PID:g3756 !'##genetics HHF1 !$#accession S45266 !'##molecule_type DNA !'##residues 1-103 ##label SM2 !'##cross-references EMBL:X00725; NID:g3757; PIDN:CAA25313.1; PID:g3759 !'##genetics HHF2 REFERENCE S07350 !$#authors Woudt, L.P.; Pastink, A.; Kempers-Veenstra, A.E.; Jansen, !1A.E.M.; Mager, W.H.; Planta, R.J. !$#journal Nucleic Acids Res. (1983) 11:5347-5360 !$#title The genes coding for histone H3 and H4 in Neurospora crassa !1are unique and contain intervening sequences. !$#cross-references MUID:83299219; PMID:6310494 !$#accession S07914 !'##molecule_type DNA !'##residues 1-103 ##label WOU !'##cross-references EMBL:K03154; NID:g171638; PIDN:AAA34660.1; !1PID:g171639 !'##genetics HHF2 !'##note the source is designated as Saccharomyces carlsbergensis REFERENCE S45730 !$#authors Lohan, A.J.E.; Wolfe, K.H. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S45861 !'##molecule_type DNA !'##residues 1-103 ##label LOH !'##cross-references EMBL:Z35878; GSPDB:GN00002; MIPS:YBR009c; !1NID:g536201; PIDN:CAA84947.1; PID:g536202 !'##genetics HHF1 REFERENCE S45862 !$#authors Entian, K.D.; Koetter, P.; Rose, M.; Li, Z.; Thermann, R.; !1Brendel, M.; Baur, A.; Boles, E.; Miosga, T.; !1Schaaff-Gerstenschlaeger, I.; Zimmermann, F.K. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S45862 !'##molecule_type DNA !'##residues 1-51 ##label ENT !'##cross-references EMBL:Z35878; GSPDB:GN00002; MIPS:YBR009c !'##genetics HHF1 REFERENCE A91100 !$#authors Brandt, W.F.; Patterson, K.; von Holt, C. !$#journal Eur. J. Biochem. (1980) 110:67-76 !$#title The histones of yeast. The isolation and partial structure !1of the core histones. !$#cross-references MUID:81066651; PMID:7002547 !$#accession A91100 !'##molecule_type protein !'##residues 25-45,'K',47-48;69-83;86-100 ##label BRA REFERENCE S62920 !$#authors Andre, B.; Iraqui Houssaini, I.; Urrestarazu, L.A.; Vissers, !1S. !$#submission submitted to the Protein Sequence Database, April 1996 !$#accession S62942 !'##molecule_type DNA !'##residues 1-103 ##label AND !'##cross-references EMBL:Z71306; GSPDB:GN00014; MIPS:YNL030w; !1NID:g1301867; PIDN:CAA95892.1; PID:g1301868 !'##experimental_source strain S288C !'##genetics HHF2 REFERENCE S62944 !$#authors Duesterhoeft, A.; Floeth, M.; Fritz, C.; Heuss-Neitzel, D.; !1Hilbert, H.; Moestl, D. !$#submission submitted to the Protein Sequence Database, April 1996 !$#accession S62952 !'##molecule_type DNA !'##residues 1-103 ##label DUE !'##cross-references EMBL:Z71306; GSPDB:GN00014; MIPS:YNL030w; !1NID:g1301867; PIDN:CAA95892.1; PID:g1301868 !'##experimental_source strain S288C !'##genetics HHF2 GENETICS HHF1 !$#gene SGD:HHF1; MIPS:YBR009c !'##cross-references MIPS:YBR009c; SGD:S0000213 !$#map_position 2R GENETICS HHF2 !$#gene SGD:HHF2; MIPS:YNL030w !'##cross-references MIPS:YNL030w; SGD:S0004975 !$#map_position 14L CLASSIFICATION #superfamily histone H4 KEYWORDS chromosomal protein; DNA binding; nucleosome core SUMMARY #length 103 #molecular-weight 11368 #checksum 9725 SEQUENCE /// ENTRY HSZP4 #type complete TITLE histone H4 [similarity] - fission yeast (Schizosaccharomyces pombe) ORGANISM #formal_name Schizosaccharomyces pombe DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 21-Jul-2000 ACCESSIONS D27399; T39289; T40748; T50114 REFERENCE A91027 !$#authors Matsumoto, S.; Yanagida, M. !$#journal EMBO J. (1985) 4:3531-3538 !$#title Histone gene organization of fission yeast: a common !1upstream sequence. !$#cross-references MUID:86135992; PMID:4092687 !$#accession D27399 !'##molecule_type DNA !'##residues 1-103 ##label MATS !'##cross-references GB:X05223; GB:M26378; NID:g4962; PIDN:CAA28853.1; !1PID:g4964 REFERENCE Z21841 !$#authors McDougall, R.C.; Rajandream, M.A.; Barrell, B.G.; !1Ramsperger, U.; Bothe, G.; Pohl, T. !$#submission submitted to the EMBL Data Library, July 1999 !$#accession T39289 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-103 ##label MCD !'##cross-references EMBL:AL096851; PIDN:CAB50975.1; GSPDB:GN00067; !1SPDB:SPBC1105.12 !'##experimental_source strain 972h-; cosmid c1105 !'##genetics MCD1 REFERENCE Z21948 !$#authors Lyne, M.; Rajandream, M.A.; Barrell, B.G.; Lauber, J.; !1Hilbert, H.; Duesterhoeft, A. !$#submission submitted to the EMBL Data Library, March 1998 !$#accession T40748 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-103 ##label LYN !'##cross-references EMBL:AL022072; PIDN:CAA17818.1; GSPDB:GN00067; !1SPDB:SPBC8D2.03c !'##experimental_source strain 972h-; cosmid c8D2 !'##genetics LYN2 REFERENCE Z25039 !$#authors Seeger, K.; Harris, D.; Wood, V.; Rajandream, M.A.; Barrell, !1B.G. !$#submission submitted to the EMBL Data Library, February 2000 !$#accession T50114 !'##molecule_type DNA !'##residues 1-103 ##label SEE !'##cross-references EMBL:AL157734; PIDN:CAB75771.1; GSPDB:GN00066; !1SPDB:SPAC1834.03c !'##experimental_source strain 972h-; cosmid c1834 !'##genetics SEE3 GENETICS MCD1 !$#gene SPBC1105.12 !$#map_position 2 GENETICS LYN2 !$#gene SPBC8D2.03c !$#map_position 2 GENETICS SEE3 !$#gene hhf1; SPAC1834.03c !$#map_position 1 CLASSIFICATION #superfamily histone H4 KEYWORDS chromosomal protein; DNA binding; nucleosome core FEATURE !$2-103 #product histone H4 #status predicted #label MAT SUMMARY #length 103 #molecular-weight 11423 #checksum 153 SEQUENCE /// ENTRY HSTE42 #type complete TITLE histone H4, minor - Tetrahymena pyriformis ORGANISM #formal_name Tetrahymena pyriformis DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 07-Dec-1999 ACCESSIONS A02649 REFERENCE A91982 !$#authors Hayashi, H.; Nomoto, M.; Iwai, K. !$#journal J. Biochem. (1984) 96:1449-1456 !$#title Tetrahymena histone H4. Complete amino acid sequences of two !1variants. !$#cross-references MUID:85130878; PMID:6441804 !$#accession A02649 !'##molecule_type protein !'##residues 1-102 ##label HAY !'##experimental_source amicronucleate GL strain COMMENT Tetrahymena pyriformis is a ciliated protozoan. COMMENT The minor histone H4 sequence from Tetrahymena pyriformis is !1identical with the fragments of the histone H4 sequence from !1T. thermophila. GENETICS !$#genetic_code SGC5 CLASSIFICATION #superfamily histone H4 KEYWORDS chromosomal protein; DNA binding; nucleosome core SUMMARY #length 102 #molecular-weight 11197 #checksum 7351 SEQUENCE /// ENTRY HSTE41 #type complete TITLE histone H4, major - Tetrahymena pyriformis ORGANISM #formal_name Tetrahymena pyriformis DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 07-Dec-1999 ACCESSIONS A02648 REFERENCE A91982 !$#authors Hayashi, H.; Nomoto, M.; Iwai, K. !$#journal J. Biochem. (1984) 96:1449-1456 !$#title Tetrahymena histone H4. Complete amino acid sequences of two !1variants. !$#cross-references MUID:85130878; PMID:6441804 !$#accession A02648 !'##molecule_type protein !'##residues 1-102 ##label HAY !'##experimental_source amicronucleate GL strain COMMENT Tetrahymena pyriformis is a ciliated protozoan. GENETICS !$#genetic_code SGC5 CLASSIFICATION #superfamily histone H4 KEYWORDS chromosomal protein; DNA binding; nucleosome core SUMMARY #length 102 #molecular-weight 11197 #checksum 7358 SEQUENCE /// ENTRY NSBOH7 #type complete TITLE nonhistone chromosomal protein HMG-17 - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Apr-1979 #sequence_revision 30-Apr-1979 #text_change 16-Feb-1997 ACCESSIONS A90200; A91248; A02651 REFERENCE A90200 !$#authors Walker, J.M.; Hastings, J.R.B.; Johns, E.W.; Gaastra, W. !$#journal Biochem. Biophys. Res. Commun. (1976) 73:72-78 !$#title The partial amino acid sequence of a non-histone chromosomal !1protein. !$#cross-references MUID:77065272; PMID:793593 !$#accession A90200 !'##molecule_type protein !'##residues 1-39 ##label WAL !'##note at position 3, smaller amounts of Val and Ala were found REFERENCE A91248 !$#authors Walker, J.M.; Hastings, J.R.B.; Johns, E.W. !$#journal Eur. J. Biochem. (1977) 76:461-468 !$#title The primary structure of a non-histone chromosomal protein. !$#cross-references MUID:77245937; PMID:330164 !$#accession A91248 !'##molecule_type protein !'##residues 28-89 ##label WA2 CLASSIFICATION #superfamily nonhistone chromosomal protein HMG-17 KEYWORDS chromosomal protein; DNA binding; nucleus SUMMARY #length 89 #molecular-weight 9248 #checksum 1648 SEQUENCE /// ENTRY NSCHH7 #type complete TITLE nonhistone chromosomal protein HMG-17 - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 31-May-1980 #sequence_revision 02-Dec-1994 #text_change 22-Jun-1999 ACCESSIONS A29951; A26811; JT0283; A90306; A91278; A02652 REFERENCE A29951 !$#authors Landsman, D.; Srikantha, T.; Bustin, M. !$#journal J. Biol. Chem. (1988) 263:3917-3923 !$#title Single copy gene for the chicken non-histone chromosomal !1protein HMG-17. !$#cross-references MUID:88153695; PMID:2831214 !$#accession A29951 !'##molecule_type DNA !'##residues 1-90 ##label LAN !'##cross-references GB:J03229; NID:g211922; PIDN:AAA48816.1; !1PID:g211923 REFERENCE A26811 !$#authors Landsman, D.; Bustin, M. !$#journal Nucleic Acids Res. (1987) 15:6750 !$#title Chicken non-histone chromosomal protein HMG-17 cDNA !1sequence. !$#cross-references MUID:87316947; PMID:3628013 !$#accession A26811 !'##molecule_type mRNA !'##residues 1-90 ##label LA2 REFERENCE JT0283 !$#authors Dodgson, J.B.; Browne, D.L.; Black, A.J. !$#journal Gene (1988) 63:287-295 !$#title Chicken chromosomal protein HMG-14 and HMG-17 cDNA clones: !1isolation, characterization and sequence comparison. !$#cross-references MUID:88255874; PMID:3384337 !$#accession JT0283 !'##molecule_type mRNA !'##residues 2-90 ##label DOD !'##cross-references GB:M26676; NID:g211924; PIDN:AAA48817.1; !1PID:g211925 REFERENCE A90306 !$#authors Walker, J.M.; Johns, E.W. !$#journal Biochem. J. (1980) 185:383-386 !$#title The isolation, characterization and partial sequences of the !1chicken erythrocyte non-histone chromosomal proteins HMG14 !1and HMG17. !$#cross-references MUID:80241724; PMID:7396821 !$#accession A90306 !'##molecule_type protein !'##residues 2-39 ##label WA1 REFERENCE A91278 !$#authors Walker, J.M.; Stearn, C.; Johns, E.W. !$#journal FEBS Lett. (1980) 112:207-210 !$#title The primary structure of non-histone chromosomal protein !1HMG17 from chicken erythrocyte nuclei. !$#cross-references MUID:80179183; PMID:7371857 !$#accession A91278 !'##molecule_type protein !'##residues 29-77,'N',79-80,'E',82-90 ##label WA2 COMMENT This protein binds directly to the nucleosome core particle. GENETICS !$#introns 5/3; 20/3; 30/3; 47/3; 79/3 CLASSIFICATION #superfamily nonhistone chromosomal protein HMG-17 KEYWORDS chromosomal protein; DNA binding; nucleus FEATURE !$2-90 #product nonhistone chromosomal protein HMG-17 !8#status experimental #label MAT SUMMARY #length 90 #molecular-weight 9453 #checksum 4833 SEQUENCE /// ENTRY NSTR6 #type complete TITLE nonhistone chromosomal protein H6 - rainbow trout ALTERNATE_NAMES histone T ORGANISM #formal_name Oncorhynchus mykiss #common_name rainbow trout DATE 30-Sep-1979 #sequence_revision 08-Oct-1981 #text_change 16-Feb-1997 ACCESSIONS A02653 REFERENCE A02653 !$#authors Watson, D.C.; Wong, N.C.W.; Dixon, G.H. !$#journal Eur. J. Biochem. (1979) 95:193-202 !$#title The complete amino-acid sequence of a trout-testis !1non-histone protein, H6, localized in a subset of !1nucleosomes and its similarity to calf-thymus non-histone !1proteins HMG-14 and HMG-17. !$#cross-references MUID:79213375; PMID:456349 !$#accession A02653 !'##molecule_type protein !'##residues 1-69 ##label WAT !'##experimental_source testis !'##note this protein was formerly called histone T CLASSIFICATION #superfamily nonhistone chromosomal protein HMG-17 KEYWORDS chromosomal protein; DNA binding; nucleus SUMMARY #length 69 #molecular-weight 6956 #checksum 5389 SEQUENCE /// ENTRY NSBOH4 #type complete TITLE nonhistone chromosomal protein HMG-14 - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Jul-1980 #sequence_revision 31-Jul-1980 #text_change 16-Feb-1997 ACCESSIONS A02654 REFERENCE A02654 !$#authors Walker, J.M.; Goodwin, G.H.; Johns, E.W. !$#journal FEBS Lett. (1979) 100:394-398 !$#title The primary structure of the nucleosome-associated !1chromosoma protein HMG 14. !$#cross-references MUID:79213800; PMID:456580 !$#accession A02654 !'##molecule_type protein !'##residues 1-100 ##label WAL CLASSIFICATION #superfamily nonhistone chromosomal protein HMG-17 KEYWORDS chromosomal protein; DNA binding; nucleus SUMMARY #length 100 #molecular-weight 10700 #checksum 3643 SEQUENCE /// ENTRY NSCHH4 #type complete TITLE nonhistone chromosomal protein HMG-14a - chicken ALTERNATE_NAMES high mobility group protein-14a ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Jun-1989 #sequence_revision 12-Apr-1996 #text_change 22-Jun-1999 ACCESSIONS S22122; JT0282; JU0140 REFERENCE S22122 !$#authors Browne, D.L.; Dodgson, J.B. !$#submission submitted to the EMBL Data Library, November 1991 !$#description The chicken HMG-14a gene is transcribed into multiple mRNAs. !$#accession S22122 !'##status preliminary !'##molecule_type DNA !'##residues 1-105 ##label BRO !'##cross-references EMBL:X63086 REFERENCE JT0283 !$#authors Dodgson, J.B.; Browne, D.L.; Black, A.J. !$#journal Gene (1988) 63:287-295 !$#title Chicken chromosomal protein HMG-14 and HMG-17 cDNA clones: !1isolation, characterization and sequence comparison. !$#cross-references MUID:88255874; PMID:3384337 !$#accession JT0282 !'##molecule_type mRNA !'##residues 2-105 ##label DOD !'##cross-references GB:M26675; NID:g211920; PIDN:AAA48815.1; !1PID:g211921 REFERENCE JU0140 !$#authors Browne, D.L.; Dodgson, J.B. !$#journal Gene (1993) 124:199-206 !$#title The gene encoding chicken chromosomal protein HMG-14a is !1transcribed into multiple mRNAs. !$#cross-references MUID:93185924; PMID:8444343 !$#accession JU0140 !'##molecule_type DNA !'##residues 2-5;16-42 ##label BR2 !'##cross-references EMBL:X63083 COMMENT The HMG proteins are small nonhistone chromosomal proteins, !1rich in both basic and acidic amino acids, and appear to be !1widely distributed in eukaryotes. COMMENT This protein is apparently one of the necessary components !1of actively transcribing chromatin. GENETICS !$#gene HHG-14a !$#introns 5/3; 15/3; 25/3; 42/3; 90/3 CLASSIFICATION #superfamily nonhistone chromosomal protein HMG-17 KEYWORDS chromosomal protein; DNA binding; nucleus SUMMARY #length 105 #molecular-weight 11357 #checksum 5870 SEQUENCE /// ENTRY NSRTH1 #type complete TITLE nonhistone chromosomal protein HMG-1 - rat ALTERNATE_NAMES 30K heparin-binding protein, brain; amphoterin ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 22-Jun-1999 ACCESSIONS A41175; A27298; A30188; B48771; A48771; C48771 REFERENCE A41175 !$#authors Merenmies, J.; Pihlaskari, R.; Laitinen, J.; Wartiovaara, !1J.; Rauvala, H. !$#journal J. Biol. Chem. (1991) 266:16722-16729 !$#title 30-kDa heparin-binding protein of brain (amphoterin) !1involved in neurite outgrowth. Amino acid sequence and !1localization in the filopodia of the advancing plasma !1membrane. !$#cross-references MUID:91358468; PMID:1885601 !$#accession A41175 !'##molecule_type mRNA !'##residues 1-215 ##label MER !'##cross-references GB:M64986; NID:g202884; PIDN:AAA40729.1; !1PID:g202885 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing !'##note the authors used antibodies to synthetic peptides to !1demonstrate this protein in filopodia of actively flattening !1and growing neurites; this differs from the expected nuclear !1location for high-mobility group proteins REFERENCE A27298 !$#authors Paonessa, G.; Frank, R.; Cortese, R. !$#journal Nucleic Acids Res. (1987) 15:9077 !$#title Nucleotide sequence of rat liver HMG1 cDNA. !$#cross-references MUID:88067717; PMID:3684582 !$#accession A27298 !'##molecule_type mRNA !'##residues 1-10,'R',12-82,84-95,97,'AS',100-215 ##label PAO REFERENCE A30188 !$#authors Rauvala, H.; Merenmies, J.; Pihlaskari, R.; Korkolainen, M.; !1Huhtala, M.L.; Panula, P. !$#journal J. Cell Biol. (1988) 107:2293-2305 !$#title The adhesive and neurite-promoting molecule p30: analysis of !1the amino-terminal sequence and production of antipeptide !1antibodies that detect p30 at the surface of neuroblastoma !1cells and of brain neurons. !$#cross-references MUID:89066894; PMID:2461949 !$#accession A30188 !'##molecule_type protein !'##residues 2-14,'X',16-21 ##label RAU REFERENCE A48771 !$#authors Parkkinen, J.; Raulo, E.; Merenmies, J.; Nolo, R.; Kajander, !1E.O.; Baumann, M.; Rauvala, H. !$#journal J. Biol. Chem. (1993) 268:19726-19738 !$#title Amphoterin, the 30-kDa protein in a family of HMG1-type !1polypeptides. Enhanced expression in transformed cells, !1leading edge localization, and interactions with plasminogen !1activation. !$#cross-references MUID:93374971; PMID:8366113 !$#accession B48771 !'##status preliminary !'##molecule_type protein !'##residues 98-105,'X',107-112 ##label PA2 !'##experimental_source postnatal brain !'##note sequence extracted from NCBI backbone (NCBIP:137788) CLASSIFICATION #superfamily nonhistone chromosomal protein HMG-2; HMG box !1homology KEYWORDS chromosomal protein; DNA binding; nucleus FEATURE !$2-215 #product nonhistone chromosomal protein HMG-1 #status !8experimental #label MAT\ !$6-83 #domain HMG box homology #label HMG1\ !$92-166 #domain HMG box homology #label HMG2 SUMMARY #length 215 #molecular-weight 24894 #checksum 295 SEQUENCE /// ENTRY S01947 #type complete TITLE nonhistone chromosomal protein HMG-1 - bovine ALTERNATE_NAMES 33K protein; high-mobility-group protein HMG-1 ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Sep-1989 #sequence_revision 22-Apr-1995 #text_change 22-Jun-1999 ACCESSIONS S01947; A61611; S10959; I45910 REFERENCE S01947 !$#authors Kaplan, D.J.; Duncan, C.H. !$#journal Nucleic Acids Res. (1988) 16:10375 !$#title Full length cDNA sequence for bovine high mobility group 1 !1(HMG1) protein. !$#cross-references MUID:89057489; PMID:3194213 !$#accession S01947 !'##molecule_type mRNA !'##residues 1-215 ##label KAP !'##cross-references EMBL:X12796; NID:g416; PIDN:CAA31284.1; PID:g417 REFERENCE A61611 !$#authors Walker, J.M.; Gooderham, K.; Hastings, J.R.B.; Mayes, E.; !1Johns, E.W. !$#journal FEBS Lett. (1980) 122:264-270 !$#title The primary structures of non-histone chromosomal proteins !1HMG 1 and 2. !$#cross-references MUID:81138848; PMID:7202717 !$#accession A61611 !'##molecule_type protein !'##residues 2-22,'S',24-40;48-105,'A',107-157,'X',160-193,'D',195 !1##label WAL REFERENCE S10726 !$#authors Christen, T.; Bischoff, M.; Hobi, R.; Kuenzle, C.C. !$#journal FEBS Lett. (1990) 267:139-141 !$#title High mobility group proteins 1 and 2 bind preferentially to !1brominated poly(dG-dC).poly(dG-dC) in the Z-DNA conformation !1but not to other types of Z-DNA. !$#cross-references MUID:90306387; PMID:2365081 !$#accession S10959 !'##molecule_type protein !'##residues 2-22,'X',24-38 ##label CHR REFERENCE I45910 !$#authors Pentecost, B.T.; Dixon, G.H. !$#journal Biosci. Rep. (1984) 4:49-57 !$#title Isolation and partial sequence of bovine cDNA clones for the !1high-mobility-group protein (HMG-1). !$#cross-references MUID:84128872; PMID:6141822 !$#accession I45910 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 'PGG',119,'V',121-215 ##label PEN !'##cross-references GB:M26110; NID:g163156; PIDN:AAA30567.1; !1PID:g163157 CLASSIFICATION #superfamily nonhistone chromosomal protein HMG-2; HMG box !1homology KEYWORDS chromosomal protein; DNA binding; duplication; nucleus FEATURE !$2-215 #product nonhistone chromosomal protein HMG-1 #status !8predicted #label MAT\ !$6-83 #domain HMG box homology #label HMG1\ !$92-166 #domain HMG box homology #label HMG2 SUMMARY #length 215 #molecular-weight 24908 #checksum 318 SEQUENCE /// ENTRY NSHUH2 #type complete TITLE nonhistone chromosomal protein HMG-2 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 22-Jun-1999 ACCESSIONS A42425; S20061; S18068 REFERENCE A42425 !$#authors Shirakawa, H.; Yoshida, M. !$#journal J. Biol. Chem. (1992) 267:6641-6645 !$#title Structure of a gene coding for human HMG2 protein. !$#cross-references MUID:92202209; PMID:1551873 !$#accession A42425 !'##molecule_type DNA !'##residues 2-209 ##label SHI !'##cross-references GB:M83665; NID:g184235; PIDN:AAA58659.1; !1PID:g184236 !'##note sequence extracted from NCBI backbone (NCBIN:89899, !1NCBIP:89900) !'##note initiator Met not shown REFERENCE S20061 !$#authors Majumdar, A.; Brown, D.; Kerby, S.; Rudzinski, I.; Polte, !1T.; Randhawa, Z.; Seidman, M.M. !$#journal Nucleic Acids Res. (1991) 19:6643 !$#title Sequence of human HMG2 cDNA. !$#cross-references MUID:92093633; PMID:1754403 !$#accession S20061 !'##molecule_type mRNA !'##residues 1-209 ##label MAJ !'##cross-references EMBL:X62534; NID:g32332; PIDN:CAA44395.1; !1PID:g32333 GENETICS !$#gene GDB:NHCP2 !'##cross-references GDB:119451; OMIM:118880 !$#map_position 7pter-7qter CLASSIFICATION #superfamily nonhistone chromosomal protein HMG-2; HMG box !1homology KEYWORDS chromosomal protein; DNA binding; nucleus FEATURE !$6-83 #domain HMG box homology #label HMG1\ !$92-166 #domain HMG box homology #label HMG2 SUMMARY #length 209 #molecular-weight 24034 #checksum 3948 SEQUENCE /// ENTRY S50980 #type complete TITLE NHP10 protein - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YD8119.05c; protein YDL002c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-Nov-1999 ACCESSIONS S50980 REFERENCE S50976 !$#authors Murphy, L.; Richards, C.; Gentles, S.; Harris, D. !$#submission submitted to the EMBL Data Library, January 1995 !$#accession S50980 !'##molecule_type DNA !'##residues 1-203 ##label MUR !'##cross-references EMBL:Z48008; NID:g642799; PIDN:CAA88059.1; !1PID:g642804; GSPDB:GN00004; MIPS:YDL002c GENETICS !$#gene SGD:NHP10; MIPS:YDL002c !'##cross-references SGD:S0002160; MIPS:YDL002c !$#map_position 4L CLASSIFICATION #superfamily yeast NHP10 protein; HMG box homology FEATURE !$91-162 #domain HMG box homology #label HMG1 SUMMARY #length 203 #molecular-weight 23857 #checksum 8549 SEQUENCE /// ENTRY S08156 #type complete TITLE gene T protein - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S08156 REFERENCE S08156 !$#authors Herrmann, B.G.; Labeit, S.; Poustka, A.; King, T.R.; !1Lehrach, H. !$#journal Nature (1990) 343:617-622 !$#title Cloning of the T gene required in mesoderm formation in the !1mouse. !$#cross-references MUID:90158787; PMID:2154694 !$#accession S08156 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-436 ##label HER !'##cross-references GB:X51683; NID:g55053; PIDN:CAA35985.1; PID:g55054 GENETICS !$#gene T !$#map_position 17 CLASSIFICATION #superfamily mouse gene T protein; T-box homology KEYWORDS DNA binding; transcription regulation FEATURE !$51-227 #domain T-box homology #label TBX SUMMARY #length 436 #molecular-weight 47440 #checksum 2829 SEQUENCE /// ENTRY A41056 #type complete TITLE brachyury homolog - African clawed frog ALTERNATE_NAMES gene T homolog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A41056 REFERENCE A41056 !$#authors Smith, J.C.; Price, B.M.J.; Green, J.B.A.; Weigel, D.; !1Herrmann, B.G. !$#journal Cell (1991) 67:79-87 !$#title Expression of a Xenopus homolog of Brachyury (T) is an !1immediate-early response to mesoderm induction. !$#cross-references MUID:92005698; PMID:1717160 !$#accession A41056 !'##molecule_type mRNA !'##residues 1-432 ##label SMI !'##cross-references GB:M77243; NID:g213999; PIDN:AAA49663.1; !1PID:g214000 COMMENT Both basic fibroblast growth factor (bFGF) and activin A !1induce expression of this protein in embryos in an !1immediate-early response to mesoderm induction. GENETICS !$#gene Xbra CLASSIFICATION #superfamily mouse gene T protein; T-box homology KEYWORDS DNA binding; mesoderm; transcription regulation FEATURE !$49-225 #domain T-box homology #label TBX SUMMARY #length 432 #molecular-weight 47599 #checksum 6460 SEQUENCE /// ENTRY A49125 #type complete TITLE gastrulation regulatory protein Zf-T - zebra fish ORGANISM #formal_name Brachydanio rerio #common_name zebra fish DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A49125 REFERENCE A49125 !$#authors Schulte-Merker, S.; Ho, R.K.; Herrmann, B.G.; !1Nusslein-Volhard, C. !$#journal Development (1992) 116:1021-1032 !$#title The protein product of the zebrafish homologue of the mouse !1T gene is expressed in nuclei of the germ ring and the !1notochord of the early embryo. !$#cross-references MUID:93201989; PMID:1295726 !$#accession A49125 !'##status preliminary !'##molecule_type mRNA !'##residues 1-423 ##label SCH !'##cross-references GB:S57147; NID:g299316; PIDN:AAB25829.1; !1PID:g299317 !'##experimental_source embryo !'##note sequence extracted from NCBI backbone (NCBIN:127982, !1NCBIP:127985) CLASSIFICATION #superfamily mouse gene T protein; T-box homology FEATURE !$44-220 #domain T-box homology #label TBX SUMMARY #length 423 #molecular-weight 45834 #checksum 7044 SEQUENCE /// ENTRY A40213 #type complete TITLE optic lobe development omb protein - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES omb protein ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A40213; S34827 REFERENCE A40213 !$#authors Pflugfelder, G.O.; Roth, H.; Poeck, B.; Kerscher, S.; !1Schwarz, H.; Jonschker, B.; Heisenberg, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:1199-1203 !$#title The lethal(1)optomotor-blind gene of Drosophila melanogaster !1is a major organizer of optic lobe development: isolation !1and characterization of the gene. !$#cross-references MUID:92159016; PMID:1741374 !$#accession A40213 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-974 ##label PFL !'##cross-references GB:M81796; NID:g158018; PIDN:AAA28736.1; !1PID:g158019 !'##note sequence extracted from NCBI backbone (NCBIP:82056) REFERENCE S34827 !$#authors Poeck, B.; Balles, J.; Pflugfelder, G.O. !$#journal Mol. Gen. Genet. (1993) 238:325-332 !$#title Transcript identification in the optomotor-blind locus of !1Drosophila melanogaster by intragenic recombination mapping !1and PCR-aided sequence analysis of lethal point mutations. !$#cross-references MUID:93261414; PMID:8492800 !$#accession S34827 !'##molecule_type DNA !'##residues 1-447 ##label POE !'##cross-references GB:S61732; NID:g402317; PIDN:AAB26697.1; !1PID:g402318 !'##experimental_source larva GENETICS !$#gene FlyBase:bi !'##cross-references FlyBase:FBgn0000179 CLASSIFICATION #superfamily optic lobe development omb protein; T-box !1homology KEYWORDS DNA binding FEATURE !$337-521 #domain T-box homology #label TBX SUMMARY #length 974 #molecular-weight 102874 #checksum 3424 SEQUENCE /// ENTRY A55160 #type complete TITLE Trg protein - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A55160 REFERENCE A55160 !$#authors Kispert, A.; Herrmann, B.G.; Leptin, M.; Reuter, R. !$#journal Genes Dev. (1994) 8:2137-2150 !$#title Homologs of the mouse Brachyury gene are involved in the !1specification of posterior terminal structures in !1Drosophila, Tribolium, and Locusta. !$#cross-references MUID:95047361; PMID:7958884 !$#accession A55160 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-720 ##label KIS GENETICS !$#gene FlyBase:Trg !'##cross-references FlyBase:FBgn0011723 CLASSIFICATION #superfamily Drosophila Trg protein; T-box homology FEATURE !$96-272 #domain T-box homology #label TBX SUMMARY #length 720 #molecular-weight 74652 #checksum 8849 SEQUENCE /// ENTRY S41019 #type complete TITLE transcription factor tbx9 - Caenorhabditis elegans ALTERNATE_NAMES Ce-Hox-9 protein; hypothetical protein T07C4.6 ORGANISM #formal_name Caenorhabditis elegans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S41019; B56530 REFERENCE S41014 !$#authors Berks, M. !$#submission submitted to the EMBL Data Library, January 1994 !$#accession S41019 !'##status preliminary !'##molecule_type DNA !'##residues 1-377 ##label BER !'##cross-references EMBL:Z29443; NID:g1067051; PID:g443833 REFERENCE A56530 !$#authors Agulnik, S.I.; Bollag, R.J.; Silver, L.M. !$#journal Genomics (1995) 25:214-219 !$#title Conservation of the T-box gene family from Mus musculus to !1Caenorhabditis elegans. !$#cross-references MUID:95293375; PMID:7774921 !$#accession B56530 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type DNA !'##residues 100-286 ##label AGU !'##cross-references GB:Z29443 GENETICS !$#introns 49/2; 83/2; 183/2; 208/3; 259/3 CLASSIFICATION #superfamily Caenorhabditis elegans transcription factor !1tbx9; T-box homology KEYWORDS DNA binding FEATURE !$100-286 #domain T-box homology #label TBX SUMMARY #length 377 #molecular-weight 43232 #checksum 8092 SEQUENCE /// ENTRY S41015 #type complete TITLE transcription factor tbx8 - Caenorhabditis elegans ALTERNATE_NAMES hypothetical protein T07C4.2 ORGANISM #formal_name Caenorhabditis elegans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S41015; A56530 REFERENCE S41014 !$#authors Berks, M. !$#submission submitted to the EMBL Data Library, January 1994 !$#accession S41015 !'##molecule_type DNA !'##residues 1-479 ##label BER !'##cross-references EMBL:Z29443 REFERENCE A56530 !$#authors Agulnik, S.I.; Bollag, R.J.; Silver, L.M. !$#journal Genomics (1995) 25:214-219 !$#title Conservation of the T-box gene family from Mus musculus to !1Caenorhabditis elegans. !$#cross-references MUID:95293375; PMID:7774921 !$#accession A56530 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type DNA !'##residues 153-340 ##label AGU !'##cross-references GB:Z29443 GENETICS !$#introns 77/3; 101/3; 134/3; 236/2; 261/3; 312/3; 450/3 CLASSIFICATION #superfamily Caenorhabditis elegans transcription factor !1tbx8; T-box homology KEYWORDS DNA binding FEATURE !$153-340 #domain T-box homology #label TBX SUMMARY #length 479 #molecular-weight 54304 #checksum 486 SEQUENCE /// ENTRY S46458 #type complete TITLE transcription factor tbx2 - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S46458 REFERENCE S46458 !$#authors Bollag, R.J.; Siegfried, Z.; Cebra-Thomas, J.A.; Garvey, N.; !1Davison, E.M.; Silver, L.M. !$#journal Nature Genet. (1994) 7:383-389 !$#title An ancient family of embryonically expressed mouse genes !1sharing a conserved protein motif with the T locus. !$#cross-references MUID:95004605; PMID:7920656 !$#accession S46458 !'##status preliminary !'##molecule_type mRNA !'##residues 1-701 ##label BOL !'##cross-references GB:U15566; NID:g558875; PIDN:AAC52697.1; !1PID:g558876 GENETICS !$#gene Tbx2 CLASSIFICATION #superfamily mouse transcription factor tbx2; T-box homology FEATURE !$104-285 #domain T-box homology #label TBX SUMMARY #length 701 #molecular-weight 74243 #checksum 9150 SEQUENCE /// ENTRY S71905 #type complete TITLE probable nonhistone chromosomal HMG protein EF1 - Chilo iridescent virus ORGANISM #formal_name Chilo iridescent virus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 23-Mar-2001 ACCESSIONS S71905; S41506; S41507 REFERENCE S71905 !$#authors Schnitzler, P.; Hug, M.; Handermann, M.; Janssen, W.; !1Koonin, E.V.; Delius, H.; Darai, C. !$#submission submitted to the EMBL Data Library, January 1994 !$#description Identification of genes encoding zinc finger proteins, !1non-histone chromosomal HMG protein homologue, and a !1putative GTP phosphohydrolase in the genome of Chilo !1iridescent virus. !$#accession S71905 !'##molecule_type DNA !'##residues 1-221 ##label SCH !'##cross-references EMBL:L22300; NID:g438679; PIDN:AAA17843.1; !1PID:g438680 REFERENCE S41506 !$#authors Schnitzler, P.; Hug, M.; Handermann, M.; Janssen, W.; !1Koonin, E.V.; Delius, H.; Darai, G. !$#journal Nucleic Acids Res. (1994) 22:158-166 !$#title Identification of genes encoding zinc finger proteins, !1non-histone chromosomal HMG protein homologue, and a !1putative GTP phosphohydrolase in the genome of Chilo !1iridescent virus. !$#cross-references MUID:94167241; PMID:8121799 !$#accession S41506 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 46-116 ##label SCW !'##cross-references EMBL:L22300 CLASSIFICATION #superfamily Chilo iridescent virus probable nonhistone !1chromosomal HMG protein EF1; HMG box homology KEYWORDS chromosomal protein FEATURE !$51-125 #domain HMG box homology #label HMG1 SUMMARY #length 221 #molecular-weight 25939 #checksum 8758 SEQUENCE /// ENTRY BGHU #type complete TITLE spermatid transition protein 1 - human ALTERNATE_NAMES testis-specific basic protein ORGANISM #formal_name Homo sapiens #common_name man DATE 01-Feb-1991 #sequence_revision 15-Oct-1996 #text_change 22-Jun-1999 ACCESSIONS A37106; S01241 REFERENCE A37106 !$#authors Luerssen, H.; Mattei, M.G.; Schroeter, M.; Grzeschik, K.H.; !1Adham, I.M.; Engel, W. !$#journal Genomics (1990) 8:324-330 !$#title Nucleotide sequence of the gene for human transition protein !11 and its chromosomal localization on chromosome 2. !$#cross-references MUID:91065651; PMID:2249851 !$#accession A37106 !'##molecule_type DNA !'##residues 1-55 ##label LUE1 !'##cross-references GB:M59924; NID:g339778; PIDN:AAA61202.1; !1PID:g339779 !'##experimental_source leukocyte REFERENCE S01241 !$#authors Luerssen, H.; Hoyer-Fender, S.; Engel, W. !$#journal Nucleic Acids Res. (1988) 16:7723 !$#title The nucleotide sequence of human transition protein 1 cDNA. !$#cross-references MUID:88319961; PMID:3412903 !$#accession S01241 !'##molecule_type mRNA !'##residues 1-55 ##label LUE2 !'##cross-references EMBL:X07948; NID:g37237; PIDN:CAA30774.1; !1PID:g37238 COMMENT This protein replaces histones and is replaced by other !1transition proteins or protamines during spermatogenesis. GENETICS !$#gene GDB:TNP1 !'##cross-references GDB:125311; OMIM:190231 !$#map_position 2q35-2q36 CLASSIFICATION #superfamily spermatid transition protein 1 KEYWORDS DNA binding; nucleus; phosphoprotein; spermatogenesis; !1testis FEATURE !$2-55 #product spermatid transition protein 1 #status !8predicted #label MAT\ !$40 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 55 #molecular-weight 6424 #checksum 9346 SEQUENCE /// ENTRY BGPG #type complete TITLE spermatid transition protein 1 - pig ALTERNATE_NAMES testis-specific basic protein ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 22-Nov-1993 #sequence_revision 15-Oct-1996 #text_change 22-Jun-1999 ACCESSIONS S21670; A37347 REFERENCE S21670 !$#authors Keime, S.; Heitland, K.; Kumm, S.; Schloesser, M.; Hroch, !1N.; Holtz, W.; Engel, W. !$#journal Biol. Chem. Hoppe-Seyler (1992) 373:261-270 !$#title Characterization of four genes encoding basic proteins of !1the porcine spermatid nucleus and close linkage of three of !1them. !$#cross-references MUID:92329006; PMID:1627265 !$#accession S21670 !'##molecule_type DNA !'##residues 1-55 ##label KEI !'##cross-references EMBL:M80679; NID:g164700 REFERENCE A37347 !$#authors Kremling, H.; Luerssen, H.; Adham, I.M.; Klemm, U.; !1Tsaousidou, S.; Engel, W. !$#journal Differentiation (1989) 40:184-190 !$#title Nucleotide sequences and expression of cDNA clones for boar !1and bull transition protein 1 and its evolutionary !1conservation in mammals. !$#cross-references MUID:89378557; PMID:2777004 !$#accession A37347 !'##molecule_type mRNA !'##residues 2-55 ##label KRE !'##cross-references GB:X16170; NID:g2139; PIDN:CAA34292.1; PID:g2140 !'##note translation of initiator Met is not shown COMMENT This protein replaces histones and is replaced by other !1transition proteins or protamines during spermatogenesis. GENETICS !$#introns 47/1 CLASSIFICATION #superfamily spermatid transition protein 1 KEYWORDS DNA binding; nucleus; phosphoprotein; spermatogenesis; !1testis FEATURE !$2-55 #product spermatid transition protein 1 #status !8predicted #label MAT\ !$40 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 55 #molecular-weight 6424 #checksum 8748 SEQUENCE /// ENTRY BGRT #type complete TITLE spermatid transition protein 1 - rat ALTERNATE_NAMES testis-specific basic protein ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 24-Apr-1984 #sequence_revision 15-Oct-1996 #text_change 22-Jun-1999 ACCESSIONS A29095; JS0109; A92171; A02655; S03177 REFERENCE A29095 !$#authors Heidaran, M.A.; Kistler, W.S. !$#journal Gene (1987) 54:281-284 !$#title Isolation of a cDNA clone for transition protein 1 (TP1), a !1major chromosomal protein of mammalian spermatids. !$#cross-references MUID:88005793; PMID:2820847 !$#accession A29095 !'##molecule_type mRNA !'##residues 1-55 ##label HEI !'##cross-references GB:M17096; NID:g207414; PIDN:AAA42260.1; !1PID:g207415 REFERENCE JS0109 !$#authors Heidaran, M.A.; Kozak, C.A.; Kistler, W.S. !$#journal Gene (1989) 75:39-46 !$#title Nucleotide sequence of the Stp-1 gene coding for rat !1spermatid nuclear transition protein 1 (TP1): homology with !1protamine P1 and assignment of the mouse Stp-1 gene to !1chromosome 1. !$#cross-references MUID:89252920; PMID:2524424 !$#accession JS0109 !'##molecule_type DNA !'##residues 1-55 ##label HEI2 !'##cross-references EMBL:X07284; NID:g57306; PIDN:CAA30264.1; !1PID:g57307 REFERENCE A92171 !$#authors Kistler, W.S.; Noyes, C.; Hsu, R.; Heinrikson, R.L. !$#journal J. Biol. Chem. (1975) 250:1847-1853 !$#title The amino acid sequence of a testis-specific basic protein !1that is associated with spermatogenesis. !$#cross-references MUID:75095670; PMID:1112834 !$#accession A92171 !'##molecule_type protein !'##residues 2-45,'S',47,'D',49-55 ##label KIS REFERENCE A90190 !$#authors Kistler, W.S.; Noyes, C.; Heinrikson, R.L. !$#journal Biochem. Biophys. Res. Commun. (1974) 57:341-347 !$#title Partial structural analysis of a highly basic low molecular !1weight protein from rat testis. !$#cross-references MUID:74167135; PMID:4829397 !$#contents annotation; partial sequence COMMENT The presence of this protein in mammalian testes is !1correlated with the occurrence of developing spermatids in !1the seminiferous tubules, but it cannot be detected in !1epididymal spermatozoa. COMMENT This protein replaces histones and is replaced by other !1transition proteins or protamines during spermatogenesis. GENETICS !$#map_position 1 !$#introns 47/1 CLASSIFICATION #superfamily spermatid transition protein 1 KEYWORDS chromosomal protein; DNA binding; nucleus; phosphoprotein; !1spermatogenesis; testis FEATURE !$2-55 #product spermatid transition protein 1 #status !8experimental #label MAT\ !$40 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 55 #molecular-weight 6395 #checksum 9605 SEQUENCE /// ENTRY BGMS #type complete TITLE spermatid transition protein 1 - mouse ALTERNATE_NAMES testis-specific basic protein ORGANISM #formal_name Mus musculus #common_name house mouse DATE 05-Jun-1992 #sequence_revision 15-Oct-1996 #text_change 22-Jun-1999 ACCESSIONS A40561; JS0038 REFERENCE A40561 !$#authors Yelick, P.C.; Kozak, C.; Kwon, Y.K.; Seldin, M.F.; Hecht, !1N.B. !$#journal Genomics (1991) 11:687-694 !$#title The mouse transition protein 1 gene contains a B1 repetitive !1element and is located on chromosome 1. !$#cross-references MUID:92128951; PMID:1685480 !$#accession A40561 !'##molecule_type DNA !'##residues 1-55 ##label YEL !'##cross-references GB:S80846; NID:g244180; PIDN:AAB21244.1; !1PID:g244181 REFERENCE JS0038 !$#authors Kleene, K.C.; Borzorgzadeh, A.; Flynn, J.F.; Yelick, P.C.; !1Hecht, N.B. !$#journal Biochim. Biophys. Acta (1988) 950:215-220 !$#title Nucleotide sequence of a cDNA clone encoding mouse !1transition protein 1. !$#cross-references MUID:88252150; PMID:3382664 !$#accession JS0038 !'##molecule_type mRNA !'##residues 1-55 ##label KLE !'##cross-references EMBL:X12521; NID:g54850; PIDN:CAA31039.1; !1PID:g54851 COMMENT This protein replaces histones and is replaced by other !1transition proteins or protamines during spermatogenesis. GENETICS !$#map_position 1 !$#introns 47/1 CLASSIFICATION #superfamily spermatid transition protein 1 KEYWORDS DNA binding; nucleus; phosphoprotein; spermatogenesis; !1testis FEATURE !$2-55 #product spermatid transition protein 1 #status !8predicted #label MAT\ !$40 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 55 #molecular-weight 6407 #checksum 9716 SEQUENCE /// ENTRY BGBO #type complete TITLE spermatid transition protein 1 - bovine ALTERNATE_NAMES testis-specific basic protein ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 21-Jul-1995 #sequence_revision 15-Oct-1996 #text_change 22-Jun-1999 ACCESSIONS A56647; B37347 REFERENCE A56647 !$#authors Kim, Y.; Kremling, H.; Tessmann, D.; Engel, W. !$#journal DNA Seq. (1992) 3:123-125 !$#title Nucleotide sequence and exon-intron structure of the bovine !1transition protein 1 gene. !$#cross-references MUID:93091245; PMID:1457814 !$#accession A56647 !'##molecule_type DNA !'##residues 1-55 ##label KIM !'##cross-references GB:X65041; NID:g807; PIDN:CAA46175.1; PID:g808 !'##note sequence modified after extraction from NCBI backbone REFERENCE A37347 !$#authors Kremling, H.; Luerssen, H.; Adham, I.M.; Klemm, U.; !1Tsaousidou, S.; Engel, W. !$#journal Differentiation (1989) 40:184-190 !$#title Nucleotide sequences and expression of cDNA clones for boar !1and bull transition protein 1 and its evolutionary !1conservation in mammals. !$#cross-references MUID:89378557; PMID:2777004 !$#accession B37347 !'##molecule_type mRNA !'##residues 2-55 ##label KRE !'##cross-references GB:X16171; NID:g805; PIDN:CAA34293.1; PID:g806 !'##note translation of initiator Met is not shown COMMENT This protein replaces histones and is replaced by other !1transition proteins or protamines during spermatogenesis. GENETICS !$#gene TNP1 !$#introns 47/1 CLASSIFICATION #superfamily spermatid transition protein 1 KEYWORDS DNA binding; nucleus; phosphoprotein; spermatogenesis; !1testis FEATURE !$2-55 #product spermatid transition protein 1 #status !8predicted #label MAT\ !$40 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 55 #molecular-weight 6455 #checksum 9292 SEQUENCE /// ENTRY BGSH #type complete TITLE spermatid transition protein 1 - sheep ALTERNATE_NAMES testis-specific basic protein; TP1; transition protein T ORGANISM #formal_name Ovis orientalis aries, Ovis ammon aries #common_name domestic sheep DATE 21-Nov-1993 #sequence_revision 15-Oct-1996 #text_change 02-Jul-1998 ACCESSIONS S16075 REFERENCE S16075 !$#authors Chirat, F.; Martinage, A.; Briand, G.; Kouach, M.; van !1Dorsselaer, A.; Loir, M.; Sautiere, P. !$#journal Eur. J. Biochem. (1991) 198:13-20 !$#title Nuclear transition protein 1 from ram elongating spermatids. !1Mass spectrometric characterization, primary structure and !1phosphorylation sites of two variants. !$#cross-references MUID:91249791; PMID:2040274 !$#accession S16075 !'##molecule_type protein !'##residues 1-54 ##label CHI !'##note 27-Gly was also seen in about 20% of the molecules COMMENT This protein replaces histones and is replaced by other !1transition proteins or protamines during spermatogenesis. CLASSIFICATION #superfamily spermatid transition protein 1 KEYWORDS DNA binding; nucleus; phosphoprotein; spermatogenesis; !1testis FEATURE !$1-54 #product spermatid transition protein 1 #status !8experimental #label MAT\ !$8,35,36,39 #binding_site phosphate (Ser) (covalent) (partial) !8#status experimental SUMMARY #length 54 #molecular-weight 6344 #checksum 4358 SEQUENCE /// ENTRY BGHU2 #type complete TITLE spermatid transition protein 2 - human ALTERNATE_NAMES TP2 ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1993 #sequence_revision 18-Oct-1996 #text_change 24-Sep-1999 ACCESSIONS A44477; A45223; I38872 REFERENCE A44477 !$#authors Schluter, G.; Kremling, H.; Engel, W. !$#journal Genomics (1992) 14:377-383 !$#title The gene for human transition protein 2: nucleotide !1sequence, assignment to the protamine gene cluster, and !1evidence for its low expression. !$#cross-references MUID:93052338; PMID:1385303 !$#accession A44477 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-138 ##label SCH !'##cross-references GB:X63759; NID:g505389; PIDN:CAA45291.1; !1PID:g505390 !'##note sequence extracted from NCBI backbone (NCBIP:117961) REFERENCE A45223 !$#authors Nelson, J.E.; Krawetz, S.A. !$#journal J. Biol. Chem. (1993) 268:2932-2936 !$#title Linkage of human spermatid-specific basic nuclear protein !1genes. Definition and evolution of the P1-->P2-->TP2 locus. !$#cross-references MUID:93155116; PMID:8428967 !$#accession A45223 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-138 ##label NEL !'##cross-references GB:L03378; NID:g292827; PIDN:AAA61203.1; !1PID:g292828 !'##experimental_source lymphocyte !'##note sequence extracted from NCBI backbone (NCBIP:124272) REFERENCE A55329 !$#authors Nelson, J.E.; Krawetz, S.A. !$#journal J. Biol. Chem. (1994) 269:31067-31073 !$#title Characterization of a human locus in transition. !$#cross-references MUID:95074145; PMID:7983046 !$#accession I38872 !'##molecule_type DNA !'##residues 1-138 ##label RES !'##cross-references EMBL:U15422; NID:g642458; PIDN:AAC50488.1; !1PID:g642461 !'##note submitted to GenBank/EMBL by S.A. Krawetz, 3 October 1994 COMMENT This protein replaces histones and is replaced by other !1transition proteins or protamines during spermatogenesis. GENETICS !$#gene GDB:TNP2 !'##cross-references GDB:125312; OMIM:190232 !$#map_position 16p13.3-16p13.3 !$#introns 134/1 CLASSIFICATION #superfamily spermatid transition protein 2 KEYWORDS DNA binding; nucleus; spermatogenesis FEATURE !$2-138 #product spermatid transition protein 2 #status !8predicted #label MAT SUMMARY #length 138 #molecular-weight 15641 #checksum 1699 SEQUENCE /// ENTRY BGPG2 #type complete TITLE spermatid transition protein 2 - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 22-Nov-1993 #sequence_revision 18-Oct-1996 #text_change 18-Oct-1996 ACCESSIONS S21671; A38886; A48385 REFERENCE S21670 !$#authors Keime, S.; Heitland, K.; Kumm, S.; Schloesser, M.; Hroch, !1N.; Holtz, W.; Engel, W. !$#journal Biol. Chem. Hoppe-Seyler (1992) 373:261-270 !$#title Characterization of four genes encoding basic proteins of !1the porcine spermatid nucleus and close linkage of three of !1them. !$#cross-references MUID:92329006; PMID:1627265 !$#accession S21671 !'##molecule_type DNA !'##residues 1-137 ##label KEI !'##cross-references EMBL:M80677; NID:g164701 REFERENCE A38886 !$#authors Keime, S. !$#submission submitted to GenBank, November 1991 !$#accession A38886 !'##status preliminary !'##molecule_type mRNA !'##residues 1-19,'TGF',22-137 ##label KEW REFERENCE A48385 !$#authors Keime, S.; Kumm, S.; Luerssen, H.; Engel, W. !$#journal Anim. Genet. (1992) 23:373-378 !$#title The nucleotide sequence of boar transition protein 2 (TNP2) !1cDNA and haploid expression of the gene during !1spermatogenesis. !$#cross-references MUID:92367962; PMID:1380212 !$#accession A48385 !'##molecule_type mRNA !'##residues 2-137 ##label KE2 !'##cross-references EMBL:X57989; GB:S42347; NID:g429146 !'##experimental_source testis !'##note sequence extracted from NCBI backbone; translation of initiator !1Met is not shown COMMENT This protein replaces histones and is replaced by other !1transition proteins or protamines during spermatogenesis. GENETICS !$#introns 133/1 CLASSIFICATION #superfamily spermatid transition protein 2 KEYWORDS DNA binding; nucleus; spermatogenesis FEATURE !$2-137 #product spermatid transition protein 2 #status !8predicted #label MAT SUMMARY #length 137 #molecular-weight 15301 #checksum 8673 SEQUENCE /// ENTRY BGBO2 #type complete TITLE spermatid transition protein 2 - bovine ALTERNATE_NAMES basic nuclear protein 2; TNP2 ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Jun-1992 #sequence_revision 18-Oct-1996 #text_change 22-Jun-1999 ACCESSIONS S16134; S36352 REFERENCE S16134 !$#authors Reinhart, N.; Kremling, H.; Luerssen, H.; Adham, I.M.; !1Engel, W. !$#journal Biol. Chem. Hoppe-Seyler (1991) 372:431-436 !$#title Characterization of a gene encoding a basic protein of the !1spermatid nucleus, TNP2, and its close linkage to the !1protamine genes in the bull. !$#cross-references MUID:92000310; PMID:1716912 !$#accession S16134 !'##molecule_type DNA !'##residues 1-131 ##label REI !'##cross-references EMBL:X56400; NID:g801; PIDN:CAA39810.1; PID:g802 !'##note translation of initiator Met is not shown !$#accession S36352 !'##molecule_type mRNA !'##residues 1-131 ##label RE2 !'##cross-references EMBL:X56401; NID:g803; PIDN:CAA39811.1; PID:g804 COMMENT This protein replaces histones and is replaced by other !1transition proteins or protamines during spermatogenesis. GENETICS !$#gene tnp2 !$#introns 127/1 CLASSIFICATION #superfamily spermatid transition protein 2 KEYWORDS DNA binding; nucleus; spermatogenesis FEATURE !$2-131 #product spermatid transition protein 2 #status !8predicted #label MAT SUMMARY #length 131 #molecular-weight 14942 #checksum 1700 SEQUENCE /// ENTRY HSSH #type complete TITLE sperm histone - sheep ALTERNATE_NAMES cysteine-rich protamine; protamine ORGANISM #formal_name Ovis orientalis aries, Ovis ammon aries #common_name domestic sheep DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 05-Sep-1997 ACCESSIONS A02658 REFERENCE A02658 !$#authors Sautiere, P.; Belaiche, D.; Martinage, A.; Loir, M. !$#journal Eur. J. Biochem. (1984) 144:121-125 !$#title Primary structure of the ram (Ovis aries) protamine. !$#cross-references MUID:85003651; PMID:6479168 !$#accession A02658 !'##molecule_type protein !'##residues 1-50 ##label SAU CLASSIFICATION #superfamily sperm histone KEYWORDS chromosomal protein; DNA binding; nucleosome core; !1spermatogenesis FEATURE !$5 #disulfide_bonds interchain (to 22) #status !8predicted\ !$6-14,39-47 #disulfide_bonds #status predicted\ !$22 #disulfide_bonds interchain (to 5) #status predicted\ !$38 #disulfide_bonds interchain #status predicted SUMMARY #length 50 #molecular-weight 6712 #checksum 2147 SEQUENCE /// ENTRY HSBOS #type complete TITLE sperm histone P1 - bovine ALTERNATE_NAMES arginine-rich protamine; cysteine-rich protamine; protamine P1; sperm basic nuclear protein ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 24-Apr-1984 #sequence_revision 30-Jun-1992 #text_change 22-Jun-1999 ACCESSIONS A29911; A26450; A26041; A24375; A61342 REFERENCE A29911 !$#authors Krawetz, S.A.; Connor, W.; Dixon, G.H. !$#journal J. Biol. Chem. (1988) 263:321-326 !$#title Bovine protamine genes contain a single intron. The !1structures of the two alleles. !$#cross-references MUID:88087109; PMID:3335501 !$#accession A29911 !'##molecule_type DNA !'##residues 1-51 ##label KRA !'##cross-references GB:M18396; NID:g163619; PIDN:AAA30735.1; !1PID:g163620 REFERENCE A26450 !$#authors Krawetz, S.A.; Connor, W.; Dixon, G.H. !$#journal DNA (1987) 6:47-57 !$#title Cloning of bovine P1 protamine cDNA and the evolution of !1vertebrate P1 protamines. !$#cross-references MUID:87161234; PMID:3829889 !$#accession A26450 !'##molecule_type mRNA !'##residues 1-51 ##label KR2 !'##cross-references GB:M14559; NID:g163632; PIDN:AAA30741.1; !1PID:g163633 REFERENCE A26041 !$#authors Lee, C.H.; Mansouri, A.; Hecht, W.; Hecht, N.B.; Engel, W. !$#journal Biol. Chem. Hoppe-Seyler (1987) 368:131-135 !$#title Nucleotide sequence of a bovine protamine cDNA. !$#cross-references MUID:87184911; PMID:2436637 !$#accession A26041 !'##molecule_type mRNA !'##residues 2-51 ##label LEE !'##cross-references GB:M18625 !'##note the codon for residue 30-Phe is shown as TCT REFERENCE A24375 !$#authors Mazrimas, J.A.; Corzett, M.; Campos, C.; Balhorn, R. !$#journal Biochim. Biophys. Acta (1986) 872:11-15 !$#title A corrected primary sequence for bull protamine. !$#cross-references MUID:86269988; PMID:3730390 !$#accession A24375 !'##molecule_type protein !'##residues 2-51 ##label MAZ REFERENCE A61342 !$#authors Coelingh, J.P.; Monfoort, C.H.; Rozijn, T.H.; Leuven, !1J.A.G.; Schiphof, R.; Steyn-Parve, E.P.; Braunitzer, G.; !1Schrank, B.; Ruhfus, A. !$#journal Biochim. Biophys. Acta (1972) 285:1-14 !$#title The complete amino acid sequence of the basic nuclear !1protein of bull spermatozoa. !$#cross-references MUID:73124384; PMID:4675900 !$#accession A61342 !'##molecule_type protein !'##residues 2-39;43-51 ##label COE REFERENCE A37137 !$#authors Balhorn, R.; Corzett, M.; Mazrimas, J.; Watkins, B. !$#journal Biochemistry (1991) 30:175-181 !$#title Identification of bull protamine disulfides. !$#cross-references MUID:91105078; PMID:1988019 !$#contents annotation: disulfide bonds GENETICS !$#introns 38/1 FUNCTION !$#description binds to and packages sperm DNA in a condensed form of !1chromatin that is transcriptionally inert CLASSIFICATION #superfamily sperm histone KEYWORDS chromosomal protein; DNA binding; nucleosome core; !1spermatogenesis FEATURE !$2-51 #product protamine P1 #status experimental #label !8MAT\ !$6 #disulfide_bonds interchain (to 23) #status !8experimental\ !$7-15,40-48 #disulfide_bonds #status experimental\ !$23 #disulfide_bonds interchain (to 6) #status !8experimental\ !$39 #disulfide_bonds interchain #status experimental SUMMARY #length 51 #molecular-weight 6758 #checksum 5466 SEQUENCE /// ENTRY HSPG #type complete TITLE sperm histone - pig ALTERNATE_NAMES cysteine-rich protamine; protamine ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 05-Sep-1997 ACCESSIONS A02659 REFERENCE A02659 !$#authors Tobita, T.; Tsutsumi, H.; Kato, A.; Suzuki, H.; Nomoto, M.; !1Nakano, M.; Ando, T. !$#journal Biochim. Biophys. Acta (1983) 744:141-146 !$#title Complete amino acid sequence of boar protamine. !$#accession A02659 !'##molecule_type protein !'##residues 1-50 ##label TOB CLASSIFICATION #superfamily sperm histone KEYWORDS chromosomal protein; DNA binding; nucleosome core; !1spermatogenesis FEATURE !$5 #disulfide_bonds interchain (to 21) #status !8predicted\ !$6-14,39-47 #disulfide_bonds #status predicted\ !$21 #disulfide_bonds interchain (to 5) #status predicted\ !$38 #disulfide_bonds interchain #status predicted SUMMARY #length 50 #molecular-weight 6584 #checksum 9934 SEQUENCE /// ENTRY HSMSS1 #type complete TITLE protamine - mouse ALTERNATE_NAMES protamine I; sperm histone P1 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 28-Feb-1986 #sequence_revision 06-Sep-1996 #text_change 22-Jun-1999 ACCESSIONS I51954; A02660; A28331; S03820 REFERENCE I51954 !$#authors Hecht, N.B. !$#journal Ann. N. Y. Acad. Sci. (1987) 513:91-101 !$#title gene expression during spermatogenesis. !$#accession I51954 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-51 ##label RES !'##cross-references GB:M27500; NID:g200502; PIDN:AAA39985.1; !1PID:g200503 REFERENCE A02660 !$#authors Kleene, K.C.; Distel, R.J.; Hecht, N.B. !$#journal Biochemistry (1985) 24:719-722 !$#title Nucleotide sequence of a cDNA clone encoding mouse protamine !11. !$#cross-references MUID:85199803; PMID:2986684 !$#accession A02660 !'##molecule_type mRNA !'##residues 2-51 ##label KLE !'##cross-references GB:K02926; NID:g200488; PIDN:AAA39980.1; !1PID:g200489 REFERENCE A28331 !$#authors Peschon, J.J.; Behringer, R.R.; Brinster, R.L.; Palmiter, !1R.D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:5316-5319 !$#title Spermatid-specific expression of protamine 1 in transgenic !1mice. !$#cross-references MUID:87260978; PMID:3037541 !$#accession A28331 !'##molecule_type DNA !'##residues 1-51 ##label PES REFERENCE S03820 !$#authors Johnson, P.A.; Peschon, J.J.; Yelick, P.C.; Palmiter, R.D.; !1Hecht, N.B. !$#journal Biochim. Biophys. Acta (1988) 950:45-53 !$#title Sequence homologies in the mouse protamine 1 and 2 genes. !$#cross-references MUID:88193085; PMID:3358932 !$#accession S03820 !'##molecule_type DNA !'##residues 1-51 ##label JOH !'##cross-references EMBL:X07625; NID:g53788; PIDN:CAA30472.1; !1PID:g53789 COMMENT The protamines of placental mammals differ from those of !1fish and birds in having cysteine residues, some of which !1are involved in disulfide bonds. GENETICS !$#map_position 16 !$#introns 36/1 CLASSIFICATION #superfamily sperm histone KEYWORDS chromosomal protein; DNA binding; nucleosome core; !1spermatogenesis FEATURE !$2-51 #product sperm histone #status predicted #label MAT\ !$6 #disulfide_bonds interchain (to 22) #status !8predicted\ !$7-15,38-48 #disulfide_bonds #status predicted\ !$22 #disulfide_bonds interchain (to 6) #status predicted\ !$37 #disulfide_bonds interchain #status predicted SUMMARY #length 51 #molecular-weight 6958 #checksum 4895 SEQUENCE /// ENTRY HSHUP1 #type complete TITLE sperm histone P1 [validated] - human ALTERNATE_NAMES protamine 1 (P1) ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1987 #sequence_revision 24-Feb-1994 #text_change 08-Dec-2000 ACCESSIONS A38515; A33330; A26843; A90708; A90730; A60896; I38870; !1A02656 REFERENCE A38515 !$#authors Domenjoud, L.; Nussbaum, G.; Adham, I.M.; Greeske, G.; !1Engel, W. !$#journal Genomics (1990) 8:127-133 !$#title Genomic sequences of human protamines whose genes, PRM1 and !1PRM2, are clustered. !$#cross-references MUID:91184796; PMID:2081589 !$#accession A38515 !'##molecule_type DNA !'##residues 1-51 ##label DOM !'##cross-references GB:M60331; NID:g190453; PIDN:AAA63249.1; !1PID:g190454 !'##note translation of initiator Met is not shown REFERENCE A33330 !$#authors Krawetz, S.A.; Herfort, M.H.; Hamerton, J.L.; Pon, R.T.; !1Dixon, G.H. !$#journal Genomics (1989) 5:639-645 !$#title Chromosomal localization and structure of the human P1 !1protamine gene. !$#cross-references MUID:90129065; PMID:2613245 !$#accession A33330 !'##molecule_type DNA !'##residues 1-51 ##label KRA !'##cross-references GB:M29706; NID:g190527; PIDN:AAA60191.1; !1PID:g190528 REFERENCE A26843 !$#authors Lee, C.H.; Hoyer-Fender, S.; Engel, W. !$#journal Nucleic Acids Res. (1987) 15:7639 !$#title The nucleotide sequence of a human protamine 1 cDNA. !$#cross-references MUID:88015622; PMID:3658707 !$#accession A26843 !'##molecule_type mRNA !'##residues 1-51 ##label LEE !'##cross-references GB:Y00443; NID:g35685; PIDN:CAA68499.1; PID:g35686 REFERENCE A90708 !$#authors Ammer, H.; Henschen, A.; Lee, C.H. !$#journal Biol. Chem. Hoppe-Seyler (1986) 367:515-522 !$#title Isolation and amino-acid sequence analysis of human sperm !1protamines P1 and P2. !$#cross-references MUID:86296190; PMID:3527226 !$#accession A90708 !'##molecule_type protein !'##residues 2-51 ##label AMM REFERENCE A90730 !$#authors McKay, D.J.; Renaux, B.S.; Dixon, G.H. !$#journal Biosci. Rep. (1985) 5:383-391 !$#title The amino acid sequence of human sperm proamine P1. !$#cross-references MUID:85280768; PMID:4027356 !$#accession A90730 !'##molecule_type protein !'##residues 2-51 ##label MCK REFERENCE A60896 !$#authors Imesch, E.; Hughes, G.J.; Zahnd, G.; Winston, R.; Jaton, !1J.C. !$#journal Mol. Immunol. (1988) 25:403-410 !$#title Detection of the major epitopes of human protamine P1 !1recognized by rabbit and mouse antibodies. !$#cross-references MUID:88288259; PMID:2456455 !$#accession A60896 !'##molecule_type protein !'##residues 2-51 ##label IME REFERENCE A55329 !$#authors Nelson, J.E.; Krawetz, S.A. !$#journal J. Biol. Chem. (1994) 269:31067-31073 !$#title Characterization of a human locus in transition. !$#cross-references MUID:95074145; PMID:7983046 !$#accession I38870 !'##molecule_type DNA !'##residues 1-51 ##label RES !'##cross-references EMBL:U15422; NID:g642458; PIDN:AAC50486.1; !1PID:g642459 REFERENCE A57865 !$#authors Chirat, F.; Arkhis, A.; Martinage, A.; Jaquinod, M.; !1Chevaillier, P.; Sautiere, P. !$#journal Biochim. Biophys. Acta (1993) 1203:109-114 !$#title Phosphorylation of human sperm protamines HP1 and HP2: !1identification of phosphorylation sites. !$#cross-references MUID:94032442; PMID:8218377 !$#contents annotation; phosphorylation sites GENETICS !$#gene GDB:PRM1 !'##cross-references GDB:120316; OMIM:182880 !$#map_position 16p13.3-16p13.3 !$#introns 38/1 FUNCTION !$#description binds to and packages sperm DNA in a condensed form of !1chromatin that is transcriptionally inert CLASSIFICATION #superfamily sperm histone KEYWORDS chromosomal protein; DNA binding; nucleosome core; !1phosphoprotein; spermatogenesis FEATURE !$2-51 #product sperm histone P1 #status experimental #label !8MAT\ !$6,39 #disulfide_bonds interchain #status predicted\ !$9,11 #binding_site phosphate (Ser) (covalent) (partial) !8#status experimental\ !$40-48 #disulfide_bonds #status predicted SUMMARY #length 51 #molecular-weight 6823 #checksum 5282 SEQUENCE /// ENTRY GACH #type complete TITLE protamine - chicken ALTERNATE_NAMES galline ORGANISM #formal_name Gallus gallus #common_name chicken DATE 22-Jun-1981 #sequence_revision 22-Jun-1981 #text_change 22-Jun-1999 ACCESSIONS A02662; A45936 REFERENCE A02662 !$#authors Nakano, M.; Tobita, T.; Ando, T. !$#journal Int. J. Pept. Protein Res. (1976) 8:565-578 !$#title Studies on a protamine (galline) from fowl sperm. !$#cross-references MUID:77050757; PMID:992941 !$#accession A02662 !'##molecule_type protein !'##residues 1-65 ##label NAK !'##experimental_source rooster sperm REFERENCE A45936 !$#authors Oliva, R.; Mezquita, J.; Mezquita, C.; Dixon, G.H. !$#journal Dev. Biol. (1988) 125:332-340 !$#title Haploid expression of the rooster protamine mRNA in the !1postmeiotic stages of spermatogenesis. !$#cross-references MUID:88112514; PMID:2892748 !$#accession A45936 !'##status preliminary !'##molecule_type mRNA !'##residues 53-65 ##label OLI !'##cross-references GB:M19078; NID:g212618; PIDN:AAA49049.1; !1PID:g212619 !'##experimental_source rooster sperm, Hubbart White Mountain breed CLASSIFICATION #superfamily sperm histone KEYWORDS chromosomal protein; DNA binding; nucleosome core; !1phosphoprotein; spermatogenesis SUMMARY #length 65 #molecular-weight 8443 #checksum 6420 SEQUENCE /// ENTRY HSHUP2 #type complete TITLE sperm histone P2 precursor [validated] - human ALTERNATE_NAMES proprotamine; protamine 2 (P2); protamine 3 (P3) CONTAINS intermediate nuclear basic protein PI1; intermediate nuclear basic protein PI2; intermediate nuclear basic protein PS1; intermediate nuclear basic protein PS2; sperm histone P2; sperm histone P3; sperm histone P4 ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1987 #sequence_revision 12-Apr-1996 #text_change 08-Dec-2000 ACCESSIONS B38515; I38871; A02661; A25395; B25395; S10801; S17219; !1S01953; S02056; A29222; S33299 REFERENCE A38515 !$#authors Domenjoud, L.; Nussbaum, G.; Adham, I.M.; Greeske, G.; !1Engel, W. !$#journal Genomics (1990) 8:127-133 !$#title Genomic sequences of human protamines whose genes, PRM1 and !1PRM2, are clustered. !$#cross-references MUID:91184796; PMID:2081589 !$#accession B38515 !'##molecule_type DNA !'##residues 1-102 ##label DOM !'##cross-references GB:M60332; NID:g190455 !'##note translation of initiator Met is not shown REFERENCE A55329 !$#authors Nelson, J.E.; Krawetz, S.A. !$#journal J. Biol. Chem. (1994) 269:31067-31073 !$#title Characterization of a human locus in transition. !$#cross-references MUID:95074145; PMID:7983046 !$#accession I38871 !'##molecule_type DNA !'##residues 1-102 ##label RES !'##cross-references EMBL:U15422; NID:g642458; PIDN:AAC50487.1; !1PID:g642460 REFERENCE A90708 !$#authors Ammer, H.; Henschen, A.; Lee, C.H. !$#journal Biol. Chem. Hoppe-Seyler (1986) 367:515-522 !$#title Isolation and amino-acid sequence analysis of human sperm !1protamines P1 and P2. !$#cross-references MUID:86296190; PMID:3527226 !$#accession A02661 !'##molecule_type protein !'##residues 46-102 ##label THE !'##note form designated P2'; form designated P2'' lacked the 3 !1amino-terminal residues REFERENCE A91168 !$#authors McKay, D.J.; Renaux, B.S.; Dixon, G.H. !$#journal Eur. J. Biochem. (1986) 156:5-8 !$#title Human sperm protamines. Amino-acid sequences of two forms of !1protamine P2. !$#cross-references MUID:86164351; PMID:3956509 !$#accession A25395 !'##molecule_type protein !'##residues 46-102 ##label MCK !'##note form P2a !$#accession B25395 !'##molecule_type protein !'##residues 49-102 ##label MC2 !'##note form P2b REFERENCE S10801 !$#authors Martinage, A.; Arkhis, A.; Alimi, E.; Sautiere, P.; !1Chevaillier, P. !$#journal Eur. J. Biochem. (1990) 191:449-451 !$#title Molecular characterization of nuclear basic protein HPI1, a !1putative precursor of human sperm protamines HP2 and HP3. !$#cross-references MUID:90345953; PMID:2384091 !$#accession S10801 !'##molecule_type protein !'##residues 2-102 ##label MAR REFERENCE S17219 !$#authors Arkhis, A.; Martinage, A.; Sautiere, P.; Chevaillier, P. !$#journal Eur. J. Biochem. (1991) 200:387-392 !$#title Molecular structure of human protamine P4 (HP4), a minor !1basic protein of human sperm nuclei. !$#cross-references MUID:91364687; PMID:1889406 !$#accession S17219 !'##molecule_type protein !'##residues 45-102 ##label ARK !'##note minor form designated protamine P4 REFERENCE S01953 !$#authors Domenjoud, L.; Fronia, C.; Uhde, F.; Engel, W. !$#journal Nucleic Acids Res. (1988) 16:7733 !$#title Sequence of human protamine 2 cDNA. !$#cross-references MUID:88319971; PMID:3412906 !$#accession S01953 !'##molecule_type mRNA !'##residues 1-37,'RM',40-102 ##label DO2 !'##cross-references EMBL:X07862 !'##note translation of initiator Met is not shown REFERENCE S02056 !$#authors Domenjoud, L. !$#submission submitted to the EMBL Data Library, June 1988 !$#accession S02056 !'##molecule_type mRNA !'##residues 1-37,'RM',40-51,'Q',53-102 ##label DO3 REFERENCE A29222 !$#authors Sautiere, P.; Martinage, A.; Belaiche, D.; Arkhis, A.; !1Chevaillier, P. !$#journal J. Biol. Chem. (1988) 263:11059-11062 !$#title Comparison of the amino acid sequences of human protamines !1HP2 and HP3 and of intermediate basic nuclear proteins HPS1 !1and HPS2. Structural evidence that HPS1 and HPS2 are !1pro-protamines. !$#cross-references MUID:88298740; PMID:3403514 !$#accession A29222 !'##molecule_type protein !'##residues 'E',35-63 ##label SAU REFERENCE S33299 !$#authors Alimi, E.; Martinage, A.; Arkhis, A.; Belaiche, D.; !1Sautiere, P.; Chevaillier, P. !$#journal Eur. J. Biochem. (1993) 214:445-450 !$#title Amino acid sequence of the human intermediate basic protein !12 (HPI2) from sperm nuclei. Structural relationship with !1protamine P2. !$#cross-references MUID:93292505; PMID:8513794 !$#accession S33299 !'##molecule_type protein !'##residues 22-46 ##label ALI REFERENCE A57865 !$#authors Chirat, F.; Arkhis, A.; Martinage, A.; Jaquinod, M.; !1Chevaillier, P.; Sautiere, P. !$#journal Biochim. Biophys. Acta (1993) 1203:109-114 !$#title Phosphorylation of human sperm protamines HP1 and HP2: !1identification of phosphorylation sites. !$#cross-references MUID:94032442; PMID:8218377 !$#contents annotation; phosphorylation site GENETICS !$#gene GDB:PRM2 !'##cross-references GDB:125271; OMIM:182890 !$#map_position 16p13.3-16p13.3 !$#introns 91/1 FUNCTION !$#description binds to and packages sperm DNA in a condensed form of !1chromatin that is transcriptionally inert CLASSIFICATION #superfamily sperm histone KEYWORDS chromosomal protein; DNA binding; nucleosome core; !1phosphoprotein; spermatogenesis FEATURE !$2-102 #product intermediate nuclear basic protein PI1 !8#status experimental #label PI1\ !$22-102 #product intermediate nuclear basic protein PI2 !8#status experimental #label PI2\ !$34-102 #product intermediate nuclear basic protein PS1 !8#status experimental #label PS1\ !$37-102 #product intermediate nuclear basic protein PS2 !8#status experimental #label PS2\ !$45-102 #product sperm histone P4 #status experimental #label !8HP4\ !$46-102 #product sperm histone P2 #status experimental #label !8HP2\ !$49-102 #product sperm histone P3 #status experimental #label !8HP3\ !$59 #binding_site phosphate (Ser) (covalent) (partial) !8#status experimental SUMMARY #length 102 #molecular-weight 13051 #checksum 9490 SEQUENCE /// ENTRY TYTUY2 #type complete TITLE protamine Y2 - bluefin tuna ALTERNATE_NAMES thynnin ORGANISM #formal_name Thunnus thynnus #common_name bluefin tuna DATE 12-Aug-1981 #sequence_revision 12-Aug-1981 #text_change 16-Feb-1997 ACCESSIONS A02663; A91652 REFERENCE A91655 !$#authors Bretzel, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1972) 353:933-943 !$#title Ueber Thynnin, das Protamin des Thunfisches. !$#cross-references MUID:72259987; PMID:4559647 !$#accession A02663 !'##molecule_type protein !'##residues 1-34 ##label BRE CLASSIFICATION #superfamily protamine Y2 KEYWORDS chromosomal protein; DNA binding; spermatogenesis SUMMARY #length 34 #molecular-weight 4569 #checksum 8347 SEQUENCE /// ENTRY TYTUZ1 #type complete TITLE protamine Z1 - bluefin tuna ALTERNATE_NAMES thynnin ORGANISM #formal_name Thunnus thynnus #common_name bluefin tuna DATE 12-Aug-1981 #sequence_revision 12-Aug-1981 #text_change 16-Feb-1997 ACCESSIONS A91656; A02664 REFERENCE A91656 !$#authors Bretzel, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1973) 354:312-320 !$#title Ueber Thynnin, das Protamin des Thunfisches. !$#cross-references MUID:75039952; PMID:4803475 !$#accession A91656 !'##molecule_type protein !'##residues 1-34 ##label BRE CLASSIFICATION #superfamily protamine Y2 KEYWORDS chromosomal protein; DNA binding; spermatogenesis; testis SUMMARY #length 34 #molecular-weight 4641 #checksum 8941 SEQUENCE /// ENTRY TYTUZ2 #type complete TITLE protamine Z2 - bluefin tuna ALTERNATE_NAMES thynnin ORGANISM #formal_name Thunnus thynnus #common_name bluefin tuna DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Feb-1997 ACCESSIONS A91657; A02664 REFERENCE A91657 !$#authors Bretzel, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1973) 354:543-549 !$#title Ueber Thynnin, das Protamin des Thunfisches. !$#cross-references MUID:75039979; PMID:4609881 !$#accession A91657 !'##molecule_type protein !'##residues 1-34 ##label BRE CLASSIFICATION #superfamily protamine Y2 KEYWORDS chromosomal protein; DNA binding; spermatogenesis; testis SUMMARY #length 34 #molecular-weight 4613 #checksum 8479 SEQUENCE /// ENTRY SRAPC #type complete TITLE protamine B - Russian sturgeon ALTERNATE_NAMES sturine ORGANISM #formal_name Acipenser gueldenstaedti #common_name Russian sturgeon DATE 12-Aug-1981 #sequence_revision 12-Aug-1981 #text_change 16-Feb-1997 ACCESSIONS A02665 REFERENCE A02665 !$#authors Yulikova, E.P.; Evseenko, L.K.; Baratova, L.A.; Belyanova, !1L.P.; Rybin, V.K.; Silaev, A.B. !$#journal Bioorg. Khim. (1976) 2:1613-1617 !$#accession A02665 !'##molecule_type protein !'##residues 1-27 ##label YUL CLASSIFICATION #superfamily protamine Y2 KEYWORDS chromosomal protein; DNA binding; spermatogenesis SUMMARY #length 27 #molecular-weight 3707 #checksum 278 SEQUENCE /// ENTRY S28546 #type complete TITLE protamine 1 - Japanese toad ORGANISM #formal_name Bufo japonicus #common_name Japanese toad DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 22-Jun-1999 ACCESSIONS S28546; S14102; JU0323 REFERENCE S14102 !$#authors Takamune, K.; Nishida, H.; Takai, M.; Katagiri, C. !$#journal Eur. J. Biochem. (1991) 196:401-406 !$#title Primary structure of toad sperm protamines and nucleotide !1sequence of their cDNAs. !$#cross-references MUID:91177013; PMID:2007404 !$#accession S28546 !'##molecule_type protein !'##residues 1-39 ##label TAK1 !$#accession S14102 !'##molecule_type mRNA !'##residues 6-39 ##label TAK2 !'##cross-references EMBL:X56529; NID:g62469; PIDN:CAA39876.1; !1PID:g62470 REFERENCE JU0323 !$#authors Takamune, K.; Nishida, H.; Takai, M.; Katagiri, C. !$#submission submitted to the Protein Sequence Database, February 1990 !$#accession JU0323 !'##molecule_type protein !'##residues 1-39 ##label TAK3 CLASSIFICATION #superfamily protamine Y2 KEYWORDS chromosomal protein; DNA binding; spermatogenesis; testis SUMMARY #length 39 #molecular-weight 5091 #checksum 1887 SEQUENCE /// ENTRY S14717 #type complete TITLE protamine 2 - Japanese toad ORGANISM #formal_name Bufo japonicus #common_name Japanese toad DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 22-Jun-1999 ACCESSIONS S14717; S28547; JU0324 REFERENCE S14102 !$#authors Takamune, K.; Nishida, H.; Takai, M.; Katagiri, C. !$#journal Eur. J. Biochem. (1991) 196:401-406 !$#title Primary structure of toad sperm protamines and nucleotide !1sequence of their cDNAs. !$#cross-references MUID:91177013; PMID:2007404 !$#accession S14717 !'##molecule_type mRNA !'##residues 1-40 ##label TAK1 !'##cross-references EMBL:X56530; NID:g62471; PIDN:CAA39877.1; !1PID:g62472 !$#accession S28547 !'##molecule_type protein !'##residues 2-40 ##label TAK2 REFERENCE JU0323 !$#authors Takamune, K.; Nishida, H.; Takai, M.; Katagiri, C. !$#submission submitted to the Protein Sequence Database, February 1990 !$#accession JU0324 !'##molecule_type mRNA !'##residues 1-40 ##label TAK3 CLASSIFICATION #superfamily protamine Y2 KEYWORDS chromosomal protein; DNA binding; phosphoprotein; !1spermatogenesis; testis FEATURE !$2-40 #product protamine 2 #status experimental #label MAT SUMMARY #length 40 #molecular-weight 5236 #checksum 5103 SEQUENCE /// ENTRY SRAPAS #type complete TITLE protamine A - stellate sturgeon ALTERNATE_NAMES stellin ORGANISM #formal_name Acipenser stellatus #common_name stellate sturgeon DATE 28-Feb-1980 #sequence_revision 12-Aug-1981 #text_change 16-Feb-1997 ACCESSIONS A02666 REFERENCE A02666 !$#authors Yulikova, E.P.; Rybin, V.K.; Silaev, A.B. !$#journal Bioorg. Khim. (1979) 5:5-10 !$#title The primary structure of stellin A. !$#accession A02666 !'##molecule_type protein !'##residues 1-27 ##label YUL !'##note article in Russian with English abstract CLASSIFICATION #superfamily protamine Y2 KEYWORDS chromosomal protein; DNA binding; spermatogenesis SUMMARY #length 27 #molecular-weight 3532 #checksum 9357 SEQUENCE /// ENTRY YZPK1 #type complete TITLE protamine I - northern pike ORGANISM #formal_name Esox lucius #common_name northern pike DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 16-Feb-1997 ACCESSIONS A02667 REFERENCE A02667 !$#authors Speckert, W.; Kennedy, B.; Daisley, S.L.; Davies, P. !$#journal Eur. J. Biochem. (1983) 136:283-289 !$#title Primary structure of protamine from the northern pike Esox !1lucius. !$#cross-references MUID:84028647; PMID:6628381 !$#accession A02667 !'##molecule_type protein !'##residues 1-32 ##label SPE !'##note 9-Ser was also found. 28-Ser was found in 50% of the molecules; !1this heterogeneity indicates the existence of other !1protamines CLASSIFICATION #superfamily protamine Y2 KEYWORDS chromosomal protein; DNA binding; spermatogenesis SUMMARY #length 32 #molecular-weight 4139 #checksum 2281 SEQUENCE /// ENTRY IRTR1B #type complete TITLE protamine IB - rainbow trout ALTERNATE_NAMES iridine ORGANISM #formal_name Oncorhynchus mykiss #common_name rainbow trout DATE 12-Aug-1981 #sequence_revision 12-Aug-1981 #text_change 16-Feb-1997 ACCESSIONS A02668 REFERENCE A91774 !$#authors Ando, T.; Watanabe, S. !$#journal Int. J. Protein Res. (1969) 1:221-224 !$#title A new method for fractionation of protamines and the amino !1acid sequences of salmine and three components of iridine. !$#cross-references MUID:72030546; PMID:4953052 !$#accession A02668 !'##molecule_type protein !'##residues 1-33 ##label AND CLASSIFICATION #superfamily protamine Y2 KEYWORDS chromosomal protein; DNA binding; spermatogenesis SUMMARY #length 33 #molecular-weight 4420 #checksum 5329 SEQUENCE /// ENTRY SLONA1 #type complete TITLE protamine AI - chum salmon ALTERNATE_NAMES salmine AI ORGANISM #formal_name Oncorhynchus keta #common_name chum salmon DATE 12-Aug-1981 #sequence_revision 12-Aug-1981 #text_change 16-Feb-1997 ACCESSIONS A02669 REFERENCE A91774 !$#authors Ando, T.; Watanabe, S. !$#journal Int. J. Protein Res. (1969) 1:221-224 !$#title A new method for fractionation of protamines and the amino !1acid sequences of salmine and three components of iridine. !$#cross-references MUID:72030546; PMID:4953052 !$#accession A02669 !'##molecule_type protein !'##residues 1-32 ##label AND CLASSIFICATION #superfamily protamine Y2 KEYWORDS chromosomal protein; DNA binding; spermatogenesis; testis SUMMARY #length 32 #molecular-weight 4250 #checksum 2796 SEQUENCE /// ENTRY IRTR1A #type complete TITLE protamine IA - rainbow trout ALTERNATE_NAMES iridine ORGANISM #formal_name Oncorhynchus mykiss #common_name rainbow trout DATE 12-Aug-1981 #sequence_revision 12-Aug-1981 #text_change 16-Feb-1997 ACCESSIONS A02670 REFERENCE A91774 !$#authors Ando, T.; Watanabe, S. !$#journal Int. J. Protein Res. (1969) 1:221-224 !$#title A new method for fractionation of protamines and the amino !1acid sequences of salmine and three components of iridine. !$#cross-references MUID:72030546; PMID:4953052 !$#accession A02670 !'##molecule_type protein !'##residues 1-33 ##label AND CLASSIFICATION #superfamily protamine Y2 KEYWORDS chromosomal protein; DNA binding; spermatogenesis SUMMARY #length 33 #molecular-weight 4406 #checksum 5485 SEQUENCE /// ENTRY IRTR59 #type complete TITLE protamine CII - rainbow trout ALTERNATE_NAMES protamine 2b ORGANISM #formal_name Oncorhynchus mykiss #common_name rainbow trout DATE 18-Aug-1982 #sequence_revision 10-Nov-1995 #text_change 22-Jun-1999 ACCESSIONS A27776; A93210; D24970; B93723; C93723; A02671 REFERENCE A93435 !$#authors States, J.C.; Connor, W.; Wosnick, M.A.; Aiken, J.M.; !1Gedamu, L.; Dixon, G.H. !$#journal Nucleic Acids Res. (1982) 10:4551-4563 !$#title Nucleotide sequence of a protamine component CII gene of !1Salmo gairdnerii. !$#cross-references MUID:83038616; PMID:6290986 !$#accession A27776 !'##molecule_type DNA !'##residues 1-33 ##label STA REFERENCE A93210 !$#authors Jenkins, J.R. !$#journal Nature (1979) 279:809-811 !$#title Sequence divergence of rainbow trout protamine mRNAs; !1comparison of coding and non-coding nucleotide sequences in !1three protamine cDNA plasmids. !$#cross-references MUID:79199790; PMID:450133 !$#accession A93210 !'##molecule_type mRNA !'##residues 7-33 ##label JEN !'##cross-references GB:M10718; NID:g213841; PIDN:AAA49608.1; !1PID:g213842 !'##experimental_source clone pTP11 REFERENCE A91170 !$#authors McKay, D.J.; Renaux, B.S.; Dixon, G.H. !$#journal Eur. J. Biochem. (1986) 158:361-366 !$#title Rainbow trout protamines. Amino acid sequences of six !1distinct proteins from a single testis. !$#cross-references MUID:86274711; PMID:3755398 !$#accession D24970 !'##molecule_type protein !'##residues 2-33 ##label MCK REFERENCE A93723 !$#authors Gedamu, L.; Wosnick, M.A.; Connor, W.; Watson, D.C.; Dixon, !1G.H.; Iatrou, K. !$#journal Nucleic Acids Res. (1981) 9:1463-1482 !$#title Molecular analysis of the protamine multi-gene family in !1rainbow trout testis. !$#cross-references MUID:81198983; PMID:6262730 !$#accession B93723 !'##molecule_type protein !'##residues 2-33 ##label GED !'##experimental_source clone pRTP59 !$#accession C93723 !'##molecule_type mRNA !'##residues 7-33 ##label GE2 COMMENT The partial protein sequences translated from mRNA clones !1pRTP59 and pTP11 are identical with that of CII; the partial !1mRNA sequences of pRTP59 and pTP11 are identical in the !1protein coding regions but not in the 3' noncoding regions. GENETICS !$#introns #status absent CLASSIFICATION #superfamily protamine Y2 KEYWORDS chromosomal protein; DNA binding; spermatogenesis FEATURE !$2-33 #product protamine CII #status experimental #label !8MAT SUMMARY #length 33 #molecular-weight 4381 #checksum 5481 SEQUENCE /// ENTRY IRTR42 #type complete TITLE protamine 2c - rainbow trout ORGANISM #formal_name Oncorhynchus mykiss #common_name rainbow trout DATE 18-Aug-1982 #sequence_revision 12-Apr-1996 #text_change 24-Sep-1999 ACCESSIONS B21211; D93723; B93210; E24970; A02676 REFERENCE A21211 !$#authors Aiken, J.M.; McKenzie, D.; Zhao, H.Z.; States, J.C.; Dixon, !1G.H. !$#journal Nucleic Acids Res. (1983) 11:4907-4922 !$#title Sequence homologies in the protamine gene family of rainbow !1trout. !$#cross-references MUID:83272939; PMID:6308564 !$#accession B21211 !'##molecule_type DNA !'##residues 1-33 ##label AIK !'##cross-references EMBL:X01596; NID:g64336; PIDN:CAA25749.1; !1PID:g64337 !'##experimental_source clone TP15 REFERENCE A93723 !$#authors Gedamu, L.; Wosnick, M.A.; Connor, W.; Watson, D.C.; Dixon, !1G.H.; Iatrou, K. !$#journal Nucleic Acids Res. (1981) 9:1463-1482 !$#title Molecular analysis of the protamine multi-gene family in !1rainbow trout testis. !$#cross-references MUID:81198983; PMID:6262730 !$#accession D93723 !'##molecule_type mRNA !'##residues 7-33 ##label GED !'##experimental_source clone pRTP242 REFERENCE A93210 !$#authors Jenkins, J.R. !$#journal Nature (1979) 279:809-811 !$#title Sequence divergence of rainbow trout protamine mRNAs; !1comparison of coding and non-coding nucleotide sequences in !1three protamine cDNA plasmids. !$#cross-references MUID:79199790; PMID:450133 !$#accession B93210 !'##molecule_type mRNA !'##residues 7-33 ##label JEN !'##cross-references GB:X02924; GB:M10717; NID:g64344; PIDN:CAA26680.1; !1PID:g64345 !'##experimental_source clone pTP8 REFERENCE A91170 !$#authors McKay, D.J.; Renaux, B.S.; Dixon, G.H. !$#journal Eur. J. Biochem. (1986) 158:361-366 !$#title Rainbow trout protamines. Amino acid sequences of six !1distinct proteins from a single testis. !$#cross-references MUID:86274711; PMID:3755398 !$#accession E24970 !'##molecule_type protein !'##residues 2-33 ##label MCK CLASSIFICATION #superfamily protamine Y2 KEYWORDS chromosomal protein; DNA binding; spermatogenesis FEATURE !$2-33 #product protamine 2c #status experimental #label MAT SUMMARY #length 33 #molecular-weight 4450 #checksum 5472 SEQUENCE /// ENTRY IRTR2 #type complete TITLE protamine II - rainbow trout ALTERNATE_NAMES iridine ORGANISM #formal_name Oncorhynchus mykiss #common_name rainbow trout DATE 12-Aug-1981 #sequence_revision 12-Aug-1981 #text_change 16-Feb-1997 ACCESSIONS A02672 REFERENCE A91774 !$#authors Ando, T.; Watanabe, S. !$#journal Int. J. Protein Res. (1969) 1:221-224 !$#title A new method for fractionation of protamines and the amino !1acid sequences of salmine and three components of iridine. !$#cross-references MUID:72030546; PMID:4953052 !$#accession A02672 !'##molecule_type protein !'##residues 1-32 ##label AND CLASSIFICATION #superfamily protamine Y2 KEYWORDS chromosomal protein; DNA binding SUMMARY #length 32 #molecular-weight 4224 #checksum 2558 SEQUENCE /// ENTRY IRTRC3 #type complete TITLE protamine CIII, major component - rainbow trout ORGANISM #formal_name Oncorhynchus mykiss #common_name rainbow trout DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 16-Feb-1997 ACCESSIONS A02673 REFERENCE A93723 !$#authors Gedamu, L.; Wosnick, M.A.; Connor, W.; Watson, D.C.; Dixon, !1G.H.; Iatrou, K. !$#journal Nucleic Acids Res. (1981) 9:1463-1482 !$#title Molecular analysis of the protamine multi-gene family in !1rainbow trout testis. !$#cross-references MUID:81198983; PMID:6262730 !$#accession A02673 !'##molecule_type protein !'##residues 1-30 ##label THE CLASSIFICATION #superfamily protamine Y2 KEYWORDS chromosomal protein; DNA binding; spermatogenesis SUMMARY #length 30 #molecular-weight 3991 #checksum 7553 SEQUENCE /// ENTRY IRTRC2 #type complete TITLE protamine 1a - rainbow trout ALTERNATE_NAMES protamine CIII, minor component 2 ORGANISM #formal_name Oncorhynchus mykiss #common_name rainbow trout DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 22-Jun-1999 ACCESSIONS B02673; A24970; A27251; A02673 REFERENCE A93723 !$#authors Gedamu, L.; Wosnick, M.A.; Connor, W.; Watson, D.C.; Dixon, !1G.H.; Iatrou, K. !$#journal Nucleic Acids Res. (1981) 9:1463-1482 !$#title Molecular analysis of the protamine multi-gene family in !1rainbow trout testis. !$#cross-references MUID:81198983; PMID:6262730 !$#accession B02673 !'##molecule_type mRNA !'##residues 1-30 ##label THE REFERENCE A91170 !$#authors McKay, D.J.; Renaux, B.S.; Dixon, G.H. !$#journal Eur. J. Biochem. (1986) 158:361-366 !$#title Rainbow trout protamines. Amino acid sequences of six !1distinct proteins from a single testis. !$#cross-references MUID:86274711; PMID:3755398 !$#accession A24970 !'##molecule_type protein !'##residues 1-30 ##label MCK REFERENCE A27251 !$#authors Sakai, M.; Fujii-Kuriyama, Y.; Saito, T.; Muramatsu, M. !$#journal J. Biochem. (1981) 89:1863-1868 !$#title Closely related mRNA sequences of protamines in rainbow !1trout testis. !$#cross-references MUID:82030654; PMID:7287661 !$#accession A27251 !'##molecule_type mRNA !'##residues 1-30 ##label SAK !'##cross-references GB:K03052; NID:g213839; PIDN:AAA49607.1; !1PID:g213840 !'##note authors suggest silent nucleotide differences between clones !1pPc66 and pPc2e represent different genes rather than !1different alleles CLASSIFICATION #superfamily protamine Y2 KEYWORDS chromosomal protein; DNA binding; spermatogenesis; testis SUMMARY #length 30 #molecular-weight 4050 #checksum 7571 SEQUENCE /// ENTRY IRTR78 #type complete TITLE protamine CIII, minor component 1 - rainbow trout ALTERNATE_NAMES protamine 1b ORGANISM #formal_name Oncorhynchus mykiss #common_name rainbow trout DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 16-Feb-1997 ACCESSIONS A93723; B24970; A02674 REFERENCE A93723 !$#authors Gedamu, L.; Wosnick, M.A.; Connor, W.; Watson, D.C.; Dixon, !1G.H.; Iatrou, K. !$#journal Nucleic Acids Res. (1981) 9:1463-1482 !$#title Molecular analysis of the protamine multi-gene family in !1rainbow trout testis. !$#cross-references MUID:81198983; PMID:6262730 !$#accession A93723 !'##molecule_type mRNA !'##residues 1-30 ##label GED !'##experimental_source clones pRTP178 and pRTP94 !'##note the partial protein sequence (residues 6-30) of pRTP94 is !1identical with that of pRTP178; the partial mRNA sequence of !1pRTP94 differs at two positions, only one of which is in the !1protein coding region REFERENCE A91170 !$#authors McKay, D.J.; Renaux, B.S.; Dixon, G.H. !$#journal Eur. J. Biochem. (1986) 158:361-366 !$#title Rainbow trout protamines. Amino acid sequences of six !1distinct proteins from a single testis. !$#cross-references MUID:86274711; PMID:3755398 !$#accession B24970 !'##molecule_type protein !'##residues 1-30 ##label MCK CLASSIFICATION #superfamily protamine Y2 KEYWORDS chromosomal protein; DNA binding; spermatogenesis SUMMARY #length 30 #molecular-weight 4064 #checksum 7441 SEQUENCE /// ENTRY IRTR4 #type complete TITLE protamine pTP4 - rainbow trout ORGANISM #formal_name Oncorhynchus mykiss #common_name rainbow trout DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 28-May-1999 ACCESSIONS A02675 REFERENCE A93210 !$#authors Jenkins, J.R. !$#journal Nature (1979) 279:809-811 !$#title Sequence divergence of rainbow trout protamine mRNAs; !1comparison of coding and non-coding nucleotide sequences in !1three protamine cDNA plasmids. !$#cross-references MUID:79199790; PMID:450133 !$#accession A02675 !'##molecule_type mRNA !'##residues 1-30 ##label JEN !'##cross-references GB:X01204; GB:M10716; NID:g64346; PIDN:CAA25623.1; !1PID:g64347 !'##experimental_source clone pTP4 CLASSIFICATION #superfamily protamine Y2 KEYWORDS chromosomal protein; DNA binding; spermatogenesis SUMMARY #length 30 #molecular-weight 4064 #checksum 7463 SEQUENCE /// ENTRY CLHRY2 #type complete TITLE protamine YII - Pacific herring ALTERNATE_NAMES clupeine ORGANISM #formal_name Clupea pallasii, Clupea harengus pallasi #common_name Pacific herring DATE 12-Aug-1981 #sequence_revision 12-Aug-1981 #text_change 16-Feb-1997 ACCESSIONS A38052; A02677 REFERENCE A38052 !$#authors Suzuki, K.; Ando, T. !$#journal J. Biochem. (1972) 72:1419-1432 !$#title Studies on protamines. XVI. The complete amino acid sequence !1of clupeine YII. !$#cross-references MUID:73223106; PMID:4664740 !$#accession A38052 !'##molecule_type protein !'##residues 1-30 ##label SUZ CLASSIFICATION #superfamily protamine Y2 KEYWORDS chromosomal protein; DNA binding; spermatogenesis SUMMARY #length 30 #molecular-weight 4049 #checksum 7662 SEQUENCE /// ENTRY CLHR2A #type complete TITLE protamine YII - Atlantic herring ALTERNATE_NAMES clupeine ORGANISM #formal_name Clupea harengus, Clupea harengus harengus #common_name Atlantic herring DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Feb-1997 ACCESSIONS A37575; A02677 REFERENCE A37575 !$#authors Chang, W.J.; Nukushina, M.; Ishii, S.; Nakahara, C.; Ando, !1T. !$#submission submitted to the Atlas, August 1970 !$#accession A37575 !'##molecule_type protein !'##residues 1-30 ##label CHA CLASSIFICATION #superfamily protamine Y2 KEYWORDS chromosomal protein; DNA binding; spermatogenesis SUMMARY #length 30 #molecular-weight 4049 #checksum 7662 SEQUENCE /// ENTRY CLHRZ #type complete TITLE protamine Z - Pacific herring ALTERNATE_NAMES clupeine ORGANISM #formal_name Clupea pallasii, Clupea harengus pallasi #common_name Pacific herring DATE 12-Aug-1981 #sequence_revision 12-Aug-1981 #text_change 16-Feb-1997 ACCESSIONS A38053; A02678 REFERENCE A38053 !$#authors Iwai, K.; Nakahara, C.; Ando, T. !$#journal J. Biochem. (1971) 69:493-509 !$#title Studies on protamines. XV. The complete amino acid sequence !1of the Z component of clupeine. Application of N leads to O !1acyl rearrangement and selective hydrolysis in sequence !1determination. !$#cross-references MUID:71157437; PMID:5551645 !$#accession A38053 !'##molecule_type protein !'##residues 1-31 ##label IWA COMMENT Clupeine Z is probably the result of a crossover between the !1genes for clupeines YI and YII. CLASSIFICATION #superfamily protamine Y2 KEYWORDS chromosomal protein; DNA binding; spermatogenesis SUMMARY #length 31 #molecular-weight 4165 #checksum 157 SEQUENCE /// ENTRY CLHRZA #type complete TITLE protamine Z - Atlantic herring ALTERNATE_NAMES clupeine ORGANISM #formal_name Clupea harengus, Clupea harengus harengus #common_name Atlantic herring DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Feb-1997 ACCESSIONS A37576; A02678 REFERENCE A37575 !$#authors Chang, W.J.; Nukushina, M.; Ishii, S.; Nakahara, C.; Ando, !1T. !$#submission submitted to the Atlas, August 1970 !$#accession A37576 !'##molecule_type protein !'##residues 1-31 ##label CHA COMMENT Clupeine Z is probably the result of a crossover between the !1genes for clupeines YI and YII. CLASSIFICATION #superfamily protamine Y2 KEYWORDS chromosomal protein; DNA binding; spermatogenesis SUMMARY #length 31 #molecular-weight 4165 #checksum 157 SEQUENCE /// ENTRY CLHRY1 #type complete TITLE protamine YI - Pacific herring ALTERNATE_NAMES clupeine ORGANISM #formal_name Clupea pallasii, Clupea harengus pallasi #common_name Pacific herring DATE 12-Aug-1981 #sequence_revision 12-Aug-1981 #text_change 16-Feb-1997 ACCESSIONS A38051; A02679 REFERENCE A38051 !$#authors Suzuki, K.; Ando, T. !$#journal J. Biochem. (1972) 72:1433-1446 !$#title Studies on protamines. XVII. The complete amino acid !1sequence of clupeine YI. !$#cross-references MUID:73223107; PMID:4664741 !$#accession A38051 !'##molecule_type protein !'##residues 1-31 ##label SUZ CLASSIFICATION #superfamily protamine Y2 KEYWORDS chromosomal protein; DNA binding; spermatogenesis SUMMARY #length 31 #molecular-weight 4112 #checksum 9868 SEQUENCE /// ENTRY CLHR1A #type complete TITLE protamine YI - Atlantic herring ALTERNATE_NAMES clupeine ORGANISM #formal_name Clupea harengus, Clupea harengus harengus #common_name Atlantic herring DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Feb-1997 ACCESSIONS A37577; A02679 REFERENCE A37575 !$#authors Chang, W.J.; Nukushina, M.; Ishii, S.; Nakahara, C.; Ando, !1T. !$#submission submitted to the Atlas, August 1970 !$#accession A37577 !'##molecule_type protein !'##residues 1-31 ##label CHA CLASSIFICATION #superfamily protamine Y2 KEYWORDS chromosomal protein; DNA binding; spermatogenesis SUMMARY #length 31 #molecular-weight 4112 #checksum 9868 SEQUENCE /// ENTRY WRECP1 #type complete TITLE protamine-like protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 01-Mar-2002 ACCESSIONS A90813; A90812; B64870; A02680 REFERENCE A90813 !$#authors Rossi, J.; Egan, J.; Hudson, L.; Landy, A. !$#journal Cell (1981) 26:305-314 !$#title The tyrT locus: termination and processing of a complex !1transcript. !$#cross-references MUID:82115308; PMID:7034960 !$#accession A90813 !'##molecule_type DNA !'##residues 1-33 ##label ROS !'##cross-references GB:K01197; GB:J01720; GB:K01198; GB:K01217; !1GB:K01300; GB:M10704; NID:g147971; PIDN:AAA24670.1; !1PID:g147972 REFERENCE A90812 !$#authors Altman, S.; Model, P.; Dixon, G.H.; Wosnick, M.A. !$#journal Cell (1981) 26:299-304 !$#title An Escherichia coli gene coding for a protamine-like !1protein. !$#cross-references MUID:82115307; PMID:7034959 !$#accession A90812 !'##molecule_type DNA !'##residues 1-33 ##label ALT !'##cross-references GB:K01197; GB:J01720; GB:K01198; GB:K01217; !1GB:K01300; GB:M10704; NID:g147971; PIDN:AAA24670.1; !1PID:g147972 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64870 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-33 ##label BLAT !'##cross-references GB:AE000221; GB:U00096; NID:g1787476; !1PIDN:AAC74313.1; PID:g1787482; UWGP:b1229 !'##experimental_source strain K-12, substrain MG1655 COMMENT Initiation may also begin with Met-5 (in vitro), producing a !1shorter basic peptide. GENETICS !$#gene tpr !$#map_position 27 min CLASSIFICATION #superfamily protamine-like protein SUMMARY #length 33 #molecular-weight 3947 #checksum 3229 SEQUENCE /// ENTRY JC6173 #type complete TITLE single-stranded DNA-binding protein 1 precursor, mitochondrial - African clawed frog ALTERNATE_NAMES helix-destabilizing protein; single-stranded DNA-binding protein s ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS JC6173; S22300; S20262; S01116 REFERENCE JC6172 !$#authors Champagne, A.M.; Dufresne, C.; Viney, L.; Gueride, M. !$#journal Gene (1997) 184:65-71 !$#title Cloning, sequencing and expression of the two genes encoding !1the mitochondrial single-stranded DNA-binding protein in !1Xenopus laevis. !$#cross-references MUID:97169147; PMID:9016954 !$#contents oocyte !$#accession JC6173 !'##molecule_type mRNA !'##residues 1-146 ##label CHA !'##cross-references EMBL:X83673; NID:g620127; PIDN:CAA58647.1; !1PID:g1890238 REFERENCE S22300 !$#authors Tiranti, V.; Barat-Gueride, M.; Bijl, J.; DiDonato, S.; !1Zeviani, M. !$#journal Nucleic Acids Res. (1991) 19:4291 !$#title A full-length cDNA encoding a mitochondrial DNA-specific !1single-stranded DNA binding protein from Xenopus laevis. !$#cross-references MUID:91334145; PMID:1870981 !$#accession S22300 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type mRNA !'##residues 1-146 ##label TIR !'##cross-references EMBL:X59285; NID:g64898; PIDN:CAA41976.1; !1PID:g64899 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1991 REFERENCE S20262 !$#authors Ghrir, R.; Lecaer, J.P.; Dufresne, C.; Gueride, M. !$#journal Arch. Biochem. Biophys. (1991) 291:395-400 !$#title Primary structure of the two variants of Xenopus laevis !1mtSSB, a mitochondrial DNA binding protein. !$#cross-references MUID:92061073; PMID:1952953 !$#accession S20262 !'##molecule_type protein !'##residues 18-142 ##label GHR REFERENCE S01116 !$#authors Mahoungou, C.; Ghrir, R.; Lecaer, J.P.; Mignotte, B.; !1Barat-Gueride, M. !$#journal FEBS Lett. (1988) 235:267-270 !$#title The amino-terminal sequence of the Xenopus laevis !1mitochondrial SSB is homologous to that of the Escherichia !1coli protein. !$#cross-references MUID:88296837; PMID:3042458 !$#accession S01116 !'##molecule_type protein !'##residues 18-26,'E',28-41 ##label MAH COMMENT This protein is essential for replication, repair of !1recombination. It is correlated with the replicative !1activity of the mitochondrial DNA, it is associated with the !1mitochondrial nucleoid, and it modulates the level of !1replication and transcription mediated by mitochondrial !1polymerases. COMMENT This protein binds preferentially to single-stranded DNA. GENETICS !$#gene ssb2 !$#genome nuclear !$#introns 8/3; 27/1; 74/1; 104/2; 134/1 CLASSIFICATION #superfamily single-stranded DNA-binding protein; !1single-stranded DNA-binding protein homology KEYWORDS DNA replication; mitochondrion; oocyte; single-stranded DNA !1binding; tetramer FEATURE !$1-17 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$18-146 #product single-stranded DNA-binding protein 1 !8#status predicted #label MAT\ !$44-129 #domain single-stranded DNA-binding protein homology !8#label SSD SUMMARY #length 146 #molecular-weight 16743 #checksum 3848 SEQUENCE /// ENTRY DDEC #type complete TITLE single-stranded DNA-binding protein - Escherichia coli (strain K-12) ALTERNATE_NAMES helix-destabilizing protein ORGANISM #formal_name Escherichia coli DATE 02-Apr-1982 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS B65214; B20023; A02681 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65214 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-178 ##label BLAT !'##cross-references GB:AE000479; GB:U00096; NID:g2367340; !1PIDN:AAC77029.1; PID:g1790494; UWGP:b4059 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A20023 !$#authors Chase, J.W.; Merrill, B.M.; Williams, K.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:5480-5484 !$#title F sex factor encodes a single-stranded DNA binding protein !1(SSB) with extensive sequence homology to Escherichia coli !1SSB. !$#cross-references MUID:83299995; PMID:6351061 !$#accession B20023 !'##molecule_type DNA !'##residues 1-121,'Q',122-171,'G',172-178 ##label CHA REFERENCE A02681 !$#authors Sancar, A.; Williams, K.R.; Chase, J.W.; Rupp, W.D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:4274-4278 !$#title Sequences of the ssb gene and protein. !$#cross-references MUID:82037821; PMID:6270666 !$#accession A02681 !'##molecule_type DNA !'##residues 1-133,'S',135-178 ##label SAN !'##cross-references GB:J01704; NID:g147869; PIDN:AAA24649.1; !1PID:g147870 COMMENT This protein is essential for replication of the E. coli !1chromosome and its single-stranded DNA phages. It is also !1involved in DNA recombination and repair. GENETICS !$#gene ssb !$#map_position 92 min CLASSIFICATION #superfamily bacterial single-stranded DNA-binding protein; !1single-stranded DNA-binding protein homology KEYWORDS DNA repair; DNA replication; single-stranded DNA binding FEATURE !$2-178 #product single-stranded DNA-binding protein #status !8predicted #label MAT\ !$22-100 #domain single-stranded DNA-binding protein homology !8#label SSD SUMMARY #length 178 #molecular-weight 18975 #checksum 4514 SEQUENCE /// ENTRY DDECIB #type complete TITLE single-stranded DNA-binding protein - Escherichia coli plasmid ColIb-P9 ALTERNATE_NAMES helix-destabilizing protein ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 28-May-1999 ACCESSIONS A32304 REFERENCE A32304 !$#authors Howland, C.J.; Rees, C.E.D.; Barth, P.T.; Wilkins, B.M. !$#journal J. Bacteriol. (1989) 171:2466-2473 !$#title The ssb gene of plasmid ColIb-P9. !$#cross-references MUID:89213928; PMID:2651402 !$#accession A32304 !'##molecule_type DNA !'##residues 1-175 ##label HOW !'##cross-references GB:M25505; NID:g144655; PIDN:AAA98056.1; !1PID:g144656 COMMENT The plasmid-encoded single-stranded DNA-binding proteins may !1be involved in DNA metabolism during bacterial conjugation; !1their functions are also related to the plasmid-mediated SOS !1initiation process. GENETICS !$#gene ssb !$#genome plasmid CLASSIFICATION #superfamily bacterial single-stranded DNA-binding protein; !1single-stranded DNA-binding protein homology KEYWORDS DNA repair; DNA replication; single-stranded DNA binding FEATURE !$2-174 #product helix-destabilizing protein #status !8predicted #label MAT\ !$22-99 #domain single-stranded DNA-binding protein homology !8#label SSD SUMMARY #length 175 #molecular-weight 19240 #checksum 1668 SEQUENCE /// ENTRY DDECF #type complete TITLE single-stranded DNA-binding protein - Escherichia coli plasmid F ALTERNATE_NAMES helix-destabilizing protein ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 28-May-1999 ACCESSIONS A20023 REFERENCE A20023 !$#authors Chase, J.W.; Merrill, B.M.; Williams, K.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:5480-5484 !$#title F sex factor encodes a single-stranded DNA binding protein !1(SSB) with extensive sequence homology to Escherichia coli !1SSB. !$#cross-references MUID:83299995; PMID:6351061 !$#accession A20023 !'##molecule_type DNA !'##residues 1-179 ##label CHA !'##cross-references GB:K00066; NID:g148614; PIDN:AAA83020.1; !1PID:g1107472 GENETICS !$#gene ssf !$#genome plasmid CLASSIFICATION #superfamily bacterial single-stranded DNA-binding protein; !1single-stranded DNA-binding protein homology KEYWORDS DNA repair; DNA replication; single-stranded DNA binding FEATURE !$2-179 #product helix-destabilizing protein #status !8predicted #label MAT\ !$22-99 #domain single-stranded DNA-binding protein homology !8#label SSD SUMMARY #length 179 #molecular-weight 19636 #checksum 4530 SEQUENCE /// ENTRY DDRT #type complete TITLE helix-destabilizing protein - rat ALTERNATE_NAMES single-stranded DNA-binding protein ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 13-Jun-1997 ACCESSIONS A02682 REFERENCE A02682 !$#authors Cobianchi, F.; SenGupta, D.N.; Zmudzka, B.Z.; Wilson, S.H. !$#journal J. Biol. Chem. (1986) 261:3536-3543 !$#title Structure of rodent helix-destabilizing protein revealed by !1cDNA cloning. !$#cross-references MUID:86140140; PMID:3005291 !$#accession A02682 !'##molecule_type mRNA !'##residues 1-320 ##label COB COMMENT This protein was isolated from the brain. CLASSIFICATION #superfamily helix-destabilizing protein; ribonucleoprotein !1repeat homology KEYWORDS acetylated amino end; brain; DNA binding; duplication; !1methylated amino acid FEATURE !$15-81 #domain ribonucleoprotein repeat homology #label !8RRM1\ !$106-172 #domain ribonucleoprotein repeat homology #label !8RRM2\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status predicted\ !$194 #modified_site omega-N,omega-N-dimethylarginine (Arg) !8#status predicted SUMMARY #length 320 #molecular-weight 34196 #checksum 7026 SEQUENCE /// ENTRY A44485 #type complete TITLE heterogeneous ribonuclear particle protein A1 - mouse ALTERNATE_NAMES helix-destabilizing protein; hnRNP core protein A1; single stranded DNA-binding protein UP1 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A44485; JC5070; JC5071 REFERENCE A44485 !$#authors Ben-David, Y.; Bani, M.R.; Chabot, B.; De Koven, A.; !1Bernstein, A. !$#journal Mol. Cell. Biol. (1992) 12:4449-4455 !$#title Retroviral insertions downstream of the heterogeneous !1nuclear ribonucleoprotein A1 gene in erythroleukemia cells: !1evidence that A1 is not essential for cell growth. !$#cross-references MUID:93024387; PMID:1406633 !$#accession A44485 !'##molecule_type mRNA !'##residues 1-320 ##label BEN !'##cross-references GB:M99167; NID:g193323; PIDN:AAA37633.1; !1PID:g193324 !'##experimental_source spleen !'##note sequence extracted from NCBI backbone (NCBIP:114165) REFERENCE JC5070 !$#authors Onishi, Y.; Kizaki, H. !$#journal Biochem. Biophys. Res. Commun. (1996) 228:7-13 !$#title Molecular cloning of the genes suppressed in RVC lymphoma !1cells by topoisomerase inhibitors. !$#cross-references MUID:97069646; PMID:8912629 !$#accession JC5070 !'##molecule_type mRNA !'##residues 1-320 ##label ONI !'##cross-references DDBJ:D86729; NID:g1711241; PIDN:BAA13162.1; !1PID:g1711242 !'##experimental_source lymphoma cell !$#accession JC5071 !'##molecule_type mRNA !'##residues 1-251,279-320 ##label ON2 !'##cross-references DDBJ:D86728 !'##experimental_source lymphoma cell COMMENT This protein inhibits the activity of the SF2/SAF factor in !1regulating the splicing of selected transcripts. CLASSIFICATION #superfamily helix-destabilizing protein; ribonucleoprotein !1repeat homology KEYWORDS acetylated amino end; alternative splicing; DNA binding; !1duplication; methylated amino acid FEATURE !$15-81 #domain ribonucleoprotein repeat homology #label !8RRM1\ !$106-172 #domain ribonucleoprotein repeat homology #label !8RRM2\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status predicted\ !$194 #modified_site omega-N,omega-N-dimethylarginine (Arg) !8#status predicted SUMMARY #length 320 #molecular-weight 34196 #checksum 7026 SEQUENCE /// ENTRY S22315 #type complete TITLE snRNP-associated protein P11 - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES heterogeneous ribonuclear particle (hnRNP) protein A1 homolog; hnRNP protein Hrb87F ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S22315; S65539; S13731 REFERENCE S22315 !$#authors Hovemann, B.T.; Dessen, E.; Mechler, H.; Mack, E. !$#journal Nucleic Acids Res. (1991) 19:4909-4914 !$#title Drosophila snRNP associated protein P11 which specifically !1binds to heat shock puff 93D reveals strong homology with !1hnRNP core protein A1. !$#cross-references MUID:92020124; PMID:1717937 !$#accession S22315 !'##molecule_type DNA !'##residues 1-386 ##label HOV !'##cross-references EMBL:X59691 REFERENCE S65539 !$#authors Reiner, B. !$#submission submitted to the EMBL Data Library, August 1991 !$#accession S65539 !'##molecule_type DNA !'##residues 1-270,'T',272-386 ##label REI !'##cross-references EMBL:X59691; NID:g8317; PIDN:CAA42212.1; PID:g8318 REFERENCE S13731 !$#authors Haynes, S.R.; Johnson, D.; Raychaudhuri, G.; Beyer, A.L. !$#journal Nucleic Acids Res. (1991) 19:25-31 !$#title The Drosophila Hrb87F gene encodes a new member of the A and !1B hnRNP protein group. !$#cross-references MUID:91187645; PMID:1849257 !$#accession S13731 !'##status preliminary !'##molecule_type mRNA !'##residues 1-386 ##label HAY !'##cross-references EMBL:X54803; NID:g8093; PIDN:CAA38574.1; PID:g8094 GENETICS !$#gene FlyBase:Hrb87F !'##cross-references FlyBase:FBgn0004237 !$#introns 16/3 CLASSIFICATION #superfamily helix-destabilizing protein; ribonucleoprotein !1repeat homology FEATURE !$25-91 #domain ribonucleoprotein repeat homology #label !8RRM1\ !$116-182 #domain ribonucleoprotein repeat homology #label RRM2 SUMMARY #length 386 #molecular-weight 39557 #checksum 2689 SEQUENCE /// ENTRY S35500 #type complete TITLE heterogeneous ribonuclear particle protein homolog - Caenorhabditis elegans ALTERNATE_NAMES heterogeneous nuclear ribonucleoprotein homolog ORGANISM #formal_name Caenorhabditis elegans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-Nov-1999 ACCESSIONS S35500; T32620 REFERENCE S35500 !$#authors Iwasaki, M.; Okumura, K.; Kondo, Y.; Tanaka, T.; Igarashi, !1H. !$#journal Nucleic Acids Res. (1992) 20:4001-4007 !$#title cDNA cloning of a novel heterogeneous nuclear !1ribonucleoprotein gene homologue in Caenorhabditis elegans !1using hamster prion protein cDNA as a hybridization probe. !$#cross-references MUID:92375684; PMID:1354852 !$#accession S35500 !'##molecule_type mRNA !'##residues 1-346 ##label IWA !'##cross-references EMBL:S43152 REFERENCE Z21201 !$#authors Du, Z.; Scheet, P.; Andrews, S. !$#submission submitted to the EMBL Data Library, December 1997 !$#description The sequence of C. elegans cosmid F42A6. !$#accession T32620 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-346 ##label DUZ !'##cross-references EMBL:AF038613; PIDN:AAB92051.1; GSPDB:GN00022; !1CESP:F42A6.7 !'##experimental_source strain Bristol N2; clone F42A6 GENETICS !$#gene CESP:F42A6.7 !$#map_position 4 !$#introns 9/3; 255/1 CLASSIFICATION #superfamily helix-destabilizing protein; ribonucleoprotein !1repeat homology FEATURE !$24-90 #domain ribonucleoprotein repeat homology #label !8RRM1\ !$115-181 #domain ribonucleoprotein repeat homology #label RRM2 SUMMARY #length 346 #molecular-weight 36344 #checksum 2824 SEQUENCE /// ENTRY B41732 #type complete TITLE heterogeneous nuclear RNP protein clone pHRP40.2 - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B41732 REFERENCE A41732 !$#authors Matunis, E.L.; Matunis, M.J.; Dreyfuss, G. !$#journal J. Cell Biol. (1992) 116:257-269 !$#title Characterization of the major hnRNP proteins from Drosophila !1melanogaster. !$#cross-references MUID:92112968; PMID:1730754 !$#accession B41732 !'##status preliminary !'##molecule_type mRNA !'##residues 1-345 ##label MAT !'##cross-references GB:X62638; NID:g11039; PIDN:CAA44504.1; PID:g11040 !'##note sequence extracted from NCBI backbone (NCBIN:76632, !1NCBIP:76633) GENETICS !$#gene FlyBase:sqd !'##cross-references FlyBase:FBgn0003498 CLASSIFICATION #superfamily helix-destabilizing protein; ribonucleoprotein !1repeat homology FEATURE !$57-123 #domain ribonucleoprotein repeat homology #label !8RRM1\ !$137-203 #domain ribonucleoprotein repeat homology #label RRM2 SUMMARY #length 345 #molecular-weight 36241 #checksum 1014 SEQUENCE /// ENTRY S56750 #type complete TITLE single stranded D box binding factor 2 - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S56750 REFERENCE S56750 !$#authors Smidt, M.P.; Russchen, B.; Snippe, L.; Wijnholds, J.; Ab, G. !$#journal Nucleic Acids Res. (1995) 23:2389-2395 !$#title Cloning and characterisation of a nuclear, site specific !1ssDNA binding protein. !$#cross-references MUID:95357145; PMID:7630716 !$#accession S56750 !'##status preliminary !'##molecule_type mRNA !'##residues 1-353 ##label SMI CLASSIFICATION #superfamily helix-destabilizing protein; ribonucleoprotein !1repeat homology FEATURE !$91-157 #domain ribonucleoprotein repeat homology #label !8RRM1\ !$175-241 #domain ribonucleoprotein repeat homology #label RRM2 SUMMARY #length 353 #molecular-weight 37664 #checksum 1270 SEQUENCE /// ENTRY S66820 #type complete TITLE heterogeneous nuclear ribonucleoprotein HRP1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein O0550; protein YOL123w; RNA-binding protein HPR1 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S66820; S62104; S65751; S72019 REFERENCE S66814 !$#authors Arino, J.; Casamayor, A.; Gamo, F.J.; Gancedo, C.; Lafuente, !1M.J.; Aldea, M.; Casas, C.; Herrero, E. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S66820 !'##molecule_type DNA !'##residues 1-534 ##label ARI !'##cross-references EMBL:Z74865; NID:g1420002; PIDN:CAA99142.1; !1PID:g1420003; GSPDB:GN00015; MIPS:YOL123w !'##experimental_source strain S288C REFERENCE S62104 !$#authors Henry, M.; Borland, C.Z.; Bossie, M.; Silver, P.A. !$#submission submitted to the EMBL Data Library, October 1995 !$#description Potential RNA binding proteins in Saccharomyces cerevisiae !1identified as suppressors of temperature-sensitive mutations !1in NPL3. !$#accession S62104 !'##molecule_type DNA !'##residues 1-293,'D',295-534 ##label HEN !'##cross-references EMBL:U38535 !'##experimental_source strain S288C REFERENCE S65751 !$#authors Henry, M.; Borland, C.Z.; Bossie, M.; Silver, P.A. !$#journal Genetics (1996) 142:103-115 !$#title Potential RNA binding proteins in Saccharomyces cerevisiae !1identified as suppressors of temperature-sensitive mutations !1in NPL3. !$#cross-references MUID:96366411; PMID:8770588 !$#accession S65751 !'##molecule_type DNA !'##residues 1-293,'D',295-534 ##label HEW !'##cross-references EMBL:U38535 REFERENCE S72019 !$#authors Lafuente, M.J.; Gamo, F.J.; Gancedo, C. !$#journal Yeast (1996) 12:1041-1045 !$#title DNA sequence analysis of a 10 624 bp fragment of the left !1arm of chromosome XV from Saccharomyces cerevisiae reveals a !1RNA binding protein, a mitochondrial protein, two ribosomal !1proteins and two new open reading frames. !$#cross-references MUID:97051591; PMID:8896268 !$#accession S72019 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-534 ##label LAF !'##cross-references EMBL:X95258; NID:g1550720; PIDN:CAA64546.1; !1PID:g1550721 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1996 GENETICS !$#gene SGD:HRP1; NAB4; MIPS:YOL123w !'##cross-references MIPS:YOL123w; SGD:S0005483 !$#map_position 15L CLASSIFICATION #superfamily yeast HRP1 protein; ribonucleoprotein repeat !1homology KEYWORDS nucleus FEATURE !$160-225 #domain ribonucleoprotein repeat homology #label !8RRM1\ !$244-310 #domain ribonucleoprotein repeat homology #label RRM2 SUMMARY #length 534 #molecular-weight 59650 #checksum 8370 SEQUENCE /// ENTRY DNHUPA #type complete TITLE polyadenylate-binding protein - human ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1989 #sequence_revision 26-May-1994 #text_change 22-Jun-1999 ACCESSIONS A93668; A29268 REFERENCE A93668 !$#authors Grange, T.; Martins de Sa, C.; Oddos, J.; Pictet, R. !$#journal Nucleic Acids Res. (1987) 15:4771-4787 !$#title Human mRNA polyadenylate binding protein: evolutionary !1conservation of a nucleic acid binding motif. !$#cross-references MUID:87259960; PMID:2885805 !$#accession A93668 !'##molecule_type mRNA !'##residues 1-633 ##label GRA !'##cross-references EMBL:Y00345; NID:g35569; PIDN:CAA68428.1; !1PID:g35570 GENETICS !$#gene GDB:PABPL1; D3S3192; PAB1 !'##cross-references GDB:134733 !$#map_position 3q22-3q25 CLASSIFICATION #superfamily polyadenylate-binding protein; !1ribonucleoprotein repeat homology KEYWORDS duplication; nucleus; RNA binding FEATURE !$12-79 #domain ribonucleoprotein repeat homology #label !8RRM1\ !$13-18 #region RNA-binding RNP2 motif\ !$52-59 #region RNA-binding RNP1 motif\ !$100-165 #domain ribonucleoprotein repeat homology #label !8RRM2\ !$101-106 #region RNA-binding RNP2 motif\ !$138-145 #region RNA-binding RNP1 motif\ !$192-255 #domain ribonucleoprotein repeat homology #label !8RRM3\ !$193-198 #region RNA-binding RNP2 motif\ !$228-235 #region RNA-binding RNP1 motif\ !$292-357 #domain ribonucleoprotein repeat homology #label !8RRM4\ !$293-298 #region RNA-binding RNP2 motif\ !$330-337 #region RNA-binding RNP1 motif SUMMARY #length 633 #molecular-weight 70324 #checksum 6684 SEQUENCE /// ENTRY DNXLPA #type complete TITLE polyadenylate-binding protein - African clawed frog ALTERNATE_NAMES poly(A)-binding protein ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 27-Feb-1990 #sequence_revision 26-May-1994 #text_change 22-Jun-1999 ACCESSIONS A32323; S12000 REFERENCE A32323 !$#authors Zelus, B.D.; Giebelhaus, D.H.; Eib, D.W.; Kenner, K.A.; !1Moon, R.T. !$#journal Mol. Cell. Biol. (1989) 9:2756-2760 !$#title Expression of the poly(A)-binding protein during development !1of Xenopus laevis. !$#cross-references MUID:89343997; PMID:2761544 !$#accession A32323 !'##molecule_type mRNA !'##residues 1-633 ##label ZEL !'##cross-references GB:M27072; NID:g623597; PIDN:AAA60936.1; !1PID:g623598 !'##note the authors translated the codon AAT for residue 197 as Phe, !1TTT for residue for residue 198 as Asn, TTT for residue 335 !1as Arg, TTT for residue 337 as Arg, ACA for residue 351 as !1Pro, and CGG for residue 563 as Pro REFERENCE S12000 !$#authors Nietfeld, W.; Mentzel, H.; Pieler, T. !$#journal EMBO J. (1990) 9:3699-3705 !$#title The Xenopus laevis poly(A) binding protein is composed of !1multiple functionally independent RNA binding domains. !$#cross-references MUID:91006071; PMID:2209558 !$#accession S12000 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-251,'N',253-283,'K',285-429,'S',431-602,'S',604-633 !1##label NIE !'##cross-references GB:X57483; NID:g64969; PIDN:CAA40721.1; PID:g64970 CLASSIFICATION #superfamily polyadenylate-binding protein; !1ribonucleoprotein repeat homology KEYWORDS duplication; nucleus; RNA binding FEATURE !$12-79 #domain ribonucleoprotein repeat homology #label !8RRM1\ !$13-18 #region RNA-binding RNP2 motif\ !$52-59 #region RNA-binding RNP1 motif\ !$100-165 #domain ribonucleoprotein repeat homology #label !8RRM2\ !$101-106 #region RNA-binding RNP2 motif\ !$138-145 #region RNA-binding RNP1 motif\ !$192-258 #domain ribonucleoprotein repeat homology #label !8RRM3\ !$193-198 #region RNA-binding RNP2 motif\ !$231-238 #region RNA-binding RNP1 motif\ !$295-360 #domain ribonucleoprotein repeat homology #label !8RRM4\ !$296-301 #region RNA-binding RNP2 motif\ !$333-340 #region RNA-binding RNP1 motif SUMMARY #length 633 #molecular-weight 70528 #checksum 7789 SEQUENCE /// ENTRY DNBYPA #type complete TITLE polyadenylate-binding protein - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES poly(A)-binding protein; protein YER165w ORGANISM #formal_name Saccharomyces cerevisiae DATE 04-Dec-1986 #sequence_revision 12-May-1995 #text_change 23-Mar-2001 ACCESSIONS A25221; S30819; A02683; S41503; S50668 REFERENCE A25221 !$#authors Adam, S.A.; Nakagawa, T.; Swanson, M.S.; Woodruff, T.K.; !1Dreyfuss, G. !$#journal Mol. Cell. Biol. (1986) 6:2932-2943 !$#title mRNA polyadenylate-binding protein: gene isolation and !1sequencing and identification of a ribonucleoprotein !1consensus sequence. !$#cross-references MUID:87064601; PMID:3537727 !$#accession A25221 !'##molecule_type DNA !'##residues 1-577 ##label ADA !'##cross-references EMBL:M13371; NID:g171966; PIDN:AAA34787.1; !1PID:g171967 REFERENCE S30812 !$#authors Mulligan, J.T.; Dietrich, F.S.; Hennessey, K.M.; Sehl, P.; !1Komp, C.; Wei, Y.; Taylor, P.; Nakahara, K.; Roberts, D.; !1Davis, R.W. !$#submission submitted to the EMBL Data Library, February 1993 !$#accession S30819 !'##molecule_type DNA !'##residues 1-577 ##label MUL !'##cross-references GB:U18922; EMBL:L10718; NID:g603405; !1PIDN:AAB64692.1; PID:g603406 REFERENCE A02683 !$#authors Sachs, A.B.; Bond, M.W.; Kornberg, R.D. !$#journal Cell (1986) 45:827-835 !$#title A single gene from yeast for both nuclear and cytoplasmic !1polyadenylate-binding proteins: domain structure and !1expression. !$#cross-references MUID:86218096; PMID:3518950 !$#accession A02683 !'##molecule_type DNA !'##residues 1-425,'R',427-577 ##label SAC !'##cross-references EMBL:M12780; NID:g172091; PIDN:AAA34838.1; !1PID:g172092 REFERENCE S41502 !$#authors Cockell, M.; Frutiger, S.; Hughes, G.J.; Gasser, S.M. !$#journal Nucleic Acids Res. (1994) 22:32-40 !$#title The yeast protein encoded by PUB1 binds T-rich single !1stranded DNA. !$#cross-references MUID:94173659; PMID:8127652 !$#accession S41503 !'##molecule_type protein !'##residues 8-15,'X',17;242-246,'X',248,'X';363-367,'X',369,'X' ##label !1COC REFERENCE S50431 !$#authors Dietrich, F.S. !$#submission submitted to the EMBL Data Library, December 1994 !$#description The sequence of S. cerevisiae cosmids 9163 and 9132. !$#accession S50668 !'##molecule_type DNA !'##residues 1-577 ##label DIE !'##cross-references EMBL:U18922; NID:g603405; PIDN:AAB64692.1; !1PID:g603406; GSPDB:GN00005; MIPS:YER165w COMMENT The cytosolic form binds the poly(A) tail of mRNA to form a !1periodic structure through a protein-protein interaction !1along a poly(A) strand. The nuclear form, which corresponds !1to the two polypeptides (53K and 17K) produced by !1proteolytic cleavage, binds the poly(A) tail without !1periodic structure. GENETICS !$#gene SGD:PAB1; MRNP; MIPS:YER165w !'##cross-references SGD:S0000967; MIPS:YER165w !$#map_position 5R CLASSIFICATION #superfamily polyadenylate-binding protein; !1ribonucleoprotein repeat homology KEYWORDS duplication; nucleus; RNA binding FEATURE !$39-106 #domain ribonucleoprotein repeat homology #label !8RRM1\ !$40-45 #region RNA-binding RNP2 motif\ !$79-86 #region RNA-binding RNP1 motif\ !$127-193 #domain ribonucleoprotein repeat homology #label !8RRM2\ !$128-133 #region RNA-binding RNP2 motif\ !$166-173 #region RNA-binding RNP1 motif\ !$220-286 #domain ribonucleoprotein repeat homology #label !8RRM3\ !$221-226 #region RNA-binding RNP2 motif\ !$259-266 #region RNA-binding RNP1 motif\ !$323-389 #domain ribonucleoprotein repeat homology #label !8RRM4\ !$324-329 #region RNA-binding RNP2 motif\ !$362-369 #region RNA-binding RNP1 motif SUMMARY #length 577 #molecular-weight 64344 #checksum 4317 SEQUENCE /// ENTRY DNZPPA #type complete TITLE polyadenylate-binding protein - fission yeast (Schizosaccharomyces pombe) ORGANISM #formal_name Schizosaccharomyces pombe DATE 14-Feb-1992 #sequence_revision 19-Jan-2001 #text_change 19-Jan-2001 ACCESSIONS T38950; A39720 REFERENCE Z21819 !$#authors Skelton, J.; Churcher, C.M.; Barrell, B.G.; Rajandream, !1M.A.; Wood, V. !$#submission submitted to the EMBL Data Library, May 1997 !$#accession T38950 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-653 ##label SKE !'##cross-references EMBL:Z95396; NID:g6090552; PIDN:CAB08762.1; !1PID:g2104439; GSPDB:GN00066; SPDB:SPAC57A7.04c !'##experimental_source strain 972h-; cosmid c57A7 REFERENCE A39720 !$#authors Burd, C.G.; Matunis, E.L.; Dreyfuss, G. !$#journal Mol. Cell. Biol. (1991) 11:3419-3424 !$#title The multiple RNA-binding domains of the mRNA poly(A)-binding !1protein have different RNA-binding activities. !$#cross-references MUID:91260690; PMID:1675426 !$#accession A39720 !'##molecule_type mRNA !'##residues 'MSLENSSTLSLCSNNTTHFW',35-348,'A',350-517,'PLSSLLEVR', !1527-642 ##label BUR !'##cross-references GB:M64603; NID:g173420; PIDN:AAA35320.1; !1PID:g173421 GENETICS !$#gene pabp; SPDB:SPAC57A7.04c !$#map_position 1 CLASSIFICATION #superfamily polyadenylate-binding protein; !1ribonucleoprotein repeat homology KEYWORDS duplication; nucleus; RNA binding FEATURE !$81-148 #domain ribonucleoprotein repeat homology #label !8RRM1\ !$82-87 #region RNA-binding RNP2 motif\ !$121-128 #region RNA-binding RNP1 motif\ !$169-235 #domain ribonucleoprotein repeat homology #label !8RRM2\ !$170-175 #region RNA-binding RNP2 motif\ !$208-215 #region RNA-binding RNP1 motif\ !$262-328 #domain ribonucleoprotein repeat homology #label !8RRM3\ !$263-268 #region RNA-binding RNP2 motif\ !$301-308 #region RNA-binding RNP1 motif\ !$365-431 #domain ribonucleoprotein repeat homology #label !8RRM4\ !$366-371 #region RNA-binding RNP2 motif\ !$404-411 #region RNA-binding RNP1 motif SUMMARY #length 653 #molecular-weight 71512 #checksum 2425 SEQUENCE /// ENTRY S58472 #type complete TITLE lysine-rich surface antigen - Entamoeba histolytica ORGANISM #formal_name Entamoeba histolytica DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S58472 REFERENCE S58472 !$#authors Bracha, R.; Nuchamowitz, Y.; Mirelman, D. !$#journal Infect. Immun. (1995) 63:917-925 !$#title Molecular cloning of a 30-kilodalton lysine-rich surface !1antigen from a nonpathogenic Entamoeba histolytica strain !1and its expression in a pathogenic strain. !$#cross-references MUID:95172741; PMID:7868264 !$#accession S58472 !'##status preliminary !'##molecule_type mRNA !'##residues 1-294 ##label BRA !'##cross-references EMBL:X80479; NID:g735965; PID:g735966 CLASSIFICATION #superfamily Entamoeba histolytica lysine-rich surface !1antigen; ribonucleoprotein repeat homology FEATURE !$3-69 #domain ribonucleoprotein repeat homology #label !8RRM1\ !$187-254 #domain ribonucleoprotein repeat homology #label RRM2 SUMMARY #length 294 #molecular-weight 33748 #checksum 7874 SEQUENCE /// ENTRY A55897 #type complete TITLE prolactin-induced T cell protein c15 - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 08-Oct-1999 ACCESSIONS A55897 REFERENCE A55897 !$#authors Axtell, S.M.; Truong, T.M.; O'Neal, K.D.; Yu-Lee, L. !$#journal Mol. Endocrinol. (1995) 9:312-318 !$#title Characterization of a prolactin-inducible gene, clone 15, in !1T cells. !$#cross-references MUID:95295743; PMID:7776977 !$#accession A55897 !'##status preliminary !'##molecule_type mRNA !'##residues 1-332 ##label AXT !'##cross-references GB:X82445; NID:g619906; PIDN:CAA57825.1; !1PID:g619907 CLASSIFICATION #superfamily rat prolactin-induced T cell protein c15 SUMMARY #length 332 #molecular-weight 38412 #checksum 4657 SEQUENCE /// ENTRY S58329 #type complete TITLE HSH49 protein - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein O6142; protein YOR319w ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S58329; S67225; S71999 REFERENCE S58318 !$#authors Pearson, B.M.; Hernando, Y.; Wolf, S.S.; Kalogeropoulos, A.; !1Schweizer, M. !$#submission submitted to the EMBL Data Library, August 1995 !$#accession S58329 !'##molecule_type DNA !'##residues 1-213 ##label PEA !'##cross-references EMBL:X90565; NID:g940836; PIDN:CAA62174.1; !1PID:g940850 REFERENCE S67213 !$#authors Pearson, B.M.; Hernando, Y.; Kalogeropoulos, A.; Schweizer, !1M. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67225 !'##molecule_type DNA !'##residues 1-213 ##label PEW !'##cross-references EMBL:Z75227; NID:g1420699; PIDN:CAA99639.1; !1PID:g1420700; GSPDB:GN00015; MIPS:YOR319w !'##experimental_source strain S288C REFERENCE S71986 !$#authors Pearson, B.M.; Hernando, Y.; Payne, J.; Wolf, S.S.; !1Kalogeropoulos, A.; Schweizer, M. !$#journal Yeast (1996) 12:1021-1031 !$#title Sequencing of a 35.71 kb DNA segment on the right arm of !1yeast chromosome XV reveals regions of similarity to !1chromosomes I and XIII. !$#cross-references MUID:97051589; PMID:8896266 !$#accession S71999 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-213 ##label PEF !'##cross-references EMBL:X90565; NID:g940836; PIDN:CAA62174.1; !1PID:g940850 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1995 GENETICS !$#gene SGD:HSH49; MIPS:YOR319w !'##cross-references SGD:S0005846; MIPS:YOR319w !$#map_position 15R FUNCTION !$#description essential splicing factor CLASSIFICATION #superfamily yeast HSH49 protein; ribonucleoprotein repeat !1homology KEYWORDS nucleus FEATURE !$10-78 #domain ribonucleoprotein repeat homology #label !8RRM1\ !$109-175 #domain ribonucleoprotein repeat homology #label RRM2 SUMMARY #length 213 #molecular-weight 24503 #checksum 5177 SEQUENCE /// ENTRY S54480 #type complete TITLE U6 snRNP protein PRP24 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YM8156.10c; protein YMR268c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 12-Nov-1999 ACCESSIONS S54480; A39562 REFERENCE S54014 !$#authors Lye, G.; Churcher, C.M. !$#submission submitted to the EMBL Data Library, May 1995 !$#accession S54480 !'##molecule_type DNA !'##residues 1-444 ##label LYE !'##cross-references EMBL:Z49260; NID:g809081; PID:g809091; !1GSPDB:GN00013; MIPS:YMR268c !'##experimental_source strain AB972 REFERENCE A39562 !$#authors Shannon, K.W.; Guthrie, C. !$#journal Genes Dev. (1991) 5:773-785 !$#title Suppressors of a U4 snRNA mutation define a novel U6 snRNP !1protein with RNA-binding motifs. !$#cross-references MUID:91224487; PMID:1827420 !$#accession A39562 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type DNA !'##residues 202-288 ##label SHA GENETICS !$#gene SGD:PRP24; MIPS:YMR268c !'##cross-references SGD:S0004881; MIPS:YMR268c !$#map_position 13R CLASSIFICATION #superfamily yeast U6 snRNP protein PRP24; ribonucleoprotein !1repeat homology FEATURE !$211-279 #domain ribonucleoprotein repeat homology #label RRM3 SUMMARY #length 444 #molecular-weight 50848 #checksum 1741 SEQUENCE /// ENTRY JC5530 #type complete TITLE T-cluster binding protein - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS JC5530 REFERENCE JC5530 !$#authors Doi, T.; Minami, T.; Itoh, M.; Aburatani, H.; Kawabe, Y.; !1Kodama, T.; Kondo, N.; Satoh, Y.; Asayama, T.; Imanishi, T. !$#journal Biochem. Biophys. Res. Commun. (1997) 235:625-630 !$#title An alternative form of nucleolysin binds to a T-cluster DNA !1in the silencer element of platelet factor 4 gene. !$#cross-references MUID:97350833; PMID:9207209 !$#accession JC5530 !'##molecule_type mRNA !'##residues 1-265 ##label DOI !'##cross-references DDBJ:D64015; NID:g2281005; PIDN:BAA21559.1; !1PID:g2281006 COMMENT This protein plays a role in the regulation of platelet !1factor 4 gene expression by binding to the T-cluster and the !1T-rich sequence. GENETICS !$#gene GDB:TIAL1; TIAR !'##cross-references GDB:679350; OMIM:603413 CLASSIFICATION #superfamily human T-cluster binding protein; !1ribonucleoprotein repeat homology FEATURE !$59-126 #domain ribonucleoprotein repeat homology #label !8RRM2\ !$60-65 #region RNA-binding RNP2 motif\ !$99-106 #region RNA-binding RNP1 motif\ !$167-228 #domain ribonucleoprotein repeat homology #label !8RRM3\ !$168-173 #region RNA-binding RNP2 motif\ !$201-208 #region RNA-binding RNP1 motif SUMMARY #length 265 #molecular-weight 29650 #checksum 7 SEQUENCE /// ENTRY S38331 #type complete TITLE glycine-rich RNA-binding protein - rape ORGANISM #formal_name Brassica napus #common_name rape DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S38331; S25120 REFERENCE S38331 !$#authors Bergeron, D.; Beauseigle, D.; Bellemare, G. !$#journal Biochim. Biophys. Acta (1993) 1216:123-125 !$#title Sequence and expression of a gene encoding a protein with !1RNA-binding and glycine-rich domains in Brassica napus. !$#cross-references MUID:94032471; PMID:7916642 !$#accession S38331 !'##molecule_type DNA !'##residues 1-169 ##label BER !'##cross-references EMBL:Z14143; NID:g17818; PIDN:CAA78513.1; !1PID:g17819 GENETICS !$#introns 36/3 CLASSIFICATION #superfamily glycine-rich RNA-binding protein; !1ribonucleoprotein repeat homology FEATURE !$7-74 #domain ribonucleoprotein repeat homology #label RRM1 SUMMARY #length 169 #molecular-weight 16304 #checksum 1481 SEQUENCE /// ENTRY S14857 #type complete TITLE glycine-rich protein - carrot ORGANISM #formal_name Daucus carota #common_name carrot DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S14857 REFERENCE S14857 !$#authors Sturm, A. !$#submission submitted to the EMBL Data Library, March 1991 !$#description A wound-inducible glycine-rich protein from Daucus carota !1with homology to single-stranded nucleic acid binding !1proteins. !$#accession S14857 !'##status preliminary !'##molecule_type mRNA !'##residues 1-157 ##label STU !'##cross-references EMBL:X58146; NID:g18346; PIDN:CAA41152.1; !1PID:g18347 CLASSIFICATION #superfamily glycine-rich RNA-binding protein; !1ribonucleoprotein repeat homology FEATURE !$7-74 #domain ribonucleoprotein repeat homology #label RRM1 SUMMARY #length 157 #molecular-weight 15718 #checksum 8087 SEQUENCE /// ENTRY S12312 #type complete TITLE glycine-rich RNA-binding protein (clone S2) - sorghum ORGANISM #formal_name Sorghum bicolor #common_name sorghum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S12312 REFERENCE S12311 !$#authors Cretin, C.; Puigdomenech, P. !$#journal Plant Mol. Biol. (1990) 15:783-785 !$#title Glycine-rich RNA-binding proteins from Sorghum vulgare. !$#cross-references MUID:91346715; PMID:1715211 !$#accession S12312 !'##molecule_type mRNA !'##residues 1-168 ##label CRE !'##cross-references EMBL:X57662; NID:g21624; PIDN:CAA40862.1; !1PID:g21625 !'##note in the authors' translation two additional Gly are shown after !1110-Gly CLASSIFICATION #superfamily glycine-rich RNA-binding protein; !1ribonucleoprotein repeat homology KEYWORDS GTP binding FEATURE !$9-76 #domain ribonucleoprotein repeat homology #label RRM1 SUMMARY #length 168 #molecular-weight 16360 #checksum 656 SEQUENCE /// ENTRY B71334 #type complete TITLE probable RNA-binding protein - syphilis spirochete ORGANISM #formal_name Treponema pallidum subsp. pallidum #common_name syphilis spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B71334 REFERENCE A71250 !$#authors Fraser, C.M.; Norris, S.J.; Weinstock, G.M.; White, O.; !1Sutton, G.G.; Dodson, R.; Gwinn, M.; Hickey, E.K.; Clayton, !1R.; Ketchum, K.A.; Sodergren, E.; Hardham, J.M.; McLeod, !1M.P.; Salzberg, S.; Peterson, J.; Khalak, H.; Richardson, !1D.; Howell, J.K.; Chidambaram, M.; Utterback, T.; McDonald, !1L.; Artiach, P.; Bowman, C.; Cotton, M.D.; Fujii, C.; !1Garland, S.; Hatch, B.; Horst, K.; Roberts, K.; Watthey, L.; !1Weidman, J.; Smith, H.O.; Venter, J.C. !$#journal Science (1998) 281:375-388 !$#title Complete genome sequence of Treponema pallidum, the syphilis !1spirochete. !$#cross-references MUID:98332770; PMID:9665876 !$#accession B71334 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-105 ##label COL !'##cross-references GB:AE001215; GB:AE000520; NID:g3322631; !1PIDN:AAC65342.1; PID:g3322634 !'##experimental_source strain Nichols GENETICS !$#gene TP0356 CLASSIFICATION #superfamily syphilis spirochete probable RNA-binding !1protein; ribonucleoprotein repeat homology FEATURE !$20-87 #domain ribonucleoprotein repeat homology #label RRM1 SUMMARY #length 105 #molecular-weight 11956 #checksum 5068 SEQUENCE /// ENTRY S46286 #type complete TITLE RNA-binding protein - wood tobacco ORGANISM #formal_name Nicotiana sylvestris #common_name wood tobacco DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S46286 REFERENCE S46286 !$#authors Hirose, T.; Sugita, M.; Sugiura, M. !$#journal Mol. Gen. Genet. (1994) 244:360-366 !$#title Characterization of a cDNA encoding a novel type of !1RNA-binding protein in tobacco: its expression and nucleic !1acid-binding properties. !$#cross-references MUID:94359458; PMID:8078461 !$#accession S46286 !'##status preliminary !'##molecule_type mRNA !'##residues 1-259 ##label HIR !'##cross-references GB:D26182; NID:g575607; PIDN:BAA05170.1; !1PID:g624925 CLASSIFICATION #superfamily wood tobacco RNA-binding protein; !1ribonucleoprotein repeat homology FEATURE !$41-108 #domain ribonucleoprotein repeat homology #label RRM1 SUMMARY #length 259 #molecular-weight 26617 #checksum 2014 SEQUENCE /// ENTRY JSBYP1 #type complete TITLE centromere-binding protein CP1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES centromere promoter factor CPF1; centromere-binding factor CBF1; protein J1730; protein YJR060w ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1991 #sequence_revision 19-Oct-1995 #text_change 12-Nov-1999 ACCESSIONS S57079; A36310; A38772; A35143; A38779; S12322; A38780; !1S71682; S12204 REFERENCE S57052 !$#authors Huang, M.E.; Chuat, J.C.; Galibert, F. !$#submission submitted to the Protein Sequence Database, September 1995 !$#accession S57079 !'##molecule_type DNA !'##residues 1-351 ##label MAN !'##cross-references EMBL:Z49560; NID:g1015730; PIDN:CAA89588.1; !1PID:g1015731; GSPDB:GN00010; MIPS:YJR060w REFERENCE A36310 !$#authors Baker, R.E.; Masison, D.C. !$#journal Mol. Cell. Biol. (1990) 10:2458-2467 !$#title Isolation of the gene encoding the Saccharomyces cerevisiae !1centromere-binding protein CP1. !$#cross-references MUID:90258829; PMID:2188087 !$#accession A36310 !'##molecule_type DNA !'##residues 1-261,'R',263-351 ##label BAK !'##cross-references EMBL:M34070; NID:g171302; PIDN:AAA34524.1; !1PID:g171303 !$#accession A38772 !'##molecule_type protein !'##residues 40-59;136-150 ##label BAK2 REFERENCE A35143 !$#authors Cai, M.; Davis, R.W. !$#journal Cell (1990) 61:437-446 !$#title Yeast centromere binding protein CBF1, of the !1helix-loop-helix protein family, is required for chromosome !1stability and methionine prototrophy. !$#cross-references MUID:90242389; PMID:2185892 !$#accession A35143 !'##molecule_type DNA !'##residues 1-261,'R',263-351 ##label CAI !'##cross-references EMBL:M33620; NID:g171212; PIDN:AAA34490.1; !1PID:g171213 !$#accession A38779 !'##molecule_type protein !'##residues 214-231 ##label CAI2 REFERENCE S12322 !$#authors Mellor, J.; Jiang, W.; Funk, M.; Rathjen, J.; Barnes, C.A.; !1Hinz, T.; Hegemann, J.H.; Philippsen, P. !$#journal EMBO J. (1990) 9:4017-4026 !$#title CPF1, a yeast protein which functions in centromeres and !1promoters. !$#cross-references MUID:91065332; PMID:2249662 !$#accession S12322 !'##molecule_type DNA !'##residues 1-143,'F',145-261,'R',263-351 ##label MEL1 !'##cross-references EMBL:X52137; NID:g3586; PIDN:CAA36382.1; PID:g3587 !$#accession A38780 !'##molecule_type protein !'##residues 24-33;40-47;66-76;102-115;166-180;209-218;236-251;302-311 !1##label MEL2 REFERENCE S71676 !$#authors Huang, M.E.; Manus, V.; Chuat, J.C.; Galibert, F. !$#journal Yeast (1996) 12:869-875 !$#title Analysis of a 62 kb DNA sequence of chromosome X reveals 36 !1open reading frames and a gene cluster with a counterpart on !1chromosome XI. !$#cross-references MUID:96437976; PMID:8840504 !$#accession S71682 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-351 ##label HUA !'##cross-references EMBL:L47993; NID:g1019675; PIDN:AAB39286.1; !1PID:g1019682 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1995 GENETICS !$#gene SGD:CBF1; CP1; CPF1; CEP1; MIPS:YJR060w !'##cross-references SGD:S0003821; MIPS:YJR060w !$#map_position 10R CLASSIFICATION #superfamily centromere-binding protein CP1 KEYWORDS DNA binding; nucleus; transcription factor SUMMARY #length 351 #molecular-weight 39387 #checksum 5314 SEQUENCE /// ENTRY JQ1528 #type complete TITLE small nuclear ribonucleoprotein U1A - human ALTERNATE_NAMES snRNP U1A ORGANISM #formal_name Homo sapiens #common_name man DATE 17-Aug-1992 #sequence_revision 02-Dec-1994 #text_change 22-Jun-1999 ACCESSIONS JQ1528; S01497; S65550 REFERENCE JQ1528 !$#authors Nelissen, R.L.H.; Sillekens, P.T.G.; Beijer, R.P.; Geurts !1van Kessel, A.H.M.; van Venrooij, W.J. !$#journal Gene (1991) 102:189-196 !$#title Structure, chromosomal localization and evolutionary !1conservation of the gene encoding human U1 snRNP-specific A !1protein. !$#cross-references MUID:91340152; PMID:1831431 !$#accession JQ1528 !'##molecule_type DNA !'##residues 1-282 ##label NEL !'##cross-references GB:M60779; GB:M60780; GB:M60781; GB:M60782 REFERENCE S01497 !$#authors Sillekens, P.T.G.; Habets, W.J.; Beijer, R.P.; van Venrooij, !1W.J. !$#journal EMBO J. (1987) 6:3841-3848 !$#title cDNA cloning of the human U1 snRNA-associated A protein: !1extensive homology between U1 and U2 snRNP-specific !1proteins. !$#cross-references MUID:88111575; PMID:2962859 !$#accession S01497 !'##molecule_type mRNA !'##residues 1-282 ##label SIL !'##cross-references EMBL:X06347; NID:g37540; PIDN:CAA29653.1; !1PID:g37541 REFERENCE S65550 !$#authors Avis, J.M.; Allain, F.H.T.; Howe, P.W.A.; Varani, G.; Nagai, !1K.; Neuhaus, D. !$#journal J. Mol. Biol. (1996) 257:398-411 !$#title Solution structure of the N-terminal RNP domain of U1A !1protein: the role of C-terminal residues in structure !1stability and RNA binding. !$#cross-references MUID:96180024; PMID:8609632 !$#accession S65550 !'##molecule_type protein !'##residues 2-11 ##label AVI GENETICS !$#gene GDB:SNRPA !'##cross-references GDB:120380 !$#map_position 19q13.2-19q13.2 !$#introns 25/1; 82/3; 142/3; 200/3; 230/2 CLASSIFICATION #superfamily small nuclear ribonucleoprotein U1A; !1ribonucleoprotein repeat homology KEYWORDS duplication; pre-mRNA splicing; RNA binding FEATURE !$11-79 #domain ribonucleoprotein repeat homology #label !8RRM1\ !$140-200 #region proline-rich\ !$209-271 #domain ribonucleoprotein repeat homology #label RRM2 SUMMARY #length 282 #molecular-weight 31279 #checksum 6379 SEQUENCE /// ENTRY S42114 #type complete TITLE small nuclear ribonucleoprotein U1A - mouse ALTERNATE_NAMES snRNP U1A ORGANISM #formal_name Mus musculus #common_name house mouse DATE 20-May-1994 #sequence_revision 02-Dec-1994 #text_change 22-Jun-1999 ACCESSIONS S42113; S42114 REFERENCE S42113 !$#authors Bennett, M.M.; Baron, M.A.; Craft, J. !$#journal Nucleic Acids Res. (1993) 21:4404 !$#title Nucleotide sequence analysis of the A protein of the U1 !1small nuclear ribonucleoprotein particle: the murine protein !1contains a 5' amino-terminal tag. !$#cross-references MUID:94021403; PMID:8415008 !$#accession S42113 !'##molecule_type mRNA !'##residues 1-31 ##label BE2 !'##cross-references EMBL:L15447 !'##note assignment of Met-1 rather than Met-7 as the initiator codon in !1this species is based on comparative electrophoretic !1properties of the protein REFERENCE S42114 !$#authors Bennett, M.M.; Baron, M.A.; Craft, J. !$#submission submitted to the EMBL Data Library, August 1993 !$#accession S42114 !'##molecule_type mRNA !'##residues 1-287 ##label BEN !'##cross-references EMBL:L15447; NID:g349003; PIDN:AAC37611.1; !1PID:g349004 CLASSIFICATION #superfamily small nuclear ribonucleoprotein U1A; !1ribonucleoprotein repeat homology KEYWORDS blocked amino end; duplication; pre-mRNA splicing; RNA !1binding FEATURE !$17-85 #domain ribonucleoprotein repeat homology #label !8RRM1\ !$145-205 #region proline-rich\ !$214-276 #domain ribonucleoprotein repeat homology #label RRM2 SUMMARY #length 287 #molecular-weight 31835 #checksum 9215 SEQUENCE /// ENTRY S30564 #type complete TITLE small nuclear ribonucleoprotein U1A - African clawed frog ALTERNATE_NAMES snRNP protein U1A ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S30564 REFERENCE S30564 !$#authors Scherly, D.; Kambach, C.; Boelens, W.; van Venrooij, W.J.; !1Mattaj, I.W. !$#submission submitted to the EMBL Data Library, February 1991 !$#description Conserved amino acids within and outside of the N-terminal !1RNP motif of the U1A snRNP protein involved in U1 RNA !1binding. !$#accession S30564 !'##status preliminary !'##molecule_type mRNA !'##residues 1-282 ##label SCH !'##cross-references EMBL:X57953; NID:g65180; PIDN:CAA41021.1; !1PID:g65181 CLASSIFICATION #superfamily small nuclear ribonucleoprotein U1A; !1ribonucleoprotein repeat homology FEATURE !$11-79 #domain ribonucleoprotein repeat homology #label !8RRM1\ !$209-271 #domain ribonucleoprotein repeat homology #label RRM2 SUMMARY #length 282 #molecular-weight 31610 #checksum 5688 SEQUENCE /// ENTRY A25910 #type complete TITLE small nuclear ribonucleoprotein U2B'' - human ALTERNATE_NAMES snRNP U2B'' ORGANISM #formal_name Homo sapiens #common_name man DATE 16-Aug-1988 #sequence_revision 02-Dec-1994 #text_change 22-Jun-1999 ACCESSIONS A25910 REFERENCE A25910 !$#authors Habets, W.J.; Sillekens, P.T.G.; Hoet, M.H.; Schalken, J.A.; !1Roebroek, A.J.M.; Leunissen, J.A.M.; van de Ven, W.J.M.; van !1Venrooij, W.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:2421-2425 !$#title Analysis of a cDNA clone expressing a human autoimmune !1antigen: full-length sequence of the U2 small nuclear !1RNA-associated B" antigen. !$#cross-references MUID:87175685; PMID:2951739 !$#accession A25910 !'##molecule_type mRNA !'##residues 1-225 ##label HAB !'##cross-references GB:M15841; NID:g340104; PIDN:AAA36796.1; !1PID:g340105 GENETICS !$#gene GDB:SNRPB2 !'##cross-references GDB:125281 !$#map_position 20pter-20qter CLASSIFICATION #superfamily small nuclear ribonucleoprotein U1A; !1ribonucleoprotein repeat homology KEYWORDS duplication; pre-mRNA splicing; RNA binding FEATURE !$8-76 #domain ribonucleoprotein repeat homology #label !8RRM1\ !$152-214 #domain ribonucleoprotein repeat homology #label RRM2 SUMMARY #length 225 #molecular-weight 25486 #checksum 8097 SEQUENCE /// ENTRY A54279 #type complete TITLE small nuclear ribonucleoprotein D25 - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES snRNP D25; splicing protein snf ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A54279; S35445 REFERENCE A54279 !$#authors Flickinger, T.W.; Salz, H.K. !$#journal Genes Dev. (1994) 8:914-925 !$#title The Drosophila sex determination gene snf encodes a nuclear !1protein with sequence and functional similarity to the !1mammalian U1A snRNP protein. !$#cross-references MUID:95011590; PMID:7926776 !$#accession A54279 !'##status preliminary !'##molecule_type DNA !'##residues 1-216 ##label FLI !'##cross-references GB:L29521; NID:g463050; PIDN:AAA28903.1; !1PID:g463051 REFERENCE S35445 !$#authors Harper, D.S.; Fresco, L.D.; Keene, J.D. !$#journal Nucleic Acids Res. (1992) 20:3645-3650 !$#title RNA binding specificity of a Drosophila snRNP protein that !1shares sequence homology with mammalian U1-A and U2-B'' !1proteins. !$#cross-references MUID:92350664; PMID:1386424 !$#accession S35445 !'##status preliminary !'##molecule_type mRNA !'##residues 1-216 ##label HAR !'##cross-references EMBL:M89775; NID:g157171; PIDN:AAA28441.1; !1PID:g157172 GENETICS !$#gene snf !'##cross-references FlyBase:FBgn0003449 !$#introns 118/2 CLASSIFICATION #superfamily small nuclear ribonucleoprotein U1A; !1ribonucleoprotein repeat homology KEYWORDS nucleus; pre-mRNA splicing FEATURE !$8-76 #domain ribonucleoprotein repeat homology #label !8RRM1\ !$143-205 #domain ribonucleoprotein repeat homology #label RRM2 SUMMARY #length 216 #molecular-weight 24546 #checksum 3825 SEQUENCE /// ENTRY S59118 #type complete TITLE small nuclear ribonucleoprotein U1A [imported] - Arabidopsis thaliana ALTERNATE_NAMES snRNP-specific protein U1A ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 02-Feb-2001 ACCESSIONS S59118; T00426; A84917 REFERENCE S59117 !$#authors Simpson, G.G.; Clark, G.P.; Rothnie, H.M.; Boelens, W.; van !1Venrooij, W.; Brown, J.W.S. !$#journal EMBO J. (1995) 14:4540-4550 !$#title Molecular characterization of the spliceosomal proteins U1A !1and U2B" from higher plants. !$#cross-references MUID:96003634; PMID:7556097 !$#accession S59118 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-250 ##label SIM !'##cross-references EMBL:Z49991; NID:g1050429; PIDN:CAA90283.1; !1PID:g1050430 REFERENCE Z14149 !$#authors Rounsley, S.D.; Lin, X.; Ketchum, K.A.; Crosby, M.L.; !1Brandon, R.C.; Sykes, S.M.; Mason, T.M.; Kerlavage, A.R.; !1Adams, M.D.; Somerville, C.R.; Venter, J.C. !$#submission submitted to the EMBL Data Library, October 1998 !$#description Arabidopsis thaliana chromosome II BAC T30B22 genomic !1sequence. !$#accession T00426 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-250 ##label ROU !'##cross-references EMBL:AC002535; NID:g2529657; PIDN:AAC62852.1; !1PID:g2529669 !'##experimental_source cultivar Columbia REFERENCE A84420 !$#authors Lin, X.; Kaul, S.; Rounsley, S.D.; Shea, T.P.; Benito, M.I.; !1Town, C.D.; Fujii, C.Y.; Mason, T.M.; Bowman, C.L.; !1Barnstead, M.E.; Feldblyum, T.V.; Buell, C.R.; Ketchum, !1K.A.; Lee, J.J.; Ronning, C.M.; Koo, H.; Moffat, K.S.; !1Cronin, L.A.; Shen, M.; VanAken, S.E.; Umayam, L.; Tallon, !1L.J.; Gill, J.E.; Adams, M.D.; Carrera, A.J.; Creasy, T.H.; !1Goodman, H.M.; Somerville, C.R.; Copenhaver, G.P.; Preuss, !1D.; Nierman, W.C.; White, O.; Eisen, J.A.; Salzberg, S.L.; !1Fraser, C.M.; Venter, J.C. !$#journal Nature (1999) 402:761-768 !$#title Sequence and analysis of chromosome 2 of the plant !1Arabidopsis thaliana. !$#cross-references MUID:20083487; PMID:10617197 !$#accession A84917 !'##status preliminary !'##molecule_type DNA !'##residues 1-250 ##label STO !'##cross-references GB:AE002093; NID:g2529669; PIDN:AAC62852.1; !1GSPDB:GN00139 GENETICS !$#gene At2g47580 !$#map_position 2 !$#introns 33/1; 90/3; 122/1; 154/3 CLASSIFICATION #superfamily small nuclear ribonucleoprotein U1A; !1ribonucleoprotein repeat homology FEATURE !$19-87 #domain ribonucleoprotein repeat homology #label !8RRM1\ !$178-240 #domain ribonucleoprotein repeat homology #label RRM2 SUMMARY #length 250 #molecular-weight 28074 #checksum 1305 SEQUENCE /// ENTRY JC6127 #type complete TITLE RNA-binding protein type 1 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS JC6127 REFERENCE JC6127 !$#authors Shimamoto, A.; Kitao, S.; Ichikawa, K.; Suzuki, N.; Yamabe, !1Y.; Imamura, O.; Tokutake, Y.; Satoh, M.; Matsumoto, T.; !1Kuromitsu, J.; Kataoka, H.; Sugawara, K.; Sugawara, M.; !1Sugimoto, M.; Goto, M.; Furuichi, Y. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1996) 93:10913-10917 !$#title A unique human gene that spans over 230 kb in the human !1chromosome 8p11-12 and codes multiple family proteins !1sharing RNA-binding motifs. !$#cross-references MUID:97008106; PMID:8855282 !$#accession JC6127 !'##molecule_type mRNA !'##residues 1-196 ##label SHI !'##cross-references DDBJ:D84107; NID:g1669546; PIDN:BAA12225.1; !1PID:g1669547 COMMENT This protein plays a role in RNA metabolism. GENETICS !$#gene GDB:RBPMS !'##cross-references GDB:9956209; OMIM:601558 !$#map_position 8p12-8p11 CLASSIFICATION #superfamily human RNA-binding protein type 1; !1ribonucleoprotein repeat homology KEYWORDS RNA binding FEATURE !$25-88 #domain ribonucleoprotein repeat homology #label RRM2 SUMMARY #length 196 #molecular-weight 21802 #checksum 3094 SEQUENCE /// ENTRY G01420 #type complete TITLE TAR RNA-binding protein 2 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 20-Apr-2000 ACCESSIONS G01420 REFERENCE G06941 !$#authors Gatignol, A. !$#submission submitted to the EMBL Data Library, April 1994 !$#accession G01420 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-366 ##label GAT !'##cross-references EMBL:U08998; NID:g478989; PIDN:AAB50581.1; !1PID:g478990 GENETICS !$#gene GDB:TARBP2; TRBP2 !'##cross-references GDB:320003 !$#map_position 12q12-12q13 CLASSIFICATION #superfamily RNA-binding protein TAR; double-stranded !1RNA-binding repeat homology FEATURE !$27-98 #domain double-stranded RNA-binding repeat homology !8#label DSR1\ !$156-228 #domain double-stranded RNA-binding repeat homology !8#label DSR2 SUMMARY #length 366 #molecular-weight 39073 #checksum 8727 SEQUENCE /// ENTRY S27945 #type complete TITLE RNA-binding protein A - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S27945 REFERENCE S27945 !$#authors Jantsch, M.F.; Gall, J.G. !$#submission submitted to the EMBL Data Library, July 1992 !$#description Xenopus laevis double-stranded RNA binding protein A. !$#accession S27945 !'##molecule_type mRNA !'##residues 1-298 ##label JAN !'##cross-references EMBL:M96370; NID:g214738; PIDN:AAA49947.1; !1PID:g214739 CLASSIFICATION #superfamily RNA-binding protein TAR; double-stranded !1RNA-binding repeat homology FEATURE !$17-88 #domain double-stranded RNA-binding repeat homology !8#label DSR1\ !$109-181 #domain double-stranded RNA-binding repeat homology !8#label DSR2 SUMMARY #length 298 #molecular-weight 32851 #checksum 9269 SEQUENCE /// ENTRY A40315 #type complete TITLE maternal effect protein (staufen) - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A40315 REFERENCE A40315 !$#authors St. Johnston, D.; Beuchle, D.; Nuesslein-Volhard, C. !$#journal Cell (1991) 66:51-63 !$#title staufen, a gene required to localize maternal RNAs in the !1Drosophila egg. !$#cross-references MUID:91300552; PMID:1712672 !$#accession A40315 !'##status preliminary !'##molecule_type mRNA !'##residues 1-1026 ##label STJ !'##cross-references GB:M69111; NID:g158505; PIDN:AAA73062.1; !1PID:g158506 GENETICS !$#gene FlyBase:stau !'##cross-references FlyBase:FBgn0003520 CLASSIFICATION #superfamily maternal effect protein; double-stranded !1RNA-binding repeat homology FEATURE !$308-379 #domain double-stranded RNA-binding repeat homology !8#label DSR1\ !$575-646 #domain double-stranded RNA-binding repeat homology !8#label DSR2\ !$708-782 #domain double-stranded RNA-binding repeat homology !8#label DSR3 SUMMARY #length 1026 #molecular-weight 110347 #checksum 187 SEQUENCE /// ENTRY I38908 #type complete TITLE UV-damaged DNA-binding protein - human ALTERNATE_NAMES damage-specific DNA binding protein 1; DDBa p127; X-associated protein 1 ORGANISM #formal_name Homo sapiens #common_name man DATE 17-Mar-2000 #sequence_revision 17-Mar-2000 #text_change 17-Mar-2000 ACCESSIONS I38908; I56904 REFERENCE I38908 !$#authors Dualan, R.; Brody, T.; Keeney, S.; Nichols, A.F.; Admon, A.; !1Linn, S. !$#journal Genomics (1995) 29:62-69 !$#title Chromosomal localization and cDNA cloning of the genes (DDB1 !1and DDB2) for the p127 and p48 subunits of a Human !1damage-specific DNA binding protein. !$#cross-references MUID:96079092; PMID:8530102 !$#accession I38908 !'##status preliminary !'##molecule_type mRNA !'##residues 1-1140 ##label DUA !'##cross-references EMBL:U18299; NID:g1052864; PIDN:AAC50349.1; !1PID:g1052865 REFERENCE I56904 !$#authors Lee, T.H.; Elledge, S.J.; Butel, J.S. !$#journal J. Virol. (1995) 69:1107-1114 !$#title Hepatitis B virus X protein interacts with a probable !1cellular DNA repair protein. !$#cross-references MUID:95115068; PMID:7815490 !$#accession I56904 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-1140 ##label LEE !'##cross-references GB:L40326; NID:g695361; PIDN:AAA62838.1; !1PID:g695362 GENETICS !$#gene GDB:DDB1 !'##cross-references GDB:595014; OMIM:600045 !$#map_position 11q12-11q13 CLASSIFICATION #superfamily UV-damaged DNA-binding protein KEYWORDS DNA binding; DNA repair SUMMARY #length 1140 #molecular-weight 126967 #checksum 3627 SEQUENCE /// ENTRY S38777 #type complete TITLE UV-damaged DNA-binding protein - green monkey ORGANISM #formal_name Cercopithecus aethiops #common_name green monkey, grivet DATE 22-Jan-1994 #sequence_revision 19-Oct-1995 #text_change 22-Jun-1999 ACCESSIONS S38777; S37614 REFERENCE S38777 !$#authors Takao, M.; Abramic, M.; Moos Jr., M.; Otrin, V.R.; Wootton, !1J.C.; McLenigan, M.; Levine, A.S.; Protic, M. !$#submission submitted to the EMBL Data Library, August 1993 !$#accession S38777 !'##molecule_type mRNA !'##residues 1-1140 ##label TAK !'##cross-references GB:L20216; NID:g304025; PIDN:AAA03021.1; !1PID:g304026 REFERENCE S37614 !$#authors Takao, M.; Abramic, M.; Moos Jr., M.; Otrin, V.R.; Wootton, !1J.C.; McLenigan, M.; Levine, A.S.; Protic, M. !$#journal Nucleic Acids Res. (1993) 21:4111-4118 !$#title A 127 kDa component of a UV-damaged DNA-binding complex, !1which is defective in some xeroderma pigmentosum group E !1patients, is homologous to a slime mold protein. !$#cross-references MUID:93382790; PMID:8371985 !$#accession S37614 !'##molecule_type mRNA !'##residues 703-1140 ##label TA2 !'##cross-references GB:L20216 !'##note parts of the sequence were confirmed by protein sequencing COMMENT This protein is part of a DNA-binding complex that may !1function in the repair of UV-induced photoproducts. It is !1found in complexes formed between UV-damaged DNA and nuclear !1extracts. CLASSIFICATION #superfamily UV-damaged DNA-binding protein KEYWORDS DNA binding; DNA repair SUMMARY #length 1140 #molecular-weight 126981 #checksum 3501 SEQUENCE /// ENTRY DNHU53 #type complete TITLE cellular tumor antigen p53 [validated] - human ALTERNATE_NAMES cellular phosphoprotein p53; oncoprotein p53; transformation suppressor p53; tumor suppressor p53 ORGANISM #formal_name Homo sapiens #common_name man DATE 05-Oct-1988 #sequence_revision 18-Nov-1994 #text_change 15-Sep-2000 ACCESSIONS A25224; A43073; JT0436; S40773; S42669; A22837; A55060; !1A25397; B25397; S42452; S42453; I38082; I38083; I38084; !1I38085; I38086; I38087; I38088; I38089; I38090; I38091; !1I38092; I38093; A44905; I58354; I78850; I52681; S60153 REFERENCE A25224 !$#authors Lamb, P.; Crawford, L. !$#journal Mol. Cell. Biol. (1986) 6:1379-1385 !$#title Characterization of the human p53 gene. !$#cross-references MUID:87064416; PMID:2946935 !$#accession A25224 !'##molecule_type DNA !'##residues 1-393 ##label LAM !'##cross-references EMBL:X01405; GB:M13121; GB:N00032; NID:g189460; !1PIDN:AAA59987.1; PID:g386994 REFERENCE JT0436 !$#authors Buchman, V.L.; Chumakov, P.M.; Ninkina, N.N.; Samarina, !1O.P.; Georgiev, G.P. !$#journal Gene (1988) 70:245-252 !$#title A variation in the structure of the protein-coding region of !1the human p53 gene. !$#cross-references MUID:89108008; PMID:2905688 !$#accession A43073 !'##molecule_type DNA !'##residues 1-393 ##label BUC1 !'##cross-references EMBL:M22898; NID:g189474 !'##note this 72-Arg allele appears to be about 5 times more frequent !1than the 72-Pro allele !$#accession JT0436 !'##molecule_type DNA !'##residues 1-71,'P',73-393 ##label BUC2 !'##cross-references EMBL:M22898; NID:g189474; PIDN:AAA59988.1; !1PID:g189476 !'##note this 72-Pro allele was found in both normal and malignant cell !1lines REFERENCE S40773 !$#authors Chumakov, P.M.; Almazov, V.P.; Jenkins, J.R. !$#submission submitted to the EMBL Data Library, August 1990 !$#accession S40773 !'##molecule_type DNA !'##residues 1-393 ##label CHU !'##cross-references EMBL:X54156; NID:g35213; PIDN:CAA38095.1; !1PID:g35214 REFERENCE S42669 !$#authors Matlashewski, G.; Lamb, P.; Pim, D.; Peacock, J.; Crawford, !1L.; Benchimol, S. !$#journal EMBO J. (1984) 3:3257-3262 !$#title Isolation and characterization of a human p53 cDNA clone: !1expression of the human p53 gene. !$#cross-references MUID:85126934; PMID:6396087 !$#accession S42669 !'##molecule_type mRNA !'##residues 101-393 ##label MKI1 !'##cross-references EMBL:X01405; NID:g35215; PIDN:CAA25652.1; !1PID:g642241 REFERENCE A22837 !$#authors Zakut-Houri, R.; Bienz-Tadmor, B.; Givol, D.; Oren, M. !$#journal EMBO J. (1985) 4:1251-1255 !$#title Human p53 cellular tumor antigen: cDNA sequence and !1expression in COS cells. !$#cross-references MUID:85230577; PMID:4006916 !$#accession A22837 !'##molecule_type mRNA !'##residues 1-71,'P',73-393 ##label ZAK !'##cross-references EMBL:X02469; EMBL:M60950; NID:g35209; !1PIDN:CAA26306.1; PID:g35210 REFERENCE A55060 !$#authors Harlow, E.; Williamson, N.M.; Ralston, R.; Helfman, D.M.; !1Adams, T.E. !$#journal Mol. Cell. Biol. (1985) 5:1601-1610 !$#title Molecular cloning and in vitro expression of a cDNA clone !1for human cellular tumor antigen p53. !$#cross-references MUID:85267676; PMID:3894933 !$#accession A55060 !'##molecule_type mRNA !'##residues 1-71,'P',73-272,'H',274-393 ##label HAR !'##cross-references GB:K03199; NID:g189478; PIDN:AAA59989.1; !1PID:g189479 !'##experimental_source clone pR4-2, cell line A431 REFERENCE A93086 !$#authors Harris, N.; Brill, E.; Shohat, O.; Prokocimer, M.; Wolf, D.; !1Arai, N.; Rotter, V. !$#journal Mol. Cell. Biol. (1986) 6:4650-4656 !$#title Molecular basis for heterogeneity of the human p53 protein. !$#cross-references MUID:87089826; PMID:3025664 !$#accession A25397 !'##molecule_type mRNA !'##residues 1-78,'T',80-393 ##label HAR1 !'##cross-references EMBL:M14694; NID:g339813; PIDN:AAA61211.1; !1PID:g339814 !'##experimental_source clone p53-H-1, transformed hybridoma SV-80 cell !1line !$#accession B25397 !'##molecule_type mRNA !'##residues 1-71,'P',73-78,'T',80-393 ##label HAR2 !'##cross-references EMBL:M14695; NID:g339815; PIDN:AAA61212.1; !1PID:g339816 !'##experimental_source clone p53-H-19, transformed hybridoma SV-80 cell !1line REFERENCE S42452 !$#authors Matlashewski, G.J.; Tuck, S.; Pim, D.; Lamb, P.; Schneider, !1J.; Crawford, L.V. !$#journal Mol. Cell. Biol. (1987) 7:961-963 !$#title Primary structure polymorphism at amino acid residue 72 of !1human p53. !$#cross-references MUID:87144273; PMID:3547088 !$#accession S42452 !'##molecule_type mRNA; DNA !'##residues 66-71,'P',73-79 ##label MKI2 !'##experimental_source clone lambda C113 !'##note 72-Cys was also found, and appears to represent a polymorphism !$#accession S42453 !'##molecule_type mRNA; DNA !'##residues 66-79 ##label MKI3 !'##experimental_source clone J6K REFERENCE I38082 !$#authors Farrell, P.J.; Allan, G.J.; Shanahan, F.; Vousden, K.H.; !1Crook, T. !$#journal EMBO J. (1991) 10:2879-2887 !$#title p53 is frequently mutated in Burkitt's lymphoma cell lines. !$#cross-references MUID:92007731; PMID:1915267 !$#accession I38082 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-189,'LLSILSEWKEICVWSIWMTETLFDIVWWCPMSRLRLALT', !1'VPPSTTTTCVTVPAWAA' ##label F01 !'##cross-references EMBL:X60010; NID:g506432; PIDN:CAA42625.1; !1PID:g506433 !'##note deletion of a C nucleotide causes a frameshift at position 566 !$#accession I38083 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-192,'R',194-393 ##label F02 !'##cross-references EMBL:X60011; NID:g506434; PIDN:CAA42626.1; !1PID:g506435 !$#accession I38084 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-393 ##label F03 !'##cross-references EMBL:X60012; NID:g506436; PIDN:CAA42627.1; !1PID:g506437 !$#accession I38085 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-245,'T',247-393 ##label F04 !'##cross-references EMBL:X60013; NID:g506438; PIDN:CAA42628.1; !1PID:g506439 !$#accession I38086 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-236,'I',238-393 ##label F05 !'##cross-references EMBL:X60014; NID:g506440; PIDN:CAA42629.1; !1PID:g506441 !$#accession I38087 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-247,'Q',249-393 ##label F06 !'##cross-references EMBL:X60015; NID:g506442; PIDN:CAA42630.1; !1PID:g506443 !$#accession I38088 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-71,'P',73-237,'Y',239-393 ##label F07 !'##cross-references EMBL:X60016; NID:g506444; PIDN:CAA42631.1; !1PID:g506445 !$#accession I38089 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-247,'Q',249-393 ##label F08 !'##cross-references EMBL:X60017; NID:g506446; PIDN:CAA42632.1; !1PID:g506447 !$#accession I38090 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-71,'P',73-162,'H',164-393 ##label F09 !'##cross-references EMBL:X60018; NID:g506448; PIDN:CAA42633.1; !1PID:g506449 !$#accession I38091 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-212,'Q',214-393 ##label F10 !'##cross-references EMBL:X60019; NID:g506450; PIDN:CAA42634.1; !1PID:g506451 !$#accession I38092 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-253,'D',255-393 ##label F11 !'##cross-references EMBL:X60020; NID:g506452; PIDN:CAA42635.1; !1PID:g506453 !'##note all sequences submitted to the EMBL/GenBank/DDBJ databases June !11991 REFERENCE I38093 !$#authors Futreal, P.A.; Barrett, J.C.; Wiseman, R.W. !$#journal Nucleic Acids Res. (1991) 19:6977 !$#title An Alu polymorphism intragenic to the TP53 gene. !$#cross-references MUID:92107726; PMID:1762941 !$#accession I38093 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-393 ##label FUT !'##cross-references EMBL:X54156; NID:g35213; PIDN:CAA38095.1; !1PID:g35214 REFERENCE A44905 !$#authors Yamada, Y.; Yoshida, T.; Hayashi, K.; Sekiya, T.; Yokota, !1J.; Hirohashi, S.; Nakatani, K.; Nakano, H.; Sugimura, T.; !1Terada, M. !$#journal Cancer Res. (1991) 51:5800-5805 !$#title p53 gene mutations in gastric cancer metastases and in !1gastric cancer cell lines derived from metastases. !$#cross-references MUID:92034678; PMID:1933850 !$#accession A44905 !'##molecule_type DNA !'##residues 246-247,'W',249-250 ##label YAM !'##cross-references GB:S63157; NID:g237829; PIDN:AAB20140.1; !1PID:g237830 !'##note sequence extracted from NCBI backbone (NCBIN:63157, !1NCBIP:63158) !'##note mutation from a liver metastasis of a gastric cancer REFERENCE I58354 !$#authors Hensel, C.H.; Xiang, R.H.; Sakaguchi, A.Y.; Naylor, S.L. !$#journal Oncogene (1991) 6:1067-1071 !$#title Use of the single strand conformation polymorphism technique !1and PCR to detect p53 gene mutations in small cell lung !1cancer. !$#cross-references MUID:91296386; PMID:1648702 !$#accession I58354 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 244-247,'W',249-252 ##label HEN1 !'##cross-references GB:S41969; NID:g1679931; PIDN:AAB19324.1; !1PID:g232814 !$#accession I78850 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 274-277,'S',279-282 ##label HEN2 !'##cross-references GB:S41977; NID:g1679932; PIDN:AAB19325.1; !1PID:g232816 REFERENCE I52681 !$#authors Chow, V.T.; Quek, H.H.; Tock, E.P.C. !$#journal Cancer Lett. (1993) 73:141-148 !$#title Alternative splicing of the p53 tumor suppressor gene in the !1Molt-4 T-lymphoblastic leukemia cell line. !$#cross-references MUID:94036762; PMID:8221626 !$#accession I52681 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 327-331,'DQTSFQKENC' ##label CHO !'##cross-references GB:S66666; NID:g436292; PIDN:AAB28601.1; !1PID:g436293 !'##note mutant sequence with altered splicing and termination expressed !1in Molt-4 T-lymphoblastic leukemia cells REFERENCE S60151 !$#authors Petersen, G.; Song, D.; Huegle-Doerr, B.; Oldenburg, I.; !1Bautz, E.K.F. !$#journal Mol. Gen. Genet. (1995) 249:425-431 !$#title Mapping of linear epitopes recognized by monoclonal !1antibodies with gene-fragment phage display libraries. !$#cross-references MUID:96133682; PMID:8552047 !$#accession S60153 !'##molecule_type DNA !'##residues 3-44 ##label PET REFERENCE A34371 !$#authors Dang, C.V.; Lee, W.M.F. !$#journal J. Biol. Chem. (1989) 264:18019-18023 !$#title Nuclear and nucleolar targeting sequences of c-erb-A, c-myb, !1N-myc, p53, HSP70, and HIV tat proteins. !$#cross-references MUID:90036876; PMID:2553699 !$#contents annotation; nuclear location signal REFERENCE A55059 !$#authors Addison, C.; Jenkins, J.R.; Stuerzbecher, H.W. !$#journal Oncogene (1990) 5:423-426 !$#title The p53 nuclear localisation signal is structurally linked !1to a p34(cdc2) kinase motif. !$#cross-references MUID:90191730; PMID:2156209 !$#contents annotation; nuclear location signal; phosphorylation REFERENCE A44683 !$#authors Samad, A.; Carroll, R.B. !$#journal Mol. Cell. Biol. (1991) 11:1598-1606 !$#title The tumor suppressor p53 is bound to RNA by a stable !1covalent linkage. !$#cross-references MUID:91141509; PMID:1705009 !$#contents annotation; RNA attachment and phosphorylation site REFERENCE A66760 !$#authors Cho, Y.; Gorina, S.; Jeffrey, P.; Pavletich, N. !$#submission submitted to the Brookhaven Protein Data Bank, July 1995 !$#cross-references PDB:1TSR !$#contents annotation; X-ray crystallography, 2.2 angstroms, residues !194-289 REFERENCE A66776 !$#authors Cho, Y.; Gorina, S.; Jeffrey, P.D.; Pavletich, N.P. !$#submission submitted to the Brookhaven Protein Data Bank, July 1995 !$#cross-references PDB:1TUP !$#contents annotation; X-ray crystallography, 2.2 angstroms, residues !194-289 REFERENCE A43072 !$#authors Cho, Y.; Gorina, S.; Jeffrey, P.D.; Pavletich, N.P. !$#journal Science (1994) 265:346-355 !$#title Crystal structure of a p53 tumor suppressor--DNA complex: !1understanding tumorigenic mutations. !$#cross-references MUID:94294806; PMID:8023157 !$#contents annotation; X-ray crystallography, 2.2 angstroms; !1DNA-binding core REFERENCE A43074 !$#authors Cariello, N.F.; Beroud, C.; Soussi, T. !$#journal Nucleic Acids Res. (1994) 22:3549-3550 !$#title Database and software for the analysis of mutations at the !1human p53 gene. !$#cross-references MUID:95023086; PMID:7937054 !$#contents annotation; database of mutations REFERENCE A43075 !$#authors Hollstein, M.; Rice, K.; Greenblatt, M.S.; Soussi, T.; !1Fuchs, R.; Soerlie, T.; Hovig, E.; Smith-Soerensen, B.; !1Montesano, R.; Harris, C.C. !$#journal Nucleic Acids Res. (1994) 22:3551-3555 !$#title Database of p53 gene somatic mutations in human tumors and !1cell lines. !$#cross-references MUID:95023087; PMID:7937055 !$#contents annotation; database of mutations REFERENCE A43078 !$#authors Merrick, B.A.; Pence, P.M.; He, C.; Patterson, R.M.; !1Selkirk, J.K. !$#journal BioTechniques (1995) 18:292-299 !$#title Phosphor image analysis of human p53 protein isoforms. !$#cross-references MUID:95244149; PMID:7727133 !$#contents annotation; phosphorylation sites COMMENT This protein plays an essential role in the regulation of !1cell division, as it is required for the transition from !1phase G0 to G1 of the cell cycle. COMMENT The tetramer association region may exhibit a beta-turn, !1beta-sheet, beta-turn, alpha-helix motif. GENETICS !$#gene GDB:TP53 !'##cross-references GDB:120445; OMIM:191170 !$#map_position 17p13.1-17p13.1 !$#introns 25/2; 32/3; 125/3; 187/1; 224/3; 261/2; 307/1; 331/3; 367/2 !$#note the first intron occurs before the initiator codon CLASSIFICATION #superfamily cellular tumor antigen p53 KEYWORDS apoptosis; cell division control; DNA binding; homotetramer; !1phosphoprotein; transcription regulation; tumor suppressor; !1zinc FEATURE !$1-43 #domain transcription activation #status predicted !8#label TRA\ !$13-23 #region conserved region I\ !$102-292 #domain DNA-binding core #status experimental #label !8DBC\ !$112-124 #region L1 loop\ !$117-142 #region conserved region II\ !$163-195 #region L2 loop\ !$171-181 #region conserved region III\ !$234-255 #region conserved region IV\ !$236-251 #region L3 loop\ !$270-286 #region conserved region V\ !$316-322 #region nuclear location signal\ !$322-360 #region tetramer association\ !$9,15,33 #binding_site phosphate (Ser) (covalent) (by casein !8kinase I) #status predicted\ !$20,37 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$176,179,238,242 #binding_site zinc (Cys, His, Cys, Cys) #status !8experimental\ !$315 #binding_site phosphate (Ser) (covalent) (by cdc2 !8kinase) #status predicted\ !$392 #binding_site phosphoryl-RNA (Ser) (covalent) #status !8experimental SUMMARY #length 393 #molecular-weight 43712 #checksum 4273 SEQUENCE /// ENTRY S06594 #type complete TITLE cellular tumor antigen p53 - green monkey ORGANISM #formal_name Cercopithecus aethiops #common_name green monkey, grivet DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S06594 REFERENCE S06594 !$#authors Rigaudy, P.; Eckhart, W. !$#journal Nucleic Acids Res. (1989) 17:8375 !$#title Nucleotide sequence of a cDNA encoding the monkey cellular !1phosphoprotein p53. !$#cross-references MUID:90045967; PMID:2530498 !$#accession S06594 !'##molecule_type mRNA !'##residues 1-393 ##label RIG !'##cross-references EMBL:X16384; NID:g22795; PIDN:CAA34420.1; !1PID:g22796 CLASSIFICATION #superfamily cellular tumor antigen p53 KEYWORDS apoptosis; cell division control; DNA binding; homotetramer; !1nucleus; phosphoprotein; transcription regulation; tumor !1suppressor; zinc FEATURE !$176,179,238,242 #binding_site zinc (Cys, His, Cys, Cys) #status !8predicted\ !$392 #binding_site phosphoryl-RNA (Ser) (covalent) #status !8predicted SUMMARY #length 393 #molecular-weight 43696 #checksum 4263 SEQUENCE /// ENTRY S51648 #type complete TITLE cellular tumor antigen p53 - bovine ALTERNATE_NAMES tumor-suppressor protein p53 ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S51648 REFERENCE S51648 !$#authors Dequiedt, F.; Willems, L.; Burny, A.; Kettmann, R. !$#submission submitted to the EMBL Data Library, September 1994 !$#description Nucleotide sequence of the ovine p53 tumor-suppressor gene !1cDNA and its genomic organisation. !$#accession S51648 !'##status preliminary !'##molecule_type mRNA !'##residues 1-386 ##label DEQ !'##cross-references EMBL:X81704; NID:g602332; PIDN:CAA57348.1; !1PID:g602333 CLASSIFICATION #superfamily cellular tumor antigen p53 KEYWORDS apoptosis; cell division control; DNA binding; homotetramer; !1phosphoprotein; transcription regulation; tumor suppressor; !1zinc FEATURE !$168,171,231,235 #binding_site zinc (Cys, His, Cys, Cys) #status !8predicted\ !$385 #binding_site phosphoryl-RNA (Ser) (covalent) #status !8predicted SUMMARY #length 386 #molecular-weight 43255 #checksum 7025 SEQUENCE /// ENTRY S02192 #type complete TITLE cellular tumor antigen p53 - rat ALTERNATE_NAMES gene p53 protein; nuclear oncoprotein p53 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S02192; S41149 REFERENCE S02192 !$#authors Soussi, T.; de Fromentel, C.C.; Breugnot, C.; May, E. !$#journal Nucleic Acids Res. (1988) 16:11384 !$#title Nucleotide sequence of a cDNA encoding the rat p53 nuclear !1oncoprotein. !$#cross-references MUID:89083585; PMID:3060862 !$#accession S02192 !'##molecule_type mRNA !'##residues 1-391 ##label SOU !'##cross-references EMBL:X13058; NID:g56828; PIDN:CAA31457.1; !1PID:g56829 REFERENCE S41149 !$#authors Hulla, J.E.; Schneider, R.P. !$#journal Nucleic Acids Res. (1993) 21:713-717 !$#title Structure of the rat p53 tumor suppressor gene. !$#cross-references MUID:93181268; PMID:8441680 !$#accession S41149 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-173,'W',175-391 ##label HUL !'##cross-references EMBL:L07909 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1992 GENETICS !$#introns 25/2; 32/3; 123/3; 185/1; 259/2; 305/1; 329/3; 365/2 CLASSIFICATION #superfamily cellular tumor antigen p53 KEYWORDS apoptosis; cell division control; DNA binding; homotetramer; !1nucleus; phosphoprotein; transcription regulation; tumor !1suppressor; zinc FEATURE !$174,177,236,240 #binding_site zinc (Cys, His, Cys, Cys) #status !8predicted\ !$390 #binding_site phosphoryl-RNA (Ser) (covalent) #status !8predicted SUMMARY #length 391 #molecular-weight 43451 #checksum 7105 SEQUENCE /// ENTRY DNMS53 #type complete TITLE cellular tumor antigen p53 - mouse ALTERNATE_NAMES oncoprotein p53 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 28-Aug-1985 #sequence_revision 04-Oct-1996 #text_change 11-May-2000 ACCESSIONS A22739; S06336; A02684; S38822; S38823; S40014; I48703 REFERENCE A22739 !$#authors Bienz, B.; Zakut-Houri, R.; Givol, D.; Oren, M. !$#journal EMBO J. (1984) 3:2179-2183 !$#title Analysis of the gene coding for the murine cellular tumour !1antigen p53. !$#cross-references MUID:85027173; PMID:6092064 !$#accession A22739 !'##molecule_type DNA !'##residues 1-134,'V',136-390 ##label BIE !'##cross-references GB:X00876; NID:g871420; PIDN:CAA25420.1; !1PID:g871421; GB:X01237; GB:K01700; NID:g53575; PID:g53576 REFERENCE S06336 !$#authors Chumakov, P.M. !$#journal Bioorg. Khim. (1987) 13:1691-1694 !$#title Primary structure of DNA complementary to murine oncoprotein !1p53 mRNA. !$#cross-references MUID:88221682; PMID:3329909 !$#accession S06336 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-134,'V',136-390 ##label CHU REFERENCE A02684 !$#authors Zakut-Houri, R.; Oren, M.; Bienz, B.; Lavie, V.; Hazum, S.; !1Givol, D. !$#journal Nature (1983) 306:594-597 !$#title A single gene and a pseudogene for the cellular tumour !1antigen p53. !$#cross-references MUID:84068204; PMID:6646235 !$#accession A02684 !'##molecule_type mRNA !'##residues 1-159,'H',161-167,'G',169-233,'I',235-390 ##label ZAK !'##cross-references GB:X01237; GB:K01700; NID:g53575 REFERENCE S38822 !$#authors Arai, N.; Nomura, D.; Yokota, K.; Wolf, D.; Brill, E.; !1Shohat, O.; Rotter, V. !$#journal Mol. Cell. Biol. (1986) 6:3232-3239 !$#title Immunologically distinct p53 molecules generated by !1alternative splicing. !$#cross-references MUID:87064640; PMID:3023970 !$#accession S38822 !'##molecule_type mRNA !'##residues 1-390 ##label ARA1 !'##cross-references EMBL:M13872; NID:g200198; PIDN:AAA39881.1; !1PID:g200199 !$#accession S38823 !'##molecule_type mRNA !'##residues 1-167,'G',169-233,'I',235-390 ##label ARA2 !'##cross-references EMBL:M13873 REFERENCE S40014 !$#authors Arai, N.; Nomura, D.; Yokota, K.; Wolf, D.; Brill, E.; !1Shohat, O.; Rotter, V. !$#submission submitted to the EMBL Data Library, July 1988 !$#accession S40014 !'##molecule_type mRNA !'##residues 1-167,'G',169-390 ##label ARA3 !'##cross-references EMBL:M13873; NID:g200200; PIDN:AAA39882.1; !1PID:g200201 REFERENCE I48703 !$#authors Jenkins, J.R.; Rudge, K.; Redmond, S.; Wade-Evans, A. !$#journal Nucleic Acids Res. (1984) 12:5609-5626 !$#title Cloning and expression analysis of full length mouse cDNA !1sequences encoding the transformation associated protein !1p53. !$#cross-references MUID:84272240; PMID:6379601 !$#accession I48703 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-47,'R',49-78,'QW',82-390 ##label RES !'##cross-references EMBL:X00741; NID:g53570; PIDN:CAA25323.1; !1PID:g53571 COMMENT This DNA-binding protein plays an essential role in the !1regulation of cell division, as it is required for the !1transition from phase G0 to G1 of the cell cycle. COMMENT The tetramer association region may exhibit a beta-turn, !1beta-sheet, beta-turn, alpha-helix motif. CLASSIFICATION #superfamily cellular tumor antigen p53 KEYWORDS apoptosis; cell division control; DNA binding; homotetramer; !1phosphoprotein; transcription regulation; tumor suppressor; !1zinc FEATURE !$1-44 #domain transcription activation #status predicted !8#label TRA\ !$16-26 #region conserved region I\ !$99-289 #domain DNA-binding core #status predicted #label !8DBC\ !$108-121 #region L1 loop\ !$114-139 #region conserved region II\ !$160-192 #region L2 loop\ !$168-178 #region conserved region III\ !$231-252 #region conserved region IV\ !$233-248 #region L3 loop\ !$267-283 #region conserved region V\ !$313-319 #region nuclear location signal\ !$319-357 #region tetramer association\ !$7,9,12,18,23,37 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$173,176,235,239 #binding_site zinc (Cys, His, Cys, Cys) #status !8predicted\ !$312 #binding_site phosphate (Ser) (covalent) (by cdc2 !8kinase) #status predicted\ !$389 #binding_site phosphoryl-RNA (Ser) (covalent) #status !8predicted SUMMARY #length 390 #molecular-weight 43458 #checksum 1260 SEQUENCE /// ENTRY JH0633 #type complete TITLE cellular tumor antigen p53 - golden hamster ALTERNATE_NAMES tumor-suppressor protein p53 ORGANISM #formal_name Mesocricetus auratus #common_name golden hamster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JH0633 REFERENCE JH0633 !$#authors Legros, Y.; McIntyre, P.; Soussi, T. !$#journal Gene (1992) 112:247-250 !$#title The cDNA cloning and immunological characterization of !1hamster p53. !$#cross-references MUID:92210007; PMID:1555773 !$#accession JH0633 !'##molecule_type mRNA !'##residues 1-396 ##label LEG !'##cross-references GB:M75144; NID:g191414; PIDN:AAA37085.1; !1PID:g191415 !'##experimental_source kidney, strain MP1 GENETICS !$#gene p53 CLASSIFICATION #superfamily cellular tumor antigen p53 KEYWORDS apoptosis; cell division control; DNA binding; homotetramer; !1nucleus; phosphoprotein; transcription regulation; tumor !1suppressor; zinc FEATURE !$179,182,241,245 #binding_site zinc (Cys, His, Cys, Cys) #status !8predicted\ !$395 #binding_site phosphoryl-RNA (Ser) (covalent) #status !8predicted SUMMARY #length 396 #molecular-weight 43631 #checksum 6617 SEQUENCE /// ENTRY S02193 #type complete TITLE cellular tumor antigen p53 - chicken ALTERNATE_NAMES nuclear oncoprotein p53 ORGANISM #formal_name Gallus gallus #common_name chicken DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S02193 REFERENCE S02193 !$#authors Soussi, T.; Begue, A.; Kress, M.; Stehelin, D.; May, P. !$#journal Nucleic Acids Res. (1988) 16:11383 !$#title Nucleotide sequence of a cDNA encoding the chicken p53 !1nuclear oncoprotein. !$#cross-references MUID:89083584; PMID:3060861 !$#accession S02193 !'##molecule_type mRNA !'##residues 1-367 ##label SOU !'##cross-references EMBL:X13057; NID:g63740; PIDN:CAA31456.1; !1PID:g63741 CLASSIFICATION #superfamily cellular tumor antigen p53 KEYWORDS apoptosis; cell division control; DNA binding; homotetramer; !1nucleus; phosphoprotein; transcription regulation; tumor !1suppressor; zinc FEATURE !$161,164,224,228 #binding_site zinc (Cys, His, Cys, Cys) #status !8predicted\ !$366 #binding_site phosphoryl-RNA (Ser) (covalent) #status !8predicted SUMMARY #length 367 #molecular-weight 40169 #checksum 5094 SEQUENCE /// ENTRY A29376 #type complete TITLE cellular tumor antigen p53 - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A29376; S61531; S72313; I51639 REFERENCE A29376 !$#authors Soussi, T.; de Fromentel, C.C.; Mechali, M.; May, P.; Kress, !1M. !$#journal Oncogene (1987) 1:71-78 !$#title Cloning and characterization of a cDNA from Xenopus laevis !1coding for a protein homologous to human and murine p53. !$#cross-references MUID:88143684; PMID:2830576 !$#accession A29376 !'##molecule_type mRNA !'##residues 1-363 ##label SOU !'##cross-references EMBL:X05191; NID:g64961; PIDN:CAA28821.1; !1PID:g64962 REFERENCE I51639 !$#authors Hoever, M.; Clement, J.H.; Wedlich, D.; Montenarh, M.; !1Knoechel, W. !$#journal Oncogene (1994) 9:109-120 !$#title Overexpression of wild-type p53 interferes with normal !1development in Xenopus laevis embryos. !$#cross-references MUID:94134403; PMID:8302570 !$#accession S61531 !'##molecule_type mRNA !'##residues 1-293,295-363 ##label HOE !'##cross-references EMBL:X77546; NID:g468513; PIDN:CAA54672.1; !1PID:g468514 REFERENCE S72313 !$#authors Hoever, M.; Clement, J.; Wedlich, D.; Montenarh, M.; !1Knochel, W. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S72313 !'##molecule_type mRNA !'##residues 1-51,'S',53-70,72-293,295-363 ##label HOW !'##cross-references EMBL:X77546; NID:g468513; PIDN:CAA54672.1; !1PID:g468514 GENETICS !$#gene p53 CLASSIFICATION #superfamily cellular tumor antigen p53 KEYWORDS apoptosis; cell division control; DNA binding; homotetramer; !1nucleus; phosphoprotein; transcription regulation; tumor !1suppressor; zinc FEATURE !$150,153,213,217 #binding_site zinc (Cys, His, Cys, Cys) #status !8predicted\ !$362 #binding_site phosphoryl-RNA (Ser) (covalent) #status !8predicted SUMMARY #length 363 #molecular-weight 40692 #checksum 6648 SEQUENCE /// ENTRY JH0631 #type complete TITLE cellular tumor antigen p53 - rainbow trout ORGANISM #formal_name Oncorhynchus mykiss #common_name rainbow trout DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JH0631 REFERENCE JH0631 !$#authors de Fromentel, C.C.; Pakdel, F.; Chapus, A.; Baney, C.; May, !1P.; Soussi, T. !$#journal Gene (1992) 112:241-245 !$#title Rainbow trout p53: cDNA cloning and biochemical !1characterization. !$#cross-references MUID:92210006; PMID:1339362 !$#accession JH0631 !'##molecule_type mRNA !'##residues 1-396 ##label DEF !'##cross-references GB:M75145; NID:g213828; PIDN:AAA49605.1; !1PID:g213829 !'##experimental_source liver COMMENT This protein is the product of a tumor suppressor gene, p53, !1whose inactivation leads to cell transformation or !1neophasia. CLASSIFICATION #superfamily cellular tumor antigen p53 KEYWORDS apoptosis; cell division control; DNA binding; homotetramer; !1nucleus; phosphoprotein; transcription regulation; tumor !1suppressor; zinc FEATURE !$164,167,227,231 #binding_site zinc (Cys, His, Cys, Cys) #status !8predicted\ !$395 #binding_site phosphoryl-RNA (Ser) (covalent) #status !8predicted SUMMARY #length 396 #molecular-weight 43966 #checksum 9018 SEQUENCE /// ENTRY WMHUET #type complete TITLE proliferating cell nuclear antigen - human ALTERNATE_NAMES cyclin; PCNA ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 22-Jun-1999 ACCESSIONS A27445; A27250; A33051 REFERENCE A27445 !$#authors Almendral, J.M.; Huebsch, D.; Blundell, P.A.; !1Macdonald-Bravo, H.; Bravo, R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:1575-1579 !$#title Cloning and sequence of the human nuclear protein cyclin: !1homology with DNA-binding proteins. !$#cross-references MUID:87175520; PMID:2882507 !$#accession A27445 !'##molecule_type mRNA !'##residues 1-261 ##label ALM !'##cross-references GB:M15796; NID:g181271; PIDN:AAA35736.1; !1PID:g181272 REFERENCE A27250 !$#authors Prelich, G.; Kostura, M.; Marshak, D.R.; Mathews, M.B.; !1Stillman, B. !$#journal Nature (1987) 326:471-475 !$#title The cell-cycle regulated proliferating cell nuclear antigen !1is required for SV40 DNA replication in vitro. !$#cross-references MUID:87173009; PMID:2882422 !$#accession A27250 !'##molecule_type protein !'##residues 1-26 ##label PRE !'##experimental_source 293 cells REFERENCE A33051 !$#authors Travali, S.; Ku, D.H.; Rizzo, M.G.; Ottavio, L.; Baserga, !1R.; Calabretta, B. !$#journal J. Biol. Chem. (1989) 264:7466-7472 !$#title Structure of the human gene for the proliferating cell !1nuclear antigen. !$#cross-references MUID:89214190; PMID:2565339 !$#accession A33051 !'##status preliminary; translation not shown; translated from GB/EMBL/ !1DDBJ !'##molecule_type DNA !'##residues 1-261 ##label TRA !'##cross-references GB:J04718; NID:g189681; PIDN:AAA60040.1; !1PID:g387005 COMMENT This protein, an auxiliary protein of DNA polymerase delta, !1is involved in DNA replication. GENETICS !$#gene GDB:PCNA !'##cross-references GDB:120261; OMIM:176740 !$#map_position 20pter-20p12 !$#introns 74/2; 107/1; 129/3; 194/3; 236/1 CLASSIFICATION #superfamily proliferating cell nuclear antigen KEYWORDS DNA binding; DNA replication; nucleus SUMMARY #length 261 #molecular-weight 28768 #checksum 5983 SEQUENCE /// ENTRY WMRTET #type complete TITLE proliferating cell nuclear antigen - rat ALTERNATE_NAMES cyclin; PCNA ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 28-May-1999 ACCESSIONS A26631 REFERENCE A26631 !$#authors Matsumoto, K.; Moriuchi, T.; Koji, T.; Nakane, P.K. !$#journal EMBO J. (1987) 6:637-642 !$#title Molecular cloning of cDNA coding for rat proliferating cell !1nuclear antigen (PCNA)/cyclin. !$#cross-references MUID:87218522; PMID:2884104 !$#accession A26631 !'##molecule_type mRNA !'##residues 1-261 ##label MAT !'##cross-references GB:Y00047; GB:M24604; NID:g56861; PIDN:CAA68261.1; !1PID:g56862 COMMENT This protein, an auxiliary protein of DNA polymerase delta, !1is involved in DNA replication. CLASSIFICATION #superfamily proliferating cell nuclear antigen KEYWORDS DNA binding; DNA replication; nucleus SUMMARY #length 261 #molecular-weight 28748 #checksum 5315 SEQUENCE /// ENTRY WMMS #type complete TITLE proliferating cell nuclear antigen - mouse ALTERNATE_NAMES cyclin; DNA-directed DNA polymerase delta auxiliary protein ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Jun-1992 #sequence_revision 30-Jun-1993 #text_change 01-Dec-2000 ACCESSIONS S15703; I48707; A60858; S11726 REFERENCE S15703 !$#authors Yamaguchi, M.; Hayashi, Y.; Hirose, F.; Matsuoka, S.; !1Moriuchi, T.; Shiroishi, T.; Moriwaki, K.; Matsukage, A. !$#journal Nucleic Acids Res. (1991) 19:2403-2410 !$#title Molecular cloning and structural analysis of mouse gene and !1pseudogenes for proliferating cell nuclear antigen. !$#cross-references MUID:91252282; PMID:1674997 !$#accession S15703 !'##molecule_type DNA !'##residues 1-261 ##label YAM !'##cross-references EMBL:X57800; NID:g53601; PIDN:CAA40938.1; !1PID:g53602 !'##note the authors translated the codon ATA for residue 137 as Val REFERENCE I48707 !$#authors Shipman-Appasamy, P.M.; Cohen, K.S.; Prystowsky, M.B. !$#journal DNA Seq. (1991) 2:181-191 !$#title Nucleotide sequence of murine PCNA: interspecies comparison !1of the cDNA and the 5' flanking region of the gene. !$#cross-references MUID:92297962; PMID:1726365 !$#accession I48707 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-66,'T',68-261 ##label SHI1 !'##cross-references EMBL:X53068; NID:g53599; PIDN:CAA37243.1; !1PID:g53600 !'##note submitted to the EMBL Data Library, May 1990 REFERENCE A60858 !$#authors Shipman, P.M.; Sabath, D.E.; Fischer, A.H.; Comber, P.G.; !1Sullivan, K.; Tan, E.M.; Prystowsky, M.B. !$#journal J. Cell. Biochem. (1988) 38:189-198 !$#title Cyclin mRNA and protein expression in recombinant !1interleukin 2-stimulated cloned murine T lymphocytes. !$#cross-references MUID:89155592; PMID:2906640 !$#accession A60858 !'##status translation not shown !'##molecule_type mRNA !'##residues 'LES',6-42 ##label SHI2 GENETICS !$#introns 74/2; 107/1; 129/3; 194/3; 236/1 CLASSIFICATION #superfamily proliferating cell nuclear antigen KEYWORDS DNA binding; DNA replication; nucleus SUMMARY #length 261 #molecular-weight 28785 #checksum 5452 SEQUENCE /// ENTRY WMZPET #type complete TITLE proliferating cell nuclear antigen [validated] - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES cyclin; DNA-directed DNA polymerase delta accessory protein ORGANISM #formal_name Schizosaccharomyces pombe DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 26-May-2000 ACCESSIONS S28053; T39573 REFERENCE S28053 !$#authors Waseem, N.H.; Labib, K.; Nurse, P.; Lane, D.P. !$#journal EMBO J. (1992) 11:5111-5120 !$#title Isolation and analysis of the fission yeast gene encoding !1polymerase delta accessory protein PCNA. !$#cross-references MUID:93099886; PMID:1361173 !$#accession S28053 !'##molecule_type DNA !'##residues 1-260 ##label WAS !'##cross-references EMBL:X54857; NID:g5002; PIDN:CAA38636.1; PID:g5003 REFERENCE Z21864 !$#authors Wood, V.; Rajandream, M.A.; Barrell, B.G.; Brown, D.; !1Churcher, C.M. !$#submission submitted to the EMBL Data Library, March 1999 !$#accession T39573 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-260 ##label WOO !'##cross-references EMBL:AL035637; PIDN:CAB38513.1; GSPDB:GN00067; !1SPDB:SPBC16D10.09 !'##experimental_source strain 972h-; cosmid c16D10 GENETICS !$#gene pcn1; SPBC16D10.09 !$#map_position 2 !$#introns 27/3 FUNCTION !$#description involved in nucleic acid metabolism and cell-cycle control !1[validated, MUID:99380549] !$#note seems to encircle DNA and tether the polymerase to the DNA !1template for processive DNA synthesis CLASSIFICATION #superfamily proliferating cell nuclear antigen KEYWORDS DNA binding; DNA replication; nucleus SUMMARY #length 260 #molecular-weight 28968 #checksum 2714 SEQUENCE /// ENTRY WMBYET #type complete TITLE proliferating cell nuclear antigen - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES cyclin; DNA-directed DNA polymerase delta auxiliary protein; protein YBR0811; protein YBR088c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 05-Nov-1999 ACCESSIONS S22851; S30599; S48256; S45956; S44671 REFERENCE S22851 !$#authors Bauer, G.A.; Burgers, P.M.J. !$#journal Nucleic Acids Res. (1990) 18:261-265 !$#title Molecular cloning, structure and expression of the yeast !1proliferating cell nuclear antigen gene. !$#cross-references MUID:90221805; PMID:1970160 !$#accession S22851 !'##molecule_type DNA !'##residues 1-258 ##label BAU1 !'##cross-references EMBL:X16676; NID:g4192; PIDN:CAA34664.1; PID:g4193 !$#accession S30599 !'##molecule_type protein !'##residues 1-41;231-240 ##label BAU2 REFERENCE S48255 !$#authors Mannhaupt, G.; Stucka, R.; Ehnle, S.; Vetter, I.; Feldmann, !1H. !$#journal Yeast (1994) 10:1363-1381 !$#title Analysis of a 70 kb region on the right arm of yeast !1chromosome II. !$#cross-references MUID:95208357; PMID:7900426 !$#accession S48256 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-258 ##label MAN !'##cross-references EMBL:X78993; NID:g476045; PIDN:CAA55594.1; !1PID:g476047 REFERENCE S45927 !$#authors Feldmann, H.; Mannhaupt, G.; Schwarzlose, C.; Vetter, I. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S45956 !'##molecule_type DNA !'##residues 1-258 ##label FE2 !'##cross-references EMBL:Z35957; NID:g536355; PIDN:CAA85038.1; !1PID:g536356; GSPDB:GN00002; MIPS:YBR088c GENETICS !$#gene SGD:POL30; MIPS:YBR088c !'##cross-references SGD:S0000292; MIPS:YBR088c !$#map_position 2R CLASSIFICATION #superfamily proliferating cell nuclear antigen KEYWORDS DNA binding; DNA replication; nucleus FEATURE !$1-258 #product proliferating cell nuclear antigen #status !8experimental #label MAT SUMMARY #length 258 #molecular-weight 28916 #checksum 4149 SEQUENCE /// ENTRY WMNVET #type complete TITLE EcoRI-T large (ETL) Ac-pcna protein - Autographa californica nuclear polyhedrosis virus ALTERNATE_NAMES proliferating cell nuclear antigen ORGANISM #formal_name Autographa californica nuclear polyhedrosis virus, AcMNPV DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 24-Nov-1999 ACCESSIONS A28147; A72856 REFERENCE A93034 !$#authors Crawford, A.M.; Miller, L.K. !$#journal J. Virol. (1988) 62:2773-2781 !$#title Characterization of an early gene accelerating expression of !1late genes of the baculovirus Autographa californica nuclear !1polyhedrosis virus. !$#cross-references MUID:88275045; PMID:3292791 !$#accession A28147 !'##molecule_type DNA !'##residues 1-256 ##label CRA !'##cross-references GB:M20718; NID:g332418; PIDN:AAA21097.1; !1PID:g332419 REFERENCE A72850 !$#authors Ayres, M.D.; Howard, S.C.; Kuzio, J.; Lopez-Ferber, M.; !1Possee, R.D. !$#journal Virology (1994) 202:586-605 !$#title The complete DNA sequence of Autographa californica nuclear !1polyhedrosis virus. !$#cross-references MUID:94303173; PMID:8030224 !$#accession A72856 !'##status preliminary !'##molecule_type DNA !'##residues 1-256 ##label AYR !'##cross-references GB:L22858; NID:g510708; PIDN:AAA66679.2; !1PID:g4376186 COMMENT This protein is related to mammalian proliferating cell !1nuclear antigen (PCNA, cyclin), which is involved in DNA !1replication. GENETICS !$#gene Ac-pcna CLASSIFICATION #superfamily proliferating cell nuclear antigen KEYWORDS DNA binding; DNA replication; early protein; nucleus SUMMARY #length 256 #molecular-weight 28635 #checksum 1274 SEQUENCE /// ENTRY A40457 #type complete TITLE replication protein A1 - human ALTERNATE_NAMES replication protein A 70K chain ORGANISM #formal_name Homo sapiens #common_name man DATE 28-Feb-1992 #sequence_revision 27-Oct-1995 #text_change 07-May-1999 ACCESSIONS A40457; A44501 REFERENCE A40457 !$#authors Erdile, L.F.; Heyer, W.D.; Kolodner, R.; Kelly, T.J. !$#journal J. Biol. Chem. (1991) 266:12090-12098 !$#title Characterization of a cDNA encoding the 70-kDa !1single-stranded DNA-binding subunit of human replication !1protein A and the role of the protein in DNA replication. !$#cross-references MUID:91268092; PMID:2050703 !$#accession A40457 !'##molecule_type mRNA !'##residues 1-216,'A',218-616 ##label ERD !'##cross-references GB:M63488 !'##note parts of the sequence determined by protein sequencing !'##note this sequence has been corrected in reference A44501 REFERENCE A44501 !$#authors Erdile, L.F.; Heyer, W.D.; Kolodner, R.; Kelly, T.J. !$#journal J. Biol. Chem. (1993) 268:2268 !$#title Characterization of a cDNA encoding the 70-kDa !1single-stranded DNA-binding subunit of human replication !1protein A and the role of the protein in DNA replication. !$#cross-references MUID:93131993; PMID:8420996 !$#accession A44501 !'##molecule_type mRNA !'##residues 217 ##label ER2 !'##cross-references GB:M63488 !'##note sequence correction GENETICS !$#gene GDB:RPA1 !'##cross-references GDB:138362; OMIM:179835 !$#map_position 17p13.3-17p13.3 COMPLEX Replication protein A is a trimer of 70K (A1), 32K (A2), and !114K (A3) chains. FUNCTION !$#description probable eukaryotic equivalent of prokaryotic !1single-stranded DNA-binding proteins, having a role in the !1generation of a single-stranded region before the initiation !1of DNA synthesis; probably also has a role in the elongation !1stage of DNA replication !$#pathway DNA replication initiation !$#note the single-stranded DNA-binding activity resides in the A1 !1protein CLASSIFICATION #superfamily replication protein A1 KEYWORDS DNA replication initiation; single-stranded DNA binding; !1trimer; zinc finger FEATURE !$481-503 #region zinc finger CCCC motif SUMMARY #length 616 #molecular-weight 68138 #checksum 9273 SEQUENCE /// ENTRY A43458 #type complete TITLE replication protein A1 - African clawed frog ALTERNATE_NAMES replication protein A 70K chain ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 10-Jun-1993 #sequence_revision 27-Oct-1995 #text_change 22-Jun-1999 ACCESSIONS A43458; S24638 REFERENCE A43458 !$#authors Adachi, Y.; Laemmli, U.K. !$#journal J. Cell Biol. (1992) 119:1-15 !$#title Identification of nuclear pre-replication centers poised for !1DNA synthesis in Xenopus egg extracts: immunolocalization !1study of replication protein A. !$#cross-references MUID:92407024; PMID:1527163 !$#accession A43458 !'##molecule_type mRNA; protein !'##residues 1-609 ##label ADA !'##cross-references EMBL:X67240; NID:g65065; PIDN:CAA47665.1; !1PID:g65066 !'##experimental_source oocyte !'##note sequence extracted from NCBI backbone (NCBIN:113390, !1NCBIP:113391) !'##note parts of the sequence determined by protein sequencing COMPLEX Replication protein A is a trimer of 70K (A1), 32K (A2), and !114K (A3) chains. FUNCTION !$#description thought to be the eukaryotic equivalent of prokaryotic !1single-stranded DNA-binding proteins and to play a role in !1the generation of a single-stranded region before the !1initiation of DNA synthesis !$#pathway DNA replication initiation CLASSIFICATION #superfamily replication protein A1 KEYWORDS DNA replication initiation; single-stranded DNA binding; !1trimer; zinc finger FEATURE !$472-494 #region zinc finger CCCC motif SUMMARY #length 609 #molecular-weight 67085 #checksum 3900 SEQUENCE /// ENTRY S20145 #type complete TITLE replication factor A chain 1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES DNA-binding protein RPA1; protein YAR007c; URS1 site-binding complex 70K chain BUF2 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S20145; A37281; E37281; S40902; B54695 REFERENCE S20145 !$#authors Heyer, W.D.; Rao, M.R.S.; Erdile, L.F.; Kelly, T.J.; !1Kolodner, R.D. !$#journal EMBO J. (1990) 9:2321-2329 !$#title An essential Saccharomyces cerevisiae single-stranded DNA !1binding protein is homologous to the large subunit of human !1RP-A. !$#cross-references MUID:90291999; PMID:2192864 !$#accession S20145 !'##molecule_type DNA !'##residues 1-621 ##label HEY !'##cross-references EMBL:M60262; NID:g172465; PIDN:AAA34994.1; !1PID:g172466 REFERENCE A37281 !$#authors Brill, S.J.; Stillman, B. !$#journal Genes Dev. (1991) 5:1589-1600 !$#title Replication factor-A from Saccharomyces cerevisiae is !1encoded by three essential genes coordinately expressed at S !1phase. !$#cross-references MUID:91357474; PMID:1885001 !$#accession A37281 !'##molecule_type DNA !'##residues 1-621 ##label BRI !'##cross-references GB:X59748; NID:g4311; PIDN:CAA42420.1; PID:g4312 !$#accession E37281 !'##molecule_type protein !'##residues 111-129;495-503 ##label BR2 REFERENCE S40891 !$#authors Clark, M.W.; Keng, T.; Storms, R.K.; Zhong, W.; Fortin, N.; !1Zeng, B.; Delaney, S.; Ouellette, F.B.; Barton, A.B.; !1Kaback, D.B.; Bussey, H. !$#submission submitted to the EMBL Data Library, November 1993 !$#description Sequencing of chromosome I of Saccharomyces cerevisiae: !1Analysis of the 42 Kbp SP07-CENI-CDC15 REGION. !$#accession S40902 !'##molecule_type DNA !'##residues 1-621 ##label CLA !'##cross-references EMBL:L22015; NID:g1339990; PIDN:AAC04960.1; !1PID:g349752; GSPDB:GN00001; MIPS:YAR007c REFERENCE A54695 !$#authors Luche, R.M.; Smart, W.C.; Marion, T.; Tillman, M.; Sumrada, !1R.A.; Cooper, T.G. !$#journal Mol. Cell. Biol. (1993) 13:5749-5761 !$#title Saccharomyces cerevisiae BUF protein binds to sequences !1participating in DNA replication in addition to those !1mediating transcriptional repression (URS1) and activation. !$#cross-references MUID:93361008; PMID:8355713 !$#accession B54695 !'##molecule_type DNA !'##residues 1-621 ##label LUC !'##cross-references GB:S64901; NID:g410540; PIDN:AAB27889.1; !1PID:g410541 GENETICS !$#gene SGD:RFA1; RPA1; BUF2; FUN3; MIPS:YAR007c !'##cross-references SGD:S0000065; MIPS:YAR007c !$#map_position 1R CLASSIFICATION #superfamily replication protein A1 KEYWORDS DNA binding; DNA replication; heterotrimer; nucleus; zinc !1finger FEATURE !$486-508 #region zinc finger SUMMARY #length 621 #molecular-weight 70347 #checksum 8323 SEQUENCE /// ENTRY DNECTS #type complete TITLE terminator sequence-binding protein tus - Escherichia coli (strain K-12) ALTERNATE_NAMES DNA replication terminus site-binding protein; DNA replication terminus site-binding protein / DNA sequence-specific contrahelicase; tau protein; ter-binding protein ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 01-Mar-2002 ACCESSIONS B32161; A34182; D64917; JT0527 REFERENCE A32161 !$#authors Hill, T.M.; Tecklenburg, M.L.; Pelletier, A.J.; Kuempel, !1P.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:1593-1597 !$#title tus, the trans-acting gene required for termination of DNA !1replication in Escherichia coli, encodes a DNA-binding !1protein. !$#cross-references MUID:89160822; PMID:2646639 !$#accession B32161 !'##molecule_type DNA !'##residues 1-309 ##label HIL !'##cross-references GB:D90037; GB:J04507; GB:J05139; NID:g216670; !1PIDN:BAA14085.1; PID:g216671 REFERENCE A34182 !$#authors Hidaka, M.; Kobayashi, T.; Takenaka, S.; Takeya, H.; !1Horiuchi, T. !$#journal J. Biol. Chem. (1989) 264:21031-21037 !$#title Purification of a DNA replication terminus (ter) !1site-binding protein in Escherichia coli and identification !1of the structural gene. !$#cross-references MUID:90078195; PMID:2687269 !$#accession A34182 !'##molecule_type DNA !'##residues 1-309 ##label HID !'##cross-references GB:D90037; GB:J04507; GB:J05139; NID:g216670; !1PIDN:BAA14085.1; PID:g216671 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64917 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-309 ##label BLAT !'##cross-references GB:AE000256; GB:U00096; NID:g1787888; !1PIDN:AAC74682.1; PID:g1787895; UWGP:b1610 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene tus; tau !$#map_position 36 min FUNCTION !$#description one of the components of the DNA replication termination !1mechanism; it binds to DNA replication terminator sequences !1to prevent the passage of replication forks; the termination !1efficiency will be affected by the affinity of this protein !1for the terminator sequence CLASSIFICATION #superfamily terminator sequence-binding protein tus KEYWORDS DNA binding; DNA replication termination SUMMARY #length 309 #molecular-weight 35783 #checksum 2321 SEQUENCE /// ENTRY DNEC17 #type complete TITLE outer membrane protein hlpA precursor - Escherichia coli (strain K-12) ALTERNATE_NAMES DNA-binding 17K protein; histone-like protein hlp ORGANISM #formal_name Escherichia coli DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 01-Mar-2002 ACCESSIONS JT0304; A38063; S13728; B64742; I54944; S20426 REFERENCE JT0304 !$#authors Holck, A.; Kleppe, K. !$#journal Gene (1988) 67:117-124 !$#title Cloning and sequencing of the gene for the DNA-binding 17K !1protein of Escherichia coli. !$#cross-references MUID:88329735; PMID:2843433 !$#accession JT0304 !'##molecule_type DNA !'##residues 1-161 ##label HO1 !'##cross-references GB:M21118; NID:g147821; PIDN:AAA24630.1; !1PID:g147822 !$#accession A38063 !'##molecule_type protein !'##residues 21-30 ##label HO2 !'##experimental_source strain B REFERENCE S13728 !$#authors Dicker, I.B.; Seetharam, S. !$#journal J. Bacteriol. (1991) 173:334-344 !$#title Cloning and nucleotide sequence of the firA gene and the !1firA200(Ts) allele from Escherichia coli. !$#cross-references MUID:91100302; PMID:1987124 !$#accession S13728 !'##status preliminary !'##molecule_type DNA !'##residues 72-161 ##label DIC !'##cross-references EMBL:X54797; NID:g41468; PIDN:CAA38567.1; !1PID:g41469 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64742 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-161 ##label BLAT !'##cross-references GB:AE000127; GB:U00096; NID:g1786370; !1PIDN:AAC73289.1; PID:g1786375; UWGP:b0178 !'##experimental_source strain K-12, substrain MG1655 REFERENCE I54944 !$#authors Hirvas, L.; Koski, P.; Vaara, M. !$#journal J. Bacteriol. (1991) 173:1223-1229 !$#title The ompH gene of Yersinia enterocolitica: cloning, !1sequencing, expression, and comparison with known !1enterobacterial ompH sequences. !$#cross-references MUID:91123198; PMID:1991717 !$#accession I54944 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-14,'L',16-148,'E',150-152,'I',154-161 ##label RES !'##cross-references EMBL:X75465; NID:g432661; PIDN:CAA53207.1; !1PID:g432662 COMMENT The hlpA protein has been believed to be a histone-like !1constituent of bacterial chromatin; it is uncertain if the !1protein binds DNA in vivo. GENETICS !$#gene hlpA; skp CLASSIFICATION #superfamily DNA-binding 17K protein KEYWORDS membrane protein FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-161 #product outer membrane protein hlpA #status !8predicted #label MAT SUMMARY #length 161 #molecular-weight 17688 #checksum 5496 SEQUENCE /// ENTRY S09104 #type complete TITLE outer membrane protein ompH precursor - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JQ0528; A34432; A37083; S09104 REFERENCE JQ0528 !$#authors Koski, P.; Hirvas, L.; Vaara, M. !$#journal Gene (1990) 88:117-120 !$#title Complete sequence of the ompH gene encoding the 16-kDa !1cationic outer membrane protein of Salmonella typhimurium. !$#cross-references MUID:90255961; PMID:2187745 !$#accession JQ0528 !'##molecule_type DNA !'##residues 1-161 ##label KOS !'##cross-references GB:J05101; GB:M36486; NID:g154209; PIDN:AAA27170.1; !1PID:g154210 !'##experimental_source strain SH5014 REFERENCE A34432 !$#authors Koski, P.; Rhen, M.; Kantele, J.; Vaara, M. !$#journal J. Biol. Chem. (1989) 264:18973-18980 !$#title Isolation, cloning, and primary structure of a cationic !116-kDa outer membrane protein of Salmonella typhimurium. !$#cross-references MUID:90037020; PMID:2681205 !$#accession A34432 !'##status preliminary !'##molecule_type DNA !'##residues 8-161 ##label KO2 !'##cross-references GB:J05101; GB:M36486 REFERENCE A37083 !$#authors Hirvas, L.; Koski, P.; Vaara, M. !$#journal Biochem. Biophys. Res. Commun. (1990) 173:53-59 !$#title Primary structure and expression of the Ssc-protein of !1Salmonella typhimurium. !$#cross-references MUID:91076898; PMID:2256935 !$#accession A37083 !'##status preliminary !'##molecule_type DNA !'##residues 98-161 ##label HI2 !'##cross-references GB:M35193 GENETICS !$#gene ompH !$#start_codon GTG CLASSIFICATION #superfamily DNA-binding 17K protein KEYWORDS membrane protein FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-161 #product outer membrane protein ompH #status !8predicted #label MAT SUMMARY #length 161 #molecular-weight 17905 #checksum 6137 SEQUENCE /// ENTRY IQECAA #type complete TITLE integration host factor himA alpha chain - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 01-Mar-2002 ACCESSIONS C23099; I41285; H64929 REFERENCE A30392 !$#authors Mechulam, Y.; Fayat, G.; Blanquet, S. !$#journal J. Bacteriol. (1985) 163:787-791 !$#title Sequence of the Escherichia coli pheST operon and !1identification of the himA gene. !$#cross-references MUID:85261100; PMID:2991205 !$#accession C23099 !'##molecule_type DNA !'##residues 1-99 ##label MEC !'##cross-references GB:V00291; GB:M10430; NID:g43065; PIDN:CAA23566.1; !1PID:g43072 REFERENCE I41281 !$#authors Miller, H.I. !$#journal Cold Spring Harb. Symp. Quant. Biol. (1984) 49:691-698 !$#title Primary structure of the himA gene of Escherichia coli: !1homology with DNA-binding protein HU and association with !1the phenylalanyl-tRNA synthetase operon. !$#cross-references MUID:85153048; PMID:6397321 !$#accession I41285 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-99 ##label RES !'##cross-references GB:K02844; NID:g146342; PIDN:AAA51471.1; !1PID:g146347 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64929 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-99 ##label BLAT !'##cross-references GB:AE000266; GB:U00096; NID:g1787997; !1PIDN:AAC74782.1; PID:g1788005; UWGP:b1712 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene himA !$#map_position 38 min COMPLEX heterodimer; alpha and beta chain FUNCTION !$#description this regulatory protein is one of the two host polypeptides !1required for the DNA recombination process of the !1site-specific integration of lambda phage into the E. coli !1chromosome CLASSIFICATION #superfamily bacterial DNA-binding protein KEYWORDS DNA binding; site-specific integration; transcription !1regulation SUMMARY #length 99 #molecular-weight 11354 #checksum 2120 SEQUENCE /// ENTRY IQECAB #type complete TITLE integration host factor beta chain - Escherichia coli (strain K-12) ALTERNATE_NAMES IHF-beta ORGANISM #formal_name Escherichia coli DATE 31-Mar-1990 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS G64830; A30385; Q00172 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64830 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-94 ##label BLAT !'##cross-references GB:AE000193; GB:U00096; NID:g1787134; !1PIDN:AAC73998.1; PID:g1787141; UWGP:b0912 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A30385 !$#authors Flamm, E.; Weisberg, R.A. !$#journal J. Mol. Biol. (1985) 183:117-128 !$#title Primary structure of the hip gene of Escherichia coli and of !1its product, the beta-subunit of integration host factor. !$#cross-references MUID:85237514; PMID:3159903 !$#accession A30385 !'##molecule_type DNA !'##residues 1-89,91-94 ##label FLA GENETICS !$#gene himD; hip !$#map_position 21 min COMPLEX heterodimer; alpha and beta chains FUNCTION !$#description required for lamda site-specific recombination as well as in !1transcriptional and translational control of specific !1integration of lambda phage into the E. coli chromosome !$#note IHF is a sequence-specific DNA-binding protein and bends DNA !1when it binds CLASSIFICATION #superfamily bacterial DNA-binding protein KEYWORDS DNA binding; DNA recombination; heterodimer; transcription !1regulation; translation regulation SUMMARY #length 94 #molecular-weight 10651 #checksum 7606 SEQUENCE /// ENTRY DNECS1 #type complete TITLE DNA-binding protein HU-1 - Escherichia coli (strain K-12) ALTERNATE_NAMES DNA-binding protein NS1; histone-like protein hupB ORGANISM #formal_name Escherichia coli DATE 31-Jan-1980 #sequence_revision 31-Jan-1980 #text_change 01-Mar-2002 ACCESSIONS S06880; S09589; A91451; A91089; A61312; H64773; A02685 REFERENCE S06880 !$#authors Kano, Y.; Yoshino, S.; Wada, M.; Yokoyama, K.; Nobuhara, M.; !1Imamoto, F. !$#journal Mol. Gen. Genet. (1985) 201:360-362 !$#title Molecular cloning and nucleotide sequence of the HU-1 gene !1of Escherichia coli. !$#cross-references MUID:86117925; PMID:3003540 !$#accession S06880 !'##molecule_type DNA !'##residues 1-90 ##label KAN !'##cross-references EMBL:X16540; NID:g41769; PIDN:CAA34539.1; !1PID:g581106 !'##experimental_source strain K12 REFERENCE S09589 !$#authors Kohno, K.; Wada, M.; Kano, Y.; Imamoto, F. !$#journal J. Mol. Biol. (1990) 213:27-36 !$#title Promoters and autogenous control of the Escherichia coli !1hupA and hupB genes. !$#cross-references MUID:90250771; PMID:2187099 !$#accession S09589 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-23,'N' ##label KOH REFERENCE A91451 !$#authors Mende, L.; Timm, B.; Subramanian, A.R. !$#journal FEBS Lett. (1978) 96:395-398 !$#title Primary structures of two homologous ribosome-associated !1DNA-binding proteins of Escherichia coli. !$#cross-references MUID:79086262; PMID:215461 !$#accession A91451 !'##molecule_type protein !'##residues 1-90 ##label MEN REFERENCE A91271 !$#authors Rouviere-Yaniv, J.; Kjeldgaard, N.O. !$#journal FEBS Lett. (1979) 106:297-300 !$#title Native Escherichia coli Hu protein is a heterotypic dimer. !$#cross-references MUID:80047240; PMID:227733 !$#contents annotation !$#note on the basis of amino acid composition and tryptic digests, !1the DNA-binding protein HU and NS1 and NS2 are identical. !1NS1 corresponds to HU beta chain; the heterotypic dimer of !1native HU, or higher polymers formed in the presence of DNA, !1may play a role similar to that of the H3-H4 tetramer in the !1condensation of DNA REFERENCE A91089 !$#authors Laine, B.; Kmiecik, D.; Sautiere, P.; Biserte, G.; !1Cohen-Solal, M. !$#journal Eur. J. Biochem. (1980) 103:447-461 !$#title Complete amino acid sequences of DNA-binding proteins HU-1 !1and HU-2 from Escherichia coli. !$#cross-references MUID:80134236; PMID:6987059 !$#accession A91089 !'##molecule_type protein !'##residues 1-90 ##label LAI REFERENCE A61312 !$#authors Laine, B.; Sautiere, P.; Biserte, G.; Cohen-Solal, M.; Gros, !1F.; Rouviere-Yaniv, J. !$#journal FEBS Lett. (1978) 89:116-120 !$#title The amino- and carboxy-terminal amino acid sequences of !1protein HU from Escherichia coli. !$#cross-references MUID:78191200; PMID:350619 !$#accession A61312 !'##molecule_type protein !'##residues 1-11,'E',13-15,'L',17-25,'E',27-37;80-90 ##label LA2 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64773 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-90 ##label BLAT !'##cross-references GB:AE000150; GB:U00096; NID:g1786639; !1PIDN:AAC73543.1; PID:g1786644; UWGP:b0440 !'##experimental_source strain K-12, substrain MG1655 COMMENT NS1 is one of two proteins that bind specifically to the !1native ribosomal 30S subunit. GENETICS !$#gene hupB; hopD !$#start_codon GTG COMPLEX heterodimer; HU-2 and HU-1 chains FUNCTION !$#description plays a role in DNA replication initiation, in proper !1chromosome partitioning directed by the mukFEB proteins and !1in correct septum placement directed by minCDE proteins; !1heterodimer is required for long term survival; may maintain !1the negative supercoiling of DNA during thermal stress and !1contribute to cellular thermotolerance CLASSIFICATION #superfamily bacterial DNA-binding protein KEYWORDS DNA binding; DNA condensation; heterodimer SUMMARY #length 90 #molecular-weight 9225 #checksum 2767 SEQUENCE /// ENTRY DNECS2 #type complete TITLE DNA-binding protein HU-2 - Escherichia coli (strain K-12) ALTERNATE_NAMES DNA-binding protein NS2; histone-like protein hupA ORGANISM #formal_name Escherichia coli DATE 31-Jan-1980 #sequence_revision 08-Oct-1981 #text_change 01-Mar-2002 ACCESSIONS S06269; B91451; B91089; B61312; S09590; C65207; A02686 REFERENCE S06269 !$#authors Kano, Y.; Osato, K.; Wada, M.; Imamoto, F. !$#journal Mol. Gen. Genet. (1987) 209:408-410 !$#title Cloning and sequencing of the HU-2 gene of Escherichia coli. !$#cross-references MUID:88038389; PMID:3312963 !$#accession S06269 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-90 ##label KAN !'##cross-references GB:X05994; NID:g41764; PIDN:CAA29412.1; PID:g41765 !'##experimental_source strain K-12, substrain LE392 REFERENCE A91451 !$#authors Mende, L.; Timm, B.; Subramanian, A.R. !$#journal FEBS Lett. (1978) 96:395-398 !$#title Primary structures of two homologous ribosome-associated !1DNA-binding proteins of Escherichia coli. !$#cross-references MUID:79086262; PMID:215461 !$#accession B91451 !'##molecule_type protein !'##residues 1-90 ##label MEN REFERENCE A91271 !$#authors Rouviere-Yaniv, J.; Kjeldgaard, N.O. !$#journal FEBS Lett. (1979) 106:297-300 !$#title Native Escherichia coli Hu protein is a heterotypic dimer. !$#cross-references MUID:80047240; PMID:227733 !$#contents annotation !$#note on the basis of amino acid composition and tryptic digests, !1the DNA-binding protein HU and NS1 and NS2 are identical. !1NS2 corresponds to HU alpha chain; the heterotypic dimer of !1native HU, or higher polymers formed in the presence of DNA, !1may play a role similar to that of the H3-H4 tetramer in the !1condensation of DNA REFERENCE A91089 !$#authors Laine, B.; Kmiecik, D.; Sautiere, P.; Biserte, G.; !1Cohen-Solal, M. !$#journal Eur. J. Biochem. (1980) 103:447-461 !$#title Complete amino acid sequences of DNA-binding proteins HU-1 !1and HU-2 from Escherichia coli. !$#cross-references MUID:80134236; PMID:6987059 !$#accession B91089 !'##molecule_type protein !'##residues 1-90 ##label LAI REFERENCE A61312 !$#authors Laine, B.; Sautiere, P.; Biserte, G.; Cohen-Solal, M.; Gros, !1F.; Rouviere-Yaniv, J. !$#journal FEBS Lett. (1978) 89:116-120 !$#title The amino- and carboxy-terminal amino acid sequences of !1protein HU from Escherichia coli. !$#cross-references MUID:78191200; PMID:350619 !$#accession B61312 !'##molecule_type protein !'##residues 1-18,'AA',21,'GR',24-25,'DAII',30,'SV',33-37 ##label LA2 REFERENCE S09589 !$#authors Kohno, K.; Wada, M.; Kano, Y.; Imamoto, F. !$#journal J. Mol. Biol. (1990) 213:27-36 !$#title Promoters and autogenous control of the Escherichia coli !1hupA and hupB genes. !$#cross-references MUID:90250771; PMID:2187099 !$#accession S09590 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-28,'K' ##label KOH REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65207 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-90 ##label BLAT !'##cross-references GB:AE000473; GB:U00096; NID:g2367336; !1PIDN:AAC76974.1; PID:g1790433; UWGP:b4000 !'##experimental_source strain K-12, substrain MG1655 COMMENT NS2 is one of two proteins that bind specifically to the !1native ribosomal 30S subunit. GENETICS !$#gene hupA COMPLEX heterodimer; HU-2 and HU-1 chains FUNCTION !$#description plays a role in DNA replication initiation, in proper !1chromosome partitioning directed by the mukFEB proteins and !1in correct septum placement directed by minCDE proteins; !1heterodimer is required for long term survival; may maintain !1the negative supercoiling of DNA during thermal stress and !1contribute to cellular thermotolerance CLASSIFICATION #superfamily bacterial DNA-binding protein KEYWORDS DNA binding; DNA condensation; heterodimer SUMMARY #length 90 #molecular-weight 9535 #checksum 4952 SEQUENCE /// ENTRY DNBS2F #type complete TITLE DNA-binding protein HU - Bacillus stearothermophilus ALTERNATE_NAMES DNA-binding protein II ORGANISM #formal_name Bacillus stearothermophilus DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 16-Jun-2000 ACCESSIONS JC1205; A02690; JC2509 REFERENCE JC1205 !$#authors Padas, P.M.; Wilson, K.S.; Vorgias, C.E. !$#journal Gene (1992) 117:39-44 !$#title The DNA-binding protein HU from mesophilic and thermophilic !1Bacilli: Gene cloning, overproduction and purification. !$#cross-references MUID:92354934; PMID:1644313 !$#accession JC1205 !'##molecule_type DNA !'##residues 1-90 ##label PAD !'##cross-references GB:M73500; NID:g143064; PIDN:AAA22532.1; !1PID:g143065 REFERENCE A02690 !$#authors Kimura, M.; Wilson, K.S. !$#journal J. Biol. Chem. (1983) 258:4007-4011 !$#title On the DNA binding protein II from Bacillus !1stearothermophilus. II. The amino acid sequence and its !1relation to those of homologous proteins from other !1prokaryotes. !$#cross-references MUID:83160950; PMID:6300069 !$#accession A02690 !'##molecule_type protein !'##residues 1-90 ##label KIM REFERENCE JC2509 !$#authors Kawamura, S.; Kajiyama, H.; Yamasaki, N.; Kimura, M. !$#journal Biosci. Biotechnol. Biochem. (1995) 59:126-129 !$#title Cloning of the gene encoding DNA binding protein HU from !1Bacillus stearothermophilus and its expression in !1Escherichia coli. !$#cross-references MUID:95201364; PMID:7765961 !$#accession JC2509 !'##status preliminary !'##molecule_type DNA !'##residues 1-90 ##label KAW !'##cross-references GB:D38080; NID:g535782; PIDN:BAA07273.1; !1PID:g1065992 GENETICS !$#gene hup FUNCTION !$#description binds to both single-stranded and double-stranded DNA and to !1RNA in stoichiometric amounts CLASSIFICATION #superfamily bacterial DNA-binding protein KEYWORDS DNA binding; RNA binding SUMMARY #length 90 #molecular-weight 9716 #checksum 4525 SEQUENCE /// ENTRY DNZRHM #type complete TITLE DNA-binding protein HRm - Rhizobium meliloti ORGANISM #formal_name Rhizobium meliloti DATE 06-Jul-1982 #sequence_revision 31-Dec-1991 #text_change 17-Jul-1998 ACCESSIONS S00053; A02688; S01456 REFERENCE S00053 !$#authors Laine, B.; Belaiche, D.; Khanaka, H.; Sautiere, P. !$#journal Eur. J. Biochem. (1983) 131:325-331 !$#title Primary structure of the DNA-binding protein HRm from !1Rhizobium meliloti. !$#cross-references MUID:83157632; PMID:6299736 !$#accession S00053 !'##molecule_type protein !'##residues 1-90 ##label LAI CLASSIFICATION #superfamily bacterial DNA-binding protein KEYWORDS DNA binding; DNA condensation SUMMARY #length 90 #molecular-weight 9303 #checksum 6137 SEQUENCE /// ENTRY DNZRH8 #type complete TITLE DNA-binding protein HRl18 - Rhizobium leguminosarum (tentative sequence) ORGANISM #formal_name Rhizobium leguminosarum DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 31-Mar-2000 ACCESSIONS A02691 REFERENCE A91142 !$#authors Khanaka, H.; Laine, B.; Sautiere, P.; Guillaume, J. !$#journal Eur. J. Biochem. (1985) 147:343-349 !$#title Characterization and primary structures of DNA-binding !1HU-type proteins from Rhizobiaceae. !$#cross-references MUID:85127048; PMID:4038648 !$#accession A02691 !'##molecule_type protein !'##residues 1-91 ##label KHA !'##experimental_source strain L18 COMMENT This protein protects DNA from thermal denaturation and is !1involved in the condensation of the DNA. COMMENT This protein is identical with DNA-binding protein HAt of !1Agrobacterium tumefaciens. CLASSIFICATION #superfamily bacterial DNA-binding protein KEYWORDS DNA binding; DNA condensation SUMMARY #length 91 #molecular-weight 9365 #checksum 8837 SEQUENCE /// ENTRY DNZRH3 #type complete TITLE DNA-binding protein HRl53 - Rhizobium leguminosarum ORGANISM #formal_name Rhizobium leguminosarum DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 30-Sep-1993 ACCESSIONS A02692 REFERENCE A91142 !$#authors Khanaka, H.; Laine, B.; Sautiere, P.; Guillaume, J. !$#journal Eur. J. Biochem. (1985) 147:343-349 !$#title Characterization and primary structures of DNA-binding !1HU-type proteins from Rhizobiaceae. !$#cross-references MUID:85127048; PMID:4038648 !$#accession A02692 !'##molecule_type protein !'##residues 1-91 ##label KHA !'##experimental_source strain L53 COMMENT This protein protects DNA from thermal denaturation and is !1involved in the condensation of the DNA. CLASSIFICATION #superfamily bacterial DNA-binding protein KEYWORDS DNA binding; DNA condensation SUMMARY #length 91 #molecular-weight 9382 #checksum 8018 SEQUENCE /// ENTRY DNYTXA #type complete TITLE DNA-binding protein - Thermoplasma acidophilum ALTERNATE_NAMES histone-like protein HTa ORGANISM #formal_name Thermoplasma acidophilum DATE 31-Mar-1980 #sequence_revision 01-Sep-1981 #text_change 07-May-1999 ACCESSIONS A92338; A92339; A61311; A02689 REFERENCE A92338 !$#authors DeLange, R.J.; Green, G.R.; Searcy, D.G. !$#journal J. Biol. Chem. (1981) 256:900-904 !$#title A histone-like protein (HTa) from Thermoplasma acidophilum. !1I. Purification and properties. !$#cross-references MUID:81094064; PMID:7451480 !$#accession A92338 !'##molecule_type protein !'##residues 1-3;2-48 ##label DE1 !'##note a form lacking the amino-terminal Met was also found REFERENCE A92339 !$#authors DeLange, R.J.; Williams, L.C.; Searcy, D.G. !$#journal J. Biol. Chem. (1981) 256:905-911 !$#title A histone-like protein (HTa) from Thermoplasma acidophilum. !1II. Complete amino acid sequence. !$#cross-references MUID:81094065; PMID:7005226 !$#accession A92339 !'##molecule_type protein !'##residues 2-90 ##label DE2 REFERENCE A61311 !$#authors Searcy, D.G.; Delange, R.J. !$#journal Biochim. Biophys. Acta (1980) 609:197-200 !$#title Thermoplasma acidophilum histone-like protein. Partial amino !1acid sequence suggestive of homology to eukaryotic histones. !$#cross-references MUID:81000492; PMID:7407184 !$#accession A61311 !'##molecule_type protein !'##residues 1-24 ##label SEA CLASSIFICATION #superfamily bacterial DNA-binding protein KEYWORDS DNA binding SUMMARY #length 90 #molecular-weight 10066 #checksum 8175 SEQUENCE /// ENTRY DNBP11 #type complete TITLE DNA-binding protein - phage SPO1 ALTERNATE_NAMES transcription factor 1 ORGANISM #formal_name phage SPO1 #note host Bacillus subtilis DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 22-Jun-1999 ACCESSIONS A02693; S13254 REFERENCE A02693 !$#authors Greene, J.R.; Brennan, S.M.; Andrew, D.J.; Thompson, C.C.; !1Richards, S.H.; Heinrikson, R.L.; Geiduschek, E.P. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:7031-7035 !$#title Sequence of the bacteriophage SP01 gene coding for !1transcription factor 1, a viral homologue of the bacterial !1type II DNA-binding proteins. !$#cross-references MUID:85063726; PMID:6438630 !$#accession A02693 !'##molecule_type DNA !'##residues 1-99 ##label GRE !'##cross-references GB:K02381; NID:g216144; PIDN:AAA32599.1; !1PID:g216145 REFERENCE S13254 !$#authors Sayre, M.H.; Geiduschek, E.P. !$#journal J. Mol. Biol. (1990) 216:819-833 !$#title Effects of mutations at amino acid 61 in the arm of TF1 on !1its DNA-binding properties. !$#cross-references MUID:91094044; PMID:2125081 !$#contents annotation COMMENT This protein, a homolog of the bacterial type II DNA-binding !1proteins (also called HU proteins), selectively inhibits the !1transcription of hydroxymethyluracil-containing DNA by host !1RNA polymerase. CLASSIFICATION #superfamily bacterial DNA-binding protein KEYWORDS DNA binding; homodimer; transcription SUMMARY #length 99 #molecular-weight 10737 #checksum 3122 SEQUENCE /// ENTRY DNECFS #type complete TITLE DNA-binding protein fis - Escherichia coli (strain K-12) ALTERNATE_NAMES Hin recombinational enhancer-binding protein; Mu enhancer-binding protein; Nbp protein; ndh-binding protein; recombinational enhancer-binding protein fis ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 01-Mar-2002 ACCESSIONS A32142; A28207; C47043; S15344; G65118; A58919 REFERENCE A32142 !$#authors Koch, C.; Vandekerckhove, J.; Kahmann, R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:4237-4241 !$#title Escherichia coli host factor for site-specific DNA !1inversion: cloning and characterization of the fis gene. !$#cross-references MUID:88247997; PMID:2837762 !$#accession A32142 !'##molecule_type DNA !'##residues 1-98 ##label KOC !'##cross-references GB:J03816; NID:g145972; PIDN:AAA98812.1; !1PID:g145973 REFERENCE A28207 !$#authors Johnson, R.C.; Ball, C.A.; Pfeffer, D.; Simon, M.I. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:3484-3488 !$#title Isolation of the gene encoding the Hin recombinational !1enhancer binding protein. !$#cross-references MUID:88217925; PMID:2835774 !$#accession A28207 !'##molecule_type DNA !'##residues 1-98 ##label JOH !'##cross-references GB:J03245; NID:g145970; PIDN:AAA83856.1; !1PID:g145971 REFERENCE A47043 !$#authors Ball, C.A.; Osuna, R.; Ferguson, K.C.; Johnson, R.C. !$#journal J. Bacteriol. (1992) 174:8043-8056 !$#title Dramatic changes in Fis levels upon nutrient upshift in !1Escherichia coli. !$#cross-references MUID:93094136; PMID:1459953 !$#accession C47043 !'##molecule_type DNA !'##residues 1-98 ##label BAL !'##cross-references GB:M95784; NID:g145974; PIDN:AAA23783.1; !1PID:g145977 !'##note sequence extracted from NCBI backbone (NCBIN:119972, !1NCBIP:119975) REFERENCE S15344 !$#authors Osuna, R.; Finkel, S.E.; Johnson, R.C. !$#journal EMBO J. (1991) 10:1593-1603 !$#title Identification of two functional regions in Fis: the !1N-terminus is required to promote Hin-mediated DNA inversion !1but not lambda excision. !$#cross-references MUID:91224111; PMID:1851089 !$#accession S15344 !'##molecule_type DNA !'##residues 1-98 ##label OSU REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65118 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-98 ##label BLAT !'##cross-references GB:AE000405; GB:U00096; NID:g1789659; !1PIDN:AAC76293.1; PID:g1789661; UWGP:b3261 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S77719 !$#authors Green, J.; Anjum, M.F.; Guest, J.R. !$#journal Mol. Microbiol. (1996) 20:1043-1055 !$#title The ndh-binding protein (Nbp) regulates the ndh gene of !1Escherichia coli in response to growth phase and is !1identical to Fis. !$#cross-references MUID:96405628; PMID:8809757 !$#accession A58919 !'##molecule_type protein !'##residues 1,'XX',4-5,'X',7-11 ##label GRE !'##experimental_source strain W3110 GENETICS !$#gene fis !$#map_position 72 min FUNCTION !$#description stimulates the Hin-mediated in vitro site-specific DNA !1inversion in E. coli and the Gin-mediated inversion of the G !1segment in phage Mu, by binding to a recombinational !1enhancer and induces some DNA-bending, a crucial structure !1alteration for enhancer function CLASSIFICATION #superfamily DNA-binding protein fis KEYWORDS DNA binding SUMMARY #length 98 #molecular-weight 11240 #checksum 3607 SEQUENCE /// ENTRY DNBPD8 #type complete TITLE DNA-binding protein Ner - phage D108 ORGANISM #formal_name phage D108 DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 22-Jun-1999 ACCESSIONS A24680; S07931 REFERENCE A24680 !$#authors Tolias, P.P.; DuBow, M.S. !$#journal EMBO J. (1985) 4:3031-3037 !$#title The cloning and characterization of the bacteriophage D108 !1regulatory DNA-binding protein ner. !$#cross-references MUID:86055744; PMID:2998774 !$#accession A24680 !'##molecule_type DNA !'##residues 1-73 ##label TOL !'##cross-references GB:M26291; NID:g166194; PIDN:AAA32206.1; !1PID:g166195 REFERENCE S07370 !$#authors Mizuuchi, M.; Weisberg, R.A.; Mizuuchi, K. !$#journal Nucleic Acids Res. (1986) 14:3813-3825 !$#title DNA sequence of the control region of phage D108: the !1N-terminal amino acid sequences of repressor and transposase !1are similar both in phage D108 and in its relative, phage !1Mu. !$#cross-references MUID:86232621; PMID:3012481 !$#accession S07931 !'##molecule_type DNA !'##residues 1-73 ##label MIZ !'##cross-references EMBL:X03847; NID:g15439; PIDN:CAA27475.1; !1PID:g15441 GENETICS !$#gene ner CLASSIFICATION #superfamily phage D108 DNA-binding protein KEYWORDS DNA binding SUMMARY #length 73 #molecular-weight 8534 #checksum 6464 SEQUENCE /// ENTRY DNBPNU #type complete TITLE DNA-binding protein ner [validated] - phage Mu ALTERNATE_NAMES protein cII ORGANISM #formal_name phage Mu DATE 31-Dec-1989 #sequence_revision 19-Apr-1996 #text_change 15-Sep-2000 ACCESSIONS S09549; JT0306 REFERENCE S07291 !$#authors Priess, H.; Kamp, D.; Kahmann, R.; Braeuer, B.; Delius, H. !$#journal Mol. Gen. Genet. (1982) 186:315-321 !$#title Nucleotide sequence of the immunity region of bacteriophage !1Mu. !$#cross-references MUID:83012203; PMID:6214696 !$#accession S09549 !'##molecule_type DNA !'##residues 1-75 ##label PRI !'##cross-references EMBL:V01464; NID:g15807; PIDN:CAA24712.1; !1PID:g15809 REFERENCE JT0306 !$#authors Allet, B.; Payton, M.; Mattaliano, R.J.; Gronenborn, A.M.; !1Clore, G.M.; Wingfield, P.T. !$#journal Gene (1988) 65:259-268 !$#title Purification and characterization of the DNA-binding protein !1Ner of bacteriophage mu. !$#cross-references MUID:88313674; PMID:2970420 !$#accession JT0306 !'##molecule_type protein !'##residues 2-75 ##label ALL REFERENCE A58979 !$#authors Rose, K.; Simona, M.G.; Savoy, L.A.; Regamey, P.O.; Green, !1B.N.; Clore, G.M.; Gronenborn, A.M.; Wingfield, P.T. !$#journal J. Biol. Chem. (1992) 267:19101-19106 !$#title Pyruvic acid is attached through its central carbon atom to !1the amino terminus of the recombinant DNA-derived !1DNA-binding protein Ner of bacteriophage Mu. !$#cross-references MUID:92406846; PMID:1388164 !$#contents annotation; post-translational modification !$#note the modification is identified as a pyruvic acid ketimine !1blocked amino end REFERENCE A66208 !$#authors Clore, G.M.; Strzelecka, T.E.; Gronenborn, A.M. !$#submission submitted to the Brookhaven Protein Data Bank, August 1995 !$#cross-references PDB:1NEQ !$#contents annotation; conformation by (1)H-, and (15)N-NMR, residues !12-75 REFERENCE A66209 !$#authors Clore, G.M.; Strzelecka, T.E.; Gronenborn, A.M. !$#submission submitted to the Brookhaven Protein Data Bank, August 1995 !$#cross-references PDB:1NER !$#contents annotation; conformation by (1)H-, and (15)N-NMR, residues !12-75 REFERENCE A34077 !$#authors Gronenborn, A.M.; Wingfield, P.T.; Clore, G.M. !$#journal Biochemistry (1989) 28:5081-5089 !$#title Determination of the secondary structure of the DNA binding !1proein ner from phage Mu using (1)H homonuclear and (15)N- !1(1)H heteronuclear NMR spectorscopy. !$#cross-references MUID:89352591; PMID:2527559 !$#contents annotation; conformation by (1)H-, and (15)N-NMR GENETICS !$#gene ner CLASSIFICATION #superfamily phage D108 DNA-binding protein KEYWORDS blocked amino end; DNA binding; transcription regulation FEATURE !$2-75 #product DNA-binding protein ner #status experimental !8#label MAT\ !$2 #modified_site pyruvate 2-iminyl amino end (Cys) (in !8mature form) #status experimental SUMMARY #length 75 #molecular-weight 8506 #checksum 7970 SEQUENCE /// ENTRY BVECNP #type complete TITLE Sugar fermentation stimulation protein B (NER-like protein) - Escherichia coli (strain K-12) ALTERNATE_NAMES ner-like protein ORGANISM #formal_name Escherichia coli DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 01-Mar-2002 ACCESSIONS JV0027; F65109 REFERENCE JV0027 !$#authors Choi, Y.L.; Nishida, T.; Kawamukai, M.; Utsumi, R.; Sakai, !1H.; Komano, T. !$#journal J. Bacteriol. (1989) 171:5222-5225 !$#title Cloning and sequencing of an Escherichia coli gene, nlp, !1highly homologous to the ner genes of bacteriophages Mu and !1D108. !$#cross-references MUID:89359178; PMID:2670911 !$#accession JV0027 !'##molecule_type DNA !'##residues 1-92 ##label CHO !'##cross-references GB:X68873; NID:g42128; PIDN:CAA48736.1; PID:g42129 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65109 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-92 ##label BLAT !'##cross-references GB:AE000399; GB:U00096; NID:g2367201; !1PIDN:AAC76220.1; PID:g1789579; UWGP:b3188 !'##experimental_source strain K-12, substrain MG1655 COMMENT This protein is involved in positive regulation of the !1metabolism of sugars. GENETICS !$#gene nlp !$#map_position 69 min CLASSIFICATION #superfamily phage D108 DNA-binding protein KEYWORDS DNA binding; transcription regulation FEATURE !$50-68 #region DNA binding #status predicted SUMMARY #length 92 #molecular-weight 10495 #checksum 4077 SEQUENCE /// ENTRY DNBPMU #type complete TITLE DNA-binding protein - phage Mu ORGANISM #formal_name phage Mu #note host Escherichia coli DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 22-Jun-1999 ACCESSIONS A24331 REFERENCE A24331 !$#authors Akroyd, J.E.; Clayson, E.; Higgins, N.P. !$#journal Nucleic Acids Res. (1986) 14:6901-6914 !$#title Purification of the gam gene-product of bacteriophage mu and !1determination of the nucleotide sequence of the gam gene. !$#cross-references MUID:87016333; PMID:2945162 !$#accession A24331 !'##molecule_type DNA !'##residues 1-174 ##label AKR !'##cross-references GB:X04390; NID:g15460; PIDN:CAA27978.1; PID:g15461 !'##note the authors translated the codon CCG for residues 61 and 145 as !1Phe GENETICS !$#gene gam CLASSIFICATION #superfamily phage Mu DNA-binding protein KEYWORDS DNA binding SUMMARY #length 174 #molecular-weight 19032 #checksum 4741 SEQUENCE /// ENTRY DNMS #type complete TITLE nucleolin - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 22-Jun-1999 ACCESSIONS A29958; A40769; A56240; I84688 REFERENCE A29958 !$#authors Bourbon, H.M.; Lapeyre, B.; Amalric, F. !$#journal J. Mol. Biol. (1988) 200:627-638 !$#title Structure of the mouse nucleolin gene. The complete sequence !1reveals that each RNA binding domain is encoded by two !1independent exons. !$#cross-references MUID:88316930; PMID:3137346 !$#accession A29958 !'##molecule_type DNA !'##residues 1-707 ##label BOU !'##cross-references GB:X07699; NID:g53453; PIDN:CAA30538.1; PID:g53454 REFERENCE A40769 !$#authors Pasternack, M.S.; Bleier, K.J.; McInerney, T.N. !$#journal J. Biol. Chem. (1991) 266:14703-14708 !$#title Granzyme A binding to target cell proteins. Granzyme A binds !1to and cleaves nucleolin in vitro. !$#cross-references MUID:91317840; PMID:1860869 !$#accession A40769 !'##molecule_type protein !'##residues 2-20,'X',22-24 ##label PAS REFERENCE A56240 !$#authors Yang, T.H.; Tsai, W.H.; Lee, Y.M.; Lei, H.Y.; Lai, M.Y.; !1Chen, D.S.; Yeh, N.H.; Lee, S.C. !$#journal Mol. Cell. Biol. (1994) 14:6068-6074 !$#title Purification and characterization of nucleolin and its !1identification as a transcription repressor. !$#cross-references MUID:94344117; PMID:8065340 !$#accession A56240 !'##molecule_type protein !'##residues 2-19;558-567 ##label YAN REFERENCE I48118 !$#authors Bourbon, H. !$#journal Gene (1988) 68:73-84 !$#title Sequence and structure of the nucleolin promoter in rodents: !1Characterization of a strikingly conserved CpG island. !$#cross-references MUID:89121496; PMID:2906027 !$#accession I84688 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-44 ##label RES !'##cross-references GB:M22089; NID:g200111; PIDN:AAA39841.1; !1PID:g554246 COMMENT This housekeeping protein is involved in the synthesis, !1packaging, and maturation of pre-mRNA and is the major !1protein of the nucleolus in exponentially growing cells. GENETICS !$#introns 6/3; 45/3; 211/1; 273/1; 302/1; 349/2; 391/1; 432/3; 484/1; !1525/2; 566/1; 608/2; 683/1 CLASSIFICATION #superfamily nucleolin; ribonucleoprotein repeat homology KEYWORDS DNA binding; duplication; nucleus; phosphoprotein; RNA !1binding; transcription regulation FEATURE !$310-375 #domain ribonucleoprotein repeat homology #label !8RRM1\ !$311-316 #region RNA-binding RNP2 motif\ !$349-356 #region RNA-binding RNP1 motif\ !$396-458 #domain ribonucleoprotein repeat homology #label !8RRM2\ !$397-402 #region RNA-binding RNP2 motif\ !$431-438 #region RNA-binding RNP1 motif\ !$488-551 #domain ribonucleoprotein repeat homology #label !8RRM3\ !$489-494 #region RNA-binding RNP2 motif\ !$524-531 #region RNA-binding RNP1 motif\ !$570-634 #domain ribonucleoprotein repeat homology #label !8RRM4\ !$571-576 #region RNA-binding RNP2 motif\ !$607-614 #region RNA-binding RNP1 motif SUMMARY #length 707 #molecular-weight 76723 #checksum 9032 SEQUENCE /// ENTRY DNCHNL #type complete TITLE nucleolin - chicken ALTERNATE_NAMES nucleolar protein C23 ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 22-Jun-1999 ACCESSIONS S08414; S10766; A32725; I50397; B30099 REFERENCE S08414 !$#authors Maridor, G.; Nigg, E.A. !$#journal Nucleic Acids Res. (1990) 18:1286 !$#title cDNA sequences of chicken nucleolin/C23 and NO38/B23, two !1major nucleolar proteins. !$#cross-references MUID:90206792; PMID:2320420 !$#accession S08414 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-694 ##label MAR !'##cross-references EMBL:X17199; NID:g63710; PIDN:CAA35060.1; !1PID:g63711 REFERENCE S10766 !$#authors Maridor, G.; Krek, W.; Nigg, E.A. !$#journal Biochim. Biophys. Acta (1990) 1049:126-133 !$#title Structure and developmental expression of chicken nucleolin !1and NO38: coordinate expression of two abundant !1non-ribosomal nucleolar proteins. !$#cross-references MUID:90304215; PMID:2114180 !$#accession S10766 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-694 ##label MAR2 REFERENCE A32725 !$#authors Peter, M.; Nakagawa, J.; Doree, M.; Labbe, J.C.; Nigg, E.A. !$#journal Cell (1990) 60:791-801 !$#title Identification of major nucleolar proteins as candidate !1mitotic substrates of cdc2 kinase. !$#cross-references MUID:90182668; PMID:2178776 !$#accession A32725 !'##molecule_type protein !'##residues 56-62;63-109;197-214 ##label PET REFERENCE I50397 !$#authors Borer, R.A.; Lehner, C.F.; Eppenberger, H.M.; Nigg, E.A. !$#journal Cell (1989) 56:379-390 !$#title Major Nucleolar Proteins Shuttle between Nucleus and !1Cytoplasm. !$#cross-references MUID:89119560; PMID:2914325 !$#accession I50397 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 407-418,'R',420-519,'T',521-694 ##label BOR !'##cross-references GB:M21791; NID:g212411; PIDN:AAA48983.1; !1PID:g212412 COMMENT Phosphorylation of this protein by cdc2 kinase may !1contribute to the reorganization of the structure of the !1nucleolus during mitosis. CLASSIFICATION #superfamily nucleolin; ribonucleoprotein repeat homology KEYWORDS DNA binding; duplication; nucleolus; nucleus; !1phosphoprotein; RNA binding; tandem repeat FEATURE !$1-247 #domain acidic #label ACI\ !$54-91 #region 7-residue repeats (T-P-A-K-K-A-[A/V])\ !$254-262 #region nuclear location signal\ !$267-275 #region nuclear location signal\ !$282-347 #domain ribonucleoprotein repeat homology #label !8RRM1\ !$283-361 #domain RNA binding #status predicted #label RNA1\ !$372-435 #domain ribonucleoprotein repeat homology #label !8RRM2\ !$373-448 #domain RNA binding #status predicted #label RNA2\ !$462-525 #domain ribonucleoprotein repeat homology #label !8RRM3\ !$463-538 #domain RNA binding #status predicted #label RNA3\ !$554-618 #domain ribonucleoprotein repeat homology #label !8RRM4\ !$555-631 #domain RNA binding #status predicted #label RNA4\ !$632-694 #domain glycine/arginine-rich #label GRR\ !$56,63,70,77,85 #binding_site phosphate (Thr) (covalent) (by cdc2 !8kinase) #status predicted SUMMARY #length 694 #molecular-weight 75640 #checksum 4564 SEQUENCE /// ENTRY A49358 #type complete TITLE RNA-binding protein EWS - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A49358; S28257 REFERENCE A49358 !$#authors Plougastel, B.; Zucman, J.; Peter, M.; Thomas, G.; Delattre, !1O. !$#journal Genomics (1993) 18:609-615 !$#title Genomic structure of the EWS gene and its relationship to !1EWSR1, a site of tumor-associated chromosome translocation. !$#cross-references MUID:94140360; PMID:8307570 !$#accession A49358 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-656 ##label RES !'##cross-references EMBL:X72990; NID:g485838; PIDN:CAA51489.1; !1PID:g825654 REFERENCE S28257 !$#authors Delattre, O.; Zucman, J.; Plougastel, B.; Desmaze, C.; !1Melot, T.; Peter, M.; Kovar, H.; Joubert, I.; de Jong, P.; !1Rouleau, G.; Aurias, A.; Thomas, G. !$#journal Nature (1992) 359:162-165 !$#title Gene fusion with an ETS DNA-binding domain caused by !1chromosome translocation in human tumours. !$#cross-references MUID:92396239; PMID:1522903 !$#accession S28257 !'##molecule_type mRNA !'##residues 1-656 ##label DEL !'##cross-references EMBL:X66899; NID:g547565; PIDN:CAA47350.1; !1PID:g31280 GENETICS !$#gene GDB:EWSR1 !'##cross-references GDB:135984; OMIM:133450 !$#map_position 22q12.1-22q12.1 !$#introns 5/1; 17/2; 34/3; 76/1; 138/2; 194/2; 265/1; 325/2; 338/1; !1349/1; 388/3; 432/1; 473/1; 527/2; 560/1; 644/2 !$#note EWSR1 region is exons 7-10 of this gene, called EWS in !1reference A49358; this region is disrupted in the !1translocations seen in Ewings sarcoma and related tumors CLASSIFICATION #superfamily RNA-binding protein EWS; ribonucleoprotein !1repeat homology KEYWORDS carcinogenesis; nucleus; RNA binding; tandem repeat FEATURE !$362-437 #domain ribonucleoprotein repeat homology #label RRM SUMMARY #length 656 #molecular-weight 68478 #checksum 7636 SEQUENCE /// ENTRY A55726 #type complete TITLE RNA-binding protein Ews - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A55726; S45007 REFERENCE A55726 !$#authors Plougastel, B.; Mattei, M.G.; Thomas, G.; Delattre, O. !$#journal Genomics (1994) 23:278-281 !$#title Cloning and chromosome localization of the mouse Ews gene. !$#cross-references MUID:95130099; PMID:7829090 !$#accession A55726 !'##status preliminary !'##molecule_type mRNA !'##residues 1-655 ##label PLO !'##cross-references GB:X79233; NID:g488512; PIDN:CAA55815.1; !1PID:g488513 !'##note authors translated the codon TCA for residue 116 as Thr, GCC !1for residue 123 as Thr, ACC for residue 126 as Ala, and GGT !1for residue 568 as Val GENETICS !$#gene Ews CLASSIFICATION #superfamily RNA-binding protein EWS; ribonucleoprotein !1repeat homology KEYWORDS carcinogenesis; nucleus; RNA binding; tandem repeat FEATURE !$361-436 #domain ribonucleoprotein repeat homology #label RRM SUMMARY #length 655 #molecular-weight 68418 #checksum 4621 SEQUENCE /// ENTRY S33799 #type complete TITLE RNA-binding protein FUS, nuclear - human ALTERNATE_NAMES RNA-binding protein TLS ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S33799; S36157 REFERENCE S33798 !$#authors Crozat, A.; Aman, P.; Mandahl, N.; Ron, D. !$#journal Nature (1993) 363:640-644 !$#title Fusion of CHOP to a novel RNA-binding protein in human !1myxoid liposarcoma. !$#cross-references MUID:93288139; PMID:8510758 !$#accession S33799 !'##molecule_type mRNA !'##residues 1-526 ##label CRO !'##cross-references GB:S62140; NID:g386156; PIDN:AAB27102.1; !1PID:g386157 !'##experimental_source liposarcoma REFERENCE S36157 !$#authors Rabbitts, T.H.; Forster, A.; Larson, R.; Nathan, P. !$#journal Nature Genet. (1993) 4:175-180 !$#title Fusion of the dominant negative transcription regulator CHOP !1with a novel gene FUS by translocation t(12;16) in malignant !1liposarcoma. !$#cross-references MUID:93350637; PMID:7503811 !$#accession S36157 !'##status preliminary !'##molecule_type mRNA !'##residues 1-63,'S',66-526 ##label RAB !'##cross-references EMBL:X71428; NID:g393415; PIDN:CAA50559.1; !1PID:g4210363 !'##experimental_source liposarcoma GENETICS !$#gene GDB:FUS !'##cross-references GDB:136048; OMIM:137070 !$#map_position 16p11.2-16p11.2 FUNCTION !$#description RNA binding; probable plays a role in transcriptional !1regulation CLASSIFICATION #superfamily RNA-binding protein EWS; ribonucleoprotein !1repeat homology KEYWORDS carcinogenesis; nucleus; RNA binding; tandem repeat FEATURE !$286-361 #domain ribonucleoprotein repeat homology #label RRM SUMMARY #length 526 #molecular-weight 53426 #checksum 9348 SEQUENCE /// ENTRY C64440 #type complete TITLE DNA repair protein RAD24 homolog (intein-containing) - Methanococcus jannaschii CONTAINS intein ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS C64440 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession C64440 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-1195 ##label BUL !'##cross-references GB:U67555; GB:L77117; NID:g1591760; !1PIDN:AAB99126.1; PID:g1499976; TIGR:MJ1124 GENETICS !$#map_position FOR1062443-1066030 CLASSIFICATION #superfamily Methanococcus jannaschii probable DNA repair !1protein RAD24 (intein-containing) KEYWORDS ATP; nucleotide binding; P-loop; protein splicing FEATURE !$39-46 #region nucleotide-binding motif A (P-loop)\ !$139-144 #region nucleotide-binding motif B\ !$143-146 #region DEXH motif SUMMARY #length 1195 #molecular-weight 138673 #checksum 8364 SEQUENCE /// ENTRY I38977 #type complete TITLE TAR DNA-binding protein-43 - human ALTERNATE_NAMES protein DKFZp564O1716.1 ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 20-Apr-2000 ACCESSIONS I38977; T08671 REFERENCE I38977 !$#authors Ou, S.H.; Wu, F.; Harrich, D.; Garcia-Martinez, L.F.; !1Gaynor, R.B. !$#journal J. Virol. (1995) 69:3584-3596 !$#title Cloning and characterization of a novel cellular protein, !1TDP-43, that binds to human immunodeficiency virus type 1 !1TAR DNA sequence motifs. !$#cross-references MUID:95264449; PMID:7745706 !$#accession I38977 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-414 ##label RES !'##cross-references EMBL:U23731; NID:g901997; PIDN:AAA70033.1; !1PID:g901998 REFERENCE Z16467 !$#authors Duesterhoeft, A.; Lauber, J.; Mewes, H.W.; Gassenhuber, J.; !1Wiemann, S. !$#submission submitted to the Protein Sequence Database, March 1999 !$#accession T08671 !'##status preliminary !'##molecule_type mRNA !'##residues 1-414 ##label DUE !'##cross-references EMBL:AL050265 !'##experimental_source fetal brain; clone DKFZp564O1716 COMMENT TAR DNA-binding protein binds to HIV-1 LTR TAR DNA region !1and can repress HIV-1 transcription. GENETICS !$#gene GDB:TDP-43 !'##cross-references GDB:9956557 !$#note DKFZp564O1716.1 CLASSIFICATION #superfamily human TAR DNA-binding protein-43; !1ribonucleoprotein repeat homology FEATURE !$105-170 #domain ribonucleoprotein repeat homology #label !8RRM1\ !$192-257 #domain ribonucleoprotein repeat homology #label RRM2 SUMMARY #length 414 #molecular-weight 44740 #checksum 1225 SEQUENCE /// ENTRY S37849 #type complete TITLE DNA intrastrand crosslink recognition protein - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YKL032c; protein YKL245; transcription factor ORD1 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S37849; S37853; S41668; S39002; A57739 REFERENCE S37832 !$#authors Rieger, M. !$#submission submitted to the Protein Sequence Database, March 1994 !$#accession S37849 !'##molecule_type DNA !'##residues 1-597 ##label RIE !'##cross-references EMBL:Z28032; NID:g486033; PIDN:CAA81867.1; !1PID:g486034; GSPDB:GN00011; MIPS:YKL032c !'##experimental_source strain S288C REFERENCE S37851 !$#authors Purnelle, B.; Skala, J.; van Dyck, L.; Tettelin, H.; !1Goffeau, A. !$#submission submitted to the Protein Sequence Database, March 1994 !$#accession S37853 !'##molecule_type DNA !'##residues 1-597 ##label PUR !'##cross-references EMBL:Z28032; NID:g486033; PIDN:CAA81867.1; !1PID:g486034; GSPDB:GN00011; MIPS:YKL032c !'##experimental_source strain S288C REFERENCE S41667 !$#authors Purnelle, B.; Skala, J.; van Dyck, L.; Goffeau, A. !$#journal Yeast (1994) 10:125-130 !$#title Analysis of an 11.7 kb DNA fragment of chromosome XI reveals !1a new tRNA gene and four new open reading frames including a !1leucing zipper protein and a homologue to the yeast !1mitochondrial regulator ABF2. !$#cross-references MUID:94262309; PMID:8203146 !$#accession S41668 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-597 ##label PU2 !'##cross-references EMBL:X71622; NID:g505182; PIDN:CAB37853.1; !1PID:g4467991 !'##experimental_source strain S288C REFERENCE S39002 !$#authors Brown, S.J.; Kellett, P.J.; Lippard, S.J. !$#submission submitted to the EMBL Data Library, July 1993 !$#description IXR1, a yeast protein that binds to platinated DNA and !1confers sensitivity to cisplatin. !$#accession S39002 !'##molecule_type DNA !'##residues 1-72,74-92,'F',94-107,113-206,'T',208-219,'TT',222-597 !1##label BRO !'##cross-references EMBL:L16900; NID:g311108; PIDN:AAA02859.1; !1PID:g311109 REFERENCE A57739 !$#authors Lambert, J.R.; Bilanchone, V.W.; Cumsky, M.G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1994) 91:7345-7349 !$#title The ORD1 gene encodes a transcription factor involved in !1oxygen regulation and is identical to IXR1, a gene that !1confers cisplatin sensitivity to Saccharomyces cerevisiae. !$#cross-references MUID:94316692; PMID:8041793 !$#accession A57739 !'##status preliminary !'##molecule_type DNA !'##residues 1-107,113-597 ##label LAM !'##cross-references GB:L16900 GENETICS !$#gene SGD:IXR1; ORD1; MIPS:YKL032c !'##cross-references SGD:S0001515; MIPS:YKL032c !$#map_position 11L CLASSIFICATION #superfamily yeast DNA intrastrand crosslink recognition !1protein; HMG box homology KEYWORDS DNA binding; nucleus; transcription factor; transcription !1regulation FEATURE !$358-429 #domain HMG box homology #label HMG1\ !$431-499 #domain HMG box homology #label HMG2 SUMMARY #length 597 #molecular-weight 67856 #checksum 2573 SEQUENCE /// ENTRY A31888 #type complete TITLE ribonucleoprotein La - human ALTERNATE_NAMES autoantigen SS-B/La; ribonucleoprotein SS-B; Sjogren syndrome antigen B ORGANISM #formal_name Homo sapiens #common_name man DATE 21-May-1990 #sequence_revision 26-May-1994 #text_change 22-Jun-1999 ACCESSIONS A31888; S03848; A22956; A61051; S11013; I55553; I70205; !1I70206; A31273 REFERENCE A31888 !$#authors Chambers, J.C.; Kenan, D.; Martin, B.J.; Keene, J.D. !$#journal J. Biol. Chem. (1988) 263:18043-18051 !$#title Genomic structure and amino acid sequence domains of the !1human La autoantigen. !$#cross-references MUID:89053970; PMID:3192525 !$#accession A31888 !'##molecule_type mRNA !'##residues 1-408 ##label CHA !'##cross-references GB:J04205; NID:g178686; PIDN:AAA51885.1; !1PID:g178687 REFERENCE S03848 !$#authors Chan, E.K.L.; Sullivan, K.F.; Tan, E.M. !$#journal Nucleic Acids Res. (1989) 17:2233-2244 !$#title Ribonucleoprotein SS-B/La belongs to a protein family with !1consensus sequences for RNA-binding. !$#cross-references MUID:89202037; PMID:2468131 !$#accession S03848 !'##molecule_type mRNA !'##residues 1-408 ##label CH2 !'##cross-references EMBL:X13697; NID:g36414; PIDN:CAA31985.1; !1PID:g36415 REFERENCE A22956 !$#authors Chambers, J.C.; Keene, J.D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:2115-2119 !$#title Isolation and analysis of cDNA clones expressing human lupus !1La antigen. !$#cross-references MUID:85166283; PMID:3856888 !$#accession A22956 !'##molecule_type mRNA !'##residues 45-97,'LK' ##label CH3 !'##cross-references GB:J04205 !'##note this sequence has been revised in reference A31888 REFERENCE A61051 !$#authors Nyman, U.; Ringertz, N.R.; Pettersson, I. !$#journal Immunol. Lett. (1989) 22:65-72 !$#title Demonstration of an amino terminal La epitope recognized by !1human anti-La sera. !$#cross-references MUID:89379261; PMID:2476379 !$#accession A61051 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-19,'E',21-47 ##label NYM REFERENCE S11013 !$#authors Sturgess, A.D.; Peterson, M.G.; McNeilage, L.J.; !1Whittingham, S.; Coppel, R.L. !$#journal J. Immunol. (1988) 140:3212-3218 !$#title Characteristics and epitope mapping of a cloned human !1autoantigen La. !$#cross-references MUID:88199081; PMID:2452201 !$#accession S11013 !'##molecule_type mRNA !'##residues 'E',55-287,'V',289-408 ##label STU !'##cross-references EMBL:M20328; NID:g337456; PIDN:AAA36577.1; !1PID:g337457 REFERENCE I55553 !$#authors Kohsaka, H.; Yamamoto, K.; Fujii, H.; Miura, H.; Miyasaka, !1N.; Nishioka, K.; Miyamoto, T. !$#journal J. Clin. Invest. (1990) 85:1566-1574 !$#title Fine epitope mapping the human SS-B/La protein: !1Identification of a distinct autoepitope homologous to a !1viral gag polyprotein. !$#cross-references MUID:90237237; PMID:1692037 !$#accession I55553 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 81-107 ##label RES !'##cross-references GB:M35261; NID:g338491; PIDN:AAA36652.1; !1PID:g338495 !$#accession I70205 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 174-224 ##label RE2 !'##cross-references GB:M35263; NID:g338492; PIDN:AAA36653.1; !1PID:g338496 !$#accession I70206 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 279-342 ##label RE3 !'##cross-references GB:M35262; NID:g338493; PIDN:AAA36654.1; !1PID:g338497 COMMENT This protein associates with a variety of small RNA !1molecules, most of which are primary transcripts generated !1by RNA polymerase III, to form ribonucleoprotein La !1particles. This protein may act as a transcription !1termination factor. GENETICS !$#gene GDB:SSB !'##cross-references GDB:125359; OMIM:109090 !$#map_position 2 !$#introns 22/3; 57/2; 115/3; 151/3; 185/2; 209/2; 223/3; 264/3; 380/2 CLASSIFICATION #superfamily ribonucleoprotein La; ribonucleoprotein repeat !1homology KEYWORDS phosphoprotein; RNA binding FEATURE !$112-178 #domain ribonucleoprotein repeat homology #label RRM\ !$113-118 #region RNA-binding RNP2 motif\ !$151-158 #region RNA-binding RNP1 motif\ !$228-408 #domain phosphorylated #status experimental #label !8PHY SUMMARY #length 408 #molecular-weight 46837 #checksum 1468 SEQUENCE /// ENTRY S03849 #type complete TITLE ribonucleoprotein La - bovine ALTERNATE_NAMES autoantigen SS-B/La; ribonucleoprotein SS-B ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Dec-1990 #sequence_revision 26-May-1994 #text_change 22-Jun-1999 ACCESSIONS S03849 REFERENCE S03848 !$#authors Chan, E.K.L.; Sullivan, K.F.; Tan, E.M. !$#journal Nucleic Acids Res. (1989) 17:2233-2244 !$#title Ribonucleoprotein SS-B/La belongs to a protein family with !1consensus sequences for RNA-binding. !$#cross-references MUID:89202037; PMID:2468131 !$#accession S03849 !'##molecule_type mRNA !'##residues 1-404 ##label CHA !'##cross-references EMBL:X13698; NID:g755; PIDN:CAA31986.1; PID:g756 !'##note part of this sequence was confirmed by protein sequencing COMMENT This protein associates with a variety of small RNA !1molecules, most of which are primary transcripts generated !1by RNA polymerase III, to form ribonucleoprotein La !1particles. This protein may act as a transcription !1termination factor. CLASSIFICATION #superfamily ribonucleoprotein La; ribonucleoprotein repeat !1homology KEYWORDS blocked amino end; phosphoprotein; RNA binding FEATURE !$112-178 #domain ribonucleoprotein repeat homology #label RRM\ !$113-118 #region RNA-binding RNP2 motif\ !$151-158 #region RNA-binding RNP1 motif\ !$228-404 #domain phosphorylated #status predicted #label PHY SUMMARY #length 404 #molecular-weight 46534 #checksum 737 SEQUENCE /// ENTRY JC1494 #type complete TITLE ribonucleoprotein La - rat ALTERNATE_NAMES autoantigen SS-B/La; ribonucleoprotein SS-B ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 24-Feb-1994 #sequence_revision 26-May-1994 #text_change 22-Jun-1999 ACCESSIONS JC1494; S25145 REFERENCE JC1494 !$#authors Semsei, I.; Troester, H.; Bartsch, H.; Schwemmle, M.; Igloi, !1G.L.; Bachmann, M. !$#journal Gene (1993) 126:265-268 !$#title Isolation of rat cDNA clones coding for the autoantigen !1SS-B/La: Detection of species-specific variations. !$#cross-references MUID:93246255; PMID:7916708 !$#accession JC1494 !'##molecule_type mRNA !'##residues 1-415 ##label SEM !'##cross-references GB:X67859; NID:g55778; PIDN:CAA48043.1; PID:g55779 !'##experimental_source liver COMMENT This protein associates with a variety of small RNA !1molecules, most of which are primary transcripts generated !1by RNA polymerase III, to form ribonucleoprotein La !1particles. This protein may act as a transcription !1termination factor. CLASSIFICATION #superfamily ribonucleoprotein La; ribonucleoprotein repeat !1homology KEYWORDS phosphoprotein; RNA binding FEATURE !$112-178 #domain ribonucleoprotein repeat homology #label RRM\ !$113-118 #region RNA-binding RNP2 motif\ !$151-158 #region RNA-binding RNP1 motif\ !$227-415 #domain phosphorylated #status predicted #label PHY SUMMARY #length 415 #molecular-weight 47777 #checksum 1509 SEQUENCE /// ENTRY S33817 #type complete TITLE ribonucleoprotein La.B - African clawed frog ALTERNATE_NAMES autoantigen SS-B/La; ribonucleoprotein SS-B ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 03-Feb-1994 #sequence_revision 26-May-1994 #text_change 22-Jun-1999 ACCESSIONS S33817; S28544 REFERENCE S33817 !$#authors Scherly, D.; Stutz, F.; Lin-Marq, N.; Clarkson, S.G. !$#journal J. Mol. Biol. (1993) 231:196-204 !$#title La proteins from Xenopus laevis. cDNA cloning and !1developmental expression. !$#cross-references MUID:93287095; PMID:8510143 !$#accession S33817 !'##molecule_type mRNA !'##residues 1-427 ##label SCH !'##cross-references EMBL:X68818; NID:g64875; PIDN:CAA48716.1; !1PID:g64876 COMMENT This protein associates with a variety of small RNA !1molecules, most of which are primary transcripts generated !1by RNA polymerase III, to form ribonucleoprotein La !1particles. This protein may act as a transcription !1termination factor. CLASSIFICATION #superfamily ribonucleoprotein La; ribonucleoprotein repeat !1homology KEYWORDS phosphoprotein; RNA binding FEATURE !$111-177 #domain ribonucleoprotein repeat homology #label RRM\ !$112-117 #region RNA-binding RNP2 motif\ !$150-157 #region RNA-binding RNP1 motif\ !$227-427 #domain phosphorylated #status predicted #label PHY SUMMARY #length 427 #molecular-weight 48995 #checksum 5985 SEQUENCE /// ENTRY S33818 #type complete TITLE ribonucleoprotein La.A - African clawed frog ALTERNATE_NAMES autoantigen SS-B/La; ribonucleoprotein SS-B ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 03-Feb-1994 #sequence_revision 26-May-1994 #text_change 22-Jun-1999 ACCESSIONS S33818; S28545 REFERENCE S33817 !$#authors Scherly, D.; Stutz, F.; Lin-Marq, N.; Clarkson, S.G. !$#journal J. Mol. Biol. (1993) 231:196-204 !$#title La proteins from Xenopus laevis. cDNA cloning and !1developmental expression. !$#cross-references MUID:93287095; PMID:8510143 !$#accession S33818 !'##molecule_type mRNA !'##residues 1-428 ##label SCH !'##cross-references EMBL:X68817; NID:g64873; PIDN:CAA48715.1; !1PID:g64874 COMMENT This protein associates with a variety of small RNA !1molecules, most of which are primary transcripts generated !1by RNA polymerase III, to form ribonucleoprotein La !1particles. This protein may act as a transcription !1termination factor. CLASSIFICATION #superfamily ribonucleoprotein La; ribonucleoprotein repeat !1homology KEYWORDS phosphoprotein; RNA binding FEATURE !$112-178 #domain ribonucleoprotein repeat homology #label RRM\ !$113-118 #region RNA-binding RNP2 motif\ !$151-158 #region RNA-binding RNP1 motif\ !$228-428 #domain phosphorylated #status predicted #label PHY SUMMARY #length 428 #molecular-weight 48864 #checksum 7828 SEQUENCE /// ENTRY A55377 #type complete TITLE CPE-binding protein - African clawed frog ALTERNATE_NAMES cytoplasmic polyadenylation element-binding protein ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A55377 REFERENCE A55377 !$#authors Hake, L.E.; Richter, J.D. !$#journal Cell (1994) 79:617-627 !$#title CPEB is a specificity factor that mediates cytoplasmic !1polyadenylation during Xenopus oocyte maturation. !$#cross-references MUID:95042759; PMID:7954828 !$#accession A55377 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-568 ##label HAK !'##cross-references GB:U14169; NID:g987224; PIDN:AAA80483.1; !1PID:g624634 CLASSIFICATION #superfamily African clawed frog CPE-binding protein; !1ribonucleoprotein repeat homology FEATURE !$314-388 #domain ribonucleoprotein repeat homology #label RRM1 SUMMARY #length 568 #molecular-weight 62559 #checksum 9751 SEQUENCE /// ENTRY A40724 #type complete TITLE fragile X mental retardation syndrome protein [validated] - human ALTERNATE_NAMES gene FMR1 protein ORGANISM #formal_name Homo sapiens #common_name man DATE 14-Aug-1998 #sequence_revision 14-Aug-1998 #text_change 23-Mar-2001 ACCESSIONS S45243; S45245; S45244; S45247; S45248; S45246; I54334; !1I68601; I68602; I68603; I68605; I68616; I68606; I68607; !1I68604; I68608; I68609; I68610; I68611; I68612; I68613; !1I68617; I51881; A39530; S37653; A40724 REFERENCE S45243 !$#authors Richards, S.; Eichler, E.E.; Lu, F.; King, J.; Pizzuti, A.; !1Nelson, D.L.; Gibbs, R.A. !$#submission submitted to the EMBL Data Library, March 1994 !$#description Complete Sequence of the Human FMR-1 locus. !$#accession S45243 !'##molecule_type DNA !'##residues 1-632 ##label RIC1 !'##cross-references EMBL:L29074; NID:g1668818; PIDN:AAB18833.1; !1PID:g457235 !$#accession S45245 !'##molecule_type DNA !'##residues 1-490,503-632 ##label RIC2 !'##cross-references EMBL:L29074; NID:g1668818; PIDN:AAB18828.1; !1PID:g457237 !$#accession S45244 !'##molecule_type DNA !'##residues 1-579,597-632 ##label RIC3 !'##cross-references EMBL:L29074; NID:g1668818; PIDN:AAB18832.1; !1PID:g457236 !$#accession S45247 !'##molecule_type DNA !'##residues 1-490,516-632 ##label RIC4 !'##cross-references EMBL:L29074; NID:g1668818; PIDN:AAB18830.1; !1PID:g457239 !$#accession S45248 !'##molecule_type DNA !'##residues 1-490,516-579,597-632 ##label RIC5 !'##cross-references EMBL:L29074; NID:g1668818; PIDN:AAB18829.1; !1PID:g457240 !$#accession S45246 !'##status preliminary !'##molecule_type DNA !'##residues 1-490,503-579,597-632 ##label RIC !'##cross-references EMBL:L29074; NID:g1668818; PIDN:AAB18831.1; !1PID:g457238 REFERENCE I54334 !$#authors Eichler, E.E.; Richards, S.; Gibbs, R.A.; Nelson, D.L. !$#journal Hum. Mol. Genet. (1993) 2:1147-1153 !$#title Fine structure of the human FMR1 gene. !$#cross-references MUID:94004853; PMID:8401496 !$#accession I54334 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-17,'VLGSRAGPIFAL' ##label EI01 !'##cross-references GB:L19476; NID:g388721; PIDN:AAA62452.1; !1PID:g388722 !$#accession I68601 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 18-34 ##label EI02 !'##cross-references GB:L19477; NID:g388723; PIDN:AAA62453.1; !1PID:g553287 !$#accession I68602 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 36-66 ##label EI03 !'##cross-references GB:L19478; NID:g388725; PIDN:AAA62454.1; !1PID:g388726 !$#accession I68603 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 67-90 ##label EI04 !'##cross-references GB:L19479; NID:g388727; PIDN:AAA62455.1; !1PID:g388728 !$#accession I68605 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 91-139 ##label EI05 !'##cross-references GB:L19481; NID:g388731; PIDN:AAA62457.1; !1PID:g553289 !$#accession I68616 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 141-171 ##label EI06 !'##cross-references GB:L19492; NID:g388751; PIDN:AAA62468.1; !1PID:g388752 !$#accession I68606 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 172-210 ##label EI07 !'##cross-references GB:L19482; NID:g388733; PIDN:AAA62458.1; !1PID:g388734 !$#accession I68607 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 211-267 ##label EI08 !'##cross-references GB:L19483; NID:g388735; PIDN:AAA62459.1; !1PID:g388736 !$#accession I68604 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 268-293 ##label EI09 !'##cross-references GB:L19480; NID:g388729; PIDN:AAA62456.1; !1PID:g553288 !$#accession I68608 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 295-330 ##label EI10 !'##cross-references GB:L19484; NID:g388737; PIDN:AAA62460.1; !1PID:g388738 !$#accession I68609 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 331-375 ##label EI11 !'##cross-references GB:L19485; NID:g388739; PIDN:AAA62461.1; !1PID:g388740 !$#accession I68610 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 376-396 ##label EI12 !'##cross-references GB:L19486; NID:g388741; PIDN:AAA62462.1; !1PID:g388742 !$#accession I68611 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 397-425 ##label EI13 !'##cross-references GB:L19487; NID:g388743; PIDN:AAA62463.1; !1PID:g388744 !$#accession I68612 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 426-490 ##label EI14 !'##cross-references GB:L19488; NID:g388745; PIDN:AAA62464.1; !1PID:g553290 !$#accession I68613 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 492-551 ##label EI15 !'##cross-references GB:L19489; NID:g393121; PIDN:AAA62465.1; !1PID:g553291 !$#accession I68617 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 580-632 ##label EI6 !'##cross-references GB:L19493; NID:g388753; PIDN:AAA62469.1; !1PID:g388754 REFERENCE I51881 !$#authors Hirst, M.; Grewal, P.; Flannery, A.; Slatter, R.; Maher, E.; !1Barton, D.; Fryns, J.P.; Davies, K. !$#journal Am. J. Hum. Genet. (1995) 56:67-74 !$#title Two new cases of FMR1 deletion associated with mental !1impairment. !$#cross-references MUID:95126142; PMID:7825604 !$#accession I51881 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-17 ##label HIR !'##cross-references GB:S76590; NID:g913380; PIDN:AAD14228.1; !1PID:g4261928 REFERENCE A39530 !$#authors Verkerk, A.J.M.H.; Pieretti, M.; Sutcliffe, J.S.; Fu, Y.H.; !1Kuhl, D.P.A.; Pizzuti, A.; Reiner, O.; Richards, S.; !1Victoria, M.F.; Zhang, F.; Eussen, B.E.; van Ommen, G.J.B.; !1Blonden, L.A.J.; Riggins, G.J.; Chastain, J.L.; Kunst, C.B.; !1Galjaard, H.; Caskey, C.T.; Nelson, D.L.; Oostra, B.A.; !1Warren, S.T. !$#journal Cell (1991) 65:905-914 !$#title Identification of a gene (FMR-1) containing a CGG repeat !1coincident with a breakpoint cluster region exhibiting !1length variation in fragile X syndrome. !$#cross-references MUID:91249396; PMID:1710175 !$#accession A39530 !'##status preliminary !'##molecule_type mRNA !'##residues 'DGGARARGRAAARRRRRRRRRRRRRRRRRR', !1'RRRRRRRRRRRRLGLERPQPTSRGRAPGAS','RAEEK',1-293,296-375, !1397-579,597-632 ##label VER1 !'##cross-references GB:M67468; NID:g182672; PIDN:AAA52458.1; !1PID:g182673 REFERENCE S37653 !$#authors Verkerk, A.J.M.H.; de Graaff, E.; de Boulle, K.; Eichler, !1E.E.; Konecki, D.S.; Reyniers, E.; Manca, A.; Poustka, A.; !1Willems, P.J.; Nelson, D.L.; Oostra, B.A. !$#journal Hum. Mol. Genet. (1993) 2:399-404 !$#title Alternative splicing in the fragile X gene FMR1. !$#cross-references MUID:93278388; PMID:8504300 !$#accession S37653 !'##molecule_type mRNA !'##residues 1-632 ##label VER2 !'##cross-references EMBL:X69962; NID:g296587; PIDN:CAA49586.1; !1PID:g296588 !'##note the authors translated 40 GAT codons as Asn and the codon GAT !1for residue 58 as Gly REFERENCE A40724 !$#authors Siomi, H.; Siomi, M.C.; Nussbaum, R.L.; Dreyfuss, G. !$#journal Cell (1993) 74:291-298 !$#title The protein product of the fragile X gene, FMR1, has !1characteristics of an RNA-binding protein. !$#cross-references MUID:93345017; PMID:7688265 !$#accession A40724 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 285-320 ##label SIO !'##note binding to RNA, particularly poly(G), is demonstrated REFERENCE A69801 !$#authors Musco, G.; Kharrat, A.; Stier, G.; Fraternali, F.; Gibson, !1T.J.; Nilges, M.; Pastore, A. !$#submission submitted to the Brookhaven Protein Data Bank, October 1997 !$#cross-references PDB:2FMR !$#contents annotation; conformation by (1)H- and (15)N-NMR, residues !1216-280 REFERENCE A58852 !$#authors Musco, G.; Kharrat, A.; Stier, G.; Fraternali, F.; Gibson, !1T.J.; Nilges, M.; Pastore, A. !$#journal Nat. Struct. Biol. (1997) 4:712-716 !$#title The solution structure of the first KH domain of FMR1, the !1protein responsible for the fragile X syndrome. !$#cross-references MUID:97448673; PMID:9302998 !$#contents annotation; conformation by (1)H-and (15)N-NMR GENETICS !$#gene GDB:FMR1; FRAXA !'##cross-references GDB:129038; OMIM:309550 !$#map_position Xq27.3-Xq27.3 !$#introns 17/3; 35/2; 66/3; 90/3; 140/2; 171/3; 210/3; 267/3; 294/1; !1330/3; 375/3; 396/3; 425/3; 491/1; 503/1; 552/1; 579/3 CLASSIFICATION #superfamily fragile X mental retardation syndrome protein KEYWORDS alternative splicing; methylated amino acid; nucleolus; RNA !1binding FEATURE !$1-632 #product fragile X mental retardation syndrome !8protein, splice form 1 #status predicted #label MAT1\ !$1-579,597-632 #product fragile X mental retardation syndrome !8protein, splice form 2 #status predicted #label MAT2\ !$1-490,503-632 #product fragile X mental retardation syndrome !8protein, splice form 3 #status predicted #label MAT3\ !$1-490,503-579, !$597-632 #product fragile X mental retardation syndrome !8protein, splice form 4 #status predicted #label MAT4\ !$1-490,516-632 #product fragile X mental retardation syndrome !8protein, splice form 5 #status predicted #label MAT5\ !$1-490,516-579, !$597-632 #product fragile X mental retardation syndrome !8protein, splice form 6 #status predicted #label MAT6\ !$1-293,296-375, !$397-579,597-632 #product fragile X mental retardation syndrome !8protein, splice form 7 #status predicted #label MAT7\ !$222-251 #domain ribonucleoprotein K #status predicted #label !8KH1\ !$285-314 #domain ribonucleoprotein K #status predicted #label !8KH2\ !$534-548 #region RNA binding RGG box\ !$528,534,539,544,546 #modified_site omega-N,omega-N-dimethylarginine (Arg) !8#status predicted SUMMARY #length 632 #molecular-weight 71174 #checksum 9878 SEQUENCE /// ENTRY S36173 #type complete TITLE fragile X mental retardation syndrome protein - mouse ALTERNATE_NAMES gene FMR1 protein ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S36173 REFERENCE S36173 !$#authors Ashley, C.T.; Sutcliffe, J.S.; Kunst, C.B.; Leiner, H.A.; !1Eichler, E.E.; Nelson, D.L.; Warren, S.T. !$#journal Nature Genet. (1993) 4:244-251 !$#title Human and murine FMR-1: alternative splicing and !1translational initiation downstream of the CGG-repeat. !$#cross-references MUID:93364418; PMID:8358432 !$#accession S36173 !'##status preliminary !'##molecule_type mRNA !'##residues 1-614 ##label ASH !'##cross-references EMBL:L23971; NID:g398044 GENETICS !$#gene MGI:FMR1 !'##cross-references MGI:95564 CLASSIFICATION #superfamily fragile X mental retardation syndrome protein KEYWORDS alternative splicing; nucleolus; RNA binding FEATURE !$222-251 #domain ribonucleoprotein K similarity #label KH1 SUMMARY #length 614 #molecular-weight 68989 #checksum 9152 SEQUENCE /// ENTRY A40669 #type complete TITLE mitochondrial receptor complex chain MOM22 - Neurospora crassa ALTERNATE_NAMES mitochondrial outer membrane preprotein receptor chain MOM22 ORGANISM #formal_name Neurospora crassa DATE 03-May-1994 #sequence_revision 02-Jun-1994 #text_change 22-Jun-1999 ACCESSIONS A40669; S33472 REFERENCE A40669 !$#authors Kiebler, M.; Keil, P.; Schneider, H.; van der Klei, I.J.; !1Pfanner, N.; Neupert, W. !$#journal Cell (1993) 74:483-492 !$#title The mitochondrial receptor complex: a central role of MOM22 !1in mediating preprotein transfer from receptors to the !1general insertion pore. !$#cross-references MUID:93351229; PMID:8348615 !$#accession A40669 !'##molecule_type mRNA !'##residues 1-154 ##label KIE !'##cross-references GB:X71021; NID:g311426; PIDN:CAA50339.1; !1PID:g311427 COMMENT This protein resides in the mitochondrial outer membrane !1(MOM) where it serves as part of the receptor complex for !1mitochondrial preproteins. GENETICS !$#gene MOM22 CLASSIFICATION #superfamily mitochondrial receptor complex chain MOM22 KEYWORDS mitochondrion; transmembrane protein FEATURE !$85-105 #domain transmembrane #status predicted #label TMM SUMMARY #length 154 #molecular-weight 16816 #checksum 9898 SEQUENCE /// ENTRY A32915 #type complete TITLE nucleophosmin - human ALTERNATE_NAMES nucleolar phosphoprotein B23; numatrin ORGANISM #formal_name Homo sapiens #common_name man DATE 22-Oct-1999 #sequence_revision 22-Oct-1999 #text_change 22-Oct-1999 ACCESSIONS A33423; A32915; A30137; S06926; B26080; A26080 REFERENCE A33423 !$#authors Zhang, X.T.; Thomis, D.C.; Samuel, C.E. !$#journal Biochem. Biophys. Res. Commun. (1989) 164:176-184 !$#title Isolation and characterization of a molecular cDNA clone of !1a human mRNA from interferon-treated cells encoding !1nucleolar protein B23, numatrin. !$#cross-references MUID:90026373; PMID:2478125 !$#accession A33423 !'##molecule_type mRNA !'##residues 1-294 ##label ZHA !'##cross-references GB:M26697; NID:g189311; PIDN:AAA36385.1; !1PID:g189312 REFERENCE A32915 !$#authors Li, X.; McNeilage, L.J.; Whittingham, S. !$#journal Biochem. Biophys. Res. Commun. (1989) 163:72-78 !$#title The nucleotide sequence of a human cDNA encoding the highly !1conserved nucleolar phosphoprotein B23. !$#cross-references MUID:89374300; PMID:2775293 !$#accession A32915 !'##molecule_type mRNA !'##residues 1-294 ##label LIX !'##cross-references GB:M28699; NID:g557545; PIDN:AAA58386.1; !1PID:g557546 REFERENCE A30137 !$#authors Chan, W.Y.; Liu, Q.R.; Borjigin, J.; Busch, H.; Rennert, !1O.M.; Tease, L.A.; Chan, P.K. !$#journal Biochemistry (1989) 28:1033-1039 !$#title Characterization of the cDNA encoding human nucleophosmin !1and studies of its role in normal and abnormal growth. !$#cross-references MUID:89229105; PMID:2713355 !$#accession A30137 !'##molecule_type mRNA !'##residues 1-294 ##label CHAW !'##cross-references GB:M23613; NID:g189271; PIDN:AAA36380.1; !1PID:g189272 REFERENCE S06926 !$#authors Hale, T.K.; Mansfield, B.C. !$#journal Nucleic Acids Res. (1989) 17:10112 !$#title Nucleotide sequence of a cDNA clone representing a third !1allele of human protein B23. !$#cross-references MUID:90098787; PMID:2602120 !$#accession S06926 !'##status translation not shown !'##molecule_type mRNA !'##residues 15-294 ##label HAL !'##cross-references EMBL:X16934; NID:g32029; PIDN:CAA34809.1; !1PID:g825671 !'##experimental_source clone hL6T REFERENCE A92562 !$#authors Chan, P.K.; Chan, W.Y.; Yung, B.Y.M.; Cook, R.G.; Aldrich, !1M.B.; Ku, D.; Goldknopf, I.L.; Busch, H. !$#journal J. Biol. Chem. (1986) 261:14335-14341 !$#title Amino acid sequence of a specific antigenic peptide of !1protein B23. !$#cross-references MUID:87033628; PMID:2429957 !$#accession B26080 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 'P',214-226 ##label CHA1 !'##cross-references GB:M31004; GB:M12775; NID:g190239 !'##experimental_source clone hpB2 !$#accession A26080 !'##molecule_type mRNA !'##residues 'P',214-215,'S',217-218,'SSS',222-294 ##label CHA2 !'##cross-references GB:J02590; NID:g190237; PIDN:AAA36473.1; !1PID:g190238 GENETICS !$#gene GDB:NPM1 !'##cross-references GDB:138455; OMIM:164040 !$#map_position 5q35-5q35 CLASSIFICATION #superfamily nucleophosmin KEYWORDS nucleolus; nucleus; phosphoprotein FEATURE !$120-132 #region glutamic acid-rich\ !$152-158 #region nuclear location signal\ !$161-188 #region aspartic acid/glutamic acid-rich\ !$191-198 #region nuclear location signal\ !$125 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 294 #molecular-weight 32575 #checksum 6645 SEQUENCE /// ENTRY DNCHFM #type complete TITLE nucleophosmin - chicken ALTERNATE_NAMES nucleolar protein B23; nucleolar protein NO38; numatrin ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 22-Jun-1999 ACCESSIONS S08415; S10767; I50398; I50399; A30099 REFERENCE S08414 !$#authors Maridor, G.; Nigg, E.A. !$#journal Nucleic Acids Res. (1990) 18:1286 !$#title cDNA sequences of chicken nucleolin/C23 and NO38/B23, two !1major nucleolar proteins. !$#cross-references MUID:90206792; PMID:2320420 !$#accession S08415 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-294 ##label MAR !'##cross-references EMBL:X17200; NID:g63704; PIDN:CAA35061.1; !1PID:g63705 REFERENCE S10766 !$#authors Maridor, G.; Krek, W.; Nigg, E.A. !$#journal Biochim. Biophys. Acta (1990) 1049:126-133 !$#title Structure and developmental expression of chicken nucleolin !1and NO38: coordinate expression of two abundant !1non-ribosomal nucleolar proteins. !$#cross-references MUID:90304215; PMID:2114180 !$#accession S10767 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-294 ##label MAR2 REFERENCE I50397 !$#authors Borer, R.A.; Lehner, C.F.; Eppenberger, H.M.; Nigg, E.A. !$#journal Cell (1989) 56:379-390 !$#title Major Nucleolar Proteins Shuttle between Nucleus and !1Cytoplasm. !$#cross-references MUID:89119560; PMID:2914325 !$#accession I50398 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-97 ##label BOR !'##cross-references GB:J03164; NID:g212453; PIDN:AAA48989.1; !1PID:g212456 !$#accession I50399 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 261-294 ##label BO2 !'##cross-references GB:J03165; NID:g212454; PIDN:AAA48990.1; !1PID:g212457 CLASSIFICATION #superfamily nucleophosmin KEYWORDS nucleus; phosphoprotein FEATURE !$122-133 #region glutamic acid-rich\ !$153-159 #region nuclear location signal\ !$161-186 #region aspartic acid/glutamic acid-rich\ !$190-197 #region nuclear location signal\ !$127 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 294 #molecular-weight 32632 #checksum 8828 SEQUENCE /// ENTRY R3EC1 #type complete TITLE ribosomal protein S1 [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 18-Aug-1982 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS F64830; S61286; A02694; B04448; S29161 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64830 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-557 ##label BLAT !'##cross-references GB:AE000193; GB:U00096; NID:g1787134; !1PIDN:AAC73997.1; PID:g1787140; UWGP:b0911 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S61284 !$#authors Freestone, P.; Grant, S.; Toth, I.; Norris, V. !$#journal Mol. Microbiol. (1995) 15:573-580 !$#title Identification of phosphoproteins in Escherichia coli. !$#cross-references MUID:95302968; PMID:7783627 !$#accession S61286 !'##status preliminary !'##molecule_type protein !'##residues 1-13,'XV' ##label FRE REFERENCE A02694 !$#authors Schnier, J.; Kimura, M.; Foulaki, K.; Subramanian, A.R.; !1Isono, K.; Wittmann-Liebold, B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:1008-1011 !$#title Primary structure of Escherichia coli ribosomal protein S1 !1and of its gene rpsA. !$#cross-references MUID:82174525; PMID:7041110 !$#accession A02694 !'##molecule_type protein !'##residues 1-124,'D',126-557 ##label SCH1 !'##experimental_source strain MRE600 REFERENCE A04448 !$#authors Schnier, J.; Isono, K. !$#journal Nucleic Acids Res. (1982) 10:1857-1865 !$#title The DNA sequence of the gene rspA of Escherichia coli coding !1for ribosomal protein S1. !$#cross-references MUID:82196866; PMID:6281725 !$#accession B04448 !'##molecule_type DNA !'##residues 1-120,'N',122-124,'D',126-180,'D',183-451,'V',453-557 !1##label SCH2 !'##cross-references GB:V00352; GB:J01681; GB:J01682; NID:g42899 !'##experimental_source strain K-12, substrain JS6.5 REFERENCE S29160 !$#authors Pedersen, S.; Skouv, J.; Kajitani, M.; Ishihama, A. !$#journal Mol. Gen. Genet. (1984) 196:135-140 !$#title Transcriptional organization of the rpsA operon of !1Escherichia coli. !$#cross-references MUID:85012047; PMID:6384724 !$#accession S29161 !'##status translation not shown !'##molecule_type DNA !'##residues 1-20 ##label PED !'##cross-references EMBL:X00785; NID:g42838; PIDN:CAA25361.1; !1PID:g42840 GENETICS !$#gene rpsA; ssyF !$#map_position 21 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX small subunit ribosomal proteins: S1 (PIR:R3EC1), S2 !1(PIR:R3EC2), S3 (PIR:R3EC3), S4 (PIR:R3EC4), S5 (PIR:R3EC5), !1S6 (PIR:R3EC6), S7 (PIR:R3EC7K), S8 (PIR:R3EC8), S9 !1(PIR:R3EC9), S10 (PIR:R3EC10), S11 (PIR:R3EC11), S12 !1(PIR:R3EC12), S13 (PIR:R3EC13), S14 (PIR:R3EC14), S15 !1(PIR:R3EC15), S16 (PIR:R3EC16), S17 (PIR:R3EC17), S18 !1(PIR:R3EC18), S19 (PIR:R3EC19), S20/L26 (PIR:R3EC20), S21 !1(PIR:R3EC21), S22 (PIR:C64901) [validated, MUID:99196679] FUNCTION !$#pathway protein biosynthesis CLASSIFICATION #superfamily Escherichia coli ribosomal protein S1 KEYWORDS duplication; protein biosynthesis; ribosome; RNA binding FEATURE !$1-557 #product ribosomal protein S1 #status experimental !8#label MAT SUMMARY #length 557 #molecular-weight 61158 #checksum 2436 SEQUENCE /// ENTRY R3ZR1 #type complete TITLE ribosomal protein S1 - Rhizobium meliloti ORGANISM #formal_name Rhizobium meliloti DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S01055 REFERENCE S01055 !$#authors Schnier, J.; Thamm, S.; Lurz, R.; Hussain, A.; Faist, G.; !1Dobrinski, B. !$#journal Nucleic Acids Res. (1988) 16:3075-3089 !$#title Cloning and characterization of a gene from Rhizobium !1melilotii 2011 coding for ribosomal protein S1. !$#cross-references MUID:88217521; PMID:3368316 !$#accession S01055 !'##molecule_type DNA !'##residues 1-568 ##label SCH !'##cross-references EMBL:X07528; NID:g46338; PIDN:CAA30404.1; !1PID:g46339 !'##note the sequence from Fig. 5 is inconsistent with that from Fig. 4 !1in having 565-Glu GENETICS !$#gene rpsA CLASSIFICATION #superfamily Escherichia coli ribosomal protein S1 KEYWORDS duplication; protein biosynthesis; ribosome; RNA binding FEATURE !$196-453 #domain RNA binding #status predicted #label RNA\ !$196-279,280-366, !$367-453 #region duplication SUMMARY #length 568 #molecular-weight 62639 #checksum 2186 SEQUENCE /// ENTRY R3HUS3 #type complete TITLE ribosomal protein S3, cytosolic - human ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1992 #sequence_revision 06-Sep-1996 #text_change 22-Jun-1999 ACCESSIONS A41247; S13109; I54090; S68941 REFERENCE A41247 !$#authors Pogue-Geile, K.; Geiser, J.R.; Shu, M.; Miller, C.; Wool, !1I.G.; Meisler, A.I.; Pipas, J.M. !$#journal Mol. Cell. Biol. (1991) 11:3842-3849 !$#title Ribosomal protein genes are overexpressed in colorectal !1cancer: isolation of a cDNA clone encoding the human S3 !1ribosomal protein. !$#cross-references MUID:91304374; PMID:1712897 !$#accession A41247 !'##molecule_type mRNA !'##residues 1-7,'R',9-243 ##label POG !'##cross-references GB:S42658 !'##note the authors translated the codon AGG for residue 8 as Lys REFERENCE S13109 !$#authors Zhang, X.T.; Tan, Y.M.; Tan, Y.H. !$#journal Nucleic Acids Res. (1990) 18:6689 !$#title Isolation of a cDNA encoding human 40S ribosomal protein s3. !$#cross-references MUID:91067464; PMID:2129557 !$#accession S13109 !'##molecule_type mRNA !'##residues 1-103,'C',105-232,'L',234-243 ##label ZHA !'##cross-references EMBL:X55715; NID:g32531; PIDN:CAA39248.1; !1PID:g32532 REFERENCE I54090 !$#authors Tycowski, K.T.; Shu, M. !$#journal Genes Dev. (1993) 7:1176-1190 !$#title A small nucleolar RNA is processed from an intron of the !1human gene encoding ribosomal protein S3. !$#cross-references MUID:93307653; PMID:8319909 !$#accession I54090 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-95 ##label RES !'##cross-references GB:L16016; NID:g347526; PIDN:AAA18095.1; !1PID:g347527 REFERENCE S68911 !$#authors Vladimirov, S.N.; Ivanov, A.V.; Karpova, G.G.; Musolyamov, !1A.K.; Egorov, T.A.; Thiede, B.; Wittmann-Liebold, B.; Otto, !1A. !$#journal Eur. J. Biochem. (1996) 239:144-149 !$#title Characterization of the human small-ribosomal-subunit !1proteins by N-terminal and internal sequencing, and mass !1spectrometry. !$#cross-references MUID:96305378; PMID:8706699 !$#accession S68941 !'##molecule_type protein !'##residues 188-191,'X',193-197 ##label VLA GENETICS !$#gene GDB:RPS3 !'##cross-references GDB:128634; OMIM:600454 !$#map_position 11q13.3-11q13.5 !$#introns 10/3; 54/2; 85/3 !$#note the list of introns may be incomplete !$#note the single-copy gene for snRNA U15A is encoded within the !1first intron CLASSIFICATION #superfamily rat ribosomal protein S3 KEYWORDS blocked amino end; protein biosynthesis; ribosome SUMMARY #length 243 #molecular-weight 26688 #checksum 4140 SEQUENCE /// ENTRY R3RT3 #type complete TITLE ribosomal protein S3, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 21-Jul-2000 ACCESSIONS S13882; S18846; S10393 REFERENCE S13882 !$#authors Chan, Y.L.; Devi, K.R.G.; Olvera, J.; Wool, I.G. !$#journal Arch. Biochem. Biophys. (1990) 283:546-550 !$#title The primary structure of rat ribosomal protein S3. !$#cross-references MUID:91112777; PMID:2275563 !$#accession S13882 !'##molecule_type mRNA !'##residues 1-243 ##label CHA !'##cross-references EMBL:X51536 !$#accession S18846 !'##molecule_type protein !'##residues 158-172 ##label CHA2 !'##note the protein is designated as ribosomal protein S3 CLASSIFICATION #superfamily rat ribosomal protein S3 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 243 #molecular-weight 26660 #checksum 4140 SEQUENCE /// ENTRY R3XL3A #type complete TITLE ribosomal protein S3a - African clawed frog ALTERNATE_NAMES ribosomal protein XS1a ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 22-Jun-1999 ACCESSIONS S15665 REFERENCE S15665 !$#authors di Cristina, M.; Menard, R.; Pierandrei-Amaldi, P. !$#journal Nucleic Acids Res. (1991) 19:1943 !$#title Xenopus laevis ribosomal protein S1a cDNA sequence. !$#cross-references MUID:91232967; PMID:2030971 !$#accession S15665 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type mRNA !'##residues 1-246 ##label DIC !'##cross-references EMBL:X57322; NID:g65090; PIDN:CAA40592.1; !1PID:g65091 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1991 CLASSIFICATION #superfamily rat ribosomal protein S3 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 246 #molecular-weight 27001 #checksum 8020 SEQUENCE /// ENTRY R3HS3S #type complete TITLE ribosomal protein S3 [validated] - Haloarcula marismortui ALTERNATE_NAMES ribosomal protein B; ribosomal protein HS1 ORGANISM #formal_name Haloarcula marismortui DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 26-May-2000 ACCESSIONS I35063; A24304 REFERENCE A35063 !$#authors Arndt, E.; Kroemer, W.; Hatakeyama, T. !$#journal J. Biol. Chem. (1990) 265:3034-3039 !$#title Organization and nucleotide sequence of a gene cluster !1coding for eight ribosomal proteins in the archaebacterium !1Halobacterium marismortui. !$#cross-references MUID:90153945; PMID:2406244 !$#accession I35063 !'##molecule_type DNA !'##residues 1-304 ##label ARN !'##cross-references EMBL:J05222; NID:g148800; PIDN:AAA86865.1; !1PID:g148807 REFERENCE A24304 !$#authors Shoham, M.; Dijk, J.; Reinhardt, R.; Wittmann-Liebold, B. !$#journal FEBS Lett. (1986) 204:323-330 !$#title Purification and characterization of ribosomal proteins from !1the 30 S subunit of the extreme halophile Halobacterium !1marismortui. !$#accession A24304 !'##molecule_type protein !'##residues 2-3,'Y',5,'Y',7-18,'N',20-22 ##label SHO CLASSIFICATION #superfamily rat ribosomal protein S3 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-304 #product ribosomal protein S3 #status experimental !8#label MAT SUMMARY #length 304 #molecular-weight 33588 #checksum 9685 SEQUENCE /// ENTRY T43822 #type complete TITLE ribosomal protein S3 [validated] - Halobacterium salinarum ALTERNATE_NAMES ribosomal protein HS4 ORGANISM #formal_name Halobacterium salinarum DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 21-Jul-2000 ACCESSIONS T43822; S11598; S11609 REFERENCE Z22697 !$#authors Itoh, T. !$#submission submitted to the EMBL Data Library, September 1997 !$#accession T43822 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-302 ##label ITO !'##cross-references EMBL:AB006961; PIDN:BAA22276.1 !'##note the source is designated as Halobacterium halobium REFERENCE S11597 !$#authors Spiridonova, V.A.; Akhmanova, A.S.; Kagramanova, V.K.; !1Koepke, A.K.E.; Mankin, A.S. !$#journal Can. J. Microbiol. (1989) 35:153-159 !$#title Ribosomal protein gene cluster of Halobacterium halobium: !1nucleotide sequence of the genes coding for S3 and L29 !1equivalent ribosomal proteins. !$#cross-references MUID:89248673; PMID:2470481 !$#accession S11598 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-31,'S',33-302 ##label SPI !'##note the source is designated as Halobacterium halobium REFERENCE S11609 !$#authors Yaguchi, M.; Visentin, L.P.; Zuker, M.; Matheson, A.T.; Roy, !1C.; Strom, A.R. !$#journal Zbl. Bakt. Hyg. I. Abt. Orig. C (1982) 3:200-208 !$#title Amino-terminal sequences of ribosomal proteins from the 30S !1subunit of archaebacterium Halobacterium cutirubrum. !$#accession S11609 !'##molecule_type protein !'##residues 'S',3-9,'E',11-23,'Z',25-31,'S',33,'Z',35-41 ##label YAG !'##note the protein is designated as ribosomal protein HS4 !'##note the source is designated as Halobacterium cutirubrum GENETICS !$#note HhaS3 CLASSIFICATION #superfamily rat ribosomal protein S3 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-302 #product ribosomal protein S3 #status experimental !8#label MAT SUMMARY #length 302 #molecular-weight 33070 #checksum 6442 SEQUENCE /// ENTRY R3EC2 #type complete TITLE ribosomal protein S2 [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 01-Sep-1981 #sequence_revision 30-Jun-1991 #text_change 01-Mar-2002 ACCESSIONS A02696; S45234; A30423; JN0288; A64741 REFERENCE A02696 !$#authors An, G.; Bendiak, D.S.; Mamelak, L.A.; Friesen, J.D. !$#journal Nucleic Acids Res. (1981) 9:4163-4172 !$#title Organization and nucleotide sequence of a new ribosomal !1operon in Escherichia coli containing the genes for !1ribosomal protein S2 and elongation factor Ts. !$#cross-references MUID:82059454; PMID:6272196 !$#accession A02696 !'##molecule_type DNA !'##residues 1-241 ##label ANG !'##cross-references GB:D26562; NID:g473770; PIDN:BAA05613.1; !1PID:g473824; GB:V00343; GB:J01684; NID:g42841; !1PIDN:CAA23631.1; PID:g42842 REFERENCE S45181 !$#authors Fujita, N. !$#submission submitted to the EMBL Data Library, January 1994 !$#accession S45234 !'##molecule_type DNA !'##residues 1-241 ##label FUJ !'##cross-references EMBL:D26562; NID:g473770; PIDN:BAA05613.1; !1PID:g473824 !'##experimental_source strain K-12, substrain W3110 REFERENCE A30423 !$#authors Wittmann-Liebold, B.; Bosserhoff, A. !$#journal FEBS Lett. (1981) 129:10-16 !$#title Primary structure of protein S2 from the Escherichia coli !1ribosome. !$#cross-references MUID:82004673; PMID:7023985 !$#accession A30423 !'##molecule_type protein !'##residues 2-241 ##label WIT !'##experimental_source strain K12 REFERENCE JN0286 !$#authors Ueshima, R.; Fujita, N.; Ishihama, A. !$#journal Biochem. Biophys. Res. Commun. (1992) 184:634-639 !$#title Identification of Escherichia coli proteins cross-reacting !1with antibodies against region 2.2 peptide of RNA polymerase !1sigma subunit. !$#cross-references MUID:92246944; PMID:1575737 !$#accession JN0288 !'##molecule_type protein !'##residues 2-31 ##label UES REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64741 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-241 ##label BLAT !'##cross-references GB:AE000126; GB:U00096; NID:g1786358; !1PIDN:AAC73280.1; PID:g1786365; UWGP:b0169 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note mass spectrographic analysis of post-translational !1modifications; any acid labile modifications may have been !1missed GENETICS !$#gene rpsB !$#map_position 4 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX small subunit ribosomal proteins: S1 (PIR:R3EC1), S2 !1(PIR:R3EC2), S3 (PIR:R3EC3), S4 (PIR:R3EC4), S5 (PIR:R3EC5), !1S6 (PIR:R3EC6), S7 (PIR:R3EC7K), S8 (PIR:R3EC8), S9 !1(PIR:R3EC9), S10 (PIR:R3EC10), S11 (PIR:R3EC11), S12 !1(PIR:R3EC12), S13 (PIR:R3EC13), S14 (PIR:R3EC14), S15 !1(PIR:R3EC15), S16 (PIR:R3EC16), S17 (PIR:R3EC17), S18 !1(PIR:R3EC18), S19 (PIR:R3EC19), S20/L26 (PIR:R3EC20), S21 !1(PIR:R3EC21), S22 (PIR:C64901) [validated, MUID:99196679] FUNCTION !$#pathway protein biosynthesis CLASSIFICATION #superfamily Escherichia coli ribosomal protein S2 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-241 #product ribosomal protein S2 #status experimental !8#label MAT SUMMARY #length 241 #molecular-weight 26743 #checksum 4810 SEQUENCE /// ENTRY R3EGS2 #type complete TITLE ribosomal protein S2 - Euglena gracilis chloroplast ORGANISM #formal_name chloroplast Euglena gracilis DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 22-Jun-1999 ACCESSIONS S29797; S34532; S34899; S26089 REFERENCE S29797 !$#authors Drager, R.G.; Hallick, R.B. !$#journal Curr. Genet. (1993) 23:271-280 !$#title A novel Euglena gracilis chloroplast operon encoding four !1ATP synthase subunits and two ribosomal proteins contains 17 !1introns. !$#cross-references MUID:93169691; PMID:8435857 !$#accession S29797 !'##molecule_type DNA !'##residues 1-240 ##label DRA !'##cross-references EMBL:Z11874; NID:g14353; PIDN:CAA77928.1; !1PID:g14378 REFERENCE S34494 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.; Monfort, !1A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#submission submitted to the EMBL Data Library, January 1993 !$#description The complete sequence of the Euglena gracilis chloroplast !1genome (tentative). !$#accession S34532 !'##molecule_type DNA !'##residues 1-240 ##label HAL1 !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50111.1; !1PID:g415767 REFERENCE S34862 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.R.; !1Monfort, A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#journal Nucleic Acids Res. (1993) 21:3537-3544 !$#title Complete sequence of Euglena gracilis chloroplast DNA. !$#cross-references MUID:93347989; PMID:8346031 !$#accession S34899 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-240 ##label HAL2 !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50111.1; !1PID:g415767 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1993 GENETICS !$#gene rps2 !$#genome chloroplast !$#introns 64/2; 115/2; 140/1; 183/3 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S2 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 240 #molecular-weight 27919 #checksum 3129 SEQUENCE /// ENTRY R3LV2 #type complete TITLE ribosomal protein S2, chloroplast - liverwort (Marchantia polymorpha) chloroplast ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 22-Jun-1999 ACCESSIONS A02697; S01576 REFERENCE A00150 !$#authors Ohyama, K. !$#submission submitted to the EMBL Data Library, October 1986 !$#accession A02697 !'##molecule_type DNA !'##residues 1-235 ##label OHY REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features REFERENCE S01567 !$#authors Umesono, K.; Inokuchi, H.; Shiki, Y.; Takeuchi, M.; Chang, !1Z.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Ohyama, K.; Ozeki, !1H. !$#journal J. Mol. Biol. (1988) 203:299-331 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. II. Gene organization of the large !1single copy region from rps'12 to atpB. !$#cross-references MUID:89068686; PMID:2974085 !$#accession S01576 !'##molecule_type DNA !'##residues 1-235 ##label UME !'##cross-references GB:X04465; GB:Y00686; NID:g11640; PIDN:CAA28064.1; !1PID:g11651 GENETICS !$#gene rps2 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein S2 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 235 #molecular-weight 26777 #checksum 3591 SEQUENCE /// ENTRY R3EJ2B #type complete TITLE ribosomal protein S2, plastid - beechdrops plastid ORGANISM #formal_name plastid Epifagus virginiana #common_name beechdrops DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 22-Jun-1999 ACCESSIONS S17795; S78380 REFERENCE S17794 !$#authors Morden, C.W.; Wolfe, K.H.; dePamphilis, C.W.; Palmer, J.D. !$#journal EMBO J. (1991) 10:3281-3288 !$#title Plastid translation and transcription genes in a !1non-photosynthetic plant: intact, missing and pseudo genes. !$#cross-references MUID:92007779; PMID:1915295 !$#accession S17795 !'##molecule_type DNA !'##residues 1-237 ##label MOR !'##cross-references EMBL:X61798; NID:g11547; PIDN:CAA43901.1; !1PID:g11549 REFERENCE S78378 !$#authors Wolfe, K.H.; Morden, C.W.; Ems, S.C.; Palmer, J.D. !$#journal J. Mol. Evol. (1992) 35:304-317 !$#title Rapid evolution of the plastid translational apparatus in a !1nonphotosynthetic plant: loss or accelerated sequence !1evolution of tRNA and ribosomal protein genes. !$#cross-references MUID:93021155; PMID:1404416 !$#accession S78380 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-237 ##label WOL !'##cross-references EMBL:M81884; NID:g336917; PIDN:AAA65851.1; !1PID:g336925 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1992 GENETICS !$#gene rps2 !$#genome plastid CLASSIFICATION #superfamily Escherichia coli ribosomal protein S2 KEYWORDS plastid; protein biosynthesis; ribosome SUMMARY #length 237 #molecular-weight 26757 #checksum 3966 SEQUENCE /// ENTRY R3NT2 #type complete TITLE ribosomal protein S2, chloroplast - common tobacco chloroplast ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 30-Jan-1998 ACCESSIONS A02698 REFERENCE A00149 !$#authors Sugiura, M. !$#submission submitted to the EMBL Data Library, August 1986 !$#accession A02698 !'##molecule_type DNA !'##residues 1-236 ##label SUG !'##experimental_source cv. Bright Yellow 4 REFERENCE A38013 !$#authors Shinozaki, K.; Ohme, M.; Tanaka, M.; Wakasugi, T.; !1Hayashida, N.; Matsubayashi, T.; Zaita, N.; Chunwongse, J.; !1Obokata, J.; Yamaguchi-Shinozaki, K.; Ohto, C.; Torazawa, !1K.; Meng, B.Y.; Sugita, M.; Deno, H.; Kamogashira, T.; !1Yamada, K.; Kusuda, J.; Takaiwa, F.; Kato, A.; Tohdoh, N.; !1Shimada, H.; Sugiura, M. !$#journal EMBO J. (1986) 5:2043-2049 !$#title The complete nucleotide sequence of the tobacco chloroplast !1genome: its gene organization and expression. !$#contents annotation; gene organization, sites, features GENETICS !$#gene rps2 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein S2 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 236 #molecular-weight 26943 #checksum 6254 SEQUENCE /// ENTRY R3SP2 #type complete TITLE ribosomal protein S2, chloroplast - spinach chloroplast ORGANISM #formal_name chloroplast Spinacia oleracea #common_name spinach DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S00581 REFERENCE S00581 !$#authors Hudson, G.S.; Mason, J.G.; Holton, T.A.; Koller, B.; Cox, !1G.B.; Whitfeld, P.R.; Bottomley, W. !$#journal J. Mol. Biol. (1987) 196:283-298 !$#title A gene cluster in the spinach and pea chloroplast genomes !1encoding one CF-1 and three CF-0 subunits of the H(+)-ATP !1synthase complex and the ribosomal protein S2. !$#cross-references MUID:88011330; PMID:2443718 !$#accession S00581 !'##molecule_type DNA !'##residues 1-236 ##label HUD !'##cross-references EMBL:X05916; NID:g12255; PIDN:CAA29343.1; !1PID:g12256 GENETICS !$#gene rps2 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein S2 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 236 #molecular-weight 26696 #checksum 5284 SEQUENCE /// ENTRY R3PM2 #type complete TITLE ribosomal protein S2, chloroplast - garden pea chloroplast ORGANISM #formal_name chloroplast Pisum sativum #common_name garden pea DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S08586; S00585 REFERENCE S07137 !$#authors Cozens, A.L.; Walker, J.E. !$#journal Biochem. J. (1986) 236:453-460 !$#title Pea chloroplast DNA encodes homologues of Escherichia coli !1ribosomal subunit S2 and the beta'-subunit of RNA !1polymerase. !$#cross-references MUID:86323089; PMID:3530249 !$#accession S08586 !'##molecule_type DNA !'##residues 1-236 ##label COZ !'##cross-references EMBL:X03912; NID:g12137; PIDN:CAA27546.1; !1PID:g12138 REFERENCE S00581 !$#authors Hudson, G.S.; Mason, J.G.; Holton, T.A.; Koller, B.; Cox, !1G.B.; Whitfeld, P.R.; Bottomley, W. !$#journal J. Mol. Biol. (1987) 196:283-298 !$#title A gene cluster in the spinach and pea chloroplast genomes !1encoding one CF-1 and three CF-0 subunits of the H(+)-ATP !1synthase complex and the ribosomal protein S2. !$#cross-references MUID:88011330; PMID:2443718 !$#accession S00585 !'##molecule_type DNA !'##residues 1-52 ##label HUD !'##cross-references EMBL:X05917 GENETICS !$#gene rps2 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein S2 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 236 #molecular-weight 26842 #checksum 4520 SEQUENCE /// ENTRY R3RZ2 #type complete TITLE ribosomal protein S2, chloroplast - rice chloroplast ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 22-Jun-1999 ACCESSIONS JQ0216; S05096 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0216 !'##molecule_type DNA !'##residues 1-236 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05096 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-236 ##label HIR !'##cross-references GB:X15901; NID:g11957; PIDN:CAA33989.1; PID:g11974 !'##experimental_source cv. Nihonbare !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1989 GENETICS !$#gene rps2 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein S2 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 236 #molecular-weight 26992 #checksum 7000 SEQUENCE /// ENTRY R3ZM2 #type complete TITLE ribosomal protein S2, chloroplast - maize chloroplast ORGANISM #formal_name chloroplast Zea mays #common_name maize DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S08249; S10173; S12803; S58545 REFERENCE S08246 !$#authors Igloi, G.L.; Doery, I.; Koessel, H. !$#journal Nucleic Acids Res. (1990) 18:663 !$#title Nucleotide and derived amino acid sequence of rps2 from !1maize chloroplasts. !$#cross-references MUID:90175001; PMID:2308853 !$#accession S08249 !'##molecule_type DNA !'##residues 1-236 ##label IGL1 !'##cross-references EMBL:X17318; NID:g12479; PIDN:CAA35198.1; !1PID:g12483 REFERENCE S10172 !$#authors Stahl, D.; Rodermel, S.R.; Subramanian, A.R.; Bogorad, L. !$#journal Nucleic Acids Res. (1990) 18:3073-3074 !$#title Nucleotide sequence of a 3.46 kb region of maize chloroplast !1DNA containing the gene cluster rpoC2-rps2-atpI-atpH. !$#cross-references MUID:90272437; PMID:2140888 !$#accession S10173 !'##molecule_type DNA !'##residues 1-236 ##label STA !'##cross-references EMBL:X52270; NID:g12408; PIDN:CAA36512.1; !1PID:g12409 REFERENCE S12800 !$#authors Igloi, G.L.; Meinke, A.; Doery, I.; Koessel, H. !$#journal Mol. Gen. Genet. (1990) 221:379-394 !$#title Nucleotide sequence of the maize chloroplast rpo B/C(1)/C(2) !1operon: comparison between the derived protein primary !1structures from various organisms with respect to functional !1domains. !$#cross-references MUID:90340289; PMID:2381419 !$#accession S12803 !'##molecule_type DNA !'##residues 1-36 ##label IGL2 !'##cross-references EMBL:X17318 REFERENCE S58531 !$#authors Maier, R.M.; Neckermann, K.; Igloi, G.L.; Koessel, H. !$#journal J. Mol. Biol. (1995) 251:614-628 !$#title Complete sequence of the maize chloroplast genome: gene !1content, hotspots of divergence and fine tuning of genetic !1information by transcript editing. !$#cross-references MUID:95395841; PMID:7666415 !$#accession S58545 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-236 ##label MAI !'##cross-references EMBL:X86563; NID:g902200; PIDN:CAA60279.1; !1PID:g902215 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1995 GENETICS !$#gene rps2 !$#map_position 74.6-78.0 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein S2 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 236 #molecular-weight 26881 #checksum 7540 SEQUENCE /// ENTRY R3WT2 #type complete TITLE ribosomal protein S2, chloroplast - wheat chloroplast ORGANISM #formal_name chloroplast Triticum aestivum #common_name common wheat DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S06322 REFERENCE S06322 !$#authors Hoeglund, A.S.; Gray, J.C. !$#journal Nucleic Acids Res. (1987) 15:10590 !$#title Nucleotide sequence of the gene for ribosomal protein S2 in !1wheat chloroplast DNA. !$#cross-references MUID:88096594; PMID:3697099 !$#accession S06322 !'##molecule_type DNA !'##residues 1-236 ##label HOE !'##cross-references GB:M35396; NID:g343688; PIDN:AAA84732.1; !1PID:g552977 !'##experimental_source cv. Mardler GENETICS !$#gene rps2 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein S2 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 236 #molecular-weight 26968 #checksum 7582 SEQUENCE /// ENTRY R3EC3 #type complete TITLE ribosomal protein S3 [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1979 #sequence_revision 30-Jun-1991 #text_change 01-Mar-2002 ACCESSIONS H23129; A02699; S59051; E65124 REFERENCE A23129 !$#authors Zurawski, G.; Zurawski, S.M. !$#journal Nucleic Acids Res. (1985) 13:4521-4526 !$#title Structure of the Escherichia coli S10 ribosomal protein !1operon. !$#cross-references MUID:85242118; PMID:3892488 !$#accession H23129 !'##molecule_type DNA !'##residues 1-233 ##label ZUR !'##cross-references GB:X02613; NID:g42825; PIDN:CAA26466.1; PID:g42832 REFERENCE A02699 !$#authors Brauer, D.; Roming, R. !$#journal FEBS Lett. (1979) 106:352-357 !$#title The primary structure of protein S3 from the small ribosomal !1subunit of Escherichia coli. !$#cross-references MUID:80047253; PMID:387449 !$#accession A02699 !'##molecule_type protein !'##residues 2-233 ##label BRA !'##experimental_source strain K REFERENCE S59051 !$#authors Urlaub, H.; Kruft, V.; Bischof, O.; Mueller, E.C.; !1Wittmann-Liebold, B. !$#journal EMBO J. (1995) 14:4578-4588 !$#title Protein-rRNA binding features and their structural and !1functional implications in ribosomes as determined by !1cross-linking studies. !$#cross-references MUID:96003638; PMID:7556101 !$#accession S59051 !'##molecule_type protein !'##residues 39-49;87-108 ##label URL REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65124 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-233 ##label BLAT !'##cross-references GB:AE000408; GB:U00096; NID:g1789694; !1PIDN:AAC76339.1; PID:g1789710; UWGP:b3314 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note mass spectrographic analysis of post-translational !1modifications; any acid labile modifications may have been !1missed GENETICS !$#gene rpsC !$#map_position 73 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX small subunit ribosomal proteins: S1 (PIR:R3EC1), S2 !1(PIR:R3EC2), S3 (PIR:R3EC3), S4 (PIR:R3EC4), S5 (PIR:R3EC5), !1S6 (PIR:R3EC6), S7 (PIR:R3EC7K), S8 (PIR:R3EC8), S9 !1(PIR:R3EC9), S10 (PIR:R3EC10), S11 (PIR:R3EC11), S12 !1(PIR:R3EC12), S13 (PIR:R3EC13), S14 (PIR:R3EC14), S15 !1(PIR:R3EC15), S16 (PIR:R3EC16), S17 (PIR:R3EC17), S18 !1(PIR:R3EC18), S19 (PIR:R3EC19), S20/L26 (PIR:R3EC20), S21 !1(PIR:R3EC21), S22 (PIR:C64901) [validated, MUID:99196679] FUNCTION !$#pathway protein biosynthesis !$#note involved in binding initiator Met-tRNA CLASSIFICATION #superfamily Escherichia coli ribosomal protein S3 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-233 #product ribosomal protein S3 #status experimental !8#label MAT SUMMARY #length 233 #molecular-weight 25983 #checksum 1853 SEQUENCE /// ENTRY R3YM3C #type complete TITLE ribosomal protein S3 - Mycoplasma capricolum ALTERNATE_NAMES protein MC008 ORGANISM #formal_name Mycoplasma capricolum DATE 28-May-1986 #sequence_revision 31-Dec-1990 #text_change 07-Dec-1999 ACCESSIONS S02837; S05073; S77859; A02700; S48575 REFERENCE S02830 !$#authors Ohkubo, S.; Muto, A.; Kawauchi, Y.; Yamao, F.; Osawa, S. !$#journal Mol. Gen. Genet. (1987) 210:314-322 !$#title The ribosomal protein gene cluster of Mycoplasma capricolum. !$#cross-references MUID:88142549; PMID:3481422 !$#accession S02837 !'##molecule_type DNA !'##residues 1-233 ##label OHK !'##cross-references EMBL:X06414 !'##experimental_source ATCC 27343 REFERENCE S05072 !$#authors Muto, A. !$#submission submitted to the EMBL Data Library, January 1989 !$#accession S05073 !'##molecule_type DNA !'##residues 1-114,'RS',117-233 ##label MUT !'##cross-references EMBL:X06414; NID:g44207; PIDN:CAA29710.1; !1PID:g44215 REFERENCE S77739 !$#authors Bork, P.; Ouzounis, C.; Casari, G.; Schneider, R.; Sander, !1C.; Dolan, M.; Gilbert, W.; Gillevet, P.M. !$#journal Mol. Microbiol. (1995) 16:955-967 !$#title Exploring the Mycoplasma capricolum genome: a minimal cell !1reveals its physiology. !$#cross-references MUID:96059641; PMID:7476192 !$#accession S77859 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-119,'V',121-173,'G',175-233 ##label BOW !'##cross-references EMBL:Z33011; NID:g541684; PIDN:CAA83692.1; !1PID:g950059 !'##experimental_source ATCC 27343 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1994 GENETICS !$#gene rps3 !$#genetic_code SGC3 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S3 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 233 #molecular-weight 26262 #checksum 5072 SEQUENCE /// ENTRY R3LV3 #type complete TITLE ribosomal protein S3, chloroplast - liverwort (Marchantia polymorpha) chloroplast ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 22-Jun-1999 ACCESSIONS A02701; S01558 REFERENCE A00150 !$#authors Ohyama, K. !$#submission submitted to the EMBL Data Library, October 1986 !$#accession A02701 !'##molecule_type DNA !'##residues 1-217 ##label OHY REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features REFERENCE S01529 !$#authors Fukuzawa, H.; Kohchi, T.; Sano, T.; Shirai, H.; Umesono, K.; !1Inokuchi, H.; Ozeki, H.; Ohyama, K. !$#journal J. Mol. Biol. (1988) 203:333-351 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. III. Gene organization of the large !1single copy region from rbcL to trnI(CAU). !$#cross-references MUID:89068687; PMID:3199436 !$#accession S01558 !'##molecule_type DNA !'##residues 1-217 ##label FUK !'##cross-references GB:X04465; GB:Y00686; NID:g11640; PIDN:CAA28124.1; !1PID:g11713 GENETICS !$#gene rps3 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein S3 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 217 #molecular-weight 25055 #checksum 9544 SEQUENCE /// ENTRY R3NT3 #type complete TITLE ribosomal protein S3, chloroplast - common tobacco chloroplast ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 30-Jan-1998 ACCESSIONS A02702; E25943 REFERENCE A00149 !$#authors Sugiura, M. !$#submission submitted to the EMBL Data Library, August 1986 !$#accession A02702 !'##molecule_type DNA !'##residues 1-218 ##label SUG !'##experimental_source cv. Bright Yellow 4 REFERENCE A38013 !$#authors Shinozaki, K.; Ohme, M.; Tanaka, M.; Wakasugi, T.; !1Hayashida, N.; Matsubayashi, T.; Zaita, N.; Chunwongse, J.; !1Obokata, J.; Yamaguchi-Shinozaki, K.; Ohto, C.; Torazawa, !1K.; Meng, B.Y.; Sugita, M.; Deno, H.; Kamogashira, T.; !1Yamada, K.; Kusuda, J.; Takaiwa, F.; Kato, A.; Tohdoh, N.; !1Shimada, H.; Sugiura, M. !$#journal EMBO J. (1986) 5:2043-2049 !$#title The complete nucleotide sequence of the tobacco chloroplast !1genome: its gene organization and expression. !$#contents annotation; gene organization, sites, features REFERENCE A94118 !$#authors Tanaka, M.; Wakasugi, T.; Sugita, M.; Shinozaki, K.; !1Sugiura, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:6030-6034 !$#title Genes for the eight ribosomal proteins are clustered on the !1chloroplast genome of tobacco (Nicotiana tabacum): !1similarity to the S10 and spc operons of Escherichia coli. !$#cross-references MUID:86287388; PMID:3016736 !$#accession E25943 !'##molecule_type DNA !'##residues 1-218 ##label TAN GENETICS !$#gene rps3 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein S3 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 218 #molecular-weight 25085 #checksum 3425 SEQUENCE /// ENTRY R3SP3 #type complete TITLE ribosomal protein S3, chloroplast - spinach chloroplast ORGANISM #formal_name chloroplast Spinacia oleracea #common_name spinach DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S01978 REFERENCE S01976 !$#authors Zhou, D.X.; Quigley, F.; Massenet, O.; Mache, R. !$#journal Mol. Gen. Genet. (1989) 216:439-445 !$#title Cotranscription of the S10- and spc-like operons in spinach !1chloroplasts and identification of three of their gene !1products. !$#cross-references MUID:89313684; PMID:2747623 !$#accession S01978 !'##molecule_type DNA !'##residues 1-218 ##label ZHO !'##cross-references EMBL:X13336; NID:g12307; PIDN:CAA31715.1; !1PID:g12310 GENETICS !$#gene rps3 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein S3 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 218 #molecular-weight 24928 #checksum 2668 SEQUENCE /// ENTRY R3RZ3 #type complete TITLE ribosomal protein S3 - rice chloroplast ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 22-Jun-1999 ACCESSIONS JQ0265; S05145 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0265 !'##molecule_type DNA !'##residues 1-239 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05145 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-239 ##label HIR !'##cross-references GB:X15901; NID:g11957; PIDN:CAA33934.1; PID:g12025 !'##experimental_source cv. Nihonbare !'##note this sequence was submitted to EMBL, July 1989 GENETICS !$#gene rps3 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein S3 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 239 #molecular-weight 27518 #checksum 5969 SEQUENCE /// ENTRY R3KT3 #type complete TITLE ribosomal protein S3, cyanelle - Cyanophora paradoxa cyanelle ORGANISM #formal_name cyanelle Cyanophora paradoxa DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 22-Jun-1999 ACCESSIONS S12212; T06884 REFERENCE S12211 !$#authors Michalowski, C.B.; Pfanzagl, B.; Loeffelhardt, W.; Bohnert, !1H.J. !$#journal Mol. Gen. Genet. (1990) 224:222-231 !$#title The cyanelle S10 spc ribosomal protein gene operon from !1Cyanophora paradoxa. !$#cross-references MUID:91117189; PMID:2126059 !$#accession S12212 !'##molecule_type DNA !'##residues 1-219 ##label MIC !'##cross-references GB:M30487; NID:g336645; PIDN:AAA63621.1; !1PID:g336647 !'##experimental_source strain LB555 UTEX !'##note the authors translated the initiation codon GTG for residue 1 !1as Val REFERENCE Z15840 !$#authors Stirewalt, V.L.; Michalowski, C.B.; Luffelhardt, W.; !1Bohnert, H.J.; Bryant, D.A. !$#submission submitted to the EMBL Data Library, July 1995 !$#description Nucleotide sequence of the cyanelle genome from Cyanophora !1paradoxa. !$#accession T06884 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-219 ##label STI !'##cross-references EMBL:U30821; NID:g1016083; PIDN:AAA81227.1; !1PID:g1016140 !'##experimental_source strain Pringsheim LB555 GENETICS !$#gene rps3 !$#genome cyanelle !$#start_codon GTG CLASSIFICATION #superfamily Escherichia coli ribosomal protein S3 KEYWORDS cyanelle; protein biosynthesis; ribosome SUMMARY #length 219 #molecular-weight 25014 #checksum 7062 SEQUENCE /// ENTRY R3ZMS3 #type complete TITLE ribosomal protein S3 - maize mitochondrion ORGANISM #formal_name mitochondrion Zea mays #common_name maize DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 22-Jun-1999 ACCESSIONS S15025 REFERENCE S15025 !$#authors Hunt, M.D.; Newton, K.J. !$#journal EMBO J. (1991) 10:1045-1052 !$#title The NCS3 mutation: genetic evidence for the expression of !1ribosomal protein genes in Zea mays mitochondria. !$#cross-references MUID:91216097; PMID:1708720 !$#accession S15025 !'##molecule_type DNA !'##residues 1-559 ##label HUN !'##cross-references EMBL:X57445; NID:g13920; PIDN:CAA40690.1; !1PID:g13921 GENETICS !$#genome mitochondrion !$#introns 25/2 CLASSIFICATION #superfamily maize mitochondrion ribosomal protein S3 KEYWORDS mitochondrion; protein biosynthesis; ribosome SUMMARY #length 559 #molecular-weight 64233 #checksum 235 SEQUENCE /// ENTRY S31847 #type complete TITLE ribosomal protein S3 - garden petunia mitochondrion ORGANISM #formal_name mitochondrion Petunia x hybrida #common_name garden petunia DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S31847; S31647 REFERENCE S31847 !$#authors Sutton, C.A.; Conklin, P.L.; Pruitt, K.D.; Jay Calfee, A.; !1Cobb, A.G.; Hanson, M.R. !$#journal Curr. Genet. (1993) 23:472-476 !$#title Editing of rps3/rpl16 transcripts creates a premature !1truncation of the rpl16 open reading frame. !$#cross-references MUID:93306753; PMID:8319305 !$#accession S31847 !'##molecule_type DNA !'##residues 1-562 ##label SUT !'##cross-references EMBL:X67028; NID:g14162; PIDN:CAA47420.1; !1PID:g14163 GENETICS !$#gene rps3 !$#genome mitochondrion !$#introns 24/3 CLASSIFICATION #superfamily maize mitochondrion ribosomal protein S3 KEYWORDS mitochondrion; protein biosynthesis; ribosome SUMMARY #length 562 #molecular-weight 64850 #checksum 2443 SEQUENCE /// ENTRY S36913 #type complete TITLE ribosomal protein S3 - rape mitochondrion ORGANISM #formal_name mitochondrion Brassica napus #common_name rape DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S36913 REFERENCE S36913 !$#authors Ye, F.; Bernhardt, J.; Abel, W.O. !$#journal Curr. Genet. (1993) 24:323-329 !$#title Genes for ribosomal proteins S3, L16, L5 and S14 are !1clustered in the mitochondrial genome of Brassica napus L. !$#cross-references MUID:94073988; PMID:8252643 !$#accession S36913 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-555 ##label YEF GENETICS !$#gene rps3 !$#genome mitochondrion CLASSIFICATION #superfamily maize mitochondrion ribosomal protein S3 KEYWORDS mitochondrion; protein biosynthesis; ribosome SUMMARY #length 555 #molecular-weight 64090 #checksum 9670 SEQUENCE /// ENTRY R3RT4 #type complete TITLE ribosomal protein S4, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1990 #sequence_revision 30-Jun-1991 #text_change 21-Jul-2000 ACCESSIONS S14080; S13073; S04971; S11413 REFERENCE S14080 !$#authors Wool, I.G. !$#submission submitted to the EMBL Data Library, October 1990 !$#accession S14080 !'##molecule_type mRNA !'##residues 1-263 ##label WO1 !'##cross-references EMBL:X14210; NID:g57134; PIDN:CAA32427.1; !1PID:g57135 REFERENCE S13071 !$#authors Wool, I.G.; Chan, Y.L.; Paz, V.; Olvera, J. !$#journal Biochim. Biophys. Acta (1990) 1050:69-73 !$#title The primary structure of rat ribosomal proteins: the amino !1acid sequences of L27a and L28 and corrections in the !1sequences of S4 and S12. !$#cross-references MUID:91002678; PMID:2207170 !$#accession S13073 !'##molecule_type mRNA !'##residues 1-212,'R',214-263 ##label WO2 !'##cross-references EMBL:X14210 !'##note this sequence has been revised in reference S14080 !'##note the protein is designated as ribosomal protein S4 REFERENCE S04971 !$#authors Devi, K.R.G.; Chan, Y.L.; Wool, I.G. !$#journal Biochim. Biophys. Acta (1989) 1008:258-262 !$#title The primary structure of rat ribosomal protein S4. !$#cross-references MUID:89287337; PMID:2660908 !$#accession S04971 !'##molecule_type mRNA !'##residues 1-212,'R',214-258,'NRAVGEMVSRRHAGGVFVPQHNKPF' ##label DEV !'##cross-references EMBL:X14210 !'##note this sequence has been revised in references S13071 and S14080 !'##note the difference at the carboxyl end is due to a frameshift error !'##note the protein is designated as ribosomal protein S4 REFERENCE S11413 !$#authors Wittmann-Liebold, B.; Geissler, A.W.; Lin, A.; Wool, I.G. !$#journal J. Supramol. Struct. (1979) 12:425-433 !$#title Sequence of the amino-terminal region of rat liver ribosomal !1proteins S4, S6, S8, L6, L7a, L18, L27, L30, L37, L37a, and !1L39. !$#cross-references MUID:80252792; PMID:398910 !$#accession S11413 !'##molecule_type protein !'##residues 2-23,'L',25,'FV',28-29,'T',31,'KL',34-35,'D',37-38 ##label !1WIT !'##note the protein is designated as ribosomal protein S4 CLASSIFICATION #superfamily rat ribosomal protein S4 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-263 #product ribosomal protein S4 #status experimental !8#label MAT SUMMARY #length 263 #molecular-weight 29597 #checksum 1095 SEQUENCE /// ENTRY R3HU4X #type complete TITLE ribosomal protein S4.X - human ALTERNATE_NAMES ribosomal protein S4, cytosolic; scar protein ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 22-Jun-1999 ACCESSIONS B36338; S07411; S15007; A53254; S68931 REFERENCE A36338 !$#authors Fisher, E.M.C.; Beer-Romero, P.; Brown, L.G.; Ridley, A.; !1McNeil, J.A.; Lawrence, J.B.; Willard, H.F.; Bieber, F.R.; !1Page, D.C. !$#journal Cell (1990) 63:1205-1218 !$#title Homologous ribosomal protein genes on the human X and Y !1chromosomes: escape from X inactivation and possible !1implications for Turner syndrome. !$#cross-references MUID:91084849; PMID:2124517 !$#accession B36338 !'##molecule_type mRNA !'##residues 1-263 ##label FIS !'##cross-references EMBL:M58458; NID:g337509; PIDN:AAA63255.1; !1PID:g337510 REFERENCE S07411 !$#authors Wiles, M.V.; Alexander, C.M.; Goodfellow, P.N. !$#journal Somat. Cell Mol. Genet. (1988) 14:31-39 !$#title Isolation of an abundantly expressed sequence from the human !1X chromosome by differential screening. !$#cross-references MUID:88127321; PMID:2829364 !$#accession S07411 !'##molecule_type mRNA !'##residues 19-263 ##label WIL1 !'##cross-references EMBL:M22146; NID:g337929 REFERENCE S15007 !$#authors Wiles, M.V. !$#submission submitted to the EMBL Data Library, January 1989 !$#accession S15007 !'##molecule_type mRNA !'##residues 19-32,34-263 ##label WIL2 !'##cross-references EMBL:M22146; NID:g337929; PIDN:AAA36597.1; !1PID:g337930 REFERENCE A53254 !$#authors Watanabe, M.; Furuno, N.; Goebl, M.; Go, M.; Miyauchi, K.; !1Sekiguchi, T.; Basilico, C.; Nishimito, T. !$#journal J. Cell Sci. (1991) 100:35-43 !$#title Molecular cloning of the human gene, CCG2, that complements !1the BHK-derived temperature-sensitive cell cycle mutant !1tsBN63: identity of CCG2 with the human X chromosomal SCAR/ !1RPS4X gene. !$#cross-references MUID:92176277; PMID:1795030 !$#accession A53254 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-9,11-263 ##label WAT REFERENCE S68911 !$#authors Vladimirov, S.N.; Ivanov, A.V.; Karpova, G.G.; Musolyamov, !1A.K.; Egorov, T.A.; Thiede, B.; Wittmann-Liebold, B.; Otto, !1A. !$#journal Eur. J. Biochem. (1996) 239:144-149 !$#title Characterization of the human small-ribosomal-subunit !1proteins by N-terminal and internal sequencing, and mass !1spectrometry. !$#cross-references MUID:96305378; PMID:8706699 !$#accession S68931 !'##molecule_type protein !'##residues 2-15 ##label VLA COMMENT For the Y chromosome gene sequence version see PIR:R3HU4Y. GENETICS !$#gene GDB:RPS4X; DXS306; CCG2 !'##cross-references GDB:128115; OMIM:312760 !$#map_position Xq13.1-Xq13.1 CLASSIFICATION #superfamily rat ribosomal protein S4 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-263 #product ribosomal protein S4.X #status predicted !8#label MAT SUMMARY #length 263 #molecular-weight 29597 #checksum 1095 SEQUENCE /// ENTRY R3HU4Y #type complete TITLE ribosomal protein S4.Y - human ALTERNATE_NAMES ribosomal protein S4, cytosolic ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 22-Jun-1999 ACCESSIONS A36338 REFERENCE A36338 !$#authors Fisher, E.M.C.; Beer-Romero, P.; Brown, L.G.; Ridley, A.; !1McNeil, J.A.; Lawrence, J.B.; Willard, H.F.; Bieber, F.R.; !1Page, D.C. !$#journal Cell (1990) 63:1205-1218 !$#title Homologous ribosomal protein genes on the human X and Y !1chromosomes: escape from X inactivation and possible !1implications for Turner syndrome. !$#cross-references MUID:91084849; PMID:2124517 !$#accession A36338 !'##molecule_type mRNA !'##residues 1-263 ##label FIS !'##cross-references EMBL:M58459; NID:g337511; PIDN:AAA63256.1; !1PID:g337512 COMMENT For the X chromosome gene sequence version see PIR:R3HU4X. GENETICS !$#gene GDB:RPS4Y !'##cross-references GDB:128052; OMIM:470000 !$#map_position Yp11.3-Yp11.3 CLASSIFICATION #superfamily rat ribosomal protein S4 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-263 #product ribosomal protein S4.Y #status predicted !8#label MAT SUMMARY #length 263 #molecular-weight 29455 #checksum 4693 SEQUENCE /// ENTRY R3MX4 #type complete TITLE ribosomal protein S4.eR - Methanococcus vannielii ALTERNATE_NAMES ribosomal protein C ORGANISM #formal_name Methanococcus vannielii DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 22-Jun-1999 ACCESSIONS S05616 REFERENCE S05611 !$#authors Auer, J.; Spicker, G.; Boeck, A. !$#journal J. Mol. Biol. (1989) 209:21-36 !$#title Organization and structure of the Methanococcus !1transcriptional unit homologous to the Escherichia coli !1"spectinomycin operon". Implications for the evolutionary !1relationship of 70 S and 80 S ribosomes. !$#cross-references MUID:90040717; PMID:2530355 !$#accession S05616 !'##molecule_type DNA !'##residues 1-244 ##label AUE !'##cross-references EMBL:X16720; NID:g44754; PIDN:CAA34692.1; !1PID:g44760 CLASSIFICATION #superfamily rat ribosomal protein S4 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 244 #molecular-weight 27325 #checksum 4076 SEQUENCE /// ENTRY R3HS4 #type complete TITLE ribosomal protein S4.eR [similarity] - Haloarcula marismortui ALTERNATE_NAMES ribosomal protein HS3 ORGANISM #formal_name Haloarcula marismortui DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 31-Mar-2000 ACCESSIONS S10736; T46799 REFERENCE S10731 !$#authors Arndt, E. !$#journal FEBS Lett. (1990) 267:193-198 !$#title Nucleotide sequence of four genes encoding ribosomal !1proteins from the 'S10 and spectinomycin' operon equivalent !1region in the archaebacterium Halobacterium marismortui. !$#cross-references MUID:90336772; PMID:2143141 !$#accession S10736 !'##molecule_type DNA !'##residues 1-234 ##label ARN !'##cross-references EMBL:X55311; NID:g43610; PIDN:CAA39020.1; !1PID:g43616 !'##note the source is designated as Halobacterium marismortui CLASSIFICATION #superfamily rat ribosomal protein S4 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-234 #product ribosomal protein S4.eR #status predicted !8#label MAT SUMMARY #length 234 #molecular-weight 25247 #checksum 233 SEQUENCE /// ENTRY R3EC4 #type complete TITLE ribosomal protein S4 [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 29-Jul-1981 #sequence_revision 30-Jun-1991 #text_change 01-Mar-2002 ACCESSIONS C23807; A02703; A30417; S59052; I57736; I77540; I77542; !1C65122 REFERENCE A23807 !$#authors Bedwell, D.; Davis, G.; Gosink, M.; Post, L.; Nomura, M.; !1Kestler, H.; Zengel, J.M.; Lindahl, L. !$#journal Nucleic Acids Res. (1985) 13:3891-3903 !$#title Nucleotide sequence of the alpha ribosomal protein operon of !1Escherichia coli. !$#cross-references MUID:85242076; PMID:2989779 !$#accession C23807 !'##molecule_type DNA !'##residues 1-206 ##label BED !'##cross-references GB:X02543; NID:g42795; PIDN:CAA26394.1; PID:g42798 REFERENCE A02703 !$#authors Schiltz, E.; Reinbolt, J. !$#journal Eur. J. Biochem. (1975) 56:467-481 !$#title Determination of the complete amino-acid sequence of protein !1S4 from Escherichia coli ribosomes. !$#cross-references MUID:76022479; PMID:1100394 !$#accession A02703 !'##molecule_type protein !'##residues 2-89,91-94,'Q',96-137,'D',139-140,'S',142-143,145-151,'E', !1153-165,'Q',167-206 ##label SCH !'##experimental_source strain K REFERENCE A30417 !$#authors Reinbolt, J.; Schiltz, E. !$#journal FEBS Lett. (1973) 36:250-252 !$#title The primary structure of ribosomal protein S4 from !1Escherichia coli. !$#cross-references MUID:74054994; PMID:4587210 !$#accession A30417 !'##molecule_type protein !'##residues 2-89,91-94,'Q',96-137,'D',139-140,'S',142-143,145-151,'E', !1153-165,'Q',167-206 ##label REI !'##experimental_source strain ab774 REFERENCE S59051 !$#authors Urlaub, H.; Kruft, V.; Bischof, O.; Mueller, E.C.; !1Wittmann-Liebold, B. !$#journal EMBO J. (1995) 14:4578-4588 !$#title Protein-rRNA binding features and their structural and !1functional implications in ribosomes as determined by !1cross-linking studies. !$#cross-references MUID:96003638; PMID:7556101 !$#accession S59052 !'##molecule_type protein !'##residues 78-91 ##label URL REFERENCE A30438 !$#authors Reinbolt, J. !$#submission submitted to the Atlas, February 1975 !$#contents annotation; strain ab774, revision to residue 166 REFERENCE I57736 !$#authors Schnier, J.; Isono, S.; Cumberlidge, A.G.; Isono, K. !$#journal Mol. Gen. Genet. (1985) 199:265-270 !$#title Unstable mutations caused by regional tandem multiplications !1in the gene for ribosomal protein S4 show thermosensitivity !1in Escherichia coli. !$#cross-references MUID:85267249; PMID:3894886 !$#accession I57736 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 147-166,'SRSGAG' ##label SCH1 !'##cross-references GB:M29822; NID:g147735; PIDN:AAA24589.1; !1PID:g147736 !$#accession I77540 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 147-177,'SV',183,'SQ',186,'GWKLML',193,'RA' ##label SCH2 !'##cross-references GB:M29823; NID:g147738; PIDN:AAA24591.1; !1PID:g147739 !$#accession I77542 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 147-157,'SGAG' ##label SCH3 !'##cross-references GB:M29824; NID:g147741; PIDN:AAA24593.1; !1PID:g147742 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65122 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-206 ##label BLAT !'##cross-references GB:AE000407; GB:U00096; NID:g2367211; !1PIDN:AAC76321.1; PID:g1789691; UWGP:b3296 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note mass spectrographic analysis of post-translational !1modifications; any acid labile modifications may have been !1missed GENETICS !$#gene rpsD !$#map_position 73 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX small subunit ribosomal proteins: S1 (PIR:R3EC1), S2 !1(PIR:R3EC2), S3 (PIR:R3EC3), S4 (PIR:R3EC4), S5 (PIR:R3EC5), !1S6 (PIR:R3EC6), S7 (PIR:R3EC7K), S8 (PIR:R3EC8), S9 !1(PIR:R3EC9), S10 (PIR:R3EC10), S11 (PIR:R3EC11), S12 !1(PIR:R3EC12), S13 (PIR:R3EC13), S14 (PIR:R3EC14), S15 !1(PIR:R3EC15), S16 (PIR:R3EC16), S17 (PIR:R3EC17), S18 !1(PIR:R3EC18), S19 (PIR:R3EC19), S20/L26 (PIR:R3EC20), S21 !1(PIR:R3EC21), S22 (PIR:C64901) [validated, MUID:99196679] FUNCTION !$#pathway protein biosynthesis !$#note binds 16S rRNA CLASSIFICATION #superfamily Escherichia coli ribosomal protein S4 KEYWORDS protein biosynthesis; ribosome; RNA binding FEATURE !$2-206 #product ribosomal protein S4 #status experimental !8#label MAT SUMMARY #length 206 #molecular-weight 23469 #checksum 5266 SEQUENCE /// ENTRY A37146 #type complete TITLE ribosomal protein S4 - Bacillus subtilis ALTERNATE_NAMES ribosomal protein BS4 (rpsD) ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A37146; A44901; S11354; C69699; I39962 REFERENCE A37146 !$#authors Grundy, F.J.; Henkin, T.M. !$#journal J. Bacteriol. (1990) 172:6372-6379 !$#title Cloning and analysis of the Bacillus subtilis rpsD gene, !1encoding ribosomal protein S4. !$#cross-references MUID:91035248; PMID:1699930 !$#accession A37146 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-200 ##label GRU1 !'##cross-references GB:M59358; GB:M34718; NID:g143466; PIDN:AAA22717.1; !1PID:g143467 REFERENCE A44901 !$#authors Grundy, F.J.; Henkin, T.M. !$#journal J. Bacteriol. (1991) 173:4595-4602 !$#title The rpsD gene, encoding ribosomal protein S4, is !1autogenously regulated in Bacillus subtilis. !$#cross-references MUID:91310564; PMID:1906866 !$#accession A44901 !'##status preliminary !'##molecule_type DNA !'##residues 1-57 ##label GRU2 !'##cross-references GB:S45404; NID:g1679974; PIDN:AAB19387.1; !1PID:g233162 !'##note sequence extracted from NCBI backbone (NCBIN:45404, !1NCBIP:45408) REFERENCE S09561 !$#authors Higo, K.I.; Otaka, E.; Osawa, S. !$#journal Mol. Gen. Genet. (1982) 185:239-244 !$#title Purification and characterization of 30S ribosomal proteins !1from Bacillus subtilis: correlation to Escherichia coli 30S !1proteins. !$#cross-references MUID:82219212; PMID:6806564 !$#accession S11354 !'##molecule_type protein !'##residues 2-25 ##label HIG REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69699 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-200 ##label KUN !'##cross-references GB:Z99119; GB:AL009126; NID:g2635411; !1PIDN:CAB14944.1; PID:g2635450 !'##experimental_source strain 168 REFERENCE I39962 !$#authors Henkin, T.M.; Chambliss, G.H.; Grundy, F.J. !$#journal J. Bacteriol. (1990) 172:6380-6385 !$#title Bacillus subtilis mutants with alternations in ribosomal !1protein S4. !$#cross-references MUID:91035249; PMID:2121712 !$#accession I39962 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 71-81,'LAGK',82-84 ##label RES !'##cross-references GB:M60889; NID:g143464; PIDN:AAA22716.1; !1PID:g143465 !'##note mutant protein GENETICS !$#gene rpsD CLASSIFICATION #superfamily Escherichia coli ribosomal protein S4 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-200 #product ribosomal protein S4 #status experimental !8#label MAT SUMMARY #length 200 #molecular-weight 22835 #checksum 4002 SEQUENCE /// ENTRY R3LV4 #type complete TITLE ribosomal protein S4, chloroplast - liverwort (Marchantia polymorpha) chloroplast ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 22-Jun-1999 ACCESSIONS A02704; S01602 REFERENCE A00150 !$#authors Ohyama, K. !$#submission submitted to the EMBL Data Library, October 1986 !$#accession A02704 !'##molecule_type DNA !'##residues 1-202 ##label OHY REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features REFERENCE S01567 !$#authors Umesono, K.; Inokuchi, H.; Shiki, Y.; Takeuchi, M.; Chang, !1Z.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Ohyama, K.; Ozeki, !1H. !$#journal J. Mol. Biol. (1988) 203:299-331 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. II. Gene organization of the large !1single copy region from rps'12 to atpB. !$#cross-references MUID:89068686; PMID:2974085 !$#accession S01602 !'##molecule_type DNA !'##residues 1-202 ##label UME !'##cross-references GB:X04465; GB:Y00686; NID:g11640; PIDN:CAA28086.1; !1PID:g11674 GENETICS !$#gene rps4 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein S4 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 202 #molecular-weight 23640 #checksum 1372 SEQUENCE /// ENTRY R3NT4 #type complete TITLE ribosomal protein S4, chloroplast - common tobacco chloroplast ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 30-Jan-1998 ACCESSIONS A02705 REFERENCE A00149 !$#authors Sugiura, M. !$#submission submitted to the EMBL Data Library, August 1986 !$#accession A02705 !'##molecule_type DNA !'##residues 1-201 ##label SUG !'##experimental_source cv. Bright Yellow 4 REFERENCE A38013 !$#authors Shinozaki, K.; Ohme, M.; Tanaka, M.; Wakasugi, T.; !1Hayashida, N.; Matsubayashi, T.; Zaita, N.; Chunwongse, J.; !1Obokata, J.; Yamaguchi-Shinozaki, K.; Ohto, C.; Torazawa, !1K.; Meng, B.Y.; Sugita, M.; Deno, H.; Kamogashira, T.; !1Yamada, K.; Kusuda, J.; Takaiwa, F.; Kato, A.; Tohdoh, N.; !1Shimada, H.; Sugiura, M. !$#journal EMBO J. (1986) 5:2043-2049 !$#title The complete nucleotide sequence of the tobacco chloroplast !1genome: its gene organization and expression. !$#contents annotation; gene organization, sites, features GENETICS !$#gene rps4 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein S4 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 201 #molecular-weight 23420 #checksum 7363 SEQUENCE /// ENTRY R3ZM4 #type complete TITLE ribosomal protein S4 - maize chloroplast ORGANISM #formal_name chloroplast Zea mays #common_name maize DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 22-Jun-1999 ACCESSIONS A02706; S58554 REFERENCE A02706 !$#authors Subramanian, A.R.; Steinmetz, A.; Bogorad, L. !$#journal Nucleic Acids Res. (1983) 11:5277-5286 !$#title Maize chloroplast DNA encodes a protein sequence homologous !1to the bacterial ribosome assembly protein S4. !$#cross-references MUID:83272969; PMID:6308577 !$#accession A02706 !'##molecule_type DNA !'##residues 1-201 ##label SUB !'##cross-references GB:X01608; NID:g12411; PIDN:CAA25754.1; PID:g12412 REFERENCE S58531 !$#authors Maier, R.M.; Neckermann, K.; Igloi, G.L.; Koessel, H. !$#journal J. Mol. Biol. (1995) 251:614-628 !$#title Complete sequence of the maize chloroplast genome: gene !1content, hotspots of divergence and fine tuning of genetic !1information by transcript editing. !$#cross-references MUID:95395841; PMID:7666415 !$#accession S58554 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-201 ##label MAI !'##cross-references EMBL:X86563; NID:g902200; PIDN:CAA60288.1; !1PID:g902224 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1995 GENETICS !$#gene rps4 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein S4 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 201 #molecular-weight 23463 #checksum 9499 SEQUENCE /// ENTRY R3RZ4 #type complete TITLE ribosomal protein S4, chloroplast - rice chloroplast ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 22-Jun-1999 ACCESSIONS JQ0225; S05105 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0225 !'##molecule_type DNA !'##residues 1-201 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05105 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-201 ##label HIR !'##cross-references GB:X15901; NID:g11957; PIDN:CAA33998.1; PID:g11986 !'##experimental_source cv. Nihonbare !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1989 GENETICS !$#gene rps4 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein S4 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 201 #molecular-weight 23422 #checksum 8309 SEQUENCE /// ENTRY R3MD4 #type complete TITLE ribosomal protein S4, chloroplast - Cryptomonas sp. chloroplast (strain phi) ORGANISM #formal_name chloroplast Cryptomonas sp. #variety strain phi DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 30-Jan-1998 ACCESSIONS S09219 REFERENCE S09219 !$#authors Douglas, S.E.; Durnford, D.G. !$#journal Nucleic Acids Res. (1990) 18:1903 !$#title Nucleotide sequence of the genes for ribosomal protein S4 !1and tRNA-Arg from the chlorophyll c-containing alga !1Cryptomonas Phi. !$#cross-references MUID:90245597; PMID:2336372 !$#accession S09219 !'##molecule_type DNA !'##residues 1-200 ##label DOU !'##cross-references EMBL:X51511; NID:g18103; PID:g18104 GENETICS !$#gene rps4 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein S4 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 200 #molecular-weight 22846 #checksum 2959 SEQUENCE /// ENTRY S21497 #type complete TITLE ribosomal protein S9, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 21-Jul-2000 ACCESSIONS JN0587; PN0499; S21497 REFERENCE JN0587 !$#authors Chan, Y.L.; Paz, V.; Olvera, J.; Wool, I.G. !$#journal Biochem. Biophys. Res. Commun. (1993) 193:106-112 !$#title The primary structure of rat ribosomal protein S9. !$#cross-references MUID:93277536; PMID:8503895 !$#accession JN0587 !'##molecule_type mRNA !'##residues 1-194 ##label CHA !'##cross-references EMBL:X66370; NID:g57142; PIDN:CAA47013.1; !1PID:g57143 !$#accession PN0499 !'##molecule_type protein !'##residues 2-28;93-122 ##label CHN !'##note the protein is designated as ribosomal protein S9 CLASSIFICATION #superfamily rat ribosomal protein S9 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-194 #product ribosomal protein S9 #status predicted !8#label RPS SUMMARY #length 194 #molecular-weight 22505 #checksum 9051 SEQUENCE /// ENTRY R3DO24 #type complete TITLE ribosomal protein S9.e - slime mold (Dictyostelium discoideum) ALTERNATE_NAMES ribosomal protein 1024; ribosomal protein V12 ORGANISM #formal_name Dictyostelium discoideum DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 22-Jun-1999 ACCESSIONS S01093; S07566 REFERENCE S01093 !$#authors Steel, L.F.; Smyth, A.; Jacobson, A. !$#journal Nucleic Acids Res. (1987) 15:10285-10298 !$#title Nucleotide sequence and characterization of the transcript !1of a Dictyostelium ribosomal protein gene. !$#cross-references MUID:88096567; PMID:2827119 !$#accession S01093 !'##molecule_type DNA !'##residues 1-185 ##label STE !'##cross-references EMBL:X06636; NID:g7352; PIDN:CAA29844.1; PID:g7353 REFERENCE S07566 !$#authors Singleton, C.K.; Manning, S.S.; Ken, R. !$#submission submitted to the EMBL Data Library, May 1989 !$#description Primary structure and regulation of vegetative specific !1genes of Dictyostelium discoideum. !$#accession S07566 !'##molecule_type mRNA !'##residues 'FHQ',65-181 ##label SIN !'##cross-references EMBL:X15384 GENETICS !$#introns 4/3 CLASSIFICATION #superfamily rat ribosomal protein S9 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 185 #molecular-weight 21204 #checksum 6655 SEQUENCE /// ENTRY S16822 #type complete TITLE ribosomal protein S9.e.A, cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein LPF4_b; protein YPL081w; ribosomal protein YP28; ribosomal protein YS11 ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jun-2000 ACCESSIONS S16822; S11577; S78222 REFERENCE S16822 !$#authors Mizuta, K.; Hashimoto, T.; Suzuki, K.; Otaka, E. !$#journal Nucleic Acids Res. (1991) 19:2603-2608 !$#title Yeast ribosomal proteins: XII. YS11 of Saccharomyces !1cerevisiae is a homologue to E.coli S4 according to the gene !1analysis. !$#cross-references MUID:91252202; PMID:2041737 !$#accession S16822 !'##molecule_type DNA !'##residues 1-197 ##label MIZ !'##cross-references EMBL:D00724; NID:g218514; PIDN:BAA00626.1; !1PID:g218515 REFERENCE S11575 !$#authors Otaka, E.; Higo, K.; Osawa, S. !$#journal Biochemistry (1982) 21:4545-4550 !$#title Isolation of seventeen proteins and amino-terminal amino !1acid sequences of eight proteins from cytoplasmic ribosomes !1of yeast. !$#cross-references MUID:83048950; PMID:6814480 !$#accession S11577 !'##molecule_type protein !'##residues 2-19,'Q',22,'B',23-24 ##label OTA REFERENCE S59677 !$#authors Hall, J.; Ahmed, A.; Bussey, H.; Fortin, N.; Friesen, J.D.; !1Storms, R.K.; Vo, D.H.; Wang, Y.; Winnett, E. !$#submission submitted to the EMBL Data Library, August 1995 !$#description The sequence of Saccharomyces cerevisiae chromosome XVI left !1arm. !$#accession S78222 !'##molecule_type DNA !'##residues 1-197 ##label HAL !'##cross-references EMBL:U41849; NID:g1147608; PIDN:AAB68268.1; !1PID:g2347168; GSPDB:GN00016; MIPS:YPL081w GENETICS !$#gene YS11A; RPS13B; MIPS:YPL081w !'##cross-references MIPS:YPL081w; SGD:S0006002 !$#map_position 16L !$#introns 3/1 CLASSIFICATION #superfamily rat ribosomal protein S9 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-197 #product ribosomal protein S9.e.A #status !8experimental #label MAT SUMMARY #length 197 #molecular-weight 22443 #checksum 3081 SEQUENCE /// ENTRY T43938 #type complete TITLE ribosomal protein S4 [validated] - Halobacterium salinarum ALTERNATE_NAMES ribosomal protein HS9 ORGANISM #formal_name Halobacterium salinarum DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 21-Jul-2000 ACCESSIONS T43938; S11612 REFERENCE Z22729 !$#authors Sano, K.; Taguchi, A.; Furumoto, H.; Uda, T.; Itoh, T. !$#journal Biochem. Biophys. Res. Commun. (1999) 264:24-28 !$#title Cloning, sequencing, and characterization of ribosomal !1protein and RNA polymerase genes from the region analogous !1to the alpha-operon of Escherichia coli in halophilic !1archaea, Halobacterium halobium. !$#cross-references MUID:99458614; PMID:10527834 !$#accession T43938 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-169 ##label SAN !'##cross-references EMBL:AB030282; PIDN:BAA85896.1 !'##note the source is designated as Halobacterium halobium REFERENCE S11609 !$#authors Yaguchi, M.; Visentin, L.P.; Zuker, M.; Matheson, A.T.; Roy, !1C.; Strom, A.R. !$#journal Zbl. Bakt. Hyg. I. Abt. Orig. C (1982) 3:200-208 !$#title Amino-terminal sequences of ribosomal proteins from the 30S !1subunit of archaebacterium Halobacterium cutirubrum. !$#accession S11612 !'##molecule_type protein !'##residues 2-20,'Z',22-27,'B',29-30,'ZK',33,'ZK',26,'D' ##label YAG !'##note the protein is designated as ribosomal protein HS9 !'##note the source is designated as Halobacterium cutirubrum CLASSIFICATION #superfamily rat ribosomal protein S9 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-169 #product ribosomal protein S4 #status experimental !8#label MAT SUMMARY #length 169 #molecular-weight 19224 #checksum 1507 SEQUENCE /// ENTRY B44126 #type complete TITLE ribosomal protein S4 [similarity] - Haloarcula marismortui ALTERNATE_NAMES ribosomal protein HmaS4 ORGANISM #formal_name Haloarcula marismortui DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 21-Jul-2000 ACCESSIONS B44126 REFERENCE A44126 !$#authors Scholzen, T.; Arndt, E. !$#journal J. Biol. Chem. (1992) 267:12123-12130 !$#title The alpha-operon equivalent genome region in the extreme !1halophilic archaebacterium Haloarcula (Halobacterium) !1marismortui. !$#cross-references MUID:92291093; PMID:1376318 !$#accession B44126 !'##status preliminary !'##molecule_type DNA !'##residues 1-171 ##label SCH !'##cross-references GB:M87833; NID:g148769; PIDN:AAA73210.1; !1PID:g148771 !'##note sequence extracted from NCBI backbone (NCBIN:106619, !1NCBIP:106621) CLASSIFICATION #superfamily rat ribosomal protein S9 SUMMARY #length 171 #molecular-weight 19541 #checksum 8349 SEQUENCE /// ENTRY R3SPS5 #type complete TITLE ribosomal protein CS-S22 precursor, chloroplast - spinach ALTERNATE_NAMES ribosomal protein CS-S5; ribosomal protein Psrp-1 ORGANISM #formal_name Spinacia oleracea #common_name spinach DATE 31-Mar-1991 #sequence_revision 31-Mar-1993 #text_change 22-Jun-1999 ACCESSIONS S19131; A36613; JQ0348; S11763 REFERENCE S19131 !$#authors Bisanz-Seyer, C.; Mache, R. !$#journal Plant Mol. Biol. (1992) 18:337-344 !$#title Organization and expression of the nuclear gene coding for !1the plastid-specific S22 ribosomal protein from spinach. !$#cross-references MUID:92119254; PMID:1731992 !$#accession S19131 !'##molecule_type DNA !'##residues 1-302 ##label BIS !'##cross-references EMBL:X59270; NID:g12315; PIDN:CAA41960.1; !1PID:g12316 REFERENCE A36613 !$#authors Johnson, C.H.; Kruft, V.; Subramanian, A.R. !$#journal J. Biol. Chem. (1990) 265:12790-12795 !$#title Identification of a plastid-specific ribosomal protein in !1the 30 S subunit of chloroplast ribosomes and isolation of !1the cDNA clone encoding its cytoplasmic precursor. !$#cross-references MUID:90330608; PMID:2376575 !$#accession A36613 !'##molecule_type mRNA !'##residues 1-28,'L',30-302 ##label JOH !'##cross-references EMBL:M55322; NID:g170130; PIDN:AAA34039.1; !1PID:g170131 REFERENCE JQ0348 !$#authors Zhou, D.X.; Mache, R. !$#journal Mol. Gen. Genet. (1989) 219:204-208 !$#title Presence in the stroma of chloroplasts of a large pool of a !1ribosomal protein not structurally related to any !1Escherichia coli ribosomal protein. !$#cross-references MUID:90136508; PMID:2693942 !$#accession JQ0348 !'##molecule_type mRNA !'##residues 1-28,'L',30-117,'S',119-203 ##label ZHO1 !'##cross-references GB:X15344 !'##note the nucleotide sequence contains a frameshift in codon 204; the !1revised sequence is given in reference S11763 REFERENCE S11763 !$#authors Zhou, D.X.; Mache, R. !$#journal Mol. Gen. Genet. (1990) 223:167 !$#cross-references MUID:91080860; PMID:2259340 !$#contents erratum !$#accession S11763 !'##molecule_type mRNA !'##residues 201-302 ##label ZHO2 GENETICS !$#gene rps22 !$#introns 85/3; 133/3; 224/3; 261/1 CLASSIFICATION #superfamily spinach chloroplast ribosomal protein CS-S5 KEYWORDS chloroplast; protein biosynthesis; ribosome FEATURE !$1-65 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$66-302 #product ribosomal protein CS-S22 #status predicted !8#label MAT SUMMARY #length 302 #molecular-weight 33749 #checksum 7394 SEQUENCE /// ENTRY R3EC5 #type complete TITLE ribosomal protein S5 [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-May-1979 #sequence_revision 14-Nov-1997 #text_change 01-Mar-2002 ACCESSIONS B65123; A02707 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65123 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-167 ##label BLAT !'##cross-references GB:AE000408; GB:U00096; NID:g1789694; !1PIDN:AAC76328.1; PID:g1789699; UWGP:b3303 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A02707 !$#authors Wittmann-Liebold, B.; Greuer, B. !$#journal FEBS Lett. (1978) 95:91-98 !$#title The primary structure of protein S5 from the small subunit !1of the Escherichia coli ribosome. !$#cross-references MUID:79065493; PMID:363452 !$#accession A02707 !'##molecule_type protein !'##residues 2-167 ##label WIT !'##experimental_source strain K REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note mass spectrographic analysis of post-translational !1modifications; any acid labile modifications may have been !1missed COMMENT The amino end is acetylated by ribosomal-protein-alanine !1N-acetyltransferase (EC 2.3.1.128) rimJ, see PIR:S01084. GENETICS !$#gene rpsE !$#map_position 73 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX small subunit ribosomal proteins: S1 (PIR:R3EC1), S2 !1(PIR:R3EC2), S3 (PIR:R3EC3), S4 (PIR:R3EC4), S5 (PIR:R3EC5), !1S6 (PIR:R3EC6), S7 (PIR:R3EC7K), S8 (PIR:R3EC8), S9 !1(PIR:R3EC9), S10 (PIR:R3EC10), S11 (PIR:R3EC11), S12 !1(PIR:R3EC12), S13 (PIR:R3EC13), S14 (PIR:R3EC14), S15 !1(PIR:R3EC15), S16 (PIR:R3EC16), S17 (PIR:R3EC17), S18 !1(PIR:R3EC18), S19 (PIR:R3EC19), S20/L26 (PIR:R3EC20), S21 !1(PIR:R3EC21), S22 (PIR:C64901) [validated, MUID:99196679] FUNCTION !$#pathway protein biosynthesis !$#note important for assembly and function of the 30S ribosomal !1subunit CLASSIFICATION #superfamily Escherichia coli ribosomal protein S5 KEYWORDS acetylated amino end; protein biosynthesis; ribosome FEATURE !$2-167 #product ribosomal protein S5 #status experimental !8#label MAT\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental SUMMARY #length 167 #molecular-weight 17603 #checksum 9685 SEQUENCE /// ENTRY R3BS5F #type complete TITLE ribosomal protein S5 - Bacillus stearothermophilus ORGANISM #formal_name Bacillus stearothermophilus DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 30-Jun-1993 ACCESSIONS A02708; A39085 REFERENCE A92442 !$#authors Kimura, M. !$#journal J. Biol. Chem. (1984) 259:1051-1055 !$#title Proteins of the Bacillus stearothermophilus ribosome. The !1amino acid sequences of protein S5 and L30. !$#cross-references MUID:84111493; PMID:6363400 !$#accession A02708 !'##molecule_type protein !'##residues 1-166 ##label KIM REFERENCE A39085 !$#authors Ramakrishnan, V.; Gerchman, S.E. !$#journal J. Biol. Chem. (1991) 266:880-885 !$#title Cloning, sequencing, and overexpression of genes for !1ribosomal proteins from Bacillus stearothermophilus. !$#cross-references MUID:91093287; PMID:1985969 !$#accession A39085 !'##molecule_type DNA !'##residues 7-156 ##label RAM !'##cross-references GB:M57621 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S5 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 166 #molecular-weight 17627 #checksum 3144 SEQUENCE /// ENTRY R3BS5S #type complete TITLE ribosomal protein S5 - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 31-Mar-1992 #sequence_revision 02-Jul-1998 #text_change 16-Jun-2000 ACCESSIONS D69699; S12680; S11355 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D69699 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-166 ##label KUN !'##cross-references GB:Z99104; GB:AL009126; NID:g2632267; !1PIDN:CAB11909.1; PID:g2632400 !'##experimental_source strain 168 REFERENCE S12680 !$#authors Yoshikawa, H.; Doi, R.H. !$#journal Nucleic Acids Res. (1990) 18:1647 !$#title Sequence of the Bacillus subtilis spectinomycin resistance !1gene region. !$#cross-references MUID:90221911; PMID:2139212 !$#accession S12680 !'##molecule_type DNA !'##residues 'MI',1-23,27-166 ##label YOS !'##cross-references EMBL:M31102; NID:g1184272; PIDN:AAB59115.1; !1PID:g143575 !'##note the authors are uncertain which methionine is the initiator REFERENCE S09561 !$#authors Higo, K.I.; Otaka, E.; Osawa, S. !$#journal Mol. Gen. Genet. (1982) 185:239-244 !$#title Purification and characterization of 30S ribosomal proteins !1from Bacillus subtilis: correlation to Escherichia coli 30S !1proteins. !$#cross-references MUID:82219212; PMID:6806564 !$#accession S11355 !'##molecule_type protein !'##residues 1-40 ##label HIG GENETICS !$#gene rpsE CLASSIFICATION #superfamily Escherichia coli ribosomal protein S5 KEYWORDS protein biosynthesis; ribosome FEATURE !$1-166 #product ribosomal protein S5 #status experimental !8#label MAT SUMMARY #length 166 #molecular-weight 17622 #checksum 4228 SEQUENCE /// ENTRY R3YM5C #type complete TITLE ribosomal protein S5 - Mycoplasma capricolum ORGANISM #formal_name Mycoplasma capricolum DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 07-Dec-1999 ACCESSIONS S02848 REFERENCE S02830 !$#authors Ohkubo, S.; Muto, A.; Kawauchi, Y.; Yamao, F.; Osawa, S. !$#journal Mol. Gen. Genet. (1987) 210:314-322 !$#title The ribosomal protein gene cluster of Mycoplasma capricolum. !$#cross-references MUID:88142549; PMID:3481422 !$#accession S02848 !'##molecule_type DNA !'##residues 1-250 ##label OHK !'##cross-references EMBL:X06414; NID:g44207; PIDN:CAA29721.1; !1PID:g44226 GENETICS !$#gene rps5 !$#genetic_code SGC3 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S5 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 250 #molecular-weight 27402 #checksum 5090 SEQUENCE /// ENTRY S16542 #type complete TITLE ribosomal protein S5 [similarity] - Haloarcula marismortui ORGANISM #formal_name Haloarcula marismortui DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 21-Jul-2000 ACCESSIONS S16542; T46807 REFERENCE S16535 !$#authors Scholzen, T.; Arndt, E. !$#journal Mol. Gen. Genet. (1991) 228:70-80 !$#title Organization and nucleotide sequence of ten ribosomal !1protein genes from the region equivalent to the !1spectinomycin operon in the archaebacterium Halobacterium !1marismortui. !$#cross-references MUID:91360093; PMID:1832208 !$#accession S16542 !'##molecule_type DNA !'##residues 1-212 ##label SCH !'##cross-references EMBL:X58395; NID:g48860; PIDN:CAA41291.1; !1PID:g48868 !'##note the source is designated as Halobacterium marismortui GENETICS !$#gene HmaS5 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S5 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 212 #molecular-weight 23048 #checksum 7973 SEQUENCE /// ENTRY R3MX5 #type complete TITLE ribosomal protein S5 - Methanococcus vannielii ORGANISM #formal_name Methanococcus vannielii DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 22-Jun-1999 ACCESSIONS S05624 REFERENCE S05611 !$#authors Auer, J.; Spicker, G.; Boeck, A. !$#journal J. Mol. Biol. (1989) 209:21-36 !$#title Organization and structure of the Methanococcus !1transcriptional unit homologous to the Escherichia coli !1"spectinomycin operon". Implications for the evolutionary !1relationship of 70 S and 80 S ribosomes. !$#cross-references MUID:90040717; PMID:2530355 !$#accession S05624 !'##molecule_type DNA !'##residues 1-225 ##label AUE !'##cross-references EMBL:X16720; NID:g44754; PIDN:CAA34700.1; !1PID:g44768 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S5 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 225 #molecular-weight 24359 #checksum 9967 SEQUENCE /// ENTRY R3RTS2 #type complete TITLE ribosomal protein S2, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 21-Jul-2000 ACCESSIONS S18828; S19170 REFERENCE S18828 !$#authors Suzuki, K.; Olvera, J.; Wool, I.G. !$#journal J. Biol. Chem. (1991) 266:20007-20010 !$#title Primary structure of rat ribosomal protein S2. A ribosomal !1protein with arginine-glycine tandem repeats and RGGF motifs !1that are associated with nucleolar localization and binding !1to ribonucleic acids. !$#cross-references MUID:92041821; PMID:1939063 !$#accession S18828 !'##molecule_type mRNA !'##residues 1-293 ##label SUZ !'##cross-references EMBL:X57432; NID:g57717; PIDN:CAA40679.1; !1PID:g57718 !$#accession S19170 !'##molecule_type protein !'##residues 111-128 ##label SUZ2 !'##note the protein is designated as ribosomal protein S2 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S5 KEYWORDS protein biosynthesis; ribosome; tandem repeat FEATURE !$9-17 #region 3-residue repeats\ !$22-29 #region 4-residue repeats\ !$34-52 #region 2-residue repeats SUMMARY #length 293 #molecular-weight 31231 #checksum 3110 SEQUENCE /// ENTRY R3BYS2 #type complete TITLE ribosomal protein S2.e, cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES omnipotent suppressor protein SUP44; protein G2893; protein YGL123w; ribosomal protein rp12; ribosomal protein YS4 ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 21-Jul-2000 ACCESSIONS A36363; A38838; S45501; S64134; S64133; S72028; S13309 REFERENCE A36363 !$#authors All-Robyn, J.A.; Brown, N.; Otaka, E.; Liebman, S.W. !$#journal Mol. Cell. Biol. (1990) 10:6544-6553 !$#title Sequence and functional similarity between a yeast ribosomal !1protein and the Escherichia coli S5 ram protein. !$#cross-references MUID:91061762; PMID:2247072 !$#accession A36363 !'##molecule_type DNA !'##residues 1-254 ##label ALL1 !'##cross-references GB:M59375; EMBL:M38029; NID:g172792; !1PIDN:AAA63576.1; PID:g172793 !$#accession A38838 !'##molecule_type protein !'##residues 33-55 ##label ALL2 REFERENCE S45500 !$#authors Takahura, H.; Tsunasawa, S.; Miyagi, M.; Warner, J.R. !$#journal J. Biol. Chem. (1992) 267:5442-5445 !$#title NH2-terminal acetylation of ribosomal proteins of !1Saccharomyces cerevisiae. !$#cross-references MUID:92184799; PMID:1544921 !$#accession S45501 !'##molecule_type protein !'##residues 2-11 ##label TAK REFERENCE S64134 !$#authors Cerdan, E.; Rodriguez-Torres, A.M.; Rodriguez-Belmonte, E.; !1Tizon, B.; Cadahia, J.L.; Gonzalez-Siso, I. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64134 !'##molecule_type DNA !'##residues 1-254 ##label CER !'##cross-references EMBL:Z72645; NID:g1322682; PIDN:CAA96831.1; !1PID:g1322683; GSPDB:GN00007; MIPS:YGL123w !'##experimental_source strain S288C REFERENCE S64122 !$#authors Lauquin, G. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64133 !'##molecule_type DNA !'##residues 170-254 ##label LAU !'##cross-references EMBL:Z72645; GSPDB:GN00007; MIPS:YGL123w !'##experimental_source strain S288C REFERENCE S72026 !$#authors Tizon, B.; Rodriguez-Torres, A.M.; Rodriguez-Belmonte, E.; !1Cadahia, J.L.; Cerdan, E. !$#journal Yeast (1996) 12:1047-1051 !$#title Identification of a putative methylenetetrahydrofolate !1reductase by sequence analysis of a 6.8 kb DNA fragment of !1yeast chromosome VII. !$#cross-references MUID:97051592; PMID:8896269 !$#accession S72028 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-254 ##label TIZ !'##cross-references EMBL:X94106; NID:g1628448; PIDN:CAA63835.1; !1PID:g1628451 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1995 GENETICS !$#gene SGD:SUP44; RPS4; MIPS:YGL123w !'##cross-references MIPS:YGL123w; SGD:S0003091 !$#map_position 7L CLASSIFICATION #superfamily Escherichia coli ribosomal protein S5 KEYWORDS acetylated amino end; blocked amino end; protein !1biosynthesis; ribosome FEATURE !$2-254 #product ribosomal protein S2.e #status experimental !8#label MAT\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental SUMMARY #length 254 #molecular-weight 27450 #checksum 5505 SEQUENCE /// ENTRY R3KT5 #type complete TITLE ribosomal protein S5, cyanelle - Cyanophora paradoxa cyanelle ORGANISM #formal_name cyanelle Cyanophora paradoxa DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 21-Jan-2000 ACCESSIONS S12220; T06876 REFERENCE S12211 !$#authors Michalowski, C.B.; Pfanzagl, B.; Loeffelhardt, W.; Bohnert, !1H.J. !$#journal Mol. Gen. Genet. (1990) 224:222-231 !$#title The cyanelle S10 spc ribosomal protein gene operon from !1Cyanophora paradoxa. !$#cross-references MUID:91117189; PMID:2126059 !$#accession S12220 !'##molecule_type DNA !'##residues 1-169 ##label MIC !'##cross-references GB:M30487; NID:g336645; PIDN:AAA63629.1; !1PID:g336655 !'##experimental_source strain LB555 UTEX REFERENCE Z15840 !$#authors Stirewalt, V.L.; Michalowski, C.B.; Luffelhardt, W.; !1Bohnert, H.J.; Bryant, D.A. !$#submission submitted to the EMBL Data Library, July 1995 !$#description Nucleotide sequence of the cyanelle genome from Cyanophora !1paradoxa. !$#accession T06876 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-169 ##label STI !'##cross-references EMBL:U30821; NID:g1016083; PIDN:AAA81219.1; !1PID:g1016132 !'##experimental_source strain Pringsheim LB555 GENETICS !$#gene rps5 !$#genome cyanelle CLASSIFICATION #superfamily Escherichia coli ribosomal protein S5 KEYWORDS cyanelle; protein biosynthesis; ribosome SUMMARY #length 169 #molecular-weight 17980 #checksum 7640 SEQUENCE /// ENTRY R3EC6 #type complete TITLE ribosomal protein S6 [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 12-Aug-1981 #sequence_revision 10-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS C65231; S56425; A02709 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65231 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-131 ##label BLAT !'##cross-references GB:AE000491; GB:U00096; NID:g2367357; !1PIDN:AAC77157.1; PID:g1790644; UWGP:b4200 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56425 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-131 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97096.1; !1PID:g537041 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A02709 !$#authors Hitz, H.; Schaefer, D.; Wittmann-Liebold, B. !$#journal Eur. J. Biochem. (1977) 75:497-512 !$#title Determination of the complete amino-acid sequence of protein !1S6 from the wild-type and a mutant of Escherichia coli. !$#cross-references MUID:77225229; PMID:328274 !$#accession A02709 !'##molecule_type protein !'##residues 1-131,'EEEE' ##label HIT !'##experimental_source strain K !'##note five forms of the protein, which differ only in the number of !1carboxyl-terminal glutamic acid residues, were isolated; the !1sequence of the longest form S6-6 is shown REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note no post-translational modifications were observed in mass !1spectrographic analysis; any acid labile modifications may !1have been missed COMMENT One to four glutamic acids are added to the carboxyl end of !1this protein by ribosomal protein S6-glutamic acid ligase !1(see PIR:D64823). GENETICS !$#gene rpsF !$#map_position 95 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX small subunit ribosomal proteins: S1 (PIR:R3EC1), S2 !1(PIR:R3EC2), S3 (PIR:R3EC3), S4 (PIR:R3EC4), S5 (PIR:R3EC5), !1S6 (PIR:R3EC6), S7 (PIR:R3EC7K), S8 (PIR:R3EC8), S9 !1(PIR:R3EC9), S10 (PIR:R3EC10), S11 (PIR:R3EC11), S12 !1(PIR:R3EC12), S13 (PIR:R3EC13), S14 (PIR:R3EC14), S15 !1(PIR:R3EC15), S16 (PIR:R3EC16), S17 (PIR:R3EC17), S18 !1(PIR:R3EC18), S19 (PIR:R3EC19), S20/L26 (PIR:R3EC20), S21 !1(PIR:R3EC21), S22 (PIR:C64901) [validated, MUID:99196679] FUNCTION !$#pathway protein biosynthesis CLASSIFICATION #superfamily Escherichia coli ribosomal protein S6 KEYWORDS protein biosynthesis; ribosome FEATURE !$1-131 #product ribosomal protein S6 #status experimental !8#label MAT\ !$131 #modified_site polyglutamate amidated carboxyl end !8(Glu) #status experimental SUMMARY #length 131 #molecular-weight 15187 #checksum 1434 SEQUENCE /// ENTRY R3RT5 #type complete TITLE ribosomal protein S5, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 21-Jul-2000 ACCESSIONS A45059; S14606 REFERENCE A45059 !$#authors Kuwano, Y.; Olvera, J.; Wool, I.G. !$#journal J. Biol. Chem. (1992) 267:25304-25308 !$#title The primary structure of rat ribosomal protein S5. A !1ribosomal protein present in the rat genome in a single !1copy. !$#cross-references MUID:93094243; PMID:1460027 !$#accession A45059 !'##molecule_type mRNA !'##residues 1-204 ##label KUW !'##cross-references EMBL:X58465; NID:g57136; PIDN:CAA41379.1; !1PID:g57137 !'##note submitted to the EMBL Data Library, March 1991 !'##note part of this sequence was confirmed by protein sequencing !'##note the protein is designated as ribosomal protein S5 !'##note sequence extracted from NCBI backbone (NCBIP:120201) CLASSIFICATION #superfamily Escherichia coli ribosomal protein S7 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 204 #molecular-weight 22878 #checksum 461 SEQUENCE /// ENTRY R3UC7 #type complete TITLE ribosomal protein S7 - Sulfolobus acidocaldarius ORGANISM #formal_name Sulfolobus acidocaldarius DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 22-Jun-1999 ACCESSIONS S12817 REFERENCE S12817 !$#authors Auer, J. !$#submission submitted to the EMBL Data Library, March 1990 !$#accession S12817 !'##molecule_type DNA !'##residues 1-195 ##label AUE !'##cross-references EMBL:X52382; NID:g46562; PIDN:CAA36607.1; !1PID:g46563 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S7 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 195 #molecular-weight 22056 #checksum 7800 SEQUENCE /// ENTRY S03583 #type complete TITLE ribosomal protein S7 [similarity] - Halobacterium salinarum ORGANISM #formal_name Halobacterium salinarum DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 21-Jul-2000 ACCESSIONS S03583 REFERENCE S03572 !$#authors Leffers, H.; Gropp, F.; Lottspeich, F.; Zillig, W.; Garrett, !1R.A. !$#journal J. Mol. Biol. (1989) 206:1-17 !$#title Sequence, organization, transcription and evolution of RNA !1polymerase subunit genes from the archaebacterial extreme !1halophiles Halobacterium halobium and Halococcus morrhuae. !$#cross-references MUID:89199633; PMID:2495365 !$#accession S03583 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-210 ##label LEF !'##cross-references GB:X57144; GB:X14999; NID:g43538; PIDN:CAA40430.1; !1PID:g43546 !'##note the source is designated as Halobacterium halobium CLASSIFICATION #superfamily Escherichia coli ribosomal protein S7 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 210 #molecular-weight 22984 #checksum 1705 SEQUENCE /// ENTRY S33228 #type complete TITLE ribosomal protein S7 [validated] - Haloarcula marismortui ORGANISM #formal_name Haloarcula marismortui DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 21-Jul-2000 ACCESSIONS S33228 REFERENCE S33228 !$#authors Klussmann, S.; Franke, P.; Bergmann, U.; Kostka, S.; !1Wittmann-Liebold, B. !$#journal Biol. Chem. Hoppe-Seyler (1993) 374:305-312 !$#title N-terminal modification and amino-acid sequence of the !1ribosomal protein HmaS7 from Haloarcula marismortui and !1homology studies to other ribosomal proteins. !$#cross-references MUID:93332645; PMID:8338632 !$#accession S33228 !'##molecule_type protein !'##residues 1-205 ##label KLU CLASSIFICATION #superfamily Escherichia coli ribosomal protein S7 KEYWORDS acetylated amino end; protein biosynthesis; ribosome FEATURE !$1 #modified_site acetylated amino end (Ser) #status !8experimental SUMMARY #length 205 #molecular-weight 22537 #checksum 3221 SEQUENCE /// ENTRY R3MX7 #type complete TITLE ribosomal protein S7 - Methanococcus vannielii ORGANISM #formal_name Methanococcus vannielii DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 22-Jun-1999 ACCESSIONS S06624 REFERENCE S06620 !$#authors Lechner, K.; Heller, G.; Boeck, A. !$#journal J. Mol. Evol. (1989) 29:20-27 !$#title Organization and nucleotide sequence of a transcriptional !1unit of Methanococcus vannielii comprising genes for protein !1synthesis elongation factors and ribosomal proteins. !$#cross-references MUID:89362493; PMID:2475640 !$#accession S06624 !'##molecule_type DNA !'##residues 1-146 ##label LEC !'##cross-references EMBL:X15970; NID:g44780; PIDN:CAA34090.1; !1PID:g44785 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S7 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 146 #molecular-weight 16115 #checksum 1749 SEQUENCE /// ENTRY R3TW7 #type complete TITLE ribosomal protein S7 - Thermus aquaticus ORGANISM #formal_name Thermus aquaticus DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 21-Jan-2000 ACCESSIONS S10250; S51058 REFERENCE S10249 !$#authors Yakhnin, A.V.; Vorozheykina, D.P.; Matvienko, N.I. !$#journal Nucleic Acids Res. (1990) 18:3659 !$#title Nucleotide sequence of the Thermus thermophilus HB8 rps12 !1and rps7 genes coding for the ribosomal proteins S12 and S7. !$#cross-references MUID:90301504; PMID:2362824 !$#accession S10250 !'##molecule_type DNA !'##residues 1-156 ##label YAK !'##cross-references EMBL:X52165; NID:g48273; PIDN:CAA36419.1; !1PID:g48275 !'##experimental_source strain HB8 !'##note the source is designated as Thermus thermophilus REFERENCE S51053 !$#authors Tsiboli, P.; Herfurth, E.; Choli, T. !$#journal Eur. J. Biochem. (1994) 226:169-177 !$#title Purification and characterization of the 30S ribosomal !1proteins from the bacterium Thermus thermophilus. !$#cross-references MUID:95045586; PMID:7957245 !$#accession S51058 !'##molecule_type protein !'##residues 2-50 ##label TSI !'##note the source is given as Thermus thermophilus CLASSIFICATION #superfamily Escherichia coli ribosomal protein S7 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 156 #molecular-weight 18016 #checksum 780 SEQUENCE /// ENTRY R3EC7K #type complete TITLE ribosomal protein S7 [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Nov-1979 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS H65127; A02710; S13739; JC1425; S59053; S19936 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65127 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-179 ##label BLAT !'##cross-references GB:AE000410; GB:U00096; NID:g1789734; !1PIDN:AAC76366.1; PID:g1789739; UWGP:b3341 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A02710 !$#authors Reinbolt, J.; Tritsch, D.; Wittmann-Liebold, B. !$#journal Biochimie (1979) 61:501-522 !$#title The primary structure of ribosomal protein S7 from !1Escherichia coli strains K and B. !$#cross-references MUID:80021286; PMID:385062 !$#accession A02710 !'##molecule_type protein !'##residues 2-91,93-179 ##label REI !'##experimental_source strains K and B !'##note the strain K sequence is shown; the sequence from strain B !1differs from that shown in lacking the carboxyl-terminal 24 !1residues REFERENCE S13738 !$#authors Post, L.E.; Nomura, M. !$#journal J. Biol. Chem. (1980) 255:4660-4666 !$#title DNA sequences from the str operon of Escherichia coli. !$#cross-references MUID:80182129; PMID:6989816 !$#accession S13739 !'##molecule_type DNA !'##residues 1-81;148-179 ##label POS !'##cross-references GB:V00355; NID:g43009; PIDN:CAA23649.1; PID:g43011; !1GB:V00356; GB:J01689; NID:g43012; PIDN:CAA23650.1; !1PID:g43013 REFERENCE JC1423 !$#authors Johanson, U.; Hughes, D. !$#journal Gene (1992) 120:93-98 !$#title Comparison of the complete sequence of the str operon in !1Salmonella typhimurium and Escherichia coli. !$#cross-references MUID:93013025; PMID:1398129 !$#accession JC1425 !'##molecule_type DNA !'##residues 82-147 ##label JOH !'##cross-references EMBL:X64592; NID:g42849 !'##experimental_source strain K-12 REFERENCE S59051 !$#authors Urlaub, H.; Kruft, V.; Bischof, O.; Mueller, E.C.; !1Wittmann-Liebold, B. !$#journal EMBO J. (1995) 14:4578-4588 !$#title Protein-rRNA binding features and their structural and !1functional implications in ribosomes as determined by !1cross-linking studies. !$#cross-references MUID:96003638; PMID:7556101 !$#accession S59053 !'##status preliminary !'##molecule_type DNA !'##residues 111-131 ##label URL REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note mass spectrographic analysis of post-translational !1modifications; any acid labile modifications may have been !1missed GENETICS !$#gene rpsG; strB !$#map_position 73 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX small subunit ribosomal proteins: S1 (PIR:R3EC1), S2 !1(PIR:R3EC2), S3 (PIR:R3EC3), S4 (PIR:R3EC4), S5 (PIR:R3EC5), !1S6 (PIR:R3EC6), S7 (PIR:R3EC7K), S8 (PIR:R3EC8), S9 !1(PIR:R3EC9), S10 (PIR:R3EC10), S11 (PIR:R3EC11), S12 !1(PIR:R3EC12), S13 (PIR:R3EC13), S14 (PIR:R3EC14), S15 !1(PIR:R3EC15), S16 (PIR:R3EC16), S17 (PIR:R3EC17), S18 !1(PIR:R3EC18), S19 (PIR:R3EC19), S20/L26 (PIR:R3EC20), S21 !1(PIR:R3EC21), S22 (PIR:C64901) [validated, MUID:99196679] FUNCTION !$#pathway protein biosynthesis !$#note binds 16S rRNA CLASSIFICATION #superfamily Escherichia coli ribosomal protein S7 KEYWORDS protein biosynthesis; ribosome; RNA binding FEATURE !$2-179 #product ribosomal protein S7 #status experimental !8#label MAT SUMMARY #length 179 #molecular-weight 20019 #checksum 1983 SEQUENCE /// ENTRY JG0008 #type complete TITLE ribosomal protein S7 - Bacillus stearothermophilus ORGANISM #formal_name Bacillus stearothermophilus DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 07-May-1999 ACCESSIONS JG0008; S59060 REFERENCE JG0007 !$#authors Kimura, M. !$#journal Agric. Biol. Chem. (1991) 55:207-213 !$#title The nucleotide sequences of Bacillus stearothermophilus !1ribosomal protein S12 and S7 genes: comparison with the str !1operon of Escherichia coli. !$#cross-references MUID:91248486; PMID:1368664 !$#accession JG0008 !'##molecule_type DNA !'##residues 1-156 ##label KIM REFERENCE S59051 !$#authors Urlaub, H.; Kruft, V.; Bischof, O.; Mueller, E.C.; !1Wittmann-Liebold, B. !$#journal EMBO J. (1995) 14:4578-4588 !$#title Protein-rRNA binding features and their structural and !1functional implications in ribosomes as determined by !1cross-linking studies. !$#cross-references MUID:96003638; PMID:7556101 !$#accession S59060 !'##molecule_type protein !'##residues 2-21;108-127 ##label URL GENETICS !$#gene rps7 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S7 KEYWORDS protein biosynthesis; ribosome; RNA binding SUMMARY #length 156 #molecular-weight 17988 #checksum 1787 SEQUENCE /// ENTRY R3SG7 #type complete TITLE ribosomal protein S7 - Spirulina platensis ORGANISM #formal_name Spirulina platensis DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S04389 REFERENCE S04388 !$#authors Buttarelli, F.R.; Calogero, R.A.; Tiboni, O.; Gualerzi, !1C.O.; Pon, C.L. !$#journal Mol. Gen. Genet. (1989) 217:97-104 !$#title Characterization of the str operon genes from Spirulina !1platensis and their evolutionary relationship to those of !1other prokaryotes. !$#cross-references MUID:89364697; PMID:2505055 !$#accession S04389 !'##molecule_type DNA !'##residues 1-156 ##label BUT !'##cross-references EMBL:X15646; NID:g47447; PIDN:CAA33671.1; !1PID:g47449 GENETICS !$#gene rpsG CLASSIFICATION #superfamily Escherichia coli ribosomal protein S7 KEYWORDS protein biosynthesis; ribosome; RNA binding SUMMARY #length 156 #molecular-weight 17883 #checksum 4203 SEQUENCE /// ENTRY R3KT7 #type complete TITLE ribosomal protein S7, cyanelle - Cyanophora paradoxa cyanelle ORGANISM #formal_name cyanelle Cyanophora paradoxa DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S14714; T06896; S10462 REFERENCE S14713 !$#authors Kraus, M.; Goetz, M.; Loeffelhardt, W. !$#journal Plant Mol. Biol. (1990) 15:561-573 !$#title The cyanelle str operon from Cyanophora paradoxa: sequence !1analysis and phylogenetic implications. !$#cross-references MUID:91338695; PMID:2129337 !$#accession S14714 !'##molecule_type DNA !'##residues 1-156 ##label KRA !'##cross-references EMBL:X52497; NID:g11413; PIDN:CAA36739.1; !1PID:g11415 !'##experimental_source strain LB555 UTEX REFERENCE Z15840 !$#authors Stirewalt, V.L.; Michalowski, C.B.; Luffelhardt, W.; !1Bohnert, H.J.; Bryant, D.A. !$#submission submitted to the EMBL Data Library, July 1995 !$#description Nucleotide sequence of the cyanelle genome from Cyanophora !1paradoxa. !$#accession T06896 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-156 ##label STI !'##cross-references EMBL:U30821; NID:g1016083; PIDN:AAA81239.1; !1PID:g1016152 GENETICS !$#gene rps7 !$#genome cyanelle CLASSIFICATION #superfamily Escherichia coli ribosomal protein S7 KEYWORDS cyanelle; protein biosynthesis; ribosome; RNA binding SUMMARY #length 156 #molecular-weight 17763 #checksum 1277 SEQUENCE /// ENTRY R3CWS7 #type complete TITLE ribosomal protein S7 - Chlamydia trachomatis ORGANISM #formal_name Chlamydia trachomatis DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 22-Jun-1999 ACCESSIONS S19249; G71514 REFERENCE S19249 !$#authors Wagar, E.A.; Pang, M. !$#journal Mol. Microbiol. (1992) 6:327-335 !$#title The gene for the S7 ribosomal protein of Chlamydia !1trachomatis: characterization within the chlamydial str !1operon. !$#cross-references MUID:92203999; PMID:1552847 !$#accession S19249 !'##molecule_type DNA !'##residues 1-157 ##label WAG !'##cross-references EMBL:Z11567; NID:g40756; PIDN:CAA77661.1; !1PID:g40757 !'##experimental_source strain L2 REFERENCE A71570 !$#authors Stephens, R.S.; Kalman, S.; Lammel, C.J.; Fan, J.; Marathe, !1R.; Aravind, L.; Mitchell, W.P.; Olinger, L.; Tatusov, R.L.; !1Zhao, Q.; Koonin, E.V.; Davis, R.W. !$#journal Science (1998) 282:754-759 !$#title Genome sequence of an obligate intracellular pathogen of !1humans: Chlamydia trachomatis. !$#cross-references MUID:99000809; PMID:9784136 !$#accession G71514 !'##molecule_type DNA !'##residues 1-72,'V',74-157 ##label ARN !'##cross-references GB:AE001317; GB:AE001273; NID:g3328863; !1PIDN:AAC68037.1; PID:g3328869 !'##experimental_source serotype D, strain UW-3/Cx GENETICS !$#gene rpsG; rs7 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S7 KEYWORDS protein biosynthesis; ribosome; RNA binding SUMMARY #length 157 #molecular-weight 17799 #checksum 1583 SEQUENCE /// ENTRY R3EG7 #type complete TITLE ribosomal protein S7 - Euglena gracilis chloroplast ORGANISM #formal_name chloroplast Euglena gracilis DATE 17-May-1985 #sequence_revision 31-Mar-1992 #text_change 24-Sep-1999 ACCESSIONS A02711; S34509; S34876; S02253 REFERENCE A93511 !$#authors Montandon, P.E.; Stutz, E. !$#journal Nucleic Acids Res. (1984) 12:2851-2859 !$#title The genes for the ribosomal proteins S12 and S7 are !1clustered with the gene for the EF-Tu protein on the !1chloroplast genome of Euglena gracilis. !$#cross-references MUID:84169577; PMID:6324129 !$#accession A02711 !'##molecule_type DNA !'##residues 1-156 ##label MON !'##cross-references GB:Z11874; GB:S55425; NID:g14353; PIDN:CAA77905.1; !1PID:g14355 !'##experimental_source strain Z REFERENCE S34494 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.; Monfort, !1A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#submission submitted to the EMBL Data Library, January 1993 !$#description The complete sequence of the Euglena gracilis chloroplast !1genome (tentative). !$#accession S34509 !'##molecule_type DNA !'##residues 1-156 ##label HAL1 !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50088.1; !1PID:g415744 REFERENCE S34862 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.R.; !1Monfort, A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#journal Nucleic Acids Res. (1993) 21:3537-3544 !$#title Complete sequence of Euglena gracilis chloroplast DNA. !$#cross-references MUID:93347989; PMID:8346031 !$#accession S34876 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-156 ##label HAL2 !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50088.1; !1PID:g415744 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1993 GENETICS !$#gene rps7 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein S7 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 156 #molecular-weight 17983 #checksum 8786 SEQUENCE /// ENTRY R3IT7 #type complete TITLE ribosomal protein S7 - euglenid (Astasia longa) plastid ORGANISM #formal_name plastid Astasia longa DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 28-Jul-2000 ACCESSIONS S14922; S38611; S08114 REFERENCE S14920 !$#authors Siemeister, G.; Buchholz, C.; Hachtel, W. !$#journal Mol. Gen. Genet. (1990) 220:425-432 !$#title Genes for the plastid elongation factor Tu and ribosomal !1protein S7 and six tRNA genes on the 73 kb DNA from Astasia !1longa that resembles the chloroplast DNA of Euglena. !$#cross-references MUID:90251252; PMID:2338940 !$#accession S14922 !'##molecule_type DNA !'##residues 1-178 ##label SIE !'##cross-references EMBL:X14385; NID:g11197; PIDN:CAA32557.1; !1PID:g4468076 REFERENCE S38590 !$#authors Gockel, G.; Baier, S.; Hachtel, W. !$#submission submitted to the EMBL Data Library, November 1993 !$#accession S38611 !'##molecule_type DNA !'##residues 1-178 ##label GOC !'##cross-references EMBL:X75652; NID:g414919; PIDN:CAA53318.1; !1PID:g414922 GENETICS !$#gene rps7 !$#genome plastid CLASSIFICATION #superfamily Escherichia coli ribosomal protein S7 KEYWORDS plastid; protein biosynthesis; ribosome SUMMARY #length 178 #molecular-weight 20787 #checksum 908 SEQUENCE /// ENTRY R3LV7 #type complete TITLE ribosomal protein S7, chloroplast - liverwort (Marchantia polymorpha) chloroplast ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 22-Jun-1999 ACCESSIONS A02712; S01568 REFERENCE A00150 !$#authors Ohyama, K. !$#submission submitted to the EMBL Data Library, October 1986 !$#accession A02712 !'##molecule_type DNA !'##residues 1-155 ##label OHY REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features REFERENCE S01567 !$#authors Umesono, K.; Inokuchi, H.; Shiki, Y.; Takeuchi, M.; Chang, !1Z.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Ohyama, K.; Ozeki, !1H. !$#journal J. Mol. Biol. (1988) 203:299-331 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. II. Gene organization of the large !1single copy region from rps'12 to atpB. !$#cross-references MUID:89068686; PMID:2974085 !$#accession S01568 !'##molecule_type DNA !'##residues 1-155 ##label UME !'##cross-references GB:X04465; GB:Y00686; NID:g11640; PIDN:CAA28057.1; !1PID:g11642 GENETICS !$#gene rps7 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein S7 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 155 #molecular-weight 17822 #checksum 8066 SEQUENCE /// ENTRY R3NT7 #type complete TITLE ribosomal protein S7, chloroplast - common tobacco chloroplast ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 30-Jan-1998 ACCESSIONS A02713 REFERENCE A00149 !$#authors Sugiura, M. !$#submission submitted to the EMBL Data Library, August 1986 !$#accession A02713 !'##molecule_type DNA !'##residues 1-155 ##label SUG !'##experimental_source cv. Bright Yellow 4 REFERENCE A38013 !$#authors Shinozaki, K.; Ohme, M.; Tanaka, M.; Wakasugi, T.; !1Hayashida, N.; Matsubayashi, T.; Zaita, N.; Chunwongse, J.; !1Obokata, J.; Yamaguchi-Shinozaki, K.; Ohto, C.; Torazawa, !1K.; Meng, B.Y.; Sugita, M.; Deno, H.; Kamogashira, T.; !1Yamada, K.; Kusuda, J.; Takaiwa, F.; Kato, A.; Tohdoh, N.; !1Shimada, H.; Sugiura, M. !$#journal EMBO J. (1986) 5:2043-2049 !$#title The complete nucleotide sequence of the tobacco chloroplast !1genome: its gene organization and expression. !$#contents annotation; gene organization, sites, features GENETICS !$#gene rps7 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein S7 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 155 #molecular-weight 17386 #checksum 7771 SEQUENCE /// ENTRY R3SY7 #type complete TITLE ribosomal protein S7 - soybean chloroplast ORGANISM #formal_name chloroplast Glycine max #common_name soybean DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 23-Mar-2001 ACCESSIONS B26574; S05718 REFERENCE A26574 !$#authors von Allmen, J.M.; Stutz, E. !$#journal Nucleic Acids Res. (1987) 15:2387 !$#title Complete sequence of `divided' rps12 (r-protein S12) and !1rps7 (r-protein S7) gene in soybean chloroplast DNA. !$#cross-references MUID:87174761; PMID:3562230 !$#accession B26574 !'##molecule_type DNA !'##residues 1-155 ##label VON1 !'##cross-references GB:X05013; NID:g11571; PIDN:CAA28662.1; PID:g11573 REFERENCE S05717 !$#authors von Allmen, J.M.; Stutz, E. !$#submission submitted to the EMBL Data Library, May 1988 !$#description Analysis of the 5' rps12 and 3' rps7 regions of soybean !1chloroplast DNA including parts of the genes rpl20 and ndhB. !$#accession S05718 !'##molecule_type DNA !'##residues 1-155 ##label VON2 !'##cross-references EMBL:X07675; NID:g11576; PIDN:CAA30523.1; !1PID:g11578 GENETICS !$#gene rps7 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein S7 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 155 #molecular-weight 17361 #checksum 7681 SEQUENCE /// ENTRY R3RZ7 #type complete TITLE ribosomal protein S7 - rice chloroplast ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jun-2000 ACCESSIONS JQ0276; S05156; S01060 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0276 !'##molecule_type DNA !'##residues 1-156 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05156 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-156 ##label HIR !'##cross-references GB:X15901; NID:g11957; PIDN:CAA33942.1; PID:g12037 !'##experimental_source cv. Nihonbare !'##note this sequence was submitted to EMBL, July 1989 REFERENCE S01057 !$#authors Kikuchi, S.; Takaiwa, F.; Oono, K. !$#journal Mol. Gen. Genet. (1987) 210:373-380 !$#title Variable copy number DNA sequences in rice. !$#cross-references MUID:88121710; PMID:3481021 !$#accession S01060 !'##molecule_type DNA !'##residues 1-97,'KSTCHSLVIRSIP',111-140,'RSNASNRLLHIFVNP' ##label KIK !'##cross-references GB:X06612; NID:g20384; PIDN:CAA29827.1; PID:g20385 GENETICS !$#gene rps7 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein S7 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 156 #molecular-weight 17629 #checksum 1007 SEQUENCE /// ENTRY R3RT7 #type complete TITLE ribosomal protein S7, cytosolic [validated] - rat ALTERNATE_NAMES ribosomal protein RS8e ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 21-Jul-2000 ACCESSIONS S12862; S18844; S33179; S14017 REFERENCE S12862 !$#authors Suzuki, K.; Olvera, J.; Wool, I.G. !$#journal FEBS Lett. (1990) 271:51-53 !$#title The primary structure of rat ribosomal protein S7. !$#cross-references MUID:91032085; PMID:2226813 !$#accession S12862 !'##molecule_type mRNA !'##residues 1-194 ##label SUZ !$#accession S18844 !'##molecule_type protein !'##residues 33-47 ##label SUZ2 !'##note the protein is designated as ribosomal protein S7 REFERENCE S33179 !$#authors Suzuki, K.; Olvera, J.; Wool, I.G. !$#submission submitted to the EMBL Data Library, June 1990 !$#description The primary structure of rat ribosomal protein S7. !$#accession S33179 !'##molecule_type mRNA !'##residues 1-194 ##label SUZ3 !'##cross-references EMBL:X53377; NID:g297171; PIDN:CAA37457.1; !1PID:g297172 REFERENCE S14017 !$#authors Guillier, M.; Leibovitch, S. !$#journal Nucleic Acids Res. (1991) 19:1339 !$#title Sequence of a cDNA encoding rat ribosomal protein homologous !1to Xenopus laevis ribosomal protein S8. !$#cross-references MUID:91232919; PMID:2030949 !$#accession S14017 !'##molecule_type mRNA !'##residues 1,'S',3-13,'K',15,'R',17-34,'E',36-37,'T',39-40,'W',42-74, !1'MAKSGK',80-115,'AQKPTLTSSADRR',129-148,'V',150-180,'PL', !1183-192,'VSV' ##label GUI !'##cross-references EMBL:X56846 CLASSIFICATION #superfamily rat ribosomal protein S7 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 194 #molecular-weight 22127 #checksum 8253 SEQUENCE /// ENTRY R3XL8 #type complete TITLE ribosomal protein S7 - African clawed frog ALTERNATE_NAMES ribosomal protein XS8 ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 17-Dec-1982 #sequence_revision 31-Mar-1992 #text_change 24-Sep-1999 ACCESSIONS JT0310; A02718; JN0872 REFERENCE JT0310 !$#authors Mariottini, P.; Bagni, C.; Annesi, F.; Amaldi, F. !$#journal Gene (1988) 67:69-74 !$#title Isolation and nucleotide sequences of cDNAs for Xenopus !1laevis ribosomal protein S8: similarities in the 5` and 3` !1untranslated regions of mRNAs for various r-proteins. !$#cross-references MUID:88329746; PMID:2843441 !$#accession JT0310 !'##molecule_type mRNA !'##residues 1-194 ##label MAR !'##cross-references GB:M21485; NID:g214760; PIDN:AAA49954.1; !1PID:g214761 !'##note the authors translated the codon CAC for residue 126 as Lys and !1AAA for residue 160 as His REFERENCE A91492 !$#authors Amaldi, F.; Beccari, E.; Bozzoni, I.; Luo, Z.X.; !1Pierandrei-Amaldi, P. !$#journal Gene (1982) 17:311-316 !$#title Nucleotide sequences of cloned cDNA fragments specific for !1six Xenopus laevis ribosomal proteins. !$#cross-references MUID:82262793; PMID:7049839 !$#accession A02718 !'##molecule_type mRNA !'##residues 19-188 ##label AMA !'##cross-references GB:V01442; GB:J00998; NID:g65052; PIDN:CAA24703.1; !1PID:g929913 REFERENCE JN0872 !$#authors Mariottini, P.; Bagni, C.; Francesconi, A.; Cecconi, F.; !1Serra, M.J.; Chen, Q.M.; Loreni, F.; Annesi, F.; Amaldi, F. !$#journal Gene (1993) 132:255-260 !$#title Sequence of the gene coding for ribosomal protein S8 of !1Xenopus laevis. !$#cross-references MUID:94040770; PMID:8224872 !$#accession JN0872 !'##molecule_type DNA !'##residues 1-194 ##label MAR2 !'##cross-references EMBL:X71081; NID:g414695; PIDN:CAA50399.1; !1PID:g414696 !'##note S8a gene GENETICS !$#gene S8a !$#introns 25/3; 49/3; 97/3; 119/2; 169/3 !$#note two loci, S8a and S8b, encode the same amino acid sequence CLASSIFICATION #superfamily rat ribosomal protein S7 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 194 #molecular-weight 22184 #checksum 8642 SEQUENCE /// ENTRY R3KM72 #type complete TITLE ribosomal protein S7-2 - Chlamydomonas reinhardtii chloroplast ORGANISM #formal_name chloroplast Chlamydomonas reinhardtii DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 22-Jun-1999 ACCESSIONS S11897 REFERENCE S11897 !$#authors Robertson, D.; Boynton, J.E.; Gillham, N.W. !$#journal Mol. Gen. Genet. (1990) 221:155-163 !$#title Cotranscription of the wild-type chloroplast atpE gene !1encoding the CF(1)/CF(0) epsilon subunit with the 3' half of !1the rps7 gene in Chlamydomonas reinhardtii and !1characterization of frameshift mutations in atpE. !$#cross-references MUID:90318312; PMID:2196429 !$#accession S11897 !'##molecule_type DNA !'##residues 1-52 ##label ROB !'##cross-references EMBL:X53977; NID:g11429; PIDN:CAA37927.1; !1PID:g11430 GENETICS !$#genome chloroplast CLASSIFICATION #superfamily Chlamydomonas chloroplast ribosomal protein !1S7-2 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 52 #molecular-weight 5885 #checksum 2923 SEQUENCE /// ENTRY R3RT8 #type complete TITLE ribosomal protein S8, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 21-Jul-2000 ACCESSIONS S01609; S11415 REFERENCE S01609 !$#authors Chan, Y.L.; Lin, A.; Paz, V.; Wool, I.G. !$#journal Nucleic Acids Res. (1987) 15:9451-9459 !$#title The primary structure of rat ribosomal protein S8. !$#cross-references MUID:88067767; PMID:3684599 !$#accession S01609 !'##molecule_type mRNA !'##residues 1-208 ##label CHA !'##cross-references EMBL:X06423; NID:g57138; PIDN:CAA29732.1; !1PID:g57139 !'##note part of this sequence was confirmed by protein sequencing !'##note the protein is designated as ribosomal protein S8 REFERENCE S11413 !$#authors Wittmann-Liebold, B.; Geissler, A.W.; Lin, A.; Wool, I.G. !$#journal J. Supramol. Struct. (1979) 12:425-433 !$#title Sequence of the amino-terminal region of rat liver ribosomal !1proteins S4, S6, S8, L6, L7a, L18, L27, L30, L37, L37a, and !1L39. !$#cross-references MUID:80252792; PMID:398910 !$#accession S11415 !'##molecule_type protein !'##residues 2-21 ##label WIT !'##note the protein is designated as ribosomal protein S8 CLASSIFICATION #superfamily rat ribosomal protein S8 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-208 #product ribosomal protein S8 #status experimental !8#label MAT SUMMARY #length 208 #molecular-weight 24205 #checksum 5794 SEQUENCE /// ENTRY S49022 #type complete TITLE ribosomal protein S8.eR [validated] - Haloarcula marismortui ALTERNATE_NAMES ribosomal protein HS23 ORGANISM #formal_name Haloarcula marismortui DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 21-Jul-2000 ACCESSIONS S49022 REFERENCE S49022 !$#authors Engemann, S.; Herfurth, E.; Briesemeister, U.; !1Wittmann-Liebold, B. !$#submission submitted to the Protein Sequence Database, November 1994 !$#description Amino acid sequence of the ribosomal protein HS23 from the !1halophilic Haloarcula marismortui and homology studies to !1other ribosomal proteins. !$#accession S49022 !'##molecule_type protein !'##residues 1-123 ##label ENG !'##note the protein is designated ribosomal protein HS23 CLASSIFICATION #superfamily rat ribosomal protein S8 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 123 #molecular-weight 13549 #checksum 9150 SEQUENCE /// ENTRY R3EC8 #type complete TITLE ribosomal protein S8 [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 24-Apr-1984 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS E65123; A02714; A30424 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65123 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-130 ##label BLAT !'##cross-references GB:AE000408; GB:U00096; NID:g1789694; !1PIDN:AAC76331.1; PID:g1789702; UWGP:b3306 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A02714 !$#authors Cerretti, D.P.; Dean, D.; Davis, G.R.; Bedwell, D.M.; !1Nomura, M. !$#journal Nucleic Acids Res. (1983) 11:2599-2616 !$#title The spc ribosomal protein operon of Escherichia coli: !1sequence and cotranscription of the ribosomal protein genes !1and a protein export gene. !$#cross-references MUID:83220807; PMID:6222285 !$#accession A02714 !'##molecule_type DNA !'##residues 1-90,'Q',92-130 ##label CER !'##cross-references GB:X01563; NID:g42977; PIDN:CAA25719.1; PID:g42983 !'##experimental_source strain K REFERENCE A30424 !$#authors Allen, G.; Wittmann-Liebold, B. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1978) 359:1509-1525 !$#title The amino acid sequence of the ribosomal protein S8 of !1Escherichia coli. !$#cross-references MUID:79087165; PMID:365698 !$#accession A30424 !'##molecule_type protein !'##residues 2-130 ##label ALL !'##experimental_source strain K REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note mass spectrographic analysis of post-translational !1modifications; any acid labile modifications may have been !1missed GENETICS !$#gene rpsH !$#map_position 73 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX small subunit ribosomal proteins: S1 (PIR:R3EC1), S2 !1(PIR:R3EC2), S3 (PIR:R3EC3), S4 (PIR:R3EC4), S5 (PIR:R3EC5), !1S6 (PIR:R3EC6), S7 (PIR:R3EC7K), S8 (PIR:R3EC8), S9 !1(PIR:R3EC9), S10 (PIR:R3EC10), S11 (PIR:R3EC11), S12 !1(PIR:R3EC12), S13 (PIR:R3EC13), S14 (PIR:R3EC14), S15 !1(PIR:R3EC15), S16 (PIR:R3EC16), S17 (PIR:R3EC17), S18 !1(PIR:R3EC18), S19 (PIR:R3EC19), S20/L26 (PIR:R3EC20), S21 !1(PIR:R3EC21), S22 (PIR:C64901) [validated, MUID:99196679] FUNCTION !$#pathway protein biosynthesis !$#note binds 16S rRNA CLASSIFICATION #superfamily Escherichia coli ribosomal protein S8 KEYWORDS protein biosynthesis; ribosome; RNA binding FEATURE !$2-130 #product ribosomal protein S8 #status experimental !8#label MAT SUMMARY #length 130 #molecular-weight 14126 #checksum 1660 SEQUENCE /// ENTRY R3YM8 #type complete TITLE ribosomal protein S8 - Mycoplasma capricolum ORGANISM #formal_name Mycoplasma capricolum DATE 17-Mar-1987 #sequence_revision 31-Dec-1990 #text_change 07-Dec-1999 ACCESSIONS S02845; A02715 REFERENCE S02830 !$#authors Ohkubo, S.; Muto, A.; Kawauchi, Y.; Yamao, F.; Osawa, S. !$#journal Mol. Gen. Genet. (1987) 210:314-322 !$#title The ribosomal protein gene cluster of Mycoplasma capricolum. !$#cross-references MUID:88142549; PMID:3481422 !$#accession S02845 !'##molecule_type DNA !'##residues 1-129 ##label OHK !'##cross-references EMBL:X06414; NID:g44207; PIDN:CAA29718.1; !1PID:g44223 GENETICS !$#gene rps8 !$#genetic_code SGC3 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S8 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 129 #molecular-weight 14191 #checksum 2880 SEQUENCE /// ENTRY R3IT8 #type complete TITLE ribosomal protein S8 - euglenid (Astasia longa) plastid ORGANISM #formal_name plastid Astasia longa DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 22-Jun-1999 ACCESSIONS S14151; S38592 REFERENCE S14125 !$#authors Siemeister, G.; Buchholz, C.; Hachtel, W. !$#journal Curr. Genet. (1990) 18:457-464 !$#title Genes for ribosomal proteins are retained on the 73 kb DNA !1from Astasia longa that resembles Euglena chloroplast DNA. !$#cross-references MUID:91176556; PMID:2078869 !$#accession S14151 !'##molecule_type DNA !'##residues 1-142 ##label SIE !'##cross-references EMBL:X16400 REFERENCE S38590 !$#authors Gockel, G.; Baier, S.; Hachtel, W. !$#submission submitted to the EMBL Data Library, November 1993 !$#accession S38592 !'##molecule_type DNA !'##residues 1-142 ##label GOC !'##cross-references EMBL:X75651; NID:g414852; PIDN:CAA53310.1; !1PID:g414857 GENETICS !$#gene rps8 !$#genome plastid !$#introns 5/3; 8/2; 116/1 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S8 KEYWORDS plastid; protein biosynthesis; ribosome SUMMARY #length 142 #molecular-weight 16239 #checksum 1173 SEQUENCE /// ENTRY R3EG8 #type complete TITLE ribosomal protein S8 - Euglena gracilis chloroplast ORGANISM #formal_name chloroplast Euglena gracilis DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 22-Jun-1999 ACCESSIONS S09289; A30467; S34529; S34896; S20206 REFERENCE S09286 !$#authors Christopher, D.A.; Hallick, R.B. !$#journal Nucleic Acids Res. (1989) 17:7591-7608 !$#title Euglena gracilis chloroplast ribosomal protein operon: a new !1chloroplast gene for ribosomal protein L5 and description of !1a novel organelle intron category designated group III. !$#cross-references MUID:90016846; PMID:2477800 !$#accession S09289 !'##molecule_type DNA !'##residues 1-140 ##label CHR !'##cross-references EMBL:Z11874; NID:g14353; PIDN:CAA77925.1; !1PID:g14375 !$#accession A30467 !'##molecule_type mRNA !'##residues 1-31 ##label CHR2 REFERENCE S34494 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.; Monfort, !1A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#submission submitted to the EMBL Data Library, January 1993 !$#description The complete sequence of the Euglena gracilis chloroplast !1genome (tentative). !$#accession S34529 !'##molecule_type DNA !'##residues 1-140 ##label HAL1 !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50108.1; !1PID:g415764 REFERENCE S34862 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.R.; !1Monfort, A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#journal Nucleic Acids Res. (1993) 21:3537-3544 !$#title Complete sequence of Euglena gracilis chloroplast DNA. !$#cross-references MUID:93347989; PMID:8346031 !$#accession S34896 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-140 ##label HAL2 !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50108.1; !1PID:g415764 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1993 GENETICS !$#gene rps8 !$#genome chloroplast !$#introns 5/3; 8/2; 114/1 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S8 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 140 #molecular-weight 15706 #checksum 609 SEQUENCE /// ENTRY R3KT8 #type complete TITLE ribosomal protein S8 - Cyanophora paradoxa cyanelle ORGANISM #formal_name cyanelle Cyanophora paradoxa DATE 31-Dec-1990 #sequence_revision 21-May-1999 #text_change 22-Jun-1999 ACCESSIONS T06879; S07068; S12217 REFERENCE Z15840 !$#authors Stirewalt, V.L.; Michalowski, C.B.; Luffelhardt, W.; !1Bohnert, H.J.; Bryant, D.A. !$#submission submitted to the EMBL Data Library, July 1995 !$#description Nucleotide sequence of the cyanelle genome from Cyanophora !1paradoxa. !$#accession T06879 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-132 ##label STI !'##cross-references EMBL:U30821; NID:g1016083; PIDN:AAA81222.1; !1PID:g1016135 !'##experimental_source strain Pringsheim LB555 REFERENCE S07067 !$#authors Bryant, D.A.; Stirewalt, V.L. !$#journal FEBS Lett. (1990) 259:273-280 !$#title The cyanelle genome of Cyanophora paradoxa encodes ribosomal !1proteins not encoded by the chloroplast genomes of higher !1plants. !$#cross-references MUID:90092562; PMID:2403527 !$#accession S07068 !'##molecule_type DNA !'##residues 1-11,'R',13-86,'V',88-132 ##label BRY !'##cross-references EMBL:X16548 REFERENCE S12211 !$#authors Michalowski, C.B.; Pfanzagl, B.; Loeffelhardt, W.; Bohnert, !1H.J. !$#journal Mol. Gen. Genet. (1990) 224:222-231 !$#title The cyanelle S10 spc ribosomal protein gene operon from !1Cyanophora paradoxa. !$#cross-references MUID:91117189; PMID:2126059 !$#accession S12217 !'##molecule_type DNA !'##residues 1-132 ##label MIC !'##cross-references GB:M30487; NID:g336645; PIDN:AAA63626.1; !1PID:g336652 !'##note the authors translated the initiation codon GTG for residue 1 !1as Val GENETICS !$#gene rps8; rpsH !$#map_position 47-48 !$#genome cyanelle !$#start_codon GTG CLASSIFICATION #superfamily Escherichia coli ribosomal protein S8 KEYWORDS cyanelle; protein biosynthesis; ribosome SUMMARY #length 132 #molecular-weight 14596 #checksum 3457 SEQUENCE /// ENTRY R3LV8 #type complete TITLE ribosomal protein S8 - liverwort (Marchantia polymorpha) chloroplast ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 22-Jun-1999 ACCESSIONS A02716; S01561 REFERENCE A00150 !$#authors Ohyama, K. !$#submission submitted to the EMBL Data Library, October 1986 !$#accession A02716 !'##molecule_type DNA !'##residues 1-132 ##label OHY REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features REFERENCE S01529 !$#authors Fukuzawa, H.; Kohchi, T.; Sano, T.; Shirai, H.; Umesono, K.; !1Inokuchi, H.; Ozeki, H.; Ohyama, K. !$#journal J. Mol. Biol. (1988) 203:333-351 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. III. Gene organization of the large !1single copy region from rbcL to trnI(CAU). !$#cross-references MUID:89068687; PMID:3199436 !$#accession S01561 !'##molecule_type DNA !'##residues 1-132 ##label FUK !'##cross-references GB:X04465; GB:Y00686; NID:g11640; PIDN:CAA28121.1; !1PID:g11710 GENETICS !$#gene rps8 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein S8 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 132 #molecular-weight 14921 #checksum 6002 SEQUENCE /// ENTRY R3NT8 #type complete TITLE ribosomal protein S8 - common tobacco chloroplast ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 17-Feb-1995 ACCESSIONS A02717; H25943 REFERENCE A00149 !$#authors Sugiura, M. !$#submission submitted to the EMBL Data Library, August 1986 !$#accession A02717 !'##molecule_type DNA !'##residues 1-134 ##label SUG !'##experimental_source cv. Bright Yellow 4 REFERENCE A38013 !$#authors Shinozaki, K.; Ohme, M.; Tanaka, M.; Wakasugi, T.; !1Hayashida, N.; Matsubayashi, T.; Zaita, N.; Chunwongse, J.; !1Obokata, J.; Yamaguchi-Shinozaki, K.; Ohto, C.; Torazawa, !1K.; Meng, B.Y.; Sugita, M.; Deno, H.; Kamogashira, T.; !1Yamada, K.; Kusuda, J.; Takaiwa, F.; Kato, A.; Tohdoh, N.; !1Shimada, H.; Sugiura, M. !$#journal EMBO J. (1986) 5:2043-2049 !$#title The complete nucleotide sequence of the tobacco chloroplast !1genome: its gene organization and expression. !$#contents annotation; gene organization, sites, features REFERENCE A94118 !$#authors Tanaka, M.; Wakasugi, T.; Sugita, M.; Shinozaki, K.; !1Sugiura, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:6030-6034 !$#title Genes for the eight ribosomal proteins are clustered on the !1chloroplast genome of tobacco (Nicotiana tabacum): !1similarity to the S10 and spc operons of Escherichia coli. !$#cross-references MUID:86287388; PMID:3016736 !$#accession H25943 !'##molecule_type DNA !'##residues 1-134 ##label TAN GENETICS !$#gene rps8 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein S8 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 134 #molecular-weight 15790 #checksum 1795 SEQUENCE /// ENTRY R3RZ8 #type complete TITLE ribosomal protein S8 - rice chloroplast ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 22-Jun-1999 ACCESSIONS JQ0262; S05142 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0262 !'##molecule_type DNA !'##residues 1-136 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05142 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-136 ##label HIR !'##cross-references GB:X15901; NID:g11957; PIDN:CAA33931.1; PID:g12022 !'##experimental_source cv. Nihonbare !'##note this sequence was submitted to EMBL, July 1989 GENETICS !$#gene rps8 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein S8 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 136 #molecular-weight 15610 #checksum 5822 SEQUENCE /// ENTRY R3ZMBC #type complete TITLE ribosomal protein S8 - maize chloroplast ORGANISM #formal_name chloroplast Zea mays #common_name maize DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S00280; S58587 REFERENCE S00278 !$#authors Markmann-Mulisch, U.; Subramanian, A.R. !$#journal Eur. J. Biochem. (1988) 170:507-514 !$#title Nucleotide sequence and linkage map position of the genes !1for ribosomal proteins L14 and S8 in the maize chloroplast !1genome. !$#cross-references MUID:88111635; PMID:2828044 !$#accession S00280 !'##molecule_type DNA !'##residues 1-136 ##label MAR !'##cross-references EMBL:X06734; NID:g12451; PIDN:CAA29913.1; !1PID:g12454 REFERENCE S58531 !$#authors Maier, R.M.; Neckermann, K.; Igloi, G.L.; Koessel, H. !$#journal J. Mol. Biol. (1995) 251:614-628 !$#title Complete sequence of the maize chloroplast genome: gene !1content, hotspots of divergence and fine tuning of genetic !1information by transcript editing. !$#cross-references MUID:95395841; PMID:7666415 !$#accession S58587 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-136 ##label MAI !'##cross-references EMBL:X86563; NID:g902200; PIDN:CAA60321.1; !1PID:g902257 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1995 GENETICS !$#gene rps8 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein S8 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 136 #molecular-weight 15638 #checksum 5892 SEQUENCE /// ENTRY S52339 #type complete TITLE ribosomal protein S15a, cytosolic [validated] - human ALTERNATE_NAMES ribosomal protein HS24 ORGANISM #formal_name Homo sapiens #common_name man DATE 05-Feb-1999 #sequence_revision 05-Feb-1999 #text_change 08-Dec-2000 ACCESSIONS S52339; S22051; S68937 REFERENCE S52339 !$#authors Mays, G.; Burchert-Graeve, M. !$#submission submitted to the EMBL Data Library, February 1995 !$#accession S52339 !'##molecule_type mRNA !'##residues 1-130 ##label MAY !'##cross-references EMBL:X84407; NID:g666046; PIDN:CAA59127.1; !1PID:g666047 REFERENCE S22051 !$#authors Schwabe, G. !$#submission submitted to the EMBL Data Library, October 1991 !$#accession S22051 !'##molecule_type mRNA !'##residues 1-23,'RC',26,'LGRLQSHRP','V',38-39,'V',41-130 ##label SCH !'##cross-references EMBL:X62691; NID:g36141; PIDN:CAA44568.1; !1PID:g36142 REFERENCE S68911 !$#authors Vladimirov, S.N.; Ivanov, A.V.; Karpova, G.G.; Musolyamov, !1A.K.; Egorov, T.A.; Thiede, B.; Wittmann-Liebold, B.; Otto, !1A. !$#journal Eur. J. Biochem. (1996) 239:144-149 !$#title Characterization of the human small-ribosomal-subunit !1proteins by N-terminal and internal sequencing, and mass !1spectrometry. !$#cross-references MUID:96305378; PMID:8706699 !$#accession S68937 !'##molecule_type protein !'##residues 2,'C',4-17;33-39,'V',41-43;44-60 ##label VLA GENETICS !$#gene GDB:RPS15A !'##cross-references GDB:9863264 !$#map_position 16p13.1-16p12.3 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S8 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-130 #product ribosomal protein S15a, cytosolic #status !8experimental #label MAT SUMMARY #length 130 #molecular-weight 14853 #checksum 310 SEQUENCE /// ENTRY JC2234 #type complete TITLE ribosomal protein S15a, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 21-Jul-2000 ACCESSIONS JC2234; PC2155 REFERENCE JC2234 !$#authors Chan, Y.L.; Olvera, J.; Paz, V.; Wool, I.G. !$#journal Biochem. Biophys. Res. Commun. (1994) 200:1498-1504 !$#title The primary structure of rat ribosomal protein S15a. !$#cross-references MUID:94242014; PMID:8185605 !$#accession JC2234 !'##molecule_type mRNA !'##residues 1-130 ##label CHA1 !'##cross-references EMBL:X77953; NID:g495272; PIDN:CAA54918.1; !1PID:g495273 !'##experimental_source clone pS15a-7 !$#accession PC2155 !'##molecule_type protein !'##residues 2-38 ##label CHA2 !'##note the protein is designated as ribosomal protein S15a GENETICS !$#gene S15a CLASSIFICATION #superfamily Escherichia coli ribosomal protein S8 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-130 #product ribosomal protein S15a #status predicted !8#label MAT SUMMARY #length 130 #molecular-weight 14839 #checksum 710 SEQUENCE /// ENTRY R4BY24 #type complete TITLE ribosomal protein S15a.e.c10, cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein J0355; protein YJL190c; ribosomal protein YS24 ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 21-Jul-2000 ACCESSIONS A23082; S46644; S11579; S56973; S56977 REFERENCE A93593 !$#authors Leer, R.J.; van Raamsdonk-Duin, M.M.C.; Kraakman, P.; Mager, !1W.H.; Planta, R.J. !$#journal Nucleic Acids Res. (1985) 13:701-709 !$#title The genes for yeast ribosomal proteins S24 and L46 are !1adjacent and divergently transcribed. !$#cross-references MUID:85215509; PMID:4000930 !$#accession A23082 !'##molecule_type DNA !'##residues 1-130 ##label LEE !'##cross-references EMBL:X01962; NID:g4406; PIDN:CAA25998.1; PID:g4407 REFERENCE S46621 !$#authors Purnelle, B.; Coster, F.; Goffeau, A. !$#journal Yeast (1994) 10:1235-1249 !$#title The sequence of a 36 kb segment on the left arm of yeast !1chromosome X identifies 24 open reading frames including !1NUC1, PRP21 (SPP91), CDC6, CRY2, the gene for S24, a !1homologue to the aconitase gene ACO1 and two homologues to !1chromosome III genes. !$#cross-references MUID:95274326; PMID:7754713 !$#accession S46644 !'##molecule_type DNA !'##residues 1-130 ##label PUR !'##cross-references EMBL:X77688; NID:g1183992; PIDN:CAA54770.1; !1PID:g547605 REFERENCE S11575 !$#authors Otaka, E.; Higo, K.; Osawa, S. !$#journal Biochemistry (1982) 21:4545-4550 !$#title Isolation of seventeen proteins and amino-terminal amino !1acid sequences of eight proteins from cytoplasmic ribosomes !1of yeast. !$#cross-references MUID:83048950; PMID:6814480 !$#accession S11579 !'##molecule_type protein !'##residues 2-40,'XZ',43-44 ##label OTA REFERENCE S56937 !$#authors Obermaier, B.; Piravandi, E.; Rinke, M.; Domdey, H. !$#submission submitted to the Protein Sequence Database, September 1995 !$#accession S56973 !'##molecule_type DNA !'##residues 1-130 ##label OBE !'##cross-references EMBL:Z49465; NID:g1008399; PIDN:CAA89485.1; !1PID:g1008400; GSPDB:GN00010; MIPS:YJL190c REFERENCE S56977 !$#authors Purnelle, B.; Coster, F.; Goffeau, A. !$#submission submitted to the Protein Sequence Database, September 1995 !$#accession S56977 !'##molecule_type DNA !'##residues 1-130 ##label PUW !'##cross-references EMBL:Z49465; NID:g1008399; PIDN:CAA89485.1; !1PID:g1008400; GSPDB:GN00010; MIPS:YJL190c GENETICS !$#gene SGD:RPS24A; MIPS:YJL190c !'##cross-references SGD:S0003726; MIPS:YJL190c !$#map_position 10L FUNCTION !$#description protein biosynthesis CLASSIFICATION #superfamily Escherichia coli ribosomal protein S8 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-130 #product ribosomal protein S15a.e #status !8experimental #label MAT SUMMARY #length 130 #molecular-weight 14626 #checksum 1477 SEQUENCE /// ENTRY S16537 #type complete TITLE ribosomal protein S8 [validated] - Haloarcula marismortui ALTERNATE_NAMES ribosomal protein G1; ribosomal protein HS16 ORGANISM #formal_name Haloarcula marismortui DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 21-Jul-2000 ACCESSIONS S16537; B29799; F24304; T46802 REFERENCE S16535 !$#authors Scholzen, T.; Arndt, E. !$#journal Mol. Gen. Genet. (1991) 228:70-80 !$#title Organization and nucleotide sequence of ten ribosomal !1protein genes from the region equivalent to the !1spectinomycin operon in the archaebacterium Halobacterium !1marismortui. !$#cross-references MUID:91360093; PMID:1832208 !$#accession S16537 !'##molecule_type DNA !'##residues 1-130 ##label SCH !'##cross-references EMBL:X58395; NID:g48860; PIDN:CAA41286.1; !1PID:g48863 !'##note the source is designated as Halobacterium marismortui REFERENCE A29799 !$#authors Kimura, J.; Kimura, M. !$#journal J. Biol. Chem. (1987) 262:12150-12157 !$#title The primary structures of ribosomal proteins S14 and S16 !1from the archaebacterium Halobacterium marismortui. !1Comparison with eubacterial and eukaryotic ribosomal !1proteins. !$#cross-references MUID:87308217; PMID:3305503 !$#accession B29799 !'##molecule_type protein !'##residues 2-88,92-107,'V',109-130 ##label KIM !'##note the source is designated as Halobacterium marismortui REFERENCE A24304 !$#authors Shoham, M.; Dijk, J.; Reinhardt, R.; Wittmann-Liebold, B. !$#journal FEBS Lett. (1986) 204:323-330 !$#title Purification and characterization of ribosomal proteins from !1the 30 S subunit of the extreme halophile Halobacterium !1marismortui. !$#accession F24304 !'##molecule_type protein !'##residues 'AI',4-5,'A',7-11,'X',13-15 ##label SHO !'##note the source is designated as Halobacterium marismortui GENETICS !$#gene HmaS8 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S8 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-130 #product ribosomal protein S8 #status experimental !8#label MAT SUMMARY #length 130 #molecular-weight 14160 #checksum 3059 SEQUENCE /// ENTRY R3MX8 #type complete TITLE ribosomal protein S8 - Methanococcus vannielii ORGANISM #formal_name Methanococcus vannielii DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 22-Jun-1999 ACCESSIONS S05619 REFERENCE S05611 !$#authors Auer, J.; Spicker, G.; Boeck, A. !$#journal J. Mol. Biol. (1989) 209:21-36 !$#title Organization and structure of the Methanococcus !1transcriptional unit homologous to the Escherichia coli !1"spectinomycin operon". Implications for the evolutionary !1relationship of 70 S and 80 S ribosomes. !$#cross-references MUID:90040717; PMID:2530355 !$#accession S05619 !'##molecule_type DNA !'##residues 1-130 ##label AUE !'##cross-references EMBL:X16720; NID:g44754; PIDN:CAA34695.1; !1PID:g44763 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S8 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 130 #molecular-weight 14335 #checksum 1907 SEQUENCE /// ENTRY R3HU16 #type complete TITLE ribosomal protein S16, cytosolic [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 08-Dec-2000 ACCESSIONS A39760; S68928 REFERENCE A39760 !$#authors Batra, S.K.; Metzgar, R.S.; Hollingsworth, M.A. !$#journal J. Biol. Chem. (1991) 266:6830-6833 !$#title Molecular cloning and sequence analysis of the human !1ribosomal protein S16. !$#cross-references MUID:91201326; PMID:2016298 !$#accession A39760 !'##molecule_type mRNA !'##residues 1-146 ##label BAT !'##cross-references GB:M60854; NID:g338446; PIDN:AAA60583.1; !1PID:g338447 REFERENCE S68911 !$#authors Vladimirov, S.N.; Ivanov, A.V.; Karpova, G.G.; Musolyamov, !1A.K.; Egorov, T.A.; Thiede, B.; Wittmann-Liebold, B.; Otto, !1A. !$#journal Eur. J. Biochem. (1996) 239:144-149 !$#title Characterization of the human small-ribosomal-subunit !1proteins by N-terminal and internal sequencing, and mass !1spectrometry. !$#cross-references MUID:96305378; PMID:8706699 !$#accession S68928 !'##molecule_type protein !'##residues 2-11 ##label VLA GENETICS !$#gene GDB:RPS16 !'##cross-references GDB:127871 !$#map_position 5q31-5q33 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S9 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-146 #product ribosomal protein S16, cytosolic #status !8experimental #label MAT SUMMARY #length 146 #molecular-weight 16445 #checksum 3880 SEQUENCE /// ENTRY R3RT16 #type complete TITLE ribosomal protein S16, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 21-Jul-2000 ACCESSIONS S09041; S20564 REFERENCE S09041 !$#authors Chan, Y.L.; Paz, V.; Olvera, J.; Wool, I.G. !$#journal FEBS Lett. (1990) 263:85-88 !$#title The primary structure of rat ribosomal protein S16. !$#cross-references MUID:90235982; PMID:2332055 !$#accession S09041 !'##molecule_type mRNA !'##residues 1-146 ##label CHA !'##cross-references EMBL:X17665; NID:g57713; PIDN:CAA35662.1; !1PID:g57714 !$#accession S20564 !'##molecule_type protein !'##residues 2-19 ##label CHA2 !'##note the protein is designated as ribosomal protein S16 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S9 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-146 #product ribosomal protein S16 #status experimental !8#label MAT SUMMARY #length 146 #molecular-weight 16445 #checksum 3880 SEQUENCE /// ENTRY R3MS16 #type complete TITLE ribosomal protein S16 - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 30-Jun-1993 ACCESSIONS S11623; S11619 REFERENCE S11623 !$#authors Perry, R.P. !$#submission submitted to the EMBL Data Library, January 1990 !$#accession S11623 !'##molecule_type DNA !'##residues 1-145 ##label PER !'##cross-references EMBL:M11408 REFERENCE S11619 !$#authors Wagner, M.; Perry, R.P. !$#journal Mol. Cell. Biol. (1985) 5:3560-3576 !$#title Characterization of the multigene family encoding the mouse !1S16 ribosomal protein: strategy for distinguishing an !1expressed gene from its processed pseudogene counterparts by !1an analysis of total genomic DNA. !$#cross-references MUID:86310836; PMID:3915781 !$#accession S11619 !'##molecule_type DNA !'##residues 1-6, !1'PAVRAGLRTQENSRCGPLQTGKWAHQGERTSPGDDRAARAAVQVTGACFASGQGAICWC !1GYS','GPCEGWWTCGPNLCHPTVHLKG',91-145 ##label WAG !'##cross-references EMBL:M11408 !'##note this sequence has been revised in reference S11623 GENETICS !$#introns 17/1; 50/1; 82/2; 98/1 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S9 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 145 #molecular-weight 16329 #checksum 1886 SEQUENCE /// ENTRY R3YL16 #type complete TITLE ribosomal protein S16, cytosolic - large-leaved lupine ORGANISM #formal_name Lupinus polyphyllus #common_name large-leaved lupine DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S15003; S08664 REFERENCE S15003 !$#authors Warskulat, U.; Perrey, R.; Wink, M. !$#journal Plant Mol. Biol. (1991) 16:739-740 !$#title Molecular cloning of a cDNA from Lupinus polyphyllus cell !1cultures encoding a ribosomal protein (rps16). !$#cross-references MUID:91329708; PMID:1868205 !$#accession S15003 !'##molecule_type mRNA !'##residues 1-145 ##label WAR !'##cross-references EMBL:X51766; NID:g19511; PIDN:CAA36068.1; !1PID:g19512 GENETICS !$#gene rps16 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S9 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 145 #molecular-weight 16189 #checksum 8866 SEQUENCE /// ENTRY R3HS3 #type complete TITLE ribosomal protein S9 [validated] - Haloarcula marismortui ALTERNATE_NAMES ribosomal protein F1; ribosomal protein HS3 ORGANISM #formal_name Haloarcula marismortui DATE 31-Mar-1991 #sequence_revision 21-Jul-2000 #text_change 21-Jul-2000 ACCESSIONS C41715; S07240; E24304 REFERENCE A41715 !$#authors Kroemer, W.J.; Arndt, E. !$#journal J. Biol. Chem. (1991) 266:24573-24579 !$#title Halobacterial S9 operon. Three ribosomal protein genes are !1cotranscribed with genes encoding a tRNA(leu), the enolase, !1and a putative membrane protein in the archaebacterium !1Haloarcula (halobacterium) marismortui. !$#cross-references MUID:92105119; PMID:1840597 !$#accession C41715 !'##status preliminary !'##molecule_type DNA !'##residues 1-132 ##label KRO !'##cross-references GB:M76567; NID:g148775; PIDN:AAA73098.1; !1PID:g148778 REFERENCE S07240 !$#authors Kimura, M.; Langner, G. !$#journal FEBS Lett. (1984) 175:213-218 !$#title The complete amino acid sequence of the ribosomal protein !1HS3 from Halobacterium marismortui, an archaebacterium. !$#accession S07240 !'##molecule_type protein !'##residues 2-75,77-92,'Q',94-132 ##label KIM !'##note the sequence from Fig. 4 is inconsistent with that from Fig. 2 !1in having 59-Tyr !'##note the source is designated as Halobacterium marismortui REFERENCE A24304 !$#authors Shoham, M.; Dijk, J.; Reinhardt, R.; Wittmann-Liebold, B. !$#journal FEBS Lett. (1986) 204:323-330 !$#title Purification and characterization of ribosomal proteins from !1the 30 S subunit of the extreme halophile Halobacterium !1marismortui. !$#accession E24304 !'##molecule_type protein !'##residues 2-5,'H',7-25,'X',27 ##label SHO !'##note the source is designated as Halobacterium marismortui CLASSIFICATION #superfamily Escherichia coli ribosomal protein S9 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-132 #product ribosomal protein S9 #status experimental !8#label MAT SUMMARY #length 132 #molecular-weight 14556 #checksum 1819 SEQUENCE /// ENTRY R3EC9 #type complete TITLE ribosomal protein S9 [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 12-Aug-1981 #sequence_revision 12-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS H65114; I77537; A02719 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65114 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-130 ##label BLAT !'##cross-references GB:AE000402; GB:U00096; NID:g1789619; !1PIDN:AAC76262.1; PID:g1789625; UWGP:b3230 !'##experimental_source strain K-12, substrain MG1655 REFERENCE I57732 !$#authors Isono, S.; Thamm, S.; Kitakawa, M.; Isono, K. !$#journal Mol. Gen. Genet. (1985) 198:279-282 !$#title Cloning and nucleotide sequencing of the genes for ribosomal !1proteins S9 (rpsI) and L13 (rplM) of Escherichia coli. !$#cross-references MUID:85162987; PMID:3884974 !$#accession I77537 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-130 ##label ISO !'##cross-references EMBL:X02130; NID:g42854; PIDN:CAA26042.1; !1PID:g535073 REFERENCE A02719 !$#authors Chen, R.; Wittmann-Liebold, B. !$#journal FEBS Lett. (1975) 52:139-140 !$#title The primary structure of protein S9 from the 30S subunit of !1Escherichia coli ribosomes. !$#cross-references MUID:75131427; PMID:1091515 !$#accession A02719 !'##molecule_type protein !'##residues 2-55,'N',57-123,125,'E',127-130 ##label CHE !'##experimental_source strain K REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note mass spectrographic analysis of post-translational !1modifications; any acid labile modifications may have been !1missed GENETICS !$#gene rpsI !$#map_position 70 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX small subunit ribosomal proteins: S1 (PIR:R3EC1), S2 !1(PIR:R3EC2), S3 (PIR:R3EC3), S4 (PIR:R3EC4), S5 (PIR:R3EC5), !1S6 (PIR:R3EC6), S7 (PIR:R3EC7K), S8 (PIR:R3EC8), S9 !1(PIR:R3EC9), S10 (PIR:R3EC10), S11 (PIR:R3EC11), S12 !1(PIR:R3EC12), S13 (PIR:R3EC13), S14 (PIR:R3EC14), S15 !1(PIR:R3EC15), S16 (PIR:R3EC16), S17 (PIR:R3EC17), S18 !1(PIR:R3EC18), S19 (PIR:R3EC19), S20/L26 (PIR:R3EC20), S21 !1(PIR:R3EC21), S22 (PIR:C64901) [validated, MUID:99196679] FUNCTION !$#pathway protein biosynthesis CLASSIFICATION #superfamily Escherichia coli ribosomal protein S9 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-130 #product ribosomal protein S9 #status experimental !8#label MAT SUMMARY #length 130 #molecular-weight 14856 #checksum 4326 SEQUENCE /// ENTRY R3BS9 #type complete TITLE ribosomal protein S9 - Bacillus stearothermophilus ALTERNATE_NAMES ribosomal protein BS10 ORGANISM #formal_name Bacillus stearothermophilus DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 30-Jun-1993 ACCESSIONS S08564 REFERENCE S07223 !$#authors Kimura, M.; Chow, C.K. !$#journal Eur. J. Biochem. (1984) 139:225-234 !$#title The complete amino acid sequences of ribosomal proteins L17, !1L27, and S9 from Bacillus stearothermophilus. !$#cross-references MUID:84132037; PMID:6365549 !$#accession S08564 !'##molecule_type protein !'##residues 1-129 ##label KIM !'##note the sequence from Fig. 5 is inconsistent with that from Fig. 3 !1in having 45-Phe CLASSIFICATION #superfamily Escherichia coli ribosomal protein S9 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 129 #molecular-weight 14340 #checksum 2086 SEQUENCE /// ENTRY R3RT20 #type complete TITLE ribosomal protein S20, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 21-Jul-2000 ACCESSIONS S14682; S10391 REFERENCE S14682 !$#authors Chan, Y.L.; Wool, I.G. !$#journal Biochim. Biophys. Acta (1990) 1049:93-95 !$#title The primary structure of rat ribosomal protein S20. !$#cross-references MUID:90291034; PMID:2357470 !$#accession S14682 !'##molecule_type mRNA !'##residues 1-119 ##label CHA !'##cross-references EMBL:X51537; NID:g57719; PIDN:CAA35917.1; !1PID:g57720 !'##experimental_source strain Sprague-Dawley !'##note the protein is designated as ribosomal protein S20 according to !1comigration analysis after in vitro translation CLASSIFICATION #superfamily Escherichia coli ribosomal protein S10 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 119 #molecular-weight 13373 #checksum 5162 SEQUENCE /// ENTRY R3EC10 #type complete TITLE ribosomal protein S10 [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 28-Feb-1981 #sequence_revision 28-Feb-1981 #text_change 01-Mar-2002 ACCESSIONS A02720; A23129; A30422; D65125 REFERENCE A02720 !$#authors Olins, P.O.; Nomura, M. !$#journal Cell (1981) 26:205-211 !$#title Regulation of the S10 ribosomal protein operon in E. coli: !1nucleotide sequence at the start of the operon. !$#cross-references MUID:82137054; PMID:7037196 !$#accession A02720 !'##molecule_type DNA !'##residues 1-103 ##label OLI !'##cross-references GB:V00344; GB:J01680; NID:g42856; PIDN:CAA23633.1; !1PID:g42857 REFERENCE A23129 !$#authors Zurawski, G.; Zurawski, S.M. !$#journal Nucleic Acids Res. (1985) 13:4521-4526 !$#title Structure of the Escherichia coli S10 ribosomal protein !1operon. !$#cross-references MUID:85242118; PMID:3892488 !$#accession A23129 !'##molecule_type DNA !'##residues 1-103 ##label ZUR !'##cross-references GB:X02613; NID:g42825; PIDN:CAA26459.1; PID:g42826 REFERENCE A30422 !$#authors Yaguchi, M.; Roy, C.; Wittmann, H.G. !$#journal FEBS Lett. (1980) 121:113-116 !$#title The primary structure of protein S10 from the small !1ribosomal subunit of Escherichia coli. !$#cross-references MUID:81114581; PMID:7007073 !$#accession A30422 !'##molecule_type protein !'##residues 1-103 ##label YAG REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65125 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-103 ##label BLAT !'##cross-references GB:AE000408; GB:U00096; NID:g1789694; !1PIDN:AAC76346.1; PID:g1789717; UWGP:b3321 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note no post-translational modifications were observed in mass !1spectrographic analysis; any acid labile modifications may !1have been missed GENETICS !$#gene rpsJ !$#map_position 73 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX small subunit ribosomal proteins: S1 (PIR:R3EC1), S2 !1(PIR:R3EC2), S3 (PIR:R3EC3), S4 (PIR:R3EC4), S5 (PIR:R3EC5), !1S6 (PIR:R3EC6), S7 (PIR:R3EC7K), S8 (PIR:R3EC8), S9 !1(PIR:R3EC9), S10 (PIR:R3EC10), S11 (PIR:R3EC11), S12 !1(PIR:R3EC12), S13 (PIR:R3EC13), S14 (PIR:R3EC14), S15 !1(PIR:R3EC15), S16 (PIR:R3EC16), S17 (PIR:R3EC17), S18 !1(PIR:R3EC18), S19 (PIR:R3EC19), S20/L26 (PIR:R3EC20), S21 !1(PIR:R3EC21), S22 (PIR:C64901) [validated, MUID:99196679] FUNCTION !$#pathway protein biosynthesis !$#note involved in binding tRNA CLASSIFICATION #superfamily Escherichia coli ribosomal protein S10 KEYWORDS protein biosynthesis; ribosome FEATURE !$1-103 #product ribosomal protein S10 #status experimental !8#label MAT SUMMARY #length 103 #molecular-weight 11735 #checksum 9468 SEQUENCE /// ENTRY R3KT10 #type complete TITLE ribosomal protein S10 - Cyanophora paradoxa cyanelle ORGANISM #formal_name cyanelle Cyanophora paradoxa DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S10428; PS0413; S14671; T06894 REFERENCE S10427 !$#authors Loeffelhardt, W. !$#submission submitted to the EMBL Data Library, March 1990 !$#accession S10428 !'##molecule_type DNA !'##residues 1-105 ##label LOE !'##cross-references EMBL:X52143; NID:g11389; PIDN:CAA36388.1; !1PID:g11391 REFERENCE JU0459 !$#authors Bryant, D.A.; Schluchter, W.M.; Stirewalt, V.L. !$#journal Gene (1991) 98:169-175 !$#title Ferredoxin and ribosomal protein S10 are encoded on the !1cyanelle genome of Cyanophora paradoxa. !$#cross-references MUID:91200662; PMID:1901820 !$#accession PS0413 !'##molecule_type DNA !'##residues 1-105 ##label BRY !'##cross-references GB:M35206; NID:g336630; PIDN:AAA31700.1; !1PID:g336632 REFERENCE S11048 !$#authors Neumann-Spallart, C.; Brandtner, M.; Kraus, M.; Jakowitsch, !1J.; Bayer, M.G.; Maier, T.L.; Schenk, H.E.A.; Loeffelhardt, !1W. !$#journal FEBS Lett. (1990) 268:55-58 !$#title The petFI gene encoding ferredoxin I is located close to the !1str operon on the cyanelle genome of Cyanophora paradoxa. !$#cross-references MUID:90346172; PMID:2116981 !$#accession S14671 !'##status translation not shown !'##molecule_type DNA !'##residues 93-105 ##label NEU REFERENCE Z15840 !$#authors Stirewalt, V.L.; Michalowski, C.B.; Luffelhardt, W.; !1Bohnert, H.J.; Bryant, D.A. !$#submission submitted to the EMBL Data Library, July 1995 !$#description Nucleotide sequence of the cyanelle genome from Cyanophora !1paradoxa. !$#accession T06894 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-105 ##label STI !'##cross-references EMBL:U30821; NID:g1016083; PIDN:AAA81237.1; !1PID:g1016150 !'##experimental_source strain Pringsheim LB555 GENETICS !$#gene rps10 !$#genome cyanelle CLASSIFICATION #superfamily Escherichia coli ribosomal protein S10 KEYWORDS cyanelle; protein biosynthesis; ribosome SUMMARY #length 105 #molecular-weight 11968 #checksum 7172 SEQUENCE /// ENTRY R3YM10 #type complete TITLE ribosomal protein S10 - Mycoplasma capricolum ORGANISM #formal_name Mycoplasma capricolum DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 07-Dec-1999 ACCESSIONS S02830 REFERENCE S02830 !$#authors Ohkubo, S.; Muto, A.; Kawauchi, Y.; Yamao, F.; Osawa, S. !$#journal Mol. Gen. Genet. (1987) 210:314-322 !$#title The ribosomal protein gene cluster of Mycoplasma capricolum. !$#cross-references MUID:88142549; PMID:3481422 !$#accession S02830 !'##molecule_type DNA !'##residues 1-102 ##label OHK !'##cross-references EMBL:X06414; NID:g44207; PIDN:CAA29703.1; !1PID:g44208 GENETICS !$#gene rps10 !$#genetic_code SGC3 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S10 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 102 #molecular-weight 11545 #checksum 4937 SEQUENCE /// ENTRY R3MX10 #type complete TITLE ribosomal protein S10 - Methanococcus vannielii ORGANISM #formal_name Methanococcus vannielii DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S06625 REFERENCE S06620 !$#authors Lechner, K.; Heller, G.; Boeck, A. !$#journal J. Mol. Evol. (1989) 29:20-27 !$#title Organization and nucleotide sequence of a transcriptional !1unit of Methanococcus vannielii comprising genes for protein !1synthesis elongation factors and ribosomal proteins. !$#cross-references MUID:89362493; PMID:2475640 !$#accession S06625 !'##molecule_type DNA !'##residues 1-91 ##label LEC !'##cross-references EMBL:X15972; NID:g44787; PIDN:CAA34093.1; !1PID:g44788 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S10 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 91 #molecular-weight 10268 #checksum 1074 SEQUENCE /// ENTRY T09380 #type complete TITLE ribosomal protein S10 [similarity] - Halobacterium salinarum ORGANISM #formal_name Halobacterium salinarum DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 21-Jul-2000 ACCESSIONS T09380 REFERENCE Z16653 !$#authors Fujita, T.; Itoh, T. !$#journal Biochem. Mol. Biol. Int. (1995) 37:107-115 !$#title Organization and nucleotide sequence of a gene cluster !1comprising the translation elongation factor 1alpha, !1ribosomal protein S10 and tRNA-ala from Halobacterium !1halobium. !$#cross-references MUID:96109483; PMID:8653072 !$#accession T09380 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-102 ##label FUJ !'##cross-references EMBL:D32120 !'##experimental_source strain A9 !'##note the source is designated as Halobacterium halobium CLASSIFICATION #superfamily Escherichia coli ribosomal protein S10 KEYWORDS ribosome SUMMARY #length 102 #molecular-weight 11466 #checksum 5085 SEQUENCE /// ENTRY R3UC10 #type complete TITLE ribosomal protein S10 - Sulfolobus acidocaldarius ORGANISM #formal_name Sulfolobus acidocaldarius DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 22-Jun-1999 ACCESSIONS S12819 REFERENCE S12817 !$#authors Auer, J. !$#submission submitted to the EMBL Data Library, March 1990 !$#accession S12819 !'##molecule_type DNA !'##residues 1-102 ##label AUE !'##cross-references EMBL:X52382; NID:g46562; PIDN:CAA36609.1; !1PID:g46565 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S10 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 102 #molecular-weight 11984 #checksum 7826 SEQUENCE /// ENTRY R3HU6 #type complete TITLE ribosomal protein S6, cytosolic [validated] - human ALTERNATE_NAMES phosphoprotein NP33 ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1990 #sequence_revision 30-Jun-1993 #text_change 08-Dec-2000 ACCESSIONS JC1394; JT0300; I38189; A28196; A60535; A61380; S68917; !1S25065 REFERENCE JC1394 !$#authors Pata, I.; Hoth, S.; Kruppa, J.; Metspalu, A. !$#journal Gene (1992) 121:387-392 !$#title The human ribosomal protein S6 gene: Isolation, primary !1structure and location in chromosome 9. !$#cross-references MUID:93077059; PMID:1446836 !$#accession JC1394 !'##molecule_type DNA !'##residues 1-249 ##label PAT !'##cross-references GB:M77232; NID:g307392; PIDN:AAA60289.1; !1PID:g307393 REFERENCE A91596 !$#authors Lott, J.B.; Mackie, G.A. !$#journal Gene (1988) 65:31-39 !$#title Isolation and characterization of cloned cDNAs that code for !1human ribosomal protein S6. !$#cross-references MUID:88284378; PMID:2840355 !$#accession JT0300 !'##molecule_type mRNA !'##residues 1-249 ##label LOT !'##cross-references GB:M77232; NID:g307392; PIDN:AAA60289.1; !1PID:g307393 REFERENCE I38189 !$#authors Antoine, M.; Fried, M. !$#journal Hum. Mol. Genet. (1992) 1:565-570 !$#title The organization of the intron-containing human S6 ribosomal !1protein (rpS6) gene and determination of its location at !1chromosome 9p21. !$#cross-references MUID:93244794; PMID:1301164 !$#accession I38189 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-249 ##label RES !'##cross-references EMBL:X67309; NID:g36147; PIDN:CAA47719.1; !1PID:g36148 REFERENCE A92710 !$#authors Heinze, H.; Arnold, H.H.; Fischer, D.; Kruppa, J. !$#journal J. Biol. Chem. (1988) 263:4139-4144 !$#title The primary structure of the human ribosomal protein S6 !1derived from a cloned cDNA. !$#cross-references MUID:88153727; PMID:3279029 !$#accession A28196 !'##molecule_type mRNA !'##residues 1-154,'EC',157-167,'R',169-218,'Q',220-249 ##label HEI !'##cross-references GB:J03537; NID:g337513; PIDN:AAA60287.1; !1PID:g337514 REFERENCE A60535 !$#authors Macfarlane, D.E.; Gailani, D. !$#journal Cancer Res. (1990) 50:2895-2900 !$#title Identification of phosphoprotein NP33 as a !1nucleus-associated ribosomal S6 protein and its !1phosphorylation in hematopoietic cells. !$#cross-references MUID:90242254; PMID:2334893 !$#accession A60535 !'##molecule_type protein !'##residues 3-9,'G',11,'G',13-16,'X',18 ##label MAC !'##note this protein copurified with nuclear matrix material but was !1also found in ribosomes REFERENCE A61380 !$#authors Penner, C.G.; Murphy, L.C.; Huzel, N.J.; Yamada, E.W. !$#journal Mol. Cell. Biochem. (1991) 108:57-66 !$#title Antigenic reactivity of ribosomal protein S6 and the !1calcium-binding ATPase inhibitor protein of mammalian !1mitochondria. !$#cross-references MUID:92123165; PMID:1837589 !$#accession A61380 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 'D',57-249 ##label PEN REFERENCE S68911 !$#authors Vladimirov, S.N.; Ivanov, A.V.; Karpova, G.G.; Musolyamov, !1A.K.; Egorov, T.A.; Thiede, B.; Wittmann-Liebold, B.; Otto, !1A. !$#journal Eur. J. Biochem. (1996) 239:144-149 !$#title Characterization of the human small-ribosomal-subunit !1proteins by N-terminal and internal sequencing, and mass !1spectrometry. !$#cross-references MUID:96305378; PMID:8706699 !$#accession S68917 !'##molecule_type protein !'##residues 1-11,'X',13-15 ##label VLA COMMENT This protein is phosphorylated by ribosomal protein S6 !1kinase (see PIR:A41687). GENETICS !$#gene GDB:RPS6 !'##cross-references GDB:118869; OMIM:180460 !$#map_position 9p21-9p21 !$#introns 2/3; 46/3; 117/1; 166/1; 218/3 CLASSIFICATION #superfamily rat ribosomal protein S6 KEYWORDS phosphoprotein; protein biosynthesis; ribosome FEATURE !$1-249 #product ribosomal protein S6, cytosolic #status !8experimental #label MAT\ !$235,236,240,244,247 #binding_site phosphate (Ser) (covalent) (by !8ribosomal protein S6 kinase) #status predicted SUMMARY #length 249 #molecular-weight 28680 #checksum 4333 SEQUENCE /// ENTRY R3RTS6 #type complete TITLE ribosomal protein S6, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 21-Jul-2000 ACCESSIONS A29929; S11414; A35713; S11573 REFERENCE A29929 !$#authors Chan, Y.L.; Wool, I.G. !$#journal J. Biol. Chem. (1988) 263:2891-2896 !$#title The primary structure of rat ribosomal protein S6. !$#cross-references MUID:88139341; PMID:3277962 !$#accession A29929 !'##molecule_type mRNA !'##residues 1-249 ##label CHA !'##cross-references GB:M29358; NID:g206746; PIDN:AAA42079.1; !1PID:g206747 !'##note part of this sequence was confirmed by protein sequencing !'##note the protein is designated as ribosomal protein S6 REFERENCE S11413 !$#authors Wittmann-Liebold, B.; Geissler, A.W.; Lin, A.; Wool, I.G. !$#journal J. Supramol. Struct. (1979) 12:425-433 !$#title Sequence of the amino-terminal region of rat liver ribosomal !1proteins S4, S6, S8, L6, L7a, L18, L27, L30, L37, L37a, and !1L39. !$#cross-references MUID:80252792; PMID:398910 !$#accession S11414 !'##molecule_type protein !'##residues 1-11,'S',13-15,'L',17-25,'X',27-30,'X',32-33 ##label WIT !'##note the protein is designated as ribosomal protein S6 REFERENCE A35713 !$#authors Franco, R.; Rosenfeld, M.G. !$#journal J. Biol. Chem. (1990) 265:4321-4325 !$#title Hormonally inducible phosphorylation of a nuclear pool of !1ribosomal protein S6. !$#cross-references MUID:90170932; PMID:2106518 !$#accession A35713 !'##molecule_type protein !'##residues 1-11,'X',13-23 ##label FRA REFERENCE S11573 !$#authors Wettenhall, R.E.H.; Morgan, F.J. !$#journal J. Biol. Chem. (1984) 259:2084-2091 !$#title Phosphorylation of hepatic ribosomal protein S6 on 80 and 40 !1S ribosomes. Primary structure of S6 in the region of the !1major phosphorylation sites for cAMP-dependent protein !1kinases. !$#cross-references MUID:84135657; PMID:6698958 !$#accession S11573 !'##molecule_type protein !'##residues 232-245,'E',247-249 ##label WET !'##note the protein is designated as ribosomal protein S6 CLASSIFICATION #superfamily rat ribosomal protein S6 KEYWORDS phosphoprotein; protein biosynthesis; ribosome; RNA binding FEATURE !$1-249 #product ribosomal protein S6 #status experimental !8#label MAT\ !$235,236 #binding_site phosphate (Ser) (covalent) (by !8ribosomal protein S6 kinase) #status experimental\ !$240,244,247 #binding_site phosphate (Ser) (covalent) (by !8ribosomal protein S6 kinase) #status predicted SUMMARY #length 249 #molecular-weight 28680 #checksum 4333 SEQUENCE /// ENTRY R3MS6 #type complete TITLE ribosomal protein S6 - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jun-2000 ACCESSIONS S00660; JC5049 REFERENCE S00660 !$#authors Lalanne, J.L.; Lucero, M.; le Moullec, J.M. !$#journal Nucleic Acids Res. (1987) 15:4990 !$#title Complete sequence of mouse S6 ribosomal protein. !$#cross-references MUID:87259978; PMID:3601662 !$#accession S00660 !'##molecule_type mRNA !'##residues 1-249 ##label LAL !'##cross-references EMBL:Y00348; NID:g54009; PIDN:CAA68430.1; !1PID:g54010 REFERENCE JC5049 !$#authors Pata, I.; Metspalu, A. !$#journal Gene (1996) 175:241-245 !$#title Structural characterization of the mouse ribosomal protein !1S6-encoding gene. !$#cross-references MUID:97074678; PMID:8917105 !$#accession JC5049 !'##molecule_type DNA !'##residues 1-249 ##label PAT !'##cross-references EMBL:Z54209; NID:g1177548; PIDN:CAA90936.1; !1PID:g1177549 COMMENT This protein is 40S subunit protein for being phosphorylated !1in response to cell growth upon mitogenic stimulation. The !1phosphorylation occurs on upto 5 serine residues near !1C-terminus. GENETICS !$#gene Rps6 !$#introns 2/3; 46/3; 117/1; 166/1 CLASSIFICATION #superfamily rat ribosomal protein S6 KEYWORDS phosphoprotein; protein biosynthesis; ribosome FEATURE !$235,236,240,244,247 #binding_site phosphate (Ser) (covalent) (by !8ribosomal protein S6 kinase) #status predicted SUMMARY #length 249 #molecular-weight 28680 #checksum 4333 SEQUENCE /// ENTRY R3ZP6E #type complete TITLE 40s ribosomal protein S6.e, cytosolic - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES protein SPAC13G6.07c; ribosomal protein SP-S6 ORGANISM #formal_name Schizosaccharomyces pombe DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 10-Dec-1999 ACCESSIONS S06463; S07293; T37642; S62436 REFERENCE S06463 !$#authors Gross, T.; Nischt, R.; Gatermann, K.; Swida, U.; Kaeufer, !1N.F. !$#journal Curr. Genet. (1988) 13:57-63 !$#title Primary structure of the ribosomal protein gene S6 from !1Schizosaccharomyces pombe. !$#cross-references MUID:88194708; PMID:2834104 !$#accession S06463 !'##molecule_type DNA !'##residues 1-239 ##label GRO !'##cross-references GB:M36382; NID:g173473; PIDN:AAA35338.1; !1PID:g173474 REFERENCE S07293 !$#authors Otaka, E.; Higo, K.I.; Itoh, T. !$#journal Mol. Gen. Genet. (1983) 191:519-524 !$#title Yeast ribosomal proteins: VII. Cytoplasmic ribosomal !1proteins from Schizosaccharomyces pombe. !$#cross-references MUID:84038947; PMID:6355773 !$#accession S07293 !'##molecule_type protein !'##residues 1-39,'A' ##label OTA !'##note the amidation states of residues 4, 10, 13, 17, 19, 20, 21, 29, !124, 25, and 39 were not determined REFERENCE Z21734 !$#authors Odell, C.; Bowman, S.; Barrell, B.G.; Rajandream, M.A.; !1Walsh, S.V.; Wood, V. !$#submission submitted to the EMBL Data Library, October 1995 !$#accession T37642 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-239 ##label OD2 !'##cross-references EMBL:Z54308; PIDN:CAA91100.1; PID:g1008992; !1GSPDB:GN00066; SPDB:SPAC13G6.07c !'##experimental_source strain 972h-; cosmid c13G6 GENETICS !$#gene RPS6 !$#map_position 1L CLASSIFICATION #superfamily rat ribosomal protein S6 KEYWORDS phosphoprotein; protein biosynthesis; ribosome FEATURE !$1-239 #product ribosomal protein S6.e #status experimental !8#label MAT\ !$235,236 #binding_site phosphate (Ser) (covalent) (by !8ribosomal protein S6 kinase) #status predicted SUMMARY #length 239 #molecular-weight 27499 #checksum 5367 SEQUENCE /// ENTRY R3BY10 #type complete TITLE ribosomal protein S6.e, cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein LPG18w; protein YBR1244; protein YBR181c; protein YPL090c; ribosomal protein YS10; ribosomal protein YS4 ORGANISM #formal_name Saccharomyces cerevisiae DATE 13-Jun-1983 #sequence_revision 30-Sep-1987 #text_change 21-Jul-2000 ACCESSIONS A23787; S46052; A02721; S44921; S11575; S61976 REFERENCE A93574 !$#authors Leer, R.J.; van Raamsdonk-Duin, M.M.C.; Molenaar, C.M.T.; !1Witsenboer, H.M.A.; Mager, W.H.; Planta, R.J. !$#journal Nucleic Acids Res. (1985) 13:5027-5039 !$#title Yeast contains two functional genes coding for ribosomal !1protein S10. !$#cross-references MUID:85269625; PMID:2991849 !$#note S. carlsbergensis, sequence of the S10-2 gene !$#accession A23787 !'##molecule_type DNA !'##residues 1-236 ##label LEE1 !'##cross-references EMBL:X02746; NID:g4401; PIDN:CAA26525.1; PID:g4402 !'##genetics RPS102 REFERENCE S46013 !$#authors Entian, K.D.; Koetter, P.; Rose, M.; Becker, J.; Grey, M.; !1Li, Z.; Niegemann, E.; Schenk-Groeninger, R.; Servos, J.; !1Wehner, E.; Wolter, R.; Brendel, M.; Bauer, J.; Braun, H.; !1Dern, K.; Duesterhus, S.; Gruenbein, R.; Hedges, D.; Kiesau, !1P.; Korol, S.; Krems, B.; Proft, M.; Siegers, K.; Baur, A.; !1Boles, E.; Miosga, T.; Schaaff-Gerstenschlaeger, I.; !1Zimmermann, F.K. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S46052 !'##molecule_type DNA !'##residues 1-236 ##label ENT !'##cross-references EMBL:Z36050; GSPDB:GN00002; MIPS:YBR181c; !1NID:g536533; PIDN:CAA85142.1; PID:g536534 !'##genetics RPS101 REFERENCE A93441 !$#authors Leer, R.J.; van Raamsdonk-Duin, M.M.C.; Molenaar, C.M.T.; !1Cohen, L.H.; Mager, W.H.; Planta, R.J. !$#journal Nucleic Acids Res. (1982) 10:5869-5878 !$#title The structure of the gene coding for the phosphorylated !1ribosomal protein S10 in yeast. !$#cross-references MUID:83064524; PMID:6292856 !$#note S. carlsbergensis, sequence of the S10-1 gene !$#accession A02721 !'##molecule_type DNA !'##residues 3-180,'S',182-236 ##label LEE2 !'##cross-references EMBL:J01350 !'##genetics RPS101 REFERENCE S07293 !$#authors Otaka, E.; Higo, K.I.; Itoh, T. !$#journal Mol. Gen. Genet. (1983) 191:519-524 !$#title Yeast ribosomal proteins: VII. Cytoplasmic ribosomal !1proteins from Schizosaccharomyces pombe. !$#cross-references MUID:84038947; PMID:6355773 !$#accession S44921 !'##molecule_type protein !'##residues 1-9,'B',11,'A',13,'L',15-24,'X',26-28,'X',30 ##label OTA !'##note this is a revision to the sequence from reference S11575 REFERENCE S11575 !$#authors Otaka, E.; Higo, K.; Osawa, S. !$#journal Biochemistry (1982) 21:4545-4550 !$#title Isolation of seventeen proteins and amino-terminal amino !1acid sequences of eight proteins from cytoplasmic ribosomes !1of yeast. !$#cross-references MUID:83048950; PMID:6814480 !$#accession S11575 !'##molecule_type protein !'##residues 'A',2-9,'B',11,'A',13,'L',15-24,'X',26-28,'X',30 ##label !1OT2 !'##note this sequence has been revised in reference S07293 REFERENCE S61959 !$#authors Wang, Y.; Ahmed, A.; Bussey, H.; Fortin, N.; Friesen, J.D.; !1Hall, J.; Storms, R.K.; Vo, D.H.; Winnett, E. !$#submission submitted to the EMBL Data Library, December 1995 !$#description The sequence of Saccharomyces cerevisiae chromosome XVI left !1arm. !$#accession S61976 !'##molecule_type DNA !'##residues 1,'R',3-236 ##label WAN !'##cross-references EMBL:U43281; NID:g1151218; PIDN:AAB68209.1; !1PID:g1151236; GSPDB:GN00016; MIPS:YPL090c !'##genetics RPS102 GENETICS RPS101 !$#gene SGD:RPS10A; RPS101; MIPS:YBR181c !'##cross-references MIPS:YBR181c; SGD:S0000385 !$#map_position 2R !$#introns 2/3 GENETICS RPS102 !$#gene RPS102; MIPS:YPL090c !'##cross-references MIPS:YPL090c !$#map_position 16L !$#introns 2/3 CLASSIFICATION #superfamily rat ribosomal protein S6 KEYWORDS phosphoprotein; protein biosynthesis; ribosome FEATURE !$232,233 #binding_site phosphate (Ser) (covalent) (by !8ribosomal protein S6 kinase) #status predicted SUMMARY #length 236 #molecular-weight 26996 #checksum 3703 SEQUENCE /// ENTRY S55918 #type complete TITLE ribosomal protein S10, cytosolic [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 28-Oct-1995 #sequence_revision 03-Nov-1995 #text_change 08-Dec-2000 ACCESSIONS S55918; S68927 REFERENCE S55912 !$#authors Frigerio, J.M.; Dagorn, J.C.; Iovanna, J.L. !$#journal Biochim. Biophys. Acta (1995) 1262:64-68 !$#title Cloning, sequencing and expression of the L5, L21, L27a, !1L28, S5, S9, S10 and S29 human ribosomal protein mRNAs. !$#cross-references MUID:95290496; PMID:7772601 !$#accession S55918 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-165 ##label FRI !'##cross-references EMBL:U14972; NID:g550024; PIDN:AAA85660.1; !1PID:g550025 !'##experimental_source colon tumor REFERENCE S68911 !$#authors Vladimirov, S.N.; Ivanov, A.V.; Karpova, G.G.; Musolyamov, !1A.K.; Egorov, T.A.; Thiede, B.; Wittmann-Liebold, B.; Otto, !1A. !$#journal Eur. J. Biochem. (1996) 239:144-149 !$#title Characterization of the human small-ribosomal-subunit !1proteins by N-terminal and internal sequencing, and mass !1spectrometry. !$#cross-references MUID:96305378; PMID:8706699 !$#accession S68927 !'##molecule_type protein !'##residues 1-15 ##label VLA GENETICS !$#gene GDB:RPS10 !'##cross-references GDB:6283091 CLASSIFICATION #superfamily rat ribosomal protein S10; ribosomal protein !1S10 homology KEYWORDS cytosol; protein biosynthesis; ribosome FEATURE !$1-165 #product ribosomal protein S10, cytosolic #status !8experimental #label MAT\ !$2-100 #domain ribosomal protein S10 homology #label RS10 SUMMARY #length 165 #molecular-weight 18898 #checksum 3876 SEQUENCE /// ENTRY R3RT10 #type complete TITLE ribosomal protein S10, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 21-Jul-2000 ACCESSIONS S01881; A38057 REFERENCE S01881 !$#authors Glueck, A.; Chan, Y.L.; Lin, A.; Wool, I.G. !$#journal Eur. J. Biochem. (1989) 182:105-109 !$#title The primary structure of rat ribosomal protein S10. !$#cross-references MUID:89276370; PMID:2543570 !$#accession S01881 !'##molecule_type mRNA !'##residues 1-165 ##label GLU !'##cross-references EMBL:X13549; NID:g57126; PIDN:CAA31901.1; !1PID:g57127 !$#accession A38057 !'##molecule_type protein !'##residues 1-24 ##label GLU2 !'##note the protein is designated as ribosomal protein S10 GENETICS !$#gene rps10 CLASSIFICATION #superfamily rat ribosomal protein S10; ribosomal protein !1S10 homology KEYWORDS protein biosynthesis; ribosome FEATURE !$1-165 #product ribosomal protein S10 #status experimental !8#label MAT\ !$2-100 #domain ribosomal protein S10 homology #label RS10 SUMMARY #length 165 #molecular-weight 18916 #checksum 4066 SEQUENCE /// ENTRY I51194 #type complete TITLE ribosomal protein S10, cytosolic - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 13-Sep-1996 #sequence_revision 13-Sep-1996 #text_change 22-Jun-1999 ACCESSIONS I51194 REFERENCE I51194 !$#authors Sarrowa, J.; Steiner, L.A. !$#journal Mol. Immunol. (1993) 30:387-394 !$#title Primary structure of Xenopus laevis S10, a ribosomal protein !1that cross-reacts with antibodies to immunoglobulin light !1chains. !$#cross-references MUID:93205015; PMID:7681149 !$#accession I51194 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-165 ##label SAR !'##cross-references GB:S57432; NID:g301828; PIDN:AAA14676.1; !1PID:g301829 CLASSIFICATION #superfamily rat ribosomal protein S10; ribosomal protein !1S10 homology KEYWORDS cytosol; protein biosynthesis; ribosome FEATURE !$2-100 #domain ribosomal protein S10 homology #label RS10 SUMMARY #length 165 #molecular-weight 18883 #checksum 2231 SEQUENCE /// ENTRY S67197 #type complete TITLE ribosomal protein S10.e.A, cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein O5611; protein YOR293w ORGANISM #formal_name Saccharomyces cerevisiae DATE 12-Jul-1996 #sequence_revision 12-Jul-1996 #text_change 19-Apr-2002 ACCESSIONS S67197 REFERENCE S67194 !$#authors Cziepluch, C.; Jauniaux, J.C.; Kordes, E.; Poirey, R.; !1Pujol, A.; Tobiasch, E. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67197 !'##molecule_type DNA !'##residues 1-105 ##label CZI !'##cross-references EMBL:Z75201; GSPDB:GN00015; MIPS:YOR293w; !1NID:g1420649; PIDN:CAA99521.1; PID:g1420650 !'##experimental_source strain S288C GENETICS !$#gene SGD:RPS10A; MIPS:YOR293w !'##cross-references SGD:S0005819 !$#map_position 15R !$#introns 18/1 CLASSIFICATION #superfamily rat ribosomal protein S10; ribosomal protein !1S10 homology KEYWORDS cytosol; protein biosynthesis; ribosome FEATURE !$2-97 #domain ribosomal protein S10 homology #label RS10 SUMMARY #length 105 #molecular-weight 12739 #checksum 1317 SEQUENCE /// ENTRY S57597 #type complete TITLE ribosomal protein S10.e.B, cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YM9959.12; protein YMR230w ORGANISM #formal_name Saccharomyces cerevisiae DATE 19-Oct-1995 #sequence_revision 03-Nov-1995 #text_change 19-Apr-2002 ACCESSIONS S57597 REFERENCE S57587 !$#authors Skelton, J.; Churcher, C.M. !$#submission submitted to the EMBL Data Library, June 1995 !$#accession S57597 !'##molecule_type DNA !'##residues 1-105 ##label SKE !'##cross-references EMBL:Z49939; NID:g887599; PIDN:CAA90201.1; !1PID:g887611; GSPDB:GN00013; MIPS:YMR230w !'##experimental_source strain AB972 GENETICS !$#gene SGD:RPS10B; MIPS:YMR230w !'##cross-references SGD:S0004843 !$#map_position 13R !$#introns 18/1 CLASSIFICATION #superfamily rat ribosomal protein S10; ribosomal protein !1S10 homology KEYWORDS cytosol; protein biosynthesis; ribosome FEATURE !$2-97 #domain ribosomal protein S10 homology #label RS10 SUMMARY #length 105 #molecular-weight 12738 #checksum 1355 SEQUENCE /// ENTRY R3EC11 #type complete TITLE ribosomal protein S11 [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 28-Feb-1981 #sequence_revision 30-Jun-1991 #text_change 01-Mar-2002 ACCESSIONS B23807; A02722; D65122 REFERENCE A23807 !$#authors Bedwell, D.; Davis, G.; Gosink, M.; Post, L.; Nomura, M.; !1Kestler, H.; Zengel, J.M.; Lindahl, L. !$#journal Nucleic Acids Res. (1985) 13:3891-3903 !$#title Nucleotide sequence of the alpha ribosomal protein operon of !1Escherichia coli. !$#cross-references MUID:85242076; PMID:2989779 !$#accession B23807 !'##molecule_type DNA !'##residues 1-129 ##label BED !'##cross-references GB:X02543; NID:g42795; PIDN:CAA26393.1; PID:g42797 REFERENCE A02722 !$#authors Kamp, R.; Wittmann-Liebold, B. !$#journal FEBS Lett. (1980) 121:117-122 !$#title Primary structure of protein S11 from Escherichia coli !1ribosomes. !$#cross-references MUID:81114582; PMID:7007074 !$#accession A02722 !'##molecule_type protein !'##residues 2-129 ##label KAM REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65122 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-129 ##label BLAT !'##cross-references GB:AE000407; GB:U00096; NID:g2367211; !1PIDN:AAC76322.1; PID:g1789692; UWGP:b3297 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note mass spectrographic analysis of post-translational !1modifications; any acid labile modifications may have been !1missed GENETICS !$#gene rpsK !$#map_position 73 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX small subunit ribosomal proteins: S1 (PIR:R3EC1), S2 !1(PIR:R3EC2), S3 (PIR:R3EC3), S4 (PIR:R3EC4), S5 (PIR:R3EC5), !1S6 (PIR:R3EC6), S7 (PIR:R3EC7K), S8 (PIR:R3EC8), S9 !1(PIR:R3EC9), S10 (PIR:R3EC10), S11 (PIR:R3EC11), S12 !1(PIR:R3EC12), S13 (PIR:R3EC13), S14 (PIR:R3EC14), S15 !1(PIR:R3EC15), S16 (PIR:R3EC16), S17 (PIR:R3EC17), S18 !1(PIR:R3EC18), S19 (PIR:R3EC19), S20/L26 (PIR:R3EC20), S21 !1(PIR:R3EC21), S22 (PIR:C64901) [validated, MUID:99196679] FUNCTION !$#pathway protein biosynthesis CLASSIFICATION #superfamily Escherichia coli ribosomal protein S11 KEYWORDS methylated amino end; protein biosynthesis; ribosome FEATURE !$2-129 #product ribosomal protein S11 #status experimental !8#label MAT\ !$2 #modified_site methylated amino end (Ala) (in mature !8form) #status experimental SUMMARY #length 129 #molecular-weight 13845 #checksum 444 SEQUENCE /// ENTRY R3BSS1 #type complete TITLE ribosomal protein S11 - Bacillus subtilis ALTERNATE_NAMES ribosomal protein BS11 ORGANISM #formal_name Bacillus subtilis DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jun-2000 ACCESSIONS D32307; B24972; S11361; B69700 REFERENCE A32307 !$#authors Boylan, S.A.; Suh, J.W.; Thomas, S.M.; Price, C.W. !$#journal J. Bacteriol. (1989) 171:2553-2562 !$#title Gene encoding the alpha core subunit of Bacillus subtilis !1RNA polymerase is cotranscribed with the genes for !1initiation factor 1 and ribosomal proteins B, S13, S11, and !1L17. !$#cross-references MUID:89213940; PMID:2496109 !$#accession D32307 !'##molecule_type DNA !'##residues 1-131 ##label BOY !'##cross-references GB:M26414; NID:g142458; PIDN:AAA22216.1; !1PID:g142462 REFERENCE A24972 !$#authors Suh, J.W.; Boylan, S.A.; Price, C.W. !$#journal J. Bacteriol. (1986) 168:65-71 !$#title Gene for the alpha subunit of Bacillus subtilis RNA !1polymerase maps in the ribosomal protein gene cluster. !$#cross-references MUID:87008431; PMID:3093467 !$#accession B24972 !'##molecule_type DNA !'##residues 1-131 ##label SUH !'##cross-references GB:M13957; NID:g143449; PIDN:AAA22707.1; !1PID:g143451 REFERENCE S09561 !$#authors Higo, K.I.; Otaka, E.; Osawa, S. !$#journal Mol. Gen. Genet. (1982) 185:239-244 !$#title Purification and characterization of 30S ribosomal proteins !1from Bacillus subtilis: correlation to Escherichia coli 30S !1proteins. !$#cross-references MUID:82219212; PMID:6806564 !$#accession S11361 !'##molecule_type protein !'##residues 4-18,'SE',21-29,'BB',32-35 ##label HIG REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69700 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-131 ##label KUN !'##cross-references GB:Z99104; GB:AL009126; NID:g2632267; !1PIDN:CAB11918.1; PID:g2632409 !'##experimental_source strain 168 GENETICS !$#gene rpsK CLASSIFICATION #superfamily Escherichia coli ribosomal protein S11 KEYWORDS protein biosynthesis; ribosome FEATURE !$4-131 #product ribosomal protein S11 #status experimental !8#label MAT SUMMARY #length 131 #molecular-weight 13925 #checksum 785 SEQUENCE /// ENTRY R3BS11 #type complete TITLE ribosomal protein S11 [validated] - Bacillus stearothermophilus ALTERNATE_NAMES ribosomal protein BS11 ORGANISM #formal_name Bacillus stearothermophilus DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 26-May-2000 ACCESSIONS S01781 REFERENCE S01781 !$#authors Kimura, M.; Kimura, J.; Hatakeyama, T. !$#journal FEBS Lett. (1988) 240:15-20 !$#title Amino acid sequences of ribosomal proteins S11 from Bacillus !1stearothermophilus and S19 from Halobacterium marismortui. !1Comparison of the ribosomal protein S11 family. !$#cross-references MUID:89052875; PMID:3191988 !$#accession S01781 !'##molecule_type protein !'##residues 1-128 ##label KIM !'##note the protein is designated ribosomal protein S11 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S11 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 128 #molecular-weight 13680 #checksum 6587 SEQUENCE /// ENTRY R3LV11 #type complete TITLE ribosomal protein S11, chloroplast - liverwort (Marchantia polymorpha) chloroplast ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 22-Jun-1999 ACCESSIONS A02723; S01564 REFERENCE A00150 !$#authors Ohyama, K. !$#submission submitted to the EMBL Data Library, October 1986 !$#accession A02723 !'##molecule_type DNA !'##residues 1-130 ##label OHY REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features REFERENCE S01529 !$#authors Fukuzawa, H.; Kohchi, T.; Sano, T.; Shirai, H.; Umesono, K.; !1Inokuchi, H.; Ozeki, H.; Ohyama, K. !$#journal J. Mol. Biol. (1988) 203:333-351 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. III. Gene organization of the large !1single copy region from rbcL to trnI(CAU). !$#cross-references MUID:89068687; PMID:3199436 !$#accession S01564 !'##molecule_type DNA !'##residues 1-130 ##label FUK !'##cross-references GB:X04465; GB:Y00686; NID:g11640; PIDN:CAA28118.1; !1PID:g11707 GENETICS !$#gene rps11 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein S11 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 130 #molecular-weight 14173 #checksum 3394 SEQUENCE /// ENTRY R3NT11 #type complete TITLE ribosomal protein S11, chloroplast - common tobacco chloroplast ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 30-Jan-1998 ACCESSIONS A02724 REFERENCE A00149 !$#authors Sugiura, M. !$#submission submitted to the EMBL Data Library, August 1986 !$#accession A02724 !'##molecule_type DNA !'##residues 1-138 ##label SUG !'##experimental_source cv. Bright Yellow 4 REFERENCE A38013 !$#authors Shinozaki, K.; Ohme, M.; Tanaka, M.; Wakasugi, T.; !1Hayashida, N.; Matsubayashi, T.; Zaita, N.; Chunwongse, J.; !1Obokata, J.; Yamaguchi-Shinozaki, K.; Ohto, C.; Torazawa, !1K.; Meng, B.Y.; Sugita, M.; Deno, H.; Kamogashira, T.; !1Yamada, K.; Kusuda, J.; Takaiwa, F.; Kato, A.; Tohdoh, N.; !1Shimada, H.; Sugiura, M. !$#journal EMBO J. (1986) 5:2043-2049 !$#title The complete nucleotide sequence of the tobacco chloroplast !1genome: its gene organization and expression. !$#contents annotation; gene organization, sites, features GENETICS !$#gene rps11 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein S11 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 138 #molecular-weight 14883 #checksum 7589 SEQUENCE /// ENTRY R3PM11 #type complete TITLE ribosomal protein S11, chloroplast - garden pea chloroplast ORGANISM #formal_name chloroplast Pisum sativum #common_name garden pea DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S04383; S11608 REFERENCE S04382 !$#authors Purton, S.; Gray, J.C. !$#journal Mol. Gen. Genet. (1989) 217:77-84 !$#title The plastid rpoA gene encoding a protein homologous to the !1bacterial RNA polymerase alpha subunit is expressed in pea !1chloroplasts. !$#cross-references MUID:89364695; PMID:2671652 !$#accession S04383 !'##molecule_type DNA !'##residues 1-138 ##label PUR !'##cross-references EMBL:X15645; NID:g12178; PIDN:CAA33667.1; !1PID:g12179 !'##experimental_source var. Feltham First GENETICS !$#gene rps11 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein S11 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 138 #molecular-weight 14915 #checksum 7516 SEQUENCE /// ENTRY R3RZ11 #type complete TITLE ribosomal protein S11 - rice chloroplast ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 22-Jun-1999 ACCESSIONS JQ0259; S05139 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0259 !'##molecule_type DNA !'##residues 1-143 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05139 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-143 ##label HIR !'##cross-references GB:X15901; NID:g11957; PIDN:CAA33980.1; PID:g12019 !'##experimental_source cv. Nihonbare !'##note this sequence was submitted to EMBL, July 1989 GENETICS !$#gene rps11 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein S11 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 143 #molecular-weight 15624 #checksum 6155 SEQUENCE /// ENTRY R4HY14 #type complete TITLE ribosomal protein S14 - Chinese hamster ORGANISM #formal_name Cricetulus griseus #common_name Chinese hamster DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 22-Jun-1999 ACCESSIONS A02725; I48124 REFERENCE A02725 !$#authors Rhoads, D.D.; Roufa, D.J. !$#journal Mol. Cell. Biol. (1985) 5:1655-1659 !$#title Emetine resistance of Chinese hamster cells: structures of !1wild-type and mutant ribosomal protein S14 mRNAs. !$#cross-references MUID:85267682; PMID:3839563 !$#accession A02725 !'##molecule_type mRNA !'##residues 1-151 ##label RHO !'##cross-references GB:M11241; NID:g191197; PIDN:AAA37016.1; !1PID:g304525 REFERENCE I48124 !$#authors Rhoads, D.; Roufa, D.J. !$#journal Mol. Biol. Evol. (1991) 8:503-514 !$#title Molecular evolution of the mammalian ribosomal protein gene. !$#cross-references MUID:92017216; PMID:1921707 !$#accession I48124 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-151 ##label RES !'##cross-references GB:M35008; NID:g191199; PIDN:AAA37017.1; !1PID:g387057 GENETICS !$#gene RPS14 !$#map_position 2q !$#introns 50/2; 104/2; 130/1 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S11 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 151 #molecular-weight 16273 #checksum 5109 SEQUENCE /// ENTRY R3RT14 #type complete TITLE ribosomal protein S14, cytosolic [similarity] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 21-Jul-2000 ACCESSIONS S14900; S06197 REFERENCE S14900 !$#authors Paz, V.; Chan, Y.L.; Glueck, A.; Wool, I.G. !$#journal Nucleic Acids Res. (1989) 17:9484 !$#title The primary structure of rat ribosomal protein S14. !$#cross-references MUID:90067957; PMID:2587275 !$#accession S14900 !'##molecule_type mRNA !'##residues 1-151 ##label PAZ !'##cross-references EMBL:X15040; NID:g57128; PIDN:CAA33143.1; !1PID:g57129 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S11 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 151 #molecular-weight 16259 #checksum 5101 SEQUENCE /// ENTRY R5BY59 #type complete TITLE ribosomal protein S14.e.A, cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YCR031c; ribosomal protein 59 ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 21-Jul-2000 ACCESSIONS A02726; A26887; S19443 REFERENCE A93541 !$#authors Teem, J.L.; Abovich, N.; Kaufer, N.F.; Schwindinger, W.F.; !1Warner, J.R.; Levy, A.; Woolford, J.; Leer, R.J.; van !1Raamsdonk-Duin, M.M.C.; Mager, W.H.; Planta, R.J.; Schultz, !1L.; Friesen, J.D.; Fried, H.; Rosbash, M. !$#journal Nucleic Acids Res. (1984) 12:8295-8312 !$#title A comparison of yeast ribosomal protein gene DNA sequences. !$#cross-references MUID:85062814; PMID:6390341 !$#accession A02726 !'##molecule_type DNA !'##residues 1-137 ##label TEE REFERENCE A26887 !$#authors Larkin, J.C.; Thompson, J.R.; Woolford Jr., J.L. !$#journal Mol. Cell. Biol. (1987) 7:1764-1775 !$#title Structure and expression of the Saccharomyces cerevisiae !1CRY1 gene: a highly conserved ribosomal protein gene. !$#cross-references MUID:87257876; PMID:3037334 !$#accession A26887 !'##molecule_type DNA !'##residues 1-137 ##label LAR !'##cross-references GB:M16126; NID:g171321; PIDN:AAA34530.1; !1PID:g171322 REFERENCE S19439 !$#authors Cederberg, H.; Hohmann, S.; Schaaff-Gerstenschlager, I.; !1Huse, K.; Zimmermann, F.K. !$#submission submitted to the Protein Sequence Database, March 1992 !$#accession S19443 !'##molecule_type DNA !'##residues 1-137 ##label CED !'##cross-references EMBL:X59720; GSPDB:GN00003; MIPS:YCR031c GENETICS !$#gene SGD:CRY1; RP59; MIPS:YCR031c !'##cross-references SGD:S0000627; MIPS:YCR031c !$#map_position 3R !$#introns 3/1 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S11 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 137 #molecular-weight 14581 #checksum 2577 SEQUENCE /// ENTRY R3HSS1 #type complete TITLE ribosomal protein S11 [validated] - Haloarcula marismortui ALTERNATE_NAMES ribosomal protein HS19 ORGANISM #formal_name Haloarcula marismortui DATE 31-Mar-1991 #sequence_revision 17-Apr-1998 #text_change 26-May-2000 ACCESSIONS C44126; S01782 REFERENCE A44126 !$#authors Scholzen, T.; Arndt, E. !$#journal J. Biol. Chem. (1992) 267:12123-12130 !$#title The alpha-operon equivalent genome region in the extreme !1halophilic archaebacterium Haloarcula (Halobacterium) !1marismortui. !$#cross-references MUID:92291093; PMID:1376318 !$#accession C44126 !'##status preliminary !'##molecule_type DNA !'##residues 1-129 ##label SCH !'##cross-references GB:M87833; NID:g148769; PIDN:AAA73211.1; !1PID:g148772 !'##note sequence extracted from NCBI backbone (NCBIN:106619, !1NCBIP:106622) REFERENCE S01781 !$#authors Kimura, M.; Kimura, J.; Hatakeyama, T. !$#journal FEBS Lett. (1988) 240:15-20 !$#title Amino acid sequences of ribosomal proteins S11 from Bacillus !1stearothermophilus and S19 from Halobacterium marismortui. !1Comparison of the ribosomal protein S11 family. !$#cross-references MUID:89052875; PMID:3191988 !$#accession S01782 !'##molecule_type protein !'##residues 2-8,'N',10-31,'Q',32-118,'N',120-129 ##label KIM !'##note the source is designated as Halobacterium marismortui !'##note the protein is designated ribosomal protein S19 GENETICS !$#gene HmaS11 FUNCTION !$#pathway protein biosynthesis CLASSIFICATION #superfamily Escherichia coli ribosomal protein S11 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 129 #molecular-weight 13495 #checksum 9323 SEQUENCE /// ENTRY T43939 #type complete TITLE ribosomal protein S11 [similarity] - Halobacterium salinarum ORGANISM #formal_name Halobacterium salinarum DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 21-Jul-2000 ACCESSIONS T43939 REFERENCE Z22729 !$#authors Sano, K.; Taguchi, A.; Furumoto, H.; Uda, T.; Itoh, T. !$#journal Biochem. Biophys. Res. Commun. (1999) 264:24-28 !$#title Cloning, sequencing, and characterization of ribosomal !1protein and RNA polymerase genes from the region analogous !1to the alpha-operon of Escherichia coli in halophilic !1archaea, Halobacterium halobium. !$#cross-references MUID:99458614; PMID:10527834 !$#accession T43939 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-127 ##label SAN !'##cross-references EMBL:AB030282; PIDN:BAA85897.1 !'##note the source is designated as Halobacterium halobium CLASSIFICATION #superfamily Escherichia coli ribosomal protein S11 SUMMARY #length 127 #molecular-weight 13442 #checksum 6701 SEQUENCE /// ENTRY R3HU12 #type complete TITLE ribosomal protein S12, cytosolic - human ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 22-Jun-1999 ACCESSIONS S22989; S68936; S14482 REFERENCE S22989 !$#authors Herault, Y.; Michel, D.; Chatelain, G.; Brun, G. !$#journal Nucleic Acids Res. (1991) 19:4001 !$#title cDNA and predicted amino acid sequences of the human !1ribosomal protein genes rpS12 and rpL17. !$#cross-references MUID:91319568; PMID:1861993 !$#accession S22989 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type mRNA !'##residues 1-132 ##label HER !'##cross-references EMBL:X53505; NID:g36145; PIDN:CAA37582.1; !1PID:g36146 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1990 REFERENCE S68911 !$#authors Vladimirov, S.N.; Ivanov, A.V.; Karpova, G.G.; Musolyamov, !1A.K.; Egorov, T.A.; Thiede, B.; Wittmann-Liebold, B.; Otto, !1A. !$#journal Eur. J. Biochem. (1996) 239:144-149 !$#title Characterization of the human small-ribosomal-subunit !1proteins by N-terminal and internal sequencing, and mass !1spectrometry. !$#cross-references MUID:96305378; PMID:8706699 !$#accession S68936 !'##molecule_type protein !'##residues 24-39 ##label VLA GENETICS !$#gene GDB:RPS12 !'##cross-references GDB:128736 !$#map_position 19q-19q CLASSIFICATION #superfamily rat ribosomal protein S12 KEYWORDS blocked amino end; protein biosynthesis; ribosome SUMMARY #length 132 #molecular-weight 14526 #checksum 1126 SEQUENCE /// ENTRY R3RT12 #type complete TITLE ribosomal protein S12, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 21-Jul-2000 ACCESSIONS S13074; A27426; A33221 REFERENCE S13071 !$#authors Wool, I.G.; Chan, Y.L.; Paz, V.; Olvera, J. !$#journal Biochim. Biophys. Acta (1990) 1050:69-73 !$#title The primary structure of rat ribosomal proteins: the amino !1acid sequences of L27a and L28 and corrections in the !1sequences of S4 and S12. !$#cross-references MUID:91002678; PMID:2207170 !$#accession S13074 !'##molecule_type mRNA !'##residues 1-132 ##label WOO !'##cross-references EMBL:M18547 REFERENCE A27426 !$#authors Lin, A.; Chan, Y.L.; Jones, R.; Wool, I.G. !$#journal J. Biol. Chem. (1987) 262:14343-14351 !$#title The primary structure of rat ribosomal protein S12. The !1relationship of rat S12 to other ribosomal proteins and a !1correlation of the amino acid sequences of rat and yeast !1ribosomal proteins. !$#cross-references MUID:88007693; PMID:3308890 !$#accession A27426 !'##molecule_type mRNA !'##residues 1-130 ##label LIN !'##cross-references EMBL:M18547; NID:g206740; PIDN:AAA42077.1; !1PID:g206741 !'##note this sequence has been revised in reference S13071 !$#accession A33221 !'##molecule_type protein !'##residues 2-130 ##label LIN2 !'##note the protein is designated as ribosomal protein S12 CLASSIFICATION #superfamily rat ribosomal protein S12 KEYWORDS blocked amino end; protein biosynthesis; ribosome FEATURE !$2-130 #product ribosomal protein S12 #status experimental !8#label MAT\ !$2 #modified_site blocked amino end (Ala) (in mature !8form) #status experimental SUMMARY #length 132 #molecular-weight 14525 #checksum 740 SEQUENCE /// ENTRY R3MS12 #type complete TITLE ribosomal protein S12 - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S05492 REFERENCE S05492 !$#authors Ayane, M.; Nielsen, P.; Koehler, G. !$#journal Nucleic Acids Res. (1989) 17:6722 !$#title Cloning and sequencing of mouse ribosomal protein S12 cDNA. !$#cross-references MUID:89385996; PMID:2780296 !$#accession S05492 !'##molecule_type mRNA !'##residues 1-132 ##label AYA !'##cross-references EMBL:X15962; NID:g54005; PIDN:CAA34084.1; !1PID:g54006 CLASSIFICATION #superfamily rat ribosomal protein S12 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 132 #molecular-weight 14525 #checksum 740 SEQUENCE /// ENTRY JC4159 #type complete TITLE ribosomal protein S12 - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JC4159; S57497 REFERENCE JC4159 !$#authors Zach, O.R.F.; Bauer, H.C.; Richter, K.; Webersinke, G.; !1Bauer, H. !$#journal Gene (1995) 159:277-278 !$#title Sequence of the porcine full-length cDNA encoding ribosomal !1protein rpS12. !$#cross-references MUID:95347612; PMID:7622064 !$#accession JC4159 !'##molecule_type mRNA !'##residues 1-132 ##label ZAC !'##cross-references EMBL:X79417; NID:g872314; PIDN:CAA55946.1; !1PID:g872315 !'##experimental_source endothelial cells GENETICS !$#gene rps12 CLASSIFICATION #superfamily rat ribosomal protein S12 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 132 #molecular-weight 14515 #checksum 632 SEQUENCE /// ENTRY S62102 #type complete TITLE ribosomal protein S12.e, cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein O6673; protein YOR369c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S62102; S59734; S67281; S68263; S68265 REFERENCE S62101 !$#authors Siede, W.; Dianova, I.; Nusspaumer, G.; Portillo, V.; !1Rodriguez, R.; Nunes, E.; Friedberg, E.C. !$#submission submitted to the EMBL Data Library, October 1995 !$#description Characterization of RAD17, a gene involved in DNA damage !1checkpoint control in Saccharomyces cerevisiae. !$#accession S62102 !'##molecule_type DNA !'##residues 1-143 ##label SIE !'##cross-references EMBL:U37460; NID:g1051277; PIDN:AAA80546.1; !1PID:g1051279 REFERENCE S59734 !$#authors Teply, R. !$#submission submitted to the EMBL Data Library, August 1993 !$#description Yeast homologue of ribosomal protein S12. !$#accession S59734 !'##molecule_type DNA !'##residues 1-89,'EGLP',93-143 ##label TEP !'##cross-references EMBL:U01049; NID:g899489; PIDN:AAA69926.1; !1PID:g899490 !'##experimental_source strain DBY747 REFERENCE S67261 !$#authors Delius, H.; Hebling, U.; Hofmann, B. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67281 !'##molecule_type DNA !'##residues 1-143 ##label DEL !'##cross-references EMBL:Z75277; NID:g1420797; PIDN:CAA99700.1; !1PID:g1420798; GSPDB:GN00015; MIPS:YOR369c !'##experimental_source strain S288C REFERENCE S68263 !$#authors Moore, J.; Jacobs, H.T.; Kaiser, K. !$#submission submitted to the EMBL Data Library, April 1995 !$#accession S68263 !'##molecule_type mRNA !'##residues 'LQGR',33-48,'R',50,'XYIYSQ',57-69,'XXLSSWLK',77-104,'QD', !1107-126 ##label MOO !'##cross-references EMBL:U24143; NID:g780797; PIDN:AAA65439.1; !1PID:g780798 REFERENCE S68264 !$#authors Siede, W.; Dianova, I.; Nusspaumer, G.; Portillo, V.; !1Rodriguez, R.; Friedberg, E.C. !$#journal Nucleic Acids Res. (1996) 24:1669-1675 !$#title Cloning and characterization of RAD17, a gene controlling !1cell cycle responses to DNA damage in Saccharomyces !1cerevisiae. !$#cross-references MUID:96211370; PMID:8649984 !$#accession S68265 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-143 ##label SIW !'##cross-references EMBL:U37460; NID:g1051277; PIDN:AAA80546.1; !1PID:g1051279 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1995 GENETICS !$#gene SGD:RPS12; MIPS:YOR369c !'##cross-references SGD:S0005896; MIPS:YOR369c !$#map_position 15R CLASSIFICATION #superfamily rat ribosomal protein S12 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 143 #molecular-weight 15472 #checksum 1007 SEQUENCE /// ENTRY S24781 #type complete TITLE ribosomal protein S12.e - Trypanosoma brucei ORGANISM #formal_name Trypanosoma brucei DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A48574; S24781 REFERENCE A48574 !$#authors Marchal, C.; Ismaili, N.; Pays, E. !$#journal Mol. Biochem. Parasitol. (1993) 57:331-334 !$#title A ribosomal S12-like gene of Trypanosoma brucei. !$#cross-references MUID:93165083; PMID:8433721 !$#accession A48574 !'##status preliminary !'##molecule_type mRNA !'##residues 1-144 ##label MAR !'##cross-references EMBL:Z15031; NID:g10531; PIDN:CAA78749.1; !1PID:g10532 !'##note sequence extracted from NCBI backbone (NCBIP:125106) CLASSIFICATION #superfamily rat ribosomal protein S12 SUMMARY #length 144 #molecular-weight 15869 #checksum 3022 SEQUENCE /// ENTRY S41955 #type complete TITLE ribosomal protein S23, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 21-Jul-2000 ACCESSIONS S41955; I52292 REFERENCE S41955 !$#authors Kitaoka, Y.; Wool, I.G. !$#submission submitted to the EMBL Data Library, January 1994 !$#description The primary structure of rat ribosomal protein S23. !$#accession S41955 !'##molecule_type mRNA !'##residues 1-143 ##label KIT !'##cross-references EMBL:X77398; NID:g453280; PIDN:CAA54584.1; !1PID:g453281 REFERENCE I52292 !$#authors Kitaoka, Y.; Olvera, J.; Wool, I.G. !$#journal Biochem. Biophys. Res. Commun. (1994) 202:314-320 !$#title The primary structure of rat ribosomal protein S23. !$#cross-references MUID:94311898; PMID:8037726 !$#accession I52292 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-143 ##label RES !'##cross-references GB:X77398; NID:g453280; PIDN:CAA54584.1; !1PID:g453281 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing !'##note the protein is designated as ribosomal protein S23 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S12 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-143 #product ribosomal protein S23 #status experimental !8#label MAT\ !$114 #modified_site beta-methylthioaspartic acid (Asp) !8#status predicted SUMMARY #length 143 #molecular-weight 15807 #checksum 565 SEQUENCE /// ENTRY R3UC12 #type complete TITLE ribosomal protein S12 - Sulfolobus acidocaldarius ORGANISM #formal_name Sulfolobus acidocaldarius DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S04721 REFERENCE S04714 !$#authors Puehler, G.; Lottspeich, F.; Zillig, W. !$#journal Nucleic Acids Res. (1989) 17:4517-4534 !$#title Organization and nucleotide sequence of the genes encoding !1the large subunits A, B and C of the DNA-dependent RNA !1polymerase of the archaebacterium Sulfolobus acidocaldarius. !$#cross-references MUID:89315197; PMID:2501756 !$#accession S04721 !'##molecule_type DNA !'##residues 1-118 ##label PUE !'##cross-references EMBL:X14818; NID:g46667; PIDN:CAA32929.1; !1PID:g46674 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S12 KEYWORDS protein biosynthesis; ribosome FEATURE !$85 #modified_site beta-methylthioaspartic acid (Asp) !8#status predicted SUMMARY #length 118 #molecular-weight 12665 #checksum 5032 SEQUENCE /// ENTRY R3MX12 #type complete TITLE ribosomal protein S12 - Methanococcus vannielii ORGANISM #formal_name Methanococcus vannielii DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 22-Jun-1999 ACCESSIONS S06623 REFERENCE S06620 !$#authors Lechner, K.; Heller, G.; Boeck, A. !$#journal J. Mol. Evol. (1989) 29:20-27 !$#title Organization and nucleotide sequence of a transcriptional !1unit of Methanococcus vannielii comprising genes for protein !1synthesis elongation factors and ribosomal proteins. !$#cross-references MUID:89362493; PMID:2475640 !$#accession S06623 !'##molecule_type DNA !'##residues 1-147 ##label LEC !'##cross-references EMBL:X15970; NID:g44780; PIDN:CAA34089.1; !1PID:g44784 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S12 KEYWORDS protein biosynthesis; ribosome FEATURE !$118 #modified_site beta-methylthioaspartic acid (Asp) !8#status predicted SUMMARY #length 147 #molecular-weight 16108 #checksum 3421 SEQUENCE /// ENTRY S03581 #type complete TITLE ribosomal protein S12 [similarity] - Halobacterium salinarum ORGANISM #formal_name Halobacterium salinarum DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 21-Jul-2000 ACCESSIONS S03581 REFERENCE S03572 !$#authors Leffers, H.; Gropp, F.; Lottspeich, F.; Zillig, W.; Garrett, !1R.A. !$#journal J. Mol. Biol. (1989) 206:1-17 !$#title Sequence, organization, transcription and evolution of RNA !1polymerase subunit genes from the archaebacterial extreme !1halophiles Halobacterium halobium and Halococcus morrhuae. !$#cross-references MUID:89199633; PMID:2495365 !$#accession S03581 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-142 ##label LEF !'##cross-references GB:X57144; GB:X14999; NID:g43538; PIDN:CAA40429.1; !1PID:g43545 !'##note the source is designated as Halobacterium halobium CLASSIFICATION #superfamily Escherichia coli ribosomal protein S12 KEYWORDS protein biosynthesis; ribosome FEATURE !$113 #modified_site beta-methylthioaspartic acid (Asp) !8#status predicted SUMMARY #length 142 #molecular-weight 15489 #checksum 6813 SEQUENCE /// ENTRY R3TW12 #type complete TITLE ribosomal protein S12 - Thermus aquaticus ORGANISM #formal_name Thermus aquaticus DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 21-Jan-2000 ACCESSIONS S10249; S51063; F48401 REFERENCE S10249 !$#authors Yakhnin, A.V.; Vorozheykina, D.P.; Matvienko, N.I. !$#journal Nucleic Acids Res. (1990) 18:3659 !$#title Nucleotide sequence of the Thermus thermophilus HB8 rps12 !1and rps7 genes coding for the ribosomal proteins S12 and S7. !$#cross-references MUID:90301504; PMID:2362824 !$#accession S10249 !'##molecule_type DNA !'##residues 1-135 ##label YAK !'##cross-references EMBL:X52165; NID:g48273; PIDN:CAA36418.1; !1PID:g581812 !'##experimental_source strain HB8 !'##note the source is designated as Thermus thermophilus REFERENCE S51053 !$#authors Tsiboli, P.; Herfurth, E.; Choli, T. !$#journal Eur. J. Biochem. (1994) 226:169-177 !$#title Purification and characterization of the 30S ribosomal !1proteins from the bacterium Thermus thermophilus. !$#cross-references MUID:95045586; PMID:7957245 !$#accession S51063 !'##molecule_type protein !'##residues 5-32 ##label TSI !'##note the source is given as Thermus thermophilus REFERENCE A48401 !$#authors Garber, M.B.; Agalarov, S.C.; Eliseikina, I.A.; Fomenkova, !1N.P.; Nikonov, S.V.; Sedelnikova, S.E.; Shikaeva, O.S.; !1Vasiliev, D.; Zhdanov, A.S.; Liljas, A.; Svensson, L.A. !$#journal Biochimie (1992) 74:327-336 !$#title Ribosomal proteins from Thermus thermophilus for structural !1investigations. !$#cross-references MUID:92345325; PMID:1637860 !$#accession F48401 !'##molecule_type protein !'##residues 'V',6-11 ##label GAR !'##note the source is given as Thermus thermophilus GENETICS !$#start_codon GTG CLASSIFICATION #superfamily Escherichia coli ribosomal protein S12 KEYWORDS protein biosynthesis; ribosome FEATURE !$5-135 #product ribosomal protein S12 #status predicted !8#label MAT\ !$92 #modified_site beta-methylthioaspartic acid (Asp) !8#status predicted SUMMARY #length 135 #molecular-weight 14883 #checksum 2780 SEQUENCE /// ENTRY R3EC12 #type complete TITLE ribosomal protein S12 [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 24-Apr-1984 #sequence_revision 30-Jun-1991 #text_change 01-Mar-2002 ACCESSIONS S13738; A02727; JH0808; A65128 REFERENCE S13738 !$#authors Post, L.E.; Nomura, M. !$#journal J. Biol. Chem. (1980) 255:4660-4666 !$#title DNA sequences from the str operon of Escherichia coli. !$#cross-references MUID:80182129; PMID:6989816 !$#accession S13738 !'##molecule_type DNA !'##residues 1-124 ##label POS !'##cross-references EMBL:V00355; NID:g43009; PIDN:CAA23648.1; !1PID:g43010 REFERENCE A02727 !$#authors Funatsu, G.; Yaguchi, M.; Wittmann-Liebold, B. !$#journal FEBS Lett. (1977) 73:12-17 !$#title Primary structure of protein S12 from the small Escherichia !1coli ribosomal subunit. !$#cross-references MUID:77116119; PMID:320034 !$#accession A02727 !'##molecule_type protein !'##residues 2-124 ##label FUN !'##experimental_source strain K REFERENCE JH0807 !$#authors Toba-Minowa, M.; Hashimoto-Gotoh, T. !$#journal Gene (1992) 121:25-33 !$#title Characterization of the spontaneous elimination of !1streptomycin sensitivity (Sm-s) on high-copy-number !1plasmids: Sm-s-enforcement cloning vectors with a synthetic !1rpsL gene. !$#cross-references MUID:93051359; PMID:1427096 !$#accession JH0808 !'##molecule_type DNA !'##residues 1-124 ##label TOB !'##experimental_source plamid vector pHSG664 !'##note the authors translated the codon GTA for residue 33 as Ile, GTA !1for residue 52 as Leu, GTT for residue 93 as Ile, AAG for !1residue 111 as Arg and GCT for residue 113 as Asp REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65128 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-124 ##label BLAT !'##cross-references GB:AE000410; GB:U00096; NID:g1789734; !1PIDN:AAC76367.1; PID:g1789740; UWGP:b3342 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A57989 !$#authors Kowalak, J.A.; Walsh, K.A. !$#journal Protein Sci. (1996) 5:1625-1632 !$#title beta-Methylthio-aspartic acid: Identification of a novel !1posttranslational modification in ribosomal protein S12 from !1Escherichia coli. !$#cross-references MUID:97001859; PMID:8844851 !$#contents annotation; identification of beta-methylthioaspartic acid REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note mass spectrographic analysis of post-translational !1modifications; any acid labile modifications may have been !1missed GENETICS !$#gene rpsL; strA !$#map_position 73 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX small subunit ribosomal proteins: S1 (PIR:R3EC1), S2 !1(PIR:R3EC2), S3 (PIR:R3EC3), S4 (PIR:R3EC4), S5 (PIR:R3EC5), !1S6 (PIR:R3EC6), S7 (PIR:R3EC7K), S8 (PIR:R3EC8), S9 !1(PIR:R3EC9), S10 (PIR:R3EC10), S11 (PIR:R3EC11), S12 !1(PIR:R3EC12), S13 (PIR:R3EC13), S14 (PIR:R3EC14), S15 !1(PIR:R3EC15), S16 (PIR:R3EC16), S17 (PIR:R3EC17), S18 !1(PIR:R3EC18), S19 (PIR:R3EC19), S20/L26 (PIR:R3EC20), S21 !1(PIR:R3EC21), S22 (PIR:C64901) [validated, MUID:99196679] FUNCTION !$#pathway protein biosynthesis CLASSIFICATION #superfamily Escherichia coli ribosomal protein S12 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-124 #product ribosomal protein S12 #status experimental !8#label MAT\ !$89 #modified_site beta-methylthioaspartic acid (Asp) !8#status experimental SUMMARY #length 124 #molecular-weight 13737 #checksum 253 SEQUENCE /// ENTRY R3EG12 #type complete TITLE ribosomal protein S12, chloroplast - Euglena gracilis chloroplast ORGANISM #formal_name chloroplast Euglena gracilis DATE 17-May-1985 #sequence_revision 31-Mar-1992 #text_change 24-Sep-1999 ACCESSIONS A02728; S34510; S34877; S02252 REFERENCE A93511 !$#authors Montandon, P.E.; Stutz, E. !$#journal Nucleic Acids Res. (1984) 12:2851-2859 !$#title The genes for the ribosomal proteins S12 and S7 are !1clustered with the gene for the EF-Tu protein on the !1chloroplast genome of Euglena gracilis. !$#cross-references MUID:84169577; PMID:6324129 !$#accession A02728 !'##molecule_type DNA !'##residues 1-125 ##label MON !'##cross-references GB:Z11874; GB:S55425; NID:g14353; PIDN:CAA77906.1; !1PID:g14356 !'##experimental_source strain Z REFERENCE S34494 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.; Monfort, !1A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#submission submitted to the EMBL Data Library, January 1993 !$#description The complete sequence of the Euglena gracilis chloroplast !1genome (tentative). !$#accession S34510 !'##molecule_type DNA !'##residues 1-125 ##label HAL1 !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50089.1; !1PID:g415745 REFERENCE S34862 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.R.; !1Monfort, A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#journal Nucleic Acids Res. (1993) 21:3537-3544 !$#title Complete sequence of Euglena gracilis chloroplast DNA. !$#cross-references MUID:93347989; PMID:8346031 !$#accession S34877 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-125 ##label HAL2 !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50089.1; !1PID:g415745 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1993 COMMENT Protein S12 is involved in the translation initiation step. GENETICS !$#gene rps12 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein S12 KEYWORDS chloroplast; protein biosynthesis; ribosome FEATURE !$43,88 #binding_site streptomycin (Lys) #status predicted\ !$89 #modified_site beta-methylthioaspartic acid (Asp) !8#status predicted SUMMARY #length 125 #molecular-weight 13976 #checksum 1186 SEQUENCE /// ENTRY R3BS12 #type complete TITLE ribosomal protein S12 - Bacillus stearothermophilus ORGANISM #formal_name Bacillus stearothermophilus DATE 30-Sep-1991 #sequence_revision 31-Dec-1992 #text_change 07-May-1999 ACCESSIONS JG0007; A29103; B29103 REFERENCE JG0007 !$#authors Kimura, M. !$#journal Agric. Biol. Chem. (1991) 55:207-213 !$#title The nucleotide sequences of Bacillus stearothermophilus !1ribosomal protein S12 and S7 genes: comparison with the str !1operon of Escherichia coli. !$#cross-references MUID:91248486; PMID:1368664 !$#accession JG0007 !'##molecule_type DNA !'##residues 1-140 ##label KIM1 REFERENCE A29103 !$#authors Kimura, M.; Kimura, J. !$#journal FEBS Lett. (1987) 210:91-96 !$#title The complete amino acid sequence of ribosomal protein S12 !1from Bacillus stearothermophilus. !$#cross-references MUID:87105937; PMID:3542563 !$#accession A29103 !'##molecule_type protein !'##residues 2-103,'P',105-113,'A',115-139 ##label KIM2 !$#accession B29103 !'##molecule_type DNA !'##residues 1-79 ##label KIM3 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S12 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-140 #product ribosomal protein S12 #status experimental !8#label MAT\ !$102 #modified_site beta-methylthioaspartic acid (Asp) !8#status predicted SUMMARY #length 140 #molecular-weight 15510 #checksum 2482 SEQUENCE /// ENTRY R3SG12 #type complete TITLE ribosomal protein S12 - Spirulina platensis ORGANISM #formal_name Spirulina platensis DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S04388 REFERENCE S04388 !$#authors Buttarelli, F.R.; Calogero, R.A.; Tiboni, O.; Gualerzi, !1C.O.; Pon, C.L. !$#journal Mol. Gen. Genet. (1989) 217:97-104 !$#title Characterization of the str operon genes from Spirulina !1platensis and their evolutionary relationship to those of !1other prokaryotes. !$#cross-references MUID:89364697; PMID:2505055 !$#accession S04388 !'##molecule_type DNA !'##residues 1-124 ##label BUT !'##cross-references EMBL:X15646; NID:g47447; PIDN:CAA33670.1; !1PID:g47448 GENETICS !$#gene rpsL CLASSIFICATION #superfamily Escherichia coli ribosomal protein S12 KEYWORDS protein biosynthesis; ribosome FEATURE !$89 #modified_site beta-methylthioaspartic acid (Asp) !8#status predicted SUMMARY #length 124 #molecular-weight 13836 #checksum 1228 SEQUENCE /// ENTRY R3KT12 #type complete TITLE ribosomal protein S12, cyanelle - Cyanophora paradoxa cyanelle ORGANISM #formal_name cyanelle Cyanophora paradoxa DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 21-Jan-2000 ACCESSIONS S14713; T06897; S10461 REFERENCE S14713 !$#authors Kraus, M.; Goetz, M.; Loeffelhardt, W. !$#journal Plant Mol. Biol. (1990) 15:561-573 !$#title The cyanelle str operon from Cyanophora paradoxa: sequence !1analysis and phylogenetic implications. !$#cross-references MUID:91338695; PMID:2129337 !$#accession S14713 !'##molecule_type DNA !'##residues 1-124 ##label KRA !'##cross-references EMBL:X52497; NID:g11413; PIDN:CAA36738.1; !1PID:g11414 !'##experimental_source strain LB555 UTEX REFERENCE Z15840 !$#authors Stirewalt, V.L.; Michalowski, C.B.; Luffelhardt, W.; !1Bohnert, H.J.; Bryant, D.A. !$#submission submitted to the EMBL Data Library, July 1995 !$#description Nucleotide sequence of the cyanelle genome from Cyanophora !1paradoxa. !$#accession T06897 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-124 ##label STI !'##cross-references EMBL:U30821; NID:g1016083; PIDN:AAA81240.1; !1PID:g1016153 !'##experimental_source strain Pringsheim LB555 GENETICS !$#gene rps12 !$#genome cyanelle CLASSIFICATION #superfamily Escherichia coli ribosomal protein S12 KEYWORDS cyanelle; protein biosynthesis; ribosome FEATURE !$89 #modified_site beta-methylthioaspartic acid (Asp) !8#status predicted SUMMARY #length 124 #molecular-weight 13813 #checksum 858 SEQUENCE /// ENTRY R3LV12 #type complete TITLE ribosomal protein S12, chloroplast - liverwort (Marchantia polymorpha) chloroplast ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 22-Jun-1999 ACCESSIONS A02729; S01546; S01567 REFERENCE A00150 !$#authors Ohyama, K. !$#submission submitted to the EMBL Data Library, October 1986 !$#accession A02729 !'##molecule_type DNA !'##residues 1-123 ##label OHY REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features REFERENCE S01529 !$#authors Fukuzawa, H.; Kohchi, T.; Sano, T.; Shirai, H.; Umesono, K.; !1Inokuchi, H.; Ozeki, H.; Ohyama, K. !$#journal J. Mol. Biol. (1988) 203:333-351 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. III. Gene organization of the large !1single copy region from rbcL to trnI(CAU). !$#cross-references MUID:89068687; PMID:3199436 !$#accession S01546 !'##molecule_type DNA !'##residues 1-38 ##label FUK REFERENCE S01567 !$#authors Umesono, K.; Inokuchi, H.; Shiki, Y.; Takeuchi, M.; Chang, !1Z.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Ohyama, K.; Ozeki, !1H. !$#journal J. Mol. Biol. (1988) 203:299-331 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. II. Gene organization of the large !1single copy region from rps'12 to atpB. !$#cross-references MUID:89068686; PMID:2974085 !$#accession S01567 !'##molecule_type DNA !'##residues 39-123 ##label UME !'##cross-references GB:X04465; GB:Y00686; NID:g11640; PIDN:CAA28056.1; !1PID:g453588 GENETICS !$#gene rps12 !$#genome chloroplast !$#introns 38/3; 116/1 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S12 KEYWORDS chloroplast; protein biosynthesis; ribosome FEATURE !$89 #modified_site beta-methylthioaspartic acid (Asp) !8#status predicted SUMMARY #length 123 #molecular-weight 13797 #checksum 433 SEQUENCE /// ENTRY R3NT12 #type complete TITLE ribosomal protein S12 - common tobacco chloroplast ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 23-Aug-1996 ACCESSIONS A02730 REFERENCE A00149 !$#authors Sugiura, M. !$#submission submitted to the EMBL Data Library, August 1986 !$#accession A02730 !'##molecule_type DNA !'##residues 1-122 ##label SUG !'##experimental_source cv. Bright Yellow 4 REFERENCE A38013 !$#authors Shinozaki, K.; Ohme, M.; Tanaka, M.; Wakasugi, T.; !1Hayashida, N.; Matsubayashi, T.; Zaita, N.; Chunwongse, J.; !1Obokata, J.; Yamaguchi-Shinozaki, K.; Ohto, C.; Torazawa, !1K.; Meng, B.Y.; Sugita, M.; Deno, H.; Kamogashira, T.; !1Yamada, K.; Kusuda, J.; Takaiwa, F.; Kato, A.; Tohdoh, N.; !1Shimada, H.; Sugiura, M. !$#journal EMBO J. (1986) 5:2043-2049 !$#title The complete nucleotide sequence of the tobacco chloroplast !1genome: its gene organization and expression. !$#contents annotation; gene organization, sites, features GENETICS !$#gene rps12 !$#genome chloroplast !$#introns 37/3; 115/1 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S12 KEYWORDS chloroplast; protein biosynthesis; ribosome FEATURE !$88 #modified_site beta-methylthioaspartic acid (Asp) !8#status predicted SUMMARY #length 122 #molecular-weight 13601 #checksum 1177 SEQUENCE /// ENTRY R3RZ12 #type complete TITLE ribosomal protein S12 - rice chloroplast ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jun-2000 ACCESSIONS JQ0250; S05130 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0250 !'##molecule_type DNA !'##residues 1-124 ##label SHI !'##experimental_source cv. Nihonbare !'##note the gene encoding this protein is divided. Exon-1 is located at !1large single copy region (LSC) and both exon-1 and exon-2 !1are located at inverted region A and B (IRA and IRB) REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05130 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-124 ##label HIR !'##cross-references GB:X15901; NID:g11957; PIDN:CAA33929.1; !1PID:g1213603 !'##experimental_source cv. Nihonbare !'##note this sequence was submitted to EMBL, July 1989 GENETICS !$#gene rps12 !$#genome chloroplast !$#introns 38/3; 116/1 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S12 KEYWORDS chloroplast; protein biosynthesis; ribosome FEATURE !$89 #modified_site beta-methylthioaspartic acid (Asp) !8#status predicted SUMMARY #length 124 #molecular-weight 13820 #checksum 9644 SEQUENCE /// ENTRY R3WT12 #type complete TITLE ribosomal protein S12 - wheat mitochondrion ORGANISM #formal_name mitochondrion Triticum aestivum #common_name common wheat DATE 31-Mar-1991 #sequence_revision 16-Aug-1996 #text_change 22-Jun-1999 ACCESSIONS JQ1375; S03610 REFERENCE JQ1374 !$#authors Gualberto, J.M.; Bonnard, G.; Lamattina, L.; Grienenberger, !1J.M. !$#journal Plant Cell (1991) 3:1109-1120 !$#title Expression of the wheat mitochondrial nad3-rps12 !1transcription unit: correlation between editing and mRNA !1maturation. !$#cross-references MUID:92338836; PMID:1726558 !$#accession JQ1375 !'##molecule_type mRNA !'##residues 1-125 ##label GUA !'##cross-references EMBL:X59153; NID:g433681; PIDN:CAA41865.1; !1PID:g433683 !'##note in plant mitochondria, RNA editing converts C in codons 24, 66, !174, 90, 95, and 97 from the genomic DNA into U in the RNA !'##note this sequence is the translation of the consensus sequence of !1three cDNA clones REFERENCE S03609 !$#authors Gualberto, J.M.; Wintz, H.; Weil, J.H.; Grienenberger, J.M. !$#journal Mol. Gen. Genet. (1988) 215:118-127 !$#title The genes coding for subunit 3 of NADH dehydrogenase and for !1ribosomal protein S12 are present in the wheat and maize !1mitochondrial genomes and are co-transcribed. !$#cross-references MUID:89201232; PMID:2853827 !$#accession S03610 !'##molecule_type DNA !'##residues 1-23,'S',25-65,'H',67-73,'S',75-89,'S',91-94,'S',96,'R', !198-125 ##label GU2 !'##cross-references EMBL:X14262; NID:g13703; PIDN:CAA32476.1; !1PID:g13705 GENETICS !$#gene rps12 !$#genome mitochondrion CLASSIFICATION #superfamily Escherichia coli ribosomal protein S12 KEYWORDS mitochondrion; protein biosynthesis; ribosome; RNA editing FEATURE !$89 #modified_site beta-methylthioaspartic acid (Asp) !8#status predicted SUMMARY #length 125 #molecular-weight 14309 #checksum 8449 SEQUENCE /// ENTRY R3ZM12 #type complete TITLE ribosomal protein S12 - maize mitochondrion ORGANISM #formal_name mitochondrion Zea mays #common_name maize DATE 31-Mar-1991 #sequence_revision 30-Jun-1992 #text_change 22-Jun-1999 ACCESSIONS S05953 REFERENCE S03609 !$#authors Gualberto, J.M.; Wintz, H.; Weil, J.H.; Grienenberger, J.M. !$#journal Mol. Gen. Genet. (1988) 215:118-127 !$#title The genes coding for subunit 3 of NADH dehydrogenase and for !1ribosomal protein S12 are present in the wheat and maize !1mitochondrial genomes and are co-transcribed. !$#cross-references MUID:89201232; PMID:2853827 !$#accession S05953 !'##molecule_type DNA !'##residues 1-125 ##label GUA !'##cross-references EMBL:X14709; NID:g13913; PIDN:CAA32834.1; !1PID:g13915 GENETICS !$#gene rps12 !$#genome mitochondrion CLASSIFICATION #superfamily Escherichia coli ribosomal protein S12 KEYWORDS mitochondrion; protein biosynthesis; ribosome FEATURE !$89 #modified_site beta-methylthioaspartic acid (Asp) !8#status predicted SUMMARY #length 125 #molecular-weight 14197 #checksum 9908 SEQUENCE /// ENTRY R3PP12 #type complete TITLE ribosomal protein S12 - Paramecium tetraurelia mitochondrion ORGANISM #formal_name mitochondrion Paramecium tetraurelia DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 07-Dec-1999 ACCESSIONS JS0234; S07735 REFERENCE JS0231 !$#authors Pritchard, A.E.; Venuti, S.E.; Ghalambor, M.A.; Sable, C.L.; !1Cummings, D.J. !$#journal Gene (1989) 78:121-134 !$#title An unusual region of Paramecium mitochondrial DNA containing !1chloroplast-like genes. !$#cross-references MUID:89357489; PMID:2670676 !$#accession JS0234 !'##molecule_type DNA !'##residues 1-139 ##label PRI !'##cross-references GB:M26930; NID:g341550; PIDN:AAA79256.1; !1PID:g1019631 !'##experimental_source strain sp. 4.51 !'##note the source is designated as Paramecium aurelia species 4 stock !151, now designated Paramecium tetraurelia, ATCC 30567 REFERENCE S07725 !$#authors Pritchard, A.E.; Seilhamer, J.J.; Mahalingam, R.; Sable, !1C.L.; Venuti, S.E.; Cummings, D.J. !$#journal Nucleic Acids Res. (1990) 18:173-180 !$#title Nucleotide sequence of the mitochondrial genome of !1Paramecium. !$#cross-references MUID:90174913; PMID:2308823 !$#accession S07735 !'##status translation not shown !'##molecule_type DNA !'##residues 1-139 ##label PRI2 !'##cross-references EMBL:X15917; NID:g13256; PIDN:CAA34044.1; !1PID:g578752 GENETICS !$#gene rps12 !$#genome mitochondrion !$#genetic_code SGC6 !$#start_codon ATT CLASSIFICATION #superfamily Escherichia coli ribosomal protein S12 KEYWORDS mitochondrion; protein biosynthesis; ribosome FEATURE !$89 #modified_site beta-methylthioaspartic acid (Asp) !8#status predicted SUMMARY #length 139 #molecular-weight 15805 #checksum 8834 SEQUENCE /// ENTRY S30393 #type complete TITLE ribosomal protein S18, cytosolic - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S30393; S68935 REFERENCE S30393 !$#authors Chassin, D.; Bellet, D.; Koman, A. !$#journal Nucleic Acids Res. (1993) 21:745 !$#title The human homolog of ribosomal protein S18. !$#cross-references MUID:93181276; PMID:8441687 !$#accession S30393 !'##molecule_type mRNA !'##residues 1-152 ##label CHA !'##cross-references EMBL:X69150; NID:g38422; PIDN:CAB56794.1; !1PID:g6006558 REFERENCE S68911 !$#authors Vladimirov, S.N.; Ivanov, A.V.; Karpova, G.G.; Musolyamov, !1A.K.; Egorov, T.A.; Thiede, B.; Wittmann-Liebold, B.; Otto, !1A. !$#journal Eur. J. Biochem. (1996) 239:144-149 !$#title Characterization of the human small-ribosomal-subunit !1proteins by N-terminal and internal sequencing, and mass !1spectrometry. !$#cross-references MUID:96305378; PMID:8706699 !$#accession S68935 !'##molecule_type protein !'##residues 'S',56-57,'X',59-64,'XX',67-69 ##label VLA GENETICS !$#gene GDB:RPS18 !'##cross-references GDB:138447; OMIM:180473 !$#map_position 6p21.3-6p21.3 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S13 KEYWORDS blocked amino end; protein biosynthesis; ribosome SUMMARY #length 152 #molecular-weight 17719 #checksum 8844 SEQUENCE /// ENTRY S37496 #type complete TITLE ribosomal protein S18.A, cytosolic - Arabidopsis thaliana ALTERNATE_NAMES protein F17A8.150; protein T22J18.5 ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S46223; S39263; S39265; S39264; T00766; T04028; S37496 REFERENCE S46223 !$#authors van Lijsebettens, M.; Vanderhaeghen, R.; de Block, M.; Bauw, !1G.; Villarroel, R.; van Montagu, M. !$#journal EMBO J. (1994) 13:3378-3388 !$#title An S18 ribosomal protein gene copy at the Arabidopsis PFL !1locus affects plant development by its specific expression !1in meristems. !$#cross-references MUID:94320602; PMID:7913892 !$#accession S46223 !'##molecule_type DNA !'##residues 1-152 ##label VAN !'##cross-references EMBL:Z23165; NID:g405612; PIDN:CAA80684.1; !1PID:g405613 REFERENCE S39263 !$#authors Vanderhaeghen, R.; Villaroel, R.; de Block, M.; Bauw, G.; !1van Montagu, M.; van Lijsebettens, M. !$#submission submitted to the EMBL Data Library, December 1993 !$#description An Arabidopsis S18 ribosomal protein gene copy, encoded by !1the PFL locus, affects plant growth and morphology by its !1specific expression in meristems. !$#accession S39263 !'##molecule_type mRNA !'##residues 1-152 ##label VAW !'##cross-references EMBL:Z28701; NID:g434342; PIDN:CAA82273.1; !1PID:g434343 !$#accession S39265 !'##molecule_type DNA !'##residues 1-152 ##label VAA !'##cross-references EMBL:Z28962; NID:g434905; PIDN:CAA82275.1; !1PID:g434906 !$#accession S39264 !'##molecule_type mRNA !'##residues 1-152 ##label VAF !'##cross-references EMBL:Z28702; NID:g434344; PIDN:CAA82274.1; !1PID:g434345 REFERENCE Z14202 !$#authors Vysotskaia, V.S.; Schwartz, J.R.; Toriumi, M.; Yu, G.; Oji, !1O.; Kwan, A.; Liu, S.; Li, J.; Araujo, R.; Au, M.; Brendel, !1V.; Buehler, E.; Conway, A.B.; Conway, A.R.; Dewar, K.; !1Feng, J.; Kim, C.; Kurtz, D.; Li, Y.; Palm, C.J.; Shinn, P.; !1Sun, H.; Davis, R.W.; Ecker, J.R.; Federspiel, N.A.; !1Theologis, A. !$#submission submitted to the EMBL Data Library, July 1998 !$#description Arabidopsis thaliana chromosome 1 BAC T22J18 sequence, !1complete sequence. !$#accession T00766 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-152 ##label VYS !'##cross-references EMBL:AC003979; NID:g3172156; PIDN:AAC25506.1; !1PID:g3287678 !'##genetics CH1 REFERENCE Z15184 !$#authors Bevan, M.; Murphy, G.; Ridley, P.; Hudson, S.; Bancroft, I.; !1Mewes, H.W.; Mayer, K.F.X.; Schueller, C. !$#submission submitted to the Protein Sequence Database, March 1999 !$#accession T04028 !'##molecule_type DNA !'##residues 1-152 ##label BEV !'##cross-references EMBL:AL049482 !'##experimental_source cultivar Columbia; BAC clone F17A8 !'##genetics CH4 GENETICS CH1 !$#map_position 1 !$#introns 1/3; 55/2; 118/2 !$#note T22J18.5 GENETICS CH4 !$#map_position 4 !$#introns 1/3; 55/2; 118/2 !$#note F17A8.150 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S13 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 152 #molecular-weight 17545 #checksum 8724 SEQUENCE /// ENTRY S51145 #type complete TITLE ribosomal protein S18.e, cytosolic - Chlamydomonas reinhardtii ORGANISM #formal_name Chlamydomonas reinhardtii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S51145 REFERENCE S51145 !$#authors Kueck, U.; Hahn, D. !$#submission submitted to the EMBL Data Library, January 1995 !$#accession S51145 !'##molecule_type mRNA !'##residues 1-153 ##label KUE !'##cross-references EMBL:X83693; NID:g624956; PIDN:CAA58668.1; !1PID:g624957 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S13 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 153 #molecular-weight 17437 #checksum 1410 SEQUENCE /// ENTRY S50886 #type complete TITLE ribosomal protein S18.e, cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YDR450w; protein YML026c; ribosomal protein S18.e.A; ribosomal protein S18.e.B ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S50886; S33677; S69729 REFERENCE S49741 !$#authors Badcock, K.; Churcher, C. !$#submission submitted to the EMBL Data Library, November 1994 !$#accession S50886 !'##molecule_type DNA !'##residues 1-146 ##label BAD !'##cross-references EMBL:Z46659; GSPDB:GN00013; MIPS:YML026c; !1NID:g575680; PIDN:CAA86629.1; PID:g575693 !'##genetics CH13 REFERENCE S33388 !$#authors Kaufmann, E. !$#journal Chromosoma (1993) 102:174-179 !$#title In vitro binding to the leucine tRNA gene identifies a novel !1yeast homeobox gene. !$#cross-references MUID:93209080; PMID:8096171 !$#accession S33677 !'##molecule_type DNA !'##residues 'EFG',30-146 ##label KAU !'##cross-references EMBL:X62392 REFERENCE S69555 !$#authors Dietrich, F.S. !$#submission submitted to the EMBL Data Library, August 1995 !$#description The sequence of S. cerevisiae lambda 3641 and cosmids 9461, !19831, and 9410. !$#accession S69729 !'##molecule_type DNA !'##residues 1-146 ##label DIE !'##cross-references EMBL:U33007; GSPDB:GN00004; MIPS:YDR450w; !1NID:g927685; PIDN:AAB64891.1; PID:g927725 !'##genetics CH4 GENETICS CH13 !$#gene RPS18EB; MIPS:YML026c !'##cross-references MIPS:YML026c !$#map_position 13L !$#introns 16/2 GENETICS CH4 !$#gene SGD:RPS18B; RPS18EA; MIPS:YDR450w !'##cross-references SGD:S0004488; SGD:S0002858; MIPS:YDR450w !$#map_position 4R !$#introns 16/2 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S13 KEYWORDS cytosol; protein biosynthesis; ribosome SUMMARY #length 146 #molecular-weight 17037 #checksum 3602 SEQUENCE /// ENTRY R3RT18 #type complete TITLE ribosomal protein S18, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 21-Jul-2000 ACCESSIONS JH0419 REFERENCE JH0419 !$#authors Chan, Y.L.; Paz, V.; Wool, I.G. !$#journal Biochem. Biophys. Res. Commun. (1991) 178:1212-1218 !$#title The primary structure of rat ribosomal protein S18. !$#cross-references MUID:91337062; PMID:1872840 !$#accession JH0419 !'##molecule_type mRNA !'##residues 1-152 ##label CHA !'##cross-references GB:X57529; NID:g433446; PIDN:CAA40750.1; !1PID:g433447 !'##note the protein is designated as ribosomal protein S18 according to !1comigration analysis after in vitro translation CLASSIFICATION #superfamily Escherichia coli ribosomal protein S13 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 152 #molecular-weight 17719 #checksum 8844 SEQUENCE /// ENTRY A44126 #type complete TITLE ribosomal protein S13 [similarity] - Haloarcula marismortui ORGANISM #formal_name Haloarcula marismortui DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A44126 REFERENCE A44126 !$#authors Scholzen, T.; Arndt, E. !$#journal J. Biol. Chem. (1992) 267:12123-12130 !$#title The alpha-operon equivalent genome region in the extreme !1halophilic archaebacterium Haloarcula (Halobacterium) !1marismortui. !$#cross-references MUID:92291093; PMID:1376318 !$#accession A44126 !'##status preliminary !'##molecule_type DNA !'##residues 1-177 ##label SCH !'##cross-references GB:M87833; NID:g148769; PIDN:AAA73209.1; !1PID:g148770 !'##note sequence extracted from NCBI backbone (NCBIN:106619, !1NCBIP:106620) CLASSIFICATION #superfamily Escherichia coli ribosomal protein S13 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 177 #molecular-weight 20050 #checksum 5151 SEQUENCE /// ENTRY T43937 #type complete TITLE ribosomal protein S13 [similarity] - Halobacterium salinarum ORGANISM #formal_name Halobacterium salinarum DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 21-Jul-2000 ACCESSIONS T43937 REFERENCE Z22729 !$#authors Sano, K.; Taguchi, A.; Furumoto, H.; Uda, T.; Itoh, T. !$#journal Biochem. Biophys. Res. Commun. (1999) 264:24-28 !$#title Cloning, sequencing, and characterization of ribosomal !1protein and RNA polymerase genes from the region analogous !1to the alpha-operon of Escherichia coli in halophilic !1archaea, Halobacterium halobium. !$#cross-references MUID:99458614; PMID:10527834 !$#accession T43937 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-171 ##label SAN !'##cross-references EMBL:AB030282; PIDN:BAA85895.1 !'##note the source is designated as Halobacterium halobium CLASSIFICATION #superfamily Escherichia coli ribosomal protein S13 SUMMARY #length 171 #molecular-weight 18917 #checksum 1619 SEQUENCE /// ENTRY S47020 #type complete TITLE ribosomal protein S13 - Sulfolobus acidocaldarius ORGANISM #formal_name Sulfolobus acidocaldarius DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 23-Mar-2001 ACCESSIONS S47020 REFERENCE S47020 !$#authors Langer, D.; Hain, J.; Thuriaux, P.; Zillig, W. !$#submission submitted to the EMBL Data Library, July 1994 !$#description Similarity of the transcription systems of Eukarya and !1Archaea. !$#accession S47020 !'##molecule_type DNA !'##residues 1-184 ##label LAN !'##cross-references EMBL:X80194; NID:g517286; PIDN:CAA56477.1; !1PID:g517287 GENETICS !$#gene rps13 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S13 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 184 #molecular-weight 21134 #checksum 5639 SEQUENCE /// ENTRY R3EC13 #type complete TITLE ribosomal protein S13 [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 24-Apr-1984 #sequence_revision 30-Jun-1991 #text_change 01-Mar-2002 ACCESSIONS A23807; A02731; E65122 REFERENCE A23807 !$#authors Bedwell, D.; Davis, G.; Gosink, M.; Post, L.; Nomura, M.; !1Kestler, H.; Zengel, J.M.; Lindahl, L. !$#journal Nucleic Acids Res. (1985) 13:3891-3903 !$#title Nucleotide sequence of the alpha ribosomal protein operon of !1Escherichia coli. !$#cross-references MUID:85242076; PMID:2989779 !$#accession A23807 !'##molecule_type DNA !'##residues 1-118 ##label BED !'##cross-references GB:X02543; NID:g42795; PIDN:CAA26392.1; PID:g581217 !'##note the authors translated the initiation codon GTG for residue 1 !1as Val REFERENCE A02731 !$#authors Lindemann, H.; Wittmann-Liebold, B. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1977) 358:843-863 !$#title Primary structure of protein S13 from the small subunit of !1Escherichia coli ribosomes. !$#cross-references MUID:77248097; PMID:330375 !$#accession A02731 !'##molecule_type protein !'##residues 2-118 ##label LIN !'##experimental_source strain K REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65122 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-118 ##label BLAT !'##cross-references GB:AE000407; GB:U00096; NID:g2367211; !1PIDN:AAC76323.1; PID:g1789693; UWGP:b3298 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note mass spectrographic analysis of post-translational !1modifications; any acid labile modifications may have been !1missed GENETICS !$#gene rpsM !$#map_position 73 min !$#start_codon GTG COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX small subunit ribosomal proteins: S1 (PIR:R3EC1), S2 !1(PIR:R3EC2), S3 (PIR:R3EC3), S4 (PIR:R3EC4), S5 (PIR:R3EC5), !1S6 (PIR:R3EC6), S7 (PIR:R3EC7K), S8 (PIR:R3EC8), S9 !1(PIR:R3EC9), S10 (PIR:R3EC10), S11 (PIR:R3EC11), S12 !1(PIR:R3EC12), S13 (PIR:R3EC13), S14 (PIR:R3EC14), S15 !1(PIR:R3EC15), S16 (PIR:R3EC16), S17 (PIR:R3EC17), S18 !1(PIR:R3EC18), S19 (PIR:R3EC19), S20/L26 (PIR:R3EC20), S21 !1(PIR:R3EC21), S22 (PIR:C64901) [validated, MUID:99196679] FUNCTION !$#pathway protein biosynthesis CLASSIFICATION #superfamily Escherichia coli ribosomal protein S13 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-118 #product ribosomal protein S13 #status experimental !8#label MAT SUMMARY #length 118 #molecular-weight 13099 #checksum 2828 SEQUENCE /// ENTRY R3BS3F #type complete TITLE ribosomal protein S13 - Bacillus stearothermophilus ORGANISM #formal_name Bacillus stearothermophilus DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 30-Jun-1993 ACCESSIONS A28679 REFERENCE A28679 !$#authors Brockmoeller, J.; Kamp, R.M. !$#journal Biochemistry (1988) 27:3372-3381 !$#title Cross-linked amino acids in the protein pair S13-S19 and !1sequence analysis of protein S13 of Bacillus !1stearothermophilus ribosomes. !$#cross-references MUID:88269533; PMID:3291949 !$#accession A28679 !'##molecule_type protein !'##residues 1-119 ##label BRO CLASSIFICATION #superfamily Escherichia coli ribosomal protein S13 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 119 #molecular-weight 13572 #checksum 5956 SEQUENCE /// ENTRY R3BS13 #type complete TITLE ribosomal protein S13 - Bacillus subtilis ALTERNATE_NAMES ribosomal protein BS14 ORGANISM #formal_name Bacillus subtilis DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jun-2000 ACCESSIONS C32307; S11363; D69700; A24972 REFERENCE A32307 !$#authors Boylan, S.A.; Suh, J.W.; Thomas, S.M.; Price, C.W. !$#journal J. Bacteriol. (1989) 171:2553-2562 !$#title Gene encoding the alpha core subunit of Bacillus subtilis !1RNA polymerase is cotranscribed with the genes for !1initiation factor 1 and ribosomal proteins B, S13, S11, and !1L17. !$#cross-references MUID:89213940; PMID:2496109 !$#accession C32307 !'##molecule_type DNA !'##residues 1-121 ##label BOY !'##cross-references GB:M26414; NID:g142458; PIDN:AAA22215.1; !1PID:g142461 REFERENCE S09561 !$#authors Higo, K.I.; Otaka, E.; Osawa, S. !$#journal Mol. Gen. Genet. (1982) 185:239-244 !$#title Purification and characterization of 30S ribosomal proteins !1from Bacillus subtilis: correlation to Escherichia coli 30S !1proteins. !$#cross-references MUID:82219212; PMID:6806564 !$#accession S11363 !'##molecule_type protein !'##residues 2-28,'R',30-42 ##label HIG REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D69700 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-121 ##label KUN !'##cross-references GB:Z99104; GB:AL009126; NID:g2632267; !1PIDN:CAB11917.1; PID:g2632408 !'##experimental_source strain 168 GENETICS !$#gene rpsM CLASSIFICATION #superfamily Escherichia coli ribosomal protein S13 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-121 #product ribosomal protein S13 #status experimental !8#label MAT SUMMARY #length 121 #molecular-weight 13801 #checksum 6862 SEQUENCE /// ENTRY S59594 #type complete TITLE ribosomal protein S13 precursor, chloroplast - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S59594; S71115 REFERENCE S59594 !$#authors Kumar, R.; Drouaud, J.; Raynal, M.; Small, I. !$#journal Curr. Genet. (1995) 28:346-352 !$#title Characterization of the nuclear gene encoding chloroplast !1ribosomal protein S13 from Arabidopsis thaliana. !$#cross-references MUID:96120863; PMID:8590480 !$#accession S59594 !'##molecule_type DNA !'##residues 1-169 ##label KUM !'##cross-references EMBL:Z47986; NID:g642161; PIDN:CAA88028.1; !1PID:g662869 REFERENCE S71114 !$#authors Sanchez, H.; Fester, T.; Kloska, S.; Schroeder, W.; !1Schuster, W. !$#journal EMBO J. (1996) 15:2138-2149 !$#title Transfer of rps19 to the nucleus involves the gain of an !1RNP-binding motif which may functionally replace RPS13 in !1Arabidopsis mitochondria. !$#cross-references MUID:96208500; PMID:8641279 !$#accession S71115 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-169 ##label SAN !'##cross-references EMBL:X86734; NID:g1515106; PIDN:CAA60413.1; !1PID:g1515107 GENETICS !$#genome nuclear !$#introns 39/3; 114/3 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S13 KEYWORDS chloroplast; protein biosynthesis; ribosome FEATURE !$1-47 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$48-169 #product ribosomal protein S13 #status predicted !8#label MAT SUMMARY #length 169 #molecular-weight 19096 #checksum 7485 SEQUENCE /// ENTRY S53856 #type complete TITLE ribosomal protein S13 - Acanthamoeba castellanii mitochondrion ORGANISM #formal_name mitochondrion Acanthamoeba castellanii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 07-Dec-1999 ACCESSIONS S53856 REFERENCE S53825 !$#authors Burger, G.; Plante, I.; Lonergan, K.M.; Gray, M.W. !$#journal J. Mol. Biol. (1995) 245:522-537 !$#title The mitochondrial DNA of the amoeboid protozoon, !1Acanthamoeba castellanii: complete sequence, gene content !1and genome organization. !$#cross-references MUID:95147275; PMID:7844823 !$#accession S53856 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-119 ##label BUR !'##cross-references GB:U12386; NID:g562028; PIDN:AAD11848.1; !1PID:g562060 !'##experimental_source strain Neff; ATCC 30010 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1994 GENETICS !$#genome mitochondrion !$#genetic_code SGC6 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S13 KEYWORDS mitochondrion; protein biosynthesis; ribosome SUMMARY #length 119 #molecular-weight 13932 #checksum 3781 SEQUENCE /// ENTRY R3MZ13 #type complete TITLE ribosomal protein S13 - maize mitochondrion ORGANISM #formal_name mitochondrion Zea mays #common_name maize DATE 31-Mar-1991 #sequence_revision 30-Jun-1992 #text_change 22-Jun-1999 ACCESSIONS S01428 REFERENCE S01427 !$#authors Bland, M.M.; Levings III, C.S.; Matzinger, D.F. !$#journal Mol. Gen. Genet. (1986) 204:8-16 !$#title The tobacco mitochondrial ATPase subunit 9 gene is closely !1linked to an open reading frame for a ribosomal protein. !$#cross-references MUID:86310310; PMID:2875379 !$#accession S01428 !'##molecule_type DNA !'##residues 1-129 ##label BLA !'##cross-references EMBL:M18339; NID:g342641; PIDN:AAA70274.1; !1PID:g897624 !'##note the authors translated the codon CGG for residue 115 as Trp, !1assuming a special genetic code for plant mitochondria GENETICS !$#genome mitochondrion CLASSIFICATION #superfamily Escherichia coli ribosomal protein S13 KEYWORDS mitochondrion; protein biosynthesis; ribosome SUMMARY #length 129 #molecular-weight 14938 #checksum 1807 SEQUENCE /// ENTRY R3WT13 #type complete TITLE ribosomal protein S13 - wheat mitochondrion ORGANISM #formal_name mitochondrion Triticum aestivum #common_name common wheat DATE 31-Mar-1991 #sequence_revision 30-Jun-1992 #text_change 22-Jun-1999 ACCESSIONS S00544 REFERENCE S00544 !$#authors Bonen, L. !$#journal Nucleic Acids Res. (1987) 15:10393-10404 !$#title The mitochondrial S13 ribosomal protein gene is silent in !1wheat embryos and seedlings. !$#cross-references MUID:88096574; PMID:2827122 !$#accession S00544 !'##molecule_type DNA !'##residues 1-116 ##label BON !'##cross-references EMBL:Y00520; NID:g13715; PIDN:CAA68574.1; !1PID:g13716 !'##note the authors translated the codon CGG for residue 115 as Trp, !1assuming a special genetic code for plant mitochondria GENETICS !$#genome mitochondrion CLASSIFICATION #superfamily Escherichia coli ribosomal protein S13 KEYWORDS mitochondrion; protein biosynthesis; ribosome SUMMARY #length 116 #molecular-weight 13437 #checksum 3477 SEQUENCE /// ENTRY R3NT13 #type complete TITLE ribosomal protein S13 - common tobacco mitochondrion ORGANISM #formal_name mitochondrion Nicotiana tabacum #common_name common tobacco DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 22-Jun-1999 ACCESSIONS S01847 REFERENCE S01427 !$#authors Bland, M.M.; Levings III, C.S.; Matzinger, D.F. !$#journal Mol. Gen. Genet. (1986) 204:8-16 !$#title The tobacco mitochondrial ATPase subunit 9 gene is closely !1linked to an open reading frame for a ribosomal protein. !$#cross-references MUID:86310310; PMID:2875379 !$#accession S01847 !'##molecule_type DNA !'##residues 1-116 ##label BLA !'##cross-references EMBL:X04019; NID:g13148; PIDN:CAA27645.1; !1PID:g13150 !'##note the authors translated the codon CGG for residue 115 as Trp, !1assuming a special genetic code for plant mitochondria GENETICS !$#genome mitochondrion CLASSIFICATION #superfamily Escherichia coli ribosomal protein S13 KEYWORDS mitochondrion; protein biosynthesis; ribosome SUMMARY #length 116 #molecular-weight 13349 #checksum 2740 SEQUENCE /// ENTRY R3PZ3M #type complete TITLE ribosomal protein S13 - carrot mitochondrion ORGANISM #formal_name mitochondrion Daucus carota #common_name carrot DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 22-Jun-1999 ACCESSIONS S20229; S12261 REFERENCE S12261 !$#authors Wissinger, B.; Schuster, W.; Brennicke, A. !$#journal Mol. Gen. Genet. (1990) 224:389-395 !$#title Species-specific RNA editing patterns in the mitochondrial !1rps13 transcripts of Oenothera and Daucus. !$#cross-references MUID:91094776; PMID:2266944 !$#accession S20229 !'##molecule_type mRNA !'##residues 1-116 ##label WIS1 !'##cross-references EMBL:X54417 !$#accession S12261 !'##molecule_type DNA !'##residues 1-8,'S',10-18,'S',20-33,'R',35-116 ##label WIS2 !'##cross-references EMBL:X54417; NID:g12905; PIDN:CAA38281.1; !1PID:g12906 GENETICS !$#gene rps13 !$#genome mitochondrion CLASSIFICATION #superfamily Escherichia coli ribosomal protein S13 KEYWORDS mitochondrion; protein biosynthesis; ribosome; RNA editing SUMMARY #length 116 #molecular-weight 13495 #checksum 2767 SEQUENCE /// ENTRY R3OB3M #type complete TITLE ribosomal protein S13 - evening primrose mitochondrion ORGANISM #formal_name mitochondrion Oenothera villaricae #common_name evening primrose DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 22-Jun-1999 ACCESSIONS S20230; S12262; S03524 REFERENCE S12261 !$#authors Wissinger, B.; Schuster, W.; Brennicke, A. !$#journal Mol. Gen. Genet. (1990) 224:389-395 !$#title Species-specific RNA editing patterns in the mitochondrial !1rps13 transcripts of Oenothera and Daucus. !$#cross-references MUID:91094776; PMID:2266944 !$#accession S20230 !'##molecule_type mRNA !'##residues 1-114 ##label WIS1 !'##cross-references EMBL:X54416 !$#accession S12262 !'##molecule_type DNA !'##residues 1-8,'S',10-93,'S',95-114 ##label WIS2 !'##cross-references EMBL:X54416; NID:g13186; PIDN:CAA38280.1; !1PID:g13187 REFERENCE S03524 !$#authors Schuster, W.; Brennicke, A. !$#journal Mol. Gen. Genet. (1987) 210:44-51 !$#title Plastid DNA in the mitochondrial genome of Oenothera: intra- !1and interorganellar rearrangements involving part of the !1plastid ribosomal cistron. !$#accession S03524 !'##molecule_type DNA !'##residues 1-8,'S',10-41,'P',43-93,'S',95-114 ##label SCH !'##note the authors translated the codon CGG for residues 106 and 113 !1as Trp, assuming a special genetic code for plant !1mitochondria !'##note this sequence has been revised in reference S12261 GENETICS !$#gene rps13 !$#genome mitochondrion CLASSIFICATION #superfamily Escherichia coli ribosomal protein S13 KEYWORDS mitochondrion; protein biosynthesis; ribosome; RNA editing SUMMARY #length 114 #molecular-weight 13238 #checksum 3863 SEQUENCE /// ENTRY S41141 #type complete TITLE ribosomal protein S13 - liverwort (Marchantia polymorpha) mitochondrion ORGANISM #formal_name mitochondrion Marchantia polymorpha DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S41141; S25982 REFERENCE S41132 !$#authors Takemura, M.; Oda, K.; Yamato, K.; Ohta, E.; Nakamura, Y.; !1Nozato, N.; Akashi, K.; Ohyama, K. !$#journal Nucleic Acids Res. (1992) 20:3199-3205 !$#title Gene clusters for ribosomal proteins in the mitochondrial !1genome of a liverwort, Marchantia polymorpha. !$#cross-references MUID:92319654; PMID:1620617 !$#accession S41141 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-120 ##label TAK !'##cross-references EMBL:M68929; NID:g786182; PIDN:AAC09423.1; !1PID:g786210 REFERENCE S25941 !$#authors Oda, K.; Yamato, K.; Ohta, E.; Nakamura, Y.; Takemura, M.; !1Nozato, N.; Akashi, K.; Kanegae, T.; Ogura, Y.; Kohchi, T.; !1Ohyama, K. !$#journal J. Mol. Biol. (1992) 223:1-7 !$#title Gene organization deduced from the complete sequence of !1liverwort Marchantia polymorpha mitochondrial DNA. A !1primitive form of plant mitochondrial genome. !$#cross-references MUID:92114051; PMID:1731062 !$#accession S25982 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-120 ##label ODA !'##cross-references EMBL:M68929; NID:g786182; PIDN:AAC09423.1; !1PID:g786210 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1February 1992 GENETICS !$#gene rps13 !$#genome mitochondrion CLASSIFICATION #superfamily Escherichia coli ribosomal protein S13 KEYWORDS mitochondrion; protein biosynthesis; ribosome SUMMARY #length 120 #molecular-weight 13764 #checksum 4729 SEQUENCE /// ENTRY S53897 #type complete TITLE probable ribosomal protein S13, mitochondrial - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein N2322; protein YNL081c ORGANISM #formal_name Saccharomyces cerevisiae DATE 08-Jul-1995 #sequence_revision 24-May-1996 #text_change 19-Apr-2002 ACCESSIONS S53897; S63013; S63020; S63926 REFERENCE S53896 !$#authors Poehlmann, R.; Philippsen, P. !$#submission submitted to the EMBL Data Library, April 1995 !$#accession S53897 !'##molecule_type DNA !'##residues 1-143 ##label POE !'##cross-references EMBL:X86470; NID:g791101; PIDN:CAA60177.1; !1PID:g791103 REFERENCE S62997 !$#authors Poehlmann, R.; Philippsen, P. !$#submission submitted to the Protein Sequence Database, April 1996 !$#accession S63013 !'##molecule_type DNA !'##residues 1-143 ##label POW !'##cross-references EMBL:Z71357; NID:g1301974; PIDN:CAA95955.1; !1PID:g1301975; GSPDB:GN00014; MIPS:YNL081c !'##experimental_source strain S288C REFERENCE S63018 !$#authors Soler-Mira, A.; Saiz, J.E.; Ballesta, J.P.G.; Remacha, M. !$#submission submitted to the Protein Sequence Database, April 1996 !$#accession S63020 !'##molecule_type DNA !'##residues 1-143 ##label SOL !'##cross-references EMBL:Z71357; NID:g1301974; PIDN:CAA95955.1; !1PID:g1301975; GSPDB:GN00014; MIPS:YNL081c !'##experimental_source strain S288C REFERENCE S63925 !$#authors Poehlmann, R.; Philippsen, P. !$#journal Yeast (1996) 12:391-402 !$#title Sequencing a cosmid clone of Saccharomyces cerevisiae !1chromosome XIV reveals 12 new open reading frames (ORFs) and !1an ancient duplication of six ORFs. !$#cross-references MUID:96267764; PMID:8701611 !$#accession S63926 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-143 ##label POF !'##cross-references EMBL:X86470; NID:g791101; PIDN:CAA60177.1; !1PID:g791103 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1995 GENETICS !$#gene MIPS:YNL081c !'##cross-references SGD:S0005025 !$#map_position 14L CLASSIFICATION #superfamily Escherichia coli ribosomal protein S13 KEYWORDS mitochondrion; protein biosynthesis; ribosome SUMMARY #length 143 #molecular-weight 16089 #checksum 6394 SEQUENCE /// ENTRY R3HS13 #type complete TITLE ribosomal protein S6.eR [validated] - Haloarcula marismortui ALTERNATE_NAMES ribosomal protein HS13 ORGANISM #formal_name Haloarcula marismortui DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 21-Jul-2000 ACCESSIONS S11593 REFERENCE S11593 !$#authors Kimura, M.; Arndt, E.; Hatakeyama, T.; Hatakeyama, T.; !1Kimura, J. !$#journal Can. J. Microbiol. (1989) 35:195-199 !$#title Ribosomal proteins in halobacteria. !$#cross-references MUID:89248680; PMID:2655851 !$#accession S11593 !'##molecule_type protein !'##residues 1-135 ##label KIM !'##note the source is designated as Halobacterium marismortui CLASSIFICATION #superfamily Haloarcula ribosomal protein HS13 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 135 #molecular-weight 14185 #checksum 6903 SEQUENCE /// ENTRY S34109 #type complete TITLE ribosomal protein S13, cytosolic [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 13-Jan-1995 #sequence_revision 19-Apr-1996 #text_change 08-Dec-2000 ACCESSIONS S34109; S45005; S68933 REFERENCE S34109 !$#authors Chadeneau, C.; LeMoullac, B.; Denis, M.G. !$#journal Nucleic Acids Res. (1993) 21:2945 !$#title Cloning and analysis of the human S13 ribosomal protein !1cDNA. !$#cross-references MUID:93324387; PMID:8332508 !$#accession S34109 !'##molecule_type mRNA !'##residues 1-151 ##label CHA !'##cross-references EMBL:L01124; NID:g307390; PIDN:AAA60283.1; !1PID:g307391 REFERENCE S45005 !$#authors Filipenko, M.L. !$#submission submitted to the EMBL Data Library, May 1994 !$#accession S45005 !'##molecule_type mRNA !'##residues 1-151 ##label FIL !'##cross-references EMBL:X79239; NID:g488416; PIDN:CAA55821.1; !1PID:g488417 REFERENCE S68911 !$#authors Vladimirov, S.N.; Ivanov, A.V.; Karpova, G.G.; Musolyamov, !1A.K.; Egorov, T.A.; Thiede, B.; Wittmann-Liebold, B.; Otto, !1A. !$#journal Eur. J. Biochem. (1996) 239:144-149 !$#title Characterization of the human small-ribosomal-subunit !1proteins by N-terminal and internal sequencing, and mass !1spectrometry. !$#cross-references MUID:96305378; PMID:8706699 !$#accession S68933 !'##molecule_type protein !'##residues 2-8 ##label VLA GENETICS !$#gene GDB:RPS13 !'##cross-references GDB:215600 !$#map_position 19q-19q CLASSIFICATION #superfamily rat ribosomal protein S13; eubacterial !1ribosomal protein S15 homology KEYWORDS protein biosynthesis; ribosome FEATURE !$2-151 #product ribosomal protein S13 #status experimental !8#label MAT\ !$82-148 #domain eubacterial ribosomal protein S15 homology !8#label ES15 SUMMARY #length 151 #molecular-weight 17222 #checksum 7030 SEQUENCE /// ENTRY S25374 #type complete TITLE ribosomal protein S13.e, cytosolic - yeast (Candida maltosa) ORGANISM #formal_name Candida maltosa DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S25374 REFERENCE S25373 !$#authors Sasnauskas, K.; Jomantiene, R.; Lebediene, E.; Lebedys, J.; !1Januska, A.; Janulaitis, A. !$#journal Yeast (1992) 8:253-259 !$#title Molecular cloning and analysis of autonomous replicating !1sequence of Candida maltosa. !$#cross-references MUID:92383945; PMID:1514324 !$#accession S25374 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-151 ##label SAS GENETICS !$#introns 7/3 CLASSIFICATION #superfamily rat ribosomal protein S13; eubacterial !1ribosomal protein S15 homology KEYWORDS protein biosynthesis; ribosome FEATURE !$2-151 #product ribosomal protein S13.e #status predicted !8#label MAT\ !$82-148 #domain eubacterial ribosomal protein S15 homology !8#label ES15 SUMMARY #length 151 #molecular-weight 16942 #checksum 7175 SEQUENCE /// ENTRY S30146 #type complete TITLE ribosomal protein S13, cytosolic - maize ORGANISM #formal_name Zea mays #common_name maize DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S30146 REFERENCE S30146 !$#authors Joanin, P.; Gigot, C.; Philipps, G. !$#journal Plant Mol. Biol. (1993) 21:701-704 !$#title cDNA nucleotide sequence and expression of a maize !1cytoplasmic ribosomal protein S13 gene. !$#cross-references MUID:93192530; PMID:8448368 !$#accession S30146 !'##molecule_type mRNA !'##residues 1-151 ##label JOA !'##cross-references EMBL:X62455; NID:g288058; PIDN:CAA44311.1; !1PID:g288059 CLASSIFICATION #superfamily rat ribosomal protein S13; eubacterial !1ribosomal protein S15 homology KEYWORDS protein biosynthesis; ribosome FEATURE !$2-151 #product ribosomal protein S13 #status predicted !8#label MAT\ !$82-148 #domain eubacterial ribosomal protein S15 homology !8#label ES15 SUMMARY #length 151 #molecular-weight 17058 #checksum 6071 SEQUENCE /// ENTRY R3RT13 #type complete TITLE ribosomal protein S13, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 21-Jul-2000 ACCESSIONS A35889; A33220; S12077 REFERENCE A35889 !$#authors Suzuki, K.; Olvera, J.; Wool, I.G. !$#journal Biochem. Biophys. Res. Commun. (1990) 171:519-524 !$#title The primary structure of rat ribosomal protein S13. !$#cross-references MUID:90386616; PMID:2403345 !$#accession A35889 !'##molecule_type mRNA !'##residues 1-151 ##label SUZ !'##cross-references EMBL:X53378; NID:g57729; PIDN:CAA37458.1; !1PID:g57730 !$#accession A33220 !'##molecule_type protein !'##residues 2-27 ##label SUZ2 !'##note the protein is designated as ribosomal protein S13 CLASSIFICATION #superfamily rat ribosomal protein S13; eubacterial !1ribosomal protein S15 homology KEYWORDS protein biosynthesis; ribosome FEATURE !$2-151 #product ribosomal protein S13 #status experimental !8#label MAT\ !$82-148 #domain eubacterial ribosomal protein S15 homology !8#label ES15 SUMMARY #length 151 #molecular-weight 17222 #checksum 7030 SEQUENCE /// ENTRY S57438 #type complete TITLE ribosomal protein S13, cytosolic - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 10-Oct-1995 #sequence_revision 19-Apr-1996 #text_change 22-Jun-1999 ACCESSIONS S57438; S66165 REFERENCE S57438 !$#authors Xia, L.; Liu, J.; Sage, C.; Trexler, B.; Andrews, M.; !1Maxwell, S. !$#submission submitted to the EMBL Data Library, June 1995 !$#description Intronic U14 snoRNAs of Xenopus laevis are located in two !1different parent genes and can be processed from their !1introns during early oogenesis. !$#accession S57438 !'##molecule_type genomic RNA !'##residues 1-151 ##label XIA !'##cross-references EMBL:Z49897; NID:g871773; PIDN:CAA90077.1; !1PID:g871774 REFERENCE S66165 !$#authors Xia, L.; Liu, J.; Sage, C.; Trexler, E.B.; Andrews, M.T.; !1Maxwell, E.S. !$#journal Nucleic Acids Res. (1995) 23:4844-4849 !$#title Intronic U14 snoRNAs of Xenopus laevis are located in two !1different parent genes and can be processed from their !1introns during early oogenesis. !$#cross-references MUID:96128298; PMID:8532527 !$#accession S66165 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-151 ##label XIW !'##cross-references EMBL:Z49897; NID:g871773; PIDN:CAA90077.1; !1PID:g871774 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1995 GENETICS !$#introns 8/2; 24/3; 51/1; 107/3; 141/2 CLASSIFICATION #superfamily rat ribosomal protein S13; eubacterial !1ribosomal protein S15 homology KEYWORDS protein biosynthesis; ribosome FEATURE !$2-151 #product ribosomal protein S13 #status predicted !8#label MAT\ !$82-148 #domain eubacterial ribosomal protein S15 homology !8#label ES15 SUMMARY #length 151 #molecular-weight 17250 #checksum 7156 SEQUENCE /// ENTRY JC4307 #type complete TITLE ribosomal protein S13.e, cytosolic - channel catfish ORGANISM #formal_name Ictalurus punctatus #common_name channel catfish DATE 16-Nov-1995 #sequence_revision 19-Apr-1996 #text_change 22-Jun-1999 ACCESSIONS JC4307 REFERENCE JC4307 !$#authors Porta, A.R.; Margolis, F.L. !$#journal Gene (1995) 163:319-320 !$#title Cloning of a cDNA encoding the S13 ribosomal protein from !1the catfish Ictalurus punctatus. !$#cross-references MUID:96011655; PMID:7590288 !$#accession JC4307 !'##molecule_type mRNA !'##residues 1-151 ##label POR !'##cross-references GB:U21163; NID:g699580; PIDN:AAA91984.1; !1PID:g699581 GENETICS !$#gene rpS13 CLASSIFICATION #superfamily rat ribosomal protein S13; eubacterial !1ribosomal protein S15 homology KEYWORDS protein biosynthesis; ribosome FEATURE !$2-151 #product ribosomal protein S13.e #status predicted !8#label MAT\ !$82-148 #domain eubacterial ribosomal protein S15 homology !8#label ES15 SUMMARY #length 151 #molecular-weight 17167 #checksum 6126 SEQUENCE /// ENTRY S33684 #type complete TITLE ribosomal protein S13.e, cytosolic - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES ribosomal protein DS17 ORGANISM #formal_name Drosophila melanogaster DATE 02-Dec-1993 #sequence_revision 14-Nov-1997 #text_change 16-Jun-2000 ACCESSIONS S70391; S70392; S33684; S31453 REFERENCE S70391 !$#authors Saeboe-Larssen, S.; Lambertsson, A. !$#journal Genetics (1996) 143:877-885 !$#title A novel Drosophila Minute locus encodes ribosomal protein !1S13. !$#cross-references MUID:96363921; PMID:8725235 !$#accession S70391 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-151 ##label SAE !'##cross-references EMBL:X91853; NID:g1107561; PIDN:CAA62964.1; !1PID:g1107562 !'##note the authors did not translate the codon for residue 1 !$#accession S70392 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-151 ##label SAW !'##cross-references EMBL:X91854; NID:g1107563; PIDN:CAA62965.1; !1PID:g1107564 !'##note the authors did not translate the codon for residue 1 REFERENCE S33684 !$#authors McNabb, S.L.; Ashburner, M. !$#journal Nucleic Acids Res. (1993) 21:2523 !$#title Identification of a Drosophila protein similar to rat S13 !1and archaebacterial S11 ribosomal proteins. !$#cross-references MUID:93281413; PMID:8506150 !$#accession S33684 !'##molecule_type mRNA !'##residues 1-39,'A',41,'QE',44,'SDSLQ',50-151 ##label MCN !'##cross-references EMBL:Z19052; NID:g8409; PIDN:CAA79496.1; PID:g8410 GENETICS !$#gene FlyBase:RpS13 !$#map_position 29A !$#introns 8/2; 51/1 CLASSIFICATION #superfamily rat ribosomal protein S13; eubacterial !1ribosomal protein S15 homology KEYWORDS protein biosynthesis; ribosome FEATURE !$2-151 #product ribosomal protein S13.e #status predicted !8#label MAT\ !$82-148 #domain eubacterial ribosomal protein S15 homology !8#label ES15 SUMMARY #length 151 #molecular-weight 17178 #checksum 5268 SEQUENCE /// ENTRY R3KW13 #type complete TITLE ribosomal protein S13.e, cytosolic - nematode (Brugia pahangi) ALTERNATE_NAMES 17.4K protein ORGANISM #formal_name Brugia pahangi DATE 30-Sep-1991 #sequence_revision 19-Apr-1996 #text_change 22-Jun-1999 ACCESSIONS S32687; S14440; S06771 REFERENCE S32687 !$#authors Ellenberger, D.L.; Pieniazek, N.J.; Lammie, P.J. !$#submission submitted to the EMBL Data Library, January 1992 !$#description Developmental modulation of relative gene numbers in a !1parasitic nematode. !$#accession S32687 !'##molecule_type DNA !'##residues 1-151 ##label ELL !'##cross-references EMBL:X63714; NID:g297070; PIDN:CAA45247.1; !1PID:g297071 REFERENCE S14440 !$#authors Ellenberger, D.L.; Pieniazek, N.J.; Lammie, P.J. !$#journal Nucleic Acids Res. (1989) 17:10121 !$#title Nucleotide sequence of Brugia pahangi 17.4 kD protein. !$#cross-references MUID:90098795; PMID:2602125 !$#accession S14440 !'##molecule_type mRNA !'##residues 1-26,'K',28-36,'V',38-106,'Q',108-118,'Q',120-123,'R', !1125-151 ##label EL2 !'##cross-references EMBL:X16591 GENETICS !$#introns 43/3; 78/3; 107/3 CLASSIFICATION #superfamily rat ribosomal protein S13; eubacterial !1ribosomal protein S15 homology KEYWORDS protein biosynthesis; ribosome FEATURE !$2-151 #product ribosomal protein S13.e #status predicted !8#label MAT\ !$82-148 #domain eubacterial ribosomal protein S15 homology !8#label ES15 SUMMARY #length 151 #molecular-weight 17388 #checksum 9365 SEQUENCE /// ENTRY S26296 #type complete TITLE 40s ribosomal protein s13 - fission yeast (Schizosaccharomyces pombe) ORGANISM #formal_name Schizosaccharomyces pombe DATE 29-Jan-1993 #sequence_revision 19-Apr-1996 #text_change 10-Dec-1999 ACCESSIONS S26296; T39041 REFERENCE S26296 !$#authors Marks, J.; Simanis, V. !$#journal Nucleic Acids Res. (1992) 20:4094 !$#title Cloning of the gene for ribosomal protein S13 from the !1fission yeast Schizosaccharomyces pombe. !$#cross-references MUID:92375702; PMID:1508697 !$#accession S26296 !'##molecule_type DNA !'##residues 1-151 ##label MAR !'##cross-references EMBL:X67030; NID:g5071; PIDN:CAA47424.1; PID:g5072 REFERENCE Z21797 !$#authors Gentles, S.; Churcher, C.M.; Barrell, B.G.; Rajandream, !1M.A.; Wood, V. !$#submission submitted to the EMBL Data Library, September 1997 !$#accession T39041 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-151 ##label GEN !'##cross-references EMBL:Z98981; PIDN:CAB11741.1; GSPDB:GN00066; !1SPDB:SPAC6F6.07c !'##experimental_source strain 972h-; cosmid c6F6 GENETICS !$#gene SPAC6F6.07c !$#map_position 1 !$#introns 68/1; 79/1; 94/3 CLASSIFICATION #superfamily rat ribosomal protein S13; eubacterial !1ribosomal protein S15 homology KEYWORDS protein biosynthesis; ribosome FEATURE !$2-151 #product ribosomal protein S13.e #status predicted !8#label MAT\ !$82-148 #domain eubacterial ribosomal protein S15 homology !8#label ES15 SUMMARY #length 151 #molecular-weight 16953 #checksum 6968 SEQUENCE /// ENTRY S36423 #type complete TITLE ribosomal protein S13, cytosolic - garden pea ORGANISM #formal_name Pisum sativum #common_name garden pea DATE 06-Jan-1995 #sequence_revision 19-Apr-1996 #text_change 22-Jun-1999 ACCESSIONS S36423 REFERENCE S36423 !$#authors Bertsch, U.; Clausen-Krueper, S.; Soll, J. !$#submission submitted to the EMBL Data Library, August 1993 !$#description Sequence of ribosomal protein S13 from spinach. !$#accession S36423 !'##molecule_type mRNA !'##residues 1-151 ##label BER !'##cross-references EMBL:Z25509; NID:g396638; PIDN:CAA80974.1; !1PID:g396639 CLASSIFICATION #superfamily rat ribosomal protein S13; eubacterial !1ribosomal protein S15 homology KEYWORDS protein biosynthesis; ribosome FEATURE !$2-151 #product ribosomal protein S13 #status predicted !8#label MAT\ !$82-148 #domain eubacterial ribosomal protein S15 homology !8#label ES15 SUMMARY #length 151 #molecular-weight 17116 #checksum 6660 SEQUENCE /// ENTRY R3HS11 #type complete TITLE ribosomal protein S15 [validated] - Haloarcula marismortui ALTERNATE_NAMES ribosomal protein HS11; ribosomal protein HS13.eR ORGANISM #formal_name Haloarcula marismortui DATE 31-Dec-1988 #sequence_revision 31-Mar-1992 #text_change 21-Jul-2000 ACCESSIONS A31906; A23602 REFERENCE A92677 !$#authors Arndt, E.; Kimura, M. !$#journal J. Biol. Chem. (1988) 263:16063-16068 !$#title Molecular cloning and nucleotide sequence of the gene for !1the ribosomal protein S11 from the archaebacterium !1Halobacterium marismortui. !$#cross-references MUID:89034064; PMID:3182783 !$#accession A31906 !'##molecule_type DNA !'##residues 1-156 ##label ARN !'##cross-references GB:J04062; NID:g148809; PIDN:AAA72208.1; !1PID:g148810 REFERENCE A23602 !$#authors Arndt, E.; Breithaupt, G.; Kimura, M. !$#journal FEBS Lett. (1986) 194:227-234 !$#title The complete amino acid sequence of ribosomal protein H-S11 !1from the archaebacterium Halobacterium marismortui. !$#accession A23602 !'##molecule_type protein !'##residues 2-25,'A',27-156 ##label ARN2 !'##note the source is given as Halobacterium marismortui CLASSIFICATION #superfamily rat ribosomal protein S13; eubacterial !1ribosomal protein S15 homology KEYWORDS protein biosynthesis; ribosome FEATURE !$2-156 #product ribosomal protein S13.eR #status !8experimental #label MAT\ !$86-151 #domain eubacterial ribosomal protein S15 homology !8#label ES15 SUMMARY #length 156 #molecular-weight 17692 #checksum 6168 SEQUENCE /// ENTRY R3BY14 #type complete TITLE ribosomal protein S14 precursor, mitochondrial - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein P9325.7; protein YPR166c; ribosomal protein MRP2 ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 21-Jul-2000 ACCESSIONS B29138; S59825 REFERENCE A92628 !$#authors Myers, A.M.; Crivellone, M.D.; Tzagoloff, A. !$#journal J. Biol. Chem. (1987) 262:3388-3397 !$#title Assembly of the mitochondrial membrane system. MRP1 and !1MRP2, two yeast nuclear genes coding for mitochondrial !1ribosomal proteins. !$#cross-references MUID:87137621; PMID:3029111 !$#accession B29138 !'##molecule_type DNA !'##residues 1-115 ##label MYE !'##cross-references GB:M15161; NID:g171975; PIDN:AAA74728.1; !1PID:g171976 REFERENCE S59821 !$#authors Hallsworth, K. !$#submission submitted to the EMBL Data Library, April 1995 !$#description The sequence of S. cerevisiae cosmid 9325. !$#accession S59825 !'##molecule_type DNA !'##residues 1-115 ##label HAL !'##cross-references EMBL:U25840; NID:g786286; PIDN:AAB68153.1; !1PID:g786291; GSPDB:GN00016; MIPS:YPR166c GENETICS !$#gene SGD:MRP2; MIPS:YPR166c !'##cross-references SGD:S0006370; MIPS:YPR166c !$#map_position 16R !$#genome nuclear CLASSIFICATION #superfamily Escherichia coli ribosomal protein S14 KEYWORDS mitochondrion; protein biosynthesis; ribosome SUMMARY #length 115 #molecular-weight 13538 #checksum 1374 SEQUENCE /// ENTRY R3EC14 #type complete TITLE ribosomal protein S14 [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 13-Jun-1983 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS F65123; A02732 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65123 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-101 ##label BLAT !'##cross-references GB:AE000408; GB:U00096; NID:g1789694; !1PIDN:AAC76332.1; PID:g1789703; UWGP:b3307 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A02732 !$#authors Yaguchi, M.; Roy, C.; Reithmeier, R.A.F.; Wittmann-Liebold, !1B. !$#submission submitted to the Atlas, October 1982 !$#accession A02732 !'##molecule_type protein !'##residues 2-91,'Q',93-98,'S' ##label YAG !'##experimental_source strain K12 REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note mass spectrographic analysis of post-translational !1modifications; any acid labile modifications may have been !1missed GENETICS !$#gene rpsN !$#map_position 73 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX small subunit ribosomal proteins: S1 (PIR:R3EC1), S2 !1(PIR:R3EC2), S3 (PIR:R3EC3), S4 (PIR:R3EC4), S5 (PIR:R3EC5), !1S6 (PIR:R3EC6), S7 (PIR:R3EC7K), S8 (PIR:R3EC8), S9 !1(PIR:R3EC9), S10 (PIR:R3EC10), S11 (PIR:R3EC11), S12 !1(PIR:R3EC12), S13 (PIR:R3EC13), S14 (PIR:R3EC14), S15 !1(PIR:R3EC15), S16 (PIR:R3EC16), S17 (PIR:R3EC17), S18 !1(PIR:R3EC18), S19 (PIR:R3EC19), S20/L26 (PIR:R3EC20), S21 !1(PIR:R3EC21), S22 (PIR:C64901) [validated, MUID:99196679] FUNCTION !$#pathway protein biosynthesis CLASSIFICATION #superfamily Escherichia coli ribosomal protein S14 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-101 #product ribosomal protein S14 #status experimental !8#label MAT SUMMARY #length 101 #molecular-weight 11580 #checksum 1009 SEQUENCE /// ENTRY R3BS14 #type complete TITLE ribosomal protein S14 - Bacillus subtilis ALTERNATE_NAMES ribosomal protein BS-A ORGANISM #formal_name Bacillus subtilis DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jun-2000 ACCESSIONS S05995; S11364; E69700 REFERENCE S05989 !$#authors Henkin, T.M.; Moon, S.H.; Mattheakis, L.C.; Nomura, M. !$#journal Nucleic Acids Res. (1989) 17:7469-7486 !$#title Cloning and analysis of the spc ribosomal protein operon of !1Bacillus subtilis: comparison with the spc operon of !1Escherichia coli. !$#cross-references MUID:90016806; PMID:2508062 !$#accession S05995 !'##molecule_type DNA !'##residues 1-61 ##label HEN !'##cross-references EMBL:X15664; NID:g40146; PIDN:CAA33704.1; !1PID:g580930 !'##note the authors translated the initiation codon GTG for residue 1 !1as Val REFERENCE S09561 !$#authors Higo, K.I.; Otaka, E.; Osawa, S. !$#journal Mol. Gen. Genet. (1982) 185:239-244 !$#title Purification and characterization of 30S ribosomal proteins !1from Bacillus subtilis: correlation to Escherichia coli 30S !1proteins. !$#cross-references MUID:82219212; PMID:6806564 !$#accession S11364 !'##molecule_type protein !'##residues 2-5,'X',7-9,'ZZ',12-18,'ZZ',21-22 ##label HIG REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69700 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-61 ##label KUN !'##cross-references GB:Z99104; GB:AL009126; NID:g2632267; !1PIDN:CAB11905.1; PID:g2632396 !'##experimental_source strain 168 GENETICS !$#gene rpsN !$#start_codon GTG CLASSIFICATION #superfamily Escherichia coli ribosomal protein S14 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-61 #product ribosomal protein S14 #status experimental !8#label MAT SUMMARY #length 61 #molecular-weight 7246 #checksum 6580 SEQUENCE /// ENTRY R3YM14 #type complete TITLE ribosomal protein S14 - Mycoplasma capricolum ORGANISM #formal_name Mycoplasma capricolum DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 07-Dec-1999 ACCESSIONS S02844 REFERENCE S02830 !$#authors Ohkubo, S.; Muto, A.; Kawauchi, Y.; Yamao, F.; Osawa, S. !$#journal Mol. Gen. Genet. (1987) 210:314-322 !$#title The ribosomal protein gene cluster of Mycoplasma capricolum. !$#cross-references MUID:88142549; PMID:3481422 !$#accession S02844 !'##molecule_type DNA !'##residues 1-61 ##label OHK !'##cross-references EMBL:X06414; NID:g44207; PIDN:CAA29717.1; !1PID:g44222 GENETICS !$#gene rps14 !$#genetic_code SGC3 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S14 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 61 #molecular-weight 7120 #checksum 4659 SEQUENCE /// ENTRY S30298 #type complete TITLE ribosomal protein S29, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 21-Jul-2000 ACCESSIONS S30298; S48901 REFERENCE S30297 !$#authors Chan, Y.L.; Suzuki, K.; Olvera, J.; Wool, I.G. !$#journal Nucleic Acids Res. (1993) 21:649-655 !$#title Zinc finger-like motifs in rat ribosomal proteins S27 and !1S29. !$#cross-references MUID:93181260; PMID:8441676 !$#accession S30298 !'##molecule_type mRNA !'##residues 1-56 ##label CHA1 !'##cross-references EMBL:X59051; NID:g57132; PIDN:CAA41778.1; !1PID:g57133 !$#accession S48901 !'##molecule_type protein !'##residues 2-5,'X',7-56 ##label CHA2 !'##note the protein is designated as ribosomal protein S29 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S14 KEYWORDS protein biosynthesis; ribosome; zinc finger FEATURE !$2-56 #product ribosomal protein S29 #status experimental !8#label MAT\ !$21-42 #region zinc finger SUMMARY #length 56 #molecular-weight 6677 #checksum 585 SEQUENCE /// ENTRY R3MX14 #type complete TITLE ribosomal protein S14 - Methanococcus vannielii ORGANISM #formal_name Methanococcus vannielii DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 22-Jun-1999 ACCESSIONS S05618 REFERENCE S05611 !$#authors Auer, J.; Spicker, G.; Boeck, A. !$#journal J. Mol. Biol. (1989) 209:21-36 !$#title Organization and structure of the Methanococcus !1transcriptional unit homologous to the Escherichia coli !1"spectinomycin operon". Implications for the evolutionary !1relationship of 70 S and 80 S ribosomes. !$#cross-references MUID:90040717; PMID:2530355 !$#accession S05618 !'##molecule_type DNA !'##residues 1-53 ##label AUE !'##cross-references EMBL:X16720; NID:g44754; PIDN:CAA34694.1; !1PID:g44762 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S14 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 53 #molecular-weight 6129 #checksum 7370 SEQUENCE /// ENTRY S16536 #type complete TITLE ribosomal protein S14 [similarity] - Haloarcula marismortui ORGANISM #formal_name Haloarcula marismortui DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 21-Jul-2000 ACCESSIONS S16536; T46801 REFERENCE S16535 !$#authors Scholzen, T.; Arndt, E. !$#journal Mol. Gen. Genet. (1991) 228:70-80 !$#title Organization and nucleotide sequence of ten ribosomal !1protein genes from the region equivalent to the !1spectinomycin operon in the archaebacterium Halobacterium !1marismortui. !$#cross-references MUID:91360093; PMID:1832208 !$#accession S16536 !'##molecule_type DNA !'##residues 1-61 ##label SCH !'##cross-references EMBL:X58395; NID:g48860; PIDN:CAA41285.1; !1PID:g48862 !'##note the source is designated as Halobacterium marismortui GENETICS !$#gene HmaS14 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S14 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 61 #molecular-weight 7017 #checksum 6013 SEQUENCE /// ENTRY R3VF14 #type complete TITLE ribosomal protein S14 - fava bean mitochondrion ORGANISM #formal_name mitochondrion Vicia faba #common_name fava bean DATE 31-Mar-1991 #sequence_revision 30-Jun-1992 #text_change 22-Jun-1999 ACCESSIONS S01224 REFERENCE S01221 !$#authors Wahleithner, J.A.; Wolstenholme, D.R. !$#journal Nucleic Acids Res. (1988) 16:6897-6913 !$#title Ribosomal protein S14 genes in broad bean mitochondrial DNA. !$#cross-references MUID:88303319; PMID:3405753 !$#accession S01224 !'##molecule_type DNA !'##residues 1-100 ##label WAH !'##cross-references EMBL:X07237; NID:g13880; PIDN:CAA30225.1; !1PID:g13881 !'##note the authors translated the codon CGG for residue 40 as Trp, !1assuming a special genetic code for plant mitochondria GENETICS !$#gene rps14 !$#genome mitochondrion CLASSIFICATION #superfamily Escherichia coli ribosomal protein S14 KEYWORDS mitochondrion; protein biosynthesis; ribosome SUMMARY #length 100 #molecular-weight 11965 #checksum 324 SEQUENCE /// ENTRY R3OB4B #type complete TITLE ribosomal protein S14 - evening primrose mitochondrion ORGANISM #formal_name mitochondrion Oenothera villaricae #common_name evening primrose DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 22-Jun-1999 ACCESSIONS S07889; S20239; S78219 REFERENCE S07889 !$#authors Schuster, W.; Unseld, M.; Wissinger, B.; Brennicke, A. !$#journal Nucleic Acids Res. (1990) 18:229-233 !$#title Ribosomal protein S14 transcripts are edited in Oenothera !1mitochondria. !$#cross-references MUID:90221801; PMID:2326162 !$#accession S07889 !'##molecule_type mRNA !'##residues 1-99 ##label SCH !'##cross-references EMBL:X17030 !$#accession S20239 !'##molecule_type DNA !'##residues 1-63,'S',65-89,'P',91-99 ##label SCH2 !'##cross-references EMBL:X17030; NID:g13193; PIDN:CAA34891.1; !1PID:g13194 REFERENCE S46517 !$#authors Schuster, W. !$#journal Plant Mol. Biol. (1994) 25:33-42 !$#title The highly edited orf206 in Oenothera mitochondria may !1encode a component of a heme transporter involved in !1cytochrome c biogenesis. !$#cross-references MUID:94272012; PMID:8003696 !$#accession S78219 !'##molecule_type DNA !'##residues 1-15 ##label SCW !'##cross-references EMBL:X74164 !'##note the source is designated as Oenothera berteriana GENETICS !$#gene rps14 !$#genome mitochondrion CLASSIFICATION #superfamily Escherichia coli ribosomal protein S14 KEYWORDS mitochondrion; protein biosynthesis; ribosome; RNA editing SUMMARY #length 99 #molecular-weight 11964 #checksum 6652 SEQUENCE /// ENTRY R3PP14 #type complete TITLE ribosomal protein S14 - Paramecium tetraurelia mitochondrion ORGANISM #formal_name mitochondrion Paramecium tetraurelia DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 07-Dec-1999 ACCESSIONS JS0231; S07732 REFERENCE JS0231 !$#authors Pritchard, A.E.; Venuti, S.E.; Ghalambor, M.A.; Sable, C.L.; !1Cummings, D.J. !$#journal Gene (1989) 78:121-134 !$#title An unusual region of Paramecium mitochondrial DNA containing !1chloroplast-like genes. !$#cross-references MUID:89357489; PMID:2670676 !$#accession JS0231 !'##molecule_type DNA !'##residues 1-102 ##label PRI !'##cross-references GB:M26930; NID:g341550; PIDN:AAA79253.1; !1PID:g1019628 !'##experimental_source strain sp. 4.51 !'##note it is uncertain whether Met-1 is the initiator or whether !1translation is initiated at 2-Ile (ATA) !'##note the source is designated as Paramecium aurelia species 4 stock !151, now designated Paramecium tetraurelia, ATCC 30567 REFERENCE S07725 !$#authors Pritchard, A.E.; Seilhamer, J.J.; Mahalingam, R.; Sable, !1C.L.; Venuti, S.E.; Cummings, D.J. !$#journal Nucleic Acids Res. (1990) 18:173-180 !$#title Nucleotide sequence of the mitochondrial genome of !1Paramecium. !$#cross-references MUID:90174913; PMID:2308823 !$#accession S07732 !'##status translation not shown !'##molecule_type DNA !'##residues 1-102 ##label PRI2 !'##cross-references EMBL:X15917; NID:g13256; PIDN:CAA34041.1; !1PID:g13264 GENETICS !$#gene rps14 !$#genome mitochondrion !$#genetic_code SGC6 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S14 KEYWORDS mitochondrion; protein biosynthesis; ribosome SUMMARY #length 102 #molecular-weight 12273 #checksum 6762 SEQUENCE /// ENTRY R3EG14 #type complete TITLE ribosomal protein S14, chloroplast - Euglena gracilis chloroplast ORGANISM #formal_name chloroplast Euglena gracilis DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S04701; S34531; S34898 REFERENCE S04701 !$#authors Nickoloff, J.A.; Christopher, D.A.; Drager, R.G.; Hallick, !1R.B. !$#journal Nucleic Acids Res. (1989) 17:4882 !$#title Nucleotide sequence of the Euglena gracilis chloroplast !1genes for isoleucine, phenylalanine and cysteine transfer !1RNAs and ribosomal protein S14. !$#cross-references MUID:89315233; PMID:2501762 !$#accession S04701 !'##molecule_type DNA !'##residues 1-100 ##label NIC !'##cross-references EMBL:X15240; NID:g11528; PIDN:CAA33318.1; !1PID:g11529 !'##experimental_source strain Z REFERENCE S34494 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.; Monfort, !1A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#submission submitted to the EMBL Data Library, January 1993 !$#description The complete sequence of the Euglena gracilis chloroplast !1genome (tentative). !$#accession S34531 !'##molecule_type DNA !'##residues 1-100 ##label HAL1 !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50110.1; !1PID:g415766 REFERENCE S34862 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.R.; !1Monfort, A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#journal Nucleic Acids Res. (1993) 21:3537-3544 !$#title Complete sequence of Euglena gracilis chloroplast DNA. !$#cross-references MUID:93347989; PMID:8346031 !$#accession S34898 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-100 ##label HAL2 !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50110.1; !1PID:g415766 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1993 GENETICS !$#gene rps14 !$#genome chloroplast !$#introns 59/3 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S14 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 100 #molecular-weight 12014 #checksum 1296 SEQUENCE /// ENTRY R3IT14 #type complete TITLE ribosomal protein S14, plastid - euglenid (Astasia longa) plastid ORGANISM #formal_name plastid Astasia longa DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 22-Jun-1999 ACCESSIONS S14153; S38594 REFERENCE S14125 !$#authors Siemeister, G.; Buchholz, C.; Hachtel, W. !$#journal Curr. Genet. (1990) 18:457-464 !$#title Genes for ribosomal proteins are retained on the 73 kb DNA !1from Astasia longa that resembles Euglena chloroplast DNA. !$#cross-references MUID:91176556; PMID:2078869 !$#accession S14153 !'##molecule_type DNA !'##residues 1-100 ##label SIE !'##cross-references EMBL:X16004; NID:g16004; PIDN:CAA34141.1; !1PID:g16011 !'##experimental_source strain 1204-17a REFERENCE S38590 !$#authors Gockel, G.; Baier, S.; Hachtel, W. !$#submission submitted to the EMBL Data Library, November 1993 !$#accession S38594 !'##molecule_type DNA !'##residues 1-100 ##label GOC !'##cross-references EMBL:X75651; NID:g414852; PIDN:CAA53312.1; !1PID:g414859 GENETICS !$#gene rps14 !$#genome plastid !$#introns 59/3 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S14 KEYWORDS plastid; protein biosynthesis; ribosome SUMMARY #length 100 #molecular-weight 12206 #checksum 8364 SEQUENCE /// ENTRY R3LV14 #type complete TITLE ribosomal protein S14, chloroplast - liverwort (Marchantia polymorpha) chloroplast ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 22-Jun-1999 ACCESSIONS A02733; S01876 REFERENCE A00150 !$#authors Ohyama, K. !$#submission submitted to the EMBL Data Library, October 1986 !$#accession A02733 !'##molecule_type DNA !'##residues 1-100 ##label OHY REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features REFERENCE S01567 !$#authors Umesono, K.; Inokuchi, H.; Shiki, Y.; Takeuchi, M.; Chang, !1Z.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Ohyama, K.; Ozeki, !1H. !$#journal J. Mol. Biol. (1988) 203:299-331 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. II. Gene organization of the large !1single copy region from rps'12 to atpB. !$#cross-references MUID:89068686; PMID:2974085 !$#accession S01876 !'##molecule_type DNA !'##residues 1-100 ##label UME !'##cross-references GB:X04465; GB:Y00686; NID:g11640; PIDN:CAA28083.1; !1PID:g11670 GENETICS !$#gene rps14 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein S14 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 100 #molecular-weight 11880 #checksum 421 SEQUENCE /// ENTRY R3EJ14 #type complete TITLE ribosomal protein S14, plastid - beechdrops plastid ORGANISM #formal_name plastid Epifagus virginiana #common_name beechdrops DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 22-Jun-1999 ACCESSIONS S17794; S78381 REFERENCE S17794 !$#authors Morden, C.W.; Wolfe, K.H.; dePamphilis, C.W.; Palmer, J.D. !$#journal EMBO J. (1991) 10:3281-3288 !$#title Plastid translation and transcription genes in a !1non-photosynthetic plant: intact, missing and pseudo genes. !$#cross-references MUID:92007779; PMID:1915295 !$#accession S17794 !'##molecule_type DNA !'##residues 1-100 ##label MOR !'##cross-references EMBL:X61798; NID:g11547; PIDN:CAA43900.1; !1PID:g11548 REFERENCE S78378 !$#authors Wolfe, K.H.; Morden, C.W.; Ems, S.C.; Palmer, J.D. !$#journal J. Mol. Evol. (1992) 35:304-317 !$#title Rapid evolution of the plastid translational apparatus in a !1nonphotosynthetic plant: loss or accelerated sequence !1evolution of tRNA and ribosomal protein genes. !$#cross-references MUID:93021155; PMID:1404416 !$#accession S78381 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-100 ##label WOL !'##cross-references EMBL:M81884; NID:g336917; PIDN:AAA65852.1; !1PID:g336926 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1992 GENETICS !$#gene rps14 !$#genome plastid CLASSIFICATION #superfamily Escherichia coli ribosomal protein S14 KEYWORDS plastid; protein biosynthesis; ribosome SUMMARY #length 100 #molecular-weight 11753 #checksum 759 SEQUENCE /// ENTRY R3NT14 #type complete TITLE ribosomal protein S14, chloroplast - common tobacco chloroplast ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 30-Jan-1998 ACCESSIONS A02734 REFERENCE A00149 !$#authors Sugiura, M. !$#submission submitted to the EMBL Data Library, August 1986 !$#accession A02734 !'##molecule_type DNA !'##residues 1-100 ##label SUG !'##experimental_source cv. Bright Yellow 4 REFERENCE A38013 !$#authors Shinozaki, K.; Ohme, M.; Tanaka, M.; Wakasugi, T.; !1Hayashida, N.; Matsubayashi, T.; Zaita, N.; Chunwongse, J.; !1Obokata, J.; Yamaguchi-Shinozaki, K.; Ohto, C.; Torazawa, !1K.; Meng, B.Y.; Sugita, M.; Deno, H.; Kamogashira, T.; !1Yamada, K.; Kusuda, J.; Takaiwa, F.; Kato, A.; Tohdoh, N.; !1Shimada, H.; Sugiura, M. !$#journal EMBO J. (1986) 5:2043-2049 !$#title The complete nucleotide sequence of the tobacco chloroplast !1genome: its gene organization and expression. !$#contents annotation; gene organization, sites, features GENETICS !$#gene rps14 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein S14 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 100 #molecular-weight 11744 #checksum 1738 SEQUENCE /// ENTRY R3SP14 #type complete TITLE ribosomal protein S14, chloroplast - spinach chloroplast ORGANISM #formal_name chloroplast Spinacia oleracea #common_name spinach DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S00455 REFERENCE S00444 !$#authors Kirsch, W.; Seyer, P.; Herrmann, R.G. !$#journal Curr. Genet. (1986) 10:843-855 !$#title Nucleotide sequence of the clustered genes for two P700 !1chlorophyll a apoproteins of the photosystem I reaction !1center and the ribosomal protein S14 of the spinach plastid !1chromosome. !$#accession S00455 !'##molecule_type DNA !'##residues 1-100 ##label KIR !'##cross-references EMBL:X04131; NID:g12269; PIDN:CAA27746.1; !1PID:g12272 GENETICS !$#gene rps14 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein S14 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 100 #molecular-weight 11781 #checksum 446 SEQUENCE /// ENTRY R3RZ14 #type complete TITLE ribosomal protein S14, chloroplast - rice chloroplast ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 22-Jun-1999 ACCESSIONS JQ0221; S05101; S03085 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0221 !'##molecule_type DNA !'##residues 1-103 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05101 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-103 ##label HIR !'##cross-references GB:X15901; NID:g11957; PIDN:CAA33994.1; PID:g11980 !'##experimental_source cv. Nihonbare !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1989 REFERENCE S03085 !$#authors Cote, J.C.; Wu, R. !$#journal Nucleic Acids Res. (1989) 17:1780 !$#title Sequence of the chloroplast rps14 gene encoding the !1chloroplast ribosomal protein S14 from rice. !$#cross-references MUID:89160351; PMID:2922301 !$#accession S03085 !'##molecule_type DNA !'##residues 1-103 ##label COT !'##cross-references EMBL:X13208; NID:g11933; PIDN:CAA31596.1; !1PID:g11934 GENETICS !$#gene rps14 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein S14 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 103 #molecular-weight 12254 #checksum 3210 SEQUENCE /// ENTRY R3ZM14 #type complete TITLE ribosomal protein S14, chloroplast - maize chloroplast ORGANISM #formal_name chloroplast Zea mays #common_name maize DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 22-Jun-1999 ACCESSIONS S00640; A27548; S58550 REFERENCE S00640 !$#authors Rodermel, S.; Orlin, P.; Bogorad, L. !$#journal Nucleic Acids Res. (1987) 15:5493 !$#title The transcription termination region between two !1convergently-transcribed photoregulated operons in the maize !1plastid chromosome contains rps14, trnR (UCU) and a putative !1trnfM pseudogene. !$#cross-references MUID:87260027; PMID:3601681 !$#accession S00640 !'##molecule_type DNA !'##residues 1-103 ##label ROD !'##cross-references EMBL:Y00359; NID:g12441; PIDN:CAA68437.1; !1PID:g12442 REFERENCE A27548 !$#authors Srinivasa, B.R.; Subramanian, A.R. !$#journal Biochemistry (1987) 26:3188-3192 !$#title Nucleotide sequence and linkage map position of the gene for !1maize chloroplast ribosomal protein S14. !$#accession A27548 !'##molecule_type DNA !'##residues 1-9,'E',11-39,'F',41-103 ##label SRI !'##cross-references GB:M16559; NID:g342602; PIDN:AAA84487.1; !1PID:g552737 REFERENCE S58531 !$#authors Maier, R.M.; Neckermann, K.; Igloi, G.L.; Koessel, H. !$#journal J. Mol. Biol. (1995) 251:614-628 !$#title Complete sequence of the maize chloroplast genome: gene !1content, hotspots of divergence and fine tuning of genetic !1information by transcript editing. !$#cross-references MUID:95395841; PMID:7666415 !$#accession S58550 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-9,'E',11-103 ##label MAI !'##cross-references EMBL:X86563; NID:g902200; PIDN:CAA60284.1; !1PID:g902220 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1995 GENETICS !$#gene rps14 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein S14 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 103 #molecular-weight 12121 #checksum 2990 SEQUENCE /// ENTRY R3EC15 #type complete TITLE ribosomal protein S15 [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 24-Apr-1984 #sequence_revision 30-Jun-1991 #text_change 01-Mar-2002 ACCESSIONS B26118; S41651; A02735; I54906; A65107; S02369; S13541 REFERENCE A26118 !$#authors Regnier, P.; Grunberg-Manago, M.; Portier, C. !$#journal J. Biol. Chem. (1987) 262:63-68 !$#title Nucleotide sequence of the pnp gene of Escherichia coli !1encoding polynucleotide phosphorylase. Homology of the !1primary structure of the protein with the RNA-binding domain !1of ribosomal protein S1. !$#cross-references MUID:87083499; PMID:2432069 !$#accession B26118 !'##molecule_type DNA !'##residues 1-89 ##label REG !'##cross-references EMBL:J02638; NID:g147744; PIDN:AAA83904.1; !1PID:g147745 REFERENCE S41651 !$#authors Takata, R.; Mukai, T.; Aoyagi, M.; Hori, K. !$#journal Mol. Gen. Genet. (1984) 197:225-229 !$#title Nucleotide sequence of the gene for Escherichia coli !1ribosomal protein S15 (rpsO). !$#cross-references MUID:85110509; PMID:6394953 !$#accession S41651 !'##molecule_type DNA !'##residues 1-89 ##label TAK !'##cross-references EMBL:X01073; NID:g42859; PIDN:CAA25536.1; !1PID:g42860 REFERENCE A02735 !$#authors Morinaga, T.; Funatsu, G.; Funatsu, M.; Wittmann, H.G. !$#journal FEBS Lett. (1976) 64:307-309 !$#title Primary structure of the 16S rRNA binding protein S15 from !1Escherichia coli ribosomes. !$#cross-references MUID:76210888; PMID:776686 !$#accession A02735 !'##molecule_type protein !'##residues 2-45,47-89 ##label MOR REFERENCE I54906 !$#authors Yano, R.; Yura, T. !$#journal J. Bacteriol. (1989) 171:1712-1717 !$#title Suppression of the Escherichia coli rpoH opal mutation by !1ribosomes lacking S15 protein. !$#cross-references MUID:89155483; PMID:2646293 !$#accession I54906 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 86-89 ##label YAN !'##cross-references GB:M24532; NID:g625122 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65107 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-89 ##label BLAT !'##cross-references GB:AE000397; GB:U00096; NID:g2367199; !1PIDN:AAC76199.1; PID:g1789556; UWGP:b3165 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note mass spectrographic analysis of post-translational !1modifications; any acid labile modifications may have been !1missed GENETICS !$#gene rpsO !$#map_position 69 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX small subunit ribosomal proteins: S1 (PIR:R3EC1), S2 !1(PIR:R3EC2), S3 (PIR:R3EC3), S4 (PIR:R3EC4), S5 (PIR:R3EC5), !1S6 (PIR:R3EC6), S7 (PIR:R3EC7K), S8 (PIR:R3EC8), S9 !1(PIR:R3EC9), S10 (PIR:R3EC10), S11 (PIR:R3EC11), S12 !1(PIR:R3EC12), S13 (PIR:R3EC13), S14 (PIR:R3EC14), S15 !1(PIR:R3EC15), S16 (PIR:R3EC16), S17 (PIR:R3EC17), S18 !1(PIR:R3EC18), S19 (PIR:R3EC19), S20/L26 (PIR:R3EC20), S21 !1(PIR:R3EC21), S22 (PIR:C64901) [validated, MUID:99196679] FUNCTION !$#pathway protein biosynthesis CLASSIFICATION #superfamily Escherichia coli ribosomal protein S15; !1eubacterial ribosomal protein S15 homology KEYWORDS protein biosynthesis; ribosome FEATURE !$2-89 #product ribosomal protein S15 #status experimental !8#label MAT\ !$23-89 #domain eubacterial ribosomal protein S15 homology !8#label ES15 SUMMARY #length 89 #molecular-weight 10269 #checksum 5074 SEQUENCE /// ENTRY S38882 #type complete TITLE ribosomal protein S15 - Xenorhabdus luminescens ORGANISM #formal_name Xenorhabdus luminescens DATE 05-Mar-1995 #sequence_revision 19-Apr-1996 #text_change 23-Mar-2001 ACCESSIONS S38882 REFERENCE S38881 !$#authors Clarke, D.J.; Dowds, B.C.A. !$#submission submitted to the EMBL Data Library, November 1993 !$#description Cloning and sequencing of the rspo-pnp operon from !1Photorhabous luminescens. !$#accession S38882 !'##molecule_type DNA !'##residues 1-89 ##label CLA !'##cross-references EMBL:X76069; NID:g442499; PIDN:CAA53670.1; !1PID:g429056 !'##note the source is designated as Photorhabdus luminescens GENETICS !$#gene rpsO; rprA CLASSIFICATION #superfamily Escherichia coli ribosomal protein S15; !1eubacterial ribosomal protein S15 homology KEYWORDS protein biosynthesis; ribosome FEATURE !$2-89 #product ribosomal protein S15 #status predicted !8#label MAT\ !$23-89 #domain eubacterial ribosomal protein S15 homology !8#label ES15 SUMMARY #length 89 #molecular-weight 10112 #checksum 5652 SEQUENCE /// ENTRY H64116 #type complete TITLE ribosomal protein S15 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS H64116; E64125 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession H64116 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-89 ##label TIG1 !'##cross-references GB:U32812; GB:L42023; NID:g1574784; !1PIDN:AAC22973.1; PID:g1574788; TIGR:HI1328 !'##note named as homolog to a protein from Escherichia coli !$#accession E64125 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-89 ##label TIG2 !'##cross-references GB:U32825; GB:L42023; NID:g1574307; !1PIDN:AAC23117.1; PID:g1574309; TIGR:HI1468 !'##note named by homology to a protein from Escherichia coli GENETICS !$#note two copies of this gene are found in the Haemophilus !1influenzae chromosome CLASSIFICATION #superfamily Escherichia coli ribosomal protein S15; !1eubacterial ribosomal protein S15 homology FEATURE !$23-89 #domain eubacterial ribosomal protein S15 homology !8#label ES15 SUMMARY #length 89 #molecular-weight 10196 #checksum 4102 SEQUENCE /// ENTRY R3LV15 #type complete TITLE ribosomal protein S15 - liverwort (Marchantia polymorpha) chloroplast ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 22-Jun-1999 ACCESSIONS A02736; S01521 REFERENCE A00150 !$#authors Ohyama, K. !$#submission submitted to the EMBL Data Library, October 1986 !$#accession A02736 !'##molecule_type DNA !'##residues 1-88 ##label OHY REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features REFERENCE S01512 !$#authors Kohchi, T.; Shirai, H.; Fukuzawa, H.; Sano, T.; Komano, T.; !1Umesono, K.; Inokuchi, H.; Ozeki, H.; Ohyama, K. !$#journal J. Mol. Biol. (1988) 203:353-372 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. IV. Inverted repeat and small single !1copy regions. !$#cross-references MUID:89068688; PMID:3199437 !$#accession S01521 !'##molecule_type DNA !'##residues 1-88 ##label KOH !'##cross-references GB:X04465; GB:Y00686; NID:g11640; PIDN:CAA28141.1; !1PID:g11730 GENETICS !$#gene rps15 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein S15; !1eubacterial ribosomal protein S15 homology KEYWORDS chloroplast; protein biosynthesis; ribosome FEATURE !$18-84 #domain eubacterial ribosomal protein S15 homology !8#label ES15 SUMMARY #length 88 #molecular-weight 10428 #checksum 5550 SEQUENCE /// ENTRY R3NT15 #type complete TITLE ribosomal protein S15 - common tobacco chloroplast ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 17-Feb-1995 ACCESSIONS A02737 REFERENCE A00149 !$#authors Sugiura, M. !$#submission submitted to the EMBL Data Library, August 1986 !$#accession A02737 !'##molecule_type DNA !'##residues 1-87 ##label SUG !'##experimental_source cv. Bright Yellow 4 REFERENCE A38013 !$#authors Shinozaki, K.; Ohme, M.; Tanaka, M.; Wakasugi, T.; !1Hayashida, N.; Matsubayashi, T.; Zaita, N.; Chunwongse, J.; !1Obokata, J.; Yamaguchi-Shinozaki, K.; Ohto, C.; Torazawa, !1K.; Meng, B.Y.; Sugita, M.; Deno, H.; Kamogashira, T.; !1Yamada, K.; Kusuda, J.; Takaiwa, F.; Kato, A.; Tohdoh, N.; !1Shimada, H.; Sugiura, M. !$#journal EMBO J. (1986) 5:2043-2049 !$#title The complete nucleotide sequence of the tobacco chloroplast !1genome: its gene organization and expression. !$#contents annotation; gene organization, sites, features GENETICS !$#gene rps15 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein S15; !1eubacterial ribosomal protein S15 homology KEYWORDS chloroplast; protein biosynthesis; ribosome FEATURE !$17-83 #domain eubacterial ribosomal protein S15 homology !8#label ES15 SUMMARY #length 87 #molecular-weight 10445 #checksum 3085 SEQUENCE /// ENTRY R3RZ15 #type complete TITLE ribosomal protein S15 - rice chloroplast ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jun-2000 ACCESSIONS JQ0284; S05163 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0284 !'##molecule_type DNA !'##residues 1-90 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05163 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-90 ##label HIR !'##cross-references GB:X15901; NID:g11957; PIDN:CAA33948.1; PID:g12045 !'##experimental_source cv. Nihonbare !'##note this sequence was submitted to EMBL, July 1989 GENETICS !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein S15; !1eubacterial ribosomal protein S15 homology KEYWORDS chloroplast; protein biosynthesis; ribosome FEATURE !$23-89 #domain eubacterial ribosomal protein S15 homology !8#label ES15 SUMMARY #length 90 #molecular-weight 10882 #checksum 8645 SEQUENCE /// ENTRY R3ZM15 #type complete TITLE ribosomal protein S15, chloroplast - maize chloroplast ORGANISM #formal_name chloroplast Zea mays #common_name maize DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jun-2000 ACCESSIONS S10153; S58622; S58611 REFERENCE S10153 !$#authors Fitzky, B.; Subramanian, A.R. !$#journal Nucleic Acids Res. (1990) 18:3407 !$#title Nucleotide sequence and map positions of the duplicated gene !1for chloroplast ribosomal protein S15 in Zea mays (maize). !$#cross-references MUID:90287730; PMID:2129550 !$#accession S10153 !'##molecule_type DNA !'##residues 1-90 ##label FIT !'##cross-references EMBL:X52614 !'##genetics GEN1 !'##note it is uncertain whether Met-1 or Met-13 is the initiator REFERENCE S58531 !$#authors Maier, R.M.; Neckermann, K.; Igloi, G.L.; Koessel, H. !$#journal J. Mol. Biol. (1995) 251:614-628 !$#title Complete sequence of the maize chloroplast genome: gene !1content, hotspots of divergence and fine tuning of genetic !1information by transcript editing. !$#cross-references MUID:95395841; PMID:7666415 !$#accession S58622 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 13-18,'Q',20-90 ##label MAI !'##cross-references EMBL:X86563; NID:g902200; PIDN:CAA60345.1; !1PID:g902280 !'##genetics GEN1 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1995 !$#accession S58611 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 13-18,'Q',20-90 ##label MAW !'##cross-references EMBL:X86563; NID:g902200; PIDN:CAA60345.1; !1PID:g902280 !'##genetics GEN2 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1995 GENETICS GEN1 !$#gene rps15 !$#map_position IR(A); IR(II) !$#genome chloroplast GENETICS GEN2 !$#gene rps15 !$#map_position IR(B) !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein S15; !1eubacterial ribosomal protein S15 homology KEYWORDS chloroplast; protein biosynthesis; ribosome FEATURE !$23-89 #domain eubacterial ribosomal protein S15 homology !8#label ES15 SUMMARY #length 90 #molecular-weight 10824 #checksum 8304 SEQUENCE /// ENTRY A34435 #type complete TITLE ribosomal protein S15 - rye chloroplast ORGANISM #formal_name chloroplast Secale cereale #common_name rye DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A34435 REFERENCE A34435 !$#authors Prombona, A.; Subramanian, A.R. !$#journal J. Biol. Chem. (1989) 264:19060-19065 !$#title A new rearrangement of angiosperm chloroplast DNA in rye !1(Secale cereale) involving translocation and duplication of !1the ribosomal rpS15 gene. !$#cross-references MUID:90037033; PMID:2808411 !$#accession A34435 !'##molecule_type DNA !'##residues 1-90 ##label PRO !'##cross-references GB:X14811; NID:g12235; PIDN:CAA32916.1; PID:g12236 GENETICS !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein S15; !1eubacterial ribosomal protein S15 homology KEYWORDS chloroplast; protein biosynthesis; ribosome FEATURE !$23-89 #domain eubacterial ribosomal protein S15 homology !8#label ES15 SUMMARY #length 90 #molecular-weight 10821 #checksum 8487 SEQUENCE /// ENTRY S12797 #type complete TITLE ribosomal protein S15 precursor, mitochondrial - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES mitochondrial ribosomal protein YS28; protein YDR337w ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-Nov-1999 ACCESSIONS S12797; S19233; S70102 REFERENCE S12797 !$#authors Dang, H.; Ellis, S.R. !$#journal Nucleic Acids Res. (1990) 18:6895-6901 !$#title Structural and functional analyses of a yeast mitochondrial !1ribosomal protein homologous to ribosomal protein S15 of !1Escherichia coli. !$#cross-references MUID:91088262; PMID:2263452 !$#accession S12797 !'##molecule_type DNA !'##residues 1-286 ##label DAN1 !'##cross-references EMBL:X55977; NID:g3985; PIDN:CAA39447.1; PID:g3986 !'##experimental_source strain W303-1B !$#accession S19233 !'##molecule_type protein !'##residues 34-53 ##label DAN2 REFERENCE S70098 !$#authors Du, Z. !$#submission submitted to the EMBL Data Library, March 1996 !$#description The sequence of S. cerevisiae cosmid 9651. !$#accession S70102 !'##molecule_type DNA !'##residues 1-286 ##label DUZ !'##cross-references EMBL:U51032; NID:g1230659; PIDN:AAB64773.1; !1PID:g1230664; GSPDB:GN00004; MIPS:YDR337w GENETICS !$#gene SGD:MRPS28; MIPS:YDR337w !'##cross-references SGD:S0002745; MIPS:YDR337w !$#map_position 4R !$#genome nuclear CLASSIFICATION #superfamily Saccharomyces cerevisiae mitochondrial !1ribosomal protein S15; eubacterial ribosomal protein S15 !1homology KEYWORDS mitochondrion; protein biosynthesis; ribosome FEATURE !$1-33 #domain transit peptide (mitochondrion) #status !8experimental #label TNP\ !$34-286 #product ribosomal protein S15 #status experimental !8#label MAT\ !$172-238 #domain eubacterial ribosomal protein S15 homology !8#label ES15 SUMMARY #length 286 #molecular-weight 33057 #checksum 5539 SEQUENCE /// ENTRY R3EC16 #type complete TITLE ribosomal protein S16 [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES DNA-binding protein, 434-specific ORGANISM #formal_name Escherichia coli DATE 12-Aug-1981 #sequence_revision 12-Aug-1981 #text_change 01-Mar-2002 ACCESSIONS S07948; A02738; A61296; D65039 REFERENCE A30380 !$#authors Bystroem, A.S.; Hjalmarsson, K.J.; Wikstroem, P.M.; Bjoerk, !1G.R. !$#journal EMBO J. (1983) 2:899-905 !$#title The nucleotide sequence of an Escherichia coli operon !1containing genes for the tRNA(m1G)methyltransferase, the !1ribosomal proteins S16 and L19 and a 21-K polypeptide. !$#cross-references MUID:84057772; PMID:6357787 !$#accession S07948 !'##molecule_type DNA !'##residues 1-82 ##label BYS !'##cross-references EMBL:X01818; NID:g43141; PIDN:CAA25958.1; !1PID:g43143 REFERENCE A02738 !$#authors Vandekerckhove, J.; Rombauts, W.; Wittmann-Liebold, B. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1977) 358:989-1002 !$#title The complete amino acid sequence of protein S16 from !1Escherichia coli. !$#cross-references MUID:78044788; PMID:336510 !$#accession A02738 !'##molecule_type protein !'##residues 1-82 ##label VAN !'##experimental_source strain K REFERENCE A61296 !$#authors Aono, J.; Iwanaga, S.; Horiuchi, T. !$#journal J. Biochem. (1983) 93:339-347 !$#title New 434-specific DNA binding protein copurified with the 434 !1tof protein from lambdaimm(434)cI dv carrier cells of !1Escherichia coli. !$#cross-references MUID:83186104; PMID:6302096 !$#accession A61296 !'##molecule_type protein !'##residues 1-11 ##label AON REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65039 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-82 ##label BLAT !'##cross-references GB:AE000346; GB:U00096; NID:g2367141; !1PIDN:AAC75658.1; PID:g1788961; UWGP:b2609 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note no post-translational modifications were observed in mass !1spectrographic analysis; any acid labile modifications may !1have been missed GENETICS !$#gene rpsP !$#map_position 57 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX small subunit ribosomal proteins: S1 (PIR:R3EC1), S2 !1(PIR:R3EC2), S3 (PIR:R3EC3), S4 (PIR:R3EC4), S5 (PIR:R3EC5), !1S6 (PIR:R3EC6), S7 (PIR:R3EC7K), S8 (PIR:R3EC8), S9 !1(PIR:R3EC9), S10 (PIR:R3EC10), S11 (PIR:R3EC11), S12 !1(PIR:R3EC12), S13 (PIR:R3EC13), S14 (PIR:R3EC14), S15 !1(PIR:R3EC15), S16 (PIR:R3EC16), S17 (PIR:R3EC17), S18 !1(PIR:R3EC18), S19 (PIR:R3EC19), S20/L26 (PIR:R3EC20), S21 !1(PIR:R3EC21), S22 (PIR:C64901) [validated, MUID:99196679] FUNCTION !$#pathway protein biosynthesis CLASSIFICATION #superfamily Escherichia coli ribosomal protein S16 KEYWORDS DNA binding; protein biosynthesis; ribosome FEATURE !$1-82 #product ribosomal protein S16 #status experimental !8#label MAT SUMMARY #length 82 #molecular-weight 9190 #checksum 8396 SEQUENCE /// ENTRY R3IS16 #type complete TITLE ribosomal protein S16, chloroplast - white mustard chloroplast ORGANISM #formal_name chloroplast Sinapis alba #common_name white mustard DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS A48313; S02721 REFERENCE A48313 !$#authors Neuhaus, H.; Scholz, A.; Link, G. !$#journal Curr. Genet. (1989) 15:63-70 !$#title Structure and expression of a split chloroplast gene from !1mustard (Sinapis alba): ribosomal protein gene rps16 reveals !1unusual transcriptional features and complex RNA maturation. !$#cross-references MUID:89304127; PMID:2545357 !$#accession A48313 !'##molecule_type DNA !'##residues 1-88 ##label NEU !'##cross-references EMBL:X13609; NID:g12216; PIDN:CAA31944.1; !1PID:g12217 !'##note submitted to the EMBL Data Library, November 1988 GENETICS !$#gene rps16 !$#genome chloroplast !$#introns 14/1 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S16 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 88 #molecular-weight 10227 #checksum 4763 SEQUENCE /// ENTRY R3NT16 #type complete TITLE ribosomal protein S16, chloroplast - common tobacco chloroplast ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 30-Jan-1998 ACCESSIONS A02739 REFERENCE A00149 !$#authors Sugiura, M. !$#submission submitted to the EMBL Data Library, August 1986 !$#accession A02739 !'##molecule_type DNA !'##residues 1-85 ##label SUG !'##experimental_source cv. Bright Yellow 4 REFERENCE A38013 !$#authors Shinozaki, K.; Ohme, M.; Tanaka, M.; Wakasugi, T.; !1Hayashida, N.; Matsubayashi, T.; Zaita, N.; Chunwongse, J.; !1Obokata, J.; Yamaguchi-Shinozaki, K.; Ohto, C.; Torazawa, !1K.; Meng, B.Y.; Sugita, M.; Deno, H.; Kamogashira, T.; !1Yamada, K.; Kusuda, J.; Takaiwa, F.; Kato, A.; Tohdoh, N.; !1Shimada, H.; Sugiura, M. !$#journal EMBO J. (1986) 5:2043-2049 !$#title The complete nucleotide sequence of the tobacco chloroplast !1genome: its gene organization and expression. !$#contents annotation; gene organization, sites, features GENETICS !$#gene rps16 !$#genome chloroplast !$#introns 14/1 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S16 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 85 #molecular-weight 9921 #checksum 9200 SEQUENCE /// ENTRY R3ZM16 #type complete TITLE ribosomal protein S16, chloroplast - maize chloroplast ORGANISM #formal_name chloroplast Zea mays #common_name maize DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 22-Jun-1999 ACCESSIONS S19119; S58533 REFERENCE S19119 !$#authors Kanakari, S.; Timmler, G.; von Knoblauch, K.; Subramanian, !1A.R. !$#journal Plant Mol. Biol. (1992) 18:419-422 !$#title Nucleotide sequence, map position and transcript pattern of !1the intron-containing gene for maize chloroplast ribosomal !1protein S16. !$#cross-references MUID:92119265; PMID:1732001 !$#accession S19119 !'##molecule_type DNA !'##residues 1-85 ##label KAN !'##cross-references EMBL:X60823; NID:g14291; PIDN:CAA43215.1; !1PID:g14292 REFERENCE S58531 !$#authors Maier, R.M.; Neckermann, K.; Igloi, G.L.; Koessel, H. !$#journal J. Mol. Biol. (1995) 251:614-628 !$#title Complete sequence of the maize chloroplast genome: gene !1content, hotspots of divergence and fine tuning of genetic !1information by transcript editing. !$#cross-references MUID:95395841; PMID:7666415 !$#accession S58533 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-85 ##label MAI !'##cross-references EMBL:X86563; NID:g902200; PIDN:CAA60267.1; !1PID:g902203 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1995 GENETICS !$#gene rps16 !$#genome chloroplast !$#introns 14/1 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S16 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 85 #molecular-weight 10090 #checksum 7852 SEQUENCE /// ENTRY R3RZ16 #type complete TITLE ribosomal protein S16 - rice chloroplast ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 22-Jun-1999 ACCESSIONS JQ0202; S05082 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0202 !'##molecule_type DNA !'##residues 1-62 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05082 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-62 ##label HIR !'##cross-references GB:X15901; NID:g11957; PIDN:CAA34009.1; PID:g669079 !'##experimental_source cv. Nihonbare !'##note this sequence was submitted to EMBL, July 1989 GENETICS !$#gene rps16 !$#genome chloroplast !$#introns 14/1 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S16 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 62 #molecular-weight 7389 #checksum 6127 SEQUENCE /// ENTRY R3HU11 #type complete TITLE ribosomal protein S11, cytosolic - human ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S02133; S68915 REFERENCE S02133 !$#authors Lott, J.B.; Mackie, G.A. !$#journal Nucleic Acids Res. (1988) 16:1205 !$#title Sequence of a cloned cDNA encoding human ribosomal protein !1S11. !$#cross-references MUID:88143998; PMID:3267208 !$#accession S02133 !'##molecule_type mRNA !'##residues 1-158 ##label LOT !'##cross-references EMBL:X06617; NID:g36143; PIDN:CAA29834.1; !1PID:g36144 REFERENCE S68911 !$#authors Vladimirov, S.N.; Ivanov, A.V.; Karpova, G.G.; Musolyamov, !1A.K.; Egorov, T.A.; Thiede, B.; Wittmann-Liebold, B.; Otto, !1A. !$#journal Eur. J. Biochem. (1996) 239:144-149 !$#title Characterization of the human small-ribosomal-subunit !1proteins by N-terminal and internal sequencing, and mass !1spectrometry. !$#cross-references MUID:96305378; PMID:8706699 !$#accession S68915 !'##molecule_type protein !'##residues 39-45;137-143 ##label VLA GENETICS !$#gene GDB:RPS11 !'##cross-references GDB:118868; OMIM:180471 !$#map_position 19q-19q CLASSIFICATION #superfamily Escherichia coli ribosomal protein S17 KEYWORDS blocked amino end; protein biosynthesis; ribosome SUMMARY #length 158 #molecular-weight 18431 #checksum 965 SEQUENCE /// ENTRY R3RT11 #type complete TITLE ribosomal protein S11, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 21-Jul-2000 ACCESSIONS A22618 REFERENCE A22618 !$#authors Tanaka, T.; Kuwano, Y.; Ishikawa, K.; Ogata, K. !$#journal J. Biol. Chem. (1985) 260:6329-6333 !$#title Nucleotide sequence of cloned cDNA specific for rat !1ribosomal protein S11. !$#cross-references MUID:85207622; PMID:3838984 !$#accession A22618 !'##molecule_type mRNA !'##residues 1-158 ##label TAN !'##cross-references GB:K03250; NID:g206738; PIDN:AAA42076.1; !1PID:g206739 !'##note the protein is designated as ribosomal protein S11 by !1comparison to the composition of ribosomal proteins CLASSIFICATION #superfamily Escherichia coli ribosomal protein S17 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 158 #molecular-weight 18431 #checksum 965 SEQUENCE /// ENTRY JC2499 #type complete TITLE ribosomal protein S11 - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 11-May-2000 ACCESSIONS JC2499; S22606; A61510; I51641 REFERENCE JC2499 !$#authors Annesi, F.; Vespignani, I.; Amaldi, F.; Mariottini, P. !$#journal Biochem. Biophys. Res. Commun. (1994) 203:768-772 !$#title Xenopus laevis ribosomal protein S11: Cloning and sequencing !1of the cDNA and primary structure of the protein. !$#cross-references MUID:94380056; PMID:8093055 !$#accession JC2499 !'##molecule_type mRNA !'##residues 1-158 ##label ANN !'##cross-references EMBL:X78805; NID:g551285; PIDN:CAA55387.1; !1PID:g551286 REFERENCE S22601 !$#authors Loreni, F.; Francesconi, A.; Jappelli, R.; Amaldi, F. !$#journal Nucleic Acids Res. (1992) 20:1859-1863 !$#title Analysis of mRNAs under translational control during Xenopus !1embryogenesis: isolation of new ribosomal protein clones. !$#cross-references MUID:92253404; PMID:1579486 !$#accession S22606 !'##molecule_type mRNA !'##residues 127-158 ##label LOR !'##cross-references EMBL:X64208 REFERENCE A61510 !$#authors Grossberger, D.; Flajnik, M.; Marcuz, A. !$#journal Comp. Biochem. Physiol. B (1991) 98:127-133 !$#title Ribosomal and chromosomal protein cDNA clones of Xenopus !1laevis thymus isolated with differential screening. !$#cross-references MUID:91284580; PMID:2060276 !$#accession A61510 !'##molecule_type mRNA !'##residues 'RHLCLLDGK',29-31,'X',33-38,'X',40,'X',42-52, !1'XHPT';123-138,'L',140-145,'A',147-158 ##label GRO GENETICS !$#gene RPS11 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S17 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 158 #molecular-weight 18421 #checksum 2280 SEQUENCE /// ENTRY R3MX17 #type complete TITLE ribosomal protein S17 - Methanococcus vannielii ORGANISM #formal_name Methanococcus vannielii DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 22-Jun-1999 ACCESSIONS S05613 REFERENCE S05611 !$#authors Auer, J.; Spicker, G.; Boeck, A. !$#journal J. Mol. Biol. (1989) 209:21-36 !$#title Organization and structure of the Methanococcus !1transcriptional unit homologous to the Escherichia coli !1"spectinomycin operon". Implications for the evolutionary !1relationship of 70 S and 80 S ribosomes. !$#cross-references MUID:90040717; PMID:2530355 !$#accession S05613 !'##molecule_type DNA !'##residues 1-109 ##label AUE !'##cross-references EMBL:X16720; NID:g44754; PIDN:CAA34689.1; !1PID:g44757 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S17 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 109 #molecular-weight 12082 #checksum 3617 SEQUENCE /// ENTRY A64358 #type complete TITLE ribosomal protein S17 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 13-Sep-1996 #sequence_revision 04-Oct-1996 #text_change 21-Jul-2000 ACCESSIONS A64358 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession A64358 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-117 ##label BUL !'##cross-references GB:U67497; GB:L77117; NID:g2826284; !1PIDN:AAB98454.1; PID:g1591167; TIGR:MJ0465 GENETICS !$#map_position FOR413128-413481 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S17 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 117 #molecular-weight 13265 #checksum 5176 SEQUENCE /// ENTRY R3HS17 #type complete TITLE ribosomal protein S17 [validated] - Haloarcula marismortui ALTERNATE_NAMES ribosomal protein HmaS17; ribosomal protein HS14 ORGANISM #formal_name Haloarcula marismortui DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 21-Jul-2000 ACCESSIONS S10733; T46796; A29799 REFERENCE S10731 !$#authors Arndt, E. !$#journal FEBS Lett. (1990) 267:193-198 !$#title Nucleotide sequence of four genes encoding ribosomal !1proteins from the 'S10 and spectinomycin' operon equivalent !1region in the archaebacterium Halobacterium marismortui. !$#cross-references MUID:90336772; PMID:2143141 !$#accession S10733 !'##molecule_type DNA !'##residues 1-112 ##label ARN !'##cross-references EMBL:X55311; NID:g43610; PIDN:CAA39017.1; !1PID:g43613 !'##note the source is designated as Halobacterium marismortui !$#accession T46796 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-112 ##label AR2 !'##cross-references EMBL:X55311; NID:g43610; PIDN:CAA39017.1; !1PID:g43613 REFERENCE A29799 !$#authors Kimura, J.; Kimura, M. !$#journal J. Biol. Chem. (1987) 262:12150-12157 !$#title The primary structures of ribosomal proteins S14 and S16 !1from the archaebacterium Halobacterium marismortui. !1Comparison with eubacterial and eukaryotic ribosomal !1proteins. !$#cross-references MUID:87308217; PMID:3305503 !$#accession A29799 !'##molecule_type protein !'##residues 2-88,'S',90-92,'P',94-109,112 ##label KIM CLASSIFICATION #superfamily Escherichia coli ribosomal protein S17 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-112 #product ribosomal protein S17 #status experimental !8#label MAT SUMMARY #length 112 #molecular-weight 12272 #checksum 4245 SEQUENCE /// ENTRY T43825 #type complete TITLE ribosomal protein S17 [validated] - Halobacterium salinarum ALTERNATE_NAMES ribosomal protein HS16 ORGANISM #formal_name Halobacterium salinarum DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 21-Jul-2000 ACCESSIONS T43825; S11616 REFERENCE Z22697 !$#authors Itoh, T. !$#submission submitted to the EMBL Data Library, September 1997 !$#accession T43825 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-109 ##label ITO !'##cross-references EMBL:AB006961; PIDN:BAA22279.1 !'##note the source is designated as Halobacterium halobium REFERENCE S11609 !$#authors Yaguchi, M.; Visentin, L.P.; Zuker, M.; Matheson, A.T.; Roy, !1C.; Strom, A.R. !$#journal Zbl. Bakt. Hyg. I. Abt. Orig. C (1982) 3:200-208 !$#title Amino-terminal sequences of ribosomal proteins from the 30S !1subunit of archaebacterium Halobacterium cutirubrum. !$#accession S11616 !'##molecule_type protein !'##residues 2-14,'C',16-32 ##label YAG !'##note the protein is designated as ribosomal protein HS16 !'##note the source is designated as Halobacterium cutirubrum GENETICS !$#note HhaS17 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S17 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-109 #product ribosomal protein S17 #status experimental !8#label MAT SUMMARY #length 109 #molecular-weight 11973 #checksum 2489 SEQUENCE /// ENTRY R3EC17 #type complete TITLE ribosomal protein S17 [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-May-1979 #sequence_revision 30-Jun-1991 #text_change 01-Mar-2002 ACCESSIONS A37519; A02740; A30421; S59055; B65124; A30420; K23129 REFERENCE A23129 !$#authors Zurawski, G.; Zurawski, S.M. !$#journal Nucleic Acids Res. (1985) 13:4521-4526 !$#title Structure of the Escherichia coli S10 ribosomal protein !1operon. !$#cross-references MUID:85242118; PMID:3892488 !$#accession A37519 !'##molecule_type DNA !'##residues 1-84 ##label ZUR !'##cross-references GB:X02613; NID:g42825; PIDN:CAA26469.1; PID:g42835 REFERENCE A02740 !$#authors Yaguchi, M.; Wittmann, H.G. !$#journal FEBS Lett. (1978) 87:37-40 !$#title The primary structure of protein S17 from the small !1ribosomal subunit of Escherichia coli. !$#cross-references MUID:78127262; PMID:344065 !$#accession A02740 !'##molecule_type protein !'##residues 2-52,54-59,'C',60-84 ##label YAG !'##experimental_source strain K REFERENCE A30421 !$#authors Post, L.E.; Arfsten, A.E.; Reusser, F.; Nomura, M. !$#journal Cell (1978) 15:215-229 !$#title DNA sequences of promoter region for the str and spc !1ribosomal protein operons in E. coli. !$#cross-references MUID:79023059; PMID:151587 !$#accession A30421 !'##molecule_type DNA !'##residues 61-63,'RPC',67-84 ##label POS !'##cross-references GB:V00357; GB:J01686; NID:g43015 REFERENCE S59051 !$#authors Urlaub, H.; Kruft, V.; Bischof, O.; Mueller, E.C.; !1Wittmann-Liebold, B. !$#journal EMBO J. (1995) 14:4578-4588 !$#title Protein-rRNA binding features and their structural and !1functional implications in ribosomes as determined by !1cross-linking studies. !$#cross-references MUID:96003638; PMID:7556101 !$#accession S59055 !'##molecule_type protein !'##residues 20-36 ##label URL REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65124 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-84 ##label BLAT !'##cross-references GB:AE000408; GB:U00096; NID:g1789694; !1PIDN:AAC76336.1; PID:g1789707; UWGP:b3311 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note mass spectrographic analysis of post-translational !1modifications; any acid labile modifications may have been !1missed COMMENT A mutation resulting in the replacement of His-31 confers !1resistance to the antibiotic neamine. GENETICS !$#gene rpsQ !$#map_position 73 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX small subunit ribosomal proteins: S1 (PIR:R3EC1), S2 !1(PIR:R3EC2), S3 (PIR:R3EC3), S4 (PIR:R3EC4), S5 (PIR:R3EC5), !1S6 (PIR:R3EC6), S7 (PIR:R3EC7K), S8 (PIR:R3EC8), S9 !1(PIR:R3EC9), S10 (PIR:R3EC10), S11 (PIR:R3EC11), S12 !1(PIR:R3EC12), S13 (PIR:R3EC13), S14 (PIR:R3EC14), S15 !1(PIR:R3EC15), S16 (PIR:R3EC16), S17 (PIR:R3EC17), S18 !1(PIR:R3EC18), S19 (PIR:R3EC19), S20/L26 (PIR:R3EC20), S21 !1(PIR:R3EC21), S22 (PIR:C64901) [validated, MUID:99196679] FUNCTION !$#pathway protein biosynthesis !$#note binds the 5' end of 16S rRNA CLASSIFICATION #superfamily Escherichia coli ribosomal protein S17 KEYWORDS antibiotic resistance; protein biosynthesis; ribosome; RNA !1binding FEATURE !$2-84 #product ribosomal protein S17 #status experimental !8#label MAT SUMMARY #length 84 #molecular-weight 9704 #checksum 4122 SEQUENCE /// ENTRY E64093 #type complete TITLE ribosomal protein S17 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS E64093 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession E64093 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-85 ##label TIGR !'##cross-references GB:U32761; GB:L42023; NID:g1573780; !1PIDN:AAC22445.1; PID:g1573796; TIGR:HI0786 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S17 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 85 #molecular-weight 9789 #checksum 7129 SEQUENCE /// ENTRY R3YM17 #type complete TITLE ribosomal protein S17 - Mycoplasma capricolum ORGANISM #formal_name Mycoplasma capricolum DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 07-Dec-1999 ACCESSIONS S02840 REFERENCE S02830 !$#authors Ohkubo, S.; Muto, A.; Kawauchi, Y.; Yamao, F.; Osawa, S. !$#journal Mol. Gen. Genet. (1987) 210:314-322 !$#title The ribosomal protein gene cluster of Mycoplasma capricolum. !$#cross-references MUID:88142549; PMID:3481422 !$#accession S02840 !'##molecule_type DNA !'##residues 1-85 ##label OHK !'##cross-references EMBL:X06414; NID:g44207; PIDN:CAA29713.1; !1PID:g44218 GENETICS !$#gene rps17 !$#genetic_code SGC3 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S17 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 85 #molecular-weight 10051 #checksum 9469 SEQUENCE /// ENTRY R3BS17 #type complete TITLE ribosomal protein S17 - Bacillus subtilis ALTERNATE_NAMES ribosomal protein BS16 ORGANISM #formal_name Bacillus subtilis DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jun-2000 ACCESSIONS S05991; S11367; H69700 REFERENCE S05989 !$#authors Henkin, T.M.; Moon, S.H.; Mattheakis, L.C.; Nomura, M. !$#journal Nucleic Acids Res. (1989) 17:7469-7486 !$#title Cloning and analysis of the spc ribosomal protein operon of !1Bacillus subtilis: comparison with the spc operon of !1Escherichia coli. !$#cross-references MUID:90016806; PMID:2508062 !$#accession S05991 !'##molecule_type DNA !'##residues 1-87 ##label HEN !'##cross-references EMBL:X15664; NID:g40146; PIDN:CAA33700.1; !1PID:g40149 REFERENCE S09561 !$#authors Higo, K.I.; Otaka, E.; Osawa, S. !$#journal Mol. Gen. Genet. (1982) 185:239-244 !$#title Purification and characterization of 30S ribosomal proteins !1from Bacillus subtilis: correlation to Escherichia coli 30S !1proteins. !$#cross-references MUID:82219212; PMID:6806564 !$#accession S11367 !'##molecule_type protein !'##residues 2-23,'G',25-38 ##label HIG REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69700 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-87 ##label KUN !'##cross-references GB:Z99104; GB:AL009126; NID:g2632267; !1PIDN:CAB11901.1; PID:g2632392 !'##experimental_source strain 168 GENETICS !$#gene rpsQ CLASSIFICATION #superfamily Escherichia coli ribosomal protein S17 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-87 #product ribosomal protein S17 #status experimental !8#label MAT SUMMARY #length 87 #molecular-weight 10199 #checksum 2699 SEQUENCE /// ENTRY R3KT17 #type complete TITLE ribosomal protein S17, cyanelle - Cyanophora paradoxa cyanelle ORGANISM #formal_name cyanelle Cyanophora paradoxa DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 21-Jan-2000 ACCESSIONS S12214; T06882 REFERENCE S12211 !$#authors Michalowski, C.B.; Pfanzagl, B.; Loeffelhardt, W.; Bohnert, !1H.J. !$#journal Mol. Gen. Genet. (1990) 224:222-231 !$#title The cyanelle S10 spc ribosomal protein gene operon from !1Cyanophora paradoxa. !$#cross-references MUID:91117189; PMID:2126059 !$#accession S12214 !'##molecule_type DNA !'##residues 1-88 ##label MIC !'##cross-references GB:M30487; NID:g336645; PIDN:AAA63623.1; !1PID:g336649 !'##experimental_source strain LB555 UTEX REFERENCE Z15840 !$#authors Stirewalt, V.L.; Michalowski, C.B.; Luffelhardt, W.; !1Bohnert, H.J.; Bryant, D.A. !$#submission submitted to the EMBL Data Library, July 1995 !$#description Nucleotide sequence of the cyanelle genome from Cyanophora !1paradoxa. !$#accession T06882 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-88 ##label STI !'##cross-references EMBL:U30821; NID:g1016083; PIDN:AAA81225.1; !1PID:g1016138 !'##experimental_source strain Pringsheim LB555 GENETICS !$#gene rps17 !$#genome cyanelle CLASSIFICATION #superfamily Escherichia coli ribosomal protein S17 KEYWORDS cyanelle; protein biosynthesis; ribosome SUMMARY #length 88 #molecular-weight 10136 #checksum 5420 SEQUENCE /// ENTRY R3MU17 #type complete TITLE ribosomal protein S17 precursor, chloroplast - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 22-Jun-1999 ACCESSIONS S20942; A35542 REFERENCE S20942 !$#authors Thompson, M.D.; Jacks, C.M.; Lenvik, T.R.; Gantt, J.S. !$#journal Plant Mol. Biol. (1992) 18:931-944 !$#title Characterization of rps17, rpl9 and rpl15: three !1nucleus-encoded plastid ribosomal protein genes. !$#cross-references MUID:92256814; PMID:1581570 !$#accession S20942 !'##molecule_type DNA !'##residues 1-149 ##label THO !'##cross-references EMBL:Z11151; NID:g16502; PIDN:CAA77502.1; !1PID:g16503 REFERENCE A35542 !$#authors Gantt, J.S.; Thompson, M.D. !$#journal J. Biol. Chem. (1990) 265:2763-2767 !$#title Plant cytosolic ribosomal protein S11 and chloroplast !1ribosomal protein CS17. Their primary structures and !1evolutionary relationships. !$#cross-references MUID:90153903; PMID:2406240 !$#accession A35542 !'##molecule_type mRNA !'##residues 1-149 ##label GAN !'##cross-references GB:J05215 !'##note the authors translated the codon GCC for residue 133 as Arg GENETICS !$#gene rps17 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S17 KEYWORDS chloroplast; ribosome SUMMARY #length 149 #molecular-weight 16282 #checksum 3757 SEQUENCE /// ENTRY C42645 #type complete TITLE ribosomal protein S17 - Chlamydia trachomatis ORGANISM #formal_name Chlamydia trachomatis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C42645; E71506 REFERENCE A42645 !$#authors Kaul, R.; Gray, G.J.; Koehncke, N.R.; Gu, L.J. !$#journal J. Bacteriol. (1992) 174:1205-1212 !$#title Cloning and sequence analysis of the Chlamydia trachomatis !1spc ribosomal protein gene cluster. !$#cross-references MUID:92138612; PMID:1735714 !$#accession C42645 !'##status preliminary !'##molecule_type DNA !'##residues 1-83 ##label KAU !'##cross-references GB:M80325; NID:g144617; PIDN:AAA23171.1; !1PID:g144620 !'##note sequence extracted from NCBI backbone (NCBIN:79464, !1NCBIP:79467) REFERENCE A71570 !$#authors Stephens, R.S.; Kalman, S.; Lammel, C.J.; Fan, J.; Marathe, !1R.; Aravind, L.; Mitchell, W.P.; Olinger, L.; Tatusov, R.L.; !1Zhao, Q.; Koonin, E.V.; Davis, R.W. !$#journal Science (1998) 282:754-759 !$#title Genome sequence of an obligate intracellular pathogen of !1humans: Chlamydia trachomatis. !$#cross-references MUID:99000809; PMID:9784136 !$#accession E71506 !'##molecule_type DNA !'##residues 1-83 ##label ARN !'##cross-references GB:AE001323; GB:AE001273; NID:g3328931; !1PIDN:AAC68120.1; PID:g3328956 !'##experimental_source serotype D, strain UW-3/Cx GENETICS !$#gene rs17 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S17 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 83 #molecular-weight 9645 #checksum 8800 SEQUENCE /// ENTRY S15436 #type complete TITLE ribosomal protein S17 - Thermus aquaticus ORGANISM #formal_name Thermus aquaticus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S15436; S51068; S52409 REFERENCE S15436 !$#authors Jahn, O.; Hartmann, R.K.; Erdmann, V.A. !$#journal Eur. J. Biochem. (1991) 197:733-740 !$#title Analysis of the spc ribosomal protein operon of Thermus !1aquaticus. !$#cross-references MUID:91231015; PMID:2029902 !$#accession S15436 !'##molecule_type DNA !'##residues 1-105 ##label JAH !'##cross-references EMBL:X56552; NID:g48102; PIDN:CAA39893.1; !1PID:g48103 REFERENCE S51053 !$#authors Tsiboli, P.; Herfurth, E.; Choli, T. !$#journal Eur. J. Biochem. (1994) 226:169-177 !$#title Purification and characterization of the 30S ribosomal !1proteins from the bacterium Thermus thermophilus. !$#cross-references MUID:95045586; PMID:7957245 !$#accession S51068 !'##molecule_type protein !'##residues 2-14 ##label TSI !'##note the source is designated as Thermus thermophilus REFERENCE S52409 !$#authors Vysotskaya, V.S.; Shcherbakov, D.V.; Garber, M.B. !$#submission submitted to the EMBL Data Library, September 1994 !$#description Cloning and analysis of the spc ribosomal protein operon of !1Thermus thermophilus. !$#accession S52409 !'##molecule_type DNA !'##residues 1-49,'K',51-52,'L',54-61,'S',63-78,'S',80-81,'M',83-89,'I', !191-95,'Q',97-105 ##label VYS !'##cross-references EMBL:Z36971; NID:g673502; PIDN:CAA85419.1; !1PID:g673503 !'##note the source is designated as Thermus thermophilus CLASSIFICATION #superfamily Escherichia coli ribosomal protein S17 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 105 #molecular-weight 12247 #checksum 9534 SEQUENCE /// ENTRY C72249 #type complete TITLE ribosomal protein S17 - Thermotoga maritima (strain MSB8) ORGANISM #formal_name Thermotoga maritima DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C72249; S40197 REFERENCE A72200 !$#authors Nelson, K.E.; Clayton, R.A.; Gill, S.R.; Gwinn, M.L.; !1Dodson, R.J.; Haft, D.H.; Hickey, E.K.; Peterson, J.D.; !1Nelson, W.C.; Ketchum, K.A.; McDonald, L.; Utterback, T.R.; !1Malek, J.A.; Linher, K.D.; Garrett, M.M.; Stewart, A.M.; !1Cotton, M.D.; Pratt, M.S.; Phillips, C.A.; Richardson, D.; !1Heidelberg, J.; Sutton, G.G.; Fleischmann, R.D.; White, O.; !1Salzberg, S.L.; Smith, H.O.; Venter, J.C.; Fraser, C.M. !$#journal Nature (1999) 399:323-329 !$#title Evidence for lateral gene transfer between Archaea and !1Bacteria from genome sequence of Thermotoga maritima. !$#cross-references MUID:99287316; PMID:10360571 !$#accession C72249 !'##molecule_type DNA !'##residues 1-107 ##label ARN !'##cross-references GB:AE001798; GB:AE000512; NID:g4982033; !1PIDN:AAD36557.1; PID:g4982055; TIGR:TM1491 !'##experimental_source strain MSB8 REFERENCE S37489 !$#authors Sanangelantoni, A.; Tiboni, O. !$#submission submitted to the EMBL Data Library, February 1993 !$#accession S40197 !'##molecule_type DNA !'##residues 1-67,'A',69-107 ##label SAN !'##cross-references EMBL:Z21677; NID:g437921; PID:g437932 GENETICS !$#gene rpsQ; TM1491 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S17 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 107 #molecular-weight 12598 #checksum 3145 SEQUENCE /// ENTRY R3EC18 #type complete TITLE ribosomal protein S18 [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 24-Apr-1984 #sequence_revision 24-May-1996 #text_change 01-Mar-2002 ACCESSIONS S56427; A02741; E65231 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56427 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-75 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97098.1; !1PID:g537043 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A02741 !$#authors Yaguchi, M. !$#journal FEBS Lett. (1975) 59:217-220 !$#title Primary structure of protein S18 from the small Escherichia !1coli ribosomal subunit. !$#cross-references MUID:76210737; PMID:776663 !$#accession A02741 !'##molecule_type protein !'##residues 2-15,'Q',17-75 ##label YAG !'##experimental_source strain K REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65231 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-75 ##label BLAT !'##cross-references GB:AE000491; GB:U00096; NID:g2367357; !1PIDN:AAC77159.1; PID:g1790646; UWGP:b4202 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note mass spectrographic analysis of post-translational !1modifications; any acid labile modifications may have been !1missed COMMENT The amino end is acetylated by ribosomal-protein-alanine !1N-acetyltransferase (EC 2.3.1.128) rimI, see PIR:D65252. GENETICS !$#gene rpsR !$#map_position 96 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX small subunit ribosomal proteins: S1 (PIR:R3EC1), S2 !1(PIR:R3EC2), S3 (PIR:R3EC3), S4 (PIR:R3EC4), S5 (PIR:R3EC5), !1S6 (PIR:R3EC6), S7 (PIR:R3EC7K), S8 (PIR:R3EC8), S9 !1(PIR:R3EC9), S10 (PIR:R3EC10), S11 (PIR:R3EC11), S12 !1(PIR:R3EC12), S13 (PIR:R3EC13), S14 (PIR:R3EC14), S15 !1(PIR:R3EC15), S16 (PIR:R3EC16), S17 (PIR:R3EC17), S18 !1(PIR:R3EC18), S19 (PIR:R3EC19), S20/L26 (PIR:R3EC20), S21 !1(PIR:R3EC21), S22 (PIR:C64901) [validated, MUID:99196679] FUNCTION !$#description may be involved in aminoacyl-transfer RNA binding; located !1at the decoding site of mRNA !$#pathway protein biosynthesis CLASSIFICATION #superfamily Escherichia coli ribosomal protein S18 KEYWORDS acetylated amino end; protein biosynthesis; ribosome FEATURE !$2-75 #product ribosomal protein S18 #status experimental !8#label MAT\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental SUMMARY #length 75 #molecular-weight 8986 #checksum 1345 SEQUENCE /// ENTRY R3BS18 #type complete TITLE ribosomal protein S18 - Bacillus stearothermophilus ORGANISM #formal_name Bacillus stearothermophilus DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 30-Jun-1993 ACCESSIONS S03556 REFERENCE S03556 !$#authors McDougall, J.; Choli, T.; Kruft, V.; Kapp, U.; !1Wittmann-Liebold, B. !$#journal FEBS Lett. (1989) 245:253-260 !$#title The complete amino acid sequence of ribosomal protein S18 !1from the moderate thermophile Bacillus stearothermophilus. !$#cross-references MUID:89171319; PMID:2647521 !$#accession S03556 !'##molecule_type protein !'##residues 1-77 ##label MCD CLASSIFICATION #superfamily Escherichia coli ribosomal protein S18 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 77 #molecular-weight 8837 #checksum 3698 SEQUENCE /// ENTRY R3KT18 #type complete TITLE ribosomal protein S18 - Cyanophora paradoxa cyanelle ORGANISM #formal_name cyanelle Cyanophora paradoxa DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S08230; T06891 REFERENCE S08230 !$#authors Evrard, J.L.; Kuntz, M.; Weil, J.H. !$#journal J. Mol. Evol. (1990) 30:16-25 !$#title The nucleotide sequence of five ribosomal protein genes from !1the cyanelles of Cyanophora paradoxa: implications !1concerning the phylogenetic relationship between cyanelles !1and chloroplasts. !$#cross-references MUID:90189174; PMID:2107321 !$#accession S08230 !'##molecule_type DNA !'##residues 1-71 ##label EVR !'##cross-references EMBL:X17498; NID:g11399; PIDN:CAA35533.1; !1PID:g11400 REFERENCE Z15840 !$#authors Stirewalt, V.L.; Michalowski, C.B.; Luffelhardt, W.; !1Bohnert, H.J.; Bryant, D.A. !$#submission submitted to the EMBL Data Library, July 1995 !$#description Nucleotide sequence of the cyanelle genome from Cyanophora !1paradoxa. !$#accession T06891 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-71 ##label STI !'##cross-references EMBL:U30821; NID:g1016083; PIDN:AAA81234.1; !1PID:g1016147 !'##experimental_source strain Pringsheim LB555 GENETICS !$#gene rps18 !$#genome cyanelle CLASSIFICATION #superfamily Escherichia coli ribosomal protein S18 KEYWORDS cyanelle; protein biosynthesis; ribosome SUMMARY #length 71 #molecular-weight 8207 #checksum 5883 SEQUENCE /// ENTRY R3LV18 #type complete TITLE ribosomal protein S18, chloroplast - liverwort (Marchantia polymorpha) chloroplast ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 22-Jun-1999 ACCESSIONS A02742; S01544 REFERENCE A00150 !$#authors Ohyama, K. !$#submission submitted to the EMBL Data Library, October 1986 !$#accession A02742 !'##molecule_type DNA !'##residues 1-75 ##label OHY REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features REFERENCE S01529 !$#authors Fukuzawa, H.; Kohchi, T.; Sano, T.; Shirai, H.; Umesono, K.; !1Inokuchi, H.; Ozeki, H.; Ohyama, K. !$#journal J. Mol. Biol. (1988) 203:333-351 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. III. Gene organization of the large !1single copy region from rbcL to trnI(CAU). !$#cross-references MUID:89068687; PMID:3199436 !$#accession S01544 !'##molecule_type DNA !'##residues 1-75 ##label FUK !'##cross-references GB:X04465; GB:Y00686; NID:g11640; PIDN:CAA28107.1; !1PID:g11695 GENETICS !$#gene rps18 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein S18 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 75 #molecular-weight 8879 #checksum 2410 SEQUENCE /// ENTRY R3NT18 #type complete TITLE ribosomal protein S18 - common tobacco chloroplast ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 17-Feb-1995 ACCESSIONS A02743 REFERENCE A00149 !$#authors Sugiura, M. !$#submission submitted to the EMBL Data Library, August 1986 !$#accession A02743 !'##molecule_type DNA !'##residues 1-101 ##label SUG !'##experimental_source cv. Bright Yellow 4 REFERENCE A38013 !$#authors Shinozaki, K.; Ohme, M.; Tanaka, M.; Wakasugi, T.; !1Hayashida, N.; Matsubayashi, T.; Zaita, N.; Chunwongse, J.; !1Obokata, J.; Yamaguchi-Shinozaki, K.; Ohto, C.; Torazawa, !1K.; Meng, B.Y.; Sugita, M.; Deno, H.; Kamogashira, T.; !1Yamada, K.; Kusuda, J.; Takaiwa, F.; Kato, A.; Tohdoh, N.; !1Shimada, H.; Sugiura, M. !$#journal EMBO J. (1986) 5:2043-2049 !$#title The complete nucleotide sequence of the tobacco chloroplast !1genome: its gene organization and expression. !$#contents annotation; gene organization, sites, features GENETICS !$#gene rps18 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein S18 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 101 #molecular-weight 12052 #checksum 4194 SEQUENCE /// ENTRY R3RZ18 #type complete TITLE ribosomal protein S18 - rice chloroplast ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 22-Jun-1999 ACCESSIONS JQ0248; S05128 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0248 !'##molecule_type DNA !'##residues 1-163 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05128 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-163 ##label HIR !'##cross-references GB:X15901; NID:g11957; PIDN:CAA33970.1; PID:g12009 !'##experimental_source cv. Nihonbare !'##note this sequence was submitted to EMBL, July 1989 GENETICS !$#gene rps18 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein S18 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 163 #molecular-weight 19643 #checksum 519 SEQUENCE /// ENTRY R3ZM18 #type complete TITLE ribosomal protein S18, chloroplast - maize chloroplast ORGANISM #formal_name chloroplast Zea mays #common_name maize DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 22-Jun-1999 ACCESSIONS S13612; S58573 REFERENCE S13611 !$#authors Wegloehner, W.; Subramanian, A.R. !$#journal FEBS Lett. (1991) 279:193-197 !$#title A heptapeptide repeat contributes to the unusual length of !1chloroplast ribosomal protein S18. Nucleotide sequence and !1map position of the rpl33-rps18 gene cluster in maize. !$#cross-references MUID:91160712; PMID:1840527 !$#accession S13612 !'##molecule_type DNA !'##residues 1-170 ##label WEG !'##cross-references EMBL:X56673; NID:g12448; PIDN:CAA39996.1; !1PID:g12450 REFERENCE S58531 !$#authors Maier, R.M.; Neckermann, K.; Igloi, G.L.; Koessel, H. !$#journal J. Mol. Biol. (1995) 251:614-628 !$#title Complete sequence of the maize chloroplast genome: gene !1content, hotspots of divergence and fine tuning of genetic !1information by transcript editing. !$#cross-references MUID:95395841; PMID:7666415 !$#accession S58573 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-170 ##label MAI !'##cross-references EMBL:X86563; NID:g902200; PIDN:CAA60307.1; !1PID:g902243 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1995 GENETICS !$#gene rps18 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein S18 KEYWORDS chloroplast; protein biosynthesis; ribosome; tandem repeat FEATURE !$4-52 #region 7-residue repeats SUMMARY #length 170 #molecular-weight 20599 #checksum 416 SEQUENCE /// ENTRY R3EG18 #type complete TITLE ribosomal protein S18 - Euglena gracilis chloroplast ORGANISM #formal_name chloroplast Euglena gracilis DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 22-Jun-1999 ACCESSIONS S29802; S33682; S34537; S34904; S26094 REFERENCE S29797 !$#authors Drager, R.G.; Hallick, R.B. !$#journal Curr. Genet. (1993) 23:271-280 !$#title A novel Euglena gracilis chloroplast operon encoding four !1ATP synthase subunits and two ribosomal proteins contains 17 !1introns. !$#cross-references MUID:93169691; PMID:8435857 !$#accession S29802 !'##molecule_type DNA !'##residues 1-64 ##label DRA1 !'##cross-references EMBL:Z11874; NID:g14353; PIDN:CAA77933.1; !1PID:g14383 REFERENCE S33682 !$#authors Drager, R.G.; Hallick, R.B. !$#journal Nucleic Acids Res. (1993) 21:2389-2394 !$#title A complex twintron is excised as four individual introns. !$#cross-references MUID:93281385; PMID:7685079 !$#accession S33682 !'##molecule_type DNA !'##residues 1-64 ##label DRA2 !'##cross-references EMBL:Z11874; NID:g14353; PIDN:CAA77933.1; !1PID:g14383 REFERENCE S34494 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.; Monfort, !1A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#submission submitted to the EMBL Data Library, January 1993 !$#description The complete sequence of the Euglena gracilis chloroplast !1genome (tentative). !$#accession S34537 !'##molecule_type DNA !'##residues 1-64 ##label HAL1 !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50116.1; !1PID:g415772 REFERENCE S34862 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.R.; !1Monfort, A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#journal Nucleic Acids Res. (1993) 21:3537-3544 !$#title Complete sequence of Euglena gracilis chloroplast DNA. !$#cross-references MUID:93347989; PMID:8346031 !$#accession S34904 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-64 ##label HAL2 !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50116.1; !1PID:g415772 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1993 GENETICS !$#gene rps18 !$#genome chloroplast !$#introns 3/1; 46/3 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S18 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 64 #molecular-weight 7809 #checksum 554 SEQUENCE /// ENTRY R3RT19 #type complete TITLE ribosomal protein S19, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 21-Jul-2000 ACCESSIONS A43770; S10392 REFERENCE A43770 !$#authors Suzuki, K.; Olvera, J.; Wool, I.G. !$#journal Biochimie (1990) 72:299-302 !$#title The primary structure of rat ribosomal protein S19. !$#cross-references MUID:90344931; PMID:2116918 !$#accession A43770 !'##molecule_type mRNA !'##residues 1-145 ##label SUZ !'##cross-references EMBL:X51707; NID:g57715; PIDN:CAA36003.1; !1PID:g57716 !'##note part of this sequence was confirmed by protein sequencing !'##note the protein is designated as ribosomal protein S19 CLASSIFICATION #superfamily rat ribosomal protein S19 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-145 #product ribosomal protein S19 #status experimental !8#label MAT SUMMARY #length 145 #molecular-weight 16085 #checksum 555 SEQUENCE /// ENTRY R3BY9E #type complete TITLE ribosomal protein S19.e.A, cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein O0559; protein YOL121c; ribosomal protein rp55; ribosomal protein YS16.A ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Jun-2000 ACCESSIONS S05868; S11580; S66818; S72022 REFERENCE S05867 !$#authors Molenaar, C.M.T.; Woudt, L.P.; Jansen, A.E.M.; Mager, W.H.; !1Planta, R.J.; Donovan, D.M.; Pearson, N.J. !$#journal Nucleic Acids Res. (1984) 12:7345-7358 !$#title Structure and organization of two linked ribosomal protein !1genes in yeast. !$#cross-references MUID:85037916; PMID:6387623 !$#accession S05868 !'##molecule_type DNA !'##residues 1-144 ##label MOL !'##cross-references EMBL:X02635; NID:g4367; PIDN:CAA26482.1; PID:g4369 REFERENCE S11575 !$#authors Otaka, E.; Higo, K.; Osawa, S. !$#journal Biochemistry (1982) 21:4545-4550 !$#title Isolation of seventeen proteins and amino-terminal amino !1acid sequences of eight proteins from cytoplasmic ribosomes !1of yeast. !$#cross-references MUID:83048950; PMID:6814480 !$#accession S11580 !'##molecule_type protein !'##residues 2-48,'B',50 ##label OTA !'##note 2-Ala was also found REFERENCE S66814 !$#authors Arino, J.; Casamayor, A.; Gamo, F.J.; Gancedo, C.; Lafuente, !1M.J.; Aldea, M.; Casas, C.; Herrero, E. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S66818 !'##molecule_type DNA !'##residues 1-144 ##label ARI !'##cross-references EMBL:Z74863; NID:g1419998; PIDN:CAA99140.1; !1PID:g1419999; GSPDB:GN00015; MIPS:YOL121c !'##experimental_source strain S288C REFERENCE S72019 !$#authors Lafuente, M.J.; Gamo, F.J.; Gancedo, C. !$#journal Yeast (1996) 12:1041-1045 !$#title DNA sequence analysis of a 10 624 bp fragment of the left !1arm of chromosome XV from Saccharomyces cerevisiae reveals a !1RNA binding protein, a mitochondrial protein, two ribosomal !1proteins and two new open reading frames. !$#cross-references MUID:97051591; PMID:8896268 !$#accession S72022 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-144 ##label LAF !'##cross-references EMBL:X95258; NID:g1550720; PIDN:CAA64549.1; !1PID:g1550724 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1996 GENETICS !$#gene SGD:RPS16B; RP55A; MIPS:YOL121c !'##cross-references MIPS:YOL121c; SGD:S0005481 !$#map_position 15L !$#introns 7/2 CLASSIFICATION #superfamily rat ribosomal protein S19 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-144 #product ribosomal protein S19.e #status experimental !8#label MAT SUMMARY #length 144 #molecular-weight 15917 #checksum 7615 SEQUENCE /// ENTRY R3HS12 #type complete TITLE ribosomal protein S19.eR [validated] - Haloarcula marismortui ALTERNATE_NAMES ribosomal protein E1.3; ribosomal protein HS12 ORGANISM #formal_name Haloarcula marismortui DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 04-Feb-2000 ACCESSIONS S00183; C24304 REFERENCE S00182 !$#authors Kimura, J.; Arndt, E.; Kimura, M. !$#journal FEBS Lett. (1987) 224:65-70 !$#title Primary structures of three highly acidic ribosomal proteins !1S6, S12 and S15 from the archaebacterium Halobacterium !1marismortui. !$#cross-references MUID:88055606; PMID:3315748 !$#accession S00183 !'##molecule_type protein !'##residues 1-147 ##label KIM !'##note the source is designated as Halobacterium marismortui !'##note the protein is designated as ribosomal protein S12 REFERENCE A24304 !$#authors Shoham, M.; Dijk, J.; Reinhardt, R.; Wittmann-Liebold, B. !$#journal FEBS Lett. (1986) 204:323-330 !$#title Purification and characterization of ribosomal proteins from !1the 30 S subunit of the extreme halophile Halobacterium !1marismortui. !$#accession C24304 !'##molecule_type protein !'##residues 1-11,'E',13-14,'I',16-18,'I',20-21 ##label SHO !'##note the source is designated as Halobacterium marismortui CLASSIFICATION #superfamily rat ribosomal protein S19 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 147 #molecular-weight 16438 #checksum 4777 SEQUENCE /// ENTRY R3EC19 #type complete TITLE ribosomal protein S19 [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-May-1979 #sequence_revision 30-Jun-1991 #text_change 01-Mar-2002 ACCESSIONS F23129; A02744; G65124 REFERENCE A23129 !$#authors Zurawski, G.; Zurawski, S.M. !$#journal Nucleic Acids Res. (1985) 13:4521-4526 !$#title Structure of the Escherichia coli S10 ribosomal protein !1operon. !$#cross-references MUID:85242118; PMID:3892488 !$#accession F23129 !'##molecule_type DNA !'##residues 1-92 ##label ZUR !'##cross-references GB:X02613; NID:g42825; PIDN:CAA26464.1; PID:g42830 REFERENCE A02744 !$#authors Yaguchi, M.; Wittmann, H.G. !$#journal FEBS Lett. (1978) 88:227-230 !$#title Primary structure of protein S19 from the small ribosomal !1subunit of Escherichia coli. !$#cross-references MUID:78169207; PMID:348496 !$#accession A02744 !'##molecule_type protein !'##residues 2-35,37-42,'DR',44-85,'N',87-92 ##label YAG !'##experimental_source strain K REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65124 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-92 ##label BLAT !'##cross-references GB:AE000408; GB:U00096; NID:g1789694; !1PIDN:AAC76341.1; PID:g1789712; UWGP:b3316 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note mass spectrographic analysis of post-translational !1modifications; any acid labile modifications may have been !1missed GENETICS !$#gene rpsS !$#map_position 73 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX small subunit ribosomal proteins: S1 (PIR:R3EC1), S2 !1(PIR:R3EC2), S3 (PIR:R3EC3), S4 (PIR:R3EC4), S5 (PIR:R3EC5), !1S6 (PIR:R3EC6), S7 (PIR:R3EC7K), S8 (PIR:R3EC8), S9 !1(PIR:R3EC9), S10 (PIR:R3EC10), S11 (PIR:R3EC11), S12 !1(PIR:R3EC12), S13 (PIR:R3EC13), S14 (PIR:R3EC14), S15 !1(PIR:R3EC15), S16 (PIR:R3EC16), S17 (PIR:R3EC17), S18 !1(PIR:R3EC18), S19 (PIR:R3EC19), S20/L26 (PIR:R3EC20), S21 !1(PIR:R3EC21), S22 (PIR:C64901) [validated, MUID:99196679] FUNCTION !$#pathway protein biosynthesis !$#note with S13 forms a complex that strongly binds 16S rRNA CLASSIFICATION #superfamily Escherichia coli ribosomal protein S19 KEYWORDS protein biosynthesis; ribosome; RNA binding FEATURE !$2-92 #product ribosomal protein S19 #status experimental !8#label MAT SUMMARY #length 92 #molecular-weight 10430 #checksum 3788 SEQUENCE /// ENTRY R3YM19 #type complete TITLE ribosomal protein S19 - Mycoplasma capricolum ORGANISM #formal_name Mycoplasma capricolum DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 07-Dec-1999 ACCESSIONS S02835 REFERENCE S02830 !$#authors Ohkubo, S.; Muto, A.; Kawauchi, Y.; Yamao, F.; Osawa, S. !$#journal Mol. Gen. Genet. (1987) 210:314-322 !$#title The ribosomal protein gene cluster of Mycoplasma capricolum. !$#cross-references MUID:88142549; PMID:3481422 !$#accession S02835 !'##molecule_type DNA !'##residues 1-88 ##label OHK !'##cross-references EMBL:X06414; NID:g44207; PIDN:CAA29708.1; !1PID:g44213 GENETICS !$#gene rps19 !$#genetic_code SGC3 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S19 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 88 #molecular-weight 9903 #checksum 3005 SEQUENCE /// ENTRY R3BS19 #type complete TITLE ribosomal protein S19 - Bacillus stearothermophilus ORGANISM #formal_name Bacillus stearothermophilus DATE 31-Dec-1990 #sequence_revision 30-Sep-1991 #text_change 22-Jun-1999 ACCESSIONS S10611; S00233 REFERENCE S10610 !$#authors Kroemer, W.J.; Hatakeyama, T.; Kimura, M. !$#journal Biol. Chem. Hoppe-Seyler (1990) 371:631-636 !$#title Nucleotide sequences of Bacillus stearothermophilus !1ribosomal protein genes: part of the ribosomal S10 operon. !$#cross-references MUID:91025633; PMID:2222862 !$#accession S10611 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-92 ##label KRO !'##cross-references GB:X54994; NID:g40104; PIDN:CAA38738.1; PID:g40106 REFERENCE S00233 !$#authors Hirano, H.; Eckart, K.; Kimura, M.; Wittmann-Liebold, B. !$#journal Eur. J. Biochem. (1987) 170:149-157 !$#title Semi-preparative HPLC purification of ribosomal proteins !1from Bacillus stearothermophilus and sequence determination !1of the highly conserved protein S19. !$#cross-references MUID:88082810; PMID:3691516 !$#accession S00233 !'##molecule_type protein !'##residues 2-10,'S',12-31,'R',33,'D',35-46,'R',48-51,'HN',54-77,'R', !179-89,'K',91,'K' ##label HIR !'##note this sequence has been revised in reference S10610 GENETICS !$#gene rps19 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S19 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-92 #product ribosomal protein S19 #status experimental !8#label MAT SUMMARY #length 92 #molecular-weight 10541 #checksum 4517 SEQUENCE /// ENTRY R3LV19 #type complete TITLE ribosomal protein S19 - liverwort (Marchantia polymorpha) chloroplast ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 22-Jun-1999 ACCESSIONS A02745; S01556 REFERENCE A00150 !$#authors Ohyama, K. !$#submission submitted to the EMBL Data Library, October 1986 !$#accession A02745 !'##molecule_type DNA !'##residues 1-92 ##label OHY REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features REFERENCE S01529 !$#authors Fukuzawa, H.; Kohchi, T.; Sano, T.; Shirai, H.; Umesono, K.; !1Inokuchi, H.; Ozeki, H.; Ohyama, K. !$#journal J. Mol. Biol. (1988) 203:333-351 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. III. Gene organization of the large !1single copy region from rbcL to trnI(CAU). !$#cross-references MUID:89068687; PMID:3199436 !$#accession S01556 !'##molecule_type DNA !'##residues 1-92 ##label FUK !'##cross-references GB:X04465; GB:Y00686; NID:g11640; PIDN:CAA28126.1; !1PID:g11715 GENETICS !$#gene rps19 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein S19 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 92 #molecular-weight 10553 #checksum 3592 SEQUENCE /// ENTRY R3SP19 #type complete TITLE ribosomal protein S19 - spinach chloroplast ALTERNATE_NAMES ribosomal protein CS-S23 ORGANISM #formal_name chloroplast Spinacia oleracea #common_name spinach DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 27-Feb-1997 ACCESSIONS S05256; S01976; S07919; S11570; S26234 REFERENCE S05256 !$#authors Mache, R. !$#submission submitted to the EMBL Data Library, October 1988 !$#accession S05256 !'##molecule_type DNA !'##residues 1-92 ##label MAC !'##cross-references EMBL:X13336 REFERENCE S01976 !$#authors Zhou, D.X.; Quigley, F.; Massenet, O.; Mache, R. !$#journal Mol. Gen. Genet. (1989) 216:439-445 !$#title Cotranscription of the S10- and spc-like operons in spinach !1chloroplasts and identification of three of their gene !1products. !$#cross-references MUID:89313684; PMID:2747623 !$#accession S01976 !'##molecule_type DNA !'##residues 75-92 ##label ZHO !'##cross-references EMBL:X13336 REFERENCE S07356 !$#authors Zurawski, G.; Bottomley, W.; Whitfeld, P.R. !$#journal Nucleic Acids Res. (1984) 12:6547-6558 !$#title Junctions of the large single copy region and the inverted !1repeats in Spinacia oleracea and Nicotiana debneyi !1chloroplast DNA: sequence of the genes for tRNA(His) and the !1ribosomal proteins S19 and L2. !$#cross-references MUID:84297246; PMID:6089120 !$#accession S07919 !'##molecule_type DNA !'##residues 1-92 ##label ZUR !'##cross-references EMBL:X00797 !'##note the authors translated the initiation codon GTG for residue 1 !1as Val REFERENCE S00728 !$#authors Thomas, F.; Massenet, O.; Dorne, A.M.; Briat, J.F.; Mache, !1R. !$#journal Nucleic Acids Res. (1988) 16:2461-2472 !$#title Expression of the rpl23, rpl2 and rps19 genes in spinach !1chloroplasts. !$#cross-references MUID:88203193; PMID:3362671 !$#accession S11570 !'##molecule_type protein !'##residues 1-12 ##label THO REFERENCE S26228 !$#authors Schmidt, J.; Herfurth, E.; Subramanian, A.R. !$#journal Plant Mol. Biol. (1992) 20:459-465 !$#title Purification and characterization of seven chloroplast !1ribosomal proteins: evidence that organelle ribosomal !1protein genes are functional and that NH(2)-terminal !1processing occurs via multiple pathways in chloroplasts. !$#cross-references MUID:93043036; PMID:1421149 !$#accession S26234 !'##molecule_type protein !'##residues 2-32 ##label SCH GENETICS !$#gene rps19 !$#genome chloroplast !$#start_codon GTG CLASSIFICATION #superfamily Escherichia coli ribosomal protein S19 KEYWORDS chloroplast; protein biosynthesis; ribosome FEATURE !$2-92 #product ribosomal protein S19 #status experimental !8#label MAT SUMMARY #length 92 #molecular-weight 10608 #checksum 2501 SEQUENCE /// ENTRY R3SY19 #type complete TITLE ribosomal protein S19 - soybean chloroplast ORGANISM #formal_name chloroplast Glycine max #common_name soybean DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 30-Jun-1993 ACCESSIONS S00719 REFERENCE S00718 !$#authors Spielmann, A.; Roux, E.; von Allmen, J.M.; Stutz, E. !$#journal Nucleic Acids Res. (1988) 16:1199 !$#title The soybean chloroplast genome: complete sequence of the !1rps19 gene, including flanking parts containing exon 2 of !1rpl2 (upstream), but lacking rpl22 (downstream). !$#cross-references MUID:88143992; PMID:3344206 !$#accession S00719 !'##molecule_type DNA !'##residues 1-92 ##label SPI !'##cross-references EMBL:X06429 GENETICS !$#gene rps19 !$#genome chloroplast !$#start_codon GTG CLASSIFICATION #superfamily Escherichia coli ribosomal protein S19 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 92 #molecular-weight 10582 #checksum 2615 SEQUENCE /// ENTRY R3NT19 #type complete TITLE ribosomal protein S19 - common tobacco chloroplast ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 13-Jun-1983 #sequence_revision 27-Jun-1983 #text_change 21-Jul-2000 ACCESSIONS A02746; C25943; S72463 REFERENCE A02746 !$#authors Sugita, M.; Sugiura, M. !$#journal Nucleic Acids Res. (1983) 11:1913-1918 !$#title A putative gene of tobacco chloroplast coding for ribosomal !1protein similar to Escherichia coli ribosomal protein S19. !$#cross-references MUID:83168931; PMID:6300784 !$#accession A02746 !'##molecule_type DNA !'##residues 1-92 ##label SUG !'##note the authors translated the codon ACA for residue 43 as Arg REFERENCE A94118 !$#authors Tanaka, M.; Wakasugi, T.; Sugita, M.; Shinozaki, K.; !1Sugiura, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:6030-6034 !$#title Genes for the eight ribosomal proteins are clustered on the !1chloroplast genome of tobacco (Nicotiana tabacum): !1similarity to the S10 and spc operons of Escherichia coli. !$#cross-references MUID:86287388; PMID:3016736 !$#accession C25943 !'##molecule_type DNA !'##residues 1-92 ##label TAN REFERENCE S72459 !$#authors Goulding, S.E.; Olmstead, R.G.; Morden, C.W.; Wolfe, K.H. !$#journal Mol. Gen. Genet. (1996) 252:195-206 !$#title Ebb and flow of the chloroplast inverted repeat. !$#cross-references MUID:96397499; PMID:8804393 !$#accession S72463 !'##status translation not shown !'##molecule_type DNA !'##residues 1-52,'X',54-72,'X',74-92 ##label GOU !'##cross-references EMBL:Z71237; NID:g1279610; PIDN:CAA94939.1; !1PID:g4379319 !'##experimental_source cv. Samsun NN !'##note only a part of the nucleic acid sequence is shown !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1996 GENETICS !$#gene rps19 !$#genome chloroplast !$#start_codon GTG FUNCTION !$#pathway protein biosynthesis CLASSIFICATION #superfamily Escherichia coli ribosomal protein S19 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 92 #molecular-weight 10443 #checksum 2570 SEQUENCE /// ENTRY R3RZ19 #type complete TITLE ribosomal protein S19 - rice chloroplast ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 17-Feb-1995 ACCESSIONS JQ0267; S05192; JA0094; S05147 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0267 !'##molecule_type DNA !'##residues 1-93 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05192 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-93 ##label HIR !'##experimental_source cv. Nihonbare !'##note this sequence was submitted to EMBL, July 1989 REFERENCE JA0092 !$#authors Moon, E.; Wu, R. !$#journal Gene (1988) 70:1-12 !$#title Organization and nucleotide sequence of genes at both !1junctions between the two inverted repeats and the large !1single-copy region in the rice chloroplast genome. !$#cross-references MUID:89196901; PMID:3240862 !$#accession JA0094 !'##molecule_type DNA !'##residues 1-24,'R',26-39,'H',41-93 ##label MOO GENETICS !$#gene rps19 !$#genome chloroplast !$#start_codon GTG CLASSIFICATION #superfamily Escherichia coli ribosomal protein S19 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 93 #molecular-weight 10695 #checksum 6506 SEQUENCE /// ENTRY R3ZM19 #type complete TITLE ribosomal protein S19 - maize chloroplast ORGANISM #formal_name chloroplast Zea mays #common_name maize DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 21-Jul-2000 ACCESSIONS S07388; S58642; S58592 REFERENCE S07388 !$#authors McLaughlin, W.E.; Larrinua, I.M. !$#journal Nucleic Acids Res. (1987) 15:3932 !$#title The sequence of the maize rps19 locus and of the inverted !1repeat/unique region junctions. !$#cross-references MUID:87231092; PMID:3588315 !$#accession S07388 !'##molecule_type DNA !'##residues 1-93 ##label MCL !'##cross-references EMBL:Y00141 REFERENCE S58531 !$#authors Maier, R.M.; Neckermann, K.; Igloi, G.L.; Koessel, H. !$#journal J. Mol. Biol. (1995) 251:614-628 !$#title Complete sequence of the maize chloroplast genome: gene !1content, hotspots of divergence and fine tuning of genetic !1information by transcript editing. !$#cross-references MUID:95395841; PMID:7666415 !$#accession S58642 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-93 ##label MAI !'##cross-references EMBL:X86563; NID:g902200; PIDN:CAA60326.1; !1PID:g2654314 !'##genetics GEN1 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1995 !$#accession S58592 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-93 ##label MAW !'##cross-references EMBL:X86563; NID:g902200; PIDN:CAA60326.1; !1PID:g2654314 !'##genetics GEN2 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1995 GENETICS GEN1 !$#gene rps19 !$#map_position IR(A) !$#genome chloroplast !$#start_codon GTG GENETICS GEN2 !$#gene rps19 !$#map_position IR(B) !$#genome chloroplast !$#start_codon GTG CLASSIFICATION #superfamily Escherichia coli ribosomal protein S19 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 93 #molecular-weight 10757 #checksum 6839 SEQUENCE /// ENTRY R3KT19 #type complete TITLE ribosomal protein S19 - Cyanophora paradoxa cyanelle ORGANISM #formal_name cyanelle Cyanophora paradoxa DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S08235; T06886 REFERENCE S08230 !$#authors Evrard, J.L.; Kuntz, M.; Weil, J.H. !$#journal J. Mol. Evol. (1990) 30:16-25 !$#title The nucleotide sequence of five ribosomal protein genes from !1the cyanelles of Cyanophora paradoxa: implications !1concerning the phylogenetic relationship between cyanelles !1and chloroplasts. !$#cross-references MUID:90189174; PMID:2107321 !$#accession S08235 !'##molecule_type DNA !'##residues 1-92 ##label EVR !'##cross-references EMBL:X17498; NID:g11399; PIDN:CAA35538.1; !1PID:g11405 REFERENCE Z15840 !$#authors Stirewalt, V.L.; Michalowski, C.B.; Luffelhardt, W.; !1Bohnert, H.J.; Bryant, D.A. !$#submission submitted to the EMBL Data Library, July 1995 !$#description Nucleotide sequence of the cyanelle genome from Cyanophora !1paradoxa. !$#accession T06886 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-92 ##label STI !'##cross-references EMBL:U30821; NID:g1016083; PIDN:AAA81229.1; !1PID:g1016142 !'##experimental_source strain Pringsheim LB555 GENETICS !$#gene rps19 !$#genome cyanelle CLASSIFICATION #superfamily Escherichia coli ribosomal protein S19 KEYWORDS cyanelle; protein biosynthesis; ribosome SUMMARY #length 92 #molecular-weight 10352 #checksum 5117 SEQUENCE /// ENTRY R3PJ19 #type complete TITLE ribosomal protein S19 - garden petunia mitochondrion ORGANISM #formal_name mitochondrion Petunia x hybrida #common_name garden petunia DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 22-Jun-1999 ACCESSIONS S29745; S16665; S31648 REFERENCE S16665 !$#authors Conklin, P.L.; Hanson, M.R. !$#journal Nucleic Acids Res. (1991) 19:2701-2705 !$#title Ribosomal protein S19 is encoded by the mitochondrial genome !1in Petunia hybrida. !$#cross-references MUID:91252215; PMID:2041746 !$#accession S29745 !'##molecule_type mRNA !'##residues 1-94 ##label CON1 !'##cross-references EMBL:X57283 !$#accession S16665 !'##molecule_type DNA !'##residues 1-38,'S',40-45,'S',47-54,'P',56-73,'S',75-94 ##label CON2 !'##cross-references GB:X57283; NID:g13339; PIDN:CAA40551.1; PID:g13340 REFERENCE S31647 !$#authors Sutton, C. !$#submission submitted to the EMBL Data Library, June 1992 !$#accession S31648 !'##molecule_type DNA !'##residues 1-38,'S',40-45,'S',47-54,'P',56-73,'S',75-94 ##label SUT !'##cross-references EMBL:X67028; NID:g14162; PIDN:CAA47421.1; !1PID:g14164 GENETICS !$#gene rps19 !$#genome mitochondrion CLASSIFICATION #superfamily Escherichia coli ribosomal protein S19 KEYWORDS mitochondrion; protein biosynthesis; ribosome; RNA editing SUMMARY #length 94 #molecular-weight 11222 #checksum 1685 SEQUENCE /// ENTRY R3HS19 #type complete TITLE ribosomal protein S19 [similarity] - Haloarcula marismortui ALTERNATE_NAMES ribosomal protein HS18 ORGANISM #formal_name Haloarcula marismortui DATE 31-Mar-1991 #sequence_revision 21-Jul-2000 #text_change 21-Jul-2000 ACCESSIONS G35063; S11594 REFERENCE A35063 !$#authors Arndt, E.; Kroemer, W.; Hatakeyama, T. !$#journal J. Biol. Chem. (1990) 265:3034-3039 !$#title Organization and nucleotide sequence of a gene cluster !1coding for eight ribosomal proteins in the archaebacterium !1Halobacterium marismortui. !$#cross-references MUID:90153945; PMID:2406244 !$#accession G35063 !'##molecule_type DNA !'##residues 1-140 ##label ARN !'##cross-references EMBL:J05222; NID:g148800; PIDN:AAA86863.1; !1PID:g148805 REFERENCE S11593 !$#authors Kimura, M.; Arndt, E.; Hatakeyama, T.; Hatakeyama, T.; !1Kimura, J. !$#journal Can. J. Microbiol. (1989) 35:195-199 !$#title Ribosomal proteins in halobacteria. !$#cross-references MUID:89248680; PMID:2655851 !$#accession S11594 !'##molecule_type DNA !'##residues 1-10,'Q',12,'P',14,'P',16-21,'F',23-63,'D',65-82,'D', !184-135,'P',137-140 ##label KIM !'##note part of this sequence, including the amino end of the mature !1protein, were confirmed by protein sequencing !'##note the source is designated as Halobacterium marismortui CLASSIFICATION #superfamily Escherichia coli ribosomal protein S19 KEYWORDS acetylated amino end; protein biosynthesis; ribosome FEATURE !$2-140 #product ribosomal protein S19 #status experimental !8#label MAT\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental SUMMARY #length 140 #molecular-weight 15863 #checksum 6694 SEQUENCE /// ENTRY R3HS9H #type complete TITLE ribosomal protein S19 [similarity] - Halobacterium salinarum ORGANISM #formal_name Halobacterium salinarum DATE 31-Mar-1991 #sequence_revision 21-Jul-2000 #text_change 21-Jul-2000 ACCESSIONS T43820; S03882 REFERENCE Z22697 !$#authors Itoh, T. !$#submission submitted to the EMBL Data Library, September 1997 !$#accession T43820 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-140 ##label ITO !'##cross-references EMBL:AB006961; PIDN:BAA22274.1 !'##note the source is designated as Halobacterium halobium REFERENCE S03882 !$#authors Mankin, A.S. !$#journal FEBS Lett. (1989) 246:13-16 !$#title The nucleotide sequence of the genes coding for the S19 and !1L22 equivalent ribosomal proteins from Halobacterium !1halobium. !$#cross-references MUID:89211383; PMID:2651152 !$#accession S03882 !'##molecule_type DNA !'##residues 26-140 ##label MAN !'##cross-references EMBL:X14967; NID:g43549; PIDN:CAA33091.1; !1PID:g43550 !'##note the source is designated as Halobacterium halobium GENETICS !$#note HhaS19 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S19 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 140 #molecular-weight 15918 #checksum 7559 SEQUENCE /// ENTRY R3HU15 #type complete TITLE ribosomal protein S15, cytosolic [validated] - human ALTERNATE_NAMES insulinoma protein rig ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 08-Dec-2000 ACCESSIONS A35908; A33885; S68923 REFERENCE A35908 !$#authors Shiga, K.; Yamamoto, H.; Okamoto, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:3594-3598 !$#title Isolation and characterization of the human homologue of rig !1and its pseudogenes: the functional gene has features !1characteristic of housekeeping genes. !$#cross-references MUID:90239060; PMID:2159154 !$#accession A35908 !'##molecule_type DNA !'##residues 1-145 ##label SHI !'##cross-references EMBL:M32405; NID:g337415; PIDN:AAA36568.1; !1PID:g337416 REFERENCE A94183 !$#authors Inoue, C.; Shiga, K.; Takasawa, S.; Kitagawa, M.; Yamamoto, !1H.; Okamoto, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:6659-6662 !$#title Evolutionary conservation of the insulinoma gene rig and its !1possible function. !$#cross-references MUID:88016150; PMID:2821540 !$#accession A33885 !'##molecule_type mRNA !'##residues 1-145 ##label INO !'##cross-references GB:J02984; NID:g184553; PIDN:AAA36036.1; !1PID:g306898 REFERENCE S68911 !$#authors Vladimirov, S.N.; Ivanov, A.V.; Karpova, G.G.; Musolyamov, !1A.K.; Egorov, T.A.; Thiede, B.; Wittmann-Liebold, B.; Otto, !1A. !$#journal Eur. J. Biochem. (1996) 239:144-149 !$#title Characterization of the human small-ribosomal-subunit !1proteins by N-terminal and internal sequencing, and mass !1spectrometry. !$#cross-references MUID:96305378; PMID:8706699 !$#accession S68923 !'##molecule_type protein !'##residues 101-113,'X',115-116 ##label VLA GENETICS !$#gene GDB:RPS15 !'##cross-references GDB:132222; OMIM:180535 !$#map_position 5q31-5q33 !$#introns 1/3; 30/2; 108/3 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S19 KEYWORDS acetylated amino end; protein biosynthesis; ribosome FEATURE !$2-145 #product ribosomal protein S15 #status experimental !8#label MAT\ !$61-68 #region nuclear location signal\ !$2 #modified_site blocked amino end (Ala) (in mature !8form) (probably acetylated) #status experimental SUMMARY #length 145 #molecular-weight 17040 #checksum 3583 SEQUENCE /// ENTRY R3RT15 #type complete TITLE ribosomal protein S15, cytosolic [validated] - rat ALTERNATE_NAMES insulinoma protein rig ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 21-Jul-2000 ACCESSIONS S28939; S07438; S15834; A30349 REFERENCE S28939 !$#authors Takasawa, S.; Tohgo, A.; Unno, M.; Shiga, K.; Yonekura, H.; !1Okamoto, H. !$#journal Biochim. Biophys. Acta (1992) 1132:228-230 !$#title The primary structure of rat rig/ribosomal protein S15 gene. !$#cross-references MUID:93003332; PMID:1390896 !$#accession S28939 !'##molecule_type DNA !'##residues 1-145 ##label TAK1 !'##cross-references GB:D11388; NID:g220898; PIDN:BAA01984.1; !1PID:g220899 REFERENCE A30349 !$#authors Takasawa, S.; Yamamoto, H.; Terazono, K.; Okamoto, H. !$#journal Diabetes (1986) 35:1178-1180 !$#title Novel gene activated in rat insulinomas. !$#cross-references MUID:87005616; PMID:3019805 !$#accession S07438 !'##molecule_type mRNA !'##residues 1-145 ##label TAK2 !'##cross-references EMBL:M19393; NID:g206663; PIDN:AAA42044.1; !1PID:g206664 REFERENCE S15834 !$#authors Kitagawa, M.; Takasawa, S.; Kikuchi, N.; Itoh, T.; Teraoka, !1H.; Yamamoto, H.; Okamoto, H. !$#journal FEBS Lett. (1991) 283:210-214 !$#title rig encodes ribosomal protein S15. The primary structure of !1mammalian ribosomal protein S15. !$#cross-references MUID:91257304; PMID:2044758 !$#accession S15834 !'##molecule_type protein !'##residues 2-28,'X',30-37;53-62;66-76;78-89;101-111,'X',113,'X', !1115-118;128-140 ##label KIT !'##note the protein is designated as ribosomal protein S15 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S19 KEYWORDS acetylated amino end; protein biosynthesis; ribosome FEATURE !$2-145 #product ribosomal protein S15 #status experimental !8#label MAT\ !$61-68 #region nuclear location signal\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental SUMMARY #length 145 #molecular-weight 17040 #checksum 3583 SEQUENCE /// ENTRY R3HY15 #type complete TITLE ribosomal protein S15 - golden hamster ALTERNATE_NAMES insulinoma protein rig ORGANISM #formal_name Mesocricetus auratus #common_name golden hamster DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 22-Jun-1999 ACCESSIONS B33885 REFERENCE A94183 !$#authors Inoue, C.; Shiga, K.; Takasawa, S.; Kitagawa, M.; Yamamoto, !1H.; Okamoto, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:6659-6662 !$#title Evolutionary conservation of the insulinoma gene rig and its !1possible function. !$#cross-references MUID:88016150; PMID:2821540 !$#accession B33885 !'##molecule_type mRNA !'##residues 1-145 ##label INO !'##cross-references GB:J02983; NID:g191434; PIDN:AAA37094.1; !1PID:g305361 GENETICS !$#gene rig CLASSIFICATION #superfamily Escherichia coli ribosomal protein S19 KEYWORDS acetylated amino end; protein biosynthesis; ribosome FEATURE !$2-145 #product ribosomal protein S15 #status predicted !8#label MAT\ !$61-68 #region nuclear location signal\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status predicted SUMMARY #length 145 #molecular-weight 17040 #checksum 3583 SEQUENCE /// ENTRY R3XL19 #type complete TITLE ribosomal protein S24 - African clawed frog ALTERNATE_NAMES ribosomal protein S19 ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 22-Jun-1999 ACCESSIONS A02747; T01063 REFERENCE A91492 !$#authors Amaldi, F.; Beccari, E.; Bozzoni, I.; Luo, Z.X.; !1Pierandrei-Amaldi, P. !$#journal Gene (1982) 17:311-316 !$#title Nucleotide sequences of cloned cDNA fragments specific for !1six Xenopus laevis ribosomal proteins. !$#cross-references MUID:82262793; PMID:7049839 !$#accession A02747 !'##molecule_type mRNA !'##residues 1-132 ##label AMA !'##cross-references GB:V01443; GB:J00997; NID:g65053; PIDN:CAA24704.1; !1PID:g65054 GENETICS !$#gene rps19 CLASSIFICATION #superfamily rat ribosomal protein S24 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 132 #molecular-weight 15284 #checksum 7029 SEQUENCE /// ENTRY R3RT24 #type complete TITLE ribosomal protein S24, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 21-Jul-2000 ACCESSIONS S09197; S20565 REFERENCE S09197 !$#authors Chan, Y.L.; Paz, V.; Olvera, J.; Wool, I.G. !$#journal FEBS Lett. (1990) 262:253-255 !$#title The primary structure of rat ribosomal protein S24. !$#cross-references MUID:90242941; PMID:2335205 !$#accession S09197 !'##molecule_type mRNA !'##residues 1-133 ##label CHA !'##cross-references EMBL:X51538; NID:g57721; PIDN:CAA35918.1; !1PID:g57722 !$#accession S20565 !'##molecule_type protein !'##residues 'XX',3-7,'X',9-17 ##label CHA2 !'##note the protein is designated as ribosomal protein S24 CLASSIFICATION #superfamily rat ribosomal protein S24 KEYWORDS protein biosynthesis; ribosome FEATURE !$1-133 #product ribosomal protein S24 #status experimental !8#label MAT SUMMARY #length 133 #molecular-weight 15423 #checksum 8803 SEQUENCE /// ENTRY R3HY24 #type complete TITLE ribosomal protein S24 - golden hamster ALTERNATE_NAMES ribosomal protein HS19 ORGANISM #formal_name Mesocricetus auratus #common_name golden hamster DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 22-Jun-1999 ACCESSIONS S10325 REFERENCE S10325 !$#authors Klein, H.; Gervais, C.; Suh, M. !$#journal Nucleic Acids Res. (1990) 18:3997 !$#title Nucleotide sequence of a hamster cDNA highly homologous to !1the Xenopus laevis S19 ribosomal protein. !$#cross-references MUID:90326533; PMID:2374723 !$#accession S10325 !'##molecule_type mRNA !'##residues 1-133 ##label KLE !'##cross-references EMBL:X52658; NID:g49651; PIDN:CAA36884.1; !1PID:g49652 CLASSIFICATION #superfamily rat ribosomal protein S24 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 133 #molecular-weight 15423 #checksum 8803 SEQUENCE /// ENTRY R3UD24 #type complete TITLE ribosomal protein S24 - Rhizomucor racemosus ALTERNATE_NAMES ribosomal protein S19 ORGANISM #formal_name Rhizomucor racemosus DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S07632 REFERENCE S07632 !$#authors Sosa, L.; Fonzi, W.A.; Sypherd, P.S. !$#journal Nucleic Acids Res. (1989) 17:9319-9331 !$#title Structure of a ribosomal protein gene in Mucor racemosus. !$#cross-references MUID:90067930; PMID:2685758 !$#accession S07632 !'##molecule_type DNA !'##residues 1-148 ##label SOS !'##cross-references EMBL:X15582; NID:g2958; PIDN:CAA33608.1; !1PID:g295925 GENETICS !$#introns 19/3 CLASSIFICATION #superfamily rat ribosomal protein S24 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 148 #molecular-weight 17228 #checksum 7990 SEQUENCE /// ENTRY R3HS15 #type complete TITLE ribosomal protein S24.eR [validated] - Haloarcula marismortui ALTERNATE_NAMES ribosomal protein E1.2; ribosomal protein HS15 ORGANISM #formal_name Haloarcula marismortui DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 04-Feb-2000 ACCESSIONS S27035; S00184; D24304 REFERENCE S27035 !$#authors Arndt, E.; Steffens, C. !$#journal FEBS Lett. (1992) 314:211-214 !$#title Nucleotide sequence of the genes for ribosomal proteins HS15 !1and HSH from Haloarcula marismortui: an archaeon-specific !1gene cluster. !$#cross-references MUID:93106152; PMID:1468549 !$#accession S27035 !'##molecule_type DNA !'##residues 1-102 ##label ARN !'##cross-references GB:X70117; GB:S51568; NID:g312778; PIDN:CAA49707.1; !1PID:g312779 REFERENCE S00182 !$#authors Kimura, J.; Arndt, E.; Kimura, M. !$#journal FEBS Lett. (1987) 224:65-70 !$#title Primary structures of three highly acidic ribosomal proteins !1S6, S12 and S15 from the archaebacterium Halobacterium !1marismortui. !$#cross-references MUID:88055606; PMID:3315748 !$#accession S00184 !'##molecule_type protein !'##residues 1-102 ##label KIM !'##note the source is designated as Halobacterium marismortui !'##note the protein is designated as ribosomal protein S15 REFERENCE A24304 !$#authors Shoham, M.; Dijk, J.; Reinhardt, R.; Wittmann-Liebold, B. !$#journal FEBS Lett. (1986) 204:323-330 !$#title Purification and characterization of ribosomal proteins from !1the 30 S subunit of the extreme halophile Halobacterium !1marismortui. !$#accession D24304 !'##molecule_type protein !'##residues 1-24,'X',26-29 ##label SHO !'##note the source is designated as Halobacterium marismortui CLASSIFICATION #superfamily rat ribosomal protein S24 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 102 #molecular-weight 11745 #checksum 910 SEQUENCE /// ENTRY R3EC20 #type complete TITLE ribosomal protein S20/L26 [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES ribosomal protein L26; ribosomal protein S20 ORGANISM #formal_name Escherichia coli DATE 15-Oct-1982 #sequence_revision 15-Oct-1982 #text_change 01-Mar-2002 ACCESSIONS A30425; A02748; S40547; G64722; S07374 REFERENCE A30425 !$#authors Mackie, G.A. !$#journal J. Biol. Chem. (1981) 256:8177-8182 !$#title Nucleotide sequence of the gene for ribosomal protein S20 !1and its flanking regions. !$#cross-references MUID:81264207; PMID:6267039 !$#accession A30425 !'##molecule_type DNA !'##residues 1-87 ##label MAC !'##cross-references GB:D10483; GB:J01597; GB:J01683; GB:J01706; !1GB:K01298; GB:K01990; GB:M10420; GB:M10611; GB:M12544; !1GB:V00259; GB:X04711; GB:X54847; GB:X54945; GB:X55034; !1GB:X56742; NID:g216434; PIDN:BAA01302.1; PID:g285763; !1GB:X04382; GB:V00345; NID:g42864; PIDN:CAA27968.1; !1PID:g581224 REFERENCE A02748 !$#authors Wittmann-Liebold, B.; Marzinzig, E.; Lehmann, A. !$#journal FEBS Lett. (1976) 68:110-114 !$#title Primary structure of protein S20 from the small ribosomal !1subunit of Escherichia coli. !$#cross-references MUID:77003692; PMID:786731 !$#accession A02748 !'##molecule_type protein !'##residues 2-87 ##label WIT !'##experimental_source strain K REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40547 !'##molecule_type DNA !'##residues 'L',2-87 ##label YUR !'##cross-references EMBL:D10483; NID:g216434; PIDN:BAA01302.1; !1PID:g285763 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64722 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-87 ##label BLAT !'##cross-references GB:AE000113; GB:U00096; NID:g2367095; !1PIDN:AAC73134.1; PID:g1786206; UWGP:b0023 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note mass spectrographic analysis of post-translational !1modifications; any acid labile modifications may have been !1missed GENETICS !$#gene rpsT !$#map_position 0 min !$#start_codon GTG COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX small subunit ribosomal proteins: S1 (PIR:R3EC1), S2 !1(PIR:R3EC2), S3 (PIR:R3EC3), S4 (PIR:R3EC4), S5 (PIR:R3EC5), !1S6 (PIR:R3EC6), S7 (PIR:R3EC7K), S8 (PIR:R3EC8), S9 !1(PIR:R3EC9), S10 (PIR:R3EC10), S11 (PIR:R3EC11), S12 !1(PIR:R3EC12), S13 (PIR:R3EC13), S14 (PIR:R3EC14), S15 !1(PIR:R3EC15), S16 (PIR:R3EC16), S17 (PIR:R3EC17), S18 !1(PIR:R3EC18), S19 (PIR:R3EC19), S20/L26 (PIR:R3EC20), S21 !1(PIR:R3EC21), S22 (PIR:C64901) [validated, MUID:99196679] FUNCTION !$#pathway protein biosynthesis !$#note binds 16S rRNA CLASSIFICATION #superfamily Escherichia coli ribosomal protein S20 KEYWORDS protein biosynthesis; ribosome; RNA binding FEATURE !$2-87 #product ribosomal protein S20 #status experimental !8#label MAT SUMMARY #length 87 #molecular-weight 9684 #checksum 6632 SEQUENCE /// ENTRY R3EC21 #type complete TITLE ribosomal protein S21 [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 24-Apr-1984 #sequence_revision 30-Jun-1991 #text_change 01-Mar-2002 ACCESSIONS A02749; A30426; I57721; G65094 REFERENCE A02749 !$#authors Burton, Z.F.; Gross, C.A.; Watanabe, K.K.; Burgess, R.R. !$#journal Cell (1983) 32:335-349 !$#title The operon that encodes the sigma subunit of RNA polymerse !1also encodes ribosomal protein S21 and DNA primase in !1Escherichia coli K12. !$#cross-references MUID:83129424; PMID:6186393 !$#accession A02749 !'##molecule_type DNA !'##residues 1-71 ##label BUR !'##cross-references GB:J01687; NID:g147753; PIDN:AAA24599.1; !1PID:g147754 REFERENCE A30426 !$#authors Vandekerckhove, J.; Rombauts, W.; Peeters, B.; !1Wittmann-Liebold, B. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1975) 356:1955-1976 !$#title Determination of the complete amino acid sequence of protein !1S21 from Escherichia coli ribosomes. !$#cross-references MUID:76119561; PMID:765257 !$#accession A30426 !'##molecule_type protein !'##residues 2-71 ##label VAN !'##experimental_source strain K REFERENCE I57721 !$#authors Lupski, J.R.; Smiley, B.L.; Godson, G.N. !$#journal Mol. Gen. Genet. (1983) 189:48-57 !$#title Regulation of the rpsU-dnaG-rpoD macromolecular synthesis !1operon and the initiation of DNA replication in Escherichia !1coli K-12. !$#cross-references MUID:83218520; PMID:6222240 !$#accession I57721 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-71 ##label LUP !'##cross-references EMBL:V00346; NID:g42867; PIDN:CAA23635.1; !1PID:g42868 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65094 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-71 ##label BLAT !'##cross-references GB:AE000388; GB:U00096; NID:g1789441; !1PIDN:AAC76101.1; PID:g1789446; UWGP:b3065 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note mass spectrographic analysis of post-translational !1modifications; any acid labile modifications may have been !1missed GENETICS !$#gene rpsU !$#map_position 67 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX small subunit ribosomal proteins: S1 (PIR:R3EC1), S2 !1(PIR:R3EC2), S3 (PIR:R3EC3), S4 (PIR:R3EC4), S5 (PIR:R3EC5), !1S6 (PIR:R3EC6), S7 (PIR:R3EC7K), S8 (PIR:R3EC8), S9 !1(PIR:R3EC9), S10 (PIR:R3EC10), S11 (PIR:R3EC11), S12 !1(PIR:R3EC12), S13 (PIR:R3EC13), S14 (PIR:R3EC14), S15 !1(PIR:R3EC15), S16 (PIR:R3EC16), S17 (PIR:R3EC17), S18 !1(PIR:R3EC18), S19 (PIR:R3EC19), S20/L26 (PIR:R3EC20), S21 !1(PIR:R3EC21), S22 (PIR:C64901) [validated, MUID:99196679] FUNCTION !$#pathway protein biosynthesis CLASSIFICATION #superfamily Escherichia coli ribosomal protein S21 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-71 #product ribosomal protein S21 #status experimental !8#label MAT SUMMARY #length 71 #molecular-weight 8500 #checksum 3352 SEQUENCE /// ENTRY I64074 #type complete TITLE ribosomal protein S21 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS I64074 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession I64074 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-71 ##label TIGR !'##cross-references GB:U32735; GB:L42023; NID:g1573509; !1PIDN:AAC22188.1; PID:g1573515; TIGR:HI0531 CLASSIFICATION #superfamily Escherichia coli ribosomal protein S21 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 71 #molecular-weight 8462 #checksum 2448 SEQUENCE /// ENTRY R3EB21 #type complete TITLE ribosomal protein S21 - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 22-Jun-1999 ACCESSIONS A23985 REFERENCE A91542 !$#authors Erickson, B.D.; Burton, Z.F.; Watanabe, K.K.; Burgess, R.R. !$#journal Gene (1985) 40:67-78 !$#title Nucleotide sequence of the rpsU-dnaG-rpoD operon from !1Salmonella typhimurium and a comparison of this sequence !1with the homologous operon of Escherichia coli. !$#cross-references MUID:86137422; PMID:3005129 !$#accession A23985 !'##molecule_type DNA !'##residues 1-71 ##label ERI !'##cross-references GB:M14427; NID:g154402; PIDN:AAA27240.1; !1PID:g154404 GENETICS !$#gene rpsU CLASSIFICATION #superfamily Escherichia coli ribosomal protein S21 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 71 #molecular-weight 8500 #checksum 3352 SEQUENCE /// ENTRY R3RT21 #type complete TITLE ribosomal protein S21, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 21-Jul-2000 ACCESSIONS C23862; JC4228; PC4064; S44312 REFERENCE A90501 !$#authors Itoh, T.; Otaka, E.; Matsui, K.A. !$#journal Biochemistry (1985) 24:7418-7423 !$#title Primary structures of ribosomal protein YS25 from !1Saccharomyces cerevisiae and its counterparts from !1Schizosaccharomyces pombe and rat liver. !$#cross-references MUID:86104253; PMID:3910104 !$#accession C23862 !'##molecule_type protein !'##residues 1-83 ##label ITO REFERENCE JC4228 !$#authors Chan, Y.L.; Olvera, J.; Wool, I.G. !$#journal Biochem. Biophys. Res. Commun. (1995) 213:1042-1050 !$#title The primary structures of rat ribosomal proteins: the !1characterization of the cDNAs for S21 and L39, corrections !1in the sequences of L7 and L18a, and the identification of !1L33. !$#cross-references MUID:95382802; PMID:7654221 !$#accession JC4228 !'##molecule_type mRNA !'##residues 1-83 ##label CHA !'##cross-references EMBL:X79059; NID:g483516; PIDN:CAA55658.1; !1PID:g483517 !$#accession PC4064 !'##molecule_type protein !'##residues 1-10 ##label CH2 !'##experimental_source liver !'##note the protein is designated as ribosomal protein S21 CLASSIFICATION #superfamily rat ribosomal protein S21 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 83 #molecular-weight 9127 #checksum 1171 SEQUENCE /// ENTRY R3BY1E #type complete TITLE ribosomal protein S21.e.A, cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YKR057w; ribosomal protein YS25; ribosomal protein YS26 ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 12-Nov-1999 ACCESSIONS S00975; A23862; S38133 REFERENCE S00975 !$#authors Suzuki, K.; Otaka, E. !$#journal Nucleic Acids Res. (1988) 16:6223 !$#title Cloning and nucleotide sequence of the gene encoding yeast !1ribosomal protein YS25. !$#cross-references MUID:88289363; PMID:2899871 !$#accession S00975 !'##molecule_type DNA !'##residues 1-87 ##label SUZ !'##cross-references EMBL:X07811; NID:g4410; PIDN:CAA30671.1; PID:g4411 REFERENCE A90501 !$#authors Itoh, T.; Otaka, E.; Matsui, K.A. !$#journal Biochemistry (1985) 24:7418-7423 !$#title Primary structures of ribosomal protein YS25 from !1Saccharomyces cerevisiae and its counterparts from !1Schizosaccharomyces pombe and rat liver. !$#cross-references MUID:86104253; PMID:3910104 !$#accession A23862 !'##molecule_type protein !'##residues 1-87 ##label ITO REFERENCE S38130 !$#authors van Vliet-Reedijk, J.C.; Planta, R.J. !$#submission submitted to the Protein Sequence Database, March 1994 !$#accession S38133 !'##molecule_type DNA !'##residues 1-87 ##label VAN !'##cross-references EMBL:Z28282; NID:g486516; PIDN:CAA82135.1; !1PID:g486517; GSPDB:GN00011; MIPS:YKR057w !'##experimental_source strain S288C GENETICS !$#gene SGD:RPS25; MIPS:YKR057w !'##cross-references SGD:S0001765; MIPS:YKR057w !$#map_position 11R !$#introns 8/3 CLASSIFICATION #superfamily rat ribosomal protein S21 KEYWORDS protein biosynthesis; ribosome FEATURE !$1-87 #product ribosomal protein S21.e #status experimental !8#label MAT SUMMARY #length 87 #molecular-weight 9746 #checksum 2309 SEQUENCE /// ENTRY C64901 #type complete TITLE ribosomal protein S22 [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 24-Sep-1999 #sequence_revision 24-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS C64901 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64901 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-45 ##label BLAT !'##cross-references GB:AE000245; GB:U00096; NID:g1787752; !1PIDN:AAC74553.1; PID:g1787755; UWGP:b1480 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note a ribosomal protein with these mass spectrographic !1characteristics was found; no post-translational !1modifications were observed in mass spectrographic analysis; !1any acid labile modifications may have been missed GENETICS !$#gene rpsV COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX small subunit ribosomal proteins: S1 (PIR:R3EC1), S2 !1(PIR:R3EC2), S3 (PIR:R3EC3), S4 (PIR:R3EC4), S5 (PIR:R3EC5), !1S6 (PIR:R3EC6), S7 (PIR:R3EC7K), S8 (PIR:R3EC8), S9 !1(PIR:R3EC9), S10 (PIR:R3EC10), S11 (PIR:R3EC11), S12 !1(PIR:R3EC12), S13 (PIR:R3EC13), S14 (PIR:R3EC14), S15 !1(PIR:R3EC15), S16 (PIR:R3EC16), S17 (PIR:R3EC17), S18 !1(PIR:R3EC18), S19 (PIR:R3EC19), S20/L26 (PIR:R3EC20), S21 !1(PIR:R3EC21), S22 (PIR:C64901) [validated, MUID:99196679] FUNCTION !$#pathway protein biosynthesis CLASSIFICATION #superfamily Escherichia coli ribosomal protein S22 KEYWORDS protein biosynthesis; ribosome FEATURE !$1-45 #product ribosomal protein S22 #status experimental !8#label MAT SUMMARY #length 45 #molecular-weight 5096 #checksum 9770 SEQUENCE /// ENTRY R3RT25 #type complete TITLE ribosomal protein S25, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 21-Jul-2000 ACCESSIONS A38969; S17353 REFERENCE JH0691 !$#authors Chan, Y.L.; Wool, I.G. !$#journal Biochem. Biophys. Res. Commun. (1992) 186:1688-1693 !$#title The primary structure of rat ribosomal protein S25. !$#cross-references MUID:92378645; PMID:1354961 !$#accession A38969 !'##molecule_type mRNA !'##residues 1-125 ##label CH2 !'##cross-references EMBL:X62482; NID:g57723; PIDN:CAA44349.1; !1PID:g57724 !'##note the protein is designated as ribosomal protein S25 by !1comparison to the composition of ribosomal proteins CLASSIFICATION #superfamily rat ribosomal protein S25 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 125 #molecular-weight 13742 #checksum 7683 SEQUENCE /// ENTRY R3BY31 #type complete TITLE ribosomal protein S25.e.A precursor, cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein G4046; protein YGR027c; ribosomal protein YS23; ribosomal protein YS31 ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Jun-2000 ACCESSIONS S05844; S11251; S64318 REFERENCE S05844 !$#authors Nieuwint, R.T.M.; Molenaar, C.M.T.; van Bommel, J.H.; van !1Raamsdonk-Duin, M.M.C.; Mager, W.H.; Planta, R.J. !$#journal Curr. Genet. (1985) 10:1-5 !$#title The gene for yeast ribosomal protein S31 contains an intron !1in the leader sequence. !$#cross-references MUID:91091952; PMID:2856436 !$#accession S05844 !'##molecule_type DNA !'##residues 1-108 ##label NIE !'##cross-references EMBL:X03013; NID:g4408; PIDN:CAA26797.1; PID:g4409 REFERENCE S11249 !$#authors Otaka, E.; Higo, K.I.; Itoh, T. !$#journal Mol. Gen. Genet. (1984) 195:544-546 !$#title Yeast ribosomal proteins. VIII. Isolation of two proteins !1and sequence characterization of twenty-four proteins from !1cytoplasmic ribosomes. !$#accession S11251 !'##molecule_type protein !'##residues 15,'R',17-19,'X',21-22 ##label OTA REFERENCE S64071 !$#authors Rieger, M.; Mueller-Auer, S.; Brueckner, M.; Schaefer, M. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64318 !'##molecule_type DNA !'##residues 1-108 ##label RIE !'##cross-references EMBL:Z72812; NID:g1325961; PIDN:CAA97010.1; !1PID:g1325962; GSPDB:GN00007; MIPS:YGR027c !'##experimental_source strain S288C GENETICS !$#gene SGD:RPS31A; MIPS:YGR027c !'##cross-references SGD:S0003259; MIPS:YGR027c !$#map_position 7R CLASSIFICATION #superfamily rat ribosomal protein S25 KEYWORDS protein biosynthesis; ribosome FEATURE !$15-108 #product ribosomal protein S25.e #status experimental !8#label MAT SUMMARY #length 108 #molecular-weight 12039 #checksum 6342 SEQUENCE /// ENTRY R3RT28 #type complete TITLE ribosomal protein S28, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 21-Jul-2000 ACCESSIONS JQ1170; PQ0218 REFERENCE JQ1170 !$#authors Chan, Y.; Olvera, J.; Wool, I.G. !$#journal Biochem. Biophys. Res. Commun. (1991) 179:314-318 !$#title The primary structure of rat ribosomal protein S28. !$#cross-references MUID:91354268; PMID:1679328 !$#accession JQ1170 !'##molecule_type mRNA !'##residues 1-69 ##label CHA !'##cross-references EMBL:X59277; NID:g57725; PIDN:CAA41967.1; !1PID:g57726 !$#accession PQ0218 !'##molecule_type protein !'##residues 36-68 ##label CH2 !'##note the protein is designated as ribosomal protein S28 CLASSIFICATION #superfamily rat ribosomal protein S28 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 69 #molecular-weight 7841 #checksum 4770 SEQUENCE /// ENTRY R3BY33 #type complete TITLE ribosomal protein S28.e.A, cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein O3598; protein YOR167c; ribosomal protein YS33 ORGANISM #formal_name Saccharomyces cerevisiae DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 21-Jul-2000 ACCESSIONS A02750; S67055 REFERENCE A02750 !$#authors Leer, R.J.; van Raamsdonk-Duin, M.M.C.; Schoppink, P.J.; !1Cornelissen, M.T.E.; Cohen, L.H.; Mager, W.H.; Planta, R.J. !$#journal Nucleic Acids Res. (1983) 11:7759-7768 !$#title Yeast ribosomal protein S33 is encoded by an unsplit gene. !$#cross-references MUID:84069801; PMID:6196722 !$#accession A02750 !'##molecule_type DNA !'##residues 1-67 ##label LEE !'##cross-references EMBL:X00128; NID:g4414; PIDN:CAA24958.1; PID:g4415 REFERENCE S67032 !$#authors Bordonne, R.; Camasses, A.; Madania, A.; Martin, R.P.; Poch, !1O.; Tarassov, I.A.; Winsor, B. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67055 !'##molecule_type DNA !'##residues 1-67 ##label BOR !'##cross-references EMBL:Z75075; NID:g1420410; PIDN:CAA99373.1; !1PID:g1420411; GSPDB:GN00015; MIPS:YOR167c !'##experimental_source strain S288C GENETICS !$#gene SGD:RPS33A; MIPS:YOR167c !'##cross-references SGD:S0005693; MIPS:YOR167c !$#map_position 15R CLASSIFICATION #superfamily rat ribosomal protein S28 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 67 #molecular-weight 7592 #checksum 3313 SEQUENCE /// ENTRY R3BYM1 #type complete TITLE ribosomal protein var1, mitochondrial - yeast (Saccharomyces cerevisiae) mitochondrion ALTERNATE_NAMES protein Q0140 ORGANISM #formal_name mitochondrion Saccharomyces cerevisiae DATE 18-Apr-1984 #sequence_revision 29-Jan-1999 #text_change 19-Apr-2002 ACCESSIONS S78670; S78671; A02751 REFERENCE S78634 !$#authors Foury, F.; Roganti, T.; Lecrenier, N.; Purnelle, B. !$#submission submitted to the Protein Sequence Database, December 1998 !$#accession S78670 !'##molecule_type DNA !'##residues 1-398 ##label FOU1 !'##cross-references EMBL:AJ011856; MIPS:Q0140 !'##experimental_source strain FY1679, isogenic derivative of strain !1S288C REFERENCE Z13743 !$#authors Foury, F.; Roganti, T.; Lecrenier, N.; Purnelle, B. !$#journal FEBS Lett. (1998) 440:325-331 !$#title The complete sequence of the mitochondrial genome of !1Saccharomyces cerevisiae. !$#cross-references MUID:99087401; PMID:9872396 !$#accession S78671 !'##molecule_type DNA !'##residues 1-398 ##label FOU2 !'##cross-references EMBL:AJ011856; NID:g4160362; PIDN:CAA09839.1; !1PID:g4160381 !'##experimental_source strain FY1679, isogenic derivative of strain !1S288C REFERENCE A02751 !$#authors Hudspeth, M.E.S.; Ainley, W.M.; Shumard, D.S.; Butow, R.A.; !1Grossman, L.I. !$#journal Cell (1982) 30:617-626 !$#title Location and structure of the var1 gene on yeast !1mitochondrial DNA: nucleotide sequence of the 40.0 allele. !$#cross-references MUID:83050946; PMID:6754087 !$#accession A02751 !'##molecule_type DNA !'##residues 1-160,163-199,'N',201-398 ##label HUD !'##cross-references EMBL:V00705; NID:g13610; PIDN:CAA24077.1; !1PID:g13611 !'##note the reading frame was confirmed by determination of the amino !1acid composition GENETICS !$#gene SGD:VAR1; var1 !'##cross-references SGD:S0007275 !$#genome mitochondrion !$#genetic_code SGC2 CLASSIFICATION #superfamily Saccharomyces cerevisiae ribosomal protein var1 KEYWORDS mitochondrion; protein biosynthesis; ribosome SUMMARY #length 398 #molecular-weight 47123 #checksum 2937 SEQUENCE /// ENTRY S42734 #type complete TITLE probable ribosomal protein var1 - yeast (Williopsis mrakii) mitochondrion ALTERNATE_NAMES hypothetical protein 2 ORGANISM #formal_name mitochondrion Williopsis mrakii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 07-Dec-1999 ACCESSIONS S42734 REFERENCE S42733 !$#authors Drissi, R.; Sor, F.; Nosek, J.; Fukuhara, H. !$#journal Yeast (1994) 10:391-398 !$#title Genes of the linear mitochondrial DNA of Williopsis mrakii: !1coding sequences for a maturase-like protein, a ribosomal !1protein VAR1 homologue, cytochrome oxidase subunit 2 and !1methionyl tRNA. !$#cross-references MUID:94287716; PMID:8017108 !$#accession S42734 !'##status preliminary; nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-380 ##label DRI !'##cross-references EMBL:X66594; NID:g296849; PIDN:CAA47158.1; !1PID:g296851 GENETICS !$#genome mitochondrion !$#genetic_code SGC2 CLASSIFICATION #superfamily Saccharomyces cerevisiae ribosomal protein var1 KEYWORDS mitochondrion SUMMARY #length 380 #molecular-weight 44376 #checksum 4171 SEQUENCE /// ENTRY QXASRI #type complete TITLE 21S rRNA intron protein - Emericella nidulans mitochondrion ORGANISM #formal_name mitochondrion Emericella nidulans, Aspergillus nidulans DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 07-Dec-1999 ACCESSIONS D93436; B94593; A02752 REFERENCE A93436 !$#authors Netzker, R.; Kochel, H.G.; Basak, N.; Kuntzel, H. !$#journal Nucleic Acids Res. (1982) 10:4783-4794 !$#title Nucleotide sequence of Aspergillus nidulans mitochondrial !1genes coding for ATPase subunit 6, cytochrome oxidase !1subunit 3, seven unidentified proteins, four tRNAs and !1L-rRNA. !$#cross-references MUID:83038633; PMID:6290989 !$#accession D93436 !'##molecule_type DNA !'##residues 1-133,'I',135-373,'A',375-410 ##label NET !'##experimental_source imperfect stage !'##note this sequence has been revised in reference A94593 REFERENCE A94593 !$#authors Lazarus, C.M.; Kuntzel, H. !$#submission submitted to the Atlas, March 1984 !$#accession B94593 !'##molecule_type DNA !'##residues 1-410 ##label LAZ GENETICS !$#genome mitochondrion !$#genetic_code SGC3 CLASSIFICATION #superfamily Saccharomyces cerevisiae ribosomal protein var1 KEYWORDS mitochondrion SUMMARY #length 410 #molecular-weight 48801 #checksum 4096 SEQUENCE /// ENTRY R4RT26 #type complete TITLE ribosomal protein S26, cytosolic - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 21-Jul-2000 ACCESSIONS A02753 REFERENCE A02753 !$#authors Kuwano, Y.; Nakanishi, O.; Nabeshima, Y.; Tanaka, T.; Ogata, !1K. !$#journal J. Biochem. (1985) 97:983-992 !$#title Molecular cloning and nucleotide sequence of DNA !1complementary to rat ribosomal protein S26 messenger RNA. !$#cross-references MUID:85289112; PMID:2993263 !$#accession A02753 !'##molecule_type mRNA !'##residues 1-115 ##label KUW !'##cross-references GB:X02414; NID:g57130; PIDN:CAA26264.1; PID:g57131 CLASSIFICATION #superfamily rat ribosomal protein S26 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 115 #molecular-weight 13015 #checksum 1139 SEQUENCE /// ENTRY S18876 #type complete TITLE ribosomal protein S26, cytosolic - black-bellied hamster ORGANISM #formal_name Cricetus cricetus #common_name black-bellied hamster DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 22-Jun-1999 ACCESSIONS S30300; S18876 REFERENCE S30300 !$#authors Vincent, S.; Marty, L.; Fort, P. !$#journal Nucleic Acids Res. (1993) 21:1498 !$#title S26 ribosomal protein RNA: an invariant control for gene !1regulation experiments in eucaryotic cells and tissues. !$#cross-references MUID:93219139; PMID:8464749 !$#accession S30300 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type mRNA !'##residues 1-115 ##label VIN !'##cross-references EMBL:X63389; NID:g49452; PIDN:CAA44996.1; !1PID:g49453 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1991 CLASSIFICATION #superfamily rat ribosomal protein S26 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 115 #molecular-weight 13016 #checksum 1061 SEQUENCE /// ENTRY R3FF26 #type complete TITLE ribosomal protein S26 - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES ribosomal protein DS31 ORGANISM #formal_name Drosophila melanogaster DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 21-Jul-2000 ACCESSIONS S03724; S03293 REFERENCE S03724 !$#authors Itoh, N.; Ohta, K.; Ohta, M.; Kawasaki, T.; Yamashina, I. !$#journal Nucleic Acids Res. (1989) 17:2121 !$#title The nucleotide sequence of a gene for a putative ribosomal !1protein S31 of Drosophila. !$#cross-references MUID:89183616; PMID:2928115 !$#accession S03724 !'##molecule_type DNA !'##residues 1-114 ##label ITO !'##cross-references EMBL:X14247; NID:g8493; PIDN:CAA32463.1; PID:g8494 REFERENCE S03293 !$#authors Itoh, N.; Ohta, K.; Ohta, M.; Kawasaki, T.; Yamashina, I. !$#journal Nucleic Acids Res. (1989) 17:441 !$#title The nucleotide sequence of cDNA for a Drosophila ribosomal !1protein with homology to rat ribosomal protein S26. !$#cross-references MUID:89098400; PMID:2911474 !$#accession S03293 !'##molecule_type mRNA !'##residues 1-114 ##label IT2 !'##cross-references EMBL:X13625; NID:g4469168; PIDN:CAB38441.1; !1PID:g4469169 GENETICS !$#gene FlyBase:RpS26 !'##cross-references FlyBase:FBgn0004413 CLASSIFICATION #superfamily rat ribosomal protein S26 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 114 #molecular-weight 13266 #checksum 2316 SEQUENCE /// ENTRY R4NC26 #type complete TITLE ribosomal protein S26.e - Neurospora crassa ORGANISM #formal_name Neurospora crassa DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 22-Jun-1999 ACCESSIONS S13082; S30612 REFERENCE S13082 !$#authors Tarawneh, K.A.; Wang, Z.; Free, S.J. !$#journal Nucleic Acids Res. (1990) 18:7445 !$#title Nucleotide sequence of a Neurospora crassa ribosomal protein !1gene. !$#cross-references MUID:91081340; PMID:2147995 !$#accession S13082 !'##molecule_type mRNA !'##residues 1-119 ##label TAR !'##cross-references EMBL:X55637; NID:g3075; PIDN:CAA39162.1; PID:g3076 REFERENCE S30612 !$#authors Wang, Z.; Tarawneh, K.A.; Free, S.J. !$#journal Curr. Genet. (1993) 23:330-333 !$#title Isolation, sequencing, and characterization of crp-5, a gene !1encoding a Neurospora ribosomal protein. !$#cross-references MUID:93223266; PMID:8467530 !$#accession S30612 !'##molecule_type DNA !'##residues 1-119 ##label FRE !'##cross-references EMBL:M95597 GENETICS !$#gene crp-5 !$#introns 51/1 CLASSIFICATION #superfamily rat ribosomal protein S26 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 119 #molecular-weight 13560 #checksum 5466 SEQUENCE /// ENTRY R3RT27 #type complete TITLE ribosomal protein S27, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 21-Jul-2000 ACCESSIONS S30297; S48900; S15501 REFERENCE S30297 !$#authors Chan, Y.L.; Suzuki, K.; Olvera, J.; Wool, I.G. !$#journal Nucleic Acids Res. (1993) 21:649-655 !$#title Zinc finger-like motifs in rat ribosomal proteins S27 and !1S29. !$#cross-references MUID:93181260; PMID:8441676 !$#accession S30297 !'##molecule_type mRNA !'##residues 1-84 ##label CHA1 !'##cross-references EMBL:X59375; NID:g57740; PIDN:CAA42019.1; !1PID:g57741 !$#accession S48900 !'##molecule_type protein !'##residues 2-34 ##label CHA2 !'##note the protein is designated as ribosomal protein S27 CLASSIFICATION #superfamily rat ribosomal protein S27 KEYWORDS protein biosynthesis; ribosome; zinc finger FEATURE !$2-84 #product ribosomal protein S27 #status experimental !8#label MAT\ !$37-64 #region zinc finger CCCC motif SUMMARY #length 84 #molecular-weight 9477 #checksum 7196 SEQUENCE /// ENTRY A45631 #type complete TITLE ribosomal protein S27 - Entamoeba histolytica ORGANISM #formal_name Entamoeba histolytica DATE 22-Apr-1993 #sequence_revision 02-Jun-1994 #text_change 22-Jun-1999 ACCESSIONS A45631 REFERENCE A45631 !$#authors Stanley Jr., S.L.; Li, E. !$#journal Mol. Biochem. Parasitol. (1992) 50:185-187 !$#title Isolation of an Entamoeba histolytica cDNA clone encoding a !1protein with a putative zinc finger domain. !$#cross-references MUID:92178287; PMID:1542313 !$#accession A45631 !'##molecule_type mRNA !'##residues 1-84 ##label STA !'##cross-references GB:M77240; NID:g158999; PIDN:AAA29118.1; !1PID:g159000 !'##note sequence extracted from NCBI backbone (NCBIN:85271, !1NCBIP:85272) !'##note the name of this protein is assigned based on sequence homology !1with rat ribosomal protein S27 CLASSIFICATION #superfamily rat ribosomal protein S27 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 84 #molecular-weight 9321 #checksum 3782 SEQUENCE /// ENTRY JC4677 #type complete TITLE ribosomal protein L10a, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 21-Jul-2000 ACCESSIONS JC4677; PC4157 REFERENCE JC4677 !$#authors Olvera, J.; Wool, I.G. !$#journal Biochem. Biophys. Res. Commun. (1996) 220:954-957 !$#title The primary structure of rat ribosomal protein L10a. !$#cross-references MUID:96183058; PMID:8607874 !$#accession JC4677 !'##molecule_type mRNA !'##residues 1-217 ##label OLV1 !'##cross-references EMBL:X93352; NID:g1370288; PIDN:CAA63732.1; !1PID:g1370289 !$#accession PC4157 !'##molecule_type protein !'##residues 199-213 ##label OLV2 !'##experimental_source liver !'##note the protein is designated as ribosomal protein L10a GENETICS !$#gene L10a CLASSIFICATION #superfamily Escherichia coli ribosomal protein L1 KEYWORDS protein biosynthesis; ribosome FEATURE !$91-106 #region lysine-rich SUMMARY #length 217 #molecular-weight 24831 #checksum 1198 SEQUENCE /// ENTRY R5EC1 #type complete TITLE ribosomal protein L1 [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-May-1979 #sequence_revision 30-Jun-1991 #text_change 01-Mar-2002 ACCESSIONS S12573; A02754; C65205 REFERENCE S12572 !$#authors Post, L.E.; Strycharz, G.D.; Nomura, M.; Lewis, H.; Dennis, !1P.P. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1979) 76:1697-1701 !$#title Nucleotide sequence of the ribosomal protein gene cluster !1adjacent to the gene for RNA polymerase subunit beta in !1Escherichia coli. !$#cross-references MUID:79201667; PMID:377281 !$#accession S12573 !'##molecule_type DNA !'##residues 1-234 ##label POS !'##cross-references EMBL:V00339; NID:g42813; PIDN:CAA23622.1; !1PID:g42815 REFERENCE A02754 !$#authors Brauer, D.; Ochsner, I. !$#journal FEBS Lett. (1978) 96:317-321 !$#title The primary structure of protein L1 from the large ribosomal !1subunit of Escherichia coli. !$#cross-references MUID:79086245; PMID:365581 !$#accession A02754 !'##molecule_type protein !'##residues 2-143,'Y',145-234 ##label BRA REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65205 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-234 ##label BLAT !'##cross-references GB:AE000472; GB:U00096; NID:g2367333; !1PIDN:AAC76958.1; PID:g1790416; UWGP:b3984 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note mass spectrographic analysis of post-translational !1modifications; any acid labile modifications may have been !1missed GENETICS !$#gene rplA !$#map_position 90 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX large subunit ribosomal proteins: L1 (PIR:R5EC1), L3 !1(PIR:R5EC3), L2 (PIR:R5EC2), L4 (PIR:R5EC4), L5 (PIR:R5EC5), !1L6 (PIR:R5EC6), L7/L12 (PIR:R5EC7), L9 (PIR:R5EC9), L10 !1(PIR:R5EC10), L11 (PIR:R5EC11), L13 (PIR:R5EC13), L14 !1(PIR:R5EC14), L15 (PIR:R5EC15), L16 (PIR:R5EC16), L17 !1(PIR:R5EC17), L18 (PIR:R5EC18), L19 (PIR:R5EC19) FUNCTION !$#pathway protein biosynthesis !$#note binds 23S rRNA CLASSIFICATION #superfamily Escherichia coli ribosomal protein L1 KEYWORDS protein biosynthesis; ribosome; RNA binding FEATURE !$2-234 #product ribosomal protein L1 #status experimental !8#label MAT SUMMARY #length 234 #molecular-weight 24729 #checksum 9821 SEQUENCE /// ENTRY R5SE1 #type complete TITLE ribosomal protein L1 - Serratia marcescens ORGANISM #formal_name Serratia marcescens DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S01968 REFERENCE S01967 !$#authors Sor, F.; Nomura, M. !$#journal Mol. Gen. Genet. (1987) 210:52-59 !$#title Cloning and DNA sequence determination of the L11 ribosomal !1protein operon of Serratia marcescens and Proteus vulgaris: !1translational feedback regulation of the Escherichia coli !1L11 operon by heterologous L1 proteins. !$#cross-references MUID:88121705; PMID:3323840 !$#accession S01968 !'##molecule_type DNA !'##residues 1-234 ##label SOR !'##cross-references EMBL:X12584; NID:g47255; PIDN:CAA31096.1; !1PID:g47257 COMMENT This protein binds to 23S rRNA. GENETICS !$#gene rplA CLASSIFICATION #superfamily Escherichia coli ribosomal protein L1 KEYWORDS protein biosynthesis; ribosome; RNA binding SUMMARY #length 234 #molecular-weight 24708 #checksum 9824 SEQUENCE /// ENTRY R5EBPV #type complete TITLE ribosomal protein L1 - Proteus vulgaris ORGANISM #formal_name Proteus vulgaris DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S01970 REFERENCE S01967 !$#authors Sor, F.; Nomura, M. !$#journal Mol. Gen. Genet. (1987) 210:52-59 !$#title Cloning and DNA sequence determination of the L11 ribosomal !1protein operon of Serratia marcescens and Proteus vulgaris: !1translational feedback regulation of the Escherichia coli !1L11 operon by heterologous L1 proteins. !$#cross-references MUID:88121705; PMID:3323840 !$#accession S01970 !'##molecule_type DNA !'##residues 1-233 ##label SOR !'##cross-references EMBL:X12585; NID:g45924; PIDN:CAA31098.1; !1PID:g45926 COMMENT This protein binds to 23S rRNA. GENETICS !$#gene rplA CLASSIFICATION #superfamily Escherichia coli ribosomal protein L1 KEYWORDS protein biosynthesis; ribosome; RNA binding SUMMARY #length 233 #molecular-weight 24519 #checksum 8512 SEQUENCE /// ENTRY R5BS1 #type complete TITLE ribosomal protein L1 - Bacillus stearothermophilus ORGANISM #formal_name Bacillus stearothermophilus DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 30-Sep-1993 ACCESSIONS A02755 REFERENCE A91149 !$#authors Kimura, M.; Kimura, J.; Ashman, K. !$#journal Eur. J. Biochem. (1985) 150:491-497 !$#title The complete primary structure of ribosomal proteins L1, !1L14, L15, L23, L24, and L29 from Bacillus !1stearothermophilus. !$#cross-references MUID:85257681; PMID:4018095 !$#accession A02755 !'##molecule_type protein !'##residues 1-232 ##label KIM CLASSIFICATION #superfamily Escherichia coli ribosomal protein L1 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 232 #molecular-weight 24840 #checksum 1592 SEQUENCE /// ENTRY R5HG1T #type complete TITLE ribosomal protein L1 - Thermotoga maritima (strain MSB8) ORGANISM #formal_name Thermotoga maritima DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 21-Jul-2000 ACCESSIONS C44466; H72375; S19900 REFERENCE A44466 !$#authors Liao, D.; Dennis, P.P. !$#journal J. Biol. Chem. (1992) 267:22787-22797 !$#title The organization and expression of essential transcription !1translation component genes in the extremely thermophilic !1eubacterium Thermotoga maritima. !$#cross-references MUID:93054590; PMID:1429627 !$#accession C44466 !'##molecule_type DNA !'##residues 1-233 ##label LIA !'##cross-references EMBL:Z11839; NID:g407020; PIDN:CAA77860.1; !1PID:g48185 !'##note sequence extracted from NCBI backbone (NCBIP:118056) REFERENCE A72200 !$#authors Nelson, K.E.; Clayton, R.A.; Gill, S.R.; Gwinn, M.L.; !1Dodson, R.J.; Haft, D.H.; Hickey, E.K.; Peterson, J.D.; !1Nelson, W.C.; Ketchum, K.A.; McDonald, L.; Utterback, T.R.; !1Malek, J.A.; Linher, K.D.; Garrett, M.M.; Stewart, A.M.; !1Cotton, M.D.; Pratt, M.S.; Phillips, C.A.; Richardson, D.; !1Heidelberg, J.; Sutton, G.G.; Fleischmann, R.D.; White, O.; !1Salzberg, S.L.; Smith, H.O.; Venter, J.C.; Fraser, C.M. !$#journal Nature (1999) 399:323-329 !$#title Evidence for lateral gene transfer between Archaea and !1Bacteria from genome sequence of Thermotoga maritima. !$#cross-references MUID:99287316; PMID:10360571 !$#accession H72375 !'##molecule_type DNA !'##residues 1-233 ##label ARN !'##cross-references GB:AE001723; GB:AE000512; NID:g4980953; !1PIDN:AAD35538.1; PID:g4980961; TIGR:TM0455 !'##experimental_source strain MSB8 GENETICS !$#gene TM0455 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L1 KEYWORDS protein biosynthesis; ribosome; RNA binding SUMMARY #length 233 #molecular-weight 25932 #checksum 8382 SEQUENCE /// ENTRY R5HSLH #type complete TITLE ribosomal protein L1 [validated] - Halobacterium salinarum ALTERNATE_NAMES ribosomal protein HL8 ORGANISM #formal_name Halobacterium salinarum DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 21-Jul-2000 ACCESSIONS S01314; S04119; S08550; S11585 REFERENCE S01314 !$#authors Itoh, T. !$#journal Eur. J. Biochem. (1988) 176:297-303 !$#title Complete nucleotide sequence of the ribosomal 'A' protein !1operon from the archaebacterium, Halobacterium halobium. !$#cross-references MUID:88329082; PMID:2458258 !$#accession S01314 !'##molecule_type DNA !'##residues 1-212 ##label ITO !'##cross-references EMBL:X13008; NID:g43532; PIDN:CAA31430.1; !1PID:g43533 !'##experimental_source strain S9 !'##note the source is designated as Halobacterium halobium REFERENCE S04116 !$#authors Shimmin, L.C.; Dennis, P.P. !$#journal EMBO J. (1989) 8:1225-1235 !$#title Characterization of the L11, L1, L10 and L12 equivalent !1ribosomal protein gene cluster of the halophilic !1archaebacterium Halobacterium cutirubrum. !$#cross-references MUID:89305527; PMID:2743981 !$#accession S04119 !'##molecule_type DNA !'##residues 1-115,'V',117-212 ##label SHI !'##cross-references EMBL:X15078; NID:g43449; PIDN:CAA33179.1; !1PID:g43453 !'##note the source is designated as Halobacterium cutirubrum REFERENCE S07437 !$#authors Matheson, A.T.; Yaguchi, M.; Christensen, P.; Rollin, C.F.; !1Hasnain, S. !$#journal Can. J. Biochem. Cell Biol. (1984) 62:426-433 !$#title Purification, properties, and N-terminal amino acid sequence !1of certain 50S ribosomal subunit proteins from the !1archaebacterium Halobacterium cutirubrum. !$#cross-references MUID:84282108; PMID:6467081 !$#accession S08550 !'##molecule_type protein !'##residues 2-14,'G',16-37 ##label MATH !'##note the source is designated as Halobacterium cutirubrum !'##note the protein is designated as ribosomal protein L8 COMMENT This protein binds to 23S rRNA. CLASSIFICATION #superfamily Escherichia coli ribosomal protein L1 KEYWORDS protein biosynthesis; ribosome; RNA binding FEATURE !$2-212 #product ribosomal protein L1 #status experimental !8#label MAT SUMMARY #length 212 #molecular-weight 23092 #checksum 142 SEQUENCE /// ENTRY R5HS1 #type complete TITLE ribosomal protein L1 [validated] - Haloarcula marismortui ALTERNATE_NAMES ribosomal protein HL8 ORGANISM #formal_name Haloarcula marismortui DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 04-Feb-2000 ACCESSIONS S08421; D28949 REFERENCE S08420 !$#authors Arndt, E.; Weigel, C. !$#journal Nucleic Acids Res. (1990) 18:1285 !$#title Nucleotide sequence of the genes encoding the L11, L1, L10 !1and L12 equivalent ribosomal proteins from the !1archaebacterium Halobacterium marismortui. !$#cross-references MUID:90206791; PMID:2320419 !$#accession S08421 !'##status translation not shown !'##molecule_type DNA !'##residues 1-212 ##label ARN !'##cross-references EMBL:X51430; NID:g43602; PIDN:CAA35794.1; !1PID:g43604 !'##note the source is designated as Halobacterium marismortui REFERENCE A28926 !$#authors Walsh, M.J.; McDougall, J.; Wittmann-Liebold, B. !$#journal Biochemistry (1988) 27:6867-6876 !$#title Extended N-terminal sequencing of proteins of !1archaebacterial ribosomes blotted from two-dimensional gels !1onto glass fiber and poly(vinylidene difluoride) membrane. !$#cross-references MUID:89062418; PMID:3196689 !$#accession D28949 !'##molecule_type protein !'##residues 2-34 ##label WAL !'##note the protein is designated as ribosomal protein L5 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L1 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-212 #product ribosomal protein L1 #status experimental !8#label MAT SUMMARY #length 212 #molecular-weight 23354 #checksum 6222 SEQUENCE /// ENTRY R5MX1 #type complete TITLE ribosomal protein L1 - Methanococcus vannielii ALTERNATE_NAMES ribosomal protein ML6 ORGANISM #formal_name Methanococcus vannielii DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 30-Jun-1993 ACCESSIONS S08390 REFERENCE S08389 !$#authors Baier, G.; Piendl, W.; Redl, B.; Stoeffler, G. !$#journal Nucleic Acids Res. (1990) 18:719-724 !$#title Structure, organization and evolution of the L1 equivalent !1ribosomal protein gene of the archaebacterium Methanococcus !1vannielii. !$#cross-references MUID:90192140; PMID:2107529 !$#accession S08390 !'##molecule_type DNA !'##residues 1-222 ##label BAI !'##cross-references EMBL:X16023 COMMENT This protein binds to 23S rRNA. CLASSIFICATION #superfamily Escherichia coli ribosomal protein L1 KEYWORDS protein biosynthesis; ribosome; RNA binding SUMMARY #length 222 #molecular-weight 24150 #checksum 4142 SEQUENCE /// ENTRY T09551 #type complete TITLE ribosomal protein L4 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 17-Mar-2000 #sequence_revision 17-Mar-2000 #text_change 17-Mar-2000 ACCESSIONS T09551; S39803; S37197 REFERENCE Z16734 !$#authors Bagni, C. !$#submission submitted to the EMBL Data Library, October 1994 !$#accession T09551 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-426 ##label BAG !'##cross-references EMBL:X73974; NID:g560475; PIDN:CAA52154.1; !1PID:g560476 REFERENCE S39803 !$#authors Bagni, C.; Mariottini, P.; Annesi, F.; Amaldi, F. !$#journal Biochim. Biophys. Acta (1993) 1216:475-478 !$#title Human ribosomal protein L4: cloning and sequencing of the !1cDNA and primary structure of the protein. !$#cross-references MUID:94092742; PMID:8268230 !$#accession S39803 !'##status preliminary !'##molecule_type mRNA !'##residues 1-27,29-45,'EKQE',50-336,'TPFFARPGITSSGWIRQLLQQR',359-409, !1'RSLQRRNL',418-426 ##label BA2 !'##cross-references GB:L20868; EMBL:X73974; NID:g307384; !1PIDN:AAA60281.1; PID:g307385 GENETICS !$#gene GDB:RPL4 !'##cross-references GDB:304619 !$#map_position 16p13.3-16p13.3 CLASSIFICATION #superfamily rat ribosomal protein L4 KEYWORDS ribosome FEATURE !$123-139 #region hydrophobic SUMMARY #length 426 #molecular-weight 47672 #checksum 3517 SEQUENCE /// ENTRY JC4277 #type complete TITLE ribosomal protein L4, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 17-Mar-2000 #sequence_revision 17-Mar-2000 #text_change 21-Jul-2000 ACCESSIONS JC4277; PC4076 REFERENCE JC4277 !$#authors Chan, Y.L.; Olvera, J.; Wool, I.G. !$#journal Biochem. Biophys. Res. Commun. (1995) 214:810-818 !$#title The primary structures of rat ribosomal proteins L4 and L41. !$#cross-references MUID:96024571; PMID:7575549 !$#accession JC4277 !'##molecule_type mRNA !'##residues 1-421 ##label CHA1 !'##cross-references EMBL:X82180; NID:g1165138 !$#accession PC4076 !'##molecule_type protein !'##residues 286-305;337-363 ##label CHA2 !'##experimental_source liver !'##note the protein is designated as ribosomal protein L4 CLASSIFICATION #superfamily rat ribosomal protein L4 KEYWORDS ribosome FEATURE !$123-139 #region hydrophobic\ !$188-205 #region basic\ !$303-316 #region basic\ !$356-363 #region alanine-rich SUMMARY #length 421 #molecular-weight 47309 #checksum 3990 SEQUENCE /// ENTRY R5XL1A #type complete TITLE ribosomal protein XL1a - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 17-Mar-2000 ACCESSIONS A24579; T00999 REFERENCE A24579 !$#authors Loreni, F.; Ruberti, I.; Bozzoni, I.; Pierandrei-Amaldi, P.; !1Amaldi, F. !$#journal EMBO J. (1985) 4:3483-3488 !$#title Nucleotide sequence of the L1 ribosomal protein gene of !1Xenopus laevis: remarkable sequence homology among introns. !$#cross-references MUID:86135987; PMID:3841512 !$#accession A24579 !'##molecule_type mRNA !'##residues 1-396 ##label LOR !$#accession T00999 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-391,'P',393-396 ##label LOW !'##cross-references EMBL:X05216; NID:g65081; PIDN:CAA28843.1; !1PID:g65082 CLASSIFICATION #superfamily rat ribosomal protein L4 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 396 #molecular-weight 44909 #checksum 9451 SEQUENCE /// ENTRY R5XL1B #type fragment TITLE ribosomal protein XL1b - African clawed frog (fragment) ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 22-Jun-1999 ACCESSIONS B24579; A02756 REFERENCE A24579 !$#authors Loreni, F.; Ruberti, I.; Bozzoni, I.; Pierandrei-Amaldi, P.; !1Amaldi, F. !$#journal EMBO J. (1985) 4:3483-3488 !$#title Nucleotide sequence of the L1 ribosomal protein gene of !1Xenopus laevis: remarkable sequence homology among introns. !$#cross-references MUID:86135987; PMID:3841512 !$#accession B24579 !'##molecule_type mRNA !'##residues 1-396 ##label LOR !'##cross-references GB:X05217; NID:g65084; PIDN:CAA28844.1; PID:g899428 CLASSIFICATION #superfamily rat ribosomal protein L4 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 396 #checksum 473 SEQUENCE /// ENTRY R5FFL1 #type complete TITLE ribosomal protein DL1 - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Jun-2000 ACCESSIONS S02209; S00882 REFERENCE S02209 !$#authors Rafti, F.; Gargiulo, G.; Manzi, A.; Malva, C.; Graziani, F. !$#journal Nucleic Acids Res. (1989) 17:456 !$#title Sequence of the ribosomal protein cDNA of D.melanogaster !1homologous to the L1 ribosomal protein gene of X.laevis. !$#cross-references MUID:89098414; PMID:2492096 !$#accession S02209 !'##molecule_type mRNA !'##residues 1-407 ##label RAF !'##cross-references EMBL:X13382; NID:g8487; PIDN:CAA31759.1; PID:g8488 REFERENCE S00882 !$#authors Rafti, F.; Gargiulo, G.; Manzi, A.; Malva, C.; Grossi, G.; !1Andone, S.; Graziani, F. !$#journal Nucleic Acids Res. (1988) 16:4915-4926 !$#title Isolation and structural analysis of a ribosomal protein !1gene in D. melanogaster. !$#cross-references MUID:88262486; PMID:3133637 !$#accession S00882 !'##molecule_type DNA !'##residues 63-116,'R',118-185 ##label RAF2 !'##cross-references EMBL:X06881; NID:g8485; PIDN:CAA29998.1; !1PID:g1335649 GENETICS !$#gene FlyBase:RpL1 !'##cross-references FlyBase:FBgn0003279 !$#map_position 3R 98AB !$#introns 62/1; 185/3 CLASSIFICATION #superfamily rat ribosomal protein L4 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 407 #molecular-weight 45755 #checksum 3232 SEQUENCE /// ENTRY R5HS6H #type complete TITLE ribosomal protein L4.eR [validated] - Haloarcula marismortui ALTERNATE_NAMES ribosomal protein HL4; ribosomal protein HL6 ORGANISM #formal_name Haloarcula marismortui DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 04-Feb-2000 ACCESSIONS D35063; A28949; S35654 REFERENCE A35063 !$#authors Arndt, E.; Kroemer, W.; Hatakeyama, T. !$#journal J. Biol. Chem. (1990) 265:3034-3039 !$#title Organization and nucleotide sequence of a gene cluster !1coding for eight ribosomal proteins in the archaebacterium !1Halobacterium marismortui. !$#cross-references MUID:90153945; PMID:2406244 !$#accession D35063 !'##molecule_type DNA !'##residues 1-246 ##label ARN !'##cross-references EMBL:J05222; NID:g148800; PIDN:AAA86860.1; !1PID:g148802 REFERENCE A28926 !$#authors Walsh, M.J.; McDougall, J.; Wittmann-Liebold, B. !$#journal Biochemistry (1988) 27:6867-6876 !$#title Extended N-terminal sequencing of proteins of !1archaebacterial ribosomes blotted from two-dimensional gels !1onto glass fiber and poly(vinylidene difluoride) membrane. !$#cross-references MUID:89062418; PMID:3196689 !$#accession A28949 !'##molecule_type protein !'##residues 1-27;153,'K',155-181 ##label WAL !'##note the protein is designated as ribosomal protein L4 REFERENCE S35654 !$#authors Bergmann, U.; Wittmann-Liebold, B. !$#journal J. Mol. Biol. (1993) 232:693-700 !$#title Localization of proteins HL29 and HL31 from Haloarcula !1marismortui within the 50 S ribosomal subunit by chemical !1crosslinking. !$#cross-references MUID:93347250; PMID:8345527 !$#accession S35654 !'##molecule_type protein !'##residues 34-47;86-117;176-200 ##label BER !'##note the protein is designated as ribosomal protein HmaL4 CLASSIFICATION #superfamily rat ribosomal protein L4 KEYWORDS protein biosynthesis; ribosome FEATURE !$1-246 #product ribosomal protein L4.eR #status experimental !8#label MAT SUMMARY #length 246 #molecular-weight 26420 #checksum 269 SEQUENCE /// ENTRY S43421 #type complete TITLE ribosomal protein L4.eR [validated] - Halobacterium salinarum ALTERNATE_NAMES ribosomal protein HL9 ORGANISM #formal_name Halobacterium salinarum DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 21-Jul-2000 ACCESSIONS S43421; T43817; S08551 REFERENCE S43418 !$#authors Yuki, Y.; Kanechika, R.; Itoh, T. !$#journal Biochim. Biophys. Acta (1993) 1216:335-338 !$#title Nucleotide sequence of the genes encoding the L3, L4 and L23 !1equivalent ribosomal proteins from the archaebacterium !1Halobacterium halobium. !$#cross-references MUID:94060115; PMID:8241282 !$#accession S43421 !'##molecule_type DNA !'##residues 1-248 ##label YUK !'##cross-references EMBL:D14879; NID:g285811; PID:g285814 !'##experimental_source strain S9 !'##note the source is designated as Halobacterium halobium REFERENCE Z22697 !$#authors Itoh, T. !$#submission submitted to the EMBL Data Library, September 1997 !$#accession T43817 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-248 ##label ITO !'##cross-references EMBL:AB006961; PIDN:BAA22271.1 !'##note the source is designated as Halobacterium halobium REFERENCE S07437 !$#authors Matheson, A.T.; Yaguchi, M.; Christensen, P.; Rollin, C.F.; !1Hasnain, S. !$#journal Can. J. Biochem. Cell Biol. (1984) 62:426-433 !$#title Purification, properties, and N-terminal amino acid sequence !1of certain 50S ribosomal subunit proteins from the !1archaebacterium Halobacterium cutirubrum. !$#cross-references MUID:84282108; PMID:6467081 !$#accession S08551 !'##molecule_type protein !'##residues 1-23,'EP',26-31,'K',33 ##label MAT !'##note the source is designated as Halobacterium cutirubrum !'##note the protein is designated as ribosomal protein L9 GENETICS !$#note HhaL4 CLASSIFICATION #superfamily rat ribosomal protein L4 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 248 #molecular-weight 26797 #checksum 5298 SEQUENCE /// ENTRY R5HUL3 #type complete TITLE ribosomal protein L3 precursor, mitochondrial - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 22-Jun-1999 ACCESSIONS A27294; S01607 REFERENCE S01607 !$#authors Ou, J.H.; Yen, T.S.B.; Wang, Y.F.; Kam, W.K.; Rutter, W.J. !$#journal Nucleic Acids Res. (1987) 15:8919-8934 !$#title Cloning and characterization of a human ribosomal protein !1gene with enhanced expression in fetal and neoplastic cells. !$#cross-references MUID:88067705; PMID:2891103 !$#accession A27294 !'##molecule_type mRNA !'##residues 1-348 ##label OUJ !'##cross-references EMBL:X06323; NID:g34753; PIDN:CAA29639.1; !1PID:g34754 GENETICS !$#gene GDB:RPL3 !'##cross-references GDB:118866 !$#map_position 17pter-17qter CLASSIFICATION #superfamily Escherichia coli ribosomal protein L3 KEYWORDS mitochondrion; protein biosynthesis; ribosome SUMMARY #length 348 #molecular-weight 38632 #checksum 9038 SEQUENCE /// ENTRY R5RTL3 #type complete TITLE ribosomal protein L3 precursor, mitochondrial [similarity] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 21-Jul-2000 ACCESSIONS S05472 REFERENCE S01607 !$#authors Ou, J.H.; Yen, T.S.B.; Wang, Y.F.; Kam, W.K.; Rutter, W.J. !$#journal Nucleic Acids Res. (1987) 15:8919-8934 !$#title Cloning and characterization of a human ribosomal protein !1gene with enhanced expression in fetal and neoplastic cells. !$#cross-references MUID:88067705; PMID:2891103 !$#accession S05472 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-347 ##label OUJ CLASSIFICATION #superfamily Escherichia coli ribosomal protein L3 KEYWORDS mitochondrion; protein biosynthesis; ribosome SUMMARY #length 347 #molecular-weight 38253 #checksum 4126 SEQUENCE /// ENTRY R5BYL3 #type complete TITLE ribosomal protein L3 precursor, mitochondrial - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein 269; protein G8520; protein YGR220c; ribosomal protein YmL9 ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 23-Mar-2001 ACCESSIONS S23455; S27032; S27008; S26756; S26637; S57683; S64544; !1S63899 REFERENCE S23455 !$#authors Graack, H.R.; Grohmann, L.; Kitakawa, M.; Schaefer, K.L.; !1Kruft, V. !$#journal Eur. J. Biochem. (1992) 206:373-380 !$#title YmL9, a nucleus-encoded mitochondrial ribosomal protein of !1yeast, is homologous to L3 ribosomal proteins from all !1natural kingdoms and photosynthetic organelles. !$#cross-references MUID:92283262; PMID:1597181 !$#accession S23455 !'##molecule_type DNA !'##residues 1-269 ##label GRA1 !'##cross-references EMBL:X65014 !'##experimental_source strain 07173 !$#accession S27032 !'##molecule_type protein !'##residues 20-53;176-182;257-261 ##label GRA2 !'##experimental_source strain 07173 REFERENCE S27008 !$#authors Graack, H. !$#submission submitted to the EMBL Data Library, March 1992 !$#accession S27008 !'##molecule_type DNA !'##residues 1-138,'Q',140-269 ##label GRA3 !'##cross-references EMBL:X65014; NID:g3983; PIDN:CAA46148.1; PID:g3984 !'##experimental_source strain 07173 REFERENCE S26754 !$#authors Graack, H.R.; Grohmann, L.; Choli, T. !$#journal FEBS Lett. (1988) 242:4-8 !$#title Mitochondrial ribosomes of yeast: isolation of individual !1proteins and N-terminal sequencing. !$#cross-references MUID:89078618; PMID:3060376 !$#accession S26756 !'##molecule_type protein !'##residues 21,'V',22-53 ##label GRA !'##experimental_source strain 07173 !'##note this sequence has been revised in reference S23455 REFERENCE S17255 !$#authors Grohmann, L.; Graack, H.R.; Kruft, V.; Choli, T.; !1Goldschmidt-Reisin, S.; Kitakawa, M. !$#journal FEBS Lett. (1991) 284:51-56 !$#title Extended N-terminal sequencing of proteins of the large !1ribosomal subunit from yeast mitochondria. !$#cross-references MUID:91285106; PMID:2060626 !$#accession S26637 !'##molecule_type protein !'##residues 176,'TF',179-182;257-261 ##label GRO REFERENCE S57680 !$#authors van der Aart, Q.J.M.; Kleine, K.; Steensma, H.Y. !$#submission submitted to the EMBL Data Library, June 1995 !$#description Sequence analysis of the 43 KB !1CRM1-YLM9-PET54-SMI1-PHO81-YHB4-PFK1 region from the right !1arm of Saccharomyces cerevisiae chromosome VII. !$#accession S57683 !'##molecule_type DNA !'##residues 1-269 ##label VAN !'##cross-references EMBL:X87941; NID:g886908; PIDN:CAA61168.1; !1PID:g886912 !'##experimental_source strain S288C REFERENCE S64541 !$#authors van der Aart, Q.J.M.; Steensma, H.Y. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64544 !'##molecule_type DNA !'##residues 1-269 ##label VAW !'##cross-references EMBL:Z73004; NID:g1323394; PIDN:CAA97248.1; !1PID:g1323396; GSPDB:GN00007; MIPS:YGR220c !'##experimental_source strain S288C REFERENCE S63896 !$#authors van der Aart, Q.J.M.; Kleine, K.; Steensma, H.Y. !$#journal Yeast (1996) 12:385-390 !$#title Sequence analysis of the 43 kb !1CRM1-YLM9-PET54-DIE2-SMI1-PHO81-YHB4-PFK1 region from the !1right arm of Saccharomyces cerevisiae chromosome VII. !$#cross-references MUID:96267763; PMID:8701610 !$#accession S63899 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-269 ##label VAF !'##cross-references EMBL:X87941; NID:g886908; PIDN:CAA61168.1; !1PID:g886912 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1995 GENETICS !$#gene SGD:MRPL9; YML9; MIPS:YGR220c !'##cross-references SGD:S0003452; MIPS:YGR220c !$#map_position 7R !$#genome nuclear CLASSIFICATION #superfamily Escherichia coli ribosomal protein L3 KEYWORDS mitochondrion; protein biosynthesis; ribosome FEATURE !$1-19 #domain transit peptide (mitochondrion) #status !8experimental #label TNP\ !$20-269 #product ribosomal protein L3, mitochondrial #status !8experimental #label MAT SUMMARY #length 269 #molecular-weight 29790 #checksum 3227 SEQUENCE /// ENTRY R5EC3 #type complete TITLE ribosomal protein L3 [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-May-1979 #sequence_revision 31-May-1979 #text_change 01-Mar-2002 ACCESSIONS A02757; B02720; B23129; C65125 REFERENCE A02757 !$#authors Muranova, T.A.; Muranov, A.V.; Markova, L.F.; Ovchinnikov, !1Y.A. !$#journal FEBS Lett. (1978) 96:301-305 !$#title The primary structure of ribosomal protein L3 from !1Escherichia coli 70 S ribosomes. !$#cross-references MUID:79086242; PMID:365579 !$#accession A02757 !'##molecule_type protein !'##residues 1-209 ##label MUR !'##experimental_source strain MRE-600 REFERENCE A02720 !$#authors Olins, P.O.; Nomura, M. !$#journal Cell (1981) 26:205-211 !$#title Regulation of the S10 ribosomal protein operon in E. coli: !1nucleotide sequence at the start of the operon. !$#cross-references MUID:82137054; PMID:7037196 !$#accession B02720 !'##molecule_type DNA !'##residues 1-80 ##label OLI !'##cross-references GB:V00344; GB:J01680; NID:g42856; PIDN:CAA23634.1; !1PID:g42858 REFERENCE A23129 !$#authors Zurawski, G.; Zurawski, S.M. !$#journal Nucleic Acids Res. (1985) 13:4521-4526 !$#title Structure of the Escherichia coli S10 ribosomal protein !1operon. !$#cross-references MUID:85242118; PMID:3892488 !$#accession B23129 !'##molecule_type DNA !'##residues 81-209 ##label ZUR !'##cross-references GB:X02613; NID:g42825 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65125 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-209 ##label BLAT !'##cross-references GB:AE000408; GB:U00096; NID:g1789694; !1PIDN:AAC76345.1; PID:g1789716; UWGP:b3320 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note mass spectrographic analysis of post-translational !1modifications; any acid labile modifications may have been !1missed GENETICS !$#gene rplC !$#map_position 73 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX large subunit ribosomal proteins: L1 (PIR:R5EC1), L3 !1(PIR:R5EC3), L2 (PIR:R5EC2), L4 (PIR:R5EC4), L5 (PIR:R5EC5), !1L6 (PIR:R5EC6), L7/L12 (PIR:R5EC7), L9 (PIR:R5EC9), L10 !1(PIR:R5EC10), L11 (PIR:R5EC11), L13 (PIR:R5EC13), L14 !1(PIR:R5EC14), L15 (PIR:R5EC15), L16 (PIR:R5EC16), L17 !1(PIR:R5EC17), L18 (PIR:R5EC18), L19 (PIR:R5EC19) FUNCTION !$#pathway protein biosynthesis !$#note binds 23S rRNA and may be involved in the formation of the !1peptidyltransferase center CLASSIFICATION #superfamily Escherichia coli ribosomal protein L3 KEYWORDS methylated amino acid; protein biosynthesis; ribosome; RNA !1binding FEATURE !$1-209 #product ribosomal protein L3 #status experimental !8#label MAT\ !$150 #modified_site N5-methylglutamine (Gln) #status !8experimental SUMMARY #length 209 #molecular-weight 22243 #checksum 5082 SEQUENCE /// ENTRY E64092 #type complete TITLE ribosomal protein L3 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS E64092 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession E64092 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-208 ##label TIGR !'##cross-references GB:U32761; GB:L42023; NID:g1573780; !1PIDN:AAC22436.1; PID:g1573787; TIGR:HI0777 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L3 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 208 #molecular-weight 22364 #checksum 3476 SEQUENCE /// ENTRY S24363 #type complete TITLE ribosomal protein L3 - Bacillus stearothermophilus ORGANISM #formal_name Bacillus stearothermophilus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S24363; S36085 REFERENCE S24363 !$#authors Herwig, S.; Kruft, V.; Wittmann-Liebold, B. !$#journal Eur. J. Biochem. (1992) 207:877-885 !$#title Primary structures of ribosomal proteins L3 and L4 from !1Bacillus stearothermophilus. !$#cross-references MUID:92362624; PMID:1499563 !$#accession S24363 !'##molecule_type DNA !'##residues 1-213 ##label HER1 !'##cross-references EMBL:X67014; NID:g40101; PIDN:CAA47402.1; !1PID:g40102 !'##note the authors did not translate the codon for residue 1 !$#accession S36085 !'##molecule_type protein !'##residues 2-92;183-213 ##label HER2 GENETICS !$#gene rpl3 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L3 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-213 #product ribosomal protein L3 #status experimental !8#label MAT SUMMARY #length 213 #molecular-weight 23188 #checksum 4488 SEQUENCE /// ENTRY S40188 #type complete TITLE ribosomal protein L3 - Thermotoga maritima (strain MSB8) ORGANISM #formal_name Thermotoga maritima DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S40188; D72250 REFERENCE S37489 !$#authors Sanangelantoni, A.; Tiboni, O. !$#submission submitted to the EMBL Data Library, February 1993 !$#accession S40188 !'##molecule_type DNA !'##residues 1-207 ##label SAN !'##cross-references EMBL:Z21677; NID:g437921; PIDN:CAA79777.1; !1PID:g437923 REFERENCE A72200 !$#authors Nelson, K.E.; Clayton, R.A.; Gill, S.R.; Gwinn, M.L.; !1Dodson, R.J.; Haft, D.H.; Hickey, E.K.; Peterson, J.D.; !1Nelson, W.C.; Ketchum, K.A.; McDonald, L.; Utterback, T.R.; !1Malek, J.A.; Linher, K.D.; Garrett, M.M.; Stewart, A.M.; !1Cotton, M.D.; Pratt, M.S.; Phillips, C.A.; Richardson, D.; !1Heidelberg, J.; Sutton, G.G.; Fleischmann, R.D.; White, O.; !1Salzberg, S.L.; Smith, H.O.; Venter, J.C.; Fraser, C.M. !$#journal Nature (1999) 399:323-329 !$#title Evidence for lateral gene transfer between Archaea and !1Bacteria from genome sequence of Thermotoga maritima. !$#cross-references MUID:99287316; PMID:10360571 !$#accession D72250 !'##molecule_type DNA !'##residues 1-207 ##label ARN !'##cross-references GB:AE001798; GB:AE000512; NID:g4982033; !1PIDN:AAD36566.1; PID:g4982064; TIGR:TM1500 !'##experimental_source strain MSB8 GENETICS !$#gene rplC CLASSIFICATION #superfamily Escherichia coli ribosomal protein L3 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 207 #molecular-weight 22784 #checksum 2069 SEQUENCE /// ENTRY R5KT3 #type complete TITLE ribosomal protein L3, cyanelle - Cyanophora paradoxa cyanelle ORGANISM #formal_name cyanelle Cyanophora paradoxa DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 21-Jan-2000 ACCESSIONS S12810; T06888; S08233 REFERENCE S12809 !$#authors Evrard, J.L.; Johnson, C.; Janssen, I.; Loeffelhardt, W.; !1Weil, J.H.; Kuntz, M. !$#journal Nucleic Acids Res. (1990) 18:1115-1119 !$#title The cyanelle genome of Cyanophora paradoxa, unlike the !1chloroplast genome, codes for the ribosomal L3 protein. !$#cross-references MUID:90206767; PMID:2108429 !$#accession S12810 !'##molecule_type DNA !'##residues 1-209 ##label EVR !'##cross-references EMBL:X17498 !'##experimental_source strain LB555 UTEX REFERENCE Z15840 !$#authors Stirewalt, V.L.; Michalowski, C.B.; Luffelhardt, W.; !1Bohnert, H.J.; Bryant, D.A. !$#submission submitted to the EMBL Data Library, July 1995 !$#description Nucleotide sequence of the cyanelle genome from Cyanophora !1paradoxa. !$#accession T06888 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-209 ##label STI !'##cross-references EMBL:U30821; NID:g1016083; PIDN:AAA81231.1; !1PID:g1016144 !'##experimental_source strain Pringsheim LB555 GENETICS !$#gene rpl3 !$#genome cyanelle !$#start_codon GTG CLASSIFICATION #superfamily Escherichia coli ribosomal protein L3 KEYWORDS cyanelle; protein biosynthesis; ribosome SUMMARY #length 209 #molecular-weight 22459 #checksum 8239 SEQUENCE /// ENTRY R5YM3C #type complete TITLE ribosomal protein L3 - Mycoplasma capricolum ORGANISM #formal_name Mycoplasma capricolum DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 07-Dec-1999 ACCESSIONS S02831 REFERENCE S02830 !$#authors Ohkubo, S.; Muto, A.; Kawauchi, Y.; Yamao, F.; Osawa, S. !$#journal Mol. Gen. Genet. (1987) 210:314-322 !$#title The ribosomal protein gene cluster of Mycoplasma capricolum. !$#cross-references MUID:88142549; PMID:3481422 !$#accession S02831 !'##molecule_type DNA !'##residues 1-223 ##label OHK !'##cross-references EMBL:X06414; NID:g44207; PIDN:CAA29704.1; !1PID:g44209 GENETICS !$#gene rpl3 !$#genetic_code SGC3 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L3 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 223 #molecular-weight 24314 #checksum 9557 SEQUENCE /// ENTRY R5RTL8 #type complete TITLE ribosomal protein L8, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 21-Jul-2000 ACCESSIONS JU0177; S17352 REFERENCE JU0177 !$#authors Chan, Y.L.; Wool, I.G. !$#journal Biochem. Biophys. Res. Commun. (1992) 185:539-547 !$#title The primary structure of rat ribosomal protein L8. !$#cross-references MUID:92304273; PMID:1610349 !$#accession JU0177 !'##molecule_type mRNA !'##residues 1-257 ##label CHA !'##cross-references EMBL:X62145; NID:g57703; PIDN:CAA44071.1; !1PID:g57704 !'##note the protein is designated as ribosomal protein L8 according to !1comigration analysis after in vitro translation CLASSIFICATION #superfamily Escherichia coli ribosomal protein L2 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 257 #molecular-weight 28025 #checksum 6489 SEQUENCE /// ENTRY R5DO2 #type complete TITLE ribosomal protein L8.e - slime mold (Dictyostelium discoideum) ALTERNATE_NAMES ribosomal protein DL2; ribosomal protein V1 ORGANISM #formal_name Dictyostelium discoideum DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 22-Jun-1999 ACCESSIONS S06087 REFERENCE S06087 !$#authors Singleton, C.K. !$#journal Nucleic Acids Res. (1989) 17:7989 !$#title Nucleotide sequence of V1, a ribosomal protein gene from !1Dictyostelium discoideum. !$#cross-references MUID:90016885; PMID:2678007 !$#accession S06087 !'##molecule_type mRNA !'##residues 1-237 ##label SIN !'##cross-references EMBL:X15710; NID:g7354; PIDN:CAA33741.1; PID:g7355 !'##note the authors translated the codon CAC for residues 22 and 23 as !1Gly and TTC for residue 187 as Pro REFERENCE S09166 !$#authors Singleton, C.K.; Delude, R.L.; McPherson, C.E. !$#journal Dev. Biol. (1987) 119:433-441 !$#title Characterization of genes which are deactivated upon the !1onset of development in Dictyostelium discoideum. !$#cross-references MUID:87106347; PMID:3803712 !$#contents annotation; differential expression GENETICS !$#introns 6/2 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L2 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 237 #molecular-weight 26298 #checksum 6695 SEQUENCE /// ENTRY R5ZPD4 #type complete TITLE ribosomal protein L8.e, cytosolic - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES 60s ribosomal protein L2; protein SPAC21E11.02; ribosomal protein K37; ribosomal protein K5; ribosomal protein KD4; ribosomal protein YL2 ORGANISM #formal_name Schizosaccharomyces pombe DATE 31-Mar-1991 #sequence_revision 08-Dec-2000 #text_change 08-Dec-2000 ACCESSIONS T40711; T40134; T38134; T38107; A48328; B48328; C48328; !1S14904; S06692; S62585; S62587 REFERENCE Z21946 !$#authors Lyne, M.; Purnelle, B.; Goffeau, A.; Wood, V.; Rajandream, !1M.A.; Barrell, B.G.; Saunders, D.; Harris, D. !$#submission submitted to the EMBL Data Library, July 1999 !$#accession T40711 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-253 ##label LYN !'##cross-references EMBL:AL096796; EMBL:AL021816; NID:g5441463; !1PIDN:CAB46697.1; PID:g5441467; GSPDB:GN00067; !1SPDB:SPBC839.04 !'##experimental_source strain 972h-; cosmid c839 REFERENCE Z21907 !$#authors Wood, V.; Rajandream, M.A.; Barrell, B.G.; Skelton, J.; !1Churcher, C.M. !$#submission submitted to the EMBL Data Library, June 1997 !$#accession T40134 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-253 ##label WOO !'##cross-references EMBL:Z97211; NID:g6273683; PIDN:CAB10155.1; !1PID:g2239237; GSPDB:GN00067; SPDB:SPBC2F12.07c !'##experimental_source strain 972h-; cosmid c2F12 REFERENCE Z21773 !$#authors McLean, J.; Harris, D.; Wood, V.; Barrell, B.G.; Rajandream, !1M.A.; Walsh, S.V. !$#submission submitted to the EMBL Data Library, November 1995 !$#accession T38134 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-253 ##label MCL !'##cross-references EMBL:Z67999; NID:g1067216; PIDN:CAA91962.1; !1PID:g1067218; GSPDB:GN00066; SPDB:SPAC21E11.02c !'##experimental_source strain 972h-; cosmid c21E11 REFERENCE Z21769 !$#authors Beck, A.; Reinhardt, R.; Murphy, L.; Niblett, D.; Harris, !1D.; Barrell, B.G.; Rajandream, M.A.; Walsh, S.V. !$#submission submitted to the EMBL Data Library, November 1995 !$#accession T38107 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 207-253 ##label MUR !'##cross-references EMBL:Z67998; NID:g1067202; PIDN:CAA91960.1; !1GSPDB:GN00066; SPDB:SPAC1F7.13c !'##experimental_source strain 972h-; cosmid c1F7 !'##note submitted to the EMBL Data Library, November 1995 REFERENCE A48328 !$#authors Gatermann, K.B.; Teletski, C.; Gross, T.; Kaeufer, N.F. !$#journal Curr. Genet. (1989) 16:361-367 !$#title A ribosomal protein gene family from Schizosaccharomyces !1pombe consisting of three active members. !$#cross-references MUID:90124720; PMID:2611912 !$#accession A48328 !'##molecule_type DNA !'##residues 1-134,'S',136-253 ##label GAT1 !'##cross-references GB:X51659; NID:g5047; PIDN:CAA35971.1; PID:g666109 !$#accession B48328 !'##molecule_type DNA !'##residues 1-157,'L',159-253 ##label GAT2 !'##cross-references GB:X51659; NID:g5047 !$#accession C48328 !'##molecule_type DNA !'##residues 1-175,'N',177-253 ##label GAT3 !'##cross-references GB:X51659; NID:g5047 REFERENCE S14904 !$#authors Teletski, C.; Kaeufer, N.F. !$#journal Nucleic Acids Res. (1989) 17:10118 !$#title Sequence of the ribosomal protein gene KD4 from !1Schizosaccharomyces pombe. !$#cross-references MUID:90098792; PMID:2602122 !$#accession S14904 !'##molecule_type DNA !'##residues 1-157,'L',159-253 ##label TEL !'##cross-references EMBL:X16392; NID:g5062; PIDN:CAA34428.1; PID:g5063 !'##experimental_source strain 972 GENETICS GE1 !$#gene RPK5; RPKD4; rpl8-1; SPAC21E11.02c; SPDB:SPAC1F7.13c !$#map_position 1L !$#note one reference says the map is 1R GENETICS GE2 !$#gene rpk5b; SPBC839.04; SPBC2F12.07c !$#map_position 2 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L2 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 253 #molecular-weight 27100 #checksum 1902 SEQUENCE /// ENTRY R5TOL8 #type complete TITLE ribosomal protein L8, cytosolic - tomato ALTERNATE_NAMES ribosomal protein TL2 ORGANISM #formal_name Lycopersicon esculentum #common_name tomato DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 22-Jun-1999 ACCESSIONS JQ2231; S19893 REFERENCE S33899 !$#authors Fleming, A.J.; Mandel, T.; Roth, I.; Kuhlemeier, C. !$#journal Plant Cell (1993) 5:297-309 !$#title The patterns of gene expression in the tomato shoot apical !1meristem. !$#cross-references MUID:93222691; PMID:8467223 !$#accession JQ2231 !'##molecule_type mRNA !'##residues 1-260 ##label FLE !'##cross-references EMBL:X64562; NID:g19342; PIDN:CAA45863.1; !1PID:g19343 !'##experimental_source vegetative shoot apical meristem GENETICS !$#gene rpl2 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L2 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 260 #molecular-weight 28271 #checksum 2069 SEQUENCE /// ENTRY T43819 #type complete TITLE ribosomal protein L2 [similarity] - Halobacterium salinarum ORGANISM #formal_name Halobacterium salinarum DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 21-Jul-2000 ACCESSIONS T43819; S43423 REFERENCE Z22697 !$#authors Itoh, T. !$#submission submitted to the EMBL Data Library, September 1997 !$#accession T43819 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-237 ##label ITO !'##cross-references EMBL:AB006961; PIDN:BAA22273.1 !'##note the source is designated as Halobacterium halobium REFERENCE S43418 !$#authors Yuki, Y.; Kanechika, R.; Itoh, T. !$#journal Biochim. Biophys. Acta (1993) 1216:335-338 !$#title Nucleotide sequence of the genes encoding the L3, L4 and L23 !1equivalent ribosomal proteins from the archaebacterium !1Halobacterium halobium. !$#cross-references MUID:94060115; PMID:8241282 !$#accession S43423 !'##molecule_type DNA !'##residues 1-208 ##label YUK !'##cross-references EMBL:D14879; NID:g285811; PID:g303574 !'##experimental_source strain S9 !'##note the source is designated as Halobacterium halobium GENETICS !$#note HhaL2 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L2 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 237 #molecular-weight 25282 #checksum 2438 SEQUENCE /// ENTRY R5HS2L #type complete TITLE ribosomal protein L2 [similarity] - Haloarcula marismortui ALTERNATE_NAMES ribosomal protein HL4 ORGANISM #formal_name Haloarcula marismortui DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 21-Jul-2000 ACCESSIONS F35063 REFERENCE A35063 !$#authors Arndt, E.; Kroemer, W.; Hatakeyama, T. !$#journal J. Biol. Chem. (1990) 265:3034-3039 !$#title Organization and nucleotide sequence of a gene cluster !1coding for eight ribosomal proteins in the archaebacterium !1Halobacterium marismortui. !$#cross-references MUID:90153945; PMID:2406244 !$#accession F35063 !'##molecule_type DNA !'##residues 1-240 ##label ARN !'##cross-references EMBL:J05222; NID:g148800; PIDN:AAA86862.1; !1PID:g148804 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L2 KEYWORDS protein biosynthesis; ribosome; RNA binding FEATURE !$2-240 #product ribosomal protein L2 #status predicted !8#label MAT SUMMARY #length 240 #molecular-weight 25322 #checksum 7581 SEQUENCE /// ENTRY R5EC2 #type complete TITLE ribosomal protein L2 [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 13-Jun-1983 #sequence_revision 30-Jun-1991 #text_change 01-Mar-2002 ACCESSIONS E23129; A02758; S59057; H65124 REFERENCE A23129 !$#authors Zurawski, G.; Zurawski, S.M. !$#journal Nucleic Acids Res. (1985) 13:4521-4526 !$#title Structure of the Escherichia coli S10 ribosomal protein !1operon. !$#cross-references MUID:85242118; PMID:3892488 !$#accession E23129 !'##molecule_type DNA !'##residues 1-273 ##label ZUR !'##cross-references GB:X02613; NID:g42825; PIDN:CAA26463.1; PID:g42829 REFERENCE A02758 !$#authors Kimura, M.; Mende, L.; Wittmann-Liebold, B. !$#journal FEBS Lett. (1982) 149:304-312 !$#title The primary structure of protein L2 from the Escherichia !1coli ribosome. !$#accession A02758 !'##molecule_type protein !'##residues 2-231,'G',233-234,'H',236-273 ##label KIM REFERENCE S59051 !$#authors Urlaub, H.; Kruft, V.; Bischof, O.; Mueller, E.C.; !1Wittmann-Liebold, B. !$#journal EMBO J. (1995) 14:4578-4588 !$#title Protein-rRNA binding features and their structural and !1functional implications in ribosomes as determined by !1cross-linking studies. !$#cross-references MUID:96003638; PMID:7556101 !$#accession S59057 !'##molecule_type protein !'##residues 60-71;200-208 ##label URL REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65124 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-273 ##label BLAT !'##cross-references GB:AE000408; GB:U00096; NID:g1789694; !1PIDN:AAC76342.1; PID:g1789713; UWGP:b3317 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note mass spectrographic analysis of post-translational !1modifications; any acid labile modifications may have been !1missed GENETICS !$#gene rplB !$#map_position 73 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX large subunit ribosomal proteins: L1 (PIR:R5EC1), L3 !1(PIR:R5EC3), L2 (PIR:R5EC2), L4 (PIR:R5EC4), L5 (PIR:R5EC5), !1L6 (PIR:R5EC6), L7/L12 (PIR:R5EC7), L9 (PIR:R5EC9), L10 !1(PIR:R5EC10), L11 (PIR:R5EC11), L13 (PIR:R5EC13), L14 !1(PIR:R5EC14), L15 (PIR:R5EC15), L16 (PIR:R5EC16), L17 !1(PIR:R5EC17), L18 (PIR:R5EC18), L19 (PIR:R5EC19) FUNCTION !$#pathway protein biosynthesis CLASSIFICATION #superfamily Escherichia coli ribosomal protein L2 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-273 #product ribosomal protein L2 #status experimental !8#label MAT SUMMARY #length 273 #molecular-weight 29860 #checksum 5560 SEQUENCE /// ENTRY R5EB2Y #type complete TITLE ribosomal protein L2 - Yersinia pseudotuberculosis ORGANISM #formal_name Yersinia pseudotuberculosis DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S04143 REFERENCE S04140 !$#authors Gross, U.; Chen, J.H.; Kono, D.H.; Lobo, J.G.; Yu, D.T.Y. !$#journal Nucleic Acids Res. (1989) 17:3601-3602 !$#title High degree of conservation between ribosomal proteins of !1Yersinia pseudotuberculosis and Escherichia coli. !$#cross-references MUID:89263812; PMID:2657663 !$#accession S04143 !'##molecule_type DNA !'##residues 1-274 ##label GRO !'##cross-references EMBL:X14363; NID:g48644; PIDN:CAA32545.1; !1PID:g48648 GENETICS !$#gene rplB CLASSIFICATION #superfamily Escherichia coli ribosomal protein L2 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 274 #molecular-weight 30073 #checksum 9773 SEQUENCE /// ENTRY R5BS2F #type complete TITLE ribosomal protein L2 - Bacillus stearothermophilus ORGANISM #formal_name Bacillus stearothermophilus DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 22-Jun-1999 ACCESSIONS A02759; S10610; S59058 REFERENCE A02759 !$#authors Kimura, M.; Kimura, J.; Watanabe, K. !$#journal Eur. J. Biochem. (1985) 153:289-297 !$#title The primary structure of ribosomal protein L2 from Bacillus !1stearothermophilus. !$#cross-references MUID:86081765; PMID:3908098 !$#accession A02759 !'##molecule_type protein !'##residues 1-275 ##label KIM REFERENCE S10610 !$#authors Kroemer, W.J.; Hatakeyama, T.; Kimura, M. !$#journal Biol. Chem. Hoppe-Seyler (1990) 371:631-636 !$#title Nucleotide sequences of Bacillus stearothermophilus !1ribosomal protein genes: part of the ribosomal S10 operon. !$#cross-references MUID:91025633; PMID:2222862 !$#accession S10610 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 80-275 ##label KRO !'##cross-references GB:X54994; NID:g40104; PIDN:CAA38737.1; PID:g40105 REFERENCE S59051 !$#authors Urlaub, H.; Kruft, V.; Bischof, O.; Mueller, E.C.; !1Wittmann-Liebold, B. !$#journal EMBO J. (1995) 14:4578-4588 !$#title Protein-rRNA binding features and their structural and !1functional implications in ribosomes as determined by !1cross-linking studies. !$#cross-references MUID:96003638; PMID:7556101 !$#accession S59058 !'##molecule_type protein !'##residues 238-246 ##label URL COMMENT This protein is a primary 23S rRNA-binding protein. It has !1peptidyltransferase activity. CLASSIFICATION #superfamily Escherichia coli ribosomal protein L2 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 275 #molecular-weight 30200 #checksum 1102 SEQUENCE /// ENTRY R5YM2C #type complete TITLE ribosomal protein L2 - Mycoplasma capricolum ORGANISM #formal_name Mycoplasma capricolum DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 07-Dec-1999 ACCESSIONS S02834; S05072 REFERENCE S02830 !$#authors Ohkubo, S.; Muto, A.; Kawauchi, Y.; Yamao, F.; Osawa, S. !$#journal Mol. Gen. Genet. (1987) 210:314-322 !$#title The ribosomal protein gene cluster of Mycoplasma capricolum. !$#cross-references MUID:88142549; PMID:3481422 !$#accession S02834 !'##molecule_type DNA !'##residues 1-281 ##label OHK !'##cross-references EMBL:X06414 REFERENCE S05072 !$#authors Muto, A. !$#submission submitted to the EMBL Data Library, January 1989 !$#accession S05072 !'##molecule_type DNA !'##residues 1-6,'N',8-18,'TECSLFNNQKIA',31-35,'GG',38-41,'TA',44-46, !1'KS',49-51,'SS',54-281 ##label MUT GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L2 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 281 #molecular-weight 30996 #checksum 9964 SEQUENCE /// ENTRY R5KT2 #type complete TITLE ribosomal protein L2, cyanelle - Cyanophora paradoxa cyanelle ORGANISM #formal_name cyanelle Cyanophora paradoxa DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S08234; T06887 REFERENCE S08230 !$#authors Evrard, J.L.; Kuntz, M.; Weil, J.H. !$#journal J. Mol. Evol. (1990) 30:16-25 !$#title The nucleotide sequence of five ribosomal protein genes from !1the cyanelles of Cyanophora paradoxa: implications !1concerning the phylogenetic relationship between cyanelles !1and chloroplasts. !$#cross-references MUID:90189174; PMID:2107321 !$#accession S08234 !'##molecule_type DNA !'##residues 1-275 ##label EVR !'##cross-references EMBL:X17498; NID:g11399; PIDN:CAA35537.1; !1PID:g11404 REFERENCE Z15840 !$#authors Stirewalt, V.L.; Michalowski, C.B.; Luffelhardt, W.; !1Bohnert, H.J.; Bryant, D.A. !$#submission submitted to the EMBL Data Library, July 1995 !$#description Nucleotide sequence of the cyanelle genome from Cyanophora !1paradoxa. !$#accession T06887 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-275 ##label STI !'##cross-references EMBL:U30821; NID:g1016083; PIDN:AAA81230.1; !1PID:g1016143 GENETICS !$#gene rpl2 !$#genome cyanelle CLASSIFICATION #superfamily Escherichia coli ribosomal protein L2 KEYWORDS cyanelle; protein biosynthesis; ribosome SUMMARY #length 275 #molecular-weight 30346 #checksum 1727 SEQUENCE /// ENTRY R5LV2 #type complete TITLE ribosomal protein L2 - liverwort (Marchantia polymorpha) chloroplast ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 22-Jun-1999 ACCESSIONS A02760; S01555 REFERENCE A00150 !$#authors Ohyama, K. !$#submission submitted to the EMBL Data Library, October 1986 !$#accession A02760 !'##molecule_type DNA !'##residues 1-277 ##label OHY REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features REFERENCE S01529 !$#authors Fukuzawa, H.; Kohchi, T.; Sano, T.; Shirai, H.; Umesono, K.; !1Inokuchi, H.; Ozeki, H.; Ohyama, K. !$#journal J. Mol. Biol. (1988) 203:333-351 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. III. Gene organization of the large !1single copy region from rbcL to trnI(CAU). !$#cross-references MUID:89068687; PMID:3199436 !$#accession S01555 !'##molecule_type DNA !'##residues 1-277 ##label FUK !'##cross-references GB:X04465; GB:Y00686; NID:g11640; PIDN:CAA28127.1; !1PID:g456520 GENETICS !$#gene rpl2 !$#genome chloroplast !$#introns 133/1 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L2 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 277 #molecular-weight 31163 #checksum 288 SEQUENCE /// ENTRY R5NT2 #type complete TITLE ribosomal protein L2 - common tobacco chloroplast ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 17-Feb-1995 ACCESSIONS A02761; B25943 REFERENCE A00149 !$#authors Sugiura, M. !$#submission submitted to the EMBL Data Library, August 1986 !$#accession A02761 !'##molecule_type DNA !'##residues 1-274 ##label SUG !'##experimental_source cv. Bright Yellow 4 REFERENCE A38013 !$#authors Shinozaki, K.; Ohme, M.; Tanaka, M.; Wakasugi, T.; !1Hayashida, N.; Matsubayashi, T.; Zaita, N.; Chunwongse, J.; !1Obokata, J.; Yamaguchi-Shinozaki, K.; Ohto, C.; Torazawa, !1K.; Meng, B.Y.; Sugita, M.; Deno, H.; Kamogashira, T.; !1Yamada, K.; Kusuda, J.; Takaiwa, F.; Kato, A.; Tohdoh, N.; !1Shimada, H.; Sugiura, M. !$#journal EMBO J. (1986) 5:2043-2049 !$#title The complete nucleotide sequence of the tobacco chloroplast !1genome: its gene organization and expression. !$#contents annotation; gene organization, sites, features REFERENCE A94118 !$#authors Tanaka, M.; Wakasugi, T.; Sugita, M.; Shinozaki, K.; !1Sugiura, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:6030-6034 !$#title Genes for the eight ribosomal proteins are clustered on the !1chloroplast genome of tobacco (Nicotiana tabacum): !1similarity to the S10 and spc operons of Escherichia coli. !$#cross-references MUID:86287388; PMID:3016736 !$#accession B25943 !'##molecule_type DNA !'##residues 1-274 ##label TAN GENETICS !$#gene rpl2 !$#genome chloroplast !$#introns 131/1 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L2 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 274 #molecular-weight 30010 #checksum 6166 SEQUENCE /// ENTRY R5NT2D #type complete TITLE ribosomal protein L2 - Debney's tobacco chloroplast ORGANISM #formal_name chloroplast Nicotiana debneyi #common_name Debney's tobacco DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 21-Jul-2000 ACCESSIONS S07356 REFERENCE S07356 !$#authors Zurawski, G.; Bottomley, W.; Whitfeld, P.R. !$#journal Nucleic Acids Res. (1984) 12:6547-6558 !$#title Junctions of the large single copy region and the inverted !1repeats in Spinacia oleracea and Nicotiana debneyi !1chloroplast DNA: sequence of the genes for tRNA(His) and the !1ribosomal proteins S19 and L2. !$#cross-references MUID:84297246; PMID:6089120 !$#accession S07356 !'##molecule_type DNA !'##residues 1-266 ##label ZUR !'##cross-references EMBL:X00798; NID:g11748; PIDN:CAB52367.1; !1PID:g5708092 !'##note the authors translated the codon AGT for residues 20 and 202 as !1Arg GENETICS !$#gene rpl2 !$#genome chloroplast !$#introns 131/1 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L2 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 266 #molecular-weight 28901 #checksum 7362 SEQUENCE /// ENTRY R5RZ2 #type complete TITLE ribosomal protein L2 - rice chloroplast ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 17-Feb-1995 ACCESSIONS JQ0270; S05150; JA0093 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0270 !'##molecule_type DNA !'##residues 1-273 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05150 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-273 ##label HIR !'##experimental_source cv. Nihonbare !'##note this sequence was submitted to EMBL, July 1989 REFERENCE JA0092 !$#authors Moon, E.; Wu, R. !$#journal Gene (1988) 70:1-12 !$#title Organization and nucleotide sequence of genes at both !1junctions between the two inverted repeats and the large !1single-copy region in the rice chloroplast genome. !$#cross-references MUID:89196901; PMID:3240862 !$#accession JA0093 !'##molecule_type DNA !'##residues 1-68,'E',70-199,'K',201-229,'MGAVKGKPPLVEKNPQP',247-273 !1##label MOO GENETICS !$#gene rpl2 !$#genome chloroplast !$#start_codon ACG !$#introns 131/1 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L2 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 273 #molecular-weight 29942 #checksum 2025 SEQUENCE /// ENTRY R5ZM2 #type complete TITLE ribosomal protein L2 - maize chloroplast ORGANISM #formal_name chloroplast Zea mays #common_name maize DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 21-Jul-2000 ACCESSIONS S10500; S17874; S58639; S58595 REFERENCE S10500 !$#authors Kavousi, M.; Giese, K.; Larrinua, I.M.; McLaughlin, W.E.; !1Subramanian, A.R. !$#journal Nucleic Acids Res. (1990) 18:4244 !$#title Nucleotide sequence and map positions of the duplicated gene !1for maize (Zea mays) chloroplast ribosomal protein L2. !$#cross-references MUID:90332419; PMID:2377464 !$#accession S10500 !'##molecule_type DNA !'##residues 1-273 ##label KAV !'##cross-references EMBL:X53066 REFERENCE S17874 !$#authors Hoch, B.; Maier, R.M.; Appel, K.; Igloi, G.L.; Koessel, H. !$#journal Nature (1991) 353:178-180 !$#title Editing of a chloroplast mRNA by creation of an initiation !1codon. !$#cross-references MUID:91367263; PMID:1653905 !$#accession S17874 !'##molecule_type mRNA !'##residues 1-150 ##label HOC !'##cross-references EMBL:X62070 REFERENCE S58531 !$#authors Maier, R.M.; Neckermann, K.; Igloi, G.L.; Koessel, H. !$#journal J. Mol. Biol. (1995) 251:614-628 !$#title Complete sequence of the maize chloroplast genome: gene !1content, hotspots of divergence and fine tuning of genetic !1information by transcript editing. !$#cross-references MUID:95395841; PMID:7666415 !$#accession S58639 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-273 ##label MAI !'##cross-references EMBL:X86563; NID:g902200; PIDN:CAA60329.1; !1PID:g2673858 !'##genetics GEN1 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1995 !$#accession S58595 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-273 ##label MAW !'##cross-references EMBL:X86563; NID:g902200; PIDN:CAA60329.1; !1PID:g2673858 !'##genetics GEN2 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1995 GENETICS GEN1 !$#map_position IR(A) !$#genome chloroplast !$#start_codon ACG !$#introns 130/3 !$#note the start codon AUG results from mRNA editing of ACG GENETICS GEN2 !$#map_position IR(B) !$#genome chloroplast !$#introns 130/3 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L2 KEYWORDS chloroplast; protein biosynthesis; ribosome; RNA editing SUMMARY #length 273 #molecular-weight 30065 #checksum 1226 SEQUENCE /// ENTRY R5SP2 #type complete TITLE ribosomal protein L2 - spinach chloroplast ALTERNATE_NAMES ribosomal protein CS-L4 ORGANISM #formal_name chloroplast Spinacia oleracea #common_name spinach DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S07918; S00730; A37536; S12167 REFERENCE S07356 !$#authors Zurawski, G.; Bottomley, W.; Whitfeld, P.R. !$#journal Nucleic Acids Res. (1984) 12:6547-6558 !$#title Junctions of the large single copy region and the inverted !1repeats in Spinacia oleracea and Nicotiana debneyi !1chloroplast DNA: sequence of the genes for tRNA(His) and the !1ribosomal proteins S19 and L2. !$#cross-references MUID:84297246; PMID:6089120 !$#accession S07918 !'##molecule_type DNA !'##residues 1-286 ##label ZUR !'##cross-references EMBL:X00797; NID:g12302; PIDN:CAA25377.1; !1PID:g12303 REFERENCE S00728 !$#authors Thomas, F.; Massenet, O.; Dorne, A.M.; Briat, J.F.; Mache, !1R. !$#journal Nucleic Acids Res. (1988) 16:2461-2472 !$#title Expression of the rpl23, rpl2 and rps19 genes in spinach !1chloroplasts. !$#cross-references MUID:88203193; PMID:3362671 !$#accession S00730 !'##molecule_type DNA !'##residues 1-20 ##label THO !'##cross-references EMBL:X07462; NID:g12319; PIDN:CAA30345.1; !1PID:g12321 !$#accession A37536 !'##molecule_type protein !'##residues 'X',3-11 ##label THO2 REFERENCE S12167 !$#authors Kamp, R.M.; Srinivasa, B.R.; von Knoblauch, K.; Subramanian, !1A.R. !$#journal Biochemistry (1987) 26:5866-5870 !$#title Occurrence of a methylated protein in chloroplast ribosomes. !$#accession S12167 !'##molecule_type protein !'##residues 2-14;122-128;131-136;221-229 ##label KAM GENETICS !$#gene rpl2 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein L2 KEYWORDS chloroplast; methylated amino end; protein biosynthesis; !1ribosome FEATURE !$2-286 #product ribosomal protein L2 #status experimental !8#label MAT\ !$2 #modified_site methylated amino end (Ala) (in mature !8form) #status experimental SUMMARY #length 286 #molecular-weight 31256 #checksum 9231 SEQUENCE /// ENTRY R5PPL2 #type complete TITLE ribosomal protein L2 - Paramecium tetraurelia mitochondrion ORGANISM #formal_name mitochondrion Paramecium tetraurelia DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 07-Dec-1999 ACCESSIONS JS0236; S07738 REFERENCE JS0231 !$#authors Pritchard, A.E.; Venuti, S.E.; Ghalambor, M.A.; Sable, C.L.; !1Cummings, D.J. !$#journal Gene (1989) 78:121-134 !$#title An unusual region of Paramecium mitochondrial DNA containing !1chloroplast-like genes. !$#cross-references MUID:89357489; PMID:2670676 !$#accession JS0236 !'##molecule_type DNA !'##residues 1-259 ##label PRI !'##cross-references GB:M26930; NID:g341550; PIDN:AAA79258.1; !1PID:g1019633 !'##experimental_source strain sp. 4.51 !'##note the source is designated as Paramecium aurelia species 4 stock !151, now designated Paramecium tetraurelia, ATCC 30567 REFERENCE S07725 !$#authors Pritchard, A.E.; Seilhamer, J.J.; Mahalingam, R.; Sable, !1C.L.; Venuti, S.E.; Cummings, D.J. !$#journal Nucleic Acids Res. (1990) 18:173-180 !$#title Nucleotide sequence of the mitochondrial genome of !1Paramecium. !$#cross-references MUID:90174913; PMID:2308823 !$#accession S07738 !'##status translation not shown !'##molecule_type DNA !'##residues 1-259 ##label PRI2 !'##cross-references EMBL:X15917; NID:g13256; PIDN:CAA34047.1; !1PID:g578755 GENETICS !$#gene rpl2 !$#genome mitochondrion !$#genetic_code SGC6 !$#start_codon GTG CLASSIFICATION #superfamily Escherichia coli ribosomal protein L2 KEYWORDS mitochondrion; protein biosynthesis; ribosome SUMMARY #length 259 #molecular-weight 29801 #checksum 960 SEQUENCE /// ENTRY R5EC4 #type complete TITLE ribosomal protein L4 [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 28-Feb-1981 #sequence_revision 28-Feb-1981 #text_change 01-Mar-2002 ACCESSIONS C23129; A02762; S59059; B65125 REFERENCE A23129 !$#authors Zurawski, G.; Zurawski, S.M. !$#journal Nucleic Acids Res. (1985) 13:4521-4526 !$#title Structure of the Escherichia coli S10 ribosomal protein !1operon. !$#cross-references MUID:85242118; PMID:3892488 !$#accession C23129 !'##molecule_type DNA !'##residues 1-201 ##label ZUR !'##cross-references GB:X02613; NID:g42825; PIDN:CAA26461.1; PID:g42828 REFERENCE A02762 !$#authors Kimura, M.; Wittmann-Liebold, B. !$#journal FEBS Lett. (1980) 121:317-322 !$#title The primary structure of protein L4 from the large subunit !1of the Escherichia coli ribosome. !$#accession A02762 !'##molecule_type protein !'##residues 1-201 ##label KIM REFERENCE S59051 !$#authors Urlaub, H.; Kruft, V.; Bischof, O.; Mueller, E.C.; !1Wittmann-Liebold, B. !$#journal EMBO J. (1995) 14:4578-4588 !$#title Protein-rRNA binding features and their structural and !1functional implications in ribosomes as determined by !1cross-linking studies. !$#cross-references MUID:96003638; PMID:7556101 !$#accession S59059 !'##molecule_type protein !'##residues 26-50 ##label URL REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65125 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-201 ##label BLAT !'##cross-references GB:AE000408; GB:U00096; NID:g1789694; !1PIDN:AAC76344.1; PID:g1789715; UWGP:b3319 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note no post-translational modifications were observed in mass !1spectrographic analysis; any acid labile modifications may !1have been missed GENETICS !$#gene rplD !$#map_position 73 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX large subunit ribosomal proteins: L1 (PIR:R5EC1), L3 !1(PIR:R5EC3), L2 (PIR:R5EC2), L4 (PIR:R5EC4), L5 (PIR:R5EC5), !1L6 (PIR:R5EC6), L7/L12 (PIR:R5EC7), L9 (PIR:R5EC9), L10 !1(PIR:R5EC10), L11 (PIR:R5EC11), L13 (PIR:R5EC13), L14 !1(PIR:R5EC14), L15 (PIR:R5EC15), L16 (PIR:R5EC16), L17 !1(PIR:R5EC17), L18 (PIR:R5EC18), L19 (PIR:R5EC19) FUNCTION !$#pathway protein biosynthesis !$#note binds 23S rRNA CLASSIFICATION #superfamily Escherichia coli ribosomal protein L4 KEYWORDS protein biosynthesis; ribosome; RNA binding FEATURE !$1-201 #product ribosomal protein L4 #status experimental !8#label MAT SUMMARY #length 201 #molecular-weight 22086 #checksum 2312 SEQUENCE /// ENTRY R5EB4Y #type complete TITLE ribosomal protein L4 - Yersinia pseudotuberculosis ORGANISM #formal_name Yersinia pseudotuberculosis DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S04141 REFERENCE S04140 !$#authors Gross, U.; Chen, J.H.; Kono, D.H.; Lobo, J.G.; Yu, D.T.Y. !$#journal Nucleic Acids Res. (1989) 17:3601-3602 !$#title High degree of conservation between ribosomal proteins of !1Yersinia pseudotuberculosis and Escherichia coli. !$#cross-references MUID:89263812; PMID:2657663 !$#accession S04141 !'##molecule_type DNA !'##residues 1-201 ##label GRO !'##cross-references EMBL:X14363; NID:g48644; PIDN:CAA32543.1; !1PID:g48646 GENETICS !$#gene rplD CLASSIFICATION #superfamily Escherichia coli ribosomal protein L4 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 201 #molecular-weight 22009 #checksum 3172 SEQUENCE /// ENTRY R5YM4C #type complete TITLE ribosomal protein L4 - Mycoplasma capricolum ORGANISM #formal_name Mycoplasma capricolum DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 07-Dec-1999 ACCESSIONS S02832 REFERENCE S02830 !$#authors Ohkubo, S.; Muto, A.; Kawauchi, Y.; Yamao, F.; Osawa, S. !$#journal Mol. Gen. Genet. (1987) 210:314-322 !$#title The ribosomal protein gene cluster of Mycoplasma capricolum. !$#cross-references MUID:88142549; PMID:3481422 !$#accession S02832 !'##molecule_type DNA !'##residues 1-208 ##label OHK !'##cross-references EMBL:X06414; NID:g44207; PIDN:CAA29705.1; !1PID:g44210 GENETICS !$#gene rpl4 !$#genetic_code SGC3 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L4 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 208 #molecular-weight 23109 #checksum 4971 SEQUENCE /// ENTRY R5RT3L #type complete TITLE ribosomal protein L3, cytosolic [validated] - rat ALTERNATE_NAMES ribosomal protein RL4 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 21-Jul-2000 ACCESSIONS JQ1536; S11553; S17318 REFERENCE JQ1536 !$#authors Kuwano, Y.; Wool, I.G. !$#journal Biochem. Biophys. Res. Commun. (1992) 187:58-64 !$#title The primary structure of rat ribosomal protein L3. !$#cross-references MUID:92392382; PMID:1520347 !$#accession JQ1536 !'##molecule_type mRNA !'##residues 1-403 ##label KU2 !'##cross-references EMBL:X62166; NID:g57697; PIDN:CAA44095.1; !1PID:g57698 !'##experimental_source liver !'##note the protein is designated as ribosomal protein L3 according to !1comigration analysis after in vitro translation REFERENCE S07293 !$#authors Otaka, E.; Higo, K.I.; Itoh, T. !$#journal Mol. Gen. Genet. (1983) 191:519-524 !$#title Yeast ribosomal proteins: VII. Cytoplasmic ribosomal !1proteins from Schizosaccharomyces pombe. !$#cross-references MUID:84038947; PMID:6355773 !$#accession S11553 !'##molecule_type protein !'##residues 2-6,'Z',8-12,'X',14-18,'T',20 ##label OTA !'##note the protein was identified as ribosomal protein L4 CLASSIFICATION #superfamily rat ribosomal protein L3 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-403 #product ribosomal protein L3 #status experimental !8#label MAT SUMMARY #length 403 #molecular-weight 46136 #checksum 2234 SEQUENCE /// ENTRY R5BY4E #type complete TITLE ribosomal protein L3.e, cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein O2812; protein YOR063w; ribosomal protein rp1; ribosomal protein YL1; tricodermin resistance protein ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1991 #sequence_revision 02-Aug-1996 #text_change 16-Jun-2000 ACCESSIONS S66946; S05843; S11552; S45512 REFERENCE S66929 !$#authors Bohn, C.; Bolotin-Fukuhara, M.; Daignan-Fornier, B.; Dang, !1D.V.; Valens, M. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S66946 !'##molecule_type DNA !'##residues 1-387 ##label BOH !'##cross-references EMBL:Z74971; NID:g1420206; PIDN:CAA99256.1; !1PID:g1420207; GSPDB:GN00015; MIPS:YOR063w !'##experimental_source strain S288C REFERENCE S05843 !$#authors Schultz, L.D.; Friesen, J.D. !$#journal J. Bacteriol. (1983) 155:8-14 !$#title Nucleotide sequence of the tcm1 gene (ribosomal protein L3) !1of Saccharomyces cerevisiae. !$#cross-references MUID:83238226; PMID:6305925 !$#accession S05843 !'##molecule_type DNA !'##residues 1-254,'C',256-387 ##label SCH !'##cross-references EMBL:J01351; NID:g172454; PIDN:AAA88732.1; !1PID:g1197059 !'##note this sequence is from the tricodermin-resistant mutant tcm1 REFERENCE S07293 !$#authors Otaka, E.; Higo, K.I.; Itoh, T. !$#journal Mol. Gen. Genet. (1983) 191:519-524 !$#title Yeast ribosomal proteins: VII. Cytoplasmic ribosomal !1proteins from Schizosaccharomyces pombe. !$#cross-references MUID:84038947; PMID:6355773 !$#accession S11552 !'##molecule_type protein !'##residues 2-18,'X',20 ##label OTA REFERENCE S45500 !$#authors Takahura, H.; Tsunasawa, S.; Miyagi, M.; Warner, J.R. !$#journal J. Biol. Chem. (1992) 267:5442-5445 !$#title NH2-terminal acetylation of ribosomal proteins of !1Saccharomyces cerevisiae. !$#cross-references MUID:92184799; PMID:1544921 !$#accession S45512 !'##molecule_type protein !'##residues 2-10 ##label TAK GENETICS !$#gene SGD:TCM1; MIPS:YOR063w !'##cross-references SGD:S0005589; MIPS:YOR063w !$#map_position 15R CLASSIFICATION #superfamily rat ribosomal protein L3 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-387 #product ribosomal protein L3.e #status experimental !8#label MAT SUMMARY #length 387 #molecular-weight 43757 #checksum 179 SEQUENCE /// ENTRY T43816 #type complete TITLE ribosomal protein L3.eR [similarity] - Halobacterium salinarum ORGANISM #formal_name Halobacterium salinarum DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 21-Jul-2000 ACCESSIONS T43816; S43420 REFERENCE Z22697 !$#authors Itoh, T. !$#submission submitted to the EMBL Data Library, September 1997 !$#accession T43816 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-330 ##label ITO !'##cross-references EMBL:AB006961; PIDN:BAA22270.1 !'##note the source is designated as Halobacterium halobium REFERENCE S43418 !$#authors Yuki, Y.; Kanechika, R.; Itoh, T. !$#journal Biochim. Biophys. Acta (1993) 1216:335-338 !$#title Nucleotide sequence of the genes encoding the L3, L4 and L23 !1equivalent ribosomal proteins from the archaebacterium !1Halobacterium halobium. !$#cross-references MUID:94060115; PMID:8241282 !$#accession S43420 !'##molecule_type DNA !'##residues 1-330 ##label YUK !'##cross-references EMBL:D14879; NID:g285811; PID:g285813 !'##experimental_source strain S9 !'##note the source is designated as Halobacterium halobium GENETICS !$#note HhaL3 CLASSIFICATION #superfamily rat ribosomal protein L3 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 330 #molecular-weight 36154 #checksum 626 SEQUENCE /// ENTRY R5HS3L #type complete TITLE ribosomal protein L3 [similarity] - Haloarcula marismortui ALTERNATE_NAMES ribosomal protein HL1; ribosomal protein HL3.eR ORGANISM #formal_name Haloarcula marismortui DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 21-Jul-2000 ACCESSIONS C35063 REFERENCE A35063 !$#authors Arndt, E.; Kroemer, W.; Hatakeyama, T. !$#journal J. Biol. Chem. (1990) 265:3034-3039 !$#title Organization and nucleotide sequence of a gene cluster !1coding for eight ribosomal proteins in the archaebacterium !1Halobacterium marismortui. !$#cross-references MUID:90153945; PMID:2406244 !$#accession C35063 !'##molecule_type DNA !'##residues 1-338 ##label ARN !'##cross-references EMBL:J05222; NID:g148800; PIDN:AAA86859.1; !1PID:g148801 CLASSIFICATION #superfamily rat ribosomal protein L3 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-338 #product ribosomal protein L3 #status predicted !8#label MAT SUMMARY #length 338 #molecular-weight 37282 #checksum 5432 SEQUENCE /// ENTRY A64322 #type complete TITLE ribosomal protein L3.eR - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 13-Sep-1996 #sequence_revision 04-Oct-1996 #text_change 21-Jul-2000 ACCESSIONS A64322 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession A64322 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-335 ##label BUL !'##cross-references GB:U67474; GB:L77117; NID:g1590921; !1PIDN:AAB98161.1; PID:g1590928; TIGR:MJ0176 GENETICS !$#map_position FOR178423-179430 CLASSIFICATION #superfamily rat ribosomal protein L3 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 335 #molecular-weight 38117 #checksum 7584 SEQUENCE /// ENTRY R5EC5 #type complete TITLE ribosomal protein L5 [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 12-Aug-1981 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS G65123; I41327; A02763 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65123 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-179 ##label BLAT !'##cross-references GB:AE000408; GB:U00096; NID:g1789694; !1PIDN:AAC76333.1; PID:g1789704; UWGP:b3308 !'##experimental_source strain K-12, substrain MG1655 REFERENCE I41326 !$#authors Olins, P.O.; Nomura, M. !$#journal Nucleic Acids Res. (1981) 9:1757-1764 !$#title Translational regulation by ribosomal protein S8 in !1Escherichia coli: Structural homology between rRNA binding !1site and feedback target on mRNA. !$#cross-references MUID:81199003; PMID:6262737 !$#accession I41327 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-18 ##label OLI !'##cross-references GB:M10195; NID:g146572; PIDN:AAA24051.1; !1PID:g146574 REFERENCE A02763 !$#authors Chen, R.; Ehrke, G. !$#journal FEBS Lett. (1976) 69:240-245 !$#title The primary structure of the 5 S RNA binding protein L5 of !1Escherichia coli ribosomes. !$#cross-references MUID:77048835; PMID:791672 !$#accession A02763 !'##molecule_type protein !'##residues 2-93,'Q',95-126,'D',128-179 ##label CHE !'##experimental_source strain K REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note mass spectrographic analysis of post-translational !1modifications; any acid labile modifications may have been !1missed GENETICS !$#gene rplE !$#map_position 73 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX large subunit ribosomal proteins: L1 (PIR:R5EC1), L3 !1(PIR:R5EC3), L2 (PIR:R5EC2), L4 (PIR:R5EC4), L5 (PIR:R5EC5), !1L6 (PIR:R5EC6), L7/L12 (PIR:R5EC7), L9 (PIR:R5EC9), L10 !1(PIR:R5EC10), L11 (PIR:R5EC11), L13 (PIR:R5EC13), L14 !1(PIR:R5EC14), L15 (PIR:R5EC15), L16 (PIR:R5EC16), L17 !1(PIR:R5EC17), L18 (PIR:R5EC18), L19 (PIR:R5EC19) FUNCTION !$#pathway protein biosynthesis !$#note mediates inclusion of 6S rRNA in the large ribosomal subunit CLASSIFICATION #superfamily Escherichia coli ribosomal protein L5 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-179 #product ribosomal protein L5 #status experimental !8#label MAT SUMMARY #length 179 #molecular-weight 20301 #checksum 5899 SEQUENCE /// ENTRY R5BS5 #type complete TITLE ribosomal protein L5 - Bacillus subtilis ALTERNATE_NAMES BL6 ORGANISM #formal_name Bacillus subtilis DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jun-2000 ACCESSIONS S05994; A69695 REFERENCE S05989 !$#authors Henkin, T.M.; Moon, S.H.; Mattheakis, L.C.; Nomura, M. !$#journal Nucleic Acids Res. (1989) 17:7469-7486 !$#title Cloning and analysis of the spc ribosomal protein operon of !1Bacillus subtilis: comparison with the spc operon of !1Escherichia coli. !$#cross-references MUID:90016806; PMID:2508062 !$#accession S05994 !'##molecule_type DNA !'##residues 1-179 ##label HEN !'##cross-references EMBL:X15664; NID:g40146; PIDN:CAA33703.1; !1PID:g40152 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69695 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-179 ##label KUN !'##cross-references GB:Z99104; GB:AL009126; NID:g2632267; !1PIDN:CAB11904.1; PID:g2632395 !'##experimental_source strain 168 GENETICS !$#gene rplE CLASSIFICATION #superfamily Escherichia coli ribosomal protein L5 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 179 #molecular-weight 20147 #checksum 9553 SEQUENCE /// ENTRY R5BS5F #type complete TITLE ribosomal protein L5 - Bacillus stearothermophilus ORGANISM #formal_name Bacillus stearothermophilus DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 30-Jun-1993 ACCESSIONS A29102 REFERENCE A29102 !$#authors Kimura, J.; Kimura, M. !$#journal FEBS Lett. (1987) 210:85-90 !$#title The complete amino acid sequences of the 5 S rRNA binding !1proteins L5 and L18 from the moderate thermophile Bacillus !1stearothermophilus ribosome. !$#cross-references MUID:87105936; PMID:3542562 !$#accession A29102 !'##molecule_type protein !'##residues 1-179 ##label KIM CLASSIFICATION #superfamily Escherichia coli ribosomal protein L5 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 179 #molecular-weight 20159 #checksum 9685 SEQUENCE /// ENTRY R5YM5C #type complete TITLE ribosomal protein L5 - Mycoplasma capricolum ORGANISM #formal_name Mycoplasma capricolum DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 07-Dec-1999 ACCESSIONS S02843 REFERENCE S02830 !$#authors Ohkubo, S.; Muto, A.; Kawauchi, Y.; Yamao, F.; Osawa, S. !$#journal Mol. Gen. Genet. (1987) 210:314-322 !$#title The ribosomal protein gene cluster of Mycoplasma capricolum. !$#cross-references MUID:88142549; PMID:3481422 !$#accession S02843 !'##molecule_type DNA !'##residues 1-180 ##label OHK !'##cross-references EMBL:X06414; NID:g44207; PIDN:CAA29716.1; !1PID:g44221 GENETICS !$#gene rpl5 !$#genetic_code SGC3 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L5 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 180 #molecular-weight 20429 #checksum 6339 SEQUENCE /// ENTRY R5KT5 #type complete TITLE ribosomal protein L5 - Cyanophora paradoxa cyanelle ORGANISM #formal_name cyanelle Cyanophora paradoxa DATE 31-Dec-1990 #sequence_revision 21-May-1999 #text_change 22-Jun-1999 ACCESSIONS T06880; S07067; S12216 REFERENCE Z15840 !$#authors Stirewalt, V.L.; Michalowski, C.B.; Luffelhardt, W.; !1Bohnert, H.J.; Bryant, D.A. !$#submission submitted to the EMBL Data Library, July 1995 !$#description Nucleotide sequence of the cyanelle genome from Cyanophora !1paradoxa. !$#accession T06880 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-181 ##label STI !'##cross-references EMBL:U30821; NID:g1016083; PIDN:AAA81223.1; !1PID:g1016136 !'##experimental_source strain Pringsheim LB555 REFERENCE S07067 !$#authors Bryant, D.A.; Stirewalt, V.L. !$#journal FEBS Lett. (1990) 259:273-280 !$#title The cyanelle genome of Cyanophora paradoxa encodes ribosomal !1proteins not encoded by the chloroplast genomes of higher !1plants. !$#cross-references MUID:90092562; PMID:2403527 !$#accession S07067 !'##molecule_type DNA !'##residues 1-145,'S',147-163,'N',165-181 ##label BRY !'##cross-references EMBL:X16548; NID:g11287; PIDN:CAA34548.1; !1PID:g11288 REFERENCE S12211 !$#authors Michalowski, C.B.; Pfanzagl, B.; Loeffelhardt, W.; Bohnert, !1H.J. !$#journal Mol. Gen. Genet. (1990) 224:222-231 !$#title The cyanelle S10 spc ribosomal protein gene operon from !1Cyanophora paradoxa. !$#cross-references MUID:91117189; PMID:2126059 !$#accession S12216 !'##molecule_type DNA !'##residues 1-181 ##label MIC !'##cross-references GB:M30487; NID:g336645; PIDN:AAA63625.1; !1PID:g336651 GENETICS !$#gene rpl5; rplE !$#map_position 47-48 !$#genome cyanelle CLASSIFICATION #superfamily Escherichia coli ribosomal protein L5 KEYWORDS cyanelle; protein biosynthesis; ribosome SUMMARY #length 181 #molecular-weight 20453 #checksum 9700 SEQUENCE /// ENTRY R5IT5 #type complete TITLE ribosomal protein L5 - euglenid (Astasia longa) plastid ORGANISM #formal_name plastid Astasia longa DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S14150; S38591; S08111 REFERENCE S14125 !$#authors Siemeister, G.; Buchholz, C.; Hachtel, W. !$#journal Curr. Genet. (1990) 18:457-464 !$#title Genes for ribosomal proteins are retained on the 73 kb DNA !1from Astasia longa that resembles Euglena chloroplast DNA. !$#cross-references MUID:91176556; PMID:2078869 !$#accession S14150 !'##molecule_type DNA !'##residues 1-179 ##label SIE !'##cross-references EMBL:X14384; NID:g11195; PIDN:CAA32554.1; !1PID:g11196 !'##note submitted to the EMBL Data Library, February 1989 REFERENCE S38590 !$#authors Gockel, G.; Baier, S.; Hachtel, W. !$#submission submitted to the EMBL Data Library, November 1993 !$#accession S38591 !'##molecule_type DNA !'##residues 1-179 ##label GOC !'##cross-references EMBL:X75651; NID:g414852; PIDN:CAA53309.1; !1PID:g414856 GENETICS !$#gene rpl5 !$#genome plastid CLASSIFICATION #superfamily Escherichia coli ribosomal protein L5 KEYWORDS plastid; protein biosynthesis; ribosome SUMMARY #length 179 #molecular-weight 20161 #checksum 1844 SEQUENCE /// ENTRY R5EG5 #type complete TITLE ribosomal protein L5 - Euglena gracilis chloroplast ORGANISM #formal_name chloroplast Euglena gracilis DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 22-Jun-1999 ACCESSIONS S09288; S34528; S34895 REFERENCE S09286 !$#authors Christopher, D.A.; Hallick, R.B. !$#journal Nucleic Acids Res. (1989) 17:7591-7608 !$#title Euglena gracilis chloroplast ribosomal protein operon: a new !1chloroplast gene for ribosomal protein L5 and description of !1a novel organelle intron category designated group III. !$#cross-references MUID:90016846; PMID:2477800 !$#accession S09288 !'##molecule_type DNA !'##residues 1-179 ##label CHR !'##cross-references EMBL:Z11874; NID:g14353; PIDN:CAA77924.1; !1PID:g14374 REFERENCE S34494 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.; Monfort, !1A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#submission submitted to the EMBL Data Library, January 1993 !$#description The complete sequence of the Euglena gracilis chloroplast !1genome (tentative). !$#accession S34528 !'##molecule_type DNA !'##residues 1-179 ##label HAL1 !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50107.1; !1PID:g415763 REFERENCE S34862 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.R.; !1Monfort, A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#journal Nucleic Acids Res. (1993) 21:3537-3544 !$#title Complete sequence of Euglena gracilis chloroplast DNA. !$#cross-references MUID:93347989; PMID:8346031 !$#accession S34895 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-179 ##label HAL2 !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50107.1; !1PID:g415763 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1993 GENETICS !$#gene rpl5 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein L5 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 179 #molecular-weight 20659 #checksum 9757 SEQUENCE /// ENTRY R5HSL5 #type complete TITLE ribosomal protein L5 [validated] - Haloarcula marismortui ALTERNATE_NAMES ribosomal protein HL13; ribosomal protein HL17 ORGANISM #formal_name Haloarcula marismortui DATE 30-Jun-1991 #sequence_revision 31-Dec-1992 #text_change 31-Mar-2000 ACCESSIONS S16535; S10762; I28949; T46800 REFERENCE S16535 !$#authors Scholzen, T.; Arndt, E. !$#journal Mol. Gen. Genet. (1991) 228:70-80 !$#title Organization and nucleotide sequence of ten ribosomal !1protein genes from the region equivalent to the !1spectinomycin operon in the archaebacterium Halobacterium !1marismortui. !$#cross-references MUID:91360093; PMID:1832208 !$#accession S16535 !'##molecule_type DNA !'##residues 1-177 ##label SCH !'##cross-references EMBL:X58395; NID:g48860; PIDN:CAA41284.1; !1PID:g48861 REFERENCE S10761 !$#authors Hatakeyama, T.; Hatakeyama, T. !$#journal Biochim. Biophys. Acta (1990) 1039:343-347 !$#title Amino acid sequences of the ribosomal proteins HL30 and !1HmaL5 from the archaebacterium Halobacterium marismortui. !$#cross-references MUID:90335268; PMID:2198942 !$#accession S10762 !'##molecule_type protein !'##residues 2-133,'R',135-177 ##label HAT !'##note the source is designated as Halobacterium marismortui !'##note the protein is designated as ribosomal protein HmaL5 REFERENCE A28926 !$#authors Walsh, M.J.; McDougall, J.; Wittmann-Liebold, B. !$#journal Biochemistry (1988) 27:6867-6876 !$#title Extended N-terminal sequencing of proteins of !1archaebacterial ribosomes blotted from two-dimensional gels !1onto glass fiber and poly(vinylidene difluoride) membrane. !$#cross-references MUID:89062418; PMID:3196689 !$#accession I28949 !'##molecule_type protein !'##residues 2-17,'X',19-23 ##label WAL !'##note the protein is designated as ribosomal protein L13 GENETICS !$#note HmaL5 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L5 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-177 #product ribosomal protein L5 #status experimental !8#label MAT SUMMARY #length 177 #molecular-weight 19528 #checksum 5826 SEQUENCE /// ENTRY R5MX5 #type complete TITLE ribosomal protein L5 - Methanococcus vannielii ORGANISM #formal_name Methanococcus vannielii DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 22-Jun-1999 ACCESSIONS S05617 REFERENCE S05611 !$#authors Auer, J.; Spicker, G.; Boeck, A. !$#journal J. Mol. Biol. (1989) 209:21-36 !$#title Organization and structure of the Methanococcus !1transcriptional unit homologous to the Escherichia coli !1"spectinomycin operon". Implications for the evolutionary !1relationship of 70 S and 80 S ribosomes. !$#cross-references MUID:90040717; PMID:2530355 !$#accession S05617 !'##molecule_type DNA !'##residues 1-181 ##label AUE !'##cross-references EMBL:X16720; NID:g44754; PIDN:CAA34693.1; !1PID:g44761 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L5 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 181 #molecular-weight 20293 #checksum 1287 SEQUENCE /// ENTRY R5RT11 #type complete TITLE ribosomal protein L11, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 21-Jul-2000 ACCESSIONS JT0606; S17351 REFERENCE JT0606 !$#authors Chan, Y.L.; Olvera, J.; Paz, V.; Wool, I.G. !$#journal Biochem. Biophys. Res. Commun. (1992) 185:356-362 !$#title The primary structure of rat ribosomal protein L11. !$#cross-references MUID:92287119; PMID:1599472 !$#accession JT0606 !'##molecule_type mRNA !'##residues 1-178 ##label CH2 !'##cross-references GB:X62146; GB:S37517; NID:g57677; PIDN:CAA44072.1; !1PID:g57678 !'##note part of this sequence was confirmed by protein sequencing !'##note the protein is designated as ribosomal protein L11 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L5 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-178 #product ribosomal protein L11 #status predicted !8#label RIP SUMMARY #length 178 #molecular-weight 20252 #checksum 8252 SEQUENCE /// ENTRY R5BY16 #type complete TITLE ribosomal protein L11.e.B, cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein G4620; protein YGR085c; ribosomal protein RP39A; ribosomal protein YL16; ribosomal protein YL22 ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 21-Jul-2000 ACCESSIONS A02764; S29371; S22844; S29372; S64380 REFERENCE A93541 !$#authors Teem, J.L.; Abovich, N.; Kaufer, N.F.; Schwindinger, W.F.; !1Warner, J.R.; Levy, A.; Woolford, J.; Leer, R.J.; van !1Raamsdonk-Duin, M.M.C.; Mager, W.H.; Planta, R.J.; Schultz, !1L.; Friesen, J.D.; Fried, H.; Rosbash, M. !$#journal Nucleic Acids Res. (1984) 12:8295-8312 !$#title A comparison of yeast ribosomal protein gene DNA sequences. !$#cross-references MUID:85062814; PMID:6390341 !$#accession A02764 !'##molecule_type DNA !'##residues 1-174 ##label TEE !'##note the authors translated the codon GTC for residue 138 as Ala REFERENCE S29371 !$#authors Leer, R.J.; van Raamsdonk-Duin, M.M.C.; Mager, W.H.; Planta, !1R.J. !$#journal FEBS Lett. (1984) 175:371-376 !$#title The primary structure of the gene encoding yeast ribosomal !1protein L16. !$#cross-references MUID:85004136; PMID:6090215 !$#accession S29371 !'##molecule_type DNA !'##residues 1-2,'A',4-24,'Q',26-174 ##label LEE !'##cross-references EMBL:X01029; NID:g4321; PIDN:CAA25515.1; PID:g4322 !'##note the authors translated the codon CAA for residue 25 as Glu !'##note the source is designated as Saccharomyces carlsbergensis REFERENCE A30237 !$#authors Partaledis, J.A.; Mason, T.L. !$#journal Mol. Cell. Biol. (1988) 8:3647-3660 !$#title Structure and regulation of a nuclear gene in Saccharomyces !1cerevisiae that specifies MRP13, a protein of the small !1subunit of the mitochondrial ribosome. !$#cross-references MUID:89127203; PMID:3065621 !$#accession S22844 !'##status translation not shown !'##molecule_type DNA !'##residues 1-125,'VSMSS' ##label PAR !'##cross-references EMBL:M22109 REFERENCE S29372 !$#authors Rotenberg, M.O.; Woolford Jr., J.L. !$#journal Mol. Cell. Biol. (1986) 6:674-687 !$#title Tripartite upstream promoter element essential for !1expression of Saccharomyces cerevisiae ribosomal protein !1genes. !$#cross-references MUID:87064353; PMID:3023862 !$#accession S29372 !'##molecule_type DNA !'##residues 1-10 ##label ROT !'##cross-references EMBL:M12933; NID:g172455; PIDN:AAA34990.1; !1PID:g172456 REFERENCE S64356 !$#authors Wedler, H.; Scharfe, M.; Wedler, E.; Wambutt, R. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64380 !'##molecule_type DNA !'##residues 1-174 ##label WED !'##cross-references EMBL:Z72870; NID:g1323122; PIDN:CAA97087.1; !1PID:g1323123; GSPDB:GN00007; MIPS:YGR085c !'##experimental_source strain S288C GENETICS !$#gene SGD:RPL16A; RP39A; MIPS:YGR085c !'##cross-references SGD:S0003317; MIPS:YGR085c !$#map_position 7R CLASSIFICATION #superfamily Escherichia coli ribosomal protein L5 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 174 #molecular-weight 19750 #checksum 1228 SEQUENCE /// ENTRY R5RT9 #type complete TITLE ribosomal protein L9, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 21-Jul-2000 ACCESSIONS JH0222; S10389 REFERENCE JH0222 !$#authors Suzuki, K.; Olvera, J.; Wool, I.G. !$#journal Gene (1990) 93:297-300 !$#title The primary structure of rat ribosomal protein L9. !$#cross-references MUID:91033042; PMID:2227441 !$#accession JH0222 !'##molecule_type mRNA !'##residues 1-192 ##label SUZ !'##cross-references EMBL:X51706; NID:g57705; PIDN:CAA36002.1; !1PID:g57706 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing !'##note the protein is designated as ribosomal protein L9 GENETICS !$#gene L9 !$#note DNA hybridization suggests 20-23 copies of the L9 gene CLASSIFICATION #superfamily Escherichia coli ribosomal protein L6 KEYWORDS protein biosynthesis; ribosome FEATURE !$1-192 #product ribosomal protein L9 #status experimental !8#label MAT SUMMARY #length 192 #molecular-weight 21893 #checksum 9436 SEQUENCE /// ENTRY R5BYL9 #type complete TITLE ribosomal protein L9.e.A, cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein G2505; protein YGL147c; ribosomal protein YL11 ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jun-2000 ACCESSIONS S19077; S11256; S64161 REFERENCE S19077 !$#authors Jones, D.G.L.; Reusser, U.; Braus, G.H. !$#journal Nucleic Acids Res. (1991) 19:5785 !$#title Cloning and characterisation of a yeast homolog of the !1mammalian ribosomal protein L9. !$#cross-references MUID:92051331; PMID:1945856 !$#accession S19077 !'##molecule_type DNA !'##residues 1-191 ##label JON !'##cross-references EMBL:X60190; NID:g3386; PIDN:CAA42746.1; PID:g3388 REFERENCE S11249 !$#authors Otaka, E.; Higo, K.I.; Itoh, T. !$#journal Mol. Gen. Genet. (1984) 195:544-546 !$#title Yeast ribosomal proteins. VIII. Isolation of two proteins !1and sequence characterization of twenty-four proteins from !1cytoplasmic ribosomes. !$#accession S11256 !'##molecule_type protein !'##residues 1-6,'ZZZ',10-13,'Q',15-36,'B',38,'X',40 ##label OTA REFERENCE S64153 !$#authors Volckaert, G.; Voet, M.; Verhasselt, P.; Defoor, E. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64161 !'##molecule_type DNA !'##residues 1-191 ##label VOL !'##cross-references EMBL:Z72669; NID:g1322729; PIDN:CAA96859.1; !1PID:g1322730; GSPDB:GN00007; MIPS:YGL147c !'##experimental_source strain S288C GENETICS !$#gene SGD:RPL9A; YL9A; YL11; RP25; MIPS:YGL147c !'##cross-references SGD:S0003115; MIPS:YGL147c !$#map_position 7L CLASSIFICATION #superfamily Escherichia coli ribosomal protein L6 KEYWORDS protein biosynthesis; ribosome FEATURE !$1-191 #product ribosomal protein L9.e #status experimental !8#label MAT SUMMARY #length 191 #molecular-weight 21569 #checksum 8224 SEQUENCE /// ENTRY R5MX6 #type complete TITLE ribosomal protein L6 - Methanococcus vannielii ORGANISM #formal_name Methanococcus vannielii DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 22-Jun-1999 ACCESSIONS S05620 REFERENCE S05611 !$#authors Auer, J.; Spicker, G.; Boeck, A. !$#journal J. Mol. Biol. (1989) 209:21-36 !$#title Organization and structure of the Methanococcus !1transcriptional unit homologous to the Escherichia coli !1"spectinomycin operon". Implications for the evolutionary !1relationship of 70 S and 80 S ribosomes. !$#cross-references MUID:90040717; PMID:2530355 !$#accession S05620 !'##molecule_type DNA !'##residues 1-182 ##label AUE !'##cross-references EMBL:X16720; NID:g44754; PIDN:CAA34696.1; !1PID:g44764 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L6 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 182 #molecular-weight 20134 #checksum 3336 SEQUENCE /// ENTRY R5HS6L #type complete TITLE ribosomal protein L6 [validated] - Haloarcula marismortui ALTERNATE_NAMES ribosomal protein HL10; ribosomal protein HL12; ribosomal protein HL9 ORGANISM #formal_name Haloarcula marismortui DATE 30-Sep-1991 #sequence_revision 31-Dec-1992 #text_change 31-Mar-2000 ACCESSIONS S16538; S14425; E28949; T46803 REFERENCE S16535 !$#authors Scholzen, T.; Arndt, E. !$#journal Mol. Gen. Genet. (1991) 228:70-80 !$#title Organization and nucleotide sequence of ten ribosomal !1protein genes from the region equivalent to the !1spectinomycin operon in the archaebacterium Halobacterium !1marismortui. !$#cross-references MUID:91360093; PMID:1832208 !$#accession S16538 !'##molecule_type DNA !'##residues 1-178 ##label SCH !'##cross-references EMBL:X58395; NID:g48860; PIDN:CAA41287.1; !1PID:g48864 REFERENCE S14425 !$#authors Dijk, J.; van den Broek, R.; Nasiulas, G.; Beck, A.; !1Reinhardt, R.; Wittmann-Liebold, B. !$#journal Biol. Chem. Hoppe-Seyler (1987) 368:921-925 !$#title The N-terminal sequence of ribosomal protein L10 from the !1archaebacterium Halobacterium marismortui and its !1relationship to eubacterial protein L6 and other ribosomal !1proteins. !$#cross-references MUID:88024437; PMID:3311072 !$#accession S14425 !'##molecule_type protein !'##residues 2-53,'X',55 ##label DIJ !'##note the sequence from Fig. 2 is inconsistent with that from Fig. 1 !1in having 7-Gly !'##note the source is designated as Halobacterium marismortui !'##note the protein is designated as ribosomal protein L10 REFERENCE A28926 !$#authors Walsh, M.J.; McDougall, J.; Wittmann-Liebold, B. !$#journal Biochemistry (1988) 27:6867-6876 !$#title Extended N-terminal sequencing of proteins of !1archaebacterial ribosomes blotted from two-dimensional gels !1onto glass fiber and poly(vinylidene difluoride) membrane. !$#cross-references MUID:89062418; PMID:3196689 !$#accession E28949 !'##molecule_type protein !'##residues 2-31 ##label WAL !'##note 3-Ser and 24-Ser were also found !'##note the protein is designated as ribosomal protein L9 GENETICS !$#gene HmaL6 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L6 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-178 #product ribosomal protein L6 #status experimental !8#label MAT SUMMARY #length 178 #molecular-weight 19944 #checksum 9354 SEQUENCE /// ENTRY R5EC6 #type complete TITLE ribosomal protein L6 [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-May-1979 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS D65123; A02765 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65123 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-177 ##label BLAT !'##cross-references GB:AE000408; GB:U00096; NID:g1789694; !1PIDN:AAC76330.1; PID:g1789701; UWGP:b3305 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A02765 !$#authors Chen, R.; Arfsten, U.; Chen-Schmeisser, U. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1977) 358:531-535 !$#title The primary structure of protein L6 from the aminoacyl-tRNA !1binding site of the Escherichia coli ribosome. !$#cross-references MUID:77186588; PMID:324885 !$#accession A02765 !'##molecule_type protein !'##residues 2-81,'D',83-87,'E',89-177 ##label CHE !'##experimental_source strain K REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note mass spectrographic analysis of post-translational !1modifications; any acid labile modifications may have been !1missed GENETICS !$#gene rplF !$#map_position 73 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX large subunit ribosomal proteins: L1 (PIR:R5EC1), L3 !1(PIR:R5EC3), L2 (PIR:R5EC2), L4 (PIR:R5EC4), L5 (PIR:R5EC5), !1L6 (PIR:R5EC6), L7/L12 (PIR:R5EC7), L9 (PIR:R5EC9), L10 !1(PIR:R5EC10), L11 (PIR:R5EC11), L13 (PIR:R5EC13), L14 !1(PIR:R5EC14), L15 (PIR:R5EC15), L16 (PIR:R5EC16), L17 !1(PIR:R5EC17), L18 (PIR:R5EC18), L19 (PIR:R5EC19) FUNCTION !$#pathway protein biosynthesis !$#note binds 23S rRNA and is located at the aminoacyl-tRNA binding !1site CLASSIFICATION #superfamily Escherichia coli ribosomal protein L6 KEYWORDS protein biosynthesis; ribosome; RNA binding FEATURE !$2-177 #product ribosomal protein L6 #status experimental !8#label MAT SUMMARY #length 177 #molecular-weight 18904 #checksum 1286 SEQUENCE /// ENTRY R5BS0F #type complete TITLE ribosomal protein L6 - Bacillus stearothermophilus ALTERNATE_NAMES ribosomal protein BL10 ORGANISM #formal_name Bacillus stearothermophilus DATE 02-Apr-1982 #sequence_revision 02-Apr-1982 #text_change 07-May-1999 ACCESSIONS A02766; B39085; S59061 REFERENCE A02766 !$#authors Kimura, M.; Rawlings, N.; Appelt, K. !$#journal FEBS Lett. (1981) 136:58-64 !$#title The amino acid sequence of protein BL10 from the 50S subunit !1of the Bacillus stearothermophilus ribosome. !$#accession A02766 !'##molecule_type protein !'##residues 1-177 ##label KIM REFERENCE A39085 !$#authors Ramakrishnan, V.; Gerchman, S.E. !$#journal J. Biol. Chem. (1991) 266:880-885 !$#title Cloning, sequencing, and overexpression of genes for !1ribosomal proteins from Bacillus stearothermophilus. !$#cross-references MUID:91093287; PMID:1985969 !$#accession B39085 !'##molecule_type DNA !'##residues 8-170 ##label RAM !'##cross-references GB:M57622 REFERENCE S59051 !$#authors Urlaub, H.; Kruft, V.; Bischof, O.; Mueller, E.C.; !1Wittmann-Liebold, B. !$#journal EMBO J. (1995) 14:4578-4588 !$#title Protein-rRNA binding features and their structural and !1functional implications in ribosomes as determined by !1cross-linking studies. !$#cross-references MUID:96003638; PMID:7556101 !$#accession S59061 !'##molecule_type protein !'##residues 149-163 ##label URL CLASSIFICATION #superfamily Escherichia coli ribosomal protein L6 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 177 #molecular-weight 19168 #checksum 4940 SEQUENCE /// ENTRY R5KT6 #type complete TITLE ribosomal protein L6 - Cyanophora paradoxa cyanelle ORGANISM #formal_name cyanelle Cyanophora paradoxa DATE 31-Dec-1990 #sequence_revision 31-Dec-1991 #text_change 22-Jun-1999 ACCESSIONS S12218; S07069; T06878 REFERENCE S12211 !$#authors Michalowski, C.B.; Pfanzagl, B.; Loeffelhardt, W.; Bohnert, !1H.J. !$#journal Mol. Gen. Genet. (1990) 224:222-231 !$#title The cyanelle S10 spc ribosomal protein gene operon from !1Cyanophora paradoxa. !$#cross-references MUID:91117189; PMID:2126059 !$#accession S12218 !'##molecule_type DNA !'##residues 1-179 ##label MIC !'##cross-references GB:M30487; NID:g336645; PIDN:AAA63627.1; !1PID:g336653 REFERENCE S07067 !$#authors Bryant, D.A.; Stirewalt, V.L. !$#journal FEBS Lett. (1990) 259:273-280 !$#title The cyanelle genome of Cyanophora paradoxa encodes ribosomal !1proteins not encoded by the chloroplast genomes of higher !1plants. !$#cross-references MUID:90092562; PMID:2403527 !$#accession S07069 !'##molecule_type DNA !'##residues 1-41 ##label BRY !'##cross-references EMBL:X16548; NID:g11287; PIDN:CAA34550.1; !1PID:g11290 REFERENCE Z15840 !$#authors Stirewalt, V.L.; Michalowski, C.B.; Luffelhardt, W.; !1Bohnert, H.J.; Bryant, D.A. !$#submission submitted to the EMBL Data Library, July 1995 !$#description Nucleotide sequence of the cyanelle genome from Cyanophora !1paradoxa. !$#accession T06878 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-179 ##label STI !'##cross-references EMBL:U30821; NID:g1016083; PIDN:AAA81221.1; !1PID:g1016134 !'##experimental_source strain Pringsheim LB555 GENETICS !$#gene rpl6; rplF !$#map_position 47-48 !$#genome cyanelle CLASSIFICATION #superfamily Escherichia coli ribosomal protein L6 KEYWORDS cyanelle; protein biosynthesis; ribosome SUMMARY #length 179 #molecular-weight 19880 #checksum 4407 SEQUENCE /// ENTRY R5YM6 #type complete TITLE ribosomal protein L6 - Mycoplasma capricolum ALTERNATE_NAMES protein MC388 ORGANISM #formal_name Mycoplasma capricolum #variety ATCC 27343 DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 07-Dec-1999 ACCESSIONS S02846; S77867; A02767; S46903 REFERENCE S02830 !$#authors Ohkubo, S.; Muto, A.; Kawauchi, Y.; Yamao, F.; Osawa, S. !$#journal Mol. Gen. Genet. (1987) 210:314-322 !$#title The ribosomal protein gene cluster of Mycoplasma capricolum. !$#cross-references MUID:88142549; PMID:3481422 !$#accession S02846 !'##molecule_type DNA !'##residues 1-180 ##label OHK !'##cross-references EMBL:X06414; NID:g44207; PIDN:CAA29719.1; !1PID:g44224 REFERENCE S77739 !$#authors Bork, P.; Ouzounis, C.; Casari, G.; Schneider, R.; Sander, !1C.; Dolan, M.; Gilbert, W.; Gillevet, P.M. !$#journal Mol. Microbiol. (1995) 16:955-967 !$#title Exploring the Mycoplasma capricolum genome: a minimal cell !1reveals its physiology. !$#cross-references MUID:96059641; PMID:7476192 !$#accession S77867 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 76-118,'X',120-126,'S' ##label BOR !'##cross-references EMBL:Z33291 !'##experimental_source ATCC 27343 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1994 GENETICS !$#gene rpl6 !$#genetic_code SGC3 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L6 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 180 #molecular-weight 19647 #checksum 3911 SEQUENCE /// ENTRY S53855 #type complete TITLE ribosomal protein L6 - Acanthamoeba castellanii mitochondrion ORGANISM #formal_name mitochondrion Acanthamoeba castellanii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 07-Dec-1999 ACCESSIONS S53855 REFERENCE S53825 !$#authors Burger, G.; Plante, I.; Lonergan, K.M.; Gray, M.W. !$#journal J. Mol. Biol. (1995) 245:522-537 !$#title The mitochondrial DNA of the amoeboid protozoon, !1Acanthamoeba castellanii: complete sequence, gene content !1and genome organization. !$#cross-references MUID:95147275; PMID:7844823 !$#accession S53855 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-181 ##label BUR !'##cross-references GB:U12386; NID:g562028; PIDN:AAD11847.1; !1PID:g562059 !'##experimental_source strain Neff; ATCC 30010 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1994 GENETICS !$#genome mitochondrion !$#genetic_code SGC6 CLASSIFICATION #superfamily Acanthamoeba castellanii ribosomal protein L6 KEYWORDS mitochondrion SUMMARY #length 181 #molecular-weight 21772 #checksum 2149 SEQUENCE /// ENTRY B70137 #type complete TITLE conserved hypothetical protein BB0298 - Lyme disease spirochete ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B70137 REFERENCE A70100 !$#authors Fraser, C.M.; Casjens, S.; Huang, W.M.; Sutton, G.G.; !1Clayton, R.; Lathigra, R.; White, O.; Ketchum, K.A.; Dodson, !1R.; Hickey, E.K.; Gwinn, M.; Dougherty, B.; Tomb, J.F.; !1Fleischmann, R.D.; Richardson, D.; Peterson, J.; Kerlavage, !1A.R.; Quackenbush, J.; Salzberg, S.; Hanson, M.; Vugt, R.V.; !1Palmer, N.; Adams, M.D.; Gocayne, J.; Weidman, J.; !1Utterback, T.; Watthey, L.; McDonald, L.; Artiach, P.; !1Bowman, C.; Garland, S.; Fujii, C.; Cotton, M.D.; Horst, K.; !1Roberts, K.; Hatch, B.; Smith, H.O.; Venter, J.C. !$#journal Nature (1997) 390:580-586 !$#title Genomic sequence of a Lyme disease spirochaete, Borrelia !1burgdorferi. !$#cross-references MUID:98065943; PMID:9403685 !$#accession B70137 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-230 ##label KLE !'##cross-references GB:AE001137; GB:AE000783; NID:g2688160; !1PIDN:AAC66650.1; PID:g2688168; TIGR:BB0298 !'##experimental_source strain B31 !'##note Region (1-230) is similar to acc I40631(840-1080) CLASSIFICATION #superfamily hypothetical protein BB0298; tetratricopeptide !1repeat homology FEATURE !$69-102 #domain tetratricopeptide repeat homology #label TT1\ !$103-136 #domain tetratricopeptide repeat homology #label TT2 SUMMARY #length 230 #molecular-weight 26497 #checksum 1211 SEQUENCE /// ENTRY R5HU7A #type complete TITLE ribosomal protein L7a, cytosolic - human ALTERNATE_NAMES DNA damage-inducible protein ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S19717; JN0570; S00261; A36002; S10437; S12368 REFERENCE S19717 !$#authors Colombo, P.; Yon, J.; Fried, M. !$#journal Biochim. Biophys. Acta (1991) 1129:93-95 !$#title The organization and expression of the human L7a ribosomal !1protein gene. !$#cross-references MUID:92096469; PMID:1756182 !$#accession S19717 !'##status translation not shown !'##molecule_type DNA !'##residues 1-266 ##label COL !'##cross-references EMBL:X61923; NID:g36646; PIDN:CAA43925.1; !1PID:g36647 REFERENCE JN0570 !$#authors De Falco, S.; Russo, G.; Angiolillo, A.; Pietropaolo, C. !$#journal Gene (1993) 126:227-235 !$#title Human L7a ribosomal protein: Sequence, structural !1organization, and expression of a functional gene. !$#cross-references MUID:93246248; PMID:8482538 !$#accession JN0570 !'##molecule_type mRNA !'##residues 1-266 ##label DEF !'##cross-references EMBL:X52138; NID:g34202; PIDN:CAA36383.1; !1PID:g34203 !'##note the authors translated the codon for residue 102 as Thr REFERENCE S00261 !$#authors Kozma, S.C.; Redmond, S.M.S.; Xiao-Chang, F.; Saurer, S.M.; !1Groner, B.; Hynes, N.E. !$#journal EMBO J. (1988) 7:147-154 !$#title Activation of the receptor kinase domain of the trk oncogene !1by recombination with two different cellular sequences. !$#cross-references MUID:88196074; PMID:2966065 !$#accession S00261 !'##molecule_type mRNA !'##residues 1-266 ##label KOZ !'##cross-references EMBL:X06705; NID:g35511; PIDN:CAA29889.1; !1PID:g35512 REFERENCE A36002 !$#authors Ben-Ishai, R.; Scharf, R.; Sharon, R.; Kapten, I. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:6039-6043 !$#title A human cellular sequence implicated in trk oncogene !1activation is DNA damage inducible. !$#cross-references MUID:90349550; PMID:1696715 !$#accession A36002 !'##molecule_type mRNA !'##residues 1-266 ##label BEN !'##cross-references GB:M36072; NID:g337494; PIDN:AAA60282.1; !1PID:g337495 REFERENCE S12368 !$#authors Ziemiecki, A.; Mueller, R.G.; Xiao-Chang, F.; Hynes, N.E.; !1Kozma, S. !$#journal EMBO J. (1990) 9:191-196 !$#title Oncogenic activation of the human trk proto-oncogene by !1recombination with the ribosomal large subunit protein L7a. !$#cross-references MUID:90107943; PMID:2403926 !$#contents annotation !$#note the trk-derived fusion protein trk-2h was shown to contain !141 residues of this ribosomal protein at the amino end GENETICS !$#gene GDB:RPL7A !'##cross-references GDB:120355; OMIM:185640 !$#map_position 9q33-9q34 !$#introns 1/3; 42/1; 92/1; 139/1; 165/3; 209/2; 232/3 CLASSIFICATION #superfamily rat ribosomal protein L7a KEYWORDS protein biosynthesis; ribosome FEATURE !$2-266 #product ribosomal protein L7a, cytosolic #status !8predicted #label MAT SUMMARY #length 266 #molecular-weight 29995 #checksum 1864 SEQUENCE /// ENTRY R5RT7A #type complete TITLE ribosomal protein L7a, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 21-Jul-2000 ACCESSIONS S04712; S11417 REFERENCE S04712 !$#authors Nakamura, H.; Tanaka, T.; Ishikawa, K. !$#journal Nucleic Acids Res. (1989) 17:4875 !$#title Nucleotide sequence of cloned cDNA specific for rat !1ribosomal protein L7a. !$#cross-references MUID:89315226; PMID:2748341 !$#accession S04712 !'##molecule_type mRNA !'##residues 1-266 ##label NAK !'##cross-references EMBL:X15013; NID:g56955; PIDN:CAA33117.1; !1PID:g56956 REFERENCE S11413 !$#authors Wittmann-Liebold, B.; Geissler, A.W.; Lin, A.; Wool, I.G. !$#journal J. Supramol. Struct. (1979) 12:425-433 !$#title Sequence of the amino-terminal region of rat liver ribosomal !1proteins S4, S6, S8, L6, L7a, L18, L27, L30, L37, L37a, and !1L39. !$#cross-references MUID:80252792; PMID:398910 !$#accession S11417 !'##molecule_type protein !'##residues 2-32,'Q',34,'S',36-40 ##label WIT !'##note the protein is designated as ribosomal protein L7a CLASSIFICATION #superfamily rat ribosomal protein L7a KEYWORDS protein biosynthesis; ribosome FEATURE !$2-266 #product ribosomal protein L7a, cytosolic #status !8experimental #label MAT SUMMARY #length 266 #molecular-weight 29995 #checksum 1864 SEQUENCE /// ENTRY S18159 #type complete TITLE ribosomal protein L7a, cytosolic - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 22-Jun-1999 ACCESSIONS A46032; I50416; S18159 REFERENCE A46032 !$#authors Colombo, P.; Yon, J.; Garson, K.; Fried, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:6358-6362 !$#title Conservation of the organization of five tightly clustered !1genes over 600 million years of divergent evolution. !$#cross-references MUID:92335297; PMID:1631131 !$#accession A46032 !'##molecule_type mRNA; DNA !'##residues 1-266 ##label COL !'##cross-references EMBL:X62640; NID:g63777; PIDN:CAA44506.1; !1PID:g63778 !'##note submitted to the EMBL Data Library, October 1991 !'##note sequence extracted from NCBI backbone (NCBIP:108733) REFERENCE I50416 !$#authors Maeda, N.; Kenmochi, N.; Tanaka, T. !$#journal Biochimie (1993) 75:785-790 !$#title The complete nucleotide sequence of chicken ribosomal !1protein L7a gene and the multiple factor binding sites in !1its 5'-flanking region. !$#cross-references MUID:94100270; PMID:8274530 !$#accession I50416 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-266 ##label MAE !'##cross-references GB:D14522; NID:g457652; PIDN:BAA03395.1; !1PID:g601884 GENETICS !$#gene surf-3/Rpl7a !$#introns 1/3; 42/1; 92/1; 139/1; 165/3; 209/2; 232/3 CLASSIFICATION #superfamily rat ribosomal protein L7a KEYWORDS protein biosynthesis; ribosome SUMMARY #length 266 #molecular-weight 29999 #checksum 1898 SEQUENCE /// ENTRY R5BY7A #type complete TITLE ribosomal protein L7a.e.A, cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YHL033c; ribosomal protein RP6; ribosomal protein YL4-2; ribosomal protein YL4A ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1991 #sequence_revision 30-Jun-1993 #text_change 12-Nov-1999 ACCESSIONS S16811; S30358; S48935; S11607; S59803; S45513 REFERENCE S16810 !$#authors Yon, J.; Giallongo, A.; Fried, M. !$#journal Mol. Gen. Genet. (1991) 227:72-80 !$#title The organization and expression of the Saccharomyces !1cerevisiae L4 ribosomal protein genes and their !1identification as the homologues of the mammalian ribosomal !1protein gene L7a. !$#cross-references MUID:91260682; PMID:2046660 !$#accession S16811 !'##molecule_type DNA !'##residues 1-256 ##label YON1 !'##cross-references EMBL:X56836; NID:g3870; PIDN:CAA40166.1; PID:g3871 !$#accession S30358 !'##molecule_type protein !'##residues 'XX',3,'XXX',7-14 ##label YON2 REFERENCE S46794 !$#authors Favello, T. !$#submission submitted to the EMBL Data Library, June 1994 !$#description The sequence of S. cerevisiae cosmid 9196. !$#accession S48935 !'##molecule_type DNA !'##residues 1-256 ##label FAV !'##cross-references EMBL:U11583; NID:g2289854; PIDN:AAB65045.1; !1PID:g2289862; GSPDB:GN00008; MIPS:YHL033c REFERENCE S11607 !$#authors Arevalo, S.G.; Warner, J.R. !$#journal Nucleic Acids Res. (1990) 18:1447-1449 !$#title Ribosomal protein L4 of Saccharomyces cerevisiae: the gene !1and its protein. !$#cross-references MUID:90221868; PMID:2183194 !$#accession S11607 !'##molecule_type DNA !'##residues 1-112,'R',114-256 ##label ARE !'##cross-references EMBL:X17204; NID:g4395; PIDN:CAA35073.1; PID:g4396 REFERENCE S59803 !$#authors Ohtake, Y.; Wickner, R.B. !$#submission submitted to the EMBL Data Library, November 1994 !$#description Yeast virus propagation depends critically on free 60S !1ribosomal subunit concentration. !$#accession S59803 !'##molecule_type DNA !'##residues 1-256 ##label OHT !'##cross-references EMBL:U17361; NID:g747612; PIDN:AAA64574.1; !1PID:g747613 REFERENCE S45500 !$#authors Takahura, H.; Tsunasawa, S.; Miyagi, M.; Warner, J.R. !$#journal J. Biol. Chem. (1992) 267:5442-5445 !$#title NH2-terminal acetylation of ribosomal proteins of !1Saccharomyces cerevisiae. !$#cross-references MUID:92184799; PMID:1544921 !$#accession S45513 !'##molecule_type protein !'##residues 2-20 ##label TAK GENETICS !$#gene SGD:RPL4A; MIPS:YHL033c !'##cross-references SGD:S0001025; MIPS:YHL033c !$#map_position 8L CLASSIFICATION #superfamily rat ribosomal protein L7a KEYWORDS protein biosynthesis; ribosome FEATURE !$1-256 #product ribosomal protein L7a.e.A #status !8experimental #label MAT SUMMARY #length 256 #molecular-weight 28125 #checksum 1538 SEQUENCE /// ENTRY S16810 #type complete TITLE ribosomal protein L7a.e.B, cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein L0717; protein YLL045c; ribosomal protein YL4-1 ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jun-2000 ACCESSIONS S16810; S30358; S27455; S41068; S64797; S27297 REFERENCE S16810 !$#authors Yon, J.; Giallongo, A.; Fried, M. !$#journal Mol. Gen. Genet. (1991) 227:72-80 !$#title The organization and expression of the Saccharomyces !1cerevisiae L4 ribosomal protein genes and their !1identification as the homologues of the mammalian ribosomal !1protein gene L7a. !$#cross-references MUID:91260682; PMID:2046660 !$#accession S16810 !'##molecule_type DNA !'##residues 1-256 ##label YON !'##cross-references EMBL:X56835; NID:g3868; PIDN:CAA40165.1; PID:g3869 !$#accession S30358 !'##molecule_type protein !'##residues 'XX',3,'XXX',7-14 ##label YON2 REFERENCE S27437 !$#authors Cusick, M.E. !$#submission submitted to the EMBL Data Library, March 1992 !$#accession S27455 !'##molecule_type DNA !'##residues 1-113,'G',116-256 ##label CUS !'##cross-references EMBL:M88608; NID:g172443; PIDN:AAA20990.1; !1PID:g172444 REFERENCE S41068 !$#authors Cusick, M.E. !$#journal Biochim. Biophys. Acta (1994) 1217:31-40 !$#title Purification and identification of two major single-stranded !1binding proteins of yeast Saccharomyces cerevisiae as !1ribosomal protein L4 and histone H2B. !$#cross-references MUID:94114570; PMID:8286414 !$#accession S41068 !'##molecule_type DNA !'##residues 1-114,'G',116-256 ##label CUW !'##cross-references EMBL:M88608 REFERENCE S64792 !$#authors Wedler, H.; Wedler, E.; Scharfe, M.; Wambutt, R. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64797 !'##molecule_type DNA !'##residues 1-256 ##label WED !'##cross-references EMBL:Z73150; NID:g1360240; PIDN:CAA97495.1; !1PID:g1360241; GSPDB:GN00012; MIPS:YLL045c !'##note experimental_source strain S288C GENETICS !$#gene SGD:RPL4B; MIPS:YLL045c !'##cross-references SGD:S0003968; MIPS:YLL045c !$#map_position 12L CLASSIFICATION #superfamily rat ribosomal protein L7a KEYWORDS protein biosynthesis; ribosome FEATURE !$1-256 #product ribosomal protein L7a.e.B #status !8experimental #label MAT SUMMARY #length 256 #molecular-weight 28112 #checksum 1436 SEQUENCE /// ENTRY R5HSS6 #type complete TITLE ribosomal protein HS6 [validated] - Haloarcula marismortui ORGANISM #formal_name Haloarcula marismortui DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 21-Jul-2000 ACCESSIONS S00182 REFERENCE S00182 !$#authors Kimura, J.; Arndt, E.; Kimura, M. !$#journal FEBS Lett. (1987) 224:65-70 !$#title Primary structures of three highly acidic ribosomal proteins !1S6, S12 and S15 from the archaebacterium Halobacterium !1marismortui. !$#cross-references MUID:88055606; PMID:3315748 !$#accession S00182 !'##molecule_type protein !'##residues 1-116 ##label KIM !'##note the source is designated as Halobacterium marismortui !'##note the protein is designated as ribosomal protein S6 !'##note the protein was extracted from the 30S small ribosomal subunit CLASSIFICATION #superfamily rat ribosomal protein L7a KEYWORDS protein biosynthesis; ribosome SUMMARY #length 116 #molecular-weight 12219 #checksum 4604 SEQUENCE /// ENTRY R5HU7 #type complete TITLE ribosomal protein L7, cytosolic - human ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jun-2000 ACCESSIONS S11709; A48502; S30212; S30213 REFERENCE S11709 !$#authors Schneider, R.; Herzog, H.; Hfferer, L.; Schweiger, M. !$#submission submitted to the EMBL Data Library, May 1990 !$#description Evolution of the ribosomal protein L7 family: cloning and !1sequencing of the human cDNA and identification of a !1putative yeast pseudogene. !$#accession S11709 !'##molecule_type mRNA !'##residues 1-248 ##label SCH !'##cross-references EMBL:X52967; NID:g36139; PIDN:CAA37139.1; !1PID:g36140 REFERENCE A48502 !$#authors Seshadri, T.; Uzman, J.A.; Oshima, J.; Campisi, J. !$#journal J. Biol. Chem. (1993) 268:18474-18480 !$#title Identification of a transcript that is down-regulated in !1senescent human fibroblasts. Cloning, sequence analysis, and !1regulation of the human L7 ribosomal protein gene. !$#cross-references MUID:93366745; PMID:8360149 !$#accession A48502 !'##status preliminary !'##molecule_type mRNA !'##residues 1-172,'S',174-248 ##label SES !'##cross-references GB:L16558; NID:g307387; PIDN:AAA03081.1; !1PID:g307388 !'##experimental_source fetal lung fibroblasts, WI-38 cells !'##note sequence modified after extraction from NCBI backbone REFERENCE S30212 !$#authors Hemmerich, P.; von Mikecz, A.; Neumann, F.; Soezeri, O.; !1Wolff-Vorbeck, G.; Zoebelein, R.; Krawinkel, U. !$#journal Nucleic Acids Res. (1993) 21:223-231 !$#title Structural and functional properties of ribosomal protein L7 !1from humans and rodents. !$#cross-references MUID:93181195; PMID:8441630 !$#accession S30212 !'##status translation not shown !'##molecule_type mRNA !'##residues 'EKAKEFRRA',5-156,'L',158-159,'A',161-165,'Q',167-248 !1##label HEW !'##cross-references EMBL:X57958; NID:g35904; PIDN:CAA41026.1; !1PID:g1335288 !$#accession S30213 !'##molecule_type mRNA !'##residues 1-156,'L',158-248 ##label HEM !'##cross-references EMBL:X57959; NID:g35902; PIDN:CAA41027.1; !1PID:g35903 GENETICS !$#gene GDB:RPL7 !'##cross-references GDB:9863267 !$#map_position 8pter-8qter CLASSIFICATION #superfamily rat ribosomal protein L7 KEYWORDS leucine zipper; protein biosynthesis; ribosome FEATURE !$133-174 #region leucine zipper motif SUMMARY #length 248 #molecular-weight 29226 #checksum 2676 SEQUENCE /// ENTRY R5RTL7 #type complete TITLE ribosomal protein L7, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1992 #sequence_revision 21-Jul-2000 #text_change 21-Jul-2000 ACCESSIONS JC4230; B27373; C27373 REFERENCE JC4228 !$#authors Chan, Y.L.; Olvera, J.; Wool, I.G. !$#journal Biochem. Biophys. Res. Commun. (1995) 213:1042-1050 !$#title The primary structures of rat ribosomal proteins: the !1characterization of the cDNAs for S21 and L39, corrections !1in the sequences of L7 and L18a, and the identification of !1L33. !$#cross-references MUID:95382802; PMID:7654221 !$#accession JC4230 !'##molecule_type mRNA !'##residues 1-260 ##label CHA !'##cross-references GB:M17422 !'##experimental_source liver REFERENCE A27373 !$#authors Lin, A.; Chan, Y.L.; McNally, J.; Peleg, D.; Meyuhas, O.; !1Wool, I.G. !$#journal J. Biol. Chem. (1987) 262:12665-12671 !$#title The primary structure of rat ribosomal protein L7. The !1presence near the amino terminus of L7 of five tandem !1repeats of a sequence of 12 amino acids. !$#cross-references MUID:87308300; PMID:3624274 !$#accession B27373 !'##molecule_type mRNA !'##residues 1-252 ##label LIN !'##cross-references EMBL:M17422; NID:g206735; PIDN:AAA42075.1; !1PID:g206736 !$#accession C27373 !'##molecule_type protein !'##residues 2-7;77-100;145-160;200-252,'EHPIKR' ##label LI2 !'##note this sequence has been revised in reference JC4228 !'##note the protein is designated as ribosomal protein L7 CLASSIFICATION #superfamily rat ribosomal protein L7 KEYWORDS protein biosynthesis; ribosome; tandem repeat FEATURE !$7-66 #region 12-residue repeats SUMMARY #length 260 #molecular-weight 30329 #checksum 6247 SEQUENCE /// ENTRY R5DO7 #type complete TITLE ribosomal protein L7 - slime mold (Dictyostelium discoideum) ORGANISM #formal_name Dictyostelium discoideum DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 22-Jun-1999 ACCESSIONS S04849; S12834 REFERENCE S04849 !$#authors Szymkowski, D.E.; Kelly, B.; Deering, R.A. !$#journal Nucleic Acids Res. (1989) 17:5393 !$#title A Dictyostelium discoideum cDNA coding for a protein with !1homology to the rat ribosomal protein L7. !$#cross-references MUID:89345108; PMID:2762135 !$#accession S04849 !'##molecule_type mRNA !'##residues 1-246 ##label SZY !'##cross-references EMBL:X14909; NID:g7356; PIDN:CAA33035.1; PID:g7357 GENETICS !$#gene rpl7 CLASSIFICATION #superfamily rat ribosomal protein L7 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 246 #molecular-weight 27932 #checksum 1533 SEQUENCE /// ENTRY R5BYL7 #type complete TITLE ribosomal protein L7.e.A, cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein G3216; protein YGL076c; ribosomal protein rp11; ribosomal protein YL8.A ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jun-2000 ACCESSIONS S22789; S11255; S45516; S64083 REFERENCE S22789 !$#authors Mizuta, K.; Hashimoto, T.; Otaka, E. !$#journal Nucleic Acids Res. (1992) 20:1011-1016 !$#title Yeast ribosomal proteins: XIII. Saccharomyces cerevisiae !1YL8A gene, interrupted with two introns, encodes a homolog !1of mammalian L7. !$#cross-references MUID:92195798; PMID:1549461 !$#accession S22789 !'##molecule_type DNA !'##residues 1-244 ##label MIZ !'##cross-references EMBL:X62627; NID:g4821; PIDN:CAA44495.1; PID:g4822 !'##experimental_source strain A364A, ATCC 22244 REFERENCE S11249 !$#authors Otaka, E.; Higo, K.I.; Itoh, T. !$#journal Mol. Gen. Genet. (1984) 195:544-546 !$#title Yeast ribosomal proteins. VIII. Isolation of two proteins !1and sequence characterization of twenty-four proteins from !1cytoplasmic ribosomes. !$#accession S11255 !'##molecule_type protein !'##residues 2-23,'Z',25-39,'X',41 ##label OTA REFERENCE S45500 !$#authors Takahura, H.; Tsunasawa, S.; Miyagi, M.; Warner, J.R. !$#journal J. Biol. Chem. (1992) 267:5442-5445 !$#title NH2-terminal acetylation of ribosomal proteins of !1Saccharomyces cerevisiae. !$#cross-references MUID:92184799; PMID:1544921 !$#accession S45516 !'##molecule_type protein !'##residues 2-16,'X',18-21 ##label TAK REFERENCE S64071 !$#authors Rieger, M.; Mueller-Auer, S.; Brueckner, M.; Schaefer, M. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64083 !'##molecule_type DNA !'##residues 1-244 ##label RIE !'##cross-references EMBL:Z72598; NID:g1322590; PIDN:CAA96781.1; !1PID:g1322591; GSPDB:GN00007; MIPS:YGL076c !'##experimental_source strain S288C GENETICS !$#gene SGD:RPL6A; YL8A; MIPS:YGL076c !'##cross-references SGD:S0003044; MIPS:YGL076c !$#map_position 7L !$#introns 4/2; 35/3 CLASSIFICATION #superfamily rat ribosomal protein L7 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-244 #product ribosomal protein L7.e.A #status !8experimental #label MAT SUMMARY #length 244 #molecular-weight 27638 #checksum 4958 SEQUENCE /// ENTRY R5BY7 #type complete TITLE 60s ribosomal protein L7 [similarity] - fission yeast (Schizosaccharomyces pombe) ORGANISM #formal_name Schizosaccharomyces pombe DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 21-Jul-2000 ACCESSIONS S10991; T50236 REFERENCE S10991 !$#authors Murray, J.M.; Watts, F.Z. !$#journal Nucleic Acids Res. (1990) 18:4590 !$#title Isolation of a Schizosaccharomyces pombe homologue to the !1rat ribosomal protein, L7. !$#cross-references MUID:90356398; PMID:2388837 !$#accession S10991 !'##molecule_type DNA !'##residues 1-249 ##label MUR !'##cross-references EMBL:X53575; NID:g5066; PIDN:CAA37639.1; !1PID:g295935 REFERENCE Z25048 !$#authors Cadieu, E.; Lelaure, V.; Galibert, F.; McDougall, R.C.; !1Rajandream, M.A.; Barrell, B.G. !$#submission submitted to the EMBL Data Library, January 1999 !$#accession T50236 !'##molecule_type DNA !'##residues 1-249 ##label CAD !'##cross-references EMBL:AL136235; PIDN:CAB65807.1; GSPDB:GN00066; !1SPDB:SPAC664.06 !'##experimental_source strain 972h(-); cosmid c664 GENETICS !$#gene SPDB:SPAC664.06 !$#map_position 1L !$#introns 41/3 CLASSIFICATION #superfamily rat ribosomal protein L7 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 249 #molecular-weight 29165 #checksum 2362 SEQUENCE /// ENTRY R5MX30 #type complete TITLE ribosomal protein L30 - Methanococcus vannielii ORGANISM #formal_name Methanococcus vannielii DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 22-Jun-1999 ACCESSIONS S05625 REFERENCE S05611 !$#authors Auer, J.; Spicker, G.; Boeck, A. !$#journal J. Mol. Biol. (1989) 209:21-36 !$#title Organization and structure of the Methanococcus !1transcriptional unit homologous to the Escherichia coli !1"spectinomycin operon". Implications for the evolutionary !1relationship of 70 S and 80 S ribosomes. !$#cross-references MUID:90040717; PMID:2530355 !$#accession S05625 !'##molecule_type DNA !'##residues 1-154 ##label AUE !'##cross-references EMBL:X16720; NID:g44754; PIDN:CAA34701.1; !1PID:g44769 CLASSIFICATION #superfamily rat ribosomal protein L7 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 154 #molecular-weight 17224 #checksum 3867 SEQUENCE /// ENTRY R5HS30 #type complete TITLE ribosomal protein L30 [validated] - Haloarcula marismortui ALTERNATE_NAMES ribosomal protein HL16; ribosomal protein HL20 ORGANISM #formal_name Haloarcula marismortui DATE 31-Mar-1991 #sequence_revision 31-Dec-1992 #text_change 31-Mar-2000 ACCESSIONS S16543; S06845; B28926; T46808 REFERENCE S16535 !$#authors Scholzen, T.; Arndt, E. !$#journal Mol. Gen. Genet. (1991) 228:70-80 !$#title Organization and nucleotide sequence of ten ribosomal !1protein genes from the region equivalent to the !1spectinomycin operon in the archaebacterium Halobacterium !1marismortui. !$#cross-references MUID:91360093; PMID:1832208 !$#accession S16543 !'##molecule_type DNA !'##residues 1-154 ##label SCH !'##cross-references EMBL:X58395; NID:g48860; PIDN:CAA41292.1; !1PID:g48869 REFERENCE S06844 !$#authors Hatakeyama, T.; Kaufmann, F.; Schroeter, B.; Hatakeyama, T. !$#journal Eur. J. Biochem. (1989) 185:685-693 !$#title Primary structures of five ribosomal proteins from the !1archaebacterium Halobacterium marismortui and their !1structural relationships to eubacterial and eukaryotic !1ribosomal proteins. !$#cross-references MUID:90076190; PMID:2591382 !$#accession S06845 !'##molecule_type protein !'##residues 1-82,'L',84-147,149-154 ##label HAT !'##note the source is designated as Halobacterium marismortui !'##note the protein is designated as ribosomal protein HL20 REFERENCE A28926 !$#authors Walsh, M.J.; McDougall, J.; Wittmann-Liebold, B. !$#journal Biochemistry (1988) 27:6867-6876 !$#title Extended N-terminal sequencing of proteins of !1archaebacterial ribosomes blotted from two-dimensional gels !1onto glass fiber and poly(vinylidene difluoride) membrane. !$#cross-references MUID:89062418; PMID:3196689 !$#accession B28926 !'##molecule_type protein !'##residues 1-30 ##label WAL !'##note the protein is designated as ribosomal protein L16 GENETICS !$#gene HmaL30 CLASSIFICATION #superfamily rat ribosomal protein L7 KEYWORDS protein biosynthesis; ribosome FEATURE !$1-154 #product ribosomal protein L30 #status experimental !8#label MAT SUMMARY #length 154 #molecular-weight 17042 #checksum 9571 SEQUENCE /// ENTRY R5EC7 #type complete TITLE ribosomal protein L7/L12 [validated] - Escherichia coli (strain K-12) CONTAINS ribosomal protein L12; ribosomal protein L7 ORGANISM #formal_name Escherichia coli DATE 24-Apr-1984 #sequence_revision 30-Jun-1991 #text_change 01-Mar-2002 ACCESSIONS S12575; A02768; B00689; S26952; I52538; I52537; E65205 REFERENCE S12572 !$#authors Post, L.E.; Strycharz, G.D.; Nomura, M.; Lewis, H.; Dennis, !1P.P. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1979) 76:1697-1701 !$#title Nucleotide sequence of the ribosomal protein gene cluster !1adjacent to the gene for RNA polymerase subunit beta in !1Escherichia coli. !$#cross-references MUID:79201667; PMID:377281 !$#accession S12575 !'##molecule_type DNA !'##residues 1-121 ##label POS !'##cross-references EMBL:V00339; NID:g42813; PIDN:CAA23624.1; !1PID:g42817 REFERENCE A02768 !$#authors Terhorst, C.; Moeller, W.; Laursen, R.; Wittmann-Liebold, B. !$#journal Eur. J. Biochem. (1973) 34:138-152 !$#title The primary structure of an acidic protein from 50-S !1ribosomes of Escherichia coli which is involved in GTP !1hydrolysis dependent of elongation factors G and T. !$#cross-references MUID:73169380; PMID:4573678 !$#accession A02768 !'##molecule_type protein !'##residues 2-121 ##label TER !'##experimental_source strain MRE-600 REFERENCE A00689 !$#authors Gurevitch, A.I.; Avakov, A.E.; Kolosov, M.N. !$#journal Bioorg. Khim. (1979) 5:1735-1738 !$#title The nucleotide sequence at the proximal end of rpoB gene of !1Escherichia coli. !$#accession B00689 !'##molecule_type DNA !'##residues 54-121 ##label GUR1 !'##cross-references EMBL:V00339; NID:g42813 REFERENCE S26952 !$#authors Bubunenko, M.G.; Chuikov, S.V.; Gudkov, A.T. !$#journal FEBS Lett. (1992) 313:232-234 !$#title The length of the interdomain region of the L7/L12 protein !1is important for its function. !$#cross-references MUID:93076902; PMID:1446741 !$#accession S26952 !'##molecule_type DNA !'##residues 39-53 ##label BUB REFERENCE I52538 !$#authors Gurevich, A.I.; Avakov, A.E.; Kolosov, M.N. !$#journal Bioorg. Khim. (1979) 5:779-781 !$#title The nucleotide sequence of a regulatory site between rplL !1and rpoB genes of E.coli. !$#accession I52538 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 116-121 ##label GUR2 !'##cross-references GB:M38332; NID:g147733; PIDN:AAA24588.1; !1PID:g147734 REFERENCE I52537 !$#authors Gurevich, A.I.; Avakov, A.E. !$#journal Bioorg. Khim. (1979) 5:301-304 !$#title Sequence determination in 3'-end proximately labelled DNA. !$#accession I52537 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 54-92 ##label GUR3 !'##cross-references GB:M38301; NID:g147698; PIDN:AAA24573.1; !1PID:g551830 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65205 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-121 ##label BLAT !'##cross-references GB:AE000472; GB:U00096; NID:g2367333; !1PIDN:AAC76960.1; PID:g1790418; UWGP:b3986 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note mass spectrographic analysis of post-translational !1modifications; any acid labile modifications may have been !1missed REFERENCE A50102 !$#authors Leijonmarck, M.; Liljas, A. !$#submission submitted to the Brookhaven Protein Data Bank, September !11986 !$#cross-references PDB:1CTF !$#contents annotation; X-ray crystallography, 1.7 angstroms, residues !154-121 REFERENCE A30651 !$#authors Leijonmarck, M.; Liljas, A. !$#journal J. Mol. Biol. (1987) 195:555-580 !$#title Structure of the C-terminal domain of the ribosomal protein !1L7/L12 from Escherichia coli at 1.7 angstroms. !$#cross-references MUID:88011269; PMID:3309338 !$#contents annotation; X-ray crystallography, 1.7 angstroms COMMENT For ribosomal-protein-serine acetyltransferase rimL, see !1PIR:XXECPL. GENETICS !$#gene rplL !$#map_position 90 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX large subunit ribosomal proteins: L1 (PIR:R5EC1), L3 !1(PIR:R5EC3), L2 (PIR:R5EC2), L4 (PIR:R5EC4), L5 (PIR:R5EC5), !1L6 (PIR:R5EC6), L7/L12 (PIR:R5EC7), L9 (PIR:R5EC9), L10 !1(PIR:R5EC10), L11 (PIR:R5EC11), L13 (PIR:R5EC13), L14 !1(PIR:R5EC14), L15 (PIR:R5EC15), L16 (PIR:R5EC16), L17 !1(PIR:R5EC17), L18 (PIR:R5EC18), L19 (PIR:R5EC19) FUNCTION !$#pathway protein biosynthesis CLASSIFICATION #superfamily Escherichia coli ribosomal protein L12 KEYWORDS acetylated amino end; methylated amino acid; protein !1biosynthesis; ribosome FEATURE !$2-121 #product ribosomal protein L12 #status experimental !8#label ML12\ !$2-121 #product ribosomal protein L7 #status experimental !8#label ML7\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #link ML7 #status experimental\ !$82 #modified_site N6-methyllysine (Lys) #link ML12 !8#status experimental SUMMARY #length 121 #molecular-weight 12295 #checksum 3011 SEQUENCE /// ENTRY R5EB12 #type complete TITLE ribosomal protein L7/L12 - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 22-Jun-1999 ACCESSIONS S12828; S10896; S12165 REFERENCE S12827 !$#authors Zhyvoloup, A.N.; Woodmaska, M.I.; Kroupskaya, I.V.; Paton, !1E.B. !$#journal Nucleic Acids Res. (1990) 18:4620 !$#title Nucleotide sequence of the rplJL operon and the deduced !1primary structure of the encoded L10 and L7/L12 proteins of !1Salmonella typhimurium compared to that of Escherichia coli. !$#cross-references MUID:90356427; PMID:2201953 !$#accession S12828 !'##molecule_type DNA !'##residues 1-121 ##label ZHY !'##cross-references EMBL:X53072; NID:g47915; PIDN:CAA37246.1; !1PID:g47917 REFERENCE S10895 !$#authors Paton, E.B.; Woodmaska, M.I.; Kroupskaya, I.V.; Zhyvoloup, !1A.N.; Matsuka, G.K. !$#journal FEBS Lett. (1990) 265:129-132 !$#title Evidence for the ability of L10 ribosomal proteins of !1Salmonella typhimurium and Klebsiella pneumoniae to regulate !1rplJL gene expression in Escherichia coli. !$#cross-references MUID:90306303; PMID:2194828 !$#accession S10896 !'##molecule_type DNA !'##residues 1-55 ##label PAT !'##cross-references EMBL:X53072 GENETICS !$#gene rplL CLASSIFICATION #superfamily Escherichia coli ribosomal protein L12 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-121 #product ribosomal protein L7/L12 #status predicted !8#label MAT SUMMARY #length 121 #molecular-weight 12299 #checksum 3233 SEQUENCE /// ENTRY R5DV7 #type complete TITLE ribosomal protein L7/L12 - Desulfovibrio vulgaris (strain Miyazaki) ORGANISM #formal_name Desulfovibrio vulgaris DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 06-Sep-1996 ACCESSIONS A02769 REFERENCE A02769 !$#authors Itoh, T.; Otaka, E. !$#journal Biochim. Biophys. Acta (1984) 789:229-233 !$#title Complete amino-acid sequence of an L7/L12-type ribosomal !1protein from Desulfovibrio vulgaris, Miyazaki. !$#accession A02769 !'##molecule_type protein !'##residues 1-126 ##label ITO CLASSIFICATION #superfamily Escherichia coli ribosomal protein L12 KEYWORDS methylated amino acid; protein biosynthesis; ribosome FEATURE !$76,87 #modified_site N6-methyllysine (Lys) #status !8experimental SUMMARY #length 126 #molecular-weight 13213 #checksum 6759 SEQUENCE /// ENTRY R5BS9 #type complete TITLE ribosomal protein L7/L12 - Bacillus subtilis ALTERNATE_NAMES ribosomal protein BL9 ORGANISM #formal_name Bacillus subtilis DATE 30-Nov-1980 #sequence_revision 17-Apr-1998 #text_change 16-Jun-2000 ACCESSIONS F69695; A02770; A91955 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69695 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-123 ##label KUN !'##cross-references GB:Z99104; GB:AL009126; NID:g2632267; !1PIDN:CAB11881.1; PID:g2632372 !'##experimental_source strain 168 REFERENCE A91450 !$#authors Itoh, T.; Wittmann-Liebold, B. !$#journal FEBS Lett. (1978) 96:392-394 !$#title The primary structure of Bacillus subtilis acidic ribosomal !1protein B-L9 and its comparison with Escherichia coli !1proteins L7/L12. !$#cross-references MUID:79086261; PMID:103754 !$#contents preliminary report !$#accession A02770 !'##molecule_type protein !'##residues 2-53,56-97,'EV',98-123 ##label ITO REFERENCE A91955 !$#authors Itoh, T.; Wittmann-Liebold, B. !$#journal J. Biochem. (1980) 87:1185-1198 !$#title The primary structure of Bacillus subtilis acidic ribosomal !1protein B-L9. !$#cross-references MUID:80227647; PMID:6771249 !$#accession A91955 !'##molecule_type protein !'##residues 2-53,56-97,'EV',98-123 ##label ITO2 !'##experimental_source ATCC 6633 GENETICS !$#gene rplL CLASSIFICATION #superfamily Escherichia coli ribosomal protein L12 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 123 #molecular-weight 12751 #checksum 4181 SEQUENCE /// ENTRY R7MCML #type complete TITLE ribosomal protein L7/L12 - Micrococcus luteus ALTERNATE_NAMES ribosomal protein MA ORGANISM #formal_name Micrococcus luteus, Micrococcus lysodeikticus DATE 29-Jun-1981 #sequence_revision 29-Jun-1981 #text_change 13-Jan-1995 ACCESSIONS A02771 REFERENCE A02771 !$#authors Itoh, T. !$#journal FEBS Lett. (1981) 127:67-70 !$#title Primary structure of an acidic ribosomal protein from !1Micrococcus lysodeikticus. !$#cross-references MUID:81237101; PMID:7250376 !$#accession A02771 !'##molecule_type protein !'##residues 1-118 ##label ITO !'##note this protein exists in two almost identical forms, MA1 and MA2, !1the only difference between them being that in MA2 the amino !1end is acetylated CLASSIFICATION #superfamily Escherichia coli ribosomal protein L12 KEYWORDS acetylated amino end; protein biosynthesis; ribosome FEATURE !$1 #modified_site acetylated amino end (Met) (partial) !8#status experimental SUMMARY #length 118 #molecular-weight 12372 #checksum 2889 SEQUENCE /// ENTRY R5BS12 #type complete TITLE ribosomal protein L12 - Bacillus stearothermophilus ALTERNATE_NAMES ribosomal A protein; ribosomal protein BL13 ORGANISM #formal_name Bacillus stearothermophilus DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 30-Jun-1993 ACCESSIONS S00076 REFERENCE S00076 !$#authors Garland, W.G.; Louie, K.A.; Matheson, A.T.; Liljas, A. !$#journal FEBS Lett. (1987) 220:43-46 !$#title The complete amino acid sequence of the ribosomal 'A' !1protein (L12) from Bacillus stearothermophilus. !$#cross-references MUID:87276569; PMID:3609321 !$#accession S00076 !'##molecule_type protein !'##residues 1-122 ##label GAR CLASSIFICATION #superfamily Escherichia coli ribosomal protein L12 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 122 #molecular-weight 12780 #checksum 1881 SEQUENCE /// ENTRY R7HG12 #type complete TITLE ribosomal protein L7/L12 - Thermotoga maritima (strain MSB8) ORGANISM #formal_name Thermotoga maritima DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 21-Jul-2000 ACCESSIONS E44466; S41465; B72376; S19902 REFERENCE A44466 !$#authors Liao, D.; Dennis, P.P. !$#journal J. Biol. Chem. (1992) 267:22787-22797 !$#title The organization and expression of essential transcription !1translation component genes in the extremely thermophilic !1eubacterium Thermotoga maritima. !$#cross-references MUID:93054590; PMID:1429627 !$#accession E44466 !'##molecule_type DNA !'##residues 1-128 ##label LIA !'##cross-references EMBL:Z11839; NID:g407020; PIDN:CAA77862.1; !1PID:g48187 !'##note sequence extracted from NCBI backbone (NCBIP:118058) REFERENCE S41462 !$#authors Palm, P.; Schleper, C.; Arnold-Ammer, I.; Holz, I.; Meier, !1T.; Lottspeich, F.; Zillig, W. !$#journal Nucleic Acids Res. (1993) 21:4904-4908 !$#title The DNA-dependent RNA-polymerase of Thermotoga maritima; !1characterisation of the enzyme and the DNA-sequence of the !1genes for the large subunits. !$#cross-references MUID:94232816; PMID:8177738 !$#accession S41465 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-128 ##label PAL !'##cross-references EMBL:X72695; NID:g425255; PIDN:CAA51245.1; !1PID:g425257 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1March 1993 REFERENCE A72200 !$#authors Nelson, K.E.; Clayton, R.A.; Gill, S.R.; Gwinn, M.L.; !1Dodson, R.J.; Haft, D.H.; Hickey, E.K.; Peterson, J.D.; !1Nelson, W.C.; Ketchum, K.A.; McDonald, L.; Utterback, T.R.; !1Malek, J.A.; Linher, K.D.; Garrett, M.M.; Stewart, A.M.; !1Cotton, M.D.; Pratt, M.S.; Phillips, C.A.; Richardson, D.; !1Heidelberg, J.; Sutton, G.G.; Fleischmann, R.D.; White, O.; !1Salzberg, S.L.; Smith, H.O.; Venter, J.C.; Fraser, C.M. !$#journal Nature (1999) 399:323-329 !$#title Evidence for lateral gene transfer between Archaea and !1Bacteria from genome sequence of Thermotoga maritima. !$#cross-references MUID:99287316; PMID:10360571 !$#accession B72376 !'##molecule_type DNA !'##residues 'MK',1-128 ##label ARN !'##cross-references GB:AE001723; GB:AE000512; NID:g4980953; !1PIDN:AAD35540.1; PID:g4980963; TIGR:TM0457 !'##experimental_source strain MSB8 GENETICS !$#gene TM0457 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L12 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 128 #molecular-weight 13457 #checksum 709 SEQUENCE /// ENTRY R5HG12 #type complete TITLE ribosomal protein L12 - Haloanaerobium praevalens ALTERNATE_NAMES ribosomal A protein ORGANISM #formal_name Haloanaerobium praevalens DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 30-Jun-1993 ACCESSIONS S06332 REFERENCE S06332 !$#authors Matheson, A.T.; Louie, K.A.; Tak, B.D.; Zuker, M. !$#journal Biochimie (1987) 69:1013-1020 !$#title The primary structure of the ribosomal A-protein (L12) from !1the halophilic eubacterium Haloanaerobium praevalens. !$#cross-references MUID:88163789; PMID:3126821 !$#accession S06332 !'##molecule_type protein !'##residues 1-122 ##label MAT CLASSIFICATION #superfamily Escherichia coli ribosomal protein L12 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 122 #molecular-weight 12705 #checksum 2632 SEQUENCE /// ENTRY R7SMG #type complete TITLE ribosomal protein L12 - Streptomyces griseus ALTERNATE_NAMES ribosomal protein SA1 ORGANISM #formal_name Streptomyces griseus DATE 14-Nov-1983 #sequence_revision 22-Jul-1994 #text_change 22-Jun-1999 ACCESSIONS S32239; A02772 REFERENCE S32234 !$#authors Kuester, K.; Kuberski, S.; Piepersberg, W.; Distler, J. !$#submission submitted to the EMBL Data Library, March 1993 !$#description Cloning and nucleotide sequence analysis of the !1nusG-rplK-rplA-rplJ-rplL gene cluster of S. griseus. !$#accession S32239 !'##molecule_type DNA !'##residues 1-127 ##label KUE !'##cross-references EMBL:X72787; NID:g575399; PIDN:CAA51301.1; !1PID:g288465 REFERENCE A02772 !$#authors Itoh, T.; Sugiyama, M.; Higo, K.I. !$#journal Biochim. Biophys. Acta (1982) 701:164-172 !$#title The primary structure of an acidic ribosomal protein from !1Streptomyces griseus. !$#accession A02772 !'##molecule_type protein !'##residues 2-53,55-127 ##label ITO GENETICS !$#gene rplL CLASSIFICATION #superfamily Escherichia coli ribosomal protein L12 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 127 #molecular-weight 13271 #checksum 7184 SEQUENCE /// ENTRY R5RFRA #type complete TITLE ribosomal protein L7/L12 - Rhodobacter sphaeroides ALTERNATE_NAMES ribosomal protein RA ORGANISM #formal_name Rhodobacter sphaeroides DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 31-Dec-1993 ACCESSIONS A02773 REFERENCE A02773 !$#authors Itoh, T.; Higo, K.I. !$#journal Biochim. Biophys. Acta (1983) 744:105-109 !$#title Complete amino acid sequence of an L7/L12-type ribosomal !1protein from Rhodopseudomonas spheroides. !$#accession A02773 !'##molecule_type protein !'##residues 1-124 ##label ITO CLASSIFICATION #superfamily Escherichia coli ribosomal protein L12 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 124 #molecular-weight 12757 #checksum 4138 SEQUENCE /// ENTRY R7SP12 #type complete TITLE ribosomal protein L12 precursor, chloroplast - spinach ORGANISM #formal_name Spinacia oleracea #common_name spinach DATE 13-Jun-1983 #sequence_revision 30-Jun-1991 #text_change 22-Jun-1999 ACCESSIONS A30115; A02774 REFERENCE A30115 !$#authors Giese, K.; Subramanian, A.R. !$#journal Biochemistry (1989) 28:3525-3529 !$#title Chloroplast ribosomal protein L12 is encoded in the nucleus: !1construction and identification of its cDNA clones and !1nucleotide sequence including the transit peptide. !$#cross-references MUID:89302955; PMID:2568127 !$#accession A30115 !'##molecule_type mRNA !'##residues 1-189 ##label GIE !'##cross-references GB:J02849; NID:g170114; PIDN:AAA34031.1; !1PID:g170115 !'##note the authors translated the codon GAA for residue 154 as Lys REFERENCE A02774 !$#authors Bartsch, M.; Kimura, M.; Subramanian, A.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:6871-6875 !$#title Purification, primary structure, and homology relationships !1of a chloroplast ribosomal protein. !$#accession A02774 !'##molecule_type protein !'##residues 57-111,115-189 ##label BAR GENETICS !$#genome nuclear CLASSIFICATION #superfamily Escherichia coli ribosomal protein L12 KEYWORDS chloroplast; protein biosynthesis; ribosome FEATURE !$1-56 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$57-189 #product ribosomal protein L12, chloroplast #status !8experimental #label MAT SUMMARY #length 189 #molecular-weight 19933 #checksum 7146 SEQUENCE /// ENTRY R5HUP0 #type complete TITLE acidic ribosomal protein P0, cytosolic [validated] - human ALTERNATE_NAMES ribosomal phosphoprotein P0; ribosomal protein HL10e ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 21-Jul-2000 ACCESSIONS A27125 REFERENCE A93096 !$#authors Rich, B.E.; Steitz, J.A. !$#journal Mol. Cell. Biol. (1987) 7:4065-4074 !$#title Human acidic ribosomal phosphoproteins P0, P1, and P2: !1analysis of cDNA clones, in vitro synthesis, and assembly. !$#cross-references MUID:88122131; PMID:3323886 !$#accession A27125 !'##molecule_type mRNA !'##residues 1-317 ##label RIC !'##cross-references GB:M17885; NID:g190231; PIDN:AAA36470.1; !1PID:g190232 !'##note the protein is designated as ribosomal protein P0 according to !1comigration analysis after in vitro translation GENETICS !$#gene GDB:RPLP0; PRLP0 !'##cross-references GDB:132840 !$#map_position 17p12-17p11.2 CLASSIFICATION #superfamily rat acidic ribosomal protein P0 KEYWORDS phosphoprotein; protein biosynthesis; ribosome; RNA binding SUMMARY #length 317 #molecular-weight 34273 #checksum 2958 SEQUENCE /// ENTRY R5RT10 #type complete TITLE acidic ribosomal protein P0, cytosolic [similarity] - rat ALTERNATE_NAMES ribosomal phosphoprotein P0; ribosomal protein RL10e ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 23-Mar-2001 ACCESSIONS S08021; S41396; A48397 REFERENCE S08022 !$#authors Chan, Y.L.; Paz, V.; Wool, I.G. !$#submission submitted to the EMBL Data Library, April 1989 !$#description The primary sequence of rat acidic ribosomal phosphoprotein !1P0. !$#accession S08021 !'##molecule_type mRNA !'##residues 1-316 ##label CHA !'##cross-references EMBL:X15096; NID:g57707; PIDN:CAA33199.1; !1PID:g57708 REFERENCE S41396 !$#authors Loedemel, O.O. !$#submission submitted to the EMBL Data Library, January 1994 !$#accession S41396 !'##molecule_type mRNA !'##residues 1-280,'V',282-286,'A',288-293,'A',294-316 ##label LOE !'##cross-references EMBL:Z29530; NID:g450369; PIDN:CAA82647.1; !1PID:g450370 REFERENCE A48397 !$#authors Wool, I.G.; Chan, Y.L.; Gluck, A.; Suzuki, K. !$#journal Biochimie (1991) 73:861-870 !$#title The primary structure of rat ribosomal proteins P0, P1, and !1P2 and a proposal for a uniform nomenclature for mammalian !1and yeast ribosomal proteins. !$#cross-references MUID:92075759; PMID:1742361 !$#accession A48397 !'##molecule_type mRNA !'##residues 1-316 ##label WOO !'##cross-references GB:X15096; NID:g57707; PIDN:CAA33199.1; PID:g57708 !'##note sequence extracted from NCBI backbone (NCBIN:69670, !1NCBIP:69671) COMPLEX ribosomal proteins P0, P1, and P2 form a heteropentameric !1subcomplex composed of two P1 chains (PIR:R5RT12), two P2 !1chains (PIR:R6RTP2), and one P0 chain (PIR:R5RT10) !1[validated, MUID:92075759] CLASSIFICATION #superfamily rat acidic ribosomal protein P0 KEYWORDS phosphoprotein; protein biosynthesis; ribosome; RNA binding SUMMARY #length 316 #molecular-weight 34200 #checksum 8873 SEQUENCE /// ENTRY R5MS10 #type complete TITLE acidic ribosomal protein P0 - mouse ALTERNATE_NAMES ribosomal phosphoprotein P0; ribosomal protein ML10e ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S05305 REFERENCE S05305 !$#authors Krowczynska, A.M.; Coutts, M.; Makrides, S.; Brawerman, G. !$#journal Nucleic Acids Res. (1989) 17:6408 !$#title The mouse homologue of the human acidic ribosomal !1phosphoprotein PO: a highly conserved polypeptide that is !1under translational control. !$#cross-references MUID:89366686; PMID:2771657 !$#accession S05305 !'##molecule_type mRNA !'##residues 1-317 ##label KRO !'##cross-references EMBL:X15267; NID:g50025; PIDN:CAA33338.1; !1PID:g50026 !'##note the authors translated the codon TTC for residue 185 as Ser CLASSIFICATION #superfamily rat acidic ribosomal protein P0 KEYWORDS phosphoprotein; protein biosynthesis; ribosome; RNA binding SUMMARY #length 317 #molecular-weight 34216 #checksum 732 SEQUENCE /// ENTRY R5FFP0 #type complete TITLE acidic ribosomal protein P0 - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES protein AP3 ORGANISM #formal_name Drosophila melanogaster DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 22-Jun-1999 ACCESSIONS A30223 REFERENCE A30223 !$#authors Kelley, M.R.; Venugopal, S.; Harless, J.; Deutsch, W.A. !$#journal Mol. Cell. Biol. (1989) 9:965-973 !$#title Antibody to a human DNA repair protein allows for cloning of !1a Drosophila cDNA that encodes an apurinic endonuclease. !$#cross-references MUID:89261760; PMID:2471063 !$#accession A30223 !'##molecule_type mRNA !'##residues 1-317 ##label KEL !'##cross-references GB:M25772; NID:g576816; PIDN:AAA53372.1; !1PID:g576817 !'##note the authors identified this protein as apurinic endonuclease GENETICS !$#gene FlyBase:Ape !'##cross-references FlyBase:FBgn0000100 !$#map_position 3 79CD CLASSIFICATION #superfamily rat acidic ribosomal protein P0 KEYWORDS phosphoprotein; protein biosynthesis; ribosome; RNA binding SUMMARY #length 317 #molecular-weight 34202 #checksum 9562 SEQUENCE /// ENTRY R5BY0E #type complete TITLE acidic ribosomal protein P0.e, cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES acidic ribosomal protein A0; protein L8300.8; protein YLR340w; ribosomal protein YL10e ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1991 #sequence_revision 19-Jul-1996 #text_change 23-Mar-2001 ACCESSIONS S51343; S00677; JU0077; E35109 REFERENCE S51339 !$#authors Du, Z. !$#submission submitted to the EMBL Data Library, December 1994 !$#description The sequence of S. cerevisiae cosmid 8300. !$#accession S51343 !'##molecule_type DNA !'##residues 1-312 ##label DUZ !'##cross-references EMBL:U19028; NID:g609380; PIDN:AAB67258.1; !1PID:g609387; GSPDB:GN00012; MIPS:YLR340w REFERENCE S00677 !$#authors Mitsui, K.; Tsurugi, K. !$#journal Nucleic Acids Res. (1988) 16:3573 !$#title cDNA and deduced amino acid sequence of 38 kDa-type acidic !1ribosomal protein A0 from Saccharomyces cerevisiae. !$#cross-references MUID:88233942; PMID:3287327 !$#accession S00677 !'##molecule_type mRNA !'##residues 1-82,'Y',84-312 ##label MIT !'##cross-references EMBL:X06959; NID:g4370; PIDN:CAA30029.1; PID:g4371 REFERENCE JU0077 !$#authors Mitsui, K.; Nakagawa, T.; Tsurugi, K. !$#journal J. Biochem. (1989) 106:223-227 !$#title The gene and the primary structure of acidic ribosomal !1protein A0 from yeast Saccharomyces cerevisiae which shows !1partial homology to bacterial ribosomal protein L10. !$#cross-references MUID:90036766; PMID:2681177 !$#accession JU0077 !'##molecule_type DNA !'##residues 1-82,'Y',84-312 ##label MIT2 !'##cross-references GB:D00529; NID:g218395; PIDN:BAA00415.1; !1PID:g218396 REFERENCE A35109 !$#authors Newton, C.H.; Shimmin, L.C.; Yee, J.; Dennis, P.P. !$#journal J. Bacteriol. (1990) 172:579-588 !$#title A family of genes encode the multiple forms of the !1Saccharomyces cerevisiae ribosomal proteins equivalent to !1the Escherichia coli L12 protein and a single form of the !1L10-equivalent ribosomal protein. !$#cross-references MUID:90130289; PMID:2404943 !$#accession E35109 !'##molecule_type DNA !'##residues 1-312 ##label NEW !'##cross-references EMBL:M26506; NID:g171807; PIDN:AAA34731.1; !1PID:g171809 GENETICS !$#gene SGD:RPL10E; RPA0; L10E; YSCA0; MIPS:YLR340w !'##cross-references SGD:S0004332; MIPS:YLR340w !$#map_position 12R CLASSIFICATION #superfamily rat acidic ribosomal protein P0 KEYWORDS phosphoprotein; protein biosynthesis; ribosome; RNA binding SUMMARY #length 312 #molecular-weight 33717 #checksum 5516 SEQUENCE /// ENTRY R5DOP0 #type complete TITLE ribosomal protein P0 - slime mold (Dictyostelium discoideum) ALTERNATE_NAMES ribosomal phosphoprotein P0 ORGANISM #formal_name Dictyostelium discoideum DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 22-Jun-1999 ACCESSIONS S14012 REFERENCE S14012 !$#authors Prieto, J.; Candel, E.; Coloma, A. !$#journal Nucleic Acids Res. (1991) 19:1342 !$#title Nucleotide sequence of a cDNA encoding ribosomal protein P0 !1in Dictyostelium discoideum. !$#cross-references MUID:91232922; PMID:2030951 !$#accession S14012 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type mRNA !'##residues 1-305 ##label PRI !'##cross-references EMBL:X56194; NID:g7336; PIDN:CAA39657.1; PID:g7337 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1990 CLASSIFICATION #superfamily rat acidic ribosomal protein P0 KEYWORDS phosphoprotein; protein biosynthesis; ribosome; RNA binding FEATURE !$257-283 #region alanine-rich SUMMARY #length 305 #molecular-weight 33051 #checksum 3637 SEQUENCE /// ENTRY R5UBP0 #type complete TITLE acidic ribosomal protein P0 - red goosefoot ALTERNATE_NAMES light-induced protein, 34K ORGANISM #formal_name Chenopodium rubrum #common_name red goosefoot DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 22-Jun-1999 ACCESSIONS S21519 REFERENCE S21519 !$#authors Kaldenhoff, R.; Richter, G. !$#submission submitted to the EMBL Data Library, May 1989 !$#description Blue light induction of early genes in plant cell cultures. !$#accession S21519 !'##molecule_type mRNA !'##residues 1-321 ##label KAL !'##cross-references EMBL:X15206; NID:g18140; PIDN:CAA33276.1; !1PID:g18141 GENETICS !$#gene CRE2 CLASSIFICATION #superfamily rat acidic ribosomal protein P0 KEYWORDS phosphoprotein; protein biosynthesis; ribosome; RNA binding SUMMARY #length 321 #molecular-weight 34351 #checksum 9782 SEQUENCE /// ENTRY R5UTP0 #type complete TITLE acidic ribosomal protein P0 - Trypanosoma cruzi ORGANISM #formal_name Trypanosoma cruzi DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 22-Jun-1999 ACCESSIONS S22951; S17338; S19949 REFERENCE S22951 !$#authors Schijman, A.G.; Levin, M.J. !$#journal Nucleic Acids Res. (1992) 20:2894 !$#title Nucleotide sequence of a cDNA encoding a Trypanosoma cruzi !1acidic ribosomal PO protein: a novel C-terminal domain in !1T.cruzi ribosomal P proteins. !$#cross-references MUID:92311000; PMID:1614881 !$#accession S22951 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type mRNA !'##residues 1-321 ##label SCH1 !'##cross-references EMBL:X65066; NID:g10641; PIDN:CAA46199.1; !1PID:g10642 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1March 1992 REFERENCE S17338 !$#authors Schijman, A.G.; Levitus, G.L.; Levin, M.J. !$#submission submitted to the EMBL Data Library, September 1991 !$#description Characterization of the C-terminal region of a Trypanosoma !1cruzi ribosomal P0 protein that does not react with Lupus !1anti-P autoantibodies. !$#accession S17338 !'##molecule_type mRNA !'##residues 244-284,'V',286-290,'V',291,293-305,'F',307-321 ##label !1SCH2 !'##cross-references EMBL:X62144; NID:g11026; PIDN:CAA44070.1; !1PID:g11027 CLASSIFICATION #superfamily rat acidic ribosomal protein P0 KEYWORDS phosphoprotein; protein biosynthesis; ribosome; RNA binding SUMMARY #length 321 #molecular-weight 34777 #checksum 1804 SEQUENCE /// ENTRY R5HSL0 #type complete TITLE ribosomal protein L10 [similarity] - Halobacterium salinarum ALTERNATE_NAMES ribosomal protein P0 ORGANISM #formal_name Halobacterium salinarum DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 21-Jul-2000 ACCESSIONS S01315; S04120; S11587 REFERENCE S01314 !$#authors Itoh, T. !$#journal Eur. J. Biochem. (1988) 176:297-303 !$#title Complete nucleotide sequence of the ribosomal 'A' protein !1operon from the archaebacterium, Halobacterium halobium. !$#cross-references MUID:88329082; PMID:2458258 !$#accession S01315 !'##molecule_type DNA !'##residues 1-352 ##label ITO !'##cross-references EMBL:X13008; NID:g43532; PIDN:CAA31431.1; !1PID:g43534 !'##experimental_source strain S9 !'##note the source is designated as Halobacterium halobium REFERENCE S04116 !$#authors Shimmin, L.C.; Dennis, P.P. !$#journal EMBO J. (1989) 8:1225-1235 !$#title Characterization of the L11, L1, L10 and L12 equivalent !1ribosomal protein gene cluster of the halophilic !1archaebacterium Halobacterium cutirubrum. !$#cross-references MUID:89305527; PMID:2743981 !$#accession S04120 !'##molecule_type DNA !'##residues 1-58,'V',60-352 ##label SHI !'##cross-references EMBL:X15078; NID:g43449; PIDN:CAA33180.1; !1PID:g43454 !'##note the source is designated as Halobacterium cutirubrum CLASSIFICATION #superfamily rat acidic ribosomal protein P0 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 352 #molecular-weight 37213 #checksum 7192 SEQUENCE /// ENTRY R5HS10 #type complete TITLE ribosomal protein L10 [similarity] - Haloarcula marismortui ORGANISM #formal_name Haloarcula marismortui DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 21-Jul-2000 ACCESSIONS S08422 REFERENCE S08420 !$#authors Arndt, E.; Weigel, C. !$#journal Nucleic Acids Res. (1990) 18:1285 !$#title Nucleotide sequence of the genes encoding the L11, L1, L10 !1and L12 equivalent ribosomal proteins from the !1archaebacterium Halobacterium marismortui. !$#cross-references MUID:90206791; PMID:2320419 !$#accession S08422 !'##status translation not shown !'##molecule_type DNA !'##residues 1-348 ##label ARN !'##cross-references EMBL:X51430; NID:g43602; PIDN:CAA35795.1; !1PID:g43605 !'##note the source is designated as Halobacterium marismortui CLASSIFICATION #superfamily rat acidic ribosomal protein P0 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 348 #molecular-weight 37194 #checksum 8859 SEQUENCE /// ENTRY R5MX10 #type complete TITLE ribosomal protein L10 - Methanococcus vannielii ALTERNATE_NAMES ribosomal protein ML2 ORGANISM #formal_name Methanococcus vannielii DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 22-Jun-1999 ACCESSIONS S03956; A37530 REFERENCE S03956 !$#authors Koepke, A.K.E.; Baier, G.; Wittmann-Liebold, B. !$#journal FEBS Lett. (1989) 247:167-172 !$#title An archaebacterial gene from Methanococcus vannielii !1encoding a protein homologous to the ribosomal protein L10 !1family. !$#cross-references MUID:89232111; PMID:2497026 !$#accession S03956 !'##molecule_type DNA !'##residues 1-336 ##label KOE !'##cross-references GB:X15352; NID:g44742; PIDN:CAA33410.1; PID:g44743 !$#accession A37530 !'##molecule_type protein !'##residues 1-5,'X',7-11 ##label KOE2 CLASSIFICATION #superfamily rat acidic ribosomal protein P0 KEYWORDS protein biosynthesis; ribosome FEATURE !$1-336 #product ribosomal protein L10 #status experimental !8#label MAT SUMMARY #length 336 #molecular-weight 35950 #checksum 6981 SEQUENCE /// ENTRY R5RTL5 #type complete TITLE ribosomal protein L5, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 21-Jul-2000 ACCESSIONS S00111; A30439; A27380 REFERENCE S00111 !$#authors Tamura, S.; Kuwano, Y.; Nakayama, T.; Tanaka, S.; Tanaka, !1T.; Ogata, K. !$#journal Eur. J. Biochem. (1987) 168:83-87 !$#title Molecular cloning and nucleotide sequence of cDNA specific !1for rat ribosomal protein L5. !$#cross-references MUID:88029432; PMID:3117543 !$#accession S00111 !'##molecule_type mRNA !'##residues 1-297 ##label TAM !'##cross-references EMBL:X06148; NID:g57124; PIDN:CAA29506.1; !1PID:g57125 !$#accession A30439 !'##molecule_type protein !'##residues 2-47 ##label TAM2 REFERENCE A27380 !$#authors Chan, Y.L.; Lin, A.; McNally, J.; Wool, I.G. !$#journal J. Biol. Chem. (1987) 262:12879-12886 !$#title The primary structure of rat ribosomal protein L5. A !1comparison of the sequence of amino acids in the proteins !1that interact with 5 S rRNA. !$#cross-references MUID:87308330; PMID:3624282 !$#accession A27380 !'##molecule_type mRNA !'##residues 1-234,236-297 ##label CHA !'##cross-references GB:M17419; NID:g206733; PIDN:AAA42074.1; !1PID:g206734 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing !'##note the protein is designated as ribosomal protein L5 COMMENT this protein binds to 5S rRNA. CLASSIFICATION #superfamily rat ribosomal protein L5 KEYWORDS protein biosynthesis; ribosome; RNA binding FEATURE !$2-297 #product ribosomal protein L5 #status experimental !8#label MAT SUMMARY #length 297 #molecular-weight 34458 #checksum 7479 SEQUENCE /// ENTRY R5MX18 #type complete TITLE ribosomal protein L18 - Methanococcus vannielii ORGANISM #formal_name Methanococcus vannielii DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 22-Jun-1999 ACCESSIONS S05623 REFERENCE S05611 !$#authors Auer, J.; Spicker, G.; Boeck, A. !$#journal J. Mol. Biol. (1989) 209:21-36 !$#title Organization and structure of the Methanococcus !1transcriptional unit homologous to the Escherichia coli !1"spectinomycin operon". Implications for the evolutionary !1relationship of 70 S and 80 S ribosomes. !$#cross-references MUID:90040717; PMID:2530355 !$#accession S05623 !'##molecule_type DNA !'##residues 1-195 ##label AUE !'##cross-references EMBL:X16720; NID:g44754; PIDN:CAA34699.1; !1PID:g44767 CLASSIFICATION #superfamily rat ribosomal protein L5 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 195 #molecular-weight 21820 #checksum 2768 SEQUENCE /// ENTRY R5HS18 #type complete TITLE ribosomal protein L18 [validated] - Haloarcula marismortui ALTERNATE_NAMES ribosomal protein HL12; ribosomal protein HL13 ORGANISM #formal_name Haloarcula marismortui DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 31-Mar-2000 ACCESSIONS S16541; G28949; A33084; T46806 REFERENCE S16535 !$#authors Scholzen, T.; Arndt, E. !$#journal Mol. Gen. Genet. (1991) 228:70-80 !$#title Organization and nucleotide sequence of ten ribosomal !1protein genes from the region equivalent to the !1spectinomycin operon in the archaebacterium Halobacterium !1marismortui. !$#cross-references MUID:91360093; PMID:1832208 !$#accession S16541 !'##molecule_type DNA !'##residues 1-187 ##label SCH !'##cross-references EMBL:X58395; NID:g48860; PIDN:CAA41290.1; !1PID:g48867 REFERENCE A28926 !$#authors Walsh, M.J.; McDougall, J.; Wittmann-Liebold, B. !$#journal Biochemistry (1988) 27:6867-6876 !$#title Extended N-terminal sequencing of proteins of !1archaebacterial ribosomes blotted from two-dimensional gels !1onto glass fiber and poly(vinylidene difluoride) membrane. !$#cross-references MUID:89062418; PMID:3196689 !$#accession G28949 !'##molecule_type protein !'##residues 2-17,'A',19-25 ##label WAL !'##note the protein is designated as ribosomal protein L12 REFERENCE A33084 !$#authors McDougall, J. !$#submission submitted to the Protein Sequence Database, June 1990 !$#accession A33084 !'##molecule_type protein !'##residues 2,'V',4-24 ##label MCD !'##experimental_source strain DSM 3752 GENETICS !$#gene HmaL18 CLASSIFICATION #superfamily rat ribosomal protein L5 KEYWORDS protein biosynthesis; ribosome; RNA binding FEATURE !$2-187 #product ribosomal protein L18 #status experimental !8#label MAT SUMMARY #length 187 #molecular-weight 20614 #checksum 3877 SEQUENCE /// ENTRY R6HUP2 #type complete TITLE acidic ribosomal protein P2, cytosolic [validated] - human ALTERNATE_NAMES ribosomal phosphoprotein P2; ribosomal protein HL12eI ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 21-Jul-2000 ACCESSIONS C27125; A60167 REFERENCE A93096 !$#authors Rich, B.E.; Steitz, J.A. !$#journal Mol. Cell. Biol. (1987) 7:4065-4074 !$#title Human acidic ribosomal phosphoproteins P0, P1, and P2: !1analysis of cDNA clones, in vitro synthesis, and assembly. !$#cross-references MUID:88122131; PMID:3323886 !$#accession C27125 !'##molecule_type mRNA !'##residues 1-115 ##label RIC !'##cross-references GB:M17887; NID:g190235; PIDN:AAA36472.1; !1PID:g190236 !'##note the protein is designated as ribosomal protein P2 according to !1comigration analysis after in vitro translation REFERENCE A60167 !$#authors Sharp, M.G.F.; Adams, S.M.; Elvin, P.; Walker, R.A.; !1Brammar, W.J.; Varley, J.M. !$#journal Br. J. Cancer (1990) 61:83-88 !$#title A sequence previously identified as metastasis-related !1encodes an acidic ribosomal phosphoprotein, P2. !$#cross-references MUID:90122586; PMID:2153399 !$#accession A60167 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-115 ##label SHA GENETICS !$#gene GDB:RPLP2 !'##cross-references GDB:132841 !$#map_position 17p12-17p11.2 CLASSIFICATION #superfamily rat acidic ribosomal protein P1 KEYWORDS phosphoprotein; protein biosynthesis; ribosome SUMMARY #length 115 #molecular-weight 11665 #checksum 2334 SEQUENCE /// ENTRY R6RTP2 #type complete TITLE acidic ribosomal protein P2, cytosolic [validated] - rat ALTERNATE_NAMES ribosomal phosphoprotein P2; ribosomal protein RL12eI ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 13-Jun-1983 #sequence_revision 31-Dec-1992 #text_change 21-Jul-2000 ACCESSIONS S22320; A02777; C48397; S29053 REFERENCE S22320 !$#authors Chan, Y.L.; Wool, I.G. !$#journal Nucleic Acids Res. (1991) 19:4895-4900 !$#title The structure of a gene containing introns and encoding rat !1ribosomal protein P2. !$#cross-references MUID:92020122; PMID:1923757 !$#accession S22320 !'##molecule_type DNA !'##residues 1-115 ##label CHA !'##cross-references EMBL:X55153; NID:g57675; PIDN:CAA38953.1; !1PID:g57676 REFERENCE A02777 !$#authors Lin, A.; Wittmann-Liebold, B.; McNally, J.; Wool, I.G. !$#journal J. Biol. Chem. (1982) 257:9189-9197 !$#title The primary structure of the acidic phosphoprotein P2 from !1rat liver 60 S ribosomal subunits. Comparison with ribosomal !1'A' proteins from other species. !$#cross-references MUID:82239417; PMID:7096359 !$#accession A02777 !'##molecule_type protein !'##residues 1-23,'A',25-38,'K',39-78,'A',80-94,100-104,'KK',107,'E', !1109-115 ##label LIN REFERENCE A48397 !$#authors Wool, I.G.; Chan, Y.L.; Gluck, A.; Suzuki, K. !$#journal Biochimie (1991) 73:861-870 !$#title The primary structure of rat ribosomal proteins P0, P1, and !1P2 and a proposal for a uniform nomenclature for mammalian !1and yeast ribosomal proteins. !$#cross-references MUID:92075759; PMID:1742361 !$#accession C48397 !'##molecule_type mRNA !'##residues 1-115 ##label WOO !'##cross-references GB:X15098; NID:g57711; PIDN:CAA33201.1; PID:g57712 !'##note sequence extracted from NCBI backbone (NCBIN:69682, !1NCBIP:69686) REFERENCE S29053 !$#authors Furukawa, T.; Uchiumi, T.; Tokunaga, R.; Taketani, S. !$#journal Arch. Biochem. Biophys. (1992) 298:182-186 !$#title Ribosomal protein P2, a novel iron-binding protein. !$#cross-references MUID:92398340; PMID:1524426 !$#accession S29053 !'##molecule_type protein !'##residues 7-20,26-38,50-74 ##label FUR GENETICS !$#introns 41/3; 58/1; 91/1 COMPLEX ribosomal proteins P0, P1, and P2 form a heteropentameric !1subcomplex composed of two P1 chains (PIR:R5RT12), two P2 !1chains (PIR:R6RTP2), and one P0 chain (PIR:R5RT10) !1[validated, MUID:92075759] CLASSIFICATION #superfamily rat acidic ribosomal protein P1 KEYWORDS phosphoprotein; protein biosynthesis; ribosome FEATURE !$1-115 #product acidic ribosomal protein P2 #status !8experimental #label MAT SUMMARY #length 115 #molecular-weight 11692 #checksum 2312 SEQUENCE /// ENTRY R6FFP2 #type complete TITLE acidic ribosomal protein P2 - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES ribosomal protein DL12eI; ribosomal protein rpA1 ORGANISM #formal_name Drosophila melanogaster DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 22-Jun-1999 ACCESSIONS A26401 REFERENCE A26401 !$#authors Qian, S.; Zhang, J.Y.; Kay, M.A.; Jacobs-Lorena, M. !$#journal Nucleic Acids Res. (1987) 15:987-1003 !$#title Structural analysis of the Drosophila rpA1 gene, a member of !1the eucaryotic `A' type ribosomal protein family. !$#cross-references MUID:87146465; PMID:3103101 !$#accession A26401 !'##molecule_type DNA !'##residues 1-113 ##label QIA !'##cross-references GB:X05016; NID:g8479; PIDN:CAA28672.1; PID:g8480 GENETICS !$#gene rpa1 !'##cross-references FlyBase:FBgn0003274 !$#map_position 53CD CLASSIFICATION #superfamily rat acidic ribosomal protein P1 KEYWORDS phosphoprotein; protein biosynthesis; ribosome SUMMARY #length 113 #molecular-weight 11757 #checksum 7106 SEQUENCE /// ENTRY R8SS12 #type complete TITLE ribosomal protein L12eI - brine shrimp ALTERNATE_NAMES ribosomal protein eL12 ORGANISM #formal_name Artemia salina #common_name brine shrimp DATE 30-Nov-1979 #sequence_revision 31-Mar-1992 #text_change 22-Jun-1999 ACCESSIONS A25208; A02775 REFERENCE A91146 !$#authors Maassen, J.A.; Schop, E.N.; Brands, J.H.G.M.; Van Hemert, !1F.J.; Lenstra, J.A.; Moller, W. !$#journal Eur. J. Biochem. (1985) 149:609-616 !$#title Molecular cloning and analysis of cDNA sequences for two !1ribosomal proteins from Artemia. The coordinate expression !1of genes for ribosomal proteins and elongation factor 1 !1during embryogenesis of Artemia. !$#cross-references MUID:85230659; PMID:3839187 !$#accession A25208 !'##molecule_type mRNA !'##residues 1-108 ##label MAA !'##cross-references GB:X02632; NID:g5686; PIDN:CAA26479.1; PID:g5687 REFERENCE A02775 !$#authors Amons, R.; Pluijms, W.; Moller, W. !$#journal FEBS Lett. (1979) 104:85-89 !$#title The primary structure of ribosomal protein eL12/eL12-P from !1Artemia salina 80 S ribosomes. !$#cross-references MUID:80004136; PMID:477981 !$#accession A02775 !'##molecule_type protein !'##residues 1-12,'T',14-18,'TX',21-33,'X',35-79,'A',81-111 ##label AMO !'##note Ser-98 is partially phosphorylated; this results in two !1slightly different forms of the protein CLASSIFICATION #superfamily rat acidic ribosomal protein P1 KEYWORDS phosphoprotein; protein biosynthesis; ribosome FEATURE !$1-111 #product ribosomal protein L12eI #status experimental !8#label MAT\ !$98 #binding_site phosphate (Ser) (covalent) (partial) !8#status experimental SUMMARY #length 111 #molecular-weight 11503 #checksum 8273 SEQUENCE /// ENTRY R5BYA1 #type complete TITLE acidic ribosomal protein P2.e.B, cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES acidic ribosomal protein P2.alpha; protein D9481.1; protein YDR382w; ribosomal protein YL12eIA; ribosomal protein YL45; ribosomal protein YPA1; RPL45 protein ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Oct-1980 #sequence_revision 31-Mar-1992 #text_change 21-Jul-2000 ACCESSIONS A35109; A28104; A02776; S61177; S69666 REFERENCE A35109 !$#authors Newton, C.H.; Shimmin, L.C.; Yee, J.; Dennis, P.P. !$#journal J. Bacteriol. (1990) 172:579-588 !$#title A family of genes encode the multiple forms of the !1Saccharomyces cerevisiae ribosomal proteins equivalent to !1the Escherichia coli L12 protein and a single form of the !1L10-equivalent ribosomal protein. !$#cross-references MUID:90130289; PMID:2404943 !$#accession A35109 !'##molecule_type DNA !'##residues 1-110 ##label NEW !'##cross-references GB:M26505; NID:g171810; PIDN:AAA34732.1; !1PID:g171811 REFERENCE A92726 !$#authors Remacha, M.; Saenz-Robles, M.T.; Vilella, M.D.; Ballesta, !1J.P.G. !$#journal J. Biol. Chem. (1988) 263:9094-9101 !$#title Independent genes coding for three acidic proteins of the !1large ribosomal subunit from Saccharomyces cerevisiae. !$#cross-references MUID:88243786; PMID:2837476 !$#accession A28104 !'##molecule_type DNA !'##residues 1-110 ##label REM !'##cross-references EMBL:J03761; NID:g172397; PIDN:AAA34972.1; !1PID:g172398 !'##note the authors translated the codon GAA for residue 28 as Ala REFERENCE A02776 !$#authors Itoh, T. !$#journal Biochim. Biophys. Acta (1981) 671:16-24 !$#title Primary structure of an acidic ribosomal protein YPA1 from !1Saccharomyces cerevisiae. Isolation and characterization of !1peptide and the complete amino acid sequence. !$#cross-references MUID:82069169; PMID:7030402 !$#accession A02776 !'##molecule_type protein !'##residues 1-74,'GPAS',79-85,'G',86-90,92-110 ##label ITO REFERENCE S61159 !$#authors Ding, H. !$#submission submitted to the EMBL Data Library, June 1995 !$#description The sequence of S. cerevisiae cosmid 9481. !$#accession S61177 !'##molecule_type DNA !'##residues 1-110 ##label DIN !'##cross-references EMBL:U28373; NID:g849184; PIDN:AAB64818.1; !1PID:g849203; GSPDB:GN00004; MIPS:YDR382w !'##experimental_source strain S288C (AB972) REFERENCE S69665 !$#authors Dietrich, F.S. !$#submission submitted to the EMBL Data Library, July 1995 !$#description The sequence of S. cerevisiae cosmids 9481, 9509, 9926, !19461, and lambda 3641. !$#accession S69666 !'##molecule_type DNA !'##residues 1-110 ##label DIE !'##cross-references EMBL:U32274; NID:g927313; PIDN:AAB64824.1; !1PID:g927315; GSPDB:GN00004; MIPS:YDR382w GENETICS !$#gene SGD:RPL45; RPLA4; MIPS:YDR382w !'##cross-references SGD:S0002790; MIPS:YDR382w !$#map_position 4R CLASSIFICATION #superfamily rat acidic ribosomal protein P1 KEYWORDS phosphoprotein; protein biosynthesis; ribosome FEATURE !$1-110 #product acidic ribosomal protein P2.e.B #status !8experimental #label MAT SUMMARY #length 110 #molecular-weight 11050 #checksum 3115 SEQUENCE /// ENTRY R5BYIB #type complete TITLE acidic ribosomal protein P2.e.A, cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES acidic ribosomal protein A2; acidic ribosomal protein P2.beta; protein O2060; protein YOL039w; ribosomal protein YL12eIB; ribosomal protein YL44 ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 21-Jul-2000 ACCESSIONS B28104; S00679; B35109; S66722; S66724; A49495 REFERENCE A92726 !$#authors Remacha, M.; Saenz-Robles, M.T.; Vilella, M.D.; Ballesta, !1J.P.G. !$#journal J. Biol. Chem. (1988) 263:9094-9101 !$#title Independent genes coding for three acidic proteins of the !1large ribosomal subunit from Saccharomyces cerevisiae. !$#cross-references MUID:88243786; PMID:2837476 !$#accession B28104 !'##molecule_type DNA !'##residues 1-106 ##label REM !'##cross-references EMBL:J03760; NID:g172395; PIDN:AAA34971.1; !1PID:g172396 REFERENCE S00679 !$#authors Mitsui, K.; Tsurugi, K. !$#journal Nucleic Acids Res. (1988) 16:3575 !$#title cDNA and deduced amino acid sequence of acidic ribosomal !1protein A2 from Saccharomyces cerevisiae. !$#cross-references MUID:88233944; PMID:3287329 !$#accession S00679 !'##molecule_type mRNA !'##residues 1-106 ##label MIT !'##cross-references EMBL:X06958; NID:g4374; PIDN:CAA30028.1; PID:g4375 REFERENCE A35109 !$#authors Newton, C.H.; Shimmin, L.C.; Yee, J.; Dennis, P.P. !$#journal J. Bacteriol. (1990) 172:579-588 !$#title A family of genes encode the multiple forms of the !1Saccharomyces cerevisiae ribosomal proteins equivalent to !1the Escherichia coli L12 protein and a single form of the !1L10-equivalent ribosomal protein. !$#cross-references MUID:90130289; PMID:2404943 !$#accession B35109 !'##molecule_type DNA !'##residues 1-106 ##label NEW !'##cross-references GB:M26503; NID:g171816; PIDN:AAA34735.1; !1PID:g171817 REFERENCE S66703 !$#authors Habbig, B.; Hattenhorst, U.; Hollenberg, C.P.; Ramezani Rad, !1M. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S66722 !'##molecule_type DNA !'##residues 1-106 ##label HAB !'##cross-references EMBL:Z74781; NID:g1419834; PIDN:CAA99041.1; !1PID:g1419835; GSPDB:GN00015; MIPS:YOL039w !'##experimental_source strain S288C REFERENCE S66723 !$#authors Ansorge, W.; Benes, V.; Rechmann, S.; Schwager, C.; Teodoru, !1C.; Voss, H.; Wiemann, S. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S66724 !'##molecule_type DNA !'##residues 1-106 ##label ANS !'##cross-references EMBL:Z74781; NID:g1419834; PIDN:CAA99041.1; !1PID:g1419835; GSPDB:GN00015; MIPS:YOL039w !'##experimental_source strain S288C REFERENCE A49495 !$#authors Santos, C.; Ortiz-Reyes, B.; Naranda, T.; Remacha, M.; !1Ballesta, J.P.G. !$#journal Biochemistry (1993) 32:4231-4236 !$#title The acidic phosphoproteins from Saccharomyces cerevisiae !1ribosomes. NH-2-terminal acetylation is a conserved !1difference between P1 and P2 proteins. !$#cross-references MUID:93237229; PMID:8476850 !$#accession A49495 !'##status preliminary !'##molecule_type protein !'##residues 1-6 ##label SAN GENETICS !$#gene SGD:RPLA2; RPA2; MIPS:YOL039w !'##cross-references SGD:S0005399; MIPS:YOL039w !$#map_position 15L CLASSIFICATION #superfamily rat acidic ribosomal protein P1 KEYWORDS phosphoprotein; protein biosynthesis; ribosome SUMMARY #length 106 #molecular-weight 10746 #checksum 9947 SEQUENCE /// ENTRY R6BY22 #type complete TITLE 60s acidic ribosomal protein P2.2 - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES acidic ribosomal protein 2; ribosomal protein SP-L40c; ribosomal protein YL12eI ORGANISM #formal_name Schizosaccharomyces pombe DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 10-Dec-1999 ACCESSIONS B34715; A27304; S10054; T40800 REFERENCE A34715 !$#authors Beltrame, M.; Bianchi, M.E. !$#journal Mol. Cell. Biol. (1990) 10:2341-2348 !$#title A gene family for acidic ribosomal proteins in !1Schizosaccharomyces pombe: two essential and two !1nonessential genes. !$#cross-references MUID:90220620; PMID:2325655 !$#accession B34715 !'##molecule_type DNA !'##residues 1-110 ##label BEL1 !'##cross-references GB:M33138; NID:g173465; PIDN:AAA35335.1; !1PID:g173466 REFERENCE A27304 !$#authors Beltrame, M.; Bianchi, M.E. !$#journal Nucleic Acids Res. (1987) 15:9089 !$#title Sequence of the cDNA for one acidic ribosomal protein of !1Schizosaccharomyces pombe. !$#cross-references MUID:88067727; PMID:3684587 !$#accession A27304 !'##molecule_type mRNA !'##residues 1-110 ##label BEL2 !'##cross-references GB:Y00466; NID:g5064; PIDN:CAA68528.1; PID:g5065 REFERENCE S07293 !$#authors Otaka, E.; Higo, K.I.; Itoh, T. !$#journal Mol. Gen. Genet. (1983) 191:519-524 !$#title Yeast ribosomal proteins: VII. Cytoplasmic ribosomal !1proteins from Schizosaccharomyces pombe. !$#cross-references MUID:84038947; PMID:6355773 !$#accession S10054 !'##molecule_type protein !'##residues 1-15,'B',17-21,'B',23,'Z',25-32,'Z',34,'ZXZ',38-39,'Z' !1##label OTA REFERENCE Z21949 !$#authors Beck, A.; Reinhardt, R.; Lyne, M.; Rajandream, M.A.; !1Barrell, B.G. !$#submission submitted to the EMBL Data Library, October 1998 !$#accession T40800 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-110 ##label BEC !'##cross-references EMBL:AL032684; PIDN:CAA21791.1; GSPDB:GN00067; !1SPDB:SPBP8B7.06 !'##experimental_source strain 972h-; clone p1 p8B7 GENETICS !$#gene rpa2 !$#map_position 2 !$#introns 103/3 CLASSIFICATION #superfamily rat acidic ribosomal protein P1 KEYWORDS phosphoprotein; protein biosynthesis; ribosome FEATURE !$1-110 #product acidic ribosomal protein P2.2 #status !8experimental #label MAT SUMMARY #length 110 #molecular-weight 11158 #checksum 2961 SEQUENCE /// ENTRY R6BY24 #type complete TITLE 60s acidic ribosomal protein p2-beta - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES acidic ribosomal protein 4; ribosomal protein YL12eI ORGANISM #formal_name Schizosaccharomyces pombe DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 10-Dec-1999 ACCESSIONS D34715; T39961 REFERENCE A34715 !$#authors Beltrame, M.; Bianchi, M.E. !$#journal Mol. Cell. Biol. (1990) 10:2341-2348 !$#title A gene family for acidic ribosomal proteins in !1Schizosaccharomyces pombe: two essential and two !1nonessential genes. !$#cross-references MUID:90220620; PMID:2325655 !$#accession D34715 !'##molecule_type DNA !'##residues 1-110 ##label BEL !'##cross-references EMBL:M33142; NID:g173469; PIDN:AAA35337.1; !1PID:g173470 REFERENCE Z21893 !$#authors Xiang, Z.; Aves, S.; Wood, V.; Rajandream, M.A.; Barrell, !1B.G. !$#submission submitted to the EMBL Data Library, January 1999 !$#accession T39961 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-110 ##label XIA !'##cross-references EMBL:AL035065; PIDN:CAA22631.1; GSPDB:GN00067; !1SPDB:SPBC23G7.15c !'##experimental_source strain 972h-; cosmid c23G7 GENETICS !$#gene rpa4 !$#map_position 2 !$#introns 103/3 CLASSIFICATION #superfamily rat acidic ribosomal protein P1 KEYWORDS phosphoprotein; protein biosynthesis; ribosome SUMMARY #length 110 #molecular-weight 11120 #checksum 4455 SEQUENCE /// ENTRY R6DOP2 #type complete TITLE acidic ribosomal protein P2 - slime mold (Dictyostelium discoideum) ALTERNATE_NAMES ribosomal phosphoprotein P2 ORGANISM #formal_name Dictyostelium discoideum DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 22-Jun-1999 ACCESSIONS S14014 REFERENCE S14014 !$#authors Prieto, J.; Candel, E.; Coloma, A. !$#journal Nucleic Acids Res. (1991) 19:1341 !$#title Nucleotide sequence of a cDNA encoding acidic ribosomal !1phosphoprotein P2 in Dictyostelium discoideum. !$#cross-references MUID:91232921; PMID:1840653 !$#accession S14014 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type mRNA !'##residues 1-106 ##label PRI !'##cross-references EMBL:X56192; NID:g7340; PIDN:CAA39655.1; PID:g7341 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1990 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing CLASSIFICATION #superfamily rat acidic ribosomal protein P1 KEYWORDS phosphoprotein; protein biosynthesis; ribosome FEATURE !$1-106 #product acidic ribosomal protein P2 #status !8experimental #label MAT\ !$64-85 #region alanine-rich SUMMARY #length 106 #molecular-weight 10509 #checksum 1337 SEQUENCE /// ENTRY R6UT2B #type complete TITLE acidic ribosomal protein P2-B - Trypanosoma cruzi ORGANISM #formal_name Trypanosoma cruzi DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 22-Jun-1999 ACCESSIONS S22950; S19948 REFERENCE S22950 !$#authors Vazquez, M.P.; Schijman, A.G.; Panebra, A.; Levin, M.J. !$#journal Nucleic Acids Res. (1992) 20:2893 !$#title Nucleotide sequence of a cDNA encoding another Trypanosoma !1cruzi acidic ribosomal P2 type protein (TcP2b). !$#cross-references MUID:92310999; PMID:1614880 !$#accession S22950 !'##molecule_type mRNA !'##residues 1-112 ##label VAZ !'##cross-references EMBL:X65065; NID:g10633; PIDN:CAA46198.1; !1PID:g10634 !'##note it is uncertain whether Met-1 or Met-3 is the initiator CLASSIFICATION #superfamily rat acidic ribosomal protein P1 KEYWORDS phosphoprotein; protein biosynthesis; ribosome SUMMARY #length 112 #molecular-weight 10926 #checksum 778 SEQUENCE /// ENTRY R5UT2E #type complete TITLE acidic ribosomal protein P2-A - Trypanosoma cruzi ALTERNATE_NAMES acidic ribosomal protein P-JL5; ribosomal protein TL12eI; TcP2-beta ORGANISM #formal_name Trypanosoma cruzi DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 22-Jun-1999 ACCESSIONS S12585; A60447; S59917 REFERENCE S12585 !$#authors Schijman, A.G.; Dusetti, N.J.; Vazquez, M.P.; Lafon, S.; !1Levy-Yeyati, P.; Levin, M.J. !$#journal Nucleic Acids Res. (1990) 18:3399 !$#title Nucleotide cDNA and complete deduced amino acid sequence of !1a Trypanosoma cruzi ribosomal P protein (P-JL5). !$#cross-references MUID:90287723; PMID:2192363 !$#accession S12585 !'##molecule_type mRNA !'##residues 1-107 ##label SCH !'##cross-references EMBL:X52323; NID:g10635; PIDN:CAA36557.1; !1PID:g10636 REFERENCE A60447 !$#authors Levin, M.J.; Mesri, E.; Benarous, R.; Levitus, G.; Schijman, !1A.; Levy-Yeyati, P.; Chiale, P.A.; Ruiz, A.M.; Kahn, A.; !1Rosenbaum, M.B.; Torres, H.N.; Segura, E.L. !$#journal Am. J. Trop. Med. Hyg. (1989) 41:530-538 !$#title Identification of major Trypanosoma cruzi antigenic !1determinants in chronic chagas' heart disease. !$#cross-references MUID:90053984; PMID:2479275 !$#accession A60447 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 73-83,'G',85-107 ##label LEV REFERENCE S59912 !$#authors Schijman, A.G.; Vazquez, M.P.; Ben Dov, C.; Ghio, S.; !1Lorenzi, H.; Levin, M.J. !$#journal Biochim. Biophys. Acta (1995) 1264:15-18 !$#title Cloning and sequence analysis of the TcP2-beta cDNA variants !1of Trypanosoma cruzi. !$#cross-references MUID:96038812; PMID:7578249 !$#accession S59917 !'##status preliminary !'##molecule_type mRNA !'##residues 1-107 ##label SC2 !'##cross-references EMBL:X52323; NID:g10635; PIDN:CAA36557.1; !1PID:g10636 CLASSIFICATION #superfamily rat acidic ribosomal protein P1 KEYWORDS phosphoprotein; protein biosynthesis; ribosome SUMMARY #length 107 #molecular-weight 10512 #checksum 2854 SEQUENCE /// ENTRY R6HUP1 #type complete TITLE acidic ribosomal protein P1, cytosolic [validated] - human ALTERNATE_NAMES ribosomal phosphoprotein P1; ribosomal protein HL12eII ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 21-Jul-2000 ACCESSIONS B27125 REFERENCE A93096 !$#authors Rich, B.E.; Steitz, J.A. !$#journal Mol. Cell. Biol. (1987) 7:4065-4074 !$#title Human acidic ribosomal phosphoproteins P0, P1, and P2: !1analysis of cDNA clones, in vitro synthesis, and assembly. !$#cross-references MUID:88122131; PMID:3323886 !$#accession B27125 !'##molecule_type mRNA !'##residues 1-114 ##label RIC !'##cross-references EMBL:M17886; NID:g190233; PIDN:AAA36471.1; !1PID:g190234 !'##note the protein is designated as ribosomal protein P1 according to !1comigration analysis after in vitro translation GENETICS !$#gene GDB:RPLP1 !'##cross-references GDB:132842 !$#map_position 17p12-17p11.2 CLASSIFICATION #superfamily rat acidic ribosomal protein P1 KEYWORDS phosphoprotein; protein biosynthesis; ribosome SUMMARY #length 114 #molecular-weight 11514 #checksum 2283 SEQUENCE /// ENTRY R5RT12 #type complete TITLE acidic ribosomal protein P1, cytosolic [validated] - rat ALTERNATE_NAMES ribosomal phosphoprotein P1; ribosomal protein RL12eII ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 21-Jul-2000 ACCESSIONS S08022; B48397 REFERENCE S08021 !$#authors Chan, Y.L.; Paz, V.; Wool, I.G. !$#submission submitted to the EMBL Data Library, April 1989 !$#description The primary sequence of rat acidic ribosomal phosphoprotein !1P1. !$#accession S08022 !'##molecule_type mRNA !'##residues 1-114 ##label CHA !'##cross-references EMBL:X15097; NID:g57709; PIDN:CAA33200.1; !1PID:g57710 REFERENCE A48397 !$#authors Wool, I.G.; Chan, Y.L.; Gluck, A.; Suzuki, K. !$#journal Biochimie (1991) 73:861-870 !$#title The primary structure of rat ribosomal proteins P0, P1, and !1P2 and a proposal for a uniform nomenclature for mammalian !1and yeast ribosomal proteins. !$#cross-references MUID:92075759; PMID:1742361 !$#accession B48397 !'##molecule_type mRNA !'##residues 1-114 ##label WOO !'##cross-references GB:X15097; NID:g57709; PIDN:CAA33200.1; PID:g57710 !'##note sequence extracted from NCBI backbone (NCBIN:69676, !1NCBIP:69680) !'##note the protein is designated as ribosomal protein P1 by comparison !1to the composition of ribosomal proteins COMPLEX ribosomal proteins P0, P1, and P2 form a heteropentameric !1subcomplex composed of two P1 chains (PIR:R5RT12), two P2 !1chains (PIR:R6RTP2), and one P0 chain (PIR:R5RT10) !1[validated, MUID:92075759] CLASSIFICATION #superfamily rat acidic ribosomal protein P1 KEYWORDS phosphoprotein; protein biosynthesis; ribosome SUMMARY #length 114 #molecular-weight 11498 #checksum 1818 SEQUENCE /// ENTRY R5CH2E #type complete TITLE acidic ribosomal protein P1 - chicken ALTERNATE_NAMES ribosomal phosphoprotein P1; ribosomal protein CL12eII ORGANISM #formal_name Gallus gallus #common_name chicken DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S02029 REFERENCE S02029 !$#authors Ferro, J.A.; Reinach, F.C. !$#journal Eur. J. Biochem. (1988) 177:513-516 !$#title The complete sequence of a chicken-muscle cDNA encoding the !1acidic ribosomal protein P1. !$#cross-references MUID:89064804; PMID:3197716 !$#accession S02029 !'##molecule_type mRNA !'##residues 1-114 ##label FER !'##cross-references EMBL:X13876; NID:g63063; PIDN:CAA32080.1; !1PID:g63064 !'##note the sequence from Fig. 4 is inconsistent with that from Fig. 1 !1in lacking 96-Glu CLASSIFICATION #superfamily rat acidic ribosomal protein P1 KEYWORDS phosphoprotein; protein biosynthesis; ribosome SUMMARY #length 114 #molecular-weight 11477 #checksum 9481 SEQUENCE /// ENTRY R6SSP2 #type complete TITLE acidic ribosomal protein P1 - brine shrimp ALTERNATE_NAMES ribosomal protein eL12'; ribosomal protein SL12eII ORGANISM #formal_name Artemia salina #common_name brine shrimp DATE 17-Dec-1982 #sequence_revision 31-Mar-1992 #text_change 24-Nov-1999 ACCESSIONS B25208; A02778 REFERENCE A91146 !$#authors Maassen, J.A.; Schop, E.N.; Brands, J.H.G.M.; Van Hemert, !1F.J.; Lenstra, J.A.; Moller, W. !$#journal Eur. J. Biochem. (1985) 149:609-616 !$#title Molecular cloning and analysis of cDNA sequences for two !1ribosomal proteins from Artemia. The coordinate expression !1of genes for ribosomal proteins and elongation factor 1 !1during embryogenesis of Artemia. !$#cross-references MUID:85230659; PMID:3839187 !$#accession B25208 !'##molecule_type mRNA !'##residues 1-107 ##label MAA !'##cross-references GB:X02633; NID:g5688; PIDN:CAA26480.1; PID:g5689 REFERENCE A02778 !$#authors Amons, R.; Pluijms, W.; Kriek, J.; Moller, W. !$#journal FEBS Lett. (1982) 146:143-147 !$#title The primary structure of protein eL12'/eL12'-P from the !1large subunit of Artemia salina ribosomes. !$#accession A02778 !'##molecule_type protein !'##residues 2-8,10-21,'V',22-42,'S',44-110 ##label AMO CLASSIFICATION #superfamily rat acidic ribosomal protein P1 KEYWORDS blocked amino end; phosphoprotein; protein biosynthesis; !1ribosome FEATURE !$2-110 #product acidic ribosomal protein P1 #status !8experimental #label MAT\ !$2 #modified_site blocked amino end (Ala) (in mature !8form) #status experimental\ !$97 #binding_site phosphate (Ser) (covalent) (partial) !8#status experimental SUMMARY #length 110 #molecular-weight 11538 #checksum 6745 SEQUENCE /// ENTRY R5FF2E #type complete TITLE acidic ribosomal protein P1 - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES ribosomal protein A; ribosomal protein DL12eII; ribosomal protein rp21C ORGANISM #formal_name Drosophila melanogaster DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S00659 REFERENCE S00659 !$#authors Wigboldus, J.D. !$#journal Nucleic Acids Res. (1987) 15:10064 !$#title cDNA and deduced amino acid sequence of Drosophila rp21C, !1another 'A'-type ribosomal protein. !$#cross-references MUID:88096510; PMID:3122177 !$#accession S00659 !'##molecule_type mRNA !'##residues 1-112 ##label WIG !'##cross-references EMBL:Y00504; NID:g8475; PIDN:CAA68557.1; PID:g8476 GENETICS !$#gene FlyBase:M(2)21C !'##cross-references FlyBase:FBgn0002593 !$#map_position 21C CLASSIFICATION #superfamily rat acidic ribosomal protein P1 KEYWORDS phosphoprotein; protein biosynthesis; ribosome SUMMARY #length 112 #molecular-weight 11511 #checksum 4768 SEQUENCE /// ENTRY R6KM1C #type complete TITLE acidic ribosomal protein P1, cytosolic - Chlamydomonas reinhardtii ORGANISM #formal_name Chlamydomonas reinhardtii DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 22-Jun-1999 ACCESSIONS S24990 REFERENCE S24989 !$#authors Dumont, F. !$#submission submitted to the EMBL Data Library, May 1992 !$#accession S24990 !'##molecule_type mRNA !'##residues 1-107 ##label DUM !'##cross-references EMBL:X66411; NID:g18210; PIDN:CAA47042.1; !1PID:g18211 CLASSIFICATION #superfamily rat acidic ribosomal protein P1 KEYWORDS phosphoprotein; protein biosynthesis; ribosome SUMMARY #length 107 #molecular-weight 10875 #checksum 3300 SEQUENCE /// ENTRY R5BY2A #type complete TITLE acidic ribosomal protein P1.e.A, cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES acidic ribosomal protein P1.alpha; protein D2450; protein YDL081c; ribosomal protein A1; ribosomal protein YL12eIIA ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1991 #sequence_revision 23-Aug-1996 #text_change 16-Jun-2000 ACCESSIONS S67617; S00678; C35109; D49495 REFERENCE S67608 !$#authors Wambutt, R.; Wedler, H.; Wedler, E.; Scharfe, M. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67617 !'##molecule_type DNA !'##residues 1-106 ##label WAM !'##cross-references EMBL:Z74129; NID:g1431101; PIDN:CAA98647.1; !1PID:g1431102; GSPDB:GN00004; MIPS:YDL081c !'##experimental_source strain S288C REFERENCE S00678 !$#authors Mitsui, K.; Tsurugi, K. !$#journal Nucleic Acids Res. (1988) 16:3574 !$#title cDNA and deduced amino acid sequence of acidic ribosomal !1protein A1 from Saccharomyces cerevisiae. !$#cross-references MUID:88233943; PMID:3287328 !$#accession S00678 !'##molecule_type mRNA !'##residues 1-36,'D',38-106 ##label MIT !'##cross-references EMBL:X06957; NID:g4372; PIDN:CAA30027.1; PID:g4373 !'##experimental_source strain IFO-40028 REFERENCE A35109 !$#authors Newton, C.H.; Shimmin, L.C.; Yee, J.; Dennis, P.P. !$#journal J. Bacteriol. (1990) 172:579-588 !$#title A family of genes encode the multiple forms of the !1Saccharomyces cerevisiae ribosomal proteins equivalent to !1the Escherichia coli L12 protein and a single form of the !1L10-equivalent ribosomal protein. !$#cross-references MUID:90130289; PMID:2404943 !$#accession C35109 !'##molecule_type DNA !'##residues 1-106 ##label NEW !'##cross-references GB:M26504; NID:g171812; PIDN:AAA34733.1; !1PID:g171813 REFERENCE A49495 !$#authors Santos, C.; Ortiz-Reyes, B.; Naranda, T.; Remacha, M.; !1Ballesta, J.P.G. !$#journal Biochemistry (1993) 32:4231-4236 !$#title The acidic phosphoproteins from Saccharomyces cerevisiae !1ribosomes. NH-2-terminal acetylation is a conserved !1difference between P1 and P2 proteins. !$#cross-references MUID:93237229; PMID:8476850 !$#accession D49495 !'##status preliminary !'##molecule_type protein !'##residues 2-5 ##label SAN GENETICS !$#gene SGD:RPLA1; MIPS:YDL081c !'##cross-references SGD:S0002239; MIPS:YDL081c !$#map_position 4L CLASSIFICATION #superfamily rat acidic ribosomal protein P1 KEYWORDS phosphoprotein; protein biosynthesis; ribosome SUMMARY #length 106 #molecular-weight 10908 #checksum 9398 SEQUENCE /// ENTRY R8BY2B #type complete TITLE acidic ribosomal protein P1.e.B, cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES acidic ribosomal protein P1.beta; protein D2203; protein YDL130w; ribosomal protein YL12eIIA; ribosomal protein YL44' ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 21-Jul-2000 ACCESSIONS C28104; D35109; C49495; B49495; S67673 REFERENCE A92726 !$#authors Remacha, M.; Saenz-Robles, M.T.; Vilella, M.D.; Ballesta, !1J.P.G. !$#journal J. Biol. Chem. (1988) 263:9094-9101 !$#title Independent genes coding for three acidic proteins of the !1large ribosomal subunit from Saccharomyces cerevisiae. !$#cross-references MUID:88243786; PMID:2837476 !$#accession C28104 !'##molecule_type DNA !'##residues 1-106 ##label REM !'##cross-references EMBL:M19238; NID:g172399; PIDN:AAA34973.1; !1PID:g172400 REFERENCE A35109 !$#authors Newton, C.H.; Shimmin, L.C.; Yee, J.; Dennis, P.P. !$#journal J. Bacteriol. (1990) 172:579-588 !$#title A family of genes encode the multiple forms of the !1Saccharomyces cerevisiae ribosomal proteins equivalent to !1the Escherichia coli L12 protein and a single form of the !1L10-equivalent ribosomal protein. !$#cross-references MUID:90130289; PMID:2404943 !$#accession D35109 !'##molecule_type DNA !'##residues 1-106 ##label NEW !'##cross-references EMBL:M26507; NID:g171814; PIDN:AAA34734.1; !1PID:g171815 REFERENCE A49495 !$#authors Santos, C.; Ortiz-Reyes, B.; Naranda, T.; Remacha, M.; !1Ballesta, J.P.G. !$#journal Biochemistry (1993) 32:4231-4236 !$#title The acidic phosphoproteins from Saccharomyces cerevisiae !1ribosomes. NH-2-terminal acetylation is a conserved !1difference between P1 and P2 proteins. !$#cross-references MUID:93237229; PMID:8476850 !$#accession C49495 !'##status preliminary !'##molecule_type protein !'##residues 9-16 ##label SAN !$#accession B49495 !'##status preliminary !'##molecule_type protein !'##residues 2-5 ##label SAW REFERENCE S67655 !$#authors Rieger, M.; Mueller-Auer, S.; Brueckner, M.; Schaefer, M.; !1Wagner, G. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67673 !'##molecule_type DNA !'##residues 1-106 ##label RIE !'##cross-references EMBL:Z74178; NID:g1431196; PIDN:CAA98698.1; !1PID:g1431197; GSPDB:GN00004; MIPS:YDL130w !'##experimental_source strain S288C GENETICS !$#gene SGD:RPLA3; RPL44; MIPS:YDL130w !'##cross-references SGD:S0002288; MIPS:YDL130w !$#map_position 4L !$#introns 38/3 CLASSIFICATION #superfamily rat acidic ribosomal protein P1 KEYWORDS phosphoprotein; protein biosynthesis; ribosome SUMMARY #length 106 #molecular-weight 10667 #checksum 7994 SEQUENCE /// ENTRY R6BY11 #type complete TITLE acidic ribosomal protein P1.1 - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES acidic ribosomal protein 1; ribosomal protein YL12eII ORGANISM #formal_name Schizosaccharomyces pombe DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 22-Jun-1999 ACCESSIONS A34715 REFERENCE A34715 !$#authors Beltrame, M.; Bianchi, M.E. !$#journal Mol. Cell. Biol. (1990) 10:2341-2348 !$#title A gene family for acidic ribosomal proteins in !1Schizosaccharomyces pombe: two essential and two !1nonessential genes. !$#cross-references MUID:90220620; PMID:2325655 !$#accession A34715 !'##molecule_type DNA !'##residues 1-109 ##label BEL !'##cross-references EMBL:M33137; NID:g173463; PIDN:AAA35334.1; !1PID:g173464 GENETICS !$#gene rpa1 !$#introns 23/3 CLASSIFICATION #superfamily rat acidic ribosomal protein P1 KEYWORDS phosphoprotein; protein biosynthesis; ribosome SUMMARY #length 109 #molecular-weight 11141 #checksum 9394 SEQUENCE /// ENTRY R6BYP3 #type complete TITLE 60s acidic ribosomal protein p1-alpha - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES acidic ribosomal protein 3; ribosomal protein YL12eII ORGANISM #formal_name Schizosaccharomyces pombe DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 10-Dec-1999 ACCESSIONS C34715; T40352 REFERENCE A34715 !$#authors Beltrame, M.; Bianchi, M.E. !$#journal Mol. Cell. Biol. (1990) 10:2341-2348 !$#title A gene family for acidic ribosomal proteins in !1Schizosaccharomyces pombe: two essential and two !1nonessential genes. !$#cross-references MUID:90220620; PMID:2325655 !$#accession C34715 !'##molecule_type DNA !'##residues 1-110 ##label BEL !'##cross-references EMBL:M33139; NID:g173467; PIDN:AAA35336.1; !1PID:g173468 REFERENCE Z21922 !$#authors Wood, V.; Rajandream, M.A.; Barrell, B.G.; Skelton, J.; !1Churcher, C.M. !$#submission submitted to the EMBL Data Library, March 1997 !$#accession T40352 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-110 ##label WOO !'##cross-references EMBL:AL022070; PIDN:CAA17793.1; GSPDB:GN00067; !1SPDB:SPBC3B9.13c !'##experimental_source strain 972h-; cosmid c3B9 GENETICS !$#gene rpa3 !$#map_position 2 !$#introns 23/3; 103/3 CLASSIFICATION #superfamily rat acidic ribosomal protein P1 KEYWORDS phosphoprotein; protein biosynthesis; ribosome SUMMARY #length 110 #molecular-weight 11171 #checksum 2791 SEQUENCE /// ENTRY R6DOP1 #type complete TITLE acidic ribosomal protein P1 - slime mold (Dictyostelium discoideum) ALTERNATE_NAMES ribosomal phosphoprotein P1 ORGANISM #formal_name Dictyostelium discoideum DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 22-Jun-1999 ACCESSIONS S14013 REFERENCE S14013 !$#authors Prieto, J.; Candel, E.; Coloma, A. !$#journal Nucleic Acids Res. (1991) 19:1340 !$#title Nucleotide sequence of a cDNA encoding ribosomal acidic !1phosphoprotein P1 from Dictyostelium discoideum: !1identification of a novel carboxy-terminal sequence in 'A' !1proteins. !$#cross-references MUID:91232920; PMID:2030950 !$#accession S14013 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type mRNA !'##residues 1-113 ##label PRI !'##cross-references EMBL:X56193; NID:g7338; PIDN:CAA39656.1; PID:g7339 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1990 CLASSIFICATION #superfamily rat acidic ribosomal protein P1 KEYWORDS phosphoprotein; protein biosynthesis; ribosome FEATURE !$70-89 #region alanine-rich SUMMARY #length 113 #molecular-weight 11704 #checksum 533 SEQUENCE /// ENTRY R6UTP1 #type complete TITLE acidic ribosomal protein P1 - Trypanosoma cruzi ORGANISM #formal_name Trypanosoma cruzi DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 22-Jun-1999 ACCESSIONS S22644; S19924 REFERENCE S22644 !$#authors Vazquez, M.P.; Schijman, A.G.; Levin, M.J. !$#journal Nucleic Acids Res. (1992) 20:2599 !$#title Nucleotide sequence of a cDNA encoding a Trypanosoma cruzi !1acidic ribosomal P1 type protein. !$#cross-references MUID:92285148; PMID:1598221 !$#accession S22644 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-109 ##label VAZ !'##cross-references EMBL:X65025; NID:g10629; PIDN:CAA46159.1; !1PID:g10630 CLASSIFICATION #superfamily rat acidic ribosomal protein P1 KEYWORDS phosphoprotein; protein biosynthesis; ribosome SUMMARY #length 109 #molecular-weight 10754 #checksum 9590 SEQUENCE /// ENTRY R6TE1T #type complete TITLE acidic ribosomal protein P1 - Tetrahymena thermophila ALTERNATE_NAMES acidic ribosomal protein TL37 ORGANISM #formal_name Tetrahymena thermophila DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 07-Dec-1999 ACCESSIONS JT0597 REFERENCE JT0597 !$#authors Hansen, T.S.; Andreasen, P.H.; Dreisig, H.; Hojrup, P.; !1Nielsen, H.; Engberg, J.; Kristiansen, K. !$#journal Gene (1991) 105:143-150 !$#title Tetrahymena thermophila acidic ribosomal protein L37 !1contains an archaebacterial type of C-terminus. !$#cross-references MUID:92039025; PMID:1937011 !$#accession JT0597 !'##molecule_type mRNA !'##residues 1-109 ##label HAN !'##cross-references GB:M59428; NID:g161845; PIDN:AAA30126.1; !1PID:g161846 GENETICS !$#genetic_code SGC5 CLASSIFICATION #superfamily rat acidic ribosomal protein P1 KEYWORDS phosphoprotein; protein biosynthesis; ribosome SUMMARY #length 109 #molecular-weight 11652 #checksum 3269 SEQUENCE /// ENTRY R5UC12 #type complete TITLE ribosomal protein L12 - Sulfolobus acidocaldarius ALTERNATE_NAMES ribosomal protein A ORGANISM #formal_name Sulfolobus acidocaldarius DATE 31-Mar-1991 #sequence_revision 05-Feb-1999 #text_change 24-Nov-1999 ACCESSIONS S53651; S11590; S40637; S00558; S29527 REFERENCE S53648 !$#authors Ramirez, C.; Shimmin, L.C.; Leggatt, P.; Matheson, A.T. !$#journal J. Mol. Biol. (1994) 244:242-249 !$#title Structure and transcription of the L11-L1-L10-L12 ribosomal !1protein gene operon from the extreme thermophilic archaeon !1Sulfolobus acidocaldarius. !$#cross-references MUID:95055761; PMID:7966335 !$#accession S53651 !'##molecule_type DNA !'##residues 1-105 ##label RAM1 !'##cross-references EMBL:X59038; NID:g47499; PIDN:CAA41765.1; !1PID:g47503 REFERENCE S11583 !$#authors Ramirez, C.; Shimmin, L.C.; Newton, C.H.; Matheson, A.T.; !1Dennis, P.P. !$#journal Can. J. Microbiol. (1989) 35:234-244 !$#title Structure and evolution of the L11, L1, L10, and L12 !1equivalent ribosomal proteins in eubacteria, archaebacteria, !1and eucaryotes. !$#cross-references MUID:89248688; PMID:2497941 !$#accession S11590 !'##molecule_type DNA !'##residues 1-105 ##label RAM2 !'##note the symbols for alanine (A) and arginine (R) are !1undistinguishable in the published sequence; they have been !1assigned according to reference S29524 REFERENCE S40637 !$#authors Koepke, A.K.E.; Leggatt, P.A. !$#journal Nucleic Acids Res. (1991) 19:5169-5172 !$#title Initiation of translation at an AUA codon for an !1archaebacterial protein gene expressed in E.coli. !$#cross-references MUID:92020200; PMID:1923803 !$#accession S40637 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-42 ##label KOE REFERENCE S00558 !$#authors Matheson, A.T.; Louie, K.A.; Boeck, A. !$#journal FEBS Lett. (1988) 231:331-335 !$#title The complete amino acid sequence of the ribosomal A protein !1(L12) from the archaebacterium Sulfolobus acidocaldarius. !$#accession S00558 !'##molecule_type protein !'##residues 1-45,'E',47-105 ##label MAT !'##note the sequence from Fig. 1 is inconsistent with that from Fig. 3 !1in having an additional Ala after 67-Ala COMMENT This protein complexes with ribosomal protein L10 in a 4:1 !1ratio and forms a well-defined domain of the large ribosomal !1subunit. CLASSIFICATION #superfamily rat acidic ribosomal protein P1 KEYWORDS blocked amino end; protein biosynthesis; ribosome FEATURE !$1 #modified_site blocked amino end (Met) #status !8experimental SUMMARY #length 105 #molecular-weight 11138 #checksum 9226 SEQUENCE /// ENTRY R6MXL2 #type complete TITLE ribosomal protein L12 - Methanococcus vannielii ORGANISM #formal_name Methanococcus vannielii DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 22-Jun-1999 ACCESSIONS B28152; A28152 REFERENCE A28152 !$#authors Strobel, O.; Koepke, A.K.E.; Kamp, R.M.; Boeck, A.; !1Wittmann-Liebold, B. !$#journal J. Biol. Chem. (1988) 263:6538-6546 !$#title Primary structure of the archaebacterial Methanococcus !1vannielii ribosomal protein L12. Amino acid sequence !1determination, oligonucleotide hybridization, and sequencing !1of the gene. !$#cross-references MUID:88198213; PMID:2834382 !$#accession B28152 !'##molecule_type DNA !'##residues 1-99 ##label ST1 !'##cross-references GB:J03187; NID:g150067; PIDN:AAA72191.1; !1PID:g150068 !$#accession A28152 !'##molecule_type protein !'##residues 1-99 ##label ST2 CLASSIFICATION #superfamily rat acidic ribosomal protein P1 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 99 #molecular-weight 9818 #checksum 4258 SEQUENCE /// ENTRY R5HS12 #type complete TITLE ribosomal protein L12 [similarity] - Haloarcula marismortui ORGANISM #formal_name Haloarcula marismortui DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 21-Jul-2000 ACCESSIONS S08423 REFERENCE S08420 !$#authors Arndt, E.; Weigel, C. !$#journal Nucleic Acids Res. (1990) 18:1285 !$#title Nucleotide sequence of the genes encoding the L11, L1, L10 !1and L12 equivalent ribosomal proteins from the !1archaebacterium Halobacterium marismortui. !$#cross-references MUID:90206791; PMID:2320419 !$#accession S08423 !'##status translation not shown !'##molecule_type DNA !'##residues 1-115 ##label ARN !'##cross-references EMBL:X51430; NID:g43602; PIDN:CAA35796.1; !1PID:g43606 !'##note the source is designated as Halobacterium marismortui CLASSIFICATION #superfamily rat acidic ribosomal protein P1 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 115 #molecular-weight 11773 #checksum 6545 SEQUENCE /// ENTRY R5HS2H #type complete TITLE ribosomal protein L12 [validated] - Halobacterium salinarum ALTERNATE_NAMES ribosomal protein A; ribosomal protein HL20 ORGANISM #formal_name Halobacterium salinarum DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 21-Jul-2000 ACCESSIONS S01745; A37527; S04121; S08560; S01316; S11589 REFERENCE S01745 !$#authors Itoh, T.; Kumazaki, T.; Sugiyama, M.; Otaka, E. !$#journal Biochim. Biophys. Acta (1988) 949:110-118 !$#title Molecular cloning and sequence analysis of the ribosomal 'A' !1protein gene from the archaebacterium, Halobacterium !1halobium. !$#accession S01745 !'##molecule_type DNA !'##residues 1-114 ##label ITO !'##cross-references EMBL:X06736; NID:g43547; PIDN:CAA29915.1; !1PID:g43548 !'##experimental_source strain S9 !$#accession A37527 !'##molecule_type protein !'##residues 1-114 ##label ITO2 !'##experimental_source strain S9 !'##note the source is designated as Halobacterium halobium !'##note the protein is designated ribosomal 'A' protein REFERENCE S04116 !$#authors Shimmin, L.C.; Dennis, P.P. !$#journal EMBO J. (1989) 8:1225-1235 !$#title Characterization of the L11, L1, L10 and L12 equivalent !1ribosomal protein gene cluster of the halophilic !1archaebacterium Halobacterium cutirubrum. !$#cross-references MUID:89305527; PMID:2743981 !$#accession S04121 !'##molecule_type DNA !'##residues 1-114 ##label SHI !'##cross-references EMBL:X15078; NID:g43449; PIDN:CAA33181.1; !1PID:g43455 !'##note the source is designated as Halobacterium cutirubrum REFERENCE S07437 !$#authors Matheson, A.T.; Yaguchi, M.; Christensen, P.; Rollin, C.F.; !1Hasnain, S. !$#journal Can. J. Biochem. Cell Biol. (1984) 62:426-433 !$#title Purification, properties, and N-terminal amino acid sequence !1of certain 50S ribosomal subunit proteins from the !1archaebacterium Halobacterium cutirubrum. !$#cross-references MUID:84282108; PMID:6467081 !$#accession S08560 !'##molecule_type protein !'##residues 1-76 ##label MAT1 !'##note the source is designated as Halobacterium cutirubrum !'##note the protein is designated as ribosomal protein L20 CLASSIFICATION #superfamily rat acidic ribosomal protein P1 KEYWORDS protein biosynthesis; ribosome FEATURE !$1-114 #product ribosomal protein L12 #status experimental !8#label MAT SUMMARY #length 114 #molecular-weight 11562 #checksum 5678 SEQUENCE /// ENTRY R6RT37 #type complete TITLE ribosomal protein L37, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 25-Feb-1985 #sequence_revision 21-Jul-2000 #text_change 21-Jul-2000 ACCESSIONS JN0478; PN0455; S21496; A02779; S11421 REFERENCE JN0478 !$#authors Chan, Y.L.; Paz, V.; Olvera, J.; Wool, I.G. !$#journal Biochem. Biophys. Res. Commun. (1993) 192:590-596 !$#title The primary structure of L37 - a rat ribosomal protein with !1a zinc finger-like motif. !$#cross-references MUID:93249430; PMID:8484768 !$#accession JN0478 !'##molecule_type mRNA !'##residues 1-97 ##label CHA !$#accession PN0455 !'##molecule_type protein !'##residues 2-40 ##label CH1 !'##note the protein is designated as ribosomal protein L37 REFERENCE S21496 !$#authors Chan, Y.L.; Paz, V.; Olvera, J.; Wool, I.G. !$#submission submitted to the EMBL Data Library, May 1992 !$#description The primary structure of rat ribosomal protein S9. !$#accession S21496 !'##molecule_type mRNA !'##residues 1-95 ##label CHW !'##cross-references EMBL:X66369 REFERENCE A02779 !$#authors Lin, A.; McNally, J.; Wool, I.G. !$#journal J. Biol. Chem. (1983) 258:10664-10671 !$#title The primary structure of rat liver ribosomal protein L37. !1Homology with yeast and bacterial ribosomal proteins. !$#cross-references MUID:83291000; PMID:6350292 !$#accession A02779 !'##molecule_type protein !'##residues 'N',3-18,'G',20-21,'KSKGKGALQKGYNSFPGKL',22-25,26-30, !1'SKKYNTLHAWKRTTGM',40-42,'C',44-94,'A' ##label LIN !'##note the protein is designated as ribosomal protein L37 REFERENCE S11413 !$#authors Wittmann-Liebold, B.; Geissler, A.W.; Lin, A.; Wool, I.G. !$#journal J. Supramol. Struct. (1979) 12:425-433 !$#title Sequence of the amino-terminal region of rat liver ribosomal !1proteins S4, S6, S8, L6, L7a, L18, L27, L30, L37, L37a, and !1L39. !$#cross-references MUID:80252792; PMID:398910 !$#accession S11421 !'##molecule_type protein !'##residues 'X',3-18,'G',20-21,'KXKGKGA',29-31 ##label WIT !'##note the protein is designated as ribosomal protein L37 CLASSIFICATION #superfamily rat ribosomal protein L37 KEYWORDS cytosol; protein biosynthesis; ribosome; zinc finger FEATURE !$2-97 #product ribosomal protein L37 #status experimental !8#label RPL\ !$19-37 #region zinc finger CCCC motif SUMMARY #length 97 #molecular-weight 11078 #checksum 234 SEQUENCE /// ENTRY R6RT39 #type complete TITLE ribosomal protein L39, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 25-Feb-1985 #sequence_revision 02-Jul-1996 #text_change 21-Jul-2000 ACCESSIONS JC4229; PC4065; A02780; S11423; S49573 REFERENCE JC4228 !$#authors Chan, Y.L.; Olvera, J.; Wool, I.G. !$#journal Biochem. Biophys. Res. Commun. (1995) 213:1042-1050 !$#title The primary structures of rat ribosomal proteins: the !1characterization of the cDNAs for S21 and L39, corrections !1in the sequences of L7 and L18a, and the identification of !1L33. !$#cross-references MUID:95382802; PMID:7654221 !$#accession JC4229 !'##molecule_type mRNA !'##residues 1-51 ##label CHA !'##cross-references EMBL:X82551; NID:g575381; PIDN:CAA57900.1; !1PID:g575382 !$#accession PC4065 !'##molecule_type protein !'##residues 25-34 ##label CH2 !'##experimental_source liver !'##note the protein is designated as ribosomal protein L39 REFERENCE A02780 !$#authors Lin, A.; McNally, J.; Wool, I.G. !$#journal J. Biol. Chem. (1984) 259:487-490 !$#title The primary structure of rat liver ribosomal protein L39. !$#cross-references MUID:84161954; PMID:6706949 !$#accession A02780 !'##molecule_type protein !'##residues 2-51 ##label LIN !'##note the protein is designated as ribosomal protein L39 REFERENCE S11413 !$#authors Wittmann-Liebold, B.; Geissler, A.W.; Lin, A.; Wool, I.G. !$#journal J. Supramol. Struct. (1979) 12:425-433 !$#title Sequence of the amino-terminal region of rat liver ribosomal !1proteins S4, S6, S8, L6, L7a, L18, L27, L30, L37, L37a, and !1L39. !$#cross-references MUID:80252792; PMID:398910 !$#accession S11423 !'##molecule_type protein !'##residues 2-19 ##label WIT !'##note the protein is designated as ribosomal protein L39 CLASSIFICATION #superfamily rat ribosomal protein L39 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-51 #product ribosomal protein L39 #status experimental !8#label MAT SUMMARY #length 51 #molecular-weight 6407 #checksum 4012 SEQUENCE /// ENTRY R6BY46 #type complete TITLE ribosomal protein L39.e, cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein J0360; protein YJL189w; ribosomal protein YL46 ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 21-Jul-2000 ACCESSIONS B23082; S56972 REFERENCE A93593 !$#authors Leer, R.J.; van Raamsdonk-Duin, M.M.C.; Kraakman, P.; Mager, !1W.H.; Planta, R.J. !$#journal Nucleic Acids Res. (1985) 13:701-709 !$#title The genes for yeast ribosomal proteins S24 and L46 are !1adjacent and divergently transcribed. !$#cross-references MUID:85215509; PMID:4000930 !$#accession B23082 !'##molecule_type DNA !'##residues 1-51 ##label LEE REFERENCE S56937 !$#authors Obermaier, B.; Piravandi, E.; Rinke, M.; Domdey, H. !$#submission submitted to the Protein Sequence Database, September 1995 !$#accession S56972 !'##molecule_type DNA !'##residues 1-51 ##label OBE !'##cross-references EMBL:Z49464; NID:g1008396; PIDN:CAA89483.1; !1PID:g1008397; GSPDB:GN00010; MIPS:YJL189w GENETICS !$#gene SGD:RPL46; MIPS:YJL189w !'##cross-references SGD:S0003725; MIPS:YJL189w !$#map_position 10L !$#introns 2/3 CLASSIFICATION #superfamily rat ribosomal protein L39 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 51 #molecular-weight 6342 #checksum 4334 SEQUENCE /// ENTRY R6UC46 #type complete TITLE ribosomal protein L39.eR - Sulfolobus solfataricus ALTERNATE_NAMES ribosomal protein SL46 ORGANISM #formal_name Sulfolobus solfataricus DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 22-Jun-1999 ACCESSIONS S05009; A37529 REFERENCE S05009 !$#authors Ramirez, C.; Louie, K.A.; Matheson, A.T. !$#journal FEBS Lett. (1989) 250:416-418 !$#title A small basic ribosomal protein in Sulfolobus solfataricus !1equivalent to L46 in yeast: structure of the protein and its !1gene. !$#cross-references MUID:89325607; PMID:2502431 !$#accession S05009 !'##molecule_type DNA !'##residues 1-51 ##label RAM !'##cross-references EMBL:X16161; NID:g47611; PIDN:CAA34287.1; !1PID:g47612 !$#accession A37529 !'##molecule_type protein !'##residues 1-51 ##label RAM2 CLASSIFICATION #superfamily rat ribosomal protein L39 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-51 #product ribosomal protein L39.eR #status !8experimental #label MAT SUMMARY #length 51 #molecular-weight 6063 #checksum 3231 SEQUENCE /// ENTRY R6HS39 #type complete TITLE ribosomal protein L39.eR [validated] - Haloarcula marismortui ALTERNATE_NAMES ribosomal protein HL46 ORGANISM #formal_name Haloarcula marismortui DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 04-Feb-2000 ACCESSIONS S13066; A38032 REFERENCE S13066 !$#authors Bergmann, U.; Arndt, E. !$#journal Biochim. Biophys. Acta (1990) 1050:56-60 !$#title Evidence for an additional archaebacterial gene cluster in !1Halobacterium marismortui encoding ribosomal proteins HL46e !1and HL30. !$#cross-references MUID:91002676; PMID:2207169 !$#accession S13066 !'##molecule_type DNA !'##residues 1-50 ##label BER !'##cross-references EMBL:X55007; NID:g43599; PIDN:CAA38750.1; !1PID:g43600 !$#accession A38032 !'##molecule_type protein !'##residues 2-24,'X',26-50 ##label BER1 !'##note the source is designated as Halobacterium marismortui !'##note the protein is designated as ribosomal protein HL46 CLASSIFICATION #superfamily rat ribosomal protein L39 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-50 #product ribosomal protein L39.eR #status !8experimental #label MAT SUMMARY #length 50 #molecular-weight 6115 #checksum 8921 SEQUENCE /// ENTRY R6HU36 #type complete TITLE ribosomal protein L36a - human ALTERNATE_NAMES ribosomal protein HL44 ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 22-Jun-1999 ACCESSIONS A25560 REFERENCE A25560 !$#authors Davies, M.S.; Henney, A.; Ward, W.H.J.; Craig, R.K. !$#journal Gene (1986) 45:183-191 !$#title Characterisation of an mRNA encoding a human ribosomal !1protein homologous to the yeast L44 ribosomal protein. !$#cross-references MUID:87106812; PMID:3542712 !$#accession A25560 !'##molecule_type mRNA !'##residues 1-106 ##label DAV !'##cross-references EMBL:M15661; NID:g337577; PIDN:AAA36589.1; !1PID:g337578 !'##note the authors translated the codon GGC for residue 29 as Glu GENETICS !$#gene GDB:RPL36A !'##cross-references GDB:128850; OMIM:180469 !$#map_position 14pter-14qter CLASSIFICATION #superfamily rat ribosomal protein L36a KEYWORDS protein biosynthesis; ribosome FEATURE !$2-106 #product ribosomal protein L36a #status predicted !8#label MAT SUMMARY #length 106 #molecular-weight 12469 #checksum 454 SEQUENCE /// ENTRY R6RT36 #type complete TITLE ribosomal protein L36a, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 21-Jul-2000 ACCESSIONS A29820; A34987 REFERENCE A29820 !$#authors Gallagher, M.J.; Chan, Y.L.; Lin, A.; Wool, I.G. !$#journal DNA (1988) 7:269-273 !$#title Primary structure of rat ribosomal protein L36a. !$#cross-references MUID:88283346; PMID:3396452 !$#accession A29820 !'##molecule_type mRNA !'##residues 1-106 ##label GAL !'##cross-references EMBL:M19635; NID:g206731; PIDN:AAB54277.1; !1PID:g206732 !$#accession A34987 !'##molecule_type protein !'##residues 2-6,'X',8-9,'X',11 ##label GAL2 !'##note the protein is designated as ribosomal protein L36a CLASSIFICATION #superfamily rat ribosomal protein L36a KEYWORDS protein biosynthesis; ribosome FEATURE !$2-106 #product ribosomal protein L36a #status experimental !8#label MAT SUMMARY #length 106 #molecular-weight 12441 #checksum 188 SEQUENCE /// ENTRY R6BY44 #type complete TITLE ribosomal protein L36a.e.c8, cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YHR141c; ribosomal protein 44; ribosomal protein YL41 ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-May-1979 #sequence_revision 12-May-1995 #text_change 23-Mar-2001 ACCESSIONS C43301; S48985; A02781 REFERENCE A43301 !$#authors Kawai, S.; Murao, S.; Mochizuki, M.; Shibuya, I.; Yano, K.; !1Takagi, M. !$#journal J. Bacteriol. (1992) 174:254-262 !$#title Drastic alteration of cycloheximide sensitivity by !1substitution of one amino acid in the L41 ribosomal protein !1of yeasts. !$#cross-references MUID:92104971; PMID:1729213 !$#accession C43301 !'##molecule_type DNA !'##residues 1-106 ##label KAW !'##cross-references EMBL:D10579; NID:g218483; PIDN:BAA01436.1; !1PID:g218484 !'##note sequence extracted from NCBI backbone (NCBIN:75362, !1NCBIP:75363) REFERENCE S48967 !$#authors Fulton, L. !$#submission submitted to the EMBL Data Library, June 1994 !$#description The sequence of S. cerevisiae cosmid 9315. !$#accession S48985 !'##molecule_type DNA !'##residues 1-106 ##label FUL !'##cross-references EMBL:U10398; NID:g551328; PIDN:AAB68420.1; !1PID:g500688; GSPDB:GN00008; MIPS:YHR141c REFERENCE A02781 !$#authors Itoh, T.; Wittmann-Liebold, B. !$#journal FEBS Lett. (1978) 96:399-402 !$#title The primary structure of protein 44 from the large subunit !1of yeast ribosomes. !$#cross-references MUID:79086263; PMID:365584 !$#accession A02781 !'##molecule_type protein !'##residues 2-39,'RK',42-87,90-106 ##label ITO !'##note the residues at positions 40 and 54 were not positively !1identified but are chemically related to monomethyllysine GENETICS !$#gene SGD:MAK18; MIPS:YHR141c !'##cross-references SGD:S0001183; MIPS:YHR141c !$#map_position 8R !$#introns 2/1 FUNCTION !$#description protein biosynthesis CLASSIFICATION #superfamily rat ribosomal protein L36a KEYWORDS methylated amino acid; protein biosynthesis; ribosome FEATURE !$2-106 #product ribosomal protein L36a.e #status !8experimental #label MAT\ !$40,55 #modified_site lysine derivative (Lys) (probably !8N6-methyllysine) #status experimental SUMMARY #length 106 #molecular-weight 12212 #checksum 9122 SEQUENCE /// ENTRY R6UT6A #type complete TITLE ribosomal protein L36a.e - Trypanosoma brucei ALTERNATE_NAMES ribosomal protein TL44 ORGANISM #formal_name Trypanosoma brucei DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 22-Jun-1999 ACCESSIONS S10012 REFERENCE S10012 !$#authors Tebabi, P.; Halleux, S.; Pays, E. !$#journal Nucleic Acids Res. (1990) 18:2809 !$#title Nucleotide sequence of a full-length cDNA coding for the !1ribosomal L44 protein of Trypanosoma brucei. !$#cross-references MUID:90251460; PMID:2339065 !$#accession S10012 !'##molecule_type mRNA !'##residues 1-106 ##label TEB !'##cross-references EMBL:X52122; NID:g10525; PIDN:CAA36367.1; !1PID:g10526 CLASSIFICATION #superfamily rat ribosomal protein L36a KEYWORDS protein biosynthesis; ribosome FEATURE !$2-106 #product ribosomal protein L36a.e #status predicted !8#label MAT SUMMARY #length 106 #molecular-weight 12454 #checksum 1379 SEQUENCE /// ENTRY S33790 #type complete TITLE ribosomal protein L36a.eR [validated] - Haloarcula marismortui ALTERNATE_NAMES ribosomal protein HLA ORGANISM #formal_name Haloarcula marismortui DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 22-Oct-2001 ACCESSIONS S33790 REFERENCE S33789 !$#authors Bergmann, U.; Wittmann-Liebold, B. !$#journal Biochim. Biophys. Acta (1993) 1173:195-200 !$#title HL35e and HLA: primary structure of two very basic and !1cysteine-rich ribosomal proteins from Haloarcula !1marismortui. !$#cross-references MUID:93277953; PMID:8504167 !$#accession S33790 !'##molecule_type protein !'##residues 1-92 ##label BER CLASSIFICATION #superfamily rat ribosomal protein L36a KEYWORDS protein biosynthesis; ribosome SUMMARY #length 92 #molecular-weight 10791 #checksum 3212 SEQUENCE /// ENTRY D69416 #type complete TITLE ribosomal protein L36a.eR [similarity] - Archaeoglobus fulgidus ALTERNATE_NAMES ribosomal protein L44E ORGANISM #formal_name Archaeoglobus fulgidus DATE 05-Dec-1997 #sequence_revision 05-Dec-1997 #text_change 22-Oct-2001 ACCESSIONS D69416 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession D69416 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-93 ##label KLE !'##cross-references GB:AE001011; GB:AE000782; NID:g2689334; !1PIDN:AAB89909.1; PID:g2649238; TIGR:AF1333 CLASSIFICATION #superfamily rat ribosomal protein L36a KEYWORDS protein biosynthesis; ribosome SUMMARY #length 93 #molecular-weight 11038 #checksum 7897 SEQUENCE /// ENTRY B64331 #type complete TITLE ribosomal protein L36a.eR [similarity] - Methanococcus jannaschii ALTERNATE_NAMES ribosomal protein ML44 ORGANISM #formal_name Methanococcus jannaschii DATE 13-Sep-1996 #sequence_revision 13-Sep-1996 #text_change 22-Oct-2001 ACCESSIONS B64331 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession B64331 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-94 ##label BUL !'##cross-references GB:U67480; GB:L77117; NID:g2826265; !1PIDN:AAB98236.1; PID:g1499028; TIGR:MJ0249 GENETICS !$#map_position FOR235632-235916 CLASSIFICATION #superfamily rat ribosomal protein L36a KEYWORDS protein biosynthesis; ribosome SUMMARY #length 94 #molecular-weight 11029 #checksum 9695 SEQUENCE /// ENTRY B69041 #type complete TITLE ribosomal protein L36a.eR [similarity] - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 05-Dec-1997 #sequence_revision 05-Dec-1997 #text_change 22-Oct-2001 ACCESSIONS B69041 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession B69041 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-92 ##label MTH !'##cross-references GB:AE000895; GB:AE000666; NID:g2622403; !1PIDN:AAB85788.1; PID:g2622415 !'##experimental_source strain Delta H GENETICS !$#gene MTH1310 CLASSIFICATION #superfamily rat ribosomal protein L36a KEYWORDS protein biosynthesis; ribosome SUMMARY #length 92 #molecular-weight 10882 #checksum 7180 SEQUENCE /// ENTRY D71209 #type complete TITLE ribosomal protein L36a.eR [similarity] - Pyrococcus horikoshii ALTERNATE_NAMES ribosomal protein L44 ORGANISM #formal_name Pyrococcus horikoshii DATE 14-Aug-1998 #sequence_revision 14-Aug-1998 #text_change 22-Oct-2001 ACCESSIONS D71209 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession D71209 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-109 ##label KAW !'##cross-references GB:AP000007; NID:g3236134; PIDN:BAA31067.1; !1PID:g3258384 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1940 CLASSIFICATION #superfamily rat ribosomal protein L36a KEYWORDS protein biosynthesis; ribosome SUMMARY #length 109 #molecular-weight 12899 #checksum 4160 SEQUENCE /// ENTRY F75022 #type complete TITLE ribosomal protein L36a.eR [similarity] - Pyrococcus abyssi (strain Orsay) ALTERNATE_NAMES ribosomal protein l44e PAB1221 ORGANISM #formal_name Pyrococcus abyssi DATE 20-Aug-1999 #sequence_revision 20-Aug-1999 #text_change 22-Oct-2001 ACCESSIONS F75022 REFERENCE A75001 !$#authors anonymous, Genoscope !$#submission submitted to the EMBL Data Library, July 1999 !$#description Pyrococcus abyssi genome sequence: insights into archaeal !1chromosome structure and evolution. !$#accession F75022 !'##molecule_type DNA !'##residues 1-94 ##label KAW !'##cross-references GB:AJ248288; GB:AL096836; NID:g5458960; !1PIDN:CAB50620.1; PID:g5459134 !'##experimental_source strain Orsay GENETICS !$#gene PAB1221 CLASSIFICATION #superfamily rat ribosomal protein L36a KEYWORDS protein biosynthesis; ribosome SUMMARY #length 94 #molecular-weight 11241 #checksum 306 SEQUENCE /// ENTRY A90257 #type complete TITLE ribosomal protein L36a.eR [similarity] - Sulfolobus solfataricus ALTERNATE_NAMES ribosomal protein L44E ORGANISM #formal_name Sulfolobus solfataricus DATE 24-May-2001 #sequence_revision 24-May-2001 #text_change 22-Oct-2001 ACCESSIONS A90257 REFERENCE A99139 !$#authors She, Q.; Singh, R.K.; Confalonieri, F.; Zivanovic, Y.; !1Allard, G.; Awayez, M.J.; Chan-Weiher, C.C.Y.; Clausen, !1I.G.; Curtis, B.A.; De Moors, A.; Erauso, G.; Fletcher, C.; !1Gordon, P.M.K.; Heikamp-de Jong, I.; Jeffries, A.C.; Kozera, !1C.J.; Medina, N.; Peng, X.; Thi-Ngoc, H.P.; Redder, P.; !1Schenk, M.E.; Theriault, C.; Tolstrup, N.; Charlebois, R.L.; !1Doolittle, W.F.; Duguet, M.; Gaasterland, T.; Garrett, R.A.; !1Ragan, M.A.; Sensen, C.W.; Van der Oost, J. !$#submission submitted to GenBank, April 2001 !$#description Sulfolobus solfataricus complete genome. !$#accession A90257 !'##molecule_type DNA !'##residues 1-95 ##label KUR !'##cross-references GB:AE006641; NID:g13814234; PIDN:AAK41312.1; !1GSPDB:GN00155 GENETICS !$#gene rpl44E CLASSIFICATION #superfamily rat ribosomal protein L36a KEYWORDS protein biosynthesis; ribosome SUMMARY #length 95 #molecular-weight 10986 #checksum 4955 SEQUENCE /// ENTRY R5RTLA #type complete TITLE ribosomal protein L27a, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 21-Jul-2000 ACCESSIONS S13071; A30447; S11392 REFERENCE S13071 !$#authors Wool, I.G.; Chan, Y.L.; Paz, V.; Olvera, J. !$#journal Biochim. Biophys. Acta (1990) 1050:69-73 !$#title The primary structure of rat ribosomal proteins: the amino !1acid sequences of L27a and L28 and corrections in the !1sequences of S4 and S12. !$#cross-references MUID:91002678; PMID:2207170 !$#accession S13071 !'##molecule_type mRNA !'##residues 1-148 ##label WOO !'##cross-references EMBL:X52733; NID:g57695; PIDN:CAA36947.1; !1PID:g57696 !$#accession A30447 !'##molecule_type protein !'##residues 2-16 ##label WO2 !'##note the protein is designated as ribosomal protein L27a CLASSIFICATION #superfamily rat ribosomal protein L27a KEYWORDS protein biosynthesis; ribosome; zinc finger FEATURE !$2-148 #product ribosomal protein L27a #status experimental !8#label MAT SUMMARY #length 148 #molecular-weight 16618 #checksum 7701 SEQUENCE /// ENTRY R5MS27 #type complete TITLE ribosomal protein L27a - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S11557 REFERENCE S11557 !$#authors Belhumeur, P.; Paterno, G.D.; Boileau, G.; Claverie, J.M.; !1Skup, D. !$#journal Nucleic Acids Res. (1987) 15:1019-1029 !$#title Isolation and characterisation of a murine cDNA clone highly !1homologous to the yeast L29 ribosomal protein gene. !$#cross-references MUID:87146413; PMID:2434927 !$#accession S11557 !'##molecule_type mRNA !'##residues 1-148 ##label BEL !'##cross-references EMBL:X05021; NID:g50320; PIDN:CAA28678.1; !1PID:g50321 CLASSIFICATION #superfamily rat ribosomal protein L27a KEYWORDS protein biosynthesis; ribosome SUMMARY #length 148 #molecular-weight 16619 #checksum 8373 SEQUENCE /// ENTRY R6BY29 #type complete TITLE ribosomal protein L27a.e, cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein G3101; protein YGL103w; ribosomal protein YL29 ORGANISM #formal_name Saccharomyces cerevisiae DATE 25-Feb-1985 #sequence_revision 30-Jun-1992 #text_change 21-Jul-2000 ACCESSIONS A02782; S45696; S64110 REFERENCE A02782 !$#authors Kaeufer, N.F.; Fried, H.M.; Schwindinger, W.F.; Jasin, M.; !1Warner, J.R. !$#journal Nucleic Acids Res. (1983) 11:3123-3135 !$#title Cycloheximide resistance in yeast: the gene and its protein. !$#cross-references MUID:83220732; PMID:6304624 !$#accession A02782 !'##molecule_type DNA !'##residues 1-149 ##label KAU !'##cross-references EMBL:X01573; NID:g3619; PIDN:CAA25729.1; PID:g3620 !'##note a mutation resulting in the replacement of Gln by Glu at !1position 38 confers resistance to cycloheximide REFERENCE S45696 !$#authors Schwindinger, W.F.; Warner, J.R. !$#journal J. Biol. Chem. (1987) 262:5690-5695 !$#title Transcriptional elements of the yeast ribosomal protein gene !1CYH2. !$#cross-references MUID:87194763; PMID:3553182 !$#accession S45696 !'##molecule_type DNA !'##residues 1-16 ##label SCH !'##cross-references EMBL:M19490; NID:g172481; PIDN:AAA35002.1; !1PID:g553140 REFERENCE S64071 !$#authors Rieger, M.; Mueller-Auer, S.; Brueckner, M.; Schaefer, M. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64110 !'##molecule_type DNA !'##residues 1-149 ##label RIE !'##cross-references EMBL:Z72625; NID:g1322642; PIDN:CAA96808.1; !1PID:g1322643; GSPDB:GN00007; MIPS:YGL103w !'##experimental_source strain S288C GENETICS !$#gene SGD:CYH2; RPL29; MIPS:YGL103w !'##cross-references SGD:S0003071; MIPS:YGL103w !$#map_position 7L !$#introns 17/1 CLASSIFICATION #superfamily rat ribosomal protein L27a KEYWORDS protein biosynthesis; ribosome FEATURE !$2-149 #product ribosomal protein L27a.e #status !8experimental #label MAT SUMMARY #length 149 #molecular-weight 16722 #checksum 6502 SEQUENCE /// ENTRY R6NC7A #type complete TITLE ribosomal protein L27a.e - Neurospora crassa ALTERNATE_NAMES ribosomal protein NL29 ORGANISM #formal_name Neurospora crassa DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 24-Sep-1999 ACCESSIONS S01744; A37526 REFERENCE S01744 !$#authors Kreader, C.A.; Heckman, J.E. !$#journal Nucleic Acids Res. (1987) 15:9027-9042 !$#title Isolation and characterization of a Neurospora crassa !1ribosomal protein gene homologous to CYH2 of yeast. !$#cross-references MUID:88067712; PMID:2960953 !$#accession S01744 !'##molecule_type DNA !'##residues 1-149 ##label KRE !'##cross-references EMBL:X06320; NID:g2990; PIDN:CAA29635.1; PID:g2991 !$#accession A37526 !'##molecule_type mRNA !'##residues 1-149 ##label KRE2 !'##cross-references GB:X06320; NID:g2990; PIDN:CAA29635.1; PID:g2991 GENETICS !$#gene crp-1 !$#introns 1/3; 14/3; 20/2; 30/2; 38/3; 48/1; 116/1 CLASSIFICATION #superfamily rat ribosomal protein L27a KEYWORDS protein biosynthesis; ribosome SUMMARY #length 149 #molecular-weight 16597 #checksum 7724 SEQUENCE /// ENTRY R6MX15 #type complete TITLE ribosomal protein L15 - Methanococcus vannielii ORGANISM #formal_name Methanococcus vannielii DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 22-Jun-1999 ACCESSIONS S05626 REFERENCE S05611 !$#authors Auer, J.; Spicker, G.; Boeck, A. !$#journal J. Mol. Biol. (1989) 209:21-36 !$#title Organization and structure of the Methanococcus !1transcriptional unit homologous to the Escherichia coli !1"spectinomycin operon". Implications for the evolutionary !1relationship of 70 S and 80 S ribosomes. !$#cross-references MUID:90040717; PMID:2530355 !$#accession S05626 !'##molecule_type DNA !'##residues 1-143 ##label AUE !'##cross-references EMBL:X16720; NID:g44754; PIDN:CAA34702.1; !1PID:g44770 CLASSIFICATION #superfamily rat ribosomal protein L27a KEYWORDS protein biosynthesis; ribosome SUMMARY #length 143 #molecular-weight 15950 #checksum 9917 SEQUENCE /// ENTRY R6HS15 #type complete TITLE ribosomal protein L15 [validated] - Haloarcula marismortui ALTERNATE_NAMES ribosomal protein HL7; ribosomal protein HL9 ORGANISM #formal_name Haloarcula marismortui DATE 31-Mar-1991 #sequence_revision 12-Apr-1996 #text_change 21-Jul-2000 ACCESSIONS S22349; S06844; S16544; C28949; T46809 REFERENCE S22349 !$#authors Arndt, E. !$#journal Biochim. Biophys. Acta (1992) 1130:113-116 !$#title The genes for ribosomal protein L15 and the protein !1equivalent to secY in the archaebacterium Haloarcula !1(Halobacterium) marismortui. !$#cross-references MUID:92182004; PMID:1543743 !$#accession S22349 !'##status preliminary !'##molecule_type DNA !'##residues 1-165 ##label ARN !'##cross-references EMBL:X63127; NID:g43607; PIDN:CAA44837.1; !1PID:g43608 REFERENCE S06844 !$#authors Hatakeyama, T.; Kaufmann, F.; Schroeter, B.; Hatakeyama, T. !$#journal Eur. J. Biochem. (1989) 185:685-693 !$#title Primary structures of five ribosomal proteins from the !1archaebacterium Halobacterium marismortui and their !1structural relationships to eubacterial and eukaryotic !1ribosomal proteins. !$#cross-references MUID:90076190; PMID:2591382 !$#accession S06844 !'##molecule_type protein !'##residues 2-155 ##label HAT !'##note the source is designated as Halobacterium marismortui !'##note the protein is designated as ribosomal protein HL9 REFERENCE S16535 !$#authors Scholzen, T.; Arndt, E. !$#journal Mol. Gen. Genet. (1991) 228:70-80 !$#title Organization and nucleotide sequence of ten ribosomal !1protein genes from the region equivalent to the !1spectinomycin operon in the archaebacterium Halobacterium !1marismortui. !$#cross-references MUID:91360093; PMID:1832208 !$#accession S16544 !'##molecule_type DNA !'##residues 1-70 ##label SCH !'##cross-references EMBL:X58395; NID:g48860; PIDN:CAA41293.1; !1PID:g48870 REFERENCE A28926 !$#authors Walsh, M.J.; McDougall, J.; Wittmann-Liebold, B. !$#journal Biochemistry (1988) 27:6867-6876 !$#title Extended N-terminal sequencing of proteins of !1archaebacterial ribosomes blotted from two-dimensional gels !1onto glass fiber and poly(vinylidene difluoride) membrane. !$#cross-references MUID:89062418; PMID:3196689 !$#accession C28949 !'##molecule_type protein !'##residues 'D',3-30,'NR' ##label WAL !'##note the protein is designated as ribosomal protein L7 GENETICS !$#note HmaL15 CLASSIFICATION #superfamily rat ribosomal protein L27a KEYWORDS protein biosynthesis; ribosome FEATURE !$2-155 #product ribosomal protein L15 #status experimental !8#label MAT SUMMARY #length 165 #molecular-weight 17973 #checksum 1801 SEQUENCE /// ENTRY JC2444 #type complete TITLE ribosomal protein L24, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 21-Jul-2000 ACCESSIONS JC2444; PC2282 REFERENCE JC2444 !$#authors Chan, Y.L.; Olvera, J.; Wool, I.G. !$#journal Biochem. Biophys. Res. Commun. (1994) 202:1176-1180 !$#title The primary structure of rat ribosomal protein L24. !$#cross-references MUID:94324945; PMID:8048931 !$#accession JC2444 !'##molecule_type mRNA !'##residues 1-157 ##label CHA1 !'##cross-references EMBL:X78443; NID:g560492; PIDN:CAA55203.1; !1PID:g560493 !$#accession PC2282 !'##molecule_type protein !'##residues 52-80 ##label CHA2 !'##note the protein is designated as ribosomal protein L24 CLASSIFICATION #superfamily rat ribosomal protein L24 SUMMARY #length 157 #molecular-weight 17779 #checksum 4587 SEQUENCE /// ENTRY R6BYT9 #type complete TITLE ribosomal protein L24.e.A, cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein G3648; protein YGL031c; ribosomal protein rp29; ribosomal protein YL21; ribosomal protein YL30.A ORGANISM #formal_name Saccharomyces cerevisiae DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 21-Jul-2000 ACCESSIONS A02783; S64033 REFERENCE A02783 !$#authors Mitra, G.; Warner, J.R. !$#journal J. Biol. Chem. (1984) 259:9218-9224 !$#title A yeast ribosomal protein gene whose intron is in the 5' !1leader. !$#cross-references MUID:84264556; PMID:6086628 !$#accession A02783 !'##molecule_type DNA !'##residues 1-155 ##label MIT !'##cross-references EMBL:K02650; NID:g172485; PIDN:AAA35004.1; !1PID:g172486 REFERENCE S64003 !$#authors Hebling, U.; Hofmann, B.; Delius, H. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64033 !'##molecule_type DNA !'##residues 1-155 ##label HEB !'##cross-references EMBL:Z72553; NID:g1322505; PIDN:CAA96732.1; !1PID:g1322506; GSPDB:GN00007; MIPS:YGL031c !'##experimental_source strain S288C GENETICS !$#gene SGD:RPL30A; MIPS:YGL031c !'##cross-references SGD:S0002999; MIPS:YGL031c !$#map_position 7L CLASSIFICATION #superfamily rat ribosomal protein L24 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 155 #molecular-weight 17613 #checksum 7501 SEQUENCE /// ENTRY R6BYY0 #type complete TITLE ribosomal protein L24.e.B, cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein G6635; protein YGR148c; ribosomal protein rp29; ribosomal protein YL21; ribosomal protein YL30.B ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 21-Jul-2000 ACCESSIONS A35925; S60439; S64457; S12770 REFERENCE A35925 !$#authors Baronas-Lowell, D.M.; Warner, J.R. !$#journal Mol. Cell. Biol. (1990) 10:5235-5243 !$#title Ribosomal protein L30 is dispensable in the yeast !1Saccharomyces cerevisiae. !$#cross-references MUID:90377213; PMID:2204809 !$#accession A35925 !'##molecule_type DNA !'##residues 1-155 ##label BAR !'##cross-references EMBL:M34387; NID:g171820; PIDN:AAA34736.1; !1PID:g171821 REFERENCE S60435 !$#authors Skala, J.; Nawrocki, A.; Goffeau, A. !$#journal Yeast (1995) 11:1421-1427 !$#title The sequence of a 27 kb segment on the right arm of !1chromosome VII from Saccharomyces cerevisiae reveals MOL1, !1NAT2, RPL30B, RSR1, CYS4, PEM1/CHO2, NSR1 genes and ten new !1open reading frames. !$#cross-references MUID:96158062; PMID:8585325 !$#accession S60439 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-155 ##label SKA !'##cross-references EMBL:X85807; NID:g1045249; PIDN:CAA59806.1; !1PID:g1045254 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1March 1995 REFERENCE S64428 !$#authors Van Dyck, L.; Skala, J.; de Wergifosse, P.; Purnelle, B.; !1Talla, E.; Nawrocki, A.; Del Bino, S.; Goffeau, A. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64457 !'##molecule_type DNA !'##residues 1-155 ##label VAN !'##cross-references EMBL:Z72933; NID:g1323249; PIDN:CAA97162.1; !1PID:g1323250; GSPDB:GN00007; MIPS:YGR148c !'##experimental_source strain S288C GENETICS !$#gene SGD:RPL30B; MIPS:YGR148c !'##cross-references SGD:S0003380; MIPS:YGR148c !$#map_position 7R CLASSIFICATION #superfamily rat ribosomal protein L24 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 155 #molecular-weight 17547 #checksum 7757 SEQUENCE /// ENTRY R6HS21 #type complete TITLE ribosomal protein L24.eR [validated] - Haloarcula marismortui ALTERNATE_NAMES ribosomal protein HL21; ribosomal protein HL22 ORGANISM #formal_name Haloarcula marismortui DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 04-Feb-2000 ACCESSIONS S06846 REFERENCE S06844 !$#authors Hatakeyama, T.; Kaufmann, F.; Schroeter, B.; Hatakeyama, T. !$#journal Eur. J. Biochem. (1989) 185:685-693 !$#title Primary structures of five ribosomal proteins from the !1archaebacterium Halobacterium marismortui and their !1structural relationships to eubacterial and eukaryotic !1ribosomal proteins. !$#cross-references MUID:90076190; PMID:2591382 !$#accession S06846 !'##molecule_type protein !'##residues 1-66 ##label HAT !'##note the source is designated as Halobacterium marismortui !'##note the protein is designated as ribosomal protein HL21/22 CLASSIFICATION #superfamily Haloarcula ribosomal protein HL21 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 66 #molecular-weight 7225 #checksum 6750 SEQUENCE /// ENTRY R4HU17 #type complete TITLE ribosomal protein S17, cytosolic [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 08-Dec-2000 ACCESSIONS JT0405; B25899; S68929 REFERENCE JT0405 !$#authors Chen, I.T.; Roufa, D.J. !$#journal Gene (1988) 70:107-116 !$#title The transcriptionally active human ribosomal protein S17 !1gene. !$#cross-references MUID:89196902; PMID:3240863 !$#accession JT0405 !'##molecule_type DNA !'##residues 1-135 ##label CHE !'##cross-references GB:M18000; NID:g337502; PIDN:AAA60285.1; !1PID:g337503 REFERENCE A94124 !$#authors Chen, I.T.; Dixit, A.; Rhoads, D.D.; Roufa, D.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:6907-6911 !$#title Homologous ribosomal proteins in bacteria, yeast, and !1humans. !$#cross-references MUID:86313681; PMID:3529092 !$#accession B25899 !'##molecule_type mRNA !'##residues 1-135 ##label CHE2 !'##cross-references GB:M13932; NID:g337500; PIDN:AAA60284.1; !1PID:g337501 REFERENCE S68911 !$#authors Vladimirov, S.N.; Ivanov, A.V.; Karpova, G.G.; Musolyamov, !1A.K.; Egorov, T.A.; Thiede, B.; Wittmann-Liebold, B.; Otto, !1A. !$#journal Eur. J. Biochem. (1996) 239:144-149 !$#title Characterization of the human small-ribosomal-subunit !1proteins by N-terminal and internal sequencing, and mass !1spectrometry. !$#cross-references MUID:96305378; PMID:8706699 !$#accession S68929 !'##molecule_type protein !'##residues 2-16 ##label VLA GENETICS !$#gene GDB:RPS17 !'##cross-references GDB:128851; OMIM:180472 !$#map_position 11pter-11p13 !$#introns 1/3; 52/2; 87/3; 109/3 CLASSIFICATION #superfamily rat ribosomal protein S17 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-135 #product ribosomal protein S17, cytosolic #status !8experimental #label MAT SUMMARY #length 135 #molecular-weight 15550 #checksum 9216 SEQUENCE /// ENTRY R4RT17 #type complete TITLE ribosomal protein S17, cytosolic - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1987 #sequence_revision 30-Jun-1991 #text_change 21-Jul-2000 ACCESSIONS A24028 REFERENCE A24028 !$#authors Nakanishi, O.; Oyanagi, M.; Kuwano, Y.; Tanaka, T.; !1Nakayama, T.; Mitsui, H.; Nabeshima, Y.I.; Ogata, K. !$#journal Gene (1985) 35:289-296 !$#title Molecular cloning and nucleotide sequences of cDNAs specific !1for rat liver ribosomal proteins S17 and L30. !$#cross-references MUID:86006278; PMID:3840111 !$#accession A24028 !'##molecule_type mRNA !'##residues 1-135 ##label NAK !'##cross-references EMBL:K02933; NID:g206744; PIDN:AAA42078.1; !1PID:g206745 CLASSIFICATION #superfamily rat ribosomal protein S17 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-135 #product ribosomal protein S17 #status predicted !8#label MAT SUMMARY #length 135 #molecular-weight 15509 #checksum 9267 SEQUENCE /// ENTRY R4FF17 #type complete TITLE ribosomal protein S17 - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 22-Jun-1999 ACCESSIONS JU0055; A30844 REFERENCE A91611 !$#authors Maki, C.; Rhoads, D.D.; Stewart, M.J.; Van Slyke, B.; Roufa, !1D.J. !$#journal Gene (1989) 79:289-298 !$#title The Drosophila melanogaster RPS17 gene encoding ribosomal !1protein S17. !$#cross-references MUID:90006758; PMID:2507396 !$#accession JU0055 !'##molecule_type DNA !'##residues 1-131 ##label MAK !'##cross-references GB:M22142; NID:g158333; PIDN:AAA28869.1; !1PID:g158334 GENETICS !$#gene RPS17 !'##cross-references FlyBase:FBgn0005533 !$#map_position 3L (67B1-5) !$#introns 1/3; 52/2 CLASSIFICATION #superfamily rat ribosomal protein S17 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 131 #molecular-weight 15285 #checksum 2257 SEQUENCE /// ENTRY R5BY51 #type complete TITLE ribosomal protein S17.e.A, cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YML024w; ribosomal protein 51A ORGANISM #formal_name Saccharomyces cerevisiae DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 19-Apr-2002 ACCESSIONS A02784; B02784; S49753 REFERENCE A02784 !$#authors Teem, J.L.; Rosbash, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:4403-4407 !$#title Expression of a beta-galactosidase gene containing the !1ribosomal protein 51 intron is sensitive to the rna2 !1mutation of yeast. !$#cross-references MUID:83273631; PMID:6308621 !$#accession A02784 !'##molecule_type DNA !'##residues 1-136 ##label TEE !'##cross-references EMBL:J01349; NID:g172457; PIDN:AAA88733.1; !1PID:g172458 !$#accession B02784 !'##molecule_type mRNA !'##residues 1-4 ##label TEE2 REFERENCE S49741 !$#authors Badcock, K.; Churcher, C. !$#submission submitted to the EMBL Data Library, November 1994 !$#accession S49753 !'##molecule_type DNA !'##residues 1-136 ##label BAD !'##cross-references EMBL:Z46659; NID:g575680; PIDN:CAA86631.1; !1PID:g575695; GSPDB:GN00013; MIPS:YML024w GENETICS !$#gene SGD:RPS17A; RP51A; MIPS:YML024w !'##cross-references SGD:S0004486 !$#map_position 13L !$#introns 1/3 CLASSIFICATION #superfamily rat ribosomal protein S17 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 136 #molecular-weight 15788 #checksum 5519 SEQUENCE /// ENTRY R4BY7B #type complete TITLE ribosomal protein S17.e.B, cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YDR447c; ribosomal protein 51B ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 23-Mar-2001 ACCESSIONS S20161; S69726 REFERENCE S20161 !$#authors Abovich, N.; Rosbash, M. !$#journal Mol. Cell. Biol. (1984) 4:1871-1879 !$#title Two genes for ribosomal protein 51 of Saccharomyces !1cerevisiae complement and contribute to the ribosomes. !$#cross-references MUID:85036340; PMID:6092944 !$#accession S20161 !'##status translation not shown !'##molecule_type DNA !'##residues 1-136 ##label ABO !'##cross-references EMBL:K02480; NID:g172459; PIDN:AAA34991.1; !1PID:g172460 !'##experimental_source strain A364A REFERENCE S69555 !$#authors Dietrich, F.S. !$#submission submitted to the EMBL Data Library, August 1995 !$#description The sequence of S. cerevisiae lambda 3641 and cosmids 9461, !19831, and 9410. !$#accession S69726 !'##molecule_type DNA !'##residues 1-136 ##label DIE !'##cross-references EMBL:U33007; NID:g927685; PIDN:AAB64890.1; !1PID:g927724; GSPDB:GN00004; MIPS:YDR447c GENETICS !$#gene SGD:RP51B; MIPS:YDR447c !'##cross-references SGD:S0002855; MIPS:YDR447c !$#map_position 4R !$#introns 1/3 CLASSIFICATION #superfamily rat ribosomal protein S17 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 136 #molecular-weight 15803 #checksum 5343 SEQUENCE /// ENTRY R5EC10 #type complete TITLE ribosomal protein L10 [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 24-Apr-1984 #sequence_revision 30-Jun-1991 #text_change 01-Mar-2002 ACCESSIONS S12574; S13546; A02785; D65205 REFERENCE S12572 !$#authors Post, L.E.; Strycharz, G.D.; Nomura, M.; Lewis, H.; Dennis, !1P.P. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1979) 76:1697-1701 !$#title Nucleotide sequence of the ribosomal protein gene cluster !1adjacent to the gene for RNA polymerase subunit beta in !1Escherichia coli. !$#cross-references MUID:79201667; PMID:377281 !$#accession S12574 !'##molecule_type DNA !'##residues 1-165 ##label POS !'##cross-references EMBL:V00339; NID:g42813; PIDN:CAA23623.1; !1PID:g42816 !'##note the authors translated the codon GAG for residue 107 as Gly REFERENCE S13546 !$#authors Heiland, I.; Brauer, D.; Wittmann-Liebold, B. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1976) 357:1751-1770 !$#title Primary structure of protein L10 from the large subunit of !1Escherichia coli ribosomes. !$#cross-references MUID:77117445; PMID:797648 !$#accession S13546 !'##molecule_type protein !'##residues 2-84,'R',85-115,'Q',117-165 ##label HEI !'##experimental_source strain K12 A19 REFERENCE A02785 !$#authors Dovgas, N.V.; Vinokurov, L.M.; Velmoga, I.S.; Alakhov, Y.B.; !1Ovchinnikov, Y.A. !$#journal FEBS Lett. (1976) 67:58-61 !$#title The primary structure of protein L10 from Escherichia coli !1ribosomes. !$#cross-references MUID:76257859; PMID:782920 !$#accession A02785 !'##molecule_type protein !'##residues 2-16,'Q',18-76,78-79,'V',81-84,'R',85-165 ##label DOV1 !'##experimental_source strain MRE-600 REFERENCE A30436 !$#authors Dovgas, N.V.; Vinokurov, L.M.; Velmoga, I.S.; Alakhov, Y.B.; !1Ovchinnikov, Y.A. !$#submission submitted to the Atlas, July 1977 !$#contents annotation; strain MRE-600, revisions REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65205 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-165 ##label BLAT !'##cross-references GB:AE000472; GB:U00096; NID:g2367333; !1PIDN:AAC76959.1; PID:g1790417; UWGP:b3985 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note mass spectrographic analysis of post-translational !1modifications; any acid labile modifications may have been !1missed GENETICS !$#gene rplJ !$#map_position 90 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX large subunit ribosomal proteins: L1 (PIR:R5EC1), L3 !1(PIR:R5EC3), L2 (PIR:R5EC2), L4 (PIR:R5EC4), L5 (PIR:R5EC5), !1L6 (PIR:R5EC6), L7/L12 (PIR:R5EC7), L9 (PIR:R5EC9), L10 !1(PIR:R5EC10), L11 (PIR:R5EC11), L13 (PIR:R5EC13), L14 !1(PIR:R5EC14), L15 (PIR:R5EC15), L16 (PIR:R5EC16), L17 !1(PIR:R5EC17), L18 (PIR:R5EC18), L19 (PIR:R5EC19) FUNCTION !$#pathway protein biosynthesis CLASSIFICATION #superfamily Escherichia coli ribosomal protein L10 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-165 #product ribosomal protein L10 #status experimental !8#label MAT SUMMARY #length 165 #molecular-weight 17711 #checksum 4735 SEQUENCE /// ENTRY R5EB10 #type complete TITLE ribosomal protein L10 - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S10895; S12827; S10011 REFERENCE S10895 !$#authors Paton, E.B.; Woodmaska, M.I.; Kroupskaya, I.V.; Zhyvoloup, !1A.N.; Matsuka, G.K. !$#journal FEBS Lett. (1990) 265:129-132 !$#title Evidence for the ability of L10 ribosomal proteins of !1Salmonella typhimurium and Klebsiella pneumoniae to regulate !1rplJL gene expression in Escherichia coli. !$#cross-references MUID:90306303; PMID:2194828 !$#accession S10895 !'##molecule_type DNA !'##residues 1-165 ##label PAT !'##cross-references EMBL:X53072; NID:g47915; PIDN:CAA37245.1; !1PID:g47916 REFERENCE S12827 !$#authors Zhyvoloup, A.N.; Woodmaska, M.I.; Kroupskaya, I.V.; Paton, !1E.B. !$#journal Nucleic Acids Res. (1990) 18:4620 !$#title Nucleotide sequence of the rplJL operon and the deduced !1primary structure of the encoded L10 and L7/L12 proteins of !1Salmonella typhimurium compared to that of Escherichia coli. !$#cross-references MUID:90356427; PMID:2201953 !$#accession S12827 !'##molecule_type DNA !'##residues 1-165 ##label ZHY !'##cross-references EMBL:X53072; NID:g47915; PIDN:CAA37245.1; !1PID:g47916 !'##note the authors translated the codon CTG for residue 81 as Glu and !1GAG for residue 107 as Gly GENETICS !$#gene rplJ CLASSIFICATION #superfamily Escherichia coli ribosomal protein L10 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-165 #product ribosomal protein L10 #status predicted !8#label MAT SUMMARY #length 165 #molecular-weight 17800 #checksum 5214 SEQUENCE /// ENTRY S32238 #type complete TITLE ribosomal protein L10 - Streptomyces griseus ORGANISM #formal_name Streptomyces griseus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S32238 REFERENCE S32234 !$#authors Kuester, K.; Kuberski, S.; Piepersberg, W.; Distler, J. !$#submission submitted to the EMBL Data Library, March 1993 !$#description Cloning and nucleotide sequence analysis of the !1nusG-rplK-rplA-rplJ-rplL gene cluster of S. griseus. !$#accession S32238 !'##molecule_type DNA !'##residues 1-185 ##label KUE !'##cross-references EMBL:X72787; NID:g575399; PIDN:CAA51300.1; !1PID:g288464 GENETICS !$#gene rplJ CLASSIFICATION #superfamily Escherichia coli ribosomal protein L10 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 185 #molecular-weight 19484 #checksum 860 SEQUENCE /// ENTRY S35492 #type complete TITLE ribosomal protein L10 - Streptomyces antibioticus ORGANISM #formal_name Streptomyces antibioticus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S35492 REFERENCE S35492 !$#authors Blanco, G.; Parra, F.; Mendez, C.; Salas, J.A. !$#journal Nucleic Acids Res. (1992) 20:5223 !$#title The nucleotide sequence of the L10 equivalent ribosomal !1protein gene of Streptomyces antibioticus. !$#cross-references MUID:93027265; PMID:1408837 !$#accession S35492 !'##molecule_type DNA !'##residues 1-176 ##label BLA !'##cross-references EMBL:M89911; NID:g153436; PIDN:AAA26810.1; !1PID:g153437 GENETICS !$#gene rplJ CLASSIFICATION #superfamily Escherichia coli ribosomal protein L10 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 176 #molecular-weight 18596 #checksum 6722 SEQUENCE /// ENTRY S13068 #type complete TITLE ribosomal protein L10 - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S13068; S77314 REFERENCE S13068 !$#authors Sibold, C.; Subramanian, A.R. !$#journal Biochim. Biophys. Acta (1990) 1050:61-68 !$#title Cloning and characterization of the genes for ribosomal !1proteins L10 and L12 from Synechocystis sp. PCC 6803: !1comparison of gene clustering pattern and protein sequence !1homology between cyanobacteria and chloroplasts. !$#cross-references MUID:91002677; PMID:2119815 !$#accession S13068 !'##molecule_type DNA !'##residues 1-173 ##label SIB !'##cross-references EMBL:X53178; NID:g47474; PIDN:CAA37317.1; !1PID:g47475 !'##experimental_source PCC 6803 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S77314 !'##status preliminary !'##molecule_type DNA !'##residues 1-173 ##label KAN !'##cross-references EMBL:D90906; GB:AB001339; NID:g1652492; !1PIDN:BAA17417.1; PID:g1652496 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene rplJ CLASSIFICATION #superfamily Escherichia coli ribosomal protein L10 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 173 #molecular-weight 18675 #checksum 3286 SEQUENCE /// ENTRY R5HG10 #type complete TITLE ribosomal protein L10 - Thermotoga maritima (strain MSB8) ORGANISM #formal_name Thermotoga maritima DATE 31-Dec-1992 #sequence_revision 18-Jun-1999 #text_change 21-Jul-2000 ACCESSIONS A72376; D44466; S41464; S19901 REFERENCE A72200 !$#authors Nelson, K.E.; Clayton, R.A.; Gill, S.R.; Gwinn, M.L.; !1Dodson, R.J.; Haft, D.H.; Hickey, E.K.; Peterson, J.D.; !1Nelson, W.C.; Ketchum, K.A.; McDonald, L.; Utterback, T.R.; !1Malek, J.A.; Linher, K.D.; Garrett, M.M.; Stewart, A.M.; !1Cotton, M.D.; Pratt, M.S.; Phillips, C.A.; Richardson, D.; !1Heidelberg, J.; Sutton, G.G.; Fleischmann, R.D.; White, O.; !1Salzberg, S.L.; Smith, H.O.; Venter, J.C.; Fraser, C.M. !$#journal Nature (1999) 399:323-329 !$#title Evidence for lateral gene transfer between Archaea and !1Bacteria from genome sequence of Thermotoga maritima. !$#cross-references MUID:99287316; PMID:10360571 !$#accession A72376 !'##status preliminary !'##molecule_type DNA !'##residues 1-179 ##label ARN !'##cross-references GB:AE001723; GB:AE000512; NID:g4980953; !1PIDN:AAD35539.1; PID:g4980962; TIGR:TM0456 !'##experimental_source strain MSB8 REFERENCE A44466 !$#authors Liao, D.; Dennis, P.P. !$#journal J. Biol. Chem. (1992) 267:22787-22797 !$#title The organization and expression of essential transcription !1translation component genes in the extremely thermophilic !1eubacterium Thermotoga maritima. !$#cross-references MUID:93054590; PMID:1429627 !$#accession D44466 !'##molecule_type DNA !'##residues 1-167,'C',169-179 ##label LIA !'##cross-references EMBL:Z11839 !'##note sequence extracted from NCBI backbone (NCBIP:118057) REFERENCE S41462 !$#authors Palm, P.; Schleper, C.; Arnold-Ammer, I.; Holz, I.; Meier, !1T.; Lottspeich, F.; Zillig, W. !$#journal Nucleic Acids Res. (1993) 21:4904-4908 !$#title The DNA-dependent RNA-polymerase of Thermotoga maritima; !1characterisation of the enzyme and the DNA-sequence of the !1genes for the large subunits. !$#cross-references MUID:94232816; PMID:8177738 !$#accession S41464 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 45-179 ##label PAL !'##cross-references EMBL:X72695; NID:g425255; PIDN:CAA51244.1; !1PID:g425256 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1March 1993 GENETICS !$#gene TM0456 !$#start_codon TTG CLASSIFICATION #superfamily Escherichia coli ribosomal protein L10 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 179 #molecular-weight 20308 #checksum 1411 SEQUENCE /// ENTRY R5EC11 #type complete TITLE ribosomal protein L11 [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-May-1979 #sequence_revision 30-Jun-1991 #text_change 01-Mar-2002 ACCESSIONS S12572; A02786; B65205; C35139 REFERENCE S12572 !$#authors Post, L.E.; Strycharz, G.D.; Nomura, M.; Lewis, H.; Dennis, !1P.P. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1979) 76:1697-1701 !$#title Nucleotide sequence of the ribosomal protein gene cluster !1adjacent to the gene for RNA polymerase subunit beta in !1Escherichia coli. !$#cross-references MUID:79201667; PMID:377281 !$#accession S12572 !'##molecule_type DNA !'##residues 1-142 ##label POS !'##cross-references EMBL:V00339; GB:J01678; GB:K00449; NID:g42813; !1PIDN:CAA23621.1; PID:g42814 !'##note the sequence in GenBank entry ECRPOBC, release 111.0, !1(PID:g42814) has the codon AGT for 132-Thr rather than the !1published ACT REFERENCE A02786 !$#authors Dognin, M.J.; Wittmann-Liebold, B. !$#journal Eur. J. Biochem. (1980) 112:131-151 !$#title Purification and primary structure determination of the !1N-terminal blocked protein, L11, from Escherichia coli !1ribosomes. !$#cross-references MUID:81090351; PMID:7004866 !$#accession A02786 !'##molecule_type protein !'##residues 2-142 ##label DOG !'##experimental_source strain K12 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65205 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-142 ##label BLAT !'##cross-references GB:AE000472; GB:U00096; NID:g2367333; !1PIDN:AAC76957.1; PID:g2367334; UWGP:b3983 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note mass spectrographic analysis of post-translational !1modifications; any acid labile modifications may have been !1missed COMMENT For ribosomal protein L11 methyltransferase (EC 2.1.1.-), !1see PIR:E65118. GENETICS !$#gene rplK !$#map_position 90 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX large subunit ribosomal proteins: L1 (PIR:R5EC1), L3 !1(PIR:R5EC3), L2 (PIR:R5EC2), L4 (PIR:R5EC4), L5 (PIR:R5EC5), !1L6 (PIR:R5EC6), L7/L12 (PIR:R5EC7), L9 (PIR:R5EC9), L10 !1(PIR:R5EC10), L11 (PIR:R5EC11), L13 (PIR:R5EC13), L14 !1(PIR:R5EC14), L15 (PIR:R5EC15), L16 (PIR:R5EC16), L17 !1(PIR:R5EC17), L18 (PIR:R5EC18), L19 (PIR:R5EC19) FUNCTION !$#pathway protein biosynthesis !$#note binds 23S rRNA CLASSIFICATION #superfamily Escherichia coli ribosomal protein L11 KEYWORDS blocked amino end; methylated amino acid; methylated amino !1end; protein biosynthesis; ribosome; RNA binding FEATURE !$2-142 #product ribosomal protein L11 #status experimental !8#label MAT\ !$2 #modified_site trimethylated amino end (Ala) (in !8mature form) #status experimental\ !$4,40 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental SUMMARY #length 142 #molecular-weight 14875 #checksum 9725 SEQUENCE /// ENTRY R5SE11 #type complete TITLE ribosomal protein L11 - Serratia marcescens ORGANISM #formal_name Serratia marcescens DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S01967 REFERENCE S01967 !$#authors Sor, F.; Nomura, M. !$#journal Mol. Gen. Genet. (1987) 210:52-59 !$#title Cloning and DNA sequence determination of the L11 ribosomal !1protein operon of Serratia marcescens and Proteus vulgaris: !1translational feedback regulation of the Escherichia coli !1L11 operon by heterologous L1 proteins. !$#cross-references MUID:88121705; PMID:3323840 !$#accession S01967 !'##molecule_type DNA !'##residues 1-142 ##label SOR !'##cross-references EMBL:X12584; NID:g47255; PIDN:CAA31095.1; !1PID:g47256 GENETICS !$#gene rplK CLASSIFICATION #superfamily Escherichia coli ribosomal protein L11 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 142 #molecular-weight 14908 #checksum 554 SEQUENCE /// ENTRY R5EB1P #type complete TITLE ribosomal protein L11 - Proteus vulgaris ORGANISM #formal_name Proteus vulgaris DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S01969 REFERENCE S01967 !$#authors Sor, F.; Nomura, M. !$#journal Mol. Gen. Genet. (1987) 210:52-59 !$#title Cloning and DNA sequence determination of the L11 ribosomal !1protein operon of Serratia marcescens and Proteus vulgaris: !1translational feedback regulation of the Escherichia coli !1L11 operon by heterologous L1 proteins. !$#cross-references MUID:88121705; PMID:3323840 !$#accession S01969 !'##molecule_type DNA !'##residues 1-142 ##label SOR !'##cross-references EMBL:X12585; NID:g45924; PIDN:CAA31097.1; !1PID:g45925 GENETICS !$#gene rplK CLASSIFICATION #superfamily Escherichia coli ribosomal protein L11 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 142 #molecular-weight 14755 #checksum 816 SEQUENCE /// ENTRY R5HG11 #type complete TITLE ribosomal protein L11 - Thermotoga maritima (strain MSB8) ORGANISM #formal_name Thermotoga maritima DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 21-Jul-2000 ACCESSIONS B44466; G72375; S19899 REFERENCE A44466 !$#authors Liao, D.; Dennis, P.P. !$#journal J. Biol. Chem. (1992) 267:22787-22797 !$#title The organization and expression of essential transcription !1translation component genes in the extremely thermophilic !1eubacterium Thermotoga maritima. !$#cross-references MUID:93054590; PMID:1429627 !$#accession B44466 !'##molecule_type DNA !'##residues 1-141 ##label LIA !'##cross-references EMBL:Z11839; NID:g407020; PIDN:CAA77859.1; !1PID:g48184 !'##note sequence extracted from NCBI backbone (NCBIP:118055) REFERENCE A72200 !$#authors Nelson, K.E.; Clayton, R.A.; Gill, S.R.; Gwinn, M.L.; !1Dodson, R.J.; Haft, D.H.; Hickey, E.K.; Peterson, J.D.; !1Nelson, W.C.; Ketchum, K.A.; McDonald, L.; Utterback, T.R.; !1Malek, J.A.; Linher, K.D.; Garrett, M.M.; Stewart, A.M.; !1Cotton, M.D.; Pratt, M.S.; Phillips, C.A.; Richardson, D.; !1Heidelberg, J.; Sutton, G.G.; Fleischmann, R.D.; White, O.; !1Salzberg, S.L.; Smith, H.O.; Venter, J.C.; Fraser, C.M. !$#journal Nature (1999) 399:323-329 !$#title Evidence for lateral gene transfer between Archaea and !1Bacteria from genome sequence of Thermotoga maritima. !$#cross-references MUID:99287316; PMID:10360571 !$#accession G72375 !'##molecule_type DNA !'##residues 1-141 ##label ARN !'##cross-references GB:AE001723; GB:AE000512; NID:g4980953; !1PIDN:AAD35537.1; PID:g4980960; TIGR:TM0454 !'##experimental_source strain MSB8 GENETICS !$#gene TM0454 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L11 KEYWORDS protein biosynthesis; ribosome; RNA binding SUMMARY #length 141 #molecular-weight 15089 #checksum 7047 SEQUENCE /// ENTRY R5SP11 #type complete TITLE ribosomal protein L11 precursor - spinach ORGANISM #formal_name Spinacia oleracea #common_name spinach DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 22-Jun-1999 ACCESSIONS S23238 REFERENCE S23238 !$#authors Smooker, P.M.; Schmidt, J.; Subramanian, A.R. !$#journal Biochimie (1991) 73:845-851 !$#title The nuclear:organelle distribution of chloroplast ribosomal !1proteins genes. Features of a cDNA clone encoding the !1cytoplasmic precursor of L11. !$#cross-references MUID:92110450; PMID:1764529 !$#accession S23238 !'##molecule_type mRNA !'##residues 1-224 ##label SMO !'##cross-references EMBL:X56615; NID:g21312; PIDN:CAA39950.1; !1PID:g21313 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L11 KEYWORDS chloroplast; protein biosynthesis; ribosome FEATURE !$1-65 #domain (or 1-66) transit peptide (chloroplast) !8#status predicted #label TNP\ !$66-224 #product (or 67-224) ribosomal protein L11 #status !8predicted #label MAT SUMMARY #length 224 #molecular-weight 23659 #checksum 5831 SEQUENCE /// ENTRY R5HSC1 #type complete TITLE ribosomal protein L11 [validated] - Halobacterium salinarum ORGANISM #formal_name Halobacterium salinarum DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 21-Jul-2000 ACCESSIONS S04118; S08553; S11583 REFERENCE S04116 !$#authors Shimmin, L.C.; Dennis, P.P. !$#journal EMBO J. (1989) 8:1225-1235 !$#title Characterization of the L11, L1, L10 and L12 equivalent !1ribosomal protein gene cluster of the halophilic !1archaebacterium Halobacterium cutirubrum. !$#cross-references MUID:89305527; PMID:2743981 !$#accession S04118 !'##molecule_type DNA !'##residues 1-163 ##label SHI !'##cross-references EMBL:X15078; NID:g43449; PIDN:CAA33178.1; !1PID:g43452 !'##note the source is designated as Halobacterium cutirubrum REFERENCE S07437 !$#authors Matheson, A.T.; Yaguchi, M.; Christensen, P.; Rollin, C.F.; !1Hasnain, S. !$#journal Can. J. Biochem. Cell Biol. (1984) 62:426-433 !$#title Purification, properties, and N-terminal amino acid sequence !1of certain 50S ribosomal subunit proteins from the !1archaebacterium Halobacterium cutirubrum. !$#cross-references MUID:84282108; PMID:6467081 !$#accession S08553 !'##molecule_type protein !'##residues 2-35 ##label MAT1 !'##note the source is designated as Halobacterium cutirubrum !'##note the protein is designated as ribosomal protein L11 FUNCTION !$#description binds to 23S rRNA CLASSIFICATION #superfamily Escherichia coli ribosomal protein L11 KEYWORDS protein biosynthesis; ribosome; RNA binding FEATURE !$2-163 #product ribosomal protein L11 #status experimental !8#label MAT SUMMARY #length 163 #molecular-weight 17038 #checksum 8555 SEQUENCE /// ENTRY R5HS11 #type complete TITLE ribosomal protein L11 [validated] - Haloarcula marismortui ALTERNATE_NAMES ribosomal protein HL10 ORGANISM #formal_name Haloarcula marismortui DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 04-Feb-2000 ACCESSIONS S08420; F28949 REFERENCE S08420 !$#authors Arndt, E.; Weigel, C. !$#journal Nucleic Acids Res. (1990) 18:1285 !$#title Nucleotide sequence of the genes encoding the L11, L1, L10 !1and L12 equivalent ribosomal proteins from the !1archaebacterium Halobacterium marismortui. !$#cross-references MUID:90206791; PMID:2320419 !$#accession S08420 !'##status translation not shown !'##molecule_type DNA !'##residues 1-162 ##label ARN !'##cross-references EMBL:X51430; NID:g43602; PIDN:CAA35793.1; !1PID:g43603 !'##note the source is designated as Halobacterium marismortui REFERENCE A28926 !$#authors Walsh, M.J.; McDougall, J.; Wittmann-Liebold, B. !$#journal Biochemistry (1988) 27:6867-6876 !$#title Extended N-terminal sequencing of proteins of !1archaebacterial ribosomes blotted from two-dimensional gels !1onto glass fiber and poly(vinylidene difluoride) membrane. !$#cross-references MUID:89062418; PMID:3196689 !$#accession F28949 !'##molecule_type protein !'##residues 2-28 ##label WAL !'##note the protein is designated as ribosomal protein L10 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L11 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-162 #product ribosomal protein L11 #status experimental !8#label MAT SUMMARY #length 162 #molecular-weight 17089 #checksum 7211 SEQUENCE /// ENTRY R7RT12 #type complete TITLE ribosomal protein L12, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 21-Jul-2000 ACCESSIONS A36667; A33222; S13113 REFERENCE A36667 !$#authors Suzuki, K.; Olvera, J.; Wool, I.G. !$#journal Biochem. Biophys. Res. Commun. (1990) 172:35-41 !$#title The primary structure of rat ribosomal protein L12. !$#cross-references MUID:91025067; PMID:1977388 !$#accession A36667 !'##molecule_type mRNA !'##residues 1-165 ##label SUZ !'##cross-references EMBL:X53504; NID:g57679; PIDN:CAA37581.1; !1PID:g57680 !$#accession A33222 !'##molecule_type protein !'##residues 7-29 ##label SUZ2 !'##note the protein is designated as ribosomal protein L12 CLASSIFICATION #superfamily rat ribosomal protein L12 KEYWORDS protein biosynthesis; ribosome; RNA binding SUMMARY #length 165 #molecular-weight 17845 #checksum 7302 SEQUENCE /// ENTRY JN0778 #type complete TITLE ribosomal protein L12 - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 03-Feb-1994 #sequence_revision 03-Feb-1994 #text_change 22-Jun-1999 ACCESSIONS JN0778 REFERENCE JN0778 !$#authors Hou, E.W.; Li, S.S.L. !$#journal Gene (1993) 130:287-290 !$#title Sequence analysis of mouse cDNAs encoding ribosomal proteins !1L12 and L18. !$#cross-references MUID:93366188; PMID:8359697 !$#accession JN0778 !'##molecule_type mRNA !'##residues 1-165 ##label HOU !'##cross-references GB:L04280; NID:g398047; PIDN:AAA40066.1; !1PID:g398048 GENETICS !$#gene L12 CLASSIFICATION #superfamily rat ribosomal protein L12 KEYWORDS protein biosynthesis; ribosome; RNA binding SUMMARY #length 165 #molecular-weight 17790 #checksum 7784 SEQUENCE /// ENTRY R5EC13 #type complete TITLE ribosomal protein L13 [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-May-1979 #sequence_revision 31-May-1979 #text_change 01-Mar-2002 ACCESSIONS A02787; I57732; A65115 REFERENCE A02787 !$#authors Mende, L. !$#journal FEBS Lett. (1978) 96:313-316 !$#title The primary structure of protein L13 from the large subunit !1of Escherichia coli ribosomes. !$#cross-references MUID:79086244; PMID:365580 !$#accession A02787 !'##molecule_type protein !'##residues 1-142 ##label MEN !'##experimental_source strain K REFERENCE I57732 !$#authors Isono, S.; Thamm, S.; Kitakawa, M.; Isono, K. !$#journal Mol. Gen. Genet. (1985) 198:279-282 !$#title Cloning and nucleotide sequencing of the genes for ribosomal !1proteins S9 (rpsI) and L13 (rplM) of Escherichia coli. !$#cross-references MUID:85162987; PMID:3884974 !$#accession I57732 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-142 ##label ISO !'##cross-references EMBL:X02130; NID:g42854; PIDN:CAA26041.1; !1PID:g42855 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65115 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-142 ##label BLAT !'##cross-references GB:AE000402; GB:U00096; NID:g1789619; !1PIDN:AAC76263.1; PID:g1789626; UWGP:b3231 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note no post-translational modifications were observed in mass !1spectrographic analysis; any acid labile modifications may !1have been missed GENETICS !$#gene rplM !$#map_position 70 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX large subunit ribosomal proteins: L1 (PIR:R5EC1), L3 !1(PIR:R5EC3), L2 (PIR:R5EC2), L4 (PIR:R5EC4), L5 (PIR:R5EC5), !1L6 (PIR:R5EC6), L7/L12 (PIR:R5EC7), L9 (PIR:R5EC9), L10 !1(PIR:R5EC10), L11 (PIR:R5EC11), L13 (PIR:R5EC13), L14 !1(PIR:R5EC14), L15 (PIR:R5EC15), L16 (PIR:R5EC16), L17 !1(PIR:R5EC17), L18 (PIR:R5EC18), L19 (PIR:R5EC19) FUNCTION !$#pathway protein biosynthesis !$#note one of the early assembly proteins of the 50S ribosomal !1subunit CLASSIFICATION #superfamily Escherichia coli ribosomal protein L13 KEYWORDS protein biosynthesis; ribosome FEATURE !$1-142 #product ribosomal protein L13 #status experimental !8#label MAT SUMMARY #length 142 #molecular-weight 16018 #checksum 2283 SEQUENCE /// ENTRY G64123 #type complete TITLE ribosomal protein L13 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS G64123 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession G64123 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-142 ##label TIGR !'##cross-references GB:U32823; GB:L42023; NID:g1574281; !1PIDN:AAC23093.1; PID:g1574283; TIGR:HI1443 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L13 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 142 #molecular-weight 15978 #checksum 2271 SEQUENCE /// ENTRY A43310 #type complete TITLE ribosomal protein L13 homolog - Haemophilus somnus ORGANISM #formal_name Haemophilus somnus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A43310 REFERENCE A43310 !$#authors Theisen, M.; Potter, A.A. !$#journal J. Bacteriol. (1992) 174:17-23 !$#title Cloning, sequencing, expression, and functional studies of a !115,000-molecular-weight Haemophilus somnus antigen similar !1to Escherichia coli ribosomal protein S9. !$#cross-references MUID:92104958; PMID:1729207 !$#accession A43310 !'##molecule_type DNA !'##residues 1-142 ##label THE !'##cross-references GB:S75161; NID:g241865; PIDN:AAB20820.1; !1PID:g241866 !'##experimental_source HS25 !'##note this sequence is inconsistent with the nucleotide translation !'##note sequence extracted from NCBI backbone (NCBIN:75161, !1NCBIP:75164) CLASSIFICATION #superfamily Escherichia coli ribosomal protein L13 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 142 #molecular-weight 15948 #checksum 2810 SEQUENCE /// ENTRY S23063 #type complete TITLE ribosomal protein L13 - Staphylococcus carnosus ORGANISM #formal_name Staphylococcus carnosus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S23063 REFERENCE S23063 !$#authors Overhoff-Freundlieb, B.; Freudl, R. !$#journal FEMS Microbiol. Lett. (1991) 84:143-150 !$#title Suppression of an Escherichia coli secA(ts) mutant by a gene !1cloned from Staphylococcus carnosus. !$#accession S23063 !'##molecule_type DNA !'##residues 1-145 ##label OVE !'##cross-references EMBL:X63912; NID:g46911; PIDN:CAA45367.1; !1PID:g46912 !'##experimental_source strain TM300 GENETICS !$#gene rplM CLASSIFICATION #superfamily Escherichia coli ribosomal protein L13 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 145 #molecular-weight 16177 #checksum 1385 SEQUENCE /// ENTRY A32033 #type complete TITLE ribosomal protein L13 precursor, chloroplast - spinach ORGANISM #formal_name Spinacia oleracea #common_name spinach DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A32033; A30782; S17144 REFERENCE A32033 !$#authors Phua, S.H.; Srinivasa, B.R.; Subramanian, A.R. !$#journal J. Biol. Chem. (1989) 264:1968-1971 !$#title Chloroplast ribosomal protein L13 is encoded in the nucleus !1and is considerably larger than its bacterial homologue. !1Construction, immunoisolation, and nucleotide sequence !1(including transit peptide) of its cDNA clone from an !1angiosperm. !$#cross-references MUID:89123257; PMID:2644249 !$#accession A32033 !'##molecule_type mRNA !'##residues 1-250 ##label PHU !'##cross-references GB:J04461; NID:g170132; PIDN:AAA34040.1; !1PID:g170133 GENETICS !$#genome nuclear CLASSIFICATION #superfamily Escherichia coli ribosomal protein L13 KEYWORDS chloroplast; protein biosynthesis; ribosome; RNA binding SUMMARY #length 250 #molecular-weight 28163 #checksum 7649 SEQUENCE /// ENTRY B41715 #type complete TITLE ribosomal protein L13 [similarity] - Haloarcula marismortui ORGANISM #formal_name Haloarcula marismortui DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 21-Jul-2000 ACCESSIONS B41715 REFERENCE A41715 !$#authors Kroemer, W.J.; Arndt, E. !$#journal J. Biol. Chem. (1991) 266:24573-24579 !$#title Halobacterial S9 operon. Three ribosomal protein genes are !1cotranscribed with genes encoding a tRNA(leu), the enolase, !1and a putative membrane protein in the archaebacterium !1Haloarcula (halobacterium) marismortui. !$#cross-references MUID:92105119; PMID:1840597 !$#accession B41715 !'##status preliminary !'##molecule_type DNA !'##residues 1-145 ##label KRO !'##cross-references GB:M76567; NID:g148775; PIDN:AAA73097.1; !1PID:g148777 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L13 SUMMARY #length 145 #molecular-weight 16228 #checksum 9222 SEQUENCE /// ENTRY A53204 #type complete TITLE ribosomal protein L13a, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 21-Jul-2000 ACCESSIONS A53204 REFERENCE A53204 !$#authors Chan, Y.L.; Olvera, J.; Glueck, A.; Wool, I.G. !$#journal J. Biol. Chem. (1994) 269:5589-5594 !$#title A leucine zipper-like motif and a basic region-leucine !1zipper-like element in rat ribosomal protein L13a. !1Identification of the tum-transplantation antigen P198. !$#cross-references MUID:94164901; PMID:8119894 !$#accession A53204 !'##molecule_type mRNA !'##residues 1-203 ##label CHA !'##cross-references GB:X68282; NID:g460775; PIDN:CAA48343.1; !1PID:g460776 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing !'##note the protein is designated as ribosomal protein L13a CLASSIFICATION #superfamily Escherichia coli ribosomal protein L13 FEATURE !$2-203 #product ribosomal protein L13a #status experimental !8#label MAT SUMMARY #length 203 #molecular-weight 23476 #checksum 9977 SEQUENCE /// ENTRY R5TE14 #type complete TITLE ribosomal protein L14 - Tetrahymena pyriformis mitochondrion ORGANISM #formal_name mitochondrion Tetrahymena pyriformis DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 07-Dec-1999 ACCESSIONS S03434 REFERENCE S03434 !$#authors Suyama, Y.; Jenney, F. !$#journal Nucleic Acids Res. (1989) 17:803 !$#title The tRNA(glu) (anticodon TTU) gene and its upstream sequence !1coding for a homolog of the E. coli large ribosome-subunit !1protein L14 in the Tetrahymena mitochondrial genome. !$#cross-references MUID:89128455; PMID:2915933 !$#accession S03434 !'##status translation not shown !'##molecule_type DNA !'##residues 1-119 ##label SUY !'##cross-references EMBL:X13117; NID:g13856; PIDN:CAA31509.1; !1PID:g13857 GENETICS !$#genome mitochondrion !$#genetic_code SGC6 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L14 KEYWORDS mitochondrion; protein biosynthesis; ribosome FEATURE !$1-119 #product ribosomal protein L14 #status predicted !8#label MAT SUMMARY #length 119 #molecular-weight 13625 #checksum 9882 SEQUENCE /// ENTRY R5PP14 #type complete TITLE ribosomal protein L14 - Paramecium tetraurelia mitochondrion ORGANISM #formal_name mitochondrion Paramecium tetraurelia DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 07-Dec-1999 ACCESSIONS S07753 REFERENCE S07725 !$#authors Pritchard, A.E.; Seilhamer, J.J.; Mahalingam, R.; Sable, !1C.L.; Venuti, S.E.; Cummings, D.J. !$#journal Nucleic Acids Res. (1990) 18:173-180 !$#title Nucleotide sequence of the mitochondrial genome of !1Paramecium. !$#cross-references MUID:90174913; PMID:2308823 !$#accession S07753 !'##status translation not shown !'##molecule_type DNA !'##residues 1-119 ##label PRI !'##cross-references EMBL:X15917; NID:g13256; PIDN:CAA34032.1; !1PID:g13285 GENETICS !$#gene rpl14 !$#genome mitochondrion !$#genetic_code SGC6 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L14 KEYWORDS mitochondrion; protein biosynthesis; ribosome FEATURE !$1-119 #product ribosomal protein L14 #status predicted !8#label MAT SUMMARY #length 119 #molecular-weight 13642 #checksum 4983 SEQUENCE /// ENTRY R5EC14 #type complete TITLE ribosomal protein L14 [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-May-1979 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS A65124; A02788; B30421; S40640; S40639 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65124 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-123 ##label BLAT !'##cross-references GB:AE000408; GB:U00096; NID:g1789694; !1PIDN:AAC76335.1; PID:g1789706; UWGP:b3310 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A02788 !$#authors Morinaga, T.; Funatsu, G.; Funatsu, M.; Wittmann-Liebold, !1B.; Wittmann, H.G. !$#journal FEBS Lett. (1978) 91:74-77 !$#title Primary structure of protein L14 isolated from Escherichia !1coli ribosomes. !$#cross-references MUID:78215057; PMID:352727 !$#accession A02788 !'##molecule_type protein !'##residues 1-62,64-83,'S',85-89,'TD',92-96,98-114,'L',116-122 ##label !1MOR !'##experimental_source strain K REFERENCE A30421 !$#authors Post, L.E.; Arfsten, A.E.; Reusser, F.; Nomura, M. !$#journal Cell (1978) 15:215-229 !$#title DNA sequences of promoter region for the str and spc !1ribosomal protein operons in E. coli. !$#cross-references MUID:79023059; PMID:151587 !$#accession B30421 !'##molecule_type DNA !'##residues 1-20 ##label POS !'##cross-references GB:V00357; GB:J01686; NID:g43015; PIDN:CAA23653.1; !1PID:g43017 REFERENCE S40639 !$#authors Yancey, J.E.; Matson, S.W. !$#journal Nucleic Acids Res. (1991) 19:3943-3951 !$#title The DNA unwinding reaction catalyzed by Rep protein is !1facilitated by an RHSP-DNA interaction. !$#cross-references MUID:91319555; PMID:1650456 !$#accession S40640 !'##molecule_type protein !'##residues 1-20 ##label YAN !$#accession S40639 !'##molecule_type protein !'##residues 'X',2-16,'IX',19-20 ##label YA2 REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note no post-translational modifications were observed in mass !1spectrographic analysis; any acid labile modifications may !1have been missed GENETICS !$#gene rplN !$#map_position 73 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX large subunit ribosomal proteins: L1 (PIR:R5EC1), L3 !1(PIR:R5EC3), L2 (PIR:R5EC2), L4 (PIR:R5EC4), L5 (PIR:R5EC5), !1L6 (PIR:R5EC6), L7/L12 (PIR:R5EC7), L9 (PIR:R5EC9), L10 !1(PIR:R5EC10), L11 (PIR:R5EC11), L13 (PIR:R5EC13), L14 !1(PIR:R5EC14), L15 (PIR:R5EC15), L16 (PIR:R5EC16), L17 !1(PIR:R5EC17), L18 (PIR:R5EC18), L19 (PIR:R5EC19) FUNCTION !$#pathway protein biosynthesis !$#note binds 23S rRNA CLASSIFICATION #superfamily Escherichia coli ribosomal protein L14 KEYWORDS protein biosynthesis; ribosome; RNA binding FEATURE !$1-122 #product ribosomal protein L14 #status experimental !8#label MAT SUMMARY #length 123 #molecular-weight 13541 #checksum 5160 SEQUENCE /// ENTRY R5BS14 #type complete TITLE ribosomal protein L14 - Bacillus stearothermophilus ORGANISM #formal_name Bacillus stearothermophilus DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 07-May-1999 ACCESSIONS A02789; S59062 REFERENCE A91149 !$#authors Kimura, M.; Kimura, J.; Ashman, K. !$#journal Eur. J. Biochem. (1985) 150:491-497 !$#title The complete primary structure of ribosomal proteins L1, !1L14, L15, L23, L24, and L29 from Bacillus !1stearothermophilus. !$#cross-references MUID:85257681; PMID:4018095 !$#accession A02789 !'##molecule_type protein !'##residues 1-122 ##label KIM REFERENCE S59051 !$#authors Urlaub, H.; Kruft, V.; Bischof, O.; Mueller, E.C.; !1Wittmann-Liebold, B. !$#journal EMBO J. (1995) 14:4578-4588 !$#title Protein-rRNA binding features and their structural and !1functional implications in ribosomes as determined by !1cross-linking studies. !$#cross-references MUID:96003638; PMID:7556101 !$#accession S59062 !'##molecule_type protein !'##residues 24-35 ##label URL CLASSIFICATION #superfamily Escherichia coli ribosomal protein L14 KEYWORDS protein biosynthesis; ribosome FEATURE !$1-120 #product ribosomal protein L14 #status predicted !8#label MAT SUMMARY #length 122 #molecular-weight 13345 #checksum 5110 SEQUENCE /// ENTRY R5BS4B #type complete TITLE ribosomal protein L14 - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jun-2000 ACCESSIONS S05992; H69695 REFERENCE S05989 !$#authors Henkin, T.M.; Moon, S.H.; Mattheakis, L.C.; Nomura, M. !$#journal Nucleic Acids Res. (1989) 17:7469-7486 !$#title Cloning and analysis of the spc ribosomal protein operon of !1Bacillus subtilis: comparison with the spc operon of !1Escherichia coli. !$#cross-references MUID:90016806; PMID:2508062 !$#accession S05992 !'##molecule_type DNA !'##residues 1-122 ##label HEN !'##cross-references EMBL:X15664; NID:g40146; PIDN:CAA33701.1; !1PID:g40150 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69695 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-122 ##label KUN !'##cross-references GB:Z99104; GB:AL009126; NID:g2632267; !1PIDN:CAB11902.1; PID:g2632393 !'##experimental_source strain 168 GENETICS !$#gene rplN CLASSIFICATION #superfamily Escherichia coli ribosomal protein L14 KEYWORDS protein biosynthesis; ribosome FEATURE !$1-122 #product ribosomal protein L14 #status predicted !8#label MAT SUMMARY #length 122 #molecular-weight 13154 #checksum 4694 SEQUENCE /// ENTRY R5YM14 #type complete TITLE ribosomal protein L14 - Mycoplasma capricolum ORGANISM #formal_name Mycoplasma capricolum DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 07-Dec-1999 ACCESSIONS S02841 REFERENCE S02830 !$#authors Ohkubo, S.; Muto, A.; Kawauchi, Y.; Yamao, F.; Osawa, S. !$#journal Mol. Gen. Genet. (1987) 210:314-322 !$#title The ribosomal protein gene cluster of Mycoplasma capricolum. !$#cross-references MUID:88142549; PMID:3481422 !$#accession S02841 !'##molecule_type DNA !'##residues 1-122 ##label OHK !'##cross-references EMBL:X06414; NID:g44207; PIDN:CAA29714.1; !1PID:g44219 GENETICS !$#gene rpl14 !$#genetic_code SGC3 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L14 KEYWORDS protein biosynthesis; ribosome FEATURE !$1-122 #product ribosomal protein L14 #status predicted !8#label MAT SUMMARY #length 122 #molecular-weight 13148 #checksum 946 SEQUENCE /// ENTRY R5LV14 #type complete TITLE ribosomal protein L14, chloroplast - liverwort (Marchantia polymorpha) chloroplast ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 22-Jun-1999 ACCESSIONS A02790; S01560 REFERENCE A00150 !$#authors Ohyama, K. !$#submission submitted to the EMBL Data Library, October 1986 !$#accession A02790 !'##molecule_type DNA !'##residues 1-122 ##label OHY REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features REFERENCE S01529 !$#authors Fukuzawa, H.; Kohchi, T.; Sano, T.; Shirai, H.; Umesono, K.; !1Inokuchi, H.; Ozeki, H.; Ohyama, K. !$#journal J. Mol. Biol. (1988) 203:333-351 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. III. Gene organization of the large !1single copy region from rbcL to trnI(CAU). !$#cross-references MUID:89068687; PMID:3199436 !$#accession S01560 !'##molecule_type DNA !'##residues 1-122 ##label FUK !'##cross-references GB:X04465; GB:Y00686; NID:g11640; PIDN:CAA28122.1; !1PID:g11711 GENETICS !$#gene rpl14 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein L14 KEYWORDS chloroplast; protein biosynthesis; ribosome FEATURE !$1-122 #product ribosomal protein L14 #status predicted !8#label MAT SUMMARY #length 122 #molecular-weight 13497 #checksum 3422 SEQUENCE /// ENTRY R5NT14 #type complete TITLE ribosomal protein L14 - common tobacco chloroplast ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 22-Nov-1996 ACCESSIONS A02791; G25943 REFERENCE A00149 !$#authors Sugiura, M. !$#submission submitted to the EMBL Data Library, August 1986 !$#accession A02791 !'##molecule_type DNA !'##residues 1-123 ##label SUG !'##experimental_source cv. Bright Yellow 4 REFERENCE A38013 !$#authors Shinozaki, K.; Ohme, M.; Tanaka, M.; Wakasugi, T.; !1Hayashida, N.; Matsubayashi, T.; Zaita, N.; Chunwongse, J.; !1Obokata, J.; Yamaguchi-Shinozaki, K.; Ohto, C.; Torazawa, !1K.; Meng, B.Y.; Sugita, M.; Deno, H.; Kamogashira, T.; !1Yamada, K.; Kusuda, J.; Takaiwa, F.; Kato, A.; Tohdoh, N.; !1Shimada, H.; Sugiura, M. !$#journal EMBO J. (1986) 5:2043-2049 !$#title The complete nucleotide sequence of the tobacco chloroplast !1genome: its gene organization and expression. !$#contents annotation; gene organization, sites, features REFERENCE A94118 !$#authors Tanaka, M.; Wakasugi, T.; Sugita, M.; Shinozaki, K.; !1Sugiura, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:6030-6034 !$#title Genes for the eight ribosomal proteins are clustered on the !1chloroplast genome of tobacco (Nicotiana tabacum): !1similarity to the S10 and spc operons of Escherichia coli. !$#cross-references MUID:86287388; PMID:3016736 !$#accession G25943 !'##molecule_type DNA !'##residues 1-123 ##label TAN GENETICS !$#gene rpl14 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein L14 KEYWORDS chloroplast; protein biosynthesis; ribosome FEATURE !$1-123 #product ribosomal protein L14 #status predicted !8#label MAT SUMMARY #length 123 #molecular-weight 13738 #checksum 3361 SEQUENCE /// ENTRY R5SP14 #type complete TITLE ribosomal protein L14, chloroplast - spinach chloroplast ALTERNATE_NAMES ribosomal protein CS-L29 ORGANISM #formal_name chloroplast Spinacia oleracea #common_name spinach DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S01980; S20560 REFERENCE S01976 !$#authors Zhou, D.X.; Quigley, F.; Massenet, O.; Mache, R. !$#journal Mol. Gen. Genet. (1989) 216:439-445 !$#title Cotranscription of the S10- and spc-like operons in spinach !1chloroplasts and identification of three of their gene !1products. !$#cross-references MUID:89313684; PMID:2747623 !$#accession S01980 !'##molecule_type DNA !'##residues 1-122 ##label ZHO !'##cross-references EMBL:X13336; NID:g12307; PIDN:CAA31717.1; !1PID:g12312 !$#accession S20560 !'##molecule_type protein !'##residues 1-16 ##label ZHO2 GENETICS !$#gene rpl14 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein L14 KEYWORDS chloroplast; protein biosynthesis; ribosome FEATURE !$1-122 #product ribosomal protein L14 #status experimental !8#label MAT SUMMARY #length 122 #molecular-weight 13564 #checksum 1723 SEQUENCE /// ENTRY R5RZ14 #type complete TITLE ribosomal protein L14, chloroplast - rice chloroplast ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 22-Jun-1999 ACCESSIONS JQ0263; S05143 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0263 !'##molecule_type DNA !'##residues 1-123 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05143 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-123 ##label HIR !'##cross-references GB:X15901; NID:g11957; PIDN:CAA33932.1; PID:g12023 !'##experimental_source cv. Nihonbare !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1989 GENETICS !$#gene rpl14 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein L14 KEYWORDS chloroplast; protein biosynthesis; ribosome FEATURE !$1-123 #product ribosomal protein L14 #status predicted !8#label MAT SUMMARY #length 123 #molecular-weight 13565 #checksum 2338 SEQUENCE /// ENTRY R5ZM14 #type complete TITLE ribosomal protein L14, chloroplast - maize chloroplast ORGANISM #formal_name chloroplast Zea mays #common_name maize DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S00279; S58588 REFERENCE S00278 !$#authors Markmann-Mulisch, U.; Subramanian, A.R. !$#journal Eur. J. Biochem. (1988) 170:507-514 !$#title Nucleotide sequence and linkage map position of the genes !1for ribosomal proteins L14 and S8 in the maize chloroplast !1genome. !$#cross-references MUID:88111635; PMID:2828044 !$#accession S00279 !'##molecule_type DNA !'##residues 1-123 ##label MAR !'##cross-references EMBL:X06734; NID:g12451; PIDN:CAA29912.1; !1PID:g12453 REFERENCE S58531 !$#authors Maier, R.M.; Neckermann, K.; Igloi, G.L.; Koessel, H. !$#journal J. Mol. Biol. (1995) 251:614-628 !$#title Complete sequence of the maize chloroplast genome: gene !1content, hotspots of divergence and fine tuning of genetic !1information by transcript editing. !$#cross-references MUID:95395841; PMID:7666415 !$#accession S58588 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-123 ##label MAI !'##cross-references EMBL:X86563; NID:g902200; PIDN:CAA60322.1; !1PID:g902258 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1995 GENETICS !$#gene rpl14 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein L14 KEYWORDS chloroplast; protein biosynthesis; ribosome FEATURE !$1-123 #product ribosomal protein L14 #status predicted !8#label MAT SUMMARY #length 123 #molecular-weight 13494 #checksum 2579 SEQUENCE /// ENTRY R5KM14 #type complete TITLE ribosomal protein L14, chloroplast - Chlamydomonas reinhardtii chloroplast ORGANISM #formal_name chloroplast Chlamydomonas reinhardtii DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S04093 REFERENCE S04093 !$#authors Lou, J.K.; Cruz, F.D.; Wu, M. !$#journal Nucleic Acids Res. (1989) 17:3587 !$#title Nucleotide sequence of the chloroplast ribosomal protein !1gene L14 in Chlamydomonas reinhardtii. !$#cross-references MUID:89263799; PMID:2726491 !$#accession S04093 !'##molecule_type DNA !'##residues 1-122 ##label LOU !'##cross-references EMBL:X14062; NID:g11432; PIDN:CAA32226.1; !1PID:g11433 GENETICS !$#gene rpl14 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein L14 KEYWORDS chloroplast; protein biosynthesis; ribosome FEATURE !$1-122 #product ribosomal protein L14 #status predicted !8#label MAT SUMMARY #length 122 #molecular-weight 13446 #checksum 2662 SEQUENCE /// ENTRY R5KT14 #type complete TITLE ribosomal protein L14, cyanelle - Cyanophora paradoxa cyanelle ORGANISM #formal_name cyanelle Cyanophora paradoxa DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 21-Jan-2000 ACCESSIONS S12215; T06881 REFERENCE S12211 !$#authors Michalowski, C.B.; Pfanzagl, B.; Loeffelhardt, W.; Bohnert, !1H.J. !$#journal Mol. Gen. Genet. (1990) 224:222-231 !$#title The cyanelle S10 spc ribosomal protein gene operon from !1Cyanophora paradoxa. !$#cross-references MUID:91117189; PMID:2126059 !$#accession S12215 !'##molecule_type DNA !'##residues 1-122 ##label MIC !'##cross-references GB:M30487; NID:g336645; PIDN:AAA63624.1; !1PID:g336650 !'##experimental_source strain LB555 UTEX REFERENCE Z15840 !$#authors Stirewalt, V.L.; Michalowski, C.B.; Luffelhardt, W.; !1Bohnert, H.J.; Bryant, D.A. !$#submission submitted to the EMBL Data Library, July 1995 !$#description Nucleotide sequence of the cyanelle genome from Cyanophora !1paradoxa. !$#accession T06881 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-122 ##label STI !'##cross-references EMBL:U30821; NID:g1016083; PIDN:AAA81224.1; !1PID:g1016137 !'##experimental_source strain Pringsheim LB555 GENETICS !$#gene rpl14 !$#genome cyanelle CLASSIFICATION #superfamily Escherichia coli ribosomal protein L14 KEYWORDS cyanelle; protein biosynthesis; ribosome FEATURE !$1-122 #product ribosomal protein L14 #status predicted !8#label MAT SUMMARY #length 122 #molecular-weight 13361 #checksum 3310 SEQUENCE /// ENTRY R5EG14 #type complete TITLE ribosomal protein L14, chloroplast - Euglena gracilis chloroplast ORGANISM #formal_name chloroplast Euglena gracilis DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 22-Jun-1999 ACCESSIONS S09287; S34527; S34894 REFERENCE S09286 !$#authors Christopher, D.A.; Hallick, R.B. !$#journal Nucleic Acids Res. (1989) 17:7591-7608 !$#title Euglena gracilis chloroplast ribosomal protein operon: a new !1chloroplast gene for ribosomal protein L5 and description of !1a novel organelle intron category designated group III. !$#cross-references MUID:90016846; PMID:2477800 !$#accession S09287 !'##molecule_type DNA !'##residues 1-121 ##label CHR !'##cross-references EMBL:Z11874; NID:g14353; PIDN:CAA77923.1; !1PID:g14373 !'##experimental_source strain Z REFERENCE S34494 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.; Monfort, !1A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#submission submitted to the EMBL Data Library, January 1993 !$#description The complete sequence of the Euglena gracilis chloroplast !1genome (tentative). !$#accession S34527 !'##molecule_type DNA !'##residues 1-121 ##label HAL1 !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50106.1; !1PID:g415762 REFERENCE S34862 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.R.; !1Monfort, A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#journal Nucleic Acids Res. (1993) 21:3537-3544 !$#title Complete sequence of Euglena gracilis chloroplast DNA. !$#cross-references MUID:93347989; PMID:8346031 !$#accession S34894 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-121 ##label HAL2 !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50106.1; !1PID:g415762 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1993 GENETICS !$#gene rpl14 !$#genome chloroplast !$#introns 43/3 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L14 KEYWORDS chloroplast; protein biosynthesis; ribosome FEATURE !$1-121 #product ribosomal protein L14 #status predicted !8#label MAT SUMMARY #length 121 #molecular-weight 13421 #checksum 1840 SEQUENCE /// ENTRY R5HU23 #type complete TITLE ribosomal protein L23 - human ALTERNATE_NAMES ribosomal protein HL17a ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1991 #sequence_revision 31-Mar-1993 #text_change 22-Jun-1999 ACCESSIONS S18815; S25094; S11630 REFERENCE S18815 !$#authors Berchtold, M.W.; Berger, M.C. !$#journal Gene (1991) 102:283-288 !$#title Isolation and analysis of a human cDNA highly homologous to !1the yeast gene encoding L17A ribosomal protein. !$#cross-references MUID:91340166; PMID:1874450 !$#accession S18815 !'##molecule_type mRNA !'##residues 1-140 ##label BER !'##cross-references EMBL:X55954 REFERENCE S22989 !$#authors Herault, Y.; Michel, D.; Chatelain, G.; Brun, G. !$#journal Nucleic Acids Res. (1991) 19:4001 !$#title cDNA and predicted amino acid sequences of the human !1ribosomal protein genes rpS12 and rpL17. !$#cross-references MUID:91319568; PMID:1861993 !$#accession S25094 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type mRNA !'##residues 1-135,'A',137-139,'A' ##label HER !'##cross-references EMBL:X52839; NID:g36125; PIDN:CAA37023.1; !1PID:g36126 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1May 1990 GENETICS !$#gene GDB:RPL17 !'##cross-references GDB:128738 !$#map_position 1p31-1p31 !$#note the GDB name for this gene is ribosomal protein L17 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L14 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 140 #molecular-weight 15036 #checksum 7838 SEQUENCE /// ENTRY R5RT23 #type complete TITLE ribosomal protein L23, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 21-Jul-2000 ACCESSIONS JH0418; S14633 REFERENCE JH0418 !$#authors Chan, Y.L.; Paz, V.; Wool, I.G. !$#journal Biochem. Biophys. Res. Commun. (1991) 178:1153-1159 !$#title The primary structure of rat ribosomal protein L23. !$#cross-references MUID:91337053; PMID:1840488 !$#accession JH0418 !'##molecule_type mRNA !'##residues 1-140 ##label CHA !'##cross-references GB:X58200; NID:g57687; PIDN:CAA41177.1; PID:g57688 !'##note the protein is designated as ribosomal protein L23 according to !1comigration analysis after in vitro translation CLASSIFICATION #superfamily Escherichia coli ribosomal protein L14 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 140 #molecular-weight 14865 #checksum 7022 SEQUENCE /// ENTRY R5BY17 #type complete TITLE ribosomal protein L23.e, cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YBL0713; protein YBL087c; protein YER117w; ribosomal protein YL17a ORGANISM #formal_name Saccharomyces cerevisiae DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 23-Mar-2001 ACCESSIONS A02792; S45418; S45828; S50620; S57256; S59215 REFERENCE A93532 !$#authors Leer, R.J.; van Raamsdonk-Duin, M.M.C.; Hagendoorn, M.J.M.; !1Mager, W.H.; Planta, R.J. !$#journal Nucleic Acids Res. (1984) 12:6685-6700 !$#title Structural comparison of yeast ribosomal protein genes. !$#cross-references MUID:85014125; PMID:6091033 !$#accession A02792 !'##molecule_type DNA !'##residues 1-137 ##label LEE !'##cross-references EMBL:X01694; NID:g4323; PIDN:CAA25841.1; PID:g4324 !'##genetics CH2 REFERENCE S45387 !$#authors Obermaier, B.; Gassenhuber, J.; Piravandi, E.; Domdey, H. !$#submission submitted to the EMBL Data Library, May 1994 !$#description Sequence analysis of a 78,6 kb segment of the left end of !1Saccaromyces cerevisiae chromosome II. !$#accession S45418 !'##molecule_type DNA !'##residues 1-137 ##label OBE !'##cross-references EMBL:X79489; NID:g496661; PIDN:CAA56018.1; !1PID:g496691 !'##genetics CH2 REFERENCE S45816 !$#authors Domdey, H.; Gassenhuber, H.; Obermaier, B.; Piravandi, E. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S45828 !'##molecule_type DNA !'##residues 1-137 ##label DOM !'##cross-references EMBL:Z35848; GSPDB:GN00002; MIPS:YBL087c; !1NID:g536141; PIDN:CAA84908.1; PID:g536142 !'##genetics CH2 REFERENCE S50437 !$#authors Dietrich, F.S. !$#submission submitted to the EMBL Data Library, December 1994 !$#description The sequence of S. cerevisiae cosmids 9781, 8198, 9115, !19981, and lambda clones 3955 and 6052. !$#accession S50620 !'##molecule_type DNA !'##residues 1-137 ##label DIE !'##cross-references EMBL:U18916; NID:g1384128; PIDN:AAC03215.1; !1PID:g603356; GSPDB:GN00005; MIPS:YER117w !'##genetics CH5 REFERENCE S57256 !$#authors Berroteran, R.W.; Hampsey, M. !$#journal Yeast (1995) 11:761-766 !$#title Sequence, map position and genome organization of the RPL17B !1gene, encoding ribosomal protein L17b in Saccharomyces !1cerevisiae. !$#cross-references MUID:95397593; PMID:7668045 !$#accession S57256 !'##molecule_type DNA !'##residues 1-137 ##label BER !'##cross-references EMBL:U15653; NID:g642467; PIDN:AAA61906.1; !1PID:g622952 !'##genetics CH5 REFERENCE S59184 !$#authors Obermaier, B.; Gassenhuber, J.; Piravandi, E.; Domdey, H. !$#journal Yeast (1995) 11:1103-1112 !$#title Sequence analysis of a 78.6 kb segment of the left end of !1Saccharomyces cerevisiae chromosome II. !$#cross-references MUID:96076635; PMID:7502586 !$#accession S59215 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-137 ##label OBW !'##cross-references EMBL:X79489; NID:g496661; PIDN:CAA56018.1; !1PID:g496691 !'##genetics CH2 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1May 1994 GENETICS CH2 !$#gene SGD:RPL17A; MIPS:YBL087c !'##cross-references MIPS:YBL087c; SGD:S0000183 !$#map_position 2L !$#introns 14/3 GENETICS CH5 !$#gene SGD:RPL17b; MIPS:YER117w !'##cross-references MIPS:YER117w; SGD:S0000919 !$#map_position 5R !$#introns 14/3 !$#note YER117w CLASSIFICATION #superfamily Escherichia coli ribosomal protein L14 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 137 #molecular-weight 14473 #checksum 954 SEQUENCE /// ENTRY R5MX14 #type complete TITLE ribosomal protein L14 - Methanococcus vannielii ORGANISM #formal_name Methanococcus vannielii DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 22-Jun-1999 ACCESSIONS S05614 REFERENCE S05611 !$#authors Auer, J.; Spicker, G.; Boeck, A. !$#journal J. Mol. Biol. (1989) 209:21-36 !$#title Organization and structure of the Methanococcus !1transcriptional unit homologous to the Escherichia coli !1"spectinomycin operon". Implications for the evolutionary !1relationship of 70 S and 80 S ribosomes. !$#cross-references MUID:90040717; PMID:2530355 !$#accession S05614 !'##molecule_type DNA !'##residues 1-132 ##label AUE !'##cross-references EMBL:X16720; NID:g44754; PIDN:CAA34690.1; !1PID:g44758 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L14 KEYWORDS protein biosynthesis; ribosome FEATURE !$1-132 #product ribosomal protein L14 #status predicted !8#label MAT SUMMARY #length 132 #molecular-weight 14205 #checksum 7668 SEQUENCE /// ENTRY R5HS14 #type complete TITLE ribosomal protein L14 [similarity] - Haloarcula marismortui ALTERNATE_NAMES ribosomal protein HL27; ribosomal protein HmaL14 ORGANISM #formal_name Haloarcula marismortui DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 31-Mar-2000 ACCESSIONS S10734; T46797 REFERENCE S10731 !$#authors Arndt, E. !$#journal FEBS Lett. (1990) 267:193-198 !$#title Nucleotide sequence of four genes encoding ribosomal !1proteins from the 'S10 and spectinomycin' operon equivalent !1region in the archaebacterium Halobacterium marismortui. !$#cross-references MUID:90336772; PMID:2143141 !$#accession S10734 !'##molecule_type DNA !'##residues 1-132 ##label ARN !'##cross-references EMBL:X55311; NID:g43610; PIDN:CAA39018.1; !1PID:g43614 !'##note the source is designated as Halobacterium marismortui CLASSIFICATION #superfamily Escherichia coli ribosomal protein L14 KEYWORDS protein biosynthesis; ribosome FEATURE !$1-132 #product ribosomal protein L14 #status predicted !8#label MAT SUMMARY #length 132 #molecular-weight 14193 #checksum 4290 SEQUENCE /// ENTRY T43826 #type complete TITLE ribosomal protein L14 [similarity] - Halobacterium salinarum ORGANISM #formal_name Halobacterium salinarum DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 21-Jul-2000 ACCESSIONS T43826 REFERENCE Z22697 !$#authors Itoh, T. !$#submission submitted to the EMBL Data Library, September 1997 !$#accession T43826 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-132 ##label ITO !'##cross-references EMBL:AB006961; PIDN:BAA22280.1 !'##note the source is designated as Halobacterium halobium GENETICS !$#note HhaL14 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L14 SUMMARY #length 132 #molecular-weight 14375 #checksum 5171 SEQUENCE /// ENTRY R5RT81 #type complete TITLE ribosomal protein L18, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 21-Jul-2000 ACCESSIONS A29906; A34988; S11418 REFERENCE A29906 !$#authors Devi, K.R.G.; Chan, Y.L.; Wool, I.G. !$#journal DNA (1988) 7:157-162 !$#title The primary structure of rat ribosomal protein L18. !$#cross-references MUID:88224560; PMID:3371159 !$#accession A29906 !'##molecule_type mRNA !'##residues 1-188 ##label DEV !'##cross-references EMBL:M20156; NID:g206723; PIDN:AAA42070.1; !1PID:g206724 !$#accession A34988 !'##molecule_type protein !'##residues 2-36 ##label DEV2 !'##note the protein is designated as ribosomal protein L18 REFERENCE S11413 !$#authors Wittmann-Liebold, B.; Geissler, A.W.; Lin, A.; Wool, I.G. !$#journal J. Supramol. Struct. (1979) 12:425-433 !$#title Sequence of the amino-terminal region of rat liver ribosomal !1proteins S4, S6, S8, L6, L7a, L18, L27, L30, L37, L37a, and !1L39. !$#cross-references MUID:80252792; PMID:398910 !$#accession S11418 !'##molecule_type protein !'##residues 2-9,'ES',12-13,'S',15-16,'L',18-19,'L' ##label WIT !'##note the protein is designated as ribosomal protein L18 CLASSIFICATION #superfamily rat ribosomal protein L18 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-188 #product ribosomal protein L18 #status experimental !8#label MAT SUMMARY #length 188 #molecular-weight 21658 #checksum 8917 SEQUENCE /// ENTRY JN0779 #type complete TITLE ribosomal protein L18 - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 03-Feb-1994 #sequence_revision 03-Feb-1994 #text_change 22-Jun-1999 ACCESSIONS JN0779 REFERENCE JN0778 !$#authors Hou, E.W.; Li, S.S.L. !$#journal Gene (1993) 130:287-290 !$#title Sequence analysis of mouse cDNAs encoding ribosomal proteins !1L12 and L18. !$#cross-references MUID:93366188; PMID:8359697 !$#accession JN0779 !'##molecule_type mRNA !'##residues 1-188 ##label HOU !'##cross-references GB:L04128; NID:g398049; PIDN:AAA40067.1; !1PID:g398050 GENETICS !$#gene L18 CLASSIFICATION #superfamily rat ribosomal protein L18 KEYWORDS protein biosynthesis; ribosome; RNA binding SUMMARY #length 188 #molecular-weight 21598 #checksum 1741 SEQUENCE /// ENTRY R5XL8A #type complete TITLE ribosomal protein L18.a - African clawed frog ALTERNATE_NAMES ribosomal protein XL14a ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 22-Jun-1999 ACCESSIONS A25766 REFERENCE A25766 !$#authors Beccari, E.; Mazzetti, P.; Mileo, A.; Bozzoni, I.; !1Pierandrei-Amaldi, P.; Amaldi, F. !$#journal Nucleic Acids Res. (1986) 14:7633-7646 !$#title Sequences coding for the ribosomal protein L14 in Xenopus !1laevis and Xenopus tropicalis; homologies in the 5' !1untranslated region are shared with other r-protein mRNAs. !$#cross-references MUID:87040730; PMID:3774540 !$#accession A25766 !'##molecule_type mRNA !'##residues 1-188 ##label BEC !'##cross-references GB:X06222; NID:g65069; PIDN:CAA29570.1; PID:g65070 GENETICS !$#introns 1/3; 30/3; 66/3; 99/3; 141/1; 164/2 CLASSIFICATION #superfamily rat ribosomal protein L18 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 188 #molecular-weight 21634 #checksum 7180 SEQUENCE /// ENTRY R5XL14 #type complete TITLE ribosomal protein L18.b - African clawed frog ALTERNATE_NAMES ribosomal protein XL14b ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 17-Dec-1982 #sequence_revision 31-Mar-1992 #text_change 21-Jul-2000 ACCESSIONS B25766; A02793; S54388 REFERENCE A25766 !$#authors Beccari, E.; Mazzetti, P.; Mileo, A.; Bozzoni, I.; !1Pierandrei-Amaldi, P.; Amaldi, F. !$#journal Nucleic Acids Res. (1986) 14:7633-7646 !$#title Sequences coding for the ribosomal protein L14 in Xenopus !1laevis and Xenopus tropicalis; homologies in the 5' !1untranslated region are shared with other r-protein mRNAs. !$#cross-references MUID:87040730; PMID:3774540 !$#accession B25766 !'##molecule_type mRNA !'##residues 1-188 ##label BEC !'##cross-references GB:X06223; NID:g65071; PIDN:CAB40827.1; !1PID:g4584831 REFERENCE A91492 !$#authors Amaldi, F.; Beccari, E.; Bozzoni, I.; Luo, Z.X.; !1Pierandrei-Amaldi, P. !$#journal Gene (1982) 17:311-316 !$#title Nucleotide sequences of cloned cDNA fragments specific for !1six Xenopus laevis ribosomal proteins. !$#cross-references MUID:82262793; PMID:7049839 !$#accession A02793 !'##molecule_type mRNA !'##residues 'DI',35-156,'G',158-188 ##label AMA !'##cross-references GB:V01439; GB:J00994; NID:g65046; PIDN:CAA24700.1; !1PID:g65047 REFERENCE S54388 !$#authors Beccari, E.; Mazzetti, P. !$#journal Nucleic Acids Res. (1987) 15:1870-1872 !$#title The nucleotide sequence of the ribosomal protein L14 gene of !1Xenopus laevis. !$#cross-references MUID:87146501; PMID:3822843 !$#accession S54388 !'##status translation not shown !'##molecule_type DNA !'##residues 1-84,'C',86-155,'LG',158-188 ##label BE2 !'##cross-references EMBL:X05025; NID:g65067; PIDN:CAA28689.1; !1PID:g65068 GENETICS !$#introns 1/3; 30/3; 66/3; 99/3; 141/1; 164/2 CLASSIFICATION #superfamily rat ribosomal protein L18 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 188 #molecular-weight 21757 #checksum 7388 SEQUENCE /// ENTRY R5ON18 #type complete TITLE ribosomal protein L18 - Atlantic salmon ORGANISM #formal_name Salmo salar #common_name Atlantic salmon DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 22-Jun-1999 ACCESSIONS JQ1003; S18829 REFERENCE JQ1003 !$#authors Powell, R.; Byrnes, L.; Gannon, F. !$#journal Gene (1991) 101:303-304 !$#title Sequence of a cDNA clone encoding an Atlantic salmon !1ribosomal protein. !$#cross-references MUID:91276288; PMID:2055494 !$#accession JQ1003 !'##molecule_type mRNA !'##residues 1-179 ##label POW !'##cross-references EMBL:X52238; NID:g64373; PIDN:CAA36483.1; !1PID:g64374 CLASSIFICATION #superfamily rat ribosomal protein L18 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 179 #molecular-weight 20518 #checksum 9493 SEQUENCE /// ENTRY R5BY8E #type complete TITLE ribosomal protein L18.e, cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein N0425; protein O0565; protein YNL0425; protein YNL301c; protein YOL120c; ribosomal protein rp28A ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Jun-2000 ACCESSIONS S05867; S60399; S63277; S66817; S72023 REFERENCE S05867 !$#authors Molenaar, C.M.T.; Woudt, L.P.; Jansen, A.E.M.; Mager, W.H.; !1Planta, R.J.; Donovan, D.M.; Pearson, N.J. !$#journal Nucleic Acids Res. (1984) 12:7345-7358 !$#title Structure and organization of two linked ribosomal protein !1genes in yeast. !$#cross-references MUID:85037916; PMID:6387623 !$#accession S05867 !'##molecule_type DNA !'##residues 1-186 ##label MOL !'##cross-references EMBL:X02635; NID:g4367; PIDN:CAA26481.1; PID:g4368 !'##experimental_source strain A364A, ATCC 22244 !'##genetics CH15 REFERENCE S60394 !$#authors Maurer, K.C.T.; Urbanus, J.H.M.; Planta, R.J. !$#journal Yeast (1995) 11:1303-1310 !$#title Sequence analysis of a 30 kb DNA segment from yeast !1chromosome XIV carrying a ribosomal protein gene cluster, !1the genes encoding a plasma membrane protein and a subunit !1of replication factor C, and a novel putative serine/ !1threonine protein kinase gene. !$#cross-references MUID:96132033; PMID:8553702 !$#accession S60399 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-186 ##label MAU !'##cross-references EMBL:U23084; NID:g1050853; PIDN:AAC49097.1; !1PID:g1050859 !'##genetics CH14 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1March 1995 REFERENCE S63266 !$#authors Maurer, C.T.C.; Urbanus, J.H.M.; Planta, R.J. !$#submission submitted to the Protein Sequence Database, April 1996 !$#accession S63277 !'##molecule_type DNA !'##residues 1-186 ##label MAW !'##cross-references EMBL:Z71577; GSPDB:GN00014; MIPS:YNL301c; !1NID:g1302395; PIDN:CAA96219.1; PID:g1302396 !'##experimental_source strain S288C !'##genetics CH14 REFERENCE S66814 !$#authors Arino, J.; Casamayor, A.; Gamo, F.J.; Gancedo, C.; Lafuente, !1M.J.; Aldea, M.; Casas, C.; Herrero, E. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S66817 !'##molecule_type DNA !'##residues 1-186 ##label ARI !'##cross-references EMBL:Z74862; GSPDB:GN00015; MIPS:YOL120c; !1NID:g1419996; PIDN:CAA99139.1; PID:g1419997 !'##experimental_source strain S288C !'##genetics CH15 REFERENCE S72019 !$#authors Lafuente, M.J.; Gamo, F.J.; Gancedo, C. !$#journal Yeast (1996) 12:1041-1045 !$#title DNA sequence analysis of a 10 624 bp fragment of the left !1arm of chromosome XV from Saccharomyces cerevisiae reveals a !1RNA binding protein, a mitochondrial protein, two ribosomal !1proteins and two new open reading frames. !$#cross-references MUID:97051591; PMID:8896268 !$#accession S72023 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-186 ##label LAF !'##cross-references EMBL:X95258; NID:g1550720; PIDN:CAA64550.1; !1PID:g1550725 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1996 GENETICS CH15 !$#gene SGD:RP28A; MIPS:YOL120c !'##cross-references MIPS:YOL120c; SGD:S0005480 !$#map_position 15L !$#introns 38/1 GENETICS CH14 !$#gene SGD:RP28B; MIPS:YNL301c !'##cross-references MIPS:YNL301c; SGD:S0005245 !$#map_position 14L !$#introns 38/1 CLASSIFICATION #superfamily rat ribosomal protein L18 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 186 #molecular-weight 20563 #checksum 6178 SEQUENCE /// ENTRY R5EC15 #type complete TITLE ribosomal protein L15 [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-May-1979 #sequence_revision 31-May-1979 #text_change 01-Mar-2002 ACCESSIONS A02794; H65122 REFERENCE A02794 !$#authors Giorginis, S.; Chen, R. !$#journal FEBS Lett. (1977) 84:347-350 !$#title The primary structure of protein L15 located at the !1peptidyl-transferase center of Escherichia coli ribosomes. !$#cross-references MUID:78084799; PMID:340263 !$#accession A02794 !'##molecule_type protein !'##residues 1-144 ##label GIO !'##experimental_source strain K REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65122 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-144 ##label BLAT !'##cross-references GB:AE000408; GB:U00096; NID:g1789694; !1PIDN:AAC76326.1; PID:g1789697; UWGP:b3301 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note no post-translational modifications were observed in mass !1spectrographic analysis; any acid labile modifications may !1have been missed GENETICS !$#gene rplO !$#map_position 73 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX large subunit ribosomal proteins: L1 (PIR:R5EC1), L3 !1(PIR:R5EC3), L2 (PIR:R5EC2), L4 (PIR:R5EC4), L5 (PIR:R5EC5), !1L6 (PIR:R5EC6), L7/L12 (PIR:R5EC7), L9 (PIR:R5EC9), L10 !1(PIR:R5EC10), L11 (PIR:R5EC11), L13 (PIR:R5EC13), L14 !1(PIR:R5EC14), L15 (PIR:R5EC15), L16 (PIR:R5EC16), L17 !1(PIR:R5EC17), L18 (PIR:R5EC18), L19 (PIR:R5EC19) FUNCTION !$#pathway protein biosynthesis !$#note binds 23S rRNA CLASSIFICATION #superfamily Escherichia coli ribosomal protein L15 KEYWORDS protein biosynthesis; ribosome; RNA binding FEATURE !$1-144 #product ribosomal protein L15 #status experimental !8#label MAT SUMMARY #length 144 #molecular-weight 14980 #checksum 1209 SEQUENCE /// ENTRY R5BS15 #type complete TITLE ribosomal protein L15 - Bacillus stearothermophilus ORGANISM #formal_name Bacillus stearothermophilus DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 30-Sep-1993 ACCESSIONS A02795 REFERENCE A91149 !$#authors Kimura, M.; Kimura, J.; Ashman, K. !$#journal Eur. J. Biochem. (1985) 150:491-497 !$#title The complete primary structure of ribosomal proteins L1, !1L14, L15, L23, L24, and L29 from Bacillus !1stearothermophilus. !$#cross-references MUID:85257681; PMID:4018095 !$#accession A02795 !'##molecule_type protein !'##residues 1-146 ##label KIM CLASSIFICATION #superfamily Escherichia coli ribosomal protein L15 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 146 #molecular-weight 15606 #checksum 786 SEQUENCE /// ENTRY R5BSL5 #type complete TITLE ribosomal protein L15 - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jun-2000 ACCESSIONS S12682; JS0491; S08628; A69696 REFERENCE S12680 !$#authors Yoshikawa, H.; Doi, R.H. !$#journal Nucleic Acids Res. (1990) 18:1647 !$#title Sequence of the Bacillus subtilis spectinomycin resistance !1gene region. !$#cross-references MUID:90221911; PMID:2139212 !$#accession S12682 !'##molecule_type DNA !'##residues 1-146 ##label YOS !'##cross-references EMBL:M31102; NID:g1184272; PIDN:AAB59117.1; !1PID:g143577 REFERENCE JS0490 !$#authors Nakamura, K.; Nakamura, A.; Takamatsu, H.; Yoshikawa, H.; !1Yamane, K. !$#journal J. Biochem. (1990) 107:603-607 !$#title Cloning and characterization of a Bacillus subtilis gene !1homologous to E. coli secY. !$#cross-references MUID:90292990; PMID:2113521 !$#accession JS0491 !'##molecule_type DNA !'##residues 1-146 ##label NAK !'##cross-references DDBJ:D00619; NID:g216336; PIDN:BAA00494.1; !1PID:g216338 REFERENCE S08628 !$#authors Suh, J.W.; Boylan, S.A.; Thomas, S.M.; Dolan, K.M.; Oliver, !1D.B.; Price, C.W. !$#journal Mol. Microbiol. (1990) 4:305-314 !$#title Isolation of a secY homologue from Bacillus subtilis: !1evidence for a common protein export pathway in eubacteria. !$#cross-references MUID:90251170; PMID:2110998 !$#accession S08628 !'##molecule_type DNA !'##residues 94-146 ##label SUH !'##cross-references EMBL:X51329; NID:g40132; PIDN:CAA35711.1; !1PID:g40133 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69696 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-146 ##label KUN !'##cross-references GB:Z99104; GB:AL009126; NID:g2632267; !1PIDN:CAB11911.1; PID:g2632402 !'##experimental_source strain 168 GENETICS !$#gene rplO CLASSIFICATION #superfamily Escherichia coli ribosomal protein L15 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 146 #molecular-weight 15383 #checksum 8836 SEQUENCE /// ENTRY R5YM15 #type complete TITLE ribosomal protein L15 - Mycoplasma capricolum ORGANISM #formal_name Mycoplasma capricolum DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 07-Dec-1999 ACCESSIONS S02849 REFERENCE S02830 !$#authors Ohkubo, S.; Muto, A.; Kawauchi, Y.; Yamao, F.; Osawa, S. !$#journal Mol. Gen. Genet. (1987) 210:314-322 !$#title The ribosomal protein gene cluster of Mycoplasma capricolum. !$#cross-references MUID:88142549; PMID:3481422 !$#accession S02849 !'##molecule_type DNA !'##residues 1-145 ##label OHK !'##cross-references EMBL:X06414; NID:g44207; PIDN:CAA29722.1; !1PID:g44227 GENETICS !$#gene rpl15 !$#genetic_code SGC3 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L15 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 145 #molecular-weight 15608 #checksum 9347 SEQUENCE /// ENTRY R5MUL5 #type complete TITLE ribosomal protein L15 precursor, chloroplast - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 22-Jun-1999 ACCESSIONS S20944; S22961; S18163; S22120 REFERENCE S20942 !$#authors Thompson, M.D.; Jacks, C.M.; Lenvik, T.R.; Gantt, J.S. !$#journal Plant Mol. Biol. (1992) 18:931-944 !$#title Characterization of rps17, rpl9 and rpl15: three !1nucleus-encoded plastid ribosomal protein genes. !$#cross-references MUID:92256814; PMID:1581570 !$#accession S20944 !'##molecule_type DNA !'##residues 1-277 ##label THO !'##cross-references EMBL:Z11508; NID:g732561; PIDN:CAA77593.1; !1PID:g16497 !$#accession S22961 !'##molecule_type mRNA !'##residues 5-277 ##label TH2 !'##cross-references EMBL:Z11507; NID:g16495; PIDN:CAA77592.1; !1PID:g388448 !'##note the sequence from Fig. 5 is inconsistent with that from Fig. 4 !1in having 84-Lys GENETICS !$#gene rpl15 !$#introns 28/3; 150/1; 200/3 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L15 KEYWORDS chloroplast; protein biosynthesis; ribosome FEATURE !$1-80 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$81-277 #product ribosomal protein L15 #status predicted !8#label MAT SUMMARY #length 277 #molecular-weight 29779 #checksum 2883 SEQUENCE /// ENTRY R5EC16 #type complete TITLE ribosomal protein L16 [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 12-Aug-1981 #sequence_revision 12-Aug-1981 #text_change 01-Mar-2002 ACCESSIONS I23129; A02796; D65124 REFERENCE A23129 !$#authors Zurawski, G.; Zurawski, S.M. !$#journal Nucleic Acids Res. (1985) 13:4521-4526 !$#title Structure of the Escherichia coli S10 ribosomal protein !1operon. !$#cross-references MUID:85242118; PMID:3892488 !$#accession I23129 !'##molecule_type DNA !'##residues 1-136 ##label ZUR !'##cross-references GB:X02613; NID:g42825; PIDN:CAA26467.1; PID:g42833 REFERENCE A02796 !$#authors Brosius, J.; Chen, R. !$#journal FEBS Lett. (1976) 68:105-109 !$#title The primary structure of protein L16 located at the !1peptidyltransferase center of Escherichia coli ribosomes. !$#cross-references MUID:77003691; PMID:786730 !$#accession A02796 !'##molecule_type protein !'##residues 1-136 ##label BRO !'##experimental_source strain K !'##note the residue at position 81 is an unusual amino acid chemically !1related to arginine REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65124 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-136 ##label BLAT !'##cross-references GB:AE000408; GB:U00096; NID:g1789694; !1PIDN:AAC76338.1; PID:g1789709; UWGP:b3313 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A30659 !$#authors Baxter, R.M.; Zahid, N. !$#journal Eur. J. Biochem. (1986) 155:273-277 !$#title L16, a bifunctional ribosomal protein and the enhancing !1effect of L6 and L11. !$#cross-references MUID:86164276; PMID:3956484 !$#contents annotation; active site REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note mass spectrographic analysis of post-translational !1modifications; any acid labile modifications may have been !1missed GENETICS !$#gene rplP !$#map_position 73 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX large subunit ribosomal proteins: L1 (PIR:R5EC1), L3 !1(PIR:R5EC3), L2 (PIR:R5EC2), L4 (PIR:R5EC4), L5 (PIR:R5EC5), !1L6 (PIR:R5EC6), L7/L12 (PIR:R5EC7), L9 (PIR:R5EC9), L10 !1(PIR:R5EC10), L11 (PIR:R5EC11), L13 (PIR:R5EC13), L14 !1(PIR:R5EC14), L15 (PIR:R5EC15), L16 (PIR:R5EC16), L17 !1(PIR:R5EC17), L18 (PIR:R5EC18), L19 (PIR:R5EC19) FUNCTION !$#pathway protein biosynthesis !$#note binds 23S rRNA; located at the A site of the !1peptidyltransferase center CLASSIFICATION #superfamily Escherichia coli ribosomal protein L16 KEYWORDS methylated amino end; protein biosynthesis; ribosome; RNA !1binding FEATURE !$1-136 #product ribosomal protein L16 #status experimental !8#label MAT\ !$1 #modified_site methylated amino end (Met) #status !8experimental\ !$13 #active_site His #status predicted\ !$81 #modified_site arginine derivative (Arg) #status !8experimental SUMMARY #length 136 #molecular-weight 15281 #checksum 1090 SEQUENCE /// ENTRY R5YM16 #type complete TITLE ribosomal protein L16 - Mycoplasma capricolum ALTERNATE_NAMES protein MC008 ORGANISM #formal_name Mycoplasma capricolum DATE 28-May-1986 #sequence_revision 31-Dec-1990 #text_change 07-Dec-1999 ACCESSIONS S02838; S77860; A02797; S48576 REFERENCE S02830 !$#authors Ohkubo, S.; Muto, A.; Kawauchi, Y.; Yamao, F.; Osawa, S. !$#journal Mol. Gen. Genet. (1987) 210:314-322 !$#title The ribosomal protein gene cluster of Mycoplasma capricolum. !$#cross-references MUID:88142549; PMID:3481422 !$#accession S02838 !'##molecule_type DNA !'##residues 1-137 ##label OHK !'##cross-references EMBL:X06414; NID:g44207; PIDN:CAA29711.1; !1PID:g44216 !'##experimental_source ATCC 27343 REFERENCE S77739 !$#authors Bork, P.; Ouzounis, C.; Casari, G.; Schneider, R.; Sander, !1C.; Dolan, M.; Gilbert, W.; Gillevet, P.M. !$#journal Mol. Microbiol. (1995) 16:955-967 !$#title Exploring the Mycoplasma capricolum genome: a minimal cell !1reveals its physiology. !$#cross-references MUID:96059641; PMID:7476192 !$#accession S77860 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-137 ##label BOR !'##cross-references EMBL:Z33011; NID:g541684; PIDN:CAA83693.1; !1PID:g950060 !'##experimental_source ATCC 27343 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1994 GENETICS !$#gene rpl16 !$#genetic_code SGC3 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L16 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 137 #molecular-weight 15799 #checksum 71 SEQUENCE /// ENTRY R5LV16 #type complete TITLE ribosomal protein L16 - liverwort (Marchantia polymorpha) chloroplast ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 22-Jun-1999 ACCESSIONS A02798; S01559 REFERENCE A00150 !$#authors Ohyama, K. !$#submission submitted to the EMBL Data Library, October 1986 !$#accession A02798 !'##molecule_type DNA !'##residues 1-143 ##label OHY REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features REFERENCE S01529 !$#authors Fukuzawa, H.; Kohchi, T.; Sano, T.; Shirai, H.; Umesono, K.; !1Inokuchi, H.; Ozeki, H.; Ohyama, K. !$#journal J. Mol. Biol. (1988) 203:333-351 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. III. Gene organization of the large !1single copy region from rbcL to trnI(CAU). !$#cross-references MUID:89068687; PMID:3199436 !$#accession S01559 !'##molecule_type DNA !'##residues 1-143 ##label FUK !'##cross-references GB:X04465; GB:Y00686; NID:g11640; PIDN:CAA28123.1; !1PID:g453595 GENETICS !$#gene rpl16 !$#genome chloroplast !$#introns 3/3 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L16 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 143 #molecular-weight 16150 #checksum 7435 SEQUENCE /// ENTRY R5KM16 #type complete TITLE ribosomal protein L16 - Chlamydomonas sp. WXM chloroplast ORGANISM #formal_name chloroplast Chlamydomonas sp. WXM DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 23-Sep-2002 ACCESSIONS S06258 REFERENCE S06258 !$#authors Lou, J.K.; Wu, M.; Chang, C.H.; Cuticchia, A.J. !$#journal Curr. Genet. (1987) 11:537-541 !$#title Localization of a r-protein gene within the chloroplast DNA !1replication origin of Chlamydomonas. !$#cross-references MUID:88223473; PMID:3450411 !$#accession S06258 !'##molecule_type DNA !'##residues 1-136 ##label LOU !'##cross-references EMBL:X05201; NID:g11466; PIDN:CAA28834.1; !1PID:g11467 !'##note the authors translated the codon GGT for residue 80 as Gln GENETICS !$#gene rpl16 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein L16 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 136 #molecular-weight 15440 #checksum 3527 SEQUENCE /// ENTRY R5KM6R #type complete TITLE ribosomal protein L16 - Chlamydomonas reinhardtii chloroplast ORGANISM #formal_name chloroplast Chlamydomonas reinhardtii DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 22-Jun-1999 ACCESSIONS A25893 REFERENCE A25893 !$#authors Wu, M.; Lou, J.K.; Chang, D.Y.; Chang, C.H.; Nie, Z.Q. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:6761-6765 !$#title Structure and function of a chloroplast DNA replication !1origin of Chlamydomonas reinhardtii. !$#accession A25893 !'##molecule_type DNA !'##residues 1-136 ##label WUM !'##cross-references GB:M13931; NID:g336670; PIDN:AAA84151.1; !1PID:g895616 GENETICS !$#gene rpl16 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein L16 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 136 #molecular-weight 15468 #checksum 3818 SEQUENCE /// ENTRY R5KT16 #type complete TITLE ribosomal protein L16, cyanelle - Cyanophora paradoxa cyanelle ORGANISM #formal_name cyanelle Cyanophora paradoxa DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 21-Jan-2000 ACCESSIONS S12213; T06883 REFERENCE S12211 !$#authors Michalowski, C.B.; Pfanzagl, B.; Loeffelhardt, W.; Bohnert, !1H.J. !$#journal Mol. Gen. Genet. (1990) 224:222-231 !$#title The cyanelle S10 spc ribosomal protein gene operon from !1Cyanophora paradoxa. !$#cross-references MUID:91117189; PMID:2126059 !$#accession S12213 !'##molecule_type DNA !'##residues 1-136 ##label MIC !'##cross-references GB:M30487; NID:g336645; PIDN:AAA63622.1; !1PID:g336648 !'##experimental_source strain LB555 UTEX REFERENCE Z15840 !$#authors Stirewalt, V.L.; Michalowski, C.B.; Luffelhardt, W.; !1Bohnert, H.J.; Bryant, D.A. !$#submission submitted to the EMBL Data Library, July 1995 !$#description Nucleotide sequence of the cyanelle genome from Cyanophora !1paradoxa. !$#accession T06883 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-136 ##label STI !'##cross-references EMBL:U30821; NID:g1016083; PIDN:AAA81226.1; !1PID:g1016139 !'##experimental_source strain Pringsheim LB555 GENETICS !$#gene rpl16 !$#genome cyanelle CLASSIFICATION #superfamily Escherichia coli ribosomal protein L16 KEYWORDS cyanelle; protein biosynthesis; ribosome SUMMARY #length 136 #molecular-weight 15537 #checksum 2623 SEQUENCE /// ENTRY R5SP16 #type complete TITLE ribosomal protein L16 - spinach chloroplast ALTERNATE_NAMES ribosomal protein CS-L24 ORGANISM #formal_name chloroplast Spinacia oleracea #common_name spinach DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S01979 REFERENCE S01976 !$#authors Zhou, D.X.; Quigley, F.; Massenet, O.; Mache, R. !$#journal Mol. Gen. Genet. (1989) 216:439-445 !$#title Cotranscription of the S10- and spc-like operons in spinach !1chloroplasts and identification of three of their gene !1products. !$#cross-references MUID:89313684; PMID:2747623 !$#accession S01979 !'##molecule_type DNA !'##residues 1-135 ##label ZHO !'##cross-references EMBL:X13336; NID:g12307; PIDN:CAA31716.1; !1PID:g12311 GENETICS !$#gene rps16 !$#genome chloroplast !$#introns 3/3 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L16 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 135 #molecular-weight 15328 #checksum 898 SEQUENCE /// ENTRY R5NT16 #type complete TITLE ribosomal protein L16 - common tobacco chloroplast ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 17-Feb-1995 ACCESSIONS A02799; F25943 REFERENCE A00149 !$#authors Sugiura, M. !$#submission submitted to the EMBL Data Library, August 1986 !$#accession A02799 !'##molecule_type DNA !'##residues 1-134 ##label SUG !'##experimental_source cv. Bright Yellow 4 REFERENCE A38013 !$#authors Shinozaki, K.; Ohme, M.; Tanaka, M.; Wakasugi, T.; !1Hayashida, N.; Matsubayashi, T.; Zaita, N.; Chunwongse, J.; !1Obokata, J.; Yamaguchi-Shinozaki, K.; Ohto, C.; Torazawa, !1K.; Meng, B.Y.; Sugita, M.; Deno, H.; Kamogashira, T.; !1Yamada, K.; Kusuda, J.; Takaiwa, F.; Kato, A.; Tohdoh, N.; !1Shimada, H.; Sugiura, M. !$#journal EMBO J. (1986) 5:2043-2049 !$#title The complete nucleotide sequence of the tobacco chloroplast !1genome: its gene organization and expression. !$#contents annotation; gene organization, sites, features REFERENCE A94118 !$#authors Tanaka, M.; Wakasugi, T.; Sugita, M.; Shinozaki, K.; !1Sugiura, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:6030-6034 !$#title Genes for the eight ribosomal proteins are clustered on the !1chloroplast genome of tobacco (Nicotiana tabacum): !1similarity to the S10 and spc operons of Escherichia coli. !$#cross-references MUID:86287388; PMID:3016736 !$#accession F25943 !'##molecule_type DNA !'##residues 1-134 ##label TAN GENETICS !$#gene rpl16 !$#genome chloroplast !$#introns 3/3 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L16 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 134 #molecular-weight 15214 #checksum 9458 SEQUENCE /// ENTRY R5RZ16 #type complete TITLE ribosomal protein L16 - rice chloroplast ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 22-Jun-1999 ACCESSIONS JQ0264; S05144 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0264 !'##molecule_type DNA !'##residues 1-136 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05144 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-136 ##label HIR !'##cross-references GB:X15901; NID:g11957; PIDN:CAA33933.1; PID:g669084 !'##experimental_source cv. Nihonbare !'##note this sequence was submitted to EMBL, July 1989 GENETICS !$#gene rpl16 !$#genome chloroplast !$#introns 3/3 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L16 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 136 #molecular-weight 15614 #checksum 4579 SEQUENCE /// ENTRY R5EG16 #type complete TITLE ribosomal protein L16 - Euglena gracilis chloroplast ORGANISM #formal_name chloroplast Euglena gracilis DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 22-Jun-1999 ACCESSIONS S09286; A30466; S34526; S34893; S20205 REFERENCE S09286 !$#authors Christopher, D.A.; Hallick, R.B. !$#journal Nucleic Acids Res. (1989) 17:7591-7608 !$#title Euglena gracilis chloroplast ribosomal protein operon: a new !1chloroplast gene for ribosomal protein L5 and description of !1a novel organelle intron category designated group III. !$#cross-references MUID:90016846; PMID:2477800 !$#accession S09286 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-133 ##label CHR !$#accession A30466 !'##molecule_type mRNA !'##residues 19-56 ##label CHR2 !'##experimental_source strain Z REFERENCE S34494 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.; Monfort, !1A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#submission submitted to the EMBL Data Library, January 1993 !$#description The complete sequence of the Euglena gracilis chloroplast !1genome (tentative). !$#accession S34526 !'##molecule_type DNA !'##residues 1-22,'LI',23-83,'R',85-133 ##label HAL1 !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50105.1; !1PID:g415761 !'##experimental_source strain Pringsheim Z REFERENCE S34862 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.R.; !1Monfort, A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#journal Nucleic Acids Res. (1993) 21:3537-3544 !$#title Complete sequence of Euglena gracilis chloroplast DNA. !$#cross-references MUID:93347989; PMID:8346031 !$#accession S34893 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-22,'LI',23-83,'R',85-133 ##label HAL2 !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50105.1; !1PID:g415761 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1993 GENETICS !$#gene rpl16 !$#genome chloroplast !$#introns 22/3; 32/1; 48/3 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L16 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 133 #molecular-weight 15277 #checksum 9815 SEQUENCE /// ENTRY R5ZM6M #type complete TITLE ribosomal protein L16 - maize mitochondrion ORGANISM #formal_name mitochondrion Zea mays #common_name maize DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 22-Jun-1999 ACCESSIONS S15026 REFERENCE S15025 !$#authors Hunt, M.D.; Newton, K.J. !$#journal EMBO J. (1991) 10:1045-1052 !$#title The NCS3 mutation: genetic evidence for the expression of !1ribosomal protein genes in Zea mays mitochondria. !$#cross-references MUID:91216097; PMID:1708720 !$#accession S15026 !'##molecule_type DNA !'##residues 1-185 ##label HUN !'##cross-references EMBL:X57445; NID:g13920; PIDN:CAA40691.1; !1PID:g13922 GENETICS !$#genome mitochondrion CLASSIFICATION #superfamily Escherichia coli ribosomal protein L16 KEYWORDS mitochondrion; protein biosynthesis; ribosome SUMMARY #length 185 #molecular-weight 21033 #checksum 9667 SEQUENCE /// ENTRY R5EC17 #type complete TITLE ribosomal protein L17 [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 01-Mar-2002 ACCESSIONS B22884; E23807; A02800; A65122 REFERENCE A22884 !$#authors Meek, D.W.; Hayward, R.S. !$#journal Nucleic Acids Res. (1984) 12:5813-5821 !$#title Nucleotide sequence of the rpoA-rplQ DNA of Escherichia !1coli: a second regulatory binding site for protein S4? !$#cross-references MUID:84272255; PMID:6379605 !$#accession B22884 !'##molecule_type DNA !'##residues 1-127 ##label MEE !'##cross-references GB:J01685; GB:X00766; NID:g147713; PIDN:AAA24578.1; !1PID:g147716 REFERENCE A23807 !$#authors Bedwell, D.; Davis, G.; Gosink, M.; Post, L.; Nomura, M.; !1Kestler, H.; Zengel, J.M.; Lindahl, L. !$#journal Nucleic Acids Res. (1985) 13:3891-3903 !$#title Nucleotide sequence of the alpha ribosomal protein operon of !1Escherichia coli. !$#cross-references MUID:85242076; PMID:2989779 !$#accession E23807 !'##molecule_type DNA !'##residues 1-127 ##label BED !'##cross-references GB:X02543; NID:g42795; PIDN:CAA26396.1; PID:g42800 REFERENCE A02800 !$#authors Rombauts, W.; Feytons, V.; Wittmann-Liebold, B. !$#journal FEBS Lett. (1982) 149:320-327 !$#title The primary structure of protein L17 from the Escherichia !1coli ribosome. !$#accession A02800 !'##molecule_type protein !'##residues 1-127 ##label ROM REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65122 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-127 ##label BLAT !'##cross-references GB:AE000407; GB:U00096; NID:g2367211; !1PIDN:AAC76319.1; PID:g1789689; UWGP:b3294 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note no post-translational modifications were observed in mass !1spectrographic analysis; any acid labile modifications may !1have been missed GENETICS !$#gene rplQ !$#map_position 73 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX large subunit ribosomal proteins: L1 (PIR:R5EC1), L3 !1(PIR:R5EC3), L2 (PIR:R5EC2), L4 (PIR:R5EC4), L5 (PIR:R5EC5), !1L6 (PIR:R5EC6), L7/L12 (PIR:R5EC7), L9 (PIR:R5EC9), L10 !1(PIR:R5EC10), L11 (PIR:R5EC11), L13 (PIR:R5EC13), L14 !1(PIR:R5EC14), L15 (PIR:R5EC15), L16 (PIR:R5EC16), L17 !1(PIR:R5EC17), L18 (PIR:R5EC18), L19 (PIR:R5EC19) FUNCTION !$#pathway protein biosynthesis CLASSIFICATION #superfamily Escherichia coli ribosomal protein L17 KEYWORDS protein biosynthesis; ribosome FEATURE !$1-127 #product ribosomal protein L17 #status experimental !8#label MAT SUMMARY #length 127 #molecular-weight 14364 #checksum 6290 SEQUENCE /// ENTRY R5BS17 #type complete TITLE ribosomal protein L17 - Bacillus stearothermophilus ALTERNATE_NAMES ribosomal protein BL21 ORGANISM #formal_name Bacillus stearothermophilus DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 30-Jun-1993 ACCESSIONS S07223 REFERENCE S07223 !$#authors Kimura, M.; Chow, C.K. !$#journal Eur. J. Biochem. (1984) 139:225-234 !$#title The complete amino acid sequences of ribosomal proteins L17, !1L27, and S9 from Bacillus stearothermophilus. !$#cross-references MUID:84132037; PMID:6365549 !$#accession S07223 !'##molecule_type protein !'##residues 1-119 ##label KIM !'##note the sequence from Fig. 5 is inconsistent with that from Fig. 1 !1in having 25-Leu and in lacking 80-Gln CLASSIFICATION #superfamily Escherichia coli ribosomal protein L17 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 119 #molecular-weight 13464 #checksum 335 SEQUENCE /// ENTRY F32307 #type complete TITLE ribosomal protein L17 - Bacillus subtilis ALTERNATE_NAMES ribosomal protein BL15 (rplQ) ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS F32307; C69696 REFERENCE A32307 !$#authors Boylan, S.A.; Suh, J.W.; Thomas, S.M.; Price, C.W. !$#journal J. Bacteriol. (1989) 171:2553-2562 !$#title Gene encoding the alpha core subunit of Bacillus subtilis !1RNA polymerase is cotranscribed with the genes for !1initiation factor 1 and ribosomal proteins B, S13, S11, and !1L17. !$#cross-references MUID:89213940; PMID:2496109 !$#accession F32307 !'##molecule_type DNA !'##residues 1-120 ##label BOY !'##cross-references GB:M26414; NID:g142458; PIDN:AAA22218.1; !1PID:g142464 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69696 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-120 ##label KUN !'##cross-references GB:Z99104; GB:AL009126; NID:g2632267; !1PIDN:CAB11920.1; PID:g2632411 !'##experimental_source strain 168 GENETICS !$#gene rplQ CLASSIFICATION #superfamily Escherichia coli ribosomal protein L17 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 120 #molecular-weight 13751 #checksum 2720 SEQUENCE /// ENTRY R5BS7F #type complete TITLE ribosomal protein L9 - Bacillus stearothermophilus ALTERNATE_NAMES ribosomal protein BL17 ORGANISM #formal_name Bacillus stearothermophilus DATE 28-Feb-1981 #sequence_revision 31-Mar-1993 #text_change 22-Jun-1999 ACCESSIONS S16974; A02801; C39085 REFERENCE S16974 !$#authors Vorgias, C.E.; Kingswell, A.J.; Dauter, Z.; Wilson, K.S. !$#journal FEBS Lett. (1991) 286:204-208 !$#title Cloning, overexpression, purification and crystallisation of !1ribosomal protein L9 from Bacillus stearothermophilus. !$#cross-references MUID:91323518; PMID:1864369 !$#accession S16974 !'##molecule_type DNA !'##residues 1-148 ##label VOR !'##cross-references GB:X62002; NID:g39816; PIDN:CAA43972.1; PID:g39817 REFERENCE A02801 !$#authors Kimura, M.; Dijk, J.; Heiland, I. !$#journal FEBS Lett. (1980) 121:323-326 !$#title The primary structure of protein BLF17 isolated from the !1large subunit of the Bacillus stearothermophilus ribosome. !$#accession A02801 !'##molecule_type protein !'##residues 1-26,28-59,61-149 ##label KIM REFERENCE A39085 !$#authors Ramakrishnan, V.; Gerchman, S.E. !$#journal J. Biol. Chem. (1991) 266:880-885 !$#title Cloning, sequencing, and overexpression of genes for !1ribosomal proteins from Bacillus stearothermophilus. !$#cross-references MUID:91093287; PMID:1985969 !$#accession C39085 !'##molecule_type DNA !'##residues 9-141 ##label RAM !'##cross-references GB:M57623 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L9 KEYWORDS protein biosynthesis; ribosome FEATURE !$1-149 #product ribosomal protein L9 #status experimental !8#label MAT SUMMARY #length 149 #molecular-weight 16311 #checksum 6025 SEQUENCE /// ENTRY R5EC9 #type complete TITLE ribosomal protein L9 [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 13-Jun-1983 #sequence_revision 10-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS F65231; S56428; A02802 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65231 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-149 ##label BLAT !'##cross-references GB:AE000491; GB:U00096; NID:g2367357; !1PIDN:AAC77160.1; PID:g1790647; UWGP:b4203 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56428 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-149 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97099.1; !1PID:g537044 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A02802 !$#authors Kamp, R.M.; Wittmann-Liebold, B. !$#journal FEBS Lett. (1982) 149:313-319 !$#title The primary structure of protein L9 from the Escherichia !1coli ribosome. !$#accession A02802 !'##molecule_type protein !'##residues 1-106,'D',107-124,'H',126-127,129-135,137-149 ##label KAM REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note no post-translational modifications were observed in mass !1spectrographic analysis; any acid labile modifications may !1have been missed GENETICS !$#gene rplI !$#map_position 96 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX large subunit ribosomal proteins: L1 (PIR:R5EC1), L3 !1(PIR:R5EC3), L2 (PIR:R5EC2), L4 (PIR:R5EC4), L5 (PIR:R5EC5), !1L6 (PIR:R5EC6), L7/L12 (PIR:R5EC7), L9 (PIR:R5EC9), L10 !1(PIR:R5EC10), L11 (PIR:R5EC11), L13 (PIR:R5EC13), L14 !1(PIR:R5EC14), L15 (PIR:R5EC15), L16 (PIR:R5EC16), L17 !1(PIR:R5EC17), L18 (PIR:R5EC18), L19 (PIR:R5EC19) FUNCTION !$#pathway protein biosynthesis CLASSIFICATION #superfamily Escherichia coli ribosomal protein L9 KEYWORDS protein biosynthesis; ribosome FEATURE !$1-149 #product ribosomal protein L9 #status experimental !8#label MAT SUMMARY #length 149 #molecular-weight 15769 #checksum 3372 SEQUENCE /// ENTRY R5PM9 #type complete TITLE ribosomal protein L9 precursor, chloroplast - garden pea ALTERNATE_NAMES ribosomal protein PsCL13 ORGANISM #formal_name Pisum sativum #common_name garden pea DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 30-Jun-1993 ACCESSIONS S04684 REFERENCE S04684 !$#authors Gantt, J.S. !$#journal Curr. Genet. (1988) 14:519-528 !$#title Nucleotide sequences of cDNAs encoding four complete !1nuclear-encoded plastid ribosomal proteins. !$#cross-references MUID:89136071; PMID:3066512 !$#accession S04684 !'##molecule_type mRNA !'##residues 1-194 ##label GAN !'##cross-references EMBL:X14019 !'##note the author translated the codon GAC for residue 20 as Ala CLASSIFICATION #superfamily Escherichia coli ribosomal protein L9 KEYWORDS chloroplast; protein biosynthesis; ribosome FEATURE !$1-34 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$35-194 #product ribosomal protein L9 #status predicted !8#label MAT SUMMARY #length 194 #molecular-weight 21810 #checksum 7203 SEQUENCE /// ENTRY R5MUL9 #type complete TITLE ribosomal protein L9 precursor, chloroplast [similarity] - Arabidopsis thaliana ALTERNATE_NAMES protein F28D10_80 ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 01-Sep-2000 ACCESSIONS S20943; S22960; T51786; S18025; S22121 REFERENCE S20942 !$#authors Thompson, M.D.; Jacks, C.M.; Lenvik, T.R.; Gantt, J.S. !$#journal Plant Mol. Biol. (1992) 18:931-944 !$#title Characterization of rps17, rpl9 and rpl15: three !1nucleus-encoded plastid ribosomal protein genes. !$#cross-references MUID:92256814; PMID:1581570 !$#accession S20943 !'##molecule_type DNA !'##residues 1-197 ##label THO !'##cross-references EMBL:Z11509; NID:g16500; PIDN:CAA77594.1; !1PID:g16501 !$#accession S22960 !'##molecule_type mRNA !'##residues 1-197 ##label TH2 !'##cross-references EMBL:Z11129; NID:g16498; PIDN:CAA77480.1; !1PID:g16499 REFERENCE Z25454 !$#authors Delseny, M.; Berger, C.; Cooke, R.; Grellet, F.; Laudie, M.; !1Mewes, H.W.; Rudd, S.; Lemcke, K.; Mayer, K.F.X.; Quetier, !1F.; Salanoubat, M. !$#submission submitted to the Protein Sequence Database, August 2000 !$#accession T51786 !'##status preliminary !'##molecule_type DNA !'##residues 1-197 ##label DEL !'##cross-references EMBL:AL391254 !'##experimental_source cultivar Columbia; BAC clone F28D10 GENETICS !$#gene rpl9 !$#map_position 3 !$#introns 51/3; 94/2; 109/3; 142/2; 158/2 !$#note F28D10_80 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L9 KEYWORDS chloroplast; protein biosynthesis; ribosome FEATURE !$1-37 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$38-197 #product ribosomal protein L9 #status predicted !8#label MAT SUMMARY #length 197 #molecular-weight 22134 #checksum 1913 SEQUENCE /// ENTRY R5EC18 #type complete TITLE ribosomal protein L18 [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 12-Aug-1981 #sequence_revision 12-Aug-1981 #text_change 01-Mar-2002 ACCESSIONS A02803; C65123 REFERENCE A02803 !$#authors Brosius, J.; Schiltz, E.; Chen, R. !$#journal FEBS Lett. (1975) 56:359-361 !$#title The primary structure of the 5S RNA binding protein L18 from !1Escherichia coli ribosomes. !$#cross-references MUID:76003293; PMID:1098937 !$#accession A02803 !'##molecule_type protein !'##residues 1-117 ##label BRO !'##experimental_source strain K REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65123 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-117 ##label BLAT !'##cross-references GB:AE000408; GB:U00096; NID:g1789694; !1PIDN:AAC76329.1; PID:g1789700; UWGP:b3304 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note no post-translational modifications were observed in mass !1spectrographic analysis; any acid labile modifications may !1have been missed GENETICS !$#gene rplR !$#map_position 73 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX large subunit ribosomal proteins: L1 (PIR:R5EC1), L3 !1(PIR:R5EC3), L2 (PIR:R5EC2), L4 (PIR:R5EC4), L5 (PIR:R5EC5), !1L6 (PIR:R5EC6), L7/L12 (PIR:R5EC7), L9 (PIR:R5EC9), L10 !1(PIR:R5EC10), L11 (PIR:R5EC11), L13 (PIR:R5EC13), L14 !1(PIR:R5EC14), L15 (PIR:R5EC15), L16 (PIR:R5EC16), L17 !1(PIR:R5EC17), L18 (PIR:R5EC18), L19 (PIR:R5EC19) FUNCTION !$#pathway protein biosynthesis CLASSIFICATION #superfamily Escherichia coli ribosomal protein L18 KEYWORDS protein biosynthesis; ribosome FEATURE !$1-117 #product ribosomal protein L18 #status experimental !8#label MAT SUMMARY #length 117 #molecular-weight 12770 #checksum 8913 SEQUENCE /// ENTRY R5BS8F #type complete TITLE ribosomal protein L18 - Bacillus stearothermophilus ORGANISM #formal_name Bacillus stearothermophilus DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 30-Jun-1993 ACCESSIONS B29102; D39085 REFERENCE A29102 !$#authors Kimura, J.; Kimura, M. !$#journal FEBS Lett. (1987) 210:85-90 !$#title The complete amino acid sequences of the 5 S rRNA binding !1proteins L5 and L18 from the moderate thermophile Bacillus !1stearothermophilus ribosome. !$#cross-references MUID:87105936; PMID:3542562 !$#accession B29102 !'##molecule_type protein !'##residues 1-120 ##label KIM REFERENCE A39085 !$#authors Ramakrishnan, V.; Gerchman, S.E. !$#journal J. Biol. Chem. (1991) 266:880-885 !$#title Cloning, sequencing, and overexpression of genes for !1ribosomal proteins from Bacillus stearothermophilus. !$#cross-references MUID:91093287; PMID:1985969 !$#accession D39085 !'##molecule_type DNA !'##residues 9-111 ##label RAM !'##cross-references GB:M57624 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L18 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 120 #molecular-weight 13471 #checksum 1969 SEQUENCE /// ENTRY R5YM18 #type complete TITLE ribosomal protein L18 - Mycoplasma capricolum ORGANISM #formal_name Mycoplasma capricolum DATE 17-Mar-1987 #sequence_revision 31-Dec-1990 #text_change 07-Dec-1999 ACCESSIONS S02847; A02804 REFERENCE S02830 !$#authors Ohkubo, S.; Muto, A.; Kawauchi, Y.; Yamao, F.; Osawa, S. !$#journal Mol. Gen. Genet. (1987) 210:314-322 !$#title The ribosomal protein gene cluster of Mycoplasma capricolum. !$#cross-references MUID:88142549; PMID:3481422 !$#accession S02847 !'##molecule_type DNA !'##residues 1-116 ##label OHK !'##cross-references EMBL:X06414; NID:g44207; PIDN:CAA29720.1; !1PID:g44225 GENETICS !$#gene rpl18 !$#genetic_code SGC3 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L18 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 116 #molecular-weight 13242 #checksum 1810 SEQUENCE /// ENTRY R5KT18 #type complete TITLE ribosomal protein L18, cyanelle - Cyanophora paradoxa cyanelle ORGANISM #formal_name cyanelle Cyanophora paradoxa DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 21-Jan-2000 ACCESSIONS S12219; T06877 REFERENCE S12211 !$#authors Michalowski, C.B.; Pfanzagl, B.; Loeffelhardt, W.; Bohnert, !1H.J. !$#journal Mol. Gen. Genet. (1990) 224:222-231 !$#title The cyanelle S10 spc ribosomal protein gene operon from !1Cyanophora paradoxa. !$#cross-references MUID:91117189; PMID:2126059 !$#accession S12219 !'##molecule_type DNA !'##residues 1-121 ##label MIC !'##cross-references GB:M30487; NID:g336645; PIDN:AAA63628.1; !1PID:g336654 !'##experimental_source strain LB555 UTEX REFERENCE Z15840 !$#authors Stirewalt, V.L.; Michalowski, C.B.; Luffelhardt, W.; !1Bohnert, H.J.; Bryant, D.A. !$#submission submitted to the EMBL Data Library, July 1995 !$#description Nucleotide sequence of the cyanelle genome from Cyanophora !1paradoxa. !$#accession T06877 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-121 ##label STI !'##cross-references EMBL:U30821; NID:g1016083; PIDN:AAA81220.1; !1PID:g1016133 !'##experimental_source strain Pringsheim LB555 GENETICS !$#gene rpl18 !$#genome cyanelle CLASSIFICATION #superfamily Escherichia coli ribosomal protein L18 KEYWORDS cyanelle; protein biosynthesis; ribosome SUMMARY #length 121 #molecular-weight 13554 #checksum 3680 SEQUENCE /// ENTRY R5PM18 #type complete TITLE ribosomal protein PsCL18 precursor, chloroplast - garden pea ORGANISM #formal_name Pisum sativum #common_name garden pea DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 22-Jun-1999 ACCESSIONS S04686 REFERENCE S04684 !$#authors Gantt, J.S. !$#journal Curr. Genet. (1988) 14:519-528 !$#title Nucleotide sequences of cDNAs encoding four complete !1nuclear-encoded plastid ribosomal proteins. !$#cross-references MUID:89136071; PMID:3066512 !$#accession S04686 !'##molecule_type mRNA !'##residues 1-145 ##label GAN !'##cross-references EMBL:X14021; NID:g20868; PIDN:CAA32186.1; !1PID:g20869 CLASSIFICATION #superfamily pea chloroplast ribosomal protein PsCL18 KEYWORDS chloroplast; protein biosynthesis; ribosome FEATURE !$1-49 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$50-145 #product ribosomal protein PsCL18 #status predicted !8#label MAT SUMMARY #length 145 #molecular-weight 16257 #checksum 1761 SEQUENCE /// ENTRY R5RT18 #type complete TITLE ribosomal protein L18a, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1990 #sequence_revision 21-Jul-2000 #text_change 21-Jul-2000 ACCESSIONS JC4231; S03957 REFERENCE JC4228 !$#authors Chan, Y.L.; Olvera, J.; Wool, I.G. !$#journal Biochem. Biophys. Res. Commun. (1995) 213:1042-1050 !$#title The primary structures of rat ribosomal proteins: the !1characterization of the cDNAs for S21 and L39, corrections !1in the sequences of L7 and L18a, and the identification of !1L33. !$#cross-references MUID:95382802; PMID:7654221 !$#accession JC4231 !'##molecule_type mRNA !'##residues 1-176 ##label CHA !'##cross-references EMBL:X14181; NID:g416553; PIDN:CAA32385.1; !1PID:g416554 !'##experimental_source liver REFERENCE S03957 !$#authors Aoyama, Y.; Chan, Y.L.; Meyuhas, O.; Wool, I.G. !$#journal FEBS Lett. (1989) 247:242-246 !$#title The primary structure of rat ribosomal protein L18a. !$#cross-references MUID:89232128; PMID:2541017 !$#accession S03957 !'##molecule_type mRNA !'##residues 1-143,'SSTTPRSSSHCPTVCCGAS',164-176 ##label AOY !'##cross-references EMBL:X14181 !'##note the protein is designated as ribosomal protein L18a according !1to comigration analysis after in vitro translation !'##note this sequence has been revised in reference JC4228 CLASSIFICATION #superfamily rat ribosomal protein L18a KEYWORDS protein biosynthesis; ribosome SUMMARY #length 176 #molecular-weight 20732 #checksum 5714 SEQUENCE /// ENTRY R5EC19 #type complete TITLE ribosomal protein L19 [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-May-1979 #sequence_revision 30-Jun-1991 #text_change 01-Mar-2002 ACCESSIONS S07951; A02805; A65039 REFERENCE A30380 !$#authors Bystroem, A.S.; Hjalmarsson, K.J.; Wikstroem, P.M.; Bjoerk, !1G.R. !$#journal EMBO J. (1983) 2:899-905 !$#title The nucleotide sequence of an Escherichia coli operon !1containing genes for the tRNA(m1G)methyltransferase, the !1ribosomal proteins S16 and L19 and a 21-K polypeptide. !$#cross-references MUID:84057772; PMID:6357787 !$#accession S07951 !'##molecule_type DNA !'##residues 1-115 ##label BYS !'##cross-references EMBL:X01818; NID:g43141; PIDN:CAA25960.1; !1PID:g43145 REFERENCE A02805 !$#authors Brosius, J.; Arfsten, U. !$#journal Biochemistry (1978) 17:508-516 !$#title Primary structure of protein L19 from the large subunit of !1Escherichia coli ribosomes. !$#cross-references MUID:78080790; PMID:339951 !$#accession A02805 !'##molecule_type protein !'##residues 2-115 ##label BRO REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65039 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-115 ##label BLAT !'##cross-references GB:AE000346; GB:U00096; NID:g2367141; !1PIDN:AAC75655.1; PID:g1788958; UWGP:b2606 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note no post-translational modifications were observed in mass !1spectrographic analysis; any acid labile modifications may !1have been missed !$#note although this protein has been reported with the initiator !1methionine removed, this modification was not observed in !1this study GENETICS !$#gene rplS !$#map_position 57 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX large subunit ribosomal proteins: L1 (PIR:R5EC1), L3 !1(PIR:R5EC3), L2 (PIR:R5EC2), L4 (PIR:R5EC4), L5 (PIR:R5EC5), !1L6 (PIR:R5EC6), L7/L12 (PIR:R5EC7), L9 (PIR:R5EC9), L10 !1(PIR:R5EC10), L11 (PIR:R5EC11), L13 (PIR:R5EC13), L14 !1(PIR:R5EC14), L15 (PIR:R5EC15), L16 (PIR:R5EC16), L17 !1(PIR:R5EC17), L18 (PIR:R5EC18), L19 (PIR:R5EC19) FUNCTION !$#pathway protein biosynthesis CLASSIFICATION #superfamily Escherichia coli ribosomal protein L19 KEYWORDS protein biosynthesis; ribosome FEATURE !$1-115 #product ribosomal protein L19, unmodified #status !8experimental #label MAT1\ !$2-115 #product ribosomal protein L19, modified #status !8experimental #label MAT2 SUMMARY #length 115 #molecular-weight 13133 #checksum 4504 SEQUENCE /// ENTRY S37176 #type complete TITLE ribosomal protein L19 - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S37176 REFERENCE S37173 !$#authors Persson, B.C. !$#submission submitted to the EMBL Data Library, September 1993 !$#accession S37176 !'##status preliminary !'##molecule_type DNA !'##residues 1-115 ##label PER !'##cross-references EMBL:X74933; NID:g402164; PIDN:CAA52888.1; !1PID:g402168 GENETICS !$#gene rplS CLASSIFICATION #superfamily Escherichia coli ribosomal protein L19 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 115 #molecular-weight 13130 #checksum 4196 SEQUENCE /// ENTRY B64054 #type complete TITLE ribosomal protein L19 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B64054 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession B64054 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-116 ##label TIGR !'##cross-references GB:U32705; GB:L42023; NID:g1573156; !1PIDN:AAC21870.1; PID:g1573161; TIGR:HI0201 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L19 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 116 #molecular-weight 13070 #checksum 4660 SEQUENCE /// ENTRY A45434 #type complete TITLE ribosomal protein L19 - Bacillus stearothermophilus ORGANISM #formal_name Bacillus stearothermophilus DATE 03-Feb-1994 #sequence_revision 03-Feb-1994 #text_change 03-Feb-1994 ACCESSIONS A45434; A37333 REFERENCE A45434 !$#authors Herwig, S.; Kruft, V.; Eckart, K.; Wittmann-Liebold, B. !$#journal J. Biol. Chem. (1993) 268:4643-4650 !$#title Cross-linked amino acids in the protein pairs L3-L19 and !1L23-L29 of Bacillus stearothermophilus ribosomes after !1treatment with diepoxybutane. !$#cross-references MUID:93186760; PMID:8444837 !$#accession A45434 !'##molecule_type protein !'##residues 1-116 ##label HER !'##note sequence extracted from NCBI backbone (NCBIP:126558) CLASSIFICATION #superfamily Escherichia coli ribosomal protein L19 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 116 #molecular-weight 13444 #checksum 3615 SEQUENCE /// ENTRY S33697 #type complete TITLE ribosomal protein L19 - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein sll1740 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S33697; S77319 REFERENCE S33696 !$#authors Schmidt, J. !$#submission submitted to the EMBL Data Library, March 1993 !$#accession S33697 !'##status preliminary !'##molecule_type DNA !'##residues 1-122 ##label SCH !'##cross-references EMBL:X72627; NID:g311687; PIDN:CAA51203.1; !1PID:g311689 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S77319 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-122 ##label KAN !'##cross-references EMBL:D90906; GB:AB001339; NID:g1652492; !1PIDN:BAA17422.1; PID:g1652501 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene rpl19 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L19 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 122 #molecular-weight 13786 #checksum 7028 SEQUENCE /// ENTRY R5RT19 #type complete TITLE ribosomal protein L19, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 21-Jul-2000 ACCESSIONS A26710; A34989; A56846; I59154; S09560 REFERENCE A26710 !$#authors Chan, Y.L.; Lin, A.; McNally, J.; Peleg, D.; Meyuhas, O.; !1Wool, I.G. !$#journal J. Biol. Chem. (1987) 262:1111-1115 !$#title The primary structure of rat ribosomal protein L19. A !1determination from the sequence of nucleotides in a cDNA and !1from the sequence of amino acids in the protein. !$#cross-references MUID:87109220; PMID:3542997 !$#accession A26710 !'##molecule_type mRNA !'##residues 1-196 ##label CHA !'##cross-references EMBL:J02650; NID:g206725; PIDN:AAA42071.1; !1PID:g206726 !$#accession A34989 !'##molecule_type protein !'##residues 4-12 ##label CHA2 !'##note the protein is designated as ribosomal protein L19 REFERENCE A56846 !$#authors Davies, B.; Fried, M. !$#journal Genomics (1995) 25:372-380 !$#title The L19 ribosomal protein gene (RPL19): gene organization, !1chromosomal mapping, and novel promoter region. !$#cross-references MUID:95309903; PMID:7789970 !$#accession A56846 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-119,'VSQPVPEGQRECVQKQADSHGAHPQTEGRQGPQEATG',157-196 !1##label RES !'##cross-references EMBL:X82202; NID:g732917; PID:g762995 !'##note the differences in the central region are due to a frameshift !1error resulting from a shifted intron/exon boundary REFERENCE I59154 !$#authors Davies, B.; Feo, S.; Heard, E.; Fried, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:6691-6695 !$#title A strategy to detect and isolate an intron-containing gene !1in the presence of multiple processed pseudogenes. !$#cross-references MUID:89367314; PMID:2771953 !$#accession I59154 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 111-145 ##label RE2 !'##cross-references GB:M30264; NID:g205112; PIDN:AAA41503.1; !1PID:g554467 GENETICS !$#gene RPL19 !$#introns 2/2; 38/1; 79/1; 119/3; 156/3 CLASSIFICATION #superfamily rat ribosomal protein L19 KEYWORDS protein biosynthesis; ribosome; RNA binding SUMMARY #length 196 #molecular-weight 23466 #checksum 3699 SEQUENCE /// ENTRY R5DO9E #type complete TITLE ribosomal protein L19.e - slime mold (Dictyostelium discoideum) ALTERNATE_NAMES 22K calmodulin-binding protein; ribosomal protein V14 ORGANISM #formal_name Dictyostelium discoideum DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 22-Jun-1999 ACCESSIONS S07561; A41574 REFERENCE S07561 !$#authors Singleton, C.K.; Manning, S.S.; Ken, R. !$#journal Nucleic Acids Res. (1989) 17:9679-9692 !$#title Primary structure and regulation of vegetative specific !1genes of Dictyostelium discoideum. !$#cross-references MUID:90098836; PMID:2602140 !$#accession S07561 !'##molecule_type DNA !'##residues 1-186 ##label SIN !'##cross-references EMBL:X15383; NID:g7389; PIDN:CAA33443.1; !1PID:g295737 REFERENCE A41574 !$#authors Sonnemann, J.; Baeuerle, A.; Winckler, T.; Mutzel, R. !$#journal J. Biol. Chem. (1991) 266:23091-23096 !$#title A ribosomal calmodulin-binding protein from Dictyostelium. !$#cross-references MUID:92078175; PMID:1744106 !$#accession A41574 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type mRNA !'##residues 1-186 ##label SON !'##cross-references GB:L27657; NID:g443590; PIDN:AAA33247.1; !1PID:g443591 GENETICS !$#introns 38/1 FUNCTION !$#description The calmodulin-binding activity of this component of the !1large ribosomal subunit suggests a physiological role for !1calmodulin in the Ca2+ regulation of eukaryotic protein !1synthesis. CLASSIFICATION #superfamily rat ribosomal protein L19 KEYWORDS calmodulin binding; protein biosynthesis; ribosome SUMMARY #length 186 #molecular-weight 21612 #checksum 9067 SEQUENCE /// ENTRY R5MXE #type complete TITLE ribosomal protein L19.eR - Methanococcus vannielii ALTERNATE_NAMES ribosomal protein E ORGANISM #formal_name Methanococcus vannielii DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 22-Jun-1999 ACCESSIONS S05622 REFERENCE S05611 !$#authors Auer, J.; Spicker, G.; Boeck, A. !$#journal J. Mol. Biol. (1989) 209:21-36 !$#title Organization and structure of the Methanococcus !1transcriptional unit homologous to the Escherichia coli !1"spectinomycin operon". Implications for the evolutionary !1relationship of 70 S and 80 S ribosomes. !$#cross-references MUID:90040717; PMID:2530355 !$#accession S05622 !'##molecule_type DNA !'##residues 1-149 ##label AUE !'##cross-references EMBL:X16720; NID:g44754; PIDN:CAA34698.1; !1PID:g44766 CLASSIFICATION #superfamily rat ribosomal protein L19 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 149 #molecular-weight 17286 #checksum 7088 SEQUENCE /// ENTRY A64359 #type complete TITLE ribosomal protein L19 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 13-Sep-1996 #sequence_revision 04-Oct-1996 #text_change 21-Jul-2000 ACCESSIONS A64359 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession A64359 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-151 ##label BUL !'##cross-references GB:U67497; GB:L77117; NID:g2826284; !1PIDN:AAB98462.1; PID:g1591175; TIGR:MJ0473 GENETICS !$#map_position FOR417350-417805 !$#start_codon GTG CLASSIFICATION #superfamily rat ribosomal protein L19 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 151 #molecular-weight 17630 #checksum 4948 SEQUENCE /// ENTRY R5HSH4 #type complete TITLE ribosomal protein L19.eR [validated] - Haloarcula marismortui ALTERNATE_NAMES ribosomal protein HL24 ORGANISM #formal_name Haloarcula marismortui DATE 31-Mar-1991 #sequence_revision 31-Dec-1992 #text_change 31-Mar-2000 ACCESSIONS S16540; S06847; T46805 REFERENCE S16535 !$#authors Scholzen, T.; Arndt, E. !$#journal Mol. Gen. Genet. (1991) 228:70-80 !$#title Organization and nucleotide sequence of ten ribosomal !1protein genes from the region equivalent to the !1spectinomycin operon in the archaebacterium Halobacterium !1marismortui. !$#cross-references MUID:91360093; PMID:1832208 !$#accession S16540 !'##molecule_type DNA !'##residues 1-149 ##label SCH !'##cross-references EMBL:X58395; NID:g48860; PIDN:CAA41289.1; !1PID:g48866 REFERENCE S06844 !$#authors Hatakeyama, T.; Kaufmann, F.; Schroeter, B.; Hatakeyama, T. !$#journal Eur. J. Biochem. (1989) 185:685-693 !$#title Primary structures of five ribosomal proteins from the !1archaebacterium Halobacterium marismortui and their !1structural relationships to eubacterial and eukaryotic !1ribosomal proteins. !$#cross-references MUID:90076190; PMID:2591382 !$#accession S06847 !'##molecule_type protein !'##residues 2-81,'G',83-149 ##label HAT !'##note the source is designated as Halobacterium marismortui !'##note the protein is designated as ribosomal protein HL24 GENETICS !$#gene HL24 CLASSIFICATION #superfamily rat ribosomal protein L19 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-149 #product ribosomal protein L19eR #status experimental !8#label MAT SUMMARY #length 149 #molecular-weight 16762 #checksum 3934 SEQUENCE /// ENTRY R5EC20 #type complete TITLE ribosomal protein L20 [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Sep-1979 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS D64930; S08608; A02806; I41282 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64930 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-118 ##label BLAT !'##cross-references GB:AE000266; GB:U00096; NID:g1787997; !1PIDN:AAC74786.1; PID:g1788009; UWGP:b1716 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A30391 !$#authors Fayat, G.; Mayaux, J.F.; Sacerdot, C.; Fromant, M.; !1Springer, M.; Grunberg-Manago, M.; Blanquet, S. !$#journal J. Mol. Biol. (1983) 171:239-261 !$#title Escherichia coli phenylalanyl-tRNA synthetase operon region. !1Evidence for an attenuation mechanism. Identification of the !1gene for the ribosomal protein L20. !$#cross-references MUID:84090239; PMID:6317865 !$#accession S08608 !'##molecule_type DNA !'##residues 1-32,'A',34-118 ##label FAY !'##cross-references EMBL:V00291; NID:g43065; PIDN:CAA23562.1; !1PID:g43068 REFERENCE A02806 !$#authors Wittmann-Liebold, B.; Seib, C. !$#journal FEBS Lett. (1979) 103:61-65 !$#title The primary structure of protein L20 from the large subunit !1of the Escherichia coli ribosome. !$#cross-references MUID:79236776; PMID:381019 !$#accession A02806 !'##molecule_type protein !'##residues 2-118 ##label WIT !'##experimental_source strain K12 A19 REFERENCE I41281 !$#authors Miller, H.I. !$#journal Cold Spring Harb. Symp. Quant. Biol. (1984) 49:691-698 !$#title Primary structure of the himA gene of Escherichia coli: !1homology with DNA-binding protein HU and association with !1the phenylalanyl-tRNA synthetase operon. !$#cross-references MUID:85153048; PMID:6397321 !$#accession I41282 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-32,'A',34-118 ##label MIL !'##cross-references GB:K02844; NID:g146342; PIDN:AAA51468.1; !1PID:g146344 REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note mass spectrographic analysis of post-translational !1modifications; any acid labile modifications may have been !1missed GENETICS !$#gene rplT; pdzA !$#map_position 38 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX large subunit ribosomal proteins: L1 (PIR:R5EC1), L3 !1(PIR:R5EC3), L2 (PIR:R5EC2), L4 (PIR:R5EC4), L5 (PIR:R5EC5), !1L6 (PIR:R5EC6), L7/L12 (PIR:R5EC7), L9 (PIR:R5EC9), L10 !1(PIR:R5EC10), L11 (PIR:R5EC11), L13 (PIR:R5EC13), L14 !1(PIR:R5EC14), L15 (PIR:R5EC15), L16 (PIR:R5EC16), L17 !1(PIR:R5EC17), L18 (PIR:R5EC18), L19 (PIR:R5EC19) FUNCTION !$#pathway protein biosynthesis !$#note binds 23S rRNA CLASSIFICATION #superfamily Escherichia coli ribosomal protein L20 KEYWORDS protein biosynthesis; ribosome; RNA binding FEATURE !$2-118 #product ribosomal protein L20 #status experimental !8#label MAT SUMMARY #length 118 #molecular-weight 13497 #checksum 1313 SEQUENCE /// ENTRY R5BS20 #type complete TITLE ribosomal protein L20 - Bacillus stearothermophilus ORGANISM #formal_name Bacillus stearothermophilus DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S05348 REFERENCE S05346 !$#authors Pon, C.L.; Brombach, M.; Thamm, S.; Gualerzi, C.O. !$#journal Mol. Gen. Genet. (1989) 218:355-357 !$#title Cloning and characterization of a gene cluster from Bacillus !1stearothermophilus comprising infC, rpmI and rplT. !$#cross-references MUID:89384464; PMID:2779520 !$#accession S05348 !'##molecule_type DNA !'##residues 1-119 ##label PON !'##cross-references EMBL:X16188; NID:g39960; PIDN:CAA34314.1; !1PID:g39963 GENETICS !$#gene rplT CLASSIFICATION #superfamily Escherichia coli ribosomal protein L20 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 119 #molecular-weight 13664 #checksum 1494 SEQUENCE /// ENTRY R5KT20 #type complete TITLE ribosomal protein L20, cyanelle - Cyanophora paradoxa cyanelle ORGANISM #formal_name cyanelle Cyanophora paradoxa DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S07071; T06850 REFERENCE S07067 !$#authors Bryant, D.A.; Stirewalt, V.L. !$#journal FEBS Lett. (1990) 259:273-280 !$#title The cyanelle genome of Cyanophora paradoxa encodes ribosomal !1proteins not encoded by the chloroplast genomes of higher !1plants. !$#cross-references MUID:90092562; PMID:2403527 !$#accession S07071 !'##molecule_type DNA !'##residues 1-114 ##label BRY !'##cross-references EMBL:X17063; NID:g11291; PIDN:CAA34908.1; !1PID:g11293 REFERENCE Z15840 !$#authors Stirewalt, V.L.; Michalowski, C.B.; Luffelhardt, W.; !1Bohnert, H.J.; Bryant, D.A. !$#submission submitted to the EMBL Data Library, July 1995 !$#description Nucleotide sequence of the cyanelle genome from Cyanophora !1paradoxa. !$#accession T06850 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-114 ##label STI !'##cross-references EMBL:U30821; NID:g1016083; PIDN:AAA81193.1; !1PID:g1016106 !'##experimental_source strain Pringsheim LB555 GENETICS !$#gene rpl20; rplT !$#map_position 27 !$#genome cyanelle CLASSIFICATION #superfamily Escherichia coli ribosomal protein L20 KEYWORDS cyanelle; protein biosynthesis; ribosome SUMMARY #length 114 #molecular-weight 13355 #checksum 1709 SEQUENCE /// ENTRY R5KM20 #type complete TITLE ribosomal protein L20, chloroplast - Chlamydomonas reinhardtii chloroplast ORGANISM #formal_name chloroplast Chlamydomonas reinhardtii DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 22-Jun-1999 ACCESSIONS S18026 REFERENCE S18026 !$#authors Yu, W.; Zhang, D.; Spreitzer, R.J. !$#submission submitted to the EMBL Data Library, October 1991 !$#description Sequences of the trnS and rpl20 genes of the Chlamydomonas !1reinhardtii chloroplast genome. !$#accession S18026 !'##molecule_type DNA !'##residues 1-112 ##label YUW !'##cross-references EMBL:X62566; NID:g11463; PIDN:CAA44439.1; !1PID:g11464 !'##experimental_source strain 2137 mt+ GENETICS !$#gene rpl20 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein L20 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 112 #molecular-weight 13548 #checksum 5041 SEQUENCE /// ENTRY R5EG20 #type complete TITLE ribosomal protein L20 - Euglena gracilis chloroplast ORGANISM #formal_name chloroplast Euglena gracilis DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S07387; S34511; S34878 REFERENCE S07387 !$#authors Manzara, T.; Hallick, R.B. !$#journal Nucleic Acids Res. (1987) 15:3927 !$#title Nucleotide sequence of the Euglena gracilis chloroplast gene !1for ribosomal protein L20. !$#cross-references MUID:87231087; PMID:3108862 !$#accession S07387 !'##molecule_type DNA !'##residues 1-124 ##label MAN !'##cross-references EMBL:Y00143; NID:g11498; PIDN:CAA68338.1; !1PID:g11499 REFERENCE S34494 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.; Monfort, !1A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#submission submitted to the EMBL Data Library, January 1993 !$#description The complete sequence of the Euglena gracilis chloroplast !1genome (tentative). !$#accession S34511 !'##molecule_type DNA !'##residues 1-124 ##label HAL1 !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50090.1; !1PID:g415746 REFERENCE S34862 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.R.; !1Monfort, A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#journal Nucleic Acids Res. (1993) 21:3537-3544 !$#title Complete sequence of Euglena gracilis chloroplast DNA. !$#cross-references MUID:93347989; PMID:8346031 !$#accession S34878 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-124 ##label HAL2 !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50090.1; !1PID:g415746 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1993 GENETICS !$#gene rpl20 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein L20 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 124 #molecular-weight 14671 #checksum 9729 SEQUENCE /// ENTRY R5LV20 #type complete TITLE ribosomal protein L20 - liverwort (Marchantia polymorpha) chloroplast ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 22-Jun-1999 ACCESSIONS A02807; S01547 REFERENCE A00150 !$#authors Ohyama, K. !$#submission submitted to the EMBL Data Library, October 1986 !$#accession A02807 !'##molecule_type DNA !'##residues 1-116 ##label OHY REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features REFERENCE S01529 !$#authors Fukuzawa, H.; Kohchi, T.; Sano, T.; Shirai, H.; Umesono, K.; !1Inokuchi, H.; Ozeki, H.; Ohyama, K. !$#journal J. Mol. Biol. (1988) 203:333-351 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. III. Gene organization of the large !1single copy region from rbcL to trnI(CAU). !$#cross-references MUID:89068687; PMID:3199436 !$#accession S01547 !'##molecule_type DNA !'##residues 1-116 ##label FUK !'##cross-references GB:X04465; GB:Y00686; NID:g11640; PIDN:CAA28108.1; !1PID:g11696 GENETICS !$#gene rpl20 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein L20 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 116 #molecular-weight 13606 #checksum 1153 SEQUENCE /// ENTRY R5NT20 #type complete TITLE ribosomal protein L20 - common tobacco chloroplast ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 17-Feb-1995 ACCESSIONS A02808 REFERENCE A00149 !$#authors Sugiura, M. !$#submission submitted to the EMBL Data Library, August 1986 !$#accession A02808 !'##molecule_type DNA !'##residues 1-128 ##label SUG !'##experimental_source cv. Bright Yellow 4 REFERENCE A38013 !$#authors Shinozaki, K.; Ohme, M.; Tanaka, M.; Wakasugi, T.; !1Hayashida, N.; Matsubayashi, T.; Zaita, N.; Chunwongse, J.; !1Obokata, J.; Yamaguchi-Shinozaki, K.; Ohto, C.; Torazawa, !1K.; Meng, B.Y.; Sugita, M.; Deno, H.; Kamogashira, T.; !1Yamada, K.; Kusuda, J.; Takaiwa, F.; Kato, A.; Tohdoh, N.; !1Shimada, H.; Sugiura, M. !$#journal EMBO J. (1986) 5:2043-2049 !$#title The complete nucleotide sequence of the tobacco chloroplast !1genome: its gene organization and expression. !$#contents annotation; gene organization, sites, features GENETICS !$#gene rpl20 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein L20 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 128 #molecular-weight 15541 #checksum 1915 SEQUENCE /// ENTRY R5RZ20 #type complete TITLE ribosomal protein L20 - rice chloroplast ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 22-Jun-1999 ACCESSIONS JQ0249; S05129 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0249 !'##molecule_type DNA !'##residues 1-119 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05129 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-119 ##label HIR !'##cross-references GB:X15901; NID:g11957; PIDN:CAA33971.1; PID:g12010 !'##experimental_source cv. Nihonbare !'##note this sequence was submitted to EMBL, July 1989 GENETICS !$#gene rpl20 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein L20 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 119 #molecular-weight 14346 #checksum 7453 SEQUENCE /// ENTRY R5ZM20 #type complete TITLE ribosomal protein L20 - maize chloroplast ORGANISM #formal_name chloroplast Zea mays #common_name maize DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 22-Jun-1999 ACCESSIONS S19128; S58574; S16735 REFERENCE S19126 !$#authors Wegloehner, W.; Subramanian, A.R. !$#journal Plant Mol. Biol. (1992) 18:415-418 !$#title Nucleotide sequence of a region of maize chloroplast DNA !1containing the 3' end of clpP, exon 1 of rps12 and rpl20 and !1their cotranscription. !$#cross-references MUID:92119264; PMID:1732000 !$#accession S19128 !'##molecule_type DNA !'##residues 1-119 ##label WEG !'##cross-references EMBL:X60548; NID:g12413; PIDN:CAA43040.1; !1PID:g12416 REFERENCE S58531 !$#authors Maier, R.M.; Neckermann, K.; Igloi, G.L.; Koessel, H. !$#journal J. Mol. Biol. (1995) 251:614-628 !$#title Complete sequence of the maize chloroplast genome: gene !1content, hotspots of divergence and fine tuning of genetic !1information by transcript editing. !$#cross-references MUID:95395841; PMID:7666415 !$#accession S58574 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-119 ##label MAI !'##cross-references EMBL:X86563; NID:g902200; PIDN:CAA60308.1; !1PID:g902244 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1995 GENETICS !$#gene rpl20 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein L20 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 119 #molecular-weight 14240 #checksum 8234 SEQUENCE /// ENTRY R5RT21 #type complete TITLE ribosomal protein L21, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 21-Jul-2000 ACCESSIONS A33295; A34990; S21396 REFERENCE A33295 !$#authors Devi, K.R.G.; Chan, Y.L.; Wool, I.G. !$#journal Biochem. Biophys. Res. Commun. (1989) 162:364-370 !$#title The primary structure of rat ribosomal protein L21. !$#cross-references MUID:89322268; PMID:2751657 !$#accession A33295 !'##molecule_type mRNA !'##residues 1-160 ##label DEV !'##cross-references EMBL:M27905; NID:g205118; PIDN:AAA41504.1; !1PID:g205119; EMBL:X15216; NID:g57685; PID:g57686 !$#accession A34990 !'##molecule_type protein !'##residues 2-46 ##label DEV2 !'##note the protein is designated as ribosomal protein L21 CLASSIFICATION #superfamily rat ribosomal protein L21 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-160 #product ribosomal protein L21 #status experimental !8#label MAT SUMMARY #length 160 #molecular-weight 18466 #checksum 5307 SEQUENCE /// ENTRY R5EC21 #type complete TITLE ribosomal protein L21 [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1979 #sequence_revision 31-Dec-1979 #text_change 01-Mar-2002 ACCESSIONS JS0766; A02809; D65109 REFERENCE JS0766 !$#authors Kitakawa, M.; Jeong, J.; Isono, S.; Isono, K. !$#submission submitted to JIPID, September 1992 !$#accession JS0766 !'##molecule_type DNA !'##residues 1-103 ##label KIT !'##cross-references DDBJ:D13267; NID:g216635; PIDN:BAA02525.1; !1PID:g216636 !'##experimental_source strain K12 REFERENCE A02809 !$#authors Heiland, I.; Wittmann-Liebold, B. !$#journal Biochemistry (1979) 18:4605-4612 !$#title Amino acid sequence of the ribosomal protein L21 of !1Escherichia coli. !$#cross-references MUID:80042967; PMID:387076 !$#accession A02809 !'##molecule_type protein !'##residues 1-103 ##label HEI REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65109 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-103 ##label BLAT !'##cross-references GB:AE000399; GB:U00096; NID:g2367201; !1PIDN:AAC76218.1; PID:g1789577; UWGP:b3186 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note no post-translational modifications were observed in mass !1spectrographic analysis; any acid labile modifications may !1have been missed GENETICS !$#gene rplU !$#map_position 69 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX large subunit ribosomal proteins: L1 (PIR:R5EC1), L3 !1(PIR:R5EC3), L2 (PIR:R5EC2), L4 (PIR:R5EC4), L5 (PIR:R5EC5), !1L6 (PIR:R5EC6), L7/L12 (PIR:R5EC7), L9 (PIR:R5EC9), L10 !1(PIR:R5EC10), L11 (PIR:R5EC11), L13 (PIR:R5EC13), L14 !1(PIR:R5EC14), L15 (PIR:R5EC15), L16 (PIR:R5EC16), L17 !1(PIR:R5EC17), L18 (PIR:R5EC18), L19 (PIR:R5EC19) FUNCTION !$#pathway protein biosynthesis !$#note binds 23S rRNA in the presence of protein L20 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L21 KEYWORDS protein biosynthesis; ribosome FEATURE !$1-103 #product ribosomal protein L21 #status experimental !8#label MAT SUMMARY #length 103 #molecular-weight 11564 #checksum 7276 SEQUENCE /// ENTRY S18439 #type complete TITLE ribosomal protein L21 - Bacillus subtilis ALTERNATE_NAMES ribosomal protein BL20; rplU ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S18439; G69696 REFERENCE S18437 !$#authors Cutting, S.; Roels, S.; Losick, R. !$#journal J. Mol. Biol. (1991) 221:1237-1256 !$#title Sporulation operon spoIVF and the characterization of !1mutations that uncouple mother-cell from forespore gene !1expression in Bacillus subtilis. !$#cross-references MUID:92046062; PMID:1942049 !$#accession S18439 !'##molecule_type DNA !'##residues 1-102 ##label CUT !'##cross-references EMBL:X59528; NID:g40170; PIDN:CAA42108.1; !1PID:g40173 !'##experimental_source strain KS179, congenic derivative of strain PY79 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69696 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-102 ##label KUN !'##cross-references GB:Z99118; GB:AL009126; NID:g2635200; !1PIDN:CAB14756.1; PID:g2635261 !'##experimental_source strain 168 GENETICS !$#gene rplU CLASSIFICATION #superfamily Escherichia coli ribosomal protein L21 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 102 #molecular-weight 11275 #checksum 5426 SEQUENCE /// ENTRY R5LV21 #type complete TITLE ribosomal protein L21, chloroplast - liverwort (Marchantia polymorpha) chloroplast ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 22-Jun-1999 ACCESSIONS A02810; S01513 REFERENCE A00150 !$#authors Ohyama, K. !$#submission submitted to the EMBL Data Library, October 1986 !$#accession A02810 !'##molecule_type DNA !'##residues 1-116 ##label OHY REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features REFERENCE S01512 !$#authors Kohchi, T.; Shirai, H.; Fukuzawa, H.; Sano, T.; Komano, T.; !1Umesono, K.; Inokuchi, H.; Ozeki, H.; Ohyama, K. !$#journal J. Mol. Biol. (1988) 203:353-372 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. IV. Inverted repeat and small single !1copy regions. !$#cross-references MUID:89068688; PMID:3199437 !$#accession S01513 !'##molecule_type DNA !'##residues 1-116 ##label KOH !'##cross-references GB:X04465; GB:Y00686; NID:g11640; PIDN:CAA28130.1; !1PID:g11719 GENETICS !$#gene rpl21 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein L21 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 116 #molecular-weight 13626 #checksum 5531 SEQUENCE /// ENTRY S75901 #type complete TITLE ribosomal protein L21 - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein slr1678 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S75901 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75901 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-124 ##label KAN !'##cross-references EMBL:D90913; GB:AB001339; NID:g1653348; !1PIDN:BAA18360.1; PID:g1653446 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene rpl21 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L21 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 124 #molecular-weight 13669 #checksum 7070 SEQUENCE /// ENTRY A48103 #type complete TITLE ribosomal protein L21 precursor, chloroplast - spinach ORGANISM #formal_name Spinacia oleracea #common_name spinach DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A48103; S13527; A37906 REFERENCE A48103 !$#authors Lagrange, T.; Franzetti, B.; Axelos, M.; Mache, R.; !1Lerbs-Mache, S. !$#journal Mol. Cell. Biol. (1993) 13:2614-2622 !$#title Structure and expression of the nuclear gene coding for the !1chloroplast ribosomal protein L21: developmental regulation !1of a housekeeping gene by alternative promoters. !$#cross-references MUID:93205007; PMID:8455634 !$#accession A48103 !'##status preliminary !'##molecule_type DNA !'##residues 1-256 ##label LAG !'##cross-references GB:M64682; NID:g310589; PIDN:AAA74715.1; !1PID:g310590 !'##note sequence extracted from NCBI backbone (NCBIN:127727, !1NCBIP:127728) REFERENCE S13527 !$#authors Martin, W.; Lagrange, T.; Li, Y.F.; Bisanz-Seyer, C.; Mache, !1R. !$#journal Curr. Genet. (1990) 18:553-556 !$#title Hypothesis for the evolutionary origin of the chloroplast !1ribosomal protein L21 of spinach. !$#cross-references MUID:91168304; PMID:2076556 !$#accession S13527 !'##molecule_type mRNA !'##residues 1-256 ##label MAR !'##cross-references EMBL:X56691; NID:g21314; PIDN:CAA40019.1; !1PID:g21315 REFERENCE A37906 !$#authors Smooker, P.M.; Kruft, V.; Subramanian, A.R. !$#journal J. Biol. Chem. (1990) 265:16699-16703 !$#title A ribosomal protein is encoded in the chloroplast DNA in a !1lower plant but in the nucleus in angiosperms. Isolation of !1the spinach L21 protein and cDNA clone with transit and an !1unusual repeat sequence. !$#cross-references MUID:90375547; PMID:2398071 !$#accession A37906 !'##molecule_type mRNA !'##residues 1-256 ##label SMO !'##cross-references GB:M57413; GB:M31763; NID:g170134; PIDN:AAA34041.1; !1PID:g170135 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L21 KEYWORDS chloroplast; protein biosynthesis; ribosome FEATURE !$1-55 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$56-256 #product ribosomal protein L21 #status predicted !8#label MAT SUMMARY #length 256 #molecular-weight 28408 #checksum 718 SEQUENCE /// ENTRY S71282 #type complete TITLE ribosomal protein L21 precursor, chloroplast - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S71282 REFERENCE S71282 !$#authors Rajasekhar, V.K.; Weihe, A. !$#submission submitted to the EMBL Data Library, May 1995 !$#description Nucleotide sequence of chloroplast RPL21 from Arabidopsis !1thaliana. !$#accession S71282 !'##molecule_type mRNA !'##residues 1-220 ##label RAJ !'##cross-references EMBL:Z49787; NID:g1149572; PIDN:CAA89887.1; !1PID:g1149573 GENETICS !$#gene rpl21 !$#genome nuclear CLASSIFICATION #superfamily Escherichia coli ribosomal protein L21 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 220 #molecular-weight 24038 #checksum 9197 SEQUENCE /// ENTRY S73130 #type complete TITLE ribosomal protein L21, chloroplast - red alga (Porphyra purpurea) chloroplast ORGANISM #formal_name chloroplast Porphyra purpurea DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S73130 REFERENCE S73108 !$#authors Reith, M.; Munholland, J. !$#journal Plant Mol. Biol. Rep. (1995) 13:333-335 !$#title Complete nucleotide sequence of the Porphyra purpurea !1chloroplast genome. !$#accession S73130 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-104 ##label REI !'##cross-references EMBL:U38804; NID:g1276652; PIDN:AAC08095.1; !1PID:g1276675 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1995 GENETICS !$#gene rpl21 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein L21 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 104 #molecular-weight 11877 #checksum 1280 SEQUENCE /// ENTRY R5HU22 #type complete TITLE ribosomal protein L17, cytosolic - human ALTERNATE_NAMES ribosomal protein HL23 ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 22-Jun-1999 ACCESSIONS S11218 REFERENCE S11218 !$#authors Mager, D.L.; Freeman, J.D. !$#journal Nucleic Acids Res. (1990) 18:5301 !$#title A human gene related to the ribosomal protein L23 gene of !1Halobacterium marismortui. !$#cross-references MUID:90384852; PMID:2402465 !$#accession S11218 !'##molecule_type mRNA !'##residues 1-184 ##label MAG !'##cross-references EMBL:X53777; NID:g34198; PIDN:CAA37793.1; !1PID:g34199 GENETICS !$#gene GDB:RPL17 !'##cross-references GDB:128738 !$#map_position 1p31-1p31 CLASSIFICATION #superfamily rat ribosomal protein L17 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 184 #molecular-weight 21397 #checksum 4281 SEQUENCE /// ENTRY R5RT17 #type complete TITLE ribosomal protein L17, cytosolic [validated] - rat ALTERNATE_NAMES ribosomal protein RL22 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 21-Jul-2000 ACCESSIONS JN0078; A39231; S30574; A40965; S14608 REFERENCE JN0078 !$#authors Suzuki, K.; Wool, I.G. !$#journal Biochem. Biophys. Res. Commun. (1991) 178:322-328 !$#title The primary structure of rat ribosomal protein L17. !$#cross-references MUID:91298968; PMID:2069571 !$#accession JN0078 !'##molecule_type mRNA !'##residues 1-184 ##label SUZ !'##cross-references EMBL:X58389; NID:g57681; PIDN:CAA41278.1; !1PID:g57682 !'##note the protein is designated as ribosomal protein L17 according to !1comigration analysis after in vitro translation REFERENCE A39231 !$#authors Shay, N.F.; Nick, H.S.; Kilberg, M.S. !$#journal J. Biol. Chem. (1990) 265:17844-17848 !$#title Molecular cloning of an amino acid-regulated mRNA (amino !1acid starvation-induced) in rat hepatoma cells. !$#cross-references MUID:91009249; PMID:2211664 !$#accession A39231 !'##molecule_type mRNA !'##residues 65-184 ##label SHA !'##cross-references EMBL:M60478; NID:g202989; PIDN:AAA40765.1; !1PID:g202990 REFERENCE S30574 !$#authors Laine, R.O.; Laipis, P.J.; Shay, N.F.; Kilberg, M.S. !$#submission submitted to the EMBL Data Library, June 1991 !$#description Identification of an amino acid-regulated mRNA (ASI) from !1rat liver as the mammalian equivalent of bacterial ribosomal !1protein L22. !$#accession S30574 !'##molecule_type mRNA !'##residues 1-184 ##label LAI !'##cross-references EMBL:X60212; NID:g57110; PIDN:CAA42765.1; !1PID:g57111 REFERENCE A40965 !$#authors Laine, R.O.; Laipis, P.J.; Shay, N.F.; Kilberg, M.S. !$#journal J. Biol. Chem. (1991) 266:16969-16972 !$#title Identification of an amino acid-regulated mRNA from rat !1liver as the mammalian equivalent of bacterial ribosomal !1protein L22. !$#cross-references MUID:91373298; PMID:1894596 !$#accession A40965 !'##status preliminary; nucleic acid sequence not shown; not compared !1with conceptual translation !'##molecule_type mRNA !'##residues 1-60,'PP',63-117,'N',119-184 ##label LA2 CLASSIFICATION #superfamily rat ribosomal protein L17 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 184 #molecular-weight 21397 #checksum 3957 SEQUENCE /// ENTRY R5HS22 #type complete TITLE ribosomal protein L22 [validated] - Haloarcula marismortui ALTERNATE_NAMES ribosomal protein HL17; ribosomal protein HL23 ORGANISM #formal_name Haloarcula marismortui DATE 31-Mar-1991 #sequence_revision 12-Apr-1996 #text_change 04-Feb-2000 ACCESSIONS H35063; C28926; S02395 REFERENCE A35063 !$#authors Arndt, E.; Kroemer, W.; Hatakeyama, T. !$#journal J. Biol. Chem. (1990) 265:3034-3039 !$#title Organization and nucleotide sequence of a gene cluster !1coding for eight ribosomal proteins in the archaebacterium !1Halobacterium marismortui. !$#cross-references MUID:90153945; PMID:2406244 !$#accession H35063 !'##molecule_type DNA !'##residues 1-155 ##label ARN !'##cross-references EMBL:J05222; NID:g148800; PIDN:AAA86864.1; !1PID:g148806 REFERENCE A28926 !$#authors Walsh, M.J.; McDougall, J.; Wittmann-Liebold, B. !$#journal Biochemistry (1988) 27:6867-6876 !$#title Extended N-terminal sequencing of proteins of !1archaebacterial ribosomes blotted from two-dimensional gels !1onto glass fiber and poly(vinylidene difluoride) membrane. !$#cross-references MUID:89062418; PMID:3196689 !$#accession C28926 !'##molecule_type protein !'##residues 2-10,'X',12-27 ##label WAL !'##note the protein is designated as ribosomal protein L17 REFERENCE S02394 !$#authors Hatakeyama, T.; Hatakeyama, T.; Kimura, M. !$#journal FEBS Lett. (1988) 240:21-28 !$#title The primary structures of ribosomal proteins L16, L23 and !1L33 from the archaebacterium Halobacterium marismortui. !$#cross-references MUID:89052888; PMID:3191994 !$#accession S02395 !'##molecule_type protein !'##residues 2-155 ##label HAT !'##note the source is designated as Halobacterium marismortui !'##note the protein is designated as ribosomal protein L23 CLASSIFICATION #superfamily rat ribosomal protein L17 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-155 #product ribosomal protein L22 #status experimental !8#label MAT SUMMARY #length 155 #molecular-weight 16941 #checksum 9573 SEQUENCE /// ENTRY R5HSH2 #type complete TITLE ribosomal protein L22 [validated] - Halobacterium salinarum ALTERNATE_NAMES ribosomal protein HL23 ORGANISM #formal_name Halobacterium salinarum DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 21-Jul-2000 ACCESSIONS S03883; T43821; S08557 REFERENCE S03882 !$#authors Mankin, A.S. !$#journal FEBS Lett. (1989) 246:13-16 !$#title The nucleotide sequence of the genes coding for the S19 and !1L22 equivalent ribosomal proteins from Halobacterium !1halobium. !$#cross-references MUID:89211383; PMID:2651152 !$#accession S03883 !'##molecule_type DNA !'##residues 1-156 ##label MAN !'##cross-references EMBL:X14967; NID:g43549; PIDN:CAA33092.1; !1PID:g43551 !'##note the source is designated as Halobacterium halobium REFERENCE Z22697 !$#authors Itoh, T. !$#submission submitted to the EMBL Data Library, September 1997 !$#accession T43821 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-156 ##label ITO !'##cross-references EMBL:AB006961; PIDN:BAA22275.1 !'##note the source is designated as Halobacterium halobium REFERENCE S07437 !$#authors Matheson, A.T.; Yaguchi, M.; Christensen, P.; Rollin, C.F.; !1Hasnain, S. !$#journal Can. J. Biochem. Cell Biol. (1984) 62:426-433 !$#title Purification, properties, and N-terminal amino acid sequence !1of certain 50S ribosomal subunit proteins from the !1archaebacterium Halobacterium cutirubrum. !$#cross-references MUID:84282108; PMID:6467081 !$#accession S08557 !'##molecule_type protein !'##residues 2-3,'F',5-9,'B',11-12,'M',14,'R',16-22,'G',24,'X',26-28 !1##label MATH !'##note the source is designated as Halobacterium cutirubrum !'##note the protein is designated as ribosomal protein L23 GENETICS !$#gene HhaL22 CLASSIFICATION #superfamily rat ribosomal protein L17 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-156 #product ribosomal protein L22 #status experimental !8#label MAT SUMMARY #length 156 #molecular-weight 17145 #checksum 6347 SEQUENCE /// ENTRY R5EC22 #type complete TITLE ribosomal protein L22 [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 28-Feb-1981 #sequence_revision 28-Feb-1981 #text_change 01-Mar-2002 ACCESSIONS G23129; A02811; F65124 REFERENCE A23129 !$#authors Zurawski, G.; Zurawski, S.M. !$#journal Nucleic Acids Res. (1985) 13:4521-4526 !$#title Structure of the Escherichia coli S10 ribosomal protein !1operon. !$#cross-references MUID:85242118; PMID:3892488 !$#accession G23129 !'##molecule_type DNA !'##residues 1-110 ##label ZUR !'##cross-references GB:X02613; NID:g42825; PIDN:CAA26465.1; PID:g42831 REFERENCE A02811 !$#authors Wittmann-Liebold, B.; Greuer, B. !$#journal FEBS Lett. (1980) 121:105-112 !$#title Amino acid sequence of protein L22 from the large subunit of !1the Escherichia coli ribosome. !$#cross-references MUID:81114579; PMID:7007072 !$#accession A02811 !'##molecule_type protein !'##residues 1-110 ##label WIT REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65124 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-110 ##label BLAT !'##cross-references GB:AE000408; GB:U00096; NID:g1789694; !1PIDN:AAC76340.1; PID:g1789711; UWGP:b3315 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note no post-translational modifications were observed in mass !1spectrographic analysis; any acid labile modifications may !1have been missed GENETICS !$#gene rplV !$#map_position 73 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX large subunit ribosomal proteins: L1 (PIR:R5EC1), L3 !1(PIR:R5EC3), L2 (PIR:R5EC2), L4 (PIR:R5EC4), L5 (PIR:R5EC5), !1L6 (PIR:R5EC6), L7/L12 (PIR:R5EC7), L9 (PIR:R5EC9), L10 !1(PIR:R5EC10), L11 (PIR:R5EC11), L13 (PIR:R5EC13), L14 !1(PIR:R5EC14), L15 (PIR:R5EC15), L16 (PIR:R5EC16), L17 !1(PIR:R5EC17), L18 (PIR:R5EC18), L19 (PIR:R5EC19) FUNCTION !$#pathway protein biosynthesis !$#note binds 23S rRNA CLASSIFICATION #superfamily Escherichia coli ribosomal protein L22 KEYWORDS protein biosynthesis; ribosome; RNA binding FEATURE !$1-110 #product ribosomal protein L22 #status experimental !8#label MAT SUMMARY #length 110 #molecular-weight 12226 #checksum 6249 SEQUENCE /// ENTRY R5YM22 #type complete TITLE ribosomal protein L22 - Mycoplasma capricolum ALTERNATE_NAMES protein MC008 ORGANISM #formal_name Mycoplasma capricolum DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 07-Dec-1999 ACCESSIONS S02836; S77858; S48574 REFERENCE S02830 !$#authors Ohkubo, S.; Muto, A.; Kawauchi, Y.; Yamao, F.; Osawa, S. !$#journal Mol. Gen. Genet. (1987) 210:314-322 !$#title The ribosomal protein gene cluster of Mycoplasma capricolum. !$#cross-references MUID:88142549; PMID:3481422 !$#accession S02836 !'##molecule_type DNA !'##residues 1-111 ##label OHK !'##cross-references EMBL:X06414; NID:g44207; PIDN:CAA29709.1; !1PID:g44214 !'##experimental_source ATCC 27343 REFERENCE S77739 !$#authors Bork, P.; Ouzounis, C.; Casari, G.; Schneider, R.; Sander, !1C.; Dolan, M.; Gilbert, W.; Gillevet, P.M. !$#journal Mol. Microbiol. (1995) 16:955-967 !$#title Exploring the Mycoplasma capricolum genome: a minimal cell !1reveals its physiology. !$#cross-references MUID:96059641; PMID:7476192 !$#accession S77858 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 64-111 ##label BOW !'##cross-references EMBL:Z33011; NID:g541684; PIDN:CAA83691.1; !1PID:g950058 !'##experimental_source ATCC 27343 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1994 GENETICS !$#gene rpl22 !$#genetic_code SGC3 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L22 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 111 #molecular-weight 12373 #checksum 9372 SEQUENCE /// ENTRY R5LV22 #type complete TITLE ribosomal protein L22 - liverwort (Marchantia polymorpha) chloroplast ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 22-Jun-1999 ACCESSIONS A02812; S01557 REFERENCE A00150 !$#authors Ohyama, K. !$#submission submitted to the EMBL Data Library, October 1986 !$#accession A02812 !'##molecule_type DNA !'##residues 1-119 ##label OHY REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features REFERENCE S01529 !$#authors Fukuzawa, H.; Kohchi, T.; Sano, T.; Shirai, H.; Umesono, K.; !1Inokuchi, H.; Ozeki, H.; Ohyama, K. !$#journal J. Mol. Biol. (1988) 203:333-351 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. III. Gene organization of the large !1single copy region from rbcL to trnI(CAU). !$#cross-references MUID:89068687; PMID:3199436 !$#accession S01557 !'##molecule_type DNA !'##residues 1-119 ##label FUK !'##cross-references GB:X04465; GB:Y00686; NID:g11640; PIDN:CAA28125.1; !1PID:g11714 GENETICS !$#gene rpl22 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein L22 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 119 #molecular-weight 13581 #checksum 4932 SEQUENCE /// ENTRY R5NT22 #type complete TITLE ribosomal protein L22 - common tobacco chloroplast ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 17-Feb-1995 ACCESSIONS A02813; D25943 REFERENCE A00149 !$#authors Sugiura, M. !$#submission submitted to the EMBL Data Library, August 1986 !$#accession A02813 !'##molecule_type DNA !'##residues 1-155 ##label SUG !'##experimental_source cv. Bright Yellow 4 REFERENCE A38013 !$#authors Shinozaki, K.; Ohme, M.; Tanaka, M.; Wakasugi, T.; !1Hayashida, N.; Matsubayashi, T.; Zaita, N.; Chunwongse, J.; !1Obokata, J.; Yamaguchi-Shinozaki, K.; Ohto, C.; Torazawa, !1K.; Meng, B.Y.; Sugita, M.; Deno, H.; Kamogashira, T.; !1Yamada, K.; Kusuda, J.; Takaiwa, F.; Kato, A.; Tohdoh, N.; !1Shimada, H.; Sugiura, M. !$#journal EMBO J. (1986) 5:2043-2049 !$#title The complete nucleotide sequence of the tobacco chloroplast !1genome: its gene organization and expression. !$#contents annotation; gene organization, sites, features REFERENCE A94118 !$#authors Tanaka, M.; Wakasugi, T.; Sugita, M.; Shinozaki, K.; !1Sugiura, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:6030-6034 !$#title Genes for the eight ribosomal proteins are clustered on the !1chloroplast genome of tobacco (Nicotiana tabacum): !1similarity to the S10 and spc operons of Escherichia coli. !$#cross-references MUID:86287388; PMID:3016736 !$#accession D25943 !'##molecule_type DNA !'##residues 1-155 ##label TAN GENETICS !$#gene rpl22 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein L22 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 155 #molecular-weight 17769 #checksum 916 SEQUENCE /// ENTRY R5SP22 #type complete TITLE ribosomal protein L22 - spinach chloroplast ALTERNATE_NAMES ribosomal protein CS-L13 ORGANISM #formal_name chloroplast Spinacia oleracea #common_name spinach DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S01977; S20559 REFERENCE S01976 !$#authors Zhou, D.X.; Quigley, F.; Massenet, O.; Mache, R. !$#journal Mol. Gen. Genet. (1989) 216:439-445 !$#title Cotranscription of the S10- and spc-like operons in spinach !1chloroplasts and identification of three of their gene !1products. !$#cross-references MUID:89313684; PMID:2747623 !$#accession S01977 !'##molecule_type DNA !'##residues 1-199 ##label ZHO !'##cross-references EMBL:X13336; NID:g12307; PIDN:CAA31714.1; !1PID:g12309 !$#accession S20559 !'##molecule_type protein !'##residues 3-11 ##label ZHO2 GENETICS !$#gene rpl22 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein L22 KEYWORDS chloroplast; protein biosynthesis; ribosome; RNA binding FEATURE !$3-199 #product ribosomal protein L22 #status experimental !8#label MAT SUMMARY #length 199 #molecular-weight 23245 #checksum 9349 SEQUENCE /// ENTRY R5RZ22 #type complete TITLE ribosomal protein L22 - rice chloroplast ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 22-Jun-1999 ACCESSIONS JQ0266; S05146 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0266 !'##molecule_type DNA !'##residues 1-149 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05146 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-149 ##label HIR !'##cross-references GB:X15901; NID:g11957; PIDN:CAA33935.1; PID:g12026 !'##experimental_source cv. Nihonbare !'##note this sequence was submitted to EMBL, July 1989 GENETICS !$#gene rpl22 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein L22 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 149 #molecular-weight 17683 #checksum 2699 SEQUENCE /// ENTRY R5KK22 #type complete TITLE ribosomal protein L22 - red alga (Gracilaria tenuistipitata) chloroplast ORGANISM #formal_name chloroplast Gracilaria tenuistipitata DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 30-Jun-1993 ACCESSIONS S12811; JH0186 REFERENCE S12811 !$#authors Kao, J.; Wu, M. !$#journal Nucleic Acids Res. (1990) 18:3067 !$#title The sequence of the plastid encoded rpl22 protein in marine !1macroalgae, Gracilaria tenuistipitata. !$#cross-references MUID:90272431; PMID:2349113 !$#accession S12811 !'##molecule_type DNA !'##residues 1-114 ##label KA1 REFERENCE JH0186 !$#authors Kao, J.S.; Wu, M.; Chiang, Y.M. !$#journal Gene (1990) 90:221-226 !$#title Cloning and characterization of chloroplast ribosomal !1protein-encoding genes, rpl16 and rps3, of the marine !1macro-algae, Gracilaria tenuistipitata. !$#cross-references MUID:90382669; PMID:2401402 !$#accession JH0186 !'##molecule_type DNA !'##residues 78-82,'P',84-114 ##label KA2 !'##cross-references GB:M32638 GENETICS !$#gene rpl22 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein L22 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 114 #molecular-weight 13106 #checksum 783 SEQUENCE /// ENTRY R5EC23 #type complete TITLE ribosomal protein L23 [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 28-Feb-1980 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS A65125; D23129; A02814 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65125 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-100 ##label BLAT !'##cross-references GB:AE000408; GB:U00096; NID:g1789694; !1PIDN:AAC76343.1; PID:g1789714; UWGP:b3318 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A23129 !$#authors Zurawski, G.; Zurawski, S.M. !$#journal Nucleic Acids Res. (1985) 13:4521-4526 !$#title Structure of the Escherichia coli S10 ribosomal protein !1operon. !$#cross-references MUID:85242118; PMID:3892488 !$#accession D23129 !'##molecule_type DNA !'##residues 1-100 ##label ZUR !'##cross-references GB:X02613; NID:g42825; PIDN:CAA26462.1; PID:g534975 !'##note translation of initiator Met is not shown; the initiator !1overlaps the last codon and terminator of rplW REFERENCE A02814 !$#authors Wittmann-Liebold, B.; Greuer, B. !$#journal FEBS Lett. (1979) 108:69-74 !$#title Primary structure of protein L23 from the Escherichia coli !1ribosome. !$#cross-references MUID:80092111; PMID:391594 !$#accession A02814 !'##molecule_type protein !'##residues 1-79,81-100 ##label WIT !'##experimental_source strain K12 REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note no post-translational modifications were observed in mass !1spectrographic analysis; any acid labile modifications may !1have been missed GENETICS !$#gene rplW !$#map_position 73 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX large subunit ribosomal proteins: L1 (PIR:R5EC1), L3 !1(PIR:R5EC3), L2 (PIR:R5EC2), L4 (PIR:R5EC4), L5 (PIR:R5EC5), !1L6 (PIR:R5EC6), L7/L12 (PIR:R5EC7), L9 (PIR:R5EC9), L10 !1(PIR:R5EC10), L11 (PIR:R5EC11), L13 (PIR:R5EC13), L14 !1(PIR:R5EC14), L15 (PIR:R5EC15), L16 (PIR:R5EC16), L17 !1(PIR:R5EC17), L18 (PIR:R5EC18), L19 (PIR:R5EC19) FUNCTION !$#pathway protein biosynthesis CLASSIFICATION #superfamily Escherichia coli ribosomal protein L23 KEYWORDS protein biosynthesis; ribosome FEATURE !$1-100 #product ribosomal protein L23 #status experimental !8#label MAT SUMMARY #length 100 #molecular-weight 11199 #checksum 6091 SEQUENCE /// ENTRY R5EB23 #type complete TITLE ribosomal protein L23 - Yersinia pseudotuberculosis ORGANISM #formal_name Yersinia pseudotuberculosis DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S04142 REFERENCE S04140 !$#authors Gross, U.; Chen, J.H.; Kono, D.H.; Lobo, J.G.; Yu, D.T.Y. !$#journal Nucleic Acids Res. (1989) 17:3601-3602 !$#title High degree of conservation between ribosomal proteins of !1Yersinia pseudotuberculosis and Escherichia coli. !$#cross-references MUID:89263812; PMID:2657663 !$#accession S04142 !'##molecule_type DNA !'##residues 1-100 ##label GRO !'##cross-references EMBL:X14363; NID:g48644; PIDN:CAA32544.1; !1PID:g48647 GENETICS !$#gene rplW CLASSIFICATION #superfamily Escherichia coli ribosomal protein L23 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 100 #molecular-weight 11230 #checksum 4380 SEQUENCE /// ENTRY G64092 #type complete TITLE ribosomal protein L23 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 23-Oct-1998 #sequence_revision 23-Oct-1998 #text_change 22-Jun-1999 ACCESSIONS G64092 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession G64092 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-99 ##label TIGR !'##cross-references GB:U32761; GB:L42023; NID:g1573780; !1PIDN:AAC22438.1; PID:g1573789; TIGR:HI0779 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L23 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 99 #molecular-weight 10897 #checksum 2688 SEQUENCE /// ENTRY R5BS23 #type complete TITLE ribosomal protein L23 - Bacillus stearothermophilus ORGANISM #formal_name Bacillus stearothermophilus DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 30-Sep-1993 ACCESSIONS A02815 REFERENCE A91149 !$#authors Kimura, M.; Kimura, J.; Ashman, K. !$#journal Eur. J. Biochem. (1985) 150:491-497 !$#title The complete primary structure of ribosomal proteins L1, !1L14, L15, L23, L24, and L29 from Bacillus !1stearothermophilus. !$#cross-references MUID:85257681; PMID:4018095 !$#accession A02815 !'##molecule_type protein !'##residues 1-95 ##label KIM CLASSIFICATION #superfamily Escherichia coli ribosomal protein L23 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 95 #molecular-weight 11083 #checksum 2851 SEQUENCE /// ENTRY A69697 #type complete TITLE ribosomal protein L23 - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 23-Oct-1998 #sequence_revision 23-Oct-1998 #text_change 16-Jun-2000 ACCESSIONS A69697 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69697 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-95 ##label KUN !'##cross-references GB:Z99104; GB:AL009126; NID:g2632267; !1PIDN:CAB11894.1; PID:g2632385 !'##experimental_source strain 168 GENETICS !$#gene rplW CLASSIFICATION #superfamily Escherichia coli ribosomal protein L23 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 95 #molecular-weight 10929 #checksum 1021 SEQUENCE /// ENTRY S40190 #type complete TITLE ribosomal protein L23 - Thermotoga maritima (strain MSB8) ORGANISM #formal_name Thermotoga maritima DATE 23-Oct-1998 #sequence_revision 23-Oct-1998 #text_change 21-Jul-2000 ACCESSIONS S40190; B72250 REFERENCE S37489 !$#authors Sanangelantoni, A.; Tiboni, O. !$#submission submitted to the EMBL Data Library, February 1993 !$#accession S40190 !'##molecule_type DNA !'##residues 1-100 ##label SAN !'##cross-references EMBL:Z21677; NID:g437921; PIDN:CAA79779.1; !1PID:g437925 REFERENCE A72200 !$#authors Nelson, K.E.; Clayton, R.A.; Gill, S.R.; Gwinn, M.L.; !1Dodson, R.J.; Haft, D.H.; Hickey, E.K.; Peterson, J.D.; !1Nelson, W.C.; Ketchum, K.A.; McDonald, L.; Utterback, T.R.; !1Malek, J.A.; Linher, K.D.; Garrett, M.M.; Stewart, A.M.; !1Cotton, M.D.; Pratt, M.S.; Phillips, C.A.; Richardson, D.; !1Heidelberg, J.; Sutton, G.G.; Fleischmann, R.D.; White, O.; !1Salzberg, S.L.; Smith, H.O.; Venter, J.C.; Fraser, C.M. !$#journal Nature (1999) 399:323-329 !$#title Evidence for lateral gene transfer between Archaea and !1Bacteria from genome sequence of Thermotoga maritima. !$#cross-references MUID:99287316; PMID:10360571 !$#accession B72250 !'##molecule_type DNA !'##residues 1-100 ##label ARN !'##cross-references GB:AE001798; GB:AE000512; NID:g4982033; !1PIDN:AAD36564.1; PID:g4982062; TIGR:TM1498 !'##experimental_source strain MSB8 GENETICS !$#gene rplW CLASSIFICATION #superfamily Escherichia coli ribosomal protein L23 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 100 #molecular-weight 11738 #checksum 7902 SEQUENCE /// ENTRY F70300 #type complete TITLE ribosomal protein L23 - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 23-Oct-1998 #sequence_revision 23-Oct-1998 #text_change 22-Jun-1999 ACCESSIONS F70300 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession F70300 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-103 ##label AQF !'##cross-references GB:AE000669; NID:g2982762; PIDN:AAC06397.1; !1PID:g2982771; GB:AE000657 !'##experimental_source strain VF5 GENETICS !$#gene rplW CLASSIFICATION #superfamily Escherichia coli ribosomal protein L23 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 103 #molecular-weight 12371 #checksum 8248 SEQUENCE /// ENTRY R5YM23 #type complete TITLE ribosomal protein L23 - Mycoplasma capricolum ORGANISM #formal_name Mycoplasma capricolum DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 07-Dec-1999 ACCESSIONS S02833 REFERENCE S02830 !$#authors Ohkubo, S.; Muto, A.; Kawauchi, Y.; Yamao, F.; Osawa, S. !$#journal Mol. Gen. Genet. (1987) 210:314-322 !$#title The ribosomal protein gene cluster of Mycoplasma capricolum. !$#cross-references MUID:88142549; PMID:3481422 !$#accession S02833 !'##molecule_type DNA !'##residues 1-94 ##label OHK !'##cross-references EMBL:X06414; NID:g44207; PIDN:CAA29706.1; !1PID:g44211 GENETICS !$#gene rpl23 !$#genetic_code SGC3 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L23 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 94 #molecular-weight 10857 #checksum 302 SEQUENCE /// ENTRY I64216 #type complete TITLE ribosomal protein L23 - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 23-Oct-1998 #sequence_revision 23-Oct-1998 #text_change 07-Dec-1999 ACCESSIONS I64216 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession I64216 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-106 ##label TIGR !'##cross-references GB:U39695; GB:L43967; NID:g1045833; PID:g1045837; !1TIGR:MG153 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L23 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 106 #molecular-weight 11880 #checksum 9410 SEQUENCE /// ENTRY R5HS23 #type complete TITLE ribosomal protein L23 [validated] - Haloarcula marismortui ALTERNATE_NAMES ribosomal protein HL21; ribosomal protein HL25 ORGANISM #formal_name Haloarcula marismortui DATE 30-Jun-1990 #sequence_revision 12-Apr-1996 #text_change 04-Feb-2000 ACCESSIONS E35063; E28926; S00368 REFERENCE A35063 !$#authors Arndt, E.; Kroemer, W.; Hatakeyama, T. !$#journal J. Biol. Chem. (1990) 265:3034-3039 !$#title Organization and nucleotide sequence of a gene cluster !1coding for eight ribosomal proteins in the archaebacterium !1Halobacterium marismortui. !$#cross-references MUID:90153945; PMID:2406244 !$#accession E35063 !'##molecule_type DNA !'##residues 1-85 ##label ARN !'##cross-references EMBL:J05222; NID:g148800; PIDN:AAA86861.1; !1PID:g148803 REFERENCE A28926 !$#authors Walsh, M.J.; McDougall, J.; Wittmann-Liebold, B. !$#journal Biochemistry (1988) 27:6867-6876 !$#title Extended N-terminal sequencing of proteins of !1archaebacterial ribosomes blotted from two-dimensional gels !1onto glass fiber and poly(vinylidene difluoride) membrane. !$#cross-references MUID:89062418; PMID:3196689 !$#accession E28926 !'##molecule_type protein !'##residues 2-23 ##label WAL !'##note the protein is designated as ribosomal protein L21 REFERENCE S00368 !$#authors Hatakeyama, T.; Kimura, M. !$#journal Eur. J. Biochem. (1988) 172:703-711 !$#title Complete amino acid sequences of the ribosomal proteins L25, !1L29 and L31 from the archaebacterium Halobacterium !1marismortui. !$#cross-references MUID:88166754; PMID:3350019 !$#accession S00368 !'##molecule_type protein !'##residues 2-85 ##label HAT !'##note the source is designated as Halobacterium marismortui !'##note the protein is designated as ribosomal protein L25 FUNCTION !$#description binds ribosomal RNA-binding; may be involved in the assembly !1of the large ribosomal subunit CLASSIFICATION #superfamily Escherichia coli ribosomal protein L23 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-85 #product ribosomal protein L23 #status experimental !8#label MAT SUMMARY #length 85 #molecular-weight 9602 #checksum 7058 SEQUENCE /// ENTRY S43422 #type complete TITLE ribosomal protein L23 [validated] - Halobacterium salinarum ALTERNATE_NAMES ribosomal protein HL31 ORGANISM #formal_name Halobacterium salinarum DATE 23-Oct-1998 #sequence_revision 23-Oct-1998 #text_change 21-Jul-2000 ACCESSIONS S43422; T43818; S08559 REFERENCE S43418 !$#authors Yuki, Y.; Kanechika, R.; Itoh, T. !$#journal Biochim. Biophys. Acta (1993) 1216:335-338 !$#title Nucleotide sequence of the genes encoding the L3, L4 and L23 !1equivalent ribosomal proteins from the archaebacterium !1Halobacterium halobium. !$#cross-references MUID:94060115; PMID:8241282 !$#accession S43422 !'##molecule_type DNA !'##residues 1-84 ##label YUK !'##cross-references EMBL:D14879; NID:g285811; PID:g285815 !'##experimental_source strain S9 !'##note the source is designated as Halobacterium halobium REFERENCE Z22697 !$#authors Itoh, T. !$#submission submitted to the EMBL Data Library, September 1997 !$#accession T43818 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-84 ##label ITO !'##cross-references EMBL:AB006961; PIDN:BAA22272.1 !'##note the source is designated as Halobacterium halobium REFERENCE S07437 !$#authors Matheson, A.T.; Yaguchi, M.; Christensen, P.; Rollin, C.F.; !1Hasnain, S. !$#journal Can. J. Biochem. Cell Biol. (1984) 62:426-433 !$#title Purification, properties, and N-terminal amino acid sequence !1of certain 50S ribosomal subunit proteins from the !1archaebacterium Halobacterium cutirubrum. !$#cross-references MUID:84282108; PMID:6467081 !$#accession S08559 !'##molecule_type protein !'##residues 1-18 ##label MAT !'##note the source is designated as Halobacterium cutirubrum !'##note the protein is designated as ribosomal protein L31 GENETICS !$#note HhaL23 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L23 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 84 #molecular-weight 9380 #checksum 5835 SEQUENCE /// ENTRY H69151 #type complete TITLE ribosomal protein L23 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 23-Oct-1998 #sequence_revision 23-Oct-1998 #text_change 22-Jun-1999 ACCESSIONS H69151 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession H69151 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-100 ##label MTH !'##cross-references GB:AE000795; GB:AE000666; NID:g2621036; !1PIDN:AAB84524.1; PID:g2621051 !'##experimental_source strain Delta H GENETICS !$#gene MTH4 !$#start_codon TTG CLASSIFICATION #superfamily Escherichia coli ribosomal protein L23 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 100 #molecular-weight 11465 #checksum 8333 SEQUENCE /// ENTRY R5MX23 #type complete TITLE ribosomal protein L23 - Methanococcus vannielii ALTERNATE_NAMES ribosomal protein ML7 ORGANISM #formal_name Methanococcus vannielii DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 22-Jun-1999 ACCESSIONS S01780; A37528 REFERENCE S01780 !$#authors Koepke, A.K.E.; Wittmann-Liebold, B. !$#journal FEBS Lett. (1988) 239:313-318 !$#title Sequence of the gene for ribosomal protein L23 from the !1archaebacterium Methanococcus vannielii. !$#cross-references MUID:89031254; PMID:3181433 !$#accession S01780 !'##molecule_type DNA !'##residues 1-86 ##label KOE !'##cross-references EMBL:Y00772; NID:g44744; PIDN:CAA68741.1; !1PID:g44745 !$#accession A37528 !'##molecule_type protein !'##residues 1-12,'XX',15-19 ##label KOE2 !'##note the sequence from Fig. 3 is inconsistent with that from Fig. 2 !1in having 84-Pro CLASSIFICATION #superfamily Escherichia coli ribosomal protein L23 KEYWORDS protein biosynthesis; ribosome FEATURE !$1-86 #product ribosomal protein L23 #status experimental !8#label MAT SUMMARY #length 86 #molecular-weight 9782 #checksum 7053 SEQUENCE /// ENTRY C64322 #type complete TITLE ribosomal protein L23 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 23-Oct-1998 #sequence_revision 23-Oct-1998 #text_change 22-Jun-1999 ACCESSIONS C64322 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession C64322 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-86 ##label BUL !'##cross-references GB:U67474; GB:L77117; NID:g1590921; !1PIDN:AAB98163.1; PID:g1498951; TIGR:MJ0178 GENETICS !$#map_position FOR180264-180524 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L23 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 86 #molecular-weight 9855 #checksum 8949 SEQUENCE /// ENTRY B69490 #type complete TITLE ribosomal protein L23 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 23-Oct-1998 #sequence_revision 23-Oct-1998 #text_change 22-Jun-1999 ACCESSIONS B69490 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession B69490 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-83 ##label KLE !'##cross-references GB:AE000971; GB:AE000782; NID:g2689294; !1PIDN:AAB89333.1; PID:g2648623; TIGR:AF1923 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L23 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 83 #molecular-weight 9579 #checksum 2713 SEQUENCE /// ENTRY S77500 #type complete TITLE ribosomal protein L23 - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein sll1801 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 23-Oct-1998 #sequence_revision 23-Oct-1998 #text_change 16-Jun-2000 ACCESSIONS S77500 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S77500 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-101 ##label KAN !'##cross-references EMBL:D90905; GB:AB001339; NID:g1652360; !1PIDN:BAA17347.1; PID:g1652425 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene rpl23 !$#start_codon GTG CLASSIFICATION #superfamily Escherichia coli ribosomal protein L23 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 101 #molecular-weight 11526 #checksum 86 SEQUENCE /// ENTRY S78274 #type complete TITLE ribosomal protein L23 - Odontella sinensis chloroplast ORGANISM #formal_name chloroplast Odontella sinensis DATE 23-Oct-1998 #sequence_revision 23-Oct-1998 #text_change 23-Oct-1998 ACCESSIONS S78274 REFERENCE S78238 !$#authors Kowallik, K.V.; Stoebe, B.; Schaffran, I.; Kroth-Pancic, P.; !1Freier, U. !$#journal Plant Mol. Biol. Rep. (1995) 13:336-342 !$#title The Chloroplast Genome of a chlorophyll a+c- containing !1Alga, Odontella sinensis. !$#accession S78274 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-102 ##label KOW !'##cross-references EMBL:Z67753 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1995 GENETICS !$#gene rpl23 !$#genome chloroplast !$#start_codon GTG CLASSIFICATION #superfamily Escherichia coli ribosomal protein L23 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 102 #molecular-weight 11846 #checksum 5944 SEQUENCE /// ENTRY S73233 #type complete TITLE ribosomal protein L23 - red alga (Porphyra purpurea) chloroplast ORGANISM #formal_name chloroplast Porphyra purpurea DATE 23-Oct-1998 #sequence_revision 23-Oct-1998 #text_change 22-Jun-1999 ACCESSIONS S73233 REFERENCE S73108 !$#authors Reith, M.; Munholland, J. !$#journal Plant Mol. Biol. Rep. (1995) 13:333-335 !$#title Complete nucleotide sequence of the Porphyra purpurea !1chloroplast genome. !$#accession S73233 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-110 ##label REI !'##cross-references EMBL:U38804; NID:g1276652; PIDN:AAC08198.1; !1PID:g1276778 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1995 GENETICS !$#gene rpl23 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein L23 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 110 #molecular-weight 12782 #checksum 3254 SEQUENCE /// ENTRY R5LV23 #type complete TITLE ribosomal protein L23 - liverwort (Marchantia polymorpha) chloroplast ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 22-Jun-1999 ACCESSIONS A02816; S01554; JS0243 REFERENCE A00150 !$#authors Ohyama, K. !$#submission submitted to the EMBL Data Library, October 1986 !$#accession A02816 !'##molecule_type DNA !'##residues 1-91 ##label OHY REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features REFERENCE S01529 !$#authors Fukuzawa, H.; Kohchi, T.; Sano, T.; Shirai, H.; Umesono, K.; !1Inokuchi, H.; Ozeki, H.; Ohyama, K. !$#journal J. Mol. Biol. (1988) 203:333-351 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. III. Gene organization of the large !1single copy region from rbcL to trnI(CAU). !$#cross-references MUID:89068687; PMID:3199436 !$#accession S01554 !'##molecule_type DNA !'##residues 1-91 ##label FUK1 !'##cross-references GB:X04465; GB:Y00686; NID:g11640; PIDN:CAA28128.1; !1PID:g11717 REFERENCE A90020 !$#authors Fukuzawa, H.; Uchida, Y.; Yamano, Y.; Ohyama, K.; Komano, T. !$#journal Agric. Biol. Chem. (1985) 49:2725-2731 !$#title Molecular cloning of promoters functional in Escherichia !1coli from chloroplast DNA of a liverwort, Marchantia !1polymorpha. !$#accession JS0243 !'##molecule_type DNA !'##residues 1-91 ##label FUK2 GENETICS !$#gene rpl23 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein L23 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 91 #molecular-weight 10769 #checksum 5234 SEQUENCE /// ENTRY S26305 #type complete TITLE ribosomal protein L23 - Arabidopsis thaliana chloroplast ORGANISM #formal_name chloroplast Arabidopsis thaliana #common_name mouse-ear cress DATE 30-Oct-1998 #sequence_revision 30-Oct-1998 #text_change 22-Jun-1999 ACCESSIONS S26305; S24933 REFERENCE S26304 !$#authors Luschnig, C.; Schweizer, D. !$#journal Nucleic Acids Res. (1992) 20:3511 !$#title Nucleotide sequence of trnI(CAU) and rpl23 from Arabidopsis !1thaliana chloroplast genome. !$#cross-references MUID:92335007; PMID:1630923 !$#accession S26305 !'##molecule_type DNA !'##residues 1-93 ##label LUS !'##cross-references EMBL:X66414; NID:g11244; PIDN:CAA47045.1; !1PID:g11245 GENETICS !$#gene rpl23 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein L23 KEYWORDS chloroplast; protein biosynthesis; ribosome FEATURE !$1-93 #product ribosomal protein L23 #status predicted !8#label MAT SUMMARY #length 93 #molecular-weight 10792 #checksum 9740 SEQUENCE /// ENTRY R5NT23 #type complete TITLE ribosomal protein L23 - common tobacco chloroplast ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 17-Feb-1995 ACCESSIONS A02817; A25943; S14810 REFERENCE A00149 !$#authors Sugiura, M. !$#submission submitted to the EMBL Data Library, August 1986 !$#accession A02817 !'##molecule_type DNA !'##residues 1-93 ##label SUG !'##experimental_source cv. Bright Yellow 4 REFERENCE A38013 !$#authors Shinozaki, K.; Ohme, M.; Tanaka, M.; Wakasugi, T.; !1Hayashida, N.; Matsubayashi, T.; Zaita, N.; Chunwongse, J.; !1Obokata, J.; Yamaguchi-Shinozaki, K.; Ohto, C.; Torazawa, !1K.; Meng, B.Y.; Sugita, M.; Deno, H.; Kamogashira, T.; !1Yamada, K.; Kusuda, J.; Takaiwa, F.; Kato, A.; Tohdoh, N.; !1Shimada, H.; Sugiura, M. !$#journal EMBO J. (1986) 5:2043-2049 !$#title The complete nucleotide sequence of the tobacco chloroplast !1genome: its gene organization and expression. !$#contents annotation; gene organization, sites, features REFERENCE A94118 !$#authors Tanaka, M.; Wakasugi, T.; Sugita, M.; Shinozaki, K.; !1Sugiura, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:6030-6034 !$#title Genes for the eight ribosomal proteins are clustered on the !1chloroplast genome of tobacco (Nicotiana tabacum): !1similarity to the S10 and spc operons of Escherichia coli. !$#cross-references MUID:86287388; PMID:3016736 !$#accession A25943 !'##molecule_type DNA !'##residues 1-93 ##label TAN REFERENCE S14810 !$#authors Yokoi, F.; Tanaka, M.; Wakasugi, T.; Sugiura, M. !$#journal FEBS Lett. (1991) 281:64-66 !$#title The chloroplast gene for ribosomal protein CL23 is !1functional in tobacco. !$#cross-references MUID:91200316; PMID:1707833 !$#accession S14810 !'##molecule_type protein !'##residues 1-20 ##label YOK !'##experimental_source cv. Bright Yellow 4 GENETICS !$#gene rpl23 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein L23 KEYWORDS chloroplast; protein biosynthesis; ribosome FEATURE !$1-93 #product ribosomal protein L23 #status experimental !8#label MAT SUMMARY #length 93 #molecular-weight 10763 #checksum 9984 SEQUENCE /// ENTRY R5RZ23 #type complete TITLE ribosomal protein L23 - rice chloroplast ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 24-Sep-1999 ACCESSIONS JQ0271; S05151; JA0092 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0271 !'##molecule_type DNA !'##residues 1-93 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05151 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-14,'A',16-93 ##label HIR !'##experimental_source cv. Nihonbare !'##note this sequence was submitted to EMBL, July 1989 REFERENCE JA0092 !$#authors Moon, E.; Wu, R. !$#journal Gene (1988) 70:1-12 !$#title Organization and nucleotide sequence of genes at both !1junctions between the two inverted repeats and the large !1single-copy region in the rice chloroplast genome. !$#cross-references MUID:89196901; PMID:3240862 !$#accession JA0092 !'##molecule_type DNA !'##residues 1-14,'A',16-45,'X',47-93 ##label MOO !'##cross-references GB:M22826; NID:g710564; PIDN:AAA84593.1; !1PID:g710565 !'##note genes located at the two inverted repeats (IRA and IRB) in the !1rice chloroplast genome are isolated and characterized; a !1ribosomal gene cluster, rpl23-rpl2-rps19, which codes for !1the ribosomal proteins L23 and L2 and S19, lies at the ends !1of the two IRs near the LSCR !'##note the 46th codon is the TAG stop codon in this publication GENETICS !$#gene rpl23 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein L23 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 93 #molecular-weight 10764 #checksum 9150 SEQUENCE /// ENTRY R5ZM23 #type complete TITLE ribosomal protein L23 - maize chloroplast ORGANISM #formal_name chloroplast Zea mays #common_name maize DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jun-2000 ACCESSIONS S01396; S60127; S58596; S58638; S20058 REFERENCE S01396 !$#authors McLaughlin, W.E.; Larrinua, I.M. !$#journal Nucleic Acids Res. (1988) 16:8183 !$#title The sequence of the maize plastid encoded rpl23 locus. !$#cross-references MUID:88335565; PMID:3419911 !$#accession S01396 !'##molecule_type DNA !'##residues 1-93 ##label MCL !'##cross-references EMBL:X07864; NID:g12417; PIDN:CAA30712.1; !1PID:g12418 !'##genetics GEN1 !$#accession S60127 !'##molecule_type DNA !'##residues 1-93 ##label MCW !'##cross-references EMBL:X07864; NID:g12417; PIDN:CAA30712.1; !1PID:g12418 !'##genetics GEN2 REFERENCE S58531 !$#authors Maier, R.M.; Neckermann, K.; Igloi, G.L.; Koessel, H. !$#journal J. Mol. Biol. (1995) 251:614-628 !$#title Complete sequence of the maize chloroplast genome: gene !1content, hotspots of divergence and fine tuning of genetic !1information by transcript editing. !$#cross-references MUID:95395841; PMID:7666415 !$#accession S58596 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-93 ##label MAI !'##cross-references EMBL:X86563; NID:g902200; PIDN:CAA60330.1; !1PID:g902265 !'##genetics GEN2 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1995 !$#accession S58638 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-93 ##label MAW !'##cross-references EMBL:X86563; NID:g902200; PIDN:CAA60330.1; !1PID:g902265 !'##genetics GEN1 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1995 REFERENCE S17874 !$#authors Hoch, B.; Maier, R.M.; Appel, K.; Igloi, G.L.; Koessel, H. !$#journal Nature (1991) 353:178-180 !$#title Editing of a chloroplast mRNA by creation of an initiation !1codon. !$#cross-references MUID:91367263; PMID:1653905 !$#accession S20058 !'##molecule_type mRNA !'##residues 81-93 ##label HOC !'##cross-references EMBL:X62070; NID:g12463; PIDN:CAA43984.1; !1PID:g12465 GENETICS GEN1 !$#gene rpl23 !$#map_position IR(A); IR(II) !$#genome chloroplast GENETICS GEN2 !$#gene rpl23 !$#map_position IR(B); IR(I) !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein L23 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 93 #molecular-weight 10737 #checksum 9465 SEQUENCE /// ENTRY R5WT23 #type complete TITLE ribosomal protein L23 - wheat chloroplast ORGANISM #formal_name chloroplast Triticum aestivum #common_name common wheat DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S06026 REFERENCE S06025 !$#authors Bowman, C.M.; Barker, R.F.; Dyer, T.A. !$#journal Curr. Genet. (1988) 14:127-136 !$#title In wheat ctDNA, segments of ribosomal protein genes are !1dispersed repeats, probably conserved by nonreciprocal !1recombination. !$#cross-references MUID:89028843; PMID:3180271 !$#accession S06026 !'##molecule_type DNA !'##residues 1-93 ##label BOW !'##cross-references EMBL:X12850; NID:g12369; PIDN:CAA31328.1; !1PID:g12370 GENETICS !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein L23 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 93 #molecular-weight 10746 #checksum 9130 SEQUENCE /// ENTRY S00728 #type complete TITLE ribosomal protein L23 - spinach chloroplast ALTERNATE_NAMES ribosomal protein L23 homolog A; ribosomal protein L23 homolog B ORGANISM #formal_name chloroplast Spinacia oleracea #common_name spinach DATE 30-Oct-1998 #sequence_revision 30-Oct-1998 #text_change 22-Jun-1999 ACCESSIONS S00728; S00729 REFERENCE S00728 !$#authors Thomas, F.; Massenet, O.; Dorne, A.M.; Briat, J.F.; Mache, !1R. !$#journal Nucleic Acids Res. (1988) 16:2461-2472 !$#title Expression of the rpl23, rpl2 and rps19 genes in spinach !1chloroplasts. !$#cross-references MUID:88203193; PMID:3362671 !$#accession S00728 !'##molecule_type DNA !'##residues 1-41,'WNSYE' ##label THO1 !'##cross-references EMBL:X07462; NID:g12319; PIDN:CAA30343.1; !1PID:g297557 !$#accession S00729 !'##molecule_type DNA !'##residues 45-88 ##label THO2 !'##cross-references EMBL:X07462; NID:g12319; PIDN:CAA30344.1; !1PID:g297558 !'##note sequence in a different reading frame overlapping the first by !18 nucleotides COMMENT This translation was produced by PIR staff from the !1published nucleotide sequence and the authors' comments. The !1reading frame is shifted as indicated below at a site prior !1to the first termination codon beginning with Gly-42. !1Alignments show that this provides the best match to similar !1sequences. GENETICS !$#gene rpl23A; rpl23B !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein L23 KEYWORDS chloroplast; ribosome; translational frameshift FEATURE !$41-42 #region minus-one translational frameshift SUMMARY #length 88 #molecular-weight 10217 #checksum 7266 SEQUENCE /// ENTRY S26080 #type complete TITLE ribosomal protein L23 - Euglena gracilis chloroplast ORGANISM #formal_name chloroplast Euglena gracilis DATE 23-Oct-1998 #sequence_revision 23-Oct-1998 #text_change 22-Jun-1999 ACCESSIONS S26080; S34887; S34520 REFERENCE S26080 !$#authors Christopher, D.A.; Cushman, J.C.; Price, C.A.; Hallick, R.B. !$#journal Curr. Genet. (1988) 14:275-286 !$#title Organization of ribosomal protein genes rpl23, rpl2, rps19, !1rpl22 and rps3 on the Euglena gracilis chloroplast genome. !$#cross-references MUID:89063445; PMID:3143485 !$#accession S26080 !'##molecule_type DNA !'##residues 1-100 ##label CHR !'##cross-references EMBL:Z11874; NID:g14353; PIDN:CAA77916.1; !1PID:g14366 REFERENCE S34862 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.R.; !1Monfort, A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#journal Nucleic Acids Res. (1993) 21:3537-3544 !$#title Complete sequence of Euglena gracilis chloroplast DNA. !$#cross-references MUID:93347989; PMID:8346031 !$#accession S34887 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-100 ##label HAL2 !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50099.1; !1PID:g415755 !'##experimental_source strain Pringsheim Z !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1993 GENETICS !$#gene rpl23 !$#genome chloroplast !$#introns 16/2; 39/3; 88/3 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L23 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 100 #molecular-weight 12166 #checksum 9029 SEQUENCE /// ENTRY S38604 #type complete TITLE ribosomal protein L23 - euglenid (Astasia longa) plastid ORGANISM #formal_name plastid Astasia longa DATE 23-Oct-1998 #sequence_revision 23-Oct-1998 #text_change 22-Jun-1999 ACCESSIONS S38604 REFERENCE S38590 !$#authors Gockel, G.; Baier, S.; Hachtel, W. !$#submission submitted to the EMBL Data Library, November 1993 !$#accession S38604 !'##molecule_type DNA !'##residues 1-98 ##label GOC !'##cross-references EMBL:X75653; NID:g414863; PIDN:CAA53328.1; !1PID:g414870 !'##experimental_source strain CCAP 1204/17a GENETICS !$#gene rpl23 !$#genome plastid !$#introns 38/3; 87/3 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L23 KEYWORDS chloroplast; plastid; protein biosynthesis; ribosome SUMMARY #length 98 #molecular-weight 11944 #checksum 3185 SEQUENCE /// ENTRY E64684 #type complete TITLE ribosomal protein L23 - Helicobacter pylori ORGANISM #formal_name Helicobacter pylori #variety strains J99, 26695 DATE 23-Oct-1998 #sequence_revision 23-Oct-1998 #text_change 24-Sep-1999 ACCESSIONS E64684; E71835 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession E64684 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-93 ##label TOM !'##cross-references GB:AE000633; GB:AE000511; NID:g2314452; !1PIDN:AAD08356.1; PID:g2314479; TIGR:HP1317 !'##experimental_source strain 26695 REFERENCE A71800 !$#authors Alm, R.A.; Ling, L.S.L.; Moir, D.T.; King, B.L.; Brown, !1E.D.; Doig, P.C.; Smith, D.R.; Noonan, B.; Guild, B.C.; !1deJonge, B.L.; Carmel, G.; Tummino, P.J.; Caruso, A.; !1Uria-Nickelsen, M.; Mills, D.M.; Ives, C.; Gibson, R.; !1Merberg, D.; Mills, S.D.; Jiang, Q.; Taylor, D.E.; Vovis, !1G.F.; Trust, T.J. !$#journal Nature (1999) 397:176-180 !$#title Genomic sequence comparison of two unrelated isolates of the !1human gastric pathogen Helicobacter pylori. !$#cross-references MUID:99120557; PMID:9923682 !$#accession E71835 !'##molecule_type DNA !'##residues 1-93 ##label ARN !'##cross-references GB:AE001547; GB:AE001439; NID:g4155811; !1PIDN:AAD06788.1; PID:g4155814 !'##experimental_source strain J99 GENETICS !$#gene rplW; HP1317 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L23 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 93 #molecular-weight 10454 #checksum 6961 SEQUENCE /// ENTRY S73990 #type complete TITLE ribosomal protein L23 - Mycoplasma pneumoniae (strain ATCC 29342) ALTERNATE_NAMES hypothetical protein VXpSPT7_orf237 ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 10-Dec-1999 ACCESSIONS S73990 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73990 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-237 ##label HIM !'##cross-references EMBL:AE000061; GB:U00089; NID:g1674336; !1PIDN:AAB96312.1; PID:g1674369 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#gene rplW !$#genetic_code SGC3 CLASSIFICATION #superfamily Mycoplasma ribosomal protein homolog KEYWORDS protein biosynthesis; ribosome SUMMARY #length 237 #molecular-weight 25839 #checksum 3937 SEQUENCE /// ENTRY R5EC24 #type complete TITLE ribosomal protein L24 [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 28-Feb-1980 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS H65123; A02818; I41326 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65123 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-104 ##label BLAT !'##cross-references GB:AE000408; GB:U00096; NID:g1789694; !1PIDN:AAC76334.1; PID:g1789705; UWGP:b3309 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A02818 !$#authors Wittmann-Liebold, B. !$#journal FEBS Lett. (1979) 108:75-80 !$#title Primary structure of protein L24 from the Escherichia coli !1ribosome. !$#cross-references MUID:80092112; PMID:391595 !$#accession A02818 !'##molecule_type protein !'##residues 2-104 ##label WIT !'##experimental_source strain K12 REFERENCE I41326 !$#authors Olins, P.O.; Nomura, M. !$#journal Nucleic Acids Res. (1981) 9:1757-1764 !$#title Translational regulation by ribosomal protein S8 in !1Escherichia coli: Structural homology between rRNA binding !1site and feedback target on mRNA. !$#cross-references MUID:81199003; PMID:6262737 !$#accession I41326 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 86-104 ##label OLI !'##cross-references GB:M10195; NID:g146572; PIDN:AAA24050.1; !1PID:g146573 REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note mass spectrographic analysis of post-translational !1modifications; any acid labile modifications may have been !1missed GENETICS !$#gene rplX !$#map_position 73 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX large subunit ribosomal proteins: L1 (PIR:R5EC1), L3 !1(PIR:R5EC3), L2 (PIR:R5EC2), L4 (PIR:R5EC4), L5 (PIR:R5EC5), !1L6 (PIR:R5EC6), L7/L12 (PIR:R5EC7), L9 (PIR:R5EC9), L10 !1(PIR:R5EC10), L11 (PIR:R5EC11), L13 (PIR:R5EC13), L14 !1(PIR:R5EC14), L15 (PIR:R5EC15), L16 (PIR:R5EC16), L17 !1(PIR:R5EC17), L18 (PIR:R5EC18), L19 (PIR:R5EC19) FUNCTION !$#pathway protein biosynthesis !$#note a constituent of the ribonucleoprotein core involved in the !1early assembly of the 50S subunit CLASSIFICATION #superfamily Escherichia coli ribosomal protein L24 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-104 #product ribosomal protein L24 #status experimental !8#label MAT SUMMARY #length 104 #molecular-weight 11316 #checksum 1779 SEQUENCE /// ENTRY G64093 #type complete TITLE ribosomal protein L24 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS G64093 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession G64093 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-103 ##label TIGR !'##cross-references GB:U32762; GB:L42023; NID:g1573797; !1PIDN:AAC22447.1; PID:g1573799; TIGR:HI0789 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L24 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 103 #molecular-weight 11285 #checksum 5397 SEQUENCE /// ENTRY R5BS24 #type complete TITLE ribosomal protein L24 - Bacillus stearothermophilus ORGANISM #formal_name Bacillus stearothermophilus DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 30-Sep-1993 ACCESSIONS A02819 REFERENCE A91149 !$#authors Kimura, M.; Kimura, J.; Ashman, K. !$#journal Eur. J. Biochem. (1985) 150:491-497 !$#title The complete primary structure of ribosomal proteins L1, !1L14, L15, L23, L24, and L29 from Bacillus !1stearothermophilus. !$#cross-references MUID:85257681; PMID:4018095 !$#accession A02819 !'##molecule_type protein !'##residues 1-103 ##label KIM CLASSIFICATION #superfamily Escherichia coli ribosomal protein L24 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 103 #molecular-weight 11218 #checksum 7478 SEQUENCE /// ENTRY R5BS2B #type complete TITLE ribosomal protein L24 - Bacillus subtilis ALTERNATE_NAMES BL23; histone-like protein HPB12 ORGANISM #formal_name Bacillus subtilis DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jun-2000 ACCESSIONS S05993; A44845; B69697 REFERENCE S05989 !$#authors Henkin, T.M.; Moon, S.H.; Mattheakis, L.C.; Nomura, M. !$#journal Nucleic Acids Res. (1989) 17:7469-7486 !$#title Cloning and analysis of the spc ribosomal protein operon of !1Bacillus subtilis: comparison with the spc operon of !1Escherichia coli. !$#cross-references MUID:90016806; PMID:2508062 !$#accession S05993 !'##molecule_type DNA !'##residues 1-103 ##label HEN !'##cross-references EMBL:X15664; NID:g40146; PIDN:CAA33702.1; !1PID:g40151 REFERENCE A44845 !$#authors Sharp, P.M.; Nolan, N.C.; ni Cholmain, N.; Devine, K.M. !$#journal J. Gen. Microbiol. (1992) 138:39-45 !$#title DNA sequence variability at the rplX locus of Bacillus !1subtilis. !$#cross-references MUID:92211327; PMID:1556555 !$#accession A44845 !'##molecule_type DNA !'##residues 1-103 ##label SHA !'##cross-references GB:M81748; NID:g143445; PIDN:AAB59023.1; !1PID:g143446 !'##experimental_source strain JH642 !'##note sequence extracted from NCBI backbone (NCBIN:92212, !1NCBIP:92213) REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69697 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-103 ##label KUN !'##cross-references GB:Z99104; GB:AL009126; NID:g2632267; !1PIDN:CAB11903.1; PID:g2632394 !'##experimental_source strain 168 GENETICS !$#gene rplX CLASSIFICATION #superfamily Escherichia coli ribosomal protein L24 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 103 #molecular-weight 11142 #checksum 89 SEQUENCE /// ENTRY S40199 #type complete TITLE ribosomal protein L24 - Thermotoga maritima (strain MSB8) ORGANISM #formal_name Thermotoga maritima DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S40199; A72249 REFERENCE S37489 !$#authors Sanangelantoni, A.; Tiboni, O. !$#submission submitted to the EMBL Data Library, February 1993 !$#accession S40199 !'##molecule_type DNA !'##residues 1-105 ##label SAN !'##cross-references EMBL:Z21677; NID:g437921; PIDN:CAA79788.1; !1PID:g437934 REFERENCE A72200 !$#authors Nelson, K.E.; Clayton, R.A.; Gill, S.R.; Gwinn, M.L.; !1Dodson, R.J.; Haft, D.H.; Hickey, E.K.; Peterson, J.D.; !1Nelson, W.C.; Ketchum, K.A.; McDonald, L.; Utterback, T.R.; !1Malek, J.A.; Linher, K.D.; Garrett, M.M.; Stewart, A.M.; !1Cotton, M.D.; Pratt, M.S.; Phillips, C.A.; Richardson, D.; !1Heidelberg, J.; Sutton, G.G.; Fleischmann, R.D.; White, O.; !1Salzberg, S.L.; Smith, H.O.; Venter, J.C.; Fraser, C.M. !$#journal Nature (1999) 399:323-329 !$#title Evidence for lateral gene transfer between Archaea and !1Bacteria from genome sequence of Thermotoga maritima. !$#cross-references MUID:99287316; PMID:10360571 !$#accession A72249 !'##molecule_type DNA !'##residues 1-105 ##label ARN !'##cross-references GB:AE001798; GB:AE000512; NID:g4982033; !1PIDN:AAD36555.1; PID:g4982053; TIGR:TM1489 !'##experimental_source strain MSB8 GENETICS !$#gene TM1489 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L24 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 105 #molecular-weight 12023 #checksum 6146 SEQUENCE /// ENTRY H70442 #type complete TITLE ribosomal protein L24 - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS H70442 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession H70442 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-132 ##label AQF !'##cross-references GB:AE000749; NID:g2983975; PIDN:AAC07534.1; !1PID:g2983988; GB:AE000657 !'##experimental_source strain VF5 GENETICS !$#gene rplX CLASSIFICATION #superfamily Escherichia coli ribosomal protein L24 SUMMARY #length 132 #molecular-weight 14942 #checksum 9850 SEQUENCE /// ENTRY S43192 #type complete TITLE ribosomal protein L24 - Thermus aquaticus ORGANISM #formal_name Thermus aquaticus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S43192; S15438 REFERENCE S43192 !$#authors Vysotskaya, V.S.; Garber, M.B. !$#submission submitted to the EMBL Data Library, April 1994 !$#description Nucleotide sequence of the rpl24 gene coding for ribosomal !1protein L24 from Thermus thermophilus. !$#accession S43192 !'##status preliminary !'##molecule_type DNA !'##residues 1-110 ##label VYS !'##cross-references EMBL:Z31726; NID:g469675; PIDN:CAA83517.1; !1PID:g469676 REFERENCE S15436 !$#authors Jahn, O.; Hartmann, R.K.; Erdmann, V.A. !$#journal Eur. J. Biochem. (1991) 197:733-740 !$#title Analysis of the spc ribosomal protein operon of Thermus !1aquaticus. !$#cross-references MUID:91231015; PMID:2029902 !$#accession S15438 !'##molecule_type DNA !'##residues 1,'QA',4,'V',6-28,'A',30-32,'R',34,'M',36-43,'L',45-50,'P', !152-54,'H',56-60,'V',62,'Q',64-91,'D',93,'R',95-97,'A', !199-104,'S',106-107,'V',109-110 ##label JAH !'##cross-references EMBL:X56552; NID:g48102; PIDN:CAA39895.1; !1PID:g48105 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L24 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 110 #molecular-weight 12056 #checksum 5830 SEQUENCE /// ENTRY R5PM24 #type complete TITLE ribosomal protein L24 precursor, chloroplast - garden pea ALTERNATE_NAMES ribosomal protein PsCL12 ORGANISM #formal_name Pisum sativum #common_name garden pea DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S04685 REFERENCE S04684 !$#authors Gantt, J.S. !$#journal Curr. Genet. (1988) 14:519-528 !$#title Nucleotide sequences of cDNAs encoding four complete !1nuclear-encoded plastid ribosomal proteins. !$#cross-references MUID:89136071; PMID:3066512 !$#accession S04685 !'##molecule_type mRNA !'##residues 1-194 ##label GAN !'##cross-references EMBL:X14020; NID:g20872; PIDN:CAA32185.1; !1PID:g20873 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L24 KEYWORDS chloroplast; protein biosynthesis; ribosome FEATURE !$1-39 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$40-194 #product ribosomal protein L24 #status predicted !8#label MAT SUMMARY #length 194 #molecular-weight 21580 #checksum 2694 SEQUENCE /// ENTRY A45113 #type complete TITLE ribosomal protein L24 precursor - common tobacco ORGANISM #formal_name Nicotiana tabacum #common_name common tobacco DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 24-Sep-1999 ACCESSIONS A45113 REFERENCE A45113 !$#authors Elhag, G.A.; Bourque, D.P. !$#journal J. Biol. Chem. (1992) 267:21705-21711 !$#title Nuclear-encoded tobacco chloroplast ribosomal protein L24. !1Protein identification, sequence analysis of cDNAs encoding !1its cytoplasmic precursor, and mRNA and genomic DNA !1analysis. !$#cross-references MUID:93016124; PMID:1400480 !$#accession A45113 !'##status preliminary !'##molecule_type mRNA; protein !'##residues 1-187 ##label ELH !'##cross-references GB:M87838; NID:g170272; PIDN:AAA34086.1; !1PID:g170273 !'##experimental_source leaf !'##note sequence extracted from NCBI backbone (NCBIN:116737, !1NCBIP:116738) CLASSIFICATION #superfamily Escherichia coli ribosomal protein L24 KEYWORDS chloroplast SUMMARY #length 187 #molecular-weight 20702 #checksum 290 SEQUENCE /// ENTRY JH0585 #type complete TITLE ribosomal protein L24 precursor, chloroplast - spinach ORGANISM #formal_name Spinacia oleracea #common_name spinach DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JH0585 REFERENCE JH0585 !$#authors Carol, P.; Li, Y.F.; Mache, R. !$#journal Gene (1991) 103:139-145 !$#title Conservation and evolution of the nucleus-encoded and !1chloroplast-specific ribosomal proteins in pea and spinach. !$#cross-references MUID:91365238; PMID:1889743 !$#accession JH0585 !'##molecule_type mRNA !'##residues 1-191 ##label CAR !'##cross-references GB:M58522; NID:g170136; PIDN:AAA34042.1; !1PID:g170137 !'##experimental_source seedling CLASSIFICATION #superfamily Escherichia coli ribosomal protein L24 KEYWORDS chloroplast; protein biosynthesis FEATURE !$1-45 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$46-191 #product ribosomal protein L24 #status predicted !8#label MAT SUMMARY #length 191 #molecular-weight 21439 #checksum 5693 SEQUENCE /// ENTRY R5YM24 #type complete TITLE ribosomal protein L24 - Mycoplasma capricolum ORGANISM #formal_name Mycoplasma capricolum DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 07-Dec-1999 ACCESSIONS S02842 REFERENCE S02830 !$#authors Ohkubo, S.; Muto, A.; Kawauchi, Y.; Yamao, F.; Osawa, S. !$#journal Mol. Gen. Genet. (1987) 210:314-322 !$#title The ribosomal protein gene cluster of Mycoplasma capricolum. !$#cross-references MUID:88142549; PMID:3481422 !$#accession S02842 !'##molecule_type DNA !'##residues 1-108 ##label OHK !'##cross-references EMBL:X06414; NID:g44207; PIDN:CAA29715.1; !1PID:g44220 GENETICS !$#gene rpl24 !$#genetic_code SGC3 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L24 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 108 #molecular-weight 11777 #checksum 8162 SEQUENCE /// ENTRY R5PM25 #type complete TITLE ribosomal protein PsCL25 precursor, chloroplast - garden pea ORGANISM #formal_name Pisum sativum #common_name garden pea DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 22-Jun-1999 ACCESSIONS S04687 REFERENCE S04684 !$#authors Gantt, J.S. !$#journal Curr. Genet. (1988) 14:519-528 !$#title Nucleotide sequences of cDNAs encoding four complete !1nuclear-encoded plastid ribosomal proteins. !$#cross-references MUID:89136071; PMID:3066512 !$#accession S04687 !'##molecule_type mRNA !'##residues 1-104 ##label GAN !'##cross-references EMBL:X14022; NID:g20876; PIDN:CAA32187.1; !1PID:g20877 CLASSIFICATION #superfamily pea chloroplast ribosomal protein PsCL25 KEYWORDS chloroplast; protein biosynthesis; ribosome FEATURE !$1-30 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$31-104 #product ribosomal protein PsCL25 #status predicted !8#label MAT SUMMARY #length 104 #molecular-weight 11257 #checksum 4172 SEQUENCE /// ENTRY R3RT3A #type complete TITLE ribosomal protein L23a, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 21-Jul-2000 ACCESSIONS A45214; S19257; S19992 REFERENCE A45214 !$#authors Suzuki, K.; Wool, I.G. !$#journal J. Biol. Chem. (1993) 268:2755-2761 !$#title The primary structure of rat ribosomal protein L23a. The !1application of homology search to the identification of !1genes for mammalian and yeast ribosomal proteins and a !1correlation of rat and yeast ribosomal proteins. !$#cross-references MUID:93155091; PMID:8428950 !$#accession A45214 !'##molecule_type mRNA !'##residues 1-156 ##label SUZ !'##cross-references EMBL:X65228; NID:g57689; PIDN:CAA46336.1; !1PID:g57690 !'##note submitted to the EMBL Data Library, March 1992 !'##note sequence extracted from NCBI backbone (NCBIP:124242) !'##note the protein is designated as ribosomal protein L23a according !1to comigration analysis after in vitro translation REFERENCE S19257 !$#authors Suzuki, K.; Wool, I.G. !$#submission submitted to the Protein Sequence Database, March 1992 !$#accession S19257 !'##molecule_type mRNA !'##residues 1-156 ##label GLU !'##note the protein is designated as ribosomal protein L23a CLASSIFICATION #superfamily rat ribosomal protein L23a KEYWORDS protein biosynthesis; ribosome; RNA binding SUMMARY #length 156 #molecular-weight 17695 #checksum 367 SEQUENCE /// ENTRY R5BY25 #type complete TITLE ribosomal protein L23a.e, cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein AOX142i; protein O0534; protein YOL127w; ribosomal protein rp61L; ribosomal protein YL25 ORGANISM #formal_name Saccharomyces cerevisiae DATE 17-Mar-1987 #sequence_revision 19-Jul-1996 #text_change 16-Jun-2000 ACCESSIONS S63443; A02820; S45520; S66824; S71981 REFERENCE S63440 !$#authors Casamayor, A.; Khalid, H.; Balcells, L.; Aldea, M.; Casas, !1C.; Herrero, E.; Arino, J. !$#submission submitted to the EMBL Data Library, November 1995 !$#description Sequencing of a 13.4 kbp fragment of the left arm of !1chromosome XV reveals a putative ser/thr protein kinase !1gene, the malate dehydrogenase MDH2 gene, a ribosomal L25 !1gene. !$#accession S63443 !'##molecule_type DNA !'##residues 1-142 ##label CAS !'##cross-references EMBL:U41293; NID:g1209710; PIDN:AAC49465.1; !1PID:g1209714 !'##experimental_source strain FY1679 REFERENCE A93532 !$#authors Leer, R.J.; van Raamsdonk-Duin, M.M.C.; Hagendoorn, M.J.M.; !1Mager, W.H.; Planta, R.J. !$#journal Nucleic Acids Res. (1984) 12:6685-6700 !$#title Structural comparison of yeast ribosomal protein genes. !$#cross-references MUID:85014125; PMID:6091033 !$#accession A02820 !'##molecule_type DNA !'##residues 1-105,'NI',113-142 ##label LEE !'##cross-references EMBL:X01014; NID:g4325; PIDN:CAA25506.1; PID:g4326 REFERENCE S45500 !$#authors Takahura, H.; Tsunasawa, S.; Miyagi, M.; Warner, J.R. !$#journal J. Biol. Chem. (1992) 267:5442-5445 !$#title NH2-terminal acetylation of ribosomal proteins of !1Saccharomyces cerevisiae. !$#cross-references MUID:92184799; PMID:1544921 !$#accession S45520 !'##molecule_type protein !'##residues 2-21 ##label TAK REFERENCE S66814 !$#authors Arino, J.; Casamayor, A.; Gamo, F.J.; Gancedo, C.; Lafuente, !1M.J.; Aldea, M.; Casas, C.; Herrero, E. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S66824 !'##molecule_type DNA !'##residues 1-142 ##label ARI !'##cross-references EMBL:Z74869; GSPDB:GN00015; MIPS:YOL127w; !1NID:g1420010; PIDN:CAA99146.1; PID:g1420011 !'##experimental_source strain S288C REFERENCE S71978 !$#authors Casamayor, A.; Khalid, H.; Balcells, L.; Aldea, M.; Casas, !1C.; Herrero, E.; Arino, J. !$#journal Yeast (1996) 12:1013-1020 !$#title Sequence analysis of a 13.4 kbp fragment from the left arm !1of chromosome XV reveals a malate dehydrogenase gene, a !1putative Ser/Thr protein kinase, the ribosomal L25 gene and !1four new open reading frames. !$#cross-references MUID:97051588; PMID:8896265 !$#accession S71981 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-142 ##label CAW !'##cross-references EMBL:U41293; NID:g1209710; PIDN:AAC49465.1; !1PID:g1209714 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1995 GENETICS !$#gene SGD:RPL25; YL25; MIPS:YOL127w !'##cross-references SGD:S0005487; MIPS:YOL127w !$#map_position 15L !$#introns 5/1 CLASSIFICATION #superfamily rat ribosomal protein L23a KEYWORDS protein biosynthesis; ribosome; RNA binding FEATURE !$2-142 #product ribosomal protein L23a.e #status !8experimental #label MAT SUMMARY #length 142 #molecular-weight 15757 #checksum 6173 SEQUENCE /// ENTRY R5HQ25 #type complete TITLE ribosomal protein L23a.e - yeast (Pichia jadinii) ALTERNATE_NAMES ribosomal protein HL25 ORGANISM #formal_name Pichia jadinii, Candida utilis DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 22-Jun-1999 ACCESSIONS S06373 REFERENCE S06373 !$#authors Woudt, L.P.; Mager, W.H.; Beek, J.G.; Wassenaar, G.M.; !1Planta, R.J. !$#journal Curr. Genet. (1987) 12:193-198 !$#title Structural and putative regulatory sequences of the gene !1encoding ribosomal protein L25 in Candida utilis. !$#cross-references MUID:88210534; PMID:3449224 !$#accession S06373 !'##molecule_type DNA !'##residues 1-142 ##label WOU !'##cross-references EMBL:X05919; NID:g2679; PIDN:CAA29354.1; PID:g2680 !'##note the authors' translation is inconsistent with the nucleotide !1sequence in having an additional Asn after 117-Asn and in !1lacking 142-Ile COMMENT This protein binds to 26S rRNA. GENETICS !$#introns 5/1 CLASSIFICATION #superfamily rat ribosomal protein L23a KEYWORDS protein biosynthesis; ribosome; RNA binding SUMMARY #length 142 #molecular-weight 15632 #checksum 5239 SEQUENCE /// ENTRY R5EC25 #type complete TITLE ribosomal protein L25 [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 12-Aug-1981 #sequence_revision 12-Aug-1981 #text_change 01-Mar-2002 ACCESSIONS S16002; A02821; A30428; A30429; H64987 REFERENCE S16002 !$#authors Uemura, Y.; Isono, S.; Isono, K. !$#journal Mol. Gen. Genet. (1991) 226:341-344 !$#title Cloning, characterization, and physical location of the rplY !1gene which encodes ribosomal protein L25 in Escherichia coli !1K12. !$#cross-references MUID:91238717; PMID:2034228 !$#accession S16002 !'##molecule_type DNA !'##residues 1-94 ##label MOL !'##cross-references EMBL:D13326; NID:g216639; PIDN:BAA02585.1; !1PID:g216640 !'##experimental_source strain K12 REFERENCE A02821 !$#authors Dovgas, N.V.; Markova, L.F.; Mednikova, T.A.; Vinokurov, !1L.M.; Alakhov, Y.B.; Ovchinnikov, Y.A. !$#journal FEBS Lett. (1975) 53:351-354 !$#title The primary structure of the 5 S RNA binding protein L25 !1from Escherichia coli ribosomes. !$#cross-references MUID:75168192; PMID:1093874 !$#accession A02821 !'##molecule_type protein !'##residues 1-94 ##label DOV1 !'##experimental_source strain MRE-600 REFERENCE A30427 !$#authors Dovgas, N.V.; Markova, L.F.; Mednikova, T.A.; Vinokurov, !1L.M.; Alakhov, Y.B.; Ovchinnikov, Y.A. !$#journal FEBS Lett. (1975) 57:305 !$#contents annotation; revision REFERENCE A30428 !$#authors Alakhov, Y.B.; Vinokurov, L.M.; Dovgas, N.V.; Markova, L.F.; !1Mednikova, T.A.; Motuz, L.P.; Kashparov, I.A.; Ovchinnikov, !1Y.A. !$#journal Bioorg. Khim. (1976) 2:5-18 !$#accession A30428 !'##molecule_type protein !'##residues 1-94 ##label ALA !'##experimental_source strain MRE-600 REFERENCE A30429 !$#authors Bitar, K.G.; Wittmann-Liebold, B. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1975) 356:1343-1352 !$#title The primary structure of the 5S rRNA binding protein L25 of !1Escherichia coli ribosomes. !$#cross-references MUID:76023782; PMID:1100506 !$#accession A30429 !'##molecule_type protein !'##residues 1-94 ##label BIT !'##experimental_source K12 strain A19 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64987 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-94 ##label BLAT !'##cross-references GB:AE000308; GB:U00096; NID:g1788508; !1PIDN:AAC75246.1; PID:g1788512; UWGP:b2185 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note no post-translational modifications were observed in mass !1spectrographic analysis; any acid labile modifications may !1have been missed GENETICS !$#gene rplY !$#map_position 48 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX large subunit ribosomal proteins: L1 (PIR:R5EC1), L3 !1(PIR:R5EC3), L2 (PIR:R5EC2), L4 (PIR:R5EC4), L5 (PIR:R5EC5), !1L6 (PIR:R5EC6), L7/L12 (PIR:R5EC7), L9 (PIR:R5EC9), L10 !1(PIR:R5EC10), L11 (PIR:R5EC11), L13 (PIR:R5EC13), L14 !1(PIR:R5EC14), L15 (PIR:R5EC15), L16 (PIR:R5EC16), L17 !1(PIR:R5EC17), L18 (PIR:R5EC18), L19 (PIR:R5EC19) FUNCTION !$#pathway protein biosynthesis CLASSIFICATION #superfamily Escherichia coli ribosomal protein L25 KEYWORDS protein biosynthesis; ribosome FEATURE !$1-94 #product ribosomal protein L25 #status experimental !8#label MAT SUMMARY #length 94 #molecular-weight 10693 #checksum 5953 SEQUENCE /// ENTRY R5RT26 #type complete TITLE ribosomal protein L26, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 21-Jul-2000 ACCESSIONS S05024; S20563 REFERENCE S05024 !$#authors Paz, V.; Olvera, J.; Chan, Y.L.; Wool, I.G. !$#journal FEBS Lett. (1989) 251:89-93 !$#title The primary structure of rat ribosomal protein L26. !$#cross-references MUID:89325695; PMID:2546830 !$#accession S05024 !'##molecule_type mRNA !'##residues 1-145 ##label PAZ !'##cross-references EMBL:X14671; NID:g57691; PIDN:CAA32801.1; !1PID:g57692 !$#accession S20563 !'##molecule_type protein !'##residues 1-13 ##label PAZ2 !'##note the protein is designated as ribosomal protein L26 CLASSIFICATION #superfamily rat ribosomal protein L26 KEYWORDS protein biosynthesis; ribosome FEATURE !$1-145 #product ribosomal protein L26 #status experimental !8#label MAT SUMMARY #length 145 #molecular-weight 17277 #checksum 5501 SEQUENCE /// ENTRY R5MX24 #type complete TITLE ribosomal protein L24 - Methanococcus vannielii ORGANISM #formal_name Methanococcus vannielii DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 22-Jun-1999 ACCESSIONS S05615 REFERENCE S05611 !$#authors Auer, J.; Spicker, G.; Boeck, A. !$#journal J. Mol. Biol. (1989) 209:21-36 !$#title Organization and structure of the Methanococcus !1transcriptional unit homologous to the Escherichia coli !1"spectinomycin operon". Implications for the evolutionary !1relationship of 70 S and 80 S ribosomes. !$#cross-references MUID:90040717; PMID:2530355 !$#accession S05615 !'##molecule_type DNA !'##residues 1-119 ##label AUE !'##cross-references EMBL:X16720; NID:g44754; PIDN:CAA34691.1; !1PID:g44759 CLASSIFICATION #superfamily rat ribosomal protein L26 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 119 #molecular-weight 13397 #checksum 5400 SEQUENCE /// ENTRY R5HS24 #type complete TITLE ribosomal protein L24 [validated] - Haloarcula marismortui ALTERNATE_NAMES ribosomal protein HL15; ribosomal protein HL16; ribosomal protein HmaL24 ORGANISM #formal_name Haloarcula marismortui DATE 31-Mar-1991 #sequence_revision 30-Jun-1991 #text_change 31-Mar-2000 ACCESSIONS S10735; S02394; A28926; T46798 REFERENCE S10731 !$#authors Arndt, E. !$#journal FEBS Lett. (1990) 267:193-198 !$#title Nucleotide sequence of four genes encoding ribosomal !1proteins from the 'S10 and spectinomycin' operon equivalent !1region in the archaebacterium Halobacterium marismortui. !$#cross-references MUID:90336772; PMID:2143141 !$#accession S10735 !'##molecule_type DNA !'##residues 1-120 ##label ARN !'##cross-references EMBL:X55311; NID:g43610; PIDN:CAA39019.1; !1PID:g43615 !'##note the source is designated as Halobacterium marismortui REFERENCE S02394 !$#authors Hatakeyama, T.; Hatakeyama, T.; Kimura, M. !$#journal FEBS Lett. (1988) 240:21-28 !$#title The primary structures of ribosomal proteins L16, L23 and !1L33 from the archaebacterium Halobacterium marismortui. !$#cross-references MUID:89052888; PMID:3191994 !$#accession S02394 !'##molecule_type protein !'##residues 2-20,'R',22-120 ##label HAT !'##note the source is designated as Halobacterium marismortui !'##note the protein is designated as ribosomal protein L16 REFERENCE A28926 !$#authors Walsh, M.J.; McDougall, J.; Wittmann-Liebold, B. !$#journal Biochemistry (1988) 27:6867-6876 !$#title Extended N-terminal sequencing of proteins of !1archaebacterial ribosomes blotted from two-dimensional gels !1onto glass fiber and poly(vinylidene difluoride) membrane. !$#cross-references MUID:89062418; PMID:3196689 !$#accession A28926 !'##molecule_type protein !'##residues 2-18 ##label WAL !'##note the protein is designated as ribosomal protein L15 CLASSIFICATION #superfamily rat ribosomal protein L26 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-120 #product ribosomal protein L24 #status experimental !8#label MAT SUMMARY #length 120 #molecular-weight 13648 #checksum 2389 SEQUENCE /// ENTRY R5RT27 #type complete TITLE ribosomal protein L27, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 21-Jul-2000 ACCESSIONS S00401; S11419 REFERENCE S00401 !$#authors Tanaka, T.; Kuwano, Y.; Ishikawa, K.; Ogata, K. !$#journal Eur. J. Biochem. (1988) 173:53-56 !$#title Nucleotide sequence of cloned cDNA specific for rat !1ribosomal protein L27. !$#cross-references MUID:88185328; PMID:2833393 !$#accession S00401 !'##molecule_type mRNA !'##residues 1-136 ##label TAN !'##cross-references EMBL:X07424; NID:g57693; PIDN:CAA30313.1; !1PID:g57694 REFERENCE S11413 !$#authors Wittmann-Liebold, B.; Geissler, A.W.; Lin, A.; Wool, I.G. !$#journal J. Supramol. Struct. (1979) 12:425-433 !$#title Sequence of the amino-terminal region of rat liver ribosomal !1proteins S4, S6, S8, L6, L7a, L18, L27, L30, L37, L37a, and !1L39. !$#cross-references MUID:80252792; PMID:398910 !$#accession S11419 !'##molecule_type protein !'##residues 2-6,'L',8-14,'K',16,'X',18,'X',20,'X',22-28 ##label WIT !'##note the protein is designated as ribosomal protein L27 CLASSIFICATION #superfamily rat ribosomal protein L27 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-136 #product ribosomal protein L27, cytosolic #status !8experimental #label MAT SUMMARY #length 136 #molecular-weight 15798 #checksum 3032 SEQUENCE /// ENTRY R5EC27 #type complete TITLE ribosomal protein L27 [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 24-Apr-1984 #sequence_revision 31-Mar-1993 #text_change 01-Mar-2002 ACCESSIONS JS0767; A02822; S59063; C65109 REFERENCE JS0766 !$#authors Kitakawa, M.; Jeong, J.; Isono, S.; Isono, K. !$#submission submitted to JIPID, September 1992 !$#accession JS0767 !'##molecule_type DNA !'##residues 1-85 ##label KIT !'##cross-references DDBJ:D13267; NID:g216635; PIDN:BAA02526.1; !1PID:g216637 !'##experimental_source strain K12 REFERENCE A02822 !$#authors Chen, R.; Mende, L.; Arfsten, U. !$#journal FEBS Lett. (1975) 59:96-99 !$#title The primary structure of protein L27 from the peptidyl-tRNA !1binding site of Escherichia coli ribosomes. !$#cross-references MUID:76188014; PMID:1225626 !$#accession A02822 !'##molecule_type protein !'##residues 2-85 ##label CHE REFERENCE S59051 !$#authors Urlaub, H.; Kruft, V.; Bischof, O.; Mueller, E.C.; !1Wittmann-Liebold, B. !$#journal EMBO J. (1995) 14:4578-4588 !$#title Protein-rRNA binding features and their structural and !1functional implications in ribosomes as determined by !1cross-linking studies. !$#cross-references MUID:96003638; PMID:7556101 !$#accession S59063 !'##molecule_type protein !'##residues 67-78 ##label URL REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65109 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-85 ##label BLAT !'##cross-references GB:AE000399; GB:U00096; NID:g2367201; !1PIDN:AAC76217.1; PID:g1789576; UWGP:b3185 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note mass spectrographic analysis of post-translational !1modifications; any acid labile modifications may have been !1missed GENETICS !$#gene rpmA !$#map_position 69 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX large subunit ribosomal proteins: L1 (PIR:R5EC1), L3 !1(PIR:R5EC3), L2 (PIR:R5EC2), L4 (PIR:R5EC4), L5 (PIR:R5EC5), !1L6 (PIR:R5EC6), L7/L12 (PIR:R5EC7), L9 (PIR:R5EC9), L10 !1(PIR:R5EC10), L11 (PIR:R5EC11), L13 (PIR:R5EC13), L14 !1(PIR:R5EC14), L15 (PIR:R5EC15), L16 (PIR:R5EC16), L17 !1(PIR:R5EC17), L18 (PIR:R5EC18), L19 (PIR:R5EC19) FUNCTION !$#pathway protein biosynthesis CLASSIFICATION #superfamily Escherichia coli ribosomal protein L27; !1eubacterial ribosomal protein L27 homology KEYWORDS protein biosynthesis; ribosome FEATURE !$2-85 #product ribosomal protein L27 #status experimental !8#label MAT\ !$2-85 #domain eubacterial ribosomal protein L27 homology !8#label L27 SUMMARY #length 85 #molecular-weight 9124 #checksum 3756 SEQUENCE /// ENTRY F64099 #type complete TITLE ribosomal protein L27 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS F64099 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession F64099 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-85 ##label TIGR !'##cross-references GB:U32769; GB:L42023; NID:g1573888; !1PIDN:AAC22535.1; PID:g1573896; TIGR:HI0879 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L27; !1eubacterial ribosomal protein L27 homology KEYWORDS protein biosynthesis; ribosome FEATURE !$2-85 #domain eubacterial ribosomal protein L27 homology !8#label L27 SUMMARY #length 85 #molecular-weight 9151 #checksum 6656 SEQUENCE /// ENTRY R5BS27 #type complete TITLE ribosomal protein L27 - Bacillus stearothermophilus ALTERNATE_NAMES ribosomal protein BL30 ORGANISM #formal_name Bacillus stearothermophilus DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 27-Jan-1995 ACCESSIONS S08563 REFERENCE S07223 !$#authors Kimura, M.; Chow, C.K. !$#journal Eur. J. Biochem. (1984) 139:225-234 !$#title The complete amino acid sequences of ribosomal proteins L17, !1L27, and S9 from Bacillus stearothermophilus. !$#cross-references MUID:84132037; PMID:6365549 !$#accession S08563 !'##molecule_type protein !'##residues 1-87 ##label KIM !'##note the sequence from Fig. 5 is inconsistent with that from Fig. 2 !1in having 54-Arg CLASSIFICATION #superfamily Escherichia coli ribosomal protein L27; !1eubacterial ribosomal protein L27 homology KEYWORDS protein biosynthesis; ribosome FEATURE !$1-83 #domain eubacterial ribosomal protein L27 homology !8#label L27 SUMMARY #length 87 #molecular-weight 9403 #checksum 2574 SEQUENCE /// ENTRY C21895 #type complete TITLE ribosomal protein L27 - Bacillus subtilis ALTERNATE_NAMES ribosomal protein BL24 (rpmA) ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS C21895; S18441; C69697 REFERENCE A94670 !$#authors Ferrari, F.A.; Trach, K.; Hoch, J.A. !$#journal J. Bacteriol. (1985) 161:556-562 !$#title Sequence analysis of the spo0B locus reveals a polycistronic !1transcription unit. !$#cross-references MUID:85104776; PMID:3918016 !$#accession C21895 !'##molecule_type DNA !'##residues 1-94 ##label FER !'##cross-references GB:X02656; GB:K02665; NID:g40184; PIDN:CAA26492.1; !1PID:g40186 REFERENCE S18437 !$#authors Cutting, S.; Roels, S.; Losick, R. !$#journal J. Mol. Biol. (1991) 221:1237-1256 !$#title Sporulation operon spoIVF and the characterization of !1mutations that uncouple mother-cell from forespore gene !1expression in Bacillus subtilis. !$#cross-references MUID:92046062; PMID:1942049 !$#accession S18441 !'##molecule_type DNA !'##residues 1-26 ##label CUT !'##cross-references EMBL:X59528; NID:g40170; PIDN:CAA42110.1; !1PID:g40175 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69697 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-94 ##label KUN !'##cross-references GB:Z99118; GB:AL009126; NID:g2635200; !1PIDN:CAB14754.1; PID:g2635259 !'##experimental_source strain 168 GENETICS !$#gene rpmA CLASSIFICATION #superfamily Escherichia coli ribosomal protein L27; !1eubacterial ribosomal protein L27 homology KEYWORDS protein biosynthesis; ribosome FEATURE !$10-92 #domain eubacterial ribosomal protein L27 homology !8#label L27 SUMMARY #length 94 #molecular-weight 10372 #checksum 718 SEQUENCE /// ENTRY A42840 #type complete TITLE ribosomal protein L27 precursor, chloroplast [similarity] - common tobacco ORGANISM #formal_name Nicotiana tabacum #common_name common tobacco DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 18-Nov-2002 ACCESSIONS A42840 REFERENCE A42840 !$#authors Elhag, G.A.; Bourque, D.P. !$#journal Biochemistry (1992) 31:6856-6864 !$#title Nuclear-encoded chloroplast ribosomal protein L27 of !1Nicotiana tabacum: cDNA sequence and analysis of mRNA and !1genes. !$#cross-references MUID:92345244; PMID:1339289 !$#accession A42840 !'##molecule_type mRNA !'##residues 1-179 ##label ELH !'##cross-references GB:M98473; NID:g170305; PIDN:AAA34104.1; !1PID:g170306 !'##experimental_source cv. Petite Havana !'##note sequence extracted from NCBI backbone (NCBIP:109648) GENETICS !$#genome nuclear CLASSIFICATION #superfamily Escherichia coli ribosomal protein L27; !1eubacterial ribosomal protein L27 homology KEYWORDS chloroplast; protein biosynthesis; ribosome FEATURE !$52-134 #domain eubacterial ribosomal protein L27 homology !8#label L27 SUMMARY #length 179 #molecular-weight 19664 #checksum 808 SEQUENCE /// ENTRY R5RT28 #type complete TITLE ribosomal protein L28, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 21-Jul-2000 ACCESSIONS S13072; A30448 REFERENCE S13071 !$#authors Wool, I.G.; Chan, Y.L.; Paz, V.; Olvera, J. !$#journal Biochim. Biophys. Acta (1990) 1050:69-73 !$#title The primary structure of rat ribosomal proteins: the amino !1acid sequences of L27a and L28 and corrections in the !1sequences of S4 and S12. !$#cross-references MUID:91002678; PMID:2207170 !$#accession S13072 !'##molecule_type mRNA !'##residues 1-137 ##label WOO !'##cross-references EMBL:X52619; NID:g57112; PIDN:CAA36846.1; !1PID:g57113 !$#accession A30448 !'##molecule_type protein !'##residues 2-13,65-94,109-137 ##label WO2 !'##note the protein is designated as ribosomal protein L28 CLASSIFICATION #superfamily rat ribosomal protein L28 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-137 #product ribosomal protein L28 #status experimental !8#label MAT SUMMARY #length 137 #molecular-weight 15848 #checksum 7501 SEQUENCE /// ENTRY R5EC28 #type complete TITLE ribosomal protein L28 [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-May-1979 #sequence_revision 03-Nov-1995 #text_change 01-Mar-2002 ACCESSIONS S42443; A02823; S59064; G65164 REFERENCE S42443 !$#authors Lee, J.S.; An, G.; Friesen, J.D.; Isono, K. !$#journal Mol. Gen. Genet. (1981) 184:218-223 !$#title Cloning and the nucleotide sequence of the genes for !1Escherichia coli ribosomal proteins L28 (rpmB) and L33 !1(rpmG). !$#cross-references MUID:82124622; PMID:7035835 !$#accession S42443 !'##molecule_type DNA !'##residues 1-78 ##label LEE !'##cross-references EMBL:J01677; NID:g147707; PIDN:AAA74099.1; !1PID:g147708 !'##note translation of initiator Met is not shown REFERENCE A02823 !$#authors Wittmann-Liebold, B.; Marzinzig, E. !$#journal FEBS Lett. (1977) 81:214-217 !$#title Primary structure of protein L28 from the large subunit of !1Escherichia coli ribosomes. !$#cross-references MUID:78003727; PMID:332524 !$#accession A02823 !'##molecule_type protein !'##residues 2-78 ##label WIT REFERENCE S59051 !$#authors Urlaub, H.; Kruft, V.; Bischof, O.; Mueller, E.C.; !1Wittmann-Liebold, B. !$#journal EMBO J. (1995) 14:4578-4588 !$#title Protein-rRNA binding features and their structural and !1functional implications in ribosomes as determined by !1cross-linking studies. !$#cross-references MUID:96003638; PMID:7556101 !$#accession S59064 !'##molecule_type protein !'##residues 55-66 ##label URL REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65164 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-78 ##label BLAT !'##cross-references GB:AE000441; GB:U00096; NID:g1790063; !1PIDN:AAC76661.1; PID:g1790068; UWGP:b3637 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note mass spectrographic analysis of post-translational !1modifications; any acid labile modifications may have been !1missed GENETICS !$#gene rpmB !$#map_position 82 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX large subunit ribosomal proteins: L1 (PIR:R5EC1), L3 !1(PIR:R5EC3), L2 (PIR:R5EC2), L4 (PIR:R5EC4), L5 (PIR:R5EC5), !1L6 (PIR:R5EC6), L7/L12 (PIR:R5EC7), L9 (PIR:R5EC9), L10 !1(PIR:R5EC10), L11 (PIR:R5EC11), L13 (PIR:R5EC13), L14 !1(PIR:R5EC14), L15 (PIR:R5EC15), L16 (PIR:R5EC16), L17 !1(PIR:R5EC17), L18 (PIR:R5EC18), L19 (PIR:R5EC19) FUNCTION !$#pathway protein biosynthesis CLASSIFICATION #superfamily Escherichia coli ribosomal protein L28 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-78 #product ribosomal protein L28 #status experimental !8#label MAT SUMMARY #length 78 #molecular-weight 9006 #checksum 5707 SEQUENCE /// ENTRY R5NT28 #type complete TITLE ribosomal protein L28 precursor, chloroplast - tobacco ORGANISM #formal_name Nicotiana sp. #common_name tobacco DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 04-Dec-1994 ACCESSIONS S24123; S26701 REFERENCE S24123 !$#authors Yokoi, F.; Sugiura, M. !$#journal FEBS Lett. (1992) 308:258-260 !$#title Tobacco chloroplast ribosomes contain a homologue of E. coli !1ribosomal protein L28. !$#cross-references MUID:92371638; PMID:1505663 !$#accession S24123 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-151 ##label YOK1 !$#accession S26701 !'##molecule_type protein !'##residues 'X',76-77,'X',79-95 ##label YOK2 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L28 KEYWORDS chloroplast; protein biosynthesis; ribosome FEATURE !$1-74 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$75-151 #product ribosomal protein L28 #status experimental !8#label MAT SUMMARY #length 151 #molecular-weight 16697 #checksum 824 SEQUENCE /// ENTRY R5EC29 #type complete TITLE ribosomal protein L29 [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 24-Apr-1984 #sequence_revision 30-Jun-1991 #text_change 01-Mar-2002 ACCESSIONS B37519; A02824; C65124; A30418; J23129 REFERENCE A23129 !$#authors Zurawski, G.; Zurawski, S.M. !$#journal Nucleic Acids Res. (1985) 13:4521-4526 !$#title Structure of the Escherichia coli S10 ribosomal protein !1operon. !$#cross-references MUID:85242118; PMID:3892488 !$#accession B37519 !'##molecule_type DNA !'##residues 1-63 ##label ZUR !'##cross-references GB:X02613; NID:g42825; PIDN:CAA26468.1; PID:g42834 REFERENCE A02824 !$#authors Bitar, K.G. !$#journal Biochim. Biophys. Acta (1975) 386:99-106 !$#title The primary structure of the ribosomal protein L29 from !1Escherichia coli. !$#cross-references MUID:75146787; PMID:1092361 !$#accession A02824 !'##molecule_type protein !'##residues 1-43,'KLQLNT',44-53,60-63 ##label BIT !'##experimental_source strain K REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65124 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-63 ##label BLAT !'##cross-references GB:AE000408; GB:U00096; NID:g1789694; !1PIDN:AAC76337.1; PID:g1789708; UWGP:b3312 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note no post-translational modifications were observed in mass !1spectrographic analysis; any acid labile modifications may !1have been missed GENETICS !$#gene rpmC !$#map_position 73 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX large subunit ribosomal proteins: L1 (PIR:R5EC1), L3 !1(PIR:R5EC3), L2 (PIR:R5EC2), L4 (PIR:R5EC4), L5 (PIR:R5EC5), !1L6 (PIR:R5EC6), L7/L12 (PIR:R5EC7), L9 (PIR:R5EC9), L10 !1(PIR:R5EC10), L11 (PIR:R5EC11), L13 (PIR:R5EC13), L14 !1(PIR:R5EC14), L15 (PIR:R5EC15), L16 (PIR:R5EC16), L17 !1(PIR:R5EC17), L18 (PIR:R5EC18), L19 (PIR:R5EC19) FUNCTION !$#pathway protein biosynthesis CLASSIFICATION #superfamily Escherichia coli ribosomal protein L29 KEYWORDS protein biosynthesis; ribosome FEATURE !$1-63 #product ribosomal protein L29 #status experimental !8#label MAT SUMMARY #length 63 #molecular-weight 7273 #checksum 9429 SEQUENCE /// ENTRY D64093 #type complete TITLE ribosomal protein L29 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS D64093 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession D64093 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-63 ##label TIGR !'##cross-references GB:U32761; GB:L42023; NID:g1573780; !1PIDN:AAC22444.1; PID:g1573795; TIGR:HI0785 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L29 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 63 #molecular-weight 7178 #checksum 9479 SEQUENCE /// ENTRY R5BS29 #type complete TITLE ribosomal protein L29 - Bacillus stearothermophilus ORGANISM #formal_name Bacillus stearothermophilus DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 07-May-1999 ACCESSIONS A02825; S59065 REFERENCE A91149 !$#authors Kimura, M.; Kimura, J.; Ashman, K. !$#journal Eur. J. Biochem. (1985) 150:491-497 !$#title The complete primary structure of ribosomal proteins L1, !1L14, L15, L23, L24, and L29 from Bacillus !1stearothermophilus. !$#cross-references MUID:85257681; PMID:4018095 !$#accession A02825 !'##molecule_type protein !'##residues 1-66 ##label KIM REFERENCE S59051 !$#authors Urlaub, H.; Kruft, V.; Bischof, O.; Mueller, E.C.; !1Wittmann-Liebold, B. !$#journal EMBO J. (1995) 14:4578-4588 !$#title Protein-rRNA binding features and their structural and !1functional implications in ribosomes as determined by !1cross-linking studies. !$#cross-references MUID:96003638; PMID:7556101 !$#accession S59065 !'##molecule_type protein !'##residues 3-17;55-66 ##label URL CLASSIFICATION #superfamily Escherichia coli ribosomal protein L29 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 66 #molecular-weight 7796 #checksum 8263 SEQUENCE /// ENTRY S40196 #type complete TITLE ribosomal protein L29 - Thermotoga maritima (strain MSB8) ORGANISM #formal_name Thermotoga maritima DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S40196; D72249 REFERENCE S37489 !$#authors Sanangelantoni, A.; Tiboni, O. !$#submission submitted to the EMBL Data Library, February 1993 !$#accession S40196 !'##molecule_type DNA !'##residues 1-66 ##label SAN !'##cross-references EMBL:Z21677; NID:g437921; PIDN:CAA79785.1; !1PID:g437931 REFERENCE A72200 !$#authors Nelson, K.E.; Clayton, R.A.; Gill, S.R.; Gwinn, M.L.; !1Dodson, R.J.; Haft, D.H.; Hickey, E.K.; Peterson, J.D.; !1Nelson, W.C.; Ketchum, K.A.; McDonald, L.; Utterback, T.R.; !1Malek, J.A.; Linher, K.D.; Garrett, M.M.; Stewart, A.M.; !1Cotton, M.D.; Pratt, M.S.; Phillips, C.A.; Richardson, D.; !1Heidelberg, J.; Sutton, G.G.; Fleischmann, R.D.; White, O.; !1Salzberg, S.L.; Smith, H.O.; Venter, J.C.; Fraser, C.M. !$#journal Nature (1999) 399:323-329 !$#title Evidence for lateral gene transfer between Archaea and !1Bacteria from genome sequence of Thermotoga maritima. !$#cross-references MUID:99287316; PMID:10360571 !$#accession D72249 !'##molecule_type DNA !'##residues 1-66 ##label ARN !'##cross-references GB:AE001798; GB:AE000512; NID:g4982033; !1PIDN:AAD36558.1; PID:g4982056; TIGR:TM1492 !'##experimental_source strain MSB8 GENETICS !$#gene rpmC CLASSIFICATION #superfamily Escherichia coli ribosomal protein L29 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 66 #molecular-weight 7972 #checksum 9004 SEQUENCE /// ENTRY R5BS2L #type complete TITLE ribosomal protein L29 - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jun-2000 ACCESSIONS S05990; E69697 REFERENCE S05989 !$#authors Henkin, T.M.; Moon, S.H.; Mattheakis, L.C.; Nomura, M. !$#journal Nucleic Acids Res. (1989) 17:7469-7486 !$#title Cloning and analysis of the spc ribosomal protein operon of !1Bacillus subtilis: comparison with the spc operon of !1Escherichia coli. !$#cross-references MUID:90016806; PMID:2508062 !$#accession S05990 !'##molecule_type DNA !'##residues 1-66 ##label HEN !'##cross-references EMBL:X15664; NID:g40146; PIDN:CAA33699.1; !1PID:g40148 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69697 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-66 ##label KUN !'##cross-references GB:Z99104; GB:AL009126; NID:g2632267; !1PIDN:CAB11900.1; PID:g2632391 !'##experimental_source strain 168 GENETICS !$#gene rpmC CLASSIFICATION #superfamily Escherichia coli ribosomal protein L29 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 66 #molecular-weight 7713 #checksum 8887 SEQUENCE /// ENTRY R5HS29 #type complete TITLE ribosomal protein L29 [validated] - Haloarcula marismortui ALTERNATE_NAMES ribosomal protein HL33 ORGANISM #formal_name Haloarcula marismortui DATE 31-Mar-1990 #sequence_revision 10-Nov-1995 #text_change 21-Jul-2000 ACCESSIONS A35064; S02396; A49080 REFERENCE A35063 !$#authors Arndt, E.; Kroemer, W.; Hatakeyama, T. !$#journal J. Biol. Chem. (1990) 265:3034-3039 !$#title Organization and nucleotide sequence of a gene cluster !1coding for eight ribosomal proteins in the archaebacterium !1Halobacterium marismortui. !$#cross-references MUID:90153945; PMID:2406244 !$#accession A35064 !'##molecule_type DNA !'##residues 1-71 ##label ARN !'##cross-references EMBL:J05222; NID:g148800; PIDN:AAA86866.1; !1PID:g148808 REFERENCE S02394 !$#authors Hatakeyama, T.; Hatakeyama, T.; Kimura, M. !$#journal FEBS Lett. (1988) 240:21-28 !$#title The primary structures of ribosomal proteins L16, L23 and !1L33 from the archaebacterium Halobacterium marismortui. !$#cross-references MUID:89052888; PMID:3191994 !$#accession S02396 !'##molecule_type protein !'##residues 2-70 ##label HAT !'##note the source is designated as Halobacterium marismortui !'##note the protein is designated as ribosomal protein L33 REFERENCE A49080 !$#authors Bergmann, U.; Wittmann-Liebold, B. !$#journal Biochemistry (1993) 32:2880-2887 !$#title Identification of cross-linked amino acids in the protein !1pair HmaL23-HmaL29 from the 50S ribosomal subunit of the !1archaebacterium Haloarcula marismortui. !$#cross-references MUID:93208105; PMID:8457554 !$#accession A49080 !'##status preliminary !'##molecule_type protein !'##residues 53-57,'X',59-71 ##label BER CLASSIFICATION #superfamily Escherichia coli ribosomal protein L29 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-71 #product ribosomal protein L29 #status experimental !8#label MAT SUMMARY #length 71 #molecular-weight 7879 #checksum 9627 SEQUENCE /// ENTRY S11599 #type complete TITLE ribosomal protein L29 [similarity] - Halobacterium salinarum ORGANISM #formal_name Halobacterium salinarum DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 21-Jul-2000 ACCESSIONS S11599; T43823 REFERENCE S11597 !$#authors Spiridonova, V.A.; Akhmanova, A.S.; Kagramanova, V.K.; !1Koepke, A.K.E.; Mankin, A.S. !$#journal Can. J. Microbiol. (1989) 35:153-159 !$#title Ribosomal protein gene cluster of Halobacterium halobium: !1nucleotide sequence of the genes coding for S3 and L29 !1equivalent ribosomal proteins. !$#cross-references MUID:89248673; PMID:2470481 !$#accession S11599 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-71 ##label SPI !'##note the source is designated as Halobacterium halobium REFERENCE Z22697 !$#authors Itoh, T. !$#submission submitted to the EMBL Data Library, September 1997 !$#accession T43823 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-71 ##label ITO !'##cross-references EMBL:AB006961; PIDN:BAA22277.1 !'##note the source is designated as Halobacterium halobium GENETICS !$#gene HhaL29 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L29 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 71 #molecular-weight 7884 #checksum 1106 SEQUENCE /// ENTRY R5YM29 #type complete TITLE ribosomal protein L29 - Mycoplasma capricolum ORGANISM #formal_name Mycoplasma capricolum DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 07-Dec-1999 ACCESSIONS S02839 REFERENCE S02830 !$#authors Ohkubo, S.; Muto, A.; Kawauchi, Y.; Yamao, F.; Osawa, S. !$#journal Mol. Gen. Genet. (1987) 210:314-322 !$#title The ribosomal protein gene cluster of Mycoplasma capricolum. !$#cross-references MUID:88142549; PMID:3481422 !$#accession S02839 !'##molecule_type DNA !'##residues 1-138 ##label OHK !'##cross-references EMBL:X06414; NID:g44207; PIDN:CAA29712.1; !1PID:g44217 GENETICS !$#gene rpl29 !$#genetic_code SGC3 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L29 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 138 #molecular-weight 15638 #checksum 1219 SEQUENCE /// ENTRY R5EC30 #type complete TITLE ribosomal protein L30 [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 12-Aug-1981 #sequence_revision 14-Nov-1997 #text_change 01-Mar-2002 ACCESSIONS A65123; A02826 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65123 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-59 ##label BLAT !'##cross-references GB:AE000408; GB:U00096; NID:g1789694; !1PIDN:AAC76327.1; PID:g1789698; UWGP:b3302 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A02826 !$#authors Ritter, E.; Wittmann-Liebold, B. !$#journal FEBS Lett. (1975) 60:153-155 !$#title The primary structure of protein L30 from Escherichia coli !1ribosomes. !$#cross-references MUID:76210773; PMID:776670 !$#accession A02826 !'##molecule_type protein !'##residues 2-59 ##label RIT !'##experimental_source strain K REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note mass spectrographic analysis of post-translational !1modifications; any acid labile modifications may have been !1missed GENETICS !$#gene rpmD !$#map_position 73 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX large subunit ribosomal proteins: L1 (PIR:R5EC1), L3 !1(PIR:R5EC3), L2 (PIR:R5EC2), L4 (PIR:R5EC4), L5 (PIR:R5EC5), !1L6 (PIR:R5EC6), L7/L12 (PIR:R5EC7), L9 (PIR:R5EC9), L10 !1(PIR:R5EC10), L11 (PIR:R5EC11), L13 (PIR:R5EC13), L14 !1(PIR:R5EC14), L15 (PIR:R5EC15), L16 (PIR:R5EC16), L17 !1(PIR:R5EC17), L18 (PIR:R5EC18), L19 (PIR:R5EC19) FUNCTION !$#pathway protein biosynthesis !$#note located near the guanosine triphosphatase center CLASSIFICATION #superfamily Escherichia coli ribosomal protein L30 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-59 #product ribosomal protein L30 #status experimental !8#label MAT SUMMARY #length 59 #molecular-weight 6542 #checksum 6641 SEQUENCE /// ENTRY R5BS3F #type complete TITLE ribosomal protein L30 - Bacillus stearothermophilus ORGANISM #formal_name Bacillus stearothermophilus DATE 28-Feb-1986 #sequence_revision 17-Mar-1987 #text_change 17-Mar-1994 ACCESSIONS A02827 REFERENCE A92442 !$#authors Kimura, M. !$#journal J. Biol. Chem. (1984) 259:1051-1055 !$#title Proteins of the Bacillus stearothermophilus ribosome. The !1amino acid sequences of protein S5 and L30. !$#cross-references MUID:84111493; PMID:6363400 !$#accession A02827 !'##molecule_type protein !'##residues 1-62 ##label KIM !'##note the amidation states of residues 61 and 62 were not determined REFERENCE A94128 !$#authors Wilson, K.S.; Appelt, K.; Badger, J.; Tanaka, I.; White, !1S.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:7251-7255 !$#title Crystal structure of a prokaryotic ribosomal protein. !$#cross-references MUID:87016925; PMID:3463963 !$#contents annotation; X-ray crystallography, 2.5 angstroms CLASSIFICATION #superfamily Escherichia coli ribosomal protein L30 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 62 #molecular-weight 7053 #checksum 8689 SEQUENCE /// ENTRY R5BS30 #type complete TITLE ribosomal protein L30 - Bacillus subtilis ALTERNATE_NAMES ribosomal protein BL27 ORGANISM #formal_name Bacillus subtilis DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jun-2000 ACCESSIONS S12681; JS0490; JP0049; F69697 REFERENCE S12680 !$#authors Yoshikawa, H.; Doi, R.H. !$#journal Nucleic Acids Res. (1990) 18:1647 !$#title Sequence of the Bacillus subtilis spectinomycin resistance !1gene region. !$#cross-references MUID:90221911; PMID:2139212 !$#accession S12681 !'##molecule_type DNA !'##residues 1-59 ##label YOS !'##cross-references EMBL:M31102; NID:g1184272; PIDN:AAB59116.1; !1PID:g143576 REFERENCE JS0490 !$#authors Nakamura, K.; Nakamura, A.; Takamatsu, H.; Yoshikawa, H.; !1Yamane, K. !$#journal J. Biochem. (1990) 107:603-607 !$#title Cloning and characterization of a Bacillus subtilis gene !1homologous to E. coli secY. !$#cross-references MUID:90292990; PMID:2113521 !$#accession JS0490 !'##molecule_type DNA !'##residues 1-59 ##label NAK !'##cross-references DDBJ:D00619; NID:g216336; PIDN:BAA00493.1; !1PID:g216337 REFERENCE JP0042 !$#authors Ochi, K. !$#submission submitted to JIPID, February 1994 !$#description Phylogenetic diversity in the genus Bacillus and comparative !1ribosomal protein AT-L30 analyses of the genus !1Thermoactinomyces and relatives. !$#accession JP0049 !'##molecule_type protein !'##residues 2-23,'X',25-28 ##label OCH REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69697 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-59 ##label KUN !'##cross-references GB:Z99104; GB:AL009126; NID:g2632267; !1PIDN:CAB11910.1; PID:g2632401 !'##experimental_source strain 168 GENETICS !$#gene rpmD CLASSIFICATION #superfamily Escherichia coli ribosomal protein L30 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 59 #molecular-weight 6638 #checksum 8688 SEQUENCE /// ENTRY R5HU31 #type complete TITLE ribosomal protein L31 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S05576; S07763 REFERENCE S05576 !$#authors Nobori, T.; Hexdall, L.E.; Carson, D.A. !$#journal Nucleic Acids Res. (1989) 17:7105 !$#title cDNA sequence of human ribosomal protein L31. !$#cross-references MUID:89386063; PMID:2780320 !$#accession S05576 !'##molecule_type mRNA !'##residues 1-125 ##label NOB !'##cross-references EMBL:X15940; NID:g36129; PIDN:CAA34066.1; !1PID:g36130 REFERENCE S07763 !$#authors Chester, K.A.; Robson, L.; Begent, R.H.J.; Talbot, I.C.; !1Pringle, J.H.; Primrose, L.; Macpherson, A.J.S.; Boxer, G.; !1Southall, P.; Malcolm, A.D.B. !$#journal Biochim. Biophys. Acta (1989) 1009:297-300 !$#title Identification of a human ribosomal protein mRNA with !1increased expression in colorectal tumours. !$#cross-references MUID:90089407; PMID:2597680 !$#accession S07763 !'##molecule_type mRNA !'##residues 1-41 ##label CHE !'##cross-references EMBL:X16953 GENETICS !$#gene GDB:RPL31 !'##cross-references GDB:118867 !$#map_position 8pter-8qter CLASSIFICATION #superfamily rat ribosomal protein L31 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 125 #molecular-weight 14463 #checksum 460 SEQUENCE /// ENTRY R5RT31 #type complete TITLE ribosomal protein L31, cytosolic - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 21-Jul-2000 ACCESSIONS A26417 REFERENCE A26417 !$#authors Tanaka, T.; Kuwano, Y.; Kuzumaki, T.; Ishikawa, K.; Ogata, !1K. !$#journal Eur. J. Biochem. (1987) 162:45-48 !$#title Nucleotide sequence of cloned cDNA specific for rat !1ribosomal protein L31. !$#cross-references MUID:87133543; PMID:3816785 !$#accession A26417 !'##molecule_type mRNA !'##residues 1-125 ##label TAN !'##cross-references GB:X04809; NID:g57114; PIDN:CAA28500.1; PID:g57115 CLASSIFICATION #superfamily rat ribosomal protein L31 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-125 #product ribosomal protein L31 #status predicted !8#label MAT SUMMARY #length 125 #molecular-weight 14463 #checksum 460 SEQUENCE /// ENTRY R5BY1E #type complete TITLE ribosomal protein L31.e.A, cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein D2478; protein YDL075w; ribosomal protein YL28; ribosomal protein YL34 ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Jun-2000 ACCESSIONS S67611; S05866; S11260; D47586 REFERENCE S67608 !$#authors Wambutt, R.; Wedler, H.; Wedler, E.; Scharfe, M. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67611 !'##molecule_type DNA !'##residues 1-113 ##label WAM !'##cross-references EMBL:Z74123; NID:g1431089; PIDN:CAA98641.1; !1PID:g1431090; GSPDB:GN00004; MIPS:YDL075w !'##experimental_source strain S288C REFERENCE S05866 !$#authors Schaap, P.J.; Molenaar, C.M.T.; Mager, W.H.; Planta, R.J. !$#journal Curr. Genet. (1984) 9:47-52 !$#title The primary structure of a gene encoding yeast ribosomal !1protein L34. !$#accession S05866 !'##molecule_type DNA !'##residues 1-113 ##label SCH !'##cross-references EMBL:X01441; NID:g4389; PIDN:CAA25679.1; PID:g4390 REFERENCE S11249 !$#authors Otaka, E.; Higo, K.I.; Itoh, T. !$#journal Mol. Gen. Genet. (1984) 195:544-546 !$#title Yeast ribosomal proteins. VIII. Isolation of two proteins !1and sequence characterization of twenty-four proteins from !1cytoplasmic ribosomes. !$#accession S11260 !'##molecule_type protein !'##residues 2-10,'Z',12-14,'B',16-34,'Z',36-46,'BB',49-51 ##label OTA REFERENCE A47586 !$#authors Parikh, V.S.; Morgan, M.M.; Scott, R.; Clements, L.S.; !1Butow, R.A. !$#journal Science (1987) 235:576-580 !$#title The mitochondrial genotype can influence nuclear gene !1expression in yeast. !$#cross-references MUID:87120291; PMID:3027892 !$#accession D47586 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 7-62,'S',64-82 ##label PAR !'##cross-references GB:M15162; NID:g171954; PIDN:AAA66923.1; !1PID:g808844 GENETICS !$#gene SGD:RPL43A; RPL34; MIPS:YDL075w !'##cross-references SGD:S0002233; MIPS:YDL075w !$#map_position 4L !$#introns 19/3 CLASSIFICATION #superfamily rat ribosomal protein L31 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-113 #product ribosomal protein L31.e #status experimental !8#label MAT SUMMARY #length 113 #molecular-weight 12953 #checksum 6902 SEQUENCE /// ENTRY R5HSER #type complete TITLE ribosomal protein L31.eR [validated] - Haloarcula marismortui ALTERNATE_NAMES ribosomal protein HL30 ORGANISM #formal_name Haloarcula marismortui DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 04-Feb-2000 ACCESSIONS S13067; S10761 REFERENCE S13066 !$#authors Bergmann, U.; Arndt, E. !$#journal Biochim. Biophys. Acta (1990) 1050:56-60 !$#title Evidence for an additional archaebacterial gene cluster in !1Halobacterium marismortui encoding ribosomal proteins HL46e !1and HL30. !$#cross-references MUID:91002676; PMID:2207169 !$#accession S13067 !'##molecule_type DNA !'##residues 1-92 ##label BER !'##cross-references EMBL:X55007; NID:g43599; PIDN:CAA38751.1; !1PID:g43601 !'##note the source is designated as Halobacterium marismortui REFERENCE S10761 !$#authors Hatakeyama, T.; Hatakeyama, T. !$#journal Biochim. Biophys. Acta (1990) 1039:343-347 !$#title Amino acid sequences of the ribosomal proteins HL30 and !1HmaL5 from the archaebacterium Halobacterium marismortui. !$#cross-references MUID:90335268; PMID:2198942 !$#accession S10761 !'##molecule_type protein !'##residues 2-92 ##label HAT !'##note the source is designated as Halobacterium marismortui !'##note the protein is designated as ribosomal protein HL30 CLASSIFICATION #superfamily rat ribosomal protein L31 KEYWORDS acetylated amino end; protein biosynthesis; ribosome FEATURE !$2-92 #product ribosomal protein L31eR #status experimental !8#label MAT\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental SUMMARY #length 92 #molecular-weight 10366 #checksum 8946 SEQUENCE /// ENTRY R5EC31 #type complete TITLE ribosomal protein L31 [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-May-1979 #sequence_revision 03-Oct-1995 #text_change 01-Mar-2002 ACCESSIONS S40879; A02828; C65200 REFERENCE S40802 !$#authors Plunkett III, G.; Burland, V.; Daniels, D.L.; Blattner, F.R. !$#journal Nucleic Acids Res. (1993) 21:3391-3398 !$#title Analysis of the Escherichia coli genome. III. DNA sequence !1of the region from 87.2 to 89.2 minutes. !$#cross-references MUID:93347969; PMID:8346018 !$#accession S40879 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-70 ##label PLU !'##cross-references EMBL:L19201; NID:g304961; PIDN:AAB03068.1; !1PID:g305039 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1993 REFERENCE A02828 !$#authors Brosius, J. !$#journal Biochemistry (1978) 17:501-508 !$#title Primary structure of Escherichia coli ribosomal protein L31. !$#cross-references MUID:78080789; PMID:339950 !$#accession A02828 !'##molecule_type protein !'##residues 1-62 ##label BRO !'##experimental_source strain B REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65200 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-70 ##label BLAT !'##cross-references GB:AE000467; GB:U00096; NID:g1790356; !1PIDN:AAC76918.1; PID:g1790371; UWGP:b3936 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note mass spectrographic analysis of post-translational !1modifications; any acid labile modifications may have been !1missed GENETICS !$#gene rpmE !$#map_position 89 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX large subunit ribosomal proteins: L1 (PIR:R5EC1), L3 !1(PIR:R5EC3), L2 (PIR:R5EC2), L4 (PIR:R5EC4), L5 (PIR:R5EC5), !1L6 (PIR:R5EC6), L7/L12 (PIR:R5EC7), L9 (PIR:R5EC9), L10 !1(PIR:R5EC10), L11 (PIR:R5EC11), L13 (PIR:R5EC13), L14 !1(PIR:R5EC14), L15 (PIR:R5EC15), L16 (PIR:R5EC16), L17 !1(PIR:R5EC17), L18 (PIR:R5EC18), L19 (PIR:R5EC19) FUNCTION !$#pathway protein biosynthesis CLASSIFICATION #superfamily Escherichia coli ribosomal protein L31 KEYWORDS protein biosynthesis; ribosome FEATURE !$1-70 #product ribosomal protein L31, unmodified #status !8experimental #label MAT1\ !$1-62 #product ribosomal protein L31, modified #status !8experimental #label MAT2 SUMMARY #length 70 #molecular-weight 7871 #checksum 2818 SEQUENCE /// ENTRY B64091 #type complete TITLE ribosomal protein L31 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 18-Aug-1995 #sequence_revision 04-Oct-1996 #text_change 22-Jun-1999 ACCESSIONS B64091 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession B64091 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-70 ##label TIGR !'##cross-references GB:U32760; GB:L42023; NID:g1573764; !1PIDN:AAC22417.1; PID:g1573767; TIGR:HI0758 GENETICS !$#gene rpL31 CLASSIFICATION #superfamily Escherichia coli ribosomal protein L31 KEYWORDS protein biosynthesis; ribosome FEATURE !$1-70 #product ribosomal protein L31 #status predicted !8#label MAT SUMMARY #length 70 #molecular-weight 7833 #checksum 4479 SEQUENCE /// ENTRY S55431 #type complete TITLE ribosomal protein L31 - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 15-Jul-1995 #sequence_revision 04-Oct-1996 #text_change 16-Jun-2000 ACCESSIONS S55431; G69697 REFERENCE S55414 !$#authors Glaser, P.; Danchin, A. !$#submission submitted to the EMBL Data Library, May 1995 !$#description Cloning and sequencing of the Bacillus subtilis chromosomal !1region from 320 degrees to 321 degrees. !$#accession S55431 !'##molecule_type DNA !'##residues 1-66 ##label GLA !'##cross-references EMBL:Z49782; NID:g853752; PIDN:CAA89878.1; !1PID:g853770 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69697 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-66 ##label KUN !'##cross-references GB:Z99122; GB:Z99123; GB:AL009126; NID:g2636240; !1PIDN:CAB15735.1; PID:g2636244; NID:g2636029; PID:g2636232 !'##experimental_source strain 168 GENETICS !$#gene rpmE CLASSIFICATION #superfamily Escherichia coli ribosomal protein L31 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 66 #molecular-weight 7444 #checksum 7525 SEQUENCE /// ENTRY H64755 #type complete TITLE ribosomal protein L31 homolog ykgM - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS H64755 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64755 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-87 ##label BLAT !'##cross-references GB:AE000137; GB:U00096; NID:g2367108; !1PIDN:AAC73399.1; PID:g2367109; UWGP:b0296 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ykgM CLASSIFICATION #superfamily Escherichia coli ribosomal protein L31 KEYWORDS ribosome SUMMARY #length 87 #molecular-weight 9920 #checksum 5044 SEQUENCE /// ENTRY R5HSH9 #type complete TITLE ribosomal protein L18.eR [validated] - Haloarcula marismortui ALTERNATE_NAMES ribosomal protein HL19; ribosomal protein HL29 ORGANISM #formal_name Haloarcula marismortui DATE 31-Mar-1991 #sequence_revision 31-Dec-1992 #text_change 21-Jul-2000 ACCESSIONS A41715; S00369; D28926; S35655; E44126 REFERENCE A41715 !$#authors Kroemer, W.J.; Arndt, E. !$#journal J. Biol. Chem. (1991) 266:24573-24579 !$#title Halobacterial S9 operon. Three ribosomal protein genes are !1cotranscribed with genes encoding a tRNA(leu), the enolase, !1and a putative membrane protein in the archaebacterium !1Haloarcula (halobacterium) marismortui. !$#cross-references MUID:92105119; PMID:1840597 !$#accession A41715 !'##molecule_type DNA !'##residues 1-116 ##label KRO !'##cross-references GB:M76567; NID:g148775; PIDN:AAA73096.1; !1PID:g148776 REFERENCE S00368 !$#authors Hatakeyama, T.; Kimura, M. !$#journal Eur. J. Biochem. (1988) 172:703-711 !$#title Complete amino acid sequences of the ribosomal proteins L25, !1L29 and L31 from the archaebacterium Halobacterium !1marismortui. !$#cross-references MUID:88166754; PMID:3350019 !$#accession S00369 !'##molecule_type protein !'##residues 2-116 ##label HAT !'##note the source is designated as Halobacterium marismortui !'##note the protein is designated as ribosomal protein L29 REFERENCE A28926 !$#authors Walsh, M.J.; McDougall, J.; Wittmann-Liebold, B. !$#journal Biochemistry (1988) 27:6867-6876 !$#title Extended N-terminal sequencing of proteins of !1archaebacterial ribosomes blotted from two-dimensional gels !1onto glass fiber and poly(vinylidene difluoride) membrane. !$#cross-references MUID:89062418; PMID:3196689 !$#accession D28926 !'##molecule_type protein !'##residues 2-24 ##label WAL !'##note the protein is designated as ribosomal protein L19 REFERENCE S35654 !$#authors Bergmann, U.; Wittmann-Liebold, B. !$#journal J. Mol. Biol. (1993) 232:693-700 !$#title Localization of proteins HL29 and HL31 from Haloarcula !1marismortui within the 50 S ribosomal subunit by chemical !1crosslinking. !$#cross-references MUID:93347250; PMID:8345527 !$#accession S35655 !'##molecule_type protein !'##residues 4-27;37-39;65-82 ##label BER !'##note the protein is designated as ribosomal protein HL29 REFERENCE A44126 !$#authors Scholzen, T.; Arndt, E. !$#journal J. Biol. Chem. (1992) 267:12123-12130 !$#title The alpha-operon equivalent genome region in the extreme !1halophilic archaebacterium Haloarcula (Halobacterium) !1marismortui. !$#cross-references MUID:92291093; PMID:1376318 !$#accession E44126 !'##status preliminary !'##molecule_type DNA !'##residues 1-72 ##label SCH !'##cross-references GB:M87833; NID:g148769; PIDN:AAA73213.1; !1PID:g148774 !'##note sequence extracted from NCBI backbone (NCBIN:106619, !1NCBIP:106624) CLASSIFICATION #superfamily Haloarcula ribosomal protein HL29 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-116 #product ribosomal protein HL29 #status experimental !8#label MAT SUMMARY #length 116 #molecular-weight 12422 #checksum 827 SEQUENCE /// ENTRY T43941 #type complete TITLE ribosomal protein L18.eR [similarity] - Halobacterium salinarum ORGANISM #formal_name Halobacterium salinarum DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 21-Jul-2000 ACCESSIONS T43941 REFERENCE Z22729 !$#authors Sano, K.; Taguchi, A.; Furumoto, H.; Uda, T.; Itoh, T. !$#journal Biochem. Biophys. Res. Commun. (1999) 264:24-28 !$#title Cloning, sequencing, and characterization of ribosomal !1protein and RNA polymerase genes from the region analogous !1to the alpha-operon of Escherichia coli in halophilic !1archaea, Halobacterium halobium. !$#cross-references MUID:99458614; PMID:10527834 !$#accession T43941 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-117 ##label SAN !'##cross-references EMBL:AB030282; PIDN:BAA85899.1 !'##note the source is designated as Halobacterium halobium CLASSIFICATION #superfamily Haloarcula ribosomal protein HL29 SUMMARY #length 117 #molecular-weight 12591 #checksum 103 SEQUENCE /// ENTRY R5HS31 #type complete TITLE ribosomal protein L21.eR [validated] - Haloarcula marismortui ALTERNATE_NAMES ribosomal protein HL31 ORGANISM #formal_name Haloarcula marismortui DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 21-Jul-2000 ACCESSIONS S00370 REFERENCE S00368 !$#authors Hatakeyama, T.; Kimura, M. !$#journal Eur. J. Biochem. (1988) 172:703-711 !$#title Complete amino acid sequences of the ribosomal proteins L25, !1L29 and L31 from the archaebacterium Halobacterium !1marismortui. !$#cross-references MUID:88166754; PMID:3350019 !$#accession S00370 !'##molecule_type protein !'##residues 1-95 ##label HAT !'##note the source is designated as Halobacterium marismortui !'##note the protein is designated as ribosomal protein L31 CLASSIFICATION #superfamily Haloarcula ribosomal protein HL31 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 95 #molecular-weight 10417 #checksum 1027 SEQUENCE /// ENTRY R5BY31 #type complete TITLE ribosomal protein YmL31 precursor, mitochondrial - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YKL138c; ribosomal protein MRP31, mitochondrial ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 12-Nov-1999 ACCESSIONS S22245; S37967; S26757 REFERENCE S22245 !$#authors Grohmann, L.; Graack, H.R.; Kitakawa, M. !$#journal Eur. J. Biochem. (1989) 183:155-160 !$#title Molecular cloning of the nuclear gene for mitochondrial !1ribosomal protein YmL31 from Saccharomyces cerevisiae. !$#cross-references MUID:89325329; PMID:2666132 !$#accession S22245 !'##molecule_type DNA !'##residues 1-131 ##label GRO !'##cross-references EMBL:X15099; NID:g3977; PIDN:CAA33202.1; PID:g3978 REFERENCE S37953 !$#authors Ramezani Rad, M.; Xu, G.; Kirchrath, L.; Fritz, C.; Keuchel, !1H.; Hollenberg, C.P. !$#submission submitted to the Protein Sequence Database, March 1994 !$#accession S37967 !'##molecule_type DNA !'##residues 1-131 ##label RAM !'##cross-references EMBL:Z28138; NID:g486232; PIDN:CAA81979.1; !1PID:g486233; GSPDB:GN00011; MIPS:YKL138c !'##experimental_source strain S288C REFERENCE S26754 !$#authors Graack, H.R.; Grohmann, L.; Choli, T. !$#journal FEBS Lett. (1988) 242:4-8 !$#title Mitochondrial ribosomes of yeast: isolation of individual !1proteins and N-terminal sequencing. !$#cross-references MUID:89078618; PMID:3060376 !$#accession S26757 !'##molecule_type protein !'##residues 13-48,'X',50 ##label GRA GENETICS !$#gene SGD:MRPL31; MIPS:YKL138c !'##cross-references SGD:S0001621; MIPS:YKL138c !$#map_position 11L !$#genome nuclear CLASSIFICATION #superfamily ribosomal protein YmL31 KEYWORDS mitochondrion; protein biosynthesis; ribosome FEATURE !$1-12 #domain transit peptide (mitochondrion) #status !8experimental #label TNP\ !$13-131 #product ribosomal protein YmL31 #status experimental !8#label MAT SUMMARY #length 131 #molecular-weight 15520 #checksum 7718 SEQUENCE /// ENTRY R5HU32 #type complete TITLE ribosomal protein L32 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S11393 REFERENCE S11393 !$#authors Young, J.A.T.; Trowsdale, J. !$#journal Nucleic Acids Res. (1985) 13:8883-8891 !$#title A processed pseudogene in an intron of the HLA-DP-beta-1 !1chain gene is a member of the ribosomal protein L32 gene !1family. !$#cross-references MUID:86093685; PMID:3866218 !$#accession S11393 !'##molecule_type mRNA !'##residues 1-135 ##label YOU !'##cross-references EMBL:X03342; NID:g36131; PIDN:CAA27048.1; !1PID:g36132 GENETICS !$#gene GDB:RPL32 !'##cross-references GDB:119567 !$#map_position 3pter-3qter CLASSIFICATION #superfamily rat ribosomal protein L32 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 135 #molecular-weight 15860 #checksum 2116 SEQUENCE /// ENTRY R5MS32 #type complete TITLE ribosomal protein L32 - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 21-Jul-2000 ACCESSIONS A02829; JH0321 REFERENCE A02829 !$#authors Dudov, K.P.; Perry, R.P. !$#journal Cell (1984) 37:457-468 !$#title The gene family encoding the mouse ribosomal protein L32 !1contains a uniquely expressed intron-containing gene and an !1unmutated processed gene. !$#cross-references MUID:84205680; PMID:6327068 !$#accession A02829 !'##molecule_type DNA !'##residues 1-135 ##label DUD !'##cross-references GB:K02060; NID:g3228365; PIDN:AAC28897.1; !1PID:g200781 REFERENCE PH0108 !$#authors Nikaido, T.; Bradley, D.W.; Pardee, A.B. !$#journal Exp. Cell Res. (1991) 192:102-109 !$#title Molecular cloning of transcripts that accumulate during the !1late G1 phase in cultured mouse cells. !$#cross-references MUID:91078351; PMID:1984406 !$#accession JH0321 !'##molecule_type mRNA !'##residues 1-135 ##label NIK GENETICS !$#introns 32/3; 93/2 CLASSIFICATION #superfamily rat ribosomal protein L32 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 135 #molecular-weight 15860 #checksum 2116 SEQUENCE /// ENTRY R5RT32 #type complete TITLE ribosomal protein L32, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 21-Jul-2000 ACCESSIONS S02123; S20561 REFERENCE S02123 !$#authors Rajchel, A.; Chan, Y.L.; Wool, I.G. !$#journal Nucleic Acids Res. (1988) 16:2347 !$#title The primary structure of rat ribosomal protein L32. !$#cross-references MUID:88189837; PMID:3357790 !$#accession S02123 !'##molecule_type mRNA !'##residues 1-135 ##label RAJ !'##cross-references EMBL:X06483; NID:g57116; PIDN:CAA29777.1; !1PID:g57117 !$#accession S20561 !'##molecule_type protein !'##residues 2-9 ##label RAJ2 !'##note the protein is designated as ribosomal protein L32 CLASSIFICATION #superfamily rat ribosomal protein L32 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-135 #product ribosomal protein L32 #status experimental !8#label MAT SUMMARY #length 135 #molecular-weight 15860 #checksum 2116 SEQUENCE /// ENTRY R5FF32 #type complete TITLE ribosomal protein L32 - fruit fly (Drosophila subobscura) ALTERNATE_NAMES ribosomal protein 49 ORGANISM #formal_name Drosophila subobscura DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 22-Jun-1999 ACCESSIONS A31207 REFERENCE A31207 !$#authors Aguade, M. !$#journal Mol. Biol. Evol. (1988) 5:433-441 !$#title Nucleotide sequence comparison of the rp49 gene region !1between Drosophila subobscura and D. melanogaster. !$#cross-references MUID:88301859; PMID:3136296 !$#accession A31207 !'##molecule_type DNA !'##residues 1-134 ##label AGU !'##cross-references GB:M21333; NID:g158307; PIDN:AAA28857.1; !1PID:g158308 GENETICS !$#gene FlyBase:Dsub/Rp49 !'##cross-references FlyBase:FBgn0012945 !$#introns 31/3 CLASSIFICATION #superfamily rat ribosomal protein L32 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 134 #molecular-weight 16076 #checksum 9903 SEQUENCE /// ENTRY R5FF49 #type complete TITLE ribosomal protein L32 - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES ribosomal protein 49 ORGANISM #formal_name Drosophila melanogaster DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 16-Feb-1997 ACCESSIONS A02830 REFERENCE A93527 !$#authors O'Connell, P.; Rosbash, M. !$#journal Nucleic Acids Res. (1984) 12:5495-5513 !$#title Sequence, structure, and codon preference of the Drosophila !1ribosomal protein 49 gene. !$#cross-references MUID:84272233; PMID:6087289 !$#accession A02830 !'##molecule_type DNA !'##residues 1-133 ##label OCO GENETICS !$#gene Rbp49 !'##cross-references FlyBase:FBgn0002626 !$#map_position 3R 99D !$#introns 31/3 CLASSIFICATION #superfamily rat ribosomal protein L32 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 133 #molecular-weight 15733 #checksum 9736 SEQUENCE /// ENTRY R5MXD #type complete TITLE ribosomal protein D - Methanococcus vannielii ORGANISM #formal_name Methanococcus vannielii DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 22-Jun-1999 ACCESSIONS S05621 REFERENCE S05611 !$#authors Auer, J.; Spicker, G.; Boeck, A. !$#journal J. Mol. Biol. (1989) 209:21-36 !$#title Organization and structure of the Methanococcus !1transcriptional unit homologous to the Escherichia coli !1"spectinomycin operon". Implications for the evolutionary !1relationship of 70 S and 80 S ribosomes. !$#cross-references MUID:90040717; PMID:2530355 !$#accession S05621 !'##molecule_type DNA !'##residues 1-135 ##label AUE !'##cross-references EMBL:X16720; NID:g44754; PIDN:CAA34697.1; !1PID:g44765 CLASSIFICATION #superfamily rat ribosomal protein L32 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 135 #molecular-weight 15524 #checksum 3417 SEQUENCE /// ENTRY R7HSH5 #type complete TITLE ribosomal protein L32.eR [validated] - Haloarcula marismortui ALTERNATE_NAMES ribosomal protein HL5 ORGANISM #formal_name Haloarcula marismortui DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 31-Mar-2000 ACCESSIONS S16539; B28949; T46804 REFERENCE S16535 !$#authors Scholzen, T.; Arndt, E. !$#journal Mol. Gen. Genet. (1991) 228:70-80 !$#title Organization and nucleotide sequence of ten ribosomal !1protein genes from the region equivalent to the !1spectinomycin operon in the archaebacterium Halobacterium !1marismortui. !$#cross-references MUID:91360093; PMID:1832208 !$#accession S16539 !'##molecule_type DNA !'##residues 1-241 ##label SCH !'##cross-references EMBL:X58395; NID:g48860; PIDN:CAA41288.1; !1PID:g48865 REFERENCE A28926 !$#authors Walsh, M.J.; McDougall, J.; Wittmann-Liebold, B. !$#journal Biochemistry (1988) 27:6867-6876 !$#title Extended N-terminal sequencing of proteins of !1archaebacterial ribosomes blotted from two-dimensional gels !1onto glass fiber and poly(vinylidene difluoride) membrane. !$#cross-references MUID:89062418; PMID:3196689 !$#accession B28949 !'##molecule_type protein !'##residues 2-25,'R',27-30,32;98-109,'SL',112-113 ##label WAL !'##note the source is designated as Halobacterium marismortui !'##note the protein is designated as ribosomal protein L5 GENETICS !$#gene HL5 CLASSIFICATION #superfamily rat ribosomal protein L32 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-241 #product ribosomal protein HL5 #status experimental !8#label MAT SUMMARY #length 241 #molecular-weight 26416 #checksum 1500 SEQUENCE /// ENTRY R6RT30 #type complete TITLE ribosomal protein L30, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1987 #sequence_revision 30-Jun-1991 #text_change 21-Jul-2000 ACCESSIONS B24028; S11420 REFERENCE A24028 !$#authors Nakanishi, O.; Oyanagi, M.; Kuwano, Y.; Tanaka, T.; !1Nakayama, T.; Mitsui, H.; Nabeshima, Y.I.; Ogata, K. !$#journal Gene (1985) 35:289-296 !$#title Molecular cloning and nucleotide sequences of cDNAs specific !1for rat liver ribosomal proteins S17 and L30. !$#cross-references MUID:86006278; PMID:3840111 !$#accession B24028 !'##molecule_type mRNA !'##residues 1-115 ##label NAK !'##cross-references EMBL:K02932; NID:g206727; PIDN:AAA42072.1; !1PID:g206728 !'##note the 5'-noncoding region including the initiator Met was missing !1from the cloned cDNA REFERENCE S11413 !$#authors Wittmann-Liebold, B.; Geissler, A.W.; Lin, A.; Wool, I.G. !$#journal J. Supramol. Struct. (1979) 12:425-433 !$#title Sequence of the amino-terminal region of rat liver ribosomal !1proteins S4, S6, S8, L6, L7a, L18, L27, L30, L37, L37a, and !1L39. !$#cross-references MUID:80252792; PMID:398910 !$#accession S11420 !'##molecule_type protein !'##residues 2-6,'L',8-33 ##label WIT !'##note the protein is designated as ribosomal protein L30 CLASSIFICATION #superfamily rat ribosomal protein L30 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-115 #product ribosomal protein L30 #status experimental !8#label MAT SUMMARY #length 115 #molecular-weight 12784 #checksum 1755 SEQUENCE /// ENTRY R6MS30 #type complete TITLE ribosomal protein L30 - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 22-Jun-1999 ACCESSIONS S11622; A37531 REFERENCE S11622 !$#authors Wiedemann, L.M.; Perry, R.P. !$#journal Mol. Cell. Biol. (1984) 4:2518-2528 !$#title Characterization of the expressed gene and several processed !1pseudogenes for the mouse ribosomal protein L30 gene family. !$#cross-references MUID:85085958; PMID:6513928 !$#accession S11622 !'##molecule_type DNA !'##residues 1-115 ##label WIE !'##cross-references EMBL:K02928; NID:g435126; PIDN:AAA03645.1; !1PID:g200777 !$#accession A37531 !'##molecule_type mRNA !'##residues 8-115 ##label WIE2 GENETICS !$#introns 7/3; 56/2; 100/1 CLASSIFICATION #superfamily rat ribosomal protein L30 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 115 #molecular-weight 12784 #checksum 1755 SEQUENCE /// ENTRY R6BY30 #type complete TITLE ribosomal protein L30.e, cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein G3652; protein YGL030w; ribosomal protein YL32 ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 21-Jul-2000 ACCESSIONS A29779; B29779; C29779; S64032 REFERENCE A29779 !$#authors Dabeva, M.D.; Warner, J.R. !$#journal J. Biol. Chem. (1987) 262:16055-16059 !$#title The yeast ribosomal protein L32 and its gene. !$#cross-references MUID:88058966; PMID:3316213 !$#accession A29779 !'##molecule_type DNA !'##residues 1-105 ##label DAB1 !'##cross-references EMBL:J03457; NID:g172487; PIDN:AAA35005.1; !1PID:g172488 !$#accession B29779 !'##molecule_type mRNA !'##residues 1-105 ##label DAB2 !'##cross-references GB:J03457; NID:g172487; PIDN:AAA35005.1; !1PID:g172488 !$#accession C29779 !'##molecule_type protein !'##residues 2-8 ##label DAB3 REFERENCE S64003 !$#authors Hebling, U.; Hofmann, B.; Delius, H. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64032 !'##molecule_type DNA !'##residues 1-105 ##label HEB !'##cross-references EMBL:Z72552; NID:g1322503; PIDN:CAA96731.1; !1PID:g1322504; GSPDB:GN00007; MIPS:YGL030w !'##experimental_source strain S288C GENETICS !$#gene SGD:RPL32; MIPS:YGL030w !'##cross-references SGD:S0002998; MIPS:YGL030w !$#map_position 7L !$#introns 1/3 CLASSIFICATION #superfamily rat ribosomal protein L30 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-105 #product ribosomal protein L30.e #status experimental !8#label MAT SUMMARY #length 105 #molecular-weight 11415 #checksum 6717 SEQUENCE /// ENTRY R6MXER #type complete TITLE ribosomal protein L30.eR - Methanococcus vannielii ORGANISM #formal_name Methanococcus vannielii DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 22-Jun-1999 ACCESSIONS S06621 REFERENCE S06620 !$#authors Lechner, K.; Heller, G.; Boeck, A. !$#journal J. Mol. Evol. (1989) 29:20-27 !$#title Organization and nucleotide sequence of a transcriptional !1unit of Methanococcus vannielii comprising genes for protein !1synthesis elongation factors and ribosomal proteins. !$#cross-references MUID:89362493; PMID:2475640 !$#accession S06621 !'##molecule_type DNA !'##residues 1-105 ##label LEC !'##cross-references EMBL:X15970; NID:g44780; PIDN:CAA34087.1; !1PID:g44782 CLASSIFICATION #superfamily rat ribosomal protein L30 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 105 #molecular-weight 11515 #checksum 2258 SEQUENCE /// ENTRY C64430 #type complete TITLE ribosomal protein L30.eR - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 13-Sep-1996 #sequence_revision 04-Oct-1996 #text_change 21-Jul-2000 ACCESSIONS C64430 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession C64430 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-110 ##label BUL !'##cross-references GB:U67547; GB:L77117; NID:g1591695; !1PIDN:AAB99048.1; PID:g1591698; TIGR:MJ1044 GENETICS !$#map_position FOR981635-981967 CLASSIFICATION #superfamily rat ribosomal protein L30 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 110 #molecular-weight 12134 #checksum 1917 SEQUENCE /// ENTRY R5HU35 #type complete TITLE ribosomal protein L35a - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 22-Jun-1999 ACCESSIONS S12710 REFERENCE S12710 !$#authors Herzog, H.; Hoefferer, L.; Schneider, R.; Schweiger, M. !$#journal Nucleic Acids Res. (1990) 18:4600 !$#title cDNA encoding the human homologue of rat ribosomal protein !1L35a. !$#cross-references MUID:90356408; PMID:2388839 !$#accession S12710 !'##molecule_type mRNA !'##residues 1-110 ##label HER !'##cross-references EMBL:X52966; NID:g34200; PIDN:CAA37138.1; !1PID:g34201 GENETICS !$#gene GDB:RPL35A !'##cross-references GDB:128849; OMIM:180468 !$#map_position 3q29-3qter CLASSIFICATION #superfamily rat ribosomal protein L35a KEYWORDS protein biosynthesis; ribosome SUMMARY #length 110 #molecular-weight 12495 #checksum 6769 SEQUENCE /// ENTRY R5RT5A #type complete TITLE ribosomal protein L35a, cytosolic - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 21-Jul-2000 ACCESSIONS A25404 REFERENCE A25404 !$#authors Tanaka, T.; Wakasugi, K.; Kuwano, Y.; Ishikawa, K.; Ogata, !1K. !$#journal Eur. J. Biochem. (1986) 154:523-527 !$#title Nucleotide sequence of cloned cDNA specific for rat !1ribosomal protein L35a. !$#cross-references MUID:86136088; PMID:3753935 !$#accession A25404 !'##molecule_type mRNA !'##residues 1-110 ##label TAN !'##cross-references EMBL:X03475; NID:g57118; PIDN:CAA27193.1; !1PID:g57119 CLASSIFICATION #superfamily rat ribosomal protein L35a KEYWORDS protein biosynthesis; ribosome SUMMARY #length 110 #molecular-weight 12554 #checksum 6825 SEQUENCE /// ENTRY R5XL32 #type complete TITLE ribosomal protein L35a - African clawed frog ALTERNATE_NAMES ribosomal protein XL32 ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 17-Dec-1982 #sequence_revision 30-Sep-1991 #text_change 22-Jun-1999 ACCESSIONS S12711; A02831 REFERENCE S12711 !$#authors Bagni, C.; Mariottini, P.; Annesi, F.; Amaldi, F. !$#journal Nucleic Acids Res. (1990) 18:4423-4426 !$#title Structure of Xenopus laevis ribosomal protein L32 and its !1expression during development. !$#cross-references MUID:90356375; PMID:2388827 !$#accession S12711 !'##molecule_type mRNA !'##residues 1-110 ##label BAG1 !'##cross-references EMBL:V01440 REFERENCE A91492 !$#authors Amaldi, F.; Beccari, E.; Bozzoni, I.; Luo, Z.X.; !1Pierandrei-Amaldi, P. !$#journal Gene (1982) 17:311-316 !$#title Nucleotide sequences of cloned cDNA fragments specific for !1six Xenopus laevis ribosomal proteins. !$#cross-references MUID:82262793; PMID:7049839 !$#accession A02831 !'##molecule_type mRNA !'##residues 41-59,'H',61-85,'T',87-88,'H',90-110 ##label BAG2 !'##cross-references EMBL:V01440; NID:g65048; PIDN:CAA24701.1; !1PID:g65049 CLASSIFICATION #superfamily rat ribosomal protein L35a KEYWORDS protein biosynthesis; ribosome SUMMARY #length 110 #molecular-weight 12604 #checksum 6740 SEQUENCE /// ENTRY T34207 #type complete TITLE ribosomal protein L35a - Caenorhabditis elegans ALTERNATE_NAMES protein F10E7.7 ORGANISM #formal_name Caenorhabditis elegans DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 05-May-2000 ACCESSIONS T34207 REFERENCE Z21489 !$#authors Pauley, A. !$#submission submitted to the EMBL Data Library, November 1995 !$#description The sequence of C. elegans cosmid F10E7. !$#accession T34207 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-124 ##label PAU !'##cross-references EMBL:U41264; PIDN:AAA82422.1; CESP:F10E7.7 GENETICS !$#gene CESP:F10E7.7 !$#introns 17/2; 71/3; 117/3 CLASSIFICATION #superfamily rat ribosomal protein L35a KEYWORDS protein biosynthesis; ribosome SUMMARY #length 124 #molecular-weight 13768 #checksum 3950 SEQUENCE /// ENTRY S18431 #type complete TITLE ribosomal protein L35a.e.c16, cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein P2625; protein YPL143w; ribosomal protein YL37 ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 03-Dec-1999 ACCESSIONS S18431; S11262; S65154; S69043 REFERENCE S18431 !$#authors Santangelo, G.M.; Tornow, J.; McLaughlin, C.S.; Moldave, K. !$#journal Gene (1991) 105:137-138 !$#title Screening a yeast promoter library leads to the isolation of !1the RP29/L32 and SNR17B/RPL37A divergent promoters and the !1discovery of a gene encoding ribosomal protein L37. !$#cross-references MUID:92039011; PMID:1840541 !$#accession S18431 !'##molecule_type DNA !'##residues 1-107 ##label SAN !'##cross-references EMBL:X57969; NID:g4391; PIDN:CAA41035.1; PID:g4392 REFERENCE S11249 !$#authors Otaka, E.; Higo, K.I.; Itoh, T. !$#journal Mol. Gen. Genet. (1984) 195:544-546 !$#title Yeast ribosomal proteins. VIII. Isolation of two proteins !1and sequence characterization of twenty-four proteins from !1cytoplasmic ribosomes. !$#accession S11262 !'##molecule_type protein !'##residues 2-23,'D',25,'B' ##label OTA REFERENCE S65154 !$#authors Purnelle, B.; Coster, F.; Goffeau, A. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S65154 !'##molecule_type DNA !'##residues 1-6 ##label PUR !'##cross-references EMBL:Z73499; GSPDB:GN00016; MIPS:YPL143w !'##experimental_source strain S288C (AB972) REFERENCE S69040 !$#authors Hall, J.; DePaulo, T.; Ahmed, A.; Bussey, H.; Fortin, N.; !1Friesen, J.D.; Storms, R.K.; Vo, D.H.; Wang, Y.; Winnett, E. !$#submission submitted to the EMBL Data Library, December 1995 !$#description The sequence of Saccharomyces cerevisiae chromosome XVI left !1arm. !$#accession S69043 !'##molecule_type DNA !'##residues 1-107 ##label HAL !'##cross-references EMBL:U43703; NID:g1244769; PIDN:AAB68218.1; !1PID:g1244773; GSPDB:GN00016; MIPS:YPL143w GENETICS !$#gene SGD:RPL37A; MIPS:YPL143w !'##cross-references SGD:S0006064; MIPS:YPL143w !$#map_position 16L !$#introns 7/1 CLASSIFICATION #superfamily rat ribosomal protein L35a KEYWORDS protein biosynthesis; ribosome FEATURE !$2-107 #product ribosomal protein L35a.e #status !8experimental #label MAT SUMMARY #length 107 #molecular-weight 12154 #checksum 7328 SEQUENCE /// ENTRY S44069 #type complete TITLE ribosomal protein L35a.e.c15, cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein O5224; protein YOR234c; ribosomal protein YL37 ORGANISM #formal_name Saccharomyces cerevisiae DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 21-Jul-2000 ACCESSIONS S44069; S67127 REFERENCE S44069 !$#authors Tornow, J.; Santangelo, G.M. !$#journal Curr. Genet. (1994) 25:480-487 !$#title Saccharomyces cerevisiae ribosomal protein L37 is encoded by !1duplicate genes that are differentially expressed. !$#cross-references MUID:94363772; PMID:8082197 !$#accession S44069 !'##molecule_type DNA !'##residues 1-107 ##label TOR !'##cross-references EMBL:L23923; NID:g484240; PIDN:AAA35006.1; !1PID:g484241 REFERENCE S67104 !$#authors Boyer, J.; Fairhead, C.; Gaillon, L.; Galisson, F.; Michaux, !1G.; Thierry, A.; Dujon, B. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67127 !'##molecule_type DNA !'##residues 1-107 ##label BOY !'##cross-references EMBL:Z75142; NID:g1420536; PIDN:CAA99454.1; !1PID:g1420537; GSPDB:GN00015; MIPS:YOR234c !'##experimental_source strain S288C GENETICS !$#gene SGD:RPL37B; MIPS:YOR234c !'##cross-references SGD:S0005760; MIPS:YOR234c !$#map_position 15R !$#introns 7/1 CLASSIFICATION #superfamily rat ribosomal protein L35a KEYWORDS protein biosynthesis; ribosome FEATURE !$2-107 #product ribosomal protein L35a.e #status predicted !8#label MAT SUMMARY #length 107 #molecular-weight 12168 #checksum 7368 SEQUENCE /// ENTRY T41698 #type complete TITLE ribosomal protein L35a - fission yeast (Schizosaccharomyces pombe) ORGANISM #formal_name Schizosaccharomyces pombe DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 05-May-2000 ACCESSIONS T41698; T43418 REFERENCE Z22010 !$#authors Wedler, H.; Duesterhoeft, A.; McDougall, R.C.; Rajandream, !1M.A.; Barrell, B.G. !$#submission submitted to the EMBL Data Library, October 1999 !$#accession T41698 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-108 ##label WED !'##cross-references EMBL:AL121859; PIDN:CAB58374.1; GSPDB:GN00068; !1SPDB:SPCP31B10.08c !'##experimental_source strain 972h-; clone p1 p31B10 REFERENCE Z22501 !$#authors Kawamukai, M. !$#submission submitted to the EMBL Data Library, September 1998 !$#description S. pombe ribosomal protein L37 homolog. !$#accession T43418 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 2-20,'N',22-108 ##label KAW !'##cross-references EMBL:AB017603; PIDN:BAA33367.1 GENETICS !$#gene SPDB:SPCP31B10.08c !$#map_position 3 !$#introns 70/2 CLASSIFICATION #superfamily rat ribosomal protein L35a KEYWORDS protein biosynthesis; ribosome SUMMARY #length 108 #molecular-weight 12108 #checksum 828 SEQUENCE /// ENTRY QQQYYW #type complete TITLE probable ribosomal protein L35 - Pyrococcus woesei ALTERNATE_NAMES hypothetical protein Y ORGANISM #formal_name Pyrococcus woesei DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 24-Sep-1999 ACCESSIONS S10651 REFERENCE S10650 !$#authors Zwickl, P.; Fabry, S.; Bogedain, C.; Haas, A.; Hensel, R. !$#journal J. Bacteriol. (1990) 172:4329-4338 !$#title Glyceraldehyde-3-phosphate dehydrogenase from the !1hyperthermophilic archaebacterium Pyrococcus woesei: !1characterization of the enzyme, cloning and sequencing of !1the gene, and expression in Escherichia coli. !$#cross-references MUID:90330536; PMID:2165475 !$#accession S10651 !'##molecule_type DNA !'##residues 1-87 ##label ZWI CLASSIFICATION #superfamily rat ribosomal protein L35a SUMMARY #length 87 #molecular-weight 9666 #checksum 2105 SEQUENCE /// ENTRY D75153 #type complete TITLE probable ribosomal protein L35 - Pyrococcus abyssi (strain Orsay) ORGANISM #formal_name Pyrococcus abyssi DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 16-Jun-2000 ACCESSIONS D75153 REFERENCE A75001 !$#authors anonymous, Genoscope !$#submission submitted to the EMBL Data Library, July 1999 !$#description Pyrococcus abyssi genome sequence: insights into archaeal !1chromosome structure and evolution. !$#accession D75153 !'##molecule_type DNA !'##residues 1-87 ##label KAW !'##cross-references GB:AJ248284; GB:AL096836; NID:g5457730; !1PIDN:CAB49307.1; PID:g5457817 !'##experimental_source strain Orsay GENETICS !$#gene PAB7092 CLASSIFICATION #superfamily rat ribosomal protein L35a KEYWORDS protein biosynthesis; ribosome SUMMARY #length 87 #molecular-weight 9736 #checksum 2131 SEQUENCE /// ENTRY F71194 #type complete TITLE probable ribosomal protein L35 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 21-Jul-2000 ACCESSIONS F71194 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession F71194 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-87 ##label KAW !'##cross-references GB:AP000007; NID:g3236134; PIDN:BAA30949.1; !1PID:g3258266 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PHS052 CLASSIFICATION #superfamily rat ribosomal protein L35a KEYWORDS protein biosynthesis; ribosome SUMMARY #length 87 #molecular-weight 9750 #checksum 2615 SEQUENCE /// ENTRY S50922 #type complete TITLE ribosomal protein L36.e.A, cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YM9646.06; protein YMR194w; ribosomal protein YL39 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S11263; S50922 REFERENCE S11249 !$#authors Otaka, E.; Higo, K.I.; Itoh, T. !$#journal Mol. Gen. Genet. (1984) 195:544-546 !$#title Yeast ribosomal proteins. VIII. Isolation of two proteins !1and sequence characterization of twenty-four proteins from !1cytoplasmic ribosomes. !$#accession S11263 !'##molecule_type protein !'##residues 'A',3-18,'Q',20-34,'D',36-41 ##label OTA REFERENCE S50917 !$#authors Pearson, D.; Bowman, S. !$#submission submitted to the EMBL Data Library, January 1995 !$#accession S50922 !'##molecule_type DNA !'##residues 1-100 ##label PEA !'##cross-references EMBL:Z47815; NID:g642280; PIDN:CAA87815.1; !1PID:g642286; GSPDB:GN00013; MIPS:YMR194w GENETICS !$#gene SGD:RPL36A; MIPS:YMR194w !'##cross-references SGD:S0004807 !$#map_position 13R !$#introns 6/1 CLASSIFICATION #superfamily rat ribosomal protein L36 KEYWORDS cytosol; protein biosynthesis; ribosome SUMMARY #length 100 #molecular-weight 11124 #checksum 9063 SEQUENCE /// ENTRY JN0483 #type complete TITLE ribosomal protein L36, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 21-Jul-2000 ACCESSIONS JN0483; PN0454 REFERENCE JN0483 !$#authors Chan, Y.L.; Paz, V.; Olvera, J.; Wool, I.G. !$#journal Biochem. Biophys. Res. Commun. (1993) 192:849-853 !$#title The primary structure of rat ribosomal protein L36. !$#cross-references MUID:93249466; PMID:8484789 !$#accession JN0483 !'##molecule_type mRNA !'##residues 1-105 ##label CHA !'##cross-references GB:X68284; NID:g312344; PIDN:CAA48345.1; !1PID:g312345 !$#accession PN0454 !'##molecule_type protein !'##residues 2-40 ##label CH1 !'##note the protein is designated as ribosomal protein L36 GENETICS !$#gene L36 CLASSIFICATION #superfamily rat ribosomal protein L36 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-105 #product ribosomal protein L36 #status predicted !8#label RBL SUMMARY #length 105 #molecular-weight 12268 #checksum 3788 SEQUENCE /// ENTRY JC2368 #type complete TITLE ribosomal protein L13, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 21-Jul-2000 ACCESSIONS JC2368; PC2232; JC2235; PC2157 REFERENCE JC2235 !$#authors Olvera, J.; Wool, I.G. !$#journal Biochem. Biophys. Res. Commun. (1994) 201:102-107 !$#title The primary structure of rat ribosomal protein L13. !$#cross-references MUID:94256964; PMID:8198561 !$#accession JC2368 !'##molecule_type mRNA !'##residues 1-211 ##label OLV1 !'##cross-references EMBL:X78327; NID:g510551; PIDN:CAA55130.1; !1PID:g510552 !$#accession PC2232 !'##molecule_type protein !'##residues 2-14;26-60;100-180 ##label OLV2 !'##experimental_source clone pL13-2,3 !'##note the protein is designated as ribosomal protein L13 CLASSIFICATION #superfamily rat ribosomal protein L13 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-211 #product ribosomal protein L13 #status predicted !8#label MAT SUMMARY #length 211 #molecular-weight 24240 #checksum 159 SEQUENCE /// ENTRY S50398 #type complete TITLE ribosomal protein L13.e.B, cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YM9375.11c; protein YMR142c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S50398 REFERENCE S50388 !$#authors Badcock, K.; Churcher, C. !$#submission submitted to the EMBL Data Library, December 1994 !$#accession S50398 !'##molecule_type DNA !'##residues 1-199 ##label BAD !'##cross-references EMBL:Z47071; NID:g606429; PIDN:CAA87356.1; !1PID:g606440; GSPDB:GN00013; MIPS:YMR142c GENETICS !$#gene SGD:RPL13B; MIPS:YMR142c !'##cross-references SGD:S0004750 !$#map_position 13R !$#introns 2/1 CLASSIFICATION #superfamily rat ribosomal protein L13 KEYWORDS cytosol; protein biosynthesis; ribosome SUMMARY #length 199 #molecular-weight 22525 #checksum 3475 SEQUENCE /// ENTRY JC2369 #type complete TITLE ribosomal protein L15, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 19-Jan-2001 ACCESSIONS JC2369; PC2233; JC2236; PC2158 REFERENCE JC2236 !$#authors Chan, Y.L.; Olvera, J.; Wool, I.G. !$#journal Biochem. Biophys. Res. Commun. (1994) 201:108-114 !$#title The primary structure of rat ribosomal protein L15. !$#cross-references MUID:94256965; PMID:8198562 !$#accession JC2369 !'##molecule_type mRNA !'##residues 1-204 ##label CHA !'##cross-references EMBL:X78167; NID:g515864; PIDN:CAA55026.1; !1PID:g515865 !$#accession PC2233 !'##molecule_type protein !'##residues 2-26;137-173 ##label CH2 !'##experimental_source liver !'##note the protein is designated as ribosomal protein L15 GENETICS !$#gene L15 CLASSIFICATION #superfamily rat ribosomal protein L15 KEYWORDS nucleotide binding; P-loop; phosphoprotein; protein !1biosynthesis; ribosome FEATURE !$2-204 #product ribosomal protein L15 #status experimental !8#label MAT\ !$126-131 #region amyloid hexapeptide TYKFFE motif\ !$163-171 #region nucleotide-binding motif A (P-loop)\ !$126 #binding_site phosphate (Thr) (covalent) (by protein !8kinase C) #status predicted SUMMARY #length 204 #molecular-weight 24146 #checksum 4284 SEQUENCE /// ENTRY S58649 #type complete TITLE ribosomal protein L22.e.B, cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YFL034c-a ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 22-Oct-1999 ACCESSIONS S58649 REFERENCE S56186 !$#authors Murakami, Y.; Naitou, M.; Hagiwara, H.; Shibata, T.; Ozawa, !1M.; Sasanuma, S.I.; Sasanuma, M.; Tsuchiya, Y.; Soeda, E.; !1Yokoyama, K.; Yamazaki, M.; Tashiro, H.; Eki, T. !$#submission submitted to the EMBL Data Library, May 1995 !$#description Analysis of the nucleotide sequence of chromosome VI from !1Saccaromyces cerevisiae. !$#accession S58649 !'##molecule_type DNA !'##residues 1-122 ##label MUR !'##cross-references EMBL:D50617; GSPDB:GN00006; MIPS:YFL034c-a GENETICS !$#gene MIPS:YFL034c-a !$#map_position 6L !$#introns 4/3 CLASSIFICATION #superfamily rat ribosomal protein L22 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 122 #molecular-weight 13826 #checksum 9158 SEQUENCE /// ENTRY S52084 #type complete TITLE ribosomal protein L22, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 21-Jul-2000 ACCESSIONS S52084 REFERENCE S52084 !$#authors Chan, Y.L.; Wool, I.G. !$#journal Biochim. Biophys. Acta (1995) 1260:113-115 !$#title The primary structure of rat ribosomal protein L22. !$#cross-references MUID:95092785; PMID:7999786 !$#accession S52084 !'##molecule_type mRNA !'##residues 1-128 ##label CHA !'##cross-references EMBL:X78444; NID:g710294; PIDN:CAA55204.1; !1PID:g710295 !'##note the protein is designated as ribosomal protein L22 according to !1comigration analysis after in vitro translation CLASSIFICATION #superfamily rat ribosomal protein L22 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 128 #molecular-weight 14789 #checksum 592 SEQUENCE /// ENTRY JC5250 #type complete TITLE ribosomal protein S3a, cytosolic [validated] - rat ALTERNATE_NAMES v-fos transformation effector fte-1 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 21-Jul-2000 ACCESSIONS JC5250; PC4306; A41974; S45052 REFERENCE JC5250 !$#authors Chan, Y.L.; Olvera, J.; Paz, V.; Wool, I.G. !$#journal Biochem. Biophys. Res. Commun. (1996) 228:141-147 !$#title The primary structures of rat ribosomal proteins S3a (The !1V-Fos transformation effector) and S3b. !$#cross-references MUID:97069666; PMID:8912649 !$#accession JC5250 !'##molecule_type mRNA !'##residues 1-264 ##label CHA1 !'##cross-references EMBL:X75161; NID:g495139; PIDN:CAA53004.1; !1PID:g495140 !$#accession PC4306 !'##molecule_type protein !'##residues 24-49 ##label CHA2 !'##note the protein is designated as ribosomal protein S3a REFERENCE A41974 !$#authors Kho, C.J.; Zarbl, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:2200-2204 !$#title Fte-1, a v-fos transformation effector gene, encodes the !1mammalian homologue of a yeast gene involved in protein !1import into mitochondria. !$#cross-references MUID:92196085; PMID:1549582 !$#accession A41974 !'##status preliminary !'##molecule_type mRNA !'##residues 1-31,'D',33-264 ##label KHO !'##cross-references EMBL:X75161; NID:g495139; PIDN:CAA53004.1; !1PID:g495140 !'##note sequence extracted from NCBI backbone (NCBIP:88068) COMMENT This protein is involved in the initiation of protein !1synthesis, and the regulation of growth and cell cycle. CLASSIFICATION #superfamily rat ribosomal protein S3a FEATURE !$2-264 #product ribosomal protein S3a #status predicted !8#label MAT SUMMARY #length 264 #molecular-weight 29959 #checksum 6830 SEQUENCE /// ENTRY S14051 #type complete TITLE ribosomal protein S0.e.B, cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES lysine-rich protein KRP-Y2; protein YML063w; ribosomal protein PLC2; ribosomal protein rp10; ribosomal protein YS3a.e ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 12-Nov-1999 ACCESSIONS S14051; S33725; S48335; S45515; S70225 REFERENCE S14051 !$#authors Garrett, J.M.; Singh, K.K.; Vonder Haar, R.A.; Emr, S.D. !$#journal Mol. Gen. Genet. (1991) 225:483-491 !$#title Mitochondrial protein import: isolation and characterization !1of the Saccharomyces cerevisiae MFT1 gene. !$#cross-references MUID:91203825; PMID:2017143 !$#accession S14051 !'##molecule_type DNA !'##residues 1-255 ##label GAR !'##cross-references EMBL:X55360; NID:g3952; PIDN:CAA39044.1; PID:g3953 !'##note the authors translated the codon GAC for residue 203 as B REFERENCE S21121 !$#authors Ito, M.; Yasui, A.; Komamine, A. !$#journal FEBS Lett. (1992) 301:29-33 !$#title A gene family homologous to the S-phase specific gene in !1higher plants is essential for cell proliferation in !1Saccharomyces cerevisiae. !$#cross-references MUID:93083617; PMID:1451783 !$#accession S33725 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type DNA !'##residues 1-255 ##label ITO REFERENCE S48326 !$#authors Bowman, S.; Churcher, C. !$#submission submitted to the EMBL Data Library, August 1994 !$#accession S48335 !'##molecule_type DNA !'##residues 1-255 ##label BOW !'##cross-references EMBL:Z38114; NID:g558402; PIDN:CAA86258.1; !1PID:g558412; GSPDB:GN00013; MIPS:YML063w REFERENCE S45500 !$#authors Takahura, H.; Tsunasawa, S.; Miyagi, M.; Warner, J.R. !$#journal J. Biol. Chem. (1992) 267:5442-5445 !$#title NH2-terminal acetylation of ribosomal proteins of !1Saccharomyces cerevisiae. !$#cross-references MUID:92184799; PMID:1544921 !$#accession S45515 !'##molecule_type protein !'##residues 2-21 ##label TAK REFERENCE S43541 !$#authors Auclair, D.; Lang, B.F.; Forest, P.; Desgroseillers, L. !$#journal Eur. J. Biochem. (1994) 220:997-1003 !$#title Analysis of genes encoding highly conserved lysine-rich !1proteins in Aplysia californica and Saccharomyces !1cerevisiae. !$#cross-references MUID:94192693; PMID:8143753 !$#accession S70225 !'##molecule_type DNA !'##residues 1-255 ##label AUC GENETICS !$#gene SGD:RP10B; PLC2; MFT1; MIPS:YML063w !'##cross-references SGD:S0004528; MIPS:YML063w !$#map_position 13L CLASSIFICATION #superfamily rat ribosomal protein S3a KEYWORDS protein biosynthesis; ribosome SUMMARY #length 255 #molecular-weight 28812 #checksum 4712 SEQUENCE /// ENTRY S42405 #type complete TITLE ribosomal protein RS.40K, cytosolic [validated] - rat ALTERNATE_NAMES 40S ribosomal subunit 40K protein; laminin receptor ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 18-Aug-2000 ACCESSIONS S42405; S65348; S65347; I53639 REFERENCE S42405 !$#authors Tohgo, A.; Takasawa, S.; Munakata, H.; Yonekura, H.; !1Hayashi, N.; Okamoto, H. !$#journal FEBS Lett. (1994) 340:133-138 !$#title Structural determination and characterization of a 40 kDa !1protein isolated from rat 40 S ribosomal subunit. !$#cross-references MUID:94164296; PMID:8119397 !$#accession S42405 !'##molecule_type mRNA !'##residues 1-295 ##label TOH !'##cross-references EMBL:D25224; NID:g466438 !'##note in the authors' translation 62-Ala is shown after residue 75 !1and, consequently, residues 63-75 are displaced one codon to !1the left !$#accession S65348 !'##molecule_type protein !'##residues 18-85;90-119;167-173;221-224 ##label TOF REFERENCE S65347 !$#authors Tohgo, A. !$#submission submitted to the EMBL Data Library, November 1993 !$#accession S65347 !'##molecule_type mRNA !'##residues 1-61,'A',62-75,77-87,'L',89-295 ##label TOW !'##cross-references EMBL:D25224; NID:g466438; PIDN:BAA04953.1; !1PID:g466439 REFERENCE I53639 !$#authors Rao, M.; Manishen, W.J.; Maheshwari, Y.; Sykes, D.E.; !1Siyanova, E.Y.; Tyner, A.L.; Weiser, M.M. !$#journal Gastroenterology (1994) 107:764-772 !$#title Laminin Receptor Expression in Rat intestine and liver !1during development and differentiation. !$#cross-references MUID:94357375; PMID:8076763 !$#accession I53639 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 199-295 ##label RAO !'##cross-references EMBL:U04942; NID:g440796; PIDN:AAB60453.1; !1PID:g440797 CLASSIFICATION #superfamily yeast ribosomal protein S1.e KEYWORDS blocked amino end; protein biosynthesis; ribosome SUMMARY #length 295 #molecular-weight 32824 #checksum 1457 SEQUENCE /// ENTRY S42143 #type complete TITLE ribosomal protein S1.e.A, cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES nucleic acid-binding protein NAB1; protein G7816; protein YGR214w ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 18-Aug-2000 ACCESSIONS S42143; S64537 REFERENCE S42143 !$#authors Miles, J.; Formosa, T.G. !$#submission submitted to the EMBL Data Library, March 1992 !$#description Yeast nucleic acid binding proteins. !$#accession S42143 !'##molecule_type DNA !'##residues 1-252 ##label MIL !'##cross-references EMBL:M88277; NID:g172025; PIDN:AAB05643.1; !1PID:g172026 REFERENCE S64071 !$#authors Rieger, M.; Mueller-Auer, S.; Brueckner, M.; Schaefer, M. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64537 !'##molecule_type DNA !'##residues 1-252 ##label RIE !'##cross-references EMBL:Z72999; NID:g1323384; PIDN:CAA97241.1; !1PID:g1323385; GSPDB:GN00007; MIPS:YGR214w !'##experimental_source strain S288C GENETICS !$#gene SGD:YST1; NAB1; MIPS:YGR214w !'##cross-references SGD:S0003446; MIPS:YGR214w !$#map_position 7R !$#introns 30/3 CLASSIFICATION #superfamily yeast ribosomal protein S1.e KEYWORDS DNA binding; protein biosynthesis; ribosome SUMMARY #length 252 #molecular-weight 28024 #checksum 4747 SEQUENCE /// ENTRY G41715 #type complete TITLE ribosomal protein S2 [validated] - Haloarcula marismortui ALTERNATE_NAMES ribosomal protein HS2 ORGANISM #formal_name Haloarcula marismortui DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 18-Aug-2000 ACCESSIONS G41715; S49023; S63964 REFERENCE A41715 !$#authors Kroemer, W.J.; Arndt, E. !$#journal J. Biol. Chem. (1991) 266:24573-24579 !$#title Halobacterial S9 operon. Three ribosomal protein genes are !1cotranscribed with genes encoding a tRNA(leu), the enolase, !1and a putative membrane protein in the archaebacterium !1Haloarcula (halobacterium) marismortui. !$#cross-references MUID:92105119; PMID:1840597 !$#accession G41715 !'##status preliminary !'##molecule_type DNA !'##residues 1-266 ##label KRO !'##cross-references GB:M76567; NID:g148775; PIDN:AAA73102.1; !1PID:g148782 REFERENCE S49023 !$#authors Engemann, S.; Herfurth, E.; Briesemeister, U.; Grelle, G.; !1Wittmann-Liebold, B. !$#submission submitted to the Protein Sequence Database, November 1994 !$#description Cartography of ribosomal proteins of the 30S subunit from !1the halophilic Haloarcula marismortui. !$#accession S49023 !'##status preliminary !'##molecule_type protein !'##residues 1-266 ##label ENG REFERENCE S63964 !$#authors Engemann, S.; Noelle, R.; Herfurth, E.; Briesemeister, U.; !1Grelle, G.; Wittmann-Liebold, B. !$#journal Eur. J. Biochem. (1995) 234:24-31 !$#title Cartography of ribosomal proteins of the 30S subunit from !1the halophilic Haloarcula marismortui and complete sequence !1analysis of protein HS26. !$#cross-references MUID:96096717; PMID:8529646 !$#accession S63964 !'##status preliminary !'##molecule_type protein !'##residues 83-96;129-138;179-184;249-259 ##label EN2 CLASSIFICATION #superfamily yeast ribosomal protein S1.e KEYWORDS blocked amino end; protein biosynthesis; ribosome SUMMARY #length 266 #molecular-weight 29287 #checksum 3078 SEQUENCE /// ENTRY A42115 #type complete TITLE ribosomal protein S2, mitochondrial - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YHL004w; ribosomal protein MRP4 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 23-Mar-2001 ACCESSIONS A42115; S46799; S27429 REFERENCE A42115 !$#authors Davis, S.C.; Tzagoloff, A.; Ellis, S.R. !$#journal J. Biol. Chem. (1992) 267:5508-5514 !$#title Characterization of a yeast mitochondrial ribosomal protein !1structurally related to the mammalian 68-kDa high affinity !1laminin receptor. !$#cross-references MUID:92184810; PMID:1531984 !$#accession A42115 !'##molecule_type DNA !'##residues 1-394 ##label DAV !'##cross-references EMBL:M82841; NID:g171981; PIDN:AAA34793.1; !1PID:g171982 !'##note sequence extracted from NCBI backbone (NCBIN:87499, !1NCBIP:87502) REFERENCE S46797 !$#authors Favello, T. !$#submission submitted to the EMBL Data Library, June 1994 !$#description The sequence of S. cerevisiae cosmid 9780. !$#accession S46799 !'##molecule_type DNA !'##residues 1-394 ##label FAV !'##cross-references EMBL:U10555; NID:g500813; PIDN:AAB68428.1; !1PID:g500819; GSPDB:GN00008; MIPS:YHL004w GENETICS !$#gene SGD:MRP4; MIPS:YHL004w !'##cross-references SGD:S0000996; MIPS:YHL004w !$#map_position 8L CLASSIFICATION #superfamily yeast ribosomal protein S2 KEYWORDS mitochondrion; protein biosynthesis; ribosome SUMMARY #length 394 #molecular-weight 44151 #checksum 1152 SEQUENCE /// ENTRY S67074 #type complete TITLE ribosomal protein S30.e, cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein O4725; protein YLR287c-a; protein YOR182c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S67074; S70775; S70776; S70774 REFERENCE S66685 !$#authors Hughes, B.; Pohl, T.M. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67074 !'##molecule_type DNA !'##residues 1-63 ##label HUG !'##cross-references EMBL:Z75090; GSPDB:GN00015; MIPS:YOR182c; !1NID:g1420438; PIDN:CAA99391.1; PID:g1420439 !'##experimental_source strain S288C !'##genetics YS30B REFERENCE S70774 !$#authors Baker, R.T.; Williamson, N.A.; Wettenhall, R.E.H. !$#journal J. Biol. Chem. (1996) 271:13549-13555 !$#title The yeast homolog of mammalian ribosomal protein S30 is !1expressed from a duplicated gene without a ubiquitin-like !1protein fusion sequence. !$#cross-references MUID:96278780; PMID:8662789 !$#accession S70775 !'##molecule_type DNA !'##residues 1-63 ##label BAK !'##cross-references EMBL:U48700; NID:g1256752; PIDN:AAC49317.1; !1PID:g1256753 !'##genetics YS30A !$#accession S70776 !'##molecule_type mRNA !'##residues 1-63 ##label BAW !'##cross-references EMBL:U48699; NID:g1256750; PIDN:AAC49316.1; !1PID:g1256751 !'##genetics YS30A !$#accession S70774 !'##molecule_type protein !'##residues 2-63 ##label BA3 GENETICS YS30B !$#gene SGD:RPS30B; MIPS:YOR182c !'##cross-references MIPS:YOR182c; SGD:S0005708 !$#map_position 15R !$#introns 1/3 GENETICS YS30A !$#gene SGD:RPS30A; MIPS:YLR287c-a !'##cross-references MIPS:YLR287c-a; SGD:S0004278 !$#map_position 12R !$#introns 1/3 CLASSIFICATION #superfamily yeast ribosomal protein S30.e KEYWORDS cytosol; protein biosynthesis; ribosome FEATURE !$2-63 #product ribosomal protein S30.e, cytosolic #status !8experimental #label MAT SUMMARY #length 63 #molecular-weight 7118 #checksum 1714 SEQUENCE /// ENTRY A47416 #type complete TITLE ubiquitin-like protein / ribosomal protein S30, cytosolic [validated] - rat CONTAINS ribosomal protein S30; ubiquitin-like protein ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 21-Jul-2000 ACCESSIONS A47416; B47416; S18101 REFERENCE A47416 !$#authors Olvera, J.; Wool, I.G. !$#journal J. Biol. Chem. (1993) 268:17967-17974 !$#title The carboxyl extension of a ubiquitin-like protein is rat !1ribosomal protein S30. !$#cross-references MUID:93352612; PMID:8394356 !$#accession A47416 !'##molecule_type mRNA !'##residues 1-133 ##label OLV !'##cross-references EMBL:X62671; NID:g407165; PIDN:CAA44545.1; !1PID:g57566 !$#accession B47416 !'##molecule_type protein !'##residues 75-92 ##label OL2 !'##note the proteins are designated as ubiquitin-like protein and !1ribosomal protein S30 CLASSIFICATION #superfamily ubiquitin-like protein / rat ribosomal protein !1S30; ubiquitin homology KEYWORDS protein biosynthesis; ribosome FEATURE !$1-74 #product ubiquitin-like protein #status predicted !8#label UBI\ !$1-74 #domain ubiquitin homology #label UBH\ !$75-133 #product ribosomal protein S30 #status experimental !8#label RIB SUMMARY #length 133 #molecular-weight 14372 #checksum 5361 SEQUENCE /// ENTRY R5EC32 #type complete TITLE ribosomal protein L32 [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 24-Apr-1984 #sequence_revision 30-Jun-1991 #text_change 01-Mar-2002 ACCESSIONS JV0048; A02832; A30419; F64852 REFERENCE JV0048 !$#authors Tanaka, Y.; Tsujimura, A.; Fujita, N.; Isono, S.; Isono, K. !$#journal J. Bacteriol. (1989) 171:5707-5712 !$#title Cloning and analysis of an Escherichia coli operon !1containing the rpmF gene for ribosomal protein L32 and the !1gene for a 30-Kilodalton protein. !$#cross-references MUID:90008815; PMID:2477362 !$#accession JV0048 !'##molecule_type DNA !'##residues 1-57 ##label TAN !'##cross-references GB:M29698; NID:g147710; PIDN:AAA24575.1; !1PID:g147712 !'##experimental_source strain K-12 REFERENCE A02832 !$#authors Wittmann-Liebold, B.; Greuer, B.; Pannenbecker, R. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1975) 356:1977-1979 !$#title The primary structure of protein L32 from the 50S subunit of !1Escherichia coli ribosomes. !$#cross-references MUID:76119562; PMID:765258 !$#accession A02832 !'##molecule_type protein !'##residues 2-57 ##label WIT !'##experimental_source strain K REFERENCE A30419 !$#authors Vinokurov, L.M.; Alakhov, Y.B.; Golov, E.A.; Ovchinnikov, !1Y.A. !$#journal Bioorg. Khim. (1976) 2:1013-1017 !$#accession A30419 !'##molecule_type protein !'##residues 2-57 ##label VIN !'##experimental_source strain MRE-600 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64852 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-57 ##label BLAT !'##cross-references GB:AE000209; GB:U00096; NID:g1787322; !1PIDN:AAC74173.1; PID:g1787330; UWGP:b1089 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note mass spectrographic analysis of post-translational !1modifications; any acid labile modifications may have been !1missed GENETICS !$#gene rpmF !$#map_position 24 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX large subunit ribosomal proteins: L1 (PIR:R5EC1), L3 !1(PIR:R5EC3), L2 (PIR:R5EC2), L4 (PIR:R5EC4), L5 (PIR:R5EC5), !1L6 (PIR:R5EC6), L7/L12 (PIR:R5EC7), L9 (PIR:R5EC9), L10 !1(PIR:R5EC10), L11 (PIR:R5EC11), L13 (PIR:R5EC13), L14 !1(PIR:R5EC14), L15 (PIR:R5EC15), L16 (PIR:R5EC16), L17 !1(PIR:R5EC17), L18 (PIR:R5EC18), L19 (PIR:R5EC19) FUNCTION !$#pathway protein biosynthesis CLASSIFICATION #superfamily Escherichia coli ribosomal protein L32 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-57 #product ribosomal protein L32 #status experimental !8#label MAT SUMMARY #length 57 #molecular-weight 6446 #checksum 6772 SEQUENCE /// ENTRY G64051 #type complete TITLE ribosomal protein L32 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 23-Oct-1998 #sequence_revision 23-Oct-1998 #text_change 28-Jul-2000 ACCESSIONS G64051 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession G64051 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-56 ##label TIGR !'##cross-references GB:U32701; GB:L42023; NID:g3212182; !1PIDN:AAC21827.1; PID:g1573115; TIGR:HI0158 GENETICS !$#gene rpmF; rpL32 FUNCTION !$#pathway protein biosynthesis CLASSIFICATION #superfamily Escherichia coli ribosomal protein L32 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-56 #product ribosomal protein L32 #status predicted !8#label MAT SUMMARY #length 56 #molecular-weight 6392 #checksum 2916 SEQUENCE /// ENTRY A41608 #type complete TITLE ribosomal protein L32 - Rhodobacter capsulatus ORGANISM #formal_name Rhodobacter capsulatus DATE 23-Oct-1998 #sequence_revision 23-Oct-1998 #text_change 22-Jun-1999 ACCESSIONS A41608 REFERENCE A41608 !$#authors Toussaint, B.; Bosc, C.; Richaud, P.; Colbeau, A.; Vignais, !1P.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:10749-10753 !$#title A mutation in a Rhodobacter capsulatus gene encoding an !1integration host factor-like protein impairs in vivo !1hydrogenase expression. !$#cross-references MUID:92073365; PMID:1961742 !$#accession A41608 !'##status preliminary !'##molecule_type DNA !'##residues 1-68 ##label TOU !'##cross-references GB:M84030; GB:M62764; NID:g151940; PIDN:AAA26125.1; !1PID:g151941 FUNCTION !$#pathway protein biosynthesis CLASSIFICATION #superfamily Escherichia coli ribosomal protein L32 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-68 #product ribosomal protein L32 #status predicted !8#label MAT SUMMARY #length 68 #molecular-weight 7409 #checksum 8267 SEQUENCE /// ENTRY B64240 #type complete TITLE ribosomal protein L32 - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 23-Oct-1998 #sequence_revision 23-Oct-1998 #text_change 07-Dec-1999 ACCESSIONS B64240 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession B64240 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-57 ##label TIGR !'##cross-references GB:U39720; GB:L43967; NID:g1046063; PID:g1046071; !1TIGR:MG363 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 FUNCTION !$#pathway protein biosynthesis CLASSIFICATION #superfamily Escherichia coli ribosomal protein L32 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-57 #product ribosomal protein L32 #status predicted !8#label MAT SUMMARY #length 57 #molecular-weight 6623 #checksum 5830 SEQUENCE /// ENTRY S73628 #type complete TITLE ribosomal protein L32 - Mycoplasma pneumoniae (strain ATCC 29342) ALTERNATE_NAMES hypothetical protein G12_orf57 ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 23-Oct-1998 #sequence_revision 23-Oct-1998 #text_change 10-Dec-1999 ACCESSIONS S73628 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73628 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-57 ##label HIM !'##cross-references EMBL:AE000028; GB:U00089; NID:g1673972; !1PIDN:AAB95950.1; PID:g1673974 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#gene rpmF !$#genetic_code SGC3 FUNCTION !$#pathway protein biosynthesis CLASSIFICATION #superfamily Escherichia coli ribosomal protein L32 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-57 #product ribosomal protein L32 #status predicted !8#label MAT SUMMARY #length 57 #molecular-weight 6623 #checksum 5670 SEQUENCE /// ENTRY H69697 #type complete TITLE ribosomal protein L32 - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 23-Oct-1998 #sequence_revision 23-Oct-1998 #text_change 16-Jun-2000 ACCESSIONS H69697 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69697 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-59 ##label KUN !'##cross-references GB:Z99111; GB:AL009126; NID:g2633699; !1PIDN:CAB13381.1; PID:g2633879 !'##experimental_source strain 168 GENETICS !$#gene rpmF FUNCTION !$#pathway protein biosynthesis CLASSIFICATION #superfamily Escherichia coli ribosomal protein L32 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-59 #product ribosomal protein L32 #status predicted !8#label MAT SUMMARY #length 59 #molecular-weight 6729 #checksum 5918 SEQUENCE /// ENTRY R5BS37 #type complete TITLE ribosomal protein L32 - Bacillus stearothermophilus ALTERNATE_NAMES ribosomal protein BL37; ribosomal protein I ORGANISM #formal_name Bacillus stearothermophilus DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 23-Oct-1998 ACCESSIONS S07236 REFERENCE S07236 !$#authors Tanaka, I.; Kimura, M.; Kimura, J.; Dijk, J. !$#journal FEBS Lett. (1984) 166:343-346 !$#title The amino acid sequence of two small ribosomal proteins from !1Bacillus stearothermophilus. !$#cross-references MUID:84108949; PMID:6420194 !$#accession S07236 !'##molecule_type protein !'##residues 1-56 ##label TAN FUNCTION !$#pathway protein biosynthesis CLASSIFICATION #superfamily Escherichia coli ribosomal protein L32 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-56 #product ribosomal protein L32 #status predicted !8#label MAT SUMMARY #length 56 #molecular-weight 6514 #checksum 2367 SEQUENCE /// ENTRY H70394 #type complete TITLE ribosomal protein L32 - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 23-Oct-1998 #sequence_revision 23-Oct-1998 #text_change 22-Jun-1999 ACCESSIONS H70394 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession H70394 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-63 ##label AQF !'##cross-references GB:AE000723; NID:g2983569; PIDN:AAC07156.1; !1PID:g2983584; GB:AE000657 !'##experimental_source strain VF5 GENETICS !$#gene rpmF FUNCTION !$#pathway protein biosynthesis CLASSIFICATION #superfamily Escherichia coli ribosomal protein L32 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-63 #product ribosomal protein L32 #status predicted !8#label MAT SUMMARY #length 63 #molecular-weight 7411 #checksum 8527 SEQUENCE /// ENTRY F70187 #type complete TITLE ribosomal protein L32 - Lyme disease spirochete ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 23-Oct-1998 #sequence_revision 23-Oct-1998 #text_change 22-Jun-1999 ACCESSIONS F70187 REFERENCE A70100 !$#authors Fraser, C.M.; Casjens, S.; Huang, W.M.; Sutton, G.G.; !1Clayton, R.; Lathigra, R.; White, O.; Ketchum, K.A.; Dodson, !1R.; Hickey, E.K.; Gwinn, M.; Dougherty, B.; Tomb, J.F.; !1Fleischmann, R.D.; Richardson, D.; Peterson, J.; Kerlavage, !1A.R.; Quackenbush, J.; Salzberg, S.; Hanson, M.; Vugt, R.V.; !1Palmer, N.; Adams, M.D.; Gocayne, J.; Weidman, J.; !1Utterback, T.; Watthey, L.; McDonald, L.; Artiach, P.; !1Bowman, C.; Garland, S.; Fujii, C.; Cotton, M.D.; Horst, K.; !1Roberts, K.; Hatch, B.; Smith, H.O.; Venter, J.C. !$#journal Nature (1997) 390:580-586 !$#title Genomic sequence of a Lyme disease spirochaete, Borrelia !1burgdorferi. !$#cross-references MUID:98065943; PMID:9403685 !$#accession F70187 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-60 ##label KLE !'##cross-references GB:AE001170; GB:AE000783; NID:g2688623; !1PIDN:AAC67042.1; PID:g2688627; TIGR:BB0703 !'##experimental_source strain B31 FUNCTION !$#pathway protein biosynthesis CLASSIFICATION #superfamily Escherichia coli ribosomal protein L32 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-60 #product ribosomal protein L32 #status predicted !8#label MAT SUMMARY #length 60 #molecular-weight 7076 #checksum 8206 SEQUENCE /// ENTRY R5HS32 #type complete TITLE ribosomal protein HL32 [validated] - Haloarcula marismortui ORGANISM #formal_name Haloarcula marismortui DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 04-Feb-2000 ACCESSIONS S06848 REFERENCE S06844 !$#authors Hatakeyama, T.; Kaufmann, F.; Schroeter, B.; Hatakeyama, T. !$#journal Eur. J. Biochem. (1989) 185:685-693 !$#title Primary structures of five ribosomal proteins from the !1archaebacterium Halobacterium marismortui and their !1structural relationships to eubacterial and eukaryotic !1ribosomal proteins. !$#cross-references MUID:90076190; PMID:2591382 !$#accession S06848 !'##molecule_type protein !'##residues 1-55 ##label HAT !'##note the source is designated as Halobacterium marismortui !'##note the protein is designated as ribosomal protein L32 CLASSIFICATION #superfamily Haloarcula ribosomal protein HL32 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 55 #molecular-weight 6257 #checksum 7230 SEQUENCE /// ENTRY R5BY32 #type complete TITLE ribosomal protein YmL32 precursor, mitochondrial - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YCR003w; protein YCR041 ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 21-Jul-2000 ACCESSIONS S22265; S19452; S40922; S17271; S20182 REFERENCE S22265 !$#authors Biteau, N.; Fremaux, C.; Hebrard, S.; Menara, A.; Aigle, M.; !1Crouzet, M. !$#journal Yeast (1992) 8:61-70 !$#title The complete sequence of a 10.8kb fragment to the right of !1the chromosome III centromere of Saccharomyces cerevisiae. !$#cross-references MUID:92254505; PMID:1580102 !$#accession S22265 !'##status translation not shown !'##molecule_type DNA !'##residues 1-183 ##label BIT !'##cross-references EMBL:X59720; NID:g1907116; PIDN:CAA42340.1; !1PID:g1907146 REFERENCE S19452 !$#authors Aigle, M.; Biteau, N.; Crouzet, M. !$#submission submitted to the Protein Sequence Database, March 1992 !$#accession S19452 !'##molecule_type DNA !'##residues 1-183 ##label AIG !'##cross-references EMBL:X59720; NID:g1907116; PIDN:CAA42340.1; !1PID:g1907146; GSPDB:GN00003; MIPS:YCR003w REFERENCE S20186 !$#authors Steensma, H.Y.; van der Aart, Q.J.M. !$#journal Yeast (1991) 7:425-429 !$#title Sequence of the CDC10 region at chromosome III of !1Saccharomyces cerevisiae. !$#cross-references MUID:91335898; PMID:1872033 !$#accession S40922 !'##status translation not shown !'##molecule_type DNA !'##residues 1-183 ##label STE !'##cross-references EMBL:S48552; NID:g233477; PIDN:AAD13857.1; !1PID:g4261557 REFERENCE S17255 !$#authors Grohmann, L.; Graack, H.R.; Kruft, V.; Choli, T.; !1Goldschmidt-Reisin, S.; Kitakawa, M. !$#journal FEBS Lett. (1991) 284:51-56 !$#title Extended N-terminal sequencing of proteins of the large !1ribosomal subunit from yeast mitochondria. !$#cross-references MUID:91285106; PMID:2060626 !$#accession S17271 !'##molecule_type protein !'##residues 72-85,'X',87-95,'Q',97-98,'X',100-102,'XG',105,'D' ##label !1GRO GENETICS !$#gene SGD:MRPL32; MIPS:YCR003w !'##cross-references SGD:S0000596; MIPS:YCR003w !$#map_position 3R !$#genome nuclear CLASSIFICATION #superfamily ribosomal protein YmL32 KEYWORDS mitochondrion; protein biosynthesis; ribosome FEATURE !$1-71 #domain transit peptide (mitochondrion) #status !8experimental #label TNP\ !$72-183 #product ribosomal protein YmL32, mitochondrial !8#status experimental #label MAT SUMMARY #length 183 #molecular-weight 21437 #checksum 4457 SEQUENCE /// ENTRY R5RZ32 #type complete TITLE ribosomal protein L32 - rice chloroplast ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 22-Jun-1999 ACCESSIONS JQ0287; S05166 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0287 !'##molecule_type DNA !'##residues 1-63 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05166 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-63 ##label HIR !'##cross-references EMBL:X15901; NID:g11957; PIDN:CAA33951.1; !1PID:g12048 !'##experimental_source cv. Nihonbare !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1989 GENETICS !$#genome chloroplast CLASSIFICATION #superfamily rice chloroplast ribosomal protein L32 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 63 #molecular-weight 7316 #checksum 1421 SEQUENCE /// ENTRY R5VF32 #type complete TITLE ribosomal protein L32 - fava bean chloroplast ORGANISM #formal_name chloroplast Vicia faba #common_name fava bean DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 22-Jun-1999 ACCESSIONS S08495; S08444 REFERENCE S08494 !$#authors Herdenberger, F.; Weil, J.H.; Steinmetz, A. !$#journal Curr. Genet. (1988) 14:609-615 !$#title Organization and nucleotide sequence of the broad bean !1chloroplast genes trnL-UAG, ndhF and two unidentified open !1reading frames. !$#cross-references MUID:89208884; PMID:3242868 !$#accession S08495 !'##molecule_type DNA !'##residues 1-48 ##label HER !'##cross-references EMBL:X51471; NID:g12387; PIDN:CAA35833.1; !1PID:g12389 GENETICS !$#genome chloroplast CLASSIFICATION #superfamily rice chloroplast ribosomal protein L32 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 48 #molecular-weight 5407 #checksum 9911 SEQUENCE /// ENTRY R5NT32 #type complete TITLE ribosomal protein L32 - common tobacco chloroplast ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jun-2000 ACCESSIONS S27288; S12978 REFERENCE A38013 !$#authors Shinozaki, K.; Ohme, M.; Tanaka, M.; Wakasugi, T.; !1Hayashida, N.; Matsubayashi, T.; Zaita, N.; Chunwongse, J.; !1Obokata, J.; Yamaguchi-Shinozaki, K.; Ohto, C.; Torazawa, !1K.; Meng, B.Y.; Sugita, M.; Deno, H.; Kamogashira, T.; !1Yamada, K.; Kusuda, J.; Takaiwa, F.; Kato, A.; Tohdoh, N.; !1Shimada, H.; Sugiura, M. !$#journal EMBO J. (1986) 5:2043-2049 !$#title The complete nucleotide sequence of the tobacco chloroplast !1genome: its gene organization and expression. !$#accession S27288 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-55 ##label SHI !'##cross-references EMBL:Z00044; NID:g2924257; PIDN:CAA77431.1; !1PID:g2924278 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1986 REFERENCE S12978 !$#authors Yokoi, F.; Vassileva, A.; Hayashida, N.; Torazawa, K.; !1Wakasugi, T.; Sugiura, M. !$#journal FEBS Lett. (1990) 276:88-90 !$#title Chloroplast ribosomal protein L32 is encoded in the !1chloroplast genome. !$#cross-references MUID:91092444; PMID:2265719 !$#accession S12978 !'##molecule_type protein !'##residues 2-19 ##label YOK GENETICS !$#genome chloroplast CLASSIFICATION #superfamily rice chloroplast ribosomal protein L32 KEYWORDS chloroplast; protein biosynthesis; ribosome FEATURE !$2-55 #product ribosomal protein L32 #status experimental !8#label MAT SUMMARY #length 55 #molecular-weight 6316 #checksum 9024 SEQUENCE /// ENTRY R5EC33 #type complete TITLE ribosomal protein L33 [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 24-Apr-1984 #sequence_revision 03-Oct-1995 #text_change 01-Mar-2002 ACCESSIONS S42444; A02833; F65164 REFERENCE S42443 !$#authors Lee, J.S.; An, G.; Friesen, J.D.; Isono, K. !$#journal Mol. Gen. Genet. (1981) 184:218-223 !$#title Cloning and the nucleotide sequence of the genes for !1Escherichia coli ribosomal proteins L28 (rpmB) and L33 !1(rpmG). !$#cross-references MUID:82124622; PMID:7035835 !$#accession S42444 !'##molecule_type DNA !'##residues 1-55 ##label LEE !'##cross-references EMBL:J01677; NID:g147707; PIDN:AAA74100.1; !1PID:g147709 !'##note translation of initiator Met is not shown REFERENCE A02833 !$#authors Wittmann-Liebold, B.; Pannenbecker, R. !$#journal FEBS Lett. (1976) 68:115-118 !$#title Primary structure of protein L33 from the large subunit of !1the Escherichia coli ribosome. !$#cross-references MUID:77003693; PMID:786732 !$#accession A02833 !'##molecule_type protein !'##residues 2-47,'YI',50-55 ##label WIT !'##experimental_source strain K REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65164 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-55 ##label BLAT !'##cross-references GB:AE000441; GB:U00096; NID:g1790063; !1PIDN:AAC76660.1; PID:g1790067; UWGP:b3636 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note mass spectrographic analysis of post-translational !1modifications; any acid labile modifications may have been !1missed GENETICS !$#gene rpmG !$#map_position 82 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX large subunit ribosomal proteins: L1 (PIR:R5EC1), L3 !1(PIR:R5EC3), L2 (PIR:R5EC2), L4 (PIR:R5EC4), L5 (PIR:R5EC5), !1L6 (PIR:R5EC6), L7/L12 (PIR:R5EC7), L9 (PIR:R5EC9), L10 !1(PIR:R5EC10), L11 (PIR:R5EC11), L13 (PIR:R5EC13), L14 !1(PIR:R5EC14), L15 (PIR:R5EC15), L16 (PIR:R5EC16), L17 !1(PIR:R5EC17), L18 (PIR:R5EC18), L19 (PIR:R5EC19) FUNCTION !$#pathway protein biosynthesis CLASSIFICATION #superfamily Escherichia coli ribosomal protein L33 KEYWORDS methylated amino end; protein biosynthesis; ribosome FEATURE !$2-55 #product ribosomal protein L33 #status experimental !8#label MAT\ !$2 #modified_site methylated amino end (Ala) (in mature !8form) #status experimental SUMMARY #length 55 #molecular-weight 6372 #checksum 8058 SEQUENCE /// ENTRY R6SO33 #type complete TITLE ribosomal protein L33 - Lactococcus lactis ORGANISM #formal_name Lactococcus lactis DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 22-Jun-1999 ACCESSIONS S18088 REFERENCE S18087 !$#authors Koivula, T.; Hemilae, H. !$#submission submitted to the EMBL Data Library, October 1991 !$#description Nucleic acid sequence for ribosomal protein L33 of !1Lactococcus lactis. !$#accession S18088 !'##molecule_type DNA !'##residues 1-48 ##label KOI !'##cross-references EMBL:X62621; NID:g44066; PIDN:CAA44489.1; !1PID:g44068 GENETICS !$#gene rpmG CLASSIFICATION #superfamily Escherichia coli ribosomal protein L33 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 48 #molecular-weight 5507 #checksum 9566 SEQUENCE /// ENTRY R5LV33 #type complete TITLE ribosomal protein L33, chloroplast - liverwort (Marchantia polymorpha) chloroplast ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 22-Jun-1999 ACCESSIONS A02834; S01543 REFERENCE A00150 !$#authors Ohyama, K. !$#submission submitted to the EMBL Data Library, October 1986 !$#accession A02834 !'##molecule_type DNA !'##residues 1-65 ##label OHY REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features REFERENCE S01529 !$#authors Fukuzawa, H.; Kohchi, T.; Sano, T.; Shirai, H.; Umesono, K.; !1Inokuchi, H.; Ozeki, H.; Ohyama, K. !$#journal J. Mol. Biol. (1988) 203:333-351 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. III. Gene organization of the large !1single copy region from rbcL to trnI(CAU). !$#cross-references MUID:89068687; PMID:3199436 !$#accession S01543 !'##molecule_type DNA !'##residues 1-65 ##label FUK !'##cross-references GB:X04465; GB:Y00686; NID:g11640; PIDN:CAA28106.1; !1PID:g11694 GENETICS !$#gene rpl33 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein L33 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 65 #molecular-weight 7782 #checksum 8571 SEQUENCE /// ENTRY R5RZ33 #type complete TITLE ribosomal protein L33, chloroplast - rice chloroplast ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 22-Jun-1999 ACCESSIONS JQ0247; S05127 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0247 !'##molecule_type DNA !'##residues 1-66 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05127 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-66 ##label HIR !'##cross-references GB:X15901; NID:g11957; PIDN:CAA33969.1; PID:g12008 !'##experimental_source cv. Nihonbare !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1989 GENETICS !$#gene rpl33 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein L33 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 66 #molecular-weight 7643 #checksum 532 SEQUENCE /// ENTRY R5ZM33 #type complete TITLE ribosomal protein L33, chloroplast - maize chloroplast ORGANISM #formal_name chloroplast Zea mays #common_name maize DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 22-Jun-1999 ACCESSIONS S13611; S58572 REFERENCE S13611 !$#authors Wegloehner, W.; Subramanian, A.R. !$#journal FEBS Lett. (1991) 279:193-197 !$#title A heptapeptide repeat contributes to the unusual length of !1chloroplast ribosomal protein S18. Nucleotide sequence and !1map position of the rpl33-rps18 gene cluster in maize. !$#cross-references MUID:91160712; PMID:1840527 !$#accession S13611 !'##molecule_type DNA !'##residues 1-66 ##label WEG !'##cross-references EMBL:X56673; NID:g12448; PIDN:CAA39995.1; !1PID:g12449 REFERENCE S58531 !$#authors Maier, R.M.; Neckermann, K.; Igloi, G.L.; Koessel, H. !$#journal J. Mol. Biol. (1995) 251:614-628 !$#title Complete sequence of the maize chloroplast genome: gene !1content, hotspots of divergence and fine tuning of genetic !1information by transcript editing. !$#cross-references MUID:95395841; PMID:7666415 !$#accession S58572 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-66 ##label MAI !'##cross-references EMBL:X86563; NID:g902200; PIDN:CAA60306.1; !1PID:g902242 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1995 GENETICS !$#gene rpl33 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein L33 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 66 #molecular-weight 7748 #checksum 1373 SEQUENCE /// ENTRY R5NT33 #type complete TITLE ribosomal protein L33, chloroplast - common tobacco chloroplast ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 30-Jan-1998 ACCESSIONS A02835 REFERENCE A00149 !$#authors Sugiura, M. !$#submission submitted to the EMBL Data Library, August 1986 !$#accession A02835 !'##molecule_type DNA !'##residues 1-66 ##label SUG !'##experimental_source cv. Bright Yellow 4 REFERENCE A38013 !$#authors Shinozaki, K.; Ohme, M.; Tanaka, M.; Wakasugi, T.; !1Hayashida, N.; Matsubayashi, T.; Zaita, N.; Chunwongse, J.; !1Obokata, J.; Yamaguchi-Shinozaki, K.; Ohto, C.; Torazawa, !1K.; Meng, B.Y.; Sugita, M.; Deno, H.; Kamogashira, T.; !1Yamada, K.; Kusuda, J.; Takaiwa, F.; Kato, A.; Tohdoh, N.; !1Shimada, H.; Sugiura, M. !$#journal EMBO J. (1986) 5:2043-2049 !$#title The complete nucleotide sequence of the tobacco chloroplast !1genome: its gene organization and expression. !$#contents annotation; gene organization, sites, features GENETICS !$#gene rpl33 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein L33 KEYWORDS chloroplast; protein biosynthesis; ribosome SUMMARY #length 66 #molecular-weight 7693 #checksum 2093 SEQUENCE /// ENTRY R5KT33 #type complete TITLE ribosomal protein L33 - Cyanophora paradoxa cyanelle ORGANISM #formal_name cyanelle Cyanophora paradoxa DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S08231; T06890 REFERENCE S08230 !$#authors Evrard, J.L.; Kuntz, M.; Weil, J.H. !$#journal J. Mol. Evol. (1990) 30:16-25 !$#title The nucleotide sequence of five ribosomal protein genes from !1the cyanelles of Cyanophora paradoxa: implications !1concerning the phylogenetic relationship between cyanelles !1and chloroplasts. !$#cross-references MUID:90189174; PMID:2107321 !$#accession S08231 !'##molecule_type DNA !'##residues 1-64 ##label EVR !'##cross-references EMBL:X17498; NID:g11399; PIDN:CAA35534.1; !1PID:g11401 REFERENCE Z15840 !$#authors Stirewalt, V.L.; Michalowski, C.B.; Luffelhardt, W.; !1Bohnert, H.J.; Bryant, D.A. !$#submission submitted to the EMBL Data Library, July 1995 !$#description Nucleotide sequence of the cyanelle genome from Cyanophora !1paradoxa. !$#accession T06890 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-64 ##label STI !'##cross-references EMBL:U30821; NID:g1016083; PIDN:AAA81233.1; !1PID:g1016146 !'##experimental_source strain Pringsheim LB555 GENETICS !$#gene rpl33 !$#genome cyanelle CLASSIFICATION #superfamily Escherichia coli ribosomal protein L33 KEYWORDS cyanelle; protein biosynthesis; ribosome SUMMARY #length 64 #molecular-weight 7402 #checksum 8751 SEQUENCE /// ENTRY R5RT34 #type complete TITLE ribosomal protein L34, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 21-Jul-2000 ACCESSIONS S04271; S20562 REFERENCE S04271 !$#authors Aoyama, Y.; Chan, Y.L.; Wool, I.G. !$#journal FEBS Lett. (1989) 249:119-122 !$#title The primary structure of rat ribosomal protein L34. !$#cross-references MUID:89252062; PMID:2721685 !$#accession S04271 !'##molecule_type mRNA !'##residues 1-117 ##label AOY !'##cross-references EMBL:X14401 !$#accession S20562 !'##molecule_type protein !'##residues 2-34 ##label AOY2 !'##note the protein is designated as ribosomal protein L34 CLASSIFICATION #superfamily rat ribosomal protein L34 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-117 #product ribosomal protein L34 #status experimental !8#label MAT SUMMARY #length 117 #molecular-weight 13507 #checksum 7267 SEQUENCE /// ENTRY R5EC34 #type complete TITLE ribosomal protein L34 [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 12-Aug-1981 #sequence_revision 12-Aug-1981 #text_change 01-Mar-2002 ACCESSIONS C21915; A02836; S11620; H65172 REFERENCE A21915 !$#authors Hansen, F.G.; Hansen, E.B.; Atlung, T. !$#journal EMBO J. (1982) 1:1043-1048 !$#title The nucleotide sequence of the dnaA gene promoter and of the !1adjacent rpmH gene, coding for the ribosomal protein L34, of !1Escherichia coli. !$#cross-references MUID:84236082; PMID:6329723 !$#accession C21915 !'##molecule_type DNA !'##residues 1-46 ##label HAN !'##cross-references GB:J01602; NID:g145758; PIDN:AAB59148.1; !1PID:g145759; GB:X01861; NID:g42801; PIDN:CAA25982.1; !1PID:g42804 REFERENCE A02836 !$#authors Chen, R. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1976) 357:873-886 !$#title The sequence determination of a protein in a micro scale: !1the sequence analysis of ribosomal protein L34 of !1Escherichia coli. !$#cross-references MUID:76258983; PMID:783033 !$#accession A02836 !'##molecule_type protein !'##residues 1-46 ##label CHE !'##experimental_source strain K12 REFERENCE S11620 !$#authors Kashiwagi, K.; Igarashi, K. !$#journal Biochim. Biophys. Acta (1987) 911:180-190 !$#title Nonspecific inhibition of Escherichia coli ornithine !1decarboxylase by various ribosomal proteins: detection of a !1new ribosomal protein possessing strong antizyme activity. !$#cross-references MUID:87101185; PMID:3542048 !$#accession S11620 !'##molecule_type protein !'##residues 1-46 ##label KAS REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65172 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-46 ##label BLAT !'##cross-references GB:AE000447; GB:U00096; NID:g2367266; !1PIDN:AAC76726.1; PID:g1790138; UWGP:b3703 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note no post-translational modifications were observed in mass !1spectrographic analysis; any acid labile modifications may !1have been missed GENETICS !$#gene rpmH !$#map_position 83 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX large subunit ribosomal proteins: L1 (PIR:R5EC1), L3 !1(PIR:R5EC3), L2 (PIR:R5EC2), L4 (PIR:R5EC4), L5 (PIR:R5EC5), !1L6 (PIR:R5EC6), L7/L12 (PIR:R5EC7), L9 (PIR:R5EC9), L10 !1(PIR:R5EC10), L11 (PIR:R5EC11), L13 (PIR:R5EC13), L14 !1(PIR:R5EC14), L15 (PIR:R5EC15), L16 (PIR:R5EC16), L17 !1(PIR:R5EC17), L18 (PIR:R5EC18), L19 (PIR:R5EC19) FUNCTION !$#pathway protein biosynthesis CLASSIFICATION #superfamily Escherichia coli ribosomal protein L34 KEYWORDS protein biosynthesis; ribosome FEATURE !$1-46 #product ribosomal protein L34 #status experimental !8#label MAT SUMMARY #length 46 #molecular-weight 5380 #checksum 3614 SEQUENCE /// ENTRY JQ0732 #type complete TITLE ribosomal protein L34 - Proteus mirabilis ORGANISM #formal_name Proteus mirabilis DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 22-Jun-1999 ACCESSIONS JQ0732 REFERENCE JQ0729 !$#authors Skovgaard, O. !$#journal Gene (1990) 93:27-34 !$#title Nucleotide sequence of a Proteus mirabilis DNA fragment !1homologous to the 60K-rnpA-rpmH-dnaA-dnaN-recF-gyrB region !1of Escherichia coli. !$#cross-references MUID:91033012; PMID:2172087 !$#accession JQ0732 !'##molecule_type DNA !'##residues 1-47 ##label SKO !'##cross-references GB:M58352; GB:M31295; NID:g150873; PIDN:AAA83957.1; !1PID:g150877 !'##experimental_source strain LM1509 GENETICS !$#gene rpmH CLASSIFICATION #superfamily Escherichia coli ribosomal protein L34 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 47 #molecular-weight 5494 #checksum 7432 SEQUENCE /// ENTRY JC1154 #type complete TITLE ribosomal protein L34 - Buchnera aphidicola ORGANISM #formal_name Buchnera aphidicola DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 22-Jun-1999 ACCESSIONS JC1154 REFERENCE JC1154 !$#authors Lai, C.Y.; Baumann, P. !$#journal Gene (1992) 113:175-181 !$#title Genetic analysis of an aphid endosymbiont DNA fragment !1homologous to the rnpA-rpmH-dnaA-dnaN-gyrB region of !1eubacteria. !$#cross-references MUID:92241666; PMID:1572539 !$#accession JC1154 !'##molecule_type DNA !'##residues 1-47 ##label LAI !'##cross-references GB:M80817; NID:g144144; PIDN:AAA73148.1; !1PID:g144148 GENETICS !$#gene rpmH CLASSIFICATION #superfamily Escherichia coli ribosomal protein L34 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 47 #molecular-weight 5663 #checksum 9138 SEQUENCE /// ENTRY R6PS34 #type complete TITLE ribosomal protein L34 - Pseudomonas putida ORGANISM #formal_name Pseudomonas putida DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 22-Jun-1999 ACCESSIONS S18090; C34835; JQ1218 REFERENCE S18071 !$#authors Ogasawara, N.; Yoshikawa, H. !$#submission submitted to the EMBL Data Library, October 1991 !$#description Genes and their organization in replication origin region of !1bacterial chromosome. !$#accession S18090 !'##molecule_type DNA !'##residues 1-44 ##label OGA !'##cross-references EMBL:X62540; NID:g45705; PIDN:CAA44414.1; !1PID:g45706 !'##experimental_source strain TN2100 REFERENCE A34835 !$#authors Yee, T.W.; Smith, D.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:1278-1282 !$#title Pseudomonas chromosomal replication origins: a bacterial !1class distinct from Escherichia coli-type origins. !$#cross-references MUID:90160310; PMID:2106132 !$#accession C34835 !'##status preliminary !'##molecule_type DNA !'##residues 1-11 ##label YEE !'##cross-references GB:M30126; NID:g151422; PIDN:AAA25917.1; !1PID:g551934 GENETICS !$#gene rpmH CLASSIFICATION #superfamily Escherichia coli ribosomal protein L34 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 44 #molecular-weight 5138 #checksum 5350 SEQUENCE /// ENTRY R6BS34 #type complete TITLE ribosomal protein L34 - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 21-Jul-2000 ACCESSIONS I40435; S66030; B69698; JQ1213; S18071 REFERENCE I40435 !$#authors Ogasawara, N.; Yoshikawa, H. !$#journal Mol. Microbiol. (1992) 6:629-634 !$#title Genes and their organization in the replication origin !1region of the bacterial chromosome. !$#cross-references MUID:92204018; PMID:1552862 !$#accession I40435 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-44 ##label RES !'##cross-references EMBL:X62539; NID:g40020; PIDN:CAA44399.1; !1PID:g40021 !'##experimental_source strain CRK2000 REFERENCE S65967 !$#authors Ogasawara, N.; Nakai, S.; Yoshikawa, H. !$#journal DNA Res. (1994) 1:1-14 !$#title Systematic sequencing of the 180 kilobase region of the !1Bacillus subtilis chromosome containing the replication !1origin. !$#cross-references MUID:96051385; PMID:7584024 !$#accession S66030 !'##status preliminary !'##molecule_type DNA !'##residues 1-44 ##label OGA !'##cross-references EMBL:D26185; NID:g467326; PIDN:BAA05236.1; !1PID:g467390 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69698 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-44 ##label KUN !'##cross-references GB:Z99124; GB:AL009126; NID:g2636442; !1PIDN:CAB16143.1; PID:g2636653 !'##experimental_source strain 168 GENETICS !$#gene rpmH CLASSIFICATION #superfamily Escherichia coli ribosomal protein L34 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 44 #molecular-weight 5253 #checksum 7203 SEQUENCE /// ENTRY R5RT35 #type complete TITLE ribosomal protein L35, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 21-Jul-2000 ACCESSIONS A34571; A34991; S10390 REFERENCE A34571 !$#authors Suzuki, K.; Olvera, J.; Wool, I.G. !$#journal Biochem. Biophys. Res. Commun. (1990) 167:1377-1382 !$#title The primary structure of rat ribosomal protein L35. !$#cross-references MUID:90211326; PMID:2322279 !$#accession A34571 !'##molecule_type mRNA !'##residues 1-123 ##label SUZ !'##cross-references EMBL:M34331; NID:g57701; PIDN:CAA36001.1; !1PID:g57702 !$#accession A34991 !'##molecule_type protein !'##residues 2-36 ##label SUZ2 !'##note the protein is designated as ribosomal protein L35 CLASSIFICATION #superfamily rat ribosomal protein L35 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-123 #product ribosomal protein L35 #status experimental !8#label MAT SUMMARY #length 123 #molecular-weight 14552 #checksum 8735 SEQUENCE /// ENTRY R5EC36 #type complete TITLE ribosomal protein L36 [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES ribosomal protein X ORGANISM #formal_name Escherichia coli DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 01-Mar-2002 ACCESSIONS S14057; B26779; F65122 REFERENCE A02714 !$#authors Cerretti, D.P.; Dean, D.; Davis, G.R.; Bedwell, D.M.; !1Nomura, M. !$#journal Nucleic Acids Res. (1983) 11:2599-2616 !$#title The spc ribosomal protein operon of Escherichia coli: !1sequence and cotranscription of the ribosomal protein genes !1and a protein export gene. !$#cross-references MUID:83220807; PMID:6222285 !$#accession S14057 !'##molecule_type DNA !'##residues 1-38 ##label CER !'##cross-references EMBL:X01563; NID:g42977; PIDN:CAA25726.1; !1PID:g42990 REFERENCE A26779 !$#authors Wada, A.; Sako, T. !$#journal J. Biochem. (1987) 101:817-820 !$#title Primary structures of and genes for new ribosomal proteins A !1and B in Escherichia coli. !$#cross-references MUID:87250369; PMID:3298224 !$#accession B26779 !'##molecule_type protein !'##residues 'X',2-10,'XX',13,'XX',16-17 ##label WAD REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65122 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-38 ##label BLAT !'##cross-references GB:AE000408; GB:U00096; NID:g1789694; !1PIDN:AAC76324.1; PID:g1789695; UWGP:b3299 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note no post-translational modifications were observed in mass !1spectrographic analysis; any acid labile modifications may !1have been missed GENETICS !$#gene rpmJ !$#map_position 73 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX large subunit ribosomal proteins: L1 (PIR:R5EC1), L3 !1(PIR:R5EC3), L2 (PIR:R5EC2), L4 (PIR:R5EC4), L5 (PIR:R5EC5), !1L6 (PIR:R5EC6), L7/L12 (PIR:R5EC7), L9 (PIR:R5EC9), L10 !1(PIR:R5EC10), L11 (PIR:R5EC11), L13 (PIR:R5EC13), L14 !1(PIR:R5EC14), L15 (PIR:R5EC15), L16 (PIR:R5EC16), L17 !1(PIR:R5EC17), L18 (PIR:R5EC18), L19 (PIR:R5EC19) FUNCTION !$#pathway protein biosynthesis CLASSIFICATION #superfamily Escherichia coli ribosomal protein L36 KEYWORDS protein biosynthesis; ribosome FEATURE !$1-38 #product ribosomal protein L36 #status experimental !8#label MAT SUMMARY #length 38 #molecular-weight 4364 #checksum 6423 SEQUENCE /// ENTRY R5RZ36 #type complete TITLE ribosomal protein L36, chloroplast - rice chloroplast ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 22-Jun-1999 ACCESSIONS JQ0260; S05140 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0260 !'##molecule_type DNA !'##residues 1-37 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05140 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-37 ##label HIR !'##cross-references GB:X15901; NID:g11957; PIDN:CAA33981.1; PID:g12020 !'##experimental_source cv. Nihonbare !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1989 GENETICS !$#gene rpl36 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein L36 KEYWORDS chloroplast; protein biosynthesis; ribosome FEATURE !$1-37 #product ribosomal protein L36a #status predicted !8#label MAT SUMMARY #length 37 #molecular-weight 4447 #checksum 4335 SEQUENCE /// ENTRY R5NT36 #type complete TITLE ribosomal protein L36, chloroplast - common tobacco chloroplast ALTERNATE_NAMES secX protein ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 30-Jan-1998 ACCESSIONS A05203 REFERENCE A00149 !$#authors Sugiura, M. !$#submission submitted to the EMBL Data Library, August 1986 !$#accession A05203 !'##molecule_type DNA !'##residues 1-37 ##label OHY !'##cross-references EMBL:Z00044 !'##experimental_source cv. Bright Yellow 4 REFERENCE A38013 !$#authors Shinozaki, K.; Ohme, M.; Tanaka, M.; Wakasugi, T.; !1Hayashida, N.; Matsubayashi, T.; Zaita, N.; Chunwongse, J.; !1Obokata, J.; Yamaguchi-Shinozaki, K.; Ohto, C.; Torazawa, !1K.; Meng, B.Y.; Sugita, M.; Deno, H.; Kamogashira, T.; !1Yamada, K.; Kusuda, J.; Takaiwa, F.; Kato, A.; Tohdoh, N.; !1Shimada, H.; Sugiura, M. !$#journal EMBO J. (1986) 5:2043-2049 !$#title The complete nucleotide sequence of the tobacco chloroplast !1genome: its gene organization and expression. !$#contents annotation; gene organization, sites, features GENETICS !$#gene secX !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein L36 KEYWORDS chloroplast; protein biosynthesis; ribosome FEATURE !$1-37 #product ribosomal protein L36a #status predicted !8#label MAT SUMMARY #length 37 #molecular-weight 4460 #checksum 4156 SEQUENCE /// ENTRY R5LV36 #type complete TITLE ribosomal protein L36, chloroplast - liverwort (Marchantia polymorpha) chloroplast ALTERNATE_NAMES secX protein ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 22-Jun-1999 ACCESSIONS A05060; S01563 REFERENCE A00150 !$#authors Ohyama, K. !$#submission submitted to the EMBL Data Library, October 1986 !$#accession A05060 !'##molecule_type DNA !'##residues 1-37 ##label OHY !'##cross-references EMBL:X04465; NID:g11640; PIDN:CAA28119.1; !1PID:g11708 REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features REFERENCE S01529 !$#authors Fukuzawa, H.; Kohchi, T.; Sano, T.; Shirai, H.; Umesono, K.; !1Inokuchi, H.; Ozeki, H.; Ohyama, K. !$#journal J. Mol. Biol. (1988) 203:333-351 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. III. Gene organization of the large !1single copy region from rbcL to trnI(CAU). !$#cross-references MUID:89068687; PMID:3199436 !$#accession S01563 !'##molecule_type DNA !'##residues 1-37 ##label FUK !'##cross-references EMBL:X04465; NID:g11640; PIDN:CAA28119.1; !1PID:g11708 GENETICS !$#gene secX !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein L36 KEYWORDS chloroplast; protein biosynthesis; ribosome FEATURE !$1-37 #product ribosomal protein L36a #status predicted !8#label MAT SUMMARY #length 37 #molecular-weight 4521 #checksum 4643 SEQUENCE /// ENTRY R5PM81 #type complete TITLE ribosomal protein L36 - garden pea chloroplast ORGANISM #formal_name chloroplast Pisum sativum #common_name garden pea DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 22-Jun-1999 ACCESSIONS A27301; S04382 REFERENCE A27301 !$#authors Purton, S.; Gray, J.C. !$#journal Nucleic Acids Res. (1987) 15:9080 !$#title Nucleotide sequence of the gene for ribosomal protein L36 in !1pea chloroplast DNA. !$#cross-references MUID:88067720; PMID:3684583 !$#accession A27301 !'##molecule_type DNA !'##residues 1-37 ##label PUR !'##cross-references GB:Y00468; NID:g12162; PIDN:CAA68531.1; PID:g12163 GENETICS !$#gene rpl36 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein L36 KEYWORDS chloroplast; protein biosynthesis; ribosome FEATURE !$1-37 #product ribosomal protein L36a #status predicted !8#label MAT SUMMARY #length 37 #molecular-weight 4333 #checksum 4051 SEQUENCE /// ENTRY R5EG36 #type complete TITLE ribosomal protein L36, chloroplast - Euglena gracilis chloroplast ORGANISM #formal_name chloroplast Euglena gracilis #variety strain Z DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 22-Jun-1999 ACCESSIONS S09290; S34530; S34897 REFERENCE S09286 !$#authors Christopher, D.A.; Hallick, R.B. !$#journal Nucleic Acids Res. (1989) 17:7591-7608 !$#title Euglena gracilis chloroplast ribosomal protein operon: a new !1chloroplast gene for ribosomal protein L5 and description of !1a novel organelle intron category designated group III. !$#cross-references MUID:90016846; PMID:2477800 !$#accession S09290 !'##molecule_type DNA !'##residues 1-37 ##label CHR !'##cross-references EMBL:Z11874; NID:g14353; PIDN:CAA77926.1; !1PID:g14376 REFERENCE S34494 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.; Monfort, !1A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#submission submitted to the EMBL Data Library, January 1993 !$#description The complete sequence of the Euglena gracilis chloroplast !1genome (tentative). !$#accession S34530 !'##molecule_type DNA !'##residues 1-37 ##label HAL1 !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50109.1; !1PID:g415765 REFERENCE S34862 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.R.; !1Monfort, A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#journal Nucleic Acids Res. (1993) 21:3537-3544 !$#title Complete sequence of Euglena gracilis chloroplast DNA. !$#cross-references MUID:93347989; PMID:8346031 !$#accession S34897 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-37 ##label HAL2 !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50109.1; !1PID:g415765 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1993 GENETICS !$#gene rpl36 !$#genome chloroplast CLASSIFICATION #superfamily Escherichia coli ribosomal protein L36 KEYWORDS chloroplast; protein biosynthesis; ribosome FEATURE !$1-37 #product ribosomal protein L36a #status predicted !8#label MAT SUMMARY #length 37 #molecular-weight 4428 #checksum 4244 SEQUENCE /// ENTRY R5BS36 #type complete TITLE ribosomal protein L36 - Bacillus stearothermophilus ALTERNATE_NAMES ribosomal protein BL38; ribosomal protein II ORGANISM #formal_name Bacillus stearothermophilus DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 07-May-1999 ACCESSIONS S08566; S59066 REFERENCE S07236 !$#authors Tanaka, I.; Kimura, M.; Kimura, J.; Dijk, J. !$#journal FEBS Lett. (1984) 166:343-346 !$#title The amino acid sequence of two small ribosomal proteins from !1Bacillus stearothermophilus. !$#cross-references MUID:84108949; PMID:6420194 !$#accession S08566 !'##molecule_type protein !'##residues 1-37 ##label TAN REFERENCE S59051 !$#authors Urlaub, H.; Kruft, V.; Bischof, O.; Mueller, E.C.; !1Wittmann-Liebold, B. !$#journal EMBO J. (1995) 14:4578-4588 !$#title Protein-rRNA binding features and their structural and !1functional implications in ribosomes as determined by !1cross-linking studies. !$#cross-references MUID:96003638; PMID:7556101 !$#accession S59066 !'##molecule_type protein !'##residues 14-31 ##label URL CLASSIFICATION #superfamily Escherichia coli ribosomal protein L36 KEYWORDS protein biosynthesis; ribosome FEATURE !$1-37 #product ribosomal protein L36a #status predicted !8#label MAT SUMMARY #length 37 #molecular-weight 4361 #checksum 3946 SEQUENCE /// ENTRY R5IT36 #type complete TITLE ribosomal protein L36 - euglenid (Astasia longa) plastid ORGANISM #formal_name plastid Astasia longa DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 22-Jun-1999 ACCESSIONS S14152; S38593 REFERENCE S14125 !$#authors Siemeister, G.; Buchholz, C.; Hachtel, W. !$#journal Curr. Genet. (1990) 18:457-464 !$#title Genes for ribosomal proteins are retained on the 73 kb DNA !1from Astasia longa that resembles Euglena chloroplast DNA. !$#cross-references MUID:91176556; PMID:2078869 !$#accession S14152 !'##molecule_type DNA !'##residues 1-37 ##label SIE !'##cross-references EMBL:X16004; NID:g16004; PIDN:CAA34140.1; !1PID:g16010 REFERENCE S38590 !$#authors Gockel, G.; Baier, S.; Hachtel, W. !$#submission submitted to the EMBL Data Library, November 1993 !$#accession S38593 !'##molecule_type DNA !'##residues 1-37 ##label GOC !'##cross-references EMBL:X75651; NID:g414852; PIDN:CAA53311.1; !1PID:g414858 GENETICS !$#gene rpl36 !$#genome plastid CLASSIFICATION #superfamily Escherichia coli ribosomal protein L36 KEYWORDS plastid; protein biosynthesis; ribosome FEATURE !$1-37 #product ribosomal protein L36a #status predicted !8#label MAT SUMMARY #length 37 #molecular-weight 4389 #checksum 4152 SEQUENCE /// ENTRY R5EC35 #type complete TITLE ribosomal protein L35 [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES ribosomal protein A; ribosomal protein X1 ORGANISM #formal_name Escherichia coli DATE 30-Jun-1991 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS E64930; S13749; S11621; A26779 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64930 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-65 ##label BLAT !'##cross-references GB:AE000266; GB:U00096; NID:g1787997; !1PIDN:AAC74787.1; PID:g1788010; UWGP:b1717 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S13748 !$#authors Sacerdot, C.; Fayat, G.; Dessen, P.; Springer, M.; !1Plumbridge, J.A.; Grunberg-Manago, M.; Blanquet, S. !$#journal EMBO J. (1982) 1:311-315 !$#title Sequence of a 1.26-kb DNA fragment containing the structural !1gene for E.coli initiation factor IF3: presence of an AUU !1initiator codon. !$#cross-references MUID:84182476; PMID:6325158 !$#accession S13749 !'##status translation not shown !'##molecule_type DNA !'##residues 1-10,'S',12-65 ##label SAC !'##cross-references EMBL:V00291; GB:M10430; NID:g43065 !'##note the nucleotide sequence contains a frameshift error in having !1an additional A between codons 4 and 5 !'##note this ORF is not annotated in GenBank entry ECTHRINF, release !1111.0 REFERENCE S11620 !$#authors Kashiwagi, K.; Igarashi, K. !$#journal Biochim. Biophys. Acta (1987) 911:180-190 !$#title Nonspecific inhibition of Escherichia coli ornithine !1decarboxylase by various ribosomal proteins: detection of a !1new ribosomal protein possessing strong antizyme activity. !$#cross-references MUID:87101185; PMID:3542048 !$#accession S11621 !'##molecule_type protein !'##residues 2-27,'D',29-42 ##label KAS1 REFERENCE A26779 !$#authors Wada, A.; Sako, T. !$#journal J. Biochem. (1987) 101:817-820 !$#title Primary structures of and genes for new ribosomal proteins A !1and B in Escherichia coli. !$#cross-references MUID:87250369; PMID:3298224 !$#accession A26779 !'##molecule_type protein !'##residues 2-19,'X',21-23,'X',25,'X',27-29,'XX',32-33,'XX',36 ##label !1KAS2 REFERENCE A59071 !$#authors Arnold, R.J.; Reilly, J.P. !$#journal Anal. Biochem. (1999) 269:105-112 !$#title Observation of Escherichia coli ribosomal proteins and their !1posttranslational modifications by mass spectrometry. !$#cross-references MUID:99196679; PMID:10094780 !$#contents annotation; mass spectrographic analysis !$#note mass spectrographic analysis of post-translational !1modifications; any acid labile modifications may have been !1missed GENETICS !$#gene rpmI !$#map_position 38 min COMPLEX the ribosome is composed of the large (50S) and small (30S) !1subunit; the large (50S) subunit consists of 23S rRNA, 5S !1rRNA, and 34 distinct proteins; the small (30S) subunit !1consists of 16S rRNA and 22 distinct proteins COMPLEX large subunit ribosomal proteins: L1 (PIR:R5EC1), L3 !1(PIR:R5EC3), L2 (PIR:R5EC2), L4 (PIR:R5EC4), L5 (PIR:R5EC5), !1L6 (PIR:R5EC6), L7/L12 (PIR:R5EC7), L9 (PIR:R5EC9), L10 !1(PIR:R5EC10), L11 (PIR:R5EC11), L13 (PIR:R5EC13), L14 !1(PIR:R5EC14), L15 (PIR:R5EC15), L16 (PIR:R5EC16), L17 !1(PIR:R5EC17), L18 (PIR:R5EC18), L19 (PIR:R5EC19) FUNCTION !$#pathway protein biosynthesis CLASSIFICATION #superfamily Escherichia coli ribosomal protein L35 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-65 #product ribosomal protein L35 #status experimental !8#label MAT SUMMARY #length 65 #molecular-weight 7289 #checksum 7411 SEQUENCE /// ENTRY R5BS35 #type complete TITLE ribosomal protein L35 - Bacillus stearothermophilus ORGANISM #formal_name Bacillus stearothermophilus DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 22-Jun-1999 ACCESSIONS S05347 REFERENCE S05346 !$#authors Pon, C.L.; Brombach, M.; Thamm, S.; Gualerzi, C.O. !$#journal Mol. Gen. Genet. (1989) 218:355-357 !$#title Cloning and characterization of a gene cluster from Bacillus !1stearothermophilus comprising infC, rpmI and rplT. !$#cross-references MUID:89384464; PMID:2779520 !$#accession S05347 !'##molecule_type DNA !'##residues 1-66 ##label PON !'##cross-references EMBL:X16188; NID:g39960; PIDN:CAA34313.1; !1PID:g39962 GENETICS !$#gene rpmI CLASSIFICATION #superfamily Escherichia coli ribosomal protein L35 KEYWORDS protein biosynthesis; ribosome SUMMARY #length 66 #molecular-weight 7690 #checksum 9523 SEQUENCE /// ENTRY R5KT35 #type complete TITLE ribosomal protein L35 - Cyanophora paradoxa cyanelle ORGANISM #formal_name cyanelle Cyanophora paradoxa DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 22-Jun-1999 ACCESSIONS S07070; T06849 REFERENCE S07067 !$#authors Bryant, D.A.; Stirewalt, V.L. !$#journal FEBS Lett. (1990) 259:273-280 !$#title The cyanelle genome of Cyanophora paradoxa encodes ribosomal !1proteins not encoded by the chloroplast genomes of higher !1plants. !$#cross-references MUID:90092562; PMID:2403527 !$#accession S07070 !'##molecule_type DNA !'##residues 1-65 ##label BRY !'##cross-references EMBL:X17063; NID:g11291; PIDN:CAA34907.1; !1PID:g11292 REFERENCE Z15840 !$#authors Stirewalt, V.L.; Michalowski, C.B.; Luffelhardt, W.; !1Bohnert, H.J.; Bryant, D.A. !$#submission submitted to the EMBL Data Library, July 1995 !$#description Nucleotide sequence of the cyanelle genome from Cyanophora !1paradoxa. !$#accession T06849 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-65 ##label STI !'##cross-references EMBL:U30821; NID:g1016083; PIDN:AAA81192.1; !1PID:g1016105 !'##experimental_source strain Pringsheim LB555 GENETICS !$#gene rpl35; rpmI !$#map_position 27 !$#genome cyanelle CLASSIFICATION #superfamily Escherichia coli ribosomal protein L35 KEYWORDS cyanelle; protein biosynthesis; ribosome SUMMARY #length 65 #molecular-weight 7607 #checksum 968 SEQUENCE /// ENTRY R5RT37 #type complete TITLE ribosomal protein L37a, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 21-Jul-2000 ACCESSIONS S05014; S11422 REFERENCE S05014 !$#authors Tanaka, T.; Aoyama, Y.; Chan, Y.L.; Wool, I.G. !$#journal Eur. J. Biochem. (1989) 183:15-18 !$#title The primary structure of rat ribosomal protein L37a. !$#cross-references MUID:89325328; PMID:2546769 !$#accession S05014 !'##molecule_type mRNA !'##residues 1-92 ##label TAN !'##cross-references EMBL:X14069; NID:g57122; PIDN:CAA32232.1; !1PID:g57123 !'##note the protein is designated as ribosomal protein L37a REFERENCE S11413 !$#authors Wittmann-Liebold, B.; Geissler, A.W.; Lin, A.; Wool, I.G. !$#journal J. Supramol. Struct. (1979) 12:425-433 !$#title Sequence of the amino-terminal region of rat liver ribosomal !1proteins S4, S6, S8, L6, L7a, L18, L27, L30, L37, L37a, and !1L39. !$#cross-references MUID:80252792; PMID:398910 !$#accession S11422 !'##molecule_type protein !'##residues 2-29 ##label WIT !'##note the protein is designated as ribosomal protein L37a CLASSIFICATION #superfamily rat ribosomal protein L37a KEYWORDS protein biosynthesis; ribosome; zinc finger FEATURE !$2-92 #product ribosomal protein L37a #status experimental !8#label MAT SUMMARY #length 92 #molecular-weight 10275 #checksum 4661 SEQUENCE /// ENTRY A64374 #type complete TITLE ribosomal protein L37a - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 13-Sep-1996 #sequence_revision 04-Oct-1996 #text_change 21-Jul-2000 ACCESSIONS A64374 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession A64374 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-92 ##label BUL !'##cross-references GB:U67508; GB:L77117; NID:g1591300; !1PIDN:AAB98587.1; PID:g1591302; TIGR:MJ0593 GENETICS !$#map_position FOR526405-526683 CLASSIFICATION #superfamily rat ribosomal protein L37a KEYWORDS protein biosynthesis; ribosome FEATURE !$2-92 #product ribosomal protein L37a #status predicted !8#label MAT SUMMARY #length 92 #molecular-weight 10183 #checksum 4389 SEQUENCE /// ENTRY R5RT38 #type complete TITLE ribosomal protein L38, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 21-Jul-2000 ACCESSIONS S15658; S19041; JT0568 REFERENCE JT0568 !$#authors Kuwano, Y.; Olvera, J.; Wool, I.G. !$#journal Biochem. Biophys. Res. Commun. (1991) 175:551-555 !$#title The primary structure of rat ribosomal protein L38. !$#cross-references MUID:91207349; PMID:1840484 !$#accession S15658 !'##molecule_type mRNA !'##residues 1-70 ##label KUW !'##cross-references EMBL:X57007; NID:g57077; PIDN:CAA40328.1; !1PID:g57078 !$#accession S19041 !'##molecule_type protein !'##residues 2-33 ##label KUW2 !'##note the protein is designated as ribosomal protein L38 CLASSIFICATION #superfamily rat ribosomal protein L38 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-70 #product ribosomal protein L38 #status experimental !8#label MAT SUMMARY #length 70 #molecular-weight 8218 #checksum 3048 SEQUENCE /// ENTRY R6RT43 #type complete TITLE ribosomal protein L29, cytosolic [validated] - rat ALTERNATE_NAMES protein p23; ribosomal protein RL43 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 01-Sep-2000 ACCESSIONS S20594; JN0477; PN0452; S20418; S19164 REFERENCE S20594 !$#authors Svoboda, M.; Ciccarelli, E.; Vandermeers-Piret, M.C.; Nagy, !1A.M.; van de Weerdt, C.; Bollen, A.; Vandermeers, A.; !1Christophe, J. !$#journal Eur. J. Biochem. (1992) 203:341-346 !$#title Purification, primary structure and molecular cloning of a !1rat ribosomal protein showing homology with yeast ribosomal !1protein YL34. !$#cross-references MUID:92137216; PMID:1735422 !$#accession S20594 !'##molecule_type mRNA !'##residues 1-156 ##label SVO !'##cross-references EMBL:X60744; NID:g57144; PIDN:CAA43146.1; !1PID:g57145 !'##experimental_source strain Wistar REFERENCE JN0477 !$#authors Chan, Y.L.; Olvera, J.; Paz, V.; Wool, I.G. !$#journal Biochem. Biophys. Res. Commun. (1993) 192:583-589 !$#title The primary structure of rat ribosomal protein L29. !$#cross-references MUID:93249429; PMID:8484767 !$#accession JN0477 !'##molecule_type mRNA !'##residues 1-156 ##label CHA !'##cross-references GB:X68283; NID:g312207; PIDN:CAA48344.1; !1PID:g312208 !$#accession PN0452 !'##molecule_type protein !'##residues 2-35 ##label CH1 !'##note the protein is designated as ribosomal protein L29 REFERENCE S20418 !$#authors Ostvold, A.C.; Hullstein, I.; Sletten, K. !$#journal FEBS Lett. (1992) 298:219-222 !$#title p23, a novel mammalian nucleic acid-binding protein with !1homology to the yeast ribosomal protein YL43. !$#cross-references MUID:92183869; PMID:1544448 !$#accession S20418 !'##molecule_type protein !'##residues 2-15,'X',17-25,'X',27-29 ##label OST GENETICS !$#gene L29 CLASSIFICATION #superfamily rat ribosomal protein L29 KEYWORDS protein biosynthesis; ribosome FEATURE !$2-156 #product ribosomal protein L29 #status experimental !8#label RBL SUMMARY #length 156 #molecular-weight 17326 #checksum 7958 SEQUENCE /// ENTRY R6BYM1 #type complete TITLE ribosomal protein MRP1 precursor, mitochondrial - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein D9651.1; protein YDR347w ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1992 #sequence_revision 07-Feb-1997 #text_change 05-Nov-1999 ACCESSIONS S70112; A29138 REFERENCE S70098 !$#authors Du, Z. !$#submission submitted to the EMBL Data Library, March 1996 !$#description The sequence of S. cerevisiae cosmid 9651. !$#accession S70112 !'##molecule_type DNA !'##residues 1-321 ##label DUZ !'##cross-references EMBL:U51032; NID:g1230659; PIDN:AAB64783.1; !1PID:g1230674; GSPDB:GN00004; MIPS:YDR347w REFERENCE A92628 !$#authors Myers, A.M.; Crivellone, M.D.; Tzagoloff, A. !$#journal J. Biol. Chem. (1987) 262:3388-3397 !$#title Assembly of the mitochondrial membrane system. MRP1 and !1MRP2, two yeast nuclear genes coding for mitochondrial !1ribosomal proteins. !$#cross-references MUID:87137621; PMID:3029111 !$#accession A29138 !'##molecule_type DNA !'##residues 1-112,'S',114-318,'H',320-321 ##label MYE !'##cross-references GB:M15160; NID:g171968; PIDN:AAA74727.1; !1PID:g171969 !'##note the authors translated the codon GAG for residue 306 as Gly GENETICS !$#gene SGD:MRP1; MIPS:YDR347w !'##cross-references SGD:S0002755; MIPS:YDR347w !$#map_position 4R !$#genome nuclear CLASSIFICATION #superfamily Saccharomyces cerevisiae mitochondrial !1ribosomal protein MRP1 KEYWORDS mitochondrion; protein biosynthesis; ribosome SUMMARY #length 321 #molecular-weight 36728 #checksum 2722 SEQUENCE /// ENTRY R6BYM7 #type complete TITLE ribosomal protein YmL2 precursor, mitochondrial - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein N2007; protein YNL005c; ribosomal protein MRP7 ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1992 #sequence_revision 17-May-1996 #text_change 16-Jun-2000 ACCESSIONS S62914; S62916; S45460; A30236; S17256; S45122 REFERENCE S62910 !$#authors Aert, R.; Verhasselt, P.; Voet, M.; Volckaert, G. !$#submission submitted to the Protein Sequence Database, April 1996 !$#accession S62914 !'##molecule_type DNA !'##residues 1-371 ##label AER !'##cross-references EMBL:Z71281; NID:g1301819; PIDN:CAA95864.1; !1PID:g1301820; GSPDB:GN00014; MIPS:YNL005c !'##experimental_source strain S288C REFERENCE S62916 !$#authors Doignon, F.; Crouzet, M. !$#submission submitted to the Protein Sequence Database, April 1996 !$#accession S62916 !'##molecule_type DNA !'##residues 35-371 ##label DOI !'##cross-references EMBL:Z71281; GSPDB:GN00014; MIPS:YNL005c !'##experimental_source strain S288C REFERENCE S45456 !$#authors Verhasselt, P.; Aert, R.; Voet, M.; Volckaert, G. !$#journal Yeast (1994) 10:945-951 !$#title Nucleotide sequence analysis of an 8887 bp region of the !1left arm of yeast chromosome XIV, encompassing the !1centromere sequence. !$#cross-references MUID:95076713; PMID:7985421 !$#accession S45460 !'##status translation not shown !'##molecule_type DNA !'##residues 1-349,'L',351-371 ##label VER !'##cross-references EMBL:X77114; NID:g496710; PIDN:CAA54379.1; !1PID:g496715 REFERENCE A30236 !$#authors Fearon, K.; Mason, T.L. !$#journal Mol. Cell. Biol. (1988) 8:3636-3646 !$#title Structure and regulation of a nuclear gene in Saccharomyces !1cerevisiae that specifies MRP7, a protein of the large !1subunit of the mitochondrial ribosome. !$#cross-references MUID:89127202; PMID:2851722 !$#accession A30236 !'##molecule_type DNA !'##residues 1-371 ##label FEA !'##cross-references EMBL:M22116; NID:g171983; PIDN:AAA34794.1; !1PID:g171984 REFERENCE S17255 !$#authors Grohmann, L.; Graack, H.R.; Kruft, V.; Choli, T.; !1Goldschmidt-Reisin, S.; Kitakawa, M. !$#journal FEBS Lett. (1991) 284:51-56 !$#title Extended N-terminal sequencing of proteins of the large !1ribosomal subunit from yeast mitochondria. !$#cross-references MUID:91285106; PMID:2060626 !$#accession S17256 !'##molecule_type protein !'##residues 'SG',30,'X',32-36,'X',38-41,'X',43-45,'X',47-48,'X',50 !1##label GRO GENETICS !$#gene SGD:MRP7; MRPL2; MIPS:YNL005c !'##cross-references SGD:S0004950; MIPS:YNL005c !$#map_position 14L CLASSIFICATION #superfamily Saccharomyces cerevisiae mitochondrial !1ribosomal protein MRP7; eubacterial ribosomal protein L27 !1homology KEYWORDS mitochondrion; protein biosynthesis; ribosome FEATURE !$1-27 #domain transit peptide (mitochondrion) #status !8experimental #label TNP\ !$28-371 #product ribosomal protein YmL2, mitochondrial !8#status experimental #label MAT\ !$28-112 #domain eubacterial ribosomal protein L27 homology !8#label L27 SUMMARY #length 371 #molecular-weight 43226 #checksum 598 SEQUENCE /// ENTRY R6BY13 #type complete TITLE ribosomal protein MRP13 precursor, mitochondrial - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein G4618; protein YGR084c; ribosomal protein YmS-A ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1992 #sequence_revision 19-Jul-1996 #text_change 16-Jun-2000 ACCESSIONS S64379; A30237; S78035; S07831 REFERENCE S64356 !$#authors Wedler, H.; Scharfe, M.; Wedler, E.; Wambutt, R. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64379 !'##molecule_type DNA !'##residues 1-339 ##label WED !'##cross-references EMBL:Z72869; NID:g1323120; PIDN:CAA97086.1; !1PID:g1323121; GSPDB:GN00007; MIPS:YGR084c !'##experimental_source strain S288C REFERENCE A30237 !$#authors Partaledis, J.A.; Mason, T.L. !$#journal Mol. Cell. Biol. (1988) 8:3647-3660 !$#title Structure and regulation of a nuclear gene in Saccharomyces !1cerevisiae that specifies MRP13, a protein of the small !1subunit of the mitochondrial ribosome. !$#cross-references MUID:89127203; PMID:3065621 !$#accession A30237 !'##molecule_type DNA !'##residues 28-113,'S',115-309,'RIQRSIRHAFESV',323,'TVGNTLSGSG',336, !1'RG',339,'IVQNTHRKYINNIL' ##label PAR !'##cross-references EMBL:M22109; NID:g171970; PIDN:AAA34788.1; !1PID:g171971 !'##note the authors translated the codon AGT for residues 4, 227, 236, !1and 282 as Phe REFERENCE S78018 !$#authors Kitakawa, M.; Graack, H.R.; Grohmann, L.; !1Goldschmidt-Reisin, S.; Herfurth, E.; Wittmann-Liebold, B.; !1Nishimura, T.; Isono, K. !$#journal Eur. J. Biochem. (1997) 245:449-456 !$#title Identification and characterization of the genes for !1mitochondrial ribosomal proteins of Saccharomyces !1cerevisiae. !$#cross-references MUID:97296414; PMID:9151978 !$#accession S78035 !'##molecule_type protein !'##residues 'X',39-51 ##label KIT GENETICS !$#gene SGD:MRP13; MIPS:YGR084c !'##cross-references SGD:S0003316; MIPS:YGR084c !$#map_position 7R !$#genome nuclear CLASSIFICATION #superfamily Saccharomyces cerevisiae mitochondrial !1ribosomal protein MRP13 KEYWORDS mitochondrion; protein biosynthesis; ribosome FEATURE !$1-47 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$48-339 #product ribosomal protein MRP13 #status predicted !8#label MAT SUMMARY #length 339 #molecular-weight 38988 #checksum 5164 SEQUENCE /// ENTRY JC4278 #type complete TITLE ribosomal protein L41, cytosolic [similarity] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 01-Sep-2000 ACCESSIONS JC4278 REFERENCE JC4277 !$#authors Chan, Y.L.; Olvera, J.; Wool, I.G. !$#journal Biochem. Biophys. Res. Commun. (1995) 214:810-818 !$#title The primary structures of rat ribosomal proteins L4 and L41. !$#cross-references MUID:96024571; PMID:7575549 !$#accession JC4278 !'##molecule_type mRNA !'##residues 1-25 ##label CHA !'##cross-references EMBL:X82550; NID:g575383; PIDN:CAA57899.1; !1PID:g575384 CLASSIFICATION #superfamily rat ribosomal protein L41 KEYWORDS ribosome SUMMARY #length 25 #molecular-weight 3456 #checksum 5742 SEQUENCE /// ENTRY R6BY4B #type complete TITLE ribosomal protein L41.e, cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein D1290; protein YDL133c-a; protein YDL184c; ribosomal protein YL41; ribosomal protein YL47 ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 01-Sep-2000 ACCESSIONS S22246; S22247; S11264; S58733; S67739; S78073 REFERENCE S22246 !$#authors Suzuki, K.; Hashimoto, T.; Otaka, E. !$#journal Curr. Genet. (1990) 17:185-190 !$#title Yeast ribosomal proteins: XI. Molecular analysis of two !1genes encoding YL41, an extremely small and basic ribosomal !1protein, from Saccharomyces cerevisiae. !$#cross-references MUID:90254826; PMID:2187623 !$#accession S22246 !'##molecule_type DNA !'##residues 1-25 ##label SUZ !'##cross-references EMBL:X16066; GSPDB:GN00004; MIPS:YDL133c-a; !1NID:g4819; PIDN:CAA34202.1; PID:g4820 !'##genetics RPL47B !$#accession S22247 !'##molecule_type DNA !'##residues 1-25 ##label SUA !'##cross-references EMBL:X16065; GSPDB:GN00004; MIPS:YDL184c; !1NID:g4817; PIDN:CAA34201.1; PID:g4818 !'##genetics RPL47A REFERENCE S11249 !$#authors Otaka, E.; Higo, K.I.; Itoh, T. !$#journal Mol. Gen. Genet. (1984) 195:544-546 !$#title Yeast ribosomal proteins. VIII. Isolation of two proteins !1and sequence characterization of twenty-four proteins from !1cytoplasmic ribosomes. !$#accession S11264 !'##molecule_type protein !'##residues 1-25 ##label OTA REFERENCE S58730 !$#authors Verhasselt, P.; Voet, M.; Volckaert, G. !$#journal Yeast (1995) 11:961-966 !$#title New open reading frames, one of which is similar to the nifV !1gene of Azotobacter vinelandii, found on a 12.5 kbp fragment !1of chromosome IV of Saccharomyces cerevisiae. !$#cross-references MUID:96021607; PMID:8533471 !$#accession S58733 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-25 ##label VER !'##cross-references EMBL:X83276; NID:g1004294; PIDN:CAA58262.1; !1PID:g1004310 !'##genetics RPL47A !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1994 REFERENCE S67735 !$#authors Volckaert, G.; Verhasselt, P.; Voet, M. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67739 !'##molecule_type DNA !'##residues 1-25 ##label VOL !'##cross-references EMBL:Z74232; GSPDB:GN00004; MIPS:YDL184c; !1NID:g1431298; PIDN:CAA98759.1; PID:g1431299 !'##experimental_source strain S288C !'##genetics RPL47A REFERENCE S67677 !$#authors Saluz, H.P.; Woelfl, S.; Hanemann, V. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S78073 !'##molecule_type DNA !'##residues 1-25 ##label SAL !'##cross-references EMBL:Z74181; NID:g1431202; PIDN:CAA98705.1; !1PID:g1903289; GSPDB:GN00004; MIPS:YDL133c-a !'##genetics RPL47B GENETICS RPL47B !$#gene SGD:RPL47B; YL41B; MIPS:YDL133c-a !'##cross-references MIPS:YDL133c-a; SGD:S0002293 !$#map_position 4L GENETICS RPL47A !$#gene SGD:RPL47A; YL41A; MIPS:YDL184c !'##cross-references MIPS:YDL184c; SGD:S0002343 !$#map_position 4L CLASSIFICATION #superfamily rat ribosomal protein L41 KEYWORDS protein biosynthesis; ribosome FEATURE !$1-25 #product ribosomal protein L41.e #status experimental !8#label MAT SUMMARY #length 25 #molecular-weight 3337 #checksum 5640 SEQUENCE /// ENTRY S15869 #type complete TITLE ribosomal protein LX - Sulfolobus solfataricus ORGANISM #formal_name Sulfolobus solfataricus DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 22-Jun-1999 ACCESSIONS S15869; S29744 REFERENCE S15869 !$#authors Ramirez, C.; Louie, K.A.; Matheson, A.T. !$#journal FEBS Lett. (1991) 284:39-41 !$#title A small basic ribosomal protein from the extreme !1thermophilic archaebacterium Sulfolobus solfataricus that !1has no equivalent in Escherichia coli. !$#cross-references MUID:91285102; PMID:1711982 !$#accession S15869 !'##molecule_type DNA !'##residues 1-71 ##label RAM1 !'##cross-references GB:S38371; NID:g1679904; PIDN:AAB19269.1; !1PID:g232499 !$#accession S29744 !'##molecule_type protein !'##residues 2-45 ##label RAM2 CLASSIFICATION #superfamily ribosomal protein LX KEYWORDS protein biosynthesis; ribosome FEATURE !$2-71 #product ribosomal protein LX #status experimental !8#label MAT SUMMARY #length 71 #molecular-weight 8329 #checksum 7263 SEQUENCE /// ENTRY S30119 #type complete TITLE ribosomal protein MRP17, mitochondrial - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YKL003c; ribosomal protein YmS16 ORGANISM #formal_name Saccharomyces cerevisiae DATE 02-May-1994 #sequence_revision 02-May-1994 #text_change 12-Nov-1999 ACCESSIONS S30119; S37814; S71109; S78033; S17030 REFERENCE S30119 !$#authors Haffter, P.; Fox, T.D. !$#journal Mol. Gen. Genet. (1992) 235:64-73 !$#title Suppression of carboxy-terminal truncations of the yeast !1mitochondrial mRNA-specific translational activator PET122 !1by mutations in two new genes, MRP17 and PET127. !$#cross-references MUID:93062809; PMID:1279374 !$#accession S30119 !'##molecule_type DNA !'##residues 1-131 ##label HAF !'##cross-references EMBL:X58362; NID:g3973; PIDN:CAA41256.1; PID:g3974 REFERENCE S37813 !$#authors Boyer, J.; Pascolo, S.; Richard, G.F.; Ghazvini, M.; !1Colleaux, L.; Thierry, A.; Monnier, A.L.; Dujon, B. !$#submission submitted to the Protein Sequence Database, March 1994 !$#accession S37814 !'##molecule_type DNA !'##residues 1-131 ##label BOY !'##cross-references EMBL:Z28003; NID:g485974; PIDN:CAA81835.1; !1PID:g485975; GSPDB:GN00011; MIPS:YKL003c !'##experimental_source strain S288C REFERENCE S71108 !$#authors Hashida-Okado, T.; Ogawa, A.; Endo, M.; Yasumoto, R.; !1Takesako, K.; Kato, I. !$#journal Mol. Gen. Genet. (1996) 251:236-244 !$#title AUR1, a novel gene conferring aureobasidin resistance on !1Saccharomyces cerevisiae: a study of defective morphologies !1in Aur1p-depleted cells. !$#cross-references MUID:96242157; PMID:8668135 !$#accession S71109 !'##status translation not shown !'##molecule_type DNA !'##residues 1-131 ##label HAS !'##cross-references EMBL:U49090; NID:g1515351; PIDN:AAB06941.1; !1PID:g1515353 REFERENCE S78018 !$#authors Kitakawa, M.; Graack, H.R.; Grohmann, L.; !1Goldschmidt-Reisin, S.; Herfurth, E.; Wittmann-Liebold, B.; !1Nishimura, T.; Isono, K. !$#journal Eur. J. Biochem. (1997) 245:449-456 !$#title Identification and characterization of the genes for !1mitochondrial ribosomal proteins of Saccharomyces !1cerevisiae. !$#cross-references MUID:97296414; PMID:9151978 !$#accession S78033 !'##molecule_type protein !'##residues 1-19 ##label KIT GENETICS !$#gene SGD:MRP17; MIPS:YKL003c !'##cross-references SGD:S0001486; MIPS:YKL003c !$#map_position 11L !$#genome nuclear CLASSIFICATION #superfamily ribosomal protein MRP17 KEYWORDS mitochondrion; protein biosynthesis; ribosome SUMMARY #length 131 #molecular-weight 15020 #checksum 6235 SEQUENCE /// ENTRY S01844 #type complete TITLE fibroin - silkworm ORGANISM #formal_name Bombyx mori #common_name silkworm DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S01844 REFERENCE S01844 !$#authors Mita, K.; Ichimura, S.; Zama, M.; James, T.C. !$#journal J. Mol. Biol. (1988) 203:917-925 !$#title Specific codon usage pattern and its implications on the !1secondary structure of silk fibroin mRNA. !$#cross-references MUID:89094868; PMID:3210244 !$#accession S01844 !'##molecule_type mRNA !'##residues 1-108 ##label MIT !'##cross-references EMBL:X13869; NID:g5873; PIDN:CAA32076.1; !1PID:g930003 CLASSIFICATION #superfamily silk fibroin SUMMARY #length 108 #molecular-weight 7525 #checksum 2220 SEQUENCE /// ENTRY KRSHHD #type complete TITLE keratin high-sulfur matrix protein B2D - sheep ORGANISM #formal_name Ovis orientalis aries, Ovis ammon aries #common_name domestic sheep DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 22-Jun-1999 ACCESSIONS S07911 REFERENCE S07349 !$#authors Powell, B.C.; Sleigh, M.J.; Ward, K.A.; Rogers, G.E. !$#journal Nucleic Acids Res. (1983) 11:5327-5346 !$#title Mammalian keratin gene families: organisation of genes !1coding for the B2 high-sulphur proteins of sheep wool. !$#cross-references MUID:83299218; PMID:6193483 !$#accession S07911 !'##molecule_type DNA !'##residues 1-182 ##label POW !'##cross-references EMBL:X01610; NID:g1295; PIDN:CAA25759.1; PID:g1298 CLASSIFICATION #superfamily keratin high-sulfur matrix protein IIIA KEYWORDS duplication; hair FEATURE !$2-182 #product keratin high-sulfur matrix protein B2D !8#status predicted #label MAT\ !$27-36,37-46,47-56, !$57-66,67-76,77-86 #region duplication SUMMARY #length 182 #molecular-weight 18810 #checksum 5092 SEQUENCE /// ENTRY KRSHHA #type complete TITLE keratin high-sulfur matrix protein B2A - sheep ORGANISM #formal_name Ovis orientalis aries, Ovis ammon aries #common_name domestic sheep DATE 24-Apr-1984 #sequence_revision 12-Apr-1996 #text_change 22-Jun-1999 ACCESSIONS S07910; A02837 REFERENCE S07349 !$#authors Powell, B.C.; Sleigh, M.J.; Ward, K.A.; Rogers, G.E. !$#journal Nucleic Acids Res. (1983) 11:5327-5346 !$#title Mammalian keratin gene families: organisation of genes !1coding for the B2 high-sulphur proteins of sheep wool. !$#cross-references MUID:83299218; PMID:6193483 !$#accession S07910 !'##molecule_type DNA !'##residues 1-172 ##label POW !'##cross-references EMBL:X01610; NID:g1295; PIDN:CAA25757.1; PID:g1296 REFERENCE A02837 !$#authors Elleman, T.C. !$#journal Biochem. J. (1972) 130:833-845 !$#title The amino acid sequence of protein SCMK-B2A from the !1high-sulphur fraction of wool keratin. !$#cross-references MUID:73224964; PMID:4679226 !$#accession A02837 !'##molecule_type protein !'##residues 2-172 ##label ELL !'##experimental_source Lincoln wool !'##note a minor component has 13-Thr, 23-Asn, and 24-Phe COMMENT The keratin products of mammalian epidermal derivatives such !1as wool and hair consist of microfibrils embedded in a rigid !1matrix of other proteins. The matrix proteins include the !1high-sulfur and high-tyrosine keratins, having molecular !1weights of 6-20 kilodaltons, whereas the microfibrils !1contain the larger, low-sulfur keratins (40-56 kilodaltons). CLASSIFICATION #superfamily keratin high-sulfur matrix protein IIIA KEYWORDS acetylated amino end; blocked amino end; duplication; hair FEATURE !$2-172 #product keratin high-sulfur matrix protein B2A !8#status experimental #label MAT\ !$27-76 #region 10-residue repeats\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental SUMMARY #length 172 #molecular-weight 17734 #checksum 8937 SEQUENCE /// ENTRY KRSHHB #type complete TITLE keratin high-sulfur matrix protein B2B - sheep ORGANISM #formal_name Ovis orientalis aries, Ovis ammon aries #common_name domestic sheep DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 16-Aug-1996 ACCESSIONS A02838 REFERENCE A02838 !$#authors Elleman, T.C.; Dopheide, T.A. !$#journal J. Biol. Chem. (1972) 247:3900-3909 !$#title The sequence of SCMK-B2B, a high sulfur protein from wool !1keratin. !$#cross-references MUID:72206034; PMID:4555954 !$#accession A02838 !'##molecule_type protein !'##residues 1-156 ##label ELL !'##experimental_source Lincoln wool !'##note a minor component has 77-Gly COMMENT Most of the sequence shows a repeating pattern of 10 !1residues. CLASSIFICATION #superfamily keratin high-sulfur matrix protein IIIA KEYWORDS acetylated amino end; duplication; hair FEATURE !$1 #modified_site acetylated amino end (Ala) #status !8experimental SUMMARY #length 156 #molecular-weight 16040 #checksum 4593 SEQUENCE /// ENTRY KRSHHC #type complete TITLE keratin high-sulfur matrix protein B2C - sheep ORGANISM #formal_name Ovis orientalis aries, Ovis ammon aries #common_name domestic sheep DATE 24-Apr-1984 #sequence_revision 30-Jun-1991 #text_change 22-Jun-1999 ACCESSIONS S07349; A02839 REFERENCE S07349 !$#authors Powell, B.C.; Sleigh, M.J.; Ward, K.A.; Rogers, G.E. !$#journal Nucleic Acids Res. (1983) 11:5327-5346 !$#title Mammalian keratin gene families: organisation of genes !1coding for the B2 high-sulphur proteins of sheep wool. !$#cross-references MUID:83299218; PMID:6193483 !$#accession S07349 !'##molecule_type DNA !'##residues 1-152 ##label POW !'##cross-references EMBL:X02925; NID:g1299; PIDN:CAA26681.1; PID:g1300 REFERENCE A02839 !$#authors Elleman, T.C. !$#journal Nature New Biol. (1971) 234:148 !$#title Amino-acid sequence of a high-sulphur protein from wool. !$#cross-references MUID:72077141; PMID:5289313 !$#accession A02839 !'##molecule_type protein !'##residues 2-152 ##label ELL !'##experimental_source Lincoln wool CLASSIFICATION #superfamily keratin high-sulfur matrix protein IIIA KEYWORDS acetylated amino end; duplication; hair FEATURE !$2-152 #product keratin high-sulfur matrix protein B2C !8#status experimental #label MAT\ !$27-36,37-46,47-56 #region duplication\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental SUMMARY #length 152 #molecular-weight 15607 #checksum 2151 SEQUENCE /// ENTRY KRSHA3 #type complete TITLE keratin high-sulfur matrix protein IIIA3 - sheep ALTERNATE_NAMES M2.6 protein ORGANISM #formal_name Ovis orientalis aries, Ovis ammon aries #common_name domestic sheep DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 16-Aug-1996 ACCESSIONS A02840 REFERENCE A90269 !$#authors Swart, L.S.; Haylett, T. !$#journal Biochem. J. (1973) 133:641-654 !$#title Studies on the high-sulphur proteins of reduced merino wool. !1Amino acid sequence of protein SCMKB-IIIA3. !$#cross-references MUID:74022242; PMID:4584026 !$#accession A02840 !'##molecule_type protein !'##residues 1-131 ##label SWA !'##experimental_source Merino wool COMMENT Wool and hair consist of microfibrils embedded in a rigid !1matrix of other proteins. The matrix proteins include the !1high-sulfur and high-tyrosine keratins. CLASSIFICATION #superfamily keratin high-sulfur matrix protein IIIA KEYWORDS duplication; hair SUMMARY #length 131 #molecular-weight 14163 #checksum 7333 SEQUENCE /// ENTRY KRGT3J #type complete TITLE keratin high-sulfur matrix protein IIIA3, major component - goat ALTERNATE_NAMES M2.6 protein ORGANISM #formal_name Capra aegagrus hircus #common_name domestic goat DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Aug-1996 ACCESSIONS A92978; A02840 REFERENCE A92978 !$#authors Joubert, F.J. !$#journal J. S. Afr. Chem. Inst. (1975) 28:250-263 !$#title Studies on the high-sulphur proteins of reduced mohair. The !1isolation and the amino acid sequence of protein SCMKB-M2.6. !$#accession A92978 !'##molecule_type protein !'##residues 1-132 ##label JOU !'##experimental_source Angora breed COMMENT Wool and hair consist of microfibrils embedded in a rigid !1matrix of other proteins. The matrix proteins include the !1high-sulfur and high-tyrosine keratins. CLASSIFICATION #superfamily keratin high-sulfur matrix protein IIIA KEYWORDS duplication; hair SUMMARY #length 132 #molecular-weight 14255 #checksum 8661 SEQUENCE /// ENTRY KRGT3M #type complete TITLE keratin high-sulfur matrix protein IIIA3, minor component - goat ALTERNATE_NAMES M2.6 protein ORGANISM #formal_name Capra aegagrus hircus #common_name domestic goat DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Aug-1996 ACCESSIONS B92978; A02840 REFERENCE A92978 !$#authors Joubert, F.J. !$#journal J. S. Afr. Chem. Inst. (1975) 28:250-263 !$#title Studies on the high-sulphur proteins of reduced mohair. The !1isolation and the amino acid sequence of protein SCMKB-M2.6. !$#accession B92978 !'##molecule_type protein !'##residues 1-131 ##label JOU !'##experimental_source Angora breed COMMENT Wool and hair consist of microfibrils embedded in a rigid !1matrix of other proteins. The matrix proteins include the !1high-sulfur and high-tyrosine keratins. CLASSIFICATION #superfamily keratin high-sulfur matrix protein IIIA KEYWORDS duplication; hair SUMMARY #length 131 #molecular-weight 14107 #checksum 6724 SEQUENCE /// ENTRY KRSH3A #type complete TITLE keratin high-sulfur matrix protein IIIA3A - sheep ORGANISM #formal_name Ovis orientalis aries, Ovis ammon aries #common_name domestic sheep DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 16-Aug-1996 ACCESSIONS A02841 REFERENCE A90269 !$#authors Swart, L.S.; Haylett, T. !$#journal Biochem. J. (1973) 133:641-654 !$#title Studies on the high-sulphur proteins of reduced merino wool. !1Amino acid sequence of protein SCMKB-IIIA3. !$#cross-references MUID:74022242; PMID:4584026 !$#accession A02841 !'##molecule_type protein !'##residues 1-130 ##label SWA !'##experimental_source Merino wool CLASSIFICATION #superfamily keratin high-sulfur matrix protein IIIA KEYWORDS duplication; hair SUMMARY #length 130 #molecular-weight 13894 #checksum 5613 SEQUENCE /// ENTRY KRSHH3 #type complete TITLE keratin high-sulfur matrix protein IIIB3 - sheep ORGANISM #formal_name Ovis orientalis aries, Ovis ammon aries #common_name domestic sheep DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 24-Feb-1995 ACCESSIONS A02842 REFERENCE A02842 !$#authors Haylett, T.; Swart, L.S.; Parris, D. !$#journal Biochem. J. (1971) 123:191-200 !$#title Studies on the high-sulphur proteins of reduced Merino wool. !1Amino acid sequence of protein SCMKB-IIIB3. !$#cross-references MUID:72063279; PMID:4942535 !$#accession A02842 !'##molecule_type protein !'##residues 1-98 ##label HAY !'##experimental_source Merino wool COMMENT The keratin products of mammalian epidermal derivatives such !1as wool and hair consist of microfibrils embedded in a rigid !1matrix of other proteins. The matrix proteins include the !1high-sulfur and high-tyrosine keratins, having molecular !1weights of 6-20 kilodaltons, whereas the microfibrils !1contain the larger, low-sulfur keratins (40-56 kilodaltons). CLASSIFICATION #superfamily keratin high-sulfur matrix protein IIIB KEYWORDS acetylated amino end FEATURE !$1 #modified_site acetylated amino end (Ala) #status !8experimental SUMMARY #length 98 #molecular-weight 10474 #checksum 4320 SEQUENCE /// ENTRY KRSHH4 #type complete TITLE keratin high-sulfur matrix protein BIIIB4 - sheep ORGANISM #formal_name Ovis orientalis aries, Ovis ammon aries #common_name domestic sheep DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 20-Apr-2001 ACCESSIONS A02843; I47085 REFERENCE A02843 !$#authors Swart, L.S.; Haylett, T. !$#journal Biochem. J. (1971) 123:201-210 !$#title Studies on the high-sulphur proteins of reduced merino wool. !$#cross-references MUID:72063282; PMID:4942536 !$#accession A02843 !'##molecule_type protein !'##residues 1-98 ##label SWA !'##experimental_source Merino wool REFERENCE I47083 !$#authors Frenkel, M.J.; Powell, B.C.; Ward, K.A.; Sleigh, M.J.; !1Rogers, G.E. !$#journal Genomics (1989) 4:182-191 !$#title The keratin BIIIB gene family: Isolation of cDNA clones and !1structure of a gene and a related pseudogene. !$#cross-references MUID:89290846; PMID:2472352 !$#accession I47085 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 83-98 ##label FRE !'##cross-references GB:M21101; NID:g165920; PIDN:AAA31542.1; !1PID:g165921 CLASSIFICATION #superfamily keratin high-sulfur matrix protein IIIB KEYWORDS acetylated amino end FEATURE !$1 #modified_site acetylated amino end (Ala) #status !8experimental SUMMARY #length 98 #molecular-weight 10472 #checksum 2030 SEQUENCE /// ENTRY KRSHH2 #type complete TITLE keratin high-sulfur matrix protein IIIB2 - sheep ORGANISM #formal_name Ovis orientalis aries, Ovis ammon aries #common_name domestic sheep DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 24-Feb-1995 ACCESSIONS A94304; A90261; A02844 REFERENCE A94304 !$#authors Haylett, T.; Swart, L.S. !$#journal Text. Res. J. (1969) 39:917-929 !$#title Studies on the high-sulfur proteins of reduced merino wool. !1Part III: The amino-acid sequence of protein SCMKB-IIIB2. !$#accession A94304 !'##molecule_type protein !'##residues 1-97 ##label HAY !'##experimental_source Merino wool REFERENCE A90261 !$#authors Elleman, T.C. !$#journal Biochem. J. (1972) 128:1229-1239 !$#title The amino acid sequence of protein SCMK-B2C from the high- !1sulphur fraction of wool keratin. !$#cross-references MUID:73067712; PMID:4678578 !$#accession A90261 !'##molecule_type protein !'##residues 1-97 ##label ELL !'##note 64-Thr was also found CLASSIFICATION #superfamily keratin high-sulfur matrix protein IIIB KEYWORDS acetylated amino end FEATURE !$1 #modified_site acetylated amino end (Ala) #status !8experimental SUMMARY #length 97 #molecular-weight 10289 #checksum 9936 SEQUENCE /// ENTRY KRGTHM #type complete TITLE keratin high-sulfur matrix protein IIIB2 - goat ALTERNATE_NAMES M1.2 protein ORGANISM #formal_name Capra aegagrus hircus #common_name domestic goat DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 24-Feb-1995 ACCESSIONS A02845 REFERENCE A02845 !$#authors Parris, D.; Swart, L.S. !$#journal Biochem. J. (1975) 145:459-467 !$#title Studies on the high-sulphur proteins of reduced mohair. The !1isolation and amino acid sequence of protein SCMKB-M1.2. !$#cross-references MUID:75224628; PMID:1098656 !$#accession A02845 !'##molecule_type protein !'##residues 1-97 ##label PAR !'##experimental_source Angora breed CLASSIFICATION #superfamily keratin high-sulfur matrix protein IIIB KEYWORDS acetylated amino end FEATURE !$1 #modified_site acetylated amino end (Ala) #status !8experimental SUMMARY #length 97 #molecular-weight 10340 #checksum 9209 SEQUENCE /// ENTRY KRSHI6 #type complete TITLE major high-(glycine/tyrosine) kreatin F - sheep ALTERNATE_NAMES component 0.62; HGT keratin F; intermediate-filament-associated protein F ORGANISM #formal_name Ovis orientalis aries, Ovis ammon aries #common_name domestic sheep DATE 24-Apr-1984 #sequence_revision 09-May-1997 #text_change 22-Jun-1999 ACCESSIONS S00031; A23262; A02846 REFERENCE S00031 !$#authors Kuczek, E.S.; Rogers, G.E. !$#journal Eur. J. Biochem. (1987) 166:79-85 !$#title Sheep wool (glycine + tyrosine)-rich keratin genes: a family !1of low sequence homology. !$#cross-references MUID:87246695; PMID:2439340 !$#accession S00031 !'##status not compared with conceptual translation !'##molecule_type DNA; mRNA !'##residues 1-62 ##label KUC !'##cross-references GB:X05639; NID:g1303; PIDN:CAA29126.1; PID:g1304 REFERENCE A23262 !$#authors Kuczek, E.; Rogers, G.E. !$#journal Eur. J. Biochem. (1985) 146:89-93 !$#title Sheep keratins: characterization of cDNA clones for the !1glycine + tyrosine-rich wool proteins using a synthetic !1probe. !$#cross-references MUID:85101390; PMID:2578389 !$#accession A23262 !'##molecule_type mRNA !'##residues 15-50,'F',52-62 ##label KUW !'##cross-references GB:M28304; NID:g165908; PIDN:AAA31536.1; !1PID:g165909 REFERENCE A02846 !$#authors Dopheide, T.A.A. !$#journal Eur. J. Biochem. (1973) 34:120-124 !$#title The primary structure of a protein, component 0.62, rich in !1glycine and aromatic residues, obtained from wool keratin. !$#cross-references MUID:73169377; PMID:4735656 !$#accession A02846 !'##molecule_type protein !'##residues 2-45,'D',47,'GS',50,'F',52-62 ##label DOP !'##experimental_source Merino wool COMMENT The keratin products of mammalian epidermal derivatives such !1as wool and hair consist of microfibrils embedded in a rigid !1matrix of other proteins. The matrix proteins include the !1high-sulfur and high-tyrosine keratins, having molecular !1weights of 6-20 kilodaltons, whereas the microfibrils !1contain the larger, low-sulfur keratins (40-56 kilodaltons). GENETICS !$#gene HGT-F CLASSIFICATION #superfamily high-tyrosine matrix keratin KEYWORDS hair FEATURE !$2-62 #product keratin, high-tyrosine matrix protein F !8#status experimental #label MAT SUMMARY #length 62 #molecular-weight 6730 #checksum 273 SEQUENCE /// ENTRY KREUB #type complete TITLE keratin, feather - emu ORGANISM #formal_name Dromaius novaehollandiae #common_name emu DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 24-Nov-1999 ACCESSIONS A02847 REFERENCE A02847 !$#authors O'Donnell, I.J. !$#journal Aust. J. Biol. Sci. (1973) 26:415-437 !$#title The complete amino acid sequence of a feather keratin from !1emu (Dromaius novae-hollandiae). !$#cross-references MUID:73216154; PMID:4577821 !$#accession A02847 !'##molecule_type protein !'##residues 1-102 ##label ODO !'##experimental_source calamus and rachis of feather COMMENT The sequence shown is that of band 3, one of four components !1obtained after electrophoresis of the reduced and !1carboxymethylated proteins from the feather. CLASSIFICATION #superfamily feather keratin KEYWORDS blocked amino end; epidermis; feather; fibrous protein; !1horn; integument FEATURE !$1 #modified_site blocked amino end (Ser) (probably !8acetylated) #status experimental SUMMARY #length 102 #molecular-weight 10293 #checksum 8652 SEQUENCE /// ENTRY KRCHF1 #type complete TITLE keratin I, feather - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 17-Dec-1982 #sequence_revision 12-Apr-1996 #text_change 22-Jun-1999 ACCESSIONS S06805; A02848 REFERENCE S06805 !$#authors Presland, R.B.; Gregg, K.; Molloy, P.L.; Morris, C.P.; !1Crocker, L.A.; Rogers, G.E. !$#journal J. Mol. Biol. (1989) 209:549-559 !$#title Avian keratin genes. I. A molecular analysis of the !1structure and expression of a group of feather keratin !1genes. !$#cross-references MUID:90064515; PMID:2479754 !$#accession S06805 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-98 ##label PRE REFERENCE A02848 !$#authors Molloy, P.L.; Powell, B.C.; Gregg, K.; Barone, E.D.; Rogers, !1G.E. !$#journal Nucleic Acids Res. (1982) 10:6007-6021 !$#title Organisation of feather keratin genes in the chick genome. !$#cross-references MUID:83064534; PMID:6183643 !$#accession A02848 !'##molecule_type DNA !'##residues 2-98 ##label MOL !'##cross-references GB:J00847; NID:g212229; PIDN:AAA48930.1; !1PID:g212230 !'##note initiator Met not shown !'##note a genomic clone containing five feather keratin genes was !1isolated and the central gene was sequenced GENETICS !$#note keratin gene C CLASSIFICATION #superfamily feather keratin KEYWORDS epidermis; feather; fibrous protein; horn; integument SUMMARY #length 98 #molecular-weight 9972 #checksum 4007 SEQUENCE /// ENTRY KRCHF2 #type complete TITLE keratin II, feather - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 22-Jun-1999 ACCESSIONS A02849 REFERENCE A90988 !$#authors Gregg, K.; Wilton, S.D.; Parry, D.A.D.; Rogers, G.E. !$#journal EMBO J. (1984) 3:175-178 !$#title A comparison of genomic coding sequences for feather and !1scale keratins: structural and evolutionary implications. !$#cross-references MUID:84158528; PMID:6200321 !$#accession A02849 !'##molecule_type DNA !'##residues 1-98 ##label GRE !'##cross-references GB:X00316; NID:g63550; PIDN:CAA25085.1; PID:g63551 CLASSIFICATION #superfamily feather keratin KEYWORDS epidermis; feather; fibrous protein; horn; integument SUMMARY #length 98 #molecular-weight 10031 #checksum 5112 SEQUENCE /// ENTRY KRDKF4 #type complete TITLE keratin B-4, feather - duck ORGANISM #formal_name Anas platyrhynchos #common_name domestic duck DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 04-Nov-1994 ACCESSIONS A24506 REFERENCE A90662 !$#authors Arai, K.M.; Takahashi, R.; Yokote, Y.; Akahane, K. !$#journal Biochim. Biophys. Acta (1986) 873:6-12 !$#title The primary structure of feather keratins from duck (Anas !1platyrhynchos) and pigeon (Columba livia). !$#accession A24506 !'##molecule_type protein !'##residues 1-95 ##label ARA CLASSIFICATION #superfamily feather keratin KEYWORDS blocked amino end; epidermis; feather; fibrous protein; !1integument FEATURE !$1 #modified_site blocked amino end (Ser) (probably !8acetylated) #status experimental SUMMARY #length 95 #molecular-weight 9662 #checksum 5708 SEQUENCE /// ENTRY KRPYF4 #type complete TITLE keratin B-4, feather - pigeon ORGANISM #formal_name Columba livia #common_name domestic pigeon DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 04-Nov-1994 ACCESSIONS B24506 REFERENCE A90662 !$#authors Arai, K.M.; Takahashi, R.; Yokote, Y.; Akahane, K. !$#journal Biochim. Biophys. Acta (1986) 873:6-12 !$#title The primary structure of feather keratins from duck (Anas !1platyrhynchos) and pigeon (Columba livia). !$#accession B24506 !'##molecule_type protein !'##residues 1-95 ##label ARA CLASSIFICATION #superfamily feather keratin KEYWORDS blocked amino end; epidermis; feather; fibrous protein; !1integument FEATURE !$1 #modified_site blocked amino end (Ser) (probably !8acetylated) #status experimental SUMMARY #length 95 #molecular-weight 9719 #checksum 7467 SEQUENCE /// ENTRY KRGLBS #type complete TITLE keratin, feather - silver gull ORGANISM #formal_name Larus novaehollandiae #common_name silver gull DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 24-Nov-1999 ACCESSIONS A02850 REFERENCE A02850 !$#authors O'Donnell, I.J.; Inglis, A.S. !$#journal Aust. J. Biol. Sci. (1974) 27:369-382 !$#title Amino acid sequence of a feather keratin from silver gull !1(Larus novae-hollandiae) and comparison with one from emu !1(Dromaius novae-hollandiae). !$#cross-references MUID:75054009; PMID:4429491 !$#accession A02850 !'##molecule_type protein !'##residues 1-98 ##label ODO !'##experimental_source calamus of wing feathers from a single bird !'##note the sequence of the region 75-83 is tentative due to carry-over !1of residues from preceding sequenator cycles !'##note 4-Asp and 27-Glu may be amidated in the original feather !'##note the alternatives 39-Gln, 48-Thr, 55-Val, 56-Ala, 62-Ala, !163-Ala, 76-Ile, 78-Ser, 80-Tyr, and 89-Tyr were also found CLASSIFICATION #superfamily feather keratin KEYWORDS blocked amino end; epidermis; feather; fibrous protein; !1horn; integument FEATURE !$1 #modified_site blocked amino end (Ala) (probably !8acetylated) #status experimental SUMMARY #length 98 #molecular-weight 9741 #checksum 4110 SEQUENCE /// ENTRY KRCHS #type complete TITLE keratin, scale - chicken ALTERNATE_NAMES beta keratin ORGANISM #formal_name Gallus gallus #common_name chicken DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 22-Jun-1999 ACCESSIONS A02851; B60136; I50168 REFERENCE A90988 !$#authors Gregg, K.; Wilton, S.D.; Parry, D.A.D.; Rogers, G.E. !$#journal EMBO J. (1984) 3:175-178 !$#title A comparison of genomic coding sequences for feather and !1scale keratins: structural and evolutionary implications. !$#cross-references MUID:84158528; PMID:6200321 !$#accession A02851 !'##molecule_type DNA !'##residues 1-155 ##label GRE !'##cross-references GB:X00315; NID:g63548; PIDN:CAA25084.1; PID:g63549 REFERENCE A60136 !$#authors Wilton, S.D.; Crocker, L.A.; Rogers, G.E. !$#journal Biochim. Biophys. Acta (1985) 824:201-208 !$#title Isolation and characterisation of keratin mRNA from the !1scale epidermis of the embryonic chick. !$#cross-references MUID:85122780; PMID:2578818 !$#accession B60136 !'##molecule_type mRNA !'##residues 90-155 ##label WIL !'##cross-references GB:M25642; NID:g212231; PIDN:AAA48931.1; !1PID:g212232 !'##note this mRNA was designated clone CSK12. See entry A60136 for !1clone CSK9 REFERENCE I50168 !$#authors Sawyer, R.H.; Shames, R.B. !$#journal Curr. Top. Dev. Biol. (1987) 22:235-253 !$#title Expression of beta-keratin genes during development of avian !1skin appendages. !$#cross-references MUID:88003561; PMID:2443313 !$#accession I50168 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 137-155 ##label SAW !'##cross-references GB:M28422; NID:g211271; PIDN:AAA48631.1; !1PID:g211272 CLASSIFICATION #superfamily feather keratin KEYWORDS duplication; epidermis; fibrous protein; horn; integument; !1tandem repeat FEATURE !$70-128 #region 13-residue repeats !8(G-G-S-S-L-G-Y-G-G-L-Y-G-Y) SUMMARY #length 155 #molecular-weight 15841 #checksum 5971 SEQUENCE /// ENTRY A24168 #type complete TITLE involucrin - human ORGANISM #formal_name Homo sapiens #common_name man DATE 25-Oct-1987 #sequence_revision 23-Feb-1996 #text_change 22-Jun-1999 ACCESSIONS A24168 REFERENCE A24168 !$#authors Eckert, R.L.; Green, H. !$#journal Cell (1986) 46:583-589 !$#title Structure and evolution of the human involucrin gene. !$#cross-references MUID:86272107; PMID:2873896 !$#accession A24168 !'##molecule_type DNA !'##residues 1-585 ##label ECK !'##cross-references GB:M13902; GB:M13903; NID:g186519; PIDN:AAA59186.1; !1PID:g386834 REFERENCE A57786 !$#authors Simon, M.; Green, H. !$#journal J. Biol. Chem. (1988) 263:18093-18098 !$#title The glutamine residues reactive in !1transglutaminase-catalyzed cross-linking of involucrin. !$#cross-references MUID:89053976; PMID:2461365 !$#contents annotation; transglutaminase-catalyzed cross-link sites of !1intact and fragmented molecule in vitro !$#note in vitro studies of native, soluble involucrin showed almost !1exclusive preference for modification of Gln-496 by !1keratinocyte transglutaminase; proteolytic cleavage in !1vitro, and possibly other modifications in vivo, allows !1modification at a number of other sites COMMENT During the terminal differentiation of keratinocytes, this !1protein from the cytosol becomes cross-linked to membrane !1proteins by transglutaminase and incorporated into an !1insoluble, cross-linked envelope under the plasma membrane. GENETICS !$#gene GDB:IVL !'##cross-references GDB:119355; OMIM:147360 !$#map_position 1q21-1q21 CLASSIFICATION #superfamily involucrin KEYWORDS cornified cell envelope; duplication; epidermis; tandem !1repeat FEATURE !$153-541 #region 10-residue repeats (Q-E-G-Q-[PLV]-[KE]-[LH] !8-[PL]-E-Q)\ !$496 #cross-link isopeptide (Gln) (interchain to Lys !8N6-amino of other proteins) #status experimental SUMMARY #length 585 #molecular-weight 68469 #checksum 6885 SEQUENCE /// ENTRY I37061 #type complete TITLE involucrin M - gorilla ORGANISM #formal_name Gorilla gorilla #common_name gorilla DATE 16-Feb-1996 #sequence_revision 23-Feb-1996 #text_change 22-Jun-1999 ACCESSIONS I37061 REFERENCE I37060 !$#authors Teumer, J.; Green, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:1283-1286 !$#title Divergent evolution of part of the involucrin gene in the !1hominoids: Unique intragenic duplications in the gorilla and !1human. !$#cross-references MUID:89145226; PMID:2919176 !$#accession I37061 !'##status translation not shown !'##molecule_type DNA !'##residues 1-605 ##label RES !'##cross-references GB:M23604; GB:J04499; NID:g340978; PIDN:AAA35472.1; !1PID:g536828 COMMENT During the terminal differentiation of keratinocytes, this !1protein from the cytosol becomes cross-linked to membrane !1proteins by transglutaminase and incorporated into an !1insoluble, cross-linked envelope under the plasma membrane. CLASSIFICATION #superfamily involucrin KEYWORDS cornified cell envelope; duplication; epidermis; tandem !1repeat FEATURE !$153-561 #region 10-residue repeats (Q-E-G-Q-[PLV]-[KE]-[LH] !8-[PL]-E-Q) SUMMARY #length 605 #molecular-weight 70623 #checksum 1559 SEQUENCE /// ENTRY I37060 #type complete TITLE involucrin L - gorilla ORGANISM #formal_name Gorilla gorilla #common_name gorilla DATE 16-Feb-1996 #sequence_revision 23-Feb-1996 #text_change 22-Jun-1999 ACCESSIONS I37060 REFERENCE I37060 !$#authors Teumer, J.; Green, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:1283-1286 !$#title Divergent evolution of part of the involucrin gene in the !1hominoids: Unique intragenic duplications in the gorilla and !1human. !$#cross-references MUID:89145226; PMID:2919176 !$#accession I37060 !'##status translation not shown !'##molecule_type DNA !'##residues 1-635 ##label RES !'##cross-references GB:M23603; GB:J04499; NID:g340977; PIDN:AAA35471.1; !1PID:g536827 COMMENT During the terminal differentiation of keratinocytes, this !1protein from the cytosol becomes cross-linked to membrane !1proteins by transglutaminase and incorporated into an !1insoluble, cross-linked envelope under the plasma membrane. CLASSIFICATION #superfamily involucrin KEYWORDS cornified cell envelope; duplication; epidermis; tandem !1repeat FEATURE !$153-590 #region 10-residue repeats (Q-E-G-Q-[PLV]-[KE]-[LH] !8-[PL]-E-Q) SUMMARY #length 635 #molecular-weight 74081 #checksum 2638 SEQUENCE /// ENTRY I57441 #type complete TITLE involucrin - orangutan ORGANISM #formal_name Pongo pygmaeus #common_name orangutan DATE 31-May-1996 #sequence_revision 23-Aug-1996 #text_change 22-Jun-1999 ACCESSIONS I57441 REFERENCE I57441 !$#authors Djian, P.; Green, H. !$#journal Mol. Biol. Evol. (1989) 6:469-477 !$#title The involucrin gene of the orang-utan: Generation of the !1late region as an evolutionary trend in the hominoids. !$#cross-references MUID:90014143; PMID:2796727 !$#accession I57441 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-835 ##label RES !'##cross-references GB:M25312; NID:g342841; PIDN:AAA36935.1; !1PID:g342842 COMMENT During the terminal differentiation of keratinocytes, this !1protein from the cytosol becomes cross-linked to membrane !1proteins by transglutaminase and incorporated into an !1insoluble, cross-linked envelope under the plasma membrane. CLASSIFICATION #superfamily involucrin KEYWORDS cornified cell envelope; duplication; epidermis; tandem !1repeat FEATURE !$154-793 #region 10-residue repeats SUMMARY #length 835 #molecular-weight 97977 #checksum 6661 SEQUENCE /// ENTRY A40125 #type complete TITLE involucrin - pygmy chimpanzee ORGANISM #formal_name Pan paniscus #common_name pygmy chimpanzee, bonobo DATE 09-Mar-1996 #sequence_revision 23-Aug-1996 #text_change 22-Jun-1999 ACCESSIONS A40125 REFERENCE A34420 !$#authors Djian, P.; Green, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:8447-8451 !$#title Vectorial expansion of the involucrin gene and the !1relatedness of the hominoids. !$#cross-references MUID:90046814; PMID:2813403 !$#accession A40125 !'##status translation not shown !'##molecule_type DNA !'##residues 1-560 ##label DJI !'##cross-references GB:M26514; NID:g176809; PIDN:AAA35422.1; !1PID:g176810 COMMENT During the terminal differentiation of keratinocytes, this !1protein from the cytosol becomes cross-linked to membrane !1proteins by transglutaminase and incorporated into an !1insoluble, cross-linked envelope under the plasma membrane. GENETICS !$#introns #status absent CLASSIFICATION #superfamily involucrin KEYWORDS cornified cell envelope; duplication; epidermis; tandem !1repeat FEATURE !$148-519 #region 10-residue repeats SUMMARY #length 560 #molecular-weight 65479 #checksum 6245 SEQUENCE /// ENTRY I37062 #type complete TITLE involucrin S - gorilla ORGANISM #formal_name Gorilla gorilla #common_name gorilla DATE 16-Feb-1996 #sequence_revision 23-Feb-1996 #text_change 22-Jun-1999 ACCESSIONS I37062 REFERENCE I37060 !$#authors Teumer, J.; Green, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:1283-1286 !$#title Divergent evolution of part of the involucrin gene in the !1hominoids: Unique intragenic duplications in the gorilla and !1human. !$#cross-references MUID:89145226; PMID:2919176 !$#accession I37062 !'##status translation not shown !'##molecule_type DNA !'##residues 1-495 ##label RES !'##cross-references GB:M23605; GB:J04499; NID:g340979; PIDN:AAA35473.1; !1PID:g536829 COMMENT During the terminal differentiation of keratinocytes, this !1protein from the cytosol becomes cross-linked to membrane !1proteins by transglutaminase and incorporated into an !1insoluble, cross-linked envelope under the plasma membrane. CLASSIFICATION #superfamily involucrin KEYWORDS cornified cell envelope; duplication; epidermis; tandem !1repeat FEATURE !$153-451 #region 10-residue repeats (Q-E-G-Q-[PLV]-[KE]-[LH] !8-[PL]-E-Q) SUMMARY #length 495 #molecular-weight 57643 #checksum 3532 SEQUENCE /// ENTRY I37037 #type complete TITLE involucrin - common gibbon ORGANISM #formal_name Hylobates lar #common_name common gibbon, white-handed gibbon DATE 16-Feb-1996 #sequence_revision 23-Feb-1996 #text_change 22-Jun-1999 ACCESSIONS I37037 REFERENCE I37037 !$#authors Djian, P.; Green, H. !$#journal Mol. Biol. Evol. (1990) 7:220-227 !$#title The involucrin gene of the gibbon: The middle region shared !1by the hominoids. !$#cross-references MUID:90294724; PMID:2359362 !$#accession I37037 !'##status translation not shown !'##molecule_type DNA !'##residues 1-522 ##label RES !'##cross-references GB:M35447; NID:g177018; PIDN:AAA35456.1; !1PID:g177019 COMMENT During the terminal differentiation of keratinocytes, this !1protein from the cytosol becomes cross-linked to membrane !1proteins by transglutaminase and incorporated into an !1insoluble, cross-linked envelope under the plasma membrane. CLASSIFICATION #superfamily involucrin KEYWORDS cornified cell envelope; duplication; epidermis; tandem !1repeat FEATURE !$153-478 #region 10-residue repeats (Q-E-G-Q-[PLV]-[KE]-[LH] !8-[PL]-E-Q) SUMMARY #length 522 #molecular-weight 61046 #checksum 5431 SEQUENCE /// ENTRY I36911 #type complete TITLE involucrin L - douroucouli ORGANISM #formal_name Aotus trivirgatus #common_name douroucouli, night monkey, owl monkey DATE 16-Feb-1996 #sequence_revision 23-Feb-1996 #text_change 22-Jun-1999 ACCESSIONS I36911 REFERENCE I36911 !$#authors Tseng, H.; Green, H. !$#journal Mol. Biol. Evol. (1989) 6:460-468 !$#title The involucrin gene of the owl monkey: origin of the early !1region. !$#cross-references MUID:90014142; PMID:2507864 !$#accession I36911 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-544 ##label RES !'##cross-references GB:M25313; NID:g176557; PIDN:AAA35375.1; !1PID:g176558 COMMENT During the terminal differentiation of keratinocytes, this !1protein from the cytosol becomes cross-linked to membrane !1proteins by transglutaminase and incorporated into an !1insoluble, cross-linked envelope under the plasma membrane. CLASSIFICATION #superfamily involucrin KEYWORDS cornified cell envelope; duplication; epidermis; tandem !1repeat FEATURE !$153-501 #region 10-residue repeats (Q-E-G-Q-[PLV]-[KE]-[LH] !8-[PL]-E-Q) SUMMARY #length 544 #molecular-weight 63927 #checksum 3259 SEQUENCE /// ENTRY I36912 #type fragment TITLE involucrin S - douroucouli (fragment) ORGANISM #formal_name Aotus trivirgatus #common_name douroucouli, night monkey, owl monkey DATE 16-Feb-1996 #sequence_revision 23-Feb-1996 #text_change 22-Jun-1999 ACCESSIONS I36912 REFERENCE I36911 !$#authors Tseng, H.; Green, H. !$#journal Mol. Biol. Evol. (1989) 6:460-468 !$#title The involucrin gene of the owl monkey: origin of the early !1region. !$#cross-references MUID:90014142; PMID:2507864 !$#accession I36912 !'##molecule_type DNA !'##residues 1-298 ##label RES !'##cross-references GB:M25314; NID:g176559; PIDN:AAA35376.1; !1PID:g176560 COMMENT During the terminal differentiation of keratinocytes, this !1protein from the cytosol becomes cross-linked to membrane !1proteins by transglutaminase and incorporated into an !1insoluble, cross-linked envelope under the plasma membrane. CLASSIFICATION #superfamily involucrin KEYWORDS cornified cell envelope; duplication; epidermis; tandem !1repeat SUMMARY #length 298 #checksum 1342 SEQUENCE /// ENTRY A57783 #type complete TITLE involucrin - cotton-top tamarin ORGANISM #formal_name Saguinus oedipus #common_name cotton-top tamarin DATE 16-Feb-1996 #sequence_revision 23-Feb-1996 #text_change 22-Jun-1999 ACCESSIONS A57783 REFERENCE A57783 !$#authors Phillips, M.A.; Rice, R.H.; Djian, P.; Green, H. !$#journal Mol. Biol. Evol. (1991) 8:579-591 !$#title The involucrin genes of the white-fronted capuchin and !1cottontop tamarin: The platyrrhine middle region. !$#cross-references MUID:92114750; PMID:1766360 !$#accession A57783 !'##molecule_type DNA !'##residues 1-493 ##label RES !'##cross-references GB:M67477; NID:g343313; PIDN:AAA36950.1; !1PID:g343314 COMMENT During the terminal differentiation of keratinocytes, this !1protein from the cytosol becomes cross-linked to membrane !1proteins by transglutaminase and incorporated into an !1insoluble, cross-linked envelope under the plasma membrane. GENETICS !$#introns #status absent CLASSIFICATION #superfamily involucrin KEYWORDS cornified cell envelope; duplication; epidermis; tandem !1repeat FEATURE !$152-451 #region 10-residue repeats (Q-E-G-Q-[PLV]-[KE]-[LH] !8-[PL]-E-Q) SUMMARY #length 493 #molecular-weight 57920 #checksum 3873 SEQUENCE /// ENTRY I36930 #type complete TITLE involucrin - white-fronted capuchin ORGANISM #formal_name Cebus albifrons #common_name white-fronted capuchin, pale-fronted capuchin DATE 16-Feb-1996 #sequence_revision 23-Feb-1996 #text_change 22-Jun-1999 ACCESSIONS I36930 REFERENCE A57783 !$#authors Phillips, M.A.; Rice, R.H.; Djian, P.; Green, H. !$#journal Mol. Biol. Evol. (1991) 8:579-591 !$#title The involucrin genes of the white-fronted capuchin and !1cottontop tamarin: The platyrrhine middle region. !$#cross-references MUID:92114750; PMID:1766360 !$#accession I36930 !'##molecule_type DNA !'##residues 1-428 ##label RES !'##cross-references GB:M67478; NID:g176629; PIDN:AAA35405.1; !1PID:g176630 COMMENT During the terminal differentiation of keratinocytes, this !1protein from the cytosol becomes cross-linked to membrane !1proteins by transglutaminase and incorporated into an !1insoluble, cross-linked envelope under the plasma membrane. GENETICS !$#introns #status absent CLASSIFICATION #superfamily involucrin KEYWORDS cornified cell envelope; duplication; epidermis; tandem !1repeat FEATURE !$153-386 #region 10-residue repeats (Q-E-G-Q-[PLV]-[KE]-[LH] !8-[PL]-E-Q) SUMMARY #length 428 #molecular-weight 50126 #checksum 9216 SEQUENCE /// ENTRY A43704 #type complete TITLE involucrin - western tarsier ORGANISM #formal_name Tarsius bancanus #common_name western tarsier DATE 20-Feb-1993 #sequence_revision 23-Feb-1996 #text_change 22-Jun-1999 ACCESSIONS A43704 REFERENCE A43704 !$#authors Djian, P.; Green, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:5321-5325 !$#title Involucrin gene of tarsioids and other primates: !1alternatives in evolution of the segment of repeats. !$#cross-references MUID:91271381; PMID:1905021 !$#accession A43704 !'##status translation not shown !'##molecule_type DNA !'##residues 1-387 ##label DJI !'##cross-references GB:M65124; NID:g343451; PIDN:AAA36960.1; !1PID:g343452 COMMENT During the terminal differentiation of keratinocytes, this !1protein from the cytosol becomes cross-linked to membrane !1proteins by transglutaminase and incorporated into an !1insoluble, cross-linked envelope under the plasma membrane. CLASSIFICATION #superfamily involucrin KEYWORDS cornified cell envelope; duplication; epidermis; tandem !1repeat SUMMARY #length 387 #molecular-weight 45077 #checksum 6132 SEQUENCE /// ENTRY A43710 #type complete TITLE involucrin - thick-tailed bush baby ORGANISM #formal_name Galago crassicaudatus, Otolemur crassicaudatus #common_name thick-tailed bush baby DATE 20-Feb-1993 #sequence_revision 23-Feb-1996 #text_change 22-Jun-1999 ACCESSIONS A43710 REFERENCE A43710 !$#authors Phillips, M.; Djian, P.; Green, H. !$#journal J. Biol. Chem. (1990) 265:7804-7807 !$#title The involucrin gene of the galago. Existence of a correction !1process acting on its segment of repeats. !$#cross-references MUID:90243643; PMID:2335506 !$#accession A43710 !'##status translation not shown !'##molecule_type DNA !'##residues 1-384 ##label PHI !'##cross-references EMBL:J05437; NID:g176996; PIDN:AAA35450.1; !1PID:g176997 COMMENT During the terminal differentiation of keratinocytes, this !1protein from the cytosol becomes cross-linked to membrane !1proteins by transglutaminase and incorporated into an !1insoluble, cross-linked envelope under the plasma membrane. CLASSIFICATION #superfamily involucrin KEYWORDS cornified cell envelope; duplication; epidermis; tandem !1repeat SUMMARY #length 384 #molecular-weight 44060 #checksum 1460 SEQUENCE /// ENTRY A43733 #type complete TITLE involucrin - ring-tailed lemur ORGANISM #formal_name Lemur catta #common_name ring-tailed lemur DATE 20-Feb-1993 #sequence_revision 23-Feb-1996 #text_change 22-Jun-1999 ACCESSIONS A43733 REFERENCE A43733 !$#authors Tseng, H.; Green, H. !$#journal Cell (1988) 54:491-496 !$#title Remodeling of the involucrin gene during primate evolution. !$#cross-references MUID:88295123; PMID:3401924 !$#accession A43733 !'##status translation not shown !'##molecule_type DNA !'##residues 1-450 ##label TSE !'##cross-references EMBL:M21864; NID:g340629; PIDN:AAA36826.1; !1PID:g340630 COMMENT During the terminal differentiation of keratinocytes, this !1protein from the cytosol becomes cross-linked to membrane !1proteins by transglutaminase and incorporated into an !1insoluble, cross-linked envelope under the plasma membrane. CLASSIFICATION #superfamily involucrin KEYWORDS cornified cell envelope; duplication; epidermis; tandem !1repeat FEATURE !$80-295 #region 13-residue repeats SUMMARY #length 450 #molecular-weight 50445 #checksum 4455 SEQUENCE /// ENTRY A49377 #type complete TITLE involucrin - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 02-Jul-1996 #sequence_revision 23-Aug-1996 #text_change 22-Jun-1999 ACCESSIONS A49377 REFERENCE A49377 !$#authors Djian, P.; Phillips, M.; Easley, K.; Huang, E.; Simon, M.; !1Rice, R.H.; Green, H. !$#journal Mol. Biol. Evol. (1993) 10:1136-1149 !$#title The involucrin genes of the mouse and the rat: study of !1their shared repeats. !$#cross-references MUID:94104476; PMID:8277848 !$#accession A49377 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-467 ##label RES !'##cross-references GB:L28819; NID:g454418; PIDN:AAA39330.1; !1PID:g454419 COMMENT During the terminal differentiation of keratinocytes, this !1protein from the cytosol becomes cross-linked to membrane !1proteins by transglutaminase and incorporated into an !1insoluble, cross-linked envelope under the plasma membrane. CLASSIFICATION #superfamily involucrin KEYWORDS cornified cell envelope; duplication; epidermis; tandem !1repeat SUMMARY #length 467 #molecular-weight 54919 #checksum 5202 SEQUENCE /// ENTRY I61106 #type complete TITLE involucrin - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 02-Aug-1996 #sequence_revision 23-Aug-1996 #text_change 22-Jun-1999 ACCESSIONS I61106 REFERENCE A49377 !$#authors Djian, P.; Phillips, M.; Easley, K.; Huang, E.; Simon, M.; !1Rice, R.H.; Green, H. !$#journal Mol. Biol. Evol. (1993) 10:1136-1149 !$#title The involucrin genes of the mouse and the rat: study of !1their shared repeats. !$#cross-references MUID:94104476; PMID:8277848 !$#accession I61106 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-568 ##label RES !'##cross-references GB:L28818; NID:g454427; PIDN:AAA41445.1; !1PID:g454428 COMMENT During the terminal differentiation of keratinocytes, this !1protein from the cytosol becomes cross-linked to membrane !1proteins by transglutaminase and incorporated into an !1insoluble, cross-linked envelope under the plasma membrane. CLASSIFICATION #superfamily involucrin KEYWORDS cornified cell envelope; duplication; epidermis; tandem !1repeat SUMMARY #length 568 #molecular-weight 67021 #checksum 9249 SEQUENCE /// ENTRY I46207 #type complete TITLE involucrin - dog ORGANISM #formal_name Canis lupus familiaris #common_name dog DATE 16-Aug-1996 #sequence_revision 23-Aug-1996 #text_change 22-Jun-1999 ACCESSIONS I46207 REFERENCE I46207 !$#authors Tseng, H.; Green, H. !$#journal Mol. Biol. Evol. (1990) 7:293-302 !$#title The involucrin genes of pig and dog: comparison of their !1segments of repeats with those of prosimians and higher !1primates. !$#cross-references MUID:90348475; PMID:2385171 !$#accession I46207 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-285 ##label TSE !'##cross-references GB:M34442; NID:g163980; PIDN:AAA30853.1; !1PID:g163981 COMMENT During the terminal differentiation of keratinocytes, this !1protein from the cytosol becomes cross-linked to membrane !1proteins by transglutaminase and incorporated into an !1insoluble, cross-linked envelope under the plasma membrane. CLASSIFICATION #superfamily involucrin KEYWORDS cornified cell envelope; duplication; epidermis; tandem !1repeat SUMMARY #length 285 #molecular-weight 33384 #checksum 2739 SEQUENCE /// ENTRY A38743 #type complete TITLE loricrin - human ORGANISM #formal_name Homo sapiens #common_name man DATE 20-Sep-1991 #sequence_revision 23-Aug-1996 #text_change 20-Oct-2000 ACCESSIONS A38743; A43410 REFERENCE A38743 !$#authors Hohl, D.; Mehrel, T.; Lichti, U.; Turner, M.L.; Roop, D.R.; !1Steinert, P.M. !$#journal J. Biol. Chem. (1991) 266:6626-6636 !$#title Characterization of human loricrin. Structure and function !1of a new class of epidermal cell envelope proteins. !$#cross-references MUID:91177926; PMID:2007607 !$#accession A38743 !'##molecule_type mRNA !'##residues 1-316 ##label HOH !'##cross-references GB:M61120; NID:g187184; PIDN:AAA36180.1; !1PID:g187185 !'##note translation of Met-1 is not shown REFERENCE A43410 !$#authors Yoneda, K.; Hohl, D.; McBride, O.W.; Wang, M.; Cehrs, K.U.; !1Idler, W.W.; Steinert, P.M. !$#journal J. Biol. Chem. (1992) 267:18060-18066 !$#title The human loricrin gene. !$#cross-references MUID:92388173; PMID:1355480 !$#accession A43410 !'##molecule_type DNA !'##residues 2-151,'C',153-232,'C',234-316 ##label YON !'##cross-references GB:M94077; NID:g187186; PIDN:AAA36181.1; !1PID:g187187 !'##note sequence inconsistent with the nucleotide translation !'##note sequence extracted from NCBI backbone (NCBIN:112880, !1NCBIP:112882) COMMENT During the terminal differentiation of epidermal (stratum !1corneum) cell, this protein from the cytosol becomes !1cross-linked to membrane proteins by transglutaminase and !1incorporated into an insoluble, cross-linked envelope (the !1cornified cell envelope) under the plasma membrane. GENETICS !$#gene GDB:LOR !'##cross-references GDB:132049; OMIM:152445 !$#map_position 1q21-1q21 !$#introns #status absent !$#note polymorphisms include variants of different lengths CLASSIFICATION #superfamily loricrin KEYWORDS cornified cell envelope; disulfide bond; duplication; !1epidermis; tandem repeat FEATURE !$89 #cross-link isopeptide (Lys) (interchain to Gln-154) !8(partial) #status experimental\ !$89 #cross-link isopeptide (Lys) (interchain to Gln-220) !8(partial) #status experimental\ !$154 #cross-link isopeptide (Gln) (interchain to Lys-89) !8#status experimental\ !$216 #cross-link isopeptide (Gln) (interchain to Lys-316) !8#status experimental\ !$220 #cross-link isopeptide (Gln) (interchain to Lys-89) !8#status experimental\ !$316 #cross-link isopeptide (Lys) (interchain to Gln-216) !8(partial) #status experimental SUMMARY #length 316 #molecular-weight 26033 #checksum 2081 SEQUENCE /// ENTRY A45973 #type complete TITLE trichohyalin - human ORGANISM #formal_name Homo sapiens #common_name man DATE 03-May-1994 #sequence_revision 01-Mar-1996 #text_change 22-Jun-1999 ACCESSIONS A45973 REFERENCE A45973 !$#authors Lee, S.C.; Kim, I.G.; Marekov, L.N.; O'Keefe, E.J.; Parry, !1D.A.D.; Steinert, P.M. !$#journal J. Biol. Chem. (1993) 268:12164-12176 !$#title The structure of human trichohyalin. Potential multiple !1roles as a functional EF-hand-like calcium-binding protein, !1a cornified cell envelope precursor, and an intermediate !1filament-associated (cross-linking) protein. !$#cross-references MUID:93280194; PMID:7685034 !$#accession A45973 !'##molecule_type DNA !'##residues 1-1898 ##label LEE !'##cross-references GB:L09190; NID:g292835; PIDN:AAA65582.1; !1PID:g292836 !'##note authors translated the codon AGG for residue 1714 as Pro COMMENT Trichohyalin is a protein of the medulla of the hair and of !1the inner root sheath cells of the hair follicle. It !1contains an extraordinary concentration of charged residues !1and glutamine. Covalent modifications to this protein !1include conversion of arginine to citrulline and !1transglutaminase-catalysed isopeptide bond cross-linking !1between glutamine and lysine side chains. GENETICS !$#gene GDB:THH !'##cross-references GDB:136223; OMIM:190370 !$#map_position 1q21-1q21 CLASSIFICATION #superfamily trichohyalin; calmodulin repeat homology KEYWORDS calcium binding; citrulline; EF hand; hair; tandem repeat FEATURE !$49-81 #domain calmodulin repeat homology #label EF2 SUMMARY #length 1898 #molecular-weight 247219 #checksum 4094 SEQUENCE /// ENTRY A40691 #type complete TITLE trichohyalin - sheep ORGANISM #formal_name Ovis orientalis aries, Ovis ammon aries #common_name domestic sheep DATE 21-Sep-1993 #sequence_revision 01-Mar-1996 #text_change 22-Jun-1999 ACCESSIONS A40691; A34209; S32633 REFERENCE A40691 !$#authors Fietz, M.J.; McLaughlan, C.J.; Campbell, M.T.; Rogers, G.E. !$#journal J. Cell Biol. (1993) 121:855-865 !$#title Analysis of the sheep trichohyalin gene: potential !1structural and calcium-binding roles of trichohyalin in the !1hair follicle. !$#cross-references MUID:93260018; PMID:7684041 !$#accession A40691 !'##molecule_type DNA !'##residues 1-1549 ##label FIE !'##cross-references EMBL:Z18361; NID:g295940; PIDN:CAA79165.1; !1PID:g295941 !'##note sequence extracted from NCBI backbone (NCBIP:132511) REFERENCE A34209 !$#authors Fietz, M.J.; Presland, R.B.; Rogers, G.E. !$#journal J. Cell Biol. (1990) 110:427-436 !$#title The cDNA-deduced amino acid sequence for trichohyalin, a !1differentiation marker in the hair follicle, contains a 23 !1amino acid repeat. !$#cross-references MUID:90130632; PMID:2298812 !$#accession A34209 !'##molecule_type mRNA !'##residues 1016-1151,1205-1257,1281-1398,'G',1400-1549 ##label FI2 !'##cross-references GB:X51695; NID:g1827; PIDN:CAA35992.1; PID:g1828 COMMENT Trichohyalin is a protein of the medulla of the hair and of !1the inner root sheath cells of the hair follicle. It !1contains an extraordinary concentration of charged residues !1and glutamine. Covalent modifications to this protein !1include conversion of arginine to citrulline and !1transglutaminase-catalysed isopeptide bond cross-linking !1between glutamine and lysine side chains. GENETICS !$#introns 46/3 !$#note single copy gene CLASSIFICATION #superfamily trichohyalin; calmodulin repeat homology KEYWORDS calcium binding; citrulline; EF hand; hair; tandem repeat FEATURE !$49-81 #domain calmodulin repeat homology #label EF2\ !$387-851 #region 28-residue repeats\ !$886-1519 #region 23-residue repeats SUMMARY #length 1549 #molecular-weight 201172 #checksum 7325 SEQUENCE /// ENTRY S28589 #type complete TITLE trichohyalin - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 12-Mar-1993 #sequence_revision 01-Mar-1996 #text_change 22-Jun-1999 ACCESSIONS S28589 REFERENCE S28589 !$#authors Fietz, M.J.; Rogers, G.E. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Examination of the gene encoding rabbit trichohyalin. !$#accession S28589 !'##molecule_type DNA !'##residues 1-1407 ##label FIE !'##cross-references EMBL:Z19092; NID:g1746; PIDN:CAA79519.1; PID:g1747 COMMENT Trichohyalin is a protein of the medulla of the hair and of !1the inner root sheath cells of the hair follicle. It !1contains an extraordinary concentration of charged residues !1and glutamine. Covalent modifications to this protein !1include conversion of arginine to citrulline and !1transglutaminase-catalysed isopeptide bond cross-linking !1between glutamine and lysine side chains. GENETICS !$#introns 46/3 CLASSIFICATION #superfamily trichohyalin; calmodulin repeat homology KEYWORDS calcium binding; citrulline; EF hand; hair; tandem repeat FEATURE !$49-81 #domain calmodulin repeat homology #label EF2 SUMMARY #length 1407 #molecular-weight 183780 #checksum 7862 SEQUENCE /// ENTRY CGHU1S #type complete TITLE collagen alpha 1(I) chain precursor - human ALTERNATE_NAMES procollagen alpha 1(I) chain ORGANISM #formal_name Homo sapiens #common_name man DATE 12-Aug-1981 #sequence_revision 04-Oct-1996 #text_change 31-Dec-2000 ACCESSIONS I60114; S01143; A93335; I55254; A39943; I55237; A35233; !1S09400; B90567; S11372; I55342; A92069; S15989; I52905; !1A90476; A22161; A35336; I54365; A47426; B47426; C47426; !1D47426; E47426; I55269; A29439; I53466; A02852; I37247 REFERENCE I60114 !$#authors D'Alessio, M.; Bernard, M.; Pretorius, P.J.; de Wet, W.; !1Ramirez, F.; Pretorious, P.J. !$#journal Gene (1988) 67:105-115 !$#title Complete nucleotide sequence of the region encompassing the !1first twenty-five exons of the human pro alpha 1(I) collagen !1gene (COL1A1). !$#cross-references MUID:88329734; PMID:2843432 !$#accession I60114 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-369,'L',371-589 ##label DAL !'##cross-references GB:M20789; NID:g179593; PIDN:AAB59373.1; !1PID:g179594 REFERENCE S01143 !$#authors Tromp, G.; Kuivaniemi, H.; Stacey, A.; Shikata, H.; Baldwin, !1C.T.; Jaenisch, R.; Prockop, D.J. !$#journal Biochem. J. (1988) 253:919-922 !$#title Structure of a full-length cDNA clone for the prepro-alpha-1 !1(I) chain of human type I procollagen. !$#cross-references MUID:89025644; PMID:3178743 !$#accession S01143 !'##molecule_type mRNA !'##residues 1-472 ##label TRO !'##cross-references EMBL:X07884; NID:g30015; PIDN:CAA30731.1; !1PID:g30016; GB:M36546; NID:g190227; PID:g553615 !'##note submitted to the EMBL/GenBank/DDBJ databases by Prockop, D.J., !113-JUN-1988 REFERENCE A93335 !$#authors Chu, M.L.; de Wet, W.; Bernard, M.; Ding, J.F.; Morabito, !1M.; Myers, J.; Williams, C.; Ramirez, F. !$#journal Nature (1984) 310:337-340 !$#title Human proalpha1(I) collagen gene structure reveals !1evolutionary conservation of a pattern of introns and exons. !$#cross-references MUID:84270697; PMID:6462220 !$#accession A93335 !'##molecule_type DNA !'##residues 1-58,'Q',60-181 ##label CHU !'##cross-references EMBL:X00820; NID:g35657; PIDN:CAA25394.1; !1PID:g35658 REFERENCE I55254 !$#authors Rossouw, C.M.S.; Vergeer, W.P.; du Plooy, S.J.; Bernard, !1M.P.; Ramirez, F.; de Wet, W.J. !$#journal J. Biol. Chem. (1987) 262:15151-15157 !$#title DNA sequences in the first intron of the human pro-alpha 1 !1(I) collagen gene enhance transcription. !$#cross-references MUID:88033098; PMID:2822714 !$#accession I55254 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-45 ##label ROS !'##cross-references GB:J02829; NID:g180387; PIDN:AAA51993.1; !1PID:g180388 REFERENCE A39943 !$#authors Bornstein, P.; McKay, J.; Morishima, J.K.; Devarayalu, S.; !1Gelinas, R.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:8869-8873 !$#title Regulatory elements in the first intron contribute to !1transcriptional control of the human alpha1(I) collagen !1gene. !$#cross-references MUID:88097389; PMID:3480516 !$#accession A39943 !'##molecule_type DNA !'##residues 1-34 ##label BOR !'##cross-references GB:J03559; NID:g180876; PIDN:AAA52052.1; !1PID:g553238 REFERENCE I55237 !$#authors Chu, M.L.; de Wet, W.; Bernard, M.; Ramirez, F. !$#journal J. Biol. Chem. (1985) 260:2315-2320 !$#title Fine structural analysis of the human pro-alpha 1 (I) !1collagen gene. Promoter structure, AluI repeats, and !1polymorphic transcripts. !$#cross-references MUID:85130970; PMID:2857713 !$#accession I55237 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-34 ##label CH2 !'##cross-references GB:M10627; NID:g180383; PIDN:AAA51992.1; !1PID:g553226 REFERENCE A35233 !$#authors Wirtz, M.K.; Keene, D.R.; Hori, H.; Glanville, R.W.; !1Steinmann, B.; Rao, V.H.; Hollister, D.W. !$#journal J. Biol. Chem. (1990) 265:6312-6317 !$#title In vivo and in vitro noncovalent association of excised !1alpha1(I) amino-terminal propeptides with mutant pNalpha2(I) !1collagen chains in native mutant collagen in a case of !1Ehlers-Danlos syndrome, type VII. !$#cross-references MUID:90202908; PMID:2318855 !$#accession A35233 !'##molecule_type protein !'##residues 33-52 ##label WIR !'##note this propeptide fragment remained non-covalently bound to a !1defective, uncleaved alpha 2(I) propeptide REFERENCE S09400 !$#authors Weil, D.; d'Alessio, M.; Ramirez, F.; de Wet, W.; Cole, !1W.G.; Chan, D.; Bateman, J.F. !$#journal EMBO J. (1989) 8:1705-1710 !$#title A base substitution in the exon of a collagen gene causes !1alternative splicing and generates a structurally abnormal !1polypeptide in a patient with Ehlers-Danlos syndrome type !1VII. !$#cross-references MUID:89356643; PMID:2767050 !$#accession S09400 !'##molecule_type mRNA !'##residues 156-183 ##label WEI REFERENCE A90567 !$#authors Click, E.M.; Bornstein, P. !$#journal Biochemistry (1970) 9:4699-4706 !$#title Isolation and characterization of the cyanogen bromide !1peptides from the alpha1 and alpha2 chains of human skin !1collagen. !$#cross-references MUID:71038625; PMID:5529814 !$#contents CNBr0-1, CNBr2, CNBr4, CNBr5 !$#accession B90567 !'##molecule_type protein !'##residues 162-198,'Z',200-201,'Z',203-206,'Z',208-209,'Z',211-228, !1'B',230,'BB',233,'Z',235-242,'Z',244-249,'Z',251-273,'B', !1275-278,'B',280-287,'Z',289-293,'ZB',296-299,'Z',301 ##label !1CLI !'##experimental_source skin !'##note evidence for 170-allysine REFERENCE S11372 !$#authors Baetge, B.; Notbohm, H.; Diebold, J.; Lehmann, H.; Bodo, M.; !1Deutzmann, R.; Mueller, P.K. !$#journal Eur. J. Biochem. (1990) 192:153-159 !$#title A critical crosslink region in human-bone-derived collagen !1type I. Specific cleavage site at residue Leu95. !$#cross-references MUID:90382436; PMID:2169412 !$#accession S11372 !'##molecule_type protein !'##residues 175-187;274-287,'P',289 ##label BAE !'##note sequence of collagen alpha 1(S)(I) isolated from bone after !1pepsin digestion REFERENCE I55342 !$#authors Deak, S.B.; Scholz, P.M.; Amenta, P.S.; Constantinou, C.D.; !1Levi-Minzi, S.A.; Gonzalez-Lavin, L.; Mackenzie, J.W. !$#journal J. Biol. Chem. (1991) 266:21827-21832 !$#title The substitution of arginine for glycine 85 of the alpha 1 !1(I) procollagen chain results in mild osteogenesis !1imperfecta. The mutation provides direct evidence for three !1discrete domains of cooperative melting of intact type I !1collagen. !$#cross-references MUID:92042092; PMID:1718984 !$#accession I55342 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 258-268;1347-1357 ##label DEA !'##cross-references GB:S67495; NID:g239007; PIDN:AAB20350.1; !1PID:g239008 !'##note sequences from the 5' and 3' ends only are shown; mutant !1sequence 263-Arg reported from patient with mild !1osteogenesis imperfecta REFERENCE A92069 !$#authors Morgan, P.H.; Jacobs, H.G.; Segrest, J.P.; Cunningham, L.W. !$#journal J. Biol. Chem. (1970) 245:5042-5048 !$#title Comparative study of glycopeptides derived from selected !1vertebrate collagens. A possible role of the carbohydrate in !1fibril formation. !$#cross-references MUID:71001508; PMID:4319110 !$#accession A92069 !'##molecule_type protein !'##residues 263-268 ##label MOR !'##experimental_source skin !'##note attachment of 2-O-alpha-D-glucosyl-O-beta-D-galactose to !15-hydroxylysine REFERENCE S15989 !$#authors Labhard, M.E.; Hollister, D.W. !$#journal Matrix (1990) 10:124-130 !$#title Segmental amplification of the entire helical and !1telopeptide regions of the cDNA for human alpha-1(I) !1collagen. !$#cross-references MUID:90326017; PMID:2374517 !$#accession S15989 !'##molecule_type mRNA !'##residues 281-302;402-420;823-843;925-944;1026-1045;1143-1162 ##label !1LAB REFERENCE I52905 !$#authors Wirtz, M.K.; Rao, V.H.; Glanville, R.W.; Labhard, M.E.; !1Pretorius, P.J.; de Vries, W.N.; de Wet, W.J.; Hollister, !1D.W. !$#journal Connect. Tissue Res. (1993) 29:1-11 !$#title A cysteine for glycine substitution at position 175 in an !1alpha 1 (I) chain of type I collagen produces a clinically !1heterogeneous form of osteogenesis imperfecta. !$#cross-references MUID:93339042; PMID:8339541 !$#accession I52905 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 342-352,'C',354-359 ##label WI2 !'##cross-references GB:S64717; NID:g408195; PIDN:AAB27677.1; !1PID:g408196 !'##note mutant sequence from patient with osteogenesis imperfecta REFERENCE A90476 !$#authors Bernard, M.P.; Chu, M.L.; Myers, J.C.; Ramirez, F.; !1Eikenberry, E.F.; Prockop, D.J. !$#journal Biochemistry (1983) 22:5213-5223 !$#title Nucleotide sequences of complementary deoxyribonucleic acids !1for the proalpha1 chain of human type I procollagen. !1Statistical evaluation of structures that are conserved !1during evolution. !$#cross-references MUID:84080385; PMID:6689127 !$#accession A90476 !'##molecule_type mRNA !'##residues 425-1250,'X',1252-1328,'S',1330-1390,'X',1392-1464 ##label !1BER !'##cross-references GB:K01228; NID:g180391; PIDN:AAA51995.1; !1PID:g180392 !'##note sequence partially completed for missing nucleotides by A29439 REFERENCE A22161 !$#authors Chu, M.L.; Gargiulo, V.; Williams, C.J.; Ramirez, F. !$#journal J. Biol. Chem. (1985) 260:691-694 !$#title Multiexon deletion in an osteogenesis imperfecta variant !1with increased type III collagen mRNA. !$#cross-references MUID:85104934; PMID:2981843 !$#accession A22161 !'##molecule_type DNA !'##residues 472-594,'R',596-607 ##label CH3 !'##cross-references GB:K03178; GB:K03179; NID:g179612; NID:g179613; !1PIDN:AAA51847.1; PID:g179615 !'##note the authors translated the codon CGT for residue 595 as Pro REFERENCE A35336 !$#authors Wallis, G.A.; Starman, B.J.; Zinn, A.B.; Byers, P.H. !$#journal Am. J. Hum. Genet. (1990) 46:1034-1040 !$#title Variable expression of osteogenesis imperfecta in a nuclear !1family is explained by somatic mosaicism for a lethal point !1mutation in the alphaI(I) gene (COLIAI) of type I collagen !1in a parent. !$#cross-references MUID:90252792; PMID:2339700 !$#accession A35336 !'##molecule_type mRNA !'##residues 710-720,'E',722-737,'E',739-745 ##label WAL !'##note the authors translated the codons CAG for 721 and CGT for 738 !1as Glu REFERENCE I54365 !$#authors Forlino, A.; Zolezzi, F.; Valli, M.; Pignatti, P.F.; Cetta, !1G.; Brunelli, P.C.; Mottes, M. !$#journal Hum. Mol. Genet. (1994) 3:2201-2206 !$#title Severe (type III) osteogenesis imperfecta due to glycine !1substitutions in the central domain of the collagen triple !1helix. !$#cross-references MUID:95187161; PMID:7881420 !$#accession I54365 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 746-766,'S',768-781 ##label FOR !'##cross-references GB:L47667; NID:g1009093; PIDN:AAB59576.1; !1PID:g1009094 REFERENCE A47426 !$#authors Chessler, S.D.; Wallis, G.A.; Byers, P.H. !$#journal J. Biol. Chem. (1993) 268:18218-18225 !$#title Mutations in the carboxyl-terminal propeptide of the pro !1alpha 1(I) chain of type I collagen result in defective !1chain association and produce lethal osteogenesis !1imperfecta. !$#cross-references MUID:93352646; PMID:8349697 !$#accession A47426 !'##molecule_type mRNA !'##residues 1179-1276,'H',1278-1336,1339-1387,'R',1389-1464 ##label CHE !'##cross-references GB:S64596; NID:g407589; PIDN:AAB27856.1; !1PID:g407590 !'##note sequence extracted from NCBI backbone (NCBIN:136444, !1NCBIP:136445) !'##note does not represent an experimentally determined sequence but !1three different mutant sequences combined in one; author !1reported sequences are presented below !$#accession B47426 !'##molecule_type mRNA !'##residues 1179-1464 ##label CH4 !'##experimental_source normal dermal fibroblast culture !$#accession C47426 !'##molecule_type mRNA !'##residues 1179-1276,'H',1278-1464 ##label CH5 !'##experimental_source fetal cell 86-237 !$#accession D47426 !'##molecule_type mRNA !'##residues 1179-1336,1339-1464 ##label CH6 !'##experimental_source fetal cell 86-146 !$#accession E47426 !'##molecule_type mRNA !'##residues 1179-1387,'R',1389-1464 ##label CH7 !'##experimental_source fetal cell 88-251 REFERENCE I55269 !$#authors Cohn, D.H.; Apone, S.; Eyre, D.R.; Starman, B.J.; !1Andreassen, P.; Charbonneau, H.; Nicholls, A.C.; Pope, F.M.; !1Byers, P.H. !$#journal J. Biol. Chem. (1988) 263:14605-14607 !$#title Substitution of Cysteine for Glycine within the !1Carboxyl-terminal Telopeptide of the alpha-1 Chain of Type I !1Collagen Produces Mild Osteogenesis Imperfecta. !$#cross-references MUID:89008319; PMID:3170557 !$#accession I55269 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1187-1194,'C',1196-1220 ##label COH !'##cross-references GB:M23213; NID:g340842; PIDN:AAB59363.1; !1PID:g499622 !'##note mutant sequence from a patient with mild osteogenesis !1imperfecta REFERENCE A29439 !$#authors Maekelae, J.K.; Raassina, M.; Virta, A.; Vuorio, E. !$#journal Nucleic Acids Res. (1988) 16:349 !$#title Human pro-alpha-1(I) collagen: cDNA sequence for the !1C-propeptide domain. !$#cross-references MUID:88124208; PMID:3340531 !$#accession A29439 !'##molecule_type mRNA !'##residues 1229-1250,'S',1252-1328,'S',1330-1390,'K',1392-1433,'T', !11435-1454 ##label MAE !'##cross-references EMBL:X06269; NID:g30092; PIDN:CAA29605.1; !1PID:g762938 !'##note the authors translated the codon CAG for residue 1351 as Glu REFERENCE I53466 !$#authors Maatta, A.; Bornstein, P.; Penttinen, R.P.K. !$#journal FEBS Lett. (1991) 279:9-13 !$#title Highly conserved sequences in the 3'-untranslated region of !1the COL1A1 gene bind cell-specific nuclear proteins. !$#cross-references MUID:91138770; PMID:1995349 !$#accession I53466 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1454-1464 ##label MAA !'##cross-references GB:M55998; NID:g180806; PIDN:AAA52036.1; !1PID:g180807 REFERENCE A56965 !$#authors Chu, M.L.; Myers, J.C.; Bernard, M.P.; Ding, J.F.; Ramirez, !1F. !$#journal Nucleic Acids Res. (1982) 10:5925-5934 !$#title Cloning and characterization of five overlapping cDNAs !1specific for the human proalpha1(I) collagen chain. !$#cross-references MUID:83064528; PMID:6183642 !$#contents annotation REFERENCE A56966 !$#authors Barsh, G.S.; Roush, C.L.; Bonadio, J.; Byers, P.H.; Gelinas, !1R.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:2870-2874 !$#title Intron-mediated recombination may cause a deletion in an !1alpha1 type I collagen chain in a lethal form of !1osteogenesis imperfecta. !$#cross-references MUID:85190598; PMID:3857621 !$#contents annotation; introns REFERENCE A56964 !$#authors Willing, M.C.; Cohn, D.H.; Byers, P.H. !$#journal J. Clin. Invest. (1990) 85:282-290 !$#title Frameshift mutation near the 3' end of the COL1A1 gene of !1type I collagen predicts an elongated Proalpha1(I) chain and !1results in osteogenesis imperfecta type I. !$#cross-references MUID:90110490; PMID:2295701 !$#contents annotation COMMENT Collagen is the most abundant protein in the vertebrate !1body. COMMENT Prolines and lysines at the third position of the tripeptide !1repeating unit (G-X-Y) are hydroxylated to varying extents. !1Prolines are predominately 4-hydroxylated; about 1 residue !1in 1000 are 3-hydroxylated. About 10% of the lysines are !15-hydroxylated and subsequently O-glycosylated. GENETICS !$#gene GDB:COL1A1 !'##cross-references GDB:119061; OMIM:120150 !$#map_position 17q21.3-17q22 !$#introns 35/1; 100/1; 111/3; 123/3; 157/3; 181/3; 196/3; 214/3; 232/ !13; 250/3; 268/3; 286/3; 301/3; 319/3; 334/3; 352/3; 385/3; !1400/3; 433/3; 451/3; 487/3; 505/3; 538/3; 556/3 589/3; 622/ !13; 640/3; 658/3 !$#note the list of introns is incomplete; there are 51 exons !$#note defects in this gene can result in perinatal lethal !1osteogenesis imperfecta, mild osteogenesis imperfecta, or !1type VIIA Ehlers-Danlos syndrome COMPLEX type I collagen heterotrimer, tropocollagen, is composed of !1two alpha 1(I) chains and one alpha 2(I) chain (see !1PIR:CGHU2S), initially linked by disulfide bonds among their !1carboxyl-terminal propeptides; small amounts of homotrimer !1also form; a polymer of collagen trimers, offset by !1approximately one-quarter of their length, is formed with !1desmosine cross-links made from lysine and allysine residues FUNCTION !$#description structural component of extracellular fibrous polymer that !1maintains integrity of tendons, ligaments, skin, bone, and !1lung CLASSIFICATION #superfamily collagen alpha 1(I) chain; fibrillar collagen !1carboxyl-terminal homology; von Willebrand factor type C !1repeat homology KEYWORDS bone; coiled coil; Ehlers-Danlos syndrome; extracellular !1matrix; glycoprotein; hydroxylysine; hydroxyproline; !1pyroglutamic acid; skin; trimer; triple helix FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-161 #domain amino-terminal propeptide #status predicted !8#label PRO\ !$23-108 #region nonhelical\ !$39-98 #domain von Willebrand factor type C repeat homology !8#label VWC\ !$109-159 #region helical\ !$162-1218 #product collagen alpha 1(I) chain #status predicted !8#label MAT\ !$162-178 #region amino-terminal nonhelical telopeptide\ !$179-1192 #region helical\ !$745-747 #region cell attachment (R-G-D) motif\ !$1093-1095 #region cell attachment (R-G-D) motif\ !$1193-1218 #region carboxyl-terminal nonhelical telopeptide\ !$1219-1464 #domain carboxyl-terminal propeptide #status !8predicted #label CPR\ !$1235-1464 #domain fibrillar collagen carboxyl-terminal homology !8#label FCC\ !$161-162 #cleavage_site Pro-Gln (procollagen N-endopeptidase) !8#status experimental\ !$162 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$170 #modified_site allysine (Lys) #status experimental\ !$265 #modified_site 5-hydroxylysine (Lys) #status !8experimental\ !$265 #binding_site carbohydrate (Lys) (covalent) #status !8experimental\ !$953-954 #cleavage_site Gly-Ile (collagenase) #status !8predicted\ !$1108 #binding_site carbohydrate (Lys) (covalent) #status !8predicted\ !$1108 #modified_site 5-hydroxylysine (Lys) #status !8predicted\ !$1164 #modified_site 3-hydroxyproline (Pro) #status !8predicted\ !$1208 #modified_site allysine (Lys) #status predicted\ !$1218-1219 #cleavage_site Ala-Asp (procollagen C-endopeptidase) !8#status experimental\ !$1259,1265,1282,1291 #disulfide_bonds interchain #status predicted\ !$1299-1462,1370-1415 #disulfide_bonds #status predicted\ !$1365 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1464 #molecular-weight 138923 #checksum 3154 SEQUENCE /// ENTRY B40333 #type complete TITLE collagen alpha 1(II) chain precursor - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B40333 REFERENCE A40333 !$#authors Su, M.W.; Suzuki, H.R.; Bieker, J.J.; Solursh, M.; Ramirez, !1F. !$#journal J. Cell Biol. (1991) 115:565-575 !$#title Expression of two nonallelic type II procollagen genes !1during Xenopus laevis embryogenesis is characterized by !1stage-specific production of alternatively spliced !1transcripts. !$#cross-references MUID:92011898; PMID:1918153 !$#accession B40333 !'##status preliminary !'##molecule_type mRNA !'##residues 1-1486 ##label SUA !'##cross-references GB:M63595 CLASSIFICATION #superfamily collagen alpha 1(I) chain; fibrillar collagen !1carboxyl-terminal homology; von Willebrand factor type C !1repeat homology KEYWORDS coiled coil; extracellular matrix; glycoprotein; trimer; !1triple helix FEATURE !$37-96 #domain von Willebrand factor type C repeat homology !8#label VWC\ !$1258-1486 #domain fibrillar collagen carboxyl-terminal homology !8#label FCC SUMMARY #length 1486 #molecular-weight 142264 #checksum 965 SEQUENCE /// ENTRY CGBO1S #type fragments TITLE collagen alpha 1(I) chain - bovine (tentative sequence) (fragments) ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 24-Apr-1984 #sequence_revision 31-Dec-1993 #text_change 31-Mar-2000 ACCESSIONS A91193; A91229; A91387; A91211; A91201; A91200; A43048; !1A02853 REFERENCE A91193 !$#authors Rauterberg, J.; Timpl, R.; Furthmayr, H. !$#journal Eur. J. Biochem. (1972) 27:231-237 !$#title Structural characterization of N-terminal antigenic !1determinants in calf and human collagen. !$#cross-references MUID:72255334; PMID:4115172 !$#accession A91193 !'##molecule_type protein !'##residues 1-19 ##label RAU !'##experimental_source skin !'##note the epsilon carbon of Lys-9, by homology with the rat alpha 1 !1(I) chain, is converted to an aldehyde group that is !1involved in cross-linking REFERENCE A91229 !$#authors Fietzek, P.P.; Kuehn, K. !$#journal Eur. J. Biochem. (1975) 52:77-82 !$#title The covalent structure of collagen: amino-acid sequence of !1the cyanogen-bromide peptides alpha1-CB2, alpha1-CB4 and !1alpha1-CB5 from calf-skin collagen. !$#cross-references MUID:76022320; PMID:1164916 !$#accession A91229 !'##molecule_type protein !'##residues 20-145 ##label FIE !'##experimental_source skin !'##note Lys-103 is hydroxylated and binds glucosylgalactose REFERENCE A91387 !$#authors Fietzek, P.P.; Wendt, P.; Kell, I.; Kuehn, K. !$#journal FEBS Lett. (1972) 26:74-76 !$#title The covalent structure of collagen: amino acid sequence of !1alpha1-CB3 from calf skin collagen. !$#cross-references MUID:73049499; PMID:4673951 !$#accession A91387 !'##molecule_type protein !'##residues 146-294 ##label FI2 !'##experimental_source skin REFERENCE A91211 !$#authors Fietzek, P.P.; Rexrodt, F.W.; Hopper, K.E.; Kuehn, K. !$#journal Eur. J. Biochem. (1973) 38:396-400 !$#title The covalent structure of collagen. 2. The amino-acid !1sequence of alpha1-CB7 from calf-skin collagen. !$#cross-references MUID:74086118; PMID:4359390 !$#accession A91211 !'##molecule_type protein !'##residues 295-562 ##label FI3 !'##experimental_source skin REFERENCE A91201 !$#authors Wendt, P.; Mark, K.V.D.; Rexrodt, F.; Kuehn, K. !$#journal Eur. J. Biochem. (1972) 30:169-183 !$#title The covalent structure of collagen. The amino-acid sequence !1of the 112 residues. Amino-terminal part of peptide !1alpha1-CB6 from calf-skin collagen. !$#cross-references MUID:73042276; PMID:4343808 !$#accession A91201 !'##molecule_type protein !'##residues 563-675 ##label WEN !'##experimental_source skin REFERENCE A91200 !$#authors Fietzek, P.P.; Rexrodt, F.W.; Wendt, P.; Stark, M.; Kuehn, !1K. !$#journal Eur. J. Biochem. (1972) 30:163-168 !$#title The covalent structure of collagen. Amino acid sequence of !1peptide alpha1-CB6-C2. !$#cross-references MUID:73042275; PMID:4343807 !$#accession A91200 !'##molecule_type protein !'##residues 676-758 ##label FI4 !'##experimental_source skin !'##note Pro-726 is the only 3-hydroxyproline and the only hydroxylated !1proline in position X (in the tripeptide unit Gly-X-Y) in !1the bovine alpha 1(I) chain REFERENCE A43048 !$#authors Rauterberg, J.; Fietzek, P.; Rexrodt, F.; Becker, U.; Stark, !1M.; Kuehn, K. !$#journal FEBS Lett. (1972) 21:75-79 !$#title The amino acid sequence of the carboxyterminal nonhelical !1cross link region of the alpha1 chain of calf skin collagen. !$#accession A43048 !'##molecule_type protein !'##residues 759-779 ##label RA2 !'##experimental_source skin COMMENT Lysines at positions 115, 124, 274, 346, 424, 496, 658, and !1670 may be hydroxylated in some or all of the chains. COMMENT Prolines in the third position of the tripeptide repeating !1unit (G-X-Y) are hydroxylated in some or all of the chains. COMMENT The order of the eight CNBr peptides in the alpha 1(I) chain !1of bovine skin collagen was determined as 0-1,2,4,5,8,3,7,6. !1The peptides have the lengths, respectively, of 19, 36, 47, !137, 279, 149, 268, and 217 residues. COMMENT The complete chain contains 1052 residues. CLASSIFICATION #superfamily collagen alpha 1(I) chain; fibrillar collagen !1carboxyl-terminal homology; von Willebrand factor type C !1repeat homology KEYWORDS coiled coil; extracellular matrix; glycoprotein; !1pyroglutamic acid; trimer; triple helix FEATURE !$1 #modified_site pyrrolidone carboxylic acid (Gln) !8#status experimental SUMMARY #length 779 #checksum 2052 SEQUENCE /// ENTRY CGRT1S #type fragments TITLE collagen alpha 1(I) chain - rat (tentative sequence) (fragments) ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 13-Jul-1981 #sequence_revision 13-Jul-1981 #text_change 31-Mar-2000 ACCESSIONS A90559; A90552; A92029; A90353; A90566; A90357; A90362; !1A90379; A91209; A91385; A02854; A02855 REFERENCE A90559 !$#authors Bornstein, P. !$#journal Biochemistry (1969) 8:63-71 !$#title Comparative sequence studies of rat skin and tendon !1collagen. II. The absence of a short sequence at the amino !1terminus of the skin alpha1 chain. !$#cross-references MUID:69155173; PMID:5777344 !$#contents CNBr0 and CNBr1 !$#accession A90559 !'##molecule_type protein !'##residues 1-19 ##label BO1 !'##experimental_source tendon !'##note sequences from skin and tendon appear to be identical !'##note the amino-terminal tetrapeptide may be removed by limited !1proteolysis during extraction REFERENCE A90552 !$#authors Kang, A.H.; Bornstein, P.; Piez, K.A. !$#journal Biochemistry (1967) 6:788-795 !$#title The amino acid sequence of peptides from the cross-linking !1region of rat skin collagen. !$#cross-references MUID:67162268; PMID:5337886 !$#contents CNBr1 !$#accession A90552 !'##molecule_type protein !'##residues 5-19 ##label KAN !'##experimental_source skin REFERENCE A92029 !$#authors Bornstein, P. !$#journal J. Biol. Chem. (1967) 242:2572-2574 !$#title The incomplete hydroxylation of individual prolyl residues !1in collagen. !$#cross-references MUID:67165368; PMID:4290711 !$#contents CNBr2 !$#accession A92029 !'##molecule_type protein !'##residues 20-55 ##label BO2 !'##experimental_source skin and tendon REFERENCE A90353 !$#authors Butler, W.T.; Ponds, S.L. !$#journal Biochemistry (1971) 10:2076-2081 !$#title Chemical studies on the cyanogen bromide peptides of rat !1skin collagen. Amino acid sequence of alpha1-CB4. !$#cross-references MUID:71263178; PMID:4327399 !$#contents CNBr4 !$#accession A90353 !'##molecule_type protein !'##residues 56-102 ##label BU1 !'##experimental_source skin REFERENCE A90566 !$#authors Butler, W.T. !$#journal Biochemistry (1970) 9:44-50 !$#title Chemical studies on the cyanogen bromide peptides of rat !1skin collagen. The covalent structure of alpha1-CB5, the !1major hexose-containing cyanogen bromide peptide of alpha1. !$#cross-references MUID:70085124; PMID:5411206 !$#contents CNBr5 !$#accession A90566 !'##molecule_type protein !'##residues 103-139 ##label BU2 !'##experimental_source skin REFERENCE A90357 !$#authors Balian, G.; Click, E.M.; Bornstein, P. !$#journal Biochemistry (1971) 10:4470-4478 !$#title Structure of rat skin collagen alpha1-CB8. Amino acid !1sequence of the hydroxylamine-produced fragment HA1. !$#cross-references MUID:72136131; PMID:4335087 !$#contents CNBr8 !$#accession A90357 !'##molecule_type protein !'##residues 140-238 ##label BA1 !'##experimental_source skin REFERENCE A90362 !$#authors Balian, G.; Click, E.M.; Hermodson, M.A.; Bornstein, P. !$#journal Biochemistry (1972) 11:3798-3806 !$#title Structure of rat skin collagen alpha1-CB8. Amino acid !1sequence of the hydroxylamine-produced fragment HA2. !$#cross-references MUID:73006942; PMID:4342027 !$#contents CNBr8 !$#accession A90362 !'##molecule_type protein !'##residues 239-418 ##label BA2 !'##experimental_source skin REFERENCE A90379 !$#authors Butler, W.T.; Underwood, S.P.; Finch Jr., J.E. !$#journal Biochemistry (1974) 13:2946-2953 !$#title Chemical studies on the cyanogen bromide peptides of rat !1skin collagen. Amino acid sequence of alpha1-CB3. !$#cross-references MUID:74271984; PMID:4366532 !$#contents CNBr3 !$#accession A90379 !'##molecule_type protein !'##residues 419-567 ##label BU3 !'##experimental_source skin REFERENCE A91209 !$#authors Stoltz, M.; Timpl, R.; Furthmayr, H.; Kuehn, K. !$#journal Eur. J. Biochem. (1973) 37:287-294 !$#title Structural and immunogenic properties of a major antigenic !1determinant in neutral salt-extracted rat-skin collagen. !$#cross-references MUID:74011954; PMID:4126850 !$#contents CNBr6 !$#accession A91209 !'##molecule_type protein !'##residues 568-651 ##label ST1 !'##experimental_source skin !'##note this region probably corresponds to positions 949-1032 of the !1alpha 1(I) chain !'##note the major antigenic determinant (of neutral salt-extracted rat !1skin collagen) involves at least Tyr-Asp at positions !1650-651 above and probably the nine residues that precede !1the dipeptide REFERENCE A91385 !$#authors Stoltz, M.; Timpl, R.; Kuehn, K. !$#journal FEBS Lett. (1972) 26:61-65 !$#title Non-helical regions in rat collagen alpha1-chain. !$#cross-references MUID:73049495; PMID:4636751 !$#contents CNBr6 !$#accession A91385 !'##molecule_type protein !'##residues 651-671 ##label ST2 !'##experimental_source skin !'##note the composition of peptides comprising residues 1-9 and 1-19 !1confirms the sequence !'##note this region (residues 651-671 above) probably corresponds to !1positions 1032-1052 of the alpha 1(I) chain COMMENT Prolines and lysines at the third position of the tripeptide !1repeating unit (G-X-Y) are hydroxylated to varying extents. !1Prolines are predominately 4-hydroxylated. Lysines are !15-hydroxylated and subsequently O-glycosylated. COMMENT The order of the nine CNBr peptides in the alpha 1(I) chain !1of rat skin collagen was determined as 0,1,2,4,5,8,3,7,6. COMMENT The complete chain contains 1052 residues. CLASSIFICATION #superfamily collagen alpha 1(I) chain; fibrillar collagen !1carboxyl-terminal homology; von Willebrand factor type C !1repeat homology KEYWORDS blocked amino end; coiled coil; extracellular matrix; !1glycoprotein; hydroxylysine; trimer; triple helix FEATURE !$1 #modified_site blocked amino end (Glx) (probably !8pyrrolidone carboxylic acid) #status experimental\ !$9 #modified_site allysine (Lys) #status experimental\ !$103,424,547 #binding_site carbohydrate (Lys) (covalent) #status !8experimental\ !$103 #modified_site 5-hydroxylysine (Lys) #status !8experimental\ !$424,547 #modified_site 5-hydroxylysine (Lys) (partial) !8#status experimental SUMMARY #length 671 #checksum 936 SEQUENCE /// ENTRY CGRB1S #type fragment TITLE collagen alpha 1(I) chain - rabbit (tentative sequence) (fragment) ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 12-Aug-1981 #sequence_revision 12-Aug-1981 #text_change 31-Mar-2000 ACCESSIONS A02856 REFERENCE A02856 !$#authors Bornstein, P.; Nesse, R. !$#journal Arch. Biochem. Biophys. (1970) 138:443-450 !$#title The comparative biochemistry of collagen: the structure of !1rabbit skin collagen and its relevance to immunochemical !1studies of collagen. !$#cross-references MUID:70252720; PMID:4194291 !$#accession A02856 !'##molecule_type protein !'##residues 1-53 ##label BOR !'##experimental_source skin !'##note the compositions of CNBr1 and CNBr2 were determined !'##note we have positioned residues by homology with rat tendon alpha 1 !1(I) chain !'##note it is assumed that the epsilon carbon of Lys-7 is converted to !1an aldehyde group that is involved in cross-linking !'##note the six prolines at the third position of the tripeptide !1repeating unit (G-X-Y) may be hydroxylated CLASSIFICATION #superfamily collagen alpha 1(I) chain; fibrillar collagen !1carboxyl-terminal homology; von Willebrand factor type C !1repeat homology KEYWORDS coiled coil; extracellular matrix; glycoprotein; trimer; !1triple helix FEATURE !$7 #modified_site allysine (Lys) #status predicted SUMMARY #length 53 #checksum 1461 SEQUENCE /// ENTRY CGCH1S #type fragments TITLE collagen alpha 1(I) chain - chicken (tentative sequence) (fragments) ORGANISM #formal_name Gallus gallus #common_name chicken DATE 12-Aug-1981 #sequence_revision 06-Jul-1982 #text_change 31-Mar-2000 ACCESSIONS A90458; A90181; A02857 REFERENCE A90458 !$#authors Highberger, J.H.; Corbett, C.; Dixit, S.N.; Yu, W.; Seyer, !1J.M.; Kang, A.H.; Gross, J. !$#journal Biochemistry (1982) 21:2048-2055 !$#title Amino acid sequence of chick skin collagen alpha1(I)-CB8 and !1the complete primary structure of the helical portion of the !1chick skin collagen alpha1(I) chain. !$#cross-references MUID:82231995; PMID:7093229 !$#accession A90458 !'##molecule_type protein !'##residues 1-1036 ##label HIG !'##experimental_source skin !'##note this is the latest in a series of papers from these workers !1elucidating the sequence of the amino-terminal 1036 residues REFERENCE A90181 !$#authors Eyre, D.R.; Glimcher, M.J. !$#journal Biochem. Biophys. Res. Commun. (1972) 48:720-726 !$#title Evidence for a previously undetected sequence at the !1carboxyterminus of the alpha1 chain of chicken bone !1collagen. !$#cross-references MUID:72243016; PMID:5047697 !$#accession A90181 !'##molecule_type protein !'##residues 1037-1042 ##label EYR !'##experimental_source skin !'##note residues 1037-1042 above correspond to the carboxyl end of the !1protein COMMENT Lysines at positions 103, 700, 934, and 946 above may be !1hydroxylated in some or all of the chains. COMMENT Most of the prolines at the third position of the tripeptide !1repeating unit (G-X-Y) are hydroxylated in some or all of !1the chains. COMMENT Pro-1002 is the only 3-hydroxyproline and the only !1hydroxylated proline in position X (in the tripeptide !1Gly-X-Y) in the chicken alpha 1(I) chain. CLASSIFICATION #superfamily collagen alpha 1(I) chain; fibrillar collagen !1carboxyl-terminal homology; von Willebrand factor type C !1repeat homology KEYWORDS coiled coil; extracellular matrix; glycoprotein; !1pyroglutamic acid; trimer; triple helix FEATURE !$1 #modified_site pyrrolidone carboxylic acid (Gln) !8#status experimental SUMMARY #length 1042 #checksum 1932 SEQUENCE /// ENTRY CGHU6C #type complete TITLE collagen alpha 1(II) chain precursor [validated] - human ALTERNATE_NAMES procollagen alpha 1(II) chain CONTAINS chondrocalcin; collagen alpha 1(II) chain precursor splice form 1; collagen alpha 1(II) chain precursor splice form 2; collagen alpha 3(XI) chain ORGANISM #formal_name Homo sapiens #common_name man DATE 28-May-1986 #sequence_revision 01-Sep-1995 #text_change 08-Dec-2000 ACCESSIONS A38513; S06715; S24270; A24828; S06496; A35428; A30147; !1A33116; S64674; S63514; I38867; S04892; S05000; A44309; !1S16502; A02858; A27280; A57033; A21733; B21733; A24561; !1S59491; I84453; I37250; I37251; I37252; I37253; I37254; !1I55338; I59535; I61910 REFERENCE A38513 !$#authors Ryan, M.C.; Sieraski, M.; Sandell, L.J. !$#journal Genomics (1990) 8:41-48 !$#title The human type II procollagen gene: identification of an !1additional protein-coding domain and location of potential !1regulatory sequences in the promoter and first intron. !$#cross-references MUID:91184811; PMID:2081599 !$#accession A38513 !'##molecule_type DNA !'##residues 1-103 ##label RYA !'##cross-references GB:M60299; NID:g180883; PIDN:AAA73873.1; !1PID:g180884 REFERENCE S06715 !$#authors Su, M.W.; Lee, B.; Ramirez, F.; Machado, M.; Horton, W. !$#journal Nucleic Acids Res. (1989) 17:9473 !$#title Nucleotide sequence of the full length cDNA encoding for !1human type II procollagen. !$#cross-references MUID:90067946; PMID:2587267 !$#accession S06715 !'##molecule_type mRNA !'##residues 1-28,'R',99-1487 ##label SU2 !'##cross-references EMBL:X16468; NID:g29515; PIDN:CAA34488.1; !1PID:g29516 !'##note alternative splice form 1 REFERENCE S24270 !$#authors Vikkula, M.; Metsaeranta, M.; Syvaenen, A.C.; Ala-Kokko, L.; !1Vuorio, E.; Peltonen, L. !$#journal Biochem. J. (1992) 285:287-294 !$#title Structural analysis of the regulatory elements of the !1type-II procollagen gene. Conservation of promoter and first !1intron sequences between human and mouse. !$#cross-references MUID:92344585; PMID:1637314 !$#accession S24270 !'##status translation not shown !'##molecule_type DNA !'##residues 1-28 ##label VIK !'##cross-references EMBL:X58709; GB:S40537; NID:g35659 !'##note this translation is not annotated in GenBank entry HSPROCOE1, !1release 111.0 REFERENCE A24828 !$#authors Nunez, A.M.; Kohno, K.; Martin, G.R.; Yamada, Y. !$#journal Gene (1986) 44:11-16 !$#title Promoter region of the human pro-alpha-1-(II)-collagen gene. !$#cross-references MUID:87031574; PMID:3021582 !$#accession A24828 !'##molecule_type DNA !'##residues 1-8,'T',10-28 ##label NUN !'##cross-references GB:M25698; NID:g180872; PIDN:AAA52051.1; !1PID:g553237 REFERENCE S06496 !$#authors Baldwin, C.T.; Reginato, A.M.; Smith, C.; Jimenez, S.A.; !1Prockop, D.J. !$#journal Biochem. J. (1989) 262:521-528 !$#title Structure of cDNA clones coding for human type II !1procollagen. The alpha-1(II) chain is more similar to the !1alpha-1(I) chain than two other alpha chains of fibrillar !1collagens. !$#cross-references MUID:90026318; PMID:2803268 !$#accession S06496 !'##molecule_type mRNA !'##residues 7-28,'R',99-157,'P',159-440,'G',442-456,'E',458-640,'A', !1642-831,'PA',834,'F',836-1005,'K',1007-1036,'Q',1038-1229 !1##label BAL !'##cross-references EMBL:X16711; NID:g30040; PIDN:CAA34683.1; !1PID:g30041 !'##note alternative splice form 1 REFERENCE A35428 !$#authors Ryan, M.C.; Sandell, L.J. !$#journal J. Biol. Chem. (1990) 265:10334-10339 !$#title Differential expression of a cysteine-rich domain in the !1amino-terminal propeptide of type II (cartilage) procollagen !1by alternative splicing of mRNA. !$#cross-references MUID:90285153; PMID:2355003 !$#accession A35428 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 27-81,'L',83-103 ##label RYA2 !'##note alternative splice form 2; splicing appears to be under !1developmental regulation REFERENCE A30147 !$#authors Su, M.W.; Benson-Chanda, V.; Vissing, H.; Ramirez, F. !$#journal Genomics (1989) 4:438-441 !$#title Organization of the exons coding for Pro alpha-1(II) !1collagen N-propeptide confirms a distinct evolutionary !1history of this domain of the fibrillar collagen genes. !$#cross-references MUID:89233138; PMID:2714801 !$#accession A30147 !'##molecule_type DNA !'##residues 104-157,'P',159-236 ##label SUM !'##cross-references GB:J03065; GB:M23660; GB:M25655; GB:M25656; !1GB:M25730; GB:M32168; GB:M64345; NID:g180867; !1PIDN:AAA58428.1; PID:g180869 REFERENCE A94227 !$#authors Ala-Kokko, L.; Baldwin, C.T.; Moskowitz, R.W.; Prockop, D.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:6565-6568 !$#title Single base mutation in the type II procollagen gene !1(COL2A1) as a cause of primary osteoarthritis associated !1with a mild chondrodysplasia. !$#cross-references MUID:90370826; PMID:1975693 !$#accession A33116 !'##molecule_type DNA !'##residues 171-172,'C',174-175 ##label ALA !'##note mutant sequence from a family with family with primary !1generalized osteoarthritis and mild chondrodysplasia REFERENCE S64673 !$#authors Diab, M.; Wu, J.J.; Eyre, D.R. !$#journal Biochem. J. (1996) 314:327-332 !$#title Collagen type IX from human cartilage: a structural profile !1of intermolecular cross-linking sites. !$#cross-references MUID:96195147; PMID:8660302 !$#accession S64674 !'##molecule_type protein !'##residues 188-189,'X',191-195;1224-1230,'X',1232-1236 ##label DIA REFERENCE S63514 !$#authors Franc, S.; Marzin, E.; Boutillon, M.M.; Lafont, R.; Lechene !1de la Porte, P.; Herbage, D. !$#journal Eur. J. Biochem. (1995) 234:125-131 !$#title Immunohistochemical and biochemical analyses of !120000-25000-year-old fossil cartilage. !$#cross-references MUID:96096730; PMID:8529631 !$#accession S63514 !'##molecule_type protein !'##residues 243-261;575-590;756-763,'X',765-779 ##label FRA REFERENCE I38867 !$#authors Tiller, G.E.; Weis, M.A.; Polumbo, P.A.; Gruber, H.E.; !1Rimoin, D.L.; Cohn, D.H.; Eyre, D.R. !$#journal Am. J. Hum. Genet. (1995) 56:388-395 !$#title An RNA-splicing mutation (G+5IVS20) in the type II collagen !1gene (COL2A1) in a family with spondyloepiphyseal dysplasia !1congenita. !$#cross-references MUID:95150028; PMID:7847372 !$#accession I38867 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 440,'G',442-456,'E',458-480,'P',482-509 ##label TIL1 !'##cross-references EMBL:U15195; NID:g557053; PIDN:AAB60370.1; !1PID:g557054 REFERENCE S04892 !$#authors Ramirez, F. !$#submission submitted to the EMBL Data Library, December 1988 !$#accession S04892 !'##molecule_type mRNA !'##residues 501-676,'A',678-783,'A',785-831,'PA',834,'F',836-1214 !1##label RAM !'##cross-references EMBL:X13783; NID:g30037; PIDN:CAA32030.1; !1PID:g930050 REFERENCE S05000 !$#authors Vikkula, M.; Peltonen, L. !$#journal FEBS Lett. (1989) 250:171-174 !$#title Structural analyses of the polymorphic area in type II !1collagen gene. !$#cross-references MUID:89325561; PMID:2753125 !$#accession S05000 !'##molecule_type DNA !'##residues 630-640,'A',642-785 ##label VIK2 !'##cross-references EMBL:X16158; NID:g29951; PIDN:CAA34278.1; !1PID:g1335018; PIDN:CAA34279.1; PID:g1335019; !1PIDN:CAA34280.1; PID:g1335020; PIDN:CAA34281.1; !1PID:g1335021; PIDN:CAA34282.1; PID:g1335022; !1PIDN:CAA34283.1; PID:g1335023; PIDN:CAA34284.1; PID:g1335024 REFERENCE A44309 !$#authors Bogaert, R.; Tiller, G.E.; Weis, M.A.; Gruber, H.E.; Rimoin, !1D.L.; Cohn, D.H.; Eyre, D.R. !$#journal J. Biol. Chem. (1992) 267:22522-22526 !$#title An amino acid substitution (Gly853-->Glu) in the collagen !1alpha 1(II) chain produces hypochondrogenesis. !$#cross-references MUID:93054548; PMID:1429602 !$#accession A44309 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type DNA; mRNA !'##residues 752-831,'PA',834,'F',836-1005,'K',1007-1036,'Q',1038-1052, !1'E',1054-1068,'T',1070-1097 ##label BOG !'##cross-references GB:L00977; NID:g180812; PIDN:AAB23914.1; !1PID:g258774 !'##note sequence extracted from NCBI backbone (NCBIP:117273); parts of !1this sequence were determined by protein sequencing !'##note this translation is not annotated and this publication is not !1cited in GenBank entry HUMCOL2A1C, release 111.0; the !1translation and publication appear in Entrez entry AAB23914 !'##note mutant sequence associated with perinatal lethal !1hypochondrogenesis REFERENCE S16502 !$#authors Tiller, G.E.; Rimoin, D.L.; Murray, L.W.; Cohn, D.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:3889-3893 !$#title Tandem duplication within a type II collagen gene (COL2A1) !1exon in an individual with spondyloepiphyseal dysplasia. !$#cross-references MUID:90251662; PMID:2339128 !$#accession S16502 !'##molecule_type DNA !'##residues 1164-1184,'GPSGKDGANGIPGPI',1185-1199 ##label TIL2 !'##cross-references EMBL:M37126; NID:g180808; PIDN:AAA52037.1; !1PID:g180809 !'##note mutant sequence from a patient with spondyloepiphyseal !1dysplasia REFERENCE A02858 !$#authors Cheah, K.S.E.; Stoker, N.G.; Griffin, J.R.; Grosveld, F.G.; !1Solomon, E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:2555-2559 !$#title Identification and characterization of the human type II !1collagen gene (COL2A1). !$#cross-references MUID:85190534; PMID:3857598 !$#accession A02858 !'##molecule_type DNA !'##residues 1032-1056,'N',1058-1068,'T',1070-1487 ##label CHE !'##cross-references GB:J00116; NID:g180395; PIDN:AAA51997.1; !1PID:g180396 REFERENCE A27280 !$#authors Elima, K.; Vuorio, T.; Vuorio, E. !$#journal Nucleic Acids Res. (1987) 15:9499-9504 !$#title Determination of the single polyadenylation site of the !1human pro-alpha-1(II) collagen gene. !$#cross-references MUID:88067771; PMID:2825137 !$#accession A27280 !'##molecule_type DNA; mRNA !'##residues 1175-1487 ##label ELI !'##cross-references EMBL:X06268; NID:g30096; PIDN:CAA29604.1; !1PID:g30097 !'##experimental_source fetal epiphyseal cartilage REFERENCE A57033 !$#authors van der Rest, M.; Rosenberg, L.C.; Olsen, B.R.; Poole, A.R. !$#journal Biochem. J. (1986) 237:923-925 !$#title Chondrocalcin is identical with the C-propeptide of type II !1procollagen. !$#cross-references MUID:87099927; PMID:3800925 !$#accession A57033 !'##molecule_type protein !'##residues 'XE',1244-1246,'N',1248,'X',1250-1265;1295-1305;1395-1408 !1##label VAN !'##note chondrocalcin identified as released collagen 1(II) chain !1carboxyl-terminal propeptide REFERENCE A21733 !$#authors Strom, C.M.; Upholt, W.B. !$#journal Nucleic Acids Res. (1984) 12:1025-1038 !$#title Isolation and characterization of genomic clones !1corresponding to the human type II procollagen gene. !$#cross-references MUID:84118798; PMID:6320112 !$#accession A21733 !'##molecule_type DNA !'##residues 1245-1295 ##label STR1 !'##cross-references EMBL:X00339; EMBL:X00298; NID:g394699; !1PIDN:CAA25092.1; PID:g4378975 !$#accession B21733 !'##molecule_type DNA !'##residues 894-909,'PE' ##label STR2 !'##cross-references GB:K01785; NID:g30035; PIDN:CAA25082.1; !1PID:g1335032 REFERENCE A24561 !$#authors Nunez, A.M.; Francomano, C.; Young, M.F.; Martin, G.R.; !1Yamada, Y. !$#journal Biochemistry (1985) 24:6343-6348 !$#title Isolation and partial characterization of genomic clones !1coding for a human pro-alpha-1(II) collagen chain and !1demonstration of restriction fragment length polymorphism at !1the 3' end of the gene. !$#cross-references MUID:86104139; PMID:3002437 !$#accession A24561 !'##molecule_type DNA !'##residues 1296-1358 ##label NUN2 !'##cross-references GB:M12048; NID:g180017 !'##note this translation is not annotated in GenBank entry HUMCCT2A, !1release 111.0 !'##note the codons given for 1333-Lys (AGG) and 1350-Gly (GCA) are !1inconsistent with the authors' translation REFERENCE I37249 !$#authors Sangiorgi, F.O.; Benson-Chanda, V.; de Wet, W.J.; Sobel, !1M.E.; Tsipouras, P.; Ramirez, F. !$#journal Nucleic Acids Res. (1985) 13:2207-2225 !$#title Isolation and partial characterization of the entire human !1pro alpha 1(II) collagen gene. !$#cross-references MUID:85215609; PMID:2987845 !$#accession S59491 !'##molecule_type DNA !'##residues 7-28;'R',99-114;541-578;786-802;1055-1056,'N',1058-1068, !1'T',1070-1109;1200-1371,'D',1373-1382,'A',1384-1399,'M', !11401-1487 ##label SAN1 !$#accession I84453 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 7-28 ##label SAN2 !'##cross-references GB:M23759; NID:g180845; EMBL:X03320; GB:M24938; !1NID:g30104 !'##note the GenBank PID is based on an incorrect reading frame !$#accession I37250 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 541-560 ##label SAN3 !'##cross-references EMBL:X02378; GB:M23870; NID:g30107; !1PIDN:CAA26227.1; PID:g929621 !$#accession I37251 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 561-578 ##label SAN4 !'##cross-references EMBL:X02377; GB:M23758; GB:M25727; NID:g30109; !1PIDN:CAA26226.1; PID:g929622 !$#accession I37252 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 786-803 ##label SAN5 !'##cross-references EMBL:X02376; GB:M23758; GB:M25055; NID:g30111; !1PIDN:CAA26225.1; PID:g575947 !$#accession I37253 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1056,'N',1058-1068,'T',1070-1109 ##label SAN6 !'##cross-references GB:M25728; GB:M23757; EMBL:X02375; NID:g30113; !1PIDN:CAA26224.1; PID:g575948 !$#accession I37254 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1200-1371,'D',1373-1382,'A',1384-1399,'M',1401-1487 ##label !1SAN7 !'##cross-references EMBL:X02371; NID:g30115; PIDN:CAA26223.1; !1PID:g825645; GB:M23756; NID:g180850; PID:g180855 REFERENCE I55338 !$#authors Chan, D.; Cole, W.G. !$#journal J. Biol. Chem. (1991) 266:12487-12494 !$#title Low basal transcription of genes for tissue-specific !1collagens by fibroblasts and lymphoblastoid cells. !1Application to the characterization of a glycine 997 to !1serine substitution in alpha 1(II) collagen chains of a !1patient with spondyloepiphyseal dysplasia. !$#cross-references MUID:91286276; PMID:1905723 !$#accession I55338 !'##status nucleic acid sequence not shown; translation not shown; !1translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1082-1270,'T',1272-1273,'A',1275-1288 ##label CHA !'##cross-references GB:M63281; NID:g180810; PIDN:AAA52038.1; !1PID:g180811 !'##note portions of several mutant sequences were determined; the !1translation of one is shown; the sequence in GenBank was !1submitted REFERENCE I59535 !$#authors Lee, B.; Vissing, H.; Ramirez, F.; Rogers, D.; Rimoin, D. !$#journal Science (1989) 244:978-980 !$#title Identification of the molecular defect in a family with !1spondyloepiphyseal dysplasia. !$#cross-references MUID:89266907; PMID:2543071 !$#accession I59535 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1146-1199 ##label LEE !'##cross-references GB:M27468; NID:g341711; PIDN:AAA52039.1; !1PID:g529398 !'##note deletion mutation of 36 residues in exon 48 in patient with !1spondyloepiphyseal dysplasia; the normal sequence inluding !1the deleted portion is shown COMMENT Prolines and lysines at the third position of the tripeptide !1repeating unit (G-X-Y) are hydroxylated to varying extents. !1Prolines are predominately 4-hydroxylated; about 2 residues !1in 1000 are 3-hydroxylated. About 50% of the lysines are !15-hydroxylated and some are subsequently O-glycosylated. GENETICS !$#gene GDB:COL2A1; SEDC !'##cross-references GDB:119063; OMIM:200610; OMIM:120140 !$#map_position 12q12-12q13.2 !$#introns 29/1; 34/3; 98/1; 103/3; 114/3; 125/3; 143/3; 177/3; 203/3; !1218/3; 236/3; 254/3; 272/3; 290/3; 308/3; 326/3; 341/3; 356/ !13; 374/3; 407/3; 422/3; 456/3; 473/3; 509/3; 527/3; 560/3; !1578/3; 596/3; 614/3; 629/3; 647/3; 662/3; 698/3; 731/3; 767/ !13; 803/3; 821/3; 839/3; 875/3; 893/3; 911/3; 965/3; 1001/3; !11037/3; 1055/3; 1091/3; 1109/3; 1145/3; 1163/3; 1199/3; !11214/3; 1296/1; 1358/3; 1439/3 !$#note defects in this gene can result in perinatal lethal !1hypochondrogenesis, chondrodysplasia, spondyloepiphyseal !1dysplasia or osteoarthritis COMPLEX type II collagen is a homotrimer of monomers initially !1linked by disulfide bonds among their carboxy-terminal !1propeptides; a polymer of collagen trimers, offset by !1approximately one-quarter of their length, is formed with !1desmosine cross-links made from lysine and allysine residues FUNCTION !$#description structural component of extracellular fibrous polymer that !1maintains integrity of cartilage, eye vitreous humor, !1notochord, and fetal and juvenile bone CLASSIFICATION #superfamily collagen alpha 1(I) chain; fibrillar collagen !1carboxyl-terminal homology; von Willebrand factor type C !1repeat homology KEYWORDS alternative splicing; cartilage; coiled coil; extracellular !1matrix; glycoprotein; hydroxylysine; hydroxyproline; !1pyroglutamic acid; trimer; triple helix FEATURE !$1-1487 #product collagen alpha 1(II) chain precursor, splice !8form 2 #status predicted #label SF2\ !$1-29,99-1487 #product collagen alpha 1(II) chain precursor, splice !8form 1 #status predicted #label SF1\ !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-1241 #product collagen alpha 3(XI) chain #status predicted !8#label MAT2\ !$26-181 #domain amino-terminal propeptide #status predicted !8#label PRO\ !$33-92 #domain von Willebrand factor type C repeat homology !8#label VWC\ !$134-136 #region cell attachment (R-G-D) motif\ !$137-139 #region cell attachment (R-G-D) motif\ !$182-1241 #product collagen alpha 1(II) chain #status predicted !8#label MAT\ !$182-200 #region amino-terminal nonhelical telopeptide\ !$201-1217 #region helical\ !$767-769 #region cell attachment (R-G-D) motif\ !$932-934 #region cell attachment (R-G-D) motif\ !$1115-1117 #region cell attachment (R-G-D) motif\ !$1218-1241 #region carboxyl-terminal nonhelical telopeptide\ !$1242-1487 #product chondrocalcin #status experimental #label !8CPR\ !$1259-1487 #domain fibrillar collagen carboxyl-terminal homology !8#label FCC\ !$26 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status predicted\ !$181-182 #cleavage_site Ala-Gln (procollagen N-endopeptidase) !8#status predicted\ !$182 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status predicted\ !$190,1231 #modified_site allysine (Lys) #status predicted\ !$287,1130 #binding_site carbohydrate (Lys) (covalent) #status !8predicted\ !$287,1130 #modified_site 5-hydroxylysine (Lys) #status !8predicted\ !$834-835 #cleavage_site Gly-Ile (collagenase) #status !8predicted\ !$1186 #modified_site 3-hydroxyproline (Pro) #status !8predicted\ !$1241-1242 #cleavage_site Ala-Asp (procollagen C-endopeptidase) !8#status predicted\ !$1283,1289,1306,1315 #disulfide_bonds interchain #status predicted\ !$1323-1485,1393-1438 #disulfide_bonds #status predicted\ !$1388 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1487 #molecular-weight 141888 #checksum 6520 SEQUENCE /// ENTRY CGBO6C #type fragments TITLE collagen alpha 1(II) chain precursor - bovine (tentative sequence) (fragments) ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 24-Apr-1984 #sequence_revision 17-May-1996 #text_change 31-Mar-2000 ACCESSIONS A90369; A90396; A92210; S03940; A90189; A05039; A02859 REFERENCE A90369 !$#authors Miller, E.J.; Lunde, L.G. !$#journal Biochemistry (1973) 12:3153-3159 !$#title Isolation and characterization of the cyanogen bromide !1peptides from the alpha1(II) chain of bovine and human !1cartilage collagen. !$#cross-references MUID:73258693; PMID:4732855 !$#contents composition of CNBr1 and CNBr4 !$#accession A90369 !'##molecule_type protein !'##residues 1-15 ##label MIL !'##experimental_source cartilage !'##note residues positioned by comparison with human alpha 1(II) chain REFERENCE A90396 !$#authors Butler, W.T.; Miller, E.J.; Finch Jr., J.E. !$#journal Biochemistry (1976) 15:3000-3006 !$#title The covalent structure of cartilage collagen. Amino acid !1sequence of the NH-2-terminal helical portion of the alpha1 !1(II) chain. !$#cross-references MUID:76253504; PMID:782511 !$#contents fragments CNBr2 (16-18), CNBr3 (19-21), CNBr6 (22-54), !1CNBr12 (55-138), and the first 39 residues of CNBr11 !1(139-417) !$#accession A90396 !'##molecule_type protein !'##residues 16-177 ##label BUT !'##experimental_source cartilage !'##note order of CNBr peptides determined REFERENCE A92210 !$#authors Butler, W.T.; Finch Jr., J.E.; Miller, E.J. !$#journal J. Biol. Chem. (1977) 252:639-643 !$#title The covalent structure of cartilage collagen. Evidence for !1sequence heterogeneity of bovine alpha1(II) chains. !$#cross-references MUID:77093864; PMID:833147 !$#accession A92210 !'##molecule_type protein !'##residues 139-178,'Z',180-184,'PA',187-190,'AS',193-194,'T',196-198 !1##label BU2 !'##experimental_source cartilage !'##note a minor, probably nonallelic, alpha 1(II) component has !1143-Ala, 164-Leu, and possibly 179-Ser REFERENCE S03940 !$#authors Seyer, J.M.; Hasty, K.A.; Kang, A.H. !$#journal Eur. J. Biochem. (1989) 181:159-173 !$#title Covalent structure of collagen. Amino acid sequence of an !1arthritogenic cyanogen bromide peptide from type II collagen !1of bovine cartilage. !$#cross-references MUID:89231683; PMID:2714276 !$#accession S03940 !'##molecule_type protein !'##residues 139-417 ##label SEY REFERENCE A90189 !$#authors Butler, W.T.; Miller, E.J.; Finch Jr., J.E.; Inagami, T. !$#journal Biochem. Biophys. Res. Commun. (1974) 57:190-195 !$#title Homologous regions of collagen alpha1 (I) and alpha1(II) !1chains: apparent clustering of variable and invariant amino !1acid residues. !$#cross-references MUID:74163168; PMID:4857180 !$#accession A90189 !'##molecule_type protein !'##residues 418-492 ##label BU3 !'##experimental_source cartilage !'##note the first 75 residues of CNBr8, which follows CNBr11 REFERENCE A05039 !$#authors Sangiorgi, F.O.; Benson-Chanda, V.; de Wet, W.J.; Sobel, !1M.E.; Ramirez, F. !$#journal Nucleic Acids Res. (1985) 13:2815-2826 !$#cross-references MUID:85215651; PMID:2582365 !$#accession A05039 !'##molecule_type mRNA !'##residues 493-673 ##label SAN !'##cross-references GB:X02420; NID:g265; PIDN:CAA26269.1; PID:g266 !'##experimental_source cartilage COMMENT Prolines in the third position of the tripeptide repeating !1unit (G-X-Y) are hydroxylated in some or all of the !1molecules. COMMENT Type II collagen molecules are trimers of identical alpha 1 !1(II) chains, genetically distinct from the other types of !1alpha chains, and are specific for cartilaginous tissues. !1The order of the CNBr peptides was determined as !11-4-2-3-6-12-11-8-10-5-9,7-14-15. CLASSIFICATION #superfamily collagen alpha 1(I) chain; fibrillar collagen !1carboxyl-terminal homology; von Willebrand factor type C !1repeat homology KEYWORDS cartilage; coiled coil; extracellular matrix; glycoprotein; !1hydroxylysine; trimer; triple helix FEATURE !$493-673 #domain carboxyl-terminal propeptide (fragment) !8#status predicted #label CTP\ !$499-673 #domain fibrillar collagen carboxyl-terminal homology !8(fragment) #label FCC\ !$9,102,114,123,189, !$423,435 #modified_site 5-hydroxylysine (Lys) #status !8experimental\ !$9,102,114,123,189, !$423,435 #binding_site carbohydrate (Lys) (covalent) #status !8experimental\ !$574 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 673 #checksum 7265 SEQUENCE /// ENTRY CGCH6C #type fragment TITLE collagen alpha 1(II) chain precursor - chicken (fragment) ORGANISM #formal_name Gallus gallus #common_name chicken DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 22-Jun-1999 ACCESSIONS A02860; I50175; A57032 REFERENCE A02860 !$#authors Sandell, L.J.; Prentice, H.L.; Kravis, D.; Upholt, W.B. !$#journal J. Biol. Chem. (1984) 259:7826-7834 !$#title Structure and sequence of the chicken type II procollagen !1gene. Characterization of the region encoding the !1carboxyl-terminal telopeptide and propeptide. !$#cross-references MUID:84239728; PMID:6330084 !$#accession A02860 !'##molecule_type DNA !'##residues 1-288 ##label SAN !'##note this sequence corresponds to the last four exons REFERENCE I50175 !$#authors Young, M.F.; Vogeli, G.; Nunez, A.M.; Fernandez, M.P.; !1Sullivan, M.; Sobel, M.E. !$#journal Nucleic Acids Res. (1984) 12:4207-4228 !$#title Isolation of cDNA and genomic DNA clones encoding type II !1collagen. !$#cross-references MUID:84221355; PMID:6203098 !$#accession I50175 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 82-201 ##label YOU !'##cross-references GB:M17866; NID:g211345; PIDN:AAA48639.1; !1PID:g211348 REFERENCE A57032 !$#authors Ninomiya, Y.; Showalter, A.M.; van der Rest, M.; Seidah, !1N.G.; Chretien, M.; Olsen, B.R. !$#journal Biochemistry (1984) 23:617-624 !$#title Structure of the carboxyl propeptide of chicken type II !1procollagen determined by DNA and protein sequence analysis. !$#accession A57032 !'##molecule_type mRNA !'##residues 34-71,'A',73-288 ##label NIN !'##cross-references GB:K01568 GENETICS !$#introns 97/1; 159/3; 240/3 CLASSIFICATION #superfamily collagen alpha 1(I) chain; fibrillar collagen !1carboxyl-terminal homology; von Willebrand factor type C !1repeat homology KEYWORDS cartilage; coiled coil; extracellular matrix; glycoprotein; !1trimer; triple helix FEATURE !$1-42 #product collagen alpha 1(II) chain (fragment) !8#status predicted #label CAH\ !$1-15 #region helical (fragment)\ !$16-42 #region carboxyl-terminal nonhelical telopeptide\ !$43-288 #domain carboxyl-terminal propeptide #status !8predicted #label CPR\ !$60-288 #domain fibrillar collagen carboxyl-terminal homology !8#label FCC\ !$42-43 #cleavage_site Ala-Asp (procollagen C-endopeptidase) !8#status experimental\ !$189 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$194-239 #disulfide_bonds #status predicted SUMMARY #length 288 #checksum 5961 SEQUENCE /// ENTRY CGHU7L #type complete TITLE collagen alpha 1(III) chain precursor - human ALTERNATE_NAMES procollagen alpha 1(III) chain ORGANISM #formal_name Homo sapiens #common_name man DATE 24-Apr-1984 #sequence_revision 01-Sep-1995 #text_change 21-Jul-2000 ACCESSIONS S05272; S04642; PE0011; S01726; S04887; A90399; A94562; !1I51868; S59511; A90414; I55349; A90438; A38303; S02119; !1A90446; A93551; I52393; I79359; A92516; A02861 REFERENCE S05272 !$#authors Prockop, D.J. !$#submission submitted to the EMBL Data Library, February 1989 !$#accession S05272 !'##status preliminary !'##molecule_type mRNA !'##residues 1-1240,'V',1242-1466 ##label PRC !'##cross-references EMBL:X14420; NID:g30057; PIDN:CAA32583.1; !1PID:g30058 REFERENCE S04642 !$#authors Ala-Kokko, L.; Kontusaari, S.; Baldwin, C.T.; Kuivaniemi, !1H.; Prockop, D.J. !$#journal Biochem. J. (1989) 260:509-516 !$#title Structure of cDNA clones coding for the entire prepro-alpha1 !1(III) chain of human type III procollagen. Differences in !1protein structure from type I procollagen and conservation !1of codon preferences. !$#cross-references MUID:89350838; PMID:2764886 !$#accession S04642 !'##molecule_type mRNA !'##residues 1-1196 ##label ALA !'##cross-references EMBL:X14420; NID:g30057; PIDN:CAA32583.1; !1PID:g30058 !'##note the complete sequence is not shown REFERENCE PE0011 !$#authors Benson-Chanda, V.; Su, M.W.; Weil, D.; Chu, M.L.; Ramirez, !1F. !$#journal Gene (1989) 78:255-265 !$#title Cloning and analysis of the 5' portion of the human type-III !1procollagen gene (COL3A1). !$#cross-references MUID:89378752; PMID:2777083 !$#accession PE0011 !'##molecule_type DNA !'##residues 1-176 ##label BEN !'##cross-references GB:M26939; NID:g180813; PIDN:AAA52040.1; !1PID:g180814 REFERENCE S01726 !$#authors Toman, P.D.; Ricca, G.A.; de Crombrugghe, B. !$#journal Nucleic Acids Res. (1988) 16:7201 !$#title Nucleotide sequence of a cDNA coding for the amino-terminal !1region of human prepro alpha-1(III) collagen. !$#cross-references MUID:88303360; PMID:3405773 !$#accession S01726 !'##molecule_type mRNA !'##residues 1-170 ##label TOM !'##cross-references EMBL:X07240; NID:g30060; PIDN:CAA30229.1; !1PID:g30061 !'##note the authors translated the codon CAG for residue 154 as His REFERENCE S04887 !$#authors Janeczko, R.A.; Ramirez, F. !$#journal Nucleic Acids Res. (1989) 17:6742 !$#title Nucleotide and amino acid sequences of the entire human !1alpha-1 (III) collagen. !$#cross-references MUID:89386015; PMID:2780304 !$#accession S04887 !'##molecule_type mRNA !'##residues 149-163,'G',164-240,'D',242-471,'D',473-487,'L',489,'S', !1491-613,'Y',615-634,'R',636-663,'E',665-1183,'S',1185-1202, !1'P',1204-1209,'A',1211-1225 ##label JAN !'##cross-references EMBL:X15332; NID:g29545; PIDN:CAA33387.1; !1PID:g930045 !'##note the authors' translation of residues 905-932 is inconsistent !1with the nucleotide sequence REFERENCE A90399 !$#authors Seyer, J.M.; Kang, A.H. !$#journal Biochemistry (1977) 16:1158-1164 !$#title Covalent structure of collagen: amino acid sequence of !1cyanogen bromide peptides from the amino-terminal segment of !1type III collagen of human liver. !$#cross-references MUID:77134724; PMID:557335 !$#accession A90399 !'##molecule_type protein !'##residues 'V',169-225,229-232,'P',234-292,'D',294-398 ##label SEY1 !'##experimental_source liver !'##note sequence corrected by A94562; attachment of !12-O-alpha-D-glucosyl-O-beta-D-galactose to 5-hydroxylysine REFERENCE A94562 !$#authors Seyer, J.M. !$#submission submitted to the Atlas, December 1977 !$#accession A94562 !'##molecule_type protein !'##residues 'V',169-225,229-277,'A',279-292,'D',294,'S',296-398 ##label !1SEY2 !'##experimental_source liver !'##note author submitted corrections to A90399 REFERENCE I51868 !$#authors Milewicz, D.M.; Witz, A.M.; Smith, A.C.; Manchester, D.K.; !1Waldstein, G.; Byers, P.H. !$#journal Am. J. Hum. Genet. (1993) 53:62-70 !$#title Parental somatic and germ-line mosaicism for a multiexon !1deletion with unusual endpoints in a type III collagen !1(COL3A1) allele produces Ehlers-Danlos syndrome type IV in !1the heterozygous offspring. !$#cross-references MUID:93304430; PMID:8317500 !$#accession I51868 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 186-194 ##label MIL !'##cross-references GB:S62925; NID:g386425; PIDN:AAD13937.1; !1PID:g4261637 REFERENCE S59511 !$#authors Chiodo, A.A.; Sillence, D.O.; Cole, W.G.; Bateman, J.F. !$#journal Biochem. J. (1995) 311:939-943 !$#title Abnormal type III collagen produced by an exon-17-skipping !1mutation of the COL3A1 gene in Ehlers-Danlos syndrome type !1IV is not incorporated into the extracellular matrix. !$#cross-references MUID:96067614; PMID:7487954 !$#accession S59511 !'##molecule_type mRNA !'##residues 302-423 ##label CHI !'##cross-references GB:S79877; NID:g1195576; PIDN:AAB35615.1; !1PID:g1195577 REFERENCE A90414 !$#authors Seyer, J.M.; Kang, A.H. !$#journal Biochemistry (1978) 17:3404-3411 !$#title Covalent structure of collagen: amino acid sequence of five !1consecutive CNBr peptides from type III collagen of human !1liver. !$#cross-references MUID:79000343; PMID:687591 !$#accession A90414 !'##molecule_type protein !'##residues 399-675,'N',677-727 ##label SEY3 !'##experimental_source liver REFERENCE I55349 !$#authors Lee, B.; Vitale, E.; Superti-Furga, A.; Steinmann, B.; !1Ramirez, F. !$#journal J. Biol. Chem. (1991) 266:5256-5259 !$#title G to T transversion at position +5 of a splice donor site !1causes skipping of the preceding exon in the type III !1procollagen transcripts of a patient with Ehlers-Danlos !1syndrome type IV. !$#cross-references MUID:91161621; PMID:1672129 !$#accession I55349 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 537-605 ##label LEE !'##cross-references GB:M59312; NID:g180815; PIDN:AAA52041.1; !1PID:g180816 REFERENCE A90438 !$#authors Seyer, J.M.; Mainardi, C.; Kang, A.H. !$#journal Biochemistry (1980) 19:1583-1589 !$#title Covalent structure of collagen: amino acid sequence of !1alpha1 (III)-CB5 from type III collagen of human liver. !$#cross-references MUID:80198282; PMID:6246925 !$#accession A90438 !'##molecule_type protein !'##residues 728-895,'A',897-964 ##label SEY4 !'##experimental_source liver REFERENCE A38303 !$#authors Cole, W.G.; Chiodo, A.A.; Lamande, S.R.; Janeczko, R.; !1Ramirez, F.; Dahl, H.H.M.; Chan, D.; Bateman, J.F. !$#journal J. Biol. Chem. (1990) 265:17070-17077 !$#title A base substitution at a splice site in the COL3A1 gene !1causes exon skipping and generates abnormal type III !1procollagen in a patient with Ehlers-Danlos syndrome type !1IV. !$#cross-references MUID:91009133; PMID:2145268 !$#accession A38303 !'##molecule_type mRNA !'##residues 861-1015 ##label COL !'##cross-references GB:J05617; GB:M55603; GB:M59227; NID:g180878; !1PIDN:AAB59383.1; PID:g180879 !'##note a mutant sequence with 942-977 spliced out from a patient with !1Ehlers-Danlos syndrome type IV REFERENCE S02119 !$#authors Mankoo, B.S.; Dalgleish, R. !$#journal Nucleic Acids Res. (1988) 16:2337 !$#title Human pro alpha1(III) collagen: cDNA sequence for the 3' !1end. !$#cross-references MUID:88189827; PMID:3357782 !$#accession S02119 !'##status translation not shown !'##molecule_type mRNA !'##residues 950-1018,'Y',1020-1183,'S',1185-1466 ##label MAN !'##cross-references EMBL:X06700; NID:g30053; PIDN:CAA29886.1; !1PID:g30054 REFERENCE A90446 !$#authors Seyer, J.M.; Kang, A.H. !$#journal Biochemistry (1981) 20:2621-2627 !$#title Covalent structure of collagen: amino acid sequence of !1alpha1 (III)-CB9 from type III collagen of human liver. !$#cross-references MUID:81208139; PMID:7016180 !$#accession A90446 !'##molecule_type protein !'##residues 965-979,'A',981-984,'PS',987,'QN',990-1096,'P',1098-1152, !1'AT',1155,'S',1157-1200 ##label SEY5 !'##experimental_source liver REFERENCE A93551 !$#authors Loidl, H.R.; Brinker, J.M.; May, M.; Pihlajaniemi, T.; !1Morrow, S.; Rosenbloom, J.; Myers, J.C. !$#journal Nucleic Acids Res. (1984) 12:9383-9394 !$#title Molecular cloning and carboxyl-propeptide analysis of human !1type III procollagen. !$#cross-references MUID:85087944; PMID:6096827 !$#accession A93551 !'##molecule_type mRNA !'##residues 1065-1155,'P',1157-1466 ##label LOI !'##cross-references EMBL:X01655; EMBL:X01742; NID:g29584; !1PIDN:CAA25821.1 REFERENCE I52393 !$#authors Miskulin, M.; Dalgleish, R.; Kluve-Beckerman, B.; Rennard, !1S.I.; Tolstoshev, P.; Brantly, M.; Crystal, R.G. !$#journal Biochemistry (1986) 25:1408-1413 !$#title Human type III collagen gene expression is coordinately !1modulated with the type I collagen genes during fibroblast !1growth. !$#cross-references MUID:86187804; PMID:3754462 !$#accession I52393 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1161-1200 ##label MIS !'##cross-references GB:M13146; NID:g180415; PIDN:AAA52003.1; !1PID:g180416 REFERENCE I59025 !$#authors Emanuel, B.S.; Cannizzaro, L.A.; Seyer, J.M.; Myers, J.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:3385-3389 !$#title Human alpha 1(III) and alpha 2(V) procollagen genes are !1located on the long arm of chromosome 2. !$#cross-references MUID:85216505; PMID:3858826 !$#accession I79359 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1165-1196 ##label EMA !'##cross-references GB:M11134; NID:g180417; PIDN:AAA52004.1; !1PID:g180418 REFERENCE A92516 !$#authors Chu, M.L.; Weil, D.; de Wet, W.; Bernard, M.; Sippola, M.; !1Ramirez, F. !$#journal J. Biol. Chem. (1985) 260:4357-4363 !$#title Isolation of cDNA and genomic clones encoding human !1pro-alpha1(III) collagen. Partial characterization of the 3' !1end region of the gene. !$#cross-references MUID:85157600; PMID:2579949 !$#accession A92516 !'##molecule_type DNA !'##residues 1176-1240,'V',1242-1356,'P',1358-1466 ##label CHU !'##cross-references GB:M10615; GB:M10793; GB:M10794; GB:M10795; !1GB:M10796; GB:M10797; GB:M10798; GB:M10799; GB:M10800; !1GB:M10801; NID:g180406; PIDN:AAA52002.1; PID:g180414 !'##experimental_source liver !'##note the authors translated the codon TTC for residue 1057 as Tyr; !1the codons given for 1052-Asp (CCT), 1065-Met (ATC), !11104-Ser (ACT), and 1162-Met (ATC) are inconsistent with the !1authors' translation COMMENT Prolines and lysines at the third position of the tripeptide !1repeating unit (G-X-Y) are hydroxylated to varying extents. !1Prolines are predominately 4-hydroxylated; no residues !1appear to be 3-hydroxylated. About 15% of the lysines are !15-hydroxylated and some are subsequently O-glycosylated. GENETICS !$#gene GDB:COL3A1 !'##cross-references GDB:118729; OMIM:120180 !$#map_position 2q31-2q31 !$#introns 27/1; 94/3; 111/3; 149/3; 176/3; 554/3; 587/3; 1175/3; 1275/ !11; 1337/3; 1418/3 !$#note the list of introns is incomplete; defects in this gene can !1result in Ehlers-Danlos syndrome type IV COMPLEX type III collagen is a homotrimer of monomers initially !1linked by disulfide bonds among their carboxy-terminal !1propeptides; a polymer of collagen trimers, offset by !1approximately one-quarter of their length, is formed with !1desmosine cross-links made from lysine and allysine residues FUNCTION !$#description structural component of extracellular fibrous polymer that !1maintains integrity, along with type I collagen, of skin, !1aorta, lung, liver, and other soft connective tissues CLASSIFICATION #superfamily collagen alpha 1(I) chain; fibrillar collagen !1carboxyl-terminal homology; von Willebrand factor type C !1repeat homology KEYWORDS coiled coil; Ehlers-Danlos syndrome; extracellular matrix; !1glycoprotein; hydroxylysine; hydroxyproline; liver; lung; !1pyroglutamic acid; skin; trimer; triple helix FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-153 #domain amino-terminal propeptide #status predicted !8#label PRO\ !$31-91 #domain von Willebrand factor type C repeat homology !8#label VWC\ !$154-1221 #product collagen alpha 1(III) chain #status !8predicted #label MAT\ !$154-167 #region amino-terminal nonhelical telopeptide\ !$168-1196 #region helical\ !$1091-1093 #region cell attachment (R-G-D) motif\ !$1197-1221 #region carboxyl-terminal nonhelical telopeptide\ !$1222-1466 #domain carboxyl-terminal propeptide #status !8predicted #label CPR\ !$1238-1466 #domain fibrillar collagen carboxyl-terminal homology !8#label FCC\ !$24 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status predicted\ !$153-154 #cleavage_site Pro-Gln (procollagen N-endopeptidase) !8#status predicted\ !$154 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status predicted\ !$161,1212 #modified_site allysine (Lys) #status predicted\ !$263,284,860,977, !$1106 #modified_site 5-hydroxylysine (Lys) #status !8experimental\ !$263 #binding_site carbohydrate (Lys) (covalent) #status !8experimental\ !$584,1094 #modified_site 5-hydroxylysine (Lys) (partial) !8#status experimental\ !$948-949 #cleavage_site Gly-Ile (collagenase) #status !8experimental\ !$1106 #binding_site carbohydrate (Lys) (covalent) #status !8predicted\ !$1162 #modified_site 3-hydroxyproline (Pro) #status absent\ !$1196,1197 #disulfide_bonds interchain #status predicted\ !$1221-1222 #cleavage_site Gly-Asp (procollagen C-endopeptidase) !8#status predicted\ !$1262,1268,1285,1294 #disulfide_bonds interchain #status predicted\ !$1302-1464,1372-1417 #disulfide_bonds #status predicted\ !$1367 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1466 #molecular-weight 138527 #checksum 7106 SEQUENCE /// ENTRY CGBO7S #type complete TITLE collagen alpha 1(III) chain - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 07-May-1999 ACCESSIONS A02862; A38001; A38002; A38003; A38004; A38005; S71946 REFERENCE A02862 !$#authors Fietzek, P.P.; Allmann, H.; Rauterberg, J.; Henkel, W.; !1Wachter, E.; Kuehn, K. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1979) 360:809-820 !$#title The covalent structure of calf skin type III collagen. I. !1The amino acid sequence of the amino terminal region of the !1alpha1(III) chain (position 1-222). !$#cross-references MUID:80026026; PMID:488906 !$#accession A02862 !'##molecule_type protein !'##residues 1-242 ##label FIE REFERENCE A38001 !$#authors Dewes, H.; Fietzek, P.P.; Kuehn, K. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1979) 360:821-832 !$#title The covalent structure of calf skin type III collagen. II. !1The amino acid sequence of the cyanogen bromide peptide !1alpha1(III)CB1,8,10,2 (positions 223-402). !$#cross-references MUID:80026027; PMID:488907 !$#accession A38001 !'##molecule_type protein !'##residues 243-422 ##label DEW1 REFERENCE A38002 !$#authors Bentz, H.; Fietzek, P.P.; Kuehn, K. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1979) 360:833-840 !$#title The covalent structure of calf skin type III collagen. III. !1The amino acid sequence of the cyanogen bromide peptide !1alpha1(III)CB4 (positions 403-551). !$#cross-references MUID:80026028; PMID:488908 !$#accession A38002 !'##molecule_type protein !'##residues 423-571 ##label BEN REFERENCE A38003 !$#authors Lang, H.; Glanville, R.W.; Fietzek, P.P.; Kuehn, K. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1979) 360:841-850 !$#title The covalent structure of calf skin type III collagen. IV. !1The amino acid sequence of the cyanogen bromide peptide !1alpha1(III)CB5 (positions 552-788). !$#cross-references MUID:80026029; PMID:488909 !$#accession A38003 !'##molecule_type protein !'##residues 572-808 ##label LAN REFERENCE A38004 !$#authors Dewes, H.; Fietzek, P.P.; Kuehn, K. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1979) 360:851-860 !$#title The covalent structure of calf skin type III collagen. V. !1The amino acid sequence of the cyanogen bromide peptide !1alpha1(III)CB9A (position 789 to 927). !$#cross-references MUID:80026030; PMID:488910 !$#accession A38004 !'##molecule_type protein !'##residues 809-947 ##label DEW2 REFERENCE A38005 !$#authors Allmann, H.; Fietzek, P.P.; Glanville, R.W.; Kuehn, K. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1979) 360:861-868 !$#title The covalent structure of calf skin type III collagen. VI. !1The amino acid sequence of the carboxyterminal cyanogen !1bromide peptide alpha1(III)CB9B (position 928-1028). !$#cross-references MUID:80026031; PMID:488911 !$#accession A38005 !'##molecule_type protein !'##residues 948-1049 ##label ALL !'##experimental_source skin REFERENCE S71946 !$#authors Henkel, W. !$#journal Biochem. J. (1996) 318:497-503 !$#title Cross-link analysis of the C-telopeptide domain from type !1III collagen. !$#cross-references MUID:96404897; PMID:8809038 !$#accession S71946 !'##molecule_type protein !'##residues 87-106;1017-1029;1037-1049 ##label HEN COMMENT Prolines at the third position of the tripeptide repeating !1unit (G-X-Y) are hydroxylated in some or all of the chains. COMMENT The type III collagen molecule is a trimer of identical !1chains, linked to each other by interchain disulfide bonds. !1Trimers are also cross-linked by allysines forming !1desmosine. CLASSIFICATION #superfamily collagen alpha 1(I) chain; fibrillar collagen !1carboxyl-terminal homology; von Willebrand factor type C !1repeat homology KEYWORDS coiled coil; extracellular matrix; glycoprotein; !1hydroxylysine; hydroxyproline; skin; trimer; triple helix FEATURE !$1-1049 #product collagen alpha 1(III) chain #status !8experimental #label CAB\ !$1-14 #region amino-terminal nonhelical telopeptide\ !$15-1040 #region helical\ !$587-589 #region cell attachment (R-G-D) motif\ !$752-754 #region cell attachment (R-G-D) motif\ !$875-877 #region cell attachment (R-G-D) motif\ !$878-880 #region cell attachment (R-G-D) motif\ !$935-937 #region cell attachment (R-G-D) motif\ !$1041-1049 #region carboxyl-terminal nonhelical telopeptide\ !$95,107,119,938,950 #modified_site 5-hydroxylysine (Lys) #status !8experimental\ !$107,950 #modified_site allysine (Lys) #status predicted\ !$107 #binding_site carbohydrate (Lys) (covalent) #status !8experimental\ !$1040,1041 #disulfide_bonds interchain #status predicted SUMMARY #length 1049 #molecular-weight 93651 #checksum 6665 SEQUENCE /// ENTRY CGHU2V #type complete TITLE collagen alpha 2(V) chain precursor - human ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Jul-1989 #sequence_revision 28-Jul-1995 #text_change 31-Dec-2000 ACCESSIONS A31427; A54555; S43643; A25874; I55239; I59025; A25374; !1A30017 REFERENCE A31427 !$#authors Woodbury, D.; Benson-Chanda, V.; Ramirez, F. !$#journal J. Biol. Chem. (1989) 264:2735-2738 !$#title Amino-terminal propeptide of human pro-alpha2(V) collagen !1conforms to the structural criteria of a fibrillar !1procollagen molecule. !$#cross-references MUID:89123368; PMID:2914927 !$#accession A31427 !'##molecule_type mRNA !'##residues 1-463 ##label WOO !'##cross-references GB:J04478; NID:g179697; PIDN:AAA51859.1; !1PID:g179698 !'##experimental_source placenta REFERENCE A54555 !$#authors Greenspan, D.S.; Lee, S.T.; Lee, B.S.; Hoffman, G.G. !$#journal Gene Expr. (1991) 1:29-39 !$#title Homology between alpha2(V) and alpha1(III) collagen !1promoters and evidence for negatively acting elements in the !1alpha2(V) first intron and 5' flanking sequences. !$#cross-references MUID:92314691; PMID:1820205 !$#accession A54555 !'##molecule_type DNA !'##residues 1-32 ##label GRE !'##cross-references GB:M58529; NID:g180834; PIDN:AAC41699.1; !1PID:g553235 REFERENCE S43642 !$#authors Moradi-Ameli, M.; Rousseau, J.C.; Kleman, J.P.; Champliaud, !1M.F.; Boutillon, M.M.; Bernillon, J.; Wallach, J.; van der !1Rest, M. !$#journal Eur. J. Biochem. (1994) 221:987-995 !$#title Diversity in the processing events at the N-terminus of !1type-V collagen. !$#cross-references MUID:94237164; PMID:8181482 !$#accession S43643 !'##molecule_type protein !'##residues 288-291,'P',293-294,'X',296-297;606,'X',608-617 ##label MOR REFERENCE A25874 !$#authors Weil, D.; Bernard, M.; Gargano, S.; Ramirez, F. !$#journal Nucleic Acids Res. (1987) 15:181-198 !$#title The pro alpha 2(V) collagen gene is evolutionarily related !1to the major fibrillar-forming collagens. !$#cross-references MUID:87146331; PMID:3029669 !$#accession A25874 !'##molecule_type mRNA; DNA !'##residues 398-1496 ##label WEI !'##cross-references GB:X04758; NID:g29588; PIDN:CAA28454.1; !1PID:g1340175 !'##experimental_source rhabdomyosarcoma cell line REFERENCE I55239 !$#authors Myers, J.C.; Loidl, H.R.; Stolle, C.A.; Seyer, J.M. !$#journal J. Biol. Chem. (1985) 260:5533-5541 !$#title Partial covalent structure of the human alpha 2 type V !1collagen chain. !$#cross-references MUID:85182703; PMID:2985598 !$#accession I55239 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1002-1226 ##label RE2 !'##cross-references GB:M10956; NID:g180427; PIDN:AAA52007.1; !1PID:g180428 !'##note part of this sequence were determined by protein sequencing REFERENCE I59025 !$#authors Emanuel, B.S.; Cannizzaro, L.A.; Seyer, J.M.; Myers, J.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:3385-3389 !$#title Human alpha 1(III) and alpha 2(V) procollagen genes are !1located on the long arm of chromosome 2. !$#cross-references MUID:85216505; PMID:3858826 !$#accession I59025 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1003-1034 ##label RES !'##cross-references GB:M11135; NID:g179693; PIDN:AAA51857.1; !1PID:g179694 !'##note part of this sequence were determined by protein sequencing REFERENCE A25374 !$#authors Myers, J.C.; Loidl, H.R.; Seyer, J.M.; Dion, A.S. !$#journal J. Biol. Chem. (1985) 260:11216-11222 !$#title Complete primary structure of the human alpha-2 type V !1procollagen COOH-terminal propeptide. !$#cross-references MUID:85289337; PMID:2411731 !$#accession A25374 !'##molecule_type mRNA !'##residues 1227-1417,'T',1419-1437,'S',1439-1496 ##label MYE !'##cross-references GB:M11718; NID:g180912; PIDN:AAA52058.1; !1PID:g180913 !'##experimental_source normal fibroblasts REFERENCE A30017 !$#authors Tsipouras, P.; Schwartz, R.C.; Liddell, A.C.; Salkeld, C.S.; !1Weil, D.; Ramirez, F. !$#journal Genomics (1988) 3:275-277 !$#title Genetic distance of two fibrillar collagen loci, COL3A1 and !1COL5A2, located on the long arm of human chromosome 2. !$#cross-references MUID:89138450; PMID:3224983 !$#accession A30017 !'##molecule_type DNA !'##residues 1449-1463,'E',1465-1495,'A' ##label TSI !'##cross-references GB:J03051; NID:g179695; PIDN:AAA51858.1; !1PID:g179696 !'##note the authors translated the codon GAA for residue 1460 as Gln, !1and GAG for residue 1464 as Gln COMMENT Prolines and lysines at the third position of the tripeptide !1repeating unit (G-X-Y) are hydroxylated to varying extents. !1Prolines are predominately 4-hydroxylated. About 50% of the !1lysines are 5-hydroxylated and subsequently O-glycosylated. COMMENT The amino-terminal propeptide domain appears not to be !1completely cleaved. GENETICS !$#gene GDB:COL5A2 !'##cross-references GDB:119064; OMIM:120190 !$#map_position 2q31-2q31 !$#introns 33/1; 812/3; 830/3; 848/3; 884/3; 902/3; 922/3; 974/3; 1046/ !13; 1064/3; 1448/3 #status incomplete COMPLEX type V collagen may be a homotrimer of alpha 1(V) chains !1(see PIR:CGHU1V), a heterotrimer of two alpha 1(V) chains !1and one alpha 2(V) chain, or a heterotrimer of one alpha 1 !1(V) chain, one alpha 2(V) chain and one alpha 3(V) chain, !1initially linked by disulfide bonds among their !1carboxyl-terminal propeptides; a polymer of collagen !1trimers, offset by approximately one-quarter of their !1length, is formed with desmosine cross-links made from !1lysine and allysine residues FUNCTION !$#description structural component of extracellular fibrous polymer !1associated with cell surfaces and interstitial fibrils; !1widely distributed but least abundant of the fibrillar !1collagens !$#note may play a role in controlling the lateral growth of !1collagen I fibrils CLASSIFICATION #superfamily collagen alpha 1(I) chain; fibrillar collagen !1carboxyl-terminal homology; von Willebrand factor type C !1repeat homology KEYWORDS coiled coil; extracellular matrix; glycoprotein; !1hydroxylysine; hydroxyproline; pyroglutamic acid; trimer; !1triple helix FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-1250 #product collagen alpha 2(V) chain #status predicted !8#label MAT\ !$27-193 #domain amino-terminal propeptide (uncleaved) #status !8predicted #label NPP\ !$27-108 #region nonhelical\ !$40-99 #domain von Willebrand factor type C repeat homology !8#label VWC\ !$109-186 #region helical\ !$187-208 #region nonhelical\ !$209-1225 #region helical\ !$503-505 #region cell attachment (R-G-D) motif\ !$941-943 #region cell attachment (R-G-D) motif\ !$1064-1066 #region cell attachment (R-G-D) motif\ !$1067-1069 #region cell attachment (R-G-D) motif\ !$1097-1099 #region cell attachment (R-G-D) motif\ !$1124-1126 #region cell attachment (R-G-D) motif\ !$1133-1135 #region cell attachment (R-G-D) motif\ !$1225-1250 #region carboxyl-terminal nonhelical telopeptide\ !$1251-1496 #domain carboxyl-terminal propeptide #status !8predicted #label CPP\ !$1269-1496 #domain fibrillar collagen carboxyl-terminal homology !8#label FCC\ !$27 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status predicted\ !$193-194 #cleavage_site Ala-Gln (procollagen N-endopeptidase) !8#status predicted\ !$194 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status predicted\ !$201 #modified_site allysine (Lys) #status predicted\ !$290,293,296,608, !$614,1004,1007,1013, !$1028,1034 #modified_site 4-hydroxyproline (Pro) #status !8experimental\ !$299,1139 #modified_site 5-hydroxylysine (Lys) #status !8predicted\ !$299,1139 #binding_site carbohydrate (Lys) (covalent) #status !8predicted\ !$1025 #modified_site 5-hydroxylysine (Lys) #status !8experimental\ !$1250-1251 #cleavage_site Glu-Asp (procollagen C-endopeptidase) !8#status predicted\ !$1259,1397 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$1293,1299,1325 #disulfide_bonds interchain #status predicted\ !$1333-1494,1402-1447 #disulfide_bonds #status predicted SUMMARY #length 1496 #molecular-weight 144720 #checksum 4764 SEQUENCE /// ENTRY CGHU2S #type complete TITLE collagen alpha 2(I) chain precursor - human ALTERNATE_NAMES procollagen alpha 2(I) chain ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1989 #sequence_revision 25-Aug-1995 #text_change 21-Jul-2000 ACCESSIONS A28500; S00824; S09176; I55311; A58111; A28472; A42165; !1A34405; A90567; I55264; I55485; B92069; A91224; I59125; !1S09174; I68663; I55369; A56799; S10768; A18855; I55285; !1I70059; S09175; I59005; A02865 REFERENCE A28500 !$#authors de Wet, W.; Bernard, M.; Benson-Chanda, V.; Chu, M.L.; !1Dickson, L.; Weil, D.; Ramirez, F. !$#journal J. Biol. Chem. (1987) 262:16032-16036 !$#title Organization of the human pro-alpha-2(I) collagen gene. !$#cross-references MUID:88058962; PMID:2824475 !$#accession A28500 !'##molecule_type DNA; mRNA !'##residues 1-248,'N',250-1366 ##label DEW !'##cross-references GB:J03464; NID:g179595; PIDN:AAB59374.1; !1PID:g179596 REFERENCE S00824 !$#authors Kuivaniemi, H.; Tromp, G.; Chu, M.L.; Prockop, D.J. !$#journal Biochem. J. (1988) 252:633-640 !$#title Structure of a full-length cDNA clone for the prepro-alpha-2 !1(I) chain of human type I procollagen. Comparison with the !1chicken gene confirms unusual patterns of gene conservation. !$#cross-references MUID:88339824; PMID:3421913 !$#accession S00824 !'##molecule_type mRNA !'##residues 1-275,'A',277-332,'V',334-337,'A',339-482,'A',484-548,'D', !1550-765 ##label KUI1 !'##cross-references EMBL:Y00724; NID:g30022; PIDN:CAA68709.1; !1PID:g30023 REFERENCE S09176 !$#authors Dickson, L.A.; de Wet, W.; di Liberto, M.; Weil, D.; !1Ramirez, F. !$#journal Nucleic Acids Res. (1985) 13:3427-3438 !$#title Analysis of the promoter region and the N-propeptide domain !1of the human proalpha-2(I) collagen gene. !$#cross-references MUID:85242047; PMID:4011429 !$#accession S09176 !'##molecule_type DNA !'##residues 1-23;33-58,'P',60-93 ##label DIC !'##cross-references EMBL:X02488; NID:g30098; PIDN:CAA26320.1; !1PID:g30099 REFERENCE I55311 !$#authors Weil, D.; D'Alessio, M.; Ramirez, F.; Eyre, D.R. !$#journal J. Biol. Chem. (1990) 265:16007-16011 !$#title Structural and functional characterization of a splicing !1mutation in the pro-alpha 2(I) collagen gene of an !1Ehlers-Danlos type VII patient. !$#cross-references MUID:90368825; PMID:2394758 !$#accession I55311 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 76-93 ##label WEI1 !'##cross-references GB:M35391; NID:g189684; PIDN:AAA60041.1; !1PID:g189685 !$#accession A58111 !'##molecule_type protein !'##residues 23-75,94-96 ##label WEI2 !'##note mutant sequence from a patient with Ehlers-Danlos syndrome type !1VII REFERENCE A28472 !$#authors Wirtz, M.K.; Glanville, R.W.; Steinmann, B.; Rao, V.H.; !1Hollister, D.W. !$#journal J. Biol. Chem. (1987) 262:16376-16385 !$#title Ehlers-Danlos syndrome type VIIB. Deletion of 18 amino acids !1comprising the N-telopeptide region of a pro-alpha-2(I) !1chain. !$#cross-references MUID:88059013; PMID:3680255 !$#accession A28472 !'##molecule_type protein !'##residues 32-75,94-111 ##label WIR !'##note mutant sequence of patient with Ehlers-Danlos syndrome type !1VIIB REFERENCE A42165 !$#authors Chiodo, A.A.; Hockey, A.; Cole, W.G. !$#journal J. Biol. Chem. (1992) 267:6361-6369 !$#title A base substitution at the splice acceptor site of intron 5 !1of the COL1A2 gene activates a cryptic splice site within !1exon 6 and generates abnormal type I procollagen in a !1patient with Ehlers-Danlos syndrome type VII. !$#cross-references MUID:92210617; PMID:1556139 !$#accession A42165 !'##molecule_type mRNA !'##residues 50-126 ##label CHI !'##note parts of this sequence were determined by protein sequencing; a !1mutant sequence lacking 76-80 is described REFERENCE A34405 !$#authors Weil, D.; D'Alessio, M.; Ramirez, F.; Steinmann, B.; Wirtz, !1M.K.; Glanville, R.W.; Hollister, D.W. !$#journal J. Biol. Chem. (1989) 264:16804-16809 !$#title Temperature-dependent expression of a collagen splicing !1defect in the fibroblasts of a patient with Ehlers-Danlos !1syndrome type VII. !$#cross-references MUID:89380311; PMID:2777808 !$#accession A34405 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 58-108 ##label WEI3 !'##cross-references GB:J05049 !'##note the accession cited by the authors is not found in GenBank !'##note parts of this sequence were determined by protein sequencing; a !1mutant having 93-Ile or lacking 76-93 depending on !1temperature is described REFERENCE A90567 !$#authors Click, E.M.; Bornstein, P. !$#journal Biochemistry (1970) 9:4699-4706 !$#title Isolation and characterization of the cyanogen bromide !1peptides from the alpha1 and alpha2 chains of human skin !1collagen. !$#cross-references MUID:71038625; PMID:5529814 !$#accession A90567 !'##molecule_type protein !'##residues 'Z',81,'B',83-96;417-447 ##label CLI !'##note the compositions of peptides CNBr1, CNBr0, and CNBr2 were !1determined; evidence for 84-allysine REFERENCE I55264 !$#authors Kuivaniemi, H.; Sabol, C.; Tromp, G.; Sippola-Thiele, M.; !1Prockop, D.J. !$#journal J. Biol. Chem. (1988) 263:11407-11413 !$#title A 19-base pair deletion in the pro-alpha 2(I) gene of type I !1procollagen that causes in-frame RNA splicing from exon 10 !1to exon 12 in a proband with atypical osteogenesis !1imperfecta and in his asymptomatic mother. !$#cross-references MUID:88298792; PMID:3403536 !$#accession I55264 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA; mRNA !'##residues 145-197 ##label KUI2 !'##cross-references GB:M21671; NID:g189521; PIDN:AAA59994.1; !1PID:g553606 !'##note single base mutation in intron leads to abnormal splicing of !1mRNA REFERENCE I55485 !$#authors Chipman, S.D.; Shapiro, J.R.; McKinstry, M.B.; Stover, M.L.; !1Branson, P.; Rowe, D.W. !$#journal J. Bone Miner. Res. (1992) 7:793-805 !$#title Expression of mutant alpha (I)-procollagen in osteoblast and !1fibroblast cultures from a proband with osteogenesis !1imperfecta type IV. !$#cross-references MUID:92351816; PMID:1642148 !$#accession I55485 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 163-181,200-213 ##label CH2 !'##cross-references GB:S41099; NID:g252702; PIDN:AAB22761.1; !1PID:g252703 !'##note mutant sequence from a patient with osteogenesis imperfecta !1type IV REFERENCE A92069 !$#authors Morgan, P.H.; Jacobs, H.G.; Segrest, J.P.; Cunningham, L.W. !$#journal J. Biol. Chem. (1970) 245:5042-5048 !$#title Comparative study of glycopeptides derived from selected !1vertebrate collagens. A possible role of the carbohydrate in !1fibril formation. !$#cross-references MUID:71001508; PMID:4319110 !$#accession B92069 !'##molecule_type protein !'##residues 175-180 ##label MOR !'##experimental_source skin !'##note attachment of 2-O-alpha-D-glucosyl-O-beta-D-galactose to !15-hydroxylysine REFERENCE A91224 !$#authors Fietzek, P.P.; Furthmayr, H.; Kuehn, K. !$#journal Eur. J. Biochem. (1974) 47:257-261 !$#title Comparative sequence studies on alpha2-CB2 from calf, human, !1rabbit and pig-skin collagen. !$#cross-references MUID:75008198; PMID:4412529 !$#accession A91224 !'##molecule_type protein !'##residues 418-447 ##label FIE REFERENCE I59125 !$#authors Tromp, G.; Prockop, D.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:5254-5258 !$#title Single base mutation in the pro alpha 2(I) collagen gene !1that causes efficient splicing of RNA from exon 27 to exon !129 and synthesis of a shortened but in-frame pro alpha 2(I) !1chain. !$#cross-references MUID:88276936; PMID:2839839 !$#accession I59125 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 520-573 ##label TRO !'##cross-references GB:M21353; NID:g180881; PIDN:AAA52053.1; !1PID:g180882 !'##note single base mutation in intron leads to splicing out of exon 28 REFERENCE S09174 !$#authors Bernard, M.P.; Myers, J.C.; Chu, M.L.; Ramirez, F.; !1Eikenberry, E.F.; Prockop, D.J. !$#journal Biochemistry (1983) 22:1139-1145 !$#title Structure of a cDNA for the proalpha-2 chain of human type I !1procollagen. Comparison with chick cDNA for proalpha-2(I) !1identifies structurally conserved features of the protein !1and the gene. !$#cross-references MUID:83178919; PMID:6687691 !$#accession S09174 !'##molecule_type mRNA !'##residues 623-742,'A',744-764,'X',766-827,'A',829-830,'P',832-836, !1'P',838-1097,'L',1099-1100,'L',1102-1366 ##label BER !'##cross-references GB:J00115; GB:V00503; NID:g30123; PIDN:CAA23761.1; !1PID:g825646 !'##experimental_source skin fibroblast cells REFERENCE I54365 !$#authors Forlino, A.; Zolezzi, F.; Valli, M.; Pignatti, P.F.; Cetta, !1G.; Brunelli, P.C.; Mottes, M. !$#journal Hum. Mol. Genet. (1994) 3:2201-2206 !$#title Severe (type III) osteogenesis imperfecta due to glycine !1substitutions in the central domain of the collagen triple !1helix. !$#cross-references MUID:95187161; PMID:7881420 !$#accession I68663 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 663-675,'V',677,'P',679-742,'A',744-746 ##label FOR !'##cross-references GB:L47668; NID:g1009095; PIDN:AAB59577.1; !1PID:g1009096 REFERENCE I55369 !$#authors Niyibizi, C.; Bonadio, J.; Byers, P.H.; Eyre, D.R. !$#journal J. Biol. Chem. (1992) 267:23108-23112 !$#title Incorporation of type I collagen molecules that contain a !1mutant alpha 2(I) chain (Gly580-->Asp) into bone matrix in a !1lethal case of osteogenesis imperfecta. !$#cross-references MUID:93054637; PMID:1385413 !$#accession I55369 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 665-666,'D',668-670 ##label NIY !'##cross-references GB:L00613; NID:g180888; PIDN:AAB59384.1; !1PID:g180889 !'##note mutant sequence from a patient with osteogenesis imperfecta REFERENCE A56799 !$#authors Bateman, J.F.; Hannagan, M.; Chan, D.; Cole, W.G. !$#journal Biochem. J. (1991) 276:765-770 !$#title Characterization of a type I collagen alpha 2(I) glycine-586 !1to valine substitution in osteogenesis imperfecta type IV. !1Detection of the mutation and prenatal diagnosis by a !1chemical cleavage method. !$#cross-references MUID:91291136; PMID:2064612 !$#accession A56799 !'##molecule_type mRNA !'##residues 672-675,'V',677,'P',679-681 ##label BAT !'##cross-references GB:S39878; NID:g1679911; PIDN:AAB19314.1; !1PID:g232761 !'##note sequence extracted from NCBI backbone (NCBIN:39878, !1NCBIP:39886) !'##note mutant sequence of patient with osteogenesis imperfecta type !1IV; the authors suggest the change at 676 caused the !1disease; the change at 678 was seen in both the mutant !1sequence and in the control sequence REFERENCE S10768 !$#authors Maekelae, J.K.; Vuorio, T.; Vuorio, E. !$#journal Biochim. Biophys. Acta (1990) 1049:171-176 !$#title Growth-dependent modulation of type I collagen production !1and mRNA levels in cultured human skin fibroblasts. !$#cross-references MUID:90304220; PMID:2364107 !$#accession S10768 !'##molecule_type mRNA !'##residues 960-1021,'L',1023-1188,'D',1190-1197,'S',1199-1356 ##label !1MAE !'##cross-references EMBL:X55525; NID:g30101; PIDN:CAA39142.1; !1PID:g30102 !'##experimental_source fibroblast cell culture REFERENCE A18855 !$#authors Myers, J.C.; Chu, M.L.; Faro, S.H.; Clark, W.J.; Prockop, !1D.J.; Ramirez, F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:3516-3520 !$#title Cloning a cDNA for the pro-alpha2 chain of human type I !1collagen. !$#cross-references MUID:81273090; PMID:6267597 !$#accession A18855 !'##molecule_type mRNA !'##residues 964-979,'V',981-1018,'Q',1020 ##label MYE !'##cross-references GB:J00114; NID:g180393; PIDN:AAA51996.1; !1PID:g180394 !'##note 1019-Leu was also found REFERENCE I55285 !$#authors Wenstrup, R.J.; Cohn, D.H.; Cohen, T.; Byers, P.H. !$#journal J. Biol. Chem. (1988) 263:7734-7740 !$#title Arginine for glycine substitution in the triple-helical !1domain of the products of one alpha 2(I) collagen allele !1(COL1A2) produces the osteogenesis imperfecta type IV !1phenotype. !$#cross-references MUID:88227975; PMID:2897363 !$#accession I55285 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1090-1107 ##label WEN1 !'##cross-references GB:M22816; NID:g179602; PIDN:AAA51844.1; !1PID:g179603 !$#accession I70059 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1090-1101,'R',1103-1107 ##label WEN2 !'##cross-references GB:M22817; NID:g179606; PIDN:AAA51846.1; !1PID:g179607 !'##note mutant sequence from a patient with osteogenesis imperfecta !1type IV REFERENCE S09175 !$#authors Myers, J.C.; Dickson, L.A.; de Wet, W.J.; Bernard, M.P.; !1Chu, M.L.; di Liberto, M.; Pepe, G.; Sangiorgi, F.O.; !1Ramirez, F. !$#journal J. Biol. Chem. (1983) 258:10128-10135 !$#title Analysis of the 3' end of the human pro-alpha-2(I) collagen !1gene. Utilization of multiple polyadenylation sites in !1cultured fibroblasts. !$#cross-references MUID:83290853; PMID:6309769 !$#accession S09175 !'##molecule_type DNA !'##residues 1319-1366 ##label MY2 !'##cross-references GB:K01078; NID:g179598; PIDN:AAA51887.1; !1PID:g179601 REFERENCE I59005 !$#authors Dickson, L.A.; Pihlajaniemi, T.; Deak, S.; Pope, F.M.; !1Nicholls, A.; Prockop, D.J.; Myers, J.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:4524-4528 !$#title Nuclease S1 mapping of a homozygous mutation in the !1carboxyl-propeptide-coding region of the pro alpha 2(I) !1collagen gene in a patient with osteogenesis imperfecta. !$#cross-references MUID:84272668; PMID:6087329 !$#accession I59005 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1319-1337,'A',1339-1349 ##label DI2 !'##cross-references GB:K02046; NID:g180389; PIDN:AAA51994.1; !1PID:g180390 !'##note the authors translated the codon GCG for residue 1338 as Arg; !1the mutant sequence has an unidentified mismatch in the !1region for residues 1328-1333 COMMENT Collagen is the most abundant protein in the vertebrate !1body. COMMENT Prolines and lysines at the third position of the tripeptide !1repeating unit (G-X-Y) are hydroxylated to varying extents. !1Prolines are predominately 4-hydroxylated; about 1 residue !1in 1000 are 3-hydroxylated. About 10% of the lysines are !15-hydroxylated and subsequently O-glycosylated. GENETICS !$#gene GDB:COL1A2 !'##cross-references GDB:119062; OMIM:120160 !$#map_position 7q22.1-7q22.1 !$#introns 24/1; 27/3; 32/3; 44/3; 75/3; 93/3; 108/3; 126/3; 144/3; !1162/3; 180/3; 198/3; 213/3; 231/3; 246/3; 264/3; 297/3; 312/ !13; 345/3; 363/3; 399/3; 417/3; 450/3; 468/3; 501/3; 519/3; !1537/3; 555/3; 573/3; 588/3; 621/3; 657/3; 675/3; 693/3; 711/ !13; 729/3; 765/3; 783/3; 801/3; 855/3; 891/3; 927/3; 945/3; !1981/3; 999/3; 1035/3; 1053/3; 1089/3; 1176/1; 1237/3; 1318/3 !$#note defects in this gene can result in perinatal lethal !1osteogenesis imperfecta, or type VIIB Ehlers-Danlos syndrome COMPLEX type I collagen heterotrimer, tropocollagen, is composed of !1two alpha 1(I) chains (see PIR:CGHU1S) and one alpha 2(I) !1chain, initially linked by disulfide bonds among their !1carboxyl-terminal propeptides; a polymer of collagen !1trimers, offset by approximately one-quarter of their !1length, is formed with desmosine cross-links made from !1lysine and allysine residues FUNCTION !$#description structural component of extracellular fibrous polymer that !1maintains integrity of tendons, ligaments, skin, and bone CLASSIFICATION #superfamily collagen alpha 2(I) chain; fibrillar collagen !1carboxyl-terminal homology KEYWORDS bone; coiled coil; Ehlers-Danlos syndrome; extracellular !1matrix; glycoprotein; hydroxylysine; hydroxyproline; !1pyroglutamic acid; skin; trimer; triple helix FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-79 #domain amino-terminal propeptide #status predicted !8#label PRO\ !$80-1119 #product collagen alpha 2(I) chain #status predicted !8#label MAT\ !$80-90 #region amino-terminal nonhelical telopeptide\ !$91-1107 #region helical\ !$777-779 #region cell attachment (R-G-D) motif\ !$822-824 #region cell attachment (R-G-D) motif\ !$1005-1007 #region cell attachment (R-G-D) motif\ !$1108-1119 #region carboxyl-terminal nonhelical telopeptide\ !$1120-1366 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$1139-1366 #domain fibrillar collagen carboxyl-terminal homology !8#label FCC\ !$23 #modified_site pyrrolidone carboxylic acid (Gln) (in !8precursor form) #link PRO #status experimental\ !$47,50,62,65,68,71, !$102,108,420 #modified_site 4-hydroxyproline (Pro) #status !8experimental\ !$79-80 #cleavage_site Ala-Gln (procollagen N-endopeptidase) !8#status experimental\ !$80 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #link MAT #status experimental\ !$84 #modified_site allysine (Lys) #status experimental\ !$177 #modified_site 5-hydroxylysine (Lys) #status !8experimental\ !$177 #binding_site carbohydrate (Lys) (covalent) #status !8experimental\ !$1023 #binding_site carbohydrate (Lys) (covalent) #status !8predicted\ !$1023 #modified_site 5-hydroxylysine (Lys) #status !8predicted\ !$1119-1120 #cleavage_site Ala-Asp (procollagen C-endopeptidase) !8#status experimental\ !$1163,1186,1195 #disulfide_bonds interchain #status predicted\ !$1203-1364,1272-1317 #disulfide_bonds #status predicted\ !$1267 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1366 #molecular-weight 129467 #checksum 5474 SEQUENCE /// ENTRY A43291 #type complete TITLE collagen alpha 2(I) chain precursor - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A43291; A54328 REFERENCE A43291 !$#authors Phillips, C.L.; Morgan, A.L.; Lever, L.W.; Wenstrup, R.J. !$#journal Genomics (1992) 13:1345-1346 !$#title Sequence analysis of a full-length cDNA for the murine pro !1alpha 2(I) collagen chain: comparison of the derived primary !1structure with human pro alpha 2(I) collagen. !$#cross-references MUID:92372043; PMID:1505972 !$#accession A43291 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-1373 ##label PHI !'##cross-references GB:X58251; NID:g50488; PIDN:CAA41205.1; PID:g50489 !'##note sequence extracted from NCBI backbone (NCBIP:112027) REFERENCE A54328 !$#authors Phillips, C.L.; Lever, L.W.; Pinnell, S.R.; Quarles, L.D.; !1Wenstrup, R.J. !$#journal J. Invest. Dermatol. (1991) 97:980-984 !$#title Construction of a full-length murine Proalpha2(I) collagen !1cDNA by the polymerase chain reaction. !$#cross-references MUID:92084969; PMID:1748823 !$#accession A54328 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-110 ##label PH2 GENETICS !$#gene COL1A2 CLASSIFICATION #superfamily collagen alpha 2(I) chain; fibrillar collagen !1carboxyl-terminal homology KEYWORDS coiled coil; extracellular matrix; glycoprotein; trimer; !1triple helix FEATURE !$1145-1373 #domain fibrillar collagen carboxyl-terminal homology !8#label FCC SUMMARY #length 1373 #molecular-weight 129602 #checksum 2740 SEQUENCE /// ENTRY CGRT2S #type fragments TITLE collagen alpha 2(I) chain - rat (tentative sequence) (fragments) ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 12-Aug-1981 #sequence_revision 12-Aug-1981 #text_change 31-Mar-2000 ACCESSIONS B90552; A90554; A91386; A90358; A91661; A91398; A02867 REFERENCE A90552 !$#authors Kang, A.H.; Bornstein, P.; Piez, K.A. !$#journal Biochemistry (1967) 6:788-795 !$#title The amino acid sequence of peptides from the cross-linking !1region of rat skin collagen. !$#cross-references MUID:67162268; PMID:5337886 !$#contents CNBr1 !$#accession B90552 !'##molecule_type protein !'##residues 1-14 ##label KAN !'##experimental_source skin REFERENCE A90554 !$#authors Fietzek, P.P.; Piez, K.A. !$#journal Biochemistry (1969) 8:2129-2133 !$#title Isolation and characterization of the cyanogen bromide !1peptides from the alpha2 chain of rat skin collagen. !$#cross-references MUID:69206881; PMID:5785232 !$#contents CNBr0 !$#accession A90554 !'##molecule_type protein !'##residues 15-17 ##label FIE !'##experimental_source skin REFERENCE A91386 !$#authors Fietzek, P.P.; Kell, I.; Kuehn, K. !$#journal FEBS Lett. (1972) 26:66-68 !$#title The covalent structure of collagen. Amino acid sequence of !1the N-terminal region of alpha2-CB4 from calf and rat skin !1collagen. !$#cross-references MUID:73049496; PMID:4636752 !$#contents CNBr4 !$#accession A91386 !'##molecule_type protein !'##residues 18-59;60 ##label FI2 !'##experimental_source skin REFERENCE A90358 !$#authors Highberger, J.H.; Kang, A.H.; Gross, J. !$#journal Biochemistry (1971) 10:610-616 !$#title Comparative studies on the amino acid sequence of the !1alpha2-CB2 peptides from chick and rat skin collagens. !$#cross-references MUID:71115216; PMID:5544653 !$#contents CNBr2 !$#accession A90358 !'##molecule_type protein !'##residues 61-90 ##label HIG !'##experimental_source skin !'##note Met-60 above is the carboxyl-terminal residue of CNBr2 !'##note the sequence of residues 61-90 above appears to correspond to !1positions 339-368 in the alpha 2 chain REFERENCE A91661 !$#authors Fietzek, P.P.; Kuehn, K. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1974) 355:647-650 !$#title The covalent structure of collagen: amino acid sequence of !1the N-terminal region of alpha2-CB3 from rat skin collagen !1and alpha2-CB3.5 from calf skin collagen. !$#cross-references MUID:75059250; PMID:4435743 !$#contents CNBr3 !$#accession A91661 !'##molecule_type protein !'##residues 91-138;139 ##label FI3 !'##experimental_source skin !'##note Met-139 above is the carboxyl-terminal residue of CNBr3 !'##note the sequence of residues 91-138 above appears to correspond to !1positions 369-416 in the alpha 2 chain REFERENCE A91398 !$#authors Fietzek, P.P.; Kuehn, K. !$#journal FEBS Lett. (1973) 36:289-291 !$#title The covalent structure of collagen: amino acid sequence of !1the N-terminal region of alpha2-CB5 from rat skin collagen. !$#cross-references MUID:74055004; PMID:4763308 !$#contents CNBr5 !$#accession A91398 !'##molecule_type protein !'##residues 140-184 ##label FI4 !'##experimental_source skin !'##note the sequence of residues 139-184 above appears to correspond to !1positions 703-749 in the alpha 2 chain REFERENCE A90169 !$#authors Vuust, J.; Lane, J.M.; Fietzek, P.P.; Miller, E.J.; Piez, !1K.A. !$#journal Biochem. Biophys. Res. Commun. (1970) 38:703-708 !$#title The order of the CNBr peptides from the alpha2 chain of !1collagen. !$#cross-references MUID:70181852; PMID:5443712 !$#contents annotation; order of CNBr peptides COMMENT The order of the six CNBr peptides in the alpha 2 chain of !1rat skin collagen was determined as 1,0,4,2,3,5. The !1peptides have the approximate lengths, respectively, of 14, !13, 321, 30, 335, and 320 residues. COMMENT Prolines and lysines at the third position of the tripeptide !1repeating unit (G-X-Y) are hydroxylated to varying extents. !1Prolines are predominately 4-hydroxylated. Lysines are !15-hydroxylated and subsequently O-glycosylated. CLASSIFICATION #superfamily collagen alpha 2(I) chain; fibrillar collagen !1carboxyl-terminal homology KEYWORDS blocked amino end; coiled coil; extracellular matrix; !1glycoprotein; trimer; triple helix FEATURE !$1 #modified_site blocked amino end (Glx) (probably !8pyrrolidone carboxylic acid) #status experimental\ !$5 #modified_site allysine (Lys) #status experimental SUMMARY #length 184 #checksum 7929 SEQUENCE /// ENTRY CGBO2S #type fragment TITLE collagen alpha 2(I) chain - bovine (fragment) ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 12-Aug-1981 #sequence_revision 12-Aug-1981 #text_change 05-Dec-1998 ACCESSIONS A90596; A91233; C91224; B91661; A02866 REFERENCE A90596 !$#authors Fietzek, P.P.; Breitkreutz, D.; Kuehn, K. !$#journal Biochim. Biophys. Acta (1974) 365:305-310 !$#title Amino acid sequence of the amino-terminal region of calf !1skin collagen. !$#cross-references MUID:75036115; PMID:4609475 !$#accession A90596 !'##molecule_type protein !'##residues 1-19 ##label FIE !'##experimental_source skin REFERENCE A91233 !$#authors Fietzek, P.P.; Rexrodt, F.W. !$#journal Eur. J. Biochem. (1975) 59:113-118 !$#title The covalent structure of collagen. The amino-acid sequence !1of alpha2-CB4 from calf-skin collagen. !$#cross-references MUID:76091874; PMID:173531 !$#accession A91233 !'##molecule_type protein !'##residues 16-336 ##label FI2 !'##experimental_source skin REFERENCE A91224 !$#authors Fietzek, P.P.; Furthmayr, H.; Kuehn, K. !$#journal Eur. J. Biochem. (1974) 47:257-261 !$#title Comparative sequence studies on alpha2-CB2 from calf, human, !1rabbit and pig-skin collagen. !$#cross-references MUID:75008198; PMID:4412529 !$#accession C91224 !'##molecule_type protein !'##residues 337-366 ##label FI3 !'##experimental_source skin REFERENCE A91661 !$#authors Fietzek, P.P.; Kuehn, K. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1974) 355:647-650 !$#title The covalent structure of collagen: amino acid sequence of !1the N-terminal region of alpha2-CB3 from rat skin collagen !1and alpha2-CB3.5 from calf skin collagen. !$#cross-references MUID:75059250; PMID:4435743 !$#accession B91661 !'##molecule_type protein !'##residues 367-402 ##label FI4 !'##experimental_source skin COMMENT Prolines at the third position of the tripeptide repeating !1unit (G-X-Y) are hydroxylated in some or all of the chains. COMMENT The order of the five CNBr peptides in the alpha 2 chain of !1bovine skin collagen was determined as 1,0,4,2,3-5. CLASSIFICATION #superfamily collagen alpha 2(I) chain; fibrillar collagen !1carboxyl-terminal homology KEYWORDS coiled coil; extracellular matrix; glycoprotein; !1hydroxylysine; hydroxyproline; pyroglutamic acid; trimer; !1triple helix FEATURE !$1 #modified_site pyrrolidone carboxylic acid (Gln) !8#status experimental\ !$5 #modified_site allysine (Lys) #status predicted\ !$21,27,36,39,42,54, !$57,66,72,87,90,93, !$111,114,120,123, !$129,138,147,174, !$177,180,192,207, !$216,225,234,240, !$243,249,267,282, !$288,291,312,315, !$321,327 #modified_site 4-hydroxyproline (Pro) (partial) !8#status experimental\ !$66,111 #modified_site 4-hydroxyproline (Pro) (partial) !8#status experimental\ !$96,117,132,183 #modified_site 5-hydroxylysine (Lys) #status !8experimental\ !$228,273 #modified_site 5-hydroxylysine (Lys) (partial) !8#status experimental SUMMARY #length 402 #checksum 7137 SEQUENCE /// ENTRY CGCH2S #type fragments TITLE collagen alpha 2(I) chain precursor - chicken (fragments) ORGANISM #formal_name Gallus gallus #common_name chicken DATE 24-Apr-1984 #sequence_revision 15-Aug-1997 #text_change 21-Jul-2000 ACCESSIONS I50206; I50207; S07354; S10848; S10480; S11146; I50628; !1I50170; I50625; I50626; I50624; A90568; A90557; B90358; !1A90555; S07327; I50623; I50172; I50171; A02868 REFERENCE I50206 !$#authors Boedtker, H.; Finer, M.; Aho, S. !$#journal Ann. N. Y. Acad. Sci. (1985) 460:85-116 !$#title The structure of the chicken alpha 2 collagen gene. !$#cross-references MUID:86185168; PMID:3868961 !$#accession I50206 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-245 ##label BOE !'##cross-references GB:M25963; NID:g211581; PIDN:AAA69960.1; !1PID:g211605 !$#accession I50207 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 246-431 ##label BO2 !'##cross-references GB:M25965; NID:g211583; PIDN:AAA69961.1; !1PID:g211606 REFERENCE S07354 !$#authors Aho, S.; Tate, V.; Boedtker, H. !$#journal Nucleic Acids Res. (1984) 12:6117-6125 !$#title Location of the 11 bp exon in the chicken pro alpha-2(I) !1collagen gene. !$#cross-references MUID:84297217; PMID:6473103 !$#accession S07354 !'##molecule_type DNA !'##residues 1-33 ##label AHO !'##cross-references EMBL:X00760; NID:g63266; PIDN:CAA25330.1; !1PID:g63267 REFERENCE S10480 !$#authors Tate, V.E.; Finer, M.H.; Boedtker, H.; Doty, P. !$#journal Nucleic Acids Res. (1983) 11:91-104 !$#title Chick pro-alpha-2 (I) collagen gene: exon location and !1coding potential for the prepropeptide. !$#cross-references MUID:83246518; PMID:6135195 !$#accession S10848 !'##molecule_type mRNA !'##residues 1-89 ##label TAT !'##cross-references EMBL:X02657; NID:g63314; PIDN:CAA26493.1; !1PID:g63315 !$#accession S10480 !'##molecule_type DNA !'##residues 17-73 ##label TAW !'##note the authors translated the codon CAG for residue 42 as Glu REFERENCE S11146 !$#authors Vogeli, G.; Ohkubo, H.; Sobel, M.E.; Yamada, Y.; Pastan, I.; !1de Crombrugghe, B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:5334-5338 !$#title Structure of the promoter for chicken alpha-2 type I !1collagen gene. !$#cross-references MUID:82060240; PMID:6946474 !$#accession S11146 !'##status preliminary !'##molecule_type DNA !'##residues 1-15 ##label VOG !'##cross-references EMBL:J00821 REFERENCE I50170 !$#authors Yamada, Y.; Avvedimento, V.E.; Mudryj, M.; Ohkubo, H.; !1Vogeli, G.; Irani, M.; Pastan, I.; de Crombrugghe, B. !$#journal Cell (1980) 22:887-892 !$#title The collagen gene: evidence for its evolutinary assembly by !1amplification of a DNA segment containing an exon of 54 bp. !$#cross-references MUID:81112157; PMID:7460017 !$#accession I50628 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 126-161 ##label YAM !'##cross-references EMBL:V00400; NID:g63305; PID:g833611 !$#accession I50170 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 126-161 ##label YA2 !'##cross-references GB:J00828; NID:g211295; PIDN:AAA51612.1; !1PID:g211317 !$#accession I50625 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 530-558 ##label YA3 !'##cross-references EMBL:V00396; NID:g63295; PID:g833609 !$#accession I50626 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 572-601 ##label YA4 !'##cross-references EMBL:V00398; NID:g63299; PID:g833610 !$#accession I50624 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 433-483 ##label YA5 !'##cross-references EMBL:V00394; NID:g63287; PID:g833608 REFERENCE A90568 !$#authors Kang, A.H.; Gross, J. !$#journal Biochemistry (1970) 9:796-804 !$#title Amino acid sequence of cyanogen bromide peptides from the !1amino-terminal region of chick skin collagen. !$#cross-references MUID:70131186; PMID:4313735 !$#accession A90568 !'##molecule_type protein !'##residues 'Z',79-92 ##label KAN !'##experimental_source skin REFERENCE A90557 !$#authors Kang, A.H.; Igarashi, S.; Gross, J. !$#journal Biochemistry (1969) 8:3200-3204 !$#title Characterization of the cyanogen bromide peptides from the !1alpha2 chain of chick skin collagen. !$#cross-references MUID:69285369; PMID:5809220 !$#accession A90557 !'##molecule_type protein !'##residues 'Z',79-95;398-409,'A',411,'V',413-428 ##label KA2 !'##experimental_source skin !'##note the compositions of the six CNBr peptides were determined. !1CNBr0 is residues 93-18. CNBr1 corresponds to residues 78-92 !1and CNBr2 corresponds to residues 399-428 REFERENCE A90358 !$#authors Highberger, J.H.; Kang, A.H.; Gross, J. !$#journal Biochemistry (1971) 10:610-616 !$#title Comparative studies on the amino acid sequence of the !1alpha2-CB2 peptides from chick and rat skin collagens. !$#cross-references MUID:71115216; PMID:5544653 !$#accession B90358 !'##molecule_type protein !'##residues 399-409,'A',411,'V',413-428 ##label HIG !'##experimental_source skin REFERENCE A90555 !$#authors Lane, J.M.; Miller, E.J. !$#journal Biochemistry (1969) 8:2134-2139 !$#title Isolation and characterization of the peptides derived from !1the alpha2 chain of chick bone collagen after cyanogen !1bromide cleavage. !$#cross-references MUID:69206882; PMID:5785233 !$#accession A90555 !'##molecule_type protein !'##residues 'Z',79-95;398-409,'A',411,'V',413-428 ##label LAN !'##experimental_source bone !'##note the compositions of the six CNBr peptides were determined !'##note the compositions of CNBr1, CNBr0, and CNBr2 are identical with !1those from skin alpha 2 chain REFERENCE A90168 !$#authors Igarashi, S.; Kang, A.H.; Gross, J. !$#journal Biochem. Biophys. Res. Commun. (1970) 38:697-702 !$#title Renaturation and ordering by electron microscopy of the !1cyanogen bromide peptides from the alpha2 chain of chick !1skin collagen. !$#cross-references MUID:70181851; PMID:5443711 !$#contents annotation; skin, order of CNBr peptides REFERENCE A90169 !$#authors Vuust, J.; Lane, J.M.; Fietzek, P.P.; Miller, E.J.; Piez, !1K.A. !$#journal Biochem. Biophys. Res. Commun. (1970) 38:703-708 !$#title The order of the CNBr peptides from the alpha2 chain of !1collagen. !$#cross-references MUID:70181852; PMID:5443712 !$#contents annotation; bone, order of CNBr peptides REFERENCE S07327 !$#authors Wozney, J.; Hanahan, D.; Tate, V.; Boedtker, H.; Doty, P. !$#journal Nature (1981) 294:129-135 !$#title Structure of the pro alpha-2(I) collagen gene. !$#cross-references MUID:82058081; PMID:6272119 !$#accession S07327 !'##molecule_type DNA !'##residues 74-92;93,247-431;432,693-774 ##label WOZ !'##cross-references EMBL:J00826 REFERENCE I50623 !$#authors Fuller, F.; Boedtker, H. !$#journal Biochemistry (1981) 20:996-1006 !$#title Sequence determination and analysis of the 3' region of !1chicken pro-alpha 1(I) and pro-alpha 2(I) collagen messenger !1ribonucleic acids including the carboxy-terminal propeptide !1sequences. !$#cross-references MUID:81160715; PMID:6927845 !$#accession I50623 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 506-830,'T',831-903,'N',904-964 ##label FUL !'##cross-references EMBL:V00390; NID:g63248; PIDN:CAA23688.1; !1PID:g63249 REFERENCE I50172 !$#authors Avvedimento, E.V.; Vogeli, G.; Yamada, Y.; Maizel, J.V. !$#journal Cell (1980) 21:689-696 !$#title Correlation between splicing sites within an intron and !1their sequence complementarity with U1 RNA. !$#cross-references MUID:81064671; PMID:6159982 !$#accession I50172 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 536-558 ##label AVV !'##cross-references GB:M10581; NID:g211323; PIDN:AAA48637.1; !1PID:g211326 REFERENCE I50171 !$#authors Lehrach, H.; Frischauf, A.M.; Hanahan, D.; Wozney, J.; !1Fuller, F.; Crkvenjakov, R.; Boedtker, H.; Doty, P. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1978) 75:5417-5421 !$#title Construction and characterization of a 2.5-kilobase !1procollagen clone. !$#cross-references MUID:79074829; PMID:364479 !$#accession I50171 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 484-505 ##label LEH !'##cross-references GB:J00837; NID:g4530617; PIDN:AAA51614.1; !1PID:g211320 GENETICS !$#gene COL1A2 !$#introns 24/1; 27/3; 33/3; 45/3; 73/3; 92/3; 107/3; 125/3; 143/3; !1161/3; 179/3; 197/3; 212/3; 230/3; 278/3; 293/3; 326/3; 344/ !13; 380/3; 398/3; 431/3; 465/3; 547/3; 583/3 !$#note the list of introns is incomplete CLASSIFICATION #superfamily collagen alpha 2(I) chain; fibrillar collagen !1carboxyl-terminal homology KEYWORDS blocked amino end; coiled coil; extracellular matrix; !1glycoprotein; hydroxyproline; trimer; triple helix FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-77 #domain amino-terminal propeptide #status predicted !8#label PRO\ !$78-964 #product collagen alpha 2(I) chain (fragments) !8#status predicted #label MATN\ !$78-89 #region amino-terminal nonhelical telopeptide\ !$737-964 #domain fibrillar collagen carboxyl-terminal homology !8#label FCC\ !$78 #modified_site blocked amino end (Gln) (in mature !8form) (probably pyrrolidone carboxylic acid) #status !8experimental\ !$83 #modified_site allysine (Lys) #status experimental\ !$422,425 #modified_site 4-hydroxyproline (Pro) #status !8experimental\ !$866 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 964 #checksum 6018 SEQUENCE /// ENTRY S23809 #type complete TITLE collagen alpha 2(I) chain homolog - sea urchin (Strongylocentrotus purpuratus) ORGANISM #formal_name Strongylocentrotus purpuratus #common_name purple urchin DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S23809 REFERENCE S23809 !$#authors Exposito, J.Y.; d'Alessio, M.; Solursh, M.; Ramirez, F. !$#journal J. Biol. Chem. (1992) 267:15559-15562 !$#title Sea urchin collagen evolutionarily homologous to vertebrate !1pro-alpha-2(I) collagen. !$#cross-references MUID:92348411; PMID:1639795 !$#accession S23809 !'##status preliminary !'##molecule_type mRNA !'##residues 1-1414 ##label EXP !'##cross-references EMBL:M92040; NID:g161435; PIDN:AAA30035.1; !1PID:g161436 CLASSIFICATION #superfamily collagen alpha 2(I) chain; fibrillar collagen !1carboxyl-terminal homology KEYWORDS coiled coil; extracellular matrix; glycoprotein; trimer; !1triple helix FEATURE !$1207-1414 #domain fibrillar collagen carboxyl-terminal homology !8#label FCC SUMMARY #length 1414 #molecular-weight 133024 #checksum 1606 SEQUENCE /// ENTRY CGHU1V #type complete TITLE collagen alpha 1(V) chain precursor - human ALTERNATE_NAMES procollagen alpha 1(V) chain ORGANISM #formal_name Homo sapiens #common_name man DATE 22-Nov-1993 #sequence_revision 03-Oct-1995 #text_change 16-Jun-2000 ACCESSIONS S18802; S16024; A61142; S11303; S03978; S43642; S58665 REFERENCE S18802 !$#authors Greenspan, D.S.; Cheng, W.; Hoffman, G.G. !$#journal J. Biol. Chem. (1991) 266:24727-24733 !$#title The pro-alpha1(V) collagen chain. Complete primary !1structure, distribution of expression, and comparison with !1the pro-alpha1(XI) collagen chain. !$#cross-references MUID:92105142; PMID:1722213 !$#accession S18802 !'##molecule_type mRNA !'##residues 1-1838 ##label GRE !'##cross-references GB:M76729; NID:g189519; PIDN:AAA59993.1; !1PID:g189520 REFERENCE S16024 !$#authors Takahara, K.; Sato, Y.; Okazawa, K.; Okamoto, N.; Noda, A.; !1Yaoi, Y.; Kato, I. !$#journal J. Biol. Chem. (1991) 266:13124-13129 !$#title Complete primary structure of human collagen alpha-1(V) !1chain. !$#cross-references MUID:91302336; PMID:2071595 !$#accession S16024 !'##molecule_type mRNA !'##residues 1-81,'QL',84-389,'A',391-676,'K',678-1294,'PS',1297,'RS', !11300-1553,'R',1555-1812,'V',1814-1838 ##label TAK !'##cross-references GB:D90279; NID:g219509; PIDN:BAA14323.1; !1PID:g219510 !'##note parts of this sequence were determined by protein sequencing REFERENCE A61142 !$#authors Yaoi, Y.; Hashimoto, K.; Takahara, K.; Kato, I. !$#journal Exp. Cell Res. (1991) 194:180-185 !$#title Insulin binds to type V collagen with retention of mitogenic !1activity. !$#cross-references MUID:91224163; PMID:1709100 !$#accession A61142 !'##molecule_type protein !'##residues 823-824,'X',826-842 ##label YAO !'##note the residue designated 'X' is probably glycosylated !1hydroxylysine; this cyanogen bromide fragment contains an !1uncharacterized growth hormone-binding region REFERENCE S11303 !$#authors Yaoi, Y.; Hashimoto, K.; Koitabashi, H.; Takahara, K.; Ito, !1M.; Kato, I. !$#journal Biochim. Biophys. Acta (1990) 1035:139-145 !$#title Primary structure of the heparin-binding site of type V !1collagen. !$#cross-references MUID:90366601; PMID:2203476 !$#accession S11303 !'##molecule_type protein !'##residues 823-824,'X',826-848,'I',850-851,'P',853,'PR',856-893,'D', !1895-932,'X',934-950 ##label YA2 !'##note the residues designated 'X' are probably glycosylated !1hydroxylysine; this sequence revised by S16024 REFERENCE S03978 !$#authors Seyer, J.M.; Kang, A.H. !$#journal Arch. Biochem. Biophys. (1989) 271:120-129 !$#title Covalent structure of collagen: amino acid sequence of three !1cyanogen bromide-derived peptides from human alpha-1(V) !1collagen chain. !$#cross-references MUID:89227189; PMID:2496661 !$#accession S03978 !'##molecule_type protein !'##residues 621-640,'G',642-649,'L',651-662,'E',664-667,'Q',669-676, !1'Q',678-683,'P',685-691,'VT',694,'E',696-697,'AP',700-726, !1'Q',728-740,'L',742-746,'Q',748-752,'A',754-758,'N',760-775, !1'QK',778-822 ##label SEY !'##note there are a number of inconsistencies between the sequences in !1figures 6 and 7; the sequence in figure 7 is given REFERENCE S43642 !$#authors Moradi-Ameli, M.; Rousseau, J.C.; Kleman, J.P.; Champliaud, !1M.F.; Boutillon, M.M.; Bernillon, J.; Wallach, J.; van der !1Rest, M. !$#journal Eur. J. Biochem. (1994) 221:987-995 !$#title Diversity in the processing events at the N-terminus of !1type-V collagen. !$#cross-references MUID:94237164; PMID:8181482 !$#accession S43642 !'##molecule_type protein !'##residues 565-576;756-758,'X',760-763,'X', !1765-772;1012-1029;1219-1232;1465-1474,'X',1476-1477 ##label !1MOR REFERENCE A56977 !$#authors Fessler, L.I.; Brosh, S.; Chapin, S.; Fessler, J.H. !$#journal J. Biol. Chem. (1986) 261:5034-5040 !$#title Tyrosine sulfation in precursors of collagen V. !$#cross-references MUID:86168226; PMID:3082875 !$#contents annotation; identification of tyrosine sulfate in the !1amino-terminal propeptide REFERENCE S58665 !$#authors Lee, S.; Greenspan, D.S. !$#journal Biochem. J. (1995) 310:15-22 !$#title Transcriptional promoter of the human alpha-1(V) collagen !1gene (COL5A1). !$#cross-references MUID:95374437; PMID:7646438 !$#accession S58665 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-36 ##label LEE !'##cross-references GB:L38808; NID:g1020325; PIDN:AAA79853.1; !1PID:g1020326 COMMENT Prolines and lysines at the third position of the tripeptide !1repeating unit (G-X-Y) are hydroxylated to varying extents. !1Prolines are predominately 4-hydroxylated. About 50% of the !1lysines are 5-hydroxylated and subsequently O-glycosylated. COMMENT A long form of the mature protein containing part of the !1amino-terminal propeptide has been detected but not !1characterized. The homotrimer is probably fully processed to !1the short form, while the heterotrimers are probably !1processed to the long form. GENETICS !$#gene GDB:COL5A1 !'##cross-references GDB:131457; OMIM:120215 !$#map_position 9q34.2-9q34.3 COMPLEX type V collagen may be a homotrimer of alpha 1(V) chains, a !1heterotrimer of two alpha 1(V) chains and one alpha 2(V) !1chain (see PIR:CGHU2V), or a heterotrimer of one alpha 1(V) !1chain, one alpha 2(V) chain and one alpha 3(V) chain, !1initially linked by disulfide bonds among their !1carboxyl-terminal propeptides; a polymer of collagen !1trimers, offset by approximately one-quarter of their !1length, is formed with desmosine cross-links made from !1lysine and allysine residues FUNCTION !$#description structural component of extracellular fibrous polymer !1associated with cell surfaces and interstitial fibrils; !1widely distributed but least abundant of the fibrillar !1collagens !$#note may play a role in controlling the lateral growth of !1collagen I fibrils CLASSIFICATION #superfamily collagen alpha 1(V) chain; fibrillar collagen !1carboxyl-terminal homology KEYWORDS coiled coil; extracellular matrix; glycoprotein; !1hydroxylysine; hydroxyproline; pyroglutamic acid; !1sulfoprotein; trimer; triple helix FEATURE !$1-37 #domain signal sequence #status predicted #label SIG\ !$36-261 #domain PARP-like #status predicted #label PARP\ !$38-541 #domain amino-terminal propeptide #status predicted !8#label PRO\ !$542-1605 #product collagen alpha 1(V) chain, short form !8#status predicted #label MAT\ !$542-558 #region amino-terminal nonhelical telopeptide\ !$559-1572 #region helical\ !$645-647 #region cell attachment (R-G-D) motif\ !$663-665 #region cell attachment (R-G-D) motif\ !$897-929 #region heparin binding\ !$1573-1605 #region carboxyl-terminal nonhelical telopeptide\ !$1606-1838 #domain carboxyl-terminal propeptide #status !8predicted #label CPR\ !$1615-1837 #domain fibrillar collagen carboxyl-terminal homology !8#label FCC\ !$38 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status predicted\ !$62-244,183-237 #disulfide_bonds #status predicted\ !$159,176,385,1672, !$1741 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$234,236,240,262, !$263,273,274,275, !$277,279,280,338, !$340,346,347,352, !$357,416,417,420,421 #binding_site sulfate (Tyr) (covalent) #status !8predicted\ !$535 #modified_site allysine (Lys) #status predicted\ !$541-542 #cleavage_site Ala-Gln (procollagen N-endopeptidase) !8#status predicted\ !$542 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status predicted\ !$570,576,621,639, !$648,654,657,675, !$678,690,693,696, !$705,717,720,726, !$732,741,750,753, !$756,762,765,771, !$780,789,816,834, !$870,873,876,888, !$891,903,906,930, !$945,1017,1020,1023, !$1029,1221,1224, !$1467,1470 #modified_site 4-hydroxyproline (Pro) #status !8experimental\ !$627,642,687,708, !$744,774,795,804, !$807,810,819,825, !$846,864,882,897 #modified_site 5-hydroxylysine (Lys) #status !8experimental\ !$627,642,687,774, !$795,804,807,810, !$819,825,846,864, !$882,897,1482 #binding_site carbohydrate (Lys) (covalent) #status !8predicted\ !$708,744 #binding_site carbohydrate (Lys) (covalent) #status !8experimental\ !$1482 #modified_site 5-hydroxylysine (Lys) #status !8predicted\ !$1605-1606 #cleavage_site Ala-Asp (procollagen C-endopeptidase) !8#status predicted\ !$1639,1645,1662,1671 #disulfide_bonds interchain #status predicted\ !$1680-1835,1746-1789 #disulfide_bonds #status predicted SUMMARY #length 1838 #molecular-weight 183611 #checksum 5425 SEQUENCE /// ENTRY CGHU1E #type complete TITLE collagen alpha 1(XI) chain precursor - human ALTERNATE_NAMES procollagen alpha 1(XI) chain ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1990 #sequence_revision 03-Oct-1995 #text_change 08-May-1998 ACCESSIONS A35239; A31795 REFERENCE A35239 !$#authors Yoshioka, H.; Ramirez, F. !$#journal J. Biol. Chem. (1990) 265:6423-6426 !$#title Pro-alpha1(XI) collagen. Structure of the amino-terminal !1propeptide and expression of the gene in tumor cell lines. !$#cross-references MUID:90202924; PMID:1690726 !$#accession A35239 !'##molecule_type mRNA !'##residues 1-558 ##label YOS !'##cross-references GB:J05407 REFERENCE A92689 !$#authors Bernard, M.; Yoshioka, H.; Rodriguez, E.; van der Rest, M.; !1Kimura, T.; Ninomiya, Y.; Olsen, B.R.; Ramirez, F. !$#journal J. Biol. Chem. (1988) 263:17159-17166 !$#title Cloning and sequencing of pro-alpha1(XI) collagen cDNA !1demonstrates that type XI belongs to the fibrillar class of !1collagens and reveals that the expression of the gene is not !1restricted to cartilagenous tissue. !$#cross-references MUID:89034222; PMID:3182841 !$#accession A31795 !'##molecule_type DNA; mRNA !'##residues 538-1806 ##label BER !'##cross-references GB:J04177 !'##note parts of this sequence were determined by protein sequencing COMMENT Prolines and lysines at the third position of the tripeptide !1repeating unit (G-X-Y) are hydroxylated to varying extents. !1Prolines are predominately 4-hydroxylated. Lysines are !15-hydroxylated and subsequently O-glycosylated. GENETICS !$#gene GDB:COL11A1; COLL6 !'##cross-references GDB:120595; OMIM:120280 !$#map_position 1p21-1p21 !$#introns 561/3; 579/3; 597/3; 615/3; 633/3; 648/3; 666/3; 681/3 !$#note the list of introns is incomplete COMPLEX type XI collagen may be a heterotrimer of two alpha 1(XI) !1chains and one alpha 2(XI) chain (see PIR:CGHU2E), or a !1heterotrimer of one alpha 1(XI) chain, one alpha 2(XI) chain !1and one alpha 3(XI) chain (see PIR:CGHU6C), initially linked !1by disulfide bonds among their carboxyl-terminal !1propeptides; a polymer of collagen trimers, offset by !1approximately one-quarter of their length, is formed with !1desmosine cross-links made from lysine and allysine residues FUNCTION !$#description structural component of extracellular fibrous polymer !1associated with cell surfaces and interstitial fibrils of !1cartilage !$#note may play a role in controlling the lateral growth of !1collagen II fibrils CLASSIFICATION #superfamily collagen alpha 1(V) chain; fibrillar collagen !1carboxyl-terminal homology KEYWORDS coiled coil; extracellular matrix; glycoprotein; !1hydroxylysine; hydroxyproline; trimer; triple helix FEATURE !$1-36 #domain signal sequence #status predicted #label SIG\ !$35-260 #domain PARP-like #status predicted #label PARP\ !$37-511 #domain amino-terminal propeptide #status predicted !8#label PRO\ !$512-1565 #product collagen alpha 1(XI) chain #status predicted !8#label MAT\ !$512-527 #region amino-terminal nonhelical telopeptide\ !$528-1542 #region helical\ !$1543-1565 #region carboxyl-terminal nonhelical telopeptide\ !$1566-1806 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$1583-1805 #domain fibrillar collagen carboxyl-terminal homology !8#label FCC\ !$61-243,182-236 #disulfide_bonds #status predicted\ !$505 #modified_site allysine (Lys) #status predicted\ !$612,1452 #modified_site 5-hydroxylysine (Lys) #status !8predicted\ !$612,1452 #binding_site carbohydrate (Lys) (covalent) #status !8predicted SUMMARY #length 1806 #molecular-weight 181138 #checksum 3590 SEQUENCE /// ENTRY CGHU2E #type fragment TITLE collagen alpha 2(XI) chain precursor - human (fragment) ALTERNATE_NAMES procollagen alpha 2(XI) chain CONTAINS proline/arginine-rich protein (PARP) ORGANISM #formal_name Homo sapiens #common_name man DATE 07-Jun-1990 #sequence_revision 03-Oct-1995 #text_change 22-Jun-1999 ACCESSIONS S34790; A32645 REFERENCE S34790 !$#authors Zhidkova, N.I.; Brewton, R.G.; Mayne, R. !$#journal FEBS Lett. (1993) 326:25-28 !$#title Molecular cloning of PARP (proline/arginine-rich protein) !1from human cartilage and subsequent demonstration that PARP !1is a fragment of the NH(2)-terminal domain of the collagen !1alpha-2(XI) chain. !$#cross-references MUID:93314796; PMID:8325374 !$#accession S34790 !'##molecule_type mRNA !'##residues 1-663 ##label ZHI !'##cross-references EMBL:L18987; NID:g306439; PIDN:AAA35498.1; !1PID:g306440 REFERENCE A32645 !$#authors Kimura, T.; Cheah, K.S.E.; Chan, S.D.H.; Lui, V.C.H.; !1Mattei, M.G.; van der Rest, M.; Ono, K.; Solomon, E.; !1Ninomiya, Y.; Olsen, B.R. !$#journal J. Biol. Chem. (1989) 264:13910-13916 !$#title The human alpha2(XI) collagen (COL11A2) chain. Molecular !1cloning of cDNA and genomic DNA reveals characteristics of a !1fibrillar collagen with differences in genomic organization. !$#cross-references MUID:89340485; PMID:2760050 !$#accession A32645 !'##molecule_type DNA; mRNA !'##residues 586-1546 ##label KIM !'##cross-references GB:J04974; NID:g180714; PIDN:AAA52034.1; !1PID:g180715 !'##note parts of this sequence were determined by protein sequencing COMMENT Prolines and lysines at the third position of the tripeptide !1repeating unit (G-X-Y) are hydroxylated to varying extents. !1Prolines are predominately 4-hydroxylated. Lysines are !15-hydroxylated and subsequently O-glycosylated. GENETICS !$#gene GDB:COL11A2 !'##cross-references GDB:119788; OMIM:120290 !$#map_position 6p21.3-6p21.3 !$#introns 1302/3; 1320/3; 1332/3; 1350/3; 1440/1; 1477/3 !$#note the list of introns is incomplete COMPLEX type XI collagen may be a heterotrimer of two alpha 1(XI) !1chains (see PIR:CGHU1E) and one alpha 2(XI) chain, or a !1heterotrimer of one alpha 1(XI) chain, one alpha 2(XI) chain !1and one alpha 3(XI) chain (see PIR:CGHU6C), initially linked !1by disulfide bonds among their carboxyl-terminal !1propeptides; a polymer of collagen trimers, offset by !1approximately one-quarter of their length, is formed with !1desmosine cross-links made from lysine and allysine residues FUNCTION !$#description structural component of extracellular fibrous polymer !1associated with cell surfaces and interstitial fibrils of !1cartilage !$#note may play a role in controlling the lateral growth of !1collagen II fibrils CLASSIFICATION #superfamily collagen alpha 1(V) chain; fibrillar collagen !1carboxyl-terminal homology KEYWORDS coiled coil; extracellular matrix; glycoprotein; !1hydroxylysine; hydroxyproline; trimer; triple helix FEATURE !$1-254 #domain non-collagenous (fragment) #status predicted !8#label NC3\ !$1-187 #product proline/arginine-rich PARP protein !8(fragment) #status predicted #label PARP\ !$255-305 #domain collagenous, triple helix #status predicted !8#label COL2\ !$306-342 #domain non-collagenous #status predicted #label NC2\ !$343-1356 #region helical\ !$429-431 #region cell attachment (R-G-D) motif\ !$447-449 #region cell attachment (R-G-D) motif\ !$1257-1259 #region cell attachment (R-G-D) motif\ !$1357-1380 #region carboxyl-terminal nonhelical telopeptide\ !$1381-1546 #domain carboxyl-terminal propeptide (fragment) !8#status predicted #label CTP\ !$1403-1546 #domain fibrillar collagen carboxyl-terminal homology !8(fragment) #status atypical #label FCC\ !$109-163,1511-1545 #disulfide_bonds #status predicted\ !$319 #modified_site allysine (Lys) #status predicted\ !$426,1266 #modified_site 5-hydroxylysine (Lys) #status !8predicted\ !$426,1266 #binding_site carbohydrate (Lys) (covalent) #status !8predicted\ !$927,933,1008,1017, !$1035,1038,1290, !$1296,1305,1317,1320 #modified_site 4-hydroxyproline (Pro) #status !8experimental\ !$929 #modified_site 4-hydroxyproline (Pro) #status !8atypical\ !$942,1023,1299 #modified_site 5-hydroxylysine (Lys) #status !8experimental\ !$942,1023,1299 #binding_site carbohydrate (Lys) (covalent) #status !8experimental\ !$1427,1433,1450,1459 #disulfide_bonds interchain #status predicted\ !$1460 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1546 #checksum 8839 SEQUENCE /// ENTRY CGHU4B #type complete TITLE collagen alpha 1(IV) chain precursor - human ALTERNATE_NAMES procollagen alpha 1(IV) chain ORGANISM #formal_name Homo sapiens #common_name man DATE 28-May-1986 #sequence_revision 31-Dec-1992 #text_change 07-Dec-1999 ACCESSIONS S16876; A32117; S02738; S00048; S25826; A23115; S00207; !1S39614; A02863; A58517; S16910; S01466; S16879; S19091; !1S03083; S16908 REFERENCE S16876 !$#authors Soininen, R.; Huotari, M.; Ganguly, A.; Prockop, D.J.; !1Tryggvason, K. !$#journal J. Biol. Chem. (1989) 264:13565-13571 !$#title Structural organization of the gene for the alpha-1 chain of !1human type IV collagen. !$#cross-references MUID:89340433; PMID:2701944 !$#accession S16876 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1669 ##label SOI1 !'##cross-references EMBL:J04217; GB:J05039; NID:g180800; !1PIDN:AAA53098.1; PID:g180803 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1988 REFERENCE A92690 !$#authors Soininen, R.; Huotari, M.; Hostikka, S.L.; Prockop, D.J.; !1Tryggvason, K. !$#journal J. Biol. Chem. (1988) 263:17217-17220 !$#title The structural genes for alpha1 and alpha2 chains of human !1type IV collagen are divergently encoded on opposite DNA !1strands and have an overlapping promoter region. !$#cross-references MUID:89034231; PMID:3182844 !$#accession A32117 !'##molecule_type DNA !'##residues 1-28 ##label SOI2 !'##cross-references EMBL:J04217; NID:g180759; PIDN:AAA53097.1; !1PID:g553233 REFERENCE S02738 !$#authors Poeschl, E.; Pollner, R.; Kuehn, K. !$#journal EMBO J. (1988) 7:2687-2695 !$#title The genes for the alpha1(IV) and alpha2(IV) chains of human !1basement membrane collagen type IV are arranged head-to-head !1and separated by a bidirectional promoter of unique !1structure. !$#cross-references MUID:89030632; PMID:2846280 !$#accession S02738 !'##status translation not shown !'##molecule_type DNA !'##residues 1-6,'L',8-28 ##label POE !'##cross-references EMBL:X12784; NID:g30072 REFERENCE S00048 !$#authors Brazel, D.; Oberbaeumer, I.; Dieringer, H.; Babel, W.; !1Glanville, R.W.; Deutzmann, R.; Kuehn, K. !$#journal Eur. J. Biochem. (1987) 168:529-536 !$#title Completion of the amino acid sequence of the alpha1 chain of !1human basement membrane collagen (type IV) reveals 21 !1non-triplet interruptions located within the collagenous !1domain. !$#cross-references MUID:88029471; PMID:3311751 !$#accession S00048 !'##molecule_type mRNA !'##residues 1-318,'A',320-944 ##label BRA1 !'##cross-references EMBL:X05561; NID:g30066; PIDN:CAA29075.1; !1PID:g30067 !$#accession S25826 !'##molecule_type protein !'##residues 271-318,'A',320-554 ##label BRA2 REFERENCE A23115 !$#authors Glanville, R.W.; Qian, R.Q.; Siebold, B.; Risteli, J.; !1Kuehn, K. !$#journal Eur. J. Biochem. (1985) 152:213-219 !$#title Amino acid sequence of the N-terminal aggregation and !1cross-linking region (7S domain) of the alpha-1(IV) chain of !1human basement membrane collagen. !$#cross-references MUID:86004708; PMID:4043082 !$#accession A23115 !'##molecule_type protein !'##residues 28-236,'KE',239-240,'K',242-243 ##label GLA !'##experimental_source placenta !'##note the amino end of the mature form is blocked REFERENCE S00207 !$#authors Soininen, R.; Haka-Risku, T.; Prockop, D.J.; Tryggvason, K. !$#journal FEBS Lett. (1987) 225:188-194 !$#title Complete primary structure of the alpha(1)-chain of human !1basement membrane (type IV) collagen. !$#cross-references MUID:88083584; PMID:3691802 !$#accession S00207 !'##molecule_type mRNA !'##residues 244-530 ##label SOI3 !'##cross-references EMBL:Y00706; NID:g29548; PIDN:CAA68698.1; !1PID:g29549 REFERENCE S39614 !$#authors Eble, J.A.; Golbik, R.; Mann, K.; Kuehn, K. !$#journal EMBO J. (1993) 12:4795-4802 !$#title The alpha-1-beta-1 integrin recognition site of the basement !1membrane collagen molecule [alpha-1(IV)](2)-alpha-2(IV). !$#cross-references MUID:94038963; PMID:8223488 !$#accession S39614 !'##molecule_type protein !'##residues 371-554 ##label EBL REFERENCE A02863 !$#authors Babel, W.; Glanville, R.W. !$#journal Eur. J. Biochem. (1984) 143:545-556 !$#title Structure of human-basement-membrane (type IV) collagen. !1Complete amino-acid sequence of a 914-residue-long pepsin !1fragment from the alpha1(IV) chain. !$#cross-references MUID:85003629; PMID:6434307 !$#accession A02863 !'##molecule_type protein !'##residues 534-718,'D',720-836,'Y',838-841,'P',843-903,'Q',905-913, !1'K',915-997,'K',999-1009,'P',1011,'K',1013-1357,'Q', !11359-1447 ##label BAB !'##experimental_source placenta REFERENCE S16908 !$#authors Glanville, R.W.; Rauter, A. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1981) 362:943-951 !$#title Pepsin fragments of human placental basement-membrane !1collagens showing interrupted triple-helical amino acid !1sequences. !$#cross-references MUID:82005835; PMID:6792033 !$#accession A58517 !'##molecule_type protein !'##residues 534-537,'G',539,'G',541-542,'X',544-553;1389-1405,'XX', !11408-1409,'X',1411-1413 ##label GLA2 REFERENCE S16910 !$#authors MacWright, R.S.; Benson, V.A.; Lovello, K.T.; van der Rest, !1M.; Fietzek, P.P. !$#journal Biochemistry (1983) 22:4940-4948 !$#title Isolation and characterization of pepsin-solubilized human !1basement membrane (type IV) collagen peptides. !$#cross-references MUID:84053346; PMID:6416291 !$#accession S16910 !'##molecule_type protein !'##residues 534-537,'G',539,'G',541-542,'G',544-549;939-940,'M', !1942-944,'V',946,'X',948-949,'E',951-954 ##label MAC !'##experimental_source placenta REFERENCE S01466 !$#authors Pihlajaniemi, T.; Tryggvason, K.; Myers, J.C.; Kurkinen, M.; !1Lebo, R.; Cheung, M.C.; Prockop, D.J.; Boyd, C.D. !$#journal J. Biol. Chem. (1985) 260:7681-7687 !$#title cDNA clones coding for the Pro-alpha-1(IV) chain of human !1type IV procollagen reveal an unusual homology of amino acid !1sequences in two halves of the carboxyl-terminal domain. !$#cross-references MUID:85207819; PMID:2581969 !$#accession S01466 !'##molecule_type mRNA !'##residues 1256-1669 ##label PIH !'##cross-references EMBL:M10940; NID:g180421; PIDN:AAA52006.1; !1PID:g180424 REFERENCE S16879 !$#authors Brinker, J.M.; Gudas, L.J.; Loidl, H.R.; Wang, S.Y.; !1Rosenbloom, J.; Kefalides, N.A.; Myers, J.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:3649-3653 !$#title Restricted homology between human alpha-1 type IV and other !1procollagen chains. !$#cross-references MUID:85216555; PMID:2582422 !$#accession S16879 !'##molecule_type mRNA !'##residues 1259-1669 ##label BRI !'##cross-references EMBL:M11315; NID:g180817; PIDN:AAA52042.1; !1PID:g180818 REFERENCE A02864 !$#authors Oberbaeumer, I.; Laurent, M.; Schwarz, U.; Sakurai, Y.; !1Yamada, Y.; Vogeli, G.; Voss, T.; Siebold, B.; Glanville, !1R.W.; Kuehn, K. !$#journal Eur. J. Biochem. (1985) 147:217-224 !$#title Amino acid sequence of the non-collagenous globular domain !1(NC1) of the alpha-1(IV) chain of basement membrane collagen !1as derived from complementary DNA. !$#cross-references MUID:85127033; PMID:2578961 !$#accession S19091 !'##molecule_type protein !'##residues 1435-1461,'H',1463-1482,'X',1484-1491;1501-1514,'X', !11516-1519;1534-1553,'X',1555;1559-1560,'X',1562,'X',1564, !1'X',1566-1568;1586-1598 ##label OBE REFERENCE S02550 !$#authors Siebold, B.; Deutzmann, R.; Kuehn, K. !$#journal Eur. J. Biochem. (1988) 176:617-624 !$#title The arrangement of intra- and intermolecular disulfide bonds !1in the carboxyterminal, non-collagenous aggregation and !1cross-linking domain of basement-membrane type IV collagen. !$#cross-references MUID:89005112; PMID:2844531 !$#contents annotation; disulfide bonds GENETICS !$#gene GDB:COL4A1 !'##cross-references GDB:119791; OMIM:120130 !$#map_position 13q34-13q34 !$#introns 28/3; 48/3; 78/3; 93/3; 108/3; 129/3; 147/3; 156/3; 184/3; !1205/3; 217/3; 231/3; 260/3; 269/3; 286/3; 301/3; 319/3; 333/ !13; 362/1; 374/1; 429/1; 461/1; 489/1; 512/3; 576/3; 633/1; !1664/1; 699/1; 731/3; 782/1; 820/1; 876/1; 906/1; 957/1; 990/ !11; 1020/1; 1066/3; 1109/1; 1136/1; 1169/1; 1186/1; 1248/1; !11292/3; 1317/1; 1341/1; 1384/1; 1417/1; 1488/1; 1547/2; !11585/3; 1643/2 COMPLEX type IV collagen is a heterotrimer of two alpha 1(IV) chains !1and one alpha 2(IV) chain (see PIR:CGHU2B); small amounts of !1homotrimer can form; a polymeric network forms with !1tetrameric associations among trimer amino-terminal domains !1(disulfide and desmosine cross-links), dimeric associations !1among trimer carboxyl-terminal domains (with disulfide !1bonds), and both intra-trimer and inter-trimer associations !1in the interrupted helical domain (with disulfide and !1desmosine cross-links FUNCTION !$#description structural component of extracellular basement membrane CLASSIFICATION #superfamily collagen alpha 1(IV) chain KEYWORDS basement membrane; blocked amino end; cell binding; coiled !1coil; duplication; extracellular matrix; glycoprotein; !1hydroxylysine; hydroxyproline; trimer; triple helix FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-1669 #product collagen alpha 1(IV) chain #status predicted !8#label MAT\ !$29-162 #domain amino-terminal nonhelical, 7S #label 7SD\ !$163-1440 #domain interrupted helical #label COL\ !$414-452 #region integrin binding #status experimental\ !$597-599 #region cell attachment (R-G-D) motif\ !$917-919 #region cell attachment (R-G-D) motif\ !$968-970 #region cell attachment (R-G-D) motif\ !$1441-1669 #domain carboxyl-terminal nonhelical, NC1 #label NC1\ !$1451-1551 #domain collagen IV carboxyl-terminal repeat #label !8CT1\ !$1561-1665 #domain collagen IV carboxyl-terminal repeat #label !8CT2\ !$27 #modified_site blocked amino end (Ala) (in mature !8form) #status experimental\ !$31,36,39,41,125, !$434,467,470 #disulfide_bonds interchain #status predicted\ !$45,48,78,90,129, !$156,172,217,228, !$231,277,295,298, !$322,343,361,460, !$463,497,527,540, !$543,573,582,617, !$635,681,698,731, !$742,757,825,828, !$842,845,878,905, !$923,926,947,950, !$956,965,992,1025, !$1043,1046,1049, !$1066,1081,1084, !$1099,1117,1132, !$1150,1165,1182, !$1185,1188,1206, !$1235,1265,1283, !$1304,1319,1328, !$1340,1356,1371, !$1380,1407 #binding_site carbohydrate (Lys) (covalent) #status !8experimental\ !$45,48,78,90,129, !$156,217,228,231, !$277,295,298,322, !$343,361,460,463, !$497,527,543,573, !$582,617,635,681, !$698,731,742,757, !$825,828,842,845, !$878,905,923,926, !$950,956,965,992, !$1025,1043,1046, !$1049,1066,1081, !$1084,1099,1117, !$1132,1150,1165, !$1182,1185,1188, !$1206,1235,1265, !$1283,1304,1319, !$1328,1340,1356, !$1371,1380,1407 #modified_site 5-hydroxylysine (Lys) #status !8experimental\ !$54,63,75,84,87,96, !$102,105,108,111, !$117,120,123,138, !$141,147,150,153, !$159,167,178,181, !$184,187,190,199, !$205,208,211,214, !$280,283,289,301, !$304,307,310,328, !$331,349,352,358, !$364,367,370,373, !$384,387,399,413, !$416,419,422,425, !$439,445,448,451, !$479,485,491,494, !$503,512,518,524, !$530,546,549,552, !$555,561,567,570, !$576,588,594,603, !$606,623,626,629, !$632,648,654,657, !$660,669,672,675, !$678,687,692,695, !$704,710,713,716, !$722,725,739,745, !$748,751,754,763 #modified_site 4-hydroxyproline (Pro) #status !8experimental\ !$126 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$129 #modified_site allysine (Lys) #status predicted\ !$172,540,947 #modified_site 5-hydroxylysine (Lys) #status !8atypical\ !$272,645,839 #modified_site 4-hydroxyproline (Pro) #status !8atypical\ !$446-447 #cleavage_site Gly-Ile (gelatinase B) #status !8predicted\ !$766,775,784,787, !$790,796,799,804, !$810,816,822,834, !$860,863,869,872, !$875,887,890,893, !$899,902,911,920, !$932,935,971,974, !$977,986,1001,1004, !$1007,1019,1022, !$1031,1037,1055, !$1060,1075,1078, !$1090,1096,1108, !$1111,1123,1129, !$1138,1141,1159, !$1171,1176,1179, !$1194,1200,1203, !$1215,1224,1227, !$1244,1247,1250, !$1256,1259,1274, !$1277,1280,1286, !$1292,1298,1310, !$1313,1322,1337, !$1346,1349,1359, !$1362,1377,1392, !$1395,1398,1404, !$1422,1425,1431,1437 #modified_site 4-hydroxyproline (Pro) #status !8experimental\ !$1120,1268 #modified_site 5-hydroxylysine (Lys) (partial) !8#status experimental\ !$1120,1268 #binding_site carbohydrate (Lys) (covalent) (partial) !8#status experimental\ !$1214,1424 #modified_site 3-hydroxyproline (Pro) #status absent\ !$1392,1395,1398,1404 #modified_site 4-hydroxyproline (Pro) #status !8experimental\ !$1460-1548,1493-1551 #disulfide_bonds (or 1460-1551, 1493-1548) #status !8predicted\ !$1505-1511,1616-1622 #disulfide_bonds #status predicted\ !$1570-1662,1604-1665 #disulfide_bonds (or 1570-1665, 1604-1662) #status !8predicted SUMMARY #length 1669 #molecular-weight 160611 #checksum 6464 SEQUENCE /// ENTRY CGMS4B #type complete TITLE collagen alpha 1(IV) chain precursor - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 28-May-1986 #sequence_revision 31-Dec-1992 #text_change 16-Jun-2000 ACCESSIONS A33525; S01454; A28066; A02864; A25636; A29301; S19079; !1A32003; A31766; S19094; S16909; A25991; B25991; S17801; !1S01458 REFERENCE A33525 !$#authors Muthukumaran, G.; Blumberg, B.; Kurkinen, M. !$#journal J. Biol. Chem. (1989) 264:6310-6317 !$#title The complete primary structure for the alpha-1-chain of !1mouse collagen IV. Differential evolution of collagen IV !1domains. !$#cross-references MUID:89197932; PMID:2703490 !$#accession A33525 !'##molecule_type mRNA !'##residues 1-1669 ##label MUT !'##cross-references EMBL:J04694; NID:g556296; PIDN:AAA50292.1; !1PID:g556297 REFERENCE S01454 !$#authors Wood, L.; Theriault, N.; Vogeli, G. !$#journal FEBS Lett. (1988) 227:5-8 !$#title cDNA clones completing the nucleotide and derived amino acid !1sequence of the alpha 1 chain of basement membrane (type IV) !1collagen from mouse. !$#cross-references MUID:88112221; PMID:3338568 !$#accession S01454 !'##molecule_type mRNA !'##residues 1-185,'L',187-318,'S',320-368,'L',370-402,'F',404-480,'L', !1482-492,'H',494-711,'I',713-812,'Q',814-981,'H',983-1154 !1##label WOO !'##cross-references EMBL:X06777 REFERENCE A28066 !$#authors Killen, P.D.; Burbelo, P.; Sakurai, Y.; Yamada, Y. !$#journal J. Biol. Chem. (1988) 263:8706-8709 !$#title Structure of the amino-terminal portion of the murine !1alpha-1(IV) collagen chain and the corresponding region of !1the gene. !$#cross-references MUID:88243724; PMID:3379041 !$#accession A28066 !'##molecule_type mRNA !'##residues 1-129 ##label KI1 !'##cross-references EMBL:J03758; NID:g192669; PIDN:AAA37439.1; !1PID:g192670 REFERENCE A02864 !$#authors Oberbaeumer, I.; Laurent, M.; Schwarz, U.; Sakurai, Y.; !1Yamada, Y.; Vogeli, G.; Voss, T.; Siebold, B.; Glanville, !1R.W.; Kuehn, K. !$#journal Eur. J. Biochem. (1985) 147:217-224 !$#title Amino acid sequence of the non-collagenous globular domain !1(NC1) of the alpha-1(IV) chain of basement membrane collagen !1as derived from complementary DNA. !$#cross-references MUID:85127033; PMID:2578961 !$#accession A02864 !'##molecule_type mRNA !'##residues 1276-1669 ##label OBE !'##cross-references EMBL:X02201; NID:g50233; PIDN:CAA26132.1; !1PID:g1333876 REFERENCE A25636 !$#authors Nath, P.; Laurent, M.; Horn, E.; Sobel, M.E.; Zon, G.; !1Vogeli, G. !$#journal Gene (1986) 43:301-304 !$#title Isolation of an alpha-1 type-IV collagen cDNA clone using a !1synthetic oligodeoxynucleotide. !$#cross-references MUID:86301886; PMID:3755692 !$#accession A25636 !'##molecule_type mRNA !'##residues 1149-1396,'S',1398-1424 ##label NAT !'##cross-references EMBL:M14042; NID:g192286; PIDN:AAA37342.1; !1PID:g192287 !'##note the authors translated the codon CAG for residue 1374 as Arg REFERENCE A94680 !$#authors Kurkinen, M.; Condon, M.R.; Blumberg, B.; Barlow, D.P.; !1Quinones, S.; Saus, J.; Pihlajaniemi, T. !$#journal J. Biol. Chem. (1987) 262:8496-8499 !$#title Extensive homology between the carboxyl-terminal peptides of !1mouse alpha-1(IV) and alpha-2(IV) collagen. !$#cross-references MUID:87250460; PMID:3597383 !$#accession A29301 !'##molecule_type mRNA !'##residues 1441-1669 ##label KUR !'##cross-references EMBL:M15832; NID:g192282; PIDN:AAA37340.1; !1PID:g387115 REFERENCE S19079 !$#authors Killen, P.D.; Burbelo, P.D.; Martin, G.R.; Yamada, Y. !$#journal J. Biol. Chem. (1988) 263:12310-12314 !$#title Characterization of the promoter for the alpha-1(IV) !1collagen gene. DNA sequences within the first intron enhance !1transcription. !$#cross-references MUID:88315019; PMID:2842328 !$#accession S19079 !'##molecule_type DNA !'##residues 1-28 ##label KI2 !'##cross-references EMBL:J03944; NID:g192673; PIDN:AAA37442.1; !1PID:g466503 REFERENCE A92702 !$#authors Kaytes, P.; Wood, L.; Theriault, N.; Kurkinen, M.; Vogeli, !1G. !$#journal J. Biol. Chem. (1988) 263:19274-19277 !$#title Head-to-head arrangement of murine type IV collagen genes. !$#cross-references MUID:89066738; PMID:3198626 !$#accession A32003 !'##molecule_type DNA !'##residues 1-28 ##label KAY !'##cross-references EMBL:J04448; NID:g192666; PIDN:AAA37437.1; !1PID:g450449 REFERENCE A94220 !$#authors Burbelo, P.D.; Martin, G.R.; Yamada, Y. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:9679-9682 !$#title Alpha1(IV) and alpha2(IV) collagen genes are regulated by a !1bidirectional promoter and a shared enhancer. !$#cross-references MUID:89071759; PMID:3200851 !$#accession A31766 !'##molecule_type DNA !'##residues 1-28 ##label BUR !'##cross-references EMBL:M23333; NID:g340878; PIDN:AAA51625.1; !1PID:g535668 REFERENCE S19094 !$#authors Sakurai, Y.; Sullivan, M.; Yamada, Y. !$#journal J. Biol. Chem. (1986) 261:6654-6657 !$#title Alpha-1 type IV collagen gene evolved differently from !1fibrillar collagen genes. !$#cross-references MUID:86196099; PMID:3009468 !$#accession S19094 !'##molecule_type DNA !'##residues 1110-1135;1189-1316;1342-1383;1418-1487 ##label SAK !'##cross-references EMBL:M13027 REFERENCE S16909 !$#authors Schuppan, D.; Timpl, R.; Glanville, R.W. !$#journal FEBS Lett. (1980) 115:297-300 !$#title Discontinuities in the triple helical sequence Gly-X-Y of !1basement membrane (type IV) collagen. !$#cross-references MUID:80246483; PMID:6772473 !$#accession S16909 !'##molecule_type protein !'##residues 940-946,'G',948-949,'G',951-955,'G',957;1213-1228,'X', !11230-1234,'P',1236-1237,'Q',1239-1242;1435-1445,'SF' ##label !1SC1 REFERENCE A25991 !$#authors Schuppan, D.; Glanville, R.W.; Timpl, R. !$#journal Eur. J. Biochem. (1982) 123:505-512 !$#title Covalent structure of mouse type-IV collagen. Isolation, !1order and partial amino-acid sequence of cyanogen-bromide !1and tryptic peptides of pepsin fragment P1 from the alpha 1 !1(IV) chain. !$#cross-references MUID:82186723; PMID:6804236 !$#accession A25991 !'##molecule_type protein !'##residues 940-946,'X',948-949,'X',951-955,'X',957-964,'X',966-991, !1'X',993-1003,'X',1005-1009,'X',1011,'X',1013-1014,'X', !11016-1024,'X',1026-1042,'X',1044-1045,'X',1047-1048,'X', !11050-1051,'X',1053-1061,'X',1063-1065,'X',1067-1080,'X', !11082-1083,'X',1085-1106,'X',1108-1115,'DE',1118-1119,'X', !11121-1131,'X',1133-1149,'X',1151-1154 ##label SC2 !$#accession B25991 !'##molecule_type protein !'##residues 1173-1181,'X',1183-1184,'X',1186-1187,'X',1189-1205,'Q', !11207,'XE',1210-1234,'P',1236-1237,'Q',1239-1244;1245, !1'SM';'GP',1247-1248,'F',1250-1251,'IN',1254-1257, !1'TPGXQ';'M',1259-1261,'G',1263,'SP',1266,'IT',1269,'SK', !11272,'DM';1275,'L',1277-1282;1316-1318,'X',1320-1327,'X', !11329-1335,'P',1337-1339,'X',1341-1351,'DGV';'S', !11417-1419;1420-1445,'SF' ##label SC3 REFERENCE S17801 !$#authors Weber, S.; Engel, J.; Wiedemann, H.; Glanville, R.W.; Timpl, !1R. !$#journal Eur. J. Biochem. (1984) 139:401-410 !$#title Subunit structure and assembly of the globular domain of !1basement-membrane collagen type IV. !$#cross-references MUID:84132058; PMID:6698021 !$#accession S17801 !'##molecule_type protein !'##residues 1435-1443 ##label WEB GENETICS !$#introns 28/3; 48/3; 78/3; 93/3; 108/3; 129/3 !$#note the list of introns may be incomplete CLASSIFICATION #superfamily collagen alpha 1(IV) chain KEYWORDS basement membrane; cell binding; coiled coil; duplication; !1extracellular matrix; glycoprotein; hydroxylysine; !1hydroxyproline; trimer; triple helix FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-1669 #product collagen alpha 1(IV) chain #status predicted !8#label MAT\ !$28-162 #domain 7S #label 7SD\ !$163-1440 #domain collagenous, triple helix #label COL\ !$597-599 #region cell attachment (R-G-D) motif\ !$781-783 #region cell attachment (R-G-D) motif\ !$917-919 #region cell attachment (R-G-D) motif\ !$968-970 #region cell attachment (R-G-D) motif\ !$1441-1669 #domain carboxyl-terminal nonhelical, NC1 #label NC1\ !$1441-1552 #region duplication\ !$1553-1669 #region duplication\ !$31,36,39,41,434, !$467,470 #disulfide_bonds interchain #status predicted\ !$126 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$971,974,977,986, !$989,1001,1007,1019, !$1022,1031,1037, !$1040,1055,1060, !$1063,1075,1078, !$1090,1093,1096, !$1102,1108,1111, !$1114,1123,1129, !$1138,1141,1176, !$1179,1194,1200, !$1203,1215,1221, !$1224,1227,1244, !$1256,1259,1292, !$1298,1310,1313, !$1322,1337,1346, !$1349,1422,1425, !$1431,1437,1440 #modified_site hydroxyproline (Pro) #status !8experimental\ !$1214,1424 #modified_site 4-hydroxyproline (Pro) #status !8experimental\ !$1304 #modified_site 5-hydroxylysine (Lys) #status !8experimental\ !$1505-1511,1616-1622 #disulfide_bonds #status predicted SUMMARY #length 1669 #molecular-weight 160680 #checksum 2835 SEQUENCE /// ENTRY S22917 #type complete TITLE collagen alpha 5(IV) chain precursor, renal splice form - human ALTERNATE_NAMES procollagen alpha 5(IV) chain CONTAINS collagen alpha 5(IV) chain precursor, leukocyte splice form ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1993 #sequence_revision 27-Feb-1997 #text_change 21-Jul-2000 ACCESSIONS S22917; A54365; A57079; A37122; I54317; A34850; S18850; !1I56971; I76598; A35335; I56975; I54188; A37969; S19029 REFERENCE S22917 !$#authors Zhou, J.; Hertz, J.M.; Leinonen, A.; Tryggvason, K. !$#journal J. Biol. Chem. (1992) 267:12475-12481 !$#title Complete amino acid sequence of the human alpha-5(IV) !1collagen chain and identification of a single-base mutation !1in exon 23 converting glycine 521 in the collagenous domain !1to cysteine in an Alport syndrome patient. !$#cross-references MUID:92316923; PMID:1352287 !$#accession S22917 !'##molecule_type mRNA !'##residues 1-967 ##label ZHO !'##cross-references GB:M90464; NID:g180826; PIDN:AAA52046.1; !1PID:g553234 REFERENCE A54365 !$#authors Zhou, J.; Leinonen, A.; Tryggvason, K. !$#journal J. Biol. Chem. (1994) 269:6608-6614 !$#title Structure of the human type IV collagen COL4A5 gene. !$#cross-references MUID:94165049; PMID:8120014 !$#accession A54365 !'##molecule_type DNA !'##residues 1-922 ##label ZH2 !'##cross-references GB:U04470; NID:g463378; GB:U04520; NID:g463428; !1PIDN:AAC27816.1; PID:g463430 REFERENCE A57079 !$#authors Zhou, J.; Mochizuki, T.; Smeets, H.; Antignac, C.; Laurila, !1P.; de Paepe, A.; Tryggvason, K.; Reeders, S.T. !$#journal Science (1993) 261:1167-1169 !$#title Deletion of the paired alpha5(IV) and alpha6(IV) collagen !1genes in inherited smooth muscle tumors. !$#cross-references MUID:93361972; PMID:8356449 !$#accession A57079 !'##molecule_type DNA !'##residues 1-27 ##label ZH4 !'##cross-references GB:Z37153; NID:g587203; PIDN:CAA85512.1; !1PID:g587204 REFERENCE A37122 !$#authors Pihlajaniemi, T.; Pohjolainen, E.R.; Myers, J.C. !$#journal J. Biol. Chem. (1990) 265:13758-13766 !$#title Complete primary structure of the triple-helical region and !1the carboxyl-terminal domain of a new type IV collagen !1chain, alpha5(IV). !$#cross-references MUID:90337990; PMID:2380186 !$#accession A37122 !'##molecule_type mRNA !'##residues 84-439,'GS',442-624,'LALQ',629-666,'FR',669-887,'R', !1889-1264,1271-1691 ##label PIH !'##cross-references GB:J05558; EMBL:M58526; NID:g1314209 !'##note submitted to the EMBL Data Library, February 1991 !'##note the authors translated the codon GCC for residue 115 as Val REFERENCE I54317 !$#authors Renieri, A.; Seri, M.; Myers, J.C.; Pihlajaniemi, T.; !1Massella, L.; Rizzoni, G.; De Marchi, M. !$#journal Hum. Mol. Genet. (1992) 1:127-129 !$#title De novo mutation in the COL4A5 gene converting glycine 325 !1to glutamic acid in Alport syndrome. !$#cross-references MUID:93244772; PMID:1363780 !$#accession I54317 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 313-324,'E',326-330 ##label REN !'##cross-references GB:S59334; NID:g299946; PIDN:AAD13909.1; !1PID:g4261609 REFERENCE A34850 !$#authors Hostikka, S.L.; Eddy, R.L.; Byers, M.G.; Hoeyhtyae, M.; !1Shows, T.B.; Tryggvason, K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:1606-1610 !$#title Identification of a distinct type IV collagen alpha chain !1with restricted kidney distribution and assignment of its !1gene to the locus of X chromosome-linked Alport syndrome. !$#cross-references MUID:90160375; PMID:1689491 !$#accession A34850 !'##molecule_type mRNA !'##residues 914-1264,1271-1691 ##label HOS !'##cross-references EMBL:M31115; NID:g180824; PIDN:AAA52045.1; !1PID:g180825 REFERENCE A37969 !$#authors Zhou, J.; Hostikka, S.L.; Chow, L.T.; Tryggvason, K. !$#journal Genomics (1991) 9:1-9 !$#title Characterization of the 3' half of the human type IV !1collagen alpha-5 gene that is affected in the Alport !1syndrome. !$#cross-references MUID:91169491; PMID:2004755 !$#accession S18850 !'##molecule_type DNA !'##residues 924-1264,1271-1691 ##label ZH3 !'##cross-references EMBL:M63455; EMBL:M63456; EMBL:M63457; EMBL:M63458; !1EMBL:M63459; EMBL:M63460; EMBL:M63461; EMBL:M63462; !1EMBL:M63463; EMBL:M63464; EMBL:M63465; EMBL:M63466; !1EMBL:M63467; EMBL:M63468; EMBL:M63470; EMBL:M63471; !1EMBL:M63472; EMBL:M63473; NID:g177922; PIDN:AAA51558.1; !1PID:g177924 REFERENCE I56971 !$#authors Guo, C.; Van Damme, B.; Van Damme-Lombaerts, R.; Van den !1Berghe, H.; Cassiman, J.J.; Marynen, P. !$#journal Kidney Int. (1993) 44:1316-1321 !$#title Differential splicing of COL4A5 mRNA in kidney and white !1blood cells: a complex mutation in the COL4A5 gene of an !1Alport patient deletes the NC1 domain. !$#cross-references MUID:94133540; PMID:8301933 !$#accession I56971 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1258-1276 ##label GUO1 !'##cross-references GB:S69168; NID:g545095; PIDN:AAC60612.1; !1PID:g545096 !'##note kidney splice form !$#accession I76598 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1284-1291,'TFLGYLACLV' ##label GUO2 !'##cross-references GB:S69169; NID:g545097; PIDN:AAC60613.1; !1PID:g545098 !'##note frameshift mutation in patient with Alport syndrome REFERENCE A35335 !$#authors Myers, J.C.; Jones, T.A.; Pohjolainen, E.R.; Kadri, A.S.; !1Goddard, A.D.; Sheer, D.; Solomon, E.; Pihlajaniemi, T. !$#journal Am. J. Hum. Genet. (1990) 46:1024-1033 !$#title Molecular cloning of alpha5(IV) collagen and assignment of !1the gene to the region of the X chromosome containing the !1Alport syndrome locus. !$#cross-references MUID:90252791; PMID:2339699 !$#accession A35335 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1448-1477 ##label MYE REFERENCE I56975 !$#authors Nakazato, H.; Hattori, S.; Ushijima, T.; Matsuura, T.; !1Koitabashi, Y.; Takada, T.; Yoshioka, K.; Endo, F.; Matsuda, !1I. !$#journal Kidney Int. (1994) 46:1307-1314 !$#title Mutations in the COL4A5 gene in Alport syndrome: a possible !1mutation in primordial germ cells. !$#cross-references MUID:95156893; PMID:7853788 !$#accession I56975 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1595-1602 ##label NAK !'##cross-references GB:S75903; NID:g913882; PIDN:AAB33374.1; !1PID:g913883 !'##note permature termination mutation from a patient with Alport !1syndrome; one other mutation is described REFERENCE I54188 !$#authors Lemmink, H.H.; Schroeder, C.H.; Brunner, H.G.; Nelen, M.R.; !1Zhou, J.; Tryggvason, K.; Haagsma-Schouten, W.A.; Roodvoets, !1A.P.; Rascher, W.; van Oost, B.A.; Smeets, H.J.M. !$#journal Genomics (1993) 17:485-489 !$#title Identification of four novel mutations in the COL4A5 gene of !1patients with Alport syndrome. !$#cross-references MUID:94010948; PMID:8406498 !$#accession I54188 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1604-1607,'VHDAYKC' ##label LEM !'##cross-references GB:S65767; NID:g425563; PIDN:AAD13967.1; !1PID:g4261667 !'##note frameshift mutation from a patient with Alport syndrome; five !1other mutations are described COMMENT Prolines and lysines at the third position of the tripeptide !1repeating unit (G-X-Y) are hydroxylated to varying extents. !1Prolines are predominately 4-hydroxylated. Lysines are !15-hydroxylated and subsequently O-glycosylated. GENETICS !$#gene GDB:COL4A5; ATS !'##cross-references GDB:120596; OMIM:303630 !$#map_position Xq22-Xq22 !$#introns 27/3; 47/3; 77/3; 92/3; 107/3; 128/3; 146/3; 155/3; 182/3; !1203/3; 215/3; 229/3; 260/3; 278/3; 297/3; 312/3; 330/3; 344/ !13; 388/1; 447/1; 475/1; 505/1; 529/3; 593/3; 650/1; 681/1; !1716/1; 748/3; 799/1; 837/1; 893/1; 923/1; 973/1; 1006/1; !11036/1; 1082/3; 1125/1; 1152/1; 1185/1; 1202/1; 1264/1; !11314/3; 1339/1; 1363/1; 1406/1; 1439/1; 1510/1; 1569/2; !11607/3; 1665/2 !$#note the alpha 5(IV) and alpha 6(IV) chain genes are encoded on !1opposite strands with overlapping promotor regions; defects !1in this gene can result in Alport's syndrome COMPLEX This minor type IV collagen is thought to form a !1heterotrimer of two alpha 5(IV) chains and one alpha 6(IV) !1chain (see PIR:CGHU6B). A polymeric network forms with !1tetrameric associations among trimer amino-terminal domains !1(with disulfide and desmosine cross-links), dimeric !1associations among trimer carboxyl-terminal domains (with !1disulfide bonds), and both intra-trimer and inter-trimer !1associations in the interrupted helical domain (with !1disulfide and desmosine cross-links). FUNCTION !$#description minor structural component of extracellular basement !1membrane CLASSIFICATION #superfamily collagen alpha 1(IV) chain KEYWORDS Alport syndrome; basement membrane; coiled coil; !1extracellular matrix; glycoprotein; hydroxylysine; !1hydroxyproline; kidney; leukocyte; trimer; triple helix FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-1691 #product collagen alpha 5(IV) chain, renal splice !8form #status predicted #label MAT1\ !$27-1264,1271-1691 #product collagen alpha 5(IV) chain, leukocyte splice !8form #status predicted #label MAT2\ !$27-41 #domain amino-terminal nonhelical, NC2 #status !8predicted #label NC2\ !$42-1462 #region interrupted helical\ !$1463-1691 #domain carboxyl-terminal nonhelical, NC1 #status !8predicted #label NC1\ !$1473-1573 #domain collagen IV carboxyl-terminal repeat #label !8CT1\ !$1583-1687 #domain collagen IV carboxyl-terminal repeat #label !8CT2\ !$29,32,38,40,124, !$451,481,484 #disulfide_bonds interchain #status predicted\ !$125 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$1482-1570,1515-1573 #disulfide_bonds (or 1482-1573, 1515-1570) #status !8predicted\ !$1527-1533,1638-1644 #disulfide_bonds #status predicted\ !$1592-1684,1626-1687 #disulfide_bonds (or 1592-1687, 1626-1684) #status !8predicted SUMMARY #length 1691 #molecular-weight 161631 #checksum 6477 SEQUENCE /// ENTRY CGHU3B #type complete TITLE collagen alpha 3(IV) chain precursor, long splice form - human ALTERNATE_NAMES Goodpasture antigen; procollagen alpha 3(IV) chain long splice form ORGANISM #formal_name Homo sapiens #common_name man DATE 28-Oct-1994 #sequence_revision 03-Oct-1995 #text_change 22-Jun-1999 ACCESSIONS A54763; A43928; A44043; A45971; A39786 REFERENCE A54763 !$#authors Mariyama, M.; Leinonen, A.; Mochizuki, T.; Tryggvason, K.; !1Reeders, S.T. !$#journal J. Biol. Chem. (1994) 269:23013-23017 !$#title Complete primary structure of the human alpha3(IV) collagen !1chain. Coexpression of the alpha3(IV) collagen chains in !1human tissues. !$#cross-references MUID:94364994; PMID:8083201 !$#accession A54763 !'##molecule_type mRNA !'##residues 1-1670 ##label MAR !'##cross-references GB:X80031; NID:g577563; PID:g577564 !'##experimental_source kidney REFERENCE A43928 !$#authors Turner, N.; Mason, P.J.; Brown, R.; Fox, M.; Povey, S.; !1Rees, A.; Pusey, C.D. !$#journal J. Clin. Invest. (1992) 89:592-601 !$#title Molecular cloning of the human Goodpasture antigen !1demonstrates it to be the alpha3 chain of type IV collagen. !$#cross-references MUID:92147878; PMID:1737849 !$#accession A43928 !'##molecule_type mRNA !'##residues 1331-1524,'I',1526-1670 ##label TUR !'##cross-references GB:M81379 !'##experimental_source kidney REFERENCE A44043 !$#authors Quinones, S.; Bernal, D.; Garcia-Sogo, M.; Elena, S.F.; !1Saus, J. !$#journal J. Biol. Chem. (1992) 267:19780-19784 !$#title Exon/intron structure of the human alpha 3(IV) gene !1encompassing the Goodpasture antigen (alpha 3(IV)NC1). !1Identification of a potentially antigenic region at the !1triple helix/NC1 domain junction. !$#cross-references MUID:93015826; PMID:1400291 !$#accession A44043 !'##molecule_type DNA; mRNA !'##residues 1386-1670 ##label QUI !'##cross-references GB:M92993; NID:g177895; PIDN:AAA21610.1; !1PID:g177896 !'##note sequence extracted from NCBI backbone (NCBIP:115597) REFERENCE A44738 !$#authors Quinones, S.; Bernal, D.; Garcia-Sogo, M.; Elena, S.F.; !1Saus, J. !$#journal J. Biol. Chem. (1994) 269:17358 !$#cross-references MUID:94274734; PMID:8006044 !$#contents annotation; erratum; correction to intronic sequence in !1A44043 REFERENCE A45971 !$#authors Bernal, D.; Quinones, S.; Saus, J. !$#journal J. Biol. Chem. (1993) 268:12090-12094 !$#title The human mRNA encoding the Goodpasture antigen is !1alternatively spliced. !$#cross-references MUID:93280184; PMID:8505332 !$#accession A45971 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1427-1444 ##label BER !'##note sequence extracted from NCBI backbone (NCBIP:133363); sequence !1incorrectly identified as being determined by protein !1sequencing and incompletely represented REFERENCE A39786 !$#authors Morrison, K.E.; Mariyama, M.; Yang-Feng, T.L.; Reeders, S.T. !$#journal Am. J. Hum. Genet. (1991) 49:545-554 !$#title Sequence and localization of a partial cDNA encoding the !1human alpha3 chain of type IV collagen. !$#cross-references MUID:91353570; PMID:1882840 !$#accession A39786 !'##molecule_type mRNA !'##residues 1453-1593,'A',1595-1670 ##label MOR !'##cross-references GB:S55790; NID:g234418; PIDN:AAB19637.1; !1PID:g234419 COMMENT Prolines and lysines at the third position of the tripeptide !1repeating unit (G-X-Y) are hydroxylated to varying extents. !1Prolines are predominately 4-hydroxylated. Lysines are !15-hydroxylated and subsequently O-glycosylated. COMMENT In Goodpasture's syndrome, an autoimmune response develops !1against an epitope in the carboxyl-terminal nonhelical NC1 !1domain. GENETICS !$#gene GDB:COL4A3 !'##cross-references GDB:128351; OMIM:120070 !$#map_position 2q36-2q37 !$#introns 1385/1; 1418/1; 1488/1; 1547/2; 1585/3; 1643/2 #status !1incomplete !$#note the alpha 3(IV) and alpha 4(IV) chain genes are encoded on !1opposite strands with overlapping promotor regions; defects !1in this gene can result in recessive form Alport's syndrome COMPLEX This minor type IV collagen is thought to form a !1heterotrimer of two alpha 3(IV) chains and one alpha 4(IV) !1chain (see PIR:CGHU1B). A polymeric network forms with !1tetrameric associations among trimer amino-terminal domains !1(with disulfide and desmosine cross-links), dimeric !1associations among trimer carboxyl-terminal domains (with !1disulfide bonds), and both intra-trimer and inter-trimer !1associations in the interrupted helical domain (with !1disulfide and desmosine cross-links). FUNCTION !$#description minor structural component of extracellular basement !1membrane in kidney glomeruli, lung aveoli, synaptic muscle !1fibers, lens capsule, cochlea, and brain CLASSIFICATION #superfamily collagen alpha 1(IV) chain KEYWORDS alternative splicing; basement membrane; cell binding; !1coiled coil; extracellular matrix; glycoprotein; !1hydroxylysine; hydroxyproline; trimer; triple helix FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-1670 #product collagen alpha 3(IV) chain, long splice form !8#status predicted #label MAT\ !$29-42 #domain amino-terminal nonhelical, NH1 #label NH1\ !$43-1438 #region interrupted helical\ !$791-793 #region cell attachment (R-G-D) motif\ !$996-998 #region cell attachment (R-G-D) motif\ !$1154-1156 #region cell attachment (R-G-D) motif\ !$1306-1308 #region cell attachment (R-G-D) motif\ !$1345-1347 #region cell attachment (R-G-D) motif\ !$1432-1434 #region cell attachment (R-G-D) motif\ !$1439-1670 #domain carboxyl-terminal nonhelical, NC1 #label NC1\ !$1451-1551 #domain collagen IV carboxyl-terminal repeat #label !8CT1\ !$1561-1665 #domain collagen IV carboxyl-terminal repeat #label !8CT2\ !$31,33,39,41,125, !$422,476,479,682, !$722,809,1387 #disulfide_bonds interchain #status predicted\ !$253 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$1460-1548,1493-1551 #disulfide_bonds (or 1460-1551, 1493-1548) #status !8predicted\ !$1505-1511,1616-1622 #disulfide_bonds #status predicted\ !$1570-1662,1604-1665 #disulfide_bonds (or 1570-1665, 1604-1662) #status !8predicted SUMMARY #length 1670 #molecular-weight 161725 #checksum 818 SEQUENCE /// ENTRY CGHU2B #type complete TITLE collagen alpha 2(IV) chain precursor - human ALTERNATE_NAMES procollagen alpha 2(IV) chain ORGANISM #formal_name Homo sapiens #common_name man DATE 07-Jun-1990 #sequence_revision 03-Oct-1995 #text_change 22-Jun-1999 ACCESSIONS A32024; S00007; S02624; S00246; S17678; S16911; B32117; !1S16877; S00165; S39615; S16912; B58517; S01450; S02550; !1B27114; C24432; S16908 REFERENCE A32024 !$#authors Hostikka, S.L.; Tryggvason, K. !$#journal J. Biol. Chem. (1988) 263:19488-19493 !$#title The complete primary structure of the alpha2 chain of human !1type IV collagen and comparison with the alpha1(IV) chain. !$#cross-references MUID:89066769; PMID:3198637 !$#accession A32024 !'##molecule_type mRNA !'##residues 1-1712 ##label HOS1 !'##cross-references EMBL:J04210; EMBL:X05610; GB:M20753; NID:g29550; !1PIDN:CAA29098.1; PID:g29551 REFERENCE S00007 !$#authors Hostikka, S.L.; Kurkinen, M.; Tryggvason, K. !$#journal FEBS Lett. (1987) 216:281-286 !$#title Nucleotide sequence coding for the human type IV collagen !1alpha-2 chain cDNA reveals extensive homology with the NC-1 !1domain of alpha-1(IV) but not with the collagenous domain or !13'-untranslated region. !$#cross-references MUID:87219158; PMID:3582677 !$#accession S00007 !'##molecule_type mRNA !'##residues 1254-1398,'V',1400-1712 ##label HOS2 !'##cross-references EMBL:J04210; EMBL:X05610; GB:M20753; NID:g29550; !1PIDN:CAA29098.1; PID:g29551 !'##note 1399-Ile was also found REFERENCE S02624 !$#authors Hostikka, S.L.; Tryggvason, K. !$#journal FEBS Lett. (1987) 224:297-305 !$#title Extensive structural differences between genes for the alpha !1(1) and alpha(2) chains of type IV collagen despite !1conservation of coding sequences. !$#cross-references MUID:88083553; PMID:2826228 !$#accession S02624 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1347-1350;1377-1383;1426-1432;1465-1471;1529-1535;1625-1630 !1##label HOS3 !'##note complete nucleotide sequence not shown REFERENCE S00246 !$#authors Brazel, D.; Pollner, R.; Oberbaeumer, I.; Kuehn, K. !$#journal Eur. J. Biochem. (1988) 172:35-42 !$#title Human basement membrane collagen (type IV): the amino acid !1sequence of the alpha2(IV) chain and its comparison with the !1alpha1(IV) chain reveals deletions in the alpha1(IV) chain. !$#cross-references MUID:88151998; PMID:3345760 !$#accession S00246 !'##molecule_type mRNA !'##residues 1-682,'G',684-1043 ##label BRA !'##cross-references EMBL:X05562; NID:g30075; PIDN:CAA29076.1; !1PID:g30076 REFERENCE S17678 !$#authors Oberbaeumer, I. !$#submission submitted to the EMBL Data Library, June 1987 !$#accession S17678 !'##molecule_type mRNA !'##residues 1-470,'P',472-682,'G',684-1043 ##label OBE !'##cross-references EMBL:X05562; NID:g30075; PIDN:CAA29076.1; !1PID:g30076 REFERENCE S02738 !$#authors Poeschl, E.; Pollner, R.; Kuehn, K. !$#journal EMBO J. (1988) 7:2687-2695 !$#title The genes for the alpha1(IV) and alpha2(IV) chains of human !1basement membrane collagen type IV are arranged head-to-head !1and separated by a bidirectional promoter of unique !1structure. !$#cross-references MUID:89030632; PMID:2846280 !$#accession S16911 !'##status translation not shown !'##molecule_type DNA !'##residues 1-33 ##label POE !'##cross-references EMBL:X12784; GB:M36963; NID:g30072; !1PIDN:CAA31275.1; PID:g30073 REFERENCE A92690 !$#authors Soininen, R.; Huotari, M.; Hostikka, S.L.; Prockop, D.J.; !1Tryggvason, K. !$#journal J. Biol. Chem. (1988) 263:17217-17220 !$#title The structural genes for alpha1 and alpha2 chains of human !1type IV collagen are divergently encoded on opposite DNA !1strands and have an overlapping promoter region. !$#cross-references MUID:89034231; PMID:3182844 !$#accession B32117 !'##molecule_type DNA !'##residues 1-33 ##label SOI1 !'##cross-references EMBL:J04217; EMBL:J05039; NID:g180759; !1PIDN:AAA53097.1; PID:g553233 REFERENCE S16876 !$#authors Soininen, R.; Huotari, M.; Ganguly, A.; Prockop, D.J.; !1Tryggvason, K. !$#journal J. Biol. Chem. (1989) 264:13565-13571 !$#title Structural organization of the gene for the alpha-1 chain of !1human type IV collagen. !$#cross-references MUID:89340433; PMID:2701944 !$#accession S16877 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-33 ##label SOI2 !'##cross-references EMBL:J04217; NID:g180759; PIDN:AAA53097.1; !1PID:g553233; EMBL:J05039 !'##note this sequence was submitted to the EMBL Data Library, October !11988 REFERENCE S00165 !$#authors Siebold, B.; Qian, R.Q.; Glanville, R.W.; Hofmann, H.; !1Deutzmann, R.; Kuehn, K. !$#journal Eur. J. Biochem. (1987) 168:569-575 !$#title Construction of a model for the aggregation and !1cross-linking region (7S domain) of type IV collagen based !1upon an evaluation of the primary structure of the alpha-1 !1and alpha-2 chains in this region. !$#cross-references MUID:88029476; PMID:3117548 !$#accession S00165 !'##molecule_type protein !'##residues 37-247 ##label SIE1 !'##note the sequence from Fig. 4 is inconsistent with that from Fig. 3 !1in having 175-Gly REFERENCE S39614 !$#authors Eble, J.A.; Golbik, R.; Mann, K.; Kuehn, K. !$#journal EMBO J. (1993) 12:4795-4802 !$#title The alpha-1-beta-1 integrin recognition site of the basement !1membrane collagen molecule [alpha-1(IV)](2)-alpha-2(IV). !$#cross-references MUID:94038963; PMID:8223488 !$#accession S39615 !'##molecule_type protein !'##residues 407-570 ##label EBL REFERENCE S16910 !$#authors MacWright, R.S.; Benson, V.A.; Lovello, K.T.; van der Rest, !1M.; Fietzek, P.P. !$#journal Biochemistry (1983) 22:4940-4948 !$#title Isolation and characterization of pepsin-solubilized human !1basement membrane (type IV) collagen peptides. !$#cross-references MUID:84053346; PMID:6416291 !$#accession S16912 !'##molecule_type protein !'##residues 490-492,'X',494-496;675-677,'G',679-680,'G',682,684-685,'P' !1##label MAC !'##experimental_source placenta REFERENCE S16908 !$#authors Glanville, R.W.; Rauter, A. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1981) 362:943-951 !$#title Pepsin fragments of human placental basement-membrane !1collagens showing interrupted triple-helical amino acid !1sequences. !$#cross-references MUID:82005835; PMID:6792033 !$#accession B58517 !'##molecule_type protein !'##residues 490-492,'X',494-501,'P',503-507;952-957,'X',959-966,'X', !1968;984-986,'X',988-989,'X',991-992;1081-1105,'X',1107-1117, !1'X',1119;1167-1168,'L',1170,'I',1172-1174,'X',1176-1177,'X', !11179,'M',1181-1185 ##label GLA REFERENCE S01450 !$#authors Killen, P.D.; Francomano, C.A.; Yamada, Y.; Modi, W.S.; !1O'Brien, S.J. !$#journal Hum. Genet. (1987) 77:318-324 !$#title Partial structure of the human alpha-2(IV) collagen chain !1and chromosomal localization of the gene (COL4A2). !$#cross-references MUID:88085168; PMID:3692475 !$#accession S01450 !'##molecule_type mRNA !'##residues 1040,'L',1042-1398,'V',1400-1418,'M',1420-1635,'V', !11637-1712 ##label KIL !'##cross-references EMBL:M24766; NID:g537328; PIDN:AAA52043.1; !1PID:g537329 REFERENCE S02550 !$#authors Siebold, B.; Deutzmann, R.; Kuehn, K. !$#journal Eur. J. Biochem. (1988) 176:617-624 !$#title The arrangement of intra- and intermolecular disulfide bonds !1in the carboxyterminal, non-collagenous aggregation and !1cross-linking domain of basement-membrane type IV collagen. !$#cross-references MUID:89005112; PMID:2844531 !$#accession S02550 !'##molecule_type protein !'##residues 1480-1535;1545-1614;1617-1662,'H',1664-1700, !1'G';1705-1708;1710-1712 ##label SIE2 !'##note the sequence form Fig. 7 is inconsistent with that shown in !1Fig. 11 in having 1701-His REFERENCE A27114 !$#authors Myers, J.C.; Howard, P.S.; Jelen, A.M.; Dion, A.S.; Macarak, !1E.J. !$#journal J. Biol. Chem. (1987) 262:9231-9238 !$#title Duplication of type IV collagen COOH-terminal repeats and !1species-specific expression of alpha-1(IV) and alpha-2(IV) !1collagen genes. !$#cross-references MUID:87250571; PMID:2439508 !$#accession B27114 !'##molecule_type mRNA !'##residues 1486-1574,'I',1576-1712 ##label MYE !'##cross-references EMBL:J02760; NID:g180425; PIDN:AAA58422.1; !1PID:g180426 COMMENT Prolines and lysines at the third position of the tripeptide !1repeating unit (G-X-Y) are hydroxylated to varying extents. !1Prolines are predominately 4-hydroxylated. Lysines are !15-hydroxylated and subsequently O-glycosylated. GENETICS !$#gene GDB:COL4A2 !'##cross-references GDB:119792; OMIM:120090 !$#map_position 13q34-13q34 !$#introns 15/2; 33/3; 1347/1; 1380/1; 1429/1; 1468/1; 1532/1; 1527/3 !1#status incomplete !$#note the alpha 1(IV) and alpha 2(IV) chain genes are encoded on !1opposite strands with overlapping promotor regions COMPLEX Type IV collagen is a heterotrimer of two alpha 1(IV) chains !1(see PIR:CGHU4B) and one alpha 2(IV) chain. A polymeric !1network forms with tetrameric associations among trimer !1amino-terminal domains (with disulfide and desmosine !1cross-links), dimeric associations among trimer !1carboxyl-terminal domains (with disulfide bonds), and both !1intra-trimer and inter-trimer associations in the !1interrupted helical domain (with disulfide and desmosine !1cross-links). FUNCTION !$#description structural component of basement membrane CLASSIFICATION #superfamily collagen alpha 1(IV) chain KEYWORDS basement membrane; cell binding; coiled coil; extracellular !1matrix; glycoprotein; heterotrimer; hydroxylysine; !1hydroxyproline; triple helix FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-1712 #product collagen alpha 2(IV) chain #status predicted !8#label MAT\ !$29-57 #domain amino-terminal nonhelical, NH1 #label NH1\ !$58-1485 #region interrupted helical\ !$362-364 #region cell attachment (R-G-D) motif\ !$784-786 #region cell attachment (R-G-D) motif\ !$868-870 #region cell attachment (R-G-D) motif\ !$889-891 #region cell attachment (R-G-D) motif\ !$970-972 #region cell attachment (R-G-D) motif\ !$1069-1071 #region cell attachment (R-G-D) motif\ !$1228-1230 #region cell attachment (R-G-D) motif\ !$1452-1454 #region cell attachment (R-G-D) motif\ !$1486-1712 #domain carboxyl-terminal nonhelical, NC1 #label NC1\ !$1495-1593 #domain collagen IV carboxyl-terminal repeat #label !8CT1\ !$1603-1708 #domain collagen IV carboxyl-terminal repeat #label !8CT2\ !$42,47,51,53,137, !$483,485 #disulfide_bonds interchain #status predicted\ !$57,87,90,102,165, !$168,225,239,242 #binding_site carbohydrate (Lys) (covalent) #status !8predicted\ !$57 #modified_site 5-hydroxylysine (Lys) #status !8atypical\ !$63,75,96,114,120, !$123,132,150,159, !$186,189,198,201, !$213,216,219,496, !$499,955,964,1103, !$1115,1172,1181,1184 #modified_site 4-hydroxyproline (Pro) #status !8experimental\ !$87,90,102,165,168, !$225,239,242 #modified_site 5-hydroxylysine (Lys) #status !8experimental\ !$138 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$209 #modified_site 4-hydroxyproline (Pro) #status !8atypical\ !$661-681 #disulfide_bonds #status predicted\ !$1275 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$1504-1590,1537-1593 #disulfide_bonds (or 1504-1593, 1537-1590) #status !8experimental\ !$1549-1555,1658-1665 #disulfide_bonds #status experimental\ !$1612-1705,1646-1708 #disulfide_bonds (or 1612-1708, 1646-1705) #status !8experimental SUMMARY #length 1712 #molecular-weight 167535 #checksum 1910 SEQUENCE /// ENTRY CGHU1B #type complete TITLE collagen alpha 4(IV) chain precursor - human ALTERNATE_NAMES procollagen alpha 4(IV) chain ORGANISM #formal_name Homo sapiens #common_name man DATE 06-Feb-1995 #sequence_revision 03-Oct-1995 #text_change 16-Jun-2000 ACCESSIONS A55360; S36854; S28777 REFERENCE A55360 !$#authors Leinonen, A.; Mariyama, M.; Mochizuki, T.; Tryggvason, K.; !1Reeders, S.T. !$#journal J. Biol. Chem. (1994) 269:26172-26177 !$#title Complete primary structure of the human type IV collagen !1alpha4(IV) chain. Comparison with structure and expression !1of the other alpha(IV) chains. !$#cross-references MUID:95014445; PMID:7523402 !$#accession A55360 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-1690 ##label LEI !'##cross-references GB:X81053; NID:g574805; PIDN:CAA56943.1; !1PID:g574806 REFERENCE S36854 !$#authors Sugimoto, M.; Oohashi, T.; Yoshioka, H.; Matsuo, N.; !1Ninomiya, Y. !$#journal FEBS Lett. (1993) 330:122-128 !$#title cDNA isolation and partial gene structure of the human !1alpha-4(IV) collagen chain. !$#cross-references MUID:93374047; PMID:8365481 !$#accession S36854 !'##molecule_type DNA; mRNA !'##residues 1219-1658,'FE',1661-1690 ##label SUG !'##cross-references DDBJ:D17391; NID:g440365; PIDN:BAA04214.1; !1PID:g457161 !'##experimental_source whole eye REFERENCE S28777 !$#authors Kamagata, Y.; Mattei, M.G.; Ninomiya, Y. !$#journal J. Biol. Chem. (1992) 267:23753-23758 !$#title Isolation and sequencing of cDNAs and genomic DNAs encoding !1the alpha4 chain of basement membrane collagen type IV and !1assignment of the gene to the distal long arm of human !1chromosome 2. !$#cross-references MUID:93054733; PMID:1429714 !$#accession S28777 !'##molecule_type DNA !'##residues 1407-1424,'G',1426-1430,'A',1432-1439,'L',1441-1507 ##label !1KAM !'##cross-references GB:L01475; GB:L01476 !'##note the codons given for 1438-Asp (GAG) and 1443-Gly (GCA) are !1inconsistent with the authors' translation COMMENT Prolines and lysines at the third position of the tripeptide !1repeating unit (G-X-Y) are hydroxylated to varying extents. !1Prolines are predominately 4-hydroxylated. Lysines are !15-hydroxylated and subsequently O-glycosylated. GENETICS !$#gene GDB:COL4A4 !'##cross-references GDB:132673; OMIM:120131 !$#map_position 2q35-2q37 !$#introns 39/1; 1406/1; 1445/1; 1508/1; 1603/3 #status incomplete !$#note the alpha 3(IV) and alpha 4(IV) chain genes are encoded on !1opposite strands with overlapping promotor regions COMPLEX this minor type IV collagen is thought to form a !1heterotrimer of two alpha 3(IV) chains (see PIR:CGHU3B) and !1one alpha 4(IV) chain. A polymeric network forms with !1tetrameric associations among trimer amino-terminal domains !1(with disulfide and desmosine cross-links), dimeric !1associations among trimer carboxyl-terminal domains (with !1disulfide bonds), and both intra-trimer and inter-trimer !1associations in the interrupted helical domain (with !1disulfide and desmosine cross-links). FUNCTION !$#description minor structural component of extracellular basement !1membrane in kidney glomeruli, lung aveoli, synaptic muscle !1fibers, lens capsule, cochlea, and brain CLASSIFICATION #superfamily collagen alpha 1(IV) chain KEYWORDS basement membrane; coiled coil; extracellular matrix; !1glycoprotein; hydroxylysine; hydroxyproline; trimer; triple !1helix FEATURE !$1-38 #domain signal sequence #status predicted #label SIG\ !$39-1690 #product collagen alpha 4(IV) chain #status predicted !8#label MAT\ !$39-61 #domain amino-terminal nonhelical, NH1 #label NH1\ !$62-1466 #region interrupted helical\ !$94-96 #region cell attachment (R-G-D) motif\ !$145-147 #region cell attachment (R-G-D) motif\ !$189-191 #region cell attachment (R-G-D) motif\ !$310-312 #region cell attachment (R-G-D) motif\ !$724-726 #region cell attachment (R-G-D) motif\ !$785-787 #region cell attachment (R-G-D) motif\ !$989-991 #region cell attachment (R-G-D) motif\ !$1212-1214 #region cell attachment (R-G-D) motif\ !$1467-1690 #domain carboxyl-terminal nonhelical, NC1 #label NC1\ !$1471-1569 #domain collagen IV carboxyl-terminal repeat #label !8CT1\ !$1579-1686 #domain collagen IV carboxyl-terminal repeat #label !8CT2\ !$47,52,55,57,266, !$400,460,492,494, !$668,790,828,1095, !$1131,1294,1317, !$1375,1407 #disulfide_bonds interchain #status predicted\ !$142,669 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$1480-1566,1513-1569 #disulfide_bonds (or 1480-1569, 1513-1566) #status !8predicted\ !$1525-1531,1634-1641 #disulfide_bonds #status predicted\ !$1588-1683,1622-1686 #disulfide_bonds (or 1588-1686, 1622-1683) #status !8predicted SUMMARY #length 1690 #molecular-weight 164095 #checksum 1578 SEQUENCE /// ENTRY CGHU6B #type complete TITLE collagen alpha 6(IV) chain precursor - human ALTERNATE_NAMES procollagen alpha 6(IV) chain ORGANISM #formal_name Homo sapiens #common_name man DATE 07-Jul-1995 #sequence_revision 03-Oct-1995 #text_change 16-Jun-2000 ACCESSIONS A54122; A53404; B57079 REFERENCE A54122 !$#authors Zhou, J.; Ding, M.; Zhao, Z.; Reeders, S.T. !$#journal J. Biol. Chem. (1994) 269:13193-13199 !$#title Complete primary structure of the sixth chain of human !1basement membrane collagen, alpha6(IV). Isolation of the !1cDNAs for alpha6(IV) and comparison with five other type IV !1collagen chains. !$#cross-references MUID:94230418; PMID:8175748 !$#accession A54122 !'##molecule_type mRNA !'##residues 1-1691 ##label ZHO !'##cross-references GB:U04845; NID:g496977; PIDN:AAA19569.1; !1PID:g496978 REFERENCE A53404 !$#authors Oohashi, T.; Sugimoto, M.; Mattei, M.G.; Ninomiya, Y. !$#journal J. Biol. Chem. (1994) 269:7520-7526 !$#title Identification of a new collagen IV chain, alpha6(IV), by !1cDNA isolation and assignment of the gene to chromosome !1Xq22, which is the same locus for COL4A5. !$#cross-references MUID:94171779; PMID:8125972 !$#accession A53404 !'##molecule_type mRNA !'##residues 'MHPG',6-169,'M',171-916,'S',918-1301,1314-1355,'A', !11357-1691 ##label OOH !'##cross-references DDBJ:D21337; NID:g466537; PIDN:BAA04809.1; !1PID:g466538 REFERENCE A57079 !$#authors Zhou, J.; Mochizuki, T.; Smeets, H.; Antignac, C.; Laurila, !1P.; de Paepe, A.; Tryggvason, K.; Reeders, S.T. !$#journal Science (1993) 261:1167-1169 !$#title Deletion of the paired alpha5(IV) and alpha6(IV) collagen !1genes in inherited smooth muscle tumors. !$#cross-references MUID:93361972; PMID:8356449 !$#accession B57079 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-546,'G' ##label ZH2 !'##cross-references GB:L22763 COMMENT Prolines and lysines at the third position of the tripeptide !1repeating unit (G-X-Y) are hydroxylated to varying extents. !1Prolines are predominately 4-hydroxylated. Lysines are !15-hydroxylated and subsequently O-glycosylated. GENETICS !$#gene GDB:COL4A6 !'##cross-references GDB:222775; OMIM:303631 !$#map_position Xq22-Xq22 !$#note the alpha 5(IV) and alpha 6(IV) chain genes are encoded on !1opposite strands with overlapping promotor regions; defects !1in this gene can result in Alport's syndrome COMPLEX this minor type IV collagen is thought to form a !1heterotrimer of two alpha 5(IV) chains (see PIR:S22917) and !1one alpha 6(IV) chain. A polymeric network forms with !1tetrameric associations among trimer amino-terminal domains !1(with disulfide and desmosine cross-links), dimeric !1associations among trimer carboxyl-terminal domains (with !1disulfide bonds), and both intra-trimer and inter-trimer !1associations in the interrupted helical domain (with !1disulfide and desmosine cross-links). FUNCTION !$#description minor structural component of extracellular basement !1membrane CLASSIFICATION #superfamily collagen alpha 1(IV) chain KEYWORDS Alport syndrome; basement membrane; coiled coil; !1extracellular matrix; glycoprotein; hydroxylysine; !1hydroxyproline; trimer; triple helix FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-1691 #product collagen alpha 6(IV) chain #status predicted !8#label MAT\ !$22-46 #domain amino-terminal nonhelical, NC2 #label NC2\ !$47-1463 #region interrupted helical\ !$1464-1691 #domain carboxyl-terminal nonhelical, NC1 #label NC1\ !$1473-1571 #domain collagen IV carboxyl-terminal repeat #label !8CT1\ !$1581-1687 #domain collagen IV carboxyl-terminal repeat #label !8CT2\ !$31,36,40,42,126, !$482,484,657 #disulfide_bonds interchain #status predicted\ !$127 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$1482-1568,1515-1571 #disulfide_bonds (or 1482-1571, 1515-1568) #status !8predicted\ !$1527-1533,1636-1643 #disulfide_bonds #status predicted\ !$1590-1684,1624-1687 #disulfide_bonds (or 1590-1687, 1624-1684) #status !8predicted SUMMARY #length 1691 #molecular-weight 163788 #checksum 3726 SEQUENCE /// ENTRY CGHU1A #type complete TITLE collagen alpha 1(VI) chain precursor - human ALTERNATE_NAMES procollagen alpha 1(VI) chain ORGANISM #formal_name Homo sapiens #common_name man DATE 07-Sep-1990 #sequence_revision 19-Oct-1995 #text_change 22-Jun-1999 ACCESSIONS S05377; S13603; S43247; S43249; S43245; S26507; A31952; !1A40572; A29848 REFERENCE S05377 !$#authors Chu, M.L.; Pan, T.C.; Conway, D.; Kuo, H.J.; Glanville, !1R.W.; Timpl, R.; Mann, K.; Deutzmann, R. !$#journal EMBO J. (1989) 8:1939-1946 !$#title Sequence analysis of alpha 1(VI) and alpha 2(VI) chains of !1human type VI collagen reveals internal triplication of !1globular domains similar to the A domains of von Willebrand !1factor and two alpha 2(VI) chain variants that differ in the !1carboxy terminus. !$#cross-references MUID:90005396; PMID:2551668 !$#accession S05377 !'##molecule_type mRNA !'##residues 1-256;593-1028 ##label CHU !'##cross-references EMBL:X15879; EMBL:X15880 !'##note parts of this sequence were determined by protein sequencing !'##note 35-Arg was also found; the amino end of the mature protein is !1blocked REFERENCE S13603 !$#authors Mann, K. !$#submission submitted to the Protein Sequence Database, January 1990 !$#accession S13603 !'##status preliminary !'##molecule_type mRNA !'##residues 1-380,'RP',383-1028 ##label MAN REFERENCE S43245 !$#authors Tillet, E.; Wiedemann, H.; Golbik, R.; Pan, T.C.; Zhang, !1R.Z.; Mann, K.; Chu, M.L.; Timpl, R. !$#journal Eur. J. Biochem. (1994) 221:177-185 !$#title Recombinant expression and structural and binding properties !1of alpha-1(VI) and alpha-2(VI) chains of human collagen type !1VI. !$#cross-references MUID:94222059; PMID:8168508 !$#accession S43247 !'##molecule_type protein !'##residues 69-74 ##label TIL !'##experimental_source human embryonic kidney 293 cells with plasmid !1pSV(2)pac !$#accession S43249 !'##molecule_type protein !'##residues 260-267,'I',269-271 ##label TI2 !'##experimental_source human embryonic kidney 293 cells with plasmid !1pSV(2)pac !$#accession S43245 !'##molecule_type protein !'##residues 581-593,'X',595-597 ##label TI3 !'##experimental_source human embryonic kidney 293 cells with plasmid !1pSV(2)pac REFERENCE S26506 !$#authors Jander, R.; Rautenberg, J.; Glanville, R.W. !$#journal Eur. J. Biochem. (1983) 133:39-46 !$#title Further characterization of the three polypeptide chains of !1bovine and human short-chain collagen (intima collagen). !$#cross-references MUID:83209648; PMID:6852033 !$#accession S26507 !'##molecule_type protein !'##residues 246,'XXR',250-251,'G',253-254,'GL',257-258 ##label JAN !'##note 255-Ala was also found REFERENCE A31952 !$#authors Chu, M.L.; Conway, D.; Pan, T.; Baldwin, C.; Mann, K.; !1Deutzmann, R.; Timpl, R. !$#journal J. Biol. Chem. (1988) 263:18601-18606 !$#title Amino acid sequence of the triple-helical domain of human !1collagen type VI. !$#cross-references MUID:89066644; PMID:3198591 !$#accession A31952 !'##molecule_type mRNA !'##residues 257-380,'R',382-592 ##label CH1 !'##cross-references GB:M20776; GB:J04211 !'##note parts of this sequence were determined by protein sequencing !'##note 321-Gln and 322-Glu were found in the peptide sequences REFERENCE A40572 !$#authors Saitta, B.; Wang, Y.M.; Renkart, L.; Zhang, R.Z.; Pan, T.C.; !1Timpl, R.; Chu, M.L. !$#journal Genomics (1991) 11:145-153 !$#title The exon organization of the triple-helical coding regions !1of the human alpha1(VI) and alpha2(VI) collagen genes is !1highly similar. !$#cross-references MUID:92112205; PMID:1765372 !$#accession A40572 !'##molecule_type DNA !'##residues 287-437,'T',439-592 ##label SAI !'##cross-references GB:S75420 !'##note the authors translated the codon GAG for residue 381 as Arg REFERENCE A29848 !$#authors Weil, D.; Mattei, M.G.; Passage, E.; Van Cong, N.; !1Pribula-Conway, D.; Mann, K.; Deutzmann, R.; Timpl, R.; Chu, !1M.L. !$#journal Am. J. Hum. Genet. (1988) 42:435-445 !$#title Cloning and chromosomal localization of human genes encoding !1the three chains of type VI collagen. !$#cross-references MUID:88161046; PMID:3348212 !$#accession A29848 !'##molecule_type mRNA !'##residues 422-437,'T',439-481 ##label WEI !'##cross-references GB:M27447; NID:g291915; PIDN:AAA52055.1; !1PID:g291916 !'##note part of this sequence was determined by protein sequencing COMMENT Prolines and lysines at the third position of the tripeptide !1repeating unit (G-X-Y) are hydroxylated to varying extents. !1Almost all the prolines are predominately 4-hydroxylated. !190% of the lysines are 5-hydroxylated and subsequently !1O-glycosylated. GENETICS !$#gene GDB:COL6A1 !'##cross-references GDB:119065; OMIM:120220 !$#map_position 21q22.3-21q22.3 !$#introns 286/3; 301/3; 310/3; 319/3; 334/3; 352/3; 373/3; 394/3; 412/ !13; 424/3; 445/3; 466/3; 487/3; 508/3; 525/3; 537/3; 558/3; !1580/3 #status incomplete COMPLEX type VI collagen is a heterotrimer of one alpha 1(VI) chain, !1one alpha 2(VI) chain (see PIR:CGHU2A) and one alpha 3(VI) !1chain (see PIR:CGHU3A). A polymeric network forms with !1tetrameric associations among trimer amino- and !1carboxyl-terminal domains (with disulfide bonds). FUNCTION !$#description structural component of extracellular tissue microfibrils !1associated with cell surfaces, soft connective tissue and !1cartilage CLASSIFICATION #superfamily collagen alpha 1(VI) chain; von Willebrand !1factor type A repeat homology KEYWORDS blocked amino end; cell binding; coiled coil; extracellular !1matrix; glycoprotein; hydroxylysine; hydroxyproline; !1pyroglutamic acid; trimer; triple helix FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-1028 #product collagen alpha 1(VI) chain #status predicted !8#label MAT\ !$20-256 #domain amino-terminal nonhelical #status predicted !8#label NH1\ !$35-213 #domain von Willebrand factor type A repeat homology !8#label VWA1\ !$257-592 #region interrupted helical\ !$262-264 #region cell attachment (R-G-D) motif\ !$442-444 #region cell attachment (R-G-D) motif\ !$478-480 #region cell attachment (R-G-D) motif\ !$593-1028 #domain carboxyl-terminal nonhelical #status !8predicted #label NH2\ !$613-793 #domain von Willebrand factor type A repeat homology !8#label VWA2\ !$827-998 #domain von Willebrand factor type A repeat homology !8#label VWA3\ !$20 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status predicted\ !$212,537,804,896 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$259,265,274,286, !$289,340,343,358, !$445,463,466,493, !$499,502,522,525, !$528,583,589 #modified_site 4-hydroxyproline (Pro) #status !8experimental\ !$280,301,304,316, !$319,334,346,361, !$370,373,475,568,571 #binding_site carbohydrate (Lys) (covalent) #status !8experimental\ !$280,301,304,316, !$319,334,346,361, !$370,373,475,568,571 #modified_site 5-hydroxylysine (Lys) #status !8experimental\ !$345 #disulfide_bonds interchain #status predicted\ !$516 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 1028 #molecular-weight 108639 #checksum 1408 SEQUENCE /// ENTRY A32856 #type complete TITLE collagen alpha 1(VI) chain precursor - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A32856; I50587; I50627; I50586 REFERENCE A32856 !$#authors Bonaldo, P.; Russo, V.; Bucciotti, F.; Bressan, G.M.; !1Colombatti, A. !$#journal J. Biol. Chem. (1989) 264:5575-5580 !$#title Alpha-1 chain of chick type VI collagen. The complete cDNA !1sequence reveals a hybrid molecule made of one short !1collagen and three Von Willebrand factor type A-like !1domains. !$#cross-references MUID:89174602; PMID:2784434 !$#accession A32856 !'##molecule_type mRNA !'##residues 1-1019 ##label BON !'##cross-references GB:J04598; NID:g576463; PIDN:AAB59954.1; !1PID:g211354 !'##note 479-Asn and 620-Asn was also found REFERENCE I50587 !$#authors Walchli, C.; Koller, E.; Trueb, J.; Trueb, B. !$#journal Eur. J. Biochem. (1992) 205:583-589 !$#title Structural comparison of the chicken genes for alpha 1(VI) !1and alpha 2(VI) collagen. !$#cross-references MUID:92241293; PMID:1572359 !$#accession I50587 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-1019 ##label WAL !'##cross-references EMBL:X57998; NID:g62874; PIDN:CAA41062.1; !1PID:g62875 !$#accession I50627 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-1019 ##label WA2 !'##cross-references EMBL:X64458; NID:g63301; PIDN:CAA45788.1; !1PID:g63302 REFERENCE I50586 !$#authors Koller, E.; Trueb, B. !$#journal Eur. J. Biochem. (1992) 208:769-774 !$#title Characterization of the chicken alpha 1(VI) collagen !1promoter. !$#cross-references MUID:93011107; PMID:1396681 !$#accession I50586 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-75 ##label KOL !'##cross-references EMBL:X57987; NID:g62872; PIDN:CAA41053.1; !1PID:g62873 GENETICS !$#gene Col6A1 !$#introns 33/1; 76/2; 143/2; 196/3; 237/3; 244/3; 251/3; 266/3; 284/3; !1299/3; 308/3; 317/3; 332/3; 350/3; 371/3; 392/3; 422/3; 443/ !13; 464/3; 485/3; 506/3; 523/3; 535/3; 556/3; 578/3; 590/3; !1603/1; 606/1; 650/3; 687/2; 748/3; 807/1; 817/1 CLASSIFICATION #superfamily collagen alpha 1(VI) chain; von Willebrand !1factor type A repeat homology KEYWORDS cell binding; coiled coil; disulfide bond; extracellular !1matrix; glycoprotein; heterotrimer; hydroxylysine; !1hydroxyproline; triple helix FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-1019 #product collagen alpha 1(VI) chain #status predicted !8#label MAT\ !$35-213 #domain von Willebrand factor type A repeat homology !8#label VWA1\ !$255-590 #domain collagenous #status predicted #label COL\ !$440-442 #region cell attachment (R-G-D) motif\ !$476-478 #region cell attachment (R-G-D) motif\ !$529-531 #region cell attachment (R-G-D) motif\ !$611-788 #domain von Willebrand factor type A repeat homology !8#label VWA2\ !$822-989 #domain von Willebrand factor type A repeat homology !8#label VWA3\ !$212,514,535,666, !$799,887 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1019 #molecular-weight 107983 #checksum 7826 SEQUENCE /// ENTRY CGHU2A #type complete TITLE collagen alpha 2(VI) chain precursor, long splice form - human ALTERNATE_NAMES collagen alpha 2C2(VI) chain; procollagen alpha 2(VI) chain ORGANISM #formal_name Homo sapiens #common_name man DATE 03-Apr-1992 #sequence_revision 24-Apr-1998 #text_change 22-Jun-1999 ACCESSIONS S05378; S26505; S13604; S20817; S43248; S43246; B40572; !1S26509; B31952; B29848; A35243 REFERENCE S05377 !$#authors Chu, M.L.; Pan, T.C.; Conway, D.; Kuo, H.J.; Glanville, !1R.W.; Timpl, R.; Mann, K.; Deutzmann, R. !$#journal EMBO J. (1989) 8:1939-1946 !$#title Sequence analysis of alpha 1(VI) and alpha 2(VI) chains of !1human type VI collagen reveals internal triplication of !1globular domains similar to the A domains of von Willebrand !1factor and two alpha 2(VI) chain variants that differ in the !1carboxy terminus. !$#cross-references MUID:90005396; PMID:2551668 !$#accession S05378 !'##molecule_type mRNA !'##residues 1-1018 ##label CHU1 !'##cross-references EMBL:X15881 !'##note the nucleotide sequence for residues 255-589 is not given !$#accession S26505 !'##molecule_type protein !'##residues 121-135,'X',137-150;197-216;232-254;590-605,'L',607-618, !1'F',620-627,'LX', !1630-631;635-649;653-674;692-706;708-715;796-820;'Q',967-975 !1##label CHU2 REFERENCE S13603 !$#authors Mann, K. !$#submission submitted to the Protein Sequence Database, January 1990 !$#accession S13604 !'##status preliminary !'##molecule_type mRNA !'##residues 1-1018 ##label MAN !'##note this sequence was revised in reference A40572 REFERENCE S20817 !$#authors Saitta, B.; Timpl, R.; Chu, M.L. !$#journal J. Biol. Chem. (1992) 267:6188-6196 !$#title Human alpha-2(VI) collagen gene. Heterogeneity at the !15'-untranslated region generated by an alternate exon. !$#cross-references MUID:92210594; PMID:1556127 !$#accession S20817 !'##molecule_type DNA !'##residues 1-94,'A',96-266 ##label SAI !'##cross-references GB:M81835 REFERENCE S43245 !$#authors Tillet, E.; Wiedemann, H.; Golbik, R.; Pan, T.C.; Zhang, !1R.Z.; Mann, K.; Chu, M.L.; Timpl, R. !$#journal Eur. J. Biochem. (1994) 221:177-185 !$#title Recombinant expression and structural and binding properties !1of alpha-1(VI) and alpha-2(VI) chains of human collagen type !1VI. !$#cross-references MUID:94222059; PMID:8168508 !$#accession S43248 !'##molecule_type protein !'##residues 179-185 ##label TIL !$#accession S43246 !'##molecule_type protein !'##residues 581-590,'X',592-594 ##label TI2 REFERENCE A40572 !$#authors Saitta, B.; Wang, Y.M.; Renkart, L.; Zhang, R.Z.; Pan, T.C.; !1Timpl, R.; Chu, M.L. !$#journal Genomics (1991) 11:145-153 !$#title The exon organization of the triple-helical coding regions !1of the human alpha1(VI) and alpha2(VI) collagen genes is !1highly similar. !$#cross-references MUID:92112205; PMID:1765372 !$#accession B40572 !'##molecule_type DNA !'##residues 245-369,'GK',372,'D',374-375,'RP',378-420,'E',422-426,'DP', !1429-486,'SR',489-569,'P',571-589 ##label SA2 !'##cross-references GB:S75462; NID:g242004; PIDN:AAB20836.1; !1PID:g242005 REFERENCE S26506 !$#authors Jander, R.; Rautenberg, J.; Glanville, R.W. !$#journal Eur. J. Biochem. (1983) 133:39-46 !$#title Further characterization of the three polypeptide chains of !1bovine and human short-chain collagen (intima collagen). !$#cross-references MUID:83209648; PMID:6852033 !$#accession S26509 !'##molecule_type protein !'##residues 251-256,'R',258-259,'X',261-262,'X',264 ##label JAN REFERENCE A31952 !$#authors Chu, M.L.; Conway, D.; Pan, T.; Baldwin, C.; Mann, K.; !1Deutzmann, R.; Timpl, R. !$#journal J. Biol. Chem. (1988) 263:18601-18606 !$#title Amino acid sequence of the triple-helical domain of human !1collagen type VI. !$#cross-references MUID:89066644; PMID:3198591 !$#accession B31952 !'##molecule_type mRNA !'##residues 255-589 ##label CH2 !'##cross-references GB:M20777; GB:J04211 REFERENCE A29848 !$#authors Weil, D.; Mattei, M.G.; Passage, E.; Van Cong, N.; !1Pribula-Conway, D.; Mann, K.; Deutzmann, R.; Timpl, R.; Chu, !1M.L. !$#journal Am. J. Hum. Genet. (1988) 42:435-445 !$#title Cloning and chromosomal localization of human genes encoding !1the three chains of type VI collagen. !$#cross-references MUID:88161046; PMID:3348212 !$#accession B29848 !'##molecule_type mRNA !'##residues 315-358 ##label WEI !'##cross-references GB:M27448; NID:g291917; PIDN:AAA52056.1; !1PID:g291918 !'##note part of this sequence was determined by protein sequencing REFERENCE A35243 !$#authors Saitta, B.; Stokes, D.G.; Vissing, H.; Timpl, R.; Chu, M.L. !$#journal J. Biol. Chem. (1990) 265:6473-6480 !$#title Alternative splicing of the human alpha2(VI) collagen gene !1generates multiple mRNA transcripts which predict three !1protein variants with distinct carboxyl termini. !$#cross-references MUID:90202932; PMID:1690728 !$#accession A35243 !'##molecule_type DNA; mRNA !'##residues 590-1018 ##label SA3 !'##cross-references GB:M34571; GB:M34573; NID:g179707; PIDN:AAA35620.1; !1PID:g179711 COMMENT Prolines and lysines at the third position of the tripeptide !1repeating unit (G-X-Y) are hydroxylated to varying extents. !160% of the prolines are predominately 4-hydroxylated. 55% of !1the lysines are 5-hydroxylated and subsequently !1O-glycosylated. GENETICS !$#gene GDB:COL6A2 !'##cross-references GDB:119793; OMIM:120240 !$#map_position 21q22.3-21q22.3 !$#introns 39/1; 237/3; 244/3; 266/3; 284/3; 299/3; 308/3; 317/3; 332/ !13; 350/3; 371/3; 392/3; 422/3; 443/3; 464/3; 485/3; 506/3; !1523/3; 535/3; 556/3; 577/3; 589/3; 605/1; 656/1; 807/1; 820/ !11 !$#note the first intron occurs before the initiator codon COMPLEX type VI collagen is a heterotrimer of one alpha 1(VI) chain !1(see PIR:CGHU1A), one alpha 2(VI) chain and one alpha 3(VI) !1chain (see PIR:CGHU3A). A polymeric network forms with !1tetrameric associations among trimer amino- and !1carboxyl-terminal domains (with disulfide bonds). FUNCTION !$#description structural component of extracellular tissue microfibrils !1associated with cell surfaces, soft connective tissue and !1cartilage CLASSIFICATION #superfamily collagen alpha 1(VI) chain; von Willebrand !1factor type A repeat homology KEYWORDS alternative splicing; blocked amino end; cell binding; !1coiled coil; extracellular matrix; glycoprotein; !1hydroxylysine; hydroxyproline; pyroglutamic acid; trimer; !1triple helix FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-1018 #product collagen alpha 2(VI) chain, long splice form !8#status predicted #label MAW\ !$21-254 #domain amino-terminal nonhelical #status predicted !8#label NH1\ !$44-215 #domain von Willebrand factor type A repeat homology !8#label VWA1\ !$255-589 #region interrupted helical\ !$365-367 #region cell attachment (R-G-D) motif\ !$425-427 #region cell attachment (R-G-D) motif\ !$497-499 #region cell attachment (R-G-D) motif\ !$590-1018 #domain carboxyl-terminal nonhelical #status !8predicted #label NH2\ !$612-788 #domain von Willebrand factor type A repeat homology !8#label VWA2\ !$830-1001 #domain von Willebrand factor type A repeat homology !8#label VWA3\ !$21 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status predicted\ !$140,629 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$260,266,269,299, !$305,308,344,389, !$392,407,410,461, !$464,526,544,550,553 #binding_site carbohydrate (Lys) (covalent) #status !8experimental\ !$260,266,269,299, !$305,308,344,389, !$392,407,410,461, !$464,526,544,550,553 #modified_site 5-hydroxylysine (Lys) #status !8experimental\ !$287,296,302,341, !$356,362,383,401, !$404,503,523,559, !$562,565,574,580, !$583,586 #modified_site 4-hydroxyproline (Pro) #status !8experimental\ !$326,784,896,953 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$343 #disulfide_bonds interchain #status predicted SUMMARY #length 1018 #molecular-weight 108335 #checksum 6539 SEQUENCE /// ENTRY S21369 #type complete TITLE collagen alpha 2(VI) chain precursor - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S21369; S28808; S13745; S18863 REFERENCE S21369 !$#authors Ibrahimi, X.Y.Z.; Bardon, X.Y.Z.; Dani, C. !$#submission submitted to the EMBL Data Library, April 1992 !$#accession S21369 !'##molecule_type mRNA !'##residues 1-1029 ##label IBR !'##cross-references EMBL:X65582; NID:g49808; PIDN:CAA46541.1; !1PID:g49809 REFERENCE S28808 !$#authors Ibrahimi, A.; Bertrand, B.; Bardon, S.; Amri, E.Z.; !1Grimaldi, P.; Ailhaud, G.; Dani, C. !$#journal Biochem. J. (1993) 289:141-147 !$#title Cloning of alpha2 chain of type VI collagen and expression !1during mouse development. !$#cross-references MUID:93143659; PMID:8380980 !$#accession S28808 !'##molecule_type mRNA !'##residues 266-1029 ##label IB2 !'##cross-references EMBL:X62332; NID:g49906; PIDN:CAA44206.1; !1PID:g49907 REFERENCE S13745 !$#authors Constantinou, C.D.; Jimenez, S.A. !$#journal Matrix (1991) 11:1-9 !$#title Structure of cDNAs encoding the triple-helical domain of !1murine alpha-2(VI) collagen chain and comparison to human !1and chick homologues. Use of polymerase chain reaction and !1partially degenerate oligonucleotides for generation of !1novel cDNA clones. !$#cross-references MUID:91226374; PMID:1709252 !$#accession S13745 !'##molecule_type mRNA !'##residues 266-267,'S',269-294,'L',296-600 ##label CON !'##cross-references GB:L06343; NID:g192671; PIDN:AAA37441.1; !1PID:g192672 !'##note the sequence from Fig. 3 is inconsistent with that from Fig. 4 !1in having 306-Ile CLASSIFICATION #superfamily collagen alpha 1(VI) chain; von Willebrand !1factor type A repeat homology KEYWORDS alternative splicing; cartilage; cell binding; connective !1tissue; disulfide bond; extracellular matrix; glycoprotein; !1heterotrimer FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-1029 #product collagen alpha 2(VI) chain #status predicted !8#label MAT\ !$29-265 #domain globular #status predicted #label NC2\ !$54-226 #domain von Willebrand factor type A repeat homology !8#label VWA1\ !$266-600 #domain collagenous #status predicted #label COL\ !$376-378 #region cell attachment (R-G-D) motif\ !$436-438 #region cell attachment (R-G-D) motif\ !$499-501 #region cell attachment (R-G-D) motif\ !$508-510 #region cell attachment (R-G-D) motif\ !$549-551 #region cell attachment (R-G-D) motif\ !$601-1029 #domain globular #status predicted #label NC1\ !$623-799 #domain von Willebrand factor type A repeat homology !8#label VWA2\ !$841-1012 #domain von Willebrand factor type A repeat homology !8#label VWA3\ !$150,337,640,907,963 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1029 #molecular-weight 109811 #checksum 3512 SEQUENCE /// ENTRY CGHU3A #type complete TITLE collagen alpha 3(VI) chain precursor [validated] - human CONTAINS collagen alpha 3(VI) chain, splice form A9/N10(-) ORGANISM #formal_name Homo sapiens #common_name man DATE 21-Nov-1993 #sequence_revision 12-Nov-1999 #text_change 15-Sep-2000 ACCESSIONS A59140; S13679; S24465; A57083; S28776; S00245; C31952; !1C29848; S26510; S48709 REFERENCE A59140 !$#authors Chu, M.L. !$#submission submitted to GenBank, May 1998 !$#accession A59140 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-3176 ##label CHU !'##cross-references GB:X52022; NID:g3127925; PIDN:CAA36267.1; !1PID:g3127926 REFERENCE S13679 !$#authors Chu, M.L.; Zhang, R.Z.; Pan, T.; Stokes, D.; Conway, D.; !1Kuo, H.J.; Glanville, R.; Mayer, U.; Mann, K.; Deutzmann, !1R.; Timpl, R. !$#journal EMBO J. (1990) 9:385-393 !$#title Mosaic structure of globular domains in the human type VI !1collagen alpha-3 chain: similarity to von Willebrand factor, !1fibronectin, actin, salivary proteins and aprotinin type !1protease inhibitors. !$#cross-references MUID:90151612; PMID:1689238 !$#accession S13679 !'##molecule_type mRNA !'##residues 1-30,237-313,'CWW',318-322,'AR',326-1815,'FD',1818-1819, !1'ID',1822-3176 ##label CH5 !'##cross-references EMBL:X52022; NID:g3127925 !$#accession S24465 !'##molecule_type protein !'##residues 574-585;965-973,'X', !1975-976;1306-1325;1361-1377;1381-1401;1473-1506,'X', !11508-1517;1720-1724,'X',1726-1741,'X',1743-1744;1789-1799, !1'X',1801;1834-1853;1857-1872,'X', !11874-1878;1914-1924;1947-1962,'X', !11964-1965;2018-2037;2374-2410;2445-2459;2466-2469,'X', !12471-2474;2504-2508,'X',2510-2527;2533-2545;2555-2601 !1##label CH2 REFERENCE S28776 !$#authors Zanussi, S.; Doliana, R.; Segat, D.; Bonaldo, P.; !1Colombatti, A. !$#journal J. Biol. Chem. (1992) 267:24082-24089 !$#title The human type VI collagen gene. mRNA and protein variants !1of the alpha3 chain generated by alternative splicing of an !1additional 5-end exon. !$#cross-references MUID:93054780; PMID:1339440 !$#accession A57083 !'##molecule_type DNA !'##residues 310-328 ##label ZAN !$#accession S28776 !'##molecule_type mRNA !'##residues 32-126,'AK',129-136,'L',138-236 ##label ZA2 !'##cross-references GB:S49432; NID:g260296; PIDN:AAB24261.1; !1PID:g260297 REFERENCE S00126 !$#authors Chu, M.L.; Mann, K.; Deutzmann, R.; Pribula-Conway, D.; !1Hsu-Chen, C.C.; Bernard, M.P.; Timpl, R. !$#journal Eur. J. Biochem. (1987) 168:309-317 !$#title Characterization of three constituent chains of collagen !1type VI by peptide sequences and cDNA clones. !$#cross-references MUID:88029444; PMID:3665927 !$#accession S00245 !'##molecule_type mRNA; protein !'##residues 2024-2046;2092-2156,'R';2203-2208,'X',2210-2211,'X', !12213-2227;2228-2251;2314-2321,'X',2323-2330,'X',2332-2336, !1'X',2338-2340;2385-2402 ##label CH3 !'##cross-references GB:X06196; NID:g30055; PIDN:CAA29557.1; !1PID:g1335034 !'##note the mRNA portion of the sequence corresponds to residues !12092-2157 REFERENCE A31952 !$#authors Chu, M.L.; Conway, D.; Pan, T.; Baldwin, C.; Mann, K.; !1Deutzmann, R.; Timpl, R. !$#journal J. Biol. Chem. (1988) 263:18601-18606 !$#title Amino acid sequence of the triple-helical domain of human !1collagen type VI. !$#cross-references MUID:89066644; PMID:3198591 !$#accession C31952 !'##molecule_type mRNA !'##residues 2038-2373 ##label CH4 !'##cross-references GB:J04211; GB:M20778 !'##note parts of this sequence were determined by protein sequencing REFERENCE A29848 !$#authors Weil, D.; Mattei, M.G.; Passage, E.; Van Cong, N.; !1Pribula-Conway, D.; Mann, K.; Deutzmann, R.; Timpl, R.; Chu, !1M.L. !$#journal Am. J. Hum. Genet. (1988) 42:435-445 !$#title Cloning and chromosomal localization of human genes encoding !1the three chains of type VI collagen. !$#cross-references MUID:88161046; PMID:3348212 !$#accession C29848 !'##molecule_type mRNA !'##residues 2092-2151 ##label WEI !'##cross-references GB:M27449; NID:g291919; PIDN:AAA52057.1; !1PID:g291920 !'##note part of this sequence was determined by protein sequencing REFERENCE S26506 !$#authors Jander, R.; Rautenberg, J.; Glanville, R.W. !$#journal Eur. J. Biochem. (1983) 133:39-46 !$#title Further characterization of the three polypeptide chains of !1bovine and human short-chain collagen (intima collagen). !$#cross-references MUID:83209648; PMID:6852033 !$#accession S26510 !'##molecule_type protein !'##residues 'SAIAGVAGVG' ##label JAN !'##note this sequence cannot be reliably placed and probably represents !1the results from an unresolved mixture of peptides REFERENCE S48709 !$#authors Mayer, U.; Poeschl, E.; Nischt, R.; Specks, U.; Pan, T.C.; !1Chu, M.L.; Timpl, R. !$#journal Eur. J. Biochem. (1994) 225:573-580 !$#title Recombinant expression and properties of the Kunitz-type !1protease-inhibitor module from human type VI collagen !1alpha-3(VI) chain. !$#cross-references MUID:95045506; PMID:7525281 !$#accession S48709 !'##molecule_type mRNA !'##residues 'MRAWIFFLLCLAGRALAA',3102-3176 ##label MAY !'##note engineered sequence to allow isolation of the Kunitz-type !1proteinase inhibitor homology domain; the amino-terminal !1section is a model signal peptide from osteonectin (see !1GEHUN) REFERENCE A52812 !$#authors Arnoux, B.; Merigeau, K.; Saludjian, P.; Norris, F.; Norris, !1K.; Bjorn, S.; Olsen, O.; Petersen, L.; Ducruix, A. !$#submission submitted to the Brookhaven Protein Data Bank, August 1994 !$#cross-references PDB:1KNT !$#contents annotation; X-ray crystallography, 1.6 angstroms, residues !13106-3160 !$#note engineered sequence expressed in Saccharomyces cerevisiae !1strain mt-663 COMMENT Prolines and lysines at the third position of the tripeptide !1repeating unit (G-X-Y) are hydroxylated to varying extents. !160% of the prolines are predominately 4-hydroxylated. 55% of !1the lysines are 5-hydroxylated and subsequently !1O-glycosylated. COMMENT The fibronectin type III repeat homology domain may be !1released during processing. GENETICS !$#gene GDB:COL6A3 !'##cross-references GDB:119066; OMIM:120250 !$#map_position 2q37.3-2q37.3 COMPLEX type VI collagen is a heterotrimer of one alpha 1(VI) chain !1(see PIR:CGHU1A), one alpha 2(VI) (see PIR:CGHU2A) chain and !1one alpha 3(VI) chain. A polymeric network forms with !1tetrameric associations among trimer amino- and !1carboxyl-terminal domains (with disulfide bonds). FUNCTION !$#description structural component of extracellular tissue microfibrils !1associated with cell surfaces, soft connective tissue and !1cartilage CLASSIFICATION #superfamily collagen alpha 3(VI) chain; animal Kunitz-type !1proteinase inhibitor homology; fibronectin type III repeat !1homology; von Willebrand factor type A repeat homology KEYWORDS alternative splicing; blocked amino end; cell binding; !1coiled coil; extracellular matrix; glycoprotein; !1hydroxylysine; hydroxyproline; pyroglutamic acid; trimer; !1triple helix FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-3176 #product collagen alpha 3(VI) chain #status predicted !8#label MAT1\ !$26-2037 #domain amino-terminal nonhelical #status predicted !8#label ANH\ !$26-30,237-3176 #product collagen alpha 3(VI) chain, splice form A9/ !8N10(-) #status predicted #label MAT2\ !$37-203 #domain von Willebrand factor type A repeat homology !8#label VW01\ !$240-405 #domain von Willebrand factor type A repeat homology !8#label VW02\ !$443-608 #domain von Willebrand factor type A repeat homology !8#label VW03\ !$637-802 #domain von Willebrand factor type A repeat homology !8#label VW04\ !$835-999 #domain von Willebrand factor type A repeat homology !8#label VW05\ !$1027-1191 #domain von Willebrand factor type A repeat homology !8#label VW06\ !$1231-1394 #domain von Willebrand factor type A repeat homology !8#label VW07\ !$1434-1599 #domain von Willebrand factor type A repeat homology !8#label VW08\ !$1637-1802 #domain von Willebrand factor type A repeat homology !8#label VW09\ !$1836-2005 #domain von Willebrand factor type A repeat homology !8#label VW10\ !$2038-2373 #region interrupted helical\ !$2040-2042 #region cell attachment (R-G-D) motif\ !$2136-2138 #region cell attachment (R-G-D) motif\ !$2148-2150 #region cell attachment (R-G-D) motif\ !$2154-2156 #region cell attachment (R-G-D) motif\ !$2370-2372 #region cell attachment (R-G-D) motif\ !$2374-3176 #domain carboxyl-terminal nonhelical #status !8predicted #label CNH\ !$2400-2571 #domain von Willebrand factor type A repeat homology !8#label VW11\ !$2617-2800 #domain von Willebrand factor type A repeat homology !8#label VW12\ !$2865-2986 #region alanine/lysine/proline/threonine/valine-rich !8repeats\ !$2987-3072 #domain fibronectin type III repeat homology #label !8FN3\ !$3111-3161 #domain animal Kunitz-type proteinase inhibitor !8homology #label BPI\ !$26 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status predicted\ !$108,116,202,251, !$2079,2331,2558, !$2677,2861,3036 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$2087 #disulfide_bonds interchain #status predicted\ !$2100,2206,2239, !$2316,2319 #modified_site 4-hydroxyproline (Pro) #status !8experimental\ !$2103,2209,2212, !$2322,2337 #binding_site carbohydrate (Lys) (covalent) #status !8experimental\ !$2103,2209,2212, !$2322,2337 #modified_site 5-hydroxylysine (Lys) #status !8experimental\ !$3111-3161, !$3120-3144,3136-3157 #disulfide_bonds #status predicted SUMMARY #length 3176 #molecular-weight 343550 #checksum 1088 SEQUENCE /// ENTRY A37797 #type complete TITLE collagen alpha 3(VI) chain precursor - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A37797; A34270; A32674 REFERENCE A37797 !$#authors Doliana, R.; Bonaldo, P.; Colombatti, A. !$#journal J. Cell Biol. (1990) 111:2197-2205 !$#title Multiple forms of chicken alpha3(VI) collagen chain !1generated by alternative splicing in type A repeated !1domains. !$#cross-references MUID:91035630; PMID:1977751 !$#accession A37797 !'##molecule_type mRNA !'##residues 1-253;312-321;434-453;504-518;635-655;704-717;832-853 !1##label DOL !'##cross-references GB:M24282 REFERENCE A34270 !$#authors Bonaldo, P.; Russo, V.; Bucciotti, F.; Doliana, R.; !1Colombatti, A. !$#journal Biochemistry (1990) 29:1245-1254 !$#title Structural and functional features of the alpha3 chain !1indicate a bridging role for chicken collagen VI in !1connective tissues. !$#cross-references MUID:90212613; PMID:2322559 !$#accession A34270 !'##molecule_type mRNA !'##residues 224-2871 ##label BON !'##cross-references GB:M24282 !'##note the authors translated the codon TTC for residue 1916 as Leu !1and TTC for residue 2131 as Ser REFERENCE A32674 !$#authors Bonaldo, P.; Colombatti, A. !$#journal J. Biol. Chem. (1989) 264:20235-20239 !$#title The carboxyl terminus of the chicken alpha3 chain of !1collagen VI is a unique mosaic structure with glycoprotein !1Ib-like, fibronectin type III, and Kunitz modules. !$#cross-references MUID:90062147; PMID:2584214 !$#accession A32674 !'##molecule_type mRNA !'##residues 2151-2199;2792-3137 ##label BO2 !'##cross-references GB:M24282 GENETICS !$#introns 30/1; 236/1; 437/1; 638/1; 838/1 CLASSIFICATION #superfamily collagen alpha 3(VI) chain; animal Kunitz-type !1proteinase inhibitor homology; fibronectin type III repeat !1homology; von Willebrand factor type A repeat homology KEYWORDS alternative splicing; cell binding; coiled coil; connective !1tissue; extracellular matrix; glycoprotein; heterotrimer; !1hydroxylysine; hydroxyproline; triple helix FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-3137 #product collagen alpha 3(VI) chain #status predicted !8#label MAT\ !$26-2042 #domain non-collagenous #status predicted #label NNC\ !$36-202 #domain von Willebrand factor type A repeat homology !8#label VW01\ !$239-404 #domain von Willebrand factor type A repeat homology !8#label VW02\ !$442-607 #domain von Willebrand factor type A repeat homology !8#label VW03\ !$642-807 #domain von Willebrand factor type A repeat homology !8#label VW04\ !$840-1004 #domain von Willebrand factor type A repeat homology !8#label VW05\ !$1033-1197 #domain von Willebrand factor type A repeat homology !8#label VW06\ !$1237-1400 #domain von Willebrand factor type A repeat homology !8#label VW07\ !$1439-1604 #domain von Willebrand factor type A repeat homology !8#label VW08\ !$1639-1804 #domain von Willebrand factor type A repeat homology !8#label VW09\ !$1838-2010 #domain von Willebrand factor type A repeat homology !8#label VW10\ !$2043-2378 #domain collagenous #status predicted #label COL\ !$2045-2047 #region cell attachment (R-G-D) motif\ !$2153-2155 #region cell attachment (R-G-D) motif\ !$2159-2161 #region cell attachment (R-G-D) motif\ !$2379-3137 #domain non-collagenous #status predicted #label CNC\ !$2405-2577 #domain von Willebrand factor type A repeat homology !8#label VW11\ !$2623-2806 #domain von Willebrand factor type A repeat homology !8#label VW12\ !$2803-2846 #domain platelet glycoprotein Ib-like #status !8predicted #label GPI\ !$2954-3039 #domain fibronectin type III repeat homology #label !8FN3\ !$3072-3122 #domain animal Kunitz-type proteinase inhibitor !8homology #label BPI\ !$201,2084,2436,2563, !$2581,2683,2867, !$2920,3003 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 3137 #molecular-weight 339596 #checksum 1757 SEQUENCE /// ENTRY A34246 #type complete TITLE collagen alpha 1(VIII) chain precursor - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A34246 REFERENCE A34246 !$#authors Yamaguchi, N.; Benya, P.D.; van der Rest, M.; Ninomiya, Y. !$#journal J. Biol. Chem. (1989) 264:16022-16029 !$#title The cloning and sequencing of alpha1(VIII) collagen cDNAs !1demonstrate that type VIII collagen is a short chain !1collagen and contains triple-helical and carboxyl-terminal !1non-triple-helical domains similar to those of type X !1collagen. !$#cross-references MUID:89380199; PMID:2476437 !$#accession A34246 !'##molecule_type mRNA !'##residues 1-744 ##label YAM !'##cross-references GB:J05042; NID:g164895; PIDN:AAA31204.1; !1PID:g164896 CLASSIFICATION #superfamily collagen alpha 1(VIII) chain; complement C1q !1carboxyl-terminal homology FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-744 #product collagen alpha 1(VIII) chain #status !8predicted #label MAT\ !$21-117 #region amino-terminal nonhelical\ !$118-571 #region interrupted helical\ !$572-744 #region carboxyl-terminal nonhelical\ !$617-743 #domain complement C1q carboxyl-terminal homology !8#label C1Q SUMMARY #length 744 #molecular-weight 73358 #checksum 337 SEQUENCE /// ENTRY S23298 #type complete TITLE collagen alpha 1(VIII) chain - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S23298 REFERENCE S22243 !$#authors Ninomiya, Y.; Castagnola, P.; Gerecke, D.; Gordon, M.K.; !1Jacenko, O.; LuValle, P.; McCarthy, M.; Muragaki, Y.; !1Nishimura, I.; Oh, S.; Rosenblum, N.; Sato, N.; Sugrue, S.; !1Taylor, R.; Vasios, G.; Yamaguchi, N.; Olsen, B.R. !$#book Extracellular Matrix Genes, Sandell L.J. and Boyd C.D., !1eds., pp.79-114, Academic Press, San Diego, 1990 !$#title The molecular biology of collagens with short triple-helical !1domains. !$#accession S23298 !'##status preliminary !'##molecule_type DNA !'##residues 1-744 ##label NIN CLASSIFICATION #superfamily collagen alpha 1(VIII) chain; complement C1q !1carboxyl-terminal homology FEATURE !$617-743 #domain complement C1q carboxyl-terminal homology !8#label C1Q SUMMARY #length 744 #molecular-weight 73372 #checksum 375 SEQUENCE /// ENTRY S23779 #type complete TITLE collagen alpha 1(VIII) chain - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S23779 REFERENCE S23779 !$#authors Muragaki, Y.; Shiota, C.; Inoue, M.; Ooshima, A.; Olsen, !1B.R.; Ninomiya, Y. !$#journal Eur. J. Biochem. (1992) 207:895-902 !$#title Alpha-1(VIII)-collagen gene transcripts encode a short-chain !1collagen polypeptide and are expressed by various !1epithelial, endothelial and mesenchymal cells in newborn !1mouse tissues. !$#cross-references MUID:92362626; PMID:1499564 !$#accession S23779 !'##status preliminary !'##molecule_type DNA !'##residues 1-743 ##label MUR !'##cross-references EMBL:X66976; NID:g50493; PIDN:CAA47387.1; !1PID:g1359953 CLASSIFICATION #superfamily collagen alpha 1(VIII) chain; complement C1q !1carboxyl-terminal homology FEATURE !$616-742 #domain complement C1q carboxyl-terminal homology !8#label C1Q SUMMARY #length 743 #molecular-weight 73595 #checksum 3864 SEQUENCE /// ENTRY CGHU1D #type complete TITLE collagen alpha 1(X) chain precursor - human ALTERNATE_NAMES procollagen alpha 1(X) chain ORGANISM #formal_name Homo sapiens #common_name man DATE 22-Nov-1993 #sequence_revision 03-Nov-1995 #text_change 22-Jun-1999 ACCESSIONS S26396; S30086; S15826; S18249; A43901; I51870; S21856 REFERENCE S26396 !$#authors Reichenberger, E.; Beier, F.; LuValle, P.; Olsen, B.R.; von !1der Mark, K.; Bertling, W.M. !$#journal FEBS Lett. (1992) 311:305-310 !$#title Genomic organization and full-length cDNA sequence of human !1collagen X. !$#cross-references MUID:93012005; PMID:1397333 !$#accession S26396 !'##molecule_type DNA !'##residues 1-680 ##label REI !'##cross-references EMBL:X68952; EMBL:X72578; EMBL:X72579; EMBL:X72580; !1GB:S47714; GB:S47722; GB:S47732; EMBL:X60382; NID:g30094; !1PIDN:CAA42933.1; PID:g30095 REFERENCE S30085 !$#authors Apte, S.S. !$#submission submitted to the EMBL Data Library, March 1992 !$#accession S30086 !'##molecule_type DNA !'##residues 'TIPFYGWVCWVCLL',52-680 ##label APT !'##cross-references EMBL:X65120; NID:g23129 !'##note the initial difference is probably due to translation of an !1intronic sequence REFERENCE S15826 !$#authors Apte, S.; Mattei, M.G.; Olsen, B.R. !$#journal FEBS Lett. (1991) 282:393-396 !$#title Cloning of human alpha-1(X) collagen DNA and localization of !1the COL10A1 gene to the q21-q22 region of human chromosome !16. !$#cross-references MUID:91243838; PMID:2037056 !$#accession S15826 !'##molecule_type DNA !'##residues 561-647,'G',649-666 ##label AP2 !'##cross-references EMBL:X58879; NID:g30013; PIDN:CAA41686.1; !1PID:g30014 REFERENCE S18249 !$#authors Thomas, J.T.; Cresswell, C.J.; Rash, B.; Nicolai, H.; Jones, !1T.; Solomon, E.; Grant, M.E.; Boot-Handford, R.P. !$#journal Biochem. J. (1991) 280:617-623 !$#title The human collagen X gene. Complete primary translated !1sequence and chromosomal localization. !$#cross-references MUID:92109659; PMID:1764025 !$#accession S18249 !'##molecule_type DNA !'##residues 1-26,'T',28-680 ##label THO !'##cross-references EMBL:X60382; NID:g30094; PIDN:CAA42933.1; !1PID:g30095 !'##note the sequence from Fig. 3 is inconsistent with that from Fig. 2 !1in having 532-Ala REFERENCE A43901 !$#authors Reichenberger, E.; Aigner, T.; von der Mark, K.; Stoss, H.; !1Bertling, W. !$#journal Dev. Biol. (1991) 148:562-572 !$#title In situ hybridization studies on the expression of type X !1collagen in fetal human cartilage. !$#cross-references MUID:92077285; PMID:1743401 !$#accession A43901 !'##molecule_type mRNA !'##residues 547-656 ##label RE2 !'##cross-references GB:M74050; GB:D57494; NID:g339884; PIDN:AAA61221.1; !1PID:g553796 !'##note sequence extracted from NCBI backbone (NCBIN:69012, !1NCBIP:69014) REFERENCE I51870 !$#authors Wallis, G.A.; Rash, B.; Sweetman, W.A.; Thomas, J.T.; Super, !1M.; Evans, G.; Grant, M.E.; Boot-Handford, R.P. !$#journal Am. J. Hum. Genet. (1994) 54:169-178 !$#title Amino acid substitutions of conserved residues in the !1carboxyl-terminal domain of the alpha 1(X) chain of type X !1collagen occur in two unrelated families with metaphyseal !1chondrodysplasia type Schmid. !$#cross-references MUID:94136476; PMID:8304336 !$#accession I51870 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 520-597,'D',599-680 ##label WAL !'##cross-references GB:S68531; NID:g545180; PIDN:AAC60615.1; !1PID:g545181 !'##note mutant sequence from patient with metaphyseal chondrodysplasia !1type Schmid !'##note a second mutant sequence with 614-Pro is also described COMMENT Prolines and lysines at the third position of the tripeptide !1repeating unit (G-X-Y) are hydroxylated to varying extents. !1Prolines are predominately 4-hydroxylated. Lysines are !15-hydroxylated and subsequently O-glycosylated. GENETICS !$#gene GDB:COL10A1 !'##cross-references GDB:128635; OMIM:120110 !$#map_position 6q21-6q22 !$#introns 52/1 !$#note a defect in this gene may cause Schmid metaphyseal !1chondrodysplasia COMPLEX type X collagen may be a homotrimer FUNCTION !$#description structural component of extracellular fibrous polymer !1specifically and transiently expressed at sites of !1endochondral ossification of bone growth plate and !1hypertrophic cartilage; may be important for skeletogenesis CLASSIFICATION #superfamily collagen alpha 1(VIII) chain; complement C1q !1carboxyl-terminal homology KEYWORDS coiled coil; extracellular matrix; glycoprotein; homotrimer; !1hydroxylysine; hydroxyproline; triple helix FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-680 #product collagen alpha 1(X) chain #status predicted !8#label MAT\ !$19-56 #domain amino-terminal nonhelical #status predicted !8#label NC2\ !$57-519 #region interrupted helical\ !$520-680 #domain amino-terminal nonhelical #status predicted !8#label NC1\ !$553-679 #domain complement C1q carboxyl-terminal homology !8#label C1Q\ !$617 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 680 #molecular-weight 66158 #checksum 4935 SEQUENCE /// ENTRY A40020 #type complete TITLE collagen alpha 1(XII) chain precursor - chicken ALTERNATE_NAMES fibrochimerin ORGANISM #formal_name Gallus gallus #common_name chicken DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS A40020; A34485; B34485; A28037; S23814; S22254; S28811 REFERENCE A40020 !$#authors Yamagata, M.; Yamada, K.M.; Yamada, S.S.; Shinomura, T.; !1Tanaka, H.; Nishida, Y.; Obara, M.; Kimata, K. !$#journal J. Cell Biol. (1991) 115:209-221 !$#title The complete primary structure of type XII collagen shows a !1chimeric molecule with reiterated fibronectin type III !1motifs, von Willebrand factor A motifs, a domain homologous !1to a noncollagenous region of type IX collagen, and short !1collagenous domains with an Arg-Gly-Asp site. !$#cross-references MUID:92011862; PMID:1918137 !$#accession A40020 !'##molecule_type mRNA !'##residues 1-3124 ##label YAM !'##cross-references GB:D00824; NID:g222810; PIDN:BAA00701.1; !1PID:g222811 !'##note in the authors' translation residues 1216-1219 are shown after !1residue 1235 and, consequently, residues 1220-1235 are !1displaced four codons to the left REFERENCE A34485 !$#authors Gordon, M.K.; Gerecke, D.R.; Dublet, B.; van der Rest, M.; !1Olsen, B.R. !$#journal J. Biol. Chem. (1989) 264:19772-19778 !$#title Type XII collagen. A large multidomain molecule with partial !1homology to type IX collagen. !$#cross-references MUID:90062079; PMID:2584192 !$#accession A34485 !'##molecule_type mRNA !'##residues 2456-2758,'A',2760-2802,'F',2804-2976,'F',2978-3124 ##label !1GOR !'##cross-references EMBL:J05137; NID:g211284; PIDN:AAA48635.1; !1PID:g211285 !$#accession B34485 !'##molecule_type protein !'##residues 2772-2792;2846-2873 ##label GOR2 REFERENCE A28037 !$#authors Gordon, M.K.; Gerecke, D.R.; Olsen, B.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:6040-6044 !$#title Type XII collagen: distinct extracellular matrix component !1discovered by cDNA cloning. !$#cross-references MUID:87317590; PMID:3476925 !$#accession A28037 !'##molecule_type mRNA !'##residues 2960-2976,'F',2978-3074,'AG' ##label GOR3 !'##cross-references EMBL:M17375; NID:g211649; PIDN:AAA48718.1; !1PID:g211650 !'##note this sequence has been revised in reference A34485 REFERENCE S23814 !$#authors Koch, M.; Bernasconi, C.; Chiquet, M. !$#journal Eur. J. Biochem. (1992) 207:847-856 !$#title A major oligomeric fibroblast proteoglycan identified as a !1novel large form of type-XII collagen. !$#cross-references MUID:92362621; PMID:1323460 !$#accession S23814 !'##molecule_type protein !'##residues 'X',1333,'Q',1335-1347;1914-1928;2504,'X',2506,'X', !12508-2511,'X',2513-2517 ##label KOC REFERENCE S22254 !$#authors Dublet, B.; van der Rest, M. !$#journal J. Biol. Chem. (1987) 262:17724-17727 !$#title Type XII collagen is expressed in embryonic chick tendons. !1Isolation of pepsin-derived fragments. !$#cross-references MUID:88087065; PMID:3121603 !$#accession S22254 !'##molecule_type protein !'##residues 2831-2832,'T',2834,'R',2836-2843;3002-3014 ##label DUB REFERENCE S28811 !$#authors Trueb, J.; Trueb, B. !$#journal Biochim. Biophys. Acta (1992) 1171:97-98 !$#title The two splice variants of collagen XII share a common 5' !1end. !$#cross-references MUID:93042014; PMID:1420368 !$#accession S28811 !'##status preliminary !'##molecule_type mRNA !'##residues 1-24,1189-1257,'S',1259-1263,'E',1265-1280 ##label TRU !'##cross-references EMBL:X67327 GENETICS !$#introns 2845/3; 2863/3; 2887/3; 2899/3; 2922/1; 2985/1; 3008/1; !13065/1 CLASSIFICATION #superfamily collagen alpha 1(XII) chain; fibronectin type !1III repeat homology; von Willebrand factor type A repeat !1homology KEYWORDS alternative splicing; cell binding; coiled coil; connective !1tissue; disulfide bond; extracellular matrix; glycoprotein; !1homotrimer; hydroxyproline; triple helix FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-3124 #product collagen alpha 1(XII) chain #status !8predicted #label MAT\ !$24,1189-3124 #product collagen alpha 1(XII) chain short splice !8form #status predicted #label MA2\ !$24-114 #domain IIIA #status predicted #label IIIA\ !$24-105 #domain fibronectin type III repeat homology #label !8FN3A\ !$137-301 #domain von Willebrand factor type A repeat homology !8#label VWA1\ !$332-425 #domain IIIB #status predicted #label IIIB\ !$332-414 #domain fibronectin type III repeat homology #label !8FN3B\ !$437-601 #domain von Willebrand factor type A repeat homology !8#label VWA2\ !$629-1178 #domain IIIC #status predicted #label IIIC\ !$630-711 #domain fibronectin type III repeat homology #label !8FN3C\ !$721-802 #domain fibronectin type III repeat homology #label !8FN3D\ !$812-895 #domain fibronectin type III repeat homology #label !8FN3E\ !$905-986 #domain fibronectin type III repeat homology #label !8FN3F\ !$995-1076 #domain fibronectin type III repeat homology #label !8FN3G\ !$1086-1169 #domain fibronectin type III repeat homology #label !8FN3H\ !$1197-1361 #domain von Willebrand factor type A repeat homology !8#label VWA3\ !$1384-2295 #domain IIID #status predicted #label IIID\ !$1384-1465 #domain fibronectin type III repeat homology #label !8FN3I\ !$1474-1557 #domain fibronectin type III repeat homology #label !8FN3J\ !$1566-1647 #domain fibronectin type III repeat homology #label !8FN3K\ !$1655-1738 #domain fibronectin type III repeat homology #label !8FN3L\ !$1756-1838 #domain fibronectin type III repeat homology #label !8FN3M\ !$1847-1928 #domain fibronectin type III repeat homology #label !8FN3N\ !$1937-2019 #domain fibronectin type III repeat homology #label !8FN3O\ !$2028-2110 #domain fibronectin type III repeat homology #label !8FN3P\ !$2119-2199 #domain fibronectin type III repeat homology #label !8FN3Q\ !$2207-2294 #domain fibronectin type III repeat homology #label !8FN3R\ !$2325-2490 #domain von Willebrand factor type A repeat homology !8#label VWA4\ !$2438-2440 #region cell adhesion #status predicted\ !$2509-2750 #domain IXP, homologous to NC4 domain of type IX !8collagen #status predicted #label IXP\ !$2751-2902 #domain collagenous COL2 #status predicted #label !8COL2\ !$2899-2901 #region cell attachment (R-G-D) motif\ !$2903-2945 #domain non-collagenous NC2 #status predicted #label !8NC2\ !$2946-3048 #domain collagenous COL1 #status predicted #label !8COL1\ !$3049-3124 #domain non-collagenous NC1 #status predicted #label !8NC1\ !$32,1006,1032,1044, !$1512,1767,2210, !$2273,2532,2683 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$2780,2789,2836, !$2842,2860,2866, !$2869,3004,3007 #modified_site hydroxyproline (Pro) #status !8experimental SUMMARY #length 3124 #molecular-weight 340580 #checksum 6491 SEQUENCE /// ENTRY A45974 #type complete TITLE collagen alpha 1(XIV) chain precursor, short form 2 - chicken ALTERNATE_NAMES undulin ORGANISM #formal_name Gallus gallus #common_name chicken DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A45974; S30085; S22916; S17035; S20833 REFERENCE A45974 !$#authors Gerecke, D.R.; Foley, J.W.; Castagnola, P.; Gennari, M.; !1Dublet, B.; Cancedda, R.; Linsenmayer, T.F.; van der Rest, !1M.; Olsen, B.R.; Gordon, M.K. !$#journal J. Biol. Chem. (1993) 268:12177-12184 !$#title Type XIV collagen is encoded by alternative transcripts with !1distinct 5' regions and is a multidomain protein with !1homologies to von Willebrand's factor, fibronectin, and !1other matrix proteins. !$#cross-references MUID:93280195; PMID:8505337 !$#accession A45974 !'##status preliminary !'##molecule_type mRNA; protein !'##residues 1-1747 ##label GER !'##experimental_source embryo skin !'##note sequence inconsistent with the nucleotide translation !'##note sequence extracted from NCBI backbone (NCBIN:133364, !1NCBIP:133365) REFERENCE S30085 !$#authors Apte, S.S. !$#submission submitted to the EMBL Data Library, March 1992 !$#accession S30085 !'##molecule_type mRNA !'##residues 1472-1660 ##label APT !'##cross-references EMBL:X65122; NID:g62871; PIDN:CAA46238.1; !1PID:g938175 REFERENCE S22916 !$#authors Trueb, J.; Trueb, B. !$#journal Eur. J. Biochem. (1992) 207:549-557 !$#title Type XIV collagen is a variant of undulin. !$#cross-references MUID:92339443; PMID:1339349 !$#accession S22916 !'##status preliminary !'##molecule_type mRNA !'##residues 286-494,'Q',496-834,'A',836-1119,'KL',1122-1402,1409-1439 !1##label TRU REFERENCE S17035 !$#authors Gordon, M.K.; Castagnola, P.; Dublet, B.; Linsenmayer, T.F.; !1van der Rest, M.; Mayne, R.; Olsen, B.R. !$#journal Eur. J. Biochem. (1991) 201:333-338 !$#title Cloning of a cDNA for a new member of the class of !1fibril-associated collagens with interrupted triple helices. !$#cross-references MUID:92037585; PMID:1935930 !$#accession S17035 !'##molecule_type mRNA !'##residues 1472-1659 ##label GOR1 !$#accession S20833 !'##molecule_type protein !'##residues 1551-1570;1593-1599;1639-1667 ##label GOR2 CLASSIFICATION #superfamily collagen alpha 1(XIV) chain; fibronectin type !1III repeat homology; von Willebrand factor type A repeat !1homology KEYWORDS alternative splicing; coiled coil; extracellular matrix; !1glycoprotein; trimer; triple helix FEATURE !$40-204 #domain von Willebrand factor type A repeat homology !8#label VWA1\ !$236-317 #domain fibronectin type III repeat homology #label !8FN3A\ !$326-409 #domain fibronectin type III repeat homology #label !8FN3B\ !$418-498 #domain fibronectin type III repeat homology #label !8FN3C\ !$507-591 #domain fibronectin type III repeat homology #label !8FN3D\ !$625-707 #domain fibronectin type III repeat homology #label !8FN3E\ !$716-798 #domain fibronectin type III repeat homology #label !8FN3F\ !$806-893 #domain fibronectin type III repeat homology #label !8FN3G\ !$924-1089 #domain von Willebrand factor type A repeat homology !8#label VWA2\ !$1111-1352 #domain non-collagenous NC4 #status predicted #label !8NC4\ !$1511-1553 #domain non-collagenous NC2 #status predicted #label !8NC2\ !$1554-1659 #domain triple helical domain COL1 #status predicted !8#label COL1 SUMMARY #length 1747 #molecular-weight 187215 #checksum 7514 SEQUENCE /// ENTRY C45051 #type complete TITLE lamprin 2 precursor, long splice form - sea lamprey ALTERNATE_NAMES lamprin L-0.9-12 CONTAINS lamprin 2 precursor, short splice form (lamprin L-0.9-10) ORGANISM #formal_name Petromyzon marinus #common_name sea lamprey DATE 30-Apr-1993 #sequence_revision 30-Apr-1993 #text_change 22-Jun-1999 ACCESSIONS C45051; A45051 REFERENCE A45051 !$#authors Robson, P.; Wright, G.M.; Sitarz, E.; Maiti, A.; Rawat, M.; !1Youson, J.H.; Keeley, F.W. !$#journal J. Biol. Chem. (1993) 268:1440-1447 !$#title Characterization of lamprin, an unusual matrix protein from !1lamprey cartilage. Implications for evolution, structure, !1and assembly of elastin and other fibrillar proteins. !$#cross-references MUID:93123269; PMID:7678258 !$#accession C45051 !'##molecule_type mRNA !'##residues 1-139 ##label ROB !'##cross-references GB:L05925; NID:g213209; PIDN:AAA49269.1; !1PID:g213210 !'##note sequence extracted from NCBI backbone (NCBIP:122170) !$#accession A45051 !'##molecule_type mRNA !'##residues 1-85,105-139 ##label RO2 !'##cross-references GB:L05924; NID:g213207; PIDN:AAA49268.1; !1PID:g213208 !'##note sequence extracted from NCBI backbone (NCBIP:122166) COMMENT These forms are encoded by a different gene than B45051; we !1have arbitrarily designated them lamprin 2 and lamprin 1. CLASSIFICATION #superfamily lamprin KEYWORDS alternative splicing; cartilage; extracellular matrix FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-139 #product lamprin 2, long splice form #status !8predicted #label MAT1\ !$20-85,105-139 #product lamprin 2, short splice form #status !8predicted #label MAT2 SUMMARY #length 139 #molecular-weight 13257 #checksum 5048 SEQUENCE /// ENTRY B45051 #type complete TITLE lamprin 1 precursor - sea lamprey ALTERNATE_NAMES lamprin L-1.8-10 ORGANISM #formal_name Petromyzon marinus #common_name sea lamprey DATE 30-Apr-1993 #sequence_revision 30-Apr-1993 #text_change 21-Jul-2000 ACCESSIONS B45051 REFERENCE A45051 !$#authors Robson, P.; Wright, G.M.; Sitarz, E.; Maiti, A.; Rawat, M.; !1Youson, J.H.; Keeley, F.W. !$#journal J. Biol. Chem. (1993) 268:1440-1447 !$#title Characterization of lamprin, an unusual matrix protein from !1lamprey cartilage. Implications for evolution, structure, !1and assembly of elastin and other fibrillar proteins. !$#cross-references MUID:93123269; PMID:7678258 !$#accession B45051 !'##molecule_type mRNA !'##residues 1-119 ##label ROB !'##cross-references GB:L05926; NID:g213211; PIDN:AAA49270.1; !1PID:g213212 !'##note sequence extracted from NCBI backbone (NCBIP:122168) COMMENT This sequence is encoded by a different gene than C45051; we !1have arbitrarily designated them lamprin 1 and lamprin 2. CLASSIFICATION #superfamily lamprin KEYWORDS cartilage; extracellular matrix FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-119 #product lamprin 1 #status predicted #label MAT SUMMARY #length 119 #molecular-weight 11329 #checksum 851 SEQUENCE /// ENTRY CGBEHS #type complete TITLE collagen-like protein - saimiriine herpesvirus 1 (strain 484-77) ORGANISM #formal_name saimiriine herpesvirus 1 DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 18-Feb-1995 ACCESSIONS A36770 REFERENCE A36770 !$#authors Geck, P.; Whitaker, S.A.; Medveczky, M.M.; Medveczky, P.G. !$#journal J. Virol. (1990) 64:3509-3515 !$#title Expression of collagen-like sequences by a tumor virus, !1Herpesvirus saimiri. !$#cross-references MUID:90279084; PMID:2161952 !$#accession A36770 !'##molecule_type DNA !'##residues 1-99 ##label GEC !'##cross-references EMBL:M31965 CLASSIFICATION #superfamily squirrel monkey herpesvirus collagen-like !1protein FEATURE !$15-70 #region collagen-like SUMMARY #length 99 #molecular-weight 9889 #checksum 6734 SEQUENCE /// ENTRY EAHU #type complete TITLE elastin precursor, long splice form - human ALTERNATE_NAMES tropoelastin ORGANISM #formal_name Homo sapiens #common_name man DATE 22-Jun-1990 #sequence_revision 26-Jul-1996 #text_change 22-Jun-1999 ACCESSIONS A32707; A33705; A30524; A53891 REFERENCE A32707 !$#authors Indik, Z.; Yeh, H.; Ornstein-Goldstein, N.; Sheppard, P.; !1Anderson, N.; Rosenbloom, J.C.; Peltonen, L.; Rosenbloom, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:5680-5684 !$#title Alternative splicing of human elastin mRNA indicated by !1sequence analysis of cloned genomic and complementary DNA. !$#cross-references MUID:87289668; PMID:3039501 !$#accession A32707 !'##molecule_type mRNA !'##residues 1-500,507-792 ##label IND !'##cross-references GB:M16983; GB:J02948 REFERENCE A33705 !$#authors Bashir, M.M.; Indik, Z.; Yeh, H.; Ornstein-Goldstein, N.; !1Rosenbloom, J.C.; Abrams, W.; Fazio, M.; Uitto, J.; !1Rosenbloom, J. !$#journal J. Biol. Chem. (1989) 264:8887-8891 !$#title Characterization of the complete human elastin gene. !1Delineation of unusual features in the 5'-flanking region. !$#cross-references MUID:89255358; PMID:2722804 !$#accession A33705 !'##molecule_type DNA !'##residues 1-27 ##label BAS !'##cross-references GB:J04821; NID:g182052; PIDN:AAA52379.1; !1PID:g553276 REFERENCE A30524 !$#authors Fazio, M.J.; Olsen, D.R.; Kauh, E.A.; Baldwin, C.T.; Indik, !1Z.; Ornstein-Goldstein, N.; Yeh, H.; Rosenbloom, J.; Uitto, !1J. !$#journal J. Invest. Dermatol. (1988) 91:458-464 !$#title Cloning of full-length elastin cDNAs from a human skin !1fibroblast recombinant cDNA library: further elucidation of !1alternative splicing utilizing exon-specific !1oligonucleotides. !$#cross-references MUID:89009960; PMID:3171221 !$#accession A30524 !'##molecule_type mRNA !'##residues 1-453,483-617,651-792 ##label FAZ !'##cross-references EMBL:M36860; NID:g182061; PIDN:AAA52382.1; !1PID:g182062 !'##note this sequence represents a composite of several splice forms REFERENCE A53891 !$#authors Fazio, M.J.; Olsen, D.R.; Kuivaniemi, H.; Chu, M.L.; !1Davidson, J.M.; Rosenbloom, J.; Uitto, J. !$#journal Lab. Invest. (1988) 58:270-277 !$#title Isolation and characterization of human elastin cDNAs, and !1age-associated variation in elastin gene expression in !1cultured skin fibroblasts. !$#cross-references MUID:88156138; PMID:2831431 !$#accession A53891 !'##molecule_type mRNA !'##residues 164-453,483-500,507-617,651-792 ##label FA2 !'##cross-references GB:M24782; NID:g182063; PIDN:AAA53190.1; !1PID:g182064 COMMENT The term tropoelastin refers to a soluble precursor form of !1the extracellular matrix protein elastin, prior to the !1extensive cross-linking of lysine residues that results from !1peptidyl-lysine oxidase activity. GENETICS !$#gene GDB:ELN !'##cross-references GDB:119107; OMIM:130160 !$#map_position 7q11.23-7q11.23 CLASSIFICATION #superfamily elastin KEYWORDS alternative splicing; extracellular matrix; glycoprotein; !1hydroxylysine FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-792 #product elastin #status predicted #label MAT\ !$782-787 #disulfide_bonds #status predicted SUMMARY #length 792 #molecular-weight 69094 #checksum 4979 SEQUENCE /// ENTRY EABO #type complete TITLE elastin precursor, splice form a - bovine ALTERNATE_NAMES tropoelastin CONTAINS elastin precursor, splice form b; elastin precursor, splice form c ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 08-Jun-1989 #sequence_revision 26-Jul-1996 #text_change 22-Jun-1999 ACCESSIONS A31865; A26728; B26728; C26728; A22343; I45886 REFERENCE A31865 !$#authors Yeh, H.; Anderson, N.; Ornstein-Goldstein, N.; Bashir, M.M.; !1Rosenbloom, J.C.; Abrams, W.; Indik, Z.; Yoon, K.; Parks, !1W.; Mecham, R.; Rosenbloom, J. !$#journal Biochemistry (1989) 28:2365-2370 !$#title Structure of the bovine elastin gene and S1 nuclease !1analysis of alternative splicing of elastin mRNA in the !1bovine nuchal ligament. !$#cross-references MUID:89274159; PMID:2543440 !$#accession A31865 !'##molecule_type DNA !'##residues 1-27 ##label YEH !'##cross-references GB:J02855; NID:g340504; PIDN:AAA30776.1; !1PID:g552339 REFERENCE A92640 !$#authors Raju, K.; Anwar, R.A. !$#journal J. Biol. Chem. (1987) 262:5755-5762 !$#title Primary structures of bovine elastin a, b, and c deduced !1from the sequences of cDNA clones. !$#cross-references MUID:87194772; PMID:3032943 !$#accession A26728 !'##molecule_type mRNA !'##residues 1,'RS',4-11,'E',13-636,'V',638-747 ##label RAJ !'##cross-references GB:J02717; NID:g163019; PIDN:AAA30503.1; !1PID:g163020 !$#accession B26728 !'##molecule_type mRNA !'##residues 1,'RS',4-11,'E',13-225,240-636,'V',638-747 ##label RA2 !'##cross-references GB:K03505; NID:g163025; PIDN:AAA30505.1; !1PID:g163026 !$#accession C26728 !'##molecule_type mRNA !'##residues 1,'RS',4-11,'E',13-225,260-636,'V',638-747 ##label RA3 !'##cross-references GB:K03506; NID:g163027; PIDN:AAA30506.1; !1PID:g163028 REFERENCE A22343 !$#authors Cicila, G.; May, M.; Ornstein-Goldstein, N.; Indik, Z.; !1Morrow, S.; Yeh, H.S.; Rosenbloom, J.; Boyd, C.; Rosenbloom, !1J.; Yoon, K. !$#journal Biochemistry (1985) 24:3075-3080 !$#title Structure of the 3' portion of the bovine elastin gene. !$#cross-references MUID:85280426; PMID:2992576 !$#accession A22343 !'##molecule_type DNA !'##residues 613-747 ##label CIC !'##cross-references GB:M20415 REFERENCE I45885 !$#authors Rosenbloom, J. !$#journal Lab. Invest. (1984) 51:605-623 !$#title Biology of disease: Elastin: Relation of protein and gene !1structure to disease. !$#cross-references MUID:85059254; PMID:6150137 !$#accession I45886 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 678-683,685-747 ##label ROS !'##cross-references GB:M31898; NID:g163015; PIDN:AAA96417.1; !1PID:g163018 REFERENCE A58621 !$#authors Brown, P.L.; Mecham, L.; Tisdale, C.; Mecham, R.P. !$#journal Biochem. Biophys. Res. Commun. (1992) 186:549-555 !$#title The cysteine residues in the carboxy terminal domain of !1tropoelastin form an intrachain disulfide bond that !1stabilizes a loop structure and positively charged pocket. !$#cross-references MUID:92337651; PMID:1632791 !$#contents annotation, disulfide bonds COMMENT The term tropoelastin refers to a soluble precursor form of !1the extracellular matrix protein elastin, prior to the !1extensive cross-linking of lysine residues that results from !1peptidyl-lysine oxidase activity. GENETICS !$#introns 634/3; 653/3; 676/3; 689/3; 707/3; 716/3; 733/3 !$#note the list of introns is incomplete CLASSIFICATION #superfamily elastin KEYWORDS alternative splicing; extracellular matrix; glycoprotein; !1hydroxylysine FEATURE !$1-747 #product elastin precursor, splice form a #status !8predicted #label EPA\ !$1-225,260-747 #product elastin precursor, splice form c #status !8predicted #label EPC\ !$1-225,240-747 #product elastin precursor, splice form b #status !8predicted #label EPB\ !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-747 #product elastin #status predicted #label MAT\ !$105,109,252,271, !$275,324,327,400, !$404,407,445,448, !$489,493,544,548, !$552,606,609,645, !$649,685,688 #modified_site allysine (Lys) #status predicted\ !$737-742 #disulfide_bonds #status experimental SUMMARY #length 747 #molecular-weight 64000 #checksum 1440 SEQUENCE /// ENTRY EAMS #type complete TITLE elastin precursor - mouse ALTERNATE_NAMES tropoelastin ORGANISM #formal_name Mus musculus #common_name house mouse DATE 18-Aug-1995 #sequence_revision 16-Aug-1996 #text_change 22-Jun-1999 ACCESSIONS A55721 REFERENCE A55721 !$#authors Wydner, K.S.; Sechler, J.L.; Boyd, C.D.; Passmore, H.C. !$#journal Genomics (1994) 23:125-131 !$#title Use of an intron length polymorphism to localize the !1tropoelastin gene to mouse chromosome 5 in a region of !1linkage conservation with human chromosome 7. !$#cross-references MUID:95130069; PMID:7829060 !$#accession A55721 !'##molecule_type mRNA !'##residues 1-860 ##label WYD !'##cross-references GB:U08210; NID:g473273; PIDN:AAA80155.1; !1PID:g473274 GENETICS !$#map_position 5 CLASSIFICATION #superfamily elastin KEYWORDS alternative splicing; extracellular matrix; glycoprotein; !1hydroxylysine FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-860 #product elastin #status predicted #label MAT\ !$850-855 #disulfide_bonds #status predicted SUMMARY #length 860 #molecular-weight 71954 #checksum 3440 SEQUENCE /// ENTRY EART #type complete TITLE elastin precursor - rat ALTERNATE_NAMES tropoelastin ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 11-Jan-1991 #sequence_revision 16-Aug-1996 #text_change 22-Jun-1999 ACCESSIONS A36106; A30878; A36523; S02173; I54172; I68505 REFERENCE A36106 !$#authors Pierce, R.A.; Deak, S.B.; Stolle, C.A.; Boyd, C.D. !$#journal Biochemistry (1990) 29:9677-9683 !$#title Heterogeneity of rat tropoelastin mRNA revealed by cDNA !1cloning. !$#cross-references MUID:91104868; PMID:1702999 !$#accession A36106 !'##molecule_type mRNA !'##residues 1-864 ##label PIE !'##cross-references GB:M60647; GB:J05292; NID:g207444; PIDN:AAA42269.1; !1PID:g207445 REFERENCE A30878 !$#authors Deak, S.B.; Pierce, R.A.; Belsky, S.A.; Riley, D.J.; Boyd, !1C.D. !$#journal J. Biol. Chem. (1988) 263:13504-13507 !$#title Rat tropoelastin is synthesized from a 3.5-kilobase mRNA. !$#cross-references MUID:88330868; PMID:2971041 !$#accession A30878 !'##status preliminary !'##molecule_type mRNA !'##residues 781-864 ##label DEA !'##cross-references GB:J04035; NID:g207442; PIDN:AAA42268.1; !1PID:g207443 REFERENCE A36523 !$#authors Franzblau, C.; Pratt, C.A.; Faris, B.; Colannino, N.M.; !1Offner, G.D.; Mogayzel Jr., P.J.; Troxler, R.F. !$#journal J. Biol. Chem. (1989) 264:15115-15119 !$#title Role of tropoelastin fragmentation in elastogenesis in rat !1smooth muscle cells. !$#cross-references MUID:89359327; PMID:2768256 !$#accession A36523 !'##molecule_type protein !'##residues 22-31 ##label FRA REFERENCE S02173 !$#authors Rich, C.B.; Foster, J.A. !$#journal Arch. Biochem. Biophys. (1989) 268:551-558 !$#title Characterization of rat heart tropoelastin. !$#cross-references MUID:89117149; PMID:2913947 !$#accession S02173 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 'IP',369-545,548-764,770-864 ##label RIC !'##experimental_source heart REFERENCE I54172 !$#authors Pierce, R.A.; Alatawi, A.; Deak, S.B.; Boyd, C.D. !$#journal Genomics (1992) 12:651-658 !$#title Elements of the rat tropoelastin gene associated with !1alternative splicing. !$#cross-references MUID:92241859; PMID:1572637 !$#accession I54172 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 264-533 ##label RES !'##cross-references GB:M86372; NID:g207455; PIDN:AAA42271.1; !1PID:g554527 !$#accession I68505 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 558-864 ##label RE2 !'##cross-references GB:M86376; NID:g207459; PIDN:AAA42272.1; !1PID:g207462 GENETICS !$#introns 277/1; 292/1; 308/1; 339/1; 359/1; 419/1; 437/1; 467/1; 484/ !11; 601/1; 621/1; 663/1; 676/1; 714/1; 733/1; 779/1; 792/1; !1809/1; 824/1; 834/1; 851/1 !$#note the list of introns may be incomplete CLASSIFICATION #superfamily elastin KEYWORDS alternative splicing; extracellular matrix; glycoprotein; !1hydroxylysine FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-864 #product elastin #status predicted #label MAT\ !$854-859 #disulfide_bonds #status predicted SUMMARY #length 864 #molecular-weight 72785 #checksum 6503 SEQUENCE /// ENTRY GZRT0 #type complete TITLE secretory granule proteoglycan core protein precursor - rat ALTERNATE_NAMES 19PG core protein; chondroitin sulfate proteoglycan core protein; RBL-1 cell proteoglycan peptide core ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 22-Jun-1999 ACCESSIONS A25644; A28059; A60653 REFERENCE A25644 !$#authors Bourdon, M.A.; Shiga, M.; Ruoslahti, E. !$#journal J. Biol. Chem. (1986) 261:12534-12537 !$#title Identification from cDNA of the precursor form of a !1chondroitin sulfate proteoglycan core protein. !$#cross-references MUID:86304425; PMID:2427521 !$#accession A25644 !'##molecule_type mRNA !'##residues 1-179 ##label BOU !'##cross-references GB:K02934; GB:M14282; NID:g207039; PIDN:AAA42171.1; !1PID:g207040 !'##experimental_source yolk sac carcinoma REFERENCE A28059 !$#authors Avraham, S.; Stevens, R.L.; Gartner, M.C.; Austen, K.F.; !1Lalley, P.A.; Weis, J.H. !$#journal J. Biol. Chem. (1988) 263:7292-7296 !$#title Isolation of a cDNA that encodes the peptide core of the !1secretory granule proteoglycan of rat basophilic leukemia-1 !1cells and assessment of its homology to the human analogue. !$#cross-references MUID:88213412; PMID:3366780 !$#accession A28059 !'##molecule_type mRNA !'##residues 1-179 ##label AVR !'##cross-references EMBL:J03224; NID:g206108; PIDN:AAA41837.1; !1PID:g206109 REFERENCE A60653 !$#authors Giorda, R.; Chambers, W.H.; Dahl, C.A.; Trucco, M. !$#journal Nat. Immun. Cell Growth Regul. (1990) 9:91-102 !$#title Isolation and characterization of a cDNA that encodes the !1core protein of the cytolytic granule proteoglycan in rat !1natural killer cells. !$#cross-references MUID:90279692; PMID:2352541 !$#accession A60653 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-179 ##label GIO CLASSIFICATION #superfamily proteoglycan 10K core protein KEYWORDS chondroitin sulfate proteoglycan; dermatan sulfate; !1extracellular matrix; fibroblast; glycoprotein; heparin !1binding FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-75 #domain activation peptide #status predicted #label !8APT\ !$76-179 #product proteoglycan 10K core protein #status !8predicted #label MPT\ !$90-138 #region chondroitin sulfate attachment (S-G repeats) SUMMARY #length 179 #molecular-weight 18577 #checksum 2381 SEQUENCE /// ENTRY LKHU #type complete TITLE proteoglycan link protein precursor [validated] - human ALTERNATE_NAMES cartilage link protein ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 08-Dec-2000 ACCESSIONS S14914; S04244; S03868; A36308; S14926; S09309; S08041 REFERENCE S14914 !$#authors Dudhia, J.; Hardingham, T.E. !$#journal Nucleic Acids Res. (1990) 18:1292 !$#title The primary structure of human cartilage link protein. !$#cross-references MUID:90206798; PMID:2320422 !$#accession S14914 !'##molecule_type mRNA !'##residues 1-354 ##label DUD !'##cross-references EMBL:X17405; NID:g463246; PIDN:CAA35462.1; !1PID:g34378 !'##note the authors translated the codon GAT for residue 93 as Ala REFERENCE S04243 !$#authors Dudhia, J.; Hardingham, T.E. !$#journal J. Mol. Biol. (1989) 206:749-753 !$#title Appendix. Isolation and sequence of cDNA clones for pig and !1human cartilage link protein. !$#accession S04244 !'##molecule_type mRNA !'##residues 223-354 ##label DUD2 !'##cross-references EMBL:Y00166 !'##note the authors translated the codon CTG for residue 264 as Arg and !1TTG for residue 309 as Trp REFERENCE S03868 !$#authors Nguyen, Q.; Murphy, G.; Roughley, P.J.; Mort, J.S. !$#journal Biochem. J. (1989) 259:61-67 !$#title Degradation of proteoglycan aggregate by a cartilage !1metalloproteinase. Evidence for the involvement of !1stromelysin in the generation of link protein heterogeneity !1in situ. !$#cross-references MUID:89246328; PMID:2719651 !$#accession S03868 !'##molecule_type protein !'##residues 16-35 ##label NGU REFERENCE A36308 !$#authors Osborne-Lawrence, S.L.; Sinclair, A.K.; Hicks, R.C.; Lacey, !1S.W.; Eddy Jr., R.L.; Byers, M.G.; Shows, T.B.; Duby, A.D. !$#journal Genomics (1990) 8:562-567 !$#title Complete amino acid sequence of human cartilage link protein !1(CRTL1) deduced from cDNA clones and chromosomal assignment !1of the gene. !$#cross-references MUID:91139126; PMID:2286376 !$#accession A36308 !'##status preliminary; nucleic acid sequence not shown; not compared !1with conceptual translation !'##molecule_type mRNA !'##residues 1-354 ##label OSB REFERENCE S14926 !$#authors Dudhia, J.; Hardingham, T.E. !$#journal Nucleic Acids Res. (1990) 18:2214 !$#title The primary structure of human cartilage link protein. !$#cross-references MUID:90245703; PMID:2336413 !$#accession S14926 !'##status preliminary !'##molecule_type mRNA !'##residues 1-92,'A',94-354 ##label NUC REFERENCE S09309 !$#authors Nguyen, Q.; Mort, J.S.; Roughley, P.J. !$#journal Biochem. J. (1990) 266:569-573 !$#title Cartilage proteoglycan aggregate is degraded more !1extensively by cathepsin L than by cathepsin B. !$#cross-references MUID:90197639; PMID:2317204 !$#accession S09309 !'##molecule_type protein !'##residues 16-38,'X',40-55,57-60,62-65,'X',67,'X',69-80 ##label NG2 GENETICS !$#gene GDB:CRTL1 !'##cross-references GDB:125232; OMIM:115435 !$#map_position 5q13-5q14 CLASSIFICATION #superfamily proteoglycan link protein; immunoglobulin !1homology; link protein repeat homology KEYWORDS cartilage; duplication; extracellular matrix; glycoprotein FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-354 #product proteoglycan link protein #status !8experimental #label MAT\ !$54-141 #domain immunoglobulin homology #label IMM\ !$176-253 #domain link protein repeat homology #label LNK1\ !$274-350 #domain link protein repeat homology #label LNK2\ !$21,56 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$61-139 #disulfide_bonds #status predicted SUMMARY #length 354 #molecular-weight 40165 #checksum 3882 SEQUENCE /// ENTRY S04243 #type complete TITLE proteoglycan link protein precursor - pig ALTERNATE_NAMES cartilage link protein ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 28-Feb-1990 #sequence_revision 28-Feb-1990 #text_change 22-Jun-1999 ACCESSIONS S04243; I47145 REFERENCE S04243 !$#authors Dudhia, J.; Hardingham, T.E. !$#journal J. Mol. Biol. (1989) 206:749-753 !$#title Appendix. Isolation and sequence of cDNA clones for pig and !1human cartilage link protein. !$#accession S04243 !'##molecule_type mRNA !'##residues 1-354 ##label DUD !'##cross-references EMBL:Y00165; NID:g2009; PIDN:CAA68358.1; PID:g2010 REFERENCE I47145 !$#authors Perkins, S.J.; Nealis, A.S.; Dudhia, J.; Hardingham, T.E. !$#journal J. Mol. Biol. (1989) 206:737-753 !$#title Immunoglobulin fold and tandem repeat structures in !1proteoglycan N-terminal domains and link protein. !$#cross-references MUID:89293837; PMID:2738916 !$#accession I47145 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-354 ##label PER !'##cross-references EMBL:Y00165; NID:g2009; PIDN:CAA68358.1; PID:g2010 CLASSIFICATION #superfamily proteoglycan link protein; immunoglobulin !1homology; link protein repeat homology KEYWORDS cartilage; duplication; extracellular matrix; glycoprotein FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-354 #product proteoglycan link protein #status predicted !8#label MAT\ !$54-141 #domain immunoglobulin homology #label IMM\ !$176-253 #domain link protein repeat homology #label LNK1\ !$274-350 #domain link protein repeat homology #label LNK2\ !$21,56 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$61-139 #disulfide_bonds #status predicted SUMMARY #length 354 #molecular-weight 40260 #checksum 3261 SEQUENCE /// ENTRY S42938 #type complete TITLE proteoglycan link protein precursor - horse ALTERNATE_NAMES cartilage link protein ORGANISM #formal_name Equus caballus #common_name domestic horse DATE 06-Jan-1995 #sequence_revision 06-Jan-1995 #text_change 22-Jun-1999 ACCESSIONS S42938 REFERENCE S42938 !$#authors Dudhia, J.; Platt, D. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S42938 !'##molecule_type mRNA !'##residues 1-354 ##label DUD !'##cross-references EMBL:X78077; NID:g459438; PIDN:CAA54987.1; !1PID:g459439 CLASSIFICATION #superfamily proteoglycan link protein; immunoglobulin !1homology; link protein repeat homology KEYWORDS cartilage; duplication; extracellular matrix; glycoprotein FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-354 #product proteoglycan link protein #status predicted !8#label MAT\ !$54-141 #domain immunoglobulin homology #label IMM\ !$176-253 #domain link protein repeat homology #label LNK1\ !$274-350 #domain link protein repeat homology #label LNK2\ !$21,56 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$61-139 #disulfide_bonds #status predicted SUMMARY #length 354 #molecular-weight 40077 #checksum 3953 SEQUENCE /// ENTRY LKRT2 #type complete TITLE proteoglycan link protein 2 precursor - rat ALTERNATE_NAMES cartilage link protein ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 13-Aug-1986 #sequence_revision 24-Oct-1997 #text_change 13-Nov-1998 ACCESSIONS A28654; A24880; A02869 REFERENCE A28654 !$#authors Rhodes, C.; Doege, K.; Sasaki, M.; Yamada, Y. !$#journal J. Biol. Chem. (1988) 263:6063-6067 !$#title Alternative splicing generates two different mRNA sepcies !1for rat link protein. !$#cross-references MUID:88198139; PMID:2452158 !$#accession A28654 !'##status preliminary !'##molecule_type mRNA !'##residues 1-408 ##label RHO REFERENCE A24880 !$#authors Doege, K.; Hassell, J.R.; Caterson, B.; Yamada, Y. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:3761-3765 !$#title Link protein cDNA sequence reveals a tandemly repeated !1protein structure. !$#cross-references MUID:86233314; PMID:3459153 !$#accession A24880 !'##molecule_type mRNA !'##residues 180-408 ##label DOE REFERENCE A02869 !$#authors Neame, P.J.; Christner, J.E.; Baker, J.R. !$#journal J. Biol. Chem. (1986) 261:3519-3535 !$#title The primary structure of link protein from rat !1chondrosarcoma proteoglycan aggregate. !$#cross-references MUID:86140139; PMID:2419334 !$#accession A02869 !'##molecule_type protein !'##residues 16-33,'A',89-375,'W',377-408 ##label NEA COMMENT This protein was extracted from rat chondrosarcoma. COMMENT Residues 259-277 and 358-376 (approximately) form epitopes !1for the species-nonspecific anti-link protein monoclonal !1antibody 8A4. COMMENT Link proteins interact with and stabilize aggregates of !1hyaluronic acid and chondroitin sulfate proteoglycan in the !1extracellular cartilage matrix. CLASSIFICATION #superfamily proteoglycan link protein; immunoglobulin !1homology; link protein repeat homology KEYWORDS cartilage; chondroitin sulfate proteoglycan; duplication; !1glycoprotein; hyaluronic acid FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-408 #product proteoglycan link protein 2 #status !8experimental #label MAT\ !$108-195 #domain immunoglobulin homology #label IMM\ !$230-307 #domain link protein repeat homology #label LNK1\ !$328-404 #domain link protein repeat homology #label LNK2\ !$110 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$115-193,235-306, !$259-280,333-403, !$358-379 #disulfide_bonds #status experimental SUMMARY #length 408 #molecular-weight 46483 #checksum 752 SEQUENCE /// ENTRY LKCH #type complete TITLE proteoglycan link protein precursor - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 22-Jun-1999 ACCESSIONS A28305; A24881; A39097; B39097 REFERENCE A28305 !$#authors Kiss, I.; Deak, F.; Mestric, S.; Delius, H.; Soos, J.; !1Dekany, K.; Argraves, W.S.; Sparks, K.J.; Goetinck, P.F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:6399-6403 !$#title Structure of the chicken link protein gene: exons correlate !1with the protein domains. !$#cross-references MUID:87317659; PMID:3476955 !$#accession A28305 !'##molecule_type DNA !'##residues 1-355 ##label KIS !'##cross-references GB:M35038; NID:g212264; PIDN:AAA48941.1; !1PID:g212267 REFERENCE A24881 !$#authors Deak, F.; Kiss, I.; Sparks, K.J.; Argraves, W.S.; Hampikian, !1G.; Goetinck, P.F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:3766-3770 !$#title Complete amino acid sequence of chicken cartilage link !1protein deduced from cDNA clones. !$#cross-references MUID:86233315; PMID:3459154 !$#accession A24881 !'##molecule_type mRNA !'##residues 1-355 ##label DEA !'##cross-references GB:M13212; NID:g212259; PIDN:AAA48940.1; !1PID:g212260 !'##experimental_source embryonic sternal cartilage REFERENCE A39097 !$#authors Wu, L.N.Y.; Genge, B.R.; Wuthier, R.E. !$#journal J. Biol. Chem. (1991) 266:1187-1194 !$#title Association between proteoglycans and matrix vesicles in the !1extracellular matrix of growth plate cartilage. !$#cross-references MUID:91093230; PMID:1985942 !$#accession A39097 !'##molecule_type protein !'##residues 40-55,'X',57-60,'X',62-75,'X',77-78,'X' ##label WUA !'##note 38K protein, a major component of matrix vesicles; Asn-56 !1appears to be glycosylated !$#accession B39097 !'##molecule_type protein !'##residues 40-55,'X',57-59 ##label WU2 !'##note 39K protein, a minor component of matrix vesicles COMMENT Link proteins stabilize the aggregates of proteoglycan !1monomers with hyaluronic acid. Further, a large proteolytic !1fragment of link protein is a major componenet of matrix !1vesicles (microstructures that induce mineralization). GENETICS !$#introns 34/1; 159/1; 260/1 !$#note single copy gene CLASSIFICATION #superfamily proteoglycan link protein; immunoglobulin !1homology; link protein repeat homology KEYWORDS cartilage; duplication; extracellular matrix; glycoprotein FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-355 #product link protein #status predicted #label MAT\ !$54-142 #domain immunoglobulin homology #label IMM\ !$177-254 #domain link protein repeat homology #label LNK1\ !$275-351 #domain link protein repeat homology #label LNK2\ !$21 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$56 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$61-140,182-253, !$206-227,280-350, !$305-326 #disulfide_bonds #status predicted SUMMARY #length 355 #molecular-weight 40533 #checksum 5632 SEQUENCE /// ENTRY A60979 #type complete TITLE versican precursor - human ALTERNATE_NAMES chondroitin sulfate proteoglycan 2; chondroitin sulfate proteoglycan core protein, fibroblast; glial hyaluronate-binding protein; proteoglycan 24K core protein CONTAINS glial hyaluronate-binding protein ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S06014; S43921; A60979; A30358; A29348; A45131; I54179 REFERENCE S06014 !$#authors Zimmermann, D.R.; Ruoslahti, E. !$#journal EMBO J. (1989) 8:2975-2981 !$#title Multiple domains of the large fibroblast proteoglycan, !1versican. !$#cross-references MUID:90059882; PMID:2583089 !$#accession S06014 !'##molecule_type mRNA !'##residues 1-2409 ##label ZIM !'##cross-references GB:X15998; NID:g37662; PIDN:CAA34128.1; PID:g37663 REFERENCE S43921 !$#authors Yao, L.Y.; Moody, C.; Schoenherr, E.; Wight, T.N.; Sandell, !1L.J. !$#journal Matrix Biol. (1994) 14:213-225 !$#title Identification of the proteoglycan versican in aorta and !1smooth muscle cells by DNA sequence analysis, in situ !1hybridization and immunohistochemistry. !$#cross-references MUID:95005762; PMID:7921538 !$#accession S43921 !'##molecule_type mRNA !'##residues 208-440;1094-1385;1910-2246 ##label YAO REFERENCE A60979 !$#authors Bignami, A.; Lane, W.S.; Andrews, D.; Dahl, D. !$#journal Brain Res. Bull. (1989) 22:67-70 !$#title Structural similarity of hyaluronate binding proteins in !1brain and cartilage. !$#cross-references MUID:89229983; PMID:2469524 !$#accession A60979 !'##molecule_type protein !'##residues 171-210;289-303 ##label BIG REFERENCE A30358 !$#authors Perides, G.; Lane, W.S.; Andrews, D.; Dahl, D.; Bignami, A. !$#journal J. Biol. Chem. (1989) 264:5981-5987 !$#title Isolation and partial characterization of a glial !1hyaluronate-binding protein. !$#cross-references MUID:89174663; PMID:2466833 !$#accession A30358 !'##molecule_type protein !'##residues 24-50;80-87,'D',89-119;128-155;167-218;229-259, !1'IR';261-268;277-283,'G',285-305;328-329,'X',331-340 ##label !1PER REFERENCE A29348 !$#authors Krusius, T.; Gehlsen, K.R.; Ruoslahti, E. !$#journal J. Biol. Chem. (1987) 262:13120-13125 !$#title A fibroblast chondroitin sulfate proteoglycan core protein !1contains lectin-like and growth factor-like sequences. !$#cross-references MUID:88007514; PMID:2820964 !$#accession A29348 !'##molecule_type mRNA !'##residues 1725,'V',1727-2409 ##label KRU !'##cross-references GB:J02814 REFERENCE A45131 !$#authors Perides, G.; Rahemtulla, F.; Lane, W.S.; Asher, R.A.; !1Bignami, A. !$#journal J. Biol. Chem. (1992) 267:23883-23887 !$#title Isolation of a large aggregating proteoglycan from human !1brain. !$#cross-references MUID:93054750; PMID:1429726 !$#contents brain !$#accession A45131 !'##molecule_type protein !'##residues 21-22,'X',24-37 ##label PE2 !'##experimental_source brain !'##note sequence extracted from NCBI backbone (NCBIP:118884) REFERENCE I54179 !$#authors Iozzo, R.V.; Naso, M.F.; Cannizzaro, L.A.; Wasmuth, J.J.; !1McPherson, J.D. !$#journal Genomics (1992) 14:845-851 !$#title Mapping of the versican proteoglycan gene (CSPG2) to the !1long arm of human chromosome 5 (5q12-5q14). !$#cross-references MUID:93122792; PMID:1478664 !$#accession I54179 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 251-347 ##label RES !'##cross-references GB:S52488; NID:g263313; PIDN:AAB24878.1; !1PID:g263314 GENETICS !$#gene GDB:CSPG2 !'##cross-references GDB:127873; OMIM:118661 !$#map_position 5q12-5q14 CLASSIFICATION #superfamily versican; C-type lectin homology; complement !1factor H repeat homology; EGF homology; link protein repeat !1homology FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-2409 #product proteoglycan 24K core protein #status !8predicted #label MAT\ !$167-244 #domain link protein repeat homology #label LNK1\ !$265-346 #domain link protein repeat homology #label LNK2\ !$559-1654 #domain chondroitin sulfate attachment #status !8predicted #label GAG\ !$2106-2137 #domain EGF homology #label EG1\ !$2144-2175 #domain EGF homology #label EG2\ !$2182-2302 #domain C-type lectin homology #label LCH\ !$2309-2365 #domain complement factor H repeat homology #label !8FHD SUMMARY #length 2409 #molecular-weight 265048 #checksum 1473 SEQUENCE /// ENTRY A55535 #type complete TITLE versican precursor - mouse ALTERNATE_NAMES chondroitin sulfate proteoglycan 2; chondroitin sulfate proteoglycan core protein, fibroblast; glial hyaluronate-binding protein; proteoglycan 24K core protein; proteoglycan, PG-M/versican CONTAINS glial hyaluronate-binding protein ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A55535 REFERENCE A55535 !$#authors Ito, K.; Shinomura, T.; Zako, M.; Ujita, M.; Kimata, K. !$#journal J. Biol. Chem. (1995) 270:958-965 !$#title Multiple forms of mouse PG-M, a large chondroitin sulfate !1proteoglycan generated by alternative splicing. !$#cross-references MUID:95122551; PMID:7822336 !$#accession A55535 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-2397 ##label RES !'##cross-references GB:D16263; NID:g862460; PIDN:BAA03796.1; !1PID:g862461 CLASSIFICATION #superfamily versican; C-type lectin homology; complement !1factor H repeat homology; EGF homology; link protein repeat !1homology FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-1654 #domain versican #status predicted #label MAT\ !$167-244 #domain link protein repeat homology #label LNK1\ !$265-346 #domain link protein repeat homology #label LNK2\ !$2095-2126 #domain EGF homology #label EG1\ !$2133-2164 #domain EGF homology #label EG2\ !$2171-2291 #domain C-type lectin homology #label LCH\ !$2298-2354 #domain complement factor H repeat homology #label !8FHD SUMMARY #length 2397 #molecular-weight 262703 #checksum 6062 SEQUENCE /// ENTRY A39086 #type complete TITLE aggrecan precursor, cartilage long splice form [validated] - human ALTERNATE_NAMES chondroitin sulfate proteoglycan 1; large aggregating proteoglycan; proteoglycan core protein CONTAINS aggrecan cartilage short splice form ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 01-Dec-2000 #text_change 08-Dec-2000 ACCESSIONS A39086; S50206; A43919; S46659; S66389; S68646; S62786; !1A34226; B43919; C43919; S08042 REFERENCE A39086 !$#authors Doege, K.J.; Sasaki, M.; Kimura, T.; Yamada, Y. !$#journal J. Biol. Chem. (1991) 266:894-902 !$#title Complete coding sequence and deduced primary structure of !1the human cartilage large aggregating proteoglycan, !1aggrecan. Human-specific repeats, and additional !1alternatively spliced forms. !$#cross-references MUID:91093289; PMID:1985970 !$#accession A39086 !'##status preliminary !'##molecule_type mRNA !'##residues 1-2162,2201-2329,'A',2392-2415 ##label DOE !'##cross-references GB:M55172; NID:g178258; PIDN:AAA62824.1; !1PID:g178259 REFERENCE S50206 !$#authors Glumoff, V.; Savontaus, M.; Vehanen, J.; Vuorio, E. !$#journal Biochim. Biophys. Acta (1994) 1219:613-622 !$#title Analysis of aggrecan and tenascin gene expression in mouse !1skeletal tissues by Northern and in situ hybridization using !1species specific cDNA probes. !$#cross-references MUID:95035091; PMID:7524681 !$#accession S50206 !'##status preliminary !'##molecule_type mRNA !'##residues 350-497 ##label GLU !'##cross-references EMBL:X80278; NID:g516295 !'##note this translation is not annotated in GenBank entry HSAGGREC, !1release 113.0 REFERENCE A43919 !$#authors Sandy, J.D.; Flannery, C.R.; Neame, P.J.; Lohmander, L.S. !$#journal J. Clin. Invest. (1992) 89:1512-1516 !$#title The structure of aggrecan fragments in human synovial fluid. !1Evidence for the involvement in osteoarthritis of a novel !1proteinase which cleaves the Glu 373-Ala 374 bond of the !1interglobular domain. !$#cross-references MUID:92235266; PMID:1569188 !$#accession A43919 !'##molecule_type protein !'##residues 361-370,'X',372-373;393-399,'X',401-407,'X',409 ##label SAN !'##cross-references PIDN:AAB22079.1; PID:g248844; PIDN:AAB22077.1; !1PID:g248842; PIDN:AAB22078.1; PID:g248843 !'##experimental_source synovial fluid !'##note sequences modified after extraction from NCBI backbone REFERENCE I46998 !$#authors Barry, F.P.; Neame, P.J.; Sasse, J.; Pearson, D. !$#journal Matrix Biol. (1994) 14:323-328 !$#title Length variation in the keratan sulfate domain of mammalian !1aggrecan. !$#cross-references MUID:95128522; PMID:7827755 !$#accession S46659 !'##molecule_type DNA !'##residues 764-765,'A',767-846,'V',848-862,'X',864 ##label BAR !'##cross-references EMBL:S74659; NID:g807127; PIDN:AAC60643.1; !1PID:g807128 !'##note the authors translated the codon GAA for residue 803 as Ala and !1CYT for residue 863 as Pro REFERENCE S66389 !$#authors Ilic, M.Z.; Mok, M.T.; Williamson, O.D.; Campbell, M.A.; !1Hughes, C.E.; Handley, C.J. !$#journal Arch. Biochem. Biophys. (1995) 322:22-30 !$#title Catabolism of aggrecan by explant cultures of human !1articular cartilage in the presence of retinoic acid. !$#cross-references MUID:96004775; PMID:7574678 !$#accession S66389 !'##status preliminary !'##molecule_type protein !'##residues 17-23;24,'X',26-27;393-401;402-403 ##label ILI REFERENCE S68646 !$#authors Fosang, A.J.; Last, K.; Knaeuper, V.; Murphy, G.; Neame, !1P.J. !$#journal FEBS Lett. (1996) 380:17-20 !$#title Degradation of cartilage aggrecan by collagenase-3 (MMP-13). !$#cross-references MUID:96181659; PMID:8603731 !$#accession S68646 !'##status preliminary !'##molecule_type protein !'##residues 'V',404-405,'XX' ##label FOS REFERENCE S62786 !$#authors Dudhia, J.; Davidson, C.M.; Wells, T.M.; Vynios, D.H.; !1Hardingham, T.E.; Bayliss, M.T. !$#journal Biochem. J. (1996) 313:933-940 !$#title Age-related changes in the content of the C-terminal region !1of aggrecan in human articular cartilage. !$#cross-references MUID:96190740; PMID:8611178 !$#accession S62786 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type mRNA !'##residues 1778-1927,'A',1929-1963,'V',1965-2162,2201-2415 ##label DUD !'##cross-references EMBL:X17406; NID:g30248; PIDN:CAA35463.1; !1PID:g30249 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1990 REFERENCE A34226 !$#authors Baldwin, C.T.; Reginato, A.M.; Prockop, D.J. !$#journal J. Biol. Chem. (1989) 264:15747-15750 !$#title A new epidermal growth factor-like domain in the human core !1protein for the large cartilage-specific proteoglycan. !1Evidence for alternative splicing of the domain. !$#cross-references MUID:89380154; PMID:2789216 !$#accession A34226 !'##molecule_type mRNA !'##residues 1936-1963,'V',1965-2069,'A',2071-2415 ##label BAL !'##cross-references GB:J05062; NID:g181167; PIDN:AAA35726.1; !1PID:g181168 GENETICS !$#gene GDB:AGC1; CSPG1; CSPGCP; MSK16 !'##cross-references GDB:127479; OMIM:155760 !$#map_position 15q26-15q26 CLASSIFICATION #superfamily aggrecan; C-type lectin homology; complement !1factor H repeat homology; EGF homology; immunoglobulin !1homology; link protein repeat homology KEYWORDS alternative splicing; cartilage; chondroitin sulfate !1proteoglycan; extracellular matrix; glycoprotein; keratan !1sulfate FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-2415 #product aggrecan cartilage long splice form #status !8predicted #label MATL\ !$20-2162,2201-2415 #product aggrecan cartilage short splice form #status !8predicted #label MATM\ !$20-2162,2201-2329, !$'A',2392-2415 #product aggrecan short splice form #status predicted !8#label MATS\ !$44-135 #domain immunoglobulin homology #label IMM\ !$170-247 #domain link protein repeat homology #label LNK1\ !$268-349 #domain link protein repeat homology #label LNK2\ !$495-572 #domain link protein repeat homology #label LNK3\ !$593-673 #domain link protein repeat homology #label LNK4\ !$677-861 #domain keratan sulfate attachment #status predicted !8#label KSA\ !$864-1510 #domain chondroitin sulfate attachment #status !8predicted #label CS1\ !$1511-2162 #domain chondroitin sulfate attachment #status !8predicted #label CS2\ !$2168-2198 #domain EGF homology #label EGF\ !$2205-2325 #domain C-type lectin homology #label LCH\ !$2332-2388 #domain complement factor H repeat homology #label !8FHD\ !$126,239,333,387, !$434,602,657,737, !$1898 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$371,376 #binding_site keratan sulfate (Thr) (covalent) !8#status predicted SUMMARY #length 2415 #molecular-weight 250229 #checksum 6990 SEQUENCE /// ENTRY A55182 #type complete TITLE aggrecan precursor - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jan-2000 ACCESSIONS A55182; S55329; S50207; S51355; I78532; I58123 REFERENCE A55182 !$#authors Walcz, E.; Deak, F.; Erhardt, P.; Coulter, S.N.; Fueloep, !1C.; Horvath, P.; Doege, K.J.; Glant, T.T. !$#journal Genomics (1994) 22:364-371 !$#title Complete coding sequence, deduced primary structure, !1chromosomal localization, and structural analysis of murine !1aggrecan. !$#cross-references MUID:95104847; PMID:7806222 !$#accession A55182 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type mRNA !'##residues 1-2132 ##label WAL !'##cross-references GB:L07049; NID:g678541; PIDN:AAC37670.1; !1PID:g191772 REFERENCE S55329 !$#authors Watanabe, H.; Gao, L.; Sugiyama, S.; Doege, K.; Kimata, K.; !1Yamada, Y. !$#journal Biochem. J. (1995) 308:433-440 !$#title Mouse aggrecan, a large cartilage proteoglycan: protein !1sequence, gene structure and promoter sequence. !$#cross-references MUID:95289972; PMID:7772024 !$#accession S55329 !'##status preliminary !'##molecule_type mRNA !'##residues 1-567,'G',569-1728,'I',1730-2132 ##label WAT1 !'##cross-references GB:U22901; NID:g886014 REFERENCE S50206 !$#authors Glumoff, V.; Savontaus, M.; Vehanen, J.; Vuorio, E. !$#journal Biochim. Biophys. Acta (1994) 1219:613-622 !$#title Analysis of aggrecan and tenascin gene expression in mouse !1skeletal tissues by Northern and in situ hybridization using !1species specific cDNA probes. !$#cross-references MUID:95035091; PMID:7524681 !$#accession S50207 !'##molecule_type mRNA !'##residues 350-481,'R',483-506 ##label GLU1 !'##cross-references EMBL:X80279; NID:g673432 REFERENCE S51355 !$#authors Glumoff, V. !$#submission submitted to the EMBL Data Library, July 1994 !$#accession S51355 !'##status preliminary !'##molecule_type mRNA !'##residues 350-383,'CPVMSQRERPWAA' ##label GLU2 !'##cross-references EMBL:X80279 REFERENCE I58123 !$#authors Watanabe, H.; Kimata, K.; Line, S.; Strong, D.; Gao, L.Y.; !1Kozak, C.A.; Yamada, Y. !$#journal Nature Genet. (1994) 7:154-157 !$#title Mouse cartilage matrix deficiency (cmd) caused by a 7 bp !1deletion in the aggrecan gene. !$#cross-references MUID:95004579; PMID:7920633 !$#accession I78532 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 211-326 ##label WAT2 !'##cross-references GB:S73722; NID:g765215; PIDN:AAB32160.1; !1PID:g765216 !$#accession I58123 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 211-240,'MCTASLRRWRVRSFMRHPQRNSPSRRQPTS', !1'AGGWGHAWPPQASSTWPGRAVWTCAALAGW','RTAACATPSPRLGPTAGATSWV' !1##label WAT3 !'##cross-references GB:S73720; NID:g765211; PIDN:AAB32159.1; !1PID:g765212 GENETICS !$#map_position 7 !$#introns 253/1 CLASSIFICATION #superfamily aggrecan; C-type lectin homology; complement !1factor H repeat homology; EGF homology; immunoglobulin !1homology; link protein repeat homology KEYWORDS cartilage; extracellular matrix FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$44-135 #domain immunoglobulin homology #label IMM\ !$170-247 #domain link protein repeat homology #label LNK1\ !$268-349 #domain link protein repeat homology #label LNK2\ !$504-581 #domain link protein repeat homology #label LNK3\ !$602-683 #domain link protein repeat homology #label LNK4\ !$1922-2042 #domain C-type lectin homology #label LCH\ !$2049-2105 #domain complement factor H repeat homology #label !8FHD SUMMARY #length 2132 #molecular-weight 222007 #checksum 2721 SEQUENCE /// ENTRY I50421 #type complete TITLE aggrecan precursor - chicken ALTERNATE_NAMES cartilage chondroitin sulfate proteoglycan core protein ORGANISM #formal_name Gallus gallus #common_name chicken DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jan-2000 ACCESSIONS I50421; S39796; S27356; A25442; A32002; I50216; A37072; !1B37072 REFERENCE A48884 !$#authors Li, H.; Schwartz, N.B.; Vertel, B.M. !$#journal J. Biol. Chem. (1993) 268:23504-23511 !$#title cDNA cloning of chick cartilage chondroitin sulfate !1(aggrecan) core protein and identification of a stop codon !1in the aggrecan gene associated with the chondrodystrophy, !1nanomelia. !$#cross-references MUID:94043149; PMID:8226878 !$#accession I50421 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-2109 ##label LIX !'##cross-references GB:L21913; NID:g416133; PIDN:AAB19128.1; !1PID:g416134 REFERENCE S39796 !$#authors Chandrasekaran, L.; Tanzer, M.L. !$#journal Biochem. J. (1993) 296:885-887 !$#cross-references MUID:94107258; PMID:8280087 !$#contents annotation; erratum !$#accession S39796 !'##molecule_type mRNA !'##residues 1-361,'DL',364-600,'R',602-999,'R',1001-1028,'P',1030-1250, !1'D',1252-1602,'A',1604-1671,'G',1673-1795,'G',1797-1855, !11894-2109 ##label CHA1 !'##cross-references GB:M88101 REFERENCE S27356 !$#authors Chandrasekaran, L.; Tanzer, M.L. !$#journal Biochem. J. (1992) 288:903-910 !$#title Molecular cloning of chicken aggrecan. Structural analyses. !$#cross-references MUID:93111968; PMID:1339285 !$#accession S27356 !'##molecule_type mRNA !'##residues 1-361,'DL',364-600,'R',602-999,'R',1001-1028,'P',1030-1250, !1'D',1252-1549,'T',1551-1553,'T',1555-1560;'S',1562-1566, !1'VH',1689,'I',1691-1795,'G',1797-1855,1894-2109 ##label CHA2 !'##cross-references EMBL:M88101 REFERENCE A25442 !$#authors Sai, S.; Tanaka, T.; Kosher, R.A.; Tanzer, M.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:5081-5085 !$#title Cloning and sequence analysis of a partial cDNA for chicken !1cartilage proteoglycan core protein. !$#cross-references MUID:86259736; PMID:3460082 !$#accession A25442 !'##molecule_type mRNA !'##residues 1693-1795,'G',1797-1855,1894-2109 ##label SAI !'##cross-references GB:M13993; NID:g211654; PIDN:AAA48720.1; !1PID:g211655 !'##experimental_source sternal cartilage REFERENCE A32002 !$#authors Tanaka, T.; Har-El, R.; Tanzer, M.L. !$#journal J. Biol. Chem. (1988) 263:15831-15835 !$#title Partial structure of the gene for chicken cartilage !1proteoglycan core protein. !$#cross-references MUID:89008500; PMID:3170613 !$#accession A32002 !'##molecule_type DNA !'##residues 1893-1987,'S',1989-2022 ##label TAN !'##note the authors translated the codon TCC for residue 1787 as Phe REFERENCE I50216 !$#authors Krueger, R.C. !$#journal J. Biol. Chem. (1990) 265:12088-12097 !$#title Chick cartilage chondroitin sulfate proteoglycan core !1protein: II. Nucleotide sequence of cDNA clone and !1localization of the S103L epitope. !$#cross-references MUID:90307744; PMID:1694853 !$#accession I50216 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 'PA',1044-1559 ##label KRU !'##cross-references GB:M38187; NID:g211685; PIDN:AAA48731.1; !1PID:g555441 REFERENCE A37072 !$#authors Krueger Jr., R.C.; Fields, T.A.; Hildreth IV, J.; Schwartz, !1N.B. !$#journal J. Biol. Chem. (1990) 265:12075-12087 !$#title Chick cartilage chondroitin sulfate proteoglycan core !1protein. I. Generation and characterization of peptides and !1specificity for glycosaminoglycan attachment. !$#cross-references MUID:90307743; PMID:2365711 !$#accession A37072 !'##molecule_type protein !'##residues 998-1015,'X',1017-1019,'X',1021-1023 ##label KR2 !'##note amino end of 86K core peptide CS-A !$#accession B37072 !'##molecule_type protein !'##residues 1247-1250,'D',1252-1272,'X',1274-1275 ##label KR3 !'##note amino end of 75K core peptide CS-B CLASSIFICATION #superfamily aggrecan; C-type lectin homology; complement !1factor H repeat homology; EGF homology; immunoglobulin !1homology; link protein repeat homology KEYWORDS alternative splicing FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-2109 #product aggrecan #status predicted #label MAT\ !$44-131 #domain immunoglobulin homology #label IMM\ !$166-243 #domain link protein repeat homology #label LNK1\ !$264-346 #domain link protein repeat homology #label LNK2\ !$537-614 #domain link protein repeat homology #label LNK3\ !$635-716 #domain link protein repeat homology #label LNK4\ !$1859-1890 #domain EGF homology #label EGF\ !$1897-2017 #domain C-type lectin homology #label LCH\ !$2024-2080 #domain complement factor H repeat homology #label !8FHD SUMMARY #length 2109 #molecular-weight 223491 #checksum 7493 SEQUENCE /// ENTRY MMHUB1 #type complete TITLE laminin beta-1 chain precursor - human ALTERNATE_NAMES laminin chain B1 ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 19-Jan-2001 ACCESSIONS S13547; A28483; A26994; S23566 REFERENCE S13547 !$#authors Vuolteenaho, R.; Chow, L.T.; Tryggvason, K. !$#journal J. Biol. Chem. (1990) 265:15611-15616 !$#title Structure of the human laminin B1 chain gene. !$#cross-references MUID:90368768; PMID:1975589 !$#accession S13547 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1786 ##label VUO !'##cross-references GB:M61951; GB:J02778; NID:g186911; PIDN:AAA59486.1; !1PID:g186913 !'##note the nucleotide sequence was submitted to GenBank, February 1991 REFERENCE A28483 !$#authors Pikkarainen, T.; Eddy, R.; Fukushima, Y.; Byers, M.; Shows, !1T.; Pihlajaniemi, T.; Saraste, M.; Tryggvason, K. !$#journal J. Biol. Chem. (1987) 262:10454-10462 !$#title Human laminin B1 chain. A multidomain protein with gene !1(LAMB1) locus in the q22 region of chromosome 7. !$#cross-references MUID:87280097; PMID:3611077 !$#accession A28483 !'##molecule_type mRNA !'##residues 1-1786 ##label PIK !'##cross-references GB:M61951; GB:J02778; NID:g186911; PIDN:AAA59486.1; !1PID:g186913 REFERENCE A26994 !$#authors Jaye, M.; Modi, W.S.; Ricca, G.A.; Mudd, R.; Chiu, I.M.; !1O'Brien, S.J.; Drohan, W.N. !$#journal Am. J. Hum. Genet. (1987) 41:605-615 !$#title Isolation of a cDNA clone for the human laminin-B1 chain and !1its gene localization. !$#cross-references MUID:88021029; PMID:3661559 !$#accession A26994 !'##molecule_type mRNA !'##residues 1276-1469,'V',1471-1695,'G',1697-1709 ##label JAY !'##cross-references EMBL:M20206; NID:g186914; PIDN:AAA59487.1; !1PID:g186915 REFERENCE S23566 !$#authors Vuolteenaho, R.; Kallunki, T.; Chow, L.; Ikonen, J.; !1Pikkarainen, T.; Tryggvason, K. !$#book Extracellular Matrix Genes, Sandell L.J. and Boyd C.D., !1eds., pp. 175-193, Academic Press, San Diego, 1990 !$#title Genes for the human laminin B1 and B2 chains. !$#accession S23566 !'##molecule_type DNA !'##residues 762-1786 ##label VU2 !'##note mRNA was also sequenced GENETICS !$#gene GDB:LAMB1 !'##cross-references GDB:119357; OMIM:150240 !$#map_position 7q31.1-7q31.3 !$#introns 13/1; 71/3; 117/1; 141/3; 204/3; 226/1; 293/3; 334/1; 397/1; !1457/1; 494/3; 521/2; 566/3; 619/3; 662/2; 703/3; 772/1; 820/ !11; 897/2; 952/1; 1027/1; 1098/3; 1131/1; 1254/2; 1316/2; !11396/3; 1464/3; 1513/1; 1582/2; 1629/3; 1688/3; 1742/1 COMPLEX Laminins are trimers of an alpha-type, a beta-type, and a !1gamma-type laminin chain. FUNCTION !$#description interact with cells and with other basement membrane !1proteins to promote differentiation, development, and cell !1migration CLASSIFICATION #superfamily laminin beta-1 chain; laminin-type EGF-like !1homology KEYWORDS basement membrane; calcium binding; cell binding; coiled !1coil; extracellular matrix; glycoprotein; heterotrimer; !1nidogen binding FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-1786 #product laminin beta-1 chain #status predicted !8#label MAT\ !$22-270 #domain VI #label DOM6\ !$271-548 #domain V #label DOM5\ !$271-332 #domain laminin-type EGF-like homology #label LE01\ !$335-395 #domain laminin-type EGF-like homology #label LE02\ !$398-455 #domain laminin-type EGF-like homology #label LE03\ !$458-507 #domain laminin-type EGF-like homology #label LE04\ !$463-468 #region cell adhesion #status predicted\ !$510-540 #domain laminin-type EGF-like homology #status !8atypical #label LE05\ !$549-774 #domain IV #label DOM4\ !$662-668 #region cell adhesion #status predicted\ !$773-818 #domain laminin-type EGF-like homology #label LE06\ !$775-1178 #domain III #label DOM3\ !$821-864 #domain laminin-type EGF-like homology #label LE07\ !$867-914 #domain laminin-type EGF-like homology #label LE08\ !$917-973 #domain laminin-type EGF-like homology #label LE09\ !$923-927 #region cell adhesion #status predicted\ !$950-954 #region cell adhesion #status predicted\ !$976-1025 #domain laminin-type EGF-like homology #label LE10\ !$1028-1081 #domain laminin-type EGF-like homology #label LE11\ !$1084-1129 #domain laminin-type EGF-like homology #label LE12\ !$1132-1176 #domain laminin-type EGF-like homology #label LE13\ !$1179-1397 #domain II #label DOM2\ !$1179-1397 #region heptad repeats\ !$1398-1430 #domain alpha #label ALP\ !$1431-1786 #domain I #label DOM1\ !$1431-1786 #region heptad repeats\ !$30-35 #disulfide_bonds #status predicted\ !$120,356,519,677, !$965,1041,1195,1279, !$1336,1343,1487, !$1542,1643 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$1179,1182,1785 #disulfide_bonds interchain #status predicted SUMMARY #length 1786 #molecular-weight 198065 #checksum 9615 SEQUENCE /// ENTRY MMMSB1 #type complete TITLE laminin beta-1 chain precursor - mouse ALTERNATE_NAMES laminin chain B1 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 28-Feb-1986 #sequence_revision 30-Jun-1991 #text_change 10-Dec-1999 ACCESSIONS A26413; S02679; S05326; S14877; A02871; S02036; S13543 REFERENCE A26413 !$#authors Sasaki, M.; Kato, S.; Kohno, K.; Martin, G.R.; Yamada, Y. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:935-939 !$#title Sequence of the cDNA encoding the laminin B1 chain reveals a !1multidomain protein containing cysteine-rich repeats. !$#cross-references MUID:87147212; PMID:3493487 !$#accession A26413 !'##molecule_type mRNA !'##residues 1-1786 ##label SAS !'##cross-references EMBL:M15525; NID:g198700 !'##note translation in GenBank has additional 48 residues at the amino !1end REFERENCE S02678 !$#authors Fujiwara, S.; Shinkai, H.; Deutzmann, R.; Paulsson, M.; !1Timpl, R. !$#journal Biochem. J. (1988) 252:453-461 !$#title Structure and distribution of N-linked oligosaccharide !1chains on various domains of mouse tumour laminin. !$#cross-references MUID:88326259; PMID:2458101 !$#accession S02679 !'##molecule_type protein !'##residues 28-42;932-946 ##label FUJ REFERENCE S00624 !$#authors Hartl, L.; Oberbaeumer, I.; Deutzmann, R. !$#journal Eur. J. Biochem. (1988) 173:629-635 !$#title The N terminus of laminin A chain is homologous to the B !1chains. !$#cross-references MUID:88225080; PMID:3267223 !$#accession S05326 !'##molecule_type protein !'##residues 457-466;854-868;932-946 ##label HAR REFERENCE S08895 !$#authors Mann, K.; Deutzmann, R.; Timpl, R. !$#journal Eur. J. Biochem. (1988) 178:71-80 !$#title Characterization of proteolytic fragments of the !1laminin-nidogen complex and their activity in ligand-binding !1assays. !$#cross-references MUID:89078415; PMID:2462498 !$#accession S14877 !'##molecule_type protein !'##residues 590-620 ##label MAN REFERENCE A02870 !$#authors Barlow, D.P.; Green, N.M.; Kurkinen, M.; Hogan, B.L.M. !$#journal EMBO J. (1984) 3:2355-2362 !$#title Sequencing of laminin B chain cDNAs reveals C-terminal !1regions of coiled-coil alpha-helix. !$#cross-references MUID:85051302; PMID:6209134 !$#accession A02871 !'##molecule_type mRNA !'##residues 1292-1530,'MEMP',1535-1691,'C',1693-1748,'N',1750-1786 !1##label BAR !'##cross-references EMBL:X05212; NID:g52861; PIDN:CAA28839.1; !1PID:g809042 REFERENCE S01790 !$#authors Deutzmann, R.; Huber, J.; Schmetz, K.A.; Oberbaeumer, I.; !1Hartl, L. !$#journal Eur. J. Biochem. (1988) 177:35-45 !$#title Structural study of long arm fragments of laminin. Evidence !1for repetitive C-terminal sequences in the A-chain, not !1present in the B-chains. !$#cross-references MUID:89030693; PMID:3181157 !$#accession S02036 !'##molecule_type protein !'##residues 1561-1587 ##label DEU REFERENCE S13543 !$#authors Paulsson, M.; Deutzmann, R.; Timpl, R.; Dalzoppo, D.; !1Odermatt, E.; Engel, J. !$#journal EMBO J. (1985) 4:309-316 !$#title Evidence for coiled-coil alpha-helical regions in the long !1arm of laminin. !$#cross-references MUID:85257455; PMID:3848400 !$#accession S13543 !'##molecule_type protein !'##residues 1700-1748,'N',1750-1759 ##label PAU GENETICS !$#gene Lamb-1 !$#map_position 12 COMPLEX Laminins are trimers of an alpha-type, a beta-type, and a !1gamma-type laminin chain. FUNCTION !$#description interact with cells and with other basement membrane !1proteins to promote differentiation, development, and cell !1migration CLASSIFICATION #superfamily laminin beta-1 chain; laminin-type EGF-like !1homology KEYWORDS basement membrane; calcium binding; cell binding; coiled !1coil; extracellular matrix; glycoprotein; heterotrimer; !1nidogen binding; pyroglutamic acid FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-1786 #product laminin beta-1 chain #status predicted !8#label MAT\ !$22-270 #domain VI #label DOM6\ !$271-540 #domain V #label DOM5\ !$271-332 #domain laminin-type EGF-like homology #label LE01\ !$335-395 #domain laminin-type EGF-like homology #label LE02\ !$398-455 #domain laminin-type EGF-like homology #label LE03\ !$458-507 #domain laminin-type EGF-like homology #label LE04\ !$510-540 #domain laminin-type EGF-like homology #status !8atypical #label LE05\ !$541-772 #domain IV #label DOM4\ !$773-1182 #domain III #label DOM3\ !$773-818 #domain laminin-type EGF-like homology #label LE06\ !$821-864 #domain laminin-type EGF-like homology #label LE07\ !$867-914 #domain laminin-type EGF-like homology #label LE08\ !$917-973 #domain laminin-type EGF-like homology #label LE09\ !$976-1025 #domain laminin-type EGF-like homology #label LE10\ !$1028-1081 #domain laminin-type EGF-like homology #label LE11\ !$1084-1129 #domain laminin-type EGF-like homology #label LE12\ !$1132-1176 #domain laminin-type EGF-like homology #label LE13\ !$1183-1397 #domain II #label DOM2\ !$1183-1397 #region heptad repeats\ !$1398-1430 #domain alpha #label ALP\ !$1431-1786 #region heptad repeats\ !$1431-1786 #domain I #label DOM1\ !$22 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status predicted\ !$30-35 #disulfide_bonds #status predicted\ !$120,356,519,677, !$1041,1195,1279, !$1336,1343,1487, !$1533,1542,1643 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$1179,1182,1785 #disulfide_bonds interchain #status predicted SUMMARY #length 1786 #molecular-weight 196903 #checksum 7799 SEQUENCE /// ENTRY MMRTS #type complete TITLE laminin beta-2 chain precursor - rat ALTERNATE_NAMES laminin chain B3; S-laminin ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 10-Dec-1999 ACCESSIONS S03539 REFERENCE S03539 !$#authors Hunter, D.D.; Shah, V.; Merlie, J.P.; Sanes, J.R. !$#journal Nature (1989) 338:229-234 !$#title A laminin-like adhesive protein concentrated in the synaptic !1cleft of the neuromuscular junction. !$#cross-references MUID:89159410; PMID:2922051 !$#accession S03539 !'##molecule_type mRNA !'##residues 1-1801 ##label HUN !'##cross-references EMBL:X16563; NID:g57250; PIDN:CAA34561.1; !1PID:g57251 COMPLEX Laminins are trimers of an alpha-type, a beta-type, and a !1gamma-type laminin chain. FUNCTION !$#description interact with cells and with other basement membrane !1proteins to promote differentiation, development, and cell !1migration CLASSIFICATION #superfamily laminin beta-1 chain; laminin-type EGF-like !1homology KEYWORDS basement membrane; calcium binding; cell binding; coiled !1coil; extracellular matrix; glycoprotein; heterotrimer; !1nidogen binding FEATURE !$1-35 #domain signal sequence #status predicted #label SIG\ !$36-1801 #product laminin beta-2 chain #status predicted !8#label MAT\ !$36-285 #domain VI #label DOM6\ !$286-555 #domain V #label DOM5\ !$286-347 #domain laminin-type EGF-like homology #label LE01\ !$350-410 #domain laminin-type EGF-like homology #label LE02\ !$413-470 #domain laminin-type EGF-like homology #label LE03\ !$473-522 #domain laminin-type EGF-like homology #label LE04\ !$525-555 #domain laminin-type EGF-like homology #status !8atypical #label LE05\ !$556-784 #domain IV #label DOM4\ !$786-831 #domain laminin-type EGF-like homology #label LE06\ !$788-1196 #domain III #label DOM3\ !$834-877 #domain laminin-type EGF-like homology #label LE07\ !$880-927 #domain laminin-type EGF-like homology #label LE08\ !$930-986 #domain laminin-type EGF-like homology #label LE09\ !$989-1038 #domain laminin-type EGF-like homology #label LE10\ !$1041-1095 #domain laminin-type EGF-like homology #label LE11\ !$1098-1143 #domain laminin-type EGF-like homology #label LE12\ !$1146-1190 #domain laminin-type EGF-like homology #label LE13\ !$1197-1412 #domain II #label DOM2\ !$1197-1412 #region heptad repeats\ !$1413-1445 #domain alpha #label ALP\ !$1446-1801 #region heptad repeats\ !$1446-1801 #domain I #label DOM1\ !$45-50 #disulfide_bonds #status predicted\ !$251,371,1088,1252, !$1311,1351,1502 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$1193,1196,1800 #disulfide_bonds interchain #status predicted SUMMARY #length 1801 #molecular-weight 196472 #checksum 8852 SEQUENCE /// ENTRY MMFFB1 #type complete TITLE laminin beta-1 chain precursor - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES laminin chain B1 ORGANISM #formal_name Drosophila melanogaster DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 19-Jan-2001 ACCESSIONS A28783; S14462; B28783 REFERENCE A28783 !$#authors Montell, D.J.; Goodman, C.S. !$#journal Cell (1988) 53:463-473 !$#title Drosophila substrate adhesion molecule: sequence of laminin !1B1 chain reveals domains of homology with mouse. !$#cross-references MUID:88210471; PMID:3365769 !$#accession A28783 !'##molecule_type mRNA !'##residues 1-1790 ##label MON1 !'##cross-references EMBL:M19525 REFERENCE S14462 !$#authors Montell, D.J.; Goodman, C.S. !$#submission submitted to the EMBL Data Library, June 1988 !$#description Drosophila substrate adhesion molecule: sequence of laminin !1B1 chain reveals domains of homology with mouse. !$#accession S14462 !'##molecule_type mRNA !'##residues 1-667,'L',669-725,'VT',728-947,950-1790 ##label MON2 !'##cross-references EMBL:M19525; NID:g157801; PIDN:AAA28663.1; !1PID:g157802 GENETICS !$#gene lamB1 !'##cross-references FlyBase:FBgn0002527 !$#map_position 2L 28D COMPLEX Laminins are trimers of an alpha-type, a beta-type, and a !1gamma-type laminin chain. FUNCTION !$#description interact with cells and with other basement membrane !1proteins to promote differentiation, development, and cell !1migration CLASSIFICATION #superfamily laminin beta-1 chain; laminin-type EGF-like !1homology KEYWORDS basement membrane; calcium binding; cell binding; coiled !1coil; extracellular matrix; glycoprotein; heterotrimer; !1nidogen binding FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-1790 #product laminin beta-1 chain #status predicted !8#label MAT\ !$27-288 #domain VI #label DOM6\ !$289-561 #domain V #label DOM5\ !$290-354 #domain laminin-type EGF-like homology #label LE01\ !$357-417 #domain laminin-type EGF-like homology #label LE02\ !$420-477 #domain laminin-type EGF-like homology #label LE03\ !$480-528 #domain laminin-type EGF-like homology #label LE04\ !$531-561 #domain laminin-type EGF-like homology #status !8atypical #label LE05\ !$562-789 #domain IV #label DOM4\ !$643-645 #region cell attachment (R-G-D) motif\ !$790-1189 #domain III #label DOM3\ !$791-836 #domain laminin-type EGF-like homology #label LE06\ !$839-882 #domain laminin-type EGF-like homology #label LE07\ !$885-932 #domain laminin-type EGF-like homology #label LE08\ !$935-990 #domain laminin-type EGF-like homology #label LE09\ !$968-972 #region cell adhesion #status predicted\ !$993-1042 #domain laminin-type EGF-like homology #label LE10\ !$1045-1093 #domain laminin-type EGF-like homology #label LE11\ !$1096-1141 #domain laminin-type EGF-like homology #label LE12\ !$1144-1188 #domain laminin-type EGF-like homology #label LE13\ !$1190-1407 #domain II #label DOM2\ !$1408-1434 #domain alpha #label ALP\ !$1435-1790 #domain I #label DOM1\ !$51-56 #disulfide_bonds #status predicted\ !$140,203,234,489, !$593,1053,1248,1303, !$1332,1343,1475, !$1495,1517,1583, !$1646,1705 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$1191,1194,1788 #disulfide_bonds interchain #status predicted SUMMARY #length 1790 #molecular-weight 198665 #checksum 1641 SEQUENCE /// ENTRY MMHUB2 #type complete TITLE laminin gamma-1 chain precursor - human ALTERNATE_NAMES laminin chain B2 ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 10-Dec-1999 ACCESSIONS S13548; A28158; S13549; B34961; S14664; S23567 REFERENCE S13548 !$#authors Kallunki, T.; Ikonen, J.; Chow, L.T.; Kallunki, P.; !1Tryggvason, K. !$#journal J. Biol. Chem. (1991) 266:221-228 !$#title Structure of the human laminin B2 chain gene reveals !1extensive divergence from the laminin B1 chain gene. !$#cross-references MUID:91093128; PMID:1985895 !$#accession S13548 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1609 ##label KAL !'##cross-references GB:M55217; NID:g186937 !'##note the nucleotide sequence was submitted to GenBank, February 1991 REFERENCE A28158 !$#authors Pikkarainen, T.; Kallunki, T.; Tryggvason, K. !$#journal J. Biol. Chem. (1988) 263:6751-6758 !$#title Human laminin B2 chain. Comparison of the complete amino !1acid sequence with the B1 chain reveals variability in !1sequence homology between different structural domains. !$#cross-references MUID:88198245; PMID:3360804 !$#accession A28158 !'##molecule_type mRNA !'##residues 1-211,'I',213-1609 ##label PIK !'##cross-references EMBL:J03202; NID:g186916; PIDN:AAA59488.1; !1PID:g307107 REFERENCE S13549 !$#authors Fukushima, Y.; Pikkarainen, T.; Kallunki, T.; Eddy, R.L.; !1Byers, M.G.; Haley, L.L.; Henry, W.M.; Tryggvason, K.; !1Shows, T.B. !$#journal Cytogenet. Cell Genet. (1988) 48:137-141 !$#title Isolation of a human laminin B2 (LAMB2) cDNA clone and !1assignment of the gene to chromosome region 1q25->q31. !$#cross-references MUID:89169663; PMID:3234037 !$#accession S13549 !'##molecule_type mRNA !'##residues 1393-1609 ##label FUK !'##cross-references EMBL:M27654; NID:g186923; PIDN:AAA59489.1; !1PID:g186924 REFERENCE A34961 !$#authors Olsen, D.; Nagayoshi, T.; Fazio, M.; Peltonen, J.; Jaakkola, !1S.; Sanborn, D.; Sasaki, T.; Kuivaniemi, H.; Chu, M.L.; !1Deutzmann, R.; Timpl, R.; Uitto, J. !$#journal Lab. Invest. (1989) 60:772-782 !$#title Human laminin: cloning and sequence analysis of cDNAs !1encoding A, B1 and B2 chains, and expression of the !1corresponding genes in human skin and cultured cells. !$#cross-references MUID:89280632; PMID:2733383 !$#accession B34961 !'##molecule_type mRNA !'##residues 868-1551,'N',1553-1609 ##label OLS REFERENCE S14664 !$#authors Santos, C.L.S.; Sabbaga, J.; Brentani, R. !$#journal DNA Seq. (1991) 1:275-277 !$#title Differences in human laminin B2 sequences. !$#cross-references MUID:92216129; PMID:1806043 !$#accession S14664 !'##molecule_type mRNA !'##residues 1282-1609 ##label SAN !'##cross-references EMBL:X13939; NID:g34237; PIDN:CAA32122.1; !1PID:g34238 REFERENCE S23566 !$#authors Vuolteenaho, R.; Kallunki, T.; Chow, L.; Ikonen, J.; !1Pikkarainen, T.; Tryggvason, K. !$#book Extracellular Matrix Genes, Sandell L.J. and Boyd C.D., !1eds., pp. 175-193, Academic Press, San Diego, 1990 !$#title Genes for the human laminin B1 and B2 chains. !$#accession S23567 !'##molecule_type DNA !'##residues 801-1481,'R',1483-1609 ##label VUO !'##note mRNA was also sequenced GENETICS !$#gene GDB:LAMC1; LAMB2 !'##cross-references GDB:120136; OMIM:150290 !$#map_position 1q31-1q31 !$#introns 140/1; 241/3; 285/2; 341/1; 404/1; 443/2; 476/2; 522/1; 563/ !11; 626/2; 664/1; 738/1; 801/1; 883/1; 934/2; 982/1; 1041/3; !11094/1; 1162/3; 1189/2; 1235/2; 1283/3; 1333/3; 1372/1; !11438/3; 1491/3; 1525/1 COMPLEX Laminins are trimers of an alpha-type, a beta-type, and a !1gamma-type laminin chain. FUNCTION !$#description interact with cells and with other basement membrane !1proteins to promote differentiation, development, and cell !1migration CLASSIFICATION #superfamily laminin beta-1 chain; laminin-type EGF-like !1homology KEYWORDS basement membrane; calcium binding; cell binding; coiled !1coil; extracellular matrix; glycoprotein; heterotrimer; !1nidogen binding FEATURE !$1-33 #domain signal sequence #status predicted #label SIG\ !$34-1609 #product laminin gamma-1 chain #status predicted !8#label MAT\ !$34-285 #domain VI #label DOM6\ !$286-504 #domain V #label DOM5\ !$286-339 #domain laminin-type EGF-like homology #label LE01\ !$342-395 #domain laminin-type EGF-like homology #label LE02\ !$398-442 #domain laminin-type EGF-like homology #label LE03\ !$445-492 #domain laminin-type EGF-like homology #label LE04\ !$495-504 #domain laminin-type EGF-like homology #status !8atypical #label LE05\ !$505-689 #domain IV #label DOM4\ !$690-1034 #domain III #label DOM3\ !$690-721 #domain laminin-type EGF-like homology #status !8atypical #label LE06\ !$724-770 #domain laminin-type EGF-like homology #label LE07\ !$773-825 #domain laminin-type EGF-like homology #label LE08\ !$828-881 #domain laminin-type EGF-like homology #label LE09\ !$884-932 #domain laminin-type EGF-like homology #label LE10\ !$935-980 #domain laminin-type EGF-like homology #label LE11\ !$983-1028 #domain laminin-type EGF-like homology #label LE12\ !$1035-1609 #domain II/I #label DOM1\ !$1035-1609 #region heptad repeats\ !$40-50 #disulfide_bonds #status predicted\ !$60,134,576,650, !$1022,1107,1161, !$1175,1205,1223, !$1241,1380,1395,1439 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$1031,1034,1600 #disulfide_bonds interchain #status predicted SUMMARY #length 1609 #molecular-weight 177605 #checksum 793 SEQUENCE /// ENTRY MMMSB2 #type complete TITLE laminin gamma-1 chain precursor - mouse ALTERNATE_NAMES laminin chain B2 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 28-Feb-1986 #sequence_revision 30-Jun-1991 #text_change 10-Dec-1999 ACCESSIONS A28469; A27729; A28082; S02680; S05327; S02037; A02870; !1S13544; S14552 REFERENCE A28469 !$#authors Sasaki, M.; Yamada, Y. !$#journal J. Biol. Chem. (1987) 262:17111-17117 !$#title The laminin B2 chain has a multidomain structure homologous !1to the B1 chain. !$#cross-references MUID:88059118; PMID:3680290 !$#accession A28469 !'##molecule_type mRNA !'##residues 1-1607 ##label SAS !'##cross-references EMBL:J03484; NID:g198694; PIDN:AAA39405.1; !1PID:g293688 REFERENCE A27729 !$#authors Durkin, M.E.; Bartos, B.B.; Liu, S.H.; Phillips, S.L.; !1Chung, A.E. !$#journal Biochemistry (1988) 27:5198-5204 !$#title Primary structure of the mouse laminin B2 chain and !1comparison with laminin B1. !$#cross-references MUID:89000737; PMID:3167041 !$#accession A27729 !'##molecule_type mRNA !'##residues 1-263,'D',265-336,'C',338-446,'PS',449-661,'S',663-885, !1887-1155,1157-1433,'A',1435-1607 ##label DUR !'##cross-references EMBL:J02930; NID:g198702; PIDN:AAA39408.1; !1PID:g293691 !'##note the authors translated the codon TAT for residue 544 as Asp and !1GCG for residue 1434 as Val; the sequence given agrees with !1that shown in the GenBank entry REFERENCE A28082 !$#authors Ogawa, K.; Burbelo, P.D.; Sasaki, M.; Yamada, Y. !$#journal J. Biol. Chem. (1988) 263:8384-8389 !$#title The laminin B2 chain promoter contains unique repeat !1sequences and is active in transient transfection. !$#cross-references MUID:88228071; PMID:2836421 !$#accession A28082 !'##molecule_type DNA !'##residues 1-215,'A',217-239 ##label OGA !'##cross-references EMBL:J03749; NID:g198704; PIDN:AAA39409.1; !1PID:g554184 REFERENCE S02678 !$#authors Fujiwara, S.; Shinkai, H.; Deutzmann, R.; Paulsson, M.; !1Timpl, R. !$#journal Biochem. J. (1988) 252:453-461 !$#title Structure and distribution of N-linked oligosaccharide !1chains on various domains of mouse tumour laminin. !$#cross-references MUID:88326259; PMID:2458101 !$#accession S02680 !'##molecule_type protein !'##residues 227-238 ##label FUJ REFERENCE S00624 !$#authors Hartl, L.; Oberbaeumer, I.; Deutzmann, R. !$#journal Eur. J. Biochem. (1988) 173:629-635 !$#title The N terminus of laminin A chain is homologous to the B !1chains. !$#cross-references MUID:88225080; PMID:3267223 !$#accession S05327 !'##molecule_type protein !'##residues 227-238;387-393,'F',395-405;881-912;1022-1034 ##label HAR REFERENCE S01790 !$#authors Deutzmann, R.; Huber, J.; Schmetz, K.A.; Oberbaeumer, I.; !1Hartl, L. !$#journal Eur. J. Biochem. (1988) 177:35-45 !$#title Structural study of long arm fragments of laminin. Evidence !1for repetitive C-terminal sequences in the A-chain, not !1present in the B-chains. !$#cross-references MUID:89030693; PMID:3181157 !$#accession S02037 !'##molecule_type protein !'##residues 1362-1377,'X',1379-1392,'X',1394-1406 ##label DEU REFERENCE A02870 !$#authors Barlow, D.P.; Green, N.M.; Kurkinen, M.; Hogan, B.L.M. !$#journal EMBO J. (1984) 3:2355-2362 !$#title Sequencing of laminin B chain cDNAs reveals C-terminal !1regions of coiled-coil alpha-helix. !$#cross-references MUID:85051302; PMID:6209134 !$#accession A02870 !'##molecule_type mRNA !'##residues 1391-1474,'K',1476-1575,'N',1577-1607 ##label BAR !'##cross-references EMBL:X05211; NID:g52862; PIDN:CAA28838.1; !1PID:g817975 REFERENCE S13543 !$#authors Paulsson, M.; Deutzmann, R.; Timpl, R.; Dalzoppo, D.; !1Odermatt, E.; Engel, J. !$#journal EMBO J. (1985) 4:309-316 !$#title Evidence for coiled-coil alpha-helical regions in the long !1arm of laminin. !$#cross-references MUID:85257455; PMID:3848400 !$#accession S13544 !'##molecule_type protein !'##residues 1506-1523,'X',1525 ##label PAU REFERENCE A34961 !$#authors Olsen, D.; Nagayoshi, T.; Fazio, M.; Peltonen, J.; Jaakkola, !1S.; Sanborn, D.; Sasaki, T.; Kuivaniemi, H.; Chu, M.L.; !1Deutzmann, R.; Timpl, R.; Uitto, J. !$#journal Lab. Invest. (1989) 60:772-782 !$#title Human laminin: cloning and sequence analysis of cDNAs !1encoding A, B1 and B2 chains, and expression of the !1corresponding genes in human skin and cultured cells. !$#cross-references MUID:89280632; PMID:2733383 !$#accession S14552 !'##molecule_type protein !'##residues !1881-912;1022-1034;1364-1377;1379-1392;1394-1409;1506-1525; !11593-1606 ##label OLS GENETICS !$#gene Lamb-2 !$#map_position 1 !$#introns 138/1; 239/3 COMPLEX Laminins are trimers of an alpha-type, a beta-type, and a !1gamma-type laminin chain. FUNCTION !$#description interact with cells and with other basement membrane !1proteins to promote differentiation, development, and cell !1migration CLASSIFICATION #superfamily laminin beta-1 chain; laminin-type EGF-like !1homology KEYWORDS basement membrane; calcium binding; cell binding; coiled !1coil; extracellular matrix; glycoprotein; heterotrimer; !1nidogen binding FEATURE !$1-33 #domain signal sequence #status predicted #label SIG\ !$34-1607 #product laminin gamma-1 chain #status predicted !8#label MAT\ !$34-283 #domain VI #label DOM6\ !$284-502 #domain V #label DOM5\ !$284-337 #domain laminin-type EGF-like homology #status !8atypical #label LE01\ !$340-393 #domain laminin-type EGF-like homology #label LE02\ !$396-440 #domain laminin-type EGF-like homology #label LE03\ !$443-490 #domain laminin-type EGF-like homology #label LE04\ !$493-502 #domain laminin-type EGF-like homology #status !8atypical #label LE05\ !$503-687 #domain IV #label DOM4\ !$688-1032 #domain III #label DOM3\ !$688-719 #domain laminin-type EGF-like homology #status !8atypical #label LE06\ !$722-768 #domain laminin-type EGF-like homology #label LE07\ !$771-823 #domain laminin-type EGF-like homology #label LE08\ !$826-879 #domain laminin-type EGF-like homology #label LE09\ !$882-930 #domain laminin-type EGF-like homology #label LE10\ !$933-978 #domain laminin-type EGF-like homology #label LE11\ !$981-1026 #domain laminin-type EGF-like homology #label LE12\ !$1033-1607 #domain II/I #label DOM2\ !$1033-1607 #region heptad repeats\ !$38-48 #disulfide_bonds #status predicted\ !$58,132,574,648, !$1020,1105,1159, !$1173,1203,1221, !$1239,1437 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$1029,1032 #disulfide_bonds interchain #status predicted\ !$1378,1393 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$1598 #disulfide_bonds interchain (to chain B1) #status !8experimental SUMMARY #length 1607 #molecular-weight 177297 #checksum 2650 SEQUENCE /// ENTRY MMFFB2 #type complete TITLE laminin gamma-1 chain precursor - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES laminin chain B2 ORGANISM #formal_name Drosophila melanogaster DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jun-2000 ACCESSIONS A31483; A33737; S01733; A40502 REFERENCE A31483 !$#authors Chi, H.C.; Hui, C.F. !$#journal J. Biol. Chem. (1989) 264:1543-1550 !$#title Primary structure of the Drosophila laminin B2 chain and !1comparison with human, mouse, and Drosophila laminin B1 and !1B2 chains. !$#cross-references MUID:89109164; PMID:2912972 !$#accession A31483 !'##molecule_type mRNA !'##residues 1-1639 ##label CHI !'##cross-references EMBL:M25063; NID:g157803; PIDN:AAA28664.1; !1PID:g157804 REFERENCE A33737 !$#authors Montell, D.J.; Goodman, C.S. !$#journal J. Cell Biol. (1989) 109:2441-2453 !$#title Drosophila laminin: sequence of B2 subunit and expression of !1all three subunits during embryogenesis. !$#cross-references MUID:90037237; PMID:2808533 !$#accession A33737 !'##molecule_type mRNA !'##residues 1-39,'T',41-891,'L',893-1106,'T',1108-1459,'HV',1462-1581, !1'G',1583-1639 ##label MON !'##note 831-Tyr was also found REFERENCE S01733 !$#authors Chi, H.C.; Hui, C.F. !$#journal Nucleic Acids Res. (1988) 16:7205-7206 !$#title cDNA and amino acid sequences of Drosophila laminin B2 !1chain. !$#cross-references MUID:88303364; PMID:3405777 !$#accession S01733 !'##molecule_type mRNA !'##residues 344-1639 ##label CH2 !'##cross-references EMBL:X07806; NID:g8179; PIDN:CAA30665.1; !1PID:g1335618 !'##note the authors translated the codon GGC for residue 409 as Phe REFERENCE A40502 !$#authors Chi, H.C.; Juminaga, D.; Wang, S.Y.; Hui, C.F. !$#journal DNA Cell Biol. (1991) 10:451-466 !$#title Structure of the Drosophila gene for the laminin B2 chain. !$#cross-references MUID:91299161; PMID:1840513 !$#accession A40502 !'##molecule_type DNA !'##residues 1-891,'L',893-1639 ##label CH3 !'##cross-references GB:M58417; NID:g157805; PIDN:AAA28665.1; !1PID:g157806 GENETICS !$#gene lamB2 !'##cross-references FlyBase:FBgn0002528 !$#map_position 3L 67C !$#introns 65/3; 110/2; 153/1; 358/1; 495/2; 1357/2; 1469/3; 1570/1 COMPLEX Laminins are trimers of an alpha-type, a beta-type, and a !1gamma-type laminin chain. FUNCTION !$#description interact with cells and with other basement membrane !1proteins to promote differentiation, development, and cell !1migration CLASSIFICATION #superfamily laminin beta-1 chain; laminin-type EGF-like !1homology KEYWORDS basement membrane; calcium binding; cell binding; coiled !1coil; extracellular matrix; glycoprotein; heterotrimer; !1nidogen binding FEATURE !$1-33 #domain signal sequence #status predicted #label SIG\ !$34-1639 #product laminin gamma-1 chain #status predicted !8#label MAT\ !$34-297 #domain VI #label DOM6\ !$298-528 #domain V #label DOM5\ !$299-356 #domain laminin-type EGF-like homology #label LE01\ !$359-411 #domain laminin-type EGF-like homology #label LE02\ !$414-458 #domain laminin-type EGF-like homology #label LE03\ !$461-511 #domain laminin-type EGF-like homology #label LE04\ !$514-523 #domain laminin-type EGF-like homology #status !8atypical #label LE05\ !$529-705 #domain IV #label DOM4\ !$706-1057 #domain III #label DOM3\ !$710-741 #domain laminin-type EGF-like homology #status !8atypical #label LE06\ !$744-790 #domain laminin-type EGF-like homology #label LE07\ !$793-844 #domain laminin-type EGF-like homology #label LE08\ !$847-899 #domain laminin-type EGF-like homology #label LE09\ !$902-953 #domain laminin-type EGF-like homology #label LE10\ !$956-1001 #domain laminin-type EGF-like homology #label LE11\ !$1004-1047 #domain laminin-type EGF-like homology #label LE12\ !$1058-1639 #domain II/I #label DOM1\ !$1058-1639 #region heptad repeats\ !$57-67 #disulfide_bonds #status predicted\ !$115,147,376,669, !$862,965,1070,1156, !$1394,1479,1584 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$1050,1053,1631 #disulfide_bonds interchain #status predicted SUMMARY #length 1639 #molecular-weight 182322 #checksum 3649 SEQUENCE /// ENTRY MMMSA #type complete TITLE laminin alpha-1 chain precursor - mouse ALTERNATE_NAMES laminin chain A1 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 19-Jan-2001 ACCESSIONS A31771; A30449; S00624; A30450; S08895; S02678; S01790; !1A30451; S14670 REFERENCE A31771 !$#authors Sasaki, M.; Kleinman, H.K.; Huber, H.; Deutzmann, R.; !1Yamada, Y. !$#journal J. Biol. Chem. (1988) 263:16536-16544 !$#title Laminin, a multidomain protein. The A chain has a unique !1globular domain and homology with the basement membrane !1proteoglycan and the laminin B chains. !$#cross-references MUID:89034134; PMID:3182802 !$#accession A31771 !'##molecule_type mRNA !'##residues 1-3084 ##label SAS !'##cross-references EMBL:J04064; NID:g309419; PIDN:AAA39410.1; !1PID:g309420 !$#accession A30449 !'##molecule_type protein !'##residues 183-195;570-571,'A',573-586;596-612,'X',614-617, !1'EMK';630-646;1217-1222,'YPF', !11226-1227;1303-1310;1498-1507;2033-2040,'X', !12042-2043;2137-2151;2156-2178;2227-2240;2406-2420;2440-2451; !12481-2486;2624-2639;2818-2843;3009-3033,'V',3035 ##label SA2 REFERENCE S00624 !$#authors Hartl, L.; Oberbaeumer, I.; Deutzmann, R. !$#journal Eur. J. Biochem. (1988) 173:629-635 !$#title The N terminus of laminin A chain is homologous to the B !1chains. !$#cross-references MUID:88225080; PMID:3267223 !$#accession S00624 !'##molecule_type mRNA !'##residues 1-208,'T',210-334 ##label HAR !'##cross-references EMBL:X07737; NID:g52857; PIDN:CAA30561.1; !1PID:g52858 !$#accession A30450 !'##molecule_type protein !'##residues 311-335,'N',337-339;630-642,'D',644;692-734;737-748,'X', !1750-760,'G',762-763;765-769,'X',771,'H',773-778;780-786,'X', !1788-802;'Q',839-852,'Q',854-855,'QXQ',859-869,'Q', !1871-874;1148-1158;1353-1389;1449-1459 ##label HA2 !'##note the sequence from Fig. 7 is inconsistent with that from Fig. 5 !1in having 209-Ile, 239-Thr, and 240-Arg; the sequence from !1Fig. 7 is inconsistent with that from Table 1 in having !1335-Thr REFERENCE S08895 !$#authors Mann, K.; Deutzmann, R.; Timpl, R. !$#journal Eur. J. Biochem. (1988) 178:71-80 !$#title Characterization of proteolytic fragments of the !1laminin-nidogen complex and their activity in ligand-binding !1assays. !$#cross-references MUID:89078415; PMID:2462498 !$#accession S08895 !'##molecule_type protein !'##residues 153-169 ##label MAN REFERENCE S02678 !$#authors Fujiwara, S.; Shinkai, H.; Deutzmann, R.; Paulsson, M.; !1Timpl, R. !$#journal Biochem. J. (1988) 252:453-461 !$#title Structure and distribution of N-linked oligosaccharide !1chains on various domains of mouse tumour laminin. !$#cross-references MUID:88326259; PMID:2458101 !$#accession S02678 !'##molecule_type protein !'##residues 630-642,'D',644;2690-2704 ##label FUJ REFERENCE S01790 !$#authors Deutzmann, R.; Huber, J.; Schmetz, K.A.; Oberbaeumer, I.; !1Hartl, L. !$#journal Eur. J. Biochem. (1988) 177:35-45 !$#title Structural study of long arm fragments of laminin. Evidence !1for repetitive C-terminal sequences in the A-chain, not !1present in the B-chains. !$#cross-references MUID:89030693; PMID:3181157 !$#accession S01790 !'##molecule_type mRNA !'##residues 2538-3084 ##label DEU !'##cross-references EMBL:X13459; NID:g55499; PIDN:CAA31807.1; !1PID:g818014 !$#accession A30451 !'##molecule_type protein !'##residues 1911-1929;1997-2006;2033-2045,'X',2047-2054,'X',2056-2066, !1'X',2068-2105;2120-2170;2182-2192, !1'TR';2209-2216;2227-2240;2247-2251,'X', !12253-2266;2289-2298;2406-2420;2424-2435;2440-2451;2461-2470; !12487-2498;2502-2525;2538-2557;2561-2591,'X', !12593-2594;2600-2610;2616-2645;2648-2655;2690-2722;2754-2780; !12795-2805;2811-2816;2818-2834;2836-2843;2858-2875,'D', !12877-2913;2935-2964;2969-2976;2980-2993;2998-3005,'A', !13007-3033,'V',3035;3068-3083 ##label DE2 !'##note 2256-Val was also found REFERENCE A34961 !$#authors Olsen, D.; Nagayoshi, T.; Fazio, M.; Peltonen, J.; Jaakkola, !1S.; Sanborn, D.; Sasaki, T.; Kuivaniemi, H.; Chu, M.L.; !1Deutzmann, R.; Timpl, R.; Uitto, J. !$#journal Lab. Invest. (1989) 60:772-782 !$#title Human laminin: cloning and sequence analysis of cDNAs !1encoding A, B1 and B2 chains, and expression of the !1corresponding genes in human skin and cultured cells. !$#cross-references MUID:89280632; PMID:2733383 !$#accession S14670 !'##molecule_type protein !'##residues !12424-2436;2440-2451;2461-2467;2487-2525;2550-2557;2561-2593; !12600-2610;2616-2645;2648-2655;2690-2704;2707-2722;2754,'L', !12756-2780;2795-2805;2811-2816;2818-2844;2858-2904,'D', !12906-2913;2935-2942,'T', !12944-2964;2969-2976;2980-2993;2998-3000,'I',3002-3018,'V', !13020-3034;3068-3083 ##label OLS COMPLEX Laminins are trimers of an alpha-type, a beta-type, and a !1gamma-type laminin chain. FUNCTION !$#description interact with cells and with other basement membrane !1proteins to promote differentiation, development, and cell !1migration CLASSIFICATION #superfamily laminin alpha-1 chain; laminin G repeat !1homology; laminin-type EGF-like homology KEYWORDS basement membrane; calcium binding; cell binding; coiled !1coil; extracellular matrix; glycoprotein; heparin binding; !1heterotrimer; pyroglutamic acid FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-3084 #product laminin alpha-1 chain #status predicted !8#label MAT\ !$25-277 #domain VI #label DOM6\ !$277-331 #domain laminin-type EGF-like homology #label LE01\ !$278-519 #domain V #label DOM5\ !$334-401 #domain laminin-type EGF-like homology #label LE02\ !$404-458 #domain laminin-type EGF-like homology #label LE03\ !$461-507 #domain laminin-type EGF-like homology #label LE04\ !$510-519 #domain laminin-type EGF-like homology #status !8atypical #label LE05\ !$520-715 #domain IVb #label DO4B\ !$716-1166 #domain IIIb #label DO3B\ !$716-746 #domain laminin-type EGF-like homology #status !8atypical #label LE06\ !$749-795 #domain laminin-type EGF-like homology #label LE07\ !$798-853 #domain laminin-type EGF-like homology #label LE08\ !$830-834 #region cell adhesion #status predicted\ !$856-906 #domain laminin-type EGF-like homology #label LE09\ !$909-955 #domain laminin-type EGF-like homology #label LE10\ !$958-1002 #domain laminin-type EGF-like homology #label LE11\ !$1005-1048 #domain laminin-type EGF-like homology #label LE12\ !$1051-1094 #domain laminin-type EGF-like homology #label LE13\ !$1097-1116 #domain laminin-type EGF-like homology #status !8atypical #label LE14\ !$1118-1154 #domain laminin-type EGF-like homology #status !8atypical #label LE15\ !$1147-1149 #region cell attachment (R-G-D) motif\ !$1157-1166 #domain laminin-type EGF-like homology #status !8atypical #label LE16\ !$1167-1368 #domain IVa #label DO4A\ !$1369-1561 #domain IIIa #label DO3A\ !$1369-1407 #domain laminin-type EGF-like homology #status !8atypical #label LE17\ !$1410-1456 #domain laminin-type EGF-like homology #label LE18\ !$1459-1513 #domain laminin-type EGF-like homology #label LE19\ !$1516-1560 #domain laminin-type EGF-like homology #label LE20\ !$1562-2133 #domain II/I #label DOM2\ !$1562-2133 #region heptad repeats\ !$2134-3084 #domain G #label DOMG\ !$2150-2308 #domain laminin G repeat homology #label LG1\ !$2337-2492 #domain laminin G repeat homology #label LG2\ !$2518-2683 #domain laminin G repeat homology #label LG3\ !$2748-2897 #domain laminin G repeat homology #label LG4\ !$2925-3082 #domain laminin G repeat homology #label LG5\ !$25 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status predicted\ !$45,79,370,374,531, !$562,672,808,914, !$959,969,1052,1344, !$1414,1586,1603, !$1659,1686,1706, !$1718,1725,1763, !$1812,1902,1906, !$1936,1982,1993, !$2027,2046,2106, !$2251,2252,2356, !$2526,2738,2924 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$304-312 #disulfide_bonds #status experimental\ !$770,857,1999,2055, !$2067,2835 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$845,2102 #binding_site carbohydrate (Asn) (covalent) #status !8absent SUMMARY #length 3084 #molecular-weight 338169 #checksum 7032 SEQUENCE /// ENTRY MMHUMH #type fragment TITLE laminin alpha-2 chain - human (fragment) ALTERNATE_NAMES laminin M chain; merosin heavy chain ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1991 #sequence_revision 21-Aug-1998 #text_change 10-Dec-1999 ACCESSIONS PX0082; A35899; A38970; S14461 REFERENCE PX0082 !$#authors Hori, H.; Kanamori, T.; Mizuta, T.; Yamaguchi, N.; Liu, Y.; !1Nagai, Y. !$#journal J. Biochem. (1994) 116:1212-1219 !$#title Human laminin M chain: Epitope analysis of its monoclonal !1antibodies by immunoscreening of cDNA clones and tissue !1expression. !$#cross-references MUID:95221315; PMID:7535762 !$#accession PX0082 !'##molecule_type mRNA !'##residues 1-1751 ##label HOR !'##experimental_source placenta REFERENCE A35899 !$#authors Ehrig, K.; Leivo, I.; Argraves, W.S.; Ruoslahti, E.; !1Engvall, E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:3264-3268 !$#title Merosin, a tissue-specific basement membrane protein, is a !1laminin-like protein. !$#cross-references MUID:90238994; PMID:2185464 !$#accession A35899 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 'V',623-1751 ##label EHR1 !'##cross-references EMBL:M59832 !$#accession A38970 !'##molecule_type protein !'##residues 1368-1384;1389-1406;1593-1607 ##label EHR2 !'##note the sequence from Fig. 1 is inconsistent with that from Fig. 2 !1in lacking 1599-Val and 1601-Leu REFERENCE S14461 !$#authors Ehrig, K.; Leivo, I.; Argraves, S.W.; Ruoslahti, E.; !1Engvall, E. !$#submission submitted to the EMBL Data Library, December 1990 !$#description The tissue-specific basement membrane protein merosin is a !1laminin-like protein. !$#accession S14461 !'##molecule_type mRNA !'##residues 'V',623-1264,'R',1266-1751 ##label LEI !'##cross-references EMBL:M59832; NID:g187520; PIDN:AAA63215.1; !1PID:g187521 COMMENT This protein is a prominent component of the basement !1membrane that mediates a number of biological activities !1such as cell adhesion, growth, migration and !1differentiation. GENETICS !$#gene GDB:LAMA2; LAMM !'##cross-references GDB:132362; OMIM:156225 !$#map_position 6q22-6q23 COMPLEX Laminins are trimers of an alpha-type, a beta-type, and a !1gamma-type laminin chain. FUNCTION !$#description interact with cells and with other basement membrane !1proteins to promote differentiation, development, and cell !1migration CLASSIFICATION #superfamily laminin alpha-1 chain; laminin G repeat !1homology; laminin-type EGF-like homology KEYWORDS basement membrane; calcium binding; coiled coil; !1extracellular matrix; glycoprotein; heparin binding; !1heterotrimer; muscular dystrophy FEATURE !$21-58 #domain laminin-type EGF-like homology #status !8atypical #label LE01\ !$61-107 #domain laminin-type EGF-like homology #label LE02\ !$110-165 #domain laminin-type EGF-like homology #label LE03\ !$168-212 #domain laminin-type EGF-like homology #label LE04\ !$527-567,1071-1300 #region 3DM and 2D9 binding\ !$811-972 #domain laminin G repeat homology #label LG1\ !$1005-1165 #domain laminin G repeat homology #label LG2\ !$1191-1354 #domain laminin G repeat homology #label LG3\ !$1430-1578 #domain laminin G repeat homology #label LG4\ !$1605-1751 #domain laminin G repeat homology #label LG5\ !$120,238,255,341, !$451,542,557,561, !$658,669,686,767, !$881,1001,1076,1119, !$1192,1199,1289, !$1509,1534 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1751 #checksum 5535 SEQUENCE /// ENTRY S53868 #type complete TITLE laminin alpha-2 chain precursor - mouse ALTERNATE_NAMES laminin M chain; merosin heavy chain ORGANISM #formal_name Mus musculus #common_name house mouse DATE 21-Aug-1998 #sequence_revision 21-Aug-1998 #text_change 10-Dec-1999 ACCESSIONS I49077; S50829; I48655; S31576; S53868 REFERENCE I49077 !$#authors Bernier, S.M.; Utani, A.; Sugiyama, S.; Doi, T.; Polistina, !1C.; Yamada, Y. !$#journal Matrix Biol. (1995) 14:447-455 !$#title Cloning and expression of laminin alpha 2 chain (M-chain) in !1the mouse. !$#cross-references MUID:95316259; PMID:7795883 !$#accession I49077 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-3106 ##label RES !'##cross-references EMBL:U12147; NID:g699109; PIDN:AAC52165.1; !1PID:g699110 REFERENCE S50829 !$#authors Xu, H.; Wu, X.R.; Wewer, U.M.; Engvall, E. !$#journal Nature Genet. (1994) 8:297-302 !$#title Murine muscular dystrophy caused by a mutation in the !1laminin alpha-2 (Lama2) gene. !$#cross-references MUID:95179178; PMID:7874173 !$#accession S50829 !'##status preliminary !'##molecule_type mRNA !'##residues 64-281 ##label XUH !'##cross-references GB:S75315; NID:g833929; PIDN:AAB33573.1; !1PID:g833930 REFERENCE I48655 !$#authors Chang, A.C.; Wadsworth, S.; Coligan, J.E. !$#journal J. Immunol. (1993) 151:1789-1801 !$#title Expression of merosin in the thymus and its interaction with !1thymocytes. !$#cross-references MUID:93346725; PMID:8345183 !$#accession I48655 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 2162-2204,'D',2206-2213,'EY',2216-2279 ##label RE2 !'##cross-references EMBL:X69869; NID:g53055; PIDN:CAA49502.1; !1PID:g53056 COMPLEX Laminins are trimers of an alpha-type, a beta-type, and a !1gamma-type laminin chain. FUNCTION !$#description interact with cells and with other basement membrane !1proteins to promote differentiation, development, and cell !1migration CLASSIFICATION #superfamily laminin alpha-1 chain; laminin G repeat !1homology; laminin-type EGF-like homology KEYWORDS basement membrane; calcium binding; coiled coil; !1extracellular matrix; glycoprotein; heparin binding; !1heterotrimer FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-3106 #product laminin alpha-2 chain #status predicted !8#label MAT\ !$283-337 #domain laminin-type EGF-like homology #label LE01\ !$340-407 #domain laminin-type EGF-like homology #label LE02\ !$410-462 #domain laminin-type EGF-like homology #label LE03\ !$465-511 #domain laminin-type EGF-like homology #label LE04\ !$514-523 #domain laminin-type EGF-like homology #status !8atypical #label LE05\ !$720-750 #domain laminin-type EGF-like homology #label LE06\ !$753-800 #domain laminin-type EGF-like homology #label LE07\ !$803-858 #domain laminin-type EGF-like homology #label LE08\ !$861-911 #domain laminin-type EGF-like homology #label LE09\ !$914-960 #domain laminin-type EGF-like homology #label LE10\ !$963-1007 #domain laminin-type EGF-like homology #label LE11\ !$1010-1053 #domain laminin-type EGF-like homology #label LE12\ !$1056-1099 #domain laminin-type EGF-like homology #label LE13\ !$1102-1121 #domain laminin-type EGF-like homology #status !8atypical #label LE14\ !$1123-1159 #domain laminin-type EGF-like homology #status !8atypical #label LE15\ !$1162-1171 #domain laminin-type EGF-like homology #status !8atypical #label LE16\ !$1376-1413 #domain laminin-type EGF-like homology #status !8atypical #label LE17\ !$1416-1462 #domain laminin-type EGF-like homology #label LE18\ !$1465-1520 #domain laminin-type EGF-like homology #label LE19\ !$1523-1567 #domain laminin-type EGF-like homology #label LE20\ !$2166-2327 #domain laminin G repeat homology #label LG1\ !$2360-2520 #domain laminin G repeat homology #label LG2\ !$2546-2709 #domain laminin G repeat homology #label LG3\ !$2785-2933 #domain laminin G repeat homology #label LG4\ !$2960-3106 #domain laminin G repeat homology #label LG5 SUMMARY #length 3106 #molecular-weight 342675 #checksum 1656 SEQUENCE /// ENTRY S68960 #type complete TITLE laminin alpha-4 chain precursor - human ALTERNATE_NAMES laminin Ah ORGANISM #formal_name Homo sapiens #common_name man DATE 21-Aug-1998 #sequence_revision 21-Aug-1998 #text_change 16-Jun-2000 ACCESSIONS S68960; S65926; S49149; S40150; I53516 REFERENCE S68960 !$#authors Richards, A.; Al-Imara, L.; Pope, F.M. !$#journal Eur. J. Biochem. (1996) 238:813-821 !$#title The complete cDNA sequence of laminin alpha-4 and its !1relationship to the other human laminin alpha chains. !$#cross-references MUID:96300249; PMID:8706685 !$#accession S68960 !'##molecule_type mRNA !'##residues 1-1816 ##label RIC !'##cross-references EMBL:X91171; NID:g1212962; PIDN:CAA62596.1; !1PID:g1212963 !'##experimental_source tissue type heart REFERENCE I53516 !$#authors Iivanainen, A.; Sainio, K.; Sariola, H.; Tryggvason, K. !$#journal FEBS Lett. (1995) 365:183-188 !$#title Primary structure and expression of a novel human laminin !1alpha-4 chain. !$#cross-references MUID:95300971; PMID:7781776 !$#accession S65926 !'##molecule_type mRNA !'##residues 1-142,'P',144-177,'F',179-490,'Y',492-1056,'P',1058-1816 !1##label IIV !'##cross-references EMBL:S78569; NID:g1042081; PIDN:AAB34635.1; !1PID:g1042082 REFERENCE S49149 !$#authors Richards, A.J.; Al-Imara, L.; Carter, N.; Leversha, M.; !1Lloyd, J.C.; Pope, F.M. !$#submission submitted to the EMBL Data Library, December 1993 !$#description Localisation of the gene (LAMA4) to chromosome 6q21 and !1isolation of a partial cDNA encoding a variant laminin A !1chain. !$#accession S49149 !'##molecule_type mRNA !'##residues 236-1816 ##label RI2 !'##cross-references EMBL:X76939; NID:g509805; PIDN:CAA54258.1; !1PID:g509806 REFERENCE S40150 !$#authors Richards, A.J.; Al-Imara, L.; Carter, N.; Lloyd, J.C.; Pope, !1F.M. !$#submission submitted to the EMBL Data Library, February 1993 !$#description Isolation of a partial cDNA encoding a protein homologous to !1laminin A. Assignment of the gene to chromosome 6. !$#accession S40150 !'##molecule_type mRNA !'##residues 1403-1541,'S',1543-1816 ##label RI3 !'##cross-references EMBL:X70904; NID:g437804; PIDN:CAA50261.1; !1PID:g437805 GENETICS !$#gene GDB:LAMA4; LAMA3 !'##cross-references GDB:203904; OMIM:600133 !$#map_position 6q21-6q21 COMPLEX Laminins are trimers of an alpha-type, a beta-type, and a !1gamma-type laminin chain. FUNCTION !$#description interact with cells and with other basement membrane !1proteins to promote differentiation, development, and cell !1migration CLASSIFICATION #superfamily laminin alpha-4 chain; laminin G repeat !1homology; laminin-type EGF-like homology KEYWORDS basement membrane; cell binding; coiled coil; extracellular !1matrix; glycoprotein; heterotrimer FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-1816 #product laminin alpha-4 chain #status predicted !8#label MAT\ !$82-129 #domain laminin-type EGF-like homology #label LE1\ !$132-184 #domain laminin-type EGF-like homology #label LE2\ !$187-238 #domain laminin-type EGF-like homology #label LE3\ !$241-265 #domain laminin-type EGF-like homology #status !8atypical #label LE4\ !$717-719 #region cell attachment (R-G-D) motif\ !$862-1031 #domain laminin G repeat homology #label LG1\ !$1068-1223 #domain laminin G repeat homology #label LG2\ !$1252-1398 #domain laminin G repeat homology #label LG3\ !$1488-1636 #domain laminin G repeat homology #label LG4\ !$1665-1816 #domain laminin G repeat homology #label LG5\ !$104,215,308,458, !$524,550,571,574, !$631,639,735,751, !$754,780,803,1086, !$1281,1359,1411 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$266,269 #disulfide_bonds interchain #status predicted SUMMARY #length 1816 #molecular-weight 201882 #checksum 8148 SEQUENCE /// ENTRY MMHUND #type complete TITLE nidogen precursor - human ALTERNATE_NAMES entactin ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 20-Oct-2000 ACCESSIONS A33322; A32437; A61367 REFERENCE A33322 !$#authors Nagayoshi, T.; Sanborn, D.; Hickok, N.J.; Olsen, D.R.; !1Fazio, M.J.; Chu, M.L.; Knowlton, R.; Mann, K.; Deutzmann, !1R.; Timpl, R.; Uitto, J. !$#journal DNA (1989) 8:581-594 !$#title Human nidogen: complete amino acid sequence and structural !1domains deduced from cDNAs, and evidence for polymorphism of !1the gene. !$#cross-references MUID:90091745; PMID:2574658 !$#accession A33322 !'##molecule_type mRNA !'##residues 1-1247 ##label NAG !'##cross-references EMBL:M30269 REFERENCE A32437 !$#authors Olsen, D.R.; Nagayoshi, T.; Fazio, M.; Mattei, M.G.; !1Passage, E.; Weil, D.; Timpl, R.; Chu, M.L.; Uitto, J. !$#journal Am. J. Hum. Genet. (1989) 44:876-885 !$#title Human nidogen: cDNA cloning, cellular expression, and !1mapping of the gene to chromosome Iq43. !$#cross-references MUID:89270475; PMID:2471408 !$#accession A32437 !'##molecule_type mRNA !'##residues 667-1247 ##label OLS !'##cross-references EMBL:M27445; NID:g602466; PIDN:AAA57261.1; !1PID:g602467 !'##note the authors translated the codon AAG for residue 966 as Cys REFERENCE A61367 !$#authors Fazio, M.J.; O'Leary, J.; Kaehaeri, V.M.; Chen, Y.Q.; !1Saitta, B.; Uitto, J. !$#journal J. Invest. Dermatol. (1991) 97:281-285 !$#title Human nidogen gene: structural and functional !1characterization of the 5'-flanking region. !$#cross-references MUID:91302882; PMID:1906509 !$#accession A61367 !'##molecule_type DNA !'##residues 1-28 ##label FAZ COMMENT This protein is a basement membrane glycoprotein that forms !1a complex with laminin and also type-IV collagen. GENETICS !$#gene GDB:NID !'##cross-references GDB:120236; OMIM:131390 !$#map_position 1q43-1q43 CLASSIFICATION #superfamily nidogen; EGF homology; LDL receptor !1YWTD-containing repeat homology; thyroglobulin type I repeat !1homology KEYWORDS basement membrane; beta-hydroxyasparagine; calcium binding; !1cell binding; collagen binding; disulfide bond; !1extracellular matrix; fibronectin binding; glycoprotein; !1laminin binding; sulfoprotein FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-1247 #product nidogen #status predicted #label MAT\ !$390-425 #domain EGF homology #label EG1\ !$672-708 #domain EGF homology #label EG2\ !$702-704 #region cell attachment (R-G-D) motif\ !$714-750 #domain EGF homology #label EG3\ !$762-800 #domain EGF homology #label EG4\ !$806-839 #domain EGF homology #label EG5\ !$849-919 #domain thyroglobulin type I repeat homology #label !8THY1\ !$990-1032 #domain LDL receptor YWTD-containing repeat homology !8#label YW1\ !$1033-1075 #domain LDL receptor YWTD-containing repeat homology !8#label YW2\ !$1076-1120 #domain LDL receptor YWTD-containing repeat homology !8#label YW3\ !$1121-1160 #domain LDL receptor YWTD-containing repeat homology !8#label YW4\ !$1161-1197 #domain LDL receptor YWTD-containing repeat homology !8#label YW5\ !$1212-1243 #domain EGF homology #label EG6\ !$289,296 #binding_site sulfate (Tyr) (covalent) #status !8predicted\ !$729,819 #modified_site erythro-beta-hydroxyasparagine (Asn) !8#status predicted\ !$756 #cross-link isopeptide (Gln) (interchain to Lys !8N6-amino of laminin) #status predicted\ !$1137 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1247 #molecular-weight 136418 #checksum 9659 SEQUENCE /// ENTRY MMMSND #type complete TITLE nidogen precursor - mouse ALTERNATE_NAMES entactin ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 20-Oct-2000 ACCESSIONS S02730; A38788; PN0669; S03637; A38789; S14878; S14836; !1A42785; A57168; A32133 REFERENCE S02730 !$#authors Durkin, M.E.; Chakravarti, S.; Bartos, B.B.; Liu, S.H.; !1Friedman, R.L.; Chung, A.E. !$#journal J. Cell Biol. (1988) 107:2749-2756 !$#title Amino acid sequence and domain structure of entactin. !1Homology with epidermal growth factor precursor and low !1density lipoprotein receptor. !$#cross-references MUID:89079780; PMID:3264556 !$#accession S02730 !'##molecule_type mRNA !'##residues 1-1245 ##label DUR !'##cross-references EMBL:X14194; NID:g50838; PIDN:CAA32408.1; !1PID:g50839 !$#accession A38788 !'##molecule_type protein !'##residues 29-30,'X',32-40 ##label DU2 REFERENCE PN0669 !$#authors Durkin, M.E.; Liu, S.H.; Reing, J.; Chung, A.E. !$#journal Gene (1993) 132:261-266 !$#title Characterization of the 5' end of the mouse Ent gene !1encoding the basement membrane protein, entactin. !$#cross-references MUID:94040771; PMID:8224873 !$#accession PN0669 !'##molecule_type DNA !'##residues 1-251 ##label DU3 !'##cross-references GB:L17322; GB:L17323; GB:L17324; NID:g410235; !1PIDN:AAA77652.1; PID:g995952 REFERENCE S03637 !$#authors Mann, K.; Deutzmann, R.; Aumailley, M.; Timpl, R.; Raimondi, !1L.; Yamada, Y.; Pan, T.; Conway, D.; Chu, M.L. !$#journal EMBO J. (1989) 8:65-72 !$#title Amino acid sequence of mouse nidogen, a multidomain basement !1membrane protein with binding activity for laminin, collagen !1IV and cells. !$#cross-references MUID:89231638; PMID:2496973 !$#accession S03637 !'##molecule_type mRNA !'##residues 1-169,'L',171-658,'K',660-966,'A',968-1245 ##label MAN !'##cross-references EMBL:X14480; NID:g53383; PIDN:CAA32642.1; !1PID:g53384 !$#accession A38789 !'##molecule_type protein !'##residues 29-53;130-167,'G',169-170,'V',172-173,'A', !1175;210-223;225-240;252-295;318-336;350-357;379-387;403-410; !1413-414;416-421;467-480;517-528;554-565;605-610;649-658,'R', !1660-694;701-733;739-753;755-761;773-796;809-836;879-902; !1955-959;969-976;990-993;1003-1098;1100-1122;1131-1141; !11144-1167;1182-1185;1187;1193-1206;1208-1218;1220-1226; !11232-1244 ##label MA1 REFERENCE S08895 !$#authors Mann, K.; Deutzmann, R.; Timpl, R. !$#journal Eur. J. Biochem. (1988) 178:71-80 !$#title Characterization of proteolytic fragments of the !1laminin-nidogen complex and their activity in ligand-binding !1assays. !$#cross-references MUID:89078415; PMID:2462498 !$#accession S14878 !'##molecule_type protein !'##residues 29-49;329-336,'F',338;649-694, !1'X';809-836;1003-1065;1066-1093 ##label MA2 REFERENCE S14836 !$#authors Paulsson, M.; Deutzmann, R.; Dziadek, M.; Nowack, H.; Timpl, !1R.; Weber, S.; Engel, J. !$#journal Eur. J. Biochem. (1986) 156:467-478 !$#title Purification and structural characterization of intact and !1fragmented nidogen obtained from a tumor basement membrane. !$#cross-references MUID:86192477; PMID:3084254 !$#accession S14836 !'##molecule_type protein !'##residues 29-38;232-240;326-330,'A',332-335;379-387,'N';649-658 !1##label PAU !'##note 328-Gly was also found REFERENCE A42785 !$#authors Aeschlimann, D.; Paulsson, M.; Mann, K. !$#journal J. Biol. Chem. (1992) 267:11316-11321 !$#title Identification of Gln(726) in nidogen as the amine acceptor !1in transglutaminase-catalyzed cross-linking of !1laminin-nidogen complexes. !$#cross-references MUID:92283840; PMID:1350783 !$#accession A42785 !'##status preliminary !'##molecule_type protein !'##residues 350-369;660-671;746-772 ##label AES REFERENCE A57168 !$#authors Durkin, M.E.; Wewer, U.M.; Chung, A.E. !$#journal Genomics (1995) 26:219-228 !$#title Exon organization of the mouse entactin gene corresponds to !1the structural domains of the polypeptide and has regional !1homology to the low-density lipoprotein receptor gene. !$#cross-references MUID:95324912; PMID:7601446 !$#accession A57168 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 252-966,'A',968-1205,'Q',1206-1245 ##label DU4 !'##cross-references GB:X83041; GB:X83042; GB:X83043; GB:X83078; !1GB:X83079; GB:X83080; GB:X83081; GB:X83082; GB:X83083; !1GB:X83084; GB:X83085; GB:X83086; GB:X83087; GB:X83088; !1GB:X83089; GB:X83090; GB:X83091; GB:X83092; GB:X83093 COMMENT This protein is a basement membrane glycoprotein that forms !1a complex with laminin and also type-IV collagen. GENETICS !$#gene ENT; Nid !$#map_position 13 CLASSIFICATION #superfamily nidogen; EGF homology; LDL receptor !1YWTD-containing repeat homology; thyroglobulin type I repeat !1homology KEYWORDS basement membrane; beta-hydroxyasparagine; calcium binding; !1cell binding; collagen binding; disulfide bond; !1extracellular matrix; fibronectin binding; glycoprotein; !1laminin binding; sulfoprotein FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-1245 #product nidogen #status experimental #label MAT\ !$43-54 #domain calcium binding #status predicted #label CA1\ !$278-289 #domain calcium binding #status predicted #label CA2\ !$388-423 #domain EGF homology #label EG1\ !$670-706 #domain EGF homology #label EG2\ !$700-702 #region cell attachment (R-G-D) motif\ !$712-748 #domain EGF homology #label EG3\ !$760-798 #domain EGF homology #label EG4\ !$804-837 #domain EGF homology #label EG5\ !$847-917 #domain thyroglobulin type I repeat homology #label !8THY1\ !$988-1030 #domain LDL receptor YWTD-containing repeat homology !8#label YW1\ !$1031-1073 #domain LDL receptor YWTD-containing repeat homology !8#label YW2\ !$1074-1118 #domain LDL receptor YWTD-containing repeat homology !8#label YW3\ !$1119-1158 #domain LDL receptor YWTD-containing repeat homology !8#label YW4\ !$1159-1195 #domain LDL receptor YWTD-containing repeat homology !8#label YW5\ !$1210-1241 #domain EGF homology #label EG6\ !$187 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$290,295 #binding_site sulfate (Tyr) (covalent) #status !8predicted\ !$415 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$727,817 #modified_site erythro-beta-hydroxyasparagine (Asn) !8#status predicted\ !$754 #cross-link isopeptide (Gln) (interchain to Lys !8N6-amino of laminin) #status experimental SUMMARY #length 1245 #molecular-weight 136622 #checksum 9267 SEQUENCE /// ENTRY S31213 #type complete TITLE nidogen precursor - sea squirt (Halocynthia roretzi) ALTERNATE_NAMES entactin ORGANISM #formal_name Halocynthia roretzi DATE 30-Sep-1993 #sequence_revision 27-Feb-1997 #text_change 16-Jun-2000 ACCESSIONS S31213 REFERENCE S31213 !$#authors Nakae, H.; Sugano, M.; Ishimori, Y.; Endo, T.; Obinata, T. !$#journal Eur. J. Biochem. (1993) 213:11-19 !$#title Ascidian entactin/nidogen. Implication of evolution by !1shuffling two kinds of cysteine-rich motifs. !$#cross-references MUID:93238676; PMID:8477687 !$#accession S31213 !'##molecule_type mRNA !'##residues 1-1161 ##label NAK !'##cross-references EMBL:D14038; NID:g217363; PIDN:BAA03127.1; !1PID:g217364 CLASSIFICATION #superfamily Ascidian nidogen; EGF homology; LDL receptor !1YWTD-containing repeat homology; thyroglobulin type I repeat !1homology KEYWORDS basement membrane; collagen binding; disulfide bond; !1duplication; extracellular matrix; fibronectin binding; !1glycoprotein; laminin binding; tandem repeat FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-1161 #product nidogen #status predicted #label MAT\ !$274-306 #domain EGF homology #label EG1\ !$560-574 #region 3-residue repeats (R-P-V)\ !$603-673 #domain thyroglobulin type I repeat homology #label !8THY1\ !$686-748 #domain thyroglobulin type I repeat homology #label !8THY2\ !$752-819 #domain thyroglobulin type I repeat homology #label !8THY3\ !$900-943 #domain LDL receptor YWTD-containing repeat homology !8#label YW1\ !$944-986 #domain LDL receptor YWTD-containing repeat homology !8#label YW2\ !$987-1031 #domain LDL receptor YWTD-containing repeat homology !8#label YW3\ !$1032-1075 #domain LDL receptor YWTD-containing repeat homology !8#label YW4\ !$1076-1114 #domain LDL receptor YWTD-containing repeat homology !8#label YW5\ !$1129-1158 #domain EGF homology #label EG2\ !$107,334,360,484 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1161 #molecular-weight 128471 #checksum 3556 SEQUENCE /// ENTRY MMBOLM #type complete TITLE lens fiber membrane major intrinsic protein - bovine ALTERNATE_NAMES lens fiber membrane intrinsic 26K protein (MIP); MP26 CONTAINS MP22 ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 22-Jun-1999 ACCESSIONS A23251; B23251; A22444 REFERENCE A23251 !$#authors Gorin, M.B.; Yancey, S.B.; Cline, J.; Revel, J.P.; Horwitz, !1J. !$#journal Cell (1984) 39:49-59 !$#title The major intrinsic protein (MIP) of the bovine lens fiber !1membrane: characterization and structure based on cDNA !1cloning. !$#cross-references MUID:85024900; PMID:6207938 !$#accession A23251 !'##molecule_type mRNA !'##residues 1-263 ##label GOR !'##cross-references GB:K02818; NID:g163296; PIDN:AAA30622.1; !1PID:g163297 !$#accession B23251 !'##molecule_type protein !'##residues 1-39 ##label GO2 REFERENCE A22444 !$#authors Ngoc, L.D.; Paroutaud, P.; Dunia, I.; Benedetti, E.L.; !1Hoebeke, J. !$#journal FEBS Lett. (1985) 181:74-78 !$#title Sequence analysis of peptide fragments from the intrinsic !1membrane protein of calf lens fibers MP26 and its natural !1maturation product MP22. !$#cross-references MUID:85127500; PMID:3882455 !$#accession A22444 !'##molecule_type protein !'##residues 1-13,'L',15-28,'R',30,'F',32,'L';184-214 ##label NGO COMMENT This protein is the major component of lens fiber gap !1junctions. CLASSIFICATION #superfamily lens fiber membrane major intrinsic protein KEYWORDS eye lens; gap junction; phosphoprotein; transmembrane !1protein FEATURE !$12-28 #domain transmembrane #status predicted #label TM1\ !$44-60 #domain transmembrane #status predicted #label TM2\ !$87-103 #domain transmembrane #status predicted #label TM3\ !$130-146 #domain transmembrane #status predicted #label TM4\ !$160-176 #domain transmembrane #status predicted #label TM5 SUMMARY #length 263 #molecular-weight 28223 #checksum 2782 SEQUENCE /// ENTRY AGRT #type complete TITLE agrin - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 17-Nov-2000 ACCESSIONS JH0399; A38856 REFERENCE JH0399 !$#authors Rupp, F.; Payan, D.G.; Magill-Solc, C.; Cowan, D.M.; !1Scheller, R.H. !$#journal Neuron (1991) 6:811-823 !$#title Structure and expression of a rat agrin. !$#cross-references MUID:91222570; PMID:1851019 !$#accession JH0399 !'##molecule_type mRNA !'##residues 1-1779;1799-1959 ##label RUP !'##cross-references GB:M64780; NID:g202798; PIDN:AAA40703.1; !1PID:g202800 !'##experimental_source embryonic spinal cord !'##note it is uncertain whether Met-1, Met-18, or Met-24 is the !1initiator REFERENCE A38856 !$#authors Rupp, F.; Oezcelik, T.; Linial, M.; Peterson, K.; Francke, !1U.; Scheller, R. !$#journal J. Neurosci. (1992) 12:3535-3544 !$#title Structure and chromosomal localization of the mammalian !1agrin gene. !$#cross-references MUID:92407628; PMID:1326608 !$#accession A38856 !'##molecule_type mRNA !'##residues 1780-1798 ##label RU2 !'##cross-references GB:S44194 COMMENT This protein mediates the motor neuron-induced aggregation !1of acetylcholine receptors and acetylcholine-esterase on the !1surface of muscle fibers of the neuromuscular junction. COMMENT 90% of rat embryonic transcripts encode the variant labeled !1below as form 3. However, alternative splicing may produce !1as many as eight different forms of agrin, which differ in !1their acetylcholine receptor clustering activity. CLASSIFICATION #superfamily agrin; EGF homology; Kazal proteinase inhibitor !1homology; laminin G repeat homology; laminin-type EGF-like !1homology KEYWORDS alternative splicing; duplication; glycoprotein; !1neuromuscular junction FEATURE !$1-1959 #product agrin, form 1 #status predicted #label AG1\ !$1-1787,1799-1959 #product agrin, form 4 #status predicted #label AG4\ !$1-1779,1799-1959 #product agrin, form 3 #status predicted #label AG3\ !$1-1779,1788-1959 #product agrin, form 5 #status predicted #label AG5\ !$1-1143,1153-1959 #product agrin, form 2 #status predicted #label AG2\ !$22-50 #region hydrophobic\ !$88-137 #domain Kazal proteinase inhibitor homology #label !8KPI1\ !$163-212 #domain Kazal proteinase inhibitor homology #label !8KPI2\ !$236-284 #domain Kazal proteinase inhibitor homology #label !8KPI3\ !$307-356 #domain Kazal proteinase inhibitor homology #label !8KPI4\ !$381-429 #domain Kazal proteinase inhibitor homology #label !8KPI5\ !$446-494 #domain Kazal proteinase inhibitor homology #label !8KPI6\ !$511-559 #domain Kazal proteinase inhibitor homology #label !8KPI7\ !$540-542 #region motor neuron attachment (L-R-E) motif\ !$596-645 #domain Kazal proteinase inhibitor homology #label !8KPI8\ !$688-739 #domain laminin-type EGF-like homology #label LE1\ !$742-786 #domain laminin-type EGF-like homology #label LE2\ !$814-864 #domain Kazal proteinase inhibitor homology #label !8KPI9\ !$869-992 #region serine/threonine-rich\ !$1084-1086 #region motor neuron attachment (L-R-E) motif\ !$1147-1215 #region serine/threonine-rich\ !$1224-1257 #domain EGF homology #label EG1\ !$1287-1442 #domain laminin G repeat homology #label LG1\ !$1444-1476 #domain EGF homology #label EG2\ !$1483-1515 #domain EGF homology #label EG3\ !$1555-1706 #domain laminin G repeat homology #label LG2\ !$1713-1747 #domain EGF homology #label EG4\ !$1807-1959 #domain laminin G repeat homology #label LG3\ !$97-116,105-137, !$171-191,180-212, !$244-263,252-284, !$316-335,324-356, !$389-408,397-429, !$454-473,462-494, !$518-538,527-559, !$604-624,613-645, !$823-843,832-864, !$1224-1235, !$1229-1246, !$1248-1257, !$1444-1455, !$1449-1465, !$1467-1476, !$1483-1494, !$1488-1504,1506-1515 #disulfide_bonds #status predicted\ !$145,672,827,957 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1959 #molecular-weight 208644 #checksum 807 SEQUENCE /// ENTRY AGCH #type complete TITLE agrin precursor - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 17-Nov-2000 ACCESSIONS JH0591; A38857; B38857; I50692 REFERENCE JH0591 !$#authors Tsim, K.W.K.; Ruegg, M.A.; Escher, G.; Kroeger, S.; McMahan, !1U.J. !$#journal Neuron (1992) 8:677-689 !$#title cDNA that encodes active agrin. !$#cross-references MUID:92232297; PMID:1314620 !$#accession JH0591 !'##molecule_type mRNA !'##residues 1-1955 ##label TSI !'##cross-references GB:M94271; NID:g211120; PIDN:AAA48585.1; !1PID:g211121 !'##experimental_source brain REFERENCE A38857 !$#authors Ruegg, M.A.; Tsim, K.W.K.; Horton, S.E.; Kroeger, S.; !1Escher, G.; Gensch, E.M.; McMahan, U.J. !$#journal Neuron (1992) 8:691-699 !$#title The agrin gene codes for a family of basal lamina proteins !1that differ in function and distribution. !$#cross-references MUID:92232298; PMID:1314621 !$#contents alternative splicing !$#accession A38857 !'##molecule_type mRNA !'##residues 1132-1783;1795-1955 ##label RU2 !'##cross-references GB:M97371 !$#accession B38857 !'##molecule_type mRNA !'##residues 1221-1647;1652-1783;1794-1955 ##label RU3 !'##cross-references GB:M97372 !'##note translation of the nucleotide sequence is not complete REFERENCE I50692 !$#authors Thomas, W.S.; O'Dowd, D.K.; Smith, M.A. !$#journal Dev. Biol. (1993) 158:523-535 !$#title Developmental expression and alternative splicing of chick !1agrin RNA. !$#cross-references MUID:93345745; PMID:8393816 !$#accession I50692 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 'SHLSNEIPA',1784-1795 ##label THO !'##cross-references EMBL:U07271; NID:g459665; PIDN:AAA16788.1; !1PID:g459666 COMMENT This protein mediates the motor neuron-induced aggregation !1of acetylcholine receptors and acetylcholine-esterase on the !1surface of muscle fibers of the neuromuscular junction. COMMENT Alternative splicing produces two inactive proteins: !1agrin-related protein 1 and agrin-related protein 2. CLASSIFICATION #superfamily agrin; EGF homology; Kazal proteinase inhibitor !1homology; laminin G repeat homology; laminin-type EGF-like !1homology KEYWORDS alternative splicing; duplication; glycoprotein; !1neuromuscular junction FEATURE !$1-38 #domain signal sequence #status predicted #label SIG\ !$39-1955 #product agrin #status predicted #label MAT\ !$39-1783,1795-1955 #product agrin-related protein 1 #status predicted !8#label AG1\ !$39-1647,1652-1783, !$1794-1955 #product agrin-related protein 2 #status predicted !8#label AG2\ !$77-126 #domain Kazal proteinase inhibitor homology #label !8KPI1\ !$152-201 #domain Kazal proteinase inhibitor homology #label !8KPI2\ !$225-273 #domain Kazal proteinase inhibitor homology #label !8KPI3\ !$295-344 #domain Kazal proteinase inhibitor homology #label !8KPI4\ !$370-418 #domain Kazal proteinase inhibitor homology #label !8KPI5\ !$435-483 #domain Kazal proteinase inhibitor homology #label !8KPI6\ !$500-548 #domain Kazal proteinase inhibitor homology #label !8KPI7\ !$584-633 #domain Kazal proteinase inhibitor homology #label !8KPI8\ !$675-726 #domain laminin-type EGF-like homology #label LE1\ !$729-773 #domain laminin-type EGF-like homology #label LE2\ !$801-851 #domain Kazal proteinase inhibitor homology #label !8KPI9\ !$856-995 #region serine/threonine-rich\ !$1150-1219 #region serine/threonine-rich\ !$1233-1264 #domain EGF homology #label EG1\ !$1294-1448 #domain laminin G repeat homology #label LG1\ !$1429-1431 #region motor neuron attachment (L-R-E) motif\ !$1450-1482 #domain EGF homology #label EG2\ !$1489-1521 #domain EGF homology #label EG3\ !$1560-1711 #domain laminin G repeat homology #label LG2\ !$1718-1751 #domain EGF homology #label EG4\ !$1803-1955 #domain laminin G repeat homology #label LG3\ !$86-105,94-126, !$160-180,169-201, !$233-252,241-273, !$304-323,312-344, !$378-397,386-418, !$443-462,451-483, !$507-527,516-548, !$592-612,601-633, !$810-830,819-851, !$1233-1244, !$1238-1253, !$1255-1264, !$1450-1461, !$1455-1471, !$1473-1482, !$1489-1500, !$1494-1510,1512-1521 #disulfide_bonds #status predicted\ !$390,659,764,814 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1955 #molecular-weight 211411 #checksum 3924 SEQUENCE /// ENTRY A27701 #type complete TITLE follistatin precursor - pig CONTAINS follistatin short form precursor ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 17-Nov-2000 ACCESSIONS A27701; A40064; B40064; A39969; A47139 REFERENCE A27701 !$#authors Shimasaki, S.; Koga, M.; Esch, F.; Mercado, M.; Cooksey, K.; !1Koba, A.; Ling, N. !$#journal Biochem. Biophys. Res. Commun. (1988) 152:717-723 !$#title Porcine follistatin gene structure supports two forms of !1mature follistatin produced by alternative splicing. !$#cross-references MUID:88209050; PMID:3365249 !$#accession A27701 !'##molecule_type DNA !'##residues 1-344 ##label SHI !'##cross-references GB:M19529; NID:g164458; PIDN:AAA31036.1; !1PID:g164459 REFERENCE A40064 !$#authors Esch, F.S.; Shimasaki, S.; Mercado, M.; Cooksey, K.; Ling, !1N.; Ying, S.; Ueno, N.; Guillemin, R. !$#journal Mol. Endocrinol. (1987) 1:849-855 !$#title Structural characterization of follistatin: a novel !1follicle-stimulating hormone release-inhibiting polypeptide !1from the gonad. !$#cross-references MUID:91042571; PMID:3153465 !$#accession A40064 !'##molecule_type mRNA !'##residues 1-344 ##label ESC1 !'##cross-references GB:M36512; GB:M36513; NID:g164461 !$#accession B40064 !'##status preliminary !'##molecule_type mRNA !'##residues 1-317 ##label ESC2 !'##cross-references GB:M36512; GB:M36513; NID:g164461 REFERENCE A39969 !$#authors Ueno, N.; Ling, N.; Ying, S.Y.; Esch, F.; Shimasaki, S.; !1Guillemin, R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:8282-8286 !$#title Isolation and partial characterization of follistatin: a !1single-chain M-r 35,000 monomeric protein that inhibits the !1release of follicle-stimulating hormone. !$#cross-references MUID:88068578; PMID:3120188 !$#accession A39969 !'##molecule_type protein !'##residues 30-37 ##label UEN REFERENCE A47139 !$#authors Sugino, K.; Kurosawa, N.; Nakamura, T.; Takio, K.; !1Shimasaki, S.; Ling, N.; Titani, K.; Sugino, H. !$#journal J. Biol. Chem. (1993) 268:15579-15587 !$#title Molecular heterogeneity of follistatin, an activin-binding !1protein. Higher affinity of the carboxyl-terminal truncated !1forms for heparan sulfate proteoglycans on the ovarian !1granulosa cell. !$#cross-references MUID:93340158; PMID:8340384 !$#accession A47139 !'##status preliminary !'##molecule_type protein !'##residues 30-35;120-128;284-292;312-344 ##label SUG COMMENT Follistatin inhibits release of pituitary follicle !1stimulating hormone. GENETICS !$#introns 29/1; 93/1; 166/1; 241/1; 318/1 CLASSIFICATION #superfamily follistatin; Kazal proteinase inhibitor !1homology KEYWORDS alternative splicing; glycoprotein; monomer FEATURE !$1-29 #domain signal sequence #status predicted #label SIG\ !$30-344 #product follistatin #status predicted #label MAT\ !$30-317 #product follistatin, short splice form #status !8predicted #label MAS\ !$114-164 #domain Kazal proteinase inhibitor homology #label !8KPI8 SUMMARY #length 344 #molecular-weight 38035 #checksum 6847 SEQUENCE /// ENTRY A24420 #type complete TITLE notch protein - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES neurogenic repetitive locus protein ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A24420; A24768; S09358; A05267 REFERENCE A24420 !$#authors Kidd, S.; Kelley, M.R.; Young, M.W. !$#journal Mol. Cell. Biol. (1986) 6:3094-3108 !$#cross-references MUID:87064624; PMID:3097517 !$#accession A24420 !'##molecule_type DNA !'##residues 1-2703 ##label KID !'##cross-references GB:K03508; NID:g157991; PIDN:AAA28725.1; !1PID:g157993 REFERENCE A24768 !$#authors Wharton, K.A.; Johansen, K.M.; Xu, T.; Artavanis-Tsakonas, !1S. !$#journal Cell (1985) 43:567-581 !$#cross-references MUID:86079539; PMID:3935325 !$#accession A24768 !'##molecule_type mRNA !'##residues 1-48,'I',50-118,'R',120-230,'I',232-256,'N',258-266,'A', !1268-872,'R',874-958,'R',960-1970,'FH',1973-2256,'G', !12258-2264,'V',2266-2406,'R',2408-2444,'L',2446-2703 ##label !1WHA1 !'##note the authors translated the codon ATC for residue 49 as Thr, ATT !1for residue 2044 as Arg, GTA for residue 2265 as Ala, CGC !1for residue 2407 as His, and CTT for residue 2445 as Arg REFERENCE S09358 !$#authors Tautz, D. !$#journal Nucleic Acids Res. (1989) 17:6463-6471 !$#title Hypervariability of simple sequences as a general source for !1polymorphic DNA markers. !$#cross-references MUID:89385974; PMID:2780284 !$#accession S09358 !'##molecule_type DNA !'##residues 2505-2551,'QQQQ',2552-2576,'E',2578-2604 ##label TAU REFERENCE A05267 !$#authors Wharton, K.A.; Yedvobnick, B.; Finnerty, V.G.; !1Artavanis-Tsakonas, S. !$#journal Cell (1985) 40:55-62 !$#title opa: a novel family of transcribed repeats shared by the !1Notch locus and other developmentally regulated loci in D. !1melanogaster. !$#cross-references MUID:85099329; PMID:2981631 !$#accession A05267 !'##molecule_type DNA !'##residues 2504-2576,'E',2578-2611 ##label WHA2 GENETICS !$#gene notch; opa !'##cross-references FlyBase:FBgn0004647 !$#map_position 8.96-9.36 !$#introns 53/3; 84/3; 171/3; 240/3; 283/3; 2333/3; 2436/3; 2588/3 CLASSIFICATION #superfamily notch protein; ankyrin repeat homology; EGF !1homology KEYWORDS differentiation; tandem repeat; transmembrane protein FEATURE !$27-43 #domain transmembrane #status predicted #label TMM1\ !$297-328 #domain EGF homology #label EGX1\ !$530-561 #domain EGF homology #label EGF1\ !$568-599 #domain EGF homology #label EGF\ !$988-1019 #domain EGF homology #label EGX2\ !$1064-1095 #domain EGF homology #label EGF3\ !$1187-1218 #domain EGF homology #label EGX3\ !$1746-1762 #domain transmembrane #status predicted #label TMM2\ !$1950-1982 #domain ankyrin repeat homology #label AN1\ !$1983-2015 #domain ankyrin repeat homology #label AN2\ !$1988-2004 #domain transmembrane #status predicted #label TMM3\ !$2017-2049 #domain ankyrin repeat homology #label AN3\ !$2050-2082 #domain ankyrin repeat homology #label AN4\ !$2083-2115 #domain ankyrin repeat homology #label AN5\ !$2538-2568 #region glutamine-rich\ !$2538-2568 #domain neurogenic repetitive element #status !8predicted #label OPA SUMMARY #length 2703 #molecular-weight 288876 #checksum 6404 SEQUENCE /// ENTRY CYBOA #type complete TITLE alpha-crystallin chain A - bovine ALTERNATE_NAMES alpha-A-crystallin ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 29-Jul-1981 #sequence_revision 29-Jul-1981 #text_change 22-Jun-1999 ACCESSIONS A29656; A02872; A31352; A49791 REFERENCE A29656 !$#authors Hay, R.E.; Petrash, J.M. !$#journal Biochem. Biophys. Res. Commun. (1987) 148:31-37 !$#title Nucleotide sequence of a bovine lens alpha-A-crystallin !1cDNA. !$#cross-references MUID:88049675; PMID:3675580 !$#accession A29656 !'##molecule_type mRNA !'##residues 1-173 ##label HAY !'##cross-references GB:M26142; NID:g162909; PIDN:AAA30471.1; !1PID:g162910 REFERENCE A02872 !$#authors van der Ouderaa, F.J.; de Jong, W.W.; Bloemendal, H. !$#journal Eur. J. Biochem. (1973) 39:207-222 !$#title The amino-acid sequence of the alphaA-2 chain of bovine !1alpha-crystallin. !$#cross-references MUID:74075721; PMID:4770792 !$#accession A02872 !'##molecule_type protein !'##residues 1-173 ##label VAN REFERENCE A90153 !$#authors McDermott, M.J.; Chiesa, R.; Spector, A. !$#journal Biochem. Biophys. Res. Commun. (1988) 157:626-631 !$#title Fe(2+) oxidation of alpha-crystallin produces a 43,000 Da !1aggregate composed of A and B chains cross-linked by !1non-reducible covalent bonds. !$#cross-references MUID:89076295; PMID:3202873 !$#accession A31352 !'##molecule_type protein !'##residues 114-130 ##label MCD REFERENCE A49791 !$#authors Smith, J.B.; Thevenon-Emeric, G.; Smith, D.L.; Green, B. !$#journal Anal. Biochem. (1991) 193:118-124 !$#title Elucidation of the primary structures of proteins by mass !1spectrometry. !$#cross-references MUID:91253722; PMID:2042736 !$#accession A49791 !'##molecule_type protein !'##residues 1-173 ##label SMI REFERENCE A58565 !$#authors Roquemore, E.P.; Dell, A.; Morris, H.R.; Panico, M.; Reason, !1A.J.; Savoy, L.A.; Wistow, G.J.; Zigler Jr., J.S.; Earles, !1B.J.; Hart, G.W. !$#journal J. Biol. Chem. (1992) 267:555-563 !$#title Vertrbrate lens alpha-crystallins are modified by O-linked !1N-acetylglucosamine. !$#cross-references MUID:92112709; PMID:1730617 !$#contents annotation; O-glycosylation !$#note O-glycosylation confirmed and positioned by mass !1spectroscopy COMMENT Forms designated A1 and A2 differ by the presence and !1absence, respectively, of a phosphate group. A minor form !1exists in which the carboxyl-terminal residue has been lost. CLASSIFICATION #superfamily alpha-crystallin KEYWORDS acetylated amino end; eye lens; glycoprotein; phosphoprotein FEATURE !$1 #modified_site acetylated amino end (Met) #status !8experimental\ !$122 #binding_site phosphate (Ser) (covalent) (partial) !8#status experimental\ !$162 #binding_site carbohydrate (Ser) (covalent) #status !8experimental SUMMARY #length 173 #molecular-weight 19790 #checksum 9913 SEQUENCE /// ENTRY CYHPAA #type complete TITLE alpha-crystallin chain A - hippopotamus (tentative sequence) ORGANISM #formal_name Hippopotamus amphibius #common_name hippopotamus DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 31-Dec-1996 ACCESSIONS A02873 REFERENCE A94432 !$#authors de Jong, W.W.; Zweers, A.; Goodman, M. !$#book Protides of the Biological Fluids, Proc. 28th Colloq., !1Peeters, H., ed., pp.161-164, Pergamon Press, Oxford, 1980 !$#title Trends in the molecular evolution of alpha-crystallin. !$#accession A02873 !'##molecule_type protein !'##residues 1-173 ##label DEJ CLASSIFICATION #superfamily alpha-crystallin KEYWORDS acetylated amino end; eye lens FEATURE !$1 #modified_site acetylated amino end (Met) #status !8predicted SUMMARY #length 173 #molecular-weight 19760 #checksum 9666 SEQUENCE /// ENTRY CYGFAA #type complete TITLE alpha-crystallin chain A - giraffe (tentative sequence) ORGANISM #formal_name Giraffa camelopardalis #common_name giraffe DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 31-Dec-1996 ACCESSIONS A94432; A02873 REFERENCE A94432 !$#authors de Jong, W.W.; Zweers, A.; Goodman, M. !$#book Protides of the Biological Fluids, Proc. 28th Colloq., !1Peeters, H., ed., pp.161-164, Pergamon Press, Oxford, 1980 !$#title Trends in the molecular evolution of alpha-crystallin. !$#accession A94432 !'##molecule_type protein !'##residues 1-173 ##label DEJ CLASSIFICATION #superfamily alpha-crystallin KEYWORDS acetylated amino end; eye lens FEATURE !$1 #modified_site acetylated amino end (Met) #status !8predicted SUMMARY #length 173 #molecular-weight 19760 #checksum 9666 SEQUENCE /// ENTRY CYCMAA #type complete TITLE alpha-crystallin chain A - Arabian camel (tentative sequence) ORGANISM #formal_name Camelus dromedarius #common_name Arabian camel DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 31-Dec-1996 ACCESSIONS A02874 REFERENCE A94432 !$#authors de Jong, W.W.; Zweers, A.; Goodman, M. !$#book Protides of the Biological Fluids, Proc. 28th Colloq., !1Peeters, H., ed., pp.161-164, Pergamon Press, Oxford, 1980 !$#title Trends in the molecular evolution of alpha-crystallin. !$#accession A02874 !'##molecule_type protein !'##residues 1-173 ##label DEJ CLASSIFICATION #superfamily alpha-crystallin KEYWORDS acetylated amino end; eye lens FEATURE !$1 #modified_site acetylated amino end (Met) #status !8predicted SUMMARY #length 173 #molecular-weight 19745 #checksum 9501 SEQUENCE /// ENTRY CYDGAA #type complete TITLE alpha-crystallin chain A - dog (tentative sequence) ORGANISM #formal_name Canis lupus familiaris #common_name dog DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 24-Nov-1999 ACCESSIONS A02875 REFERENCE A91230 !$#authors de Jong, W.W.; van der Ouderaa, F.J.; Versteeg, M.; !1Groenewoud, G.; van Amelsvoort, J.M.; Bloemendal, H. !$#journal Eur. J. Biochem. (1975) 53:237-242 !$#title Primary structures of the alpha-crystallin A chains of seven !1mammalian species. !$#accession A02875 !'##molecule_type protein !'##residues 1-173 ##label DEJ !'##note the compositions of tryptic peptides and sequences of residues !113-16, 89-92, and 146-150 were determined !'##note the tryptic peptides were aligned by homology with the bovine !1sequence CLASSIFICATION #superfamily alpha-crystallin KEYWORDS blocked amino end; eye lens FEATURE !$1 #modified_site blocked amino end (Met) (probably !8acetylated) #status experimental SUMMARY #length 173 #molecular-weight 19731 #checksum 9917 SEQUENCE /// ENTRY CYCTAA #type complete TITLE alpha-crystallin chain A - cat (tentative sequence) ORGANISM #formal_name Felis silvestris catus #common_name domestic cat DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 24-Nov-1999 ACCESSIONS A91230; A02875 REFERENCE A91230 !$#authors de Jong, W.W.; van der Ouderaa, F.J.; Versteeg, M.; !1Groenewoud, G.; van Amelsvoort, J.M.; Bloemendal, H. !$#journal Eur. J. Biochem. (1975) 53:237-242 !$#title Primary structures of the alpha-crystallin A chains of seven !1mammalian species. !$#accession A91230 !'##molecule_type protein !'##residues 1-173 ##label DEJ !'##note the compositions of tryptic peptides and sequences of residues !113-16, 89-91, and 146-150 were determined !'##note the tryptic peptides were aligned by homology with the bovine !1sequence CLASSIFICATION #superfamily alpha-crystallin KEYWORDS blocked amino end; eye lens FEATURE !$1 #modified_site blocked amino end (Met) (probably !8acetylated) #status experimental SUMMARY #length 173 #molecular-weight 19731 #checksum 9917 SEQUENCE /// ENTRY CYWHAA #type complete TITLE alpha-crystallin chain A - minke whale (tentative sequence) ORGANISM #formal_name Balaenoptera acutorostrata #common_name minke whale, lesser rorqual DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 24-Nov-1999 ACCESSIONS A02876 REFERENCE A90618 !$#authors de Jong, W.W.; Nuy-Terwindt, E.C.; Versteeg, M. !$#journal Biochim. Biophys. Acta (1977) 491:573-580 !$#title Primary structures of alpha-crystallin a chains of elephant, !1whale, hyrax and rhinoceros. !$#cross-references MUID:77158093; PMID:870070 !$#accession A02876 !'##molecule_type protein !'##residues 1-173 ##label DEJ !'##note compositions of tryptic peptides and sequences of residues 13 !1and 146-153 were determined; the tryptic peptides were !1positioned by homology with the bovine sequence CLASSIFICATION #superfamily alpha-crystallin KEYWORDS blocked amino end; eye lens FEATURE !$1 #modified_site blocked amino end (Met) (probably !8acetylated) #status experimental SUMMARY #length 173 #molecular-weight 19778 #checksum 9758 SEQUENCE /// ENTRY CYPGAA #type complete TITLE alpha-crystallin chain A - pig (tentative sequence) ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 30-Sep-1993 ACCESSIONS A02877 REFERENCE A91230 !$#authors de Jong, W.W.; van der Ouderaa, F.J.; Versteeg, M.; !1Groenewoud, G.; van Amelsvoort, J.M.; Bloemendal, H. !$#journal Eur. J. Biochem. (1975) 53:237-242 !$#title Primary structures of the alpha-crystallin A chains of seven !1mammalian species. !$#accession A02877 !'##molecule_type protein !'##residues 1-173 ##label DEJ !'##note compositions of tryptic and thermolytic peptides and sequences !1of residues 13-17, 55-61, 146-147, and 164-173 were !1determined; the tryptic peptides were aligned by homology !1with the bovine sequence CLASSIFICATION #superfamily alpha-crystallin KEYWORDS blocked amino end; eye lens FEATURE !$1 #modified_site blocked amino end (Met) (probably !8acetylated) #status experimental SUMMARY #length 173 #molecular-weight 19746 #checksum 135 SEQUENCE /// ENTRY CYTPAA #type complete TITLE alpha-crystallin chain A - Asiatic tapir (tentative sequence) ORGANISM #formal_name Tapirus indicus #common_name Asiatic tapir, Malayan tapir DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 31-Dec-1996 ACCESSIONS A02878 REFERENCE A94432 !$#authors de Jong, W.W.; Zweers, A.; Goodman, M. !$#book Protides of the Biological Fluids, Proc. 28th Colloq., !1Peeters, H., ed., pp.161-164, Pergamon Press, Oxford, 1980 !$#title Trends in the molecular evolution of alpha-crystallin. !$#accession A02878 !'##molecule_type protein !'##residues 1-173 ##label DEJ CLASSIFICATION #superfamily alpha-crystallin KEYWORDS acetylated amino end; eye lens FEATURE !$1 #modified_site acetylated amino end (Met) #status !8predicted SUMMARY #length 173 #molecular-weight 19804 #checksum 9982 SEQUENCE /// ENTRY CYPEAA #type complete TITLE alpha-crystallin chain A - harbor porpoise (tentative sequence) ORGANISM #formal_name Phocoena phocoena #common_name harbor porpoise DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 31-Dec-1996 ACCESSIONS A02879 REFERENCE A94432 !$#authors de Jong, W.W.; Zweers, A.; Goodman, M. !$#book Protides of the Biological Fluids, Proc. 28th Colloq., !1Peeters, H., ed., pp.161-164, Pergamon Press, Oxford, 1980 !$#title Trends in the molecular evolution of alpha-crystallin. !$#accession A02879 !'##molecule_type protein !'##residues 1-173 ##label DEJ CLASSIFICATION #superfamily alpha-crystallin KEYWORDS acetylated amino end; eye lens FEATURE !$1 #modified_site acetylated amino end (Met) #status !8predicted SUMMARY #length 173 #molecular-weight 19768 #checksum 9835 SEQUENCE /// ENTRY CYHOAA #type complete TITLE alpha-crystallin chain A - horse (tentative sequence) ORGANISM #formal_name Equus caballus #common_name domestic horse DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 30-Sep-1993 ACCESSIONS A02880 REFERENCE A91230 !$#authors de Jong, W.W.; van der Ouderaa, F.J.; Versteeg, M.; !1Groenewoud, G.; van Amelsvoort, J.M.; Bloemendal, H. !$#journal Eur. J. Biochem. (1975) 53:237-242 !$#title Primary structures of the alpha-crystallin A chains of seven !1mammalian species. !$#accession A02880 !'##molecule_type protein !'##residues 1-173 ##label DEJ !'##note compositions of tryptic and thermolytic peptides and sequences !1of residues 13-16, 120-127, 132-139, 146-150, and 164-173 !1were determined; the tryptic peptides were aligned by !1homology with the bovine sequence CLASSIFICATION #superfamily alpha-crystallin KEYWORDS blocked amino end; eye lens FEATURE !$1 #modified_site blocked amino end (Met) (probably !8acetylated) #status experimental SUMMARY #length 173 #molecular-weight 19762 #checksum 8897 SEQUENCE /// ENTRY CYRNAA #type complete TITLE alpha-crystallin chain A - white rhinoceros (tentative sequence) ORGANISM #formal_name Ceratotherium simum #common_name white rhinoceros, square-lipped rhinoceros DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 24-Nov-1999 ACCESSIONS A02881 REFERENCE A90618 !$#authors de Jong, W.W.; Nuy-Terwindt, E.C.; Versteeg, M. !$#journal Biochim. Biophys. Acta (1977) 491:573-580 !$#title Primary structures of alpha-crystallin a chains of elephant, !1whale, hyrax and rhinoceros. !$#cross-references MUID:77158093; PMID:870070 !$#accession A02881 !'##molecule_type protein !'##residues 1-173 ##label DEJ !'##note compositions of tryptic peptides and sequences of residues !113-17, 55-62, 120-127, 132-141, and 146-150 were determined; !1the tryptic peptides were positioned by homology with the !1bovine sequence CLASSIFICATION #superfamily alpha-crystallin KEYWORDS blocked amino end; eye lens FEATURE !$1 #modified_site blocked amino end (Met) (probably !8acetylated) #status experimental SUMMARY #length 173 #molecular-weight 19808 #checksum 9599 SEQUENCE /// ENTRY CYBRAA #type complete TITLE alpha-crystallin chain A - sloth bear (tentative sequence) ORGANISM #formal_name Melursus ursinus, Ursus ursinus #common_name sloth bear DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 31-Dec-1996 ACCESSIONS A02882 REFERENCE A94432 !$#authors de Jong, W.W.; Zweers, A.; Goodman, M. !$#book Protides of the Biological Fluids, Proc. 28th Colloq., !1Peeters, H., ed., pp.161-164, Pergamon Press, Oxford, 1980 !$#title Trends in the molecular evolution of alpha-crystallin. !$#accession A02882 !'##molecule_type protein !'##residues 1-173 ##label DEJ CLASSIFICATION #superfamily alpha-crystallin KEYWORDS acetylated amino end; eye lens FEATURE !$1 #modified_site acetylated amino end (Met) #status !8predicted SUMMARY #length 173 #molecular-weight 19779 #checksum 9916 SEQUENCE /// ENTRY CYSLAA #type complete TITLE alpha-crystallin chain A - gray seal (tentative sequence) ORGANISM #formal_name Halichoerus grypus #common_name gray seal DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 31-Dec-1996 ACCESSIONS A02883 REFERENCE A94432 !$#authors de Jong, W.W.; Zweers, A.; Goodman, M. !$#book Protides of the Biological Fluids, Proc. 28th Colloq., !1Peeters, H., ed., pp.161-164, Pergamon Press, Oxford, 1980 !$#title Trends in the molecular evolution of alpha-crystallin. !$#accession A02883 !'##molecule_type protein !'##residues 1-173 ##label DEJ CLASSIFICATION #superfamily alpha-crystallin KEYWORDS acetylated amino end; eye lens FEATURE !$1 #modified_site acetylated amino end (Met) #status !8predicted SUMMARY #length 173 #molecular-weight 19713 #checksum 229 SEQUENCE /// ENTRY CYZCAA #type complete TITLE alpha-crystallin chain A - California sealion (tentative sequence) ORGANISM #formal_name Zalophus californianus #common_name California sealion DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 31-Dec-1996 ACCESSIONS B94432; A02883 REFERENCE A94432 !$#authors de Jong, W.W.; Zweers, A.; Goodman, M. !$#book Protides of the Biological Fluids, Proc. 28th Colloq., !1Peeters, H., ed., pp.161-164, Pergamon Press, Oxford, 1980 !$#title Trends in the molecular evolution of alpha-crystallin. !$#accession B94432 !'##molecule_type protein !'##residues 1-173 ##label DEJ CLASSIFICATION #superfamily alpha-crystallin KEYWORDS acetylated amino end; eye lens FEATURE !$1 #modified_site acetylated amino end (Met) #status !8predicted SUMMARY #length 173 #molecular-weight 19713 #checksum 229 SEQUENCE /// ENTRY CYBTAA #type complete TITLE alpha-crystallin chain A - fruit bat (Artibeus jamaicensis) (tentative sequence) ORGANISM #formal_name Artibeus jamaicensis DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 31-Dec-1996 ACCESSIONS A02884 REFERENCE A94432 !$#authors de Jong, W.W.; Zweers, A.; Goodman, M. !$#book Protides of the Biological Fluids, Proc. 28th Colloq., !1Peeters, H., ed., pp.161-164, Pergamon Press, Oxford, 1980 !$#title Trends in the molecular evolution of alpha-crystallin. !$#accession A02884 !'##molecule_type protein !'##residues 1-173 ##label DEJ CLASSIFICATION #superfamily alpha-crystallin KEYWORDS acetylated amino end; eye lens FEATURE !$1 #modified_site acetylated amino end (Met) #status !8predicted SUMMARY #length 173 #molecular-weight 19807 #checksum 99 SEQUENCE /// ENTRY CYMNAA #type complete TITLE alpha-crystallin chain A - American mink (tentative sequence) ORGANISM #formal_name Mustela vison #common_name American mink DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 31-Dec-1996 ACCESSIONS A02885 REFERENCE A94432 !$#authors de Jong, W.W.; Zweers, A.; Goodman, M. !$#book Protides of the Biological Fluids, Proc. 28th Colloq., !1Peeters, H., ed., pp.161-164, Pergamon Press, Oxford, 1980 !$#title Trends in the molecular evolution of alpha-crystallin. !$#accession A02885 !'##molecule_type protein !'##residues 1-173 ##label DEJ CLASSIFICATION #superfamily alpha-crystallin KEYWORDS acetylated amino end; eye lens FEATURE !$1 #modified_site acetylated amino end (Met) #status !8predicted SUMMARY #length 173 #molecular-weight 19725 #checksum 477 SEQUENCE /// ENTRY CYPNAA #type complete TITLE alpha-crystallin chain A - Malayan pangolin (tentative sequence) ORGANISM #formal_name Manis javanica #common_name Malayan pangolin DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 31-Dec-1996 ACCESSIONS A02886 REFERENCE A94432 !$#authors de Jong, W.W.; Zweers, A.; Goodman, M. !$#book Protides of the Biological Fluids, Proc. 28th Colloq., !1Peeters, H., ed., pp.161-164, Pergamon Press, Oxford, 1980 !$#title Trends in the molecular evolution of alpha-crystallin. !$#accession A02886 !'##molecule_type protein !'##residues 1-173 ##label DEJ CLASSIFICATION #superfamily alpha-crystallin KEYWORDS acetylated amino end; eye lens FEATURE !$1 #modified_site acetylated amino end (Met) #status !8predicted SUMMARY #length 173 #molecular-weight 19720 #checksum 2118 SEQUENCE /// ENTRY CYMFAA #type complete TITLE alpha-crystallin chain A - Mexican collared anteater (tentative sequence) ORGANISM #formal_name Tamandua mexicana #common_name Mexican collared anteater DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 31-Dec-1996 ACCESSIONS A02887 REFERENCE A94432 !$#authors de Jong, W.W.; Zweers, A.; Goodman, M. !$#book Protides of the Biological Fluids, Proc. 28th Colloq., !1Peeters, H., ed., pp.161-164, Pergamon Press, Oxford, 1980 !$#title Trends in the molecular evolution of alpha-crystallin. !$#accession A02887 !'##molecule_type protein !'##residues 1-170 ##label DEJ CLASSIFICATION #superfamily alpha-crystallin KEYWORDS acetylated amino end; eye lens FEATURE !$1 #modified_site acetylated amino end (Met) #status !8predicted SUMMARY #length 170 #molecular-weight 19499 #checksum 5876 SEQUENCE /// ENTRY CYOWA2 #type complete TITLE alpha-crystallin chain A - Hoffmann's two-fingered sloth (tentative sequence) ORGANISM #formal_name Choloepus hoffmanni #common_name Hoffmann's two-fingered sloth DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 31-Dec-1996 ACCESSIONS A02888 REFERENCE A94432 !$#authors de Jong, W.W.; Zweers, A.; Goodman, M. !$#book Protides of the Biological Fluids, Proc. 28th Colloq., !1Peeters, H., ed., pp.161-164, Pergamon Press, Oxford, 1980 !$#title Trends in the molecular evolution of alpha-crystallin. !$#accession A02888 !'##molecule_type protein !'##residues 1-170 ##label DEJ CLASSIFICATION #superfamily alpha-crystallin KEYWORDS acetylated amino end; eye lens FEATURE !$1 #modified_site acetylated amino end (Met) #status !8predicted SUMMARY #length 170 #molecular-weight 19591 #checksum 7296 SEQUENCE /// ENTRY CYOWA3 #type complete TITLE alpha-crystallin chain A - brown-throated sloth (tentative sequence) ORGANISM #formal_name Bradypus variegatus #common_name brown-throated sloth DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 31-Dec-1996 ACCESSIONS A02889 REFERENCE A94432 !$#authors de Jong, W.W.; Zweers, A.; Goodman, M. !$#book Protides of the Biological Fluids, Proc. 28th Colloq., !1Peeters, H., ed., pp.161-164, Pergamon Press, Oxford, 1980 !$#title Trends in the molecular evolution of alpha-crystallin. !$#accession A02889 !'##molecule_type protein !'##residues 1-170 ##label DEJ CLASSIFICATION #superfamily alpha-crystallin KEYWORDS acetylated amino end; eye lens FEATURE !$1 #modified_site acetylated amino end (Met) #status !8predicted SUMMARY #length 170 #molecular-weight 19388 #checksum 5840 SEQUENCE /// ENTRY CYMQAA #type complete TITLE alpha-crystallin chain A - rhesus macaque (tentative sequence) ORGANISM #formal_name Macaca mulatta #common_name rhesus macaque DATE 24-Apr-1984 #sequence_revision 27-Nov-1985 #text_change 30-Sep-1993 ACCESSIONS A02890 REFERENCE A91230 !$#authors de Jong, W.W.; van der Ouderaa, F.J.; Versteeg, M.; !1Groenewoud, G.; van Amelsvoort, J.M.; Bloemendal, H. !$#journal Eur. J. Biochem. (1975) 53:237-242 !$#title Primary structures of the alpha-crystallin A chains of seven !1mammalian species. !$#accession A02890 !'##molecule_type protein !'##residues 1-172 ##label DEJ !'##note compositions of tryptic peptides and sequences of residues 2-6, !189-96, and 146-162 were determined; the tryptic peptides !1were aligned by homology with the bovine sequence CLASSIFICATION #superfamily alpha-crystallin KEYWORDS blocked amino end; eye lens FEATURE !$1 #modified_site blocked amino end (Met) (probably !8acetylated) #status experimental SUMMARY #length 172 #molecular-weight 19792 #checksum 9312 SEQUENCE /// ENTRY CYHUAA #type complete TITLE alpha-crystallin chain A - human ALTERNATE_NAMES alpha-A-crystallin ORGANISM #formal_name Homo sapiens #common_name man DATE 27-Nov-1985 #sequence_revision 25-Apr-1997 #text_change 22-Jun-1999 ACCESSIONS S03344; A45947; I56464; A91421; A94588; JX0351; I39379; !1JC5690; A02891 REFERENCE S03344 !$#authors Jaworski, C.J.; Piatigorsky, J. !$#journal Nature (1989) 337:752-754 !$#title A pseudo-exon in the functional human alpha-A--crystallin !1gene. !$#cross-references MUID:89143747; PMID:2918909 !$#accession S03344 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-104 ##label JAW1 !'##cross-references EMBL:X14789; NID:g28633; PIDN:CAA32891.1; !1PID:g28634 REFERENCE A45947 !$#authors McDevitt, D.S.; Hawkins, J.W.; Jaworski, C.J.; Piatigorsky, !1J. !$#journal Exp. Eye Res. (1986) 43:285-291 !$#title Isolation and partial characterization of the human !1alphaA-crystallin gene. !$#cross-references MUID:87005033; PMID:3758227 !$#accession A45947 !'##molecule_type DNA !'##residues 1-63;166-173 ##label MCD !'##cross-references GB:M35629; NID:g181077; PIDN:AAA52105.1; !1PID:g181080; GB:M35628; NID:g181078; PID:g181081 REFERENCE I56464 !$#authors Jaworski, C.J.; Chepelinsky, A.B.; Piatigorsky, J. !$#journal J. Mol. Evol. (1991) 33:495-505 !$#title The alpha A-crystallin gene: conserved features of the !15'-flanking regions in human, mouse, and chicken. !$#cross-references MUID:92139443; PMID:1779432 !$#accession I56464 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-3 ##label JAW2 !'##cross-references GB:S79457; NID:g244474; PIDN:AAB21309.1; !1PID:g244475 REFERENCE A91421 !$#authors de Jong, W.W.; Terwindt, E.C.; Bloemendal, H. !$#journal FEBS Lett. (1975) 58:310-313 !$#title The amino acid sequence of the A chain of human !1alpha-crystallin. !$#cross-references MUID:76187952; PMID:817940 !$#contents compositions of tryptic and thermolytic peptides !$#accession A91421 !'##molecule_type protein !'##residues 132-135;146-151;158-162;166-173 ##label DEJ !'##note the tryptic peptides were aligned by homology with the bovine !1and monkey sequences REFERENCE A94588 !$#authors Kramps, J.A.; de Jong, W.W. !$#submission submitted to the Atlas, June 1977 !$#contents revisions !$#accession A94588 !'##molecule_type protein !'##residues 1-152,'HT',156-173 ##label KRA REFERENCE JX0351 !$#authors Fujii, N.; Satoh, K.; Harada, K.; Ishibashi, Y. !$#journal J. Biochem. (1994) 116:663-669 !$#title Simultaneous stereoinversion and isomerization at specific !1aspartic acid residues in alpha A-crystallin from human !1lens. !$#cross-references MUID:95155281; PMID:7852288 !$#accession JX0351 !'##molecule_type protein !'##residues 1-127,129-173 ##label FUJ !'##experimental_source lens !'##note aspartic acids 58 and 150 are shown to undergo uncatalyzed, !1aging-related stereoisomerization coupled with conversion of !1peptide to isopeptide bonds REFERENCE I39379 !$#authors Caspers, G.J.; Pennings, J.; De Jong, W.W. !$#journal Exp. Eye Res. (1994) 59:125-126 !$#title A partial cDNA sequence corrects the human alpha !1A-crystallin primary structure [letter]. !$#cross-references MUID:95137069; PMID:7835394 !$#accession I39379 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 105-156,'A',158-160 ##label CAS !'##cross-references GB:L25781; NID:g531191; PIDN:AAC37570.1; !1PID:g688439 REFERENCE A58565 !$#authors Roquemore, E.P.; Dell, A.; Morris, H.R.; Panico, M.; Reason, !1A.J.; Savoy, L.A.; Wistow, G.J.; Zigler Jr., J.S.; Earles, !1B.J.; Hart, G.W. !$#journal J. Biol. Chem. (1992) 267:555-563 !$#title Vertrbrate lens alpha-crystallins are modified by O-linked !1N-acetylglucosamine. !$#cross-references MUID:92112709; PMID:1730617 !$#contents annotation; O-glycosylation !$#note O-glycosylation confirmed but not positioned in human !1protein REFERENCE JC5690 !$#authors Fujii, N.; Momose, Y.; Yamasaki, M.; Yamagaki, T.; !1Nakanishi, H.; Uemura, T.; Takita, M.; Ishii, N. !$#journal Biochem. Biophys. Res. Commun. (1997) 239:918-923 !$#title The conformation formed by the domain after alanine-155 !1induces inversion of aspartic acid-151 in alpha A-crystallin !1from aged human lenses. !$#cross-references MUID:98042494; PMID:9367870 !$#accession JC5690 !'##molecule_type protein !'##residues 1-173 ##label FU2 COMMENT Forms designated A1 and A2 differ by the presence and !1absence, respectively, of a phosphate group. A minor form !1exists in which the carboxyl-terminal residue has been lost. COMMENT This protein is a small heat shock protein and acts as a !1molecular chaperone to maintain lens clarity. GENETICS !$#gene GDB:CRYAA; CRYA1 !'##cross-references GDB:119074; OMIM:123580 !$#map_position 21q22.3-21q22.3 FUNCTION !$#description structural component of the eye lens CLASSIFICATION #superfamily alpha-crystallin KEYWORDS blocked amino end; eye lens; glycoprotein; phosphoprotein FEATURE !$1 #modified_site blocked amino end (Met) (probably !8acetylated) #status experimental\ !$122 #binding_site phosphate (Ser) (covalent) (by !8cAMP-dependent kinase) #status predicted\ !$162 #binding_site carbohydrate (Ser) (covalent) #status !8predicted SUMMARY #length 173 #molecular-weight 19909 #checksum 9076 SEQUENCE /// ENTRY CYRTA #type complete TITLE alpha-crystallin chain A - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 15-Oct-1982 #sequence_revision 27-Nov-1985 #text_change 16-Jun-2000 ACCESSIONS A02892; A93739; I55370; I70087 REFERENCE A91230 !$#authors de Jong, W.W.; van der Ouderaa, F.J.; Versteeg, M.; !1Groenewoud, G.; van Amelsvoort, J.M.; Bloemendal, H. !$#journal Eur. J. Biochem. (1975) 53:237-242 !$#title Primary structures of the alpha-crystallin A chains of seven !1mammalian species. !$#accession A02892 !'##molecule_type protein !'##residues 1-173 ##label DEJ !'##note the compositions of tryptic peptides and sequences of residues !12-6, 13-16, 89-92, and 146-150 were determined !'##note the tryptic peptides were positioned by homology with the !1bovine sequence REFERENCE A93739 !$#authors Moormann, R.J.M.; van der Velden, H.M.W.; Dodemont, H.J.; !1Andreoli, P.M.; Bloemendal, H.; Schoenmakers, J.G.G. !$#journal Nucleic Acids Res. (1981) 9:4813-4822 !$#title An unusully long non-coding region in rat lens !1alpha-crystallin messenger RNA. !$#cross-references MUID:82081811; PMID:6171772 !$#accession A93739 !'##molecule_type mRNA !'##residues 53-173 ##label MOO !'##cross-references GB:V01219; GB:J00715; NID:g55598; PIDN:CAA24530.1; !1PID:g809074 REFERENCE I55370 !$#authors Srinivasan, A.N.; Nagineni, C.N.; Bhat, S.P. !$#journal J. Biol. Chem. (1992) 267:23337-23341 !$#title Alpha A-crystallin is expressed in non-ocular tissues. !$#cross-references MUID:93054670; PMID:1429679 !$#accession I55370 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 90-172 ##label RES !'##cross-references GB:M96949; NID:g202619; PIDN:AAA40644.1; !1PID:g202620 !'##experimental_source spleen !$#accession I70087 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 90-123,'M',125-172 ##label RE2 !'##cross-references GB:M96950; NID:g202621; PIDN:AAA40645.1; !1PID:g202622 !'##experimental_source eye GENETICS !$#gene alpha A-crystallin CLASSIFICATION #superfamily alpha-crystallin KEYWORDS alternative splicing; blocked amino end; eye lens FEATURE !$1 #modified_site blocked amino end (Met) (probably !8acetylated) #status experimental SUMMARY #length 173 #molecular-weight 19792 #checksum 9705 SEQUENCE /// ENTRY CYHYAB #type complete TITLE alpha-crystallin chain A - Mongolian jird (tentative sequence) ORGANISM #formal_name Meriones unguiculatus #common_name Mongolian jird DATE 30-Jun-1988 #sequence_revision 31-Dec-1991 #text_change 24-Nov-1999 ACCESSIONS C94432; A02892 REFERENCE A94432 !$#authors de Jong, W.W.; Zweers, A.; Goodman, M. !$#book Protides of the Biological Fluids, Proc. 28th Colloq., !1Peeters, H., ed., pp.161-164, Pergamon Press, Oxford, 1980 !$#title Trends in the molecular evolution of alpha-crystallin. !$#accession C94432 !'##molecule_type protein !'##residues 1-173 ##label DEJ CLASSIFICATION #superfamily alpha-crystallin KEYWORDS alternative splicing; blocked amino end; eye lens FEATURE !$1 #modified_site blocked amino end (Met) (probably !8acetylated) #status experimental SUMMARY #length 173 #molecular-weight 19792 #checksum 9705 SEQUENCE /// ENTRY CYHYA #type complete TITLE alpha-crystallin chain A - golden hamster (tentative sequence) ORGANISM #formal_name Mesocricetus auratus #common_name golden hamster DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 24-Nov-1999 ACCESSIONS D94432; A02892 REFERENCE A94432 !$#authors de Jong, W.W.; Zweers, A.; Goodman, M. !$#book Protides of the Biological Fluids, Proc. 28th Colloq., !1Peeters, H., ed., pp.161-164, Pergamon Press, Oxford, 1980 !$#title Trends in the molecular evolution of alpha-crystallin. !$#accession D94432 !'##molecule_type protein !'##residues 1-173 ##label DEJ CLASSIFICATION #superfamily alpha-crystallin KEYWORDS alternative splicing; blocked amino end; eye lens FEATURE !$1 #modified_site blocked amino end (Met) (probably !8acetylated) #status experimental SUMMARY #length 173 #molecular-weight 19792 #checksum 9705 SEQUENCE /// ENTRY CYMSA #type complete TITLE alpha-crystallin chain A - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 25-Feb-1985 #sequence_revision 19-Apr-1996 #text_change 22-Jun-1999 ACCESSIONS A02893; A18860 REFERENCE A02893 !$#authors King, C.R.; Shinohara, T.; Piatigorsky, J. !$#journal Science (1982) 215:985-987 !$#title alphaA-crystallin messenger RNA of the mouse lens: more !1noncoding than coding sequences. !$#cross-references MUID:83119896; PMID:7156978 !$#accession A02893 !'##molecule_type mRNA !'##residues 11-173 ##label KI2 !'##cross-references GB:J00376; NID:g192760; PIDN:AAA37471.1; !1PID:g387134 !'##note the mouse sequence appears to be identical with the rat !1sequence REFERENCE A18860 !$#authors King, C.R.; Piatigorsky, J. !$#journal Cell (1983) 32:707-712 !$#title Alternative RNA splicing of the murine alphaA-crystallin !1gene: protein-coding information within an intron. !$#cross-references MUID:83155647; PMID:6187470 !$#accession A18860 !'##molecule_type DNA !'##residues 1-104 ##label KIN CLASSIFICATION #superfamily alpha-crystallin KEYWORDS acetylated amino end; alternative splicing; eye lens FEATURE !$1 #modified_site acetylated amino end (Met) #status !8predicted SUMMARY #length 173 #molecular-weight 19792 #checksum 9705 SEQUENCE /// ENTRY CYGPAA #type complete TITLE alpha-crystallin chain A - guinea pig (tentative sequence) ORGANISM #formal_name Cavia porcellus #common_name guinea pig DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 31-Dec-1996 ACCESSIONS A02894 REFERENCE A94432 !$#authors de Jong, W.W.; Zweers, A.; Goodman, M. !$#book Protides of the Biological Fluids, Proc. 28th Colloq., !1Peeters, H., ed., pp.161-164, Pergamon Press, Oxford, 1980 !$#title Trends in the molecular evolution of alpha-crystallin. !$#accession A02894 !'##molecule_type protein !'##residues 1-173 ##label DEJ CLASSIFICATION #superfamily alpha-crystallin KEYWORDS acetylated amino end; eye lens FEATURE !$1 #modified_site acetylated amino end (Met) #status !8predicted SUMMARY #length 173 #molecular-weight 19807 #checksum 9870 SEQUENCE /// ENTRY CYCPAA #type complete TITLE alpha-crystallin chain A - springhaas (tentative sequence) ORGANISM #formal_name Pedetes capensis #common_name springhaas, springhare DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 31-Dec-1996 ACCESSIONS E94432; A02894 REFERENCE A94432 !$#authors de Jong, W.W.; Zweers, A.; Goodman, M. !$#book Protides of the Biological Fluids, Proc. 28th Colloq., !1Peeters, H., ed., pp.161-164, Pergamon Press, Oxford, 1980 !$#title Trends in the molecular evolution of alpha-crystallin. !$#accession E94432 !'##molecule_type protein !'##residues 1-173 ##label DEJ CLASSIFICATION #superfamily alpha-crystallin KEYWORDS acetylated amino end; eye lens FEATURE !$1 #modified_site acetylated amino end (Met) #status !8predicted SUMMARY #length 173 #molecular-weight 19807 #checksum 9870 SEQUENCE /// ENTRY CYOIAA #type complete TITLE alpha-crystallin chain A - southern American pika (tentative sequence) ORGANISM #formal_name Ochotona princeps #common_name southern American pika DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 31-Dec-1996 ACCESSIONS A02895 REFERENCE A94432 !$#authors de Jong, W.W.; Zweers, A.; Goodman, M. !$#book Protides of the Biological Fluids, Proc. 28th Colloq., !1Peeters, H., ed., pp.161-164, Pergamon Press, Oxford, 1980 !$#title Trends in the molecular evolution of alpha-crystallin. !$#accession A02895 !'##molecule_type protein !'##residues 1-173 ##label DEJ CLASSIFICATION #superfamily alpha-crystallin KEYWORDS acetylated amino end; eye lens FEATURE !$1 #modified_site acetylated amino end (Met) #status !8predicted SUMMARY #length 173 #molecular-weight 19780 #checksum 90 SEQUENCE /// ENTRY CYRBAA #type complete TITLE alpha-crystallin chain A - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 17-Nov-1995 ACCESSIONS A02896; B53871 REFERENCE A91230 !$#authors de Jong, W.W.; van der Ouderaa, F.J.; Versteeg, M.; !1Groenewoud, G.; van Amelsvoort, J.M.; Bloemendal, H. !$#journal Eur. J. Biochem. (1975) 53:237-242 !$#title Primary structures of the alpha-crystallin A chains of seven !1mammalian species. !$#accession A02896 !'##molecule_type protein !'##residues 1-173 ##label DEJ !'##note compositions of tryptic peptides and sequences of residues 2-6 !1and 146-150 were determined; the tryptic peptides were !1aligned by homology with the bovine sequence REFERENCE A53871 !$#authors Parveen, R.; Smith, J.B.; Sun, Y.; Smith, D.L. !$#journal J. Protein Chem. (1993) 12:93-101 !$#title Primary structure of rabbit lens alpha-crystallins. !$#cross-references MUID:93151974; PMID:8427639 !$#accession B53871 !'##molecule_type protein !'##residues 1-173 ##label PAR !'##experimental_source lens !'##note sequence extracted from NCBI backbone (NCBIP:124613) !'##note tentative sequence confirmed by mass spectrometry; peptide !1corresponding to residues 119-129 is phosphorylated CLASSIFICATION #superfamily alpha-crystallin KEYWORDS acetylated amino end; eye lens; phosphoprotein FEATURE !$1-168 #product alpha crystallin chain A, minor form #status !8experimental #label MIN\ !$1 #modified_site acetylated amino end (Met) #status !8experimental\ !$122 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 173 #molecular-weight 19837 #checksum 117 SEQUENCE /// ENTRY CYLEAA #type complete TITLE alpha-crystallin chain A - brown lemur (tentative sequence) ORGANISM #formal_name Lemur fulvus fulvus #common_name brown lemur DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 31-Dec-1996 ACCESSIONS A02897 REFERENCE A94432 !$#authors de Jong, W.W.; Zweers, A.; Goodman, M. !$#book Protides of the Biological Fluids, Proc. 28th Colloq., !1Peeters, H., ed., pp.161-164, Pergamon Press, Oxford, 1980 !$#title Trends in the molecular evolution of alpha-crystallin. !$#accession A02897 !'##molecule_type protein !'##residues 1-173 ##label DEJ CLASSIFICATION #superfamily alpha-crystallin KEYWORDS acetylated amino end; eye lens FEATURE !$1 #modified_site acetylated amino end (Met) #status !8predicted SUMMARY #length 173 #molecular-weight 19819 #checksum 117 SEQUENCE /// ENTRY CYLPAA #type complete TITLE alpha-crystallin chain A - potto (tentative sequence) ORGANISM #formal_name Perodicticus potto #common_name potto DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 31-Dec-1996 ACCESSIONS A02898 REFERENCE A94432 !$#authors de Jong, W.W.; Zweers, A.; Goodman, M. !$#book Protides of the Biological Fluids, Proc. 28th Colloq., !1Peeters, H., ed., pp.161-164, Pergamon Press, Oxford, 1980 !$#title Trends in the molecular evolution of alpha-crystallin. !$#accession A02898 !'##molecule_type protein !'##residues 1-173 ##label DEJ CLASSIFICATION #superfamily alpha-crystallin KEYWORDS acetylated amino end; eye lens FEATURE !$1 #modified_site acetylated amino end (Met) #status !8predicted SUMMARY #length 173 #molecular-weight 19805 #checksum 307 SEQUENCE /// ENTRY CYGCAA #type complete TITLE alpha-crystallin chain A - bush baby (tentative sequence) ORGANISM #formal_name Galago sp. #common_name bush baby DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 31-Dec-1996 ACCESSIONS F94432; A02898 REFERENCE A94432 !$#authors de Jong, W.W.; Zweers, A.; Goodman, M. !$#book Protides of the Biological Fluids, Proc. 28th Colloq., !1Peeters, H., ed., pp.161-164, Pergamon Press, Oxford, 1980 !$#title Trends in the molecular evolution of alpha-crystallin. !$#accession F94432 !'##molecule_type protein !'##residues 1-173 ##label DEJ CLASSIFICATION #superfamily alpha-crystallin KEYWORDS acetylated amino end; eye lens FEATURE !$1 #modified_site acetylated amino end (Met) #status !8predicted SUMMARY #length 173 #molecular-weight 19805 #checksum 307 SEQUENCE /// ENTRY CYRTAM #type complete TITLE alpha-crystallin chain A, minor component - rat (tentative sequence) ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Oct-1979 #sequence_revision 31-Oct-1979 #text_change 24-Feb-1995 ACCESSIONS A02899 REFERENCE A02899 !$#authors Cohen, L.H.; Westerhuis, L.W.; de Jong, W.W.; Bloemendal, H. !$#journal Eur. J. Biochem. (1978) 89:259-266 !$#title Rat alpha-crystallin A chain with an insertion of 22 !1residues. !$#cross-references MUID:79024611; PMID:699911 !$#contents compositions of tryptic peptides and sequences of residues !155-61 and 64-87 !$#accession A02899 !'##molecule_type protein !'##residues 1-195 ##label COH !'##note the tryptic peptides other than the insertion sequence were !1aligned by homology with the rat major component COMMENT The minor component differs from the major in having an !1insertion of 22 residues after position 63. CLASSIFICATION #superfamily alpha-crystallin KEYWORDS alternative splicing; blocked amino end; eye lens FEATURE !$1 #modified_site blocked amino end (Met) (probably !8acetylated) #status experimental SUMMARY #length 195 #molecular-weight 22261 #checksum 5400 SEQUENCE /// ENTRY CYHYAM #type complete TITLE alpha-crystallin chain A, minor component - golden hamster (tentative sequence) ORGANISM #formal_name Mesocricetus auratus #common_name golden hamster DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 31-Dec-1996 ACCESSIONS A02900 REFERENCE A02900 !$#authors de Jong, W.W.; Cohen, L.H.; Leunissen, J.A.M.; Zweers, A. !$#journal Biochem. Biophys. Res. Commun. (1980) 96:648-655 !$#title Internally elongated rodent alpha-crystallin a chain: !1resulting from incomplete RNA splicing? !$#cross-references MUID:81038775; PMID:7426005 !$#contents compositions of tryptic peptides and sequence of residues !181-84 !$#accession A02900 !'##molecule_type protein !'##residues 1-195 ##label DEJ !'##note the tryptic peptides were aligned by homology with the rat !1minor component COMMENT The minor component differs from the major in having an !1insertion of 22 residues after position 63. CLASSIFICATION #superfamily alpha-crystallin KEYWORDS acetylated amino end; alternative splicing; eye lens FEATURE !$1 #modified_site acetylated amino end (Met) #status !8predicted SUMMARY #length 195 #molecular-weight 22317 #checksum 5454 SEQUENCE /// ENTRY CYELAA #type complete TITLE alpha-crystallin chain A - African elephant (tentative sequence) ORGANISM #formal_name Loxodonta africana #common_name African elephant DATE 01-Sep-1981 #sequence_revision 27-Nov-1985 #text_change 04-Nov-1994 ACCESSIONS A02901 REFERENCE A90618 !$#authors de Jong, W.W.; Nuy-Terwindt, E.C.; Versteeg, M. !$#journal Biochim. Biophys. Acta (1977) 491:573-580 !$#title Primary structures of alpha-crystallin a chains of elephant, !1whale, hyrax and rhinoceros. !$#cross-references MUID:77158093; PMID:870070 !$#accession A02901 !'##molecule_type protein !'##residues 1-173 ##label DEJ !'##note compositions of tryptic peptides and sequences of residues !166-67, 69-78, 80, 89-94, 104-106, 139-141, 143-149, and !1151-159 were determined; the tryptic peptides were !1positioned by homology with the bovine sequence CLASSIFICATION #superfamily alpha-crystallin KEYWORDS blocked amino end; eye lens FEATURE !$1 #modified_site blocked amino end (Met) (probably !8acetylated) #status experimental SUMMARY #length 173 #molecular-weight 19837 #checksum 9656 SEQUENCE /// ENTRY CYHXAA #type complete TITLE alpha-crystallin chain A - Cape rock hyrax (tentative sequence) ORGANISM #formal_name Procavia capensis #common_name Cape rock hyrax DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 04-Nov-1994 ACCESSIONS A02902 REFERENCE A90618 !$#authors de Jong, W.W.; Nuy-Terwindt, E.C.; Versteeg, M. !$#journal Biochim. Biophys. Acta (1977) 491:573-580 !$#title Primary structures of alpha-crystallin a chains of elephant, !1whale, hyrax and rhinoceros. !$#cross-references MUID:77158093; PMID:870070 !$#accession A02902 !'##molecule_type protein !'##residues 1-173 ##label DEJ !'##note compositions of tryptic peptides and sequences of residues 13, !155-57, 66-75, and 89-91 were determined; the tryptic !1peptides were positioned by homology with the bovine !1sequence !'##note 55-Ala was found in 50% of the molecules CLASSIFICATION #superfamily alpha-crystallin KEYWORDS blocked amino end; eye lens FEATURE !$1 #modified_site blocked amino end (Met) (probably !8acetylated) #status experimental SUMMARY #length 173 #molecular-weight 19822 #checksum 9757 SEQUENCE /// ENTRY CYOYAA #type complete TITLE alpha-crystallin chain A - aardvark (tentative sequence) ORGANISM #formal_name Orycteropus afer #common_name aardvark DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 04-Nov-1994 ACCESSIONS A02904 REFERENCE A02903 !$#authors de Jong, W.W.; Zweers, A.; Goodman, M. !$#journal Nature (1981) 292:538-540 !$#title Relationship of aardvark to elephants, hyraxes and sea cows !1from alpha-crystallin sequences. !$#cross-references MUID:81245239; PMID:7254349 !$#accession A02904 !'##molecule_type protein !'##residues 1-173 ##label DEJ !'##note compositions of tryptic and chymotryptic peptides and sequences !1of residues 56-57, 66-67, 90-91, 139, 146-148, 158-161, and !1168-170 were determined; the peptides were aligned by !1homology with the bovine sequence CLASSIFICATION #superfamily alpha-crystallin KEYWORDS blocked amino end; eye lens FEATURE !$1 #modified_site blocked amino end (Met) (probably !8acetylated) #status experimental SUMMARY #length 173 #molecular-weight 19908 #checksum 1026 SEQUENCE /// ENTRY CYKGAA #type complete TITLE alpha-crystallin chain A - red kangaroo (tentative sequence) ORGANISM #formal_name Macropus rufus, Megaleia rufa #common_name red kangaroo DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 31-Mar-2000 ACCESSIONS A02905 REFERENCE A91239 !$#authors de Jong, W.W.; Terwindt, E.C. !$#journal Eur. J. Biochem. (1976) 67:503-510 !$#title The amino-acid sequences of the alpha-crystallin A chains of !1red kangaroo and Virginia opossum. !$#cross-references MUID:77003051; PMID:964255 !$#accession A02905 !'##molecule_type protein !'##residues 1-173 ##label DEJ !'##note some of the chains lack the carboxyl-terminal five residues, !1probably due to normal in vivo degradation CLASSIFICATION #superfamily alpha-crystallin KEYWORDS blocked amino end; eye lens FEATURE !$1 #modified_site blocked amino end (Met) (probably !8acetylated) #status experimental SUMMARY #length 173 #molecular-weight 19906 #checksum 63 SEQUENCE /// ENTRY CYOPAA #type complete TITLE alpha-crystallin chain A - North American opossum (tentative sequence) ORGANISM #formal_name Didelphis virginiana, Didelphis marsupialis virginiana #common_name North American opossum DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 30-Sep-1993 ACCESSIONS A02906 REFERENCE A91239 !$#authors de Jong, W.W.; Terwindt, E.C. !$#journal Eur. J. Biochem. (1976) 67:503-510 !$#title The amino-acid sequences of the alpha-crystallin A chains of !1red kangaroo and Virginia opossum. !$#cross-references MUID:77003051; PMID:964255 !$#accession A02906 !'##molecule_type protein !'##residues 1-173 ##label DEJ !'##note compositions of tryptic and thermolytic peptides and sequences !1of residues 13-18, 66-75, 89-96, 100-103, 132-141, 146-155, !1158-163, and 167-170 were determined; the peptides were !1aligned by homology with the kangaroo sequence CLASSIFICATION #superfamily alpha-crystallin KEYWORDS blocked amino end; eye lens FEATURE !$1 #modified_site blocked amino end (Met) (probably !8acetylated) #status experimental SUMMARY #length 173 #molecular-weight 19995 #checksum 2232 SEQUENCE /// ENTRY CYCHAA #type complete TITLE alpha-crystallin chain A - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 25-Feb-1985 #sequence_revision 06-Jan-1995 #text_change 22-Jun-1999 ACCESSIONS A27309; A02907 REFERENCE A27309 !$#authors Thompson, M.A.; Hawkins, J.W.; Piatigorsky, J. !$#journal Gene (1987) 56:173-184 !$#title Complete nucleotide sequence of the chicken !1alpha-A-crystallin gene and its 5' flanking region. !$#cross-references MUID:88056321; PMID:3678835 !$#accession A27309 !'##molecule_type DNA !'##residues 1-173 ##label THO !'##cross-references GB:M17627; NID:g211664; PIDN:AAA48722.1; !1PID:g211665 REFERENCE A91137 !$#authors de Jong, W.W.; Zweers, A.; Versteeg, M.; Nuy-Terwindt, E.C. !$#journal Eur. J. Biochem. (1984) 141:131-140 !$#title Primary structure of the alpha-crystallin A chains of !1twenty-eight mammalian species, chicken and frog. !$#cross-references MUID:84208008; PMID:6723655 !$#accession A02907 !'##molecule_type protein !'##residues 1-148,'D',150-173 ##label DEJ GENETICS !$#introns 63/3; 104/3 CLASSIFICATION #superfamily alpha-crystallin KEYWORDS blocked amino end; eye lens FEATURE !$1 #modified_site blocked amino end (Met) (probably !8acetylated) #status experimental SUMMARY #length 173 #molecular-weight 19787 #checksum 1548 SEQUENCE /// ENTRY CYEHAA #type complete TITLE alpha-crystallin chain A - greater rhea ORGANISM #formal_name Rhea americana #common_name greater rhea, common rhea DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 24-Nov-1999 ACCESSIONS A02908 REFERENCE A02908 !$#authors Stapel, S.O.; Leunissen, J.A.M.; Versteeg, M.; Wattel, J.; !1de Jong, W.W. !$#journal Nature (1984) 311:257-259 !$#title Ratites as oldest offshoot of avian stem-evidence from !1alpha-crystallin A sequences. !$#cross-references MUID:85012654; PMID:6482951 !$#accession A02908 !'##molecule_type protein !'##residues 1-173 ##label STA CLASSIFICATION #superfamily alpha-crystallin KEYWORDS blocked amino end; eye lens FEATURE !$1 #modified_site blocked amino end (Met) (probably !8acetylated) #status experimental SUMMARY #length 173 #molecular-weight 19832 #checksum 1125 SEQUENCE /// ENTRY CYAQAA #type complete TITLE alpha-crystallin chain A - American alligator (tentative sequence) ORGANISM #formal_name Alligator mississippiensis #common_name American alligator DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 04-Nov-1994 ACCESSIONS A25753 REFERENCE A93057 !$#authors de Jong, W.W.; Zweers, A.; Versteeg, M.; Dessauer, H.C.; !1Goodman, M. !$#journal Mol. Biol. Evol. (1985) 2:484-493 !$#title alpha-Crystallin A sequences of Alligator mississippiensis !1and the lizard Tupinambis teguixin: molecular evolution and !1reptilian phylogeny. !$#cross-references MUID:88216135; PMID:3870872 !$#accession A25753 !'##molecule_type protein !'##residues 1-173 ##label DEJ !'##note compositions of peptides were determined; unsequenced residues !1and some amides were assigned by homology CLASSIFICATION #superfamily alpha-crystallin KEYWORDS blocked amino end; eye lens FEATURE !$1 #modified_site blocked amino end (Met) (probably !8acetylated) #status experimental SUMMARY #length 173 #molecular-weight 19769 #checksum 796 SEQUENCE /// ENTRY CYLZAA #type complete TITLE alpha-crystallin chain A - common tegu (tentative sequence) ORGANISM #formal_name Tupinambis teguixin #common_name common tegu DATE 25-Feb-1985 #sequence_revision 30-Sep-1987 #text_change 04-Nov-1994 ACCESSIONS B25753; A02909 REFERENCE A93057 !$#authors de Jong, W.W.; Zweers, A.; Versteeg, M.; Dessauer, H.C.; !1Goodman, M. !$#journal Mol. Biol. Evol. (1985) 2:484-493 !$#title alpha-Crystallin A sequences of Alligator mississippiensis !1and the lizard Tupinambis teguixin: molecular evolution and !1reptilian phylogeny. !$#cross-references MUID:88216135; PMID:3870872 !$#accession B25753 !'##molecule_type protein !'##residues 1-173 ##label DEJ !'##note compositions of peptides were determined; unsequenced residues !1and some amides were assigned by homology CLASSIFICATION #superfamily alpha-crystallin KEYWORDS blocked amino end; eye lens FEATURE !$1 #modified_site blocked amino end (Met) (probably !8acetylated) #status experimental SUMMARY #length 173 #molecular-weight 19898 #checksum 453 SEQUENCE /// ENTRY CYFGAA #type fragments TITLE alpha-crystallin chain A - edible frog (tentative sequence) (fragments) ORGANISM #formal_name Rana esculenta #common_name edible frog DATE 15-Nov-1984 #sequence_revision 25-Feb-1985 #text_change 31-Mar-2000 ACCESSIONS A02910 REFERENCE A91137 !$#authors de Jong, W.W.; Zweers, A.; Versteeg, M.; Nuy-Terwindt, E.C. !$#journal Eur. J. Biochem. (1984) 141:131-140 !$#title Primary structure of the alpha-crystallin A chains of !1twenty-eight mammalian species, chicken and frog. !$#cross-references MUID:84208008; PMID:6723655 !$#accession A02910 !'##molecule_type protein !'##residues 1-167 ##label DEJ CLASSIFICATION #superfamily alpha-crystallin KEYWORDS blocked amino end; eye lens FEATURE !$1 #modified_site blocked amino end (Met) (probably !8acetylated) #status experimental SUMMARY #length 167 #checksum 4146 SEQUENCE /// ENTRY CYFGA2 #type fragment TITLE alpha-crystallin chain A - common frog (fragment) ORGANISM #formal_name Rana temporaria #common_name common frog DATE 15-Nov-1984 #sequence_revision 30-Sep-1988 #text_change 16-Jun-2000 ACCESSIONS A02911 REFERENCE A02911 !$#authors Tomarev, S.I.; Zinovieva, R.D.; Dolgilevich, S.M.; Krayev, !1A.S.; Skryabin, K.G.; Gause Jr., G.G. !$#journal FEBS Lett. (1983) 162:47-51 !$#title The absence of the long 3'-non-translated region in mRNA !1coding for eye lens alphaA-2-crystallin of the frog (Rana !1temporaria). !$#cross-references MUID:84005173; PMID:6604666 !$#accession A02911 !'##molecule_type mRNA !'##residues 1-149 ##label TOM !'##cross-references GB:X00716; GB:X00058; NID:g64292; PIDN:CAA25308.1; !1PID:g1334774 CLASSIFICATION #superfamily alpha-crystallin KEYWORDS eye lens SUMMARY #length 149 #checksum 2166 SEQUENCE /// ENTRY CYDFAA #type complete TITLE alpha-crystallin chain A - spiny dogfish ORGANISM #formal_name Squalus acanthias #common_name spiny dogfish DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 04-Nov-1994 ACCESSIONS A28190; A02912 REFERENCE A92715 !$#authors de Jong, W.W.; Leunissen, J.A.M.; Leenen, P.J.M.; Zweers, !1A.; Versteeg, M. !$#journal J. Biol. Chem. (1988) 263:5141-5149 !$#title Dogfish alpha-crystallin sequences. Comparison with small !1heat shock proteins and Schistosoma egg antigen. !$#cross-references MUID:88186800; PMID:3356684 !$#accession A28190 !'##molecule_type protein !'##residues 1-177 ##label DE2 CLASSIFICATION #superfamily alpha-crystallin KEYWORDS blocked amino end; eye lens FEATURE !$1 #modified_site blocked amino end (Met) (probably !8acetylated) #status experimental SUMMARY #length 177 #molecular-weight 20680 #checksum 2582 SEQUENCE /// ENTRY CYBOAB #type complete TITLE alpha-crystallin chain B - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 24-Apr-1984 #sequence_revision 31-Dec-1992 #text_change 07-May-1999 ACCESSIONS A42446; A02913; B31352; JC5688 REFERENCE A42446 !$#authors Smith, J.B.; Sun, Y.; Smith, D.L.; Green, B. !$#journal Protein Sci. (1992) 1:601-608 !$#title Identification of the posttranslational modifications of !1bovine lens alphaB-crystallins by mass spectrometry. !$#cross-references MUID:93278289; PMID:1304359 !$#accession A42446 !'##molecule_type protein !'##residues 1-175 ##label SMI !'##note additional details from this paper support the identification !1of residue 80 as Asp REFERENCE A02913 !$#authors van der Ouderaa, F.J.; de Jong, W.W.; Hilderink, A.; !1Bloemendal, H. !$#journal Eur. J. Biochem. (1974) 49:157-168 !$#title The amino-acid sequence of the alphaB-2 chain of bovine !1alpha-crystallin. !$#cross-references MUID:75149531; PMID:4477528 !$#accession A02913 !'##molecule_type protein !'##residues 1-79,'N',81-175 ##label VAN REFERENCE A90153 !$#authors McDermott, M.J.; Chiesa, R.; Spector, A. !$#journal Biochem. Biophys. Res. Commun. (1988) 157:626-631 !$#title Fe(2+) oxidation of alpha-crystallin produces a 43,000 Da !1aggregate composed of A and B chains cross-linked by !1non-reducible covalent bonds. !$#cross-references MUID:89076295; PMID:3202873 !$#accession B31352 !'##molecule_type protein !'##residues 35-47,'T',49;111-135 ##label MCD REFERENCE JC5688 !$#authors Sharma, K.K.; Kaur, H.; Kester, K. !$#journal Biochem. Biophys. Res. Commun. (1997) 239:217-222 !$#title Functional elements in molecular chaperone alpha-crystallin: !1Identification of binding sites in alpha B-crystallin. !$#cross-references MUID:98005109; PMID:9345298 !$#accession JC5688 !'##molecule_type protein !'##residues 1-126,'B',128-175 ##label SHA COMMENT This protein acts as a chaperone in vivo to maintain the !1lens clarity; it looses this activity during aging. CLASSIFICATION #superfamily alpha-crystallin KEYWORDS acetylated amino end; eye lens; molecular chaperone; !1phosphoprotein FEATURE !$57-69,93-107 #domain alcohol dehydrogenase binding #status !8predicted #label ADB\ !$1 #modified_site acetylated amino end (Met) #status !8experimental\ !$19,45,59 #binding_site phosphate (Ser) (covalent) (partial) !8#status experimental SUMMARY #length 175 #molecular-weight 20037 #checksum 7664 SEQUENCE /// ENTRY CYHUAB #type complete TITLE alpha-crystallin chain B [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 27-Nov-1985 #sequence_revision 05-Jan-1996 #text_change 08-Dec-2000 ACCESSIONS A35332; A32288; A02914; S42754; I58184; S58404 REFERENCE A35332 !$#authors Dubin, R.A.; Ally, A.H.; Chung, S.; Piatigorsky, J. !$#journal Genomics (1990) 7:594-601 !$#title Human alphaB-crystallin gene and preferential promoter !1function in lens. !$#cross-references MUID:90353958; PMID:2387586 !$#accession A35332 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-175 ##label DUB !'##cross-references GB:M28638; NID:g181075; PIDN:AAA52104.1; !1PID:g181076 REFERENCE A32288 !$#authors Iwaki, T.; Kume-Iwaki, A.; Liem, R.K.H.; Goldman, J.E. !$#journal Cell (1989) 57:71-78 !$#title alpha-B-crystallin is expressed in non-lenticular tissues !1and accumulates in Alexander's disease brain. !$#cross-references MUID:89195224; PMID:2539261 !$#accession A32288 !'##status preliminary !'##molecule_type mRNA !'##residues 107-175 ##label IWA !'##cross-references GB:M24906; NID:g537531; PIDN:AAA60267.1; !1PID:g537532 REFERENCE A02914 !$#authors Kramps, J.A.; de Man, B.M.; de Jong, W.W. !$#journal FEBS Lett. (1977) 74:82-84 !$#title The primary structure of the B-2 chain of human !1alpha-crystallin. !$#cross-references MUID:77116204; PMID:838078 !$#contents compositions of tryptic, thermolytic, and chymotryptic !1peptides and sequences of residues 57-61 and 150-152 !$#accession A02914 !'##molecule_type protein !'##residues 1-79,'N',81-131,'A',133-175 ##label KRA !'##note the peptides were aligned by homology with the bovine sequence REFERENCE S42754 !$#authors Fujii, N.; Ishibashi, Y.; Satoh, K.; Fujino, M.; Harada, K. !$#journal Biochim. Biophys. Acta (1994) 1204:157-163 !$#title Simultaneous racemization and isomerization at specific !1aspartic acid residues in alpha-B-crystallin from the aged !1human lens. !$#cross-references MUID:94190996; PMID:8142454 !$#accession S42754 !'##status preliminary !'##molecule_type protein !'##residues 1-175 ##label FUJ REFERENCE I58184 !$#authors Iwaki, A.; Iwaki, T.; Goldman, J.E.; Ogomori, K.; Tateishi, !1J.; Sakaki, Y. !$#journal Neurosci. Lett. (1992) 140:89-92 !$#title Accumulation of alpha B-crystallin in brains of patients !1with Alexander's disease is not due to an abnormality of the !15'-flanking and coding sequence of the genomic DNA. !$#cross-references MUID:93025869; PMID:1407707 !$#accession I58184 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-175 ##label RES !'##cross-references GB:S45630; NID:g256398; PIDN:AAB23453.1; !1PID:g256399 REFERENCE S58404 !$#authors van Noort, J.M.; van Sechel, A.C.; Bajramovic, J.J.; El !1Ouagmiri, M.; Polman, C.H.; Lassmann, H.; Ravid, R. !$#journal Nature (1995) 375:798-801 !$#title The small heat-shock protein alpha-B-crystallin as candidate !1autoantigen in multiple sclerosis. !$#cross-references MUID:95319510; PMID:7596414 !$#accession S58404 !'##molecule_type protein !'##residues 23-27,'R';48-50;57-69;124-131 ##label VAN !'##experimental_source myelin from multiple sclerosis-affected white !1matter GENETICS !$#gene GDB:CRYAB; CRYA2 !'##cross-references GDB:119805; OMIM:123590 !$#map_position 11q22.3-11q23.1 CLASSIFICATION #superfamily alpha-crystallin KEYWORDS blocked amino end; eye lens; phosphoprotein FEATURE !$1-175 #product alpha-crystallin chain B #status !8experimental #label MAT\ !$1 #modified_site blocked amino end (Met) (probably !8acetylated) #status experimental SUMMARY #length 175 #molecular-weight 20159 #checksum 9552 SEQUENCE /// ENTRY CYDFAB #type complete TITLE alpha-crystallin chain B - spiny dogfish ORGANISM #formal_name Squalus acanthias #common_name spiny dogfish DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 04-Nov-1994 ACCESSIONS B28190; A02915 REFERENCE A92715 !$#authors de Jong, W.W.; Leunissen, J.A.M.; Leenen, P.J.M.; Zweers, !1A.; Versteeg, M. !$#journal J. Biol. Chem. (1988) 263:5141-5149 !$#title Dogfish alpha-crystallin sequences. Comparison with small !1heat shock proteins and Schistosoma egg antigen. !$#cross-references MUID:88186800; PMID:3356684 !$#accession B28190 !'##molecule_type protein !'##residues 1-177 ##label DE2 CLASSIFICATION #superfamily alpha-crystallin KEYWORDS blocked amino end; eye lens FEATURE !$1 #modified_site blocked amino end (Met) (probably !8acetylated) #status experimental SUMMARY #length 177 #molecular-weight 20254 #checksum 7610 SEQUENCE /// ENTRY HHHU27 #type complete TITLE heat shock protein 27 - human ALTERNATE_NAMES estrogen receptor-related 29K protein; heat shock protein HSP27 ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1988 #sequence_revision 12-Apr-1996 #text_change 22-Jun-1999 ACCESSIONS S12102; S39199; A24017; A41619; A60710; S06875; A47110 REFERENCE S12102 !$#authors Carper, S.W.; Rocheleau, T.A.; Storm, F.K. !$#journal Nucleic Acids Res. (1990) 18:6457 !$#title cDNA sequence of a human heat shock protein HSP27. !$#cross-references MUID:91057161; PMID:2243808 !$#accession S12102 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type mRNA !'##residues 1-205 ##label CAR !'##cross-references EMBL:X54079; NID:g32477; PIDN:CAA38016.1; !1PID:g32478 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1990 !'##note the authors report the presence of two additional cytosines-not !1previously detected due to compression-which results in a !1frameshift and six additional residues REFERENCE S39199 !$#authors Briolay, J.; Chareyron, P.; Mehlen, P.; Arrigo, A. !$#submission submitted to the EMBL Data Library, June 1993 !$#description Identification of a new cDNA sequence from human breast !1carcinoma cells encoding the 28kDa heat shock protein. !$#accession S39199 !'##status preliminary !'##molecule_type mRNA !'##residues 1-205 ##label BRI !'##cross-references EMBL:Z23090; NID:g433597; PIDN:CAA80636.1; !1PID:g433598 REFERENCE A24017 !$#authors Hickey, E.; Brandon, S.E.; Potter, R.; Stein, G.; Stein, J.; !1Weber, L.A. !$#journal Nucleic Acids Res. (1986) 14:4127-4145 !$#title Sequence and organization of genes encoding the human 27 kDa !1heat shock protein. !$#cross-references MUID:86232547; PMID:3714473 !$#accession A24017 !'##molecule_type DNA !'##residues 1-193,'RSCKIR' ##label HIC !'##cross-references GB:L39370; NID:g662840; PIDN:AAA62175.1; !1PID:g662841; GB:X03900; NID:g32475; PID:g32476 REFERENCE A41619 !$#authors Mendelsohn, M.E.; Zhu, Y.; O'Neill, S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:11212-11216 !$#title The 29-kDa proteins phosphorylated in thrombin-activated !1human platelets are forms of the estrogen receptor-related !127-kDa heat shock protein. !$#cross-references MUID:92107919; PMID:1763035 !$#accession A41619 !'##molecule_type mRNA !'##residues 122-193,'RSCKIR' ##label MEN !'##cross-references GB:S74571; NID:g241306; PIDN:AAB20722.1; !1PID:g241307 REFERENCE A60710 !$#authors Strahler, J.R.; Kuick, R.; Eckerskorn, C.; Lottspeich, F.; !1Richardson, B.C.; Fox, D.A.; Stoolman, L.M.; Hanson, C.A.; !1Nichols, D.; Tueche, H.J.; Hanash, S.M. !$#journal J. Clin. Invest. (1990) 85:200-207 !$#title Identification of two related markers for common acute !1lymphoblastic leukemia as heat shock proteins. !$#cross-references MUID:90110479; PMID:2295696 !$#accession A60710 !'##molecule_type protein !'##residues 5-9,'I',11-12;97-112;141-154;172-188 ##label STR REFERENCE S06875 !$#authors Fuqua, S.A.W.; Blum-Salingaros, M.; McGuire, W.L. !$#journal Cancer Res. (1989) 49:4126-4129 !$#title Induction of the estrogen-regulated "24K" protein by heat !1shock. !$#cross-references MUID:89303813; PMID:2743305 !$#accession S06875 !'##molecule_type mRNA !'##residues 109-193,'RSCKIR' ##label FUQ !'##cross-references EMBL:X16477; NID:g35181; PIDN:CAA34498.1; !1PID:g35182 REFERENCE A47110 !$#authors Faucher, C.; Capdevielle, J.; Canal, I.; Ferrara, P.; !1Mazarguil, H.; McGuire, W.L.; Darbon, J.M. !$#journal J. Biol. Chem. (1993) 268:15168-15173 !$#title The 28-kDa protein whose phosphorylation is induced by !1protein kinase C activators in MCF-7 cells belongs to the !1family of low molecular mass heat shock proteins and is the !1estrogen-regulated 24-kDa protein. !$#cross-references MUID:93315498; PMID:8325890 !$#accession A47110 !'##status preliminary !'##molecule_type protein !'##residues 172-186 ##label FAU !'##experimental_source mammary adenocarcinoma MCF-7 cells !'##note sequence extracted from NCBI backbone (NCBIP:135009) COMMENT In platelets, this protein in rapidly phosphorylated after !1cellular activation by thrombin. GENETICS !$#gene GDB:HSPB1 !'##cross-references GDB:127602 !$#map_position Xpter-Xqter !$#introns 121/3; 143/3 CLASSIFICATION #superfamily alpha-crystallin KEYWORDS heat shock; phosphoprotein; stress-induced protein SUMMARY #length 205 #molecular-weight 22782 #checksum 9932 SEQUENCE /// ENTRY HHKW48 #type complete TITLE heat shock protein 16-48 - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 25-Feb-1985 #sequence_revision 19-Oct-1995 #text_change 29-Oct-1999 ACCESSIONS A24289; S31036; A02916; T25928; T25929 REFERENCE A24289 !$#authors Russnak, R.H.; Candido, E.P.M. !$#journal Mol. Cell. Biol. (1985) 5:1268-1278 !$#cross-references MUID:85295957; PMID:4033652 !$#accession A24289 !'##molecule_type DNA !'##residues 1-143 ##label RUS !'##cross-references EMBL:K03273; NID:g156333; PIDN:AAA28069.1; !1PID:g156337 REFERENCE S31036 !$#authors Kay, R.J.; Russnak, R.H.; Jones, D.; Mathias, C.; Candido, !1E.P.M. !$#journal Nucleic Acids Res. (1987) 15:3723-3741 !$#title Expression of intron-containing C. elegans heat shock genes !1in mouse cells demonstrates divergence of 3' splice site !1recognition sequences between nematodes and vertebrates, and !1an inhibitory effect of heat shock on the mammalian splicing !1apparatus. !$#cross-references MUID:87231065; PMID:3588308 !$#accession S31036 !'##status translation not shown !'##molecule_type DNA !'##residues 46-67 ##label KAY !'##cross-references EMBL:M31339; NID:g156341; PIDN:AAA28072.1; !1PID:g156342 REFERENCE A93467 !$#authors Russnak, R.H.; Jones, D.; Candido, E.P.M. !$#journal Nucleic Acids Res. (1983) 11:3187-3205 !$#title Cloning and analysis of cDNA sequences coding for two 16 !1kilodalton heat shock protein (hsps) in Caenorhabditis !1elegans: homology with the small hsps of Drosophila. !$#cross-references MUID:83220736; PMID:6190129 !$#accession A02916 !'##molecule_type mRNA !'##residues 9-143 ##label RU2 !'##cross-references GB:X01576; GB:K01863; NID:g6756; PIDN:CAA25731.1; !1PID:g6757 REFERENCE Z20111 !$#authors Bradshaw, H. !$#submission submitted to the EMBL Data Library, July 1996 !$#description The sequence of C. elegans cosmid T27E4. !$#accession T25928 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-143 ##label BRA !'##cross-references EMBL:U64837; PIDN:AAB04840.1; GSPDB:GN00023; !1CESP:T27E4.3 !'##experimental_source strain Bristol N2; clone T27E4 !$#accession T25929 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-143 ##label BR2 !'##cross-references EMBL:U64837; PIDN:AAB04841.1; GSPDB:GN00023; !1CESP:T27E4.9 !'##experimental_source strain Bristol N2; clone T27E4 GENETICS !$#gene CESP:T27E4.3; CESP:T27E4.9 !$#map_position 5 !$#introns 46/3 CLASSIFICATION #superfamily alpha-crystallin KEYWORDS heat shock; stress-induced protein SUMMARY #length 143 #molecular-weight 16299 #checksum 5284 SEQUENCE /// ENTRY HHKW41 #type complete TITLE heat shock protein 16-41 - Caenorhabditis elegans ALTERNATE_NAMES heat shock protein 16 2 ORGANISM #formal_name Caenorhabditis elegans DATE 25-Feb-1985 #sequence_revision 19-Oct-1995 #text_change 22-Jun-1999 ACCESSIONS A25199; A38884; A02917 REFERENCE A92555 !$#authors Jones, D.; Russnak, R.H.; Kay, R.J.; Candido, E.P.M. !$#journal J. Biol. Chem. (1986) 261:12006-12015 !$#title Structure, expression, and evolution of a heat shock gene !1locus in Caenorhabditis elegans that is flanked by !1repetitive elements. !$#cross-references MUID:86304344; PMID:3017958 !$#accession A25199 !'##molecule_type DNA !'##residues 1-143 ##label JON REFERENCE A38884 !$#authors Candido, E.P.M. !$#submission submitted to GenBank, November 1985 !$#accession A38884 !'##molecule_type mRNA !'##residues 47-143 ##label CAN !'##cross-references GB:X01577; NID:g6758; PIDN:CAA25732.1; PID:g780186 REFERENCE A93467 !$#authors Russnak, R.H.; Jones, D.; Candido, E.P.M. !$#journal Nucleic Acids Res. (1983) 11:3187-3205 !$#title Cloning and analysis of cDNA sequences coding for two 16 !1kilodalton heat shock protein (hsps) in Caenorhabditis !1elegans: homology with the small hsps of Drosophila. !$#cross-references MUID:83220736; PMID:6190129 !$#accession A02917 !'##molecule_type mRNA !'##residues 'KLCSFFQ',47-143 ##label RUS !'##cross-references GB:K01864; NID:g156331; PIDN:AAA28065.1; !1PID:g156332 !'##note the authors translated the codon UUG for residue 46 as Phe !'##note this sequence has been revised in reference A38884 CLASSIFICATION #superfamily alpha-crystallin KEYWORDS heat shock; stress-induced protein SUMMARY #length 143 #molecular-weight 16252 #checksum 4180 SEQUENCE /// ENTRY HHFF22 #type complete TITLE heat shock protein 22 - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 15-Nov-1984 #sequence_revision 15-Nov-1984 #text_change 16-Feb-1997 ACCESSIONS A02918 REFERENCE A93909 !$#authors Ingolia, T.D.; Craig, E.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:2360-2364 !$#title Four small Drosophila heat shock proteins are related to !1each other and to mammalian alpha-crystallin. !$#cross-references MUID:82248004; PMID:6285380 !$#accession A02918 !'##molecule_type DNA !'##residues 1-174 ##label ING !'##note the authors translated the codon CAT for residue 44 as Gln, GAG !1for residue 83 as Gly, GAG for residue 89 as Gly, and GCA !1for residue 90 as Gly !'##note the codon usage table proposed by the authors and the !1translation of the protein by the authors are inconsistent !1with our translation from the DNA sequence COMMENT This small heat shock protein is related to alpha !1crystallin. GENETICS !$#gene FlyBase:Hsp22 !'##cross-references FlyBase:FBgn0001223 !$#map_position 3L (67B) CLASSIFICATION #superfamily alpha-crystallin KEYWORDS heat shock; stress-induced protein SUMMARY #length 174 #molecular-weight 19822 #checksum 886 SEQUENCE /// ENTRY HHFF23 #type complete TITLE heat shock protein 23 - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 15-Nov-1984 #sequence_revision 15-Nov-1984 #text_change 16-Feb-1997 ACCESSIONS A02919 REFERENCE A93909 !$#authors Ingolia, T.D.; Craig, E.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:2360-2364 !$#title Four small Drosophila heat shock proteins are related to !1each other and to mammalian alpha-crystallin. !$#cross-references MUID:82248004; PMID:6285380 !$#accession A02919 !'##molecule_type DNA !'##residues 1-186 ##label ING !'##note the authors translated the codon CCC for residue 25 as Leu, CGA !1for residue 32 as Gly, and GTG for residue 95 as Leu !'##note the codon usage table proposed by the authors and the !1translation of the protein by the authors are inconsistent !1with our translation from the DNA sequence COMMENT This small heat shock protein is related to alpha !1crystallin. GENETICS !$#gene FlyBase:Hsp23 !'##cross-references FlyBase:FBgn0001224 !$#map_position 3L (67B) CLASSIFICATION #superfamily alpha-crystallin KEYWORDS heat shock; stress-induced protein SUMMARY #length 186 #molecular-weight 20430 #checksum 8685 SEQUENCE /// ENTRY HHFF26 #type complete TITLE heat shock protein 26 - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 15-Nov-1984 #sequence_revision 15-Nov-1984 #text_change 16-Feb-1997 ACCESSIONS A02920 REFERENCE A93909 !$#authors Ingolia, T.D.; Craig, E.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:2360-2364 !$#title Four small Drosophila heat shock proteins are related to !1each other and to mammalian alpha-crystallin. !$#cross-references MUID:82248004; PMID:6285380 !$#accession A02920 !'##molecule_type DNA !'##residues 1-209 ##label ING !'##note the authors translated the codon GAC for residue 15 as Glu, CAG !1for residue 22 as Glu, GGC for residue 131 as Arg, and GAG !1for residue 166 as Gln !'##note the codon usage table proposed by the authors and the !1translation of the protein by the authors are inconsistent !1with our translation from the DNA sequence COMMENT This small heat shock protein is related to alpha !1crystallin. GENETICS !$#gene FlyBase:Hsp26 !'##cross-references FlyBase:FBgn0001225 !$#map_position 3L (67B) CLASSIFICATION #superfamily alpha-crystallin KEYWORDS heat shock; stress-induced protein SUMMARY #length 209 #molecular-weight 22910 #checksum 5209 SEQUENCE /// ENTRY HHFF27 #type complete TITLE heat shock protein 27 - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 15-Nov-1984 #sequence_revision 15-Nov-1984 #text_change 16-Feb-1997 ACCESSIONS A02921 REFERENCE A93909 !$#authors Ingolia, T.D.; Craig, E.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:2360-2364 !$#title Four small Drosophila heat shock proteins are related to !1each other and to mammalian alpha-crystallin. !$#cross-references MUID:82248004; PMID:6285380 !$#accession A02921 !'##molecule_type DNA !'##residues 1-213 ##label ING !'##note the authors translated the codon GAG for residue 123 as Gly and !1GAG for residue 155 as Asp !'##note the codon usage table proposed by the authors and the !1translation of the protein by the authors are inconsistent !1with our translation from the DNA sequence COMMENT This small heat shock protein is related to alpha !1crystallin. GENETICS !$#gene FlyBase:Hsp27 !'##cross-references FlyBase:FBgn0001226 !$#map_position 3L (67B) CLASSIFICATION #superfamily alpha-crystallin KEYWORDS heat shock; stress-induced protein SUMMARY #length 213 #molecular-weight 23598 #checksum 478 SEQUENCE /// ENTRY HHFF67 #type complete TITLE heat shock protein 67B1 - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 22-Jun-1999 ACCESSIONS A24675 REFERENCE A24675 !$#authors Ayme, A.; Tissieres, A. !$#journal EMBO J. (1985) 4:2949-2954 !$#title Locus 67B of Drosophila melanogaster contains seven, not !1four, closely related heat shock genes. !$#cross-references MUID:86055735; PMID:3933974 !$#accession A24675 !'##molecule_type DNA !'##residues 1-238 ##label AYM !'##cross-references GB:M26267; NID:g157686; PIDN:AAA28634.1; !1PID:g157687 GENETICS !$#gene FlyBase:Hsp67Ba !'##cross-references FlyBase:FBgn0001227 !$#map_position 3L (67B) CLASSIFICATION #superfamily alpha-crystallin KEYWORDS heat shock; stress-induced protein SUMMARY #length 238 #molecular-weight 26591 #checksum 7898 SEQUENCE /// ENTRY HHSY17 #type complete TITLE heat shock protein 17 - soybean ALTERNATE_NAMES heat shock protein 6871 ORGANISM #formal_name Glycine max #common_name soybean DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 22-Jun-1999 ACCESSIONS A02922; T07627 REFERENCE A90994 !$#authors Schoffl, F.; Raschke, E.; Nagao, R.T. !$#journal EMBO J. (1984) 3:2491-2497 !$#title The DNA sequence analysis of soybean heat-shock genes and !1identification of possible regulatory promoter elements. !$#accession A02922 !'##molecule_type DNA !'##residues 1-153 ##label SCH REFERENCE Z16061 !$#authors Schoeffl, F. !$#submission submitted to the EMBL Data Library, August 1985 !$#accession T07627 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-153 ##label SC2 !'##cross-references EMBL:X01104; NID:g18655; PIDN:CAA25578.1; !1PID:g18656 GENETICS !$#gene hs6871 CLASSIFICATION #superfamily alpha-crystallin KEYWORDS heat shock; stress-induced protein SUMMARY #length 153 #molecular-weight 17347 #checksum 2927 SEQUENCE /// ENTRY HHSY34 #type fragment TITLE heat shock protein 34 - soybean (fragment) ORGANISM #formal_name Glycine max #common_name soybean DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 15-Nov-1996 ACCESSIONS A02923 REFERENCE A90994 !$#authors Schoffl, F.; Raschke, E.; Nagao, R.T. !$#journal EMBO J. (1984) 3:2491-2497 !$#title The DNA sequence analysis of soybean heat-shock genes and !1identification of possible regulatory promoter elements. !$#accession A02923 !'##molecule_type DNA !'##residues 1-74 ##label SCH GENETICS !$#gene hs6834 CLASSIFICATION #superfamily alpha-crystallin KEYWORDS heat shock; stress-induced protein SUMMARY #length 74 #checksum 9754 SEQUENCE /// ENTRY CYPZ77 #type complete TITLE heat shock protein (clone DChsp17.7) - carrot ORGANISM #formal_name Daucus carota #common_name carrot DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 22-Jun-1999 ACCESSIONS S14999; S18260 REFERENCE S14999 !$#authors Darwish, K.; Wang, L.; Hwang, C.H.; Apuya, N.; Zimmerman, !1J.L. !$#journal Plant Mol. Biol. (1991) 16:729-731 !$#title Cloning and characterization of genes encoding low molecular !1weight heat shock proteins from carrot. !$#cross-references MUID:91329706; PMID:1840684 !$#accession S14999 !'##molecule_type DNA !'##residues 1-157 ##label DAR !'##cross-references EMBL:X53851 REFERENCE S18260 !$#authors Zimmerman, J. !$#submission submitted to the EMBL Data Library, July 1990 !$#accession S18260 !'##molecule_type DNA !'##residues 1-135,'V',137-157 ##label ZIM !'##cross-references EMBL:X53851; NID:g18352; PIDN:CAA37847.1; !1PID:g18353 CLASSIFICATION #superfamily alpha-crystallin KEYWORDS heat shock; stress-induced protein SUMMARY #length 157 #molecular-weight 17785 #checksum 2489 SEQUENCE /// ENTRY CYPZ79 #type complete TITLE heat shock protein (clone DChsp17.9) - carrot ORGANISM #formal_name Daucus carota #common_name carrot DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 22-Jun-1999 ACCESSIONS S15000 REFERENCE S14999 !$#authors Darwish, K.; Wang, L.; Hwang, C.H.; Apuya, N.; Zimmerman, !1J.L. !$#journal Plant Mol. Biol. (1991) 16:729-731 !$#title Cloning and characterization of genes encoding low molecular !1weight heat shock proteins from carrot. !$#cross-references MUID:91329706; PMID:1840684 !$#accession S15000 !'##molecule_type DNA !'##residues 1-159 ##label DAR !'##cross-references EMBL:X53852; NID:g18354; PIDN:CAA37848.1; !1PID:g18355 !'##note the authors translated the codon CAT for residue 156 as Asp CLASSIFICATION #superfamily alpha-crystallin KEYWORDS heat shock; stress-induced protein SUMMARY #length 159 #molecular-weight 18032 #checksum 178 SEQUENCE /// ENTRY HHWT17 #type complete TITLE heat shock protein 17 - wheat ORGANISM #formal_name Triticum aestivum #common_name common wheat DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 22-Jun-1999 ACCESSIONS S03178 REFERENCE S03178 !$#authors McElwain, E.F.; Spiker, S. !$#journal Nucleic Acids Res. (1989) 17:1764 !$#title A wheat cDNA clone which is homologous to the 17 kd !1heat-shock protein gene family of soybean. !$#cross-references MUID:89160335; PMID:2922294 !$#accession S03178 !'##molecule_type mRNA !'##residues 1-151 ##label MCE !'##cross-references EMBL:X13431; NID:g21812; PIDN:CAA31785.1; !1PID:g21813 CLASSIFICATION #superfamily alpha-crystallin KEYWORDS heat shock; stress-induced protein SUMMARY #length 151 #molecular-weight 16878 #checksum 4608 SEQUENCE /// ENTRY HHPM17 #type complete TITLE heat shock protein 17.7 - garden pea ORGANISM #formal_name Pisum sativum #common_name garden pea DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 15-Nov-1996 ACCESSIONS S12720 REFERENCE S12720 !$#authors Lauzon, L.M.; Helm, K.W.; Vierling, E. !$#journal Nucleic Acids Res. (1990) 18:4274 !$#title A cDNA clone from Pisum sativum encoding a low molecular !1weight heat shock protein. !$#cross-references MUID:90332446; PMID:2377479 !$#accession S12720 !'##molecule_type mRNA !'##residues 1-157 ##label LAU !'##cross-references EMBL:M33901 CLASSIFICATION #superfamily alpha-crystallin KEYWORDS heat shock; stress-induced protein SUMMARY #length 157 #molecular-weight 17732 #checksum 3606 SEQUENCE /// ENTRY HHMU17 #type complete TITLE heat shock protein 17.6-II [similarity] - Arabidopsis thaliana ALTERNATE_NAMES protein F14F18.190 ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-May-2000 ACCESSIONS S20871; T48561; S19816 REFERENCE S20871 !$#authors Bartling, D.; Buelter, H.; Liebeton, K.; Weiler, E.W. !$#journal Plant Mol. Biol. (1992) 18:1007-1008 !$#title An Arabidopsis thaliana cDNA clone encoding a 17.6 kDa class !1II heat shock protein. !$#cross-references MUID:92256800; PMID:1581560 !$#accession S20871 !'##molecule_type mRNA !'##residues 1-155 ##label BAR !'##cross-references EMBL:X63443; NID:g16337; PIDN:CAA45039.1; !1PID:g16338 REFERENCE Z24490 !$#authors Bevan, M.; Hilbert, H.; Braun, M.; Holzer, E.; Brandt, A.; !1Duesterhoeft, A.; Bancroft, I.; Mewes, H.W.; Rudd, S.; !1Lemcke, K.; Mayer, K.F.X. !$#submission submitted to the Protein Sequence Database, April 2000 !$#accession T48561 !'##status preliminary !'##molecule_type DNA !'##residues 1-155 ##label BEV !'##cross-references EMBL:AL163812 !'##experimental_source cultivar Columbia; BAC clone F14F18 GENETICS !$#map_position 5 !$#note F14F18.190 CLASSIFICATION #superfamily alpha-crystallin KEYWORDS heat shock; stress-induced protein SUMMARY #length 155 #molecular-weight 17623 #checksum 8521 SEQUENCE /// ENTRY HHPM21 #type complete TITLE heat shock protein 21 precursor - garden pea ORGANISM #formal_name Pisum sativum #common_name garden pea DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 22-Jun-1999 ACCESSIONS S00374 REFERENCE S00374 !$#authors Vierling, E.; Nagao, R.T.; DeRocher, A.E.; Harris, L.M. !$#journal EMBO J. (1988) 7:575-581 !$#title A heat shock protein localized to chloroplasts is a member !1of a eukaryotic superfamily of heat shock proteins. !$#cross-references MUID:88283623; PMID:3396532 !$#accession S00374 !'##molecule_type mRNA !'##residues 1-232 ##label VIE !'##cross-references EMBL:X07187; NID:g20763; PIDN:CAA30167.1; !1PID:g20764 CLASSIFICATION #superfamily alpha-crystallin KEYWORDS chloroplast; heat shock; stress-induced protein FEATURE !$1-47 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$48-232 #product heat shock protein 21 #status predicted !8#label MAT SUMMARY #length 232 #molecular-weight 26179 #checksum 5905 SEQUENCE /// ENTRY JN0275 #type complete TITLE heat shock protein 30D - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 09-Oct-1992 #sequence_revision 03-Nov-1995 #text_change 22-Jun-1999 ACCESSIONS JN0275; S23793 REFERENCE JN0274 !$#authors Krone, P.H.; Snow, A.; Ali, A.; Pasternak, J.J.; Heikkila, !1J.J. !$#journal Gene (1992) 110:159-166 !$#title Comparison of regulatory and structural regions of the !1Xenopus laevis small heat-shock protein-encoding gene !1family. !$#cross-references MUID:92165054; PMID:1537552 !$#accession JN0275 !'##molecule_type DNA !'##residues 1-215 ##label KRO !'##cross-references GB:X57963; NID:g64791; PIDN:CAA41031.1; PID:g64792 GENETICS !$#gene hsp30D !$#note closely linked to hsp30C and hsp30E; hsp30A and hsp30B form !1another linkage groupc CLASSIFICATION #superfamily alpha-crystallin KEYWORDS heat shock; stress-induced protein SUMMARY #length 215 #molecular-weight 24522 #checksum 2195 SEQUENCE /// ENTRY JN0274 #type complete TITLE heat shock protein 30C - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 09-Oct-1992 #sequence_revision 03-Nov-1995 #text_change 22-Jun-1999 ACCESSIONS JN0274; S23792 REFERENCE JN0274 !$#authors Krone, P.H.; Snow, A.; Ali, A.; Pasternak, J.J.; Heikkila, !1J.J. !$#journal Gene (1992) 110:159-166 !$#title Comparison of regulatory and structural regions of the !1Xenopus laevis small heat-shock protein-encoding gene !1family. !$#cross-references MUID:92165054; PMID:1537552 !$#accession JN0274 !'##molecule_type DNA !'##residues 1-213 ##label KRO !'##cross-references GB:X57962; NID:g64789; PIDN:CAA41030.1; PID:g64790 GENETICS !$#gene hsp30C !$#note closely linked to hsp30D and hsp30E; hsp30A and hsp30B form !1another linkage groupc CLASSIFICATION #superfamily alpha-crystallin KEYWORDS heat shock; stress-induced protein SUMMARY #length 213 #molecular-weight 24199 #checksum 6149 SEQUENCE /// ENTRY CYBOB #type complete TITLE beta-crystallin B2 [validated] - bovine ALTERNATE_NAMES beta-crystallin chain Bp ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 01-Sep-1981 #sequence_revision 12-May-1995 #text_change 15-Sep-2000 ACCESSIONS A54730; A02924 REFERENCE A54730 !$#authors Hogg, D.; Gorin, M.B.; Heinzmann, C.; Zollman, S.; Mohandas, !1T.; Klisak, I.; Sparkes, R.S.; Breitman, M.; Tsui, L.C.; !1Horwitz, J. !$#journal Curr. Eye Res. (1987) 6:1335-1342 !$#title Nucleotide sequence for the cDNA of the bovine betaB2 !1crystallin and assignment of the orthologous human locus to !1chromosome 22. !$#cross-references MUID:88110635; PMID:3427982 !$#accession A54730 !'##molecule_type mRNA !'##residues 1-205 ##label HOG !'##cross-references GB:M22466; NID:g162911; PIDN:AAA30472.1; !1PID:g162912 REFERENCE A02924 !$#authors Driessen, H.P.C.; Herbrink, P.; Bloemendal, H.; de Jong, !1W.W. !$#journal Eur. J. Biochem. (1981) 121:83-91 !$#title Primary structure of the bovine beta-crystallin Bp chain. !1Internal duplication and homology with gamma-crystallin. !$#cross-references MUID:82117057; PMID:7035168 !$#accession A02924 !'##molecule_type protein !'##residues 2-3,'N',5,'E',7-27,'H',29-31,'Q',33-34,'BPGB',39,'C',41-205 !1##label DRI REFERENCE A51450 !$#authors Bax, B.; Lapatto, R.; Nalini, V.; Driessen, H.; Lindley, !1P.F.; Mahadevan, D.; Blundell, T.L.; Slingsby, C. !$#submission submitted to the Brookhaven Protein Data Bank, September !11992 !$#cross-references PDB:2BB2 !$#contents annotation; X-ray crystallography, 2.1 angstroms, residues !115-195 REFERENCE A58563 !$#authors Bax, B.; Lapatlo, R.; Nalini, V.; Driessen, H.; Lindley, !1P.F.; Mahadevan, D.; Blundell, T.L.; Slingsby, C. !$#journal Nature (1990) 347:776-780 !$#title X-ray analysis of beta B2-crystallin and evolution of !1oligomeric lens proteins. !$#cross-references MUID:91043031; PMID:2234050 !$#contents annotation; X-ray crystallography, 2.1 angstroms CLASSIFICATION #superfamily beta-crystallin KEYWORDS acetylated amino end; duplication; eye lens FEATURE !$2-205 #product beta-crystallin B2 #status experimental !8#label MAT\ !$17-56 #domain crystallin repeat #label GK1\ !$57-101 #domain crystallin repeat #label GK2\ !$107-148 #domain crystallin repeat #label GK3\ !$149-191 #domain crystallin repeat #label GK4\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental SUMMARY #length 205 #molecular-weight 23298 #checksum 33 SEQUENCE /// ENTRY CYRTB1 #type complete TITLE beta-crystallin B1 precursor - rat CONTAINS beta B1b crystallin ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 22-Jun-1999 ACCESSIONS A02925; B02925; S33586 REFERENCE A90654 !$#authors den Dunnen, J.T.; Moormann, R.J.M.; Schoenmakers, J.G.G. !$#journal Biochim. Biophys. Acta (1985) 824:295-303 !$#title Rat lens beta-crystallins are internally duplicated and !1homologous to gamma-crystallins. !$#cross-references MUID:85175137; PMID:3879970 !$#accession A02925 !'##molecule_type DNA !'##residues 1-50 ##label DE1 !'##cross-references GB:X06377; NID:g56014; PIDN:CAA29679.1; PID:g56015 !$#accession B02925 !'##molecule_type mRNA !'##residues 34-249 ##label DE2 REFERENCE S33586 !$#authors David, L.L.; Shearer, T.R. !$#journal FEBS Lett. (1993) 324:265-270 !$#title beta-crystallins insolubilized by calpain II in vitro !1contain cleavage sites similar to beta-crystallins !1insolubilized during cataract. !$#cross-references MUID:94009594; PMID:8405363 !$#accession S33586 !'##molecule_type protein !'##residues 50-55,233,'X',235-238,'X',240 ##label DAV CLASSIFICATION #superfamily beta-crystallin KEYWORDS duplication; eye lens FEATURE !$12-249 #product beta-crystallin B1b #status predicted #label !8BBC\ !$56-95 #domain crystallin repeat #label GK1\ !$96-140 #domain crystallin repeat #label GK2\ !$146-187 #domain crystallin repeat #label GK3\ !$188-230 #domain crystallin repeat #label GK4 SUMMARY #length 249 #molecular-weight 28043 #checksum 4754 SEQUENCE /// ENTRY CYCHB1 #type complete TITLE beta-crystallin B1 precursor - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 10-Dec-1999 ACCESSIONS S53533; A25628 REFERENCE S53533 !$#authors Duncan, M.K.; Roth, H.J.; Thompson, M.; Kantorow, M.; !1Piatigorsky, J. !$#journal Biochim. Biophys. Acta (1995) 1261:68-76 !$#title Chicken beta-B1 crystallin: gene sequence and evidence for !1functional conservation of promoter activity between chicken !1and mouse. !$#cross-references MUID:95200974; PMID:7893762 !$#accession S53533 !'##status preliminary !'##molecule_type DNA !'##residues 1-238 ##label DUN REFERENCE A25628 !$#authors Hejtmancik, J.F.; Thompson, M.A.; Wistow, G.; Piatigorsky, !1J. !$#journal J. Biol. Chem. (1986) 261:982-987 !$#title cDNA and deduced protein sequence for the beta-B1-crystallin !1polypeptide of the chicken lens. !$#cross-references MUID:86085945; PMID:3753603 !$#accession A25628 !'##molecule_type mRNA !'##residues 1-238 ##label HEJ !'##cross-references GB:M11619; NID:g211666; PIDN:AAA48723.1; !1PID:g211667 COMMENT This beta crystallin is synthesized specifically in the !1elongating lens cells. CLASSIFICATION #superfamily beta-crystallin KEYWORDS duplication; eye lens FEATURE !$46-85 #domain crystallin repeat #label GK1\ !$86-130 #domain crystallin repeat #label GK2\ !$136-177 #domain crystallin repeat #label GK3\ !$178-220 #domain crystallin repeat #label GK4 SUMMARY #length 238 #molecular-weight 27267 #checksum 8147 SEQUENCE /// ENTRY CYRTB3 #type complete TITLE beta-crystallin B3 - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 22-Jun-1999 ACCESSIONS A02926; S33588 REFERENCE A90654 !$#authors den Dunnen, J.T.; Moormann, R.J.M.; Schoenmakers, J.G.G. !$#journal Biochim. Biophys. Acta (1985) 824:295-303 !$#title Rat lens beta-crystallins are internally duplicated and !1homologous to gamma-crystallins. !$#cross-references MUID:85175137; PMID:3879970 !$#accession A02926 !'##molecule_type mRNA !'##residues 1-211 ##label DEN !'##cross-references GB:X05899; GB:M15901; NID:g56018; PIDN:CAA29328.1; !1PID:g56019 REFERENCE S33586 !$#authors David, L.L.; Shearer, T.R. !$#journal FEBS Lett. (1993) 324:265-270 !$#title beta-crystallins insolubilized by calpain II in vitro !1contain cleavage sites similar to beta-crystallins !1insolubilized during cataract. !$#cross-references MUID:94009594; PMID:8405363 !$#accession S33588 !'##molecule_type protein !'##residues 6-11,16-23 ##label DAV CLASSIFICATION #superfamily beta-crystallin KEYWORDS duplication; eye lens FEATURE !$24-63 #domain crystallin repeat #label GK1\ !$64-108 #domain crystallin repeat #label GK2\ !$114-155 #domain crystallin repeat #label GK3\ !$156-198 #domain crystallin repeat #label GK4 SUMMARY #length 211 #molecular-weight 24276 #checksum 3240 SEQUENCE /// ENTRY CYHUB3 #type complete TITLE beta-crystallin A3 precursor - human CONTAINS beta crystallin A1 ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 02-Sep-1997 ACCESSIONS A25202 REFERENCE A25202 !$#authors Hogg, D.; Tsui, L.C.; Gorin, M.; Breitman, M.L. !$#journal J. Biol. Chem. (1986) 261:12420-12427 !$#title Characterization of the human beta-crystallin gene !1Hu-beta-A3/A1 reveals ancestral relationships among the !1beta-gamma-crystallin superfamily. !$#cross-references MUID:86304407; PMID:3745196 !$#accession A25202 !'##molecule_type mRNA !'##residues 1-215 ##label HOG GENETICS !$#gene GDB:CRYBA1; CRYB1 !'##cross-references GDB:119806; OMIM:123610 !$#map_position 17q11.2-17q12 !$#introns 11/1; 32/3; 72/2; 119/3; 167/2 CLASSIFICATION #superfamily beta-crystallin KEYWORDS duplication; eye lens FEATURE !$18-215 #product beta-crystallin A1 #status predicted #label !8CA1\ !$31-70 #domain crystallin repeat #label GK1\ !$71-118 #domain crystallin repeat #label GK2\ !$124-165 #domain crystallin repeat #label GK3\ !$166-214 #domain crystallin repeat #label GK4 SUMMARY #length 215 #molecular-weight 25275 #checksum 8724 SEQUENCE /// ENTRY CYMSB #type complete TITLE beta-crystallin - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 17-Dec-1982 #sequence_revision 17-Mar-1987 #text_change 16-Jun-2000 ACCESSIONS A02927; B02927 REFERENCE A93298 !$#authors Inana, G.; Piatigorsky, J.; Norman, B.; Slingsby, C.; !1Blundell, T. !$#journal Nature (1983) 302:310-315 !$#title Gene and protein structure of a beta-crystallin polypeptide !1in murine lens: relationship of exons and structural motifs. !$#cross-references MUID:83167473; PMID:6835368 !$#accession A02927 !'##molecule_type DNA !'##residues 1-54 ##label IN1 REFERENCE A92384 !$#authors Inana, G.; Shinohara, T.; Maizel Jr., J.V.; Piatigorsky, J. !$#journal J. Biol. Chem. (1982) 257:9064-9071 !$#title Evolution and diversity of the crystallins. Nucleotide !1sequence of a beta-crystallin mRNA from the mouse lens. !$#cross-references MUID:82239402; PMID:6896514 !$#accession B02927 !'##molecule_type mRNA !'##residues 16-198 ##label IN2 !'##cross-references GB:V00728; NID:g50538; PIDN:CAA24106.1; !1PID:g1333886 COMMENT This protein contains four similar motifs with most striking !1similarities between motifs 1 and 3 and between motifs 2 and !14. GENETICS !$#introns 55/2 !$#note the list of introns may be incomplete CLASSIFICATION #superfamily beta-crystallin KEYWORDS duplication; eye lens FEATURE !$14-53 #domain crystallin repeat #label GK1\ !$54-101 #domain crystallin repeat #label GK2\ !$107-148 #domain crystallin repeat #label GK3\ !$149-197 #domain crystallin repeat #label GK4 SUMMARY #length 198 #molecular-weight 23402 #checksum 8473 SEQUENCE /// ENTRY CYBOS #type complete TITLE gamma-s-crystallin - bovine ALTERNATE_NAMES beta-s crystallin ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 24-Nov-1999 ACCESSIONS A91017; A91607; A24643; JE0064 REFERENCE A91017 !$#authors Quax-Jeuken, Y.; Driessen, H.; Leunissen, J.; Quax, W.; de !1Jong, W.; Bloemendal, H. !$#journal EMBO J. (1985) 4:2597-2602 !$#title Beta-s-crystallin: structure and evolution of a distinct !1member of the beta-gamma-superfamily. !$#cross-references MUID:86030239; PMID:4054100 !$#accession A91017 !'##molecule_type mRNA !'##residues 1-178 ##label QUA !'##cross-references GB:X03006; NID:g152; PIDN:CAA26791.1; PID:g153 !'##note part of this sequence was confirmed by protein sequencing REFERENCE A91607 !$#authors van Rens, G.L.M.; Raats, J.M.H.; Driessen, H.P.C.; !1Oldenburg, M.; Wijnen, J.T.; Khan, P.M.; de Jong, W.W.; !1Bloemendal, H. !$#journal Gene (1989) 78:225-233 !$#title Structure of the bovine eye lens gamma s-crystallin gene !1(formerly beta s). !$#cross-references MUID:89378749; PMID:2476364 !$#accession A91607 !'##molecule_type DNA !'##residues 1-178 ##label VAN !'##cross-references GB:M21095; NID:g162923; PIDN:AAA30477.1; !1PID:g162925 GENETICS !$#introns 7/3; 88/3 CLASSIFICATION #superfamily beta-crystallin KEYWORDS blocked amino end; duplication; eye lens FEATURE !$2-178 #product gamma-s-crystallin #status experimental !8#label MPT\ !$6-44 #domain crystallin repeat #label GK1\ !$45-87 #domain crystallin repeat #label GK2\ !$93-134 #domain crystallin repeat #label GK3\ !$135-177 #domain crystallin repeat #label GK4\ !$2 #modified_site blocked amino end (Ser) (in mature !8form) #status experimental SUMMARY #length 178 #molecular-weight 20927 #checksum 9588 SEQUENCE /// ENTRY CYHUG1 #type complete TITLE gamma-crystallin 1-2 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 22-Jun-1999 ACCESSIONS A24520 REFERENCE A91536 !$#authors den Dunnen, J.T.; Moormann, R.J.M.; Cremers, F.P.M.; !1Schoenmakers, J.G.G. !$#journal Gene (1985) 38:197-204 !$#title Two human gamma-crystallin genes are linked and riddled with !1Alu-repeats. !$#cross-references MUID:86056977; PMID:4065573 !$#accession A24520 !'##molecule_type DNA !'##residues 1-175 ##label DEN !'##cross-references GB:M11971; NID:g181114; PIDN:AAA52113.1; !1PID:g181118 GENETICS !$#gene GDB:CRYGA; CRYG1 !'##cross-references GDB:119076; OMIM:123660 !$#map_position 2q33-2q35 !$#introns 3/3; 84/3 CLASSIFICATION #superfamily beta-crystallin KEYWORDS duplication; eye lens FEATURE !$2-175 #product gamma-crystallin 1-2 #status predicted !8#label MPT\ !$2-40 #domain crystallin repeat #label GK1\ !$41-83 #domain crystallin repeat #label GK2\ !$89-129 #domain crystallin repeat #label GK3\ !$130-169 #domain crystallin repeat #label GK4 SUMMARY #length 175 #molecular-weight 20907 #checksum 4897 SEQUENCE /// ENTRY CYBOG #type complete TITLE gamma-crystallin II - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 28-Feb-1986 #sequence_revision 03-Feb-1994 #text_change 24-Sep-1999 ACCESSIONS A29655; A02928; A90263; A60890; A60815; A02929; S04265 REFERENCE A90133 !$#authors Hay, R.E.; Woods, W.D.; Church, R.L.; Petrash, J.M. !$#journal Biochem. Biophys. Res. Commun. (1987) 146:332-338 !$#title cDNA clones encoding bovine gamma-crystallins. !$#cross-references MUID:87270760; PMID:3606621 !$#accession A29655 !'##molecule_type mRNA !'##residues 1-175 ##label HAY !'##cross-references GB:M16894; NID:g162918; PIDN:AAA30476.1; !1PID:g162919 REFERENCE A02928 !$#authors Bhat, S.P.; Spector, A. !$#journal DNA (1984) 3:287-295 !$#title Complete nucleotide sequence of a cDNA derived from calf !1lens gamma-crystallin mRNA: presence of Alu I-like DNA !1sequences. !$#cross-references MUID:85026663; PMID:6092016 !$#accession A02928 !'##molecule_type mRNA !'##residues 2-119,'S',121-175 ##label BHA !'##cross-references GB:K02112; GB:X01036; NID:g162916; PIDN:AAA30475.1; !1PID:g162917 !'##note initiator Met not shown REFERENCE A90263 !$#authors Croft, L.R. !$#journal Biochem. J. (1972) 128:961-970 !$#title The amino acid sequence of gamma-crystallin (fraction II) !1from calf lens. !$#cross-references MUID:73054483; PMID:4674126 !$#accession A90263 !'##molecule_type protein !'##residues 2-17,'Q',19-21,'NN',23,'LQP',28-39,'VHSL',45-46,'MLQ', !148-49,'D',51,53-54,56,'Q',60-61,'N',63-64,'Q',66-67,69-72, !1'D',74-108,'P',110,'D',112-122,'NY',127-133,'I',135-175 !1##label CRO !'##note portions of this sequence were assigned by composition rather !1than by direct sequencing REFERENCE A60890 !$#authors Chiou, S.H.; Azari, P.; Himmel, M.E. !$#journal J. Protein Chem. (1988) 7:67-80 !$#title Physicochemical characterization of gamma-crystallins from !1bovine lens-hydrodynamic and biochemical properties. !$#cross-references MUID:89351571; PMID:3255364 !$#accession A60890 !'##molecule_type protein !'##residues 2-26 ##label CHI REFERENCE A60815 !$#authors McDermott, M.J.; Gawinowicz-Kolks, M.A.; Chiesa, R.; !1Spector, A. !$#journal Arch. Biochem. Biophys. (1988) 262:609-619 !$#title The disulfide content of calf gamma-crystallin. !$#cross-references MUID:88208422; PMID:3364984 !$#accession A60815 !'##molecule_type protein !'##residues 2-26 ##label MCD REFERENCE A93247 !$#authors Blundell, T.; Lindley, P.; Miller, L.; Moss, D.; Slingsby, !1C.; Tickle, I.; Turnell, B.; Wistow, G. !$#journal Nature (1981) 289:771-777 !$#title The molecular structure and stability of the eye lens: x-ray !1analysis of gamma-crystallin II. !$#cross-references MUID:81123111; PMID:7464942 !$#contents annotation; X-ray crystallography, 2.6 angstroms REFERENCE S04265 !$#authors White, H.E.; Driessen, H.P.C.; Slingsby, C.; Moss, D.S.; !1Lindley, P.F. !$#journal J. Mol. Biol. (1989) 207:217-235 !$#title Packing interactions in the eye-lens. Structural analysis, !1internal symmetry and lattice interactions of bovine !1gamma-IVa--crystallin. !$#cross-references MUID:89293855; PMID:2738925 !$#contents annotation COMMENT The protein has a two-domain beta-structure, folded into !1four very similar Greek key motifs. COMMENT Evidence from reference A90263 suggests an absence of !1disulfide bonds. Evidence from reference A60815 suggests the !1presence of a single disulfide bond. CLASSIFICATION #superfamily beta-crystallin KEYWORDS duplication; eye lens FEATURE !$2-40 #domain crystallin repeat #label GK1\ !$41-83 #domain crystallin repeat #label GK2\ !$89-129 #domain crystallin repeat #label GK3\ !$130-169 #domain crystallin repeat #label GK4 SUMMARY #length 175 #molecular-weight 21097 #checksum 5414 SEQUENCE /// ENTRY CYRTG1 #type complete TITLE gamma-crystallin 1 - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 22-Jun-1999 ACCESSIONS A02930 REFERENCE A93934 !$#authors Moormann, R.J.M.; den Dunnen, J.T.; Bloemendal, H.; !1Schoenmakers, J.G.G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:6876-6880 !$#title Extensive intragenic sequence homology in two distinct rat !1lens gamma-crystallin cDNAs suggests duplications of a !1primordial gene. !$#cross-references MUID:83091061; PMID:6294661 !$#accession A02930 !'##molecule_type mRNA !'##residues 1-173 ##label MOO !'##cross-references GB:J00716; NID:g203634; PIDN:AAA40987.1; !1PID:g203635 CLASSIFICATION #superfamily beta-crystallin KEYWORDS duplication; eye lens FEATURE !$1-39 #domain crystallin repeat #label GK1\ !$40-82 #domain crystallin repeat #label GK2\ !$87-127 #domain crystallin repeat #label GK3\ !$128-167 #domain crystallin repeat #label GK4 SUMMARY #length 173 #molecular-weight 21132 #checksum 3707 SEQUENCE /// ENTRY CYMSG2 #type complete TITLE gamma-crystallin 2 - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 22-Jun-1999 ACCESSIONS A02931 REFERENCE A94021 !$#authors Breitman, M.L.; Lok, S.; Wistow, G.; Piatigorsky, J.; !1Treton, J.A.; Gold, R.J.M.; Tsui, L.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:7762-7766 !$#title gamma-crystallin family of the mous lens: structural and !1evolutionary relationships. !$#cross-references MUID:85088487; PMID:6096855 !$#accession A02931 !'##molecule_type mRNA !'##residues 1-174 ##label BRE !'##cross-references GB:K02584; NID:g192786; PIDN:AAA03228.1; !1PID:g309198 COMMENT There are at least seven different gamma crystallins !1identified in mouse lens. CLASSIFICATION #superfamily beta-crystallin KEYWORDS duplication; eye lens FEATURE !$2-40 #domain crystallin repeat #label GK1\ !$41-83 #domain crystallin repeat #label GK2\ !$88-128 #domain crystallin repeat #label GK3\ !$129-168 #domain crystallin repeat #label GK4 SUMMARY #length 174 #molecular-weight 21264 #checksum 4289 SEQUENCE /// ENTRY CYMSG1 #type complete TITLE gamma-crystallin 1 - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 22-Jun-1999 ACCESSIONS A02932 REFERENCE A94021 !$#authors Breitman, M.L.; Lok, S.; Wistow, G.; Piatigorsky, J.; !1Treton, J.A.; Gold, R.J.M.; Tsui, L.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:7762-7766 !$#title gamma-crystallin family of the mous lens: structural and !1evolutionary relationships. !$#cross-references MUID:85088487; PMID:6096855 !$#accession A02932 !'##molecule_type mRNA !'##residues 1-174 ##label BRE !'##cross-references GB:K02583; NID:g192778; PIDN:AAA37475.1; !1PID:g309197 COMMENT There are at least seven different gamma crystallins !1identified in mouse lens. CLASSIFICATION #superfamily beta-crystallin KEYWORDS duplication; eye lens FEATURE !$2-40 #domain crystallin repeat #label GK1\ !$41-83 #domain crystallin repeat #label GK2\ !$88-128 #domain crystallin repeat #label GK3\ !$129-168 #domain crystallin repeat #label GK4 SUMMARY #length 174 #molecular-weight 21008 #checksum 2936 SEQUENCE /// ENTRY CYMSG3 #type complete TITLE gamma-B-crystallin - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 17-Mar-1987 #sequence_revision 12-Jul-1996 #text_change 22-Jun-1999 ACCESSIONS I48359; A02933; S33523 REFERENCE I48359 !$#authors Graw, J.; Liebstein, A.; Pietrowski, D.; Schmitt-John, T.; !1Werner, T. !$#journal Gene (1993) 136:145-156 !$#title Genomic sequences of murine gamma B- and gamma !1C-crystallin-encoding genes: promoter analysis and complete !1evolutionary pattern of mouse, rat and human !1gamma-crystallins. !$#cross-references MUID:94123992; PMID:8293998 !$#accession I48359 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-175 ##label RES !'##cross-references EMBL:Z22573; NID:g311633; PIDN:CAA80296.1; !1PID:g311634 REFERENCE A94021 !$#authors Breitman, M.L.; Lok, S.; Wistow, G.; Piatigorsky, J.; !1Treton, J.A.; Gold, R.J.M.; Tsui, L.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:7762-7766 !$#title gamma-crystallin family of the mous lens: structural and !1evolutionary relationships. !$#cross-references MUID:85088487; PMID:6096855 !$#accession A02933 !'##molecule_type mRNA !'##residues 41-150,'M',152-175 ##label BRE COMMENT There are at least seven different gamma crystallins !1identified in mouse lens. GENETICS !$#introns 3/3; 84/3 CLASSIFICATION #superfamily beta-crystallin KEYWORDS duplication; eye lens FEATURE !$2-40 #domain crystallin repeat #label GK1\ !$41-83 #domain crystallin repeat #label GK2\ !$89-129 #domain crystallin repeat #label GK3\ !$130-169 #domain crystallin repeat #label GK4 SUMMARY #length 175 #molecular-weight 21139 #checksum 5032 SEQUENCE /// ENTRY CYHUG2 #type complete TITLE gamma-crystallin 2-1 - human ALTERNATE_NAMES gamma-C-crystallin ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 22-Jun-1999 ACCESSIONS B24520; I77412 REFERENCE A91536 !$#authors den Dunnen, J.T.; Moormann, R.J.M.; Cremers, F.P.M.; !1Schoenmakers, J.G.G. !$#journal Gene (1985) 38:197-204 !$#title Two human gamma-crystallin genes are linked and riddled with !1Alu-repeats. !$#cross-references MUID:86056977; PMID:4065573 !$#accession B24520 !'##molecule_type DNA !'##residues 1-174 ##label DEN !'##cross-references GB:M11973; NID:g181116; PIDN:AAA52114.1; !1PID:g181119 REFERENCE I57581 !$#authors Meakin, S.O.; Breitman, M.L.; Tsui, L.C. !$#journal Mol. Cell. Biol. (1985) 5:1408-1414 !$#title Structural and evolutionary relationships among five members !1of the human gamma-crystallin gene family. !$#cross-references MUID:85295974; PMID:4033658 !$#accession I77412 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-174 ##label RES !'##cross-references GB:K03004; NID:g181105; PIDN:AAA52111.1; !1PID:g181111 GENETICS !$#gene GDB:CRYGB; CRYG2 !'##cross-references GDB:119077; OMIM:123670 !$#map_position 2q33-2q35 !$#introns 3/3; 84/3 CLASSIFICATION #superfamily beta-crystallin KEYWORDS duplication; eye lens FEATURE !$2-174 #product gamma-crystallin 2-1 #status predicted !8#label MPT\ !$2-40 #domain crystallin repeat #label GK1\ !$41-83 #domain crystallin repeat #label GK2\ !$88-128 #domain crystallin repeat #label GK3\ !$129-168 #domain crystallin repeat #label GK4 SUMMARY #length 174 #molecular-weight 20878 #checksum 4132 SEQUENCE /// ENTRY CYRTG2 #type fragment TITLE gamma-crystallin 2 - rat (fragment) ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 22-Jun-1999 ACCESSIONS A02934 REFERENCE A93934 !$#authors Moormann, R.J.M.; den Dunnen, J.T.; Bloemendal, H.; !1Schoenmakers, J.G.G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:6876-6880 !$#title Extensive intragenic sequence homology in two distinct rat !1lens gamma-crystallin cDNAs suggests duplications of a !1primordial gene. !$#cross-references MUID:83091061; PMID:6294661 !$#accession A02934 !'##molecule_type mRNA !'##residues 1-170 ##label MOO !'##cross-references GB:J00717; NID:g203632; PIDN:AAA40986.1; !1PID:g203633 CLASSIFICATION #superfamily beta-crystallin KEYWORDS duplication; eye lens FEATURE !$1-36 #domain crystallin repeat (fragment) #label GK1\ !$37-79 #domain crystallin repeat #label GK2\ !$84-124 #domain crystallin repeat #label GK3\ !$125-164 #domain crystallin repeat #label GK4 SUMMARY #length 170 #checksum 7795 SEQUENCE /// ENTRY CYMSG4 #type complete TITLE gamma-crystallin 4 - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 22-Jun-1999 ACCESSIONS A02935; I49613 REFERENCE A94021 !$#authors Breitman, M.L.; Lok, S.; Wistow, G.; Piatigorsky, J.; !1Treton, J.A.; Gold, R.J.M.; Tsui, L.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:7762-7766 !$#title gamma-crystallin family of the mous lens: structural and !1evolutionary relationships. !$#cross-references MUID:85088487; PMID:6096855 !$#accession A02935 !'##molecule_type mRNA !'##residues 1-174 ##label BRE !'##note the authors translated the codon ATC for residue 36 as Val REFERENCE I48353 !$#authors Lok, S.; Tsui, L.C.; Shinohara, T.; Piatigorsky, J.; Gold, !1R.; Breitman, M. !$#journal Nucleic Acids Res. (1984) 12:4517-4529 !$#title Analysis of the mouse gamma-crystallin gene family: !1assignment of multiple cDNAs to discrete genomic sequences !1and characterization of a representative gene. !$#cross-references MUID:84247318; PMID:6330674 !$#accession I49613 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-174 ##label RES !'##cross-references GB:K02587; NID:g192771; PIDN:AAA37473.1; !1PID:g387135 COMMENT There are at least seven different gamma crystallins !1identified in mouse lens. GENETICS !$#introns 3/3; 84/3 CLASSIFICATION #superfamily beta-crystallin KEYWORDS duplication; eye lens FEATURE !$2-40 #domain crystallin repeat #label GK1\ !$41-83 #domain crystallin repeat #label GK2\ !$88-128 #domain crystallin repeat #label GK3\ !$129-168 #domain crystallin repeat #label GK4 SUMMARY #length 174 #molecular-weight 21149 #checksum 4994 SEQUENCE /// ENTRY CYCAG1 #type complete TITLE gamma-crystallin m1 - common carp ORGANISM #formal_name Cyprinus carpio #common_name common carp DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 22-Jun-1999 ACCESSIONS JS0061; S04214; S12964 REFERENCE JS0061 !$#authors Chang, T.; Jiang, Y.J.; Chiou, S.H.; Chang, W.C. !$#journal Biochim. Biophys. Acta (1988) 951:226-229 !$#title Carp gamma-crystallins with high methionine content: cloning !1and sequencing of the complementary DNA. !$#cross-references MUID:89051015; PMID:3191133 !$#accession JS0061 !'##molecule_type mRNA !'##residues 1-178 ##label CHA !'##cross-references EMBL:X12902; NID:g62601; PIDN:CAA31387.1; !1PID:g62602; EMBL:M33115 !'##note the authors translated the codon ACC for residue 101 as Asn CLASSIFICATION #superfamily beta-crystallin KEYWORDS duplication; eye lens FEATURE !$2-178 #product gamma-crystallin m1 #status predicted #label !8MAT\ !$2-40 #domain crystallin repeat #label GK1\ !$41-86 #domain crystallin repeat #label GK2\ !$92-132 #domain crystallin repeat #label GK3\ !$133-172 #domain crystallin repeat #label GK4 SUMMARY #length 178 #molecular-weight 21882 #checksum 5383 SEQUENCE /// ENTRY CYCAG2 #type complete TITLE gamma-crystallin m2 precursor - common carp ORGANISM #formal_name Cyprinus carpio #common_name common carp DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 22-Jun-1999 ACCESSIONS JS0062; S04215 REFERENCE JS0061 !$#authors Chang, T.; Jiang, Y.J.; Chiou, S.H.; Chang, W.C. !$#journal Biochim. Biophys. Acta (1988) 951:226-229 !$#title Carp gamma-crystallins with high methionine content: cloning !1and sequencing of the complementary DNA. !$#cross-references MUID:89051015; PMID:3191133 !$#accession JS0062 !'##molecule_type mRNA !'##residues 1-173 ##label CHA !'##cross-references EMBL:X12903; NID:g62603; PIDN:CAA31388.1; !1PID:g62604 !'##note the authors translated the codon CAC for residue 38 as Ser and !1AGC for residue 39 as His CLASSIFICATION #superfamily beta-crystallin KEYWORDS duplication; eye lens FEATURE !$1-39 #domain crystallin repeat #label GK1\ !$2-173 #product gamma crystallin m2 #status predicted #label !8MAT\ !$40-82 #domain crystallin repeat #label GK2\ !$88-128 #domain crystallin repeat #label GK3\ !$129-166 #domain crystallin repeat #label GK4 SUMMARY #length 173 #molecular-weight 21367 #checksum 1346 SEQUENCE /// ENTRY CYFGG #type fragment TITLE gamma-crystallin I - common frog (fragment) ORGANISM #formal_name Rana temporaria #common_name common frog DATE 13-Jun-1983 #sequence_revision 30-Sep-1988 #text_change 22-Jun-1999 ACCESSIONS A02936; I51166 REFERENCE A02936 !$#authors Tomarev, S.I.; Krayev, A.S.; Skryabin, K.G.; Bayev, A.A.; !1Gause Jr., G.G. !$#journal FEBS Lett. (1982) 146:315-318 !$#title The nucleotide sequence of a cloned cDNA corresponding to !1one of the gamma-crystallins from the eye lens of the frog !1Rana temporaria. !$#accession A02936 !'##molecule_type mRNA !'##residues 1-133 ##label TOM !'##note the authors translated the codon GCU for residue 125 as Ser REFERENCE I51166 !$#authors Tomarev, S.I.; Krayev, A.S.; Skryabin, K.G.; Gause, G.G.; !1Bayev, A.A. !$#journal Dokl. Biochem. (1982) 263:117-120 !$#title Presence of internal duplication in mRNA coding one of the !1gamma-crystallins of the crystalline lens of the eye of the !1frog Rana temporaria. !$#accession I51166 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-133 ##label TO2 !'##cross-references GB:J00928; NID:g213665; PIDN:AAA49520.1; !1PID:g213666 CLASSIFICATION #superfamily beta-crystallin KEYWORDS duplication; eye lens FEATURE !$1-41 #domain crystallin repeat (fragment) #label GK2\ !$47-87 #domain crystallin repeat #label GK3\ !$88-127 #domain crystallin repeat #label GK4 SUMMARY #length 133 #checksum 2215 SEQUENCE /// ENTRY CYFGG2 #type fragment TITLE gamma-crystallin II - common frog (fragment) ORGANISM #formal_name Rana temporaria #common_name common frog DATE 28-May-1986 #sequence_revision 30-Sep-1988 #text_change 11-Apr-1997 ACCESSIONS A02937 REFERENCE A02937 !$#authors Tomarev, S.I.; Zinovieva, R.D.; Chalovka, P.; Krayev, A.S.; !1Skryabin, K.G.; Gause Jr., G.G. !$#journal Gene (1984) 27:301-308 !$#title Multiple genes coding for the frog eye lens !1gamma-crystallins. !$#cross-references MUID:84237544; PMID:6610602 !$#accession A02937 !'##molecule_type mRNA !'##residues 1-168 ##label TOM !'##note the authors translated the codon CTG for residue 39 as Ile, GAC !1for residue 59 as Asn, and CTC for residue 110 as His COMMENT There are at least four genes coding for nonidentical gamma !1crystallins in this multigene family. CLASSIFICATION #superfamily beta-crystallin KEYWORDS duplication; eye lens FEATURE !$1-34 #domain crystallin repeat (fragment) #label GK1\ !$35-77 #domain crystallin repeat #label GK2\ !$83-123 #domain crystallin repeat #label GK3\ !$124-163 #domain crystallin repeat #label GK4 SUMMARY #length 168 #checksum 6869 SEQUENCE /// ENTRY KRHUE #type complete TITLE keratin 14, type I, cytoskeletal - human ALTERNATE_NAMES 50K type I keratin; cytokeratin 14; epidermal type I keratin ORGANISM #formal_name Homo sapiens #common_name man DATE 13-Jun-1983 #sequence_revision 08-Feb-1996 #text_change 10-Dec-1999 ACCESSIONS A26763; A90858; A90829; I39329; A02939 REFERENCE A26763 !$#authors Marchuk, D.; McCrohon, S.; Fuchs, E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:1609-1613 !$#title Complete sequence of a gene encoding a human type I keratin: !1sequences homologous to enhancer elements in the regulatory !1region of the gene. !$#cross-references MUID:85166180; PMID:2580298 !$#accession A26763 !'##molecule_type DNA !'##residues 1-472 ##label MAR1 !'##cross-references GB:J00124; NID:g186704; PIDN:AAB59562.1; !1PID:g386848 REFERENCE A90858 !$#authors Marchuk, D.; McCrohon, S.; Fuchs, E. !$#journal Cell (1984) 39:491-498 !$#title Remarkable conservation of structure among intermediate !1filament genes. !$#cross-references MUID:85074457; PMID:6210150 !$#accession A90858 !'##molecule_type DNA !'##residues 2-472 ##label MAR2 !'##cross-references GB:J00124; NID:g186704; PIDN:AAB59562.1; !1PID:g386848 !'##note initiator Met not shown REFERENCE A90829 !$#authors Hanukoglu, I.; Fuchs, E. !$#journal Cell (1982) 31:243-252 !$#title The cDNA sequence of a human epidermal keratin: divergence !1of sequence but conservation of structure among intermediate !1filament proteins. !$#cross-references MUID:83129327; PMID:6186381 !$#accession A90829 !'##molecule_type mRNA !'##residues 64-93,'T',95-472 ##label HAN !'##cross-references GB:J00124; NID:g186704 REFERENCE I39329 !$#authors Albers, K.; Fuchs, E. !$#journal J. Cell Biol. (1987) 105:791-806 !$#title The expression of mutant epidermal keratin cDNAs transfected !1in simple epithelial and squamous cell carcinoma lines. !$#cross-references MUID:87308384; PMID:2442174 !$#accession I39329 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 326-348,'V',350-467,'DGSSSSASCQFFGLM' ##label ALB !'##cross-references GB:M28646; NID:g177138; PIDN:AAA96689.1; !1PID:g177139 COMMENT The mammalian cytokeratins are a heterogeneous group of !1intermediate filament (IF) proteins. These proteins have a !1large conserved domain, composed of four helices separated !1by three short segments with beta conformation, and amino !1and carboxyl ends with diverse length and sequence. COMMENT The helical core plays a role in the polymerization of two !1polypeptide chains into a protofibril with coiled coil !1conformation. The diversity of the amino and carboxyl ends !1confers functional specificity to each chain and is !1responsible for the end-to-end linkage of about 10 !1protofibrils into a microfibril. COMMENT Each end domain consists of a set of subdomains distributed !1with bilateral symmetry around the rod domain. This !1structural organization is conserved among taxonomically !1distant species, suggesting functional significance. Because !1they are easily removed by proteolysis, these subdomains are !1thought to reside at the periphery of the IF molecule where !1they interact with cell constituents. COMMENT The rod domain is flanked by V1 and V2 subdomains that are !1highly variable in both length and sequence, often contain !1tandem repeats, and are rich in glycine and/or serine. The !1E1 and E2 subdomains are strongly basic and are also !1variable in sequence. COMMENT The cytoskeletal and microfibrillar keratins are classified !1into two types, type I (40-55 kilodaltons, generally acidic) !1and type II (56-70 kilodaltons, generally basic). The basic !1cytokeratin IF protein subunit appears to be a !1heterotetramer of two type I and two type II proteins. GENETICS !$#gene GDB:KRT14; EBS4; EBS3 !'##cross-references GDB:132145; OMIM:148066 !$#map_position 17q12-17q21 !$#introns 175/3; 203/2; 255/3; 309/3; 351/3; 425/2; 441/1 !$#note defects in this gene may result in epidermolysis bullosa !1simplex, Dowling-Meara syndrome type, and Koebner phenomenon COMPLEX heterotetramer of two type I and two type II proteins, !1usually keratin 5 (see PIR:A29904) CLASSIFICATION #superfamily cytoskeletal keratin KEYWORDS coiled coil; heterotetramer; intermediate filament FEATURE !$2-472 #product keratin, 50K type 1 cytoskeletal #status !8predicted #label MAT\ !$2-115 #domain head #label HED\ !$2-115 #region E1 and V1 subdomains\ !$116-426 #domain rod #label ROD\ !$116-150 #region coil 1A\ !$151-161 #region linker 1\ !$162-262 #region coil 1B\ !$263-278 #region linker 12\ !$279-297 #region coil 2A\ !$298-305 #region linker 2\ !$306-426 #region coil 2B\ !$364 #region stutter\ !$427-472 #domain tail #label END\ !$427-472 #region V2 and E2 subdomains SUMMARY #length 472 #molecular-weight 51662 #checksum 7666 SEQUENCE /// ENTRY KRHU9 #type complete TITLE keratin 19, type I, cytoskeletal - human ALTERNATE_NAMES cytokeratin 19 ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1991 #sequence_revision 23-Mar-1995 #text_change 10-Dec-1999 ACCESSIONS A31370; A61556; A60779; S00658; S60152 REFERENCE A31370 !$#authors Eckert, R.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:1114-1118 !$#title Sequence of the human 40-kDa keratin reveals an unusual !1structure with very high sequence identity to the !1corresponding bovine keratin. !$#cross-references MUID:88124986; PMID:2448790 !$#accession A31370 !'##molecule_type mRNA !'##residues 1-400 ##label ECK !'##cross-references GB:J03607; NID:g184658; PIDN:AAA36044.1; !1PID:g386803 REFERENCE A61556 !$#authors Bader, B.L.; Jahn, L.; Franke, W.W. !$#journal Eur. J. Cell Biol. (1988) 47:300-319 !$#title Low level expression of cytokeratins 8, 18 and 19 in !1vascular smooth muscle cells of human umbilical cord and in !1cultured cells derived therefrom, with an analysis of the !1chromosomal locus containing the cytokeratin 19 gene. !$#cross-references MUID:89210901; PMID:2468493 !$#accession A61556 !'##molecule_type mRNA !'##residues 1-400 ##label BAD REFERENCE A60779 !$#authors Stasiak, P.C.; Purkis, P.E.; Leigh, I.M.; Lane, E.B. !$#journal J. Invest. Dermatol. (1989) 92:707-716 !$#title Keratin 19: predicted amino acid sequence and broad tissue !1distribution suggest it evolved from keratinocyte keratins. !$#cross-references MUID:89235250; PMID:2469734 !$#accession A60779 !'##molecule_type mRNA !'##residues 1-349,'A',351-400 ##label STA !'##cross-references EMBL:Y00503; NID:g34038; PIDN:CAA68556.1; !1PID:g34039 REFERENCE S00658 !$#authors Stasiak, P.C.; Lane, E.B. !$#journal Nucleic Acids Res. (1987) 15:10058 !$#title Sequence of cDNA coding for human keratin 19. !$#cross-references MUID:88096504; PMID:2447559 !$#accession S00658 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-75,'H',78-341,'Y',343-349,'A',351-400 ##label ST2 !'##cross-references EMBL:Y00503 !'##note this sequence has been revised REFERENCE S60151 !$#authors Petersen, G.; Song, D.; Huegle-Doerr, B.; Oldenburg, I.; !1Bautz, E.K.F. !$#journal Mol. Gen. Genet. (1995) 249:425-431 !$#title Mapping of linear epitopes recognized by monoclonal !1antibodies with gene-fragment phage display libraries. !$#cross-references MUID:96133682; PMID:8552047 !$#accession S60152 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 331-349,'A',351-380 ##label PET COMMENT Keratin 19 is the smallest human keratin, as the !1non-alpha-helical tail present in all other keratins is !1replaced by a thirteen-amino acid alpha-helical extension. GENETICS !$#gene GDB:KRT19 !'##cross-references GDB:120131; OMIM:148020 !$#map_position 17q21-17q23 CLASSIFICATION #superfamily cytoskeletal keratin KEYWORDS coiled coil; intermediate filament FEATURE !$1-73 #domain head #label HEA\ !$74-386 #domain helical rod #status predicted #label ROD\ !$387-399 #domain tail #label TAI SUMMARY #length 400 #molecular-weight 44092 #checksum 5480 SEQUENCE /// ENTRY KRHU5 #type complete TITLE keratin 15, type I, cytoskeletal - human ALTERNATE_NAMES acidic cytokeratin; cytokeratin 15 ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 10-Dec-1999 ACCESSIONS S01069; B61556; A33211; B30186 REFERENCE S01068 !$#authors Leube, R.E.; Bader, B.L.; Bosch, F.X.; Zimbelmann, R.; !1Achtstaetter, T.; Franke, W.W. !$#journal J. Cell Biol. (1988) 106:1249-1261 !$#title Molecular characterization and expression of the !1stratification-related cytokeratins 4 and 15. !$#cross-references MUID:88198369; PMID:2452170 !$#accession S01069 !'##molecule_type mRNA !'##residues 1-456 ##label LEU !'##cross-references EMBL:X07696; NID:g34070; PIDN:CAA30535.1; !1PID:g34071 REFERENCE A61556 !$#authors Bader, B.L.; Jahn, L.; Franke, W.W. !$#journal Eur. J. Cell Biol. (1988) 47:300-319 !$#title Low level expression of cytokeratins 8, 18 and 19 in !1vascular smooth muscle cells of human umbilical cord and in !1cultured cells derived therefrom, with an analysis of the !1chromosomal locus containing the cytokeratin 19 gene. !$#cross-references MUID:89210901; PMID:2468493 !$#accession B61556 !'##molecule_type DNA !'##residues 1-166,195-456 ##label BAD !'##note authors translated the codon GTC for residue 259 as Gly !'##note translation of this genomic sequence omits, between regions !1shown as exon 1 and exon 2, a sequence of amino acids !1encoded in the mRNA reported in reference S01068; no part of !1intron 1 from this paper appears to correspond to the !1missing coding region GENETICS !$#gene GDB:KRT15 !'##cross-references GDB:120124; OMIM:148030 !$#map_position 17q21-17q22 CLASSIFICATION #superfamily cytoskeletal keratin KEYWORDS coiled coil; intermediate filament FEATURE !$1-97 #domain head #label HEA\ !$98-413 #domain helical rod #status predicted #label ROD\ !$414-456 #domain tail #label TAI SUMMARY #length 456 #molecular-weight 49167 #checksum 938 SEQUENCE /// ENTRY KRHU3 #type complete TITLE keratin 13, type I, cytoskeletal, long splice form - human ALTERNATE_NAMES cytokeratin 13 ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 10-Dec-1999 ACCESSIONS S06088; A33216; B37343; A33403 REFERENCE S06088 !$#authors Mischke, D.; Wachter, E.; Hochstrasser, K.; Wild, A.G.; !1Schulz, P. !$#journal Nucleic Acids Res. (1989) 17:7984 !$#title The N-, but not the C-terminal domains of human keratins 13 !1and 15 are closely related. !$#cross-references MUID:90016882; PMID:2477803 !$#accession S06088 !'##molecule_type mRNA !'##residues 1-458 ##label MIS1 !'##cross-references EMBL:X14640; NID:g34032; PIDN:CAA32786.1; !1PID:g34033 !$#accession A33216 !'##molecule_type protein !'##residues 291-299 ##label MIS2 REFERENCE A37343 !$#authors Kuruc, N.; Leube, R.E.; Moll, I.; Bader, B.L.; Franke, W.W. !$#journal Differentiation (1989) 42:111-123 !$#title Synthesis of cytokeratin 13, a component characteristic of !1internal stratified epithelia, is not induced in human !1epidermal tumors. !$#cross-references MUID:90228645; PMID:2483837 !$#accession B37343 !'##molecule_type mRNA !'##residues 1-57,'G',59-458 ##label KUR !'##cross-references GB:X52426 REFERENCE A33403 !$#authors Schulz, P.; Wachter, E.; Hochstrasser, K.; Wild, A.G.; !1Mischke, D. !$#journal Biochem. Biophys. Res. Commun. (1989) 162:1522-1527 !$#title Sequence of a human keratin 13 specific cDNA encompassing !1coil 1B through the 3' end(+). !$#cross-references MUID:89350978; PMID:2475110 !$#accession A33403 !'##molecule_type mRNA !'##residues 158-458 ##label SCH GENETICS !$#gene GDB:KRT13 !'##cross-references GDB:120740; OMIM:148065 !$#map_position 17q21-17q22 CLASSIFICATION #superfamily cytoskeletal keratin KEYWORDS alternative splicing; coiled coil; intermediate filament FEATURE !$1-96 #domain head #label HEA\ !$97-412 #domain helical rod #status predicted #label ROD\ !$413-458 #domain tail #label TAI SUMMARY #length 458 #molecular-weight 49644 #checksum 8053 SEQUENCE /// ENTRY KRMSE1 #type complete TITLE keratin, 59K type I cytoskeletal - mouse ALTERNATE_NAMES 59-kDa type I keratin ORGANISM #formal_name Mus musculus #common_name house mouse DATE 15-Nov-1984 #sequence_revision 04-Dec-1986 #text_change 10-Dec-1999 ACCESSIONS A02940 REFERENCE A02940 !$#authors Krieg, T.M.; Schafer, M.P.; Cheng, C.K.; Filpula, D.; !1Flaherty, P.; Steinert, P.M.; Roop, D.R. !$#journal J. Biol. Chem. (1985) 260:5867-5870 !$#title Organization of a type I keratin gene. Evidence for !1evolution of intermediate filaments from a common ancestral !1gene. !$#cross-references MUID:85207552; PMID:2581944 !$#accession A02940 !'##molecule_type DNA !'##residues 1-569 ##label KRI !'##cross-references GB:L00193; GB:K00391; NID:g198625; PIDN:AAA39391.1; !1PID:g387397 !'##note initiator Met not shown !'##note the authors translated the codon GAG for residue 41 as Gly COMMENT Fourier analysis has identified a 7-residue repeating !1pattern (heptad) between residues 138-454, in which the !1first and fourth residues are apolar and the remainder are !1polar. This region forms a stable alpha-helical coiled coil !1but is interrupted by three short regions with beta !1conformation. COMMENT Most of the introns of the gene encoding this protein are !1located within the regions predicted to form alpha helices; !1although they do not demarcate structural domains, they do !1interrupt the sequence at or near the beginning of heptad !1repeats. Several of these sites are conserved in genes !1encoding type II and III intermediate filaments. COMMENT The amino and carboxyl ends are rich in glycine, serine, and !1aromatic residues arranged in short, tandem repeats !1characteristic of cytoskeletal keratins. GENETICS !$#introns 206/3; 234/2; 286/3; 340/3; 382/3; 455/2; 568/2 CLASSIFICATION #superfamily cytoskeletal keratin KEYWORDS coiled coil; intermediate filament FEATURE !$1-143 #domain head #label HED\ !$1-143 #region E1 and V1 subdomains\ !$144-457 #domain rod #label ROD\ !$144-178 #region coil 1A\ !$179-192 #region linker 1\ !$193-293 #region coil 1B\ !$294-309 #region linker 12\ !$310-328 #region coil 2A\ !$329-336 #region linker 2\ !$337-457 #region coil 2B\ !$395 #region stutter\ !$458-569 #domain tail #label END\ !$458-569 #region V2 and E2 subdomains SUMMARY #length 569 #molecular-weight 57711 #checksum 435 SEQUENCE /// ENTRY KRHU0 #type complete TITLE keratin 10, type I, cytoskeletal - human ALTERNATE_NAMES cytokeratin 10 ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 10-Dec-1999 ACCESSIONS S02158; C38182; B38182; PC1102; S14666; S14669 REFERENCE S02158 !$#authors Rieger, M.; Franke, W.W. !$#journal J. Mol. Biol. (1988) 204:841-856 !$#title Identification of an orthologous mammalian cytokeratin gene. !1High degree of intron sequence conservation during evolution !1of human cytokeratin 10. !$#cross-references MUID:89125611; PMID:2464696 !$#accession S02158 !'##molecule_type DNA !'##residues 1-593 ##label RIE !'##cross-references EMBL:X14487; NID:g28316; PIDN:CAA32649.1; !1PID:g28317 !'##experimental_source clone lambda-KH10-5 REFERENCE A38182 !$#authors Korge, B.P.; Gan, S.Q.; McBride, O.W.; Mischke, D.; !1Steinert, P.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:910-914 !$#title Extensive size polymorphism of the human keratin 10 chain !1resides in the C-terminal V2 subdomain due to variable !1numbers and sizes of glycine loops. !$#cross-references MUID:92141228; PMID:1371013 !$#accession C38182 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 452-593 ##label KOR1 !'##cross-references PIDN:AAB21315.1; PID:g244509 !'##note sequence extracted from NCBI backbone (NCBIP:79427) !$#accession B38182 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 452-463,'P',465-507,'Y',523-593 ##label KOR2 !'##cross-references PIDN:AAB21314.1; PID:g244508 !'##note sequence extracted from NCBI backbone (NCBIP:79431) REFERENCE PC1102 !$#authors Tkachenko, A.V.; Buchman, V.L.; Bliskovsky, V.V.; Shvets, !1Y.P.; Kisselev, L.L. !$#journal Gene (1992) 116:245-251 !$#title Exons I and VII of the gene (Ker10) encoding human keratin !110 undergo structural rearrangements within repeats. !$#cross-references MUID:92339897; PMID:1378806 !$#accession PC1102 !'##molecule_type mRNA !'##residues 'G',198-407,'Q',409-450,'G',452-486,491-524,534-593 ##label !1TKA !'##cross-references GB:M77663; NID:g186628; PIDN:AAA59199.1; !1PID:g186629 !'##experimental_source embryonic skin, clone HK51 REFERENCE S14666 !$#authors Darmon, M.Y.; Semat, A.; Darmon, M.C.; Vasseur, M. !$#journal Mol. Biol. Rep. (1987) 12:277-283 !$#title Sequence of a cDNA encoding human keratin No 10 selected !1according to structural homologies of keratins and their !1tissue-specific expression. !$#cross-references MUID:88122104; PMID:2448602 !$#accession S14666 !'##molecule_type mRNA !'##residues 130-278,'YV',281-311,'I',313-339,'V',341-373,'R',375-407, !1'Q',409-459,'RS',462-476,'T',478-481,'T',483-502,'T', !1504-507,'T',509-512,'LRGELHGGHAH',535,'T',537-542,'N', !1544-550,'LR',553,'RH',556-579,'P',581-593 ##label DAR1 !'##cross-references EMBL:M19156; NID:g186769 !'##note the sequence from Fig. 3 is inconsistent with the nucleotide !1sequence from Fig. 2 in having additional residues !1Ile-Lys-Ile-Arg-Leu after 442-Leu REFERENCE S14667 !$#authors Darmon, M.Y.; Semat, A.; Darmon, M.C.; Vasseur, M. !$#submission submitted to the EMBL Data Library, May 1988 !$#accession S14669 !'##molecule_type mRNA !'##residues 130-278,'YV',281-311,'I',313-339,'V',341-373,'R',375-407, !1'Q',409-459,'RS',462-476,'T',478-481,'T',483-502,'T', !1504-507,'T',509-512,'LRGELHGGHAH',535,'T',537-542,'N', !1544-550,'LR',553,'RH',556-593 ##label DAR2 !'##cross-references EMBL:M19156; NID:g186769; PIDN:AAA59468.1; !1PID:g307086 !'##note the translated sequence in GenBank entry HUMKRT10A, release !1111.0, differs from the published sequence in beginning !1incorrectly at the internal 21-Met AUG codon GENETICS !$#gene GDB:KRT10; KPP !'##cross-references GDB:118828; OMIM:148080 !$#map_position 17q12-17q21 !$#introns 209/3; 237/2; 289/3; 343/3; 385/3; 458/2; 592/3 !$#note this gene encodes variants with considerable length !1polymorphism !$#note mutations in this gene can cause epidermolytic !1hyperkeratosis and keratosis palmaris et plantaris COMPLEX heterotetramer of two type I and two type II proteins, !1usually keratin 1 (see PIR:KRHU2) CLASSIFICATION #superfamily cytoskeletal keratin KEYWORDS coiled coil; heterotetramer; intermediate filament; !1polymorphism FEATURE !$1-145 #domain head #label HEA\ !$146-456 #domain helical rod #status predicted #label ROD\ !$457-593 #domain tail #label TAI SUMMARY #length 593 #molecular-weight 59528 #checksum 1460 SEQUENCE /// ENTRY KRBOVI #type complete TITLE keratin, 54K type I cytoskeletal - bovine ALTERNATE_NAMES 54-kDa type I keratin; cytokeratin VIb ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 10-Dec-1999 ACCESSIONS A02941; S07262 REFERENCE A02941 !$#authors Rieger, M.; Jorcano, J.L.; Franke, W.W. !$#journal EMBO J. (1985) 4:2261-2267 !$#title Complete sequence of a bovine type I cytokeratin gene: !1conserved and variable intron positions in genes of !1polypeptides of the same cytokeratin subfamily. !$#cross-references MUID:86081734; PMID:2416562 !$#accession A02941 !'##molecule_type DNA !'##residues 1-526 ##label RIE !'##cross-references GB:X02870; NID:g478; PIDN:CAA26626.1; PID:g479 REFERENCE S07262 !$#authors Jorcano, J.L.; Rieger, M.; Franz, J.K.; Schiller, D.L.; !1Moll, R.; Franke, W.W. !$#journal J. Mol. Biol. (1984) 179:257-281 !$#title Identification of two types of keratin polypeptides within !1the acidic cytokeratin subfamily I. !$#cross-references MUID:85058191; PMID:6209405 !$#accession S07262 !'##molecule_type mRNA !'##residues 281-466,'PAAATAAEVQRWRPRRXFRRQYG',490-491,494,'PVAVARRRK', !1504-526 ##label JOR !'##cross-references EMBL:X01460 !'##note this sequence has been revised in reference A02941 GENETICS !$#gene cytokeratin VIb !$#introns 190/3; 218/2; 270/3; 324/3; 366/3; 439/2; 525/2 CLASSIFICATION #superfamily cytoskeletal keratin KEYWORDS coiled coil; intermediate filament FEATURE !$1-127 #domain head #label HED\ !$1-127 #region E1 and V1 subdomains\ !$128-441 #domain rod #label ROD\ !$128-162 #region coil 1A\ !$163-176 #region linker 1\ !$177-277 #region coil 1B\ !$278-293 #region linker 12\ !$294-312 #region coil 2A\ !$313-320 #region linker 2\ !$321-441 #region coil 2B\ !$379 #region stutter\ !$442-526 #domain tail #label END\ !$442-526 #region V2 and E2 subdomains SUMMARY #length 526 #molecular-weight 54848 #checksum 3237 SEQUENCE /// ENTRY KRXL #type complete TITLE keratin 3, type I, cytoskeletal (clone pUF1001) - African clawed frog ALTERNATE_NAMES cytokeratin, 51K ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 28-Aug-1985 #sequence_revision 30-Sep-1991 #text_change 10-Dec-1999 ACCESSIONS S01327; A02943 REFERENCE S01327 !$#authors Hoffmann, W.; Sterrer, S.; Koenigstorfer, A. !$#journal FEBS Lett. (1988) 237:178-182 !$#title Amino acid sequence microheterogeneities of a type I !1cytokeratin of M(r) 51000 from Xenopus laevis epidermis. !$#cross-references MUID:89005622; PMID:2458965 !$#accession S01327 !'##molecule_type mRNA !'##residues 1-486 ##label HOF !'##cross-references EMBL:Y00968; NID:g64490; PIDN:CAA68783.1; !1PID:g64491 REFERENCE A02943 !$#authors Hoffmann, W.; Franz, J.K. !$#journal EMBO J. (1984) 3:1301-1306 !$#title Amino acid sequence of the carboxy-terminal part of an !1acidic type I cytokeratin of molecular weight 51 000 from !1Xenopus laevis epidermis as predicted from the cDNA !1sequence. !$#cross-references MUID:84261417; PMID:6204859 !$#accession A02943 !'##molecule_type mRNA !'##residues 339-351,'T',353-486 ##label HOF2 !'##cross-references GB:X00629; NID:g64868; PIDN:CAA25263.1; PID:g833626 !'##note this sequence has been revised in paper S01327 CLASSIFICATION #superfamily cytoskeletal keratin KEYWORDS coiled coil; intermediate filament FEATURE !$1-120 #domain head #label HEA\ !$121-438 #domain helical rod #status predicted #label ROD\ !$439-486 #domain tail #label TAI SUMMARY #length 486 #molecular-weight 51889 #checksum 3211 SEQUENCE /// ENTRY KRSHL1 #type complete TITLE keratin, 48K type I microfibrillar, component 8c-1 - sheep ALTERNATE_NAMES 48-kDa type I keratin; low-sulfur keratin ORGANISM #formal_name Ovis orientalis aries, Ovis ammon aries #common_name domestic sheep DATE 15-Nov-1984 #sequence_revision 04-Dec-1986 #text_change 10-Dec-1999 ACCESSIONS A02942 REFERENCE A02942 !$#authors Dowling, L.M.; Crewther, W.G.; Inglis, A.S. !$#journal Biochem. J. (1986) 236:695-703 !$#title The primary structure of component 8c-1, a subunit protein !1of intermediate filaments in wool keratin. Relationships !1with proteins from other intermediate filaments. !$#cross-references MUID:87075644; PMID:2431679 !$#accession A02942 !'##molecule_type protein !'##residues 1-412 ##label DOW !'##experimental_source Merino wool !'##note overlaps were not obtained for residues 115-116, 119-120, !1125-126, 142-143, and 171-172 COMMENT This low-sulfur protein fraction was prepared from an !1extract of S-carboxymethylated Merino wool. COMMENT The low-sulfur proteins, derived from the microfibrillar !1fraction of wool extracts, are composed of two families, !1each consisting of four homologous subunits: the type I !1components (8c-1, 8c-2, 8a, and 8b) and the type II !1components (5, 7a, 7b, and 7c). CLASSIFICATION #superfamily cytoskeletal keratin KEYWORDS acetylated amino end; coiled coil; intermediate filament FEATURE !$1-55 #region E1 and V1 subdomains\ !$1-55 #domain head #label HED\ !$56-366 #domain rod #label ROD\ !$56-90 #region coil 1A\ !$91-101 #region linker 1\ !$102-202 #region coil 1B\ !$203-218 #region linker 12\ !$219-237 #region coil 2A\ !$238-245 #region linker 2\ !$246-366 #region coil 2B\ !$304 #region stutter\ !$367-412 #region V2 and E2 subdomains\ !$367-412 #domain tail #label END\ !$1 #modified_site acetylated amino end (Ser) #status !8experimental SUMMARY #length 412 #molecular-weight 46674 #checksum 863 SEQUENCE /// ENTRY KRHUEA #type complete TITLE keratin 6a, type II - human ALTERNATE_NAMES 56-kDa type II keratin; keratin cytoskeletal ORGANISM #formal_name Homo sapiens #common_name man DATE 15-Nov-1984 #sequence_revision 15-Oct-1999 #text_change 21-Jul-2000 ACCESSIONS A57398; A02944 REFERENCE A57398 !$#authors Takahashi, K.; Paladini, R.D.; Coulombe, P.A. !$#journal J. Biol. Chem. (1995) 270:18581-18592 !$#title Cloning and characterization of multiple human genes and !1cDNAs encoding highly related type II keratin 6 isoforms. !$#cross-references MUID:95355491; PMID:7543104 !$#accession A57398 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-564 ##label TAK !'##cross-references GB:L42575; NID:g908769; GB:L42576; NID:g908770; !1GB:L42577; NID:g908771; GB:L42578; NID:g908772; GB:L42579; !1NID:g908773; GB:L42580; NID:g908774; GB:L42581; NID:g908775; !1GB:L42582; NID:g908776; GB:L42583; NID:g908777; !1PIDN:AAC41767.1; PID:g908779 REFERENCE A02944 !$#authors Hanukoglu, I.; Fuchs, E. !$#journal Cell (1983) 33:915-924 !$#title The cDNA sequence of a type II cytoskeletal keratin reveals !1constant and variable structural domains among keratins. !$#cross-references MUID:83259278; PMID:6191871 !$#accession A02944 !'##molecule_type mRNA !'##residues 208-394,'S',396-564 ##label HAN !'##cross-references GB:J00269; NID:g34068; PIDN:CAA24760.1; PID:g34069 COMMENT The cytoskeletal and microfibrillar keratins are classified !1into two types, type I (40-55 kilodaltons, generally acidic) !1and type II (56-70 kilodaltons, generally basic). The basic !1cytokeratin IF protein subunit appears to be a !1heterotetramer of two type I and two type II proteins. GENETICS !$#gene GDB:KRT6A !'##cross-references GDB:128111; OMIM:148041 !$#map_position 12q12-12q21 !$#introns 180/3; 252/2; 272/3; 304/3; 359/3; 401/3; 475/2; 487/1 CLASSIFICATION #superfamily cytoskeletal keratin KEYWORDS coiled coil; intermediate filament FEATURE !$2-163 #domain head #label HED\ !$2-126 #region E1 and V1 subdomains\ !$127-163 #region H1 subdomain\ !$162-476 #domain rod #label ROD\ !$199-210 #region linker 1\ !$211-311 #region coil 1B\ !$312-328 #region linker 12\ !$329-347 #region coil 2A\ !$348-355 #region linker 2\ !$356-476 #region coil 2B\ !$414 #region stutter\ !$477-564 #domain tail #label END\ !$477-496 #region H2 subdomain\ !$497-564 #region V2 and E2 subdomains SUMMARY #length 564 #molecular-weight 60045 #checksum 2901 SEQUENCE /// ENTRY KRHUEB #type complete TITLE keratin 6b, type II - human ALTERNATE_NAMES 56K type II keratin; keratin, cytoskeletal ORGANISM #formal_name Homo sapiens #common_name man DATE 04-Dec-1986 #sequence_revision 15-Oct-1999 #text_change 10-Dec-1999 ACCESSIONS I61767; A02945 REFERENCE A57398 !$#authors Takahashi, K.; Paladini, R.D.; Coulombe, P.A. !$#journal J. Biol. Chem. (1995) 270:18581-18592 !$#title Cloning and characterization of multiple human genes and !1cDNAs encoding highly related type II keratin 6 isoforms. !$#cross-references MUID:95355491; PMID:7543104 !$#accession I61767 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-564 ##label RES !'##cross-references GB:L42584; NID:g908780; GB:L42585; NID:g908781; !1GB:L42586; NID:g908782; GB:L42587; NID:g908783; GB:L42588; !1NID:g908784; GB:L42589; NID:g908785; GB:L42590; NID:g908786; !1GB:L42591; NID:g908787; GB:L42592; NID:g908788; !1PIDN:AAC41768.1; PID:g908790 REFERENCE A02945 !$#authors Tyner, A.L.; Eichman, M.J.; Fuchs, E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:4683-4687 !$#title The sequence of a type II keratin gene expressed in human !1skin: conservation of structure among all intermediate !1filament genes. !$#cross-references MUID:85270392; PMID:2410904 !$#accession A02945 !'##molecule_type DNA !'##residues 2-88,'AG',91-115,'PA',118,'LC',122-158,'IG',161-254,'V', !1256-564 ##label TYN !'##cross-references GB:M11229; GB:L00205; NID:g186714; PIDN:AAA59466.1; !1PID:g386849 !'##note initiator Met not shown COMMENT There are two types of cytoskeletal and microfibrillar !1keratin, I (acidic) and II (neutral to basic) (40-55 and !156-70 kilodaltons, respectively). The cytokeratin IF !1proteins appear to be obligate heteropolymers, composed of !1complexes formed by the aggregation of at least one type I !1and one type II protein. GENETICS !$#gene GDB:KRT6B !'##cross-references GDB:128113; OMIM:148042 !$#map_position 12pter-12qter !$#introns 180/3; 252/2; 272/3; 304/3; 359/3; 401/3; 475/2; 487/1 CLASSIFICATION #superfamily cytoskeletal keratin KEYWORDS coiled coil; intermediate filament FEATURE !$2-163 #domain head #label HED\ !$2-127 #region E1 and V1 subdomains\ !$128-163 #region H1 subdomain\ !$164-476 #domain rod #label ROD\ !$164-198 #region coil 1A\ !$199-210 #region linker 1\ !$211-311 #region coil 1B\ !$312-328 #region linker 12\ !$329-347 #region coil 2A\ !$348-355 #region linker 2\ !$356-476 #region coil 2B\ !$414 #region stutter\ !$477-564 #domain tail #label END\ !$477-496 #region H2 subdomain\ !$497-564 #region V2 and E2 subdomains SUMMARY #length 564 #molecular-weight 59998 #checksum 2197 SEQUENCE /// ENTRY KRBO2B #type fragment TITLE keratin, 68K type II cytoskeletal, component Ib - bovine (fragment) ALTERNATE_NAMES 68-kDa type II keratin ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 10-Dec-1999 ACCESSIONS A02948 REFERENCE A02946 !$#authors Jorcano, J.L.; Franz, J.K.; Franke, W.W. !$#journal Differentiation (1984) 28:155-163 !$#title Amino acid sequence diversity between bovine epidermal !1cytokeratin polypeptides of the basic (type II) subfamily as !1determined from cDNA clones. !$#cross-references MUID:85128114; PMID:6084625 !$#accession A02948 !'##molecule_type mRNA !'##residues 1-166 ##label JOR !'##cross-references GB:K03534; NID:g163250; PIDN:AAA30601.1; !1PID:g163251 !'##experimental_source muzzle epidermis CLASSIFICATION #superfamily cytoskeletal keratin KEYWORDS coiled coil; intermediate filament FEATURE !$1-41 #domain rod (fragment) #label ROD\ !$1-41 #region coil 2B (fragment)\ !$42-166 #domain tail #label END SUMMARY #length 166 #checksum 8257 SEQUENCE /// ENTRY KRBO2A #type fragment TITLE keratin, 68K type II cytoskeletal, component Ia - bovine (fragment) ALTERNATE_NAMES 68-kDa type II keratin ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 10-Dec-1999 ACCESSIONS A02949 REFERENCE A02946 !$#authors Jorcano, J.L.; Franz, J.K.; Franke, W.W. !$#journal Differentiation (1984) 28:155-163 !$#title Amino acid sequence diversity between bovine epidermal !1cytokeratin polypeptides of the basic (type II) subfamily as !1determined from cDNA clones. !$#cross-references MUID:85128114; PMID:6084625 !$#accession A02949 !'##molecule_type mRNA !'##residues 1-182 ##label JOR !'##cross-references GB:K03533; NID:g163246; PIDN:AAA30599.1; !1PID:g163247 !'##experimental_source muzzle epidermis CLASSIFICATION #superfamily cytoskeletal keratin KEYWORDS coiled coil; intermediate filament FEATURE !$1-66 #domain rod (fragment) #label ROD\ !$1-66 #region coil 2B (fragment)\ !$4 #region stutter\ !$67-182 #domain tail #label END\ !$67-86 #region H2 subdomain\ !$87-162 #region V2 subdomain\ !$163-182 #region E2 subdomain SUMMARY #length 182 #checksum 3030 SEQUENCE /// ENTRY KRHU2 #type complete TITLE keratin 1, type II, cytoskeletal - human ALTERNATE_NAMES 67K type II epidermal keratin; cytokeratin 1 ORGANISM #formal_name Homo sapiens #common_name man DATE 04-Dec-1986 #sequence_revision 22-Oct-1999 #text_change 10-Dec-1999 ACCESSIONS A22940; A02950; A43342 REFERENCE A22940 !$#authors Johnson, L.D.; Idler, W.W.; Zhou, X.M.; Roop, D.R.; !1Steinert, P.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:1896-1900 !$#cross-references MUID:85166239; PMID:2580302 !$#accession A22940 !'##molecule_type DNA !'##residues 1-643 ##label JOH !'##cross-references GB:M98776; GB:M11215; GB:M11845; GB:M11846; !1NID:g1843461 !'##note translation of initiator Met is not shown REFERENCE A92535 !$#authors Steinert, P.M.; Parry, D.A.D.; Idler, W.W.; Johnson, L.D.; !1Steven, A.C.; Roop, D.R. !$#journal J. Biol. Chem. (1985) 260:7142-7149 !$#title Amino acid sequences of mouse and human epidermal type II !1keratins of M-r 67,000 provide a systematic basis for the !1structural and functional diversity of the end domains of !1keratin intermediate filament subunits. !$#cross-references MUID:85207740; PMID:2581964 !$#accession A02950 !'##molecule_type mRNA !'##residues 151-183,'K',185-199,'M',201-204,'K',206-236,'S',238-239, !1'R',241-356,'Y',358-402,'M',404-445,'M',447-457,'A',459-461, !1'C',463-464,'H',466-510,'M',512-535,'C',537-555,'S',557-631, !1'R',633-636,'S',638-643 ##label STE !'##cross-references GB:M10938; NID:g186787; PIDN:AAA36153.1; !1PID:g386854 !'##experimental_source tissue neonatal foreskin !'##note the authors translated the codon CUG for residue 476 as Met REFERENCE A43342 !$#authors Chipev, C.C.; Korge, B.P.; Markova, N.; Bale, S.J.; !1DiGiovanna, J.J.; Compton, J.G.; Steinert, P.M. !$#journal Cell (1992) 70:821-828 !$#title A leucine----proline mutation in the H1 subdomain of keratin !11 causes epidermolytic hyperkeratosis. !$#cross-references MUID:92386601; PMID:1381288 !$#accession A43342 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 144-146,'P',148-159,'P',161-183,'K',185-186 ##label CHI !'##cross-references GB:M98776; GB:M11215; GB:M11845; GB:M11846; !1NID:g1843461 !'##note sequence extracted from NCBI backbone (NCBIP:112784) COMMENT The cytoskeletal and microfibrillar keratins are classified !1into two types, type I (40-55 kilodaltons, generally acidic) !1and type II (56-70 kilodaltons, generally basic). The basic !1cytokeratin IF protein subunit appears to be a !1heterotetramer of two type I and two type II proteins. COMMENT Keratin 1 is expressed in terminally differentiating !1epidermis. GENETICS !$#gene GDB:KRT1 !'##cross-references GDB:128198; OMIM:139350 !$#map_position 12q11-12q13 !$#note defects in this gene may result in epidermolytic !1hyperkeratosis COMPLEX heterotetramer of two type I, usually keratin 10 (see !1PIR:KRHU0), and two type II proteins CLASSIFICATION #superfamily cytoskeletal keratin KEYWORDS coiled coil; heterotetramer; intermediate filament FEATURE !$4-179 #domain head #label HED\ !$4-143 #region E1 and V1 subdomains\ !$14-179 #region H1 subdomain\ !$180-492 #domain rod #label ROD\ !$180-214 #region coil 1A\ !$215-226 #region linker 1\ !$227-327 #region coil 1B\ !$328-344 #region linker 12\ !$345-363 #region coil 2A\ !$364-371 #region linker 2\ !$372-492 #region coil 2B\ !$430 #region stutter\ !$493-643 #domain tail #label END\ !$493-512 #region H2 subdomain\ !$513-643 #region V2 and E2 subdomains SUMMARY #length 643 #molecular-weight 65494 #checksum 3501 SEQUENCE /// ENTRY KRMS2 #type fragment TITLE keratin, type II cytoskeletal - mouse (fragment) ALTERNATE_NAMES 67-kDa type II keratin ORGANISM #formal_name Mus musculus #common_name house mouse DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 20-Mar-1998 ACCESSIONS A02951 REFERENCE A92535 !$#authors Steinert, P.M.; Parry, D.A.D.; Idler, W.W.; Johnson, L.D.; !1Steven, A.C.; Roop, D.R. !$#journal J. Biol. Chem. (1985) 260:7142-7149 !$#title Amino acid sequences of mouse and human epidermal type II !1keratins of M-r 67,000 provide a systematic basis for the !1structural and functional diversity of the end domains of !1keratin intermediate filament subunits. !$#cross-references MUID:85207740; PMID:2581964 !$#accession A02951 !'##molecule_type mRNA !'##residues 1-581 ##label STE !'##cross-references GB:M10937; NID:g198622; PID:g387396 CLASSIFICATION #superfamily cytoskeletal keratin KEYWORDS coiled coil; intermediate filament FEATURE !$1-106 #domain head (fragment) #label HED\ !$1-70 #region V1 subdomain (fragment)\ !$71-106 #region H1 subdomain\ !$107-419 #domain rod #label ROD\ !$107-141 #region coil 1A\ !$142-153 #region linker 1\ !$154-254 #region coil 1B\ !$255-271 #region linker 12\ !$272-290 #region coil 2A\ !$291-298 #region linker 2\ !$299-419 #region coil 2B\ !$357 #region stutter\ !$420-581 #domain tail #label END\ !$420-439 #region H2 subdomain\ !$440-581 #region V2 and E2 subdomains SUMMARY #length 581 #checksum 3732 SEQUENCE /// ENTRY KRXL2B #type fragment TITLE keratin, 64K type II cytoskeletal (clone pUF164) - African clawed frog (fragment) ALTERNATE_NAMES 64-kDa type II keratin ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 10-Dec-1999 ACCESSIONS A02952 REFERENCE A92914 !$#authors Hoffmann, W.; Franz, J.K.; Franke, W.W. !$#journal J. Mol. Biol. (1985) 184:713-724 !$#title Amino acid sequence microheterogeneities of basic (type II) !1cytokeratins of Xenopus laevis epidermis and evolutionary !1conservativity of helical and non-helical domains. !$#cross-references MUID:86011576; PMID:2413219 !$#accession A02952 !'##molecule_type mRNA !'##residues 1-419 ##label HOF !'##cross-references GB:X02895; GB:M13954; NID:g64866; PIDN:CAA26654.1; !1PID:g64867 !'##experimental_source clone pUF164 CLASSIFICATION #superfamily cytoskeletal keratin KEYWORDS coiled coil; intermediate filament FEATURE !$1-275 #domain rod (fragment) #label ROD\ !$1-9 #region linker 1\ !$10-110 #region coil 1B\ !$111-127 #region linker 12\ !$128-146 #region coil 2A\ !$147-154 #region linker 2\ !$155-275 #region coil 2B\ !$213 #region stutter\ !$276-419 #domain tail #label END\ !$276-399 #region H2 and V2 subdomains\ !$400-419 #region E2 subdomain SUMMARY #length 419 #checksum 4685 SEQUENCE /// ENTRY KRXL2A #type fragment TITLE keratin, 64K type II cytoskeletal (clone pUF23) - African clawed frog (fragment) ALTERNATE_NAMES 64-kDa type II keratin ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 10-Dec-1999 ACCESSIONS A02953 REFERENCE A92914 !$#authors Hoffmann, W.; Franz, J.K.; Franke, W.W. !$#journal J. Mol. Biol. (1985) 184:713-724 !$#title Amino acid sequence microheterogeneities of basic (type II) !1cytokeratins of Xenopus laevis epidermis and evolutionary !1conservativity of helical and non-helical domains. !$#cross-references MUID:86011576; PMID:2413219 !$#accession A02953 !'##molecule_type mRNA !'##residues 1-425 ##label HOF !'##cross-references GB:X02894; GB:M13956; NID:g64865; PIDN:CAA26653.1; !1PID:g899427 !'##experimental_source clone pUF23 COMMENT The cytokeratin IF proteins appear to be obligate !1heteropolymers, composed of complexes formed by the !1aggregation of at least one type I and one type II protein. !1Homology between these two types of proteins is low and !1restricted to specific isolated regions within the rod !1domain that are well conserved among all IF proteins. COMMENT Three subdomains, each characterized by a distinctive amino !1acid composition, can be distinguished within the nonhelical !1tail domain. Although the tail is hypervariable in both !1sequence and length among the intermediate filament !1proteins, the arrangement of its subdomains presents a !1pattern of alternating hydroxyamino- and glycine-enriched !1regions that, being conserved among taxonomically distant !1species, suggests functional significance. COMMENT There is only one group of closely related type II amphibian !1cytokeratins. This is in contrast to the organizational !1complexity of type II mammalian proteins and may reflect the !1simpler state of differentiation of the amphibian epidermis, !1which lacks a true stratum corneum. CLASSIFICATION #superfamily cytoskeletal keratin KEYWORDS coiled coil; intermediate filament FEATURE !$1-296 #domain rod (fragment) #label ROD\ !$1-16 #region coil 1A (fragment)\ !$17-30 #region linker 1\ !$31-131 #region coil 1B\ !$132-148 #region linker 12\ !$149-167 #region coil 2A\ !$168-175 #region linker 2\ !$176-296 #region coil 2B\ !$234 #region stutter\ !$297-425 #domain tail #label END\ !$297-405 #region H2 and V2 subdomains\ !$406-425 #region E2 subdomain SUMMARY #length 425 #checksum 584 SEQUENCE /// ENTRY KRSHL2 #type complete TITLE keratin type II, microfibrillar - sheep ALTERNATE_NAMES intermediate filament protein KII-9; low-sulfur keratin ORGANISM #formal_name Ovis orientalis aries, Ovis ammon aries #common_name domestic sheep DATE 15-Nov-1984 #sequence_revision 15-May-1998 #text_change 10-Dec-1999 ACCESSIONS I46409; A02954; S22025 REFERENCE I46409 !$#authors Powell, B.; Crocker, L.; Rogers, G. !$#journal Development (1992) 114:417-433 !$#title Hair follicle differentiation: expression, structure and !1evolutionary conservation of the hair type II keratin !1intermediate filament gene family. !$#cross-references MUID:92274852; PMID:1375545 !$#accession I46409 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-508 ##label PO2 !'##cross-references EMBL:X62509; NID:g1307; PIDN:CAA44368.1; PID:g1308 REFERENCE A02954 !$#authors Crewther, W.G.; Inglis, A.S.; McKern, N.M. !$#journal Biochem. J. (1978) 173:365-371 !$#title Amino acid sequences of alpha-helical segments from !1S-carboxymethylkerateine-A. Complete sequence of a type-II !1segment. !$#cross-references MUID:79020757; PMID:581264 !$#accession A02954 !'##molecule_type protein !'##residues 142-190,192-251 ##label CRE !'##note 51-Lys and 52-Lys were also found GENETICS !$#gene KII-9 !$#introns 123/3; 193/3; 214/3; 246/3; 301/3; 343/3; 417/2; 428/1 CLASSIFICATION #superfamily cytoskeletal keratin KEYWORDS coiled coil; cytoskeleton; hair; intermediate filament FEATURE !$126-418 #domain rod #status predicted #label ROD\ !$126-253 #region coiled coil 1 #status predicted\ !$271-418 #region coiled coil 2 #status predicted SUMMARY #length 508 #molecular-weight 55245 #checksum 2105 SEQUENCE /// ENTRY DMHU #type complete TITLE desmin - human ALTERNATE_NAMES type III intermediate filament ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 10-Dec-1999 ACCESSIONS JE0063 REFERENCE JE0063 !$#authors Li, Z.; Lilienbaum, A.; Butler-Browne, G.; Paulin, D. !$#journal Gene (1989) 78:243-254 !$#title Human desmin-coding gene: complete nucleotide sequence, !1characterization and regulation of expression during !1myogenesis and development. !$#cross-references MUID:89378751; PMID:2673923 !$#accession JE0063 !'##molecule_type DNA !'##residues 1-469 ##label LIZ !'##cross-references GB:M63391; GB:M26935; GB:M58168; GB:M59379; !1GB:M65071; GB:X53154; NID:g181539; PIDN:AAA99221.1; !1PID:g181540 !'##note the introns of this gene contain 1.2K of repetitive sequences !1belonging to the human AluI family COMMENT Desmin intermediate filaments are found in the cytoplasm of !1cultured myogenic cells but are redistributed during !1differentiation. In adult striated muscle they form a !1fibrous network connecting myofibrils to each other and to !1the plasma membrane from the periphery of the Z-line !1structures. COMMENT The molecule contains three structurally distinct domains. !1The surface-exposed, very basic amino-terminal domain is !1called the headpiece. The rod-like middle domain is mainly !1alpha-helical. The tailpiece comprises the carboxyl-terminal !1residues. GENETICS !$#gene GDB:DES !'##cross-references GDB:119841; OMIM:125660 !$#map_position 2q35-2q35 !$#introns 192/2; 212/3; 244/3; 298/3; 340/3; 414/2; 429/1; 456/3 CLASSIFICATION #superfamily cytoskeletal keratin KEYWORDS acetylated amino end; coiled coil; intermediate filament; !1muscle; phosphoprotein FEATURE !$2-469 #product desmin #status predicted #label MDM\ !$2-108 #domain head #label HED\ !$109-415 #domain rod #label ROD\ !$416-469 #domain tail #label END\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status predicted\ !$7,32 #binding_site phosphate (Ser) (covalent) (by cdc2 !8kinase) #status predicted\ !$13,48 #binding_site phosphate (Ser) (covalent) (by protein !8kinase C) #status predicted\ !$45,60 #binding_site phosphate (Ser) (covalent) (by !8cAMP-dependent kinase) #status predicted SUMMARY #length 469 #molecular-weight 53519 #checksum 4929 SEQUENCE /// ENTRY DMPG #type fragment TITLE desmin - pig (fragment) ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 18-Dec-1981 #sequence_revision 18-Dec-1981 #text_change 31-Dec-1993 ACCESSIONS A02955 REFERENCE A02955 !$#authors Geisler, N.; Weber, K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:4120-4123 !$#title Comparison of the proteins of two immunologically distinct !1intermediate-sized filaments by amino acid sequence !1analysis: desmin and vimentin. !$#cross-references MUID:82037793; PMID:6945574 !$#accession A02955 !'##molecule_type protein !'##residues 1-138 ##label GEI !'##note some peptides and residues were positioned by homology with the !1chicken sequence COMMENT Desmin occurs in intermediate-sized filaments in certain !1muscle types. CLASSIFICATION #superfamily cytoskeletal keratin KEYWORDS coiled coil SUMMARY #length 138 #checksum 4772 SEQUENCE /// ENTRY DMHY #type fragment TITLE desmin - golden hamster (fragment) ORGANISM #formal_name Mesocricetus auratus #common_name golden hamster DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 22-Jun-1999 ACCESSIONS A02956 REFERENCE A02956 !$#authors Quax, W.; van den Heuvel, R.; Egberts, W.V.; Quax-Jeuken, !1Y.; Bloemendal, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:5970-5974 !$#title Intermediate filament cDNAs from BHK-21 cells: demonstration !1of distinct genes for desmin and vimentin in all vertebrate !1classes. !$#cross-references MUID:85014890; PMID:6091127 !$#accession A02956 !'##molecule_type mRNA !'##residues 1-298 ##label QUA !'##cross-references GB:K02407; NID:g191356; PIDN:AAA37071.1; !1PID:g387070 !'##experimental_source baby hamster kidney cells, BHK-21 COMMENT There is a single gene for desmin in the hamster genome. CLASSIFICATION #superfamily cytoskeletal keratin KEYWORDS coiled coil; intermediate filament FEATURE !$245-298 #domain tail #label TLE SUMMARY #length 298 #checksum 8666 SEQUENCE /// ENTRY DMCH #type complete TITLE desmin - chicken ALTERNATE_NAMES type III intermediate filament ORGANISM #formal_name Gallus gallus #common_name chicken DATE 18-Dec-1981 #sequence_revision 12-Apr-1996 #text_change 10-Dec-1999 ACCESSIONS A90969; A94014; JC1459; S02448; A32858; S23189; A02957 REFERENCE A90969 !$#authors Geisler, N.; Weber, K. !$#journal EMBO J. (1982) 1:1649-1656 !$#title The amino acid sequence of chicken muscle desmin provides a !1common structural model for intermediate filament proteins. !$#cross-references MUID:84207925; PMID:6202512 !$#accession A90969 !'##molecule_type protein !'##residues 1-463 ##label GEI REFERENCE A94014 !$#authors Capetanaki, Y.G.; Ngai, J.; Lazarides, E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:6909-6913 !$#title Characterization and regulation in the expression of a gene !1coding for the intermediate filament protein desmin. !$#cross-references MUID:85063701; PMID:6594672 !$#accession A94014 !'##molecule_type mRNA !'##residues 366-463 ##label CAP !'##cross-references GB:K02445; NID:g211727; PIDN:AAA48751.1; !1PID:g211728 REFERENCE JC1459 !$#authors Kusubata, M.; Matsuoka, Y.; Tsujimura, K.; Ito, H.; Ando, !1S.; Kamijo, M.; Yasuda, H.; Ohba, Y.; Okumura, E.; !1Kishimoto, T.; Inagaki, M. !$#journal Biochem. Biophys. Res. Commun. (1993) 190:927-934 !$#title cdc2 Kinase phosphorylation of desmin at three serine/ !1threonine residues in the amino-terminal head domain. !$#cross-references MUID:93176201; PMID:8439342 !$#accession JC1459 !'##molecule_type protein !'##residues 5-9;16-27;63-67 ##label KUS REFERENCE S02448 !$#authors Geisler, N.; Weber, K. !$#journal EMBO J. (1988) 7:15-20 !$#title Phosphorylation of desmin in vitro inhibits formation of !1intermediate filaments; identification of three kinase A !1sites in the aminoterminal head domain. !$#cross-references MUID:88196075; PMID:3359992 !$#accession S02448 !'##molecule_type protein !'##residues 1-69 ##label GE2 REFERENCE A32858 !$#authors Kitamura, S.; Ando, S.; Shibata, M.; Tanabe, K.; Sato, C.; !1Inagaki, M. !$#journal J. Biol. Chem. (1989) 264:5674-5678 !$#title Protein kinase C phosphorylation of desmin at four serine !1residues within the non-alpha-helical head domain. !$#cross-references MUID:89174618; PMID:2494168 !$#accession A32858 !'##molecule_type protein !'##residues 10-14;28-42;49-59 ##label KIT REFERENCE S23189 !$#authors Geisler, N.; Schuenemann, J.; Weber, K. !$#journal Eur. J. Biochem. (1992) 206:841-852 !$#title Chemical cross-linking indicates a staggered and !1antiparallel protofilament of desmin intermediate filaments !1and characterizes one higher-level complex between !1protofilaments. !$#cross-references MUID:92299013; PMID:1606966 !$#accession S23189 !'##status preliminary !'##molecule_type protein !'##residues 110-118;255-266;274-282;393-401 ##label GE3 COMMENT This protein was isolated from chicken gizzard. COMMENT There appears to be a single desmin gene in the haploid !1chicken genome that is transcribed into a single mRNA. Its !1expression is transcriptionally regulated and !1tissue-specific, occurring predominantly in skeletal, !1cardiac, and most types of smooth muscle cells during !1myogenic terminal differentiation. COMMENT Desmin intermediate filaments are found in the cytoplasm of !1cultured myogenic cells but are redistributed during !1differentiation. In adult striated muscle they form a !1fibrous network connecting myofibrils to each other and to !1the plasma membrane from the periphery of the Z-line !1structures. COMMENT The molecule contains three structurally distinct domains. !1The surface-exposed, very basic amino-terminal domain is !1called the headpiece. The rod-like middle domain is mainly !1alpha-helical. The tailpiece comprises the carboxyl-terminal !1residues. CLASSIFICATION #superfamily cytoskeletal keratin KEYWORDS blocked amino end; coiled coil; intermediate filament; !1muscle; phosphoprotein FEATURE !$1-99 #domain head #label HED\ !$100-407 #domain rod #label ROD\ !$100-132 #region coil 1A\ !$133-142 #region linker 1\ !$143-243 #region coil 1B\ !$244-259 #region linker 12\ !$260-278 #region coil 2A\ !$279-286 #region linker 2\ !$287-407 #region coil 2B\ !$345 #region stutter\ !$408-463 #domain tail #label END\ !$1 #modified_site blocked amino end (Ser) (probably !8acetylated) #status experimental\ !$6,22 #binding_site phosphate (Ser) (covalent) (by cdc2 !8kinase) #status experimental\ !$12,29,38,56 #binding_site phosphate (Ser) (covalent) (by protein !8kinase C) #status experimental\ !$29,35,50 #binding_site phosphate (Ser) (covalent) (by !8cAMP-dependent kinase) #status predicted\ !$64 #binding_site phosphate (Thr) (covalent) (by cdc2 !8kinase) #status experimental SUMMARY #length 463 #molecular-weight 53279 #checksum 8757 SEQUENCE /// ENTRY VEHY #type complete TITLE vimentin - golden hamster ORGANISM #formal_name Mesocricetus auratus #common_name golden hamster DATE 19-Feb-1984 #sequence_revision 27-Nov-1985 #text_change 22-Jun-1999 ACCESSIONS A90842; A93953; A39731; A02959 REFERENCE A90842 !$#authors Quax, W.; Egberts, W.V.; Hendriks, W.; Quax-Jeuken, Y.; !1Bloemendal, H. !$#journal Cell (1983) 35:215-223 !$#title The structure of the vimentin gene. !$#cross-references MUID:84026520; PMID:6194898 !$#accession A90842 !'##molecule_type DNA !'##residues 1-464 ##label QU1 !'##cross-references GB:K00927; NID:g191465; PIDN:AAA37104.1; !1PID:g387077 REFERENCE A93953 !$#authors Quax-Jeuken, Y.E.F.M.; Quax, W.J.; Bloemendal, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:3548-3552 !$#title Primary and secondary structure of hamster vimentin !1predicted from the nucleotide sequence. !$#cross-references MUID:83221633; PMID:6304716 !$#accession A93953 !'##molecule_type mRNA !'##residues 'PRHLEPAG',25-40,'A',42-113,'D',115-180,'I',182-464 ##label !1QU2 !'##experimental_source lens REFERENCE A39731 !$#authors Chou, Y.H.; Ngai, K.L.; Goldman, R. !$#journal J. Biol. Chem. (1991) 266:7325-7328 !$#title The regulation of intermediate filament reorganization in !1mitosis. p34(cdc2) phosphorylates vimentin at a unique !1N-terminal site. !$#cross-references MUID:91210232; PMID:2019567 !$#accession A39731 !'##molecule_type protein !'##residues 36-41,'A',42-47,'T',48;49,50-62;63-67 ##label CHO !'##note the phosphorylated residue described as 40-Ser may be 41-Ser; !1nucleic acid sequencing from other studies suggests residue !140 is Gly COMMENT The initiator Met is not shown. COMMENT Vimentin occurs in intermediate-sized filaments in various !1nonepithelial cells, especially mesenchymal cells. GENETICS !$#introns 187/2; 207/3; 239/3; 293/3; 335/3; 409/2; 424/1; 452/3 CLASSIFICATION #superfamily cytoskeletal keratin KEYWORDS acetylated amino end; coiled coil; intermediate filament; !1phosphoprotein FEATURE !$411-464 #domain tail #label TLE\ !$1 #modified_site acetylated amino end (Ser) #status !8predicted\ !$41 #binding_site phosphate (Ser) (covalent) (by cdc2 !8kinase) #status predicted\ !$52,64 #binding_site phosphate (Ser) (covalent) (by cdc2 !8kinase) #status experimental SUMMARY #length 464 #molecular-weight 53598 #checksum 7883 SEQUENCE /// ENTRY VEMSGF #type complete TITLE glial fibrillary acidic protein, astrocyte - mouse ALTERNATE_NAMES GFAP ORGANISM #formal_name Mus musculus #common_name house mouse DATE 13-Aug-1986 #sequence_revision 30-Jun-1993 #text_change 10-Dec-1999 ACCESSIONS B60052; A24343; A02960; S42464; I49688 REFERENCE A60052 !$#authors Brenner, M.; Lampel, K.; Nakatani, Y.; Mill, J.; Banner, C.; !1Mearow, K.; Dohadwala, M.; Lipsky, R.; Freese, E. !$#journal Brain Res. Mol. Brain Res. (1990) 7:277-286 !$#title Characterization of human cDNA and genomic clones for glial !1fibrillary acidic protein. !$#cross-references MUID:90294716; PMID:2163003 !$#accession B60052 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-57 ##label BRE !'##note the authors present evidence that the sequence in reference !1A24343 contains a frameshift error near the amino end REFERENCE A24343 !$#authors Balcarek, J.M.; Cowan, N.J. !$#journal Nucleic Acids Res. (1985) 13:5527-5543 !$#title Structure of the mouse glial fibrillary acidic protein gene: !1implications for the evolution of the intermediate filament !1multigene family. !$#cross-references MUID:85297756; PMID:2994002 !$#accession A24343 !'##molecule_type DNA !'##residues 'MPPRRWSGAS',23-346,'H',348-430 ##label BAL !'##cross-references GB:X02801; NID:g51065; PIDN:CAA26571.1; PID:g51066 !'##note the authors translated the codon CAT for residue 174 as Asp, !1ACC for residue 290 as Arg, CAC for residue 347 as Gln, and !1CTC for residue 350 as Ala REFERENCE A02960 !$#authors Lewis, S.A.; Balcarek, J.M.; Krek, V.; Shelanski, M.; Cowan, !1N.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:2743-2746 !$#title Sequence of a cDNA clone encoding mouse glial fibrillary !1acidic protein: structural conservation of intermediate !1filaments. !$#cross-references MUID:84194082; PMID:6585825 !$#accession A02960 !'##molecule_type mRNA !'##residues 28-430 ##label LEW !'##cross-references GB:K01347; NID:g193465; PIDN:AAA37678.1; !1PID:g387163 !'##experimental_source clone G1 !'##note the authors translated the codon CAT for residue 147 as Asp REFERENCE S42464 !$#authors Ralton, J.E.; Lu, X.; Hutcheson, A.M.; Quinlan, R.A. !$#submission submitted to the EMBL Data Library, March 1994 !$#description Identification of two non-alpha-helical domain motifs !1important in the assembly of glial fibrillary acidic !1protein. !$#accession S42464 !'##status preliminary !'##molecule_type DNA !'##residues 1-26 ##label RAL !'##cross-references EMBL:X78141; NID:g460826; PIDN:CAA55020.1; !1PID:g460827 REFERENCE I49688 !$#authors Cowan, N.J.; Lewis, S.A.; Balcarek, J.M.; Krek, V.; !1Shelanski, M.L. !$#journal Ann. N. Y. Acad. Sci. (1985) 455:575-582 !$#title Structural implications of a cDNA clone encoding mouse glial !1fibrillary acidic protein. !$#cross-references MUID:86101618; PMID:3866511 !$#accession I49688 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 28-430 ##label RES !'##cross-references GB:M25937; NID:g193467; PIDN:AAA37679.1; !1PID:g387164 COMMENT GFAP is a cell-specific marker that, during the development !1of the central nervous system, distinguishes astrocytes from !1other glial cells. CLASSIFICATION #superfamily cytoskeletal keratin KEYWORDS coiled coil; intermediate filament FEATURE !$1-19 #domain head (fragment) #status predicted #label HED\ !$20-348 #domain rod #status predicted #label ROD\ !$349-403 #domain tail #status predicted #label TLE SUMMARY #length 430 #molecular-weight 49908 #checksum 5621 SEQUENCE /// ENTRY VEHULA #type complete TITLE lamin A - human ALTERNATE_NAMES 70kDa lamin ORGANISM #formal_name Homo sapiens #common_name man DATE 28-May-1986 #sequence_revision 04-Dec-1986 #text_change 10-Dec-1999 ACCESSIONS A02961; B24249; C24249 REFERENCE A02962 !$#authors McKeon, F.D.; Kirschner, M.W.; Caput, D. !$#journal Nature (1986) 319:463-468 !$#title Homologies in both primary and secondary structure between !1nuclear envelope and intermediate filament proteins. !$#cross-references MUID:86118697; PMID:3453101 !$#accession A02961 !'##molecule_type mRNA !'##residues 1-582,'LAHRAVRDLRAACRQGICQRLRSPGGRTHL', !1'LWLFCLQCHGHSQLPQCGGQWGWQLRGQSG', !1'HPLLPPGQLQPPNPEPPELQHHVIWDLPGR', !1'GGGGGFLRPPHLMPTPCPARHGRGLEAKEK' ##label MCK !'##cross-references GB:X03444; NID:g34227; PIDN:CAA27173.1; PID:g34228 !'##note this sequence has been corrected in reference A94121; an !1omitted nucleotide caused a reading frame error begining at !1position 583 REFERENCE A94121 !$#authors Fisher, D.Z.; Chaudhary, N.; Blobel, G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:6450-6454 !$#title cDNA sequencing of nuclear lamins A and C reveals primary !1and secondary structural homology to intermediate filament !1proteins. !$#cross-references MUID:86313596; PMID:3462705 !$#note parts of sequences from rat lamins, but not human, were !1determined by protein sequencing !$#accession B24249 !'##molecule_type mRNA !'##residues 537-664 ##label FIS !'##note sequence fragment shown in publication !$#accession C24249 !'##molecule_type mRNA !'##residues 150-664 ##label FI2 !'##cross-references GB:M13452; NID:g186838; PIDN:AAA36160.1; !1PID:g386856 !'##note submitted sequence extracted from GenBank COMMENT Lamins A and C (see PIR:VEHULC) are products of alternative !1splicing of the same gene. COMMENT The lamins (A, B, and C) contains several alpha-helical !1domains capable of forming coiled coils. COMMENT The association of lamins, dependent upon ionic !1interactions, is interrupted by hyperphosphorylation during !1the interphase-metaphase period of the cell cycle. The !1nuclear envelope disintegrates with lamin dissociation; it !1does not reform until telophase, when the lamins are !1dephosphorylated to interphase levels and then reassociate. GENETICS !$#gene GDB:LMNA; LMN1 !'##cross-references GDB:132146; OMIM:150330 !$#map_position 1q21.2-1q21.3 FUNCTION !$#description structural component of the nuclear lamina, a fibrous !1meshwork on the nucleoplasmic surface of the nuclear !1membrane CLASSIFICATION #superfamily cytoskeletal keratin KEYWORDS alternative splicing; coiled coil; lipoprotein; membrane !1protein; methylated carboxyl end; nuclear membrane; !1phosphoprotein; prenylated cysteine; structural protein FEATURE !$2-661 #product lamin A #status predicted #label MAT\ !$2-33 #domain head #label HED\ !$34-388 #domain rod #label ROD\ !$34-70 #region coil 1A\ !$81-218 #region coil 1B\ !$243-388 #region coil 2\ !$325 #region stutter\ !$389-661 #domain tail #label END\ !$417-420 #region nuclear location signal\ !$661 #binding_site farnesyl (Cys) (covalent) #status !8predicted\ !$661 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted SUMMARY #length 664 #molecular-weight 74139 #checksum 9955 SEQUENCE /// ENTRY VEHULC #type complete TITLE lamin C - human ORGANISM #formal_name Homo sapiens #common_name man DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 10-Dec-1999 ACCESSIONS A02962; A24249 REFERENCE A02962 !$#authors McKeon, F.D.; Kirschner, M.W.; Caput, D. !$#journal Nature (1986) 319:463-468 !$#title Homologies in both primary and secondary structure between !1nuclear envelope and intermediate filament proteins. !$#cross-references MUID:86118697; PMID:3453101 !$#accession A02962 !'##molecule_type mRNA !'##residues 1-572 ##label MCK !'##cross-references GB:X03445; NID:g34235; PIDN:CAA27174.1; PID:g34236 REFERENCE A94121 !$#authors Fisher, D.Z.; Chaudhary, N.; Blobel, G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:6450-6454 !$#title cDNA sequencing of nuclear lamins A and C reveals primary !1and secondary structural homology to intermediate filament !1proteins. !$#cross-references MUID:86313596; PMID:3462705 !$#accession A24249 !'##molecule_type mRNA !'##residues 1-572 ##label FIS !'##cross-references GB:M13451; NID:g186925; PIDN:AAA36164.1; !1PID:g307108 COMMENT Lamins A (see PIR:VEHULA) and C are products of alternative !1splicing of the same gene. COMMENT The lamins (A, B, and C) contains several alpha-helical !1domains capable of forming coiled coils. COMMENT The association of lamins, dependent upon ionic !1interactions, is interrupted by hyperphosphorylation during !1the interphase-metaphase period of the cell cycle. The !1nuclear envelope disintegrates with lamin dissociation; it !1does not reform until telophase, when the lamins are !1dephosphorylated to interphase levels and then reassociate. GENETICS !$#gene GDB:LMNA; LMN1 !'##cross-references GDB:132146; OMIM:150330 !$#map_position 1q21.2-1q21.3 FUNCTION !$#description structural component of the nuclear lamina, a fibrous !1meshwork on the nucleoplasmic surface of the nuclear !1membrane CLASSIFICATION #superfamily cytoskeletal keratin KEYWORDS alternative splicing; coiled coil; membrane protein; nuclear !1membrane; phosphoprotein; structural protein FEATURE !$2-572 #product lamin C #status predicted #label MAT\ !$2-33 #domain head #label HED\ !$34-388 #domain rod #label ROD\ !$34-70 #region coil 1A\ !$81-218 #region coil 1B\ !$243-388 #region coil 2\ !$266 #region heptad change of phase\ !$330 #region heptad change of phase\ !$389-572 #domain tail #label END\ !$417-420 #region nuclear location signal SUMMARY #length 572 #molecular-weight 65134 #checksum 6769 SEQUENCE /// ENTRY VEHULB #type complete TITLE lamin B1 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1991 #sequence_revision 15-Nov-1996 #text_change 10-Dec-1999 ACCESSIONS A34707; A57124 REFERENCE A34707 !$#authors Pollard, K.M.; Chan, E.K.L.; Grant, B.J.; Sullivan, K.F.; !1Tan, E.M.; Glass, C.A. !$#journal Mol. Cell. Biol. (1990) 10:2164-2175 !$#title In vitro posttranslational modification of lamin B cloned !1from a human T-cell line. !$#cross-references MUID:90220602; PMID:2325650 !$#accession A34707 !'##molecule_type mRNA !'##residues 1-586 ##label POL !'##cross-references GB:M34458; NID:g186877; PIDN:AAA36162.1; !1PID:g307106 REFERENCE A57124 !$#authors Lin, F.; Worman, H.J. !$#journal Genomics (1995) 27:230-236 !$#title Structural organization of the human gene (LMNB1) encoding !1nuclear lamin B1. !$#cross-references MUID:96044426; PMID:7557986 !$#accession A57124 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-586 ##label RES !'##cross-references GB:L37747; NID:g576838; PIDN:AAC37575.1; !1PID:g576840 COMMENT The lamins (A, B, and C) contains several alpha-helical !1domains capable of forming coiled coils. COMMENT The association of lamins, dependent upon ionic !1interactions, is interrupted by hyperphosphorylation during !1the interphase-metaphase period of the cell cycle. The !1nuclear envelope disintegrates with lamin dissociation; it !1does not reform until telophase, when the lamins are !1dephosphorylated to interphase levels and then reassociate. GENETICS !$#gene GDB:LMNB1 !'##cross-references GDB:512284; OMIM:150340 !$#map_position 5q23.3-5q31.1 !$#introns 120/2; 172/3; 214/3; 271/3; 313/3; 387/2; 462/3; 497/3; 537/ !13; 573/3 FUNCTION !$#description structural component of the nuclear lamina, a fibrous !1meshwork on the nucleoplasmic surface of the nuclear !1membrane, in somatic cells CLASSIFICATION #superfamily cytoskeletal keratin KEYWORDS coiled coil; lipoprotein; membrane protein; methylated !1carboxyl end; nuclear membrane; prenylated cysteine; !1structural protein FEATURE !$2-583 #product lamin B1 #status predicted #label MAT\ !$2-34 #domain head #label HED\ !$35-390 #domain rod #label ROD\ !$35-71 #region coil 1A\ !$82-240 #region coil 1B\ !$244-390 #region coil 2\ !$391-583 #domain tail #label END\ !$415-418 #region nuclear location signal\ !$583 #binding_site farnesyl (Cys) (covalent) #status !8predicted\ !$583 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted SUMMARY #length 586 #molecular-weight 66408 #checksum 2399 SEQUENCE /// ENTRY QFPGL #type complete TITLE neurofilament triplet L protein - pig ALTERNATE_NAMES 68K neurofilament protein ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 15-Nov-1984 #sequence_revision 28-May-1986 #text_change 10-Oct-1997 ACCESSIONS A91337; A90973; A34569; A02963 REFERENCE A91337 !$#authors Geisler, N.; Plessmann, U.; Weber, K. !$#journal FEBS Lett. (1985) 182:475-478 !$#title The complete amino acid sequence of the major mammalian !1neurofilament protein (NF-L). !$#cross-references MUID:85154583; PMID:3920075 !$#accession A91337 !'##molecule_type protein !'##residues 1-547 ##label GE1 REFERENCE A90973 !$#authors Geisler, N.; Kaufmann, E.; Fischer, S.; Plessmann, U.; !1Weber, K. !$#journal EMBO J. (1983) 2:1295-1302 !$#title Neurofilament architecture combines structural principles of !1intermediate filaments with carboxy-terminal extensions !1increasing in size between triplet proteins. !$#accession A90973 !'##molecule_type protein !'##residues 1-82;278-548 ##label GE2 !'##note residue 322 is either lysine or arginine REFERENCE A34569 !$#authors Gonda, Y.; Nishizawa, K.; Ando, S.; Kitamura, S.; Minoura, !1Y.; Nishi, Y.; Inagaki, M. !$#journal Biochem. Biophys. Res. Commun. (1990) 167:1316-1325 !$#title Involvement of protein kinase C in the regulation of !1assembly-disassembly of neurofilaments in vitro. !$#cross-references MUID:90211318; PMID:2108674 !$#accession A34569 !'##status preliminary !'##molecule_type protein !'##residues 9-14;23-29;30-53 ##label GON COMMENT Mammalian neurofilaments usually contain three polypeptides, !1L, M, and H (with apparent molecular weights of 68, 160, and !1200 kilodaltons, respectively). Structurally, each is !1organized like all other intermediate filament proteins: a !1conserved alpha-helical region, whose helices form !1interpolypeptide coiled coils, is flanked by highly variable !1non-alpha-helical domains. COMMENT The amino-terminal headpiece is basic with a high content of !1hydroxyamino acids. The carboxyl-terminal tailpiece has two !1distinct subdomains: domain a has many hydroxyamino acids !1and several beta turns; domain b is acidic and rich in !1glutamic acid and lysine residues. COMMENT The extra mass and high charge density that distinguish the !1neurofilament proteins from all other intermediate filament !1proteins are due to the tailpiece extensions. This region !1may form a charged scaffolding structure suitable for !1interaction with other neuronal components or ions. COMMENT The boundaries of the domains between residues 70-92 and !1399-402 are not yet clarified. COMMENT This protein was isolated from spinal cord. CLASSIFICATION #superfamily cytoskeletal keratin KEYWORDS coiled coil; intermediate filament FEATURE !$1-70 #domain head #label HED\ !$92-123 #domain coil 1a, alpha-helical rod #label R1A\ !$137-232 #domain coil 1b, alpha-helical rod #label R1B\ !$255-399 #domain coil 2, alpha-helical rod #label RD2\ !$402-548 #domain tail #label TAI\ !$402-442 #region tail subdomain a\ !$443-548 #region tail subdomain b SUMMARY #length 548 #molecular-weight 61894 #checksum 6469 SEQUENCE /// ENTRY QFMSL #type complete TITLE neurofilament triplet L protein - mouse ALTERNATE_NAMES 68K neurofilament protein; NF-L(low) protein; type IV IF protein ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Mar-1988 #sequence_revision 30-Sep-1993 #text_change 22-Jun-1999 ACCESSIONS A25227; A26562; A43772; A41012; I55316 REFERENCE A25227 !$#authors Lewis, S.A.; Cowan, N.J. !$#journal Mol. Cell. Biol. (1986) 6:1529-1534 !$#title Anomalous placement of introns in a member of the !1intermediate filament multigene family: an evolutionary !1conundrum. !$#cross-references MUID:87064433; PMID:3785173 !$#accession A25227 !'##molecule_type DNA !'##residues 1-543 ##label LEW !'##cross-references GB:M13016; NID:g200023; PIDN:AAA39810.1; !1PID:g387492 !'##note the authors translated the codon GGC for residue 5 as Ala, ACA !1for residue 88 as Ile, CAT for residue 99 as Asp, GAG for !1residue 121 as Gly, GAG for residue 131 as Gly, and CAG for !1residue 161 as Glu REFERENCE A26562 !$#authors Lewis, S.A.; Cowan, N.J. !$#journal J. Cell Biol. (1985) 100:843-850 !$#title Genetics, evolution, and expression of the 68,000-mol-wt !1neurofilament protein: isolation of a cloned cDNA probe. !$#cross-references MUID:85131334; PMID:3919033 !$#accession A26562 !'##molecule_type mRNA !'##residues 242-543 ##label LE2 !'##cross-references GB:X02165 !'##experimental_source brain REFERENCE A43772 !$#authors Julien, J.P.; Meyer, D.; Flavell, D.; Hurst, J.; Grosveld, !1F. !$#journal Brain Res. Mol. Brain Res. (1986) 1:243-250 !$#title Cloning and developmental expression of the murine !1neurofilament gene family. !$#accession A43772 !'##molecule_type mRNA !'##residues 1-5,'Y',7-8,'Y',10-64,'M',66-72,'L',74-98,'D',100-194,'R', !1196-202,204-239,'Y',241-543 ##label JUL !'##cross-references GB:M20480; NID:g200037; PIDN:AAA39814.1; !1PID:g200038 !'##note the authors translated the codon CGC for residue 195 as Ala REFERENCE A41012 !$#authors Sihag, R.K.; Nixon, R.A. !$#journal J. Biol. Chem. (1991) 266:18861-18867 !$#title Identification of Ser-55 as a major protein kinase A !1phosphorylation site on the 70-kDa subunit of !1neurofilaments. Early turnover during axonal transport. !$#cross-references MUID:92011653; PMID:1717455 !$#accession A41012 !'##molecule_type protein !'##residues 52-57 ##label SIH REFERENCE I55316 !$#authors Nakahira, K.; Ikenaka, K.; Wada, K.; Tamura, T. !$#journal J. Biol. Chem. (1990) 265:19786-19791 !$#title Structure of the 68-kDa neurofilament gene and regulation of !1its expression. !$#cross-references MUID:91060592; PMID:2246261 !$#accession I55316 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-5,'Y',7-8,'Y',10-28 ##label RES !'##cross-references GB:M55423; NID:g200027; PIDN:AAA39812.1; !1PID:g554245 COMMENT This is the most abundant of the three neurofilament !1proteins and, as the other nonepithelial intermediate !1filament proteins, it can form homopolymeric 10-nm !1filaments. GENETICS !$#introns 349/3; 391/2; 498/1 CLASSIFICATION #superfamily cytoskeletal keratin KEYWORDS coiled coil; intermediate filament FEATURE !$2-72 #domain head #label HED\ !$94-125 #domain coil 1a, alpha-helical rod #status predicted !8#label R1A\ !$126-138 #region linker 1\ !$139-234 #domain coil 1b, alpha-helical rod #status predicted !8#label R1B\ !$235-256 #region linker 12\ !$257-272 #domain coil 2a, alpha-helical rod #status predicted !8#label R2A\ !$273-281 #region linker 2\ !$282-401 #domain coil 2b, alpha-helical rod #status predicted !8#label R2B\ !$404-543 #domain tail #label TAI\ !$404-444 #region tail subdomain a\ !$445-543 #region tail subdomain b SUMMARY #length 543 #molecular-weight 61337 #checksum 4621 SEQUENCE /// ENTRY QFBO #type complete TITLE micro glutamic acid-rich protein - bovine ALTERNATE_NAMES neurofilament triplet L protein (fragment) ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 22-Nov-1996 ACCESSIONS A02964 REFERENCE A02964 !$#authors Isobe, T.; Okuyama, T. !$#journal FEBS Lett. (1985) 182:389-392 !$#title Brain micro glutamic acid-rich protein is the C-terminal !1endpiece of the neurofilament 68-kDa protein as determined !1by the primary sequence. !$#cross-references MUID:85154567; PMID:3884373 !$#accession A02964 !'##molecule_type protein !'##residues 1-82 ##label ISO COMMENT This acidic protein, isolated from the cytosolic fraction of !1brain tissue, contains only nine different amino acids, 50% !1of which are glutamic acid or glutamine. COMMENT The similarity of this sequence to part of the neurofilament !1triplet L protein suggests that it may arise by restricted !1proteolysis of the carboxyl end (thought to determine !1specificity) of the L protein. COMMENT Although there are, as yet, no known biological functions !1ascribed to this protein, proteolytic processing of !1neurofilament proteins is now regarded as a normal !1intracellular event related to cytoplasmic neuronal !1transport occurring in the presence of calcium ion and !1possibly involving a calcium-activated protease. CLASSIFICATION #superfamily cytoskeletal keratin KEYWORDS brain; coiled coil; cytosol; intermediate filament FEATURE !$1-82 #domain neurofilament triplet L protein tail !8subdomain b (fragment) #label SIG SUMMARY #length 82 #molecular-weight 9001 #checksum 7503 SEQUENCE /// ENTRY QFPGM #type fragments TITLE neurofilament triplet M protein - pig (fragments) ALTERNATE_NAMES 160K neurofilament protein; NF-M(medium) protein; type IV IF protein ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 31-Mar-1988 #sequence_revision 02-Jul-1998 #text_change 10-Jul-1998 ACCESSIONS A05075; S02570 REFERENCE A05075 !$#authors Geisler, N.; Fischer, S.; Vandekerckhove, J.; Plessmann, U.; !1Weber, K. !$#journal EMBO J. (1984) 3:2701-2706 !$#title Hybrid character of a large neurofilament protein (NF-M): !1intermediate filament type sequence followed by a long and !1acidic carboxy-terminal extension. !$#cross-references MUID:85076594; PMID:6439558 !$#accession A05075 !'##molecule_type protein !'##residues 1-454 ##label GEI !'##experimental_source spinal cord REFERENCE S02570 !$#authors Geisler, N.; Vandekerckhove, J.; Weber, K. !$#journal FEBS Lett. (1987) 221:403-407 !$#title Location and sequence characterization of the major !1phosphorylation sites of the high molecular mass !1neurofilament proteins M and H. !$#cross-references MUID:87304852; PMID:3114005 !$#accession S02570 !'##molecule_type protein !'##residues 438-450;455-459;460-475;476-514;515-532 ##label GEI2 !'##experimental_source spinal cord CLASSIFICATION #superfamily cytoskeletal keratin KEYWORDS blocked amino end; coiled coil; intermediate filament; !1phosphoprotein FEATURE !$1-98 #domain head #status predicted #label HED\ !$99-412 #domain alpha-helical rod #label ROD\ !$438-454,455-459, !$460-475,476-514 #domain tail (fragments) #status predicted #label !8TLP1\ !$515-532 #domain tail (fragment) #status predicted #label !8TLP2\ !$1 #modified_site blocked amino end (Ser) (probably !8acetylated) #status experimental\ !$456,462,465,479 #binding_site phosphate (Ser) (covalent) #status !8experimental SUMMARY #length 532 #checksum 5520 SEQUENCE /// ENTRY QFHUH #type complete TITLE neurofilament triplet H protein - human ALTERNATE_NAMES neurofilament protein, 112K ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jun-2000 ACCESSIONS S00979 REFERENCE S00979 !$#authors Lees, J.F.; Shneidman, P.S.; Skuntz, S.F.; Carden, M.J.; !1Lazzarini, R.A. !$#journal EMBO J. (1988) 7:1947-1955 !$#title The structure and organization of the human heavy !1neurofilament subunit (NF-H) and the gene encoding it. !$#cross-references MUID:88328981; PMID:3138108 !$#accession S00979 !'##molecule_type DNA !'##residues 1-1020 ##label LEE !'##cross-references EMBL:X15306; NID:g35028; PIDN:CAA33366.1; !1PID:g1841430 !'##note it is uncertain whether Met-1 or Met-2 is the initiator GENETICS !$#gene GDB:NEFH !'##cross-references GDB:120225; OMIM:162230 !$#map_position 22q12.1-22q13.1 !$#introns 295/1; 361/3; 403/2 CLASSIFICATION #superfamily neurofilament triplet H protein KEYWORDS coiled coil; heterotrimer; intermediate filament; nerve; !1phosphoprotein FEATURE !$1-100 #domain amino-terminal #label NTD\ !$101-410 #domain rod #status predicted #label ROD\ !$411-1020 #domain carboxyl-terminal #label CTD\ !$502-826 #region 14-residue repeats\ !$503,511,518,526, !$532,540,546,552, !$560,566,574,580, !$586,594,600,606, !$614,620,628,634, !$640,648,654,662, !$668,676,682,690, !$696,704,710,718, !$724,738,746,752, !$763,776,787,795, !$801,822 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$732,768 #binding_site phosphate (Thr) (covalent) #status !8predicted SUMMARY #length 1020 #molecular-weight 111779 #checksum 7921 SEQUENCE /// ENTRY QFMSH #type complete TITLE neurofilament triplet H protein - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 22-Jun-1999 ACCESSIONS JT0368; A43778; S42616 REFERENCE JT0368 !$#authors Julien, J.P.; Cote, F.; Beaudet, L.; Sidky, M.; Flavell, D.; !1Grosveld, F.; Mushynski, W. !$#journal Gene (1988) 68:307-314 !$#title Sequence and structure of the mouse gene coding for the !1largest neurofilament subunit. !$#cross-references MUID:89121513; PMID:3220257 !$#accession JT0368 !'##molecule_type DNA !'##residues 1-1087 ##label JUL !'##cross-references GB:M23349; GB:M24496; NID:g200034; PIDN:AAA39813.1; !1PID:g387493 REFERENCE A43778 !$#authors Shneidman, P.S.; Carden, M.J.; Lees, J.F.; Lazzarini, R.A. !$#journal Brain Res. Mol. Brain Res. (1988) 4:217-231 !$#title The structure of the largest murine neurofilament protein !1(NF-H) as revealed by cDNA and genomic sequences. !$#accession A43778 !'##status preliminary !'##molecule_type mRNA !'##residues 'M',1-132,'QA',134-199,'R',200-280,'T',282-491,'G',493-533, !1'GEAKSP',534-545,'R',547-696,721-813,'M',815-842,'ND', !1845-1087 ##label SHN !'##cross-references GB:M35131; NID:g200021; PIDN:AAA39809.1; !1PID:g200022 REFERENCE S42616 !$#authors Carden, M.J. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S42616 !'##status preliminary !'##molecule_type DNA !'##residues 1-132,'QA',134-199,'R',200-280,'T',282-491,'G',493-533, !1'GEAKSP',534-545,'R',547-696,721-813,'M',815-842,'ND', !1845-1087 ##label CAR !'##cross-references EMBL:Z31012; NID:g463249; PIDN:CAA83229.1; !1PID:g463250 GENETICS !$#gene nfh !$#introns 290/1; 356/3; 398/2 CLASSIFICATION #superfamily neurofilament triplet H protein KEYWORDS coiled coil; cytoskeleton; heterotrimer; intermediate !1filament; nerve; phosphoprotein; tandem repeat FEATURE !$1-97 #domain amino-terminal #label NTE\ !$98-408 #domain rod #status predicted #label ROD\ !$409-1087 #domain carboxyl-terminal #label CTE\ !$519-886 #region 6-residue repeats\ !$520,526,532,538, !$544,550,556,562, !$568,574,580,586, !$592,598,604,610, !$616,622,628,634, !$640,646,652,658, !$664,670,676,682, !$688,694,700,706, !$712,718,724,730, !$736,742,748,754, !$760,766,780,786, !$792,806,812,831, !$856,873,885 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$772 #binding_site phosphate (Thr) (covalent) #status !8predicted SUMMARY #length 1087 #molecular-weight 116612 #checksum 9298 SEQUENCE /// ENTRY A37221 #type complete TITLE neurofilament triplet H protein - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Dec-1999 ACCESSIONS A37221; A25649; A30796; A32757; B25649 REFERENCE A37221 !$#authors Chin, S.S.M.; Liem, R.K.H. !$#journal J. Neurosci. (1990) 10:3714-3726 !$#title Transfected rat high-molecular-weight neurofilament (NF-H) !1coassembles with vimentin in a predominantly !1nonphosphorylated form. !$#cross-references MUID:91038277; PMID:2230956 !$#accession A37221 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-1072 ##label CHI !'##cross-references GB:AF031879; NID:g2642597; PIDN:AAB87068.1; !1PID:g2642598 REFERENCE A25649 !$#authors Robinson, P.A.; Wion, D.; Anderton, B.H. !$#journal FEBS Lett. (1986) 209:203-205 !$#title Isolation of a cDNA for the rat heavy neurofilament !1polypeptide (NF-H). !$#cross-references MUID:87080760; PMID:2878828 !$#accession A25649 !'##molecule_type mRNA !'##residues 230-318;472-542 ##label ROB !'##cross-references GB:M37227 REFERENCE A30796 !$#authors Dautigny, A.; Pham-Dinh, D.; Roussel, C.; Felix, J.M.; !1Nussbaum, J.L.; Jolles, P. !$#journal Biochem. Biophys. Res. Commun. (1988) 154:1099-1106 !$#title The large neurofilament subunit (NF-H) of the rat: cDNA !1cloning and in situ detection. !$#cross-references MUID:88309090; PMID:2457365 !$#accession A30796 !'##molecule_type mRNA !'##residues 266-421,'T',423-427,'T',429-542,'V',556-566,'E',568-613, !1'A',615-725,'S',727-1009,'L',1011-1022,'E',1024-1072 ##label !1RAU !'##cross-references GB:M21964; NID:g205685; PIDN:AAA41695.1; !1PID:g205686 REFERENCE A32757 !$#authors Lieberburg, I.; Spinner, N.; Snyder, S.; Anderson, J.; !1Goldgaber, D.; Smulowitz, M.; Carroll, Z.; Emanuel, B.; !1Breitner, J.; Rubin, L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:2463-2467 !$#title Cloning of a cDNA encoding the rat high molecular weight !1neurofilament peptide (NF-H): developmental and tissue !1expression in the rat, and mapping of its human homologue to !1chromosomes 1 and 22. !$#cross-references MUID:89184647; PMID:2928342 !$#accession A32757 !'##status preliminary !'##molecule_type mRNA !'##residues 559-566,'E',568-967,'V',969-997,'GST',1001-1022,'E', !11024-1072 ##label LIE !'##cross-references GB:J04517; NID:g205679; PIDN:AAA41692.1; !1PID:g205680 CLASSIFICATION #superfamily neurofilament triplet H protein KEYWORDS coiled coil; heterotrimer; intermediate filament; nerve; !1phosphoprotein SUMMARY #length 1072 #molecular-weight 115348 #checksum 7479 SEQUENCE /// ENTRY SJGQBG #type complete TITLE giardin beta chain - Giardia lamblia ALTERNATE_NAMES beta-giardin; protein 14B ORGANISM #formal_name Giardia lamblia DATE 30-Sep-1991 #sequence_revision 12-Apr-1996 #text_change 10-Dec-1999 ACCESSIONS S52744; S03666; S02069 REFERENCE S52744 !$#authors Holberton, D.V. !$#submission submitted to the EMBL Data Library, March 1995 !$#accession S52744 !'##molecule_type DNA !'##residues 1-272 ##label HOL !'##cross-references EMBL:X85958; NID:g757856; PIDN:CAA59935.1; !1PID:g757857 REFERENCE S03666 !$#authors Baker, D.A.; Holberton, D.V.; Marshall, J. !$#journal Nucleic Acids Res. (1988) 16:7177 !$#title Sequence of a giardin subunit cDNA from Giardia lamblia. !$#cross-references MUID:88303337; PMID:3405761 !$#accession S03666 !'##molecule_type mRNA !'##residues 14-272 ##label BAK !'##cross-references EMBL:X07919; NID:g9356; PIDN:CAA30752.1; PID:g9357 REFERENCE S02069 !$#authors Holberton, D.; Baker, D.A.; Marshall, J. !$#journal J. Mol. Biol. (1988) 204:789-795 !$#title Segmented alpha-helical coiled-coil structure of the protein !1giardin from the Giardia cytoskeleton. !$#cross-references MUID:89141771; PMID:3225852 !$#accession S02069 !'##molecule_type mRNA !'##residues 14-272 ##label HO2 !'##cross-references EMBL:M36728; NID:g159102; PIDN:AAA29154.1; !1PID:g159103 CLASSIFICATION #superfamily giardin beta chain KEYWORDS coiled coil; cytoskeleton SUMMARY #length 272 #molecular-weight 30877 #checksum 2369 SEQUENCE /// ENTRY A40936 #type complete TITLE stathmin - human ALTERNATE_NAMES leukemia-associated phosphoprotein p18; oncoprotein 18; Pr22 protein; proliferation-related phosphoprotein p18 ORGANISM #formal_name Homo sapiens #common_name man DATE 28-May-1992 #sequence_revision 02-Jul-1996 #text_change 22-Jun-1999 ACCESSIONS A40936; A44780; S31624; S10565; A39215; S42211 REFERENCE A40936 !$#authors Melhem, R.F.; Zhu, X.; Hailat, N.; Strahler, J.R.; Hanash, !1S.M. !$#journal J. Biol. Chem. (1991) 266:17747-17753 !$#title Characterization of the gene for a proliferation-related !1phosphoprotein (oncoprotein 18) expressed in high amounts in !1acute leukemia. !$#cross-references MUID:92011487; PMID:1917919 !$#accession A40936 !'##molecule_type DNA !'##residues 1-149 ##label MEL !'##cross-references GB:M31303; NID:g189387; PIDN:AAA59971.1; !1PID:g189388 REFERENCE A44780 !$#authors Zhu, X.; Kozarsky, K.; Strahler, J.R.; Eckerskorn, C.; !1Lottspeich, F.; Melhem, R.; Lowe, J.; Fox, D.A.; Hanash, !1S.M.; Atweh, G.F. !$#journal J. Biol. Chem. (1989) 264:14556-14560 !$#title Molecular cloning of a novel human leukemia-associated gene. !1Evidence of conservation in animal species. !$#cross-references MUID:89340581; PMID:2760073 !$#accession A44780 !'##molecule_type mRNA !'##residues 1-149 ##label ZHU !'##cross-references GB:J04991; NID:g189425; PIDN:AAA59980.1; !1PID:g189426 REFERENCE S31624 !$#authors Marunouchi, T. !$#submission submitted to the EMBL Data Library, January 1992 !$#accession S31624 !'##status preliminary !'##molecule_type mRNA !'##residues 1-149 ##label MAR !'##cross-references EMBL:Z11566; NID:g1066270; PIDN:CAA77660.1; !1PID:g35595 REFERENCE S10565 !$#authors Maucuer, A.; Doye, V.; Sobel, A. !$#journal FEBS Lett. (1990) 264:275-278 !$#title A single amino acid difference distinguishes the human and !1the rat sequences of stathmin, a ubiquitous intracellular !1phosphoprotein associated with cell regulations. !$#cross-references MUID:90292224; PMID:2358074 !$#accession S10565 !'##status preliminary !'##molecule_type mRNA !'##residues 1-149 ##label MAU !'##cross-references GB:X53305; NID:g57869; PIDN:CAA37391.1; PID:g57870 REFERENCE A39215 !$#authors Gullberg, M.; Noreus, K.; Brattsand, G.; Friedrich, B.; !1Shingler, V. !$#journal J. Biol. Chem. (1990) 265:17499-17505 !$#title Purification and characterization of a 19-kilodalton !1intracellular protein. An activation-regulated putative !1protein kinase C substrate of T lymphocytes. !$#cross-references MUID:91009201; PMID:2211643 !$#accession A39215 !'##molecule_type protein !'##residues 117-136 ##label GUL REFERENCE S42211 !$#authors Brattsand, G.; Marklund, U.; Nylander, K.; Roos, G.; !1Gullberg, M. !$#journal Eur. J. Biochem. (1994) 220:359-368 !$#title Cell-cycle-regulated phosphorylation of oncoprotein 18 on !1Ser16, Ser25 and Ser38. !$#cross-references MUID:94170783; PMID:8125092 !$#accession S42211 !'##status preliminary !'##molecule_type protein !'##residues 11-44 ##label BRA REFERENCE A42591 !$#authors Labdon, J.E.; Nieves, E.; Schubart, U.K. !$#journal J. Biol. Chem. (1992) 267:3506-3513 !$#title Analysis of phosphoprotein p19 by liquid chromatography/mass !1spectrometry. Identification of two proline-directed serine !1phosphorylation sites and a blocked amino terminus. !$#cross-references MUID:92147715; PMID:1737801 !$#contents annotation; phosphorylation site REFERENCE A38982 !$#authors Beretta, L.; Dobransky, T.; Sobel, A. !$#journal J. Biol. Chem. (1993) 268:20076-20084 !$#title Multiple phosphorylation of stathmin: identification of four !1sites phosphorylated in intact cells and in vitro by cyclic !1AMP-dependent protein kinase and p34cdc2. !$#cross-references MUID:93388570; PMID:8376365 !$#contents annotation; phosphorylation site GENETICS !$#gene GDB:LAP18 !'##cross-references GDB:127971; OMIM:151442 !$#map_position 1p36.1-1p35 !$#introns 5/1; 62/3; 126/3 !$#note the first intron occurs before the initiator codon CLASSIFICATION #superfamily stathmin KEYWORDS cytosol; phosphoprotein FEATURE !$16 #binding_site phosphate (Ser) (covalent) (by protein !8kinase A and calmodulin-dependent kinase) #status !8experimental\ !$25 #binding_site phosphate (Ser) (covalent) (by MAP and !8cdc2 kinases) #status experimental\ !$38 #binding_site phosphate (Ser) (covalent) (by cdc2 !8kinase) #status experimental\ !$63 #binding_site phosphate (Ser) (covalent) (by protein !8kinase A) #status experimental SUMMARY #length 149 #molecular-weight 17302 #checksum 1901 SEQUENCE /// ENTRY S31791 #type complete TITLE stathmin - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S31791 REFERENCE S20720 !$#authors Godbout, R. !$#submission submitted to the EMBL Data Library, April 1992 !$#description Identification and characterization of transcripts present !1at elevated levels in the undifferentiated chick retina. !$#accession S31791 !'##status preliminary !'##molecule_type mRNA !'##residues 1-148 ##label GOD !'##cross-references EMBL:X67840; NID:g63792; PIDN:CAA48035.1; !1PID:g63793 CLASSIFICATION #superfamily stathmin KEYWORDS phosphoprotein SUMMARY #length 148 #molecular-weight 17082 #checksum 8231 SEQUENCE /// ENTRY QRHUMT #type complete TITLE microtubule-associated protein 2, splice form MAP-2b - human ALTERNATE_NAMES MAP2 ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1989 #sequence_revision 12-Apr-1996 #text_change 21-Jul-2000 ACCESSIONS I53693; A61085; PL0024; S34131 REFERENCE I53693 !$#authors Albala, J.S.; Kalcheva, N.; Shafit-Zagardo, B. !$#journal Gene (1993) 136:377-378 !$#title Characterization of the transcripts encoding two isoforms of !1human microtubule-associated protein-2 (MAP-2). !$#cross-references MUID:94124038; PMID:8294038 !$#accession I53693 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-1824 ##label ALB !'##cross-references EMBL:Z21958; GB:L12563; NID:g1850616; !1PIDN:AAB48098.1; PID:g1850617 REFERENCE A61085 !$#authors Dammerman, M.; Yen, S.H.; Shafit-Zagardo, B. !$#journal J. Neurosci. Res. (1989) 24:487-495 !$#title Sequence of a human MAP-2 region sharing epitopes with !1Alzheimer neurofibrillary tangles. !$#cross-references MUID:90096190; PMID:2481044 !$#accession A61085 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 77-645 ##label DAM REFERENCE PL0024 !$#authors Kosik, K.S.; Orecchio, L.D.; Bakalis, S.; Duffy, L.; Neve, !1R.L. !$#journal J. Neurochem. (1988) 51:587-598 !$#title Partial sequence of MAP2 in the region of a shared epitope !1with Alzheimer neurofibrillary tangles. !$#cross-references MUID:88274407; PMID:2455776 !$#accession PL0024 !'##molecule_type mRNA !'##residues 489-1558 ##label KOS !'##cross-references GB:M25668; NID:g187380; PIDN:AAA59552.1; !1PID:g187381 COMMENT Microtubule-associated proteins are a complex group !1consisting of the high molecular weight proteins MAP1 and !1MAP2 and a heterogeneous protein designated tau. Their !1function is unknown but they may stabilize the microtubules !1against depolymerization. GENETICS !$#gene GDB:MAP2 !'##cross-references GDB:118836; OMIM:157130 !$#map_position 2q34-2q35 CLASSIFICATION #superfamily microtubule-associated protein MAP2b; MAP2/tau !1repeat homology KEYWORDS alternative splicing; microtubule binding; phosphoprotein; !1tandem repeat FEATURE !$1455-1463 #region microtubule binding #status predicted\ !$1666-1696 #domain MAP2/tau repeat homology #label MT1\ !$1697-1727 #domain MAP2/tau repeat homology #label MT2\ !$1728-1759 #domain MAP2/tau repeat homology #label MT3\ !$657,958,1064,1250, !$1436,1503 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$697,817,829,1320, !$1417,1542,1551 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 1824 #molecular-weight 199166 #checksum 4659 SEQUENCE /// ENTRY QRHUT1 #type complete TITLE microtubule-associated protein tau, long splice form - human ALTERNATE_NAMES microtubule-binding protein tau; neurofibrillary tangle protein paired helical filament-tau; PHF-tau CONTAINS microtubule-associated protein tau type II; microtubule-associated protein tau, fetal ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1990 #sequence_revision 03-May-1996 #text_change 22-Jun-1999 ACCESSIONS JS0370; A30217; JN0009; S03796; S26665; S26666; S26662; !1S17302; A43444; A27669 REFERENCE JS0370 !$#authors Goedert, M.; Spillantini, M.G.; Jakes, R.; Rutherford, D.; !1Crowther, R.A. !$#journal Neuron (1989) 3:519-526 !$#title Multiple isoforms of human microtubule-associated protein !1tau: sequences and localization in neurofibrillary tangles !1of Alzheimer's disease. !$#cross-references MUID:90380393; PMID:2484340 !$#accession JS0370 !'##molecule_type mRNA !'##residues 1-441 ##label GOE !'##note six isoforms are found; the clone htau40 sequence is shown. !1Residues 45-73, 74-102, and 275-305 refer to inserts 1, 2, !1and 3, respectively; the clone htau23 sequence lacks all of !1the inserts; the clone htau24 sequence lacks inserts 1 and !12; the clone htau37 sequence lacks inserts 2 and 3; the !1clone htau34 sequence lacks insert 2; the clone htau39 !1sequence lacks insert 3 REFERENCE A30217 !$#authors Goedert, M.; Wischik, C.M.; Crowther, R.A.; Walker, J.E.; !1Klug, A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:4051-4055 !$#title Cloning and sequencing of the cDNA encoding a core protein !1of the paired helical filament of Alzheimer disease: !1identification as the microtubule-associated protein tau. !$#cross-references MUID:88234557; PMID:3131773 !$#accession A30217 !'##molecule_type mRNA !'##residues 1-44,103-274,306-441 ##label GO2 !'##cross-references GB:J03778; NID:g338684; PIDN:AAA60615.1; !1PID:g338685 REFERENCE JN0009 !$#authors Lee, G.; Neve, R.L.; Kosik, K.S. !$#journal Neuron (1989) 2:1615-1624 !$#title The microtubule binding domain of tau protein. !$#cross-references MUID:90180482; PMID:2516729 !$#accession JN0009 !'##molecule_type mRNA !'##residues 1-44,103-274,306-441 ##label LEE REFERENCE S03796 !$#authors Goedert, M.; Spillantini, M.G.; Potier, M.C.; Ulrich, J.; !1Crowther, R.A. !$#journal EMBO J. (1989) 8:393-399 !$#title Cloning and sequencing of the cDNA encoding an isoform of !1microtubule-associated protein tau containing four tandem !1repeats: differential expression of tau protein mRNAs in !1human brain. !$#cross-references MUID:89251564; PMID:2498079 !$#accession S03796 !'##molecule_type mRNA !'##residues 1-44,103-441 ##label GO3 !'##cross-references EMBL:X14474; NID:g36724; PIDN:CAA32636.1; !1PID:g36725 REFERENCE S26662 !$#authors Andreadis, A.; Brown, W.M.; Kosik, K.S. !$#journal Biochemistry (1992) 31:10626-10633 !$#title Structure and novel exons of the human tau gene. !$#cross-references MUID:93041757; PMID:1420178 !$#accession S26665 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 144-185 ##label AND !'##cross-references EMBL:X61372; NID:g36718; PID:g36719 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1991 !$#accession S26666 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 187-274 ##label AN2 !'##cross-references EMBL:X61374; NID:g36722; PID:g36723 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1991 !$#accession S26662 !'##molecule_type DNA !'##residues 371-441 ##label ANW !'##cross-references EMBL:X61373 REFERENCE S17302 !$#authors Jakes, R.; Novak, M.; Davison, M.; Wischik, C.M. !$#journal EMBO J. (1991) 10:2725-2729 !$#title Identification of 3- and 4-repeat tau isoforms within the !1PHF in Alzheimer's disease. !$#cross-references MUID:92007714; PMID:1915258 !$#accession S17302 !'##status preliminary !'##molecule_type protein !'##residues 268-274,306-395 ##label JAK REFERENCE A43444 !$#authors Hasegawa, M.; Morishima-Kawashima, M.; Takio, K.; Suzuki, !1M.; Titani, K.; Ihara, Y. !$#journal J. Biol. Chem. (1992) 267:17047-17054 !$#title Protein sequence and mass spectrometric analyses of tau in !1the Alzheimer's disease brain. !$#cross-references MUID:92381012; PMID:1512244 !$#accession A43444 !'##molecule_type protein !'##residues !12-73;103-130;151-180;191-254;260-269;275-290;299-317; !1322-340;344-347;354-383;386-441 ##label HAS !'##experimental_source Alzheimer's disease brain !'##note sequence extracted from NCBI backbone (NCBIP:112039) COMMENT This heterogeneous protein, which is found predominantly in !1cells of the nervous system, not only promotes assembly, but !1also stabilizes microtubules in the neuronal cell. It !1contributes to the core protein of the paired helical !1filament of Alzheimer's disease. GENETICS !$#gene GDB:MAPT !'##cross-references GDB:119434; OMIM:157140 !$#map_position 17q21-17q21 CLASSIFICATION #superfamily microtubule-associated protein tau; MAP2/tau !1repeat homology KEYWORDS alternative splicing; Alzheimer's disease; duplication; !1microtubule binding; tandem repeat FEATURE !$1-441 #product microtubule-associated protein tau, long !8splice form #status predicted #label MAT\ !$1-274,306-441 #product microtubule-associated protein tau (clone !8htau39) #status predicted #label MA6\ !$1-73,103-441 #product microtubule-associated protein tau (clone !8htau34) #status predicted #label MA5\ !$1-73,103-274, !$306-441 #product microtubule-associated protein tau (clone !8htau37) #status predicted #label MA4\ !$1-44,103-274, !$306-441 #product microtubule-associated protein tau, fetal !8#status predicted #label MA2\ !$1-44,103-441 #product microtubule-associated protein tau type II !8#status predicted #label MA3\ !$252-282 #domain MAP2/tau repeat homology #label MT1\ !$283-313 #domain MAP2/tau repeat homology #label MT2\ !$314-344 #domain MAP2/tau repeat homology #label MT3\ !$345-376 #domain MAP2/tau repeat homology #label MT4 SUMMARY #length 441 #molecular-weight 45850 #checksum 9299 SEQUENCE /// ENTRY QRHUT2 #type complete TITLE microtubule-associated protein tau, fetal (clone p18) - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 02-Sep-1997 ACCESSIONS PN0001 REFERENCE JN0009 !$#authors Lee, G.; Neve, R.L.; Kosik, K.S. !$#journal Neuron (1989) 2:1615-1624 !$#title The microtubule binding domain of tau protein. !$#cross-references MUID:90180482; PMID:2516729 !$#accession PN0001 !'##molecule_type mRNA !'##residues 1-316 ##label LEE !'##note this sequence differs from a previously reported fetal tau !1protein sequence only at the amino end, where the first 10 !1residues shown replace the first 46 residues of the longer !1sequence GENETICS !$#gene GDB:MAPT; MTBT1 !'##cross-references GDB:119434; OMIM:157140 !$#map_position 17q21-17q21 CLASSIFICATION #superfamily microtubule-associated protein tau; MAP2/tau !1repeat homology KEYWORDS alternative splicing; Alzheimer's disease; duplication; !1microtubule binding; tandem repeat FEATURE !$158-188 #domain MAP2/tau repeat homology #label MT1\ !$189-219 #domain MAP2/tau repeat homology #label MT2\ !$220-251 #domain MAP2/tau repeat homology #label MT3 SUMMARY #length 316 #molecular-weight 32944 #checksum 1790 SEQUENCE /// ENTRY QRBOT1 #type complete TITLE microtubule-associated protein tau, form 1 - bovine CONTAINS microtubule-associated protein tau, form 2 ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 22-Jun-1999 ACCESSIONS A31939; A33914; S04005; A48885; A28173; B33734 REFERENCE A31939 !$#authors Himmler, A.; Drechsel, D.; Kirschner, M.W.; Martin Jr., D.W. !$#journal Mol. Cell. Biol. (1989) 9:1381-1388 !$#title Tau consists of a set of proteins with repeated C-terminal !1microtubule-binding domains and variable N-terminal domains. !$#cross-references MUID:89261765; PMID:2498649 !$#accession A31939 !'##molecule_type mRNA !'##residues 1-448 ##label HIM !'##cross-references GB:M26157; NID:g514913; PIDN:AAA30770.1; !1PID:g514914 REFERENCE A33914 !$#authors Iqbal, K.; Grundke-Iqbal, I.; Smith, A.J.; George, L.; Tung, !1Y.C.; Zaidi, T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:5646-5650 !$#title Identification and localization of a tau-peptide to paired !1helical filaments of Alzheimer disease. !$#cross-references MUID:89315854; PMID:2501795 !$#accession A33914 !'##molecule_type protein !'##residues 28,'A',30-38,'IG',41,'AP',44,'LK' ##label IQB !'##experimental_source brain !'##note 40-Pro was also found REFERENCE S04005 !$#authors Iqbal, K.; Smith, A.J.; Zaidi, T.; Grundke-Iqbal, I. !$#journal FEBS Lett. (1989) 248:87-91 !$#title Microtubule-associated protein tau. Identification of a !1novel peptide from bovine brain. !$#cross-references MUID:89252057; PMID:2498127 !$#accession S04005 !'##molecule_type protein !'##residues 28,'A',30-38,'IG',41,'AP',44,'LK' ##label IQ2 !'##experimental_source brain !'##note 40-Pro was also found REFERENCE A48885 !$#authors Paudel, H.K.; Lew, J.; Ali, Z.; Wang, J.H. !$#journal J. Biol. Chem. (1993) 268:23512-23518 !$#title Brain proline-directed protein kinase phosphorylates tau on !1sites that are abnormally phosphorylated in tau associated !1with Alzheimer's paired helical filaments. !$#cross-references MUID:94043150; PMID:8226879 !$#accession A48885 !'##molecule_type protein !'##residues 'X',203-208,'X',210-211,'X',213-216;238-241,'X',243-247, !1'X';404-410,'X',412-413 ##label PAU !'##experimental_source brain !'##note sequence modified after extraction from NCBI backbone REFERENCE A28173 !$#authors Aizawa, H.; Kawasaki, H.; Murofushi, H.; Kotani, S.; Suzuki, !1K.; Sakai, H. !$#journal J. Biol. Chem. (1988) 263:7703-7707 !$#title Microtubule-binding domain of Tau proteins. !$#cross-references MUID:88227970; PMID:3131325 !$#accession A28173 !'##molecule_type protein !'##residues 205-218,'X',220-223 ##label AIZ !'##experimental_source brain CLASSIFICATION #superfamily microtubule-associated protein tau; MAP2/tau !1repeat homology KEYWORDS alternative splicing; microtubule binding; phosphoprotein; !1tandem repeat FEATURE !$1-448 #product microtubule-associated protein tau, form 1 !8#status predicted #label BT43\ !$1-174,193-448 #product microtubule-associated protein tau, form 2 !8#status predicted #label BT12\ !$205-223 #region microtubule binding #status experimental\ !$259-289 #domain MAP2/tau repeat homology #label MT1\ !$290-320 #domain MAP2/tau repeat homology #label MT2\ !$321-351 #domain MAP2/tau repeat homology #label MT3\ !$352-383 #domain MAP2/tau repeat homology #label MT4\ !$202,209,242,248,411 #binding_site phosphate (Ser) (covalent) (by !8proline-directed kinase) #status experimental\ !$212 #binding_site phosphate (Thr) (covalent) (by !8proline-directed kinase) #status experimental SUMMARY #length 448 #molecular-weight 46332 #checksum 9301 SEQUENCE /// ENTRY QRBOT2 #type complete TITLE microtubule-associated protein tau, form 3 - bovine CONTAINS microtubule-associated protein tau, form 4; microtubule-associated protein tau, form 5 ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 31-Mar-1996 ACCESSIONS B31939; A48885; A28173 REFERENCE A31939 !$#authors Himmler, A.; Drechsel, D.; Kirschner, M.W.; Martin Jr., D.W. !$#journal Mol. Cell. Biol. (1989) 9:1381-1388 !$#title Tau consists of a set of proteins with repeated C-terminal !1microtubule-binding domains and variable N-terminal domains. !$#cross-references MUID:89261765; PMID:2498649 !$#accession B31939 !'##molecule_type mRNA !'##residues 1-402 ##label HIM !'##cross-references GB:M26157; GB:M26158 REFERENCE A48885 !$#authors Paudel, H.K.; Lew, J.; Ali, Z.; Wang, J.H. !$#journal J. Biol. Chem. (1993) 268:23512-23518 !$#title Brain proline-directed protein kinase phosphorylates tau on !1sites that are abnormally phosphorylated in tau associated !1with Alzheimer's paired helical filaments. !$#cross-references MUID:94043150; PMID:8226879 !$#accession A48885 !'##molecule_type protein !'##residues 'X',157-162,'X',164-165,'X',167-170;192-195,'X',197-201, !1'X';358-364,'X',366-367 ##label PAU !'##experimental_source brain !'##note sequence modified after extraction from NCBI backbone REFERENCE A28173 !$#authors Aizawa, H.; Kawasaki, H.; Murofushi, H.; Kotani, S.; Suzuki, !1K.; Sakai, H. !$#journal J. Biol. Chem. (1988) 263:7703-7707 !$#title Microtubule-binding domain of Tau proteins. !$#cross-references MUID:88227970; PMID:3131325 !$#accession A28173 !'##molecule_type protein !'##residues 159-172,'X',174-177 ##label AIZ !'##experimental_source brain CLASSIFICATION #superfamily microtubule-associated protein tau; MAP2/tau !1repeat homology KEYWORDS alternative splicing; microtubule binding; phosphoprotein; !1tandem repeat FEATURE !$1-402 #product microtubule-associated protein tau, form 3 !8#status predicted #label BT4\ !$1-234,297-402 #product microtubule-associated protein tau, form 5 !8#status predicted #label BT20\ !$101-402 #product microtubule-associated protein tau, form 4 !8#status predicted #label BT7\ !$159-177 #region microtubule binding #status experimental\ !$213-243 #domain MAP2/tau repeat homology #label MT1\ !$244-274 #domain MAP2/tau repeat homology #label MT2\ !$275-305 #domain MAP2/tau repeat homology #label MT3\ !$306-337 #domain MAP2/tau repeat homology #label MT4\ !$156,163,196,202,365 #binding_site phosphate (Ser) (covalent) (by !8proline-directed kinase) #status predicted\ !$166 #binding_site phosphate (Thr) (covalent) (by !8proline-directed kinase) #status predicted SUMMARY #length 402 #molecular-weight 42232 #checksum 1750 SEQUENCE /// ENTRY QRMSP1 #type complete TITLE microtubule-associated protein MAP1B - mouse ALTERNATE_NAMES microtubule-associated protein MAP1(X); microtubule-associated protein MAP1.2; microtubule-associated protein MAP5 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 01-Sep-2000 ACCESSIONS S07549; S44387; A33645 REFERENCE A33645 !$#authors Noble, M.; Lewis, S.A.; Cowan, N.J. !$#journal J. Cell Biol. (1989) 109:3367-3376 !$#title The microtubule binding domain of microtubule-associated !1protein MAP1B contains a repeated sequence motif unrelated !1to that of MAP2 and tau. !$#cross-references MUID:90094539; PMID:2480963 !$#accession S07549 !'##molecule_type mRNA !'##residues 1-2464 ##label NOB !'##cross-references EMBL:X51396; NID:g52999; PIDN:CAA35761.1; !1PID:g53000 REFERENCE S44387 !$#authors Sanchez, C.; Padilla, R.; Paciucci, R.; Zabala, J.C.; Avila, !1J. !$#journal Arch. Biochem. Biophys. (1994) 310:428-432 !$#title Binding of heat-shock protein 70 (hsp70) to tubulin. !$#cross-references MUID:94234720; PMID:8179328 !$#accession S44387 !'##status preliminary !'##molecule_type protein !'##residues 653-663,'IC' ##label SAN CLASSIFICATION #superfamily microtubule-associated protein MAP1B KEYWORDS microtubule binding; phosphoprotein; tandem repeat FEATURE !$589-786 #domain microtubule binding #status experimental !8#label MTB\ !$589-592,639-642, !$649-652,655-658, !$660-663,668-671, !$674-677,679-682, !$683-686,687-690, !$691-694,695-698, !$699-702,708-711, !$712-715,716-719, !$720-723,727-730, !$758-761,764-767, !$783-786 #region 4-residue repeats (K/R-K-E/D-X)\ !$1861-2064 #region 17-residue repeats\ !$91,116,351,888, !$1124,1153,1168, !$1208,1662,1877, !$1918,2003,2030, !$2054,2083 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$147,969,1336,1562, !$1563,1702,1708, !$1990,2057,2063,2419 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$1953 #binding_site phosphate (Tyr) (covalent) #status !8predicted SUMMARY #length 2464 #molecular-weight 270408 #checksum 2525 SEQUENCE /// ENTRY LRRTB2 #type fragment TITLE clathrin light chain B2 - rat (fragment) ALTERNATE_NAMES LCB2 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 10-Dec-1999 ACCESSIONS B25994 REFERENCE A94292 !$#authors Kirchhausen, T.; Scarmato, P.; Harrison, S.C.; Monroe, J.J.; !1Chow, E.P.; Mattaliano, R.J.; Ramachandran, K.L.; Smart, !1J.E.; Ahn, A.H.; Brosius, J. !$#journal Science (1987) 236:320-324 !$#title Clathrin light chains LCA and LCB are similar, polymorphic, !1and share repeated heptad motifs. !$#cross-references MUID:87178007; PMID:3563513 !$#accession B25994 !'##molecule_type mRNA !'##residues 1-238 ##label KIR CLASSIFICATION #superfamily clathrin light chain KEYWORDS alternative splicing; coated pits; coiled coil; endocytosis; !1phosphoprotein FEATURE !$102-172 #domain coiled coil #label HEP SUMMARY #length 238 #checksum 8849 SEQUENCE /// ENTRY LRRTA1 #type fragment TITLE clathrin light chain A1 - rat (fragment) ALTERNATE_NAMES LCA1 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 10-Dec-1999 ACCESSIONS A25994 REFERENCE A94292 !$#authors Kirchhausen, T.; Scarmato, P.; Harrison, S.C.; Monroe, J.J.; !1Chow, E.P.; Mattaliano, R.J.; Ramachandran, K.L.; Smart, !1J.E.; Ahn, A.H.; Brosius, J. !$#journal Science (1987) 236:320-324 !$#title Clathrin light chains LCA and LCB are similar, polymorphic, !1and share repeated heptad motifs. !$#cross-references MUID:87178007; PMID:3563513 !$#accession A25994 !'##molecule_type mRNA !'##residues 1-286 ##label KIR COMMENT Clathrin, the major protein component of coated pits and !1vesicles, is a three-legged, pinwheel-shaped structure. Each !1leg contains a heavy chain with a light chain noncovalently !1bonded near its carboxyl end. The heavy chains are also held !1together by noncovalent interactions. COMMENT Each light chain class contains multiple forms (probably the !1result of alternative mRNA splicing). CLASSIFICATION #superfamily clathrin light chain KEYWORDS alternative splicing; coated pits; coiled coil; endocytosis FEATURE !$138-238 #domain coiled coil #label HEP SUMMARY #length 286 #checksum 2958 SEQUENCE /// ENTRY LRRTH #type complete TITLE clathrin heavy chain - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 22-Jun-1999 ACCESSIONS A39941 REFERENCE A39941 !$#authors Kirchhausen, T.; Harrison, S.C.; Ping Chow, E.; Mattaliano, !1R.J.; Ramachandran, K.L.; Smart, J.; Brosius, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:8805-8809 !$#title Clathrin heavy chain: molecular cloning and complete primary !1structure. !$#cross-references MUID:88097376; PMID:3480512 !$#accession A39941 !'##molecule_type mRNA !'##residues 1-1675 ##label KIR !'##cross-references GB:J03583; NID:g203301; PIDN:AAA40874.1; !1PID:g203302 COMMENT Clathrin, the major protein component of coated pits and !1vesicles, is a three-legged, pinwheel-shaped structure. Each !1leg contains a heavy chain with a light chain noncovalently !1bonded near its carboxyl end. The heavy chains are also held !1together by noncovalent interactions. COMMENT The amino end of the mature protein is blocked. CLASSIFICATION #superfamily clathrin heavy chain KEYWORDS coated pits FEATURE !$1-479 #domain amino-terminal #label TER\ !$480-523 #region link\ !$524-634 #domain distal #label DIS\ !$635-638 #region joint #status predicted\ !$639-1675 #domain proximal #label PRX SUMMARY #length 1675 #molecular-weight 191597 #checksum 8002 SEQUENCE /// ENTRY GJRT #type complete TITLE gap junction protein Cx32 - rat ALTERNATE_NAMES connexin 32; gap junction beta-1 protein ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 22-Jun-1999 ACCESSIONS A92745; A92530; I53461; A24231; A26278; B24047 REFERENCE A92745 !$#authors Paul, D.L. !$#journal J. Cell Biol. (1986) 103:123-134 !$#title Molecular cloning of cDNA for rat liver gap junction !1protein. !$#cross-references MUID:86251013; PMID:3013898 !$#accession A92745 !'##molecule_type mRNA !'##residues 1-283 ##label PAU !'##cross-references GB:X04070; NID:g56205; PIDN:CAA27705.1; PID:g56206 REFERENCE A92530 !$#authors Nicholson, B.J.; Gros, D.B.; Kent, S.B.H.; Hood, L.E.; !1Revel, J.P. !$#journal J. Biol. Chem. (1985) 260:6514-6517 !$#title The Mr 28,000 gap junction proteins from rat heart and liver !1are different but related. !$#cross-references MUID:85207650; PMID:2987225 !$#accession A92530 !'##molecule_type protein !'##residues 1-40 ##label NIC REFERENCE A92647 !$#authors Zimmer, D.B.; Green, C.R.; Evans, W.H.; Gilula, N.B. !$#journal J. Biol. Chem. (1987) 262:7751-7763 !$#title Topological analysis of the major protein in isolated intact !1rat liver gap junctions and gap junction-derived single !1membrane structures. !$#cross-references MUID:87222403; PMID:3034905 !$#contents annotation; topology REFERENCE A90891 !$#authors Loewenstein, W.R. !$#journal Cell (1987) 48:725-726 !$#title The cell-to-cell channel of gap junctions. !$#cross-references MUID:87131085; PMID:3815521 !$#contents annotation; minireview REFERENCE I53461 !$#authors Heynkes, R.; Kozjek, G.; Traub, O.; Willecke, K. !$#journal FEBS Lett. (1986) 205:56-60 !$#title Identification of a rat liver cDNA and mRNA coding for the !128 kDa gap junction protein. !$#cross-references MUID:86301142; PMID:3017758 !$#accession I53461 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 7-120 ##label RES !'##cross-references EMBL:X04303; NID:g56191; PIDN:CAA27846.1; !1PID:g939964 COMMENT The gap junction is a specialized plasma membrane structure !1composed of clusters of intercellular channels that connect !1the cytoplasms of adjacent cells, enabling direct !1communication of small molecules between them. It is !1regulated by intracellular conditions (calcium !1concentration, transmembrane potential, and pH), !1phosphorylation, and calmodulin. COMMENT The channel structure is symmetrical and bipartite with one !1half of the structure contributed by each cell. Each half is !1composed of six identical chains aggregated axially. !1End-to-end aggregation of both halves forms the !1transmembrane tunnel (with an internal diameter of 16-20 !1angstroms in mammalian cells). A shutter mechanism seals off !1the channel when intracellular conditions dictate. COMMENT Topological predictions include cytoplasmic amino and !1carboxyl ends and a transmembrane domain that crosses the !1membrane at least four times. X-ray diffraction confirms !1significant beta-sheet conformation within the hydrophobic !1regions. CLASSIFICATION #superfamily gap junction protein KEYWORDS calcium; gap junction; liver; phosphoprotein; transmembrane !1protein FEATURE !$1-17 #domain intracellular #status predicted #label INT1\ !$18-40 #domain transmembrane #status predicted #label TM1\ !$41-73 #domain extracellular #status predicted #label EE1\ !$74-96 #domain transmembrane #status predicted #label TM2\ !$97-128 #domain intracellular #status predicted #label INT2\ !$129-160 #domain transmembrane #status predicted #label TM3\ !$161-187 #domain extracellular #status predicted #label EE2\ !$188-214 #domain transmembrane #status predicted #label TM4\ !$215-283 #domain intracellular #status predicted #label INT3\ !$229,240,281 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 283 #molecular-weight 32003 #checksum 2199 SEQUENCE /// ENTRY B49769 #type complete TITLE gap junction protein Cx32 - mouse ALTERNATE_NAMES connexin 32; gap junction beta-1 protein ORGANISM #formal_name Mus musculus #common_name house mouse DATE 07-Apr-1994 #sequence_revision 02-Jun-1994 #text_change 01-Nov-1996 ACCESSIONS B49769 REFERENCE A49769 !$#authors Nishi, M.; Kumar, N.M.; Gilula, N.B. !$#journal Dev. Biol. (1991) 146:117-130 !$#title Developmental regulation of gap junction gene expression !1during mouse embryonic development. !$#cross-references MUID:91285228; PMID:2060697 !$#accession B49769 !'##molecule_type mRNA !'##residues 1-283 ##label NIS !'##cross-references GB:M63802 CLASSIFICATION #superfamily gap junction protein KEYWORDS gap junction; phosphoprotein; transmembrane protein FEATURE !$1-17 #domain intracellular #status predicted #label INT1\ !$18-40 #domain transmembrane #status predicted #label TM1\ !$41-73 #domain extracellular #status predicted #label EE1\ !$74-96 #domain transmembrane #status predicted #label TM2\ !$97-128 #domain intracellular #status predicted #label INT2\ !$129-160 #domain transmembrane #status predicted #label TM3\ !$161-187 #domain extracellular #status predicted #label EE2\ !$188-214 #domain transmembrane #status predicted #label TM4\ !$215-283 #domain intracellular #status predicted #label INT3\ !$229,240,281 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 283 #molecular-weight 31982 #checksum 3371 SEQUENCE /// ENTRY B29005 #type complete TITLE gap junction protein Cx32 - human ALTERNATE_NAMES connexin 32; gap junction beta-1 protein ORGANISM #formal_name Homo sapiens #common_name man DATE 21-May-1988 #sequence_revision 02-Jun-1994 #text_change 22-Jun-1999 ACCESSIONS B29005; S02460 REFERENCE A29005 !$#authors Kumar, N.M.; Gilula, N.B. !$#journal J. Cell Biol. (1986) 103:767-776 !$#title Cloning and characterization of human and rat liver cDNAs !1coding for a gap junction protein. !$#cross-references MUID:86304555; PMID:2875078 !$#accession B29005 !'##molecule_type mRNA !'##residues 1-283 ##label KUM !'##cross-references EMBL:X04325; NID:g31646; PIDN:CAA27856.1; !1PID:g31647 REFERENCE S02460 !$#authors Milks, L.C.; Kumar, N.M.; Houghten, R.; Unwin, N.; Gilula, !1N.B. !$#journal EMBO J. (1988) 7:2967-2975 !$#title Topology of the 32-kd liver gap junction protein determined !1by site-directed antibody localizations. !$#cross-references MUID:89030588; PMID:2460334 !$#contents annotation; membrane topology is described GENETICS !$#gene GDB:GJB1; CMTX1; CMTX !'##cross-references GDB:125246; OMIM:304040 !$#map_position Xq13.1-Xq13.1 !$#note defects in this gene can result in X-linked !1Charcot-Marie-Tooth neuropathy CLASSIFICATION #superfamily gap junction protein KEYWORDS gap junction; liver; phosphoprotein; transmembrane protein FEATURE !$1-17 #domain intracellular #status predicted #label INT1\ !$18-40 #domain transmembrane #status predicted #label TM1\ !$41-73 #domain extracellular #status predicted #label EE1\ !$74-96 #domain transmembrane #status predicted #label TM2\ !$97-128 #domain intracellular #status predicted #label INT2\ !$129-160 #domain transmembrane #status predicted #label TM3\ !$161-187 #domain extracellular #status predicted #label EE2\ !$188-214 #domain transmembrane #status predicted #label TM4\ !$215-283 #domain intracellular #status predicted #label INT3\ !$229,240,281 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 283 #molecular-weight 32024 #checksum 4493 SEQUENCE /// ENTRY A31102 #type complete TITLE gap junction protein Cx30 - African clawed frog ALTERNATE_NAMES connexin 30; gap junction beta-1 protein ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 31-Mar-1990 #sequence_revision 02-Jun-1994 #text_change 22-Jun-1999 ACCESSIONS A31102; S05284 REFERENCE A31102 !$#authors Gimlich, R.L.; Kumar, N.M.; Gilula, N.B. !$#journal J. Cell Biol. (1988) 107:1065-1073 !$#title Sequence and developmental expression of mRNA coding for a !1gap junction protein in Xenopus. !$#cross-references MUID:88331091; PMID:2843548 !$#accession A31102 !'##molecule_type mRNA !'##residues 1-265 ##label GIM !'##cross-references EMBL:Y00791 REFERENCE S05284 !$#authors Gimlich, R.L. !$#submission submitted to the EMBL Data Library, July 1988 !$#accession S05284 !'##molecule_type mRNA !'##residues 1-109,'R',111-165,'L',167-252,254-265 ##label GI2 !'##cross-references EMBL:Y00791; NID:g64711; PIDN:CAA68745.1; !1PID:g64712 CLASSIFICATION #superfamily gap junction protein KEYWORDS gap junction; phosphoprotein; transmembrane protein FEATURE !$1-17 #domain intracellular #status predicted #label INT1\ !$18-40 #domain transmembrane #status predicted #label TM1\ !$41-73 #domain extracellular #status predicted #label EE1\ !$74-96 #domain transmembrane #status predicted #label TM2\ !$97-128 #domain intracellular #status predicted #label INT2\ !$129-160 #domain transmembrane #status predicted #label TM3\ !$161-187 #domain extracellular #status predicted #label EE2\ !$188-214 #domain transmembrane #status predicted #label TM4\ !$215-265 #domain intracellular #status predicted #label INT3\ !$171 #binding_site phosphate (Tyr) (covalent) #status !8predicted\ !$227 #binding_site phosphate (Ser) (covalent) (by protein !8kinase A) #status predicted SUMMARY #length 265 #molecular-weight 29979 #checksum 8038 SEQUENCE /// ENTRY A43424 #type complete TITLE gap junction protein Cx26 - human ALTERNATE_NAMES connexin 26; gap junction beta-2 protein ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1993 #sequence_revision 02-Jun-1994 #text_change 21-Jul-2000 ACCESSIONS A43424 REFERENCE A43424 !$#authors Lee, S.W.; Tomasetto, C.; Paul, D.; Keyomarsi, K.; Sager, R. !$#journal J. Cell Biol. (1992) 118:1213-1221 !$#title Transcriptional downregulation of gap-junction proteins !1blocks junctional communication in human mammary tumor cell !1lines. !$#cross-references MUID:92381106; PMID:1324944 !$#accession A43424 !'##molecule_type mRNA !'##residues 1-226 ##label LEE !'##cross-references GB:M86849; NID:g4481752; PIDN:AAD21314.1; !1PID:g4481753 !'##experimental_source N76, normal human mammary epithelial cells !'##note sequence extracted from NCBI backbone (NCBIN:111954, !1NCBIP:111955) GENETICS !$#gene GDB:GJB2 !'##cross-references GDB:125247; OMIM:121011 !$#map_position 13q11-13q12.1 CLASSIFICATION #superfamily gap junction protein KEYWORDS calcium; gap junction; phosphoprotein; transmembrane protein FEATURE !$1-17 #domain intracellular #status predicted #label INT1\ !$18-40 #domain transmembrane #status predicted #label TM1\ !$41-73 #domain extracellular #status predicted #label EE1\ !$74-96 #domain transmembrane #status predicted #label TM2\ !$97-129 #domain intracellular #status predicted #label INT2\ !$130-161 #domain transmembrane #status predicted #label TM3\ !$162-188 #domain extracellular #status predicted #label EE2\ !$189-215 #domain transmembrane #status predicted #label TM4\ !$97,217 #binding_site phosphate (Tyr) (covalent) #status !8predicted\ !$219 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 226 #molecular-weight 26201 #checksum 7506 SEQUENCE /// ENTRY C49769 #type complete TITLE gap junction protein Cx26 - mouse ALTERNATE_NAMES connexin 26; gap junction beta-2 protein ORGANISM #formal_name Mus musculus #common_name house mouse DATE 07-Apr-1994 #sequence_revision 02-Jun-1994 #text_change 22-Jun-1999 ACCESSIONS C49769; A56601 REFERENCE A49769 !$#authors Nishi, M.; Kumar, N.M.; Gilula, N.B. !$#journal Dev. Biol. (1991) 146:117-130 !$#title Developmental regulation of gap junction gene expression !1during mouse embryonic development. !$#cross-references MUID:91285228; PMID:2060697 !$#accession C49769 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-226 ##label NIS !'##cross-references GB:M63803 !'##note the authors translated the codon CAC for residue 68 as Tyr and !1GTT for residue 215 as Ile REFERENCE A56601 !$#authors Hennemann, H.; Kozjek, G.; Dahl, E.; Nicholson, B.; !1Willecke, K. !$#journal Eur. J. Cell Biol. (1992) 58:81-89 !$#title Molecular cloning of mouse connexins26 and -32: similar !1genomic organization but distinct promoter sequences of two !1gap junction genes. !$#cross-references MUID:92354576; PMID:1322820 !$#accession A56601 !'##status preliminary !'##molecule_type DNA !'##residues 1-67,'H',69-214,'V',216-226 ##label HEN !'##cross-references GB:M81445; NID:g192844; PIDN:AAA37495.1; !1PID:g192845 !'##note sequence extracted from NCBI backbone (NCBIN:110434, !1NCBIP:110439) GENETICS !$#introns #status absent !$#note the entire coding region lies within exon 2 CLASSIFICATION #superfamily gap junction protein KEYWORDS calcium; gap junction; phosphoprotein; transmembrane protein FEATURE !$1-17 #domain intracellular #status predicted #label INT1\ !$18-40 #domain transmembrane #status predicted #label TM1\ !$41-73 #domain extracellular #status predicted #label EE1\ !$74-96 #domain transmembrane #status predicted #label TM2\ !$97-129 #domain intracellular #status predicted #label INT2\ !$130-161 #domain transmembrane #status predicted #label TM3\ !$162-188 #domain extracellular #status predicted #label EE2\ !$189-215 #domain transmembrane #status predicted #label TM4\ !$97,217 #binding_site phosphate (Tyr) (covalent) #status !8predicted\ !$219 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 226 #molecular-weight 26451 #checksum 7638 SEQUENCE /// ENTRY A33646 #type complete TITLE gap junction protein Cx26, hepatic - rat ALTERNATE_NAMES connexin 26; gap junction beta-2 protein ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 11-Apr-1990 #sequence_revision 02-Jun-1994 #text_change 01-Nov-1996 ACCESSIONS A33646 REFERENCE A33646 !$#authors Zhang, J.T.; Nicholson, B.J. !$#journal J. Cell Biol. (1989) 109:3391-3401 !$#title Sequence and tissue distribution of a second protein of !1hepatic gap junctions, Cx26, as deduced from its cDNA. !$#cross-references MUID:90094541; PMID:2557354 !$#accession A33646 !'##molecule_type mRNA !'##residues 1-226 ##label ZHA !'##cross-references GB:X51615 CLASSIFICATION #superfamily gap junction protein KEYWORDS gap junction; liver; phosphoprotein; transmembrane protein FEATURE !$1-17 #domain intracellular #status predicted #label INT1\ !$18-40 #domain transmembrane #status predicted #label TM1\ !$41-73 #domain extracellular #status predicted #label EE1\ !$74-96 #domain transmembrane #status predicted #label TM2\ !$97-129 #domain intracellular #status predicted #label INT2\ !$130-161 #domain transmembrane #status predicted #label TM3\ !$162-188 #domain extracellular #status predicted #label EE2\ !$189-215 #domain transmembrane #status predicted #label TM4\ !$97,217 #binding_site phosphate (Tyr) (covalent) #status !8predicted\ !$219 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 226 #molecular-weight 26451 #checksum 7638 SEQUENCE /// ENTRY A48171 #type complete TITLE gap junction protein Cx43 - chicken ALTERNATE_NAMES connexin 43; gap junction alpha-1 protein ORGANISM #formal_name Gallus gallus #common_name chicken DATE 03-Feb-1994 #sequence_revision 02-Jun-1994 #text_change 22-Jun-1999 ACCESSIONS A48171 REFERENCE A48171 !$#authors Musil, L.S.; Beyer, E.C.; Goodenough, D.A. !$#journal J. Membr. Biol. (1990) 116:163-175 !$#title Expression of the gap junction protein connexin43 in !1embryonic chick lens: molecular cloning, ultrastructural !1localization, and post-translational phosphorylation. !$#cross-references MUID:90339470; PMID:2166164 !$#accession A48171 !'##molecule_type mRNA !'##residues 1-381 ##label MUS !'##cross-references GB:M29003; NID:g211642; PIDN:AAA48715.1; !1PID:g211643 CLASSIFICATION #superfamily gap junction protein KEYWORDS gap junction; phosphoprotein; transmembrane protein FEATURE !$1-18 #domain intracellular #status predicted #label INT1\ !$19-41 #domain transmembrane #status predicted #label TM1\ !$42-76 #domain extracellular #status predicted #label EE1\ !$77-98 #domain transmembrane #status predicted #label TM2\ !$99-153 #domain intracellular #status predicted #label INT2\ !$154-184 #domain transmembrane #status predicted #label TM3\ !$185-206 #domain extracellular #status predicted #label EE2\ !$207-229 #domain transmembrane #status predicted #label TM4\ !$230-381 #domain intracellular #status predicted #label INT3\ !$296,364,367,368, !$371,372 #binding_site phosphate (Ser) (covalent) (by protein !8kinase C) #status predicted SUMMARY #length 381 #molecular-weight 43172 #checksum 8914 SEQUENCE /// ENTRY A35853 #type complete TITLE gap junction protein Cx43, cardiac - human ALTERNATE_NAMES connexin 43; gap junction alpha-1 protein ORGANISM #formal_name Homo sapiens #common_name man DATE 23-Oct-1990 #sequence_revision 02-Jun-1994 #text_change 16-Jul-1999 ACCESSIONS A35853; S10470 REFERENCE A35853 !$#authors Fishman, G.I.; Spray, D.C.; Leinwand, L.A. !$#journal J. Cell Biol. (1990) 111:589-598 !$#title Molecular characterization and functional expression of the !1human cardiac gap junction channel. !$#cross-references MUID:90338113; PMID:1696265 !$#accession A35853 !'##molecule_type mRNA !'##residues 1-382 ##label FIS !'##cross-references GB:X52947; NID:g29916; PIDN:CAA37122.1; PID:g29917 GENETICS !$#gene GDB:GJA1 !'##cross-references GDB:125196; OMIM:121014 !$#map_position 6q21-6q23.2 CLASSIFICATION #superfamily gap junction protein KEYWORDS cardiac muscle; gap junction; heart; phosphoprotein; !1transmembrane protein FEATURE !$1-18 #domain intracellular #status predicted #label INT1\ !$19-41 #domain transmembrane #status predicted #label TM1\ !$42-76 #domain extracellular #status predicted #label EE1\ !$77-98 #domain transmembrane #status predicted #label TM2\ !$99-153 #domain intracellular #status predicted #label INT2\ !$154-184 #domain transmembrane #status predicted #label TM3\ !$185-206 #domain extracellular #status predicted #label EE2\ !$207-229 #domain transmembrane #status predicted #label TM4\ !$230-382 #domain intracellular #status predicted #label INT3\ !$297,364,365,368, !$369,372,373 #binding_site phosphate (Ser) (covalent) (by protein !8kinase C) #status predicted SUMMARY #length 382 #molecular-weight 43008 #checksum 9008 SEQUENCE /// ENTRY A36623 #type complete TITLE gap junction protein Cx43 - bovine ALTERNATE_NAMES connexin 43; gap junction alpha-1 protein ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 28-Mar-1991 #sequence_revision 02-Jun-1994 #text_change 22-Jun-1999 ACCESSIONS A36623 REFERENCE A36623 !$#authors Lash, J.A.; Critser, E.S.; Pressler, M.L. !$#journal J. Biol. Chem. (1990) 265:13113-13117 !$#title Cloning of a gap junctional protein from vascular smooth !1muscle and expression in two-cell mouse embryos. !$#cross-references MUID:90330653; PMID:1695901 !$#accession A36623 !'##molecule_type mRNA !'##residues 1-383 ##label LAS !'##cross-references GB:J05535; NID:g162888; PIDN:AAA30459.1; !1PID:g162889 CLASSIFICATION #superfamily gap junction protein KEYWORDS gap junction; phosphoprotein; transmembrane protein FEATURE !$1-18 #domain intracellular #status predicted #label INT1\ !$19-41 #domain transmembrane #status predicted #label TM1\ !$42-76 #domain extracellular #status predicted #label EE1\ !$77-98 #domain transmembrane #status predicted #label TM2\ !$99-154 #domain intracellular #status predicted #label INT2\ !$155-185 #domain transmembrane #status predicted #label TM3\ !$186-207 #domain extracellular #status predicted #label EE2\ !$208-230 #domain transmembrane #status predicted #label TM4\ !$231-383 #domain intracellular #status predicted #label INT3\ !$298,365,366,369, !$370,373,374 #binding_site phosphate (Ser) (covalent) (by protein !8kinase C) #status predicted SUMMARY #length 383 #molecular-weight 43187 #checksum 3782 SEQUENCE /// ENTRY A39802 #type complete TITLE gap junction protein Cx43 - mouse ALTERNATE_NAMES connexin 43; gap junction alpha-1 protein ORGANISM #formal_name Mus musculus #common_name house mouse DATE 20-Mar-1992 #sequence_revision 02-Jun-1994 #text_change 22-Jun-1999 ACCESSIONS A39802; S18110; A49769; S23110 REFERENCE A39802 !$#authors Beyer, E.C.; Steinberg, T.H. !$#journal J. Biol. Chem. (1991) 266:7971-7974 !$#title Evidence that the gap junction protein connexin-43 is the !1ATP-induced pore of mouse macrophages. !$#cross-references MUID:91217014; PMID:1708769 !$#accession A39802 !'##molecule_type mRNA !'##residues 1-382 ##label BEY !'##cross-references GB:M61896; NID:g192678; PIDN:AAA37444.1; !1PID:g192679 REFERENCE S18110 !$#authors Ruangvoravat, C.P.; Morgan, J.L.; Lo, C.W. !$#submission submitted to the EMBL Data Library, September 1991 !$#description Connexin 43 expression in the early mouse embryo: !1differential distribution in the embryonic and !1extraembryonic regions. !$#accession S18110 !'##molecule_type mRNA !'##residues 1-382 ##label RUA !'##cross-references EMBL:X61576; NID:g50509; PIDN:CAA43778.1; !1PID:g50510 REFERENCE A49769 !$#authors Nishi, M.; Kumar, N.M.; Gilula, N.B. !$#journal Dev. Biol. (1991) 146:117-130 !$#title Developmental regulation of gap junction gene expression !1during mouse embryonic development. !$#cross-references MUID:91285228; PMID:2060697 !$#accession A49769 !'##molecule_type mRNA !'##residues 1-319,'T',321-340,'N',342-382 ##label NIS !'##cross-references GB:M63801; NID:g191773; PIDN:AAA53027.1; !1PID:g567197 REFERENCE S23110 !$#authors Willecke, K. !$#submission submitted to the EMBL Data Library, October 1991 !$#accession S23110 !'##status preliminary !'##molecule_type DNA !'##residues 1-382 ##label WIL !'##cross-references EMBL:X62836; NID:g50522; PIDN:CAA44640.1; !1PID:g50523 CLASSIFICATION #superfamily gap junction protein KEYWORDS gap junction; phosphoprotein; transmembrane protein FEATURE !$1-18 #domain intracellular #status predicted #label INT1\ !$19-41 #domain transmembrane #status predicted #label TM1\ !$42-76 #domain extracellular #status predicted #label EE1\ !$77-98 #domain transmembrane #status predicted #label TM2\ !$99-153 #domain intracellular #status predicted #label INT2\ !$154-184 #domain transmembrane #status predicted #label TM3\ !$185-206 #domain extracellular #status predicted #label EE2\ !$207-229 #domain transmembrane #status predicted #label TM4\ !$230-382 #domain intracellular #status predicted #label INT3\ !$297,364,365,368, !$369,372,373 #binding_site phosphate (Ser) (covalent) (by protein !8kinase C) #status predicted SUMMARY #length 382 #molecular-weight 43004 #checksum 952 SEQUENCE /// ENTRY S00532 #type complete TITLE gap junction protein Cx43 - rat ALTERNATE_NAMES connexin 43; gap junction alpha-1 protein ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1989 #sequence_revision 02-Jun-1994 #text_change 22-Jun-1999 ACCESSIONS S00532 REFERENCE S00532 !$#authors Beyer, E.C.; Paul, D.L.; Goodenough, D.A. !$#journal J. Cell Biol. (1987) 105:2621-2629 !$#title Connexin43: a protein from rat heart homologous to a gap !1junction protein from liver. !$#cross-references MUID:88087396; PMID:2826492 !$#accession S00532 !'##molecule_type mRNA !'##residues 1-382 ##label BEY !'##cross-references EMBL:X06656; NID:g55978; PIDN:CAA29855.1; !1PID:g55979 CLASSIFICATION #superfamily gap junction protein KEYWORDS gap junction; phosphoprotein; transmembrane protein FEATURE !$1-18 #domain intracellular #status predicted #label INT1\ !$19-41 #domain transmembrane #status predicted #label TM1\ !$42-76 #domain extracellular #status predicted #label EE1\ !$77-98 #domain transmembrane #status predicted #label TM2\ !$99-153 #domain intracellular #status predicted #label INT2\ !$154-184 #domain transmembrane #status predicted #label TM3\ !$185-206 #domain extracellular #status predicted #label EE2\ !$207-229 #domain transmembrane #status predicted #label TM4\ !$230-382 #domain intracellular #status predicted #label INT3\ !$297,364,365,368, !$369,372,373 #binding_site phosphate (Ser) (covalent) (by protein !8kinase C) #status predicted SUMMARY #length 382 #molecular-weight 43031 #checksum 672 SEQUENCE /// ENTRY A34575 #type complete TITLE gap junction protein Cx43 - African clawed frog ALTERNATE_NAMES connexin 43; gap junction alpha-1 protein ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 22-Jun-1990 #sequence_revision 02-Jun-1994 #text_change 22-Jun-1999 ACCESSIONS A34575 REFERENCE A34575 !$#authors Gimlich, R.L.; Kumar, N.M.; Gilula, N.B. !$#journal J. Cell Biol. (1990) 110:597-605 !$#title Differential regulation of the levels of three gap junction !1mRNAs in Xenopus embryos. !$#cross-references MUID:90171034; PMID:2155241 !$#accession A34575 !'##molecule_type mRNA !'##residues 1-379 ##label GIM !'##cross-references GB:X17243; NID:g64498; PIDN:CAA35108.1; PID:g64499 CLASSIFICATION #superfamily gap junction protein KEYWORDS gap junction; phosphoprotein; transmembrane protein FEATURE !$1-18 #domain intracellular #status predicted #label INT1\ !$19-41 #domain transmembrane #status predicted #label TM1\ !$42-76 #domain extracellular #status predicted #label EE1\ !$77-98 #domain transmembrane #status predicted #label TM2\ !$99-153 #domain intracellular #status predicted #label INT2\ !$154-184 #domain transmembrane #status predicted #label TM3\ !$185-206 #domain extracellular #status predicted #label EE2\ !$207-229 #domain transmembrane #status predicted #label TM4\ !$230-379 #domain intracellular #status predicted #label INT3\ !$294,361,362,365, !$366,369,370 #binding_site phosphate (Ser) (covalent) (by protein !8kinase C) #status predicted SUMMARY #length 379 #molecular-weight 42961 #checksum 494 SEQUENCE /// ENTRY A40166 #type complete TITLE gap junction protein Cx38, embryonic - African clawed frog ALTERNATE_NAMES connexin 38 ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 24-Jul-1992 #sequence_revision 02-Jun-1994 #text_change 25-Oct-1996 ACCESSIONS A40166 REFERENCE A40166 !$#authors Ebihara, L.; Beyer, E.C.; Swenson, K.I.; Paul, D.L.; !1Goodenough, D.A. !$#journal Science (1989) 243:1194-1195 !$#title Cloning and expression of a Xenopus embryonic gap junction !1protein. !$#cross-references MUID:89162052; PMID:2466337 !$#accession A40166 !'##molecule_type mRNA !'##residues 1-334 ##label EBI !'##cross-references GB:J03091 CLASSIFICATION #superfamily gap junction protein KEYWORDS gap junction; phosphoprotein; transmembrane protein FEATURE !$1-23 #domain intracellular #status predicted #label INT1\ !$24-41 #domain transmembrane #status predicted #label TM1\ !$42-77 #domain extracellular #status predicted #label EE1\ !$78-97 #domain transmembrane #status predicted #label TM2\ !$98-139 #domain intracellular #status predicted #label INT2\ !$140-177 #domain transmembrane #status predicted #label TM3\ !$178-196 #domain extracellular #status predicted #label EE2\ !$197-223 #domain transmembrane #status predicted #label TM4\ !$224-334 #domain intracellular #status predicted #label INT3 SUMMARY #length 334 #molecular-weight 37840 #checksum 2497 SEQUENCE /// ENTRY B34575 #type complete TITLE gap junction protein Cx38 - African clawed frog ALTERNATE_NAMES connexin 38; gap junction alpha-2 protein ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 22-Jun-1990 #sequence_revision 02-Jun-1994 #text_change 22-Jun-1999 ACCESSIONS B34575 REFERENCE A34575 !$#authors Gimlich, R.L.; Kumar, N.M.; Gilula, N.B. !$#journal J. Cell Biol. (1990) 110:597-605 !$#title Differential regulation of the levels of three gap junction !1mRNAs in Xenopus embryos. !$#cross-references MUID:90171034; PMID:2155241 !$#accession B34575 !'##molecule_type mRNA !'##residues 1-334 ##label GIM !'##cross-references GB:X17242; NID:g64503; PIDN:CAA35107.1; PID:g64504 CLASSIFICATION #superfamily gap junction protein KEYWORDS gap junction; phosphoprotein; transmembrane protein FEATURE !$1-23 #domain intracellular #status predicted #label INT1\ !$24-41 #domain transmembrane #status predicted #label TM1\ !$42-77 #domain extracellular #status predicted #label EE1\ !$78-97 #domain transmembrane #status predicted #label TM2\ !$98-139 #domain intracellular #status predicted #label INT2\ !$140-177 #domain transmembrane #status predicted #label TM3\ !$178-196 #domain extracellular #status predicted #label EE2\ !$197-223 #domain transmembrane #status predicted #label TM4\ !$224-334 #domain intracellular #status predicted #label INT3 SUMMARY #length 334 #molecular-weight 37832 #checksum 2629 SEQUENCE /// ENTRY A40548 #type complete TITLE gap junction protein Cx37 - mouse ALTERNATE_NAMES connexin 37; Cx37.6 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 17-Jul-1992 #sequence_revision 02-Jun-1994 #text_change 22-Jun-1999 ACCESSIONS A40548; S43973; S18831 REFERENCE A40548 !$#authors Willecke, K.; Heynkes, R.; Dahl, E.; Stutenkemper, R.; !1Hennemann, H.; Jungbluth, S.; Suchyna, T.; Nicholson, B.J. !$#journal J. Cell Biol. (1991) 114:1049-1057 !$#title Mouse connexin37: cloning and functional expression of a gap !1junction gene highly expressed in lung. !$#cross-references MUID:91340829; PMID:1651942 !$#accession A40548 !'##molecule_type mRNA !'##residues 1-333 ##label WIL !'##cross-references GB:X57971; NID:g50511; PIDN:CAA41037.1; PID:g50512 REFERENCE S43971 !$#authors Mandelboim, O.; Berke, G.; Fridkin, M.; Feldman, M.; !1Eisenstein, M.; Eisenbach, L. !$#journal Nature (1994) 369:67-71 !$#title CTL induction by a tumour-associated antigen octapeptide !1derived from a murine lung carcinoma. !$#cross-references MUID:94217811; PMID:8164742 !$#accession S43973 !'##status preliminary !'##molecule_type protein !'##residues 52-59 ##label MAN GENETICS !$#introns #status absent CLASSIFICATION #superfamily gap junction protein KEYWORDS gap junction; phosphoprotein; transmembrane protein FEATURE !$1-23 #domain intracellular #status predicted #label INT1\ !$24-41 #domain transmembrane #status predicted #label TM1\ !$42-77 #domain extracellular #status predicted #label EE1\ !$78-97 #domain transmembrane #status predicted #label TM2\ !$98-150 #domain intracellular #status predicted #label INT2\ !$151-187 #domain transmembrane #status predicted #label TM3\ !$188-207 #domain extracellular #status predicted #label EE2\ !$208-234 #domain transmembrane #status predicted #label TM4\ !$235-333 #domain intracellular #status predicted #label INT3 SUMMARY #length 333 #molecular-weight 37596 #checksum 7433 SEQUENCE /// ENTRY B42053 #type complete TITLE gap junction protein CX37 - rat ALTERNATE_NAMES connexin 37 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 04-Mar-1993 #sequence_revision 02-Jun-1994 #text_change 22-Jun-1999 ACCESSIONS B42053 REFERENCE A42053 !$#authors Haefliger, J.A.; Bruzzone, R.; Jenkins, N.A.; Gilbert, D.J.; !1Copeland, N.G.; Paul, D.L. !$#journal J. Biol. Chem. (1992) 267:2057-2064 !$#title Four novel members of the connexin family of gap junction !1proteins. Molecular cloning, expression, and chromosome !1mapping. !$#cross-references MUID:92112940; PMID:1370487 !$#accession B42053 !'##molecule_type DNA !'##residues 1-333 ##label HAE !'##cross-references GB:M76532; NID:g203665; PIDN:AAA40999.1; !1PID:g203666 !'##note sequence extracted from NCBI backbone (NCBIP:76096) CLASSIFICATION #superfamily gap junction protein KEYWORDS gap junction; phosphoprotein; transmembrane protein FEATURE !$1-23 #domain intracellular #status predicted #label INT1\ !$24-41 #domain transmembrane #status predicted #label TM1\ !$42-77 #domain extracellular #status predicted #label EE1\ !$78-97 #domain transmembrane #status predicted #label TM2\ !$98-150 #domain intracellular #status predicted #label INT2\ !$151-187 #domain transmembrane #status predicted #label TM3\ !$188-207 #domain extracellular #status predicted #label EE2\ !$208-234 #domain transmembrane #status predicted #label TM4\ !$234-333 #domain intracellular #status predicted #label INT3 SUMMARY #length 333 #molecular-weight 37556 #checksum 7191 SEQUENCE /// ENTRY C42053 #type complete TITLE gap junction protein Cx33 - rat ALTERNATE_NAMES connexin 33 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 04-Mar-1993 #sequence_revision 02-Jun-1994 #text_change 22-Jun-1999 ACCESSIONS C42053 REFERENCE A42053 !$#authors Haefliger, J.A.; Bruzzone, R.; Jenkins, N.A.; Gilbert, D.J.; !1Copeland, N.G.; Paul, D.L. !$#journal J. Biol. Chem. (1992) 267:2057-2064 !$#title Four novel members of the connexin family of gap junction !1proteins. Molecular cloning, expression, and chromosome !1mapping. !$#cross-references MUID:92112940; PMID:1370487 !$#accession C42053 !'##molecule_type DNA !'##residues 1-286 ##label HAE !'##cross-references GB:M76534; NID:g203663; PIDN:AAA40998.1; !1PID:g203664 !'##note sequence extracted from NCBI backbone (NCBIP:76095) CLASSIFICATION #superfamily gap junction protein KEYWORDS gap junction; phosphoprotein; transmembrane protein FEATURE !$1-23 #domain intracellular #status predicted #label INT1\ !$24-41 #domain transmembrane #status predicted #label TM1\ !$42-77 #domain extracellular #status predicted #label EE1\ !$78-97 #domain transmembrane #status predicted #label TM2\ !$98-150 #domain intracellular #status predicted #label INT2\ !$151-187 #domain transmembrane #status predicted #label TM3\ !$188-207 #domain extracellular #status predicted #label EE2\ !$208-234 #domain transmembrane #status predicted #label TM4\ !$235-286 #domain intracellular #status predicted #label INT3 SUMMARY #length 286 #molecular-weight 32860 #checksum 5511 SEQUENCE /// ENTRY A42053 #type complete TITLE gap junction protein Cx40 - rat ALTERNATE_NAMES connexin 40 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 04-Mar-1993 #sequence_revision 02-Jun-1994 #text_change 22-Jun-1999 ACCESSIONS A42053 REFERENCE A42053 !$#authors Haefliger, J.A.; Bruzzone, R.; Jenkins, N.A.; Gilbert, D.J.; !1Copeland, N.G.; Paul, D.L. !$#journal J. Biol. Chem. (1992) 267:2057-2064 !$#title Four novel members of the connexin family of gap junction !1proteins. Molecular cloning, expression, and chromosome !1mapping. !$#cross-references MUID:92112940; PMID:1370487 !$#accession A42053 !'##molecule_type DNA !'##residues 1-356 ##label HAE !'##cross-references GB:M76535; NID:g203667; PIDN:AAA41000.1; !1PID:g203668 !'##note sequence extracted from NCBI backbone (NCBIP:76097) CLASSIFICATION #superfamily gap junction protein KEYWORDS gap junction; phosphoprotein; transmembrane protein FEATURE !$1-23 #domain intracellular #status predicted #label INT1\ !$24-41 #domain transmembrane #status predicted #label TM1\ !$42-77 #domain extracellular #status predicted #label EE1\ !$78-97 #domain transmembrane #status predicted #label TM2\ !$98-148 #domain intracellular #status predicted #label INT2\ !$149-185 #domain transmembrane #status predicted #label TM3\ !$186-205 #domain extracellular #status predicted #label EE2\ !$206-232 #domain transmembrane #status predicted #label TM4\ !$233-356 #domain intracellular #status predicted #label INT3 SUMMARY #length 356 #molecular-weight 40233 #checksum 5366 SEQUENCE /// ENTRY B43433 #type complete TITLE gap junction protein Cx31.1 - mouse ALTERNATE_NAMES connexin 31.1 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 04-Mar-1993 #sequence_revision 02-Jun-1994 #text_change 24-Sep-1999 ACCESSIONS B43433 REFERENCE A43433 !$#authors Hennemann, H.; Dahl, E.; White, J.B.; Schwarz, H.J.; Lalley, !1P.A.; Chang, S.; Nicholson, B.J.; Willecke, K. !$#journal J. Biol. Chem. (1992) 267:17225-17233 !$#title Two gap junction genes, connexin 31.1 and 30.3, are closely !1linked on mouse chromosome 4 and preferentially expressed in !1skin. !$#cross-references MUID:92381038; PMID:1512260 !$#accession B43433 !'##molecule_type DNA !'##residues 1-271 ##label HEN !'##cross-references GB:M91236; NID:g192642; PIDN:AAA37426.1; !1PID:g192643 !'##note sequence extracted from NCBI backbone (NCBIN:111979, !1NCBIP:111980) CLASSIFICATION #superfamily gap junction protein KEYWORDS gap junction; phosphoprotein; transmembrane protein FEATURE !$1-20 #domain intracellular #status predicted #label INT1\ !$21-40 #domain transmembrane #status predicted #label TM1\ !$41-73 #domain extracellular #status predicted #label EE1\ !$74-96 #domain transmembrane #status predicted #label TM2\ !$97-122 #domain intracellular #status predicted #label INT2\ !$123-159 #domain transmembrane #status predicted #label TM3\ !$160-184 #domain extracellular #status predicted #label EE2\ !$185-207 #domain transmembrane #status predicted #label TM4\ !$208-271 #domain intracellular #status predicted #label INT3 SUMMARY #length 271 #molecular-weight 31194 #checksum 9069 SEQUENCE /// ENTRY D42053 #type complete TITLE gap junction protein Cx31.1 - rat ALTERNATE_NAMES connexin 33.1 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 03-Feb-1994 #sequence_revision 02-Jun-1994 #text_change 22-Jun-1999 ACCESSIONS D42053 REFERENCE A42053 !$#authors Haefliger, J.A.; Bruzzone, R.; Jenkins, N.A.; Gilbert, D.J.; !1Copeland, N.G.; Paul, D.L. !$#journal J. Biol. Chem. (1992) 267:2057-2064 !$#title Four novel members of the connexin family of gap junction !1proteins. Molecular cloning, expression, and chromosome !1mapping. !$#cross-references MUID:92112940; PMID:1370487 !$#accession D42053 !'##molecule_type DNA !'##residues 1-271 ##label HAE !'##cross-references GB:M76533; NID:g203661; PIDN:AAB38538.1; !1PID:g203662 !'##note sequence extracted from NCBI backbone (NCBIP:76094) GENETICS !$#gene CXN-31.1 CLASSIFICATION #superfamily gap junction protein KEYWORDS calcium; gap junction; liver; phosphoprotein; transmembrane !1protein FEATURE !$1-20 #domain intracellular #status predicted #label INT1\ !$21-40 #domain transmembrane #status predicted #label TM1\ !$41-73 #domain extracellular #status predicted #label EE1\ !$74-96 #domain transmembrane #status predicted #label TM2\ !$97-122 #domain intracellular #status predicted #label INT2\ !$123-159 #domain transmembrane #status predicted #label TM3\ !$160-184 #domain extracellular #status predicted #label EE2\ !$185-207 #domain transmembrane #status predicted #label TM4\ !$208-271 #domain intracellular #status predicted #label INT3 SUMMARY #length 271 #molecular-weight 31046 #checksum 654 SEQUENCE /// ENTRY A43433 #type complete TITLE gap junction protein Cx30.3 - mouse ALTERNATE_NAMES connexin 30.3 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1993 #sequence_revision 02-Jun-1994 #text_change 22-Jun-1999 ACCESSIONS A43433 REFERENCE A43433 !$#authors Hennemann, H.; Dahl, E.; White, J.B.; Schwarz, H.J.; Lalley, !1P.A.; Chang, S.; Nicholson, B.J.; Willecke, K. !$#journal J. Biol. Chem. (1992) 267:17225-17233 !$#title Two gap junction genes, connexin 31.1 and 30.3, are closely !1linked on mouse chromosome 4 and preferentially expressed in !1skin. !$#cross-references MUID:92381038; PMID:1512260 !$#accession A43433 !'##molecule_type DNA !'##residues 1-266 ##label HEN !'##cross-references GB:M91443; NID:g192646; PIDN:AAA37428.1; !1PID:g192647 !'##note sequence extracted from NCBI backbone (NCBIN:111981, !1NCBIP:111982) CLASSIFICATION #superfamily gap junction protein KEYWORDS gap junction; phosphoprotein; transmembrane protein FEATURE !$1-20 #domain intracellular #status predicted #label INT1\ !$21-40 #domain transmembrane #status predicted #label TM1\ !$41-73 #domain extracellular #status predicted #label EE1\ !$74-96 #domain transmembrane #status predicted #label TM2\ !$97-122 #domain intracellular #status predicted #label INT2\ !$123-159 #domain transmembrane #status predicted #label TM3\ !$160-184 #domain extracellular #status predicted #label EE2\ !$185-207 #domain transmembrane #status predicted #label TM4\ !$208-266 #domain intracellular #status predicted #label INT3 SUMMARY #length 266 #molecular-weight 30388 #checksum 5530 SEQUENCE /// ENTRY A38737 #type complete TITLE gap junction protein Cx31 - rat ALTERNATE_NAMES connexin-31 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 13-Sep-1991 #sequence_revision 02-Jun-1994 #text_change 22-Jun-1999 ACCESSIONS A38737 REFERENCE A38737 !$#authors Hoh, J.H.; John, S.A.; Revel, J.P. !$#journal J. Biol. Chem. (1991) 266:6524-6531 !$#title Molecular cloning and characterization of a new member of !1the gap junction gene family, connexin-31. !$#cross-references MUID:91177912; PMID:1706719 !$#accession A38737 !'##molecule_type DNA !'##residues 1-270 ##label HOH !'##cross-references GB:M59936; NID:g203659; PIDN:AAA40997.1; !1PID:g203660 !'##note the authors translated the codon CAG for residue 7 as Gly and !1GAC for residue 8 as Asn CLASSIFICATION #superfamily gap junction protein KEYWORDS gap junction; phosphoprotein; placenta; transmembrane !1protein FEATURE !$1-20 #domain intracellular #status predicted #label INT1\ !$21-40 #domain transmembrane #status predicted #label TM1\ !$41-73 #domain extracellular #status predicted #label EE1\ !$74-96 #domain transmembrane #status predicted #label TM2\ !$97-122 #domain intracellular #status predicted #label INT2\ !$123-159 #domain transmembrane #status predicted #label TM3\ !$160-184 #domain extracellular #status predicted #label EE2\ !$185-207 #domain transmembrane #status predicted #label TM4\ !$208-270 #domain intracellular #status predicted #label INT3 SUMMARY #length 270 #molecular-weight 30969 #checksum 4845 SEQUENCE /// ENTRY A35955 #type complete TITLE meta-vinculin - human CONTAINS vinculin ORGANISM #formal_name Homo sapiens #common_name man DATE 09-Nov-1990 #sequence_revision 02-Aug-1996 #text_change 22-Jun-1999 ACCESSIONS A35955; S39760; S21180; S39758; S24424 REFERENCE A35955 !$#authors Weller, P.A.; Ogryzko, E.P.; Corben, E.B.; Zhidkova, N.I.; !1Patel, B.; Price, G.J.; Spurr, N.K.; Koteliansky, V.E.; !1Critchley, D.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:5667-5671 !$#title Complete sequence of human vinculin and assignment of the !1gene to chromosome 10. !$#cross-references MUID:90332642; PMID:2116004 !$#accession A35955 !'##molecule_type mRNA !'##residues 1-915,984-1134 ##label WEL !'##cross-references GB:M33308; NID:g340236; PIDN:AAA61283.1; !1PID:g340237 !'##note the authors translated the codon GAG for residue 60 as Gln REFERENCE S21180 !$#authors Koteliansky, V.E.; Ogryzko, E.P.; Zhidkova, N.I.; Weller, !1P.A.; Critchley, D.R.; Vancompernolle, K.; Vandekerckhove, !1J.; Strasser, P.; Way, M.; Gimona, M.; Small, J.V. !$#journal Eur. J. Biochem. (1992) 204:767-772 !$#title An additional exon in the human vinculin gene specifically !1encodes meta-vinculin-specific difference peptide. !1Cross-species comparison reveals variable and conserved !1motifs in the meta-vinculin insert. !$#cross-references MUID:92174935; PMID:1339348 !$#accession S39760 !'##status preliminary !'##molecule_type DNA !'##residues 854-1051 ##label KOT !'##cross-references GB:S87180; NID:g246706; PIDN:AAB21656.1; !1PID:g246707 !$#accession S21180 !'##molecule_type mRNA !'##residues 901-995 ##label KO3 !$#accession S39758 !'##status preliminary !'##molecule_type mRNA !'##residues 911-983 ##label KO2 !'##note meta-vinculin isoform is specific to muscle GENETICS !$#gene GDB:VCL !'##cross-references GDB:125348; OMIM:193065 !$#map_position 10q22.1-10q23 !$#introns 915/3; 983/3 CLASSIFICATION #superfamily meta-vinculin; vinculin amino-terminal !1homology; vinculin carboxyl-terminal homology KEYWORDS alternative splicing; cell adhesion; cytoskeleton; !1duplication; lipid binding; phosphoprotein FEATURE !$1-1134 #product meta-vinculin #status predicted #label MA1\ !$1-915,984-1134 #product vinculin #status predicted #label MAT\ !$4-257 #domain vinculin amino-terminal homology #label VINN\ !$167-207 #region talin binding\ !$259-589 #region 112-residue repeats\ !$581-1132 #domain vinculin carboxyl-terminal homology #label !8VINC\ !$837-878 #region proline-rich\ !$822 #binding_site phosphate (Tyr) (covalent) #status !8predicted SUMMARY #length 1134 #molecular-weight 123798 #checksum 5090 SEQUENCE /// ENTRY A29997 #type complete TITLE meta-vinculin - chicken CONTAINS vinculin ORGANISM #formal_name Gallus gallus #common_name chicken DATE 31-Dec-1988 #sequence_revision 02-Aug-1996 #text_change 22-Jun-1999 ACCESSIONS A31346; S03973; A27884; S39759; S32807; S65691; A29997 REFERENCE A31346 !$#authors Coutu, M.D.; Craig, S.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:8535-8539 !$#title cDNA-derived sequence of chicken embryo vinculin. !$#cross-references MUID:89042216; PMID:3141928 !$#accession A31346 !'##molecule_type mRNA !'##residues 1-915,985-1135 ##label COU !'##cross-references GB:J04126; NID:g212872; PIDN:AAA49136.1; !1PID:g212873 REFERENCE S03973 !$#authors Price, G.J.; Jones, P.; Davison, M.D.; Patel, B.; Bendori, !1R.; Geiger, B.; Critchley, D.R. !$#journal Biochem. J. (1989) 259:453-461 !$#title Primary sequence and domain structure of chicken vinculin. !$#cross-references MUID:89246350; PMID:2497736 !$#accession S03973 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-441,'QLSCQI',448-700,'H',702-915,985-1135 ##label PRI !'##note this sequence has been revised in reference A35955 REFERENCE A27884 !$#authors Price, G.J.; Jones, P.; Davison, M.D.; Patel, B.; Eperon, !1I.C.; Critchley, D.R. !$#journal Biochem. J. (1987) 245:595-603 !$#title Isolation and characterization of a vinculin cDNA from !1chick-embryo fibroblasts. !$#cross-references MUID:88024106; PMID:3117046 !$#accession A27884 !'##molecule_type mRNA !'##residues 1-441,'QLSCQI',448-700,'H',702-879,'K',881 ##label PR2 !'##note this sequence has been revised in reference A35955 REFERENCE A35955 !$#authors Weller, P.A.; Ogryzko, E.P.; Corben, E.B.; Zhidkova, N.I.; !1Patel, B.; Price, G.J.; Spurr, N.K.; Koteliansky, V.E.; !1Critchley, D.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:5667-5671 !$#title Complete sequence of human vinculin and assignment of the !1gene to chromosome 10. !$#cross-references MUID:90332642; PMID:2116004 !$#contents annotation; revisions to residues 442-447 REFERENCE S21180 !$#authors Koteliansky, V.E.; Ogryzko, E.P.; Zhidkova, N.I.; Weller, !1P.A.; Critchley, D.R.; Vancompernolle, K.; Vandekerckhove, !1J.; Strasser, P.; Way, M.; Gimona, M.; Small, J.V. !$#journal Eur. J. Biochem. (1992) 204:767-772 !$#title An additional exon in the human vinculin gene specifically !1encodes meta-vinculin-specific difference peptide. !1Cross-species comparison reveals variable and conserved !1motifs in the meta-vinculin insert. !$#cross-references MUID:92174935; PMID:1339348 !$#accession S39759 !'##molecule_type mRNA !'##residues 911-984 ##label KOT REFERENCE S32807 !$#authors Byrne, B.J.; Kaczorowski, Y.J.; Coutu, M.D.; Craig, S.W. !$#journal J. Biol. Chem. (1992) 267:12845-12850 !$#title Chicken vinculin and meta-vinculin are derived from a single !1gene by alternative splicing of a 207-base pair exon unique !1to meta-vinculin. !$#cross-references MUID:92316975; PMID:1618784 !$#accession S32807 !'##molecule_type DNA !'##residues 916-943,'S',945-984 ##label BYR !'##cross-references EMBL:M87837; NID:g212870; PIDN:AAA49135.1; !1PID:g212871 !$#accession S65691 !'##molecule_type mRNA !'##residues 916-943,'S',945-984 ##label BYX !'##cross-references EMBL:M87837; NID:g212870; PIDN:AAA49135.1; !1PID:g212871 !'##note meta-vinculin isoform is specific to muscle GENETICS !$#gene vinc1 !$#map_position 14 CLASSIFICATION #superfamily meta-vinculin; vinculin amino-terminal !1homology; vinculin carboxyl-terminal homology KEYWORDS alternative splicing; cell adhesion; cytoskeleton; !1duplication; lipid binding; phosphoprotein FEATURE !$1-1135 #product meta-vinculin #status predicted #label MAT\ !$1-915,985-1135 #product vinculin #status predicted #label MA2\ !$4-257 #domain vinculin amino-terminal homology #label VINN\ !$167-207 #region talin binding\ !$259-589 #region 112-residue repeats\ !$581-1133 #domain vinculin carboxyl-terminal homology #label !8VINC\ !$837-878 #region proline-rich\ !$822 #binding_site phosphate (Tyr) (covalent) #status !8predicted SUMMARY #length 1135 #molecular-weight 124569 #checksum 7285 SEQUENCE /// ENTRY JN0607 #type complete TITLE alpha-catenin 1 - human ALTERNATE_NAMES cadherin-associated 102K protein (CAP102) ORGANISM #formal_name Homo sapiens #common_name man DATE 17-Mar-2000 #sequence_revision 17-Mar-2000 #text_change 16-Jun-2000 ACCESSIONS JN0607; I39388; I39438 REFERENCE JN0607 !$#authors Oda, T.; Kanai, Y.; Shimoyama, Y.; Nagafuchi, A.; Tsukita, !1S.; Hirohashi, S. !$#journal Biochem. Biophys. Res. Commun. (1993) 193:897-904 !$#title Cloning of the human alpha-catenin cDNA and its aberrant !1mRNA in a human cancer cell line. !$#cross-references MUID:93312345; PMID:8323564 !$#accession JN0607 !'##molecule_type mRNA !'##residues 1-906 ##label ODA !'##cross-references GB:D13866; NID:g433410; PIDN:BAA02979.1; !1PID:g433411 REFERENCE I39388 !$#authors McPherson, J.D.; Morton, R.A.; Ewing, C.M.; Wasmuth, J.J.; !1Overhauser, J.; Nagafuchi, A.; Tsukita, S.; Isaacs, W.B. !$#journal Genomics (1994) 19:188-190 !$#title Assignment of the human alpha-catenin gene (CTNNA1) to !1chromosome 5q21-q22. !$#cross-references MUID:94245167; PMID:8188230 !$#accession I39388 !'##status preliminary !'##molecule_type mRNA !'##residues 159-250 ##label MCP !'##cross-references GB:L22080; NID:g347315; PIDN:AAA35502.1; !1PID:g347316 REFERENCE I39438 !$#authors Furukawa, Y.; Nakatsuru, S.; Nagafuchi, A.; Tsukita, S.; !1Muto, T.; Nakamura, Y.; Horii, A. !$#journal Cytogenet. Cell Genet. (1994) 65:74-78 !$#title Structure, expression and chromosome assignment of the human !1catenin (cadherin-associated protein) alpha 1 gene (CTNNA1). !$#cross-references MUID:94007995; PMID:8404069 !$#accession I39438 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-341,'K',343-788,'H',790-906 ##label FUR !'##cross-references GB:D14705; NID:g415305; PIDN:BAA03530.1; !1PID:g404105 COMMENT Alpha-catenin works as a connector which anchors the !1epithelial-cadherin to the cytoskeletal actin bundle through !1the cadherin cytoplasmic domain. GENETICS !$#gene GDB:CTNNA1 !'##cross-references GDB:141920; OMIM:116805 !$#map_position 5q31-5q31 CLASSIFICATION #superfamily alpha-catenin; vinculin amino-terminal !1homology; vinculin carboxyl-terminal homology KEYWORDS cytoskeleton FEATURE !$20-268 #domain vinculin amino-terminal homology #label VINN\ !$376-859 #domain vinculin carboxyl-terminal homology #label !8VINC SUMMARY #length 906 #molecular-weight 100070 #checksum 5940 SEQUENCE /// ENTRY A45011 #type complete TITLE alpha-catenin 2 - human ALTERNATE_NAMES alpha catenin-related protein; cadherin-associated protein alpha; CAP-R protein; vinculin homolog ORGANISM #formal_name Homo sapiens #common_name man DATE 17-Mar-2000 #sequence_revision 17-Mar-2000 #text_change 17-Mar-2000 ACCESSIONS A45011 REFERENCE A45011 !$#authors Claverie, J.M.; Hardelin, J.P.; Legouis, R.; Levilliers, J.; !1Bougueleret, L.; Mattei, M.G.; Petit, C. !$#journal Genomics (1993) 15:13-20 !$#title Characterization and chromosomal assignment of a human cDNA !1encoding a protein related to the murine 102-kDa !1cadherin-associated protein (alpha-catenin). !$#cross-references MUID:93162640; PMID:8432524 !$#accession A45011 !'##molecule_type mRNA !'##residues 1-945 ##label CLA !'##cross-references GB:M94151; NID:g179923; PIDN:AAA58407.1; !1PID:g179925 !'##experimental_source fetal brain !'##note sequence extracted from NCBI backbone (NCBIP:124896) GENETICS !$#gene GDB:CTNNA2; CAP-R !'##cross-references GDB:137725; OMIM:114025 !$#map_position 2p12-2p11.1 CLASSIFICATION #superfamily alpha-catenin; vinculin amino-terminal !1homology; vinculin carboxyl-terminal homology KEYWORDS cytoskeleton FEATURE !$19-267 #domain vinculin amino-terminal homology #label VINN\ !$374-906 #domain vinculin carboxyl-terminal homology #label !8VINC SUMMARY #length 945 #molecular-weight 104397 #checksum 9950 SEQUENCE /// ENTRY SJHUA #type complete TITLE spectrin alpha chain - human ORGANISM #formal_name Homo sapiens #common_name man DATE 17-May-1985 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS A35716; A45755; A23533; A91528; A42872; A02965; S13138; !1A05282; A23965; A27016 REFERENCE A35716 !$#authors Sahr, K.E.; Laurila, P.; Kotula, L.; Scarpa, A.L.; Coupal, !1E.; Leto, T.L.; Linnenbach, A.J.; Winkelmann, J.C.; !1Speicher, D.W.; Marchesi, V.T.; Curtis, P.J.; Forget, B.G. !$#journal J. Biol. Chem. (1990) 265:4434-4443 !$#title The complete cDNA and polypeptide sequences of human !1erythroid alpha-spectrin. !$#cross-references MUID:90170949; PMID:1689726 !$#accession A35716 !'##molecule_type mRNA !'##residues 1-2429 ##label SAH !'##cross-references GB:J05244 REFERENCE A45755 !$#authors Sahr, K.E.; Tobe, T.; Scarpa, A.; Laughinghouse, K.; !1Marchesi, S.L.; Agre, P.; Linnenbach, A.J.; Marchesi, V.T.; !1Forget, B.G. !$#journal J. Clin. Invest. (1989) 84:1243-1252 !$#title Sequence and exon-intron organization of the DNA encoding !1the alphaI domain of human spectrin. Application to the !1study of mutations causing hereditary elliptocytosis. !$#cross-references MUID:90009318; PMID:2794061 !$#accession A45755 !'##molecule_type DNA !'##residues 1-394,'G',396-533 ##label SA2 !'##cross-references GB:M29983 !'##note the authors translated the codon GGT for residue 395 as Ala REFERENCE A23533 !$#authors Linnenbach, A.J.; Speicher, D.W.; Marchesi, V.T.; Forget, !1B.G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:2397-2401 !$#title Cloning of a portion of the chromosomal gene for human !1erythrocyte alpha-spectrin by using a synthetic gene !1fragment. !$#cross-references MUID:86205962; PMID:3458204 !$#accession A23533 !'##molecule_type DNA !'##residues 320-450 ##label LIN !'##cross-references GB:M13233; NID:g182242; PIDN:AAA53103.1; !1PID:g182243 REFERENCE A91528 !$#authors Curtis, P.J.; Palumbo, A.; Ming, J.; Fraser, P.; Cioe, L.; !1Meo, P.; Shane, S.; Rovera, G. !$#journal Gene (1985) 36:357-362 !$#title Sequence comparison of human and murine erythrocyte !1alpha-spectrin cDNA. !$#cross-references MUID:86083178; PMID:3000887 !$#accession A91528 !'##molecule_type mRNA !'##residues 1451-1687 ##label CUR !'##cross-references GB:M11049; NID:g338310; PIDN:AAA60569.1; !1PID:g553648 REFERENCE A42872 !$#authors Speicher, D.W.; Weglarz, L.; DeSilva, T.M. !$#journal J. Biol. Chem. (1992) 267:14775-14782 !$#title Properties of human red cell spectrin heterodimer !1(side-to-side) assembly and identification of an essential !1nucleation site. !$#cross-references MUID:92340516; PMID:1634521 !$#accession A42872 !'##molecule_type protein !'##residues 7-16;46-55;680-689;1047-1056;1921-1930 ##label SPI REFERENCE A92408 !$#authors Speicher, D.W.; Davis, G.; Marchesi, V.T. !$#journal J. Biol. Chem. (1983) 258:14938-14947 !$#title Structure of human erythrocyte spectrin. II. The sequence of !1the alpha-I domain. !$#cross-references MUID:84087888; PMID:6654896 !$#accession A02965 !'##molecule_type protein !'##residues 7-601 ##label SPC REFERENCE S13138 !$#authors Speicher, D.W.; Davis, G.; Yurchenco, P.D.; Marchesi, V.T. !$#journal J. Biol. Chem. (1983) 258:14931-14937 !$#title Structure of human erythrocyte spectrin. I. Isolation of the !1alpha-I domain and its cyanogen bromide peptides. !$#cross-references MUID:84087887; PMID:6654895 !$#accession S13138 !'##molecule_type protein !'##residues 7-92,'X',94-96,110-151;317-342;345-366,'Z',368-370,'X', !1372-373;387-434;452-457,'X',459-464,'X',466;493-523 ##label !1SPE REFERENCE A38928 !$#authors Lusitani, D.M.; Qtaishat, N.; LaBrake, C.C.; Yu, R.N.; !1Davis, J.; Kelley, M.R.; Fung, L.W.M. !$#journal J. Biol. Chem. (1994) 269:25955-25958 !$#title The first human alpha-spectrin structural domain begins with !1serine. !$#cross-references MUID:95014412; PMID:7929303 !$#contents annotation; determination of structural domain COMMENT Spectrin associates with band 4.1 and actin to form the !1cytoskeletal superstructure of the erythrocyte plasma !1membrane. The alpha and beta chains contain different !1numbers of tandem repeats of approximately 106 residues !1each. GENETICS !$#gene GDB:SPTA1 !'##cross-references GDB:119601; OMIM:182860 !$#map_position 1q21-1q21 CLASSIFICATION #superfamily spectrin alpha chain; calmodulin repeat !1homology; SH3 homology; spectrin/dystrophin repeat homology KEYWORDS actin binding; cytoskeleton; duplication; EF hand; !1erythrocyte; heterodimer; membrane protein FEATURE !$52-156 #domain spectrin/dystrophin repeat homology #label !8SP1\ !$157-262 #domain spectrin/dystrophin repeat homology #label !8SP2\ !$263-368 #domain spectrin/dystrophin repeat homology #label !8SP3\ !$369-474 #domain spectrin/dystrophin repeat homology #label !8SP4\ !$475-580 #domain spectrin/dystrophin repeat homology #label !8SP5\ !$581-685 #domain spectrin/dystrophin repeat homology #label !8SP6\ !$686-791 #domain spectrin/dystrophin repeat homology #label !8SP7\ !$792-897 #domain spectrin/dystrophin repeat homology #label !8SP8\ !$898-983 #domain spectrin/dystrophin repeat homology #status !8atypical #label SP9\ !$984-1031 #domain SH3 homology #label SH3\ !$1081-1181 #domain spectrin/dystrophin repeat homology #label !8SP10\ !$1182-1287 #domain spectrin/dystrophin repeat homology #label !8SP11\ !$1288-1393 #domain spectrin/dystrophin repeat homology #label !8SP12\ !$1394-1498 #domain spectrin/dystrophin repeat homology #label !8SP13\ !$1499-1604 #domain spectrin/dystrophin repeat homology #label !8SP14\ !$1605-1710 #domain spectrin/dystrophin repeat homology #label !8SP15\ !$1711-1816 #domain spectrin/dystrophin repeat homology #label !8SP16\ !$1817-1925 #domain spectrin/dystrophin repeat homology #label !8SP17\ !$1926-2032 #domain spectrin/dystrophin repeat homology #label !8SP18\ !$2041-2146 #domain spectrin/dystrophin repeat homology #label !8SP19\ !$2155-2257 #domain spectrin/dystrophin repeat homology #label !8SP20\ !$2270-2302 #domain calmodulin repeat homology #label EF1\ !$2313-2345 #domain calmodulin repeat homology #label EF2 SUMMARY #length 2429 #molecular-weight 281055 #checksum 8282 SEQUENCE /// ENTRY SJCHA #type complete TITLE spectrin alpha chain, brain - chicken ALTERNATE_NAMES calspectin alpha chain; fodrin alpha chain ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 01-Aug-1997 ACCESSIONS A30122; A31866; A22723; S02425; S03190 REFERENCE A30122 !$#authors Wasenius, V.M.; Saraste, M.; Salven, P.; Eraemaa, M.; Holm, !1L.; Lehto, V.P. !$#journal J. Cell Biol. (1989) 108:1177-1178 !$#contents erratum !$#accession A30122 !'##molecule_type mRNA !'##residues 1-2477 ##label WAS !'##cross-references GB:X14519 REFERENCE A31866 !$#authors Wasenius, V.M.; Saraste, M.; Salven, P.; Eraemaa, M.; Holm, !1L.; Lehto, V.P. !$#journal J. Cell Biol. (1989) 108:79-93 !$#title Primary structure of the brain alpha-spectrin. !$#cross-references MUID:89093238; PMID:2910879 !$#accession A31866 !'##molecule_type mRNA !'##residues 1-2477 ##label WA2 !'##cross-references EMBL:X13701 !'##note residues 1880-2359 are shown between residues 1399 and 1400 in !1Fig. 2 CLASSIFICATION #superfamily spectrin alpha chain; calmodulin repeat !1homology; SH3 homology; spectrin/dystrophin repeat homology KEYWORDS actin binding; calcium binding; cytoskeleton; duplication; !1EF hand; heterodimer FEATURE !$43-147 #domain spectrin/dystrophin repeat homology #label !8SP1\ !$148-253 #domain spectrin/dystrophin repeat homology #label !8SP2\ !$254-359 #domain spectrin/dystrophin repeat homology #label !8SP3\ !$360-465 #domain spectrin/dystrophin repeat homology #label !8SP4\ !$466-571 #domain spectrin/dystrophin repeat homology #label !8SP5\ !$572-676 #domain spectrin/dystrophin repeat homology #label !8SP6\ !$677-782 #domain spectrin/dystrophin repeat homology #label !8SP7\ !$783-888 #domain spectrin/dystrophin repeat homology #label !8SP8\ !$889-973 #domain spectrin/dystrophin repeat homology #status !8atypical #label SP9\ !$974-1021 #domain SH3 homology #label SH3\ !$1090-1231 #domain spectrin/dystrophin repeat homology #status !8atypical #label SP10\ !$1232-1337 #domain spectrin/dystrophin repeat homology #label !8SP11\ !$1338-1443 #domain spectrin/dystrophin repeat homology #label !8SP12\ !$1444-1549 #domain spectrin/dystrophin repeat homology #label !8SP13\ !$1550-1661 #domain spectrin/dystrophin repeat homology #label !8SP14\ !$1662-1767 #domain spectrin/dystrophin repeat homology #label !8SP15\ !$1768-1873 #domain spectrin/dystrophin repeat homology #label !8SP16\ !$1874-1979 #domain spectrin/dystrophin repeat homology #label !8SP17\ !$1980-2086 #domain spectrin/dystrophin repeat homology #label !8SP18\ !$2095-2200 #domain spectrin/dystrophin repeat homology #label !8SP19\ !$2209-2315 #domain spectrin/dystrophin repeat homology #label !8SP20\ !$2328-2360 #domain calmodulin repeat homology #label EF1\ !$2371-2403 #domain calmodulin repeat homology #label EF2 SUMMARY #length 2477 #molecular-weight 285361 #checksum 4744 SEQUENCE /// ENTRY A33733 #type complete TITLE spectrin alpha chain - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jun-2002 ACCESSIONS A33733; A49468; B49468 REFERENCE A33733 !$#authors Dubreuil, R.R.; Byers, T.J.; Sillman, A.L.; Bar-Zvi, D.; !1Goldstein, L.S.B.; Branton, D. !$#journal J. Cell Biol. (1989) 109:2197-2205 !$#title The complete sequence of Drosophila alpha-spectrin: !1conservation of structural domains between alpha-spectrins !1and alpha-actinin. !$#cross-references MUID:90037215; PMID:2808524 !$#accession A33733 !'##status preliminary !'##molecule_type mRNA !'##residues 1-2415 ##label DUB !'##cross-references GB:M26400; NID:g158488; PIDN:AAA28907.1; !1PID:g158489 REFERENCE A49468 !$#authors Lee, J.K.; Coyne, R.S.; Dubreuil, R.R.; Goldstein, L.S.; !1Branton, D. !$#journal J. Cell Biol. (1993) 123:1797-1809 !$#title Cell shape and interaction defects in alpha-spectrin mutants !1of Drosophila melanogaster. !$#cross-references MUID:94103334; PMID:8276898 !$#accession A49468 !'##status preliminary !'##molecule_type DNA !'##residues 1-150 ##label LEE !'##cross-references GB:S67765; NID:g544666; PIDN:AAB29441.1; !1PID:g544667 !'##note sequence extracted from NCBI backbone (NCBIN:141786, !1NCBIN:141790, NCBIP:141792) !$#accession B49468 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 2192-2415 ##label LE2 !'##cross-references GB:S67765; NID:g544666; PIDN:AAB29442.1; !1PID:g544668 !'##note sequence extracted from NCBI backbone (NCBIP:141794) GENETICS !$#gene FlyBase:alpha-Spec !'##cross-references FlyBase:FBgn0003470 CLASSIFICATION #superfamily spectrin alpha chain; calmodulin repeat !1homology; SH3 homology; spectrin/dystrophin repeat homology KEYWORDS actin binding; cytoskeleton; EF hand FEATURE !$46-150 #domain spectrin/dystrophin repeat homology #label !8SP1\ !$151-256 #domain spectrin/dystrophin repeat homology #label !8SP2\ !$257-362 #domain spectrin/dystrophin repeat homology #label !8SP3\ !$363-468 #domain spectrin/dystrophin repeat homology #label !8SP4\ !$469-574 #domain spectrin/dystrophin repeat homology #label !8SP5\ !$575-679 #domain spectrin/dystrophin repeat homology #label !8SP6\ !$680-785 #domain spectrin/dystrophin repeat homology #label !8SP7\ !$786-891 #domain spectrin/dystrophin repeat homology #label !8SP8\ !$892-976 #domain spectrin/dystrophin repeat homology #status !8atypical #label SP9\ !$977-1024 #domain SH3 homology #label SH3\ !$1072-1179 #domain spectrin/dystrophin repeat homology #label !8SP10\ !$1180-1285 #domain spectrin/dystrophin repeat homology #label !8SP11\ !$1286-1391 #domain spectrin/dystrophin repeat homology #label !8SP12\ !$1392-1497 #domain spectrin/dystrophin repeat homology #label !8SP13\ !$1498-1604 #domain spectrin/dystrophin repeat homology #label !8SP14\ !$1605-1710 #domain spectrin/dystrophin repeat homology #label !8SP15\ !$1711-1816 #domain spectrin/dystrophin repeat homology #label !8SP16\ !$1817-1922 #domain spectrin/dystrophin repeat homology #label !8SP17\ !$1923-2029 #domain spectrin/dystrophin repeat homology #label !8SP18\ !$2038-2143 #domain spectrin/dystrophin repeat homology #label !8SP19\ !$2152-2252 #domain spectrin/dystrophin repeat homology #label !8SP20\ !$2265-2297 #domain calmodulin repeat homology #label EF1\ !$2308-2340 #domain calmodulin repeat homology #label EF2 SUMMARY #length 2415 #molecular-weight 278329 #checksum 1002 SEQUENCE /// ENTRY SJHUB #type complete TITLE spectrin beta chain - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS A37064; A39346; JT0554; A28777; A39885; B23659; B42872; !1B27016; A32514 REFERENCE A37064 !$#authors Winkelmann, J.C.; Chang, J.G.; Tse, W.T.; Scarpa, A.L.; !1Marchesi, V.T.; Forget, B.G. !$#journal J. Biol. Chem. (1990) 265:11827-11832 !$#title Full-length sequence of the cDNA for human erythroid !1beta-spectrin. !$#cross-references MUID:90307707; PMID:2195026 !$#accession A37064 !'##molecule_type mRNA !'##residues 1-2137 ##label WIN !'##cross-references GB:J05500 !'##note the authors translated the codon GAG for residue 596 as Arg, !1CAC for residue 801 as Lys, CAG for residue 1704 as Lys, and !1AGC for residue 1910 as Glu REFERENCE A39346 !$#authors Gallagher, P.G.; Tse, W.T.; Costa, F.; Scarpa, A.; Boivin, !1P.; Delaunay, J.; Forget, B.G. !$#journal J. Biol. Chem. (1991) 266:15154-15159 !$#title A splice site mutation of the beta-spectrin gene causing !1exon skipping in hereditary elliptocytosis associated with a !1truncated beta-spectrin chain. !$#cross-references MUID:91332035; PMID:1840591 !$#accession A39346 !'##molecule_type DNA !'##residues 2002-2137 ##label GAL !'##cross-references GB:J05500 REFERENCE JT0554 !$#authors Yoon, S.H.; Kentros, C.G.; Prchal, J.T. !$#journal Gene (1990) 91:297-302 !$#title Identification of an unusual deletion within homologous !1repeats of human reticulocyte beta-spectrin and probable !1peptide polymorphism. !$#cross-references MUID:91007291; PMID:1976574 !$#accession JT0554 !'##molecule_type mRNA !'##residues 928-957,'NY',960-982,'L',984-1030,'D',1032-1755 ##label YOO !'##cross-references GB:M57948 REFERENCE A90733 !$#authors Winkelmann, J.C.; Leto, T.L.; Watkins, P.C.; Eddy, R.; !1Shows, T.B.; Linnenbach, A.J.; Sahr, K.E.; Kathuria, N.; !1Marchesi, V.T.; Forget, B.G. !$#journal Blood (1988) 72:328-334 !$#title Molecular cloning of the cDNA for human erythrocyte !1beta-spectrin. !$#cross-references MUID:88269838; PMID:3390609 !$#accession A28777 !'##molecule_type mRNA !'##residues 1334-1373,'R',1375-1432;1909-2137 ##label WI2 !'##cross-references GB:J05500 !'##note authors Yoon et al. show His to be the predominant residue at !1position 1374 and Arg to be a minor allelic form or in error REFERENCE A39885 !$#authors Prchal, J.T.; Morley, B.J.; Yoon, S.H.; Coetzer, T.L.; !1Palek, J.; Conboy, J.G.; Kan, Y.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:7468-7472 !$#title Isolation and characterization of cDNA clones for human !1erythrocyte beta-spectrin. !$#cross-references MUID:88041127; PMID:3478706 !$#accession A39885 !'##molecule_type mRNA !'##residues 1209-1482 ##label PRC !'##cross-references GB:M18054; NID:g338333; PIDN:AAA60572.1; !1PID:g338334 !'##experimental_source reticulocyte REFERENCE A23659 !$#authors Winkelmann, J.C.; Costa, F.F.; Linzie, B.L.; Forget, B.G. !$#journal J. Biol. Chem. (1990) 265:20449-20454 !$#title Beta spectrin in human skeletal muscle. Tissue-specific !1differential processing of 3' beta spectrin pre-mRNA !1generates a beta spectrin isoform with a unique carboxyl !1terminus. !$#cross-references MUID:91056094; PMID:2243099 !$#accession B23659 !'##molecule_type mRNA !'##residues 2105-2137 ##label WI3 !'##cross-references GB:M37885 REFERENCE A42872 !$#authors Speicher, D.W.; Weglarz, L.; DeSilva, T.M. !$#journal J. Biol. Chem. (1992) 267:14775-14782 !$#title Properties of human red cell spectrin heterodimer !1(side-to-side) assembly and identification of an essential !1nucleation site. !$#cross-references MUID:92340516; PMID:1634521 !$#accession B42872 !'##molecule_type protein !'##residues 47-56;293-302;1837-1846 ##label SP2 REFERENCE A93341 !$#authors Speicher, D.W.; Marchesi, V.T. !$#journal Nature (1984) 311:177-180 !$#title Erythrocyte spectrin is comprised of many homologous triple !1helical segments. !$#cross-references MUID:84295638; PMID:6472478 !$#accession B27016 !'##molecule_type protein !'##residues 292-324,'X',326-329,'Y',331-332;434-532;718-734,'V', !1736-773,'X',775-777;1036-1072,'X',1074-1077;1386-1439,'X', !11441-1443,'X',1445-1449;1479-1509,'X',1511-1513;1936-1988, !1'XX',1991-1992,'X',1994-1997 ##label SPE !'##note the purified protein had a blocked amino end COMMENT Spectrin is a major structural component of the erythrocyte !1membrane cytoskeleton and associates with ankyrin, actin, !1and band 4.1. GENETICS !$#gene GDB:SPTB !'##cross-references GDB:119602; OMIM:182870 !$#map_position 14q23-14q23 CLASSIFICATION #superfamily spectrin beta chain; alpha-actinin !1actin-binding domain homology; spectrin/dystrophin repeat !1homology KEYWORDS actin binding; cytoskeleton; duplication; erythrocyte; !1heterodimer; membrane protein FEATURE !$53-271 #domain alpha-actinin actin-binding domain homology !8#label ACT\ !$301-412 #domain spectrin/dystrophin repeat homology #label !8SP01\ !$421-526 #domain spectrin/dystrophin repeat homology #label !8SP02\ !$527-635 #domain spectrin/dystrophin repeat homology #label !8SP03\ !$636-741 #domain spectrin/dystrophin repeat homology #label !8SP04\ !$742-846 #domain spectrin/dystrophin repeat homology #label !8SP05\ !$847-952 #domain spectrin/dystrophin repeat homology #label !8SP06\ !$953-1059 #domain spectrin/dystrophin repeat homology #label !8SP07\ !$1060-1166 #domain spectrin/dystrophin repeat homology #label !8SP08\ !$1167-1272 #domain spectrin/dystrophin repeat homology #status !8atypical #label SP09\ !$1273-1377 #domain spectrin/dystrophin repeat homology #label !8SP10\ !$1378-1476 #domain spectrin/dystrophin repeat homology #label !8SP11\ !$1477-1582 #domain spectrin/dystrophin repeat homology #label !8SP12\ !$1583-1688 #domain spectrin/dystrophin repeat homology #label !8SP13\ !$1689-1795 #domain spectrin/dystrophin repeat homology #label !8SP14\ !$1796-1901 #domain spectrin/dystrophin repeat homology #label !8SP15\ !$1902-2007 #domain spectrin/dystrophin repeat homology #label !8SP16\ !$2008-2118 #domain spectrin/dystrophin repeat homology #label !8SP17 SUMMARY #length 2137 #molecular-weight 246320 #checksum 7336 SEQUENCE /// ENTRY A44159 #type complete TITLE spectrin beta-G chain - human ALTERNATE_NAMES beta-spectrin general isoform, beta G-spectrin ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A44159 REFERENCE A44159 !$#authors Hu, R.J.; Watanabe, M.; Bennett, V. !$#journal J. Biol. Chem. (1992) 267:18715-18722 !$#title Characterization of human brain cDNA encoding the general !1isoform of beta-spectrin. !$#cross-references MUID:92406787; PMID:1527002 !$#accession A44159 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-2364 ##label HU1 !'##cross-references GB:M96803; NID:g338442; PIDN:AAA60580.1; !1PID:g338443 !'##experimental_source brain !'##note sequence extracted from NCBI backbone (NCBIP:113399) GENETICS !$#gene GDB:SPTBN1 !'##cross-references GDB:120386; OMIM:182790 !$#map_position 2p21-2p21 CLASSIFICATION #superfamily spectrin beta-G chain; alpha-actinin !1actin-binding domain homology; pleckstrin repeat homology; !1spectrin/dystrophin repeat homology KEYWORDS actin binding; cytoskeleton; duplication; heterodimer; !1membrane protein FEATURE !$53-271 #domain alpha-actinin actin-binding domain homology !8#label ACT\ !$301-412 #domain spectrin/dystrophin repeat homology #label !8SP1\ !$1697-1803 #domain spectrin/dystrophin repeat homology #label !8SP2\ !$2196-2305 #domain pleckstrin repeat homology #label PLK SUMMARY #length 2364 #molecular-weight 274629 #checksum 7143 SEQUENCE /// ENTRY A46147 #type complete TITLE spectrin beta chain - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jun-2002 ACCESSIONS A46147; A33657 REFERENCE A46147 !$#authors Byers, T.J.; Brandin, E.; Lue, R.A.; Winograd, E.; Branton, !1D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:6187-6191 !$#title The complete sequence of Drosophila beta-spectrin reveals !1supra-motifs comprising eight 106-residue segments. !$#cross-references MUID:92335263; PMID:1631106 !$#accession A46147 !'##status preliminary !'##molecule_type DNA !'##residues 1-2291 ##label BYE !'##cross-references GB:M92288; NID:g157019; PIDN:AAA28399.1; !1PID:g157020 !'##note sequence extracted from NCBI backbone (NCBIP:108607) REFERENCE A33657 !$#authors Byers, T.J.; Husain-Chishti, A.; Dubreuil, R.R.; Branton, !1D.; Goldstein, L.S.B. !$#journal J. Cell Biol. (1989) 109:1633-1641 !$#title Sequence similarity of the amino-terminal domain of !1Drosophila beta spectrin to alpha actinin and dystrophin. !$#cross-references MUID:90009037; PMID:2677025 !$#accession A33657 !'##status preliminary !'##molecule_type mRNA !'##residues 1-800 ##label BY2 !'##cross-references GB:M92288 GENETICS !$#gene FlyBase:beta-Spec !'##cross-references FlyBase:FBgn0003471 CLASSIFICATION #superfamily spectrin beta-G chain; alpha-actinin !1actin-binding domain homology; pleckstrin repeat homology; !1spectrin/dystrophin repeat homology KEYWORDS actin binding; cytoskeleton FEATURE !$49-267 #domain alpha-actinin actin-binding domain homology !8#label ACT\ !$297-408 #domain spectrin/dystrophin repeat homology #label !8SP1\ !$417-522 #domain spectrin/dystrophin repeat homology #label !8SP2\ !$1698-1804 #domain spectrin/dystrophin repeat homology #label !8SP3\ !$2146-2257 #domain pleckstrin repeat homology #label PLK SUMMARY #length 2291 #molecular-weight 265785 #checksum 9818 SEQUENCE /// ENTRY SJHUK #type complete TITLE ankyrin 1, erythrocyte splice form 1 - human ALTERNATE_NAMES ankyrin 2.1, erythrocyte; ankyrin-R CONTAINS ankyrin 2.2 ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 22-Jun-1999 ACCESSIONS S08275; A33219; PC2220; A35443 REFERENCE S08275 !$#authors Lux, S.E.; John, K.M.; Bennett, V. !$#journal Nature (1990) 344:36-42 !$#title Analysis of cDNA for human erythrocyte ankyrin indicates a !1repeated structure with homology to tissue-differentiation !1and cell-cycle control proteins. !$#cross-references MUID:90158830; PMID:2137557 !$#accession S08275 !'##molecule_type mRNA !'##residues 1-1881 ##label LU1 !'##cross-references EMBL:X16609; NID:g28701; PIDN:CAA34610.1; !1PID:g28702 !$#accession A33219 !'##molecule_type protein !'##residues 2-7,'X',9-17,'X',19-20,'T',22-30;733-749,'A', !1751-753;828-833,'X',835-855,'X',857-859,'XX', !1862-871;959-1003;1106-1120,'XX', !11123-1128;1149-1172;1282-1285,'E', !11287-1288;1307-1332;1345-1365,'X', !11367;1383-1427;1601-1630;1686-1698,'D',1700;1763-1772 !1##label LUX !'##note 845-Arg and 1392-Thr were also found REFERENCE PC2220 !$#authors Hermann, J.; Barel, M.; Frade, R. !$#journal Biochem. Biophys. Res. Commun. (1994) 204:453-460 !$#title Human erythrocyte ankyrin, a cytoskeleton component, !1generates the p57 membrane proteinase which cleaves C3, the !1third component of complement. !$#cross-references MUID:95071348; PMID:7526850 !$#accession PC2220 !'##molecule_type protein !'##residues 910-929 ##label HER REFERENCE A35443 !$#authors Davis, L.H.; Bennett, V. !$#journal J. Biol. Chem. (1990) 265:10589-10596 !$#title Mapping the binding sites of human erythrocyte ankyrin for !1the anion exchanger and spectrin. !$#cross-references MUID:90285190; PMID:2141335 !$#accession A35443 !'##molecule_type protein !'##residues 'X',5,'X',7-12;403-417,'X',419-422,'H',424,'LQ';797-800, !1'L',802-814;862-863,'X',865-877;'X',899-901,'T',903-909,'X', !1911-912 ##label DAV GENETICS !$#gene GDB:ANK1; ANK !'##cross-references GDB:118737; OMIM:182900 !$#map_position 8p11.2-8p11.2 CLASSIFICATION #superfamily ankyrin; ankyrin repeat homology KEYWORDS alternative splicing; phosphoprotein FEATURE !$2-1881 #product ankyrin 1, erythrocyte form 1 #status !8predicted #label MAT1\ !$2-1512,1675-1881 #product ankyrin 2.2, erythrocyte #status predicted !8#label MAT2\ !$2-827 #domain 89K #status predicted #label DOM1\ !$2-827 #region anion exchange protein binding\ !$44-76 #domain ankyrin repeat homology #label AN01\ !$77-109 #domain ankyrin repeat homology #label AN02\ !$110-142 #domain ankyrin repeat homology #label AN03\ !$143-171 #domain ankyrin repeat homology #label AN04\ !$172-204 #domain ankyrin repeat homology #label AN05\ !$205-237 #domain ankyrin repeat homology #label AN06\ !$238-270 #domain ankyrin repeat homology #label AN07\ !$271-303 #domain ankyrin repeat homology #label AN08\ !$304-336 #domain ankyrin repeat homology #label AN09\ !$337-369 #domain ankyrin repeat homology #label AN10\ !$370-402 #domain ankyrin repeat homology #label AN11\ !$403-435 #domain ankyrin repeat homology #label AN12\ !$436-468 #domain ankyrin repeat homology #label AN13\ !$469-501 #domain ankyrin repeat homology #label AN14\ !$502-534 #domain ankyrin repeat homology #label AN15\ !$535-567 #domain ankyrin repeat homology #label AN16\ !$568-600 #domain ankyrin repeat homology #label AN17\ !$601-633 #domain ankyrin repeat homology #label AN18\ !$634-666 #domain ankyrin repeat homology #label AN19\ !$667-699 #domain ankyrin repeat homology #label AN20\ !$700-732 #domain ankyrin repeat homology #label AN21\ !$733-765 #domain ankyrin repeat homology #label AN22\ !$766-798 #domain ankyrin repeat homology #label AN23\ !$828-1382 #domain 62K #status predicted #label DOM2\ !$828-1382 #region spectrin binding\ !$1383-1881 #domain 55K #status predicted #label DOM3 SUMMARY #length 1881 #molecular-weight 206275 #checksum 2619 SEQUENCE /// ENTRY H71274 #type complete TITLE probable ankyrin - syphilis spirochete ORGANISM #formal_name Treponema pallidum subsp. pallidum #common_name syphilis spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS H71274 REFERENCE A71250 !$#authors Fraser, C.M.; Norris, S.J.; Weinstock, G.M.; White, O.; !1Sutton, G.G.; Dodson, R.; Gwinn, M.; Hickey, E.K.; Clayton, !1R.; Ketchum, K.A.; Sodergren, E.; Hardham, J.M.; McLeod, !1M.P.; Salzberg, S.; Peterson, J.; Khalak, H.; Richardson, !1D.; Howell, J.K.; Chidambaram, M.; Utterback, T.; McDonald, !1L.; Artiach, P.; Bowman, C.; Cotton, M.D.; Fujii, C.; !1Garland, S.; Hatch, B.; Horst, K.; Roberts, K.; Watthey, L.; !1Weidman, J.; Smith, H.O.; Venter, J.C. !$#journal Science (1998) 281:375-388 !$#title Complete genome sequence of Treponema pallidum, the syphilis !1spirochete. !$#cross-references MUID:98332770; PMID:9665876 !$#accession H71274 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-934 ##label COL !'##cross-references GB:AE001254; GB:AE000520; NID:g3323148; !1PIDN:AAC65803.1; PID:g3323149 !'##experimental_source strain Nichols GENETICS !$#gene TP0835 CLASSIFICATION #superfamily syphilis spirochete probable ankyrin; ankyrin !1repeat homology FEATURE !$281-313 #domain ankyrin repeat homology #label AN22 SUMMARY #length 934 #molecular-weight 100687 #checksum 9300 SEQUENCE /// ENTRY FAHUAA #type complete TITLE alpha-actinin 1 - human ALTERNATE_NAMES cytoskeletal alpha-actinin ORGANISM #formal_name Homo sapiens #common_name man DATE 07-Sep-1990 #sequence_revision 14-Jul-1994 #text_change 22-Jun-1999 ACCESSIONS S05503; A35211; A60541; S65608 REFERENCE S05503 !$#authors Millake, D.B.; Blanchard, A.D.; Patel, B.; Critchley, D.R. !$#journal Nucleic Acids Res. (1989) 17:6725 !$#title The cDNA sequence of a human placental alpha-actinin. !$#cross-references MUID:89385999; PMID:2780298 !$#accession S05503 !'##molecule_type mRNA !'##residues 1-892 ##label MIL !'##cross-references EMBL:X15804; NID:g28333; PIDN:CAA33803.1; !1PID:g28334 REFERENCE A35211 !$#authors Youssoufian, H.; McAfee, M.; Kwiatkowski, D.J. !$#journal Am. J. Hum. Genet. (1990) 47:62-72 !$#title Cloning and chromosomal localization of the human !1cytoskeletal alpha-actinin gene reveals linkage to the !1beta-spectrin gene. !$#cross-references MUID:90274024; PMID:2349951 !$#accession A35211 !'##molecule_type mRNA !'##residues 1-629,'RL',632-892 ##label YOU !'##cross-references GB:M95178; NID:g178051; PIDN:AAA51582.1; !1PID:g178052 REFERENCE A60541 !$#authors Nishiyama, M.; Ozturk, M.; Frohlich, M.; Mafune, K.; Steele !1Jr., G.; Wands, J.R. !$#journal Cancer Res. (1990) 50:6291-6294 !$#title Expression of human alpha-actinin in human hepatocellular !1carcinoma. !$#cross-references MUID:90381709; PMID:2169343 !$#accession A60541 !'##molecule_type mRNA !'##residues 297-316,'L',318-476,'L',478-653,'A',655,'F',657-673,'D', !1675-777,'S',779-892 ##label NIS !'##cross-references GB:X55187; NID:g28722; PIDN:CAA38970.1; PID:g28723 !'##note expression is high in hepatoma compared with normal liver REFERENCE S65608 !$#authors Dubernard, V.; Faucher, D.; Launay, J.M.; Legrand, C. !$#journal FEBS Lett. (1995) 364:109-114 !$#title Identification of the cytoskeletal protein alpha-actinin as !1a platelet thrombospondin-binding protein. !$#cross-references MUID:95269780; PMID:7750553 !$#accession S65608 !'##molecule_type protein !'##residues 566-577;727-738;835-849;851-859,'X',861-863 ##label DUB COMMENT Cytoskeletal alpha-actinin is associated with microfilaments !1and may mediate their attachment to the cell membrane. COMMENT Calcium inhibits actin binding by cytoskeletal (but not !1smooth or skeletal muscle) alpha-actinin. COMMENT The amino-terminal domain is involved in actin binding, the !1middle domain in formation of the antiparallel homodimer; !1the carboxyl-terminal domain may influence actin binding by !1the adjacent chain. GENETICS !$#gene GDB:ACTN1 !'##cross-references GDB:125187; OMIM:102575 !$#map_position 14q24.1-14q24.2 COMPLEX homodimer CLASSIFICATION #superfamily alpha-actinin; alpha-actinin actin-binding !1domain homology; calmodulin repeat homology; spectrin/ !1dystrophin repeat homology KEYWORDS actin binding; calcium binding; duplication; EF hand; !1homodimer FEATURE !$30-243 #domain alpha-actinin actin-binding domain homology !8#label ACT\ !$273-384 #domain spectrin/dystrophin repeat homology #label !8SP1\ !$393-499 #domain spectrin/dystrophin repeat homology #label !8SP2\ !$508-620 #domain spectrin/dystrophin repeat homology #label !8SP3\ !$629-733 #domain spectrin/dystrophin repeat homology #label !8SP4\ !$746-778 #domain calmodulin repeat homology #label EF1\ !$787-819 #domain calmodulin repeat homology #label EF2 SUMMARY #length 892 #molecular-weight 102974 #checksum 2872 SEQUENCE /// ENTRY FAHUA2 #type complete TITLE alpha-actinin 2 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 16-Oct-1992 #sequence_revision 06-Jan-1995 #text_change 22-Jun-1999 ACCESSIONS A40199 REFERENCE A40199 !$#authors Beggs, A.H.; Byers, T.J.; Knoll, J.H.M.; Boyce, F.M.; Bruns, !1G.A.P.; Kunkel, L.M. !$#journal J. Biol. Chem. (1992) 267:9281-9288 !$#title Cloning and characterization of two human skeletal muscle !1alpha-actinin genes located on chromosomes 1 and 11. !$#cross-references MUID:92250531; PMID:1339456 !$#accession A40199 !'##molecule_type mRNA !'##residues 1-894 ##label BEG !'##cross-references GB:M86406; NID:g178053; PIDN:AAA51583.1; !1PID:g178054 COMMENT The EF hand structures are predicted to be incapable of !1binding calcium. COMMENT The amino-terminal domain is involved in actin binding, the !1middle domain in formation of the homodimer with !1antiparallel major axes; the carboxyl-terminal domain may !1influence actin binding by the adjacent chain. GENETICS !$#gene GDB:ACTN2 !'##cross-references GDB:127919; OMIM:102573 !$#map_position 1q42-1q43 COMPLEX homodimer CLASSIFICATION #superfamily alpha-actinin; alpha-actinin actin-binding !1domain homology; calmodulin repeat homology; spectrin/ !1dystrophin repeat homology KEYWORDS actin binding; cardiac muscle; duplication; EF hand; heart; !1homodimer; skeletal muscle FEATURE !$37-250 #domain alpha-actinin actin-binding domain homology !8#label ACT\ !$280-391 #domain spectrin/dystrophin repeat homology #label !8SP1\ !$400-506 #domain spectrin/dystrophin repeat homology #label !8SP2\ !$515-627 #domain spectrin/dystrophin repeat homology #label !8SP3\ !$636-740 #domain spectrin/dystrophin repeat homology #label !8SP4\ !$753-785 #domain calmodulin repeat homology #label EF1\ !$789-821 #domain calmodulin repeat homology #label EF2 SUMMARY #length 894 #molecular-weight 103853 #checksum 2107 SEQUENCE /// ENTRY FAHUA3 #type complete TITLE alpha-actinin 3 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 16-Oct-1992 #sequence_revision 06-Jan-1995 #text_change 22-Jun-1999 ACCESSIONS B40199 REFERENCE A40199 !$#authors Beggs, A.H.; Byers, T.J.; Knoll, J.H.M.; Boyce, F.M.; Bruns, !1G.A.P.; Kunkel, L.M. !$#journal J. Biol. Chem. (1992) 267:9281-9288 !$#title Cloning and characterization of two human skeletal muscle !1alpha-actinin genes located on chromosomes 1 and 11. !$#cross-references MUID:92250531; PMID:1339456 !$#accession B40199 !'##molecule_type mRNA !'##residues 1-901 ##label BEG !'##cross-references GB:M86407; NID:g178057; PIDN:AAA51585.1; !1PID:g178058 COMMENT The EF hand structures are predicted to be incapable of !1binding calcium. COMMENT The amino-terminal domain is involved in actin binding, the !1middle domain in formation of the homodimer with !1antiparallel major axes; the carboxyl-terminal domain may !1influence actin binding by the adjacent chain. GENETICS !$#gene GDB:ACTN3 !'##cross-references GDB:127920; OMIM:102574 !$#map_position 11q13-11q13 COMPLEX homodimer CLASSIFICATION #superfamily alpha-actinin; alpha-actinin actin-binding !1domain homology; calmodulin repeat homology; spectrin/ !1dystrophin repeat homology KEYWORDS actin binding; duplication; EF hand; homodimer; skeletal !1muscle FEATURE !$44-257 #domain alpha-actinin actin-binding domain homology !8#label ACT\ !$287-398 #domain spectrin/dystrophin repeat homology #label !8SP1\ !$407-513 #domain spectrin/dystrophin repeat homology #label !8SP2\ !$522-634 #domain spectrin/dystrophin repeat homology #label !8SP3\ !$643-747 #domain spectrin/dystrophin repeat homology #label !8SP4\ !$760-792 #domain calmodulin repeat homology #label EF1\ !$796-828 #domain calmodulin repeat homology #label EF2 SUMMARY #length 901 #molecular-weight 103293 #checksum 6416 SEQUENCE /// ENTRY FAFFAA #type complete TITLE alpha-actinin - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 30-Jun-1991 #sequence_revision 06-Jan-1995 #text_change 22-Jun-1999 ACCESSIONS A35598; S10436 REFERENCE A35598 !$#authors Fyrberg, E.; Kelly, M.; Ball, E.; Fyrberg, C.; Reedy, M.C. !$#journal J. Cell Biol. (1990) 110:1999-2011 !$#title Molecular genetics of Drosophila alpha-actinin: mutant !1alleles disrupt Z disc integrity and muscle insertions. !$#cross-references MUID:90277718; PMID:2112549 !$#accession A35598 !'##molecule_type mRNA !'##residues 1-895 ##label FYR !'##cross-references EMBL:X51753 REFERENCE S10436 !$#authors Fyrberg, E.A. !$#submission submitted to the EMBL Data Library, January 1990 !$#accession S10436 !'##molecule_type mRNA !'##residues 1-379,'G',381-389,'M',391-444,'C',446-895 ##label FY2 !'##cross-references EMBL:X51753; NID:g8185; PIDN:CAA36042.1; PID:g8186 COMMENT In contrast to mammalian skeletal muscle alpha-actinins, the !1EF hand structures are predicted to be capable of binding !1calcium. COMMENT The amino-terminal domain is involved in actin binding, the !1middle domain in formation of the homodimer with !1antiparallel major axes; the carboxyl-terminal domain may !1influence actin binding by the adjacent chain. GENETICS !$#gene FlyBase:Actn !'##cross-references FlyBase:FBgn0000667 !$#map_position 1 2C COMPLEX homodimer CLASSIFICATION #superfamily alpha-actinin; alpha-actinin actin-binding !1domain homology; calmodulin repeat homology; spectrin/ !1dystrophin repeat homology KEYWORDS actin binding; calcium binding; duplication; EF hand; !1homodimer; skeletal muscle FEATURE !$33-246 #domain alpha-actinin actin-binding domain homology !8#label ACT\ !$276-387 #domain spectrin/dystrophin repeat homology #label !8SP1\ !$396-502 #domain spectrin/dystrophin repeat homology #label !8SP2\ !$511-623 #domain spectrin/dystrophin repeat homology #label !8SP3\ !$632-736 #domain spectrin/dystrophin repeat homology #label !8SP4\ !$749-781 #domain calmodulin repeat homology #label EF1\ !$790-822 #domain calmodulin repeat homology #label EF2 SUMMARY #length 895 #molecular-weight 104110 #checksum 2990 SEQUENCE /// ENTRY FADOAA #type complete TITLE alpha-actinin - slime mold (Dictyostelium discoideum) ORGANISM #formal_name Dictyostelium discoideum DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 22-Jun-1999 ACCESSIONS S00103; A29006 REFERENCE S00103 !$#authors Noegel, A.; Witke, W.; Schleicher, M. !$#journal FEBS Lett. (1987) 221:391-396 !$#title Calcium-sensitive non-muscle alpha-actinin contains EF-hand !1structures and highly conserved regions. !$#cross-references MUID:87304850; PMID:3622778 !$#accession S00103 !'##molecule_type mRNA !'##residues 1-862 ##label NOE !'##cross-references EMBL:Y00689; NID:g7177; PIDN:CAA68685.1; PID:g7178 REFERENCE A29006 !$#authors Witke, W.; Schleicher, M.; Lottspeich, F.; Noegel, A. !$#journal J. Cell Biol. (1986) 103:969-975 !$#title Studies on the transcription, translation, and structure of !1alpha-actinin in Dictyostelium discoideum. !$#cross-references MUID:86304574; PMID:3745276 !$#accession A29006 !'##molecule_type DNA !'##residues 92-359,'P',361-500,'T',502-505 ##label WIT !'##cross-references EMBL:X04324; NID:g7202; PIDN:CAA27855.1; !1PID:g929034 CLASSIFICATION #superfamily alpha-actinin; alpha-actinin actin-binding !1domain homology; calmodulin repeat homology; spectrin/ !1dystrophin repeat homology KEYWORDS actin binding; calcium binding; duplication; EF hand; !1homodimer FEATURE !$21-236 #domain alpha-actinin actin-binding domain homology !8#label ACT\ !$266-377 #domain spectrin/dystrophin repeat homology #label !8SP1\ !$386-493 #domain spectrin/dystrophin repeat homology #label !8SP2\ !$502-607 #domain spectrin/dystrophin repeat homology #label !8SP3\ !$616-717 #domain spectrin/dystrophin repeat homology #label !8SP4\ !$730-762 #domain calmodulin repeat homology #label EF1\ !$766-798 #domain calmodulin repeat homology #label EF2 SUMMARY #length 862 #molecular-weight 97598 #checksum 5300 SEQUENCE /// ENTRY A35836 #type complete TITLE L-plastin - human ALTERNATE_NAMES 65K phosphoprotein; p65 protein ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Oct-1990 #sequence_revision 14-Jul-1994 #text_change 16-Jul-1999 ACCESSIONS A35836; A31559; B34789; A45215; A34262; A28643 REFERENCE A35836 !$#authors Zu, Y.; Shigesada, K.; Nishida, E.; Kubota, I.; Kohno, M.; !1Hanaoka, M.; Namba, Y. !$#journal Biochemistry (1990) 29:8319-8324 !$#title 65-Kilodalton protein phosphorylated by interleukin 2 !1stimulation bears two putative actin-binding sites and two !1calcium-binding sites. !$#cross-references MUID:91070054; PMID:2252891 !$#accession A35836 !'##molecule_type mRNA !'##residues 1-627 ##label ZUA !'##cross-references GB:J02923; NID:g189501; PIDN:AAA63236.1; !1PID:g189502 !'##experimental_source T-lymphocyte cells REFERENCE A93107 !$#authors Lin, C.S.; Aebersold, R.H.; Kent, S.B.; Varma, M.; Leavitt, !1J. !$#journal Mol. Cell. Biol. (1988) 8:4659-4668 !$#title Molecular cloning and characterization of plastin, a human !1leukocyte protein expressed in transformed human !1fibroblasts. !$#cross-references MUID:89096835; PMID:3211125 !$#accession A31559 !'##molecule_type mRNA !'##residues 58-627 ##label LIN !'##cross-references GB:M22300; NID:g190029; PIDN:AAB02845.1; !1PID:g190030 REFERENCE A34789 !$#authors Lin, C.S.; Aebersold, R.H.; Leavitt, J. !$#journal Mol. Cell. Biol. (1990) 10:1818-1821 !$#title Correction of the N-terminal sequences of the human plastin !1isoforms by using anchored polymerase chain reaction: !1identification of a potential calcium-binding domain. !$#cross-references MUID:90205868; PMID:2378651 !$#accession B34789 !'##molecule_type mRNA !'##residues 1-140 ##label LI2 !'##cross-references GB:M34426; NID:g187213; PIDN:AAA36184.1; !1PID:g187214 REFERENCE A45215 !$#authors Lin, C.S.; Park, T.; Chen, Z.P.; Leavitt, J. !$#journal J. Biol. Chem. (1993) 268:2781-2792 !$#title Human plastin genes. Comparative gene structure, chromosome !1location, and differential expression in normal and !1neoplastic cells. !$#cross-references MUID:93155095; PMID:8428952 !$#accession A45215 !'##molecule_type DNA !'##residues 585-627 ##label LI3 !'##cross-references GB:L05492; NID:g187220; PIDN:AAA59529.1; !1PID:g187222 !'##note sequence extracted from NCBI backbone (NCBIP:124247) REFERENCE A34262 !$#authors Zu, Y.; Kohno, M.; Kubota, I.; Nishida, E.; Hanaoka, M.; !1Namba, Y. !$#journal Biochemistry (1990) 29:1055-1062 !$#title Characterization of interleukin 2 stimulated 65-kilodalton !1phosphoprotein in human T cells. !$#cross-references MUID:90254117; PMID:2111166 !$#accession A34262 !'##molecule_type protein !'##residues 264-282;516-533;593-609 ##label ZUY REFERENCE A28643 !$#authors Matsushima, K.; Shiroo, M.; Kung, H.; Copeland, T.D. !$#journal Biochemistry (1988) 27:3765-3770 !$#title Purification and characterization of a cytosolic !165-kilodalton phosphoprotein in human leukocytes whose !1phosphorylation is augmented by stimulation with interleukin !11. !$#cross-references MUID:88309781; PMID:3261603 !$#accession A28643 !'##molecule_type protein !'##residues 590-610,'T' ##label MAT GENETICS !$#gene GDB:LCP1 !'##cross-references GDB:119361; OMIM:153430 !$#map_position 13q14.3-13q14.3 CLASSIFICATION #superfamily plastin; alpha-actinin actin-binding domain !1homology; calmodulin repeat homology KEYWORDS actin binding; blocked amino end; calcium binding; EF hand; !1phosphoprotein FEATURE !$9-41 #domain calmodulin repeat homology #label EF1\ !$49-81 #domain calmodulin repeat homology #label EF2\ !$119-370 #domain alpha-actinin actin-binding domain homology !8#label ACT1\ !$393-619 #domain alpha-actinin actin-binding domain homology !8#label ACT2 SUMMARY #length 627 #molecular-weight 70289 #checksum 6540 SEQUENCE /// ENTRY A34789 #type complete TITLE T-plastin - human ORGANISM #formal_name Homo sapiens #common_name man DATE 13-Jul-1990 #sequence_revision 14-Jul-1994 #text_change 16-Jul-1999 ACCESSIONS A34789; B31559; B45215 REFERENCE A34789 !$#authors Lin, C.S.; Aebersold, R.H.; Leavitt, J. !$#journal Mol. Cell. Biol. (1990) 10:1818-1821 !$#title Correction of the N-terminal sequences of the human plastin !1isoforms by using anchored polymerase chain reaction: !1identification of a potential calcium-binding domain. !$#cross-references MUID:90205868; PMID:2378651 !$#accession A34789 !'##molecule_type mRNA !'##residues 1-143 ##label LIN !'##cross-references GB:M34427; NID:g339847; PIDN:AAA36759.1; !1PID:g339848 REFERENCE A93107 !$#authors Lin, C.S.; Aebersold, R.H.; Kent, S.B.; Varma, M.; Leavitt, !1J. !$#journal Mol. Cell. Biol. (1988) 8:4659-4668 !$#title Molecular cloning and characterization of plastin, a human !1leukocyte protein expressed in transformed human !1fibroblasts. !$#cross-references MUID:89096835; PMID:3211125 !$#accession B31559 !'##molecule_type mRNA !'##residues 61-630 ##label LI2 !'##cross-references GB:M22299; NID:g190027; PIDN:AAB02844.1; !1PID:g190028 REFERENCE A45215 !$#authors Lin, C.S.; Park, T.; Chen, Z.P.; Leavitt, J. !$#journal J. Biol. Chem. (1993) 268:2781-2792 !$#title Human plastin genes. Comparative gene structure, chromosome !1location, and differential expression in normal and !1neoplastic cells. !$#cross-references MUID:93155095; PMID:8428952 !$#accession B45215 !'##molecule_type DNA !'##residues 588-630 ##label LI3 !'##cross-references GB:L05491; NID:g292831; PIDN:AAA61214.1; !1PID:g292832; GB:L05492 !'##note sequence extracted from NCBI backbone (NCBIP:124249) GENETICS !$#gene GDB:PLTN2 !'##cross-references GDB:6774663 !$#map_position X CLASSIFICATION #superfamily plastin; alpha-actinin actin-binding domain !1homology; calmodulin repeat homology KEYWORDS actin binding; calcium binding; EF hand FEATURE !$12-44 #domain calmodulin repeat homology #label EF1\ !$52-84 #domain calmodulin repeat homology #label EF2\ !$122-373 #domain alpha-actinin actin-binding domain homology !8#label ACT1\ !$396-622 #domain alpha-actinin actin-binding domain homology !8#label ACT2 SUMMARY #length 630 #molecular-weight 70810 #checksum 5970 SEQUENCE /// ENTRY A37097 #type complete TITLE fimbrin - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 01-Feb-1991 #sequence_revision 14-Jul-1994 #text_change 16-Jul-1999 ACCESSIONS A37097; S12080 REFERENCE A37097 !$#authors de Arruda, M.V.; Watson, S.; Lin, C.S.; Leavitt, J.; !1Matsudaira, P. !$#journal J. Cell Biol. (1990) 111:1069-1079 !$#title Fimbrin is a homologue of the cytoplasmic phosphoprotein !1plastin and has domains homologous with calmodulin and actin !1gelation proteins. !$#cross-references MUID:90361735; PMID:2391360 !$#accession A37097 !'##molecule_type mRNA !'##residues 1-630 ##label DEA !'##cross-references GB:X52562; NID:g62889; PIDN:CAA36796.1; PID:g62890 CLASSIFICATION #superfamily plastin; alpha-actinin actin-binding domain !1homology; calmodulin repeat homology KEYWORDS actin binding; blocked amino end; calcium binding; EF hand FEATURE !$11-43 #domain calmodulin repeat homology #label EF1\ !$51-83 #domain calmodulin repeat homology #label EF2\ !$121-372 #domain alpha-actinin actin-binding domain homology !8#label ACT1\ !$395-621 #domain alpha-actinin actin-binding domain homology !8#label ACT2 SUMMARY #length 630 #molecular-weight 70938 #checksum 1840 SEQUENCE /// ENTRY S29320 #type complete TITLE fimbrin - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YD9302.04c; protein YDR129c ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Dec-1993 #sequence_revision 14-Jul-1994 #text_change 05-Nov-1999 ACCESSIONS S29320; S51856 REFERENCE S29320 !$#authors Adams, A.E.M.; Botstein, D.; Drubin, D.G. !$#journal Nature (1991) 354:404-408 !$#title Requirement of yeast fimbrin for actin organization and !1morphogenesis in vivo. !$#cross-references MUID:92065984; PMID:1956405 !$#accession S29320 !'##molecule_type DNA !'##residues 1-642 ##label ADA !'##cross-references EMBL:X63867; NID:g4419; PIDN:CAA45346.1; PID:g4420 REFERENCE S51853 !$#authors Oliver, K.; Harris, D. !$#submission submitted to the EMBL Data Library, February 1995 !$#accession S51856 !'##molecule_type DNA !'##residues 1-642 ##label OLI !'##cross-references EMBL:Z48179; NID:g665657; PIDN:CAA88210.1; !1PID:g665661; GSPDB:GN00004; MIPS:YDR129c GENETICS !$#gene SGD:SAC6; MIPS:YDR129c !'##cross-references SGD:S0002536; MIPS:YDR129c !$#map_position 4R !$#introns 7/3 CLASSIFICATION #superfamily plastin; alpha-actinin actin-binding domain !1homology; calmodulin repeat homology KEYWORDS actin binding; calcium binding; EF hand FEATURE !$16-48 #domain calmodulin repeat homology #label EF1\ !$51-83 #domain calmodulin repeat homology #label EF2\ !$138-385 #domain alpha-actinin actin-binding domain homology !8#label ACT1\ !$410-637 #domain alpha-actinin actin-binding domain homology !8#label ACT2 SUMMARY #length 642 #molecular-weight 71772 #checksum 4629 SEQUENCE /// ENTRY S05943 #type complete TITLE gelation factor - slime mold (Dictyostelium discoideum) ORGANISM #formal_name Dictyostelium discoideum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S05943; A30944 REFERENCE S05943 !$#authors Noegel, A.A.; Rapp, S.; Lottspeich, F.; Schleicher, M.; !1Stewart, M. !$#journal J. Cell Biol. (1989) 109:607-618 !$#title The Dictyostelium gelation factor shares a putative actin !1binding site with alpha-actinins and dystrophin and also has !1a rod domain containing six 100-residue motifs that appear !1to have a cross-beta conformation. !$#cross-references MUID:89340643; PMID:2668299 !$#accession S05943 !'##molecule_type mRNA !'##residues 1-857 ##label NOE !'##cross-references EMBL:X15430; NID:g7285; PIDN:CAA33471.1; PID:g7286 !'##note part of this sequence was confirmed by protein sequencing CLASSIFICATION #superfamily Dictyostelium gelation factor; alpha-actinin !1actin-binding domain homology KEYWORDS actin binding; duplication; tandem repeat FEATURE !$11-220 #domain alpha-actinin actin-binding domain homology !8#label ACT SUMMARY #length 857 #molecular-weight 92206 #checksum 9762 SEQUENCE /// ENTRY MMHUE4 #type complete TITLE erythrocyte membrane protein 4.1, parent splice form - human CONTAINS erythrocyte membrane protein 4.1; lymphocyte membrane protein 4.1 ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1990 #sequence_revision 08-Feb-1996 #text_change 22-Jun-1999 ACCESSIONS A39810; A60244; A30207; A94143; A31260; B31260; C31260; !1S13152; A92559; A34377; A25306; A26656; JS0207 REFERENCE A39810 !$#authors Conboy, J.G.; Chan, J.Y.; Chasis, J.A.; Kan, Y.W.; Mohandas, !1N. !$#journal J. Biol. Chem. (1991) 266:8273-8280 !$#title Tissue- and development-specific alternative RNA splicing !1regulates expression of multiple isoforms of erythroid !1membrane protein 4.1. !$#cross-references MUID:91217063; PMID:2022644 !$#accession A39810 !'##molecule_type mRNA !'##residues 1-850 ##label CON !'##cross-references GB:M61733 REFERENCE A60244 !$#authors Tang, T.K.; Leto, T.L.; Marchesi, V.T.; Benz Jr., E.J. !$#journal Adv. Exp. Med. Biol. (1988) 241:81-95 !$#title Expression of specific isoforms of protein 4.1 in erythroid !1and non-erythroid tissues. !$#cross-references MUID:89132003; PMID:3223413 !$#accession A60244 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-50,'Q',52,'L',54-167,'F',169-227,263-615,656-787,'K', !1789-850 ##label TAN !'##experimental_source T-cell leukemia line MOLT-4 !'##note lymphocyte membrane protein 4.1 REFERENCE A94196 !$#authors Tang, T.K.; Leto, T.L.; Correas, I.; Alonso, M.A.; Marchesi, !1V.T.; Benz Jr., E.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:3713-3717 !$#title Selective expression of an erythroid-specific isoform of !1protein 4.1. !$#cross-references MUID:88234496; PMID:3375238 !$#accession A30207 !'##molecule_type mRNA !'##residues 210-227,263-615,656-787,'K',789-850 ##label TA2 !'##cross-references GB:J03796; NID:g182072; PIDN:AAA35794.1; !1PID:g182074 !'##experimental_source T-cell leukemia line MOLT-4 !'##note the authors translated the codon AAA for residue 539 as Gln REFERENCE A94143 !$#authors Conboy, J.; Kan, Y.W.; Shohet, S.B.; Mohandas, N. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:9512-9516 !$#title Molecular cloning of protein 4.1, a major structural element !1of the human erythrocyte membrane skeleton. !$#cross-references MUID:87092279; PMID:3467321 !$#accession A94143 !'##molecule_type mRNA !'##residues 210-615,635-758,793-850 ##label CO2 !'##cross-references GB:M14993; NID:g182075; PIDN:AAA35795.1; !1PID:g182076 !'##experimental_source reticulocyte REFERENCE A94215 !$#authors Conboy, J.G.; Chan, J.; Mohandas, N.; Kan, Y.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:9062-9065 !$#title Multiple protein 4.1 isoforms produced by alternative !1splicing in human erythroid cells. !$#cross-references MUID:89057876; PMID:3194408 !$#accession A31260 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type mRNA !'##residues 615,656-700 ##label CO3 !'##experimental_source reticulocyte !$#accession B31260 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type mRNA !'##residues 701-714,758-837,'L',839-848,'E' ##label CO4 !'##experimental_source reticulocyte !$#accession C31260 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type mRNA !'##residues 701-758,793-837,'L',839-848,'E' ##label CO5 !'##experimental_source reticulocyte REFERENCE S13152 !$#authors Horne, W.C.; Prinz, W.C.; Tang, E.K.Y. !$#journal Biochim. Biophys. Acta (1990) 1055:87-92 !$#title Identification of two cAMP-dependent phosphorylation sites !1on erythrocyte protein 4.1. !$#cross-references MUID:91027920; PMID:2171679 !$#accession S13152 !'##molecule_type protein !'##residues 534-541;693-701;758,793-794 ##label HOR REFERENCE A92559 !$#authors Correas, I.; Speicher, D.W.; Marchesi, V.T. !$#journal J. Biol. Chem. (1986) 261:13362-13366 !$#title Structure of the spectrin-actin binding site of erythrocyte !1protein 4.1. !$#cross-references MUID:87008553; PMID:3531202 !$#accession A92559 !'##molecule_type protein !'##residues 615,635-700 ##label COR !'##note this 67-residue peptide forms a ternary complex with spectrin !1and actin; antibodies to this peptide inhibit the !1interaction of protein 4.1, spectrin, and actin !'##note this peptide contains several possible sites for !1phosphorylation by cAMP-dependent protein kinase REFERENCE A34377 !$#authors Inaba, M.; Maede, Y. !$#journal J. Biol. Chem. (1989) 264:18149-18155 !$#title O-N-acetyl-D-glucosamine moiety on discrete peptide of !1multiple protein 4.1 isoforms regulated by alternative !1pathways. !$#cross-references MUID:90036892; PMID:2808371 !$#accession A34377 !'##molecule_type protein !'##residues 772-791 ##label INA !'##note this peptide region appears to have several partially !1glycosylated Ser and Thr residues COMMENT In mammalian erythrocytes, protein 4.1 stabilizes the !1spectrin-actin network and helps bind this membrane skeleton !1to the lipid bilayer through interaction with the !1transmembrane proteins band 3 and glycophorin. COMMENT Four domains are proposed based on the properties of !1peptides released after limited chymotryptic cleavage. The !1amino-terminal 30K peptide binds to the cell membrane, !1interacting with band 3, glycophorin, and phospholipids. !1This domain is hydrophobic, and has two potential !1phosphorylation and 3 potential glycosylation sites. This !1domain is followed by a 16K hydrophilic domain that is high !1in proline. COMMENT Following the highly-charged domain that binds spectrin and !1actin (residues 615-700) is a carboxyl-terminal domain that !1is quite acidic. COMMENT The boundary between the membrane-binding and hydrophilic !1domains is uncertain. GENETICS !$#gene GDB:EPB41 !'##cross-references GDB:119865; OMIM:130500 !$#map_position 1p36.2-1p34 CLASSIFICATION #superfamily membrane protein 4.1; protein 4.1 !1membrane-binding domain homology KEYWORDS alternative initiators; alternative splicing; cytoskeleton; !1erythrocyte; membrane protein; phosphoprotein FEATURE !$1-227,263-615, !$656-850 #product lymphocyte membrane protein 4.1 #status !8predicted #label MAT\ !$210-615,635-758, !$793-850 #product erythrocyte membrane protein 4.1 #status !8predicted #label MA2\ !$210-487 #domain membrane-bound #status predicted #label DM1\ !$212-487 #domain protein 4.1 membrane-binding domain homology !8#label B41\ !$488-614 #domain hydrophilic #label DM2\ !$615-700 #domain spectrin/actin binding #status predicted !8#label DM3\ !$701-850 #domain carboxyl-terminal #label DM4\ !$540,695 #binding_site phosphate (Ser) (covalent) (by !8cAMP-dependent kinase) #status experimental SUMMARY #length 850 #molecular-weight 95238 #checksum 9393 SEQUENCE /// ENTRY A34400 #type complete TITLE ezrin [validated] - human ALTERNATE_NAMES cytovillin; p81 protein; villin 2 ORGANISM #formal_name Homo sapiens #common_name man DATE 22-Jun-1990 #sequence_revision 14-Jul-1994 #text_change 08-Dec-2000 ACCESSIONS A34400; S09263; E61002 REFERENCE A34400 !$#authors Turunen, O.; Winqvist, R.; Pakkanen, R.; Grzeschik, K.H.; !1Wahlstroem, T.; Vaheri, A. !$#journal J. Biol. Chem. (1989) 264:16727-16732 !$#title Cytovillin, a microvillar M-r 75,000 protein. cDNA sequence, !1prokaryotic expression, and chromosomal localization. !$#cross-references MUID:89380299; PMID:2674140 !$#accession A34400 !'##molecule_type mRNA !'##residues 1-586 ##label TUR !'##cross-references GB:J05021 !'##note the translation of residues 1-11 is not given !'##note parts of this sequence were confirmed by protein sequencing REFERENCE S09263 !$#authors Gould, K.L.; Bretscher, A.; Esch, F.S.; Hunter, T. !$#journal EMBO J. (1989) 8:4133-4142 !$#title cDNA cloning and sequencing of the protein-tyrosine kinase !1substrate, ezrin, reveals homology to band 4.1. !$#cross-references MUID:90076135; PMID:2591371 !$#accession S09263 !'##molecule_type mRNA !'##residues 2-586 ##label GOU !'##cross-references GB:X51521; NID:g31282; PIDN:CAA35893.1; PID:g31283 REFERENCE A61002 !$#authors Bauw, G.; Rasmussen, H.H.; Van Den Bulcke, M.; Van Damme, !1J.; Puype, M.; Gesser, B.; Celis, J.E.; Vandekerckhove, J. !$#journal Electrophoresis (1990) 11:528-536 !$#title Two-dimensional gel electrophoresis, protein electroblotting !1and microsequencing: a direct link between proteins and !1genes. !$#cross-references MUID:91031404; PMID:1699755 !$#accession E61002 !'##molecule_type protein !'##residues 255-263;194,'Q',196-199,'X',201;264-270 ##label BAU !'##note it is not certain whether this material represents ezrin or !1radixin (see entry A46127), both of which have identical !1sequences in the regions corresponding to the fragments !1sequenced !'##note this material corresponds to transformed epithelial amnion cell !1(AMA) database protein IEF 4717 COMMENT This protein is located in microvilli and is proposed to !1play a role in modulating the association of the cortical !1cytoskeleton to the plasma membrane. GENETICS !$#gene GDB:VIL2 !'##cross-references GDB:120489; OMIM:123900 !$#map_position 6q25-6q26 CLASSIFICATION #superfamily ezrin; protein 4.1 membrane-binding domain !1homology KEYWORDS actin binding; cytoskeleton; membrane-associated protein; !1phosphoprotein FEATURE !$2-586 #product ezrin #status experimental #label MAT\ !$7-291 #domain protein 4.1 membrane-binding domain homology !8#label B41\ !$553-586 #region actin binding #status predicted\ !$66 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$214,299,332 #binding_site phosphate (Thr) (covalent) #status !8predicted SUMMARY #length 586 #molecular-weight 69398 #checksum 3305 SEQUENCE /// ENTRY B41129 #type complete TITLE ezrin - mouse ALTERNATE_NAMES cytovillin; p81 protein; radixin; villin 2 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 03-Aug-1992 #sequence_revision 14-Jul-1994 #text_change 22-Jun-1999 ACCESSIONS B41129; C46501; A46501; B46501; S24200 REFERENCE A41129 !$#authors Funayama, N.; Nagafuchi, A.; Sato, N.; Tsukita, S.; Tsukita, !1S. !$#journal J. Cell Biol. (1991) 115:1039-1048 !$#title Radixin is a novel member of the band 4.1 family. !$#cross-references MUID:92064635; PMID:1955455 !$#accession B41129 !'##molecule_type mRNA !'##residues 1-586 ##label FUN !'##cross-references EMBL:X60671; NID:g50880; PIDN:CAA43086.1; !1PID:g50881 REFERENCE A46501 !$#authors Egerton, M.; Burgess, W.H.; Chen, D.; Druker, B.J.; !1Bretscher, A.; Samelson, L.E. !$#journal J. Immunol. (1992) 149:1847-1852 !$#title Identification of ezrin as an 81-kDa tyrosine-phosphorylated !1protein in T cells. !$#cross-references MUID:92388649; PMID:1381389 !$#accession C46501 !'##status preliminary !'##molecule_type protein !'##residues 412-426 ##label EGE !'##experimental_source MRL lpr/lpr, T-cells !'##note sequence extracted from NCBI backbone (NCBIP:112938) !$#accession A46501 !'##status preliminary !'##molecule_type protein !'##residues 27-33,'E' ##label EG2 !'##experimental_source MRL lpr/lpr, T-cells !'##note sequence extracted from NCBI backbone (NCBIP:112936) !$#accession B46501 !'##status preliminary !'##molecule_type protein !'##residues 53-57,148,'L',150,'G',152-155 ##label EG3 !'##experimental_source MRL lpr/lpr, T-cells !'##note sequence extracted from NCBI backbone (NCBIP:112940) COMMENT This protein is located in microvilli and is proposed to !1play a role in modulating the association of the cortical !1cytoskeleton to the plasma membrane. CLASSIFICATION #superfamily ezrin; protein 4.1 membrane-binding domain !1homology KEYWORDS actin binding; cytoskeleton; cytosol; membrane-associated !1protein; phosphoprotein FEATURE !$2-586 #product ezrin #status predicted #label MAT\ !$7-291 #domain protein 4.1 membrane-binding domain homology !8#label B41\ !$553-586 #region actin binding #status predicted\ !$66 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$214,299,332 #binding_site phosphate (Thr) (covalent) #status !8predicted SUMMARY #length 586 #molecular-weight 69345 #checksum 1215 SEQUENCE /// ENTRY A46127 #type complete TITLE radixin - human ORGANISM #formal_name Homo sapiens #common_name man DATE 21-Sep-1993 #sequence_revision 14-Jul-1994 #text_change 22-Jun-1999 ACCESSIONS A46127 REFERENCE A46127 !$#authors Wilgenbus, K.K.; Milatovich, A.; Francke, U.; Furthmayr, H. !$#journal Genomics (1993) 16:199-206 !$#title Molecular cloning, cDNA sequence, and chromosomal assignment !1of the human radixin gene and two dispersed pseudogenes. !$#cross-references MUID:93252378; PMID:8486357 !$#accession A46127 !'##molecule_type mRNA !'##residues 1-583 ##label WIL !'##cross-references GB:L02320; NID:g307365; PIDN:AAA36541.1; !1PID:g307366 !'##note sequence extracted from NCBI backbone (NCBIN:131481, !1NCBIP:131482) COMMENT Radixin is a capping protein for the barbed end of actin !1filaments and it is proposed to play a role in the !1association of actin filaments with the plasma membrane. GENETICS !$#gene GDB:RDX !'##cross-references GDB:136270; OMIM:179410 !$#map_position 11q23-11q23 CLASSIFICATION #superfamily ezrin; protein 4.1 membrane-binding domain !1homology KEYWORDS actin binding; cytoskeleton FEATURE !$7-291 #domain protein 4.1 membrane-binding domain homology !8#label B41\ !$470-477 #region proline-rich\ !$550-583 #region actin binding #status predicted SUMMARY #length 583 #molecular-weight 68563 #checksum 9557 SEQUENCE /// ENTRY S39805 #type complete TITLE radixin - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 19-May-1994 #sequence_revision 14-Jul-1994 #text_change 22-Jun-1999 ACCESSIONS S39805 REFERENCE S39804 !$#authors Lankes, W.T.; Schwartz-Albiez, R.; Furthmayr, H. !$#journal Biochim. Biophys. Acta (1993) 1216:479-482 !$#title Cloning and sequencing of porcine moesin and radixin cDNA !1and identification of highly conserved domains. !$#cross-references MUID:94092743; PMID:8268231 !$#accession S39805 !'##molecule_type mRNA !'##residues 1-583 ##label LAN !'##cross-references GB:M86444; EMBL:M86391; NID:g164585; !1PIDN:AAB02865.1; PID:g164586 COMMENT Radixin is a capping protein for the barbed end of actin !1filaments and it is proposed to play a role in the !1association of actin filaments with the plasma membrane. CLASSIFICATION #superfamily ezrin; protein 4.1 membrane-binding domain !1homology KEYWORDS actin binding; cytoskeleton FEATURE !$7-291 #domain protein 4.1 membrane-binding domain homology !8#label B41\ !$470-477 #region proline-rich\ !$550-583 #region actin binding #status predicted SUMMARY #length 583 #molecular-weight 68549 #checksum 9915 SEQUENCE /// ENTRY A41129 #type complete TITLE radixin - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 03-Aug-1992 #sequence_revision 14-Jul-1994 #text_change 05-Sep-1997 ACCESSIONS A41129; S24201 REFERENCE A41129 !$#authors Funayama, N.; Nagafuchi, A.; Sato, N.; Tsukita, S.; Tsukita, !1S. !$#journal J. Cell Biol. (1991) 115:1039-1048 !$#title Radixin is a novel member of the band 4.1 family. !$#cross-references MUID:92064635; PMID:1955455 !$#accession A41129 !'##molecule_type mRNA !'##residues 1-583 ##label FUN !'##cross-references EMBL:X60672; NID:g1033049; PID:g1334260 !'##note part of this sequence was confirmed by protein sequencing COMMENT Radixin is a capping protein for the barbed end of actin !1filaments and it is proposed to play a role in the !1association of actin filaments with the plasma membrane. CLASSIFICATION #superfamily ezrin; protein 4.1 membrane-binding domain !1homology KEYWORDS actin binding; cytoskeleton FEATURE !$7-291 #domain protein 4.1 membrane-binding domain homology !8#label B41\ !$470-477 #region proline-rich\ !$550-583 #region actin binding #status predicted SUMMARY #length 583 #molecular-weight 68451 #checksum 1462 SEQUENCE /// ENTRY A41289 #type complete TITLE moesin - human ALTERNATE_NAMES membrane-organizing extension spike protein ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1992 #sequence_revision 14-Jul-1994 #text_change 22-Jun-1999 ACCESSIONS A41289 REFERENCE A41289 !$#authors Lankes, W.T.; Furthmayr, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:8297-8301 !$#title Moesin: a member of the protein 4.1-talin-ezrin family of !1proteins. !$#cross-references MUID:92020840; PMID:1924289 !$#accession A41289 !'##molecule_type mRNA !'##residues 1-577 ##label LAN !'##cross-references GB:M69066; NID:g188625; PIDN:AAA36322.1; !1PID:g188626 COMMENT Moesin is proposed to be involved in linking the !1cytoskeleton to the plasma membrane. GENETICS !$#gene GDB:MSN !'##cross-references GDB:136819; OMIM:309845 !$#map_position Xq11.2-Xq12 CLASSIFICATION #superfamily ezrin; protein 4.1 membrane-binding domain !1homology KEYWORDS actin binding; cytoskeleton; membrane protein FEATURE !$2-577 #product moesin #status predicted #label MAT\ !$7-291 #domain protein 4.1 membrane-binding domain homology !8#label B41\ !$544-577 #region actin binding #status predicted SUMMARY #length 577 #molecular-weight 67820 #checksum 7311 SEQUENCE /// ENTRY S39804 #type complete TITLE moesin - pig ALTERNATE_NAMES membrane-organizing extension spike protein ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 19-May-1994 #sequence_revision 14-Jul-1994 #text_change 22-Jun-1999 ACCESSIONS S39804 REFERENCE S39804 !$#authors Lankes, W.T.; Schwartz-Albiez, R.; Furthmayr, H. !$#journal Biochim. Biophys. Acta (1993) 1216:479-482 !$#title Cloning and sequencing of porcine moesin and radixin cDNA !1and identification of highly conserved domains. !$#cross-references MUID:94092743; PMID:8268231 !$#accession S39804 !'##molecule_type mRNA !'##residues 1-577 ##label LAN !'##cross-references EMBL:M86450; NID:g164581; PIDN:AAB02864.1; !1PID:g164582 COMMENT Moesin is proposed to be involved in linking the !1cytoskeleton to the plasma membrane. CLASSIFICATION #superfamily ezrin; protein 4.1 membrane-binding domain !1homology KEYWORDS actin binding; cytoskeleton; membrane protein FEATURE !$2-577 #product moesin #status predicted #label MAT\ !$7-291 #domain protein 4.1 membrane-binding domain homology !8#label B41\ !$544-577 #region actin binding #status predicted SUMMARY #length 577 #molecular-weight 67660 #checksum 6263 SEQUENCE /// ENTRY UBPGA #type complete TITLE tubulin alpha chain - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 01-Sep-1981 #sequence_revision 01-Sep-1981 #text_change 07-May-1999 ACCESSIONS A93874; S29191; A02966 REFERENCE A93874 !$#authors Ponstingl, H.; Krauhs, E.; Little, M.; Kempf, T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:2757-2761 !$#title Complete amino acid sequence of alpha-tubulin from porcine !1brain. !$#cross-references MUID:81247365; PMID:7019911 !$#accession A93874 !'##molecule_type protein !'##residues 1-451 ##label PON !'##note 265-Ile and 265-Gly, 266-Ile, 271-Arg, 272-Phe, and 273-Asx !1were also found !'##note Tyr-451 was found in only 15% of the molecules REFERENCE S29191 !$#authors Ruediger, M.; Plessman, U.; Kloeppel, K.D.; Wehland, J.; !1Weber, K. !$#journal FEBS Lett. (1992) 308:101-105 !$#title Class II tubulin, the major brain beta tubulin isotype is !1polyglutamylated on glutamic acid residue 435. !$#cross-references MUID:92354756; PMID:1379548 !$#accession S29191 !'##molecule_type protein !'##residues 1-3,'X',5-10,'R',11-16;214-226;357,'Q', !1359-369;429-438;439-450 ##label RUE REFERENCE A90072 !$#authors Zabrecky, J.R.; Cole, R.D. !$#journal Arch. Biochem. Biophys. (1983) 225:475-481 !$#title Localization of the ATP binding site on alpha-tubulin. !$#cross-references MUID:84022547; PMID:6688710 !$#contents annotation; binding site COMMENT Tubulin is found in the microtubules of eukaryote cells. It !1binds ATP on its alpha chain and GTP both at an exchangeable !1site on its beta chain and at a nonexchangeable site not yet !1identified. COMMENT The highly acidic carboxyl-terminal region may bind cations !1such as calcium. COMPLEX heterodimer of alpha and beta (see PIR:UBPGB) chains CLASSIFICATION #superfamily tubulin KEYWORDS heterodimer; microtubule FEATURE !$142-148 #region tubulin/FtsZ GTP/GDP-binding (G-G-G-T-G-[ST] !8-G) motif\ !$445 #binding_site polyglutamate (Glu) (covalent) #status !8experimental\ !$450-451 #cleavage_site Glu-Tyr (tubulin-specific !8carboxypeptidase) #status experimental\ !$450-451 #cross-link peptide (Glu-Tyr) (by tubulin-tyrosine !8ligase) #status experimental SUMMARY #length 451 #molecular-weight 50068 #checksum 9474 SEQUENCE /// ENTRY UBRTA #type complete TITLE tubulin alpha chain - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 22-Jun-1999 ACCESSIONS A92869; A93728; A02967 REFERENCE A92869 !$#authors Lemischka, I.R.; Farmer, S.; Racaniello, V.R.; Sharp, P.A. !$#journal J. Mol. Biol. (1981) 151:101-120 !$#title Nucleotide sequence and evolution of a mammalian !1alpha-tubulin messenger RNA. !$#cross-references MUID:82122570; PMID:7328649 !$#accession A92869 !'##molecule_type mRNA !'##residues 1-451 ##label LEM !'##cross-references GB:J00798; NID:g207546; PIDN:AAA42306.1; !1PID:g207548; GB:V01227; NID:g55776; PID:g55777 REFERENCE A93728 !$#authors Ginzburg, I.; Behar, L.; Givol, D.; Littauer, U.Z. !$#journal Nucleic Acids Res. (1981) 9:2691-2697 !$#title The nucleotide sequence of rat alpha-tubulin: 3'-end !1characteristics, and evolutionary conservation. !$#cross-references MUID:82014864; PMID:6269058 !$#accession A93728 !'##molecule_type mRNA !'##residues 307-339,'S',341-451 ##label GIN !'##cross-references GB:V01226; GB:J00796; NID:g55774; PIDN:CAA24536.1; !1PID:g55775 !'##note this sequence is encoded by a gene different from that coding !1for the sequence shown COMMENT Tubulin is a dimer of alpha and beta chains and is found in !1the microtubules of all eukaryote cells. It binds (by !1homology with the bovine sequence) ATP on its alpha chain !1and GTP both at an exchangeable site on its beta chain and !1at a nonexchangeable site not yet identified. CLASSIFICATION #superfamily tubulin KEYWORDS heterodimer; microtubule FEATURE !$142-148 #region tubulin/FtsZ GTP/GDP-binding (G-G-G-T-G-[ST] !8-G) motif\ !$445 #binding_site polyglutamate (Glu) (covalent) #status !8predicted\ !$450-451 #cleavage_site Glu-Tyr (tubulin-specific !8carboxypeptidase) #status predicted\ !$450-451 #cross-link peptide (Glu-Tyr) (by tubulin-tyrosine !8ligase) #status predicted SUMMARY #length 451 #molecular-weight 50135 #checksum 9808 SEQUENCE /// ENTRY UBCHA #type fragment TITLE tubulin alpha chain - chicken (fragment) ORGANISM #formal_name Gallus gallus #common_name chicken DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 22-Jun-1999 ACCESSIONS A02968 REFERENCE A93246 !$#authors Valenzuela, P.; Quiroga, M.; Zaldivar, J.; Rutter, W.J.; !1Kirschner, M.W.; Cleveland, D.W. !$#journal Nature (1981) 289:650-655 !$#title Nucleotide and corresponding amino acid sequences encoded by !1alpha and beta tubulin mRNAs. !$#cross-references MUID:81123093; PMID:7464932 !$#accession A02968 !'##molecule_type mRNA !'##residues 1-411 ##label VAL !'##cross-references GB:J00912; NID:g212835; PIDN:AAA49121.1; !1PID:g212836; GB:V00388; NID:g63069; PID:g63070 CLASSIFICATION #superfamily tubulin KEYWORDS heterodimer; microtubule FEATURE !$102-108 #region tubulin/FtsZ GTP/GDP-binding (G-G-G-T-G-[ST] !8-G) motif\ !$405 #binding_site polyglutamate (Glu) (covalent) #status !8predicted\ !$410-411 #cleavage_site Glu-Tyr (tubulin-specific !8carboxypeptidase) #status predicted\ !$410-411 #cross-link peptide (Glu-Tyr) (by tubulin-tyrosine !8ligase) #status predicted SUMMARY #length 411 #checksum 7596 SEQUENCE /// ENTRY UBURAL #type fragment TITLE tubulin alpha chain - sea urchin (Lytechinus pictus) (fragment) ORGANISM #formal_name Lytechinus pictus #common_name painted urchin DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 10-Jul-1998 ACCESSIONS A02969 REFERENCE A92958 !$#authors Alexandraki, D.; Ruderman, J.V. !$#journal J. Mol. Evol. (1983) 19:397-410 !$#title Evolution of alpha- and beta-tubulin genes as inferred by !1the nucleotide sequence of sea urchin cDNA clones. !$#cross-references MUID:84090258; PMID:6317873 !$#accession A02969 !'##molecule_type mRNA !'##residues 1-161 ##label ALE CLASSIFICATION #superfamily tubulin KEYWORDS heterodimer; microtubule FEATURE !$160-161 #cleavage_site Glu-Tyr (tubulin-specific !8carboxypeptidase) #status predicted\ !$160-161 #cross-link peptide (Glu-Tyr) (by tubulin-tyrosine !8ligase) #status predicted SUMMARY #length 161 #checksum 1974 SEQUENCE /// ENTRY UBCHA5 #type complete TITLE tubulin alpha-5 chain - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 04-Oct-1996 ACCESSIONS S00470 REFERENCE S00468 !$#authors Pratt, L.F.; Cleveland, D.W. !$#journal EMBO J. (1988) 7:931-940 !$#title A survey of the alpha-tubulin gene family in chicken: !1unexpected sequence heterogeneity in the polypeptides !1encoded by five expressed genes. !$#cross-references MUID:88296435; PMID:3267229 !$#accession S00470 !'##molecule_type DNA !'##residues 1-448 ##label PRA !'##cross-references EMBL:X08061 !'##note the authors translated the codon TGT for residue 137 as Val in !1Fig. 3 and as Ile in Fig. 6 COMMENT Tubulin is a dimer of alpha and beta chains. GENETICS !$#introns 1/3; 76/1; 125/3 CLASSIFICATION #superfamily tubulin KEYWORDS heterodimer; microtubule FEATURE !$142-148 #region tubulin/FtsZ GTP/GDP-binding (G-G-G-T-G-[ST] !8-G) motif SUMMARY #length 448 #molecular-weight 49966 #checksum 6090 SEQUENCE /// ENTRY UBCHA8 #type fragment TITLE tubulin alpha-8 chain - chicken (fragment) ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jun-2000 ACCESSIONS S00472 REFERENCE S00468 !$#authors Pratt, L.F.; Cleveland, D.W. !$#journal EMBO J. (1988) 7:931-940 !$#title A survey of the alpha-tubulin gene family in chicken: !1unexpected sequence heterogeneity in the polypeptides !1encoded by five expressed genes. !$#cross-references MUID:88296435; PMID:3267229 !$#accession S00472 !'##molecule_type DNA !'##residues 1-324 ##label PRA !'##cross-references EMBL:X08064; NID:g63857; PIDN:CAA30853.1; !1PID:g1334749 !'##note the authors translated the codon GTC for residue 1 as Ala COMMENT Tubulin is a dimer of alpha and beta chains. GENETICS !$#introns 227/3 CLASSIFICATION #superfamily tubulin KEYWORDS heterodimer; microtubule FEATURE !$17-23 #region tubulin/FtsZ GTP/GDP-binding (G-G-G-T-G-[ST] !8-G) motif\ !$318 #binding_site polyglutamate (Glu) (covalent) #status !8predicted\ !$323-324 #cleavage_site Glu-Tyr (tubulin-specific !8carboxypeptidase) #status predicted\ !$323-324 #cross-link peptide (Glu-Tyr) (by tubulin-tyrosine !8ligase) #status predicted SUMMARY #length 324 #checksum 448 SEQUENCE /// ENTRY UBCHA4 #type fragment TITLE tubulin alpha-4 chain - chicken (fragment) ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jun-2000 ACCESSIONS S00469 REFERENCE S00468 !$#authors Pratt, L.F.; Cleveland, D.W. !$#journal EMBO J. (1988) 7:931-940 !$#title A survey of the alpha-tubulin gene family in chicken: !1unexpected sequence heterogeneity in the polypeptides !1encoded by five expressed genes. !$#cross-references MUID:88296435; PMID:3267229 !$#accession S00469 !'##molecule_type DNA !'##residues 1-322 ##label PRA !'##cross-references EMBL:X07443; NID:g63850; PIDN:CAA30325.1; !1PID:g1212913 COMMENT Tubulin is a dimer of alpha and beta chains. GENETICS !$#introns 227/3 CLASSIFICATION #superfamily tubulin KEYWORDS heterodimer; microtubule FEATURE !$17-23 #region tubulin/FtsZ GTP/GDP-binding (G-G-G-T-G-[ST] !8-G) motif SUMMARY #length 322 #checksum 6900 SEQUENCE /// ENTRY UBCHA3 #type fragment TITLE tubulin alpha-3 chain - chicken (fragment) ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jun-2000 ACCESSIONS S00468 REFERENCE S00468 !$#authors Pratt, L.F.; Cleveland, D.W. !$#journal EMBO J. (1988) 7:931-940 !$#title A survey of the alpha-tubulin gene family in chicken: !1unexpected sequence heterogeneity in the polypeptides !1encoded by five expressed genes. !$#cross-references MUID:88296435; PMID:3267229 !$#accession S00468 !'##molecule_type DNA !'##residues 1-322 ##label PRA !'##cross-references EMBL:X07442; NID:g63848; PIDN:CAA30324.1; !1PID:g1334747 !'##note the authors translated the codon AGT for residue 5 as Thr and !1AGC for residue 37 as Arg COMMENT Tubulin is a dimer of alpha and beta chains. CLASSIFICATION #superfamily tubulin KEYWORDS heterodimer; microtubule FEATURE !$17-23 #region tubulin/FtsZ GTP/GDP-binding (G-G-G-T-G-[ST] !8-G) motif SUMMARY #length 322 #checksum 6846 SEQUENCE /// ENTRY UBUTA #type complete TITLE tubulin alpha chain - Trypanosoma brucei rhodesiense ORGANISM #formal_name Trypanosoma brucei rhodesiense DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 22-Jun-1999 ACCESSIONS A02970 REFERENCE A91524 !$#authors Kimmel, B.E.; Samson, S.; Wu, J.; Hirschberg, R.; Yarbrough, !1L.R. !$#journal Gene (1985) 35:237-248 !$#title Tubulin genes of the African trypanosome Trypanosoma brucei !1rhodesiense: nucleotide sequence of a 3.7-kb fragment !1containing genes for alpha and beta tubulins. !$#cross-references MUID:86006273; PMID:4043732 !$#accession A02970 !'##molecule_type DNA !'##residues 1-451 ##label KIM !'##cross-references GB:K02836; NID:g162318; PIDN:AAA30262.1; !1PID:g162320 COMMENT Most of the tubulin genes of this trypanosome are contained !1in tandemly repeated units; although they appear to have the !1potential for expression, it is difficult to determine !1whether a specific gene is expressed. CLASSIFICATION #superfamily tubulin KEYWORDS heterodimer; microtubule FEATURE !$142-148 #region tubulin/FtsZ GTP/GDP-binding (G-G-G-T-G-[ST] !8-G) motif\ !$445 #binding_site polyglutamate (Glu) (covalent) #status !8predicted\ !$450-451 #cleavage_site Glu-Tyr (tubulin-specific !8carboxypeptidase) #status predicted\ !$450-451 #cross-link peptide (Glu-Tyr) (by tubulin-tyrosine !8ligase) #status predicted SUMMARY #length 451 #molecular-weight 49787 #checksum 869 SEQUENCE /// ENTRY UBFYA #type fragment TITLE tubulin alpha-1 chain - slime mold (Physarum polycephalum) (fragment) ORGANISM #formal_name Physarum polycephalum DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 22-Jun-1999 ACCESSIONS A02971 REFERENCE A02971 !$#authors Krammer, G.; Singhofer-Wowra, M.; Seedorf, K.; Little, M.; !1Schedl, T. !$#journal J. Mol. Biol. (1985) 183:633-638 !$#title A plasmodial alpha-tubulin cDNA from Physarum polycephalum. !1Nucleotide sequence and comparative analysis. !$#cross-references MUID:85264815; PMID:4020874 !$#accession A02971 !'##molecule_type mRNA !'##residues 1-423 ##label KRA !'##cross-references GB:X02625; NID:g3248; PIDN:CAA26477.1; PID:g3249 COMMENT The source of this protein was the multinucleated plasmodium !1of the slime mold. At least two alpha tubulin genes are !1expressed in the plasmodium. COMMENT Mitosis in the slime mold plasmodium differs from the !1process in many eukaryotes. The tubulin chains must be !1transported to the nuclei for intranuclear assembly of the !1spindle. CLASSIFICATION #superfamily tubulin KEYWORDS heterodimer; microtubule FEATURE !$142-148 #region tubulin/FtsZ GTP/GDP-binding (G-G-G-T-G-[ST] !8-G) motif SUMMARY #length 423 #checksum 9301 SEQUENCE /// ENTRY UBMUAM #type complete TITLE tubulin alpha-1 chain - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 04-Oct-1996 ACCESSIONS JA0062 REFERENCE JA0062 !$#authors Ludwig, S.R.; Oppenheimer, D.G.; Silflow, C.D.; Snustad, !1D.P. !$#journal Plant Mol. Biol. (1988) 10:311-321 !$#title The alpha 1-tubulin gene of Arabidopsis thaliana: primary !1structure and preferential expression in flowers. !$#accession JA0062 !'##molecule_type DNA !'##residues 1-450 ##label LUD GENETICS !$#introns 38/2; 110/1; 176/3; 346/2 CLASSIFICATION #superfamily tubulin KEYWORDS heterodimer; microtubule FEATURE !$142-148 #region tubulin/FtsZ GTP/GDP-binding (G-G-G-T-G-[ST] !8-G) motif SUMMARY #length 450 #molecular-weight 49800 #checksum 7575 SEQUENCE /// ENTRY UBHU5B #type complete TITLE tubulin beta chain - human ALTERNATE_NAMES 5-beta tubulin ORGANISM #formal_name Homo sapiens #common_name man DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 22-Jun-1999 ACCESSIONS A02972 REFERENCE A02972 !$#authors Lee, M.G.S.; Loomis, C.; Cowan, N.J. !$#journal Nucleic Acids Res. (1984) 12:5823-5836 !$#title Sequence of an expressed human beta-tubulin gene containing !1ten Alu family members. !$#cross-references MUID:84272256; PMID:6462917 !$#accession A02972 !'##molecule_type DNA !'##residues 1-444 ##label LEE !'##cross-references GB:X00734; NID:g35958; PIDN:CAA25318.1; PID:g35959 !'##note the authors translated the codon AAT for residue 58 as Lys and !1ATG for residue 155 as Ile COMMENT Tubulin is a dimer of alpha and beta chains and is found in !1the microtubules of all eukaryote cells. It binds (by !1homology with the bovine sequence) ATP on its alpha chain !1and GTP at an exchangeable site on its beta chain and at a !1nonexchangeable site not yet identified. COMMENT The highly acidic carboxyl-terminal region may bind cations !1such as calcium. COMMENT Although the majority of the human beta tubulin genes are !1pseudogenes lacking introns, proteins encoded by at least !1two beta genes are known to be expressed. Although both !1isotypes can be expressed in the same cell, it is not known !1if both are assembled into the same microtubule. GENETICS !$#gene GDB:TUBB !'##cross-references GDB:119622; OMIM:191130 !$#map_position 6p21.3-6p21.3 !$#introns 19/3; 56/1; 93/1 CLASSIFICATION #superfamily tubulin KEYWORDS microtubule FEATURE !$140-146 #region tubulin/FtsZ GTP/GDP-binding (G-G-G-T-G-[ST] !8-G) motif SUMMARY #length 444 #molecular-weight 49631 #checksum 2399 SEQUENCE /// ENTRY UBPGB #type complete TITLE tubulin beta chain - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 18-Dec-1981 #sequence_revision 18-Dec-1981 #text_change 07-May-1999 ACCESSIONS A02973; A31984; S29192 REFERENCE A93878 !$#authors Krauhs, E.; Little, M.; Kempf, T.; Hofer-Warbinek, R.; Ade, !1W.; Ponstingl, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:4156-4160 !$#title Complete amino acid sequence of beta-tubulin from porcine !1brain. !$#cross-references MUID:82037798; PMID:6945576 !$#accession A02973 !'##molecule_type protein !'##residues 1-445 ##label KRA !'##note pig brain contains at least two forms of this protein; a !1peptide corresponding to residues 47-58 and having 48-Ser, !155-Ser, 56-Ser, and 57-His was isolated. 37-Val and 275-Ala !1were also found REFERENCE A90072 !$#authors Zabrecky, J.R.; Cole, R.D. !$#journal Arch. Biochem. Biophys. (1983) 225:475-481 !$#title Localization of the ATP binding site on alpha-tubulin. !$#cross-references MUID:84022547; PMID:6688710 !$#contents annotation; guanine nucleotide binding sites REFERENCE A58110 !$#authors Hesse, J.; Thierauf, M.; Ponsting, H. !$#journal J. Biol. Chem. (1987) 262:15472-15475 !$#title Tubulin sequence region beta155-174 is involved in binding !1exchangeable guanosine triphosphate. !$#cross-references MUID:88058878; PMID:3680207 !$#contents annotation; exchangeable guanine nucleotide binding site !$#note photoaffinity labelling and antibodies to synthetic peptides !1demonstrated the contribution of the region 155-174 to !1guanine nucleotide binding; based on their own and cited !1evidence, the authors suggest that region 63-77 may bind to !1the purine moiety, 155-174 to the ribose, while 137-146 may !1serve as a triphosphate binding loop or, more likely, !1regulate the access to the binding site REFERENCE A31984 !$#authors Linse, K.; Mandelkow, E.M. !$#journal J. Biol. Chem. (1988) 263:15205-15210 !$#title The GTP-binding peptide of beta-tubulin. Localization by !1direct photoaffinity labeling and comparison with !1nucleotide-binding proteins. !$#cross-references MUID:89008408; PMID:3170578 !$#accession A31984 !'##molecule_type protein !'##residues 63-77 ##label LIN REFERENCE S29191 !$#authors Ruediger, M.; Plessman, U.; Kloeppel, K.D.; Wehland, J.; !1Weber, K. !$#journal FEBS Lett. (1992) 308:101-105 !$#title Class II tubulin, the major brain beta tubulin isotype is !1polyglutamylated on glutamic acid residue 435. !$#cross-references MUID:92354756; PMID:1379548 !$#accession S29192 !'##molecule_type protein !'##residues 1-11,'X',13-15;154-162;216-225;434-439,'EG',442-444 ##label !1RUE !'##note 7-Leu was also found COMMENT Tubulin is found in the microtubules of eukaryote cells. It !1binds ATP on its alpha chain and GTP both at an exchangeable !1site on its beta chain and at a nonexchangeable site not yet !1identified. COMMENT The highly acidic carboxyl-terminal region may bind cations !1such as calcium. COMPLEX heterodimer of alpha (see PIR:UBPGA) and beta chains CLASSIFICATION #superfamily tubulin KEYWORDS GTP binding; heterodimer; microtubule FEATURE !$63-77,137-146, !$155-174 #region exchangeable (E) GTP binding site\ !$140-146 #region tubulin/FtsZ GTP/GDP-binding (G-G-G-T-G-[ST] !8-G) motif\ !$435 #binding_site polyglutamate (Glu) (covalent) #status !8experimental SUMMARY #length 445 #molecular-weight 49861 #checksum 4439 SEQUENCE /// ENTRY UBCHB #type complete TITLE tubulin beta chain, embryonic - chicken ALTERNATE_NAMES tubulin beta-2 ORGANISM #formal_name Gallus gallus #common_name chicken DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 24-Sep-1999 ACCESSIONS A02974; I50436 REFERENCE A93246 !$#authors Valenzuela, P.; Quiroga, M.; Zaldivar, J.; Rutter, W.J.; !1Kirschner, M.W.; Cleveland, D.W. !$#journal Nature (1981) 289:650-655 !$#title Nucleotide and corresponding amino acid sequences encoded by !1alpha and beta tubulin mRNAs. !$#cross-references MUID:81123093; PMID:7464932 !$#accession A02974 !'##molecule_type mRNA !'##residues 1-445 ##label VAL !'##cross-references GB:J00913; NID:g212839; PIDN:AAA49123.1; !1PID:g212840 REFERENCE I50435 !$#authors Sullivan, K.F.; Lau, J.T.Y.; Cleveland, D.W. !$#journal Mol. Cell. Biol. (1985) 5:2454-2465 !$#title Apparent gene conversion between beta-tubulin genes yields !1multiple regulatory pathways for a single beta-tubulin !1polypeptide isotype. !$#cross-references MUID:86284689; PMID:3837190 !$#accession I50436 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-445 ##label SUL !'##cross-references GB:M11443; NID:g212843; PIDN:AAA49125.1; !1PID:g212844 CLASSIFICATION #superfamily tubulin KEYWORDS microtubule FEATURE !$140-146 #region tubulin/FtsZ GTP/GDP-binding (G-G-G-T-G-[ST] !8-G) motif SUMMARY #length 445 #molecular-weight 49953 #checksum 4775 SEQUENCE /// ENTRY UBURB #type fragment TITLE tubulin beta chain - sea urchin (Lytechinus pictus) (fragment) ORGANISM #formal_name Lytechinus pictus #common_name painted urchin DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 22-Jun-1999 ACCESSIONS A02975; B02975 REFERENCE A92958 !$#authors Alexandraki, D.; Ruderman, J.V. !$#journal J. Mol. Evol. (1983) 19:397-410 !$#title Evolution of alpha- and beta-tubulin genes as inferred by !1the nucleotide sequence of sea urchin cDNA clones. !$#cross-references MUID:84090258; PMID:6317873 !$#accession A02975 !'##molecule_type mRNA !'##residues 1-177 ##label ALE !'##cross-references GB:M32427; NID:g1162987; PIDN:AAA85475.1; !1PID:g1162988 !'##experimental_source clone p-beta-3 !$#accession B02975 !'##molecule_type mRNA !'##residues 80-172,'E',173-177 ##label AL2 !'##cross-references GB:M32431; NID:g1162983; PIDN:AAA85473.1; !1PID:g1162984 !'##experimental_source clone p-beta-1 CLASSIFICATION #superfamily tubulin KEYWORDS microtubule SUMMARY #length 177 #checksum 5198 SEQUENCE /// ENTRY UBUTB #type complete TITLE tubulin beta chain - Trypanosoma brucei rhodesiense ORGANISM #formal_name Trypanosoma brucei rhodesiense DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 22-Jun-1999 ACCESSIONS A02976 REFERENCE A91524 !$#authors Kimmel, B.E.; Samson, S.; Wu, J.; Hirschberg, R.; Yarbrough, !1L.R. !$#journal Gene (1985) 35:237-248 !$#title Tubulin genes of the African trypanosome Trypanosoma brucei !1rhodesiense: nucleotide sequence of a 3.7-kb fragment !1containing genes for alpha and beta tubulins. !$#cross-references MUID:86006273; PMID:4043732 !$#accession A02976 !'##molecule_type DNA !'##residues 1-442 ##label KIM !'##cross-references GB:K02836; NID:g162318; PIDN:AAA30261.1; !1PID:g162319 COMMENT Most of the tubulin genes of this trypanosome are contained !1in tandemly repeated units; although they appear to have the !1potential for expression, it is difficult to determine !1whether a specific gene is expressed. CLASSIFICATION #superfamily tubulin KEYWORDS microtubule FEATURE !$140-146 #region tubulin/FtsZ GTP/GDP-binding (G-G-G-T-G-[ST] !8-G) motif SUMMARY #length 442 #molecular-weight 49704 #checksum 3499 SEQUENCE /// ENTRY UBZQF #type complete TITLE tubulin beta chain - malaria parasite (Plasmodium falciparum) ORGANISM #formal_name Plasmodium falciparum DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 09-Jun-2000 ACCESSIONS S07460 REFERENCE S07460 !$#authors Delves, C.J.; Ridley, R.G.; Goman, M.; Holloway, S.P.; Hyde, !1J.E.; Scaife, J.G. !$#journal Mol. Microbiol. (1989) 3:1511-1519 !$#title Cloning of a beta-tubulin gene from Plasmodium falciparum. !$#cross-references MUID:90136081; PMID:2693902 !$#accession S07460 !'##molecule_type DNA !'##residues 1-445 ##label DEL !'##cross-references EMBL:X16075; NID:g9981; PIDN:CAA34207.1; !1PID:g295762 GENETICS !$#introns 32/3; 350/2 CLASSIFICATION #superfamily tubulin KEYWORDS GTP binding; heterodimer; microtubule FEATURE !$140-146 #region tubulin/FtsZ GTP/GDP-binding (G-G-G-T-G-[ST] !8-G) motif SUMMARY #length 445 #molecular-weight 49751 #checksum 1858 SEQUENCE /// ENTRY UBMUBM #type complete TITLE tubulin beta-1 chain - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 22-Jun-1999 ACCESSIONS JT0275 REFERENCE JT0275 !$#authors Oppenheimer, D.G.; Haas, N.; Silflow, C.D.; Snustad, D.P. !$#journal Gene (1988) 63:87-102 !$#title The beta-tubulin gene family of Arabidopsis thaliana: !1preferential accumulation of the beta-1 transcript in roots. !$#cross-references MUID:88255862; PMID:3384336 !$#accession JT0275 !'##molecule_type DNA !'##residues 1-447 ##label OPP !'##cross-references GB:M20405; NID:g166921; PIDN:AAA32893.1; !1PID:g166922 !'##note the genome of A. thaliana contains a beta-tubulin gene family !1consisting of at least seven distinct genes and/or !1pseudogenes !'##note the transcript of this beta-1 tubulin gene accumulates !1predominantly in roots GENETICS !$#introns 133/1; 223/1 CLASSIFICATION #superfamily tubulin KEYWORDS microtubule FEATURE !$141-147 #region tubulin/FtsZ GTP/GDP-binding (G-G-G-T-G-[ST] !8-G) motif SUMMARY #length 447 #molecular-weight 50217 #checksum 3159 SEQUENCE /// ENTRY UBKM #type complete TITLE tubulin beta chain - Chlamydomonas reinhardtii ORGANISM #formal_name Chlamydomonas reinhardtii DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 22-Jun-1999 ACCESSIONS A29141 REFERENCE A29141 !$#authors Youngblom, J.; Schloss, J.A.; Silflow, C.D. !$#journal Mol. Cell. Biol. (1984) 4:2686-2696 !$#title The two beta-tubulin genes of Chlamydomonas reinhardtii code !1for identical proteins. !$#cross-references MUID:85137460; PMID:6098820 !$#accession A29141 !'##molecule_type DNA !'##residues 1-443 ##label YOU !'##cross-references GB:K03281; NID:g167457; PIDN:AAA33102.1; !1PID:g167458 COMMENT Tubulin, a dimer of alpha and beta chains, is the major !1constituent of microtubules. It binds two moles of GTP, one !1at an exchangeable site on the beta chain and one at a !1nonexchangeable site on the alpha-chain. Two beta-tubulin !1genes (beta-1 and beta-2) of Chlamydomonas are found to !1encode the same protein. GENETICS !$#introns 8/3; 57/1; 132/1 CLASSIFICATION #superfamily tubulin KEYWORDS GTP binding; microtubule FEATURE !$140-146 #region tubulin/FtsZ GTP/GDP-binding (G-G-G-T-G-[ST] !8-G) motif SUMMARY #length 443 #molecular-weight 49619 #checksum 6709 SEQUENCE /// ENTRY UBBYB #type complete TITLE tubulin beta chain - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein R002; protein YFL037w ORGANISM #formal_name Saccharomyces cerevisiae DATE 03-Aug-1984 #sequence_revision 19-Oct-1995 #text_change 21-Jul-2000 ACCESSIONS S56217; A02977; S60499 REFERENCE S56186 !$#authors Murakami, Y.; Naitou, M.; Hagiwara, H.; Shibata, T.; Ozawa, !1M.; Sasanuma, S.I.; Sasanuma, M.; Tsuchiya, Y.; Soeda, E.; !1Yokoyama, K.; Yamazaki, M.; Tashiro, H.; Eki, T. !$#submission submitted to the EMBL Data Library, May 1995 !$#description Analysis of the nucleotide sequence of chromosome VI from !1Saccaromyces cerevisiae. !$#accession S56217 !'##molecule_type DNA !'##residues 1-457 ##label MUR !'##cross-references EMBL:D50617; NID:g836685; PIDN:BAA09202.1; !1PID:g836717; GSPDB:GN00006; MIPS:YFL037w REFERENCE A02977 !$#authors Neff, N.F.; Thomas, J.H.; Grisafi, P.; Botstein, D. !$#journal Cell (1983) 33:211-219 !$#title Isolation of the beta-tubulin gene from yeast and !1demonstration of its essential function in vivo. !$#cross-references MUID:84282671; PMID:6380751 !$#accession A02977 !'##molecule_type DNA !'##residues 1-8,'A',10-11,'Y',13-70,'W',72-151,'F',153-155,'K',157-158, !1'L',160-457 ##label NEF !'##cross-references EMBL:V01296; NID:g3434; PIDN:CAA24603.1; PID:g3435 !'##note the authors translated the codon TAC for residue 422 as Trp REFERENCE S60495 !$#authors Naitou, M.; Ozawa, M.; Sasanuma, S.I.; Kobayashi, M.; !1Hagiwara, H.; Shibata, T.; Hanaoka, F.; Watanabe, K.; Ono, !1A.; Yamazaki, M.; Tashiro, H.; Eki, T.; Murakami, Y. !$#journal Yeast (1995) 11:1525-1532 !$#title Sequencing of an 18.8 kb fragment from Saccharomyces !1cerevisiae chromosome VI. !$#cross-references MUID:96353435; PMID:8750241 !$#accession S60499 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-457 ##label NAI !'##cross-references EMBL:D44598; NID:g871933; PIDN:BAA08027.1; !1PID:g871936 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1994 GENETICS !$#gene SGD:TUB2; MIPS:YFL037w !'##cross-references SGD:S0001857; MIPS:YFL037w !$#map_position 6L CLASSIFICATION #superfamily tubulin KEYWORDS microtubule FEATURE !$140-146 #region tubulin/FtsZ GTP/GDP-binding (G-G-G-T-G-[ST] !8-G) motif SUMMARY #length 457 #molecular-weight 50922 #checksum 5466 SEQUENCE /// ENTRY UBCKBA #type complete TITLE tubulin beta chain - yeast (Candida albicans) ORGANISM #formal_name Candida albicans DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 22-Jun-1999 ACCESSIONS JT0276 REFERENCE JT0276 !$#authors Smith, H.A.; Allaudeen, H.S.; Whitman, M.H.; Koltin, Y.; !1Gorman, J.A. !$#journal Gene (1988) 63:53-63 !$#title Isolation and characterization of a beta-tubulin gene from !1Candida albicans. !$#cross-references MUID:88255859; PMID:3290053 !$#accession JT0276 !'##molecule_type DNA !'##residues 1-449 ##label SMI !'##cross-references GB:M19398; NID:g170937; PIDN:AAA34375.1; !1PID:g170938 GENETICS !$#gene TUB2 !$#introns 4/3; 16/3 CLASSIFICATION #superfamily tubulin KEYWORDS microtubule FEATURE !$140-146 #region tubulin/FtsZ GTP/GDP-binding (G-G-G-T-G-[ST] !8-G) motif SUMMARY #length 449 #molecular-weight 49942 #checksum 881 SEQUENCE /// ENTRY UBHUG #type complete TITLE tubulin gamma chain - human ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 22-Jun-1999 ACCESSIONS A39527 REFERENCE A39527 !$#authors Zheng, Y.; Jung, M.K.; Oakley, B.R. !$#journal Cell (1991) 65:817-823 !$#title Gamma-tubulin is present in Drosophila melanogaster and Homo !1sapiens and is associated with the centrosome. !$#cross-references MUID:91249388; PMID:1904010 !$#accession A39527 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-451 ##label ZHE !'##cross-references GB:M61764; NID:g183702; PIDN:AAA52620.1; !1PID:g183703 COMMENT This protein is a component of the centrosome that may play !1a role in microtubule organization. GENETICS !$#gene GDB:TUBG !'##cross-references GDB:128600; OMIM:191135 !$#map_position 13q13-13q14.1 CLASSIFICATION #superfamily tubulin KEYWORDS GTP binding; microtubule SUMMARY #length 451 #molecular-weight 51198 #checksum 4164 SEQUENCE /// ENTRY UBXLG #type complete TITLE tubulin gamma chain - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 22-Jun-1999 ACCESSIONS A39528 REFERENCE A39528 !$#authors Stearns, T.; Evans, L.; Kirschner, M. !$#journal Cell (1991) 65:825-836 !$#title Gamma-tubulin is a highly conserved component of the !1centrosome. !$#cross-references MUID:91249389; PMID:1840506 !$#accession A39528 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-451 ##label STE !'##cross-references GB:M63446; NID:g214164; PIDN:AAA49720.1; !1PID:g214165 COMMENT This protein is a component of the centrosome that may play !1a role in microtubule organization. GENETICS !$#gene Xgam CLASSIFICATION #superfamily tubulin KEYWORDS GTP binding; microtubule SUMMARY #length 451 #molecular-weight 51167 #checksum 4011 SEQUENCE /// ENTRY UBFFG #type complete TITLE tubulin gamma chain - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 21-Jun-2002 ACCESSIONS B39527 REFERENCE A39527 !$#authors Zheng, Y.; Jung, M.K.; Oakley, B.R. !$#journal Cell (1991) 65:817-823 !$#title Gamma-tubulin is present in Drosophila melanogaster and Homo !1sapiens and is associated with the centrosome. !$#cross-references MUID:91249388; PMID:1904010 !$#accession B39527 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-475 ##label ZHE !'##cross-references GB:M61765; NID:g157569; PIDN:AAA28597.1; !1PID:g157570 COMMENT This protein is a component of the centrosome that may play !1a role in microtubule organization. GENETICS !$#gene FlyBase:yem-alpha !'##cross-references FlyBase:FBgn0004176 CLASSIFICATION #superfamily tubulin KEYWORDS GTP binding; microtubule SUMMARY #length 475 #molecular-weight 53311 #checksum 7707 SEQUENCE /// ENTRY UBZPG #type complete TITLE tubulin gamma chain - fission yeast (Schizosaccharomyces pombe) ORGANISM #formal_name Schizosaccharomyces pombe DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 28-Jan-2000 ACCESSIONS B39528; S23327; T40228 REFERENCE A39528 !$#authors Stearns, T.; Evans, L.; Kirschner, M. !$#journal Cell (1991) 65:825-836 !$#title Gamma-tubulin is a highly conserved component of the !1centrosome. !$#cross-references MUID:91249389; PMID:1840506 !$#accession B39528 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-446 ##label STE !'##cross-references GB:M63447; NID:g173389; PIDN:AAA35305.1; !1PID:g173390 !'##note the sequence shown follows the authors' translation, which is !1inconsistent at residue 17 with the nucleotide sequence !1submitted to Genbank REFERENCE S23327 !$#authors Horio, T.; Uzawa, S.; Jung, M.K.; Oakley, B.R.; Tanaka, K.; !1Yanagida, M. !$#journal J. Cell Sci. (1991) 99:693-700 !$#title The fission yeast gamma-tubulin is essential for mitosis and !1is localized at microtubule organizing centers. !$#cross-references MUID:92121241; PMID:1770000 !$#accession S23327 !'##status preliminary !'##molecule_type DNA !'##residues 1-446 ##label HOR !'##cross-references EMBL:X62031; NID:g4955; PIDN:CAA43976.1; PID:g4956 REFERENCE Z21915 !$#authors Moreno, S.; Wood, V.; Rajandream, M.A.; Barrell, B.G. !$#submission submitted to the EMBL Data Library, June 1998 !$#accession T40228 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-446 ##label MOR !'##cross-references EMBL:AL023796; PIDN:CAA19365.1; GSPDB:GN00067; !1SPDB:SPBC32F12.04 !'##experimental_source strain 972h-; cosmid c32F12 COMMENT This protein is a component of the centrosome that may play !1a role in microtubule organization. GENETICS STE1 !$#gene tug1+ !$#introns 17/3; 54/3; 72/3; 231/3; 356/3; 425/3 GENETICS MOR1 !$#gene SPBC32F12.04 !$#map_position 2 !$#introns 17/1; 54/3; 72/3; 231/3; 386/3; 425/2 CLASSIFICATION #superfamily tubulin KEYWORDS GTP binding; microtubule SUMMARY #length 446 #molecular-weight 49965 #checksum 9004 SEQUENCE /// ENTRY A38905 #type complete TITLE dynein heavy chain, cytosolic - rat CONTAINS dynein ATPase (EC 3.6.4.2) ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 15-Apr-1994 #sequence_revision 02-May-1994 #text_change 19-Apr-2002 ACCESSIONS A38905; I58139 REFERENCE A38905 !$#authors Zhang, Z.; Tanaka, Y.; Nonaka, S.; Aizawa, H.; Kawasaki, H.; !1Nakata, T.; Hirokawa, N. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:7928-7932 !$#title The primary structure of rat brain (cytoplasmic) dynein !1heavy chain, a cytoplasmic motor enzyme. !$#cross-references MUID:93376715; PMID:7690137 !$#accession A38905 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-4644 ##label ZHA !'##cross-references GB:D13896; NID:g402527; PIDN:BAA02996.1; !1PID:g402528 REFERENCE I58139 !$#authors Mikami, A.; Paschal, B.M.; Mazumdar, M.; Vallee, R.B. !$#journal Neuron (1993) 10:787-796 !$#title Molecular cloning of the retrograde transport motor !1cytoplasmic dynein MAP 1C. !$#cross-references MUID:93264075; PMID:7684232 !$#accession I58139 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-1023,'MP',1026-1771,'D',1773-2097,'A',2099-2138,'V', !12140-2174,'A',2176-2184,'Q',2186-2365,'V',2367-2381,'S', !12383-2462,'A',2464-3218,'D',3220-4130,'K',4132-4365,'S', !14367-4510,'G',4512-4644 ##label RES !'##cross-references GB:L08505; NID:g294542; PIDN:AAA41103.1; !1PID:g294543 CLASSIFICATION #superfamily dynein heavy chain, cytosolic KEYWORDS ATP; blocked amino end; heterotetramer; hydrolase; !1microtubule binding; nucleotide binding; P-loop FEATURE !$1904-1911 #region nucleotide-binding motif A (P-loop)\ !$2222-2229 #region nucleotide-binding motif A (P-loop)\ !$2593-2600 #region nucleotide-binding motif A (P-loop)\ !$2935-2942 #region nucleotide-binding motif A (P-loop)\ !$1910 #binding_site ATP (Lys) #status predicted\ !$2228 #binding_site ATP (Lys) #status predicted\ !$2599 #binding_site ATP (Lys) #status predicted\ !$2941 #binding_site ATP (Lys) #status predicted SUMMARY #length 4644 #molecular-weight 532247 #checksum 1141 SEQUENCE /// ENTRY A54794 #type complete TITLE dynein heavy chain, cytosolic - fruit fly (Drosophila melanogaster) CONTAINS dynein ATPase (EC 3.6.4.2) ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS A54794 REFERENCE A54794 !$#authors Li, M.; McGrail, M.; Serr, M.; Hays, T.S. !$#journal J. Cell Biol. (1994) 126:1475-1494 !$#title Drosophila cytoplasmic dynein, a microtubule motor that is !1asymmetrically localized in the oocyte. !$#cross-references MUID:94375524; PMID:8089180 !$#accession A54794 !'##molecule_type mRNA !'##residues 1-4639 ##label LIA !'##cross-references GB:L23195; NID:g349668; PIDN:AAA60323.1; !1PID:g349669 GENETICS !$#gene FlyBase:Dhc64C !'##cross-references FlyBase:FBgn0010349 CLASSIFICATION #superfamily dynein heavy chain, cytosolic KEYWORDS ATP; heterotetramer; hydrolase; microtubule binding; !1nucleotide binding; P-loop FEATURE !$1895-1902 #region nucleotide-binding motif A (P-loop)\ !$2210-2217 #region nucleotide-binding motif A (P-loop)\ !$2580-2587 #region nucleotide-binding motif A (P-loop)\ !$2922-2929 #region nucleotide-binding motif A (P-loop)\ !$1901 #binding_site ATP (Lys) #status predicted\ !$2216 #binding_site ATP (Lys) #status predicted\ !$2586 #binding_site ATP (Lys) #status predicted\ !$2928 #binding_site ATP (Lys) #status predicted SUMMARY #length 4639 #molecular-weight 530160 #checksum 7956 SEQUENCE /// ENTRY A44357 #type complete TITLE dynein heavy chain, cytosolic - slime mold (Dictyostelium discoideum) CONTAINS dynein ATPase (EC 3.6.4.2) ORGANISM #formal_name Dictyostelium discoideum DATE 03-Feb-1994 #sequence_revision 02-May-1994 #text_change 19-Apr-2002 ACCESSIONS A44357; S28504 REFERENCE A44357 !$#authors Koonce, M.P.; Grissom, P.M.; McIntosh, J.R. !$#journal J. Cell Biol. (1992) 119:1597-1604 !$#title Dynein from Dictyostelium: primary structure comparisons !1between a cytoplasmic motor enzyme and flagellar dynein. !$#cross-references MUID:93107159; PMID:1469051 !$#accession A44357 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-4725 ##label KOO !'##cross-references EMBL:Z15124; NID:g7226; PIDN:CAA78827.1; PID:g7227 !'##note sequence extracted from NCBI backbone (NCBIP:121195) CLASSIFICATION #superfamily dynein heavy chain, cytosolic KEYWORDS ATP; heterotetramer; hydrolase; microtubule binding; !1nucleotide binding; P-loop FEATURE !$1969-1976 #region nucleotide-binding motif A (P-loop)\ !$2271-2278 #region nucleotide-binding motif A (P-loop)\ !$2669-2676 #region nucleotide-binding motif A (P-loop)\ !$3011-3018 #region nucleotide-binding motif A (P-loop)\ !$1975 #binding_site ATP (Lys) #status predicted\ !$2277 #binding_site ATP (Lys) #status predicted\ !$2675 #binding_site ATP (Lys) #status predicted\ !$3017 #binding_site ATP (Lys) #status predicted SUMMARY #length 4725 #molecular-weight 538814 #checksum 4652 SEQUENCE /// ENTRY S38128 #type complete TITLE dynein heavy chain, cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YKR054c CONTAINS dynein ATPase (EC 3.6.4.2) ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S38128; S38130; S37701; S43936; S43077 REFERENCE S38118 !$#authors Vissers, S.; Urrestarazu, L.A.; Jauniaux, J.C. !$#submission submitted to the Protein Sequence Database, March 1994 !$#accession S38128 !'##molecule_type DNA !'##residues 1-4092 ##label VIS !'##cross-references EMBL:Z28279; NID:g486510; PIDN:CAA82132.1; !1PID:g486511; GSPDB:GN00011; MIPS:YKR054c !'##experimental_source strain S288C REFERENCE S38130 !$#authors van Vliet-Reedijk, J.C.; Planta, R.J. !$#submission submitted to the Protein Sequence Database, March 1994 !$#accession S38130 !'##molecule_type DNA !'##residues 1-787 ##label VAN !'##cross-references EMBL:Z28279; GSPDB:GN00011; MIPS:YKR054c REFERENCE S37701 !$#authors Li, Y.Y.; Yeh, E.Y.; Hays, T.; Bloom, K.S. !$#submission submitted to the EMBL Data Library, May 1993 !$#description Disruption of mitotic spindle orientation in a yeast dynein !1mutant. !$#accession S37701 !'##molecule_type DNA !'##residues 1-588,'C',590-600,'A',602-1363,'A',1365-2631,'P',2633-2657, !12659,'IGW',2660-2661 ##label LIY !'##cross-references EMBL:L15626 REFERENCE S43936 !$#authors Eshel, D.; Urrestarazu, L.A.; Vissers, S.; Jauniaux, J.C.; !1van Vliet-Reedijk, J.C.; Planta, R.J.; Gibbons, I.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:11172-11176 !$#title Cytoplasmic dynein is required for normal nuclear !1segregation in yeast. !$#cross-references MUID:94068566; PMID:8248224 !$#accession S43936 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-2117,'IV',2120-4092 ##label ESH !'##cross-references EMBL:Z21877; NID:g439287; PIDN:CAA79923.1; !1PID:g439288 GENETICS !$#gene SGD:DYN1; DHC1; MIPS:YKR054c !'##cross-references SGD:S0001762; MIPS:YKR054c !$#map_position 11R FUNCTION !$#description probably acts in cytoplasmic microtubule-based motile !1processes including vesicle transport, and chromosome !1movements; probably required for normal progression of the !1cell cycle; required for nuclear segregation; required to !1achieve and maintain proper spindle positioning CLASSIFICATION #superfamily dynein heavy chain, cytosolic KEYWORDS ATP; heterotetramer; hydrolase; microtubule binding; !1nucleotide binding; P-loop FEATURE !$1796-1803 #region nucleotide-binding motif A (P-loop)\ !$2074-2081 #region nucleotide-binding motif A (P-loop)\ !$2418-2425 #region nucleotide-binding motif A (P-loop)\ !$2760-2767 #region nucleotide-binding motif A (P-loop)\ !$1802 #binding_site ATP (Lys) #status predicted\ !$2080 #binding_site ATP (Lys) #status predicted\ !$2424 #binding_site ATP (Lys) #status predicted\ !$2766 #binding_site ATP (Lys) #status predicted SUMMARY #length 4092 #molecular-weight 471343 #checksum 4662 SEQUENCE /// ENTRY B54802 #type complete TITLE dynein heavy chain, cytosolic - Neurospora crassa CONTAINS dynein ATPase (EC 3.6.4.2) ORGANISM #formal_name Neurospora crassa DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS B54802 REFERENCE A54802 !$#authors Plamann, M.; Minke, P.F.; Tinsley, J.H.; Bruno, K.S. !$#journal J. Cell Biol. (1994) 127:139-149 !$#title Cytoplasmic dynein and actin-related protein Arp1 are !1required for normal nuclear distribution in filamentous !1fungi. !$#cross-references MUID:95014704; PMID:7929559 !$#accession B54802 !'##molecule_type DNA !'##residues 1-4367 ##label PLA !'##cross-references GB:L31504; NID:g473489; PIDN:AAA64908.1; !1PID:g473490 GENETICS !$#introns 104/1; 4205/3 CLASSIFICATION #superfamily dynein heavy chain, cytosolic KEYWORDS ATP; heterotetramer; hydrolase; microtubule binding; !1nucleotide binding; P-loop FEATURE !$1943-1950 #region nucleotide-binding motif A (P-loop)\ !$2240-2247 #region nucleotide-binding motif A (P-loop)\ !$2605-2612 #region nucleotide-binding motif A (P-loop)\ !$2947-2954 #region nucleotide-binding motif A (P-loop)\ !$1949 #binding_site ATP (Lys) #status predicted\ !$2246 #binding_site ATP (Lys) #status predicted\ !$2611 #binding_site ATP (Lys) #status predicted\ !$2953 #binding_site ATP (Lys) #status predicted SUMMARY #length 4367 #molecular-weight 495574 #checksum 8268 SEQUENCE /// ENTRY A53489 #type complete TITLE dynein heavy chain, cytosolic - Emericella nidulans CONTAINS dynein ATPase (EC 3.6.4.2) ORGANISM #formal_name Emericella nidulans, Aspergillus nidulans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS A53489 REFERENCE A53489 !$#authors Xiang, X.; Beckwith, S.M.; Morris, N.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1994) 91:2100-2104 !$#title Cytoplasmic dynein is involved in nuclear migration in !1Aspergillus nidulans. !$#cross-references MUID:94181539; PMID:8134356 !$#accession A53489 !'##molecule_type DNA !'##residues 1-4344 ##label XIA !'##cross-references GB:U03904; NID:g451538; PIDN:AAA18338.1; !1PID:g451539 CLASSIFICATION #superfamily dynein heavy chain, cytosolic KEYWORDS ATP; heterotetramer; hydrolase; microtubule binding; !1nucleotide binding; P-loop FEATURE !$1933-1940 #region nucleotide-binding motif A (P-loop)\ !$2228-2235 #region nucleotide-binding motif A (P-loop)\ !$2592-2599 #region nucleotide-binding motif A (P-loop)\ !$2932-2939 #region nucleotide-binding motif A (P-loop)\ !$1939 #binding_site ATP (Lys) #status predicted\ !$2234 #binding_site ATP (Lys) #status predicted\ !$2598 #binding_site ATP (Lys) #status predicted\ !$2938 #binding_site ATP (Lys) #status predicted SUMMARY #length 4344 #molecular-weight 492476 #checksum 8396 SEQUENCE /// ENTRY S17231 #type complete TITLE dynein beta heavy chain, ciliary - sea urchin (Anthocidaris crassispina) CONTAINS dynein ATPase (EC 3.6.4.2) ORGANISM #formal_name Anthocidaris crassispina DATE 30-Sep-1991 #sequence_revision 02-May-1994 #text_change 19-Apr-2002 ACCESSIONS S17231; PS0415 REFERENCE S17231 !$#authors Ogawa, K. !$#journal Nature (1991) 352:643-645 !$#title Four ATP-binding sites in the midregion of the beta heavy !1chain of dynein. !$#cross-references MUID:91326104; PMID:1830928 !$#accession S17231 !'##molecule_type mRNA !'##residues 1-4466 ##label OGA !'##cross-references GB:D01021; NID:g217202; PIDN:BAA00827.1; !1PID:g217203 REFERENCE PS0415 !$#authors Ogawa, K. !$#journal Proc. Jpn. Acad. B Phys. Biol. Sci. (1991) 67:27-31 !$#title ATP-binding site in dynein beta-heavy chain: identification !1by molecular cloning. !$#accession PS0415 !'##molecule_type mRNA !'##residues 764-1001,'APQ',1005-2036,'VPSSVET' ##label OG2 CLASSIFICATION #superfamily dynein heavy chain, ciliary KEYWORDS ATP; heterotetramer; hydrolase; microtubule binding; !1nucleotide binding; P-loop FEATURE !$154-161 #region nucleotide-binding motif A (P-loop)\ !$1852-1859 #region nucleotide-binding motif A (P-loop)\ !$2133-2140 #region nucleotide-binding motif A (P-loop)\ !$2460-2467 #region nucleotide-binding motif A (P-loop)\ !$2805-2812 #region nucleotide-binding motif A (P-loop)\ !$160 #binding_site ATP (Lys) #status predicted\ !$1858 #binding_site ATP (Lys) #status predicted\ !$2139 #binding_site ATP (Lys) #status predicted\ !$2466 #binding_site ATP (Lys) #status predicted\ !$2811 #binding_site ATP (Lys) #status predicted SUMMARY #length 4466 #molecular-weight 511778 #checksum 6291 SEQUENCE /// ENTRY S17653 #type complete TITLE dynein beta heavy chain, ciliary - sea urchin (Tripneustes gratilla) CONTAINS dynein ATPase (EC 3.6.4.2) ORGANISM #formal_name Tripneustes gratilla DATE 04-Dec-1992 #sequence_revision 02-May-1994 #text_change 19-Apr-2002 ACCESSIONS S17653; S24628 REFERENCE S17653 !$#authors Gibbons, I.R.; Gibbons, B.H.; Mocz, G.; Asai, D.J. !$#journal Nature (1991) 352:640-643 !$#title Multiple nucleotide-binding sites in the sequence of dynein !1beta heavy chain. !$#cross-references MUID:91326103; PMID:1830927 !$#accession S17653 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-4466 ##label GIB1 !'##cross-references EMBL:X59603; NID:g10709; PIDN:CAA42170.1; !1PID:g10710 !$#accession S24628 !'##molecule_type protein !'##residues 162-172;1193-1204;3240-3259;3325-3339 ##label GIB2 CLASSIFICATION #superfamily dynein heavy chain, ciliary KEYWORDS ATP; heterotetramer; hydrolase; microtubule binding; !1nucleotide binding; P-loop FEATURE !$154-161 #region nucleotide-binding motif A (P-loop)\ !$1852-1859 #region nucleotide-binding motif A (P-loop)\ !$2133-2140 #region nucleotide-binding motif A (P-loop)\ !$2460-2467 #region nucleotide-binding motif A (P-loop)\ !$2805-2812 #region nucleotide-binding motif A (P-loop)\ !$1858 #binding_site ATP (Lys) #status predicted\ !$2139 #binding_site ATP (Lys) #status predicted\ !$2466 #binding_site ATP (Lys) #status predicted\ !$2811 #binding_site ATP (Lys) #status predicted SUMMARY #length 4466 #molecular-weight 511777 #checksum 9337 SEQUENCE /// ENTRY A41919 #type complete TITLE kinesin heavy chain - human CONTAINS kinesin ATPase (EC 3.6.1.-) ORGANISM #formal_name Homo sapiens #common_name man DATE 03-Mar-1994 #sequence_revision 03-Mar-1994 #text_change 19-Jan-2001 ACCESSIONS A41919; S24603 REFERENCE A41919 !$#authors Navone, F.; Niclas, J.; Hom-Booher, N.; Sparks, L.; !1Bernstein, H.D.; McCaffrey, G.; Vale, R.D. !$#journal J. Cell Biol. (1992) 117:1263-1275 !$#title Cloning and expression of a human kinesin heavy chain gene: !1interaction of the COOH-terminal domain with cytoplasmic !1microtubules in transfected CV-1 cells. !$#cross-references MUID:92299683; PMID:1607388 !$#accession A41919 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-963 ##label NAV !'##cross-references GB:X65873; NID:g34082; PIDN:CAA46703.1; PID:g34083 GENETICS !$#gene GDB:KNS1; KNS !'##cross-references GDB:135352 CLASSIFICATION #superfamily kinesin heavy chain; kinesin motor domain !1homology KEYWORDS ATP; coiled coil; heterotetramer; hydrolase; microtubule !1binding; nucleotide binding; P-loop FEATURE !$9-331 #domain kinesin motor domain homology #label KMOT\ !$85-92 #region nucleotide-binding motif A (P-loop)\ !$402-860 #domain rod #status predicted #label RDD\ !$861-963 #domain globular #status predicted #label GBD\ !$91 #binding_site ATP (Lys) #status predicted SUMMARY #length 963 #molecular-weight 109684 #checksum 5105 SEQUENCE /// ENTRY A35075 #type complete TITLE kinesin heavy chain - longfin squid CONTAINS kinesin ATPase (EC 3.6.1.-) ORGANISM #formal_name Loligo pealeii #common_name longfin squid DATE 03-Mar-1994 #sequence_revision 03-Mar-1994 #text_change 19-Jan-2001 ACCESSIONS A35075 REFERENCE A35075 !$#authors Kosik, K.S.; Orecchio, L.D.; Schnapp, B.; Inouye, H.; Neve, !1R.L. !$#journal J. Biol. Chem. (1990) 265:3278-3283 !$#title The primary structure and analysis of the squid kinesin !1heavy chain. !$#cross-references MUID:90153980; PMID:2137456 !$#accession A35075 !'##molecule_type mRNA !'##residues 1-967 ##label KOS !'##cross-references GB:J05258; NID:g460682; PIDN:AAA29990.1; !1PID:g161290 CLASSIFICATION #superfamily kinesin heavy chain; kinesin motor domain !1homology KEYWORDS ATP; coiled coil; heterotetramer; hydrolase; methylated !1amino acid; microtubule binding; nucleotide binding; P-loop; !1phosphoprotein FEATURE !$9-332 #domain kinesin motor domain homology #label KMOT\ !$85-92 #region nucleotide-binding motif A (P-loop)\ !$392-861 #domain rod #status predicted #label RDD\ !$862-967 #domain globular #status predicted #label GBD\ !$27,174,206 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$32 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8predicted\ !$91 #binding_site ATP (Lys) #status predicted\ !$546 #binding_site phosphate (Thr) (covalent) #status !8predicted SUMMARY #length 967 #molecular-weight 109407 #checksum 5824 SEQUENCE /// ENTRY A31497 #type complete TITLE kinesin heavy chain - fruit fly (Drosophila melanogaster) CONTAINS kinesin ATPase (EC 3.6.1.-) ORGANISM #formal_name Drosophila melanogaster DATE 03-Mar-1994 #sequence_revision 03-Mar-1994 #text_change 19-Jan-2001 ACCESSIONS A31497 REFERENCE A31497 !$#authors Yang, J.T.; Laymon, R.A.; Goldstein, L.S.B. !$#journal Cell (1989) 56:879-889 !$#title A three-domain structure of kinesin heavy chain revealed by !1DNA sequence and microtubule binding analyses. !$#cross-references MUID:89168428; PMID:2522352 !$#accession A31497 !'##molecule_type mRNA !'##residues 1-975 ##label YAN !'##cross-references GB:M24441; NID:g157777; PIDN:AAA28652.1; !1PID:g157778 GENETICS !$#gene FlyBase:Khc !'##cross-references FlyBase:FBgn0001308 CLASSIFICATION #superfamily kinesin heavy chain; kinesin motor domain !1homology KEYWORDS ATP; coiled coil; heterotetramer; hydrolase; microtubule !1binding; nucleotide binding; P-loop FEATURE !$13-339 #domain kinesin motor domain homology #label KMOT\ !$92-99 #region nucleotide-binding motif A (P-loop)\ !$399-883 #domain rod #status predicted #label RDD\ !$884-975 #domain globular #status predicted #label GBD\ !$98 #binding_site ATP (Lys) #status predicted SUMMARY #length 975 #molecular-weight 110429 #checksum 9224 SEQUENCE /// ENTRY A38713 #type complete TITLE kinesin heavy chain - sea urchin (Strongylocentrotus purpuratus) CONTAINS kinesin ATPase (EC 3.6.1.-) ORGANISM #formal_name Strongylocentrotus purpuratus #common_name purple urchin DATE 03-Mar-1994 #sequence_revision 03-Mar-1994 #text_change 19-Jan-2001 ACCESSIONS A38713; S24308 REFERENCE A38713 !$#authors Wright, B.D.; Henson, J.H.; Wedaman, K.P.; Willy, P.J.; !1Morand, J.N.; Scholey, J.M. !$#journal J. Cell Biol. (1991) 113:817-833 !$#title Subcellular localization and sequence of sea urchin kinesin !1heavy chain: evidence for its association with membranes in !1the mitotic apparatus and interphase cytoplasm. !$#cross-references MUID:91225077; PMID:1827446 !$#accession A38713 !'##molecule_type mRNA !'##residues 1-1031 ##label WRI !'##cross-references GB:X56844; NID:g10269; PIDN:CAA40175.1; PID:g10270 CLASSIFICATION #superfamily kinesin heavy chain; kinesin motor domain !1homology KEYWORDS ATP; coiled coil; heterotetramer; hydrolase; microtubule !1binding; mitosis; nucleotide binding; P-loop FEATURE !$9-331 #domain kinesin motor domain homology #label KMOT\ !$84-91 #region nucleotide-binding motif A (P-loop)\ !$393-857 #domain rod #status predicted #label RDD\ !$858-1031 #domain globular #status predicted #label GBD\ !$90 #binding_site ATP (Lys) #status predicted SUMMARY #length 1031 #molecular-weight 117522 #checksum 3166 SEQUENCE /// ENTRY S28262 #type complete TITLE kinesin-related protein MKLP-1 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 17-Apr-1993 #sequence_revision 02-May-1994 #text_change 19-Jan-2001 ACCESSIONS S28262 REFERENCE S28262 !$#authors Nislow, C.; Lombillo, V.A.; Kuriyama, R.; McIntosh, J.R. !$#journal Nature (1992) 359:543-547 !$#title A plus-end-directed motor enzyme that moves antiparallel !1microtubules in vitro localizes to the interzone of mitotic !1spindles. !$#cross-references MUID:93024924; PMID:1406973 !$#accession S28262 !'##molecule_type mRNA !'##residues 1-960 ##label NIS !'##cross-references EMBL:X67155; NID:g34671; PIDN:CAA47628.1; !1PID:g34672 GENETICS !$#gene GDB:KNSL5; MKLP1 !'##cross-references GDB:9956859 CLASSIFICATION #superfamily kinesin-related protein MKLP-1; kinesin motor !1domain homology KEYWORDS ATP; coiled coil; microtubule binding; mitosis; nucleotide !1binding; P-loop FEATURE !$25-440 #domain kinesin motor domain homology #label KMOT\ !$110-117 #region nucleotide-binding motif A (P-loop)\ !$485-655 #domain coiled coil #status predicted #label COI\ !$116 #binding_site ATP (Lys) #status predicted SUMMARY #length 960 #molecular-weight 110252 #checksum 7301 SEQUENCE /// ENTRY A40264 #type complete TITLE kinesin-related protein Eg5 - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 03-Mar-1994 #sequence_revision 03-Mar-1994 #text_change 19-Jan-2001 ACCESSIONS A40264; S18764 REFERENCE A40264 !$#authors Le Guellec, R.; Paris, J.; Couturier, A.; Roghi, C.; !1Philippe, M. !$#journal Mol. Cell. Biol. (1991) 11:3395-3398 !$#title Cloning by differential screening of a Xenopus cDNA that !1encodes a kinesin-related protein. !$#cross-references MUID:91246212; PMID:1710028 !$#accession A40264 !'##molecule_type mRNA !'##residues 1-1060 ##label LEG !'##cross-references EMBL:X54002; NID:g64869; PIDN:CAA37950.1; !1PID:g64870 !'##note the authors translated the codon GCT for residue 784 as Leu CLASSIFICATION #superfamily kinesin-related protein Eg5; kinesin motor !1domain homology KEYWORDS ATP; coiled coil; microtubule binding; mitosis; nucleotide !1binding; P-loop; phosphoprotein FEATURE !$12-358 #domain kinesin motor domain homology #label KMOT\ !$98-105 #region nucleotide-binding motif A (P-loop)\ !$104 #binding_site ATP (Lys) #status predicted SUMMARY #length 1060 #molecular-weight 119331 #checksum 868 SEQUENCE /// ENTRY G02157 #type complete TITLE kinesin-like spindle protein HKSP - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS G02157 REFERENCE H00839 !$#authors Whitehead, C. !$#submission submitted to the EMBL Data Library, September 1995 !$#accession G02157 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-1056 ##label WHI !'##cross-references EMBL:U37426; NID:g1171152; PIDN:AAA86132.1; !1PID:g1171153 GENETICS !$#gene GDB:KNSL1; Eg5; KSP !'##cross-references GDB:132856; OMIM:148760 !$#map_position 10q24.1-10q24.1 CLASSIFICATION #superfamily kinesin-related protein Eg5; kinesin motor !1domain homology KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$19-365 #domain kinesin motor domain homology #label KMOT\ !$105-112 #region nucleotide-binding motif A (P-loop) SUMMARY #length 1056 #molecular-weight 119158 #checksum 5519 SEQUENCE /// ENTRY A34795 #type complete TITLE kinesin-related protein bimC - Emericella nidulans ORGANISM #formal_name Emericella nidulans, Aspergillus nidulans DATE 03-Mar-1994 #sequence_revision 03-Mar-1994 #text_change 19-Jan-2001 ACCESSIONS A34795; B34795 REFERENCE A34795 !$#authors Enos, A.P.; Morris, N.R. !$#journal Cell (1990) 60:1019-1027 !$#title Mutation of a gene that encodes a kinesin-like protein !1blocks nuclear division in A. nidulans. !$#cross-references MUID:90199865; PMID:2138511 !$#accession A34795 !'##molecule_type DNA !'##residues 1-1184 ##label ENO !'##cross-references GB:M32075; NID:g168022; PIDN:AAA33298.1; !1PID:g168023 CLASSIFICATION #superfamily kinesin-related protein Eg5; kinesin motor !1domain homology KEYWORDS ATP; microtubule binding; mitosis; nucleotide binding; !1P-loop FEATURE !$82-422 #domain kinesin motor domain homology #label KMOT\ !$167-174 #region nucleotide-binding motif A (P-loop)\ !$173 #binding_site ATP (Lys) #status predicted SUMMARY #length 1184 #molecular-weight 131629 #checksum 9420 SEQUENCE /// ENTRY B71405 #type complete TITLE probable kinesin - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress #variety columbia DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS B71405 REFERENCE A71400 !$#authors Bevan, M.; Bancroft, I.; Bent, E.; Love, K.; Goodman, H.; !1Dean, C.; Bergkamp, R.; Dirkse, W.; Van Staveren, M.; !1Stiekema, W.; Drost, L.; Ridley, P.; Hudson, S.A.; Patel, !1K.; Murphy, G.; Piffanelli, P.; Wedler, H.; Wedler, E.; !1Wambutt, R.; Weitzenegger, T.; Pohl, T.M.; Terryn, N.; !1Gielen, J.; Villarroel, R.; De Clerck, R.; Van Montagu, M.; !1Lecharny, A.; Auborg, S.; Gy, I.; Kreis, M.; Lao, N.; !1Kavanagh, T.; Hempel, S.; Kotter, P.; Entian, K.D.; Rieger, !1M.; Schaeffer, M.; Funk, B.; Mueller-Auer, S.; Silvey, M.; !1James, R.; Montfort, A.; Pons, A.; Puigdomenech, P.; Douka, !1A.; Voukelatou, E.; Milioni, D.; Hatzopoulos, P.; Piravandi, !1E.; Obermaier, B.; Hilbert, H.; Duesterhoft, A.; Moores, T.; !1Jones, J.D.G.; Eneva, T.; Palme, K.; Benes, V.; Rechman, S.; !1Ansorge, W.; Cooke, R.; Berger, C.; Delseny, M.; Voet, M.; !1Volckaert, G.; Mewes, H.W.; Klosterman, S.; Schueller, C.; !1Chalwatzis, N. !$#journal Nature (1998) 391:485-488 !$#title Analysis of 1.9 Mb of contiguous sequence from chromosome 4 !1of Arabidopsis thaliana. !$#cross-references MUID:98121113; PMID:9461215 !$#accession B71405 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-959 ##label BEV !'##cross-references GB:Z97336; NID:g2244788; PIDN:CAB10212.1; !1PID:g2244790 GENETICS !$#map_position 4COP9-4G3845 CLASSIFICATION #superfamily Arabidopsis thaliana 107.5K kinesin-related !1protein; kinesin motor domain homology FEATURE !$49-379 #domain kinesin motor domain homology #label KMOT SUMMARY #length 959 #molecular-weight 107515 #checksum 6071 SEQUENCE /// ENTRY H71402 #type complete TITLE probable kinesin - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress #variety columbia DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS H71402 REFERENCE A71400 !$#authors Bevan, M.; Bancroft, I.; Bent, E.; Love, K.; Goodman, H.; !1Dean, C.; Bergkamp, R.; Dirkse, W.; Van Staveren, M.; !1Stiekema, W.; Drost, L.; Ridley, P.; Hudson, S.A.; Patel, !1K.; Murphy, G.; Piffanelli, P.; Wedler, H.; Wedler, E.; !1Wambutt, R.; Weitzenegger, T.; Pohl, T.M.; Terryn, N.; !1Gielen, J.; Villarroel, R.; De Clerck, R.; Van Montagu, M.; !1Lecharny, A.; Auborg, S.; Gy, I.; Kreis, M.; Lao, N.; !1Kavanagh, T.; Hempel, S.; Kotter, P.; Entian, K.D.; Rieger, !1M.; Schaeffer, M.; Funk, B.; Mueller-Auer, S.; Silvey, M.; !1James, R.; Montfort, A.; Pons, A.; Puigdomenech, P.; Douka, !1A.; Voukelatou, E.; Milioni, D.; Hatzopoulos, P.; Piravandi, !1E.; Obermaier, B.; Hilbert, H.; Duesterhoft, A.; Moores, T.; !1Jones, J.D.G.; Eneva, T.; Palme, K.; Benes, V.; Rechman, S.; !1Ansorge, W.; Cooke, R.; Berger, C.; Delseny, M.; Voet, M.; !1Volckaert, G.; Mewes, H.W.; Klosterman, S.; Schueller, C.; !1Chalwatzis, N. !$#journal Nature (1998) 391:485-488 !$#title Analysis of 1.9 Mb of contiguous sequence from chromosome 4 !1of Arabidopsis thaliana. !$#cross-references MUID:98121113; PMID:9461215 !$#accession H71402 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-1662 ##label BEV !'##cross-references GB:Z97335; NID:g2244747; PIDN:CAB10194.1; !1PID:g2244771 GENETICS !$#map_position 4COP9-4G3845 CLASSIFICATION #superfamily Arabidopsis thaliana 186.9K kinesin-related !1protein; kinesin motor domain homology FEATURE !$43-423 #domain kinesin motor domain homology #label KMOT SUMMARY #length 1662 #molecular-weight 186876 #checksum 4165 SEQUENCE /// ENTRY B42641 #type complete TITLE kinesin-related protein CIN8 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YEL061c ORGANISM #formal_name Saccharomyces cerevisiae DATE 03-Mar-1994 #sequence_revision 19-May-1995 #text_change 23-Mar-2001 ACCESSIONS S50528; B42641; S44939; S69009; S20134 REFERENCE S50434 !$#authors Dietrich, F.S. !$#submission submitted to the EMBL Data Library, December 1994 !$#description The sequence of S. cerevisiae cosmids 9669, 8334, 8199, and !1lambda clone 1160. !$#accession S50528 !'##molecule_type DNA !'##residues 1-1038 ##label DIE !'##cross-references EMBL:U18795; NID:g603241; PIDN:AAB65026.1; !1PID:g603257; GSPDB:GN00005; MIPS:YEL061c REFERENCE A42641 !$#authors Hoyt, M.A.; He, L.; Loo, K.K.; Saunders, W.S. !$#journal J. Cell Biol. (1992) 118:109-120 !$#title Two Saccharomyces cerevisiae kinesin-related gene products !1required for mitotic spindle assembly. !$#cross-references MUID:92317149; PMID:1618897 !$#accession B42641 !'##molecule_type DNA !'##residues 1-253,'A',255-830,'H',832-1038 ##label HOY !'##cross-references EMBL:Z11859; NID:g3541; PIDN:CAA77885.1; PID:g3542 !'##note sequence extracted from NCBI backbone (NCBIN:107723, !1NCBIP:107726) REFERENCE S44938 !$#authors Rousselet, G.; Simon, M.; Ripoche, P.; Buhler, J.M. !$#submission submitted to the EMBL Data Library, May 1994 !$#description A second nitrogen permease regulator in Saccharomyces !1cerevisiae. !$#accession S44939 !'##molecule_type DNA !'##residues 1021-1038 ##label ROU !'##cross-references EMBL:X79105; NID:g485969; PIDN:CAA55722.1; !1PID:g485971 REFERENCE S69008 !$#authors Rousselet, G.; Simon, M.; Ripoche, P.; Buhler, J.M. !$#journal FEBS Lett. (1995) 359:215-219 !$#title A second nitrogen permease regulator in Saccharomyces !1cerevisiae. !$#cross-references MUID:95172238; PMID:7867803 !$#accession S69009 !'##status translation not shown !'##molecule_type DNA !'##residues 1021-1038 ##label ROW !'##cross-references EMBL:X79105; NID:g485969; PIDN:CAA55722.1; !1PID:g485971 GENETICS !$#gene SGD:CIN8; MIPS:YEL061c !'##cross-references SGD:S0000787; MIPS:YEL061c !$#map_position 5L CLASSIFICATION #superfamily kinesin-related protein CIN8; kinesin motor !1domain homology KEYWORDS ATP; coiled coil; microtubule binding; mitosis; nucleotide !1binding; P-loop FEATURE !$75-520 #domain kinesin motor domain homology #status !8atypical #label KMOT\ !$166-173 #region nucleotide-binding motif A (P-loop)\ !$172 #binding_site ATP (Lys) #status predicted SUMMARY #length 1038 #molecular-weight 117998 #checksum 485 SEQUENCE /// ENTRY A42640 #type complete TITLE kinesin-related protein KIP1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YBL0504; protein YBL0521; protein YBL063w ORGANISM #formal_name Saccharomyces cerevisiae DATE 03-Mar-1994 #sequence_revision 03-Mar-1994 #text_change 19-Jan-2001 ACCESSIONS A42640; S39826; S45798; S37327 REFERENCE A42640 !$#authors Roof, D.M.; Meluh, P.B.; Rose, M.D. !$#journal J. Cell Biol. (1992) 118:95-108 !$#title Kinesin-related proteins required for assembly of the !1mitotic spindle. !$#cross-references MUID:92317166; PMID:1618910 !$#accession A42640 !'##molecule_type DNA !'##residues 1-1111 ##label ROO !'##cross-references EMBL:Z11962; NID:g3850; PIDN:CAA78019.1; PID:g3851 !'##note sequence extracted from NCBI backbone (NCBIN:107715, !1NCBIP:107718) REFERENCE S39824 !$#authors Scherens, B.; el Bakkoury, M.; Vierendeels, F.; Dubois, E.; !1Messenguy, F. !$#journal Yeast (1993) 9:1355-1371 !$#title Sequencing and functional analysis of a 32 560 bp segment on !1the left arm of yeast chromosome II. Identification of 26 !1open reading frames, including the KIP1 and SEC17 genes. !$#cross-references MUID:94205266; PMID:8154187 !$#accession S39826 !'##molecule_type DNA !'##residues 1-1111 ##label SCH !'##cross-references EMBL:Z23261; NID:g313733; PIDN:CAA80785.1; !1PID:g313736 REFERENCE S45782 !$#authors Dubois, E.; El Bakkoury, M.; Glansdorff, N.; Messenguy, F.; !1Pierard, A.; Scherens, B.; Vierendeels, F. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S45798 !'##molecule_type DNA !'##residues 1-1111 ##label DUB !'##cross-references EMBL:Z35824; NID:g536098; PIDN:CAA84883.1; !1PID:g536099; GSPDB:GN00002; MIPS:YBL063w GENETICS !$#gene SGD:KIP1; MIPS:YBL063w !'##cross-references SGD:S0000159; MIPS:YBL063w !$#map_position 2L CLASSIFICATION #superfamily kinesin-related protein KIP1; kinesin motor !1domain homology KEYWORDS ATP; coiled coil; microtubule binding; mitosis; nucleotide !1binding; P-loop FEATURE !$53-416 #domain kinesin motor domain homology #label KMOT\ !$141-148 #region nucleotide-binding motif A (P-loop)\ !$147 #binding_site ATP (Lys) #status predicted SUMMARY #length 1111 #molecular-weight 125793 #checksum 3299 SEQUENCE /// ENTRY A48669 #type complete TITLE kinesin-related protein KLP61F - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS A48669; B41298 REFERENCE A48669 !$#authors Heck, M.M.S.; Pereira, A.; Pesavento, P.; Yannoni, Y.; !1Spradling, A.C.; Goldstein, L.S.B. !$#journal J. Cell Biol. (1993) 123:665-679 !$#title The kinesin-like protein KLP61F is essential for mitosis in !1Drosophila. !$#cross-references MUID:94043448; PMID:8227131 !$#accession A48669 !'##status preliminary !'##molecule_type mRNA !'##residues 1-1066 ##label HEC !'##cross-references GB:U01842; NID:g416040; PIDN:AAA03718.1; !1PID:g416041 REFERENCE A41298 !$#authors Stewart, R.J.; Pesavento, P.A.; Woerpel, D.N.; Goldstein, !1L.S.B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:8470-8474 !$#title Identification and partial characterization of six members !1of the kinesin superfamily in Drosophila. !$#cross-references MUID:92020874; PMID:1924306 !$#accession B41298 !'##molecule_type DNA !'##residues 228-357 ##label STE !'##cross-references GB:M74428; NID:g157785; PIDN:AAA28655.1; !1PID:g157786 GENETICS !$#gene FlyBase:Klp61F !'##cross-references FlyBase:FBgn0004378 CLASSIFICATION #superfamily kinesin-related protein KLP61F; kinesin motor !1domain homology KEYWORDS ATP; cell division; mitosis; nucleotide binding; P-loop FEATURE !$20-362 #domain kinesin motor domain homology #label KMOT\ !$103-110 #region nucleotide-binding motif A (P-loop) SUMMARY #length 1066 #molecular-weight 121193 #checksum 4770 SEQUENCE /// ENTRY B44259 #type complete TITLE kinesin-related protein KIF3A - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 03-Mar-1994 #sequence_revision 03-Mar-1994 #text_change 19-Jan-2001 ACCESSIONS B44259; S27872 REFERENCE A44259 !$#authors Aizawa, H.; Sekine, Y.; Takemura, R.; Zhang, Z.; Nangaku, !1M.; Hirokawa, N. !$#journal J. Cell Biol. (1992) 119:1287-1296 !$#title Kinesin family in murine central nervous system. !$#cross-references MUID:93077686; PMID:1447303 !$#accession B44259 !'##molecule_type mRNA !'##residues 1-701 ##label AIZ !'##cross-references EMBL:D12645; NID:g220469; PIDN:BAA02166.1; !1PID:g220470 !'##experimental_source brain !'##note sequence extracted from NCBI backbone (NCBIP:118911) COMPLEX heterodimer with KIF3B (PIR:A57107); the KIF3A/3B !1heterodimer associates with kinesin superfamily-associated !1protein (KAP3) (PIR:JC6161) to form a heterotrimer FUNCTION !$#description KIF3 complex is a motor protein that provides anterograde !1fast axonal transport of membranous organelles CLASSIFICATION #superfamily kinesin-related protein KIF3; kinesin motor !1domain homology KEYWORDS ATP; coiled coil; heterodimer; heterotrimer; microtubule !1binding; nucleotide binding; P-loop FEATURE !$1-368 #domain head globular #status predicted #label HGL\ !$15-351 #domain kinesin motor domain homology #label KMOT\ !$100-107 #region nucleotide-binding motif A (P-loop)\ !$369-599 #domain helical rod #status predicted #label ROD\ !$600-701 #domain tail globular #status predicted #label TGL\ !$106 #binding_site ATP (Lys) #status predicted SUMMARY #length 701 #molecular-weight 80167 #checksum 60 SEQUENCE /// ENTRY S38982 #type complete TITLE kinesin-related protein KRP85 - sea urchin (Strongylocentrotus purpuratus) ALTERNATE_NAMES kinesin-2 chain A; KRP (85/95) 85K chain ORGANISM #formal_name Strongylocentrotus purpuratus #common_name purple urchin DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S38982; S72551 REFERENCE S38982 !$#authors Cole, D.G.; Chinn, S.W.; Wedaman, K.P.; Hall, K.; Vuong, T.; !1Scholey, J.M. !$#journal Nature (1993) 366:268-270 !$#title Novel heterotrimeric kinesin-related protein purified from !1sea urchin eggs. !$#cross-references MUID:94050179; PMID:8232586 !$#accession S38982 !'##molecule_type mRNA !'##residues 1-699 ##label COL1 !'##cross-references EMBL:L16993; NID:g295245; PIDN:AAA16098.1; !1PID:g295246 !$#accession S72551 !'##molecule_type protein !'##residues 2-5,'X',7-11;59-64;125-132;222-226,'X',228-230 ##label COL2 COMPLEX heterotrimer of a 115K chain and two kinesin-related chains !1of 95K (PIR:S58691) and 85K CLASSIFICATION #superfamily kinesin-related protein KIF3; kinesin motor !1domain homology KEYWORDS ATP; heterotrimer; microtubule binding; nucleotide binding; !1P-loop FEATURE !$11-348 #domain kinesin motor domain homology #label KMOT\ !$97-104 #region nucleotide-binding motif A (P-loop)\ !$103 #binding_site ATP (Lys) #status predicted SUMMARY #length 699 #molecular-weight 78697 #checksum 1222 SEQUENCE /// ENTRY A57107 #type complete TITLE kinesin-related protein KIF3B - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 03-Nov-1995 #sequence_revision 03-Nov-1995 #text_change 19-Jan-2001 ACCESSIONS A57107 REFERENCE A57107 !$#authors Yamazaki, H.; Nakata, T.; Okada, Y.; Hirokawa, N. !$#journal J. Cell Biol. (1995) 130:1387-1399 !$#title KIF3A/B: a heterodimeric kinesin superfamily protein that !1works as a microtubule plus end-directed motor for membrane !1organelle transport. !$#cross-references MUID:96032268; PMID:7559760 !$#accession A57107 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-747 ##label YAM !'##cross-references GB:D26077; NID:g1060922; PIDN:BAA05070.1; !1PID:g1060923 !'##experimental_source brain COMPLEX heterodimer with KIF3A (PIR:B44259); the KIF3A/3B !1heterodimer associates with a kinesin superfamily-associated !1protein (KAP3) (PIR:JC6161 in testis) to form a heterotrimer FUNCTION !$#description KIF3 complex is a motor protein that provides anterograde !1fast axonal transport for an unknown cargo CLASSIFICATION #superfamily kinesin-related protein KIF3; kinesin motor !1domain homology KEYWORDS ATP; coiled coil; heterodimer; heterotrimer; microtubule !1binding; nucleotide binding; P-loop FEATURE !$1-363 #domain head globular #status predicted #label HGL\ !$10-346 #domain kinesin motor domain homology #label KMOT\ !$96-103 #region nucleotide-binding motif A (P-loop)\ !$364-592 #domain helical rod #status predicted #label ROD\ !$594-747 #domain tail globular #status predicted #label TGL\ !$102 #binding_site ATP (Lys) #status predicted SUMMARY #length 747 #molecular-weight 85288 #checksum 7951 SEQUENCE /// ENTRY S58691 #type complete TITLE kinesin-related protein KRP95 - sea urchin (Strongylocentrotus droebechiensis) ALTERNATE_NAMES kinesin-2 chain B; KRP (85/95) 95K chain ORGANISM #formal_name Strongylocentrotus droebechiensis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S58691 REFERENCE S58691 !$#authors Rashid, D.J.; Wedaman, K.P.; Scholey, J.M. !$#journal J. Mol. Biol. (1995) 252:157-162 !$#title Heterodimerization of the two motor subunits of the !1heterotrimeric kinesin, KRP(85/95). !$#cross-references MUID:95404610; PMID:7674298 !$#accession S58691 !'##status preliminary; nucleic acid sequence not shown; not compared !1with conceptual translation !'##molecule_type mRNA !'##residues 1-742 ##label RAS COMPLEX heterotrimer of a 115K chain and two kinesin-related chains !1of 85K (PIR:S38982) and 95K CLASSIFICATION #superfamily kinesin-related protein KIF3; kinesin motor !1domain homology KEYWORDS ATP; heterotrimer; microtubule binding; nucleotide binding; !1P-loop FEATURE !$9-345 #domain kinesin motor domain homology #label KMOT\ !$95-102 #region nucleotide-binding motif A (P-loop)\ !$101 #binding_site ATP (Lys) #status predicted SUMMARY #length 742 #molecular-weight 84156 #checksum 2976 SEQUENCE /// ENTRY A55236 #type complete TITLE kinesin-related protein KLP68D - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES kinesin-like protein 5; KLP5 ORGANISM #formal_name Drosophila melanogaster DATE 23-Mar-1995 #sequence_revision 23-Mar-1995 #text_change 19-Jan-2001 ACCESSIONS A55236; E41298 REFERENCE A55236 !$#authors Pesavento, P.A.; Stewart, R.J.; Goldstein, L.S.B. !$#journal J. Cell Biol. (1994) 127:1041-1048 !$#title Characterization of the KLP68D kinesin-like protein in !1Drosophila: possible roles in axonal transport. !$#cross-references MUID:95050960; PMID:7525600 !$#accession A55236 !'##molecule_type mRNA !'##residues 1-784 ##label PES !'##cross-references GB:U15974; NID:g595912; PIDN:AAA69929.1; !1PID:g565090 REFERENCE A41298 !$#authors Stewart, R.J.; Pesavento, P.A.; Woerpel, D.N.; Goldstein, !1L.S.B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:8470-8474 !$#title Identification and partial characterization of six members !1of the kinesin superfamily in Drosophila. !$#cross-references MUID:92020874; PMID:1924306 !$#accession E41298 !'##molecule_type DNA !'##residues 'TC',222-337,'VRGQV' ##label STE !'##cross-references GB:M74431; NID:g157791; PIDN:AAA28658.1; !1PID:g157792 GENETICS !$#gene FlyBase:Klp68D; KLP5 !'##cross-references FlyBase:FBgn0004381 FUNCTION !$#description may be part of a motor protein that provides anterograde !1fast axonal transport CLASSIFICATION #superfamily kinesin-related protein KIF3; kinesin motor !1domain homology KEYWORDS ATP; coiled coil; microtubule binding; nucleotide binding; !1P-loop FEATURE !$1-349 #domain head globular #status predicted #label HGL\ !$20-350 #domain kinesin motor domain homology #label KMOT\ !$106-113 #region nucleotide-binding motif A (P-loop)\ !$350-580 #domain helical rod #status predicted #label ROD\ !$581-784 #domain tail globular #status predicted #label TGL\ !$112 #binding_site ATP (Lys) #status predicted SUMMARY #length 784 #molecular-weight 88193 #checksum 3313 SEQUENCE /// ENTRY A36026 #type complete TITLE kinesin-related protein nodA - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 03-Mar-1994 #sequence_revision 03-Mar-1994 #text_change 19-Jan-2001 ACCESSIONS A36026 REFERENCE A36026 !$#authors Zhang, P.; Knowles, B.A.; Goldstein, L.S.B.; Hawley, R.S. !$#journal Cell (1990) 62:1053-1062 !$#title A kinesin-like protein required for distributive chromosome !1segregation in Drosophila. !$#cross-references MUID:90381763; PMID:2144792 !$#accession A36026 !'##molecule_type mRNA !'##residues 1-666 ##label ZHA !'##cross-references GB:M36195; NID:g157779; PIDN:AAA28653.1; !1PID:g157780 GENETICS !$#gene FlyBase:nod !'##cross-references FlyBase:FBgn0002948 CLASSIFICATION #superfamily kinesin-related protein nodA; kinesin motor !1domain homology KEYWORDS ATP; microtubule binding; mitosis; nucleotide binding; !1P-loop FEATURE !$9-326 #domain kinesin motor domain homology #label KMOT\ !$87-94 #region nucleotide-binding motif A (P-loop)\ !$93 #binding_site ATP (Lys) #status predicted SUMMARY #length 666 #molecular-weight 73907 #checksum 7642 SEQUENCE /// ENTRY S25732 #type complete TITLE suppressor protein SMY1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES kinesin-like protein; protein YKL079w; protein YKL409 ORGANISM #formal_name Saccharomyces cerevisiae DATE 03-Mar-1994 #sequence_revision 03-Mar-1994 #text_change 12-Nov-1999 ACCESSIONS S25732; S37904; S42007; C41765; S39119 REFERENCE S25732 !$#authors Lillie, S.H.; Brown, S.S. !$#journal Nature (1992) 356:358-361 !$#title Suppression of a myosin defect by a kinesin-related gene. !$#cross-references MUID:92195411; PMID:1549181 !$#accession S25732 !'##molecule_type DNA !'##residues 1-656 ##label LIL !'##cross-references EMBL:M69021; NID:g172625; PIDN:AAA35056.1; !1PID:g172626 REFERENCE S37897 !$#authors Pohl, T.M.; Pohl, F.M. !$#submission submitted to the Protein Sequence Database, March 1994 !$#accession S37904 !'##molecule_type DNA !'##residues 1-656 ##label POH !'##cross-references EMBL:Z28079; NID:g486113; PIDN:CAA81916.1; !1PID:g486114; GSPDB:GN00011; MIPS:YKL079w !'##experimental_source strain S288C REFERENCE S42006 !$#authors James, C.M.; Gent, M.E.; Indge, K.J.; Oliver, S.G. !$#journal Yeast (1994) 10:247-255 !$#title Sequence analysis of a 10 kb fragment of yeast chromosome XI !1identifies the SMY1 locus and reveals sequences related to a !1pre-mRNA splicing factor and vacuolar ATPase subunit C plus !1a number of unidentified open reading frames. !$#cross-references MUID:94262328; PMID:8203165 !$#accession S42007 !'##molecule_type DNA !'##residues 1-656 ##label JAM !'##cross-references EMBL:X75560; NID:g414713; PIDN:CAA53238.1; !1PID:g414715 REFERENCE A41765 !$#authors Beltran, C.; Kopecky, J.; Pan, Y.C.; Nelson, H.; Nelson, N. !$#journal J. Biol. Chem. (1992) 267:774-779 !$#title Cloning and mutational analysis of the gene encoding subunit !1C of yeast vacuolar H(+)-ATPase. !$#cross-references MUID:92112808; PMID:1730668 !$#accession C41765 !'##molecule_type DNA !'##residues 1-185 ##label BEL !'##cross-references EMBL:M77143; NID:g171098; PIDN:AAA34441.1; !1PID:g171100 !'##note sequence extracted from NCBI backbone (NCBIN:75489, !1NCBIP:75494) GENETICS !$#gene SGD:SMY1; MIPS:YKL079w !'##cross-references SGD:S0001562; MIPS:YKL079w !$#map_position 11L CLASSIFICATION #superfamily suppressor protein SMY1; kinesin motor domain !1homology KEYWORDS ATP; P-loop; purine nucleotide binding FEATURE !$28-370 #domain kinesin motor domain homology #label KMOT\ !$114-121 #region nucleotide-binding motif A (P-loop)\ !$120 #binding_site ATP/GTP (Lys) #status predicted SUMMARY #length 656 #molecular-weight 73799 #checksum 9523 SEQUENCE /// ENTRY S28261 #type complete TITLE centromere protein E - human ALTERNATE_NAMES centromere 312K protein; kinesin-related protein CENP-E ORGANISM #formal_name Homo sapiens #common_name man DATE 03-Mar-1994 #sequence_revision 03-Mar-1994 #text_change 19-Jan-2001 ACCESSIONS S28261 REFERENCE S28261 !$#authors Yen, T.J.; Li, G.; Schaar, B.T.; Szilak, I.; Cleveland, D.W. !$#journal Nature (1992) 359:536-539 !$#title CENP-E is a putative kinetochore motor that accumulates just !1before mitosis. !$#cross-references MUID:93024922; PMID:1406971 !$#accession S28261 !'##molecule_type mRNA !'##residues 1-2663 ##label YEN !'##cross-references EMBL:Z15005; NID:g29864; PIDN:CAA78727.1; !1PID:g29865 GENETICS !$#gene GDB:CENPE !'##cross-references GDB:361164; OMIM:117143 !$#map_position 4q24-4q25 CLASSIFICATION #superfamily centromere protein E; kinesin motor domain !1homology KEYWORDS ATP; coiled coil; microtubule binding; mitosis; nucleotide !1binding; P-loop FEATURE !$7-335 #domain kinesin motor domain homology #label KMOT\ !$86-93 #region nucleotide-binding motif A (P-loop)\ !$486-2183 #domain coiled coil #status predicted #label COI\ !$92 #binding_site ATP (Lys) #status predicted SUMMARY #length 2663 #molecular-weight 312088 #checksum 1750 SEQUENCE /// ENTRY JN0114 #type complete TITLE kinesin-related protein unc-104 - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 03-Mar-1994 #sequence_revision 03-Mar-1994 #text_change 19-Jan-2001 ACCESSIONS JN0114 REFERENCE JN0114 !$#authors Otsuka, A.J.; Jeyaprakash, A.; Garcia-Anoveros, J.; Tang, !1L.Z.; Fisk, G.; Hartshorne, T.; Franco, R.; Born, T. !$#journal Neuron (1991) 6:113-122 !$#title The C. elegans unc-104 gene encodes a putative kinesin heavy !1chain-like protein. !$#cross-references MUID:91097805; PMID:1846075 !$#accession JN0114 !'##molecule_type mRNA !'##residues 1-1584 ##label OTS !'##cross-references GB:M58582 !'##note 598-Thr and 930-Met were also found GENETICS !$#gene unc-104 CLASSIFICATION #superfamily kinesin-related protein unc-104; kinesin motor !1domain homology; pleckstrin repeat homology KEYWORDS ATP; microtubule binding; nucleotide binding; P-loop FEATURE !$4-353 #domain kinesin motor domain homology #label KMOT\ !$93-100 #region nucleotide-binding motif A (P-loop)\ !$1285-1287 #region cell attachment (R-G-D) motif\ !$99 #binding_site ATP (Lys) #status predicted SUMMARY #length 1584 #molecular-weight 179651 #checksum 5761 SEQUENCE /// ENTRY A55289 #type complete TITLE kinesin-like protein KIF1B - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS A55289 REFERENCE A55289 !$#authors Nangaku, M.; Sato-Yoshitake, R.; Okada, Y.; Noda, Y.; !1Takemura, R.; Yamazaki, H.; Hirokawa, N. !$#journal Cell (1994) 79:1209-1220 !$#title KIF1B, a novel microtubule plus end-directed monomeric motor !1protein for transport of mitochondria. !$#cross-references MUID:95094296; PMID:7528108 !$#accession A55289 !'##status preliminary !'##molecule_type mRNA !'##residues 1-1150 ##label NAN !'##cross-references GB:D17577; NID:g407338; PIDN:BAA04503.1; !1PID:g407339 CLASSIFICATION #superfamily kinesin-related protein KIF1B; kinesin motor !1domain homology KEYWORDS nucleotide binding; P-loop FEATURE !$6-354 #domain kinesin motor domain homology #label KMOT\ !$97-104 #region nucleotide-binding motif A (P-loop) SUMMARY #length 1150 #molecular-weight 130277 #checksum 5200 SEQUENCE /// ENTRY A44259 #type complete TITLE kinesin-related protein KIF2 - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 03-Mar-1994 #sequence_revision 03-Mar-1994 #text_change 19-Jan-2001 ACCESSIONS A44259; S27871 REFERENCE A44259 !$#authors Aizawa, H.; Sekine, Y.; Takemura, R.; Zhang, Z.; Nangaku, !1M.; Hirokawa, N. !$#journal J. Cell Biol. (1992) 119:1287-1296 !$#title Kinesin family in murine central nervous system. !$#cross-references MUID:93077686; PMID:1447303 !$#accession A44259 !'##molecule_type mRNA !'##residues 1-716 ##label AIZ !'##cross-references EMBL:D12644; NID:g220467; PIDN:BAA02165.1; !1PID:g220468 !'##experimental_source brain !'##note sequence extracted from NCBI backbone (NCBIP:118908) CLASSIFICATION #superfamily kinesin-related protein KIF2; kinesin motor !1domain homology KEYWORDS ATP; microtubule binding; nucleotide binding; P-loop FEATURE !$196-531 #domain kinesin motor domain homology #label KMOT\ !$285-292 #region nucleotide-binding motif A (P-loop)\ !$291 #binding_site ATP (Lys) #status predicted SUMMARY #length 716 #molecular-weight 80946 #checksum 4220 SEQUENCE /// ENTRY C42640 #type complete TITLE kinesin-related protein KIP2 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein P2581; protein YPL155c ORGANISM #formal_name Saccharomyces cerevisiae DATE 03-Mar-1994 #sequence_revision 03-Mar-1994 #text_change 19-Jan-2001 ACCESSIONS C42640; S65166; S69444; S28232; S28234 REFERENCE A42640 !$#authors Roof, D.M.; Meluh, P.B.; Rose, M.D. !$#journal J. Cell Biol. (1992) 118:95-108 !$#title Kinesin-related proteins required for assembly of the !1mitotic spindle. !$#cross-references MUID:92317166; PMID:1618910 !$#accession C42640 !'##molecule_type DNA !'##residues 1-706 ##label ROO !'##cross-references EMBL:Z11963; NID:g3852; PIDN:CAA78021.1; PID:g3854 !'##note sequence extracted from NCBI backbone (NCBIN:107719, !1NCBIP:107722) REFERENCE S65154 !$#authors Purnelle, B.; Coster, F.; Goffeau, A. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S65166 !'##molecule_type DNA !'##residues 1-706 ##label PUR !'##cross-references EMBL:Z73511; NID:g1370329; PIDN:CAA97860.1; !1PID:g1370330; GSPDB:GN00016; MIPS:YPL155c !'##experimental_source strain S288C (AB972) REFERENCE S69428 !$#authors Purnelle, B.; Comblez, S.; Coster, F.; Naveau, F.; Goffeau, !1A. !$#submission submitted to the EMBL Data Library, March 1996 !$#description The sequence of 55 kb on the left arm of yeast chromosome !1XVI identifies 28 open reading frames including 18 unknown !1among which a new putative serine/threonine protein kinase, !1a homologue to the human phosphotyrosyl phosphatase !1activator PTPA and a homologue to the plant pleiotropic !1regulator PRL1 of PP1 and PP2a phosphatases. !$#accession S69444 !'##molecule_type DNA !'##residues 1-706 ##label PUW !'##cross-references EMBL:X96770; NID:g1403537; PIDN:CAA65566.1; !1PID:g1403554 GENETICS !$#gene SGD:KIP2; MIPS:YPL155c !'##cross-references SGD:S0006076; MIPS:YPL155c !$#map_position 16L CLASSIFICATION #superfamily kinesin-related protein KIF2; kinesin motor !1domain homology KEYWORDS ATP; coiled coil; microtubule binding; nucleotide binding; !1P-loop FEATURE !$159-499 #domain kinesin motor domain homology #status !8atypical #label KMOT\ !$202-209 #region nucleotide-binding motif A (P-loop)\ !$208 #binding_site ATP (Lys) #status predicted SUMMARY #length 706 #molecular-weight 78377 #checksum 6305 SEQUENCE /// ENTRY S09748 #type complete TITLE kinesin-related protein ncd1 - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES ncdD protein ORGANISM #formal_name Drosophila melanogaster DATE 21-Sep-1990 #sequence_revision 02-May-1994 #text_change 19-Jan-2001 ACCESSIONS S09748; A38902; A35624; S13368; S17037 REFERENCE S09748 !$#authors Endow, S.A.; Henikoff, S.; Soler-Niedziela, L. !$#journal Nature (1990) 345:81-83 !$#title Mediation of meiotic and early mitotic chromosome !1segregation in Drosophila by a protein related to kinesin. !$#cross-references MUID:90231469; PMID:1691829 !$#accession S09748 !'##molecule_type mRNA !'##residues 27-700 ##label END !'##cross-references GB:X52814 !$#accession A38902 !'##molecule_type DNA !'##residues 1-27 ##label EN2 !'##cross-references GB:X52814 !'##note it is uncertain whether Met-1 or Met-16 is the initiator REFERENCE A35624 !$#authors McDonald, H.B.; Goldstein, L.S.B. !$#journal Cell (1990) 61:991-1000 !$#title Identification and characterization of a gene encoding a !1kinesin-like protein in Drosophila. !$#cross-references MUID:90275618; PMID:2140958 !$#accession A35624 !'##molecule_type mRNA !'##residues 16-696,'S',698-700 ##label MCD !'##cross-references GB:M33932; NID:g157958; PIDN:AAA28716.1; !1PID:g157959 REFERENCE S13368 !$#authors Komma, D.J.; Horne, A.S.; Endow, S.A. !$#journal EMBO J. (1991) 10:419-424 !$#title Separation of meiotic and mitotic effects of claret !1non-disjunctional on chromosome segregation in Drosophila. !$#cross-references MUID:91122049; PMID:1825056 !$#accession S13368 !'##status preliminary !'##molecule_type DNA !'##residues 337-677 ##label KOM !'##cross-references EMBL:X57475 REFERENCE S17037 !$#authors Endow, S.A. !$#submission submitted to the EMBL Data Library, May 1991 !$#accession S17037 !'##status preliminary !'##molecule_type DNA !'##residues 1-555,'F',557-696,'S',698-700 ##label ENW !'##cross-references EMBL:X57475; NID:g8285; PIDN:CAA40713.1; PID:g8286 GENETICS !$#gene FlyBase:ncd !'##cross-references FlyBase:FBgn0002924 !$#map_position 3R, 99B/C !$#introns 74/2; 287/3; 410/2; 623/3 CLASSIFICATION #superfamily kinesin-related protein KLPA; kinesin motor !1domain homology KEYWORDS ATP; coiled coil; microtubule binding; mitosis; nucleotide !1binding; P-loop FEATURE !$1-198 #domain globular #status predicted #label GBD\ !$199-247 #domain coiled coil #status predicted #label COI\ !$349-676 #domain kinesin motor domain homology #label KMOT\ !$434-441 #region nucleotide-binding motif A (P-loop)\ !$440 #binding_site ATP (Lys) #status predicted SUMMARY #length 700 #molecular-weight 77500 #checksum 511 SEQUENCE /// ENTRY A44337 #type complete TITLE kinesin-related protein KLPA - Emericella nidulans ALTERNATE_NAMES kinesin-like protein, KAR3-related; KLPA protein ORGANISM #formal_name Emericella nidulans, Aspergillus nidulans DATE 03-Mar-1994 #sequence_revision 03-Mar-1994 #text_change 19-Jan-2001 ACCESSIONS A44337; S24830 REFERENCE A44337 !$#authors O'Connell, M.J.; Meluh, P.B.; Rose, M.D.; Morris, N.R. !$#journal J. Cell Biol. (1993) 120:153-162 !$#title Suppression of the bimC4 mitotic spindle defect by deletion !1of klpA, a gene encoding a KAR3-related kinesin-like protein !1in Aspergillus nidulans. !$#cross-references MUID:93107178; PMID:8416986 !$#accession A44337 !'##molecule_type mRNA !'##residues 1-770 ##label O1C !'##cross-references GB:X64603; NID:g2703; PIDN:CAA45887.1; PID:g2704 !'##note sequence extracted from NCBI backbone (NCBIP:121121) GENETICS !$#gene klpA !$#map_position 1 CLASSIFICATION #superfamily kinesin-related protein KLPA; kinesin motor !1domain homology KEYWORDS ATP; coiled coil; microtubule binding; nucleotide binding; !1P-loop FEATURE !$422-762 #domain kinesin motor domain homology #label KMOT\ !$514-521 #region nucleotide-binding motif A (P-loop)\ !$520 #binding_site ATP (Lys) #status predicted SUMMARY #length 770 #molecular-weight 85800 #checksum 629 SEQUENCE /// ENTRY A34796 #type complete TITLE kinesin-related protein KAR3 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES nuclear fusion protein KAR3; protein P9659.16; protein YPR141c ORGANISM #formal_name Saccharomyces cerevisiae DATE 03-Mar-1994 #sequence_revision 03-Mar-1994 #text_change 23-Mar-2001 ACCESSIONS A34796; S69030 REFERENCE A34796 !$#authors Meluh, P.B.; Rose, M.D. !$#journal Cell (1990) 60:1029-1041 !$#title KAR3, a kinesin-related gene required for yeast nuclear !1fusion. !$#cross-references MUID:90199866; PMID:2138512 !$#accession A34796 !'##molecule_type DNA !'##residues 1-729 ##label MEL !'##cross-references GB:M31719; NID:g171774; PIDN:AAA34715.1; !1PID:g171775 REFERENCE S69022 !$#authors Fulton, L. !$#submission submitted to the EMBL Data Library, November 1995 !$#description The sequence of S. cerevisiae cosmid 9659. !$#accession S69030 !'##molecule_type DNA !'##residues 1-729 ##label FUL !'##cross-references EMBL:U40829; NID:g1066476; PIDN:AAB68281.1; !1PID:g1066492; GSPDB:GN00016; MIPS:YPR141c GENETICS !$#gene SGD:KAR3; MIPS:YPR141c !'##cross-references SGD:S0006345; MIPS:YPR141c !$#map_position 16R CLASSIFICATION #superfamily kinesin-related protein KLPA; kinesin motor !1domain homology KEYWORDS coiled coil; GTP binding; microtubule binding; mitosis; !1nucleotide binding; P-loop FEATURE !$1-109 #domain globular #status predicted #label GBD\ !$110-385 #domain coiled coil #status predicted #label COI\ !$387-729 #domain kinesin motor domain homology #label KMOT\ !$474-481 #region nucleotide-binding motif A (P-loop)\ !$537-540 #region GTP-binding NKXD motif\ !$480 #binding_site ATP (Lys) #status predicted SUMMARY #length 729 #molecular-weight 84003 #checksum 6307 SEQUENCE /// ENTRY JC6161 #type complete TITLE kinesin-associated protein KAP3 splice form A - mouse ALTERNATE_NAMES KAP3A ORGANISM #formal_name Mus musculus #common_name house mouse DATE 11-Apr-1997 #sequence_revision 09-May-1997 #text_change 16-Jun-2000 ACCESSIONS JC6161; PC6040 REFERENCE JC6161 !$#authors Yamazaki, H.; Nakata, T.; Okada, Y.; Hirokawa, N. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1996) 93:8443-8448 !$#title Cloning and characterization of KAP3: A novel kinesin !1superfamily-associated protein of KIF3A/3B. !$#cross-references MUID:96323241; PMID:8710890 !$#accession JC6161 !'##molecule_type mRNA !'##residues 1-793 ##label YAM1 !'##cross-references DDBJ:D50366; NID:g1526418; PIDN:BAA08901.1; !1PID:g1526419 !'##experimental_source brain !$#accession PC6040 !'##molecule_type protein !'##residues 86-106;150-184;486-498 ##label YAM2 !'##experimental_source testis COMMENT This globular protein binds to the tail globular domain of !1the KIF3A/3B heterodimer. It may regulate the membrane !1binding of KIF3A/3B. COMPLEX associates with heterodimer of KIF3A (PIR:B44259) and KIF3B !1(PIR:A57107) to form a heterotrimer, the KIF3 complex FUNCTION !$#description KIF3 complex is a motor protein that provides anterograde !1fast axonal transport of membranous organelles CLASSIFICATION #superfamily kinesin-associated protein KAP3 KEYWORDS alternative splicing; heterotrimer SUMMARY #length 793 #molecular-weight 91290 #checksum 94 SEQUENCE /// ENTRY A42336 #type complete TITLE tropomodulin - human ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 22-Jun-1999 ACCESSIONS A42336 REFERENCE A42336 !$#authors Sung, L.A.; Fowler, V.M.; Lambert, K.; Sussman, M.A.; Karr, !1D.; Chien, S. !$#journal J. Biol. Chem. (1992) 267:2616-2621 !$#title Molecular cloning and characterization of human fetal liver !1tropomodulin. A tropomyosin-binding protein. !$#cross-references MUID:92129352; PMID:1370827 !$#accession A42336 !'##molecule_type mRNA !'##residues 1-359 ##label SUN !'##cross-references GB:M77016; NID:g339947; PIDN:AAA61224.1; !1PID:g339948 !'##experimental_source fetal liver cDNA expression library !'##note sequence extracted from NCBI backbone (NCBIN:78698, !1NCBIP:78699) !'##note parts of this sequence were confirmed by sequencing fragments !1of erythocyte tropomodulin REFERENCE PC2283 !$#authors Sung, L.A.; Lin, J.J.C. !$#journal Biochem. Biophys. Res. Commun. (1994) 201:627-634 !$#title Erythrocyte tropomodulin binds to the N-terminus of hTM5, a !1tropomyosin isoform encoded by the gamma-tropomyosin gene. !$#cross-references MUID:94271211; PMID:8002995 !$#contents annotation GENETICS !$#gene GDB:TMOD; D9S57E !'##cross-references GDB:127386; OMIM:190930 !$#map_position 9q22.2-9q22.3 FUNCTION !$#description modulates the binding of certain isoforms of tropomyosin to !1actin filaments CLASSIFICATION #superfamily tropomodulin KEYWORDS cytoskeleton FEATURE !$6-94 #region tropomyosin skeletal muscle isoform-binding\ !$90-184 #region tropomyosin erythrocyte isoform-binding SUMMARY #length 359 #molecular-weight 40569 #checksum 1400 SEQUENCE /// ENTRY I53091 #type complete TITLE tropomodulin - mouse ORGANISM #formal_name Mus sp. #common_name mouse DATE 02-Aug-1996 #sequence_revision 02-Aug-1996 #text_change 22-Jun-1999 ACCESSIONS I53091 REFERENCE I53091 !$#authors Ito, M.; Swanson, B.; Sussman, M.A.; Kedes, L.; Lyons, G. !$#journal Dev. Biol. (1995) 167:317-328 !$#title Cloning of tropomodulin cDNA and localization of gene !1transcripts during mouse embryogenesis. !$#cross-references MUID:95154574; PMID:7851652 !$#accession I53091 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-359 ##label RES !'##cross-references GB:S76831; NID:g914213; PIDN:AAB33388.1; !1PID:g914214 GENETICS !$#gene Tmod FUNCTION !$#description modulates the binding of certain isoforms of tropomyosin to !1actin filaments CLASSIFICATION #superfamily tropomodulin KEYWORDS cytoskeleton SUMMARY #length 359 #molecular-weight 40484 #checksum 1096 SEQUENCE /// ENTRY A55463 #type complete TITLE tropomodulin, skeletal muscle - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 23-Mar-1995 #sequence_revision 23-Mar-1995 #text_change 22-Jun-1999 ACCESSIONS A55463 REFERENCE A55463 !$#authors Babcock, G.G.; Fowler, V.M. !$#journal J. Biol. Chem. (1994) 269:27510-27518 !$#title Isoform-specific interaction of tropomodulin with skeletal !1muscle and erythrocyte tropomyosins. !$#cross-references MUID:95050495; PMID:7961666 !$#accession A55463 !'##status preliminary !'##molecule_type mRNA !'##residues 1-359 ##label BAB !'##cross-references GB:L36678; NID:g562262; PIDN:AAC14459.1; !1PID:g562263 FUNCTION !$#description modulates the binding of certain isoforms of tropomyosin to !1actin filaments CLASSIFICATION #superfamily tropomodulin KEYWORDS cytoskeleton; skeletal muscle SUMMARY #length 359 #molecular-weight 40340 #checksum 9456 SEQUENCE /// ENTRY TMRBA #type complete TITLE tropomyosin alpha chain, cardiac and skeletal muscle [validated] - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 31-Mar-1980 #sequence_revision 08-Oct-1981 #text_change 16-Jun-2000 ACCESSIONS I47056; A92222; A92282; I46508; A02978 REFERENCE I47056 !$#authors Kluwe, L.; Maeda, K.; Miegel, A.; Fujita-Becker, S.; Maeda, !1Y.; Talbo, G.; Houthaeve, T.; Kellner, R. !$#journal J. Muscle Res. Cell. Motil. (1995) 16:103-110 !$#title Rabbit skeletal muscle alpha alpha-tropomyosin expressed in !1baculovirus-infected insect cells possesses the authentic !1N-terminus structure and functions. !$#cross-references MUID:95348266; PMID:7622625 !$#accession I47056 !'##molecule_type mRNA !'##residues 1-284 ##label KLU !'##cross-references GB:S78854; NID:g1042002; PIDN:AAB34957.1; !1PID:g1042003 REFERENCE A92222 !$#authors Stone, D.; Smillie, L.B. !$#journal J. Biol. Chem. (1978) 253:1137-1148 !$#title The amino acid sequence of rabbit skeletal !1alpha-tropomyosin. The NH-2-terminal half and complete !1sequence. !$#cross-references MUID:78109457; PMID:624724 !$#accession A92222 !'##molecule_type protein !'##residues 1-284 ##label STO !'##experimental_source skeletal muscle REFERENCE A92282 !$#authors Lewis, W.G.; Smillie, L.B. !$#journal J. Biol. Chem. (1980) 255:6854-6859 !$#title The amino acid sequence of rabbit cardiac tropomyosin. !$#cross-references MUID:80227850; PMID:6993480 !$#accession A92282 !'##molecule_type protein !'##residues 1-284 ##label LEW !'##experimental_source cardiac muscle REFERENCE A93819 !$#authors Mak, A.; Smillie, L.B.; Barany, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1978) 75:3588-3592 !$#title Specific phosphorylation at serine-283 of alpha tropomyosin !1from frog skeletal and rabbit skeletal and cardiac muscle. !$#cross-references MUID:79012453; PMID:278975 !$#contents annotation; skeletal muscle, phosphorylation site REFERENCE I46471 !$#authors Putney, S.D.; Herlihy, W.C.; Schimmel, P. !$#journal Nature (1983) 302:718-721 !$#title A new troponin T and cDNA clones for 13 different muscle !1proteins, found by shotgun sequencing. !$#cross-references MUID:83167564; PMID:6687628 !$#accession I46508 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 103-146 ##label PUT !'##cross-references EMBL:V00892; NID:g1726; PIDN:CAA24257.1; !1PID:g929762 COMMENT The molecule is a coiled coil of two similar helical chains. !1The sequence exhibits a prominent seven-residue periodicity. CLASSIFICATION #superfamily tropomyosin KEYWORDS acetylated amino end; cardiac muscle; coiled coil; heart; !1phosphoprotein FEATURE !$1-284 #product tropomyosin alpha chain #status experimental !8#label MAT\ !$1 #modified_site acetylated amino end (Met) #status !8experimental\ !$283 #binding_site phosphate (Ser) (covalent) (partial) !8#status experimental SUMMARY #length 284 #molecular-weight 32680 #checksum 394 SEQUENCE /// ENTRY TMCHA #type complete TITLE tropomyosin 2, skeletal muscle alpha splice form CTm7 - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 05-Apr-1983 #sequence_revision 18-Jul-1997 #text_change 22-Jun-1999 ACCESSIONS S24399; I50434; A02979; A26985; PC2286 REFERENCE S24399 !$#authors Lemonnier, M.; Balvay, L.; Mouly, V.; Libri, D.; Fiszman, !1M.Y. !$#journal Gene (1991) 107:229-240 !$#title The chicken gene encoding the alpha isoform of tropomyosin !1of fast-twitch muscle fibers: organization, expression and !1identification of the major proteins synthesized. !$#cross-references MUID:92084115; PMID:1748294 !$#accession S24399 !'##status translation not shown !'##molecule_type DNA !'##residues 1-284 ##label LEM !'##cross-references EMBL:X57994 REFERENCE I50433 !$#authors Fanning, A.S.; Wolenski, J.S.; Mooseker, M.S.; Izant, J.G. !$#journal Cell Motil. Cytoskeleton (1994) 29:29-45 !$#title Differential regulation of skeletal muscle myosin-II and !1brush border myosin-I enzymology and mechanochemistry by !1bacterially produced tropomyosin isoforms. !$#cross-references MUID:95120819; PMID:7820856 !$#accession I50434 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-284 ##label FAN !'##cross-references GB:M36337; NID:g212818; PIDN:AAA65121.1; !1PID:g212819 !'##note this form was designated CTm7 REFERENCE A02979 !$#authors MacLeod, A.R. !$#journal Eur. J. Biochem. (1982) 126:293-297 !$#title Distinct alpha-tropomyosin mRNA sequences in chicken !1skeletal muscle. !$#cross-references MUID:83027321; PMID:7128591 !$#accession A02979 !'##molecule_type mRNA !'##residues 24-284 ##label MAC !'##cross-references GB:J00910; NID:g212814; PIDN:AAA49113.1; !1PID:g212815 REFERENCE A26985 !$#authors Gooding, C.; Reinach, F.C.; Macleod, A.R. !$#journal Nucleic Acids Res. (1987) 15:8105 !$#title Complete nucleotide sequence of the fast-twitch isoform of !1chicken skeletal muscle alpha-tropomyosin. !$#cross-references MUID:88040430; PMID:3671073 !$#accession A26985 !'##molecule_type mRNA !'##residues 1-164,'A',166-284 ##label GOO !'##cross-references GB:M32441; NID:g211225; PIDN:AAA48610.1; !1PID:g211226 REFERENCE PC2283 !$#authors Sung, L.A.; Lin, J.J.C. !$#journal Biochem. Biophys. Res. Commun. (1994) 201:627-634 !$#title Erythrocyte tropomodulin binds to the N-terminus of hTM5, a !1tropomyosin isoform encoded by the gamma-tropomyosin gene. !$#cross-references MUID:94271211; PMID:8002995 !$#contents annotation; tropomodulin binding to tropomyosin GENETICS !$#gene TM2 !$#introns 38/3; 80/3; 125/3; 164/3; 188/2; 213/3; 234/3; 258/1 CLASSIFICATION #superfamily tropomyosin KEYWORDS actin binding; alternative splicing; coiled coil; muscle; !1skeletal muscle SUMMARY #length 284 #molecular-weight 32765 #checksum 325 SEQUENCE /// ENTRY TMRBB #type complete TITLE tropomyosin beta chain, skeletal muscle [validated] - rabbit (tentative sequence) ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 31-Jul-1980 #sequence_revision 31-Jul-1980 #text_change 16-Jun-2000 ACCESSIONS A02980; I46509 REFERENCE A02980 !$#authors Mak, A.S.; Smillie, L.B.; Steward, G.R. !$#journal J. Biol. Chem. (1980) 255:3647-3655 !$#title A comparison of the amino acid sequences of rabbit skeletal !1muscle alpha- and beta-tropomyosins. !$#cross-references MUID:80159993; PMID:7364764 !$#accession A02980 !'##molecule_type protein !'##residues 1-284 ##label MAK !'##note peptides that appeared to be identical with corresponding !1peptides of tropomyosin alpha chain were not sequenced. Some !1peptides have been ordered solely on the basis of homology !'##note minor heterogeneity was detected at 11 positions REFERENCE I46471 !$#authors Putney, S.D.; Herlihy, W.C.; Schimmel, P. !$#journal Nature (1983) 302:718-721 !$#title A new troponin T and cDNA clones for 13 different muscle !1proteins, found by shotgun sequencing. !$#cross-references MUID:83167564; PMID:6687628 !$#accession I46509 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 131-172 ##label PUT !'##cross-references EMBL:V00893; NID:g1728; PIDN:CAA24258.1; !1PID:g929763 CLASSIFICATION #superfamily tropomyosin KEYWORDS acetylated amino end; alternative splicing; coiled coil FEATURE !$1-284 #product tropomyosin beta chain #status experimental !8#label MAT\ !$1 #modified_site acetylated amino end (Met) #status !8experimental SUMMARY #length 284 #molecular-weight 32836 #checksum 911 SEQUENCE /// ENTRY TMRTF1 #type complete TITLE tropomyosin 1, embryonic fibroblast - rat ALTERNATE_NAMES TM-1 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 10-Dec-1999 ACCESSIONS A02981; A25073 REFERENCE A02981 !$#authors Yamawaki-Kataoka, Y.; Helfman, D.M. !$#journal J. Biol. Chem. (1985) 260:14440-14445 !$#title Rat embryonic fibroblast tropomyosin 1. cDNA and complete !1primary amino acid sequence. !$#cross-references MUID:86033945; PMID:3840484 !$#accession A02981 !'##molecule_type mRNA !'##residues 1-284 ##label YAM REFERENCE A93081 !$#authors Helfman, D.M.; Cheley, S.; Kuismanen, E.; Finn, L.A.; !1Yamawaki-Kataoka, Y. !$#journal Mol. Cell. Biol. (1986) 6:3582-3595 !$#title Nonmuscle and muscle tropomyosin isoforms are expressed from !1a single gene by alternative RNA splicing and !1polyadenylation. !$#cross-references MUID:87089698; PMID:2432392 !$#accession A25073 !'##molecule_type mRNA !'##residues 1-284 ##label HEL !'##cross-references GB:L00382; GB:M14127; NID:g207495; PIDN:AAA42289.1; !1PID:g207498 COMMENT Rat embryonic fibroblasts contain three major (1, 2, and 4) !1and two minor (3 and 5) TM isoforms. The homology between !1this protein and the alpha-tropomyosin of the chicken smooth !1muscle indicates that they belong to the same isotype. COMMENT The presence of TM in cells devoid of troponin (nonmuscle !1and smooth muscle cells) suggests that it fulfills a role !1other than actin-myosin regulation in these cells. Also, the !1tropomyosins of these cell types, unlike skeletal and !1cardiac muscle TM, do not appear to be subject to regulation !1by phosphorylation (of a carboxyl-terminal serine). CLASSIFICATION #superfamily tropomyosin KEYWORDS alternative splicing; coiled coil SUMMARY #length 284 #molecular-weight 32957 #checksum 1501 SEQUENCE /// ENTRY TMCHS1 #type complete TITLE tropomyosin 1, smooth muscle alpha splice form - chicken ALTERNATE_NAMES gizzard beta-tropomyosin; tropomyosin beta chain, smooth muscle ORGANISM #formal_name Gallus gallus #common_name chicken DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 10-Dec-1999 ACCESSIONS A92462; A92537; B31433; I50685; A02982; PC2288 REFERENCE A92462 !$#authors Helfman, D.M.; Feramisco, J.R.; Ricci, W.M.; Hughes, S.H. !$#journal J. Biol. Chem. (1984) 259:14136-14143 !$#title Isolation and sequence of a cDNA clone that contains the !1entire coding region for chicken smooth-muscle !1alpha-tropomyosin. !$#cross-references MUID:85054861; PMID:6548747 !$#accession A92462 !'##molecule_type mRNA !'##residues 1-284 ##label HEL !'##cross-references GB:K02446; NID:g212806; PIDN:AAA49109.1; !1PID:g212807 REFERENCE A92537 !$#authors Sanders, C.; Smillie, L.B. !$#journal J. Biol. Chem. (1985) 260:7264-7275 !$#title Amino acid sequence of chicken gizzard beta-tropomyosin. !1Comparison of the chicken gizzard, rabbit skeletal, and !1equine platelet tropomyosins. !$#cross-references MUID:85207759; PMID:3997867 !$#accession A92537 !'##molecule_type protein !'##residues 1-284 ##label SAN !'##note the sequence is based in part on homology with rabbit skeletal !1muscle tropomyosins REFERENCE A31433 !$#authors Libri, D.; Lemonnier, M.; Meinnel, T.; Fiszman, M.Y. !$#journal J. Biol. Chem. (1989) 264:2935-2944 !$#title A single gene codes for the beta-subunits of smooth and !1skeletal muscle tropomyosin in the chicken. !$#cross-references MUID:89123396; PMID:2914939 !$#accession B31433 !'##molecule_type DNA !'##residues 1-284 ##label LIB !'##note the authors translated the codon ATC for residue 19 as Thr, and !1TTA for residue 256 as Phe REFERENCE PC2283 !$#authors Sung, L.A.; Lin, J.J.C. !$#journal Biochem. Biophys. Res. Commun. (1994) 201:627-634 !$#title Erythrocyte tropomodulin binds to the N-terminus of hTM5, a !1tropomyosin isoform encoded by the gamma-tropomyosin gene. !$#cross-references MUID:94271211; PMID:8002995 !$#contents annotation REFERENCE I50685 !$#authors Helfman, D.M.; Feramisco, J.R.; Fiddes, J.C.; Thomas, G.P.; !1Hughes, S.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:31-35 !$#title Identification of clones that encode chicken tropomyosin by !1direct immunological screening of a cDNA expression library. !$#cross-references MUID:83117845; PMID:6185958 !$#accession I50685 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 151-187 ##label HE2 !'##cross-references EMBL:V00445; NID:g63837; PIDN:CAA23724.1; !1PID:g929598 GENETICS !$#gene TM1 CLASSIFICATION #superfamily tropomyosin KEYWORDS actin binding; alternative splicing; blocked amino end; !1coiled coil FEATURE !$1 #modified_site blocked amino end (Met) (probably !8acetylated) #status experimental SUMMARY #length 284 #molecular-weight 32853 #checksum 2919 SEQUENCE /// ENTRY TMCHS2 #type complete TITLE tropomyosin 2, gizzard gamma splice form - chicken ALTERNATE_NAMES gizzard gamma-tropomyosin ORGANISM #formal_name Gallus gallus #common_name chicken DATE 04-Dec-1986 #sequence_revision 18-Jul-1997 #text_change 10-Dec-1999 ACCESSIONS S24400; A02983; PC2287 REFERENCE S24399 !$#authors Lemonnier, M.; Balvay, L.; Mouly, V.; Libri, D.; Fiszman, !1M.Y. !$#journal Gene (1991) 107:229-240 !$#title The chicken gene encoding the alpha isoform of tropomyosin !1of fast-twitch muscle fibers: organization, expression and !1identification of the major proteins synthesized. !$#cross-references MUID:92084115; PMID:1748294 !$#accession S24400 !'##status preliminary; translation not shown !'##molecule_type DNA !'##residues 1-284 ##label LEM !'##cross-references EMBL:X57994 REFERENCE A02983 !$#authors Lau, S.Y.M.; Sanders, C.; Smillie, L.B. !$#journal J. Biol. Chem. (1985) 260:7257-7263 !$#title Amino acid sequence of chicken gizzard gamma-tropomyosin. !$#cross-references MUID:85207758; PMID:3997866 !$#accession A02983 !'##molecule_type protein !'##residues 1-72,'S',74-171,'L',173-198,'L',200-202,'EA',205-284 !1##label LAU !'##note the sequence is based in part on homology with rabbit skeletal !1muscle tropomyosins !'##note 70-Asx, 171-Val, and 175-Glu were also found REFERENCE PC2283 !$#authors Sung, L.A.; Lin, J.J.C. !$#journal Biochem. Biophys. Res. Commun. (1994) 201:627-634 !$#title Erythrocyte tropomodulin binds to the N-terminus of hTM5, a !1tropomyosin isoform encoded by the gamma-tropomyosin gene. !$#cross-references MUID:94271211; PMID:8002995 !$#contents annotation; tropomodulin binding to tropomyosin COMMENT This is one of two major tropomyosin forms found in adult !1chicken smooth muscle (gizzard). GENETICS !$#gene TM2 !$#introns 38/3; 80/3; 125/3; 164/3; 188/2; 213/3; 234/3; 258/1 CLASSIFICATION #superfamily tropomyosin KEYWORDS actin binding; alternative splicing; blocked amino end; !1coiled coil FEATURE !$1 #modified_site blocked amino end (Met) (probably !8acetylated) #status experimental SUMMARY #length 284 #molecular-weight 32925 #checksum 3200 SEQUENCE /// ENTRY TMHOBP #type complete TITLE tropomyosin beta chain, platelet - horse ORGANISM #formal_name Equus caballus #common_name domestic horse DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 28-Feb-1997 ACCESSIONS A02984 REFERENCE A02984 !$#authors Lewis, W.G.; Cote, G.P.; Mak, A.S.; Smillie, L.B. !$#journal FEBS Lett. (1983) 156:269-273 !$#title Amino acid sequence of equine platelet tropomyosin. !1Correlation with interaction properties. !$#cross-references MUID:83210221; PMID:6852260 !$#accession A02984 !'##molecule_type protein !'##residues 1-247 ##label LEW COMMENT This protein is similar to muscle tropomyosin in its !17-residue periodicity and amino acid composition, but it !1differs significantly in its length and in the sequences of !1its amino and carboxyl ends. These differences can be !1correlated with its weaker head-to-tail polymerization, !1binding with actin, and interaction with troponins, compared !1with muscle tropomyosin. COMMENT This protein can span only six actin monomers. CLASSIFICATION #superfamily tropomyosin KEYWORDS coiled coil; platelet; tandem repeat FEATURE !$1-247 #region 7-residue repeats SUMMARY #length 247 #molecular-weight 28391 #checksum 2794 SEQUENCE /// ENTRY A46762 #type complete TITLE myosin alpha heavy chain, cardiac muscle - human CONTAINS myosin ATPase (EC 3.6.4.1) ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 19-Apr-2002 ACCESSIONS A46762; B46762; A49354; S18830; B32562; B33835; B27858; !1A28908 REFERENCE A46762 !$#authors Matsuoka, R.; Beisel, K.W.; Furutani, M.; Arai, S.; Takao, !1A. !$#journal Am. J. Med. Genet. (1991) 41:537-547 !$#title Complete sequence of human cardiac alpha-myosin heavy chain !1gene and amino acid comparison to other myosins based on !1structural and functional differences. !$#cross-references MUID:92133665; PMID:1776652 !$#accession A46762 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-1939 ##label MAT !'##cross-references DDBJ:D00943; NID:g219523; PIDN:BAA00791.1; !1PID:g219524 !$#accession B46762 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-1461 ##label MA2 REFERENCE A49354 !$#authors Epp, T.A.; Dixon, I.M.C.; Wang, H.Y.; Sole, M.J.; Liew, C.C. !$#journal Genomics (1993) 18:505-509 !$#title Structural organization of the human cardiac alpha-myosin !1heavy chain gene (MYH6). !$#cross-references MUID:94140346; PMID:8307559 !$#accession A49354 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-87,'Q',89-573,'Q',575-607,'A',609-743,'T',745-789,'M', !1791-1013,'V',1015-1020,'S',1022-1100,'A',1102-1289,'A', !11291-1372,'W',1374-1704,'EQ',1707-1732,'ES',1735-1736,'T', !11738-1762,'D',1764-1939 ##label EPP !'##cross-references GB:Z20656; NID:g297023; PIDN:CAA79675.1; !1PID:g297024 REFERENCE S18830 !$#authors Brand, N.J.; Dabhade, N.; Yacoub, M.; Barton, P.J.R. !$#journal Biochem. Biophys. Res. Commun. (1991) 179:1255-1258 !$#title Determination of the 5' exon structure of the human cardiac !1alpha-myosin heavy chain gene. !$#cross-references MUID:92028859; PMID:1930170 !$#accession S18830 !'##status preliminary !'##molecule_type mRNA !'##residues 1-32 ##label BRA !'##cross-references EMBL:X56181; NID:g28318; PIDN:CAA39642.1; !1PID:g28319 REFERENCE A94224 !$#authors Yamauchi-Takihara, K.; Sole, M.J.; Liew, J.; Ing, D.; Liew, !1C.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:3504-3508 !$#title Characterization of human cardiac myosin heavy chain genes. !$#cross-references MUID:89264452; PMID:2726733 !$#accession B32562 !'##molecule_type DNA !'##residues 1-87,'Q',89-177;1551-1732,'E',1734-1736,'T',1738-1762,'D', !11764-1848 ##label YA1 REFERENCE A94226 !$#authors Yamauchi-Takihara, K.; Sole, M.J.; Liew, J.; Ing, D.; Liew, !1C.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:7416-7417 !$#contents erratum !$#accession B33835 !'##molecule_type DNA !'##residues 1-87,'Q',89-177;1551-1732,'E',1734-1736,'T',1738-1762,'D', !11764-1939 ##label YA2 REFERENCE A93669 !$#authors Saez, L.J.; Gianola, K.M.; McNally, E.M.; Feghali, R.; Eddy, !1R.; Shows, T.B.; Leinwand, L.A. !$#journal Nucleic Acids Res. (1987) 15:5443-5459 !$#title Human cardiac myosin heavy chain genes and their linkage in !1the genome. !$#cross-references MUID:87260010; PMID:3037493 !$#accession B27858 !'##molecule_type DNA !'##residues 1-3,'S',5-10,'T',12,14-67 ##label SAE REFERENCE A92770 !$#authors Kurabayashi, M.; Tsuchimochi, H.; Komuro, I.; Takaku, F.; !1Yazaki, Y. !$#journal J. Clin. Invest. (1988) 82:524-531 !$#title Molecular cloning and characterization of human cardiac !1alpha- and beta-form myosin heavy chain complementary DNA !1clones. Regulation of expression during development and !1pressure overload in human atrium. !$#cross-references MUID:88299163; PMID:2969919 !$#accession A28908 !'##molecule_type mRNA !'##residues 1407-1532,'N',1534-1539,'M',1541-1576,'NV',1579-1704,'EQ', !11707-1762,'D',1764-1870,'N',1872-1881,'G',1883-1889,'R', !11891-1932,1934-1939 ##label KUR !'##cross-references GB:M21664; NID:g189006; PIDN:AAA36344.1; !1PID:g386972 !'##experimental_source fetal heart GENETICS !$#gene GDB:MYH6 !'##cross-references GDB:120214; OMIM:160710 !$#map_position 14q11.2-14q13 CLASSIFICATION #superfamily myosin heavy chain; myosin motor domain !1homology KEYWORDS actin binding; ATP; cardiac muscle; coiled coil; heart; !1hydrolase; methylated amino acid; muscle contraction; !1nucleotide binding; P-loop; tandem repeat; thick filament FEATURE !$88-768 #domain myosin motor domain homology #label MMOT\ !$178-185 #region nucleotide-binding motif A (P-loop)\ !$549-586 #region actin binding #status predicted\ !$657-679 #region actin binding #status predicted\ !$841-1939 #domain coiled coil #status predicted #label COI\ !$841-1281 #region S2\ !$1282-1939 #region light meromyosin\ !$129 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8predicted\ !$184 #binding_site ATP (Lys) #status predicted\ !$697,707 #active_site Cys #status predicted SUMMARY #length 1939 #molecular-weight 223551 #checksum 4405 SEQUENCE /// ENTRY S06005 #type complete TITLE myosin alpha heavy chain, cardiac muscle [similarity] - rat ALTERNATE_NAMES alpha-myosin heavy chain CONTAINS myosin ATPase (EC 3.6.4.1) ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 19-Apr-2002 ACCESSIONS S06005; S07535; A20971; A02988; I53305 REFERENCE S06005 !$#authors McNally, E.M.; Gianola, K.M.; Leinwand, L.A. !$#journal Nucleic Acids Res. (1989) 17:7527-7528 !$#title Complete nucleotide sequence of full length cDNA for rat !1alpha cardiac myosin heavy chain. !$#cross-references MUID:90016822; PMID:2798111 !$#accession S06005 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-1938 ##label MCN !'##cross-references EMBL:X15938; NID:g56654; PIDN:CAA34064.1; !1PID:g56655 REFERENCE S07535 !$#authors McNally, E.M.; Kraft, R.; Bravo-Zehnder, M.; Taylor, D.A.; !1Leinwand, L.A. !$#journal J. Mol. Biol. (1989) 210:665-671 !$#title Full-length rat alpha and beta cardiac myosin heavy chain !1sequences. Comparisons suggest a molecular basis for !1functional differences. !$#cross-references MUID:90133919; PMID:2614840 !$#accession S07535 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-1938 ##label MC2 REFERENCE A20971 !$#authors Mahdavi, V.; Chambers, A.P.; Nadal-Ginard, B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:2626-2630 !$#title Cardiac alpha- and beta-myosin heavy chain genes are !1organized in tandem. !$#cross-references MUID:84194059; PMID:6585819 !$#accession A20971 !'##molecule_type protein !'##residues 1-12,'AP',14-45,'A',47-50,'AP',53-81,'E',83-86,'Q',88-109, !1111-133,'H',135-166 ##label MAH REFERENCE A02988 !$#authors Mahdavi, V.; Periasamy, M.; Nadal-Ginard, B. !$#journal Nature (1982) 297:659-664 !$#title Molecular characterization of two myosin heavy chain genes !1expressed in the adult heart. !$#cross-references MUID:82220036; PMID:7045682 !$#accession A02988 !'##molecule_type mRNA !'##residues 1512-1574,'S',1576-1721,'N',1723-1851,'N',1853-1869,'N', !11871-1933,'I',1935-1938 ##label MA2 !'##note there are 10 or more myosin heavy chain genes in the rat, at !1least two of which are specific for adult cardiac myosin !1heavy chains REFERENCE I53305 !$#authors Mahdavi, V.; Lompre, A.M.; Chambers, A.P.; Nadal-Ginard, B. !$#journal Eur. Heart J. (1984) 5:181-191 !$#title Cardiac myosin heavy chain isozymic transitions during !1development and under pathological conditions are regulated !1at the level of mRNA availability. !$#cross-references MUID:85179510; PMID:6241892 !$#accession I53305 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1872-1933,'I',1935-1938 ##label RES !'##cross-references GB:M32697; NID:g205596; PIDN:AAA41658.1; !1PID:g205597 CLASSIFICATION #superfamily myosin heavy chain; myosin motor domain !1homology KEYWORDS actin binding; ATP; cardiac muscle; coiled coil; heart; !1hydrolase; methylated amino acid; muscle contraction; !1nucleotide binding; P-loop; tandem repeat; thick filament FEATURE !$87-767 #domain myosin motor domain homology #label MMOT\ !$177-184 #region nucleotide-binding motif A (P-loop)\ !$548-585 #region actin binding #status predicted\ !$656-678 #region actin binding #status predicted\ !$840-1938 #domain coiled coil #status predicted #label COI\ !$840-1280 #region S2\ !$1281-1938 #region light meromyosin\ !$128 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8predicted\ !$183 #binding_site ATP (Lys) #status predicted\ !$696,706 #active_site Cys #status predicted SUMMARY #length 1938 #molecular-weight 223507 #checksum 572 SEQUENCE /// ENTRY A37102 #type complete TITLE myosin beta heavy chain, cardiac and skeletal muscle - human CONTAINS myosin ATPase (EC 3.6.4.1) ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 19-Apr-2002 ACCESSIONS A37102; S12733; A94224; B28908; A24997; A27858; I54254; !1S12458; S09331; S02229; B23767; A32562; A33835 REFERENCE A37102 !$#authors Jaenicke, T.; Diederich, K.W.; Haas, W.; Schleich, J.; !1Lichter, P.; Pfordt, M.; Bach, A.; Vosberg, H.P. !$#journal Genomics (1990) 8:194-206 !$#title The complete sequence of the human beta-myosin heavy chain !1gene and a comparative analysis of its product. !$#cross-references MUID:91065634; PMID:2249844 !$#accession A37102 !'##molecule_type DNA !'##residues 1-1935 ##label JAE !'##cross-references GB:M57965; GB:M30603; NID:g179507; PIDN:AAA51837.1; !1PID:g179508; GB:M30604; GB:M30605 REFERENCE S12733 !$#authors Liew, C.C.; Sole, M.J.; Yamauchi-Takihara, K.; Kellam, B.; !1Anderson, D.H.; Lin, L.; Liew, J.C. !$#journal Nucleic Acids Res. (1990) 18:3647-3651 !$#title Complete sequence and organization of the human cardiac !1beta-myosin heavy chain gene. !$#cross-references MUID:90301496; PMID:2362820 !$#accession S12733 !'##molecule_type DNA !'##residues 1-106,'E',108-671,'LYH',675-857,'A',859-941,'NV',944-1123, !1'A',1125-1158,'C',1160-1680,1682-1702,'DR',1705-1935 ##label !1LIE !'##cross-references EMBL:X52889; NID:g29726; PIDN:CAA37068.1; !1PID:g29727 REFERENCE A94224 !$#authors Yamauchi-Takihara, K.; Sole, M.J.; Liew, J.; Ing, D.; Liew, !1C.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:3504-3508 !$#title Characterization of human cardiac myosin heavy chain genes. !$#cross-references MUID:89264452; PMID:2726733 !$#accession A94224 !'##molecule_type DNA !'##residues 1-87,'Q',89-106,'E',108-177;1325-1702,'DR',1705-1786, !11788-1803,'E',1804-1935 ##label YAM REFERENCE A94226 !$#authors Yamauchi-Takihara, K.; Sole, M.J.; Liew, J.; Ing, D.; Liew, !1C.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:7416-7417 !$#contents annotation; erratum REFERENCE A92770 !$#authors Kurabayashi, M.; Tsuchimochi, H.; Komuro, I.; Takaku, F.; !1Yazaki, Y. !$#journal J. Clin. Invest. (1988) 82:524-531 !$#title Molecular cloning and characterization of human cardiac !1alpha- and beta-form myosin heavy chain complementary DNA !1clones. Regulation of expression during development and !1pressure overload in human atrium. !$#cross-references MUID:88299163; PMID:2969919 !$#accession B28908 !'##molecule_type mRNA !'##residues 1412-1518,'R',1520-1574,'NV',1577-1935 ##label KUR !'##cross-references GB:M21665 !'##note the authors translated the codon AGC for residue 108 as Arg REFERENCE A24997 !$#authors Lichter, P.; Umeda, P.K.; Levin, J.E.; Vosberg, H.P. !$#journal Eur. J. Biochem. (1986) 160:419-426 !$#title Partial characterization of the human beta-myosin !1heavy-chain gene which is expressed in heart and skeletal !1muscle. !$#cross-references MUID:87030293; PMID:3021460 !$#accession A24997 !'##molecule_type DNA !'##residues 682-721;975-1112;1854-1935 ##label LIC !'##cross-references GB:X04627 REFERENCE A93669 !$#authors Saez, L.J.; Gianola, K.M.; McNally, E.M.; Feghali, R.; Eddy, !1R.; Shows, T.B.; Leinwand, L.A. !$#journal Nucleic Acids Res. (1987) 15:5443-5459 !$#title Human cardiac myosin heavy chain genes and their linkage in !1the genome. !$#cross-references MUID:87260010; PMID:3037493 !$#accession A27858 !'##molecule_type DNA !'##residues 1854-1865,'A',1867-1935 ##label SAE !'##cross-references GB:X05631; GB:Y00362; NID:g34643; PIDN:CAA29119.1; !1PID:g34644 REFERENCE I54254 !$#authors Diederich, K.W.; Eisele, I.; Ried, T.; Jaenicke, T.; !1Lichter, P.; Vosberg, H.P. !$#journal Hum. Genet. (1989) 81:214-220 !$#title Isolation and characterization of the complete human !1beta-myosin heavy chain gene. !$#cross-references MUID:89154425; PMID:2522082 !$#accession I54254 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 653-720 ##label RES !'##cross-references GB:M27636; NID:g179511; PIDN:AAA79019.1; !1PID:g601916 REFERENCE S12458 !$#authors Bober, E. !$#submission submitted to the EMBL Data Library, January 1989 !$#accession S12458 !'##molecule_type mRNA !'##residues 785-1076,'E',1078-1123,'A',1125-1702,'DE',1705-1935 ##label !1BOB !'##cross-references EMBL:X51591; NID:g29467; PIDN:CAA35940.1; !1PID:g29468 REFERENCE S09331 !$#authors Bober, E.; Buchberger-Seidl, A.; Braun, T.; Singh, S.; !1Goedde, H.W.; Arnold, H.H. !$#journal Eur. J. Biochem. (1990) 189:55-65 !$#title Identification of three developmentally controlled isoforms !1of human myosin heavy chains. !$#cross-references MUID:90235862; PMID:1691980 !$#accession S09331 !'##molecule_type mRNA !'##residues 785-830,'X',832-900,'X',902-970,'X',972-1040,'X',1042-1076, !1'E',1078-1110,'X',1112-1123,'A',1125-1180,'X',1182-1250,'X', !11252-1320,'X',1322-1390,'X',1392-1460,'X',1462-1530,'X', !11532-1600,'X',1602-1670,'X',1672-1702,'DE',1705-1740,'X', !11742-1810,'X',1812-1935 ##label BOW !'##cross-references EMBL:X51591 REFERENCE S02229 !$#authors Jandreski, M.A.; Liew, C.C. !$#journal Hum. Genet. (1987) 76:47-53 !$#title Construction of a human ventricular cDNA library and !1characterization of a beta myosin heavy chain cDNA clone. !$#cross-references MUID:87192738; PMID:3032769 !$#accession S02229 !'##molecule_type mRNA !'##residues 1393-1702,'DR',1705-1935 ##label JAN !'##cross-references EMBL:X06976; NID:g34860; PIDN:CAA30039.1; !1PID:g825694 REFERENCE A93616 !$#authors Saez, L.; Leinwand, L.A. !$#journal Nucleic Acids Res. (1986) 14:2951-2969 !$#title Characterization of diverse forms of myosin heavy chain !1expressed in adult human skeletal muscle. !$#cross-references MUID:86176778; PMID:2421254 !$#accession B23767 !'##molecule_type mRNA !'##residues 'LLGVGELASG',1311-1312,'G',1314-1355,'R',1357-1358,'GD', !11361-1438,'LQ',1441-1563,'V',1565-1575,'RQ',1578-1593,'E', !11595-1606,'N',1608-1641,'NLRAS',1647,'E',1649-1738,'G', !11740-1935 ##label SA2 !'##note the first ten codons of the sequence figure show the reverse !1complementary strand, probably in error, and the !1corresponding incorrect amino acid translation GENETICS !$#gene GDB:MYH7 !'##cross-references GDB:120215; OMIM:160760 !$#map_position 14q12-14q12 !$#introns 67/3; 115/3; 168/1; 177/2; 213/3; 244/3; 266/1; 299/1; 333/ !13; 380/1; 419/3; 469/3; 526/3; 630/1; 652/3; 682/1; 721/2; !1762/3; 808/2; 893/3; 974/3; 1033/3; 1082/2; 1112/3; 1242/3; !11285/1; 1324/3; 1390/2; 1451/3; 1507/1; 1548/3; 1651/3; !11719/3; 1761/3; 1853/3; 1885/3; 1930/3 CLASSIFICATION #superfamily myosin heavy chain; myosin motor domain !1homology KEYWORDS actin binding; ATP; cardiac muscle; coiled coil; heart; !1hydrolase; methylated amino acid; muscle contraction; !1nucleotide binding; P-loop; skeletal muscle; tandem repeat; !1thick filament FEATURE !$88-766 #domain myosin motor domain homology #label MMOT\ !$178-185 #region nucleotide-binding motif A (P-loop)\ !$548-585 #region actin binding #status predicted\ !$655-677 #region actin binding #status predicted\ !$839-1935 #domain coiled coil #status predicted #label COI\ !$839-1279 #region S2\ !$1280-1935 #region light meromyosin\ !$129 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8predicted\ !$184 #binding_site ATP (Lys) #status predicted\ !$695,705 #active_site Cys #status predicted SUMMARY #length 1935 #molecular-weight 223112 #checksum 666 SEQUENCE /// ENTRY S06006 #type complete TITLE myosin beta heavy chain, cardiac muscle [similarity] - rat CONTAINS myosin ATPase (EC 3.6.4.1) ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 19-Apr-2002 ACCESSIONS S06006; S07536; I67441; A02989 REFERENCE S06006 !$#authors Kraft, R.; Bravo-Zehnder, M.; Taylor, D.A.; Leinwand, L.A. !$#journal Nucleic Acids Res. (1989) 17:7529-7530 !$#title Complete nucleotide sequence of full length cDNA for rat !1beta cardiac myosin heavy chain. !$#cross-references MUID:90016823; PMID:2798112 !$#accession S06006 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-1935 ##label KRA !'##cross-references EMBL:X15939; NID:g56656; PIDN:CAA34065.1; !1PID:g56657 REFERENCE S07535 !$#authors McNally, E.M.; Kraft, R.; Bravo-Zehnder, M.; Taylor, D.A.; !1Leinwand, L.A. !$#journal J. Mol. Biol. (1989) 210:665-671 !$#title Full-length rat alpha and beta cardiac myosin heavy chain !1sequences. Comparisons suggest a molecular basis for !1functional differences. !$#cross-references MUID:90133919; PMID:2614840 !$#accession S07536 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-950,'RK',953-1935 ##label MCN REFERENCE I53305 !$#authors Mahdavi, V.; Lompre, A.M.; Chambers, A.P.; Nadal-Ginard, B. !$#journal Eur. Heart J. (1984) 5:181-191 !$#title Cardiac myosin heavy chain isozymic transitions during !1development and under pathological conditions are regulated !1at the level of mRNA availability. !$#cross-references MUID:85179510; PMID:6241892 !$#accession I67441 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1871-1935 ##label RES !'##cross-references GB:M32698; NID:g205598; PIDN:AAA41659.1; !1PID:g205599 REFERENCE A02988 !$#authors Mahdavi, V.; Periasamy, M.; Nadal-Ginard, B. !$#journal Nature (1982) 297:659-664 !$#title Molecular characterization of two myosin heavy chain genes !1expressed in the adult heart. !$#cross-references MUID:82220036; PMID:7045682 !$#accession A02989 !'##molecule_type mRNA !'##residues 1524-1528,'V',1530,'R',1532-1730,'H',1732-1783,'K', !11785-1850,'N',1852-1857,'K',1859-1935 ##label MAH !'##cross-references GB:J00752; NID:g205577; PIDN:AAA41654.1; !1PID:g205578 CLASSIFICATION #superfamily myosin heavy chain; myosin motor domain !1homology KEYWORDS actin binding; ATP; cardiac muscle; coiled coil; heart; !1hydrolase; methylated amino acid; muscle contraction; !1nucleotide binding; P-loop; tandem repeat; thick filament FEATURE !$88-766 #domain myosin motor domain homology #label MMOT\ !$178-185 #region nucleotide-binding motif A (P-loop)\ !$548-585 #region actin binding #status predicted\ !$655-677 #region actin binding #status predicted\ !$839-1935 #domain coiled coil #status predicted #label COI\ !$839-1279 #region S2\ !$1280-1935 #region light meromyosin\ !$129 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8predicted\ !$184 #binding_site ATP (Lys) #status predicted\ !$695,705 #active_site Cys #status predicted SUMMARY #length 1935 #molecular-weight 223081 #checksum 574 SEQUENCE /// ENTRY MWRBCB #type fragment TITLE myosin beta heavy chain, cardiac muscle [similarity] - rabbit (fragment) ALTERNATE_NAMES beta isomyosin CONTAINS myosin ATPase (EC 3.6.4.1) ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 17-Mar-1987 #sequence_revision 06-Sep-1996 #text_change 19-Apr-2002 ACCESSIONS S49153; A02987; I46867; I46870 REFERENCE S49119 !$#authors Jaenicke, T.; Goldspink, G. !$#submission submitted to the EMBL Data Library, June 1994 !$#description unpublished. !$#accession S49153 !'##molecule_type mRNA !'##residues 1-1038 ##label JAE !'##cross-references EMBL:Z34886; NID:g510177; PIDN:CAA84369.1; !1PID:g510178 REFERENCE A02986 !$#authors Kavinsky, C.J.; Umeda, P.K.; Levin, J.E.; Sinha, A.M.; !1Nigro, J.M.; Jakovcic, S.; Rabinowitz, M. !$#journal J. Biol. Chem. (1984) 259:2775-2781 !$#title Analysis of cloned mRNA sequences encoding subfragment 2 and !1part of subfragment 1 of alpha- and beta-myosin heavy chains !1of rabbit heart. !$#cross-references MUID:84135762; PMID:6321481 !$#accession A02987 !'##molecule_type mRNA !'##residues 74-125,'L',127-149,'L',151-513,'T',515-628,'L',630-631,'K', !1633-809 ##label KAV !'##cross-references GB:K02444; NID:g165536; PIDN:AAA31414.1; !1PID:g165537 !'##experimental_source normal adult ventricular muscle REFERENCE I46865 !$#authors Sinha, A.M.; Umeda, P.K.; Kavinsky, C.J.; Rajamanickam, C.; !1Hsu, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:5847-5851 !$#title Molecular cloning of mRNA sequences for cardiac alpha- and !1beta-form myosin heavy chains: expression in ventricles of !1normal, hypothyroid, and thyrotoxic rabbits. !$#cross-references MUID:83299886; PMID:6193509 !$#accession I46867 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 673-793 ##label SIN !'##cross-references GB:J00672; NID:g165534; PIDN:AAA31413.1; !1PID:g165535 REFERENCE I46868 !$#authors Friedman, D.J.; Umeda, P.K.; Sinha, A.M.; Hsu, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:3044-3048 !$#title Characterization of genomic clones specifying rabbit alpha- !1and beta-ventricular myosin heavy chains. !$#cross-references MUID:84221901; PMID:6328491 !$#accession I46870 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 531-617 ##label FRI !'##cross-references GB:K01696; NID:g165542; PIDN:AAA31417.1; !1PID:g165543 COMMENT Protease-sensitive junctional regions located at the !1head-rod (S1-S2 subfragments) and S2-light meromyosin !1interfaces may act as hinges that facilitate interaction !1between the globular myosin head and actin filament during !1contraction. COMMENT Experimental alkylation of 332-Cys and 342-Cys modifies !1myosin ATPase activity. CLASSIFICATION #superfamily myosin heavy chain; myosin motor domain !1homology KEYWORDS actin binding; ATP; cardiac muscle; coiled coil; heart; !1hydrolase; muscle contraction; tandem repeat; thick filament FEATURE !$1-403 #domain myosin motor domain homology (fragment) !8#label MMOT\ !$185-222 #region actin binding #status predicted\ !$292-314 #region actin binding #status predicted\ !$476-1038 #domain S2 (fragment) #status predicted #label DS2\ !$476-916 #domain coiled coil #status predicted #label COI\ !$332,342 #active_site Cys #status predicted SUMMARY #length 1038 #checksum 2343 SEQUENCE /// ENTRY JX0178 #type complete TITLE myosin heavy chain, fast skeletal muscle, adult [validated] - chicken CONTAINS myosin ATPase (EC 3.6.4.1) ORGANISM #formal_name Gallus gallus #common_name chicken DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 19-Apr-2002 ACCESSIONS PX0050; PX0051; PX0052; JX0178; A26365; S02082; PW0009; !1S39081; S24351; S05515; S04501; A60877; A24124; C25217 REFERENCE PX0050 !$#authors Hayashida, M.; Maita, T.; Matsuda, G. !$#journal J. Biochem. (1991) 110:54-59 !$#title The primary structure of skeletal muscle myosin heavy chain: !1I. Sequence of the amino-terminal 23 kDa fragment. !$#cross-references MUID:92041767; PMID:1939027 !$#accession PX0050 !'##molecule_type protein !'##residues 1-205 ##label HAY REFERENCE PX0051 !$#authors Komine, Y.; Maita, T.; Matsuda, G. !$#journal J. Biochem. (1991) 110:60-67 !$#title The primary structure of skeletal muscle myosin heavy chain: !1II. Sequence of the 50kDa fragment of subfragment-1. !$#cross-references MUID:92041768; PMID:1939028 !$#accession PX0051 !'##molecule_type protein !'##residues 206-636 ##label KOM REFERENCE PX0052 !$#authors Maita, T.; Miyanishi, T.; Matsuzono, K.; Tanioka, Y.; !1Matsuda, G. !$#journal J. Biochem. (1991) 110:68-74 !$#title The primary structure of skeletal muscle myosin heavy chain: !1III. Sequence of the 22kDa fragment and the alignment of the !123kDa, 50kDa, and 22kDa fragments. !$#cross-references MUID:92041769; PMID:1939029 !$#accession PX0052 !'##molecule_type protein !'##residues 201-213;632-837 ##label MAI REFERENCE JX0178 !$#authors Maita, T.; Yajima, E.; Nagata, S.; Miyanishi, T.; Nakayama, !1S.; Matsuda, G. !$#journal J. Biochem. (1991) 110:75-87 !$#title The primary structure of skeletal muscle myosin heavy chain: !1IV. Sequence of the rod, and the complete 1,938-residue !1sequence of the heavy chain. !$#cross-references MUID:92041770; PMID:1939030 !$#accession JX0178 !'##molecule_type protein !'##residues 833-1938 ##label MA2 REFERENCE A26365 !$#authors Maita, T.; Hayashida, M.; Tanioka, Y.; Komine, Y.; Matsuda, !1G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:416-420 !$#title The primary structure of the myosin head. !$#cross-references MUID:87092420; PMID:3467365 !$#accession A26365 !'##molecule_type protein !'##residues 1-129,'X',131-139,141-550,'X',552-754,'X',756-784,'QL', !1787-804,806-810 ##label MA3 REFERENCE S02082 !$#authors Watanabe, B. !$#journal Biol. Chem. Hoppe-Seyler (1989) 370:55-61 !$#title Amino-acid sequence of the hinge region in chicken myosin !1subfragment-2. !$#cross-references MUID:89228549; PMID:2713098 !$#accession S02082 !'##molecule_type protein !'##residues 1144-1270 ##label WAT REFERENCE PW0009 !$#authors Yajima, E. !$#journal Nagasaki Igakkai Zasshi (1990) 65:409-430 !$#title Study on tail region of skeletal muscle myosin; primary !1structure and protease cleavage sites. !$#accession PW0009 !'##molecule_type protein !'##residues 1304-1938 ##label YAJ REFERENCE S39081 !$#authors Moore, L.A.; Arrizubieta, M.J.; Tidyman, W.E.; Herman, L.A.; !1Bandman, E. !$#submission submitted to the EMBL Data Library, August 1991 !$#description Analysis of the chicken fast myosin heavy chain family: !1Localization of isoform-specific antibody epitopes and !1regions of divergence. !$#accession S39081 !'##molecule_type mRNA !'##residues 1081-1203,'DV',1206-1342,'E',1344-1544,'S',1546-1795,'HV', !11798-1829,'S',1831-1938 ##label MOO1 !'##cross-references EMBL:M74084 REFERENCE S24348 !$#authors Moore, L.A.; Arrizubieta, M.J.; Tidyman, W.E.; Herman, L.A.; !1Bandman, E. !$#journal J. Mol. Biol. (1992) 225:1143-1151 !$#title Analysis of the chicken fast myosin heavy chain family. !1Localization of isoform-specific antibody epitopes and !1regions of divergence. !$#cross-references MUID:92309413; PMID:1377278 !$#accession S24351 !'##molecule_type mRNA !'##residues 1082-1182,'T',1184-1203,'DV',1206-1342,'E',1344-1544,'S', !11546-1780,'M',1782-1787,'LHV',1791-1796,'H',1798-1829,'S', !11831-1938 ##label MOO2 !'##cross-references EMBL:M74084 REFERENCE S05515 !$#authors Watanabe, B. !$#journal Biol. Chem. Hoppe-Seyler (1989) 370:1027-1034 !$#title Complete amino-acid sequence of subfragment-2 in adult !1chicken skeletal muscle myosin. !$#cross-references MUID:90121764; PMID:2610940 !$#accession S05515 !'##molecule_type protein !'##residues 842-906,'Q',908-1270 ##label WA3 REFERENCE S04501 !$#authors Watanabe, B. !$#journal Biol. Chem. Hoppe-Seyler (1989) 370:549-558 !$#title Amino-acid sequence of the short subfragment-2 in adult !1chicken skeletal muscle myosin. !$#cross-references MUID:89374803; PMID:2775482 !$#accession S04501 !'##molecule_type protein !'##residues 852-906,'Q',908-1108 ##label WA2 REFERENCE A60877 !$#authors Matsuda, G.; Maita, T.; Miyanishi, T.; Hayashida, M. !$#journal J. Protein Chem. (1987) 6:33-46 !$#title Structure and function of muscle myosin. !$#accession A60877 !'##molecule_type protein !'##residues 1-139,141-205 ##label MA1 REFERENCE A92507 !$#authors Gulick, J.; Kropp, K.; Robbins, J. !$#journal J. Biol. Chem. (1985) 260:14513-14520 !$#title The structure of two fast-white myosin heavy chain !1promoters. A comparative study. !$#cross-references MUID:86033956; PMID:2997212 !$#accession A24124 !'##molecule_type DNA !'##residues 'M',1-168 ##label GUL !'##cross-references GB:M13512; GB:M12083; GB:M13510; NID:g212363; !1PIDN:AAA48966.1; PID:g555467 REFERENCE A92587 !$#authors Kropp, K.; Gulick, J.; Robbins, J. !$#journal J. Biol. Chem. (1986) 261:6613-6618 !$#title A canonical sequence organization at the 5'-end of the !1myosin heavy chain genes. !$#cross-references MUID:86196091; PMID:3009465 !$#accession C25217 !'##molecule_type DNA !'##residues 'M',1-56,'T',58-76,'I',78-168 ##label KRO !'##cross-references GB:M13515; GB:M13511; NID:g212373; PIDN:AAA48971.1; !1PID:g555468 COMMENT This is a fragment of the globular head. CLASSIFICATION #superfamily myosin heavy chain; myosin motor domain !1homology KEYWORDS acetylated amino end; actin binding; ATP; coiled coil; !1hydrolase; methylated amino acid; muscle contraction; !1nucleotide binding; P-loop; skeletal muscle; tandem repeat; !1thick filament FEATURE !$1-1938 #product myosin heavy chain #status experimental !8#label MAT\ !$89-768 #domain myosin motor domain homology #label MMOT\ !$179-186 #region nucleotide-binding motif A (P-loop)\ !$550-587 #region actin binding #status predicted\ !$657-679 #region actin binding #status predicted\ !$841-1938 #domain coiled coil #label COI\ !$841-1289 #region S2\ !$852-1108 #domain short subfragment 2 #label SUB2\ !$1290-1938 #region light meromyosin\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$35 #modified_site N6-methyllysine (Lys) #status !8experimental\ !$130,551 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental\ !$185 #binding_site ATP (Lys) #status predicted\ !$697,707 #active_site Cys #status predicted\ !$755 #modified_site 3'-methylhistidine (His) #status !8experimental SUMMARY #length 1938 #molecular-weight 222971 #checksum 215 SEQUENCE /// ENTRY S04090 #type complete TITLE myosin heavy chain 3, skeletal muscle, embryonic - human CONTAINS myosin ATPase (EC 3.6.4.1) ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 19-Apr-2002 ACCESSIONS S04090; S06146; S05442; S12460; S09333; A35082 REFERENCE S04090 !$#authors Eller, M.; Stedman, H.H.; Sylvester, J.E.; Fertels, S.H.; !1Rubinstein, N.A.; Kelly, A.M.; Sarkar, S. !$#journal Nucleic Acids Res. (1989) 17:3591-3592 !$#title Nucleotide sequence of full length human embryonic myosin !1heavy chain cDNA. !$#cross-references MUID:89263803; PMID:2726495 !$#accession S04090 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-1940 ##label ELL !'##cross-references EMBL:X13988; NID:g34843; PIDN:CAA32167.1; !1PID:g34844 REFERENCE S06146 !$#authors Eller, M.; Stedman, H.H.; Sylvester, J.E.; Fertels, S.H.; !1Wu, Q.L.; Raychowdhury, M.K.; Rubinstein, N.A.; Kelly, A.M.; !1Sarkar, S. !$#journal FEBS Lett. (1989) 256:21-28 !$#title Human embryonic myosin heavy chain cDNA. Interspecies !1sequence conservation of the myosin rod, chromosomal locus !1and isoform specific transcription of the gene. !$#cross-references MUID:90033298; PMID:2806546 !$#accession S06146 !'##molecule_type mRNA !'##residues 774-1662,'QT',1665-1940 ##label EL2 !'##cross-references EMBL:X13100; NID:g31143; PIDN:CAA31492.1; !1PID:g31144 REFERENCE S05442 !$#authors Karsch-Mizrachi, I.; Travis, M.; Blau, H.; Leinwand, L.A. !$#journal Nucleic Acids Res. (1989) 17:6167-6179 !$#title Expression and DNA sequence analysis of a human embryonic !1skeletal muscle myosin heavy chain gene. !$#cross-references MUID:89366648; PMID:2771643 !$#accession S05442 !'##molecule_type DNA !'##residues 856-1390,'KK',1393-1940 ##label KAR !'##cross-references EMBL:X15696; NID:g36504; PIDN:CAA33731.1; !1PID:g1335313 REFERENCE A35082 !$#authors Stedman, H.H.; Eller, M.; Jullian, E.H.; Fertels, S.H.; !1Sarkar, S.; Sylvester, J.E.; Kelly, A.M.; Rubinstein, N.A. !$#journal J. Biol. Chem. (1990) 265:3568-3576 !$#title The human embryonic myosin heavy chain. Complete primary !1structure reveals evolutionary relationships with other !1developmental isoforms. !$#cross-references MUID:90154023; PMID:2303463 !$#contents annotation; chromosomal assignment REFERENCE S12458 !$#authors Bober, E. !$#submission submitted to the EMBL Data Library, January 1989 !$#accession S12460 !'##molecule_type mRNA !'##residues 856-1330,'G',1332-1390,'KK',1393-1607,'RA',1610-1940 !1##label BOB !'##cross-references EMBL:X51593; NID:g29463; PIDN:CAA35942.1; !1PID:g29464 !'##experimental_source clone gtMHC-E REFERENCE S09331 !$#authors Bober, E.; Buchberger-Seidl, A.; Braun, T.; Singh, S.; !1Goedde, H.W.; Arnold, H.H. !$#journal Eur. J. Biochem. (1990) 189:55-65 !$#title Identification of three developmentally controlled isoforms !1of human myosin heavy chains. !$#cross-references MUID:90235862; PMID:1691980 !$#accession S09333 !'##molecule_type mRNA !'##residues 856-901,'X',903-971,'X',973-1041,'X',1043-1111,'X', !11113-1181,'X',1183-1251,'X',1253-1321,'X',1323-1330,'G', !11332-1390,'KX',1393-1461,'X',1463-1531,'X',1533-1601,'X', !11603-1607,'RA',1610-1671,'X',1673-1741,'X',1743-1811,'X', !11813-1881,'X',1883-1940 ##label BOW !'##cross-references EMBL:X51593 GENETICS !$#gene GDB:MYH3 !'##cross-references GDB:119443; OMIM:160720 !$#map_position 17p13.1-17p13.1 CLASSIFICATION #superfamily myosin heavy chain; myosin motor domain !1homology KEYWORDS actin binding; ATP; coiled coil; hydrolase; methylated amino !1acid; muscle contraction; nucleotide binding; P-loop; !1skeletal muscle; tandem repeat; thick filament FEATURE !$89-767 #domain myosin motor domain homology #label MMOT\ !$179-186 #region nucleotide-binding motif A (P-loop)\ !$549-586 #region actin binding #status predicted\ !$656-678 #region actin binding #status predicted\ !$840-1940 #domain coiled coil #status predicted #label COI\ !$840-1280 #region S2\ !$1281-1940 #region light meromyosin\ !$130 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8predicted\ !$185 #binding_site ATP (Lys) #status predicted\ !$696,706 #active_site Cys #status predicted SUMMARY #length 1940 #molecular-weight 224035 #checksum 6726 SEQUENCE /// ENTRY A24922 #type complete TITLE myosin heavy chain, skeletal muscle, embryonic - rat CONTAINS myosin ATPase (EC 3.6.4.1) ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 19-Apr-2002 ACCESSIONS A24922; A22538; B24263 REFERENCE A24922 !$#authors Strehler, E.E.; Strehler-Page, M.A.; Perriard, J.C.; !1Periasamy, M.; Nadal-Ginard, B. !$#journal J. Mol. Biol. (1986) 190:291-317 !$#title Complete nucleotide and encoded amino acid sequence of a !1mammalian myosin heavy chain gene. Evidence against !1intron-dependent evolution of the rod. !$#cross-references MUID:87060988; PMID:3783701 !$#accession A24922 !'##molecule_type DNA !'##residues 1-1940 ##label STR !'##cross-references GB:X04267; GB:X05004; NID:g56658; PIDN:CAA27817.1; !1PID:g1619328 REFERENCE A22538 !$#authors Strehler, E.E.; Mahdavi, V.; Periasamy, M.; Nadal-Ginard, B. !$#journal J. Biol. Chem. (1985) 260:468-471 !$#title Intron positions are conserved in the 5' end region of !1myosin heavy-chain genes. !$#cross-references MUID:85080119; PMID:2981212 !$#accession A22538 !'##molecule_type DNA !'##residues 1-168 ##label ST2 !'##cross-references GB:L00370; GB:M10135; NID:g205580; PIDN:AAA41655.1; !1PID:g554476 REFERENCE A24263 !$#authors Periasamy, M.; Wydro, R.M.; Strehler-Page, M.A.; Strehler, !1E.E.; Nadal-Ginard, B. !$#journal J. Biol. Chem. (1985) 260:15856-15862 !$#title Characterization of cDNA and genomic sequences corresponding !1to an embryonic myosin heavy chain. !$#cross-references MUID:86059474; PMID:2999140 !$#accession B24263 !'##status preliminary !'##molecule_type mRNA !'##residues 1358-1490,'G' ##label PER !'##cross-references GB:K03468; NID:g205573; PIDN:AAA41652.1; !1PID:g205574 !'##experimental_source clone pMHC-72 GENETICS !$#introns 68/3; 116/3; 169/1 !$#note the list of intron positions may be incomplete CLASSIFICATION #superfamily myosin heavy chain; myosin motor domain !1homology KEYWORDS actin binding; ATP; coiled coil; hydrolase; methylated amino !1acid; muscle contraction; nucleotide binding; P-loop; !1skeletal muscle; tandem repeat; thick filament FEATURE !$89-767 #domain myosin motor domain homology #label MMOT\ !$179-186 #region nucleotide-binding motif A (P-loop)\ !$549-586 #region actin binding #status predicted\ !$656-678 #region actin binding #status predicted\ !$840-1940 #domain coiled coil #status predicted #label COI\ !$840-1280 #region S2\ !$1281-1940 #region light meromyosin\ !$130 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8predicted\ !$185 #binding_site ATP (Lys) #status predicted\ !$696,706 #active_site Cys #status predicted SUMMARY #length 1940 #molecular-weight 223856 #checksum 7355 SEQUENCE /// ENTRY A40997 #type complete TITLE myosin heavy chain, striated adductor muscle - scallop (Aequipecten irradians) CONTAINS myosin ATPase (EC 3.6.4.1) ORGANISM #formal_name Aequipecten irradians DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 19-Apr-2002 ACCESSIONS A40997; S13557 REFERENCE A40997 !$#authors Nyitray, L.; Goodwin, E.B.; Szent-Gyoergyi, A.G. !$#journal J. Biol. Chem. (1991) 266:18469-18476 !$#title Complete primary structure of a scallop striated muscle !1myosin heavy chain. Sequence comparison with other heavy !1chains reveals regions that might be critical for !1regulation. !$#cross-references MUID:92011595; PMID:1917970 !$#accession A40997 !'##molecule_type mRNA !'##residues 1-1938 ##label NYI !'##cross-references GB:X55714; NID:g5611; PIDN:CAA39247.1; PID:g5612 CLASSIFICATION #superfamily myosin heavy chain; myosin motor domain !1homology KEYWORDS actin binding; ATP; coiled coil; hydrolase; muscle !1contraction; nucleotide binding; P-loop; tandem repeat; !1thick filament FEATURE !$86-763 #domain myosin motor domain homology #label MMOT\ !$176-183 #region nucleotide-binding motif A (P-loop)\ !$547-586 #region actin binding #status predicted\ !$653-675 #region actin binding #status predicted\ !$836-1938 #domain coiled coil #status predicted #label COI\ !$836-1276 #region S2\ !$1277-1938 #region light meromyosin\ !$182 #binding_site ATP (Lys) #status predicted\ !$693,703 #active_site Cys #status predicted SUMMARY #length 1938 #molecular-weight 222820 #checksum 5215 SEQUENCE /// ENTRY S02771 #type complete TITLE myosin heavy chain A [similarity] - Caenorhabditis elegans CONTAINS myosin ATPase (EC 3.6.4.1) ORGANISM #formal_name Caenorhabditis elegans DATE 31-Dec-1993 #sequence_revision 19-May-2000 #text_change 19-Apr-2002 ACCESSIONS T23622; S02771 REFERENCE Z19773 !$#authors Harris, B. !$#submission submitted to the EMBL Data Library, August 1996 !$#accession T23622 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-1992 ##label WIL !'##cross-references EMBL:Z78199; PIDN:CAB01576.1; GSPDB:GN00023; !1CESP:K12F2.1 !'##experimental_source clone K12F2 REFERENCE S02771 !$#authors Dibb, N.J.; Maruyama, I.N.; Krause, M.; Karn, J. !$#journal J. Mol. Biol. (1989) 205:603-613 !$#title Sequence analysis of the complete Caenorhabditis elegans !1myosin heavy chain gene family. !$#cross-references MUID:89178677; PMID:2926820 !$#accession S02771 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-116,140-1992 ##label DIB !'##cross-references EMBL:X08067; NID:g6798; PIDN:CAA30856.1; PID:g6799 GENETICS !$#gene myo-3; CESP:K12F2.1 !$#map_position 5 !$#introns 46/1; 192/1; 292/1; 468/2; 1921/3 CLASSIFICATION #superfamily myosin heavy chain; myosin motor domain !1homology KEYWORDS actin binding; ATP; coiled coil; hydrolase; methylated amino !1acid; muscle contraction; nucleotide binding; P-loop; tandem !1repeat FEATURE !$89-802 #domain myosin motor domain homology #label MMOT\ !$202-209 #region nucleotide-binding motif A (P-loop)\ !$690-712 #region actin binding #status predicted\ !$793-807 #region actin binding #status predicted\ !$875-1992 #domain coiled coil #status predicted #label COI\ !$875-1189 #region S2\ !$1190-1992 #region light meromyosin\ !$153 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8predicted\ !$208 #binding_site ATP (Lys) #status predicted\ !$730,740 #active_site Cys #status predicted SUMMARY #length 1992 #molecular-weight 228361 #checksum 1310 SEQUENCE /// ENTRY MWKW #type complete TITLE myosin heavy chain B [similarity] - Caenorhabditis elegans CONTAINS myosin ATPase (EC 3.6.4.1) ORGANISM #formal_name Caenorhabditis elegans DATE 13-Jun-1983 #sequence_revision 19-May-2000 #text_change 19-Apr-2002 ACCESSIONS T20770; T21629; A93958; A93287; A21074; A02992 REFERENCE Z19322 !$#authors Kershaw, J. !$#submission submitted to the EMBL Data Library, November 1996 !$#accession T20770 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-1963 ##label WIL !'##cross-references EMBL:Z81499; PIDN:CAB04089.1; GSPDB:GN00019; !1CESP:F11C3.3 !'##experimental_source clone F11C3 !$#accession T21629 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-1963 ##label WI2 !'##cross-references EMBL:Z83107; PIDN:CAB05505.1; GSPDB:GN00019; !1CESP:F11C3.3 !'##experimental_source clone F32A7 REFERENCE A93958 !$#authors Karn, J.; Brenner, S.; Barnett, L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:4253-4257 !$#title Protein structural domains in the Caenorhabditis elegans !1unc-54 myosin heavy chain gene are not separated by introns. !$#cross-references MUID:83273600; PMID:6576334 !$#accession A93958 !'##molecule_type DNA !'##residues 1-61,'EMSVIQ',65-376,'V',378-1963 ##label KAR !'##cross-references GB:J01050; NID:g156399; PIDN:AAA28124.1; !1PID:g156400 REFERENCE A93287 !$#authors McLachlan, A.D.; Karn, J. !$#journal Nature (1982) 299:226-231 !$#title Periodic charge distributions in the myosin rod amino acid !1sequence match cross-bridge spacings in muscle. !$#cross-references MUID:82272395; PMID:7202124 !$#accession A93287 !'##molecule_type DNA !'##residues 847-1333,'R',1335-1876,'L',1878-1963 ##label MCL REFERENCE A21074 !$#authors Wills, N.; Gesteland, R.F.; Karn, J.; Barnett, L.; Bolten, !1S.; Waterston, R.H. !$#journal Cell (1983) 33:575-583 !$#title The genes sup-7 X and sup-5 III of Caenorhabditis elegans !1suppress amber nonsense mutations via altered transfer RNA. !$#cross-references MUID:83232892; PMID:6571695 !$#accession A21074 !'##molecule_type DNA !'##residues 1873-1963 ##label WI3 !'##cross-references GB:V01494; GB:J01049; NID:g6783; PIDN:CAA24738.1; !1PID:g6784 GENETICS !$#gene unc-54; CESP:F11C3.3 !$#map_position 1 !$#introns 21/3; 64/3; 111/3; 264/1; 525/3; 951/2; 1747/3; 1819/3; !11894/3 CLASSIFICATION #superfamily myosin heavy chain; myosin motor domain !1homology KEYWORDS actin binding; ATP; coiled coil; hydrolase; methylated amino !1acid; muscle contraction; nucleotide binding; P-loop; tandem !1repeat FEATURE !$84-775 #domain myosin motor domain homology #label MMOT\ !$174-181 #region nucleotide-binding motif A (P-loop)\ !$662-684 #region actin binding #status predicted\ !$766-780 #region actin binding #status predicted\ !$848-1963 #domain coiled coil #status predicted #label COI\ !$848-1162 #region S2\ !$1163-1963 #region light meromyosin\ !$125 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8predicted\ !$180 #binding_site ATP (Lys) #status predicted\ !$702,712 #active_site Cys #status predicted SUMMARY #length 1963 #molecular-weight 224753 #checksum 4811 SEQUENCE /// ENTRY S05697 #type complete TITLE myosin heavy chain C [similarity] - Caenorhabditis elegans CONTAINS myosin ATPase (EC 3.6.4.1) ORGANISM #formal_name Caenorhabditis elegans DATE 31-Dec-1993 #sequence_revision 19-May-2000 #text_change 19-Apr-2002 ACCESSIONS T22232; T24967; S05697; S02773 REFERENCE Z19534 !$#authors McMurray, A. !$#submission submitted to the EMBL Data Library, November 1995 !$#accession T22232 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-1968 ##label WIL1 !'##cross-references EMBL:Z68117; PIDN:CAA92183.1; GSPDB:GN00028; !1CESP:T18D3.4 !'##experimental_source clone F45E6 !$#accession T24967 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-1968 ##label WIL2 !'##cross-references EMBL:Z68119; PIDN:CAA92197.1; GSPDB:GN00028; !1CESP:T18D3.4 !'##experimental_source clone T18D3 REFERENCE S05282 !$#authors Karn, J. !$#submission submitted to the EMBL Data Library, June 1988 !$#accession S05697 !'##molecule_type DNA !'##residues 1-131,'E',133-285,'S',287-419,'K',421-1247,'C',1249-1270, !1'QTS',1274-1807,1829-1968 ##label KAR !'##cross-references EMBL:X08066; NID:g6787; PIDN:CAA30855.1; !1PID:g295767 REFERENCE S02771 !$#authors Dibb, N.J.; Maruyama, I.N.; Krause, M.; Karn, J. !$#journal J. Mol. Biol. (1989) 205:603-613 !$#title Sequence analysis of the complete Caenorhabditis elegans !1myosin heavy chain gene family. !$#cross-references MUID:89178677; PMID:2926820 !$#accession S02773 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-64,'V',65-131,'E',133-285,'S',287-419,'K',421-1247,'C', !11249-1270,'QTS',1274-1807,1829-1968 ##label DIB !'##cross-references EMBL:X08066 GENETICS !$#gene myo-2; CESP:T18D3.4 !$#map_position X !$#introns 21/3; 64/3; 111/3; 270/1; 330/3; 384/1; 592/1; 814/3; 1660/ !12; 1710/3; 1807/3; 1828/3; 1922/3 CLASSIFICATION #superfamily myosin heavy chain; myosin motor domain !1homology KEYWORDS actin binding; ATP; coiled coil; hydrolase; methylated amino !1acid; muscle contraction; nucleotide binding; P-loop; tandem !1repeat FEATURE !$84-782 #domain myosin motor domain homology #label MMOT\ !$174-181 #region nucleotide-binding motif A (P-loop)\ !$668-690 #region actin binding #status predicted\ !$773-787 #region actin binding #status predicted\ !$855-1968 #domain coiled coil #status predicted #label COI\ !$855-1169 #region S2\ !$1170-1968 #region light meromyosin\ !$125 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8predicted\ !$180 #binding_site ATP (Lys) #status predicted\ !$708,718 #active_site Cys #status predicted SUMMARY #length 1968 #molecular-weight 225431 #checksum 8190 SEQUENCE /// ENTRY MWKW1 #type complete TITLE myosin heavy chain D [similarity] - Caenorhabditis elegans ALTERNATE_NAMES myosin heavy chain I CONTAINS myosin ATPase (EC 3.6.4.1) ORGANISM #formal_name Caenorhabditis elegans DATE 28-Feb-1986 #sequence_revision 19-May-2000 #text_change 19-Apr-2002 ACCESSIONS T21193; T23973; S02772; A02993 REFERENCE Z19388 !$#authors McMurray, A. !$#submission submitted to the EMBL Data Library, April 1996 !$#accession T21193 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-1938 ##label WIL !'##cross-references EMBL:Z71261; PIDN:CAA95806.1; GSPDB:GN00019; !1CESP:R06C7.10 !'##experimental_source clone F21C3 REFERENCE Z19825 !$#authors Gardner, A. !$#submission submitted to the EMBL Data Library, April 1996 !$#accession T23973 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-1938 ##label WI2 !'##cross-references EMBL:Z71266; PIDN:CAA95848.1; GSPDB:GN00019; !1CESP:R06C7.10 !'##experimental_source clone R06C7 REFERENCE S02771 !$#authors Dibb, N.J.; Maruyama, I.N.; Krause, M.; Karn, J. !$#journal J. Mol. Biol. (1989) 205:603-613 !$#title Sequence analysis of the complete Caenorhabditis elegans !1myosin heavy chain gene family. !$#cross-references MUID:89178677; PMID:2926820 !$#accession S02772 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-376,'V',378-390,'V',392-576,'L',578-680,'I',682-1938 !1##label DIB !'##cross-references EMBL:X08065; NID:g6785; PIDN:CAA30854.1; PID:g6786 REFERENCE A93958 !$#authors Karn, J.; Brenner, S.; Barnett, L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:4253-4257 !$#title Protein structural domains in the Caenorhabditis elegans !1unc-54 myosin heavy chain gene are not separated by introns. !$#cross-references MUID:83273600; PMID:6576334 !$#accession A02993 !'##molecule_type DNA !'##residues 24-93,'E',95-97,'R',99-376,'V',378-388,'GDV',392-407,'N', !1409-473,'G',475-576,'L',578-680,'I',682-1372,'D',1374-1795 !1##label KAR GENETICS !$#gene myo-1; CESP:R06C7.10 !$#map_position 1 !$#introns 23/3; 114/3; 229/1; 264/1; 320/1; 857/3; 1745/3; 1814/1; !11892/3 CLASSIFICATION #superfamily myosin heavy chain; myosin motor domain !1homology KEYWORDS actin binding; ATP; coiled coil; hydrolase; methylated amino !1acid; muscle contraction; nucleotide binding; P-loop; tandem !1repeat FEATURE !$87-773 #domain myosin motor domain homology #label MMOT\ !$177-184 #region nucleotide-binding motif A (P-loop)\ !$660-682 #region actin binding #status predicted\ !$764-778 #region actin binding #status predicted\ !$846-1938 #domain coiled coil #status predicted #label COI\ !$846-1160 #region S2\ !$1161-1938 #region light meromyosin\ !$128 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8predicted\ !$183 #binding_site ATP (Lys) #status predicted\ !$700,710 #active_site Cys #status predicted SUMMARY #length 1938 #molecular-weight 223321 #checksum 7952 SEQUENCE /// ENTRY A41604 #type complete TITLE myosin heavy chain, smooth muscle, long splice form - rabbit CONTAINS myosin ATPase (EC 3.6.4.1) ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 19-Apr-2002 ACCESSIONS A41604; A33501 REFERENCE A41604 !$#authors Babij, P.; Kelly, C.; Periasamy, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:10676-10680 !$#title Characterization of a mammalian smooth muscle myosin !1heavy-chain gene: complete nucleotide and protein coding !1sequence and analysis of the 5' end of the gene. !$#cross-references MUID:92073350; PMID:1961735 !$#accession A41604 !'##molecule_type mRNA !'##residues 1-1972 ##label BAB !'##cross-references GB:M77812 REFERENCE A33501 !$#authors Nagai, R.; Kuro-o, M.; Babij, P.; Periasamy, M. !$#journal J. Biol. Chem. (1989) 264:9734-9737 !$#title Identification of two types of smooth muscle myosin heavy !1chain isoforms by cDNA cloning and immunoblot analysis. !$#cross-references MUID:89255535; PMID:2722872 !$#accession A33501 !'##molecule_type mRNA !'##residues 1455-1972 ##label NAG !'##cross-references GB:J04833; NID:g165519; PIDN:AAA31407.1; !1PID:g165520 !'##experimental_source smooth muscle !'##note examination by Southern blotting for the regions of difference !1between this isoform and a shorter isoform suggests the !1presence of a single gene (data not shown) and therefore !1suggests alternative splicing CLASSIFICATION #superfamily myosin heavy chain; myosin motor domain !1homology KEYWORDS actin binding; alternative splicing; ATP; coiled coil; !1hydrolase; methylated amino acid; muscle contraction; !1nucleotide binding; P-loop; tandem repeat; thick filament FEATURE !$88-771 #domain myosin motor domain homology #label MMOT\ !$178-185 #region nucleotide-binding motif A (P-loop)\ !$559-572 #region actin binding #status predicted\ !$633-647 #region actin binding #status predicted\ !$844-1938 #domain coiled coil #status predicted #label COI\ !$844-1284 #region S2\ !$1285-1972 #region light meromyosin\ !$1939-1972 #domain carboxyl-terminal #label CBT\ !$129 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8predicted\ !$184 #binding_site ATP (Lys) #status predicted\ !$701,711 #active_site Cys #status predicted SUMMARY #length 1972 #molecular-weight 227345 #checksum 7274 SEQUENCE /// ENTRY S03166 #type complete TITLE myosin heavy chain, gizzard smooth muscle [similarity] - chicken CONTAINS myosin ATPase (EC 3.6.4.1) ORGANISM #formal_name Gallus gallus #common_name chicken DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 19-Apr-2002 ACCESSIONS S03166; A27066; A26045; A36604; A43298 REFERENCE S03166 !$#authors Yanagisawa, M.; Hamada, Y.; Katsuragawa, Y.; Imamura, M.; !1Mikawa, T.; Masaki, T. !$#journal J. Mol. Biol. (1987) 198:143-157 !$#title Complete primary structure of vertebrate smooth muscle !1myosin heavy chain deduced from its complementary DNA !1sequence. Implications on topography and function of myosin. !$#cross-references MUID:88118918; PMID:2892941 !$#accession S03166 !'##molecule_type mRNA !'##residues 1-1979 ##label YAN !'##cross-references EMBL:X06546; NID:g63633; PIDN:CAA29793.1; !1PID:g63634 !'##note part of this sequence was confirmed by protein sequencing REFERENCE A27066 !$#authors Maita, T.; Onishi, H.; Yajima, E.; Matsuda, G. !$#journal J. Biochem. (1987) 102:133-145 !$#title Amino acid sequence of the amino-terminal 24 kDa fragment of !1the heavy chain of chicken gizzard myosin. !$#cross-references MUID:88032919; PMID:3312184 !$#accession A27066 !'##molecule_type protein !'##residues 2,'Z',4-204 ##label MAI REFERENCE A26045 !$#authors Onishi, H.; Maita, T.; Miyanishi, T.; Watanabe, S.; Matsuda, !1G. !$#journal J. Biochem. (1986) 100:1433-1447 !$#title Amino acid sequence of the 203-residue fragment of the heavy !1chain of chicken gizzard myosin containing the SH1-type !1cysteine residue. !$#cross-references MUID:87194651; PMID:3571180 !$#accession A26045 !'##molecule_type protein !'##residues 653-855 ##label ONI REFERENCE A36604 !$#authors Onishi, H.; Maita, T.; Matsuda, G.; Fujiwara, K. !$#journal J. Biol. Chem. (1990) 265:19362-19368 !$#title Lys-65 and Glu-168 are the residues for !1carbodiimide-catalyzed cross-linking between the two heads !1of rigor smooth muscle heavy meromyosin. !$#cross-references MUID:91035476; PMID:1977747 !$#accession A36604 !'##status preliminary !'##molecule_type protein !'##residues 54-67;146-183 ##label ON2 REFERENCE A43298 !$#authors Cole, D.G.; Yount, R.G. !$#journal Biochemistry (1992) 31:6186-6192 !$#title Stability and photochemical properties of vanadate-trapped !1nucleotide complexes of gizzard myosin in the 6S and 10S !1conformations: identification of an active-site serine. !$#cross-references MUID:92329440; PMID:1385724 !$#accession A43298 !'##status preliminary !'##molecule_type protein !'##residues 169-183 ##label COL CLASSIFICATION #superfamily myosin heavy chain; myosin motor domain !1homology KEYWORDS actin binding; ATP; blocked amino end; coiled coil; !1hydrolase; methylated amino acid; muscle contraction; !1nucleotide binding; P-loop; tandem repeat; thick filament FEATURE !$87-777 #domain myosin motor domain homology #label MMOT\ !$177-184 #region nucleotide-binding motif A (P-loop)\ !$565-578 #region actin binding #status predicted\ !$639-653 #region actin binding #status predicted\ !$850-1940 #domain coiled coil #label COI\ !$850-1290 #region S2\ !$1291-1979 #region light meromyosin\ !$1941-1979 #domain carboxyl-terminal #label CBT\ !$2 #modified_site blocked amino end (Ser) (in mature !8form) #status experimental\ !$128 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental\ !$183 #binding_site ATP (Lys) #status predicted\ !$707,717 #active_site Cys #status predicted SUMMARY #length 1979 #molecular-weight 228892 #checksum 4458 SEQUENCE /// ENTRY A61231 #type complete TITLE myosin heavy chain nonmuscle form A - human ALTERNATE_NAMES cellular myosin heavy chain; myosin type 9; NMMHC-A CONTAINS myosin ATPase (EC 3.6.4.1) ORGANISM #formal_name Homo sapiens #common_name man DATE 12-May-1994 #sequence_revision 14-Jul-1994 #text_change 19-Apr-2002 ACCESSIONS A61231; A34876; I52562; I61692 REFERENCE A61231 !$#authors Simons, M.; Wang, M.; McBride, O.W.; Kawamoto, S.; Yamakawa, !1K.; Gdula, D.; Adelstein, R.S.; Weir, L. !$#journal Circ. Res. (1991) 69:530-539 !$#title Human nonmuscle myosin heavy chains are encoded by two genes !1located on different chromosomes. !$#cross-references MUID:91316803; PMID:1860190 !$#accession A61231 !'##molecule_type mRNA !'##residues 1-715 ##label SIM !'##cross-references GB:M69180; NID:g189029; PIDN:AAA61765.1; !1PID:g189030 REFERENCE A34876 !$#authors Saez, C.G.; Myers, J.C.; Shows, T.B.; Leinwand, L.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:1164-1168 !$#title Human nonmuscle myosin heavy chain mRNA: generation of !1diversity through alternative polyadenylylation. !$#cross-references MUID:90138958; PMID:1967836 !$#accession A34876 !'##molecule_type mRNA !'##residues 715-1961 ##label SAE !'##cross-references GB:M31013; NID:g189035; PIDN:AAA36349.1; !1PID:g189036 REFERENCE I52562 !$#authors Toothaker, L.E.; Gonzalez, D.A.; Tung, N.; Lemons, R.S.; Le !1Beau, M.M.; Arnaout, M.A.; Clayton, L.K.; Tenen, D.G. !$#journal Blood (1991) 78:1826-1833 !$#title Cellular myosin heavy chain in human leukocytes: isolation !1of 5' cDNA clones, characterization of the protein, !1chromosomal localization, and upregulation during myeloid !1differentiation. !$#cross-references MUID:92003925; PMID:1912569 !$#accession I52562 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-52,'EAI',56-659,'T',661-868,'T',870-930,'C',932-1239, !1'KG',1242-1337 ##label RES !'##cross-references GB:M81105; NID:g188988; PIDN:AAA59888.1; !1PID:g553596 REFERENCE A55758 !$#authors Bement, W.M.; Hasson, T.; Wirth, J.A.; Cheney, R.E.; !1Mooseker, M.S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1994) 91:6549-6553 !$#title Identification and overlapping expression of multiple !1unconventional myosin genes in vertebrate cell types. !$#cross-references MUID:94294418; PMID:8022818 !$#accession I61692 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 182-218 ##label BEM !'##cross-references GB:L29141; NID:g457249; PIDN:AAA20904.1; !1PID:g531134 GENETICS !$#gene GDB:MYH9 !'##cross-references GDB:120216; OMIM:160775 !$#map_position 22q12.3-22q13.1 CLASSIFICATION #superfamily myosin heavy chain; myosin motor domain !1homology KEYWORDS actin binding; ATP; coiled coil; hydrolase; methylated amino !1acid; nucleotide binding; P-loop; tandem repeat FEATURE !$84-764 #domain myosin motor domain homology #label MMOT\ !$174-181 #region nucleotide-binding motif A (P-loop)\ !$552-565 #region actin binding #status predicted\ !$626-640 #region actin binding #status predicted\ !$837-1938 #domain coiled coil #status predicted #label COI\ !$837-1277 #domain S2 #status predicted #label DS2\ !$1278-1961 #domain light meromyosin #status predicted #label !8LMM\ !$1939-1961 #domain carboxyl-terminal #label CBT\ !$125 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8predicted\ !$180 #binding_site ATP (Lys) #status predicted\ !$694,704 #active_site Cys #status predicted SUMMARY #length 1961 #molecular-weight 226741 #checksum 9108 SEQUENCE /// ENTRY S21801 #type complete TITLE myosin heavy chain, neuronal [similarity] - rat ALTERNATE_NAMES myosin II CONTAINS myosin ATPase (EC 3.6.4.1) ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 19-Apr-2002 ACCESSIONS S21801; PN0013; S18134 REFERENCE S21801 !$#authors Sun, W.; Chantler, P.D. !$#journal J. Mol. Biol. (1992) 224:1185-1193 !$#title Cloning of the cDNA encoding a neuronal myosin heavy chain !1from mammalian brain and its differential expression within !1the central nervous system. !$#cross-references MUID:92235856; PMID:1569576 !$#accession S21801 !'##molecule_type mRNA !'##residues 1-1999 ##label SUN !'##cross-references EMBL:X62659 REFERENCE PN0013 !$#authors Sun, W.; Chantler, P.D. !$#journal Biochem. Biophys. Res. Commun. (1991) 175:244-249 !$#title A unique cellular myosin II exhibiting differential !1expression in the cerebral cortex. !$#cross-references MUID:91151356; PMID:1998509 !$#accession PN0013 !'##molecule_type mRNA !'##residues 1914-1998,'I' ##label SU2 !'##experimental_source brain CLASSIFICATION #superfamily myosin heavy chain; myosin motor domain !1homology KEYWORDS actin binding; ATP; coiled coil; hydrolase; methylated amino !1acid; nucleotide binding; P-loop; phosphoprotein; tandem !1repeat FEATURE !$84-763 #domain myosin motor domain homology #label MMOT\ !$174-181 #region nucleotide-binding motif A (P-loop)\ !$541-575 #region actin binding #status predicted\ !$653-675 #region actin binding #status predicted\ !$836-1999 #domain coiled coil #status predicted #label COI\ !$836-1276 #region S2\ !$1277-1999 #region light meromyosin\ !$125 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8predicted\ !$180 #binding_site ATP (Lys) #status predicted\ !$693,703 #active_site Cys #status predicted\ !$1916 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$1943 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 1999 #molecular-weight 231456 #checksum 1092 SEQUENCE /// ENTRY A33977 #type complete TITLE myosin heavy chain, nonmuscle - chicken CONTAINS myosin ATPase (EC 3.6.4.1) ORGANISM #formal_name Gallus gallus #common_name chicken DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 19-Apr-2002 ACCESSIONS A33977; S06116; A43422 REFERENCE A33977 !$#authors Shohet, R.V.; Conti, M.A.; Kawamoto, S.; Preston, Y.A.; !1Brill, D.A.; Adelstein, R.S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:7726-7730 !$#title Cloning of the cDNA encoding the myosin heavy chain of a !1vertebrate cellular myosin. !$#cross-references MUID:90046668; PMID:2813355 !$#accession A33977 !'##molecule_type mRNA !'##residues 1-1959 ##label SHO !'##cross-references GB:M26510; NID:g212382; PIDN:AAA48974.1; !1PID:g212383 REFERENCE S06116 !$#authors Katsuragawa, Y.; Yanagisawa, M.; Inoue, A.; Masaki, T. !$#journal Eur. J. Biochem. (1989) 184:611-616 !$#title Two distinct nonmuscle myosin-heavy-chain mRNAs are !1differentially expressed in various chicken tissues. !1Identification of a novel gene family of vertebrate !1non-sarcomeric myosin heavy chains. !$#cross-references MUID:90032648; PMID:2806244 !$#accession S06116 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 716-1008 ##label KAT !'##cross-references GB:X17589 !'##note this translation is not annotated in GenBank entry GGMHCFMHA, !1release 114 REFERENCE A43422 !$#authors Hodge, T.P.; Cross, R.; Kendrick-Jones, J. !$#journal J. Cell Biol. (1992) 118:1085-1095 !$#title Role of the COOH-terminal nonhelical tailpiece in the !1assembly of a vertebrate nonmuscle myosin rod. !$#cross-references MUID:92381096; PMID:1512291 !$#accession A43422 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type mRNA !'##residues 1900-1959 ##label HOD !'##experimental_source brush border !'##note sequence extracted from NCBI backbone (NCBIP:111947) CLASSIFICATION #superfamily myosin heavy chain; myosin motor domain !1homology KEYWORDS actin binding; ATP; coiled coil; hydrolase; methylated amino !1acid; nucleotide binding; P-loop; tandem repeat FEATURE !$84-764 #domain myosin motor domain homology #label MMOT\ !$174-181 #region nucleotide-binding motif A (P-loop)\ !$552-565 #region actin binding #status predicted\ !$626-640 #region actin binding #status predicted\ !$837-1936 #domain coiled coil #status predicted #label COI\ !$837-1277 #region S2\ !$1278-1959 #region light meromyosin\ !$1937-1959 #domain carboxyl-terminal #label CBT\ !$125 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8predicted\ !$180 #binding_site ATP (Lys) #status predicted\ !$694,704 #active_site Cys #status predicted SUMMARY #length 1959 #molecular-weight 226502 #checksum 3641 SEQUENCE /// ENTRY B43402 #type complete TITLE myosin heavy chain-B, neuronal - chicken CONTAINS myosin ATPase (EC 3.6.4.1) ORGANISM #formal_name Gallus gallus #common_name chicken DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 19-Apr-2002 ACCESSIONS B43402; A43402 REFERENCE A43402 !$#authors Takahashi, M.; Kawamoto, S.; Adelstein, R.S. !$#journal J. Biol. Chem. (1992) 267:17864-17871 !$#title Evidence for inserted sequences in the head region of !1nonmuscle myosin specific to the nervous system. Cloning of !1the cDNA encoding the myosin heavy chain-B isoform of !1vertebrate nonmuscle myosin. !$#cross-references MUID:92388144; PMID:1355479 !$#accession B43402 !'##molecule_type mRNA !'##residues 1-2007 ##label TAK !'##cross-references GB:M93676; NID:g212448; PIDN:AAA48988.1; !1PID:g212452 !'##note the sequence of residues 212-221 and 632-652 and the !1corresponding nucleotide sequences are not given !$#accession A43402 !'##molecule_type mRNA !'##residues 1-211;222-631;653-2007 ##label TA2 !'##cross-references GB:M93676; NID:g212448; PIDN:AAA48985.1; !1PID:g212449 !'##note sequence extracted from NCBI backbone (NCBIN:112864) COMMENT Alternatively spliced segments 1 and 2 are found exclusively !1in nonmuscle myosin heavy chain isolated from the nervous !1system. CLASSIFICATION #superfamily myosin heavy chain; myosin motor domain !1homology KEYWORDS actin binding; alternative splicing; ATP; coiled coil; !1hydrolase; methylated amino acid; nucleotide binding; !1P-loop; phosphoprotein FEATURE !$1-2007 #product myosin heavy chain-B, neuronal #status !8predicted #label MYN\ !$1-211,222-631, !$653-2007 #product myosin heavy chain-B, nonmuscle #status !8predicted #label MYS\ !$88-802 #domain myosin motor domain homology #label MMOT\ !$178-185 #region nucleotide-binding motif A (P-loop)\ !$212-221 #region alternatively spliced segment 1 #status !8experimental\ !$559-593 #region actin binding #status predicted\ !$632-652 #region alternatively spliced segment 2 #status !8experimental\ !$692-714 #region actin binding #status predicted\ !$875-2007 #domain coiled coil #status predicted #label COI\ !$875-1315 #region S2\ !$1316-2007 #region light meromyosin\ !$129 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8predicted\ !$184 #binding_site ATP (Lys) #status predicted\ !$732,742 #active_site Cys #status predicted\ !$1954 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$1987 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 2007 #molecular-weight 232592 #checksum 7899 SEQUENCE /// ENTRY A36014 #type complete TITLE myosin heavy chain, nonmuscle - fruit fly (Drosophila melanogaster) CONTAINS myosin ATPase (EC 3.6.4.1) ORGANISM #formal_name Drosophila melanogaster DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 19-Apr-2002 ACCESSIONS A36014; B36014 REFERENCE A36014 !$#authors Ketchum, A.S.; Stewart, C.T.; Stewart, M.; Kiehart, D.P. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:6316-6320 !$#title Complete sequence of the Drosophila nonmuscle myosin !1heavy-chain transcript: conserved sequences in the myosin !1tail and differential splicing in the 5' untranslated !1sequence. !$#cross-references MUID:90349606; PMID:2117279 !$#accession A36014 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-2017 ##label KET !'##cross-references GB:M35012 GENETICS !$#gene FlyBase:zip !'##cross-references FlyBase:FBgn0005634 CLASSIFICATION #superfamily myosin heavy chain; myosin motor domain !1homology KEYWORDS actin binding; alternative splicing; ATP; coiled coil; !1hydrolase; methylated amino acid; nucleotide binding; !1P-loop; tandem repeat FEATURE !$1-2017 #product myosin heavy chain, form I #status predicted !8#label MA1\ !$46-2017 #product myosin heavy chain, form II #status !8predicted #label MA2\ !$135-815 #domain myosin motor domain homology #label MMOT\ !$225-232 #region nucleotide-binding motif A (P-loop)\ !$598-631 #region actin binding #status predicted\ !$705-727 #region actin binding #status predicted\ !$888-2017 #domain coiled coil #status predicted #label COI\ !$888-1328 #region S2\ !$1329-2017 #region light meromyosin\ !$176 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8predicted\ !$231 #binding_site ATP (Lys) #status predicted\ !$745,755 #active_site Cys #status predicted SUMMARY #length 2017 #molecular-weight 232016 #checksum 7419 SEQUENCE /// ENTRY A27224 #type complete TITLE myosin heavy chain II - Acanthamoeba castellanii CONTAINS myosin ATPase (EC 3.6.4.1) ORGANISM #formal_name Acanthamoeba castellanii DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 19-Apr-2002 ACCESSIONS A27224 REFERENCE A27224 !$#authors Hammer III, J.A.; Bowers, B.; Paterson, B.M.; Korn, E.D. !$#journal J. Cell Biol. (1987) 105:913-925 !$#title Complete nucleotide sequence and deduced polypeptide !1sequence of a nonmuscle myosin heavy chain gene from !1Acanthamoeba: evidence of a hinge in the rodlike tail. !$#cross-references MUID:87308395; PMID:3040773 !$#accession A27224 !'##molecule_type DNA !'##residues 1-1509 ##label HAM !'##cross-references GB:Y00624; GB:M12702; GB:M12703; GB:M19549; !1NID:g5585; PIDN:CAA68663.1; PID:g5586 GENETICS !$#introns 69/3; 119/3; 181/2 CLASSIFICATION #superfamily myosin heavy chain; myosin motor domain !1homology KEYWORDS actin binding; ATP; coiled coil; hydrolase; methylated amino !1acid; nucleotide binding; P-loop; phosphoprotein; tandem !1repeat FEATURE !$92-775 #domain myosin motor domain homology #label MMOT\ !$182-189 #region nucleotide-binding motif A (P-loop)\ !$544-576 #region actin binding #status predicted\ !$660-682 #region actin binding #status predicted\ !$848-1227 #domain coiled coil #status predicted #label COI\ !$1228-1247 #domain hinge #label HIN\ !$1248-1482 #domain coiled coil #status predicted #label CO2\ !$1483-1509 #domain carboxyl-terminal #label CBT\ !$133 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8predicted\ !$188 #binding_site ATP (Lys) #status predicted SUMMARY #length 1509 #molecular-weight 171200 #checksum 528 SEQUENCE /// ENTRY A23662 #type complete TITLE myosin I, high molecular weight - Acanthamoeba sp. ALTERNATE_NAMES myosin, HMWMI CONTAINS myosin ATPase (EC 3.6.4.1) ORGANISM #formal_name Acanthamoeba sp. DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 19-Apr-2002 ACCESSIONS A23662 REFERENCE A23662 !$#authors Horowitz, J.A.; Hammer III, J.A. !$#journal J. Biol. Chem. (1990) 265:20646-20652 !$#title A new Acanthamoeba myosin heavy chain. Cloning of the gene !1and immunological identification of the polypeptide. !$#cross-references MUID:91056121; PMID:2243110 !$#accession A23662 !'##molecule_type DNA !'##residues 1-1576 ##label HOR !'##cross-references GB:J05678 !'##note the authors translated the codon GGT for residue 280 as Ser, !1and failed to translate the codon TCG for residue 281 as Ser !'##note the nucleotide sequence in GB:J05678 differs from that shown in !1the paper in having the codon TGT for residue 725 and in !1having an additional three nucleotides, "HTG," between the !1codons for residues 725 and 726 GENETICS !$#introns 54/3; 105/3; 162/3; 210/1; 324/2; 416/3; 577/1; 644/2; 731/ !11; 1038/1; 1090/1; 1167/3; 1203/2; 1295/2; 1377/3; 1406/3; !11541/2 CLASSIFICATION #superfamily myosin I, high molecular weight; myosin motor !1domain homology; SH3 homology KEYWORDS actin binding; ATP; hydrolase; nucleotide binding; P-loop FEATURE !$78-738 #domain myosin motor domain homology #label MMOT\ !$168-175 #region nucleotide-binding motif A (P-loop)\ !$629-650 #region actin binding #status predicted\ !$783-1575 #domain carboxyl-terminal #label CTD\ !$1445-1510 #region glutamine-rich\ !$1525-1573 #domain SH3 homology #label SH3\ !$174 #binding_site ATP (Lys) #status predicted SUMMARY #length 1576 #molecular-weight 177502 #checksum 6844 SEQUENCE /// ENTRY S19188 #type complete TITLE myosin-V - chicken ALTERNATE_NAMES calmodulin-binding protein; myosin I heavy chain, 190K ORGANISM #formal_name Gallus gallus #common_name chicken DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 19-Jan-2001 ACCESSIONS S19188; A44359; B44359; S29249 REFERENCE S19188 !$#authors Espreafico, E.M.; Cheney, R.E.; Matteoli, M.; Nascimento, !1A.A.; De-Camilli, P.V.; Larson, R.E.; Mooseker, M.S. !$#submission submitted to the EMBL Data Library, February 1992 !$#description Complete cDNA coding sequence of chicken brain p190, a !1calmodulin binding unconventional myosin that shares !1similarity with the mouse Dilute and yeast MYO2 gene !1products. !$#accession S19188 !'##molecule_type mRNA !'##residues 1-1830 ##label ESP !'##cross-references EMBL:Z11718 REFERENCE A44359 !$#authors Espreafico, E.M.; Cheney, R.E.; Matteoli, M.; Nascimento, !1A.A.; De Camilli, P.V.; Larson, R.E.; Mooseker, M.S. !$#journal J. Cell Biol. (1992) 119:1541-1557 !$#title Primary structure and cellular localization of chicken brain !1myosin-V (p190), an unconventional myosin with calmodulin !1light chains. !$#cross-references MUID:93107155; PMID:1469047 !$#accession A44359 !'##molecule_type mRNA !'##residues 1-1688,'R',1690-1830 ##label ES2 !'##experimental_source brain !'##note sequence extracted from NCBI backbone (NCBIN:121153, !1NCBIP:121154) !'##note the codon CGC for residue 1689 is inconsistent with the codon !1AGC for residue 1689 in reference S19188 !$#accession B44359 !'##molecule_type protein !'##residues 155-164 ##label ES3 REFERENCE S29249 !$#authors Sanders, G.; Lichte, B.; Meyer, H.E.; Kilimann, M.W. !$#journal FEBS Lett. (1992) 311:295-298 !$#title cDNA encoding the chicken ortholog of the mouse dilute gene !1product. Sequence comparison reveals a myosin I subfamily !1with conserved C-terminal domains. !$#cross-references MUID:93012002; PMID:1383040 !$#accession S29249 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-1142,1144-1830 ##label SAN !'##cross-references EMBL:X67251; NID:g63364; PIDN:CAA47673.1; !1PID:g63365 COMMENT The neck domain comprises six approximately 23-residue !1tandem repeats; this domain may be responsible for !1calmodulin binding. CLASSIFICATION #superfamily myosin MYO2; myosin motor domain homology KEYWORDS actin binding; ATP; brain; coiled coil; nucleotide binding; !1P-loop; phosphoprotein; tandem repeat FEATURE !$72-752 #domain myosin motor domain homology #label MMOT\ !$163-170 #region nucleotide-binding motif A (P-loop)\ !$645-666 #region actin binding #status predicted\ !$765-909 #domain neck #status predicted #label NEC\ !$912-1420 #domain coiled coil #status predicted #label COI\ !$1421-1830 #domain carboxyl-terminal domain #status predicted !8#label CTD\ !$169 #binding_site ATP (Lys) #status predicted\ !$1735 #binding_site phosphate (Thr) (covalent) #status !8predicted SUMMARY #length 1830 #molecular-weight 212509 #checksum 6383 SEQUENCE /// ENTRY A46761 #type complete TITLE myosin heavy chain, dilute - mouse CONTAINS myosin ATPase (EC 3.6.4.1) ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 19-Apr-2002 ACCESSIONS A46761; S13652 REFERENCE A46761 !$#authors Mercer, J.A. !$#submission submitted to GenBank, June 1991 !$#accession A46761 !'##molecule_type mRNA !'##residues 1-1853 ##label MER !'##cross-references GB:X57377; NID:g50714; PIDN:CAA40651.1; PID:g50715 REFERENCE S13652 !$#authors Mercer, J.A.; Seperack, P.K.; Strobel, M.C.; Copeland, N.G.; !1Jenkins, N.A. !$#journal Nature (1991) 349:709-713 !$#title Novel myosin heavy chain encoded by murine dilute coat !1colour locus. !$#cross-references MUID:91141583; PMID:1996138 !$#accession S13652 !'##molecule_type mRNA !'##residues 1-366,'IMKRCVTALPPKA',381-1853 ##label ME2 COMMENT The neck domain comprises six approximately 23-residue !1tandem repeats; this domain may be responsible for !1calmodulin binding. CLASSIFICATION #superfamily myosin MYO2; myosin motor domain homology KEYWORDS actin binding; ATP; coiled coil; hydrolase; nucleotide !1binding; P-loop; phosphoprotein; tandem repeat FEATURE !$72-751 #domain myosin motor domain homology #label MMOT\ !$163-170 #region nucleotide-binding motif A (P-loop)\ !$644-665 #region actin binding #status predicted\ !$764-908 #domain neck #label NEC\ !$911-1443 #domain coiled coil #status predicted #label COI\ !$1444-1853 #domain carboxyl-terminal #label CTD\ !$169 #binding_site ATP (Lys) #status predicted\ !$1758 #binding_site phosphate (Thr) (covalent) #status !8predicted SUMMARY #length 1853 #molecular-weight 215593 #checksum 8703 SEQUENCE /// ENTRY A38454 #type complete TITLE myosin MYO2 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein O6167; protein YOR326w CONTAINS myosin ATPase (EC 3.6.4.1) ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 19-Apr-2002 ACCESSIONS A38454; S58339; S62058; S67232; S67233; S71966; S72009 REFERENCE A38454 !$#authors Johnston, G.C.; Prendergast, J.A.; Singer, R.A. !$#journal J. Cell Biol. (1991) 113:539-551 !$#title The Saccharomyces cerevisiae MYO2 gene encodes an essential !1myosin for vectorial transport of vesicles. !$#cross-references MUID:91201404; PMID:2016335 !$#accession A38454 !'##molecule_type DNA !'##residues 1-1574 ##label JOH !'##cross-references GB:M35532; NID:g172021; PIDN:AAA34810.1; !1PID:g172022 REFERENCE S58318 !$#authors Pearson, B.M.; Hernando, Y.; Wolf, S.S.; Kalogeropoulos, A.; !1Schweizer, M. !$#submission submitted to the EMBL Data Library, August 1995 !$#accession S58339 !'##molecule_type DNA !'##residues 1-748 ##label PEA !'##cross-references EMBL:X90565; NID:g940836; PIDN:CAA62184.1; !1PID:g940860 REFERENCE S62058 !$#authors Parle, A.G.; Hand, N.J.; Goulding, S.G.; Wolfe, K.H. !$#submission submitted to the EMBL Data Library, June 1995 !$#description Sequence of 29 kilobases around the PDR10 locus on the right !1arm of Saccharomyces cerevisiae chromosome XV: similarity to !1part of chromosome I. !$#accession S62058 !'##molecule_type DNA !'##residues 677-1574 ##label PAR !'##cross-references EMBL:Z49821; NID:g1163062; PIDN:CAA89973.1; !1PID:g1163063 REFERENCE S67213 !$#authors Pearson, B.M.; Hernando, Y.; Kalogeropoulos, A.; Schweizer, !1M. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67232 !'##molecule_type DNA !'##residues 1-748 ##label PEW !'##cross-references EMBL:Z75234; GSPDB:GN00015; MIPS:YOR326w !'##experimental_source strain S288C REFERENCE S67233 !$#authors Goulding, S.E.; Hand, N.J.; Parle-McDermott, A.G.; Wolfe, !1K.H. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67233 !'##molecule_type DNA !'##residues 677-1574 ##label GOU !'##cross-references EMBL:Z75234; GSPDB:GN00015; MIPS:YOR326w !'##experimental_source strain S288C REFERENCE S71966 !$#authors Parle-McDermott, A.G.; Hand, N.J.; Goulding, S.E.; Wolfe, !1K.H. !$#journal Yeast (1996) 12:999-1004 !$#title Sequence of 29 kb around the PDR10 locus on the right arm of !1Saccharomyces cerevisiae chromosome XV: similarity to part !1of chromosome I. !$#cross-references MUID:97051586; PMID:8896263 !$#accession S71966 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 677-1574 ##label PAW !'##cross-references EMBL:Z49821; NID:g1163062; PIDN:CAA89973.1; !1PID:g1163063 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1995 REFERENCE S71986 !$#authors Pearson, B.M.; Hernando, Y.; Payne, J.; Wolf, S.S.; !1Kalogeropoulos, A.; Schweizer, M. !$#journal Yeast (1996) 12:1021-1031 !$#title Sequencing of a 35.71 kb DNA segment on the right arm of !1yeast chromosome XV reveals regions of similarity to !1chromosomes I and XIII. !$#cross-references MUID:97051589; PMID:8896266 !$#accession S72009 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-748 ##label PEF !'##cross-references EMBL:X90565; NID:g940836; PIDN:CAA62184.1; !1PID:g940860 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1995 COMMENT The neck domain comprises six approximately 23-residue !1tandem repeats; this domain may be responsible for !1calmodulin binding. GENETICS !$#gene SGD:MYO2; MIPS:YOR326w !'##cross-references SGD:S0005853; MIPS:YOR326w !$#map_position 15R FUNCTION !$#description involved in vacuole inheritance; involved in polarized !1growth and secretion; plays a role in vesicle transport !1along actin cables to the bud site CLASSIFICATION #superfamily myosin MYO2; myosin motor domain homology KEYWORDS actin binding; ATP; coiled coil; cytoskeleton; hydrolase; !1nucleotide binding; P-loop; phosphoprotein; tandem repeat FEATURE !$73-769 #domain myosin motor domain homology #label MMOT\ !$164-171 #region nucleotide-binding motif A (P-loop)\ !$652-673 #region actin binding #status predicted\ !$782-926 #domain neck #status predicted #label NEC\ !$942-1086 #domain coiled coil #status predicted #label COI\ !$1087-1574 #domain carboxyl-terminal #status predicted #label !8CTD\ !$170 #binding_site ATP (Lys) #status predicted\ !$692,702 #active_site Cys #status predicted\ !$1097,1452 #binding_site phosphate (Thr) (covalent) #status !8predicted SUMMARY #length 1574 #molecular-weight 180679 #checksum 13 SEQUENCE /// ENTRY S30790 #type complete TITLE myosin MYO4 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YAL029c CONTAINS myosin ATPase (EC 3.6.4.1) ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 19-Apr-2002 ACCESSIONS S30790; S51991 REFERENCE S30790 !$#authors Haarer, B.K.; Brown, S.S. !$#submission submitted to the EMBL Data Library, March 1992 !$#description Identification of a yeast myosin gene that is similar to the !1yeast MY02 gene. !$#accession S30790 !'##molecule_type DNA !'##residues 1-1471 ##label HAA !'##cross-references EMBL:M90057; NID:g172023; PIDN:AAC37409.1; !1PID:g172024 REFERENCE S51956 !$#authors Bussey, H.; Kaback, D.B.; Zhong, W.; Vo, D.T.; Clark, M.W.; !1Fortin, N.; Hall, J.; Ouellette, B.F.F.; Keng, T.; Barton, !1A.B.; Su, Y.; Davies, C.K.; Storms, R.K. !$#submission submitted to the EMBL Data Library, August 1994 !$#description The sequence of chromosome 1 of Saccharomyces cerevisiae. !$#accession S51991 !'##molecule_type DNA !'##residues 1-1471 ##label BUS !'##cross-references EMBL:U12980; NID:g1326053; PIDN:AAC05003.1; !1PID:g595556; GSPDB:GN00001; MIPS:YAL029c COMMENT The neck domain comprises six approximately 23-residue !1tandem repeats; this domain may be responsible for !1calmodulin binding. GENETICS !$#gene SGD:MYO4; SHE1; FUN22; MIPS:YAL029c !'##cross-references SGD:S0000027; MIPS:YAL029c !$#map_position 1L CLASSIFICATION #superfamily myosin MYO2; myosin motor domain homology KEYWORDS actin binding; ATP; coiled coil; hydrolase; nucleotide !1binding; P-loop; tandem repeat FEATURE !$74-765 #domain myosin motor domain homology #label MMOT\ !$165-172 #region nucleotide-binding motif A (P-loop)\ !$648-669 #region actin binding #status predicted\ !$778-922 #domain neck #status predicted #label NEC\ !$938-1063 #domain coiled coil #status predicted #label COI\ !$1064-1471 #domain carboxyl-terminal #status predicted #label !8CTD\ !$171 #binding_site ATP (Lys) #status predicted\ !$688,698 #active_site Cys #status predicted SUMMARY #length 1471 #molecular-weight 169342 #checksum 5941 SEQUENCE /// ENTRY A44400 #type complete TITLE myosin heavy chain 95F - fruit fly (Drosophila melanogaster) CONTAINS myosin ATPase (EC 3.6.4.1) ORGANISM #formal_name Drosophila melanogaster DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 19-Apr-2002 ACCESSIONS A44400; S28457 REFERENCE A44400 !$#authors Kellerman, K.A.; Miller, K.G. !$#journal J. Cell Biol. (1992) 119:823-834 !$#title An unconventional myosin heavy chain gene from Drosophila !1melanogaster. !$#cross-references MUID:93054915; PMID:1429838 !$#accession A44400 !'##molecule_type mRNA !'##residues 1-1253 ##label KEL !'##cross-references EMBL:X67077; NID:g8213; PIDN:CAA47462.1; PID:g8214 !'##experimental_source clone Em-3 !'##note sequence extracted from NCBI backbone (NCBIP:117200) GENETICS !$#gene FlyBase:Mhc95F !'##cross-references FlyBase:FBgn0011225 !$#map_position 95F CLASSIFICATION #superfamily myosin heavy chain 95F; myosin motor domain !1homology KEYWORDS actin binding; alternative splicing; ATP; coiled coil; !1hydrolase; nucleotide binding; P-loop FEATURE !$60-754 #domain myosin motor domain homology #label MMOT\ !$151-158 #region nucleotide-binding motif A (P-loop)\ !$643-666 #region actin binding #status predicted\ !$815-826 #region myosin light chain binding #status predicted\ !$912-1008 #domain coiled coil #status predicted #label COI\ !$157 #binding_site ATP (Lys) #status predicted SUMMARY #length 1253 #molecular-weight 143284 #checksum 243 SEQUENCE /// ENTRY MWAXIB #type complete TITLE myosin heavy chain IB - Acanthamoeba castellanii CONTAINS myosin ATPase (EC 3.6.4.1) ORGANISM #formal_name Acanthamoeba castellanii DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 19-Apr-2002 ACCESSIONS JQ0095; B34448 REFERENCE JQ0095 !$#authors Jung, G.; Schmidt, C.J.; Hammer III, J.A. !$#journal Gene (1989) 82:269-280 !$#title Myosin I heavy-chain genes of Acanthamoeba castellanii: !1cloning of a second gene and evidence for the existence of a !1third isoform. !$#cross-references MUID:90060816; PMID:2511079 !$#accession JQ0095 !'##molecule_type DNA !'##residues 1-1147 ##label JUN !'##cross-references GB:M30780 !'##note this organism expresses at least three isoforms of myosin I !1heavy-chain, encoded by genes MIA, MIB, and MIC; the protein !1shown here, called MIL by the authors, is now known to be !1the product of gene MIB, whereas the protein previously !1identified as MIB is the product of gene MIC REFERENCE A34448 !$#authors Brzeska, H.; Lynch, T.J.; Martin, B.; Korn, E.D. !$#journal J. Biol. Chem. (1989) 264:19340-19348 !$#title The localization and sequence of the phosphorylation sites !1of Acanthamoeba myosins I. An improved method for locating !1the phosphorylated amino acid. !$#cross-references MUID:90037074; PMID:2530230 !$#accession B34448 !'##molecule_type protein !'##residues 538-550,'X',552-559 ##label BRZ COMMENT In this protein, the coiled-coil rod-like region found in !1many myosin heavy chains is replaced by a carboxyl-terminal !1domain containing a region rich in glycine, alanine, and !1proline. The protein is globular and does not self-assemble !1into filaments. GENETICS !$#gene MIB !$#introns 1/3; 39/3; 102/2; 135/3; 183/3; 212/1; 291/3; 379/3; 492/3; !1617/2; 649/3; 789/1; 860/2; 907/1; 994/1; 1094/3 CLASSIFICATION #superfamily protozoan myosin heavy chain IB; myosin motor !1domain homology; SH3 homology KEYWORDS actin binding; ATP; hydrolase; nucleotide binding; P-loop; !1phosphoprotein; tandem repeat FEATURE !$12-664 #domain myosin motor domain homology #label MMOT\ !$103-110 #region nucleotide-binding motif A (P-loop)\ !$552-573 #region actin binding #status predicted\ !$698-1147 #domain carboxyl-terminal #label CTD\ !$698-889 #region basic\ !$910-1094 #region alanine/glycine/proline-rich\ !$1097-1144 #domain SH3 homology #label SH3\ !$109 #binding_site ATP (Lys) #status predicted\ !$315 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 1147 #molecular-weight 124915 #checksum 5031 SEQUENCE /// ENTRY A33284 #type complete TITLE myosin heavy chain IB - slime mold (Dictyostelium discoideum) CONTAINS myosin ATPase (EC 3.6.4.1) ORGANISM #formal_name Dictyostelium discoideum DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 19-Apr-2002 ACCESSIONS A33284 REFERENCE A33284 !$#authors Jung, G.; Saxe III, C.L.; Kimmel, A.R.; Hammer III, J.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:6186-6190 !$#title Dictyostelium discoideum contains a gene encoding a myosin I !1heavy chain. !$#cross-references MUID:89345628; PMID:2762320 !$#accession A33284 !'##molecule_type DNA !'##residues 1-1111 ##label JUN !'##cross-references GB:M26037; NID:g167838; PIDN:AAA33229.1; !1PID:g167839 GENETICS !$#introns 1/3; 39/3 CLASSIFICATION #superfamily protozoan myosin heavy chain IB; myosin motor !1domain homology; SH3 homology KEYWORDS actin binding; ATP; hydrolase; nucleotide binding; P-loop; !1phosphoprotein; tandem repeat FEATURE !$12-678 #domain myosin motor domain homology #label MMOT\ !$102-109 #region nucleotide-binding motif A (P-loop)\ !$566-587 #region actin binding #status predicted\ !$712-1111 #domain carboxyl-terminal #label CTD\ !$712-901 #region basic\ !$922-1058 #region alanine/glutamine/glycine/proline-rich\ !$1060-1108 #domain SH3 homology #label SH3\ !$108 #binding_site ATP (Lys) #status predicted\ !$332 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 1111 #molecular-weight 124313 #checksum 697 SEQUENCE /// ENTRY MWAXIC #type complete TITLE myosin heavy chain IC - Acanthamoeba castellanii CONTAINS myosin ATPase (EC 3.6.4.1) ORGANISM #formal_name Acanthamoeba castellanii DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 19-Apr-2002 ACCESSIONS A33891; C34448; A24146 REFERENCE A33891 !$#authors Jung, G.; Korn, E.D.; Hammer III, J.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:6720-6724 !$#title The heavy chain of Acanthamoeba myosin IB is a fusion of !1myosin-like and non-myosin-like sequences. !$#cross-references MUID:88016163; PMID:3477803 !$#accession A33891 !'##molecule_type DNA !'##residues 1-1168 ##label JUN !'##cross-references GB:J02974; NID:g155624; PIDN:AAA27707.1; !1PID:g155625 !'##note this gene and protein are called MIB in this paper REFERENCE A34448 !$#authors Brzeska, H.; Lynch, T.J.; Martin, B.; Korn, E.D. !$#journal J. Biol. Chem. (1989) 264:19340-19348 !$#title The localization and sequence of the phosphorylation sites !1of Acanthamoeba myosins I. An improved method for locating !1the phosphorylated amino acid. !$#cross-references MUID:90037074; PMID:2530230 !$#accession C34448 !'##molecule_type protein !'##residues 308-314,'X',316-329 ##label BRZ COMMENT In this protein, the coiled-coil rod-like region found in !1many myosin heavy chains is replaced by a carboxyl-terminal !1domain containing two regions rich in glycine, alanine, and !1proline. The protein is globular and does not self-associate !1into filaments. GENETICS !$#gene MIC !$#introns 1/3; 37/3; 60/2; 100/2; 153/3; 179/3; 208/2; 242/3; 287/3; !1321/3; 371/3; 428/3; 452/2; 482/3; 515/3; 627/1; 687/2; 736/ !11; 808/1; 895/1; 977/1; 1056/1; 1129/1 CLASSIFICATION #superfamily protozoan myosin heavy chain IB; myosin motor !1domain homology; SH3 homology KEYWORDS actin binding; ATP; hydrolase; nucleotide binding; P-loop; !1phosphoprotein; tandem repeat FEATURE !$10-653 #domain myosin motor domain homology #label MMOT\ !$101-108 #region nucleotide-binding motif A (P-loop)\ !$543-564 #region actin binding #status predicted\ !$671-1168 #domain carboxyl-terminal #label CTD\ !$675-883 #region basic\ !$923-978 #region alanine/glycine/proline-rich\ !$983-1030 #domain SH3 homology #label SH3\ !$1034-1168 #region alanine/glycine/proline-rich\ !$107 #binding_site ATP (Lys) #status predicted\ !$311 #binding_site phosphate (Ser) (covalent) #status !8experimental SUMMARY #length 1168 #molecular-weight 127309 #checksum 4021 SEQUENCE /// ENTRY A47106 #type complete TITLE myosin heavy chain ID - slime mold (Dictyostelium discoideum) CONTAINS myosin ATPase (EC 3.6.4.1) ORGANISM #formal_name Dictyostelium discoideum DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 19-Apr-2002 ACCESSIONS A47106; B47106 REFERENCE A47106 !$#authors Jung, G.; Fukui, Y.; Martin, B.; Hammer III, J.A. !$#journal J. Biol. Chem. (1993) 268:14981-14990 !$#title Sequence, expression pattern, intracellular localization, !1and targeted disruption of the Dictyostelium myosin ID heavy !1chain isoform. !$#cross-references MUID:93315475; PMID:8325874 !$#contents AX3 !$#accession A47106 !'##molecule_type DNA !'##residues 1-782 ##label JUN !'##note sequence extracted from NCBI backbone (NCBIN:134989, !1NCBIP:134990) !$#accession B47106 !'##molecule_type mRNA !'##residues 577-1113 ##label JU2 !'##note sequence extracted from NCBI backbone (NCBIN:134989, !1NCBIP:134990) GENETICS !$#introns 37/3; 214/1 CLASSIFICATION #superfamily protozoan myosin heavy chain IB; myosin motor !1domain homology; SH3 homology KEYWORDS actin binding; ATP; hydrolase; nucleotide binding; P-loop; !1tandem repeat FEATURE !$10-678 #domain myosin motor domain homology #label MMOT\ !$101-108 #region nucleotide-binding motif A (P-loop)\ !$565-586 #region actin binding #status predicted\ !$685-1113 #domain carboxyl-terminal #label CTD\ !$685-913 #region basic\ !$920-968 #region alanine/glycine/proline-rich\ !$969-1016 #domain SH3 homology #label SH3\ !$1016-1113 #region alanine/glycine/proline-rich\ !$107 #binding_site ATP (Lys) #status predicted SUMMARY #length 1113 #molecular-weight 124637 #checksum 7004 SEQUENCE /// ENTRY S31926 #type complete TITLE myosin IB heavy chain, brush border - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S31926 REFERENCE S31926 !$#authors Knight, A.E.; Kendrick-Jones, J. !$#submission submitted to the EMBL Data Library, February 1993 !$#description A novel vertebrate myosin I. !$#accession S31926 !'##status preliminary !'##molecule_type mRNA !'##residues 1-1099 ##label KNI !'##cross-references EMBL:X70400; NID:g65323; PIDN:CAA49850.1; !1PID:g65324 CLASSIFICATION #superfamily protozoan myosin heavy chain IB; myosin motor !1domain homology; SH3 homology KEYWORDS nucleotide binding; P-loop FEATURE !$20-677 #domain myosin motor domain homology #label MMOT\ !$110-117 #region nucleotide-binding motif A (P-loop)\ !$1049-1096 #domain SH3 homology #label SH3 SUMMARY #length 1099 #molecular-weight 126207 #checksum 2081 SEQUENCE /// ENTRY S52517 #type complete TITLE myosin I heavy chain - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S52517 REFERENCE S52517 !$#authors Stoeffler, H.E.; Reinhard, J.; Ruppert, C.; Baehler, M. !$#submission submitted to the EMBL Data Library, August 1993 !$#description Identification of a rat myosin I with a C-terminal !1SH3-domain. !$#accession S52517 !'##status preliminary !'##molecule_type mRNA !'##residues 1-1107 ##label STO !'##cross-references EMBL:X74815; NID:g693994; PIDN:CAA52815.1; !1PID:g693995 CLASSIFICATION #superfamily protozoan myosin heavy chain IB; myosin motor !1domain homology; SH3 homology KEYWORDS nucleotide binding; P-loop FEATURE !$22-679 #domain myosin motor domain homology #label MMOT\ !$112-119 #region nucleotide-binding motif A (P-loop)\ !$1057-1104 #domain SH3 homology #label SH3 SUMMARY #length 1107 #molecular-weight 126826 #checksum 2420 SEQUENCE /// ENTRY A29483 #type complete TITLE myosin heavy chain I, brush border - bovine ALTERNATE_NAMES myosin I heavy chain-like protein, MIHC CONTAINS myosin ATPase (EC 3.6.4.1) ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 19-Apr-2002 ACCESSIONS A29483; JX0208 REFERENCE A29483 !$#authors Hoshimaru, M.; Nakanishi, S. !$#journal J. Biol. Chem. (1987) 262:14625-14632 !$#title Identification of a new type of mammalian myosin heavy chain !1by molecular cloning. Overlap of its mRNA with !1preprotachykinin B mRNA. !$#cross-references MUID:88033016; PMID:3667594 !$#accession A29483 !'##molecule_type mRNA !'##residues 1-1043 ##label HOS !'##cross-references GB:J02819; NID:g163405; PIDN:AAA30658.1; !1PID:g163406 REFERENCE JX0208 !$#authors Kawakami, H.; Moriyoshi, K.; Utsumi, T.; Nakanishi, S. !$#journal J. Biochem. (1992) 111:302-309 !$#title Structural organization and expression of the gene for !1bovine myosin I heavy chain. !$#cross-references MUID:92268028; PMID:1587791 !$#accession JX0208 !'##molecule_type DNA !'##residues 1-789 ##label KAW !'##note nucleotide sequence is not complete GENETICS !$#introns 38/3; 77/2; 109/1; 144/1; 159/3; 181/1; 214/1; 248/3; 298/1; !1337/3; 366/3; 388/3; 423/3; 444/3; 511/3; 587/2; 654/2; 685/ !13; 735/3; 758/3; 783/3 CLASSIFICATION #superfamily brush border myosin heavy chain I; myosin motor !1domain homology KEYWORDS actin binding; hydrolase; intestine; nucleotide binding; !1P-loop FEATURE !$11-681 #domain myosin motor domain homology #label MMOT\ !$101-108 #region nucleotide-binding motif A (P-loop)\ !$572-593 #region actin binding #status predicted\ !$723-1043 #domain carboxyl-terminal #label CTD\ !$107 #binding_site ATP (Lys) #status predicted SUMMARY #length 1043 #molecular-weight 118868 #checksum 8238 SEQUENCE /// ENTRY A33620 #type fragment TITLE myosin heavy chain I, brush border - chicken (fragment) CONTAINS myosin ATPase (EC 3.6.4.1) ORGANISM #formal_name Gallus gallus #common_name chicken DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 19-Apr-2002 ACCESSIONS A33620 REFERENCE A33620 !$#authors Garcia, A.; Coudrier, E.; Carboni, J.; Anderson, J.; !1Vandekerkhove, J.; Mooseker, M.; Louvard, D.; Arpin, M. !$#journal J. Cell Biol. (1989) 109:2895-2903 !$#title Partial deduced sequence of the 110-kD-calmodulin complex of !1the avian intestinal microvillus shows that this !1mechanoenzyme is a member of the myosin I family. !$#cross-references MUID:90078325; PMID:2687288 !$#accession A33620 !'##molecule_type mRNA !'##residues 1-1000 ##label GAR !'##cross-references GB:X58479; NID:g63075; PIDN:CAA41388.1; PID:g63076 CLASSIFICATION #superfamily brush border myosin heavy chain I; myosin motor !1domain homology KEYWORDS actin binding; hydrolase; intestine; nucleotide binding; !1P-loop FEATURE !$1-639 #domain myosin motor domain homology #label MMO\ !$59-66 #region nucleotide-binding motif A (P-loop)\ !$530-551 #region actin binding #status predicted\ !$681-1000 #domain carboxyl-terminal #label CTD\ !$65 #binding_site ATP (Lys) #status predicted SUMMARY #length 1000 #checksum 4562 SEQUENCE /// ENTRY JQ0151 #type complete TITLE myosin heavy chain IA - slime mold (Dictyostelium sp.) ALTERNATE_NAMES ambA protein CONTAINS myosin ATPase (EC 3.6.4.1) ORGANISM #formal_name Dictyostelium sp. DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 19-Apr-2002 ACCESSIONS JQ0151 REFERENCE JQ0151 !$#authors Titus, M.A.; Warrick, H.M.; Spudich, J.A. !$#journal Cell Regul. (1989) 1:55-63 !$#title Multiple actin-based motor genes in Dictyostelium. !$#cross-references MUID:92096486; PMID:2519618 !$#accession JQ0151 !'##molecule_type DNA !'##residues 1-994 ##label TIT !'##cross-references GB:S73909; NID:g241267; PIDN:AAB20711.1; !1PID:g241268 !'##experimental_source strain A5-2 GENETICS !$#gene abmA !$#introns 1/2; 42/3 CLASSIFICATION #superfamily brush border myosin heavy chain I; myosin motor !1domain homology KEYWORDS actin binding; hydrolase; nucleotide binding; P-loop FEATURE !$15-706 #domain myosin motor domain homology #label MMOT\ !$105-112 #region nucleotide-binding motif A (P-loop)\ !$594-615 #region actin binding #status predicted\ !$783-994 #domain carboxyl-terminal #label CTD\ !$829-935 #region basic\ !$111 #binding_site ATP (Lys) #status predicted SUMMARY #length 994 #molecular-weight 113286 #checksum 8769 SEQUENCE /// ENTRY A29813 #type complete TITLE 132K ninaC protein - fruit fly (Drosophila melanogaster) CONTAINS protein kinase (EC 2.7.1.-) ORGANISM #formal_name Drosophila melanogaster DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 19-Jan-2001 ACCESSIONS A29813 REFERENCE A90898 !$#authors Montell, C.; Rubin, G.M. !$#journal Cell (1988) 52:757-772 !$#title The Drosophila ninaC locus encodes two photoreceptor cell !1specific proteins with domains homologous to protein kinases !1and the myosin heavy chain head. !$#cross-references MUID:88151067; PMID:2449973 !$#accession A29813 !'##molecule_type mRNA !'##residues 1-1135 ##label MON !'##cross-references GB:M20231; NID:g157965; PIDN:AAA28720.1; !1PID:g157966 GENETICS !$#gene FlyBase:ninaC !'##cross-references FlyBase:FBgn0002938 CLASSIFICATION #superfamily ninaC protein; myosin motor domain homology; !1protein kinase homology KEYWORDS actin binding; alternative splicing; ATP; nucleotide !1binding; P-loop; phosphotransferase; photoreceptor; serine/ !1threonine-specific protein kinase FEATURE !$14-282 #domain protein kinase homology #label KIN\ !$335-1022 #domain myosin motor domain homology #label MMOT\ !$425-432 #region nucleotide-binding motif A (P-loop)\ !$911-936 #region actin binding #status predicted\ !$1054-1135 #domain carboxyl-terminal #label CBT\ !$45,60,145 #active_site Lys, Glu, Asp #status predicted\ !$431 #binding_site ATP (Lys) #status predicted SUMMARY #length 1135 #molecular-weight 131833 #checksum 9470 SEQUENCE /// ENTRY B29813 #type complete TITLE 174K ninaC protein - fruit fly (Drosophila melanogaster) CONTAINS protein kinase (EC 2.7.1.-) ORGANISM #formal_name Drosophila melanogaster DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 19-Jan-2001 ACCESSIONS B29813 REFERENCE A90898 !$#authors Montell, C.; Rubin, G.M. !$#journal Cell (1988) 52:757-772 !$#title The Drosophila ninaC locus encodes two photoreceptor cell !1specific proteins with domains homologous to protein kinases !1and the myosin heavy chain head. !$#cross-references MUID:88151067; PMID:2449973 !$#accession B29813 !'##molecule_type mRNA !'##residues 1-1501 ##label MON !'##cross-references GB:M20230; NID:g157967; PIDN:AAA28721.1; !1PID:g157968 GENETICS !$#gene FlyBase:ninaC !'##cross-references FlyBase:FBgn0002938 CLASSIFICATION #superfamily ninaC protein; myosin motor domain homology; !1protein kinase homology KEYWORDS actin binding; alternative splicing; ATP; nucleotide !1binding; P-loop; phosphotransferase; photoreceptor; serine/ !1threonine-specific protein kinase FEATURE !$14-282 #domain protein kinase homology #label KIN\ !$335-1022 #domain myosin motor domain homology #label MMOT\ !$425-432 #region nucleotide-binding motif A (P-loop)\ !$911-936 #region actin binding #status predicted\ !$1054-1501 #domain carboxyl-terminal #label CBT\ !$45,60,145 #active_site Lys, Glu, Asp #status predicted\ !$431 #binding_site ATP (Lys) #status predicted SUMMARY #length 1501 #molecular-weight 174327 #checksum 959 SEQUENCE /// ENTRY B47734 #type complete TITLE actin-capping protein beta chain - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 29-Oct-1999 ACCESSIONS B47734; S31327; T23741; S31325 REFERENCE A47734 !$#authors Waddle, J.A.; Cooper, J.A.; Waterston, R.H. !$#journal Mol. Biol. Cell (1993) 4:907-917 !$#title The alpha and beta subunits of nematode actin capping !1protein function in yeast. !$#cross-references MUID:94080017; PMID:8257793 !$#accession B47734 !'##status preliminary !'##molecule_type DNA !'##residues 1-270 ##label WAD !'##cross-references GB:Z18806; NID:g6689; PIDN:CAA79270.1; PID:g6690 REFERENCE S31324 !$#authors Waddle, J.A.; Cooper, J.A.; Waterston, R.H. !$#submission submitted to the EMBL Data Library, November 1992 !$#description Analysis of the genes encoding actin-capping protein in C. !1elegans: Complementation of yeast capping protein null !1mutants with the nematode genes. !$#accession S31327 !'##status preliminary !'##molecule_type mRNA !'##residues 1-270 ##label WA2 !'##cross-references EMBL:Z18854; NID:g6691; PIDN:CAA79306.1; PID:g6692 REFERENCE Z19792 !$#authors Palmer, S. !$#submission submitted to the EMBL Data Library, December 1994 !$#accession T23741 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-270 ##label WIL !'##cross-references EMBL:Z46935; PIDN:CAA87051.1; GSPDB:GN00020; !1CESP:M106.5 !'##experimental_source clone M106 GENETICS !$#gene cap-2 !$#map_position 2 !$#introns 1/3; 41/1; 72/2; 110/2; 160/3; 195/3; 237/3 CLASSIFICATION #superfamily actin-capping protein beta chain KEYWORDS actin binding SUMMARY #length 270 #molecular-weight 30785 #checksum 7773 SEQUENCE /// ENTRY A61042 #type complete TITLE Ca2+-independent f-actin-capping protein 32K chain - slime mold (Dictyostelium discoideum) ALTERNATE_NAMES heterodimeric capping protein cap32 ORGANISM #formal_name Dictyostelium discoideum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A61042; A34334; A30945 REFERENCE A61042 !$#authors Hartmann, H.; Schleicher, M.; Noegel, A.A. !$#journal Dev. Genet. (1990) 11:369-376 !$#title Heterodimeric capping proteins constitute a highly conserved !1group of actin-binding proteins. !$#cross-references MUID:91256503; PMID:1710551 !$#accession A61042 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type DNA !'##residues 1-272 ##label HAR REFERENCE A34334 !$#authors Hartmann, H.; Noegel, A.A.; Eckerskorn, C.; Rapp, S.; !1Schleicher, M. !$#journal J. Biol. Chem. (1989) 264:12639-12647 !$#title Ca(2+)-independent F-actin capping proteins. Cap 32/34, a !1capping protein from Dictyostelium discoideum, does not !1share sequence homologies with known actin-binding proteins. !$#cross-references MUID:89308700; PMID:2663863 !$#accession A34334 !'##molecule_type mRNA !'##residues 1-272 ##label HA2 !'##cross-references GB:M25131; NID:g167679; PIDN:AAA33175.1; !1PID:g167680 !'##experimental_source strain AX3 !'##note part of this sequence was confirmed by protein sequencing GENETICS !$#gene cap32 CLASSIFICATION #superfamily actin-capping protein beta chain KEYWORDS actin binding; blocked amino end SUMMARY #length 272 #molecular-weight 30694 #checksum 647 SEQUENCE /// ENTRY S49944 #type complete TITLE actin-capping protein beta chain - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YI9905.14c; protein YIL034c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 12-Nov-1999 ACCESSIONS S49944; S31471; S22847; S32594; B26911 REFERENCE S49931 !$#authors Odell, C.; Bowman, S. !$#submission submitted to the EMBL Data Library, December 1994 !$#accession S49944 !'##molecule_type DNA !'##residues 1-287 ##label ODE !'##cross-references GB:Z47047; EMBL:Z46861; NID:g603997; PID:g763312; !1GSPDB:GN00009; MIPS:YIL034c REFERENCE S31471 !$#authors Cooper, J.A. !$#submission submitted to the EMBL Data Library, October 1991 !$#accession S31471 !'##molecule_type DNA !'##residues 1-287 ##label COO !'##cross-references EMBL:X62630; NID:g3446; PIDN:CAA44497.1; PID:g3447 REFERENCE S22847 !$#authors Amatruda, J.F.; Cannon, J.F.; Tatchell, K.; Hug, C.; Cooper, !1J.A. !$#journal Nature (1990) 344:352-354 !$#title Disruption of the actin cytoskeleton in yeast capping !1protein mutants. !$#cross-references MUID:90190869; PMID:2179733 !$#accession S22847 !'##molecule_type DNA !'##residues 1-139,'Y',141-145,'I',148-287 ##label AMA !'##cross-references EMBL:X62630 REFERENCE S32594 !$#authors Amatruda, J.F.; Cooper, J.A. !$#journal J. Cell Biol. (1992) 117:1067-1076 !$#title Purification, characterization, and immunofluorescence !1localization of Saccharomyces cerevisiae capping protein. !$#cross-references MUID:92250730; PMID:1315784 !$#accession S32594 !'##molecule_type protein !'##residues 148-155 ##label AM2 REFERENCE A93094 !$#authors Cannon, J.F.; Tatchell, K. !$#journal Mol. Cell. Biol. (1987) 7:2653-2663 !$#title Characterization of Saccharomyces cerevisiae genes encoding !1subunits of cyclic AMP-dependent protein kinase. !$#cross-references MUID:88038803; PMID:2823100 !$#accession B26911 !'##molecule_type DNA !'##residues 1-139,'Y',141-145,'I',148-194 ##label CAN !'##cross-references EMBL:M17223 GENETICS !$#gene SGD:CAP2; MIPS:YIL034c !'##cross-references SGD:S0001296; MIPS:YIL034c !$#map_position 9L COMPLEX heterodimer CLASSIFICATION #superfamily actin-capping protein beta chain KEYWORDS actin binding; heterodimer SUMMARY #length 287 #molecular-weight 32629 #checksum 2208 SEQUENCE /// ENTRY ATHU #type complete TITLE actin alpha 1, skeletal muscle - human ORGANISM #formal_name Homo sapiens #common_name man DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 22-Jun-1999 ACCESSIONS A31251; A93468; A02994 REFERENCE A31251 !$#authors Taylor, A.; Erba, H.P.; Muscat, G.E.O.; Kedes, L. !$#journal Genomics (1988) 3:323-336 !$#title Nucleotide sequence and expression of the human skeletal !1alpha-actin gene: evolution of functional regulatory !1domains. !$#cross-references MUID:89212595; PMID:2907503 !$#accession A31251 !'##molecule_type DNA !'##residues 1-377 ##label TAY !'##cross-references GB:M20543; NID:g337745; PIDN:AAA60296.1; !1PID:g337746 REFERENCE A93468 !$#authors Hanauer, A.; Levin, M.; Heilig, R.; Daegelen, D.; Kahn, A.; !1Mandel, J.L. !$#journal Nucleic Acids Res. (1983) 11:3503-3516 !$#title Isolation and characterization of cDNA clones for human !1skeletal muscle alpha actin. !$#cross-references MUID:83220757; PMID:6190133 !$#accession A93468 !'##molecule_type mRNA !'##residues 1-377 ##label HAN !'##cross-references GB:J00068; NID:g178028; PIDN:AAB59376.1; !1PID:g178029 GENETICS !$#gene GDB:ACTA1; ACTA !'##cross-references GDB:120535; OMIM:102610 !$#map_position 1q42.1-1q42.3 !$#introns 43/3; 152/1; 206/1; 270/1; 330/3 CLASSIFICATION #superfamily actin KEYWORDS acetylated amino end; methylated amino acid; muscle !1contraction FEATURE !$3-377 #product actin #status predicted #label MAT\ !$3 #modified_site acetylated amino end (Asp) (in mature !8form) #status predicted\ !$75 #modified_site 3'-methylhistidine (His) #status !8predicted SUMMARY #length 377 #molecular-weight 42051 #checksum 6702 SEQUENCE /// ENTRY ATRB #type complete TITLE actin, skeletal muscle - rabbit ALTERNATE_NAMES F-actin ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 07-May-1999 ACCESSIONS A92182; A14185; S65873; S70610; S44393; A02994 REFERENCE A92182 !$#authors Collins, J.H.; Elzinga, M. !$#journal J. Biol. Chem. (1975) 250:5915-5920 !$#title The primary structure of actin from rabbit skeletal muscle. !1Completion and analysis of the amino acid sequence. !$#cross-references MUID:75211334; PMID:1150665 !$#accession A92182 !'##molecule_type protein !'##residues 1-2,'T',4,'D',6-11,'D',13-73,'W',74-78,80-234,236-308,'T', !1310-375 ##label COL !'##note this is the final paper in a series !'##note this sequence has been revised in references A14185 and A90406 REFERENCE A14185 !$#authors Vandekerckhove, J.; Weber, K. !$#journal Eur. J. Biochem. (1978) 90:451-462 !$#title Actin amino-acid sequences. Comparison of actins from calf !1thymus, bovine brain, and SV40-transformed mouse 3T3 cells !1with rabbit skeletal muscle actin. !$#cross-references MUID:79045349; PMID:213279 !$#accession A14185 !'##molecule_type protein !'##residues 1-18;69-84 ##label VAN REFERENCE A90406 !$#authors Lu, R.C.; Elzinga, M. !$#journal Biochemistry (1977) 16:5801-5806 !$#title Partial amino acid sequence of brain actin and its homology !1with muscle actin. !$#cross-references MUID:78060866; PMID:588555 !$#contents annotation !$#note residue 235 has been added and residue 309 has been revised REFERENCE S65873 !$#authors Vahdat, A.; Miller, C.; Phillips, M.; Muhlrad, A.; Reisler, !1E. !$#journal FEBS Lett. (1995) 365:149-151 !$#title A novel 27/16 kDa form of subtilisin cleaved actin: !1structural and functional consequences of cleavage between !1Ser(234) and Ser(235). !$#cross-references MUID:95300963; PMID:7781768 !$#accession S65873 !'##molecule_type protein !'##residues 235-241 ##label VAH REFERENCE S70610 !$#authors Strzelecka-Golaszewska, H.; Wozniak, A.; Hult, T.; Lindberg, !1U. !$#journal Biochem. J. (1996) 316:713-721 !$#title Effects of the type of divalent cation, Ca2+ or Mg2+, bound !1at the high-affinity site and of the ionic composition of !1the solution on the structure of F-actin. !$#cross-references MUID:96265033; PMID:8670143 !$#accession S70610 !'##molecule_type protein !'##residues 48-54;68-72;235-243 ##label STR !'##experimental_source skeletal muscle REFERENCE S44393 !$#authors Bertrand, R.; Derancourt, J.; Kassab, R. !$#journal FEBS Lett. (1994) 345:113-119 !$#title The covalent maleimidobenzoyl-actin-myosin head complex. !1Cross-linking of the 50 kDa heavy chain region to actin !1subdomain-2. !$#cross-references MUID:94259162; PMID:8200441 !$#accession S44393 !'##molecule_type protein !'##residues 48-64 ##label BER !'##experimental_source skeletal muscle CLASSIFICATION #superfamily actin KEYWORDS acetylated amino end; ATP binding; methylated amino acid; !1muscle contraction FEATURE !$1-375 #product actin #status experimental #label MAT\ !$1 #modified_site acetylated amino end (Asp) #status !8experimental\ !$73 #modified_site 3'-methylhistidine (His) #status !8experimental SUMMARY #length 375 #molecular-weight 41816 #checksum 7663 SEQUENCE /// ENTRY ATRT #type complete TITLE actin, skeletal muscle - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 28-May-1999 ACCESSIONS A93283; A02994 REFERENCE A93283 !$#authors Zakut, R.; Shani, M.; Givol, D.; Neuman, S.; Yaffe, D.; !1Nudel, U. !$#journal Nature (1982) 298:857-859 !$#title Nucleotide sequence of the rat skeletal muscle actin gene. !$#cross-references MUID:82272341; PMID:6287276 !$#accession A93283 !'##molecule_type DNA !'##residues 1-377 ##label ZAK !'##cross-references GB:V01218; GB:J00690; GB:J00692; NID:g55576; !1PIDN:CAA24529.1; PID:g55577 GENETICS !$#introns 43/3; 152/1; 206/1; 270/1; 330/3 CLASSIFICATION #superfamily actin KEYWORDS acetylated amino end; methylated amino acid; muscle !1contraction FEATURE !$3-377 #product actin #status predicted #label MAT\ !$3 #modified_site acetylated amino end (Asp) (in mature !8form) #status predicted\ !$75 #modified_site 3'-methylhistidine (His) #status !8predicted SUMMARY #length 377 #molecular-weight 42051 #checksum 6702 SEQUENCE /// ENTRY A24904 #type complete TITLE actin alpha, skeletal muscle - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 19-Nov-1988 #sequence_revision 11-Apr-1997 #text_change 22-Jun-1999 ACCESSIONS A24904; A25460; C25819 REFERENCE A24904 !$#authors Hu, M.C.T.; Sharp, S.B.; Davidson, N. !$#journal Mol. Cell. Biol. (1986) 6:15-25 !$#title The complete sequence of the mouse skeletal alpha-actin gene !1reveals several conserved and inverted repeat sequences !1outside of the protein-coding region. !$#cross-references MUID:87064281; PMID:3023820 !$#accession A24904 !'##molecule_type DNA !'##residues 1-377 ##label HUM !'##cross-references GB:M12347; NID:g191572; PIDN:AAA37141.1; !1PID:g387081 !'##experimental_source strain BALB/c REFERENCE A25460 !$#authors Leader, D.P.; Gall, I.; Campbell, P.; Frischauf, A.M. !$#journal DNA (1986) 5:235-238 !$#title Isolation and characterization of cDNA clones from mouse !1skeletal muscle actin mRNA. !$#cross-references MUID:86246890; PMID:3013550 !$#accession A25460 !'##molecule_type mRNA !'##residues 1-377 ##label LEA !'##cross-references GB:M12866; NID:g191642; PIDN:AAA37164.1; !1PID:g309088 REFERENCE A25819 !$#authors Alonso, S.; Minty, A.; Bourlet, Y.; Buckingham, M. !$#journal J. Mol. Evol. (1986) 23:11-22 !$#title Comparison of three actin-coding sequences in the mouse; !1evolutionary relationships between the actin genes of !1warm-blooded vertebrates. !$#cross-references MUID:86200234; PMID:3084797 !$#accession C25819 !'##molecule_type mRNA !'##residues 42-377 ##label ALO !'##cross-references EMBL:X03766; NID:g49863; PIDN:CAA27397.1; !1PID:g49864 GENETICS !$#introns 43/3; 152/1; 206/1; 270/1; 330/3 CLASSIFICATION #superfamily actin KEYWORDS acetylated amino end; methylated amino acid; muscle !1contraction; skeletal muscle FEATURE !$3-377 #product actin #status predicted #label MAT\ !$3 #modified_site acetylated amino end (Asp) (in mature !8form) #status predicted\ !$75 #modified_site 3'-methylhistidine (His) #status !8predicted SUMMARY #length 377 #molecular-weight 42051 #checksum 6702 SEQUENCE /// ENTRY ATCH #type complete TITLE actin alpha, skeletal muscle - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 28-May-1999 ACCESSIONS A93432; JH0146; B43616; A91269; A02994 REFERENCE A93432 !$#authors Fornwald, J.A.; Kuncio, G.; Peng, I.; Ordahl, C.P. !$#journal Nucleic Acids Res. (1982) 10:3861-3876 !$#title The complete nucleotide sequence of the chick a-actin gene !1and its evolutionary relationship to the actin gene family. !$#cross-references MUID:82274223; PMID:6287424 !$#accession A93432 !'##molecule_type DNA !'##residues 1-377 ##label FORN !'##cross-references GB:V01507; GB:J00805; GB:K02172; GB:K02257; !1NID:g63028; PIDN:CAA24753.1; PID:g63029 REFERENCE JH0146 !$#authors French, B.A.; Bergsma, D.J.; Schwartz, R.J. !$#journal Gene (1990) 88:173-180 !$#title Analysis of a CR1 (chicken repeat) sequence flanking the 5' !1end of the gene encoding alpha-skeletal actin. !$#cross-references MUID:90269605; PMID:2347492 !$#accession JH0146 !'##molecule_type DNA !'##residues 1-377 ##label FRE REFERENCE A43616 !$#authors Paterson, B.M.; Eldridge, J.D. !$#journal Science (1984) 224:1436-1438 !$#title alpha-Cardiac actin is the major sarcomeric isoform !1expressed in embryonic avian skeletal muscle. !$#cross-references MUID:84223949; PMID:6729461 !$#accession B43616 !'##molecule_type DNA !'##residues 1-43 ##label PAT !'##cross-references GB:J00805 REFERENCE A91269 !$#authors Vandekerckhove, J.; Weber, K. !$#journal FEBS Lett. (1979) 102:219-222 !$#title The amino acid sequence of actin from chicken skeletal !1muscle actin and chicken gizzard smooth muscle actin. !$#cross-references MUID:79213846; PMID:456601 !$#accession A91269 !'##molecule_type protein !'##residues 3-377 ##label VAN GENETICS !$#gene asa !$#introns 43/3; 152/1; 206/1; 270/1; 330/3 CLASSIFICATION #superfamily actin KEYWORDS acetylated amino end; methylated amino acid; muscle !1contraction FEATURE !$3-377 #product actin #status experimental #label MAT\ !$3 #modified_site acetylated amino end (Asp) (in mature !8form) #status predicted\ !$75 #modified_site 3'-methylhistidine (His) #status !8predicted SUMMARY #length 377 #molecular-weight 42051 #checksum 6702 SEQUENCE /// ENTRY ATCHSM #type complete TITLE actin gamma, smooth muscle - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 04-Dec-1986 #sequence_revision 11-Apr-1997 #text_change 22-Jun-1999 ACCESSIONS I51208; B91269; A02995; B93432 REFERENCE I51208 !$#authors Kovacs, A.M.; Zimmer, W.E. !$#journal Cell Motil. Cytoskeleton (1993) 24:67-81 !$#title Molecular cloning and expression of the chicken smooth !1muscle gamma-actin mRNA. !$#cross-references MUID:93306712; PMID:8319268 !$#accession I51208 !'##status preliminary !'##molecule_type mRNA !'##residues 1-376 ##label KOV !'##cross-references GB:S63494; NID:g386590; PIDN:AAB27386.1; !1PID:g386591 REFERENCE A91269 !$#authors Vandekerckhove, J.; Weber, K. !$#journal FEBS Lett. (1979) 102:219-222 !$#title The amino acid sequence of actin from chicken skeletal !1muscle actin and chicken gizzard smooth muscle actin. !$#cross-references MUID:79213846; PMID:456601 !$#accession B91269 !'##molecule_type protein !'##residues 3-19;86-92;292-312;358-360 ##label VAN !'##experimental_source gizzard smooth muscle CLASSIFICATION #superfamily actin KEYWORDS blocked amino end; methylated amino acid; muscle !1contraction; smooth muscle FEATURE !$3-376 #product actin gamma, smooth muscle #status !8experimental #label MAT\ !$3 #modified_site blocked amino end (Glu) (in mature !8form) (probably acetylated) #status experimental\ !$74 #modified_site 3'-methylhistidine (His) #status !8predicted SUMMARY #length 376 #molecular-weight 41876 #checksum 2300 SEQUENCE /// ENTRY ATHUSM #type complete TITLE actin alpha 2, aortic smooth muscle - human ORGANISM #formal_name Homo sapiens #common_name man DATE 13-Aug-1986 #sequence_revision 05-Apr-1995 #text_change 22-Jun-1999 ACCESSIONS A35020; S03286; I54050; A02996 REFERENCE A35020 !$#authors Reddy, S.; Ozgur, K.; Lu, M.; Chang, W.; Mohan, S.R.; Kumar, !1C.C.; Ruley, H.E. !$#journal J. Biol. Chem. (1990) 265:1683-1687 !$#title Structure of the human smooth muscle alpha-actin gene. !1Analysis of a cDNA and 5' upstream region. !$#cross-references MUID:90110236; PMID:2295650 !$#accession A35020 !'##molecule_type mRNA !'##residues 1-377 ##label RED !'##cross-references GB:J05192; NID:g178026; PIDN:AAA51577.1; !1PID:g178027 REFERENCE S03286 !$#authors Kamada, S.; Kakunaga, T. !$#journal Nucleic Acids Res. (1989) 17:1767 !$#title The nucleotide sequence of a human smooth muscle alpha-actin !1(aortic type) cDNA. !$#cross-references MUID:89160338; PMID:2701935 !$#accession S03286 !'##molecule_type mRNA !'##residues 1-233,'S',235-377 ##label KAM1 !'##cross-references EMBL:X13839; NID:g28329; PIDN:CAA32064.1; !1PID:g28330 REFERENCE I54050 !$#authors Kamada, S.; Nakano, Y.; Kakunaga, T. !$#journal Gene (1989) 84:455-462 !$#title Structure of 3'-downstream segment of the human smooth !1muscle (aortic-type) alpha-actin-encoding gene and isolation !1of the specific DNA probe. !$#cross-references MUID:90128290; PMID:2612915 !$#accession I54050 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 331-377 ##label KAM2 !'##cross-references GB:M33216; NID:g338234 REFERENCE A02996 !$#authors Ueyama, H.; Hamada, H.; Battula, N.; Kakunaga, T. !$#journal Mol. Cell. Biol. (1984) 4:1073-1078 !$#title Structure of a human smooth muscle actin gene (aortic type) !1with a unique intron site. !$#cross-references MUID:84245506; PMID:6330528 !$#accession A02996 !'##molecule_type DNA !'##residues 1-233,'S',235-330 ##label UEY !'##cross-references GB:K01747; NID:g178065; PIDN:AAA51586.1; !1PID:g178067 !'##experimental_source human fibroblast cell line chemically !1transformed by 4-nitroquinoline-1-oxide, which causes a !1point mutation changing 312-Ala into 312-Val !'##note the authors translated the codon CAG for residue 265 as Glu !'##note the codon given for residue 234 (TGG) is inconsistent with the !1authors' translation and statement that this sequence is !1identical with the bovine protein sequence GENETICS !$#gene GDB:ACTA2 !'##cross-references GDB:125197; OMIM:102620 !$#map_position 10q22-10q24 !$#introns 43/3; 86/3; 123/3; 152/1; 206/1; 270/1; 330/3 !$#note aortic and enteric smooth muscle actin genes have two more !1intron sites than do the skeletal and cardiac muscle actin !1genes; site 86/3 is unique to the smooth muscle genes, !1whereas 123/3 is common to beta-actin genes CLASSIFICATION #superfamily actin KEYWORDS acetylated amino end; methylated amino acid; muscle !1contraction; smooth muscle FEATURE !$3-377 #product actin alpha 2, aortic smooth muscle #status !8predicted #label MAT\ !$3 #modified_site acetylated amino end (Glu) (in mature !8form) #status predicted\ !$75 #modified_site 3'-methylhistidine (His) #status !8predicted SUMMARY #length 377 #molecular-weight 42108 #checksum 6292 SEQUENCE /// ENTRY ATBOSM #type complete TITLE actin, aortic smooth muscle - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 06-Sep-1996 ACCESSIONS A02997; S13480 REFERENCE A02997 !$#authors Vandekerckhove, J.; Weber, K. !$#journal Differentiation (1979) 14:123-133 !$#title The complete amino acid sequence of actins from bovine !1aorta, bovine heart, bovine fast skeletal muscle, and rabbit !1slow skeletal muscle. A protein-chemical analysis of muscle !1actin differentiation. !$#cross-references MUID:80047657; PMID:499690 !$#accession A02997 !'##molecule_type protein !'##residues 1-375 ##label VAN REFERENCE S13480 !$#authors Zevgolis, V.G.; Sotiroudis, T.G.; Evangelopoulos, A.E. !$#journal Biochim. Biophys. Acta (1991) 1091:222-230 !$#title Phosphorylase kinase from bovine stomach smooth muscle: a Ca !1(2+)-dependent protein kinase associated with an actin-like !1molecule. !$#cross-references MUID:91137633; PMID:1995080 !$#accession S13480 !'##molecule_type protein !'##residues 40-49 ##label ZEV !'##experimental_source stomach !'##note this material appears to be actin of aortic smooth muscle type !1or a related molecule copurifying with the phosphorylase !1kinase fraction CLASSIFICATION #superfamily actin KEYWORDS acetylated amino end; methylated amino acid; muscle !1contraction FEATURE !$1 #modified_site acetylated amino end (Glu) #status !8predicted\ !$73 #modified_site 3'-methylhistidine (His) #status !8experimental SUMMARY #length 375 #molecular-weight 41774 #checksum 7273 SEQUENCE /// ENTRY A22224 #type complete TITLE actin alpha, vascular smooth muscle - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 05-Jun-1987 #sequence_revision 11-Apr-1997 #text_change 22-Jun-1999 ACCESSIONS S02135; A37904; A22224 REFERENCE S02135 !$#authors Min, B.; Strauch, A.R.; Foster, D.N. !$#journal Nucleic Acids Res. (1988) 16:10374 !$#title Nucleotide sequence of a mouse vascular smooth muscle !1alpha-actin cDNA. !$#cross-references MUID:89057488; PMID:3194212 !$#accession S02135 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-377 ##label MIN !'##cross-references EMBL:X13297; NID:g49861; PIDN:CAA31659.1; !1PID:g49862 !'##experimental_source strain C3H, differentiated myocytes REFERENCE A37904 !$#authors Min, B.; Foster, D.N.; Strauch, A.R. !$#journal J. Biol. Chem. (1990) 265:16667-16675 !$#title The 5'-flanking region of the mouse vascular smooth muscle !1alpha-actin gene contains evolutionarily conserved sequence !1motifs within a functional promoter. !$#cross-references MUID:90375543; PMID:2398068 !$#accession A37904 !'##molecule_type DNA !'##residues 1-7 ##label MI2 !'##cross-references GB:M57409; NID:g191546 !'##experimental_source vascular smooth muscle REFERENCE A22224 !$#authors Strauch, A.R.; Rubenstein, P.A. !$#journal J. Biol. Chem. (1984) 259:7224-7229 !$#title Vascular smooth muscle alpha-isoactin biosynthetic !1intermediate in BC3H1 cells. !$#cross-references MUID:84212581; PMID:6725286 !$#accession A22224 !'##molecule_type protein !'##residues 3-20 ##label STR CLASSIFICATION #superfamily actin KEYWORDS acetylated amino end; methylated amino acid; muscle !1contraction; smooth muscle FEATURE !$3-377 #product actin alpha, smooth muscle #status predicted !8#label MAT\ !$3 #modified_site acetylated amino end (Glu) (in mature !8form) #status predicted\ !$75 #modified_site 3'-methylhistidine (His) #status !8predicted SUMMARY #length 377 #molecular-weight 42009 #checksum 6268 SEQUENCE /// ENTRY ATRBSM #type complete TITLE actin alpha, smooth muscle - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 22-Jun-1999 ACCESSIONS JH0636; S23329 REFERENCE JH0636 !$#authors Harris, D.E.; Warshaw, D.M.; Periasamy, M. !$#journal Gene (1992) 112:265-266 !$#title Nucleotide sequences of the rabbit alpha-smooth-muscle and !1beta-non-muscle actin mRNAs. !$#cross-references MUID:92210011; PMID:1555776 !$#accession JH0636 !'##molecule_type mRNA !'##residues 1-377 ##label HAR !'##cross-references GB:X60732; NID:g1700; PIDN:CAA43139.1; PID:g1701 !'##note the sequence was cloned from a cDNA library constructed from !1rabbit uterus CLASSIFICATION #superfamily actin KEYWORDS acetylated amino end; methylated amino acid; muscle !1contraction FEATURE !$3-377 #product actin alpha, smooth muscle #status predicted !8#label MAT\ !$3 #modified_site acetylated amino end (Glu) (in mature !8form) #status predicted\ !$75 #modified_site 3'-methylhistidine (His) #status !8predicted SUMMARY #length 377 #molecular-weight 42009 #checksum 6268 SEQUENCE /// ENTRY A25719 #type complete TITLE actin alpha, aortic smooth muscle - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Jun-1988 #sequence_revision 11-Apr-1997 #text_change 22-Jun-1999 ACCESSIONS A25719 REFERENCE A25719 !$#authors Carroll, S.L.; Bergsma, D.J.; Schwartz, R.J. !$#journal J. Biol. Chem. (1986) 261:8965-8976 !$#title Structure and complete nucleotide sequence of the chicken !1alpha-smooth muscle (aortic) actin gene. An actin gene which !1produces multiple messenger RNAs. !$#cross-references MUID:86250825; PMID:3013870 !$#accession A25719 !'##molecule_type DNA !'##residues 1-377 ##label CAR !'##cross-references GB:M13756; NID:g211204; PIDN:AAB12010.1; !1PID:g211205 !'##experimental_source liver GENETICS !$#gene asma !$#introns 43/3; 86/3; 123/3; 152/1; 206/1; 270/1; 330/3 CLASSIFICATION #superfamily actin KEYWORDS acetylated amino end; methylated amino acid; muscle !1contraction; smooth muscle FEATURE !$3-377 #product actin alpha, smooth muscle #status predicted !8#label MAT\ !$3 #modified_site acetylated amino end (Glu) (in mature !8form) #status predicted\ !$75 #modified_site 3'-methylhistidine (His) #status !8predicted SUMMARY #length 377 #molecular-weight 42009 #checksum 6268 SEQUENCE /// ENTRY ATHUC #type complete TITLE actin, cardiac muscle - human ORGANISM #formal_name Homo sapiens #common_name man DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 16-Jul-1999 ACCESSIONS A02998 REFERENCE A02998 !$#authors Hamada, H.; Petrino, M.G.; Kakunaga, T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:5901-5905 !$#title Molecular structure and evolutionary origin of human cardiac !1muscle actin gene. !$#cross-references MUID:83299896; PMID:6310553 !$#accession A02998 !'##molecule_type DNA !'##residues 1-377 ##label HAM !'##cross-references GB:J00070; GB:J00071; GB:J00072; GB:J00073; !1NID:g178037; PIDN:AAB59619.1; PID:g178039 !'##experimental_source human cardiac muscle COMMENT The first two residues shown are removed after translation. GENETICS !$#gene GDB:ACTC !'##cross-references GDB:118970; OMIM:102540 !$#map_position 15pter-15q14 !$#introns 43/3; 152/1; 206/1; 270/1; 330/3 CLASSIFICATION #superfamily actin KEYWORDS acetylated amino end; cardiac muscle; heart; methylated !1amino acid; muscle contraction FEATURE !$3-377 #product actin, cardiac muscle #status predicted !8#label MAT\ !$3 #modified_site acetylated amino end (Asp) (in mature !8form) #status predicted\ !$75 #modified_site 3'-methylhistidine (His) #status !8predicted SUMMARY #length 377 #molecular-weight 42019 #checksum 6669 SEQUENCE /// ENTRY A23022 #type complete TITLE actin, cardiac muscle - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Jun-1987 #sequence_revision 11-Apr-1997 #text_change 22-Jun-1999 ACCESSIONS A23022 REFERENCE A23022 !$#authors Chang, K.S.; Rothblum, K.N.; Schwartz, R.J. !$#journal Nucleic Acids Res. (1985) 13:1223-1237 !$#cross-references MUID:85215542; PMID:3855241 !$#accession A23022 !'##molecule_type DNA !'##residues 1-377 ##label CHA !'##cross-references EMBL:X02212; NID:g63026; PIDN:CAA26135.1; !1PID:g63027 GENETICS !$#introns 43/3; 152/1; 206/1; 270/1; 330/3 CLASSIFICATION #superfamily actin KEYWORDS acetylated amino end; cardiac muscle; heart; methylated !1amino acid; muscle contraction FEATURE !$3-377 #product actin, cardiac muscle #status predicted !8#label MAT\ !$3 #modified_site acetylated amino end (Asp) (in mature !8form) #status predicted\ !$75 #modified_site 3'-methylhistidine (His) #status !8predicted SUMMARY #length 377 #molecular-weight 42019 #checksum 6669 SEQUENCE /// ENTRY B29686 #type complete TITLE actin alpha, cardiac muscle - western clawed frog ORGANISM #formal_name Xenopus tropicalis #common_name western clawed frog DATE 31-Dec-1988 #sequence_revision 11-Apr-1997 #text_change 11-Apr-1997 ACCESSIONS B29686 REFERENCE A91073 !$#authors Stutz, F.; Spohr, G. !$#journal EMBO J. (1987) 6:1989-1995 !$#title A processed gene coding for a sarcomeric actin in Xenopus !1laevis and Xenopus tropicalis. !$#cross-references MUID:88004409; PMID:3653078 !$#accession B29686 !'##molecule_type DNA !'##residues 1-377 ##label STU !'##experimental_source sarcomere CLASSIFICATION #superfamily actin KEYWORDS acetylated amino end; cardiac muscle; heart; methylated !1amino acid; muscle contraction FEATURE !$3-377 #product actin, cardiac muscle #status predicted !8#label MAT\ !$3 #modified_site acetylated amino end (Asp) (in mature !8form) #status predicted\ !$75 #modified_site 3'-methylhistidine (His) #status !8predicted SUMMARY #length 377 #molecular-weight 42033 #checksum 6687 SEQUENCE /// ENTRY ATHUB #type complete TITLE actin beta - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 22-Jun-1999 ACCESSIONS A25168; A37248; S23707; A37247; I39394; S38782; A02999 REFERENCE A25168 !$#authors Nakajima-Iijima, S.; Hamada, H.; Reddy, P.; Kakunaga, T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:6133-6137 !$#title Molecular structure of the human cytoplasmic beta-actin !1gene: interspecies homology of sequences in the introns. !$#cross-references MUID:85298307; PMID:2994062 !$#accession A25168 !'##molecule_type DNA !'##residues 1-375 ##label NAK !'##cross-references GB:M10277; NID:g177967; PIDN:AAA51567.1; !1PID:g177968 !'##note the authors translated the codon CAG for residue 137 as Glu REFERENCE A37248 !$#authors Ng, S.Y.; Gunning, P.; Eddy, R.; Ponte, P.; Leavitt, J.; !1Shows, T.; Kedes, L. !$#journal Mol. Cell. Biol. (1985) 5:2720-2732 !$#title Evolution of the functional human beta-actin gene and its !1multi-pseudogene family: conservation of noncoding regions !1and chromosomal dispersion of pseudogenes. !$#cross-references MUID:86284634; PMID:3837182 !$#accession A37248 !'##molecule_type mRNA !'##residues 1-375 ##label NGX !'##cross-references EMBL:X00351; DDBJ:J00074; GB:M10278; NID:g28251; !1PIDN:CAA25099.1; PID:g28252 !'##note the human genome contains one functional beta-actin gene and a !1number of processed pseudogenes REFERENCE S23707 !$#authors Ponte, P.; Ng, S.Y.; Engel, J.; Gunning, P.; Kedes, L. !$#journal Nucleic Acids Res. (1984) 12:1687-1696 !$#title Evolutionary conservation in the untranslated regions of !1actin mRNAs: DNA sequence of a human beta-actin cDNA. !$#cross-references MUID:84144061; PMID:6322116 !$#accession S23707 !'##status preliminary !'##molecule_type mRNA !'##residues 1-375 ##label PON !'##cross-references EMBL:X63432; NID:g28335; PIDN:CAA45026.1; !1PID:g28336 REFERENCE A37247 !$#authors Hanukoglu, I.; Tanese, N.; Fuchs, E. !$#journal J. Mol. Biol. (1983) 163:673-678 !$#title Complementary DNA sequence of a human cytoplasmic actin. !1Interspecies divergence of 3' non-coding regions. !$#cross-references MUID:83189093; PMID:6842590 !$#accession A37247 !'##molecule_type mRNA !'##residues 252-375 ##label HAN !'##cross-references EMBL:V00478; NID:g28244; PIDN:CAA23745.1; !1PID:g825616 REFERENCE I39394 !$#authors Gunning, P.; Ponte, P.; Okayama, H.; Engel, J.; Blau, H.; !1Kedes, L. !$#journal Mol. Cell. Biol. (1983) 3:787-795 !$#title Isolation and characterization of full-length cDNA clones !1for human alpha-, beta-, and gamma-actin mRNAs: skeletal but !1not cytoplasmic actins have an amino-terminal cysteine that !1is subsequently removed. !$#cross-references MUID:83244575; PMID:6865942 !$#accession I39394 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-17 ##label GUN !'##cross-references GB:K00790; NID:g178031; PIDN:AAA51578.1; !1PID:g178032 REFERENCE S38782 !$#authors Ohmuri, H. !$#submission submitted to the EMBL Data Library, October 1991 !$#accession S38782 !'##status preliminary !'##molecule_type mRNA !'##residues 1-138,'M',140-294,'D',296-375 ##label OHM !'##cross-references EMBL:X63432; NID:g28335; PIDN:CAA45026.1; !1PID:g28336 COMMENT Vertebrate nonmuscle cells contain two highly conserved !1cytoskeletal actins, beta and gamma, that are major !1components of the microfilaments. GENETICS !$#gene GDB:ACTB !'##cross-references GDB:118964; OMIM:102630 !$#map_position 7p22-7p22 !$#introns 41/3; 121/3; 268/1; 328/3 CLASSIFICATION #superfamily actin KEYWORDS cell motility; cytoskeleton; methylated amino acid; !1microfilament; mitosis; structural protein FEATURE !$2-375 #product actin beta #status predicted #label MAT\ !$73 #modified_site 3'-methylhistidine (His) #status !8predicted SUMMARY #length 375 #molecular-weight 41736 #checksum 7223 SEQUENCE /// ENTRY ATMSB #type complete TITLE actin beta - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 22-Jun-1999 ACCESSIONS A39104; D14185; A25819; S12857; A31900; A02999; A24943 REFERENCE A24943 !$#authors Tokunaga, K.; Taniguchi, H.; Yoda, K.; Shimizu, M.; !1Sakiyama, S. !$#journal Nucleic Acids Res. (1986) 14:2829 !$#title Nucleotide sequence of a full-length cDNA for mouse !1cytoskeletal beta-actin mRNA. !$#cross-references MUID:86176768; PMID:3754329 !$#accession A39104 !'##molecule_type mRNA !'##residues 1-375 ##label TOK !'##cross-references EMBL:X03672; NID:g49865; PIDN:CAA27307.1; !1PID:g49866 REFERENCE A14185 !$#authors Vandekerckhove, J.; Weber, K. !$#journal Eur. J. Biochem. (1978) 90:451-462 !$#title Actin amino-acid sequences. Comparison of actins from calf !1thymus, bovine brain, and SV40-transformed mouse 3T3 cells !1with rabbit skeletal muscle actin. !$#cross-references MUID:79045349; PMID:213279 !$#accession D14185 !'##molecule_type protein !'##residues 2-375 ##label VAN !'##note only peptides that differed in composition from the !1corresponding peptides of rabbit skeletal muscle actin were !1sequenced REFERENCE A25819 !$#authors Alonso, S.; Minty, A.; Bourlet, Y.; Buckingham, M. !$#journal J. Mol. Evol. (1986) 23:11-22 !$#title Comparison of three actin-coding sequences in the mouse; !1evolutionary relationships between the actin genes of !1warm-blooded vertebrates. !$#cross-references MUID:86200234; PMID:3084797 !$#accession A25819 !'##molecule_type mRNA !'##residues 27-37,'S',39-375 ##label ALO !'##cross-references GB:M12481; NID:g191581; PIDN:AAA37144.1; !1PID:g387083 REFERENCE S12857 !$#authors Sadano, H.; Taniguchi, S.; Baba, T. !$#journal FEBS Lett. (1990) 271:23-27 !$#title Newly identified type of beta-actin reduces invasiveness of !1mouse B16-melanoma. !$#cross-references MUID:91032075; PMID:2226807 !$#accession S12857 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 23-27,'L',29-33 ##label SAD REFERENCE A31900 !$#authors Sadano, H.; Taniguchi, S.; Kakunaga, T.; Baba, T. !$#journal J. Biol. Chem. (1988) 263:15868-15871 !$#title cDNA cloning and sequence of a new type of actin in mouse !1B16 melanoma. !$#cross-references MUID:89034035; PMID:3182774 !$#accession A31900 !'##molecule_type mRNA !'##residues 1-27,'L',29-375 ##label SA2 !'##cross-references GB:J04181; NID:g191660; PIDN:AAA37170.1; !1PID:g309090 COMMENT Vertebrate nonmuscle cells contain two highly conserved !1cytoskeletal actins, beta and gamma, that are major !1components of the microfilaments. CLASSIFICATION #superfamily actin KEYWORDS blocked amino end; cell motility; cytoskeleton; methylated !1amino acid; microfilament; mitosis; structural protein FEATURE !$2-375 #product actin beta #status experimental #label MAT\ !$2 #modified_site blocked amino end (Asp) (in mature !8form) (probably acetylated) #status experimental\ !$73 #modified_site 3'-methylhistidine (His) #status !8experimental SUMMARY #length 375 #molecular-weight 41736 #checksum 7223 SEQUENCE /// ENTRY ATRTC #type complete TITLE actin beta - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 22-Jun-1999 ACCESSIONS A38571; A02999 REFERENCE A38571 !$#authors Nudel, U.; Zakut, R.; Shani, M.; Neuman, S.; Levy, Z.; !1Yaffe, D. !$#journal Nucleic Acids Res. (1983) 11:1759-1771 !$#title The nucleotide sequence of the rat cytoplasmic beta-actin !1gene. !$#cross-references MUID:83168920; PMID:6300777 !$#accession A38571 !'##molecule_type DNA !'##residues 1-375 ##label NUD !'##cross-references GB:J00691; NID:g202653; PIDN:AAA40657.1; !1PID:g202654 COMMENT Vertebrate nonmuscle cells contain two highly conserved !1cytoskeletal actins, beta and gamma, that are major !1components of the microfilaments. GENETICS !$#introns 41/3; 121/3; 268/1; 328/3 CLASSIFICATION #superfamily actin KEYWORDS cell motility; cytoskeleton; methylated amino acid; !1microfilament; mitosis; structural protein FEATURE !$2-375 #product actin beta #status predicted #label MAT\ !$73 #modified_site 3'-methylhistidine (His) #status !8predicted SUMMARY #length 375 #molecular-weight 41750 #checksum 7133 SEQUENCE /// ENTRY ATRBB #type complete TITLE actin beta, non-muscle - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 22-Jun-1999 ACCESSIONS JH0637; S23330 REFERENCE JH0636 !$#authors Harris, D.E.; Warshaw, D.M.; Periasamy, M. !$#journal Gene (1992) 112:265-266 !$#title Nucleotide sequences of the rabbit alpha-smooth-muscle and !1beta-non-muscle actin mRNAs. !$#cross-references MUID:92210011; PMID:1555776 !$#accession JH0637 !'##molecule_type mRNA !'##residues 1-375 ##label HAR !'##cross-references GB:X60733; NID:g1702; PIDN:CAA43140.1; PID:g1703 COMMENT Vertebrate nonmuscle cells contain two highly conserved !1cytoskeletal actins, beta and gamma, that are major !1components of the microfilaments. CLASSIFICATION #superfamily actin KEYWORDS acetylated amino end; cell motility; cytoskeleton; !1methylated amino acid; microfilament; mitosis; structural !1protein FEATURE !$2-375 #product actin beta #status predicted #label MAT\ !$2 #modified_site acetylated amino end (Asp) (in mature !8form) #status predicted\ !$73 #modified_site 3'-methylhistidine (His) #status !8predicted SUMMARY #length 375 #molecular-weight 41755 #checksum 7663 SEQUENCE /// ENTRY ATBOB #type complete TITLE actin beta - bovine (tentative sequence) ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 24-Nov-1999 ACCESSIONS E14185; A39105; A02999; A14185 REFERENCE A14185 !$#authors Vandekerckhove, J.; Weber, K. !$#journal Eur. J. Biochem. (1978) 90:451-462 !$#title Actin amino-acid sequences. Comparison of actins from calf !1thymus, bovine brain, and SV40-transformed mouse 3T3 cells !1with rabbit skeletal muscle actin. !$#cross-references MUID:79045349; PMID:213279 !$#accession E14185 !'##molecule_type protein !'##residues 1-374 ##label VAN !'##note only peptides that differed in composition from the !1corresponding peptides of rabbit skeletal muscle actin were !1sequenced REFERENCE A39105 !$#authors Degen, J.L.; Neubauer, M.G.; Degen, S.J.F.; Seyfried, C.E.; !1Morris, D.R. !$#journal J. Biol. Chem. (1983) 258:12153-12162 !$#title Regulation of protein synthesis in mitogen-activated bovine !1lymphocytes. Analysis of actin-specific and total mRNA !1accumulation and utilization. !$#cross-references MUID:84032385; PMID:6195151 !$#accession A39105 !'##molecule_type mRNA !'##residues 76-227;344-374 ##label DEG !'##cross-references GB:K00622; GB:K00623 !'##note actins beta and gamma were not distinguished in this study COMMENT Vertebrate nonmuscle cells contain two highly conserved !1cytoskeletal actins, beta and gamma, that are major !1components of the microfilaments. CLASSIFICATION #superfamily actin KEYWORDS blocked amino end; cell motility; cytoskeleton; methylated !1amino acid; microfilament; mitosis; structural protein FEATURE !$1 #modified_site blocked amino end (Asp) (probably !8acetylated) #status experimental\ !$72 #modified_site 3'-methylhistidine (His) #status !8predicted SUMMARY #length 374 #molecular-weight 41605 #checksum 4120 SEQUENCE /// ENTRY ATCHB #type complete TITLE actin beta - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 22-Jun-1999 ACCESSIONS A20888; I50154 REFERENCE A20888 !$#authors Kost, T.A.; Theodorakis, N.; Hughes, S.H. !$#journal Nucleic Acids Res. (1983) 11:8287-8301 !$#title The nucleotide sequence of the chick cytoplasmic beta-actin !1gene. !$#cross-references MUID:84169478; PMID:6324080 !$#accession A20888 !'##molecule_type DNA !'##residues 1-375 ##label KOS !'##cross-references EMBL:X00182 !'##note the sequence shown follows the authors' translation at position !1336 REFERENCE I50153 !$#authors Chang, K. !$#journal Mol. Cell. Biol. (1984) 4:2498-2508 !$#title Isolation and characterization of six different chicken !1actin genes. !$#cross-references MUID:85085956; PMID:6513927 !$#accession I50154 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-17 ##label CHA !'##cross-references GB:K02259; NID:g211086; PIDN:AAA48572.1; !1PID:g211087 COMMENT Vertebrate nonmuscle cells contain two highly conserved !1cytoskeletal actins, beta and gamma, that are major !1components of the microfilaments. GENETICS !$#introns 41/3; 121/3; 268/1; 328/3 CLASSIFICATION #superfamily actin KEYWORDS acetylated amino end; cell motility; cytoskeleton; !1methylated amino acid; microfilament; mitosis; structural !1protein FEATURE !$2-375 #product actin beta #status predicted #label MAT\ !$2 #modified_site acetylated amino end (Asp) (in mature !8form) #status predicted\ !$73 #modified_site 3'-methylhistidine (His) #status !8predicted SUMMARY #length 375 #molecular-weight 41736 #checksum 7223 SEQUENCE /// ENTRY A48324 #type complete TITLE actin beta, cytoskeletal - common carp ORGANISM #formal_name Cyprinus carpio #common_name common carp DATE 03-Feb-1994 #sequence_revision 11-Apr-1997 #text_change 22-Jun-1999 ACCESSIONS A48324 REFERENCE A48324 !$#authors Liu, Z.; Zhu, Z.; Roberg, K.; Faras, A.; Guise, K.; !1Kapuscinski, A.R.; Hackett, P.B. !$#journal DNA Seq. (1990) 1:125-136 !$#title Isolation and characterization of beta-actin gene of carp !1(Cyprinus carpio). !$#cross-references MUID:92190540; PMID:2134183 !$#accession A48324 !'##molecule_type DNA !'##residues 1-375 ##label LIU !'##cross-references GB:M24113; NID:g213041; PIDN:AAA68886.1; !1PID:g213042 !'##note the authors translated the codon TTC for residue 21 as Pro, AAG !1for residue 50 as Leu, GTT for residue 54 as Tyr, AAG for !1residue 61 as Leu, TTT for residue 124 as Pro, and TTC for !1residue 127 as Pro !'##note the authors failed to translated the codon GGT for residue 42 !1as Gly COMMENT Vertebrate nonmuscle cells contain two highly conserved !1cytoskeletal actins, beta and gamma, that are major !1components of the microfilaments. GENETICS !$#introns 41/3; 121/3; 268/3; 328/3 CLASSIFICATION #superfamily actin KEYWORDS acetylated amino end; cell motility; cytoskeleton; !1methylated amino acid; microfilament; mitosis; structural !1protein FEATURE !$2-375 #product actin beta, cytoskeletal #status predicted !8#label MAT\ !$2 #modified_site acetylated amino end (Asp) (in mature !8form) #status predicted\ !$73 #modified_site 3'-methylhistidine (His) #status !8predicted SUMMARY #length 375 #molecular-weight 41752 #checksum 8181 SEQUENCE /// ENTRY ATURS #type complete TITLE actin CyI - sea urchin (Strongylocentrotus purpuratus) ORGANISM #formal_name Strongylocentrotus purpuratus #common_name purple urchin DATE 18-Aug-1982 #sequence_revision 10-Sep-1982 #text_change 22-Jun-1999 ACCESSIONS A03001; A60829 REFERENCE A03001 !$#authors Cooper, A.D.; Crain Jr., W.R. !$#journal Nucleic Acids Res. (1982) 10:4081-4092 !$#title Complete nucleotide sequence of a sea urchin actin gene. !$#cross-references MUID:82274239; PMID:7111028 !$#accession A03001 !'##molecule_type DNA !'##residues 1-376 ##label COO !'##cross-references GB:J01202; NID:g161433; PIDN:AAA30034.1; !1PID:g161434 REFERENCE A60829 !$#authors Katula, K.S.; Hough-Evans, B.R.; Britten, R.J.; Davidson, !1E.H. !$#journal Development (1987) 101:437-447 !$#title Ontogenic expression of a CyI actin fusion gene injected !1into sea urchin eggs. !$#cross-references MUID:89004610; PMID:3502991 !$#accession A60829 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-14 ##label KAT COMMENT This actin gene is expressed early in embryogenesis. !1Experiments with a fusion protein of this actin to a !1reporter enzyme show high levels of expression by 14 hours !1after fertilization. GENETICS !$#gene CyI !$#introns 122/3; 205/1 CLASSIFICATION #superfamily actin KEYWORDS methylated amino acid FEATURE !$74 #modified_site 3'-methylhistidine (His) #status !8predicted SUMMARY #length 376 #molecular-weight 41830 #checksum 1007 SEQUENCE /// ENTRY ATHUG #type complete TITLE actin gamma 1 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 22-Jun-1999 ACCESSIONS A28098; A23644; A30600; A29861; I39395 REFERENCE A28098 !$#authors Erba, H.P.; Eddy, R.; Shows, T.; Kedes, L.; Gunning, P. !$#journal Mol. Cell. Biol. (1988) 8:1775-1789 !$#title Structure, chromosome location, and expression of the human !1gamma-actin gene: differential evolution, location, and !1expression of the cytoskeletal beta- and gamma-actin genes. !$#cross-references MUID:88246448; PMID:2837653 !$#accession A28098 !'##molecule_type DNA !'##residues 1-375 ##label ERB1 !'##cross-references GB:M19283; NID:g178042; PIDN:AAA51579.1; !1PID:g178043 !'##note the human genome probably contains only one functional !1gamma-actin gene, which is polymorphic in the human !1population; a number of processed pseudogenes were also !1detected REFERENCE A23644 !$#authors Erba, H.P.; Gunning, P.; Kedes, L. !$#journal Nucleic Acids Res. (1986) 14:5275-5294 !$#title Nucleotide sequence of the human gamma cytoskeletal actin !1mRNA: anomalous evolution of vertebrate non-muscle actin !1genes. !$#cross-references MUID:86286543; PMID:3737401 !$#accession A23644 !'##molecule_type mRNA !'##residues 1-375 ##label ERB2 !'##cross-references GB:M24241; NID:g28338; PIDN:CAA27723.1; PID:g28339 REFERENCE A30600 !$#authors Snyder, E.L.; Horne, W.C.; Napychank, P.; Heinemann, F.S.; !1Dunn, B. !$#journal Blood (1989) 73:1380-1385 !$#title Calcium-dependent proteolysis of actin during storage of !1platelet concentrates. !$#cross-references MUID:89194390; PMID:2649176 !$#accession A30600 !'##molecule_type protein !'##residues 106-124 ##label SNY !'##experimental_source platelets !'##note peptides produced by proteolysis during blood bank storage of !1platelets REFERENCE A29861 !$#authors Chou, C.C.; Davis, R.C.; Fuller, M.L.; Slovin, J.P.; Wong, !1A.; Wright, J.; Kania, S.; Shaked, R.; Gatti, R.A.; Salser, !1W.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:2575-2579 !$#title Gamma-actin: unusual mRNA 3'-untranslated sequence !1conservation and amino acid substitutions that may be cancer !1related. !$#cross-references MUID:87204173; PMID:3472224 !$#accession A29861 !'##molecule_type mRNA !'##residues 144-315,'K',317-343,'F',345-375 ##label CHO !'##cross-references GB:M16247; NID:g178044; PIDN:AAA51580.1; !1PID:g178045 !'##note variant sequence isolated from a chemically transformed cell !1line REFERENCE I39394 !$#authors Gunning, P.; Ponte, P.; Okayama, H.; Engel, J.; Blau, H.; !1Kedes, L. !$#journal Mol. Cell. Biol. (1983) 3:787-795 !$#title Isolation and characterization of full-length cDNA clones !1for human alpha-, beta-, and gamma-actin mRNAs: skeletal but !1not cytoplasmic actins have an amino-terminal cysteine that !1is subsequently removed. !$#cross-references MUID:83244575; PMID:6865942 !$#accession I39395 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-17 ##label GUN !'##cross-references GB:K00791; NID:g178046; PIDN:AAA51581.1; !1PID:g178047 COMMENT Vertebrate nonmuscle cells contain two highly conserved !1cytoskeletal actins, beta and gamma. GENETICS !$#gene GDB:ACTG1; ACTG !'##cross-references GDB:120536; OMIM:102560 !$#map_position 17q25-17q25 !$#introns 41/3; 121/3; 268/1; 328/3 FUNCTION !$#description structural component of cytoskeletal microfilaments CLASSIFICATION #superfamily actin KEYWORDS acetylated amino end; cell motility; cytoskeleton; !1methylated amino acid; microfilament; mitosis; structural !1protein FEATURE !$2-375 #product actin gamma #status predicted #label MAT\ !$2 #modified_site acetylated amino end (Glu) (in mature !8form) #status predicted\ !$73 #modified_site 3'-methylhistidine (His) #status !8predicted SUMMARY #length 375 #molecular-weight 41792 #checksum 7102 SEQUENCE /// ENTRY ATMSG #type complete TITLE actin gamma - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 22-Jun-1999 ACCESSIONS A30243; S01833; C14185; A02999 REFERENCE A30243 !$#authors Tokunaga, K.; Takeda, K.; Kamiyama, K.; Kageyama, H.; !1Takenaga, K.; Sakiyama, S. !$#journal Mol. Cell. Biol. (1988) 8:3929-3933 !$#title Isolation of cDNA clones for mouse cytoskeletal gamma-actin !1and differential expression of cytoskeletal actin mRNAs in !1mouse cells. !$#cross-references MUID:89127235; PMID:3221869 !$#accession A30243 !'##molecule_type mRNA !'##residues 1-375 ##label TOK !'##cross-references GB:M21495; NID:g191656; PIDN:AAA37168.1; !1PID:g309089 !'##note 272-Gly was found in one of 7 clones REFERENCE S01833 !$#authors Peter, B.; Man, Y.M.; Begg, C.E.; Gall, I.; Leader, D.P. !$#journal J. Mol. Biol. (1988) 203:665-675 !$#title Mouse cytoskeletal gamma-actin: analysis and implications of !1the structure of cloned cDNA and processed pseudogenes. !$#cross-references MUID:89094834; PMID:3210229 !$#accession S01833 !'##molecule_type mRNA !'##residues 8-375 ##label PET !'##cross-references EMBL:X13055; NID:g51042; PIDN:CAA31455.1; !1PID:g809561 REFERENCE A14185 !$#authors Vandekerckhove, J.; Weber, K. !$#journal Eur. J. Biochem. (1978) 90:451-462 !$#title Actin amino-acid sequences. Comparison of actins from calf !1thymus, bovine brain, and SV40-transformed mouse 3T3 cells !1with rabbit skeletal muscle actin. !$#cross-references MUID:79045349; PMID:213279 !$#accession C14185 !'##molecule_type protein !'##residues 2-375 ##label VAN !'##note only peptides that differed in composition from the !1corresponding peptides of rabbit skeletal muscle actin were !1sequenced COMMENT Vertebrate nonmuscle cells contain two highly conserved !1cytoskeletal actins, beta and gamma, that are major !1components of the microfilaments. CLASSIFICATION #superfamily actin KEYWORDS blocked amino end; cell motility; cytoskeleton; methylated !1amino acid; microfilament; mitosis; structural protein FEATURE !$2-375 #product actin gamma #status experimental #label MAT\ !$2 #modified_site blocked amino end (Glu) (in mature !8form) (probably acetylated) #status experimental\ !$73 #modified_site 3'-methylhistidine (His) #status !8experimental SUMMARY #length 375 #molecular-weight 41792 #checksum 7102 SEQUENCE /// ENTRY S11222 #type complete TITLE actin gamma, cytoskeletal - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 17-Apr-1993 #sequence_revision 11-Apr-1997 #text_change 22-Jun-1999 ACCESSIONS S11222; A35488 REFERENCE S11222 !$#authors Brown, C.W.; McHugh, K.M.; Lessard, J.L. !$#journal Nucleic Acids Res. (1990) 18:5312 !$#title A cDNA sequence encoding cytoskeletal gamma-actin from rat. !$#cross-references MUID:90384863; PMID:2402472 !$#accession S11222 !'##molecule_type mRNA !'##residues 1-375 ##label BRO !'##cross-references EMBL:X52815; NID:g57573; PIDN:CAA36999.1; !1PID:g57574 REFERENCE A35488 !$#authors Akamizu, T.; Saji, M.; Kohn, L.D. !$#journal Biochem. Biophys. Res. Commun. (1990) 170:351-358 !$#title A microsequencing approach to identify proteins which appear !1to interact with thyrotropin in rat FRTL-5 thyroid cells. !$#cross-references MUID:90321251; PMID:2372296 !$#accession A35488 !'##molecule_type protein !'##residues 4-8,'X',10-13,'X',15-16,'X',18-19;228-231 ##label AKA COMMENT Vertebrate nonmuscle cells contain two highly conserved !1cytoskeletal actins, beta and gamma, that are major !1components of the microfilaments. CLASSIFICATION #superfamily actin KEYWORDS acetylated amino end; cell motility; cytoskeleton; !1methylated amino acid; microfilament; mitosis; structural !1protein FEATURE !$2-375 #product actin gamma, cytoskeletal #status predicted !8#label MAT\ !$2 #modified_site blocked amino end (Glu) (in mature !8form) (probably acetylated) #status experimental\ !$73 #modified_site 3'-methylhistidine (His) #status !8predicted SUMMARY #length 375 #molecular-weight 41792 #checksum 7102 SEQUENCE /// ENTRY ATBOG #type complete TITLE actin gamma - bovine (tentative sequence) ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 24-Nov-1999 ACCESSIONS B14185; A02999 REFERENCE A14185 !$#authors Vandekerckhove, J.; Weber, K. !$#journal Eur. J. Biochem. (1978) 90:451-462 !$#title Actin amino-acid sequences. Comparison of actins from calf !1thymus, bovine brain, and SV40-transformed mouse 3T3 cells !1with rabbit skeletal muscle actin. !$#cross-references MUID:79045349; PMID:213279 !$#accession B14185 !'##molecule_type protein !'##residues 1-374 ##label VAN !'##note only peptides that differed in composition from the !1corresponding peptides of rabbit skeletal muscle actin were !1sequenced COMMENT Vertebrate nonmuscle cells contain two highly conserved !1cytoskeletal actins, beta and gamma, that are major !1components of the microfilaments. CLASSIFICATION #superfamily actin KEYWORDS blocked amino end; cell motility; cytoskeleton; methylated !1amino acid; microfilament; mitosis; structural protein FEATURE !$1 #modified_site blocked amino end (Glu) (probably !8acetylated) #status experimental\ !$72 #modified_site 3'-methylhistidine (His) #status !8predicted SUMMARY #length 374 #molecular-weight 41661 #checksum 4009 SEQUENCE /// ENTRY A43552 #type complete TITLE actin gamma, cytoskeletal type 5 - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 01-Dec-1992 #sequence_revision 11-Apr-1997 #text_change 22-Jun-1999 ACCESSIONS A43552 REFERENCE A43552 !$#authors Mohun, T.J.; Garrett, N. !$#journal Development (1987) 101:393-402 !$#title An amphibian cytoskeletal-type actin gene is expressed !1exclusively in muscle tissue. !$#cross-references MUID:88185231; PMID:3446480 !$#accession A43552 !'##molecule_type DNA !'##residues 1-376 ##label MOH !'##cross-references GB:M24769; NID:g341243; PIDN:AAA49638.1; !1PID:g537596 !'##note the authors translated the codon CAA for residue 138 as Gly COMMENT Vertebrate nonmuscle cells contain two highly conserved !1cytoskeletal actins, beta and gamma, that are major !1components of the microfilaments. CLASSIFICATION #superfamily actin KEYWORDS acetylated amino end; cell motility; cytoskeleton; !1methylated amino acid; microfilament; mitosis; structural !1protein FEATURE !$3-376 #product actin gamma, cytoskeletal type 5 #status !8predicted #label MAT\ !$3 #modified_site acetylated amino end (Asp) (in mature !8form) #status predicted\ !$74 #modified_site 3'-methylhistidine (His) #status !8predicted SUMMARY #length 376 #molecular-weight 41850 #checksum 2126 SEQUENCE /// ENTRY ATFF7 #type complete TITLE actin 7 - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 16-Feb-1997 ACCESSIONS A03002 REFERENCE A92894 !$#authors Sanchez, F.; Tobin, S.L.; Rdest, U.; Zulauf, E.; McCarthy, !1B.J. !$#journal J. Mol. Biol. (1983) 163:533-551 !$#title Two Drosophila actin genes in detail. Gene structure, !1protein structure and transcription during development. !$#cross-references MUID:83189087; PMID:6405041 !$#accession A03002 !'##molecule_type DNA !'##residues 1-376 ##label SAN GENETICS !$#gene FlyBase:Act79B !'##cross-references FlyBase:FBgn0000045 !$#introns 309/1 CLASSIFICATION #superfamily actin KEYWORDS methylated amino acid FEATURE !$74 #modified_site 3'-methylhistidine (His) #status !8predicted SUMMARY #length 376 #molecular-weight 41804 #checksum 2781 SEQUENCE /// ENTRY ATFF8 #type complete TITLE actin 8 - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 22-Jun-1999 ACCESSIONS A03003 REFERENCE A92894 !$#authors Sanchez, F.; Tobin, S.L.; Rdest, U.; Zulauf, E.; McCarthy, !1B.J. !$#journal J. Mol. Biol. (1983) 163:533-551 !$#title Two Drosophila actin genes in detail. Gene structure, !1protein structure and transcription during development. !$#cross-references MUID:83189087; PMID:6405041 !$#accession A03003 !'##molecule_type DNA !'##residues 1-376 ##label SAN !'##cross-references GB:M18830; GB:J01065; NID:g156772; PIDN:AAA28321.1; !1PID:g156773 GENETICS !$#gene FlyBase:Act88F !'##cross-references FlyBase:FBgn0000047 !$#introns 309/1 CLASSIFICATION #superfamily actin KEYWORDS methylated amino acid FEATURE !$74 #modified_site 3'-methylhistidine (His) #status !8predicted SUMMARY #length 376 #molecular-weight 41774 #checksum 1938 SEQUENCE /// ENTRY ATFY #type complete TITLE actin - slime mold (Physarum polycephalum) ALTERNATE_NAMES C-actin ORGANISM #formal_name Physarum polycephalum DATE 31-Jul-1979 #sequence_revision 12-Apr-1996 #text_change 24-Nov-1999 ACCESSIONS A29044; S01370; A29903; S21863; A03004 REFERENCE A29044 !$#authors Nader, W.F.; Isenberg, G.; Sauer, H.W. !$#journal Gene (1986) 48:133-144 !$#title Structure of Physarum actin gene locus ardA: a !1nonpalindromic sequence causes inviability of phage lambda !1and recA-independent deletions. !$#cross-references MUID:87163508; PMID:2951301 !$#accession A29044 !'##molecule_type DNA !'##residues 1-376 ##label NAD !'##cross-references GB:M15272; NID:g161211; PIDN:AAA29971.1; !1PID:g161212 REFERENCE S01370 !$#authors Gonzalez-y-Merchand, J.A.; Cox, R.A. !$#journal J. Mol. Biol. (1988) 202:161-168 !$#title Structure and expression of an actin gene of Physarum !1polycephalum. !$#cross-references MUID:89011939; PMID:3172209 !$#accession S01370 !'##molecule_type DNA !'##residues 1-376 ##label GON !'##cross-references EMBL:X07792; NID:g3186; PIDN:CAA30629.1; PID:g3187 REFERENCE A29903 !$#authors Hamelin, M.; Adam, L.; Lemieux, G.; Pallotta, D. !$#journal DNA (1988) 7:317-328 !$#title Expression of the three unlinked isocoding actin genes of !1Physarum polycephalum. !$#cross-references MUID:88296080; PMID:3402310 !$#accession A29903 !'##molecule_type mRNA !'##residues 1-376 ##label HAM !'##cross-references GB:M21500; NID:g161207; PIDN:AAA29969.1; !1PID:g161208 REFERENCE S21863 !$#authors Boudreau, A.; Adam, L.; Pallotta, D. !$#submission submitted to the EMBL Data Library, July 1991 !$#description Nucleotide sequence of the ardB actin from Physarum !1polycephalum. !$#accession S21863 !'##status preliminary !'##molecule_type DNA !'##residues 1-376 ##label BOU !'##cross-references EMBL:X60788; NID:g3190; PIDN:CAA43201.1; PID:g3191 REFERENCE A93203 !$#authors Vandekerckhove, J.; Weber, K. !$#journal Nature (1978) 276:720-721 !$#title The amino acid sequence of Physarum actin. !$#cross-references MUID:79093998; PMID:732876 !$#accession A03004 !'##molecule_type protein !'##residues 2-376 ##label VAN COMMENT This protein is the only actin found in the cytoplasm of the !1plasmodium of Physarum polycephalum, a true slime mold. GENETICS !$#gene ArdA; ardC2 !$#introns 27/1; 94/1; 214/3; 321/3; 365/3 CLASSIFICATION #superfamily actin KEYWORDS blocked amino end; methylated amino acid; phosphoprotein FEATURE !$2 #modified_site blocked amino end (Glu) (in mature !8form) #status experimental\ !$74 #modified_site 3'-methylhistidine (His) #status !8predicted SUMMARY #length 376 #molecular-weight 41799 #checksum 2628 SEQUENCE /// ENTRY ATDO #type complete TITLE actin - slime mold (Dictyostelium discoideum) ORGANISM #formal_name Dictyostelium discoideum DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 20-Feb-1998 ACCESSIONS A93223; A92871; S67999; A03004 REFERENCE A93223 !$#authors Vandekerckhove, J.; Weber, K. !$#journal Nature (1980) 284:475-477 !$#title Vegetative Dictyostelium cells containing 17 actin genes !1express a single major actin. !$#cross-references MUID:80143270; PMID:6892652 !$#accession A93223 !'##molecule_type protein !'##residues 1-375 ##label VAN REFERENCE A92871 !$#authors McKeown, M.; Firtel, R.A. !$#journal J. Mol. Biol. (1981) 151:593-606 !$#title Evidence for sub-families of actin genes in Dictyostelium as !1determined by comparisons of 3' end sequences. !$#cross-references MUID:82122583; PMID:6276562 !$#accession A92871 !'##molecule_type mRNA; DNA !'##residues 288-375 ##label MCK REFERENCE S67999 !$#authors Jungbluth, A.; Eckerskorn, C.; Gerisch, G.; Lottspeich, F.; !1Stocker, S.; Schweiger, A. !$#journal FEBS Lett. (1995) 375:87-90 !$#title Stress-induced tyrosine phosphorylation of actin in !1Dictyostelium cells and localization of the phosphorylation !1site to tyrosine-53 adjacent to the DNase I binding loop. !$#cross-references MUID:96087090; PMID:7498488 !$#accession S67999 !'##molecule_type protein !'##residues 51-61 ##label JUN COMMENT Although Dictyostelium may contain 17 actin genes, only one !1major actin is expressed in vegetative cells. CLASSIFICATION #superfamily actin KEYWORDS methylated amino acid FEATURE !$73 #modified_site 3'-methylhistidine (His) #status !8predicted SUMMARY #length 375 #molecular-weight 41601 #checksum 7490 SEQUENCE /// ENTRY ATAX #type complete TITLE actin - Acanthamoeba castellanii ORGANISM #formal_name Acanthamoeba castellanii DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 22-Jun-1999 ACCESSIONS A92886; A03004 REFERENCE A92886 !$#authors Nellen, W.; Gallwitz, D. !$#journal J. Mol. Biol. (1982) 159:1-18 !$#title Actin genes and actin messenger RNA in Acanthamoeba !1castellanii. Nucleotide sequence of the split actin gene I. !$#cross-references MUID:83033627; PMID:6290670 !$#accession A92886 !'##molecule_type DNA !'##residues 1-375 ##label NEL !'##cross-references GB:V00002; GB:J01016; NID:g5565; PIDN:CAA23399.1; !1PID:g5566 COMMENT There are at least three actin genes in A. castellanii. GENETICS !$#introns 105/3 CLASSIFICATION #superfamily actin KEYWORDS methylated amino acid FEATURE !$73 #modified_site 3'-methylhistidine (His) #status !8predicted SUMMARY #length 375 #molecular-weight 41675 #checksum 8009 SEQUENCE /// ENTRY ATAXE #type complete TITLE actin - Entamoeba histolytica ORGANISM #formal_name Entamoeba histolytica DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 24-Sep-1999 ACCESSIONS A29877; A54526; S33463 REFERENCE A29877 !$#authors Edman, U.; Meza, I.; Agabian, N. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:3024-3028 !$#title Genomic and cDNA actin sequences from a virulent strain of !1Entamoeba histolytica. !$#cross-references MUID:87204260; PMID:2883657 !$#accession A29877 !'##molecule_type mRNA !'##residues 1-376 ##label EDM !'##cross-references GB:M16339; NID:g290647; PIDN:AAA29082.1; !1PID:g158908 !'##experimental_source strain HM1:IMSS REFERENCE A54526 !$#authors Huber, M.; Garfinkel, L.; Gitler, C.; Mirelman, D.; Revel, !1M.; Rozenblatt, S. !$#journal Mol. Biochem. Parasitol. (1987) 24:227-235 !$#title Entamoeba histolytica: cloning and characterization of actin !1cDNA. !$#cross-references MUID:87315198; PMID:2888016 !$#accession A54526 !'##molecule_type mRNA !'##residues 1-376 ##label HUB !'##cross-references GB:M19871; NID:g158915; PIDN:AAA29086.1; !1PID:g158916 !'##experimental_source strain 200-NIH, clone A !'##note this clone represents the most highly expressed of several !1actin genes REFERENCE S33462 !$#authors Brachhaus, I.; Loippe, M.; Lioutas, C.; Tannich, E. !$#submission submitted to the EMBL Data Library, January 1993 !$#description Analysis of gene organization in the protozoan parasite !1Entamoeba histolytica. !$#accession S33463 !'##status preliminary !'##molecule_type DNA !'##residues 1-137 ##label BRA !'##cross-references EMBL:X70852; NID:g312771; PIDN:CAA50205.1; !1PID:g312773 COMMENT This parasitic protozoan causes amoebiasis. Virulent strains !1are characterized by aggressive behavior associated with !1cell motility and actin function. GENETICS !$#note the number of actin genes varies among Entamoeba histolytica !1isolates, with at least four genes present in strains !1200:NIH and Rhaman and at least five in strain HM-1:IMSS CLASSIFICATION #superfamily actin KEYWORDS cell motility; cytoskeleton; methylated amino acid FEATURE !$74 #modified_site 3'-methylhistidine (His) #status !8predicted SUMMARY #length 376 #molecular-weight 42030 #checksum 1497 SEQUENCE /// ENTRY ATBY #type complete TITLE actin - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein F007; protein YFL039c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1980 #sequence_revision 18-Aug-1982 #text_change 21-Jul-2000 ACCESSIONS A03005; A93850; A92831; S56186; S60494; S60497; S50779 REFERENCE A93845 !$#authors Gallwitz, D.; Sures, I. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1980) 77:2546-2550 !$#title Structure of a split yeast gene: complete nucleotide !1sequence of the actin gene in Saccharomyces cerevisiae. !$#cross-references MUID:80234659; PMID:6994099 !$#accession A03005 !'##molecule_type DNA !'##residues 1-375 ##label GAL !'##cross-references GB:V01288; NID:g3325; PIDN:CAA24597.1; PID:g3326 REFERENCE A93850 !$#authors Ng, R.; Abelson, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1980) 77:3912-3916 !$#title Isolation and sequence of the gene for actin in !1Saccharomyces cerevisiae. !$#cross-references MUID:81054682; PMID:7001447 !$#accession A93850 !'##molecule_type DNA !'##residues 1-113,'X',115-116,'X',118,'X',120-177,'L',179-307,'S', !1309-367,'X',369-375 ##label NGR !'##cross-references GB:V01289 REFERENCE A92831 !$#authors Nellen, W.; Donath, C.; Moos, M.; Gallwitz, D. !$#journal J. Mol. Appl. Genet. (1981) 1:239-244 !$#title The nucleotide sequences of the actin genes from !1Saccharomyces carlsbergensis and Saccharomyces cerevisiae !1are identical except for their introns. !$#cross-references MUID:82267660; PMID:6286825 !$#note S. carlsbergensis !$#accession A92831 !'##molecule_type DNA !'##residues 1-375 ##label NEL !'##cross-references EMBL:V01290 REFERENCE S56186 !$#authors Murakami, Y.; Naitou, M.; Hagiwara, H.; Shibata, T.; Ozawa, !1M.; Sasanuma, S.I.; Sasanuma, M.; Tsuchiya, Y.; Soeda, E.; !1Yokoyama, K.; Yamazaki, M.; Tashiro, H.; Eki, T. !$#submission submitted to the EMBL Data Library, May 1995 !$#description Analysis of the nucleotide sequence of chromosome VI from !1Saccaromyces cerevisiae. !$#accession S56186 !'##molecule_type DNA !'##residues 1-375 ##label MUR !'##cross-references EMBL:D50617; NID:g836685; PIDN:BAA21512.1; !1PID:g2262056; GSPDB:GN00006; MIPS:YFL039c REFERENCE S60494 !$#authors Naitou, M.; Kobayashi, M.; Ozawa, M.; Sasanuma, S.I.; !1Hagiwara, H.; Watanabe, K.; Ono, A.; Yamazaki, M.; Tashiro, !1H.; Eki, T.; Murakami, Y. !$#submission submitted to the EMBL Data Library, June 1995 !$#description Sequencing of an 18.8Kb fragment, clone 4121 of yeast !1chromosome VI. !$#accession S60494 !'##molecule_type DNA !'##residues 1-375 ##label NAI !'##cross-references EMBL:D44598; NID:g871933; PIDN:BAA21511.1; !1PID:g2262057 REFERENCE S60495 !$#authors Naitou, M.; Ozawa, M.; Sasanuma, S.I.; Kobayashi, M.; !1Hagiwara, H.; Shibata, T.; Hanaoka, F.; Watanabe, K.; Ono, !1A.; Yamazaki, M.; Tashiro, H.; Eki, T.; Murakami, Y. !$#journal Yeast (1995) 11:1525-1532 !$#title Sequencing of an 18.8 kb fragment from Saccharomyces !1cerevisiae chromosome VI. !$#cross-references MUID:96353435; PMID:8750241 !$#accession S60497 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 16-375 ##label NAW !'##cross-references EMBL:D44598 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1994 REFERENCE S50779 !$#authors Gallwitz, D.; Seidel, R. !$#journal Nucleic Acids Res. (1980) 8:1043-1059 !$#title Molecular cloning of the actin gene from yeast Saccharomyces !1cerevisiae. !$#cross-references MUID:81076663; PMID:7003553 !$#accession S50779 !'##molecule_type DNA !'##residues 5-57 ##label GAW GENETICS !$#gene SGD:ACT1; MIPS:YFL039c !'##cross-references SGD:S0001855; MIPS:YFL039c !$#map_position 6L !$#introns 4/1 CLASSIFICATION #superfamily actin KEYWORDS methylated amino acid FEATURE !$2-375 #product actin #status predicted #label MAT\ !$73 #modified_site 3'-methylhistidine (His) #status !8predicted SUMMARY #length 375 #molecular-weight 41689 #checksum 546 SEQUENCE /// ENTRY JS0702 #type complete TITLE actin - yeast (Saccharomyces bayanus) ORGANISM #formal_name Saccharomyces bayanus DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jun-2000 ACCESSIONS JS0702 REFERENCE JS0702 !$#authors Kaneko, Y.; Takeuchi, M. !$#submission submitted to JIPID, July 1992 !$#accession JS0702 !'##molecule_type DNA !'##residues 1-375 ##label KAN !'##cross-references DDBJ:D12534; NID:g218393; PIDN:BAA02097.1; !1PID:g218394 !'##experimental_source strain B19-3C GENETICS !$#gene ABY1 !$#introns 4/1 CLASSIFICATION #superfamily actin KEYWORDS methylated amino acid; structural protein FEATURE !$2-375 #product actin #status predicted #label MAT\ !$73 #modified_site 3'-methylhistidine (His) #status !8predicted SUMMARY #length 375 #molecular-weight 41689 #checksum 546 SEQUENCE /// ENTRY ATMUM1 #type complete TITLE actin - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 22-Jun-1999 ACCESSIONS JA0066; S68111 REFERENCE JA0066 !$#authors Nairn, C.J.; Winesett, L.; Ferl, R.J. !$#journal Gene (1988) 65:247-257 !$#title Nucleotide sequence of an actin gene from Arabidopsis !1thaliana. !$#cross-references MUID:88313673; PMID:3410320 !$#accession JA0066 !'##molecule_type DNA !'##residues 1-377 ##label NAI !'##cross-references GB:M20016; NID:g166581; PIDN:AAA32727.1; !1PID:g166582 !'##note comparison of the nucleotide sequence of the AAc1 gene with !1other cloned plant actin genes reveals four exons separated !1by three introns conservatively located in all plant actin !1genes REFERENCE S68089 !$#authors McDowell, J.M.; Huang, S.; McKinney, E.C.; An, Y.Q.; !1Meagher, R.B. !$#journal Genetics (1996) 142:587-602 !$#title Structure and evolution of the actin gene family in !1Arabidopsis thaliana. !$#cross-references MUID:96158109; PMID:8852856 !$#accession S68111 !'##status preliminary !'##molecule_type DNA !'##residues 1-377 ##label MCD !'##cross-references EMBL:U39449; NID:g1145692; PIDN:AAA98561.1; !1PID:g1145693 !'##note the authors did not translate the codons for residues 105, 221, !1229, 254, and 264 GENETICS !$#gene AAc1; ACT1 !$#introns 20/3; 152/1; 356/3 CLASSIFICATION #superfamily actin KEYWORDS cytoskeleton; methylated amino acid; structural protein FEATURE !$75 #modified_site 3'-methylhistidine (His) #status !8predicted SUMMARY #length 377 #molecular-weight 41763 #checksum 7181 SEQUENCE /// ENTRY ATRZ1 #type complete TITLE actin 1 - rice ORGANISM #formal_name Oryza sativa #common_name rice DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 23-Mar-2001 ACCESSIONS S10020; S11871; S12474; S12490; PQ0142 REFERENCE S10020 !$#authors Reece, K.S.; McElroy, D.; Wu, R. !$#journal Plant Mol. Biol. (1990) 14:621-624 !$#title Genomic nucleotide sequence of four rice (Oryza sativa) !1actin genes. !$#cross-references MUID:91346651; PMID:2102841 !$#accession S10020 !'##molecule_type DNA !'##residues 1-377 ##label MCE !'##cross-references EMBL:X15865 !'##experimental_source v.IR36 !'##note the authors translated the codon GAG for residue 119 as Leu REFERENCE S11871 !$#authors McElroy, D.; Rothenberg, M.; Wu, R. !$#journal Plant Mol. Biol. (1990) 14:163-171 !$#title Structural characterization of a rice actin gene. !$#cross-references MUID:91329671; PMID:2101689 !$#accession S11871 !'##molecule_type mRNA !'##residues 1-377 ##label MC1 !'##cross-references EMBL:X16280 REFERENCE S12474 !$#authors McElroy, D. !$#submission submitted to the EMBL Data Library, July 1989 !$#accession S12474 !'##molecule_type mRNA !'##residues 1-152,'N',154-177,'P',179-257,'R',259-313,'R',315-367,'D', !1369-377 ##label MC2 !'##cross-references EMBL:X16280; NID:g20321; PIDN:CAA34356.1; !1PID:g20322 !$#accession S12490 !'##molecule_type DNA !'##residues 1-257,'R',259-313,'R',315-377 ##label MC3 !'##cross-references EMBL:X15865; NID:g20323; PIDN:CAA33874.1; !1PID:g295885 REFERENCE PQ0142 !$#authors McElroy, D.; Zhang, W.; Cao, J.; Wu, R. !$#journal Plant Cell (1990) 2:163-171 !$#title Isolation of an efficient actin promoter for use in rice !1transformation. !$#cross-references MUID:92404732; PMID:2136633 !$#accession PQ0142 !'##molecule_type DNA !'##residues 1-7 ##label MC4 !'##cross-references GB:S44221; NID:g256131; PIDN:AAD13837.1; !1PID:g4261543 !'##experimental_source cv. Lemont GENETICS !$#gene Act1 !$#introns 20/3; 152/1; 356/3 CLASSIFICATION #superfamily actin KEYWORDS cytoskeleton; methylated amino acid FEATURE !$75 #modified_site 3'-methylhistidine (His) #status !8predicted SUMMARY #length 377 #molecular-weight 41796 #checksum 6190 SEQUENCE /// ENTRY ATRZ3 #type complete TITLE actin 3 - rice ORGANISM #formal_name Oryza sativa #common_name rice DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 22-Jun-1999 ACCESSIONS S10022 REFERENCE S10020 !$#authors Reece, K.S.; McElroy, D.; Wu, R. !$#journal Plant Mol. Biol. (1990) 14:621-624 !$#title Genomic nucleotide sequence of four rice (Oryza sativa) !1actin genes. !$#cross-references MUID:91346651; PMID:2102841 !$#accession S10022 !'##status translation not shown !'##molecule_type DNA !'##residues 1-376 ##label REE !'##cross-references EMBL:X15862; NID:g20330; PIDN:CAA33871.1; !1PID:g20331 GENETICS !$#introns 20/3; 152/2; 355/3 CLASSIFICATION #superfamily actin KEYWORDS cytoskeleton; methylated amino acid FEATURE !$75 #modified_site 3'-methylhistidine (His) #status !8predicted SUMMARY #length 376 #molecular-weight 41765 #checksum 5497 SEQUENCE /// ENTRY ATRZ2 #type complete TITLE actin 2 - rice ORGANISM #formal_name Oryza sativa #common_name rice DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 22-Jun-1999 ACCESSIONS S10021 REFERENCE S10020 !$#authors Reece, K.S.; McElroy, D.; Wu, R. !$#journal Plant Mol. Biol. (1990) 14:621-624 !$#title Genomic nucleotide sequence of four rice (Oryza sativa) !1actin genes. !$#cross-references MUID:91346651; PMID:2102841 !$#accession S10021 !'##status translation not shown !'##molecule_type DNA !'##residues 1-379 ##label REE !'##cross-references EMBL:X15864; NID:g20328; PIDN:CAA33873.1; !1PID:g20329 GENETICS !$#introns 20/3; 154/2; 359/2 CLASSIFICATION #superfamily actin KEYWORDS cytoskeleton; methylated amino acid FEATURE !$75 #modified_site 3'-methylhistidine (His) #status !8predicted SUMMARY #length 379 #molecular-weight 42003 #checksum 2267 SEQUENCE /// ENTRY ATRZ7 #type complete TITLE actin 7 - rice ORGANISM #formal_name Oryza sativa #common_name rice DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 22-Jun-1999 ACCESSIONS S10023 REFERENCE S10020 !$#authors Reece, K.S.; McElroy, D.; Wu, R. !$#journal Plant Mol. Biol. (1990) 14:621-624 !$#title Genomic nucleotide sequence of four rice (Oryza sativa) !1actin genes. !$#cross-references MUID:91346651; PMID:2102841 !$#accession S10023 !'##status translation not shown !'##molecule_type DNA !'##residues 1-376 ##label REE !'##cross-references EMBL:X15863; NID:g20332; PIDN:CAA33872.1; !1PID:g20333 GENETICS !$#introns 19/3; 153/2; 356/1 CLASSIFICATION #superfamily actin KEYWORDS cytoskeleton; methylated amino acid FEATURE !$76 #modified_site 3'-methylhistidine (His) #status !8predicted SUMMARY #length 376 #molecular-weight 41725 #checksum 2361 SEQUENCE /// ENTRY ATSY3 #type complete TITLE actin - soybean ORGANISM #formal_name Glycine max #common_name soybean DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 15-Oct-1996 ACCESSIONS A03006 REFERENCE A03006 !$#authors Shah, D.M.; Hightower, R.C.; Meagher, R.B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:1022-1026 !$#title Complete nucleotide sequence of a soybean actin gene. !$#accession A03006 !'##molecule_type DNA !'##residues 1-376 ##label SHA !'##note soybean contains a small multigene family of actin-related !1sequences GENETICS !$#introns 20/3; 151/1; 355/3 CLASSIFICATION #superfamily actin KEYWORDS methylated amino acid FEATURE !$75 #modified_site 3'-methylhistidine (His) #status !8predicted SUMMARY #length 376 #molecular-weight 41591 #checksum 5514 SEQUENCE /// ENTRY ATSY1 #type complete TITLE actin 1 - soybean ORGANISM #formal_name Glycine max #common_name soybean DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 15-Oct-1996 ACCESSIONS A03007 REFERENCE A92835 !$#authors Shah, D.M.; Hightower, R.C.; Meagher, R.B. !$#journal J. Mol. Appl. Genet. (1983) 2:111-126 !$#title Genes encoding actin in higher plants: intron positions are !1highly conserved but the coding sequences are not. !$#cross-references MUID:83187987; PMID:6842118 !$#accession A03007 !'##molecule_type DNA !'##residues 1-378 ##label SHA GENETICS !$#introns 20/3; 153/1; 357/3 CLASSIFICATION #superfamily actin KEYWORDS methylated amino acid FEATURE !$76 #modified_site 3'-methylhistidine (His) #status !8predicted SUMMARY #length 378 #molecular-weight 41507 #checksum 468 SEQUENCE /// ENTRY ATZM1 #type complete TITLE actin - maize ORGANISM #formal_name Zea mays #common_name maize DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 15-Oct-1996 ACCESSIONS A03008 REFERENCE A92835 !$#authors Shah, D.M.; Hightower, R.C.; Meagher, R.B. !$#journal J. Mol. Appl. Genet. (1983) 2:111-126 !$#title Genes encoding actin in higher plants: intron positions are !1highly conserved but the coding sequences are not. !$#cross-references MUID:83187987; PMID:6842118 !$#accession A03008 !'##molecule_type DNA !'##residues 1-375 ##label SHA COMMENT This protein is coded by one member of a multigene family. GENETICS !$#introns 19/3; 150/1; 354/3 CLASSIFICATION #superfamily actin KEYWORDS methylated amino acid FEATURE !$74 #modified_site 3'-methylhistidine (His) #status !8predicted SUMMARY #length 375 #molecular-weight 41617 #checksum 4823 SEQUENCE /// ENTRY ATJN #type complete TITLE actin - Phytophthora megasperma f. sp. glycinea ORGANISM #formal_name Phytophthora megasperma f. sp. glycinea #common_name potato pink rot agent DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 22-Jun-1999 ACCESSIONS S14894; S06062 REFERENCE S14894 !$#authors Dudler, R. !$#journal Plant Mol. Biol. (1990) 14:415-422 !$#title The single-copy actin gene of Phytophthora megasperma !1encodes a protein considerably diverged from any other known !1actin. !$#cross-references MUID:91346628; PMID:2102822 !$#accession S14894 !'##molecule_type DNA !'##residues 1-375 ##label DUD !'##cross-references EMBL:X15900; NID:g3180; PIDN:CAA33907.1; PID:g3181 CLASSIFICATION #superfamily actin KEYWORDS cytoskeleton; methylated amino acid; microfilament FEATURE !$73 #modified_site 3'-methylhistidine (His) #status !8predicted SUMMARY #length 375 #molecular-weight 41988 #checksum 7502 SEQUENCE /// ENTRY ATOQ #type complete TITLE actin - Oxytricha fallax ORGANISM #formal_name Oxytricha fallax DATE 05-Apr-1983 #sequence_revision 05-Apr-1983 #text_change 07-Dec-1999 ACCESSIONS A03009 REFERENCE A03009 !$#authors Kaine, B.P.; Spear, B.B. !$#journal Nature (1982) 295:430-432 !$#title Nucleotide sequence of a macronuclear gene for actin in !1Oxytricha fallax. !$#cross-references MUID:82125465; PMID:6799836 !$#accession A03009 !'##molecule_type DNA !'##residues 1-357 ##label KAI !'##note this sequence is translated from macronuclear DNA COMMENT Oxytricha fallax is a ciliated protozoan that can process !1its genome into a collection of transcriptionally active, !1gene-sized segments called the macronuclear DNA. GENETICS !$#genetic_code SGC5 CLASSIFICATION #superfamily actin KEYWORDS cell motility; structural protein FEATURE !$2-357 #product actin #status predicted #label MAT SUMMARY #length 357 #molecular-weight 39890 #checksum 6759 SEQUENCE /// ENTRY FAUTPC #type complete TITLE procyclic acidic repetitive protein precursor (clone pAP3) - Trypanosoma brucei brucei ALTERNATE_NAMES procyclin ORGANISM #formal_name Trypanosoma brucei brucei DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 22-Jun-1999 ACCESSIONS S14896; S06170 REFERENCE S14896 !$#authors Koenig, E.; Delius, H.; Carrington, M.; Williams, R.O.; !1Roditi, I. !$#journal Nucleic Acids Res. (1989) 17:8727-8739 !$#title Duplication and transcription of procyclin genes in !1Trypanosoma brucei. !$#cross-references MUID:90067841; PMID:2573878 !$#accession S14896 !'##molecule_type DNA !'##residues 1-115 ##label KOE !'##cross-references EMBL:X16015; NID:g10512; PIDN:CAA34147.1; !1PID:g10513 GENETICS !$#gene ProA CLASSIFICATION #superfamily procyclic acidic repetitive protein KEYWORDS glycoprotein; tandem repeat FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-115 #product procyclic acidic repetitive protein #status !8predicted #label MAT\ !$63-92 #region 2-residue repeats (E-P)\ !$56 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 115 #molecular-weight 11714 #checksum 1874 SEQUENCE /// ENTRY JH0628 #type complete TITLE caldesmon - human ALTERNATE_NAMES nonmuscle caldesmon; smooth muscle caldesmon CONTAINS h-caldesmon; l-caldesmon ORGANISM #formal_name Homo sapiens #common_name man DATE 17-Aug-1992 #sequence_revision 27-Jun-1994 #text_change 22-Jun-1999 ACCESSIONS JH0628; A41186; B47193; A47193 REFERENCE JH0628 !$#authors Humphrey, M.B.; Herrera-Sosa, H.; Gonzalez, G.; Lee, R.; !1Bryan, J. !$#journal Gene (1992) 112:197-204 !$#title Cloning of cDNAs encoding human caldesmons. !$#cross-references MUID:92209999; PMID:1555769 !$#accession JH0628 !'##molecule_type mRNA !'##residues 1-793 ##label HUM !'##cross-references GB:M83216; NID:g306508; PIDN:AAA58419.1; !1PID:g180195 !'##experimental_source aorta REFERENCE A41186 !$#authors Novy, R.E.; Lin, J.L.C.; Lin, J.J.C. !$#journal J. Biol. Chem. (1991) 266:16917-16924 !$#title Characterization of cDNA clones encoding a human fibroblast !1caldesmon isoform and analysis of caldesmon expression in !1normal and transformed cells. !$#cross-references MUID:91358497; PMID:1885618 !$#accession A41186 !'##molecule_type mRNA !'##residues 1-207,463-529,'M',531-793 ##label NOV !'##cross-references GB:M64110; NID:g179829; PIDN:AAA35636.1; !1PID:g179830 !'##experimental_source fetal lung REFERENCE A47193 !$#authors Hayashi, K.; Yano, H.; Hashida, T.; Takeuchi, R.; Takeda, !1O.; Asada, K.; Takahashi, E.; Kato, I.; Sobue, K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:12122-12126 !$#title Genomic structure of the human caldesmon gene. !$#cross-references MUID:93101679; PMID:1465449 !$#accession B47193 !'##molecule_type DNA !'##residues 74-436 ##label HA2 !'##experimental_source placenta !'##note sequence extracted from NCBI backbone (NCBIN:120706, !1NCBIP:120707) COMMENT Because of its ability to inhibit the ATPase activity of !1actomyosin, caldesmon is thought to play a role in the !1regulation of smooth muscle contraction. COMMENT The binding of caldesmon to F-actin is modulated by calcium !1and calmodulin. COMMENT Two calmodulin molecules can bind to nonoverlapping domains !1of each caldesmon. GENETICS !$#gene GDB:CALD1 !'##cross-references GDB:133717; OMIM:114213 !$#map_position 7q33-7q33 CLASSIFICATION #superfamily caldesmon KEYWORDS actin binding; alternative splicing; calmodulin binding; !1muscle; phosphoprotein; tandem repeat FEATURE !$1-793 #product h-caldesmon #status predicted #label MAT\ !$1-207,463-793 #product l-caldesmon #status predicted #label MA2\ !$257-389 #region 13-residue repeats\ !$638,730,753 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$724,759 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 793 #molecular-weight 93250 #checksum 2305 SEQUENCE /// ENTRY A33430 #type complete TITLE h-caldesmon - chicken ALTERNATE_NAMES caldesmon, smooth muscle; calmodulin- and actin-binding protein ORGANISM #formal_name Gallus gallus #common_name chicken DATE 27-Feb-1990 #sequence_revision 27-Jun-1994 #text_change 22-Jun-1999 ACCESSIONS A33430; A32642; A32445; A41064; A60461; PC2003; PX0022 REFERENCE A33430 !$#authors Hayashi, K.; Kanda, K.; Kimizuka, F.; Kato, I.; Sobue, K. !$#journal Biochem. Biophys. Res. Commun. (1989) 164:503-511 !$#title Primary structure and functional expression of h-caldesmon !1complementary DNA. !$#cross-references MUID:90026426; PMID:2803315 !$#accession A33430 !'##molecule_type mRNA !'##residues 1-771 ##label HAY !'##cross-references GB:M28417; NID:g211895; PIDN:AAA48810.1; !1PID:g211896 !'##experimental_source gizzard !'##note part of this sequence was confirmed by protein sequencing REFERENCE A32642 !$#authors Bryan, J.; Imai, M.; Lee, R.; Moore, P.; Cook, R.G.; Lin, !1W.G. !$#journal J. Biol. Chem. (1989) 264:13873-13879 !$#title Cloning and expression of a smooth muscle caldesmon. !$#cross-references MUID:89340480; PMID:2760048 !$#accession A32642 !'##molecule_type mRNA !'##residues 1-318,334-771 ##label BRY !'##cross-references GB:J04968; NID:g212656; PIDN:AAA49067.1; !1PID:g212657 !'##note the authors translated the codon GAA for residue 743 as Leu !'##note this alternative splice form is a high molecular weight !1caldesmon (h-caldesmon) REFERENCE A32445 !$#authors Hayashi, K.; Yamada, S.; Kanda, K.; Kimizuka, F.; Kato, I.; !1Sobue, K. !$#journal Biochem. Biophys. Res. Commun. (1989) 161:38-45 !$#title 35kDa fragment of h-caldesmon conserves two consensus !1sequences of the tropomyosin-binding domain in troponin T. !$#cross-references MUID:89273666; PMID:2730665 !$#accession A32445 !'##molecule_type mRNA !'##residues 466-771 ##label HA2 !'##cross-references GB:M26684; NID:g211897; PIDN:AAA48811.1; !1PID:g211898 REFERENCE A41064 !$#authors Mak, A.S.; Carpenter, M.; Smillie, L.B.; Wang, J.H. !$#journal J. Biol. Chem. (1991) 266:19971-19975 !$#title Phosphorylation of caldesmon by p34(cdc2) kinase. !1Identification of phosphorylation sites. !$#cross-references MUID:92041815; PMID:1939059 !$#accession A41064 !'##molecule_type protein !'##residues 597-600;678-696;711-721 ##label MAK REFERENCE A60461 !$#authors Wang, C.L.A.; Wang, L.W.C.; Lu, R.C. !$#journal Biochem. Biophys. Res. Commun. (1989) 162:746-752 !$#title Caldesmon has two calmodulin-binding domains. !$#cross-references MUID:89334885; PMID:2757638 !$#accession A60461 !'##molecule_type protein !'##residues 2-17,'X',19-38;466-485 ##label WAN REFERENCE PC2003 !$#authors Haruna, M.; Hayashi, K.; Yano, H.; Takeuchi, O.; Sobue, K. !$#journal Biochem. Biophys. Res. Commun. (1993) 197:145-153 !$#title Common structural and expressional properties of vertebrate !1caldesmon genes. !$#cross-references MUID:94071934; PMID:8250919 !$#accession PC2003 !'##molecule_type DNA !'##residues 74-419 ##label HAR REFERENCE PX0022 !$#authors Takagi, T.; Yazawa, M.; Ueno, T.; Suzuki, S.; Yagi, K. !$#journal J. Biochem. (1989) 106:778-783 !$#title Amino acid sequence studies on cyanogen bromide peptides of !1chicken caldesmon which bind to calmodulin. !$#cross-references MUID:90130380; PMID:2613684 !$#accession PX0022 !'##molecule_type protein !'##residues 462-477,'D',479-563;674-762,'A',763-771 ##label TAK COMMENT This protein plays a vital role in the regulation of smooth !1muscle and nonmuscle actin-myosin interaction. COMMENT The binding of caldesmon to F-actin is modulated by calcium !1and calmodulin. COMMENT Two calmodulin molecules can bind to nonoverlapping domains !1of each caldesmon. CLASSIFICATION #superfamily caldesmon KEYWORDS actin binding; alternative splicing; calmodulin binding; !1cytoskeleton; muscle; phosphoprotein; tandem repeat FEATURE !$1-771 #product h-caldesmon #status predicted #label HMAT\ !$1-318,334-771 #product h-caldesmon, alternative splice form #status !8predicted #label LMAT\ !$266-390 #region 13-residue repeats\ !$511-582 #region tropomyosin binding\ !$622-636 #region tropomyosin binding\ !$597,682,717 #binding_site phosphate (Ser) (covalent) (by cdc2 !8kinase) #status experimental\ !$688,711 #binding_site phosphate (Thr) (covalent) (by cdc2 !8kinase) #status experimental SUMMARY #length 771 #molecular-weight 88746 #checksum 8982 SEQUENCE /// ENTRY A39038 #type complete TITLE l-caldesmon, nonmuscle - chicken ALTERNATE_NAMES caldesmon, nonmuscle ORGANISM #formal_name Gallus gallus #common_name chicken DATE 31-Jul-1991 #sequence_revision 27-Jun-1994 #text_change 22-Jun-1999 ACCESSIONS A39038 REFERENCE A39038 !$#authors Hayashi, K.; Fujio, Y.; Kato, I.; Sobue, K. !$#journal J. Biol. Chem. (1991) 266:355-361 !$#title Structural and functional relationships between h- and !1l-caldesmons. !$#cross-references MUID:91093148; PMID:1824698 !$#accession A39038 !'##molecule_type mRNA !'##residues 1-517 ##label HAY !'##cross-references GB:M60620; GB:M38015; NID:g212242; PIDN:AAA48936.1; !1PID:g212243 !'##experimental_source brain COMMENT The binding of caldesmon to F-actin is modulated by calcium !1and calmodulin. COMMENT Two calmodulin molecules can bind to nonoverlapping domains !1of each caldesmon. CLASSIFICATION #superfamily caldesmon KEYWORDS actin binding; calmodulin binding; phosphoprotein FEATURE !$342,427,462 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$433,456 #binding_site phosphate (Thr) (covalent) #status !8predicted SUMMARY #length 517 #molecular-weight 58859 #checksum 8838 SEQUENCE /// ENTRY A48222 #type complete TITLE dematin 48K chain - human ALTERNATE_NAMES erythrocyte membrane band 49 protein; erythrocyte protein 4.9 ORGANISM #formal_name Homo sapiens #common_name man DATE 26-May-1994 #sequence_revision 27-Jun-1994 #text_change 22-Jun-1999 ACCESSIONS A48222 REFERENCE A48222 !$#authors Rana, A.P.; Ruff, P.; Maalouf, G.J.; Speicher, D.W.; !1Chishti, A.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:6651-6655 !$#title Cloning of human erythroid dematin reveals another member of !1the villin family. !$#cross-references MUID:93342048; PMID:8341682 !$#accession A48222 !'##molecule_type mRNA !'##residues 1-383 ##label RAN !'##cross-references GB:L19713; NID:g347318; PIDN:AAA58438.1; !1PID:g347319 COMMENT Dematin is proposed to play a role in cytoskeletal !1reorganization during erythroblast maturation. COMMENT Phosphorylation of dematin by cAMP-dependent protein kinase !1abolishes its actin-bundling activity. GENETICS !$#gene GDB:EPB49 !'##cross-references GDB:642103; OMIM:125305 !$#map_position 8p21.1-8p21.1 CLASSIFICATION #superfamily dematin; villin headpiece homology KEYWORDS actin binding; blocked amino end; erythrocyte; !1phosphoprotein; trimer FEATURE !$318-383 #domain villin headpiece homology #label VHH\ !$318-383 #region actin binding #status predicted\ !$71,134,226,269,309, !$350,361 #binding_site phosphate (Ser) (covalent) (by casein !8kinase II) #status predicted\ !$87,170 #binding_site phosphate (Ser) (covalent) (by protein !8kinase C) #status predicted\ !$120,133,284,329 #binding_site phosphate (Thr) (covalent) (by protein !8kinase C) #status predicted\ !$211,381 #binding_site phosphate (Ser) (covalent) (by cAMP- !8and cGMP-dependent kinases) #status predicted\ !$267 #binding_site phosphate (Thr) (covalent) (by cAMP- !8and cGMP-dependent kinases) #status predicted SUMMARY #length 383 #molecular-weight 43121 #checksum 6420 SEQUENCE /// ENTRY A27605 #type complete TITLE dystrophin, muscle - human ALTERNATE_NAMES Duchenne muscular dystrophy protein ORGANISM #formal_name Homo sapiens #common_name man DATE 19-Nov-1988 #sequence_revision 27-Jun-1994 #text_change 16-Jun-2000 ACCESSIONS A27605; S07710; A27162; S05291; A40134; S06051; S10346; !1S02243; S02242; S02244; S02109; S23736; S09071; I54186; !1I68509; I68510; I54175; I54166; S03902 REFERENCE A27605 !$#authors Koenig, M.; Monaco, A.P.; Kunkel, L.M. !$#journal Cell (1988) 53:219-228 !$#title The complete sequence of dystrophin predicts a rod-shaped !1cytoskeletal protein. !$#cross-references MUID:88194521; PMID:3282674 !$#accession A27605 !'##molecule_type mRNA !'##residues 1-3685 ##label KOE !'##cross-references GB:M18533; NID:g181856; PIDN:AAA53189.1; !1PID:g181857 REFERENCE S07710 !$#authors Rosenthal, A.; Speer, A.; Billwitz, H.; Cross, G.S.; !1Forrest, S.M.; Davies, K.E. !$#journal Nucleic Acids Res. (1989) 17:5391 !$#title Two human cDNA molecules coding for the Duchenne muscular !1dystrophy (DMD) locus are highly homologous. !$#cross-references MUID:89345106; PMID:2668885 !$#accession S07710 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type mRNA !'##residues 1-132,'P',134-622,'I',624-783,'G',785-1196,'F',1198-1376, !1'N',1378-1468,'Q',1470-1744,'H',1746-1843,'S',1845-2365,'K', !12367-3685 ##label ROS !'##cross-references EMBL:X14298; NID:g30845; PIDN:CAA32479.1; !1PID:g30846 !'##note this sequence was submitted to the EMBL Data Library, February !11989 REFERENCE A90897 !$#authors Koenig, M.; Hoffman, E.P.; Bertelson, C.J.; Monaco, A.P.; !1Feener, C.; Kunkel, L.M. !$#journal Cell (1987) 50:509-517 !$#title Complete cloning of the Duchenne muscular dystrophy (DMD) !1cDNA and preliminary genomic organization of the DMD gene in !1normal and affected individuals. !$#cross-references MUID:87273512; PMID:3607877 !$#accession A27162 !'##molecule_type mRNA !'##residues 1-497 ##label KO2 !'##cross-references GB:M18533 REFERENCE S01263 !$#authors Cross, G.S.; Speer, A.; Rosenthal, A.; Forrest, S.M.; Smith, !1T.J.; Edwards, Y.; Flint, T.; Hill, D.; Davies, K.E. !$#journal EMBO J. (1987) 6:3277-3283 !$#title Deletions of fetal and adult muscle cDNA in Duchenne and !1Becker muscular dystrophy patients. !$#cross-references MUID:88111512; PMID:3428261 !$#accession S05291 !'##molecule_type mRNA !'##residues 404-556,'T',558-610,'K',612-622,'I',624-664,'M',665-783, !1'G',785-1137,'PN' ##label CRO !'##cross-references EMBL:X06178 !'##note 475-Ile and 529-Glu were also found REFERENCE A40134 !$#authors Hoffman, E.P.; Monaco, A.P.; Feener, C.C.; Kunkel, L.M. !$#journal Science (1987) 238:347-350 !$#title Conservation of the Duchenne muscular dystrophy gene in mice !1and humans. !$#cross-references MUID:88018015; PMID:3659917 !$#accession A40134 !'##molecule_type mRNA !'##residues 491-1207 ##label HOF !'##cross-references GB:M18533 REFERENCE S06051 !$#authors Blonden, L.A.J.; den Dunnen, J.T.; van Paassen, H.M.B.; !1Wapenaar, M.C.; Grootscholten, P.M.; Ginjaar, H.B.; Bakker, !1E.; Pearson, P.L.; van Ommen, G.J.B. !$#journal Nucleic Acids Res. (1989) 17:5611-5621 !$#title High resolution deletion breakpoint mapping in the DMD gene !1by whole cosmid hybridization. !$#cross-references MUID:89345155; PMID:2569720 !$#accession S06051 !'##status translation not shown !'##molecule_type DNA !'##residues 2147-2204 ##label BLO !'##cross-references EMBL:X15495; NID:g30829; PIDN:CAA33518.1; !1PID:g1335049 REFERENCE S10346 !$#authors Speer, A.; Billwitz, H.; Huth, A.; Coutelle, C.; England, !1S.; Love, D.; Davies, K.E. !$#submission submitted to the EMBL Data Library, February 1990 !$#accession S10346 !'##molecule_type DNA !'##residues 2438-2480 ##label SPE !'##cross-references EMBL:X51934 REFERENCE S02109 !$#authors Chamberlain, J.S.; Gibbs, R.A.; Ranier, J.E.; Nguyen, P.N.; !1Caskey, C.T. !$#journal Nucleic Acids Res. (1988) 16:11141-11156 !$#title Deletion screening of the Duchenne muscular dystrophy locus !1via multiplex DNA amplification. !$#cross-references MUID:89083552; PMID:3205741 !$#accession S02243 !'##status preliminary; translation not shown !'##molecule_type DNA !'##residues 665-722 ##label CHA !'##cross-references EMBL:X13045; NID:g30825; PIDN:CAA31451.1; !1PID:g1335048 !$#accession S02242 !'##status preliminary; translation not shown !'##molecule_type DNA !'##residues 2098-2146 ##label CH2 !'##cross-references EMBL:X13046; NID:g30827; PIDN:CAA31452.1; !1PID:g809549 !$#accession S02244 !'##status preliminary; translation not shown !'##molecule_type DNA !'##residues 2147-2204 ##label CH3 !'##cross-references EMBL:X13048; NID:g30833; PIDN:CAA31454.1; !1PID:g1335051 !$#accession S02109 !'##status preliminary; translation not shown !'##molecule_type DNA !'##residues 2305-2365,'K' ##label CH4 !'##cross-references EMBL:X13047; NID:g30831; PIDN:CAA31453.1; !1PID:g1335050 REFERENCE S23736 !$#authors Ginjaar, I.H.B.; van Paassen, M.H.M.B.; den Dunnen, J.J.T.; !1van Ommen, G.G.J.B. !$#submission submitted to the EMBL Data Library, March 1992 !$#description Sequence of Duchenne muscular dystrophy gene exon 60, !1located directly 5' of J66 (DXS268). !$#accession S23736 !'##status preliminary !'##molecule_type DNA !'##residues 2980-2995,'K',2997-3028 ##label GIN !'##cross-references EMBL:Z11860 REFERENCE S09071 !$#authors Heilig, R.; Lemaire, C.; Mandel, J.L. !$#journal Nucleic Acids Res. (1987) 15:9129-9142 !$#title A 230kb cosmid walk in the Duchenne muscular dystrophy gene: !1detection of a conserved sequence and of a possible deletion !1prone region. !$#cross-references MUID:88067745; PMID:2825128 !$#accession S09071 !'##molecule_type DNA !'##residues 'SGGHSWTIHCSLIYRLPLTLI';218-277 ##label HEI !'##cross-references EMBL:X06293; EMBL:Y00494 !'##note sequence N-terminal of residue 218 correspond to a putative !1exon REFERENCE I54186 !$#authors Roberts, R.G.; Coffey, A.J.; Bobrow, M.; Bentley, D.R. !$#journal Genomics (1993) 16:536-538 !$#title Exon structure of the human dystrophin gene. !$#cross-references MUID:93300536; PMID:8314593 !$#accession I54186 !'##status nucleic acid sequence not shown; translation not shown; !1translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 984-1411 ##label RE3 !'##cross-references GB:L05642; NID:g181892; PIDN:AAA74506.1; !1PID:g950344 !$#accession I68509 !'##status nucleic acid sequence not shown; translation not shown; !1translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1776-1913 ##label RE2 !'##cross-references GB:L05646; NID:g181896; PIDN:AAA74507.1; !1PID:g950345 !$#accession I68510 !'##status nucleic acid sequence not shown; translation not shown; !1translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 2850-2979 ##label ROB !'##cross-references GB:L05649; NID:g181899; PIDN:AAA74508.1; !1PID:g950346 REFERENCE I54175 !$#authors Roberts, R.G.; Coffey, A.J.; Bobrow, M.; Bentley, D.R. !$#journal Genomics (1992) 13:942-950 !$#title Determination of the exon structure of the distal protion of !1the dystrophin gene by vectorette PCR. !$#cross-references MUID:92372062; PMID:1505985 !$#accession I54175 !'##status nucleic acid sequence not shown; translation not shown; !1translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 2980-3685 ##label RES !'##cross-references GB:M86903; NID:g181881; PIDN:AAA35779.1; !1PID:g457519 REFERENCE I54166 !$#authors Ehrenpreis, J.; Hillers, M.; Junkes, B.; Pfordt, M.; !1Schwinger, E.; Vosberg, H.P. !$#journal Genomics (1991) 10:551-557 !$#title Analysis of a dystrophin gene deletion by amplification of !1mRNA isolated from DMD myotubes cultured in vitro. !$#cross-references MUID:91365360; PMID:1889805 !$#accession I54166 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 2250-2254 ##label RE4 !'##cross-references GB:S54699; NID:g235303; PIDN:AAB19754.1; !1PID:g235304 REFERENCE S03902 !$#authors Feener, C.A.; Koenig, M.; Kunkel, L.M. !$#journal Nature (1989) 338:509-511 !$#title Alternative splicing of human dystrophin mRNA generates !1isoforms at the carboxy terminus. !$#cross-references MUID:89181947; PMID:2648158 !$#accession S03902 !'##molecule_type mRNA !'##residues 'MED',12-32;3377-3408 ##label FEE !'##cross-references EMBL:X15148 COMMENT Dystrophin is proposed to play a role in anchoring the !1cytoskeleton to the plasma membrane. COMMENT Defects in dystrophin are responsible for the Duchenne/ !1Becker muscular dystrophies. GENETICS !$#gene GDB:DMD !'##cross-references GDB:119850; OMIM:310200 !$#map_position Xp21.2-Xp21.2 !$#introns 11/1; 31/3; 62/3; 88/3; 119/3; 177/2; 217/1; 277/3; 320/3; !1383/3; 444/2; 494/3; 534/3; 568/3; 604/3; 664/3; 723/2; 764/ !13; 794/1; 874/3; 935/1; 1816/3; 1862/3; 1913/3; 1974/3; !12890/1; 3028/3; 3055/1; 3075/2; 3096/1; 3121/1; 3188/2; !13217/1; 3269/3; 3325/2; 3362/3; 3408/2; 3421/2; 3443/2; !13465/2; 3518/2; 3599/3; 3641/1; 3672/1; 3682/3 !$#note the list of introns is incomplete CLASSIFICATION #superfamily dystrophin; alpha-actinin actin-binding domain !1homology; spectrin/dystrophin repeat homology; WW repeat !1homology KEYWORDS actin binding; alternative splicing; calmodulin binding; !1cytoskeleton; leucine zipper; membrane-associated protein; !1muscle; muscular dystrophy; structural protein; tandem !1repeat; triple helix FEATURE !$14-233 #domain alpha-actinin actin-binding domain homology !8#label ACT\ !$253-327 #region hinge\ !$338-447 #domain spectrin/dystrophin repeat homology #label !8SP01\ !$448-556 #domain spectrin/dystrophin repeat homology #label !8SP02\ !$558-667 #domain spectrin/dystrophin repeat homology #label !8SP03\ !$668-717 #region hinge\ !$718-828 #domain spectrin/dystrophin repeat homology #label !8SP04\ !$836-934 #domain spectrin/dystrophin repeat homology #label !8SP05\ !$938-1045 #domain spectrin/dystrophin repeat homology #label !8SP06\ !$1047-1154 #domain spectrin/dystrophin repeat homology #label !8SP07\ !$1156-1263 #domain spectrin/dystrophin repeat homology #label !8SP08\ !$1265-1367 #domain spectrin/dystrophin repeat homology #label !8SP09\ !$1372-1477 #domain spectrin/dystrophin repeat homology #label !8SP10\ !$1478-1568 #domain spectrin/dystrophin repeat homology #status !8atypical #label SP11\ !$1570-1676 #domain spectrin/dystrophin repeat homology #label !8SP12\ !$1678-1782 #domain spectrin/dystrophin repeat homology #label !8SP13\ !$1784-1875 #domain spectrin/dystrophin repeat homology #status !8atypical #label SP14\ !$1876-1982 #domain spectrin/dystrophin repeat homology #label !8SP15\ !$1984-2101 #domain spectrin/dystrophin repeat homology #label !8SP16\ !$2103-2208 #domain spectrin/dystrophin repeat homology #label !8SP17\ !$2210-2316 #domain spectrin/dystrophin repeat homology #label !8SP18\ !$2327-2423 #domain spectrin/dystrophin repeat homology #label !8SP19\ !$2424-2470 #region hinge\ !$2471-2577 #domain spectrin/dystrophin repeat homology #label !8SP20\ !$2579-2686 #domain spectrin/dystrophin repeat homology #label !8SP21\ !$2688-2802 #domain spectrin/dystrophin repeat homology #label !8SP22\ !$2804-2931 #domain spectrin/dystrophin repeat homology #label !8SP23\ !$2933-3040 #domain spectrin/dystrophin repeat homology #label !8SP24\ !$3041-3112 #region hinge\ !$3055-3092 #domain WW repeat homology #label WW1\ !$3080-3360 #region cysteine-rich\ !$3506-3527 #region leucine zipper motif\ !$3572-3593 #region leucine zipper motif SUMMARY #length 3685 #molecular-weight 426674 #checksum 7073 SEQUENCE /// ENTRY S02041 #type complete TITLE dystrophin, muscle - chicken ALTERNATE_NAMES duchenne muscular dystrophy protein ORGANISM #formal_name Gallus gallus #common_name chicken DATE 07-Sep-1990 #sequence_revision 27-Jun-1994 #text_change 16-Jul-1999 ACCESSIONS S02041; S02013; S71487 REFERENCE S02041 !$#authors Lemaire, C.; Heilig, R.; Mandel, J.L. !$#journal Nucleic Acids Res. (1988) 16:11815-11816 !$#title Nucleotide sequence of chicken dystrophin cDNA. !$#cross-references MUID:89098331; PMID:3062582 !$#accession S02041 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-3660 ##label LEM !'##cross-references EMBL:X13369; NID:g63369; PIDN:CAA31746.1; !1PID:g63370 !'##note 1869-His, 1885-Arg, and sequences lacking 1171-Met were also !1found REFERENCE S02013 !$#authors Lemaire, C.; Heilig, R.; Mandel, J.L. !$#journal EMBO J. (1988) 7:4157-4162 !$#title The chicken dystrophin cDNA: striking conservation of the !1C-terminal coding and 3' untranslated regions between man !1and chicken. !$#cross-references MUID:89210800; PMID:3072195 !$#accession S02013 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-3573,'HA',3576-3660 ##label LEM2 REFERENCE S09071 !$#authors Heilig, R.; Lemaire, C.; Mandel, J.L. !$#journal Nucleic Acids Res. (1987) 15:9129-9142 !$#title A 230kb cosmid walk in the Duchenne muscular dystrophy gene: !1detection of a conserved sequence and of a possible deletion !1prone region. !$#cross-references MUID:88067745; PMID:2825128 !$#accession S71487 !'##molecule_type DNA !'##residues 222-281 ##label HEI COMMENT Dystrophin is proposed to play a role in anchoring the !1cytoskeleton to the plasma membrane. COMMENT Defects in dystrophin are responsible for the Duchenne/ !1Becker muscular dystrophies. CLASSIFICATION #superfamily dystrophin; alpha-actinin actin-binding domain !1homology; spectrin/dystrophin repeat homology; WW repeat !1homology KEYWORDS actin binding; calmodulin binding; cytoskeleton; leucine !1zipper; membrane-associated protein; muscle; structural !1protein; tandem repeat; triple helix FEATURE !$18-237 #domain alpha-actinin actin-binding domain homology !8#label ACT\ !$253-327 #region hinge\ !$340-449 #domain spectrin/dystrophin repeat homology #label !8SP01\ !$450-558 #domain spectrin/dystrophin repeat homology #label !8SP02\ !$560-669 #domain spectrin/dystrophin repeat homology #label !8SP03\ !$670-719 #region hinge\ !$720-830 #domain spectrin/dystrophin repeat homology #label !8SP04\ !$838-936 #domain spectrin/dystrophin repeat homology #label !8SP05\ !$940-1047 #domain spectrin/dystrophin repeat homology #label !8SP06\ !$1049-1156 #domain spectrin/dystrophin repeat homology #label !8SP07\ !$1158-1265 #domain spectrin/dystrophin repeat homology #label !8SP08\ !$1267-1369 #domain spectrin/dystrophin repeat homology #label !8SP09\ !$1374-1479 #domain spectrin/dystrophin repeat homology #label !8SP10\ !$1480-1570 #domain spectrin/dystrophin repeat homology #status !8atypical #label SP11\ !$1572-1678 #domain spectrin/dystrophin repeat homology #label !8SP12\ !$1680-1784 #domain spectrin/dystrophin repeat homology #label !8SP13\ !$1787-1877 #domain spectrin/dystrophin repeat homology #status !8atypical #label SP14\ !$1878-1984 #domain spectrin/dystrophin repeat homology #label !8SP15\ !$1986-2103 #domain spectrin/dystrophin repeat homology #label !8SP16\ !$2105-2211 #domain spectrin/dystrophin repeat homology #label !8SP17\ !$2213-2319 #domain spectrin/dystrophin repeat homology #label !8SP18\ !$2323-2419 #domain spectrin/dystrophin repeat homology #label !8SP19\ !$2420-2467 #region hinge\ !$2468-2574 #domain spectrin/dystrophin repeat homology #label !8SP20\ !$2576-2683 #domain spectrin/dystrophin repeat homology #label !8SP21\ !$2685-2799 #domain spectrin/dystrophin repeat homology #label !8SP22\ !$2801-2928 #domain spectrin/dystrophin repeat homology #label !8SP23\ !$2930-3037 #domain spectrin/dystrophin repeat homology #label !8SP24\ !$3038-3075 #region hinge\ !$3052-3089 #domain WW repeat homology #label WW1\ !$3079-3357 #region cysteine-rich\ !$3481-3502 #region leucine zipper motif\ !$3547-3568 #region leucine zipper motif SUMMARY #length 3660 #molecular-weight 422878 #checksum 959 SEQUENCE /// ENTRY S28381 #type complete TITLE utrophin - human ALTERNATE_NAMES dystrophin-related protein ORGANISM #formal_name Homo sapiens #common_name man DATE 17-Apr-1993 #sequence_revision 03-Oct-1995 #text_change 16-Jul-1999 ACCESSIONS S28381; S28914; S03966 REFERENCE S28381 !$#authors Tinsley, J.M. !$#submission submitted to the EMBL Data Library, November 1992 !$#accession S28381 !'##molecule_type mRNA !'##residues 1-3433 ##label TIN1 !'##cross-references EMBL:X69086; NID:g34811; PIDN:CAA48829.1; !1PID:g34812 REFERENCE S28914 !$#authors Tinsley, J.M.; Blake, D.J.; Roche, A.; Fairbrother, U.; !1Riss, J.; Byth, B.C.; Knight, A.E.; Kendrick-Jones, J.; !1Suthers, G.K.; Love, D.R.; Edwards, Y.H.; Davies, K.E. !$#journal Nature (1992) 360:591-593 !$#title Primary structure of dystrophin-related protein. !$#cross-references MUID:93096045; PMID:1461283 !$#accession S28914 !'##molecule_type mRNA !'##residues 27-246;2839-3343 ##label TIN2 !'##cross-references EMBL:X69086 REFERENCE S03966 !$#authors Love, D.R.; Hill, D.F.; Dickson, G.; Spurr, N.K.; Byth, !1B.C.; Marsden, R.F.; Walsh, F.S.; Edwards, Y.H.; Davies, !1K.E. !$#journal Nature (1989) 339:55-58 !$#title An autosomal transcript in skeletal muscle with homology to !1dystrophin. !$#cross-references MUID:89238543; PMID:2541343 !$#accession S03966 !'##molecule_type mRNA !'##residues 2944-3433 ##label LOV !'##cross-references EMBL:X15488; NID:g30933; PIDN:CAA33515.1; !1PID:g930062 COMMENT This protein is found primarily at the neuromuscular !1junctions in adult muscle. In patients with Duchenne !1muscular dystrophy, it is also found in the sarcolemma. It !1also occurs in fetal and regenerating muscle. GENETICS !$#gene GDB:UTRN; DMDL !'##cross-references GDB:119851; OMIM:128240 !$#map_position 6q24-6q24 CLASSIFICATION #superfamily dystrophin; alpha-actinin actin-binding domain !1homology; spectrin/dystrophin repeat homology; WW repeat !1homology KEYWORDS actin binding; cytoskeleton; leucine zipper; !1membrane-associated protein; muscle; neuromuscular junction; !1structural protein; tandem repeat; triple helix FEATURE !$30-248 #domain alpha-actinin actin-binding domain homology !8#label ACT\ !$308-417 #domain spectrin/dystrophin repeat homology #label !8SP01\ !$418-526 #domain spectrin/dystrophin repeat homology #label !8SP02\ !$528-637 #domain spectrin/dystrophin repeat homology #label !8SP03\ !$638-685 #region hinge\ !$686-796 #domain spectrin/dystrophin repeat homology #label !8SP04\ !$804-902 #domain spectrin/dystrophin repeat homology #label !8SP05\ !$906-1013 #domain spectrin/dystrophin repeat homology #label !8SP06\ !$1015-1122 #domain spectrin/dystrophin repeat homology #label !8SP07\ !$1124-1230 #domain spectrin/dystrophin repeat homology #label !8SP08\ !$1232-1334 #domain spectrin/dystrophin repeat homology #label !8SP09\ !$1339-1450 #domain spectrin/dystrophin repeat homology #label !8SP10\ !$1451-1541 #domain spectrin/dystrophin repeat homology #status !8atypical #label SP11\ !$1543-1649 #domain spectrin/dystrophin repeat homology #label !8SP12\ !$1651-1755 #domain spectrin/dystrophin repeat homology #label !8SP13\ !$1856-1973 #domain spectrin/dystrophin repeat homology #label !8SP14\ !$1975-2081 #domain spectrin/dystrophin repeat homology #label !8SP15\ !$2083-2185 #domain spectrin/dystrophin repeat homology #label !8SP16\ !$2227-2333 #domain spectrin/dystrophin repeat homology #label !8SP17\ !$2335-2440 #domain spectrin/dystrophin repeat homology #label !8SP18\ !$2442-2556 #domain spectrin/dystrophin repeat homology #label !8SP19\ !$2558-2688 #domain spectrin/dystrophin repeat homology #label !8SP20\ !$2690-2797 #domain spectrin/dystrophin repeat homology #label !8SP21\ !$2798-2869 #region hinge\ !$2812-2849 #domain WW repeat homology #label WW1\ !$2837-3117 #region cysteine-rich\ !$3263-3284 #region leucine zipper motif\ !$3328-3349 #region leucine zipper motif SUMMARY #length 3433 #molecular-weight 394491 #checksum 1548 SEQUENCE /// ENTRY A28622 #type complete TITLE profilin [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 17-Oct-1988 #sequence_revision 05-Aug-1994 #text_change 08-Dec-2000 ACCESSIONS A28622; S00307 REFERENCE A28622 !$#authors Kwiatkowski, D.J.; Bruns, G.A.P. !$#journal J. Biol. Chem. (1988) 263:5910-5915 !$#title Human profilin. Molecular cloning, sequence comparison, and !1chromosomal analysis. !$#cross-references MUID:88186915; PMID:3356709 !$#accession A28622 !'##molecule_type mRNA !'##residues 1-140 ##label KWI !'##cross-references GB:J03191; NID:g190385; PIDN:AAA36486.1; !1PID:g190386 REFERENCE S00307 !$#authors Ampe, C.; Markey, F.; Lindberg, U.; Vandekerckhove, J. !$#journal FEBS Lett. (1988) 228:17-21 !$#title The primary structure of human platelet profilin: !1reinvestigation of the calf spleen profilin sequence. !$#cross-references MUID:88137589; PMID:3342873 !$#accession S00307 !'##molecule_type protein !'##residues 2-140 ##label AMP COMMENT Profilin, which prevents the polymerization of actin, occurs !1in many kinds of cells as a complex with monomeric actin in !1a 1:1 ratio. GENETICS !$#gene GDB:PFN1 !'##cross-references GDB:120278; OMIM:176610 !$#map_position 17p13.3-17p13.3 CLASSIFICATION #superfamily profilin KEYWORDS actin binding; blocked amino end FEATURE !$2-140 #product profilin #status experimental #label MAT\ !$2 #modified_site blocked amino end (Ala) (in mature !8form) (probably acetylated) #status experimental SUMMARY #length 140 #molecular-weight 15054 #checksum 2551 SEQUENCE /// ENTRY FABO #type complete TITLE profilin - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Jul-1979 #sequence_revision 05-Aug-1994 #text_change 26-Feb-1999 ACCESSIONS S00308; A03010 REFERENCE S00307 !$#authors Ampe, C.; Markey, F.; Lindberg, U.; Vandekerckhove, J. !$#journal FEBS Lett. (1988) 228:17-21 !$#title The primary structure of human platelet profilin: !1reinvestigation of the calf spleen profilin sequence. !$#cross-references MUID:88137589; PMID:3342873 !$#accession S00308 !'##molecule_type protein !'##residues 1-139 ##label AMP !'##note this is a revision to the sequence from reference A03010 REFERENCE A03010 !$#authors Nystrom, L.E.; Lindberg, U.; Kendrick-Jones, J.; Jakes, R. !$#journal FEBS Lett. (1979) 101:161-165 !$#title The amino acid sequence of profilin from calf spleen. !$#cross-references MUID:79191816; PMID:446730 !$#accession A03010 !'##molecule_type protein !'##residues 1-12,'N',14-67,'E',69-112,'NGE',113-115,'Q',117-128,'Q', !1130-139 ##label NYS !'##experimental_source calf spleen REFERENCE A38914 !$#authors Schutt, C.E.; Myslik, J.C.; Rozycki, M.D.; Goonesekere, !1N.C.W.; Lindberg, U. !$#journal Nature (1993) 365:810-816 !$#title The structure of crystalline profilin-beta-actin. !$#cross-references MUID:94019858; PMID:8413665 !$#contents annotation; X-ray crystallography; 2.5 angstroms !$#note the structure of extensive contacts between profilin and !1actin are described COMMENT Profilin, which prevents the polymerization of actin, occurs !1in many kinds of cells as a complex with monomeric actin in !1a 1:1 ratio. CLASSIFICATION #superfamily profilin KEYWORDS acetylated amino end; actin binding FEATURE !$1 #modified_site acetylated amino end (Ala) #status !8experimental SUMMARY #length 139 #molecular-weight 14926 #checksum 9353 SEQUENCE /// ENTRY S04067 #type complete TITLE profilin - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 28-Feb-1990 #sequence_revision 22-Jul-1994 #text_change 22-Jun-1999 ACCESSIONS S04067 REFERENCE S04067 !$#authors Sri Widada, J.; Ferraz, C.; Liautard, J.P. !$#journal Nucleic Acids Res. (1989) 17:2855 !$#title Total coding sequence of profilin cDNA from Mus musculus !1macrophage. !$#cross-references MUID:89240043; PMID:2717414 !$#accession S04067 !'##molecule_type mRNA !'##residues 1-140 ##label SRI !'##cross-references EMBL:X14425; NID:g53781; PIDN:CAA32586.1; !1PID:g53782 COMMENT Profilin, which prevents the polymerization of actin, occurs !1in many kinds of cells as a complex with monomeric actin in !1a 1:1 ratio. CLASSIFICATION #superfamily profilin KEYWORDS acetylated amino end; actin binding FEATURE !$2-140 #product profilin #status predicted #label MAT\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status predicted SUMMARY #length 140 #molecular-weight 14957 #checksum 2728 SEQUENCE /// ENTRY FAVZVR #type complete TITLE profilin homolog - vaccinia virus ALTERNATE_NAMES A42R protein; SalF4R protein ORGANISM #formal_name vaccinia virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jun-2000 ACCESSIONS B40897; JQ1779; H42521 REFERENCE A40897 !$#authors Blasco, R.; Cole, N.B.; Moss, B. !$#journal J. Virol. (1991) 65:4598-4608 !$#title Sequence analysis, expression, and deletion of a vaccinia !1virus gene encoding a homolog of profilin, a eukaryotic !1actin-binding protein. !$#cross-references MUID:91332999; PMID:1870190 !$#accession B40897 !'##molecule_type DNA !'##residues 1-133 ##label BLA !'##cross-references GB:M72474; NID:g335761; PIDN:AAA48308.1; !1PID:g335763 !'##experimental_source strain WR REFERENCE JQ1767 !$#authors Smith, G.L.; Chan, Y.S.; Howard, S.T. !$#journal J. Gen. Virol. (1991) 72:1349-1376 !$#title Nucleotide sequence of 42kbp of vaccinia virus strain WR !1from near the right inverted terminal repeat. !$#cross-references MUID:91259063; PMID:2045793 !$#accession JQ1779 !'##molecule_type DNA !'##residues 1-133 ##label SMI !'##cross-references DDBJ:D11079; NID:g222717; PIDN:BAA01815.1; !1PID:g222730 !'##experimental_source strain WR REFERENCE A33172 !$#authors Johnson, G.P. !$#submission submitted to GenBank, June 1990 !$#accession H42521 !'##molecule_type DNA !'##residues 1-133 ##label JOH !'##experimental_source strain Copenhagen COMMENT Profilin is an actin-binding protein. CLASSIFICATION #superfamily profilin KEYWORDS actin binding; late protein SUMMARY #length 133 #molecular-weight 15052 #checksum 7774 SEQUENCE /// ENTRY FAAX2 #type complete TITLE profilin II - Acanthamoeba castellanii ORGANISM #formal_name Acanthamoeba castellanii DATE 31-Mar-1992 #sequence_revision 22-Jul-1994 #text_change 22-Jun-1999 ACCESSIONS A48405; S00282 REFERENCE A48405 !$#authors Pollard, T.D.; Rimm, D.L. !$#journal Cell Motil. Cytoskeleton (1991) 20:169-177 !$#title Analysis of cDNA clones for Acanthamoeba profilin-I and !1profilin-II shows end to end homology with vertebrate !1profilins and a small family of profilin genes. !$#cross-references MUID:92089911; PMID:1751969 !$#accession A48405 !'##molecule_type mRNA !'##residues 1-126 ##label POL !'##cross-references GB:L27486; NID:g453654; PIDN:AAA27711.1; !1PID:g453655 !'##note sequence extracted from NCBI backbone (NCBIN:71287, !1NCBIP:71319) REFERENCE S00282 !$#authors Ampe, C.; Sato, M.; Pollard, T.D.; Vandekerckhove, J. !$#journal Eur. J. Biochem. (1988) 170:597-601 !$#title The primary structure of the basic isoform of Acanthamoeba !1profilin. !$#cross-references MUID:88111645; PMID:3338456 !$#accession S00282 !'##molecule_type protein !'##residues 'T',3-4,'S',6-126 ##label AMP COMMENT Profilin, which prevents the polymerization of actin, occurs !1in many kinds of cells as a complex with monomeric actin in !1a 1:1 ratio. CLASSIFICATION #superfamily profilin KEYWORDS actin binding; blocked amino end; methylated amino acid FEATURE !$2-126 #product profilin II #status experimental #label MAT\ !$2 #modified_site blocked amino end (Ser) (in mature !8form) (probably acetylated) #status experimental\ !$104 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental SUMMARY #length 126 #molecular-weight 13057 #checksum 4755 SEQUENCE /// ENTRY B48405 #type complete TITLE profilin IA - Acanthamoeba castellanii ORGANISM #formal_name Acanthamoeba castellanii DATE 19-Nov-1993 #sequence_revision 22-Jul-1994 #text_change 22-Jun-1999 ACCESSIONS B48405; B22163 REFERENCE A48405 !$#authors Pollard, T.D.; Rimm, D.L. !$#journal Cell Motil. Cytoskeleton (1991) 20:169-177 !$#title Analysis of cDNA clones for Acanthamoeba profilin-I and !1profilin-II shows end to end homology with vertebrate !1profilins and a small family of profilin genes. !$#cross-references MUID:92089911; PMID:1751969 !$#accession B48405 !'##molecule_type mRNA !'##residues 1-126 ##label POL !'##cross-references GB:L27485; NID:g440265; PIDN:AAA27710.1; !1PID:g440266 !'##note sequence extracted from NCBI backbone (NCBIN:71288, !1NCBIP:71317) REFERENCE A22163 !$#authors Ampe, C.; Vandekerckhove, J.; Brenner, S.L.; Tobacman, L.; !1Korn, E.D. !$#journal J. Biol. Chem. (1985) 260:834-840 !$#title The amino acid sequence of Acanthamoeba profilin. !$#cross-references MUID:85104958; PMID:3881427 !$#accession B22163 !'##molecule_type protein !'##residues 'T',3-4,'S',6-31,'SF',34-47,'G',49-126 ##label AMP COMMENT Profilin, which prevents the polymerization of actin, occurs !1in many kinds of cells as a complex with monomeric actin in !1a 1:1 ratio. CLASSIFICATION #superfamily profilin KEYWORDS actin binding; blocked amino end; methylated amino acid FEATURE !$2-126 #product profilin II #status experimental #label MAT\ !$2 #modified_site blocked amino end (Ser) (in mature !8form) (probably acetylated) #status experimental\ !$104 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental SUMMARY #length 126 #molecular-weight 13084 #checksum 8413 SEQUENCE /// ENTRY FADO1 #type complete TITLE profilin I - slime mold (Dictyostelium discoideum) ORGANISM #formal_name Dictyostelium discoideum DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 22-Jun-1999 ACCESSIONS A53255; S18027 REFERENCE A53255 !$#authors Haugwitz, M.; Noegel, A.A.; Rieger, D.; Lottspeich, F.; !1Schleicher, M. !$#journal J. Cell Sci. (1991) 100:481-489 !$#title Dictyostelium discoideum contains two profilin isoforms that !1differ in structure and function. !$#cross-references MUID:92226170; PMID:1725525 !$#accession A53255 !'##molecule_type mRNA !'##residues 1-126 ##label HA2 !'##cross-references EMBL:X61581; NID:g7323; PIDN:CAA43781.1; PID:g7324 !'##note parts of this sequence were confirmed by peptide sequencing CLASSIFICATION #superfamily profilin KEYWORDS actin binding; blocked amino end; methylated amino acid FEATURE !$104 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8predicted SUMMARY #length 126 #molecular-weight 13064 #checksum 4120 SEQUENCE /// ENTRY FADO2 #type complete TITLE profilin II - slime mold (Dictyostelium discoideum) ORGANISM #formal_name Dictyostelium discoideum DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 22-Jun-1999 ACCESSIONS B53255; S18028 REFERENCE A53255 !$#authors Haugwitz, M.; Noegel, A.A.; Rieger, D.; Lottspeich, F.; !1Schleicher, M. !$#journal J. Cell Sci. (1991) 100:481-489 !$#title Dictyostelium discoideum contains two profilin isoforms that !1differ in structure and function. !$#cross-references MUID:92226170; PMID:1725525 !$#accession B53255 !'##molecule_type mRNA !'##residues 1-124 ##label HA2 !'##cross-references EMBL:X61580; NID:g7325; PIDN:CAA43780.1; PID:g7326 !'##note parts of this sequence, including the amino end of the mature !1protein, were confirmed by peptide sequencing CLASSIFICATION #superfamily profilin KEYWORDS actin binding; methylated amino acid FEATURE !$2-124 #product profilin II #status experimental #label MAT\ !$102 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8predicted SUMMARY #length 124 #molecular-weight 12729 #checksum 7303 SEQUENCE /// ENTRY JT0572 #type complete TITLE profilin - Tetrahymena pyriformis ORGANISM #formal_name Tetrahymena pyriformis DATE 17-Apr-1993 #sequence_revision 22-Jul-1994 #text_change 16-Jun-2000 ACCESSIONS JT0572 REFERENCE JT0572 !$#authors Edamatsu, M.; Hirono, M.; Takemasa, T.; Watanabe, Y. !$#journal Biochem. Biophys. Res. Commun. (1991) 175:543-550 !$#title The primary structure of Tetrahymena profilin. !$#cross-references MUID:91207348; PMID:1902095 !$#accession JT0572 !'##molecule_type mRNA !'##residues 1-153 ##label EDA !'##cross-references GB:D00813; NID:g217411; PIDN:BAA00694.1; !1PID:g2160484 COMMENT Profilin, which prevents the polymerization of actin, occurs !1in many kinds of cells as a complex with monomeric actin in !1a 1:1 ratio. COMMENT The amino end of the mature protein is blocked. GENETICS !$#genetic_code SGC5 CLASSIFICATION #superfamily profilin KEYWORDS acetylated amino end; actin binding FEATURE !$2-126 #product profilin #status predicted #label MAT\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status predicted SUMMARY #length 153 #molecular-weight 16785 #checksum 3390 SEQUENCE /// ENTRY S12632 #type complete TITLE cofilin - human ORGANISM #formal_name Homo sapiens #common_name man DATE 03-Feb-1994 #sequence_revision 27-Jun-1994 #text_change 16-Jun-2000 ACCESSIONS S12632 REFERENCE S12632 !$#authors Ogawa, K.; Tashima, M.; Yumoto, Y.; Okuda, T.; Sawada, H.; !1Okuma, M.; Maruyama, Y. !$#journal Nucleic Acids Res. (1990) 18:7169 !$#title Coding sequence of human placenta Cofilin cDNA. !$#cross-references MUID:91088330; PMID:2263493 !$#accession S12632 !'##molecule_type mRNA !'##residues 1-166 ##label OGA !'##cross-references EMBL:D00682; NID:g219544; PIDN:BAA00589.1; !1PID:g219545 COMMENT Cofilin reversibly regulates actin polymerization and !1depolymerization in a pH-dependent manner. GENETICS !$#gene GDB:CFL1; CFL !'##cross-references GDB:126798; OMIM:601442 !$#map_position 11q13-11q13 CLASSIFICATION #superfamily cofilin KEYWORDS actin binding; phosphoprotein FEATURE !$26-36 #region nuclear location signal\ !$104-134 #region actin binding #status predicted SUMMARY #length 166 #molecular-weight 18502 #checksum 2529 SEQUENCE /// ENTRY A29240 #type complete TITLE cofilin - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 28-Aug-1989 #sequence_revision 27-Jun-1994 #text_change 22-Jun-1999 ACCESSIONS A29240 REFERENCE A29240 !$#authors Matsuzaki, F.; Matsumoto, S.; Yahara, I.; Yonezawa, N.; !1Nishida, E.; Sakai, H. !$#journal J. Biol. Chem. (1988) 263:11564-11568 !$#title Cloning and characterization of porcine brain cofilin cDNA. !1Cofilin contains the nuclear transport signal sequence. !$#cross-references MUID:88298817; PMID:3403546 !$#accession A29240 !'##molecule_type mRNA !'##residues 1-166 ##label MAT !'##cross-references GB:M20866; NID:g164424; PIDN:AAA31020.1; !1PID:g164425; GB:J03917 COMMENT Cofilin reversibly regulates actin polymerization and !1depolymerization in a pH-dependent manner. CLASSIFICATION #superfamily cofilin KEYWORDS actin binding; phosphoprotein FEATURE !$26-36 #region nuclear location signal\ !$104-134 #region actin binding #status predicted SUMMARY #length 166 #molecular-weight 18518 #checksum 1713 SEQUENCE /// ENTRY S12584 #type complete TITLE cofilin - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 03-Feb-1994 #sequence_revision 27-Jun-1994 #text_change 16-Jun-2000 ACCESSIONS S12584; JU0201 REFERENCE S12584 !$#authors Moriyama, K.; Matsumoto, S.; Nishida, E.; Sakai, H.; Yahara, !1I. !$#journal Nucleic Acids Res. (1990) 18:3053 !$#title Nucleotide sequence of mouse cofilin cDNA. !$#cross-references MUID:90272419; PMID:2349104 !$#accession S12584 !'##molecule_type mRNA !'##residues 1-166 ##label MOR !'##cross-references EMBL:D00472; NID:g220383; PIDN:BAA00364.1; !1PID:g220384 COMMENT Cofilin reversibly regulates actin polymerization and !1depolymerization in a pH-dependent manner. CLASSIFICATION #superfamily cofilin KEYWORDS actin binding; phosphoprotein FEATURE !$26-36 #region nuclear location signal\ !$104-134 #region actin binding #status predicted SUMMARY #length 166 #molecular-weight 18559 #checksum 2502 SEQUENCE /// ENTRY B35703 #type complete TITLE cofilin - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 12-Oct-1990 #sequence_revision 27-Jun-1994 #text_change 22-Jun-1999 ACCESSIONS B35703 REFERENCE A35703 !$#authors Abe, H.; Endo, T.; Yamamoto, K.; Obinata, T. !$#journal Biochemistry (1990) 29:7420-7425 !$#title Sequence of cDNAs encoding actin depolymerizing factor and !1cofilin of embryonic chicken skeletal muscle: two !1functionally distinct actin-regulatory proteins exhibit high !1structural homology. !$#cross-references MUID:91027755; PMID:1699599 !$#accession B35703 !'##molecule_type mRNA !'##residues 1-166 ##label ABE !'##cross-references GB:M55659; NID:g211569; PIDN:AAA62732.1; !1PID:g211570; GB:J02915 COMMENT Cofilin reversibly regulates actin polymerization and !1depolymerization in a pH-dependent manner. CLASSIFICATION #superfamily cofilin KEYWORDS actin binding; phosphoprotein FEATURE !$26-36 #region nuclear location signal\ !$104-134 #region actin binding #status predicted SUMMARY #length 166 #molecular-weight 18662 #checksum 5732 SEQUENCE /// ENTRY A54184 #type complete TITLE destrin [validated] - human ALTERNATE_NAMES actin-depolymerizing factor (ADF) ORGANISM #formal_name Homo sapiens #common_name man DATE 13-Sep-1994 #sequence_revision 02-Aug-1996 #text_change 15-Sep-2000 ACCESSIONS A54184 REFERENCE A54184 !$#authors Hawkins, M.; Pope, B.; Maciver, S.K.; Weeds, A.G. !$#journal Biochemistry (1993) 32:9985-9993 !$#title Human actin depolymerizing factor mediates a pH-sensitive !1destruction of actin filaments. !$#cross-references MUID:94002009; PMID:8399167 !$#accession A54184 !'##molecule_type mRNA !'##residues 1-165 ##label HAW !'##cross-references GB:S65738; NID:g415586; PIDN:AAB28361.1; !1PID:g415587 !'##experimental_source fetal brain !'##note sequence extracted from NCBI backbone (NCBIN:137963, !1NCBIP:137964) REFERENCE A67992 !$#authors Hatanaka, H.; Moriyama, K.; Ogura, K.; Ichikawa, S.; Yahara, !1I.; Inagaki, F. !$#submission submitted to the Brookhaven Protein Data Bank, May 1997 !$#cross-references PDB:1AK6 !$#contents annotation; conformation by (1)H-, (13)C-, and (15)N-NMR, !1residues 'TMITPSSGNS',2-165 REFERENCE A38990 !$#authors Hatanaka, H.; Ogura, K.; Moriyama, K.; Ichikawa, S.; Yahara, !1I.; Inagaki, F. !$#journal Cell (1996) 85:1047-1055 !$#title Tertiary structure of destrin and structural similarity !1between two actin-regulating protein families. !$#cross-references MUID:96270507; PMID:8674111 !$#contents annotation; NMR COMMENT The unphosphorylated form of destrin is capable of rapidly !1depolymerizing F-actin in a pH-insensitive, stoichiometric !1manner. GENETICS !$#gene GDB:ACTDP !'##cross-references GDB:249179 CLASSIFICATION #superfamily cofilin KEYWORDS acetylated amino end; actin binding; phosphoprotein FEATURE !$2-165 #product destrin #status predicted #label MAT\ !$26-36 #region nuclear location signal\ !$104-134 #region actin binding #status predicted\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status predicted\ !$3 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 165 #molecular-weight 18506 #checksum 4691 SEQUENCE /// ENTRY A35179 #type complete TITLE destrin - pig ALTERNATE_NAMES actin-depolymerizing factor ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 03-Aug-1990 #sequence_revision 05-Aug-1994 #text_change 16-Jun-2000 ACCESSIONS A35179 REFERENCE A35179 !$#authors Moriyama, K.; Nishida, E.; Yonezawa, N.; Sakai, H.; !1Matsumoto, S.; Iida, K.; Yahara, I. !$#journal J. Biol. Chem. (1990) 265:5768-5773 !$#title Destrin, a mammalian actin-depolymerizing protein, is !1closely related to cofilin. Cloning and expression of !1porcine brain destrin cDNA. !$#cross-references MUID:90202824; PMID:2156828 !$#accession A35179 !'##molecule_type mRNA !'##residues 1-165 ##label MOR !'##cross-references GB:D90053; GB:J05290; NID:g217681; PIDN:BAA14105.1; !1PID:g217682 !'##experimental_source brain COMMENT Destrin is an actin-binding protein that is capable of !1rapidly depolymerizing F-actin in a pH-insensitive, !1stoichiometric manner. CLASSIFICATION #superfamily cofilin KEYWORDS acetylated amino end; actin binding; phosphoprotein FEATURE !$2-165 #product destrin #status predicted #label MAT\ !$26-36 #region nuclear location signal\ !$104-134 #region actin binding #status predicted\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status predicted\ !$3 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 165 #molecular-weight 18506 #checksum 4691 SEQUENCE /// ENTRY A35702 #type complete TITLE destrin - chicken ALTERNATE_NAMES actin-depolymerizing factor ORGANISM #formal_name Gallus gallus #common_name chicken DATE 12-Oct-1990 #sequence_revision 05-Aug-1994 #text_change 22-Jun-1999 ACCESSIONS A35702; A35703; A40672 REFERENCE A35702 !$#authors Adams, M.E.; Minamide, L.S.; Duester, G.; Bamburg, J.R. !$#journal Biochemistry (1990) 29:7414-7420 !$#title Nucleotide sequence and expression of a cDNA encoding chick !1brain actin depolymerizing factor. !$#cross-references MUID:91027754; PMID:2223773 !$#accession A35702 !'##molecule_type mRNA !'##residues 1-165 ##label ADA !'##cross-references GB:J02912; NID:g211096; PIDN:AAA48575.1; !1PID:g211097 !'##experimental_source brain !'##note part of this sequence was confirmed by peptide sequencing REFERENCE A35703 !$#authors Abe, H.; Endo, T.; Yamamoto, K.; Obinata, T. !$#journal Biochemistry (1990) 29:7420-7425 !$#title Sequence of cDNAs encoding actin depolymerizing factor and !1cofilin of embryonic chicken skeletal muscle: two !1functionally distinct actin-regulatory proteins exhibit high !1structural homology. !$#cross-references MUID:91027755; PMID:1699599 !$#accession A35703 !'##molecule_type mRNA !'##residues 1-165 ##label ABE !'##cross-references GB:M55660; GB:J02915; NID:g211092; PIDN:AAA48573.1; !1PID:g211093 !'##experimental_source muscle !'##note part of this sequence was confirmed by peptide sequencing REFERENCE A40672 !$#authors Morgan, T.E.; Lockerbie, R.O.; Minamide, L.S.; Browning, !1M.D.; Bamburg, J.R. !$#journal J. Cell Biol. (1993) 122:623-633 !$#title Isolation and characterization of a regulated form of actin !1depolymerizing factor. !$#cross-references MUID:93328764; PMID:7687605 !$#accession A40672 !'##molecule_type protein !'##residues 20-30 ##label MOR REFERENCE A38989 !$#authors Agnew, B.J.; Minamide, L.S.; Bamburg, J.R. !$#journal J. Biol. Chem. (1995) 270:17582-17587 !$#title Reactivation of phosphorylated actin depolymerizing factor !1and identification of the regulatory site. !$#cross-references MUID:95340558; PMID:7615564 !$#contents annotation; acetylated amino end; phosphorylation site COMMENT Destrin is an actin-binding protein that is capable of !1rapidly depolymerizing F-actin in a pH-insensitive, !1stoichiometric manner. CLASSIFICATION #superfamily cofilin KEYWORDS acetylated amino end; actin binding; phosphoprotein FEATURE !$2-165 #product destrin #status predicted #label MAT\ !$26-36 #region nuclear location signal\ !$104-134 #region actin binding #status predicted\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental\ !$3 #binding_site phosphate (Ser) (covalent) #status !8experimental SUMMARY #length 165 #molecular-weight 18532 #checksum 7089 SEQUENCE /// ENTRY A44397 #type complete TITLE cofilin - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein L0595; protein YLL050c ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Dec-1993 #sequence_revision 27-Jun-1994 #text_change 21-Jul-2000 ACCESSIONS A44397; B44397; JN0529; S64802; S50970; S31309; S36087 REFERENCE A44397 !$#authors Moon, A.L.; Janmey, P.A.; Louie, K.A.; Drubin, D.G. !$#journal J. Cell Biol. (1993) 120:421-435 !$#title Cofilin is an essential component of the yeast cortical !1cytoskeleton. !$#cross-references MUID:93132073; PMID:8421056 !$#accession A44397 !'##molecule_type DNA !'##residues 1-143 ##label MOO !'##cross-references EMBL:Z14971; NID:g3563; PIDN:CAA78694.1; PID:g3564 !'##note sequence extracted from NCBI backbone (NCBIN:122683, !1NCBIP:122684) !$#accession B44397 !'##molecule_type protein !'##residues 43-56;83-96,'X',98;106-129,'DS',132-141 ##label MO2 !'##note sequence extracted from NCBI backbone REFERENCE JN0529 !$#authors Iida, K.; Moriyama, K.; Matsumoto, S.; Kawasaki, H.; !1Nishida, E.; Yahara, I. !$#journal Gene (1993) 124:115-120 !$#title Isolation of a yeast essential gene, COF1, that encodes a !1homologue of mammalian cofilin, a low-Mr actin-binding and !1depolymerizing protein. !$#cross-references MUID:93178959; PMID:8440472 !$#accession JN0529 !'##molecule_type DNA !'##residues 1-143 ##label IID !'##cross-references GB:D13230; NID:g287599; PIDN:BAA02514.1; !1PID:g287600 REFERENCE S64792 !$#authors Wedler, H.; Wedler, E.; Scharfe, M.; Wambutt, R. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64802 !'##molecule_type DNA !'##residues 1-143 ##label WED !'##cross-references EMBL:Z73155; NID:g1360250; PIDN:CAA97502.1; !1PID:g1360251; GSPDB:GN00012; MIPS:YLL050c !'##note experimental_source strain S288C REFERENCE S50950 !$#authors Wedler, H.; Wambutt, R. !$#submission submitted to the EMBL Data Library, January 1995 !$#description Sequence of a 37 kb DNA fragment from chromosome XII of !1Saccharomyces cerevisiae including the subtelomeric region !1of the left arm. !$#accession S50970 !'##molecule_type DNA !'##residues 'MWGKKFIRSQENVKFLCS',6-143 ##label WEW !'##cross-references EMBL:Z47973; NID:g642313; PIDN:CAA88007.1; !1PID:g642334 COMMENT Cofilin reversibly regulates actin polymerization and !1depolymerization in a pH-dependent manner. GENETICS !$#gene SGD:COF1; MIPS:YLL050c !'##cross-references SGD:S0003973; MIPS:YLL050c !$#map_position 12L !$#introns 5/2 CLASSIFICATION #superfamily cofilin KEYWORDS actin binding FEATURE !$88-118 #region actin binding #status predicted SUMMARY #length 143 #molecular-weight 15901 #checksum 5280 SEQUENCE /// ENTRY S31484 #type complete TITLE calponin H1 - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 20-Feb-1995 #sequence_revision 07-Jul-1995 #text_change 22-Jun-1999 ACCESSIONS S36146; S31484 REFERENCE S36145 !$#authors Strasser, P.; Gimona, M.; Moessler, H.; Herzog, M.; Small, !1J.V. !$#journal FEBS Lett. (1993) 330:13-18 !$#title Mammalian calponin. Identification and expression of genetic !1variants. !$#cross-references MUID:93380560; PMID:8370452 !$#accession S36146 !'##molecule_type mRNA !'##residues 1-297 ##label ST2 !'##cross-references EMBL:Z19538; NID:g1959; PIDN:CAA79598.1; PID:g1960 COMMENT This thin filament-associated protein binds actin, !1tropomyosin, and calmodulin. It appears to promote the !1relaxation of smooth muscle by inhibiting the !1actin-activated MgATPase activity of myosin. Phosphorylation !1of calponin causes dissociation from actin and tropomyosin !1and blocks this inhibition. CLASSIFICATION #superfamily calponin; calponin repeat homology; smooth !1muscle protein SM22 homology KEYWORDS actin binding; calmodulin binding; muscle contraction; !1phosphoprotein; smooth muscle FEATURE !$6-190 #domain smooth muscle protein SM22 homology #label !8SMH\ !$164-194 #domain calponin repeat homology #label CRH1\ !$204-234 #domain calponin repeat homology #label CRH2\ !$243-273 #domain calponin repeat homology #label CRH3 SUMMARY #length 297 #molecular-weight 33226 #checksum 3874 SEQUENCE /// ENTRY S31486 #type complete TITLE calponin H1 - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 20-Feb-1995 #sequence_revision 07-Jul-1995 #text_change 22-Jun-1999 ACCESSIONS S36145; S31486 REFERENCE S36145 !$#authors Strasser, P.; Gimona, M.; Moessler, H.; Herzog, M.; Small, !1J.V. !$#journal FEBS Lett. (1993) 330:13-18 !$#title Mammalian calponin. Identification and expression of genetic !1variants. !$#cross-references MUID:93380560; PMID:8370452 !$#accession S36145 !'##molecule_type mRNA !'##residues 1-297 ##label ST2 !'##cross-references EMBL:Z19542; NID:g51137; PIDN:CAA79602.1; !1PID:g51138 COMMENT This thin filament-associated protein binds actin, !1tropomyosin, and calmodulin. It appears to promote the !1relaxation of smooth muscle by inhibiting the !1actin-activated MgATPase activity of myosin. Phosphorylation !1of calponin causes dissociation from actin and tropomyosin !1and blocks this inhibition. CLASSIFICATION #superfamily calponin; calponin repeat homology; smooth !1muscle protein SM22 homology KEYWORDS actin binding; calmodulin binding; muscle contraction; !1phosphoprotein; smooth muscle FEATURE !$6-190 #domain smooth muscle protein SM22 homology #label !8SMH\ !$164-194 #domain calponin repeat homology #label CRH1\ !$204-234 #domain calponin repeat homology #label CRH2\ !$243-273 #domain calponin repeat homology #label CRH3 SUMMARY #length 297 #molecular-weight 33355 #checksum 5612 SEQUENCE /// ENTRY JN0773 #type complete TITLE calponin H1 - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1993 #sequence_revision 07-Jul-1995 #text_change 16-Jun-2000 ACCESSIONS S37640; JN0773 REFERENCE S37637 !$#authors Shanahan, C.M.; Weissberg, P.L.; Metcalfe, J.C. !$#journal Circ. Res. (1993) 73:193-204 !$#title Isolation of gene markers of differentiated and !1proliferating vascular smooth muscle cells. !$#cross-references MUID:93284726; PMID:8508530 !$#accession S37640 !'##molecule_type mRNA !'##residues 1-297 ##label SHA !'##cross-references EMBL:X71071; NID:g313817; PIDN:CAA50397.1; !1PID:g313818 REFERENCE JN0773 !$#authors Nishida, W.; Kitami, Y.; Hiwada, K. !$#journal Gene (1993) 130:297-302 !$#title cDNA cloning and mRNA expression of calponin and SM22 in rat !1aorta smooth muscle cells. !$#cross-references MUID:93366190; PMID:8359698 !$#accession JN0773 !'##molecule_type mRNA !'##residues 1-96,'E',98-297 ##label NIS !'##cross-references GB:D14437; NID:g436047; PIDN:BAA03320.1; !1PID:g436048 COMMENT This thin filament-associated protein binds actin, !1tropomyosin, and calmodulin. It appears to promote the !1relaxation of smooth muscle by inhibiting the !1actin-activated MgATPase activity of myosin. Phosphorylation !1of calponin causes dissociation from actin and tropomyosin !1and blocks this inhibition. CLASSIFICATION #superfamily calponin; calponin repeat homology; smooth !1muscle protein SM22 homology KEYWORDS actin binding; calmodulin binding; muscle contraction; !1phosphoprotein; smooth muscle FEATURE !$6-190 #domain smooth muscle protein SM22 homology #label !8SMH\ !$52-144 #region calmodulin binding #status predicted\ !$145-182 #region actin binding #status predicted\ !$164-194 #domain calponin repeat homology #label CRH1\ !$204-234 #domain calponin repeat homology #label CRH2\ !$243-273 #domain calponin repeat homology #label CRH3 SUMMARY #length 297 #molecular-weight 33343 #checksum 5324 SEQUENCE /// ENTRY A39871 #type complete TITLE calponin alpha, smooth muscle - chicken CONTAINS calponin beta, smooth muscle ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Dec-1991 #sequence_revision 07-Jul-1995 #text_change 22-Jun-1999 ACCESSIONS A39871; B39871; A46007; A42859; S39778 REFERENCE A39871 !$#authors Takahashi, K.; Nadal-Ginard, B. !$#journal J. Biol. Chem. (1991) 266:13284-13288 !$#title Molecular cloning and sequence analysis of smooth muscle !1calponin. !$#cross-references MUID:91302359; PMID:2071603 !$#accession A39871 !'##molecule_type mRNA !'##residues 1-292 ##label TAK !'##cross-references GB:M63559; NID:g211387; PIDN:AAA48651.1; !1PID:g211388 !$#accession B39871 !'##molecule_type mRNA !'##residues 1-216,257-292 ##label TA2 !'##cross-references GB:M63560; NID:g211389; PIDN:AAA48652.1; !1PID:g211390 REFERENCE A46007 !$#authors Nakamura, F.; Mino, T.; Yamamoto, J.; Naka, M.; Tanaka, T. !$#journal J. Biol. Chem. (1993) 268:6194-6201 !$#title Identification of the regulatory site in smooth muscle !1calponin that is phosphorylated by protein kinase C. !$#cross-references MUID:93203204; PMID:8454594 !$#accession A46007 !'##molecule_type protein !'##residues 173-185;213-225;252-265 ##label NAK REFERENCE A42859 !$#authors Mezgueldi, M.; Fattoum, A.; Derancourt, J.; Kassab, R. !$#journal J. Biol. Chem. (1992) 267:15943-15951 !$#title Mapping of the functional domains in the amino-terminal !1region of calponin. !$#cross-references MUID:92348464; PMID:1639822 !$#accession A42859 !'##molecule_type protein !'##residues 7-21;52-65,'K';183-194 ##label MEZ !'##note authors found Thr-184 to be the preferred and functionally most !1important site for phosphorylation by protein kinase C REFERENCE S39778 !$#authors Winder, S.J.; Allen, B.G.; Fraser, E.D.; Kang, H.M.; !1Kargacin, G.J.; Walsh, M.P. !$#journal Biochem. J. (1993) 296:827-836 !$#title Calponin phosphorylation in vitro and in intact muscle. !$#cross-references MUID:94107251; PMID:8280082 !$#accession S39778 !'##molecule_type protein !'##residues 67-74;173-185;252-256 ##label WIN !'##note authors found phosphorylation at Ser-175, the major site for !1modification by protein kinase C or Ca2+/ !1calmodulin-dependent protein kinase II, causes dissociation !1of calponin from actin COMMENT This thin filament-associated protein binds actin, !1tropomyosin, and calmodulin. It appears to promote the !1relaxation of smooth muscle by inhibiting the !1actin-activated MgATPase activity of myosin. Phosphorylation !1of calponin causes dissociation from actin and tropomyosin !1and blocks this inhibition. CLASSIFICATION #superfamily calponin; calponin repeat homology; smooth !1muscle protein SM22 homology KEYWORDS actin binding; alternative splicing; calmodulin binding; !1muscle contraction; phosphoprotein; smooth muscle FEATURE !$1-292 #domain calponin alpha, smooth muscle #status !8predicted #label CALA\ !$1-216,257-292 #domain calponin beta, smooth muscle #status !8predicted #label CALB\ !$6-190 #domain smooth muscle protein SM22 homology #label !8SMH\ !$52-144 #region calmodulin binding #status predicted\ !$145-182 #region actin binding #status predicted\ !$164-194 #domain calponin repeat homology #label CRH1\ !$204-234 #domain calponin repeat homology #label CRH2\ !$243-273 #domain calponin repeat homology #label CRH3 SUMMARY #length 292 #molecular-weight 32333 #checksum 8648 SEQUENCE /// ENTRY S31483 #type fragment TITLE calponin H2 - pig (fragment) ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 13-Jun-1995 #sequence_revision 07-Jul-1995 #text_change 22-Jun-1999 ACCESSIONS S36148; S31483 REFERENCE S36145 !$#authors Strasser, P.; Gimona, M.; Moessler, H.; Herzog, M.; Small, !1J.V. !$#journal FEBS Lett. (1993) 330:13-18 !$#title Mammalian calponin. Identification and expression of genetic !1variants. !$#cross-references MUID:93380560; PMID:8370452 !$#accession S36148 !'##molecule_type mRNA !'##residues 1-296 ##label STR !'##cross-references EMBL:Z19539; NID:g1961; PIDN:CAA79599.1; PID:g1962 COMMENT This thin filament-associated protein binds actin, !1tropomyosin, and calmodulin. It appears to promote the !1relaxation of smooth muscle by inhibiting the !1actin-activated MgATPase activity of myosin. Phosphorylation !1of calponin causes dissociation from actin and tropomyosin !1and blocks this inhibition. CLASSIFICATION #superfamily calponin; calponin repeat homology; smooth !1muscle protein SM22 homology KEYWORDS actin binding; calmodulin binding; muscle contraction; !1phosphoprotein; smooth muscle FEATURE !$6-192 #domain smooth muscle protein SM22 homology #label !8SMH\ !$166-196 #domain calponin repeat homology #label CRH1\ !$206-236 #domain calponin repeat homology #label CRH2\ !$245-274 #domain calponin repeat homology #label CRH3 SUMMARY #length 296 #checksum 2220 SEQUENCE /// ENTRY S31485 #type complete TITLE calponin H2 - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 20-Feb-1995 #sequence_revision 07-Jul-1995 #text_change 22-Jun-1999 ACCESSIONS S36147; S31485 REFERENCE S36145 !$#authors Strasser, P.; Gimona, M.; Moessler, H.; Herzog, M.; Small, !1J.V. !$#journal FEBS Lett. (1993) 330:13-18 !$#title Mammalian calponin. Identification and expression of genetic !1variants. !$#cross-references MUID:93380560; PMID:8370452 !$#accession S36147 !'##molecule_type mRNA !'##residues 1-305 ##label STR !'##cross-references EMBL:Z19543; NID:g51143; PIDN:CAA79603.1; !1PID:g51144 COMMENT This thin filament-associated protein binds actin, !1tropomyosin, and calmodulin. It appears to promote the !1relaxation of smooth muscle by inhibiting the !1actin-activated MgATPase activity of myosin. Phosphorylation !1of calponin causes dissociation from actin and tropomyosin !1and blocks this inhibition. CLASSIFICATION #superfamily calponin; calponin repeat homology; smooth !1muscle protein SM22 homology KEYWORDS actin binding; calmodulin binding; muscle contraction; !1phosphoprotein; smooth muscle FEATURE !$6-192 #domain smooth muscle protein SM22 homology #label !8SMH\ !$166-196 #domain calponin repeat homology #label CRH1\ !$206-236 #domain calponin repeat homology #label CRH2\ !$245-274 #domain calponin repeat homology #label CRH3 SUMMARY #length 305 #molecular-weight 33155 #checksum 2233 SEQUENCE /// ENTRY JS0774 #type complete TITLE smooth muscle protein SM22 - human ALTERNATE_NAMES actin-associated protein SM22alpha; transgelin ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1993 #sequence_revision 15-Oct-1999 #text_change 16-Jun-2000 ACCESSIONS JC5577; JS0774; I84756 REFERENCE JC5577 !$#authors Yamamura, H.; Masuda, H.; Ikeda, W.; Tokuyama, T.; Takagi, !1M.; Shibata, N.; Tatsuta, M.; Takahashi, K. !$#journal J. Biochem. (1997) 122:157-167 !$#title Structure and expression of the human SM22alpha gene, !1assignment of the gene to chromosome 11, and repression of !1the promoter activity by cytosine DNA methylation. !$#cross-references MUID:97420698; PMID:9276683 !$#accession JC5577 !'##molecule_type mRNA !'##residues 1-201 ##label YAM !'##cross-references DDBJ:D17409; NID:g2335046; PIDN:BAA21811.1; !1PID:g2335047 REFERENCE JS0774 !$#authors Thweatt, R.; Lumpkin Jr., C.K.; Goldstein, S. !$#journal Biochem. Biophys. Res. Commun. (1992) 187:1-7 !$#title A novel gene encoding a smooth muscle protein is !1overexpressed in senescent human fibroblasts. !$#cross-references MUID:92392308; PMID:1520290 !$#accession JS0774 !'##molecule_type mRNA !'##residues 1-48,'P',50-103,'S',105-201 ##label THW !'##cross-references GB:M95787; NID:g177174; PIDN:AAA58351.1; !1PID:g177175 !'##note the authors translated the codon TCT for residue 104 as Tyr !'##note one of several proteins overexpressed in Werner syndrome !1fibroblasts and senescent normal fibroblasts REFERENCE I50236 !$#authors Nishida, W.; Kitami, Y.; Abe, M.; Kiwada, K. !$#journal Biochem. Int. (1991) 23:663-668 !$#title Gene cloning and nucleotide sequence of SM22-alpha from the !1chicken gizzard smooth muscle. !$#cross-references MUID:91337140; PMID:1872880 !$#accession I84756 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-71,'E',73-103,'C',105-178,'V',180-201 ##label NIS !'##cross-references GB:M83106; NID:g179031; PIDN:AAA58375.1; !1PID:g179032 GENETICS !$#gene GDB:WS3-10; SM22; SM22alpha !'##cross-references GDB:3922383; OMIM:600818 !$#map_position 11q23.2 !$#introns 60/3; 120/1; 154/2 CLASSIFICATION #superfamily smooth muscle protein SM22; calponin repeat !1homology; smooth muscle protein SM22 homology KEYWORDS actin binding; smooth muscle FEATURE !$2-201 #domain smooth muscle protein SM22 homology #label !8SMH\ !$175-201 #domain calponin repeat homology #label CRH SUMMARY #length 201 #molecular-weight 22611 #checksum 4187 SEQUENCE /// ENTRY JN0774 #type complete TITLE smooth muscle protein SM22 - rat ALTERNATE_NAMES transgelin ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1993 #sequence_revision 07-Jul-1995 #text_change 22-Jun-1999 ACCESSIONS JN0774; S37637; I63215; I52840 REFERENCE JN0773 !$#authors Nishida, W.; Kitami, Y.; Hiwada, K. !$#journal Gene (1993) 130:297-302 !$#title cDNA cloning and mRNA expression of calponin and SM22 in rat !1aorta smooth muscle cells. !$#cross-references MUID:93366190; PMID:8359698 !$#accession JN0774 !'##molecule_type mRNA !'##residues 1-201 ##label NIS !'##cross-references GB:M83107; NID:g202982; PIDN:AAA40762.1; !1PID:g202983 REFERENCE S37637 !$#authors Shanahan, C.M.; Weissberg, P.L.; Metcalfe, J.C. !$#journal Circ. Res. (1993) 73:193-204 !$#title Isolation of gene markers of differentiated and !1proliferating vascular smooth muscle cells. !$#cross-references MUID:93284726; PMID:8508530 !$#accession S37637 !'##molecule_type mRNA !'##residues 1-201 ##label SHA !'##cross-references EMBL:X71070; NID:g313811; PIDN:CAA50396.1; !1PID:g313812 REFERENCE I50236 !$#authors Nishida, W.; Kitami, Y.; Abe, M.; Kiwada, K. !$#journal Biochem. Int. (1991) 23:663-668 !$#title Gene cloning and nucleotide sequence of SM22-alpha from the !1chicken gizzard smooth muscle. !$#cross-references MUID:91337140; PMID:1872880 !$#accession I63215 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-201 ##label NIS2 !'##cross-references GB:M83107; NID:g202982; PIDN:AAA40762.1; !1PID:g202983 REFERENCE I52840 !$#authors Prinjha, R.K.; Shapland, C.E.; Hsuan, J.J.; Totty, N.F.; !1Mason, I.J.; Lawson, D. !$#journal Cell Motil. Cytoskeleton (1994) 28:243-255 !$#title Cloning and sequencing of cDNAs encoding the actin !1cross-linking protein transgelin defines a new family of !1actin-associated proteins. !$#cross-references MUID:95042787; PMID:7954852 !$#accession I52840 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-201 ##label PRI !'##cross-references EMBL:X64422; NID:g603876; PIDN:CAA45769.1; !1PID:g603877 GENETICS !$#gene SM22 CLASSIFICATION #superfamily smooth muscle protein SM22; calponin repeat !1homology; smooth muscle protein SM22 homology KEYWORDS actin binding; smooth muscle FEATURE !$2-201 #domain smooth muscle protein SM22 homology #label !8SMH\ !$175-201 #domain calponin repeat homology #label CRH SUMMARY #length 201 #molecular-weight 22603 #checksum 4992 SEQUENCE /// ENTRY A60598 #type complete TITLE smooth muscle protein SM22 homolog - mouse ALTERNATE_NAMES actin-associated protein p27 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 17-Apr-1993 #sequence_revision 07-Jul-1995 #text_change 07-Jul-1995 ACCESSIONS A60598 REFERENCE A60598 !$#authors Almendral, J.M.; Santaren, J.F.; Perera, J.; Zerial, M.; !1Bravo, R. !$#journal Exp. Cell Res. (1989) 181:518-530 !$#title Expression, cloning and cDNA sequence of a fibroblast !1serum-regulated gene encoding a putative actin-associated !1protein (p27). !$#cross-references MUID:89170984; PMID:2924801 !$#accession A60598 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-201 ##label ALM !'##experimental_source NIH 3T3 fibroblasts COMMENT Expression of this actin-associated protein increases in !1response to growth factors. CLASSIFICATION #superfamily smooth muscle protein SM22; calponin repeat !1homology; smooth muscle protein SM22 homology KEYWORDS actin binding; cytoskeleton FEATURE !$2-201 #domain smooth muscle protein SM22 homology #label !8SMH\ !$175-201 #domain calponin repeat homology #label CRH SUMMARY #length 201 #molecular-weight 22491 #checksum 4066 SEQUENCE /// ENTRY A26694 #type complete TITLE smooth muscle protein SM22-alpha - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 21-May-1988 #sequence_revision 13-Mar-1997 #text_change 03-Dec-1999 ACCESSIONS I50236; A26694 REFERENCE I50236 !$#authors Nishida, W.; Kitami, Y.; Abe, M.; Kiwada, K. !$#journal Biochem. Int. (1991) 23:663-668 !$#title Gene cloning and nucleotide sequence of SM22-alpha from the !1chicken gizzard smooth muscle. !$#cross-references MUID:91337140; PMID:1872880 !$#accession I50236 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-200 ##label NIS !'##cross-references GB:M83105; NID:g211812; PIDN:AAA48782.1; !1PID:g211813 REFERENCE A26694 !$#authors Pearlstone, J.R.; Weber, M.; Lees-Miller, J.P.; Carpenter, !1M.R.; Smillie, L.B. !$#journal J. Biol. Chem. (1987) 262:5985-5991 !$#title Amino acid sequence of chicken gizzard smooth muscle !1SM22-alpha. !$#cross-references MUID:87194808; PMID:3571244 !$#accession A26694 !'##molecule_type protein !'##residues 2-198 ##label PEA !'##experimental_source gizzard GENETICS !$#gene SM22 CLASSIFICATION #superfamily smooth muscle protein SM22; calponin repeat !1homology; smooth muscle protein SM22 homology KEYWORDS acetylated amino end; smooth muscle FEATURE !$2-200 #domain smooth muscle protein SM22 homology #label !8SMH\ !$175-200 #domain calponin repeat homology #label CRH\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental SUMMARY #length 200 #molecular-weight 22314 #checksum 1588 SEQUENCE /// ENTRY A30128 #type complete TITLE synchronous muscle-specific protein mp20 - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 07-Jun-1990 #sequence_revision 07-Jul-1995 #text_change 16-Feb-1997 ACCESSIONS A30128 REFERENCE A30128 !$#authors Ayme-Southgate, A.; Lasko, P.; French, C.; Pardue, M.L. !$#journal J. Cell Biol. (1989) 108:521-531 !$#title Characterization of the gene for mp20: a Drosophila muscle !1protein that is not found in asynchronous oscillatory flight !1muscle. !$#cross-references MUID:89139570; PMID:2537318 !$#accession A30128 !'##molecule_type DNA !'##residues 1-184 ##label AYM GENETICS !$#gene FlyBase:Mp20 !'##cross-references FlyBase:FBgn0002789 !$#introns 10/3; 121/3 CLASSIFICATION #superfamily smooth muscle protein SM22; calponin repeat !1homology; smooth muscle protein SM22 homology KEYWORDS muscle FEATURE !$1-182 #domain smooth muscle protein SM22 homology #label !8SMH\ !$20-31 #domain calcium binding #status predicted #label CA1\ !$93-104 #domain calcium binding #status predicted #label CA2\ !$157-184 #domain calponin repeat homology #label CRH SUMMARY #length 184 #molecular-weight 20190 #checksum 155 SEQUENCE /// ENTRY FAHUP #type complete TITLE gelsolin precursor, plasma [validated] - human ALTERNATE_NAMES actin-depolymerizing factor; brevin CONTAINS amyloid protein, 12K; gelsolin, cytosolic ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 08-Dec-2000 ACCESSIONS A03011; A38797; S03073; A60849; A36029; A61263; A34562; !1A34137 REFERENCE A93383 !$#authors Kwiatkowski, D.J.; Stossel, T.P.; Orkin, S.H.; Mole, J.E.; !1Colten, H.R.; Yin, H.L. !$#journal Nature (1986) 323:455-458 !$#title Plasma and cytoplasmic gelsolins are encoded by a single !1gene and contain a duplicated actin-binding domain. !$#cross-references MUID:87014807; PMID:3020431 !$#accession A03011 !'##molecule_type mRNA !'##residues 1-782 ##label KWI !'##cross-references EMBL:X04412; NID:g35447; PIDN:CAA28000.1; !1PID:g736249 !$#accession A38797 !'##molecule_type protein !'##residues 28-52;178-194,'XX',197;279-290,'S',292-294,'XX', !1297-303;434-449,'XX',452-453,'X',455-459;538-542,'XX', !1545-581 ##label KW2 REFERENCE S03073 !$#authors Kwiatkowski, D.J.; Mehl, R.; Yin, H.L. !$#journal J. Cell Biol. (1988) 106:375-384 !$#title Genomic organization and biosynthesis of secreted and !1cytoplasmic forms of gelsolin. !$#cross-references MUID:88115587; PMID:2828382 !$#accession S03073 !'##status translation not shown !'##molecule_type DNA !'##residues 1-116 ##label KW3 !'##cross-references EMBL:X07065 !'##note 1-Met is the initiator for plasma gelsolin. 52-Met is the !1initiator for cytosolic gelsolin REFERENCE A60849 !$#authors Bryan, J.; Hwo, S. !$#journal J. Cell Biol. (1986) 102:1439-1446 !$#title Definition of an N-terminal actin-binding domain and a !1C-terminal Ca(2+) regulatory domain in human brevin. !$#cross-references MUID:86168493; PMID:3082893 !$#accession A60849 !'##molecule_type protein !'##residues 'X',52-55,'X',57-59,'X',61-62 ##label BRY REFERENCE A36029 !$#authors Vandekerckhove, J.; Bauw, G.; Vancompernolle, K.; Honore, !1B.; Celis, J. !$#journal J. Cell Biol. (1990) 111:95-102 !$#title Comparative two-dimensional gel analysis and microsequencing !1identifies gelsolin as one of the most prominent !1downregulated markers of transformed human fibroblast and !1epithelial cells. !$#cross-references MUID:90307803; PMID:2164032 !$#accession A36029 !'##molecule_type protein !'##residues 'XX',150-153,'X',155,'X',157-159;486-492,'X',494-498,'X', !1500,'X';628-641,'X',643 ##label VAN REFERENCE A61263 !$#authors Maury, C.P.J. !$#journal J. Clin. Invest. (1991) 87:1195-1199 !$#title Gelsolin-related amyloidosis. Identification of the amyloid !1protein in Finnish hereditary amyloidosis as a fragment of !1variant gelsolin. !$#cross-references MUID:91185597; PMID:1849145 !$#accession A61263 !'##molecule_type protein !'##residues 200-213,'N',215-270 ##label MAU !'##experimental_source familial amyloid polyneuropathy (Finnish-type) !1heart and kidney amyloid fibrils !'##note the substitution of Asn for 214-Asp causes disease REFERENCE A34562 !$#authors Haltia, M.; Prelli, F.; Ghiso, J.; Kiuru, S.; Somer, H.; !1Palo, J.; Frangione, B. !$#journal Biochem. Biophys. Res. Commun. (1990) 167:927-932 !$#title Amyloid protein in familial amyloidosis (Finnish type) is !1homologous to gelsolin, an actin-binding protein. !$#cross-references MUID:90211339; PMID:2157434 !$#accession A34562 !'##molecule_type protein !'##residues 200-214 ##label HAL !'##experimental_source diseased kidney, familial amyloidosis (Finnish !1type) REFERENCE A92450 !$#authors Lind, S.E.; Janmey, P.A. !$#journal J. Biol. Chem. (1984) 259:13262-13266 !$#title Human plasma gelsolin binds to fibronectin. !$#cross-references MUID:85030446; PMID:6092370 !$#contents annotation; fibronectin binding REFERENCE A34137 !$#authors Maury, C.P.J.; Alli, K.; Baumann, M. !$#journal FEBS Lett. (1990) 260:85-87 !$#title Finnish hereditary amyloidosis. Amino acid sequence homology !1between the amyloid fibril protein and human plasma !1gelsoline. !$#cross-references MUID:90127414; PMID:2153578 !$#accession A34137 !'##molecule_type protein !'##residues 235-237;240-252;258-269 ##label MA2 !'##experimental_source kidney, Finnish hereditary amyloidosis patient COMMENT Gelsolin is a calcium-regulated, actin-modulating protein !1that binds to the plus (or barbed) ends of actin monomers or !1filaments, preventing monomer exchange (end-blocking or !1capping). It can promote the assembly of monomers into !1filaments (nucleation) as well as sever filaments already !1formed. COMMENT A single gene encodes two forms of gelsolin; one remains !1associated with the cell cytoplasm, the other is secreted. !1In addition to its role in actin regulation, this protein is !1known to bind with high affinity to fibronectin. GENETICS !$#gene GDB:GSN !'##cross-references GDB:120019; OMIM:105120; OMIM:137350 !$#map_position 9q33-9q33 !$#introns 48/3; 117/1 CLASSIFICATION #superfamily gelsolin; gelsolin repeat homology KEYWORDS actin binding; alternative splicing; amyloid; calcium; !1duplication FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-782 #product gelsolin, plasma #status experimental #label !8MAT1\ !$51-176 #domain actin-severing #status predicted #label SEV\ !$53-782 #product gelsolin, cytosolic #status experimental !8#label MAT2\ !$66-397 #domain gelsolin repeat homology #label GEL1\ !$123-126 #region actin-actin interfilament contact\ !$434-782 #domain calcium-sensitive, actin binding #status !8predicted #label ACT\ !$445-764 #domain gelsolin repeat homology #label GEL2 SUMMARY #length 782 #molecular-weight 85697 #checksum 6638 SEQUENCE /// ENTRY A32621 #type complete TITLE gelsolin, cytosolic - mouse ALTERNATE_NAMES actin-depolymerizing factor; brevin ORGANISM #formal_name Mus musculus #common_name house mouse DATE 21-May-1990 #sequence_revision 14-Jul-1994 #text_change 22-Jun-1999 ACCESSIONS A32621 REFERENCE A32621 !$#authors Dieffenbach, C.W.; SenGupta, D.N.; Krause, D.; Sawzak, D.; !1Silverman, R.H. !$#journal J. Biol. Chem. (1989) 264:13281-13288 !$#title Cloning of murine gelsolin and its regulation during !1differentiation of embryonal carcinoma cells. !$#cross-references MUID:89327303; PMID:2546951 !$#accession A32621 !'##molecule_type mRNA !'##residues 1-731 ##label DIE !'##cross-references GB:J04953; NID:g193463; PIDN:AAA37677.1; !1PID:g309249 COMMENT Gelsolin is a calcium-regulated, actin-modulating protein !1that binds to the plus (or barbed) ends of actin monomers or !1filaments, preventing monomer exchange (end-blocking or !1capping). It can promote the assembly of monomers into !1filaments (nucleation) as well as sever filaments already !1formed. CLASSIFICATION #superfamily gelsolin; gelsolin repeat homology KEYWORDS actin binding; alternative splicing; calcium; duplication FEATURE !$2-731 #product gelsolin, cytosolic #status predicted #label !8MAT2\ !$2-125 #domain actin-severing #status predicted #label SEV\ !$15-346 #domain gelsolin repeat homology #label GEL1\ !$72-75 #region actin-actin interfilament contact\ !$383-731 #domain calcium-sensitive, actin binding #status !8predicted #label ACT\ !$394-713 #domain gelsolin repeat homology #label GEL2 SUMMARY #length 731 #molecular-weight 80877 #checksum 3681 SEQUENCE /// ENTRY A31642 #type complete TITLE villin [validated] - human ALTERNATE_NAMES villin 1 ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1990 #sequence_revision 05-Apr-1995 #text_change 08-Dec-2000 ACCESSIONS A31642; B25703; G02820 REFERENCE A31642 !$#authors Arpin, M.; Pringault, E.; Finidori, J.; Garcia, A.; Jeltsch, !1J.M.; Vandekerckhove, J.; Louvard, D. !$#journal J. Cell Biol. (1988) 107:1759-1766 !$#title Sequence of human villin: a large duplicated domain !1homologous with other actin-severing proteins and a unique !1small carboxy-terminal domain related to villin specificity. !$#cross-references MUID:89034434; PMID:2846586 !$#accession A31642 !'##molecule_type mRNA !'##residues 1-827 ##label ARP !'##cross-references EMBL:X12901; NID:g37842; PIDN:CAA31386.1; !1PID:g37843 !'##note Ala-2 was also found during direct protein sequencing of the !1amino end REFERENCE A91057 !$#authors Pringault, E.; Arpin, M.; Garcia, A.; Finidori, J.; Louvard, !1D. !$#journal EMBO J. (1986) 5:3119-3124 !$#title A human villin cDNA clone to investigate the differentiation !1of intestinal and kidney cells in vivo and in culture. !$#cross-references MUID:87133467; PMID:3453110 !$#accession B25703 !'##molecule_type mRNA !'##residues 718-734,'S',736-827 ##label PRI !'##cross-references GB:X04657; NID:g37844; PIDN:CAA28355.1; PID:g37845 COMMENT Villin is abundant in the microvilli of intestinal !1epithelial cells and kidney proximal tubule cells. GENETICS !$#gene GDB:VIL1; VIL !'##cross-references GDB:120531; OMIM:193040 !$#map_position 2q35-2q35 FUNCTION !$#description calcium-regulated actin-binding; in vitro, bundles actin at !1low Ca++ concentrations, severs and caps actin filaments at !1higher concentrations CLASSIFICATION #superfamily villin; gelsolin repeat homology; villin !1headpiece homology KEYWORDS actin binding; calcium binding; duplication FEATURE !$2-827 #product villin #status experimental #label MAT\ !$17-350 #domain gelsolin repeat homology #label GEL1\ !$398-715 #domain gelsolin repeat homology #label GEL2\ !$764-827 #domain villin headpiece homology #label VHH SUMMARY #length 827 #molecular-weight 92695 #checksum 5903 SEQUENCE /// ENTRY A31822 #type complete TITLE villin - chicken ALTERNATE_NAMES villin 1 ORGANISM #formal_name Gallus gallus #common_name chicken DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A31822; A25703; A03082; A42816 REFERENCE A31822 !$#authors Bazari, W.L.; Matsudaira, P.; Wallek, M.; Smeal, T.; Jakes, !1R.; Ahmed, Y. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:4986-4990 !$#title Villin sequence and peptide map identify six homologous !1domains. !$#cross-references MUID:88276884; PMID:2839826 !$#accession A31822 !'##molecule_type mRNA !'##residues 1-826 ##label BAZ !'##cross-references GB:J03781; NID:g212862; PIDN:AAA49133.1; !1PID:g212863 REFERENCE A91057 !$#authors Pringault, E.; Arpin, M.; Garcia, A.; Finidori, J.; Louvard, !1D. !$#journal EMBO J. (1986) 5:3119-3124 !$#title A human villin cDNA clone to investigate the differentiation !1of intestinal and kidney cells in vivo and in culture. !$#cross-references MUID:87133467; PMID:3453110 !$#accession A25703 !'##molecule_type mRNA !'##residues 751-826 ##label PRI REFERENCE A92333 !$#authors Glenney Jr., J.R.; Geisler, N.; Kaulfus, P.; Weber, K. !$#journal J. Biol. Chem. (1981) 256:8156-8161 !$#title Demonstration of at least two different actin-binding sites !1in villin, a calcium-regulated modulator of F-actin !1organization. !$#cross-references MUID:81264203; PMID:6790532 !$#accession A03082 !'##molecule_type protein !'##residues 751-826 ##label GLE REFERENCE A92418 !$#authors Hesterberg, L.K.; Weber, K. !$#journal J. Biol. Chem. (1983) 258:365-369 !$#title Demonstration of three distinct calcium-binding sites in !1villin, a modulator of actin assembly. !$#cross-references MUID:83082892; PMID:6848508 !$#contents annotation !$#note Gly-32, Asp-34, Ser-36, Lys-38, Asn-40, and Ser-43 may be !1involved in calcium binding REFERENCE A42816 !$#authors de Arruda, M.V.; Bazari, H.; Wallek, M.; Matsudaira, P. !$#journal J. Biol. Chem. (1992) 267:13079-13085 !$#title An actin footprint on villin. Single site substitutions in a !1cluster of basic residues inhibit the actin severing but not !1capping activity of villin. !$#cross-references MUID:92317005; PMID:1618806 !$#accession A42816 !'##status preliminary !'##molecule_type protein !'##residues 1-11;128-132 ##label DEA COMMENT Villin is abundant in the microvilli of intestinal !1epithelial cells and kidney proximal tubule cells. FUNCTION !$#description calcium-regulated actin-binding; in vitro, bundles actin at !1low Ca++ concentrations, severs and caps actin filaments at !1higher concentrations CLASSIFICATION #superfamily villin; gelsolin repeat homology; villin !1headpiece homology KEYWORDS actin binding; calcium binding; duplication FEATURE !$2-826 #product villin #status experimental #label MAT\ !$17-350 #domain gelsolin repeat homology #label GEL1\ !$17-49,398-430 #region repeats a, a'\ !$62-78,174-190, !$295-311,443-459, !$554-570,658-674 #region repeats b, c, d, b', c', d'\ !$398-715 #domain gelsolin repeat homology #label GEL2\ !$763-826 #domain villin headpiece homology #label VHH SUMMARY #length 826 #molecular-weight 92479 #checksum 2768 SEQUENCE /// ENTRY A39834 #type complete TITLE actin-capping protein gCap39 - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A39834 REFERENCE A39834 !$#authors Yu, F.X.; Johnston, P.A.; Suedhof, T.C.; Yin, H.L. !$#journal Science (1990) 250:1413-1415 !$#title gCap39, a calcium ion- and polyphosphoinositide-regulated !1actin capping protein. !$#cross-references MUID:91075231; PMID:2255912 !$#accession A39834 !'##status preliminary; nucleic acid sequence not shown; not compared !1with conceptual translation !'##molecule_type mRNA !'##residues 1-352 ##label YUA CLASSIFICATION #superfamily severin; gelsolin repeat homology KEYWORDS DNA binding; nucleus FEATURE !$19-352 #domain gelsolin repeat homology #label GEL SUMMARY #length 352 #molecular-weight 39240 #checksum 6279 SEQUENCE /// ENTRY A28517 #type complete TITLE severin - slime mold (Dictyostelium discoideum) ORGANISM #formal_name Dictyostelium discoideum DATE 31-Dec-1988 #sequence_revision 05-Aug-1994 #text_change 22-Jun-1999 ACCESSIONS A28517 REFERENCE A28517 !$#authors Andre, E.; Lottspeich, F.; Schleicher, M.; Noegel, A. !$#journal J. Biol. Chem. (1988) 263:722-727 !$#title Severin, gelsolin, and villin share a homologous sequence in !1regions presumed to contain F-actin severing domains. !$#cross-references MUID:88087190; PMID:2826459 !$#accession A28517 !'##molecule_type mRNA !'##residues 1-362 ##label AND !'##cross-references GB:J03515; NID:g167878; PIDN:AAA33250.1; !1PID:g167879 REFERENCE A37923 !$#authors Eichinger, L.; Noegel, A.A.; Schleicher, M. !$#journal J. Cell Biol. (1991) 112:665-676 !$#title Domain structure in actin-binding proteins: expression and !1functional characterization of truncated severin. !$#cross-references MUID:91131692; PMID:1847147 !$#contents annotation COMMENT Severin is a calcium-regulated, actin-modulating protein !1that binds to the plus (or barbed) ends of actin monomers or !1filaments, preventing monomer exchange (end-blocking or !1capping). It can promote assembly of monomers into filaments !1(nucleation) as well as disassociation (severing) of !1filaments already formed. COMMENT Both actin-binding regions are necessary for severin's !1nucleating and severing activities. CLASSIFICATION #superfamily severin; gelsolin repeat homology KEYWORDS actin binding; calcium FEATURE !$1-151 #region actin binding\ !$43-362 #domain gelsolin repeat homology #label GEL\ !$99-120 #region actin-capping\ !$152-262 #region actin binding SUMMARY #length 362 #molecular-weight 39870 #checksum 7683 SEQUENCE /// ENTRY A60424 #type complete TITLE calsequestrin precursor, fast skeletal muscle - human ALTERNATE_NAMES 58K dihydropyridine-binding protein; aspartactin; calmitine; laminin-binding protein ORGANISM #formal_name Homo sapiens #common_name man DATE 16-Jul-1999 #sequence_revision 16-Jul-1999 #text_change 20-Aug-1999 ACCESSIONS A60424; JC2449 REFERENCE A60424 !$#authors Fujii, J.; Willard, H.F.; MacLennan, D.H. !$#journal Somat. Cell Mol. Genet. (1990) 16:185-189 !$#title Characterization and localization to human chromosome 1 of !1human fast-twitch skeletal muscle calsequestrin gene. !$#cross-references MUID:90208531; PMID:2321095 !$#accession A60424 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-390 ##label FUJ REFERENCE JC2449 !$#authors Bataille, N.; Schmitt, N.; Aumercier-Maes, P.; Ollivier, B.; !1Lucas-Heron, B.; Lestienne, P. !$#journal Biochem. Biophys. Res. Commun. (1994) 203:1477-1482 !$#title Molecular cloning of human calmitine, a mitochondrial !1calcium binding protein, reveals identity with !1calsequestrine. !$#cross-references MUID:95032018; PMID:7945294 !$#accession JC2449 !'##molecule_type mRNA !'##residues 1-390 ##label BAT !'##cross-references GB:S73775; NID:g688291; PIDN:AAB32063.1; !1PID:g688292 !'##note the authors claim this protein is also found in the !1mitochondrion COMMENT Calsequestrin is a high-capacity and moderate-affinity !1calcium binding protein located in the luminal space of !1junctional sarcoplasmic reticulum. COMMENT Calsequestrin acts as a calcium buffer, and the release of !1calcium bound to calsequestrin through a calcium release !1channel triggers muscle contraction. COMMENT The fast skeletal muscle isoform of calsequestrin can be !1phosphorylated in vitro but contains only traces of !1phosphate when isolated from in vivo. GENETICS !$#gene GDB:CASQ1 !'##cross-references GDB:125180; OMIM:114250 !$#map_position 1q21-1q21 !$#introns 87/3; 116/1; 149/3; 187/1; 211/3; 255/2; 270/2; 289/1; 322/ !13; 347/3 !$#note protein is lacking in Duchenne and Becker patients as well !1as in dystrophic C57 BL 6j dy/dy mice CLASSIFICATION #superfamily calsequestrin KEYWORDS calcium binding; glycoprotein; skeletal muscle FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-28 #domain propeptide #status predicted #label PRO\ !$29-390 #product calsequestrin, fast skeletal muscle #status !8predicted #label MAT\ !$344 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 390 #molecular-weight 44581 #checksum 6834 SEQUENCE /// ENTRY A25887 #type complete TITLE calsequestrin precursor, fast skeletal muscle - rabbit ALTERNATE_NAMES 58K dihydropyridine-binding protein; aspartactin; calmitine; laminin-binding protein ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 16-Jul-1999 #sequence_revision 16-Jul-1999 #text_change 20-Aug-1999 ACCESSIONS A28142; A25887; A27499; A27433; B33409 REFERENCE A28142 !$#authors Zarain-Herzberg, A.; Fliegel, L.; MacLennan, D.H. !$#journal J. Biol. Chem. (1988) 263:4807-4812 !$#title Structure of the rabbit fast-twitch skeletal muscle !1calsequestrin gene. !$#cross-references MUID:88169601; PMID:2832408 !$#accession A28142 !'##molecule_type DNA !'##residues 1-395 ##label ZAR !'##cross-references GB:M20142; GB:J03181 REFERENCE A25887 !$#authors Fliegel, L.; Ohnishi, M.; Carpenter, M.R.; Khanna, V.K.; !1Reithmeier, R.A.F.; MacLennan, D.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:1167-1171 !$#title Amino acid sequence of rabbit fast-twitch skeletal muscle !1calsequestrin deduced from cDNA and peptide sequencing. !$#cross-references MUID:87147234; PMID:3469659 !$#accession A25887 !'##molecule_type mRNA !'##residues 1-395 ##label FLI !'##cross-references GB:M15747; NID:g164841; PIDN:AAA31184.1; !1PID:g164842 REFERENCE A90520 !$#authors Slupsky, J.R.; Ohnishi, M.; Carpenter, M.R.; Reithmeier, !1R.A.F. !$#journal Biochemistry (1987) 26:6539-6544 !$#title Characterization of cardiac calsequestrin. !$#cross-references MUID:88107564; PMID:3427023 !$#accession A27499 !'##molecule_type protein !'##residues 29-69,'XXX',73-85,'X',87 ##label SLU REFERENCE A27433 !$#authors Ohnishi, M.; Reithmeier, R.A.F. !$#journal Biochemistry (1987) 26:7458-7465 !$#title Fragmentation of rabbit skeletal muscle calsequestrin: !1spectral and ion binding properties of the carboxyl-terminal !1region. !$#cross-references MUID:88107697; PMID:3427087 !$#accession A27433 !'##molecule_type protein !'##residues 330-386,388,'E' ##label OHN !'##experimental_source skeletal muscle REFERENCE A33409 !$#authors Hamilton, S.L.; Hawkes, M.J.; Brush, K.; Cook, R. !$#journal Biochemistry (1989) 28:7820-7828 !$#title Subunit composition of the purified dihydropyridine binding !1protein from skeletal muscle. !$#cross-references MUID:90122765; PMID:2558713 !$#accession B33409 !'##status preliminary !'##molecule_type protein !'##residues 29-69,'K',71-75 ##label HAM COMMENT Calsequestrin is a high-capacity and moderate-affinity !1calcium binding protein located in the luminal space of !1junctional sarcoplasmic reticulum. COMMENT Calsequestrin acts as a calcium buffer, and the release of !1calcium bound to calsequestrin through a calcium release !1channel triggers muscle contraction. COMMENT The fast skeletal muscle isoform of calsequestrin can be !1phosphorylated in vitro but contains only traces of !1phosphate when isolated from in vivo. CLASSIFICATION #superfamily calsequestrin KEYWORDS calcium binding; glycoprotein; skeletal muscle FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-28 #domain propeptide #status predicted #label PRO\ !$29-395 #product calsequestrin, fast skeletal muscle #status !8experimental #label MAT\ !$344 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 395 #molecular-weight 45262 #checksum 3963 SEQUENCE /// ENTRY S22418 #type complete TITLE calsequestrin precursor, skeletal muscle - edible frog ALTERNATE_NAMES 58K dihydropyridine-binding protein; aspartactin; calmitine; laminin-binding protein ORGANISM #formal_name Rana esculenta #common_name edible frog DATE 16-Jul-1999 #sequence_revision 16-Jul-1999 #text_change 20-Aug-1999 ACCESSIONS S22418 REFERENCE S22418 !$#authors Treves, S.; Vilsen, B.; Chiozzi, P.; Andersen, J.P.; !1Zorzato, F. !$#journal Biochem. J. (1992) 283:767-772 !$#title Molecular cloning, functional expression and tissue !1distribution of the cDNA encoding frog skeletal muscle !1calsequestrin. !$#cross-references MUID:92272676; PMID:1375450 !$#accession S22418 !'##status preliminary !'##molecule_type mRNA !'##residues 1-420 ##label TRE !'##cross-references EMBL:X64324; NID:g64276; PIDN:CAA45609.1; !1PID:g64277 COMMENT Calsequestrin is a high-capacity and moderate-affinity !1calcium binding protein located in the luminal space of !1junctional sarcoplasmic reticulum. COMMENT Calsequestrin acts as a calcium buffer, and the release of !1calcium bound to calsequestrin through a calcium release !1channel triggers muscle contraction. COMMENT The fast skeletal muscle isoform of calsequestrin can be !1phosphorylated in vitro but contains only traces of !1phosphate when isolated from in vivo. CLASSIFICATION #superfamily calsequestrin KEYWORDS calcium binding; glycoprotein; skeletal muscle FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-28 #domain propeptide #status predicted #label PRO\ !$23-420 #product calsequestrin, fast skeletal muscle #status !8predicted #label MAT\ !$338 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 420 #molecular-weight 48204 #checksum 176 SEQUENCE /// ENTRY A31050 #type complete TITLE calsequestrin precursor, cardiac and skeletal muscle - chicken ALTERNATE_NAMES 58K dihydropyridine-binding protein; aspartactin; calmitine; laminin-binding protein ORGANISM #formal_name Gallus gallus #common_name chicken DATE 16-Jul-1999 #sequence_revision 16-Jul-1999 #text_change 20-Aug-1999 ACCESSIONS A31050; B31049; A35709; A34652 REFERENCE A31050 !$#authors Clegg, D.O.; Helder, J.C.; Hann, B.C.; Hall, D.E.; !1Reichardt, L.F. !$#journal J. Cell Biol. (1988) 107:699-705 !$#title Amino acid sequence and distribution of mRNA encoding a !1major skeletal muscle laminin binding protein: an !1extracellular matrix-associated protein with an unusual !1COOH-terminal polyaspartate domain. !$#cross-references MUID:88331074; PMID:3417769 !$#accession A31050 !'##molecule_type mRNA !'##residues 1-406 ##label CLE !'##cross-references EMBL:Y00789; NID:g63561; PIDN:CAA68743.1; !1PID:g63562 REFERENCE A92751 !$#authors Hall, D.E.; Frazer, K.A.; Hann, B.C.; Reichardt, L.F. !$#journal J. Cell Biol. (1988) 107:687-697 !$#title Isolation and characterization of a laminin-binding protein !1from rat and chick muscle. !$#cross-references MUID:88331073; PMID:3417768 !$#accession B31049 !'##molecule_type protein !'##residues 20-39 ##label HAL REFERENCE A35709 !$#authors Yazaki, P.J.; Salvatori, S.; Dahms, A.S. !$#journal Biochem. Biophys. Res. Commun. (1990) 170:1089-1095 !$#title Amino acid sequence of chicken calsequestrin deduced from c !1DNA: comparison of calsequestrin and aspartactin. !$#cross-references MUID:90358803; PMID:2390076 !$#accession A35709 !'##status preliminary !'##molecule_type mRNA !'##residues 20-147,'I',149-406 ##label YAZ !'##cross-references GB:M58048; NID:g211496; PIDN:AAA48674.1; !1PID:g211497 REFERENCE A34652 !$#authors Yazaki, P.J.; Salvatori, S.; Sabbadini, R.A.; Dahms, A.S. !$#journal Biochem. Biophys. Res. Commun. (1990) 166:898-903 !$#title Calsequestrin, and intracellular calcium-binding protein of !1skeletal muscle sarcoplasmic reticulum, is homologous to !1aspartactin, a putative laminin-binding protein of the !1extracellular matrix. !$#cross-references MUID:90147805; PMID:2302244 !$#accession A34652 !'##status preliminary !'##molecule_type protein !'##residues 20-39 ##label YA2 COMMENT Calsequestrin is a high-capacity and moderate-affinity !1calcium binding protein located in the luminal space of !1junctional sarcoplasmic reticulum. COMMENT Calsequestrin acts as a calcium buffer, and the release of !1calcium bound to calsequestrin through a calcium release !1channel triggers muscle contraction. CLASSIFICATION #superfamily calsequestrin KEYWORDS calcium binding; cardiac muscle; glycoprotein; heart; !1skeletal muscle FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-406 #product calsequestrin, cardiac and skeletal muscle !8#status experimental #label MAT\ !$335 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 406 #molecular-weight 47151 #checksum 8209 SEQUENCE /// ENTRY JQ1396 #type complete TITLE calsequestrin precursor, cardiac and slow skeletal muscle - rabbit ALTERNATE_NAMES 58K dihydropyridine-binding protein; aspartactin; calmitine; laminin-binding protein ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 16-Jul-1999 #sequence_revision 16-Jul-1999 #text_change 20-Aug-1999 ACCESSIONS JQ1396; D27499; S20113 REFERENCE JQ1396 !$#authors Arai, M.; Alpert, N.R.; Periasamy, M. !$#journal Gene (1991) 109:275-279 !$#title Cloning and characterization of the gene encoding rabbit !1cardiac calsequestrin. !$#cross-references MUID:92112055; PMID:1662658 !$#accession JQ1396 !'##molecule_type mRNA !'##residues 1-409 ##label ARA !'##cross-references EMBL:X55040; NID:g1511; PIDN:CAA38880.1; PID:g1512 REFERENCE A90520 !$#authors Slupsky, J.R.; Ohnishi, M.; Carpenter, M.R.; Reithmeier, !1R.A.F. !$#journal Biochemistry (1987) 26:6539-6544 !$#title Characterization of cardiac calsequestrin. !$#cross-references MUID:88107564; PMID:3427023 !$#accession D27499 !'##molecule_type protein !'##residues 20-44,'S',46-49 ##label SLU COMMENT Calsequestrin is a high-capacity and moderate-affinity !1calcium binding protein located in the luminal space of !1junctional sarcoplasmic reticulum. COMMENT Calsequestrin acts as a calcium buffer, and the release of !1calcium bound to calsequestrin through a calcium release !1channel triggers muscle contraction. CLASSIFICATION #superfamily calsequestrin KEYWORDS calcium binding; cardiac muscle; glycoprotein; heart; !1phosphoprotein; skeletal muscle FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-409 #product calsequestrin, cardiac and slow skeletal !8muscle #status predicted #label MAT\ !$335 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$396,404 #binding_site phosphate (Ser) (covalent) (by casein !8kinase II) #status predicted SUMMARY #length 409 #molecular-weight 47356 #checksum 7967 SEQUENCE /// ENTRY A28071 #type complete TITLE calsequestrin precursor, cardiac and slow skeletal muscle - dog ALTERNATE_NAMES 58K dihydropyridine-binding protein; aspartactin; calmitine; laminin-binding protein ORGANISM #formal_name Canis lupus familiaris #common_name dog DATE 16-Jul-1999 #sequence_revision 16-Jul-1999 #text_change 20-Aug-1999 ACCESSIONS A28071; C27499 REFERENCE A92724 !$#authors Scott, B.T.; Simmerman, H.K.B.; Collins, J.H.; Nadal-Ginard, !1B.; Jones, L.R. !$#journal J. Biol. Chem. (1988) 263:8958-8964 !$#title Complete amino acid sequence of canine cardiac calsequestrin !1deduced by cDNA cloning. !$#cross-references MUID:88243763; PMID:3379055 !$#accession A28071 !'##molecule_type mRNA !'##residues 1-410 ##label SCO !'##cross-references GB:J03766; NID:g163914; PIDN:AAA30833.1; !1PID:g163915 REFERENCE A90520 !$#authors Slupsky, J.R.; Ohnishi, M.; Carpenter, M.R.; Reithmeier, !1R.A.F. !$#journal Biochemistry (1987) 26:6539-6544 !$#title Characterization of cardiac calsequestrin. !$#cross-references MUID:88107564; PMID:3427023 !$#accession C27499 !'##molecule_type protein !'##residues 20-52,'X',54,'XXX',58,'X',60,'XXX',64,'X',66-70,'E' ##label !1SLU COMMENT Calsequestrin is a high-capacity and moderate-affinity !1calcium binding protein located in the luminal space of !1junctional sarcoplasmic reticulum. COMMENT Calsequestrin acts as a calcium buffer, and the release of !1calcium bound to calsequestrin through a calcium release !1channel triggers muscle contraction. CLASSIFICATION #superfamily calsequestrin KEYWORDS calcium binding; cardiac muscle; glycoprotein; heart; !1phosphoprotein; skeletal muscle FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-410 #product calsequestrin, cardiac and slow skeletal !8muscle #status experimental #label MAT\ !$335 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$397,405 #binding_site phosphate (Ser) (covalent) (by casein !8kinase II) #status predicted SUMMARY #length 410 #molecular-weight 47416 #checksum 7939 SEQUENCE /// ENTRY TPHUCS #type complete TITLE troponin C, fast skeletal muscle [validated] - human ALTERNATE_NAMES troponin C2 ORGANISM #formal_name Homo sapiens #common_name man DATE 27-Nov-1985 #sequence_revision 03-Oct-1995 #text_change 08-Dec-2000 ACCESSIONS A36574; B29990; A03012 REFERENCE A36574 !$#authors Gahlmann, R.; Kedes, L. !$#journal J. Biol. Chem. (1990) 265:12520-12528 !$#title Cloning, structural analysis, and expression of the human !1fast twitch skeletal muscle troponin C gene. !$#cross-references MUID:90324243; PMID:2373703 !$#accession A36574 !'##molecule_type DNA !'##residues 1-160 ##label GAH !'##cross-references GB:M33771; GB:M33772; NID:g339734; PIDN:AAA61197.1; !1PID:g339736 REFERENCE A29990 !$#authors Gahlmann, R.; Wade, R.; Gunning, P.; Kedes, L. !$#journal J. Mol. Biol. (1988) 201:379-391 !$#title Differential expression of slow and fast skeletal muscle !1troponin C. Slow skeletal muscle troponin C is expressed in !1human fibroblasts. !$#cross-references MUID:88332973; PMID:3166492 !$#accession B29990 !'##molecule_type mRNA !'##residues 1-160 ##label GA2 !'##cross-references GB:X07898; NID:g36728; PIDN:CAA30737.1; PID:g36729 REFERENCE A03012 !$#authors Romero-Herrera, A.E.; Castillo, O.; Lehmann, H. !$#journal J. Mol. Evol. (1976) 8:251-270 !$#title Human skeletal muscle proteins. The primary structure of !1troponin C. !$#cross-references MUID:77031728; PMID:978749 !$#accession A03012 !'##molecule_type protein !'##residues 'DT',4-160 ##label ROM COMMENT One molecule of fast skeletal muscle troponin C binds four !1calcium ions. GENETICS !$#gene GDB:TNNC2 !'##cross-references GDB:578903; OMIM:191039 !$#map_position 3p21.3-3p14.3 !$#introns 1/3; 19/1; 67/1; 105/2 151/1 COMPLEX troponin is a heterotrimer with one molecule each of !1troponin C (calcium binding component), troponin I !1(inhibitory component), and troponin T (tropomyosin-binding !1component) FUNCTION !$#description binds calcium and relieves the inhibition of myosin ATPase !1by troponin I; with tropomyosin mediates contraction of !1vertebrate striated muscle in response to calcium !$#pathway muscle contraction CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS blocked amino end; calcium binding; duplication; EF hand; !1muscle contraction; skeletal muscle; thin filaments FEATURE !$2-160 #product troponin C, fast skeletal muscle #status !8experimental #label MAT\ !$15-47 #domain calmodulin repeat homology #label EF1\ !$51-83 #domain calmodulin repeat homology #label EF2\ !$91-123 #domain calmodulin repeat homology #label EF3\ !$127-159 #domain calmodulin repeat homology #label EF4\ !$2 #modified_site blocked amino end (Thr) (in mature !8form) (probably acetylated) #status experimental\ !$28,30,32,34,39 #binding_site calcium (Asp, Asp, Gly, Asp, Glu) !8#status predicted\ !$64,66,68,70,75 #binding_site calcium (Asp, Asp, Ser, Thr, Glu) !8#status predicted\ !$104,106,108,110,115 #binding_site calcium (Asp, Asn, Asp, Tyr, Glu) !8#status predicted\ !$140,142,144,146,151 #binding_site calcium (Asp, Asn, Asp, Arg, Glu) !8#status predicted SUMMARY #length 160 #molecular-weight 18122 #checksum 4698 SEQUENCE /// ENTRY TPRBCS #type complete TITLE troponin C, fast skeletal muscle - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 30-Nov-1980 #sequence_revision 03-Oct-1995 #text_change 22-Jun-1999 ACCESSIONS A28442; S00309; A03013; A49728; I46510 REFERENCE A28442 !$#authors Zot, A.S.; Potter, J.D.; Strauss, W.L. !$#journal J. Biol. Chem. (1987) 262:15418-15421 !$#title Isolation and sequence of a cDNA clone for rabbit fast !1skeletal muscle troponin C. Homology with calmodulin and !1parvalbumin. !$#cross-references MUID:88058870; PMID:3680204 !$#accession A28442 !'##molecule_type mRNA !'##residues 1-160 ##label ZOT !'##cross-references GB:J03462; NID:g165746; PIDN:AAA31481.1; !1PID:g165747 !'##experimental_source neonatal skeletal muscle REFERENCE S00309 !$#authors Chen, Q.; Taljanidisz, J.; Sarkar, S.; Tao, T.; Gergely, J. !$#journal FEBS Lett. (1988) 228:22-26 !$#title Cloning, sequencing and expression of a full-length rabbit !1fast skeletal troponin-C cDNA. !$#cross-references MUID:88137596; PMID:3277860 !$#accession S00309 !'##molecule_type mRNA !'##residues 1-160 ##label CHE !'##cross-references EMBL:Y00760; NID:g1754; PIDN:CAA68729.1; PID:g1755 REFERENCE A03013 !$#authors Collins, J.H.; Greaser, M.L.; Potter, J.D.; Horn, M.J. !$#journal J. Biol. Chem. (1977) 252:6356-6362 !$#title Determination of the amino acid sequence of troponin C from !1rabbit skeletal muscle. !$#accession A03013 !'##molecule_type protein !'##residues 'DT',4-160 ##label COL REFERENCE A49728 !$#authors Ngai, S.M.; Soennichsen, F.D.; Hodges, R.S. !$#journal J. Biol. Chem. (1994) 269:2165-2172 !$#title Photochemical cross-linking between native rabbit skeletal !1troponin C and benzoylbenzoyl-troponin I inhibitory peptide, !1residues 104-115. !$#cross-references MUID:94124574; PMID:8294472 !$#accession A49728 !'##molecule_type protein !'##residues 90-101;155-160 ##label NGA REFERENCE I46471 !$#authors Putney, S.D.; Herlihy, W.C.; Schimmel, P. !$#journal Nature (1983) 302:718-721 !$#title A new troponin T and cDNA clones for 13 different muscle !1proteins, found by shotgun sequencing. !$#cross-references MUID:83167564; PMID:6687628 !$#accession I46510 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 74-103 ##label PUT !'##cross-references EMBL:V00894; NID:g1730; PIDN:CAA24259.1; !1PID:g929764 COMMENT One molecule of fast skeletal muscle troponin C binds four !1calcium ions. COMPLEX troponin is a heterotrimer with one molecule each of !1troponin C (calcium binding component), troponin I !1(inhibitory component), and troponin T (tropomyosin-binding !1component) FUNCTION !$#description binds calcium and relieves the inhibition of myosin ATPase !1by troponin I; with tropomyosin mediates contraction of !1vertebrate striated muscle in response to calcium !$#pathway muscle contraction CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS acetylated amino end; calcium binding; duplication; EF hand; !1muscle contraction; skeletal muscle; thin filaments FEATURE !$2-160 #product troponin C, fast skeletal muscle #status !8experimental #label MAT\ !$15-47 #domain calmodulin repeat homology #label EF1\ !$51-83 #domain calmodulin repeat homology #label EF2\ !$91-123 #domain calmodulin repeat homology #label EF3\ !$127-159 #domain calmodulin repeat homology #label EF4\ !$2 #modified_site acetylated amino end (Thr) (in mature !8form) #status experimental\ !$28,30,32,34,39 #binding_site calcium (Asp, Asp, Gly, Asp, Glu) !8#status predicted\ !$64,66,68,70,75 #binding_site calcium (Asp, Asp, Ser, Thr, Glu) !8#status predicted\ !$104,106,108,110,115 #binding_site calcium (Asp, Asn, Asp, Tyr, Glu) !8#status predicted\ !$140,142,144,146,151 #binding_site calcium (Asp, Asn, Asp, Arg, Glu) !8#status predicted SUMMARY #length 160 #molecular-weight 18096 #checksum 3858 SEQUENCE /// ENTRY TPPGCS #type complete TITLE troponin C, skeletal muscle - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 17-Apr-1998 ACCESSIONS A03014 REFERENCE A03014 !$#authors Lorkin, P.A.; Lehmann, H. !$#journal FEBS Lett. (1983) 153:81-87 !$#title Malignant hyperthermia in pigs: a search for abnormalities !1in Ca(2+) binding proteins. !$#cross-references MUID:83132407; PMID:6825863 !$#accession A03014 !'##molecule_type protein !'##residues 1-159 ##label LOR COMPLEX troponin is a heterotrimer with one molecule each of !1troponin C (calcium binding component), troponin I !1(inhibitory component), and troponin T (tropomyosin-binding !1component) FUNCTION !$#description binds calcium and relieves the inhibition of myosin ATPase !1by troponin I; with tropomyosin mediates contraction of !1vertebrate striated muscle in response to calcium !$#pathway muscle contraction CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS calcium binding; duplication; EF hand; muscle contraction; !1thin filaments FEATURE !$14-46 #domain calmodulin repeat homology #label EF1\ !$50-82 #domain calmodulin repeat homology #label EF2\ !$90-122 #domain calmodulin repeat homology #label EF3\ !$126-158 #domain calmodulin repeat homology #label EF4\ !$27,29,31,33,38 #binding_site calcium (Asp, Asp, Gly, Asp, Glu) !8#status predicted\ !$63,65,67,69,74 #binding_site calcium (Asp, Asp, Ser, Thr, Glu) !8#status predicted\ !$103,105,107,109,114 #binding_site calcium (Asp, Asn, Asp, Tyr, Glu) !8#status predicted\ !$139,141,143,145,150 #binding_site calcium (Asp, Asn, Asp, Arg, Glu) !8#status predicted SUMMARY #length 159 #molecular-weight 18025 #checksum 253 SEQUENCE /// ENTRY TPCHCS #type complete TITLE troponin C, skeletal muscle - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 24-Apr-1984 #sequence_revision 30-Jun-1992 #text_change 24-Nov-1999 ACCESSIONS A03015; A28362; B40803 REFERENCE A03015 !$#authors Wilkinson, J.M. !$#journal FEBS Lett. (1976) 70:254-256 !$#title The amino acid sequence of troponin C from chicken skeletal !1muscle. !$#cross-references MUID:77048905; PMID:992069 !$#accession A03015 !'##molecule_type protein !'##residues 'SA',4-100,'D',102-163 ##label WIL !'##note the order of residues 2-5 was not determined REFERENCE A28362 !$#authors Reinach, F.C.; Karlsson, R. !$#journal J. Biol. Chem. (1988) 263:2371-2376 !$#title Cloning, expression, and site-directed mutagenesis of !1chicken skeletal muscle troponin C. !$#cross-references MUID:88115383; PMID:2963002 !$#accession A28362 !'##molecule_type mRNA !'##residues 1-130,'I',132-163 ##label REI !'##cross-references GB:M19027; NID:g212777; PIDN:AAA49097.1; !1PID:g212778 REFERENCE A40803 !$#authors Golosinska, K.; Pearlstone, J.R.; Borgford, T.; Oikawa, K.; !1Kay, C.M.; Carpenter, M.R.; Smillie, L.B. !$#journal J. Biol. Chem. (1991) 266:15797-15809 !$#title Determination of and corrections to sequences of turkey and !1chicken troponins-C. Effects of Thr-130 to Ile mutation on !1Ca(2+) affinity. !$#cross-references MUID:91340719; PMID:1908459 !$#accession B40803 !'##molecule_type protein !'##residues 88-133,'E',135-139 ##label GOL COMMENT The X-ray crystallographic structure of chicken troponin C !1is a dumbbell of two globular domains attached by a long !1alpha helix. The N-terminal domain binds two cations of !1calcium, while the C-terminal domain binds two cations of !1calcium or magnesium. COMPLEX troponin is a heterotrimer with one molecule each of !1troponin C (calcium binding component), troponin I !1(inhibitory component), and troponin T (tropomyosin-binding !1component) FUNCTION !$#description binds calcium and relieves the inhibition of myosin ATPase !1by troponin I; with tropomyosin mediates contraction of !1vertebrate striated muscle in response to calcium !$#pathway muscle contraction CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS blocked amino end; calcium binding; EF hand FEATURE !$18-50 #domain calmodulin repeat homology #label EF1\ !$54-86 #domain calmodulin repeat homology #label EF2\ !$94-126 #domain calmodulin repeat homology #label EF3\ !$130-162 #domain calmodulin repeat homology #label EF4\ !$2 #modified_site blocked amino end (Ala) (in mature !8form) #status experimental SUMMARY #length 163 #molecular-weight 18375 #checksum 4204 SEQUENCE /// ENTRY A40803 #type complete TITLE troponin C, skeletal muscle [validated] - turkey ORGANISM #formal_name Meleagris gallopavo #common_name common turkey DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 15-Sep-2000 ACCESSIONS A40803 REFERENCE A40803 !$#authors Golosinska, K.; Pearlstone, J.R.; Borgford, T.; Oikawa, K.; !1Kay, C.M.; Carpenter, M.R.; Smillie, L.B. !$#journal J. Biol. Chem. (1991) 266:15797-15809 !$#title Determination of and corrections to sequences of turkey and !1chicken troponins-C. Effects of Thr-130 to Ile mutation on !1Ca(2+) affinity. !$#cross-references MUID:91340719; PMID:1908459 !$#accession A40803 !'##molecule_type protein !'##residues 1-162 ##label GOL REFERENCE A50746 !$#authors Herzberg, O.; James, M.N.G. !$#submission submitted to the Brookhaven Protein Data Bank, May 1988 !$#cross-references PDB:5TNC !$#contents annotation; X-ray crystallography, 2.0 angstroms, residues !12-98,'ED',101-132,'D',134-162 REFERENCE A58790 !$#authors Herzberg, O.; James, M.N.G. !$#journal J. Mol. Biol. (1988) 203:761-779 !$#title Refined crystal structure of troponin C from turkey skeletal !1muscle at 2.0 Angstroms resolution. !$#cross-references MUID:89094842; PMID:3210231 !$#contents annotation; X-ray crystallography, 2.0 angstroms REFERENCE A52687 !$#authors Findlay, W.A.; Soennichsen, F.D.; Sykes, B.D. !$#submission submitted to the Brookhaven Protein Data Bank, December 1993 !$#cross-references PDB:1TRF !$#contents annotation; conformation by (1)H-NMR, residues 12-87 REFERENCE A58791 !$#authors Findlay, W.A.; Soennichsen, F.D.; Sykes, B.D. !$#journal J. Biol. Chem. (1994) 269:6773-6778 !$#title Solution structure of the TR1C fragment of skeletal muscle !1troponin-C. !$#cross-references MUID:94165075; PMID:8120037 !$#contents annotation; conformation by (1)H-NMR, residues 12-87 COMMENT This troponin C is unusual in that its amino end is not !1blocked. COMPLEX troponin is a heterotrimer with one molecule each of !1troponin C (calcium binding component), troponin I !1(inhibitory component), and troponin T (tropomyosin-binding !1component) FUNCTION !$#description binds calcium and relieves the inhibition of myosin ATPase !1by troponin I; with tropomyosin mediates contraction of !1vertebrate striated muscle in response to calcium !$#pathway muscle contraction CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS calcium binding; EF hand; skeletal muscle FEATURE !$17-49 #domain calmodulin repeat homology #label EF1\ !$53-85 #domain calmodulin repeat homology #label EF2\ !$93-125 #domain calmodulin repeat homology #label EF3\ !$129-161 #domain calmodulin repeat homology #label EF4\ !$30,32,34,36,41 #binding_site calcium, low affinity (Asp, Asp, Gly, !8Asp, Glu) #status predicted\ !$66,68,70,72,77 #binding_site calcium, low affinity (Asp, Asp, Ser, !8Thr, Glu) #status predicted\ !$106,108,110,112,117 #binding_site calcium, high affinity (Asp, Asn, Asp, !8Phe, Glu) #status experimental\ !$142,144,146,148,153 #binding_site calcium, high affinity (Asp, Asn, Asp, !8Arg, Glu) #status experimental SUMMARY #length 162 #molecular-weight 18284 #checksum 79 SEQUENCE /// ENTRY TPFGCS #type complete TITLE troponin C, skeletal muscle - edible frog (tentative sequence) ORGANISM #formal_name Rana esculenta #common_name edible frog DATE 01-Sep-1981 #sequence_revision 01-Sep-1981 #text_change 31-Mar-2000 ACCESSIONS A03016 REFERENCE A03016 !$#authors van Eerd, J.P.; Capony, J.P.; Ferraz, C.; Pechere, J.F. !$#journal Eur. J. Biochem. (1978) 91:231-242 !$#title The amino-acid sequence of troponin C from frog skeletal !1muscle. !$#cross-references MUID:79065043; PMID:309817 !$#accession A03016 !'##molecule_type protein !'##residues 1-162 ##label VAN COMPLEX troponin is a heterotrimer with one molecule each of !1troponin C (calcium binding component), troponin I !1(inhibitory component), and troponin T (tropomyosin-binding !1component) FUNCTION !$#description binds calcium and relieves the inhibition of myosin ATPase !1by troponin I; with tropomyosin mediates contraction of !1vertebrate striated muscle in response to calcium !$#pathway muscle contraction CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS acetylated amino end; calcium binding; EF hand FEATURE !$17-49 #domain calmodulin repeat homology #label EF1\ !$53-85 #domain calmodulin repeat homology #label EF2\ !$93-125 #domain calmodulin repeat homology #label EF3\ !$129-161 #domain calmodulin repeat homology #label EF4\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental SUMMARY #length 162 #molecular-weight 18257 #checksum 1716 SEQUENCE /// ENTRY TPHUCC #type complete TITLE troponin C, cardiac and slow skeletal muscle - human ALTERNATE_NAMES troponin C1 ORGANISM #formal_name Homo sapiens #common_name man DATE 17-Mar-1987 #sequence_revision 03-Oct-1995 #text_change 16-Jul-1999 ACCESSIONS A38341; A29990; A03017 REFERENCE A38341 !$#authors Schreier, T.; Kedes, L.; Gahlmann, R. !$#journal J. Biol. Chem. (1990) 265:21247-21253 !$#title Cloning, structural analysis, and expression of the human !1slow twitch skeletal muscle/cardiac troponin C gene. !$#cross-references MUID:91065942; PMID:2250022 !$#accession A38341 !'##molecule_type DNA !'##residues 1-161 ##label SCH !'##cross-references GB:M37984; NID:g339945; PIDN:AAA36772.1; !1PID:g339946 REFERENCE A29990 !$#authors Gahlmann, R.; Wade, R.; Gunning, P.; Kedes, L. !$#journal J. Mol. Biol. (1988) 201:379-391 !$#title Differential expression of slow and fast skeletal muscle !1troponin C. Slow skeletal muscle troponin C is expressed in !1human fibroblasts. !$#cross-references MUID:88332973; PMID:3166492 !$#accession A29990 !'##molecule_type mRNA !'##residues 1-161 ##label GAH !'##cross-references GB:X07897; NID:g37207; PIDN:CAA30736.1; PID:g37208 !'##note this protein was also detected in cultured fibroblasts REFERENCE A03017 !$#authors Roher, A.; Lieska, N.; Spitz, W. !$#journal Muscle Nerve (1986) 9:73-77 !$#title The amino acid sequence of human cardiac troponin-C. !$#cross-references MUID:86146728; PMID:3951483 !$#accession A03017 !'##molecule_type protein !'##residues 1-114,'E',116-161 ##label ROH !'##experimental_source ventricular muscle COMMENT One molecule of cardiac muscle troponin C binds three !1calcium ions. GENETICS !$#gene GDB:TNNC1; TNNC !'##cross-references GDB:125307; OMIM:191040 !$#map_position 3p21.3-3p14.3 !$#introns 8/3; 19/1; 68/1; 106/2; 152/1 COMPLEX troponin is a heterotrimer with one molecule each of !1troponin C (calcium binding component), troponin I !1(inhibitory component), and troponin T (tropomyosin-binding !1component) FUNCTION !$#description binds calcium and relieves the inhibition of myosin ATPase !1by troponin I; with tropomyosin mediates contraction of !1vertebrate striated muscle in response to calcium !$#pathway muscle contraction CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS blocked amino end; calcium binding; cardiac muscle; !1duplication; EF hand; heart; muscle contraction; thin !1filaments FEATURE !$15-48 #domain calmodulin repeat homology #label EF1\ !$52-84 #domain calmodulin repeat homology #label EF2\ !$92-124 #domain calmodulin repeat homology #label EF3\ !$128-160 #domain calmodulin repeat homology #label EF4\ !$1 #modified_site blocked amino end (Met) (probably !8acetylated) #status experimental\ !$65,67,69,71,76 #binding_site calcium (Asp, Asp, Ser, Thr, Glu) !8#status predicted\ !$105,107,109,111,116 #binding_site calcium (Asp, Asn, Asp, Tyr, Glu) !8#status predicted\ !$141,143,145,147,152 #binding_site calcium (Asp, Asn, Asp, Arg, Glu) !8#status predicted SUMMARY #length 161 #molecular-weight 18402 #checksum 9494 SEQUENCE /// ENTRY TPBOCC #type complete TITLE troponin C, cardiac muscle - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 16-Jul-1999 ACCESSIONS A03018 REFERENCE A03018 !$#authors van Eerd, J.P.; Takahashi, K. !$#journal Biochemistry (1976) 15:1171-1180 !$#title Determination of the complete amino acid sequence of bovine !1cardiac troponin C. !$#cross-references MUID:76136387; PMID:1252434 !$#accession A03018 !'##molecule_type protein !'##residues 1-161 ##label VAN COMPLEX troponin is a heterotrimer with one molecule each of !1troponin C (calcium binding component), troponin I !1(inhibitory component), and troponin T (tropomyosin-binding !1component) FUNCTION !$#description binds calcium and relieves the inhibition of myosin ATPase !1by troponin I; with tropomyosin mediates contraction of !1vertebrate striated muscle in response to calcium !$#pathway muscle contraction CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS acetylated amino end; calcium binding; cardiac muscle; EF !1hand; heart FEATURE !$15-48 #domain calmodulin repeat homology #label EF1\ !$52-84 #domain calmodulin repeat homology #label EF2\ !$92-124 #domain calmodulin repeat homology #label EF3\ !$128-160 #domain calmodulin repeat homology #label EF4\ !$1 #modified_site acetylated amino end (Met) #status !8experimental SUMMARY #length 161 #molecular-weight 18416 #checksum 9495 SEQUENCE /// ENTRY TPRBCW #type complete TITLE troponin C, cardiac and slow skeletal muscle - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 02-Apr-1982 #sequence_revision 02-Apr-1982 #text_change 24-Nov-1999 ACCESSIONS A03019 REFERENCE A03019 !$#authors Wilkinson, J.M. !$#journal Eur. J. Biochem. (1980) 103:179-188 !$#title Troponin C from rabbit slow skeltal and cardiac muscle is !1the product of a single gene. !$#cross-references MUID:80134219; PMID:7358047 !$#accession A03019 !'##molecule_type protein !'##residues 1-161 ##label WIL !'##experimental_source slow skeletal muscle !'##note the cardiac muscle and slow skeletal muscle proteins appear to !1be identical and to differ from the bovine cardiac muscle !1troponin C at only one position COMPLEX troponin is a heterotrimer with one molecule each of !1troponin C (calcium binding component), troponin I !1(inhibitory component), and troponin T (tropomyosin-binding !1component) FUNCTION !$#description binds calcium and relieves the inhibition of myosin ATPase !1by troponin I; with tropomyosin mediates contraction of !1vertebrate striated muscle in response to calcium !$#pathway muscle contraction CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS blocked amino end; calcium binding; cardiac muscle; EF hand; !1heart FEATURE !$15-48 #domain calmodulin repeat homology #label EF1\ !$52-84 #domain calmodulin repeat homology #label EF2\ !$92-124 #domain calmodulin repeat homology #label EF3\ !$128-160 #domain calmodulin repeat homology #label EF4\ !$1 #modified_site blocked amino end (Met) (probably !8acetylated) #status experimental SUMMARY #length 161 #molecular-weight 18402 #checksum 9494 SEQUENCE /// ENTRY S22971 #type complete TITLE calmodulin - trumpet lily ORGANISM #formal_name Lilium longiflorum #common_name trumpet lily DATE 17-Mar-1994 #sequence_revision 11-Apr-1997 #text_change 22-Jun-1999 ACCESSIONS S22971 REFERENCE S22860 !$#authors Choi, Y.; Kim, S.; Poovaiah, B.W.; An, G. !$#submission submitted to the EMBL Data Library, June 1992 !$#description Structural organization of monocot calmodulin genes and !1promoter activity in transgenic tobacco plants. !$#accession S22971 !'##molecule_type mRNA !'##residues 1-149 ##label CHO !'##cross-references EMBL:Z12839; NID:g19446; PIDN:CAA78301.1; !1PID:g19447 !'##experimental_source pollen of strain Thunb. cv. Nellie White CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS calcium binding; duplication; EF hand; methylated amino acid FEATURE !$2-149 #product calmodulin #status predicted #label MAT\ !$8-40 #domain calmodulin repeat homology #label EF1\ !$44-76 #domain calmodulin repeat homology #label EF2\ !$81-113 #domain calmodulin repeat homology #label EF3\ !$117-149 #domain calmodulin repeat homology #label EF4\ !$116 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8predicted SUMMARY #length 149 #molecular-weight 16848 #checksum 4494 SEQUENCE /// ENTRY S70768 #type complete TITLE calmodulin CAM81 - garden petunia ORGANISM #formal_name Petunia x hybrida #common_name garden petunia DATE 28-Oct-1996 #sequence_revision 11-Apr-1997 #text_change 22-Jun-1999 ACCESSIONS S70768 REFERENCE S70768 !$#authors Fromm, H.; Carlenor, E.; Chua, N.H. !$#submission submitted to the EMBL Data Library, August 1994 !$#description Molecular characterization of petunia cDNAs encoding !1calmodulins and a calmodulin-related protein. !$#accession S70768 !'##molecule_type mRNA !'##residues 1-149 ##label FRO !'##cross-references EMBL:M80836; NID:g169206; PIDN:AAA33706.1; !1PID:g169207 GENETICS !$#gene CAM81 CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS calcium binding; duplication; EF hand; methylated amino acid FEATURE !$2-149 #product calmodulin CAM81 #status predicted #label !8MAT\ !$8-40 #domain calmodulin repeat homology #label EF1\ !$44-76 #domain calmodulin repeat homology #label EF2\ !$81-113 #domain calmodulin repeat homology #label EF3\ !$117-149 #domain calmodulin repeat homology #label EF4\ !$116 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8predicted SUMMARY #length 149 #molecular-weight 16848 #checksum 4494 SEQUENCE /// ENTRY S40301 #type complete TITLE calmodulin - red bryony ORGANISM #formal_name Bryonia dioica #common_name red bryony DATE 19-Mar-1997 #sequence_revision 11-Apr-1997 #text_change 22-Jun-1999 ACCESSIONS S40301 REFERENCE S40301 !$#authors Galaud, J.P.; Lareyre, J.J.; Boyer, N. !$#journal Plant Mol. Biol. (1993) 23:839-846 !$#title Isolation, sequencing and analysis of the expression of !1Bryonia calmodulin after mechanical perturbation. !$#cross-references MUID:94072731; PMID:8251636 !$#accession S40301 !'##status preliminary !'##molecule_type mRNA !'##residues 1-149 ##label GAL !'##cross-references GB:L14071; NID:g289524; PIDN:AAA16320.1; !1PID:g289525 CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS calcium binding; duplication; EF hand; methylated amino acid FEATURE !$2-149 #product calmodulin #status predicted #label MAT\ !$8-40 #domain calmodulin repeat homology #label EF1\ !$44-76 #domain calmodulin repeat homology #label EF2\ !$81-113 #domain calmodulin repeat homology #label EF3\ !$117-149 #domain calmodulin repeat homology #label EF4\ !$116 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8predicted SUMMARY #length 149 #molecular-weight 16848 #checksum 4494 SEQUENCE /// ENTRY S53006 #type complete TITLE calmodulin - leaf mustard ORGANISM #formal_name Brassica juncea #common_name leaf mustard DATE 14-Jul-1995 #sequence_revision 11-Apr-1997 #text_change 22-Jun-1999 ACCESSIONS S53006 REFERENCE S53006 !$#authors Chye, M.L.; Liu, C.M.; Tan, C.T. !$#journal Plant Mol. Biol. (1995) 27:419-423 !$#title A cDNA clone encoding Brassica calmodulin. !$#cross-references MUID:95195168; PMID:7888630 !$#accession S53006 !'##status preliminary !'##molecule_type mRNA !'##residues 1-149 ##label CHY !'##cross-references GB:M88307; NID:g899057; PIDN:AAA87347.1; !1PID:g899058 CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS calcium binding; duplication; EF hand; methylated amino acid FEATURE !$2-149 #product calmodulin #status predicted #label MAT\ !$8-40 #domain calmodulin repeat homology #label EF1\ !$44-76 #domain calmodulin repeat homology #label EF2\ !$81-113 #domain calmodulin repeat homology #label EF3\ !$117-149 #domain calmodulin repeat homology #label EF4\ !$116 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8predicted SUMMARY #length 149 #molecular-weight 16820 #checksum 4403 SEQUENCE /// ENTRY S22503 #type complete TITLE calmodulin [similarity] - Arabidopsis thaliana ALTERNATE_NAMES protein T8M16_130 CONTAINS calmodulin 3; calmodulin 5; protein T3K9.12 ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 13-Jan-1995 #sequence_revision 11-Apr-1997 #text_change 01-Sep-2000 ACCESSIONS S22503; S22504; A34669; S35186; S71513; T02108; T50930; !1T51268; S25135 REFERENCE S22503 !$#authors Perera, I.Y.; Zielinski, R.E. !$#journal Plant Mol. Biol. (1992) 19:649-664 !$#title Structure and expression of the Arabidopsis CaM-3 calmodulin !1gene. !$#cross-references MUID:92329725; PMID:1627778 !$#accession S22503 !'##molecule_type DNA !'##residues 1-149 ##label PER !'##cross-references EMBL:M73711; NID:g166652; PIDN:AAA32764.1; !1PID:g166653 !'##experimental_source strain Landsberg erecta !'##genetics CAM3 !$#accession S22504 !'##molecule_type mRNA !'##residues 7-149 ##label PEW !'##cross-references EMBL:M73712; NID:g166654; PIDN:AAA32765.1; !1PID:g166655 !'##experimental_source strain Columbia, leaf !'##genetics CAM3 REFERENCE A34669 !$#authors Braam, J.; Davis, R.W. !$#journal Cell (1990) 60:357-364 !$#title Rain-, wind-, and touch-induced expression of calmodulin and !1calmodulin-related genes in Arabidopsis. !$#cross-references MUID:90150263; PMID:2302732 !$#accession A34669 !'##status preliminary; nucleic acid sequence not shown; not compared !1with conceptual translation !'##molecule_type mRNA !'##residues 12-149 ##label BRA REFERENCE S35185 !$#authors Gawienowski, M.C.; Szymanski, D.; Perera, I.Y.; Zielinski, !1R.E. !$#journal Plant Mol. Biol. (1993) 22:215-225 !$#title Calmodulin isoforms in Arabidopsis encoded by multiple !1divergent mRNAs. !$#cross-references MUID:93283627; PMID:8507825 !$#accession S35186 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 12-149 ##label GAW !'##cross-references EMBL:Z12023; NID:g16224; PIDN:CAA78058.1; !1PID:g16225 !'##experimental_source strain Columbia, leaf !'##genetics CAM5 REFERENCE S71513 !$#authors Chandra, A.; Upadhyaya, K.C. !$#journal Cell. Mol. Biol. Res. (1993) 39:509-516 !$#title Structure and organization of a novel calmodulin gene of !1Arabidopsis thaliana. !$#cross-references MUID:94227846; PMID:8173593 !$#accession S71513 !'##status preliminary !'##molecule_type DNA !'##residues 1-149 ##label CHA !'##cross-references EMBL:X67273; NID:g474182; PIDN:CAA47690.1; !1PID:g474183 !'##experimental_source strain Columbia, C-24, seedlings !'##note the authors did not translate the codon for residue 1 REFERENCE Z14570 !$#authors Rounsley, S.D.; Kaul, S.; Lin, X.; Ketchum, K.A.; Crosby, !1M.L.; Brandon, R.C.; Sykes, S.M.; Mason, T.M.; Kerlavage, !1A.R.; Adams, M.D.; Somerville, C.R.; Venter, J.C. !$#submission submitted to the EMBL Data Library, February 1999 !$#description Arabidopsis thaliana chromosome II BAC T3K9 genomic !1sequence. !$#accession T02108 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-149 ##label ROU !'##cross-references EMBL:AC004261; NID:g3402695; PIDN:AAD12000.1; !1PID:g3402706 !'##experimental_source cultivar Columbia REFERENCE Z25106 !$#authors Ling, V.; Perera, I.; Zielinski, R.E. !$#journal Plant Physiol. (1991) 96:1196-1202 !$#title Primary sturctures of Arabidopsis calmodulin isoforms !1deduced from the sequences of cDNA clones. !$#accession T50930 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-149 ##label LIN !'##cross-references EMBL:M38380; PIDN:AAA32763.1 REFERENCE Z25346 !$#authors Benes, V.; Wurmbach, E.; Drzonek, H.; Ansorge, W.; Mewes, !1H.W.; Rudd, S.; Lemcke, K.; Mayer, K.F.X.; Quetier, F.; !1Salanoubat, M. !$#submission submitted to the Protein Sequence Database, August 2000 !$#accession T51268 !'##status preliminary !'##molecule_type DNA !'##residues 1-149 ##label BEN !'##cross-references EMBL:AL390921; PIDN:CAC00743.1 !'##experimental_source cultivar Columbia; BAC clone T8M16 !'##genetics CAM2 GENETICS CAM2 !$#map_position 3 !$#introns 26/1 !$#note T8M16_130 GENETICS CAM3 !$#gene CaM3 !$#map_position 2 !$#introns 26/1 !$#note T3K9.12 GENETICS CAM5 !$#gene CaM5 CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS calcium binding; duplication; EF hand; methylated amino acid FEATURE !$2-149 #product calmodulin #status predicted #label MAT\ !$8-40 #domain calmodulin repeat homology #label EF1\ !$44-76 #domain calmodulin repeat homology #label EF2\ !$81-113 #domain calmodulin repeat homology #label EF3\ !$117-149 #domain calmodulin repeat homology #label EF4\ !$94,96,98,100,105 #binding_site calcium (Asp, Asp, Asn, Phe, Glu) !8#status predicted\ !$116 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8predicted SUMMARY #length 149 #molecular-weight 16820 #checksum 4403 SEQUENCE /// ENTRY AQJFNV #type complete TITLE aequorin precursor - hydromedusa (Aequorea victoria) ORGANISM #formal_name Aequorea victoria DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 26-May-2000 ACCESSIONS A03020 REFERENCE A03020 !$#authors Inouye, S.; Noguchi, M.; Sakaki, Y.; Takagi, Y.; Miyata, T.; !1Iwanaga, S.; Miyata, T.; Tsuji, F.I. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:3154-3158 !$#title Cloning and sequence analysis of cDNA for the luminescent !1protein aequorin. !$#cross-references MUID:85216460; PMID:3858813 !$#accession A03020 !'##molecule_type mRNA !'##residues 1-196 ##label INO !'##cross-references GB:M11394; NID:g155658; PIDN:AAA27719.1; !1PID:g155659; GB:L29571; NID:g461374; PID:g461375 !'##experimental_source clone AQ440 COMMENT The precise function of residues 1-7 is not known. COMMENT The authors suggest that there are three calcium-binding !1sites, and that residues 47-57, 62-72, and 107-117 may !1interact with the chromophore. COMMENT Trace amounts of calcium ion trigger the oxidation of the !1functional chromophore, coelenterazine, to coelenteramide. !1In its excited oxidized state, the chromophore bound to !1apoaequorin emits a blue light. COMMENT Cysteine residues appear to be critical to the ability of !1this photoprotein to luminesce. Treatment of aequorin with !1N-ethylmaleimide, a sulfhydryl-blocking agent, eliminates !1light emission, and mercaptoethanol is necessary to !1regenerate aequorin from apoaequorin. CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS calcium binding; EF hand; luminescence FEATURE !$8-196 #product aequorin #status predicted #label MAT\ !$18-50 #domain calmodulin repeat homology #label EF1\ !$111-143 #domain calmodulin repeat homology #label EF2\ !$147-179 #domain calmodulin repeat homology #label EF3\ !$31,33,35,37,42 #binding_site calcium (Asp, Asn, Asn, Lys, Glu) !8#status predicted\ !$124,126,128,130,135 #binding_site calcium (Asp, Asp, Asn, Ala, Glu) !8#status predicted\ !$160,162,164,166,171 #binding_site calcium (Asp, Asp, Ser, Gln, Glu) !8#status predicted SUMMARY #length 196 #molecular-weight 22285 #checksum 6516 SEQUENCE /// ENTRY MCHU #type complete TITLE calmodulin [validated] - human ALTERNATE_NAMES modulator protein; phosphodiesterase activator; phosphorylase kinase delta chain ORGANISM #formal_name Homo sapiens #common_name man DATE 14-Nov-1983 #sequence_revision 30-Jun-1992 #text_change 15-Sep-2000 ACCESSIONS S48728; S13159; A31787; A28479; A90460; JN0365; I52348; !1A03021 REFERENCE S48728 !$#authors Rhyner, J.A.; Ottiger, M.; Wicki, R.; Greenwood, T.M.; !1Strehler, E.E. !$#journal Eur. J. Biochem. (1994) 225:71-82 !$#title Structure of the human CALM1 calmodulin gene and !1identification of two CALM1-related pseudogenes CALM1P1 and !1CALM1P2. !$#cross-references MUID:95010144; PMID:7925473 !$#accession S48728 !'##molecule_type DNA !'##residues 1-149 ##label RHY !'##cross-references EMBL:U11886; NID:g531824; EMBL:U12022; NID:g531825; !1PIDN:AAB60644.1; PID:g531827 !'##genetics CAL1 REFERENCE S13159 !$#authors Koller, M.; Schnyder, B.; Strehler, E.E. !$#journal Biochim. Biophys. Acta (1990) 1087:180-189 !$#title Structural organization of the human CaMIII calmodulin gene. !$#cross-references MUID:91027929; PMID:2223880 !$#accession S13159 !'##molecule_type DNA !'##residues 1-149 ##label KOL !'##cross-references EMBL:X52606; EMBL:X52607; EMBL:X52608; NID:g29637; !1PIDN:CAA36839.1; PID:g825635 !'##genetics CAL3 REFERENCE A31787 !$#authors Fischer, R.; Koller, M.; Flura, M.; Mathews, S.; !1Strehler-Page, M.A.; Krebs, J.; Penniston, J.T.; Carafoli, !1E.; Strehler, E.E. !$#journal J. Biol. Chem. (1988) 263:17055-17062 !$#title Multiple divergent mRNAs code for a single human calmodulin. !$#cross-references MUID:89034207; PMID:3182832 !$#accession A31787 !'##molecule_type mRNA !'##residues 1-149 ##label FIS !'##cross-references GB:J04046; NID:g179887; PIDN:AAA51918.1; !1PID:g179888 !'##genetics CAL1 REFERENCE A92620 !$#authors SenGupta, B.; Friedberg, F.; Detera-Wadleigh, S.D. !$#journal J. Biol. Chem. (1987) 262:16663-16670 !$#title Molecular analysis of human and rat calmodulin complementary !1DNA clones. Evidence for additional active genes in these !1species. !$#cross-references MUID:88059053; PMID:2445749 !$#accession A28479 !'##molecule_type mRNA !'##residues 1-149 ##label SEN !'##cross-references GB:J03468; GB:M19311; NID:g179883; PIDN:AAA35641.1; !1PID:g179884 !'##genetics CAL2 REFERENCE A90460 !$#authors Sasagawa, T.; Ericsson, L.H.; Walsh, K.A.; Schreiber, W.E.; !1Fischer, E.H.; Titani, K. !$#journal Biochemistry (1982) 21:2565-2569 !$#title Complete amino acid sequence of human brain calmodulin. !$#cross-references MUID:82231946; PMID:7093203 !$#accession A90460 !'##molecule_type protein !'##residues 2-149 ##label SAS REFERENCE JN0365 !$#authors Alakhov, V.U.; Severin, E.S.; Vinokurov, L.M.; Dudkin, S.M. !$#journal Bioorg. Khim. (1983) 9:123-126 !$#title Primary structrue of calmodulin from human brain. !$#cross-references MUID:85022799; PMID:6679753 !$#accession JN0365 !'##molecule_type protein !'##residues 2-60,'D',62-104,'Q',106-149 ##label ALA !'##experimental_source brain REFERENCE I52348 !$#authors Wawrzynczak, E.J.; Perham, R.N. !$#journal Biochem. Int. (1984) 9:177-185 !$#title Isolation and nucleotide sequence of a cDNA encoding human !1calmodulin. !$#cross-references MUID:85022688; PMID:6385987 !$#accession I52348 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-149 ##label RES !'##cross-references GB:M27319; NID:g179809; PIDN:AAA35635.1; !1PID:g179810 REFERENCE A57450 !$#authors Chattopadhyaya, R.; Meador, W.E.; Means, A.R.; Quiocho, F.A. !$#journal J. Mol. Biol. (1992) 228:1177-1192 !$#title Calmodulin structure refined at 1.7 angstrom resolution. !$#cross-references MUID:93116061; PMID:1474585 !$#contents annotation; X-ray crystallography, 1.7 angstroms, residues !15-148 REFERENCE A51098 !$#authors Chattopadhyaya, R.; Quiocho, F.A. !$#submission submitted to the Brookhaven Protein Data Bank, September !11992 !$#cross-references PDB:1CLL !$#contents annotation; X-ray crystallography, 1.7 angstroms, residues !15-148 REFERENCE A57451 !$#authors Ikura, M.; Clore, G.M.; Gronenborn, A.M.; Zhu, G.; Klee, !1C.B.; Bax, A. !$#journal Science (1992) 256:632-638 !$#title Solution structure of a calmodulin-target peptide complex by !1multidimensional NMR. !$#cross-references MUID:92263094; PMID:1585175 !$#contents annotation; conformation of calmodulin and target peptide by !1(1)H-NMR REFERENCE A57452 !$#authors Meador, W.E.; Means, A.R.; Quiocho, F.A. !$#journal Science (1992) 257:1251-1255 !$#title Target enzyme recognition by calmodulin: 2.4 angstrom !1structure of a calmodulin-peptide complex. !$#cross-references MUID:92390716; PMID:1519061 !$#contents annotation; X-ray crystallography, 2.4 angstroms, calmodulin !1and target peptide GENETICS CAL1 !$#gene GDB:CALM1; CALML2 !'##cross-references GDB:127560; OMIM:114180 !$#map_position 14q32-14q32 !$#introns 1/3; 12/1; 60/1; 95/3; 141/1 !$#note the multiple calmodulin genes produce different mRNA's but !1identical protein sequences GENETICS CAL2 !$#gene GDB:CALM2; CAMII; PHKD !'##cross-references GDB:127561; OMIM:114182 !$#map_position 2p21-2p21 GENETICS CAL3 !$#gene GDB:CALM3; PHKD !'##cross-references GDB:127562; OMIM:114183 !$#map_position 19q13.3-19q13.3 !$#introns 1/3; 12/1; 60/1; 95/3; 141/1 COMPLEX in phosphorylase kinase participates in a polymer of 16 !1chains, four each of alpha regulatory chains, and beta !1regulatory chains, gamma catalytic chains, and delta !1calmodulin chains; the crystalline form is monomeric FUNCTION !$#description this protein has multiple, calcium-dependent, regulatory !1activities in various tissues CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS acetylated amino end; calcium binding; duplication; EF hand; !1methylated amino acid FEATURE !$2-149 #product calmodulin #status experimental #label MAT\ !$8-40 #domain calmodulin repeat homology #label EF1\ !$44-76 #domain calmodulin repeat homology #label EF2\ !$81-113 #domain calmodulin repeat homology #label EF3\ !$117-149 #domain calmodulin repeat homology #label EF4\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental\ !$21,23,25,27,32 #binding_site calcium (Asp, Asp, Asp, Thr, Glu) !8#status experimental\ !$57,59,61,63,68 #binding_site calcium (Asp, Asp, Asn, Thr, Glu) !8#status experimental\ !$94,96,98,100,105 #binding_site calcium (Asp, Asp, Asn, Tyr, Glu) !8#status experimental\ !$116 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental\ !$130,132,134,136,141 #binding_site calcium (Asp, Asp, Asp, Gln, Glu) !8#status experimental SUMMARY #length 149 #molecular-weight 16837 #checksum 5619 SEQUENCE /// ENTRY MCRB #type complete TITLE calmodulin - rabbit (tentative sequence) ALTERNATE_NAMES modulator protein; phosphodiesterase activator; phosphorylase kinase delta chain ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 31-Mar-2000 ACCESSIONS A91104; A03021 REFERENCE A91104 !$#authors Grand, R.J.A.; Shenolikar, S.; Cohen, P. !$#journal Eur. J. Biochem. (1981) 113:359-367 !$#title The amino acid sequence of the delta subunit (calmodulin) of !1rabbit skeletal muscle phosphorylase kinase. !$#cross-references MUID:81138220; PMID:7202416 !$#accession A91104 !'##molecule_type protein !'##residues 1-148 ##label GRA !'##note this protein was isolated as the delta chain of phosphorylase !1kinase COMMENT This protein has multiple, calcium-dependent, regulatory !1activities in various tissues. CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS blocked amino end; calcium binding; duplication; EF hand; !1methylated amino acid FEATURE !$7-39 #domain calmodulin repeat homology #label EF1\ !$43-75 #domain calmodulin repeat homology #label EF2\ !$80-112 #domain calmodulin repeat homology #label EF3\ !$116-148 #domain calmodulin repeat homology #label EF4\ !$1 #modified_site blocked amino end #status !8experimental\ !$20,22,24,26,31 #binding_site calcium (Asp, Asp, Asp, Thr, Glu) !8#status predicted\ !$56,58,60,62,67 #binding_site calcium (Asp, Asp, Asn, Thr, Glu) !8#status predicted\ !$93,95,97,99,104 #binding_site calcium (Asp, Asp, Asn, Tyr, Glu) !8#status predicted\ !$115 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental\ !$129,131,133,135,140 #binding_site calcium (Asn, Asp, Asp, Gln, Glu) !8#status predicted SUMMARY #length 148 #molecular-weight 16705 #checksum 2310 SEQUENCE /// ENTRY MCRT #type complete TITLE calmodulin [validated] - rat ALTERNATE_NAMES modulator protein; phosphodiesterase activator; phosphorylase kinase delta chain ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 15-Sep-2000 ACCESSIONS S03206; A30899; S05228; S05227; I57616; B28479; A29082; !1S17536; A03021 REFERENCE S03206 !$#authors Nojima, H.; Sokabe, H. !$#journal J. Mol. Biol. (1987) 193:439-445 !$#title Structure of a gene for rat calmodulin. !$#cross-references MUID:87226204; PMID:3035194 !$#accession S03206 !'##molecule_type DNA !'##residues 1-149 ##label NO1 !'##cross-references EMBL:X13931; NID:g55860; PIDN:CAA32119.1; !1PID:g1334203 !'##experimental_source strain Wistar-Kyoto !'##genetics CAM1 !$#accession A30899 !'##molecule_type mRNA !'##residues 1-149 ##label NO2 !'##cross-references EMBL:X13933; NID:g57040; PIDN:CAA32120.1; !1PID:g57041 !'##experimental_source strain Sprague-Dawley REFERENCE S05227 !$#authors Nojima, H. !$#journal J. Mol. Biol. (1989) 208:269-282 !$#title Structural organization of multiple rat calmodulin genes. !$#cross-references MUID:89362474; PMID:2527998 !$#accession S05228 !'##molecule_type DNA !'##residues 1-149 ##label NO4 !'##cross-references EMBL:X14265; NID:g55866; PIDN:CAA32478.1; !1PID:g55867 !'##genetics CAM2 !$#accession S05227 !'##molecule_type DNA !'##residues 1-149 ##label NO5 !'##cross-references EMBL:X13833; NID:g55863; PIDN:CAA32062.1; !1PID:g818020 !'##genetics CAM3 REFERENCE I57616 !$#authors Nojima, H.; Kishi, K.; Sokabe, H. !$#journal Mol. Cell. Biol. (1987) 7:1873-1880 !$#title Multiple calmodulin mRNA species are derived from two !1distinct genes. !$#cross-references MUID:87257889; PMID:3037336 !$#accession I57616 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-149 ##label NO3 !'##cross-references GB:M17069; NID:g203257; PIDN:AAA40863.1; !1PID:g203258 REFERENCE A92620 !$#authors SenGupta, B.; Friedberg, F.; Detera-Wadleigh, S.D. !$#journal J. Biol. Chem. (1987) 262:16663-16670 !$#title Molecular analysis of human and rat calmodulin complementary !1DNA clones. Evidence for additional active genes in these !1species. !$#cross-references MUID:88059053; PMID:2445749 !$#accession B28479 !'##molecule_type mRNA !'##residues 1-149 ##label SEN !'##cross-references GB:M19312; NID:g203255; PIDN:AAA40862.1; !1PID:g203256 REFERENCE A29082 !$#authors Sherbany, A.A.; Parent, A.S.; Brosius, J. !$#journal DNA (1987) 6:267-272 !$#title Rat calmodulin cDNA. !$#cross-references MUID:87246077; PMID:2885164 !$#accession A29082 !'##molecule_type mRNA !'##residues 1-149 ##label SHE !'##cross-references GB:M16659; NID:g203259; PIDN:AAA40864.1; !1PID:g203260 REFERENCE S17536 !$#authors Wright, L.S.; Collins, J.H.; Finn, K.A.; Siegel, F.L. !$#journal Biochim. Biophys. Acta (1991) 1079:174-181 !$#title A calmodulin endoproteinase from mitochondrial membranes. !$#cross-references MUID:92002131; PMID:1911840 !$#accession S17536 !'##molecule_type protein !'##residues 77-92,94-96 ##label WRI REFERENCE A92228 !$#authors Dedman, J.R.; Jackson, R.L.; Schreiber, W.E.; Means, A.R. !$#journal J. Biol. Chem. (1978) 253:343-346 !$#title Sequence homology of the Ca2+-dependent regulator of cyclic !1nucleotide phosphodiesterase from rat testis with other !1Ca2+-binding proteins. !$#cross-references MUID:78066877; PMID:201628 !$#contents annotation; partial sequence determination REFERENCE A50576 !$#authors Babu, Y.S.; Bugg, C.E.; Cook, W.J. !$#submission submitted to the Brookhaven Protein Data Bank, May 1988 !$#cross-references PDB:3CLN !$#contents annotation; X-ray crystallography, 2.2 angstroms, residues !16-129,'N',131-148 REFERENCE A37299 !$#authors Babu, Y.S.; Bugg, C.E.; Cook, W.J. !$#journal J. Mol. Biol. (1988) 204:191-204 !$#title Structure of calmodulin refined at 2.2 A resolution. !$#cross-references MUID:89110997; PMID:3145979 !$#contents annotation; X-ray crystallography, 2.2 angstroms !$#note crystals of both rat and cow calmodulin, having identical !1sequences, were used in the refinement REFERENCE A37298 !$#authors Babu, Y.S.; Sack, J.S.; Greenhough, T.J.; Bugg, C.E.; Means, !1A.R.; Cook, W.J. !$#journal Nature (1985) 315:37-40 !$#title Three-dimensional structure of calmodulin. !$#cross-references MUID:85188323; PMID:3990807 !$#contents annotation; X-ray crystallography, 3.0 angstroms COMMENT Calmodulin regulates many calcium-dependent activities in !1various tissues. GENETICS CAM1 !$#gene CaMI !$#introns 1/3; 12/1; 60/1; 95/3; 141/1 GENETICS CAM2 !$#gene CaMII !$#introns 1/3; 12/1; 95/3; 141/1 GENETICS CAM3 !$#gene CaMIII !$#introns 1/3; 12/1; 60/1; 95/3; 141/1 CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS acetylated amino end; calcium binding; duplication; EF hand; !1methylated amino acid FEATURE !$2-149 #product calmodulin #status experimental #label MAT\ !$8-40 #domain calmodulin repeat homology #label EF1\ !$44-76 #domain calmodulin repeat homology #label EF2\ !$81-113 #domain calmodulin repeat homology #label EF3\ !$117-149 #domain calmodulin repeat homology #label EF4\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental\ !$21,23,25,27,32 #binding_site calcium (Asp, Asp, Asp, Thr, Glu) !8#status experimental\ !$57,59,61,63,68 #binding_site calcium (Asp, Asp, Asn, Thr, Glu) !8#status experimental\ !$94,96,98,100,105 #binding_site calcium (Asp, Asp, Asn, Tyr, Glu) !8#status experimental\ !$116 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental\ !$130,132,134,136,141 #binding_site calcium (Asp, Asp, Asp, Gln, Glu) !8#status experimental SUMMARY #length 149 #molecular-weight 16837 #checksum 5619 SEQUENCE /// ENTRY MCBO #type complete TITLE calmodulin [validated] - bovine ALTERNATE_NAMES modulator protein; phosphodiesterase activator; phosphorylase kinase delta chain; protein kinase C inhibitor ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 15-Sep-2000 ACCESSIONS A90719; A92291; A91449; S02034; S54345; A03021 REFERENCE A90719 !$#authors Kasai, H.; Kato, Y.; Isobe, T.; Kawasaki, H.; Okuyama, T. !$#journal Biomed. Res. (1980) 1:248-264 !$#title Determination of the complete amino acid sequence of !1calmodulin (phenylalanine-rich acidic protein II) from !1bovine brain. !$#accession A90719 !'##molecule_type protein !'##residues 1-59,'D',61-96,'D',98-148 ##label KAS REFERENCE A92291 !$#authors Watterson, D.M.; Sharief, F.; Vanaman, T.C. !$#journal J. Biol. Chem. (1980) 255:962-975 !$#title The complete amino acid sequence of the Ca2+-dependent !1modulator protein (calmodulin) of bovine brain. !$#cross-references MUID:80094551; PMID:7356670 !$#accession A92291 !'##molecule_type protein !'##residues 1-23,'N',25-128,'N',130-134,'E',136-148 ##label WAT REFERENCE A91449 !$#authors Grand, R.J.A.; Perry, S.V. !$#journal FEBS Lett. (1978) 92:137-142 !$#title The amino acid sequence of the troponin C-like protein !1(modulator protein) from bovine uterus. !$#accession A91449 !'##molecule_type protein !'##residues 1-96,'D',98-128,'N',130-134,'E',136-148 ##label GRA REFERENCE S02034 !$#authors Pribilla, I.; Krueger, H.; Buchner, K.; Otto, H.; Schiebler, !1W.; Tripier, D.; Hucho, F. !$#journal Eur. J. Biochem. (1988) 177:657-664 !$#title Heat-resistant inhibitors of protein kinase C from bovine !1brain. !$#cross-references MUID:89064822; PMID:3058479 !$#accession S02034 !'##molecule_type protein !'##residues 38-60 ##label PRI REFERENCE A37299 !$#authors Babu, Y.S.; Bugg, C.E.; Cook, W.J. !$#journal J. Mol. Biol. (1988) 204:191-204 !$#title Structure of calmodulin refined at 2.2 A resolution. !$#cross-references MUID:89110997; PMID:3145979 !$#contents annotation; X-ray crystallography, 2.2 angstroms REFERENCE A58244 !$#authors Strynadka, N.C.J.; James, M.N.G. !$#journal Proteins (1988) 3:1-17 !$#title Two trifluoperazine-binding sites on calmodulin predicted !1from comparative molecular modeling with troponin-C. !$#cross-references MUID:88234481; PMID:3375233 !$#contents annotation; molecular model REFERENCE A50421 !$#authors Strynadka, N.C.J.; James, M.N.G. !$#submission submitted to the Brookhaven Protein Data Bank, February 1988 !$#cross-references PDB:2CLN !$#contents annotation; molecular model REFERENCE S54343 !$#authors Okazaki, K.; Obata, N.H.; Inoue, S.; Hidaka, H. !$#journal Biochem. J. (1995) 306:551-555 !$#title S100-beta is a target protein of neurocalcin delta, an !1abundant isoform in glial cells. !$#cross-references MUID:95194333; PMID:7887910 !$#accession S54345 !'##molecule_type protein !'##residues 78-91 ##label OKA FUNCTION !$#description this protein has multiple, calcium-dependent, regulatory !1activities in various tissues CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS acetylated amino end; calcium binding; duplication; EF hand; !1methylated amino acid FEATURE !$7-39 #domain calmodulin repeat homology #label EF1\ !$43-75 #domain calmodulin repeat homology #label EF2\ !$80-112 #domain calmodulin repeat homology #label EF3\ !$116-148 #domain calmodulin repeat homology #label EF4\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$20,22,24,26,31 #binding_site calcium (Asp, Asp, Asp, Thr, Glu) !8#status experimental\ !$56,58,60,62,67 #binding_site calcium (Asp, Asp, Asn, Thr, Glu) !8#status experimental\ !$93,95,97,99,104 #binding_site calcium (Asp, Asp, Asn, Tyr, Glu) !8#status experimental\ !$115 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental\ !$129,131,133,135,140 #binding_site calcium (Asp, Asp, Asp, Gln, Glu) !8#status experimental SUMMARY #length 148 #molecular-weight 16706 #checksum 2160 SEQUENCE /// ENTRY MCCH #type complete TITLE calmodulin - chicken ALTERNATE_NAMES modulator protein; phosphodiesterase activator; phosphorylase kinase delta chain ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 22-Jun-1999 ACCESSIONS A92394; I50184; A03021 REFERENCE A92394 !$#authors Putkey, J.A.; Ts'ui, K.F.; Tanaka, T.; Lagace, L.; Stein, !1J.P.; Lai, E.C.; Means, A.R. !$#journal J. Biol. Chem. (1983) 258:11864-11870 !$#title Chicken calmodulin genes. A species comparison of cDNA !1sequences and isolation of a genomic clone. !$#cross-references MUID:84008199; PMID:6137485 !$#accession A92394 !'##molecule_type mRNA !'##residues 1-149 ##label PUT !'##cross-references GB:L00101; EMBL:K00430; NID:g211396; !1PIDN:AAA48653.1; PID:g211398 REFERENCE A37301 !$#authors Simmen, R.C.M.; Tanaka, T.; Ts'ui, K.F.; Putkey, J.A.; !1Scott, M.J.; Lai, E.C.; Means, A.R. !$#journal J. Biol. Chem. (1985) 260:907-912 !$#title The structural organization of the chicken calmodulin gene. !$#cross-references MUID:85104969; PMID:2981850 !$#contents annotation REFERENCE A37302 !$#authors Simmen, R.C.M.; Tanaka, T.; Ts'ui, K.F.; Putkey, J.A.; !1Scott, M.J.; Lai, E.C.; Means, A.R. !$#journal J. Biol. Chem. (1987) 262:4928-4929 !$#title The structural organization of the chicken calmodulin gene: !1a correction. !$#contents annotation REFERENCE I50184 !$#authors Iida, Y. !$#journal Bull. Chem. Soc. Jpn. (1984) 57:2667-2668 !$#title cDNA sequences and molecular evolution of calmodulin genes !1of chicken and eel. !$#accession I50184 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-149 ##label IID !'##cross-references GB:M36167; NID:g211385; PIDN:AAA48650.1; !1PID:g211386 COMMENT This protein has multiple, calcium-dependent, regulatory !1activities in various tissues. GENETICS !$#introns 1/3; 12/1; 60/1; 95/3; 141/1 CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS calcium binding; duplication; EF hand; methylated amino acid FEATURE !$2-149 #product calmodulin #status predicted #label MAT\ !$8-40 #domain calmodulin repeat homology #label EF1\ !$44-76 #domain calmodulin repeat homology #label EF2\ !$81-113 #domain calmodulin repeat homology #label EF3\ !$117-149 #domain calmodulin repeat homology #label EF4\ !$21,23,25,27,32 #binding_site calcium (Asp, Asp, Asp, Thr, Glu) !8#status predicted\ !$57,59,61,63,68 #binding_site calcium (Asp, Asp, Asn, Thr, Glu) !8#status predicted\ !$94,96,98,100,105 #binding_site calcium (Asp, Asp, Asn, Tyr, Glu) !8#status predicted\ !$116 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8predicted\ !$130,132,134,136,141 #binding_site calcium (Asp, Asp, Asp, Gln, Glu) !8#status predicted SUMMARY #length 149 #molecular-weight 16837 #checksum 5619 SEQUENCE /// ENTRY I51202 #type complete TITLE calmodulin - duck ALTERNATE_NAMES modulator protein; phosphodiesterase activator; phosphorylase kinase delta chain ORGANISM #formal_name Anas platyrhynchos #common_name domestic duck DATE 19-Mar-1997 #sequence_revision 11-Apr-1997 #text_change 22-Jun-1999 ACCESSIONS I51202 REFERENCE I51201 !$#authors Kimura, N.; Kurosawa, N.; Kondo, K.; Tsukada, Y. !$#journal Brain Res. Mol. Brain Res. (1993) 17:351-355 !$#title Molecular cloning of the kainate-binding protein and !1calmodulin genes which are induced by an imprinting stimulus !1in ducklings. !$#cross-references MUID:93287810; PMID:8389959 !$#accession I51202 !'##status preliminary !'##molecule_type mRNA !'##residues 1-149 ##label KIM !'##cross-references GB:D83350; NID:g1199918; PIDN:BAA11896.1; !1PID:g1199919 COMMENT This protein has multiple, calcium-dependent, regulatory !1activities in various tissues. CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS calcium binding; duplication; EF hand; methylated amino acid FEATURE !$2-149 #product calmodulin #status predicted #label MAT\ !$8-40 #domain calmodulin repeat homology #label EF1\ !$44-76 #domain calmodulin repeat homology #label EF2\ !$81-113 #domain calmodulin repeat homology #label EF3\ !$117-149 #domain calmodulin repeat homology #label EF4\ !$116 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8predicted SUMMARY #length 149 #molecular-weight 16837 #checksum 5619 SEQUENCE /// ENTRY MCON #type complete TITLE calmodulin - salmon ALTERNATE_NAMES modulator protein; phosphodiesterase activator; phosphorylase kinase delta chain ORGANISM #formal_name Oncorhynchus sp. #common_name salmon DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 17-Apr-1998 ACCESSIONS A94541; JK0013 REFERENCE A94541 !$#authors Yazawa, M.; Toda, H.; Yagi, Y. !$#submission submitted to JIPID, May 1988 !$#accession A94541 !'##molecule_type protein !'##residues 1-148 ##label YA1 REFERENCE JK0013 !$#authors Yazawa, M.; Toda, H.; Yagi, Y. !$#journal Seikagaku (1985) 57:1037 !$#title Amino acid sequence of salmon calmodulin. !$#note author-supplied citation !$#accession JK0013 !'##molecule_type protein !'##residues 1-148 ##label YA2 COMMENT This protein has multiple, calcium-dependent, regulatory !1activities in various tissues. CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS acetylated amino end; calcium binding; duplication; EF hand; !1methylated amino acid FEATURE !$7-39 #domain calmodulin repeat homology #label EF1\ !$43-75 #domain calmodulin repeat homology #label EF2\ !$80-112 #domain calmodulin repeat homology #label EF3\ !$116-148 #domain calmodulin repeat homology #label EF4\ !$1 #modified_site acetylated amino end (Ala) #status !8predicted\ !$20,22,24,26,31 #binding_site calcium (Asp, Asp, Asp, Thr, Glu) !8#status predicted\ !$56,58,60,62,67 #binding_site calcium (Asp, Asp, Asn, Thr, Glu) !8#status predicted\ !$93,95,97,99,104 #binding_site calcium (Asp, Asp, Asn, Tyr, Glu) !8#status predicted\ !$115 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8predicted\ !$129,131,133,135,140 #binding_site calcium (Asp, Asp, Asp, Gln, Glu) !8#status predicted SUMMARY #length 148 #molecular-weight 16706 #checksum 2160 SEQUENCE /// ENTRY MCEE #type complete TITLE calmodulin - electric eel ALTERNATE_NAMES modulator protein; phosphodiesterase activator; phosphorylase kinase delta chain ORGANISM #formal_name Electrophorus electricus #common_name electric eel DATE 25-Feb-1985 #sequence_revision 30-Jun-1992 #text_change 22-Jun-1999 ACCESSIONS A03022; A60781; I50534 REFERENCE A03022 !$#authors Lagace, L.; Chandra, T.; Woo, S.L.C.; Means, A.R. !$#journal J. Biol. Chem. (1983) 258:1684-1688 !$#title Identification of multiple species of calmodulin messenger !1RNA using a full length complementary DNA. !$#cross-references MUID:83108962; PMID:6185488 !$#accession A03022 !'##molecule_type mRNA !'##residues 1-149 ##label LAG !'##cross-references GB:J00931; NID:g213131 !'##experimental_source electroplax !'##note this ORF is not annotated in GenBank entry ELCCALMA, release !1103 REFERENCE JK0011 !$#authors Toda, H.; Abe, Y.; Yazawa, M.; Yagi, K. !$#journal Seikagaku (1985) 57:1037 !$#title Amino acid sequence of sea cucumber calmodulin. !$#note author-supplied citation !$#accession A60781 !'##molecule_type protein !'##residues 2-74,'R',76-149 ##label YAZ !'##note 75-Lys also found REFERENCE I50184 !$#authors Iida, Y. !$#journal Bull. Chem. Soc. Jpn. (1984) 57:2667-2668 !$#title cDNA sequences and molecular evolution of calmodulin genes !1of chicken and eel. !$#accession I50534 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-149 ##label IID !'##cross-references GB:M36168; NID:g213129; PIDN:AAA49236.1; !1PID:g213130 COMMENT This protein has multiple, calcium-dependent, regulatory !1activities in various tissues. CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS calcium binding; duplication; EF hand; methylated amino acid FEATURE !$2-149 #product calmodulin #status predicted #label MAT\ !$8-40 #domain calmodulin repeat homology #label EF1\ !$44-76 #domain calmodulin repeat homology #label EF2\ !$81-113 #domain calmodulin repeat homology #label EF3\ !$117-149 #domain calmodulin repeat homology #label EF4\ !$21,23,25,27,32 #binding_site calcium (Asp, Asp, Asp, Thr, Glu) !8#status predicted\ !$57,59,61,63,68 #binding_site calcium (Asp, Asp, Asn, Thr, Glu) !8#status predicted\ !$94,96,98,100,105 #binding_site calcium (Asp, Asp, Asn, Tyr, Glu) !8#status predicted\ !$116 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8predicted\ !$130,132,134,136,141 #binding_site calcium (Asp, Asp, Asp, Gln, Glu) !8#status predicted SUMMARY #length 149 #molecular-weight 16809 #checksum 5493 SEQUENCE /// ENTRY MCFF #type complete TITLE calmodulin [validated] - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES modulator protein; phosphodiesterase activator; phosphorylase kinase delta chain ORGANISM #formal_name Drosophila melanogaster DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 15-Sep-2000 ACCESSIONS S01173; A27515; S10637 REFERENCE S01173 !$#authors Smith, V.L.; Doyle, K.E.; Maune, J.F.; Munjaal, R.P.; !1Beckingham, K. !$#journal J. Mol. Biol. (1987) 196:471-485 !$#title Structure and sequence of the Drosophila melanogaster !1calmodulin gene. !$#cross-references MUID:88062687; PMID:3119855 !$#accession S01173 !'##molecule_type DNA !'##residues 1-149 ##label SMI !'##cross-references EMBL:X05948 REFERENCE A27515 !$#authors Yamanaka, M.K.; Saugstad, J.A.; Hanson-Painton, O.; !1McCarthy, B.J.; Tobin, S.L. !$#journal Nucleic Acids Res. (1987) 15:3335-3348 !$#title Structure and expression of the Drosophila calmodulin gene. !$#cross-references MUID:87203365; PMID:3106931 !$#accession A27515 !'##molecule_type DNA; mRNA !'##residues 2-149 ##label YAM !'##cross-references EMBL:Y00133; NID:g7687; PIDN:CAA68327.1; PID:g7688 REFERENCE A30897 !$#authors Goerlach, M.; Dieter, P.; Seydewitz, H.H.; Kaiser, C.; Witt, !1I.; Marme, D. !$#journal Biochim. Biophys. Acta (1985) 832:228-232 !$#title Characterisation of calmodulin from Drosophila heads. !$#contents annotation !$#note trimethyllysine is absent from fruit fly calmodulin REFERENCE A58243 !$#authors Taylor, D.A.; Sack, J.S.; Maune, J.F.; Beckingham, K.; !1Quiocho, F.A. !$#journal J. Biol. Chem. (1991) 266:21375-21380 !$#title Structure of a recombinant calmodulin from Drosophila !1melanogaster refined at 2.2-angstroms resolution. !$#cross-references MUID:92042027; PMID:1939171 !$#contents annotation; X-ray crystallography, 2.2 angstroms, residues !12-148 !$#note recombinant form expressed in Escherichia coli REFERENCE A50648 !$#authors Taylor, D.A.; Sack, J.S.; Maune, J.F.; Beckingham, K.; !1Quiocho, F.A. !$#submission submitted to the Brookhaven Protein Data Bank, June 1991 !$#cross-references PDB:4CLN !$#contents annotation; X-ray crystallography, 2.2 angstroms, residues !12-148 GENETICS !$#gene Cal49A !'##cross-references FlyBase:FBgn0000253 !$#map_position 2-[64] !$#introns 1/3; 60/1; 141/1 FUNCTION !$#description this protein has multiple, calcium-dependent, regulatory !1activities in various tissues CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS calcium binding; duplication; EF hand FEATURE !$2-149 #product calmodulin #status predicted #label MAT\ !$8-40 #domain calmodulin repeat homology #label EF1\ !$44-76 #domain calmodulin repeat homology #label EF2\ !$81-113 #domain calmodulin repeat homology #label EF3\ !$117-149 #domain calmodulin repeat homology #label EF4\ !$21,23,25,27,32 #binding_site calcium (Asp, Asp, Asp, Thr, Glu) !8#status experimental\ !$57,59,61,63,68 #binding_site calcium (Asp, Asp, Asn, Thr, Glu) !8#status experimental\ !$94,96,98,100,105 #binding_site calcium (Asp, Asp, Asn, Phe, Glu) !8#status experimental\ !$116 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8absent\ !$130,132,134,136,141 #binding_site calcium (Asp, Asp, Asp, Gln, Glu) !8#status experimental SUMMARY #length 149 #molecular-weight 16810 #checksum 5504 SEQUENCE /// ENTRY MCLQ #type complete TITLE calmodulin - migratory locust ALTERNATE_NAMES modulator protein ORGANISM #formal_name Locusta migratoria #common_name migratory locust DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 24-Nov-1999 ACCESSIONS JK0010 REFERENCE A94537 !$#authors Toda, H. !$#submission submitted to JIPID, May 1988 !$#accession JK0010 !'##molecule_type protein !'##residues 1-148 ##label TOD CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS blocked amino end; calcium binding; duplication; EF hand; !1methylated amino acid FEATURE !$7-39 #domain calmodulin repeat homology #label EF1\ !$43-75 #domain calmodulin repeat homology #label EF2\ !$80-112 #domain calmodulin repeat homology #label EF3\ !$116-148 #domain calmodulin repeat homology #label EF4\ !$1 #modified_site blocked amino end (Ala) #status !8experimental\ !$20,22,24,26,31 #binding_site calcium (Asp, Asp, Asp, Thr, Glu) !8#status predicted\ !$56,58,60,62,67 #binding_site calcium (Asp, Asp, Asn, Thr, Glu) !8#status predicted\ !$93,95,97,99,104 #binding_site calcium (Asp, Asp, Asn, Phe, Glu) !8#status predicted\ !$115 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental\ !$129,131,133,135,140 #binding_site calcium (Asp, Asp, Asp, Gln, Glu) !8#status predicted SUMMARY #length 148 #molecular-weight 16679 #checksum 2043 SEQUENCE /// ENTRY MCGAC #type complete TITLE calmodulin - California sea hare ALTERNATE_NAMES modulator protein ORGANISM #formal_name Aplysia californica #common_name California sea hare DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 22-Jun-1999 ACCESSIONS S13248; A30898 REFERENCE S13248 !$#authors Swanson, M.E.; Sturner, S.F.; Schwartz, J.H. !$#journal J. Mol. Biol. (1990) 216:545-553 !$#title Structure and expression of the Aplysia californica !1calmodulin gene. !$#cross-references MUID:91080147; PMID:2258931 !$#accession S13248 !'##molecule_type DNA !'##residues 2-149 ##label SWA !'##cross-references GB:X56888; NID:g5571; PIDN:CAA40207.1; PID:g5572 !$#accession A30898 !'##molecule_type mRNA !'##residues 1-149 ##label SW2 !'##cross-references GB:X56888; NID:g5571; PIDN:CAA40207.1; PID:g5572 GENETICS !$#introns 1/3; 12/1; 60/1; 141/1 CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS calcium binding; duplication; EF hand; methylated amino acid FEATURE !$2-149 #product calmodulin #status predicted #label MAT\ !$8-40 #domain calmodulin repeat homology #label EF1\ !$44-76 #domain calmodulin repeat homology #label EF2\ !$81-113 #domain calmodulin repeat homology #label EF3\ !$117-149 #domain calmodulin repeat homology #label EF4\ !$21,23,25,27,32 #binding_site calcium (Asp, Asp, Asp, Thr, Glu) !8#status predicted\ !$57,59,61,63,68 #binding_site calcium (Asp, Asp, Asn, Thr, Glu) !8#status predicted\ !$94,96,98,100,105 #binding_site calcium (Asp, Asp, Asn, Phe, Glu) !8#status predicted\ !$116 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8predicted\ !$130,132,134,136,141 #binding_site calcium (Asp, Asp, Asp, Gln, Glu) !8#status predicted SUMMARY #length 149 #molecular-weight 16810 #checksum 5504 SEQUENCE /// ENTRY MCSFCU #type complete TITLE calmodulin - sea cucumber (Stichopus japonicus) ALTERNATE_NAMES modulator protein ORGANISM #formal_name Stichopus japonicus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 24-Nov-1999 ACCESSIONS JK0011 REFERENCE JK0011 !$#authors Toda, H.; Abe, Y.; Yazawa, M.; Yagi, K. !$#journal Seikagaku (1985) 57:1037 !$#title Amino acid sequence of sea cucumber calmodulin. !$#note author-supplied citation !$#accession JK0011 !'##molecule_type protein !'##residues 1-148 ##label TOD !'##note 78-Glu and 99-Phe were also found CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS blocked amino end; calcium binding; duplication; EF hand; !1methylated amino acid FEATURE !$7-39 #domain calmodulin repeat homology #label EF1\ !$43-75 #domain calmodulin repeat homology #label EF2\ !$80-112 #domain calmodulin repeat homology #label EF3\ !$116-148 #domain calmodulin repeat homology #label EF4\ !$1 #modified_site blocked amino end (Ala) #status !8experimental\ !$20,22,24,26,31 #binding_site calcium (Asp, Asp, Asp, Thr, Glu) !8#status predicted\ !$56,58,60,62,67 #binding_site calcium (Asp, Asp, Asn, Thr, Glu) !8#status predicted\ !$93,95,97,99,104 #binding_site calcium (Asp, Asp, Asn, Tyr, Glu) !8#status predicted\ !$115 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental\ !$129,131,133,135,140 #binding_site calcium (Asp, Asp, Asp, Gln, Glu) !8#status predicted SUMMARY #length 148 #molecular-weight 16695 #checksum 2841 SEQUENCE /// ENTRY MCAZS #type complete TITLE calmodulin - sea squirt ALTERNATE_NAMES modulator protein ORGANISM #formal_name Ascidiacea indet. #common_name sea squirt DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 17-Apr-1998 ACCESSIONS JK0015 REFERENCE A94540 !$#authors Yazawa, M.; Toda, H.; Sakiyama, F.; Yagi, K. !$#submission submitted to JIPID, May 1988 !$#accession JK0015 !'##molecule_type protein !'##residues 1-148 ##label YAZ CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS acetylated amino end; calcium binding; duplication; EF hand; !1methylated amino acid FEATURE !$7-39 #domain calmodulin repeat homology #label EF1\ !$43-75 #domain calmodulin repeat homology #label EF2\ !$80-112 #domain calmodulin repeat homology #label EF3\ !$116-148 #domain calmodulin repeat homology #label EF4\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$20,22,24,26,31 #binding_site calcium (Asp, Asp, Asp, Thr, Glu) !8#status predicted\ !$56,58,60,62,67 #binding_site calcium (Asp, Asp, Asp, Thr, Glu) !8#status predicted\ !$93,95,97,99,104 #binding_site calcium (Asp, Asp, Asn, Phe, Glu) !8#status predicted\ !$115 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8predicted\ !$129,131,133,135,140 #binding_site calcium (Asp, Asp, Asp, Gln, Glu) !8#status predicted SUMMARY #length 148 #molecular-weight 16680 #checksum 2013 SEQUENCE /// ENTRY MCSW #type complete TITLE calmodulin - scallop (Patinopecten sp.) (tentative sequence) ALTERNATE_NAMES modulator protein ORGANISM #formal_name Patinopecten sp. DATE 19-Feb-1984 #sequence_revision 30-Sep-1988 #text_change 31-Mar-2000 ACCESSIONS A03023 REFERENCE A91962 !$#authors Toda, H.; Yazawa, M.; Kondo, K.; Honma, T.; Narita, K.; !1Yagi, K. !$#journal J. Biochem. (1981) 90:1493-1505 !$#title Amino acid sequence of calmodulin from scallop !1(Patinopecten) adductor muscle. !$#cross-references MUID:82167261; PMID:7338518 !$#accession A03023 !'##molecule_type protein !'##residues 1-148 ##label TOD CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS acetylated amino end; calcium binding; duplication; EF hand; !1methylated amino acid FEATURE !$7-39 #domain calmodulin repeat homology #label EF1\ !$43-75 #domain calmodulin repeat homology #label EF2\ !$80-112 #domain calmodulin repeat homology #label EF3\ !$116-148 #domain calmodulin repeat homology #label EF4\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$20,22,24,26,31 #binding_site calcium (Asp, Asp, Asp, Thr, Glu) !8#status predicted\ !$56,58,60,62,67 #binding_site calcium (Asp, Asp, Asp, Thr, Glu) !8#status predicted\ !$93,95,97,99,104 #binding_site calcium (Asp, Asp, Asp, Phe, Glu) !8#status predicted\ !$115 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental\ !$129,131,133,135,140 #binding_site calcium (Asp, Asp, Asp, Gln, Glu) !8#status predicted SUMMARY #length 148 #molecular-weight 16681 #checksum 1613 SEQUENCE /// ENTRY MCXAM #type complete TITLE calmodulin - sea anemone (Metridium senile) (tentative sequence) ALTERNATE_NAMES modulator protein ORGANISM #formal_name Metridium senile #common_name brown sea anemone, frilled sea anemone DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 24-Nov-1999 ACCESSIONS A90223; A03023 REFERENCE A90223 !$#authors Takagi, T.; Nemoto, T.; Konishi, K.; Yazawa, M.; Yagi, K. !$#journal Biochem. Biophys. Res. Commun. (1980) 96:377-381 !$#title The amino acid sequence of the calmodulin obtained from sea !1anemone (Metridium senile) muscle. !$#cross-references MUID:81062446; PMID:6108109 !$#accession A90223 !'##molecule_type protein !'##residues 1-148 ##label TAK CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS blocked amino end; calcium binding; duplication; EF hand; !1methylated amino acid FEATURE !$7-39 #domain calmodulin repeat homology #label EF1\ !$43-75 #domain calmodulin repeat homology #label EF2\ !$80-112 #domain calmodulin repeat homology #label EF3\ !$116-148 #domain calmodulin repeat homology #label EF4\ !$1 #modified_site blocked amino end (Ala) #status !8experimental\ !$20,22,24,26,31 #binding_site calcium (Asp, Asp, Asp, Thr, Glu) !8#status predicted\ !$56,58,60,62,67 #binding_site calcium (Asp, Asp, Asp, Thr, Glu) !8#status predicted\ !$93,95,97,99,104 #binding_site calcium (Asp, Asp, Asp, Phe, Glu) !8#status predicted\ !$115 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental\ !$129,131,133,135,140 #binding_site calcium (Asp, Asp, Asp, Gln, Glu) !8#status predicted SUMMARY #length 148 #molecular-weight 16708 #checksum 1352 SEQUENCE /// ENTRY MCJZR #type complete TITLE calmodulin - sea pansy (Renilla reniformis) (tentative sequence) ALTERNATE_NAMES modulator protein ORGANISM #formal_name Renilla reniformis #common_name sea pansy DATE 31-Dec-1991 #sequence_revision 30-Jun-1992 #text_change 24-Nov-1999 ACCESSIONS A90036; A03023 REFERENCE A90036 !$#authors Jamieson Jr., G.A.; Bronson, D.D.; Schachat, F.H.; Vanaman, !1T.C. !$#journal Ann. N. Y. Acad. Sci. (1980) 356:1-13 !$#title Structure and function relationships among calmodulins and !1troponin C-like proteins from divergent eukaryotic !1organisms. !$#cross-references MUID:81205529; PMID:6263143 !$#accession A90036 !'##molecule_type protein !'##residues 1-147 ##label JAM CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS blocked amino end; calcium binding; duplication; EF hand; !1methylated amino acid FEATURE !$6-38 #domain calmodulin repeat homology #label EF1\ !$42-74 #domain calmodulin repeat homology #label EF2\ !$79-111 #domain calmodulin repeat homology #label EF3\ !$115-147 #domain calmodulin repeat homology #label EF4\ !$1 #modified_site blocked amino end (Ala) #status !8experimental\ !$19,21,23,25,30 #binding_site calcium (Asp, Asp, Asp, Thr, Glu) !8#status predicted\ !$55,57,59,61,66 #binding_site calcium (Asp, Asp, Asx, Thr, Glu) !8#status predicted\ !$92,94,96,98,103 #binding_site calcium (Asp, Asp, Asp, Phe, Glu) !8#status predicted\ !$114 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental\ !$128,130,132,134,139 #binding_site calcium (Asp, Asp, Asp, Gln, Glu) !8#status predicted SUMMARY #length 147 #molecular-weight 16580 #checksum 8477 SEQUENCE /// ENTRY MCUMAK #type complete TITLE calmodulin - Achlya klebsiana ALTERNATE_NAMES modulator protein ORGANISM #formal_name Achlya klebsiana DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 22-Jun-1999 ACCESSIONS A34450 REFERENCE A34450 !$#authors LeJohn, H.B. !$#journal J. Biol. Chem. (1989) 264:19366-19372 !$#title Structure and expression of fungal calmodulin gene. !$#cross-references MUID:90037077; PMID:2808429 !$#accession A34450 !'##molecule_type DNA !'##residues 1-149 ##label LEJ !'##cross-references GB:J05116; NID:g166303; PIDN:AAA32627.1; !1PID:g166304 CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS calcium binding; duplication; EF hand; methylated amino acid FEATURE !$2-149 #product calmodulin #status predicted #label MAT\ !$8-40 #domain calmodulin repeat homology #label EF1\ !$44-76 #domain calmodulin repeat homology #label EF2\ !$81-113 #domain calmodulin repeat homology #label EF3\ !$117-149 #domain calmodulin repeat homology #label EF4\ !$21,23,25,27,32 #binding_site calcium (Asp, Asp, Asp, Thr, Glu) !8#status predicted\ !$57,59,61,63,68 #binding_site calcium (Asp, Asp, Asn, Thr, Glu) !8#status predicted\ !$94,96,98,100,105 #binding_site calcium (Asp, Asp, Asn, Phe, Glu) !8#status predicted\ !$116 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8predicted\ !$130,132,134,136,141 #binding_site calcium (Asp, Asp, Asp, Gln, Glu) !8#status predicted SUMMARY #length 149 #molecular-weight 16696 #checksum 3914 SEQUENCE /// ENTRY MCMRP #type complete TITLE calmodulin - cornucopia mushroom ALTERNATE_NAMES modulator protein ORGANISM #formal_name Pleurotus cornucopiae #common_name cornucopia mushroom DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 17-Apr-1998 ACCESSIONS JK0014 REFERENCE A94538 !$#authors Toda, H.; Sakiyama, F.; Yokono, T.; Miura, K.; Nakamura, T. !$#submission submitted to JIPID, May 1988 !$#accession JK0014 !'##molecule_type protein !'##residues 1-148 ##label TO1 REFERENCE A94301 !$#authors Toda, H.; Sakiyama, F.; Yokono, T.; Miura, K.; Nakamura, T. !$#journal Seikagaku (1987) 59:589 !$#title Amino acid sequence of Pleurotus cornucopiae calmodulin. !$#contents annotation !$#note author-supplied citation !$#note unlike other calmodulins, Lys-115 is not trimethylated CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS acetylated amino end; calcium binding; duplication; EF hand FEATURE !$7-39 #domain calmodulin repeat homology #label EF1\ !$43-75 #domain calmodulin repeat homology #label EF2\ !$80-112 #domain calmodulin repeat homology #label EF3\ !$116-148 #domain calmodulin repeat homology #label EF4\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$20,22,24,26,31 #binding_site calcium (Asp, Asp, Asp, Thr, Glu) !8#status predicted\ !$56,58,60,62,67 #binding_site calcium (Asp, Asp, Asn, Thr, Glu) !8#status predicted\ !$93,95,97,99,104 #binding_site calcium (Asp, Asp, Asn, Tyr, Glu) !8#status predicted\ !$115 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8absent\ !$129,131,133,135,140 #binding_site calcium (Asp, Asp, Asp, Gln, Glu) !8#status predicted SUMMARY #length 148 #molecular-weight 16707 #checksum 1964 SEQUENCE /// ENTRY MCDO #type complete TITLE calmodulin - slime mold (Dictyostelium discoideum) (tentative sequence) ALTERNATE_NAMES modulator protein ORGANISM #formal_name Dictyostelium discoideum DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 31-Mar-2000 ACCESSIONS A03029; A25232 REFERENCE A03029 !$#authors Marshak, D.R.; Clarke, M.; Roberts, D.M.; Watterson, D.M. !$#journal Biochemistry (1984) 23:2891-2899 !$#title Structural and functional properties of calmodulin from the !1eukaryotic microorganism Dictyostelium discoideum. !$#cross-references MUID:84280856; PMID:6087882 !$#accession A03029 !'##molecule_type protein !'##residues 1-151 ##label MAR !'##experimental_source strain AX3 REFERENCE A25232 !$#authors Goldhagen, H.; Clarke, M. !$#journal Mol. Cell. Biol. (1986) 6:1851-1854 !$#title Identification of the single gene for calmodulin in !1Dictyostelium discoideum. !$#cross-references MUID:87064473; PMID:3785182 !$#accession A25232 !'##molecule_type mRNA !'##residues 13-151 ##label GOL !'##cross-references GB:M13009; NID:g167675; PIDN:AAA33171.1; !1PID:g167676 !'##note the authors translated the codon CTT for residue 114 as Glu CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS blocked amino end; calcium binding; duplication; EF hand FEATURE !$9-41 #domain calmodulin repeat homology #label EF1\ !$45-77 #domain calmodulin repeat homology #label EF2\ !$82-114 #domain calmodulin repeat homology #label EF3\ !$118-150 #domain calmodulin repeat homology #label EF4\ !$1 #modified_site blocked amino end #status !8experimental\ !$22,24,26,28,33 #binding_site calcium (Asp, Asp, Asp, Ser, Glu) !8#status predicted\ !$58,60,62,64,69 #binding_site calcium (Asp, Asp, Asn, Asn, Glu) !8#status predicted\ !$95,97,99,101,106 #binding_site calcium (Asp, Asp, Asn, Tyr, Glu) !8#status predicted\ !$117 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8absent\ !$131,133,135,137,142 #binding_site calcium (Asp, Asp, Asp, Gln, Glu) !8#status predicted SUMMARY #length 151 #molecular-weight 17020 #checksum 2580 SEQUENCE /// ENTRY MCZQF #type complete TITLE calmodulin - malaria parasite (Plasmodium falciparum) ALTERNATE_NAMES modulator protein; phosphodiesterase activator; phosphorylase kinase delta chain ORGANISM #formal_name Plasmodium falciparum DATE 22-Apr-1993 #sequence_revision 01-Sep-1995 #text_change 09-Jun-2000 ACCESSIONS B45594; A49774; S21813 REFERENCE A45594 !$#authors Robson, K.J.; Jennings, M.W. !$#journal Mol. Biochem. Parasitol. (1991) 46:19-34 !$#title The structure of the calmodulin gene of Plasmodium !1falciparum. !$#cross-references MUID:91304518; PMID:1852174 !$#accession B45594 !'##molecule_type DNA !'##residues 1-149 ##label ROB !'##cross-references GB:M59770; NID:g160127; PIDN:AAA29510.1; !1PID:g160128 !'##note sequence extracted from NCBI backbone (NCBIN:42930, !1NCBIP:42935) REFERENCE A49774 !$#authors Cowman, A.F.; Galatis, D. !$#journal Exp. Parasitol. (1991) 73:269-275 !$#title Plasmodium falciparum: the calmodulin gene is not amplified !1or overexpressed in chloroquine resistant or sensitive !1isolates. !$#cross-references MUID:92008475; PMID:1915742 !$#accession A49774 !'##molecule_type DNA !'##residues 1-149 ##label COW !'##cross-references EMBL:X56950 GENETICS !$#map_position 14 !$#introns 27/1 !$#note only one gene for calmodulin was found FUNCTION !$#description calcium-dependent regulation of a number of essential !1enzymes CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS acetylated amino end; calcium binding; duplication; EF hand; !1methylated amino acid FEATURE !$2-149 #product calmodulin #status predicted #label MAT\ !$8-40 #domain calmodulin repeat homology #label EF1\ !$44-76 #domain calmodulin repeat homology #label EF2\ !$81-113 #domain calmodulin repeat homology #label EF3\ !$117-149 #domain calmodulin repeat homology #label EF4\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status predicted\ !$21,23,25,27,32 #binding_site calcium (Asp, Asp, Asp, Thr, Glu) !8#status predicted\ !$57,59,61,63,68 #binding_site calcium (Asp, Asp, Asn, Thr, Glu) !8#status predicted\ !$94,96,98,100,105 #binding_site calcium (Asp, Asp, Asp, Tyr, Glu) !8#status predicted\ !$116 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8predicted\ !$130,132,134,136,141 #binding_site calcium (Asp, Asp, Asp, Gln, Glu) !8#status predicted SUMMARY #length 149 #molecular-weight 16931 #checksum 4096 SEQUENCE /// ENTRY MCTE #type complete TITLE calmodulin - Tetrahymena pyriformis ALTERNATE_NAMES modulator protein ORGANISM #formal_name Tetrahymena pyriformis DATE 18-Aug-1982 #sequence_revision 10-Nov-1995 #text_change 16-Jun-2000 ACCESSIONS S28956; A36684; A03027 REFERENCE S28956 !$#authors Takemasa, T.; Takagi, T.; Edamatsu, M.; Watanabe, Y. !$#journal Biochim. Biophys. Acta (1992) 1132:219-221 !$#title Calmodulin cDNAs from two species of Tetrahymena. !$#cross-references MUID:93003329; PMID:1339295 !$#accession S28956 !'##molecule_type mRNA !'##residues 1-149 ##label TAK !'##cross-references EMBL:D10521; NID:g217404; PIDN:BAA01391.1; !1PID:g217405 !'##experimental_source strain NT-1 REFERENCE A36684 !$#authors Hinrichsen, R.; Wilson, E.; Lukas, T.; Craig, T.; Schultz, !1J.; Watterson, D.M. !$#journal J. Cell Biol. (1990) 111:2537-2542 !$#title Analysis of the molecular basis of calmodulin defects that !1affect ion channel-mediated cellular responses: !1site-specific mutagenesis and microinjection. !$#cross-references MUID:91115946; PMID:1703538 !$#accession A36684 !'##molecule_type protein !'##residues 2-17,'A',19-149 ##label HIN REFERENCE A03027 !$#authors Yazawa, M.; Yagi, K.; Toda, H.; Kondo, K.; Narita, K.; !1Yamazaki, R.; Sobue, K.; Kakiuchi, S.; Nagao, S.; Nozawa, Y. !$#journal Biochem. Biophys. Res. Commun. (1981) 99:1051-1057 !$#title The amino acid sequence of the Tetrahymena calmodulin which !1specifically interacts with guanylate cyclase. !$#cross-references MUID:81255811; PMID:6114734 !$#accession A03027 !'##molecule_type protein !'##residues 2-60,'D',62-81,'S',83-97,'D',99-101,'T',103-146,'AK' !1##label YAZ GENETICS !$#genetic_code SGC5 CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS acetylated amino end; calcium binding; duplication; EF hand; !1methylated amino acid FEATURE !$8-40 #domain calmodulin repeat homology #label EF1\ !$44-76 #domain calmodulin repeat homology #label EF2\ !$81-113 #domain calmodulin repeat homology #label EF3\ !$117-149 #domain calmodulin repeat homology #label EF4\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental\ !$21,23,25,27,32 #binding_site calcium (Asp, Asp, Asp, Thr, Glu) !8#status predicted\ !$57,59,61,63,68 #binding_site calcium (Asp, Asp, Asn, Thr, Glu) !8#status predicted\ !$94,96,98,100,105 #binding_site calcium (Asp, Asp, Asn, Leu, Glu) !8#status predicted\ !$116 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental\ !$130,132,134,136,141 #binding_site calcium (Asp, Asp, Asp, His, Glu) !8#status predicted SUMMARY #length 149 #molecular-weight 16808 #checksum 4203 SEQUENCE /// ENTRY MCPP #type complete TITLE calmodulin - Paramecium tetraurelia ALTERNATE_NAMES modulator protein ORGANISM #formal_name Paramecium tetraurelia DATE 30-Sep-1988 #sequence_revision 30-Jun-1992 #text_change 07-Dec-1999 ACCESSIONS A35603; JK0006 REFERENCE A35603 !$#authors Kink, J.A.; Maley, M.E.; Preston, R.R.; Ling, K.Y.; !1Wallen-Friedman, M.A.; Saimi, Y.; Kung, C. !$#journal Cell (1990) 62:165-174 !$#title Mutations in Paramecium calmodulin indicate functional !1differences between the C-terminal and N-terminal lobes in !1vivo. !$#cross-references MUID:90304906; PMID:2163766 !$#accession A35603 !'##molecule_type DNA !'##residues 1-149 ##label KIN !'##cross-references GB:M34540; NID:g159993; PIDN:AAA29443.1; !1PID:g159994 !'##note the authors translated the codon ACA for residue 6 as Leu in !1Fig. 2 REFERENCE JK0006 !$#authors Schaefer, W.H.; Lukas, T.J.; Blair, I.A.; Schultz, J.E.; !1Watterson, D.M. !$#journal J. Biol. Chem. (1987) 262:1025-1029 !$#title Amino acid sequence of a novel calmodulin from Paramecium !1tetraurelia that contains dimethyllysine in the first !1domain. !$#cross-references MUID:87109207; PMID:3100523 !$#accession JK0006 !'##molecule_type protein !'##residues 2-149 ##label SCH GENETICS !$#genetic_code SGC5 CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS acetylated amino end; calcium binding; duplication; EF hand; !1methylated amino acid FEATURE !$2-149 #product calmodulin #status experimental #label MAT\ !$8-40 #domain calmodulin repeat homology #label EF1\ !$44-76 #domain calmodulin repeat homology #label EF2\ !$81-113 #domain calmodulin repeat homology #label EF3\ !$117-149 #domain calmodulin repeat homology #label EF4\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental\ !$14 #modified_site N6,N6-dimethyllysine (Lys) #status !8experimental\ !$21,23,25,27,32 #binding_site calcium (Asp, Asp, Asp, Thr, Glu) !8#status experimental\ !$57,59,61,63,68 #binding_site calcium (Asp, Asp, Asn, Thr, Glu) !8#status experimental\ !$94,96,98,100,105 #binding_site calcium (Asp, Asp, Asn, Leu, Glu) !8#status experimental\ !$116 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental\ !$130,132,134,136,141 #binding_site calcium (Asp, Asp, Asp, His, Glu) !8#status experimental SUMMARY #length 149 #molecular-weight 16803 #checksum 4713 SEQUENCE /// ENTRY MCUTG #type complete TITLE calmodulin - Trypanosoma brucei gambiense ALTERNATE_NAMES modulator protein ORGANISM #formal_name Trypanosoma brucei gambiense DATE 17-Mar-1987 #sequence_revision 30-Jun-1992 #text_change 17-Apr-1998 ACCESSIONS A03028 REFERENCE A03028 !$#authors Tschudi, C.; Young, A.S.; Ruben, L.; Patton, C.L.; Richards, !1F.F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:3998-4002 !$#title Calmodulin genes in trypanosomes are tandemly repeated and !1produce multiple mRNAs with a common 5' leader sequence. !$#cross-references MUID:85216620; PMID:3858856 !$#accession A03028 !'##molecule_type DNA !'##residues 1-149 ##label TSC !'##cross-references GB:K02944 !'##note calmodulin is encoded by three identical intronless genes in !1this organism CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS calcium binding; duplication; EF hand; methylated amino acid FEATURE !$2-149 #product calmodulin #status predicted #label MAT\ !$8-40 #domain calmodulin repeat homology #label EF1\ !$44-76 #domain calmodulin repeat homology #label EF2\ !$81-113 #domain calmodulin repeat homology #label EF3\ !$117-149 #domain calmodulin repeat homology #label EF4\ !$21,23,25,27,32 #binding_site calcium (Asp, Asp, Asp, Thr, Glu) !8#status predicted\ !$57,59,61,63,68 #binding_site calcium (Asp, Asp, Ser, Thr, Glu) !8#status predicted\ !$94,96,98,100,105 #binding_site calcium (Asp, Asp, Asn, Phe, Glu) !8#status predicted\ !$116 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental\ !$130,132,134,136,141 #binding_site calcium (Asp, Asp, Asp, Gln, Glu) !8#status predicted SUMMARY #length 149 #molecular-weight 16838 #checksum 4418 SEQUENCE /// ENTRY MCUTC #type complete TITLE calmodulin - Trypanosoma cruzi ALTERNATE_NAMES modulator protein ORGANISM #formal_name Trypanosoma cruzi DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 22-Jun-1999 ACCESSIONS S10995 REFERENCE S10995 !$#authors Chung, S.H.; Swindle, J. !$#journal Nucleic Acids Res. (1990) 18:4561-4569 !$#title Linkage of the calmodulin and ubiquitin loci in Trypanosoma !1cruzi. !$#cross-references MUID:90356392; PMID:2167471 !$#accession S10995 !'##molecule_type DNA !'##residues 1-149 ##label SWI !'##cross-references EMBL:X52096; NID:g10603; PIDN:CAA36316.1; !1PID:g10604 GENETICS !$#gene CalA2 CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS calcium binding; duplication; EF hand; methylated amino acid FEATURE !$2-149 #product calmodulin #status predicted #label MAT\ !$8-40 #domain calmodulin repeat homology #label EF1\ !$44-76 #domain calmodulin repeat homology #label EF2\ !$81-113 #domain calmodulin repeat homology #label EF3\ !$117-149 #domain calmodulin repeat homology #label EF4\ !$21,23,25,27,32 #binding_site calcium (Asp, Asp, Asp, Thr, Glu) !8#status predicted\ !$57,59,61,63,68 #binding_site calcium (Asp, Asp, Ser, Thr, Glu) !8#status predicted\ !$94,96,98,100,105 #binding_site calcium (Asp, Asp, Asn, Phe, Glu) !8#status predicted\ !$116 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8predicted\ !$130,132,134,136,141 #binding_site calcium (Asp, Asp, Asp, Gln, Glu) !8#status predicted SUMMARY #length 149 #molecular-weight 16824 #checksum 5094 SEQUENCE /// ENTRY MCEG #type complete TITLE calmodulin - Euglena gracilis ALTERNATE_NAMES modulator protein ORGANISM #formal_name Euglena gracilis DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 17-Apr-1998 ACCESSIONS S21212; JK0008 REFERENCE S21212 !$#authors Toda, H.; Yazawa, M.; Yagi, K. !$#journal Eur. J. Biochem. (1992) 205:653-660 !$#title Amino acid sequence of calmodulin from Euglena gracilis. !$#cross-references MUID:92241300; PMID:1572365 !$#accession S21212 !'##molecule_type protein !'##residues 1-148 ##label TO2 CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS acetylated amino end; calcium binding; duplication; EF hand; !1methylated amino acid FEATURE !$7-39 #domain calmodulin repeat homology #label EF1\ !$43-75 #domain calmodulin repeat homology #label EF2\ !$80-112 #domain calmodulin repeat homology #label EF3\ !$116-148 #domain calmodulin repeat homology #label EF4\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$20,22,24,26,31 #binding_site calcium (Asp, Asp, Asp, Thr, Glu) !8#status predicted\ !$56,58,60,62,67 #binding_site calcium (Asp, Asp, Ser, Thr, Glu) !8#status predicted\ !$93,95,97,99,104 #binding_site calcium (Asp, Asp, Asn, Phe, Glu) !8#status predicted\ !$115,148 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental\ !$129,131,133,135,140 #binding_site calcium (Asp, Asp, Asp, Gln, Glu) !8#status predicted SUMMARY #length 148 #molecular-weight 16724 #checksum 2414 SEQUENCE /// ENTRY MCBH #type complete TITLE calmodulin - barley ALTERNATE_NAMES modulator protein ORGANISM #formal_name Hordeum vulgare #common_name barley DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 22-Jun-1999 ACCESSIONS A30900 REFERENCE A30900 !$#authors Ling, V.; Zielinski, R.E. !$#journal Plant Physiol. (1989) 90:714-719 !$#title Cloning of cDNA sequences encoding the calcium-binding !1protein, calmodulin, from barley (Hordeum vulgare L.). !$#accession A30900 !'##molecule_type mRNA !'##residues 1-149 ##label LIN !'##cross-references GB:M27303; NID:g167007; PIDN:AAA32938.1; !1PID:g167008 CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS calcium binding; duplication; EF hand; methylated amino acid FEATURE !$2-149 #product calmodulin #status predicted #label MAT\ !$8-40 #domain calmodulin repeat homology #label EF1\ !$44-76 #domain calmodulin repeat homology #label EF2\ !$81-113 #domain calmodulin repeat homology #label EF3\ !$117-149 #domain calmodulin repeat homology #label EF4\ !$21,23,25,27,32 #binding_site calcium (Asp, Asp, Asp, Cys, Glu) !8#status predicted\ !$57,59,61,63,68 #binding_site calcium (Asp, Asp, Asn, Thr, Glu) !8#status predicted\ !$94,96,98,100,105 #binding_site calcium (Asp, Asp, Asn, Phe, Glu) !8#status predicted\ !$116 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8predicted\ !$130,132,134,136,141 #binding_site calcium (Asp, Asp, Asp, Gln, Glu) !8#status predicted SUMMARY #length 149 #molecular-weight 16832 #checksum 4296 SEQUENCE /// ENTRY MCAA #type complete TITLE calmodulin - alfalfa ALTERNATE_NAMES modulator protein ORGANISM #formal_name Medicago sativa #common_name alfalfa DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 22-Jun-1999 ACCESSIONS S10533 REFERENCE S10533 !$#authors Barnett, M.J.; Long, S.R. !$#journal Nucleic Acids Res. (1990) 18:3395 !$#title Nucleotide sequence of an alfalfa calmodulin cDNA. !$#cross-references MUID:90287719; PMID:2356128 !$#accession S10533 !'##molecule_type mRNA !'##residues 1-149 ##label BAR !'##cross-references EMBL:X52398; NID:g19578; PIDN:CAA36644.1; !1PID:g19579 CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS calcium binding; duplication; EF hand; methylated amino acid FEATURE !$2-149 #product calmodulin #status predicted #label MAT\ !$8-40 #domain calmodulin repeat homology #label EF1\ !$44-76 #domain calmodulin repeat homology #label EF2\ !$81-113 #domain calmodulin repeat homology #label EF3\ !$117-149 #domain calmodulin repeat homology #label EF4\ !$21,23,25,27,32 #binding_site calcium (Asp, Asp, Asp, Cys, Glu) !8#status predicted\ !$57,59,61,63,68 #binding_site calcium (Asp, Asp, Asn, Thr, Glu) !8#status predicted\ !$94,96,98,100,105 #binding_site calcium (Asp, Asp, Asn, Phe, Glu) !8#status predicted\ !$116 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8predicted\ !$130,132,134,136,141 #binding_site calcium (Asp, Asp, Asp, Gln, Glu) !8#status predicted SUMMARY #length 149 #molecular-weight 16862 #checksum 4502 SEQUENCE /// ENTRY MCPZDC #type complete TITLE calmodulin - carrot ALTERNATE_NAMES modulator protein ORGANISM #formal_name Daucus carota #common_name carrot DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 22-Jun-1999 ACCESSIONS S16138 REFERENCE S16138 !$#authors Perera, I.V.; Zielinski, R.E. !$#submission submitted to the EMBL Data Library, July 1991 !$#description Synthesis and accumulation of calmodulin in suspension !1cultures of carrot. !$#accession S16138 !'##molecule_type mRNA !'##residues 1-149 ##label PER !'##cross-references EMBL:X59751; NID:g18325; PIDN:CAA42423.1; !1PID:g18326 CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS calcium binding; duplication; EF hand; methylated amino acid FEATURE !$2-149 #product calmodulin #status predicted #label MAT\ !$8-40 #domain calmodulin repeat homology #label EF1\ !$44-76 #domain calmodulin repeat homology #label EF2\ !$81-113 #domain calmodulin repeat homology #label EF3\ !$117-149 #domain calmodulin repeat homology #label EF4\ !$21,23,25,27,32 #binding_site calcium (Asp, Asp, Asp, Cys, Glu) !8#status predicted\ !$57,59,61,63,68 #binding_site calcium (Asp, Asp, Asn, Thr, Glu) !8#status predicted\ !$94,96,98,100,105 #binding_site calcium (Asp, Asp, Asn, Phe, Glu) !8#status predicted\ !$116 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8predicted\ !$130,132,134,136,141 #binding_site calcium (Asp, Asp, Asp, Gln, Glu) !8#status predicted SUMMARY #length 149 #molecular-weight 16848 #checksum 4494 SEQUENCE /// ENTRY MCSP #type complete TITLE calmodulin - spinach (tentative sequence) ALTERNATE_NAMES modulator protein ORGANISM #formal_name Spinacia oleracea #common_name spinach DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 31-Mar-2000 ACCESSIONS A03024 REFERENCE A03024 !$#authors Lukas, T.J.; Iverson, D.B.; Schleicher, M.; Watterson, D.M. !$#journal Plant Physiol. (1984) 75:788-795 !$#title Structural characterization of a higher plant calmodulin: !1Spinacia oleracea. !$#accession A03024 !'##molecule_type protein !'##residues 1-148 ##label LUK CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS blocked amino end; calcium binding; duplication; EF hand; !1methylated amino acid FEATURE !$7-39 #domain calmodulin repeat homology #label EF1\ !$43-75 #domain calmodulin repeat homology #label EF2\ !$80-112 #domain calmodulin repeat homology #label EF3\ !$116-148 #domain calmodulin repeat homology #label EF4\ !$1 #modified_site blocked amino end #status !8experimental\ !$20,22,24,26,31 #binding_site calcium (Asp, Asp, Asp, Cys, Glu) !8#status predicted\ !$56,58,60,62,67 #binding_site calcium (Asp, Asp, Asn, Thr, Glu) !8#status predicted\ !$93,95,97,99,104 #binding_site calcium (Asp, Asp, Asn, Phe, Glu) !8#status predicted\ !$115 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental\ !$129,131,133,135,140 #binding_site calcium (Asp, Asp, Asp, Gln, Glu) !8#status predicted SUMMARY #length 148 #molecular-weight 16728 #checksum 958 SEQUENCE /// ENTRY MCWT #type complete TITLE calmodulin - wheat ALTERNATE_NAMES modulator protein ORGANISM #formal_name Triticum aestivum #common_name common wheat DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 07-May-1999 ACCESSIONS A03025; PC2046 REFERENCE A03025 !$#authors Toda, H.; Yazawa, M.; Sakiyama, F.; Yagi, K. !$#journal J. Biochem. (1985) 98:833-842 !$#title Amino acid sequence of calmodulin from wheat germ. !$#cross-references MUID:86111690; PMID:4086472 !$#accession A03025 !'##molecule_type protein !'##residues 1-149 ##label TOD REFERENCE PC2046 !$#authors Toda, H.; Yazawo, M.; Sakiyama, F.; Yagi, K. !$#journal J. Biochem. (1994) 115:367 !$#title Correction: Amino acid sequence of calmodulin from wheat !1germ. !$#cross-references MUID:94266769; PMID:8206888 !$#accession PC2046 !'##molecule_type protein !'##residues 1-8;10-14 ##label TO2 CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS acetylated amino end; calcium binding; duplication; EF hand; !1methylated amino acid FEATURE !$7-40 #domain calmodulin repeat homology #label EF1\ !$44-76 #domain calmodulin repeat homology #label EF2\ !$81-113 #domain calmodulin repeat homology #label EF3\ !$117-149 #domain calmodulin repeat homology #label EF4\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$21,23,25,27,32 #binding_site calcium (Asp, Asp, Asp, Cys, Glu) !8#status predicted\ !$57,59,61,63,68 #binding_site calcium (Asp, Asp, Asn, Thr, Glu) !8#status predicted\ !$94,96,98,100,105 #binding_site calcium (Asp, Asp, Asp, Phe, Glu) !8#status predicted\ !$116 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental\ !$130,132,134,136,141 #binding_site calcium (Asp, Asp, Asp, Gln, Glu) !8#status predicted SUMMARY #length 149 #molecular-weight 16829 #checksum 3927 SEQUENCE /// ENTRY MCPO #type complete TITLE calmodulin - potato ALTERNATE_NAMES modulator protein ORGANISM #formal_name Solanum tuberosum #common_name potato DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 22-Jun-1999 ACCESSIONS A32556; S77733 REFERENCE A32556 !$#authors Jena, P.K.; Reddy, A.S.N.; Poovaiah, B.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:3644-3648 !$#title Molecular cloning and sequencing of a cDNA for plant !1calmodulin: signal-induced changes in the expression of !1calmodulin. !$#cross-references MUID:89264480; PMID:2726741 !$#accession A32556 !'##molecule_type mRNA !'##residues 1-149 ##label JEN !'##cross-references GB:J04559; NID:g169476; PIDN:AAA74405.1; !1PID:g169477 REFERENCE S60234 !$#authors Takezawa, D.; Liu, Z.H.; An, G.; Poovaiah, B.W. !$#journal Plant Mol. Biol. (1995) 27:693-703 !$#title Calmodulin gene family in potato: developmental and !1touch-induced expression of the mRNA encoding a novel !1isoform. !$#cross-references MUID:95244831; PMID:7727747 !$#accession S77733 !'##molecule_type DNA !'##residues 1-149 ##label TAK !'##note the authors did not translate the codon for residue 1 !'##note the authors mention an intron at position 26-Gly CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS calcium binding; duplication; EF hand; methylated amino acid FEATURE !$2-149 #product calmodulin #status predicted #label MAT\ !$8-40 #domain calmodulin repeat homology #label EF1\ !$44-76 #domain calmodulin repeat homology #label EF2\ !$81-113 #domain calmodulin repeat homology #label EF3\ !$117-149 #domain calmodulin repeat homology #label EF4\ !$21,23,25,27,32 #binding_site calcium (Asp, Asp, Asp, Cys, Glu) !8#status predicted\ !$57,59,61,63,68 #binding_site calcium (Asp, Asp, Asn, Thr, Glu) !8#status predicted\ !$94,96,98,100,105 #binding_site calcium (Asp, Asp, Asn, Phe, Glu) !8#status predicted\ !$116 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8predicted\ !$130,132,134,136,141 #binding_site calcium (Asp, Asp, Asp, Gln, Glu) !8#status predicted SUMMARY #length 149 #molecular-weight 16904 #checksum 3176 SEQUENCE /// ENTRY MCKM #type complete TITLE calmodulin - Chlamydomonas reinhardtii ALTERNATE_NAMES modulator protein ORGANISM #formal_name Chlamydomonas reinhardtii DATE 17-Mar-1987 #sequence_revision 30-Sep-1991 #text_change 22-Jun-1999 ACCESSIONS A32005; A03030; JK0003 REFERENCE A32005 !$#authors Zimmer, W.E.; Schloss, J.A.; Silflow, C.D.; Youngblom, J.; !1Watterson, D.M. !$#journal J. Biol. Chem. (1988) 263:19370-19383 !$#title Structural organization, DNA sequence, and expression of the !1calmodulin gene. !$#cross-references MUID:89066752; PMID:3198631 !$#accession A32005 !'##molecule_type DNA !'##residues 1-163 ##label ZIM !'##cross-references GB:M20729; NID:g167410; PIDN:AAA33083.1; !1PID:g167411 !'##note the authors translated the codon GGT for residue 136 as Asn REFERENCE JK0003 !$#authors Lukas, T.J.; Wiggins, M.E.; Watterson, D.M. !$#journal Plant Physiol. (1985) 78:477-483 !$#title Amino acid sequence of a novel calmodulin from the !1unicellular alga Chlamydomonas. !$#accession A03030 !'##molecule_type protein !'##residues 2-163 ##label LUK COMMENT The methylation state of Lys-119 may be important in the !1quantitative regulation of plant NAD kinase activity. Among !1the eukaryotic calmodulins, only the Chlamydomonas and !1Dictyostelium proteins have an unmethylated lysine at this !1position, and only these proteins can increase (4- to !16-fold) the maximal activation of this enzyme. COMMENT This protein is unusual among eukaryotic calmodulins in !1having an 11-residue extension of its carboxyl end. GENETICS !$#introns 30/1; 82/3; 109/3; 131/2; 144/3 CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS acetylated amino end; calcium binding; duplication; EF hand FEATURE !$2-163 #product calmodulin #status experimental #label MAT\ !$11-43 #domain calmodulin repeat homology #label EF1\ !$47-79 #domain calmodulin repeat homology #label EF2\ !$84-116 #domain calmodulin repeat homology #label EF3\ !$120-152 #domain calmodulin repeat homology #label EF4\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental\ !$24,26,28,30,35 #binding_site calcium (Asp, Asp, Asp, Thr, Glu) !8#status predicted\ !$60,62,64,66,71 #binding_site calcium (Asp, Asp, Asn, Thr, Glu) !8#status predicted\ !$97,99,101,103,108 #binding_site calcium (Asp, Asp, Asn, Phe, Glu) !8#status predicted\ !$119 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8absent\ !$133,135,137,139,144 #binding_site calcium (Asp, Asp, Asp, Gln, Glu) !8#status predicted SUMMARY #length 163 #molecular-weight 18296 #checksum 8158 SEQUENCE /// ENTRY MCCHM #type complete TITLE calmodulin, striated muscle - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 15-Nov-1984 #sequence_revision 30-Jun-1992 #text_change 22-Jun-1999 ACCESSIONS A03026 REFERENCE A03026 !$#authors Stein, J.P.; Munjaal, R.P.; Lagace, L.; Lai, E.C.; O'Malley, !1B.W.; Means, A.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:6485-6489 !$#title Tissue-specific expression of a chicken calmodulin !1pseudogene lacking intervening sequences. !$#cross-references MUID:84042496; PMID:6579534 !$#accession A03026 !'##molecule_type DNA !'##residues 1-149 ##label STE !'##cross-references GB:K00510; NID:g211537; PIDN:AAA48693.1; !1PID:g211542 COMMENT This sequence differs from other calmodulin sequences by at !1least 13%. Many of the differences are nonconservative and !1some probably render the first and fourth potential !1calcium-binding regions nonfunctional. COMMENT The authors' data suggest that there are at least two !1different calmodulin genes in the chicken genome, cCM1 and !1cCL1. Whereas cCL1 is thought to be the primary gene !1responsible for production of calmodulin, cCM1 codes for the !1sequence shown and is expressed only in cardiac and !1skeletal, not smooth, muscle. GENETICS !$#gene cCM1 CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS calcium binding; duplication; EF hand; methylated amino acid FEATURE !$2-149 #product calmodulin #status predicted #label MAT\ !$8-40 #domain calmodulin repeat homology #label EF1\ !$44-76 #domain calmodulin repeat homology #label EF2\ !$81-113 #domain calmodulin repeat homology #label EF3\ !$117-149 #domain calmodulin repeat homology #label EF4\ !$57,59,61,63,68 #binding_site calcium (Asp, Asp, Ser, Thr, Glu) !8#status predicted\ !$94,96,98,100,105 #binding_site calcium (Asp, Asp, Asn, Tyr, Glu) !8#status predicted\ !$116 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8predicted SUMMARY #length 149 #molecular-weight 16887 #checksum 6089 SEQUENCE /// ENTRY MCHUNB #type complete TITLE calmodulin-related protein NB-1 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 22-Jun-1999 ACCESSIONS A38278 REFERENCE A38278 !$#authors Yaswen, P.; Smoll, A.; Peehl, D.M.; Trask, D.K.; Sager, R.; !1Stampfer, M.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:7360-7364 !$#title Down-regulation of a calmodulin-related gene during !1transformation of human mammary epithelial cells. !$#cross-references MUID:91017505; PMID:2217169 !$#accession A38278 !'##molecule_type mRNA !'##residues 1-149 ##label YAS !'##cross-references GB:M58026; NID:g189080; PIDN:AAA36356.1; !1PID:g189081 COMMENT This protein is expressed in normal mammary, prostate, !1cervical, and epidermal tissues. It is greatly reduced or !1undetectable in transformed cells. GENETICS !$#gene GDB:CALML3; CLP !'##cross-references GDB:138290; OMIM:114184 !$#map_position 10pter-10p13 CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS calcium binding; duplication; EF hand; methylated amino acid FEATURE !$2-149 #product calmodulin NB-1 #status predicted #label !8MAT\ !$8-40 #domain calmodulin repeat homology #label EF1\ !$44-76 #domain calmodulin repeat homology #label EF2\ !$81-113 #domain calmodulin repeat homology #label EF3\ !$117-149 #domain calmodulin repeat homology #label EF4\ !$21,23,25,27,32 #binding_site calcium (Asp, Asp, Asp, Cys, Glu) !8#status predicted\ !$57,59,61,63,68 #binding_site calcium (Asp, Asp, Asn, Thr, Glu) !8#status predicted\ !$94,96,98,100,105 #binding_site calcium (Asp, Asp, Asn, Phe, Glu) !8#status predicted\ !$116 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8predicted\ !$130,132,134,136,141 #binding_site calcium (Asp, Asp, Asp, Gln, Glu) !8#status predicted SUMMARY #length 149 #molecular-weight 16891 #checksum 6378 SEQUENCE /// ENTRY MCAS #type complete TITLE calmodulin - Emericella nidulans ALTERNATE_NAMES modulator protein ORGANISM #formal_name Emericella nidulans, Aspergillus nidulans DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 22-Jun-1999 ACCESSIONS A37123 REFERENCE A37123 !$#authors Rasmussen, C.D.; Means, R.L.; Lu, K.P.; May, G.S.; Means, !1A.R. !$#journal J. Biol. Chem. (1990) 265:13767-13775 !$#title Characterization and expression of the unique calmodulin !1gene of Aspergillus nidulans. !$#cross-references MUID:90337991; PMID:2199442 !$#accession A37123 !'##molecule_type DNA !'##residues 1-149 ##label RAS !'##cross-references GB:J05545; NID:g168030; PIDN:AAA62800.1; !1PID:g168031 GENETICS !$#map_position VII !$#introns 1/3; 20/3; 26/1; 68/1; 139/1 CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS calcium binding; duplication; EF hand; methylated amino acid FEATURE !$2-149 #product calmodulin #status predicted #label MAT\ !$8-40 #domain calmodulin repeat homology #label EF1\ !$44-76 #domain calmodulin repeat homology #label EF2\ !$81-113 #domain calmodulin repeat homology #label EF3\ !$117-149 #domain calmodulin repeat homology #label EF4\ !$21,23,25,27,32 #binding_site calcium (Asp, Asp, Asp, Gln, Glu) !8#status predicted\ !$57,59,61,63,68 #binding_site calcium (Asp, Asp, Asn, Thr, Glu) !8#status predicted\ !$94,96,98,100,105 #binding_site calcium (Asp, Asp, Asn, Phe, Glu) !8#status predicted\ !$116 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8predicted\ !$130,132,134,136,141 #binding_site calcium (Asp, Asp, Asp, Arg, Glu) !8#status predicted SUMMARY #length 149 #molecular-weight 17013 #checksum 6670 SEQUENCE /// ENTRY MCCKA #type complete TITLE calmodulin - yeast (Candida albicans) ALTERNATE_NAMES modulator protein ORGANISM #formal_name Candida albicans DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 22-Jun-1999 ACCESSIONS JU0276 REFERENCE JU0276 !$#authors Saporito, S.M.; Sypherd, P.S. !$#journal Gene (1991) 106:43-49 !$#title The isolation and characterization of a calmodulin-encoding !1gene (CMD1) from the dimorphic fungus Candida albicans. !$#cross-references MUID:92039062; PMID:1937040 !$#accession JU0276 !'##molecule_type DNA !'##residues 1-149 ##label SAP !'##cross-references GB:M61128; NID:g170838; PIDN:AAA34331.1; !1PID:g170839 !'##note the authors translated the codon TTT for residue 69 as Leu and !1TTG for residue 70 as Gly GENETICS !$#gene CMD1 !$#map_position 3 !$#introns 1/3 CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS acetylated amino end; calcium binding; duplication; EF hand; !1methylated amino acid FEATURE !$2-149 #product calmodulin #status predicted #label MAT\ !$8-40 #domain calmodulin repeat homology #label EF1\ !$44-76 #domain calmodulin repeat homology #label EF2\ !$81-113 #domain calmodulin repeat homology #label EF3\ !$117-149 #domain calmodulin repeat homology #label EF4\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status predicted\ !$21,23,25,27,32 #binding_site calcium (Asp, Asp, Asp, Lys, Glu) !8#status predicted\ !$57,59,61,63,68 #binding_site calcium (Asp, Asn, Asp, Ser, Glu) !8#status predicted\ !$94,96,98,100,105 #binding_site calcium (Asp, Asn, Asp, Lys, Glu) !8#status predicted\ !$116 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8predicted\ !$130,132,134,136,141 #binding_site calcium (Asp, Asn, Asp, Glu, Glu) !8#status predicted SUMMARY #length 149 #molecular-weight 16518 #checksum 3742 SEQUENCE /// ENTRY MCZP #type complete TITLE calmodulin - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES modulator protein ORGANISM #formal_name Schizosaccharomyces pombe DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 10-Dec-1999 ACCESSIONS A26614; T38682 REFERENCE A26614 !$#authors Takeda, T.; Yamamoto, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:3580-3584 !$#title Analysis and in vivo disruption of the gene coding for !1calmodulin in Schizosaccharomyces pombe. !$#cross-references MUID:87231861; PMID:3035538 !$#accession A26614 !'##molecule_type DNA !'##residues 1-150 ##label TAK !'##cross-references GB:M16475; NID:g173356; PIDN:AAA35291.1; !1PID:g173357 REFERENCE Z21772 !$#authors Badcock, K.; Churcher, C.M.; Wood, V.; Barrell, B.G.; !1Rajandream, M.A. !$#submission submitted to the EMBL Data Library, May 1997 !$#accession T38682 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-150 ##label BAD !'##cross-references EMBL:Z95395; PIDN:CAB08742.1; GSPDB:GN00066; !1SPDB:SPAC3A12.14 !'##experimental_source strain 972h-; cosmid c3A12 GENETICS !$#gene cam1 !$#map_position 1 !$#introns 1/3 CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS calcium binding; duplication; EF hand FEATURE !$2-150 #product calmodulin #status predicted #label MAT\ !$9-41 #domain calmodulin repeat homology #label EF1\ !$45-77 #domain calmodulin repeat homology #label EF2\ !$82-114 #domain calmodulin repeat homology #label EF3\ !$118-150 #domain calmodulin repeat homology #label EF4\ !$22,24,26,28,33 #binding_site calcium (Asp, Asp, Asp, Asn, Glu) !8#status predicted\ !$58,60,62,64,69 #binding_site calcium (Asp, Asp, Asn, Thr, Glu) !8#status predicted\ !$95,97,99,101,106 #binding_site calcium (Asp, Asp, Asn, Tyr, Glu) !8#status predicted\ !$131,133,135,137,142 #binding_site calcium (Asp, Asp, Asp, Val, Glu) !8#status predicted SUMMARY #length 150 #molecular-weight 16905 #checksum 1850 SEQUENCE /// ENTRY MCBY #type complete TITLE calmodulin - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES modulator protein; phosphodiesterase activator; protein YBR0904; protein YBR109c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 21-Jul-2000 ACCESSIONS A25060; B25060; S48274; S45977; S20551; S44689 REFERENCE A25060 !$#authors Davis, T.N.; Urdea, M.S.; Masiarz, F.R.; Thorner, J. !$#journal Cell (1986) 47:423-431 !$#title Isolation of the yeast calmodulin gene: calmodulin is an !1essential protein. !$#cross-references MUID:87028234; PMID:3533275 !$#accession A25060 !'##molecule_type DNA !'##residues 1-147 ##label DAV !'##cross-references GB:M14760; NID:g171248; PIDN:AAA34504.1; !1PID:g171249 !$#accession B25060 !'##molecule_type protein !'##residues 15-30;128-145 ##label DA2 REFERENCE S48255 !$#authors Mannhaupt, G.; Stucka, R.; Ehnle, S.; Vetter, I.; Feldmann, !1H. !$#journal Yeast (1994) 10:1363-1381 !$#title Analysis of a 70 kb region on the right arm of yeast !1chromosome II. !$#cross-references MUID:95208357; PMID:7900426 !$#accession S48274 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-147 ##label MAN !'##cross-references EMBL:X78993; NID:g476045; PIDN:CAA55612.1; !1PID:g476065 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1994 REFERENCE S45927 !$#authors Feldmann, H.; Mannhaupt, G.; Schwarzlose, C.; Vetter, I. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S45977 !'##molecule_type DNA !'##residues 1-147 ##label FE2 !'##cross-references EMBL:Z35978; NID:g536372; PIDN:CAA85064.1; !1PID:g536373; GSPDB:GN00002; MIPS:YBR109c REFERENCE A42133 !$#authors Brockerhoff, S.E.; Edmonds, C.G.; Davis, T.N. !$#journal Protein Sci. (1992) 1:504-516 !$#title Structural analysis of wild-type and mutant yeast !1calmodulins by limited proteolysis and electrospray !1ionization mass spectrometry. !$#cross-references MUID:93278279; PMID:1304352 !$#contents annotation COMMENT This protein has three high-affinity calcium-binding sites. GENETICS !$#gene SGD:CMD1; MIPS:YBR109c !'##cross-references SGD:S0000313; MIPS:YBR109c !$#map_position 2R CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS blocked amino end; calcium binding; duplication; EF hand; !1methylated amino acid FEATURE !$2-147 #product calmodulin #status predicted #label MAT\ !$8-40 #domain calmodulin repeat homology #label EF1\ !$44-76 #domain calmodulin repeat homology #label EF2\ !$81-113 #domain calmodulin repeat homology #label EF3\ !$117-147 #domain calmodulin repeat homology #label EF4\ !$21,23,25,27,32 #binding_site calcium (Asp, Asp, Asn, Ser, Glu) !8#status predicted\ !$57,59,61,63,68 #binding_site calcium (Asp, Asp, Asn, Gln, Glu) !8#status predicted\ !$94,96,98,100,105 #binding_site calcium (Asp, Asn, Asp, Leu, Glu) !8#status predicted\ !$116 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8predicted SUMMARY #length 147 #molecular-weight 16135 #checksum 9508 SEQUENCE /// ENTRY BCKM #type complete TITLE caltractin - Chlamydomonas reinhardtii ORGANISM #formal_name Chlamydomonas reinhardtii DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 22-Jun-1999 ACCESSIONS A28216; S17673 REFERENCE A28216 !$#authors Huang, B.; Mengersen, A.; Lee, V.D. !$#journal J. Cell Biol. (1988) 107:133-140 !$#title Molecular cloning of cDNA for caltractin, a basal !1body-associated Ca(2+)-binding protein: homology in its !1protein sequence with calmodulin and the yeast CDC31 gene !1product. !$#cross-references MUID:88273296; PMID:2839516 !$#accession A28216 !'##molecule_type mRNA !'##residues 1-169 ##label HUA !'##cross-references EMBL:X12634; NID:g18126; PIDN:CAA31163.1; !1PID:g18127 REFERENCE S17673 !$#authors Lee, V.D.; Stapleton, M.; Huang, B. !$#journal J. Mol. Biol. (1991) 221:175-191 !$#title Genomic structure of Chlamydomonas caltractin. Evidence for !1intron insertion suggests a probable genealogy for the !1EF-hand superfamily of proteins. !$#cross-references MUID:92015207; PMID:1920403 !$#accession S17673 !'##molecule_type DNA !'##residues 1-169 ##label LEE !'##cross-references EMBL:X57973; NID:g18132; PIDN:CAA41039.1; !1PID:g18133 COMMENT This calcium-binding protein is found in the basal body !1complexes (the functional homolog of the centrosome in !1animal cell). In mitotic cells it is specifically associated !1with the poles of the mitotic spindles at the sites of the !1duplicated basal body complexes. GENETICS !$#introns 36/2; 48/3; 65/3; 121/3; 136/1; 161/2 CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS calcium binding; cell division; duplication; EF hand; !1mitosis FEATURE !$2-169 #product caltractin #status predicted #label MAT\ !$25-57 #domain calmodulin repeat homology #label EF1\ !$61-93 #domain calmodulin repeat homology #label EF2\ !$98-130 #domain calmodulin repeat homology #label EF3\ !$134-166 #domain calmodulin repeat homology #label EF4\ !$38,40,42,44,49 #binding_site calcium (Asp, Asp, Ser, Thr, Glu) !8#status predicted\ !$74,76,78,80,85 #binding_site calcium (Asp, Asp, Ser, Thr, Glu) !8#status predicted\ !$111,113,115,117,122 #binding_site calcium (Asp, Asp, Ser, Thr, Asp) !8#status predicted\ !$147,149,151,153,158 #binding_site calcium (Asp, Asn, Asp, Glu, Glu) !8#status predicted SUMMARY #length 169 #molecular-weight 19459 #checksum 7805 SEQUENCE /// ENTRY MCUR1C #type complete TITLE Spec1 protein - sea urchin (Strongylocentrotus purpuratus) ORGANISM #formal_name Strongylocentrotus purpuratus #common_name purple urchin DATE 17-Mar-1987 #sequence_revision 03-Oct-1995 #text_change 16-Jul-1999 ACCESSIONS S03249; A03031 REFERENCE S03249 !$#authors Hardin, S.H.; Carpenter, C.D.; Hardin, P.E.; Bruskin, A.M.; !1Klein, W.H. !$#journal J. Mol. Biol. (1985) 186:243-255 !$#title Structure of the Spec1 gene encoding a major calcium-binding !1protein in the embryonic ectoderm of the sea urchin, !1Strongylocentrotus purpuratus. !$#cross-references MUID:86115267; PMID:2935638 !$#accession S03249 !'##molecule_type DNA !'##residues 1-152 ##label HAR !'##cross-references EMBL:X03287; NID:g10315; PIDN:CAA27036.1; !1PID:g763026 !'##note the authors translated the codon AGT for residue 105 as Arg; !1this is the Spec1a allele REFERENCE A90843 !$#authors Carpenter, C.D.; Bruskin, A.M.; Hardin, P.E.; Keast, M.J.; !1Anstrom, J.; Tyner, A.L.; Brandhorst, B.P.; Klein, W.H. !$#journal Cell (1984) 36:663-671 !$#title Novel proteins belonging to the troponin C superfamily are !1encoded by a set of mRNAs in sea urchin embryos. !$#cross-references MUID:84130177; PMID:6697391 !$#accession A03031 !'##molecule_type mRNA !'##residues 'MVSQLPK',1-11,'I',13-49,'G',51-152 ##label CAR !'##note this is the Spec1c allele; Spec1a, Spec1b, and Spec1c appear to !1encode identical proteins COMMENT Spec proteins are calcium-binding proteins involved in !1larval development and metamorphosis. GENETICS !$#gene Spec1 !$#introns 1/3; 14/1; 62/1; 105/2; 144/1 !$#note alleles Spec1a and Spec1b differ in their 3' untranslated !1regions; Spec1c and other variants are probably also allelic CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS calcium binding; duplication; EF hand FEATURE !$10-42 #domain calmodulin repeat homology #label EF1\ !$46-78 #domain calmodulin repeat homology #label EF2\ !$84-116 #domain calmodulin repeat homology #label EF3\ !$120-152 #domain calmodulin repeat homology #label EF4\ !$23,25,27,29,34 #binding_site calcium (Asp, Asp, Ser, Ser, Glu) !8#status predicted\ !$59,61,63,65,70 #binding_site calcium (Asp, Asp, Ser, Thr, Glu) !8#status predicted\ !$97,99,101,103,108 #binding_site calcium (Asp, Asp, Asn, Ser, Glu) !8#status predicted\ !$133,135,137,139,144 #binding_site calcium (Asp, Asn, Asp, Lys, Glu) !8#status predicted SUMMARY #length 152 #molecular-weight 17466 #checksum 3543 SEQUENCE /// ENTRY MCUR2A #type complete TITLE Spec 2a protein - sea urchin (Strongylocentrotus purpuratus) ORGANISM #formal_name Strongylocentrotus purpuratus #common_name purple urchin DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 16-Jul-1999 ACCESSIONS A03032 REFERENCE A90843 !$#authors Carpenter, C.D.; Bruskin, A.M.; Hardin, P.E.; Keast, M.J.; !1Anstrom, J.; Tyner, A.L.; Brandhorst, B.P.; Klein, W.H. !$#journal Cell (1984) 36:663-671 !$#title Novel proteins belonging to the troponin C superfamily are !1encoded by a set of mRNAs in sea urchin embryos. !$#cross-references MUID:84130177; PMID:6697391 !$#accession A03032 !'##molecule_type protein !'##residues 1-150 ##label CAR COMMENT The Spec proteins are calcium-binding proteins involved in !1larval development and metamorphosis. CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS calcium binding; duplication; EF hand FEATURE !$10-42 #domain calmodulin repeat homology #label EF1\ !$46-78 #domain calmodulin repeat homology #label EF2\ !$81-113 #domain calmodulin repeat homology #label EF3\ !$118-150 #domain calmodulin repeat homology #label EF4\ !$23,25,27,29,34 #binding_site calcium (Asp, Asp, Asp, Lys, Glu) !8#status predicted\ !$59,61,63,65,70 #binding_site calcium (Asp, Asp, Ser, Asp, Glu) !8#status predicted\ !$94,96,98,100,105 #binding_site calcium (Asp, Asp, Asp, Ser, Glu) !8#status predicted\ !$131,133,135,137,142 #binding_site calcium (Asp, Asn, Asp, Lys, Glu) !8#status predicted SUMMARY #length 150 #molecular-weight 17014 #checksum 6444 SEQUENCE /// ENTRY MCUR2C #type complete TITLE Spec2c protein - sea urchin (Strongylocentrotus purpuratus) ORGANISM #formal_name Strongylocentrotus purpuratus #common_name purple urchin DATE 17-Mar-1987 #sequence_revision 03-Oct-1995 #text_change 16-Jul-1999 ACCESSIONS S01771; A03033 REFERENCE S01770 !$#authors Hardin, P.E.; Angerer, L.M.; Hardin, S.H.; Angerer, R.C.; !1Klein, W.H. !$#journal J. Mol. Biol. (1988) 202:417-431 !$#title Spec2 genes of Strongylocentrotus purpuratus. Structure and !1differential expression in embryonic aboral ectoderm cells. !$#cross-references MUID:89011969; PMID:3172223 !$#accession S01771 !'##molecule_type DNA !'##residues 1-151 ##label HAR !'##cross-references EMBL:X12772 REFERENCE A90843 !$#authors Carpenter, C.D.; Bruskin, A.M.; Hardin, P.E.; Keast, M.J.; !1Anstrom, J.; Tyner, A.L.; Brandhorst, B.P.; Klein, W.H. !$#journal Cell (1984) 36:663-671 !$#title Novel proteins belonging to the troponin C superfamily are !1encoded by a set of mRNAs in sea urchin embryos. !$#cross-references MUID:84130177; PMID:6697391 !$#accession A03033 !'##molecule_type protein !'##residues 1-44,'D',46-76,'L',78-136,'K',138-139,'VQ',142-144,'K', !1146-147,'E',149-151 ##label CAR COMMENT Spec proteins are calcium-binding proteins involved in !1larval development and metamorphosis. GENETICS !$#gene Spec2c !$#introns 1/3; 14/1; 62/1; 102/2; 142/1 CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS calcium binding; duplication; EF hand FEATURE !$10-42 #domain calmodulin repeat homology #label EF1\ !$46-78 #domain calmodulin repeat homology #label EF2\ !$81-113 #domain calmodulin repeat homology #label EF3\ !$118-150 #domain calmodulin repeat homology #label EF4\ !$23,25,27,29,34 #binding_site calcium (Asp, Asp, Asp, Lys, Glu) !8#status predicted\ !$59,61,63,65,70 #binding_site calcium (Asp, Asp, Ser, Pro, Glu) !8#status predicted\ !$94,96,98,100,105 #binding_site calcium (Asp, Asp, Ser, Ser, Glu) !8#status predicted\ !$131,133,135,137,142 #binding_site calcium (Asp, Asn, Asp, Glu, Glu) !8#status predicted SUMMARY #length 151 #molecular-weight 16991 #checksum 9761 SEQUENCE /// ENTRY MOHUA1 #type complete TITLE myosin alkali light chain 1, fast skeletal muscle, form 1 - human ALTERNATE_NAMES MLC1fast; myosin A1 catalytic light chain; myosin L1 catalytic light chain ORGANISM #formal_name Homo sapiens #common_name man DATE 20-Feb-1995 #sequence_revision 03-Oct-1995 #text_change 21-Jul-2000 ACCESSIONS JS0431; S07393; A34249 REFERENCE JS0431 !$#authors Seidel, U.; Bober, E.; Winter, B.; Lenz, S.; Lohse, P.; !1Goedde, H.W.; Grzeschik, K.H.; Arnold, H.H. !$#journal Gene (1988) 66:135-146 !$#title Alkali myosin light chains in man are encoded by a multigene !1family that includes the adult skeletal muscle, the !1embryonic or atrial, and nonsarcomeric isoforms. !$#cross-references MUID:88329722; PMID:2458299 !$#accession JS0431 !'##molecule_type mRNA !'##residues 1-194 ##label SEI !'##cross-references GB:M20642; NID:g188591; PIDN:AAA59854.1; !1PID:g188592 !'##experimental_source fetal quadriceps muscle REFERENCE S07393 !$#authors Seidel, U.; Bober, E.; Winter, B.; Lenz, S.; Lohse, P.; !1Arnold, H.H. !$#journal Nucleic Acids Res. (1987) 15:4989 !$#title The complete nucleotide sequences of cDNA clones coding for !1human myosin light chains 1 and 3. !$#cross-references MUID:87259977; PMID:3601661 !$#accession S07393 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-44,'M',46-194 ##label SE2 !'##cross-references EMBL:X05450; NID:g34679; PIDN:CAB42646.1; !1PID:g4803698 !'##experimental_source fetal skeletal muscle REFERENCE A34249 !$#authors Seidel, U.; Arnold, H.H. !$#journal J. Biol. Chem. (1989) 264:16109-16117 !$#title Identification of the functional promoter regions in the !1human gene encoding the myosin alkali light chains MLC1 and !1MLC3 of fast skeletal muscle. !$#cross-references MUID:89380210; PMID:2777779 !$#accession A34249 !'##molecule_type DNA !'##residues 1-44 ##label SE3 !'##cross-references GB:J05026; NID:g809118; PIDN:AAA66960.1; !1PID:g188573 GENETICS !$#gene GDB:MYL1 !'##cross-references GDB:120217; OMIM:160780 !$#map_position 2q32.1-2qter !$#introns 44/1 #status incomplete CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS alternative splicing; blocked amino end; calcium binding; !1duplication; EF hand; methylated amino end; muscle !1contraction; skeletal muscle FEATURE !$50-82 #domain calmodulin repeat homology #label EF1\ !$127-159 #domain calmodulin repeat homology #label EF3\ !$162-194 #domain calmodulin repeat homology #label EF4\ !$2 #modified_site trimethylated amino end (Ala) (in !8mature form) #status predicted SUMMARY #length 194 #molecular-weight 21145 #checksum 8812 SEQUENCE /// ENTRY MOHUA2 #type complete TITLE myosin alkali light chain 1, fast skeletal muscle, form 2 - human ALTERNATE_NAMES MLC3fast; myosin A2 catalytic light chain; myosin L3 catalytic light chain; myosin light chain 3 ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1991 #sequence_revision 03-Oct-1995 #text_change 22-Jun-1999 ACCESSIONS S07939 REFERENCE S07393 !$#authors Seidel, U.; Bober, E.; Winter, B.; Lenz, S.; Lohse, P.; !1Arnold, H.H. !$#journal Nucleic Acids Res. (1987) 15:4989 !$#title The complete nucleotide sequences of cDNA clones coding for !1human myosin light chains 1 and 3. !$#cross-references MUID:87259977; PMID:3601661 !$#accession S07939 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-150 ##label SEI !'##cross-references EMBL:X05451; NID:g34688; PIDN:CAA29020.1; !1PID:g34689 !'##experimental_source fetal skeletal muscle GENETICS !$#gene GDB:MYL1 !'##cross-references GDB:120217; OMIM:160780 !$#map_position 2q32.1-2qter CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS acetylated amino end; alternative splicing; calcium binding; !1duplication; EF hand; muscle contraction; skeletal muscle FEATURE !$6-38 #domain calmodulin repeat homology #label EF1\ !$83-115 #domain calmodulin repeat homology #label EF3\ !$118-150 #domain calmodulin repeat homology #label EF4\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status predicted SUMMARY #length 150 #molecular-weight 16684 #checksum 927 SEQUENCE /// ENTRY MORTA1 #type complete TITLE myosin alkali light chain 1, fast skeletal muscle, form 1 - rat ALTERNATE_NAMES MLC1fast; myosin A1 catalytic light chain; myosin L1 catalytic light chain ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 22-Jun-1999 ACCESSIONS A03034 REFERENCE A92456 !$#authors Periasamy, M.; Strehler, E.E.; Garfinkel, L.I.; Gubits, !1R.M.; Ruiz-Opazo, N.; Nadal-Ginard, B. !$#journal J. Biol. Chem. (1984) 259:13595-13604 !$#title Fast skeletal muscle myosin light chains 1 and 3 are !1produced from a single gene by a combined process of !1differential RNA transcription and splicing. !$#cross-references MUID:85030494; PMID:6092382 !$#accession A03034 !'##molecule_type mRNA !'##residues 1-190 ##label PER !'##cross-references GB:L00088; GB:J00753; NID:g205472; PIDN:AAA98533.1; !1PID:g205474 !'##note initiator Met not shown GENETICS !$#introns 40/3; 49/1; 97/1; 155/1; 181/1 CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS alternative splicing; blocked amino end; calcium binding; !1duplication; EF hand; methylated amino end; muscle !1contraction; skeletal muscle FEATURE !$46-78 #domain calmodulin repeat homology #label EF1\ !$123-155 #domain calmodulin repeat homology #label EF3\ !$158-190 #domain calmodulin repeat homology #label EF4\ !$1 #modified_site trimethylated amino end (Ala) #status !8predicted SUMMARY #length 190 #molecular-weight 20716 #checksum 2514 SEQUENCE /// ENTRY MORTA2 #type complete TITLE myosin alkali light chain 1, fast skeletal muscle, form 2 [similarity] - rat ALTERNATE_NAMES myosin A2 catalytic light chain; myosin light chain 3 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 28-Feb-1986 #sequence_revision 16-Jun-2000 #text_change 16-Jun-2000 ACCESSIONS I77418; A03035 REFERENCE I57590 !$#authors Strehler, E.E.; Periasamy, M.; Strehler-Page, M. !$#journal Mol. Cell. Biol. (1985) 5:3168-3182 !$#title Myosin light-chain 1 and 3 gene has two structurally !1distinct and differentially regulated promoters evolving at !1different rates. !$#cross-references MUID:86310786; PMID:3018505 !$#accession I77418 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-150 ##label RES !'##cross-references GB:M12021; NID:g205482; PIDN:AAA41623.1; !1PID:g205486 REFERENCE A92456 !$#authors Periasamy, M.; Strehler, E.E.; Garfinkel, L.I.; Gubits, !1R.M.; Ruiz-Opazo, N.; Nadal-Ginard, B. !$#journal J. Biol. Chem. (1984) 259:13595-13604 !$#title Fast skeletal muscle myosin light chains 1 and 3 are !1produced from a single gene by a combined process of !1differential RNA transcription and splicing. !$#cross-references MUID:85030494; PMID:6092382 !$#accession A03035 !'##molecule_type mRNA !'##residues 2-113,'T',115-150 ##label PER !'##cross-references GB:L00088; GB:J00753; NID:g205472; PIDN:AAA98534.1; !1PID:g205475 !'##note initiator Met not shown GENETICS !$#introns 1/3; 10/1; 58/1; 116/1; 142/1 CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS acetylated amino end; alternative splicing; calcium binding; !1duplication; EF hand; muscle contraction; skeletal muscle FEATURE !$2-150 #product myosin light chain #status predicted #label !8MAT\ !$6-38 #domain calmodulin repeat homology #label EF1\ !$83-115 #domain calmodulin repeat homology #label EF2\ !$118-150 #domain calmodulin repeat homology #label EF3\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status predicted SUMMARY #length 150 #molecular-weight 16626 #checksum 9864 SEQUENCE /// ENTRY MORBLA #type complete TITLE myosin alkali light chain 1, fast skeletal muscle, form 1 - rabbit ALTERNATE_NAMES MLC1fast; myosin A1 catalytic light chain; myosin L1 catalytic light chain ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 24-Apr-1984 #sequence_revision 03-Oct-1995 #text_change 22-Jun-1999 ACCESSIONS S15061; S12692; A03036; A91423 REFERENCE S15061 !$#authors Maeda, K. !$#submission submitted to the EMBL Data Library, August 1990 !$#accession S15061 !'##molecule_type mRNA !'##residues 1-192 ##label MAE !'##cross-references EMBL:X54041; NID:g1632; PIDN:CAA37974.1; PID:g1633 REFERENCE S12692 !$#authors Mueller, B.; Maeda, K.; Wittinghofer, A. !$#journal Nucleic Acids Res. (1990) 18:6688 !$#title Sequence of the myosin light chain 1/3 isolated from a !1rabbit fast skeletal muscle lambda library. !$#cross-references MUID:91067463; PMID:2147476 !$#accession S12692 !'##molecule_type mRNA !'##residues 1-51 ##label MUE !'##cross-references EMBL:X54041 REFERENCE A91219 !$#authors Frank, G.; Weeds, A.G. !$#journal Eur. J. Biochem. (1974) 44:317-334 !$#title The amino-acid sequence of the alkali light chains of rabbit !1skeletal-muscle myosin. !$#cross-references MUID:74257123; PMID:4838672 !$#accession A03036 !'##molecule_type protein !'##residues 'X',3-5,'N',7-18,'K',19-29,31-97,'D',99,'Q',101-140, !1'DGTVG',146-192 ##label FRA REFERENCE A91423 !$#authors Weeds, A.G. !$#journal FEBS Lett. (1975) 59:203-208 !$#title Cyanogen bromide fragments of the cardiac I light chain from !1bovine myosin: evidence for sequence homology with rabbit !1skeletal myosin alkali light chains. !$#cross-references MUID:76210734; PMID:1227935 !$#contents revision to residues 141-142 !$#accession A91423 !'##molecule_type protein !'##residues 'X',3-5,'N',7-18,'K',19-29,31-97,'D',99,'Q',101-141,'DTVG', !1146-192 ##label WEE CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS alternative splicing; blocked amino end; calcium binding; !1duplication; EF hand; methylated amino end; muscle !1contraction; skeletal muscle FEATURE !$48-80 #domain calmodulin repeat homology #label EF1\ !$125-157 #domain calmodulin repeat homology #label EF3\ !$160-192 #domain calmodulin repeat homology #label EF4\ !$2 #modified_site trimethylated amino end (Ala) (in !8mature form) #status experimental SUMMARY #length 192 #molecular-weight 20949 #checksum 4665 SEQUENCE /// ENTRY MORBL2 #type complete TITLE myosin alkali light 1, fast skeletal muscle, form 2 - rabbit ALTERNATE_NAMES MLC3fast; myosin A2 catalytic light chain; myosin L3 catalytic light chain; myosin light chain 3 ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 30-Sep-1993 #sequence_revision 03-Oct-1995 #text_change 22-Jun-1999 ACCESSIONS S12693; B03036 REFERENCE S12692 !$#authors Mueller, B.; Maeda, K.; Wittinghofer, A. !$#journal Nucleic Acids Res. (1990) 18:6688 !$#title Sequence of the myosin light chain 1/3 isolated from a !1rabbit fast skeletal muscle lambda library. !$#cross-references MUID:91067463; PMID:2147476 !$#accession S12693 !'##molecule_type mRNA !'##residues 1-150 ##label MUE !'##cross-references EMBL:X54044; NID:g1638; PIDN:CAA37977.1; PID:g1639 REFERENCE A91219 !$#authors Frank, G.; Weeds, A.G. !$#journal Eur. J. Biochem. (1974) 44:317-334 !$#title The amino-acid sequence of the alkali light chains of rabbit !1skeletal-muscle myosin. !$#cross-references MUID:74257123; PMID:4838672 !$#accession B03036 !'##molecule_type protein !'##residues 2-55,'D',57,'Q',59-99,'DTVG',104-150 ##label FRA CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS acetylated amino end; alternative splicing; calcium binding; !1duplication; EF hand; muscle contraction; skeletal muscle FEATURE !$6-38 #domain calmodulin repeat homology #label EF1\ !$83-115 #domain calmodulin repeat homology #label EF3\ !$118-150 #domain calmodulin repeat homology #label EF4\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental SUMMARY #length 150 #molecular-weight 16658 #checksum 1075 SEQUENCE /// ENTRY MOCHLA #type complete TITLE myosin alkali light chain 1, fast skeletal muscle, splice form 1 - chicken ALTERNATE_NAMES MLC1fast; myosin A1 catalytic light chain; myosin L1 catalytic light chain ORGANISM #formal_name Gallus gallus #common_name chicken DATE 01-Sep-1981 #sequence_revision 21-Feb-1997 #text_change 16-Jun-2000 ACCESSIONS A91284; A91703; A93443; I50666; I50663; I50383; A03037; !1A91107; B93443 REFERENCE A91284 !$#authors Matsuda, G.; Maita, T.; Umegane, T. !$#journal FEBS Lett. (1981) 126:111-113 !$#title The primary structure of L-1 light chain of chicken fast !1skeletal muscle myosin and its genetic implication. !$#cross-references MUID:81212763; PMID:7238855 !$#accession A91284 !'##molecule_type protein !'##residues 3-5,'D',7-192 ##label MAS REFERENCE A91703 !$#authors Umegane, T.; Maita, T.; Matsuda, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1982) 363:1321-1330 !$#title Amino-acid sequence of the L-1 light chain of chicken fast !1skeletal-muscle myosin. !$#cross-references MUID:83081015; PMID:7173826 !$#accession A91703 !'##molecule_type protein !'##residues 3-5,'D',7-192 ##label UME REFERENCE A93443 !$#authors Nabeshima, Y.; Fujii-Kuriyama, Y.; Muramatsu, M.; Ogata, K. !$#journal Nucleic Acids Res. (1982) 10:6099-6110 !$#title Molecular cloning and nucleotide sequences of the !1complementary DNAs to chicken skeletal muscle myosin two !1alkali light chain mRNAs. !$#cross-references MUID:83064541; PMID:6128725 !$#accession A93443 !'##molecule_type mRNA !'##residues 16-192 ##label NAB1 !'##cross-references GB:J00887; NID:g212346 REFERENCE I50383 !$#authors Nabeshima, Y.; Fujii-Kuriyama, Y.; Muramatsu, M.; Ogata, K. !$#journal Nature (1984) 308:333-338 !$#title Alternative transcription and two modes of splicing result !1in two myosin light chains from one gene. !$#cross-references MUID:84168118; PMID:6709041 !$#accession I50666 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 43-51 ##label NAB2 !'##cross-references GB:X00459; GB:K02609; NID:g63623; PID:g1334737 !$#accession I50663 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-42 ##label NAB3 !'##cross-references EMBL:X00458; NID:g63621; PID:g63622 !$#accession I50383 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-116,'M',117-145,147-192 ##label NAB4 !'##cross-references GB:K02610; NID:g212328; PIDN:AAA48955.1; !1PID:g212330 GENETICS !$#introns 42/3; 52/1; 100/1; 158/1; 184/1 CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS alternative splicing; blocked amino end; calcium binding; !1duplication; EF hand; muscle contraction; skeletal muscle FEATURE !$3-192 #product myosin alkali light chain 1, fast skeletal !8muscle, splice form 1 #status experimental #label !8MAT\ !$48-80 #domain calmodulin repeat homology #label EF1\ !$125-157 #domain calmodulin repeat homology #label EF3\ !$160-192 #domain calmodulin repeat homology #label EF4\ !$3 #modified_site blocked amino end (Pro) (in mature !8form) #status experimental SUMMARY #length 192 #molecular-weight 20913 #checksum 5051 SEQUENCE /// ENTRY MOCHA2 #type complete TITLE myosin alkali light chain 1, fast skeletal muscle, splice form 2 - chicken ALTERNATE_NAMES myosin A2 catalytic light chain; myosin L4 catalytic light chain ORGANISM #formal_name Gallus gallus #common_name chicken DATE 01-Sep-1981 #sequence_revision 16-Oct-1998 #text_change 16-Jun-2000 ACCESSIONS I50384; I50665; B93443; A91107 REFERENCE I50383 !$#authors Nabeshima, Y.; Fujii-Kuriyama, Y.; Muramatsu, M.; Ogata, K. !$#journal Nature (1984) 308:333-338 !$#title Alternative transcription and two modes of splicing result !1in two myosin light chains from one gene. !$#cross-references MUID:84168118; PMID:6709041 !$#accession I50384 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-74,'M',75-103,105-150 ##label NAB1 !'##cross-references GB:K02610; NID:g212328; PIDN:AAA48956.1; !1PID:g212331 !$#accession I50665 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-9 ##label NAB2 !'##cross-references GB:X00459; GB:K02609; NID:g63623; PID:g584508; !1PID:g1334736 REFERENCE A93443 !$#authors Nabeshima, Y.; Fujii-Kuriyama, Y.; Muramatsu, M.; Ogata, K. !$#journal Nucleic Acids Res. (1982) 10:6099-6110 !$#title Molecular cloning and nucleotide sequences of the !1complementary DNAs to chicken skeletal muscle myosin two !1alkali light chain mRNAs. !$#cross-references MUID:83064541; PMID:6128725 !$#accession B93443 !'##molecule_type mRNA !'##residues 2-150 ##label NAB3 !'##cross-references GB:J00888; NID:g212348 REFERENCE A91107 !$#authors Maita, T.; Umegane, T.; Matsuda, G. !$#journal Eur. J. Biochem. (1981) 114:45-49 !$#title Amino-acid sequence of the L-4 light chain of chicken !1skeletal-muscle myosin. !$#cross-references MUID:81164496; PMID:6783403 !$#accession A91107 !'##molecule_type protein !'##residues 2-6,'Q',8,'D',10-99,'D',101-150 ##label MAI GENETICS !$#gene MLC !$#introns 1/3; 10/1; 58/1; 116/1; 142/1 CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS alternative splicing; blocked amino end; calcium binding; !1duplication; EF hand; muscle contraction; skeletal muscle FEATURE !$2-150 #product myosin alkali light chain 1, fast skeletal !8muscle, splice form 2 #status experimental #label !8MAT\ !$6-38 #domain calmodulin repeat homology #label EF1\ !$83-115 #domain calmodulin repeat homology #label EF3\ !$118-150 #domain calmodulin repeat homology #label EF4\ !$2 #modified_site blocked amino end (Ser) (in mature !8form) (probably acetylated) #status experimental SUMMARY #length 150 #molecular-weight 16710 #checksum 8566 SEQUENCE /// ENTRY MOHU3V #type complete TITLE myosin alkali light chain 3, ventricular and slow skeletal muscle - human ALTERNATE_NAMES MLC1sb; MLC1v; myosin L1 catalytic light chain, cardiac muscle; ventricular myosin light chain 1 ORGANISM #formal_name Homo sapiens #common_name man DATE 01-Dec-1989 #sequence_revision 03-Oct-1995 #text_change 22-Jun-1999 ACCESSIONS B30881; A32037; S00732 REFERENCE A92669 !$#authors Kurabayashi, M.; Komuro, I.; Tsuchimochi, H.; Takaku, F.; !1Yazaki, Y. !$#journal J. Biol. Chem. (1988) 263:13930-13936 !$#title Molecular cloning and characterization of human atrial and !1ventricular myosin alkali light chain cDNA clones. !$#cross-references MUID:88330932; PMID:3417683 !$#accession B30881 !'##molecule_type mRNA !'##residues 1-195 ##label KUR !'##cross-references GB:M24122; NID:g189026; PIDN:AAA59895.1; !1PID:g189027; GB:J03954 REFERENCE A32037 !$#authors Fodor, W.L.; Darras, B.; Seharaseyon, J.; Falkenthal, S.; !1Francke, U.; Vanin, E.F. !$#journal J. Biol. Chem. (1989) 264:2143-2149 !$#title Human ventricular/slow twitch myosin alkali light chain gene !1characterization, sequence, and chromosomal location. !$#cross-references MUID:89123281; PMID:2789520 !$#accession A32037 !'##molecule_type DNA !'##residues 1-195 ##label FOD !'##cross-references GB:M24247; GB:J04462; NID:g188579; PIDN:AAA59851.1; !1PID:g459827 REFERENCE S00732 !$#authors Hoffmann, E.; Shi, Q.W.; Floroff, M.; Mickle, D.A.G.; Wu, !1T.W.; Olley, P.M.; Jackowski, G. !$#journal Nucleic Acids Res. (1988) 16:2353 !$#title Molecular cloning and complete nucleotide sequence of a !1human ventricular myosin light chain 1. !$#cross-references MUID:88189843; PMID:3357795 !$#accession S00732 !'##molecule_type mRNA !'##residues 1-23,'E',25-71,'N',73-97,'NRSK',102-170,'R',172-195 ##label !1HOF !'##cross-references EMBL:X07373 !'##note the authors translated the codon AAC for residue 72 as Thr and !1AGG for residue 171 as Lys GENETICS !$#gene GDB:MYL3 !'##cross-references GDB:120218; OMIM:160790 !$#map_position 3p21.3-3p21.2 CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS blocked amino end; calcium binding; cardiac muscle; !1duplication; EF hand; heart; muscle contraction; skeletal !1muscle FEATURE !$49-83 #domain calmodulin repeat homology #label EF1\ !$128-160 #domain calmodulin repeat homology #label EF3\ !$163-195 #domain calmodulin repeat homology #label EF4\ !$3 #modified_site blocked amino end (Pro) (in mature !8form) #status predicted SUMMARY #length 195 #molecular-weight 21932 #checksum 3656 SEQUENCE /// ENTRY MORT3V #type complete TITLE myosin alkali light chain 3, ventricular and slow skeletal muscle - rat ALTERNATE_NAMES MLC1sb; MLC1v; myosin L1 catalytic light chain, cardiac muscle; ventricular myosin light chain 1 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 12-Feb-1993 #sequence_revision 03-Oct-1995 #text_change 16-Jul-1999 ACCESSIONS S09573; S15759; S06169 REFERENCE S09573 !$#authors McNally, E.M.; Buttrick, P.M.; Leinwand, L.A. !$#journal Nucleic Acids Res. (1989) 17:2753-2767 !$#title Ventricular myosin light chain 1 is developmentally !1regulated and does not change in hypertension. !$#cross-references MUID:89240031; PMID:2717409 !$#accession S09573 !'##molecule_type mRNA !'##residues 1-200 ##label MCN !'##cross-references EMBL:X14812; NID:g56669; PIDN:CAA32917.1; !1PID:g56670 !'##experimental_source heart REFERENCE S15759 !$#authors Periasamy, M.; Wadgaonkar, R.; Kumar, C.; Martin, B.J.; !1Siddiqui, M.A.Q. !$#journal Nucleic Acids Res. (1989) 17:7723-7734 !$#title Characterization of a rat myosin alkali light chain gene !1expressed in ventricular and slow twitch skeletal muscles. !$#cross-references MUID:90016857; PMID:2798124 !$#accession S15759 !'##molecule_type DNA !'##residues 1-200 ##label PE2 !'##cross-references EMBL:X16325; NID:g56671; PIDN:CAA34388.1; !1PID:g763179 GENETICS !$#introns 48/3; 58/1; 108/1; 166/1; 192/1 CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS blocked amino end; calcium binding; cardiac muscle; !1duplication; EF hand; heart; muscle contraction; skeletal !1muscle FEATURE !$54-88 #domain calmodulin repeat homology #label EF1\ !$133-165 #domain calmodulin repeat homology #label EF3\ !$168-200 #domain calmodulin repeat homology #label EF4\ !$3 #modified_site blocked amino end (Pro) (in mature !8form) #status predicted SUMMARY #length 200 #molecular-weight 22156 #checksum 3698 SEQUENCE /// ENTRY MOCHLC #type complete TITLE myosin alkali light chain 3, cardiac and slow skeletal muscle - chicken ALTERNATE_NAMES MLC1sb; MLC1v; myosin L1 catalytic light chain, cardiac muscle; ventricular myosin light chain 1 ORGANISM #formal_name Gallus gallus #common_name chicken DATE 01-Sep-1981 #sequence_revision 03-Oct-1995 #text_change 16-Jun-2000 ACCESSIONS S01843; A03038 REFERENCE S01843 !$#authors Nakamura, S.; Nabeshima, Y.I.; Kobayashi, H.; Nabeshima, Y.; !1Nonomura, Y.; Fujii-Kuriyama, Y. !$#journal J. Mol. Biol. (1988) 203:895-904 !$#title Single chicken cardiac myosin alkali light-chain gene !1generates two different mRNAs by alternative splicing of a !1complex exon. !$#cross-references MUID:89094866; PMID:3210243 !$#accession S01843 !'##molecule_type mRNA; DNA !'##residues 1-194 ##label NAK !'##cross-references EMBL:X13861; NID:g63637; PIDN:CAA32072.1; !1PID:g1772515; EMBL:X13862; NID:g63638; PID:g63639; !1EMBL:X13863; EMBL:X13864; EMBL:X13865; EMBL:X13866; !1EMBL:X13867 !'##experimental_source atrial, ventricular, and anterior latissimus !1dorsi muscles of adult chicken REFERENCE A03038 !$#authors Maita, T.; Umegane, T.; Kato, Y.; Matsuda, G. !$#journal Eur. J. Biochem. (1980) 107:565-575 !$#title Amino-acid sequence of the L-1 light chain of chicken !1cardiac-muscle myosin. !$#cross-references MUID:80246034; PMID:6772448 !$#accession A03038 !'##molecule_type protein !'##residues 3-143,'D',145-156,'A',158-194 ##label MAI COMMENT This protein is expressed in atrial and ventricular cardiac !1muscle. GENETICS !$#introns 42/3; 52/1; 102/1; 160/1; 186/1 !$#note alternative splicing occurs 3' to the coding region CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS blocked amino end; calcium binding; cardiac muscle; !1duplication; EF hand; heart; muscle contraction; skeletal !1muscle FEATURE !$48-82 #domain calmodulin repeat homology #label EF1\ !$127-159 #domain calmodulin repeat homology #label EF3\ !$162-194 #domain calmodulin repeat homology #label EF4\ !$3 #modified_site blocked amino end (Pro) (in mature !8form) #status experimental SUMMARY #length 194 #molecular-weight 21996 #checksum 2739 SEQUENCE /// ENTRY MOHU4E #type complete TITLE myosin alkali light chain 4, embryonic and atrial - human ALTERNATE_NAMES MLC1A; MLC1emb; myosin L1 catalytic light chain, atrial ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1991 #sequence_revision 03-Oct-1995 #text_change 22-Jun-1999 ACCESSIONS A32730; S09117; S02009; S15710; A30881; PS0100; S31135 REFERENCE A32730 !$#authors Seharaseyon, J.; Bober, E.; Hsieh, C.L.; Fodor, W.L.; !1Francke, U.; Arnold, H.H.; Vanin, E.F. !$#journal Genomics (1990) 7:289-293 !$#title Human embryonic/atrial myosin alkali light chain gene: !1characterization, sequence, and chromosomal location. !$#cross-references MUID:90269822; PMID:2129532 !$#accession A32730 !'##molecule_type DNA !'##residues 1-197 ##label SEH !'##cross-references GB:M37069; GB:M37070; GB:M37071; GB:M37072; !1GB:M37073; GB:M37074; NID:g188602; PIDN:AAA59858.1; !1PID:g188605; GB:M37075 !'##note the authors translated the codon CAG for residue 87 as Glu, CAG !1for residue 93 as glu, and GAA for residue 104 as Gln REFERENCE S09117 !$#authors Zimmermann, K.; Kautz, S.; Hajdu, G.; Winter, C.; Whalen, !1R.G.; Starzinski-Powitz, A. !$#journal J. Mol. Biol. (1990) 211:505-513 !$#title Heterogenic mRNAs with an identical protein-coding region of !1the human embryonic myosin alkali light chain in skeletal !1muscle cells. !$#cross-references MUID:90172417; PMID:2308163 !$#accession S09117 !'##molecule_type mRNA !'##residues 1-197 ##label ZIM REFERENCE S02009 !$#authors Arnold, H.H.; Lohse, P.; Seidel, U.; Bober, E. !$#journal Eur. J. Biochem. (1988) 178:53-60 !$#title A novel human myosin alkali light chain is developmentally !1regulated. Expression in fetal cardiac and skeletal muscle !1and in adult atria. !$#cross-references MUID:89078413; PMID:2849544 !$#accession S02009 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-197 ##label ARN !'##cross-references EMBL:X13955; NID:g34673; PIDN:CAA32137.1; !1PID:g34674 REFERENCE S15710 !$#authors Rotter, M.; Zimmerman, K.; Poustka, A.; Starzinski-Powitz, !1A. !$#journal Nucleic Acids Res. (1991) 19:1497-1504 !$#title The human embryonic myosin alkali light chain gene: use of !1alternative promoters and 3' non-coding regions. !$#cross-references MUID:91227141; PMID:2027757 !$#accession S15710 !'##status translation not shown !'##molecule_type DNA !'##residues 1-197 ##label ROT !'##cross-references EMBL:X58851; NID:g34680; PIDN:CAA41655.1; !1PID:g825691 !'##note an additional author's name has been added in reference S31135 REFERENCE S31135 !$#authors Rotter, M.; Zimmermann, K.; Poustka, A.; Soussi-Yanicostas, !1N.; Starzinski-Powitz, A. !$#journal Nucleic Acids Res. (1991) 19:3485 !$#contents annotation; an author's name has been added REFERENCE A92669 !$#authors Kurabayashi, M.; Komuro, I.; Tsuchimochi, H.; Takaku, F.; !1Yazaki, Y. !$#journal J. Biol. Chem. (1988) 263:13930-13936 !$#title Molecular cloning and characterization of human atrial and !1ventricular myosin alkali light chain cDNA clones. !$#cross-references MUID:88330932; PMID:3417683 !$#accession A30881 !'##molecule_type mRNA !'##residues 1-50,'E',52-55,'L',57-142,'E',144-149,'D',151-197 ##label !1KUR !'##cross-references GB:M24121; NID:g189014; PIDN:AAA59891.1; !1PID:g189015; GB:J03954 !'##note the authors translated the codon TTA for residue 56 as Phe, TAT !1for residue 132 as Glu, GAG for residue 133 as Gat and GCT !1for residue 169 as Val REFERENCE JS0431 !$#authors Seidel, U.; Bober, E.; Winter, B.; Lenz, S.; Lohse, P.; !1Goedde, H.W.; Grzeschik, K.H.; Arnold, H.H. !$#journal Gene (1988) 66:135-146 !$#title Alkali myosin light chains in man are encoded by a multigene !1family that includes the adult skeletal muscle, the !1embryonic or atrial, and nonsarcomeric isoforms. !$#cross-references MUID:88329722; PMID:2458299 !$#accession PS0100 !'##molecule_type mRNA !'##residues 104-118,'V',120-180,'V',182-184,'V',186-197 ##label SEI !'##cross-references GB:M20641; NID:g188595; PIDN:AAA59856.1; !1PID:g386954 COMMENT In mammals, this form is found in fetal and regenerating !1skeletal muscle, fetal ventricular muscle, and adult atrial !1muscle. GENETICS !$#gene GDB:MYL4 !'##cross-references GDB:120219; OMIM:160770 !$#map_position 17q21-17qter !$#introns 45/3; 55/1; 105/1; 163/1; 189/1 CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS calcium binding; cardiac muscle; duplication; EF hand; !1heart; muscle contraction FEATURE !$51-85 #domain calmodulin repeat homology #label EF1\ !$130-162 #domain calmodulin repeat homology #label EF3\ !$165-197 #domain calmodulin repeat homology #label EF4 SUMMARY #length 197 #molecular-weight 21564 #checksum 6920 SEQUENCE /// ENTRY MORT4E #type complete TITLE myosin alkali light chain 4, embryonic and atrial - rat ALTERNATE_NAMES MLC1A; MLC1emb; myosin L1 catalytic light chain, atrial ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 29-Jan-1993 #sequence_revision 03-Oct-1995 #text_change 22-Jun-1999 ACCESSIONS S09236 REFERENCE S09236 !$#authors Rovner, A.S.; McNally, E.M.; Leinwand, L.A. !$#journal Nucleic Acids Res. (1990) 18:1581-1586 !$#title Complete cDNA sequence of rat atrial myosin light chain 1: !1patterns of expression during development and with !1hypertension. !$#cross-references MUID:90221887; PMID:2326197 !$#accession S09236 !'##molecule_type mRNA !'##residues 1-193 ##label ROV !'##cross-references EMBL:X51531; NID:g57512; PIDN:CAA35911.1; !1PID:g57513 COMMENT In mammals, this form is found in fetal and regenerating !1skeletal muscle, fetal ventricular muscle, and adult atrial !1muscle. CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS calcium binding; cardiac muscle; duplication; EF hand; !1heart; muscle contraction FEATURE !$47-81 #domain calmodulin repeat homology #label EF1\ !$126-158 #domain calmodulin repeat homology #label EF3\ !$161-193 #domain calmodulin repeat homology #label EF4 SUMMARY #length 193 #molecular-weight 21282 #checksum 425 SEQUENCE /// ENTRY MOMS4E #type complete TITLE myosin alkali light chain 4, embryonic and atrial - mouse ALTERNATE_NAMES MLC1A; MLC1emb; myosin L1 catalytic light chain, atrial ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Mar-1990 #sequence_revision 03-Oct-1995 #text_change 22-Jun-1999 ACCESSIONS A31114; S01944 REFERENCE A31114 !$#authors Barton, P.J.R.; Robert, B.; Cohen, A.; Garner, I.; Sassoon, !1D.; Weydert, A.; Buckingham, M.E. !$#journal J. Biol. Chem. (1988) 263:12669-12676 !$#title Structure and sequence of the myosin alkali light chain gene !1expressed in adult cardiac atria and fetal striated muscle. !$#cross-references MUID:88315068; PMID:2842339 !$#accession A31114 !'##molecule_type DNA !'##residues 1-193 ##label BAR !'##cross-references GB:M20772; GB:J03932; GB:M19435; NID:g199731; !1PIDN:AAA39721.1; PID:g387483 REFERENCE S01944 !$#authors Cohen, A.; Barton, P.J.R.; Robert, B.; Garner, I.; Alonso, !1S.; Buckingham, M.E. !$#journal Nucleic Acids Res. (1988) 16:10037-10052 !$#title Promoter analysis of myosin alkali light chain genes !1expressed in mouse striated muscle. !$#cross-references MUID:89057447; PMID:3194193 !$#accession S01944 !'##molecule_type DNA !'##residues 1-41 ##label COH !'##cross-references EMBL:X12971; NID:g53138; PIDN:CAA31414.1; !1PID:g53139 COMMENT In mammals, this form is found in fetal and regenerating !1skeletal muscle, fetal ventricular muscle, and adult atrial !1muscle. GENETICS !$#introns 41/3; 51/1; 101/1; 159/1; 185/1 CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS calcium binding; cardiac muscle; duplication; EF hand; !1heart; muscle contraction FEATURE !$47-81 #domain calmodulin repeat homology #label EF1\ !$126-158 #domain calmodulin repeat homology #label EF3\ !$161-193 #domain calmodulin repeat homology #label EF4 SUMMARY #length 193 #molecular-weight 21159 #checksum 9584 SEQUENCE /// ENTRY MOCH4E #type complete TITLE myosin alkali light chain 4, embryonic - chicken ALTERNATE_NAMES myosin L23 catalytic light chain ORGANISM #formal_name Gallus gallus #common_name chicken DATE 01-Dec-1989 #sequence_revision 03-Oct-1995 #text_change 22-Jun-1999 ACCESSIONS S02065; A29473 REFERENCE S02065 !$#authors Nabeshima, Y.I.; Nabeshima, Y.; Kawashima, M.; Nakamura, S.; !1Nonomura, Y.; Fujii-Kuriyama, Y. !$#journal J. Mol. Biol. (1988) 204:497-505 !$#title Isolation of the chick myosin alkali light chain gene !1expressed in embryonic gizzard muscle and transitional !1expression of the light chain gene family in vivo. !$#cross-references MUID:89141751; PMID:3225843 !$#accession S02065 !'##molecule_type DNA !'##residues 1-185 ##label NAB !'##cross-references EMBL:X14428 !'##note the authors translated the codon CGG for residue 71 as Ala REFERENCE A29473 !$#authors Kawashima, M.; Nabeshima, Y.; Obinata, T.; Fujii-Kuriyama, !1Y. !$#journal J. Biol. Chem. (1987) 262:14408-14414 !$#title A common myosin light chain is expressed in chicken !1embryonic skeletal, cardiac, and smooth muscles and in brain !1continuously from embryo to adult. !$#cross-references MUID:88032983; PMID:3667580 !$#accession A29473 !'##molecule_type mRNA !'##residues 1-93,'L',95-165,'L',167-185 ##label KAW !'##cross-references GB:J02823; NID:g212339; PIDN:AAA48957.1; !1PID:g212340 !'##note the authors translated the codon CTG for residue 94 as Met and !1TAC for residue 175 as Thr COMMENT In chicken, this form is transiently expressed in embryonic !1skeletal, cardiac, and smooth muscle and in embryonic and !1adult brain. GENETICS !$#introns 33/3; 43/1; 93/1; 151/1; 177/1 COMPLEX The myosin molecule contains two heavy chains, two alkali !1light chains, and two regulatory light chains. CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS brain; calcium binding; duplication; EF hand; muscle !1contraction FEATURE !$39-73 #domain calmodulin repeat homology #label EF1\ !$118-150 #domain calmodulin repeat homology #label EF3\ !$153-185 #domain calmodulin repeat homology #label EF4 SUMMARY #length 185 #molecular-weight 20652 #checksum 9004 SEQUENCE /// ENTRY MOHU6M #type complete TITLE myosin alkali light chain 6, smooth muscle form - human ORGANISM #formal_name Homo sapiens #common_name man DATE 09-Mar-1990 #sequence_revision 03-Oct-1995 #text_change 22-Jun-1999 ACCESSIONS B33709; B34757; PS0099 REFERENCE A33709 !$#authors Lenz, S.; Lohse, P.; Seidel, U.; Arnold, H.H. !$#journal J. Biol. Chem. (1989) 264:9009-9015 !$#title The alkali light chains of human smooth and nonmuscle !1myosins are encoded by a single gene. Tissue-specific !1expression by alternative splicing pathways. !$#cross-references MUID:89255377; PMID:2722814 !$#accession B33709 !'##molecule_type DNA; mRNA !'##residues 1-151 ##label LEN !'##cross-references GB:M22920; GB:J04722 !'##experimental_source heart aorta smooth muscle cells REFERENCE A34757 !$#authors Hailstones, D.L.; Gunning, P.W. !$#journal Mol. Cell. Biol. (1990) 10:1095-1104 !$#title Characterization of human myosin light chains 1sa and 3nm: !1implications for isoform evolution and function. !$#cross-references MUID:90158572; PMID:2304459 !$#accession B34757 !'##molecule_type mRNA !'##residues 1-44,'D',46-151 ##label HAI !'##cross-references GB:M31212; NID:g188589; PIDN:AAA59853.1; !1PID:g188590 !'##experimental_source fibroblasts REFERENCE JS0431 !$#authors Seidel, U.; Bober, E.; Winter, B.; Lenz, S.; Lohse, P.; !1Goedde, H.W.; Grzeschik, K.H.; Arnold, H.H. !$#journal Gene (1988) 66:135-146 !$#title Alkali myosin light chains in man are encoded by a multigene !1family that includes the adult skeletal muscle, the !1embryonic or atrial, and nonsarcomeric isoforms. !$#cross-references MUID:88329722; PMID:2458299 !$#accession PS0099 !'##molecule_type mRNA !'##residues 11-84,'A',86-151 ##label SEI !'##experimental_source fetal skeletal muscle GENETICS !$#gene GDB:MYL6 !'##cross-references GDB:344773 !$#map_position 4p16.3-4p16.3 !$#introns 1/3; 11/1; 59/1; 117/1; 143/1 !$#note alternatively spliced forms are expressed in nonmuscle cells !1and eye; see A33709 and A49620 CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS acetylated amino end; alternative splicing; calcium binding; !1duplication; EF hand; muscle contraction; smooth muscle FEATURE !$7-39 #domain calmodulin repeat homology #label EF1\ !$84-116 #domain calmodulin repeat homology #label EF3\ !$119-151 #domain calmodulin repeat homology #label EF4\ !$2 #modified_site acetylated amino end (Cys) (in mature !8form) #status predicted SUMMARY #length 151 #molecular-weight 16930 #checksum 4748 SEQUENCE /// ENTRY MOHU6E #type complete TITLE myosin alkali light chain 6, eye form - human ORGANISM #formal_name Homo sapiens #common_name man DATE 20-Feb-1995 #sequence_revision 03-Oct-1995 #text_change 03-Dec-1999 ACCESSIONS A49620 REFERENCE A49620 !$#authors Bora, P.S.; Bora, N.S.; Wu, X.; Kaplan, H.J.; Lange, L.G. !$#journal Genomics (1994) 19:186-188 !$#title Molecular cloning, sequencing, and characterization of !1smooth muscle myosin alkali light chain from human eye cDNA: !1homology with myocardial fatty acid ethyl ester synthase-III !1cDNA. !$#cross-references MUID:94245166; PMID:8188229 !$#accession A49620 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-157 ##label BOR !'##cross-references GB:U02629; NID:g467827; PIDN:AAA20643.1; !1PID:g467828 COMMENT This form is also expressed in aorta and heart. GENETICS !$#gene GDB:MYL6 !'##cross-references GDB:344773 !$#map_position 4p16.3-4p16.3 !$#note alternatively spliced forms are expressed in smooth muscle !1and nonmuscle cells (see B33709 and A33709) CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS acetylated amino end; alternative splicing; calcium binding; !1duplication; EF hand; eye FEATURE !$7-45 #domain calmodulin repeat homology #label EF1\ !$90-122 #domain calmodulin repeat homology #label EF3\ !$125-157 #domain calmodulin repeat homology #label EF4\ !$2 #modified_site acetylated amino end (Cys) (in mature !8form) #status predicted SUMMARY #length 157 #molecular-weight 17612 #checksum 1468 SEQUENCE /// ENTRY MOHU6N #type complete TITLE myosin alkali light chain 6, nonmuscle form - human ALTERNATE_NAMES MLC1nm ORGANISM #formal_name Homo sapiens #common_name man DATE 09-Mar-1990 #sequence_revision 03-Oct-1995 #text_change 22-Jun-1999 ACCESSIONS A33709 REFERENCE A33709 !$#authors Lenz, S.; Lohse, P.; Seidel, U.; Arnold, H.H. !$#journal J. Biol. Chem. (1989) 264:9009-9015 !$#title The alkali light chains of human smooth and nonmuscle !1myosins are encoded by a single gene. Tissue-specific !1expression by alternative splicing pathways. !$#cross-references MUID:89255377; PMID:2722814 !$#accession A33709 !'##molecule_type DNA; mRNA !'##residues 1-151 ##label LEN !'##cross-references GB:M22919; NID:g189016; PIDN:AAA59893.1; !1PID:g189018; GB:J04722 !'##experimental_source cultured lymphoblasts GENETICS !$#gene GDB:MYL6 !'##cross-references GDB:344773 !$#map_position 4p16.3-4p16.3 !$#introns 1/3; 11/1; 59/1; 117/1; 143/1 !$#note alternatively spliced forms are expressed in smooth muscle !1and eye; see B33709 and A49620 CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS acetylated amino end; alternative splicing; calcium binding; !1duplication; EF hand FEATURE !$7-39 #domain calmodulin repeat homology #label EF1\ !$84-116 #domain calmodulin repeat homology #label EF3\ !$119-151 #domain calmodulin repeat homology #label EF4\ !$2 #modified_site acetylated amino end (Cys) (in mature !8form) #status predicted SUMMARY #length 151 #molecular-weight 16961 #checksum 5471 SEQUENCE /// ENTRY MOCH6N #type complete TITLE myosin alkali light chain 6, nonmuscle form - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Jun-1989 #sequence_revision 03-Oct-1995 #text_change 03-Oct-1995 ACCESSIONS B28488 REFERENCE A92602 !$#authors Nabeshima, Y.; Nabeshima, Y.; Nonomura, Y.; Fujii-Kuriyama, !1Y. !$#journal J. Biol. Chem. (1987) 262:10608-10612 !$#title Nonmuscle and smooth muscle myosin light chain mRNAs are !1generated from a single gene by the tissue-specific !1alternative RNA splicing. !$#cross-references MUID:87280121; PMID:3038890 !$#accession B28488 !'##molecule_type mRNA !'##residues 1-152 ##label NAB !'##experimental_source fibroblasts !'##note the authors translated the codon AAG for residue 66 as Asn; the !1sequence follows the authors translation COMMENT The equivalent form in humans was identified as the smooth !1muscle form in reference A34757. CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS acetylated amino end; alternative splicing; calcium binding; !1duplication; EF hand FEATURE !$7-39 #domain calmodulin repeat homology #label EF1\ !$84-116 #domain calmodulin repeat homology #label EF3\ !$119-152 #domain calmodulin repeat homology #label EF4\ !$2 #modified_site acetylated amino end (Cys) (in mature !8form) #status predicted SUMMARY #length 152 #molecular-weight 17098 #checksum 6394 SEQUENCE /// ENTRY MOCHG2 #type complete TITLE myosin alkali light chain 6, smooth muscle form - chicken ALTERNATE_NAMES myosin G2 catalytic light chain, smooth muscle ORGANISM #formal_name Gallus gallus #common_name chicken DATE 02-Apr-1982 #sequence_revision 03-Oct-1995 #text_change 22-Jun-1999 ACCESSIONS A28488; B03044; A90317; A03039 REFERENCE A92602 !$#authors Nabeshima, Y.; Nabeshima, Y.; Nonomura, Y.; Fujii-Kuriyama, !1Y. !$#journal J. Biol. Chem. (1987) 262:10608-10612 !$#title Nonmuscle and smooth muscle myosin light chain mRNAs are !1generated from a single gene by the tissue-specific !1alternative RNA splicing. !$#cross-references MUID:87280121; PMID:3038890 !$#accession A28488 !'##molecule_type mRNA !'##residues 1-65,'K',67-151 ##label NAB !'##cross-references GB:M15645; GB:J02786; NID:g212392; PIDN:AAA48978.1; !1PID:g212393 !'##experimental_source gizzard !'##note the authors translated the codon AAG for residue 66 as Asn REFERENCE A91298 !$#authors Matsuda, G.; Maita, T.; Kato, Y.; Chen, J.; Umegane, T. !$#journal FEBS Lett. (1981) 135:232-236 !$#title Amino acid sequences of the cardiac L-2A, L-2B and gizzard !117 000-M-r light chains of chicken muscle myosin. !$#cross-references MUID:82095601; PMID:7319048 !$#accession B03044 !'##molecule_type protein !'##residues 2-151 ##label MAT REFERENCE A90317 !$#authors Grand, R.J.A.; Perry, S.V. !$#journal Biochem. J. (1983) 211:267-272 !$#title Preparation of the alkali and P light chains of chicken !1gizzard myosin. Amino acid sequence of the alkali light !1chain. !$#cross-references MUID:83256438; PMID:6870825 !$#accession A90317 !'##molecule_type protein !'##residues 2-100,'D',102-151 ##label GRA COMMENT The equivalent form in humans is identified as the nonmuscle !1form in reference A34757. CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS acetylated amino end; alternative splicing; calcium binding; !1duplication; EF hand; muscle contraction; smooth muscle FEATURE !$7-39 #domain calmodulin repeat homology #label EF1\ !$84-116 #domain calmodulin repeat homology #label EF3\ !$119-151 #domain calmodulin repeat homology #label EF4\ !$2 #modified_site acetylated amino end (Cys) (in mature !8form) #status experimental SUMMARY #length 151 #molecular-weight 16973 #checksum 4618 SEQUENCE /// ENTRY MOHUSA #type complete TITLE myosin alkali light chain, slow skeletal muscle - human ALTERNATE_NAMES MLC1sa ORGANISM #formal_name Homo sapiens #common_name man DATE 13-Jul-1990 #sequence_revision 03-Oct-1995 #text_change 22-Jun-1999 ACCESSIONS A34757; S06913 REFERENCE A34757 !$#authors Hailstones, D.L.; Gunning, P.W. !$#journal Mol. Cell. Biol. (1990) 10:1095-1104 !$#title Characterization of human myosin light chains 1sa and 3nm: !1implications for isoform evolution and function. !$#cross-references MUID:90158572; PMID:2304459 !$#accession A34757 !'##molecule_type mRNA !'##residues 1-208 ##label HAI !'##cross-references GB:M31211; NID:g188582; PIDN:AAA36320.1; !1PID:g188583 !'##experimental_source skeletal muscle REFERENCE S06913 !$#authors Zimmermann, K.; Starzinski-Powitz, A. !$#journal Nucleic Acids Res. (1989) 17:10496 !$#title A novel isoform of myosin alkali light chain isolated from !1human muscle cells. !$#cross-references MUID:90098889; PMID:2602161 !$#accession S06913 !'##molecule_type mRNA !'##residues 1-208 ##label ZIM !'##cross-references EMBL:X16434; NID:g34675; PIDN:CAA34457.1; !1PID:g34676 !'##note the authors translated the codon AAC for residue 111 as Met CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS calcium binding; duplication; EF hand; muscle contraction; !1skeletal muscle FEATURE !$64-96 #domain calmodulin repeat homology #label EF1\ !$141-173 #domain calmodulin repeat homology #label EF3\ !$176-208 #domain calmodulin repeat homology #label EF4 SUMMARY #length 208 #molecular-weight 22764 #checksum 9541 SEQUENCE /// ENTRY MORBLD #type complete TITLE myosin L2 (DTNB) regulatory light chain, skeletal muscle - rabbit ALTERNATE_NAMES MLC2 regulatory light chain; myosin g2 chain ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 31-May-1979 #sequence_revision 01-Mar-1996 #text_change 24-Nov-1999 ACCESSIONS S12691; A03040; S13445; I46493; I46494 REFERENCE S12691 !$#authors Maeda, K.; Mueller-Gerhardt, E.; Wittinghofer, A. !$#journal Nucleic Acids Res. (1990) 18:6687 !$#title Sequence of two isoforms of myosin light chain 2 isolated !1from a rabbit fast skeletal muscle lambda library. !$#cross-references MUID:91067462; PMID:2147475 !$#accession S12691 !'##molecule_type mRNA !'##residues 1-170 ##label MAE !'##cross-references EMBL:X54043; NID:g1636; PIDN:CAA37976.1; PID:g1637 !'##note the authors translated the codon TTC for residue 20 as Ser and !1TGC for residue 158 as Ile REFERENCE A03040 !$#authors Matsuda, G.; Maita, T.; Suzuyama, Y.; Setoguchi, M.; !1Umegane, T. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1978) 359:629-640 !$#title The amino acid sequences of the tryptic, chymotryptic and !1peptic peptides from the L-2 light chain of rabbit skeletal !1muscle myosin. !$#cross-references MUID:78216701; PMID:352892 !$#accession A03040 !'##molecule_type protein !'##residues 3-170 ##label MAT REFERENCE S13445 !$#authors Matsuda, G.; Maita, T.; Suzuyama, Y.; Setoguchi, M.; !1Umegane, T. !$#journal J. Biochem. (1977) 81:809-811 !$#title Amino acid sequence of the L-2 light chain of rabbit !1skeletal muscle myosin. !$#cross-references MUID:77187770; PMID:863872 !$#accession S13445 !'##status preliminary !'##molecule_type protein !'##residues 3-170 ##label MA2 REFERENCE I46471 !$#authors Putney, S.D.; Herlihy, W.C.; Schimmel, P. !$#journal Nature (1983) 302:718-721 !$#title A new troponin T and cDNA clones for 13 different muscle !1proteins, found by shotgun sequencing. !$#cross-references MUID:83167564; PMID:6687628 !$#accession I46493 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 28-39 ##label PUT !'##cross-references EMBL:V00887; NID:g1629; PIDN:CAA24255.1; !1PID:g929758 !$#accession I46494 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 113-146 ##label PU2 !'##cross-references EMBL:V00888; NID:g1631; PIDN:CAA24256.1; !1PID:g929759 CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS blocked amino end; calcium binding; EF hand; muscle; muscle !1contraction; phosphoprotein FEATURE !$26-58 #domain calmodulin repeat homology #label EF1\ !$96-128 #domain calmodulin repeat homology #label EF2\ !$2 #modified_site blocked amino end (Ala) (in mature !8form) (probably trimethylated) #status experimental\ !$17 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$39,41,43,45,50 #binding_site calcium (Asp, Asn, Asp, Ile, Asp) !8#status predicted SUMMARY #length 170 #molecular-weight 19026 #checksum 4395 SEQUENCE /// ENTRY MORTL2 #type complete TITLE myosin L2 (DTNB) regulatory light chain precursor, skeletal muscle - rat ALTERNATE_NAMES MLC2 light chain; myosin g2 chain ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 16-Jul-1999 ACCESSIONS A03041; I55219 REFERENCE A03041 !$#authors Nudel, U.; Calvo, J.M.; Shani, M.; Levy, Z. !$#journal Nucleic Acids Res. (1984) 12:7175-7186 !$#title The nucleotide sequence of a rat myosin light chain 2 gene. !$#cross-references MUID:85014159; PMID:6091059 !$#accession A03041 !'##molecule_type DNA !'##residues 1-169 ##label NUD !'##cross-references GB:X00975; NID:g56726; PIDN:CAA25480.1; PID:g825539 REFERENCE I55219 !$#authors Garfinkel, L.I.; Periasamy, M.; Nadal-Ginard, B. !$#journal J. Biol. Chem. (1982) 257:11078-11086 !$#title Cloning and characterization of cdna sequences corresponding !1to myosin light chains 1, 2, and 3, troponin-c, troponin-t, !1alpha-tropomyosin, and alpha-actin. !$#cross-references MUID:82265830; PMID:6179945 !$#accession I55219 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 70-169 ##label RES !'##cross-references GB:J00754; NID:g205600; PIDN:AAA41660.1; !1PID:g205601 COMMENT Adult rat skeletal muscle contains three light chains: MLC1, !1MLC2, and MLC3 (with molecular weights of approximately 23K, !118K, and 15K, respectively). GENETICS !$#gene MLC2 !$#introns 1/3; 32/3; 58/1; 93/1; 119/2; 135/3 CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS calcium binding; EF hand; muscle contraction; phosphoprotein FEATURE !$2-169 #product myosin L2 (DTNB) regulatory light chain !8#status predicted #label MAT\ !$25-57 #domain calmodulin repeat homology #label EF1\ !$95-127 #domain calmodulin repeat homology #label EF2\ !$16 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$38,40,42,44,49 #binding_site calcium (Asp, Asn, Asp, Ile, Asp) !8#status predicted SUMMARY #length 169 #molecular-weight 18969 #checksum 899 SEQUENCE /// ENTRY MOCHLS #type complete TITLE myosin light chain type 2 (LC2f) [validated] - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Apr-1979 #sequence_revision 16-Jun-2000 #text_change 16-Jun-2000 ACCESSIONS I50393; A03042 REFERENCE I50393 !$#authors Reinach, F.C.; Fischman, D.A. !$#journal J. Mol. Biol. (1985) 181:411-422 !$#title Recombinant DNA approach for defining the primary structure !1of monoclonal antibody epitopes. !$#cross-references MUID:85160861; PMID:2580100 !$#accession I50393 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-168 ##label REI !'##cross-references GB:M11030; NID:g212397; PIDN:AAA48980.1; !1PID:g212398 REFERENCE A03042 !$#authors Suzuyama, Y.; Umegane, T.; Maita, T.; Matsuda, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1980) 361:119-127 !$#title The amino acid sequence of the L-2 light chain of chicken !1skeletal muscle myosin. !$#cross-references MUID:80135740; PMID:7358336 !$#accession A03042 !'##molecule_type protein !'##residues 3-60,'V',62-102,'F',104-168 ##label SUZ !'##note Ser-15 may be phosphorylated; the phosphorylated chain is !1called L3 CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS blocked amino end; calcium binding; EF hand; phosphoprotein FEATURE !$3-168 #product myosin light chain #status experimental !8#label MAT\ !$24-56 #domain calmodulin repeat homology #label EF1\ !$94-126 #domain calmodulin repeat homology #label EF2\ !$3 #modified_site blocked amino end (Pro) (in mature !8form) #status experimental\ !$37,39,41,43,48 #binding_site calcium (Asp, Asn, Asp, Ile, Asp) !8#status predicted SUMMARY #length 168 #molecular-weight 18819 #checksum 5886 SEQUENCE /// ENTRY MOHUL2 #type complete TITLE myosin regulatory light chain 2, slow ventricular muscle - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 22-Jun-1999 ACCESSIONS S03708; S22101 REFERENCE S03708 !$#authors Libera, L.D.; Hoffmann, E.; Floroff, M.; Jackowski, G. !$#journal Nucleic Acids Res. (1989) 17:2360 !$#title Isolation and nucleotide sequence of the cDNA encoding human !1ventricular myosin light chain 2. !$#cross-references MUID:89202052; PMID:2704627 !$#accession S03708 !'##molecule_type mRNA !'##residues 1-165 ##label LIB !'##cross-references EMBL:X14332; NID:g34686; PIDN:CAA32510.1; !1PID:g34687 REFERENCE S22101 !$#authors Grant, J.W.; Jedeloh, J.; Spray, T.; Church, S.L. !$#submission submitted to the EMBL Data Library, May 1992 !$#accession S22101 !'##molecule_type mRNA !'##residues 1-56,'G',57-82,'S',84-165 ##label GRA !'##cross-references EMBL:X66141; NID:g34845; PIDN:CAA46931.1; !1PID:g34846 GENETICS !$#gene GDB:MYL2 !'##cross-references GDB:128829; OMIM:160781 !$#map_position 12q23-12q24.3 CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS calcium binding; cardiac muscle; duplication; EF hand; !1heart; muscle contraction; phosphoprotein FEATURE !$24-56 #domain calmodulin repeat homology #label EF1\ !$93-125 #domain calmodulin repeat homology #label EF3\ !$128-161 #domain calmodulin repeat homology #label EF4\ !$15 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 165 #molecular-weight 18732 #checksum 4701 SEQUENCE /// ENTRY MORT2C #type complete TITLE myosin regulatory light chain L2, cardiac muscle - rat ALTERNATE_NAMES myosin light chain-2 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jul-1999 ACCESSIONS S00752; A34376; A25325 REFERENCE S00752 !$#authors Henderson, S.A.; Xu, Y.C.; Chien, K.R. !$#journal Nucleic Acids Res. (1988) 16:4722 !$#title Nucleotide sequence of full length cDNAs encoding rat !1cardiac myosin light chain-2. !$#cross-references MUID:88247773; PMID:3380697 !$#accession S00752 !'##molecule_type mRNA !'##residues 1-166 ##label HEN !'##cross-references EMBL:X07314; NID:g56682; PIDN:CAA30277.1; !1PID:g56683 REFERENCE A34376 !$#authors Henderson, S.A.; Spencer, M.; Sen, A.; Kumar, C.; Siddiqui, !1M.A.Q.; Chien, K.R. !$#journal J. Biol. Chem. (1989) 264:18142-18148 !$#title Structure, organization, and expression of the rat cardiac !1myosin light chain-2 gene. Identification of a 250-base pair !1fragment which confers cardiac-specific expression. !$#cross-references MUID:90036891; PMID:2808370 !$#accession A34376 !'##status preliminary !'##molecule_type DNA !'##residues 1-166 ##label HEN2 !'##cross-references GB:M30298; GB:J05078; GB:M30299; GB:M30300; !1GB:M30301; GB:M30302; GB:M30303; GB:M30304; NID:g205493; !1PIDN:AAA41624.1; PID:g205495 CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS calcium binding; cardiac muscle; EF hand; heart; !1phosphoprotein FEATURE !$24-56 #domain calmodulin repeat homology #label EF1\ !$94-126 #domain calmodulin repeat homology #label EF2\ !$15 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 166 #molecular-weight 18880 #checksum 7803 SEQUENCE /// ENTRY MOCHAC #type complete TITLE myosin L2A regulatory light chain, cardiac muscle - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 02-Apr-1982 #sequence_revision 02-Apr-1982 #text_change 24-Nov-1999 ACCESSIONS C03044; A93455; I50391; A03043 REFERENCE A91298 !$#authors Matsuda, G.; Maita, T.; Kato, Y.; Chen, J.; Umegane, T. !$#journal FEBS Lett. (1981) 135:232-236 !$#title Amino acid sequences of the cardiac L-2A, L-2B and gizzard !117 000-M-r light chains of chicken muscle myosin. !$#cross-references MUID:82095601; PMID:7319048 !$#accession C03044 !'##molecule_type protein !'##residues 1-163 ##label MAT REFERENCE A93455 !$#authors Arnold, H.H.; Krauskopf, M.; Siddiqui, M.A.Q. !$#journal Nucleic Acids Res. (1983) 11:1123-1131 !$#title The nucleotide sequence of myosin light chain (L-2A) mRNA !1from embryonic chicken cardiac muscle tissue. !$#cross-references MUID:83143327; PMID:6298733 !$#accession A93455 !'##molecule_type mRNA !'##residues 10-123,'GE',126-163 ##label ARN !'##cross-references GB:J00890; NID:g212384 !'##note this ORF is not annotated in GenBank entry CHKMYL2A, release !1103 REFERENCE I50390 !$#authors Winter, B.; Klapthor, H.; Wiebauer, K.; Delius, H.; Arnold, !1H.H. !$#journal J. Biol. Chem. (1985) 260:4478-4483 !$#title Isolation and characterization of the chicken cardiac myosin !1light chain (L-2A) gene. !$#cross-references MUID:85157617; PMID:2984206 !$#accession I50391 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 132-163 ##label WIN !'##cross-references GB:M10991; NID:g212386; PIDN:AAA48976.1; !1PID:g212389 CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS blocked amino end; calcium binding; cardiac muscle; EF hand; !1heart; muscle contraction; phosphoprotein FEATURE !$22-54 #domain calmodulin repeat homology #label EF1\ !$92-123 #domain calmodulin repeat homology #label EF2\ !$1 #modified_site blocked amino end (Pro) #status !8experimental\ !$13 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$35,37,39,41,46 #binding_site calcium (Asp, Asn, Asp, Phe, Asp) !8#status predicted SUMMARY #length 163 #molecular-weight 18503 #checksum 5681 SEQUENCE /// ENTRY MOCHBC #type complete TITLE myosin L2B regulatory light chain, cardiac muscle - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 02-Apr-1982 #sequence_revision 02-Apr-1982 #text_change 24-Nov-1999 ACCESSIONS A03044 REFERENCE A91298 !$#authors Matsuda, G.; Maita, T.; Kato, Y.; Chen, J.; Umegane, T. !$#journal FEBS Lett. (1981) 135:232-236 !$#title Amino acid sequences of the cardiac L-2A, L-2B and gizzard !117 000-M-r light chains of chicken muscle myosin. !$#cross-references MUID:82095601; PMID:7319048 !$#accession A03044 !'##molecule_type protein !'##residues 1-163 ##label MAT CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS blocked amino end; calcium binding; cardiac muscle; EF hand; !1heart; phosphoprotein FEATURE !$21-53 #domain calmodulin repeat homology #label EF1\ !$91-123 #domain calmodulin repeat homology #label EF2\ !$1 #modified_site blocked amino end (Pro) #status !8experimental\ !$12 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$34,36,38,40,45 #binding_site calcium (Asp, Asn, Asp, Phe, Asp) !8#status predicted SUMMARY #length 163 #molecular-weight 18587 #checksum 5593 SEQUENCE /// ENTRY MOHULP #type complete TITLE myosin regulatory light chain, placental - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jul-1999 ACCESSIONS S11493 REFERENCE S11493 !$#authors Grant, J.W.; Zhong, R.Q.; McEwen, P.M.; Church, S.L. !$#journal Nucleic Acids Res. (1990) 18:5892 !$#title Human nonsarcomeric 20,000 Da myosin regulatory light chain !1cDNA. !$#cross-references MUID:91016942; PMID:2216787 !$#accession S11493 !'##molecule_type mRNA !'##residues 1-171 ##label GRA !'##cross-references EMBL:X54304; NID:g34755; PIDN:CAA38201.1; !1PID:g34756 CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS calcium binding; EF hand; phosphoprotein FEATURE !$28-60 #domain calmodulin repeat homology #label EF1\ !$97-129 #domain calmodulin repeat homology #label EF2\ !$19 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 171 #molecular-weight 19794 #checksum 6170 SEQUENCE /// ENTRY MOCH2G #type complete TITLE myosin regulatory light chain 2, smooth muscle (minor) - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jul-1999 ACCESSIONS S05530 REFERENCE S05530 !$#authors Inoue, A.; Yanagisawa, M.; Takano-Ohmuro, H.; Masaki, T. !$#journal Eur. J. Biochem. (1989) 183:645-651 !$#title Two isoforms of smooth muscle myosin regulatory light chain !1in chicken gizzard. !$#cross-references MUID:89377832; PMID:2776758 !$#accession S05530 !'##molecule_type mRNA !'##residues 1-172 ##label INO !'##cross-references EMBL:X16532; NID:g62937; PIDN:CAA34535.1; !1PID:g62938 CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS calcium binding; EF hand; phosphoprotein FEATURE !$2-172 #product myosin regulatory chain #status predicted !8#label MAT\ !$29-61 #domain calmodulin repeat homology #label EF1\ !$98-130 #domain calmodulin repeat homology #label EF2\ !$19 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$20 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 172 #molecular-weight 19911 #checksum 5936 SEQUENCE /// ENTRY MOCHG1 #type complete TITLE myosin regulatory light chain 2, smooth muscle (major) - chicken ALTERNATE_NAMES myosin regulatory light chain G1 ORGANISM #formal_name Gallus gallus #common_name chicken DATE 02-Apr-1982 #sequence_revision 30-Sep-1991 #text_change 21-Jul-2000 ACCESSIONS S03184; S00665; A03045; S10230; S15359 REFERENCE S03184 !$#authors Messer, N.G.; Kendrick-Jones, J. !$#journal FEBS Lett. (1988) 234:49-52 !$#title Molecular cloning and sequencing of the chicken smooth !1muscle myosin regulatory light chain. !$#cross-references MUID:88271623; PMID:3391271 !$#accession S03184 !'##molecule_type mRNA !'##residues 1-172 ##label MES !'##cross-references EMBL:Y00983; NID:g63612; PIDN:CAB46269.1; !1PID:g5326989 REFERENCE S00665 !$#authors Zavodny, P.J.; Petro, M.E.; Kumar, C.C.; Dailey, S.H.; !1Lonial, H.K.; Narula, S.K.; Leibowitz, P.J. !$#journal Nucleic Acids Res. (1988) 16:1214 !$#title The nucleotide sequence of chicken smooth muscle myosin !1light chain two. !$#cross-references MUID:88144007; PMID:3344215 !$#accession S00665 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-172 ##label ZAV !'##cross-references EMBL:X06387; NID:g63605; PIDN:CAA29684.1; !1PID:g63606 REFERENCE A03045 !$#authors Maita, T.; Chen, J.; Matsuda, G. !$#journal Eur. J. Biochem. (1981) 117:417-424 !$#title Amino-acid sequence of the 20 000-molecular-weight light !1chain of chicken gizzard-muscle myosin. !$#cross-references MUID:82004185; PMID:7274219 !$#accession A03045 !'##molecule_type protein !'##residues 2-5;6-12;13-17;18-172 ##label MAI REFERENCE S10230 !$#authors Pearson, R.B.; Jakes, R.; John, M.; Kendrick-Jones, J.; !1Kemp, B.E. !$#journal FEBS Lett. (1984) 168:108-112 !$#title Phosphorylation site sequence of smooth muscle myosin light !1chain (Mr=20000). !$#cross-references MUID:84158942; PMID:6546724 !$#accession S10230 !'##molecule_type protein !'##residues 2-23 ##label PEA REFERENCE S05530 !$#authors Inoue, A.; Yanagisawa, M.; Takano-Ohmuro, H.; Masaki, T. !$#journal Eur. J. Biochem. (1989) 183:645-651 !$#title Two isoforms of smooth muscle myosin regulatory light chain !1in chicken gizzard. !$#cross-references MUID:89377832; PMID:2776758 !$#accession S15359 !'##molecule_type protein !'##residues 64-73 ##label INO CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS acetylated amino end; calcium binding; EF hand; !1phosphoprotein FEATURE !$2-172 #product myosin regulatory light chain 2 #status !8experimental #label MAT\ !$29-61 #domain calmodulin repeat homology #label EF1\ !$98-130 #domain calmodulin repeat homology #label EF2\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental\ !$19 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$20 #binding_site phosphate (Ser) (covalent) #status !8experimental SUMMARY #length 172 #molecular-weight 19845 #checksum 6387 SEQUENCE /// ENTRY MOSWLE #type complete TITLE myosin EDTA regulatory light chain - scallop (Pectinidae gen. sp.) ORGANISM #formal_name Pectinidae gen. sp. #common_name scallop DATE 31-May-1979 #sequence_revision 31-May-1979 #text_change 24-Nov-1999 ACCESSIONS A03046 REFERENCE A03046 !$#authors Kendrick-Jones, J.; Jakes, R. !$#book Myocardial Failure (Int. Boehringer Mannheim Symp.), !1Riecker, G., Weber, A., and Goodwin, J., eds., pp.28-40, !1Springer-Verlag, Berlin and New York, 1977 !$#accession A03046 !'##molecule_type protein !'##residues 1-153 ##label KEN CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS blocked amino end; calcium binding; EF hand FEATURE !$15-47 #domain calmodulin repeat homology #label EF1\ !$81-113 #domain calmodulin repeat homology #label EF2\ !$1 #modified_site blocked amino end (Ala) #status !8experimental\ !$28,30,32,34,39 #binding_site calcium (Asp, Asp, Asp, Phe, Asp) !8#status predicted SUMMARY #length 153 #molecular-weight 17207 #checksum 3883 SEQUENCE /// ENTRY MOSWLA #type complete TITLE myosin regulatory light chain a, smooth muscle - scallop (Patinopecten yessoensis) ALTERNATE_NAMES myosin RLCa ORGANISM #formal_name Patinopecten yessoensis #common_name Yesso scallop DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 24-Nov-1999 ACCESSIONS A03048 REFERENCE A91994 !$#authors Miyanishi, T.; Maita, T.; Morita, F.; Kondo, S.; Matsuda, G. !$#journal J. Biochem. (1985) 97:541-551 !$#title Amino acid sequences of the two kinds of regulatory light !1chains of adductor smooth muscle myosin from Patinopecten !1yessoensis. !$#cross-references MUID:85234437; PMID:4008467 !$#accession A03048 !'##molecule_type protein !'##residues 1-161 ##label MIY COMMENT This protein came from the adductor smooth muscle. COMMENT Smooth muscle myosin from the scallop adductor muscle !1contains two kinds of RLC proteins, a and b. Because RLCa !1hydrolyzes ATP and superprecipitates more slowly than RLCb, !1myosins containing RLCa are thought to induce the catch !1mechanism, a tonic contraction characterizing smooth muscle !1that is maintained with very slow ATP hydrolysis. COMMENT The calcium affinity of the smooth muscle RLC is !1approximately 10 times that of the RLC of striated muscle. CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS ATP; blocked amino end; calcium binding; EF hand; muscle !1contraction FEATURE !$20-52 #domain calmodulin repeat homology #label EF1\ !$89-121 #domain calmodulin repeat homology #label EF2\ !$1 #modified_site blocked amino end (Ala) #status !8experimental\ !$33,35,37,39,44 #binding_site calcium (Asp, Asn, Asp, Phe, Asp) !8#status predicted SUMMARY #length 161 #molecular-weight 18384 #checksum 1584 SEQUENCE /// ENTRY MOSWLB #type complete TITLE myosin regulatory light chain b, smooth muscle - scallop (Patinopecten yessoensis) ALTERNATE_NAMES myosin RLCb ORGANISM #formal_name Patinopecten yessoensis #common_name Yesso scallop DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 24-Nov-1999 ACCESSIONS A03047 REFERENCE A91994 !$#authors Miyanishi, T.; Maita, T.; Morita, F.; Kondo, S.; Matsuda, G. !$#journal J. Biochem. (1985) 97:541-551 !$#title Amino acid sequences of the two kinds of regulatory light !1chains of adductor smooth muscle myosin from Patinopecten !1yessoensis. !$#cross-references MUID:85234437; PMID:4008467 !$#accession A03047 !'##molecule_type protein !'##residues 1-156 ##label MIY COMMENT This protein came from the adductor smooth muscle. COMMENT Smooth muscle myosin from the scallop adductor muscle !1contains two kinds of RLC proteins, a and b. Because RLCa !1hydrolyzes ATP and superprecipitates more slowly than RLCb, !1myosins containing RLCa are thought to induce the catch !1mechanism, a tonic contraction characterizing smooth muscle !1that is maintained with very slow ATP hydrolysis. COMMENT The calcium affinity of the smooth muscle RLC is !1approximately 10 times that of the RLC of striated muscle. CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS ATP; blocked amino end; calcium binding; EF hand; muscle !1contraction FEATURE !$15-47 #domain calmodulin repeat homology #label EF1\ !$84-116 #domain calmodulin repeat homology #label EF2\ !$1 #modified_site blocked amino end (Ala) #status !8experimental\ !$28,30,32,34,39 #binding_site calcium (Asp, Asn, Asp, Phe, Asp) !8#status predicted SUMMARY #length 156 #molecular-weight 17621 #checksum 4052 SEQUENCE /// ENTRY KLSSBS #type complete TITLE calcium-binding protein beta chain - penaeid shrimp (Penaeus sp.) ALTERNATE_NAMES sarcoplasmic calcium-binding protein (SCP) ORGANISM #formal_name Penaeus sp. DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 17-Apr-1998 ACCESSIONS A03072 REFERENCE A03072 !$#authors Takagi, T.; Konishi, K. !$#journal J. Biochem. (1984) 96:59-67 !$#title Amino acid sequence of the beta chain of sarcoplasmic !1calcium binding protein (SCP) obtained from shrimp tail !1muscle. !$#cross-references MUID:85030293; PMID:6490607 !$#accession A03072 !'##molecule_type protein !'##residues 1-192 ##label TAK COMMENT This protein has three high-affinity calcium-binding sites; !1however, by comparison with the sarcoplasmic calcium-binding !1proteins from scallop and sandworm, it appears that there !1may originally have been a fourth site (residues 140-152) !1that lost its affinity for calcium due to amino acid !1replacements. COMMENT The sarcoplasmic calcium-binding proteins are abundant in !1the muscle of arthropods, molluscs, annelids, and !1protochordates. Most are monomers; only the crustacean !1protein exists as a dimer of either identical or very !1similar chains. The biological function of these proteins !1may be similar to that of vertebrate parvalbumin. CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS acetylated amino end; calcium binding; duplication; EF hand; !1muscle FEATURE !$4-36 #domain calmodulin repeat homology #label EF1\ !$56-88 #domain calmodulin repeat homology #label EF2\ !$100-132 #domain calmodulin repeat homology #label EF3\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$17,19,21,23,28 #binding_site calcium (Asp, Asp, Asp, Phe, Asp) !8#status predicted\ !$69,71,73,75,80 #binding_site calcium (Asp, Asn, Asp, Glu, Glu) !8#status predicted\ !$113,115,117,119,124 #binding_site calcium (Asp, Asp, Asp, Met, Glu) !8#status predicted SUMMARY #length 192 #molecular-weight 21967 #checksum 7324 SEQUENCE /// ENTRY KLSSAB #type complete TITLE calcium-binding protein alpha-b chain - penaeid shrimp (Penaeus sp.) ALTERNATE_NAMES sarcoplasmic calcium-binding protein (SCP) ORGANISM #formal_name Penaeus sp. DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 17-Apr-1998 ACCESSIONS A03073 REFERENCE A91977 !$#authors Takagi, T.; Konishi, K. !$#journal J. Biochem. (1984) 95:1603-1615 !$#title Amino acid sequence of alpha chain of sarcoplasmic calcium !1binding protein obtained from shrimp tail muscle. !$#cross-references MUID:84289338; PMID:6469940 !$#accession A03073 !'##molecule_type protein !'##residues 1-192 ##label TAK COMMENT The SCPs from crayfish, lobster, and shrimp are polymorphic !1dimers; three isotypes (alpha-alpha, alpha-beta, and !1beta-beta) have been identified. COMMENT This protein has three high-affinity calcium-binding sites; !1a fourth possible site (residues 140-152) has lost its !1affinity for calcium due to amino acid replacements. CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS acetylated amino end; calcium binding; duplication; EF hand; !1muscle FEATURE !$4-36 #domain calmodulin repeat homology #label EF1\ !$56-88 #domain calmodulin repeat homology #label EF2\ !$100-132 #domain calmodulin repeat homology #label EF3\ !$139-171 #domain calmodulin repeat homology #label EF4\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$17,19,21,23,28 #binding_site calcium (Asp, Asp, Asp, Phe, Asp) !8#status predicted\ !$69,71,73,75,80 #binding_site calcium (Asp, Asn, Asp, Glu, Glu) !8#status predicted\ !$113,115,117,119,124 #binding_site calcium (Asp, Asn, Asp, Lys, Glu) !8#status predicted SUMMARY #length 192 #molecular-weight 21979 #checksum 7985 SEQUENCE /// ENTRY KLSSAA #type complete TITLE calcium-binding protein alpha-a chain - penaeid shrimp (Penaeus sp.) ALTERNATE_NAMES sarcoplasmic calcium-binding protein (SCP) ORGANISM #formal_name Penaeus sp. DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 07-Aug-1998 ACCESSIONS A03074 REFERENCE A91977 !$#authors Takagi, T.; Konishi, K. !$#journal J. Biochem. (1984) 95:1603-1615 !$#title Amino acid sequence of alpha chain of sarcoplasmic calcium !1binding protein obtained from shrimp tail muscle. !$#cross-references MUID:84289338; PMID:6469940 !$#accession A03074 !'##molecule_type protein !'##residues 1-190 ##label TAK !'##experimental_source tail muscle COMMENT The SCPs from crayfish, lobster, and shrimp are polymorphic !1dimers; three isotypes (alpha-alpha, alpha-beta, and !1beta-beta) have been identified. COMMENT This protein has three high-affinity calcium-binding sites; !1a fourth possible site (residues 138-149) has lost its !1affinity for calcium due to amino acid replacements. CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS acetylated amino end; calcium binding; duplication; EF hand; !1muscle FEATURE !$3-35 #domain calmodulin repeat homology #label EF1\ !$55-86 #domain calmodulin repeat homology #label EF2\ !$98-130 #domain calmodulin repeat homology #label EF3\ !$137-169 #domain calmodulin repeat homology #label EF4\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$16,18,20,22,27 #binding_site calcium (Asp, Asp, Asp, Phe, Asp) !8#status predicted\ !$67,69,71,73,78 #binding_site calcium (Asp, Asn, Asp, Glu, Glu) !8#status predicted\ !$111,113,115,117,122 #binding_site calcium (Asp, Asn, Asp, Lys, Glu) !8#status predicted SUMMARY #length 190 #molecular-weight 21578 #checksum 4653 SEQUENCE /// ENTRY KLSWM #type complete TITLE calcium-binding protein, muscle - scallop (Patinopecten yessoensis) (tentative sequence) ALTERNATE_NAMES sarcoplasmic calcium-binding protein (SCP) ORGANISM #formal_name Patinopecten yessoensis #common_name Yesso scallop DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 31-Mar-2000 ACCESSIONS A03075 REFERENCE A03075 !$#authors Takagi, T.; Kobayashi, T.; Konishi, K. !$#journal Biochim. Biophys. Acta (1984) 787:252-257 !$#title Amino-acid sequence of sarcoplasmic calcium-binding protein !1from scallop (Patinopecten yessoensis) adductor striated !1muscle. !$#accession A03075 !'##molecule_type protein !'##residues 1-176 ##label TAK COMMENT This protein has only two functional calcium-binding sites; !1potential sites II and IV have lost affinity for calcium, !1possibly due to evolutionary changes in their amino acid !1sequences. CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS acetylated amino end; calcium binding; EF hand; muscle FEATURE !$31-63 #domain calmodulin repeat homology #label EF1\ !$91-123 #domain calmodulin repeat homology #label EF2\ !$1 #modified_site acetylated amino end (Thr) #status !8experimental\ !$16,18,20,22,27 #binding_site calcium (Asp, Asn, Asp, Ile, Asn) !8#status predicted\ !$104,106,108,110,115 #binding_site calcium (Asp, Asp, Asp, Ser, Glu) !8#status predicted SUMMARY #length 176 #molecular-weight 20087 #checksum 8066 SEQUENCE /// ENTRY A33391 #type complete TITLE calcineurin regulatory chain - human ALTERNATE_NAMES calcineurin beta subunit; calcineurin chain B; phosphoprotein phosphatase chain B; protein phosphatase 2B ORGANISM #formal_name Homo sapiens #common_name man DATE 09-Mar-1990 #sequence_revision 09-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS A33391 REFERENCE A33391 !$#authors Guerini, D.; Krinks, M.H.; Sikela, J.M.; Hahn, W.E.; Klee, !1C.B. !$#journal DNA (1989) 8:675-682 !$#title Isolation and sequence of a cDNA clone for human calcineurin !1B, the Ca(2+)-binding subunit of the Ca(2+)/ !1calmodulin-stimulated protein phosphatase. !$#cross-references MUID:90126237; PMID:2558868 !$#accession A33391 !'##molecule_type mRNA !'##residues 1-170 ##label GUE !'##cross-references GB:M30773; NID:g180704; PIDN:AAB08721.1; !1PID:g180705 GENETICS !$#gene GDB:PPP3R1; CALNB !'##cross-references GDB:136804; OMIM:601302 !$#map_position 2p16-2p15 COMPLEX heterodimer with calcineurin catalytic chain CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS blocked amino end; calcium binding; duplication; EF hand; !1heterodimer; lipoprotein; myristylation FEATURE !$2-170 #product calcineurin regulatory chain #status !8predicted #label MAT\ !$18-49 #domain calmodulin repeat homology #label EF1\ !$50-82 #domain calmodulin repeat homology #label EF2\ !$87-119 #domain calmodulin repeat homology #label EF3\ !$128-160 #domain calmodulin repeat homology #label EF4\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #modified_site aspartic acid (Asn) #status predicted\ !$31,33,35,37,42 #binding_site calcium (Asp, Asp, Ser, Ser, Glu) !8#status predicted\ !$63,65,67,69,74 #binding_site calcium (Asp, Asp, Asn, Glu, Glu) !8#status predicted\ !$100,102,104,106,111 #binding_site calcium (Asp, Asp, Asp, Tyr, Glu) !8#status predicted\ !$141,143,145,147,152 #binding_site calcium (Asp, Asp, Asp, Arg, Glu) !8#status predicted SUMMARY #length 170 #molecular-weight 19300 #checksum 294 SEQUENCE /// ENTRY S34127 #type complete TITLE calcineurin regulatory chain [validated] - bovine ALTERNATE_NAMES calcineurin beta subunit; calcineurin chain B; phosphoprotein phosphatase chain B; protein phosphatase 2B ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 15-Sep-2000 ACCESSIONS I45831; JT0297; S34127 REFERENCE I45831 !$#authors Nargang, C.E.; Bottorff, D.A.; Adachi, K. !$#journal DNA Seq. (1994) 4:313-318 !$#title Isolation and characterization of a cDNA clone coding for !1the calcium-binding subunit of calcineurin from bovine !1brain: an identical amino acid sequence to the human !1protein. !$#cross-references MUID:95102111; PMID:7803816 !$#accession I45831 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-170 ##label NA2 !'##cross-references EMBL:X71666; NID:g312968; PIDN:CAA50659.1; !1PID:g312969 REFERENCE JT0297 !$#authors Aitken, A.; Klee, C.B.; Cohen, P. !$#journal Eur. J. Biochem. (1984) 139:663-671 !$#title The structure of the B subunit of calcineurin. !$#cross-references MUID:84132092; PMID:6321184 !$#accession JT0297 !'##molecule_type protein !'##residues 2-11,'M',13-153,'S',155-169 ##label AIT REFERENCE A66708 !$#authors Griffith, J.P.; Kim, J.L.; Kim, E.E.; Sintchak, M.D.; !1Thomson, J.A.; Fitzgibbon, M.J.; Fleming, M.A.; Caron, P.R.; !1Hsiao, K.; Navia, M.A. !$#submission submitted to the Brookhaven Protein Data Bank, August 1996 !$#cross-references PDB:1TCO !$#contents annotation; X-ray crystallography, 2.5 angstroms, residues !12-170 REFERENCE A56967 !$#authors Griffith, J.P.; Kim, J.L.; Kim, E.E.; Sintchak, M.D.; !1Thomson, J.A.; Fitzgibbon, M.J.; Fleming, M.A.; Caron, P.R.; !1Hsiao, K.; Navia, M.A. !$#journal Cell (1995) 82:507-522 !$#title X-ray structure of calcineurin inhibited by the !1immunophilin-immunosuppressant FKBP12-FK506 complex. !$#cross-references MUID:95360994; PMID:7543369 !$#contents annotation; X-ray crystallography, 2.5 angstroms COMPLEX heterodimer with calcineurin catalytic chain (see !1PIR:A56968) CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS blocked amino end; calcium binding; duplication; EF hand; !1heterodimer; lipoprotein; myristylation FEATURE !$2-170 #product calcineurin regulatory chain #status !8experimental #label MAT\ !$18-49 #domain calmodulin repeat homology #label EF1\ !$50-82 #domain calmodulin repeat homology #label EF2\ !$87-119 #domain calmodulin repeat homology #label EF3\ !$128-160 #domain calmodulin repeat homology #label EF4\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status experimental\ !$3 #modified_site aspartic acid (Asn) #status predicted\ !$31,33,35,37,42 #binding_site calcium (Asp, Asp, Ser, Ser, Glu) !8#status experimental\ !$63,65,67,69,74 #binding_site calcium (Asp, Asp, Asn, Glu, Glu) !8#status experimental\ !$100,102,104,106,111 #binding_site calcium (Asp, Asp, Asp, Tyr, Glu) !8#status experimental\ !$141,143,145,147,152 #binding_site calcium (Asp, Asp, Asp, Arg, Glu) !8#status experimental SUMMARY #length 170 #molecular-weight 19300 #checksum 294 SEQUENCE /// ENTRY S42716 #type complete TITLE calcineurin regulatory chain, long splice form - rat ALTERNATE_NAMES calcineurin beta subunit; calcineurin chain B; phosphoprotein phosphatase chain B; protein phosphatase 2B CONTAINS calcineurin regulatory chain, short splice form ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S42716; S42717 REFERENCE S42716 !$#authors Chang, C.D.; Mukai, H.; Kuno, T.; Tanaka, C. !$#journal Biochim. Biophys. Acta (1994) 1217:174-180 !$#title cDNA cloning of an alternatively spliced isoform of the !1regulatory subunit of Ca(2+)/calmodulin-dependent protein !1phosphatase (calcineurin B-alpha-2). !$#cross-references MUID:94153993; PMID:8110831 !$#accession S42716 !'##status preliminary !'##molecule_type mRNA !'##residues 1-216 ##label CHA1 !'##cross-references EMBL:D14425; NID:g286205; PIDN:BAA03318.1; !1PID:g286206 !$#accession S42717 !'##status preliminary !'##molecule_type mRNA !'##residues 'M',48-216 ##label CHA2 !'##cross-references EMBL:D14568; NID:g286255; PIDN:BAA03422.1; !1PID:g286256 COMPLEX heterodimer with calcineurin catalytic chain CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS alternative splicing; blocked amino end; calcium binding; !1duplication; EF hand; heterodimer; lipoprotein; !1myristylation FEATURE !$2-216 #product calcineurin regulatory chain, long splice !8form #status predicted #label MATL\ !$48-216 #product calcineurin regulatory chain, short splice !8form #status predicted #label MATS\ !$64-95 #domain calmodulin repeat homology #label EF1\ !$96-128 #domain calmodulin repeat homology #label EF2\ !$'M',48-216 #product calcineurin regulatory chain, short splice !8form precursor #status predicted #label PRES\ !$133-165 #domain calmodulin repeat homology #label EF3\ !$174-206 #domain calmodulin repeat homology #label EF4\ !$48 #modified_site myristylated amino end (Gly) (in !8mature form) #status experimental\ !$49 #modified_site aspartic acid (Asn) #status predicted SUMMARY #length 216 #molecular-weight 24979 #checksum 4062 SEQUENCE /// ENTRY JC1220 #type complete TITLE calcineurin regulatory chain, brain - mouse ALTERNATE_NAMES calcineurin beta-1 subunit; calcineurin chain B-1; phosphoprotein phosphatase chain B; protein phosphatase 2B ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JC1220 REFERENCE JC1220 !$#authors Ueki, K.; Muramatsu, T.; Kincaid, R.L. !$#journal Biochem. Biophys. Res. Commun. (1992) 187:537-543 !$#title Structure and expression of two isoforms of the murine !1calmodulin-dependent protein phosphatase regulatory subunit !1(calcineurin B). !$#cross-references MUID:92392379; PMID:1325794 !$#accession JC1220 !'##molecule_type mRNA !'##residues 1-170 ##label UEK !'##cross-references GB:S43864; NID:g255078; PIDN:AAB23171.1; !1PID:g255079 !'##experimental_source brain COMMENT With calcineurin catalytic chain plays an important role in !1neural and nonneural calcium-regulated signaling. GENETICS !$#gene PP2B-beta-1 COMPLEX heterodimer with calcineurin catalytic chain CLASSIFICATION #superfamily calmodulin; calmodulin repeat homology KEYWORDS blocked amino end; calcium binding; duplication; EF hand; !1heterodimer; lipoprotein; myristylation FEATURE !$2-170 #product calcineurin regulatory chain #status !8predicted #label MAT\ !$18-49 #domain calmodulin repeat homology #label EF1\ !$50-82 #domain calmodulin repeat homology #label EF2\ !$87-119 #domain calmodulin repeat homology #label EF3\ !$128-160 #domain calmodulin repeat homology #label EF4\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted SUMMARY #length 170 #molecular-weight 19273 #checksum 309 SEQUENCE /// ENTRY A60253 #type complete TITLE calretinin - human ALTERNATE_NAMES calbindin 29 ORGANISM #formal_name Homo sapiens #common_name man DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 05-May-2000 ACCESSIONS S14109; A60253 REFERENCE S14109 !$#authors Parmentier, M.; Lefort, A. !$#journal Eur. J. Biochem. (1991) 196:79-85 !$#title Structure of the human brain calcium-binding protein !1calretinin and its expression in bacteria. !$#cross-references MUID:91160569; PMID:2001709 !$#accession S14109 !'##status preliminary !'##molecule_type DNA !'##residues 1-271 ##label PAR !'##cross-references GB:X56667; NID:g29635; PIDN:CAA39991.1; PID:g29636 REFERENCE A60253 !$#authors Parmentier, M. !$#journal Adv. Exp. Med. Biol. (1989) 255:233-240 !$#title The human calbindins: cDNA and gene cloning. !$#cross-references MUID:90144185; PMID:2618861 !$#accession A60253 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-271 ##label PA2 GENETICS !$#gene GDB:CALB2; CAL2 !'##cross-references GDB:125374; OMIM:114051 !$#map_position 16q22.2-16q22.2 CLASSIFICATION #superfamily calretinin; calmodulin repeat homology KEYWORDS brain; calcium binding; duplication; EF hand FEATURE !$16-48 #domain calmodulin repeat homology #label EF1\ !$63-95 #domain calmodulin repeat homology #label EF2\ !$107-139 #domain calmodulin repeat homology #label EF3\ !$151-183 #domain calmodulin repeat homology #label EF4\ !$195-227 #domain calmodulin repeat homology #label EF5\ !$29,31,33,35,40 #binding_site calcium (Asp, Asp, Asn, Tyr, Glu) !8#status predicted\ !$120,122,124,126,131 #binding_site calcium (Asp, Asp, Ser, Tyr, Glu) !8#status predicted\ !$164,166,168,170,175 #binding_site calcium (Asp, Asn, Asp, Lys, Glu) !8#status predicted\ !$208,210,212,214,219 #binding_site calcium (Asp, Asp, Ser, Tyr, Glu) !8#status predicted SUMMARY #length 271 #molecular-weight 31522 #checksum 6222 SEQUENCE /// ENTRY S25006 #type complete TITLE calretinin - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 05-May-2000 ACCESSIONS S25006; B38396 REFERENCE S25006 !$#authors Strauss, K.I.; Jacobowitz, D.M. !$#submission submitted to the EMBL Data Library, June 1992 !$#description Nucleotide sequence of rat calretinin cDNA: Evolutionary !1conservation of coding and noncoding regions. !$#accession S25006 !'##molecule_type mRNA !'##residues 1-271 ##label STR !'##cross-references EMBL:X66974; NID:g55852; PIDN:CAA47385.1; !1PID:g55853 REFERENCE A38396 !$#authors Gabrielides, C.; McCormack, A.L.; Hunt, D.F.; Christakos, S. !$#journal Biochemistry (1991) 30:656-662 !$#title Brain calbindin-D-28k and an M-r 29 000 calcium binding !1protein in cerebellum are different but related proteins: !1evidence obtained from sequence analysis by tandem mass !1spectrometry. !$#cross-references MUID:91105154; PMID:1988053 !$#accession B38396 !'##status preliminary !'##molecule_type protein !'##residues 'E',3,'X',5-6,'X',8-10,'X',12,'X',14-15,'X',17-21,'X';23, !1'X',42-47,'X',49-50;'X',89-90,'XX',93-98,'XX';103-109,'SD', !1112;124-126,'X',128-131,'X',133-135,'X',137-138,'XX', !1141-147;'X',153-158,'XX',161;164,'XD',167-170,'X',172,'X', !1174-178,'XX',181-186,'XX',189;'XN','XSVAYK';'W',248-249, !1'PS',252-255,'X',257-260,'X',262,'X',264,'X' ##label GAB CLASSIFICATION #superfamily calretinin; calmodulin repeat homology KEYWORDS brain; calcium binding; duplication; EF hand FEATURE !$16-48 #domain calmodulin repeat homology #label EF1\ !$63-95 #domain calmodulin repeat homology #label EF2\ !$107-139 #domain calmodulin repeat homology #label EF3\ !$151-183 #domain calmodulin repeat homology #label EF4\ !$195-227 #domain calmodulin repeat homology #label EF5 SUMMARY #length 271 #molecular-weight 31404 #checksum 6176 SEQUENCE /// ENTRY A27067 #type complete TITLE calretinin - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 05-May-2000 ACCESSIONS S34773; A92748; B29957; A27067; S18108 REFERENCE S34773 !$#authors Cheung, W.T.; Richards, D.E.; Rogers, J.H. !$#journal Eur. J. Biochem. (1993) 215:401-410 !$#title Calcium binding by chick calretinin and rat calbindin D28k !1synthesised in bacteria. !$#cross-references MUID:93345528; PMID:8344307 !$#accession S34773 !'##molecule_type mRNA !'##residues 1-269 ##label CHE !'##cross-references EMBL:X62866; NID:g63162; PIDN:CAA44666.1; !1PID:g63163 REFERENCE A92748 !$#authors Rogers, J.H. !$#journal J. Cell Biol. (1987) 105:1343-1353 !$#title Calretinin: a gene for a novel calcium-binding protein !1expressed principally in neurons. !$#cross-references MUID:88007859; PMID:3654755 !$#accession A92748 !'##molecule_type mRNA !'##residues 6-194 ##label ROG !'##cross-references GB:Y00625; NID:g63160; PIDN:CAA68664.1; PID:g939871 REFERENCE A92753 !$#authors Rogers, J.H. !$#journal J. Cell Biol. (1990) 110:1843 !$#contents annotation; correction of typographical error REFERENCE A29957 !$#authors Wilson, P.W.; Rogers, J.; Harding, M.; Pohl, V.; Pattyn, G.; !1Lawson, D.E.M. !$#journal J. Mol. Biol. (1988) 200:615-625 !$#title Structure of chick chromosomal genes for calbindin and !1calretinin. !$#cross-references MUID:88316929; PMID:3411606 !$#accession B29957 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type DNA !'##residues 54-207 ##label WIL CLASSIFICATION #superfamily calretinin; calmodulin repeat homology KEYWORDS brain; calcium binding; duplication; EF hand FEATURE !$14-46 #domain calmodulin repeat homology #label EF1\ !$61-93 #domain calmodulin repeat homology #label EF2\ !$105-137 #domain calmodulin repeat homology #label EF3\ !$149-181 #domain calmodulin repeat homology #label EF4\ !$193-225 #domain calmodulin repeat homology #label EF5 SUMMARY #length 269 #molecular-weight 31077 #checksum 9372 SEQUENCE /// ENTRY S00234 #type complete TITLE calcium-binding protein, vitamin D-dependent - human ALTERNATE_NAMES calbindin D28 ORGANISM #formal_name Homo sapiens #common_name man DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 05-May-2000 ACCESSIONS S00234; A30143 REFERENCE S00234 !$#authors Parmentier, M.; Lawson, D.E.M.; Vassart, G. !$#journal Eur. J. Biochem. (1987) 170:207-215 !$#title Human 27-kDa calbindin complementary DNA sequence. !1Evolutionary and functional implications. !$#cross-references MUID:88082818; PMID:3691519 !$#accession S00234 !'##molecule_type mRNA !'##residues 1-261 ##label PAR !'##cross-references EMBL:X06661; NID:g29603; PIDN:CAA29860.1; !1PID:g29604 REFERENCE A30143 !$#authors Parmentier, M.; De Vijlder, J.J.M.; Muir, E.; Szpirer, C.; !1Islam, M.Q.; van Kessel, A.G.; Lawson, D.E.M.; Vassart, G. !$#journal Genomics (1989) 4:309-319 !$#title The human calbindin 27-kDa gene: structural organization of !1the 5' and 3' regions, chromosomal assignment, and !1restriction fragment length polymorphism. !$#cross-references MUID:89233120; PMID:2565876 !$#accession A30143 !'##molecule_type DNA !'##residues 1-52,201-261 ##label PA2 GENETICS !$#gene GDB:CALB1; CALB !'##cross-references GDB:119744; OMIM:114050 !$#map_position 8p12-8q11.2 !$#introns 26/1; 52/3; 224/3 CLASSIFICATION #superfamily calretinin; calmodulin repeat homology KEYWORDS acetylated amino end; calcium binding; duplication; EF hand; !1vitamin D FEATURE !$2-261 #product calcium-binding protein, vitamin D-dependent !8#status predicted #label MAT\ !$11-43 #domain calmodulin repeat homology #label EF1\ !$53-85 #domain calmodulin repeat homology #label EF2\ !$98-130 #domain calmodulin repeat homology #label EF3\ !$142-174 #domain calmodulin repeat homology #label EF4\ !$186-218 #domain calmodulin repeat homology #label EF5\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status predicted\ !$24,26,28,30,35 #binding_site calcium (Asp, Asp, Ser, Tyr, Glu) !8#status predicted\ !$111,113,115,117,122 #binding_site calcium (Asp, Asp, Ser, Phe, Glu) !8#status predicted\ !$155,157,159,161,166 #binding_site calcium (Asp, Asn, Asp, Lys, Glu) !8#status predicted\ !$199,201,203,205,210 #binding_site calcium (Asp, Asp, Asn, Tyr, Glu) !8#status predicted SUMMARY #length 261 #molecular-weight 30025 #checksum 5336 SEQUENCE /// ENTRY KLRTB #type complete TITLE calcium-binding protein, vitamin D-dependent - rat ALTERNATE_NAMES calbindin D28 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 05-May-2000 ACCESSIONS A30808; A29158; A26374; A40924; I54042; A38396 REFERENCE A30808 !$#authors Gross, M.D.; Kumar, R.; Hunziker, W. !$#journal J. Biol. Chem. (1988) 263:14426-14432 !$#title Expression in Escherichia coli of full-length and mutant rat !1brain calbindin D28. Comparison with the purified native !1protein. !$#cross-references MUID:89008292; PMID:3049577 !$#accession A30808 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-261 ##label GRO !'##note compositional analysis of the native protein indicates that !1Met-1 is removed after translation REFERENCE A29158 !$#authors Yamakuni, T.; Kuwano, R.; Odani, S.; Miki, N.; Yamaguchi, !1K.; Takahashi, Y. !$#journal J. Neurochem. (1987) 48:1590-1596 !$#title Molecular cloning of cDNA to mRNA for a cerebellar spot 35 !1protein. !$#cross-references MUID:87168446; PMID:3031218 !$#accession A29158 !'##molecule_type mRNA !'##residues 1-261 ##label YAM !'##cross-references EMBL:X04280; NID:g57300; PIDN:CAA27828.1; !1PID:g57301 !'##note the authors translated the codon GAG for residues 100 and 163 !1as Gln REFERENCE A26374 !$#authors Yamakuni, T.; Kuwano, R.; Odani, S.; Miki, N.; Yamaguchi, !1Y.; Takahashi, Y. !$#journal Nucleic Acids Res. (1986) 14:6768 !$#title Nucleotide sequence of cDNA to mRNA for a cerebellar !1Ca-binding protein, spot 35 protein. !$#cross-references MUID:86312934; PMID:3755822 !$#accession A26374 !'##molecule_type mRNA !'##residues 1-261 ##label YA2 !'##cross-references EMBL:X04280; NID:g57300; PIDN:CAA27828.1; !1PID:g57301 !'##note the authors translated the codon GAG for residues 100 and 163 !1as Gln REFERENCE A40924 !$#authors Hunziker, W.; Schrickel, S. !$#journal Mol. Endocrinol. (1988) 2:465-473 !$#title Rat brain Calbindin D28: six domain structure and extensive !1amino acid homology with chicken Calbindin D28. !$#cross-references MUID:88334547; PMID:2843757 !$#accession A40924 !'##status preliminary !'##molecule_type mRNA !'##residues 1-261 ##label HUN !'##cross-references GB:M31178; NID:g203234; PIDN:AAA40851.1; !1PID:g203235 !'##experimental_source brain REFERENCE I54042 !$#authors Lomri, N. !$#journal Gene (1989) 80:87-98 !$#title Cloning and analysis of calbindin-d28k cDNA and its !1expression in the central nervous system. !$#cross-references MUID:90006789; PMID:2792772 !$#accession I54042 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-138,'H',140-261 ##label RES !'##cross-references GB:M27839; NID:g203236; PIDN:AAA40852.1; !1PID:g203237 REFERENCE A38396 !$#authors Gabrielides, C.; McCormack, A.L.; Hunt, D.F.; Christakos, S. !$#journal Biochemistry (1991) 30:656-662 !$#title Brain calbindin-D-28k and an M-r 29 000 calcium binding !1protein in cerebellum are different but related proteins: !1evidence obtained from sequence analysis by tandem mass !1spectrometry. !$#cross-references MUID:91105154; PMID:1988053 !$#accession A38396 !'##status preliminary !'##molecule_type protein !'##residues 2-5,'X',7-9,'XX',12-18,'X',20,'X',22-30,'X',32-35,'X', !137-38,'XX',41-42,'XX',45-50,'KX',53,'X',55-72,'X',74,'X', !176-77,'X',79-81,'X',83-88,'XXX',92-93;110-117,'X',119-122, !1'X',124-126,'X',128-129,'XX',132-139;'X',144-148,'X',150, !1'X',152;'X','QX',165-169,'XX',172-177,'XX',180;194-196,'X', !1198-205,'X',207-210,'X',212-213,'XX',216;224-225,'X',227, !1'X',229-230,'X',232-235;237,'X',239-240,'X',242-246,'X', !1248-251,'X',253,'XXX',257-261 ##label GAB CLASSIFICATION #superfamily calretinin; calmodulin repeat homology KEYWORDS acetylated amino end; calcium binding; duplication; EF hand; !1vitamin D FEATURE !$2-261 #product calcium-binding protein, vitamin D-dependent !8#status predicted #label MAT\ !$11-43 #domain calmodulin repeat homology #label EF1\ !$53-85 #domain calmodulin repeat homology #label EF2\ !$98-130 #domain calmodulin repeat homology #label EF3\ !$142-174 #domain calmodulin repeat homology #label EF4\ !$186-218 #domain calmodulin repeat homology #label EF5\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status predicted\ !$24,26,28,30,35 #binding_site calcium (Asp, Asp, Ser, Tyr, Glu) !8#status predicted\ !$111,113,115,117,122 #binding_site calcium (Asp, Asp, Ser, Phe, Glu) !8#status predicted\ !$155,157,159,161,166 #binding_site calcium (Asp, Asn, Asp, Lys, Glu) !8#status predicted\ !$199,201,203,205,210 #binding_site calcium (Asp, Asp, Asn, Tyr, Glu) !8#status predicted SUMMARY #length 261 #molecular-weight 29994 #checksum 5630 SEQUENCE /// ENTRY A34955 #type complete TITLE calcium-binding protein, vitamin D-dependent - mouse ALTERNATE_NAMES calbindin D28 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 05-May-2000 ACCESSIONS A34955; A31851 REFERENCE A92975 !$#authors Nordquist, D.T.; Kozak, C.A.; Orr, H.T. !$#journal J. Neurosci. (1988) 8:4780-4789 !$#title cDNA cloning and characterization of three genes uniquely !1expressed in cerebellum by Purkinje neurons. !$#cross-references MUID:89068131; PMID:3199205 !$#accession A34955 !'##molecule_type mRNA !'##residues 1-261 ##label NOR !'##cross-references GB:M21531; NID:g200247; PIDN:AAA39898.1; !1PID:g200248 !'##experimental_source brain REFERENCE A31851 !$#authors Wood, T.L.; Kobayashi, Y.; Frantz, G.; Varghese, S.; !1Christakos, S.; Tobin, A.J. !$#journal DNA (1988) 7:585-593 !$#title Molecular cloning of mammalian 28,000 M-r vitamin !1D-dependent calcium binding protein (calbindin-D-28K): !1expression of calbindin-D-28K RNAs in rodent brain and !1kidney. !$#cross-references MUID:89152745; PMID:2465881 !$#accession A31851 !'##molecule_type mRNA !'##residues 102-261 ##label WOO !'##cross-references GB:M23663; NID:g575507; PIDN:AAA53198.1; !1PID:g575508 !'##experimental_source brain and kidney GENETICS !$#map_position 4 CLASSIFICATION #superfamily calretinin; calmodulin repeat homology KEYWORDS acetylated amino end; calcium binding; duplication; EF hand; !1vitamin D FEATURE !$2-261 #product calcium-binding protein, vitamin D-dependent !8#status predicted #label MAT\ !$11-43 #domain calmodulin repeat homology #label EF1\ !$53-85 #domain calmodulin repeat homology #label EF2\ !$98-130 #domain calmodulin repeat homology #label EF3\ !$142-174 #domain calmodulin repeat homology #label EF4\ !$186-218 #domain calmodulin repeat homology #label EF5\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status predicted\ !$24,26,28,30,32,35 #binding_site calcium (Asp, Asp, Ser, Tyr, Glu, Glu) !8#status predicted\ !$111,113,115,117, !$119,122 #binding_site calcium (Asp, Asp, Ser, Phe, Glu, Glu) !8#status predicted\ !$155,157,159,161, !$163,166 #binding_site calcium (Asp, Asn, Asp, Lys, Glu, Glu) !8#status predicted\ !$199,201,203,205, !$207,210 #binding_site calcium (Asp, Asp, Asn, Tyr, Asp, Glu) !8#status predicted SUMMARY #length 261 #molecular-weight 29994 #checksum 5631 SEQUENCE /// ENTRY KLBOB #type complete TITLE calcium-binding protein, vitamin D-dependent, brain - bovine ALTERNATE_NAMES avian type CaBP; large CaBP ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 05-May-2000 ACCESSIONS A03071 REFERENCE A03071 !$#authors Takagi, T.; Nojiri, M.; Konishi, K.; Maruyama, K.; Nonomura, !1Y. !$#journal FEBS Lett. (1986) 201:41-45 !$#title Amino acid sequence of vitamin D-dependent calcium-binding !1protein from bovine cerebellum. !$#cross-references MUID:86220795; PMID:3754823 !$#accession A03071 !'##molecule_type protein !'##residues 1-260 ##label TAK !'##experimental_source cerebellum COMMENT Four calcium ions can be bound per molecule. COMMENT The six domains of this protein are thought to derive from !1duplication of an ancestral sequence with two !1calcium-binding domains. Due to changes in sequence, domains !1II and VI (residues 56-84 and 229-258, respectively) no !1longer bind calcium. CLASSIFICATION #superfamily calretinin; calmodulin repeat homology KEYWORDS acetylated amino end; calcium binding; duplication; EF hand; !1vitamin D FEATURE !$10-42 #domain calmodulin repeat homology #label EF1\ !$52-84 #domain calmodulin repeat homology #label EF2\ !$97-129 #domain calmodulin repeat homology #label EF3\ !$141-173 #domain calmodulin repeat homology #label EF4\ !$185-217 #domain calmodulin repeat homology #label EF5\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$23,25,27,29,34 #binding_site calcium (Asp, Asp, Ser, Tyr, Glu) !8#status predicted\ !$110,112,114,116,121 #binding_site calcium (Asp, Asp, Ser, Phe, Glu) !8#status predicted\ !$154,156,158,160,165 #binding_site calcium (Asp, Asn, Asp, Lys, Glu) !8#status predicted\ !$198,200,202,204,209 #binding_site calcium (Asp, Asp, Asp, Tyr, Glu) !8#status predicted SUMMARY #length 260 #molecular-weight 29834 #checksum 4134 SEQUENCE /// ENTRY KLCHI #type complete TITLE calcium-binding protein, vitamin D-dependent - chicken ALTERNATE_NAMES avian type CaBP; calbindin; large CaBP ORGANISM #formal_name Gallus gallus #common_name chicken DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 16-Jun-2000 ACCESSIONS A40926; A93605; A94129; A29957; A94166; A03070; A28026; !1JT0298 REFERENCE A40926 !$#authors Minghetti, P.P.; Cancela, L.; Fujisawa, Y.; Theofan, G.; !1Norman, A.W. !$#journal Mol. Endocrinol. (1988) 2:355-367 !$#title Molecular structure of the chicken vitamin D-induced !1calbindin-D-28K gene reveals eleven exons, six Ca !1(2+)-binding domains, and numerous promoter regulatory !1elements. !$#cross-references MUID:88246474; PMID:2967915 !$#accession A40926 !'##molecule_type DNA !'##residues 1-262 ##label MIN !'##cross-references GB:M31139 REFERENCE A93605 !$#authors Wilson, P.W.; Harding, M.; Lawson, D.E.M. !$#journal Nucleic Acids Res. (1985) 13:8867-8881 !$#title Putative amino acid sequence of chick calcium-binding !1protein deduced from a complementary DNA sequence. !$#cross-references MUID:86093684; PMID:3841205 !$#accession A93605 !'##molecule_type mRNA !'##residues 1-262 ##label WIL !'##cross-references GB:X03343; NID:g63170; PIDN:CAA27049.1; PID:g63171 !'##note the authors translated the codon ACU for residue 70 as Tyr and !1GAU for residues 130, 156, and 160 as Glu REFERENCE A94129 !$#authors Hunziker, W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:7578-7582 !$#title The 28-kDa vitamin D-dependent calcium-binding protein has a !1six-domain structure. !$#cross-references MUID:87016992; PMID:3463988 !$#accession A94129 !'##molecule_type mRNA !'##residues 1-262 ##label HUN !'##cross-references GB:M14230; NID:g211429; PIDN:AAA48659.1; !1PID:g211430 REFERENCE A29957 !$#authors Wilson, P.W.; Rogers, J.; Harding, M.; Pohl, V.; Pattyn, G.; !1Lawson, D.E.M. !$#journal J. Mol. Biol. (1988) 200:615-625 !$#title Structure of chick chromosomal genes for calbindin and !1calretinin. !$#cross-references MUID:88316929; PMID:3411606 !$#accession A29957 !'##molecule_type DNA !'##residues 1-262 ##label WI2 !'##cross-references EMBL:X06629; NID:g63133; PIDN:CAA29843.1; !1PID:g1772927 REFERENCE A94166 !$#authors Fullmer, C.S.; Wasserman, R.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:4772-4776 !$#title Chicken intestinal 28-kilodalton calbindin-D: complete amino !1acid sequence and structural considerations. !$#cross-references MUID:87260872; PMID:3474624 !$#accession A94166 !'##molecule_type protein !'##residues 2-262 ##label FUL COMMENT This protein is involved in vitamin D-stimulated calcium !1absorption from the intestine. Synthesis of CaBP mRNA, in !1the nuclei of mucosal cells, is dependent on the hormonal !1form of vitamin D; without it, synthesis quickly stops. COMMENT Four calcium ions can be bound per molecule. COMMENT The six domains of this protein are thought to derive from !1duplication of an ancestral sequence with two !1calcium-binding domains. Due to changes in sequence, domains !1II and VI (residues 58-86 and 231-260, respectively) no !1longer bind calcium. GENETICS !$#introns 28/1; 53/3; 78/3; 106/3; 125/3; 151/3; 170/2; 183/3; 201/3; !1225/3 CLASSIFICATION #superfamily calretinin; calmodulin repeat homology KEYWORDS blocked amino end; calcium binding; duplication; EF hand; !1vitamin D FEATURE !$2-262 #product calcium-binding protein, vitamin D-dependent !8#status experimental #label MAT\ !$12-44 #domain calmodulin repeat homology #label EF1\ !$54-86 #domain calmodulin repeat homology #label EF2\ !$99-131 #domain calmodulin repeat homology #label EF3\ !$143-175 #domain calmodulin repeat homology #label EF4\ !$187-219 #domain calmodulin repeat homology #label EF5\ !$2 #modified_site blocked amino end (Thr) (in mature !8form) #status experimental\ !$25,27,29,31,36 #binding_site calcium (Asp, Asp, Asn, Tyr, Glu) !8#status predicted\ !$112,114,116,118,123 #binding_site calcium (Asp, Asp, Ser, Phe, Glu) !8#status predicted\ !$156,158,160,162,167 #binding_site calcium (Asp, Asn, Asp, Lys, Glu) !8#status predicted\ !$200,202,204,206,211 #binding_site calcium (Asp, Asp, Asn, Tyr, Glu) !8#status predicted SUMMARY #length 262 #molecular-weight 30167 #checksum 8427 SEQUENCE /// ENTRY S37695 #type complete TITLE calcium-binding protein, vitamin D-dependent - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES calbindin-32 ORGANISM #formal_name Drosophila melanogaster DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 05-May-2000 ACCESSIONS S37695 REFERENCE S37695 !$#authors Reifegerste, R.; Grimm, S.; Albert, S.; Lipski, N.; !1Heimbeck, G.; Hofbauer, A.; Pflugfelder, G.O.; Quack, D.; !1Reichmuth, C.; Schug, B.; Zinsmaier, K.E.; Buchner, S.; !1Buchner, E. !$#journal J. Neurosci. (1993) 13:2186-2198 !$#title An invertebrate calcium-binding protein of the calbindin !1subfamily: protein structure, genomic organization, and !1expression pattern of the calbindin-32 gene of Drosophila. !$#cross-references MUID:93240238; PMID:8478695 !$#accession S37695 !'##molecule_type mRNA !'##residues 1-310 ##label REI !'##cross-references EMBL:X68566; NID:g396506; PIDN:CAA48566.1; !1PID:g396507 GENETICS !$#gene FlyBase:Cbp53E !'##cross-references FlyBase:FBgn0004580 !$#map_position 2 53E CLASSIFICATION #superfamily calretinin; calmodulin repeat homology KEYWORDS calcium binding; duplication; EF hand; vitamin D FEATURE !$35-67 #domain calmodulin repeat homology #label EF1\ !$84-117 #domain calmodulin repeat homology #status atypical !8#label EF2\ !$131-163 #domain calmodulin repeat homology #label EF3\ !$177-209 #domain calmodulin repeat homology #label EF4\ !$224-256 #domain calmodulin repeat homology #label EF5\ !$48,50,52,54,59 #binding_site calcium (Asp, Asp, Asn, Tyr, Glu) !8#status predicted\ !$144,146,148,150,155 #binding_site calcium (Asp, Asp, Ser, Tyr, Glu) !8#status predicted\ !$190,192,194,196,201 #binding_site calcium (Asp, Asn, Asp, Arg, Glu) !8#status predicted\ !$237,239,241,243,248 #binding_site calcium (Asp, Asp, Ser, Thr, Glu) !8#status predicted SUMMARY #length 310 #molecular-weight 35717 #checksum 2039 SEQUENCE /// ENTRY A37414 #type complete TITLE parvalbumin - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A37414 REFERENCE A37414 !$#authors Zuehlke, C.; Schoeffl, F.; Jockusch, H.; Simon, D.; Guenet, !1J.L. !$#journal Genet. Res. (1989) 54:37-43 !$#title cDNA sequence and chromosomal localization of the mouse !1parvalbumin gene, Pva. !$#cross-references MUID:90034167; PMID:2572511 !$#accession A37414 !'##status preliminary !'##molecule_type mRNA !'##residues 1-110 ##label ZUE !'##cross-references GB:X54613; NID:g53818; PIDN:CAA38434.1; PID:g53819 GENETICS !$#introns 7/3; 11/1; 14/2; 16/3; 18/3; 22/3 CLASSIFICATION #superfamily parvalbumin; calmodulin repeat homology KEYWORDS EF hand FEATURE !$39-71 #domain calmodulin repeat homology #label EF1\ !$78-110 #domain calmodulin repeat homology #label EF2 SUMMARY #length 110 #molecular-weight 11944 #checksum 8535 SEQUENCE /// ENTRY PVRTA #type complete TITLE parvalbumin alpha - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 05-Apr-1983 #sequence_revision 30-Jun-1992 #text_change 24-Nov-1999 ACCESSIONS A29308; A24323; A03060; I59015; I79349 REFERENCE A29308 !$#authors Berchtold, M.W.; Epstein, P.; Beaudet, A.L.; Payne, M.E.; !1Heizmann, C.W.; Means, A.R. !$#journal J. Biol. Chem. (1987) 262:8696-8701 !$#title Structural organization and chromosomal assignment of the !1parvalbumin gene. !$#cross-references MUID:87250489; PMID:3036821 !$#accession A29308 !'##molecule_type DNA !'##residues 1-110 ##label BE1 !'##cross-references GB:M15453 REFERENCE A24323 !$#authors Epstein, P.; Means, A.R.; Berchtold, M.W. !$#journal J. Biol. Chem. (1986) 261:5886-5891 !$#title Isolation of a rat parvalbumin gene and full length cDNA. !$#cross-references MUID:86195984; PMID:3009434 !$#accession A24323 !'##molecule_type mRNA !'##residues 1-110 ##label EPS !'##cross-references GB:M12725; NID:g205972; PIDN:AAA41799.1; !1PID:g205973 !'##note the authors' translation of the codons for residues 39-41 is !1inconsistent with the nucleotide sequence and with their !1statement that the sequence confirms the previously !1determined protein sequence REFERENCE A03060 !$#authors Berchtold, M.W.; Heizmann, C.W.; Wilson, K.J. !$#journal Eur. J. Biochem. (1982) 127:381-389 !$#title Primary structure of parvalbumin from rat skeletal muscle. !$#cross-references MUID:83053404; PMID:6754379 !$#accession A03060 !'##molecule_type protein !'##residues 2-110 ##label BE2 REFERENCE I59015 !$#authors Berchtold, M.W.; Means, A.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:1414-1418 !$#title The Ca-2+-binding protein parvalbumin: Molecular cloning and !1developmental regulation of mRNA abundance. !$#cross-references MUID:85140307; PMID:3856270 !$#accession I59015 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 35-55 ##label RES !'##cross-references GB:M10764; NID:g205967; PIDN:AAA41797.1; !1PID:g205970 !'##experimental_source Sprague-Dawley !$#accession I79349 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 84-92 ##label RE2 !'##cross-references GB:M10765; NID:g205968; PIDN:AAA41798.1; !1PID:g554481 GENETICS !$#introns 21/1; 65/2; 102/1 CLASSIFICATION #superfamily parvalbumin; calmodulin repeat homology KEYWORDS blocked amino end; calcium binding; duplication; EF hand; !1muscle FEATURE !$2-110 #product parvalbumin alpha #status experimental !8#label MAT\ !$39-71 #domain calmodulin repeat homology #label EF1\ !$78-110 #domain calmodulin repeat homology #label EF2\ !$2 #modified_site blocked amino end (Ser) (in mature !8form) (probably acetylated) #status experimental\ !$52,54,56,58,60,63 #binding_site calcium (Asp, Asp, Ser, Phe, Glu, Glu) !8#status experimental\ !$91,93,95,97,102 #binding_site calcium (Asp, Asp, Asp, Lys, Glu) !8#status experimental SUMMARY #length 110 #molecular-weight 11925 #checksum 8374 SEQUENCE /// ENTRY PVRB #type complete TITLE parvalbumin alpha - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 01-Sep-1995 ACCESSIONS A93795; A91242; A03059 REFERENCE A93795 !$#authors Enfield, D.L.; Ericsson, L.H.; Blum, H.E.; Fischer, E.H.; !1Neurath, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1975) 72:1309-1313 !$#title Amino-acid sequence of parvalbumin from rabbit skeletal !1muscle. !$#cross-references MUID:75158281; PMID:1055405 !$#accession A93795 !'##molecule_type protein !'##residues 1-109 ##label ENF REFERENCE A91242 !$#authors Capony, J.P.; Pina, C.; Pechere, J.F. !$#journal Eur. J. Biochem. (1976) 70:123-135 !$#title Parvalbumin from rabbit muscle: isolation and primary !1structure. !$#cross-references MUID:77090977; PMID:1009923 !$#accession A91242 !'##molecule_type protein !'##residues 1-109 ##label CAP CLASSIFICATION #superfamily parvalbumin; calmodulin repeat homology KEYWORDS acetylated amino end; calcium binding; duplication; EF hand; !1muscle FEATURE !$38-70 #domain calmodulin repeat homology #label EF1\ !$77-109 #domain calmodulin repeat homology #label EF2\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$51,53,55,57,59,62 #binding_site calcium (Asp, Asp, Ser, Phe, Glu, Glu) !8#status predicted\ !$90,92,94,96,101 #binding_site calcium (Asp, Asp, Asp, Lys, Glu) !8#status predicted SUMMARY #length 109 #molecular-weight 11933 #checksum 4951 SEQUENCE /// ENTRY PVCHA #type complete TITLE parvalbumin alpha - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 22-Jun-1999 ACCESSIONS JT0973; A40297; PT0206; A33180 REFERENCE JT0973 !$#authors Brewer, J.M.; Arnold, J.; Beach, G.G.; Ragland, W.L.; !1Wunderlich, J.K. !$#journal Biochem. Biophys. Res. Commun. (1991) 181:226-231 !$#title Comparison of the amino acid sequences of tissue-specific !1parvalbumins from chicken muscle and thymus and possible !1evolutionary significance. !$#cross-references MUID:92068196; PMID:1958191 !$#accession JT0973 !'##molecule_type protein !'##residues 1-109 ##label BRE REFERENCE A40297 !$#authors Kuster, T.; Staudenmann, W.; Hughes, G.J.; Heizmann, C.W. !$#journal Biochemistry (1991) 30:8812-8816 !$#title Parvalbumin isoforms in chicken muscle and thymus. Amino !1acid sequence analysis of muscle parvalbumin by tandem mass !1spectrometry. !$#cross-references MUID:91363374; PMID:1888741 !$#accession A40297 !'##molecule_type protein !'##residues 1-109 ##label KUS REFERENCE PT0206 !$#authors Palmisano, W.A.; Henzl, M.T. !$#journal Biochem. Biophys. Res. Commun. (1991) 176:328-334 !$#title Avian thymic hormone and chicken (muscle) parvalbumin are !1distinct proteins: isolation of a muscle parvalbumin cDNA !1fragment by PCR. !$#cross-references MUID:91207414; PMID:1708248 !$#accession PT0206 !'##molecule_type mRNA !'##residues 57-60,'D',62-98,'VEK' ##label PAL !'##cross-references GB:M65068; NID:g212534; PIDN:AAA49004.1; !1PID:g212535 !'##experimental_source muscle CLASSIFICATION #superfamily parvalbumin; calmodulin repeat homology KEYWORDS blocked amino end; calcium binding; duplication; EF hand; !1muscle FEATURE !$38-70 #domain calmodulin repeat homology #label EF1\ !$77-109 #domain calmodulin repeat homology #label EF2\ !$1 #modified_site blocked amino end (Ala) (probably !8acetylated) #status experimental\ !$51,53,55,57,59,62 #binding_site calcium (Asp, Asp, Ser, Phe, Glu, Glu) !8#status predicted\ !$90,92,94,96,101 #binding_site calcium (Asp, Asp, Asp, Lys, Glu) !8#status predicted SUMMARY #length 109 #molecular-weight 11941 #checksum 3750 SEQUENCE /// ENTRY PVFGA #type complete TITLE parvalbumin alpha - edible frog ORGANISM #formal_name Rana esculenta #common_name edible frog DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 01-Sep-1995 ACCESSIONS A03062 REFERENCE A03062 !$#authors Jauregui-Adell, J.; Pechere, J.F.; Briand, G.; Richet, C.; !1Demaille, J.G. !$#journal Eur. J. Biochem. (1982) 123:337-345 !$#title Amino-acid sequence of an alpha-parvalbumin, pI=4.88, from !1frog skeletal muscle. !$#cross-references MUID:82186701; PMID:7042341 !$#accession A03062 !'##molecule_type protein !'##residues 1-109 ##label JAU CLASSIFICATION #superfamily parvalbumin; calmodulin repeat homology KEYWORDS calcium binding; duplication; EF hand; muscle FEATURE !$38-70 #domain calmodulin repeat homology #label EF1\ !$77-109 #domain calmodulin repeat homology #label EF2\ !$51,53,55,57,59,62 #binding_site calcium (Asp, Asp, Ser, Phe, Glu, Glu) !8#status predicted\ !$90,92,94,96,101 #binding_site calcium (Asp, Asp, Asp, Lys, Glu) !8#status predicted SUMMARY #length 109 #molecular-weight 11797 #checksum 6973 SEQUENCE /// ENTRY PVNESA #type complete TITLE parvalbumin alpha - two-toed amphiuma (tentative sequence) ORGANISM #formal_name Amphiuma means #common_name two-toed amphiuma DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 31-Mar-2000 ACCESSIONS A03061 REFERENCE A93053 !$#authors Maeda, N.; Zhu, D.; Fitch, W.M. !$#journal Mol. Biol. Evol. (1984) 1:473-488 !$#title Amino acid sequences of lower vertebrate parvalbumins and !1their evolution: parvalbumins of boa, turtle, and !1salamander. !$#cross-references MUID:88174327; PMID:6599978 !$#accession A03061 !'##molecule_type protein !'##residues 1-109 ##label MAE CLASSIFICATION #superfamily parvalbumin; calmodulin repeat homology KEYWORDS calcium binding; duplication; EF hand; muscle FEATURE !$38-70 #domain calmodulin repeat homology #label EF1\ !$77-109 #domain calmodulin repeat homology #label EF2\ !$51,53,55,57,59,62 #binding_site calcium (Asp, Asp, Ser, Tyr, Glu, Glu) !8#status predicted\ !$90,92,94,96,101 #binding_site calcium (Asp, Asp, Asp, Lys, Glu) !8#status predicted SUMMARY #length 109 #molecular-weight 12125 #checksum 5564 SEQUENCE /// ENTRY PVPK #type complete TITLE parvalbumin alpha [validated] - northern pike ALTERNATE_NAMES parvalbumin III; parvalbumin, pI 5.0 ORGANISM #formal_name Esox lucius #common_name northern pike DATE 30-Nov-1980 #sequence_revision 17-Apr-1998 #text_change 15-Sep-2000 ACCESSIONS A67143; A03063; A91397 REFERENCE A67143 !$#authors Declercq, J.P.; Tinant, B.; Roquet, F.; Rambaud, J.; !1Parello, J. !$#submission submitted to the Brookhaven Protein Data Bank, January 1995 !$#cross-references PDB:1PVA !$#contents annotation; X-ray crystallography, 1.65 angstroms !$#accession A67143 !'##molecule_type protein !'##residues 1-109 ##label DEC !'##note authors confirm the acetylated amino terminal sequence Ala-Ala REFERENCE A94570 !$#authors Gerday, C. !$#submission submitted to the Atlas, January 1975 !$#accession A03063 !'##molecule_type protein !'##residues 2-109 ##label GER REFERENCE A91397 !$#authors Frankenne, F.; Joassin, L.; Gerday, C. !$#journal FEBS Lett. (1973) 35:145-147 !$#title The amino acid sequence of the pike (Esox lucius) !1parvalbumin III. !$#cross-references MUID:74028764; PMID:4751989 !$#accession A91397 !'##molecule_type protein !'##residues 2-12,'L',13-27,'A',29-31,'K',33-109 ##label FRA REFERENCE A58792 !$#authors Roepstorff, P.; Klarskov, K.; Andersen, J.; Mann, M.; Vorm, !1O.; Etienne, G.; Parello, J. !$#journal Int. J. Mass Spectrom. Ion Process. (1991) 111:151-172 !$#title Mass spectrometry of proteins: studies of parvalbumins by !1plasma desorption, laser desorption and electrospray mass !1spectrometry. !$#contents annotation; sequence revision !$#note mass spectrometry indicates the amino terminal sequence is !1acetylated Ala-Ala REFERENCE A58797 !$#authors Blancuzzi, Y.; Padilla, A.; Parello, J.; Cave, A. !$#journal Biochemistry (1993) 32:1302-1309 !$#title Symmetrical rearrangement of cation-binding sites of !1parvalbumin upon Ca(2+)/Mg(2+) exchange. A study by (1)H 2D !1NMR. !$#cross-references MUID:93192233; PMID:8095405 !$#contents annotation; conformation by (1)H-NMR REFERENCE A52497 !$#authors Padilla, A.; Cave, A.; Parello, J.; Etienne, G.; Baldellon, !1C. !$#submission submitted to the Brookhaven Protein Data Bank, March 1994 !$#cross-references PDB:3PAT !$#contents annotation; conformation by (1)H-NMR, residues 1-109 REFERENCE A58796 !$#authors Alattia, T.; Padilla, A.; Cave, A. !$#journal Eur. J. Biochem. (1996) 237:561-574 !$#title Assignment of (13)C resonances and analysis of relaxation !1properties and internal dynamics of pike parvalbumin by !1(13)C-NMR at natural abundance. !$#cross-references MUID:96235219; PMID:8647099 !$#contents annotation; conformation by (13)C-NMR !$#note authors confirm the acetylated amino terminal sequence !1Ala-Ala COMMENT This is the major parvalbumin component and has an !1isoelectric point of 5.0. CLASSIFICATION #superfamily parvalbumin; calmodulin repeat homology KEYWORDS acetylated amino end; calcium binding; duplication; EF hand; !1muscle FEATURE !$38-70 #domain calmodulin repeat homology #label EF1\ !$77-109 #domain calmodulin repeat homology #label EF2\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$51,53,55,57,59,62 #binding_site calcium (Asp, Asp, Ser, Phe, Glu, Glu) !8#status experimental\ !$90,92,94,96,101 #binding_site calcium (Asp, Asp, Asp, Lys, Glu) !8#status experimental SUMMARY #length 109 #molecular-weight 11778 #checksum 9961 SEQUENCE /// ENTRY PVLA #type complete TITLE parvalbumin alpha - coelacanth (tentative sequence) ORGANISM #formal_name Latimeria chalumnae #common_name coelacanth DATE 31-May-1979 #sequence_revision 31-May-1979 #text_change 31-Mar-2000 ACCESSIONS A03064 REFERENCE A03064 !$#authors Pechere, J.F.; Rochat, H.; Ferraz, C. !$#journal Biochim. Biophys. Acta (1978) 536:269-274 !$#title Parvalbumins from coelacanth muscle. II. Amino acid sequence !1of the two less acidic components. !$#cross-references MUID:79042275; PMID:30486 !$#accession A03064 !'##molecule_type protein !'##residues 1-111 ##label PEC !'##note the isoelectric point of this parvalbumin is 5.4. Also present !1is another parvalbumin having an isoelectric point of 5.0 !1and an identical sequence except that the amino end is !1blocked CLASSIFICATION #superfamily parvalbumin; calmodulin repeat homology KEYWORDS blocked amino end; calcium binding; duplication; EF hand; !1muscle FEATURE !$40-72 #domain calmodulin repeat homology #label EF1\ !$79-110 #domain calmodulin repeat homology #label EF2\ !$1 #modified_site blocked amino end (Thr) (partial) !8(probably acetylated) #status experimental\ !$53,55,57,59,61,64 #binding_site calcium (Asp, Asp, Ser, Tyr, Glu, Glu) !8#status predicted\ !$92,94,96,98,103 #binding_site calcium (Asp, Asp, Asp, Lys, Glu) !8#status predicted SUMMARY #length 111 #molecular-weight 12208 #checksum 1358 SEQUENCE /// ENTRY PVSNBB #type complete TITLE parvalbumin beta - boa (tentative sequence) ORGANISM #formal_name Boa constrictor #common_name boa DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 31-Mar-2000 ACCESSIONS A03050 REFERENCE A93053 !$#authors Maeda, N.; Zhu, D.; Fitch, W.M. !$#journal Mol. Biol. Evol. (1984) 1:473-488 !$#title Amino acid sequences of lower vertebrate parvalbumins and !1their evolution: parvalbumins of boa, turtle, and !1salamander. !$#cross-references MUID:88174327; PMID:6599978 !$#accession A03050 !'##molecule_type protein !'##residues 1-109 ##label MAE CLASSIFICATION #superfamily parvalbumin; calmodulin repeat homology KEYWORDS calcium binding; duplication; EF hand; muscle FEATURE !$38-70 #domain calmodulin repeat homology #label EF1\ !$77-109 #domain calmodulin repeat homology #label EF2\ !$51,53,55,57,59,62 #binding_site calcium (Asp, Asp, Ser, Tyr, Glu, Glu) !8#status predicted\ !$90,92,94,96,101 #binding_site calcium (Asp, Asp, Asp, Lys, Glu) !8#status predicted SUMMARY #length 109 #molecular-weight 11804 #checksum 7828 SEQUENCE /// ENTRY PVTTMB #type complete TITLE parvalbumin beta - map turtle ORGANISM #formal_name Graptemys geographica #common_name map turtle DATE 28-May-1986 #sequence_revision 30-Jun-1989 #text_change 01-Sep-1995 ACCESSIONS A03049 REFERENCE A93053 !$#authors Maeda, N.; Zhu, D.; Fitch, W.M. !$#journal Mol. Biol. Evol. (1984) 1:473-488 !$#title Amino acid sequences of lower vertebrate parvalbumins and !1their evolution: parvalbumins of boa, turtle, and !1salamander. !$#cross-references MUID:88174327; PMID:6599978 !$#accession A03049 !'##molecule_type protein !'##residues 1-108 ##label MAE !'##note tryptic peptides were positioned by homology CLASSIFICATION #superfamily parvalbumin; calmodulin repeat homology KEYWORDS calcium binding; duplication; EF hand; muscle FEATURE !$38-70 #domain calmodulin repeat homology #label EF1\ !$77-108 #domain calmodulin repeat homology #label EF2\ !$51,53,55,57,59,62 #binding_site calcium (Asp, Asp, Ser, Phe, Glu, Glu) !8#status predicted\ !$90,92,94,96,101 #binding_site calcium (Asp, Asp, Asp, Lys, Glu) !8#status predicted SUMMARY #length 108 #molecular-weight 11583 #checksum 955 SEQUENCE /// ENTRY PVNESB #type complete TITLE parvalbumin beta - two-toed amphiuma (tentative sequence) ORGANISM #formal_name Amphiuma means #common_name two-toed amphiuma DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 31-Mar-2000 ACCESSIONS A03051 REFERENCE A93053 !$#authors Maeda, N.; Zhu, D.; Fitch, W.M. !$#journal Mol. Biol. Evol. (1984) 1:473-488 !$#title Amino acid sequences of lower vertebrate parvalbumins and !1their evolution: parvalbumins of boa, turtle, and !1salamander. !$#cross-references MUID:88174327; PMID:6599978 !$#accession A03051 !'##molecule_type protein !'##residues 1-108 ##label MAE CLASSIFICATION #superfamily parvalbumin; calmodulin repeat homology KEYWORDS calcium binding; duplication; EF hand; muscle FEATURE !$38-70 #domain calmodulin repeat homology #label EF1\ !$77-108 #domain calmodulin repeat homology #label EF2\ !$51,53,55,57,59,62 #binding_site calcium (Asp, Asp, Ser, Tyr, Glu, Glu) !8#status predicted\ !$90,92,94,96,101 #binding_site calcium (Asp, Asp, Asp, Lys, Glu) !8#status predicted SUMMARY #length 108 #molecular-weight 11741 #checksum 3329 SEQUENCE /// ENTRY PVFG #type complete TITLE parvalbumin beta - edible frog ORGANISM #formal_name Rana esculenta #common_name edible frog DATE 30-Nov-1980 #sequence_revision 30-Nov-1980 #text_change 24-Nov-1999 ACCESSIONS A03052 REFERENCE A03052 !$#authors Capony, J.P.; Demaille, J.; Pina, C.; Pechere, J.F. !$#journal Eur. J. Biochem. (1975) 56:215-227 !$#title The amino-acid sequence of the most acidic major parvalbumin !1from frog muscle. !$#cross-references MUID:76022442; PMID:1080707 !$#accession A03052 !'##molecule_type protein !'##residues 1-108 ##label CAP !'##note the isoelectric point of this protein is 4.5 CLASSIFICATION #superfamily parvalbumin; calmodulin repeat homology KEYWORDS blocked amino end; calcium binding; duplication; EF hand; !1muscle FEATURE !$38-70 #domain calmodulin repeat homology #label EF1\ !$77-108 #domain calmodulin repeat homology #label EF2\ !$1 #modified_site blocked amino end (Ser) (probably !8acetylated) #status experimental\ !$51,53,55,57,59,62 #binding_site calcium (Asp, Asp, Ser, Phe, Glu, Glu) !8#status predicted\ !$90,92,94,96,101 #binding_site calcium (Asp, Asp, Asp, Lys, Glu) !8#status predicted SUMMARY #length 108 #molecular-weight 11581 #checksum 9217 SEQUENCE /// ENTRY PVXLB #type complete TITLE parvalbumin beta - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 01-Sep-1995 ACCESSIONS A27273 REFERENCE A27273 !$#authors Kay, B.K.; Shah, A.J.; Halstead, W.E. !$#journal J. Cell Biol. (1987) 104:841-847 !$#title Expression of the Ca2+-binding protein, parvalbumin, during !1embryonic development of the frog, Xenopus laevis. !$#cross-references MUID:87166182; PMID:3558484 !$#accession A27273 !'##molecule_type mRNA !'##residues 1-109 ##label KAY !'##cross-references GB:M28644 !'##experimental_source tadpole CLASSIFICATION #superfamily parvalbumin; calmodulin repeat homology KEYWORDS calcium binding; duplication; EF hand; muscle FEATURE !$2-109 #product parvalbumin beta #status predicted #label !8MAT\ !$39-71 #domain calmodulin repeat homology #label EF1\ !$78-109 #domain calmodulin repeat homology #label EF2\ !$52,54,56,58,60,63 #binding_site calcium (Asp, Asp, Ser, Phe, Glu, Glu) !8#status predicted\ !$91,93,95,97,102 #binding_site calcium (Asp, Asp, Asp, Lys, Glu) !8#status predicted SUMMARY #length 109 #molecular-weight 11623 #checksum 5590 SEQUENCE /// ENTRY PVTFB3 #type complete TITLE parvalbumin beta IIIf - oyster toadfish ORGANISM #formal_name Opsanus tau #common_name oyster toadfish DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 11-May-2000 ACCESSIONS JL0094 REFERENCE JL0094 !$#authors Gerday, C.; Collin, S.; Gerardin-Otthiers, N. !$#journal Comp. Biochem. Physiol. B (1989) 93:49-55 !$#title The amino acid sequence of the parvalbumin from the very !1fast swimbladder muscle of the toadfish (Opsanus tau). !$#cross-references MUID:89324657; PMID:2752733 !$#accession JL0094 !'##molecule_type protein !'##residues 1-109 ##label GER !'##note three parvalbumin isotypes, in nearly equal proportions, are !1found in toadfish white trunk muscle whereas only one main !1component (IIIf) is present in the swimbladder muscle of !1adult specimens CLASSIFICATION #superfamily parvalbumin; calmodulin repeat homology KEYWORDS acetylated amino end; calcium binding; duplication; EF hand; !1muscle FEATURE !$38-70 #domain calmodulin repeat homology #label EF1\ !$77-109 #domain calmodulin repeat homology #label EF2\ !$1 #modified_site acetylated amino end (Ser) #status !8experimental\ !$51,53,55,57,59,62 #binding_site calcium (Asp, Asp, Ser, Phe, Glu, Glu) !8#status predicted\ !$90,92,94,96,101 #binding_site calcium (Asp, Asp, Asp, Lys, Glu) !8#status predicted SUMMARY #length 109 #molecular-weight 11757 #checksum 2383 SEQUENCE /// ENTRY PVCAB #type complete TITLE parvalbumin beta [validated] - common carp ALTERNATE_NAMES muscle calcium-binding protein B ORGANISM #formal_name Cyprinus carpio #common_name common carp DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 15-Sep-2000 ACCESSIONS A92133; A03053 REFERENCE A92133 !$#authors Coffee, C.J.; Bradshaw, R.A. !$#journal J. Biol. Chem. (1973) 248:3305-3312 !$#title Carp muscle calcium-binding protein. I. Characterization of !1the tryptic peptides and the complete amino acid sequence of !1component B. !$#accession A92133 !'##molecule_type protein !'##residues 1-24,'D',26-108 ##label CO1 !'##note peptides were positioned with the aid of X-ray crystallographic !1data and by homology REFERENCE A92140 !$#authors Coffee, C.J.; Bradshaw, R.A. !$#journal J. Biol. Chem. (1973) 248:6576 !$#contents erratum !$#accession A03053 !'##molecule_type protein !'##residues 1-108 ##label CO2 REFERENCE A93407 !$#authors Kretsinger, R.H. !$#journal Nature New Biol. (1972) 240:85-88 !$#title Gene triplication deduced from the tertiary structure of a !1muscle calcium binding protein. !$#cross-references MUID:73046848; PMID:4508374 !$#contents annotation REFERENCE A92134 !$#authors Kretsinger, R.H.; Nockolds, C.E. !$#journal J. Biol. Chem. (1973) 248:3313-3326 !$#title Carp muscle calcium-binding protein. II. Structure !1determination and general description. !$#cross-references MUID:73166580; PMID:4700463 !$#contents annotation; X-ray crystallography, 1.85 angstroms REFERENCE A50652 !$#authors Kumar, V.D.; Lee, L.; Edwards, B.F.P. !$#submission submitted to the Brookhaven Protein Data Bank, October 1989 !$#cross-references PDB:4CPV !$#contents annotation; X-ray crystallography, 1.5 angstroms, residues !11-108 REFERENCE A34545 !$#authors Kumar, V.D.; Lee, L.; Edwards, B.F.P. !$#journal Biochemistry (1990) 29:1404-1412 !$#title Refined crystal structure of calcium-liganded carp !1parvalbumin 4.25 at 1.5-angstrom resolution. !$#cross-references MUID:90241934; PMID:2334704 !$#contents annotation; X-ray crystallography, 1.5 angstroms REFERENCE A50711 !$#authors Swain, A.L.; Kretsinger, R.H.; Amma, E.L. !$#submission submitted to the Brookhaven Protein Data Bank, January 1990 !$#cross-references PDB:5CPV !$#contents annotation; X-ray crystallography, 1.6 angstroms, residues !11-108 REFERENCE A34395 !$#authors Swain, A.L.; Kretsinger, R.H.; Amma, E.L. !$#journal J. Biol. Chem. (1989) 264:16620-16628 !$#title Restrained least squares refinement of native (calcium) and !1cadmium-substituted carp parvalbumin usine X-ray !1crystallographic data at 1.6-angstrom resolution. !$#cross-references MUID:89380285; PMID:2777802 !$#contents annotation; X-ray crystallography, 1.6 angstroms CLASSIFICATION #superfamily parvalbumin; calmodulin repeat homology KEYWORDS acetylated amino end; calcium binding; duplication; EF hand; !1muscle FEATURE !$38-70 #domain calmodulin repeat homology #label EF1\ !$77-108 #domain calmodulin repeat homology #label EF2\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$51,53,55,57,59,62 #binding_site calcium (Asp, Asp, Ser, Phe, Glu, Glu) !8#status experimental\ !$90,92,94,96,101 #binding_site calcium (Asp, Asp, Asp, Lys, Glu) !8#status experimental SUMMARY #length 108 #molecular-weight 11436 #checksum 7716 SEQUENCE /// ENTRY PVPK2 #type complete TITLE parvalbumin beta [validated] - northern pike ALTERNATE_NAMES parvalbumin II; parvalbumin, pI 4.1 ORGANISM #formal_name Esox lucius #common_name northern pike DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 15-Sep-2000 ACCESSIONS A03054 REFERENCE A03054 !$#authors Gerday, C. !$#journal Eur. J. Biochem. (1976) 70:305-318 !$#title The primary structure of the parvalbumin II of pike (Esox !1lucius). !$#cross-references MUID:77090998; PMID:1009932 !$#accession A03054 !'##molecule_type protein !'##residues 1-107 ##label GER REFERENCE A50616 !$#authors Declercq, J.P.; Tinant, B.; Parello, J.; Rambaud, J. !$#submission submitted to the Brookhaven Protein Data Bank, November 1990 !$#cross-references PDB:3PAL !$#contents annotation; X-ray crystallography, 2.4 angstroms, residues !11-107 REFERENCE A58798 !$#authors Declercq, J.P.; Tinant, B.; Parello, J.; Rambaud, J. !$#journal J. Mol. Biol. (1991) 220:1017-1039 !$#title Ionic interactions with parvalbumins. Crystal structure !1determination of pike 4.10 parvalbumin in four different !1ionic environments. !$#cross-references MUID:91350177; PMID:1880797 !$#contents annotation; X-ray crystallography, 1.65 angstroms REFERENCE A67144 !$#authors Declercq, J.P.; Tinant, B.; Parello, J. !$#submission submitted to the Brookhaven Protein Data Bank, January 1995 !$#cross-references PDB:1PVB !$#contents annotation; X-ray crystallography, 1.75 angstroms, residues !11-107 COMMENT This is the minor parvalbumin component and has an !1isoelectric point of 4.1. CLASSIFICATION #superfamily parvalbumin; calmodulin repeat homology KEYWORDS acetylated amino end; calcium binding; duplication; EF hand; !1muscle FEATURE !$37-69 #domain calmodulin repeat homology #label EF1\ !$76-107 #domain calmodulin repeat homology #label EF2\ !$1 #modified_site acetylated amino end (Ser) #status !8experimental\ !$50,52,54,56,58,61 #binding_site calcium (Asp, Asp, Ser, Phe, Glu, Glu) !8#status experimental\ !$89,91,93,95,100 #binding_site calcium (Asp, Asp, Asp, Met, Glu) !8#status experimental SUMMARY #length 107 #molecular-weight 11390 #checksum 3823 SEQUENCE /// ENTRY PVHK #type complete TITLE parvalbumin beta - European hake ORGANISM #formal_name Merluccius merluccius #common_name European hake DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 01-Sep-1995 ACCESSIONS A03055 REFERENCE A03055 !$#authors Capony, J.P.; Ryden, L.; Demaille, J.; Pechere, J.F. !$#journal Eur. J. Biochem. (1973) 32:97-108 !$#title The primary structure of the major parvalbumin from hake !1muscle: overlapping peptides obtained with chemical and !1enzymatic methods. The complete amino acid sequence. !$#cross-references MUID:73121411; PMID:4569071 !$#accession A03055 !'##molecule_type protein !'##residues 1-108 ##label CAP !'##note this is the major parvalbumin, having an isoelectric point of !14.36 CLASSIFICATION #superfamily parvalbumin; calmodulin repeat homology KEYWORDS acetylated amino end; calcium binding; duplication; EF hand; !1muscle FEATURE !$38-70 #domain calmodulin repeat homology #label EF1\ !$77-108 #domain calmodulin repeat homology #label EF2\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$51,53,55,57,59,62 #binding_site calcium (Asp, Asp, Ser, Phe, Glu, Glu) !8#status predicted\ !$90,92,94,96,101 #binding_site calcium (Asp, Asp, Asp, Lys, Glu) !8#status predicted SUMMARY #length 108 #molecular-weight 11295 #checksum 6897 SEQUENCE /// ENTRY PVWI #type complete TITLE parvalbumin beta - whiting ORGANISM #formal_name Merlangius merlangus #common_name whiting DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 11-May-2000 ACCESSIONS A03056 REFERENCE A03056 !$#authors Joassin, L.; Gerday, C. !$#journal Comp. Biochem. Physiol. B (1977) 57:159-161 !$#title The amino acid sequence of the major parvalbumin of the !1whiting (Gadus merlangus). !$#cross-references MUID:89337603; PMID:318435 !$#accession A03056 !'##molecule_type protein !'##residues 1-108 ##label JOA CLASSIFICATION #superfamily parvalbumin; calmodulin repeat homology KEYWORDS acetylated amino end; calcium binding; duplication; EF hand; !1muscle FEATURE !$38-70 #domain calmodulin repeat homology #label EF1\ !$77-108 #domain calmodulin repeat homology #label EF2\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$51,53,55,57,59,62 #binding_site calcium (Asp, Asp, Ser, Phe, Glu, Glu) !8#status predicted\ !$90,92,94,96,101 #binding_site calcium (Asp, Asp, Asp, Ala, Glu) !8#status predicted SUMMARY #length 108 #molecular-weight 11323 #checksum 7393 SEQUENCE /// ENTRY PVCD #type complete TITLE parvalbumin beta - Baltic cod (tentative sequence) ALTERNATE_NAMES allergen M ORGANISM #formal_name Gadus morhua callarias #common_name Baltic cod DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 31-Mar-2000 ACCESSIONS A94236; A94235; A03057 REFERENCE A94236 !$#authors Elsayed, S.; Bennich, H. !$#journal Scand. J. Immunol. (1975) 4:203-208 !$#title The primary structure of allergen M from cod. !$#cross-references MUID:75198151; PMID:1145128 !$#accession A94236 !'##molecule_type protein !'##residues 1-75 ##label EL1 !'##note the protein contains covalently bound glucose, possibly at !118-Cys !'##note this protein is allergenic and is called allergen M by these !1authors REFERENCE A94235 !$#authors Elsayed, S.; von Bahr-Lindstrom, H.; Bennich, H. !$#journal Scand. J. Immunol. (1974) 3:683-686 !$#cross-references MUID:75031395; PMID:4423465 !$#accession A94235 !'##molecule_type protein !'##residues 76-113 ##label EL2 CLASSIFICATION #superfamily parvalbumin; calmodulin repeat homology KEYWORDS acetylated amino end; calcium binding; duplication; EF hand; !1glycoprotein; muscle FEATURE !$38-70 #domain calmodulin repeat homology #label EF1\ !$77-109 #domain calmodulin repeat homology #label EF2\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$18 #binding_site carbohydrate (Cys) (covalent) #status !8predicted\ !$51,53,55,57,59,62 #binding_site calcium (Asp, Asp, Glu, Phe, Glu, Glu) !8#status predicted\ !$90,92,94,96,101 #binding_site calcium (Asp, Asp, Asp, Lys, Glu) !8#status predicted SUMMARY #length 113 #molecular-weight 12107 #checksum 4207 SEQUENCE /// ENTRY PVLAB #type complete TITLE parvalbumin beta - coelacanth (tentative sequence) ORGANISM #formal_name Latimeria chalumnae #common_name coelacanth DATE 30-Apr-1979 #sequence_revision 30-Apr-1979 #text_change 31-Mar-2000 ACCESSIONS A03058 REFERENCE A03058 !$#authors Jauregui-Adell, J.; Pechere, J.F. !$#journal Biochim. Biophys. Acta (1978) 536:275-282 !$#title Parvalbumins from coelacanth muscle. III. Amino acid !1sequence of the major component. !$#cross-references MUID:79042277; PMID:708767 !$#accession A03058 !'##molecule_type protein !'##residues 1-108 ##label JAU !'##note this is the predominant parvalbumin in latimeria muscle CLASSIFICATION #superfamily parvalbumin; calmodulin repeat homology KEYWORDS acetylated amino end; calcium binding; duplication; EF hand; !1muscle FEATURE !$38-70 #domain calmodulin repeat homology #label EF1\ !$77-108 #domain calmodulin repeat homology #label EF2\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$51,53,55,57,59,62 #binding_site calcium (Asp, Asp, Ser, Phe, Glu, Glu) !8#status predicted\ !$90,92,94,96,101 #binding_site calcium (Asp, Asp, Asp, Lys, Glu) !8#status predicted SUMMARY #length 108 #molecular-weight 11732 #checksum 9739 SEQUENCE /// ENTRY PVRYC #type complete TITLE parvalbumin - thornback ray (tentative sequence) ORGANISM #formal_name Raja clavata #common_name thornback ray DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 31-Mar-2000 ACCESSIONS A03065 REFERENCE A03065 !$#authors Thatcher, D.R.; Pechere, J.F. !$#journal Eur. J. Biochem. (1977) 75:121-132 !$#title The amino-acid sequence of the major parvalbumin from !1thornback-ray muscle. !$#cross-references MUID:77184993; PMID:862613 !$#accession A03065 !'##molecule_type protein !'##residues 1-109 ##label THA CLASSIFICATION #superfamily parvalbumin; calmodulin repeat homology KEYWORDS acetylated amino end; calcium binding; EF hand FEATURE !$38-70 #domain calmodulin repeat homology #label EF1\ !$77-108 #domain calmodulin repeat homology #label EF2\ !$1 #modified_site acetylated amino end (Ser) #status !8experimental SUMMARY #length 109 #molecular-weight 11779 #checksum 4245 SEQUENCE /// ENTRY PVHUO #type complete TITLE oncomodulin - human ALTERNATE_NAMES parvalbumin beta ORGANISM #formal_name Homo sapiens #common_name man DATE 19-May-1994 #sequence_revision 11-Nov-1994 #text_change 07-May-1999 ACCESSIONS S35041 REFERENCE S35041 !$#authors Foehr, U.G.; Weber, B.R.; Muentener, M.; Staudenmann, W.; !1Hughes, G.J.; Frutiger, S.; Banville, D.; Schaefer, B.W.; !1Heizmann, C.W. !$#journal Eur. J. Biochem. (1993) 215:719-727 !$#title Human alpha and beta parvalbumins. Structure and !1tissue-specific expression. !$#cross-references MUID:93358895; PMID:8354278 !$#accession S35041 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 2-109 ##label FOE !'##cross-references GB:L20345 !'##note initiator Met not shown COMMENT Oncomodulin is an acidic calcium-binding protein found in !1placenta and tumor tissues and not detected in normal adult !1tissues. It can activate phosphodiesterase and calcineurin !1and inhibit glutathione reductase. Its function is not !1understood. GENETICS !$#gene GDB:OCM !'##cross-references GDB:132239; OMIM:164795 !$#map_position 7p13-7p11 CLASSIFICATION #superfamily parvalbumin; calmodulin repeat homology KEYWORDS acetylated amino end; calcium binding; duplication; EF hand; !1placenta; tumor FEATURE !$2-109 #product oncomodulin #status predicted #label MAT\ !$39-71 #domain calmodulin repeat homology #label EF1\ !$78-109 #domain calmodulin repeat homology #label EF2\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status predicted\ !$52,54,56,58,63 #binding_site calcium (Asp, Asp, Ser, Tyr, Glu) !8#status predicted\ !$91,93,95,97,102 #binding_site calcium (Asp, Asp, Asp, Lys, Glu) !8#status predicted SUMMARY #length 109 #molecular-weight 12156 #checksum 6078 SEQUENCE /// ENTRY PVRTO #type complete TITLE oncomodulin [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 03-Aug-1984 #sequence_revision 30-Jun-1992 #text_change 15-Sep-2000 ACCESSIONS S04616; A29547; A03066 REFERENCE S04616 !$#authors Banville, D.; Boie, Y. !$#journal J. Mol. Biol. (1989) 207:481-490 !$#title Retroviral long terminal repeat is the promoter of the gene !1encoding the tumor-associated calcium-binding protein !1oncomodulin in the rat. !$#cross-references MUID:89342434; PMID:2474657 !$#accession S04616 !'##molecule_type DNA !'##residues 1-109 ##label BAN !'##cross-references EMBL:X15836; NID:g56794; PIDN:CAA33840.1; !1PID:g1289279 REFERENCE A29547 !$#authors Gillen, M.F.; Banville, D.; Rutledge, R.G.; Narang, S.; !1Seligy, V.L.; Whitfield, J.F.; MacManus, J.P. !$#journal J. Biol. Chem. (1987) 262:5308-5312 !$#title A complete complementary DNA for the oncodevelopmental !1calcium-binding protein, oncomodulin. !$#cross-references MUID:87165971; PMID:3558395 !$#accession A29547 !'##molecule_type mRNA !'##residues 1-109 ##label GIL !'##cross-references GB:J02705; NID:g205847; PIDN:AAA41756.1; !1PID:g205848 REFERENCE A03066 !$#authors MacManus, J.P.; Watson, D.C.; Yaguchi, M. !$#journal Eur. J. Biochem. (1983) 136:9-17 !$#title The complete amino acid sequence of oncomodulin--a !1parvalbumin-like calcium-binding protein from Morris !1hepatoma 5123tc. !$#cross-references MUID:84004413; PMID:6617664 !$#accession A03066 !'##molecule_type protein !'##residues 2-25,'Q',27-109 ##label MAC REFERENCE A50293 !$#authors Ahmed, F.R.; Przybylska, M.; Rose, D.R.; Birnbaum, G.I.; !1Pippy, M.E.; MacManus, J.P. !$#submission submitted to the Brookhaven Protein Data Bank, April 1990 !$#cross-references PDB:1OMD !$#contents annotation; X-ray crystallography, 1.85 angstroms, residues !13-109 REFERENCE A37304 !$#authors Ahmed, F.R.; Przybylska, M.; Rose, D.R.; Birnbaum, G.I.; !1Pippy, M.E.; MacManus, J.P. !$#journal J. Mol. Biol. (1990) 216:127-140 !$#title Structure of oncomodulin refined at 1.85 angstroms !1resolution: an example of extensive molecular aggregation !1via Ca2+. !$#cross-references MUID:91039328; PMID:2231727 !$#contents annotation; X-ray crystallography, 1.85 angstroms !$#note in the crystal structure, a third calcium ion is bound by !1Gln-72 and Asp-74 of one molecule, Gln-55 of another, and !1Glu-80 of a third COMMENT Oncomodulin is an acidic calcium-binding protein found in !1placenta and tumor tissues and not detected in normal adult !1tissues. It can activate phosphodiesterase and calcineurin !1and inhibit glutathione reductase. Its function is not !1understood. GENETICS !$#introns 21/1; 65/2; 102/1 CLASSIFICATION #superfamily parvalbumin; calmodulin repeat homology KEYWORDS acetylated amino end; calcium binding; duplication; EF hand; !1placenta; tumor FEATURE !$2-109 #product oncomodulin #status experimental #label MAT\ !$39-71 #domain calmodulin repeat homology #label EF1\ !$78-109 #domain calmodulin repeat homology #label EF2\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental\ !$52,54,56,58,63 #binding_site calcium (Asp, Asp, Ser, Tyr, Glu) !8#status experimental\ !$91,93,95,97,102 #binding_site calcium (Asp, Asp, Asp, Lys, Glu) !8#status experimental SUMMARY #length 109 #molecular-weight 12188 #checksum 5961 SEQUENCE /// ENTRY BCHUIA #type complete TITLE S-100 protein alpha chain - human ALTERNATE_NAMES S-100 calcium-binding protein A1 (S100A1) ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1993 #sequence_revision 23-May-1997 #text_change 22-Jun-1999 ACCESSIONS A44470; S16740 REFERENCE A44470 !$#authors Engelkamp, D.; Schafer, B.W.; Erne, P.; Heizmann, C.W. !$#journal Biochemistry (1992) 31:10258-10264 !$#title S100 alpha, CAPL, and CACY: molecular cloning and expression !1analysis of three calcium-binding proteins from human heart. !$#cross-references MUID:93041710; PMID:1384693 !$#accession A44470 !'##molecule_type mRNA !'##residues 1-94 ##label ENG !'##cross-references EMBL:X58079; NID:g36175; PIDN:CAA41107.1; !1PID:g36176 !'##experimental_source heart !'##note sequence extracted from NCBI backbone (NCBIP:116494) COMMENT This protein binds p53, tubulin and many other proteins at !1physiological concentrations of calcium and modulates their !1phosphorylation by protein kinase. COMMENT S-100 is an intracellular protein that binds calcium. It !1binds zinc more tightly, however, and this appears to !1increase the affinity of the protein for calcium. Distinct !1binding sites with different affinities exist for both ions !1on each monomer. Physiological concentrations of potassium !1ion antagonize the binding of both divalent cations, !1especially affecting high-affinity calcium-binding sites. COMMENT Although predominant among the water-soluble brain proteins, !1S-100 is also found in a variety of other tissues. GENETICS !$#gene GDB:S100A1; S100A !'##cross-references GDB:126839; OMIM:176940 !$#map_position 1q21-1q21 COMPLEX homodimer; heterodimer with S-100 protein beta chain (see !1PIR:BCHUIB) CLASSIFICATION #superfamily S-100 protein; calmodulin repeat homology KEYWORDS brain; calcium binding; EF hand; heterodimer; homodimer; !1zinc FEATURE !$7-41 #domain calmodulin repeat homology #label EF1\ !$50-82 #domain calmodulin repeat homology #label EF2 SUMMARY #length 94 #molecular-weight 10546 #checksum 6574 SEQUENCE /// ENTRY BCBOIA #type complete TITLE S-100 protein alpha chain - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 14-Nov-1983 #sequence_revision 06-Feb-1995 #text_change 24-Nov-1999 ACCESSIONS A24156; A91110; S54346; A03078 REFERENCE A24156 !$#authors Kuwano, R.; Maeda, T.; Usui, H.; Araki, K.; Yamakuni, T.; !1Ohshima, Y.; Kurihara, T.; Takahashi, Y. !$#journal FEBS Lett. (1986) 202:97-101 !$#title Molecular cloning of cDNA of S100alpha subunit mRNA. !$#cross-references MUID:86248083; PMID:3755105 !$#accession A24156 !'##molecule_type mRNA !'##residues 1-94 ##label KUW REFERENCE A91110 !$#authors Isobe, T.; Okuyama, T. !$#journal Eur. J. Biochem. (1981) 116:79-86 !$#title The amino-acid sequence of the alpha subunit in bovine brain !1S-100 a protein. !$#cross-references MUID:81236562; PMID:7250124 !$#accession A91110 !'##molecule_type protein !'##residues 2-64,'D',66-94 ##label ISO REFERENCE A90471 !$#authors Baudier, J.; Gerard, D. !$#journal Biochemistry (1983) 22:3360-3369 !$#title Ions binding to S100 proteins: structural changes induced by !1calcium and zinc on S100a and S100b proteins. !$#cross-references MUID:84000339; PMID:6615778 !$#contents annotation; metal ion-binding properties REFERENCE S54343 !$#authors Okazaki, K.; Obata, N.H.; Inoue, S.; Hidaka, H. !$#journal Biochem. J. (1995) 306:551-555 !$#title S100-beta is a target protein of neurocalcin delta, an !1abundant isoform in glial cells. !$#cross-references MUID:95194333; PMID:7887910 !$#accession S54346 !'##molecule_type protein !'##residues 24-33 ##label OKA COMMENT The S-100 protein is composed of two related polypeptide !1chains, alpha and beta, that form dimers, S-100a !1(alpha-beta) and S-100b (beta-beta). Although predominant !1among the water-soluble brain proteins, S-100 is also found !1in a variety of other tissues. COMMENT S-100 is an intracellular protein that weakly binds calcium. !1It binds zinc very tightly, however, and this appears to !1increase the affinity of the protein for calcium. Distinct !1binding sites, with different affinities, exist for both !1ions on each monomer. Physiological concentrations of !1potassium ion antagonize the binding of both divalent !1cations, especially affecting high-affinity calcium-binding !1sites. CLASSIFICATION #superfamily S-100 protein; calmodulin repeat homology KEYWORDS blocked amino end; brain; calcium binding; EF hand; zinc FEATURE !$2-94 #product S-100 protein alpha chain #status predicted !8#label MAT\ !$7-41 #domain calmodulin repeat homology #label EF1\ !$50-82 #domain calmodulin repeat homology #label EF2\ !$2 #modified_site blocked amino end (Gly) (in mature !8form) (probably acetylated) #status experimental\ !$20,23,25,28,33 #binding_site calcium (Ser, Glu, Asp, Lys, Glu) !8#status predicted\ !$63,65,67,69,74 #binding_site calcium (Asp, Asn, Asp, Glu, Glu) !8#status predicted SUMMARY #length 94 #molecular-weight 10518 #checksum 5482 SEQUENCE /// ENTRY S35985 #type complete TITLE S-100 protein alpha chain - weatherfish ORGANISM #formal_name Misgurnus fossilis #common_name weatherfish DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S35985 REFERENCE S35985 !$#authors Ivanenkov, V.V.; Gerke, V.; Minin, A.A.; Plessmann, U.; !1Weber, K. !$#journal Mech. Dev. (1993) 42:151-158 !$#title Transduction of Ca(2+) signals upon fertilization of eggs; !1identification of an S-100 protein as a major Ca(2+)-binding !1protein. !$#cross-references MUID:94031845; PMID:8217841 !$#accession S35985 !'##molecule_type protein !'##residues 1-95 ##label IVA CLASSIFICATION #superfamily S-100 protein; calmodulin repeat homology KEYWORDS calcium binding; EF hand FEATURE !$49-81 #domain calmodulin repeat homology #label EF2 SUMMARY #length 95 #molecular-weight 10672 #checksum 734 SEQUENCE /// ENTRY BCHUIB #type complete TITLE S-100 protein beta chain [validated] - human ALTERNATE_NAMES neural S-100 calcium-binding protein beta ORGANISM #formal_name Homo sapiens #common_name man DATE 04-Dec-1986 #sequence_revision 06-Jan-1995 #text_change 08-Dec-2000 ACCESSIONS A38364; A92972; A03076 REFERENCE A38364 !$#authors Allore, R.J.; Friend, W.C.; O'Hanlon, D.; Neilson, K.M.; !1Baumal, R.; Dunn, R.J.; Marks, A. !$#journal J. Biol. Chem. (1990) 265:15537-15543 !$#title Cloning and expression of the human S100beta gene. !$#cross-references MUID:90368757; PMID:2394738 !$#accession A38364 !'##molecule_type DNA !'##residues 1-92 ##label ALL !'##cross-references GB:J05600; GB:M59486; NID:g337726; GB:M59487; !1NID:g337727; GB:M59488; NID:g337728; PIDN:AAA60367.1; !1PID:g337730 REFERENCE A92972 !$#authors Jensen, R.; Marshak, D.R.; Anderson, C.; Lukas, T.J.; !1Watterson, D.M. !$#journal J. Neurochem. (1985) 45:700-705 !$#title Characterization of human brain S100 protein fraction: amino !1acid sequence of S100beta. !$#cross-references MUID:85291729; PMID:4031854 !$#accession A92972 !'##molecule_type protein !'##residues 2-92 ##label JEN REFERENCE A90653 !$#authors Baudier, J.; Glasser, N.; Haglid, K.; Gerard, D. !$#journal Biochim. Biophys. Acta (1984) 790:164-173 !$#title Purification, characterization and ion binding properties of !1human brain S100b protein. !$#cross-references MUID:85023393; PMID:6487634 !$#contents annotation; metal ion-binding properties COMMENT This protein binds p53, tubulin and many other proteins at !1physiological concentrations of calcium and modulates their !1phosphorylation by protein kinase. COMMENT S-100 is an intracellular protein that binds calcium. It !1binds zinc more tightly, however, and this appears to !1increase the affinity of the protein for calcium. Distinct !1binding sites with different affinities exist for both ions !1on each monomer. Physiological concentrations of potassium !1ion antagonize the binding of both divalent cations, !1especially affecting high-affinity calcium-binding sites. COMMENT This protein is expressed predominantly in brain tissue by !1astroglial cells. It is expressed in other tissues to a !1lesser extent than the alpha chain. COMMENT The homodimer contains disulfide bonds, but the bond pattern !1has not been determined. GENETICS !$#gene GDB:S100B !'##cross-references GDB:120360; OMIM:176990 !$#map_position 21q22.3-21q22.3 !$#introns 46/3 !$#note the first intron occurs before the initiator codon COMPLEX homodimer; heterodimer with S-100 protein alpha chain (see !1PIR:BCHUIA) CLASSIFICATION #superfamily S-100 protein; calmodulin repeat homology KEYWORDS blocked amino end; brain; calcium binding; EF hand; !1heterodimer; homodimer; zinc FEATURE !$2-92 #product S-100 protein beta chain #status !8experimental #label MAT\ !$6-40 #domain calmodulin repeat homology #label EF1\ !$49-81 #domain calmodulin repeat homology #label EF2\ !$2 #modified_site blocked amino end (Ser) (in mature !8form) (probably acetylated) #status experimental\ !$19,22,24,27,32 #binding_site calcium (Ser, Glu, Asp, Lys, Glu) !8#status predicted\ !$62,64,66,68,73 #binding_site calcium (Asp, Asp, Asp, Glu, Glu) !8#status predicted SUMMARY #length 92 #molecular-weight 10713 #checksum 9912 SEQUENCE /// ENTRY BCBOIB #type complete TITLE S-100 protein beta chain - bovine ALTERNATE_NAMES neurocalcin delta-binding protein S100-beta ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-May-1979 #sequence_revision 14-Nov-1983 #text_change 24-Nov-1999 ACCESSIONS A91254; B91110; A90075; S54348; A03077 REFERENCE A91254 !$#authors Isobe, T.; Okuyama, T. !$#journal Eur. J. Biochem. (1978) 89:379-388 !$#title The amino-acid sequence of S-100 protein (PAP-I-b protein) !1and its relation to the calcium-binding proteins. !$#cross-references MUID:79045265; PMID:710399 !$#accession A91254 !'##molecule_type protein !'##residues 'ESEL',5-91 ##label ISO !'##experimental_source brain !'##note this sequence has since been revised in reference A91110 REFERENCE A91110 !$#authors Isobe, T.; Okuyama, T. !$#journal Eur. J. Biochem. (1981) 116:79-86 !$#title The amino-acid sequence of the alpha subunit in bovine brain !1S-100 a protein. !$#cross-references MUID:81236562; PMID:7250124 !$#accession B91110 !'##molecule_type protein !'##residues 1-91 ##label IS2 REFERENCE A90471 !$#authors Baudier, J.; Gerard, D. !$#journal Biochemistry (1983) 22:3360-3369 !$#title Ions binding to S100 proteins: structural changes induced by !1calcium and zinc on S100a and S100b proteins. !$#cross-references MUID:84000339; PMID:6615778 !$#contents annotation; metal ion-binding properties REFERENCE A90075 !$#authors Marshak, D.R.; Umekawa, H.; Watterson, D.M.; Hidaka, H. !$#journal Arch. Biochem. Biophys. (1985) 240:777-780 !$#title Structural characterization of the calcium binding protein !1S100 from adipose tissue. !$#cross-references MUID:85278169; PMID:4026304 !$#accession A90075 !'##molecule_type protein !'##residues 1-91 ##label MAR !'##experimental_source adipose tissue REFERENCE S54343 !$#authors Okazaki, K.; Obata, N.H.; Inoue, S.; Hidaka, H. !$#journal Biochem. J. (1995) 306:551-555 !$#title S100-beta is a target protein of neurocalcin delta, an !1abundant isoform in glial cells. !$#cross-references MUID:95194333; PMID:7887910 !$#accession S54348 !'##molecule_type protein !'##residues 56-61,'N',63-79,'V' ##label OKA COMMENT The S-100 protein is composed of two related polypeptide !1chains, alpha and beta, that form dimers, S-100a !1(alpha-beta) and S-100b (beta-beta). Although predominant !1among the water-soluble brain proteins, S-100 is also found !1in a variety of other tissues. COMMENT S-100 is an intracellular protein that weakly binds calcium. !1It binds zinc very tightly, however, and this appears to !1increase the affinity of the protein for calcium. Distinct !1binding sites with different affinities exist for both ions !1on each monomer. Physiological concentrations of potassium !1ion antagonize the binding of both divalent cations, !1especially affecting high-affinity calcium-binding sites. CLASSIFICATION #superfamily S-100 protein; calmodulin repeat homology KEYWORDS blocked amino end; brain; calcium binding; EF hand; zinc FEATURE !$5-39 #domain calmodulin repeat homology #label EF1\ !$48-80 #domain calmodulin repeat homology #label EF2\ !$1 #modified_site blocked amino end (Ser) (probably !8acetylated) #status experimental\ !$18,21,23,26,31 #binding_site calcium (Ser, Glu, Asp, Lys, Glu) !8#status predicted\ !$61,63,65,67,72 #binding_site calcium (Asp, Asp, Asp, Glu, Glu) !8#status predicted SUMMARY #length 91 #molecular-weight 10537 #checksum 7271 SEQUENCE /// ENTRY S27011 #type complete TITLE calcyclin - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S27011; S20264; S16116 REFERENCE S27011 !$#authors Ando, Y.; Watanabe, M.; Akatsuka, H.; Tokumitsu, H.; Hidaka, !1H. !$#journal FEBS Lett. (1992) 314:109-113 !$#title Site-directed mutation makes rabbit calcyclin dimer. !$#cross-references MUID:93093152; PMID:1459239 !$#accession S27011 !'##molecule_type mRNA !'##residues 1-90 ##label AND !'##cross-references EMBL:D10885; NID:g217743; PIDN:BAA01707.1; !1PID:g217744 !'##experimental_source lung REFERENCE S20264 !$#authors Tokumitsu, H.; Kobayashi, R.; Hidaka, H. !$#journal Arch. Biochem. Biophys. (1991) 291:401 !$#title Corrigendum. A calcium-binding protein from rabbit lung !1cytosol identified as the product of growth-regulated gene !1(2A9) and its binding proteins. !$#cross-references MUID:92061074; PMID:1952954 !$#accession S20264 !'##molecule_type protein !'##residues 23-30;35-46;55-89 ##label TOK !'##experimental_source lung REFERENCE S16116 !$#authors Tokumitsu, H.; Kobayashi, R.; Hidaka, H. !$#journal Arch. Biochem. Biophys. (1991) 288:202-207 !$#title A calcium-binding protein from rabbit lung cytosol !1identified as the product of growth-regulated gene (2A9) and !1its binding proteins. !$#cross-references MUID:91378440; PMID:1898017 !$#accession S16116 !'##molecule_type protein !'##residues 23-27,'G',29-30;35-42,'G',44-46;55-81,'V',83-89 ##label TOW !'##experimental_source lung CLASSIFICATION #superfamily S-100 protein; calmodulin repeat homology KEYWORDS calcium binding; EF hand; monomer FEATURE !$7-41 #domain calmodulin repeat homology #label EF1\ !$48-80 #domain calmodulin repeat homology #label EF2 SUMMARY #length 90 #molecular-weight 10154 #checksum 5694 SEQUENCE /// ENTRY JH0663 #type complete TITLE calpactin I light chain - chicken ALTERNATE_NAMES p10 protein; p11 protein ORGANISM #formal_name Gallus gallus #common_name chicken DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JH0663 REFERENCE JH0662 !$#authors Kube, E.; Weber, K.; Gerke, V. !$#journal Gene (1991) 102:255-259 !$#title Primary structure of human, chicken, and Xenopus laevis p11, !1a cellular ligand of the Src-kinase substrate, annexin II. !$#cross-references MUID:91340161; PMID:1831433 !$#accession JH0663 !'##molecule_type mRNA !'##residues 1-97 ##label KUB !'##cross-references GB:M38592; NID:g211531; PIDN:AAA48690.1; !1PID:g211532 COMMENT This protein interacts with annexin II. CLASSIFICATION #superfamily S-100 protein; calmodulin repeat homology KEYWORDS calcium binding; EF hand FEATURE !$2-97 #product p11 protein #status predicted #label P11\ !$18-29 #domain calcium binding #status predicted #label CA1\ !$47-79 #domain calmodulin repeat homology #label EFH\ !$59-70 #domain calcium binding #status predicted #label CA2 SUMMARY #length 97 #molecular-weight 11290 #checksum 5364 SEQUENCE /// ENTRY JH0664 #type complete TITLE calpactin I light chain - African clawed frog ALTERNATE_NAMES p10 protein; p11 protein ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JH0664 REFERENCE JH0662 !$#authors Kube, E.; Weber, K.; Gerke, V. !$#journal Gene (1991) 102:255-259 !$#title Primary structure of human, chicken, and Xenopus laevis p11, !1a cellular ligand of the Src-kinase substrate, annexin II. !$#cross-references MUID:91340161; PMID:1831433 !$#accession JH0664 !'##molecule_type mRNA !'##residues 1-96 ##label KUB !'##cross-references GB:M38593; NID:g214037; PIDN:AAA49676.1; !1PID:g214038 COMMENT This protein interacts with annexin II. CLASSIFICATION #superfamily S-100 protein; calmodulin repeat homology KEYWORDS calcium binding; EF hand FEATURE !$2-96 #product p11 protein #status predicted #label P11\ !$20-31 #domain calcium binding #status predicted #label CA1\ !$49-81 #domain calmodulin repeat homology #label EFH\ !$61-72 #domain calcium binding #status predicted #label CA2 SUMMARY #length 96 #molecular-weight 11329 #checksum 4373 SEQUENCE /// ENTRY I37080 #type complete TITLE calgizzarin - human ALTERNATE_NAMES MLN 70k protein; S-100 calcium-binding protein C (S100C) ORGANISM #formal_name Homo sapiens #common_name man DATE 01-Nov-1996 #sequence_revision 23-May-1997 #text_change 22-Jun-1999 ACCESSIONS I37080; I52684; S60679 REFERENCE I37080 !$#authors Tomasetto, C.; Regnier, C.H.; Moog-Lutz, C.; Mattei, M.G.; !1Chenard, M.P.; Lidereau, R.; Basset, P.; Rio, M.C. !$#journal Genomics (1995) 28:367-376 !$#title Identification of four novel human genes amplified and !1overexpressed in breast carcinoma and located to the !1q11-q21.3 region of chromosome 17. !$#cross-references MUID:96039245; PMID:7490069 !$#accession I37080 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-105 ##label TOM !'##cross-references EMBL:X80201; NID:g951232; PIDN:CAA56492.1; !1PID:g951233 !'##note submitted to the EMBL Data Library, July 1994 REFERENCE I52684 !$#authors Tanaka, M.; Adzuma, K.; Iwami, M.; Yoshimoto, K.; Monden, !1Y.; Itakura, M. !$#journal Cancer Lett. (1995) 89:195-200 !$#title Human calgizzarin; one colorectal cancer-related gene !1selected by a large scale random cDNA sequencing and !1northern blot analysis. !$#cross-references MUID:95196222; PMID:7889529 !$#accession I52684 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-105 ##label TAN !'##cross-references DDBJ:D38583; NID:g560790; PIDN:BAA07597.1; !1PID:g560791 COMMENT This protein apparently binds annexin I and possibly other !1cytoskeletal proteins at physiological concentrations of !1calcium and modulates their phosphorylation by protein !1kinase C. GENETICS !$#gene GDB:S100A11; S100C; MLN70 !'##cross-references GDB:5218372 !$#map_position 1q21-1q21 CLASSIFICATION #superfamily S-100 protein; calmodulin repeat homology KEYWORDS calcium binding; EF hand FEATURE !$12-46 #domain calmodulin repeat homology #label EF1\ !$55-87 #domain calmodulin repeat homology #label EF2 SUMMARY #length 105 #molecular-weight 11740 #checksum 4009 SEQUENCE /// ENTRY JQ1300 #type complete TITLE calgizzarin - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS JQ1300; PQ0243; B41004 REFERENCE JQ1300 !$#authors Watanabe, M.; Ando, Y.; Todoroki, H.; Minami, H.; Hidaka, H. !$#journal Biochem. Biophys. Res. Commun. (1991) 181:644-649 !$#title Molecular cloning and sequencing of a cDNA clone encoding a !1new calcium binding protein, named calgizzarin, from rabbit !1lung. !$#cross-references MUID:92095968; PMID:1836726 !$#accession JQ1300 !'##molecule_type mRNA !'##residues 1-102 ##label WAT !'##cross-references GB:D10586; GB:D90531; NID:g217745; PIDN:BAA01443.1; !1PID:g217746 !$#accession PQ0243 !'##molecule_type protein !'##residues 25-49;53-62 ##label WAT2 !'##experimental_source lung REFERENCE A41004 !$#authors Todoroki, H.; Kobayashi, R.; Watanabe, M.; Minami, H.; !1Hidaka, H. !$#journal J. Biol. Chem. (1991) 266:18668-18673 !$#title Purification, characterization, and partial sequence !1analysis of a newly identified EF-hand type 13-kDa Ca !1(2+)-binding protein from smooth muscle and non-muscle !1tissues. !$#cross-references MUID:92011625; PMID:1917990 !$#accession B41004 !'##status preliminary !'##molecule_type protein !'##residues 25-49,53-58,'Y',60-62 ##label TOD CLASSIFICATION #superfamily S-100 protein; calmodulin repeat homology KEYWORDS calcium binding; EF hand FEATURE !$9-43 #domain calmodulin repeat homology #label EF1\ !$52-84 #domain calmodulin repeat homology #label EF2 SUMMARY #length 102 #molecular-weight 11429 #checksum 2261 SEQUENCE /// ENTRY BCHUY #type complete TITLE calcyclin - human ALTERNATE_NAMES growth factor-inducible protein 2A9; prolactin receptor-associated protein ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1988 #sequence_revision 31-Dec-1992 #text_change 22-Jun-1999 ACCESSIONS A28363; A25645; A30356; PC1222 REFERENCE A92705 !$#authors Murphy, L.C.; Murphy, L.J.; Tsuyuki, D.; Duckworth, M.L.; !1Shiu, R.P.C. !$#journal J. Biol. Chem. (1988) 263:2397-2401 !$#title Cloning and characterization of a cDNA encoding a highly !1conserved, putative calcium binding protein, identified by !1an anti-prolactin receptor antiserum. !$#cross-references MUID:88115387; PMID:2448309 !$#accession A28363 !'##molecule_type mRNA !'##residues 1-90 ##label MUR !'##cross-references GB:M18981; NID:g179767; PIDN:AAA51906.1; !1PID:g179768 REFERENCE A25645 !$#authors Calabretta, B.; Battini, R.; Kaczmarek, L.; de Riel, J.K.; !1Baserga, R. !$#journal J. Biol. Chem. (1986) 261:12628-12632 !$#title Molecular cloning of the cDNA for a growth factor-inducible !1gene with strong homology to S-100, a calcium-binding !1protein. !$#cross-references MUID:86304442; PMID:3755724 !$#accession A25645 !'##molecule_type mRNA !'##residues 2-90 ##label CAL !'##cross-references GB:M14300; NID:g183097; PIDN:AAA35886.1; !1PID:g183098 !'##experimental_source fibroblasts REFERENCE A30356 !$#authors Gabius, H.J.; Bardosi, A.; Gabius, S.; Hellmann, K.P.; !1Karas, M.; Kratzin, H. !$#journal Biochem. Biophys. Res. Commun. (1989) 163:506-512 !$#title Identification of a cell cycle-dependent gene product as a !1sialic acid-binding protein. !$#cross-references MUID:89374276; PMID:2775283 !$#accession A30356 !'##molecule_type protein !'##residues 57-63,'X',65,'X',67-70,'X',72-74 ##label GAB !'##note the amino end of the intact protein is blocked REFERENCE PC1222 !$#authors Tomida, Y.; Terasawa, M.; Kobayashi, R.; Hidaka, H. !$#journal Biochem. Biophys. Res. Commun. (1992) 189:1310-1316 !$#title Calcyclin and calvasculin exist in human platelets. !$#cross-references MUID:93129189; PMID:1482346 !$#accession PC1222 !'##molecule_type protein !'##residues 27-31;48-87,'XX' ##label TOM !'##experimental_source platelets COMMENT This protein is expressed in a cell cycle-specific manner. !1Not found in the G-0 phase, it is rapidly produced when !1quiescent cells are stimulated to proliferate; its !1concentration remains high in cycling cells. It is !1overproduced in certain acute myeloid leukemias. COMMENT Homology of this protein to the S-100 proteins is of !1interest given the role of calcium in the regulation of cell !1proliferation. Calmodulin, also expressed in a cell !1cycle-dependent manner, is postulated to have a role in !1cell-cycle regulation. COMMENT This protein binds sialic acid in the presence of calcium. GENETICS !$#gene GDB:S100A6; CACY !'##cross-references GDB:119048; OMIM:114110 !$#map_position 1q21-1q21 CLASSIFICATION #superfamily S-100 protein; calmodulin repeat homology KEYWORDS calcium binding; EF hand; growth regulation; mitogen FEATURE !$7-41 #domain calmodulin repeat homology #label EF1\ !$48-80 #domain calmodulin repeat homology #label EF2 SUMMARY #length 90 #molecular-weight 10180 #checksum 5333 SEQUENCE /// ENTRY LUPG10 #type complete TITLE calpactin I light chain - pig ALTERNATE_NAMES p10 protein; p11 protein ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 18-Jul-1997 ACCESSIONS A03079; A24063 REFERENCE A03079 !$#authors Gerke, V.; Weber, K. !$#journal EMBO J. (1985) 4:2917-2920 !$#title The regulatory chain in the p36-kd substrate complex of !1viral tyrosine-specific protein kinases is related in !1sequence to the S-100 protein of glial cells. !$#cross-references MUID:86055730; PMID:2998764 !$#accession A03079 !'##molecule_type protein !'##residues 1-95 ##label GER REFERENCE A24063 !$#authors Hexham, J.M.; Totty, N.F.; Waterfield, M.D.; Crumpton, M.J. !$#journal Biochem. Biophys. Res. Commun. (1986) 134:248-254 !$#title Homology between the subunits of S100 and A 10kDa !1polypeptide associated with p36 of pig lymphocytes. !$#cross-references MUID:86130472; PMID:2936341 !$#accession A24063 !'##molecule_type protein !'##residues 1-51,'XX',54-55 ##label HEX COMMENT Calpactin I light does not appear to bind calcium. COMPLEX Calpactin I is a tetramer of two light chains and two heavy !1chains (annexin II). FUNCTION !$#description found in lamina beneath plasma membrane where it may !1cross-link plasma membrane lipids with cytoskeletal actin !$#pathway exocytosis CLASSIFICATION #superfamily S-100 protein; calmodulin repeat homology KEYWORDS EF hand; intestine FEATURE !$6-37 #domain calmodulin repeat homology #label EF1\ !$46-78 #domain calmodulin repeat homology #label EF2 SUMMARY #length 95 #molecular-weight 10944 #checksum 8878 SEQUENCE /// ENTRY JN0246 #type complete TITLE calcium-binding protein, intestinal - human ALTERNATE_NAMES calbindin D9K; ICBP ORGANISM #formal_name Homo sapiens #common_name man DATE 17-Aug-1992 #sequence_revision 06-Dec-1996 #text_change 22-Jun-1999 ACCESSIONS JN0246; S24047; I56435; S21501 REFERENCE JN0246 !$#authors Howard, A.; Legon, S.; Spurr, N.K.; Walters, J.R.F. !$#journal Biochem. Biophys. Res. Commun. (1992) 185:663-669 !$#title Molecular cloning and chromosomal assignment of human !1calbindin-D9k. !$#cross-references MUID:92304291; PMID:1610358 !$#accession JN0246 !'##molecule_type mRNA !'##residues 1-79 ##label HOW !'##cross-references EMBL:X65869; NID:g29601; PIDN:CAA46699.1; !1PID:g29602 !'##experimental_source intestine REFERENCE S24047 !$#authors Jeung, E.B.; Krisinger, J.; Dann, J.L.; Leung, P.C.K. !$#journal FEBS Lett. (1992) 307:224-228 !$#title Molecular cloning of the full-length cDNA encoding the human !1calbindin-D(9k). !$#cross-references MUID:92354716; PMID:1379540 !$#accession S24047 !'##status preliminary !'##molecule_type mRNA !'##residues 1-79 ##label JEU1 !'##cross-references GB:L13220; NID:g291883; PIDN:AAA35638.1; !1PID:g291884 REFERENCE I56435 !$#authors Jeung, E. !$#journal J. Mol. Biol. (1994) 235:1231-1238 !$#title The human calbindin-D9k gene: complete structure and !1implications on rsdteroid hormone regulation. !$#cross-references MUID:94141916; PMID:8308886 !$#accession I56435 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-78,'S' ##label JEU2 !'##cross-references GB:L13042; NID:g291881; PIDN:AAA35637.1; !1PID:g553213 COMMENT This protein increases calcium absorption by buffering !1calcium in the cytoplasm, and also increases ATP-dependent !1calcium transport in duodenal basolateral membrane vesicles. COMMENT This protein binds to the regulatory calmodulin binding !1domain of the plasma membrane calcium pump. GENETICS !$#gene GDB:CALB3 !'##cross-references GDB:133780; OMIM:302020 !$#map_position Xp22.2-Xp22.2 !$#introns 45/3 CLASSIFICATION #superfamily S-100 protein; calmodulin repeat homology KEYWORDS acetylated amino end; calcium binding; duplication; EF hand; !1vitamin D FEATURE !$2-79 #product calcium-binding protein, intestinal #status !8predicted #label MAT\ !$5-39 #domain calmodulin repeat homology #label EF1\ !$45-77 #domain calmodulin repeat homology #label EF2\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status predicted\ !$18,21,23,26,31 #binding_site calcium, low affinity (Ala, Glu, Asp, !8Gln, Glu) #status predicted\ !$58,60,62,64,69 #binding_site calcium, high affinity (Asp, Asn, Asp, !8Glu, Glu) #status predicted SUMMARY #length 79 #molecular-weight 9016 #checksum 2701 SEQUENCE /// ENTRY KLRTI #type complete TITLE calcium-binding protein, intestinal - rat ALTERNATE_NAMES calbindin D9K; cholecalcin; mammalian type CaBP; small CaBP ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 28-Aug-1985 #sequence_revision 30-Jun-1992 #text_change 21-Jul-2000 ACCESSIONS A31258; S00330; A28039; A03069; A92404; A37336; S34063 REFERENCE A31258 !$#authors Krisinger, J.; Darwish, H.; Maeda, N.; DeLuca, H.F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:8988-8992 !$#title Structure and nucleotide sequence of the rat intestinal !1vitamin D-dependent calcium binding protein gene. !$#cross-references MUID:89057864; PMID:3194402 !$#accession A31258 !'##molecule_type DNA !'##residues 1-79 ##label KRI !'##cross-references GB:J04133 REFERENCE S00330 !$#authors Perret, C.; Lomri, N.; Gouhier, N.; Auffray, C.; Thomasset, !1M. !$#journal Eur. J. Biochem. (1988) 172:43-51 !$#title The rat vitamin-D-dependent calcium-binding protein (9-kDa !1CaBP) gene: complete nucleotide sequence and structural !1organization. !$#cross-references MUID:88151999; PMID:3345761 !$#accession S00330 !'##molecule_type DNA !'##residues 1-79 ##label PER !'##cross-references EMBL:X16635; NID:g3287250; PIDN:CAA34627.1; !1PID:g297532 REFERENCE A28039 !$#authors Darwish, H.M.; Krisinger, J.; Strom, M.; DeLuca, H.F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:6108-6111 !$#title Molecular cloning of the cDNA and chromosomal gene for !1vitamin D-dependent calcium-binding protein of rat !1intestine. !$#cross-references MUID:87317604; PMID:3476932 !$#accession A28039 !'##molecule_type mRNA !'##residues 1-79 ##label DAR !'##cross-references GB:J02954; NID:g207644; PIDN:AAA42333.1; !1PID:g207645 REFERENCE A90330 !$#authors MacManus, J.P.; Watson, D.C.; Yaguchi, M. !$#journal Biochem. J. (1986) 235:585-595 !$#title The purification and complete amino acid sequence of the !19000-Mr Ca2+-binding protein from rat placenta. !$#cross-references MUID:86295646; PMID:3741407 !$#accession A03069 !'##molecule_type protein !'##residues 'AS',4-59,'D',61-79 ##label MAC REFERENCE A92404 !$#authors Desplan, C.; Heidmann, O.; Lillie, J.W.; Auffray, C.; !1Thomasset, M. !$#journal J. Biol. Chem. (1983) 258:13502-13505 !$#title Sequence of rat intestinal vitamin D-dependent !1calcium-binding protein derived from a cDNA clone. !$#cross-references MUID:84061748; PMID:6315698 !$#accession A92404 !'##molecule_type mRNA !'##residues 11-41,'N',43-54,'Q',56-60,'D',62-79 ##label DES !'##cross-references GB:K00994 REFERENCE A37336 !$#authors Hubbard, M.J. !$#submission submitted to the Protein Sequence Database, November 1992 !$#accession A37336 !'##molecule_type protein !'##residues 56-75 ##label HUB REFERENCE S34063 !$#authors Hubbard, M.J. !$#journal Biochem. J. (1993) 293:223-227 !$#title Rapid purification and direct microassay of calbindin(9kDa) !1utilizing its solubility in perchloric acid. !$#cross-references MUID:93319513; PMID:8392333 !$#accession S34063 !'##molecule_type protein !'##residues 56-75 ##label HU2 COMMENT The synthesis of this protein in the duodenum is vitamin !1D3-dependent. GENETICS !$#introns 45/3 CLASSIFICATION #superfamily S-100 protein; calmodulin repeat homology KEYWORDS blocked amino end; calcium binding; duplication; EF hand FEATURE !$2-79 #product calcium-binding protein, intestinal #status !8experimental #label MAT\ !$5-39 #domain calmodulin repeat homology #label EF1\ !$45-77 #domain calmodulin repeat homology #label EF2\ !$2 #modified_site blocked amino end (Ser) (in mature !8form) (probably acetylated) #status experimental\ !$18,21,23,26,31 #binding_site calcium (Ala, Glu, Asp, Gln, Glu) !8#status predicted\ !$58,60,62,64,69 #binding_site calcium (Asp, Asn, Asp, Glu, Glu) !8#status predicted SUMMARY #length 79 #molecular-weight 9038 #checksum 3819 SEQUENCE /// ENTRY KLBOI #type complete TITLE calcium-binding protein, intestinal [validated] - bovine ALTERNATE_NAMES calbindin D9K ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 29-Jul-1981 #sequence_revision 30-Jun-1992 #text_change 15-Sep-2000 ACCESSIONS A40151; A03068 REFERENCE A40151 !$#authors Kumar, R.; Wieben, E.; Beecher, S.J. !$#journal Mol. Endocrinol. (1989) 3:427-432 !$#title The molecular cloning of the complementary deoxyribonucleic !1acid for bovine vitamin D-dependent calcium-binding protein: !1structure of the full-length protein and evidence for !1homologies with other calcium-binding proteins of the !1troponin-C superfamily of proteins. !$#cross-references MUID:89219112; PMID:2710141 !$#accession A40151 !'##molecule_type mRNA !'##residues 1-79 ##label KUM !'##cross-references GB:M18344; NID:g162774; PIDN:AAA30420.1; !1PID:g162775 REFERENCE A92325 !$#authors Fullmer, C.S.; Wasserman, R.H. !$#journal J. Biol. Chem. (1981) 256:5669-5674 !$#title The amino acid sequence of bovine intestinal calcium-binding !1protein. !$#cross-references MUID:81215479; PMID:7240164 !$#accession A03068 !'##molecule_type protein !'##residues 5-79 ##label FUL !'##note the sequence of the minor A component was determined; this is !1one of several irreversibly altered forms that appear during !1isolation and storage; it has an unblocked amino end and may !1differ slightly in amino acid composition from the native !1protein, which is blocked at the amino end REFERENCE A68294 !$#authors Andersson, E.M. !$#submission submitted to the Brookhaven Protein Data Bank, March 1997 !$#cross-references PDB:6ICB !$#contents annotation; X-ray crystallography, 1.85 angstroms, residues !1'M',5-75 REFERENCE A68292 !$#authors Andersson, E.M.; Svensson, L.A. !$#submission submitted to the Brookhaven Protein Data Bank, March 1997 !$#cross-references PDB:5ICB !$#contents annotation; X-ray crystallography, 1.5 angstroms, residues !15-75 REFERENCE A51526 !$#authors Svensson, L.A. !$#submission submitted to the Brookhaven Protein Data Bank, August 1991 !$#cross-references PDB:4ICB !$#contents annotation; X-ray crystallography, 1.6 angstroms, residues !1'M',5-75 REFERENCE A50604 !$#authors Szebenyi, D.M.E.; Moffat, K. !$#submission submitted to the Brookhaven Protein Data Bank, September !11986 !$#cross-references PDB:3ICB !$#contents annotation; X-ray crystallography, 2.3 angstroms, residues !15-75 REFERENCE A93267 !$#authors Szebenyi, D.M.E.; Obendorf, S.K.; Moffat, K. !$#journal Nature (1981) 294:327-332 !$#title Structure of vitamin D-dependent calcium-binding protein !1from bovine intestine. !$#cross-references MUID:82080639; PMID:7312031 !$#contents annotation; X-ray crystallography, 2.3 angstroms COMMENT This protein increases calcium absorption by buffering !1calcium in the cytoplasm, and also increases ATP-dependent !1calcium transport in duodenal basolateral membrane vesicles. COMMENT This protein binds to the regulatory calmodulin binding !1domain of the plasma membrane calcium pump. CLASSIFICATION #superfamily S-100 protein; calmodulin repeat homology KEYWORDS blocked amino end; calcium binding; duplication; EF hand; !1vitamin D FEATURE !$2-79 #product calcium-binding protein, intestinal #status !8predicted #label MAT\ !$5-39 #domain calmodulin repeat homology #label EF1\ !$45-77 #domain calmodulin repeat homology #label EF2\ !$2 #modified_site blocked amino end (Ser) (in mature !8form) (probably acetylated) #status experimental\ !$18,21,23,26,31 #binding_site calcium, low affinity (Ala, Glu, Asp, !8Gln, Glu) #status experimental\ !$58,60,62,64,69 #binding_site calcium, high affinity (Asp, Asn, Asp, !8Glu, Glu) #status experimental SUMMARY #length 79 #molecular-weight 8918 #checksum 3254 SEQUENCE /// ENTRY KLPGI #type complete TITLE calcium-binding protein, intestinal - pig ALTERNATE_NAMES calbindin D9K; cholecalcin; mammalian type CaBP; small CaBP; vitamin D-dependent calcium binding protein, 9K ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 30-Nov-1979 #sequence_revision 08-May-1998 #text_change 22-Jun-1999 ACCESSIONS A56802; A03067 REFERENCE A56802 !$#authors Jeung, E.B.; Krisinger, J.; Dann, J.L.; Leung, P.C. !$#journal Biol. Reprod. (1992) 47:503-508 !$#title Cloning of the porcine calbindin-D9k complementary !1deoxyribonucleic acid by anchored polymerase chain reaction !1technique. !$#cross-references MUID:93003906; PMID:1391336 !$#accession A56802 !'##status preliminary !'##molecule_type mRNA !'##residues 1-79 ##label JEU !'##cross-references GB:L13068; NID:g294215; PIDN:AAA81524.1; !1PID:g550499 !'##experimental_source duodenum !'##note sequence extracted from NCBI backbone (NCBIN:116912, !1NCBIP:116913) REFERENCE A03067 !$#authors Hofmann, T.; Kawakami, M.; Hitchman, A.J.W.; Harrison, J.E.; !1Dorrington, K.J. !$#journal Can. J. Biochem. (1979) 57:737-748 !$#title The amino acid sequence of porcine intestinal !1calcium-binding protein. !$#cross-references MUID:80001355; PMID:476518 !$#accession A03067 !'##molecule_type protein !'##residues 2-61,'N',63-79 ##label HOF !'##note a minor component lacks Ser-2; its amino end is also acetylated COMMENT This protein increases calcium absorption by buffering !1calcium in the cytoplasm, and also increases ATP-dependent !1calcium transport in duodenal basolateral membrane vesicles. COMMENT This protein binds to the regulatory calmodulin binding !1domain of the plasma membrane calcium pump. CLASSIFICATION #superfamily S-100 protein; calmodulin repeat homology KEYWORDS acetylated amino end; calcium binding; duplication; EF hand; !1vitamin D FEATURE !$2-79 #product calcium-binding protein, intestinal, major !8component #status experimental #label MAJ\ !$3-79 #product calcium-binding protein, intestinal, minor !8component #status experimental #label MIN\ !$5-39 #domain calmodulin repeat homology #label EF1\ !$45-77 #domain calmodulin repeat homology #label EF2\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental\ !$3 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental\ !$18,21,23,26,31 #binding_site calcium, low affinity (Ala, Glu, Asp, !8Gln, Glu) #status predicted\ !$58,60,62,64,69 #binding_site calcium, high affinity (Asp, Asn, Asp, !8Glu, Glu) #status predicted SUMMARY #length 79 #molecular-weight 8929 #checksum 3290 SEQUENCE /// ENTRY BCHUCF #type complete TITLE calgranulin A [validated] - human ALTERNATE_NAMES calcium-binding protein MRP-8; cystic fibrosis-associated antigen (CF Ag) light chain; leukocyte L1 complex light chain; macrophage migration inhibitory factor-related 8K protein (MRP-8); MIF-related protein 8K chain; oncodevelopmental protein; S-100 calcium-binding protein A8 (S100A8) ORGANISM #formal_name Homo sapiens #common_name man DATE 28-Dec-1987 #sequence_revision 07-Oct-1994 #text_change 08-Dec-2000 ACCESSIONS A31848; S00705; S13454; A29764; A60911; A61082; C54327; !1A44111; S53791 REFERENCE A93102 !$#authors Lagasse, E.; Clerc, R.G. !$#journal Mol. Cell. Biol. (1988) 8:2402-2410 !$#title Cloning and expression of two human genes encoding !1calcium-binding proteins that are regulated during myeloid !1differentiation. !$#cross-references MUID:88302148; PMID:3405210 !$#accession A31848 !'##molecule_type DNA !'##residues 1-93 ##label LAG !'##cross-references GB:M21005; NID:g188691; PIDN:AAA36327.1; !1PID:g386959 REFERENCE S00667 !$#authors Odink, K.; Cerletti, N.; Brueggen, J.; Clerc, R.G.; Tarcsay, !1L.; Zwadlo, G.; Gerhards, G.; Schlegel, R.; Sorg, C. !$#journal Nature (1987) 330:80-82 !$#title Two calcium-binding proteins in infiltrate macrophages of !1rheumatoid arthritis. !$#cross-references MUID:88039099; PMID:3313057 !$#accession S00705 !'##molecule_type mRNA !'##residues 1-93 ##label ODI !'##cross-references EMBL:X06234; NID:g34772; PIDN:CAA29580.1; !1PID:g34773 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE S13454 !$#authors Schaefer, T.; Sachse, G.E.; Gassen, H.G. !$#journal Biol. Chem. Hoppe-Seyler (1991) 372:1-4 !$#title The calcium-binding protein MRP-8 is produced by human !1pulmonary tumor cells. !$#cross-references MUID:91248411; PMID:2039599 !$#accession S13454 !'##status preliminary !'##molecule_type mRNA !'##residues 1-93 ##label SCH REFERENCE A29764 !$#authors Dorin, J.R.; Novak, M.; Hill, R.E.; Brock, D.J.H.; Secher, !1D.S.; van Heyningen, V. !$#journal Nature (1987) 326:614-617 !$#title A clue to the basic defect in cystic fibrosis from cloning !1the CF antigen gene. !$#cross-references MUID:87173041; PMID:3561500 !$#accession A29764 !'##molecule_type mRNA !'##residues 1-78,'AWQPTKKAMKKATKSS' ##label DOR !'##cross-references EMBL:Y00278; NID:g29887; PIDN:CAA68390.1; !1PID:g29888 !'##note the differences after residue 78 are due to a frameshift REFERENCE A60911 !$#authors Andersson, K.B.; Sletten, K.; Berntzen, H.B.; Dale, I.; !1Brandtzaeg, P.; Jellum, E.; Fagerhol, M.K. !$#journal Scand. J. Immunol. (1988) 28:241-245 !$#title The leucocyte L1 protein: identity with the cystic fibrosis !1antigen and the calcium-binding MRP-8 and MRP-14 macrophage !1components. !$#cross-references MUID:88321575; PMID:3413449 !$#accession A60911 !'##molecule_type protein !'##residues 1-53,'X',55-56,'X',58-59;78-84,'X',86-89 ##label AND REFERENCE A61082 !$#authors Tobe, T.; Murakami, K.; Tomita, M.; Nozawa, R. !$#journal Chem. Pharm. Bull. (1989) 37:1576-1580 !$#title Amino acid sequences of 60B8 antigens induced in HL-60 cells !1by 1,25-dihydroxyvitamin D-3. The antigens are identical !1with macrophage-related protein-14 and -8. !$#cross-references MUID:89376638; PMID:2776242 !$#accession A61082 !'##molecule_type protein !'##residues 1-27;29-33;40-46;58-69;71-81,'S',83-84,'S' ##label TOB !'##experimental_source chronic myeloid leukemic cell line REFERENCE A54327 !$#authors Madsen, P.; Rasmussen, H.H.; Leffers, H.; Honore, B.; !1Dejgaard, K.; Olsen, E.; Kiil, J.; Walbum, E.; Andersen, !1A.H.; Basse, B.; Lauridsen, J.B.; Ratz, G.P.; Celis, A.; !1Vandekerckhove, J.; Celis, J.E. !$#journal J. Invest. Dermatol. (1991) 97:701-712 !$#title Molecular cloning, occurrence, and expression of a novel !1partially secreted protein "psoriasin" that is highly !1up-regulated in psoriatic skin. !$#cross-references MUID:92043866; PMID:1940442 !$#accession C54327 !'##molecule_type protein !'##residues 'X',38-47;50-53,'X',55-56 ##label MAD REFERENCE A44111 !$#authors Lemarchand, P.; Vaglio, M.; Mauel, J.; Markert, M. !$#journal J. Biol. Chem. (1992) 267:19379-19382 !$#title Translocation of a small cytosolic calcium-binding protein !1(MRP-8) to plasma membrane correlates with human neutrophil !1activation. !$#cross-references MUID:92406885; PMID:1326551 !$#accession A44111 !'##molecule_type protein !'##residues 1-25 ##label LEM !'##experimental_source zymosan-activated neutrophils !'##note sequence extracted from NCBI backbone (NCBIP:113895) REFERENCE S53791 !$#authors Nakai, M.; Ishikawa, M.; Hamada, Y.; Sugano, S. !$#journal Biol. Chem. Hoppe-Seyler (1994) 375:789-792 !$#title Isolation of an ascitic oncodevelopmental protein exhibiting !1high sequence homology with calcium-binding protein MRP8. !$#cross-references MUID:95209785; PMID:7695842 !$#accession S53791 !'##molecule_type protein !'##residues 1-16,'X',18-20 ##label NAK COMMENT Concentrations of this protein, a product of normal and !1leukemic granulocytes, are elevated in cystic fibrosis !1homozygotes and heterozygotes. COMMENT This protein can bind two calcium ions per molecule with an !1affinity similar to that of other S-100 proteins. GENETICS !$#gene GDB:S100A8; CAGA; CFAG !'##cross-references GDB:120569; OMIM:123885 !$#map_position 1q21-1q21 !$#introns 47/3 !$#note the first intron occurs before the initiator codon COMPLEX homodimer; heterodimer and higher complexes with calgranulin !1B (see PIR:B31848) CLASSIFICATION #superfamily S-100 protein; calmodulin repeat homology KEYWORDS calcium binding; cytokine; EF hand; heterodimer; homodimer; !1inflammation FEATURE !$1-93 #product calgranulin A #status experimental #label !8MAT\ !$7-41 #domain calmodulin repeat homology #label EF1\ !$46-78 #domain calmodulin repeat homology #label EF2 SUMMARY #length 93 #molecular-weight 10834 #checksum 4464 SEQUENCE /// ENTRY JN0685 #type complete TITLE calgranulin A - rat ALTERNATE_NAMES calcium-binding protein MRP-8; macrophage migration inhibitory factor-related 8K protein (MRP-8) ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 03-May-1994 #sequence_revision 23-May-1997 #text_change 22-Jun-1999 ACCESSIONS JN0685 REFERENCE JN0685 !$#authors Imamichi, T.; Uchida, I.; Wahl, S.M.; McCartney-Francis, N. !$#journal Biochem. Biophys. Res. Commun. (1993) 194:819-825 !$#title Expression and cloning of migration inhibitory !1factor-related protein (MRP)8 and MRP14 in !1arthritis-susceptible rats. !$#cross-references MUID:93343942; PMID:8343166 !$#accession JN0685 !'##molecule_type mRNA !'##residues 1-89 ##label IMA !'##cross-references GB:L18891; NID:g349548; PIDN:AAA41637.1; !1PID:g349549 !'##experimental_source strains LEW/N and F344/N COMMENT This protein has a role in susceptibility to SCW-induced !1chronic disease. GENETICS !$#gene MRP8 COMPLEX homodimer; heterodimer and higher complexes with calgranulin !1B CLASSIFICATION #superfamily S-100 protein; calmodulin repeat homology KEYWORDS calcium binding; cytokine; EF hand; heterodimer; homodimer; !1inflammation FEATURE !$7-41 #domain calmodulin repeat homology #label EF1\ !$46-78 #domain calmodulin repeat homology #label EF2 SUMMARY #length 89 #molecular-weight 10210 #checksum 5536 SEQUENCE /// ENTRY I56163 #type complete TITLE calgranulin A - mouse ALTERNATE_NAMES calcium-binding protein MRP-8; CP-10 chemotactic protein; macrophage migration inhibitory factor-related 8K protein (MRP-8) ORGANISM #formal_name Mus musculus #common_name house mouse DATE 26-Jul-1996 #sequence_revision 23-May-1997 #text_change 22-Jun-1999 ACCESSIONS I56163; A42488 REFERENCE I56163 !$#authors Lackmann, M.; Rajasekariah, P.; Iismaa, S.E.; Jones, G.; !1Cornish, C.J.; Hu, S.; Simpson, R.J.; Moritz, R.L.; Geczy, !1C.L. !$#journal J. Immunol. (1993) 150:2981-2991 !$#title Identification of a chemotactic domain of the !1pro-inflammatory S100 protein CP-10. !$#cross-references MUID:93203618; PMID:8454868 !$#accession I56163 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-89 ##label LAC1 !'##cross-references GB:S57123; NID:g298706; PIDN:AAB25840.1; !1PID:g298707 REFERENCE A42488 !$#authors Lackmann, M.; Cornish, C.J.; Simpson, R.J.; Moritz, R.L.; !1Geczy, C.L. !$#journal J. Biol. Chem. (1992) 267:7499-7504 !$#title Purification and structural analysis of a murine chemotactic !1cytokine (CP-10) with sequence homology to S100 proteins. !$#cross-references MUID:92218405; PMID:1559987 !$#accession A42488 !'##molecule_type protein !'##residues 2-77 ##label LAC2 !'##note sequence extracted from NCBI backbone (NCBIP:94068) GENETICS !$#gene MRP8 COMPLEX homodimer; heterodimer and higher complexes with calgranulin !1B CLASSIFICATION #superfamily S-100 protein; calmodulin repeat homology KEYWORDS calcium binding; cytokine; EF hand; heterodimer; homodimer; !1inflammation FEATURE !$2-89 #product calgranulin A #status experimental #label !8MAT\ !$7-41 #domain calmodulin repeat homology #label EF1\ !$46-78 #domain calmodulin repeat homology #label EF2 SUMMARY #length 89 #molecular-weight 10295 #checksum 5328 SEQUENCE /// ENTRY B31848 #type complete TITLE calgranulin B [validated] - human ALTERNATE_NAMES calcium-binding protein MRP-14; cystic fibrosis-associated antigen (CF Ag) heavy chain; leukocyte L1 complex heavy chain; macrophage migration inhibitory factor-related 14K protein (MRP-14); MIF-related 14K protein; S-100 calcium-binding protein A9 (S100A9) ORGANISM #formal_name Homo sapiens #common_name man DATE 21-May-1990 #sequence_revision 23-May-1997 #text_change 08-Dec-2000 ACCESSIONS B31848; S00667; A33819; B60911; B61082; D54327 REFERENCE A93102 !$#authors Lagasse, E.; Clerc, R.G. !$#journal Mol. Cell. Biol. (1988) 8:2402-2410 !$#title Cloning and expression of two human genes encoding !1calcium-binding proteins that are regulated during myeloid !1differentiation. !$#cross-references MUID:88302148; PMID:3405210 !$#accession B31848 !'##molecule_type DNA !'##residues 1-114 ##label LAG !'##cross-references GB:M21064; NID:g188689; PIDN:AAA36326.1; !1PID:g386958 REFERENCE S00667 !$#authors Odink, K.; Cerletti, N.; Brueggen, J.; Clerc, R.G.; Tarcsay, !1L.; Zwadlo, G.; Gerhards, G.; Schlegel, R.; Sorg, C. !$#journal Nature (1987) 330:80-82 !$#title Two calcium-binding proteins in infiltrate macrophages of !1rheumatoid arthritis. !$#cross-references MUID:88039099; PMID:3313057 !$#accession S00667 !'##molecule_type mRNA !'##residues 1-114 ##label ODI !'##cross-references EMBL:X06233; NID:g34770; PIDN:CAA29579.1; !1PID:g34771 !'##note parts of this sequence were confirmed by protein sequencing REFERENCE A33819 !$#authors Murao, S.; Collart, F.R.; Huberman, E. !$#journal J. Biol. Chem. (1989) 264:8356-8360 !$#title A protein containing the cystic fibrosis antigen is an !1inhibitor of protein kinases. !$#cross-references MUID:89255276; PMID:2656677 !$#accession A33819 !'##molecule_type mRNA !'##residues 1-114 ##label MUR !'##cross-references GB:M26311; NID:g862619; PIDN:AAA68480.1; !1PID:g516621 !'##note part of this sequence was confirmed by protein sequencing; the !1amino end of the mature protein is blocked REFERENCE A60911 !$#authors Andersson, K.B.; Sletten, K.; Berntzen, H.B.; Dale, I.; !1Brandtzaeg, P.; Jellum, E.; Fagerhol, M.K. !$#journal Scand. J. Immunol. (1988) 28:241-245 !$#title The leucocyte L1 protein: identity with the cystic fibrosis !1antigen and the calcium-binding MRP-8 and MRP-14 macrophage !1components. !$#cross-references MUID:88321575; PMID:3413449 !$#accession B60911 !'##molecule_type protein !'##residues 39-42,'X',44-50;64-77,'X',79;84,'X',86-90,'X',92-94,'X', !196-98 ##label AND REFERENCE A61082 !$#authors Tobe, T.; Murakami, K.; Tomita, M.; Nozawa, R. !$#journal Chem. Pharm. Bull. (1989) 37:1576-1580 !$#title Amino acid sequences of 60B8 antigens induced in HL-60 cells !1by 1,25-dihydroxyvitamin D-3. The antigens are identical !1with macrophage-related protein-14 and -8. !$#cross-references MUID:89376638; PMID:2776242 !$#accession B61082 !'##molecule_type protein !'##residues 5-77;80-90,'A',92-114 ##label TOB !'##note the blocked amino end of the mature protein is identified as !12-Thr; residue 91-His is misidentified as PTH-Ala but !1confirmed by peptide composition REFERENCE A54327 !$#authors Madsen, P.; Rasmussen, H.H.; Leffers, H.; Honore, B.; !1Dejgaard, K.; Olsen, E.; Kiil, J.; Walbum, E.; Andersen, !1A.H.; Basse, B.; Lauridsen, J.B.; Ratz, G.P.; Celis, A.; !1Vandekerckhove, J.; Celis, J.E. !$#journal J. Invest. Dermatol. (1991) 97:701-712 !$#title Molecular cloning, occurrence, and expression of a novel !1partially secreted protein "psoriasin" that is highly !1up-regulated in psoriatic skin. !$#cross-references MUID:92043866; PMID:1940442 !$#accession D54327 !'##molecule_type protein !'##residues 11-19;26-38;94-105,'X',107 ##label MAD !'##note in several peptide samples no PTH was detected for 95-His but !1in one peptide PTH was detected for 105-His COMMENT This protein appears to be expressed only in cells of !1myeloid origin actively involved in acute and chronic !1inflammation. It inhibits some serine/threonine protein !1kinases. COMMENT The presence of 3'-methylhistidine at position 105, !1corresponding to 107-His in mouse calgranulin B, does not !1appear to be supported. GENETICS !$#gene GDB:S100A9; 60B8AG; CAGB; CFAG; LIAG; MAC387; MIF; MRP14; !1NIF; P14 !'##cross-references GDB:120570; OMIM:123886 !$#map_position 1q21-1q21 !$#introns 50/3 !$#note the first intron occurs before the initiator codon COMPLEX heterodimer and higher complexes with calgranulin A (see !1PIR:BCHUCF) CLASSIFICATION #superfamily S-100 protein; calmodulin repeat homology KEYWORDS blocked amino end; calcium binding; EF hand; heterodimer; !1inflammation; phosphoprotein FEATURE !$2-114 #product calgranulin B #status experimental #label !8MAT\ !$10-44 #domain calmodulin repeat homology #label EF1\ !$54-86 #domain calmodulin repeat homology #label EF2\ !$2 #modified_site blocked amino end (Thr) (in mature !8form) (probably acetylated) #status experimental\ !$113 #binding_site phosphate (Thr) (covalent) #status !8predicted SUMMARY #length 114 #molecular-weight 13242 #checksum 7481 SEQUENCE /// ENTRY S68242 #type complete TITLE calgranulin B - mouse ALTERNATE_NAMES calcium-binding protein MRP-14; macrophage migration inhibitory factor-related 14K protein (MRP-14); MIF-related 14K protein ORGANISM #formal_name Mus musculus #common_name house mouse DATE 06-Sep-1996 #sequence_revision 23-May-1997 #text_change 22-Jun-1999 ACCESSIONS S68242; S68272 REFERENCE S68242 !$#authors Lagasse, E.; Weissman, I.L. !$#submission submitted to the EMBL Data Library, February 1992 !$#description Mouse MRP8 and MRP14, two intracellular calcium-binding !1proteins associated with the development of the Myeloid !1lineage. !$#accession S68242 !'##molecule_type mRNA !'##residues 1-113 ##label LAG !'##cross-references EMBL:M83219; NID:g199807; PIDN:AAB07228.1; !1PID:g199808 REFERENCE S68272 !$#authors Raftery, M.J.; Harrison, C.A.; Alewood, P.; Jones, A.; !1Geczy, C.L. !$#journal Biochem. J. (1996) 316:285-293 !$#title Isolation of the murine S100 protein MRP14 (14 kDa !1migration-inhibitory-factor-related protein) from activated !1spleen cells: characterization of post-translational !1modifications and zinc binding. !$#cross-references MUID:96235204; PMID:8645219 !$#accession S68272 !'##molecule_type protein !'##residues 2-10;95-109 ##label RAF !'##note 107-His is identified as 3'-methylhistidine; the authors' !1source for the reference standard acknowledges that their !1name, 1'-methylhistidine, is a misnomer for the IUPAC !1standard name 3'-methylhistidine GENETICS !$#gene MRP14 COMPLEX heterodimer and higher complexes with calgranulin A CLASSIFICATION #superfamily S-100 protein; calmodulin repeat homology KEYWORDS acetylated amino end; calcium binding; EF hand; heterodimer; !1inflammation; methylated amino acid; phosphoprotein; zinc FEATURE !$2-113 #product calgranulin B #status predicted #label MAT\ !$11-45 #domain calmodulin repeat homology #label EF1\ !$55-87 #domain calmodulin repeat homology #label EF2\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental\ !$80-91 #disulfide_bonds #status experimental\ !$103,105,107 #binding_site zinc (His) #status predicted\ !$107 #modified_site 3'-methylhistidine (His) #status !8experimental SUMMARY #length 113 #molecular-weight 13049 #checksum 2342 SEQUENCE /// ENTRY JN0686 #type complete TITLE calgranulin B - rat ALTERNATE_NAMES calcium-binding protein MRP-14; macrophage migration inhibitory factor-related 14K protein (MRP-14); MIF-related 14K protein ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 03-May-1994 #sequence_revision 23-May-1997 #text_change 22-Jun-1999 ACCESSIONS JN0686 REFERENCE JN0685 !$#authors Imamichi, T.; Uchida, I.; Wahl, S.M.; McCartney-Francis, N. !$#journal Biochem. Biophys. Res. Commun. (1993) 194:819-825 !$#title Expression and cloning of migration inhibitory !1factor-related protein (MRP)8 and MRP14 in !1arthritis-susceptible rats. !$#cross-references MUID:93343942; PMID:8343166 !$#accession JN0686 !'##molecule_type mRNA !'##residues 1-113 ##label IMA !'##cross-references GB:L18948; NID:g488156; PIDN:AAA18214.1; !1PID:g488157 GENETICS !$#gene MRP14 COMPLEX heterodimer and higher complexes with calgranulin A CLASSIFICATION #superfamily S-100 protein; calmodulin repeat homology KEYWORDS acetylated amino end; calcium binding; EF hand; heterodimer; !1inflammation; phosphoprotein FEATURE !$2-113 #product calgranulin B #status predicted #label MAT\ !$11-45 #domain calmodulin repeat homology #label EF1\ !$55-87 #domain calmodulin repeat homology #label EF2\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status predicted\ !$80-91 #disulfide_bonds #status predicted SUMMARY #length 113 #molecular-weight 13214 #checksum 2785 SEQUENCE /// ENTRY A42628 #type fragment TITLE calgranulin B - bovine (fragment) ALTERNATE_NAMES calcium-binding protein MRP-14; macrophage migration inhibitory factor-related 14K protein (MRP-14); MIF-related 14K protein; neutrophil cytosolic 23K phosphoprotein; nuclear protein 2 ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Sep-1993 #sequence_revision 23-May-1997 #text_change 23-May-1997 ACCESSIONS B22309; A42628 REFERENCE A22309 !$#authors Tang, T.K.; Hong, T.M.; Lin, C.Y.; Lai, M.L.; Liu, C.H.L.; !1Lo, H.J.; Wang, M.E.; Chen, L.B.; Chen, W.T.; Chien, S.; Ip, !1W.; Lin, D.C. !$#submission submitted to the Protein Sequence Database, July 1992 !$#accession B22309 !'##status preliminary !'##molecule_type protein !'##residues 1-122 ##label TAN REFERENCE A42628 !$#authors Dianoux, A.C.; Stasia, M.J.; Garin, J.; Gagnon, J.; Vignais, !1P.V. !$#journal Biochemistry (1992) 31:5898-5905 !$#title The 23-kilodalton protein, a substrate of protein kinase C, !1in bovine neutrophil cytosol is a member of the S100 family. !$#cross-references MUID:92304974; PMID:1610833 !$#accession A42628 !'##molecule_type protein !'##residues 4-32,'F',34-56 ##label DIA COMPLEX heterodimer and higher complexes with calgranulin A CLASSIFICATION #superfamily S-100 protein; calmodulin repeat homology KEYWORDS blocked amino end; calcium binding; EF hand; heterodimer; !1inflammation; phosphoprotein FEATURE !$6-40 #domain calmodulin repeat homology #label EF1\ !$50-82 #domain calmodulin repeat homology #label EF2 SUMMARY #length 122 #checksum 2297 SEQUENCE /// ENTRY A54327 #type complete TITLE psoriasin [validated] - human ALTERNATE_NAMES S-100 calcium-binding protein A7 (S100A7) ORGANISM #formal_name Homo sapiens #common_name man DATE 09-Sep-1994 #sequence_revision 23-May-1997 #text_change 08-Dec-2000 ACCESSIONS A54327; E54327; A58578 REFERENCE A54327 !$#authors Madsen, P.; Rasmussen, H.H.; Leffers, H.; Honore, B.; !1Dejgaard, K.; Olsen, E.; Kiil, J.; Walbum, E.; Andersen, !1A.H.; Basse, B.; Lauridsen, J.B.; Ratz, G.P.; Celis, A.; !1Vandekerckhove, J.; Celis, J.E. !$#journal J. Invest. Dermatol. (1991) 97:701-712 !$#title Molecular cloning, occurrence, and expression of a novel !1partially secreted protein "psoriasin" that is highly !1up-regulated in psoriatic skin. !$#cross-references MUID:92043866; PMID:1940442 !$#accession A54327 !'##molecule_type mRNA !'##residues 1-101 ##label MAD1 !'##cross-references GB:M86757; NID:g190667; PIDN:AAA60210.1; !1PID:g190668 !$#accession E54327 !'##molecule_type protein !'##residues 9-19;38-46,'X',48;50-61;69-87 ##label MAD2 REFERENCE A58578 !$#authors Burgisser, D.M.; Siegenthaler, G.; Kuster, T.; Hellman, U.; !1Hunziker, P.; Birchler, N.; Heizmann, C.W. !$#journal Biochem. Biophys. Res. Commun. (1995) 217:257-263 !$#cross-references MUID:96095666; PMID:8526920 !$#accession A58578 !'##molecule_type protein !'##residues 2-101 ##label BUR COMMENT This protein is expressed in fetal and squamous stratified !1epithelial cells and may play a role in skin inflammatory !1response. GENETICS !$#gene GDB:S100A7; PSOR1 !'##cross-references GDB:129731; OMIM:600353 !$#map_position 1q21-1q21 CLASSIFICATION #superfamily S-100 protein; calmodulin repeat homology KEYWORDS acetylated amino end; calcium binding; EF hand; !1inflammation; skin FEATURE !$2-101 #product psoriasin #status experimental #label MAT\ !$8-39 #domain calmodulin repeat homology #label EF1\ !$50-82 #domain calmodulin repeat homology #label EF2\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental SUMMARY #length 101 #molecular-weight 11457 #checksum 8005 SEQUENCE /// ENTRY A26615 #type complete TITLE calpain inhibitor precursor - rabbit CONTAINS calcium-activated neutral proteinase inhibitor (CANPI) ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 24-Nov-1999 ACCESSIONS A26615; A27526; A26904 REFERENCE A26615 !$#authors Emori, Y.; Kawasaki, H.; Imajoh, S.; Imahori, K.; Suzuki, K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:3590-3594 !$#title Endogenous inhibitor for calcium-dependent cysteine protease !1contains four internal repeats that could be responsible for !1its multiple reactive sites. !$#cross-references MUID:87231863; PMID:3035539 !$#accession A26615 !'##molecule_type mRNA !'##residues 1-718 ##label EMO !'##cross-references GB:M16476; NID:g164852; PIDN:AAA31186.1; !1PID:g164853 REFERENCE A27526 !$#authors Imajoh, S.; Kawasaki, H.; Emori, Y.; Ishiura, S.; Minami, !1Y.; Sugita, H.; Imahori, K.; Suzuki, K. !$#journal FEBS Lett. (1987) 215:274-278 !$#title A fragment of an endogenous inhibitor produced in !1Escherichia coli for calcium-activated neutral protease !1(CANP) retains an inhibitory activity. !$#cross-references MUID:87219099; PMID:3034666 !$#accession A27526 !'##molecule_type protein !'##residues 80-90 ##label IMA !'##experimental_source liver REFERENCE A26904 !$#authors Imajoh, S.; Kawasaki, H.; Emori, Y.; Suzuki, K. !$#journal Biochem. Biophys. Res. Commun. (1987) 146:630-637 !$#title Calcium-activated neutral protease inhibitor from rabbit !1erythrocytes lacks the N-terminal region of the liver !1inhibitor but retains three inhibitory units. !$#cross-references MUID:87298487; PMID:3039985 !$#accession A26904 !'##molecule_type protein !'##residues 290-718 ##label IM2 CLASSIFICATION #superfamily calpain inhibitor KEYWORDS blocked amino end; cysteine proteinase inhibitor; !1duplication FEATURE !$1-79 #domain signal sequence and propeptide #status !8predicted #label SIP\ !$80-718 #product calpain inhibitor, hepatic form #status !8experimental #label MHF\ !$290-718 #product calcium-activated neutral proteinase !8inhibitor, erythrocyte form #status predicted #label !8MEF\ !$290 #modified_site blocked amino end (Ser) (in mature !8form) #status experimental SUMMARY #length 718 #molecular-weight 76965 #checksum 8980 SEQUENCE /// ENTRY A31797 #type complete TITLE Spec-related protein (clone LpS1) - sea urchin (Lytechinus pictus) ORGANISM #formal_name Lytechinus pictus #common_name painted urchin DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A31797 REFERENCE A31797 !$#authors Xiang, M.; Bedard, P.A.; Wessel, G.; Filion, M.; Brandhorst, !1B.P.; Klein, W.H. !$#journal J. Biol. Chem. (1988) 263:17173-17180 !$#title Tandem duplication and divergence of a sea urchin protein !1belonging to the troponin C superfamily. !$#cross-references MUID:89034224; PMID:3182842 !$#accession A31797 !'##molecule_type mRNA !'##residues 1-317 ##label XIA !'##cross-references GB:J04068; NID:g161331; PIDN:AAA30007.1; !1PID:g161332 CLASSIFICATION #superfamily spec-related protein LpS1; calmodulin repeat !1homology KEYWORDS calcium binding; EF hand FEATURE !$12-42 #domain calmodulin repeat homology #label EF1\ !$43-75 #domain calmodulin repeat homology #label EF2\ !$81-113 #domain calmodulin repeat homology #label EF3\ !$117-149 #domain calmodulin repeat homology #label EF4\ !$161-193 #domain calmodulin repeat homology #label EF5\ !$196-228 #domain calmodulin repeat homology #label EF6\ !$229-260 #domain calmodulin repeat homology #label EF7\ !$265-297 #domain calmodulin repeat homology #label EF8 SUMMARY #length 317 #molecular-weight 36706 #checksum 3435 SEQUENCE /// ENTRY A37047 #type complete TITLE calreticulin precursor - human ALTERNATE_NAMES 52K ribonucleoprotein autoantigen Ro/SS-A; 60K integrin-binding protein; granule-associated 60-kD protein ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 18-Feb-2000 ACCESSIONS A42330; A37047; A46452; A28812; PH1525; A40346; S11475; !1T45075 REFERENCE A42330 !$#authors McCauliffe, D.P.; Yang, Y.S.; Wilson, J.; Sontheimer, R.D.; !1Capra, J.D. !$#journal J. Biol. Chem. (1992) 267:2557-2562 !$#title The 5'-flanking region of the human calreticulin gene shares !1homology with the human GRP78, GRP94, and protein disulfide !1isomerase promoters. !$#cross-references MUID:92129342; PMID:1733953 !$#accession A42330 !'##molecule_type DNA !'##residues 1-417 ##label MC2 !'##note sequence extracted from NCBI backbone (NCBIN:78537, !1NCBIP:78536) REFERENCE A37047 !$#authors McCauliffe, D.P.; Lux, F.A.; Lieu, T.S.; Sanz, I.; Hanke, !1J.; Newkirk, M.M.; Bachinski, L.L.; Itoh, Y.; Siciliano, !1M.J.; Reichlin, M.; Sontheimer, R.D.; Capra, J.D. !$#journal J. Clin. Invest. (1990) 85:1379-1391 !$#title Molecular cloning, expression, and chromosome 19 !1localization of a human Ro/SS-A autoantigen. !$#cross-references MUID:90237213; PMID:2332496 !$#accession A37047 !'##molecule_type mRNA !'##residues 1-417 ##label MCC !'##cross-references GB:M32294; NID:g337486; PIDN:AAA36582.1; !1PID:g337487 !'##note the authors translated the codon GTA for residue 349 as Tyr REFERENCE A46452 !$#authors Rokeach, L.A.; Haselby, J.A.; Meilof, J.F.; Smeenk, R.J.; !1Unnasch, T.R.; Greene, B.M.; Hoch, S.O. !$#journal J. Immunol. (1991) 147:3031-3039 !$#title Characterization of the autoantigen calreticulin. !$#cross-references MUID:92013129; PMID:1919005 !$#accession A46452 !'##molecule_type mRNA !'##residues 1-417 ##label ROK !'##cross-references GB:M84739; NID:g179881; PIDN:AAA51916.1; !1PID:g179882 !'##note sequence extracted from NCBI backbone (NCBIN:60749, !1NCBIP:60750) REFERENCE A28812 !$#authors Lieu, T.S.; Newkirk, M.M.; Capra, J.D.; Sontheimer, R.D. !$#journal J. Clin. Invest. (1988) 82:96-101 !$#title Molecular characterization of human Ro/SS-A antigen. Amino !1terminal sequence of the protein moiety of human Ro/SS-A !1antigen and immunological activity of a corresponding !1synthetic peptide. !$#cross-references MUID:88273610; PMID:3260607 !$#accession A28812 !'##molecule_type protein !'##residues 18-41 ##label LIE !'##note 18-Ala was also found REFERENCE PH1525 !$#authors Dupuis, M.; Schaerer, E.; Krause, K.H.; Tschopp, J. !$#journal J. Exp. Med. (1993) 177:1-7 !$#title The calcium-binding protein calreticulin is a major !1constituent of lytic granules in cytolytic T lymphocytes. !$#cross-references MUID:93115648; PMID:8418194 !$#accession PH1525 !'##molecule_type protein !'##residues 18-27 ##label DUP !'##experimental_source LAK cell REFERENCE A40346 !$#authors Rojiani, M.V.; Finlay, B.B.; Gray, V.; Dedhar, S. !$#journal Biochemistry (1991) 30:9859-9866 !$#title In vitro interaction of a polypeptide homologous to human !1Ro/SS-A antigen (calreticulin) with a highly conserved amino !1acid sequence in the cytoplasmic domain of integrin alpha !1subunits. !$#cross-references MUID:92002034; PMID:1911778 !$#accession A40346 !'##molecule_type protein !'##residues 18-34,'R' ##label ROJ REFERENCE S11475 !$#authors Krause, K.H.; Simmerman, H.K.B.; Jones, L.R.; Campbell, K.P. !$#journal Biochem. J. (1990) 270:545-548 !$#title Sequence similarity of calreticulin with a Ca(2+)-binding !1protein that co-purifies with an Ins(1,4,5)P(3)-sensitive Ca !1(2+) store in HL-60 cells. !$#cross-references MUID:90380058; PMID:2400400 !$#accession S11475 !'##molecule_type protein !'##residues 18-32 ##label KRA REFERENCE Z22906 !$#authors Lamerdin, J.; McCready, P.; Stilwagen, S.; Ramirez, M.; !1Carrano, A. !$#submission submitted to the EMBL Data Library, November 1996 !$#description Characterization by genomic sequence analysis of a gene-rich !1111 kb region of 19p13.2 containing the human DNA repair !1gene, RAD23A. !$#accession T45075 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-417 ##label LAM !'##cross-references EMBL:AD000092; PIDN:AAB51176.1 !'##experimental_source cell line 5HL2-B; fibroblast COMMENT Autoantibodies specific for this protein are found in !1Sjogren's syndrome and several systemic lupus !1erythematosus-related disorders. GENETICS !$#gene GDB:CALR !'##cross-references GDB:125179; OMIM:109091 !$#map_position 19p13.3-19p13.2 !$#introns 31/1; 65/1; 133/1; 164/3; 234/3; 272/3; 320/3; 351/3 !$#note CRTC CLASSIFICATION #superfamily calreticulin KEYWORDS calcium binding; integrin binding FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-417 #product calreticulin #status predicted #label MAT\ !$414-417 #region endoplasmic reticulum retention signal SUMMARY #length 417 #molecular-weight 48141 #checksum 8726 SEQUENCE /// ENTRY S06763 #type complete TITLE calreticulin precursor - mouse ALTERNATE_NAMES 55K calcium-binding reticuloplasmin; calregulin ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S06763; JC1444; PC1233; A57498 REFERENCE S06763 !$#authors Smith, M.J.; Koch, G.L.E. !$#journal EMBO J. (1989) 8:3581-3586 !$#title Multiple zones in the sequence of calreticulin (CRP55, !1calregulin, HACBP), a major calcium binding ER/SR protein. !$#cross-references MUID:90059955; PMID:2583110 !$#accession S06763 !'##molecule_type DNA !'##residues 1-416 ##label SMI !'##cross-references EMBL:X14926; NID:g50567; PIDN:CAA33053.1; !1PID:g50568 REFERENCE JC1444 !$#authors Mazzarella, R.A.; Gold, P.; Cunningham, M.; Green, M. !$#journal Gene (1992) 120:217-225 !$#title Determination of the sequence of an expressible cDNA clone !1encoding ERp60/calregulin by the use of a novel nested set !1method. !$#cross-references MUID:93013037; PMID:1398135 !$#accession JC1444 !'##molecule_type mRNA !'##residues 1-416 ##label MAZ !'##cross-references GB:M92988; NID:g193084; PIDN:AAA37569.1; !1PID:g193085 !$#accession PC1233 !'##molecule_type protein !'##residues 18-41 ##label MA2 REFERENCE A57498 !$#authors White, T.K.; Zhu, Q.; Tanzer, M.L. !$#journal J. Biol. Chem. (1995) 270:15926-15929 !$#title Cell surface calreticulin is a putative mannoside lectin !1which triggers mouse melanoma cell spreading. !$#cross-references MUID:95332280; PMID:7608143 !$#accession A57498 !'##status preliminary !'##molecule_type protein !'##residues 74-80;142-151;186-193 ##label WHI CLASSIFICATION #superfamily calreticulin KEYWORDS calcium binding FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-416 #product calregulin #status experimental #label MAT\ !$413-416 #region endoplasmic reticulum retention signal SUMMARY #length 416 #molecular-weight 47994 #checksum 5745 SEQUENCE /// ENTRY A34154 #type complete TITLE calreticulin precursor, skeletal muscle - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A34154; S13047 REFERENCE A34154 !$#authors Fliegel, L.; Burns, K.; MacLennan, D.H.; Reithmeier, R.A.F.; !1Michalak, M. !$#journal J. Biol. Chem. (1989) 264:21522-21528 !$#title Molecular cloning of the high affinity calcium-binding !1protein (calreticulin) of skeletal muscle sarcoplasmic !1reticulum. !$#cross-references MUID:90094320; PMID:2600080 !$#accession A34154 !'##status preliminary !'##molecule_type mRNA !'##residues 1-418 ##label FLI !'##cross-references GB:J05138; NID:g164858; PIDN:AAA31188.1; !1PID:g164859 REFERENCE S13045 !$#authors Treves, S.; de Mattei, M.; Lanfredi, M.; Villa, A.; Green, !1N.M.; MacLennan, D.H.; Meldolesi, J.; Pozzan, T. !$#journal Biochem. J. (1990) 271:473-480 !$#title Calreticulin is a candidate for a calsequestrin-like !1function in Ca(2+)-storage compartments (calciosomes) of !1liver and brain. !$#cross-references MUID:91054414; PMID:2241926 !$#accession S13047 !'##molecule_type protein !'##residues 19-32 ##label TRE CLASSIFICATION #superfamily calreticulin KEYWORDS skeletal muscle FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$415-418 #region endoplasmic reticulum retention signal SUMMARY #length 418 #molecular-weight 48274 #checksum 8862 SEQUENCE /// ENTRY JH0795 #type complete TITLE calreticulin precursor - California sea hare ALTERNATE_NAMES protein 407 ORGANISM #formal_name Aplysia californica #common_name California sea hare DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JH0795; B31409; F60977 REFERENCE JH0795 !$#authors Kennedy, T.E.; Kuhl, D.; Barzilai, A.; Sweatt, J.D.; Kandel, !1E.R. !$#journal Neuron (1992) 9:1013-1024 !$#title Long-term sensitization training in aplysia leads to an !1increase in calreticulin, a major presynaptic !1calcium-binding protein. !$#cross-references MUID:93098937; PMID:1463604 !$#accession JH0795 !'##molecule_type mRNA !'##residues 1-405 ##label KEN !'##cross-references GB:S51239; NID:g262053; PIDN:AAB24569.1; !1PID:g262054 !'##experimental_source abdominal ganglion and antral nervous system REFERENCE A94207 !$#authors Kennedy, T.E.; Gawinowicz, M.A.; Barzilai, A.; Kandel, E.R.; !1Sweatt, J.D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:7008-7012 !$#title Sequencing of proteins from two-dimensional gels by using in !1situ digestion and transfer of peptides to polyvinylidene !1difluoride membranes: application to proteins associated !1with sensitization in Aplysia. !$#cross-references MUID:88320566; PMID:3413132 !$#accession B31409 !'##molecule_type protein !'##residues 'X',17-28,'X',30-31 ##label KE2 REFERENCE A60977 !$#authors Sweatt, J.D.; Kennedy, T.E.; Wager-Smith, K.; Gawinowicz, !1M.A.; Barzilai, A.; Karl, K.A.; Kandel, E.R. !$#journal Electrophoresis (1989) 10:152-157 !$#title Development of a database of amino acid sequences for !1proteins identified and isolated on two-dimensional !1polyacrylamide gels. !$#cross-references MUID:89276264; PMID:2731514 !$#accession F60977 !'##molecule_type protein !'##residues 'X',17-28,'X',30-31 ##label SWE CLASSIFICATION #superfamily calreticulin KEYWORDS calcium binding; endoplasmic reticulum FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-405 #product calreticulin #status experimental #label !8MAT\ !$402-405 #region endoplasmic reticulum retention signal SUMMARY #length 405 #molecular-weight 46738 #checksum 2378 SEQUENCE /// ENTRY A48573 #type complete TITLE calreticulin autoantigen homolog precursor - fluke (Schistosoma mansoni) ORGANISM #formal_name Schistosoma mansoni DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A48573 REFERENCE A48573 !$#authors Khalife, J.; Trottein, F.; Schacht, A.M.; Godin, C.; Pierce, !1R.J.; Capron, A. !$#journal Mol. Biochem. Parasitol. (1993) 57:193-202 !$#title Cloning of the gene encoding a Schistosoma mansoni antigen !1homologous to human Ro/SS-A autoantigen. !$#cross-references MUID:93165070; PMID:8433712 !$#accession A48573 !'##status preliminary !'##molecule_type mRNA !'##residues 1-393 ##label KHA !'##cross-references GB:M93097; NID:g160928 !'##note sequence inconsistent with the nucleotide translation !'##note sequence extracted from NCBI backbone (NCBIN:125085, !1NCBIP:125086) CLASSIFICATION #superfamily calreticulin FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$390-393 #region endoplasmic reticulum retention signal SUMMARY #length 393 #molecular-weight 45386 #checksum 6104 SEQUENCE /// ENTRY A37273 #type complete TITLE calnexin precursor - dog ALTERNATE_NAMES band VII ORGANISM #formal_name Canis lupus familiaris #common_name dog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A37273; S17366; A45224 REFERENCE A37273 !$#authors Wada, I.; Rindress, D.; Cameron, P.H.; Ou, W.J.; Doherty II, !1J.J.; Louvard, D.; Bell, A.W.; Dignard, D.; Thomas, D.Y.; !1Bergeron, J.J.M. !$#journal J. Biol. Chem. (1991) 266:19599-19610 !$#title SSRalpha and associated calnexin are major calcium binding !1proteins of the endoplasmic reticulum membrane. !$#cross-references MUID:92011761; PMID:1918067 !$#accession A37273 !'##molecule_type mRNA !'##residues 1-593 ##label WAD !'##cross-references GB:X53616 REFERENCE S15510 !$#authors Wada, I.; Bell, A.W.; Dignard, D.; Thomas, D.Y.; Bergeron, !1J.J.M. !$#submission submitted to the EMBL Data Library, June 1990 !$#description Primary strucure of a heterooligomeric complex of !1phosphoglycoproteins of the ER. !$#accession S17366 !'##molecule_type mRNA !'##residues 1-418,'L',420-593 ##label WA2 !'##cross-references EMBL:X53616 REFERENCE A45224 !$#authors Cala, S.E.; Ulbright, C.; Kelley, J.S.; Jones, L.R. !$#journal J. Biol. Chem. (1993) 268:2969-2975 !$#title Purification of a 90-kDa protein (Band VII) from cardiac !1sarcoplasmic reticulum. Identification as calnexin and !1localization of casein kinase II phosphorylation sites. !$#cross-references MUID:93155121; PMID:8428970 !$#contents cardiac sarcoplasmic reticulum !$#accession A45224 !'##molecule_type protein !'##residues 47-56;63-66,'T', !168-72;79-100;120-135;172-186;201-206;229-234;236-274; !1276-301;371-380;447-456;461-470;509-515;517-526;553-561; !1575-583 ##label CAL !'##note sequence extracted from NCBI backbone (NCBIP:124276, !1NCBIP:124278, NCBIP:124280, NCBIP:124282, NCBIP:124284, !1NCBIP:124286, NCBIP:124288, NCBIP:124290, NCBIP:124292, !1NCBIP:124294, NCBIP:124297, NCBIP:124300, NCBIP:124303, !1NCBIP:124305, NCBIP:124307, NCBIP:124309) CLASSIFICATION #superfamily calnexin KEYWORDS molecular chaperone; transmembrane protein SUMMARY #length 593 #molecular-weight 67589 #checksum 6392 SEQUENCE /// ENTRY AQUT17 #type complete TITLE flagellar calcium-binding protein TB17 - Trypanosoma brucei ORGANISM #formal_name Trypanosoma brucei DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 22-Jun-1999 ACCESSIONS S10515 REFERENCE S10515 !$#authors Lee, M.G.S.; Chen, J.; Ho, A.W.M.; d'Alesandro, P.A.; van !1der Ploeg, L.H.T. !$#journal Nucleic Acids Res. (1990) 18:4252 !$#title A putative flagellar Ca2+-binding protein of the flagellum !1of trypanosomatid protozoan parasites. !$#cross-references MUID:90332427; PMID:2198539 !$#accession S10515 !'##molecule_type mRNA !'##residues 1-233 ##label LEE !'##cross-references EMBL:X53464; NID:g10540; PIDN:CAA37558.1; !1PID:g10541 !'##note the authors translated the codon TCA for residue 4 as Ala, CGG !1for residue 30 as Gly, CGT for residue 36 as Gly, ATC for !1residue 138 as Met, CAC for residue 153 as Gln, and AAG for !1residue 156 as Arg CLASSIFICATION #superfamily flagellar calcium-binding protein; calmodulin !1repeat homology KEYWORDS calcium binding; duplication; EF hand; flagellum FEATURE !$48-80 #domain calmodulin repeat homology #label EF1\ !$97-129 #domain calmodulin repeat homology #label EF2\ !$130-162 #domain calmodulin repeat homology #label EF3\ !$167-199 #domain calmodulin repeat homology #label EF4 SUMMARY #length 233 #molecular-weight 25492 #checksum 2801 SEQUENCE /// ENTRY A34311 #type complete TITLE flagellar calcium-binding protein 1F8 - Trypanosoma cruzi ORGANISM #formal_name Trypanosoma cruzi DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A34311; A24069 REFERENCE A34311 !$#authors Engman, D.M.; Krause, K.H.; Blumin, J.H.; Kim, K.S.; !1Kirchhoff, L.V.; Donelson, J.E. !$#journal J. Biol. Chem. (1989) 264:18627-18631 !$#title A novel flagellar Ca(2+)-binding protein in trypanosomes. !$#cross-references MUID:90036966; PMID:2681200 !$#accession A34311 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-211 ##label ENG !'##note the protein binds 1-2 calcium ions with high affinity REFERENCE A24069 !$#authors Gonzalez, A.; Lerner, T.J.; Huecas, M.; Sosa-Pineda, B.; !1Nogueira, N.; Lizardi, P.M. !$#journal Nucleic Acids Res. (1985) 13:5789-5804 !$#cross-references MUID:85297776; PMID:2412209 !$#accession A24069 !'##molecule_type DNA !'##residues 1-211 ##label GON !'##cross-references GB:X02838; NID:g10597; PIDN:CAA26599.1; PID:g10598 CLASSIFICATION #superfamily flagellar calcium-binding protein; calmodulin !1repeat homology KEYWORDS calcium binding; duplication; EF hand; flagellum FEATURE !$45-77 #domain calmodulin repeat homology #label EF1\ !$94-126 #domain calmodulin repeat homology #label EF2\ !$127-159 #domain calmodulin repeat homology #label EF3\ !$164-196 #domain calmodulin repeat homology #label EF4 SUMMARY #length 211 #molecular-weight 23736 #checksum 9013 SEQUENCE /// ENTRY LUHU #type complete TITLE annexin I - human ALTERNATE_NAMES calpactin II; lipocortin I; p35; phospholipase A2 inhibitory protein ORGANISM #formal_name Homo sapiens #common_name man DATE 04-Dec-1986 #sequence_revision 30-Sep-1992 #text_change 22-Jun-1999 ACCESSIONS A03080; A28641; A38842; A34459; S07909; S28846 REFERENCE A03080 !$#authors Wallner, B.P.; Mattaliano, R.J.; Hession, C.; Cate, R.L.; !1Tizard, R.; Sinclair, L.K.; Foeller, C.; Chow, E.P.; !1Browning, J.L.; Ramachandran, K.L.; Pepinsky, R.B. !$#journal Nature (1986) 320:77-81 !$#title Cloning and expression of human lipocortin, a phospholipase !1A2 inhibitor with potential anti-inflammatory activity. !$#cross-references MUID:86146879; PMID:2936963 !$#accession A03080 !'##molecule_type mRNA !'##residues 1-346 ##label WAL !'##cross-references EMBL:X05908; NID:g34387; PIDN:CAA29338.1; !1PID:g34388 REFERENCE A28641 !$#authors Varticovski, L.; Chahwala, S.B.; Whitman, M.; Cantley, L.; !1Schindler, D.; Chow, E.P.; Sinclair, L.K.; Pepinsky, R.B. !$#journal Biochemistry (1988) 27:3682-3690 !$#title Location of sites in human lipocortin I that are !1phosphorylated by protein tyrosine kinases and protein !1kinases A and C. !$#cross-references MUID:88309771; PMID:2457390 !$#accession A28641 !'##molecule_type protein !'##residues 10-26;214-233 ##label VAR REFERENCE A38842 !$#authors Pepinsky, R.B.; Sinclair, L.K.; Chow, E.P.; O'Brine-Greco, !1B. !$#journal Biochem. J. (1989) 263:97-103 !$#title A dimeric form of lipocortin-1 in human placenta. !$#cross-references MUID:90104259; PMID:2532504 !$#accession A38842 !'##molecule_type protein !'##residues 10-18,'X',20-26;30-49;59-71;129-144;215-228;318-323,'X', !1325-332 ##label PEP !'##experimental_source placenta !'##note in placenta, approximately 20% of annexin I was observed as a !1dimer; the authors propose that a cross-link may be !1generated between 19-Gln and an undetermined Lys by !1transglutaminase REFERENCE A40301 !$#authors Kovacic, R.T.; Tizard, R.; Cate, R.L.; Frey, A.Z.; Wallner, !1B.P. !$#journal Biochemistry (1991) 30:9015-9021 !$#title Correlation of gene and protein structure of rat and human !1lipocortin I. !$#cross-references MUID:91369906; PMID:1832554 !$#contents annotation REFERENCE A38843 !$#authors Biemann, K.; Scoble, H.A. !$#journal Science (1987) 237:992-998 !$#title Characterization by tandem mass spectrometry of structural !1modifications in proteins. !$#cross-references MUID:87292145; PMID:3303336 !$#contents annotation; amino-terminal acetylation REFERENCE S28846 !$#authors Arcone, R.; Arpaia, G.; Ruoppolo, M.; Malorni, A.; Pucci, !1P.; Marino, G.; Ialenti, A.; di Rosa, M.; Ciliberto, G. !$#journal Eur. J. Biochem. (1993) 211:347-355 !$#title Structural characterization of a biologically active human !1lipocortin 1 expressed in Escherichia coli. !$#cross-references MUID:93145967; PMID:8425544 !$#contents annotation REFERENCE A34459 !$#authors Hayashi, H.; Owada, M.K.; Sonobe, S.; Kakunaga, T. !$#journal J. Biol. Chem. (1989) 264:17222-17230 !$#title Characterizations of two distinct Ca(2+)-dependent !1phospholipid-binding proteins of 68-kDa isolated from human !1placenta. !$#cross-references MUID:90008880; PMID:2529258 !$#accession A34459 !'##molecule_type protein !'##residues 30-45;82-97;114-128;148-161;275-281 ##label HAY COMMENT Annexins undergo reversible, calcium-dependent binding to !1membrane phospholipids. Although a number have been !1proposed, the physiological roles of the various annexins !1are not yet fully understood. COMMENT Annexin I has been shown to be both an intracellular and an !1extracellular protein. A proposed extracellular role of !1annexin I is that of a steroid-inducible inhibitor of !1phospholipase A2 activity. Unphosphorylated it is a potent !1inhibitor of the enzyme, mimicking the ameliorating effects !1glucocorticoids have on the inflammatory response by !1blocking the hydrolysis of membrane phospholipids. !1Phosphorylation of annexin I results in loss of its !1inhibitory activity. COMMENT This protein contains four homologous repeats. Each contains !1an "endonexin fold," a consensus sequence common to all !1annexins. A pair of these repeats may form one binding site !1for calcium and phospholipid. GENETICS !$#gene GDB:ANX1 !'##cross-references GDB:120550; OMIM:151690 !$#map_position 9q11-9q22 !$#introns 22/3; 59/1; 90/3; 128/3; 159/1; 185/3; 204/3; 236/1; 268/1; !1287/3; 328/3 CLASSIFICATION #superfamily annexin I; annexin repeat homology KEYWORDS acetylated amino end; calcium binding; duplication; !1endonexin fold; glycoprotein; inflammation; phospholipid !1binding; phosphoprotein FEATURE !$2-346 #product annexin I #status predicted #label MAT\ !$45-116 #domain annexin repeat homology #label AX1\ !$56-72 #region endonexin fold #status predicted\ !$117-188 #domain annexin repeat homology #label AX2\ !$128-144 #region endonexin fold #status predicted\ !$200-272 #domain annexin repeat homology #label AX3\ !$212-228 #region endonexin fold #status predicted\ !$276-346 #domain annexin repeat homology #label AX4\ !$287-303 #region endonexin fold #status predicted\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental\ !$21 #binding_site phosphate (Tyr) (covalent) (by EGF !8receptor/kinase) #status experimental\ !$27 #binding_site phosphate (Ser) (covalent) (by protein !8kinase C) #status experimental\ !$43 #binding_site carbohydrate (Asn) (covalent) #status !8absent\ !$216 #binding_site phosphate (Thr) (covalent) (by !8cAMP-dependent kinase) #status experimental SUMMARY #length 346 #molecular-weight 38714 #checksum 9402 SEQUENCE /// ENTRY S28228 #type complete TITLE annexin I - bovine ALTERNATE_NAMES calpactin II ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 13-Jan-1995 #sequence_revision 05-Apr-1995 #text_change 22-Jun-1999 ACCESSIONS S28228; A60851 REFERENCE S28228 !$#authors Ernst, J.D. !$#journal Biochem. J. (1993) 289:539-542 !$#title Epitope mapping of annexin I: antibodies that compete with !1phospholipids and calcium recognize amino acids 42-99. !$#cross-references MUID:93143727; PMID:7678738 !$#accession S28228 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-346 ##label ERN !'##cross-references EMBL:X56649; NID:g73; PIDN:CAA39971.1; PID:g74 !'##experimental_source Madin-Darby kidney cell line REFERENCE A60851 !$#authors Glenney Jr., J.R.; Tack, B.; Powell, M.A. !$#journal J. Cell Biol. (1987) 104:503-511 !$#title Calpactins: two distinct CA(++)-regulated phospholipid- and !1actin-binding proteins isolated from lung and placenta. !$#cross-references MUID:87137890; PMID:2950118 !$#accession A60851 !'##molecule_type protein !'##residues 13-40 ##label GLE !'##experimental_source lung COMMENT Annexins undergo reversible, calcium-dependent binding to !1membrane phospholipids. Although a number have been !1proposed, the physiological roles of the various annexins !1are not yet fully understood. COMMENT Annexin I has been shown to be both an intracellular and an !1extracellular protein. A proposed extracellular role of !1annexin I is that of a steroid-inducible inhibitor of !1phospholipase A2 activity. Unphosphorylated it is a potent !1inhibitor of the enzyme, mimicking the ameliorating effects !1glucocorticoids have on the inflammatory response by !1blocking the hydrolysis of membrane phospholipids. !1Phosphorylation of annexin I results in loss of its !1inhibitory activity. COMMENT This protein contains four homologous repeats. Each contains !1an "endonexin fold," a consensus sequence common to all !1annexins. A pair of these repeats may form one binding site !1for calcium and phospholipid. CLASSIFICATION #superfamily annexin I; annexin repeat homology KEYWORDS blocked amino end; calcium binding; duplication; endonexin !1fold; glycoprotein; inflammation; phospholipid binding; !1phosphoprotein FEATURE !$2-346 #product annexin I #status predicted #label MAT\ !$45-116 #domain annexin repeat homology #label AX1\ !$56-72 #region endonexin fold #status predicted\ !$117-188 #domain annexin repeat homology #label AX2\ !$128-144 #region endonexin fold #status predicted\ !$200-272 #domain annexin repeat homology #label AX3\ !$212-228 #region endonexin fold #status predicted\ !$276-346 #domain annexin repeat homology #label AX4\ !$287-303 #region endonexin fold #status predicted\ !$2 #modified_site blocked amino end (Ala) (in mature !8form) (probably acetylated) #status experimental\ !$21 #binding_site phosphate (Tyr) (covalent) (by EGF !8receptor/kinase) #status predicted\ !$216 #binding_site phosphate (Thr) (covalent) (by !8cAMP-dependent kinase) #status predicted SUMMARY #length 346 #molecular-weight 38897 #checksum 9038 SEQUENCE /// ENTRY LUGP1 #type complete TITLE annexin I - guinea pig ALTERNATE_NAMES 33K protein; calpactin II; lipocortin I ORGANISM #formal_name Cavia porcellus #common_name guinea pig DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 22-Jun-1999 ACCESSIONS S02779; S26635 REFERENCE S02779 !$#authors Sato, E.F.; Tanaka, Y.; Utsumi, K. !$#journal FEBS Lett. (1989) 244:108-112 !$#title cDNA cloning and nucleotide sequence of lipocortin-like 33 !1kDa protein in guinea pig neutrophils. !$#cross-references MUID:89171240; PMID:2522394 !$#accession S02779 !'##molecule_type mRNA !'##residues 1-346 ##label SAT !'##cross-references EMBL:X14635; NID:g49437; PIDN:CAA32783.1; !1PID:g49438 REFERENCE S07909 !$#authors Sato, E.F.; Miyahara, M.; Utsumi, K. !$#journal FEBS Lett. (1988) 227:131-135 !$#title Purification and characterization of a lipocortin-like 33 !1kDa protein from guinea pig neutrophils. !$#cross-references MUID:88112235; PMID:2962884 !$#accession S26635 !'##molecule_type protein !'##residues 10-15,'D';30-44;248-249,'X',251-256,'X', !1258-259;286-292;308-316,'XT' ##label SA2 COMMENT Annexins undergo reversible, calcium-dependent binding to !1membrane phospholipids. Although a number have been !1proposed, the physiological roles of the various annexins !1are not yet fully understood. COMMENT Annexin I has been shown to be both an intracellular and an !1extracellular protein. A proposed extracellular role of !1annexin I is that of a steroid-inducible inhibitor of !1phospholipase A2 activity. Unphosphorylated it is a potent !1inhibitor of the enzyme, mimicking the ameliorating effects !1glucocorticoids have on the inflammatory response by !1blocking the hydrolysis of membrane phospholipids. !1Phosphorylation of annexin I results in loss of its !1inhibitory activity. COMMENT This protein contains four homologous repeats. Each contains !1an "endonexin fold," a consensus sequence common to all !1annexins. A pair of these repeats may form one binding site !1for calcium and phospholipid. CLASSIFICATION #superfamily annexin I; annexin repeat homology KEYWORDS calcium binding; duplication; endonexin fold; inflammation; !1phospholipid binding; phosphoprotein FEATURE !$2-346 #product annexin I #status predicted #label MAT\ !$45-116 #domain annexin repeat homology #label AX1\ !$56-72 #region endonexin fold #status predicted\ !$117-188 #domain annexin repeat homology #label AX2\ !$128-144 #region endonexin fold #status predicted\ !$200-272 #domain annexin repeat homology #label AX3\ !$212-228 #region endonexin fold #status predicted\ !$276-346 #domain annexin repeat homology #label AX4\ !$287-303 #region endonexin fold #status predicted\ !$21 #binding_site phosphate (Tyr) (covalent) (by EGF !8receptor/kinase) #status predicted\ !$27 #binding_site phosphate (Ser) (covalent) (by protein !8kinase C) #status predicted\ !$216 #binding_site phosphate (Thr) (covalent) (by !8cAMP-dependent kinase) #status predicted SUMMARY #length 346 #molecular-weight 38555 #checksum 8748 SEQUENCE /// ENTRY LURT1 #type complete TITLE annexin I - rat ALTERNATE_NAMES calpactin II; lipocortin I; p35; phospholipase A2 inhibitory protein ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 22-Jun-1999 ACCESSIONS JT0303; A26841; A40301; A30896; B53507 REFERENCE A91595 !$#authors Shimizu, Y.; Takabayashi, E.; Yano, S.; Shimizu, N.; Yamada, !1K.; Gushima, H. !$#journal Gene (1988) 65:141-147 !$#title Molecular cloning and expression in Escherichia coli of the !1cDNA coding for rat lipocortin I (calpactin II). !$#cross-references MUID:88284376; PMID:2969352 !$#accession JT0303 !'##molecule_type mRNA !'##residues 1-346 ##label SHI !'##cross-references GB:M19967; NID:g203251; PIDN:AAA40861.1; !1PID:g203252 REFERENCE A26841 !$#authors Tamaki, M.; Nakamura, E.; Nishikubo, C.; Sakata, T.; Shin, !1M.; Teraoka, H. !$#journal Nucleic Acids Res. (1987) 15:7637 !$#title Rat lipocortin I cDNA. !$#cross-references MUID:88015620; PMID:2958780 !$#accession A26841 !'##molecule_type mRNA !'##residues 1-346 ##label TAM !'##cross-references GB:Y00446; NID:g56565; PIDN:CAA68500.1; PID:g56566 REFERENCE A40301 !$#authors Kovacic, R.T.; Tizard, R.; Cate, R.L.; Frey, A.Z.; Wallner, !1B.P. !$#journal Biochemistry (1991) 30:9015-9021 !$#title Correlation of gene and protein structure of rat and human !1lipocortin I. !$#cross-references MUID:91369906; PMID:1832554 !$#accession A40301 !'##molecule_type DNA !'##residues 1-321,'S',323-346 ##label KOV !'##cross-references GB:S57478; GB:J05339; NID:g235878; PIDN:AAB19866.1; !1PID:g235879 REFERENCE A92578 !$#authors Pepinsky, R.B.; Sinclair, L.K.; Browning, J.L.; Mattaliano, !1R.J.; Smart, J.E.; Chow, E.P.; Falbel, T.; Ribolini, A.; !1Garwin, J.L.; Waller, B.P. !$#journal J. Biol. Chem. (1986) 261:4239-4246 !$#title Purification and partial sequence analysis of a 37-kDAa !1protein that inhibits phospholipase A2 activity from rat !1peritoneal exudates. !$#cross-references MUID:86140249; PMID:3081518 !$#accession A30896 !'##molecule_type protein !'##residues 27-50;54-71;82-97;111-123,'L',124;129-134,'EX',137-138,'X', !1140;155-161;167-177;205-210,'Q',212;214-234;236-257;282-292, !1'R',294-297;304-317;332-337 ##label PEP REFERENCE A53507 !$#authors Hyatt, S.L.; Liao, L.; Chapline, C.; Jaken, S. !$#journal Biochemistry (1994) 33:1223-1228 !$#title Identification and characterization of alpha-protein kinase !1C binding proteins in normal and transformed REF52 cells. !$#cross-references MUID:94153907; PMID:8110754 !$#accession B53507 !'##status preliminary !'##molecule_type protein !'##residues 59-64,'T',66;82-97 ##label HYA COMMENT Annexins undergo reversible, calcium-dependent binding to !1membrane phospholipids. Although a number have been !1proposed, the physiological roles of the various annexins !1are not yet fully understood. COMMENT Annexin I has been shown to be both an intracellular and an !1extracellular protein. A proposed extracellular role of !1annexin I is that of a steroid-inducible inhibitor of !1phospholipase A2 activity. Unphosphorylated it is a potent !1inhibitor of the enzyme, mimicking the ameliorating effects !1glucocorticoids have on the inflammatory response by !1blocking the hydrolysis of membrane phospholipids. !1Phosphorylation of annexin I results in loss of its !1inhibitory activity. COMMENT This protein contains four homologous repeats. Each contains !1an "endonexin fold," a consensus sequence common to all !1annexins. A pair of these repeats may form one binding site !1for calcium and phospholipid. GENETICS !$#introns 22/3; 59/1; 90/3; 128/3; 159/1; 185/3; 204/3; 236/1; 268/1; !1287/3; 328/3 CLASSIFICATION #superfamily annexin I; annexin repeat homology KEYWORDS acetylated amino end; calcium binding; duplication; !1endonexin fold; glycoprotein; inflammation; phospholipid !1binding; phosphoprotein FEATURE !$2-346 #product annexin I #status predicted #label MAT\ !$45-116 #domain annexin repeat homology #label AX1\ !$56-72 #region endonexin fold #status predicted\ !$117-188 #domain annexin repeat homology #label AX2\ !$128-144 #region endonexin fold #status predicted\ !$200-272 #domain annexin repeat homology #label AX3\ !$212-228 #region endonexin fold #status predicted\ !$276-346 #domain annexin repeat homology #label AX4\ !$287-303 #region endonexin fold #status predicted\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status predicted\ !$21 #binding_site phosphate (Tyr) (covalent) (by EGF !8receptor/kinase) #status predicted\ !$27 #binding_site phosphate (Ser) (covalent) (by protein !8kinase C) #status predicted\ !$43 #binding_site carbohydrate (Asn) (covalent) #status !8absent\ !$216 #binding_site phosphate (Thr) (covalent) (by !8cAMP-dependent kinase) #status predicted SUMMARY #length 346 #molecular-weight 38829 #checksum 2530 SEQUENCE /// ENTRY LUMS1 #type complete TITLE annexin I - mouse ALTERNATE_NAMES calpactin II; lipocortin I; p35; phospholipase A2 inhibitory protein ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 22-Jun-1999 ACCESSIONS S02181; A39902; A32299 REFERENCE S02181 !$#authors Sakata, T.; Iwagami, S.; Tsuruta, Y.; Suzuki, R.; Hojo, K.; !1Sato, K.; Teraoka, H. !$#journal Nucleic Acids Res. (1988) 16:11818 !$#title Mouse lipocortin I cDNA. !$#cross-references MUID:89098333; PMID:2974946 !$#accession S02181 !'##molecule_type mRNA !'##residues 1-346 ##label SAK !'##cross-references EMBL:X07486; NID:g52875; PIDN:CAA30371.1; !1PID:g52876 REFERENCE A39902 !$#authors Horlick, K.R.; Cheng, I.C.; Wong, W.T.; Wakeland, E.K.; !1Nick, H.S. !$#journal Genomics (1991) 10:365-374 !$#title Mouse lipocortin I gene structure and chromosomal !1assignment: gene duplication and the origins of a gene !1family. !$#cross-references MUID:91301692; PMID:1676980 !$#accession A39902 !'##molecule_type DNA !'##residues 1-211,'I',213-346 ##label HOR !'##cross-references GB:M69260; NID:g198843; PIDN:AAA39437.1; !1PID:g198845 !'##note the authors translated the codon ATT for residue 212 as Arg REFERENCE A32299 !$#authors Philipps, C.; Rose-John, S.; Rincke, G.; Fuerstenberger, G.; !1Marks, F. !$#journal Biochem. Biophys. Res. Commun. (1989) 159:155-162 !$#title cDNA-cloning, sequencing and expression in !1glucocorticoid-stimulated quiescent Swiss 3T3 fibroblasts of !1mouse lipocortin I. !$#cross-references MUID:89165848; PMID:2522299 !$#accession A32299 !'##molecule_type mRNA !'##residues 6-77,'PR',80-221,'H',223-273,'H',275-346 ##label PHI !'##cross-references GB:M24554; NID:g198761; PIDN:AAA39420.1; !1PID:g387403 !'##experimental_source Swiss 3T3 cells COMMENT Annexins undergo reversible, calcium-dependent binding to !1membrane phospholipids. Although a number have been !1proposed, the physiological roles of the various annexins !1are not yet fully understood. COMMENT Annexin I has been shown to be both an intracellular and an !1extracellular protein. A proposed extracellular role of !1annexin I is that of a steroid-inducible inhibitor of !1phospholipase A2 activity. Unphosphorylated it is a potent !1inhibitor of the enzyme, mimicking the ameliorating effects !1glucocorticoids have on the inflammatory response by !1blocking the hydrolysis of membrane phospholipids. !1Phosphorylation of annexin I results in loss of its !1inhibitory activity. COMMENT This protein contains four homologous repeats. Each contains !1an "endonexin fold," a consensus sequence common to all !1annexins. A pair of these repeats may form one binding site !1for calcium and phospholipid. GENETICS !$#gene LipoI !$#map_position 19 !$#introns 22/3; 59/1; 90/3; 128/3; 159/1; 185/3; 204/3; 236/1; 268/1; !1287/3; 328/3 CLASSIFICATION #superfamily annexin I; annexin repeat homology KEYWORDS acetylated amino end; calcium binding; duplication; !1endonexin fold; glycoprotein; inflammation; phospholipid !1binding; phosphoprotein FEATURE !$2-346 #product annexin I #status predicted #label MAT\ !$45-116 #domain annexin repeat homology #label AX1\ !$56-72 #region endonexin fold #status predicted\ !$117-188 #domain annexin repeat homology #label AX2\ !$128-144 #region endonexin fold #status predicted\ !$200-272 #domain annexin repeat homology #label AX3\ !$212-228 #region endonexin fold #status predicted\ !$276-346 #domain annexin repeat homology #label AX4\ !$287-303 #region endonexin fold #status predicted\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status predicted\ !$21 #binding_site phosphate (Tyr) (covalent) (by EGF !8receptor/kinase) #status predicted\ !$27 #binding_site phosphate (Ser) (covalent) (by protein !8kinase C) #status predicted\ !$43 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$216 #binding_site phosphate (Thr) (covalent) (by !8cAMP-dependent kinase) #status predicted SUMMARY #length 346 #molecular-weight 38734 #checksum 2648 SEQUENCE /// ENTRY LUPY1 #type complete TITLE annexin I type 1 - pigeon ALTERNATE_NAMES calpactin II; calpactin/lipocortin homolog; cropsac 35K protein; phospholipase A2 inhibitory protein ORGANISM #formal_name Columba livia #common_name domestic pigeon DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Feb-1997 ACCESSIONS A40153; PH0846 REFERENCE A40153 !$#authors Horseman, N.D. !$#journal Mol. Endocrinol. (1989) 3:773-779 !$#title A prolactin-inducible gene product which is a member of the !1calpactin/lipocortin family. !$#cross-references MUID:89330493; PMID:2526923 !$#accession A40153 !'##molecule_type mRNA !'##residues 1-341 ##label HOR !'##cross-references GB:M22635 REFERENCE PH0846 !$#authors Hitti, Y.S.; Horseman, N.D. !$#journal Gene (1991) 103:185-192 !$#title Structure of the gene encoding columbid annexin I cp35. !$#cross-references MUID:91365244; PMID:1832409 !$#accession PH0846 !'##molecule_type DNA !'##residues 1-53 ##label HIT GENETICS !$#gene cp35 !$#introns 22/3; 54/1 CLASSIFICATION #superfamily annexin I; annexin repeat homology KEYWORDS calcium; duplication; endonexin fold; inflammation; !1phospholipase A2 inhibitor; phospholipid binding; !1phosphoprotein FEATURE !$2-340 #product annexin I #status predicted #label MAT\ !$40-111 #domain annexin repeat homology #label AX1\ !$51-67 #region endonexin fold #status predicted\ !$112-183 #domain annexin repeat homology #label AX2\ !$123-139 #region endonexin fold #status predicted\ !$195-266 #domain annexin repeat homology #label AX3\ !$207-223 #region endonexin fold #status predicted\ !$270-341 #domain annexin repeat homology #label AX4\ !$281-297 #region endonexin fold #status predicted\ !$211 #binding_site phosphate (Thr) (covalent) (by !8cAMP-dependent kinase) #status predicted SUMMARY #length 341 #molecular-weight 38482 #checksum 2231 SEQUENCE /// ENTRY A44118 #type complete TITLE annexin I type 2 - pigeon ALTERNATE_NAMES calpactin II; calpactin/lipocortin homolog; cp37 protein; cropsac 37K protein ORGANISM #formal_name Columba livia #common_name domestic pigeon DATE 31-Dec-1993 #sequence_revision 26-May-1994 #text_change 22-Jun-1999 ACCESSIONS A44118; B44118; A38909; I51112 REFERENCE A44118 !$#authors Haigler, H.T.; Mangili, J.A.; Gao, Y.; Jones, J.; Horseman, !1N.D. !$#journal J. Biol. Chem. (1992) 267:19123-19129 !$#title Identification and characterization of columbid annexin !1Icp37. Insights into the evolution of annexin I !1phosphorylation sites. !$#cross-references MUID:92406850; PMID:1388165 !$#accession A44118 !'##molecule_type mRNA !'##residues 1-343 ##label HAI !'##note sequence extracted from NCBI backbone (NCBIN:113807, !1NCBIP:113808) !$#accession B44118 !'##molecule_type protein !'##residues 13-15,'X',17,'X',19-28,'X',30-50 ##label HA2 REFERENCE A38909 !$#authors Haigler, H.T.; Mangili, J.A.; Gao, Y.; Jones, J.; Horseman, !1N.D. !$#submission submitted to GenBank, October 1992 !$#accession A38909 !'##molecule_type mRNA !'##residues 1-73,'HR',76-343 ##label HA3 !'##cross-references GB:M91008; NID:g213521; PIDN:AAA49447.1; !1PID:g213522 !'##note amino end is blocked in the mature form REFERENCE I51112 !$#authors Gao, Y.; Horseman, N.D. !$#journal Gene (1994) 143:179-186 !$#title Structural and functional divergences of the columbid !1annexin I-encoding cp37 and cp35 genes. !$#cross-references MUID:94266150; PMID:8206371 !$#accession I51112 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-154 ##label GAO !'##cross-references GB:L02504; NID:g213535; PIDN:AAA20674.1; !1PID:g529725 GENETICS !$#gene cp37 !$#introns 22/3; 55/1; 86/3; 124/3 CLASSIFICATION #superfamily annexin I; annexin repeat homology KEYWORDS acetylated amino end; calcium binding; duplication; !1endonexin fold; inflammation; phospholipid binding; !1phosphoprotein FEATURE !$2-342 #product annexin I #status predicted #label MAT\ !$41-112 #domain annexin repeat homology #label AX1\ !$52-68 #region endonexin fold #status predicted\ !$113-184 #domain annexin repeat homology #label AX2\ !$124-140 #region endonexin fold #status predicted\ !$196-268 #domain annexin repeat homology #label AX3\ !$208-224 #region endonexin fold #status predicted\ !$272-343 #domain annexin repeat homology #label AX4\ !$283-299 #region endonexin fold #status predicted\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status predicted\ !$21 #binding_site phosphate (Tyr) (covalent) (by EGF !8receptor/kinase) #status predicted\ !$24 #binding_site phosphate (Ser) (covalent) (by protein !8kinase C) #status predicted SUMMARY #length 343 #molecular-weight 38811 #checksum 9583 SEQUENCE /// ENTRY LUHU36 #type complete TITLE annexin II - human ALTERNATE_NAMES calcium-dependent phospholipid-actin-binding protein; calpactin I heavy chain; chromobindin 8; lipocortin II; p36; PAP-IV; placental anticoagulant protein IV; primer recognition protein PRP-2 ORGANISM #formal_name Homo sapiens #common_name man DATE 28-Dec-1987 #sequence_revision 30-Sep-1992 #text_change 16-Jun-2000 ACCESSIONS A23942; JH0305; A45440; PC2039; C53507; A23717; A05153 REFERENCE A90881 !$#authors Huang, K.S.; Wallner, B.P.; Mattaliano, R.J.; Tizard, R.; !1Burne, C.; Frey, A.; Hession, C.; McGray, P.; Sinclair, !1L.K.; Chow, E.P.; Browning, J.L.; Ramachandran, K.L.; Tang, !1J.; Smart, J.E.; Pepinsky, R.B. !$#journal Cell (1986) 46:191-199 !$#title Two human 35 kd inhibitors of phospholipase A2 are related !1to substrates of pp60v-src and of the epidermal growth !1factor receptor/kinase. !$#cross-references MUID:86245065; PMID:3013422 !$#accession A23942 !'##molecule_type mRNA !'##residues 1-339 ##label HUA !'##cross-references GB:D00017; GB:M14043; NID:g219909; PIDN:BAA00013.1; !1PID:g219910 !'##experimental_source placenta !'##note part of this sequence was confirmed by protein sequencing REFERENCE JH0305 !$#authors Spano, F.; Raugei, G.; Palla, E.; Colella, C.; Melli, M. !$#journal Gene (1990) 95:243-251 !$#title Characterization of the human lipocortin-2-encoding !1multigene family: its structure suggests the existence of a !1short amino acid unit undergoing duplication. !$#cross-references MUID:91065537; PMID:2174397 !$#accession JH0305 !'##molecule_type DNA !'##residues 1-339 ##label SPA !'##cross-references DDBJ:D00017; NID:g219909; PIDN:BAA00013.1; !1PID:g219910 REFERENCE A45440 !$#authors Emans, N.; Gorvel, J.P.; Walter, C.; Gerke, V.; Kellner, R.; !1Griffiths, G.; Gruenberg, J. !$#journal J. Cell Biol. (1993) 120:1357-1369 !$#title Annexin II is a major component of fusogenic endosomal !1vesicles. !$#cross-references MUID:93194942; PMID:8449982 !$#accession A45440 !'##molecule_type protein !'##residues 234-241;252-261 ##label EMA !'##note this protein was demonstrated in early endosomes in vivo and !1shown to be transferred efficiently from small sonicated !1endosomes in an assay of membrane trafficking in vitro REFERENCE PC2039 !$#authors Wright, J.F.; Kurosky, A.; Wasi, S. !$#journal Biochem. Biophys. Res. Commun. (1994) 198:983-989 !$#title An endothelial cell-surface form of annexin II binds human !1cytomegalovirus. !$#cross-references MUID:94161769; PMID:8117306 !$#accession PC2039 !'##molecule_type protein !'##residues 18-37;119-126;172-191;301-304,'X',306-307 ##label WRI REFERENCE A53507 !$#authors Hyatt, S.L.; Liao, L.; Chapline, C.; Jaken, S. !$#journal Biochemistry (1994) 33:1223-1228 !$#title Identification and characterization of alpha-protein kinase !1C binding proteins in normal and transformed REF52 cells. !$#cross-references MUID:94153907; PMID:8110754 !$#accession C53507 !'##molecule_type protein !'##residues 'LXXXX',15-28,'P',30-40;50-51,'XX',54-63 ##label HYA REFERENCE A23717 !$#authors Jindal, H.K.; Chaney, W.G.; Anderson, C.W.; Davis, R.G.; !1Vishwanatha, J.K. !$#journal J. Biol. Chem. (1991) 266:5169-5176 !$#title The protein-tyrosine kinase substrate, calpactin I heavy !1chain (p36), is part of the primer recognition protein !1complex that interacts with DNA polymerase alpha. !$#cross-references MUID:91161611; PMID:1825830 !$#accession A23717 !'##molecule_type protein !'##residues 11-28;50-63;69-77;120-135;314-324;330-339 ##label JIN COMMENT Annexins undergo reversible, calcium-dependent binding to !1membrane phospholipids. COMMENT Calpactin I, a tetramer of two heavy chains and two light !1chains, is found in the lamina beneath the plasma membrane. !1It may cross-link plasma membrane phospholipids with actin !1and the cytoskeleton and be involved with exocytosis. COMMENT Annexin II is the heavy chain component of calpactin I. The !1affinity of annexin II for calcium is greatly enhanced by !1anionic phospholipids. In the presence of !1phosphatidylserine, calpactin I binds two moles of calcium !1ion per mole of annexin II. These ligands make annexin II a !1better substrate for tyrosine kinases. COMMENT Annexin II may act as a regulator of intracellular !1phospholipase activity. GENETICS !$#gene GDB:ANX2 !'##cross-references GDB:120554; OMIM:151740 !$#map_position 15q21-15q22 !$#introns 16/3; 50/1; 81/3; 119/3; 150/1; 176/3; 196/3; 228/1; 260/1; !1279/3; 320/3 CLASSIFICATION #superfamily annexin I; annexin repeat homology KEYWORDS acetylated amino end; actin binding; calcium binding; !1duplication; endonexin fold; heterotetramer; phospholipid !1binding; phosphoprotein FEATURE !$2-339 #product annexin II #status predicted #label MAT\ !$2-12 #region calpactin I light chain binding #status !8predicted\ !$36-107 #domain annexin repeat homology #label AX1\ !$47-63 #region endonexin fold #status predicted\ !$108-179 #domain annexin repeat homology #label AX2\ !$119-135 #region endonexin fold #status predicted\ !$192-264 #domain annexin repeat homology #label AX3\ !$204-220 #region endonexin fold #status predicted\ !$268-339 #domain annexin repeat homology #label AX4\ !$279-295 #region endonexin fold #status predicted\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status predicted\ !$24 #binding_site phosphate (Tyr) (covalent) #status !8predicted\ !$26 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 339 #molecular-weight 38604 #checksum 3105 SEQUENCE /// ENTRY LUBO36 #type complete TITLE annexin II - bovine ALTERNATE_NAMES 36K protein; calcium-dependent phospholipid-actin-binding protein; calpactin I heavy chain; chromobindin 8; lipocortin II; p36; PAP-IV; placental anticoagulant protein IV ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 04-Dec-1986 #sequence_revision 30-Sep-1992 #text_change 22-Jun-1999 ACCESSIONS A03081; S02477 REFERENCE A03081 !$#authors Kristensen, T.; Saris, C.J.M.; Hunter, T.; Hicks, L.J.; !1Noonan, D.J.; Glenney Jr., J.R.; Tack, B.F. !$#journal Biochemistry (1986) 25:4497-4503 !$#title Primary structure of bovine calpactin I heavy chain (p36), a !1major cellular substrate for retroviral protein-tyrosine !1kinases: homology with the human phospholipase A-2 inhibitor !1lipocortin. !$#cross-references MUID:87026517; PMID:2945590 !$#accession A03081 !'##molecule_type mRNA !'##residues 1-339 ##label KRI !'##cross-references GB:M14056; NID:g162778; PIDN:AAA30421.1; !1PID:g162779 !'##experimental_source Madin-Darby kidney cell line MDBK REFERENCE S02477 !$#authors Martin, F.; Derancourt, J.; Capony, J.P.; Watrin, A.; !1Cavadore, J.C. !$#journal Biochem. J. (1988) 251:777-785 !$#title A 36 kDa monomeric protein and its complex with a 10 kDa !1protein both isolated from bovine aorta are calpactin-like !1proteins that differ in their Ca(2+)-dependent !1calmodulin-binding and actin-severing properties. !$#cross-references MUID:88326216; PMID:2970844 !$#accession S02477 !'##molecule_type protein !'##residues 27-61 ##label MAR !'##experimental_source aorta !'##note 44-Lys was also found REFERENCE A38844 !$#authors Glenny Jr., J.R.; Boudreau, M.; Galyean, R.; Hunter, T.; !1Tack, B. !$#journal J. Biol. Chem. (1986) 261:10485-10488 !$#title Association of the S-100-related calpactin I light chain !1with the NH2-terminal tail of the 36-kDa heavy chain. !$#cross-references MUID:86278112; PMID:2942542 !$#contents annotation; amino-terminal acetylation COMMENT Annexins undergo reversible, calcium-dependent binding to !1membrane phospholipids. Although a number have been !1proposed, the physiological roles of the various annexins !1are not yet fully understood. COMMENT Calpactin I, a tetramer of two heavy chains and two light !1chains, is found in the lamina beneath the plasma membrane. !1It may cross-link plasma membrane phospholipids with actin !1and the cytoskeleton and be involved with exocytosis. COMMENT Annexin II is the heavy chain component of calpactin I. The !1affinity of annexin II for calcium is greatly enhanced by !1anionic phospholipids. In the presence of !1phosphatidylserine, calpactin I binds two moles of calcium !1ion per mole of annexin II. These ligands make annexin II a !1better substrate for tyrosine kinases. COMMENT Annexin II may act as a regulator of intracellular !1phospholipase activity. CLASSIFICATION #superfamily annexin I; annexin repeat homology KEYWORDS acetylated amino end; actin binding; calcium binding; !1duplication; endonexin fold; heterotetramer; phospholipid !1binding; phosphoprotein FEATURE !$2-339 #product annexin II #status experimental #label MAT\ !$2-12 #region calpactin I light chain binding #status !8predicted\ !$36-107 #domain annexin repeat homology #label AX1\ !$47-63 #region endonexin fold #status predicted\ !$108-179 #domain annexin repeat homology #label AX2\ !$119-135 #region endonexin fold #status predicted\ !$192-264 #domain annexin repeat homology #label AX3\ !$204-220 #region endonexin fold #status predicted\ !$268-339 #domain annexin repeat homology #label AX4\ !$279-295 #region endonexin fold #status predicted\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental\ !$24 #binding_site phosphate (Tyr) (covalent) #status !8predicted\ !$26 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 339 #molecular-weight 38612 #checksum 2778 SEQUENCE /// ENTRY LUMS36 #type complete TITLE annexin II - mouse ALTERNATE_NAMES calcium-dependent phospholipid-actin-binding protein; calpactin I heavy chain; chromobindin 8; lipocortin II; p36; PAP-IV; placental anticoagulant protein IV ORGANISM #formal_name Mus musculus #common_name house mouse DATE 28-Dec-1987 #sequence_revision 30-Sep-1992 #text_change 22-Jun-1999 ACCESSIONS A23943; A35600 REFERENCE A23943 !$#authors Saris, C.J.M.; Tack, B.F.; Kristensen, T.; Glenney Jr., !1J.R.; Hunter, T. !$#journal Cell (1986) 46:201-212 !$#title The cDNA sequence for the protein-tyrosine kinase substrate !1p36 (calpactin I heavy chain) reveals a multidomain protein !1with internal repeats. !$#cross-references MUID:86245066; PMID:3013423 !$#accession A23943 !'##molecule_type mRNA !'##residues 1-339 ##label SAR !'##cross-references GB:M14044; NID:g192353; PIDN:AAA37360.1; !1PID:g309133 REFERENCE A35600 !$#authors Amiguet, P.; D'Eustachio, P.; Kristensen, T.; Wetsel, R.A.; !1Saris, C.J.M.; Hunter, T.; Chaplin, D.D.; Tack, B.F. !$#journal Biochemistry (1990) 29:1226-1232 !$#title Structure and chromosome assignment of the murine p36 !1(calpactin I heavy chain) gene. !$#cross-references MUID:90212611; PMID:2138915 !$#accession A35600 !'##molecule_type DNA !'##residues 1-15;322-339 ##label AMI !'##cross-references GB:M33321; GB:M33322 !'##experimental_source Abelson murine leukemia virus-transformed NIH3T3 !1cells (ANN-1) COMMENT Annexins undergo reversible, calcium-dependent binding to !1membrane phospholipids. Although a number have been !1proposed, the physiological roles of the various annexins !1are not yet fully understood. COMMENT Calpactin I, a tetramer of two heavy chains and two light !1chains, is found in the lamina beneath the plasma membrane. !1It may cross-link plasma membrane phospholipids with actin !1and the cytoskeleton and be involved with exocytosis. COMMENT Annexin II is the heavy chain component of calpactin I. The !1affinity of annexin II for calcium is greatly enhanced by !1anionic phospholipids. In the presence of !1phosphatidylserine, calpactin I binds two moles of calcium !1ion per mole of annexin II. These ligands make annexin II a !1better substrate for tyrosine kinases. COMMENT Annexin II may act as a regulator of intracellular !1phospholipase activity. GENETICS !$#gene Cal1h !$#map_position 9 !$#introns 16/3; 50/1; 81/3; 119/3; 150/1; 176/3; 196/3; 228/1; 260/1; !1279/3; 321/3 CLASSIFICATION #superfamily annexin I; annexin repeat homology KEYWORDS acetylated amino end; actin binding; calcium binding; !1duplication; endonexin fold; heterotetramer; phospholipid !1binding; phosphoprotein FEATURE !$2-339 #product annexin II #status predicted #label MAT\ !$2-12 #region calpactin I light chain binding #status !8predicted\ !$36-107 #domain annexin repeat homology #label AX1\ !$47-63 #region endonexin fold #status predicted\ !$108-179 #domain annexin repeat homology #label AX2\ !$119-135 #region endonexin fold #status predicted\ !$192-264 #domain annexin repeat homology #label AX3\ !$204-220 #region endonexin fold #status predicted\ !$268-339 #domain annexin repeat homology #label AX4\ !$279-295 #region endonexin fold #status predicted\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status predicted\ !$24 #binding_site phosphate (Tyr) (covalent) #status !8predicted\ !$26 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 339 #molecular-weight 38676 #checksum 3965 SEQUENCE /// ENTRY LUCH2 #type complete TITLE annexin II - chicken ALTERNATE_NAMES 36K protein; calpactin I heavy chain; lipocortin II ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 22-Jun-1999 ACCESSIONS S10501; S01129; A40404; S01160 REFERENCE S10501 !$#authors Gerke, V.; Koch, W. !$#journal Nucleic Acids Res. (1990) 18:4246 !$#title The cDNA sequence of chicken annexin II. !$#cross-references MUID:90332421; PMID:2143014 !$#accession S10501 !'##molecule_type mRNA !'##residues 1-339 ##label GER !'##cross-references EMBL:X53334; NID:g62850; PIDN:CAA37421.1; !1PID:g62851 REFERENCE S01128 !$#authors Johnsson, N.; Johnsson, K.; Weber, K. !$#journal FEBS Lett. (1988) 236:201-204 !$#title A discontinuous epitope on p36, the major substrate of src !1tyrosine-protein-kinase, brings the phosphorylation site !1into the neighbourhood of a consensus sequence for Ca(2+)/ !1lipid-binding proteins. !$#cross-references MUID:88296872; PMID:2456953 !$#accession S01129 !'##molecule_type protein !'##residues 2-70 ##label JOH REFERENCE A40404 !$#authors Genge, B.R.; Wu, L.N.Y.; Adkisson IV, H.D.; Wuthier, R.E. !$#journal J. Biol. Chem. (1991) 266:10678-10685 !$#title Matrix vesicle annexins exhibit proteolipid-like properties. !1Selective partitioning into lipophilic solvents under acidic !1conditions. !$#cross-references MUID:91244852; PMID:2037607 !$#accession A40404 !'##molecule_type protein !'##residues 214-223,'X',225-229 ##label GEN !'##experimental_source epiphyseal growth plate cartilage (matrix !1vesicle-enriched microsomes) COMMENT Annexins undergo reversible, calcium-dependent binding to !1membrane phospholipids. Although a number have been !1proposed, the physiological roles of the various annexins !1are not yet fully understood. COMMENT Calpactin I, a tetramer of two heavy chains and two light !1chains, is found in the lamina beneath the plasma membrane. !1It may cross-link plasma membrane phospholipids with actin !1and the cytoskeleton and be involved with exocytosis. COMMENT Annexin II is the heavy chain component of calpactin I. The !1affinity of annexin II for calcium is greatly enhanced by !1anionic phospholipids. In the presence of !1phosphatidylserine, calpactin I binds two moles of calcium !1ion per mole of annexin II. These ligands make annexin II a !1better substrate for tyrosine kinases. COMMENT Annexin II may act as a regulator of intracellular !1phospholipase activity. CLASSIFICATION #superfamily annexin I; annexin repeat homology KEYWORDS calcium binding; duplication; endonexin fold; phospholipid !1binding; phosphoprotein FEATURE !$2-339 #product annexin II #status experimental #label MAT\ !$36-107 #domain annexin repeat homology #label AX1\ !$47-63 #region endonexin fold #status predicted\ !$108-179 #domain annexin repeat homology #label AX2\ !$119-135 #region endonexin fold #status predicted\ !$192-264 #domain annexin repeat homology #label AX3\ !$204-220 #region endonexin fold #status predicted\ !$268-339 #domain annexin repeat homology #label AX4\ !$279-295 #region endonexin fold #status predicted\ !$24 #binding_site phosphate (Tyr) (covalent) #status !8predicted\ !$26 #binding_site phosphate (Thr) (covalent) #status !8predicted SUMMARY #length 339 #molecular-weight 38640 #checksum 9546 SEQUENCE /// ENTRY JQ1297 #type complete TITLE annexin II type 1 - African clawed frog ALTERNATE_NAMES calpactin I; lipocortin II; p36 ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 31-Mar-1992 #sequence_revision 26-May-1994 #text_change 22-Jun-1999 ACCESSIONS JQ1297 REFERENCE JQ1297 !$#authors Gerke, V.; Koch, W.; Thiel, C. !$#journal Gene (1991) 104:259-264 !$#title Primary structure and expression of the Xenopus laevis gene !1encoding annexin II. !$#cross-references MUID:92009222; PMID:1833269 !$#accession JQ1297 !'##molecule_type mRNA !'##residues 1-340 ##label GER !'##cross-references GB:M60768; NID:g214530; PIDN:AAA49885.1; !1PID:g214531 !'##experimental_source kidney GENETICS !$#gene Anx II-1 CLASSIFICATION #superfamily annexin I; annexin repeat homology KEYWORDS calcium binding; duplication; endonexin fold; inflammation; !1phospholipid binding; phosphoprotein FEATURE !$2-340 #product annexin II type 1 #status predicted #label !8MAT\ !$37-108 #domain annexin repeat homology #label AX1\ !$48-64 #region endonexin fold #status predicted\ !$109-180 #domain annexin repeat homology #label AX2\ !$120-136 #region endonexin fold #status predicted\ !$193-265 #domain annexin repeat homology #label AX3\ !$205-221 #region endonexin fold #status predicted\ !$269-340 #domain annexin repeat homology #label AX4\ !$280-296 #region endonexin fold #status predicted\ !$27 #binding_site phosphate (Thr) (covalent) #status !8predicted SUMMARY #length 340 #molecular-weight 38545 #checksum 1690 SEQUENCE /// ENTRY JQ1298 #type complete TITLE annexin II type 2 - African clawed frog ALTERNATE_NAMES calpactin I; lipocortin II; p36 ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 31-Mar-1992 #sequence_revision 26-May-1994 #text_change 22-Jun-1999 ACCESSIONS JQ1298; A41002; B41002 REFERENCE JQ1297 !$#authors Gerke, V.; Koch, W.; Thiel, C. !$#journal Gene (1991) 104:259-264 !$#title Primary structure and expression of the Xenopus laevis gene !1encoding annexin II. !$#cross-references MUID:92009222; PMID:1833269 !$#accession JQ1298 !'##molecule_type mRNA !'##residues 1-340 ##label GER !'##cross-references GB:M60769; NID:g214532; PIDN:AAA49886.1; !1PID:g214533 !'##experimental_source kidney REFERENCE A41002 !$#authors Izant, J.G.; Bryson, L.J. !$#journal J. Biol. Chem. (1991) 266:18560-18566 !$#title Xenopus annexin II (calpactin I) heavy chain has a distinct !1amino terminus. !$#cross-references MUID:92011609; PMID:1833398 !$#accession A41002 !'##molecule_type mRNA !'##residues 1-222,'HP',225-296,'RN',299-340 ##label IZA !'##cross-references GB:M58575; NID:g214007; PIDN:AAA49664.1; !1PID:g214008; GB:M58576; NID:g214009; PID:g214010 !'##experimental_source ovary; clones A3 and C4 !$#accession B41002 !'##molecule_type mRNA !'##residues 52-222,'HP',225-243,'R',245-257,'S',259-296,'RN',299-340 !1##label IZ2 !'##cross-references GB:M58577 !'##experimental_source ovary; clones E4 and F4 !'##note translation of the nucleotide sequence is not complete GENETICS !$#gene Anx II-2 CLASSIFICATION #superfamily annexin I; annexin repeat homology KEYWORDS calcium binding; duplication; endonexin fold; inflammation; !1phospholipid binding; phosphoprotein FEATURE !$2-340 #product annexin II type 2 #status predicted #label !8MAT\ !$37-108 #domain annexin repeat homology #label AX1\ !$48-64 #region endonexin fold #status predicted\ !$109-180 #domain annexin repeat homology #label AX2\ !$120-136 #region endonexin fold #status predicted\ !$193-265 #domain annexin repeat homology #label AX3\ !$205-221 #region endonexin fold #status predicted\ !$269-340 #domain annexin repeat homology #label AX4\ !$280-296 #region endonexin fold #status predicted\ !$27 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 340 #molecular-weight 38702 #checksum 409 SEQUENCE /// ENTRY LUHU3 #type complete TITLE annexin III - human ALTERNATE_NAMES 1,2-cyclic-inositol-phosphate phosphodiesterase (EC 3.1.4.36); calcimedin 35alpha; lipocortin III; placental anticoagulant protein III ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 22-Jun-1999 ACCESSIONS A47658; B29250; A41213; B31046; A60707 REFERENCE A47658 !$#authors Tait, J.F.; Smith, C.; Xu, L.; Cookson, B.T. !$#journal Genomics (1993) 18:79-86 !$#title Structure and polymorphisms of the human annexin III (ANX3) !1gene. !$#cross-references MUID:94102764; PMID:8276419 !$#accession A47658 !'##status translation not shown !'##molecule_type DNA !'##residues 1-323 ##label RES !'##cross-references GB:L20591; NID:g410200; PIDN:AAA16713.1; !1PID:g410202 REFERENCE A92659 !$#authors Pepinsky, R.B.; Tizard, R.; Mattaliano, R.J.; Sinclair, !1L.K.; Miller, G.T.; Browning, J.L.; Chow, E.P.; Burne, C.; !1Huang, K.S.; Pratt, D.; Wachter, L.; Hession, C.; Frey, !1A.Z.; Wallner, B.P. !$#journal J. Biol. Chem. (1988) 263:10799-10811 !$#title Five distinct calcium and phospholipid binding proteins !1share homology with lipocortin I. !$#cross-references MUID:88273202; PMID:2968983 !$#accession B29250 !'##molecule_type mRNA !'##residues 1-323 ##label PEP !'##cross-references EMBL:M20560; NID:g186967; PIDN:AAA59496.1; !1PID:g307115; EMBL:J03899 REFERENCE A41213 !$#authors Ross, T.S.; Tait, J.F.; Majerus, P.W. !$#journal Science (1990) 248:605-607 !$#title Identity of inositol 1,2-cyclic phosphate 2-phosphohydrolase !1with lipocortin III. !$#cross-references MUID:90239555; PMID:2159184 !$#accession A41213 !'##molecule_type protein !'##residues 41-102;126-138 ##label ROS REFERENCE A90534 !$#authors Tait, J.F.; Sakata, M.; McMullen, B.A.; Miao, C.H.; !1Funakoshi, T.; Hendrickson, L.E.; Fujikawa, K. !$#journal Biochemistry (1988) 27:6268-6276 !$#title Placental anticoagulant proteins: isolation and comparative !1characterization of four members of the lipocortin family. !$#cross-references MUID:89118212; PMID:2975506 !$#accession B31046 !'##molecule_type protein !'##residues 41-79;85-88;104-119;126-128,'X',130-145,'G',147-153,'X', !1155-157,'X',159-160;277-293,'R',295-323 ##label TAI REFERENCE A60707 !$#authors Ernst, J.D.; Hoye, E.; Blackwood, R.A.; Jaye, D. !$#journal J. Clin. Invest. (1990) 85:1065-1071 !$#title Purification and characterization of an abundant cytosolic !1protein from human neutrophils that promotes Ca !1(2+)-dependent aggregation of isolated specific granules. !$#cross-references MUID:90203211; PMID:2138632 !$#accession A60707 !'##molecule_type protein !'##residues 42-55;74-82;105-126;155-169;177-204,'L', !1206-209;264-274;305-315 ##label ERN COMMENT Annexins undergo reversible, calcium-dependent binding to !1membrane phospholipids. Although a number have been !1proposed, the physiological roles of the various annexins !1are not yet fully understood. GENETICS !$#gene GDB:ANX3 !'##cross-references GDB:125900; OMIM:106490 !$#map_position 4q21-4q21 !$#introns 5/3; 35/1; 66/3; 104/3; 135/1; 161/3; 180/3; 212/1; 244/1; !1263/3; 304/3 CLASSIFICATION #superfamily annexin I; annexin repeat homology KEYWORDS calcium binding; duplication; endonexin fold; glycoprotein; !1phospholipid binding; phosphoric diester hydrolase FEATURE !$2-323 #product annexin III #status predicted #label MAT\ !$21-92 #domain annexin repeat homology #label AX1\ !$32-48 #region endonexin fold #status predicted\ !$93-164 #domain annexin repeat homology #label AX2\ !$104-120 #region endonexin fold #status predicted\ !$176-248 #domain annexin repeat homology #label AX3\ !$188-204 #region endonexin fold #status predicted\ !$252-323 #domain annexin repeat homology #label AX4\ !$263-279 #region endonexin fold #status predicted\ !$218 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 323 #molecular-weight 36375 #checksum 515 SEQUENCE /// ENTRY LURT3 #type complete TITLE annexin III - rat ALTERNATE_NAMES 1,2-cyclic-inositol-phosphate phosphodiesterase (EC 3.1.4.36); calcimedin 35alpha; lipocortin III; placental anticoagulant protein III ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 07-Oct-1994 ACCESSIONS A29250 REFERENCE A92659 !$#authors Pepinsky, R.B.; Tizard, R.; Mattaliano, R.J.; Sinclair, !1L.K.; Miller, G.T.; Browning, J.L.; Chow, E.P.; Burne, C.; !1Huang, K.S.; Pratt, D.; Wachter, L.; Hession, C.; Frey, !1A.Z.; Wallner, B.P. !$#journal J. Biol. Chem. (1988) 263:10799-10811 !$#title Five distinct calcium and phospholipid binding proteins !1share homology with lipocortin I. !$#cross-references MUID:88273202; PMID:2968983 !$#accession A29250 !'##molecule_type mRNA !'##residues 1-324 ##label PEP !'##cross-references GB:M20559; GB:J03898 COMMENT Annexins undergo reversible, calcium-dependent binding to !1membrane phospholipids. Although a number have been !1proposed, the physiological roles of the various annexins !1are not yet fully understood. CLASSIFICATION #superfamily annexin I; annexin repeat homology KEYWORDS calcium binding; duplication; endonexin fold; glycoprotein; !1phospholipid binding; phosphoric diester hydrolase FEATURE !$2-324 #product annexin III #status predicted #label MAT\ !$22-93 #domain annexin repeat homology #label AX1\ !$33-49 #region endonexin fold #status predicted\ !$94-165 #domain annexin repeat homology #label AX2\ !$105-121 #region endonexin fold #status predicted\ !$177-249 #domain annexin repeat homology #label AX3\ !$189-205 #region endonexin fold #status predicted\ !$253-324 #domain annexin repeat homology #label AX4\ !$264-280 #region endonexin fold #status predicted\ !$20,219 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 324 #molecular-weight 36363 #checksum 2785 SEQUENCE /// ENTRY A42077 #type complete TITLE annexin IV - human ALTERNATE_NAMES endonexin I; placental anticoagulant protein II; PP4-X protein ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jan-1993 #sequence_revision 26-May-1994 #text_change 22-Jun-1999 ACCESSIONS A42077; B42077; S07434; A31953; A31046 REFERENCE A42077 !$#authors Tait, J.F.; Smith, C.; Frankenberry, D.A.; Miao, C.H.; !1Adler, D.A.; Disteche, C.M. !$#journal Genomics (1992) 12:313-318 !$#title Chromosomal mapping of the human annexin IV (ANX4) gene. !$#cross-references MUID:92155721; PMID:1346776 !$#accession A42077 !'##molecule_type mRNA !'##residues 1-321 ##label TAI !'##cross-references GB:M82809; NID:g178698; PIDN:AAA51740.1; !1PID:g178699 !$#accession B42077 !'##molecule_type DNA !'##residues 87-129 ##label TA2 REFERENCE S07434 !$#authors Grundmann, U.; Amann, E.; Abel, K.J.; Kuepper, H.A. !$#journal Behring Inst. Mitt. (1988) 82:59-67 !$#title Isolation and expression of cDNA coding for a new member of !1the phospholipase A2 inhibitor family. !$#cross-references MUID:88309022; PMID:2970257 !$#accession S07434 !'##status preliminary !'##molecule_type mRNA !'##residues 1-97,'Q',99-321 ##label GRU !'##cross-references EMBL:M19383; NID:g189616; PIDN:AAC41689.1; !1PID:g189617 REFERENCE A92696 !$#authors Ahn, N.G.; Teller, D.C.; Bienkowski, M.J.; McMullen, B.A.; !1Lipkin, E.W.; de Haen, C. !$#journal J. Biol. Chem. (1988) 263:18657-18663 !$#title Sedimentation equilibrium analysis of five !1lipocortin-related phospholipase A-2 inhibitors from human !1placenta. Evidence against a mechanistically relevant !1association between enzyme and inhibitor. !$#cross-references MUID:89066652; PMID:2974032 !$#accession A31953 !'##molecule_type protein !'##residues 29-58;101-126;282-310 ##label AHN REFERENCE A90534 !$#authors Tait, J.F.; Sakata, M.; McMullen, B.A.; Miao, C.H.; !1Funakoshi, T.; Hendrickson, L.E.; Fujikawa, K. !$#journal Biochemistry (1988) 27:6268-6276 !$#title Placental anticoagulant proteins: isolation and comparative !1characterization of four members of the lipocortin family. !$#cross-references MUID:89118212; PMID:2975506 !$#accession A31046 !'##molecule_type protein !'##residues 4-17;30-74;102-146;283-321 ##label TA3 GENETICS !$#gene GDB:ANX4 !'##cross-references GDB:131395; OMIM:106491 !$#map_position 2p13-2p13 !$#introns 102/3 CLASSIFICATION #superfamily annexin I; annexin repeat homology KEYWORDS acetylated amino end; calcium binding; duplication; !1endonexin fold; glycoprotein; phospholipid binding; !1phosphoprotein FEATURE !$2-321 #product annexin IV #status predicted #label MAT\ !$19-90 #domain annexin repeat homology #label AX1\ !$30-46 #region endonexin fold #status predicted\ !$91-162 #domain annexin repeat homology #label AX2\ !$102-118 #region endonexin fold #status predicted\ !$174-246 #domain annexin repeat homology #label AX3\ !$186-202 #region endonexin fold #status predicted\ !$250-321 #domain annexin repeat homology #label AX4\ !$261-277 #region endonexin fold #status predicted\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status predicted\ !$9 #binding_site phosphate (Thr) (covalent) (by protein !8kinase C) #status predicted\ !$247 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 321 #molecular-weight 36085 #checksum 6685 SEQUENCE /// ENTRY LUBO4 #type complete TITLE annexin IV - bovine ALTERNATE_NAMES 32K calelectrin; chromobindin IV; endonexin; lipocortin IV; protein II ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 22-Jun-1999 ACCESSIONS A31578; D45066; S59624; A45066; B45066; C45066; F45066; !1G45066; H45066 REFERENCE A31578 !$#authors Hamman, H.C.; Gaffey, L.C.; Lynch, K.R.; Creutz, C.E. !$#journal Biochem. Biophys. Res. Commun. (1988) 156:660-667 !$#title Cloning and characterization of a cDNA encoding bovine !1endonexin (chromobindin 4). !$#cross-references MUID:89050088; PMID:2847715 !$#accession A31578 !'##molecule_type mRNA !'##residues 1-319 ##label HAM !'##cross-references GB:X13627; NID:g215; PIDN:CAA31954.1; PID:g216; !1GB:M22248; NID:g163029; PID:g163030 REFERENCE A45066 !$#authors Kojima, K.; Ogawa, H.K.; Seno, N.; Yamamoto, K.; Irimura, !1T.; Osawa, T.; Matsumoto, I. !$#journal J. Biol. Chem. (1992) 267:20536-20539 !$#title Carbohydrate-binding proteins in bovine kidney have !1consensus amino acid sequences of annexin family proteins. !$#cross-references MUID:93015942; PMID:1400371 !$#accession D45066 !'##molecule_type protein !'##residues 10-18,'X',20-22,'X',24-25;29-48;101-107,'X',109-118;'X', !1194-197,'Y',199,'X',201,'X',204-212;260-288 ##label KOJ !'##experimental_source kidney !'##note sequence extracted from NCBI backbone (NCBIP:116211, !1NCBIP:116208, NCBIP:116209, NCBIP:116210, NCBIP:116213, !1NCBIP:116214, NCBIP:116215) !'##note these fragments are derived from a 33K protein that exhibited !1Ca++-dependent binding to carbohydrate !'##note 12-Met and 12-Tyr were also found REFERENCE S59624 !$#authors Sohma, H.; Matsushima, N.; Watanabe, T.; Hattori, A.; !1Kuroki, Y.; Akino, T. !$#journal Biochem. J. (1995) 312:175-181 !$#title Ca(2+)-dependent binding of annexin IV to surfactant protein !1A and lamellar bodies in alveolar type II cells. !$#cross-references MUID:96077142; PMID:7492310 !$#accession S59624 !'##status preliminary !'##molecule_type protein !'##residues 29-44;72-77;112-119;163-180;181-190;226-235 ##label SOH COMMENT Annexins undergo reversible, calcium-dependent binding to !1membrane phospholipids. Although a number have been !1proposed, the physiological roles of the various annexins !1are not yet fully understood. CLASSIFICATION #superfamily annexin I; annexin repeat homology KEYWORDS calcium binding; duplication; endonexin fold; glycoprotein; !1phospholipid binding; phosphoprotein FEATURE !$2-319 #product annexin IV #status predicted #label MAT\ !$17-88 #domain annexin repeat homology #label AX1\ !$28-44 #region endonexin fold #status predicted\ !$89-160 #domain annexin repeat homology #label AX2\ !$100-116 #region endonexin fold #status predicted\ !$172-244 #domain annexin repeat homology #label AX3\ !$184-200 #region endonexin fold #status predicted\ !$248-319 #domain annexin repeat homology #label AX4\ !$259-275 #region endonexin fold #status predicted\ !$7 #binding_site phosphate (Thr) (covalent) (by protein !8kinase C) #status predicted\ !$125,245 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 319 #molecular-weight 35888 #checksum 9592 SEQUENCE /// ENTRY LUPG4 #type complete TITLE annexin IV - pig ALTERNATE_NAMES 32K calelectrin; chromobindin IV; endonexin; lipocortin IV; protein II ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 24-Nov-1999 ACCESSIONS A27107 REFERENCE A27107 !$#authors Weber, K.; Johnsson, N.; Plessmann, U.; Van, P.N.; Soling, !1H.D.; Ampe, C.; Vandekerckhove, J. !$#journal EMBO J. (1987) 6:1599-1604 !$#title The amino acid sequence of protein II and its !1phosphorylation site for protein kinase C; the domain !1structure Ca2+-modulated lipid binding proteins. !$#cross-references MUID:87275850; PMID:2956093 !$#accession A27107 !'##molecule_type protein !'##residues 1-318 ##label WEB !'##experimental_source intestinal epithelium COMMENT Annexins undergo reversible, calcium-dependent binding to !1membrane phospholipids. Although a number have been !1proposed, the physiological roles of the various annexins !1are not yet fully understood. CLASSIFICATION #superfamily annexin I; annexin repeat homology KEYWORDS blocked amino end; calcium binding; duplication; endonexin !1fold; glycoprotein; phospholipid binding; phosphoprotein FEATURE !$16-87 #domain annexin repeat homology #label AX1\ !$27-43 #region endonexin fold #status predicted\ !$88-159 #domain annexin repeat homology #label AX2\ !$99-115 #region endonexin fold #status predicted\ !$171-243 #domain annexin repeat homology #label AX3\ !$183-199 #region endonexin fold #status predicted\ !$247-318 #domain annexin repeat homology #label AX4\ !$258-274 #region endonexin fold #status predicted\ !$1 #modified_site blocked amino end (Ala) (probably !8acetylated) #status experimental\ !$6 #binding_site phosphate (Thr) (covalent) (by protein !8kinase C) #status predicted\ !$124,244 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 318 #molecular-weight 35697 #checksum 354 SEQUENCE /// ENTRY AQHUP #type complete TITLE annexin V [validated] - human ALTERNATE_NAMES endonexin II; lipocortin V; placental anticoagulant protein; placental protein 4 ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 08-Dec-2000 ACCESSIONS D29250; A30206; A28076; S01016; A29417; A41514; A28038; !1C31953; S06646; A29670; I37172; B28038; C28038; D28038 REFERENCE A92659 !$#authors Pepinsky, R.B.; Tizard, R.; Mattaliano, R.J.; Sinclair, !1L.K.; Miller, G.T.; Browning, J.L.; Chow, E.P.; Burne, C.; !1Huang, K.S.; Pratt, D.; Wachter, L.; Hession, C.; Frey, !1A.Z.; Wallner, B.P. !$#journal J. Biol. Chem. (1988) 263:10799-10811 !$#title Five distinct calcium and phospholipid binding proteins !1share homology with lipocortin I. !$#cross-references MUID:88273202; PMID:2968983 !$#accession D29250 !'##molecule_type mRNA !'##residues 1-320 ##label PEP !'##cross-references GB:M21731; NID:g186969; PIDN:AAA36166.1; !1PID:g307116 REFERENCE A30206 !$#authors Grundmann, U.; Abel, K.J.; Bohn, H.; Loebermann, H.; !1Lottspeich, F.; Kuepper, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:3708-3712 !$#title Characterization of cDNA encoding human placental !1anticoagulant protein (PP4): homology with the lipocortin !1family. !$#cross-references MUID:88234495; PMID:2967495 !$#accession A30206 !'##molecule_type mRNA !'##residues 1-320 ##label GRU !'##cross-references GB:M19384; NID:g189614; PIDN:AAB59545.1; !1PID:g189615 REFERENCE A28076 !$#authors Kaplan, R.; Jaye, M.; Burgess, W.H.; Schlaepfer, D.D.; !1Haigler, H.T. !$#journal J. Biol. Chem. (1988) 263:8037-8043 !$#title Cloning and expression of cDNA for human endonexin II, a Ca !1(2+) and phospholipid binding protein. !$#cross-references MUID:88228020; PMID:2967291 !$#accession A28076 !'##molecule_type mRNA !'##residues 1-320 ##label KAP !'##cross-references GB:J03745; NID:g182111; PIDN:AAA52386.1; !1PID:g182112 REFERENCE S01016 !$#authors Maurer-Fogy, I.; Reutelingsperger, C.P.M.; Pieters, J.; !1Bodo, G.; Stratowa, C.; Hauptmann, R. !$#journal Eur. J. Biochem. (1988) 174:585-592 !$#title Cloning and expression of cDNA for human vascular !1anticoagulant, a Ca-dependent phospholipid-binding protein. !$#cross-references MUID:88271329; PMID:2455636 !$#accession S01016 !'##molecule_type mRNA !'##residues 1-320 ##label MAU !'##cross-references EMBL:X12454; NID:g37636; PIDN:CAA30985.1; !1PID:g37637 !'##note part of this sequence was confirmed by protein sequencing REFERENCE A29417 !$#authors Funakoshi, T.; Hendrickson, L.E.; McMullen, B.A.; Fujikawa, !1K. !$#journal Biochemistry (1987) 26:8087-8092 !$#title Primary structure of human placental anticoagulant protein. !$#cross-references MUID:88163463; PMID:2964863 !$#contents amino-terminal acetylation !$#accession A29417 !'##molecule_type mRNA !'##residues 1-320 ##label FUN !'##cross-references EMBL:M18366; NID:g179131; PIDN:AAA35570.1; !1PID:g179132 REFERENCE A41514 !$#authors Iwasaki, A.; Suda, M.; Nakao, H.; Nagoya, T.; Saino, Y.; !1Arai, K.; Mizoguchi, T.; Sato, F.; Yoshizaki, H.; Hirata, !1M.; Miyata, T.; Shidara, Y.; Murata, M.; Maki, M. !$#journal J. Biochem. (1987) 102:1261-1273 !$#title Structure and expression of cDNA for an inhibitor of blood !1coagulation isolated from human placenta: a new !1lipocortin-like protein. !$#cross-references MUID:88139278; PMID:2963810 !$#accession A41514 !'##molecule_type mRNA !'##residues 1-320 ##label IWA !'##cross-references GB:D00172; NID:g219480; PIDN:BAA00122.1; !1PID:g219481 !'##note part of this sequence was confirmed by protein sequencing REFERENCE A28038 !$#authors Schlaepfer, D.D.; Mehlman, T.; Burgess, W.H.; Haigler, H.T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:6078-6082 !$#title Structural and functional characterization of endonexin II, !1a calcium- and phospholipid-binding protein. !$#cross-references MUID:87317598; PMID:2957692 !$#accession A28038 !'##molecule_type protein !'##residues 86-131,'W',260-272,274-297,300-315,'X',317-320 ##label SCH REFERENCE A92696 !$#authors Ahn, N.G.; Teller, D.C.; Bienkowski, M.J.; McMullen, B.A.; !1Lipkin, E.W.; de Haen, C. !$#journal J. Biol. Chem. (1988) 263:18657-18663 !$#title Sedimentation equilibrium analysis of five !1lipocortin-related phospholipase A-2 inhibitors from human !1placenta. Evidence against a mechanistically relevant !1association between enzyme and inhibitor. !$#cross-references MUID:89066652; PMID:2974032 !$#accession C31953 !'##molecule_type protein !'##residues 85-93 ##label AHN REFERENCE S06646 !$#authors Rothhut, B.; Comera, C.; Cortial, S.; Haumont, P.Y.; Diep !1Le, K.H.; Cavadore, J.C.; Conard, J.; Russo-Marie, F.; !1Lederer, F. !$#journal Biochem. J. (1989) 263:929-935 !$#title A 32 kDa lipocortin from human mononuclear cells appears to !1be identical with the placental inhibitor of blood !1coagulation. !$#cross-references MUID:90088443; PMID:2532007 !$#accession S06646 !'##molecule_type protein !'##residues 7-25;27-42;51-74,'X', !176-151;181-198;202-207;209-226;228-238;246-271;277-282; !1286-302,'X',304-309;311-320 ##label ROT REFERENCE A37250 !$#authors Huber, R.; Schneider, M.; Mayr, I.; Roemisch, J.; Paques, !1E.P. !$#journal FEBS Lett. (1990) 275:15-21 !$#title The calcium binding sites in human annexin V by crystal !1structure analysis at 2.0 A resolution. !$#cross-references MUID:91085549; PMID:2148156 !$#contents annotation; X-ray crystallography, 2.0 angstroms !$#note three calcium ions are strongly bound at sites in the first, !1second, and fourth repeats; there are also two weak !1calcium-binding sites REFERENCE A29670 !$#authors Funakoshi, T.; Heimark, R.L.; Hendrickson, L.E.; McMullen, !1B.A.; Fujikawa, K. !$#journal Biochemistry (1987) 26:5572-5578 !$#title Human placental anticoagulant protein: isolation and !1characterization. !$#cross-references MUID:88050845; PMID:2960376 !$#accession A29670 !'##molecule_type protein !'##residues 29-73;274-297;300-320 ##label FU2 REFERENCE I37172 !$#authors Fernandez, M.P.; Morgan, R.O.; Fernandez, M.R.; Carcedo, !1M.T. !$#journal Gene (1994) 149:253-260 !$#title The gene encoding human annexin V has a TATA-less promoter !1with a high G+C content. !$#cross-references MUID:95047484; PMID:7958998 !$#accession I37172 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-320 ##label RES !'##cross-references EMBL:U01691; NID:g430964; PIDN:AAB40047.1; !1PID:g430966 COMMENT Annexins undergo reversible, calcium-dependent binding to !1membrane phospholipids. Although a number have been !1proposed, the physiological roles of the various annexins !1are not yet fully understood. COMMENT Annexin V has been proposed to play a role in the inhibition !1of blood coagulation. The purified protein inhibits the !1thromboplastin-mediated extrinsic pathway of coagulation !1through phospholipid-binding rather than proteolytic !1inactivation. It does not affect thrombin-dependent fibrin !1formation. GENETICS !$#gene GDB:ANX5 !'##cross-references GDB:120555; OMIM:131230 !$#map_position 4q26-4q28 !$#introns 3/3; 32/1; 63/3; 101/3; 132/1; 158/3; 177/3; 209/1; 241/1; !1260/3; 301/3 CLASSIFICATION #superfamily annexin I; annexin repeat homology KEYWORDS acetylated amino end; anticoagulant; calcium binding; !1duplication; endonexin fold; membrane-associated protein; !1phospholipid binding; phosphoprotein FEATURE !$2-320 #product annexin V #status experimental #label MAT\ !$18-89 #domain annexin repeat homology #label AX1\ !$29-45 #region endonexin fold #status predicted\ !$90-161 #domain annexin repeat homology #label AX2\ !$101-117 #region endonexin fold #status predicted\ !$173-245 #domain annexin repeat homology #label AX3\ !$185-201 #region endonexin fold #status predicted\ !$249-320 #domain annexin repeat homology #label AX4\ !$260-276 #region endonexin fold #status predicted\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental\ !$23 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$28,30,32,72 #binding_site calcium, high affinity (Met, Gly, Gly, !8Glu) #status experimental\ !$33,35,36 #binding_site calcium, low affinity (Thr, Glu, Glu) !8#status experimental\ !$73,78 #binding_site calcium, low affinity (Leu, Glu) !8#status experimental\ !$100,102,104,144 #binding_site calcium, high affinity (Leu, Gly, Gly, !8Asp) #status experimental\ !$259,261,263,303 #binding_site calcium, high affinity (Met, Gly, Gly, !8Asp) #status experimental SUMMARY #length 320 #molecular-weight 35936 #checksum 2349 SEQUENCE /// ENTRY S27214 #type complete TITLE annexin V - bovine ALTERNATE_NAMES CaBP33; CaBP37 ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 08-Jun-1994 #sequence_revision 10-Feb-1995 #text_change 26-Feb-1999 ACCESSIONS S27214; S27215 REFERENCE S27214 !$#authors Learmonth, M.P.; Howell, S.A.; Harris, A.C.M.; Amess, B.; !1Patel, Y.; Giambanco, I.; Bianchi, R.; Pula, G.; Ceccarelli, !1P.; Donato, R.; Green, B.N.; Aitken, A. !$#journal Biochim. Biophys. Acta (1992) 1160:76-83 !$#title Novel isoforms of CaBP 33/37 (Annexin V) from mammalian !1brain: structural and phosphorylation differences that !1suggest distinct biological roles. !$#cross-references MUID:93041974; PMID:1420335 !$#accession S27214 !'##molecule_type protein !'##residues 1-320 ##label LEA !$#accession S27215 !'##molecule_type protein !'##residues 1-35,'T',37-124,'E',126-320 ##label LE2 !'##note It is uncertain whether the sequence differences are due to !1allelic variation or multiple genes COMMENT Annexins undergo reversible, calcium-dependent binding to !1membrane phospholipids. Although a number have been !1proposed, the physiological roles of the various annexins !1are not yet fully understood. COMMENT Annexin V has been proposed to play a role in the inhibition !1of blood coagulation. The purified protein inhibits the !1thromboplastin-mediated extrinsic pathway of coagulation !1through phospholipid-binding rather than proteolytic !1inactivation. It does not affect thrombin-dependent fibrin !1formation. CLASSIFICATION #superfamily annexin I; annexin repeat homology KEYWORDS acetylated amino end; anticoagulant; calcium binding; !1duplication; endonexin fold; membrane-associated protein; !1phospholipid binding; phosphoprotein FEATURE !$17-88 #domain annexin repeat homology #label AX1\ !$28-44 #region endonexin fold #status predicted\ !$89-160 #domain annexin repeat homology #label AX2\ !$100-116 #region endonexin fold #status predicted\ !$172-244 #domain annexin repeat homology #label AX3\ !$184-200 #region endonexin fold #status predicted\ !$248-319 #domain annexin repeat homology #label AX4\ !$259-275 #region endonexin fold #status predicted\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$22 #binding_site phosphate (Thr) (covalent) #status !8experimental\ !$27,29,31,71 #binding_site calcium, high affinity (Met, Gly, Gly, !8Glu) #status predicted\ !$32,34,35 #binding_site calcium, low affinity (Thr, Glu, Glu) !8#status predicted\ !$72,77 #binding_site calcium, low affinity (Leu, Glu) !8#status predicted\ !$99,101,103,143 #binding_site calcium, high affinity (Leu, Gly, Gly, !8Asp) #status predicted\ !$258,260,262,302 #binding_site calcium, high affinity (Met, Gly, Gly, !8Asp) #status predicted SUMMARY #length 320 #molecular-weight 35942 #checksum 4340 SEQUENCE /// ENTRY LURT5 #type complete TITLE annexin V - rat ALTERNATE_NAMES endonexin II; lipocortin V; placental anticoagulant protein; placental protein 4 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 22-Jun-1999 ACCESSIONS C29250; S66680 REFERENCE A92659 !$#authors Pepinsky, R.B.; Tizard, R.; Mattaliano, R.J.; Sinclair, !1L.K.; Miller, G.T.; Browning, J.L.; Chow, E.P.; Burne, C.; !1Huang, K.S.; Pratt, D.; Wachter, L.; Hession, C.; Frey, !1A.Z.; Wallner, B.P. !$#journal J. Biol. Chem. (1988) 263:10799-10811 !$#title Five distinct calcium and phospholipid binding proteins !1share homology with lipocortin I. !$#cross-references MUID:88273202; PMID:2968983 !$#accession C29250 !'##molecule_type mRNA !'##residues 1-319 ##label PEP !'##cross-references GB:M21730; NID:g205138; PIDN:AAA41512.1; !1PID:g205139 REFERENCE S66680 !$#authors Imai, Y.; Kohsaka, S. !$#journal Eur. J. Biochem. (1995) 232:327-334 !$#title Structure of rat annexin V gene and molecular diversity of !1its transcripts. !$#cross-references MUID:96035863; PMID:7556178 !$#accession S66680 !'##status preliminary; translation not shown !'##molecule_type DNA !'##residues 1-319 ##label IMA !'##cross-references EMBL:D42136 COMMENT Annexins undergo reversible, calcium-dependent binding to !1membrane phospholipids. Although a number have been !1proposed, the physiological roles of the various annexins !1are not yet fully understood. COMMENT Annexin V has been proposed to play a role in the inhibition !1of blood coagulation. The purified protein inhibits the !1thromboplastin-mediated extrinsic pathway of coagulation !1through phospholipid-binding rather than proteolytic !1inactivation. It does not affect thrombin-dependent fibrin !1formation. GENETICS !$#introns 1/3; 30/1; 61/3; 99/3; 130/1; 156/3; 175/3; 207/1; 239/1; !1258/3; 299/3 CLASSIFICATION #superfamily annexin I; annexin repeat homology KEYWORDS calcium binding; duplication; endonexin fold; !1membrane-associated protein; phospholipid binding FEATURE !$2-319 #product annexin V #status predicted #label MAT\ !$16-87 #domain annexin repeat homology #label AX1\ !$27-43 #region endonexin fold #status predicted\ !$88-159 #domain annexin repeat homology #label AX2\ !$99-115 #region endonexin fold #status predicted\ !$171-243 #domain annexin repeat homology #label AX3\ !$183-199 #region endonexin fold #status predicted\ !$247-318 #domain annexin repeat homology #label AX4\ !$258-274 #region endonexin fold #status predicted\ !$26,28,30,70 #binding_site calcium, high affinity (Met, Gly, Gly, !8Glu) #status predicted\ !$31,33,34 #binding_site calcium, low affinity (Thr, Glu, Asp) !8#status predicted\ !$71,76 #binding_site calcium, low affinity (Leu, Glu) !8#status predicted\ !$98,100,102,142 #binding_site calcium, high affinity (Leu, Gly, Gly, !8Asp) #status predicted\ !$257,259,261,301 #binding_site calcium, high affinity (Met, Gly, Gly, !8Asp) #status predicted SUMMARY #length 319 #molecular-weight 35744 #checksum 9709 SEQUENCE /// ENTRY LUCH5 #type complete TITLE annexin V - chicken ALTERNATE_NAMES anchorin CII; endonexin II; lipocortin V; placental anticoagulant protein; placental protein 4 ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 02-Jun-2000 ACCESSIONS A35381; A28623; B40404; S32523; S08771 REFERENCE A35381 !$#authors Fernandez, M.P.; Selmin, O.; Martin, G.R.; Yamada, Y.; !1Pfaeffle, M.; Deutzmann, R.; Mollenhauer, J.; von der Mark, !1K. !$#journal J. Biol. Chem. (1990) 265:8344 !$#cross-references MUID:90243721; PMID:2159478 !$#contents erratum !$#accession A35381 !'##molecule_type mRNA !'##residues 1-321 ##label FER !'##cross-references GB:M30971; GB:J03194; NID:g211138; PIDN:AAA48591.1; !1PID:g211139 REFERENCE A28623 !$#authors Fernandez, M.P.; Selmin, O.; Martin, G.R.; Yamada, Y.; !1Pfaeffle, M.; Deutzmann, R.; Mollenhauer, J.; von der Mark, !1K. !$#journal J. Biol. Chem. (1988) 263:5921-5925 !$#title The structure of anchorin CII, a collagen binding protein !1isolated from chondrocyte membrane. !$#cross-references MUID:88186917; PMID:2833522 !$#accession A28623 !'##molecule_type mRNA !'##residues 1-118,'LLKCRILNRFNMQEYEANLGRNKITGRRHQAIFRDCWWSCCRQIEI', !1163-167,'E',169-321 ##label FE2 !'##cross-references GB:M30971; GB:J03194; NID:g211138 REFERENCE A40404 !$#authors Genge, B.R.; Wu, L.N.Y.; Adkisson IV, H.D.; Wuthier, R.E. !$#journal J. Biol. Chem. (1991) 266:10678-10685 !$#title Matrix vesicle annexins exhibit proteolipid-like properties. !1Selective partitioning into lipophilic solvents under acidic !1conditions. !$#cross-references MUID:91244852; PMID:2037607 !$#accession B40404 !'##molecule_type protein !'##residues 188-199 ##label GEN !'##experimental_source epiphyseal growth plate cartilage (matrix !1vesicle-enriched microsomes) REFERENCE S32523 !$#authors Boustead, C.M.; Brown, R.; Walker, J.H. !$#journal Biochem. J. (1993) 291:601-608 !$#title Isolation, characterization and localization of annexin V !1from chicken liver. !$#cross-references MUID:93249384; PMID:8484740 !$#accession S32523 !'##status preliminary !'##molecule_type protein !'##residues 6-20;85,'X',87-88,'X',90-93,'X',95-96,'XX',99-100,'X', !1102-103,'XX',106-107;130-137 ##label BOU COMMENT Annexins undergo reversible, calcium-dependent binding to !1membrane phospholipids. Although a number have been !1proposed, the physiological roles of the various annexins !1are not yet fully understood. COMMENT Annexin V has been proposed to play a role in the inhibition !1of blood coagulation. The purified protein inhibits the !1thromboplastin-mediated extrinsic pathway of coagulation !1through phospholipid-binding rather than proteolytic !1inactivation. It does not affect thrombin-dependent fibrin !1formation. CLASSIFICATION #superfamily annexin I; annexin repeat homology KEYWORDS calcium binding; collagen binding; duplication; endonexin !1fold; membrane-associated protein; phospholipid binding FEATURE !$2-321 #product annexin V #status predicted #label MAT\ !$18-89 #domain annexin repeat homology #label AX1\ !$29-45 #region endonexin fold #status predicted\ !$90-161 #domain annexin repeat homology #label AX2\ !$101-117 #region endonexin fold #status predicted\ !$173-245 #domain annexin repeat homology #label AX3\ !$185-201 #region endonexin fold #status predicted\ !$249-320 #domain annexin repeat homology #label AX4\ !$260-276 #region endonexin fold #status predicted\ !$28,30,32,72 #binding_site calcium, high affinity (Met, Gly, Gly, !8Glu) #status predicted\ !$33,35,36 #binding_site calcium, low affinity (Thr, Glu, Glu) !8#status predicted\ !$73,78 #binding_site calcium, low affinity (Leu, Glu) !8#status predicted\ !$100,102,104,144 #binding_site calcium, high affinity (Ile, Gly, Gly, !8Glu) #status predicted\ !$259,261,263,303 #binding_site calcium, high affinity (Met, Gly, Gly, !8Asp) #status predicted SUMMARY #length 321 #molecular-weight 36198 #checksum 3658 SEQUENCE /// ENTRY LUHU8 #type complete TITLE annexin VIII - human ALTERNATE_NAMES vascular anticoagulant beta ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 22-Jun-1999 ACCESSIONS S06476; A38847 REFERENCE S06476 !$#authors Hauptmann, R.; Maurer-Fogy, I.; Krystek, E.; Bodo, G.; !1Andree, H.; Reutelingsperger, C.P.M. !$#journal Eur. J. Biochem. (1989) 185:63-71 !$#title Vascular anticoagulant beta: a novel human Ca(2+)/ !1phospholipid binding protein that inhibits coagulation and !1phospholipase A(2) activity. Its molecular cloning, !1expression and comparison with VAC-alpha. !$#cross-references MUID:90032687; PMID:2530088 !$#accession S06476 !'##molecule_type mRNA !'##residues 1-327 ##label HAU !'##cross-references EMBL:X16662 !'##note the sequence from Fig. 3 is inconsistent with that in Fig. 1 in !1lacking 208-Arg !'##note 6-Ala was also found !'##note 77-Ala, 80-Ala, 96-Ala, 122-Ala were also found REFERENCE A38847 !$#authors Chang, K.S.; Wang, G.; Freireich, E.J.; Daly, M.; Naylor, !1S.L.; Trujillo, J.M.; Stass, S.A. !$#journal Blood (1992) 79:1802-1810 !$#title Specific expression of the annexin VIII gene in acute !1promyelocytic leukemia. !$#cross-references MUID:92216091; PMID:1313714 !$#accession A38847 !'##molecule_type mRNA !'##residues 1-57,'T',59-82,'L',84-156,'S',158-176,'G',178-312,'RY', !1315-327 ##label CHA !'##cross-references GB:M81844; NID:g178700; PIDN:AAB46383.1; !1PID:g178701 !'##note the authors translated the codon TTG for residue 83 as Phe, AGT !1for residue 157 as Arg, and AGG for residue 313 as Gly !'##note the authors state that the protein sequence differs from that !1in reference S06476 only in having 58-Thr and 177-Gly COMMENT Annexins undergo reversible, calcium-dependent binding to !1membrane phospholipids. Although a number have been !1proposed, the physiological roles of the various annexins !1are not yet fully understood. GENETICS !$#gene GDB:ANX8 !'##cross-references GDB:128069 !$#map_position 10q11.2-10q11.2 CLASSIFICATION #superfamily annexin I; annexin repeat homology KEYWORDS calcium binding; duplication; endonexin fold; phospholipid !1binding FEATURE !$2-327 #product annexin VIII #status predicted #label MAT\ !$24-95 #domain annexin repeat homology #label AX1\ !$35-51 #region endonexin fold #status predicted\ !$96-167 #domain annexin repeat homology #label AX2\ !$107-123 #region endonexin fold #status predicted\ !$180-252 #domain annexin repeat homology #label AX3\ !$192-208 #region endonexin fold #status predicted\ !$256-327 #domain annexin repeat homology #label AX4\ !$267-283 #region endonexin fold #status predicted SUMMARY #length 327 #molecular-weight 36895 #checksum 8264 SEQUENCE /// ENTRY LUFF9 #type fragment TITLE annexin IX - fruit fly (Drosophila melanogaster) (fragment) ORGANISM #formal_name Drosophila melanogaster DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 22-Jun-1999 ACCESSIONS A42234 REFERENCE A42234 !$#authors Johnston, P.A.; Perin, M.S.; Reynolds, G.A.; Wasserman, !1S.A.; Suedhof, T.C. !$#journal J. Biol. Chem. (1990) 265:11382-11388 !$#title Two novel annexins from Drosophila melanogaster. Cloning, !1characterization, and differential expression in !1development. !$#cross-references MUID:90293092; PMID:2141610 !$#accession A42234 !'##molecule_type mRNA !'##residues 1-296 ##label JOH !'##cross-references GB:M34068; GB:J05501; NID:g156926; PIDN:AAA28370.1; !1PID:g156927 COMMENT Annexins undergo reversible, calcium-dependent binding to !1membrane phospholipids. Although a number have been !1proposed, the physiological roles of the various annexins !1are not yet fully understood. GENETICS !$#gene FlyBase:AnnIX !'##cross-references FlyBase:FBgn0000083 !$#map_position 3 93B CLASSIFICATION #superfamily annexin I; annexin repeat homology KEYWORDS calcium binding; duplication; endonexin fold; phospholipid !1binding FEATURE !$1-66 #domain annexin repeat homology (fragment) #label !8AX1\ !$7-23 #region endonexin fold #status predicted\ !$68-139 #domain annexin repeat homology #label AX2\ !$79-95 #region endonexin fold #status predicted\ !$151-223 #domain annexin repeat homology #label AX3\ !$163-179 #region endonexin fold #status predicted\ !$227-296 #domain annexin repeat homology #label AX4\ !$238-254 #region endonexin fold #status predicted SUMMARY #length 296 #checksum 1926 SEQUENCE /// ENTRY LUFF10 #type complete TITLE annexin X - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 22-Jun-1999 ACCESSIONS B42234 REFERENCE A42234 !$#authors Johnston, P.A.; Perin, M.S.; Reynolds, G.A.; Wasserman, !1S.A.; Suedhof, T.C. !$#journal J. Biol. Chem. (1990) 265:11382-11388 !$#title Two novel annexins from Drosophila melanogaster. Cloning, !1characterization, and differential expression in !1development. !$#cross-references MUID:90293092; PMID:2141610 !$#accession B42234 !'##molecule_type mRNA !'##residues 1-321 ##label JOH !'##cross-references GB:M34069; GB:J05501; NID:g156928; PIDN:AAA28371.1; !1PID:g156929 COMMENT Annexins undergo reversible, calcium-dependent binding to !1membrane phospholipids. Although a number have been !1proposed, the physiological roles of the various annexins !1are not yet fully understood. GENETICS !$#gene FlyBase:AnnX !'##cross-references FlyBase:FBgn0000084 !$#map_position X 19A-4,7 CLASSIFICATION #superfamily annexin I; annexin repeat homology KEYWORDS calcium binding; duplication; endonexin fold; phospholipid !1binding FEATURE !$2-321 #product annexin X #status predicted #label MAT\ !$18-89 #domain annexin repeat homology #label AX1\ !$29-45 #region endonexin fold #status predicted\ !$90-161 #domain annexin repeat homology #label AX2\ !$101-117 #region endonexin fold #status predicted\ !$174-246 #domain annexin repeat homology #label AX3\ !$186-202 #region endonexin fold #status predicted\ !$250-321 #domain annexin repeat homology #label AX4\ !$261-277 #region endonexin fold #status predicted SUMMARY #length 321 #molecular-weight 35705 #checksum 6851 SEQUENCE /// ENTRY LUJF12 #type complete TITLE annexin XII - Hydra vulgaris ORGANISM #formal_name Hydra vulgaris DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 22-Jun-1999 ACCESSIONS A42660; B42660 REFERENCE A42660 !$#authors Schlaepfer, D.D.; Fisher, D.A.; Brandt, M.E.; Bode, H.R.; !1Jones, J.M.; Haigler, H.T. !$#journal J. Biol. Chem. (1992) 267:9529-9539 !$#title Identification of a novel annexin in Hydra vulgaris. !1Characterization, cDNA cloning, and protein kinase C !1phosphorylation of annexin XII. !$#cross-references MUID:92250599; PMID:1339458 !$#accession A42660 !'##molecule_type mRNA !'##residues 1-316 ##label SCH !'##cross-references GB:M83736; NID:g159255; PIDN:AAA29206.1; !1PID:g159256 !$#accession B42660 !'##molecule_type protein !'##residues 2-9,'D',11-30;246-251,'E' ##label SC2 COMMENT Annexins undergo reversible, calcium-dependent binding to !1membrane phospholipids. Although a number have been !1proposed, the physiological roles of the various annexins !1are not yet fully understood. CLASSIFICATION #superfamily annexin I; annexin repeat homology KEYWORDS calcium binding; duplication; endonexin fold; glycoprotein; !1phospholipid binding; phosphoprotein FEATURE !$2-316 #product annexin IV #status experimental #label MAT\ !$16-87 #domain annexin repeat homology #label AX1\ !$27-43 #region endonexin fold #status predicted\ !$88-159 #domain annexin repeat homology #label AX2\ !$99-115 #region endonexin fold #status predicted\ !$171-243 #domain annexin repeat homology #label AX3\ !$183-199 #region endonexin fold #status predicted\ !$247-316 #domain annexin repeat homology #label AX4\ !$258-274 #region endonexin fold #status predicted\ !$6 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$216 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 316 #molecular-weight 35108 #checksum 8489 SEQUENCE /// ENTRY LUHUIS #type complete TITLE annexin XIII, intestinal [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 08-Dec-2000 ACCESSIONS A41733; S18162 REFERENCE A41733 !$#authors Wice, B.M.; Gordon, J.I. !$#journal J. Cell Biol. (1992) 116:405-422 !$#title A strategy for isolation of cDNAs encoding proteins !1affecting human intestinal epithelial cell growth and !1differentiation: characterization of a novel gut-specific !1N-myristoylated annexin. !$#cross-references MUID:92112982; PMID:1530946 !$#accession A41733 !'##molecule_type mRNA !'##residues 1-316 ##label WIC !'##cross-references EMBL:Z11502; NID:g33979; PIDN:CAA77578.1; !1PID:g33980 COMMENT Annexins undergo reversible, calcium-dependent binding to !1membrane phospholipids. Although a number have been !1proposed, the physiological roles of the various annexins !1are not yet fully understood. GENETICS !$#gene GDB:ANXA13 !'##cross-references GDB:9836021; OMIM:602573 !$#map_position 8q24.1-8q24.2 CLASSIFICATION #superfamily annexin I; annexin repeat homology KEYWORDS blocked amino end; calcium binding; duplication; endonexin !1fold; lipoprotein; myristylation; phospholipid binding FEATURE !$2-316 #product annexin intestine-specific #status !8experimental #label MAT\ !$17-88 #domain annexin repeat homology #label AX1\ !$28-44 #region endonexin fold #status predicted\ !$89-160 #domain annexin repeat homology #label AX2\ !$100-116 #region endonexin fold #status predicted\ !$172-244 #domain annexin repeat homology #label AX3\ !$184-200 #region endonexin fold #status predicted\ !$248-316 #domain annexin repeat homology #label AX4\ !$259-275 #region endonexin fold #status predicted\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status experimental\ !$3 #modified_site aspartic acid (Asn) #status predicted SUMMARY #length 316 #molecular-weight 35463 #checksum 7382 SEQUENCE /// ENTRY LUHU7 #type complete TITLE annexin VII, long form - human ALTERNATE_NAMES synexin CONTAINS annexin VII, long form; annexin VII, short form ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1992 #sequence_revision 26-Jan-1996 #text_change 22-Jun-1999 ACCESSIONS A54467; A32554; A39513; B39513 REFERENCE A54467 !$#authors Shirvan, A.; Srivastava, M.; Wang, M.G.; Cultraro, C.; !1Magendzo, K.; McBride, O.W.; Pollard, H.B.; Burns, A.L. !$#journal Biochemistry (1994) 33:6888-6901 !$#title Divergent structure of the human synexin (annexin VII) gene !1and assignment to chromosome 10. !$#cross-references MUID:94264005; PMID:7515686 !$#accession A54467 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-488 ##label SHI REFERENCE A32554 !$#authors Burns, A.L.; Magendzo, K.; Shirvan, A.; Srivastava, M.; !1Rojas, E.; Alijani, M.R.; Pollard, H.B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:3798-3802 !$#title Calcium channel activity of purified human synexin and !1structure of the human synexin gene. !$#cross-references MUID:89264510; PMID:2542947 !$#accession A32554 !'##molecule_type mRNA !'##residues 1-145,168-488 ##label BUR !'##cross-references EMBL:J04543; NID:g338243; PIDN:AAA36616.1; !1PID:g338244 REFERENCE A39513 !$#authors Magendzo, K.; Shirvan, A.; Cultraro, C.; Srivastava, M.; !1Pollard, H.B.; Burns, A.L. !$#journal J. Biol. Chem. (1991) 266:3228-3232 !$#title Alternative splicing of human synexin mRNA in brain, !1cardiac, and skeletal muscle alters the unique N-terminal !1domain. !$#cross-references MUID:91131630; PMID:1825209 !$#accession A39513 !'##molecule_type mRNA !'##residues 137-145,168-176 ##label MAG !'##cross-references EMBL:J05732 !$#accession B39513 !'##molecule_type mRNA !'##residues 137-176 ##label MA2 COMMENT Annexins undergo reversible, calcium-dependent binding to !1membrane phospholipids. Although a number have been !1proposed, the physiological roles of the various annexins !1are not yet fully understood. COMMENT The long form of annexin VII is more prevalent in brain, !1heart, and skeletal muscle. GENETICS !$#gene GDB:ANX7 !'##cross-references GDB:369042; OMIM:186360 !$#map_position 10q21.1-10q21.2 !$#introns 17/3; 87/1; 124/1; 145/3; 167/3; 202/2; 233/3; 271/3; 328/3; !1385/3; 411/1; 448/3 CLASSIFICATION #superfamily annexin VII; annexin repeat homology KEYWORDS alternative splicing; calcium binding; calcium channel; !1duplication; endonexin fold; ion channel; phospholipid !1binding; voltage-gated ion channel FEATURE !$1-488 #product annexin VII, long form #status predicted !8#label MAT\ !$1-145,168-488 #product annexin VII, short form #status predicted !8#label MA3\ !$188-259 #domain annexin repeat homology #label AX1\ !$199-215 #region endonexin fold #status predicted\ !$260-331 #domain annexin repeat homology #label AX2\ !$271-287 #region endonexin fold #status predicted\ !$343-415 #domain annexin repeat homology #label AX3\ !$355-371 #region endonexin fold #status predicted\ !$419-488 #domain annexin repeat homology #label AX4\ !$430-446 #region endonexin fold #status predicted SUMMARY #length 488 #molecular-weight 52739 #checksum 6481 SEQUENCE /// ENTRY LUDO7 #type complete TITLE annexin VII - slime mold (Dictyostelium discoideum) ALTERNATE_NAMES synexin CONTAINS annexin VII, short form ORGANISM #formal_name Dictyostelium discoideum DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 22-Jun-1999 ACCESSIONS S14723; S22756; A40977; A38670 REFERENCE S14723 !$#authors Greenwood, M.; Tsang, A. !$#journal Biochim. Biophys. Acta (1991) 1088:429-432 !$#title Sequence and expression of annexin VII of Dictyostelium !1discoideum. !$#cross-references MUID:91198150; PMID:1826615 !$#accession S14723 !'##molecule_type DNA !'##residues 1-339 ##label GRE1 !'##cross-references EMBL:X60269 !$#accession S22756 !'##molecule_type mRNA !'##residues 17-462 ##label GRE2 !'##cross-references EMBL:X60270; NID:g7209; PIDN:CAA42816.1; !1PID:g671859 REFERENCE A40977 !$#authors Doering, V.; Schleicher, M.; Noegel, A.A. !$#journal J. Biol. Chem. (1991) 266:17509-17515 !$#title Dictyostelium annexin VII (synexin). cDNA sequence and !1isolation of a gene disruption mutant. !$#cross-references MUID:91373375; PMID:1832674 !$#accession A40977 !'##molecule_type mRNA !'##residues 1-8,52-462 ##label DOE !'##cross-references GB:M69022 REFERENCE A38670 !$#authors Gerke, V. !$#journal J. Biol. Chem. (1991) 266:1697-1700 !$#title Identification of a homologue for annexin VII (synexin) in !1Dictyostelium discoideum. !$#cross-references MUID:91107669; PMID:1824843 !$#accession A38670 !'##molecule_type protein !'##residues 143-155;176-185;192,'X',194-197,'X', !1199;217-222;264-272;302-305;347-360;431-437 ##label GER COMMENT Annexins undergo reversible, calcium-dependent binding to !1membrane phospholipids. Although a number have been !1proposed, the physiological roles of the various annexins !1are not yet fully understood. GENETICS !$#gene DdANN7 !$#introns 8/2; 51/2 CLASSIFICATION #superfamily annexin VII; annexin repeat homology KEYWORDS alternative splicing; calcium binding; calcium channel; !1duplication; endonexin fold; ion channel; phospholipid !1binding; tandem repeat; voltage-gated ion channel FEATURE !$1-462 #product annexin VII #status predicted #label MAT1\ !$1-8,52-462 #product annexin VII short splice form #status !8predicted #label MAT2\ !$25-131 #region 6-residue repeats (Q-Q-G-Y-P-P)\ !$164-235 #domain annexin repeat homology #label AX1\ !$175-191 #region endonexin fold\ !$236-307 #domain annexin repeat homology #label AX2\ !$247-263 #region endonexin fold\ !$318-391 #domain annexin repeat homology #label AX3\ !$330-346 #region endonexin fold\ !$395-462 #domain annexin repeat homology #label AX4\ !$406-422 #region endonexin fold SUMMARY #length 462 #molecular-weight 51172 #checksum 5459 SEQUENCE /// ENTRY LUBO11 #type complete TITLE annexin XI form A - bovine ALTERNATE_NAMES calcyclin-associated protein peptide, CAP-50 ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 22-Jun-1999 ACCESSIONS A42113; A42909; B42909; C42909; D42909 REFERENCE A42113 !$#authors Towle, C.A.; Treadwell, B.V. !$#journal J. Biol. Chem. (1992) 267:5416-5423 !$#title Identification of a novel mammalian annexin. cDNA cloning, !1sequence analysis, and ubiquitous expression of the annexin !1XI gene. !$#cross-references MUID:92184796; PMID:1372001 !$#accession A42113 !'##molecule_type mRNA !'##residues 1-503 ##label TOW !'##cross-references GB:M82802; NID:g162673; PIDN:AAA30379.1; !1PID:g162674 !'##note the authors did not translate the codon GAC for residue 503 REFERENCE A42909 !$#authors Mizutani, A.; Usuda, N.; Tokumitsu, H.; Minami, H.; Yasui, !1K.; Kobayashi, R.; Hidaka, H. !$#journal J. Biol. Chem. (1992) 267:13498-13504 !$#title CAP-50, a newly identified annexin, localizes in nuclei of !1cultured fibroblast 3Y1 cells. !$#cross-references MUID:92317074; PMID:1618851 !$#accession A42909 !'##molecule_type protein !'##residues 213-223,'X',225-226;319-325,'G',327-328,'X',330-333,'Q', !1335-339;441-450,'X',452-454,'D',456-460;479-497 ##label MIZ !'##experimental_source lung !'##note sequence modified after extraction from NCBI backbone COMMENT Annexins undergo reversible, calcium-dependent binding to !1membrane phospholipids. Although a number have been !1proposed, the physiological roles of the various annexins !1are not yet fully understood. GENETICS !$#introns 19/1; 56/2 !$#note the list of introns is incomplete CLASSIFICATION #superfamily annexin VII; annexin repeat homology KEYWORDS calcium binding; duplication; endonexin fold; glycoprotein; !1phospholipid binding FEATURE !$201-272 #domain annexin repeat homology #label AX1\ !$212-228 #region endonexin fold #status predicted\ !$273-344 #domain annexin repeat homology #label AX2\ !$284-300 #region endonexin fold #status predicted\ !$356-428 #domain annexin repeat homology #label AX3\ !$368-384 #region endonexin fold #status predicted\ !$432-503 #domain annexin repeat homology #label AX4\ !$443-459 #region endonexin fold #status predicted\ !$59,111 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 503 #molecular-weight 54018 #checksum 5855 SEQUENCE /// ENTRY S23447 #type complete TITLE annexin XI form B - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 22-Nov-1993 #sequence_revision 10-Feb-1995 #text_change 22-Jun-1999 ACCESSIONS S23447; S36136 REFERENCE S23447 !$#authors Towle, C. !$#submission submitted to the EMBL Data Library, February 1992 !$#accession S23447 !'##molecule_type mRNA !'##residues 1-505 ##label TOW !'##cross-references EMBL:Z11742; NID:g77; PIDN:CAA77801.1; PID:g78 REFERENCE S36136 !$#authors Towle, C.A.; Weissbach, L.; Treadwell, B.V. !$#journal Biochim. Biophys. Acta (1992) 1131:223-226 !$#title Alternatively spliced annexin XI transcripts encode proteins !1that differ near the amino-terminus. !$#cross-references MUID:92305067; PMID:1535225 !$#accession S36136 !'##molecule_type mRNA !'##residues 1-77 ##label TO2 !'##cross-references EMBL:Z11742 COMMENT Annexins undergo reversible, calcium-dependent binding to !1membrane phospholipids. Although a number have been !1proposed, the physiological roles of the various annexins !1are not yet fully understood. GENETICS !$#introns 19/1; 58/2 !$#note the list of introns is incomplete CLASSIFICATION #superfamily annexin VII; annexin repeat homology KEYWORDS alternative splicing; calcium binding; duplication; !1endonexin fold; glycoprotein; phospholipid binding FEATURE !$203-274 #domain annexin repeat homology #label AX1\ !$214-230 #region endonexin fold #status predicted\ !$275-346 #domain annexin repeat homology #label AX2\ !$286-302 #region endonexin fold #status predicted\ !$358-430 #domain annexin repeat homology #label AX3\ !$370-386 #region endonexin fold #status predicted\ !$434-505 #domain annexin repeat homology #label AX4\ !$445-461 #region endonexin fold #status predicted\ !$61,113 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 505 #molecular-weight 54215 #checksum 8853 SEQUENCE /// ENTRY LURB11 #type complete TITLE annexin XI - rabbit ALTERNATE_NAMES calcyclin-associated annexin protein CAP-50 ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jun-2000 ACCESSIONS JH0694; PH0950; A38250; PS0263 REFERENCE JH0694 !$#authors Tokumitsu, H.; Mizutani, A.; Muramatsu, M.; Yokota, T.; !1Arai, K.; Hidaka, H. !$#journal Biochem. Biophys. Res. Commun. (1992) 186:1227-1235 !$#title Molecular cloning of rabbit CAP-50, a calcyclin-associated !1annexin protein. !$#cross-references MUID:92378579; PMID:1380798 !$#accession JH0694 !'##molecule_type mRNA !'##residues 1-503 ##label TOK !'##cross-references DDBJ:D10883; NID:g471147; PIDN:BAA01705.1; !1PID:g471148 !'##experimental_source lung !$#accession PH0950 !'##molecule_type protein !'##residues !1104-141;213-231;254-262;270-280;285-309;319-337;429-448; !1478-492 ##label TK2 REFERENCE A38250 !$#authors Tokumitsu, H.; Mizutani, A.; Minami, H.; Kobayashi, R.; !1Hidaka, H. !$#journal J. Biol. Chem. (1992) 267:8919-8924 !$#title A calcyclin-associated protein is a newly identified member !1of the Ca(2+)/phospholipid-binding proteins, annexin family. !$#cross-references MUID:92250478; PMID:1533622 !$#accession A38250 !'##molecule_type protein !'##residues 104-141;213-223,'X',225-231;254-263;271-280;285-291,'X', !1293-300,'X',302-309;319-337;429-448;478-492 ##label TO3 COMMENT This protein binds specifically to calcyclin in a Ca2+ !1dependent manner. CLASSIFICATION #superfamily annexin VII; annexin repeat homology KEYWORDS calcium binding; duplication; endonexin fold; glycoprotein; !1phospholipid binding FEATURE !$201-272 #domain annexin repeat homology #label AX1\ !$212-228 #region endonexin fold #status predicted\ !$273-344 #domain annexin repeat homology #label AX2\ !$284-300 #region endonexin fold #status predicted\ !$356-428 #domain annexin repeat homology #label AX3\ !$368-384 #region endonexin fold #status predicted\ !$432-503 #domain annexin repeat homology #label AX4\ !$443-459 #region endonexin fold #status predicted\ !$58 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 503 #molecular-weight 54034 #checksum 4870 SEQUENCE /// ENTRY AQHU68 #type complete TITLE annexin VI [validated] - human ALTERNATE_NAMES calcium-binding protein, 68K; calelectrin; calphobindin II ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1992 #sequence_revision 30-Sep-1992 #text_change 08-Dec-2000 ACCESSIONS JU0032; S00263; S18519; A31079; JX0091; B34459; B31953; !1A53507 REFERENCE JU0032 !$#authors Iwasaki, A.; Suda, M.; Watanabe, M.; Nakao, H.; Hattori, Y.; !1Nagoya, T.; Saino, Y.; Shidara, Y.; Maki, M. !$#journal J. Biochem. (1989) 106:43-49 !$#title Structure and expression of cDNA for calphobindin II, a !1human placental coagulation inhibitor. !$#cross-references MUID:89380132; PMID:2528541 !$#accession JU0032 !'##molecule_type mRNA !'##residues 1-673 ##label IWA !'##cross-references EMBL:D00510; NID:g219550; PIDN:BAA00400.1; !1PID:g219551 REFERENCE S00263 !$#authors Crompton, M.R.; Owens, R.J.; Totty, N.F.; Moss, S.E.; !1Waterfield, M.D.; Crumpton, M.J. !$#journal EMBO J. (1988) 7:21-27 !$#title Primary structure of the human, membrane-associated Ca !1(2+)-binding protein p68: a novel member of a protein !1family. !$#cross-references MUID:88196081; PMID:3258820 !$#accession S00263 !'##molecule_type mRNA !'##residues 1-618,'D',620-673 ##label CR1 !'##cross-references EMBL:Y00097; NID:g35217; PIDN:CAA68286.1; !1PID:g35218 !$#accession S18519 !'##molecule_type protein !'##residues 103-113;167-172,'X',174-177;232-235,'F', !1237-240;251-258;277-281;359-362,'G',364-370 ##label CRO !'##note the sequence from Fig. 6 is inconsistent with that from Fig. 4 !1in having 619-Glu !'##note eight calcium ions are bound in the presence of phospholipid REFERENCE A31079 !$#authors Suedhof, T.C.; Slaughter, C.A.; Leznicki, I.; Barjon, P.; !1Reynolds, G.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:664-668 !$#title Human 67-kDa calelectrin contains a duplication of four !1repeats found in 35-kDa lipocortins. !$#cross-references MUID:88124902; PMID:2963335 !$#accession A31079 !'##molecule_type mRNA !'##residues 1-225,'MK',228-554,'T',556-673 ##label SUE !'##cross-references GB:J03578; NID:g179975; PIDN:AAA35656.1; !1PID:g179976 REFERENCE JX0091 !$#authors Yoshizaki, H.; Mizoguchi, T.; Arai, K.; Shiratsuchi, M.; !1Shidara, Y.; Maki, M. !$#journal J. Biochem. (1990) 107:43-50 !$#title Structure and properties of calphobindin II, an !1anticoagulant protein from human placenta. !$#cross-references MUID:90236978; PMID:2139657 !$#accession JX0091 !'##molecule_type protein !'##residues 2-299;307-314;320-445;447-549;581-673 ##label YOS REFERENCE A34459 !$#authors Hayashi, H.; Owada, M.K.; Sonobe, S.; Kakunaga, T. !$#journal J. Biol. Chem. (1989) 264:17222-17230 !$#title Characterizations of two distinct Ca(2+)-dependent !1phospholipid-binding proteins of 68-kDa isolated from human !1placenta. !$#cross-references MUID:90008880; PMID:2529258 !$#accession B34459 !'##molecule_type protein !'##residues 10-25;69-75;136-151;192-207;209-220;300-306 ##label HAY !'##experimental_source placenta REFERENCE A92696 !$#authors Ahn, N.G.; Teller, D.C.; Bienkowski, M.J.; McMullen, B.A.; !1Lipkin, E.W.; de Haen, C. !$#journal J. Biol. Chem. (1988) 263:18657-18663 !$#title Sedimentation equilibrium analysis of five !1lipocortin-related phospholipase A-2 inhibitors from human !1placenta. Evidence against a mechanistically relevant !1association between enzyme and inhibitor. !$#cross-references MUID:89066652; PMID:2974032 !$#accession B31953 !'##molecule_type protein !'##residues 90-108,'L',110-126;127,265-276;286-302;626-654 ##label AHN REFERENCE A53507 !$#authors Hyatt, S.L.; Liao, L.; Chapline, C.; Jaken, S. !$#journal Biochemistry (1994) 33:1223-1228 !$#title Identification and characterization of alpha-protein kinase !1C binding proteins in normal and transformed REF52 cells. !$#cross-references MUID:94153907; PMID:8110754 !$#accession A53507 !'##molecule_type protein !'##residues 'X',473-480,'DY' ##label HYA COMMENT This abundant cytosolic protein binds to the inner surface !1of the cell membrane; in the sarcoplasmic reticulum it can !1regulate the calcium-release channel. GENETICS !$#gene GDB:ANX6 !'##cross-references GDB:119681; OMIM:114070 !$#map_position 5q32-5q34 CLASSIFICATION #superfamily annexin VI; annexin repeat homology KEYWORDS acetylated amino end; calcium binding; duplication; !1endonexin fold; phospholipid binding FEATURE !$2-673 #product annexin VI #status experimental #label MAT\ !$23-94 #domain annexin repeat homology #label AX1\ !$34-50 #region endonexin fold #status predicted\ !$95-166 #domain annexin repeat homology #label AX2\ !$106-122 #region endonexin fold #status predicted\ !$178-250 #domain annexin repeat homology #label AX3\ !$190-206 #region endonexin fold #status predicted\ !$254-325 #domain annexin repeat homology #label AX4\ !$265-281 #region endonexin fold #status predicted\ !$366-437 #domain annexin repeat homology #label AX5\ !$377-393 #region endonexin fold #status predicted\ !$438-509 #domain annexin repeat homology #label AX6\ !$449-465 #region endonexin fold #status predicted\ !$527-598 #domain annexin repeat homology #label AX7\ !$538-554 #region endonexin fold #status predicted\ !$602-673 #domain annexin repeat homology #label AX8\ !$613-629 #region endonexin fold #status predicted\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental SUMMARY #length 673 #molecular-weight 75872 #checksum 9084 SEQUENCE /// ENTRY S01786 #type complete TITLE annexin VI - mouse ALTERNATE_NAMES calcium-binding protein p68; calelectrin; calphobindin II ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Sep-1989 #sequence_revision 26-May-1994 #text_change 22-Jun-1999 ACCESSIONS S01786 REFERENCE S01786 !$#authors Moss, S.E.; Crompton, M.R.; Crumpton, M.J. !$#journal Eur. J. Biochem. (1988) 177:21-27 !$#title Molecular cloning of murine p68, a Ca-binding protein of the !1lipocortin family. !$#cross-references MUID:89030687; PMID:2972541 !$#accession S01786 !'##molecule_type mRNA !'##residues 1-673 ##label MOS !'##cross-references EMBL:X13460; NID:g53580; PIDN:CAA31808.1; !1PID:g53581 !'##note the authors translated the codon GCC for residue 329 as Gly COMMENT This abundant cytosolic protein binds to the inner surface !1of the cell membrane; in the sarcoplasmic reticulum it can !1regulate the calcium-release channel. CLASSIFICATION #superfamily annexin VI; annexin repeat homology KEYWORDS acetylated amino end; calcium binding; duplication; !1endonexin fold; phospholipid binding FEATURE !$2-673 #product annexin VI #status predicted #label MAT\ !$23-94 #domain annexin repeat homology #label AX1\ !$34-50 #region endonexin fold #status predicted\ !$95-166 #domain annexin repeat homology #label AX2\ !$106-122 #region endonexin fold #status predicted\ !$178-250 #domain annexin repeat homology #label AX3\ !$190-206 #region endonexin fold #status predicted\ !$254-325 #domain annexin repeat homology #label AX4\ !$265-281 #region endonexin fold #status predicted\ !$366-437 #domain annexin repeat homology #label AX5\ !$377-393 #region endonexin fold #status predicted\ !$438-509 #domain annexin repeat homology #label AX6\ !$449-465 #region endonexin fold #status predicted\ !$527-598 #domain annexin repeat homology #label AX7\ !$538-554 #region endonexin fold #status predicted\ !$602-673 #domain annexin repeat homology #label AX8\ !$613-629 #region endonexin fold #status predicted\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status predicted SUMMARY #length 673 #molecular-weight 75886 #checksum 9057 SEQUENCE /// ENTRY S52844 #type complete TITLE annexin VI - rat ALTERNATE_NAMES calcium-binding protein 65/67 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S65683; S52844 REFERENCE S65683 !$#authors Fan, H.; Josic, D.; Lim, Y.P.; Reutter, W. !$#journal Eur. J. Biochem. (1995) 230:741-751 !$#title cDNA cloning and tissue-specific regulation of expression of !1rat calcium-binding protein 65/67. Identification as a !1homologue of annexin VI. !$#cross-references MUID:95331313; PMID:7607247 !$#accession S65683 !'##molecule_type mRNA !'##residues 1-673 ##label FAN !'##cross-references EMBL:X86086; NID:g763180; PIDN:CAA60040.1; !1PID:g763181 !'##experimental_source liver CLASSIFICATION #superfamily annexin VI; annexin repeat homology KEYWORDS acetylated amino end; calcium binding; endonexin fold; !1membrane-associated protein; phospholipid binding FEATURE !$2-673 #product annexin VI #status predicted #label MAT\ !$23-94 #domain annexin repeat homology #label AX1\ !$34-50 #region endonexin fold #status predicted\ !$95-166 #domain annexin repeat homology #label AX2\ !$106-122 #region endonexin fold #status predicted\ !$178-250 #domain annexin repeat homology #label AX3\ !$190-206 #region endonexin fold #status predicted\ !$254-325 #domain annexin repeat homology #label AX4\ !$265-281 #region endonexin fold #status predicted\ !$366-437 #domain annexin repeat homology #label AX5\ !$377-393 #region endonexin fold #status predicted\ !$438-509 #domain annexin repeat homology #label AX6\ !$449-465 #region endonexin fold #status predicted\ !$527-598 #domain annexin repeat homology #label AX7\ !$538-554 #region endonexin fold #status predicted\ !$602-673 #domain annexin repeat homology #label AX8\ !$613-629 #region endonexin fold #status predicted\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status predicted SUMMARY #length 673 #molecular-weight 75753 #checksum 69 SEQUENCE /// ENTRY LLBY #type complete TITLE actin-binding protein ABP1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YCR088w ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1991 #sequence_revision 31-Dec-1993 #text_change 05-Nov-1999 ACCESSIONS S19503; S19767; S07608 REFERENCE S19351 !$#authors Dusterhoft, A.; Erdmann, D.; Hegemann, J.; Philippsen, P.; !1Schweitzer, B.; Spiegelberg, R.; Steiner, S. !$#submission submitted to the Protein Sequence Database, March 1992 !$#accession S19503 !'##molecule_type DNA !'##residues 1-476 ##label DUS !'##cross-references EMBL:X59720; GSPDB:GN00003; MIPS:YCR088w REFERENCE S19504 !$#authors Frontali, L.; Grisanti, P. !$#submission submitted to the Protein Sequence Database, March 1992 !$#accession S19767 !'##molecule_type DNA !'##residues 14-592 ##label FRO !'##cross-references EMBL:X59720; GSPDB:GN00003; MIPS:YCR088w REFERENCE S07608 !$#authors Drubin, D.G.; Mulholland, J.; Zhu, Z.; Botstein, D. !$#journal Nature (1990) 343:288-290 !$#title Homology of a yeast actin-binding protein to signal !1transduction proteins and myosin-I. !$#cross-references MUID:90136906; PMID:2405279 !$#accession S07608 !'##molecule_type DNA !'##residues 1-57,'S',59-311,'I',313-592 ##label DRU !'##cross-references EMBL:X51780; NID:g3321; PIDN:CAA36075.1; PID:g3322 GENETICS !$#gene SGD:ABP1; MIPS:YCR088w !'##cross-references SGD:S0000684; MIPS:YCR088w !$#map_position 3R CLASSIFICATION #superfamily actin-binding protein ABP1; SH3 homology KEYWORDS actin binding; duplication FEATURE !$158-180,378-401 #region duplication\ !$539-588 #domain SH3 homology #label SH3 SUMMARY #length 592 #molecular-weight 65576 #checksum 4775 SEQUENCE /// ENTRY TPRBTS #type complete TITLE troponin T, fast skeletal muscle - rabbit CONTAINS troponin T, fast skeletal muscle splice form 1; troponin T, fast skeletal muscle splice form 2; troponin T, fast skeletal muscle splice form 3 ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 24-Apr-1984 #sequence_revision 17-May-1996 #text_change 22-Jun-1999 ACCESSIONS A03083; S03590; S03591; S03592; I46515; I46516 REFERENCE A92220 !$#authors Pearlstone, J.R.; Johnson, P.; Carpenter, M.R.; Smillie, !1L.B. !$#journal J. Biol. Chem. (1977) 252:983-989 !$#title Primary structure of rabbit skeletal muscle troponin-T. !1Sequence determination of the NH-2-terminal fragment CB3 and !1the complete sequence of troponin-T. !$#cross-references MUID:77118575; PMID:320204 !$#accession A03083 !'##molecule_type protein !'##residues 1-10,17-18,'E',20-48,50-266 ##label PE2 !'##note this is the final paper in a series REFERENCE S03590 !$#authors Briggs, M.M.; Schachat, F. !$#journal J. Mol. Biol. (1989) 206:245-249 !$#title N-terminal amino acid sequences of three functionally !1different troponin T isoforms from rabbit fast skeletal !1muscle. !$#cross-references MUID:89199646; PMID:2704041 !$#accession S03590 !'##molecule_type protein !'##residues 1-10,17-53 ##label BRI !'##note splice form 2 !$#accession S03591 !'##molecule_type protein !'##residues 1-53 ##label BR2 !'##note splice form 1 !$#accession S03592 !'##molecule_type protein !'##residues 1-21,39-53 ##label BR3 REFERENCE A90295 !$#authors Moir, A.J.G.; Cole, H.A.; Perry, S.V. !$#journal Biochem. J. (1977) 161:371-382 !$#title The phosphorylation sites of troponin T from white skeletal !1muscle and the effects of interaction with troponin C on !1their phosphorylation by phosphorylase kinase. !$#cross-references MUID:77157104; PMID:849266 !$#contents annotation; phosphorylation sites !$#note phosphorylation under in vivo conditions occurred at !1positions that may not be accessible in troponin complex REFERENCE I46471 !$#authors Putney, S.D.; Herlihy, W.C.; Schimmel, P. !$#journal Nature (1983) 302:718-721 !$#title A new troponin T and cDNA clones for 13 different muscle !1proteins, found by shotgun sequencing. !$#cross-references MUID:83167564; PMID:6687628 !$#accession I46515 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 56-136 ##label PUT !'##cross-references EMBL:V00899; NID:g1740; PIDN:CAA24264.1; !1PID:g929768 !$#accession I46516 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 240-266 ##label PU2 !'##cross-references EMBL:V00900; NID:g1742; PIDN:CAA24265.1; !1PID:g833794 COMPLEX troponin is a heterotrimer with one molecule each of !1troponin C (calcium binding component), troponin I !1(inhibitory component), and troponin T (tropomyosin-binding !1component) FUNCTION !$#description binds the troponin complex to tropomyosin; with tropomyosin !1mediates contraction of vertebrate striated muscle in !1response to calcium !$#pathway muscle contraction CLASSIFICATION #superfamily troponin T KEYWORDS acetylated amino end; alternative splicing; differentiation; !1muscle contraction; phosphoprotein; skeletal muscle FEATURE !$1-266 #product troponin T, fast skeletal muscle splice form !81 #status experimental #label MAT1\ !$1-21,39-266 #product troponin T, fast skeletal muscle splice form !83 #status experimental #label MAT3\ !$1-10,17-266 #product troponin T, fast skeletal muscle splice form !82 #status experimental #label MAT2\ !$1 #modified_site acetylated amino end (Ser) #status !8experimental\ !$1 #binding_site phosphate (Ser) (covalent) (by troponin !8T kinase) #status experimental SUMMARY #length 266 #molecular-weight 31426 #checksum 9215 SEQUENCE /// ENTRY TPQJT1 #type fragment TITLE troponin T, embryonic skeletal muscle (clone cC113) - Japanese quail (fragment) ORGANISM #formal_name Coturnix coturnix japonica #common_name Japanese quail DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 23-Feb-1997 ACCESSIONS A03084 REFERENCE A92502 !$#authors Hastings, K.E.M.; Bucher, E.A.; Emerson Jr., C.P. !$#journal J. Biol. Chem. (1985) 260:13699-13703 !$#title Generation of troponin T isoforms by alternative RNA !1splicing in avian skeletal muscle. Conserved and divergent !1features in birds and mammals. !$#cross-references MUID:86033836; PMID:3840482 !$#accession A03084 !'##molecule_type mRNA !'##residues 1-145 ##label HAS !'##experimental_source embryonic skeletal muscle myoblasts COMMENT This isoform is generated by a differential mRNA splicing !1mechanism that discriminates between two alternative exons !1in a single gene. CLASSIFICATION #superfamily troponin T KEYWORDS alternative splicing; differentiation; muscle; !1phosphoprotein SUMMARY #length 145 #checksum 319 SEQUENCE /// ENTRY TPQJT2 #type fragment TITLE troponin T, embryonic skeletal muscle (clone cC119) - Japanese quail (fragment) ORGANISM #formal_name Coturnix coturnix japonica #common_name Japanese quail DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 23-Feb-1997 ACCESSIONS A03085 REFERENCE A92502 !$#authors Hastings, K.E.M.; Bucher, E.A.; Emerson Jr., C.P. !$#journal J. Biol. Chem. (1985) 260:13699-13703 !$#title Generation of troponin T isoforms by alternative RNA !1splicing in avian skeletal muscle. Conserved and divergent !1features in birds and mammals. !$#cross-references MUID:86033836; PMID:3840482 !$#accession A03085 !'##molecule_type mRNA !'##residues 1-145 ##label HAS !'##experimental_source embryonic skeletal muscle myoblasts COMMENT This isoform is generated by a differential mRNA splicing !1mechanism that discriminates between two alternative exons !1in a single gene. CLASSIFICATION #superfamily troponin T KEYWORDS alternative splicing; differentiation; muscle; !1phosphoprotein SUMMARY #length 145 #checksum 359 SEQUENCE /// ENTRY TPHUTW #type complete TITLE troponin T, slow skeletal muscle - human ALTERNATE_NAMES troponin T1 ORGANISM #formal_name Homo sapiens #common_name man DATE 20-Jun-1989 #sequence_revision 17-May-1996 #text_change 22-Jun-1999 ACCESSIONS A29783; B29783; JC2126; A57979 REFERENCE A29783 !$#authors Gahlmann, R.; Troutt, A.B.; Wade, R.P.; Gunning, P.; Kedes, !1L. !$#journal J. Biol. Chem. (1987) 262:16122-16126 !$#title Alternative splicing generates variants in important !1functional domains of human slow skeletal troponin T. !$#cross-references MUID:88058976; PMID:2824479 !$#accession A29783 !'##molecule_type mRNA !'##residues 1-19,'D',21-278 ##label GAH !'##cross-references GB:M19309; NID:g339780; PIDN:AAA61204.1; !1PID:g339781; GB:J03476 !'##experimental_source clone H22h !$#accession B29783 !'##molecule_type mRNA !'##residues 1-24,36-204,221-278 ##label GA2 !'##cross-references GB:M19308; NID:g339782; PIDN:AAA61205.1; !1PID:g339783; GB:J03476 !'##experimental_source clone M1 REFERENCE JC2126 !$#authors Samson, F.; Mesnard, L.; Mihovilovic, M.; Potter, T.G.; !1Mercadier, J.J.; Roses, A.D.; Gilbert, J.R. !$#journal Biochem. Biophys. Res. Commun. (1994) 199:841-847 !$#title A new human slow skeletal troponin T (TnTs) mRNA isoform !1derived from alternative splicing of a single gene. !$#cross-references MUID:94183266; PMID:8135831 !$#accession JC2126 !'##molecule_type mRNA !'##residues 1-204,221-278 ##label SAM !'##cross-references GB:S69208; NID:g546020; PIDN:AAB30272.1; !1PID:g546021 !$#accession A57979 !'##molecule_type mRNA !'##residues 1-24,36-204,221-278 ##label SA2 !'##cross-references GB:S69209; NID:g546022; PIDN:AAB30273.1; !1PID:g546023 GENETICS !$#gene GDB:TNNT1 !'##cross-references GDB:125310; OMIM:191041 !$#map_position 19q13.4-19q13.4 COMPLEX troponin is a heterotrimer with one molecule each of !1troponin C (calcium binding component), troponin I !1(inhibitory component), and troponin T (tropomyosin-binding !1component) FUNCTION !$#description binds the troponin complex to tropomyosin; with tropomyosin !1mediates contraction of vertebrate striated muscle in !1response to calcium !$#pathway muscle contraction CLASSIFICATION #superfamily troponin T KEYWORDS acetylated amino end; actin binding; alternative splicing; !1muscle contraction; phosphoprotein; skeletal muscle; thin !1filaments FEATURE !$2-278 #product troponin T, slow skeletal muscle splice form !81 #status predicted #label MAT1\ !$2-204,221-278 #product troponin T, slow skeletal muscle splice form !82 #status predicted #label MAT2\ !$2-24,36-204,221-278 #product troponin T, slow skeletal muscle splice form !83 #status predicted #label MAT3\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status predicted\ !$2 #binding_site phosphate (Ser) (covalent) (by troponin !8T kinase) #status predicted\ !$177 #binding_site phosphate (Thr) (covalent) (by !8calmodulin-dependent kinase II) #status predicted SUMMARY #length 278 #molecular-weight 32948 #checksum 4551 SEQUENCE /// ENTRY TPHUTC #type complete TITLE troponin T, cardiac muscle - human ALTERNATE_NAMES troponin T2 ORGANISM #formal_name Homo sapiens #common_name man DATE 18-Aug-1995 #sequence_revision 12-Jul-1996 #text_change 16-Jul-1999 ACCESSIONS A54671; S35684; I52865; S48792; S48791; S48794 REFERENCE A54671 !$#authors Townsend, P.J.; Farza, H.; MacGeoch, C.; Spurr, N.K.; Wade, !1R.; Gahlmann, R.; Yacoub, M.H.; Barton, P.J.R. !$#journal Genomics (1994) 21:311-316 !$#title Human cardiac troponin T: identification of fetal isoforms !1and assignment of the TNNT2 locus to chromosome 1q. !$#cross-references MUID:94375053; PMID:8088824 !$#accession A54671 !'##molecule_type mRNA !'##residues 1-23,34-298 ##label TOW !'##cross-references GB:X74819; NID:g510601; PIDN:CAA52818.1; !1PID:g510602 !'##experimental_source heart REFERENCE S35684 !$#authors Mesnard, L.; Samson, F.; Espinasse, I.; Durand, J.; Neveux, !1J.Y.; Mercadier, J.J. !$#journal FEBS Lett. (1993) 328:139-144 !$#title Molecular cloning and developmental expression of human !1cardiac troponin T. !$#cross-references MUID:93345675; PMID:8344420 !$#accession S35684 !'##molecule_type mRNA !'##residues 1-23,34-138,'K',140-248,'T',250-298 ##label MES !'##cross-references GB:S64668; NID:g408216; PIDN:AAB27731.1; !1PID:g408217 !'##experimental_source heart REFERENCE I52865 !$#authors Anderson, P.A.; Greig, A.; Mark, T.M.; Malouf, N.N.; !1Oakeley, A.E.; Ungerleider, R.M.; Allen, P.D.; Kay, B.K. !$#journal Circ. Res. (1995) 76:681-686 !$#title Molecular basis of human cardiac troponin T isoforms !1expressed in the developing, adult, and failing heart. !$#cross-references MUID:95202803; PMID:7534662 !$#accession I52865 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-23,34-298 ##label AND !'##cross-references GB:L40162; NID:g685177; PIDN:AAA67422.1; !1PID:g685178 !'##note cardiac muscle isoform TnT3 REFERENCE S48790 !$#authors Farza, H. !$#submission submitted to the EMBL Data Library, June 1994 !$#accession S48792 !'##molecule_type mRNA !'##residues 1-163 ##label FAR !'##cross-references EMBL:X79856; NID:g587437; PIDN:CAA56236.1; !1PID:g587438 !'##experimental_source clone TNT5-11/HTNT5b !$#accession S48791 !'##molecule_type mRNA !'##residues 1-108 ##label FA2 !'##cross-references EMBL:X79855; NID:g587435; PIDN:CAA56235.1; !1PID:g587436 !'##experimental_source clone TNT5-11/HTNT5a !$#accession S48794 !'##molecule_type mRNA !'##residues 1-54,56-98,138-200,204-298 ##label FA3 !'##cross-references EMBL:X79857; NID:g587431; PIDN:CAA56237.1; !1PID:g587432 !'##experimental_source clone TNT5-1/HTNT4 GENETICS !$#gene GDB:TNNT2 !'##cross-references GDB:221879; OMIM:191045 !$#map_position 1q32-1q32 COMPLEX troponin is a heterotrimer with one molecule each of !1troponin C (calcium binding component), troponin I !1(inhibitory component), and troponin T (tropomyosin-binding !1component) FUNCTION !$#description binds the troponin complex to tropomyosin; with tropomyosin !1mediates contraction of vertebrate striated muscle in !1response to calcium !$#pathway muscle contraction CLASSIFICATION #superfamily troponin T KEYWORDS acetylated amino end; actin binding; alternative splicing; !1cardiac muscle; heart; muscle contraction; phosphoprotein; !1thin filaments FEATURE !$2-298 #product troponin T, cardiac muscle isoform TnT1 !8#status predicted #label MAT1\ !$2-23,34-298 #product troponin T, cardiac muscle isoform TnT3 !8#status predicted #label MAT3\ !$2-18,24-298 #product troponin T, cardiac muscle isoform TnT2 !8#status predicted #label MAT2\ !$2-18,34-298 #product troponin T, cardiac muscle isoform TnT4 !8#status predicted #label MAT4\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status predicted\ !$2 #binding_site phosphate (Ser) (covalent) (by troponin !8T kinase) #status predicted\ !$204,213,294 #binding_site phosphate (Thr) (covalent) (by !8calmodulin-dependent kinase II) #status predicted SUMMARY #length 298 #molecular-weight 35923 #checksum 4495 SEQUENCE /// ENTRY TPCHTC #type complete TITLE troponin T, cardiac muscle, embryonic splice form - chicken CONTAINS cardiac muscle troponin T, adult splice form ORGANISM #formal_name Gallus gallus #common_name chicken DATE 28-Aug-1985 #sequence_revision 12-Apr-1996 #text_change 16-Jul-1999 ACCESSIONS A25373; A03086 REFERENCE A25373 !$#authors Cooper, T.A.; Ordahl, C.P. !$#journal J. Biol. Chem. (1985) 260:11140-11148 !$#title A single cardiac troponin T gene generates embryonic and !1adult isoforms via developmentally regulated alternate !1splicing. !$#cross-references MUID:85289327; PMID:2993302 !$#accession A25373 !'##molecule_type mRNA !'##residues 1-302 ##label COO !'##cross-references GB:M10013; NID:g212783; PIDN:AAA49099.1; !1PID:g212784 REFERENCE A03086 !$#authors Cooper, T.A.; Ordahl, C.P. !$#journal Science (1984) 226:979-982 !$#title A single troponin T gene regulated by different programs in !1cardiac and skeletal muscle development. !$#cross-references MUID:85065747; PMID:6095446 !$#accession A03086 !'##molecule_type mRNA !'##residues 68-302 ##label CO2 !'##cross-references GB:K02263; NID:g212781; PIDN:AAA49098.1; !1PID:g212782 COMMENT This protein, found in adult cardiac muscle and transiently !1in embryonic skeletal muscle, is encoded by one gene whose !1expression is regulated by different developmental programs !1in heart and skeletal muscle. Down-regulation of the protein !1in the late stages of skeletal muscle differentiation has !1been shown, in vitro, to be under neurogenic control. CLASSIFICATION #superfamily troponin T KEYWORDS alternative splicing; cardiac muscle; differentiation; !1heart; muscle; phosphoprotein FEATURE !$1-302 #product troponin T, cardiac muscle, embryonic splice !8form #status predicted #label MATE\ !$1-22,33-302 #product troponin T, cardiac muscle, adult splice !8form #status predicted #label MATA SUMMARY #length 302 #molecular-weight 35986 #checksum 1173 SEQUENCE /// ENTRY TPHUIS #type complete TITLE troponin I, fast skeletal muscle - human ORGANISM #formal_name Homo sapiens #common_name man DATE 13-Jan-1995 #sequence_revision 03-May-1996 #text_change 22-Jun-1999 ACCESSIONS S43508 REFERENCE S43508 !$#authors Zhu, L.; Perez-Alvarado, G.; Wade, R. !$#journal Biochim. Biophys. Acta (1994) 1217:338-340 !$#title Sequencing of a cDNA encoding the human fast-twitch skeletal !1muscle isoform of troponin I. !$#cross-references MUID:94198300; PMID:8148383 !$#accession S43508 !'##molecule_type mRNA !'##residues 1-182 ##label ZHU !'##cross-references GB:L21715; NID:g452077; PIDN:AAA19813.1; !1PID:g452078 GENETICS !$#gene GDB:TNNI2 !'##cross-references GDB:125308; OMIM:191043 !$#map_position 1q32-1q32 COMPLEX troponin is a heterotrimer with one molecule each of !1troponin C (calcium binding component), troponin I !1(inhibitory component), and troponin T (tropomyosin-binding !1component) FUNCTION !$#description binds actin and inhibits myosin ATPase activity; with !1tropomyosin mediates contraction of vertebrate striated !1muscle in response to calcium !$#pathway muscle contraction CLASSIFICATION #superfamily troponin I KEYWORDS acetylated amino end; actin binding; muscle contraction; !1skeletal muscle FEATURE !$2 #modified_site acetylated amino end (Gly) (in mature !8form) #status predicted SUMMARY #length 182 #molecular-weight 21338 #checksum 9151 SEQUENCE /// ENTRY TPRBIS #type complete TITLE troponin I, fast skeletal muscle - rabbit ALTERNATE_NAMES TnI ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 24-Apr-1984 #sequence_revision 03-May-1996 #text_change 22-Jun-1999 ACCESSIONS A45060; A93193; A90286; I46514; A03087 REFERENCE A45060 !$#authors Sheng, Z.; Pan, B.S.; Miller, T.E.; Potter, J.D. !$#journal J. Biol. Chem. (1992) 267:25407-25413 !$#title Isolation, expression, and mutation of a rabbit skeletal !1muscle cDNA clone for troponin I. The role of the NH2 !1terminus of fast skeletal muscle troponin I in its !1biological activity. !$#cross-references MUID:93094259; PMID:1339446 !$#accession A45060 !'##molecule_type mRNA !'##residues 1-46,'DS',49-182 ##label SHE !'##cross-references GB:L04347 !'##experimental_source skeletal muscle !'##note sequence extracted from NCBI backbone (NCBIP:120236) and !1corrected to correspond with the published sequence !'##note the authors translated the codons GGC for residue 56 as Gln, !1and TAT for residue 80 as Thr REFERENCE A93193 !$#authors Wilkinson, J.M.; Grand, R.J.A. !$#journal Nature (1978) 271:31-35 !$#title Comparison of amino acid sequence of troponin I from !1different striated muscles. !$#cross-references MUID:78114026; PMID:146828 !$#accession A93193 !'##molecule_type protein !'##residues 2-154,158-182 ##label WIL REFERENCE A90286 !$#authors Wilkinson, J.M.; Grand, R.J.A. !$#journal Biochem. J. (1975) 149:493-496 !$#title The amino acid sequence of troponin I from rabbit skeletal !1muscle. !$#cross-references MUID:76039510; PMID:1180911 !$#accession A90286 !'##molecule_type protein !'##residues 2-114,'R',115-154,158-182 ##label WI2 REFERENCE A91408 !$#authors Moir, A.J.G.; Wilkinson, J.M.; Perry, S.V. !$#journal FEBS Lett. (1974) 42:253-256 !$#title The phosphorylation sites of troponin I from white skeletal !1muscle of the rabbit. !$#cross-references MUID:74309023; PMID:4369337 !$#contents annotation; phosphorylation sites REFERENCE A91407 !$#authors Huang, T.S.; Bylund, D.B.; Stull, J.T.; Krebs, E.G. !$#journal FEBS Lett. (1974) 42:249-252 !$#title The amino acid sequences of the phosphorylated sites in !1troponin-I from rabbit skeletal muscle. !$#cross-references MUID:74308154; PMID:4369265 !$#contents annotation; phosphorylation sites REFERENCE I46471 !$#authors Putney, S.D.; Herlihy, W.C.; Schimmel, P. !$#journal Nature (1983) 302:718-721 !$#title A new troponin T and cDNA clones for 13 different muscle !1proteins, found by shotgun sequencing. !$#cross-references MUID:83167564; PMID:6687628 !$#accession I46514 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 166-178 ##label PUT !'##cross-references EMBL:V00898; NID:g1738; PIDN:CAA24263.1; !1PID:g929767 COMPLEX troponin is a heterotrimer with one molecule each of !1troponin C (calcium binding component), troponin I !1(inhibitory component), and troponin T (tropomyosin-binding !1component) FUNCTION !$#description binds actin and inhibits myosin ATPase activity; with !1tropomyosin mediates contraction of vertebrate striated !1muscle in response to calcium !$#pathway muscle contraction CLASSIFICATION #superfamily troponin I KEYWORDS acetylated amino end; actin binding; muscle contraction; !1phosphoprotein; skeletal muscle FEATURE !$2 #modified_site acetylated amino end (Gly) (in mature !8form) #status experimental\ !$12 #binding_site phosphate (Thr) (covalent) (by !8cAMP-dependent kinase) #status experimental\ !$20,90,118 #binding_site phosphate (Ser) (covalent) (by !8cAMP-dependent kinase) #status experimental SUMMARY #length 182 #molecular-weight 21214 #checksum 8861 SEQUENCE /// ENTRY TPCHIS #type complete TITLE troponin I, fast skeletal muscle - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 31-May-1979 #sequence_revision 02-Dec-1994 #text_change 24-Nov-1999 ACCESSIONS A24918; A03088; I50714 REFERENCE A24918 !$#authors Nikovits Jr., W.; Kuncio, G.; Ordahl, C.P. !$#journal Nucleic Acids Res. (1986) 14:3377-3390 !$#title The chicken fast skeletal troponin I gene: exon organization !1and sequence. !$#cross-references MUID:86205240; PMID:3010234 !$#accession A24918 !'##molecule_type mRNA !'##residues 1-183 ##label NIK REFERENCE A03088 !$#authors Wilkinson, J.M.; Grand, R.J.A. !$#journal Eur. J. Biochem. (1978) 82:493-501 !$#title The amino-acid sequence of chicken fast-skeletal-muscle !1troponin I. !$#cross-references MUID:78106727; PMID:624283 !$#accession A03088 !'##molecule_type protein !'##residues 2-183 ##label WIL !'##note the sequences of troponin I from leg and breast muscle are !1apparently identical REFERENCE I50714 !$#authors Quaggio, R.B.; Ferro, J.A.; Monteiro, P.B.; Reinach, F.C. !$#journal Protein Sci. (1993) 2:1053-1056 !$#title Cloning and expression of chicken skeletal muscle troponin I !1in Escherichia coli: the role of rare codons on the !1expression level. !$#cross-references MUID:93306193; PMID:8318890 !$#accession I50714 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-183 ##label QUA !'##cross-references EMBL:U19926; NID:g642959; PIDN:AAA61952.1; !1PID:g642960 GENETICS !$#gene tni CLASSIFICATION #superfamily troponin I KEYWORDS actin binding; blocked amino end FEATURE !$2-183 #product troponin I, fast skeletal muscle #status !8experimental #label MAT\ !$2 #modified_site blocked amino end (Ser) (in mature !8form) (probably acetylated) #status experimental SUMMARY #length 183 #molecular-weight 21234 #checksum 225 SEQUENCE /// ENTRY TPHUIW #type complete TITLE troponin I, slow skeletal muscle - human ORGANISM #formal_name Homo sapiens #common_name man DATE 06-Jan-1995 #sequence_revision 03-May-1996 #text_change 22-Jun-1999 ACCESSIONS A53740; A35355 REFERENCE A53740 !$#authors Corin, S.J.; Juhasz, O.; Zhu, L.; Conley, P.; Kedes, L.; !1Wade, R. !$#journal J. Biol. Chem. (1994) 269:10651-10659 !$#title Structure and expression of the human slow twitch skeletal !1muscle troponin I gene. !$#cross-references MUID:94193765; PMID:8144655 !$#accession A53740 !'##molecule_type DNA !'##residues 1-187 ##label COR !'##cross-references GB:L21905 REFERENCE A35355 !$#authors Wade, R.; Eddy, R.; Shows, T.B.; Kedes, L. !$#journal Genomics (1990) 7:346-357 !$#title cDNA sequence, tissue-specific expression, and chromosomal !1mapping of the human slow-twitch skeletal muscle isoform of !1troponin I. !$#cross-references MUID:90307007; PMID:2365354 !$#accession A35355 !'##molecule_type mRNA !'##residues 1-181,'NA',184-187 ##label WAD !'##cross-references GB:J04760; NID:g339964; PIDN:AAA61228.1; !1PID:g339965 GENETICS !$#gene GDB:TNNI1 !'##cross-references GDB:120443; OMIM:191042 !$#map_position 1q32-1q32 !$#introns 4/2; 5/3; 19/3; 63/3; 93/3; 152/3 !$#note the first intron occurs before the initiator codon COMPLEX troponin is a heterotrimer with one molecule each of !1troponin C (calcium binding component), troponin I !1(inhibitory component), and troponin T (tropomyosin-binding !1component) FUNCTION !$#description binds actin and inhibits myosin ATPase activity; with !1tropomyosin mediates contraction of vertebrate striated !1muscle in response to calcium !$#pathway muscle contraction CLASSIFICATION #superfamily troponin I KEYWORDS acetylated amino end; actin binding; muscle contraction; !1skeletal muscle FEATURE !$2 #modified_site acetylated amino end (Pro) (in mature !8form) #status predicted SUMMARY #length 187 #molecular-weight 21692 #checksum 7017 SEQUENCE /// ENTRY TPRBIW #type complete TITLE troponin I, slow skeletal muscle - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 30-Apr-1979 #sequence_revision 30-Apr-1979 #text_change 24-Nov-1999 ACCESSIONS A03089 REFERENCE A90296 !$#authors Grand, R.J.A.; Wilkinson, J.M. !$#journal Biochem. J. (1977) 167:183-192 !$#title The amino acid sequence of rabbit slow-muscle troponin I. !$#cross-references MUID:78060292; PMID:588250 !$#accession A03089 !'##molecule_type protein !'##residues 1-184 ##label GRA !'##note some of the molecules lack residues 183 and 184 COMPLEX troponin is a heterotrimer with one molecule each of !1troponin C (calcium binding component), troponin I !1(inhibitory component), and troponin T (tropomyosin-binding !1component) FUNCTION !$#description binds actin and inhibits myosin ATPase activity; with !1tropomyosin mediates contraction of vertebrate striated !1muscle in response to calcium !$#pathway muscle contraction CLASSIFICATION #superfamily troponin I KEYWORDS actin binding; blocked amino end FEATURE !$1 #modified_site blocked amino end (Pro) (partial) !8(probably acetylated) #status experimental SUMMARY #length 184 #molecular-weight 21143 #checksum 4497 SEQUENCE /// ENTRY TPHUIC #type complete TITLE troponin I, cardiac muscle - human ORGANISM #formal_name Homo sapiens #common_name man DATE 03-May-1994 #sequence_revision 03-May-1996 #text_change 22-Jun-1999 ACCESSIONS A61229; JN0837; S11522; A33185; S63690 REFERENCE A61229 !$#authors Hunkeler, N.M.; Kullman, J.; Murphy, A.M. !$#journal Circ. Res. (1991) 69:1409-1414 !$#title Troponin I isoform expression in human heart. !$#cross-references MUID:92035427; PMID:1934363 !$#accession A61229 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-210 ##label HUN REFERENCE JN0837 !$#authors Armour, K.L.; Harris, W.J.; Tempest, P.R. !$#journal Gene (1993) 131:287-292 !$#title Cloning and expression in Escherichia coli of the cDNA !1encoding human cardiac troponin I. !$#cross-references MUID:94010323; PMID:8406024 !$#accession JN0837 !'##molecule_type mRNA !'##residues 1-210 ##label AR2 !'##cross-references GB:M64247; NID:g339966; PIDN:AAA16157.1; !1PID:g339967 REFERENCE S11522 !$#authors Vallins, W.J.; Brand, N.J.; Dabhade, N.; Butler-Browne, G.; !1Yacoub, M.H.; Barton, P.J.R. !$#journal FEBS Lett. (1990) 270:57-61 !$#title Molecular cloning of human cardiac troponin I using !1polymerase chain reaction. !$#cross-references MUID:91032031; PMID:2226790 !$#accession S11522 !'##molecule_type mRNA !'##residues 1-85,'T',87-210 ##label VAL !'##cross-references EMBL:X54163; NID:g37427; PIDN:CAA38102.1; !1PID:g37428 REFERENCE S12886 !$#authors Mittmann, K.; Jaquet, K.; Heilmeyer Jr., L.M.G. !$#journal FEBS Lett. (1990) 273:41-45 !$#title A common motif of two adjacent phosphoserines in bovine, !1rabbit and human cardiac troponin I. !$#cross-references MUID:91032199; PMID:2226863 !$#contents annotation; acetylated amino end; phosphorylation sites GENETICS !$#gene GDB:TNNI3 !'##cross-references GDB:125309; OMIM:191044 !$#map_position 19p13.2-19q13.2 COMPLEX troponin is a heterotrimer with one molecule each of !1troponin C (calcium binding component), troponin I !1(inhibitory component), and troponin T (tropomyosin-binding !1component) FUNCTION !$#description binds actin and inhibits myosin ATPase activity; with !1tropomyosin mediates contraction of vertebrate striated !1muscle in response to calcium !$#pathway muscle contraction CLASSIFICATION #superfamily troponin I KEYWORDS acetylated amino end; actin binding; cardiac muscle; heart; !1muscle contraction; phosphoprotein FEATURE !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental\ !$23,24 #binding_site phosphate (Ser) (covalent) (by !8cAMP-dependent kinase) #status experimental SUMMARY #length 210 #molecular-weight 24007 #checksum 1669 SEQUENCE /// ENTRY TPRBIC #type complete TITLE troponin I, cardiac muscle - rabbit (tentative sequence) ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 24-Apr-1984 #sequence_revision 03-May-1996 #text_change 31-Mar-2000 ACCESSIONS A90296; A90294; S12886; A03090 REFERENCE A90296 !$#authors Grand, R.J.A.; Wilkinson, J.M. !$#journal Biochem. J. (1977) 167:183-192 !$#title The amino acid sequence of rabbit slow-muscle troponin I. !$#cross-references MUID:78060292; PMID:588250 !$#accession A90296 !'##molecule_type protein !'##residues 1-4,'R',6-16,18-20,22,'D',27-211 ##label GRA REFERENCE A90294 !$#authors Grand, R.J.A.; Wilkinson, J.M.; Mole, L.E. !$#journal Biochem. J. (1976) 159:633-641 !$#title The amino acid sequence of rabbit cardiac troponin I. !$#cross-references MUID:77087072; PMID:1008822 !$#accession A90294 !'##molecule_type protein !'##residues 1-4,'R',6-11,'K',13-16,18-20,22,'D',27-211 ##label GR2 REFERENCE S12886 !$#authors Mittmann, K.; Jaquet, K.; Heilmeyer Jr., L.M.G. !$#journal FEBS Lett. (1990) 273:41-45 !$#title A common motif of two adjacent phosphoserines in bovine, !1rabbit and human cardiac troponin I. !$#cross-references MUID:91032199; PMID:2226863 !$#accession S12886 !'##molecule_type protein !'##residues 1-36 ##label MIT !'##note peptide sequences corrected; amino terminal acetylation; !1phosphorylation sites REFERENCE A93181 !$#authors Solaro, R.J.; Moir, A.J.G.; Perry, S.V. !$#journal Nature (1976) 262:615-617 !$#title Phosphorylation of troponin I and the inotropic effect of !1adrenaline in the perfused rabbit heart. !$#cross-references MUID:76267707; PMID:958429 !$#contents annotation; phosphorylation sites COMPLEX troponin is a heterotrimer with one molecule each of !1troponin C (calcium binding component), troponin I !1(inhibitory component), and troponin T (tropomyosin-binding !1component) FUNCTION !$#description binds actin and inhibits myosin ATPase activity; with !1tropomyosin mediates contraction of vertebrate striated !1muscle in response to calcium !$#pathway muscle contraction CLASSIFICATION #superfamily troponin I KEYWORDS acetylated amino end; actin binding; cardiac muscle; heart; !1muscle contraction; phosphoprotein FEATURE !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$22,23 #binding_site phosphate (Ser) (covalent) (by !8cAMP-dependent kinase) #status experimental SUMMARY #length 211 #molecular-weight 24067 #checksum 6537 SEQUENCE /// ENTRY JQ1514 #type complete TITLE green-fluorescent protein [validated] - hydromedusa (Aequorea victoria) ORGANISM #formal_name Aequorea victoria DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 23-Mar-2001 ACCESSIONS JS0692; JQ1514; PQ0335; S48693; S51330; S51331 REFERENCE JQ1514 !$#authors Prasher, D.C.; Eckenrode, V.K.; Ward, W.W.; Prendergast, !1F.G.; Cormier, M.J. !$#journal Gene (1992) 111:229-233 !$#title Primary structure of the Aequorea victoria green-fluorescent !1protein. !$#cross-references MUID:92175527; PMID:1347277 !$#accession JS0692 !'##molecule_type DNA !'##residues 1-107,'S',109-238 ##label PRA1 !'##cross-references GB:M62654; NID:g155662; PIDN:AAA27722.1; !1PID:g155663 !$#accession JQ1514 !'##molecule_type mRNA !'##residues 1-99,'F',101-140,'L',142-218,'V',220-238 ##label PRA2 !'##cross-references GB:M62653; NID:g155660; PIDN:AAA27721.1; !1PID:g155661 !$#accession PQ0335 !'##molecule_type protein !'##residues 46-64;74-122;132-151;154-183;185-200 ##label PRA3 REFERENCE S48693 !$#authors Inouye, S.; Tsuji, F.I. !$#journal FEBS Lett. (1994) 351:211-214 !$#title Evidence for redox forms of the Aequorea green fluorescent !1protein. !$#cross-references MUID:94364470; PMID:8082767 !$#accession S48693 !'##status preliminary !'##molecule_type mRNA !'##residues 1-24,'Q',26-156,'P',158-171,'K',173-238 ##label INO !'##cross-references GB:L29345; NID:g606383; PIDN:AAA58246.1; !1PID:g606384 REFERENCE S51330 !$#authors Watkins, J.N.; Campbell, A.K. !$#submission submitted to the EMBL Data Library, January 1995 !$#accession S51330 !'##molecule_type mRNA !'##residues 1-13,'V',15-24,'Q',26-44,'N',46-153,'G',155-156,'P', !1158-171,'K',173-227,'R',229-238 ##label WAT !'##cross-references EMBL:X83959; NID:g634008; PIDN:CAA58789.1; !1PID:g634009 !'##experimental_source clone gfp1 !$#accession S51331 !'##molecule_type mRNA !'##residues 1-24,'Q',26-29,'R',31-83,'L',85-153,'G',155-156,'P', !1158-171,'K',173-208,'Q',210-211,'HG',214-218,'V',220-225, !1'S',227-238 ##label WA2 !'##cross-references EMBL:X83960; NID:g634010; PIDN:CAA58790.1; !1PID:g634011 !'##experimental_source clone gfp2 REFERENCE A65692 !$#authors Yang, F.; Moss, L.G.; Phillips Jr., G.N. !$#submission submitted to the Brookhaven Protein Data Bank, August 1996 !$#cross-references PDB:1GFL !$#contents annotation; X-ray crystallography, 1.9 angstroms, residues !1'A',2-79,'R',81-99,'F',101-140,'L',142-218,'V',220-230 !$#note engineered sequence based on JQ1514, cloned and expressed in !1Escherichia coli REFERENCE A58953 !$#authors Yang, F.; Moss, L.G.; Phillips Jr., G.N. !$#journal Nat. Biotechnol. (1996) 14:1246-1251 !$#title The molecular structure of green fluorescent protein. !$#cross-references MUID:98294543; PMID:9631087 !$#contents annotation; X-ray crystallography, 1.9 angstroms COMMENT This protein is excited by the photoprotein aequorin (see !1PIR:AQJFNV) emitting green light. COMMENT The chromophore of this protein is formed by modification of !1Ser-dehydro-Tyr-Gly within the polypeptide. GENETICS !$#gene GFP !$#introns 69/3; 167/3 CLASSIFICATION #superfamily green-fluorescent protein KEYWORDS chromoprotein; luminescence FEATURE !$65-67 #cross-link 5-imidazolinone (Ser-Gly) #status !8experimental\ !$66 #modified_site dehydrotyrosine (Tyr) #status !8experimental SUMMARY #length 238 #molecular-weight 26934 #checksum 7103 SEQUENCE /// ENTRY LPHUB #type complete TITLE apolipoprotein B-100 precursor - human CONTAINS apolipoprotein B-26; apolipoprotein B-48; apolipoprotein B-74 ORGANISM #formal_name Homo sapiens #common_name man DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 21-Jul-2000 ACCESSIONS A27850; A25679; A25263; A25267; A25266; A24320; A24684; !1A23817; A25774; A26533; A29671; A29287; A25572; A24738; !1B40133; A40133; A28002; A24269; A29659; A35783; A22006; !1B22006; I37180; I84452; I61909; I59510; I39474; I39469; !1I84624; I37179; PS0058 REFERENCE A27850 !$#authors Ludwig, E.H.; Blackhart, B.D.; Pierotti, V.R.; Caiati, L.; !1Fortier, C.; Knott, T.; Scott, J.; Mahley, R.W.; !1Levy-Wilson, B.; McCarthy, B.J. !$#journal DNA (1987) 6:363-372 !$#title DNA sequence of the human apolipoprotein B gene. !$#cross-references MUID:88003974; PMID:3652907 !$#accession A27850 !'##molecule_type DNA !'##residues 1-617,'A',619-1929,'F',1931-3318,'D',3320-3426,'T', !13428-3431,'Q',3433-3731,'I',3733-3948,'F',3950-3963,'Y', !13965-4180,'E',4182-4563 ##label LUD !'##cross-references GB:M14162 REFERENCE A91058 !$#authors Cladaras, C.; Hadzopoulou-Cladaras, M.; Nolte, R.T.; !1Atkinson, D.; Zannis, V.I. !$#journal EMBO J. (1986) 5:3495-3507 !$#title The complete sequence and structural analysis of human !1apolipoprotein B-100: relationship between apoB-100 and !1apoB-48 forms. !$#cross-references MUID:87161758; PMID:3030729 !$#accession A25679 !'##molecule_type mRNA !'##residues 1-11,15-2539,'S',2541-3823,'R',3825-4563 ##label CLA !'##note 1109-Asp was also found REFERENCE A93639 !$#authors Knott, T.J.; Wallis, S.C.; Powell, L.M.; Pease, R.J.; Lusis, !1A.J.; Blackhart, B.; McCarthy, B.J.; Mahley, R.W.; !1Levy-Wilson, B.; Scott, J. !$#journal Nucleic Acids Res. (1986) 14:7501-7503 !$#title Complete cDNA and derived protein sequence of human !1apolipoprotein B-100. !$#cross-references MUID:87016385; PMID:3763409 !$#accession A25263 !'##molecule_type mRNA !'##residues 1-272,'N',274-617,'A',619-1217,'E',1219-2091,'V',2093-2364, !1'T',2366-2679,'Q',2681-4563 ##label KNO !'##cross-references GB:X04506; NID:g34330; PIDN:CAA28191.1; PID:g34331 REFERENCE A94134 !$#authors Law, S.W.; Grant, S.M.; Higuchi, K.; Hospattankar, A.; !1Lackner, K.; Lee, N.; Brewer Jr., H.B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:8142-8146 !$#title Human liver apolipoprotein B-100 cDNA: complete nucleic acid !1and derived amino acid sequence. !$#cross-references MUID:87041416; PMID:3464946 !$#accession A25267 !'##molecule_type mRNA !'##residues 1-617,'A',619-703,'P',705-792,'R',794-1270,'S',1272-1866, !1'G',1868-2036,'N',2038-2217,'T',2219-2932,'S',2934-3285,'I', !13287-3318,'D',3320-3430,'P',3432-3781,'T',3783-3963,'Y', !13965-4187,'K',4189-4220,'M',4222-4563 ##label LAW !'##note the codons given for residues 704, 793, 1271, 2037, 2933, 3286, !13782, 4188, and 4221 are inconsistent with the authors' !1translation REFERENCE A92556 !$#authors Chen, S.H.; Yang, C.Y.; Chen, P.F.; Setzer, D.; Tanimura, !1M.; Li, W.H.; Gotto Jr., A.M.; Chan, L. !$#journal J. Biol. Chem. (1986) 261:12918-12921 !$#title The complete cDNA and amino acid sequence of human !1apolipoprotein B-100. !$#cross-references MUID:87008488; PMID:3759943 !$#accession A25266 !'##molecule_type mRNA !'##residues 1-97,'I',99-328,'V',330-644,'I',646-918,'P',920-3318,'D', !13320-3426,'T',3428-3431,'Q',3433-3731,'I',3733-3875,'A', !13877-3948,'F',3950-3963,'Y',3965-4109,'DH',4112-4121,'E', !14123-4127,'E',4129-4132,'G',4134-4180,'E',4182-4563 ##label !1CHE !'##cross-references GB:J02610; NID:g178803; PIDN:AAA35549.1; !1PID:g178804 !'##note a total of 2366 residues were confirmed by direct sequencing of !1tryptic peptides REFERENCE A24320 !$#authors Protter, A.A.; Hardman, D.A.; Sato, K.Y.; Schilling, J.W.; !1Yamanaka, M.; Hort, Y.J.; Hjerrild, K.A.; Chen, G.C.; Kane, !1J.P. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:5678-5682 !$#title Analysis of cDNA clones encoding the entire B-26 region of !1human apolipoprotein B. !$#cross-references MUID:86287319; PMID:3461454 !$#accession A24320 !'##molecule_type mRNA !'##residues 1-97,'I',99-617,'A',619-941,'YYIWSLPPKP',951-1138, !1'PTGRLPNCFSNGLICYSLWLHSFQE',1165-1179,'R',1181-1370, !1'GLLQWWQHQHRPFQ',1385-1444,'I',1446-1534,'E',1536-1669,'D' !1##label PR2 !'##cross-references GB:M14081; NID:g178795; PIDN:AAA51752.1; !1PID:g553189 REFERENCE A24684 !$#authors Law, S.W.; Lackner, K.J.; Hospattankar, A.V.; Anchors, J.M.; !1Sakaguchi, A.Y.; Naylor, S.L.; Brewer Jr., H.B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:8340-8344 !$#title Human apolipoprotein B-100: cloning, analysis of liver mRNA, !1and assignment of the gene to chromosome 2. !$#cross-references MUID:86094221; PMID:3001697 !$#accession A24684 !'##molecule_type mRNA !'##residues 485-617,'A',619-1044 ##label LA2 !'##cross-references GB:M12480; NID:g178791; PIDN:AAA51751.1; !1PID:g178792 REFERENCE A94088 !$#authors Protter, A.A.; Hardman, D.A.; Schilling, J.W.; Miller, J.; !1Appleby, V.; Chen, G.C.; Kirsher, S.W.; McEnroe, G.; Kane, !1J.P. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:1467-1471 !$#title Isolation of a cDNA clone encoding the amino-terminal region !1of human apolipoprotein B. !$#cross-references MUID:86149325; PMID:3513177 !$#accession A23817 !'##molecule_type mRNA !'##residues 1-291 ##label PRO !'##cross-references GB:M12681; NID:g178797; PIDN:AAA51753.1; !1PID:g178798 REFERENCE A25774 !$#authors Deeb, S.S.; Motulsky, A.G.; Albers, J.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:4983-4986 !$#title A partial cDNA clone for human apoliprotein B. !$#cross-references MUID:85270450; PMID:3860836 !$#accession A25774 !'##molecule_type mRNA !'##residues 709-791,'SSSWKAASHGCPHSAGD',810-906 ##label DEE !'##cross-references GB:K03175; NID:g178821; PIDN:AAA51759.1; !1PID:g178822 REFERENCE A91565 !$#authors Carlsson, P.; Darnfors, C.; Olofsson, S.O.; Bjursell, G. !$#journal Gene (1986) 49:29-51 !$#title Analysis of the human apolipoprotein B gene; complete !1structure of the B-74 region. !$#cross-references MUID:87191999; PMID:2883086 !$#accession A26533 !'##molecule_type mRNA !'##residues 1282-2721,2742-3290,'L',3292-3336,'N',3338-3948,'F', !13950-3963,'Y',3965-4180,'E',4182-4563 ##label CAR !'##cross-references GB:M15421; NID:g178817; PIDN:AAA51758.1; !1PID:g178818 REFERENCE A29671 !$#authors Hardman, D.A.; Protter, A.A.; Chen, G.C.; Schilling, J.W.; !1Sato, K.Y.; Lau, K.; Yamanaka, M.; Mikita, T.; Miller, J.; !1Crisp, T.; McEnroe, G.; Scarborough, R.M.; Kane, J.P. !$#journal Biochemistry (1987) 26:5478-5486 !$#title Structural comparison of human apolipoproteins B-48 and !1B-100. !$#cross-references MUID:88050832; PMID:3676265 !$#accession A29671 !'##molecule_type mRNA !'##residues 1671-2323,'PYW',2327-2352,'H',2354-2398 ##label HAR !'##cross-references GB:M17367; NID:g178731; PIDN:AAA51741.1; !1PID:g178732 REFERENCE A90084 !$#authors Shoulders, C.C.; Myant, N.B.; Sidoli, A.; Rodriguez, J.C.; !1Cortese, C.; Baralle, F.E.; Cortese, R. !$#journal Atherosclerosis (1985) 58:277-289 !$#title Molecular cloning of human LDL apolipoprotein B cDNA. !1Evidence for more than one gene per haploid genome. !$#cross-references MUID:86130855; PMID:3841481 !$#accession A29287 !'##molecule_type mRNA !'##residues 3846-4298 ##label SHO REFERENCE A25572 !$#authors Pfitzner, R.; Wagener, R.; Stoffel, W. !$#journal Biol. Chem. Hoppe-Seyler (1986) 367:1077-1083 !$#title Isolation, expression and characterization of a human !1apolipoprotein B 100-specific cDNA clone. !$#cross-references MUID:87076044; PMID:3024665 !$#accession A25572 !'##molecule_type mRNA !'##residues 4219-4337,'S',4339-4563 ##label PFI !'##cross-references GB:M36676 REFERENCE A24738 !$#authors Wei, C.F.; Chen, S.H.; Yang, C.Y.; Marcel, Y.L.; Milne, !1R.W.; Li, W.H.; Sparrow, J.T.; Gotto, A.M.; Chan, L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:7265-7269 !$#cross-references MUID:86042646; PMID:2932736 !$#accession A24738 !'##molecule_type mRNA !'##residues 'N',3729-3731,'I',3733-3875,'A',3877-3948,'F',3950-3963, !1'Y',3965-3982,'S',3984-4001,'P',4003-4109,'DH',4112-4121, !1'E',4123-4127,'E',4129-4132,'G',4134-4180,'E',4182-4563 !1##label WE1 !'##cross-references GB:M12413; NID:g178735; PIDN:AAA51742.1; !1PID:g178736 REFERENCE A40133 !$#authors Chen, S.H.; Habib, G.; Yang, C.Y.; Gu, Z.W.; Lee, B.R.; !1Weng, S.; Silberman, S.R.; Cai, S.J.; Deslypere, J.P.; !1Rosseneu, M.; Gotto Jr., A.M.; Li, W.H.; Chan, L. !$#journal Science (1987) 238:363-366 !$#title Apolipoprotein B-48 is the product of a messenger RNA with !1an organ-specific in-frame stop codon. !$#cross-references MUID:88018019; PMID:3659919 !$#accession B40133 !'##molecule_type mRNA !'##residues 2165-2179 ##label CH1 !'##cross-references GB:M18036; NID:g178799; PIDN:AAA51754.1; !1PID:g178800 !'##note this mRNA includes the stop codon of the organ-specific mRNA !1for apo48 !$#accession A40133 !'##molecule_type protein !'##residues !151-75;101-110;129-139;158-174;197-207;276-287;298-304; !1306-314;526-532;538-557;636-669;696-707;779-797;950-960; !11001-1024;1028-1043;1053-1078;1092-1099;1122-1128;1312-1317; !11393-1415;1430-1436;1486-1498;1537-1556;1563-1572;1601-1610; !11647-1661;1697-1724;1770-1781;1859-1897;1968-1982;2005-2012; !12044-2062;2151-2178 ##label CH2 !'##note these fragments were derived from apo48 REFERENCE A28002 !$#authors Hardman, D.A.; Protter, A.A.; Schilling, J.W.; Kane, J.P. !$#journal Biochem. Biophys. Res. Commun. (1987) 149:1214-1219 !$#title Carboxyl terminal analysis of human B-48 protein confirms !1the novel mechanism proposed for chain termination. !$#cross-references MUID:88106542; PMID:3426612 !$#accession A28002 !'##molecule_type mRNA !'##residues 2129-2179,2181-2235 ##label HA2 !'##cross-references GB:M18471 !'##experimental_source intestine !'##note this mRNA from intestine includes a stop codon created by RNA !1editing in place of residue 2180; a carboxyl-terminal Ile !1residue was detected REFERENCE A24269 !$#authors Mehrabian, M.; Schumaker, V.N.; Fareed, G.C.; West, R.; !1Johnson, D.F.; Kirchgessner, T.; Lin, H.C.; Wang, X.; Ma, !1Y.; Mendiaz, E.; Lusis, A.J. !$#journal Nucleic Acids Res. (1985) 13:6937-6953 !$#title Human apolipoprotein B: identification of cDNA clones and !1characterization of mRNA. !$#cross-references MUID:86041888; PMID:3903660 !$#accession A24269 !'##molecule_type mRNA !'##residues 3056-3159 ##label MEH !'##cross-references GB:X03045; NID:g28783; PIDN:CAA26850.1; PID:g929609 REFERENCE A29659 !$#authors Hospattankar, A.V.; Higuchi, K.; Law, S.W.; Meglin, N.; !1Brewer Jr., H.B. !$#journal Biochem. Biophys. Res. Commun. (1987) 148:279-285 !$#title Identification of a novel in-frame translational stop codon !1in human intestine ApoB mRNA. !$#cross-references MUID:88049670; PMID:2445342 !$#accession A29659 !'##molecule_type mRNA !'##residues 2169-2179 ##label HOS !'##note the sequence shown represents the carboxyl end of !1apolipoprotein B-48 !'##note two RNA species, 14.1kb and 7.5kb in length, were isolated from !1the human intestine by hybridization with a cDNA probe of !1the 5' region of the apoB-100 mRNA. In the shorter mRNA !1sequence, which encodes the 250K apoB-48, CAA encoding !12180-Gln is substituted by the stop codon TAA, this mRNA !1encodes the 250K apoB-48 REFERENCE A35783 !$#authors Yang, C.; Kim, T.W.; Weng, S.; Lee, B.; Yang, M.; Gotto Jr., !1A.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:5523-5527 !$#title Isolation and characterization of sulfhydryl and disulfide !1peptides of human apolipoprotein B-100. !$#cross-references MUID:90319144; PMID:2115173 !$#contents disulfide bonds !$#accession A35783 !'##molecule_type protein !'##residues 28-41;76-97,'I', !199-100;175-193;206-215;239-249;259-266;357-399;455-490; !1512-521;961-1000;1101-1115;1416-1427;1499-1507;1662-1683; !13184-3202;3322-3344;3906-3910,'Y',3912-3935;4214-4222 !1##label YAN !'##note cysteines at positions 1112, 1422, 1505, 1662, 3761, 3917, and !14217 have free sulfhydryls; it is not known whether Cys-2933 !1and Cys-4353 have free sulfhydryls REFERENCE A22006 !$#authors LeBoeuf, R.C.; Miller, C.; Shively, J.E.; Schumaker, V.N.; !1Balla, M.A.; Lusis, A.J. !$#journal FEBS Lett. (1984) 170:105-108 !$#title Human apolipoprotein B: partial amino acid sequence. !$#cross-references MUID:84208786; PMID:6373369 !$#accession A22006 !'##molecule_type protein !'##residues 873-892,'K',894-896 ##label LE1 !$#accession B22006 !'##molecule_type protein !'##residues 3113,'L',3115-3130,'R',3132-3133,'P',3135-3136,'R' ##label !1LE2 REFERENCE A92564 !$#authors Blackhart, B.D.; Ludwig, E.M.; Pierotti, V.R.; Caiati, L.; !1Onasch, M.A.; Wallis, S.C.; Powell, L.; Pease, R.; Knott, !1T.J.; Chu, M.L.; Mahley, R.W.; Scott, J.; McCarthy, B.J.; !1Levy-Wilson, B. !$#journal J. Biol. Chem. (1986) 261:15364-15367 !$#title Structure of the human apolipoprotein B gene. !$#cross-references MUID:87057153; PMID:2946672 !$#contents annotation; gene structure REFERENCE A90715 !$#authors Wagener, R.; Pfitzner, R.; Stoffel, W. !$#journal Biol. Chem. Hoppe-Seyler (1987) 368:419-425 !$#title Studies on the organization of the human apolipoprotein B !1100 gene. !$#cross-references MUID:87271140; PMID:2886136 !$#contents annotation; gene structure REFERENCE A92605 !$#authors Weisgraber, K.H.; Rall Jr., S.C. !$#journal J. Biol. Chem. (1987) 262:11097-11103 !$#title Human apolipoprotein B-100 heparin-binding sites. !$#cross-references MUID:87280197; PMID:3301850 !$#contents annotation; heparin binding and disulfide bond REFERENCE A90125 !$#authors Dashti, N.; Lee, D.M.; Mok, T. !$#journal Biochem. Biophys. Res. Commun. (1986) 137:493-499 !$#title Apolipoprotein B is a calcium binding protein. !$#cross-references MUID:86242245; PMID:3087360 !$#contents annotation; calcium binding REFERENCE I37178 !$#authors Carlsson, P.; Olofsson, S.O.; Bondjers, G.; Darnfors, C.; !1Wiklund, O.; Bjursell, G. !$#journal Nucleic Acids Res. (1985) 13:8813-8826 !$#title Molecular cloning of human apolipoprotein B cDNA. !$#cross-references MUID:86093680; PMID:3841204 !$#accession I37180 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1937-2018 ##label RE6 !'##cross-references EMBL:X03326; NID:g28790; PIDN:CAA27045.1; !1PID:g28791 !$#accession I84452 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 4183-4334 ##label RE2 !'##cross-references GB:M31030; NID:g178813; PIDN:AAA51756.1; !1PID:g178814 !$#accession I61909 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 3811-3948,'F',3950-3963,'Y',3965-4180,'E',4182 ##label RES !'##cross-references GB:M14570; EMBL:X03325; NID:g28788; !1PIDN:CAA27044.1; PID:g28789 REFERENCE I59510 !$#authors Knott, T.J.; Rall, S.C. !$#journal Science (1985) 230:37-43 !$#title Human apolipoprotein B: structure of carboxyl-terminal !1domains, sites of gene expression, and chromosomal !1localization. !$#cross-references MUID:85300528; PMID:2994225 !$#accession I59510 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 3109-3823,'R',3825-4563 ##label RE3 !'##cross-references GB:M10374; NID:g178789; PIDN:AAA51750.1; !1PID:g178790 REFERENCE I39474 !$#authors Higuchi, K.; Hospattankar, A.V.; Law, S.W.; Meglin, N.; !1Cortright, J.; Brewer, H.B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:1772-1776 !$#title Human apolipoprotein B (apoB) mRNA: Identification of two !1distinct apoB mRNAs, an mRNA with the apoB-100 sequence and !1an apoB mRNA containing a premature in-frame translational !1stop codon, in both liver and intestine. !$#cross-references MUID:88158075; PMID:2450346 !$#accession I39474 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 2127-2179 ##label RE4 !'##cross-references GB:M19734; NID:g178754; PIDN:AAA35544.1; !1PID:g178755 REFERENCE I39469 !$#authors Huang, L.S.; Ripps, M.E.; Korman, S.H.; Deckelbaum, R.J.; !1Breslow, J.L. !$#journal J. Biol. Chem. (1989) 264:11394-11400 !$#title Hypobetalipoproteinemia due to an apolipoprotein B gene exon !121 deletion derived by Alu-Alu recombination. !$#cross-references MUID:89291895; PMID:2567736 !$#accession I39469 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1042-1232 ##label RE5 !'##cross-references GB:J04838; NID:g178737; PIDN:AAA53373.1; !1PID:g178739 REFERENCE I46680 !$#authors Powell, L.M.; Wallis, S.C.; Pease, R.J.; Edwards, Y.H.; !1Knott, T.J.; Scott, J. !$#journal Cell (1987) 50:831-840 !$#title A novel form of tissue-specific RNA processing produces !1apolipoprotein-B48 in intestine. !$#cross-references MUID:87301727; PMID:3621347 !$#accession I84624 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 2115-2179 ##label RE7 !'##cross-references GB:M17779; NID:g178801; PIDN:AAA51755.1; !1PID:g178802 COMMENT ApoB-100 is the major component of very low density !1lipoproteins (VLDL), low density lipoproteins (LDL), and !1plasma chylomicrons. Binding of apoB-100 to the apoB,E !1receptor (LDL receptor) is necessary for the clearance of !1LDL from the circulation. ApoB also binds calcium and !1possibly heparin and immunoregulatory receptors of !1lymphocytes. COMMENT ApoB-100 is synthesized in the liver. Organ-specific mRNA !1editing in the intestine leads to an in-frame stop codon and !1the truncated form apo-B48. GENETICS !$#gene GDB:APOB !'##cross-references GDB:119686; OMIM:107730 !$#map_position 2p24-2p24 !$#introns 28/1; 41/1; 79/3; 128/2; 179/3; 231/3; 273/2; 302/1; 375/2; !1451/2; 490/3; 539/3; 610/2; 689/3; 748/3; 812/3; 868/3; 939/ !12; 1000/2; 1041/1; 1111/2; 1170/1; 1232/3; 1281/2; 1406/1; !13930/1; 3968/2; 4029/3 CLASSIFICATION #superfamily apolipoprotein B KEYWORDS atherosclerosis; calcium; cholesterol metabolism; !1chylomicron; glycoprotein; intestine; LDL; lipid binding; !1lipid transport; lipoprotein; liver; plasma; RNA editing; !1VLDL FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-4563 #product apolipoprotein B-100 #status predicted !8#label B100\ !$28-2179 #product apolipoprotein B-48 #status predicted #label !8B48\ !$28-1323 #product apolipoprotein B-26 #status predicted #label !8B26\ !$32-126,232-306, !$902-959,2043-2178, !$3161-3236, !$3383-3516,3686-3746 #region heparin binding #status experimental\ !$1324-4563 #product apolipoprotein B-74 #status predicted #label !8B74\ !$3372-3408 #region LDL receptor binding #status predicted\ !$34,185,983,1368, !$1377,1523,2239, !$2560,2779,2982, !$3101,3224,3336, !$3358,3411,3465, !$3895,4237,4431 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$39-88,78-97, !$186-212,245-261, !$385-390,478-513, !$966-976,3194-3324 #disulfide_bonds #status experimental SUMMARY #length 4563 #molecular-weight 515568 #checksum 6090 SEQUENCE /// ENTRY LPCHA1 #type complete TITLE apolipoprotein A-I precursor - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 31-Mar-1990 #sequence_revision 25-Aug-1995 #text_change 22-Jun-1999 ACCESSIONS JH0471; A29657; S01453; S28888; A29616; S00187; S10973; !1S11023; I50156 REFERENCE JH0471 !$#authors Bhattacharyya, N.; Chattapadhyay, R.; Hirsch, A.; Banerjee, !1D. !$#journal Gene (1991) 104:163-168 !$#title Isolation, characterization and sequencing of the chicken !1apolipoprotein-AI-encoding gene. !$#cross-references MUID:92009209; PMID:1916289 !$#accession JH0471 !'##molecule_type DNA !'##residues 1-264 ##label BHA REFERENCE A29657 !$#authors Byrnes, L.; Luo, C.C.; Li, W.H.; Yang, C.; Chan, L. !$#journal Biochem. Biophys. Res. Commun. (1987) 148:485-492 !$#title Chicken apolipoprotein A-I: cDNA sequence, tissue expression !1and evolution. !$#cross-references MUID:88049703; PMID:3118875 !$#accession A29657 !'##molecule_type mRNA !'##residues 1-264 ##label BYR !'##cross-references EMBL:M17961; NID:g211147; PIDN:AAA48593.1; !1PID:g211148 REFERENCE S01453 !$#authors Rajavashisth, T.B.; Dawson, P.A.; Williams, D.L.; !1Shackelford, J.E.; Lebherz, H.; Lusis, A.J. !$#journal J. Biol. Chem. (1987) 262:7058-7065 !$#title Structure, evolution, and regulation of chicken !1apolipoprotein A-I. !$#cross-references MUID:87222301; PMID:3108248 !$#accession S01453 !'##molecule_type mRNA !'##residues 1-15,'I',17-147,'K',149-264 ##label RAJ !'##cross-references GB:M25559; EMBL:J02739; NID:g211145; !1PIDN:AAA48592.1; PID:g211146 !$#accession S28888 !'##molecule_type protein !'##residues 25-44;230-256 ##label RA2 REFERENCE A29616 !$#authors Ferrari, S.; Tarugi, P.; Drusiani, E.; Calandra, S.; Fregni, !1M. !$#journal Gene (1987) 60:39-46 !$#title The complete sequence of chick apolipoprotein AI mRNA and !1its expression in the developing chick. !$#cross-references MUID:88152500; PMID:3126099 !$#accession A29616 !'##molecule_type mRNA !'##residues 1-264 ##label FER !'##cross-references EMBL:M18746; NID:g211149; PIDN:AAA48594.1; !1PID:g211150 REFERENCE S00187 !$#authors Yang, C.Y.; Gu, Z.W.; Patsch, W.; Weng, S.A.; Kim, T.W.; !1Chan, L. !$#journal FEBS Lett. (1987) 224:261-266 !$#title The complete amino acid sequence of proapolipoprotein A-I of !1chicken high density lipoproteins. !$#cross-references MUID:88083548; PMID:3121386 !$#accession S00187 !'##molecule_type protein !'##residues 19-264 ##label YAN REFERENCE S10973 !$#authors Banerjee, D.; Mukherjee, T.K.; Redman, C.M. !$#journal J. Cell Biol. (1985) 101:1219-1226 !$#title Biosynthesis of high density lipoprotein by chicken liver: !1intracellular transport and proteolytic processing of !1nascent apolipoprotein A-1. !$#cross-references MUID:86008443; PMID:3930506 !$#accession S10973 !'##molecule_type protein !'##residues 19,'H',21-23,'Q',25-44 ##label BAN !'##note the sequence from Fig. 4 is inconsistent with that from Table !1II in having 41-Thr REFERENCE S11023 !$#authors Shackelford, J.E.; Lebherz, H.G. !$#journal J. Biol. Chem. (1983) 258:7175-7180 !$#title Synthesis and secretion of apolipoprotein A1 by chick breast !1muscle. !$#cross-references MUID:83213468; PMID:6406496 !$#accession S11023 !'##molecule_type protein !'##residues 25-44 ##label SHA REFERENCE I50156 !$#authors Lamon-Fava, S.; Sastry, R.; Ferrari, S.; Rajavashisth, T.B.; !1Lusis, A.J.; Karathanasis, S.K. !$#journal J. Lipid Res. (1992) 33:831-842 !$#title Evolutionary distinct mechanisms regulate apolipoprotein A-I !1gene expression: Differences between avian and mammalian !1apoA-I gene transcription control regions. !$#cross-references MUID:92381402; PMID:1512510 !$#accession I50156 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-15,'I',17-264 ##label LAM !'##cross-references GB:M96012; NID:g211158; PIDN:AAA48597.1; !1PID:g211159 COMMENT This protein is synthesized only in the liver in mammals, !1whereas in chicken it is synthesized in a variety of !1peripheral tissues. COMMENT This protein is a major component of the high density !1lipoproteins in plasma. It acts as a cofactor for the !1lecithin cholesterol acyltransferase. GENETICS !$#gene ApoAI !$#introns 15/1; 66/2 CLASSIFICATION #superfamily apolipoprotein A-I KEYWORDS cholesterol metabolism; HDL; intestine; lipid binding; lipid !1transport; lipoprotein; liver; plasma; tandem repeat FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-24 #domain propeptide #status experimental #label PRO\ !$25-264 #product apolipoprotein A-I #status experimental !8#label MAT SUMMARY #length 264 #molecular-weight 30680 #checksum 966 SEQUENCE /// ENTRY LPRB1B #type complete TITLE apolipoprotein A-I precursor (clone pRBA-502) - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S00230; S20557 REFERENCE S00230 !$#authors Pan, T.C.; Hao, Q.L.; Yamin, T.T.; Dai, P.H.; Chen, B.S.; !1Chen, S.L.; Kroon, P.A.; Chao, Y.S. !$#journal Eur. J. Biochem. (1987) 170:99-104 !$#title Rabbit apolipoprotein A-I mRNA and gene. Evidence that !1rabbit apolipoprotein A-I is synthesized in the intestine !1but not in the liver. !$#cross-references MUID:88082866; PMID:3121329 !$#accession S00230 !'##molecule_type mRNA !'##residues 1-265 ##label PAN !'##cross-references EMBL:X06658; NID:g1461; PIDN:CAA29857.1; PID:g1462 !'##note the authors translated the codon AGC for residue 174 as Arg !$#accession S20557 !'##molecule_type DNA !'##residues 1-17,'R',19-44,'I',46-122,'Y',124-146,'V',148-265 ##label !1PAN2 !'##cross-references EMBL:X06659; NID:g1459; PIDN:CAA29858.1; PID:g1460 COMMENT This protein is synthesized in the small intestine. COMMENT This protein is a major component of the high density !1lipoproteins in plasma. It acts as a cofactor for the !1lecithin cholesterol acyltransferase. GENETICS !$#introns 15/1; 66/2 CLASSIFICATION #superfamily apolipoprotein A-I KEYWORDS cholesterol metabolism; HDL; intestine; lipid transport; !1plasma; tandem repeat FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-24 #domain propeptide #status predicted #label PRO\ !$25-265 #product apolipoprotein A-I #status experimental !8#label MAT SUMMARY #length 265 #molecular-weight 30375 #checksum 5991 SEQUENCE /// ENTRY LPRB1Z #type complete TITLE apolipoprotein A-I precursor (clone 2Zap AI) - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S06064 REFERENCE S06064 !$#authors Paraskevopoulou, T.B.; Kritis, A.; Zannis, V. !$#submission submitted to the EMBL Data Library, July 1989 !$#accession S06064 !'##molecule_type mRNA !'##residues 1-266 ##label PAR !'##cross-references EMBL:X15908; NID:g1457; PIDN:CAA34024.1; PID:g1458 COMMENT This protein is synthesized in the small intestine. COMMENT This protein is a major component of the high density !1lipoproteins in plasma. It acts as a cofactor for the !1lecithin cholesterol acyltransferase. CLASSIFICATION #superfamily apolipoprotein A-I KEYWORDS cholesterol metabolism; HDL; intestine; lipid transport; !1plasma; tandem repeat FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-24 #domain propeptide #status predicted #label PRO\ !$25-266 #product apolipoprotein A-I #status experimental !8#label MAT SUMMARY #length 266 #molecular-weight 30591 #checksum 9617 SEQUENCE /// ENTRY LPHUA1 #type complete TITLE apolipoprotein A-I precursor [validated] - human ALTERNATE_NAMES apoA-I-2; apoA-I-4; preproapoA-I; prostacyclin stabilizing factor ORGANISM #formal_name Homo sapiens #common_name man DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 08-Dec-2000 ACCESSIONS A90947; B90947; S02373; A93465; A21147; A93519; B93519; !1A93472; A94010; A21118; A90112; A90209; A30516; A31582; !1A34409; S02737; B19913; A56815; A54223; I39476; I39475; !1I55236; A03091; S16197 REFERENCE A90947 !$#authors Seilhamer, J.J.; Protter, A.A.; Frossard, P.; Levy-Wilson, !1B. !$#journal DNA (1984) 3:309-317 !$#title Isolation and DNA sequence of full-length cDNA and of the !1entire gene for human apolipoprotein AI-discovery of a new !1genetic polymorphism in the apo AI gene. !$#cross-references MUID:85026665; PMID:6207999 !$#accession A90947 !'##molecule_type DNA !'##residues 1-267 ##label SEI !'##cross-references GB:X01038; NID:g28769; PIDN:CAA25519.1; PID:g296635 !$#accession B90947 !'##molecule_type mRNA !'##residues 1-267 ##label SE2 !'##cross-references GB:X01038; NID:g28769; PIDN:CAA25519.1; PID:g296635 REFERENCE S02373 !$#authors Makrides, S.C.; Ruiz-Opazo, N.; Hayden, M.; Nussbaum, A.L.; !1Breslow, J.L.; Zannis, V.I. !$#journal Eur. J. Biochem. (1988) 173:465-471 !$#title Sequence and expression of Tangier apoA-I gene. !$#cross-references MUID:88196137; PMID:3129297 !$#accession S02373 !'##molecule_type DNA !'##residues 1-267 ##label MAK !'##cross-references EMBL:X07496; NID:g28774; PIDN:CAA30377.1; !1PID:g296729 REFERENCE A93465 !$#authors Shoulders, C.C.; Kornblihtt, A.R.; Munro, B.S.; Baralle, !1F.E. !$#journal Nucleic Acids Res. (1983) 11:2827-2837 !$#title Gene structure of human apolipoprotein A1. !$#cross-references MUID:83220822; PMID:6406984 !$#accession A93465 !'##molecule_type DNA !'##residues 1-267 ##label SHO !'##cross-references GB:J00098; GB:J00099; GB:J00100; GB:J00101; !1GB:J03222; GB:K01518; GB:M10372; GB:X00566; GB:X00567; !1NID:g178765; PIDN:AAB59514.1; PID:g178768 REFERENCE A21147 !$#authors Karathanasis, S.K.; Zannis, V.I.; Breslow, J.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:6147-6151 !$#title Isolation and characterization of the human apolipoprotein !1A-I gene. !$#cross-references MUID:84016011; PMID:6413973 !$#accession A21147 !'##molecule_type DNA !'##residues 1-267 ##label KAR !'##cross-references GB:J00098; GB:J03222; NID:g178765; PIDN:AAB59514.1; !1PID:g178768 REFERENCE A93519 !$#authors Sharpe, C.R.; Sidoli, A.; Shelley, C.S.; Lucero, M.A.; !1Shoulders, C.C.; Baralle, F.E. !$#journal Nucleic Acids Res. (1984) 12:3917-3932 !$#title Human apolipoproteins AI, AII, CII and CIII. cDNA sequences !1and mRNA abundance. !$#cross-references MUID:84221405; PMID:6328445 !$#accession A93519 !'##molecule_type mRNA !'##residues 1-267 ##label SHA !'##cross-references GB:X00566; NID:g28765; PIDN:CAA25232.1; PID:g732753 !$#accession B93519 !'##molecule_type DNA !'##residues 1-24 ##label SH2 REFERENCE A93472 !$#authors Cheung, P.; Chan, L. !$#journal Nucleic Acids Res. (1983) 11:3703-3715 !$#title Nucleotide sequence of cloned cDNA of human apolipoprotein !1A-I. !$#cross-references MUID:83220772; PMID:6304641 !$#accession A93472 !'##molecule_type mRNA !'##residues 1-267 ##label CHE !'##cross-references GB:J00098; GB:J00099; GB:J00100; GB:J00101; !1GB:J03222; GB:K01518; GB:M10372; GB:X00566; GB:X00567; !1NID:g178765; PIDN:AAB59514.1; PID:g178768 REFERENCE A94010 !$#authors Law, S.W.; Brewer Jr., H.B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:66-70 !$#title Nucleotide sequence and the encoded amino acids of human !1apolipoprotein A-I mRNA. !$#cross-references MUID:84119464; PMID:6198645 !$#accession A94010 !'##molecule_type mRNA !'##residues 1-267 ##label LAW !'##cross-references GB:J00098; GB:J00099; GB:J00100; GB:J00101; !1GB:J03222; GB:K01518; GB:M10372; GB:X00566; GB:X00567; !1NID:g178765; PIDN:AAB59514.1; PID:g178768 REFERENCE A21118 !$#authors Zannis, V.I.; Karathanasis, S.K.; Keutmann, H.T.; !1Goldberger, G.; Breslow, J.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:2574-2578 !$#title Intracellular and extracellular processing of human !1apolipoprotein A-I: secreted apolipoprotein A-I isoprotein 2 !1is a propeptide. !$#cross-references MUID:83195100; PMID:6405383 !$#accession A21118 !'##molecule_type mRNA !'##residues 1-24 ##label ZAN REFERENCE A90112 !$#authors Brewer Jr., H.B.; Fairwell, T.; Kay, L.; Meng, M.; Ronan, !1R.; Law, S.; Light, J.A. !$#journal Biochem. Biophys. Res. Commun. (1983) 113:626-632 !$#title Human plasma proapoa-I: isolation and amino-terminal !1sequence. !$#cross-references MUID:83256553; PMID:6409108 !$#accession A90112 !'##molecule_type protein !'##residues 19-27 ##label BRE REFERENCE A90209 !$#authors Brewer Jr., H.B.; Fairwell, T.; LaRue, A.; Ronan, R.; !1Houser, A.; Bronzert, T.J. !$#journal Biochem. Biophys. Res. Commun. (1978) 80:623-630 !$#title The amino acid sequence of human APOA-I, an apolipoprotein !1isolated from high density lipoproteins. !$#cross-references MUID:78123731; PMID:204308 !$#accession A90209 !'##molecule_type protein !'##residues 25-57,'Q',59-169,'QQ',172-267 ##label BR2 REFERENCE A30516 !$#authors Yui, Y.; Aoyama, T.; Morishita, H.; Takahashi, M.; Takatsu, !1Y.; Kawai, C. !$#journal J. Clin. Invest. (1988) 82:803-807 !$#title Serum prostacyclin stabilizing factor is identical to !1apolipoprotein A-I (Apo A-I). A novel function of Apo A-I. !$#cross-references MUID:88331387; PMID:3047170 !$#accession A30516 !'##molecule_type protein !'##residues 25-56 ##label YUI REFERENCE A31582 !$#authors Nichols, W.C.; Dwulet, F.E.; Liepnieks, J.; Benson, M.D. !$#journal Biochem. Biophys. Res. Commun. (1988) 156:762-768 !$#title Variant apolipoprotein AI as a major constituent of a human !1hereditary amyloid. !$#cross-references MUID:89050104; PMID:3142462 !$#accession A31582 !'##molecule_type protein !'##residues 25-49,'R',51-85,'D',87-107 ##label NIC !'##note variant sequence from patient with familial amyloidotic !1polyneuropathy type III REFERENCE A34409 !$#authors Manjunath, P.; Marcel, Y.L.; Uma, J.; Seidah, N.G.; !1Chretien, M.; Chapdelaine, A. !$#journal J. Biol. Chem. (1989) 264:16853-16857 !$#title Apolipoprotein A-I binds to a family of bovine seminal !1plasma proteins. !$#cross-references MUID:89380318; PMID:2506184 !$#accession A34409 !'##molecule_type protein !'##residues 25-48 ##label MAN REFERENCE S02737 !$#authors Stoffel, W.; Binczek, E. !$#journal Biol. Chem. Hoppe-Seyler (1988) 369:1055-1063 !$#title Structural requirements of human preproapolipoprotein AI for !1translocation and processing studied by site-directed !1mutagenesis in vitro. !$#cross-references MUID:89149957; PMID:3228490 !$#accession S02737 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-6,'AV',9,'LV',12-29 ##label STO !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE S16197 !$#authors Stoffel, W.; Binczek, E. !$#journal Biol. Chem. Hoppe-Seyler (1991) 372:481-488 !$#title Transient expression of wild type and mutant human !1apolipoprotein AI in COS cells. !$#cross-references MUID:92029676; PMID:1930731 !$#contents annotation; extension of studies in reference S02737 REFERENCE A19913 !$#authors Stoffel, W.; Kruger, E.; Deutzmann, R. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1983) 364:227-237 !$#title Cell-free translation of human liver apolipoprotein AI and !1AII mRNA processing of primary translation products. !$#cross-references MUID:83236195; PMID:6407957 !$#accession B19913 !'##molecule_type protein !'##residues 1-6,'X',8-13,'XXX',17-18,'XX',21,'X',23-25,'X',27-29 !1##label ST2 REFERENCE A56815 !$#authors Ehnholm, C.; Bozas, S.E.; Tenkanen, H.; Kirszbaum, L.; !1Metso, J.; Murphy, B.; Walker, I.D. !$#journal Biochim. Biophys. Acta (1991) 1086:255-260 !$#title The apolipoprotein A-I binding protein of placenta and the !1SP-40,40 protein of human blood are different proteins which !1both bind to apolipoprotein A-I. !$#cross-references MUID:92075698; PMID:1742316 !$#accession A56815 !'##molecule_type protein !'##residues 25-31,'P',33 ##label EHN !'##experimental_source serum !'##note sequence extracted from NCBI backbone (NCBIP:69759) !'##note 32-Trp was also found REFERENCE A54223 !$#authors Kunitake, S.T.; Carilli, C.T.; Lau, K.; Protter, A.A.; !1Naya-Vigne, J.; Kane, J.P. !$#journal Biochemistry (1994) 33:1988-1993 !$#title Identification of proteins associated with apolipoprotein !1A-I-containing lipoproteins purified by selected-affinity !1immunosorption. !$#cross-references MUID:94162201; PMID:8117655 !$#accession A54223 !'##molecule_type protein !'##residues 25-39 ##label KUN REFERENCE I39476 !$#authors Moguilevsky, N.; Roobol, C.; Loriau, R.; Guillaume, J.P.; !1Jacobs, P.; Cravador, A.; Herzog, A.; Brouwers, L.; Scarso, !1A.; Gilles, P.; Holmquist, L.; Carlson, L.A.; Bollen, A. !$#journal DNA (1989) 8:429-436 !$#title Production of human recombinant proapolipoprotein A-I in !1Escherichia coli: purification and biochemical !1characterization. !$#cross-references MUID:89377481; PMID:2673706 !$#accession I39476 !'##molecule_type mRNA !'##residues 19-267 ##label RES !'##cross-references GB:M29068; NID:g178774; PIDN:AAA51747.1; !1PID:g178775 REFERENCE I39475 !$#authors Higuchi, K.; Law, S.W.; Hoeg, J.M.; Schumacher, U.K.; !1Meglin, N.; Brewer, H.B. !$#journal J. Biol. Chem. (1988) 263:18530-18536 !$#title Tissue-specific expression of apolipoprotein A-I (ApoA-I) is !1regulated by the 5'-flanking region of the human ApoA-I !1gene. !$#cross-references MUID:89054040; PMID:3142880 !$#accession I39475 !'##molecule_type DNA !'##residues 1-14 ##label RE2 !'##cross-references GB:J04066; NID:g178763; PIDN:AAA51746.1; !1PID:g553183 REFERENCE A90042 !$#authors Breslow, J.L. !$#journal Annu. Rev. Biochem. (1985) 54:699-727 !$#title Human apolipoprotein molecular biology and genetic !1variation. !$#cross-references MUID:85278004; PMID:3896129 !$#contents annotation; review of sequences, variants and gene location REFERENCE A92577 !$#authors Hoeg, J.M.; Meng, M.S.; Ronan, R.; Fairwell, T.; Brewer Jr., !1H.B. !$#journal J. Biol. Chem. (1986) 261:3911-3914 !$#title Human apolipoprotein A-I. Post-translational modification by !1fatty acid acylation. !$#cross-references MUID:86140194; PMID:3005308 !$#contents annotation; acylation with palmitate !$#note an undetermined serine or threonine is acylated by fatty !1acid; the acylating fatty acid may be catalytically removed !1in plasma REFERENCE I55236 !$#authors Law, S.W.; Brewer, H.B. !$#journal J. Biol. Chem. (1985) 260:12810-12814 !$#title Tangier disease: The complete mRNA sequence encoding for !1preproapo-A-I. !$#cross-references MUID:86008382; PMID:2995392 !$#accession I55236 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-143,'D',145-267 ##label RE3 !'##cross-references GB:M11791; NID:g178776; PIDN:AAA35545.1; !1PID:g178777 COMMENT Apolipoprotein A-I precursor is synthesized in the liver and !1small intestine. The propeptide is cleaved extracellularly. !1ApoA-I makes up about 70% of the protein of the high density !1lipoproteins (HDL) in plasma. GENETICS !$#gene GDB:APOA1 !'##cross-references GDB:119684; OMIM:107680 !$#map_position 11q23.3-11q23.3 !$#introns 15/1; 67/2 FUNCTION !$#description participates in the reverse transport of cholesterol from !1tissues to the liver for excretion by promoting cholesterol !1efflux from tissues and by acting as a cofactor for lecithin !1cholesterol acyltransferase (LCAT); noncovalently binds and !1stabilizes prostacyclin (PGI-2) CLASSIFICATION #superfamily apolipoprotein A-I KEYWORDS atherosclerosis; cholesterol metabolism; HDL; intestine; !1lipid binding; lipid transport; lipoprotein; liver; plasma FEATURE !$1-18 #domain signal sequence #status experimental #label !8SIG\ !$19-24 #domain propeptide #status experimental #label PRO\ !$25-267 #product apolipoprotein A-I #status experimental !8#label MAT SUMMARY #length 267 #molecular-weight 30778 #checksum 3504 SEQUENCE /// ENTRY A26529 #type complete TITLE apolipoprotein A-I precursor - crab-eating macaque ORGANISM #formal_name Macaca fascicularis #common_name crab-eating macaque DATE 30-Sep-1989 #sequence_revision 19-Oct-1995 #text_change 22-Jun-1999 ACCESSIONS A26529; A26627; S23135; A57766 REFERENCE A26529 !$#authors Polites, H.G.; Melchior, G.W.; Castle, C.K.; Marotti, K.R. !$#journal Gene (1986) 49:103-110 !$#title The primary structure of cynomolgus monkey apolipoprotein !1A-1 deduced from the cDNA sequence: comparison to the human !1sequence. !$#cross-references MUID:87191989; PMID:3106152 !$#accession A26529 !'##molecule_type mRNA !'##residues 1-267 ##label POL !'##cross-references GB:M15411; NID:g342074; PIDN:AAA36834.1; !1PID:g342075 REFERENCE A26627 !$#authors Herbert, P.N.; Bausserman, L.L.; Lynch, K.M.; Saritelli, !1A.L.; Kantor, M.A.; Nicolosi, R.J.; Shulman, R.S. !$#journal Biochemistry (1987) 26:1457-1463 !$#title Homologues of the human C and A apolipoproteins in the !1Macaca fascicularis (cynomolgus) monkey. !$#cross-references MUID:87185451; PMID:3105581 !$#accession A26627 !'##molecule_type protein !'##residues 25-48 ##label HER REFERENCE S23135 !$#authors Murray, R.W.; Marotti, K.R. !$#journal Biochim. Biophys. Acta (1992) 1131:207-210 !$#title Nucleotide sequence of the cynomolgus monkey apolipoprotein !1A-I gene and corresponding flanking regions. !$#cross-references MUID:92305062; PMID:1610902 !$#accession S23135 !'##molecule_type DNA !'##residues 1-12,'L',14-267 ##label MUR !'##cross-references GB:M83242; NID:g342070; PIDN:AAA36832.1; !1PID:g342071 REFERENCE A57766 !$#authors Sorci-Thomas, M.; Kearns, M.W. !$#journal J. Biol. Chem. (1991) 266:18045-18050 !$#title Transcriptional regulation of the apolipoprotein A-I gene. !$#cross-references MUID:92011532; PMID:1917942 !$#accession A57766 !'##molecule_type DNA !'##residues 1-10 ##label RES !'##cross-references GB:M69223; NID:g342066; PIDN:AAA36831.1; !1PID:g553820 COMMENT The precursor is synthesized in the liver and small !1intestine. The propeptide is cleaved extracellularly. COMMENT ApoA-I makes up about 70% of the protein of the high density !1lipoproteins (HDL) in plasma and participates in the reverse !1transport of cholesterol from tissues to the liver for !1excretion by promoting cholesterol efflux from tissues and !1by acting as a cofactor for the lecithin cholesterol !1acyltransferase (LCAT). GENETICS !$#introns 15/1; 67/2 CLASSIFICATION #superfamily apolipoprotein A-I KEYWORDS cholesterol metabolism; HDL; intestine; lipid transport; !1plasma; tandem repeat FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-24 #domain propeptide #status predicted #label PPT\ !$25-267 #product apolipoprotein A-I #status predicted #label !8MAT SUMMARY #length 267 #molecular-weight 30719 #checksum 3746 SEQUENCE /// ENTRY LPDGA1 #type complete TITLE apolipoprotein A-I precursor - dog ORGANISM #formal_name Canis lupus familiaris #common_name dog DATE 17-Dec-1982 #sequence_revision 14-Jul-1994 #text_change 07-May-1999 ACCESSIONS A60940; A03092; A61418 REFERENCE A60940 !$#authors Luo, C.C.; Li, W.H.; Chan, L. !$#journal J. Lipid Res. (1989) 30:1735-1746 !$#title Structure and expression of dog apolipoprotein A-I, E, and !1C-I mRNAs: implications for the evolution and functional !1constraints of apolipoprotein structure. !$#cross-references MUID:90132271; PMID:2515239 !$#accession A60940 !'##molecule_type mRNA !'##residues 1-266 ##label LUO REFERENCE A03092 !$#authors Chung, H.; Randolph, A.; Reardon, I.; Heinrikson, R.L. !$#journal J. Biol. Chem. (1982) 257:2961-2967 !$#title The covalent structure of apolipoprotein A-I from canine !1high density lipoproteins. !$#cross-references MUID:82142425; PMID:6801039 !$#accession A03092 !'##molecule_type protein !'##residues 25-167,'G',169-201,'Q',203-234,'Q',236-266 ##label CHU REFERENCE A61418 !$#authors Nakai, T.; Whayne, T.F.; Tang, J. !$#journal FEBS Lett. (1976) 64:409-411 !$#title The amino- and carboxyl-terminal sequences of canine !1apolipoprotein A-I. !$#cross-references MUID:76210910; PMID:179887 !$#accession A61418 !'##molecule_type protein !'##residues 25-56,'Z';261-262,'A' ##label NAK CLASSIFICATION #superfamily apolipoprotein A-I KEYWORDS atherosclerosis; cholesterol metabolism; HDL; intestine; !1lipid transport; liver; plasma FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-24 #domain propeptide #status predicted #label PRO\ !$25-266 #product apolipoprotein A-I #status experimental !8#label MAT SUMMARY #length 266 #molecular-weight 30196 #checksum 5651 SEQUENCE /// ENTRY LPHUE #type complete TITLE apolipoprotein E precursor [validated] - human ALTERNATE_NAMES apo-E CONTAINS apolipoprotein E2; apolipoprotein E3; apolipoprotein E4; apolipoprotein E5 ORGANISM #formal_name Homo sapiens #common_name man DATE 06-Jul-1982 #sequence_revision 04-Dec-1986 #text_change 08-Dec-2000 ACCESSIONS A92478; A92481; A94047; A92368; A36536; JS0084; I37181; !1A03093 REFERENCE A92478 !$#authors Zannis, V.I.; McPherson, J.; Goldberger, G.; Karathanasis, !1S.K.; Breslow, J.L. !$#journal J. Biol. Chem. (1984) 259:5495-5499 !$#title Synthesis, intracellular processing, and signal peptide of !1human apolipoprotein E. !$#cross-references MUID:84185684; PMID:6325438 !$#contents variant E3 !$#accession A92478 !'##molecule_type mRNA !'##residues 1-317 ##label ZAN !'##cross-references GB:K00396; GB:X00199; NID:g178850; PIDN:AAB59546.1; !1PID:g178851 REFERENCE A92481 !$#authors McLean, J.W.; Elshourbagy, N.A.; Chang, D.J.; Mahley, R.W.; !1Taylor, J.M. !$#journal J. Biol. Chem. (1984) 259:6498-6504 !$#title Human apolipoprotein E mRNA. cDNA cloning and nucleotide !1sequencing of a new variant. !$#cross-references MUID:84212473; PMID:6327682 !$#contents variant E3 !$#accession A92481 !'##molecule_type mRNA !'##residues 1-116,'T',118-169,'P',171-317 ##label MCL !'##cross-references GB:M12529; NID:g178848; PIDN:AAB59518.1; !1PID:g178849 REFERENCE A94047 !$#authors Paik, Y.K.; Chang, D.J.; Reardon, C.A.; Davies, G.E.; !1Mahley, R.W.; Taylor, J.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:3445-3449 !$#title Nucleotide sequence and structure of the human !1apolipoprotein E gene. !$#cross-references MUID:85216517; PMID:2987927 !$#contents variant E4 !$#accession A94047 !'##molecule_type DNA !'##residues 1-129,'R',131-317 ##label PAI !'##cross-references GB:M10065; GB:J03053; GB:J03054; NID:g178852; !1PIDN:AAB59397.1; PID:g178853 REFERENCE A92368 !$#authors Rall Jr., S.C.; Weisgraber, K.H.; Mahley, R.W. !$#journal J. Biol. Chem. (1982) 257:4171-4178 !$#title Human apolipoprotein E. The complete amino acid sequence. !$#cross-references MUID:82167490; PMID:7068630 !$#contents variant E2 !$#accession A92368 !'##molecule_type protein !'##residues 19-175,'C',177-317 ##label RAL !'##note evidence is found for O-linked carbohydrate in the peptide for !1residues 57-79 REFERENCE A36536 !$#authors Hornes, E.; Hultman, T.; Moks, T.; Uhlen, M. !$#journal BioTechniques (1990) 9:730-737 !$#title Direct cloning of the human genomic apolipoprotein E gene !1using magnetic separation of single-stranded DNA. !$#cross-references MUID:91104014; PMID:2271176 !$#contents variant E4 !$#accession A36536 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 87-129,'R',131-196 ##label HOR REFERENCE JS0084 !$#authors Maeda, H.; Nakamura, H.; Kobori, S.; Okada, M.; Niki, H.; !1Ogura, T.; Hiraga, S. !$#journal J. Biochem. (1989) 105:491-493 !$#title Molecular cloning of a human apolipoprotein E variant: E5 !1(Glu3 -> Lys3). !$#cross-references MUID:89340369; PMID:2760009 !$#contents variant E5 !$#accession JS0084 !'##molecule_type DNA !'##residues 1-20,'K',22-317 ##label MAE REFERENCE A90120 !$#authors Cardin, A.D.; Hirose, N.; Blankenship, D.T.; Jackson, R.L.; !1Harmony, J.A.K.; Sparrow, D.A.; Sparrow, J.T. !$#journal Biochem. Biophys. Res. Commun. (1986) 134:783-789 !$#title Binding of a high reactive heparin to human apolipoprotein !1E: identification of two heparin-binding domains. !$#cross-references MUID:86130564; PMID:3947350 !$#contents annotation; heparin binding sites REFERENCE I37181 !$#authors Wallis, S.C.; Rogne, S.; Gill, L.; Markham, A.; Edge, M.; !1Woods, D.; Williamson, R.; Humphries, S. !$#journal EMBO J. (1983) 2:2369-2373 !$#title The isolation of cDNA clones for human apolipoprotein E and !1the detection of apoE RNA in hepatic and extra-hepatic !1tissues. !$#cross-references MUID:84131952; PMID:6199196 !$#accession I37181 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 64-239 ##label RES !'##cross-references EMBL:X00199; NID:g28808; PIDN:CAA25017.1; !1PID:g929610 COMMENT The sequence of the most common variant E3 is shown. COMMENT There are at least nine alleles of the apo-E gene. The three !1common allelic variants are E2, E3, and E4. Over 90% of !1individuals with type III hyperlipoproteinemia have the E2/ !1E2 phenotype. COMMENT Apo-E occurs in all lipoprotein fractions in plasma. It !1constitutes 10-20% of very low density lipoproteins (VLDL) !1and 1-2% of high density lipoproteins (HDL). COMMENT Apo-E is synthesized with the sialic acid attached by !1O-glycosidic linkage and is subsequently desialated in !1plasma. The synthesis occurs in liver and to a minor extent !1in intestine. However, in contrast to other apolipoproteins, !1synthesis has been documented also in a wide variety of !1other tissues including kidney, adrenal gland, !1reticuloendothelial cells, and brain. GENETICS !$#gene GDB:APOE !'##cross-references GDB:119691; OMIM:107741 !$#map_position 19q13.2-19q13.2 !$#introns 15/1; 79/2 !$#note the first intron occurs before the initiator codon FUNCTION !$#description mediates binding, internalization, and catabolism of !1lipoprotein particles by serving as a ligand for the LDL(apo !1B/E) receptor and the specific apo-E receptor (chylomicron !1remnant) of hepatic tissues, fibroblasts and other !1peripheral cells CLASSIFICATION #superfamily apolipoprotein A-I KEYWORDS atherosclerosis; cholesterol; chylomicron; duplication; HDL; !1lipid binding; lipid transport; plasma; sialoglycoprotein; !1tandem repeat; VLDL FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-317 #product apolipoprotein E #status experimental #label !8MAT\ !$80-255 #region 22-residue repeats\ !$158-168 #region LDL receptor binding #status predicted\ !$162-165,229-236 #region heparin binding #status experimental SUMMARY #length 317 #molecular-weight 36154 #checksum 9493 SEQUENCE /// ENTRY LPRTE #type complete TITLE apolipoprotein E precursor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 25-Feb-1985 #sequence_revision 19-Jan-2001 #text_change 19-Jan-2001 ACCESSIONS A26189; A25576; A03094; I52081 REFERENCE A26189 !$#authors Fung, W.P.; Howlett, G.J.; Schreiber, G. !$#journal J. Biol. Chem. (1986) 261:13777-13783 !$#title Structure and expression of the rat apolipoprotein E gene. !$#cross-references MUID:87008617; PMID:3020048 !$#accession A26189 !'##molecule_type DNA !'##residues 1-312 ##label FUN !'##cross-references GB:J02582; NID:g202957; PIDN:AAA40755.1; !1PID:g202958 REFERENCE A25576 !$#authors Fukazawa, C.; Matsumoto, A.; Taylor, J.M. !$#journal Nucleic Acids Res. (1986) 14:9527-9528 !$#title Complete nucleotide sequence of the gene encoding the rat !1apolipoprotein E. !$#cross-references MUID:87091580; PMID:3797247 !$#accession A25576 !'##molecule_type DNA !'##residues 1-103,'T',105-205,'RWRRPA',212,214-312 ##label FUK !'##cross-references GB:X04979; NID:g55755; PIDN:CAA28650.1; PID:g295916 !'##note the authors translated the codon ACT for residue 104 as Ala REFERENCE A03094 !$#authors McLean, J.W.; Fukazawa, C.; Taylor, J.M. !$#journal J. Biol. Chem. (1983) 258:8993-9000 !$#title Rat apolipoprotein E mRNA. Cloning and sequencing of !1dougle-stranded cDNA. !$#cross-references MUID:83238546; PMID:6190813 !$#accession A03094 !'##molecule_type mRNA !'##residues 1-109,'T',111-140,'D',142-205,'RWRRPA',212,214-308,'WR', !1311-312 ##label MCL REFERENCE I52081 !$#authors Nomura, N.; Yamada, H.; Matsubara, N.; Horinouchi, S.; !1Beppu, T. !$#journal Appl. Microbiol. Biotechnol. (1995) 42:865-870 !$#title Secretion by Saccharomyces cerevisiae of rat apolipoprotein !1E as a fusion to Mucor rennin. !$#cross-references MUID:95226077; PMID:7766086 !$#accession I52081 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-109,'T',111-140,'D',142-308,'WR',311-312 ##label NOM !'##cross-references GB:S76779; NID:g913985; PIDN:AAC60703.1; !1PID:g913986 COMMENT The mature protein has no cysteine residues; however, in !1different allelic variants where cysteine residues replace !1arginine at positions 155 or 168, binding of apo-E to cell !1membrane receptors is decreased. The amino end of this !1protein is therefore thought to interact with the receptor. COMMENT The secondary structure of the carboxyl domain !1(approximately the last third of the sequence) is predicted !1to have three amphipathic helical regions. Such a structure, !1postulated for other apolipoproteins as well, may be !1responsible for the lipid-binding abilities of these !1proteins. GENETICS !$#gene rApoE CLASSIFICATION #superfamily apolipoprotein A-I KEYWORDS chylomicron; HDL; lipid binding; lipoprotein; VLDL FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-312 #product apolipoprotein E #status predicted #label !8MAT SUMMARY #length 312 #molecular-weight 35753 #checksum 142 SEQUENCE /// ENTRY LPHUA4 #type complete TITLE apolipoprotein A-IV precursor [validated] - human ALTERNATE_NAMES apoA-IV ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 08-Dec-2000 ACCESSIONS A94137; A94059; A24449; A29330; A26280; I37177; C54223; !1A61203; A26481; S02715 REFERENCE A94137 !$#authors Karathanasis, S.K.; Oettgen, P.; Haddad, I.A.; Antonarakis, !1S.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:8457-8461 !$#title Structure, evolution, and polymorphisms of the human !1apolipoprotein A4 gene (APOA4). !$#cross-references MUID:87041474; PMID:3095836 !$#accession A94137 !'##molecule_type DNA !'##residues 1-396 ##label KAR1 !'##cross-references GB:M14642; NID:g178760; PIDN:AAA51745.1; !1PID:g178761 REFERENCE A94059 !$#authors Karathanasis, S.K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:6374-6378 !$#title Apolipoprotein multigene family: tandem organization of !1human apolipoprotein AI, CIII, and AIV genes. !$#cross-references MUID:86016704; PMID:3931073 !$#accession A94059 !'##molecule_type mRNA !'##residues 135-378 ##label KAR2 !'##cross-references GB:M10373; NID:g563319; PIDN:AAB59516.1; !1PID:g563320 REFERENCE A24449 !$#authors Karathanasis, S.K.; Yunis, I. !$#journal Biochemistry (1986) 25:3962-3970 !$#title Structure, evolution, and tissue-specific synthesis of human !1apolipoprotein AIV. !$#cross-references MUID:86296629; PMID:3755616 !$#accession A24449 !'##molecule_type mRNA !'##residues 1-396 ##label KAR3 !'##cross-references GB:M13654; NID:g178758; PIDN:AAA51744.1; !1PID:g178759 REFERENCE A92475 !$#authors Gordon, J.I.; Bisgaier, C.L.; Sims, H.F.; Sachdev, O.P.; !1Glickman, R.M.; Strauss, A.W. !$#journal J. Biol. Chem. (1984) 259:468-474 !$#title Biosynthesis of human preapolipoprotein A-IV. !$#cross-references MUID:84161950; PMID:6706947 !$#contents annotation; signal sequence cleavage site REFERENCE A29330 !$#authors Elshourbagy, N.A.; Walker, D.W.; Paik, Y.K.; Boguski, M.S.; !1Freeman, M.; Gordon, J.I.; Taylor, J.M. !$#journal J. Biol. Chem. (1987) 262:7973-7981 !$#title Structure and expression of the human apolipoprotein A-IV !1gene. !$#cross-references MUID:87250378; PMID:3036793 !$#accession A29330 !'##molecule_type DNA !'##residues 1-157,'T',159,'Y',161-278,'R',280-326,'T',328-379,'H', !1381-396 ##label ELS !'##cross-references GB:J02758; NID:g178756; PIDN:AAA96731.1; !1PID:g178757 REFERENCE A26280 !$#authors Elshourbagy, N.A.; Walker, D.W.; Boguski, M.S.; Gordon, !1J.I.; Taylor, J.M. !$#journal J. Biol. Chem. (1986) 261:1998-2002 !$#title The nucleotide and derived amino acid sequence of human !1apolipoprotein A-IV mRNA and the close linkage of its gene !1to the genes of apolipoproteins A-I and C-III. !$#cross-references MUID:86111885; PMID:3080432 !$#accession A26280 !'##molecule_type mRNA !'##residues 21-157,'T',159,'Y',161-278,'R',280-326,'T',328-379,'H', !1381-396 ##label EL2 !'##cross-references GB:M14566; NID:g178778; PIDN:AAA51748.1; !1PID:g178779 REFERENCE I37177 !$#authors Yang, C.Y.; Gu, Z.W.; Chong, I.S.; Xiong, W.J.; Rosseneu, !1M.; Yang, H.X.; Lee, B.R.; Gotto, A.M. !$#journal Biochim. Biophys. Acta (1989) 1002:231-237 !$#title The primary structure of human apolipoprotein A-IV. !$#cross-references MUID:89194198; PMID:2930771 !$#accession I37177 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-157,'T',159,'Y',161-278,'R',280-396 ##label YAN1 !'##cross-references EMBL:X13629; NID:g28761; PIDN:CAA31955.1; !1PID:g28762 !'##note submitted to the EMBL Data Library, January 1989 REFERENCE A54223 !$#authors Kunitake, S.T.; Carilli, C.T.; Lau, K.; Protter, A.A.; !1Naya-Vigne, J.; Kane, J.P. !$#journal Biochemistry (1994) 33:1988-1993 !$#title Identification of proteins associated with apolipoprotein !1A-I-containing lipoproteins purified by selected-affinity !1immunosorption. !$#cross-references MUID:94162201; PMID:8117655 !$#accession C54223 !'##molecule_type protein !'##residues 'X',22,'X',24,'X',26-31,'X',33-34 ##label KUN REFERENCE A61203 !$#authors Tenkanen, H.; Lukka, M.; Jauhiainen, M.; Metso, J.; Baumann, !1M.; Peltonen, L.; Ehnholm, C. !$#journal Arterioscler. Thromb. (1991) 11:851-856 !$#title The mutation causing the common apolipoprotein A-IV !1polymorphism is a glutamine to histidine substitution of !1amino acid 360. !$#cross-references MUID:91291788; PMID:2065039 !$#accession A61203 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 378-379,'H',381-382 ##label TEN COMMENT ApoA-IV is a major lipoprotein of lymph chylomicrons. In !1human plasma, it is present unassociated with lipoproteins. COMMENT ApoA-IV is synthesized primarily in the intestine. GENETICS !$#gene GDB:APOA4 !'##cross-references GDB:119000; OMIM:107690 !$#map_position 11q23-11q23 !$#introns 17/1; 59/2 CLASSIFICATION #superfamily apolipoprotein A-I KEYWORDS chylomicron; HDL; intestine; lipid binding; lipid transport; !1lipoprotein; plasma; tandem repeat FEATURE !$1-20 #domain signal sequence #status experimental #label !8SIG\ !$21-396 #product apolipoprotein A-IV #status experimental !8#label MAT SUMMARY #length 396 #molecular-weight 45335 #checksum 5214 SEQUENCE /// ENTRY LPRTA4 #type complete TITLE apolipoprotein A-IV precursor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 22-Jun-1999 ACCESSIONS A03095; A25214; C24700 REFERENCE A03095 !$#authors Boguski, M.S.; Elshourbagy, N.; Taylor, J.M.; Gordon, J.I. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:5021-5025 !$#title Rat apolipoprotein A-IV contains 13 tandem repetitions of a !122-amino acid segment with amphipathic helical potential. !$#cross-references MUID:84298074; PMID:6591177 !$#accession A03095 !'##molecule_type mRNA !'##residues 1-391 ##label BOG !'##cross-references GB:M00002; GB:K02421; NID:g202949; PIDN:AAA85909.1; !1PID:g202950 REFERENCE A25214 !$#authors Boguski, M.S.; Birkenmeier, E.H.; Elshourbagy, N.A.; Taylor, !1J.M.; Gordon, J.I. !$#journal J. Biol. Chem. (1986) 261:6398-6407 !$#title Evolution of the apolipoproteins. Structure of the rat !1APO-A-IV gene and its relationship to the human genes for !1APO-A-I, C-III, and E. !$#cross-references MUID:86196059; PMID:3009456 !$#accession A25214 !'##molecule_type protein !'##residues 1-252,'Q',254-391 ##label BO2 REFERENCE A92558 !$#authors Haddad, I.A.; Ordovas, J.M.; Fitzpatrick, T.; Karathanasis, !1S.K. !$#journal J. Biol. Chem. (1986) 261:13268-13277 !$#title Linkage, evolution, and expression of the rat apolipoprotein !1A-I, C-III, and A-IV genes. !$#cross-references MUID:87008540; PMID:3020028 !$#accession C24700 !'##molecule_type DNA !'##residues 1-252,'Q',254-391 ##label HAD !'##cross-references GB:J02588; NID:g202937; PIDN:AAA40747.1; !1PID:g202941 COMMENT This apoprotein is a major component of HDL and chylomicrons !1but, unlike other apoproteins, approximately 50% of the !1plasma apoA-IV is not associated with the classical !1lipoproteins. COMMENT Nine of the thirteen 22-amino acid tandem repeats (each !122-mer is actually a tandem array of two, A and B, related !111-mers) occurring in this sequence are predicted to be !1highly alpha-helical, and many of these helices are !1amphipathic. They may therefore serve as lipid-binding !1domains with lecithin:cholesterol acyltransferase (LCAT) !1activating abilities. CLASSIFICATION #superfamily apolipoprotein A-I KEYWORDS chylomicron; duplication; HDL; lipid transport; plasma; !1tandem repeat FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-391 #product apolipoprotein A-IV #status predicted #label !8MAT\ !$33-330 #region 22-residue repeats SUMMARY #length 391 #molecular-weight 44465 #checksum 2943 SEQUENCE /// ENTRY LPHUA2 #type complete TITLE apolipoprotein A-II precursor [validated] - human ALTERNATE_NAMES preproapoA-II ORGANISM #formal_name Homo sapiens #common_name man DATE 24-Apr-1984 #sequence_revision 30-Jun-1987 #text_change 08-Dec-2000 ACCESSIONS A93586; A93572; C93519; A92467; A92117; A19913; B54223; !1I39437; A03096 REFERENCE A93586 !$#authors Knott, T.J.; Wallis, S.C.; Robertson, M.E.; Priestley, L.M.; !1Urdea, M.; Rall, L.B.; Scott, J. !$#journal Nucleic Acids Res. (1985) 13:6387-6398 !$#title The human apolipoprotein AII gene: structural organization !1and sites of expression. !$#cross-references MUID:86016095; PMID:2995928 !$#accession A93586 !'##molecule_type DNA !'##residues 1-100 ##label KNO !'##cross-references GB:X02905; NID:g28757; PIDN:CAA26665.1; PID:g296634 REFERENCE A93572 !$#authors Lackner, K.J.; Law, S.W.; Brewer Jr., H.B. !$#journal Nucleic Acids Res. (1985) 13:4597-4608 !$#title The human apolipoprotein A-II gene: complete nucleic acid !1sequence and genomic organization. !$#cross-references MUID:85242123; PMID:2989800 !$#accession A93572 !'##molecule_type DNA !'##residues 1-100 ##label LAC !'##cross-references GB:X02619; NID:g28751; PIDN:CAA26474.1; PID:g296633 REFERENCE A93519 !$#authors Sharpe, C.R.; Sidoli, A.; Shelley, C.S.; Lucero, M.A.; !1Shoulders, C.C.; Baralle, F.E. !$#journal Nucleic Acids Res. (1984) 12:3917-3932 !$#title Human apolipoproteins AI, AII, CII and CIII. cDNA sequences !1and mRNA abundance. !$#cross-references MUID:84221405; PMID:6328445 !$#accession C93519 !'##molecule_type mRNA !'##residues 1-100 ##label SHA !'##cross-references GB:X00955; GB:K01686; GB:K02216; GB:X00569; !1GB:X00927; NID:g28747; PIDN:CAA25467.1; PID:g28748 REFERENCE A92467 !$#authors Gordon, J.I.; Sims, H.F.; Edelstein, C.; Scanu, A.M.; !1Strauss, A.W. !$#journal J. Biol. Chem. (1984) 259:15556-15563 !$#title Human proapolipoprotein A-II is cleaved following secretion !1from hep G2 cells by a thiol protease. !$#cross-references MUID:85080054; PMID:6096378 !$#contents cleavage of propeptide !$#accession A92467 !'##molecule_type protein !'##residues 19-44 ##label GOR REFERENCE A92117 !$#authors Lux, S.E.; John, K.M.; Ronan, R.; Brewer Jr., H.B. !$#journal J. Biol. Chem. (1972) 247:7519-7527 !$#title Isolation and characterization of the tryptic and cyanogen !1bromide peptides of apoLp-Gln-II (ApoA-II), a plasma high !1density apolipoprotein. !$#cross-references MUID:73048503; PMID:4344225 !$#accession A92117 !'##molecule_type protein !'##residues 24-59,'Q',61-100 ##label LUX REFERENCE A19913 !$#authors Stoffel, W.; Kruger, E.; Deutzmann, R. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1983) 364:227-237 !$#title Cell-free translation of human liver apolipoprotein AI and !1AII mRNA processing of primary translation products. !$#cross-references MUID:83236195; PMID:6407957 !$#accession A19913 !'##molecule_type protein !'##residues 1-6,'X',8-11,'XX',14,'X',16,'XX',19-21,'XQX',25-26,'X', !128-29 ##label STO REFERENCE A54223 !$#authors Kunitake, S.T.; Carilli, C.T.; Lau, K.; Protter, A.A.; !1Naya-Vigne, J.; Kane, J.P. !$#journal Biochemistry (1994) 33:1988-1993 !$#title Identification of proteins associated with apolipoprotein !1A-I-containing lipoproteins purified by selected-affinity !1immunosorption. !$#cross-references MUID:94162201; PMID:8117655 !$#accession B54223 !'##molecule_type protein !'##residues 52-60 ##label KUN REFERENCE I39437 !$#authors Chan, L.; Moore, M.N.; Tsao, Y.K. !$#journal Meth. Enzymol. (1986) 128:745-752 !$#title Molecular cloning and sequence analysis of human !1apolipoprotein A-II cDNA. !$#cross-references MUID:86256573; PMID:3088392 !$#accession I39437 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-100 ##label RES !'##cross-references GB:M29882; NID:g178423; PIDN:AAA51701.1; !1PID:g178424 COMMENT ApoA-II makes up about 20% of the protein fraction of high !1density lipoprotein (HDL). COMMENT The precursor is synthesized in the liver and intestine. In !1the hepatoma cells, the cleavage of propeptide was found to !1occur extracellularly. GENETICS !$#gene GDB:APOA2 !'##cross-references GDB:119685; OMIM:107670 !$#map_position 1q21-1q23 !$#introns 18/1; 62/2 CLASSIFICATION #superfamily apolipoprotein A-I KEYWORDS HDL; homodimer; intestine; lipid transport; liver; plasma; !1pyroglutamic acid FEATURE !$1-18 #domain signal sequence #status experimental #label !8SIG\ !$19-23 #domain propeptide #status experimental #label APT\ !$24-100 #product apolipoprotein A-II #status experimental !8#label MPT\ !$24 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$29 #disulfide_bonds interchain (partial) #status !8experimental\ !$29 #disulfide_bonds interchain (partial) (to !8apolipoprotein D 136) #status experimental SUMMARY #length 100 #molecular-weight 11175 #checksum 588 SEQUENCE /// ENTRY S29564 #type complete TITLE apolipoprotein A-II precursor - crab-eating macaque ORGANISM #formal_name Macaca fascicularis #common_name crab-eating macaque DATE 06-Jan-1995 #sequence_revision 19-Oct-1995 #text_change 22-Jun-1999 ACCESSIONS S30197; B26627; S29564 REFERENCE S30197 !$#authors Osada, J.; Garces, C.; Sastre, J.; Schaefer, E.J.; Ordovas, !1J.M. !$#journal Biochim. Biophys. Acta (1993) 1172:340-342 !$#title Molecular cloning and sequence of the cynomolgus monkey !1apolipoprotein A-II gene. !$#cross-references MUID:93192331; PMID:8448213 !$#accession S30197 !'##molecule_type DNA !'##residues 1-100 ##label OS2 !'##cross-references EMBL:X68360; NID:g38048; PIDN:CAA48420.1; !1PID:g38049 REFERENCE A26627 !$#authors Herbert, P.N.; Bausserman, L.L.; Lynch, K.M.; Saritelli, !1A.L.; Kantor, M.A.; Nicolosi, R.J.; Shulman, R.S. !$#journal Biochemistry (1987) 26:1457-1463 !$#title Homologues of the human C and A apolipoproteins in the !1Macaca fascicularis (cynomolgus) monkey. !$#cross-references MUID:87185451; PMID:3105581 !$#accession B26627 !'##molecule_type protein !'##residues 'Z',25,'Q',27-48 ##label HER COMMENT ApoA-II makes up about 20% of the protein fraction of high !1density lipoprotein (HDL). COMMENT The precursor is synthesized in the liver and intestine. In !1the hepatoma cells, the cleavage of propeptide occurs !1extracellularly. GENETICS !$#introns 18/1; 62/2 CLASSIFICATION #superfamily apolipoprotein A-I KEYWORDS HDL; intestine; lipid binding; lipid transport; lipoprotein; !1liver; plasma; pyroglutamic acid FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-23 #domain propeptide #status predicted #label APT\ !$24-100 #product apolipoprotein A-II #status experimental !8#label MAT\ !$24 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental SUMMARY #length 100 #molecular-weight 11214 #checksum 1453 SEQUENCE /// ENTRY LPMQA2 #type complete TITLE apolipoprotein A-II - rhesus macaque ORGANISM #formal_name Macaca mulatta #common_name rhesus macaque DATE 23-Oct-1981 #sequence_revision 23-Oct-1981 #text_change 05-Aug-1994 ACCESSIONS A03097 REFERENCE A03097 !$#authors Edelstein, C.; Noyes, C.; Keim, P.; Heinrikson, R.L.; !1Fellows, R.E.; Scanu, A.M. !$#journal Biochemistry (1976) 15:1262-1268 !$#title Covalent structure of apolipoprotein A-II from Macaca !1mulatta serum high-density lipoproteins. !$#cross-references MUID:76136410; PMID:814923 !$#accession A03097 !'##molecule_type protein !'##residues 1-77 ##label EDE CLASSIFICATION #superfamily apolipoprotein A-I KEYWORDS HDL; pyroglutamic acid FEATURE !$1 #modified_site pyrrolidone carboxylic acid (Gln) !8#status experimental SUMMARY #length 77 #molecular-weight 8747 #checksum 2389 SEQUENCE /// ENTRY LPHUC1 #type complete TITLE apolipoprotein C-I precursor [validated] - human ALTERNATE_NAMES apo-CI ORGANISM #formal_name Homo sapiens #common_name man DATE 24-Apr-1984 #sequence_revision 04-Dec-1986 #text_change 08-Dec-2000 ACCESSIONS A28057; A93518; A92170; A92159; I52225; I54250; A03098 REFERENCE A28057 !$#authors Lauer, S.J.; Walker, D.; Elshourbagy, N.A.; Reardon, C.A.; !1Levy-Wilson, B.; Taylor, J.M. !$#journal J. Biol. Chem. (1988) 263:7277-7286 !$#title Two copies of the human apolipoprotein C-I gene are linked !1closely to the apolipoprotein E gene. !$#cross-references MUID:88213410; PMID:2835369 !$#accession A28057 !'##molecule_type DNA !'##residues 1-83 ##label LAU !'##cross-references GB:M20902; GB:J03217; NID:g178830; PIDN:AAA88018.1; !1PID:g178831 REFERENCE A93518 !$#authors Knott, T.J.; Robertson, M.E.; Priestley, L.M.; Urdea, M.; !1Wallis, S.; Scott, J. !$#journal Nucleic Acids Res. (1984) 12:3909-3915 !$#title Characterisation of mRNAs encoding the precursor for human !1apolipoprotein C1. !$#cross-references MUID:84221404; PMID:6328444 !$#accession A93518 !'##molecule_type mRNA !'##residues 1-83 ##label KNO !'##cross-references GB:X00570; NID:g28802; PIDN:CAA25235.1; PID:g757914 REFERENCE A92170 !$#authors Shulman, R.S.; Herbert, P.N.; Wehrly, K.; Fredrickson, D.S. !$#journal J. Biol. Chem. (1975) 250:182-190 !$#title The complete amino acid sequence of C-I (ApoLp-Ser), an !1apolipoprotein from human very low density lipoproteins. !$#cross-references MUID:75189350; PMID:166984 !$#accession A92170 !'##molecule_type protein !'##residues 27-83 ##label SHU REFERENCE A92159 !$#authors Jackson, R.L.; Sparrow, J.T.; Baker, H.N.; Morrisett, J.D.; !1Taunton, O.D.; Gotto Jr., A.M. !$#journal J. Biol. Chem. (1974) 249:5308-5313 !$#title The primary structure of apolipoprotein-serine. !$#cross-references MUID:74309060; PMID:4369340 !$#accession A92159 !'##molecule_type protein !'##residues 27-83 ##label JAC REFERENCE I52225 !$#authors Smit, M.; van der Kooij-Meijs, E.; Woudt, L.P.; Havekes, !1L.M.; Frants, R.R. !$#journal Biochem. Biophys. Res. Commun. (1988) 152:1282-1288 !$#title Exact localization of the familial dysbetalipoproteinemia !1associated HpaI restriction site in the promoter region of !1the APOC1 gene. !$#cross-references MUID:88240344; PMID:2897845 !$#accession I52225 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-19 ##label RES !'##cross-references GB:M20843; NID:g178837; PIDN:AAA51763.1; !1PID:g553191 REFERENCE I54250 !$#authors Tata, F.; Henry, I.; Markham, A.F.; Wallis, S.C.; Weil, D.; !1Grzeschik, K.H.; Junien, C.; Williamson, R.; Humphries, S.E. !$#journal Hum. Genet. (1985) 69:345-349 !$#title Isolation and characterisation of a cDNA clone for human !1apolipoprotein CI and assignment of the gene to chromosome !119. !$#cross-references MUID:85181206; PMID:2985493 !$#accession I54250 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 15-83 ##label RE2 !'##cross-references GB:M27359; NID:g178833; PIDN:AAA51762.1; !1PID:g178834 COMMENT Apo-CI makes up about 10% of the protein of the VLDL (very !1low density lipoprotein) and 2% of that of HDL (high density !1lipoprotein). COMMENT Apo-CI is synthesized mainly in liver and to a minor degree !1in intestine. GENETICS !$#gene GDB:APOC1 !'##cross-references GDB:119687; OMIM:107710 !$#map_position 19q13.2-19q13.2 CLASSIFICATION #superfamily apolipoprotein A-I KEYWORDS intestine; lipid transport; liver; plasma; VLDL FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-83 #product apolipoprotein C-I #status experimental !8#label MPT SUMMARY #length 83 #molecular-weight 9332 #checksum 1556 SEQUENCE /// ENTRY A42006 #type complete TITLE apolipoprotein C-I precursor - baboon ALTERNATE_NAMES apo-CI ORGANISM #formal_name Papio sp. #common_name baboon DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 13-Jun-1997 ACCESSIONS A42006; B42006 REFERENCE A42006 !$#authors Pastorcic, M.; Birnbaum, S.; Hixson, J.E. !$#journal Genomics (1992) 13:368-374 !$#title Baboon apolipoprotein C-I: cDNA and gene structure and !1evolution. !$#cross-references MUID:92307671; PMID:1612596 !$#accession A42006 !'##molecule_type DNA !'##residues 1-83 ##label PAS1 !$#accession B42006 !'##molecule_type mRNA !'##residues 1-83 ##label PAS2 !'##cross-references GB:S38664 GENETICS !$#introns 20/1; 65/2 CLASSIFICATION #superfamily apolipoprotein A-I KEYWORDS intestine; lipid transport; liver; plasma; VLDL FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-83 #product apolipoprotein C-I #status predicted #label !8MPT SUMMARY #length 83 #molecular-weight 9418 #checksum 2377 SEQUENCE /// ENTRY B60940 #type complete TITLE apolipoprotein C-I precursor - dog ALTERNATE_NAMES apo-CI ORGANISM #formal_name Canis lupus familiaris #common_name dog DATE 31-Dec-1993 #sequence_revision 09-Sep-1994 #text_change 09-Sep-1994 ACCESSIONS B60940 REFERENCE A60940 !$#authors Luo, C.C.; Li, W.H.; Chan, L. !$#journal J. Lipid Res. (1989) 30:1735-1746 !$#title Structure and expression of dog apolipoprotein A-I, E, and !1C-I mRNAs: implications for the evolution and functional !1constraints of apolipoprotein structure. !$#cross-references MUID:90132271; PMID:2515239 !$#accession B60940 !'##molecule_type mRNA !'##residues 1-88 ##label LUO !'##note authors translated the codon GGT for residue 20 as Val, and TTT !1for residue 34 as Leu COMMENT Apo-CI makes up about 10% of the protein of the VLDL (very !1low density lipoprotein) and 2% of that of HDL (high density !1lipoprotein). COMMENT Apo-CI is synthesized mainly in liver and to a minor degree !1in intestine. CLASSIFICATION #superfamily apolipoprotein A-I KEYWORDS intestine; lipid transport; liver; plasma; VLDL FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-88 #product apolipoprotein C-I #status predicted #label !8MAT SUMMARY #length 88 #molecular-weight 9741 #checksum 9286 SEQUENCE /// ENTRY LPHUC2 #type complete TITLE apolipoprotein C-II precursor [validated] - human ALTERNATE_NAMES ApoC-II; preapolipoprotein C-II; preproapolipoprotein C-II ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Apr-1979 #sequence_revision 27-Nov-1985 #text_change 08-Dec-2000 ACCESSIONS A24238; A27408; A26643; A94008; A26180; A26178; A92471; !1A93809; I39471; A03099 REFERENCE A24238 !$#authors Wei, C.F.; Tsao, Y.K.; Robberson, D.L.; Gotto Jr., A.M.; !1Brown, K.; Chan, L. !$#journal J. Biol. Chem. (1985) 260:15211-15221 !$#title The structure of the human apolipoprotein C-II gene. !1Electron microscopic analysis of RNA:DNA hybrids, complete !1nucleotide sequence, and identification of 5' homologous !1sequences among apolipoprotein genes. !$#cross-references MUID:86059374; PMID:2415514 !$#accession A24238 !'##molecule_type DNA !'##residues 1-101 ##label WEI !'##cross-references GB:M10612; GB:K00946; GB:K02045; GB:K02092; !1GB:X00568; NID:g178835; PIDN:AAB59380.1; PID:g178836 REFERENCE A27408 !$#authors Das, H.K.; Jackson, C.L.; Miller, D.A.; Leff, T.; Breslow, !1J.L. !$#journal J. Biol. Chem. (1987) 262:4787-4793 !$#title The human apolipoprotein C-II gene sequence contains a novel !1chromosome 19-specific minisatellite in its third intron. !$#cross-references MUID:87165892; PMID:3558370 !$#accession A27408 !'##molecule_type DNA !'##residues 1-101 ##label DAS !'##cross-references GB:J02698; NID:g178824; PIDN:AAA98743.1; !1PID:g178825 REFERENCE A26643 !$#authors Fojo, S.S.; Law, S.W.; Brewer Jr., H.B. !$#journal FEBS Lett. (1987) 213:221-226 !$#title The human preproapolipoprotein C-II gene. Complete nucleic !1acid sequence and genomic organization. !$#cross-references MUID:87162474; PMID:3030808 !$#accession A26643 !'##molecule_type DNA !'##residues 1-101 ##label FO2 !'##cross-references GB:X05151; NID:g28792; PIDN:CAA28798.1; PID:g296636 REFERENCE A94008 !$#authors Fojo, S.S.; Law, S.W.; Brewer Jr., H.B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:6354-6357 !$#title Human apolipoprotein C-II: complete nucleic acid sequence of !1preapolipoprotein C-II. !$#cross-references MUID:85038515; PMID:6593704 !$#accession A94008 !'##molecule_type mRNA !'##residues 1-101 ##label FOJ !'##cross-references GB:M10612; NID:g178835; PIDN:AAB59380.1; !1PID:g178836 REFERENCE A26180 !$#authors Jackson, C.L.; Bruns, G.A.P.; Breslow, J.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:2945-2949 !$#title Isolation and sequence of a human apolipoprotein C-II cDNA !1clone and its use to isolate and map to human chromosome 19 !1the gene for apolipoprotein C-II. !$#cross-references MUID:84221883; PMID:6328478 !$#accession A26180 !'##molecule_type mRNA !'##residues 11-101 ##label JA2 !'##cross-references GB:M10612 REFERENCE A26178 !$#authors Myklebost, O.; Williamson, B.; Markham, A.F.; Myklebost, !1S.R.; Rogers, J.; Woods, D.E.; Humphries, S.E. !$#journal J. Biol. Chem. (1984) 259:4401-4404 !$#title The isolation and characterization of cDNA clones for human !1apolipoprotein C-II. !$#cross-references MUID:84162145; PMID:6546757 !$#accession A26178 !'##molecule_type mRNA !'##residues 'V',6-101 ##label MYK !'##cross-references GB:M10612 REFERENCE A92471 !$#authors Hospattankar, A.V.; Fairwell, T.; Ronan, R.; Brewer Jr., !1H.B. !$#journal J. Biol. Chem. (1984) 259:318-322 !$#title Amino acid sequence of human plasma apolipoprotein C-II from !1normal and hyperlipoproteinemic subjects. !$#cross-references MUID:84161925; PMID:6706938 !$#accession A92471 !'##molecule_type protein !'##residues 23-101 ##label HOS REFERENCE A93809 !$#authors Jackson, R.L.; Baker, H.N.; Gilliam, E.B.; Gotto Jr., A.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1977) 74:1942-1945 !$#title Primary structure of very low density apolipoprotein C-II of !1human plasma. !$#cross-references MUID:77193958; PMID:194244 !$#accession A93809 !'##molecule_type protein !'##residues 23,'E',25-38,'E',40-42,'W',44-47,'Q',50-101 ##label JAC1 REFERENCE I39471 !$#authors Jackson, C.L.; Bruns, G.A.; Breslow, J.L. !$#journal Meth. Enzymol. (1986) 128:788-800 !$#title Isolation of cDNA and genomic clones for apolipoprotein !1C-II. !$#cross-references MUID:86256576; PMID:3014272 !$#accession I39471 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 11-101 ##label JAC2 !'##cross-references GB:M29844; NID:g178740; PIDN:AAA51743.1; !1PID:g178741 COMMENT This protein is a component of the very low density !1lipoprotein (VLDL) fraction in plasma. The association of !1apoC-II with plasma chylomicrons, VLDL, and HDL is !1reversible, a function of the secretion and catabolism of !1triglyceride-rich lipoproteins, and changes rapidly. GENETICS !$#gene GDB:APOC2 !'##cross-references GDB:119689; OMIM:207750 !$#map_position 19q13.2-19q13.2 !$#introns 19/1; 72/2 FUNCTION !$#description activating cofactor for several triacylglycerol lipases CLASSIFICATION #superfamily apolipoprotein A-I KEYWORDS chylomicron; lipid binding; lipid metabolism; lipoprotein; !1plasma; VLDL FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-28 #domain propeptide #status experimental #label PRO\ !$29-101 #product apolipoprotein C-II #status experimental !8#label MAT\ !$65-73 #region lipid binding #status predicted\ !$77-100 #region lipoprotein lipase cofactor #status predicted SUMMARY #length 101 #molecular-weight 11284 #checksum 4525 SEQUENCE /// ENTRY LPHUC3 #type complete TITLE apolipoprotein C-III precursor [validated] - human ALTERNATE_NAMES preapoC-III ORGANISM #formal_name Homo sapiens #common_name man DATE 24-Apr-1984 #sequence_revision 27-Nov-1985 #text_change 08-Dec-2000 ACCESSIONS A90950; A90948; D93519; A92158; A23627; D54223; I56331; !1I73337; I37176; I37235; A03100 REFERENCE A90950 !$#authors Protter, A.A.; Levy-Wilson, B.; Miller, J.; Bencen, G.; !1White, T.; Seilhamer, J.J. !$#journal DNA (1984) 3:449-456 !$#title Isolation and sequence analysis of the human apolipoprotein !1CIII gene and the intergenic region between the Apo AI and !1Apo CIII genes. !$#cross-references MUID:85076175; PMID:6439535 !$#accession A90950 !'##molecule_type DNA !'##residues 1-99 ##label PRO !'##cross-references GB:X01392; NID:g28725; PIDN:CAA25648.1; PID:g296632 REFERENCE A90948 !$#authors Levy-Wilson, B.; Appleby, V.; Protter, A.; Auperin, D.; !1Seilhamer, J.J. !$#journal DNA (1984) 3:359-364 !$#title Isolation and DNA sequence of full-length cDNA for human !1preapolipoprotein CIII. !$#cross-references MUID:85076166; PMID:6548954 !$#accession A90948 !'##molecule_type mRNA !'##residues 1-99 ##label LEV !'##cross-references GB:X01388; NID:g28727; PIDN:CAA25644.1; PID:g28728 REFERENCE A93519 !$#authors Sharpe, C.R.; Sidoli, A.; Shelley, C.S.; Lucero, M.A.; !1Shoulders, C.C.; Baralle, F.E. !$#journal Nucleic Acids Res. (1984) 12:3917-3932 !$#title Human apolipoproteins AI, AII, CII and CIII. cDNA sequences !1and mRNA abundance. !$#cross-references MUID:84221405; PMID:6328445 !$#accession D93519 !'##molecule_type mRNA !'##residues 1-99 ##label SHA !'##cross-references GB:X00567; NID:g28799; PIDN:CAA25233.1; PID:g757913 REFERENCE A92158 !$#authors Brewer Jr., H.B.; Shulman, R.; Herbert, P.; Ronan, R.; !1Wehrly, K. !$#journal J. Biol. Chem. (1974) 249:4975-4984 !$#title The complete amino acid sequence of alanine apolipoprotein !1(apoC-III), an apolipoprotein from human plasma very low !1density lipoproteins. !$#cross-references MUID:74288207; PMID:4846755 !$#accession A92158 !'##molecule_type protein !'##residues 21-51,'SQ',54-56,'A',58,'Q',60-99 ##label BRE REFERENCE A23627 !$#authors Hospattankar, A.V.; Brewer Jr., H.B.; Ronan, R.; Fairwell, !1T. !$#journal FEBS Lett. (1986) 197:67-73 !$#title Amino acid sequence of human plasma apolipoprotein C-III !1from normalipidemic subjects. !$#cross-references MUID:86136604; PMID:3949020 !$#accession A23627 !'##molecule_type protein !'##residues 21-99 ##label HOS REFERENCE A54223 !$#authors Kunitake, S.T.; Carilli, C.T.; Lau, K.; Protter, A.A.; !1Naya-Vigne, J.; Kane, J.P. !$#journal Biochemistry (1994) 33:1988-1993 !$#title Identification of proteins associated with apolipoprotein !1A-I-containing lipoproteins purified by selected-affinity !1immunosorption. !$#cross-references MUID:94162201; PMID:8117655 !$#accession D54223 !'##molecule_type protein !'##residues 21-28,'XX',31-34 ##label KUN REFERENCE I56331 !$#authors Karathanasis, S.K.; Zannis, V.I.; Breslow, J.L. !$#journal J. Lipid Res. (1985) 26:451-456 !$#title Isolation and characterization of cDNA clones corresponding !1to two different human apoC-III alleles. !$#cross-references MUID:85236022; PMID:2989400 !$#accession I56331 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-99 ##label RES !'##cross-references GB:M28613; NID:g178826; PIDN:AAA51760.1; !1PID:g178827 !$#accession I73337 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-99 ##label RE3 !'##cross-references GB:M28614; NID:g178828; PIDN:AAA51761.1; !1PID:g178829 REFERENCE I37176 !$#authors Shelley, C.S.; Sharpe, C.R.; Baralle, F.E.; Shoulders, C.C. !$#journal J. Mol. Biol. (1985) 186:43-51 !$#title Comparison of the human apolipoprotein genes. Apo AII !1presents a unique functional intron-exon junction. !$#cross-references MUID:86089113; PMID:3935800 !$#accession I37176 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-99 ##label RE2 !'##cross-references EMBL:X03120; NID:g28731; PIDN:CAA26895.1; !1PID:g671881 REFERENCE I37235 !$#authors Karathanasis, S.K.; McPherson, J.; Zannis, V.I.; Breslow, !1J.L. !$#journal Nature (1983) 304:371-373 !$#title Linkage of human apolipoproteins A-I and C-III genes. !$#cross-references MUID:83271478; PMID:6308458 !$#accession I37235 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 78-99 ##label RE4 !'##cross-references EMBL:V01513; NID:g29959; PIDN:CAA24757.1; !1PID:g29960 COMMENT One molecule of apoC-III binds one molecule each of !1galactose and galactosamine and 0, 1, or 2 molecules of !1sialic acid. COMMENT ApoC-III constitutes 50% of the protein fraction of VLDL !1(very low density lipoprotein) and 2% of that of HDL (high !1density lipoprotein). COMMENT In vitro, apoC-III inhibits lipoprotein lipase and hepatic !1lipase and decreases the uptake of lymph chylomicrons by !1hepatic cells. This suggests that apoC-III delays catabolism !1of triglyceride-rich particles. COMMENT ApoC-III is synthesized in liver and to a lesser degree in !1intestine. GENETICS !$#gene GDB:APOC3 !'##cross-references GDB:119001; OMIM:107720 !$#map_position 11q23.1-11q23.2 !$#introns 19/1; 60/2 CLASSIFICATION #superfamily apolipoprotein A-I KEYWORDS chylomicron; glycoprotein; intestine; lipid metabolism; !1liver; plasma; VLDL FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-99 #product apolipoprotein C-III #status experimental !8#label MAT\ !$68-99 #region lipid binding\ !$94 #binding_site carbohydrate (Thr) (covalent) #status !8experimental SUMMARY #length 99 #molecular-weight 10852 #checksum 4659 SEQUENCE /// ENTRY S29566 #type complete TITLE apolipoprotein C-III precursor - crab-eating macaque ORGANISM #formal_name Macaca fascicularis #common_name crab-eating macaque DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S30196; F26627; S29566 REFERENCE S30195 !$#authors Osada, J.; Pocovi, M.; Nicolosi, R.J.; Schaefer, E.J.; !1Ordovas, J.M. !$#journal Biochim. Biophys. Acta (1993) 1172:335-339 !$#title Nucleotide sequences of the Macaca fascicularis !1apolipoprotein C-III and A-IV genes. !$#cross-references MUID:93192330; PMID:8448212 !$#accession S30196 !'##status preliminary !'##molecule_type DNA !'##residues 1-99 ##label OSA !'##cross-references EMBL:X68359; NID:g38052; PIDN:CAA48419.1; !1PID:g38053 REFERENCE A26627 !$#authors Herbert, P.N.; Bausserman, L.L.; Lynch, K.M.; Saritelli, !1A.L.; Kantor, M.A.; Nicolosi, R.J.; Shulman, R.S. !$#journal Biochemistry (1987) 26:1457-1463 !$#title Homologues of the human C and A apolipoproteins in the !1Macaca fascicularis (cynomolgus) monkey. !$#cross-references MUID:87185451; PMID:3105581 !$#accession F26627 !'##molecule_type protein !'##residues 21-36 ##label HER COMMENT One molecule of apoC-III binds one molecule each of !1galactose and galactosamine and 0, 1, or 2 molecules of !1sialic acid. COMMENT ApoC-III constitutes 50% of the protein fraction of VLDL !1(very low density lipoprotein) and 2% of that of HDL (high !1density lipoprotein). COMMENT In vitro, apoC-III inhibits lipoprotein lipase and hepatic !1lipase and decreases the uptake of lymph chylomicrons by !1hepatic cells. This suggests that apoC-III delays catabolism !1of triglyceride-rich particles. COMMENT ApoC-III is synthesized in liver and to a lesser degree in !1intestine. GENETICS !$#introns 19/1; 60/2 CLASSIFICATION #superfamily apolipoprotein A-I KEYWORDS chylomicron; glycoprotein; intestine; lipid binding; lipid !1metabolism; lipoprotein; liver; plasma; VLDL FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-99 #product apolipoprotein C-III #status experimental !8#label MAT\ !$68-99 #region lipid binding\ !$94 #binding_site carbohydrate (Thr) (covalent) #status !8predicted SUMMARY #length 99 #molecular-weight 10747 #checksum 3709 SEQUENCE /// ENTRY A41386 #type complete TITLE clusterin precursor [validated] - human ALTERNATE_NAMES apolipoprotein J; complement cytolysis inhibitor SP-40; complement-associated protein SP-40,40; lipoprotein-associated protein NA2; serum protein SP40,40; sulfated glycoprotein 2; TRPM-2/clusterin protein CONTAINS clusterin alpha chain; clusterin beta chain ORGANISM #formal_name Homo sapiens #common_name man DATE 03-Apr-1992 #sequence_revision 17-Nov-1995 #text_change 08-Dec-2000 ACCESSIONS S43646; S04662; A41386; A35833; S34056; A53177; A37816; !1B37816; PL0136; PL0135; S09339; S07433; E54223; F54223; !1I59206; I63132 REFERENCE S43646 !$#authors Wong, P.; Taillefer, D.; Lakins, J.; Pineault, J.; Chader, !1G.; Tenniswood, M. !$#journal Eur. J. Biochem. (1994) 221:917-925 !$#title Molecular characterization of human TRPM-2/clusterin, a gene !1associated with sperm maturation, apoptosis and !1neurodegeneration. !$#cross-references MUID:94237156; PMID:8181474 !$#accession S43646 !'##molecule_type DNA !'##residues 1-449 ##label WON !'##cross-references GB:M64722; NID:g339972; PIDN:AAB06508.1; !1PID:g339973 REFERENCE S04662 !$#authors Kirszbaum, L.; Sharpe, J.A.; Murphy, B.; d'Apice, A.J.F.; !1Classon, B.; Hudson, P.; Walker, I.D. !$#journal EMBO J. (1989) 8:711-718 !$#title Molecular cloning and characterization of the novel, human !1complement-associated protein, SP-40,40: a link between the !1complement and reproductive systems. !$#cross-references MUID:89251601; PMID:2721499 !$#accession S04662 !'##molecule_type mRNA !'##residues 1-449 ##label KIR !'##cross-references EMBL:X14723; NID:g30250; PIDN:CAA32847.1; !1PID:g30251 !'##note parts of this sequence, including the amino end of the mature !1protein, were confirmed by protein sequencing REFERENCE A41386 !$#authors Jenne, D.E.; Tschopp, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:7123-7127 !$#title Molecular structure and functional characterization of a !1human complement cytolysis inhibitor found in blood and !1seminal plasma: identity to sulfated glycoprotein 2, a !1constituent of rat testis fluid. !$#cross-references MUID:89386692; PMID:2780565 !$#accession A41386 !'##molecule_type mRNA !'##residues 2-449 ##label JEN !'##cross-references GB:M25915; NID:g180619; PIDN:AAA35692.1; !1PID:g180620 REFERENCE A35833 !$#authors de Silva, H.V.; Harmony, J.A.K.; Stuart, W.D.; Gil, C.M.; !1Robbins, J. !$#journal Biochemistry (1990) 29:5380-5389 !$#title Apolipoprotein J: structure and tissue distribution. !$#cross-references MUID:90344779; PMID:1974459 !$#accession A35833 !'##molecule_type mRNA !'##residues 34-449 ##label DES !'##cross-references GB:J02908; NID:g178854; PIDN:AAA51765.1; !1PID:g178855 REFERENCE S34056 !$#authors Ghiso, J.; Matsubara, E.; Koudinov, A.; Choi-Miura, N.H.; !1Tomita, M.; Wisniewski, T.; Frangione, B. !$#journal Biochem. J. (1993) 293:27-30 !$#title Research Communication. The cerebrospinal-fluid soluble form !1of Alzheimer's amyloid beta is complexed to SP-40,40 !1(apolipoprotein J), an inhibitor of the complement !1membrane-attack complex. !$#cross-references MUID:93319521; PMID:8328966 !$#accession S34056 !'##molecule_type protein !'##residues 228-240,'X',242-246;23-24,'X',26-34,'X',36-38,'X',40-41 !1##label GHI REFERENCE A53177 !$#authors James, R.W.; Hochstrasser, A.C.; Borghini, I.; Martin, B.; !1Pometta, D.; Hochstrasser, D. !$#journal Arterioscler. Thromb. (1991) 11:645-652 !$#title Characterization of a human high density !1lipoprotein-associated protein, NA1/NA2. Identity with !1SP-40,40, an inhibitor of complement-mediated cytolysis. !$#cross-references MUID:91230083; PMID:1903064 !$#accession A53177 !'##molecule_type protein !'##residues 229-242;303-304,'M',306-312,'X',314-317;397-403 ##label JAM REFERENCE A37816 !$#authors de Silva, H.V.; Stuart, W.D.; Park, Y.B.; Mao, S.J.T.; Gil, !1C.M.; Wetterau, J.R.; Busch, S.J.; Harmony, J.A.K. !$#journal J. Biol. Chem. (1990) 265:14292-14297 !$#title Purification and characterization of apolipoprotein J. !$#cross-references MUID:90354412; PMID:2387851 !$#accession A37816 !'##molecule_type protein !'##residues 23-46,'H',48-51,'Q' ##label DE3 !'##note amino end of the alpha chain !$#accession B37816 !'##molecule_type protein !'##residues 228-257 ##label DE2 !'##note amino end of the beta chain REFERENCE PL0135 !$#authors Choi, N.H.; Mazda, T.; Tomita, M. !$#journal Mol. Immunol. (1989) 26:835-840 !$#title A serum protein SP40,40 modulates the formation of membrane !1attack complex of complement on erythrocytes. !$#cross-references MUID:90097955; PMID:2601725 !$#accession PL0136 !'##molecule_type protein !'##residues 23-37 ##label CHO !'##note this fragment was isolated from the membrane attack complex !1SC5b-9 !$#accession PL0135 !'##molecule_type protein !'##residues 228-242 ##label CH2 !'##note this fragment was isolated from the membrane attack complex !1SC5b-9 REFERENCE S07433 !$#authors Hochstrasser, A.C.; James, R.W.; Martin, B.M.; Harrington, !1M.; Hochstrasser, D.; Pometta, D.; Merril, C.R. !$#journal Appl. Theor. Electrophor. (1988) 1:73-76 !$#title HDL particle associated proteins in plasma and cerebrospinal !1fluid: identification and partial sequencing. !$#cross-references MUID:91265608; PMID:3154963 !$#accession S09339 !'##molecule_type protein !'##residues 229-240 ##label HOC !$#accession S07433 !'##molecule_type protein !'##residues 24-27,'S',29-33 ##label HO2 REFERENCE A56293 !$#authors Kirszbaum, L.; Bozas, S.E.; Walker, I.D. !$#journal FEBS Lett. (1992) 297:70-76 !$#title SP-40,40, a protein involved in the control of the !1complement pathway, possesses a unique array of disulphide !1bridges. !$#cross-references MUID:92201397; PMID:1551440 !$#contents annotation; disulfide bonds, carbohydrate binding sites REFERENCE A54223 !$#authors Kunitake, S.T.; Carilli, C.T.; Lau, K.; Protter, A.A.; !1Naya-Vigne, J.; Kane, J.P. !$#journal Biochemistry (1994) 33:1988-1993 !$#title Identification of proteins associated with apolipoprotein !1A-I-containing lipoproteins purified by selected-affinity !1immunosorption. !$#cross-references MUID:94162201; PMID:8117655 !$#accession E54223 !'##molecule_type protein !'##residues 228-246 ##label KUN !'##experimental_source apolipoprotein A-I-containing lipoproteins, !1plasma !$#accession F54223 !'##molecule_type protein !'##residues 23-34,'X',36-37 ##label KU2 !'##experimental_source apolipoprotein A-I-containing lipoproteins, !1plasma REFERENCE I59206 !$#authors Danik, M.; Chabot, J.G.; Mercier, C.; Benabid, A.L.; !1Chauvin, C.; Quirion, R.; Suh, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:8577-8581 !$#title Human gliomas and epileptic foci express high levels of a !1mRNA related to rat testicular sulfated glycoprotein 2, a !1purported marker of cell death. !$#cross-references MUID:92020896; PMID:1924317 !$#accession I59206 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 61-449 ##label RES !'##cross-references GB:M74816; NID:g338056; PIDN:AAA60321.1; !1PID:g338057 REFERENCE I48174 !$#authors Duguid, J.R.; Bohmont, C.W.; Liu, N.G.; Tourtellotte, W.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:7260-7264 !$#title Changes in brain gene expression shared by scrapie and !1Alzheimer disease. !$#cross-references MUID:89386721; PMID:2780570 !$#accession I63132 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 103-168 ##label RE2 !'##cross-references GB:M26639; NID:g338070; PIDN:AAA36609.1; !1PID:g553644 COMMENT This protein has been implicated in complement cascade !1inhibition, membrane remodelling, lipid transport, and sperm !1maturation. It is expressed in solid tissues undergoing !1apoptosis, as well as in normal brain, in tissues affected !1by neurodegenerative disease processes, and on mature sperm !1cells. COMMENT This protein may assist in preventing the formation of !1Alzheimer's disease-associated amyloid fibrils by binding to !1the amyloid beta protein in solution. GENETICS !$#gene GDB:CLU; CLI !'##cross-references GDB:125226; OMIM:185430 !$#map_position 8p21-8p21 !$#note appears to be a single-copy gene; alternative exon usage in !15'-untranslated region b is suggested CLASSIFICATION #superfamily clusterin KEYWORDS apoptosis; complement inhibitor; extracellular protein; !1glycoprotein; HDL; lipid binding; lipoprotein; plasma FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-227 #domain clusterin beta chain #status experimental !8#label BCH\ !$23-227,228-449 #product clusterin #status experimental #label MAT\ !$228-449 #domain clusterin alpha chain #status experimental !8#label ACH\ !$86,103,145,291,354, !$374 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$102-313,121-295, !$129-285 #disulfide_bonds #status experimental\ !$113-305,116-302 #disulfide_bonds (or 113-302, 116-305) #status !8experimental\ !$317 #binding_site carbohydrate (Asn) (covalent) #status !8absent SUMMARY #length 449 #molecular-weight 52494 #checksum 4400 SEQUENCE /// ENTRY VLEU1 #type complete TITLE apovitellenin I - emu ORGANISM #formal_name Dromaius novaehollandiae #common_name emu DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 23-Aug-1996 ACCESSIONS A03101 REFERENCE A03101 !$#authors Dopheide, T.A.A.; Inglis, A.S. !$#journal Aust. J. Biol. Sci. (1974) 27:15-21 !$#title The amino acid sequence of a protein (apovitellenin I) from !1the low-density lipoprotein of emu egg yolk. !$#cross-references MUID:74151324; PMID:4363370 !$#accession A03101 !'##molecule_type protein !'##residues 1-84 ##label DOP COMMENT Apovitellenin I is the major protein component of the very !1low density lipoprotein fraction of the egg yolk. CLASSIFICATION #superfamily apovitellenin I KEYWORDS egg yolk; homodimer SUMMARY #length 84 #molecular-weight 9740 #checksum 5970 SEQUENCE /// ENTRY VLDK1 #type complete TITLE apovitellenin I - duck (tentative sequence) ORGANISM #formal_name Anas platyrhynchos #common_name domestic duck DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 31-Mar-2000 ACCESSIONS A03102 REFERENCE A03102 !$#authors Inglis, A.S.; Burley, R.W. !$#journal FEBS Lett. (1977) 73:33-37 !$#title Determination of the amino acid sequence of apovitellenin I !1from duck's egg yolk using an improved sequenator procedure: !1a comparison with other avian species. !$#cross-references MUID:77116126; PMID:838046 !$#accession A03102 !'##molecule_type protein !'##residues 1-82 ##label ING !'##experimental_source Pekin breed CLASSIFICATION #superfamily apovitellenin I KEYWORDS egg yolk; homodimer SUMMARY #length 82 #molecular-weight 9492 #checksum 3360 SEQUENCE /// ENTRY VLCH1 #type complete TITLE apovitellenin I precursor - chicken ALTERNATE_NAMES very low density lipoprotein II ORGANISM #formal_name Gallus gallus #common_name chicken DATE 29-Jun-1981 #sequence_revision 29-Jun-1981 #text_change 24-Sep-1999 ACCESSIONS A93464; A93740; A91484; B91484; A92263; A90091; A92202; !1A03103 REFERENCE A93464 !$#authors van het Schip, A.D.; Meijlink, F.C.P.W.; Strijker, R.; !1Gruber, M.; van Vliet, A.J.; van de Klundert, J.A.M.; AB, G. !$#journal Nucleic Acids Res. (1983) 11:2529-2540 !$#title The nucleotide sequence of the chicken apo very low density !1lipoprotein II gene. !$#cross-references MUID:83220801; PMID:6856469 !$#accession A93464 !'##molecule_type DNA !'##residues 1-106 ##label VAN !'##cross-references GB:J00810; GB:J00809; GB:M14120; NID:g211155; !1PIDN:AAA48596.1; PID:g211156 REFERENCE A93740 !$#authors Wieringa, B.; AB, G.; Gruber, M. !$#journal Nucleic Acids Res. (1981) 9:489-501 !$#title The nucleotide sequence of the very low density lipoprotein !1II mRNA from chicken. !$#cross-references MUID:81174717; PMID:7012793 !$#accession A93740 !'##molecule_type mRNA !'##residues 1-106 ##label WIE !'##cross-references GB:J00810; GB:J00809; GB:M14120; NID:g211155; !1PIDN:AAA48596.1; PID:g211156 REFERENCE A91484 !$#authors Dugaiczyk, A.; Inglis, A.S.; Strike, P.M.; Burley, R.W.; !1Beattie, W.G.; Chan, L. !$#journal Gene (1981) 14:175-182 !$#title Comparison of the nucleotide sequence of cloned DNA coding !1for an apolipoprotein (apoVLDL-II) from avian blood and the !1amino acid sequence of an egg-yolk protein (apovitellenin !1I): equivalence of the two sequences. !$#cross-references MUID:82028654; PMID:7286648 !$#accession A91484 !'##molecule_type mRNA !'##residues 1-106 ##label DU1 !'##cross-references GB:J00810; GB:J00809; GB:M14120; NID:g211155; !1PIDN:AAA48596.1; PID:g211156 !$#accession B91484 !'##molecule_type protein !'##residues 1-106 ##label DU2 REFERENCE A92263 !$#authors Chan, L.; Bradley, W.A.; Means, A.R. !$#journal J. Biol. Chem. (1980) 255:10060-10063 !$#title Amino acid sequence of the signal peptide of ApoVLDL-II, a !1major apoprotein in avian very low density lipoproteins. !$#cross-references MUID:81046825; PMID:7430115 !$#accession A92263 !'##molecule_type protein !'##residues 1,3-22,'C',24-51 ##label CHA REFERENCE A90091 !$#authors Dopheide, T.A.A.; Inglis, A.S. !$#journal Aust. J. Biol. Sci. (1976) 29:175-180 !$#title Primary structure of apovitellenin I from hen egg yolk and !1its comparison with emu apovitellenin I. !$#cross-references MUID:77044306; PMID:988817 !$#accession A90091 !'##molecule_type protein !'##residues 25-70,'IGS',74-90,'ML',93-106 ##label DOP !'##experimental_source egg yolk REFERENCE A92202 !$#authors Jackson, R.L.; Lin, H.Y.; Chan, L.; Means, A.R. !$#journal J. Biol. Chem. (1977) 252:250-253 !$#title Amino acid sequence of a major apoprotein from hen plasma !1very low density lipoproteins. !$#cross-references MUID:77093798; PMID:188805 !$#accession A92202 !'##molecule_type protein !'##residues 25-106 ##label JAC !'##experimental_source plasma !'##note this sequence differs from that shown at several positions COMMENT This protein is found in egg yolk and in plasma. GENETICS !$#introns 21/1; 74/2 CLASSIFICATION #superfamily apovitellenin I KEYWORDS egg yolk; homodimer FEATURE !$1-24 #domain signal sequence #status experimental #label !8SIG\ !$25-106 #product apovitellenin I #status experimental #label !8MAT\ !$99 #disulfide_bonds interchain #status experimental SUMMARY #length 106 #molecular-weight 11966 #checksum 859 SEQUENCE /// ENTRY VLTK1 #type complete TITLE apovitellenin I - turkey ORGANISM #formal_name Meleagris gallopavo #common_name common turkey DATE 30-Apr-1979 #sequence_revision 30-Apr-1979 #text_change 23-Aug-1996 ACCESSIONS A03104 REFERENCE A03104 !$#authors Inglis, A.S.; Strike, P.M.; Osborne, W.C.; Burley, R.W. !$#journal FEBS Lett. (1979) 97:179-182 !$#title Sequenator determination of the amino acid sequence of !1apovitellenin I from turkey's egg yolk. !$#cross-references MUID:79107437; PMID:570128 !$#accession A03104 !'##molecule_type protein !'##residues 1-82 ##label ING CLASSIFICATION #superfamily apovitellenin I KEYWORDS egg yolk; homodimer SUMMARY #length 82 #molecular-weight 9538 #checksum 4107 SEQUENCE /// ENTRY KART #type complete TITLE alpha-casein precursor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 16-Aug-1996 ACCESSIONS A03105; A23514 REFERENCE A93452 !$#authors Hobbs, A.A.; Rosen, J.M. !$#journal Nucleic Acids Res. (1982) 10:8079-8098 !$#title Sequence of rat alpha- and gamma-casein mRNAs: evolutionary !1comparison of the calcium-dependent rat casein multigene !1family. !$#cross-references MUID:83143278; PMID:6298707 !$#accession A03105 !'##molecule_type mRNA !'##residues 1-284 ##label HOB !'##cross-references GB:J00710 REFERENCE A23514 !$#authors Yu-Lee, L.Y.; Richter-Mann, L.; Couch, C.H.; Stewart, A.F.; !1Mackinlay, A.G.; Rosen, J.M. !$#journal Nucleic Acids Res. (1986) 14:1883-1902 !$#title Evolution of the casein multigene family: conserved !1sequences in the 5' flanking and exon regions. !$#cross-references MUID:86148515; PMID:3952000 !$#accession A23514 !'##molecule_type DNA !'##residues 1-52 ##label YUL !'##cross-references GB:X03585 GENETICS !$#introns 17/3; 28/3; 37/3; 52/3 CLASSIFICATION #superfamily alpha-s1-casein KEYWORDS mammary gland; milk; phosphoprotein FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-284 #product alpha-casein #status predicted #label MAT SUMMARY #length 284 #molecular-weight 31801 #checksum 3848 SEQUENCE /// ENTRY KABOSB #type complete TITLE alpha-s1-casein precursor - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 24-Apr-1984 #sequence_revision 06-Feb-1995 #text_change 21-Jul-2000 ACCESSIONS S22575; A23071; S02202; A90940; A91188; A91192; A91274; !1S23156; A90738; I45871; I45852; I45870; I45872; A03106; !1S13300 REFERENCE S22575 !$#authors Koczan, D.; Hobom, G.; Seyfert, H.M. !$#journal Nucleic Acids Res. (1991) 19:5591-5596 !$#title Genomic organization of the bovine alpha-S1 casein gene. !$#cross-references MUID:92051301; PMID:1658736 !$#accession S22575 !'##status translation not shown !'##molecule_type DNA !'##residues 1-214 ##label KOC !'##cross-references EMBL:X59856; NID:g91; PIDN:CAA42516.1; PID:g92 REFERENCE A93517 !$#authors Stewart, A.F.; Willis, I.M.; Mackinlay, A.G. !$#journal Nucleic Acids Res. (1984) 12:3895-3907 !$#title Nucleotide sequences of bovine alpha-s1- and kappa-casein !1cDNAs. !$#cross-references MUID:84221403; PMID:6328443 !$#accession A23071 !'##molecule_type mRNA !'##residues 1-214 ##label STE !'##cross-references GB:X00564; NID:g175; PIDN:CAB57792.1; PID:g6015490 REFERENCE S02202 !$#authors Gorodetskii, S.I.; Zakharyev, V.M.; Kyarshulite, D.R.; !1Kapelinskaya, T.V.; Skryabin, K.G. !$#journal Biochemistry (N.Y.) (1986) 51:1402-1409 !$#title Cloning and nucleotide sequence of cDNA for bovine alpha !1(S1)-casein. !$#accession S02202 !'##molecule_type mRNA !'##residues 1-142,'D',144-210,'IS',213-214 ##label GOR !'##cross-references EMBL:M38641 !'##note this paper is a translation of the Russian paper published in !1Biokhimiya (1986) 51: 1641-1648 !'##note the authors translated the codon CAA for residue 74 as Glu, GAG !1for residue 84 as Gly, GAT for residue 143 as His, ATC for !1residue 211 as Met, and TCA for residue 212 as Pro REFERENCE A91214 !$#authors Mercier, J.C.; Grosclaude, F.; Ribadeau-Dumas, B. !$#journal Eur. J. Biochem. (1973) 40:323 !$#title Structure primaire de la caseine alpha-s1 et de la caseine !1beta bovine. !$#cross-references MUID:74082545; PMID:4797901 !$#contents annotation; A, B, C, and D variants, revisions to positions !174 and 92-93 REFERENCE A90940 !$#authors Willis, I.M.; Stewart, A.F.; Caputo, A.; Thompson, A.R.; !1Mackinlay, A.G. !$#journal DNA (1982) 1:375-386 !$#title Construction and identification by partial nucleotide !1sequence analysis of bovine casein and beta-lactoglobulin !1cDNA clones. !$#cross-references MUID:83182023; PMID:6897774 !$#accession A90940 !'##molecule_type mRNA !'##residues 55-130 ##label WIL !'##cross-references GB:K01084 REFERENCE A91188 !$#authors Mercier, J.C.; Grosclaude, F.; Ribadeau-Dumas, B. !$#journal Eur. J. Biochem. (1971) 23:41-51 !$#title Structure primaire de la caseine alpha-s1-bovine. Sequence !1complete. !$#cross-references MUID:72063417; PMID:4331376 !$#contents B variant !$#accession A91188 !'##molecule_type protein !'##residues 16-44,'Q',46-214 ##label MER !'##note the sequences of residues 85-99 and of 125-140 are similar, !1having 10 identities within 16 positions REFERENCE A91192 !$#authors Grosclaude, F.; Mahe, M.F.; Mercier, J.C.; Ribadeau-Dumas, !1B. !$#journal Eur. J. Biochem. (1972) 26:328-337 !$#title Caracterisation des variants genetiques des caseines !1alpha-S1 et beta bovines. !$#cross-references MUID:72214259; PMID:5064450 !$#contents annotation; D variant !$#accession A91192 !'##molecule_type protein !'##residues 16-44,'Q',46-67,'T',69-214 ##label GRO !'##note the D variant has a phosphorylated Thr at position 68 REFERENCE A91274 !$#authors Grosclaude, F.; Mahe, M.F.; Mercier, J.C.; Ribadeau-Dumas, !1B. !$#journal FEBS Lett. (1970) 11:109-112 !$#title Localisation, dans la partie NH-2-terminale de la caseine !1alpha-s1 bovine, d'une deletion de 13 acides amines !1differenciant le variant a des variants B et C. !$#contents A variant !$#accession A91274 !'##molecule_type protein !'##residues 23-28,42-44,'Q',46-49 ##label GR2 !'##note the sequence of the A variant lacks residues 29-41 of the B !1variant REFERENCE S23156 !$#authors Neuteboom, B.; Giuffrida, M.G.; Conti, A. !$#journal FEBS Lett. (1992) 305:189-191 !$#title Isolation of a new ligand-carrying casein fragment from !1bovine mammary gland microsomes. !$#cross-references MUID:93231344; PMID:1299613 !$#accession S23156 !'##molecule_type protein !'##residues 39-55 ##label NEU REFERENCE A90738 !$#authors Grosclaude, F.; Mercier, J.C.; Ribadeau-Dumas, B. !$#journal C. R. Acad. Sci. Hebd. Seances Acad. Sci. D (1969) !1268:3133-3136 !$#title Sur la localisation, dans la sequence COOH-terminale de la !1caseine alpha-s1 bovine, de la substitution GLU/GLY !1differenciant les variants genetiques B et C. !$#cross-references MUID:69257961; PMID:4979278 !$#contents C variant !$#accession A90738 !'##molecule_type protein !'##residues 205-206,'G',208-214 ##label GR3 REFERENCE A90740 !$#authors Grosclaude, F.; Mercier, J.C.; Ribadeau-Dumas, B. !$#journal C. R. Acad. Sci. D Sci. Nat. (1970) 271:563 !$#contents annotation; erratum; C variant, revision REFERENCE S13300 !$#authors Exterkate, F.A.; Alting, A.C.; Slangen, C.J. !$#journal Biochem. J. (1991) 273:135-139 !$#title Specificity of two genetically related cell-envelope !1proteinases of Lactococcus lactis subsp. cremoris towards !1alpha(s1)-casein-(1-23)-fragment. !$#cross-references MUID:91113130; PMID:1899185 !$#contents annotation; cleavage by Lactococcus lactis subsp. cremoris !1cell-envelope proteinases REFERENCE I45871 !$#authors Nagao, M.; Maki, M.; Sasaki, R.; Chiba, R. !$#journal Agric. Biol. Chem. (1984) 48:1663-1667 !$#title Isolation and sequence analysis of bovine alpha-s1-casein !1cDNA clone. !$#accession I45871 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-214 ##label NAG !'##cross-references GB:M33123; NID:g162791; PIDN:AAA30428.1; !1PID:g162792 REFERENCE I45852 !$#authors Kiarshulite, D.R.; Zakhar'ev, V.M.; Gorodetskii, S.I. !$#journal Dokl. Akad. Nauk SSSR (1985) 280:1433-1437 !$#title [Nucleotide sequence of the 3'-nontranslated region of the !1mRNA of alpha S1-casein in cows]. !$#cross-references MUID:85178933; PMID:3838718 !$#accession I45852 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 122-202,'L',204-214 ##label KIA !'##cross-references GB:M38658; NID:g162649; PIDN:AAA62707.1; !1PID:g162650 REFERENCE I45870 !$#authors Maki, M.; Nagao, M.; Hirose, M.; Chiba, H. !$#journal Agric. Biol. Chem. (1983) 47:441-444 !$#title Cloning of cDNA sequence coding for bovine alpha-s1-casein. !$#accession I45870 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 185-202 ##label MAK !'##cross-references GB:D00412; NID:g217532; PIDN:BAA00313.1; !1PID:g217533 REFERENCE I45872 !$#authors Gorodetskii, S.I.; Zakhar'ev, V.M.; Kyarshulite, D.R.; !1Kapelinskaya, T.V.; Skryabin, K.G. !$#journal Biokhimiia (1986) 51:1402-1409 !$#title Cloning and nucleotide sequence of cDNA for bovine !1alpha-S1-casein. !$#accession I45872 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-41,'L',43-142,'D',144-210,'IS',213-214 ##label GO2 !'##cross-references GB:M38641; NID:g162793; PIDN:AAA30429.1; !1PID:g162794 COMMENT The B variant sequence is shown. GENETICS !$#map_position 6 !$#introns 17/3; 28/3; 41/3; 49/3; 57/3; 65/3; 73/3; 84/3; 92/3; 110/3; !1124/3; 132/3; 146/3; 155/3; 163/3 CLASSIFICATION #superfamily alpha-s1-casein KEYWORDS mammary gland; milk; phosphoprotein FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-214 #product alpha-s1-casein #status predicted #label !8MAT\ !$61,63,79,81,82,83, !$90,130 #binding_site phosphate (Ser) (covalent) #status !8experimental SUMMARY #length 214 #molecular-weight 24529 #checksum 2471 SEQUENCE /// ENTRY KASHS1 #type complete TITLE alpha-s1-casein precursor - sheep ORGANISM #formal_name Ovis orientalis aries, Ovis ammon aries #common_name domestic sheep DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 22-Jun-1999 ACCESSIONS A25069 REFERENCE A25069 !$#authors Mercier, J.C.; Gaye, P.; Soulier, S.; Hue-Delahaie, D.; !1Vilotte, J.L. !$#journal Biochimie (1985) 67:959-971 !$#title Construction and identification of recombinant plasmids !1carrying cDNAs coding for ovine alpha-s1-, alpha-s2-, beta-, !1kappa-casein and beta-lactoglobulin. Nucleotide sequence of !1alpha-s1-casein cDNA. !$#cross-references MUID:86104473; PMID:3002501 !$#accession A25069 !'##molecule_type mRNA !'##residues 1-206 ##label MER !'##cross-references GB:X03237; NID:g1247; PIDN:CAA26982.1; PID:g1248 !'##note the authors translated the codon TCT for residue 27 as Asp GENETICS !$#map_position 2 CLASSIFICATION #superfamily alpha-s1-casein KEYWORDS mammary gland; milk; phosphoprotein FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-206 #product alpha-s1-casein #status predicted #label !8KA1\ !$105-111 #region opioid-like peptide sequence\ !$79,80,81,82,83 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 206 #molecular-weight 23303 #checksum 8365 SEQUENCE /// ENTRY A45661 #type complete TITLE alpha s1-casein - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 22-Apr-1993 #sequence_revision 02-Jun-1994 #text_change 22-Jun-1999 ACCESSIONS A45661 REFERENCE A45661 !$#authors Alexander, L.J.; Beattie, C.W. !$#journal Anim. Genet. (1992) 23:283-288 !$#title The sequence of porcine alpha s1-casein cDNA: evidence for !1protein variants generated by altered RNA splicing. !$#cross-references MUID:92367946; PMID:1503265 !$#accession A45661 !'##molecule_type mRNA !'##residues 1-206 ##label ALE !'##cross-references GB:X54973; GB:S42665; NID:g406770; PIDN:CAA38717.1; !1PID:g406771 !'##experimental_source mammary gland !'##note sequence extracted from NCBI backbone (NCBIN:111173, !1NCBIP:111174) CLASSIFICATION #superfamily alpha-s1-casein KEYWORDS mammary gland; milk; phosphoprotein SUMMARY #length 206 #molecular-weight 24148 #checksum 8226 SEQUENCE /// ENTRY KABOS2 #type complete TITLE alpha-s2-casein precursor - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 01-Sep-1981 #sequence_revision 03-Feb-1994 #text_change 22-Jun-1999 ACCESSIONS JQ2008; A29087; A91438; S66626; A03107 REFERENCE JQ2008 !$#authors Groenen, M.A.M.; Dijkhof, R.J.M.; Verstege, A.J.M.; van der !1Poel, J.J. !$#journal Gene (1993) 123:187-193 !$#title The complete sequence of the gene encoding bovine !1alphas2-casein. !$#cross-references MUID:93154583; PMID:8428658 !$#accession JQ2008 !'##status translation not shown !'##molecule_type DNA !'##residues 1-222 ##label GRO !'##cross-references GB:M94327 REFERENCE A93062 !$#authors Stewart, A.F.; Bonsing, J.; Beattie, C.W.; Shah, F.; Willis, !1I.M.; Mackinlay, A.G. !$#journal Mol. Biol. Evol. (1987) 4:231-241 !$#title Complete nucleotide sequences of bovine alpha-s2- and !1beta-casein cDNAs: comparisons with related sequences in !1other species. !$#cross-references MUID:88188989; PMID:2833669 !$#accession A29087 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-222 ##label STE !'##cross-references GB:M16644; NID:g162928; PIDN:AAA30479.1; !1PID:g162929 REFERENCE A91438 !$#authors Brignon, G.; Ribadeau Dumas, B.; Mercier, J.C.; Pelissier, !1J.P.; Das, B.C. !$#journal FEBS Lett. (1977) 76:274-279 !$#title Complete amino acid sequence of bovine alpha-S2-casein. !$#cross-references MUID:77185633; PMID:862906 !$#contents A allele !$#accession A91438 !'##molecule_type protein !'##residues 16-101,'EE',104-222 ##label BRI !'##note four fractions, previously designated s2, s3, s4, and s6, !1appear to have the same primary structure and to differ only !1in phosphate content; the sequence shown was determined on a !1mixture of these REFERENCE A92771 !$#authors Grosclaude, F.; Joudrier, P.; Mahe, M.F. !$#journal J. Dairy Res. (1979) 46:211-213 !$#title A genetic and biochemical analysis of a polymorphism of !1bovine alpha-s2-casein. !$#cross-references MUID:79239837; PMID:469044 !$#contents annotation; D allele !$#note the sequence of the D allele has a deletion of nine !1residues, which may be 49-58, 50-59, or 51-60 REFERENCE S66626 !$#authors Zucht, H.D.; Raida, M.; Adermann, K.; Maegert, H.J.; !1Forssmann, W.G. !$#journal FEBS Lett. (1995) 372:185-188 !$#title Casocidin-I: a casein-alpha(s2) derived peptide exhibits !1antibacterial activity. !$#cross-references MUID:96000204; PMID:7556666 !$#accession S66626 !'##molecule_type protein !'##residues 165-203 ##label ZUC COMMENT The sequence of the A allele is shown. GENETICS !$#gene alphas2ca !$#map_position 6 !$#introns 17/3; 26/3; 33/3; 47/3; 56/3; 65/3; 74/3; 82/3; 97/3; 138/3; !1147/3; 156/3; 164/3; 179/3; 219/3 CLASSIFICATION #superfamily alpha-s2-casein KEYWORDS mammary gland; milk; phosphoprotein FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-222 #product alpha-s2-casein #status experimental #label !8MAT\ !$23,24,25,31,71,72, !$73,76,144,146,158 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 222 #molecular-weight 26019 #checksum 6555 SEQUENCE /// ENTRY KASHS2 #type complete TITLE alpha-s2-casein precursor - sheep ORGANISM #formal_name Ovis orientalis aries, Ovis ammon aries #common_name domestic sheep DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 22-Jun-1999 ACCESSIONS A25070; S17856 REFERENCE A25070 !$#authors Boisnard, M.; Petrissant, G. !$#journal Biochimie (1985) 67:1043-1051 !$#title Complete sequence of ovine alpha-s2-casein messenger RNA. !$#cross-references MUID:86104467; PMID:3002499 !$#accession A25070 !'##molecule_type mRNA !'##residues 1-223 ##label BOI !'##cross-references GB:X03238; NID:g1238; PIDN:CAA26983.1; PID:g732894 !'##note 64-Asn was also found REFERENCE S17856 !$#authors Boisnard, M.; Hue, D.; Bouniol, C.; Mercier, J.C.; Gaye, P. !$#journal Eur. J. Biochem. (1991) 201:633-641 !$#title Multiple mRNA species code for two non-allelic forms of !1ovine alphas2-casein. !$#cross-references MUID:92037619; PMID:1935959 !$#accession S17856 !'##status preliminary !'##molecule_type mRNA !'##residues 1-93,'T',95-223 ##label BO2 CLASSIFICATION #superfamily alpha-s2-casein KEYWORDS mammary gland; milk; phosphoprotein FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-223 #product alpha-s2-casein #status predicted #label !8KA2\ !$23,24,25,32,55,72, !$73,74,77,145,147, !$159 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$53,88,146,154,170, !$198 #binding_site phosphate (Thr) (covalent) #status !8predicted SUMMARY #length 223 #molecular-weight 26332 #checksum 9591 SEQUENCE /// ENTRY KEMS #type complete TITLE epsilon-casein precursor - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 21-Jan-1997 ACCESSIONS A03108 REFERENCE A03108 !$#authors Hennighausen, L.G.; Steudle, A.; Sippel, A.E. !$#journal Eur. J. Biochem. (1982) 126:569-572 !$#title Nucleotide sequence of cloned cDNA coding for mouse epsilon !1casein. !$#cross-references MUID:83053340; PMID:6897225 !$#accession A03108 !'##molecule_type mRNA !'##residues 1-143 ##label HEN CLASSIFICATION #superfamily alpha-s2-casein KEYWORDS phosphoprotein FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-143 #product epsilon-casein #status predicted #label MAT\ !$24,25,28,32,47,61 #binding_site phosphate (Ser) (covalent) (by casein !8kinase II) #status predicted SUMMARY #length 143 #molecular-weight 16911 #checksum 1388 SEQUENCE /// ENTRY KBRT #type complete TITLE beta-casein precursor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 22-Jun-1999 ACCESSIONS A93420; A92533; A03109; A24052 REFERENCE A93420 !$#authors Blackburn, D.E.; Hobbs, A.A.; Rosen, J.M. !$#journal Nucleic Acids Res. (1982) 10:2295-2307 !$#title Rat beta casein cDNA: sequence nalysis and evolutionary !1comparisons. !$#cross-references MUID:82221409; PMID:6283475 !$#accession A93420 !'##molecule_type mRNA !'##residues 1-231 ##label BLA !'##cross-references GB:J00711; NID:g203306; PIDN:AAA40878.1; !1PID:g203307 REFERENCE A92533 !$#authors Jones, W.K.; Yu-Lee, L.; Clift, S.M.; Brown, T.L.; Rosen, !1J.M. !$#journal J. Biol. Chem. (1985) 260:7042-7050 !$#title The rat casein multigene family. Fine structure and !1evolution of the beta-casein gene. !$#cross-references MUID:85207725; PMID:3997858 !$#accession A92533 !'##molecule_type DNA !'##residues 1-231 ##label JON !'##note the codons given for residues 100 (GTT), 113 (GAA), and 115 !1(GAA) are inconsistent with the authors' translation and !1with their statement that the sequence differs from that !1determined from the mRNA at only one position (71-Gln) COMMENT Caseins aggregate into loose micelles by the interaction of !1their hydrophobic carboxyl ends. COMMENT Beta casein binds calcium. GENETICS !$#introns 17/3; 26/3; 33/3; 41/3; 55/3; 230/3 CLASSIFICATION #superfamily beta-casein KEYWORDS calcium; lactation; mammary gland; milk; phosphoprotein FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-231 #product beta-casein #status predicted #label MPT\ !$24,29,31,32,35,105 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 231 #molecular-weight 25385 #checksum 8546 SEQUENCE /// ENTRY KBHU #type complete TITLE beta-casein precursor [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1988 #sequence_revision 15-Aug-1997 #text_change 08-Dec-2000 ACCESSIONS I53730; S08040; S04049; S11072; A27219; A30773 REFERENCE I53730 !$#authors Hansson, L.; Edlund, A.; Johansson, T.; Hernell, O.; !1Stromqvist, M.; Lindquist, S.; Lonnerdal, B.; Bergstrom, S. !$#journal Gene (1994) 139:193-199 !$#title Structure of the human beta-casein encoding gene. !$#cross-references MUID:94156198; PMID:8112603 !$#accession I53730 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-226 ##label RES !'##cross-references GB:L10615; NID:g2695660; PIDN:AAC82978.1; !1PID:g2695661 REFERENCE S08040 !$#authors Menon, R.S. !$#submission submitted to the EMBL Data Library, October 1989 !$#accession S08040 !'##molecule_type mRNA !'##residues 1-132,'V',134-139,'Q',141-226 ##label MEN !'##cross-references EMBL:X17070 REFERENCE S04049 !$#authors Menon, R.S.; Ham, R.G. !$#journal Nucleic Acids Res. (1989) 17:2869 !$#title Human beta-casein: partial cDNA sequence and apparent !1polymorphism. !$#cross-references MUID:89240053; PMID:2717418 !$#accession S04049 !'##molecule_type mRNA !'##residues 161-226 ##label MEN2 !'##cross-references EMBL:X13766; NID:g29673; PIDN:CAA32017.1; !1PID:g29674 REFERENCE S11072 !$#authors Loennerdal, B.; Bergstroem, S.; Andersson, Y.; Hjalmarsson, !1K.; Sundqvist, A.K.; Hernell, O. !$#journal FEBS Lett. (1990) 269:153-156 !$#title Cloning and sequencing of a cDNA encoding human milk !1beta-casein. !$#cross-references MUID:90353560; PMID:2387396 !$#accession S11072 !'##status preliminary !'##molecule_type mRNA !'##residues 1-33,35-226 ##label LOE !'##cross-references GB:X55739; NID:g288097; PIDN:CAA39270.1; !1PID:g288098 REFERENCE A27219 !$#authors Greenberg, R.; Groves, M.L.; Dower, H.J. !$#journal J. Biol. Chem. (1984) 259:5132-5138 !$#title Human beta-casein: amino acid sequence and identification of !1phosphorylation sites. !$#cross-references MUID:84185624; PMID:6715339 !$#accession A27219 !'##molecule_type protein !'##residues 16-29,'P',31-47,'T',49,'Q',51-119,'Q',121-148,'S',150-172, !1'E',174-181,'E',183,'L',185-187,'V',189-206,'P',208-213, !1'PE',216,'STTZABH',223-226 ##label GRE GENETICS !$#gene GDB:CSN2; CASB !'##cross-references GDB:125234; OMIM:115460 !$#map_position 4q13-4q21 !$#introns 17/3; 26/3; 33/3; 48/3; 225/3 CLASSIFICATION #superfamily beta-casein KEYWORDS calcium; milk; phosphoprotein FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-226 #product beta-casein #status experimental #label MAT\ !$18 #binding_site phosphate (Thr) (covalent) #status !8experimental\ !$21,23,24,25 #binding_site phosphate (Ser) (covalent) #status !8experimental SUMMARY #length 226 #molecular-weight 25382 #checksum 5687 SEQUENCE /// ENTRY KBBOA2 #type complete TITLE beta-casein precursor - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 24-Apr-1984 #sequence_revision 12-May-1995 #text_change 11-May-2000 ACCESSIONS I45873; B29087; S01860; A25846; S02429; A90489; A91191; !1B91192; C91192; D91192; A90739; I46963; A91413; A03110 REFERENCE I45873 !$#authors Bonsing, J.; Ring, J.M.; Stewart, A.F.; Mackinlay, A.G. !$#journal Aust. J. Biol. Sci. (1988) 41:527-537 !$#title Complete nucleotide sequence of the bovine beta-casein gene. !$#cross-references MUID:90147279; PMID:3271384 !$#accession I45873 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-81,'H',83-224 ##label BON !'##cross-references GB:M55158; NID:g162804; PIDN:AAA30431.1; !1PID:g162805 REFERENCE A93062 !$#authors Stewart, A.F.; Bonsing, J.; Beattie, C.W.; Shah, F.; Willis, !1I.M.; Mackinlay, A.G. !$#journal Mol. Biol. Evol. (1987) 4:231-241 !$#title Complete nucleotide sequences of bovine alpha-s2- and !1beta-casein cDNAs: comparisons with related sequences in !1other species. !$#cross-references MUID:88188989; PMID:2833669 !$#accession B29087 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-224 ##label STE !'##cross-references GB:M16645; NID:g162930; PIDN:AAA30480.1; !1PID:g162931 !'##experimental_source A2 variant REFERENCE S01860 !$#authors Baev, A.A.; Smirnov, I.K.; Gorodetskii, S.I. !$#journal Mol. Biol. (1987) 21:214-222 !$#title Primary structure of bovine beta-casein cDNA. !$#accession S01860 !'##molecule_type mRNA !'##residues 1-81,'H',83-224 ##label BAE !'##cross-references EMBL:X06359; NID:g171; PIDN:CAA29658.1; PID:g757752 !'##experimental_source A1 variant !'##note this paper is a translation of the Russian paper published in !1Mol. Biol. Moscow (1987) 21: 255-265 REFERENCE A25846 !$#authors Jimenez-Flores, R.; Kang, Y.C.; Richardson, T. !$#journal Biochem. Biophys. Res. Commun. (1987) 142:617-621 !$#title Cloning and sequence analysis of bovine beta-casein cDNA. !$#cross-references MUID:87128158; PMID:3814153 !$#accession A25846 !'##molecule_type mRNA !'##residues 1-107,'L',109-151,'PL',154-209,'Q',211-224 ##label JIM !'##cross-references GB:M15132; NID:g162796; PIDN:AAA30430.1; !1PID:g162797 REFERENCE S02429 !$#authors Carles, C.; Huet, J.C.; Ribadeau-Dumas, B. !$#journal FEBS Lett. (1988) 229:265-272 !$#title A new strategy for primary structure determination of !1proteins: application to bovine beta-casein. !$#cross-references MUID:88152252; PMID:3278933 !$#accession S02429 !'##molecule_type protein !'##residues 16-81,'H',83-224 ##label CAR !'##experimental_source A1 variant REFERENCE A90489 !$#authors Yan, S.B.; Wold, F. !$#journal Biochemistry (1984) 23:3759-3765 !$#title Neoglycoproteins: in vitro introduction of glycosyl units at !1glutaminesin beta-casein using transglutaminase. !$#cross-references MUID:85000478; PMID:6148101 !$#accession A90489 !'##molecule_type protein !'##residues 16-224 ##label YAN REFERENCE A91191 !$#authors Ribadeau-Dumas, B.; Brignon, G.; Grosclaude, F.; Mercier, !1J.C. !$#journal Eur. J. Biochem. (1972) 25:505-514 !$#title Structure primaire de la caseine beta bovine. !$#cross-references MUID:72233212; PMID:4557764 !$#accession A91191 !'##molecule_type protein !'##residues 16-131,'Q',133-151,'PL',154-189,'E',191-209,'Q',211-224 !1##label RIB !'##experimental_source A2 variant !'##note article in French with an English abstract REFERENCE A91192 !$#authors Grosclaude, F.; Mahe, M.F.; Mercier, J.C.; Ribadeau-Dumas, !1B. !$#journal Eur. J. Biochem. (1972) 26:328-337 !$#title Caracterisation des variants genetiques des caseines !1alpha-S1 et beta bovines. !$#cross-references MUID:72214259; PMID:5064450 !$#note article in French with an English abstract !$#accession B91192 !'##molecule_type protein !'##residues 16-81,'H',83-131,'Q',133-151,'PL',154-189,'E',191-209,'Q', !1211-224 ##label VA1 !'##experimental_source A1 variant !$#accession C91192 !'##molecule_type protein !'##residues 16-81,'H',83-131,'Q',133-136,'R',138-151,'PL',154-189,'E', !1191-209,'Q',211-224 ##label VAB !'##experimental_source B variant !$#accession D91192 !'##molecule_type protein !'##residues 16-51,'K',53-81,'H',83-131,'Q',133-151,'PL',154-189,'E', !1191-209,'Q',211-224 ##label VAC !'##experimental_source C variant !'##note this variant lacks a phosphate group on 50-Ser REFERENCE A90739 !$#authors Ribadeau-Dumas, B.; Grosclaude, F.; Mercier, J.C. !$#journal C. R. Acad. Sci. Hebd. Seances Acad. Sci. D (1970) !1270:2369-2372 !$#title Localisation dans la chaine peptidique de la caseine beta !1bovine de la substitution His/Gln differenciant les variants !1genetiques A2 et A3. !$#cross-references MUID:71252171; PMID:4997616 !$#note article in French with an English abstract !$#accession A90739 !'##molecule_type protein !'##residues 118-120,'Q',122-124 ##label VA3 !'##experimental_source A3 variant REFERENCE I46963 !$#authors Simons, G.; van den Heuvel, W.; Reynen, T.; Frijters, A.; !1Rutten, G.; Slangen, C.J.; Groenen, M.; de Vos, W.M.; !1Siezen, R.J. !$#journal Protein Eng. (1993) 6:763-770 !$#title Overproduction of bovine beta-casein in Escherichia coli and !1engineering of its main chymosin cleavage site. !$#cross-references MUID:94068382; PMID:8248100 !$#accession I46963 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-120,'Q',122-224 ##label SIM !'##cross-references GB:S67277; NID:g459291; PIDN:AAB29137.1; !1PID:g459292 !'##experimental_source A3 variant REFERENCE A91413 !$#authors Grosclaude, F.; Mahe, M.F.; Voglino, G.F. !$#journal FEBS Lett. (1974) 45:3-5 !$#title Le variant beta-E et le code de phosphorylation des caseines !1bovines. !$#cross-references MUID:75005247; PMID:4411121 !$#note article in French with an English abstract !$#accession A91413 !'##molecule_type protein !'##residues 48-50,'K',52-63 ##label VAE !'##experimental_source E variant !'##note 50-Ser is phosphorylated COMMENT The sequence shown is the A2 variant. GENETICS !$#introns 17/3; 26/3; 35/3; 43/3; 57/3; 223/3 CLASSIFICATION #superfamily beta-casein KEYWORDS milk; phosphoprotein FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-224 #product beta-casein #status experimental #label MAT\ !$30,32,33,34 #binding_site phosphate (Ser) (covalent) (by casein !8kinase II) #status experimental\ !$50 #binding_site phosphate (Ser) (covalent) (by casein !8kinase II) (partial) #status experimental SUMMARY #length 224 #molecular-weight 25107 #checksum 8112 SEQUENCE /// ENTRY KGRT #type complete TITLE gamma-casein precursor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 31-May-1996 ACCESSIONS A03111 REFERENCE A93452 !$#authors Hobbs, A.A.; Rosen, J.M. !$#journal Nucleic Acids Res. (1982) 10:8079-8098 !$#title Sequence of rat alpha- and gamma-casein mRNAs: evolutionary !1comparison of the calcium-dependent rat casein multigene !1family. !$#cross-references MUID:83143278; PMID:6298707 !$#accession A03111 !'##molecule_type mRNA !'##residues 1-179 ##label HOB CLASSIFICATION #superfamily gamma-casein KEYWORDS phosphoprotein FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-179 #product gamma-casein #status predicted #label MAT SUMMARY #length 179 #molecular-weight 20277 #checksum 450 SEQUENCE /// ENTRY KKHU #type complete TITLE casein kappa precursor [validated] - human ALTERNATE_NAMES kappa-casein CONTAINS caseinoglycopeptide ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1988 #sequence_revision 03-Oct-1995 #text_change 08-Dec-2000 ACCESSIONS JC4957; A56638; A24001; A16604; S22070 REFERENCE JC4957 !$#authors Edlund, A.; Johansson, T.; Leidvik, B.; Hansson, L. !$#journal Gene (1996) 174:65-69 !$#title Structure of the human kappa-casein gene. !$#cross-references MUID:97017129; PMID:8863730 !$#accession JC4957 !'##molecule_type DNA !'##residues 1-182 ##label EDL !'##cross-references GB:U51899; NID:g1245481; PIDN:AAC50772.1; !1PID:g1245482 REFERENCE A56638 !$#authors Bergstroem, S.; Hansson, L.; Hernell, O.; Loennerdal, B.; !1Nilsson, A.K.; Stroemqvist, M. !$#journal DNA Seq. (1992) 3:245-246 !$#title Cloning and sequencing of human kappa-casein cDNA. !$#cross-references MUID:93208373; PMID:1296818 !$#accession A56638 !'##molecule_type mRNA !'##residues 1-182 ##label BER !'##cross-references EMBL:X66417; NID:g29675; PIDN:CAA47048.1; !1PID:g29676 !'##experimental_source lactating mammary gland !'##note sequence extracted from NCBI backbone (NCBIP:128264) REFERENCE A24001 !$#authors Brignon, G.; Chtourou, A.; Ribadeau-Dumas, B. !$#journal FEBS Lett. (1985) 188:48-54 !$#title Preparation and amino acid sequence of human kappa-casein. !$#cross-references MUID:85258132; PMID:4018271 !$#accession A24001 !'##molecule_type protein !'##residues 'E',25-26,28-123 ##label BRI !'##note the amino-terminal residue forms pyrrolidone carboxylic acid; !1therefore, we have shown it as Gln REFERENCE A16604 !$#authors Fiat, A.M.; Jolles, J.; Aubert, J.P.; Loucheux-Lefebvre, !1M.H.; Jolles, P. !$#journal Eur. J. Biochem. (1980) 111:333-339 !$#title Localisation and importance of the sugar part of human !1casein. !$#cross-references MUID:81114144; PMID:7460900 !$#accession A16604 !'##molecule_type protein !'##residues 118-160,'TT',163-172,'P',174-177,'PTTS',182 ##label FIA COMMENT This protein is only a minor component in human milk, !1whereas it is a cows milk. GENETICS !$#gene GDB:CSN10; casK; CSN3; Kca !'##cross-references GDB:5916337; OMIM:601695 !$#map_position 4q21.1-4q21.1 !$#introns 18/3; 29/3 !$#note the first intron occurs before the initiator codon CLASSIFICATION #superfamily kappa-casein KEYWORDS glycoprotein; mammary gland; milk; pyroglutamic acid FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-182 #product kappa-casein #status experimental #label !8MAT\ !$118-182 #product caseinoglycopeptide #status experimental !8#label CGP\ !$23 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$117-118 #cleavage_site Phe-Ile (chymosin) #status !8experimental\ !$133,143,148,151, !$157,167,169,178,181 #binding_site carbohydrate (Thr) (covalent) #status !8experimental\ !$162 #binding_site carbohydrate (Ser) (covalent) #status !8experimental SUMMARY #length 182 #molecular-weight 20305 #checksum 5383 SEQUENCE /// ENTRY KKBOB #type complete TITLE kappa-casein precursor - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 24-Apr-1984 #sequence_revision 23-Mar-1995 #text_change 16-Jun-2000 ACCESSIONS S02076; B23071; S06376; JN0364; A91206; A90033; A90920; !1A91634; A90592; A60833; S03993; I45875; A03112 REFERENCE S02076 !$#authors Alexander, L.J.; Stewart, A.F.; Mackinlay, A.G.; !1Kapelinskaya, T.V.; Tkach, T.M.; Gorodetsky, S.I. !$#journal Eur. J. Biochem. (1988) 178:395-401 !$#title Isolation and characterization of the bovine kappa-casein !1gene. !$#cross-references MUID:89091174; PMID:3208764 !$#contents A variant !$#accession S02076 !'##molecule_type DNA !'##residues 1-190 ##label ALE !'##cross-references EMBL:X14907; NID:g177; PIDN:CAA33034.1; !1PID:g1228078 REFERENCE A93517 !$#authors Stewart, A.F.; Willis, I.M.; Mackinlay, A.G. !$#journal Nucleic Acids Res. (1984) 12:3895-3907 !$#title Nucleotide sequences of bovine alpha-s1- and kappa-casein !1cDNAs. !$#cross-references MUID:84221403; PMID:6328443 !$#contents A variant !$#accession B23071 !'##molecule_type mRNA !'##residues 1-190 ##label STE !'##cross-references GB:X00565; NID:g170; PIDN:CAA25231.1; PID:g1364187 REFERENCE S06376 !$#authors Gorodetskii, S.I.; Kaledin, A.S. !$#journal Sov. Genet. (1987) 23:398-404 !$#title Analysis of nucleotide sequence of bovine kappa-casein cDNA. !$#contents B2 variant !$#accession S06376 !'##molecule_type mRNA !'##residues 1-138,'G',140-156,'I',158-168,'A',170-173,'T',175-190 !1##label GOR REFERENCE JN0364 !$#authors Gorodetsky, S.I.; Kershulite, D.D.; Korobko, B.G. !$#journal Bioorg. Khim. (1983) 9:1693-1694 !$#title Primary structure of cDNA of Bos taurus kappa-casein !1macropeptide. !$#cross-references MUID:85022828; PMID:6689612 !$#contents B2 variant !$#accession JN0364 !'##molecule_type mRNA !'##residues 92-156,'I',158-168,'A',170-173,'T',175-190 ##label GO2 !'##cross-references GB:M38333; NID:g162806; PIDN:AAA30432.1; !1PID:g162807 !'##note the authors translated the codon TTG for residue 100 as Pro and !1GAA for residue 139 as Gly REFERENCE A91206 !$#authors Mercier, J.C.; Brignon, G.; Ribadeau-Dumas, B. !$#journal Eur. J. Biochem. (1973) 35:222-235 !$#title Structure primaire de la caseine kappaB bovine. Sequence !1complete. !$#cross-references MUID:73216467; PMID:4577852 !$#contents B variant !$#accession A91206 !'##molecule_type protein !'##residues 22-101,'D',103-127 ##label MER !'##note the amino-terminal residue appears to be pyrrolidone carboxylic !1acid, but cyclization may have occurred during isolation and !1purification REFERENCE A90033 !$#authors Grosclaude, F.; Mahe, M.F.; Mercier, J.C.; Ribadeau-Dumas, !1B. !$#journal Ann. Genet. Sel. Anim. (1972) 4:515-521 !$#title Localisation des substitutions d'acides amines differenciant !1les variants A et B de la caseine kappa bovine. !$#contents A variant !$#accession A90033 !'##molecule_type protein !'##residues 128-190 ##label GRO !'##note article in French with English abstract REFERENCE A90920 !$#authors Jolles, J.; Schoentgen, F.; Alais, C.; Jolles, P. !$#journal Chimia (1972) 26:645-646 !$#contents A variant !$#accession A90920 !'##molecule_type protein !'##residues 22,'Q',24-25,'E',27,'E',29-126 ##label JO2 REFERENCE A91634 !$#authors Jolles, J.; Schoentgen, F.; Alais, C.; Fiat, A.M.; Jolles, !1P. !$#journal Helv. Chim. Acta (1972) 55:2872-2883 !$#title Studies on the primary structure of cow kappa-casein. !1Structural features of para-kappa-casein: N-terminal !1sequence of kappa-caseinoglycopeptide studied with a !1sequencer. !$#cross-references MUID:73124636; PMID:4653404 !$#contents B variant !$#accession A91634 !'##molecule_type protein !'##residues 22-101,'D',103-156,'I',158-168,'A',170-190 ##label JOL REFERENCE A90592 !$#authors Guerin, J.; Alais, C.; Jolles, J.; Jolles, P. !$#journal Biochim. Biophys. Acta (1974) 351:325-332 !$#title kappa-Casein from bovine colostrum. !$#cross-references MUID:74269749; PMID:4407313 !$#accession A90592 !'##molecule_type protein !'##residues 127-156,'I',158-168;187-190 ##label GUE !'##experimental_source colostrum REFERENCE A60833 !$#authors Mercier, J.C.; Uro, J.; Ribadeau-Dumas, B.; Grosclaude, F. !$#journal Eur. J. Biochem. (1972) 27:535-547 !$#title Structure primaire du caseinomacropeptide de la caseine !1kappaB-1 bovine. !$#cross-references MUID:72254481; PMID:4559180 !$#contents B variant !$#accession A60833 !'##molecule_type protein !'##residues 128-156,'I',158-168,'A',170-190 ##label ME2 !'##note article in French with English abstract REFERENCE S03993 !$#authors Drohse, H.B.; Foltmann, B. !$#journal Biochim. Biophys. Acta (1989) 995:221-224 !$#title Specificity of milk-clotting enzymes towards bovine !1kappa-casein. !$#cross-references MUID:89207571; PMID:2495817 !$#accession S03993 !'##molecule_type protein !'##residues 126-130 ##label DRO REFERENCE I45875 !$#authors Gorodetskii, S.I.; Kaledin, A.S. !$#journal Genetika (1987) 23:398-404 !$#title Analysis of nucleotide sequence of bovine kappa-casein cdna. !$#accession I45875 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-156,'I',158-168,'A',170-173,'T',175-190 ##label GO3 !'##cross-references GB:M36641; NID:g162810; PIDN:AAA30433.1; !1PID:g162811 COMMENT The sequence shown is the A variant. GENETICS !$#introns 19/3; 30/3 CLASSIFICATION #superfamily kappa-casein KEYWORDS glycoprotein; milk; phosphoprotein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-190 #product kappa-casein #status predicted #label MAT\ !$126-127 #cleavage_site Phe-Met (chymosin) #status !8experimental\ !$152 #binding_site carbohydrate (Thr) (covalent) #status !8experimental\ !$170 #binding_site phosphate (Ser) (covalent) #status !8experimental SUMMARY #length 190 #molecular-weight 21269 #checksum 9305 SEQUENCE /// ENTRY KKSHA #type complete TITLE kappa-casein precursor - sheep ORGANISM #formal_name Ovis orientalis aries, Ovis ammon aries #common_name domestic sheep DATE 24-Apr-1984 #sequence_revision 30-Sep-1991 #text_change 22-Jun-1999 ACCESSIONS S14711; A03113; A90597; S08655 REFERENCE S14711 !$#authors Furet, J.P.; Mercier, J.C.; Soulier, S.; Gaye, P.; !1Hue-Delahaie, D.; Vilotte, J.L. !$#journal Nucleic Acids Res. (1990) 18:5286 !$#title Nucleotide sequence of ovine kappa-casein cDNA. !$#cross-references MUID:90384837; PMID:2402453 !$#accession S14711 !'##molecule_type mRNA !'##residues 1-192 ##label FUR !'##cross-references EMBL:X51822; NID:g1293; PIDN:CAA36122.1; PID:g1294 REFERENCE A91221 !$#authors Jolles, J.; Schoentgen, F.; Hermann, J.; Alais, C.; Jolles, !1P. !$#journal Eur. J. Biochem. (1974) 46:127-132 !$#title The sequence of sheep kappa-casein: primary structure of !1para-kappa-A-casein. !$#cross-references MUID:74309256; PMID:4605338 !$#accession A03113 !'##molecule_type protein !'##residues 22,'Q',24-27,'E',29-129 ##label JOL1 REFERENCE A90597 !$#authors Jolles, J.; Fiat, A.M.; Schoentgen, F.; Alais, C.; Jolles, !1P. !$#journal Biochim. Biophys. Acta (1974) 365:335-343 !$#title The amino acid sequence of sheep kappa-A-casein. II. !1Sequence studies concerning the kappa-A-caseinoglycopeptide !1and establishment of the complete primary structure of the !1protein. !$#cross-references MUID:75036120; PMID:4429673 !$#accession A90597 !'##molecule_type protein !'##residues 127-192 ##label JOL2 CLASSIFICATION #superfamily kappa-casein KEYWORDS glycoprotein; mammary gland; milk; phosphoprotein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-192 #product kappa-casein #status experimental #label MAT SUMMARY #length 192 #molecular-weight 21438 #checksum 9739 SEQUENCE /// ENTRY KKGT #type complete TITLE kappa-casein - goat ORGANISM #formal_name Capra aegagrus hircus #common_name domestic goat DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 31-Dec-2000 ACCESSIONS A94479; A90670; A03114 REFERENCE A94479 !$#authors Mercier, J.C.; Addeo, F.; Pelissier, J.P. !$#citation unpublished results, cited by Mercier, J.C., Chobert, J.M., !1and Addeo, F., FEBS Lett. 72, 208-214, 1976 !$#description Comparative study of the amino acid sequences of the !1caseinomacropeptides from seven species. !$#accession A94479 !'##molecule_type protein !'##residues 1-171 ##label ME1 !'##note the amino-terminal residue appears to be pyrrolidone carboxylic !1acid, but cyclization may have occurred during isolation and !1purification REFERENCE A90670 !$#authors Mercier, J.C.; Addeo, F.; Pelissier, J.P. !$#journal Biochimie (1976) 58:1303-1310 !$#title Structure primaire du caseinomacropeptide de la caseine K !1caprine. !$#cross-references MUID:77112689; PMID:1016651 !$#accession A90670 !'##molecule_type protein !'##residues 106-171 ##label ME2 !'##note 119-Val was also found !'##note Ser-151 and Ser-168 are phosphorylated COMMENT Chymosin hydrolyzes the peptide bond between Phe-105 and !1Met-106. CLASSIFICATION #superfamily kappa-casein KEYWORDS mammary gland; milk; phosphoprotein SUMMARY #length 171 #molecular-weight 19160 #checksum 5408 SEQUENCE /// ENTRY KKRT #type complete TITLE kappa-casein precursor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 22-Jun-1999 ACCESSIONS A03115 REFERENCE A03115 !$#authors Nakhasi, H.L.; Grantham, F.H.; Gullino, P.M. !$#journal J. Biol. Chem. (1984) 259:14894-14898 !$#title Expression of kappa-casein in normal and neoplastic rat !1mammary gland is under the control of prolactin. !$#cross-references MUID:85054984; PMID:6094580 !$#accession A03115 !'##molecule_type mRNA !'##residues 1-178 ##label NAK !'##cross-references GB:K02598; NID:g203320; PIDN:AAA40880.1; !1PID:g203321 COMMENT Kappa casein stabilizes micelle formation, preventing casein !1precipitation in milk. COMMENT Prolactin modulates the production of kappa casein mRNA. CLASSIFICATION #superfamily kappa-casein KEYWORDS glycoprotein; mammary gland; phosphoprotein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-178 #product kappa-casein #status predicted #label KCA\ !$112 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$115-116 #cleavage_site Phe-Leu (chymosin) #status predicted\ !$120,145,165 #binding_site phosphate (Thr) (covalent) #status !8predicted SUMMARY #length 178 #molecular-weight 19548 #checksum 3665 SEQUENCE /// ENTRY FGHUA #type complete TITLE fibrinogen alpha chain precursor, short splice form [validated] - human ALTERNATE_NAMES coagulation factor I CONTAINS fibrinopeptide A ORGANISM #formal_name Homo sapiens #common_name man DATE 24-Apr-1984 #sequence_revision 30-Jun-1987 #text_change 08-Dec-2000 ACCESSIONS A93956; A43568; A90468; I84456; A44234; C44234; B94433; !1A90433; B94309; S19297; A60905; A03116; A33261; A37117; !1JC4334 REFERENCE A93956 !$#authors Kant, J.A.; Lord, S.T.; Crabtree, G.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:3953-3957 !$#title Partial mRNA sequences for human Aalpha, Bbeta, and gamma !1fibrinogen chains: evolutionary and functional implications. !$#cross-references MUID:83247396; PMID:6575389 !$#accession A93956 !'##molecule_type mRNA !'##residues 1-644 ##label KAN !'##cross-references GB:J00128; NID:g182425; PIDN:AAA52427.1; !1PID:g182426 !'##note the authors translated the codon GAG for residue 247 as Gly, !1GGA for residue 438 as Glu, and GAA for residue 610 as Gly REFERENCE A43568 !$#authors Chung, D.W.; Harris, J.E.; Davie, E.W. !$#journal Adv. Exp. Med. Biol. (1990) 281:39-48 !$#title Nucleotide sequences of the three genes coding for human !1fibrinogen. !$#cross-references MUID:91344740; PMID:2102623 !$#accession A43568 !'##molecule_type DNA !'##residues 1-330,'A',332-644 ##label CHU !'##cross-references GB:M64982; NID:g458553; PIDN:AAA17055.1; !1PID:g458554 REFERENCE A90468 !$#authors Rixon, M.W.; Chan, W.Y.; Davie, E.W.; Chung, D.W. !$#journal Biochemistry (1983) 22:3237-3244 !$#title Characterization of a complementary deoxyribonucleic acid !1coding for the alpha chain of human fibrinogen. !$#cross-references MUID:83283432; PMID:6688355 !$#accession A90468 !'##molecule_type mRNA !'##residues 1-330,'A',332-629 ##label RIX !'##cross-references GB:J00127; NID:g182423; PIDN:AAA52426.1; !1PID:g182424 REFERENCE I37393 !$#authors Imam, A.M.A.; Eaton, M.A.W.; Williamson, R.; Humphries, S. !$#journal Nucleic Acids Res. (1983) 11:7427-7434 !$#title Isolation and characterisation of cDNA clones for the !1Aalpha- and gamma-chains of human fibrinogen. !$#cross-references MUID:84069777; PMID:6689067 !$#accession I84456 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 110-156 ##label RES !'##cross-references GB:K02272; NID:g182427; PIDN:AAA52428.1; !1PID:g182428 REFERENCE A44234 !$#authors Fu, Y.; Weissbach, L.; Plant, P.W.; Oddoux, C.; Cao, Y.; !1Liang, T.J.; Roy, S.N.; Redman, C.M.; Grieninger, G. !$#journal Biochemistry (1992) 31:11968-11972 !$#title Carboxy-terminal-extended variant of the human fibrinogen !1alpha subunit: a novel exon conferring marked homology to !1beta and gamma subunits. !$#cross-references MUID:93090725; PMID:1457396 !$#accession A44234 !'##molecule_type mRNA !'##residues 1-51 ##label FU1 !'##cross-references GB:M64982; NID:g458553; PIDN:AAA17055.1; !1PID:g458554 !'##note sequence extracted from NCBI backbone (NCBIN:119912, !1NCBIN:119914, NCBIP:119918) !$#accession C44234 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 605-644 ##label FU2 !'##cross-references GB:M64982; NID:g458553; PIDN:AAA17055.1; !1PID:g458554 !'##note sequence extracted from NCBI backbone (NCBIP:119920) REFERENCE A94433 !$#authors Henschen, A.; Lottspeich, F.; Southan, C.; Topfer-Petersen, !1E. !$#book Protides of the Biological Fluids, Proc. 28th Colloq., !1Peeters, H., ed., pp.51-56, Pergamon Press, Oxford, 1980 !$#title Human fibrinogen: sequence, sulfur bridges, glycosylation !1and some structural variants. !$#accession B94433 !'##molecule_type protein !'##residues 20-214,'RS',217-298,'G',300-303,'G',305-629 ##label HEN REFERENCE A90433 !$#authors Watt, K.W.K.; Cottrell, B.A.; Strong, D.D.; Doolittle, R.F. !$#journal Biochemistry (1979) 18:5410-5416 !$#title Amino acid sequences studies on the alpha chain of human !1fibrinogen. Overlapping sequences providing the complete !1sequence. !$#cross-references MUID:80088231; PMID:518846 !$#contents disulfide bonds !$#accession A90433 !'##molecule_type protein !'##residues 20-146,'Q',148-195,'N',197-230,'N',232-316,'SG',319-406, !1'D',408,'N',410-629 ##label WAT REFERENCE A94309 !$#authors Blomback, B.; Hessel, B.; Hogg, D. !$#journal Thromb. Res. (1976) 8:639-658 !$#title Disulfide bridges in NH-2-terminal part of human fibrinogen. !$#cross-references MUID:76225080; PMID:936108 !$#contents variant, and disulfide bonds !$#accession B94309 !'##molecule_type protein !'##residues 20-65,'T',67-629 ##label BLO REFERENCE S19297 !$#authors Dewey, R.S.; Liesch, J.M.; Williams, H.R.; Sugg, E.E.; !1Dolan, C.A.; Davies, P.; Mumford, R.A.; Albers-Schoenberg, !1G. !$#journal Biochem. J. (1992) 281:519-524 !$#title Purification and characterization by fast-atom-bombardment !1mass spectrometry of the !1polymorphonuclear-leucocyte-elastase-generated Aalpha(1-21) !1fragment of fibrinogen from human blood after incubation !1with calcium ionophore A23187. !$#cross-references MUID:92143822; PMID:1736899 !$#accession S19297 !'##molecule_type protein !'##residues 20-40 ##label DEW REFERENCE A60905 !$#authors Retzios, A.D.; Markland Jr., F.S. !$#journal Thromb. Res. (1988) 52:541-552 !$#title A direct-acting fibrinolytic enzyme from the venom of !1Agkistrodon contortrix contortrix: effects on various !1components of the human blood coagulation and fibrinolysis !1systems. !$#cross-references MUID:89162316; PMID:3232124 !$#accession A60905 !'##molecule_type protein !'##residues 433-451 ##label RET REFERENCE A92225 !$#authors Fretto, L.J.; Ferguson, E.W.; Steinman, H.M.; McKee, P.A. !$#journal J. Biol. Chem. (1978) 253:2184-2195 !$#title Localization of the alpha-chain cross-link acceptor sites of !1human fibrin. !$#cross-references MUID:78130085; PMID:632262 !$#contents annotation; cross-linking acceptor sites REFERENCE A90432 !$#authors Cottrell, B.A.; Strong, D.D.; Watt, K.W.K.; Doolittle, R.F. !$#journal Biochemistry (1979) 18:5405-5410 !$#title Amino acid sequence studies on the alpha chain of human !1fibrinogen. Exact location of cross-linking acceptor sites. !$#cross-references MUID:80088230; PMID:518845 !$#contents annotation; cross-linking acceptor sites REFERENCE A90037 !$#authors Henschen, A.; Lottspeich, F.; Kehl, M.; Southan, C. !$#journal Ann. N. Y. Acad. Sci. (1983) 408:28-43 !$#title Covalent structure of fibrinogen. !$#cross-references MUID:83254370; PMID:6575689 !$#contents annotation; review, disulfide bonds REFERENCE A90116 !$#authors Itarte, E.; Plana, M.; Guasch, M.D.; Martos, C. !$#journal Biochem. Biophys. Res. Commun. (1983) 117:631-636 !$#title Phosphorylation of fibrinogen by casein kinase 1. !$#cross-references MUID:84104274; PMID:6318767 !$#contents annotation; phosphorylation !$#note about one-third of alpha chain molecules in blood were found !1to be phosphorylated REFERENCE A90041 !$#authors Doolittle, R.F. !$#journal Annu. Rev. Biochem. (1984) 53:195-229 !$#title Fibrinogen and fibrin. !$#cross-references MUID:84305751; PMID:6383194 !$#contents annotation; review, EM structure, polymerization, ligands REFERENCE A92565 !$#authors Kimura, S.; Aoki, N. !$#journal J. Biol. Chem. (1986) 261:15591-15595 !$#title Cross-linking site in fibrinogen for alpha-2-plasmin !1inhibitor. !$#cross-references MUID:87057190; PMID:2877981 !$#contents annotation; cross-linking site for alpha-2-plasmin inhibitor REFERENCE A33261 !$#authors Krishnamurthi, S.; Dickens, T.A.; Patel, Y.; Wheeler-Jones, !1C.P.D.; Kakkar, V.V. !$#journal Biochem. Biophys. Res. Commun. (1989) 163:1256-1264 !$#title The fibrinogen-derived peptide (RGDS) prevents proteolytic !1degradation of protein kinase C in platelets by inhibiting !1platelet aggregation. !$#cross-references MUID:89392031; PMID:2783136 !$#contents annotation; activity of cell attachment (R-G-D) motif REFERENCE A37117 !$#authors Kirschbaum, N.E.; Budzynski, A.Z. !$#journal J. Biol. Chem. (1990) 265:13669-13676 !$#title A unique proteolytic fragment of human fibrinogen containing !1the Aalpha COOH-terminal domain of the native molecule. !$#cross-references MUID:90337977; PMID:2143188 !$#contents annotation; hementin cleavage site !$#note hementin, a protease from Haementeria ghilianii, the giant !1South American leech, cleaves fibrinogen alpha chain between !1Asn-121 and Asn-122 REFERENCE JC4334 !$#authors Staendker, L.; Sillard, R.; Bensch, K.W.; Ruf, A.; Raida, !1M.; Schulz-Knappe, P.; Schepky, A.G.; Patscheke, H.; !1Forssmann, W.G. !$#journal Biochem. Biophys. Res. Commun. (1995) 215:896-902 !$#title In vivo degradation of human fibrinogen A alpha: Detection !1of cleavage sites and release of antithrombotic peptides. !$#cross-references MUID:96027996; PMID:7488058 !$#contents annotation; composition and amino-terminal sequences of !1carboxyl end peptides found in blood filtrate and produced !1by natural degradation COMMENT Unlike the beta and gamma chains, the alpha chain is not !1glycosylated. COMMENT The alpha chain binds by 2-4 cross-links to the amino end of !1fibronectin. COMMENT The conversion of fibrinogen to fibrin is triggered by !1thrombin, which cleaves fibrinopeptides A and B from alpha !1and beta chains, respectively, and thus exposes the !1amino-terminal polymerization sites responsible for the !1formation of the soft clot. COMMENT The soft clot is converted into the hard clot by factor !1XIIIa (fibrin-stabilizing factor, FSF), which catalyzes the !1epsilon-(gamma-glutamyl)lysine cross-linking between gamma !1chains (stronger) and between alpha chains (weaker) of !1different monomers. COMMENT All fibrinogen chains are synthesized in the liver. COMMENT See PIR:D44234 for the minor alternative splice form. GENETICS !$#gene GDB:FGA !'##cross-references GDB:119129; OMIM:134820 !$#map_position 4q28-4q28 !$#introns 18/3; 60/3; 122/1; 171/2 !$#note the list of introns is incomplete COMPLEX The fibrinogen molecule is a hexamer containing two sets of !1alpha, beta (see PIR:FGHUB) and gamma (see PIR:FGHUG) !1chains, linked to each other by disulfide bonds. The amino !1ends of all chains are contained in the core. Two !1three-chain coiled coils emerge from this core and connect !1it to nodes containing the distal domains. The long carboxyl !1ends of the alpha chains extend peripherally from the distal !1domain nodes. FUNCTION !$#description fibrinogen cleaved by thrombin yields monomers that are !1polymerized into fibrin, and act as a cofactor in platelet !1aggregation !$#pathway blood coagulation CLASSIFICATION #superfamily fibrinogen alpha chain; fibrinogen disulfide !1ring homology KEYWORDS alternative splicing; blood coagulation; coiled coil; !1glycoprotein; liver; phosphoprotein; plasma FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-629 #product fibrinogen alpha chain #status experimental !8#label MAT\ !$20-35 #product fibrinopeptide A #status experimental #label !8APT\ !$36-629 #product fibrin alpha chain #status experimental !8#label FGA\ !$36-38 #region polymerization site, binding to the distal !8domain of the gamma chain of another fibrin monomer\ !$57-185 #domain fibrinogen disulfide ring homology #label !8FDR\ !$591-593 #region cell attachment (R-G-D) motif\ !$22,460 #binding_site phosphate (Ser) (covalent) #status !8experimental\ !$35-36 #cleavage_site Arg-Gly (thrombin) #status !8experimental\ !$47 #disulfide_bonds interchain (to alpha-47) #status !8experimental\ !$55 #disulfide_bonds interchain (to beta-95) #status !8experimental\ !$64 #disulfide_bonds interchain (to gamma-49) #status !8experimental\ !$68 #disulfide_bonds interchain (to beta-106) #status !8experimental\ !$180 #disulfide_bonds interchain (to gamma-165) #status !8experimental\ !$184 #disulfide_bonds interchain (to beta-223) #status !8experimental\ !$288,419 #binding_site carbohydrate (Asn) (covalent) #status !8absent\ !$322 #cross-link isopeptide (Lys) (interchain to Gln-41 of !8alpha-2-plasmin inhibitor) #status experimental\ !$347,385 #cross-link isopeptide (Gln) (interchain to Lys !8N6-amino of alpha) #status experimental\ !$461-491 #disulfide_bonds #status experimental\ !$527,558,575,581,599 #cross-link isopeptide (Lys) (interchain to Gln of !8alpha) #status predicted SUMMARY #length 644 #molecular-weight 69756 #checksum 7640 SEQUENCE /// ENTRY FGRTA #type complete TITLE fibrinogen alpha chain precursor - rat CONTAINS fibrinopeptide A ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 25-Oct-1996 ACCESSIONS A92915; B03118; A03119 REFERENCE A92915 !$#authors Crabtree, G.R.; Comeau, C.M.; Fowlkes, D.M.; Fornace Jr., !1A.J.; Malley, J.D.; Kant, J.A. !$#journal J. Mol. Biol. (1985) 185:1-19 !$#title Evolution and structure of the fibrinogen genes. Random !1insertion of introns or selective loss? !$#cross-references MUID:86011580; PMID:4046033 !$#accession A92915 !'##molecule_type DNA !'##residues 1-550 ##label CRA REFERENCE A03118 !$#authors Blombaeck, B.; Blombaeck, M.; Groendahl, N.J. !$#journal Acta Chem. Scand. (1965) 19:1789-1791 !$#title Studies on fibrinopeptides from mammals. !$#accession B03118 !'##molecule_type protein !'##residues 20-29 ##label BLO COMMENT Unlike the beta and gamma chains, the alpha chain is not !1glycosylated. COMMENT Fibrinogen chains are synthesized in the liver. GENETICS !$#introns 18/3; 61/3; 123/1; 171/3 CLASSIFICATION #superfamily fibrinogen alpha chain; fibrinogen disulfide !1ring homology KEYWORDS blood coagulation; liver; plasma; platelet FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-36 #product fibrinopeptide A #status experimental #label !8APT\ !$37-550 #product fibrinogen alpha chain #status predicted !8#label MPT\ !$58-186 #domain fibrinogen disulfide ring homology #label !8FDR\ !$48 #disulfide_bonds interchain (to alpha-48) #status !8predicted\ !$56,69,185 #disulfide_bonds interchain (to beta chain) #status !8predicted\ !$65 #disulfide_bonds interchain (to gamma-49) #status !8predicted\ !$181 #disulfide_bonds interchain (to gamma-165) #status !8predicted\ !$404-434 #disulfide_bonds #status predicted SUMMARY #length 550 #molecular-weight 60682 #checksum 4997 SEQUENCE /// ENTRY A41932 #type complete TITLE fibrinogen alpha-II chain precursor - sea lamprey ORGANISM #formal_name Petromyzon marinus #common_name sea lamprey DATE 31-Dec-1993 #sequence_revision 26-Jan-1996 #text_change 19-Feb-1999 ACCESSIONS A41932; S27940 REFERENCE A41932 !$#authors Pan, Y.; Doolittle, R.F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:2066-2070 !$#title cDNA sequence of a second fibrinogen alpha chain in lamprey: !1an archetypal version alignable with full-length beta and !1gamma chains. !$#cross-references MUID:92196058; PMID:1549566 !$#accession A41932 !'##molecule_type mRNA !'##residues 1-641 ##label PAN !'##cross-references EMBL:M84565 !'##experimental_source liver !'##note this sequence is inconsistent with the nucleotide translation !'##note sequence extracted from NCBI backbone (NCBIN:87920, !1NCBIP:87922) CLASSIFICATION #superfamily lamprey fibrinogen alpha-II chain; fibrinogen !1beta/gamma homology; fibrinogen disulfide ring homology KEYWORDS blood coagulation; liver; plasma FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-641 #product fibrinogen alpha-2 chain #status predicted !8#label MAT\ !$56-184 #domain fibrinogen disulfide ring homology #label !8FDR\ !$401-635 #domain fibrinogen beta/gamma homology #label FBG\ !$404-435,571-584 #disulfide_bonds #status predicted SUMMARY #length 641 #molecular-weight 70770 #checksum 5993 SEQUENCE /// ENTRY FGHUB #type complete TITLE fibrinogen beta chain precursor [validated] - human ALTERNATE_NAMES coagulation factor I CONTAINS fibrinopeptide B ORGANISM #formal_name Homo sapiens #common_name man DATE 24-Apr-1984 #sequence_revision 31-Mar-1993 #text_change 08-Dec-2000 ACCESSIONS B43568; A90469; B90469; I37389; A94433; A90437; A94309; !1G54223; A03121; B37117 REFERENCE A43568 !$#authors Chung, D.W.; Harris, J.E.; Davie, E.W. !$#journal Adv. Exp. Med. Biol. (1990) 281:39-48 !$#title Nucleotide sequences of the three genes coding for human !1fibrinogen. !$#cross-references MUID:91344740; PMID:2102623 !$#accession B43568 !'##molecule_type DNA !'##residues 9-191,'P',193-491 ##label CHU REFERENCE A90469 !$#authors Chung, D.W.; Que, B.G.; Rixon, M.W.; Mace Jr., M.; Davie, !1E.W. !$#journal Biochemistry (1983) 22:3244-3250 !$#title Characterization of complementary deoxyribonucleic acid and !1genomic deoxyribonucleic acid for the beta chain of human !1fibrinogen. !$#cross-references MUID:83283433; PMID:6688356 !$#accession A90469 !'##molecule_type DNA !'##residues 1-38 ##label CH1 !$#accession B90469 !'##molecule_type mRNA !'##residues 9-191,'A',193-491 ##label CH2 !'##cross-references GB:J00129; NID:g182429; PIDN:AAA52429.1; !1PID:g182430 REFERENCE I37389 !$#authors Huber, P.; Dalmon, J.; Courtois, G.; Laurent, M.; Assouline, !1Z.; Marguerie, G. !$#journal Nucleic Acids Res. (1987) 15:1615-1625 !$#title Characterization of the 5'-flanking region for the human !1fibrinogen beta gene. !$#cross-references MUID:87146483; PMID:3029722 !$#accession I37389 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-38 ##label HUB !'##cross-references EMBL:X05018; NID:g31400; PIDN:CAA28674.1; !1PID:g31401 REFERENCE A94433 !$#authors Henschen, A.; Lottspeich, F.; Southan, C.; Topfer-Petersen, !1E. !$#book Protides of the Biological Fluids, Proc. 28th Colloq., !1Peeters, H., ed., pp.51-56, Pergamon Press, Oxford, 1980 !$#title Human fibrinogen: sequence, sulfur bridges, glycosylation !1and some structural variants. !$#contents carbohydrate binding !$#accession A94433 !'##molecule_type protein !'##residues 31-137,'QS',140-144,'QF',147-491 ##label HEN REFERENCE A90437 !$#authors Watt, K.W.K.; Takagi, T.; Doolittle, R.F. !$#journal Biochemistry (1979) 18:68-76 !$#title Amino acid sequence of the beta chain of human fibrinogen. !$#cross-references MUID:79124640; PMID:420779 !$#accession A90437 !'##molecule_type protein !'##residues 31-144,'QF',147-231,'D',233-330,'E',332-491 ##label WAT REFERENCE A94309 !$#authors Blomback, B.; Hessel, B.; Hogg, D. !$#journal Thromb. Res. (1976) 8:639-658 !$#title Disulfide bridges in NH-2-terminal part of human fibrinogen. !$#cross-references MUID:76225080; PMID:936108 !$#contents disulfide bonds !$#accession A94309 !'##molecule_type protein !'##residues 31-112,'E',114-137,'QS',140-144,'QF',147-148 ##label BLO REFERENCE A54223 !$#authors Kunitake, S.T.; Carilli, C.T.; Lau, K.; Protter, A.A.; !1Naya-Vigne, J.; Kane, J.P. !$#journal Biochemistry (1994) 33:1988-1993 !$#title Identification of proteins associated with apolipoprotein !1A-I-containing lipoproteins purified by selected-affinity !1immunosorption. !$#cross-references MUID:94162201; PMID:8117655 !$#accession G54223 !'##molecule_type protein !'##residues 164-174 ##label KUN !'##note identification of tryptic peptides from high-density !1lipoproteins REFERENCE A90037 !$#authors Henschen, A.; Lottspeich, F.; Kehl, M.; Southan, C. !$#journal Ann. N. Y. Acad. Sci. (1983) 408:28-43 !$#title Covalent structure of fibrinogen. !$#cross-references MUID:83254370; PMID:6575689 !$#contents annotation; review, disulfide bonds REFERENCE A91249 !$#authors Gardlund, B.; Hessel, B.; Marguerie, G.; Murano, G.; !1Blomback, B. !$#journal Eur. J. Biochem. (1977) 77:595-610 !$#title Primary structure of human fibrinogen. Characterization of !1disulfide-containing cyanogen-bromide fragments. !$#cross-references MUID:77245999; PMID:891553 !$#contents annotation; disulfide bonds REFERENCE A94437 !$#authors Doolittle, R.F.; Takagi, T.; Watt, K.; Bouma III, H.; !1Cottrell, B.A.; Cassman, K.G.; Goldbaum, D.M.; Doolittle, !1L.R.; Friezner, S.J. !$#book Regulatory Proteolytic Enzymes and Their Inhibitors, !1Magnusson, S., Ottesen, M., Foltmann, B., Dano, K., and !1Neurath, H., eds., pp.163-172, Pergamon Press, Oxford, New !1York, 1978 !$#title The structures of fibrinogen and fibrin. !$#contents annotation; disulfide bonds REFERENCE A90041 !$#authors Doolittle, R.F. !$#journal Annu. Rev. Biochem. (1984) 53:195-229 !$#title Fibrinogen and fibrin. !$#cross-references MUID:84305751; PMID:6383194 !$#contents annotation; review, EM structure, polymerization, ligands REFERENCE A90038 !$#authors Chung, D.W.; Rixon, M.W.; Que, B.G.; Davie, E.W. !$#journal Ann. N. Y. Acad. Sci. (1983) 408:449-456 !$#title Cloning of fibrinogen genes and their cDNA. !$#cross-references MUID:83254384; PMID:6575700 !$#contents annotation REFERENCE A37117 !$#authors Kirschbaum, N.E.; Budzynski, A.Z. !$#journal J. Biol. Chem. (1990) 265:13669-13676 !$#title A unique proteolytic fragment of human fibrinogen containing !1the Aalpha COOH-terminal domain of the native molecule. !$#cross-references MUID:90337977; PMID:2143188 !$#contents annotation; hementin cleavage site !$#note hementin, a protease from Haementeria ghilianii, the giant !1South American leech, cleaves fibrinogen alpha chain between !1Asn-121 and Asn-122 COMMENT The conversion of fibrinogen to fibrin is triggered by !1thrombin, which cleaves fibrinopeptides A and B from alpha !1and beta chains, respectively, and thus exposes the !1amino-terminal polymerization sites responsible for the !1formation of the soft clot. COMMENT The soft clot is converted into the hard clot by factor !1XIIIa (fibrin-stabilizing factor, FSF), which catalyzes the !1epsilon-(gamma-glutamyl)lysine cross-linking between gamma !1chains (stronger) and between alpha chains (weaker) of !1different monomers. COMMENT All fibrinogen chains are synthesized in the liver. GENETICS !$#gene GDB:FGB !'##cross-references GDB:119130; OMIM:134830 !$#map_position 4q28-4q28 !$#introns 38/3; 102/3; 164/1; 240/1; 278/1; 320/1; 415/2 COMPLEX The fibrinogen molecule is a hexamer containing two sets of !1alpha (see PIR:FGHUA), beta and gamma (see PIR:FGHUG) !1chains, linked to each other by disulfide bonds. The amino !1ends of all chains are contained in the core. Two !1three-chain coiled coils emerge from this core and connect !1it to nodes containing the distal domains. The long carboxyl !1ends of the alpha chains extend peripherally from the distal !1domain nodes. FUNCTION !$#description fibrinogen cleaved by thrombin yields monomers that are !1polymerized into fibrin, and act as a cofactor in platelet !1aggregation !$#pathway blood coagulation CLASSIFICATION #superfamily fibrinogen beta chain; fibrinogen beta/gamma !1homology; fibrinogen disulfide ring homology KEYWORDS blood coagulation; coiled coil; glycoprotein; liver; plasma; !1pyroglutamic acid FEATURE !$1-30 #domain (or 4-30 or 15-30) signal sequence #status !8predicted #label SIG\ !$31-491 #product fibrinogen beta chain #status experimental !8#label MAT\ !$31-44 #product fibrinopeptide B #status experimental #label !8APT\ !$45-491 #product fibrin beta chain #status experimental !8#label FGB\ !$45-47 #region polymerization site\ !$99-228 #domain fibrinogen disulfide ring homology #label !8FDR\ !$238-487 #domain fibrinogen beta/gamma homology #label FBG\ !$31 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$44-45 #cleavage_site Arg-Gly (thrombin) #status !8experimental\ !$95 #disulfide_bonds interchain (to alpha-55) #status !8experimental\ !$106 #disulfide_bonds interchain (to alpha-68) #status !8experimental\ !$110 #disulfide_bonds interchain (to gamma-45) #status !8experimental\ !$223 #disulfide_bonds interchain (to alpha-184) #status !8experimental\ !$227 #disulfide_bonds interchain (to gamma-161) #status !8experimental\ !$231-316,241-270, !$424-437 #disulfide_bonds #status experimental\ !$394 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 491 #molecular-weight 55928 #checksum 4634 SEQUENCE /// ENTRY FGBOB #type complete TITLE fibrinogen beta chain - bovine CONTAINS fibrinopeptide B ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 29-Jul-1981 #sequence_revision 29-Jul-1981 #text_change 13-Sep-1996 ACCESSIONS A03122; B03117; B37507; A37513; S02443 REFERENCE A03122 !$#authors Blomback, B.; Doolittle, R.F. !$#journal Acta Chem. Scand. (1963) 17:1816-1819 !$#title The sequence of amino acids at the N-terminal end of bovine !1fibrinopeptide B. !$#accession A03122 !'##molecule_type protein !'##residues 1-4 ##label BLO REFERENCE A03117 !$#authors Sjoquist, J.; Blomback, B.; Wallen, P. !$#journal Ark. Kemi (1960) 16:425-436 !$#title Amino acid sequence of bovine fibrinopeptides. !$#accession B03117 !'##molecule_type protein !'##residues 5-21 ##label SJO REFERENCE A37507 !$#authors Martinelli, R.A.; Inglis, A.S.; Rubira, M.R.; Hageman, T.C.; !1Hurrell, J.G.R.; Leach, S.J.; Scheraga, H.A. !$#journal Arch. Biochem. Biophys. (1979) 192:27-32 !$#title Amino acid sequences of portions of the alpha and beta !1chains of bovine fibrinogen. !$#cross-references MUID:79164394; PMID:434821 !$#accession B37507 !'##molecule_type protein !'##residues 22-53 ##label MAR REFERENCE A37513 !$#authors Chung, D.W.; Rixon, M.W.; MacGillivray, R.T.A.; Davie, E.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:1466-1470 !$#title Characterization of a cDNA clone coding for the beta chain !1of bovine fibrinogen. !$#cross-references MUID:81199473; PMID:6262803 !$#accession A37513 !'##molecule_type mRNA !'##residues 44-468 ##label CHU REFERENCE S02443 !$#authors Medved, L.V.; Platonova, T.N.; Litvinovich, S.V.; Lukinova, !1N.I. !$#journal FEBS Lett. (1988) 232:56-60 !$#title The cleavage of beta-chain in bovine fibrinogen D(H) !1fragment (95 kDa) leads to a significant increase in its !1anticlotting activity. !$#cross-references MUID:88211875; PMID:2966748 !$#accession S02443 !'##molecule_type protein !'##residues 373-374 ##label MED COMMENT Thrombin cleaves the bond between Arg-21 and Gly-22 to !1release fibrinopeptide B. COMMENT Fibrinogen is a hexamer containing two sets of three !1nonidentical chains (alpha, beta, and gamma) linked by !1several disulfide bonds. CLASSIFICATION #superfamily fibrinogen beta chain; fibrinogen beta/gamma !1homology; fibrinogen disulfide ring homology KEYWORDS blood coagulation; glycoprotein; plasma; pyroglutamic acid; !1sulfoprotein FEATURE !$76-205 #domain fibrinogen disulfide ring homology #label !8FDR\ !$215-464 #domain fibrinogen beta/gamma homology #label FBG\ !$1 #modified_site pyrrolidone carboxylic acid (Gln) !8#status experimental\ !$6 #binding_site sulfate (Tyr) (covalent) #status !8experimental\ !$21-22 #cleavage_site Arg-Gly (thrombin) #status !8experimental\ !$371 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$372-373 #cleavage_site Arg-Thr (plasmin) #status experimental SUMMARY #length 468 #molecular-weight 53354 #checksum 4309 SEQUENCE /// ENTRY FGHUG #type complete TITLE fibrinogen gamma-A chain precursor [validated] - human ALTERNATE_NAMES coagulation factor I ORGANISM #formal_name Homo sapiens #common_name man DATE 24-Apr-1984 #sequence_revision 25-Feb-1985 #text_change 08-Dec-2000 ACCESSIONS A90470; B90494; C94433; B93956; B92448; I37393; A40698; !1H54223; A03125; C37117 REFERENCE A90470 !$#authors Chung, D.W.; Chan, W.Y.; Davie, E.W. !$#journal Biochemistry (1983) 22:3250-3256 !$#title Characterization of a complementary deoxyribonucleic acid !1coding for the gamma chain of human fibrinogen. !$#cross-references MUID:83283434; PMID:6688357 !$#accession A90470 !'##molecule_type mRNA !'##residues 1-437 ##label CHU REFERENCE A90494 !$#authors Rixon, M.W.; Chung, D.W.; Davie, E.W. !$#journal Biochemistry (1985) 24:2077-2086 !$#title Nucleotide sequence of the gene for the gamma chain of human !1fibrinogen. !$#cross-references MUID:85252774; PMID:2990550 !$#accession B90494 !'##molecule_type DNA !'##residues 1-113,'I',115-437 ##label RIX !'##cross-references GB:X02415; GB:M10014; NID:g182438; PIDN:AAB59531.1; !1PID:g182439 REFERENCE A94433 !$#authors Henschen, A.; Lottspeich, F.; Southan, C.; Topfer-Petersen, !1E. !$#book Protides of the Biological Fluids, Proc. 28th Colloq., !1Peeters, H., ed., pp.51-56, Pergamon Press, Oxford, 1980 !$#title Human fibrinogen: sequence, sulfur bridges, glycosylation !1and some structural variants. !$#accession C94433 !'##molecule_type protein !'##residues 27-437 ##label HEN REFERENCE A93956 !$#authors Kant, J.A.; Lord, S.T.; Crabtree, G.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:3953-3957 !$#title Partial mRNA sequences for human Aalpha, Bbeta, and gamma !1fibrinogen chains: evolutionary and functional implications. !$#cross-references MUID:83247396; PMID:6575389 !$#accession B93956 !'##molecule_type mRNA !'##residues 276-437 ##label KAN REFERENCE A92448 !$#authors Fornace Jr., A.J.; Cummings, D.E.; Comeau, C.M.; Kant, J.A.; !1Crabtree, G.R. !$#journal J. Biol. Chem. (1984) 259:12826-12830 !$#title Structure of the human gamma-fibrinogen gene. Alternate mRNA !1splicing near the 3' end of the gene produces gammaA and !1gammaB forms of gamma-fibrinogen. !$#cross-references MUID:85030379; PMID:6092346 !$#accession B92448 !'##molecule_type DNA !'##residues 286-437 ##label FOR REFERENCE I37393 !$#authors Imam, A.M.A.; Eaton, M.A.W.; Williamson, R.; Humphries, S. !$#journal Nucleic Acids Res. (1983) 11:7427-7434 !$#title Isolation and characterisation of cDNA clones for the !1Aalpha- and gamma-chains of human fibrinogen. !$#cross-references MUID:84069777; PMID:6689067 !$#accession I37393 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 209-270 ##label RES !'##cross-references EMBL:X00086; NID:g31445; PIDN:CAA24944.1; !1PID:g577055 REFERENCE A40698 !$#authors Bertagnolli, M.E.; Beckerle, M.C. !$#journal J. Cell Biol. (1993) 121:1329-1342 !$#title Evidence for the selective association of a subpopulation of !1GPIIb-IIIa with the actin cytoskeletons of !1thrombin-activated platelets. !$#cross-references MUID:93286185; PMID:8509453 !$#accession A40698 !'##molecule_type protein !'##residues 27-33,'XX',36-41 ##label BER !'##experimental_source thrombin-activated platelets !'##note sequence extracted from NCBI backbone (NCBIP:133734) REFERENCE A54223 !$#authors Kunitake, S.T.; Carilli, C.T.; Lau, K.; Protter, A.A.; !1Naya-Vigne, J.; Kane, J.P. !$#journal Biochemistry (1994) 33:1988-1993 !$#title Identification of proteins associated with apolipoprotein !1A-I-containing lipoproteins purified by selected-affinity !1immunosorption. !$#cross-references MUID:94162201; PMID:8117655 !$#accession H54223 !'##molecule_type protein !'##residues 27-33,'XX',36-41 ##label KUN !'##note identification of tryptic peptides from high-density !1lipoproteins REFERENCE A90037 !$#authors Henschen, A.; Lottspeich, F.; Kehl, M.; Southan, C. !$#journal Ann. N. Y. Acad. Sci. (1983) 408:28-43 !$#title Covalent structure of fibrinogen. !$#cross-references MUID:83254370; PMID:6575689 !$#contents annotation; review, disulfide bonds REFERENCE A94437 !$#authors Doolittle, R.F.; Takagi, T.; Watt, K.; Bouma III, H.; !1Cottrell, B.A.; Cassman, K.G.; Goldbaum, D.M.; Doolittle, !1L.R.; Friezner, S.J. !$#book Regulatory Proteolytic Enzymes and Their Inhibitors, !1Magnusson, S., Ottesen, M., Foltmann, B., Dano, K., and !1Neurath, H., eds., pp.163-172, Pergamon Press, Oxford, New !1York, 1978 !$#title The structures of fibrinogen and fibrin. !$#contents annotation; disulfide bonds REFERENCE A94309 !$#authors Blomback, B.; Hessel, B.; Hogg, D. !$#journal Thromb. Res. (1976) 8:639-658 !$#title Disulfide bridges in NH-2-terminal part of human fibrinogen. !$#cross-references MUID:76225080; PMID:936108 !$#contents annotation; disulfide bonds REFERENCE A90467 !$#authors Hoeprich, P.D.; Doolittle, R.F. !$#journal Biochemistry (1983) 22:2049-2055 !$#title Dimeric half-molecules of human fibrinogen are joined !1through disulfide bonds in an antiparallel orientation. !$#cross-references MUID:83231465; PMID:6860649 !$#contents annotation; quaternary structure, disulfide bonds REFERENCE A90041 !$#authors Doolittle, R.F. !$#journal Annu. Rev. Biochem. (1984) 53:195-229 !$#title Fibrinogen and fibrin. !$#cross-references MUID:84305751; PMID:6383194 !$#contents annotation; review, EM structure, polymerization, ligands REFERENCE A94006 !$#authors Horwitz, B.H.; Varadi, A.; Scheraga, H.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:5980-5984 !$#title Localization of a fibrin gamma-chain polymerization site !1within segment Thr-374 to Glu-396 of human fibrinogen. !$#cross-references MUID:85014892; PMID:6592597 !$#contents annotation; polymerization region REFERENCE A90483 !$#authors Kloczewiak, M.; Timmons, S.; Lukas, T.J.; Hawiger, J. !$#journal Biochemistry (1984) 23:1767-1774 !$#title Platelet receptor recognition site on human fibrinogen. !1Synthesis and structure-function relationship of peptides !1corresponding to the carboxy-terminal segment of the gamma !1chain. !$#cross-references MUID:84203545; PMID:6326808 !$#contents annotation; platelet aggregation region REFERENCE A92477 !$#authors Plow, E.F.; Srouji, A.H.; Meyer, D.; Marguerie, G.; !1Ginsberg, M.H. !$#journal J. Biol. Chem. (1984) 259:5388-5391 !$#title Evidence that three adhesive proteins interact with a common !1recognition site on activated platelets. !$#cross-references MUID:84185664; PMID:6325435 !$#contents annotation; platelet aggregation region REFERENCE A92549 !$#authors Dang, C.V.; Ebert, R.F.; Bell, W.R. !$#journal J. Biol. Chem. (1985) 260:9713-9719 !$#title Localization of a fibrinogen calcium binding site between !1gamma-subunit positions 311 and 336 by terbium fluorescence. !$#cross-references MUID:85261382; PMID:3160702 !$#contents annotation; calcium binding region REFERENCE A37117 !$#authors Kirschbaum, N.E.; Budzynski, A.Z. !$#journal J. Biol. Chem. (1990) 265:13669-13676 !$#title A unique proteolytic fragment of human fibrinogen containing !1the Aalpha COOH-terminal domain of the native molecule. !$#cross-references MUID:90337977; PMID:2143188 !$#contents annotation; hementin cleavage site !$#note hementin, a protease from Haementeria ghilianii, the giant !1South American leech, cleaves fibrinogen alpha chain between !1Asn-121 and Asn-122 COMMENT The conversion of fibrinogen to fibrin is triggered by !1thrombin, which cleaves fibrinopeptides A and B from alpha !1and beta chains, respectively, and thus exposes the !1amino-terminal polymerization sites responsible for the !1formation of the soft clot. COMMENT The soft clot is converted into the hard clot by factor !1XIIIa (fibrin-stabilizing factor, FSF), which catalyzes the !1epsilon-(gamma-glutamyl)lysine cross-linking between gamma !1chains (stronger) and between alpha chains (weaker) of !1different monomers. COMMENT All fibrinogen chains are synthesized in the liver. COMMENT The two forms of gamma chain, A and B (see PIR:FGHUGB), !1arise by alternate splicing of the mRNA coded by the FGG !1gene. The gamma-A chain arises by the splicing out of one !1more 3'-terminal intron, which makes this chain different !1from the gamma-B chain at positions 434-437 and shorter by !116 residues at the carboxyl end. GENETICS !$#gene GDB:FGG !'##cross-references GDB:119132; OMIM:134850 !$#map_position 4q28-4q28 !$#introns 26/3; 41/3; 103/1; 134/2; 178/1; 222/3; 284/2; 377/1; 433/3 COMPLEX The fibrinogen molecule is a hexamer containing two sets of !1alpha (see PIR:FGHUA), beta (see PIR:FGHUB) and gamma !1chains, linked to each other by disulfide bonds. The amino !1ends of all chains are contained in the core. Two !1three-chain coiled coils emerge from this core and connect !1it to nodes containing the distal domains. The long carboxyl !1ends of the alpha chains extend peripherally from the distal !1domain nodes. FUNCTION !$#description fibrinogen cleaved by thrombin yields monomers that are !1polymerized into fibrin, and act as a cofactor in platelet !1aggregation !$#pathway blood coagulation CLASSIFICATION #superfamily fibrinogen gamma chain; fibrinogen beta/gamma !1homology KEYWORDS alternative splicing; blood coagulation; calcium; coiled !1coil; glycoprotein; liver; plasma; platelet aggregation FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-437 #product fibrinogen gamma-A chain #status !8experimental #label MPT\ !$176-415 #domain fibrinogen beta/gamma homology #label FBG\ !$341-355 #domain calcium binding #status predicted #label CAB\ !$400-422 #region polymerization site, binding to the amino end !8of the alpha chain of another fibrin monomer\ !$423-437 #region platelet aggregation #status predicted\ !$34 #disulfide_bonds interchain (to gamma-35) #status !8experimental\ !$35 #disulfide_bonds interchain (to gamma-34) #status !8experimental\ !$45 #disulfide_bonds interchain (to beta-110) #status !8experimental\ !$49 #disulfide_bonds interchain (to alpha-64) #status !8experimental\ !$78 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$161 #disulfide_bonds interchain (to beta-227) #status !8experimental\ !$165 #disulfide_bonds interchain (to alpha-180) #status !8experimental\ !$179-208,352-365 #disulfide_bonds #status experimental\ !$424 #cross-link isopeptide (Gln) (interchain to Lys-432 !8N6-amino) #status experimental\ !$432 #cross-link isopeptide (Lys) (interchain to Gln-424) !8#status experimental SUMMARY #length 437 #molecular-weight 49496 #checksum 7688 SEQUENCE /// ENTRY FGHUGB #type complete TITLE fibrinogen gamma-B chain precursor [validated] - human ALTERNATE_NAMES coagulation factor I; fibrinogen gamma-55 chain ORGANISM #formal_name Homo sapiens #common_name man DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 08-Dec-2000 ACCESSIONS A90494; A92448; A90453; A28203; B28203; I37390; A03126 REFERENCE A90494 !$#authors Rixon, M.W.; Chung, D.W.; Davie, E.W. !$#journal Biochemistry (1985) 24:2077-2086 !$#title Nucleotide sequence of the gene for the gamma chain of human !1fibrinogen. !$#cross-references MUID:85252774; PMID:2990550 !$#accession A90494 !'##molecule_type DNA !'##residues 1-113,'I',115-453 ##label RIX !'##cross-references GB:M10014; GB:J00134; GB:J00135; GB:X00086; !1NID:g182438; PIDN:AAB59530.1; PID:g182440 REFERENCE A92448 !$#authors Fornace Jr., A.J.; Cummings, D.E.; Comeau, C.M.; Kant, J.A.; !1Crabtree, G.R. !$#journal J. Biol. Chem. (1984) 259:12826-12830 !$#title Structure of the human gamma-fibrinogen gene. Alternate mRNA !1splicing near the 3' end of the gene produces gammaA and !1gammaB forms of gamma-fibrinogen. !$#cross-references MUID:85030379; PMID:6092346 !$#accession A92448 !'##molecule_type DNA !'##residues 286-453 ##label FOR REFERENCE A90453 !$#authors Wolfenstein-Todel, C.; Mosesson, M.W. !$#journal Biochemistry (1981) 20:6146-6149 !$#title Carboxy-terminal amino acid sequence of a human fibrinogen !1gamma-chain variant (gamma'). !$#cross-references MUID:82068993; PMID:7306501 !$#accession A90453 !'##molecule_type protein !'##residues 411-434,'Y',436-440,'Z',442,'Z',444,'B',446-447,'R',449, !1'ZBB',453 ##label WOL REFERENCE A94194 !$#authors Francis, C.W.; Mueller, E.; Henschen, A.; Simpson, P.J.; !1Marder, V.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:3358-3362 !$#title Carboxyl-terminal amino acid sequences of two variant forms !1of the gamma-chain of human plasma fibrinogen. !$#cross-references MUID:88217900; PMID:3368448 !$#accession A28203 !'##molecule_type protein !'##residues 433-449 ##label FRA !$#accession B28203 !'##molecule_type protein !'##residues 433-453 ##label FR2 REFERENCE I37390 !$#authors Marchetti, L.; Zanelli, T.; Malcovati, M.; Tenchini, M.L. !$#journal DNA Seq. (1991) 1:419-422 !$#title Polymorphism of the human gamma chain fibrinogen gene. !$#cross-references MUID:92119334; PMID:1685103 !$#accession I37390 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 75-286 ##label RES !'##cross-references EMBL:X51473; NID:g31410; PIDN:CAA35837.1; !1PID:g930064 COMMENT The two forms of gamma chain, A (see PIR:FGHUG) and B, arise !1by alternate splicing of the mRNA coded by the FGG gene. The !1gamma-A chain arises by the splicing out of one less !13'-terminal intron, which makes this chain different from !1the gamma-B chain at positions 434-437 and longer by 16 !1residues at the carboxyl end. COMMENT The gamma-B chain is present in about 10% of the fibrinogen !1molecules in plasma but absent from those in the platelets. GENETICS !$#gene GDB:FGG !'##cross-references GDB:119132; OMIM:134850 !$#map_position 4q28-4q28 !$#introns 26/3; 41/3; 103/1; 134/2; 178/1; 222/3; 284/2; 377/1 COMPLEX The fibrinogen molecule is a hexamer containing two sets of !1alpha (see PIR:FGHUA), beta (see PIR:FGHUB) and gamma !1chains, linked to each other by disulfide bonds. The amino !1ends of all chains are contained in the core. Two !1three-chain coiled coils emerge from this core and connect !1it to nodes containing the distal domains. The long carboxyl !1ends of the alpha chains extend peripherally from the distal !1domain nodes. FUNCTION !$#description fibrinogen cleaved by thrombin yields monomers that are !1polymerized into fibrin, and act as a cofactor in platelet !1aggregation !$#pathway blood coagulation CLASSIFICATION #superfamily fibrinogen gamma chain; fibrinogen beta/gamma !1homology KEYWORDS alternative splicing; blood coagulation; calcium; coiled !1coil; glycoprotein; liver; plasma; platelet aggregation FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-453 #product fibrinogen gamma-B chain #status !8experimental #label MPT\ !$176-415 #domain fibrinogen beta/gamma homology #label FBG\ !$341-355 #domain calcium binding #status predicted #label CAB\ !$400-422 #region polymerization site, binding to the amino end !8of the alpha chain of another fibrin monomer\ !$34 #disulfide_bonds interchain (to gamma-35) #status !8predicted\ !$35 #disulfide_bonds interchain (to gamma-34) #status !8predicted\ !$45 #disulfide_bonds interchain (to beta-110) #status !8predicted\ !$49 #disulfide_bonds interchain (to alpha-64) #status !8predicted\ !$78 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$161 #disulfide_bonds interchain (to beta-227) #status !8predicted\ !$165 #disulfide_bonds interchain (to alpha-180) #status !8predicted\ !$179-208,352-365 #disulfide_bonds #status predicted\ !$424 #cross-link isopeptide (Gln) (interchain to Lys-432 !8N6-amino) #status predicted\ !$432 #cross-link isopeptide (Lys) (interchain to Gln-424) !8#status predicted SUMMARY #length 453 #molecular-weight 51511 #checksum 4642 SEQUENCE /// ENTRY FGRTGA #type complete TITLE fibrinogen gamma-A chain precursor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 22-Jun-1999 ACCESSIONS A90828; A93989; A03127 REFERENCE A90828 !$#authors Crabtree, G.R.; Kant, J.A. !$#journal Cell (1982) 31:159-166 !$#title Organization of the rat gamma-fibrinogen gene: alternative !1mRNA splice patterns produce the gammaA and gammaB (gamma') !1chains of fibrinogen. !$#cross-references MUID:83129318; PMID:6897622 !$#accession A90828 !'##molecule_type mRNA !'##residues 1-437 ##label CRA REFERENCE A93989 !$#authors Fowlkes, D.M.; Mullis, N.T.; Comeau, C.M.; Crabtree, G.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:2313-2316 !$#title Potential basis for regulation of the coordinately expressed !1fibrinogen genes: homology in the 5' flanking regions. !$#cross-references MUID:84194000; PMID:6232608 !$#accession A93989 !'##molecule_type DNA !'##residues 1-102 ##label FOW !'##cross-references GB:K01337; NID:g204102; PIDN:AAA98626.1; !1PID:g204103 COMMENT The fibrinogen molecule is a hexamer containing two sets of !1three nonidentical chains (alpha, beta, and gamma) linked by !1several disulfide bonds. GENETICS !$#introns 25/3; 41/3 CLASSIFICATION #superfamily fibrinogen gamma chain; fibrinogen beta/gamma !1homology KEYWORDS alternative splicing; blood coagulation; plasma FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-437 #product fibrinogen gamma-A chain #status predicted !8#label FGA\ !$176-415 #domain fibrinogen beta/gamma homology #label FBG SUMMARY #length 437 #molecular-weight 49519 #checksum 1132 SEQUENCE /// ENTRY FGRTGB #type complete TITLE fibrinogen gamma-B chain precursor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 27-Feb-1997 ACCESSIONS A03128; I58265 REFERENCE A90828 !$#authors Crabtree, G.R.; Kant, J.A. !$#journal Cell (1982) 31:159-166 !$#title Organization of the rat gamma-fibrinogen gene: alternative !1mRNA splice patterns produce the gammaA and gammaB (gamma') !1chains of fibrinogen. !$#cross-references MUID:83129318; PMID:6897622 !$#accession A03128 !'##molecule_type mRNA !'##residues 1-445 ##label CRA REFERENCE I58265 !$#authors Morgan, J.G.; Holbrook, N.J.; Crabtree, G.R. !$#journal Nucleic Acids Res. (1987) 15:2774-2776 !$#title Nucleotide sequence of the gamma chain gene of rat !1fibrinogen: conserved intronic sequences. !$#cross-references MUID:87174801; PMID:3562236 !$#accession I58265 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-134 ##label RES !'##cross-references EMBL:X05860; NID:g56147; PID:g56148 COMMENT Gamma-B is formed from the same gene as gamma-A, probably as !1a result of failure to splice out the last intron during !1mRNA processing. COMMENT The fibrinogen molecule is a hexamer containing two sets of !1three nonidentical chains (alpha, beta, and gamma) linked by !1several disulfide bonds. GENETICS !$#introns 25/3; 41/3; 103/1 CLASSIFICATION #superfamily fibrinogen gamma chain; fibrinogen beta/gamma !1homology KEYWORDS alternative splicing; blood coagulation; plasma FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-445 #product fibrinogen gamma-B chain #status predicted !8#label FGB\ !$176-415 #domain fibrinogen beta/gamma homology #label FBG SUMMARY #length 445 #molecular-weight 50500 #checksum 8295 SEQUENCE /// ENTRY FGLMGS #type complete TITLE fibrinogen gamma chain precursor - sea lamprey ORGANISM #formal_name Petromyzon marinus #common_name sea lamprey DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 20-Oct-2000 ACCESSIONS A03129 REFERENCE A03129 !$#authors Strong, D.D.; Moore, M.; Cottrell, B.A.; Bohonus, V.L.; !1Pontes, M.; Evans, B.; Riley, M.; Doolittle, R.F. !$#journal Biochemistry (1985) 24:92-101 !$#title Lamprey fibrinogen gamma chain: cloning, cDNA sequencing, !1and general characterization. !$#cross-references MUID:85199776; PMID:2581603 !$#accession A03129 !'##molecule_type mRNA !'##residues 1-432 ##label STR !'##cross-references GB:K03049; NID:g213193; PIDN:AAA49262.1; !1PID:g213194 CLASSIFICATION #superfamily fibrinogen gamma chain; fibrinogen beta/gamma !1homology KEYWORDS blood coagulation; glycoprotein; liver; plasma; pyroglutamic !1acid FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-432 #product fibrinogen gamma chain #status experimental !8#label MPT\ !$175-411 #domain fibrinogen beta/gamma homology #label FBG\ !$25 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$227 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$421 #cross-link isopeptide (Gln) (interchain to Lys-425 !8N6-amino) #status predicted\ !$425 #cross-link isopeptide (Lys) (interchain to Gln-421) !8#status predicted SUMMARY #length 432 #molecular-weight 49203 #checksum 7618 SEQUENCE /// ENTRY WCHCJ #type complete TITLE coagulogen I - horseshoe crab (Tachypleus tridentatus) CONTAINS coagulin I; coagulogen I chain B; peptide C ORGANISM #formal_name Tachypleus tridentatus DATE 31-May-1979 #sequence_revision 31-May-1979 #text_change 07-May-1999 ACCESSIONS A94306; A27257; A90199; A28866; B61305; A03130 REFERENCE A94306 !$#authors Takagi, T.; Nakamura, S.; Hokama, Y.; Miyata, T.; Niwa, M.; !1Iwanaga, S. !$#journal Thromb. Haemost. (1979) 42:272 !$#title The primary structure of horseshoe crab (Tachypleus !1tridentatus) coagulogen and its homologies with platelet !1factor 4. !$#accession A94306 !'##molecule_type protein !'##residues 1-175 ##label TAK REFERENCE A91905 !$#authors Miyata, T.; Matsumoto, H.; Hattori, M.; Sakaki, Y.; Iwanaga, !1S. !$#journal J. Biochem. (1986) 100:213-220 !$#title Two types of coagulogen mRNAs found in horseshoe crab !1(Tachypleus tridentatus) hemocytes: molecular cloning and !1nucleotide sequences. !$#cross-references MUID:87008471; PMID:3759932 !$#accession A27257 !'##molecule_type mRNA !'##residues 20-175 ##label MIY REFERENCE A90199 !$#authors Nakamura, S.; Takagi, T.; Iwanaga, S.; Niwa, M.; Takahashi, !1K. !$#journal Biochem. Biophys. Res. Commun. (1976) 72:902-908 !$#title Amino acid sequence studies on the fragments produced from !1horseshoe crab coagulogen during gel formation: homologies !1with primate fibrinopeptide B. !$#cross-references MUID:77044896; PMID:985525 !$#accession A90199 !'##molecule_type protein !'##residues 1-51 ##label NAK REFERENCE A28866 !$#authors Takagi, T.; Hokama, Y.; Miyata, T.; Morita, T.; Iwanaga, S. !$#journal J. Biochem. (1984) 95:1445-1457 !$#title Amino acid sequence of Japanese horseshoe crab (Tachypleus !1tridentatus) coagulogen B chain: completion of the !1coagulogen sequence. !$#cross-references MUID:84264459; PMID:6378899 !$#accession A28866 !'##molecule_type protein !'##residues 47-175 ##label TA2 REFERENCE A61305 !$#authors Shishikura, F.; Nakamura, S.; Takahashi, K.; Sekiguchi, K. !$#journal J. Biochem. (1983) 94:1279-1287 !$#title Coagulogens from four living species of horseshoe crabs !1(Limulidae): comparison of their biochemical and !1immunochemical properties. !$#cross-references MUID:84087782; PMID:6418729 !$#accession B61305 !'##molecule_type protein !'##residues 1-14 ##label SHI COMMENT Coagulogen is a gel-forming protein of hemolymph. COMMENT Coagulogen is cleaved after Arg-18 and Arg-46 by a clotting !1enzyme contained in the hemocyte and activated by a !1bacterial endotoxin (lipopolysaccharide). This cleavage !1releases the 28-residue peptide C and leaves two chains of !1coagulin, A and B, linked by two disulfide bonds. Coagulin !1molecules interlink to form a gel. COMMENT Eight disulfide bonds are present. COMMENT The carboxyl end (residues 39-46) of peptide C is similar to !1that of fibrinopeptide B of primates. CLASSIFICATION #superfamily coagulogen KEYWORDS coagulation; hemolymph coagulation FEATURE !$1-18 #product coagulin I, chain A #status experimental !8#label COA\ !$19-46 #product peptide C #status experimental #label APT\ !$47-175 #product coagulin I, chain B #status experimental !8#label COB SUMMARY #length 175 #molecular-weight 19739 #checksum 8733 SEQUENCE /// ENTRY B27257 #type complete TITLE coagulogen II precursor - horseshoe crab (Tachypleus tridentatus) CONTAINS coagulin II; coagulogen II chain B; peptide C ORGANISM #formal_name Tachypleus tridentatus DATE 19-Nov-1988 #sequence_revision 05-Aug-1994 #text_change 16-Jun-2000 ACCESSIONS B27257; C27257 REFERENCE A91905 !$#authors Miyata, T.; Matsumoto, H.; Hattori, M.; Sakaki, Y.; Iwanaga, !1S. !$#journal J. Biochem. (1986) 100:213-220 !$#title Two types of coagulogen mRNAs found in horseshoe crab !1(Tachypleus tridentatus) hemocytes: molecular cloning and !1nucleotide sequences. !$#cross-references MUID:87008471; PMID:3759932 !$#accession B27257 !'##molecule_type mRNA !'##residues 1-195 ##label MIY !'##cross-references GB:D00077; NID:g217394; PIDN:BAA00051.1; !1PID:g217395 !$#accession C27257 !'##molecule_type protein !'##residues 95-113 ##label MI2 COMMENT Coagulogen is a gel-forming protein of hemolymph. COMMENT Coagulogen is cleaved after Arg-18 and Arg-46 by a clotting !1enzyme contained in the hemocyte and activated by a !1bacterial endotoxin (lipopolysaccharide). This cleavage !1releases the 28-residue peptide C and leaves two chains of !1coagulin, A and B, linked by two disulfide bonds. Coagulin !1molecules interlink to form a gel. COMMENT Eight disulfide bonds are present. COMMENT The carboxyl end (residues 39-46) of peptide C is similar to !1that of fibrinopeptide B of primates. CLASSIFICATION #superfamily coagulogen KEYWORDS coagulation; hemolymph coagulation FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-195 #product coagulogen II #status predicted #label MAT\ !$21-38 #product coagulin, chain A #status predicted #label !8COA\ !$39-66 #product peptide C #status predicted #label APT\ !$67-195 #product coagulin, chain B #status predicted #label !8COB SUMMARY #length 195 #molecular-weight 21826 #checksum 2906 SEQUENCE /// ENTRY WCHCS #type complete TITLE coagulogen - horseshoe crab (Carcinoscorpius rotundicauda) CONTAINS coagulin; peptide C ORGANISM #formal_name Carcinoscorpius rotundicauda DATE 13-Aug-1986 #sequence_revision 13-Aug-1986 #text_change 07-May-1999 ACCESSIONS A03131; D61305 REFERENCE A03131 !$#authors Srimal, S.; Miyata, T.; Kawabata, S.; Miyata, T.; Iwanaga, !1S. !$#journal J. Biochem. (1985) 98:305-318 !$#title The complete amino acid sequence of coagulogen isolated from !1Southeast asian horseshoe crab, Carcinoscorpius !1rotundicauda. !$#cross-references MUID:86059292; PMID:3905780 !$#accession A03131 !'##molecule_type protein !'##residues 1-175 ##label SRI REFERENCE A61305 !$#authors Shishikura, F.; Nakamura, S.; Takahashi, K.; Sekiguchi, K. !$#journal J. Biochem. (1983) 94:1279-1287 !$#title Coagulogens from four living species of horseshoe crabs !1(Limulidae): comparison of their biochemical and !1immunochemical properties. !$#cross-references MUID:84087782; PMID:6418729 !$#accession D61305 !'##molecule_type protein !'##residues 1-14 ##label SHI COMMENT Coagulogen is a gel-forming protein of hemolymph. COMMENT Coagulogen is cleaved after Arg-18 and Arg-46 by a clotting !1enzyme contained in the hemocyte and activated by a !1bacterial endotoxin (lipopolysaccharide). This cleavage !1releases the 28-residue peptide C and leaves two chains of !1coagulin, A and B, linked by two disulfide bonds. Coagulin !1molecules interlink to form a gel. COMMENT Eight disulfide bonds are present. COMMENT The carboxyl end (residues 39-46) of peptide C is similar to !1that of fibrinopeptide B of primates. CLASSIFICATION #superfamily coagulogen KEYWORDS coagulation; hemolymph coagulation FEATURE !$1-18 #product coagulin, chain A #status experimental !8#label COA\ !$19-46 #product peptide C #status experimental #label APT\ !$47-175 #product coagulin, chain B #status experimental !8#label COB SUMMARY #length 175 #molecular-weight 19765 #checksum 8929 SEQUENCE /// ENTRY A28851 #type complete TITLE coagulogen - horseshoe crab (Tachypleus gigas) ORGANISM #formal_name Tachypleus gigas DATE 19-May-1989 #sequence_revision 05-Aug-1994 #text_change 07-May-1999 ACCESSIONS A28851; C61305 REFERENCE A28851 !$#authors Miyata, T.; Usui, K.; Iwanaga, S. !$#journal J. Biochem. (1984) 95:1793-1801 !$#title The amino acid sequence of coagulogen isolated from !1Southeast Asian horseshoe crab, Tachypleus gigas. !$#cross-references MUID:84289359; PMID:6469947 !$#accession A28851 !'##molecule_type protein !'##residues 1-175 ##label MIY REFERENCE A61305 !$#authors Shishikura, F.; Nakamura, S.; Takahashi, K.; Sekiguchi, K. !$#journal J. Biochem. (1983) 94:1279-1287 !$#title Coagulogens from four living species of horseshoe crabs !1(Limulidae): comparison of their biochemical and !1immunochemical properties. !$#cross-references MUID:84087782; PMID:6418729 !$#accession C61305 !'##molecule_type protein !'##residues 1-6,'I',8-14 ##label SHI COMMENT Coagulogen is a gel-forming protein of hemolymph. COMMENT Coagulogen is cleaved after Arg-18 and Arg-46 by a clotting !1enzyme contained in the hemocyte and activated by a !1bacterial endotoxin (lipopolysaccharide). This cleavage !1releases the 28-residue peptide C and leaves two chains of !1coagulin, A and B, linked by two disulfide bonds. Coagulin !1molecules interlink to form a gel. COMMENT Eight disulfide bonds are present. COMMENT The carboxyl end (residues 39-46) of peptide C is similar to !1that of fibrinopeptide B of primates. CLASSIFICATION #superfamily coagulogen KEYWORDS coagulation; hemolymph coagulation FEATURE !$1-18 #product coagulin, chain A #status experimental !8#label COA\ !$19-46 #product peptide C #status experimental #label APT\ !$47-175 #product coagulin, chain B #status experimental !8#label COB SUMMARY #length 175 #molecular-weight 19770 #checksum 6316 SEQUENCE /// ENTRY WCHCA #type complete TITLE coagulogen precursor - Atlantic horseshoe crab CONTAINS coagulin; peptide C ORGANISM #formal_name Limulus polyphemus #common_name Atlantic horseshoe crab DATE 13-Aug-1986 #sequence_revision 31-Mar-1993 #text_change 22-Jun-1999 ACCESSIONS A43790; A03132; A61305 REFERENCE A43790 !$#authors Cheng, S.M.; Suzuki, A.; Zon, G.; Liu, T.Y. !$#journal Biochim. Biophys. Acta (1986) 868:1-8 !$#title Characterization of a complementary deoxyribonucleic acid !1for the coagulogen of Limulus polyphemus. !$#cross-references MUID:87000614; PMID:3756166 !$#accession A43790 !'##molecule_type mRNA !'##residues 1-195 ##label CHE !'##cross-references GB:X04424; NID:g9608; PIDN:CAA28020.1; PID:g758141 REFERENCE A03132 !$#authors Miyata, T.; Hiranaga, M.; Umezu, M.; Iwanaga, S. !$#journal J. Biol. Chem. (1984) 259:8924-8933 !$#title Amino acid sequence of the coagulogen from Limulus !1polyphemus hemocytes. !$#cross-references MUID:84264512; PMID:6378904 !$#accession A03132 !'##molecule_type protein !'##residues 21-101,'S',103-104,'HP',107-195 ##label MIY REFERENCE A61305 !$#authors Shishikura, F.; Nakamura, S.; Takahashi, K.; Sekiguchi, K. !$#journal J. Biochem. (1983) 94:1279-1287 !$#title Coagulogens from four living species of horseshoe crabs !1(Limulidae): comparison of their biochemical and !1immunochemical properties. !$#cross-references MUID:84087782; PMID:6418729 !$#accession A61305 !'##molecule_type protein !'##residues 21-34 ##label SHI COMMENT Coagulogen is a gel-forming protein of hemolymph. COMMENT Coagulogen is cleaved by a clotting enzyme contained in the !1hemocyte and activated by a bacterial endotoxin !1(lipopolysaccharide). This cleavage releases peptide C and !1leaves two chains of coagulin, A and B, linked by two !1disulfide bonds. Coagulin molecules interlink to form a gel. COMMENT Eight disulfide bonds are present. COMMENT The carboxyl end of peptide C is similar to that of !1fibrinopeptide B of primates. CLASSIFICATION #superfamily coagulogen KEYWORDS disulfide bond; hemolymph coagulation FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-38 #product coagulin chain A #status experimental #label !8ACH\ !$39-66 #product peptide C #status experimental #label APT\ !$67-195 #product coagulin chain B #status experimental #label !8BCH SUMMARY #length 195 #molecular-weight 21818 #checksum 2945 SEQUENCE /// ENTRY UJHU #type complete TITLE major prion protein precursor - human ALTERNATE_NAMES 11K amyloid protein; 27-30K sialoglycoprotein; PrP 27-30; PrP 33-35C; scrapie prion protein ORGANISM #formal_name Homo sapiens #common_name man DATE 25-Oct-1987 #sequence_revision 12-Apr-1996 #text_change 16-Jun-2000 ACCESSIONS A24173; A40372; A05017; S14078; I54322; I68597; I58135; !1I59184; I79633; I79634 REFERENCE A24173 !$#authors Kretzschmar, H.A.; Stowring, L.E.; Westaway, D.; !1Stubblebine, W.H.; Prusiner, S.B.; Dearmond, S.J. !$#journal DNA (1986) 5:315-324 !$#title Molecular cloning of a human prion protein cDNA. !$#cross-references MUID:86300093; PMID:3755672 !$#accession A24173 !'##molecule_type mRNA !'##residues 1-253 ##label KRE !'##cross-references GB:M13899; NID:g190467; PIDN:AAA60182.1; !1PID:g190468 REFERENCE A40372 !$#authors Puckett, C.; Concannon, P.; Casey, C.; Hood, L. !$#journal Am. J. Hum. Genet. (1991) 49:320-329 !$#title Genomic structure of the human prion protein gene. !$#cross-references MUID:91328137; PMID:1678248 !$#accession A40372 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-80,89-253 ##label PUC !'##cross-references GB:X83416; NID:g747846; PIDN:CAA58442.1; !1PID:g747847 !'##note the deletion may be a polymorphism; the alternative deletion of !182-89 could not be ruled out REFERENCE A05017 !$#authors Liao, Y.C.J.; Lebo, R.V.; Clawson, G.A.; Smuckler, E.A. !$#journal Science (1986) 233:364-367 !$#cross-references MUID:86261778; PMID:3014653 !$#accession A05017 !'##molecule_type mRNA !'##residues 8-117,119-253 ##label LIA !'##cross-references GB:D00015; NID:g220015; PIDN:BAA00011.1; !1PID:g220016; GB:M13667; NID:g190469; PID:g190470 REFERENCE S14078 !$#authors Tagliavini, F.; Prelli, F.; Ghiso, J.; Bugiani, O.; Serban, !1D.; Prusiner, S.B.; Farlow, M.R.; Ghetti, B.; Frangione, B. !$#journal EMBO J. (1991) 10:513-519 !$#title Amyloid protein of Gerstmann-Straeussler-Scheinker disease !1(Indiana kindred) is an 11 kd fragment of prion protein with !1an N-terminal glycine at codon 58. !$#cross-references MUID:91160504; PMID:1672107 !$#accession S14078 !'##molecule_type protein !'##residues 58-72,'X',74-76,'XX',79,'XXX',83-86;111-128,'V',130-150 !1##label TAG REFERENCE I54322 !$#authors Diedrich, J.F.; Knopman, D.S.; List, J.F.; Olson, K.; Frey, !1W.H. !$#journal Hum. Mol. Genet. (1992) 1:443-444 !$#title Deletion in the prion protein gene in a demented patient. !$#cross-references MUID:93250789; PMID:1363802 !$#accession I54322 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 9-83,92-240 ##label RES !'##cross-references GB:M81929; NID:g190517; PIDN:AAB59442.1; !1PID:g190518 !$#accession I68597 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 8-240 ##label RE3 !'##cross-references GB:M81930; NID:g190519; PIDN:AAB59443.1; !1PID:g190520 REFERENCE I58135 !$#authors Brown, P.; Goldfarb, L.G.; McCombie, W.R.; Nieto, A.; !1Squillacote, D.; Sheremata, W.; Little, B.W.; Godec, M.S.; !1Gibbs, C.J. !$#journal Neurology (1992) 42:422-427 !$#title Atypical Creutzfeldt-Jakob disease in an American family !1with an insert mutation in the PRNP amyloid precursor gene. !$#cross-references MUID:92140671; PMID:1736177 !$#accession I58135 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 51-91, !1'PHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGG' !1##label RE2 !'##cross-references GB:S80539; NID:g244698; PIDN:AAB21334.1; !1PID:g244699 REFERENCE I59184 !$#authors Goldfarb, L.G.; Brown, P.; McCombie, W.R.; Goldgaber, D.; !1Swergold, G.D.; Wills, P.R.; Cervenakova, L.; Baron, H.; !1Gibbs, C.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:10926-10930 !$#title Transmissible familial Creutzfeldt-Jakob disease associated !1with five, seven, and eight extra octapeptide coding repeats !1in the PRNP gene. !$#cross-references MUID:92073400; PMID:1683708 !$#accession I59184 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 60-67 ##label GOL !'##cross-references GB:S71208; NID:g239877; PIDN:AAB20521.1; !1PID:g239878; GB:S71210; NID:g239879; PID:g239880; GB:S71212; !1NID:g239881; PID:g239882 GENETICS !$#gene GDB:PRNP; CJD; PRIP !'##cross-references GDB:120720; OMIM:176640; OMIM:137440 !$#map_position 20pter-20p12 !$#introns #status absent !$#note one intron occurs before the initiator codon !$#note this gene is associated with Creutzfeld-Jakob disease (CJD), !1Gerstmann-Strausler-Scheinker syndrome (GSS), kuru, and !1fatal familial insomnia (FFI) CLASSIFICATION #superfamily major prion protein KEYWORDS amyloid; blocked carboxyl end; brain; glycoprotein; !1lipoprotein; phosphatidylinositol linkage; phosphoprotein; !1prion; scrapie; tandem repeat; transmembrane protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-230 #product major prion protein #status predicted #label !8MAT\ !$54-92 #region 8-residue repeats (P-H-G-G-G-W-G-Q)\ !$112-134 #domain transmembrane #status predicted #label TM1\ !$231-253 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$179-214 #disulfide_bonds #status predicted\ !$181,197 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$230 #modified_site GPI-anchor ethanolamine amidated !8carboxyl end (Ser) (in mature form) #status predicted SUMMARY #length 253 #molecular-weight 27661 #checksum 8781 SEQUENCE /// ENTRY UJHYIH #type complete TITLE major prion PrP-Sc protein precursor - golden hamster CONTAINS scrapie amyloid protein (PrP27-30) ORGANISM #formal_name Mesocricetus auratus #common_name golden hamster DATE 04-Dec-1986 #sequence_revision 12-Apr-1996 #text_change 28-Jan-2000 ACCESSIONS I48168; A03133; I48167; S02520; A36019; A40665 REFERENCE I48168 !$#authors Basler, K.; Oesch, B.; Scott, M.G.; Westaway, D.; Waelchli, !1M.; Groth, D.F.; McKinley, M.P.; Prusiner, S.B.; Weissmann, !1C. !$#journal Cell (1986) 46:417-428 !$#title Scrapie and cellular PrP isoforms are encoded by the same !1chromosomal gene. !$#cross-references MUID:86272089; PMID:2873895 !$#accession I48168 !'##molecule_type DNA !'##residues 1-254 ##label RES !'##cross-references GB:M14054; NID:g191425; PIDN:AAA37091.1; !1PID:g387076 REFERENCE A03133 !$#authors Oesch, B.; Westaway, D.; Walchli, M.; McKinley, M.P.; Kent, !1S.B.H.; Aebersold, R.; Barry, R.A.; Tempst, P.; Teplow, !1D.B.; Hood, L.E.; Prusiner, S.B.; Weissmann, C. !$#journal Cell (1985) 40:735-746 !$#title A cellular gene encodes scrapie PrP 27-30 protein. !$#cross-references MUID:85176927; PMID:2859120 !$#accession A03133 !'##molecule_type mRNA !'##residues 15-254 ##label OES !'##cross-references GB:K02234; NID:g191429; PIDN:AAA37092.1; !1PID:g191430 !'##note this mRNA, isolated from the brain of scrapie-infected hamster, !1is the product of a cellular gene and is found also in !1normal animals REFERENCE A40665 !$#authors Stahl, N.; Baldwin, M.A.; Teplow, D.B.; Hood, L.; Gibson, !1B.W.; Burlingame, A.L.; Prusiner, S.B. !$#journal Biochemistry (1993) 32:1991-2002 !$#title Structural studies of the scrapie prion protein using mass !1spectrometry and amino acid sequencing. !$#cross-references MUID:93192259; PMID:8448158 !$#contents annotation; chemical (not conformational) identity of PrPSc !1and PrPC molecular forms !$#note no chemical difference between cellular (PrPC) and scrapie !1(PrPSc) forms of this protein could be determined by !1sequencing mass spectrometry on protein fragments REFERENCE I48167 !$#authors McKinley, M.P.; Prusiner, S.B. !$#journal Int. Rev. Neurobiol. (1986) 28:1-57 !$#title Biology and structure of scrapie prions. !$#cross-references MUID:87108309; PMID:3100471 !$#accession I48167 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 12-254 ##label RE2 !'##cross-references GB:M37381; NID:g191422; PIDN:AAA37090.1; !1PID:g191423 REFERENCE S02519 !$#authors Turk, E.; Teplow, D.B.; Hood, L.E.; Prusiner, S.B. !$#journal Eur. J. Biochem. (1988) 176:21-30 !$#title Purification and properties of the cellular and scrapie !1hamster prion proteins. !$#cross-references MUID:88329062; PMID:3138115 !$#accession S02520 !'##molecule_type protein !'##residues 23-24,'X',26-36,'X',38-55 ##label TUR !'##experimental_source strain Lak:LVG REFERENCE A36019 !$#authors Safar, J.; Wang, W.; Padgett, M.P.; Ceroni, M.; Piccardo, !1P.; Zopf, D.; Gajdusek, D.C.; Gibbs Jr., C.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:6373-6377 !$#title Molecular mass, biochemical composition, and physicochemical !1behavior of the infectious form of the scrapie precursor !1protein monomer. !$#cross-references MUID:90349618; PMID:1974720 !$#accession A36019 !'##molecule_type protein !'##residues 'S',24-32 ##label SAF !'##experimental_source brain, strain 263-K COMMENT Scrapie amyloid protein PrP27-30 is a strongly aggregating, !1amyloid fibril-forming product formed from mature PrP-Sc by !1proteolytic cleavage. GENETICS !$#introns #status absent !$#note an intron is found 5' to the coding region CLASSIFICATION #superfamily major prion protein KEYWORDS blocked carboxyl end; brain; glycoprotein; lipoprotein; !1phosphatidylinositol linkage; phosphoprotein; scrapie FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-231 #product major prion PrP27-30 protein #status !8experimental #label MAT\ !$232-254 #domain carboxyl-terminal propeptide #status !8predicted #label CPP\ !$181,197 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$231 #modified_site GPI-anchor ethanolamine amidated !8carboxyl end (Ser) (in mature form) #status !8experimental SUMMARY #length 254 #molecular-weight 27919 #checksum 1340 SEQUENCE /// ENTRY UJCH #type complete TITLE major prion protein homolog precursor - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 22-Jun-1999 ACCESSIONS A41280; B41280 REFERENCE A41280 !$#authors Harris, D.A.; Falls, D.L.; Johnson, F.A.; Fischbach, G.D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:7664-7668 !$#title A prion-like protein from chicken brain copurifies with an !1acetylcholine receptor-inducing activity. !$#cross-references MUID:91352049; PMID:1715573 !$#accession A41280 !'##molecule_type mRNA !'##residues 1-267 ##label HAR !'##cross-references GB:M61145; NID:g212614; PIDN:AAA49041.1; !1PID:g212615 !'##experimental_source day-18 brain !$#accession B41280 !'##molecule_type protein !'##residues 25-51 ##label HA2 !'##note the protein was purified from adult chicken brain on the basis !1of its ability to stimulate the synthesis of acetylcholine !1receptors in cultured chicken myotubes COMMENT Enzymatic release studies show that this protein has a !1glycosylphosphatidylinositol anchor. CLASSIFICATION #superfamily major prion protein KEYWORDS brain; glycoprotein; phosphatidylinositol linkage; prion; !1scrapie FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-267 #product major prion protein homolog #status !8predicted #label MAT\ !$188,203,212 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 267 #molecular-weight 29312 #checksum 4468 SEQUENCE /// ENTRY QRHUA4 #type complete TITLE Alzheimer's disease amyloid beta protein precursor [validated] - human ALTERNATE_NAMES Alzheimer's disease amyloid A4 protein; coagulation factor XIa inhibitor; proteinase nexin II (PN-II) CONTAINS amyloid beta protein long, plaque form; amyloid beta protein short, vascular form; amyloid protein precursor splice form APP(695); amyloid protein precursor splice form APP(751); amyloid protein precursor splice form APP(770) ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1987 #sequence_revision 28-Jul-1995 #text_change 15-Sep-2000 ACCESSIONS S02260; S05194; A32277; A33260; A35486; I39452; I39451; !1I39453; I59562; A44017; B44017; A03134; A29030; A47584; !1A47585; S02638; S00707; S00925; A38949; A30320; B30320; !1C30320; A31087; A24668; A28583; A29302; A60805; JL0038; !1S06121; A60355; A59011; A38384; S29076; S38252; S32539; !1S48148; S48692; S51186; S51185; S51184; S51183; A54238; !1I58075; I52250; S09010; S10737; S24127; S43644 REFERENCE S02260 !$#authors Lemaire, H.G.; Salbaum, J.M.; Multhaup, G.; Kang, J.; !1Bayney, R.M.; Unterbeck, A.; Beyreuther, K.; Mueller-Hill, !1B. !$#journal Nucleic Acids Res. (1989) 17:517-522 !$#title The PreA4(695) precursor protein of Alzheimer's disease A4 !1amyloid is encoded by 16 exons. !$#cross-references MUID:89128427; PMID:2783775 !$#accession S02260 !'##molecule_type DNA !'##residues 1-288,'V',365-770 ##label LEM1 !'##cross-references EMBL:X13466 !'##note alternative splice form APP(695) REFERENCE S05194 !$#authors Lemaire, H.G. !$#submission submitted to the EMBL Data Library, November 1988 !$#accession S05194 !'##molecule_type DNA !'##residues 1-14,'VW',17-288,'V',365-770 ##label LEM2 !'##cross-references EMBL:X13466; NID:g35598; PIDN:CAA31830.1; !1PID:g871360 !'##note alternative splice form APP(695) REFERENCE A32277 !$#authors La Fauci, G.; Lahiri, D.K.; Salton, S.R.J.; Robakis, N.K. !$#journal Biochem. Biophys. Res. Commun. (1989) 159:297-304 !$#title Characterization of the 5'-end region and the first two !1exons of the beta-protein precursor gene. !$#cross-references MUID:89165870; PMID:2538123 !$#accession A32277 !'##molecule_type DNA !'##residues 1-75 ##label LAF !'##cross-references GB:M24546; GB:M24547; NID:g341202; PIDN:AAC13654.1; !1PID:g516074 REFERENCE A33260 !$#authors Johnstone, E.M.; Chaney, M.O.; Moore, R.E.; Ward, K.E.; !1Norris, F.H.; Little, S.P. !$#journal Biochem. Biophys. Res. Commun. (1989) 163:1248-1255 !$#title Alzheimer's disease amyloid peptide is encoded by two exons !1and shows similarity to soybean trypsin inhibitor. !$#cross-references MUID:89392030; PMID:2675837 !$#accession A33260 !'##molecule_type DNA !'##residues 656-737 ##label JOH !'##cross-references GB:M29270; NID:g178863; PIDN:AAA51768.1; !1PID:g178865 REFERENCE A35486 !$#authors Prelli, F.; Levy, E.; van Duinen, S.G.; Bots, G.T.A.M.; !1Luyendijk, W.; Frangione, B. !$#journal Biochem. Biophys. Res. Commun. (1990) 170:301-307 !$#title Expression of a normal and variant Alzheimer's beta-protein !1gene in amyloid of hereditary cerebral hemorrhage, Dutch !1type: DNA and protein diagnostic assays. !$#cross-references MUID:90321244; PMID:2196878 !$#accession A35486 !'##molecule_type DNA !'##residues 672-710 ##label PRE1 !'##note 693-Gln was found in DNA isolated from HCHWA-D patients REFERENCE I39451 !$#authors Yoshikai, S.I.; Sasaki, H.; Doh-ura, K.; Furuya, H.; Sakaki, !1Y. !$#journal Gene (1990) 87:257-263 !$#title Genomic organization of the human amyloid beta-protein !1precursor gene. !$#cross-references MUID:90236318; PMID:2110105 !$#accession I39452 !'##status nucleic acid sequence not shown; translation not shown; !1translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-770 ##label YOS1 !'##cross-references GB:M33112; NID:g178613; PIDN:AAB59502.1; !1PID:g178616 !$#accession I39451 !'##status nucleic acid sequence not shown; translation not shown; !1translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-530,'QWLMPVIPAFWEAKVGR' ##label YOS2 !'##cross-references GB:M34875; NID:g178608; PIDN:AAB59501.1; !1PID:g178615 REFERENCE A59020 !$#authors Yoshikai, S.I.; Sasaki, H.; Doh-ura, K.; Furuya, H.; Sakaki, !1Y. !$#journal Gene (1991) 102:291-292 !$#cross-references MUID:91340168; PMID:1908403 !$#contents annotation; erratum !$#note revised physical map for reference I39451 REFERENCE I39453 !$#authors Levy, E.; Carman, M.D.; Fernandez-Madrid, I.J.; Power, M.D.; !1Lieberburg, I.; van Duinen, S.G.; Bots, G.T.; Luyendijk, W.; !1Frangione, B. !$#journal Science (1990) 248:1124-1126 !$#title Mutation of the Alzheimer's disease amyloid gene in !1hereditary cerebral hemorrhage, Dutch type. !$#cross-references MUID:90260663; PMID:2111584 !$#accession I39453 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 656-737 ##label LEV !'##cross-references GB:M37896; NID:g178618; PIDN:AAA51727.1; !1PID:g178620 !'##note a mutation with 693-Gln is presented REFERENCE I59562 !$#authors Murrell, J.; Farlow, M.; Ghetti, B.; Benson, M.D. !$#journal Science (1991) 254:97-99 !$#title A mutation in the amyloid precursor protein associated with !1hereditary Alzheimer's disease. !$#cross-references MUID:92022553; PMID:1925564 !$#accession I59562 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 689-716,'F',718-737 ##label MUR !'##cross-references GB:S57665; NID:g236720; PIDN:AAB19991.1; !1PID:g236721 REFERENCE A44017 !$#authors Kamino, K.; Orr, H.T.; Payami, H.; Wijsman, E.M.; Alonso, !1M.E.; Pulst, S.M.; Anderson, L.; O'dahl, S.; Nemens, E.; !1White, J.A.; Sadovnick, A.D.; Ball, M.J.; Kaye, J.; Warren, !1A.; McInnis, M.; Antonarakis, S.E.; Korenberg, J.R.; Sharma, !1V.; Kukull, W.; Larson, E.; Heston, L.L.; Martin, G.M.; !1Bird, T.D.; Schellenberg, G.D. !$#journal Am. J. Hum. Genet. (1992) 51:998-1014 !$#title Linkage and mutational analysis of familial Alzheimer !1disease kindreds for the APP gene region. !$#cross-references MUID:93035397; PMID:1415269 !$#accession A44017 !'##molecule_type DNA !'##residues 687-692,'G',694-718 ##label KAM1 !'##cross-references GB:S45135; NID:g257377; PIDN:AAB23645.1; !1PID:g257378 !'##experimental_source familial Alzheimer disease family SB !'##note sequence extracted from NCBI backbone (NCBIP:115374) !$#accession B44017 !'##molecule_type DNA !'##residues 687-718 ##label KAM2 !'##cross-references GB:S45136; NID:g257379; PIDN:AAB23646.1; !1PID:g257380 !'##experimental_source familial Alzheimer disease family LIT !'##note sequence extracted from NCBI backbone (NCBIP:115376) !'##note this sequence has a silent mutation REFERENCE A03134 !$#authors Kang, J.; Lemaire, H.G.; Unterbeck, A.; Salbaum, J.M.; !1Masters, C.L.; Grzeschik, K.H.; Multhaup, G.; Beyreuther, !1K.; Muller-Hill, B. !$#journal Nature (1987) 325:733-736 !$#title The precursor of Alzheimer's disease amyloid A4 protein !1resembles a cell-surface receptor. !$#cross-references MUID:87144572; PMID:2881207 !$#accession A03134 !'##molecule_type mRNA !'##residues 1-288,'V',365-770 ##label KAN !'##cross-references GB:Y00264; NID:g28525; PIDN:CAA68374.1; PID:g28526 !'##note alternative splice form APP(695) REFERENCE A29030 !$#authors Robakis, N.K.; Ramakrishna, N.; Wolfe, G.; Wisniewski, H.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:4190-4194 !$#title Molecular cloning and characterization of a cDNA encoding !1the cerebrovascular and the neuritic plaque amyloid !1peptides. !$#cross-references MUID:87231971; PMID:3035574 !$#accession A29030 !'##molecule_type mRNA !'##residues 284-288,'V',365-646,'E',648-770 ##label ROB !'##cross-references GB:M16765; NID:g178539; PIDN:AAA51722.1; !1PID:g178540 !'##note the authors translated the codon GAG for residue 647 as Asp REFERENCE A47584 !$#authors Goldgaber, D.; Lerman, M.I.; McBride, O.W.; Saffiotti, U.; !1Gajdusek, D.C. !$#journal Science (1987) 235:877-880 !$#title Characterization and chromosomal localization of a cDNA !1encoding brain amyloid of Alzheimer's disease. !$#cross-references MUID:87120328; PMID:3810169 !$#accession A47584 !'##molecule_type mRNA !'##residues 674-756,'S',758-770 ##label GOL !'##cross-references GB:M15533; NID:g178706; PIDN:AAA35540.1; !1PID:g178707 !'##experimental_source brain REFERENCE A47585 !$#authors Tanzi, R.E.; Gusella, J.F.; Watkins, P.C.; Bruns, G.A.P.; St !1George-Hyslop, P.; Van Keuren, M.L.; Patterson, D.; Pagan, !1S.; Kurnit, D.M.; Neve, R.L. !$#journal Science (1987) 235:880-884 !$#title Amyloid beta protein gene: cDNA, mRNA distribution, and !1genetic linkage near the Alzheimer locus. !$#cross-references MUID:87120329; PMID:2949367 !$#accession A47585 !'##molecule_type mRNA !'##residues 674-703 ##label TAN1 !'##cross-references GB:M15532; NID:g177957; PIDN:AAA51564.1; !1PID:g177958 REFERENCE S02638 !$#authors Dyrks, T.; Weidemann, A.; Multhaup, G.; Salbaum, J.M.; !1Lemaire, H.G.; Kang, J.; Mueller-Hill, B.; Masters, C.L.; !1Beyreuther, K. !$#journal EMBO J. (1988) 7:949-957 !$#title Identification, transmembrane orientation and biogenesis of !1the amyloid A4 precursor of Alzheimer's disease. !$#cross-references MUID:88296437; PMID:2900137 !$#accession S02638 !'##molecule_type mRNA !'##residues 672-678 ##label DYR REFERENCE S00707 !$#authors Tanzi, R.E.; McClatchey, A.I.; Lamperti, E.D.; !1Villa-Komaroff, L.; Gusella, J.F.; Neve, R.L. !$#journal Nature (1988) 331:528-530 !$#title Protease inhibitor domain encoded by an amyloid protein !1precursor mRNA associated with Alzheimer's disease. !$#cross-references MUID:88122640; PMID:2893290 !$#accession S00707 !'##molecule_type mRNA !'##residues 286-344,'I',365-366 ##label TAN2 !'##cross-references EMBL:X06982; NID:g28817; PIDN:CAA30042.1; !1PID:g929612 !'##experimental_source promyelocytic leukemia cell line HL60 !'##note alternative splice form APP(751) REFERENCE S00925 !$#authors Ponte, P.; Gonzalez-DeWhitt, P.; Schilling, J.; Miller, J.; !1Hsu, D.; Greenberg, B.; Davis, K.; Wallace, W.; Lieberburg, !1I.; Fuller, F.; Cordell, B. !$#journal Nature (1988) 331:525-527 !$#title A new A4 amyloid mRNA contains a domain homologous to serine !1proteinase inhibitors. !$#cross-references MUID:88122639; PMID:2893289 !$#accession S00925 !'##molecule_type mRNA !'##residues 1-344,'I',365-770 ##label PO2 !'##cross-references GB:X06989; EMBL:Y00297; NID:g28720; !1PIDN:CAA30050.1; PID:g28721 !'##note alternative splice form APP(751) REFERENCE A38949 !$#authors Kitaguchi, N.; Takahashi, Y.; Tokushima, Y.; Shiojiri, S.; !1Ito, H. !$#journal Nature (1988) 331:530-532 !$#title Novel precursor of Alzheimer's disease amyloid protein shows !1protease inhibitory activity. !$#cross-references MUID:88122641; PMID:2893291 !$#accession A38949 !'##molecule_type mRNA !'##residues 287-367 ##label KIT !'##cross-references GB:X06981; NID:g28816; PIDN:CAA30041.1; PID:g929611 !'##experimental_source glioblastoma cell line !'##note alternative splice form APP(770) REFERENCE A30320 !$#authors Vitek, M.P.; Rasool, C.G.; de Sauvage, F.; Vitek, S.M.; !1Bartus, R.T.; Beer, B.; Ashton, R.A.; Macq, A.F.; Maloteaux, !1J.M.; Blume, A.J.; Octave, J.N. !$#journal Brain Res. Mol. Brain Res. (1988) 4:121-131 !$#title Absence of mutation in the beta-amyloid cDNAs cloned from !1the brains of three patients with sporadic Alzheimer's !1disease. !$#accession A30320 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 284-288,'V',365-770 ##label VIT1 !$#accession B30320 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 122-288,'V',365-770 ##label VIT2 !$#accession C30320 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 606-770 ##label VIT3 REFERENCE A31087 !$#authors Zain, S.B.; Salim, M.; Chou, W.G.; Sajdel-Sulkowska, E.M.; !1Majocha, R.E.; Marotta, C.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:929-933 !$#title Molecular cloning of amyloid cDNA derived from mRNA of the !1Alzheimer disease brain: coding and noncoding regions of the !1fetal precursor mRNA are expressed in the cortex. !$#cross-references MUID:88124954; PMID:2893379 !$#accession A31087 !'##molecule_type mRNA !'##residues 507-770 ##label ZAI !'##cross-references GB:M18734; NID:g178572; PIDN:AAA51726.1; !1PID:g178573 !'##note the authors translated the codon GAA for residue 599 as Gly, !1ACC for residue 603 as Val, GTG for residue 604 as Glu, GAG !1for residue 605 as Leu, CTT for residue 607 as Pro, CCC for !1residue 608 as Val, GTG for residue 609 as Asn, AAT for !1residue 610 as Gly, and GGT for residue 655 as Ser !'##note the cited Genbank accession number, J03594, is not in release !1101.0 REFERENCE A24668 !$#authors Masters, C.L.; Multhaup, G.; Simms, G.; Pottgiesser, J.; !1Martins, R.N.; Beyreuther, K. !$#journal EMBO J. (1985) 4:2757-2763 !$#title Neuronal origin of a cerebral amyloid: neurofibrillary !1tangles of Alzheimer's disease contain the same protein as !1the amyloid of plaque cores and blood vessels. !$#cross-references MUID:86055707; PMID:4065091 !$#accession A24668 !'##molecule_type protein !'##residues 672-686 ##label MAS REFERENCE A28583 !$#authors Pardridge, W.M.; Vinters, H.V.; Yang, J.; Eisenberg, J.; !1Choi, T.B.; Tourtellotte, W.W.; Huebner, V.; Shively, J.E. !$#journal J. Neurochem. (1987) 49:1394-1401 !$#title Amyloid angiopathy of Alzheimer's disease: amino acid !1composition and partial sequence of a 4,200-dalton peptide !1isolated from cortical microvessels. !$#cross-references MUID:88035004; PMID:3312495 !$#accession A28583 !'##molecule_type protein !'##residues 672-681 ##label PAR REFERENCE A29302 !$#authors Van Nostrand, W.E.; Cunningham, D.D. !$#journal J. Biol. Chem. (1987) 262:8508-8514 !$#title Purification of protease nexin II from human fibroblasts. !$#cross-references MUID:87250462; PMID:3597385 !$#accession A29302 !'##molecule_type protein !'##residues 18-43,'F',45-50 ##label VAN2 REFERENCE A60805 !$#authors Joachim, C.L.; Duffy, L.K.; Morris, J.H.; Selkoe, D.J. !$#journal Brain Res. (1988) 474:100-111 !$#title Protein chemical and immunocytochemical studies of !1meningovascular beta-amyloid protein in Alzheimer's disease !1and normal aging. !$#cross-references MUID:89105735; PMID:3214703 !$#accession A60805 !'##molecule_type protein !'##residues 672-701,'XXXX',706-711 ##label JOA REFERENCE JL0038 !$#authors Prelli, F.; Castano, E.; Glenner, G.G.; Frangione, B. !$#journal J. Neurochem. (1988) 51:648-651 !$#title Differences between vascular and plaque core amyloid in !1Alzheimer's disease. !$#cross-references MUID:88274415; PMID:3292706 !$#accession JL0038 !'##molecule_type protein !'##residues 672-710 ##label PRE2 !'##experimental_source brain REFERENCE S06121 !$#authors Van Nostrand, W.E.; Wagner, S.L.; Suzuki, M.; Choi, B.H.; !1Farrow, J.S.; Geddes, J.W.; Cotman, C.W.; Cunningham, D.D. !$#journal Nature (1989) 341:546-549 !$#title Protease nexin-II, a potent anti-chymotrypsin, shows !1identity to amyloid beta-protein precursor. !$#cross-references MUID:90015171; PMID:2507928 !$#accession S06121 !'##molecule_type protein !'##residues 18-43,'F',45-72;107,'X',109-116 ##label VAN1 REFERENCE A60355 !$#authors Palmert, M.R.; Usiak, M.; Mayeux, R.; Raskind, M.; !1Tourtellotte, W.W.; Younkin, S.G. !$#journal Neurology (1990) 40:1028-1034 !$#title Soluble derivatives of the beta amyloid protein precursor in !1cerebrospinal fluid: alterations in normal aging and in !1Alzheimer's disease. !$#cross-references MUID:90287364; PMID:2113204 !$#accession A60355 !'##molecule_type protein !'##residues 18-37,'X',39,'X',41-42 ##label PAL !'##note this protein was found as a soluble 25K derivative in !1cerebrospinal fluid REFERENCE A59011 !$#authors Smith, R.P.; Higuchi, D.A.; Broze Jr., G.J. !$#journal Science (1990) 248:1126-1128 !$#title Platelet coagulation factor XIa-inhibitor, a form of !1Alzheimer amyloid precursor protein. !$#cross-references MUID:90260664; PMID:2111585 !$#accession A59011 !'##molecule_type protein !'##residues 'X',19-33 ##label SMI REFERENCE A38384 !$#authors Bush, A.I.; Martins, R.N.; Rumble, B.; Moir, R.; Fuller, S.; !1Milward, E.; Currie, J.; Ames, D.; Weidemann, A.; Fischer, !1P.; Multhaup, G.; Beyreuther, K.; Masters, C.L. !$#journal J. Biol. Chem. (1990) 265:15977-15983 !$#title The amyloid precursor protein of Alzheimer's disease is !1released by human platelets. !$#cross-references MUID:90368820; PMID:2118534 !$#accession A38384 !'##molecule_type protein !'##residues 18-37,'X',39,'X',41-42,'X',44-45,'X',47 ##label BUS !'##note this protein was purified from normal human platelets, where it !1exists in membrane-associated and soluble forms REFERENCE S29076 !$#authors Seubert, P.; Vigo-Pelfrey, C.; Esch, F.; Lee, M.; Dovey, H.; !1Davis, D.; Sinha, S.; Schlossmacher, M.; Whaley, J.; !1Swindlehurst, C.; McCormack, R.; Wolfert, R.; Selkoe, D.; !1Lieberburg, I.; Schenk, D. !$#journal Nature (1992) 359:325-327 !$#title Isolation and quantification of soluble Alzheimer's !1beta-peptide from biological fluids. !$#cross-references MUID:93024877; PMID:1406936 !$#accession S29076 !'##molecule_type protein !'##residues 672-701 ##label SEU REFERENCE S38252 !$#authors Matsumoto, A.; Fujiwara, Y. !$#journal Eur. J. Biochem. (1993) 217:21-27 !$#title Aberrant proteolysis of the beta-amyloid precursor protein !1in familial Alzheimer's disease lymphoblastoid cells. !$#cross-references MUID:94039038; PMID:8223557 !$#accession S38252 !'##molecule_type protein !'##residues 639-646;654-666;703-716;719-726 ##label MAO REFERENCE S32539 !$#authors Miyazaki, K.; Hasegawa, M.; Funahashi, K.; Umeda, M. !$#journal Nature (1993) 362:839-841 !$#title A metalloproteinase inhibitor domain in Alzheimer amyloid !1protein precursor. !$#cross-references MUID:93241295; PMID:8479521 !$#accession S32539 !'##molecule_type protein !'##residues 18-28;439-446;681-691 ##label MIY REFERENCE S48148 !$#authors Dreyer, R.N.; Bausch, K.M.; Fracasso, P.; Hammond, L.J.; !1Wunderlich, D.; Wirak, D.O.; Davis, G.; Brini, C.M.; !1Buckholz, T.M.; Koenig, G.; Kamarck, M.E.; Tamburini, P.P. !$#journal Eur. J. Biochem. (1994) 224:265-271 !$#title Processing of the pre-beta-amyloid protein by cathepsin D is !1enhanced by a familial Alzheimer's disease mutation. !$#cross-references MUID:95010002; PMID:7523115 !$#accession S48148 !'##molecule_type protein !'##residues 18-27;'X',482-487,'X',489-490;608-613,'X', !1615-617;625-634;669-678 ##label DR2 REFERENCE S48692 !$#authors Kametani, F.; Tanaka, K.; Tokuda, T.; Ikeda, S. !$#journal FEBS Lett. (1994) 351:165-167 !$#title Secretory cleavage site of Alzheimer amyloid precursor !1protein is heterogeneous in Down's syndrome brain. !$#cross-references MUID:94364460; PMID:8082757 !$#accession S48692 !'##molecule_type protein !'##residues 660-701;756-770 ##label KAM3 REFERENCE S51183 !$#authors Matsumoto, A.; Matsumoto, R. !$#journal Eur. J. Biochem. (1994) 225:1055-1062 !$#title Familial Alzheimer's disease cells abnormally accumulate !1beta-amyloid-harbouring peptides preferentially in cytosol !1but not in extracellular fluid. !$#cross-references MUID:95045534; PMID:7957195 !$#accession S51186 !'##molecule_type protein !'##residues 672-677 ##label MAT1 !$#accession S51185 !'##molecule_type protein !'##residues 672-676,'X',678 ##label MAT2 !$#accession S51184 !'##molecule_type protein !'##residues 688-695 ##label MAT3 !$#accession S51183 !'##molecule_type protein !'##residues 688-693,'X',695-697 ##label MAT4 REFERENCE A54238 !$#authors Matsumoto, A.; Fujiwara, Y. !$#journal Biochemistry (1994) 33:3941-3948 !$#title Ca(2+)-dependent 68-kilodalton protease in familial !1Alzheimer's disease cells cleaves the N-terminus of !1beta-amyloid. !$#cross-references MUID:94190922; PMID:8142398 !$#accession A54238 !'##molecule_type protein !'##residues 671-681 ##label MAF !'##note partial cleavage before and after Met-671 is observed REFERENCE I58075 !$#authors Chartier-Harlin, M.C.; Crawford, F.; Houlden, H.; Warren, !1A.; Hughes, D.; Fidani, L.; Goate, A.; Rossor, M.; Roques, !1P.; Hardy, J. !$#journal Nature (1991) 353:844-846 !$#title Early-onset Alzheimer's disease caused by mutations at codon !1717 of the beta-amyloid precursor protein gene. !$#cross-references MUID:92049731; PMID:1944558 !$#accession I58075 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 716-718 ##label CHA !'##cross-references GB:S60983; NID:g237970; PIDN:AAB20156.1; !1PID:g237971 !'##note a mutant sequence with 717-Gly is reported from a patient with !1early-onset Alzheimer's disease; the normal sequence is !1shown in GenBank entry S60983, release 111.0 REFERENCE I52250 !$#authors Yoshioka, K.; Miki, T.; Katsuya, T.; Ogihara, T.; Sakaki, Y. !$#journal Biochem. Biophys. Res. Commun. (1991) 178:1141-1146 !$#title The 717Val----Ile substitution in amyloid precursor protein !1is associated with familial Alzheimer's disease regardless !1of ethnic groups. !$#cross-references MUID:91337051; PMID:1908231 !$#accession I52250 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 715-716,'I',718 ##label YOS !'##cross-references GB:S50522; NID:g233659; PIDN:AAB19483.1; !1PID:g233660 !'##note a mutant sequence with 717-Ile is reported from a patient with !1early-onset Alzheimer's disease; the normal sequence is !1shown in GenBank entry S60983, release 111.0 REFERENCE A38950 !$#authors Hynes, T.R.; Randal, M.; Kennedy, L.A.; Eigenbrot, C.; !1Kossiakoff, A.A. !$#journal Biochemistry (1990) 29:10018-10022 !$#title X-ray crystal structure of the protease inhibitor domain of !1Alzheimer's amyloid beta-protein precursor. !$#cross-references MUID:91104913; PMID:2125487 !$#contents annotation; X-ray crystallography, protease inhibitor !1domain, 1.5 angstroms REFERENCE A50058 !$#authors Hynes, T.R.; Randal, M.; Kennedy, L.A.; Eigenbrot, C.; !1Kossiakoff, A.A. !$#submission submitted to the Brookhaven Protein Data Bank, September !11990 !$#cross-references PDB:1AAP !$#contents annotation; X-ray crystallography, 1.5 angstroms, residues !1287-342 REFERENCE S10737 !$#authors Castro, M.; Marks, C.B.; Nilsson, B.; Anderson, S. !$#journal FEBS Lett. (1990) 267:207-212 !$#title Does the Kunitz domain from the Alzheimer's amyloid beta !1protein precursor inhibit a kallikrein responsible for !1post-translational processing of nerve growth factor !1precursor? !$#cross-references MUID:90336775; PMID:1696210 !$#contents annotation REFERENCE A47335 !$#authors Bush, A.I.; Multhaup, G.; Moir, R.D.; Williamson, T.G.; !1Small, D.H.; Rumble, B.; Pollwein, P.; Beyreuther, K.; !1Masters, C.L. !$#journal J. Biol. Chem. (1993) 268:16109-16112 !$#title A novel zinc(II) binding site modulates the function of the !1betaA4 amyloid protein precursor of Alzheimer's disease. !$#cross-references MUID:93346344; PMID:8344894 !$#contents annotation; zinc binding peptide REFERENCE A58655 !$#authors Nishimoto, I.; Okamoto, T.; Matsuura, Y.; Takahashi, S.; !1Okamoto, T.; Murayama, Y.; Ogata, E. !$#journal Nature (1993) 362:75-79 !$#title Alzheimer amyloid protein precursor complexes with brain !1GTP-binding protein G-0. !$#cross-references MUID:93188965; PMID:8446172 !$#contents annotation; interaction with GTP-binding regulatory protein !1Go REFERENCE S46251 !$#authors Hesse, L.; Beher, D.; Masters, C.L.; Multhaup, G. !$#journal FEBS Lett. (1994) 349:109-116 !$#title The beta-A4 amyloid precursor protein binding to copper. !$#cross-references MUID:94320627; PMID:7913895 !$#contents annotation; copper binding peptides REFERENCE S43644 !$#authors Fabian, H.; Szendrei, G.I.; Mantsch, H.H.; Greenberg, B.D.; !1Oetvoes Jr., L. !$#journal Eur. J. Biochem. (1994) 221:959-964 !$#title Synthetic post-translationally modified human A-beta peptide !1exhibits a markedly increased tendency to form beta-pleated !1sheets in vitro. !$#cross-references MUID:94237160; PMID:8181478 !$#contents annotation; circular dichroism REFERENCE A52735 !$#authors Talafous, J.; Marcinowski, K.J.; Klopman, G.; Zagorski, M.G. !$#submission submitted to the Brookhaven Protein Data Bank, October 1994 !$#cross-references PDB:1AMB !$#contents annotation; conformation by (1)H-NMR, residues 672-699 REFERENCE A58654 !$#authors Talafous, J.; Marcinowski, K.J.; Klopman, G.; Zagorski, M.G. !$#journal Biochemistry (1994) 33:7788-7796 !$#title Solution structure of residues 1-28 of the amyloid !1beta-peptide. !$#cross-references MUID:94281210; PMID:7516706 !$#contents annotation; conformation by (1)H-NMR COMMENT Deposition of fibrillar amyloid proteins intraneuronally as !1neurofibrillary tangles and extracellularly as plaques and !1in blood vessels is characteristic of both Down's syndrome !1and Alzheimer's disease in older persons. The major protein !1found within these deposits is the small, insoluble, and !1highly aggregating amyloid beta protein (A4) that is thought !1to be derived from aberrant degradation of the precursor, a !1glycosylated cell-surface receptor. COMMENT A number of alternative splice forms are produced in various !1tissues. APP(695) which lacks the Kunitz-type proteinase !1inhibitor domain is expressed predominantly in the brain. GENETICS !$#gene GDB:APP !'##cross-references GDB:119692; OMIM:104760 !$#map_position 21q21.2-21q21.2 !$#introns 19/3; 75/3; 119/1; 156/3; 221/2; 289/1; 345/1; 364/1; 408/3; !1433/3; 486/3; 529/3; 563/1; 637/1; 655/1; 688/3; 737/3 FUNCTION !$#description transmembrane receptor coupled to the intracellular !1signaling pathway by interaction with GTP-binding protein G !1(0) CLASSIFICATION #superfamily Alzheimer's disease amyloid beta protein; !1animal Kunitz-type proteinase inhibitor homology KEYWORDS alternative splicing; Alzheimer's disease; amyloid; copper; !1Down's syndrome; glycoprotein; serine proteinase inhibitor; !1transmembrane protein; zinc FEATURE !$1-770 #product amyloid protein precursor splice form APP !8(770) #status predicted #label A770\ !$1-344,'I',365-770 #product amyloid protein precursor splice form APP !8(751) #status predicted #label A751\ !$1-288,'V',365-770 #product amyloid protein precursor splice form APP !8(695) #status predicted #label A695\ !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-770 #product Alzheimer's disease amyloid beta protein !8precursor #status predicted #label MAT\ !$18-699 #domain extracellular #status predicted #label EXT\ !$190-265 #region acidic\ !$291-341 #domain animal Kunitz-type proteinase inhibitor !8homology #label BPI\ !$439-671 #region gelatinase inhibitory #status predicted\ !$672-713 #product amyloid beta protein long, plaque form !8#status predicted #label ALZ\ !$672-710 #product amyloid beta protein short, vascular form !8#status experimental #label AL2\ !$700-723 #domain transmembrane #status predicted #label TMM\ !$724-770 #domain intracellular #status predicted #label INT\ !$108,110 #binding_site copper (His) (type 2) #status !8predicted\ !$147,149 #binding_site copper (His) (type 2) #status !8predicted\ !$149,151 #binding_site copper (His) (type 2) #status !8predicted\ !$183,186,187 #binding_site zinc (Glu, Cys, Cys) #status predicted\ !$291-341,300-324, !$316-337 #disulfide_bonds #status experimental\ !$301 #inhibitory_site Arg (unidentified proteinase) !8#status predicted\ !$388,390 #binding_site copper (His) (type 2) #status !8predicted\ !$542,571 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$670-671 #cleavage_site Lys-Met (calcium-dependent 68K !8proteinase) #status predicted\ !$671-672 #cleavage_site Met-Asp (calcium-dependent 68K !8proteinase) #status predicted\ !$686-687 #cleavage_site Gln-Lys (multicatalytic endopeptidase !8complex) #status predicted\ !$687-688 #cleavage_site Lys-Leu (gelatinase A) #status !8predicted SUMMARY #length 770 #molecular-weight 86943 #checksum 2126 SEQUENCE /// ENTRY A49795 #type complete TITLE Alzheimer's disease amyloid beta protein precursor - crab-eating macaque ORGANISM #formal_name Macaca fascicularis #common_name crab-eating macaque DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A49795 REFERENCE A49795 !$#authors Podlisny, M.B.; Tolan, D.R.; Selkoe, D.J. !$#journal Am. J. Pathol. (1991) 138:1423-1435 !$#title Homology of the amyloid beta protein precursor in monkey and !1human supports a primate model for beta amyloidosis in !1Alzheimer's disease. !$#cross-references MUID:91273117; PMID:1905108 !$#accession A49795 !'##status preliminary !'##molecule_type mRNA !'##residues 1-695 ##label POD !'##cross-references GB:M58727; NID:g342062; PIDN:AAA36829.1; !1PID:g342063 CLASSIFICATION #superfamily Alzheimer's disease amyloid beta protein; !1animal Kunitz-type proteinase inhibitor homology KEYWORDS alternative splicing SUMMARY #length 695 #molecular-weight 78662 #checksum 802 SEQUENCE /// ENTRY BNRT1 #type fragment TITLE brain neuron cytoplasmic protein 1 - rat (fragment) ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 22-Jun-1999 ACCESSIONS A03136 REFERENCE A90836 !$#authors Sutcliffe, J.G.; Milner, R.J.; Shinnick, T.M.; Bloom, F.E. !$#journal Cell (1983) 33:671-682 !$#title Identifying the protein products of brain-specific genes !1with antibodies to chemically synthesized peptides. !$#cross-references MUID:83259254; PMID:6347394 !$#accession A03136 !'##molecule_type mRNA !'##residues 1-83 ##label SUT !'##cross-references GB:V01543; GB:J00755; NID:g56876; PIDN:CAA24784.1; !1PID:g56877 !'##experimental_source clone p1A75 CLASSIFICATION #superfamily brain neuron cytoplasmic protein 1 KEYWORDS brain; cytosol SUMMARY #length 83 #checksum 4308 SEQUENCE /// ENTRY BNRT2 #type complete TITLE brain neuron cytoplasmic protein 2 - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 22-Jun-1999 ACCESSIONS A03137 REFERENCE A90836 !$#authors Sutcliffe, J.G.; Milner, R.J.; Shinnick, T.M.; Bloom, F.E. !$#journal Cell (1983) 33:671-682 !$#title Identifying the protein products of brain-specific genes !1with antibodies to chemically synthesized peptides. !$#cross-references MUID:83259254; PMID:6347394 !$#accession A03137 !'##molecule_type mRNA !'##residues 1-119 ##label SUT !'##cross-references GB:V01543; GB:J00755; NID:g56876; PIDN:CAA24785.1; !1PID:g56878 !'##experimental_source clone p1A75 CLASSIFICATION #superfamily brain neuron cytoplasmic protein 2 KEYWORDS brain; cytosol SUMMARY #length 119 #molecular-weight 13209 #checksum 1319 SEQUENCE /// ENTRY BMHU1Y #type complete TITLE synaptotagmin I - human ALTERNATE_NAMES p65 ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 22-Jun-1999 ACCESSIONS A39052 REFERENCE A39052 !$#authors Perin, M.S.; Johnston, P.A.; Oezcelik, T.; Jahn, R.; !1Francke, U.; Suedhof, T.C. !$#journal J. Biol. Chem. (1991) 266:615-622 !$#title Structural and functional conservation of synaptotagmin !1(p65) in Drosophila and humans. !$#cross-references MUID:91093190; PMID:1840599 !$#accession A39052 !'##molecule_type mRNA !'##residues 1-422 ##label PER !'##cross-references GB:M55047; GB:J05710; NID:g338657; PIDN:AAA60609.1; !1PID:g338658 COMMENT Synaptotagmins are a major component of synaptic vesicle !1membranes and are thought to play a role in synaptic vesicle !1exocytosis. GENETICS !$#gene GDB:SYT1; SYT !'##cross-references GDB:125296; OMIM:185605 !$#map_position 12cen-12q21 CLASSIFICATION #superfamily synaptotagmin; protein kinase C C2 region !1homology KEYWORDS dimer; duplication; glycoprotein; membrane trafficking; !1phospholipid binding; synaptic vesicle; transmembrane !1protein FEATURE !$1-53 #domain intravesicular #status predicted #label INT\ !$54-80 #domain transmembrane #status predicted #label TMM\ !$81-422 #domain extravesicular #status predicted #label EXT\ !$136-382 #region phospholipid binding #status experimental\ !$136-249 #domain protein kinase C C2 region homology #label !8KC2A\ !$267-382 #domain protein kinase C C2 region homology #label !8KC2B\ !$25 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 422 #molecular-weight 47573 #checksum 8264 SEQUENCE /// ENTRY BMRT2Y #type complete TITLE synaptotagmin II - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 22-Jun-1999 ACCESSIONS A39454 REFERENCE A39454 !$#authors Geppert, M.; Archer III, B.T.; Suedhof, T.C. !$#journal J. Biol. Chem. (1991) 266:13548-13552 !$#title Synaptotagmin II. A novel differentially distributed form of !1synaptotagmin. !$#cross-references MUID:91310620; PMID:1856191 !$#accession A39454 !'##molecule_type mRNA !'##residues 1-422 ##label GEP !'##cross-references GB:M64488; NID:g207144; PIDN:AAA63502.1; !1PID:g207145 COMMENT Synaptotagmins are a major component of synaptic vesicle !1membranes and are thought to play a role in synaptic vesicle !1exocytosis. CLASSIFICATION #superfamily synaptotagmin; protein kinase C C2 region !1homology KEYWORDS duplication; glycoprotein; membrane trafficking; !1phospholipid binding; synaptic vesicle; transmembrane !1protein FEATURE !$1-60 #domain intravesicular #status predicted #label INT\ !$61-87 #domain transmembrane #status predicted #label TMM\ !$88-422 #domain extravesicular #status predicted #label EXT\ !$136-382 #region phospholipid binding #status predicted\ !$136-249 #domain protein kinase C C2 region homology #label !8KC2A\ !$267-382 #domain protein kinase C C2 region homology #label !8KC2B\ !$32 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 422 #molecular-weight 47209 #checksum 5077 SEQUENCE /// ENTRY BMFFSY #type complete TITLE synaptotagmin - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES p65 ORGANISM #formal_name Drosophila melanogaster DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 22-Jun-1999 ACCESSIONS B39052 REFERENCE A39052 !$#authors Perin, M.S.; Johnston, P.A.; Oezcelik, T.; Jahn, R.; !1Francke, U.; Suedhof, T.C. !$#journal J. Biol. Chem. (1991) 266:615-622 !$#title Structural and functional conservation of synaptotagmin !1(p65) in Drosophila and humans. !$#cross-references MUID:91093190; PMID:1840599 !$#accession B39052 !'##molecule_type mRNA !'##residues 1-474 ##label PER !'##cross-references GB:M55048; GB:J05711; NID:g158526; PIDN:AAA28925.1; !1PID:g158527 COMMENT Synaptotagmins are a major component of synaptic vesicle !1membranes and are thought to play a role in synaptic vesicle !1exocytosis. GENETICS !$#gene FlyBase:syt !'##cross-references FlyBase:FBgn0004242 !$#map_position 23B CLASSIFICATION #superfamily synaptotagmin; protein kinase C C2 region !1homology KEYWORDS duplication; membrane trafficking; phospholipid binding; !1synaptic vesicle; transmembrane protein FEATURE !$1-107 #domain intravesicular #status predicted #label INT\ !$108-134 #domain transmembrane #status predicted #label TMM\ !$135-474 #domain extravesicular #status predicted #label EXT\ !$186-434 #region phospholipid binding #status experimental\ !$186-300 #domain protein kinase C C2 region homology #label !8KC2A\ !$319-434 #domain protein kinase C C2 region homology #label !8KC2B SUMMARY #length 474 #molecular-weight 53278 #checksum 8722 SEQUENCE /// ENTRY S22700 #type complete TITLE amphiphysin - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S22700 REFERENCE S22700 !$#authors Lichte, B.; Veh, R.W.; Meyer, H.E.; Kilimann, M.W. !$#journal EMBO J. (1992) 11:2521-2530 !$#title Amphiphysin, a novel protein associated with synaptic !1vesicles. !$#cross-references MUID:92331604; PMID:1628617 !$#accession S22700 !'##molecule_type mRNA !'##residues 1-682 ##label LIC !'##cross-references EMBL:X60422; NID:g62842; PIDN:CAA42953.1; !1PID:g62843 CLASSIFICATION #superfamily amphiphysin; RVS161 protein homology FEATURE !$11-270 #domain RVS161 protein homology #label RVS SUMMARY #length 682 #molecular-weight 75205 #checksum 413 SEQUENCE /// ENTRY MPHUPL #type complete TITLE myelin proteolipid protein [validated] - human ALTERNATE_NAMES lipophilin; PLP ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1987 #sequence_revision 18-Aug-1995 #text_change 08-Dec-2000 ACCESSIONS A26665; A26905; A24657; A32988; S13432; I59155; I56568 REFERENCE A26665 !$#authors Diehl, H.J.; Schaich, M.; Budzinski, R.M.; Stoffel, W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:9807-9811 !$#title Individual exons encode the integral membrane domains of !1human myelin proteolipid protein. !$#cross-references MUID:87092337; PMID:3467339 !$#accession A26665 !'##molecule_type DNA !'##residues 1-277 ##label DIE !'##cross-references GB:M15026 REFERENCE A26905 !$#authors Simons, R.; Alon, N.; Riordan, J.R. !$#journal Biochem. Biophys. Res. Commun. (1987) 146:666-671 !$#title Human myelin DM-20 proteolipid protein deletion defined by !1cDNA sequence. !$#cross-references MUID:87298492; PMID:2441695 !$#accession A26905 !'##molecule_type mRNA !'##residues 1-116,152-277 ##label SIM !'##cross-references GB:M17085; NID:g190087; PIDN:AAA60118.1; !1PID:g190088 !'##experimental_source clone pDM-20 REFERENCE A24657 !$#authors Stoffel, W.; Giersiefen, H.; Hillen, H.; Schroeder, W.; !1Tunggal, B. !$#journal Biol. Chem. Hoppe-Seyler (1985) 366:627-635 !$#title Amino-acid sequence of human and bovine brain myelin !1proteolipid protein (lipophilin) is completely conserved. !$#cross-references MUID:86000127; PMID:4041237 !$#accession A24657 !'##molecule_type protein !'##residues 2-35,'EV',38-88,'X',90-143,'C',145-188,'A',190,'C',192-198, !1'T',200-277 ##label STO REFERENCE A32988 !$#authors Gencic, S.; Abuelo, D.; Ambler, M.; Hudson, L.D. !$#journal Am. J. Hum. Genet. (1989) 45:435-442 !$#title Pelizaeus-Merzbacher disease: an X-linked neurologic !1disorder of myelin metabolism with a novel mutation in the !1gene encoding proteolipid protein. !$#cross-references MUID:89371750; PMID:2773936 !$#accession A32988 !'##molecule_type DNA !'##residues 208-215,'S',217-232 ##label GEN !'##note 216-Ser mutation associated with Pelizaeus-Merzbacher disease REFERENCE S13432 !$#authors Weimbs, T.; Dick, T.; Stoffel, W.; Boltshauser, E. !$#journal Biol. Chem. Hoppe-Seyler (1990) 371:1175-1183 !$#title A point mutation at the X-chromosomal proteolipid protein !1locus in Pelizaeus-Merzbacher disease leads to disruption of !1myelinogenesis. !$#cross-references MUID:91214553; PMID:1708672 !$#accession S13432 !'##status preliminary !'##molecule_type DNA !'##residues 152-155,'I',157-180,'TW',183-190 ##label WEI !'##note 156-Ile mutation associated with Pelizaeus-Merzbacher disease REFERENCE I59155 !$#authors Hudson, L.D.; Puckett, C.; Berndt, J.; Chan, J.; Gencic, S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:8128-8131 !$#title Mutation of the proteolipid protein gene PLP in a human X !1chromosome-linked myelin disorder. !$#cross-references MUID:90046751; PMID:2479017 !$#accession I59155 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-139,'T',141-277 ##label RES !'##cross-references GB:M27110; NID:g190084; PIDN:AAA60117.1; !1PID:g190085 REFERENCE I56568 !$#authors Kronquist, K.E.; Crandall, B.F.; Macklin, W.B.; Campagnoni, !1A.T. !$#journal J. Neurosci. Res. (1987) 18:395-401 !$#title Expression of myelin proteins in the developing human spinal !1cord: cloning and sequencing of human proteolipid protein !1cDNA. !$#cross-references MUID:88141333; PMID:2449536 !$#accession I56568 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-184,'D',186-212,'I',214-277 ##label RE2 !'##cross-references GB:M54927; NID:g187416; PIDN:AAA59565.1; !1PID:g187417 COMMENT Five hydrophobic domains are present; three are !1transmembrane domains and two are intramembranous domains. COMMENT Most, and perhaps all, of the Cys residues are involved in !1disulfide bonds. COMMENT This is the major protein of myelin from the central nervous !1system. GENETICS !$#gene GDB:PLP !'##cross-references GDB:120302; OMIM:312080 !$#map_position Xq22-Xq22 !$#introns 2/1; 64/2; 151/3; 208/1; 232/3; 254/3 FUNCTION !$#description with myelin basic protein (see MBHUB) probably maintains !1myelin structure CLASSIFICATION #superfamily myelin proteolipid protein KEYWORDS alternative splicing; lipoprotein; myelin; oligodendrocyte; !1structural protein; thiolester bond; transmembrane protein FEATURE !$2-277 #product myelin proteolipid protein, long form !8#status experimental #label MAT\ !$2-116,152-277 #product myelin proteolipid protein, short form !8#status predicted #label MA2\ !$10-35 #domain transmembrane #status predicted #label TM1\ !$60-97 #domain transmembrane #status predicted #label TM2\ !$152-191 #domain intramembrane #status predicted #label HC1\ !$206-217 #domain intramembrane #status predicted #label HC2\ !$233-268 #domain transmembrane #status predicted #label TM3\ !$109 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$199 #binding_site fatty acid (Ser) (covalent) #status !8predicted SUMMARY #length 277 #molecular-weight 30077 #checksum 3149 SEQUENCE /// ENTRY MPBOPL #type complete TITLE myelin proteolipid protein - bovine ALTERNATE_NAMES Folch-protein; lipophilin; PLP; proteolipid P-II beta' ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 03-Dec-1999 ACCESSIONS A25289; A60217; A24281 REFERENCE A91715 !$#authors Stoffel, W.; Hillen, H.; Schroeder, W.; Deutzmann, R. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1983) 364:1455-1466 !$#title The primary structure of bovine brain myelin lipophilin !1(proteolipid apoprotein). !$#cross-references MUID:84059642; PMID:6642431 !$#accession A25289 !'##molecule_type protein !'##residues 1-276 ##label STO REFERENCE A60217 !$#authors Schindler, P.; Luu, B.; Sorokine, O.; Trifilieff, E.; Van !1Dorsselaer, A. !$#journal J. Neurochem. (1990) 55:2079-2085 !$#title Developmental study of proteolipids in bovine brain: a novel !1proteolipid and DM-20 appear before proteolipid protein !1(PLP) during myelination. !$#cross-references MUID:91038090; PMID:1700073 !$#accession A60217 !'##molecule_type protein !'##residues 1-4,'XX',7-8,'X',10-23,'X',25-31 ##label SCH REFERENCE A93597 !$#authors Naismith, A.L.; Hoffman-Chudzik, E.; Tsui, L.C.; Riordan, !1J.R. !$#journal Nucleic Acids Res. (1985) 13:7413-7425 !$#title Study of the expression of myelin proteolipid protein !1(lipophilin) using a cloned complementary DNA. !$#cross-references MUID:86041923; PMID:3840591 !$#accession A24281 !'##molecule_type mRNA !'##residues 129-142,'K',144-189,'S',191-253,'L',255-276 ##label NAI !'##cross-references GB:X03098; NID:g640; PIDN:CAA26884.1; PID:g641 REFERENCE A35489 !$#authors Bizzozero, O.A.; Good, L.K.; Evans, J.E. !$#journal Biochem. Biophys. Res. Commun. (1990) 170:375-382 !$#title Cysteine-108 is an acylation site in myelin proteolipid !1protein. !$#cross-references MUID:90321254; PMID:1695508 !$#contents annotation; cysteine palmitylation REFERENCE A94001 !$#authors Stoffel, W.; Hillen, H.; Giersiefen, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:5012-5016 !$#title Structure and molecular arrangement of proteolipid protein !1of central nervous system myelin. !$#cross-references MUID:84298072; PMID:6206491 !$#contents annotation; domain structure COMMENT Five hydrophobic domains are present; it is proposed that !1three are transmembrane domains and two are intramembranous !1domains. FUNCTION !$#description with myelin basic protein (see PIR:MBBOB) probably maintains !1myelin structure CLASSIFICATION #superfamily myelin proteolipid protein KEYWORDS acetylated amino end; lipoprotein; myelin; oligodendrocyte; !1structural protein; thiolester bond; transmembrane protein FEATURE !$9-34 #domain transmembrane #status predicted #label TM1\ !$59-96 #domain transmembrane #status predicted #label TM2\ !$151-190 #domain intramembrane #status predicted #label HC1\ !$205-216 #domain intramembrane #status predicted #label HC2\ !$232-267 #domain transmembrane #status predicted #label TM3\ !$1 #modified_site acetylated amino end (Gly) (partial) !8#status experimental\ !$108 #binding_site palmitate (Cys) (covalent) #status !8experimental\ !$198 #binding_site fatty acid (Thr) (covalent) #status !8experimental SUMMARY #length 276 #molecular-weight 29876 #checksum 819 SEQUENCE /// ENTRY MPRTPL #type complete TITLE myelin proteolipid protein - rat ALTERNATE_NAMES lipophilin; PLP ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1987 #sequence_revision 21-Feb-1997 #text_change 22-Jun-1999 ACCESSIONS I52775; A24000; S09379; A25280 REFERENCE I52775 !$#authors Milner, R.J.; Lai, C.; Nave, K. !$#journal Cell (1985) 42:931-939 !$#title Nucleotide sequences of two mRNAs for rat brain myelin !1proteolipid protein. !$#cross-references MUID:86028189; PMID:2414013 !$#accession I52775 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-277 ##label RES !'##cross-references GB:M11185; NID:g206246; PIDN:AAA41898.1; !1PID:g206247 !'##experimental_source brain REFERENCE A24000 !$#authors Dautigny, A.; Alliel, P.M.; d'Auriol, L.; Dinh, D.P.; !1Nussbaum, J.L.; Galibert, F.; Jolles, P. !$#journal FEBS Lett. (1985) 188:33-36 !$#title Molecular cloning and nucleotide sequence of a cDNA clone !1coding for rat brain myelin proteolipid. !$#cross-references MUID:85258131; PMID:2410294 !$#accession A24000 !'##molecule_type mRNA !'##residues 2-277 ##label DAU !'##cross-references GB:X02809; NID:g56698; PIDN:CAA26577.1; PID:g56699 REFERENCE S09379 !$#authors Boison, D.; Stoffel, W. !$#journal EMBO J. (1989) 8:3295-3302 !$#title Myelin-deficient rat: a point mutation in exon III (A -> C, !1Thr75 -> Pro) of the myelin proteolipid protein causes !1dysmyelination and oligodendrocyte death. !$#cross-references MUID:90059921; PMID:2479544 !$#accession S09379 !'##molecule_type DNA !'##residues 65-151 ##label BOI REFERENCE A25280 !$#authors Gardinier, M.V.; Macklin, W.B.; Diniak, A.J.; Deininger, !1P.L. !$#journal Mol. Cell. Biol. (1986) 6:3755-3762 !$#title Characterization of myelin proteolipid mRNAs in normal and !1jimpy mice. !$#cross-references MUID:87089716; PMID:2432393 !$#accession A25280 !'##molecule_type mRNA !'##residues 176-270 ##label GAR COMMENT By homology with the human sequence, five hydrophobic !1domains are present, three of which are transmembrane !1domains and two of which are intramembranous domains. COMMENT Most, and perhaps all, of the Cys residues are involved in !1disulfide bonds. COMMENT This is the major protein of myelin from the central nervous !1system. CLASSIFICATION #superfamily myelin proteolipid protein KEYWORDS alternative splicing; lipoprotein; myelin; oligodendrocyte; !1structural protein; thiolester bond; transmembrane protein FEATURE !$10-35 #domain transmembrane #status predicted #label TM1\ !$60-97 #domain transmembrane #status predicted #label TM2\ !$152-191 #domain intramembrane #status predicted #label HC1\ !$206-217 #domain intramembrane #status predicted #label HC2\ !$233-268 #domain transmembrane #status predicted #label TM3\ !$109 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$196 #binding_site fatty acid (Ser) (covalent) #status !8predicted SUMMARY #length 277 #molecular-weight 30077 #checksum 3149 SEQUENCE /// ENTRY S34792 #type complete TITLE myelin proteolipid protein - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1993 #sequence_revision 12-Apr-1996 #text_change 22-Jun-1999 ACCESSIONS S34792; A25886; S01716; S02370; A27221; A32706; A25926 REFERENCE S34792 !$#authors Macklin, W.B.; Campagnoni, C.W.; Deininger, P.L.; Gardinier, !1M.V. !$#journal J. Neurosci. Res. (1987) 18:383-394 !$#title Structure and expression of the mouse myelin proteolipid !1protein gene. !$#cross-references MUID:88141332; PMID:2449535 !$#accession S34792 !'##molecule_type DNA !'##residues 1-277 ##label MAC1 !'##cross-references EMBL:M37334 REFERENCE A25886 !$#authors Hudson, L.D.; Berndt, J.A.; Puckett, C.; Kozak, C.A.; !1Lazzarini, R.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:1454-1458 !$#title Aberrant splicing of proteolipid protein mRNA in the !1dysmyelinating jimpy mutant mouse. !$#cross-references MUID:87147292; PMID:3469678 !$#accession A25886 !'##molecule_type mRNA !'##residues 1-277 ##label HUD !'##cross-references GB:M15442; GB:M25442; NID:g200410; PIDN:AAA39953.1; !1PID:g200413 REFERENCE S01716 !$#authors Ikenaka, K.; Furuichi, T.; Iwasaki, Y.; Moriguchi, A.; !1Okano, H.; Mikoshiba, K. !$#journal J. Mol. Biol. (1988) 199:587-596 !$#title Myelin proteolipid protein gene structure and its regulation !1of expression in normal and Jimpy mutant mice. !$#cross-references MUID:88172505; PMID:2451027 !$#accession S01716 !'##molecule_type DNA !'##residues 1-68,'P',70-277 ##label IKE !'##cross-references EMBL:X07215 !'##note the authors translated the codon CCG for residue 69 as Gln REFERENCE S02370 !$#authors Macklin, W.B.; Gardinier, M.V.; King, K.D.; Kampf, K. !$#journal FEBS Lett. (1987) 223:417-421 !$#title An AG->GG transition at a splice site in the myelin !1proteolipid protein gene in jimpy mice results in the !1removal of an exon. !$#cross-references MUID:88030089; PMID:2444462 !$#accession S02370 !'##molecule_type DNA !'##residues 1-25 ##label MAC2 !'##cross-references EMBL:X06375 REFERENCE A27221 !$#authors Sorg, B.A.; Smith, M.M.; Campagnoni, A.T. !$#journal J. Neurochem. (1987) 49:1146-1154 !$#title Developmental expression of the myelin proteolipid protein !1and basic protein mRNAs in normal and dysmyelinating mutant !1mice. !$#cross-references MUID:87310464; PMID:2442307 !$#accession A27221 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 50-95,'S',97-277 ##label SOR REFERENCE A32706 !$#authors Nave, K.A.; Lai, C.; Bloom, F.E.; Milner, R.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:5665-5669 !$#title Splice site selection in the proteolipid protein (PLP) gene !1transcript and primary structure of the DM-20 protein of !1central nervous system myelin. !$#cross-references MUID:87289665; PMID:2441390 !$#accession A32706 !'##molecule_type mRNA !'##residues 1-69,'C',71-116,152-277 ##label NAV !'##cross-references GB:M16472; NID:g200408; PIDN:AAA39950.1; !1PID:g200409; GB:J02945 !'##note the authors translated the codon GCT for residue 96 as Ser, and !1TAC for residue 161 as Thr REFERENCE A25926 !$#authors Nave, K.A.; Lai, C.; Bloom, F.E.; Milner, R.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:9264-9268 !$#title Jimpy mutant mouse: A 74-base deletion in the mRNA for !1myelin proteolipid protein and evidence for a primary defect !1in RNA splicing. !$#cross-references MUID:87067491; PMID:3466187 !$#accession A25926 !'##molecule_type mRNA !'##residues 1-69,'C',71-125,'Y',127-207,'VPNDLPPVYCCVC',208,'CCGHTS', !1215-216,'AHLHDCCH',225,'QLRRP' ##label NA2 !'##cross-references GB:M20752; NID:g200426; PIDN:AAA39956.1; !1PID:g200427 !'##note the authors translated the codon GCT for residue 96 as Ser, TAC !1for residue 126 as Thr and CGC for residue 228 as Cys GENETICS !$#introns 2/1; 64/2; 151/3; 208/1; 232/3; 254/3 CLASSIFICATION #superfamily myelin proteolipid protein KEYWORDS alternative splicing; lipoprotein; thiolester bond; !1transmembrane protein FEATURE !$109 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$196 #binding_site fatty acid (Ser) (covalent) #status !8predicted SUMMARY #length 277 #molecular-weight 30077 #checksum 3149 SEQUENCE /// ENTRY MBHUB #type complete TITLE myelin basic protein [validated] - human CONTAINS myelin basic protein precursor, 17.2K splice form; myelin basic protein precursor, 18.5K splice form; myelin basic protein precursor, 20.2K splice form; myelin basic protein precursor, 21.5K splice form ORGANISM #formal_name Homo sapiens #common_name man DATE 18-Dec-1981 #sequence_revision 25-Aug-1995 #text_change 20-Apr-2001 ACCESSIONS S10482; A94106; B94106; A90256; JH0802; A60862; A61420; !1A33273; I54219; I56567; I73634; I56565; S66383; A03139; !1A24153 REFERENCE S10482 !$#authors Streicher, R.; Stoffel, W. !$#journal Biol. Chem. Hoppe-Seyler (1989) 370:503-510 !$#title The organization of the human myelin basic protein gene. !1Comparison with the mouse gene. !$#cross-references MUID:89302693; PMID:2472816 !$#accession S10482 !'##status translation not shown !'##molecule_type DNA !'##residues 1-197 ##label STR !'##cross-references EMBL:X17286; NID:g34490; PIDN:CAA35179.1; !1PID:g1184244 REFERENCE A94106 !$#authors Kamholz, J.; De Ferra, F.; Puckett, C.; Lazzarini, R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:4962-4966 !$#title Identification of three forms of human myelin basic protein !1by cDNA cloning. !$#cross-references MUID:86259714; PMID:2425357 !$#accession A94106 !'##molecule_type mRNA !'##residues 1-59,86-197 ##label KAM !'##cross-references GB:M13577; NID:g187408; PIDN:AAA59562.1; !1PID:g307160 !'##note 18.5K splice form !$#accession B94106 !'##molecule_type mRNA !'##residues 1-197 ##label KA2 !'##note antibody to the exon 2 encoded sequence detected a 21.5K splice !1form !'##note a 17.2K splice form is also described !'##note antibody to the exon 2 encoded sequence detected a 21.5K splice !1form; a 17.2K splice form is also described REFERENCE A90256 !$#authors Carnegie, P.R. !$#journal Biochem. J. (1971) 123:57-67 !$#title Amino acid sequence of the encephalitogenic basic protein !1from human myelin. !$#cross-references MUID:72066400; PMID:4108501 !$#accession A90256 !'##molecule_type protein !'##residues 2-59,86-197 ##label CAR REFERENCE JH0802 !$#authors Proost, P.; Van Damme, J.; Opdenakker, G. !$#journal Biochem. Biophys. Res. Commun. (1993) 192:1175-1181 !$#title Leukocyte gelatinase B cleavage releases encephalitogens !1from human myelin basic protein. !$#cross-references MUID:93282820; PMID:7685161 !$#accession JH0802 !'##molecule_type protein !'##residues 2-59,86-197 ##label PRO !'##experimental_source brain REFERENCE A60862 !$#authors Scoble, H.A.; Whitaker, J.N.; Biemann, K. !$#journal J. Neurochem. (1986) 47:614-616 !$#title Analysis of the primary sequence of human myelin basic !1protein peptides 1-44 and 90-170 by fast atom bombardment !1mass spectrometry. !$#cross-references MUID:86280476; PMID:2426402 !$#accession A60862 !'##molecule_type protein !'##residues 2-45;117-197 ##label SCO !'##note evidence for acetylated amino end REFERENCE A61420 !$#authors Gibson, B.W.; Gilliom, R.D.; Whitaker, J.N.; Biemann, K. !$#journal J. Biol. Chem. (1984) 259:5028-5031 !$#title Amino acid sequence of human myelin basic protein peptide !145-89 as determined by mass spectrometry. !$#cross-references MUID:84185608; PMID:6201481 !$#accession A61420 !'##molecule_type protein !'##residues 46-59,86-116 ##label GIB REFERENCE A33273 !$#authors Wood, D.D.; Moscarello, M.A. !$#journal J. Biol. Chem. (1989) 264:5121-5127 !$#title The isolation, characterization, and lipid-aggregating !1properties of a citrulline containing myelin basic protein. !$#cross-references MUID:89174797; PMID:2466844 !$#accession A33273 !'##molecule_type protein !'##residues 15-25,'X',27-31,'X',33-59,86-148,'X',150-156,'X',158-185, !1'X',187-196,'X' ##label WOO !'##note form C-8; residues designated 'X' were determined as citrulline REFERENCE A90257 !$#authors Baldwin, G.S.; Carnegie, P.R. !$#journal Biochem. J. (1971) 123:69-74 !$#title Isolation and partial characterization of methylated !1arginines from the encephalitogenic basic protein of myelin. !$#cross-references MUID:72066401; PMID:5128665 !$#contents annotation; methylarginine !$#note Arg-134 may be unmodified, monomethylarginine, or !1dimethylarginine in the approximate ratio of 1:6:10 REFERENCE A92806 !$#authors Lennon, V.A.; Wilks, A.V.; Carnegie, P.R. !$#journal J. Immunol. (1970) 105:1223-1230 !$#cross-references MUID:71088405; PMID:4099924 !$#contents annotation !$#note a region including residues 139-149 induces experimental !1autoimmune encephalomyelitis REFERENCE I54219 !$#authors Boylan, K.B.; Ayres, T.M.; Popko, B.; Takahashi, N.; Hood, !1L.E.; Prusiner, S.B. !$#journal Genomics (1990) 6:16-22 !$#title Repetitive DNA (TGGA)n 5' to the human myelin basic protein !1gene: a new form of oligonucleotide repetitive sequence !1showing length polymorphism. !$#cross-references MUID:90152679; PMID:1689270 !$#accession I54219 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-59 ##label RES !'##cross-references GB:M63599; NID:g187402; PIDN:AAA59560.1; !1PID:g187403 REFERENCE I56567 !$#authors Roth, H.J.; Kronquist, K.E.; Kerlero de Rosbo, N.; Crandall, !1B.F.; Campagnoni, A.T. !$#journal J. Neurosci. Res. (1987) 17:321-328 !$#title Evidence for the expression of four myelin basic protein !1variants in the developing human spinal cord through cDNA !1cloning. !$#cross-references MUID:87311781; PMID:2442403 !$#accession I56567 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-132,144-197 ##label RE2 !'##cross-references GB:M30516; NID:g187410; PIDN:AAA59563.1; !1PID:g307161 !$#accession I73634 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-197 ##label RE3 !'##cross-references GB:M30515; NID:g187412; PIDN:AAA59564.1; !1PID:g307162 REFERENCE I56565 !$#authors Roth, H.J.; Kronquist, K.; Pretorius, P.J.; Crandall, B.F.; !1Campagnoni, A.T. !$#journal J. Neurosci. Res. (1986) 16:227-238 !$#title Isolation and characterization of a cDNA coding for a novel !1human 17.3K myelin basic protein (MBP) variant. !$#cross-references MUID:86308101; PMID:2427738 !$#accession I56565 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-59,86-133,145-197 ##label RE4 !'##cross-references GB:M30047; NID:g187400; PIDN:AAA59559.1; !1PID:g307159 REFERENCE S66383 !$#authors Boulias, C.; Pang, H.; Mastronardi, F.; Moscarello, M.A. !$#journal Arch. Biochem. Biophys. (1995) 322:174-182 !$#title The isolation and characterization of four myelin basic !1proteins from the unbound fraction during CM52 !1chromatography. !$#cross-references MUID:96004793; PMID:7574672 !$#accession S66383 !'##molecule_type protein !'##residues 23-25,'X',27-39 ##label BOU COMMENT Four alternatively spliced forms of myelin basic protein !1have been observed, 21.5K, 20.2K, the most abundant 18.5K, !1and 17.2K. GENETICS !$#gene GDB:MBP !'##cross-references GDB:119379; OMIM:159430 !$#map_position 18q22-18qter !$#introns 59/3; 85/3; 120/3; 132/3; 143/3; 183/3 FUNCTION !$#description probably helps maintain myelin structure CLASSIFICATION #superfamily myelin basic protein KEYWORDS acetylated amino end; alternative splicing; citrulline; !1experimental autoimmune encephalomyelitis; methylated amino !1acid; myelin; structural protein FEATURE !$2-197 #product myelin basic protein, 21.5K splice form !8#status predicted #label MAT1\ !$2-132,144-197 #product myelin basic protein, 20.2K splice form !8#status predicted #label MAT2\ !$2-59,86-197 #product myelin basic protein, 18.5K splice form !8#status experimental #label MAT3\ !$2-59,86-132,144-197 #product myelin basic protein, 17.2K splice form !8#status predicted #label MAT4\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental\ !$26,32,149,157,186, !$197 #modified_site citrulline (Arg) (in form C-8) #status !8experimental\ !$134 #modified_site omega-N-methylarginine or omega-N, !8omega-N'-dimethylarginine (Arg) (partial) #status !8experimental SUMMARY #length 197 #molecular-weight 21493 #checksum 4642 SEQUENCE /// ENTRY MBCZB #type complete TITLE myelin basic protein - chimpanzee (tentative sequence) ALTERNATE_NAMES MBP ORGANISM #formal_name Pan troglodytes #common_name chimpanzee DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 06-Sep-1996 ACCESSIONS A03139 REFERENCE A03139 !$#authors Westall, F.C.; Thompson, M.; Kalter, S.S. !$#journal Life Sci. (1975) 17:219-223 !$#title The proposed sequence of the encephalitogenic protein from !1chimpanzee brain. !$#cross-references MUID:76009821; PMID:51459 !$#accession A03139 !'##molecule_type protein !'##residues 1-171 ##label WES COMMENT This protein may function in maintaining the proper !1structure of myelin. CLASSIFICATION #superfamily myelin basic protein KEYWORDS blocked amino end; methylated amino acid; myelin; structural !1protein FEATURE !$1 #modified_site blocked amino end (Ala) (probably !8acetylated) #status experimental\ !$107 #modified_site omega-N-methylarginine or omega-N, !8omega-N'-dimethylarginine (Arg) #status experimental SUMMARY #length 171 #molecular-weight 18560 #checksum 7537 SEQUENCE /// ENTRY MBBOB #type complete TITLE myelin basic protein - bovine ALTERNATE_NAMES myelin A1 protein CONTAINS myelin peptide amide-12 (MPA-12); myelin peptide amide-16 (MPA-16) ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 18-Dec-1981 #sequence_revision 18-Dec-1981 #text_change 07-May-1999 ACCESSIONS A92089; A92160; A92087; S54343; A61641; B61641; A03140 REFERENCE A92089 !$#authors Eylar, E.H.; Brostoff, S.; Hashim, G.; Caccam, J.; Burnett, !1P. !$#journal J. Biol. Chem. (1971) 246:5770-5784 !$#title Basic A1 protein of the myelin membrane. The complete amino !1acid sequence. !$#cross-references MUID:72007306; PMID:5096093 !$#accession A92089 !'##molecule_type protein !'##residues 1,'S',2-169 ##label EYL REFERENCE A92160 !$#authors Brostoff, S.W.; Reuter, W.; Hichens, M.; Eylar, E.H. !$#journal J. Biol. Chem. (1974) 249:559-567 !$#title Specific cleavage of the A1 protein from myelin with !1cathepsin D. !$#cross-references MUID:74070688; PMID:4129204 !$#accession A92160 !'##molecule_type protein !'##residues 1-169 ##label BRO REFERENCE A92087 !$#authors Shapira, R.; McKneally, S.S.; Chou, F.; Kibler, R.F. !$#journal J. Biol. Chem. (1971) 246:4630-4640 !$#title Encephalitogenic fragment of myelin basic protein. Amino !1acid sequence of bovine, rabbit, guinea pig, monkey, and !1human fragments. !$#accession A92087 !'##molecule_type protein !'##residues 43-87 ##label SHA REFERENCE S54343 !$#authors Okazaki, K.; Obata, N.H.; Inoue, S.; Hidaka, H. !$#journal Biochem. J. (1995) 306:551-555 !$#title S100-beta is a target protein of neurocalcin delta, an !1abundant isoform in glial cells. !$#cross-references MUID:95194333; PMID:7887910 !$#accession S54343 !'##molecule_type protein !'##residues 74-75,'HG',78-82,'D',84-88;105,'X',107-108,'X',110-114,'X', !1116-119 ##label OKA REFERENCE A61641 !$#authors Takamatsu, K.; Tatemoto, K. !$#journal Neurochem. Res. (1992) 17:239-246 !$#title Isolation and characterization of two novel peptide amides !1originating from myelin basic protein in bovine brain. !$#cross-references MUID:92319189; PMID:1377792 !$#accession A61641 !'##molecule_type protein !'##residues 1-12 ##label TAK !$#accession B61641 !'##molecule_type protein !'##residues 1-16 ##label TA2 !'##note these peptides have carboxyl-terminal amides probably produced !1by a non-enzymatic reaction REFERENCE A93777 !$#authors Brostoff, S.; Eylar, E.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1971) 68:765-769 !$#title Localization of methylated arginine in the A1 protein from !1myelin. !$#cross-references MUID:71153946; PMID:4994464 !$#contents annotation !$#note Arg-106 is modified to monomethylarginine and !1dimethylarginine REFERENCE A94241 !$#authors Eylar, E.H.; Caccam, J.; Jackson, J.J.; Westall, F.C.; !1Robinson, A.B. !$#journal Science (1970) 168:1220-1223 !$#title Experimental allergic encephalomyelitis: synthesis of !1disease-inducing site of the basic protein. !$#cross-references MUID:70178977; PMID:5442707 !$#contents annotation !$#note the region including residues 114-122 induces experimental !1allergic encephalomyelitis in guinea pigs CLASSIFICATION #superfamily myelin basic protein KEYWORDS acetylated amino end; amidated carboxyl end; experimental !1autoimmune encephalomyelitis; methylated amino acid; myelin FEATURE !$1-169 #product myelin basic protein #status experimental !8#label MAT\ !$1-16 #product myelin peptide amide-16 #status experimental !8#label PA16\ !$1-12 #product myelin peptide amide-12 #status experimental !8#label PA12\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$12 #modified_site amidated carboxyl end (Tyr) (amide in !8mature form myelin peptide amide-12 from following !8leucine) #status atypical\ !$16 #modified_site amidated carboxyl end (Ala) (amide in !8mature form myelin peptide amide-16 from following !8serine) #status atypical\ !$106 #modified_site omega-N-methylarginine or omega-N, !8omega-N'-dimethylarginine (Arg) (partial) #status !8experimental SUMMARY #length 169 #molecular-weight 18323 #checksum 9501 SEQUENCE /// ENTRY MBPGB #type complete TITLE myelin basic protein - pig (tentative sequence) ALTERNATE_NAMES myelin A1 protein CONTAINS myelin basic protein amide 14 ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 19-Apr-1996 #sequence_revision 26-Apr-1996 #text_change 07-May-1999 ACCESSIONS A61640; A36245 REFERENCE A61640 !$#authors Kira, J.; Deibler, G.E.; Krutzsch, H.C.; Martenson, R.E. !$#journal J. Neurochem. (1985) 44:134-142 !$#title Amino acid sequence of porcine myelin basic protein. !$#cross-references MUID:85056964; PMID:2578056 !$#accession A61640 !'##molecule_type protein !'##residues 1-171 ##label KIR !'##note some peptides were ordered by homology REFERENCE A36245 !$#authors Takamatsu, K.; Tatemoto, K. !$#journal Biochem. Biophys. Res. Commun. (1990) 172:1167-1174 !$#title Isolation and characterization of a novel peptide amide from !1porcine brain. !$#cross-references MUID:91058553; PMID:1700904 !$#accession A36245 !'##molecule_type protein !'##residues 1-14 ##label TAK !'##note the sequence in the abstract is inconsistent with that in !1figure 3 in having Glu rather than Gln at positions 3 and 8 !'##note this peptide has a carboxyl-terminal amide probably produced by !1a non-enzymatic reaction CLASSIFICATION #superfamily myelin basic protein KEYWORDS acetylated amino end; amidated carboxyl end; experimental !1autoimmune encephalomyelitis; methylated amino acid; myelin FEATURE !$1-171 #product myelin basic protein #status experimental !8#label MAT\ !$1-14 #product myelin peptide amide-14 #status experimental !8#label PA12\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental\ !$14 #modified_site amidated carboxyl end (Tyr) (amide in !8mature form myelin peptide amide-14 from following !8leucine) #status atypical\ !$107 #modified_site omega-N-methylarginine or omega-N, !8omega-N'-dimethylarginine (Arg) (partial) #status !8experimental SUMMARY #length 171 #molecular-weight 18487 #checksum 7068 SEQUENCE /// ENTRY MBMSB #type complete TITLE golli-myelin basic protein precursor - mouse ALTERNATE_NAMES golli-mbp protein; MBP CONTAINS myelin basic protein ORGANISM #formal_name Mus musculus #common_name house mouse DATE 17-Mar-1987 #sequence_revision 07-Oct-1994 #text_change 22-Jun-1999 ACCESSIONS A45421; B45421; A90875; A90867; A26591; B26591; A60920; !1I48407; I58996; I54033; I53256; A03141; A24772; S25122 REFERENCE A45421 !$#authors Campagnoni, A.T.; Pribyl, T.M.; Campagnoni, C.W.; Kampf, K.; !1Amur-Umarjee, S.; Landry, C.F.; Handley, V.W.; Newman, S.L.; !1Garbay, B.; Kitamura, K. !$#journal J. Biol. Chem. (1993) 268:4930-4938 !$#title Structure and developmental regulation of Golli-mbp, a !1105-kilobase gene that encompasses the myelin basic protein !1gene and is expressed in cells in the oligodendrocyte !1lineage in the brain. !$#cross-references MUID:93186801; PMID:7680345 !$#accession A45421 !'##molecule_type mRNA !'##residues 1-190;217-276;316-328 ##label CAM1 !'##cross-references GB:L07507; NID:g193584 !'##experimental_source clone J37 !'##note sequence extracted from NCBI backbone (NCBIN:126696) and !1modified !$#accession B45421 !'##status preliminary !'##molecule_type mRNA !'##residues 1-191,'SSEP' ##label CAM2 !'##cross-references GB:L07508; NID:g193586; PIDN:AAA37721.1; !1PID:g193587 !'##experimental_source clone BG21 !'##note sequence extracted from NCBI backbone (NCBIN:126700, !1NCBIP:126715) REFERENCE A90875 !$#authors de Ferra, F.; Engh, H.; Hudson, L.; Kamholz, J.; Puckett, !1C.; Molineaux, S.; Lazzarini, R.A. !$#journal Cell (1985) 43:721-727 !$#title Alternative splicing accounts for the four forms of myelin !1basic protein. !$#cross-references MUID:86079555; PMID:2416470 !$#accession A90875 !'##molecule_type mRNA !'##residues 134-328 ##label DEF !'##cross-references GB:L00404; GB:M11669; NID:g199060; PIDN:AAA39502.1; !1PID:g387419 !'##experimental_source 21.5K REFERENCE A90867 !$#authors Takahashi, N.; Roach, A.; Teplow, D.B.; Prusiner, S.B.; !1Hood, L. !$#journal Cell (1985) 42:139-148 !$#title Cloning and characterization of the myelin basic protein !1gene from mouse: one gene can encode both 14 kd and 18.5 kd !1MBPs by alternate use of exons. !$#cross-references MUID:85254913; PMID:2410136 !$#accession A90867 !'##molecule_type DNA !'##residues 134-190;217-328 ##label TAK !'##cross-references GB:M11533; NID:g199044; PIDN:AAA39496.1; !1PID:g387414 !'##experimental_source 18.5K REFERENCE A94188 !$#authors Newman, S.; Kitamura, K.; Campagnoni, A.T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:886-890 !$#title Identification of a cDNA coding for a fifth form of myelin !1basic protein in mouse. !$#cross-references MUID:87118269; PMID:2433693 !$#accession A26591 !'##molecule_type mRNA !'##residues 134-274;316-328 ##label NEW1 !'##cross-references GB:M15060; NID:g199048; PIDN:AAB59711.1; !1PID:g199049 !'##experimental_source clone M722; splice form 17.22K !$#accession B26591 !'##molecule_type mRNA !'##residues 134-190;217-263;275-328 ##label NEW2 !'##cross-references GB:M15062; NID:g199050 !'##experimental_source clone M78; splice form 17.24K REFERENCE A60920 !$#authors Kitamura, K.; Newman, S.L.; Campagnoni, C.W.; Verdi, J.M.; !1Mohandas, T.; Handley, V.W.; Campagnoni, A.T. !$#journal J. Neurochem. (1990) 54:2032-2041 !$#title Expression of a novel transcript of the myelin basic protein !1gene. !$#cross-references MUID:90250449; PMID:1692584 !$#accession A60920 !'##status translation not shown !'##molecule_type mRNA !'##residues 134-190;217-274;316-328 ##label KIT !'##experimental_source M41; splice form 14K REFERENCE I48407 !$#authors Grima, B.; Zelenika, D.; Pessac, B. !$#journal J. Neurochem. (1992) 59:2318-2323 !$#title A novel transcript overlapping the myelin basic protein !1gene. !$#cross-references MUID:93057537; PMID:1279125 !$#accession I48407 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-191,'SSEP' ##label GRI !'##cross-references EMBL:X67319; NID:g51332; PIDN:CAA47733.1; !1PID:g51333 !'##note submitted to the EMBL Data Library, July 1992 REFERENCE I58996 !$#authors Zeller, N.K.; Hunkeler, M.J.; Campagnoni, A.T.; Sprague, J.; !1Lazzarini, R.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:18-22 !$#title Characterization of mouse myelin basic protein messenger !1RNAs with a myelin basic protein cDNA clone. !$#cross-references MUID:84119431; PMID:6198644 !$#accession I58996 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 219-248 ##label ZEL !'##cross-references GB:K00989; NID:g199037; PIDN:AAA39495.1; !1PID:g554195 REFERENCE I54033 !$#authors Miura, M.; Tamura, T. !$#journal Gene (1989) 75:31-38 !$#title The promoter elements of the mouse myelin basic protein gene !1function efficiently in NG108-15 neuronal/glial cells. !$#cross-references MUID:89252919; PMID:2470651 !$#accession I54033 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 134-157 ##label MIU !'##cross-references GB:M24410; NID:g199052; PIDN:AAA39498.1; !1PID:g554196 REFERENCE I53256 !$#authors Okano, H.; Tamura, T.; Miura, M.; Aoyama, A.; Ikenaka, K.; !1Oshimura, M.; Mikoshiba, K. !$#journal EMBO J. (1988) 7:77-83 !$#title Gene organization and transcription of duplicated MBP genes !1of myelin deficient (shi-mld) mutant mouse. !$#cross-references MUID:88196094; PMID:2452084 !$#accession I53256 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 217-229,'HN',232-250 ##label OKA !'##cross-references GB:M36275; NID:g199069; PIDN:AAA39504.1; !1PID:g293725 !'##note hypothetical translation of the reversed and complementary !1sequence to that shown in Figure 7 COMMENT Mice have five forms of myelin basic protein: 21.5K, 18.5K, !117.24K, 17.22K and 14K. GENETICS !$#gene Golli-mbp; shi-mld !$#introns 190/3; 250/3; 262/3; 273/3; 314/3 FUNCTION !$#description probably helps maintain myelin structure CLASSIFICATION #superfamily myelin basic protein KEYWORDS alternative splicing; myelin; structural protein FEATURE !$1-190,217-276, !$316-328 #product Golli-mbp protein (clone J37) #status !8predicted #label MA1\ !$134-328 #product myelin basic protein, splice form 21.5K !8#status predicted #label MAT\ !$134-274,316-328 #product myelin basic protein, splice form 17K-a !8#status predicted #label MA3\ !$134-190,217-328 #product myelin basic protein, splice form 18.5K !8#status predicted #label MA2\ !$134-190,217-263, !$275-328 #product myelin basic protein, splice form 17K-b !8#status predicted #label MA4\ !$134-190,217-274, !$316-328 #product myelin basic protein, splice form 14K !8#status predicted #label MA5 SUMMARY #length 328 #molecular-weight 35706 #checksum 1602 SEQUENCE /// ENTRY MBRTS #type complete TITLE myelin basic protein S - rat ALTERNATE_NAMES small myelin basic protein ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 24-Apr-1984 #sequence_revision 08-Feb-1996 #text_change 22-Jun-1999 ACCESSIONS B24351; A90275; A94243; A21062; A03142 REFERENCE A24351 !$#authors Schaich, M.; Budzinski, R.M.; Stoffel, W. !$#journal Biol. Chem. Hoppe-Seyler (1986) 367:825-834 !$#title Cloned proteolipid protein and myelin basic protein cDNA. !1Transcription of the two genes during myelination. !$#cross-references MUID:87026249; PMID:2429678 !$#accession B24351 !'##molecule_type mRNA !'##residues 1-128 ##label SCH !'##cross-references EMBL:M25889; NID:g205321; PIDN:AAA41575.1; !1PID:g205322 REFERENCE A90275 !$#authors Dunkley, P.R.; Carnegie, P.R. !$#journal Biochem. J. (1974) 141:243-255 !$#title Amino acid sequence of the smaller basic protein from rat !1brain myelin. !$#cross-references MUID:75127359; PMID:4141893 !$#accession A90275 !'##molecule_type protein !'##residues 2-128 ##label DUN !'##note at position 105, arginine, monomethylarginine, and !1dimethylarginine occur in the ratio 4:4:1 !'##note rats have two myelin basic proteins; the smaller one, shown !1above, is missing 40 residues (following residue 114 or 115) !1with respect to the larger ones from other species REFERENCE A94243 !$#authors McFarlin, D.E.; Blank, S.E.; Kibler, R.F.; McKneally, S.; !1Shapira, R. !$#journal Science (1973) 179:478-480 !$#title Experimental allergic encephalomyelitis in the rat: response !1to encephalitogenic proteins and peptides. !$#cross-references MUID:73180720; PMID:4122324 !$#accession A94243 !'##molecule_type protein !'##residues 46-86 ##label MCF !'##note the sequence reported for this encephalitogenic peptide differs !1from that shown by a transposition of residues 47 and 48; !1two other differences are printing errors REFERENCE A21062 !$#authors Roach, A.; Boylan, K.; Horvath, S.; Prusiner, S.B.; Hood, !1L.E. !$#journal Cell (1983) 34:799-806 !$#title Characterization of cloned cDNA representing rat myelin !1basic protein: absence of expression in brain of shiverer !1mutant mice. !$#cross-references MUID:84026484; PMID:6194889 !$#accession A21062 !'##molecule_type mRNA !'##residues 1-124,'I',126-128 ##label ROA !'##experimental_source strain Sprague-Dawley CLASSIFICATION #superfamily myelin basic protein KEYWORDS alternative splicing; blocked amino end; experimental !1autoimmune encephalomyelitis; methylated amino acid; myelin FEATURE !$2-128 #product myelin basic protein S #status experimental !8#label MAT\ !$2 #modified_site blocked amino end (Ala) (in mature !8form) (probably acetylated) #status experimental\ !$105 #modified_site omega-N-methylarginine or omega-N, !8omega-N'-dimethylarginine (Arg) (partial) #status !8experimental SUMMARY #length 128 #molecular-weight 14211 #checksum 2812 SEQUENCE /// ENTRY JH0252 #type complete TITLE myelin P0 protein precursor - human ALTERNATE_NAMES myelin protein zero ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1992 #sequence_revision 06-Dec-1996 #text_change 16-Jun-2000 ACCESSIONS JH0252; JN0704; I39378; I58118 REFERENCE JH0252 !$#authors Hayasaka, K.; Nanao, K.; Tahara, M.; Sato, W.; Takada, G.; !1Miura, M.; Uyemura, K. !$#journal Biochem. Biophys. Res. Commun. (1991) 180:515-518 !$#title Isolation and sequence determination of cDNA encoding the !1major structural protein of human peripheral myelin. !$#cross-references MUID:92062068; PMID:1719967 !$#accession JH0252 !'##molecule_type mRNA !'##residues 1-248 ##label HAY !'##cross-references GB:D10537; GB:D90501; NID:g220073; PIDN:BAA01395.1; !1PID:g220074 !'##experimental_source fetus spinal cord REFERENCE JN0704 !$#authors Hayasaka, K.; Ohnishi, A.; Takada, G.; Fukushima, Y.; Murai, !1Y. !$#journal Biochem. Biophys. Res. Commun. (1993) 194:1317-1322 !$#title Mutation of the myelin Po gene in charcot-marie-tooth !1neuropathy type 1. !$#cross-references MUID:93356807; PMID:7688964 !$#accession JN0704 !'##molecule_type mRNA !'##residues 1-248 ##label HA2 REFERENCE I39378 !$#authors Pham-Dinh, D.; Fourbil, Y.; Blanquet, F.; Mattei, M.G.; !1Roeckel, N.; Latour, P.; Chazot, G.; Vandenberghe, A.; !1Dautigny, A. !$#journal Hum. Mol. Genet. (1993) 2:2051-2054 !$#title The major peripheral myelin protein zero gene: structure and !1localization in the cluster of Fc gamma receptor genes on !1human chromosome 1q21.3-q23. !$#cross-references MUID:94154677; PMID:7509228 !$#accession I39378 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-248 ##label RES !'##cross-references GB:L24893; NID:g454412; PIDN:AAA20656.1; !1PID:g529405 REFERENCE I58118 !$#authors Kulkens, T.; Bolhuis, P.A.; Wolterman, R.A.; Kemp, S.; te !1Nijenhuis, S.; Valentijn, L.J.; Hensels, G.W.; Jennekens, !1F.G.; de Visser, M.; Hoogendijk, J.E. !$#journal Nature Genet. (1993) 5:35-39 !$#title Deletion of the serine 34 codon from the major peripheral !1myelin protein P0 gene in Charcot-Marie-Tooth disease type !11B. !$#cross-references MUID:94035114; PMID:7693130 !$#accession I58118 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-62,64-115 ##label RE2 !'##cross-references GB:S66705; NID:g437048; PIDN:AAB28708.1; !1PID:g437049 !'##experimental_source disease-state mutant COMMENT This protein, a small integral membrane glycoprotein, is the !1most abundant protein component of mammalian peripheral !1myelin. COMMENT This protein plays essential roles in both the elaboration !1and the subsequent compaction of the myelin sheath. GENETICS !$#gene GDB:MPZ; CMT1; CMT1B; HMSNIB !'##cross-references GDB:125266; OMIM:159440 !$#map_position 1q22-1q23 !$#introns 23/1; 78/3; 150/1; 195/2; 215/3 CLASSIFICATION #superfamily myelin P0 protein; immunoglobulin homology KEYWORDS glycoprotein; membrane protein; myelin; Schwann cell; !1structural protein FEATURE !$1-29 #domain signal sequence #status predicted #label SIG\ !$30-248 #product peripheral myelin #status predicted #label !8PER\ !$43-129 #domain immunoglobulin homology #label IMM\ !$50-127 #disulfide_bonds #status predicted\ !$122 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 248 #molecular-weight 27555 #checksum 8376 SEQUENCE /// ENTRY MPRT0 #type complete TITLE myelin P0 protein precursor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 18-Feb-1995 ACCESSIONS JQ0622; A22822 REFERENCE JQ0622 !$#authors Lemke, G.; Lamar, E.; Patterson, J. !$#journal Neuron (1988) 1:73-83 !$#title Isolation and analysis of the gene encoding peripheral !1myelin protein zero. !$#cross-references MUID:90166482; PMID:2483091 !$#accession JQ0622 !'##molecule_type DNA !'##residues 1-248 ##label LEM REFERENCE A22822 !$#authors Lemke, G.; Axel, R. !$#journal Cell (1985) 40:501-508 !$#title Isolation and sequence of a cDNA encoding the major !1structural protein of peripheral myelin. !$#cross-references MUID:85124601; PMID:2578885 !$#accession A22822 !'##molecule_type mRNA !'##residues 1-248 ##label LEM2 COMMENT This protein is found only in peripheral nervous system !1Schwann cells. GENETICS !$#introns 23/1; 78/3; 150/1; 195/2; 215/3 CLASSIFICATION #superfamily myelin P0 protein; immunoglobulin homology KEYWORDS glycoprotein; myelin; Schwann cell; structural protein; !1transmembrane protein FEATURE !$1-29 #domain signal sequence #status predicted #label SIG\ !$30-248 #product myelin P0 protein #status predicted #label !8MAT\ !$30-153 #domain extracellular #status predicted #label EXD\ !$43-129 #domain immunoglobulin homology #label IMM\ !$154-179 #domain transmembrane #status predicted #label TMD\ !$180-248 #domain intracellular #status predicted #label IND\ !$122 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 248 #molecular-weight 27570 #checksum 9341 SEQUENCE /// ENTRY A54662 #type complete TITLE myelin P0 protein - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jan-2000 ACCESSIONS A54662 REFERENCE A54662 !$#authors You, K.H.; Hsieh, C.L.; Hayes, C.; Stahl, N.; Francke, U.; !1Popko, B. !$#journal Genomics (1991) 9:751-757 !$#title DNA sequence, genomic organization, and chromosomal !1localization of the mouse peripheral myelin protein zero !1gene: identification of polymorphic alleles. !$#cross-references MUID:91244320; PMID:1709914 !$#accession A54662 !'##status preliminary !'##molecule_type DNA !'##residues 1-247 ##label YOU !'##cross-references GB:M62427 CLASSIFICATION #superfamily myelin P0 protein; immunoglobulin homology FEATURE !$43-128 #domain immunoglobulin homology #label IMM SUMMARY #length 247 #molecular-weight 27524 #checksum 6320 SEQUENCE /// ENTRY A29128 #type complete TITLE myelin P0 protein - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jan-2000 ACCESSIONS A29128 REFERENCE A29128 !$#authors Sakamoto, Y.; Kitamura, K.; Yoshimura, K.; Nishijima, T.; !1Uyemura, K. !$#journal J. Biol. Chem. (1987) 262:4208-4214 !$#title Complete amino acid sequence of P0 protein in bovine !1peripheral nerve myelin. !$#cross-references MUID:87166035; PMID:2435734 !$#accession A29128 !'##molecule_type protein !'##residues 1-219 ##label SAK CLASSIFICATION #superfamily myelin P0 protein; immunoglobulin homology KEYWORDS glycoprotein; membrane protein; myelin; phosphoprotein; !1Schwann cell; structural protein FEATURE !$14-100 #domain immunoglobulin homology #label IMM SUMMARY #length 219 #molecular-weight 24710 #checksum 9913 SEQUENCE /// ENTRY A61087 #type complete TITLE myelin P0 glycoprotein precursor - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jan-2000 ACCESSIONS A61087 REFERENCE A61087 !$#authors Barbu, M. !$#journal J. Neurosci. Res. (1990) 25:143-151 !$#title Molecular cloning of cDNAs that encode the chicken Po !1protein: evidence for early expression in avians. !$#cross-references MUID:90204597; PMID:1690817 !$#accession A61087 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-249 ##label BAR COMMENT This protein is found only in peripheral nervous system !1Schwann cells. CLASSIFICATION #superfamily myelin P0 protein; immunoglobulin homology KEYWORDS glycoprotein; myelin; Schwann cell; structural protein; !1transmembrane protein FEATURE !$1-29 #domain signal sequence #status predicted #label SIG\ !$30-249 #product myelin P0 glycoprotein #status predicted !8#label MAT\ !$30-153 #domain extracellular #status predicted #label EXT\ !$43-129 #domain immunoglobulin homology #label IMM\ !$154-179 #domain transmembrane #status predicted #label TMM\ !$180-249 #domain intracellular #status predicted #label INT\ !$122 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 249 #molecular-weight 27466 #checksum 1317 SEQUENCE /// ENTRY A32999 #type complete TITLE myelin P0 protein precursor - horn shark ORGANISM #formal_name Heterodontus francisci #common_name horn shark DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A32999 REFERENCE A32999 !$#authors Saavedra, R.A.; Fors, L.; Aebersold, R.H.; Arden, B.; !1Horvath, S.; Sanders, J.; Hood, L. !$#journal J. Mol. Evol. (1989) 29:149-156 !$#title The myelin proteins of the shark brain are similar to the !1myelin proteins of the mammalian peripheral nervous system. !$#cross-references MUID:90040744; PMID:2478717 !$#accession A32999 !'##status preliminary !'##molecule_type mRNA !'##residues 1-246 ##label SAA !'##cross-references GB:X16714; NID:g63976; PIDN:CAB37865.1; !1PID:g4467434 CLASSIFICATION #superfamily myelin P0 protein; immunoglobulin homology KEYWORDS glycoprotein; membrane protein; myelin; Schwann cell; !1structural protein FEATURE !$41-127 #domain immunoglobulin homology #label IMM SUMMARY #length 246 #molecular-weight 27335 #checksum 4295 SEQUENCE /// ENTRY MPHU2 #type complete TITLE myelin P2 protein [validated] - human ALTERNATE_NAMES peripheral myelin protein 2 ORGANISM #formal_name Homo sapiens #common_name man DATE 05-Apr-1983 #sequence_revision 27-Jan-1995 #text_change 08-Dec-2000 ACCESSIONS JT0977; A03143; S24224 REFERENCE JT0977 !$#authors Hayasaka, K.; Nanao, K.; Tahara, M.; Sato, W.; Takada, G.; !1Miura, M.; Uyemura, K. !$#journal Biochem. Biophys. Res. Commun. (1991) 181:204-207 !$#title Isolation and sequence determination of cDNA encoding P2 !1protein of human peripheral myelin. !$#cross-references MUID:92068191; PMID:1720307 !$#accession JT0977 !'##molecule_type mRNA !'##residues 1-132 ##label HAY !'##cross-references EMBL:X62167; NID:g35185; PIDN:CAA44096.1; !1PID:g35186 !'##experimental_source fetal spinal cord peripheral myelin !'##note authors did not translate the codon for residue 1 REFERENCE A03143 !$#authors Suzuki, M.; Kitamura, K.; Sakamoto, Y.; Uyemura, K. !$#journal J. Neurochem. (1982) 39:1759-1762 !$#title The complete amino acid sequence of human P2 protein. !$#cross-references MUID:83058785; PMID:6183401 !$#accession A03143 !'##molecule_type protein !'##residues 2-98,'N',100-110,'D',112-132 ##label SUZ COMMENT P2 protein and myelin basic protein together constitute a !1major fraction of peripheral nervous system myelin protein. GENETICS !$#gene GDB:PMP2 !'##cross-references GDB:129030; OMIM:170715 !$#map_position 8q21.3-8q22.1 CLASSIFICATION #superfamily myelin P2 protein KEYWORDS acetylated amino end; myelin; phosphoprotein FEATURE !$2-132 #product myelin P2 protein #status experimental !8#label MAT\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental\ !$20 #binding_site phosphate (Tyr) (covalent) #status !8predicted\ !$118-125 #disulfide_bonds #status experimental SUMMARY #length 132 #molecular-weight 14909 #checksum 8103 SEQUENCE /// ENTRY MPBO2 #type complete TITLE myelin P2 protein - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Aug-1980 #sequence_revision 31-Aug-1980 #text_change 05-Aug-1994 ACCESSIONS A03144 REFERENCE A03144 !$#authors Kitamura, K.; Suzuki, M.; Suzuki, A.; Uyemura, K. !$#journal FEBS Lett. (1980) 115:27-30 !$#title The complete amino acid sequence of the P2 protein in bovine !1peripheral nerve myelin. !$#cross-references MUID:80225120; PMID:6156092 !$#accession A03144 !'##molecule_type protein !'##residues 1-131 ##label KIT CLASSIFICATION #superfamily myelin P2 protein KEYWORDS acetylated amino end FEATURE !$1 #modified_site acetylated amino end (Ser) #status !8experimental\ !$117-124 #disulfide_bonds #status experimental SUMMARY #length 131 #molecular-weight 14818 #checksum 6122 SEQUENCE /// ENTRY MPRB2 #type complete TITLE myelin P2 protein - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 30-Jun-1980 #sequence_revision 10-May-1996 #text_change 22-Jun-1999 ACCESSIONS A28081; A92266; A92372; A03145 REFERENCE A28081 !$#authors Narayanan, V.; Barbosa, E.; Reed, R.; Tennekoon, G. !$#journal J. Biol. Chem. (1988) 263:8332-8337 !$#title Characterization of a cloned cDNA encoding rabbit myelin P-2 !1protein. !$#cross-references MUID:88228063; PMID:2453513 !$#accession A28081 !'##molecule_type mRNA !'##residues 1-132 ##label NAR !'##cross-references GB:J03744; NID:g165657; PIDN:AAA31451.1; !1PID:g165658 !'##note translation of initiator Met is not shown REFERENCE A92266 !$#authors Ishaque, A.; Hofmann, T.; Rhee, S.; Eylar, E.H. !$#journal J. Biol. Chem. (1980) 255:1058-1063 !$#title The NH-2-terminal region of the P2 protein from rabbit !1sciatic nerve myelin. !$#cross-references MUID:80094496; PMID:7356651 !$#accession A92266 !'##molecule_type protein !'##residues 2-56 ##label IS1 REFERENCE A92372 !$#authors Ishaque, A.; Hofmann, T.; Eylar, E.H. !$#journal J. Biol. Chem. (1982) 257:592-595 !$#title The complete amino acid sequence of thr rabbit P2 protein. !$#cross-references MUID:82098098; PMID:6172423 !$#accession A92372 !'##molecule_type protein !'##residues 56-72,'Q',74-83,'T',85-98,'N',100-132 ##label IS2 COMMENT P2 protein and myelin basic protein together constitute a !1major fraction of peripheral nervous system myelin protein. CLASSIFICATION #superfamily myelin P2 protein KEYWORDS acetylated amino end; myelin; phosphoprotein FEATURE !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental\ !$20 #binding_site phosphate (Tyr) (covalent) #status !8predicted\ !$118-125 #disulfide_bonds #status predicted SUMMARY #length 132 #molecular-weight 14922 #checksum 5737 SEQUENCE /// ENTRY FZHUF #type complete TITLE fatty acid-binding protein, adipocyte - human ALTERNATE_NAMES adipocyte lipid-binding protein (ALBP); fatty acid binding protein 4 (FABP4) ORGANISM #formal_name Homo sapiens #common_name man DATE 20-Dec-1989 #sequence_revision 03-May-1996 #text_change 22-Jun-1999 ACCESSIONS A33363 REFERENCE A33363 !$#authors Baxa, C.A.; Sha, R.S.; Buelt, M.K.; Smith, A.J.; Matarese, !1V.; Chinander, L.L.; Boundy, K.L.; Bernlohr, D.A. !$#journal Biochemistry (1989) 28:8683-8690 !$#title Human adipocyte lipid-binding protein: purification of the !1protein and cloning of its complementary DNA. !$#cross-references MUID:90105397; PMID:2481498 !$#accession A33363 !'##molecule_type mRNA !'##residues 1-132 ##label BAX !'##cross-references GB:J02874; NID:g178346; PIDN:AAA51689.1; !1PID:g178347 !'##experimental_source subcutaneous fat GENETICS !$#gene GDB:FABP4 !'##cross-references GDB:128030 !$#map_position 1p33-1p32 CLASSIFICATION #superfamily myelin P2 protein KEYWORDS blocked amino end; lipid binding; phosphoprotein FEATURE !$2 #modified_site blocked amino end (Cys) (in mature !8form) (probably acetylated) #status experimental\ !$20 #binding_site phosphate (Tyr) (covalent) #status !8predicted\ !$127,129 #binding_site fatty acid (Arg, Tyr) #status predicted SUMMARY #length 132 #molecular-weight 14719 #checksum 6627 SEQUENCE /// ENTRY FZHUC #type complete TITLE fatty acid-binding protein, cardiac and skeletal muscle - human ALTERNATE_NAMES fatty acid-binding protein 3 (FABP3) ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1991 #sequence_revision 03-May-1996 #text_change 16-Jul-1999 ACCESSIONS S15432; JH0199; S00603; I54275; A27248 REFERENCE S15432 !$#authors Peeters, R.A.; Veerkamp, J.H.; van Kessel, A.G.; Kanda, T.; !1Ono, T. !$#journal Biochem. J. (1991) 276:203-207 !$#title Cloning of the cDNA encoding human skeletal-muscle !1fatty-acid-binding protein, its peptide sequence and !1chromosomal localization. !$#cross-references MUID:91248148; PMID:1710107 !$#accession S15432 !'##molecule_type mRNA; protein !'##residues 1-133 ##label PEE !'##cross-references EMBL:X56549; NID:g31292; PIDN:CAA39889.1; !1PID:g31293 !'##experimental_source heart muscle; skeletal muscle REFERENCE JH0199 !$#authors Boerchers, T.; Hojrup, P.; Nielsen, S.U.; Roepstorff, P.; !1Spener, F.; Knudsen, J. !$#journal Mol. Cell. Biochem. (1990) 98:127-133 !$#title Revision of the amino acid sequence of human heart fatty !1acid-binding protein. !$#cross-references MUID:91094793; PMID:2266954 !$#accession JH0199 !'##molecule_type protein !'##residues 2-129,'Q',131-133 ##label BOE REFERENCE S00603 !$#authors Offner, G.D.; Brecher, P.; Sawlivich, W.B.; Costello, C.E.; !1Troxler, R.F. !$#journal Biochem. J. (1988) 252:191-198 !$#title Characterization and amino acid sequence of a fatty !1acid-binding protein from human heart. !$#cross-references MUID:88339792; PMID:3421901 !$#accession S00603 !'##molecule_type protein !'##residues 2-104,'K',106-124,'S',126-133 ##label OFF !'##note submitted to the Protein Sequence Database, May 1988 REFERENCE A49251 !$#authors Zanotti, G.; Scapin, G.; Spadon, P.; Veerkamp, J.H.; !1Sacchettini, J.C. !$#journal J. Biol. Chem. (1992) 267:18541-18550 !$#title Three-dimensional structure of recombinant human muscle !1fatty acid-binding protein. !$#cross-references MUID:92406763; PMID:1526991 !$#contents annotation; X-ray crystallography, 2.1 angstroms !$#note recombinant protein expressed in Escherichia coli REFERENCE I54275 !$#authors Troxler, R.F.; Offner, G.D.; Jiang, J.W.; Wu, B.L.; Skare, !1J.C.; Milunsky, A.; Wyandt, H.E. !$#journal Hum. Genet. (1993) 92:563-566 !$#title Localization of the gene for human heart fatty acid binding !1protein to chromosome 1p32-1p33. !$#cross-references MUID:94085953; PMID:8262516 !$#accession I54275 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 15-133 ##label RES !'##cross-references GB:S67314; NID:g458861; PIDN:AAB29294.1; !1PID:g458862 GENETICS !$#gene GDB:FABP3 !'##cross-references GDB:128008; OMIM:134651 !$#map_position 1p33-1p32 CLASSIFICATION #superfamily myelin P2 protein KEYWORDS acetylated amino end; cardiac muscle; heart; lipid binding; !1phosphoprotein FEATURE !$2 #modified_site acetylated amino end (Val) (in mature !8form) #status experimental\ !$20 #binding_site phosphate (Tyr) (covalent) #status !8predicted\ !$127,129 #binding_site fatty acid (Arg, Tyr) #status !8experimental SUMMARY #length 133 #molecular-weight 14858 #checksum 7533 SEQUENCE /// ENTRY RJHU1 #type complete TITLE retinoic acid-binding protein I, cellular - human ALTERNATE_NAMES CRABP I ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 22-Jun-1999 ACCESSIONS JH0548; A40982; A44867 REFERENCE A44867 !$#authors Eller, M.S.; Oleksiak, M.F.; McQuaid, T.J.; McAfee, S.G.; !1Gilchrest, B.A. !$#journal Exp. Cell Res. (1992) 198:328-336 !$#title The molecular cloning and expression of two CRABP cDNAs from !1human skin. !$#cross-references MUID:92104256; PMID:1309505 !$#accession JH0548 !'##molecule_type mRNA !'##residues 1-137 ##label ELL !'##cross-references GB:S74445; NID:g241541; PIDN:AAB20773.1; !1PID:g241542 REFERENCE A40982 !$#authors Astroem, A.; Tavakkol, A.; Pettersson, U.; Cromie, M.; !1Elder, J.T.; Voorhees, J.J. !$#journal J. Biol. Chem. (1991) 266:17662-17666 !$#title Molecular cloning of two human cellular retinoic !1acid-binding proteins (CRABP). Retinoic acid-induced !1expression of CRABP-II but not CRABP-I in adult human skin !1in vivo and in skin fibroblasts in vitro. !$#cross-references MUID:91373396; PMID:1654334 !$#accession A40982 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-137 ##label AST COMMENT This protein is involved in mediating the action of retinoic !1acid. GENETICS !$#gene GDB:CRABP1; RBP5 !'##cross-references GDB:120343; OMIM:180230 !$#map_position 15q24-15q24 CLASSIFICATION #superfamily myelin P2 protein KEYWORDS lipid binding; transport protein; vitamin A FEATURE !$2-137 #product retinoic acid-binding protein I, cellular !8#status predicted #label MAT\ !$132,134 #binding_site retinoic acid (Arg, Tyr) #status !8predicted SUMMARY #length 137 #molecular-weight 15565 #checksum 3665 SEQUENCE /// ENTRY RJBOA #type complete TITLE retinoic acid-binding protein, cellular - bovine ALTERNATE_NAMES CRABP ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 05-Apr-1983 #sequence_revision 02-Dec-1994 #text_change 22-Jun-1999 ACCESSIONS A32704; S00400; B40902; A92528; A91295; A03151 REFERENCE A32704 !$#authors Shubeita, H.E.; Sambrook, J.F.; McCormick, A.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:5645-5649 !$#title Molecular cloning and analysis of functional cDNA and !1genomic clones encoding bovine cellular retinoic !1acid-binding protein. !$#cross-references MUID:87289661; PMID:3039499 !$#accession A32704 !'##molecule_type DNA; mRNA !'##residues 1-137 ##label SH2 REFERENCE S00400 !$#authors Nilsson, M.H.L.; Spurr, N.K.; Saksena, P.; Busch, C.; !1Nordlinder, H.; Peterson, P.A.; Rask, L.; Sundelin, J. !$#journal Eur. J. Biochem. (1988) 173:45-51 !$#title Isolation and characterization of a cDNA clone corresponding !1to bovine cellular retinoic-acid-binding protein and !1chromosomal localization of the corresponding human gene. !$#cross-references MUID:88185327; PMID:2833392 !$#accession S00400 !'##molecule_type mRNA !'##residues 1-137 ##label NIL !'##cross-references EMBL:X07436; NID:g283; PIDN:CAA30317.1; PID:g284 !'##experimental_source adrenal gland REFERENCE A40902 !$#authors Wei, L.N.; Mertz, J.R.; Goodman, D.S.; Nguyen-Huu, M.C. !$#journal Mol. Endocrinol. (1987) 1:526-534 !$#title Cellular retinoic acid- and cellular retinol-binding !1proteins: complementary deoxyribonucleic acid cloning, !1chromosomal assignment, and tissue specific expression. !$#cross-references MUID:91042593; PMID:2856408 !$#accession B40902 !'##molecule_type mRNA !'##residues 1-137 ##label WEI !'##cross-references GB:M63808 REFERENCE A92528 !$#authors Sundelin, J.; Das, S.R.; Eriksson, U.; Rask, L.; Peterson, !1P.A. !$#journal J. Biol. Chem. (1985) 260:6494-6499 !$#title The primary structure of bovine cellular retinoic !1acid-binding protein. !$#cross-references MUID:85207646; PMID:2581956 !$#accession A92528 !'##molecule_type protein !'##residues 2-137 ##label SUN !'##experimental_source adrenal gland REFERENCE A91295 !$#authors Crabb, J.W.; Saari, J.C. !$#journal FEBS Lett. (1981) 130:15-18 !$#title N-terminal sequence homology among retinoid-binding proteins !1from bovine retina. !$#cross-references MUID:82027750; PMID:6269887 !$#accession A91295 !'##molecule_type protein !'##residues 2-30 ##label CRA !'##experimental_source retina GENETICS !$#gene CRABP !$#introns 24/1; 83/3; 121/3 CLASSIFICATION #superfamily myelin P2 protein KEYWORDS lipid binding; transport protein; vitamin A FEATURE !$2-137 #product retinoic acid-binding protein, cellular !8#status experimental #label MAT\ !$132,134 #binding_site retinoic acid (Arg, Tyr) #status !8predicted SUMMARY #length 137 #molecular-weight 15591 #checksum 4100 SEQUENCE /// ENTRY RJHU2 #type complete TITLE retinoic acid-binding protein II, cellular - human ALTERNATE_NAMES CRABP-II ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 22-Jun-1999 ACCESSIONS A45057; B40982; JH0549 REFERENCE A45057 !$#authors Astrom, A.; Pettersson, U.; Voorhees, J.J. !$#journal J. Biol. Chem. (1992) 267:25251-25255 !$#title Structure of the human cellular retinoic acid-binding !1protein II gene. Early transcriptional regulation by !1retinoic acid. !$#cross-references MUID:93094236; PMID:1334086 !$#accession A45057 !'##molecule_type DNA !'##residues 1-138 ##label AS1 !'##cross-references GB:M97815; NID:g181028; PIDN:AAA58430.1; !1PID:g181030 !'##experimental_source placenta !'##note sequence extracted from NCBI backbone (NCBIP:120193) REFERENCE A40982 !$#authors Astroem, A.; Tavakkol, A.; Pettersson, U.; Cromie, M.; !1Elder, J.T.; Voorhees, J.J. !$#journal J. Biol. Chem. (1991) 266:17662-17666 !$#title Molecular cloning of two human cellular retinoic !1acid-binding proteins (CRABP). Retinoic acid-induced !1expression of CRABP-II but not CRABP-I in adult human skin !1in vivo and in skin fibroblasts in vitro. !$#cross-references MUID:91373396; PMID:1654334 !$#accession B40982 !'##molecule_type mRNA !'##residues 1-138 ##label AS2 !'##cross-references GB:M68867; NID:g181025; PIDN:AAA52068.1; !1PID:g181026 REFERENCE JH0548 !$#authors Eller, M.S.; Oleksiak, M.F.; McQuaid, T.J.; McAfee, S.G.; !1Gilchrest, B.A. !$#journal Exp. Cell Res. (1992) 199:328-336 !$#title The molecular cloning and expression of two CRABP cDNAs from !1human skin. !$#accession JH0549 !'##molecule_type mRNA !'##residues 1-138 ##label ELL COMMENT This protein is involved in mediating the action of retinoic !1acid. GENETICS !$#gene GDB:CRABP2 !'##cross-references GDB:134819; OMIM:180231 !$#map_position 1q21.3-1q21.3 !$#introns 24/1; 83/3; 122/3 CLASSIFICATION #superfamily myelin P2 protein KEYWORDS lipid binding; transport protein; vitamin A FEATURE !$2-138 #product retinoic acid-binding protein II, cellular !8#status predicted #label MAT\ !$133,135 #binding_site retinoic acid (Arg, Tyr) #status !8predicted SUMMARY #length 138 #molecular-weight 15693 #checksum 6424 SEQUENCE /// ENTRY RJHUO #type complete TITLE retinol-binding protein, cellular - human ALTERNATE_NAMES cellular retinol-binding protein 2; CRBP ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1989 #sequence_revision 10-May-1996 #text_change 21-Jul-2000 ACCESSIONS S00399; S02300; A40902 REFERENCE S00399 !$#authors Nilsson, M.H.L.; Spurr, N.K.; Lundvall, J.; Rask, L.; !1Peterson, P.A. !$#journal Eur. J. Biochem. (1988) 173:35-44 !$#title Human cellular retinol-binding protein gene organization and !1chromosomal location. !$#cross-references MUID:88185326; PMID:3356192 !$#accession S00399 !'##molecule_type DNA !'##residues 1-135 ##label NIL !'##cross-references EMBL:X07437; NID:g30207; PIDN:CAA30318.1; !1PID:g4378977 REFERENCE S02300 !$#authors Colantuoni, V.; Cortese, R.; Nilsson, M.; Lundvall, J.; !1Bavik, C.O.; Eriksson, U.; Peterson, P.A.; Sundelin, J. !$#journal Biochem. Biophys. Res. Commun. (1985) 130:431-439 !$#title Cloning and sequencing of a full length cDNA corresponding !1to human cellular retinol-binding protein. !$#cross-references MUID:85279409; PMID:2992469 !$#accession S02300 !'##molecule_type mRNA !'##residues 1-135 ##label COL !'##cross-references GB:M11433; NID:g190947; PIDN:AAA60257.1; !1PID:g190948 REFERENCE A40902 !$#authors Wei, L.N.; Mertz, J.R.; Goodman, D.S.; Nguyen-Huu, M.C. !$#journal Mol. Endocrinol. (1987) 1:526-534 !$#title Cellular retinoic acid- and cellular retinol-binding !1proteins: complementary deoxyribonucleic acid cloning, !1chromosomal assignment, and tissue specific expression. !$#cross-references MUID:91042593; PMID:2856408 !$#accession A40902 !'##molecule_type mRNA !'##residues 1-121 ##label WEI !'##cross-references GB:M63809 GENETICS !$#gene GDB:RBP2 !'##cross-references GDB:119548; OMIM:180280 !$#map_position 3q21-3qter !$#introns 25/1; 84/3; 118/3 CLASSIFICATION #superfamily myelin P2 protein KEYWORDS lipid binding; transport protein; vitamin A FEATURE !$2-135 #product retinol-binding protein, cellular #status !8predicted #label MAT SUMMARY #length 135 #molecular-weight 15850 #checksum 8766 SEQUENCE /// ENTRY RJRTO #type complete TITLE retinol-binding protein, cellular - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 05-Apr-1983 #sequence_revision 19-Oct-1995 #text_change 22-Jun-1999 ACCESSIONS A29570; A28016; A92527; A92455; A03149 REFERENCE A29570 !$#authors Levin, M.S.; Li, E.; Ong, D.E.; Gordon, J.I. !$#journal J. Biol. Chem. (1987) 262:7118-7124 !$#title Comparison of the tissue-specific expression and !1developmental regulation of two closely linked rodent genes !1encoding cytosolic retinol-binding proteins. !$#cross-references MUID:87222311; PMID:3584109 !$#accession A29570 !'##molecule_type mRNA !'##residues 1-135 ##label LEV !'##cross-references GB:M19257; GB:J02731; NID:g203583; PIDN:AAA40962.1; !1PID:g203584 REFERENCE A28016 !$#authors Sherman, D.R.; Lloyd, R.S.; Chytil, F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:3209-3213 !$#title Rat cellular retinol-binding protein: cDNA sequence and !1rapid retinol-dependent accumulation of mRNA. !$#cross-references MUID:87204107; PMID:3472205 !$#accession A28016 !'##molecule_type mRNA !'##residues 1-135 ##label SHE !'##cross-references GB:M16459; NID:g206590; PIDN:AAA42021.1; !1PID:g206591 REFERENCE A92527 !$#authors Sundelin, J.; Anundi, H.; Tragardh, L.; Eriksson, U.; Lind, !1P.; Ronne, H.; Peterson, P.A.; Rask, L. !$#journal J. Biol. Chem. (1985) 260:6488-6493 !$#title The primary structure of rat liver cellular retinol-binding !1protein. !$#cross-references MUID:85207645; PMID:4039728 !$#accession A92527 !'##molecule_type protein !'##residues 2-135 ##label SUN !'##experimental_source liver REFERENCE A92455 !$#authors Eriksson, U.; Das, K.; Busch, C.; Nordlinder, H.; Rask, L.; !1Sundelin, J.; Sallstrom, J.; Peterson, P.A. !$#journal J. Biol. Chem. (1984) 259:13464-13470 !$#title Cellular retinol-binding protein. Quantitation and !1distribution. !$#cross-references MUID:85030476; PMID:6541654 !$#accession A92455 !'##molecule_type protein !'##residues 2-51 ##label ERI !'##experimental_source testis CLASSIFICATION #superfamily myelin P2 protein KEYWORDS lipid binding; transport protein; vitamin A FEATURE !$2-135 #product retinol-binding protein, cellular #status !8experimental #label MAT SUMMARY #length 135 #molecular-weight 15834 #checksum 8310 SEQUENCE /// ENTRY FZHUI #type complete TITLE fatty acid-binding protein, intestinal - human ALTERNATE_NAMES fatty acid-binding protein 2 ORGANISM #formal_name Homo sapiens #common_name man DATE 20-Jun-1989 #sequence_revision 10-May-1996 #text_change 22-Jun-1999 ACCESSIONS A29781 REFERENCE A29781 !$#authors Sweetser, D.A.; Birkenmeier, E.H.; Klisak, I.J.; Zollman, !1S.; Sparkes, R.S.; Mohandas, T.; Lusis, A.J.; Gordon, J.I. !$#journal J. Biol. Chem. (1987) 262:16060-16071 !$#title The human and rodent intestinal fatty acid binding protein !1genes. A comparative analysis of their structure, !1expression, and linkage relationships. !$#cross-references MUID:88058967; PMID:2824476 !$#accession A29781 !'##molecule_type DNA !'##residues 1-132 ##label SWE !'##cross-references GB:M18079; GB:J03465; NID:g182351; PIDN:AAA52417.1; !1PID:g182352 GENETICS !$#gene GDB:FABP2 !'##cross-references GDB:119127; OMIM:134640 !$#map_position 4q28-4q31 !$#introns 23/1; 80/3; 116/3 CLASSIFICATION #superfamily myelin P2 protein KEYWORDS acetylated amino end; intestine; lipid binding FEATURE !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status predicted\ !$127 #binding_site fatty acid (Arg) #status predicted SUMMARY #length 132 #molecular-weight 15207 #checksum 3063 SEQUENCE /// ENTRY FZRTI #type complete TITLE fatty acid-binding protein, intestinal - rat ALTERNATE_NAMES FABP ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 17-Dec-1982 #sequence_revision 21-Feb-1997 #text_change 22-Jun-1999 ACCESSIONS I65761; A03147 REFERENCE I52850 !$#authors Gordon, J.I.; Lowe, J.B. !$#journal Chem. Phys. Lipids (1985) 38:137-158 !$#title Analyzing the structures, functions and evolution of two !1abundant gastrointestinal fatty acid binding proteins with !1recombinant DNA and computational techniques. !$#cross-references MUID:86053743; PMID:3840724 !$#accession I65761 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-132 ##label RES !'##cross-references GB:M35992; NID:g204087; PIDN:AAA41141.1; !1PID:g204088 REFERENCE A03147 !$#authors Alpers, D.H.; Strauss, A.W.; Ockner, R.K.; Bass, N.M.; !1Gordon, J.I. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:313-317 !$#title Cloning of a cDNA encoding rat intestinal fatty acid binding !1protein. !$#cross-references MUID:84119477; PMID:6582489 !$#accession A03147 !'##molecule_type mRNA !'##residues 1-9,'Y',11-82,'L',84-132 ##label ALP !'##cross-references GB:K01180; NID:g204081; PIDN:AAA41138.1; !1PID:g204082 CLASSIFICATION #superfamily myelin P2 protein KEYWORDS blocked amino end; intestine; lipid binding FEATURE !$2 #modified_site blocked amino end (Ala) (in mature !8form) (probably acetylated) #status experimental\ !$127 #binding_site fatty acid (Arg) #status predicted SUMMARY #length 132 #molecular-weight 15124 #checksum 4038 SEQUENCE /// ENTRY FZHUL #type complete TITLE fatty acid-binding protein, hepatic - human ALTERNATE_NAMES fatty acid binding protein 1; sterol carrier protein; Z protein ORGANISM #formal_name Homo sapiens #common_name man DATE 25-Oct-1987 #sequence_revision 10-May-1996 #text_change 22-Jun-1999 ACCESSIONS A22289; A22283 REFERENCE A22289 !$#authors Chan, L.; Wei, C.F.; Li, W.H.; Yang, C.Y.; Ratner, P.; !1Pownall, H.; Gotto Jr., A.M.; Smith, L.C. !$#journal J. Biol. Chem. (1985) 260:2629-2632 !$#title Human liver fatty acid binding protein cDNA and amino acid !1sequence. Functional and evolutionary implications. !$#cross-references MUID:85131017; PMID:3838309 !$#accession A22289 !'##molecule_type mRNA !'##residues 1-127 ##label CHA !'##cross-references GB:M10617; NID:g182357; PIDN:AAA52419.1; !1PID:g182358 REFERENCE A22283 !$#authors Lowe, J.B.; Boguski, M.S.; Sweetser, D.A.; Elshourbagy, !1N.A.; Taylor, J.M.; Gordon, J.I. !$#journal J. Biol. Chem. (1985) 260:3413-3417 !$#title Human liver fatty acid binding protein. !$#cross-references MUID:85131136; PMID:3838313 !$#accession A22283 !'##molecule_type mRNA !'##residues 1-93,'A',95-127 ##label LOW !'##cross-references GB:M10050; NID:g182355; PIDN:AAA52418.1; !1PID:g182356 !'##note parts of this sequence, including the amino end of the !1precursor protein, were determined by protein sequencing !'##note the isolation and sequencing of a cyanogen bromide fragment !1beginning with 2-Ser indicates it is not acetylated and that !1the mature protein probably begins with 1-Met GENETICS !$#gene GDB:FABP1 !'##cross-references GDB:119126; OMIM:134650 !$#map_position 2p11-2p11 CLASSIFICATION #superfamily myelin P2 protein KEYWORDS acetylated amino end; lipid binding FEATURE !$1 #modified_site acetylated amino end (Met) #status !8predicted\ !$69 #binding_site cysteine (Cys) (covalent) #status !8predicted\ !$69 #binding_site glutathione (Cys) (covalent) #status !8predicted\ !$122 #binding_site fatty acid (Arg) #status predicted SUMMARY #length 127 #molecular-weight 14208 #checksum 8654 SEQUENCE /// ENTRY FZRTL #type complete TITLE fatty acid-binding protein, hepatic - rat ALTERNATE_NAMES squalene- and sterol-carrier protein; Z-protein ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 22-Jun-1999 ACCESSIONS A92416; A91303; A25607; A39496; S41665; I59103; A03146 REFERENCE A92416 !$#authors Gordon, J.I.; Alpers, D.H.; Ockner, R.K.; Strauss, A.W. !$#journal J. Biol. Chem. (1983) 258:3356-3363 !$#title The nucleotide sequence of rat liver fatty acid binding !1protein mRNA. !$#cross-references MUID:83135795; PMID:6298233 !$#accession A92416 !'##molecule_type mRNA !'##residues 1-127 ##label GOR REFERENCE A91303 !$#authors Takahashi, K.; Odani, S.; Ono, T. !$#journal FEBS Lett. (1982) 140:63-66 !$#title Primary structure of rat liver Z-protein. A low-M-r cytosol !1protein that binds sterols, fatty acids and other small !1molecules. !$#cross-references MUID:82211146; PMID:7084456 !$#contents Z-protein !$#accession A91303 !'##molecule_type protein !'##residues 1-124,'K',126-127 ##label TAK REFERENCE A25607 !$#authors Sweetser, D.A.; Lowe, J.B.; Gordon, J.I. !$#journal J. Biol. Chem. (1986) 261:5553-5561 !$#title The nucleotide sequence of the rat liver fatty acid-binding !1protein gene. Evidence that exon 1 encodes an oligopeptide !1domain shared by a family of proteins which bind hydrophobic !1ligands. !$#cross-references MUID:86168302; PMID:3007511 !$#accession A25607 !'##molecule_type DNA !'##residues 1-124,'K',126-127 ##label SWE !'##cross-references GB:M13501; NID:g204085; PIDN:AAA41140.1; !1PID:g204086 REFERENCE A39496 !$#authors Myszka, D.G.; Swenson, R.P. !$#journal J. Biol. Chem. (1991) 266:20725-20731 !$#title Identification by photoaffinity labeling of fatty !1acid-binding protein as a potential warfarin receptor in rat !1liver. !$#cross-references MUID:92041926; PMID:1939124 !$#accession A39496 !'##molecule_type protein !'##residues 1-20 ##label MYS REFERENCE S41665 !$#authors Odani, S.; Okazaki, Y.; Kato, C.; Uchiumi, T.; Takahashi, Y. !$#journal Arch. Biochem. Biophys. (1994) 309:81-84 !$#title On the molecular origin of charge heterogeneity of rat liver !1fatty acid-binding protein (Z-protein). !$#cross-references MUID:94161561; PMID:8117116 !$#accession S41665 !'##molecule_type protein !'##residues 1-124,'K',126-127 ##label ODA REFERENCE I59103 !$#authors Bassuk, J.A.; Tsichlis, P.N.; Sorof, S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:7547-7551 !$#title Liver fatty acid binding protein is the mitosis-associated !1polypeptide target of a carcinogen in rat hepatocytes. !$#cross-references MUID:88041142; PMID:3478711 !$#accession I59103 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-102 ##label RES !'##cross-references GB:M17899; NID:g204073; PIDN:AAA41134.1; !1PID:g204074 COMMENT This protein binds free fatty acids and their coenzyme A !1derivatives, bilirubin, and some other small molecules in !1the cytoplasm; it may be involved in intracellular lipid !1transport. It is structurally related to myelin P2 protein !1and to the cellular retinol- and retinoic acid-binding !1proteins. GENETICS !$#introns 23/1; 80/3; 111/3 CLASSIFICATION #superfamily myelin P2 protein KEYWORDS acetylated amino end; lipid binding FEATURE !$1 #modified_site acetylated amino end (Met) #status !8experimental\ !$69 #binding_site cysteine (Cys) (covalent) #status !8predicted\ !$69 #binding_site glutathione (Cys) (covalent) #status !8predicted\ !$122 #binding_site fatty acid (Arg) #status predicted SUMMARY #length 127 #molecular-weight 14201 #checksum 295 SEQUENCE /// ENTRY RJBOP #type complete TITLE interphotoreceptor retinoid-binding protein precursor - bovine ALTERNATE_NAMES 7S receptor; interstitial retinoid-binding protein; IRBP ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 22-Jun-1999 ACCESSIONS A32205; A60819; JS0368; A23312; A22535; B25735 REFERENCE A32205 !$#authors Borst, D.E.; Redmond, T.M.; Elser, J.E.; Gonda, M.A.; !1Wiggert, B.; Chader, G.J.; Nickerson, J.M. !$#journal J. Biol. Chem. (1989) 264:1115-1123 !$#title Interphotoreceptor retinoid-binding protein: gene !1characterization, protein repeat structure, and its !1evolution. !$#cross-references MUID:89093097; PMID:2910846 !$#accession A32205 !'##molecule_type DNA !'##residues 1-1286 ##label BOR !'##cross-references GB:M20748; GB:J04441; NID:g163229; PIDN:AAA30591.1; !1PID:g163230 !'##note nearly half of the sequence of the mature protein was confirmed !1by protein sequencing !'##note the sequences of the signal sequence and propeptide are not !1shown in this publication; the 22 residues shown here were !1obtained by translation of the DNA sequence REFERENCE A60819 !$#authors Borst, D.E.; Nickerson, J.M. !$#journal Exp. Eye Res. (1988) 47:825-838 !$#title The isolation of a gene encoding interphotoreceptor !1retinoid-binding protein. !$#cross-references MUID:89107463; PMID:3215295 !$#accession A60819 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-75 ##label BO2 REFERENCE JS0368 !$#authors Redmond, T.M.; Si, J.S.; Barrett, D.J.; Borst, D.E.; !1Rainier, S.; Kotake, S.; Gery, I.; Nickerson, J.M. !$#journal Gene (1989) 80:109-118 !$#title Synthesis of an immunopathogenic fusion protein derived from !1a bovine interphotoreceptor retinoid-binding protein cDNA !1clone. !$#cross-references MUID:90006770; PMID:2676730 !$#accession JS0368 !'##molecule_type mRNA !'##residues 736-1114,'D',1116-1286 ##label RED REFERENCE A23312 !$#authors Barrett, D.J.; Redmond, T.M.; Wiggert, B.; Oprian, D.D.; !1Chader, G.J.; Nickerson, J.M. !$#journal Biochem. Biophys. Res. Commun. (1985) 131:1086-1093 !$#title cDNA clones encoding bovine interphotoreceptor retiniod !1binding protein. !$#cross-references MUID:86025569; PMID:2413855 !$#accession A23312 !'##molecule_type mRNA; protein !'##residues 1194-1221 ##label BAR !'##cross-references GB:M26119; NID:g163236; PIDN:AAA30593.1; !1PID:g163237 REFERENCE A22535 !$#authors Saari, J.C.; Teller, D.C.; Crabb, J.W.; Bredberg, L. !$#journal J. Biol. Chem. (1985) 260:195-201 !$#title Properties of an interphotoreceptor retinoid-binding protein !1from bovine retina. !$#cross-references MUID:85080077; PMID:2981203 !$#accession A22535 !'##molecule_type protein !'##residues 23-39,'T',41-43,'V',45-46 ##label SAA REFERENCE A90335 !$#authors Redmond, T.M.; Wiggert, B.; Robey, F.A.; Chader, G.J. !$#journal Biochem. J. (1986) 240:19-26 !$#title Interspecies conservation of structure of interphotoreceptor !1retinoid-binding protein. Similarities and differences as !1adjudged by peptide mapping and N-terminal sequencing. !$#cross-references MUID:87156570; PMID:3827838 !$#accession B25735 !'##molecule_type protein !'##residues 23-39,'E',41-56 ##label RE2 COMMENT This protein is a large glycolipoprotein found in the !1interphotoreceptor matrix between the neural retina and !1retinal pigment epithelium. GENETICS !$#introns 1016/3; 1080/2; 1128/1 CLASSIFICATION #superfamily interphotoreceptor retinoid-binding protein KEYWORDS duplication; extracellular matrix; glycoprotein; !1lipoprotein; monomer; phosphoprotein; retina; retinol !1binding FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-22 #domain propeptide #status predicted #label PRO\ !$23-1286 #product interphotoreceptor retinoid-binding protein !8#status experimental #label MAT\ !$23-323 #region duplication\ !$324-631 #region duplication\ !$632-932 #region duplication\ !$933-1231 #region duplication\ !$90,274,444,506,520, !$834,975,1116,1133, !$1238,1258 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$107,161,205,513, !$1114 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$173,206,342,515, !$531,545,930 #binding_site phosphate (Thr) (covalent) #status !8predicted SUMMARY #length 1286 #molecular-weight 139697 #checksum 391 SEQUENCE /// ENTRY RBHU #type complete TITLE retinoblastoma-associated protein - human ALTERNATE_NAMES retinoblastoma suspectibility protein ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1987 #sequence_revision 30-Jun-1990 #text_change 17-Mar-2000 ACCESSIONS JS0276; A03152; A91613; A39947; A44987; I68660; I54364; !1I68638; I68639; I68641; I68640; I68642; I68643; I68644; !1I68645; I68646; I68647; I68659; I68649; I68662; I68651; !1I68650; I68652; I68653; I68654; I68658; I68657; I68656; !1I68661; I68648; I68655; I58362; I78863; I78866; I78872; !1I78873; A35590 REFERENCE JS0276 !$#authors Lee, W.H.; Shew, J.Y.; Hong, F.D.; Sery, T.W.; Donoso, L.A.; !1Young, L.J.; Bookstein, R.; Lee, E.Y.H.P. !$#journal Nature (1987) 329:642-645 !$#title The retinoblastoma susceptibility gene encodes a nuclear !1phosphoprotein associated with DNA binding activity. !$#cross-references MUID:88014238; PMID:3657987 !$#accession JS0276 !'##molecule_type mRNA !'##residues 1-928 ##label LE1 !'##cross-references GB:M28419; NID:g190962; PIDN:AAA69808.1; !1PID:g190963 !'##note this sequence has two possible initiation sites, 1-Met and !1113-Met REFERENCE A03152 !$#authors Lee, W.H.; Bookstein, R.; Hong, F.; Young, L.J.; Shew, J.Y.; !1Lee, E.Y.H.P. !$#journal Science (1987) 235:1394-1399 !$#title Human retinoblastoma susceptibility gene: cloning, !1identification, and sequence. !$#cross-references MUID:87149066; PMID:3823889 !$#accession A03152 !'##molecule_type mRNA !'##residues 113-116,'LLSYRKTY',125-332,'R',334-367,'I',369-928 ##label !1LE2 !'##cross-references GB:M15400; NID:g190958; PIDN:AAA69807.1; !1PID:g190959 REFERENCE A91613 !$#authors McGee, T.L.; Yandell, D.W.; Dryja, T.P. !$#journal Gene (1989) 80:119-128 !$#title Structure and partial genomic sequence of the human !1retinoblastoma susceptibility gene. !$#cross-references MUID:90006771; PMID:2701949 !$#accession A91613 !'##molecule_type DNA !'##residues 1-928 ##label MCG !'##cross-references GB:M27845; GB:L11910; NID:g292420; PIDN:AAA53483.1; !1PID:g292421 !'##note the authors translated the codon GAA for residue 559 as Gly REFERENCE A39947 !$#authors Friend, S.H.; Horowitz, J.M.; Gerber, M.R.; Wang, X.F.; !1Bogenmann, E.; Li, F.P.; Weinberg, R.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:9059-9063 !$#title Deletions of a DNA sequence in retinoblastomas and !1mesenchymal tumors: organization of the sequence and its !1encoded protein. !$#cross-references MUID:88097427; PMID:3480530 !$#accession A39947 !'##molecule_type mRNA !'##residues 1-928 ##label FRI !'##cross-references GB:M33647; GB:J02994; NID:g190945; PIDN:AAA69806.1; !1PID:g190946 REFERENCE A44987 !$#authors T'Ang, A.; Wu, K.J.; Hashimoto, T.; Liu, W.Y.; Takahashi, !1R.; Shi, X.H.; Mihara, K.; Zhang, F.H.; Chen, Y.Y.; Du, C.; !1Qian, J.; Lin, Y.G.; Murphree, A.L.; Qiu, W.R.; Thompson, !1T.; Benedict, W.F.; Fung, Y.K.T. !$#journal Oncogene (1989) 4:401-407 !$#title Genomic organization of the human retinoblastoma gene. !$#cross-references MUID:89239464; PMID:2717184 !$#accession A44987 !'##molecule_type DNA !'##residues 1-46 ##label TAA !'##cross-references EMBL:X16439; NID:g35894; PIDN:CAA34462.1; !1PID:g35895 REFERENCE I54364 !$#authors Lohmann, D.R.; Brandt, B.; Hopping, W.; Passarge, E.; !1Horsthemke, B. !$#journal Hum. Mol. Genet. (1994) 3:2187-2193 !$#title Spectrum of small length germline mutations in the RB1 gene. !$#cross-references MUID:95187159; PMID:7881418 !$#accession I68660 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 47-65,'DTRSCQRESLVNLGESFICGWSI' ##label LO01 !'##cross-references GB:L49208; NID:g1088332; PIDN:AAA82561.1; !1PID:g1088333 !'##note one base insertion mutant with premature termination after !1residue 96; GenBank entry HUMRB1I66D, release 114.0, !1PIDN:AAA82561.1, incorrectly stops after residue 88, !1omitting 'GKDFLKTF' !$#accession I54364 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 128-133 ##label LO02 !'##cross-references GB:L49209; NID:g1088286; PIDN:AAA82538.1; !1PID:g1088287 !'##note four base deletion mutant with premature termination after !1residue 133 !$#accession I68638 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 128-159,'VCTLQQIGK' ##label LO03 !'##cross-references GB:L49210; NID:g1088288; PIDN:AAA82539.1; !1PID:g1088289 !'##note four base insertion mutant with premature termination after !1residue 171; GenBank entry HUMRB1160V, release 114.0, !1PIDN:AAA82539.1, incorrectly stops after residue 168, !1omitting 'VK' !$#accession I68639 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 168-177,'NPAV' ##label LO04 !'##cross-references GB:L49211; NID:g1088290; PIDN:AAA82540.1; !1PID:g1088291 !'##note five base insertion mutant with premature termination after !1residue 183; GenBank entry HUMRB1178N, release 114.0, !1PIDN:AAA82540.1, incorrectly stops after residue 181, !1omitting 'RK' !$#accession I68641 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 241-259,'VHG' ##label LO05 !'##cross-references GB:L49213; NID:g1088294; PIDN:AAA82542.1; !1PID:g1088295 !'##note one base deletion mutant with premature termination after !1residue 262 !$#accession I68640 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 241-255,'VRTGVHG' ##label LO06 !'##cross-references GB:L49212; NID:g1088292; PIDN:AAA82541.1; !1PID:g1088293 !'##note one base deletion mutant with premature termination after !1residue 162 !$#accession I68642 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 288-303,'D',305 ##label LO07 !'##cross-references GB:L49214; NID:g1088296; PIDN:AAA82543.1; !1PID:g1088297 !'##note one base deletion mutant with premature termination after !1residue 305 !$#accession I68643 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 351-362,'G' ##label LO08 !'##cross-references GB:L49215; NID:g1088298; PIDN:AAA82544.1; !1PID:g1088299 !'##note one base insertion mutant with premature termination after !1residue 363 !$#accession I68644 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 351-364,'R' ##label LO09 !'##cross-references GB:L49216; NID:g1088300; PIDN:AAA82545.1; !1PID:g1088301 !'##note one base deletion mutant with premature termination after !1residue 365 !$#accession I68645 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 377-386,'IDFKFSK' ##label LO10 !'##cross-references GB:L49217; NID:g1088302; PIDN:AAA82546.1; !1PID:g1088303 !'##note one base insertion mutant with premature termination after !1residue 393 !$#accession I68646 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 406-412,'KVY' ##label LO11 !'##cross-references GB:L49218; NID:g1088304; PIDN:AAA82547.1; !1PID:g1088305 !'##note one base deletion mutant with premature termination after !1residue 415 !$#accession I68647 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 475-485,'WRALLRL' ##label LO12 !'##cross-references GB:L49219; NID:g1088306; PIDN:AAA82548.1; !1PID:g1088307 !'##note four base deletion mutant with premature termination after !1residue 492 !$#accession I68659 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 501-539,546-565 ##label LO13 !'##cross-references GB:L49221; NID:g1088330; PIDN:AAA82560.1; !1PID:g1088331 !'##note eighteen base deletion mutant !$#accession I68649 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 566-603,'EI' ##label LO14 !'##cross-references GB:L49222; NID:g1088310; PIDN:AAA82550.1; !1PID:g1088311 !'##note two base insertion mutant with premature termination after !1residue 610; Genbank entry HUMRB1604E, release 114.0, !1PIDN:AAA82550.1, incorrectly stops after residue 605 !$#accession I68662 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 606-653 ##label LO15 !'##cross-references GB:L49225; NID:g1088336; PIDN:AAA82563.1; !1PID:g1088337 !'##note one base deletion mutant at exon 19 boundary !$#accession I68651 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 606-645,'FFHCFIKK' ##label LO16 !'##cross-references GB:L49224; NID:g1088314; PIDN:AAA82552.1; !1PID:g1088315 !'##note one base deletion mutant with premature termination after !1residue 656; Genbank entry HUMRB1646F, release 114.0, !1PIDN:AAA82552.1, incorrectly stops after residue 653 !1omitting 'VSR' !$#accession I68650 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 606-609,'KISKEKRFNYACKFYCKCRDTSNLSLPDPEAIEIYLSFTVL' ##label !1LO17 !'##cross-references GB:L49223; NID:g1088312; PIDN:AAA82551.1; !1PID:g1088313 !'##note two base deletion mutant with premature termination after !1residue 650 !$#accession I68652 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 703-725,'QHTRIFLMLFR' ##label LO18 !'##cross-references GB:L49226; NID:g1088316; PIDN:AAA82553.1; !1PID:g1088317 !'##note one base deletion mutant with premature termination after !1residue 737; Genbank entry HUMRB1726Q, release 114.0, !1PIDN:AAA82553.1, incorrectly stops after residue 736 !1omitting 'R' !$#accession I68653 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 703-732,'MLFR' ##label LO19 !'##cross-references GB:L49227; NID:g1088318; PIDN:AAA82554.1; !1PID:g1088319 !'##note one base deletion mutant with premature termination after !1residue 737; Genbank entry HUMRB1733M, release 114.0, !1PIDN:AAA82554.1, incorrectly stops after residue 736 !1omitting 'R' !$#accession I68654 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 703-733,'GCSG' ##label LO20 !'##cross-references GB:L49228; NID:g1088320; PIDN:AAA82555.1; !1PID:g1088321 !'##note one base insertion mutant with premature termination after !1residue 739; Genbank entry HUMRB1734G, release 114.0, !1PIDN:AAA82555.1, incorrectly stops after residue 737 !1omitting 'GR' !$#accession I68658 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 738-754,756-775 ##label LO21 !'##cross-references GB:L49229; NID:g1088328; PIDN:AAA82559.1; !1PID:g1088329 !'##note three base deletion mutant !$#accession I68657 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 776-808 ##label LO22 !'##cross-references GB:L49232; NID:g1088326; PIDN:AAA82558.1; !1PID:g1088327 !'##note one base deletion mutant with premature termination after !1residue 808 !$#accession I68656 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 777-804 ##label LO23 !'##cross-references GB:L49231; NID:g1088324; PIDN:AAA82557.1; !1PID:g1088325 !'##note one base deletion mutant with premature termination after !1residue 804 !$#accession I68661 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 831-840 ##label LO24 !'##cross-references GB:L49233; NID:g1088334; PIDN:AAA82562.1; !1PID:g1088335 !'##note four base deletion mutant exon 24 donor site !$#accession I68648 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 'VHLRILILEQICLSHGF' ##label LO25 !'##cross-references GB:L49220; NID:g1088308; PIDN:AAA82549.1; !1PID:g1088309 !'##note one base deletion mutant with premature termination after !1residue 518 !$#accession I68655 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 'PLPCHQYLTFLEALTSFLVHPYGFLEGTSIFHP' ##label LO26 !'##cross-references GB:L49230; NID:g1088322; PIDN:AAA82556.1; !1PID:g1088323 !'##note one base deletion mutant with premature termination after !1residue 808 REFERENCE I58362 !$#authors Hogg, A.; Onadim, Z.; Baird, P.N.; Cowell, J.K. !$#journal Oncogene (1992) 7:1445-1451 !$#title Detection of heterozygous mutations in the RB1 gene in !1retinoblastoma patients using single-strand conformation !1polymorphism analysis and polymerase chain reaction !1sequencing. !$#cross-references MUID:92319557; PMID:1352398 !$#accession I58362 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-45 ##label HOG1 !'##cross-references GB:L41889; NID:g793948; PIDN:AAB59467.1; !1PID:g793949 !$#accession I78863 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 377-394 ##label HOG2 !'##cross-references GB:L41900; NID:g793969; PIDN:AAB59472.1; !1PID:g793972 !$#accession I78866 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 655-671 ##label HOG3 !'##cross-references GB:L41907; NID:g801729; PIDN:AAB59489.1; !1PID:g801730 !$#accession I78872 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 889-904 ##label HOG4 !'##cross-references GB:L41913; NID:g794008; PIDN:AAA65748.1; !1PID:g794009 !$#accession I78873 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 906-928 ##label HOG5 !'##cross-references GB:L41914; NID:g794010; PIDN:AAA65749.1; !1PID:g794011 REFERENCE A35590 !$#authors Lee, E.Y.H.P.; Bookstein, R.; Young, L.J.; Lin, C.J.; !1Rosenfeld, M.G.; Lee, W.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:6017-6021 !$#title Molecular mechanism of retinoblastoma gene inactivation in !1retinoblastoma cell line Y79. !$#cross-references MUID:88320373; PMID:3413073 !$#contents annotation REFERENCE A38988 !$#authors Lees, J.A.; Buchkovich, K.J.; Marshak, D.R.; Anderson, C.W.; !1Harlow, E. !$#journal EMBO J. (1991) 10:4279-4290 !$#title The retinoblastoma protein is phosphorylated on multiple !1sites by human cdc2. !$#cross-references MUID:92097548; PMID:1756735 !$#contents annotation; phosphorylation sites GENETICS !$#gene GDB:RB1 !'##cross-references GDB:118734; OMIM:180200 !$#map_position 13q14.3-13q14.3 !$#introns 46/2; 88/3; 127/2; 167/2; 180/2; 203/1; 240/1; 287/3; 313/3; !1350/2; 376/2; 405/3; 444/3; 463/3; 474/2; 500/1; 565/3; 605/ !12; 654/1; 702/3; 737/3; 775/3; 830/2; 840/3; 888/2; 905/1 !$#note mutations in the germline gene predispose to hereditary !1retinoblastoma; somatic mutations have been found in a !1variety of human cancers including retinoblastoma and !1osteosarcoma CLASSIFICATION #superfamily retinoblastoma-associated protein KEYWORDS cell cycle control; DNA binding; leucine zipper; !1osteosarcoma; phosphoprotein; retinoblastoma; transcription !1regulation; tumor suppressor FEATURE !$10-18 #region alanine-rich\ !$20-29 #region proline-rich\ !$662-683 #region leucine zipper motif\ !$249,807,811 #binding_site phosphate (Ser) (covalent) (by cdc2 !8kinase) #status predicted\ !$252,373 #binding_site phosphate (Thr) (covalent) (by cdc2 !8kinase) #status predicted SUMMARY #length 928 #molecular-weight 106158 #checksum 3504 SEQUENCE /// ENTRY I58383 #type complete TITLE retinoblastoma binding protein 1, splice form I - human ALTERNATE_NAMES retinoblastoma-associated protein 2 (misnomer) CONTAINS retinoblastoma binding protein 1, splice form II ORGANISM #formal_name Homo sapiens #common_name man DATE 17-Mar-2000 #sequence_revision 17-Mar-2000 #text_change 17-Mar-2000 ACCESSIONS I58383; I58390; I78883; S16953; B42997 REFERENCE I58383 !$#authors Fattaey, A.R.; Helin, K.; Dembski, M.S.; Dyson, N.; Harlow, !1E.; Vuocolo, G.A.; Hanobik, M.G.; Haskell, K.M.; Oliff, A.; !1Defeo-Jones, D. !$#journal Oncogene (1993) 8:3149-3156 !$#title Characterization of the retinoblastoma binding proteins RBP1 !1and RBP2. !$#cross-references MUID:94020841; PMID:8414517 !$#accession I58383 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-1257 ##label FAT !'##cross-references GB:S66427; NID:g435775; PIDN:AAB28543.1; !1PID:g435776 REFERENCE I58390 !$#authors Otterson, G.A.; Kratzke, R.A.; Lin, A.Y.; Johnston, P.G.; !1Kaye, F.J. !$#journal Oncogene (1993) 8:949-957 !$#title Alternative splicing of the RBP1 gene clusters in an !1internal exon that encodes potential phosphorylation sites. !$#cross-references MUID:93205410; PMID:8455946 !$#accession I58390 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 338-384,'V',386-617,'R',619-652,'V',654-778,'T',780-1257 !1##label OTT1 !'##cross-references GB:S57153; NID:g298681; PIDN:AAB25833.1; !1PID:g298682 !$#accession I78883 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 338-384,'V',386-617,'R',619-652,'V',654-778,'T',780-1120, !11175-1257 ##label OTT2 !'##cross-references GB:S57160; NID:g298683; PIDN:AAB25834.1; !1PID:g298684 REFERENCE S16953 !$#authors Defeo-Jones, D.; Huang, P.S.; Jones, R.E.; Haskell, K.M.; !1Vuocolo, G.A.; Hanobik, M.G.; Huber, H.E.; Oliff, A. !$#journal Nature (1991) 352:251-254 !$#title Cloning of cDNAs for cellular proteins that bind to the !1retinoblastoma gene product. !$#cross-references MUID:91312450; PMID:1857421 !$#accession S16953 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 855-1177,'S',1179-1195,'SENIICL' ##label DEF REFERENCE A42997 !$#authors Kaelin Jr., W.G.; Krek, W.; Sellers, W.R.; DeCaprio, J.A.; !1Ajchenbaum, F.; Fuchs, C.S.; Chittenden, T.; Li, Y.; !1Farnham, P.J.; Blanar, M.A.; Livingston, D.M.; Flemington, !1E.K. !$#journal Cell (1992) 70:351-364 !$#title Expression cloning of a cDNA encoding a !1retinoblastoma-binding protein with E2F-like properties. !$#cross-references MUID:92346721; PMID:1638635 !$#accession B42997 !'##molecule_type mRNA !'##residues 'MMTMKL',510-617,'R',619-1257 ##label KAE !'##experimental_source Akata cells !'##note the cited GenBank accession number, M96577, is apparently a !1misprint and does not apply to this sequence report !'##note sequence extracted from NCBI backbone (NCBIN:110020, !1NCBIP:110022) GENETICS !$#gene GDB:RBP1 !'##cross-references GDB:120340; OMIM:180260 !$#map_position 3q21-3q22 CLASSIFICATION #superfamily human retinoblastoma binding protein 1 KEYWORDS alternative splicing FEATURE !$1-1257 #product retinoblastoma binding protein 1, splice !8form I #status predicted #label SF1\ !$1-1120,1175-1257 #product retinoblastoma binding protein 1, splice !8form II #status predicted #label SF2 SUMMARY #length 1257 #molecular-weight 142665 #checksum 2872 SEQUENCE /// ENTRY I78879 #type complete TITLE retinoblastoma binding protein 2 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 17-Mar-2000 #sequence_revision 17-Mar-2000 #text_change 17-Mar-2000 ACCESSIONS I78879; S16954 REFERENCE I58383 !$#authors Fattaey, A.R.; Helin, K.; Dembski, M.S.; Dyson, N.; Harlow, !1E.; Vuocolo, G.A.; Hanobik, M.G.; Haskell, K.M.; Oliff, A.; !1Defeo-Jones, D. !$#journal Oncogene (1993) 8:3149-3156 !$#title Characterization of the retinoblastoma binding proteins RBP1 !1and RBP2. !$#cross-references MUID:94020841; PMID:8414517 !$#accession I78879 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-1722 ##label FAT !'##cross-references GB:S66431; NID:g435777; PIDN:AAB28544.1; !1PID:g435778 REFERENCE S16953 !$#authors Defeo-Jones, D.; Huang, P.S.; Jones, R.E.; Haskell, K.M.; !1Vuocolo, G.A.; Hanobik, M.G.; Huber, H.E.; Oliff, A. !$#journal Nature (1991) 352:251-254 !$#title Cloning of cDNAs for cellular proteins that bind to the !1retinoblastoma gene product. !$#cross-references MUID:91312450; PMID:1857421 !$#accession S16954 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1102-1562,'KKK' ##label DEF GENETICS !$#gene GDB:RBP2 !'##cross-references GDB:119548; OMIM:180280 !$#map_position 3q21-3qter CLASSIFICATION #superfamily human retinoblastoma binding protein 2 SUMMARY #length 1722 #molecular-weight 195814 #checksum 942 SEQUENCE /// ENTRY I38902 #type complete TITLE retinoblastoma binding protein RIZ - human ALTERNATE_NAMES retinoblastoma interacting zinc-finger (RIZ) protein; transcription factor GATA3-binding (G3B) protein ORGANISM #formal_name Homo sapiens #common_name man DATE 17-Mar-2000 #sequence_revision 17-Mar-2000 #text_change 21-Jul-2000 ACCESSIONS I38902; A59221; PC4095 REFERENCE I38902 !$#authors Buyse, I.M.; Shao, G.; Huang, S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1995) 92:4467-4471 !$#title The retinoblastoma protein binds to RIZ, a zinc-finger !1protein that shares an epitope with the adenovirus E1A !1protein. !$#cross-references MUID:95273384; PMID:7538672 !$#accession I38902 !'##status nucleic acid sequence not shown; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 3-1721 ##label BUY1 !'##cross-references EMBL:U17838; NID:g949997 !$#accession A59221 !'##status nucleic acid sequence not shown; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-1721 ##label BUY2 !'##cross-references EMBL:U17838; NID:g1669774; PIDN:AAC50820.1; !1PID:g3645905 !'##note the sequence is revised in GenBank entry HSU17838, release !1114.0, PIDN:AAC50820.1 REFERENCE PC4095 !$#authors Shapiro, V.S.; Lee, P.; Winoto, A. !$#journal Gene (1995) 163:329-330 !$#title Identification and cloning of the G3B cDNA encoding a 3' !1segment of a protein binding to GATA-3. !$#cross-references MUID:96011660; PMID:7590293 !$#accession PC4095 !'##molecule_type mRNA !'##residues 161-165,'T',167-197,'S',199-201,'G',203-277, !1'VGGGGGVVVVVSWKARGE',296-308,'SQKYGVMRSQKI',321-337,'DL', !1340-372,'I',374-467,'VS',470-535,'PRTCMYQAQSRRGRGSR' ##label !1SHA !'##cross-references GB:U23736; NID:g915214; PIDN:AAA87023.1; !1PID:g915215 GENETICS !$#gene GDB:RIZ; G3B !'##cross-references GDB:636678; OMIM:601196 !$#map_position 1p36.23-1p36.13 CLASSIFICATION #superfamily human retinoblastoma binding protein RIZ; SH3 !1homology KEYWORDS zinc finger FEATURE !$364-384 #region zinc finger CCHH motif\ !$394-414 #region zinc finger CCHH motif\ !$487-508 #region zinc finger CCHH motif\ !$752-805 #domain SH3 homology #label SH3\ !$1139-1159 #region zinc finger CCHH motif\ !$1167-1188 #region zinc finger CCHH motif\ !$1196-1217 #region zinc finger CCHH motif\ !$1338-1358 #region zinc finger CCHH motif\ !$1460-1481 #region zinc finger CCHH motif SUMMARY #length 1721 #molecular-weight 189270 #checksum 6277 SEQUENCE /// ENTRY RBHUAP #type complete TITLE adenomatous polyposis coli protein - human ALTERNATE_NAMES polyposis coli locus protein DP2.5; tumor suppressor APC ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 21-Jul-2000 ACCESSIONS A37261; B39658; A44928; A49319; I54271 REFERENCE A37261 !$#authors Kinzler, K.W.; Nilbert, M.C.; Su, L.K.; Vogelstein, B.; !1Bryan, T.M.; Levy, D.B.; Smith, K.J.; Preisinger, A.C.; !1Hedge, P.; McKechnie, D.; Finniear, R.; Markham, A.; !1Groffen, J.; Boguski, M.S.; Altschul, S.F.; Horii, A.; Ando, !1H.; Miyoshi, Y.; Miki, Y.; Nishisho, I.; Nakamura, Y. !$#journal Science (1991) 253:661-665 !$#title Identification of FAP locus genes from chromosome 5q21. !$#cross-references MUID:91335210; PMID:1651562 !$#accession A37261 !'##molecule_type mRNA !'##residues 1-2843 ##label KIN !'##cross-references GB:M74088; NID:g182396; PIDN:AAA03586.1; !1PID:g182397 REFERENCE A39658 !$#authors Joslyn, G.; Carlson, M.; Thliveris, A.; Albertsen, H.; !1Gelbert, L.; Samowitz, W.; Groden, J.; Stevens, J.; Spirio, !1L.; Robertson, M.; Sargeant, L.; Krapcho, K.; Wolff, E.; !1Burt, R.; Hughes, J.P.; Warrington, J.; McPherson, J.; !1Wasmuth, J.; Le Paslier, D.; Abderrahim, H.; Cohen, D.; !1Leppert, M.; White, R. !$#journal Cell (1991) 66:601-613 !$#title Identification of deletion mutations and three new genes at !1the familial polyposis locus. !$#cross-references MUID:91330307; PMID:1678319 !$#accession B39658 !'##molecule_type DNA !'##residues 1-183,'L',185-969,'N',971-1308,'G',1310-1324,'SS',1326, !1'HSTLE',1332-1354,'P',1356-1590,'G',1592-2722,'T',2724-2754, !1'P',2756-2843 ##label JOS !'##cross-references GB:M73548; NID:g190163; PIDN:AAA60354.1; !1PID:g190164 REFERENCE A44928 !$#authors Miki, Y.; Nishisho, I.; Horii, A.; Miyoshi, Y.; Utsunomiya, !1J.; Kinzler, K.W.; Vogelstein, B.; Nakamura, Y. !$#journal Cancer Res. (1992) 52:643-645 !$#title Disruption of the APC gene by a retrotransposal insertion of !1L1 sequence in a colon cancer. !$#cross-references MUID:92119623; PMID:1310068 !$#accession A44928 !'##molecule_type DNA !'##residues 1506-1525 ##label MIK !'##cross-references GB:S78214; NID:g243541; PIDN:AAB21145.1; !1PID:g243542 !'##note sequence extracted from NCBI backbone (NCBIN:78214, !1NCBIP:78218) REFERENCE A49319 !$#authors Spirio, L.; Olschwang, S.; Groden, J.; Robertson, M.; !1Samowitz, W.; Joslyn, G.; Gelbert, L.; Thliveris, A.; !1Carlson, M.; Otterud, B. !$#journal Cell (1993) 75:951-957 !$#title Alleles of the APC gene: an attenuated form of familial !1polyposis. !$#cross-references MUID:94073973; PMID:8252630 !$#accession A49319 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 'G',143-171,'P',173-179 ##label SPI !'##cross-references GB:S67787; NID:g461061; PIDN:AAD13997.1; !1PID:g4261697 REFERENCE I54271 !$#authors Lambertz, S.; Ballhausen, W.G. !$#journal Hum. Genet. (1993) 90:650-652 !$#title Identification of an alternative 5' untranslated region of !1the adenomatous polyposis coli gene. !$#cross-references MUID:93186137; PMID:8383094 !$#accession I54271 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-4 ##label LAM !'##cross-references GB:S56365; NID:g266243; PIDN:AAD14918.1; !1PID:g4262770 GENETICS !$#gene GDB:APC !'##cross-references GDB:119682; OMIM:175100 !$#map_position 5q21-5q22 !$#note mutations of this gene can result in familial adenomatous !1polyposis or sporadic colorectal cancers CLASSIFICATION #superfamily adenomatous polyposis coli protein KEYWORDS cancer; familial adenomatous polyposis; tumor suppressor FEATURE !$1-730 #domain leucine-rich #label NTD\ !$7-72 #region coil #status predicted\ !$185-227 #region coil #status predicted\ !$731-2832 #domain serine-rich #label CTD\ !$1131-1156 #region acidic\ !$1558-1577 #region acidic\ !$1866-1893 #region highly charged SUMMARY #length 2843 #molecular-weight 311659 #checksum 7110 SEQUENCE /// ENTRY G02334 #type complete TITLE breast cancer tumor suppressor BRCA2 - human ALTERNATE_NAMES breast cancer susceptibility protein BRCA2 ORGANISM #formal_name Homo sapiens #common_name man DATE 21-Dec-1996 #sequence_revision 06-Jun-1997 #text_change 22-Jun-1999 ACCESSIONS G02334; S68501 REFERENCE H01078 !$#authors Tavtigian, S.V.; Rommens, J.M.; Couch, F.J.; Neuhausen, S.; !1Bell, R.; Berry, S.; Bogden, R.; Chen, Q.; Davis, T.; Frye, !1C.; Hattier, T.; Jammulapati, S.; Janecki, T.; Jiang, P.; !1Kehrer, R.; Schroeder, M.; Snyder, S.; Stringfellow, M.; !1Stroup, C.; Swedlund, B.; Teng, D.; Thomas, A.; Tran, T.; !1Weaver-Feldhaus, J.; Wong, A.; Leblanc, J. !$#submission submitted to the EMBL Data Library, December 1995 !$#accession G02334 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-3418 ##label TAV !'##cross-references EMBL:U43746; NID:g1161383; PIDN:AAB07223.1; !1PID:g1161384 REFERENCE S68501 !$#authors Wooster, R.; Bignell, G.; Lancaster, J.; Swift, S.; Seal, !1S.; Mangion, J.; Collins, N.; Gregory, S.; Gumbs, C.; !1Micklem, G.; Barfoot, R.; Hamoudi, R.; Patel, S.; Rice, C.; !1Biggs, P.; Hashim, Y.; Smith, A.; Connor, F.; Arason, A.; !1Gudmundsson, J.; Ficenec, D.; Kelsell, D.; Ford, D.; Tonin, !1P.; Bishop, D.T.; Spurr, N.K.; Ponder, B.A.J.; Eeles, R.; !1Peto, J.; Devilee, P.; Cornelisse, C.; Lynch, H.; Narod, S.; !1Lenoir, G.; Egilsson, V.; Barkadottir, R.B.; Easton, D.F.; !1Bentley, D.R.; Futreal, P.A.; Ashworth, A.; Stratton, M.R. !$#journal Nature (1995) 378:789-792 !$#title Identification of the breast cancer susceptibility gene !1BRCA2. !$#cross-references MUID:96112016; PMID:8524414 !$#accession S68501 !'##molecule_type mRNA !'##residues 282-371,'N',373-598,'S',600-1108,'EQ',1111-1119,'D', !11121-2321,'V',2323-2386,'GNK',2390,'G',2392-2394,'K', !12396-2429,'G',2431-2606,'VKAT' ##label WOO GENETICS !$#gene GDB:BRCA2 !'##cross-references GDB:387848; OMIM:600185 !$#map_position 13q12.3-13q12.3 CLASSIFICATION #superfamily breast cancer tumor suppressor BRCA2 KEYWORDS polymorphism; tumor suppressor SUMMARY #length 3418 #molecular-weight 384282 #checksum 709 SEQUENCE /// ENTRY RGBOGT #type complete TITLE GTP-binding regulatory protein gamma-6 chain precursor - bovine ALTERNATE_NAMES guanine nucleotide binding protein gamma-6 chain; heterotrimeric G-protein gamma-6 chain; transducin gamma-6 chain ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 28-Aug-1985 #sequence_revision 31-Dec-1992 #text_change 22-Jun-1999 ACCESSIONS I46939; A03153; A22944; A91329; I45984 REFERENCE I46939 !$#authors Tao, L.; Pandey, S.; Simon, M.I.; Fong, H.K. !$#journal Exp. Eye Res. (1993) 56:497-507 !$#title Structure of the bovine transducin gamma subunit gene and !1analysis of promoter function in transgenic mice. !$#cross-references MUID:93272877; PMID:8500562 !$#accession I46939 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-74 ##label TAO !'##cross-references GB:S62031; NID:g385281; PIDN:AAB26895.1; !1PID:g385282 REFERENCE A94016 !$#authors Hurley, J.B.; Fong, H.K.W.; Teplow, D.B.; Dreyer, W.J.; !1Simon, M.I. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:6948-6952 !$#title Isolation and characterization of a cDNA clone for the gamma !1subunit of bovine retinal transducin. !$#cross-references MUID:85063709; PMID:6438626 !$#accession A03153 !'##molecule_type mRNA !'##residues 1-74 ##label HUR !'##cross-references GB:K02199; NID:g163786; PIDN:AAA30793.1; !1PID:g163787 !'##note the authors translated the codon GGG for residue 49 as Glu REFERENCE A22944 !$#authors Yatsunami, K.; Pandya, B.V.; Oprian, D.D.; Khorana, H.G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:1936-1940 !$#title cDNA-derived amino acid sequence of the gamma subunit of !1GTPase from bovine rod outer segments. !$#cross-references MUID:85166247; PMID:2984674 !$#accession A22944 !'##molecule_type mRNA !'##residues 1-74 ##label YAT !'##cross-references GB:K03255; NID:g163788; PIDN:AAA30794.1; !1PID:g163789 REFERENCE A91329 !$#authors Ovchinnikov, Y.A.; Lipkin, V.M.; Shuvaeva, T.M.; Bogachuk, !1A.P.; Shemyakin, V.V. !$#journal FEBS Lett. (1985) 179:107-110 !$#title Complete amino acid sequence of gamma-subunit of the !1GTP-binding protein from cattle retina. !$#cross-references MUID:85076983; PMID:3917402 !$#accession A91329 !'##molecule_type protein !'##residues 2-70 ##label OVC !'##note this protein was isolated from retinal rod outer segment REFERENCE I45984 !$#authors Van Dop, C.; Medynski, D.; Sullivan, K.; Wu, A.M.; Fung, !1B.K. !$#journal Biochem. Biophys. Res. Commun. (1984) 124:250-255 !$#title Partial cDNA sequence of the gamma subunit of transducin. !$#cross-references MUID:85046503; PMID:6149748 !$#accession I45984 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-40 ##label VAN !'##cross-references GB:K02436; NID:g163774; PIDN:AAA30788.1; !1PID:g163775 COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. COMMENT In mammals, several distinct types of gamma chains have been !1found. GENETICS !$#introns 32/3 CLASSIFICATION #superfamily GTP-binding regulatory protein gamma chain KEYWORDS GTP binding; heterotrimer; lipoprotein; methylated carboxyl !1end; prenylated cysteine; signal transduction FEATURE !$2-71 #product GTP-binding regulatory protein gamma chain !8#status experimental #label MAT\ !$36-37 #disulfide_bonds #status experimental\ !$71 #binding_site farnesyl (Cys) (covalent) #status !8predicted\ !$71 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted SUMMARY #length 74 #molecular-weight 8544 #checksum 6375 SEQUENCE /// ENTRY RGBOG2 #type complete TITLE GTP-binding regulatory protein gamma-2 chain - bovine ALTERNATE_NAMES GTP-binding regulatory protein S4 chain; guanine nucleotide binding protein gamma-2 chain; heterotrimeric G-protein gamma-2 chain; transducin gamma-2 chain ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 22-Jun-1999 ACCESSIONS B34228; A41352; JN0702; B36204 REFERENCE A92734 !$#authors Robishaw, J.D.; Kalman, V.K.; Moomaw, C.R.; Slaughter, C.A. !$#journal J. Biol. Chem. (1989) 264:15758-15761 !$#title Existence of two gamma subunits of the G proteins in brain. !$#cross-references MUID:89380157; PMID:2506169 !$#accession B34228 !'##molecule_type mRNA !'##residues 1-71 ##label ROB !'##cross-references GB:J05126 !'##experimental_source brain REFERENCE A41352 !$#authors Gautam, N.; Baetscher, M.; Aebersold, R.; Simon, M.I. !$#journal Science (1989) 244:971-974 !$#title A G protein gamma subunit shares homology with ras proteins. !$#cross-references MUID:89266904; PMID:2499046 !$#accession A41352 !'##molecule_type mRNA !'##residues 1-71 ##label GAU !'##cross-references GB:M37183; NID:g163116; PIDN:AAA30555.1; !1PID:g163117 REFERENCE JN0700 !$#authors Morishita, R.; Masuda, K.; Niwa, M.; Kato, K.; Asano, T. !$#journal Biochem. Biophys. Res. Commun. (1993) 194:1221-1227 !$#title Identification of three forms of the gamma subunit of G !1proteins isolated from bovine spleen. !$#cross-references MUID:93356792; PMID:8352779 !$#accession JN0702 !'##molecule_type protein !'##residues 5-29;37-40,'X',42-59;64-67 ##label MOR !'##experimental_source spleen REFERENCE A36204 !$#authors Gautam, N.; Northup, J.; Tamir, H.; Simon, M.I. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:7973-7977 !$#title G protein diversity is increased by associations with a !1variety of gamma subunits. !$#cross-references MUID:91045919; PMID:2122451 !$#contents annotation COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. COMMENT In mammals, several distinct types of gamma chains have been !1found. CLASSIFICATION #superfamily GTP-binding regulatory protein gamma chain KEYWORDS GTP binding; heterotrimer; lipoprotein; methylated carboxyl !1end; prenylated cysteine; signal transduction FEATURE !$2-68 #product GTP-binding regulatory protein gamma chain !8#status experimental #label MAT\ !$68 #binding_site geranyl-geranyl (Cys) (covalent) !8#status predicted\ !$68 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted SUMMARY #length 71 #molecular-weight 7850 #checksum 621 SEQUENCE /// ENTRY RGBOG3 #type complete TITLE GTP-binding regulatory protein gamma-3 chain - bovine ALTERNATE_NAMES guanine nucleotide binding protein gamma-3 chain; heterotrimeric G-protein gamma-3 chain; transducin gamma-3 chain ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 22-Jun-1999 ACCESSIONS A36204; S40452 REFERENCE A36204 !$#authors Gautam, N.; Northup, J.; Tamir, H.; Simon, M.I. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:7973-7977 !$#title G protein diversity is increased by associations with a !1variety of gamma subunits. !$#cross-references MUID:91045919; PMID:2122451 !$#accession A36204 !'##molecule_type mRNA !'##residues 1-75 ##label GAU !'##cross-references GB:M58349; NID:g163083; PIDN:AAA30539.1; !1PID:g163084 !'##experimental_source brain REFERENCE S40452 !$#authors Morishita, R.; Kato, K.; Asano, T. !$#journal FEBS Lett. (1994) 337:23-26 !$#title A brain-specific gamma subunit of G protein freed from the !1corresponding beta subunit under non-denaturing conditions. !$#cross-references MUID:94102396; PMID:8276106 !$#accession S40452 !'##molecule_type protein !'##residues 1-19 ##label MOR !'##experimental_source brain COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. COMMENT In mammals, several distinct types of gamma chains have been !1found. CLASSIFICATION #superfamily GTP-binding regulatory protein gamma chain KEYWORDS GTP binding; heterotrimer; lipoprotein; methylated carboxyl !1end; prenylated cysteine; signal transduction FEATURE !$1-72 #product GTP-binding regulatory protein gamma chain !8#status predicted #label MAT\ !$72 #binding_site geranyl-geranyl (Cys) (covalent) !8#status predicted\ !$72 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted SUMMARY #length 75 #molecular-weight 8305 #checksum 5356 SEQUENCE /// ENTRY RGHUB1 #type complete TITLE GTP-binding regulatory protein beta-1 chain - human ALTERNATE_NAMES guanine nucleotide binding protein beta-1 chain; heterotrimeric G-protein beta-1 chain; transducin beta-1 chain ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 22-Jun-1999 ACCESSIONS A24853 REFERENCE A91368 !$#authors Codina, J.; Stengel, D.; Woo, S.L.C.; Birnbaumer, L. !$#journal FEBS Lett. (1986) 207:187-192 !$#title Beta-subunits of the human liver Gs/Gi signal-transducing !1proteins and those of bovine retinal rod cell transducin are !1identical. !$#cross-references MUID:87030912; PMID:3095147 !$#accession A24853 !'##molecule_type mRNA !'##residues 1-340 ##label COD !'##cross-references GB:X04526; NID:g31667; PIDN:CAA28207.1; PID:g31669 !'##experimental_source liver !'##note the authors translated the codon GAG for residues 138 and 172 !1as Gln COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. COMMENT In mammals, four distinct types of beta chains have been !1found. GENETICS !$#gene GDB:GNB1 !'##cross-references GDB:119279; OMIM:139380 !$#map_position 1p36-1p31.2 CLASSIFICATION #superfamily GTP-binding regulatory protein beta chain; WD !1repeat homology KEYWORDS GTP binding; heterotrimer; signal transduction FEATURE !$51-84 #domain WD repeat homology #label WD1\ !$88-126 #domain WD repeat homology #label WD2\ !$139-171 #domain WD repeat homology #label WD3\ !$180-213 #domain WD repeat homology #label WD4\ !$222-255 #domain WD repeat homology #label WD5\ !$263-299 #domain WD repeat homology #label WD6\ !$308-340 #domain WD repeat homology #label WD7 SUMMARY #length 340 #molecular-weight 37377 #checksum 7578 SEQUENCE /// ENTRY RGBOB1 #type complete TITLE GTP-binding regulatory protein beta-1 chain - bovine ALTERNATE_NAMES guanine nucleotide binding protein beta-1 chain; heterotrimeric G-protein beta-1 chain; transducin beta-1 chain ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 22-Jun-1999 ACCESSIONS A24225; A25457 REFERENCE A24225 !$#authors Sugimoto, K.; Nukada, T.; Tanabe, T.; Takahashi, H.; Noda, !1M.; Minamino, N.; Kangawa, K.; Matsuo, H.; Hirose, T.; !1Inayama, S.; Numa, S. !$#journal FEBS Lett. (1985) 191:235-240 !$#title Primary structure of the beta-subunit of bovine transducin !1deduced from the cDNA sequence. !$#cross-references MUID:86030675; PMID:2414128 !$#accession A24225 !'##molecule_type mRNA !'##residues 1-340 ##label SUG !'##cross-references GB:X03073 REFERENCE A25457 !$#authors Fong, H.K.W.; Hurley, J.B.; Hopkins, R.S.; Miake-Lye, R.; !1Johnson, M.S.; Doolittle, R.F.; Simon, M.I. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:2162-2166 !$#title Repetitive segmental structure of the transducin beta !1subunit: homology with the CDC4 gene and identification of !1related mRNAs. !$#cross-references MUID:86177563; PMID:3083416 !$#accession A25457 !'##molecule_type mRNA !'##residues 1-340 ##label FON !'##cross-references GB:M13236; NID:g163782; PIDN:AAA30792.1; !1PID:g163783 COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. COMMENT In mammals, four distinct types of beta chains have been !1found. CLASSIFICATION #superfamily GTP-binding regulatory protein beta chain; WD !1repeat homology KEYWORDS GTP binding; heterotrimer; signal transduction FEATURE !$51-84 #domain WD repeat homology #label WD1\ !$88-126 #domain WD repeat homology #label WD2\ !$139-171 #domain WD repeat homology #label WD3\ !$180-213 #domain WD repeat homology #label WD4\ !$222-255 #domain WD repeat homology #label WD5\ !$263-299 #domain WD repeat homology #label WD6\ !$308-340 #domain WD repeat homology #label WD7 SUMMARY #length 340 #molecular-weight 37377 #checksum 7578 SEQUENCE /// ENTRY RGHUB2 #type complete TITLE GTP-binding regulatory protein beta-2 chain - human ALTERNATE_NAMES guanine nucleotide binding protein beta-2 chain; heterotrimeric G-protein beta-2 chain; transducin beta-2 chain ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 22-Jun-1999 ACCESSIONS B26617; B28040 REFERENCE A94155 !$#authors Fong, H.K.W.; Amatruda III, T.T.; Birren, B.W.; Simon, M.I. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:3792-3796 !$#title Distinct forms of the beta-subunit of GTP-binding regulatory !1proteins identified by molecular cloning. !$#cross-references MUID:87231903; PMID:3108879 !$#accession B26617 !'##molecule_type mRNA !'##residues 1-340 ##label FON !'##cross-references GB:M16514; NID:g183469; PIDN:AAA03179.1; !1PID:g386751 REFERENCE A94177 !$#authors Gao, B.; Gilman, A.G.; Robishaw, J.D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:6122-6125 !$#title A second form of the beta subunit of signal-transducing G !1proteins. !$#cross-references MUID:87317607; PMID:3114742 !$#accession B28040 !'##molecule_type mRNA !'##residues 1-340 ##label GAO !'##cross-references GB:M16538 COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. COMMENT In mammals, four distinct types of beta chains have been !1found. GENETICS !$#gene GDB:GNB2 !'##cross-references GDB:120004; OMIM:139390 !$#map_position 7q21.3-7q22.1 CLASSIFICATION #superfamily GTP-binding regulatory protein beta chain; WD !1repeat homology KEYWORDS GTP binding; heterotrimer; signal transduction FEATURE !$51-84 #domain WD repeat homology #label WD1\ !$88-126 #domain WD repeat homology #label WD2\ !$139-171 #domain WD repeat homology #label WD3\ !$180-213 #domain WD repeat homology #label WD4\ !$222-255 #domain WD repeat homology #label WD5\ !$263-299 #domain WD repeat homology #label WD6\ !$308-340 #domain WD repeat homology #label WD7 SUMMARY #length 340 #molecular-weight 37331 #checksum 6054 SEQUENCE /// ENTRY RGBOB2 #type fragment TITLE GTP-binding regulatory protein beta-2 chain - bovine (fragment) ALTERNATE_NAMES guanine nucleotide binding protein beta-2 chain; heterotrimeric G-protein beta-2 chain; transducin beta-2 chain ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 22-Jun-1999 ACCESSIONS A26617; A28040 REFERENCE A94155 !$#authors Fong, H.K.W.; Amatruda III, T.T.; Birren, B.W.; Simon, M.I. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:3792-3796 !$#title Distinct forms of the beta-subunit of GTP-binding regulatory !1proteins identified by molecular cloning. !$#cross-references MUID:87231903; PMID:3108879 !$#accession A26617 !'##molecule_type mRNA !'##residues 1-326 ##label FON !'##cross-references GB:M16480; NID:g163112; PIDN:AAA30553.1; !1PID:g163113 REFERENCE A94177 !$#authors Gao, B.; Gilman, A.G.; Robishaw, J.D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:6122-6125 !$#title A second form of the beta subunit of signal-transducing G !1proteins. !$#cross-references MUID:87317607; PMID:3114742 !$#accession A28040 !'##molecule_type mRNA !'##residues 88-270,'V',272-302 ##label GAO !'##cross-references GB:M16539; NID:g163110; PIDN:AAA30552.1; !1PID:g163111 COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. COMMENT In mammals, four distinct types of beta chains have been !1found. CLASSIFICATION #superfamily GTP-binding regulatory protein beta chain; WD !1repeat homology KEYWORDS GTP binding; heterotrimer; signal transduction FEATURE !$37-70 #domain WD repeat homology #label WD1\ !$74-112 #domain WD repeat homology #label WD2\ !$125-157 #domain WD repeat homology #label WD3\ !$166-199 #domain WD repeat homology #label WD4\ !$208-241 #domain WD repeat homology #label WD5\ !$249-285 #domain WD repeat homology #label WD6\ !$294-326 #domain WD repeat homology #label WD7 SUMMARY #length 326 #checksum 2664 SEQUENCE /// ENTRY RGHUB3 #type complete TITLE GTP-binding regulatory protein beta-3 chain - human ALTERNATE_NAMES guanine nucleotide binding protein beta-3 chain; heterotrimeric G-protein beta-3 chain; transducin beta-3 chain ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 22-Jun-1999 ACCESSIONS A35096 REFERENCE A35096 !$#authors Levine, M.A.; Smallwood, P.M.; Moen Jr., P.T.; Helman, L.J.; !1Ahn, T.G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:2329-2333 !$#title Molecular cloning of beta3 subunit, a third form of the G !1protein beta-subunit polypeptide. !$#cross-references MUID:90192801; PMID:2107550 !$#accession A35096 !'##molecule_type mRNA !'##residues 1-340 ##label LEV !'##cross-references GB:M31328; NID:g183412; PIDN:AAA52582.1; !1PID:g306776 COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. COMMENT In mammals, four distinct types of beta chains have been !1found. GENETICS !$#gene GDB:GNB3 !'##cross-references GDB:120005; OMIM:139130 !$#map_position 12p13-12p13 CLASSIFICATION #superfamily GTP-binding regulatory protein beta chain; WD !1repeat homology KEYWORDS GTP binding; heterotrimer; signal transduction FEATURE !$51-84 #domain WD repeat homology #label WD1\ !$88-126 #domain WD repeat homology #label WD2\ !$139-171 #domain WD repeat homology #label WD3\ !$180-213 #domain WD repeat homology #label WD4\ !$222-255 #domain WD repeat homology #label WD5\ !$263-299 #domain WD repeat homology #label WD6\ !$308-340 #domain WD repeat homology #label WD7 SUMMARY #length 340 #molecular-weight 37221 #checksum 5483 SEQUENCE /// ENTRY RGMSB4 #type complete TITLE GTP-binding regulatory protein beta-4 chain - mouse ALTERNATE_NAMES guanine nucleotide binding protein beta-4 chain; heterotrimeric G-protein beta-4 chain; transducin beta-4 chain ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 22-Jun-1999 ACCESSIONS JS0669 REFERENCE JS0669 !$#authors von Weizsaecker, E.; Strathmann, M.P.; Simon, M.I. !$#journal Biochem. Biophys. Res. Commun. (1992) 183:350-356 !$#title Diversity among the beta subunits of heterotrimeric !1GTP-binding proteins: characterization of a novel !1beta-subunit cDNA. !$#cross-references MUID:92181467; PMID:1543505 !$#accession JS0669 !'##molecule_type mRNA !'##residues 1-340 ##label VON !'##cross-references GB:S86124; NID:g246469; PIDN:AAB21609.1; !1PID:g246470 COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. COMMENT In mammals, four distinct types of beta chains have been !1found. CLASSIFICATION #superfamily GTP-binding regulatory protein beta chain; WD !1repeat homology KEYWORDS GTP binding; heterotrimer; signal transduction FEATURE !$51-84 #domain WD repeat homology #label WD1\ !$88-126 #domain WD repeat homology #label WD2\ !$139-171 #domain WD repeat homology #label WD3\ !$180-213 #domain WD repeat homology #label WD4\ !$222-255 #domain WD repeat homology #label WD5\ !$263-299 #domain WD repeat homology #label WD6\ !$308-340 #domain WD repeat homology #label WD7 SUMMARY #length 340 #molecular-weight 37354 #checksum 7739 SEQUENCE /// ENTRY RGKWB #type complete TITLE GTP-binding regulatory protein beta chain - Caenorhabditis elegans ALTERNATE_NAMES guanine nucleotide binding protein beta chain; heterotrimeric G-protein beta chain; transducin beta chain ORGANISM #formal_name Caenorhabditis elegans DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 22-Jun-1999 ACCESSIONS S09591 REFERENCE S09591 !$#authors van der Voorn, L.; Gebbink, M.; Plasterk, R.H.A.; Ploegh, !1H.L. !$#journal J. Mol. Biol. (1990) 213:17-26 !$#title Characterization of a G-protein beta-subunit gene from the !1nematode Caenorhabditis elegans. !$#cross-references MUID:90250769; PMID:2110981 !$#accession S09591 !'##molecule_type DNA !'##residues 1-340 ##label VAN !'##cross-references EMBL:X17497; NID:g6642; PIDN:CAA35532.1; PID:g6643 COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. COMMENT In mammals, four distinct types of beta chains have been !1found. GENETICS !$#introns 19/3; 57/3; 89/3; 115/2; 166/1; 209/3; 233/3; 305/2 CLASSIFICATION #superfamily GTP-binding regulatory protein beta chain; WD !1repeat homology KEYWORDS GTP binding; heterotrimer; signal transduction FEATURE !$51-84 #domain WD repeat homology #label WD1\ !$88-126 #domain WD repeat homology #label WD2\ !$139-171 #domain WD repeat homology #label WD3\ !$180-213 #domain WD repeat homology #label WD4\ !$222-255 #domain WD repeat homology #label WD5\ !$263-299 #domain WD repeat homology #label WD6\ !$308-340 #domain WD repeat homology #label WD7 SUMMARY #length 340 #molecular-weight 37491 #checksum 5633 SEQUENCE /// ENTRY RGOOBE #type complete TITLE GTP-binding regulatory protein beta chain - northern European squid ALTERNATE_NAMES guanine nucleotide binding protein beta chain; heterotrimeric G-protein beta chain; transducin beta chain ORGANISM #formal_name Loligo forbesi #common_name northern European squid DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 22-Jun-1999 ACCESSIONS S13302 REFERENCE S13302 !$#authors Ryba, N.J.P.; Pottinger, J.D.D.; Keen, J.N.; Findlay, J.B.C. !$#journal Biochem. J. (1991) 273:225-228 !$#title Sequence of the beta-subunit of the !1phosphatidylinositol-specific phospholipase C-directed !1GTP-binding protein from squid (Loligo forbesi) !1photoreceptors. !$#cross-references MUID:91113146; PMID:1899186 !$#accession S13302 !'##molecule_type mRNA !'##residues 1-341 ##label RYB !'##cross-references EMBL:X56757; NID:g9507; PIDN:CAA40077.1; PID:g9508 COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. CLASSIFICATION #superfamily GTP-binding regulatory protein beta chain; WD !1repeat homology KEYWORDS GTP binding; heterotrimer; signal transduction FEATURE !$52-85 #domain WD repeat homology #label WD1\ !$89-127 #domain WD repeat homology #label WD2\ !$140-172 #domain WD repeat homology #label WD3\ !$181-214 #domain WD repeat homology #label WD4\ !$223-256 #domain WD repeat homology #label WD5\ !$264-300 #domain WD repeat homology #label WD6\ !$309-341 #domain WD repeat homology #label WD7 SUMMARY #length 341 #molecular-weight 37323 #checksum 507 SEQUENCE /// ENTRY RGFFBH #type complete TITLE GTP-binding regulatory protein beta chain homolog - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 21-Jun-2002 ACCESSIONS A40489 REFERENCE A40489 !$#authors Yarfitz, S.; Provost, N.M.; Hurley, J.B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:7134-7138 !$#title Cloning of a Drosophila melanogaster guanine nucleotide !1regulatory protein beta-subunit gene and characterization of !1its expression during development. !$#cross-references MUID:89017152; PMID:3140235 !$#accession A40489 !'##molecule_type mRNA !'##residues 1-340 ##label YAR !'##cross-references GB:M22567; GB:J04083; NID:g157497; PIDN:AAB59247.1; !1PID:g157498 GENETICS !$#gene FlyBase:G-beta-13F !'##cross-references FlyBase:FBgn0001105 !$#map_position X13F CLASSIFICATION #superfamily GTP-binding regulatory protein beta chain; WD !1repeat homology FEATURE !$51-84 #domain WD repeat homology #label WD1\ !$88-126 #domain WD repeat homology #label WD2\ !$139-171 #domain WD repeat homology #label WD3\ !$180-213 #domain WD repeat homology #label WD4\ !$222-255 #domain WD repeat homology #label WD5\ !$263-299 #domain WD repeat homology #label WD6\ !$308-340 #domain WD repeat homology #label WD7 SUMMARY #length 340 #molecular-weight 37133 #checksum 5984 SEQUENCE /// ENTRY RGFFB #type complete TITLE GTP-binding regulatory protein beta chain - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES guanine nucleotide binding protein beta chain; heterotrimeric G-protein beta chain; transducin beta chain ORGANISM #formal_name Drosophila melanogaster DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 13-Sep-1997 ACCESSIONS JU0269 REFERENCE JU0269 !$#authors Yarfitz, S.; Niemi, G.A.; McConnell, J.L.; Fitch, C.L.; !1Hurley, J.B. !$#journal Neuron (1991) 7:429-438 !$#title A Gbeta protein in the Drosophila compound eye is different !1from that in the brain. !$#cross-references MUID:92000689; PMID:1910788 !$#accession JU0269 !'##molecule_type mRNA !'##residues 1-346 ##label YAR !'##cross-references GB:M76593 !'##experimental_source eye !'##note the authors translated the codon GTG for residue 116 as Glu COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. GENETICS !$#gene Gbe !'##cross-references FlyBase:FBgn0004623 CLASSIFICATION #superfamily GTP-binding regulatory protein beta chain; WD !1repeat homology KEYWORDS GTP binding; heterotrimer; signal transduction FEATURE !$55-88 #domain WD repeat homology #label WD1\ !$92-130 #domain WD repeat homology #label WD2\ !$145-177 #domain WD repeat homology #label WD3\ !$186-219 #domain WD repeat homology #label WD4\ !$228-261 #domain WD repeat homology #label WD5\ !$269-305 #domain WD repeat homology #label WD6\ !$314-346 #domain WD repeat homology #label WD7 SUMMARY #length 346 #molecular-weight 38303 #checksum 4681 SEQUENCE /// ENTRY RGHUA2 #type complete TITLE GTP-binding regulatory protein Gs alpha chain (adenylate cyclase-stimulating), splice form 2 - human ALTERNATE_NAMES guanine nucleotide binding protein Gs alpha-S2 chain; heterotrimeric G-protein Gs alpha-S2 chain CONTAINS GTP-binding regulatory protein Gs alpha chain, splice form 1 ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1990 #sequence_revision 15-Jun-1996 #text_change 19-Jan-2001 ACCESSIONS B31927; A31927; A24366; S02122; A25919 REFERENCE A31927 !$#authors Kozasa, T.; Itoh, H.; Tsukamoto, T.; Kaziro, Y. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:2081-2085 !$#title Isolation and characterization of the human G-s-alpha gene. !$#cross-references MUID:88176890; PMID:3127824 !$#accession B31927 !'##molecule_type DNA !'##residues 1-395 ##label KOZ2 !'##cross-references GB:M21142; DDBJ:J03647; NID:g183402; !1PIDN:AAA53147.1; PID:g386744 !'##note splice form 2 !$#accession A31927 !'##molecule_type DNA !'##residues 1-86,88-395 ##label KOZ1 !'##cross-references GB:M21142; DDBJ:J03647; NID:g183402; !1PIDN:AAA53146.1; PID:g386743 !'##note splice form 1 REFERENCE A24366 !$#authors Mattera, R.; Codina, J.; Crozat, A.; Kidd, V.; Woo, S.L.C.; !1Birnbaumer, L. !$#journal FEBS Lett. (1986) 206:36-42 !$#title Identification by molecular cloning of two forms of the !1alpha-subunit of the human liver stimulatory (Gs) regulatory !1component of adenylyl cyclase. !$#cross-references MUID:87005246; PMID:3093273 !$#accession A24366 !'##molecule_type mRNA !'##residues 1-86,88-395 ##label MAT !'##cross-references EMBL:X04408; NID:g31914; PIDN:CAA27996.1; !1PID:g31915 REFERENCE S02122 !$#authors Harris, B.A. !$#journal Nucleic Acids Res. (1988) 16:3585 !$#title Complete cDNA sequence of a human stimulatory GTP-binding !1protein alpha subunit. !$#cross-references MUID:88233954; PMID:3131741 !$#accession S02122 !'##molecule_type mRNA !'##residues 1-5,'T',7-86,88-395 ##label HAR !'##cross-references EMBL:X07036; NID:g31951; PIDN:CAA30084.1; !1PID:g31952 REFERENCE A25919 !$#authors Bray, P.; Carter, A.; Simons, C.; Guo, V.; Puckett, C.; !1Kamholz, J.; Spiegel, A.; Nirenberg, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:8893-8897 !$#title Human cDNA clones for four species of G-alpha-s-signal !1transduction protein. !$#cross-references MUID:87067419; PMID:3024154 !$#accession A25919 !'##molecule_type mRNA !'##residues 12-230,'Q',232-395 ##label BRA !'##cross-references GB:M14631; NID:g183416; PIDN:AAA52583.1; !1PID:g386748 !'##note the authors translated the codon CAA for residue 221 as Glu COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. COMMENT The Gs alpha chain is specific for G protein that is !1responsible for transduction of stimulatory signals from !1receptors to adenylate cyclase; it activates the cyclase in !1response to adrenergic stimuli. COMMENT See also PIR:RGHUA1. GENETICS !$#gene GDB:GNAS1; GNAS !'##cross-references GDB:120628; OMIM:139320 !$#map_position 20q13.2-20q13.3 !$#introns 47/1; 71/2; 86/2; 105/3; 145/3; 178/2; 196/3; 221/2; 241/1; !1281/2; 325/1; 347/3 CLASSIFICATION #superfamily GTP-binding regulatory protein Gs alpha chain KEYWORDS alternative splicing; blocked amino end; GTP binding; !1heterotrimer; lipoprotein; myristylation; nucleotide !1binding; P-loop; signal transduction; thiolester bond FEATURE !$2-395 #product GTP-binding regulatory protein Gs alpha !8chain, splice form 2 #status predicted #label MAT2\ !$2-86,88-395 #product GTP-binding regulatory protein Gs alpha !8chain, splice form 1 #status predicted #label MAT1\ !$47-54 #region nucleotide-binding motif A (P-loop)\ !$293-296 #region GTP-binding NKXD motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$202 #modified_site ADP-ribosylarginine (Arg) (by cholera !8toxin) #status predicted SUMMARY #length 395 #molecular-weight 45751 #checksum 4643 SEQUENCE /// ENTRY RGHUA1 #type complete TITLE GTP-binding regulatory protein Gs alpha chain (adenylate cyclase-stimulating), splice form 4 - human ALTERNATE_NAMES guanine nucleotide binding protein Gs alpha-S1 chain; heterotrimeric G-protein Gs alpha-S1 chain CONTAINS GTP-binding regulatory protein Gs alpha chain, splice form 3 ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 19-Jan-2001 ACCESSIONS C31927; D31927; B24366 REFERENCE A31927 !$#authors Kozasa, T.; Itoh, H.; Tsukamoto, T.; Kaziro, Y. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:2081-2085 !$#title Isolation and characterization of the human G-s-alpha gene. !$#cross-references MUID:88176890; PMID:3127824 !$#accession C31927 !'##molecule_type DNA !'##residues 1-71,73-380 ##label KOZ3 !'##cross-references GB:M21142; DDBJ:J03647; NID:g183402; !1PIDN:AAA53148.1; PID:g386745 !'##note splice form 3 !$#accession D31927 !'##molecule_type DNA !'##residues 1-380 ##label KOZ4 !'##cross-references GB:M21142; DDBJ:J03647; NID:g183402; !1PIDN:AAA53149.1; PID:g386746 !'##note splice form 4 REFERENCE A24366 !$#authors Mattera, R.; Codina, J.; Crozat, A.; Kidd, V.; Woo, S.L.C.; !1Birnbaumer, L. !$#journal FEBS Lett. (1986) 206:36-42 !$#title Identification by molecular cloning of two forms of the !1alpha-subunit of the human liver stimulatory (Gs) regulatory !1component of adenylyl cyclase. !$#cross-references MUID:87005246; PMID:3093273 !$#accession B24366 !'##molecule_type mRNA !'##residues 1-380 ##label MAT !'##cross-references EMBL:X04409; NID:g31912; PIDN:CAA27997.1; !1PID:g31913 COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. COMMENT The Gs alpha chain is specific for G protein that is !1responsible for transduction of stimulatory signals from !1receptors to adenylate cyclase; it activates the cyclase in !1response to adrenergic stimuli. COMMENT See also PIR:RGHUA2. GENETICS !$#gene GDB:GNAS1; GNAS !'##cross-references GDB:120628; OMIM:139320 !$#map_position 20q13.2-20q13.3 CLASSIFICATION #superfamily GTP-binding regulatory protein Gs alpha chain KEYWORDS alternative splicing; blocked amino end; GTP binding; !1heterotrimer; lipoprotein; myristylation; nucleotide !1binding; P-loop; signal transduction; thiolester bond FEATURE !$2-380 #product GTP-binding regulatory protein Gs alpha !8chain, splice form 4 #status predicted #label MAT4\ !$2-71,73-380 #product GTP-binding regulatory protein Gs alpha !8chain, splice form 3 #status predicted #label MAT3\ !$47-54 #region nucleotide-binding motif A (P-loop)\ !$278-281 #region GTP-binding NKXD motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$187 #modified_site ADP-ribosylarginine (Arg) (by cholera !8toxin) #status predicted SUMMARY #length 380 #molecular-weight 44266 #checksum 856 SEQUENCE /// ENTRY RGMSA2 #type complete TITLE GTP-binding regulatory protein Gs alpha-S2 chain (adenylate cyclase-stimulating) - mouse ALTERNATE_NAMES guanine nucleotide binding protein Gs alpha-S2 chain; heterotrimeric G-protein Gs alpha-S2 chain ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-Jan-2001 ACCESSIONS S03075 REFERENCE S03075 !$#authors Rall, T.; Harris, B.A. !$#journal FEBS Lett. (1987) 224:365-371 !$#title Identification of the lesion in the stimulatory GTP-binding !1protein of the uncoupled S49 lymphoma. !$#cross-references MUID:88083563; PMID:2826231 !$#accession S03075 !'##molecule_type mRNA !'##residues 1-394 ##label RAL !'##cross-references GB:Y00703; NID:g51127; PIDN:CAA68695.1; PID:g51128 COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. COMMENT The Gs alpha chain is specific for G protein that is !1responsible for transduction of stimulatory signals from !1receptors to adenylate cyclase; it activates the cyclase in !1response to adrenergic stimuli. CLASSIFICATION #superfamily GTP-binding regulatory protein Gs alpha chain KEYWORDS alternative splicing; blocked amino end; GTP binding; !1heterotrimer; lipoprotein; myristylation; nucleotide !1binding; P-loop; signal transduction; thiolester bond FEATURE !$2-394 #product GTP-binding regulatory protein Gs alpha-S2 !8chain #status predicted #label MAT\ !$47-54 #region nucleotide-binding motif A (P-loop)\ !$292-295 #region GTP-binding NKXD motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$201 #modified_site ADP-ribosylarginine (Arg) (by cholera !8toxin) #status predicted SUMMARY #length 394 #molecular-weight 45605 #checksum 1351 SEQUENCE /// ENTRY RGBOGA #type complete TITLE GTP-binding regulatory protein Gs alpha-2 chain (adenylate cyclase-stimulating) - bovine ALTERNATE_NAMES guanine nucleotide binding protein Gs alpha-2 chain; heterotrimeric G-protein Gs alpha-2 chain ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 19-Jan-2001 ACCESSIONS A23818; A23615; A23813 REFERENCE A23813 !$#authors Robishaw, J.D.; Russell, D.W.; Harris, B.A.; Smigel, M.D.; !1Gilman, A.G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:1251-1255 !$#title Deduced primary structure of the alpha subunit of the !1GTP-binding stimulatory protein of adenylate cyclase. !$#cross-references MUID:86149283; PMID:3081893 !$#accession A23818 !'##molecule_type mRNA !'##residues 1-394 ##label ROB !'##cross-references GB:M13006; NID:g163127; PIDN:AAA30560.1; !1PID:g163128 REFERENCE A23615 !$#authors Nukada, T.; Tanabe, T.; Takahashi, H.; Noda, M.; Hirose, T.; !1Inayama, S.; Numa, S. !$#journal FEBS Lett. (1986) 195:220-224 !$#title Primary structure of the alpha-subunit of bovine adenylate !1cyclase-stimulating G-protein deduced from the cDNA !1sequence. !$#cross-references MUID:86108870; PMID:3080331 !$#accession A23615 !'##molecule_type mRNA !'##residues 1-17,'A',19-84,'D',86-362,'F',364-394 ##label NUK !'##cross-references GB:M13006 COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. COMMENT The Gs alpha chain is specific for G protein that is !1responsible for transduction of stimulatory signals from !1receptors to adenylate cyclase; it activates the cyclase in !1response to adrenergic stimuli. CLASSIFICATION #superfamily GTP-binding regulatory protein Gs alpha chain KEYWORDS alternative splicing; blocked amino end; GTP binding; !1heterotrimer; lipoprotein; myristylation; nucleotide !1binding; P-loop; signal transduction; thiolester bond FEATURE !$2-394 #product GTP-binding regulatory protein Gs alpha-2 !8chain #status predicted #label MAT\ !$47-54 #region nucleotide-binding motif A (P-loop)\ !$292-295 #region GTP-binding NKXD motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$201 #modified_site ADP-ribosylarginine (Arg) (by cholera !8toxin) #status predicted SUMMARY #length 394 #molecular-weight 45606 #checksum 2297 SEQUENCE /// ENTRY RGRTA2 #type complete TITLE GTP-binding regulatory protein Gs alpha-2 chain (adenylate cyclase-stimulating) - rat ALTERNATE_NAMES guanine nucleotide binding protein Gs alpha-2 chain; heterotrimeric G-protein Gs alpha-2 chain ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-Jan-2001 ACCESSIONS A27423; C24882 REFERENCE A92614 !$#authors Jones, D.T.; Reed, R.R. !$#journal J. Biol. Chem. (1987) 262:14241-14249 !$#title Molecular cloning of five GTP-binding protein cDNA species !1from rat olfactory neuroepithelium. !$#cross-references MUID:88007678; PMID:2820999 !$#accession A27423 !'##molecule_type mRNA !'##residues 1-394 ##label JON !'##cross-references GB:M17525; NID:g203171; PIDN:AAA40827.1; !1PID:g203172 REFERENCE A94707 !$#authors Itoh, H.; Kozasa, T.; Nagata, S.; Nakamura, S.; Katada, T.; !1Ui, M.; Iwai, S.; Ohtsuka, E.; Kawasaki, H.; Suzuki, K.; !1Kaziro, Y. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:3776-3780 !$#title Molecular cloning and sequence determination of cDNAs for !1alpha subunits of the guanine nucleotide-binding proteins !1G-s, G-i, and G-o from rat brain. !$#cross-references MUID:86233317; PMID:3086867 !$#accession C24882 !'##molecule_type mRNA !'##residues 1-394 ##label ITO !'##cross-references GB:M12673; NID:g204441; PIDN:AAA41261.1; !1PID:g204442 COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. COMMENT The Gs alpha chain is specific for G protein that is !1responsible for transduction of stimulatory signals from !1receptors to adenylate cyclase; it activates the cyclase in !1response to adrenergic stimuli. CLASSIFICATION #superfamily GTP-binding regulatory protein Gs alpha chain KEYWORDS blocked amino end; GTP binding; lipoprotein; myristylation; !1nucleotide binding; P-loop; signal transduction; thiolester !1bond FEATURE !$2-394 #product GTP-binding regulatory protein Gs alpha-2 !8chain #status predicted #label MAT\ !$47-54 #region nucleotide-binding motif A (P-loop)\ !$292-295 #region GTP-binding NKXD motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$201 #modified_site ADP-ribosylarginine (Arg) (by cholera !8toxin) #status predicted SUMMARY #length 394 #molecular-weight 45663 #checksum 1695 SEQUENCE /// ENTRY RGHYA2 #type complete TITLE GTP-binding regulatory protein Gs alpha-2 chain (adenylate cyclase-stimulating) - golden hamster ALTERNATE_NAMES guanine nucleotide binding protein Gs alpha-2 chain; heterotrimeric G-protein Gs alpha-2 chain ORGANISM #formal_name Mesocricetus auratus #common_name golden hamster DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-Jan-2001 ACCESSIONS S10508 REFERENCE S10508 !$#authors Conner, D.A.; Feldman, A.M.; van Dop, C. !$#journal Nucleic Acids Res. (1990) 18:4279 !$#title cDNA sequence for the alpha subunit of the guanine !1nucleotide-binding protein that stimulates adenylyl cyclase !1(G) in Syrian hamster heart (Mesocricetus auratus). !$#cross-references MUID:90332451; PMID:2115997 !$#accession S10508 !'##molecule_type mRNA !'##residues 1-394 ##label CON !'##cross-references EMBL:X53139; NID:g49642; PIDN:CAA37299.1; !1PID:g49643 COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. COMMENT The Gs alpha chain is specific for G protein that is !1responsible for transduction of stimulatory signals from !1receptors to adenylate cyclase; it activates the cyclase in !1response to adrenergic stimuli. CLASSIFICATION #superfamily GTP-binding regulatory protein Gs alpha chain KEYWORDS alternative splicing; blocked amino end; GTP binding; !1heterotrimer; lipoprotein; myristylation; nucleotide !1binding; P-loop; signal transduction; thiolester bond FEATURE !$2-394 #product GTP-binding regulatory protein Gs alpha-2 !8chain #status predicted #label MAT\ !$47-54 #region nucleotide-binding motif A (P-loop)\ !$292-295 #region GTP-binding NKXD motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$201 #modified_site ADP-ribosylarginine (Arg) (by cholera !8toxin) #status predicted SUMMARY #length 394 #molecular-weight 45663 #checksum 1695 SEQUENCE /// ENTRY RGHYAE #type complete TITLE GTP-binding regulatory protein Gs alpha-2 chain (adenylate cyclase-stimulating) - Chinese hamster ALTERNATE_NAMES guanine nucleotide binding protein Gs alpha-2 chain; heterotrimeric G-protein Gs alpha-2 chain ORGANISM #formal_name Cricetulus griseus #common_name Chinese hamster DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-Jan-2001 ACCESSIONS S08140 REFERENCE S08140 !$#authors Mercken, L.; Moras, V.; Tocque, B.; Mayaux, J.F. !$#journal Nucleic Acids Res. (1990) 18:662 !$#title The cDNA sequence of the alpha-subunit of the Chinese !1hamster adenylate cyclase-stimulatory G-protein. !$#cross-references MUID:90175000; PMID:2106672 !$#accession S08140 !'##molecule_type mRNA !'##residues 1-394 ##label MER !'##cross-references EMBL:X17481; NID:g49491; PIDN:CAA35516.1; !1PID:g49492 COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. COMMENT The Gs alpha chain is specific for G protein that is !1responsible for transduction of stimulatory signals from !1receptors to adenylate cyclase; it activates the cyclase in !1response to adrenergic stimuli. CLASSIFICATION #superfamily GTP-binding regulatory protein Gs alpha chain KEYWORDS alternative splicing; blocked amino end; GTP binding; !1heterotrimer; lipoprotein; myristylation; nucleotide !1binding; P-loop; signal transduction; thiolester bond FEATURE !$2-394 #product GTP-binding regulatory protein Gs alpha-2 !8chain #status predicted #label MAT\ !$47-54 #region nucleotide-binding motif A (P-loop)\ !$292-295 #region GTP-binding NKXD motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$201 #modified_site ADP-ribosylarginine (Arg) (by cholera !8toxin) #status predicted SUMMARY #length 394 #molecular-weight 45664 #checksum 1635 SEQUENCE /// ENTRY RGPGA2 #type complete TITLE GTP-binding regulatory protein Gs alpha-2 chain (adenylate cyclase-stimulating) - pig ALTERNATE_NAMES guanine nucleotide binding protein Gs alpha-2 chain; heterotrimeric G-protein Gs alpha-2 chain ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-Jan-2001 ACCESSIONS S18963 REFERENCE S18963 !$#authors Roth, D.A.; Kay, R.A.M.; Hammond, H.K. !$#submission submitted to the EMBL Data Library, January 1992 !$#accession S18963 !'##molecule_type mRNA !'##residues 1-397 ##label ROT !'##cross-references EMBL:X63893; NID:g1957; PIDN:CAA45355.1; PID:g1958 COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. COMMENT The Gs alpha chain is specific for G protein that is !1responsible for transduction of stimulatory signals from !1receptors to adenylate cyclase; it activates the cyclase in !1response to adrenergic stimuli. CLASSIFICATION #superfamily GTP-binding regulatory protein Gs alpha chain KEYWORDS alternative splicing; blocked amino end; GTP binding; !1heterotrimer; lipoprotein; myristylation; nucleotide !1binding; P-loop; signal transduction; thiolester bond FEATURE !$2-397 #product GTP-binding regulatory protein Gs alpha-2 !8chain #status predicted #label MAT\ !$47-54 #region nucleotide-binding motif A (P-loop)\ !$277-280 #region GTP-binding NKXD motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$186 #modified_site ADP-ribosylarginine (Arg) (by cholera !8toxin) #status predicted SUMMARY #length 397 #molecular-weight 46476 #checksum 1249 SEQUENCE /// ENTRY RGMSA1 #type complete TITLE GTP-binding regulatory protein Gs alpha-S1 chain (adenylate cyclase-stimulating) - mouse ALTERNATE_NAMES guanine nucleotide binding protein Gs alpha-S1 chain; heterotrimeric G-protein Gs alpha-S1 chain ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-Jan-2001 ACCESSIONS A25889 REFERENCE A94123 !$#authors Sullivan, K.A.; Liao, Y.C.; Alborzi, A.; Beiderman, B.; !1Chang, F.H.; Masters, S.B.; Levinson, A.D.; Bourne, H.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:6687-6691 !$#title Inhibitory and stimulatory G proteins of adenylate cyclase: !1cDNA and amino acid sequences of the alpha chains. !$#cross-references MUID:86313643; PMID:3092218 !$#accession A25889 !'##molecule_type mRNA !'##residues 1-377 ##label SUL !'##cross-references GB:M13964; NID:g193652; PIDN:AAA37745.1; !1PID:g309277 COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. COMMENT The Gs alpha chain is specific for G protein that is !1responsible for transduction of stimulatory signals from !1receptors to adenylate cyclase; it activates the cyclase in !1response to adrenergic stimuli. CLASSIFICATION #superfamily GTP-binding regulatory protein Gs alpha chain KEYWORDS alternative splicing; GTP binding; heterotrimer; nucleotide !1binding; P-loop; signal transduction FEATURE !$45-52 #region nucleotide-binding motif A (P-loop)\ !$275-278 #region GTP-binding NKXD motif\ !$51 #binding_site GTP (Lys) #status predicted\ !$184 #modified_site ADP-ribosylarginine (Arg) (by cholera !8toxin) #status predicted SUMMARY #length 377 #molecular-weight 43654 #checksum 1398 SEQUENCE /// ENTRY RGXLA #type complete TITLE GTP-binding regulatory protein Gs alpha chain (adenylate cyclase-stimulating) - African clawed frog ALTERNATE_NAMES guanine nucleotide binding protein Gs alpha chain; heterotrimeric G-protein Gs alpha chain ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-Jan-2001 ACCESSIONS S11047 REFERENCE S11045 !$#authors Olate, J.; Martinez, S.; Purcell, P.; Jorquera, H.; Codina, !1J.; Birnbaumer, L.; Allende, J.E. !$#journal FEBS Lett. (1990) 268:27-31 !$#title Molecular cloning and sequence determination of four !1different cDNA species coding for alpha-subunits of G !1proteins from Xenopus laevis oocytes. !$#cross-references MUID:90346157; PMID:2116977 !$#accession S11047 !'##molecule_type mRNA !'##residues 1-379 ##label OLA !'##cross-references GB:X56091; NID:g64713; PIDN:CAA39571.1; PID:g64714 COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. CLASSIFICATION #superfamily GTP-binding regulatory protein Gs alpha chain KEYWORDS alternative splicing; blocked amino end; GTP binding; !1heterotrimer; lipoprotein; myristylation; nucleotide !1binding; P-loop; signal transduction; thiolester bond FEATURE !$2-379 #product GTP-binding regulatory protein Gs alpha !8chain #status predicted #label MAT\ !$47-54 #region nucleotide-binding motif A (P-loop)\ !$277-280 #region GTP-binding NKXD motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$186 #modified_site ADP-ribosylarginine (Arg) (by cholera !8toxin) #status predicted SUMMARY #length 379 #molecular-weight 44546 #checksum 8668 SEQUENCE /// ENTRY RGFFAL #type complete TITLE GTP-binding regulatory protein Gs alpha-L chain (adenylate cyclase-stimulating) - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES guanine nucleotide binding protein Gs alpha-L chain; heterotrimeric G-protein Gs alpha-L chain ORGANISM #formal_name Drosophila melanogaster DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 21-Jun-2002 ACCESSIONS A34754; A32911 REFERENCE A34754 !$#authors Quan, F.; Forte, M.A. !$#journal Mol. Cell. Biol. (1990) 10:910-917 !$#title Two forms of Drosophila melanogaster Gsalpha are produced by !1alternate splicing involving an unusual splice site. !$#cross-references MUID:90158605; PMID:2106072 !$#accession A34754 !'##molecule_type DNA !'##residues 1-385 ##label QUA2 !'##cross-references GB:M33997; GB:M33998; NID:g157524; PIDN:AAA28578.1; !1PID:g157526 REFERENCE A32911 !$#authors Quan, F.; Wolfgang, W.J.; Forte, M.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:4321-4325 !$#title The Drosophila gene coding for the alpha subunit of a !1stimulatory G protein is preferentially expressed in the !1nervous system. !$#cross-references MUID:89264611; PMID:2498884 !$#accession A32911 !'##molecule_type mRNA !'##residues 1-385 ##label QUA1 !'##cross-references GB:M23233; NID:g158509; PIDN:AAA28917.1; !1PID:g158510 COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. COMMENT The Gs alpha chain is specific for G protein that is !1responsible for transduction of stimulatory signals from !1receptors to adenylate cyclase; it activates the cyclase in !1response to adrenergic stimuli. GENETICS !$#gene FlyBase:G-s-alpha-60A !'##cross-references FlyBase:FBgn0001123 !$#introns 92/3; 125/1; 165/2; 208/2; 268/2; 310/1; 337/3 CLASSIFICATION #superfamily GTP-binding regulatory protein Gs alpha chain KEYWORDS alternative splicing; blocked amino end; GTP binding; !1heterotrimer; lipoprotein; myristylation; nucleotide !1binding; P-loop; signal transduction; thiolester bond FEATURE !$2-385 #product GTP-binding regulatory protein Gs alpha-L !8chain #status predicted #label MAT\ !$50-57 #region nucleotide-binding motif A (P-loop)\ !$280-283 #region GTP-binding NKXD motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$189 #modified_site ADP-ribosylarginine (Arg) (by cholera !8toxin) #status predicted SUMMARY #length 385 #molecular-weight 44999 #checksum 7711 SEQUENCE /// ENTRY RGFFAS #type complete TITLE GTP-binding regulatory protein Gs alpha-S chain (adenylate cyclase-stimulating) - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES guanine nucleotide binding protein Gs alpha-S chain; heterotrimeric G protein Gs alpha-S chain ORGANISM #formal_name Drosophila melanogaster DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 21-Jun-2002 ACCESSIONS B34754 REFERENCE A34754 !$#authors Quan, F.; Forte, M.A. !$#journal Mol. Cell. Biol. (1990) 10:910-917 !$#title Two forms of Drosophila melanogaster Gsalpha are produced by !1alternate splicing involving an unusual splice site. !$#cross-references MUID:90158605; PMID:2106072 !$#accession B34754 !'##molecule_type DNA !'##residues 1-382 ##label QUA !'##cross-references GB:M33997; GB:M33998; NID:g157524; PIDN:AAA28579.1; !1PID:g157527 COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. COMMENT The Gs alpha chain is specific for G protein that is !1responsible for transduction of stimulatory signals from !1receptors to adenylate cyclase; it activates the cyclase in !1response to adrenergic stimuli. GENETICS !$#gene FlyBase:G-s-alpha-60A !'##cross-references FlyBase:FBgn0001123 !$#introns 92/3; 125/1; 165/2; 208/2; 268/2; 310/1; 337/3 CLASSIFICATION #superfamily GTP-binding regulatory protein Gs alpha chain KEYWORDS blocked amino end; GTP binding; lipoprotein; myristylation; !1nucleotide binding; P-loop; signal transduction; thiolester !1bond FEATURE !$2-382 #product GTP-binding regulatory protein Gs alpha-S !8chain #status predicted #label MAT\ !$50-57 #region nucleotide-binding motif A (P-loop)\ !$280-283 #region GTP-binding NKXD motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$189 #modified_site ADP-ribosylarginine (Arg) (by cholera !8toxin) #status predicted SUMMARY #length 382 #molecular-weight 44699 #checksum 8310 SEQUENCE /// ENTRY RGHUI1 #type complete TITLE GTP-binding regulatory protein Gi alpha-1 chain (adenylate cyclase-inhibiting) - human ALTERNATE_NAMES guanine nucleotide binding protein Gi alpha-1 chain; heterotrimeric G-protein Gi alpha-1 chain; protein DKFZp564K1216.1 ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1992 #sequence_revision 22-Nov-1996 #text_change 19-Jan-2001 ACCESSIONS A28318; D28154; T08669 REFERENCE A28318 !$#authors Bray, P.; Carter, A.; Guo, V.; Puckett, C.; Kamholz, J.; !1Spiegel, A.; Nirenberg, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:5115-5119 !$#title Human cDNA clones for an alpha subunit of Gi !1signal-transduction protein. !$#cross-references MUID:87260939; PMID:3110783 !$#accession A28318 !'##molecule_type mRNA !'##residues 6-354 ##label BRA !'##cross-references GB:M17219; NID:g183410; PIDN:AAA52581.1; !1PID:g386747 REFERENCE A28154 !$#authors Itoh, H.; Toyama, R.; Kozasa, T.; Tsukamoto, T.; Matsuoka, !1M.; Kaziro, Y. !$#journal J. Biol. Chem. (1988) 263:6656-6664 !$#title Presence of three distinct molecular species of G-i protein !1alpha-subunit. Structure of rat cDNAs and human genomic !1DNAs. !$#cross-references MUID:88198230; PMID:2834384 !$#accession D28154 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-101 ##label ITO !'##cross-references GB:M20596; GB:M19476; NID:g183189; PIDN:AAA35893.1; !1PID:g183191 REFERENCE Z16467 !$#authors Duesterhoeft, A.; Lauber, J.; Mewes, H.W.; Gassenhuber, J.; !1Wiemann, S. !$#submission submitted to the Protein Sequence Database, March 1999 !$#accession T08669 !'##molecule_type mRNA !'##residues !1'WGGCSAATGGSAAATVPRDSKPQTRDLGALSRAGKQSLVVRNSRPLLSAPLRTASPSTP !1LRKWWGRRGPRREAFERPLGERKDSPVLGARTRARRERRQALAFGT',1-137,'G', !1139-354 ##label DUE !'##cross-references EMBL:AL049933 !'##experimental_source fetal brain; clone DKFZp564K1216 !'##note differences are due to different assignment of start codons COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. COMMENT The Gi alpha chain is specific for G protein that is !1involved in hormonal regulation of adenylate cyclase; it !1inhibits the cyclase in response to beta-adrenergic stimuli. GENETICS !$#gene GDB:GNAI1 !'##cross-references GDB:120001; OMIM:139310 !$#map_position 7q21-7q21 !$#note DKFZp564K1216.1 CLASSIFICATION #superfamily GTP-binding regulatory protein Gs alpha chain KEYWORDS blocked amino end; GTP binding; heterotrimer; lipoprotein; !1myristylation; nucleotide binding; P-loop; signal !1transduction; thiolester bond FEATURE !$2-354 #product GTP-binding regulatory protein Gi alpha-1 !8chain #status predicted #label MAT\ !$40-47 #region nucleotide-binding motif A (P-loop)\ !$269-272 #region GTP-binding NKXD motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$178 #modified_site ADP-ribosylarginine (Arg) (by cholera !8toxin) #status predicted\ !$351 #modified_site ADP-ribosylcysteine (Cys) (by !8pertussis toxin) #status predicted SUMMARY #length 354 #molecular-weight 40361 #checksum 3009 SEQUENCE /// ENTRY RGBOI1 #type complete TITLE GTP-binding regulatory protein Gi alpha-1 chain (adenylate cyclase-inhibiting) - bovine ALTERNATE_NAMES guanine nucleotide binding protein Gi alpha-1 chain; heterotrimeric G-protein Gi alpha-1 chain ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-Jan-2001 ACCESSIONS A23631; A25888 REFERENCE A23631 !$#authors Nukada, T.; Tanabe, T.; Takahashi, H.; Noda, M.; Haga, K.; !1Haga, T.; Ichiyama, A.; Kangawa, K.; Hiranaga, M.; Matsuo, !1H.; Numa, S. !$#journal FEBS Lett. (1986) 197:305-310 !$#title Primary structure of the alpha-subunit of bovine adenylate !1cyclase-inhibiting G-protein deduced from the cDNA sequence. !$#cross-references MUID:86136587; PMID:2419165 !$#accession A23631 !'##molecule_type mRNA !'##residues 1-354 ##label NUK !'##cross-references GB:X03642; NID:g390; PIDN:CAA27288.1; PID:g391 REFERENCE A94131 !$#authors Michel, T.; Winslow, J.W.; Smith, J.A.; Seidman, J.G.; Neer, !1E.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:7663-7667 !$#title Molecular cloning and characterization of cDNA encoding the !1GTP-binding protein alpha-i and identification of a related !1protein, alpha-h. !$#cross-references MUID:87017009; PMID:3094012 !$#accession A25888 !'##molecule_type mRNA !'##residues 106-112,'S',114-329,'N',331-336,'E',338-354 ##label MIC !'##cross-references GB:M14207; NID:g163129; PIDN:AAA30561.1; !1PID:g163130 COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. COMMENT The Gi alpha chain is specific for G protein that is !1involved in hormonal regulation of adenylate cyclase; it !1inhibits the cyclase in response to beta-adrenergic stimuli. CLASSIFICATION #superfamily GTP-binding regulatory protein Gs alpha chain KEYWORDS blocked amino end; GTP binding; heterotrimer; lipoprotein; !1myristylation; nucleotide binding; P-loop; signal !1transduction; thiolester bond FEATURE !$2-354 #product GTP-binding regulatory protein Gi alpha-1 !8chain #status predicted #label MAT\ !$40-47 #region nucleotide-binding motif A (P-loop)\ !$269-272 #region GTP-binding NKXD motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$178 #modified_site ADP-ribosylarginine (Arg) (by cholera !8toxin) #status predicted\ !$351 #modified_site ADP-ribosylcysteine (Cys) (by !8pertussis toxin) #status predicted SUMMARY #length 354 #molecular-weight 40361 #checksum 3009 SEQUENCE /// ENTRY RGRTI1 #type complete TITLE GTP-binding regulatory protein Gi alpha-1 chain (adenylate cyclase-inhibiting) - rat ALTERNATE_NAMES guanine nucleotide binding protein Gi alpha-1 chain; heterotrimeric G-protein Gi alpha-1 chain ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-Jan-2001 ACCESSIONS C27423 REFERENCE A92614 !$#authors Jones, D.T.; Reed, R.R. !$#journal J. Biol. Chem. (1987) 262:14241-14249 !$#title Molecular cloning of five GTP-binding protein cDNA species !1from rat olfactory neuroepithelium. !$#cross-references MUID:88007678; PMID:2820999 !$#accession C27423 !'##molecule_type mRNA !'##residues 1-354 ##label JON !'##cross-references GB:M17527; NID:g203167; PIDN:AAA40825.1; !1PID:g203168 COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. COMMENT The Gi alpha chain is specific for G protein that is !1involved in hormonal regulation of adenylate cyclase; it !1inhibits the cyclase in response to beta-adrenergic stimuli. CLASSIFICATION #superfamily GTP-binding regulatory protein Gs alpha chain KEYWORDS blocked amino end; GTP binding; heterotrimer; lipoprotein; !1myristylation; nucleotide binding; P-loop; signal !1transduction; thiolester bond FEATURE !$2-354 #product GTP-binding regulatory protein Gi alpha-1 !8chain #status predicted #label MAT\ !$40-47 #region nucleotide-binding motif A (P-loop)\ !$269-272 #region GTP-binding NKXD motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$178 #modified_site ADP-ribosylarginine (Arg) (by cholera !8toxin) #status predicted\ !$351 #modified_site ADP-ribosylcysteine (Cys) (by !8pertussis toxin) #status predicted SUMMARY #length 354 #molecular-weight 40345 #checksum 2271 SEQUENCE /// ENTRY RGXLI1 #type complete TITLE GTP-binding regulatory protein Gi alpha-1 chain (adenylate cyclase-inhibiting) - African clawed frog ALTERNATE_NAMES guanine nucleotide binding protein Gi alpha-1 chain; heterotrimeric G-protein Gi alpha-1 chain ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-Jan-2001 ACCESSIONS S11045 REFERENCE S11045 !$#authors Olate, J.; Martinez, S.; Purcell, P.; Jorquera, H.; Codina, !1J.; Birnbaumer, L.; Allende, J.E. !$#journal FEBS Lett. (1990) 268:27-31 !$#title Molecular cloning and sequence determination of four !1different cDNA species coding for alpha-subunits of G !1proteins from Xenopus laevis oocytes. !$#cross-references MUID:90346157; PMID:2116977 !$#accession S11045 !'##molecule_type mRNA !'##residues 1-354 ##label OLA !'##cross-references GB:X56089; NID:g64707; PIDN:CAA39569.1; PID:g64708 COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. COMMENT The Gi alpha chain is specific for G protein that is !1involved in hormonal regulation of adenylate cyclase; it !1inhibits the cyclase in response to beta-adrenergic stimuli. CLASSIFICATION #superfamily GTP-binding regulatory protein Gs alpha chain KEYWORDS blocked amino end; GTP binding; heterotrimer; lipoprotein; !1myristylation; nucleotide binding; P-loop; signal !1transduction; thiolester bond FEATURE !$2-354 #product GTP-binding regulatory protein Gi alpha-1 !8chain #status predicted #label MAT\ !$40-47 #region nucleotide-binding motif A (P-loop)\ !$269-272 #region GTP-binding NKXD motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$178 #modified_site ADP-ribosylarginine (Arg) (by cholera !8toxin) #status predicted\ !$351 #modified_site ADP-ribosylcysteine (Cys) (by !8pertussis toxin) #status predicted SUMMARY #length 354 #molecular-weight 40401 #checksum 4014 SEQUENCE /// ENTRY RGHUI2 #type complete TITLE GTP-binding regulatory protein Gi alpha-2 chain (adenylate cyclase-inhibiting) - human ALTERNATE_NAMES guanine nucleotide binding protein Gi alpha-2 chain; heterotrimeric G-protein Gi alpha-2 chain ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 19-Jan-2001 ACCESSIONS S02319; A29025; B28154; S00618; S02320 REFERENCE S02319 !$#authors Beals, C.R.; Wilson, C.B.; Perlmutter, R.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:7886-7890 !$#title A small multigene family encodes G(i) signal-transduction !1proteins. !$#cross-references MUID:88068503; PMID:3120178 !$#accession S02319 !'##molecule_type mRNA !'##residues 1-355 ##label BEA !'##cross-references EMBL:J03004; NID:g183181; PIDN:AAA52556.1; !1PID:g183182 REFERENCE A29025 !$#authors Didsbury, J.R.; Ho, Y.S.; Snyderman, R. !$#journal FEBS Lett. (1987) 211:160-164 !$#title Human Gi protein alpha-subunit: deduction of amino acid !1structure from a cloned cDNA. !$#cross-references MUID:87105966; PMID:3100330 !$#accession A29025 !'##molecule_type mRNA !'##residues 1-355 ##label DID !'##cross-references EMBL:X04828; NID:g31743; PIDN:CAA28512.1; !1PID:g31744 REFERENCE A28154 !$#authors Itoh, H.; Toyama, R.; Kozasa, T.; Tsukamoto, T.; Matsuoka, !1M.; Kaziro, Y. !$#journal J. Biol. Chem. (1988) 263:6656-6664 !$#title Presence of three distinct molecular species of G-i protein !1alpha-subunit. Structure of rat cDNAs and human genomic !1DNAs. !$#cross-references MUID:88198230; PMID:2834384 !$#accession B28154 !'##molecule_type mRNA !'##residues 1-355 ##label ITO !'##cross-references GB:J03221 REFERENCE S00618 !$#authors Weinstein, L.S.; Spiegel, A.M.; Carter, A.D. !$#journal FEBS Lett. (1988) 232:333-340 !$#title Cloning and characterization of the human gene for the !1alpha-subunit of Gi2, a GTP-binding signal transduction !1protein. !$#cross-references MUID:88242822; PMID:2837412 !$#accession S00618 !'##molecule_type DNA !'##residues 1-39 ##label WEI !'##cross-references EMBL:X07854; NID:g31739; PIDN:CAA30703.1; !1PID:g31740 COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. COMMENT The Gi alpha chain is specific for G protein that is !1involved in hormonal regulation of adenylate cyclase; it !1inhibits the cyclase in response to beta-adrenergic stimuli. GENETICS !$#gene GDB:GNAI2; GNAI2B !'##cross-references GDB:120516; OMIM:139360 !$#map_position 3p21.3-3p21.2 !$#introns 40/1; 54/2; 101/3; 155/2; 198/2; 241/3; 293/1 CLASSIFICATION #superfamily GTP-binding regulatory protein Gs alpha chain KEYWORDS blocked amino end; GTP binding; heterotrimer; lipoprotein; !1myristylation; nucleotide binding; P-loop; signal !1transduction; thiolester bond FEATURE !$2-355 #product GTP-binding regulatory protein Gi alpha-2 !8chain #status predicted #label MAT\ !$40-47 #region nucleotide-binding motif A (P-loop)\ !$270-273 #region GTP-binding NKXD motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$179 #modified_site ADP-ribosylarginine (Arg) (by cholera !8toxin) #status predicted\ !$352 #modified_site ADP-ribosylcysteine (Cys) (by !8pertussis toxin) #status predicted SUMMARY #length 355 #molecular-weight 40451 #checksum 4146 SEQUENCE /// ENTRY RGRTI2 #type complete TITLE GTP-binding regulatory protein Gi alpha-2 chain (adenylate cyclase-inhibiting) - rat ALTERNATE_NAMES guanine nucleotide binding protein Gi alpha-2 chain; heterotrimeric G-protein Gi alpha-2 chain ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-Jan-2001 ACCESSIONS D27423; B24882; B35377 REFERENCE A92614 !$#authors Jones, D.T.; Reed, R.R. !$#journal J. Biol. Chem. (1987) 262:14241-14249 !$#title Molecular cloning of five GTP-binding protein cDNA species !1from rat olfactory neuroepithelium. !$#cross-references MUID:88007678; PMID:2820999 !$#accession D27423 !'##molecule_type mRNA !'##residues 1-355 ##label JON !'##cross-references GB:M17528; NID:g203165; PIDN:AAA40824.1; !1PID:g203166 REFERENCE A94707 !$#authors Itoh, H.; Kozasa, T.; Nagata, S.; Nakamura, S.; Katada, T.; !1Ui, M.; Iwai, S.; Ohtsuka, E.; Kawasaki, H.; Suzuki, K.; !1Kaziro, Y. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:3776-3780 !$#title Molecular cloning and sequence determination of cDNAs for !1alpha subunits of the guanine nucleotide-binding proteins !1G-s, G-i, and G-o from rat brain. !$#cross-references MUID:86233317; PMID:3086867 !$#accession B24882 !'##molecule_type mRNA !'##residues 1-355 ##label ITO !'##cross-references GB:M12672; NID:g204439; PIDN:AAA41260.1; !1PID:g204440 REFERENCE A35377 !$#authors Linder, M.E.; Ewald, D.A.; Miller, R.J.; Gilman, A.G. !$#journal J. Biol. Chem. (1990) 265:8243-8251 !$#title Purification and characterization of G-oalpha and three !1types of G-ialpha after expression in Escherichia coli. !$#cross-references MUID:90243707; PMID:2159473 !$#accession B35377 !'##molecule_type protein !'##residues 112-126 ##label LIN COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. COMMENT The Gi alpha chain is specific for G protein that is !1involved in hormonal regulation of adenylate cyclase; it !1inhibits the cyclase in response to beta-adrenergic stimuli. CLASSIFICATION #superfamily GTP-binding regulatory protein Gs alpha chain KEYWORDS blocked amino end; GTP binding; heterotrimer; lipoprotein; !1myristylation; nucleotide binding; P-loop; signal !1transduction; thiolester bond FEATURE !$2-355 #product GTP-binding regulatory protein Gi alpha-2 !8chain #status predicted #label MAT\ !$40-47 #region nucleotide-binding motif A (P-loop)\ !$270-273 #region GTP-binding NKXD motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$179 #modified_site ADP-ribosylarginine (Arg) (by cholera !8toxin) #status predicted\ !$352 #modified_site ADP-ribosylcysteine (Cys) (by !8pertussis toxin) #status predicted SUMMARY #length 355 #molecular-weight 40499 #checksum 3438 SEQUENCE /// ENTRY RGMSI2 #type complete TITLE GTP-binding regulatory protein Gi alpha-2 chain (adenylate cyclase-inhibiting) - mouse ALTERNATE_NAMES guanine nucleotide binding protein Gi alpha-2 chain; heterotrimeric G-protein Gi alpha-2 chain ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-Jan-2001 ACCESSIONS B25889 REFERENCE A94123 !$#authors Sullivan, K.A.; Liao, Y.C.; Alborzi, A.; Beiderman, B.; !1Chang, F.H.; Masters, S.B.; Levinson, A.D.; Bourne, H.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:6687-6691 !$#title Inhibitory and stimulatory G proteins of adenylate cyclase: !1cDNA and amino acid sequences of the alpha chains. !$#cross-references MUID:86313643; PMID:3092218 !$#accession B25889 !'##molecule_type mRNA !'##residues 1-355 ##label SUL !'##cross-references GB:M13963; NID:g193513; PIDN:AAA37692.1; !1PID:g309255 COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. COMMENT The Gi alpha chain is specific for G protein that is !1involved in hormonal regulation of adenylate cyclase; it !1inhibits the cyclase in response to beta-adrenergic stimuli. CLASSIFICATION #superfamily GTP-binding regulatory protein Gs alpha chain KEYWORDS blocked amino end; GTP binding; heterotrimer; lipoprotein; !1myristylation; nucleotide binding; P-loop; signal !1transduction; thiolester bond FEATURE !$2-355 #product GTP-binding regulatory protein Gi alpha-2 !8chain #status predicted #label MAT\ !$40-47 #region nucleotide-binding motif A (P-loop)\ !$270-273 #region GTP-binding NKXD motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$179 #modified_site ADP-ribosylarginine (Arg) (by cholera !8toxin) #status predicted\ !$352 #modified_site ADP-ribosylcysteine (Cys) (by !8pertussis toxin) #status predicted SUMMARY #length 355 #molecular-weight 40556 #checksum 4088 SEQUENCE /// ENTRY RGHUI3 #type complete TITLE GTP-binding regulatory protein Gi alpha-3 chain (adenylate cyclase-inhibiting) - human ALTERNATE_NAMES GTP-binding regulatory protein Gk alpha chain; guanine nucleotide binding protein Gi alpha-3 chain; heterotrimeric G-protein Gi alpha-3 chain ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 19-Jan-2001 ACCESSIONS S02348; S00055; A32139; C28154; A28157; S00078 REFERENCE S02319 !$#authors Beals, C.R.; Wilson, C.B.; Perlmutter, R.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:7886-7890 !$#title A small multigene family encodes G(i) signal-transduction !1proteins. !$#cross-references MUID:88068503; PMID:3120178 !$#accession S02348 !'##molecule_type mRNA !'##residues 1-354 ##label BEA !'##cross-references EMBL:J03005; NID:g183183; PIDN:AAA52557.1; !1PID:g183184 REFERENCE S00055 !$#authors Didsbury, J.R.; Snyderman, R. !$#journal FEBS Lett. (1987) 219:259-263 !$#title Molecular cloning of a new human G protein. Evidence for two !1G(i-alpha)-like protein families. !$#cross-references MUID:87247315; PMID:3109953 !$#accession S00055 !'##molecule_type mRNA !'##residues 1-354 ##label DID !'##cross-references EMBL:M27543; NID:g183395; PIDN:AAA52579.1; !1PID:g183396 !'##note the sequence from Fig. 2 is inconsistent with that from Fig. 1 !1in having 17-Met and 18-Lys REFERENCE A32139 !$#authors Kim, S.; Ang, S.L.; Bloch, D.B.; Bloch, K.D.; Kawahara, Y.; !1Tolman, C.; Lee, R.; Seidman, J.G.; Neer, E.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:4153-4157 !$#title Identification of cDNA encoding an additional alpha-subunit !1of a human GTP-binding protein: expression of three alpha-i !1subtypes in human tissues and cell lines. !$#cross-references MUID:88247980; PMID:3132707 !$#accession A32139 !'##molecule_type mRNA !'##residues 1-354 ##label KIM !'##cross-references GB:J03238; NID:g183686; PIDN:AAA35939.1; !1PID:g306822 REFERENCE A28154 !$#authors Itoh, H.; Toyama, R.; Kozasa, T.; Tsukamoto, T.; Matsuoka, !1M.; Kaziro, Y. !$#journal J. Biol. Chem. (1988) 263:6656-6664 !$#title Presence of three distinct molecular species of G-i protein !1alpha-subunit. Structure of rat cDNAs and human genomic !1DNAs. !$#cross-references MUID:88198230; PMID:2834384 !$#accession C28154 !'##molecule_type DNA !'##residues 1-354 ##label ITO !'##cross-references GB:J03220 REFERENCE A28157 !$#authors Codina, J.; Olate, J.; Abramowitz, J.; Mattera, R.; Cook, !1R.G.; Birnbaumer, L. !$#journal J. Biol. Chem. (1988) 263:6746-6750 !$#title Alpha-i-3 cDNA encodes the alpha-subunit of G-K, the !1stimulatory G protein of receptor-regulated K+ channels. !$#cross-references MUID:88198244; PMID:2452165 !$#accession A28157 !'##molecule_type mRNA !'##residues 1-354 ##label COD !'##cross-references GB:J03198; NID:g183224; PIDN:AAA35896.1; !1PID:g183225 REFERENCE S00078 !$#authors Suki, W.N.; Abramowitz, J.; Mattera, R.; Codina, J.; !1Birnbaumer, L. !$#journal FEBS Lett. (1987) 220:187-192 !$#title The human genome encodes at least three non-allellic G !1proteins with alpha(i)-type subunits. !$#cross-references MUID:87276552; PMID:2440724 !$#accession S00078 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 'C',22-354 ##label SUK COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. COMMENT The Gi alpha chain is specific for G protein that is !1involved in hormonal regulation of adenylate cyclase; it !1inhibits the cyclase in response to beta-adrenergic stimuli. GENETICS !$#gene GDB:GNAI3 !'##cross-references GDB:119276; OMIM:139370 !$#map_position 1p13-1p13 CLASSIFICATION #superfamily GTP-binding regulatory protein Gs alpha chain KEYWORDS blocked amino end; GTP binding; heterotrimer; lipoprotein; !1myristylation; nucleotide binding; P-loop; signal !1transduction; thiolester bond FEATURE !$2-354 #product GTP-binding regulatory protein Gi alpha-3 !8chain #status predicted #label MAT\ !$40-47 #region nucleotide-binding motif A (P-loop)\ !$269-272 #region GTP-binding NKXD motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$178 #modified_site ADP-ribosylarginine (Arg) (by cholera !8toxin) #status predicted\ !$351 #modified_site ADP-ribosylcysteine (Cys) (by !8pertussis toxin) #status predicted SUMMARY #length 354 #molecular-weight 40532 #checksum 6659 SEQUENCE /// ENTRY RGRTI3 #type complete TITLE GTP-binding regulatory protein Gi alpha-3 chain (adenylate cyclase-inhibiting) - rat ALTERNATE_NAMES GTP-binding regulatory protein Gk alpha chain; guanine nucleotide binding protein Gi alpha-3 chain; heterotrimeric G-protein Gi alpha-3 chain ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-Jan-2001 ACCESSIONS E27423; A28154; C35377 REFERENCE A92614 !$#authors Jones, D.T.; Reed, R.R. !$#journal J. Biol. Chem. (1987) 262:14241-14249 !$#title Molecular cloning of five GTP-binding protein cDNA species !1from rat olfactory neuroepithelium. !$#cross-references MUID:88007678; PMID:2820999 !$#accession E27423 !'##molecule_type mRNA !'##residues 1-354 ##label JON !'##cross-references GB:M20713; NID:g203163; PIDN:AAA40823.1; !1PID:g203164 REFERENCE A28154 !$#authors Itoh, H.; Toyama, R.; Kozasa, T.; Tsukamoto, T.; Matsuoka, !1M.; Kaziro, Y. !$#journal J. Biol. Chem. (1988) 263:6656-6664 !$#title Presence of three distinct molecular species of G-i protein !1alpha-subunit. Structure of rat cDNAs and human genomic !1DNAs. !$#cross-references MUID:88198230; PMID:2834384 !$#accession A28154 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-354 ##label ITO !'##cross-references GB:J03219; NID:g204320; PIDN:AAA41224.1; !1PID:g204321 REFERENCE A35377 !$#authors Linder, M.E.; Ewald, D.A.; Miller, R.J.; Gilman, A.G. !$#journal J. Biol. Chem. (1990) 265:8243-8251 !$#title Purification and characterization of G-oalpha and three !1types of G-ialpha after expression in Escherichia coli. !$#cross-references MUID:90243707; PMID:2159473 !$#accession C35377 !'##status preliminary !'##molecule_type protein !'##residues 111-125 ##label LIN COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. COMMENT The Gi alpha chain is specific for G protein that is !1involved in hormonal regulation of adenylate cyclase; it !1inhibits the cyclase in response to beta-adrenergic stimuli. CLASSIFICATION #superfamily GTP-binding regulatory protein Gs alpha chain KEYWORDS blocked amino end; GTP binding; heterotrimer; lipoprotein; !1myristylation; nucleotide binding; P-loop; signal !1transduction; thiolester bond FEATURE !$2-354 #product GTP-binding regulatory protein Gi alpha-3 !8chain #status predicted #label MAT\ !$40-47 #region nucleotide-binding motif A (P-loop)\ !$269-272 #region GTP-binding NKXD motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$178 #modified_site ADP-ribosylarginine (Arg) (by cholera !8toxin) #status predicted\ !$351 #modified_site ADP-ribosylcysteine (Cys) (by !8pertussis toxin) #status predicted SUMMARY #length 354 #molecular-weight 40522 #checksum 7162 SEQUENCE /// ENTRY RGXLI3 #type fragment TITLE GTP-binding regulatory protein Gi alpha-3 chain (adenylate cyclase-inhibiting) - African clawed frog (fragment) ALTERNATE_NAMES GTP-binding regulatory protein Gk alpha chain; guanine nucleotide binding protein Gi alpha-3 chain; heterotrimeric G-protein Gi alpha-3 chain ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-Jan-2001 ACCESSIONS S11046 REFERENCE S11045 !$#authors Olate, J.; Martinez, S.; Purcell, P.; Jorquera, H.; Codina, !1J.; Birnbaumer, L.; Allende, J.E. !$#journal FEBS Lett. (1990) 268:27-31 !$#title Molecular cloning and sequence determination of four !1different cDNA species coding for alpha-subunits of G !1proteins from Xenopus laevis oocytes. !$#cross-references MUID:90346157; PMID:2116977 !$#accession S11046 !'##molecule_type mRNA !'##residues 1-345 ##label OLA !'##cross-references GB:X56090; NID:g64709; PIDN:CAA39570.1; PID:g64710 COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. COMMENT The Gi alpha chain is specific for G protein that is !1involved in hormonal regulation of adenylate cyclase; it !1inhibits the cyclase in response to beta-adrenergic stimuli. CLASSIFICATION #superfamily GTP-binding regulatory protein Gs alpha chain KEYWORDS GTP binding; heterotrimer; nucleotide binding; P-loop; !1signal transduction FEATURE !$31-38 #region nucleotide-binding motif A (P-loop)\ !$260-263 #region GTP-binding NKXD motif\ !$37 #binding_site GTP (Lys) #status predicted\ !$169 #modified_site ADP-ribosylarginine (Arg) (by cholera !8toxin) #status predicted\ !$342 #modified_site ADP-ribosylcysteine (Cys) (by !8pertussis toxin) #status predicted SUMMARY #length 345 #checksum 2092 SEQUENCE /// ENTRY RGFFA #type complete TITLE GTP-binding regulatory protein Gi alpha chain (adenylate cyclase-inhibiting) - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES guanine nucleotide binding protein Gi alpha chain; heterotrimeric G-protein Gi alpha chain ORGANISM #formal_name Drosophila melanogaster DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 21-Jun-2002 ACCESSIONS A31076 REFERENCE A31076 !$#authors Provost, N.M.; Somers, D.E.; Hurley, J.B. !$#journal J. Biol. Chem. (1988) 263:12070-12076 !$#title A Drosophila melanogaster G protein alpha-subunit gene is !1expressed primarily in embryos and pupae. !$#cross-references MUID:88298893; PMID:3136172 !$#accession A31076 !'##molecule_type mRNA !'##residues 1-355 ##label PRO !'##cross-references GB:M23094; GB:J03903; NID:g340809; PIDN:AAA28565.1; !1PID:g517048 COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. COMMENT The Gi alpha chain is specific for G protein that is !1involved in hormonal regulation of adenylate cyclase; it !1inhibits the cyclase in response to beta-adrenergic stimuli. GENETICS !$#gene FlyBase:G-i-alpha-65A !'##cross-references FlyBase:FBgn0001104 CLASSIFICATION #superfamily GTP-binding regulatory protein Gs alpha chain KEYWORDS blocked amino end; GTP binding; heterotrimer; lipoprotein; !1myristylation; nucleotide binding; P-loop; signal !1transduction; thiolester bond FEATURE !$2-355 #product GTP-binding regulatory protein Gi alpha !8chain #status predicted #label MAT\ !$41-48 #region nucleotide-binding motif A (P-loop)\ !$270-273 #region GTP-binding NKXD motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$179 #modified_site ADP-ribosylarginine (Arg) (by cholera !8toxin) #status predicted SUMMARY #length 355 #molecular-weight 40609 #checksum 8255 SEQUENCE /// ENTRY RGRTGX #type complete TITLE GTP-binding regulatory protein Gx alpha chain - rat ALTERNATE_NAMES guanine nucleotide binding protein Gx alpha chain; heterotrimeric G-protein Gx alpha chain ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-Jan-2001 ACCESSIONS A31316 REFERENCE A31316 !$#authors Matsuoka, M.; Itoh, H.; Kozasa, T.; Kaziro, Y. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:5384-5388 !$#title Sequence analysis of cDNA and genomic DNA for a putative !1pertussis toxin-insensitive guanine nucleotide-binding !1regulatory protein alpha-subunit. !$#cross-references MUID:88289726; PMID:2456569 !$#accession A31316 !'##molecule_type mRNA !'##residues 1-355 ##label MAT !'##cross-references GB:J03773; NID:g204546; PIDN:AAA41304.1; !1PID:g204547 COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. CLASSIFICATION #superfamily GTP-binding regulatory protein Gs alpha chain KEYWORDS blocked amino end; GTP binding; heterotrimer; lipoprotein; !1myristylation; nucleotide binding; P-loop; signal !1transduction; thiolester bond FEATURE !$2-355 #product GTP-binding regulatory protein Gx alpha !8chain #status predicted #label MAC\ !$40-47 #region nucleotide-binding motif A (P-loop)\ !$270-273 #region GTP-binding NKXD motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$179 #modified_site ADP-ribosylarginine (Arg) (by cholera !8toxin) #status predicted SUMMARY #length 355 #molecular-weight 40879 #checksum 8343 SEQUENCE /// ENTRY RGHUGY #type complete TITLE GTP-binding regulatory protein Gy alpha chain - human ALTERNATE_NAMES guanine nucleotide binding protein Gy alpha chain; heterotrimeric G-protein Gy alpha chain ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-Jan-2001 ACCESSIONS A39394 REFERENCE A39394 !$#authors Jiang, M.; Pandey, S.; Tran, V.T.; Fong, H.K.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:3907-3911 !$#title Guanine nucleotide-binding regulatory proteins in retinal !1pigment epithelial cells. !$#cross-references MUID:91219481; PMID:1902575 !$#accession A39394 !'##molecule_type mRNA !'##residues 1-359 ##label JIA !'##cross-references GB:M69013; NID:g183690; PIDN:AAA58624.1; !1PID:g183691 COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. GENETICS !$#gene GDB:GNA11 !'##cross-references GDB:132587; OMIM:139313 !$#map_position 19p13.3-19p13.3 CLASSIFICATION #superfamily GTP-binding regulatory protein Gs alpha chain KEYWORDS GTP binding; heterotrimer; nucleotide binding; P-loop; !1signal transduction FEATURE !$46-53 #region nucleotide-binding motif A (P-loop)\ !$274-277 #region GTP-binding NKXD motif\ !$52 #binding_site GTP (Lys) #status predicted\ !$183 #modified_site ADP-ribosylarginine (Arg) (by cholera !8toxin) #status predicted SUMMARY #length 359 #molecular-weight 42163 #checksum 6732 SEQUENCE /// ENTRY RGHUGX #type complete TITLE GTP-binding regulatory protein Gx alpha chain - human ALTERNATE_NAMES GTP-binding regulatory protein G-z alpha chain; guanine nucleotide binding protein Gx alpha chain; heterotrimeric G-protein Gx alpha chain ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-Jan-2001 ACCESSIONS A36628; A31339; A61179 REFERENCE A36628 !$#authors Matsuoka, M.; Itoh, H.; Kaziro, Y. !$#journal J. Biol. Chem. (1990) 265:13215-13220 !$#title Characterization of the human gene for G-xalpha, a pertussis !1toxin-insensitive regulatory GTP-binding protein. !$#cross-references MUID:90330667; PMID:2115889 !$#accession A36628 !'##molecule_type DNA !'##residues 1-355 ##label MAT !'##cross-references GB:J05541 REFERENCE A31339 !$#authors Fong, H.K.W.; Yoshimoto, K.K.; Eversole-Cire, P.; Simon, !1M.I. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:3066-3070 !$#title Identification of a GTP-binding protein alpha-subunit that !1lacks an apparent ADP-ribosylation site for pertussis toxin. !$#cross-references MUID:88203641; PMID:3129724 !$#accession A31339 !'##molecule_type mRNA !'##residues 1-355 ##label FON !'##cross-references GB:D90150 REFERENCE A61179 !$#authors Gagnon, A.W.; Manning, D.R.; Catani, L.; Gewirtz, A.; Poncz, !1M.; Brass, L.F. !$#journal Blood (1991) 78:1247-1253 !$#title Identification of G-zalpha as a pertussis toxin-insensitive !1G protein in human platelets and megakaryocytes. !$#cross-references MUID:91346834; PMID:1908722 !$#accession A61179 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-355 ##label GAG !'##note the authors translated the codon TGG for residue 132 as Tyr and !1GAC for residue 273 as Asn COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. GENETICS !$#gene GDB:GNAZ !'##cross-references GDB:120003; OMIM:139160 !$#map_position 22q11.2-22q11.2 !$#introns 241/3 CLASSIFICATION #superfamily GTP-binding regulatory protein Gs alpha chain KEYWORDS blocked amino end; GTP binding; heterotrimer; lipoprotein; !1myristylation; nucleotide binding; P-loop; signal !1transduction; thiolester bond FEATURE !$2-355 #product GTP-binding regulatory protein Gx alpha !8chain #status predicted #label MAC\ !$40-47 #region nucleotide-binding motif A (P-loop)\ !$270-273 #region GTP-binding NKXD motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$179 #modified_site ADP-ribosylarginine (Arg) (by cholera !8toxin) #status predicted SUMMARY #length 355 #molecular-weight 40923 #checksum 7324 SEQUENCE /// ENTRY RGHUO1 #type complete TITLE GTP-binding regulatory protein Go alpha chain, splice form alpha-1 - human ALTERNATE_NAMES guanine nucleotide binding protein Go alpha-1 chain; heterotrimeric G-protein Go alpha-1 chain ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-Jan-2001 ACCESSIONS A40436; I52224 REFERENCE A40436 !$#authors Tsukamoto, T.; Toyama, R.; Itoh, H.; Kozasa, T.; Matsuoka, !1M.; Kaziro, Y. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:2974-2978 !$#title Structure of the human gene and two rat cDNAs encoding the !1alpha chain of GTP-binding regulatory protein G-o: two !1different mRNAs are generated by alternative splicing. !$#cross-references MUID:91195273; PMID:1901650 !$#accession A40436 !'##molecule_type DNA !'##residues 1-354 ##label TSU !'##cross-references GB:M60156 !'##note the authors translated the codon AAG for residue 17 as Leu REFERENCE I52224 !$#authors Lavu, S.; Clark, J.; Swarup, R.; Matsushima, K.; Paturu, K.; !1Moss, J.; Kung, H.F. !$#journal Biochem. Biophys. Res. Commun. (1988) 150:811-815 !$#title Molecular cloning and DNA sequence analysis of the human !1guanine nucleotide-binding protein Go alpha. !$#cross-references MUID:88134191; PMID:3124840 !$#accession I52224 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-15,'G',17-170,'L',172-217,'E',219-354 ##label LAV !'##cross-references GB:M19182; NID:g183424; PIDN:AAA52584.1; !1PID:g386750 COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. COMMENT The Go alpha chain, a substrate for ADP-ribosylation by !1cholera toxin and pertussis toxin, exists mainly in !1mammalian brain and neuronal tissues. GENETICS !$#gene GDB:GNAO1 !'##cross-references GDB:118803; OMIM:139311 !$#map_position 16q13-16q13 !$#introns 40/1; 54/2; 101/3; 155/2; 188/2; 241/3; 293/1 CLASSIFICATION #superfamily GTP-binding regulatory protein Gs alpha chain KEYWORDS alternative splicing; blocked amino end; GTP binding; !1heterotrimer; lipoprotein; myristylation; nucleotide !1binding; P-loop; signal transduction; thiolester bond FEATURE !$2-354 #product GTP-binding regulatory protein Go alpha-1 !8chain #status predicted #label MAT\ !$40-47 #region nucleotide-binding motif A (P-loop)\ !$270-273 #region GTP-binding NKXD motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$46 #binding_site GTP (Lys) #status predicted\ !$179 #modified_site ADP-ribosylarginine (Arg) (by cholera !8toxin) #status predicted\ !$351 #modified_site ADP-ribosylcysteine (Cys) (by !8pertussis toxin) #status predicted SUMMARY #length 354 #molecular-weight 40050 #checksum 5191 SEQUENCE /// ENTRY RGBOO1 #type complete TITLE GTP-binding regulatory protein Go alpha chain, splice form alpha-1 [validated] - bovine ALTERNATE_NAMES GTP-binding regulatory protein 39K chain; guanine nucleotide binding protein Go alpha-1 chain; heterotrimeric G-protein Go alpha-1 chain ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-Jan-2001 ACCESSIONS S00213; S05600; A34980; A28011; A25948; C25888 REFERENCE S00213 !$#authors Ovchinnikov, Y.A.; Slepak, V.Z.; Pronin, A.N.; Shlensky, !1A.B.; Levina, N.B.; Voeikov, V.L.; Lipkin, V.M. !$#journal FEBS Lett. (1987) 226:91-95 !$#title Primary structure of bovine cerebellum GTP-binding protein !1G39 and its effect on the adenylate cyclase system. !$#cross-references MUID:88083643; PMID:3121394 !$#accession S00213 !'##molecule_type mRNA !'##residues 1-354 ##label OVC1 !'##note part of this sequence was confirmed by protein sequencing REFERENCE S05600 !$#authors Ovchinnikov, Y.A.; Slepak, V.Z.; Pronin, A.N.; Shlenskii, !1A.B.; Levina, N.B.; Voeikov, V.L.; Bystrov, N.S.; !1Severtsova, I.V.; Lipkin, V.M. !$#journal Dokl. Biochem. (1987) 297:404-406 !$#title G39, GTP-binding protein from bovine cerebellum. Amino acid !1sequence and nucleotide sequence of the corresponding cDNA. !$#accession S05600 !'##molecule_type mRNA !'##residues 1-354 ##label OVC2 !'##cross-references EMBL:X12924 !'##note the authors translated the codon TTC for residue 253 as Ser !$#accession A34980 !'##molecule_type protein !'##residues 22-42;47-51;53-58, !159-67;75-80;89-105;114-130;146-159;163-171;182-185;194-198; !1291-298,299-307;319-320;322-324;326-328 ##label OVC3 !'##note this paper is a translation of the Russian paper published in !1Dokl. Akad. Nauk SSSR (1987) 297: 1006-1009 REFERENCE A28011 !$#authors Van Meurs, K.P.; Angus, C.W.; Lavu, S.; Kung, H.F.; !1Czarnecki, S.K.; Moss, J.; Vaughan, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:3107-3111 !$#title Deduced amino acid sequence of bovine retinal G-o-alpha: !1similarities to other guanine nucleotide-binding proteins. !$#cross-references MUID:87204086; PMID:3106961 !$#accession A28011 !'##molecule_type mRNA !'##residues 1-262,'I',264-354 ##label VAN !'##cross-references GB:M16116; NID:g163067; PIDN:AAA30530.1; !1PID:g163068 REFERENCE A25948 !$#authors Angus, C.W.; Van Meurs, K.P.; Tsai, S.C.; Adamik, R.; !1Miedel, M.C.; Pan, Y.C.E.; Kung, H.F.; Moss, J.; Vaughan, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:5813-5816 !$#title Identification of the probable site of choleragen-catalyzed !1ADP-ribosylation in a G-o-alpha-like protein based on cDNA !1sequence. !$#cross-references MUID:86287343; PMID:3090546 !$#accession A25948 !'##molecule_type mRNA !'##residues 146-206 ##label ANG !'##cross-references GB:M14489; NID:g163107; PIDN:AAA30551.1; !1PID:g163108 REFERENCE A94131 !$#authors Michel, T.; Winslow, J.W.; Smith, J.A.; Seidman, J.G.; Neer, !1E.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:7663-7667 !$#title Molecular cloning and characterization of cDNA encoding the !1GTP-binding protein alpha-i and identification of a related !1protein, alpha-h. !$#cross-references MUID:87017009; PMID:3094012 !$#accession C25888 !'##molecule_type protein !'##residues 156-176;191-197;212-232,'X',234-235 ##label MIC COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. COMMENT The Go alpha chain, a substrate for ADP-ribosylation by !1cholera toxin and pertussis toxin, exists mainly in !1mammalian brain and neuronal tissues. CLASSIFICATION #superfamily GTP-binding regulatory protein Gs alpha chain KEYWORDS alternative splicing; blocked amino end; GTP binding; !1heterotrimer; lipoprotein; myristylation; nucleotide !1binding; P-loop; signal transduction; thiolester bond FEATURE !$2-354 #product GTP-binding regulatory protein Go alpha-1 !8chain #status predicted #label MAT\ !$40-47 #region nucleotide-binding motif A (P-loop)\ !$270-273 #region GTP-binding NKXD motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$46 #binding_site GTP (Lys) #status predicted\ !$179 #modified_site ADP-ribosylarginine (Arg) (by cholera !8toxin) #status predicted\ !$351 #modified_site ADP-ribosylcysteine (Cys) (by !8pertussis toxin) #status predicted SUMMARY #length 354 #molecular-weight 40066 #checksum 5338 SEQUENCE /// ENTRY RGRTO1 #type complete TITLE GTP-binding regulatory protein Go alpha chain, splice form alpha-1 [validated] - rat ALTERNATE_NAMES guanine nucleotide binding protein Go alpha-1 chain; heterotrimeric G-protein Go alpha-1 chain ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-Jan-2001 ACCESSIONS C40436; B27423; A24882; D35377; S12990 REFERENCE A40436 !$#authors Tsukamoto, T.; Toyama, R.; Itoh, H.; Kozasa, T.; Matsuoka, !1M.; Kaziro, Y. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:2974-2978 !$#title Structure of the human gene and two rat cDNAs encoding the !1alpha chain of GTP-binding regulatory protein G-o: two !1different mRNAs are generated by alternative splicing. !$#cross-references MUID:91195273; PMID:1901650 !$#accession C40436 !'##molecule_type mRNA !'##residues 1-354 ##label TSU REFERENCE A92614 !$#authors Jones, D.T.; Reed, R.R. !$#journal J. Biol. Chem. (1987) 262:14241-14249 !$#title Molecular cloning of five GTP-binding protein cDNA species !1from rat olfactory neuroepithelium. !$#cross-references MUID:88007678; PMID:2820999 !$#accession B27423 !'##molecule_type mRNA !'##residues 1-354 ##label JON !'##cross-references GB:M17526; NID:g203169; PIDN:AAA40826.1; !1PID:g203170 REFERENCE A94707 !$#authors Itoh, H.; Kozasa, T.; Nagata, S.; Nakamura, S.; Katada, T.; !1Ui, M.; Iwai, S.; Ohtsuka, E.; Kawasaki, H.; Suzuki, K.; !1Kaziro, Y. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:3776-3780 !$#title Molecular cloning and sequence determination of cDNAs for !1alpha subunits of the guanine nucleotide-binding proteins !1G-s, G-i, and G-o from rat brain. !$#cross-references MUID:86233317; PMID:3086867 !$#accession A24882 !'##molecule_type mRNA !'##residues 45-354 ##label ITO !'##cross-references GB:M12671; NID:g204443; PIDN:AAA41262.1; !1PID:g204444 REFERENCE A35377 !$#authors Linder, M.E.; Ewald, D.A.; Miller, R.J.; Gilman, A.G. !$#journal J. Biol. Chem. (1990) 265:8243-8251 !$#title Purification and characterization of G-oalpha and three !1types of G-ialpha after expression in Escherichia coli. !$#cross-references MUID:90243707; PMID:2159473 !$#accession D35377 !'##molecule_type protein !'##residues 22-35 ##label LIN REFERENCE S12990 !$#authors Hoshino, S.; Kikkawa, S.; Takahashi, K.; Itoh, H.; Kaziro, !1Y.; Kawasaki, H.; Suzuki, K.; Katada, T.; Ui, M. !$#journal FEBS Lett. (1990) 276:227-231 !$#title Identification of sites for alkylation by N-ethylmaleimide !1and pertussis toxin-catalyzed ADP-ribosylation on !1GTP-binding proteins. !$#cross-references MUID:91092425; PMID:2125009 !$#accession S12990 !'##molecule_type protein !'##residues 106-107,'X',109-113;350,'X',352-354 ##label HOS !'##note identified only as Go alpha chain; the sequenced regions are !1identical in the two splice forms COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. COMMENT The Go alpha chain, a substrate for ADP-ribosylation by !1cholera toxin and pertussis toxin, exists mainly in !1mammalian brain and neuronal tissues. CLASSIFICATION #superfamily GTP-binding regulatory protein Gs alpha chain KEYWORDS alternative splicing; blocked amino end; GTP binding; !1heterotrimer; lipoprotein; myristylation; nucleotide !1binding; P-loop; signal transduction; thiolester bond FEATURE !$2-354 #product GTP-binding regulatory protein Go alpha-1 !8chain #status predicted #label MAT\ !$40-47 #region nucleotide-binding motif A (P-loop)\ !$270-273 #region GTP-binding NKXD motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$46 #binding_site GTP (Lys) #status predicted\ !$179 #modified_site ADP-ribosylarginine (Arg) (by cholera !8toxin) #status predicted\ !$351 #modified_site ADP-ribosylcysteine (Cys) (by !8pertussis toxin) #status experimental SUMMARY #length 354 #molecular-weight 40068 #checksum 6903 SEQUENCE /// ENTRY RGMSO1 #type complete TITLE GTP-binding regulatory protein Go alpha chain, splice form alpha-1 - mouse ALTERNATE_NAMES guanine nucleotide binding protein Go alpha-1 chain; heterotrimeric G-protein Go alpha-1 chain ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-Jan-2001 ACCESSIONS A36038 REFERENCE A36038 !$#authors Strathmann, M.; Wilkie, T.M.; Simon, M.I. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:6477-6481 !$#title Alternative splicing produces transcripts encoding two forms !1of the alpha subunit of GTP-binding protein G-o. !$#cross-references MUID:90370808; PMID:1697681 !$#accession A36038 !'##molecule_type mRNA !'##residues 1-354 ##label STR !'##cross-references GB:M36777; NID:g193359; PIDN:AAA37645.1; !1PID:g193360 COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. COMMENT The Go alpha chain, a substrate for ADP-ribosylation by !1cholera toxin and pertussis toxin, exists mainly in !1mammalian brain and neuronal tissues. CLASSIFICATION #superfamily GTP-binding regulatory protein Gs alpha chain KEYWORDS alternative splicing; blocked amino end; GTP binding; !1heterotrimer; lipoprotein; myristylation; nucleotide !1binding; P-loop; signal transduction; thiolester bond FEATURE !$2-354 #product GTP-binding regulatory protein Go alpha-1 !8chain #status predicted #label MAT\ !$40-47 #region nucleotide-binding motif A (P-loop)\ !$270-273 #region GTP-binding NKXD motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$46 #binding_site GTP (Lys) #status predicted\ !$179 #modified_site ADP-ribosylarginine (Arg) (by cholera !8toxin) #status predicted\ !$351 #modified_site ADP-ribosylcysteine (Cys) (by !8pertussis toxin) #status predicted SUMMARY #length 354 #molecular-weight 40084 #checksum 8070 SEQUENCE /// ENTRY RGHYO1 #type complete TITLE GTP-binding regulatory protein Go alpha chain, splice form alpha-1 - golden hamster ALTERNATE_NAMES guanine nucleotide binding protein Go alpha-1 chain; heterotrimeric G-protein Go alpha-1 chain ORGANISM #formal_name Mesocricetus auratus #common_name golden hamster DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-Jan-2001 ACCESSIONS A42228 REFERENCE A42228 !$#authors Hsu, W.H.; Rudolph, U.; Sanford, J.; Bertrand, P.; Olate, !1J.; Nelson, C.; Moss, L.G.; Boyd III, A.E.; Codina, J.; !1Birnbaumer, L. !$#journal J. Biol. Chem. (1990) 265:11220-11226 !$#title Molecular cloning of a novel splice variant of the alpha !1subunit of the mammalian G-o protein. !$#cross-references MUID:90293067; PMID:2113531 !$#accession A42228 !'##molecule_type mRNA !'##residues 1-354 ##label HSU !'##cross-references GB:M33661; GB:J05476; NID:g191092; PIDN:AAA36987.1; !1PID:g304513 COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. COMMENT The Go alpha chain, a substrate for ADP-ribosylation by !1cholera toxin and pertussis toxin, exists mainly in !1mammalian brain and neuronal tissues. CLASSIFICATION #superfamily GTP-binding regulatory protein Gs alpha chain KEYWORDS alternative splicing; blocked amino end; GTP binding; !1heterotrimer; lipoprotein; myristylation; nucleotide !1binding; P-loop; signal transduction; thiolester bond FEATURE !$2-354 #product GTP-binding regulatory protein Go alpha-1 !8chain #status predicted #label MAT\ !$40-47 #region nucleotide-binding motif A (P-loop)\ !$270-273 #region GTP-binding NKXD motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$46 #binding_site GTP (Lys) #status predicted\ !$179 #modified_site ADP-ribosylarginine (Arg) (by cholera !8toxin) #status predicted\ !$351 #modified_site ADP-ribosylcysteine (Cys) (by !8pertussis toxin) #status predicted SUMMARY #length 354 #molecular-weight 40068 #checksum 6903 SEQUENCE /// ENTRY RGHUO2 #type complete TITLE GTP-binding regulatory protein Go alpha chain, splice form alpha-2 - human ALTERNATE_NAMES guanine nucleotide binding protein Go alpha-2 chain; heterotrimeric G-protein Go alpha-2 chain ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-Jan-2001 ACCESSIONS B40436 REFERENCE A40436 !$#authors Tsukamoto, T.; Toyama, R.; Itoh, H.; Kozasa, T.; Matsuoka, !1M.; Kaziro, Y. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:2974-2978 !$#title Structure of the human gene and two rat cDNAs encoding the !1alpha chain of GTP-binding regulatory protein G-o: two !1different mRNAs are generated by alternative splicing. !$#cross-references MUID:91195273; PMID:1901650 !$#accession B40436 !'##molecule_type DNA !'##residues 1-354 ##label TSU !'##cross-references GB:M60156 !'##note the authors translated the codon AAG for residue 17 as Leu COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. COMMENT The Go alpha chain, a substrate for ADP-ribosylation by !1cholera toxin and pertussis toxin, exists mainly in !1mammalian brain and neuronal tissues. GENETICS !$#gene GDB:GNAO1 !'##cross-references GDB:118803; OMIM:139311 !$#map_position 16q13-16q13 !$#introns 40/1; 54/2; 101/3; 155/2; 188/2; 241/3; 293/1 CLASSIFICATION #superfamily GTP-binding regulatory protein Gs alpha chain KEYWORDS alternative splicing; blocked amino end; GTP binding; !1heterotrimer; lipoprotein; myristylation; nucleotide !1binding; P-loop; signal transduction; thiolester bond FEATURE !$2-354 #product GTP-binding regulatory protein Go alpha-2 !8chain #status predicted #label MAT\ !$40-47 #region nucleotide-binding motif A (P-loop)\ !$270-273 #region GTP-binding NKXD motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$46 #binding_site GTP (Lys) #status predicted\ !$179 #modified_site ADP-ribosylarginine (Arg) (by cholera !8toxin) #status predicted\ !$351 #modified_site ADP-ribosylcysteine (Cys) (by !8pertussis toxin) #status predicted SUMMARY #length 354 #molecular-weight 40072 #checksum 6431 SEQUENCE /// ENTRY RGRTO2 #type complete TITLE GTP-binding regulatory protein Go alpha chain, splice form alpha-2 [validated] - rat ALTERNATE_NAMES guanine nucleotide binding protein Go alpha-2 chain; heterotrimeric G-protein Go alpha-2 chain ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-Jan-2001 ACCESSIONS D40436; S12990 REFERENCE A40436 !$#authors Tsukamoto, T.; Toyama, R.; Itoh, H.; Kozasa, T.; Matsuoka, !1M.; Kaziro, Y. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:2974-2978 !$#title Structure of the human gene and two rat cDNAs encoding the !1alpha chain of GTP-binding regulatory protein G-o: two !1different mRNAs are generated by alternative splicing. !$#cross-references MUID:91195273; PMID:1901650 !$#accession D40436 !'##molecule_type mRNA !'##residues 1-354 ##label TSU REFERENCE S12990 !$#authors Hoshino, S.; Kikkawa, S.; Takahashi, K.; Itoh, H.; Kaziro, !1Y.; Kawasaki, H.; Suzuki, K.; Katada, T.; Ui, M. !$#journal FEBS Lett. (1990) 276:227-231 !$#title Identification of sites for alkylation by N-ethylmaleimide !1and pertussis toxin-catalyzed ADP-ribosylation on !1GTP-binding proteins. !$#cross-references MUID:91092425; PMID:2125009 !$#accession S12990 !'##molecule_type protein !'##residues 106-107,'X',109-113;350,'X',352-354 ##label HOS !'##note identified only as Go alpha chain; the sequenced regions are !1identical in the two splice forms COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. COMMENT The Go alpha chain, a substrate for ADP-ribosylation by !1cholera toxin and pertussis toxin, exists mainly in !1mammalian brain and neuronal tissues. CLASSIFICATION #superfamily GTP-binding regulatory protein Gs alpha chain KEYWORDS alternative splicing; blocked amino end; GTP binding; !1heterotrimer; lipoprotein; myristylation; nucleotide !1binding; P-loop; signal transduction; thiolester bond FEATURE !$2-354 #product GTP-binding regulatory protein Go alpha-2 !8chain #status predicted #label MAT\ !$40-47 #region nucleotide-binding motif A (P-loop)\ !$270-273 #region GTP-binding NKXD motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$46 #binding_site GTP (Lys) #status predicted\ !$179 #modified_site ADP-ribosylarginine (Arg) (by cholera !8toxin) #status predicted\ !$351 #modified_site ADP-ribosylcysteine (Cys) (by !8pertussis toxin) #status experimental SUMMARY #length 354 #molecular-weight 40080 #checksum 7760 SEQUENCE /// ENTRY RGHYO2 #type complete TITLE GTP-binding regulatory protein Go alpha chain, splice form alpha-2 - golden hamster ALTERNATE_NAMES guanine nucleotide binding protein Go alpha-2 chain; heterotrimeric G-protein Go alpha-2 chain ORGANISM #formal_name Mesocricetus auratus #common_name golden hamster DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-Jan-2001 ACCESSIONS B42228 REFERENCE A42228 !$#authors Hsu, W.H.; Rudolph, U.; Sanford, J.; Bertrand, P.; Olate, !1J.; Nelson, C.; Moss, L.G.; Boyd III, A.E.; Codina, J.; !1Birnbaumer, L. !$#journal J. Biol. Chem. (1990) 265:11220-11226 !$#title Molecular cloning of a novel splice variant of the alpha !1subunit of the mammalian G-o protein. !$#cross-references MUID:90293067; PMID:2113531 !$#accession B42228 !'##molecule_type mRNA !'##residues 1-354 ##label HSU !'##cross-references GB:M33662; GB:J05476; NID:g191094; PIDN:AAA36988.1; !1PID:g304514 COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. COMMENT The Go alpha chain, a substrate for ADP-ribosylation by !1cholera toxin and pertussis toxin, exists mainly in !1mammalian brain and neuronal tissues. CLASSIFICATION #superfamily GTP-binding regulatory protein Gs alpha chain KEYWORDS alternative splicing; blocked amino end; GTP binding; !1heterotrimer; lipoprotein; myristylation; nucleotide !1binding; P-loop; signal transduction; thiolester bond FEATURE !$2-354 #product GTP-binding regulatory protein Go alpha-2 !8chain #status predicted #label MAT\ !$40-47 #region nucleotide-binding motif A (P-loop)\ !$270-273 #region GTP-binding NKXD motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$46 #binding_site GTP (Lys) #status predicted\ !$179 #modified_site ADP-ribosylarginine (Arg) (by cholera !8toxin) #status predicted\ !$351 #modified_site ADP-ribosylcysteine (Cys) (by !8pertussis toxin) #status predicted SUMMARY #length 354 #molecular-weight 40097 #checksum 7832 SEQUENCE /// ENTRY RGMSO2 #type complete TITLE GTP-binding regulatory protein Go alpha chain, splice form alpha-2 - mouse ALTERNATE_NAMES guanine nucleotide binding protein Go alpha-2 chain; heterotrimeric G-protein Go alpha-2 chain ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-Jan-2001 ACCESSIONS B36038 REFERENCE A36038 !$#authors Strathmann, M.; Wilkie, T.M.; Simon, M.I. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:6477-6481 !$#title Alternative splicing produces transcripts encoding two forms !1of the alpha subunit of GTP-binding protein G-o. !$#cross-references MUID:90370808; PMID:1697681 !$#accession B36038 !'##molecule_type mRNA !'##residues 1-354 ##label STR !'##cross-references GB:M36778; NID:g951087; PIDN:AAA74566.1; !1PID:g193362 COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. COMMENT The Go alpha chain, a substrate for ADP-ribosylation by !1cholera toxin and pertussis toxin, exists mainly in !1mammalian brain and neuronal tissues. CLASSIFICATION #superfamily GTP-binding regulatory protein Gs alpha chain KEYWORDS alternative splicing; blocked amino end; GTP binding; !1heterotrimer; lipoprotein; myristylation; nucleotide !1binding; P-loop; signal transduction; thiolester bond FEATURE !$2-354 #product GTP-binding regulatory protein Go alpha-2 !8chain #status predicted #label MAT\ !$40-47 #region nucleotide-binding motif A (P-loop)\ !$270-273 #region GTP-binding NKXD motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$46 #binding_site GTP (Lys) #status predicted\ !$179 #modified_site ADP-ribosylarginine (Arg) (by cholera !8toxin) #status predicted\ !$351 #modified_site ADP-ribosylcysteine (Cys) (by !8pertussis toxin) #status predicted SUMMARY #length 354 #molecular-weight 40036 #checksum 9174 SEQUENCE /// ENTRY RGXLOA #type complete TITLE GTP-binding regulatory protein Go alpha chain - African clawed frog ALTERNATE_NAMES guanine nucleotide binding protein Go alpha-2 chain; heterotrimeric G-protein Go alpha-2 chain ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-Jan-2001 ACCESSIONS S02785 REFERENCE S02785 !$#authors Olate, J.; Jorquera, H.; Purcell, P.; Codina, J.; !1Birnbaumer, L.; Allende, J.E. !$#journal FEBS Lett. (1989) 244:188-192 !$#title Molecular cloning and sequence determination of a cDNA !1coding for the alpha-subunit of a G(o)-type protein of !1Xenopus laevis oocytes. !$#cross-references MUID:89171257; PMID:2494063 !$#accession S02785 !'##molecule_type mRNA !'##residues 1-354 ##label OLA !'##cross-references EMBL:X14636 !'##note the authors translated the codon GTG for residue 13 as Leu, GAG !1for residue 52 as Gln, CGA for residue 82 as Ala, GTA for !1residues 124 and 125 as Leu, TCT for residue 197 as Phe, GAA !1for residue 290 as Leu, and CAG for residues 305 and 307 as !1Glu COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. COMMENT The Go alpha chain, a substrate for ADP-ribosylation by !1cholera toxin and pertussis toxin, exists mainly in !1mammalian brain and neuronal tissues. CLASSIFICATION #superfamily GTP-binding regulatory protein Gs alpha chain KEYWORDS blocked amino end; GTP binding; heterotrimer; lipoprotein; !1myristylation; nucleotide binding; P-loop; signal !1transduction; thiolester bond FEATURE !$2-354 #product GTP-binding regulatory protein Go alpha !8chain #status predicted #label MAT\ !$40-47 #region nucleotide-binding motif A (P-loop)\ !$270-273 #region GTP-binding NKXD motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$46 #binding_site GTP (Lys) #status predicted\ !$179 #modified_site ADP-ribosylarginine (Arg) (by cholera !8toxin) #status predicted\ !$351 #modified_site ADP-ribosylcysteine (Cys) (by !8pertussis toxin) #status predicted SUMMARY #length 354 #molecular-weight 40447 #checksum 942 SEQUENCE /// ENTRY RGFFO2 #type complete TITLE GTP-binding regulatory protein Go alpha chain homolog 2 - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 21-Jun-2002 ACCESSIONS B34304; JQ0155; B34305; B34306 REFERENCE A34304 !$#authors Yoon, J.; Shortridge, R.D.; Bloomquist, B.T.; Schneuwly, S.; !1Perdew, M.H.; Pak, W.L. !$#journal J. Biol. Chem. (1989) 264:18536-18543 !$#title Molecular characterization of Drosophila gene encoding G-o !1alpha subunit homolog. !$#cross-references MUID:90036955; PMID:2509462 !$#accession B34304 !'##molecule_type DNA !'##residues 1-354 ##label YOO !'##cross-references GB:M29602; GB:J05083; NID:g157551; PIDN:AAA28587.1; !1PID:g157552 REFERENCE JQ0155 !$#authors Schmidt, C.J.; Garen-Fazio, S.; Chow, Y.K.; Neer, E.J. !$#journal Cell Regul. (1989) 1:125-134 !$#title Neuronal expression of a newly identified Drosophila !1melanogaster G protein alpha-0 subunit. !$#cross-references MUID:92096479; PMID:2519611 !$#accession JQ0155 !'##molecule_type mRNA !'##residues 1-354 ##label SCH !'##cross-references GB:M86660; NID:g157520; PIDN:AAA28577.1; !1PID:g157521 REFERENCE A34305 !$#authors de Sousa, S.M.; Hoveland, L.L.; Yarfitz, S.; Hurley, J.B. !$#journal J. Biol. Chem. (1989) 264:18544-18551 !$#title The Drosophila G-o-alpha-like G protein gene produces !1multiple transcripts and is expressed in the nervous system !1and in ovaries. !$#cross-references MUID:90036956; PMID:2509463 !$#accession B34305 !'##molecule_type mRNA !'##residues 1-354 ##label DES !'##cross-references GB:M30151; NID:g157538; PIDN:AAA28584.1; !1PID:g157539 REFERENCE A34306 !$#authors Thambi, N.C.; Quan, F.; Wolfgang, W.J.; Spiegel, A.; Forte, !1M. !$#journal J. Biol. Chem. (1989) 264:18552-18560 !$#title Immunological and molecular characterization of !1G-oalpha-like proteins in the Drosophila central nervous !1system. !$#cross-references MUID:90036957; PMID:2509464 !$#accession B34306 !'##molecule_type mRNA !'##residues 1-354 ##label THA !'##cross-references GB:M29731; NID:g157530; PIDN:AAA28580.1; !1PID:g157531 GENETICS !$#gene FlyBase:G-o-alpha-47A !'##cross-references FlyBase:FBgn0001122 !$#introns 40/1; 101/3; 155/2 198/2; 241/3; 293/1 CLASSIFICATION #superfamily GTP-binding regulatory protein Gs alpha chain KEYWORDS alternative splicing; blocked amino end; GTP binding; !1lipoprotein; myristylation; nucleotide binding; P-loop; !1thiolester bond FEATURE !$2-354 #product GTP-binding regulatory protein Go alpha !8chain homolog 2 #status predicted #label MAT\ !$40-47 #region nucleotide-binding motif A (P-loop)\ !$270-273 #region GTP-binding NKXD motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 354 #molecular-weight 40537 #checksum 6958 SEQUENCE /// ENTRY RGFFO1 #type complete TITLE GTP-binding regulatory protein Go alpha chain homolog 1 - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 21-Jun-2002 ACCESSIONS A34304; A34305; A34306 REFERENCE A34304 !$#authors Yoon, J.; Shortridge, R.D.; Bloomquist, B.T.; Schneuwly, S.; !1Perdew, M.H.; Pak, W.L. !$#journal J. Biol. Chem. (1989) 264:18536-18543 !$#title Molecular characterization of Drosophila gene encoding G-o !1alpha subunit homolog. !$#cross-references MUID:90036955; PMID:2509462 !$#accession A34304 !'##molecule_type DNA !'##residues 1-354 ##label YOO !'##cross-references GB:M29602 REFERENCE A34305 !$#authors de Sousa, S.M.; Hoveland, L.L.; Yarfitz, S.; Hurley, J.B. !$#journal J. Biol. Chem. (1989) 264:18544-18551 !$#title The Drosophila G-o-alpha-like G protein gene produces !1multiple transcripts and is expressed in the nervous system !1and in ovaries. !$#cross-references MUID:90036956; PMID:2509463 !$#accession A34305 !'##molecule_type mRNA !'##residues 1-354 ##label DES !'##cross-references GB:M30152; NID:g157540; PIDN:AAA28585.1; !1PID:g157541 REFERENCE A34306 !$#authors Thambi, N.C.; Quan, F.; Wolfgang, W.J.; Spiegel, A.; Forte, !1M. !$#journal J. Biol. Chem. (1989) 264:18552-18560 !$#title Immunological and molecular characterization of !1G-oalpha-like proteins in the Drosophila central nervous !1system. !$#cross-references MUID:90036957; PMID:2509464 !$#accession A34306 !'##molecule_type mRNA !'##residues 1-354 ##label THA !'##cross-references GB:M29732 GENETICS !$#gene FlyBase:G-o-alpha-47A !'##cross-references FlyBase:FBgn0001122 !$#introns 40/1; 101/3; 155/2 198/2; 241/3; 293/1 CLASSIFICATION #superfamily GTP-binding regulatory protein Gs alpha chain KEYWORDS alternative splicing; blocked amino end; GTP binding; !1lipoprotein; myristylation; nucleotide binding; P-loop; !1thiolester bond FEATURE !$2-354 #product GTP-binding regulatory protein Go alpha !8chain homolog 1 #status predicted #label MAT\ !$40-47 #region nucleotide-binding motif A (P-loop)\ !$270-273 #region GTP-binding NKXD motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 354 #molecular-weight 40457 #checksum 6591 SEQUENCE /// ENTRY RGHUT1 #type complete TITLE GTP-binding regulatory protein Gt alpha-1 chain - human ALTERNATE_NAMES GTP-binding regulatory protein Tr alpha chain; guanine nucleotide binding protein Gt alpha-1 chain; heterotrimeric G-protein Gt alpha-1 chain; rod transducin alpha chain; transducin alpha-1 chain ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-Jan-2001 ACCESSIONS S22953; S04699; JQ0078 REFERENCE S22953 !$#authors Fong, S.L. !$#journal Nucleic Acids Res. (1992) 20:2865-2870 !$#title Characterization of the human rod transducin alpha-subunit !1gene. !$#cross-references MUID:92310988; PMID:1614872 !$#accession S22953 !'##molecule_type DNA !'##residues 1-350 ##label FON !'##cross-references EMBL:X63749; NID:g37049; PIDN:CAB37839.2; !1PID:g4467845 REFERENCE S04699 !$#authors van Dop, C.; Medynski, D.C.; Apone, L.M. !$#journal Nucleic Acids Res. (1989) 17:4887 !$#title Nucleotide sequence for a cDNA encoding the alpha subunit of !1retinal transducin (GNAT1) isolated from the human eye. !$#cross-references MUID:89315237; PMID:2748346 !$#accession S04699 !'##molecule_type mRNA !'##residues 1-203,'P',205-223,'T',225-273,'V',275-330,'C',332-350 !1##label VAN !'##cross-references EMBL:X15088; NID:g31864; PIDN:CAA33196.1; !1PID:g31865 REFERENCE JQ0078 !$#authors Lerea, C.L.; Bunt-Milam, A.H.; Hurley, J.B. !$#journal Neuron (1989) 3:367-376 !$#title Alpha transducin is present in blue-, green-, and !1red-sensitive cone photoreceptors in the human retina. !$#cross-references MUID:90380379; PMID:2534964 !$#accession JQ0078 !'##molecule_type mRNA !'##residues 1-203,'P',205-223,'T',225-350 ##label LER !'##note the authors translated the codon GAG for residue 342 as Gly COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. COMMENT Transducin, a specific G protein containing Gt alpha chain, !1is an amplifier and one of the transducers of a visual !1impulse that performs the coupling between rhodopsin and !1cGMP-phosphodiesterase. GENETICS !$#gene GDB:GNAT1 !'##cross-references GDB:119277; OMIM:139330 !$#map_position 3p21.3-3p21.2 !$#introns 35/1; 50/2; 97/3; 150/2; 193/2; 236/3; 288/1 CLASSIFICATION #superfamily GTP-binding regulatory protein Gs alpha chain KEYWORDS GTP binding; heterotrimer; nucleotide binding; P-loop; !1signal transduction FEATURE !$36-43 #region nucleotide-binding motif A (P-loop)\ !$265-268 #region GTP-binding NKXD motif\ !$42 #binding_site GTP (Lys) #status predicted\ !$174 #modified_site ADP-ribosylarginine (Arg) (by cholera !8toxin) #status predicted\ !$347 #modified_site ADP-ribosylcysteine (Cys) (by !8pertussis toxin) #status predicted SUMMARY #length 350 #molecular-weight 40040 #checksum 1614 SEQUENCE /// ENTRY RGBOT1 #type complete TITLE GTP-binding regulatory protein Gt alpha-1 chain - bovine ALTERNATE_NAMES GTP-binding regulatory protein Tr alpha chain; guanine nucleotide binding protein Gt alpha-1 chain; heterotrimeric G-protein Gt alpha-1 chain; rod transducin alpha chain; transducin alpha-1 chain ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-Jan-2001 ACCESSIONS A22244; A23155; A23156; JT0013; A61290; A61415 REFERENCE A94699 !$#authors Tanabe, T.; Nukada, T.; Nishikawa, Y.; Sugimoto, K.; Suzuki, !1H.; Takahashi, H.; Noda, M.; Haga, T.; Ichiyama, A.; !1Kangawa, K.; Minamino, N.; Matsuo, H.; Numa, S. !$#journal Nature (1985) 315:242-245 !$#title Primary structure of the alpha-subunit of transducin and its !1relationship to ras proteins. !$#cross-references MUID:85213821; PMID:3923359 !$#accession A22244 !'##molecule_type mRNA !'##residues 1-350 ##label TAN !'##cross-references GB:X02440; NID:g811; PIDN:CAA26285.1; PID:g812 REFERENCE A23155 !$#authors Medynski, D.C.; Sullivan, K.; Smith, D.; Van Dop, C.; Chang, !1F.H.; Fung, B.K.K.; Seeburg, P.H.; Bourne, H.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:4311-4315 !$#title Amino acid sequence of the alpha subunit of transducin !1deduced from the cDNA sequence. !$#cross-references MUID:85242674; PMID:2409555 !$#accession A23155 !'##molecule_type mRNA !'##residues 1-350 ##label MED !'##cross-references GB:K03253; NID:g163772; PIDN:AAA30787.1; !1PID:g163773 REFERENCE A23156 !$#authors Yatsunami, K.; Khorana, H.G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:4316-4320 !$#title GTPase of bovine rod outer segments: the amino acid sequence !1of the alpha subunit as derived from the cDNA sequence. !$#cross-references MUID:85242675; PMID:2989813 !$#accession A23156 !'##molecule_type mRNA !'##residues 1-350 ##label YAT !'##cross-references GB:K03254; NID:g163780; PIDN:AAA30791.1; !1PID:g163781 REFERENCE A90721 !$#authors Lipkin, V.M.; Obukhov, A.N.; Bogachuk, A.P.; Telezhinskaya, !1I.N.; Shemyakin, V.V. !$#journal Bioorg. Khim. (1985) 11:1481-1492 !$#title Isolation and characteristics of cyanogen bromide peptides !1of transducin alpha- and beta-subunits. !$#cross-references MUID:86130762; PMID:3867352 !$#accession JT0013 !'##molecule_type protein !'##residues 1,3-350 ##label LIP REFERENCE A61290 !$#authors Van Dop, C.; Tsubokawa, M.; Bourne, H.R.; Ramachandran, J. !$#journal J. Biol. Chem. (1984) 259:696-698 !$#title Amino acid sequence of retinal transducin at the site !1ADP-ribosylated by cholera toxin. !$#cross-references MUID:84111542; PMID:6582062 !$#accession A61290 !'##molecule_type protein !'##residues 173-176 ##label VAN REFERENCE A61415 !$#authors West Jr., R.E.; Moss, J.; Vaughan, M.; Liu, T.; Liu, T.Y. !$#journal J. Biol. Chem. (1985) 260:14428-14430 !$#title Pertussis toxin-catalyzed ADP-ribosylation of transducin. !1Cysteine 347 is the ADP-ribose acceptor site. !$#cross-references MUID:86033942; PMID:3863818 !$#accession A61415 !'##molecule_type protein !'##residues 342-350 ##label WES REFERENCE A49065 !$#authors Neubert, T.A.; Johnson, R.S.; Hurley, J.B.; Walsh, K.A. !$#journal J. Biol. Chem. (1992) 267:18274-18277 !$#title The rod transducin alpha subunit amino terminus is !1heterogeneously fatty acylated. !$#cross-references MUID:92406722; PMID:1326520 !$#contents annotation; myristylated glycine amino end with composition !1of saturated and unsaturated fatty acid components COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. COMMENT Transducin, a specific G protein containing Gt alpha chain, !1is an amplifier and one of the transducers of a visual !1impulse that performs the coupling between rhodopsin and !1cGMP-phosphodiesterase. CLASSIFICATION #superfamily GTP-binding regulatory protein Gs alpha chain KEYWORDS blocked amino end; GTP binding; heterotrimer; lipoprotein; !1myristylation; nucleotide binding; P-loop; signal !1transduction FEATURE !$36-43 #region nucleotide-binding motif A (P-loop)\ !$265-268 #region GTP-binding NKXD motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status experimental\ !$42 #binding_site GTP (Lys) #status predicted\ !$174 #modified_site ADP-ribosylarginine (Arg) (by cholera !8toxin) #status experimental\ !$347 #modified_site ADP-ribosylcysteine (Cys) (by !8pertussis toxin) #status experimental SUMMARY #length 350 #molecular-weight 39965 #checksum 2170 SEQUENCE /// ENTRY RGMST1 #type complete TITLE GTP-binding regulatory protein Gt alpha-1 chain - mouse ALTERNATE_NAMES GTP-binding regulatory protein Tr alpha chain; guanine nucleotide binding protein Gt alpha-1 chain; heterotrimeric G-protein Gt alpha-1 chain; rod transducin alpha chain; transducin alpha-1 chain ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-Jan-2001 ACCESSIONS A33352 REFERENCE A33352 !$#authors Raport, C.J.; Dere, B.; Hurley, J.B. !$#journal J. Biol. Chem. (1989) 264:7122-7128 !$#title Characterization of the mouse rod transducin alpha-subunit !1gene. !$#cross-references MUID:89214143; PMID:2708360 !$#accession A33352 !'##molecule_type DNA !'##residues 1-350 ##label RAP !'##cross-references GB:M22506 COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. COMMENT Transducin, a specific G protein containing Gt alpha chain, !1is an amplifier and one of the transducers of a visual !1impulse that performs the coupling between rhodopsin and !1cGMP-phosphodiesterase. GENETICS !$#introns 35/1; 50/2; 97/3; 150/2; 193/2; 236/3; 288/1 CLASSIFICATION #superfamily GTP-binding regulatory protein Gs alpha chain KEYWORDS GTP binding; heterotrimer; nucleotide binding; P-loop; !1signal transduction FEATURE !$36-43 #region nucleotide-binding motif A (P-loop)\ !$265-268 #region GTP-binding NKXD motif\ !$42 #binding_site GTP (Lys) #status predicted\ !$174 #modified_site ADP-ribosylarginine (Arg) (by cholera !8toxin) #status predicted\ !$347 #modified_site ADP-ribosylcysteine (Cys) (by !8pertussis toxin) #status predicted SUMMARY #length 350 #molecular-weight 39966 #checksum 2150 SEQUENCE /// ENTRY RGHUT2 #type complete TITLE GTP-binding regulatory protein Gt alpha-2 chain - human ALTERNATE_NAMES cone transducin alpha chain; GTP-binding regulatory protein Tc alpha chain; guanine nucleotide binding protein Gt alpha-2 chain; heterotrimeric G-protein Gt alpha-2 chain; transducin alpha-2 chain ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-Jan-2001 ACCESSIONS A47219; S18303; JQ0079 REFERENCE A47219 !$#authors Morris, T.A.; Fong, S.L. !$#journal Genomics (1993) 17:442-448 !$#title Characterization of the gene encoding human cone transducin !1alpha-subunit (GNAT2). !$#cross-references MUID:94010942; PMID:8406495 !$#accession A47219 !'##molecule_type DNA !'##residues 1-354 ##label MOR !'##cross-references GB:Z18859; NID:g312991; PIDN:CAA79310.1; !1PID:g732760 REFERENCE S18303 !$#authors Kubo, M.; Hirano, T.; Kakinuma, M. !$#journal FEBS Lett. (1991) 291:245-248 !$#title Molecular cloning and sequence analysis of cDNA and genomic !1DNA for the human cone transducin alpha subunit. !$#cross-references MUID:92038044; PMID:1936270 !$#accession S18303 !'##molecule_type DNA; mRNA !'##residues 1-354 ##label KUB1 !'##cross-references GB:D10384; GB:D90445; NID:g220096; PIDN:BAA01211.1; !1PID:g220098 REFERENCE JQ0078 !$#authors Lerea, C.L.; Bunt-Milam, A.H.; Hurley, J.B. !$#journal Neuron (1989) 3:367-376 !$#title Alpha transducin is present in blue-, green-, and !1red-sensitive cone photoreceptors in the human retina. !$#cross-references MUID:90380379; PMID:2534964 !$#accession JQ0079 !'##molecule_type mRNA !'##residues 1-105,'HV',108-354 ##label LER !'##note the authors translated the codon CAG for residues 24, 52, 58, !179, and 147 as Asn, CAA for residue 137 as Asn, and UGG for !1residue 211 as Thr !'##note DNA sequences of the genomic clones were also sequenced COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. COMMENT Transducin, a specific G protein containing Gt alpha chain, !1is an amplifier and one of the transducers of a visual !1impulse that performs the coupling between rhodopsin and !1cGMP-phosphodiesterase. GENETICS !$#gene GDB:GNAT2 !'##cross-references GDB:119278; OMIM:139340 !$#map_position 1p13-1p13 !$#introns 40/1; 54/2; 101/3; 154/2; 197/2; 240/3; 292/1 CLASSIFICATION #superfamily GTP-binding regulatory protein Gs alpha chain KEYWORDS GTP binding; heterotrimer; nucleotide binding; P-loop; !1signal transduction FEATURE !$40-47 #region nucleotide-binding motif A (P-loop)\ !$269-272 #region GTP-binding NKXD motif\ !$46 #binding_site GTP (Lys) #status predicted\ !$178 #modified_site ADP-ribosylarginine (Arg) (by cholera !8toxin) #status predicted\ !$351 #modified_site ADP-ribosylcysteine (Cys) (by !8pertussis toxin) #status predicted SUMMARY #length 354 #molecular-weight 40175 #checksum 2760 SEQUENCE /// ENTRY RGBOT2 #type complete TITLE GTP-binding regulatory protein Gt alpha-2 chain - bovine ALTERNATE_NAMES cone transducin alpha chain; GTP-binding regulatory protein Tc alpha chain; guanine nucleotide binding protein Gt alpha-2 chain; heterotrimeric G-protein Gt alpha-2 chain; transducin alpha-2 chain ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-Jan-2001 ACCESSIONS A94279 REFERENCE A94279 !$#authors Lochrie, M.A.; Hurley, J.B.; Simon, M.I. !$#journal Science (1985) 228:96-99 !$#title Sequence of the alpha subunit of photoreceptor G protein: !1homologies between transducin, ras, and elongation factors. !$#cross-references MUID:85142187; PMID:3856323 !$#accession A94279 !'##molecule_type mRNA !'##residues 1-354 ##label LOC !'##cross-references GB:M11116; NID:g163778; PIDN:AAA30790.1; !1PID:g163779 COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. COMMENT Transducin, a specific G protein containing Gt alpha chain, !1is an amplifier and one of the transducers of a visual !1impulse that performs the coupling between rhodopsin and !1cGMP-phosphodiesterase. CLASSIFICATION #superfamily GTP-binding regulatory protein Gs alpha chain KEYWORDS GTP binding; heterotrimer; nucleotide binding; P-loop; !1signal transduction FEATURE !$40-47 #region nucleotide-binding motif A (P-loop)\ !$269-272 #region GTP-binding NKXD motif\ !$46 #binding_site GTP (Lys) #status predicted\ !$178 #modified_site ADP-ribosylarginine (Arg) (by cholera !8toxin) #status predicted\ !$351 #modified_site ADP-ribosylcysteine (Cys) (by !8pertussis toxin) #status predicted SUMMARY #length 354 #molecular-weight 40143 #checksum 3842 SEQUENCE /// ENTRY RGTOOA #type complete TITLE GTP-binding regulatory protein Go alpha chain - tomato ALTERNATE_NAMES guanine nucleotide binding protein Go alpha chain; heterotrimeric G-protein Go alpha chain ORGANISM #formal_name Lycopersicon esculentum #common_name tomato DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-Jan-2001 ACCESSIONS JH0514 REFERENCE JH0514 !$#authors Ma, H.; Yanofsky, M.F.; Huang, H. !$#journal Gene (1991) 107:189-195 !$#title Isolation and sequence analysis of TGA1 cDNAs encoding a !1tomato G protein alpha subunit. !$#cross-references MUID:92084110; PMID:1748292 !$#accession JH0514 !'##molecule_type mRNA !'##residues 1-384 ##label MAH !'##cross-references GB:M74419; NID:g455375; PIDN:AAA34167.1; !1PID:g170450 !'##experimental_source pistil, strain VF36 COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. COMMENT The Go alpha chain, a substrate for ADP-ribosylation by !1cholera toxin and pertussis toxin, exists mainly in !1mammalian brain and neuronal tissues. GENETICS !$#gene TGA1 CLASSIFICATION #superfamily GTP-binding regulatory protein Gs alpha chain KEYWORDS GTP binding; heterotrimer; nucleotide binding; P-loop; !1signal transduction FEATURE !$46-53 #region nucleotide-binding motif A (P-loop)\ !$288-291 #region GTP-binding NKXD motif\ !$52 #binding_site GTP (Lys) #status predicted\ !$191 #modified_site ADP-ribosylarginine (Arg) (by cholera !8toxin) #status predicted SUMMARY #length 384 #molecular-weight 44903 #checksum 9133 SEQUENCE /// ENTRY RGMUOA #type complete TITLE GTP-binding regulatory protein Go alpha chain - Arabidopsis thaliana ALTERNATE_NAMES guanine nucleotide binding protein Go alpha chain; heterotrimeric G-protein Go alpha chain ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 02-Mar-2001 ACCESSIONS A35864; G84658 REFERENCE A35864 !$#authors Ma, H.; Yanofsky, M.F.; Meyerowitz, E.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:3821-3825 !$#title Molecular cloning and characterization of GPA1, a G protein !1alpha subunit gene from Arabidopsis thaliana. !$#cross-references MUID:90251649; PMID:2111018 !$#accession A35864 !'##molecule_type DNA !'##residues 1-383 ##label MAA !'##cross-references GB:M32887; NID:g166726; PIDN:AAA32805.1; !1PID:g166729 REFERENCE A84420 !$#authors Lin, X.; Kaul, S.; Rounsley, S.D.; Shea, T.P.; Benito, M.I.; !1Town, C.D.; Fujii, C.Y.; Mason, T.M.; Bowman, C.L.; !1Barnstead, M.E.; Feldblyum, T.V.; Buell, C.R.; Ketchum, !1K.A.; Lee, J.J.; Ronning, C.M.; Koo, H.; Moffat, K.S.; !1Cronin, L.A.; Shen, M.; VanAken, S.E.; Umayam, L.; Tallon, !1L.J.; Gill, J.E.; Adams, M.D.; Carrera, A.J.; Creasy, T.H.; !1Goodman, H.M.; Somerville, C.R.; Copenhaver, G.P.; Preuss, !1D.; Nierman, W.C.; White, O.; Eisen, J.A.; Salzberg, S.L.; !1Fraser, C.M.; Venter, J.C. !$#journal Nature (1999) 402:761-768 !$#title Sequence and analysis of chromosome 2 of the plant !1Arabidopsis thaliana. !$#cross-references MUID:20083487; PMID:10617197 !$#accession G84658 !'##status preliminary !'##molecule_type DNA !'##residues 1-383 ##label STO !'##cross-references GB:AE002093; NID:g3075388; PIDN:AAC14520.1; !1GSPDB:GN00139 COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. COMMENT The Go alpha chain, a substrate for ADP-ribosylation by !1cholera toxin and pertussis toxin, exists mainly in !1mammalian brain and neuronal tissues. GENETICS !$#gene At2g26300 !$#map_position 2 CLASSIFICATION #superfamily GTP-binding regulatory protein Gs alpha chain KEYWORDS GTP binding; heterotrimer; nucleotide binding; P-loop; !1signal transduction FEATURE !$45-52 #region nucleotide-binding motif A (P-loop)\ !$287-290 #region GTP-binding NKXD motif\ !$51 #binding_site GTP (Lys) #status predicted\ !$190 #modified_site ADP-ribosylarginine (Arg) (by cholera !8toxin) #status predicted SUMMARY #length 383 #molecular-weight 44546 #checksum 8194 SEQUENCE /// ENTRY RGMSQ #type complete TITLE GTP-binding regulatory protein Gq alpha chain - mouse ALTERNATE_NAMES guanine nucleotide binding protein Gq alpha chain; heterotrimeric G-protein Gq alpha chain ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-Jan-2001 ACCESSIONS A38414 REFERENCE A38414 !$#authors Strathmann, M.; Simon, M.I. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:9113-9117 !$#title G protein diversity: a distinct class of alpha subunits is !1present in vertebrates and invertebrates. !$#cross-references MUID:91067657; PMID:2123549 !$#accession A38414 !'##molecule_type mRNA !'##residues 1-359 ##label STR !'##cross-references GB:M55412; NID:g193501; PIDN:AAA63306.1; !1PID:g193502 COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. CLASSIFICATION #superfamily GTP-binding regulatory protein Gs alpha chain KEYWORDS GTP binding; heterotrimer; nucleotide binding; P-loop; !1signal transduction FEATURE !$46-53 #region nucleotide-binding motif A (P-loop)\ !$274-277 #region GTP-binding NKXD motif\ !$52 #binding_site GTP (Lys) #status predicted\ !$183 #modified_site ADP-ribosylarginine (Arg) (by cholera !8toxin) #status predicted SUMMARY #length 359 #molecular-weight 42153 #checksum 8443 SEQUENCE /// ENTRY RGMS11 #type complete TITLE GTP-binding regulatory protein G11 alpha chain - mouse ALTERNATE_NAMES guanine nucleotide binding protein G11 alpha chain; heterotrimeric G-protein G11 alpha chain ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-Jan-2001 ACCESSIONS B38414 REFERENCE A38414 !$#authors Strathmann, M.; Simon, M.I. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:9113-9117 !$#title G protein diversity: a distinct class of alpha subunits is !1present in vertebrates and invertebrates. !$#cross-references MUID:91067657; PMID:2123549 !$#accession B38414 !'##molecule_type mRNA !'##residues 1-359 ##label STR !'##cross-references GB:M55411; NID:g193499; PIDN:AAA63305.1; !1PID:g193500 COMMENT The G proteins are a family of guanine nucleotide-binding !1proteins that relay signals from cell surface receptors to !1intracellular effectors; they are composed of alpha, beta, !1and gamma chains. The beta and gamma chains, required for !1GTPase activity, appear to be common to all G proteins. The !1alpha chain contains the guanine nucleotide binding site and !1serves to activate phosphodiesterase; it is specific for !1each type of G protein. CLASSIFICATION #superfamily GTP-binding regulatory protein Gs alpha chain KEYWORDS GTP binding; heterotrimer; nucleotide binding; P-loop; !1signal transduction FEATURE !$46-53 #region nucleotide-binding motif A (P-loop)\ !$274-277 #region GTP-binding NKXD motif\ !$52 #binding_site GTP (Lys) #status predicted\ !$183 #modified_site ADP-ribosylarginine (Arg) (by cholera !8toxin) #status predicted SUMMARY #length 359 #molecular-weight 42024 #checksum 6384 SEQUENCE /// ENTRY B32804 #type complete TITLE GTP-binding protein obg - Bacillus subtilis ALTERNATE_NAMES spo0B-associated GTP-binding protein ORGANISM #formal_name Bacillus subtilis DATE 20-Oct-1989 #sequence_revision 06-Feb-1995 #text_change 19-Jan-2001 ACCESSIONS B32804; B21895; D69668 REFERENCE A32804 !$#authors Trach, K.; Hoch, J.A. !$#journal J. Bacteriol. (1989) 171:1362-1371 !$#title The Bacillus subtilis spo0B stage 0 sporulation operon !1encodes an essential GTP-binding protein. !$#cross-references MUID:89155435; PMID:2537815 !$#accession B32804 !'##molecule_type DNA !'##residues 1-428 ##label TRA !'##cross-references GB:M24537; NID:g341195; PIDN:AAA22505.1; !1PID:g508979 REFERENCE A94670 !$#authors Ferrari, F.A.; Trach, K.; Hoch, J.A. !$#journal J. Bacteriol. (1985) 161:556-562 !$#title Sequence analysis of the spo0B locus reveals a polycistronic !1transcription unit. !$#cross-references MUID:85104776; PMID:3918016 !$#accession B21895 !'##molecule_type DNA !'##residues 1-65 ##label FER !'##cross-references GB:K02666; GB:X02655; NID:g40178; PIDN:CAA26490.1; !1PID:g40180 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D69668 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-428 ##label KUN !'##cross-references GB:Z99118; GB:AL009126; NID:g2635200; !1PIDN:CAB14752.1; PID:g2635257 !'##experimental_source strain 168 COMMENT The function of this essential gene is not known. GENETICS !$#gene obg CLASSIFICATION #superfamily GTP-binding protein obg; translation elongation !1factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop; sporulation FEATURE !$159-285 #domain translation elongation factor Tu homology !8#label ETU\ !$165-172 #region nucleotide-binding motif A (P-loop)\ !$188-193 #region GTP-binding #status predicted\ !$212-215 #region GTP-binding #status predicted\ !$282-285 #region GTP-binding #status predicted\ !$308-312 #region GTP-binding #status predicted SUMMARY #length 428 #molecular-weight 47689 #checksum 8013 SEQUENCE /// ENTRY E70477 #type complete TITLE GTP-binding protein obg - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 24-Jul-1998 #sequence_revision 24-Jul-1998 #text_change 19-Jan-2001 ACCESSIONS E70477 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession E70477 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-343 ##label AQF !'##cross-references GB:AE000771; NID:g2984286; PIDN:AAC07816.1; !1PID:g2984292; GB:AE000657 !'##experimental_source strain VF5 GENETICS !$#gene obg CLASSIFICATION #superfamily GTP-binding protein obg; translation elongation !1factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop FEATURE !$161-287 #domain translation elongation factor Tu homology !8#label ETU\ !$167-174 #region nucleotide-binding motif A (P-loop)\ !$190-195 #region GTP-binding #status predicted\ !$214-217 #region GTP-binding #status predicted\ !$284-287 #region GTP-binding #status predicted\ !$311-315 #region GTP-binding #status predicted SUMMARY #length 343 #molecular-weight 37796 #checksum 6333 SEQUENCE /// ENTRY A65109 #type complete TITLE GTP-binding protein obg - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 24-Jul-1998 #sequence_revision 24-Jul-1998 #text_change 01-Mar-2002 ACCESSIONS A65109 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65109 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-390 ##label BLAT !'##cross-references GB:AE000399; GB:U00096; NID:g2367201; !1PIDN:AAC76215.1; PID:g1789574; UWGP:b3183 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yhbZ CLASSIFICATION #superfamily GTP-binding protein obg; translation elongation !1factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop FEATURE !$160-286 #domain translation elongation factor Tu homology !8#label ETU\ !$166-173 #region nucleotide-binding motif A (P-loop)\ !$189-194 #region GTP-binding #status predicted\ !$213-216 #region GTP-binding #status predicted\ !$283-286 #region GTP-binding #status predicted\ !$312-316 #region GTP-binding #status predicted SUMMARY #length 390 #molecular-weight 43286 #checksum 4231 SEQUENCE /// ENTRY E64099 #type complete TITLE GTP-binding protein obg - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES GTP-binding protein homolog HI0877 ORGANISM #formal_name Haemophilus influenzae DATE 24-Jul-1998 #sequence_revision 24-Jul-1998 #text_change 19-Jan-2001 ACCESSIONS E64099 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession E64099 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-390 ##label TIGR !'##cross-references GB:U32769; GB:L42023; NID:g1573888; !1PIDN:AAC22533.1; PID:g1573894; TIGR:HI0877 CLASSIFICATION #superfamily GTP-binding protein obg; translation elongation !1factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop FEATURE !$160-286 #domain translation elongation factor Tu homology !8#label ETU\ !$166-173 #region nucleotide-binding motif A (P-loop)\ !$189-194 #region GTP-binding #status predicted\ !$213-216 #region GTP-binding #status predicted\ !$283-286 #region GTP-binding #status predicted\ !$312-316 #region GTP-binding #status predicted SUMMARY #length 390 #molecular-weight 43376 #checksum 1062 SEQUENCE /// ENTRY S74797 #type complete TITLE GTP-binding protein obg - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein slr1090 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 24-Jul-1998 #sequence_revision 24-Jul-1998 #text_change 19-Jan-2001 ACCESSIONS S74797 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74797 !'##molecule_type DNA !'##residues 1-368 ##label KAN !'##cross-references EMBL:D90901; GB:AB001339; NID:g1651897; !1PIDN:BAA16948.1; PID:g1652022 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily GTP-binding protein obg; translation elongation !1factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop FEATURE !$160-283 #domain translation elongation factor Tu homology !8#label ETU\ !$166-173 #region nucleotide-binding motif A (P-loop)\ !$189-194 #region GTP-binding #status predicted\ !$213-216 #region GTP-binding #status predicted\ !$280-283 #region GTP-binding #status predicted\ !$307-311 #region GTP-binding #status predicted SUMMARY #length 368 #molecular-weight 39206 #checksum 9845 SEQUENCE /// ENTRY D70197 #type complete TITLE GTP-binding protein obg - Lyme disease spirochete ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 24-Jul-1998 #sequence_revision 24-Jul-1998 #text_change 19-Jan-2001 ACCESSIONS D70197 REFERENCE A70100 !$#authors Fraser, C.M.; Casjens, S.; Huang, W.M.; Sutton, G.G.; !1Clayton, R.; Lathigra, R.; White, O.; Ketchum, K.A.; Dodson, !1R.; Hickey, E.K.; Gwinn, M.; Dougherty, B.; Tomb, J.F.; !1Fleischmann, R.D.; Richardson, D.; Peterson, J.; Kerlavage, !1A.R.; Quackenbush, J.; Salzberg, S.; Hanson, M.; Vugt, R.V.; !1Palmer, N.; Adams, M.D.; Gocayne, J.; Weidman, J.; !1Utterback, T.; Watthey, L.; McDonald, L.; Artiach, P.; !1Bowman, C.; Garland, S.; Fujii, C.; Cotton, M.D.; Horst, K.; !1Roberts, K.; Hatch, B.; Smith, H.O.; Venter, J.C. !$#journal Nature (1997) 390:580-586 !$#title Genomic sequence of a Lyme disease spirochaete, Borrelia !1burgdorferi. !$#cross-references MUID:98065943; PMID:9403685 !$#accession D70197 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-328 ##label KLE !'##cross-references GB:AE001177; GB:AE000783; NID:g2688711; !1PIDN:AAC67127.1; PID:g2688719; TIGR:BB0781 !'##experimental_source strain B31 CLASSIFICATION #superfamily GTP-binding protein obg; translation elongation !1factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop FEATURE !$161-283 #domain translation elongation factor Tu homology !8#label ETU\ !$167-174 #region nucleotide-binding motif A (P-loop)\ !$190-195 #region GTP-binding #status predicted\ !$213-216 #region GTP-binding #status predicted\ !$280-283 #region GTP-binding #status predicted\ !$305-309 #region GTP-binding #status predicted SUMMARY #length 328 #molecular-weight 35735 #checksum 6473 SEQUENCE /// ENTRY G64557 #type complete TITLE GTP-binding protein obg - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 24-Jul-1998 #sequence_revision 24-Jul-1998 #text_change 19-Jan-2001 ACCESSIONS G64557 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession G64557 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-360 ##label TOM !'##cross-references GB:AE000548; GB:AE000511; NID:g2313391; !1PIDN:AAD07372.1; PID:g2313401; TIGR:HP0303 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily GTP-binding protein obg; translation elongation !1factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop FEATURE !$157-282 #domain translation elongation factor Tu homology !8#label ETU\ !$163-170 #region nucleotide-binding motif A (P-loop)\ !$186-191 #region GTP-binding #status predicted\ !$210-213 #region GTP-binding #status predicted\ !$279-282 #region GTP-binding #status predicted\ !$299-303 #region GTP-binding #status predicted SUMMARY #length 360 #molecular-weight 38707 #checksum 8958 SEQUENCE /// ENTRY E64242 #type complete TITLE GTP-binding protein obg - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 24-Jul-1998 #sequence_revision 24-Jul-1998 #text_change 19-Jan-2001 ACCESSIONS E64242 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession E64242 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-433 ##label TIGR !'##cross-references GB:U39723; GB:L43967; NID:g1046092; PID:g1046095; !1TIGR:MG384 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily GTP-binding protein obg; translation elongation !1factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop FEATURE !$160-285 #domain translation elongation factor Tu homology !8#label ETU\ !$166-173 #region nucleotide-binding motif A (P-loop)\ !$189-194 #region GTP-binding #status predicted\ !$212-215 #region GTP-binding #status predicted\ !$282-285 #region GTP-binding #status predicted\ !$309-313 #region GTP-binding #status predicted SUMMARY #length 433 #molecular-weight 48166 #checksum 2231 SEQUENCE /// ENTRY S73605 #type complete TITLE GTP-binding protein obg - Mycoplasma pneumoniae (strain ATCC 29342) ALTERNATE_NAMES hypothetical protein H03_orf433 ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 24-Jul-1998 #sequence_revision 24-Jul-1998 #text_change 19-Jan-2001 ACCESSIONS S73605 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73605 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-433 ##label HIM !'##cross-references EMBL:AE000027; GB:U00089; NID:g1673941; !1PIDN:AAB95927.1; PID:g1673950 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#gene obg !$#genetic_code SGC3 CLASSIFICATION #superfamily GTP-binding protein obg; translation elongation !1factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop FEATURE !$160-285 #domain translation elongation factor Tu homology !8#label ETU\ !$166-173 #region nucleotide-binding motif A (P-loop)\ !$189-194 #region GTP-binding #status predicted\ !$212-215 #region GTP-binding #status predicted\ !$282-285 #region GTP-binding #status predicted\ !$309-313 #region GTP-binding #status predicted SUMMARY #length 433 #molecular-weight 47950 #checksum 9915 SEQUENCE /// ENTRY A55014 #type complete TITLE GTP-binding protein DRG homolog - human ORGANISM #formal_name Homo sapiens #common_name man DATE 24-Jul-1998 #sequence_revision 24-Jul-1998 #text_change 19-Jan-2001 ACCESSIONS A55014 REFERENCE A55014 !$#authors Schenker, T.; Lach, C.; Kessler, B.; Calderara, S.; Trueb, !1B. !$#journal J. Biol. Chem. (1994) 269:25447-25453 !$#title A novel GTP-binding protein which is selectively repressed !1in SV40 transformed fibroblasts. !$#cross-references MUID:95014343; PMID:7929244 !$#accession A55014 !'##status preliminary !'##molecule_type mRNA !'##residues 1-364 ##label SCH !'##cross-references GB:X80754; NID:g577778; PIDN:CAA56730.1; !1PID:g577779 !'##experimental_source fibroblasts COMMENT This protein is expressed in normal fibroblasts but !1repressed in transformed cells. GENETICS !$#gene GDB:NEDD3; DRG1 !'##cross-references GDB:270141 CLASSIFICATION #superfamily GTP-binding protein DRG; translation elongation !1factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop FEATURE !$63-174 #domain translation elongation factor Tu homology !8#label ETU\ !$69-76 #region nucleotide-binding motif A (P-loop)\ !$92-97 #region GTP binding #status predicted\ !$115-118 #region GTP binding #status predicted\ !$246-249 #region GTP binding #status predicted\ !$337-341 #region GTP binding #status predicted SUMMARY #length 364 #molecular-weight 40746 #checksum 4795 SEQUENCE /// ENTRY JT0741 #type complete TITLE GTP-binding protein 1 - fission yeast (Schizosaccharomyces pombe) ORGANISM #formal_name Schizosaccharomyces pombe DATE 24-Jul-1998 #sequence_revision 24-Jul-1998 #text_change 19-Jan-2001 ACCESSIONS JT0741 REFERENCE JT0741 !$#authors Hudson, J.D.; Young, P.G. !$#journal Gene (1993) 125:191-193 !$#title Sequence of the Schizosaccharomyces pombe gtp1 gene and !1identification of a novel family of putative GTP-binding !1proteins. !$#cross-references MUID:93216121; PMID:8462872 !$#accession JT0741 !'##molecule_type DNA !'##residues 1-364 ##label HUD !'##cross-references GB:L00671; NID:g173395; PIDN:AAA35308.1; !1PID:g173396 GENETICS !$#gene gtp1 !$#introns 6/3; 29/3; 86/3 CLASSIFICATION #superfamily GTP-binding protein DRG; translation elongation !1factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop FEATURE !$63-183 #domain translation elongation factor Tu homology !8#label ETU\ !$69-76 #region nucleotide-binding motif A (P-loop)\ !$92-97 #region GTP binding #status predicted\ !$115-118 #region GTP binding #status predicted\ !$246-249 #region GTP binding #status predicted\ !$337-341 #region GTP binding #status predicted SUMMARY #length 364 #molecular-weight 40939 #checksum 1829 SEQUENCE /// ENTRY S64487 #type complete TITLE GTP-binding protein DRG homolog - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein G7112; hypothetical protein YGR173w ORGANISM #formal_name Saccharomyces cerevisiae DATE 24-Jul-1998 #sequence_revision 24-Jul-1998 #text_change 19-Apr-2002 ACCESSIONS S64487 REFERENCE S64003 !$#authors Hebling, U.; Hofmann, B.; Delius, H. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64487 !'##molecule_type DNA !'##residues 1-368 ##label HEB !'##cross-references EMBL:Z72958; NID:g1323305; PIDN:CAA97199.1; !1PID:g1323306; GSPDB:GN00007; MIPS:YGR173w !'##experimental_source strain S288C GENETICS !$#gene MIPS:YGR173w !'##cross-references SGD:S0003405 !$#map_position 7R CLASSIFICATION #superfamily GTP-binding protein DRG; translation elongation !1factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop FEATURE !$64-183 #domain translation elongation factor Tu homology !8#label ETU\ !$70-77 #region nucleotide-binding motif A (P-loop)\ !$93-98 #region GTP binding #status predicted\ !$116-119 #region GTP binding #status predicted\ !$250-253 #region GTP binding #status predicted\ !$341-345 #region GTP binding #status predicted SUMMARY #length 368 #molecular-weight 41006 #checksum 829 SEQUENCE /// ENTRY JC1349 #type complete TITLE GTP-binding protein DRG [validated] - mouse ALTERNATE_NAMES developmentally-regulated GTP-binding protein ORGANISM #formal_name Mus musculus #common_name house mouse DATE 24-Jul-1998 #sequence_revision 24-Jul-1998 #text_change 19-Jan-2001 ACCESSIONS JC1349 REFERENCE JC1349 !$#authors Sazuka, T.; Tomooka, Y.; Ikawa, Y.; Noda, M.; Kumar, S. !$#journal Biochem. Biophys. Res. Commun. (1992) 189:363-370 !$#title DRG: a novel developmentally regulated GTP-binding protein. !$#cross-references MUID:93080583; PMID:1449490 !$#accession JC1349 !'##molecule_type mRNA !'##residues 1-367 ##label SAZ !'##cross-references GB:D10715; NID:g220506 !'##experimental_source embryonic brain !'##note the authors translated the codon GAG for residue 229 as Asp GENETICS !$#gene drg; NEDD-3 FUNCTION !$#description protein binds GTP in vitro [validated, MUID:93080583] CLASSIFICATION #superfamily GTP-binding protein DRG; translation elongation !1factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop FEATURE !$65-185 #domain translation elongation factor Tu homology !8#label ETU\ !$71-78 #region nucleotide-binding motif A (P-loop)\ !$94-99 #region GTP binding #status predicted\ !$117-120 #region GTP binding #status predicted\ !$248-251 #region GTP binding #status predicted\ !$340-344 #region GTP binding #status predicted SUMMARY #length 367 #molecular-weight 40526 #checksum 4360 SEQUENCE /// ENTRY I51426 #type complete TITLE GTP-binding protein DRG - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 24-Jul-1998 #sequence_revision 24-Jul-1998 #text_change 19-Jan-2001 ACCESSIONS I51426 REFERENCE I51426 !$#authors Kumar, S.; Iwao, M.; Yamagishi, T.; Noda, M.; Asashima, M. !$#journal Int. J. Dev. Biol. (1993) 37:539-546 !$#title Expression of GTP-binding protein gene drg during Xenopus !1laevis development. !$#cross-references MUID:94235417; PMID:8179998 !$#accession I51426 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-367 ##label KUM !'##cross-references GB:D13865; NID:g433421; PIDN:BAA02978.1; !1PID:g433422 GENETICS !$#gene Xdrg CLASSIFICATION #superfamily GTP-binding protein DRG; translation elongation !1factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop FEATURE !$65-185 #domain translation elongation factor Tu homology !8#label ETU\ !$71-78 #region nucleotide-binding motif A (P-loop)\ !$94-99 #region GTP binding #status predicted\ !$117-120 #region GTP binding #status predicted\ !$248-251 #region GTP binding #status predicted\ !$340-344 #region GTP binding #status predicted SUMMARY #length 367 #molecular-weight 40414 #checksum 3356 SEQUENCE /// ENTRY S42582 #type complete TITLE GTP-binding protein 128up - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 24-Jul-1998 #sequence_revision 24-Jul-1998 #text_change 19-Jan-2001 ACCESSIONS S42582; S33467 REFERENCE S42582 !$#authors Sommer, K.A.; Petersen, G.; Bautz, E.K.F. !$#journal Mol. Gen. Genet. (1994) 242:391-398 !$#title The gene upstream of DmRP128 codes for a novel GTP-binding !1protein of Drosophila melanogaster. !$#cross-references MUID:94166747; PMID:8121394 !$#accession S42582 !'##status preliminary !'##molecule_type DNA !'##residues 1-368 ##label SOM !'##cross-references EMBL:X71866; NID:g311342; PIDN:CAA50701.1; !1PID:g311343 !'##note submitted to the EMBL Data Library, May 1993 GENETICS !$#gene FlyBase:128up !'##cross-references FlyBase:FBgn0010339 !$#introns 14/3; 55/1; 335/2 CLASSIFICATION #superfamily GTP-binding protein DRG; translation elongation !1factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop FEATURE !$65-184 #domain translation elongation factor Tu homology !8#label ETU\ !$71-78 #region nucleotide-binding motif A (P-loop)\ !$94-99 #region GTP binding #status predicted\ !$117-120 #region GTP binding #status predicted\ !$248-251 #region GTP binding #status predicted\ !$340-344 #region GTP binding #status predicted SUMMARY #length 368 #molecular-weight 41129 #checksum 6891 SEQUENCE /// ENTRY S51983 #type complete TITLE FUN11 protein - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YAL036c ORGANISM #formal_name Saccharomyces cerevisiae DATE 24-Jul-1998 #sequence_revision 24-Jul-1998 #text_change 19-Apr-2002 ACCESSIONS S51983 REFERENCE S51956 !$#authors Bussey, H.; Kaback, D.B.; Zhong, W.; Vo, D.T.; Clark, M.W.; !1Fortin, N.; Hall, J.; Ouellette, B.F.F.; Keng, T.; Barton, !1A.B.; Su, Y.; Davies, C.K.; Storms, R.K. !$#submission submitted to the EMBL Data Library, August 1994 !$#description The sequence of chromosome 1 of Saccharomyces cerevisiae. !$#accession S51983 !'##molecule_type DNA !'##residues 1-369 ##label BUS !'##cross-references EMBL:U12980; NID:g1326053; PIDN:AAC04995.1; !1PID:g595548; GSPDB:GN00001; MIPS:YAL036c GENETICS !$#gene SGD:FUN11; FUN11; MIPS:YAL036c !'##cross-references SGD:S0000034 !$#map_position 1L CLASSIFICATION #superfamily GTP-binding protein DRG; translation elongation !1factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop FEATURE !$66-186 #domain translation elongation factor Tu homology !8#label ETU\ !$72-79 #region nucleotide-binding motif A (P-loop)\ !$95-100 #region GTP binding #status predicted\ !$118-121 #region GTP binding #status predicted\ !$250-253 #region GTP binding #status predicted\ !$342-346 #region GTP binding #status predicted SUMMARY #length 369 #molecular-weight 40701 #checksum 1350 SEQUENCE /// ENTRY B69518 #type complete TITLE GTP-binding protein DRG homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 24-Jul-1998 #sequence_revision 24-Jul-1998 #text_change 19-Jan-2001 ACCESSIONS B69518 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession B69518 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-355 ##label KLE !'##cross-references GB:AE000956; GB:AE000782; NID:g2689279; !1PIDN:AAB89108.1; PID:g2648391; TIGR:AF2146 CLASSIFICATION #superfamily GTP-binding protein DRG; translation elongation !1factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop FEATURE !$64-183 #domain translation elongation factor Tu homology !8#label ETU\ !$70-77 #region nucleotide-binding motif A (P-loop)\ !$93-98 #region GTP binding #status predicted\ !$116-119 #region GTP binding #status predicted\ !$245-248 #region GTP binding #status predicted\ !$329-333 #region GTP binding #status predicted SUMMARY #length 355 #molecular-weight 39534 #checksum 8330 SEQUENCE /// ENTRY E64465 #type complete TITLE GTP-binding protein DRG homolog - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 24-Jul-1998 #sequence_revision 24-Jul-1998 #text_change 19-Jan-2001 ACCESSIONS E64465 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession E64465 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-391 ##label BUL !'##cross-references GB:U67573; GB:L77117; NID:g2826395; !1PIDN:AAB99336.1; PID:g1591967; TIGR:MJ1326 GENETICS !$#map_position FOR1275899-1277074 CLASSIFICATION #superfamily GTP-binding protein DRG; translation elongation !1factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop FEATURE !$85-204 #domain translation elongation factor Tu homology !8#label ETU\ !$91-98 #region nucleotide-binding motif A (P-loop)\ !$114-119 #region GTP binding #status predicted\ !$137-140 #region GTP binding #status predicted\ !$267-270 #region GTP binding #status predicted\ !$363-367 #region GTP binding #status predicted SUMMARY #length 391 #molecular-weight 43648 #checksum 5502 SEQUENCE /// ENTRY F69083 #type complete TITLE GTP-binding protein DRG homolog - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 24-Jul-1998 #sequence_revision 24-Jul-1998 #text_change 19-Jan-2001 ACCESSIONS F69083 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession F69083 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-380 ##label MTH !'##cross-references GB:AE000921; GB:AE000666; NID:g2622744; !1PIDN:AAB86094.1; PID:g2622747 !'##experimental_source strain Delta H GENETICS !$#gene MTH1621 CLASSIFICATION #superfamily GTP-binding protein DRG; translation elongation !1factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop FEATURE !$78-197 #domain translation elongation factor Tu homology !8#label ETU\ !$84-91 #region nucleotide-binding motif A (P-loop)\ !$107-112 #region GTP binding #status predicted\ !$130-133 #region GTP binding #status predicted\ !$260-263 #region GTP binding #status predicted\ !$352-356 #region GTP binding #status predicted SUMMARY #length 380 #molecular-weight 42896 #checksum 6626 SEQUENCE /// ENTRY QQHS4C #type complete TITLE GTP-binding protein DRG homolog - Halobacterium salinarum (strain cutirubrum) ORGANISM #formal_name Halobacterium salinarum #variety strain cutirubrum DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 19-Jan-2001 ACCESSIONS S04116 REFERENCE S04116 !$#authors Shimmin, L.C.; Dennis, P.P. !$#journal EMBO J. (1989) 8:1225-1235 !$#title Characterization of the L11, L1, L10 and L12 equivalent !1ribosomal protein gene cluster of the halophilic !1archaebacterium Halobacterium cutirubrum. !$#cross-references MUID:89305527; PMID:2743981 !$#accession S04116 !'##molecule_type DNA !'##residues 1-370 ##label SHI !'##cross-references EMBL:X15078; NID:g43449; PIDN:CAA33176.1; !1PID:g43450 !'##note the authors translated the codon AAG for residue 33 as Asn, CTC !1for residue 34 as Val, GGC for residue 342 as Arg and CCG !1for residue 343 as Arg !'##note the source is designated as Halobacterium cutirubrum CLASSIFICATION #superfamily GTP-binding protein DRG; translation elongation !1factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop FEATURE !$62-181 #domain translation elongation factor Tu homology !8#label ETU\ !$68-75 #region nucleotide-binding motif A (P-loop)\ !$91-96 #region GTP binding #status predicted\ !$114-117 #region GTP binding #status predicted\ !$243-246 #region GTP binding #status predicted\ !$342-346 #region GTP binding #status predicted SUMMARY #length 370 #molecular-weight 40329 #checksum 8480 SEQUENCE /// ENTRY A44842 #type complete TITLE cGMP-gated ion channel protein - human ALTERNATE_NAMES rod photoreceptor cGMP-gated channel ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A44842 REFERENCE A44842 !$#authors Dhallan, R.S.; Macke, J.P.; Eddy, R.L.; Shows, T.B.; Reed, !1R.R.; Yau, K.W.; Nathans, J. !$#journal J. Neurosci. (1992) 12:3248-3256 !$#title Human rod photoreceptor cGMP-gated channel: amino acid !1sequence, gene structure, and functional expression. !$#cross-references MUID:92356211; PMID:1379636 !$#accession A44842 !'##molecule_type mRNA !'##residues 1-686 ##label DHA !'##cross-references GB:S42457; NID:g252853; PIDN:AAB22778.1; !1PID:g252854 !'##experimental_source retina !'##note sequence extracted from NCBI backbone (NCBIN:110250, !1NCBIP:110251) !'##note intron positions were determined from genomic sequence GENETICS !$#gene GDB:CNCG1; CNCG !'##cross-references GDB:127557; OMIM:123825 !$#map_position 4p14-4q13 !$#introns 36/2; 75/2; 95/2; 110/2; 146/2; 182/2; 218/2 CLASSIFICATION #superfamily cyclic nucleotide-gated channel; cAMP receptor !1protein cyclic nucleotide-binding domain homology KEYWORDS cGMP binding; eye; ion channel; ion transport; retina; !1transmembrane protein FEATURE !$475-599 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP SUMMARY #length 686 #molecular-weight 79124 #checksum 1768 SEQUENCE /// ENTRY S07103 #type complete TITLE cGMP-gated ion channel protein - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S07103 REFERENCE S07103 !$#authors Kaupp, U.B.; Niidome, T.; Tanabe, T.; Terada, S.; Boenigk, !1W.; Stuehmer, W.; Cook, N.J.; Kangawa, K.; Matsuo, H.; !1Hirose, T.; Miyata, T.; Numa, S. !$#journal Nature (1989) 342:762-766 !$#title Primary structure and functional expression from !1complementary DNA of the rod photoreceptor cyclic GMP-gated !1channel. !$#cross-references MUID:90098076; PMID:2481236 !$#accession S07103 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-690 ##label KAU !'##cross-references GB:X51604; NID:g203; PIDN:CAA35947.1; PID:g204 !'##note part of this sequence was confirmed by protein sequencing CLASSIFICATION #superfamily cyclic nucleotide-gated channel; cAMP receptor !1protein cyclic nucleotide-binding domain homology KEYWORDS cGMP binding; eye; ion channel; ion transport; retina; !1transmembrane protein FEATURE !$477-601 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP SUMMARY #length 690 #molecular-weight 79602 #checksum 3315 SEQUENCE /// ENTRY JH0560 #type complete TITLE cyclic nucleotide-gated channel - channel catfish ORGANISM #formal_name Ictalurus punctatus #common_name channel catfish DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JH0560 REFERENCE JH0560 !$#authors Goulding, E.H.; Ngai, J.; Kramer, R.H.; Colicos, S.; Axel, !1R.; Siegelbaum, S.A.; Chess, A. !$#journal Neuron (1992) 8:45-58 !$#title Molecular cloning and single-channel properties of the !1cyclic nucleotide-gated channel from catfish olfactory !1neurons. !$#cross-references MUID:92110008; PMID:1370374 !$#accession JH0560 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-682 ##label GOU !'##cross-references GB:M83111 !'##experimental_source olfactory epithelium COMMENT This cyclic nucleotide-gated channel is activated equally !1well by both cAMP and cGMP. CLASSIFICATION #superfamily cyclic nucleotide-gated channel; cAMP receptor !1protein cyclic nucleotide-binding domain homology KEYWORDS cAMP binding; cGMP binding; ion channel; ion transport; !1olfaction; transmembrane protein FEATURE !$137-157 #domain transmembrane #status predicted #label TS1\ !$173-193 #domain transmembrane #status predicted #label TS2\ !$217-236 #domain transmembrane #status predicted #label TS3\ !$241-261 #domain transmembrane #status predicted #label TS4\ !$277-297 #domain transmembrane #status predicted #label TS5\ !$319-337 #domain transmembrane #status predicted #label TH5\ !$350-370 #domain transmembrane #status predicted #label TS6\ !$447-571 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP SUMMARY #length 682 #molecular-weight 78019 #checksum 5516 SEQUENCE /// ENTRY S04987 #type complete TITLE SITS-binding protein sp105 - Pacific electric ray ORGANISM #formal_name Torpedo californica #common_name Pacific electric ray DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 22-Jun-1999 ACCESSIONS S04987; S30070 REFERENCE S04987 !$#authors Jentsch, T.J.; Garcia, A.M.; Lodish, H.F. !$#journal Biochem. J. (1989) 261:155-166 !$#title Primary structure of a novel !14-acetamido-4'-isothiocyanostilbene-2,2'-disulphonic acid !1(SITS)-binding membrane protein highly expressed in Torpedo !1californica electroplax. !$#cross-references MUID:89374082; PMID:2775201 !$#accession S04987 !'##molecule_type mRNA !'##residues 1-697 ##label JEN1 !'##cross-references EMBL:X16078; NID:g64403; PIDN:CAA34209.1; !1PID:g64404 !$#accession S30070 !'##molecule_type protein !'##residues 2-11;435-449,'X',451-452,'X',454-459;634-649 ##label JEN2 CLASSIFICATION #superfamily SITS-binding protein sp105 KEYWORDS disulfide bond; glycoprotein; homodimer; transmembrane !1protein FEATURE !$2-697 #product SITS-binding protein #status experimental !8#label MAT\ !$30-50 #domain transmembrane #status predicted #label TM1\ !$503-521 #domain transmembrane #status predicted #label TM2\ !$542-562 #domain transmembrane #status predicted #label TM3\ !$25,112,134,162,386, !$405,470,568 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 697 #molecular-weight 78456 #checksum 6575 SEQUENCE /// ENTRY A35422 #type complete TITLE phosducin, retinal - human ALTERNATE_NAMES MEKA protein ORGANISM #formal_name Homo sapiens #common_name man DATE 18-Jan-1991 #sequence_revision 14-Jul-1994 #text_change 22-Jun-1999 ACCESSIONS A35422; JH0214 REFERENCE A35422 !$#authors Watanabe, Y.; Kawasaki, K.; Miki, N.; Kuo, C.H. !$#journal Biochem. Biophys. Res. Commun. (1990) 170:951-956 !$#title Isolation and analysis of the human MEKA gene encoding a !1retina-specific protein. !$#cross-references MUID:90343823; PMID:2383274 !$#accession A35422 !'##molecule_type DNA !'##residues 1-246 ##label WAT !'##cross-references GB:M60720; GB:M38058; GB:M38059; NID:g187515; !1PIDN:AAA36210.1; PID:g187517 REFERENCE JH0214 !$#authors Abe, T.; Nakabayashi, H.; Tamada, H.; Takagi, T.; Sakuragi, !1S.; Yamaki, K.; Shinohara, T. !$#journal Gene (1990) 91:209-215 !$#title Analysis of the human, bovine and rat 33-kDa proteins and !1cDNA in retina and pineal gland. !$#cross-references MUID:91007277; PMID:2210381 !$#accession JH0214 !'##molecule_type mRNA !'##residues 1-139,'I',141-246 ##label ABE !'##cross-references GB:M33478; NID:g177186; PIDN:AAA35486.1; !1PID:g177187 COMMENT This protein is a principal protein of retinal photoreceptor !1that modulates the phototransduction cascade by interacting !1with transducin. GENETICS !$#gene GDB:PDC; MEKA; phosducin !'##cross-references GDB:125268; OMIM:171490 !$#map_position 1q25-1q32.1 CLASSIFICATION #superfamily phosducin KEYWORDS glycoprotein; phosphoprotein; photoreceptor; retina FEATURE !$8,58 #binding_site phosphate (Ser) (covalent) (by casein !8kinase II) #status predicted\ !$45,69 #binding_site phosphate (Ser) (covalent) (by protein !8kinase C) #status predicted\ !$73 #binding_site phosphate (Ser) (covalent) (by protein !8kinase A) #status predicted\ !$152 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$238 #binding_site phosphate (Thr) (covalent) (by casein !8kinase II) #status predicted SUMMARY #length 246 #molecular-weight 28246 #checksum 3692 SEQUENCE /// ENTRY JC2018 #type complete TITLE phosducin - mouse ALTERNATE_NAMES G-protein-inhibitor ORGANISM #formal_name Mus musculus #common_name house mouse DATE 14-Jul-1994 #sequence_revision 14-Jul-1994 #text_change 26-Feb-1999 ACCESSIONS JC2018 REFERENCE JC2018 !$#authors Abe, T.; Kikuchi, T.; Chang, T.; Shinohara, T. !$#journal Gene (1993) 133:179-186 !$#title The sequence of the mouse phosducin-encoding gene and its !15'-flanking region. !$#cross-references MUID:94040808; PMID:8224906 !$#accession JC2018 !'##molecule_type DNA !'##residues 1-244 ##label ABE COMMENT This protein is a principal protein of retinal photoreceptor !1that modulates the phototransduction cascade by interacting !1with transducin. CLASSIFICATION #superfamily phosducin KEYWORDS glycoprotein; phosphoprotein; photoreceptor; retina FEATURE !$8,58 #binding_site phosphate (Ser) (covalent) (by casein !8kinase II) #status predicted\ !$45,67 #binding_site phosphate (Ser) (covalent) (by protein !8kinase C) #status predicted\ !$71 #binding_site phosphate (Ser) (covalent) (by protein !8kinase A) #status predicted\ !$150 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$236 #binding_site phosphate (Thr) (covalent) (by casein !8kinase II) #status predicted SUMMARY #length 244 #molecular-weight 28016 #checksum 2566 SEQUENCE /// ENTRY JH0216 #type complete TITLE phosducin, retinal - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 21-Nov-1993 #sequence_revision 14-Jul-1994 #text_change 22-Jun-1999 ACCESSIONS JH0216 REFERENCE JH0214 !$#authors Abe, T.; Nakabayashi, H.; Tamada, H.; Takagi, T.; Sakuragi, !1S.; Yamaki, K.; Shinohara, T. !$#journal Gene (1990) 91:209-215 !$#title Analysis of the human, bovine and rat 33-kDa proteins and !1cDNA in retina and pineal gland. !$#cross-references MUID:91007277; PMID:2210381 !$#accession JH0216 !'##molecule_type mRNA !'##residues 1-246 ##label ABE !'##cross-references GB:M33528; NID:g202526; PIDN:AAA40604.1; !1PID:g202527 CLASSIFICATION #superfamily phosducin KEYWORDS glycoprotein; phosphoprotein; photoreceptor; retina FEATURE !$8,58 #binding_site phosphate (Ser) (covalent) (by casein !8kinase II) #status predicted\ !$45,69 #binding_site phosphate (Ser) (covalent) (by protein !8kinase C) #status predicted\ !$73 #binding_site phosphate (Ser) (covalent) (by protein !8kinase A) #status experimental\ !$152 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$238 #binding_site phosphate (Thr) (covalent) (by casein !8kinase II) #status predicted SUMMARY #length 246 #molecular-weight 28143 #checksum 3101 SEQUENCE /// ENTRY A39903 #type complete TITLE phosducin, pineal gland - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 20-Mar-1992 #sequence_revision 14-Jul-1994 #text_change 22-Jun-1999 ACCESSIONS A39903; JH0217 REFERENCE A39903 !$#authors Craft, C.M.; Lolley, R.N.; Seldin, M.F.; Lee, R.H. !$#journal Genomics (1991) 10:400-409 !$#title Rat pineal gland phosducin: cDNA isolation, nucleotide !1sequence, and chromosomal assignment in the mouse. !$#cross-references MUID:91301696; PMID:2071146 !$#accession A39903 !'##molecule_type mRNA !'##residues 1-246 ##label CRA !'##cross-references GB:M60738; GB:M61147; NID:g206118; PIDN:AAA41841.1; !1PID:g206119 REFERENCE JH0214 !$#authors Abe, T.; Nakabayashi, H.; Tamada, H.; Takagi, T.; Sakuragi, !1S.; Yamaki, K.; Shinohara, T. !$#journal Gene (1990) 91:209-215 !$#title Analysis of the human, bovine and rat 33-kDa proteins and !1cDNA in retina and pineal gland. !$#cross-references MUID:91007277; PMID:2210381 !$#accession JH0217 !'##molecule_type mRNA !'##residues 1-38,'G',40-87,'G',89-118,'T',120-210,'D',212-246 ##label !1ABE !'##cross-references GB:M33530; NID:g202524; PIDN:AAA40603.1; !1PID:g202525 CLASSIFICATION #superfamily phosducin KEYWORDS glycoprotein; phosphoprotein; photoreceptor; retina FEATURE !$8,58 #binding_site phosphate (Ser) (covalent) (by casein !8kinase II) #status predicted\ !$45,69 #binding_site phosphate (Ser) (covalent) (by protein !8kinase C) #status predicted\ !$73 #binding_site phosphate (Ser) (covalent) (by protein !8kinase A) #status predicted\ !$152 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$238 #binding_site phosphate (Thr) (covalent) (by casein !8kinase II) #status predicted SUMMARY #length 246 #molecular-weight 28201 #checksum 4329 SEQUENCE /// ENTRY A38379 #type complete TITLE phosducin, retinal - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 28-Jun-1991 #sequence_revision 14-Jul-1994 #text_change 04-Oct-1996 ACCESSIONS A38379; JH0215; A38378 REFERENCE A38379 !$#authors Lee, R.H.; Fowler, A.; McGinnis, J.F.; Lolley, R.N.; Craft, !1C.M. !$#journal J. Biol. Chem. (1990) 265:15867-15873 !$#title Amino acid and cDNA sequence of bovine phosducin, a soluble !1phosphoprotein from photoreceptor cells. !$#cross-references MUID:90368806; PMID:2203790 !$#accession A38379 !'##molecule_type protein !'##residues 1-245 ##label LEE REFERENCE JH0214 !$#authors Abe, T.; Nakabayashi, H.; Tamada, H.; Takagi, T.; Sakuragi, !1S.; Yamaki, K.; Shinohara, T. !$#journal Gene (1990) 91:209-215 !$#title Analysis of the human, bovine and rat 33-kDa proteins and !1cDNA in retina and pineal gland. !$#cross-references MUID:91007277; PMID:2210381 !$#accession JH0215 !'##molecule_type mRNA !'##residues 1-43,'P',45-238,'K',240-245 ##label ABE !'##cross-references GB:M33529 REFERENCE A38378 !$#authors Lee, R.H.; Brown, B.M.; Lolley, R.N. !$#journal J. Biol. Chem. (1990) 265:15860-15866 !$#title Protein kinase A phosphorylates retinal phosducin on serine !173 in Situ. !$#cross-references MUID:90368805; PMID:2394752 !$#accession A38378 !'##molecule_type protein !'##residues 54-58,'X',60-61,'X',63-64,'XX',67-70,'X',72-88,'X',90,'X', !192-93;102-114,'XTI' ##label LE2 CLASSIFICATION #superfamily phosducin KEYWORDS glycoprotein; phosphoprotein; photoreceptor; retina FEATURE !$8,58,238 #binding_site phosphate (Ser) (covalent) (by casein !8kinase II) #status predicted\ !$45,69 #binding_site phosphate (Ser) (covalent) (by protein !8kinase C) #status predicted\ !$73 #binding_site phosphate (Ser) (covalent) (by protein !8kinase A) #status experimental\ !$152 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 245 #molecular-weight 28216 #checksum 3282 SEQUENCE /// ENTRY OOHU #type complete TITLE rhodopsin - human ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 21-Jul-2000 ACCESSIONS A41200; A36235; A36537; I51864; I64813; I64814 REFERENCE A41200 !$#authors Nathans, J.; Hogness, D.S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:4851-4855 !$#title Isolation and nucleotide sequence of the gene encoding human !1rhodopsin. !$#cross-references MUID:84272729; PMID:6589631 !$#accession A41200 !'##molecule_type DNA !'##residues 1-348 ##label NAT !'##cross-references GB:K02281; NID:g1236136; PIDN:AAC31763.1; !1PID:g1236137 REFERENCE A36235 !$#authors Farrar, G.J.; Kenna, P.; Redmond, R.; McWilliam, P.; !1Bradley, D.G.; Humphries, M.M.; Sharp, E.M.; Inglehearn, !1C.F.; Bashir, R.; Jay, M.; Watty, A.; Ludwig, M.; Schinzel, !1A.; Samanns, C.; Gal, A.; Bhattacharya, S.; Humphries, P. !$#journal Am. J. Hum. Genet. (1990) 47:941-945 !$#title Autosomal dominant retinitis pigmentosa: absence of the !1rhodopsin proline->histidine substitution (codon 23) in !1pedigrees from Europe. !$#cross-references MUID:91051574; PMID:2239971 !$#accession A36235 !'##molecule_type DNA !'##residues 18-27 ##label FAR REFERENCE A36537 !$#authors Inglehearn, C.F.; Bashir, R.; Lester, D.H.; Jay, M.; Bird, !1A.C.; Bhattacharya, S.S. !$#journal Am. J. Hum. Genet. (1991) 48:26-30 !$#title A 3-bp deletion in the rhodopsin gene in a family with !1autosomal dominant retinitis pigmentosa. !$#cross-references MUID:91090106; PMID:1985460 !$#accession A36537 !'##molecule_type DNA !'##residues 248-263 ##label ING REFERENCE I51864 !$#authors Sheffield, V.C.; Fishman, G.A.; Beck, J.S.; Kimura, A.E.; !1Stone, E.M. !$#journal Am. J. Hum. Genet. (1991) 49:699-706 !$#title Identification of novel rhodopsin mutations associated with !1retinitis pigmentosa by GC-clamped denaturing gradient gel !1electrophoresis. !$#cross-references MUID:91377732; PMID:1897520 !$#accession I51864 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 14-16,'M',18-20 ##label SHE !'##cross-references GB:S55797; NID:g235658; PIDN:AAB19830.1; !1PID:g235659 !$#accession I64813 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 179-181,'S',183-185 ##label SH2 !'##cross-references GB:S55799; NID:g235660; PIDN:AAB19831.1; !1PID:g235661 !$#accession I64814 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 264-266,'L',268-270 ##label SH3 !'##cross-references GB:S55874; NID:g235662; PIDN:AAB19832.1; !1PID:g235663 GENETICS !$#gene GDB:RHO !'##cross-references GDB:120347; OMIM:180380 !$#map_position 3q21.3-3q24 !$#introns 121/1; 177/2; 232/3; 312/3 !$#note defects in this gene can result in retinitis pigmentosa CLASSIFICATION #superfamily vertebrate rhodopsin KEYWORDS acetylated amino end; chromoprotein; eye; G protein-coupled !1receptor; glycoprotein; lipoprotein; phosphoprotein; !1photoreceptor; retina; retinal; thiolester bond; !1transmembrane protein; vision FEATURE !$1-36 #domain extracellular #status predicted #label EX1\ !$37-61 #domain transmembrane #status predicted #label TM1\ !$62-73 #domain intracellular #status predicted #label IN1\ !$74-99 #domain transmembrane #status predicted #label TM2\ !$100-113 #domain extracellular #status predicted #label EX2\ !$114-133 #domain transmembrane #status predicted #label TM3\ !$134-152 #domain intracellular #status predicted #label IN2\ !$153-175 #domain transmembrane #status predicted #label TM4\ !$176-202 #domain extracellular #status predicted #label EX3\ !$203-230 #domain transmembrane #status predicted #label TM5\ !$231-252 #domain intracellular #status predicted #label IN3\ !$253-276 #domain transmembrane #status predicted #label TM6\ !$277-284 #domain extracellular #status predicted #label EX4\ !$285-309 #domain transmembrane #status predicted #label TM7\ !$310-348 #domain intracellular #status predicted #label IN4\ !$1 #modified_site acetylated amino end (Met) #status !8predicted\ !$2,15 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$110-187 #disulfide_bonds #status predicted\ !$296 #binding_site retinal (Lys) (covalent) #status !8predicted\ !$322,323 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$334,338,343 #binding_site phosphate (Ser) (covalent) (by !8rhodopsin kinase) #status predicted\ !$336 #binding_site phosphate (Thr) (covalent) (by !8rhodopsin kinase) #status predicted SUMMARY #length 348 #molecular-weight 38892 #checksum 7644 SEQUENCE /// ENTRY JC4267 #type complete TITLE opsin - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JC4267; PC4072 REFERENCE JC4267 !$#authors Smith, W.C.; Martinko, J.M.; Wheeler, J.N.; Hargrave, P.A.; !1McDowell, J.H. !$#journal Gene (1995) 162:331-332 !$#title The deduced amino-acid sequence of opsin from rabbit rod !1photoreceptors. !$#cross-references MUID:96032368; PMID:7557454 !$#accession JC4267 !'##molecule_type mRNA !'##residues 1-348 ##label SMI !'##cross-references GB:U21688; NID:g710429; PIDN:AAA91640.1; !1PID:g710430 !$#accession PC4072 !'##molecule_type protein !'##residues 1-39;318-348 ##label SM2 !'##experimental_source rod photoreceptor cells COMMENT This protein is a component of rhodopsin together with the !1retinoid chromophore. CLASSIFICATION #superfamily vertebrate rhodopsin KEYWORDS chromoprotein; eye; G protein-coupled receptor; !1glycoprotein; lipoprotein; phosphoprotein; photoreceptor; !1retina; retinal; thiolester bond; transmembrane protein; !1vision FEATURE !$37-61 #domain transmembrane #status predicted #label TM1\ !$75-99 #domain transmembrane #status predicted #label TM2\ !$109-133 #domain transmembrane #status predicted #label TM3\ !$152-176 #domain transmembrane #status predicted #label TM4\ !$203-227 #domain transmembrane #status predicted #label TM5\ !$253-277 #domain transmembrane #status predicted #label TM6\ !$286-310 #domain transmembrane #status predicted #label TM7\ !$2,15 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$110-187 #disulfide_bonds #status predicted\ !$296 #binding_site retinal (Lys) (covalent) #status !8predicted\ !$322,323 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$334,338,343 #binding_site phosphate (Ser) (covalent) (by !8rhodopsin kinase) #status predicted\ !$336,340,342 #binding_site phosphate (Thr) (covalent) (by !8rhodopsin kinase) #status predicted SUMMARY #length 348 #molecular-weight 38994 #checksum 7133 SEQUENCE /// ENTRY S32696 #type complete TITLE opsin, rod - dog ORGANISM #formal_name Canis lupus familiaris #common_name dog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S32696 REFERENCE S32696 !$#authors Petersen-Jones, S.M.; Sohal, A.K.; Sargan, D.R. !$#submission submitted to the EMBL Data Library, March 1993 !$#description The nucleotide sequence of the canine rod opsin gene. !$#accession S32696 !'##status preliminary !'##molecule_type DNA !'##residues 1-312 ##label PET !'##cross-references EMBL:X71380 CLASSIFICATION #superfamily vertebrate rhodopsin KEYWORDS chromoprotein; eye; G protein-coupled receptor; lipoprotein; !1phosphoprotein; photoreceptor; retina; retinal; !1transmembrane protein; vision FEATURE !$296 #binding_site retinal (Lys) (covalent) #status !8predicted SUMMARY #length 312 #molecular-weight 35262 #checksum 9846 SEQUENCE /// ENTRY S51677 #type complete TITLE rhodopsin - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S51677 REFERENCE S51677 !$#authors Huber, A.; Baker, B.B.; Sander, P.; Gerdon, G.; Paulsen, R.; !1Williams, T.P. !$#submission submitted to the EMBL Data Library, December 1994 !$#description Light-history effects: Levels of rhodopsin, opsin and opsin !1mRNA in albino rats born and reared in two different !1intensities of cyclic light. !$#accession S51677 !'##status preliminary !'##molecule_type mRNA !'##residues 1-348 ##label HUB !'##cross-references EMBL:Z46957; NID:g603874; PIDN:CAA87081.1; !1PID:g603875 CLASSIFICATION #superfamily vertebrate rhodopsin KEYWORDS chromoprotein; eye; G protein-coupled receptor; lipoprotein; !1phosphoprotein; photoreceptor; retina; retinal; thiolester !1bond; transmembrane protein; vision FEATURE !$296 #binding_site retinal (Lys) (covalent) #status !8predicted\ !$322,323 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 348 #molecular-weight 39056 #checksum 7282 SEQUENCE /// ENTRY A23665 #type complete TITLE opsin - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A23665; S01656 REFERENCE A23665 !$#authors Al-Ubaidi, M.R.; Pittler, S.J.; Champagne, M.S.; !1Triantafyllos, J.T.; McGinnis, J.F.; Baehr, W. !$#journal J. Biol. Chem. (1990) 265:20563-20569 !$#title Mouse opsin. Gene structure and molecular basis of multiple !1transcripts. !$#cross-references MUID:91056108; PMID:1978723 !$#accession A23665 !'##molecule_type DNA !'##residues 1-348 ##label ALA !'##cross-references GB:M55171; NID:g200144; PIDN:AAA63392.1; !1PID:g200145 REFERENCE S01656 !$#authors Baehr, W.; Falk, J.D.; Bugra, K.; Triantafyllos, J.T.; !1McGinnis, J.F. !$#journal FEBS Lett. (1988) 238:253-256 !$#title Isolation and analysis of the mouse opsin gene. !$#cross-references MUID:89005694; PMID:2844600 !$#accession S01656 !'##molecule_type DNA !'##residues 1-348 ##label BAE !'##cross-references EMBL:M36695 GENETICS !$#introns 121/1; 177/2; 232/3; 312/3 CLASSIFICATION #superfamily vertebrate rhodopsin KEYWORDS chromoprotein; eye; G protein-coupled receptor; !1glycoprotein; lipoprotein; phosphoprotein; photoreceptor; !1retina; retinal; transmembrane protein; vision FEATURE !$37-61 #domain transmembrane #status predicted #label TM1\ !$74-96 #domain transmembrane #status predicted #label TM2\ !$114-133 #domain transmembrane #status predicted #label TM3\ !$153-175 #domain transmembrane #status predicted #label TM4\ !$203-230 #domain transmembrane #status predicted #label TM5\ !$253-276 #domain transmembrane #status predicted #label TM6\ !$285-309 #domain transmembrane #status predicted #label TM7\ !$296 #binding_site retinal (Lys) (covalent) #status !8predicted SUMMARY #length 348 #molecular-weight 39027 #checksum 7513 SEQUENCE /// ENTRY S23398 #type complete TITLE rhodopsin - Chinese hamster ORGANISM #formal_name Cricetulus griseus #common_name Chinese hamster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S23398 REFERENCE S23398 !$#authors Gale, J.M.; Tobey, R.A.; D'Anna, J.A. !$#journal J. Mol. Biol. (1992) 224:343-358 !$#title Localization and DNA sequence of a replication origin in the !1rhodopsin gene locus of Chinese hamster cells. !$#cross-references MUID:92219256; PMID:1560457 !$#accession S23398 !'##status translation not shown !'##molecule_type DNA !'##residues 1-348 ##label GAL !'##cross-references EMBL:X61084; NID:g49478; PIDN:CAA43398.1; !1PID:g49479 GENETICS !$#introns 121/1; 177/2; 232/3; 312/3 CLASSIFICATION #superfamily vertebrate rhodopsin KEYWORDS chromoprotein; eye; G protein-coupled receptor; !1glycoprotein; lipoprotein; phosphoprotein; photoreceptor; !1retina; retinal; transmembrane protein; vision FEATURE !$37-61 #domain transmembrane #status predicted #label TM1\ !$74-96 #domain transmembrane #status predicted #label TM2\ !$114-133 #domain transmembrane #status predicted #label TM3\ !$153-175 #domain transmembrane #status predicted #label TM4\ !$203-230 #domain transmembrane #status predicted #label TM5\ !$253-276 #domain transmembrane #status predicted #label TM6\ !$285-309 #domain transmembrane #status predicted #label TM7\ !$296 #binding_site retinal (Lys) (covalent) #status !8predicted SUMMARY #length 348 #molecular-weight 39097 #checksum 7081 SEQUENCE /// ENTRY OOBO #type complete TITLE rhodopsin - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 15-Nov-1984 #sequence_revision 15-Nov-1984 #text_change 22-Jun-1999 ACCESSIONS A90840; A43773; A91306; A90115; A03154 REFERENCE A90840 !$#authors Nathans, J.; Hogness, D.S. !$#journal Cell (1983) 34:807-814 !$#title Isolation, sequence analysis, and intron-exon arrangement of !1the gene encoding bovine rhodopsin. !$#cross-references MUID:84026485; PMID:6194890 !$#accession A90840 !'##molecule_type DNA !'##residues 1-348 ##label NAT !'##cross-references GB:K00506; NID:g163441; PIDN:AAA30674.1; !1PID:g163443 REFERENCE A43773 !$#authors Kuo, C.H.; Yamagata, K.; Moyzis, R.K.; Bitensky, M.W.; Miki, !1N. !$#journal Brain Res. Mol. Brain Res. (1986) 1:251-260 !$#title Multiple opsin mRNA species in bovine retina. !$#contents clone LR-8 !$#accession A43773 !'##molecule_type mRNA !'##residues 6-280,'F',282-348 ##label KUO !'##cross-references GB:M21606; NID:g163444; PIDN:AAA30675.1; !1PID:g163445 !'##note the authors translated the codon TTC for residue 281 as Ser REFERENCE A91306 !$#authors Ovchinnikov, Y.A. !$#journal FEBS Lett. (1982) 148:179-191 !$#title Rhodopsin and bacteriorhodopsin: structure-function !1relationships. !$#cross-references MUID:83105679; PMID:6759163 !$#accession A91306 !'##molecule_type protein !'##residues 1-348 ##label OVC REFERENCE A90115 !$#authors Koike, S.; Nabeshima, Y.; Ogata, K.; Fukui, T.; Ohtsuka, E.; !1Ikehara, M.; Tokunaga, F. !$#journal Biochem. Biophys. Res. Commun. (1983) 116:563-567 !$#title Isolation and nucleotide sequence of a partial cDNA clone !1for bovine opsin. !$#cross-references MUID:84079861; PMID:6228228 !$#accession A90115 !'##molecule_type mRNA !'##residues 205-212,'V',214-348 ##label KOI REFERENCE A94631 !$#authors Hargrave, P.A. !$#submission submitted to the Protein Sequence Database, June 1984 !$#contents annotation; carbohydrate binding sites REFERENCE A90318 !$#authors Mullen, E.; Akhtar, M. !$#journal Biochem. J. (1983) 211:45-54 !$#title Structural studies on membrane-bound bovine rhodopsin. !$#cross-references MUID:83256442; PMID:6870827 !$#contents annotation; retinal binding site GENETICS !$#introns 121/1; 177/2; 232/3; 312/3 CLASSIFICATION #superfamily vertebrate rhodopsin KEYWORDS acetylated amino end; chromoprotein; eye; G protein-coupled !1receptor; glycoprotein; lipoprotein; phosphoprotein; !1photoreceptor; retina; retinal; thiolester bond; !1transmembrane protein; vision FEATURE !$37-61 #domain transmembrane #status predicted #label TM1\ !$74-96 #domain transmembrane #status predicted #label TM2\ !$114-133 #domain transmembrane #status predicted #label TM3\ !$153-175 #domain transmembrane #status predicted #label TM4\ !$203-230 #domain transmembrane #status predicted #label TM5\ !$253-276 #domain transmembrane #status predicted #label TM6\ !$285-309 #domain transmembrane #status predicted #label TM7\ !$1 #modified_site acetylated amino end (Met) #status !8experimental\ !$2,15 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$296 #binding_site retinal (Lys) (covalent) #status !8experimental\ !$322,323 #binding_site palmitate (Cys) (covalent) #status !8experimental\ !$334,338,343 #binding_site phosphate (Ser) (covalent) (by !8rhodopsin kinase) #status predicted\ !$335,336 #binding_site phosphate (Thr) (covalent) (by !8rhodopsin kinase) #status predicted SUMMARY #length 348 #molecular-weight 39007 #checksum 6843 SEQUENCE /// ENTRY OOSH #type complete TITLE rhodopsin - sheep ORGANISM #formal_name Ovis orientalis aries, Ovis ammon aries #common_name domestic sheep DATE 18-Aug-1982 #sequence_revision 30-Sep-1990 #text_change 07-May-1999 ACCESSIONS A30407; A90319; A93264; A03155 REFERENCE A91755 !$#authors Pappin, D.J.C.; Elipoulos, E.; Brett, M.; Findlay, J.B.C. !$#journal Int. J. Biol. Macromol. (1984) 6:73-76 !$#title A structural model for ovine rhodopsin. !$#accession A30407 !'##molecule_type protein !'##residues 1-348 ##label PAP !'##note no explanation is given for the differences in the sequence as !1seen in this paper from the original reports cited below !'##note peptides and unsequenced residues are ordered by homology with !1bovine rhodopsin REFERENCE A90319 !$#authors Brett, M.; Findlay, J.B.C. !$#journal Biochem. J. (1983) 211:661-670 !$#title Isolation and characterization of the CNBr peptides from the !1proteolytically derived N-terminal fragment of ovine opsin. !$#cross-references MUID:83282605; PMID:6224479 !$#accession A90319 !'##molecule_type protein !'##residues !11;40-44;45-86;87-111;144-155;156-163;164-183;184-207;208-241 !1##label BRE REFERENCE A93264 !$#authors Findlay, J.B.C.; Brett, M.; Pappin, D.J.C. !$#journal Nature (1981) 293:314-316 !$#title Primary structure of C-terminal functional sites in ovine !1rhodopsin. !$#cross-references MUID:82013638; PMID:7278988 !$#accession A93264 !'##molecule_type protein !'##residues 240-348 ##label FIN REFERENCE A90324 !$#authors Pappin, D.J.C.; Findlay, J.B.C. !$#journal Biochem. J. (1984) 217:605-613 !$#title Sequence variability in the retinal-attachment domain of !1mammalian rhodopsins. !$#cross-references MUID:84178280; PMID:6370231 !$#contents annotation; retinal binding site REFERENCE A44548 !$#authors Thompson, P.; Findlay, J.B.C. !$#journal Biochem. J. (1984) 220:773-780 !$#title Phosphorylation of ovine rhodopsin: identification of the !1phosphorylated sites. !$#cross-references MUID:84279984; PMID:6466303 !$#contents annotation; phosphorylation sites CLASSIFICATION #superfamily vertebrate rhodopsin KEYWORDS acetylated amino end; chromoprotein; eye; G protein-coupled !1receptor; glycoprotein; lipoprotein; phosphoprotein; !1photoreceptor; retina; retinal; thiolester bond; !1transmembrane protein; vision FEATURE !$37-61 #domain transmembrane #status predicted #label TM1\ !$74-96 #domain transmembrane #status predicted #label TM2\ !$114-133 #domain transmembrane #status predicted #label TM3\ !$153-175 #domain transmembrane #status predicted #label TM4\ !$203-230 #domain transmembrane #status predicted #label TM5\ !$253-276 #domain transmembrane #status predicted #label TM6\ !$285-309 #domain transmembrane #status predicted #label TM7\ !$1 #modified_site acetylated amino end (Met) #status !8experimental\ !$2,15 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$296 #binding_site retinal (Lys) (covalent) #status !8experimental\ !$322,323 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$334,338,343 #binding_site phosphate (Ser) (covalent) (by !8rhodopsin kinase) #status experimental\ !$335,336 #binding_site phosphate (Thr) (covalent) (by !8rhodopsin kinase) #status experimental SUMMARY #length 348 #molecular-weight 38891 #checksum 7301 SEQUENCE /// ENTRY S27231 #type complete TITLE rhodopsin - northern leopard frog ORGANISM #formal_name Rana pipiens #common_name northern leopard frog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S27231 REFERENCE S27231 !$#authors Pittler, S.J.; Fliesler, S.J.; Baehr, W. !$#journal FEBS Lett. (1992) 313:103-108 !$#title Primary structure of frog rhodopsin. !$#cross-references MUID:93050229; PMID:1426275 !$#accession S27231 !'##status preliminary !'##molecule_type mRNA !'##residues 1-354 ##label PIT !'##cross-references GB:S49004; NID:g260314; PIDN:AAB24265.1; !1PID:g260315 CLASSIFICATION #superfamily vertebrate rhodopsin KEYWORDS chromoprotein; eye; G protein-coupled receptor; lipoprotein; !1phosphoprotein; photoreceptor; retina; retinal; thiolester !1bond; transmembrane protein; vision FEATURE !$296 #binding_site retinal (Lys) (covalent) #status !8predicted\ !$322,323 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 354 #molecular-weight 39939 #checksum 2761 SEQUENCE /// ENTRY I51200 #type complete TITLE rhodopsin - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS I51200; S31474; S31473 REFERENCE I51200 !$#authors Saha, M.S.; Grainger, R.M. !$#journal Brain Res. Mol. Brain Res. (1993) 17:307-318 !$#title Early opsin expression in Xenopus embryos precedes !1photoreceptor differentiation. !$#cross-references MUID:93287804; PMID:8510503 !$#accession I51200 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-354 ##label SAH !'##cross-references GB:S62229; NID:g386187; PIDN:AAB27128.1; !1PID:g386188; EMBL:L04692; NID:g214633; PID:g214634 REFERENCE S31474 !$#authors Knox, B.E.; Scalzetti, L.C.; Batni, S.; Wang, J.Q. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Molecular cloning of the abundant rod opsin and transducin !1from Xenopus laevis. !$#accession S31474 !'##molecule_type mRNA !'##residues 1-106,'Q',108-136,'M',138-240,'A',242-354 ##label KNO !'##cross-references EMBL:L07770; NID:g214734; PIDN:AAC42232.1; !1PID:g214735 CLASSIFICATION #superfamily vertebrate rhodopsin KEYWORDS chromoprotein; eye; G protein-coupled receptor; !1glycoprotein; lipoprotein; phosphoprotein; photoreceptor; !1retina; retinal; transmembrane protein; vision FEATURE !$37-61 #domain transmembrane #status predicted #label TM1\ !$74-96 #domain transmembrane #status predicted #label TM2\ !$114-133 #domain transmembrane #status predicted #label TM3\ !$153-175 #domain transmembrane #status predicted #label TM4\ !$203-230 #domain transmembrane #status predicted #label TM5\ !$253-276 #domain transmembrane #status predicted #label TM6\ !$285-309 #domain transmembrane #status predicted #label TM7\ !$2,15 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$296 #binding_site retinal (Lys) (covalent) #status !8predicted SUMMARY #length 354 #molecular-weight 39786 #checksum 2767 SEQUENCE /// ENTRY JN0120 #type complete TITLE rhodopsin - Japanese lamprey ORGANISM #formal_name Lampetra japonica #common_name Japanese lamprey DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 22-Jun-1999 ACCESSIONS JN0120 REFERENCE JN0120 !$#authors Hisatomi, O.; Iwasa, T.; Tokunaga, F.; Yasui, A. !$#journal Biochem. Biophys. Res. Commun. (1991) 174:1125-1132 !$#title Isolation and characterization of lamprey rhodopsin cDNA. !$#cross-references MUID:91144585; PMID:1840482 !$#accession JN0120 !'##molecule_type mRNA !'##residues 1-353 ##label HIS !'##cross-references GB:M63632; NID:g213348; PIDN:AAA49342.1; !1PID:g213349 !'##experimental_source liver !'##note the authors translated the codon AAC for residue 195 as Glu CLASSIFICATION #superfamily vertebrate rhodopsin KEYWORDS chromoprotein; eye; G protein-coupled receptor; !1glycoprotein; lipoprotein; phosphoprotein; photoreceptor; !1retina; retinal; thiolester bond; transmembrane protein; !1vision FEATURE !$37-61 #domain transmembrane #status predicted #label TM1\ !$74-96 #domain transmembrane #status predicted #label TM2\ !$115-140 #domain transmembrane #status predicted #label TM3\ !$153-173 #domain transmembrane #status predicted #label TM4\ !$203-230 #domain transmembrane #status predicted #label TM5\ !$253-276 #domain transmembrane #status predicted #label TM6\ !$286-309 #domain transmembrane #status predicted #label TM7\ !$2,15 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$296 #binding_site retinal (Lys) (covalent) #status !8predicted\ !$322,323 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 353 #molecular-weight 39408 #checksum 2612 SEQUENCE /// ENTRY A48191 #type complete TITLE opsin, ultraviolet-sensitive - zebra fish ALTERNATE_NAMES ultraviolet visual pigment ORGANISM #formal_name Brachydanio rerio #common_name zebra fish DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A48191 REFERENCE A48191 !$#authors Robinson, J.; Schmitt, E.A.; Harosi, F.I.; Reece, R.J.; !1Dowling, J.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:6009-6012 !$#title Zebrafish ultraviolet visual pigment: absorption spectrum, !1sequence, and localization. !$#cross-references MUID:93317613; PMID:8327475 !$#accession A48191 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-354 ##label ROB !'##cross-references GB:L11014; NID:g215040; PIDN:AAA85566.1; !1PID:g1164505 CLASSIFICATION #superfamily vertebrate rhodopsin KEYWORDS chromoprotein; eye; G protein-coupled receptor; lipoprotein; !1phosphoprotein; photoreceptor; retina; retinal; thiolester !1bond; transmembrane protein; vision FEATURE !$296 #binding_site retinal (Lys) (covalent) #status !8predicted\ !$322,323 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 354 #molecular-weight 39753 #checksum 2515 SEQUENCE /// ENTRY S40688 #type complete TITLE opsin, rod - Pomatoschistus minutus ORGANISM #formal_name Pomatoschistus minutus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S40688 REFERENCE S40688 !$#authors Archer, S.N.; Lythgoe, J.N.; Hall, L. !$#journal Proc. R. Soc. Lond. B Biol. Sci. (1992) 248:19-25 !$#title Rod opsin cDNA sequence from the sand goby (Pomatoschistus !1minutus) compared with those of other vertebrates. !$#cross-references MUID:92396703; PMID:1381834 !$#accession S40688 !'##molecule_type mRNA !'##residues 1-352 ##label ARC !'##cross-references EMBL:X62405; NID:g433817; PIDN:CAA44275.1; !1PID:g433818 CLASSIFICATION #superfamily vertebrate rhodopsin KEYWORDS chromoprotein; eye; G protein-coupled receptor; !1glycoprotein; lipoprotein; phosphoprotein; photoreceptor; !1retina; retinal; transmembrane protein; vision FEATURE !$37-61 #domain transmembrane #status predicted #label TM1\ !$74-96 #domain transmembrane #status predicted #label TM2\ !$114-140 #domain transmembrane #status predicted #label TM3\ !$153-173 #domain transmembrane #status predicted #label TM4\ !$203-230 #domain transmembrane #status predicted #label TM5\ !$253-276 #domain transmembrane #status predicted #label TM6\ !$286-309 #domain transmembrane #status predicted #label TM7\ !$110-187 #disulfide_bonds #status predicted\ !$296 #binding_site retinal (Lys) (covalent) #status !8predicted SUMMARY #length 352 #molecular-weight 39409 #checksum 9436 SEQUENCE /// ENTRY A46191 #type complete TITLE iodopsin homolog - tokay ORGANISM #formal_name Gekko gecko #common_name tokay DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A46191 REFERENCE A46191 !$#authors Kojima, D.; Okano, T.; Fukada, Y.; Shichida, Y.; Yoshizawa, !1T.; Ebrey, T.G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:6841-6845 !$#title Cone visual pigments are present in gecko rod cells. !$#cross-references MUID:92357726; PMID:1379723 !$#accession A46191 !'##status preliminary !'##molecule_type mRNA !'##residues 1-355 ##label KOJ !'##cross-references GB:M92035; NID:g213258; PIDN:AAA49307.1; !1PID:g213259 !'##experimental_source retinas !'##note sequence extracted from NCBI backbone (NCBIN:110992, !1NCBIP:110993) CLASSIFICATION #superfamily vertebrate rhodopsin KEYWORDS chromoprotein; eye; G protein-coupled receptor; lipoprotein; !1phosphoprotein; photoreceptor; retina; retinal; thiolester !1bond; transmembrane protein; vision FEATURE !$296 #binding_site retinal (Lys) (covalent) #status !8predicted\ !$322,323 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 355 #molecular-weight 39688 #checksum 4503 SEQUENCE /// ENTRY A55962 #type complete TITLE opsin, pineal gland-specific - chicken ALTERNATE_NAMES P-opsin; pinopsin ORGANISM #formal_name Gallus gallus #common_name chicken DATE 23-Mar-1995 #sequence_revision 05-Apr-1995 #text_change 22-Jun-1999 ACCESSIONS A55962; S50857 REFERENCE A55962 !$#authors Max, M.; McKinnon, P.J.; Seidenman, K.J.; Barrett, R.K.; !1Applebury, M.L.; Takahashi, J.S.; Margolskee, R.F. !$#journal Science (1995) 267:1502-1506 !$#title Pineal opsin: a nonvisual opsin expressed in chick pineal. !$#cross-references MUID:95184012; PMID:7878470 !$#accession A55962 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-351 ##label MAX !'##cross-references GB:U87449; NID:g1842098 REFERENCE S50857 !$#authors Okano, T.; Yoshizawa, T.; Fukada, Y. !$#journal Nature (1994) 372:94-97 !$#title Pinopsin is a chicken pineal photoreceptive molecule. !$#cross-references MUID:95059405; PMID:7969427 !$#accession S50857 !'##molecule_type mRNA !'##residues 1-134,'R',136-162,'T',164-351 ##label OKA !'##cross-references GB:U15762; NID:g726462; PIDN:AAA64223.1; !1PID:g726463 FUNCTION !$#description modulation of melatonin biosynthesis by suppressing !1N-acetyltransferase activity in response to light in the !1pineal gland !$#note abundant in pineal gland but absent from retina CLASSIFICATION #superfamily vertebrate rhodopsin KEYWORDS chromoprotein; G protein-coupled receptor; glycoprotein; !1lipoprotein; phosphoprotein; photoreceptor; pineal gland; !1retinal; thiolester bond; transmembrane protein FEATURE !$1-30 #domain extracellular #status predicted #label EX1\ !$31-55 #domain transmembrane #status predicted #label TM1\ !$56-67 #domain intracellular #status predicted #label IN1\ !$68-90 #domain transmembrane #status predicted #label TM2\ !$91-107 #domain extracellular #status predicted #label EX2\ !$108-127 #domain transmembrane #status predicted #label TM3\ !$128-146 #domain intracellular #status predicted #label IN2\ !$147-169 #domain transmembrane #status predicted #label TM4\ !$170-194 #domain extracellular #status predicted #label EX3\ !$195-222 #domain transmembrane #status predicted #label TM5\ !$223-244 #domain intracellular #status predicted #label IN3\ !$245-268 #domain transmembrane #status predicted #label TM6\ !$269-277 #domain extracellular #status predicted #label EX4\ !$278-301 #domain transmembrane #status predicted #label TM7\ !$302-351 #domain intracellular #status predicted #label IN4\ !$104-181 #disulfide_bonds #status predicted\ !$288 #binding_site retinal (Lys) (covalent) #status !8predicted\ !$314,315 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 351 #molecular-weight 38173 #checksum 8662 SEQUENCE /// ENTRY JC5490 #type complete TITLE opsin, pineal gland-specific - pigeon ALTERNATE_NAMES P-opsin; pinopsin ORGANISM #formal_name Columba livia #common_name domestic pigeon DATE 07-Jul-1997 #sequence_revision 29-Aug-1997 #text_change 22-Jun-1999 ACCESSIONS JC5490 REFERENCE JC5490 !$#authors Kawamura, S.; Yokoyama, S. !$#journal Gene (1996) 182:213-214 !$#title Molecular characterization of the pigeon P-opsin gene. !$#cross-references MUID:97136713; PMID:8982090 !$#accession JC5490 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-349 ##label KAW !'##cross-references GB:U50598; NID:g1255098; PIDN:AAB40945.1; !1PID:g1255099 FUNCTION !$#description modulation of melatonin biosynthesis by suppressing !1N-acetyltransferase activity in response to light in the !1pineal gland !$#note abundant in pineal gland but absent from retina CLASSIFICATION #superfamily vertebrate rhodopsin KEYWORDS chromoprotein; G protein-coupled receptor; glycoprotein; !1lipoprotein; phosphoprotein; photoreceptor; pineal gland; !1retinal; thiolester bond; transmembrane protein FEATURE !$1-32 #domain extracellular #status predicted #label EX1\ !$33-57 #domain transmembrane #status predicted #label TM1\ !$58-69 #domain intracellular #status predicted #label IN1\ !$70-92 #domain transmembrane #status predicted #label TM2\ !$93-109 #domain extracellular #status predicted #label EX2\ !$110-129 #domain transmembrane #status predicted #label TM3\ !$130-148 #domain intracellular #status predicted #label IN2\ !$149-171 #domain transmembrane #status predicted #label TM4\ !$172-196 #domain extracellular #status predicted #label EX3\ !$197-224 #domain transmembrane #status predicted #label TM5\ !$225-246 #domain intracellular #status predicted #label IN3\ !$247-270 #domain transmembrane #status predicted #label TM6\ !$271-279 #domain extracellular #status predicted #label EX4\ !$280-303 #domain transmembrane #status predicted #label TM7\ !$304-349 #domain intracellular #status predicted #label IN4\ !$106-183 #disulfide_bonds #status predicted\ !$290 #binding_site retinal (Lys) (covalent) #status !8predicted\ !$316,317 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 349 #molecular-weight 38364 #checksum 5176 SEQUENCE /// ENTRY OOHUB #type complete TITLE opsin, blue-sensitive - human ALTERNATE_NAMES blue visual pigment ORGANISM #formal_name Homo sapiens #common_name man DATE 13-Aug-1986 #sequence_revision 13-Aug-1986 #text_change 22-Jun-1999 ACCESSIONS A03156; I59533 REFERENCE A94286 !$#authors Nathans, J.; Thomas, D.; Hogness, D.S. !$#journal Science (1986) 232:193-202 !$#title Molecular genetics of human color vision: the genes encoding !1blue, green, and red pigments. !$#cross-references MUID:86151699; PMID:2937147 !$#accession A03156 !'##molecule_type DNA !'##residues 1-348 ##label NAT !'##cross-references GB:M13299; NID:g1469901; PIDN:AAB05207.1; !1PID:g180685 !'##experimental_source retinal cones REFERENCE I59533 !$#authors Sarkar, G.; Sommer, S.S. !$#journal Science (1989) 244:331-334 !$#title Access to a messenger RNA sequence or its protein product is !1not limited by tissue or species specificity. !$#cross-references MUID:89222444; PMID:2565599 !$#accession I59533 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 272-307,'VKL' ##label RES !'##cross-references GB:M26172; NID:g418013; PIDN:AAA35608.1; !1PID:g553205 GENETICS !$#gene GDB:BCP !'##cross-references GDB:119032; OMIM:190900 !$#map_position 7q31.3-7q32 !$#introns 118/1; 174/2; 229/3; 309/3 CLASSIFICATION #superfamily vertebrate rhodopsin KEYWORDS chromoprotein; color vision; G protein-coupled receptor; !1glycoprotein; photoreceptor; retinal; transmembrane protein FEATURE !$34-57 #domain transmembrane #status predicted #label TM1\ !$71-94 #domain transmembrane #status predicted #label TM2\ !$113-136 #domain transmembrane #status predicted #label TM3\ !$149-172 #domain transmembrane #status predicted #label TM4\ !$198-221 #domain transmembrane #status predicted #label TM5\ !$250-273 #domain transmembrane #status predicted #label TM6\ !$283-306 #domain transmembrane #status predicted #label TM7\ !$14,75 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$293 #binding_site retinal (Lys) (covalent) #status !8predicted SUMMARY #length 348 #molecular-weight 39135 #checksum 2154 SEQUENCE /// ENTRY B54679 #type complete TITLE opsin, blue-sensitive - mouse ALTERNATE_NAMES blue visual pigment ORGANISM #formal_name Mus musculus #common_name house mouse DATE 18-Aug-1995 #sequence_revision 18-Aug-1995 #text_change 22-Jun-1999 ACCESSIONS B54679 REFERENCE A54679 !$#authors Chiu, M.I.; Zack, D.J.; Wang, Y.; Nathans, J. !$#journal Genomics (1994) 21:440-443 !$#title Murine and bovine blue cone pigment genes: cloning and !1characterization of two new members of the S family of !1visual pigments. !$#cross-references MUID:94375074; PMID:8088841 !$#accession B54679 !'##status preliminary !'##molecule_type DNA !'##residues 1-346 ##label CHI !'##cross-references GB:U92562; NID:g2058673; PIDN:AAB53320.1; !1PID:g2058675 CLASSIFICATION #superfamily vertebrate rhodopsin KEYWORDS chromoprotein; color vision; G protein-coupled receptor; !1glycoprotein; photoreceptor; retinal; transmembrane protein FEATURE !$32-55 #domain transmembrane #status predicted #label TM1\ !$69-92 #domain transmembrane #status predicted #label TM2\ !$111-134 #domain transmembrane #status predicted #label TM3\ !$147-170 #domain transmembrane #status predicted #label TM4\ !$196-219 #domain transmembrane #status predicted #label TM5\ !$248-271 #domain transmembrane #status predicted #label TM6\ !$281-304 #domain transmembrane #status predicted #label TM7\ !$12,73 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$291 #binding_site retinal (Lys) (covalent) #status !8predicted SUMMARY #length 346 #molecular-weight 38921 #checksum 2679 SEQUENCE /// ENTRY A54679 #type complete TITLE opsin, blue-sensitive - bovine ALTERNATE_NAMES blue visual pigment ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 18-Aug-1995 #sequence_revision 18-Aug-1995 #text_change 22-Jun-1999 ACCESSIONS A54679 REFERENCE A54679 !$#authors Chiu, M.I.; Zack, D.J.; Wang, Y.; Nathans, J. !$#journal Genomics (1994) 21:440-443 !$#title Murine and bovine blue cone pigment genes: cloning and !1characterization of two new members of the S family of !1visual pigments. !$#cross-references MUID:94375074; PMID:8088841 !$#accession A54679 !'##status preliminary !'##molecule_type DNA !'##residues 1-349 ##label CHI !'##cross-references GB:U49764; NID:g1237444; PIDN:AAA93189.1; !1PID:g1237446 CLASSIFICATION #superfamily vertebrate rhodopsin KEYWORDS chromoprotein; color vision; G protein-coupled receptor; !1glycoprotein; photoreceptor; retinal; transmembrane protein FEATURE !$35-58 #domain transmembrane #status predicted #label TM1\ !$72-95 #domain transmembrane #status predicted #label TM2\ !$114-137 #domain transmembrane #status predicted #label TM3\ !$150-173 #domain transmembrane #status predicted #label TM4\ !$199-222 #domain transmembrane #status predicted #label TM5\ !$251-274 #domain transmembrane #status predicted #label TM6\ !$284-307 #domain transmembrane #status predicted #label TM7\ !$15,76 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$294 #binding_site retinal (Lys) (covalent) #status !8predicted SUMMARY #length 349 #molecular-weight 39302 #checksum 4648 SEQUENCE /// ENTRY C46137 #type complete TITLE opsin, violet-sensitive - chicken ALTERNATE_NAMES violet visual pigment ORGANISM #formal_name Gallus gallus #common_name chicken DATE 21-Sep-1993 #sequence_revision 18-Nov-1994 #text_change 22-Jun-1999 ACCESSIONS C46137 REFERENCE A46137 !$#authors Okano, T.; Kojima, D.; Fukada, Y.; Shichida, Y.; Yoshizawa, !1T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:5932-5936 !$#title Primary structures of chicken cone visual pigments: !1vertebrate rhodopsins have evolved out of cone visual !1pigments. !$#cross-references MUID:92335211; PMID:1385866 !$#accession C46137 !'##status preliminary !'##molecule_type mRNA !'##residues 1-347 ##label OKA !'##cross-references GB:M92039; NID:g212885; PIDN:AAA49141.1; !1PID:g212886 !'##experimental_source retina !'##note sequence extracted from NCBI backbone (NCBIP:108556) CLASSIFICATION #superfamily vertebrate rhodopsin KEYWORDS chromoprotein; color vision; G protein-coupled receptor; !1glycoprotein; photoreceptor; retinal; transmembrane protein FEATURE !$32-55 #domain transmembrane #status predicted #label TM1\ !$69-92 #domain transmembrane #status predicted #label TM2\ !$111-134 #domain transmembrane #status predicted #label TM3\ !$147-170 #domain transmembrane #status predicted #label TM4\ !$196-219 #domain transmembrane #status predicted #label TM5\ !$248-271 #domain transmembrane #status predicted #label TM6\ !$281-304 #domain transmembrane #status predicted #label TM7\ !$12,73 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$291 #binding_site retinal (Lys) (covalent) #status !8predicted SUMMARY #length 347 #molecular-weight 38720 #checksum 7971 SEQUENCE /// ENTRY OOFF #type complete TITLE rhodopsin - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 22-Jun-1999 ACCESSIONS A90864; A90865; A22012 REFERENCE A90864 !$#authors O'Tousa, J.E.; Baehr, W.; Martin, R.L.; Hirsh, J.; Pak, !1W.L.; Applebury, M.L. !$#journal Cell (1985) 40:839-850 !$#title The Drosophila ninaE gen encodes an opsin. !$#cross-references MUID:85176937; PMID:2985266 !$#accession A90864 !'##molecule_type DNA !'##residues 1-373 ##label OTO !'##cross-references GB:K02315; NID:g158007; PIDN:AAA28733.1; !1PID:g158008 REFERENCE A90865 !$#authors Zuker, C.S.; Cowman, A.F.; Rubin, G.M. !$#journal Cell (1985) 40:851-858 !$#title Isolation and structure of a rhodopsin gene from Drosophila !1melanogaster. !$#cross-references MUID:85176938; PMID:2580638 !$#accession A90865 !'##molecule_type mRNA !'##residues 1-373 ##label ZUK COMMENT The domains were proposed from hydropathy indices. COMMENT Some or all of the carboxyl-terminal Ser or Thr residues may !1be phosphorylated. GENETICS !$#gene ninaE !'##cross-references FlyBase:FBgn0002940 !$#map_position 3R66 (92B8-11) !$#introns 3/2; 190/2; 239/3; 332/2 CLASSIFICATION #superfamily vertebrate rhodopsin KEYWORDS chromoprotein; G protein-coupled receptor; glycoprotein; !1photoreceptor; retinal; transmembrane protein FEATURE !$1-49 #domain extracellular #status predicted #label EX1\ !$50-74 #domain transmembrane #status predicted #label TM1\ !$75-86 #domain intracellular #status predicted #label IN1\ !$87-109 #domain transmembrane #status predicted #label TM2\ !$110-127 #domain extracellular #status predicted #label EX2\ !$128-153 #domain transmembrane #status predicted #label TM3\ !$154-160 #domain intracellular #status predicted #label IN2\ !$161-181 #domain transmembrane #status predicted #label TM4\ !$182-215 #domain extracellular #status predicted #label EX3\ !$216-243 #domain transmembrane #status predicted #label TM5\ !$244-276 #domain intracellular #status predicted #label IN3\ !$277-300 #domain transmembrane #status predicted #label TM6\ !$301-308 #domain extracellular #status predicted #label EX4\ !$309-332 #domain transmembrane #status predicted #label TM7\ !$333-373 #domain intracellular #status predicted #label IN4\ !$20,196 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$319 #binding_site retinal (Lys) (covalent) #status !8predicted SUMMARY #length 373 #molecular-weight 41494 #checksum 4358 SEQUENCE /// ENTRY OOFF2 #type complete TITLE opsin 2 - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 22-Jun-1999 ACCESSIONS A24058 REFERENCE A24058 !$#authors Cowman, A.F.; Zuker, C.S.; Rubin, G.M. !$#journal Cell (1986) 44:705-710 !$#title An opsin gene expressed in only one photoreceptor cell type !1of the Drosophila eye. !$#cross-references MUID:86133563; PMID:2936466 !$#accession A24058 !'##molecule_type DNA !'##residues 1-381 ##label COW !'##cross-references GB:M12896; NID:g158009; PIDN:AAA28734.1; !1PID:g158010 COMMENT This protein is specifically expressed in photoreceptor cell !1R8 of the Drosophila compound eye. GENETICS !$#gene Rh2 !'##cross-references FlyBase:FBgn0003248 !$#map_position 3R (91D1-2) !$#introns 33/3; 339/2; 350/3 CLASSIFICATION #superfamily vertebrate rhodopsin KEYWORDS chromoprotein; G protein-coupled receptor; photoreceptor; !1retinal; transmembrane protein FEATURE !$1-56 #domain extracellular #status predicted #label EX1\ !$57-81 #domain transmembrane #status predicted #label TM1\ !$82-93 #domain intracellular #status predicted #label IN1\ !$94-116 #domain transmembrane #status predicted #label TM2\ !$117-134 #domain extracellular #status predicted #label EX2\ !$135-160 #domain transmembrane #status predicted #label TM3\ !$161-167 #domain intracellular #status predicted #label IN2\ !$168-188 #domain transmembrane #status predicted #label TM4\ !$189-222 #domain extracellular #status predicted #label EX3\ !$223-250 #domain transmembrane #status predicted #label TM5\ !$251-283 #domain intracellular #status predicted #label IN3\ !$284-307 #domain transmembrane #status predicted #label TM6\ !$308-315 #domain extracellular #status predicted #label EX4\ !$316-339 #domain transmembrane #status predicted #label TM7\ !$340-381 #domain intracellular #status predicted #label IN4\ !$326 #binding_site retinal (Lys) (covalent) #status !8predicted SUMMARY #length 381 #molecular-weight 42722 #checksum 113 SEQUENCE /// ENTRY OOHUR #type complete TITLE opsin, red-sensitive - human ORGANISM #formal_name Homo sapiens #common_name man DATE 13-Aug-1986 #sequence_revision 13-Aug-1986 #text_change 22-Jun-1999 ACCESSIONS A03157 REFERENCE A94286 !$#authors Nathans, J.; Thomas, D.; Hogness, D.S. !$#journal Science (1986) 232:193-202 !$#title Molecular genetics of human color vision: the genes encoding !1blue, green, and red pigments. !$#cross-references MUID:86151699; PMID:2937147 !$#accession A03157 !'##molecule_type DNA !'##residues 1-364 ##label NAT !'##cross-references GB:M13305; NID:g180701; PIDN:AAB59524.1; !1PID:g180703 !'##experimental_source retinal cones GENETICS !$#gene GDB:RCP !'##cross-references GDB:120724; OMIM:303900 !$#map_position Xq28-Xq28 !$#introns 38/1; 137/1; 193/2; 248/3; 328/3 CLASSIFICATION #superfamily vertebrate rhodopsin KEYWORDS chromoprotein; color vision; G protein-coupled receptor; !1glycoprotein; photoreceptor; retinal; sex-linked !1inheritance; transmembrane protein FEATURE !$53-76 #domain transmembrane #status predicted #label TM1\ !$90-113 #domain transmembrane #status predicted #label TM2\ !$132-155 #domain transmembrane #status predicted #label TM3\ !$168-191 #domain transmembrane #status predicted #label TM4\ !$217-240 #domain transmembrane #status predicted #label TM5\ !$269-292 #domain transmembrane #status predicted #label TM6\ !$302-325 #domain transmembrane #status predicted #label TM7\ !$34 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$312 #binding_site retinal (Lys) (covalent) #status !8predicted SUMMARY #length 364 #molecular-weight 40572 #checksum 7888 SEQUENCE /// ENTRY OOHUG #type complete TITLE opsin, green-sensitive - human ALTERNATE_NAMES middle wavelength sensitive cone pigment (MWS) ORGANISM #formal_name Homo sapiens #common_name man DATE 13-Aug-1986 #sequence_revision 13-Aug-1986 #text_change 22-Jun-1999 ACCESSIONS A03158 REFERENCE A94286 !$#authors Nathans, J.; Thomas, D.; Hogness, D.S. !$#journal Science (1986) 232:193-202 !$#title Molecular genetics of human color vision: the genes encoding !1blue, green, and red pigments. !$#cross-references MUID:86151699; PMID:2937147 !$#accession A03158 !'##molecule_type DNA !'##residues 1-364 ##label NAT !'##cross-references GB:K03494; NID:g180693; PIDN:AAB59503.1; !1PID:g180695 !'##experimental_source retinal cones GENETICS !$#gene GDB:GCP; CBD !'##cross-references GDB:120622; OMIM:303800 !$#map_position Xq28-Xq28 !$#introns 38/1; 137/1; 193/2; 248/3; 328/3 !$#note the number of genes in phenotypically normal individuals !1apparently varies between 1 and 3 CLASSIFICATION #superfamily vertebrate rhodopsin KEYWORDS chromoprotein; color vision; G protein-coupled receptor; !1glycoprotein; photoreceptor; retinal; sex-linked !1inheritance; transmembrane protein FEATURE !$53-76 #domain transmembrane #status predicted #label TM1\ !$90-113 #domain transmembrane #status predicted #label TM2\ !$132-155 #domain transmembrane #status predicted #label TM3\ !$168-191 #domain transmembrane #status predicted #label TM4\ !$217-240 #domain transmembrane #status predicted #label TM5\ !$269-292 #domain transmembrane #status predicted #label TM6\ !$302-325 #domain transmembrane #status predicted #label TM7\ !$34 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$312 #binding_site retinal (Lys) (covalent) #status !8predicted SUMMARY #length 364 #molecular-weight 40584 #checksum 6364 SEQUENCE /// ENTRY S12864 #type complete TITLE retinal isomerase (EC 5.2.1.3) [validated] - Japanese flying squid ALTERNATE_NAMES retinochrome ORGANISM #formal_name Todarodes pacificus #common_name Japanese flying squid DATE 18-Aug-2000 #sequence_revision 18-Aug-2000 #text_change 01-Sep-2000 ACCESSIONS S12864; S39449 REFERENCE S12864 !$#authors Hara-Nishimura, I.; Matsumoto, T.; Mori, H.; Nishimura, M.; !1Hara, R.; Hara, T. !$#journal FEBS Lett. (1990) 271:106-110 !$#title Cloning and nucleotide sequence of cDNA for retinochrome, !1retinal photoisomerase from the squid retina. !$#cross-references MUID:91032043; PMID:2226795 !$#accession S12864 !'##molecule_type mRNA !'##residues 1-301 ##label HAR !'##cross-references EMBL:X57143; NID:g10776; PID:g10777 REFERENCE S39449 !$#authors Hara-Nishimura, I.; Kondo, M.; Nishimura, M.; Hara, R.; !1Hara, T. !$#journal FEBS Lett. (1993) 335:94-98 !$#title Amino acid sequence surrounding the retinal-binding site in !1retinochrome of the squid, Todarodes pacificus. !$#cross-references MUID:94063090; PMID:8243675 !$#accession S39449 !'##status preliminary !'##molecule_type protein !'##residues 274-277,'X',279-282 ##label HA2 CLASSIFICATION #superfamily vertebrate rhodopsin KEYWORDS chromoprotein; cis-trans-isomerase; G protein-coupled !1receptor; glycoprotein; photoreceptor; retinal; !1transmembrane protein FEATURE !$1-301 #product retinal isomerase #status experimental !8#label MAT\ !$19-43 #domain transmembrane #status predicted #label TM1\ !$54-75 #domain transmembrane #status predicted #label TM2\ !$95-120 #domain transmembrane #status predicted #label TM3\ !$133-153 #domain transmembrane #status predicted #label TM4\ !$181-208 #domain transmembrane #status predicted #label TM5\ !$231-255 #domain transmembrane #status predicted #label TM6\ !$265-288 #domain transmembrane #status predicted #label TM7\ !$170 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$275 #binding_site retinal (Lys) (covalent) #status !8experimental SUMMARY #length 301 #molecular-weight 33490 #checksum 8849 SEQUENCE /// ENTRY QRHUB2 #type complete TITLE beta-2-adrenergic receptor - human ORGANISM #formal_name Homo sapiens #common_name man DATE 07-Mar-1988 #sequence_revision 18-Aug-1995 #text_change 22-Jun-1999 ACCESSIONS A27525; A28405; A29574; A29061; A29026 REFERENCE A27525 !$#authors Schofield, P.R.; Rhee, L.M.; Peralta, E.G. !$#journal Nucleic Acids Res. (1987) 15:3636 !$#title Primary structure of the human beta-adrenergic receptor !1gene. !$#cross-references MUID:87203400; PMID:3033609 !$#accession A27525 !'##molecule_type DNA !'##residues 1-413 ##label SCH !'##cross-references GB:Y00106; NID:g29370; PIDN:CAA68289.1; PID:g29371 REFERENCE A28405 !$#authors Emorine, L.J.; Marullo, S.; Delavier-Klutchko, C.; Kaveri, !1S.V.; Durieu-Trautmann, O.; Strosberg, A.D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:6995-6999 !$#title Structure of the gene for human beta-2-adrenergic receptor: !1expression and promoter characterization. !$#cross-references MUID:88041037; PMID:2823249 !$#accession A28405 !'##molecule_type DNA !'##residues 1-15,'G',17-413 ##label EMO !'##cross-references GB:J02960; NID:g178203; PIDN:AAA88017.1; !1PID:g178204 REFERENCE A29574 !$#authors Kobilka, B.K.; Frielle, T.; Dohlman, H.G.; Bolanowski, M.A.; !1Dixon, R.A.F.; Keller, P.; Caron, M.G.; Lefkowitz, R.J. !$#journal J. Biol. Chem. (1987) 262:7321-7327 !$#title Delineation of the intronless nature of the genes for the !1human and hamster beta-2-adrenergic receptor and their !1putative promoter regions. !$#cross-references MUID:87222338; PMID:3034889 !$#accession A29574 !'##molecule_type DNA; mRNA !'##residues 1-413 ##label KO2 !'##cross-references GB:M15169; GB:J02728; NID:g178201; PIDN:AAA88015.1; !1PID:g178202; GB:M16106 REFERENCE A29061 !$#authors Kobilka, B.K.; Dixon, R.A.F.; Frielle, T.; Dohlman, H.G.; !1Bolanowski, M.A.; Sigal, I.S.; Yang-Feng, T.L.; Francke, U.; !1Caron, M.G.; Lefkowitz, R.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:46-50 !$#title cDNA for the human beta-2-adrenergic receptor: a protein !1with multiple membrane-spanning domains and encoded by a !1gene whose chromosomal location is shared with that of the !1receptor for platelet-derived growth factor. !$#cross-references MUID:87092393; PMID:3025863 !$#accession A29061 !'##molecule_type mRNA !'##residues 1-413 ##label KOB !'##cross-references GB:M15169; NID:g178201; PIDN:AAA88015.1; !1PID:g178202 REFERENCE A29026 !$#authors Chung, F.Z.; Lentes, K.U.; Gocayne, J.; Fitzgerald, M.; !1Robinson, D.; Kerlavage, A.R.; Fraser, C.M.; Venter, J.C. !$#journal FEBS Lett. (1987) 211:200-206 !$#title Cloning and sequence analysis of the human brain !1beta-adrenergic receptor. Evolutionary relationship to !1rodent and avian beta-receptors and porcine muscarinic !1receptors. !$#cross-references MUID:87105974; PMID:3026848 !$#accession A29026 !'##molecule_type mRNA !'##residues 1-140,'S',142-413 ##label CHU !'##cross-references GB:X04827 !'##experimental_source brain stem GENETICS !$#gene GDB:ADRB2; ADRB2R !'##cross-references GDB:120541; OMIM:109690 !$#map_position 5q31-5q32 !$#introns #status absent CLASSIFICATION #superfamily vertebrate rhodopsin KEYWORDS G protein-coupled receptor; glycoprotein; transmembrane !1protein FEATURE !$33-59 #domain transmembrane #status predicted #label TM1\ !$69-96 #domain transmembrane #status predicted #label TM2\ !$108-129 #domain transmembrane #status predicted #label TM3\ !$152-174 #domain transmembrane #status predicted #label TM4\ !$199-220 #domain transmembrane #status predicted #label TM5\ !$274-295 #domain transmembrane #status predicted #label TM6\ !$307-326 #domain transmembrane #status predicted #label TM7\ !$6,15,187 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 413 #molecular-weight 46556 #checksum 4127 SEQUENCE /// ENTRY QRHYB2 #type complete TITLE beta-2-adrenergic receptor - hamster ORGANISM #formal_name Cricetinae gen. sp. #common_name hamster DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 31-Dec-1993 ACCESSIONS A03159 REFERENCE A03159 !$#authors Dixon, R.A.F.; Kobilka, B.K.; Strader, D.J.; Benovic, J.L.; !1Dohlman, H.G.; Frielle, T.; Bolanowski, M.A.; Bennett, C.D.; !1Rands, E.; Diehl, R.E.; Mumford, R.A.; Slater, E.E.; Sigal, !1I.S.; Caron, M.G.; Lefkowitz, R.J.; Strader, C.D. !$#journal Nature (1986) 321:75-79 !$#title Cloning of the gene and cDNA for mammalian beta-adrenergic !1receptor and homology with rhodopsin. !$#cross-references MUID:86203654; PMID:3010132 !$#accession A03159 !'##molecule_type mRNA !'##residues 1-418 ##label DIX COMMENT This protein may have up to seven hydrophobic !1membrane-spanning helices, as does rhodopsin, but the exact !1limits have not yet been determined. COMMENT This protein was isolated from the lung. CLASSIFICATION #superfamily vertebrate rhodopsin KEYWORDS G protein-coupled receptor; glycoprotein; lung; membrane !1protein; phosphoprotein FEATURE !$6,15 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$261,262,345,346,347 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 418 #molecular-weight 46861 #checksum 1677 SEQUENCE /// ENTRY QRHUB1 #type complete TITLE beta-1-adrenergic receptor - human ORGANISM #formal_name Homo sapiens #common_name man DATE 22-Jan-1993 #sequence_revision 18-Aug-1995 #text_change 22-Jun-1999 ACCESSIONS A39911 REFERENCE A39911 !$#authors Frielle, T.; Collins, S.; Daniel, K.W.; Caron, M.G.; !1Lefkowitz, R.J.; Kobilka, B.K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:7920-7924 !$#title Cloning of the cDNA for the human beta-1-adrenergic !1receptor. !$#cross-references MUID:88068509; PMID:2825170 !$#accession A39911 !'##molecule_type mRNA !'##residues 1-477 ##label FRI !'##cross-references GB:J03019; NID:g178199; PIDN:AAA51667.1; !1PID:g178200 GENETICS !$#gene GDB:ADRB1; ADRB1R !'##cross-references GDB:119654; OMIM:109630 !$#map_position 10q25-10q25 CLASSIFICATION #superfamily vertebrate rhodopsin KEYWORDS G protein-coupled receptor; glycoprotein; transmembrane !1protein FEATURE !$58-84 #domain transmembrane #status predicted #label TM1\ !$94-121 #domain transmembrane #status predicted #label TM2\ !$133-154 #domain transmembrane #status predicted #label TM3\ !$177-199 #domain transmembrane #status predicted #label TM4\ !$224-245 #domain transmembrane #status predicted #label TM5\ !$325-346 #domain transmembrane #status predicted #label TM6\ !$358-377 #domain transmembrane #status predicted #label TM7\ !$15 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 477 #molecular-weight 51223 #checksum 1819 SEQUENCE /// ENTRY QRHUB3 #type complete TITLE beta-3-adrenergic receptor, splice form 2 - human ALTERNATE_NAMES beta-3-adrenergic receptor form A CONTAINS beta-3-adrenergic receptor splice form 1 ORGANISM #formal_name Homo sapiens #common_name man DATE 22-Jan-1993 #sequence_revision 18-Aug-1995 #text_change 16-Jun-2000 ACCESSIONS A41348; S33752 REFERENCE A41348 !$#authors Emorine, L.J.; Marullo, S.; Briend-Sutren, M.M.; Patey, G.; !1Tate, K.; Delavier-Klutchko, C.; Strosberg, A.D. !$#journal Science (1989) 245:1118-1121 !$#title Molecular characterization of the human beta-3-adrenergic !1receptor. !$#cross-references MUID:89368947; PMID:2570461 !$#accession A41348 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-402 ##label EMO !'##cross-references GB:M29932; NID:g178895; PIDN:AAA35550.1; !1PID:g178896 !'##note splice form 1 REFERENCE S33751 !$#authors Lelias, J.M.; Kaghad, M.; Rodriguez, M.; Chalon, P.; Bonnin, !1J.; Dupre, I.; Delpech, B.; Bensaid, M.; LeFur, G.; Ferrara, !1P.; Caput, D. !$#journal FEBS Lett. (1993) 324:127-130 !$#title Molecular cloning of a human beta-3-adrenergic receptor !1cDNA. !$#cross-references MUID:93285320; PMID:8389717 !$#accession S33752 !'##molecule_type DNA !'##residues 392-414 ##label LEL !'##cross-references EMBL:X70812; NID:g312398; PIDN:CAA50142.1; !1PID:g1666375 !'##note splice form 2 GENETICS !$#gene GDB:ADRB3 !'##cross-references GDB:203869; OMIM:109691 !$#map_position 8p12-8p11.1 !$#introns 402/2 CLASSIFICATION #superfamily vertebrate rhodopsin KEYWORDS alternative splicing; G protein-coupled receptor; !1glycoprotein; transmembrane protein FEATURE !$1-414 #product beta-3-adrenergic receptor precursor splice !8form 2 #status predicted #label MAT2\ !$1-402 #product beta-3-adrenergic receptor precursor splice !8form 1 #status predicted #label MAT1\ !$37-63 #domain transmembrane #status predicted #label TM1\ !$73-101 #domain transmembrane #status predicted #label TM2\ !$113-133 #domain transmembrane #status predicted #label TM3\ !$156-178 #domain transmembrane #status predicted #label TM4\ !$204-225 #domain transmembrane #status predicted #label TM5\ !$293-314 #domain transmembrane #status predicted #label TM6\ !$327-347 #domain transmembrane #status predicted #label TM7\ !$8,26 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 414 #molecular-weight 44147 #checksum 2370 SEQUENCE /// ENTRY QRHUBE #type complete TITLE beta-3-adrenergic receptor, splice form 3 - human ALTERNATE_NAMES beta-3-adrenergic receptor form B CONTAINS beta-3-adrenergic receptor splice form 1 ORGANISM #formal_name Homo sapiens #common_name man DATE 03-Feb-1994 #sequence_revision 18-Aug-1995 #text_change 16-Jun-2000 ACCESSIONS S33751; S33753; S32803; S32826 REFERENCE S33751 !$#authors Lelias, J.M.; Kaghad, M.; Rodriguez, M.; Chalon, P.; Bonnin, !1J.; Dupre, I.; Delpech, B.; Bensaid, M.; LeFur, G.; Ferrara, !1P.; Caput, D. !$#journal FEBS Lett. (1993) 324:127-130 !$#title Molecular cloning of a human beta-3-adrenergic receptor !1cDNA. !$#cross-references MUID:93285320; PMID:8389717 !$#accession S33751 !'##molecule_type mRNA !'##residues 1-408 ##label LEL1 !'##cross-references EMBL:X70811; NID:g312396; PIDN:CAA50141.1; !1PID:g312397 !'##note splice form 3 !$#accession S33753 !'##molecule_type DNA !'##residues 392-408 ##label LEL2 !'##cross-references GB:X70812; NID:g312398; PIDN:CAA50143.1; !1PID:g1666376 REFERENCE S32803 !$#authors Emorine, L.J. !$#submission submitted to the EMBL Data Library, March 1993 !$#accession S32803 !'##molecule_type DNA !'##residues 1-408 ##label EMO !'##cross-references EMBL:X72861; NID:g298094; PIDN:CAA51383.1; !1PID:g298095 REFERENCE S32826 !$#authors van Spronsen, A.; Nahmias, C.; Krief, S.; Briend-Sutren, !1M.M.; Strosberg, A.D.; Emorine, L.J. !$#journal Eur. J. Biochem. (1993) 213:1117-1124 !$#title The promoter and intron/exon structure of the human and !1mouse beta3-adrenergic-receptor genes. !$#cross-references MUID:93279311; PMID:8389293 !$#accession S32826 !'##molecule_type DNA !'##residues 1-8;344-350;394-408 ##label SPR GENETICS !$#gene GDB:ADRB3 !'##cross-references GDB:203869; OMIM:109691 !$#map_position 8p12-8p11.1 !$#introns 402/2 CLASSIFICATION #superfamily vertebrate rhodopsin KEYWORDS alternative splicing; G protein-coupled receptor; !1glycoprotein; transmembrane protein FEATURE !$1-408 #product beta-3-adrenergic receptor precursor splice !8form 3 #status predicted #label MAT3\ !$1-402 #product beta-3-adrenergic receptor precursor splice !8form 1 #status predicted #label MAT1\ !$37-63 #domain transmembrane #status predicted #label TM1\ !$73-101 #domain transmembrane #status predicted #label TM2\ !$113-133 #domain transmembrane #status predicted #label TM3\ !$156-178 #domain transmembrane #status predicted #label TM4\ !$204-225 #domain transmembrane #status predicted #label TM5\ !$293-314 #domain transmembrane #status predicted #label TM6\ !$327-347 #domain transmembrane #status predicted #label TM7\ !$8,26 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 408 #molecular-weight 43519 #checksum 6799 SEQUENCE /// ENTRY DYHUD1 #type complete TITLE dopamine receptor D1 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 22-Jun-1999 ACCESSIONS S11377; S11376; S11379 REFERENCE S11377 !$#authors Zhou, Q.Y.; Grandy, D.K.; Thambi, L.; Kushner, J.A.; van !1Tol, H.H.M.; Cone, R.; Pribnow, D.; Salon, J.; Bunzow, J.R.; !1Civelli, O. !$#journal Nature (1990) 347:76-80 !$#title Cloning and expression of human and rat D(1) dopamine !1receptors. !$#cross-references MUID:90370094; PMID:2168520 !$#accession S11377 !'##molecule_type DNA !'##residues 1-446 ##label ZHO !'##cross-references EMBL:X58987 REFERENCE S11376 !$#authors Dearry, A.; Gingrich, J.A.; Falardeau, P.; Fremeau Jr., !1R.T.; Bates, M.D.; Caron, M.G. !$#journal Nature (1990) 347:72-76 !$#title Molecular cloning and expression of the gene for a human D !1(1) dopamine receptor. !$#cross-references MUID:90370093; PMID:2144334 !$#accession S11376 !'##molecule_type DNA; mRNA !'##residues 1-446 ##label DEA !'##cross-references EMBL:X55760; NID:g30396; PIDN:CAA39286.1; !1PID:g30397 REFERENCE S11379 !$#authors Sunahara, R.K.; Niznik, H.B.; Weiner, D.M.; Stormann, T.M.; !1Brann, M.R.; Kennedy, J.L.; Gelernter, J.E.; Rozmahel, R.; !1Yang, Y.; Israel, Y.; Seeman, P.; O'Dowd, B.F. !$#journal Nature (1990) 347:80-83 !$#title Human dopamine D(1) receptor encoded by an intronless gene !1on chromosome 5. !$#cross-references MUID:90370095; PMID:1975640 !$#accession S11379 !'##molecule_type DNA !'##residues 1-446 ##label SUN !'##cross-references GB:X55758; NID:g288931; PIDN:CAA39284.1; !1PID:g288932 GENETICS !$#gene GDB:DRD1 !'##cross-references GDB:125240; OMIM:126449 !$#map_position 5q34-5q35 CLASSIFICATION #superfamily vertebrate rhodopsin KEYWORDS G protein-coupled receptor; glycoprotein; lipoprotein; !1neurotransmitter receptor; phosphoprotein; thiolester bond; !1transmembrane protein FEATURE !$25-49 #domain transmembrane #status predicted #label TM1\ !$61-87 #domain transmembrane #status predicted #label TM2\ !$98-119 #domain transmembrane #status predicted #label TM3\ !$140-163 #domain transmembrane #status predicted #label TM4\ !$194-214 #domain transmembrane #status predicted #label TM5\ !$215-273 #domain intracellular #status predicted #label CYT\ !$274-295 #domain transmembrane #status predicted #label TM6\ !$313-333 #domain transmembrane #status predicted #label TM7\ !$5,175 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$96-186 #disulfide_bonds #status predicted\ !$136,268 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$259,263 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$347 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 446 #molecular-weight 49293 #checksum 4546 SEQUENCE /// ENTRY DYRTD1 #type complete TITLE dopamine receptor D1 - rat ALTERNATE_NAMES catecholamine receptor G36 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1992 #sequence_revision 03-Oct-1995 #text_change 22-Jun-1999 ACCESSIONS A36049; S11378; S40690; S09096; B34555 REFERENCE A36049 !$#authors Monsma Jr., F.J.; Mahan, L.C.; McVittie, L.D.; Gerfen, C.R.; !1Sibley, D.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:6723-6727 !$#title Molecular cloning and expression of a D-1 dopamine receptor !1linked to adenylyl cyclase activation. !$#cross-references MUID:90370857; PMID:2168556 !$#accession A36049 !'##status preliminary !'##molecule_type mRNA !'##residues 1-487 ##label MON !'##cross-references GB:M35077 REFERENCE S11377 !$#authors Zhou, Q.Y.; Grandy, D.K.; Thambi, L.; Kushner, J.A.; van !1Tol, H.H.M.; Cone, R.; Pribnow, D.; Salon, J.; Bunzow, J.R.; !1Civelli, O. !$#journal Nature (1990) 347:76-80 !$#title Cloning and expression of human and rat D(1) dopamine !1receptors. !$#cross-references MUID:90370094; PMID:2168520 !$#accession S11378 !'##status not compared with conceptual translation !'##molecule_type DNA; mRNA !'##residues 42-131,'F',133,'S',135-487 ##label ZHO REFERENCE S40690 !$#authors Zhou, Q.Y.; Li, C.; Civelli, O. !$#journal J. Neurochem. (1992) 59:1875-1883 !$#title Characterization of gene organization and promoter region of !1the rat dopamine D1 receptor gene. !$#cross-references MUID:93019272; PMID:1402930 !$#accession S40690 !'##status preliminary !'##molecule_type DNA !'##residues 42-131,'F',133,'S',135-487 ##label ZH2 !'##cross-references EMBL:S46131; NID:g258143; PIDN:AAB23803.1; !1PID:g258144 REFERENCE S09096 !$#authors O'Dowd, B.F.; Nguyen, T.; Tirpak, A.; Jarvie, K.R.; Israel, !1Y.; Seeman, P.; Niznik, H.B. !$#journal FEBS Lett. (1990) 262:8-12 !$#title Cloning of two additional catecholamine receptors from rat !1brain. !$#cross-references MUID:90201380; PMID:2138567 !$#accession S09096 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 155-205,'T',207-230,'F',232-267,'G',269-293,'W',295-304 !1##label ODO CLASSIFICATION #superfamily vertebrate rhodopsin KEYWORDS G protein-coupled receptor; glycoprotein; lipoprotein; !1neurotransmitter receptor; phosphoprotein; thiolester bond; !1transmembrane protein FEATURE !$65-89 #domain transmembrane #status predicted #label TM1\ !$101-127 #domain transmembrane #status predicted #label TM2\ !$138-159 #domain transmembrane #status predicted #label TM3\ !$180-202 #domain transmembrane #status predicted #label TM4\ !$235-255 #domain transmembrane #status predicted #label TM5\ !$256-314 #domain intracellular #status predicted #label CYT\ !$314-336 #domain transmembrane #status predicted #label TM6\ !$354-374 #domain transmembrane #status predicted #label TM7\ !$45,215 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$176,309 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$270,300,304 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$388 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 487 #molecular-weight 54253 #checksum 5612 SEQUENCE /// ENTRY DYHUD2 #type complete TITLE dopamine receptor D2 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 21-Jul-2000 ACCESSIONS S08417; S09618; S20842; A33392; A34502; A37013; A37384; !1A48409; S40694 REFERENCE S08417 !$#authors Robakis, N.K.; Mohamadi, M.; Fu, D.Y.; Sambamurti, K.; !1Refolo, L.M. !$#journal Nucleic Acids Res. (1990) 18:1299 !$#title Human retina D2 receptor cDNAs have multiple polyadenylation !1sites and differ from a pituitary clone at the 5' non-coding !1region. !$#cross-references MUID:90206805; PMID:2138729 !$#accession S08417 !'##molecule_type mRNA !'##residues 1-443 ##label ROB !'##cross-references EMBL:X51362; NID:g30495; PIDN:CAA35746.1; !1PID:g30496 REFERENCE S09618 !$#authors dal Toso, R.; Sommer, B.; Ewert, M.; Herb, A.; Pritchett, !1D.B.; Bach, A.; Shivers, B.D.; Seeburg, P.H. !$#journal EMBO J. (1989) 8:4025-4034 !$#title The dopamine D2 receptor: two molecular forms generated by !1alternative splicing. !$#cross-references MUID:90076122; PMID:2531656 !$#accession S09618 !'##molecule_type mRNA !'##residues 1-443 ##label DAL !'##cross-references EMBL:X51645; NID:g30867; PIDN:CAB56463.1; !1PID:g5921480 !$#accession S20842 !'##molecule_type DNA !'##residues 179-379 ##label DA2 !'##cross-references EMBL:X51646; NID:g30868; PIDN:CAB37869.1; !1PID:g4467834 REFERENCE A33392 !$#authors Selbie, L.A.; Hayes, G.; Shine, J. !$#journal DNA (1989) 8:683-689 !$#title The major dopamine D2 receptor: molecular analysis of the !1human D2-A subtype. !$#cross-references MUID:90126238; PMID:2533064 !$#accession A33392 !'##molecule_type mRNA !'##residues 1-443 ##label SEL !'##cross-references GB:M30625; NID:g181431; PIDN:AAA88024.1; !1PID:g181432 REFERENCE A34502 !$#authors Grandy, D.K.; Marchionni, M.A.; Makam, H.; Stofko, R.E.; !1Alfano, M.; Frothingham, L.; Fischer, J.B.; Burke-Howie, !1K.J.; Bunzow, J.R.; Server, A.C.; Civelli, O. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:9762-9766 !$#title Cloning of the cDNA and gene for a human D-2 dopamine !1receptor. !$#cross-references MUID:90099344; PMID:2532362 !$#accession A34502 !'##molecule_type mRNA !'##residues 1-443 ##label GRA !'##cross-references GB:M29066; NID:g181828; PIDN:AAA52761.1; !1PID:g181829; GB:M77247; GB:M77248; GB:M77249; GB:M77250 REFERENCE A37013 !$#authors Stormann, T.M.; Gdula, D.C.; Weiner, D.M.; Brann, M.R. !$#journal Mol. Pharmacol. (1990) 37:1-6 !$#title Molecular cloning and expression of a dopamine D2 receptor !1from human retina. !$#cross-references MUID:90136534; PMID:2137193 !$#accession A37013 !'##molecule_type mRNA !'##residues 1-241,271-443 ##label STO REFERENCE A37384 !$#authors Selbie, L.A.; Hayes, G.; Shine, J. !$#journal Adv. Second Messenger Phosphoprotein Res. (1990) 24:9-14 !$#title DNA homology screening: isolation and characterization of !1the human D2-A dopamine receptor subtype. !$#cross-references MUID:91000955; PMID:2144985 !$#accession A37384 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-443 ##label SE2 !'##experimental_source fetal brain and pituitary REFERENCE A48409 !$#authors Dearry, A.; Falardeau, P.; Shores, C.; Caron, M.G. !$#journal Cell. Mol. Neurobiol. (1991) 11:437-453 !$#title D2 dopamine receptors in the human retina: cloning of cDNA !1and localization of mRNA. !$#cross-references MUID:92076439; PMID:1835903 !$#accession A48409 !'##molecule_type mRNA !'##residues 1-241,271-443 ##label DEA !'##cross-references GB:S69899; NID:g240290; PIDN:AAB20571.1; !1PID:g240291 !'##experimental_source retina !'##note sequence extracted from NCBI backbone (NCBIN:69899, !1NCBIP:69900) REFERENCE S40694 !$#authors Araki, K.; Kuwano, R.; Morii, K.; Hayashi, S.; Minoshima, !1S.; Shimizu, N.; Katagiri, T.; Usui, H.; Kumanishi, T.; !1Takahashi, Y. !$#journal Neurochem. Int. (1992) 21:91-98 !$#title Structure and expression of human and rat D2 dopamine !1receptor genes. !$#cross-references MUID:93264902; PMID:1363862 !$#accession S40694 !'##status preliminary !'##molecule_type mRNA !'##residues 1-39,'R',41-443 ##label ARA !'##cross-references GB:S62137; NID:g405309; PIDN:AAB26819.1; !1PID:g405310 GENETICS !$#gene GDB:DRD2 !'##cross-references GDB:119852; OMIM:126450 !$#map_position 11q23.1-11q23.1 !$#introns 178/1; 241/3; 270/3; 380/1 CLASSIFICATION #superfamily vertebrate rhodopsin KEYWORDS alternative splicing; G protein-coupled receptor; !1glycoprotein; lipoprotein; neurotransmitter receptor; !1phosphoprotein; thiolester bond; transmembrane protein FEATURE !$1-443 #product dopamine receptor D2 (long form) #status !8predicted #label MAT1\ !$1-241,271-443 #product dopamine receptor D2 (short form) #status !8predicted #label MAT2\ !$38-59 #domain transmembrane #status predicted #label TM1\ !$71-94 #domain transmembrane #status predicted #label TM2\ !$109-130 #domain transmembrane #status predicted #label TM3\ !$152-174 #domain transmembrane #status predicted #label TM4\ !$188-210 #domain transmembrane #status predicted #label TM5\ !$211-373 #domain intracellular #status predicted #label CYT\ !$374-397 #domain transmembrane #status predicted #label TM6\ !$406-429 #domain transmembrane #status predicted #label TM7\ !$5,17,23 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$107-182 #disulfide_bonds #status predicted\ !$443 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 443 #molecular-weight 50619 #checksum 6706 SEQUENCE /// ENTRY DYBOD2 #type complete TITLE dopamine receptor D2 - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 22-Jun-1999 ACCESSIONS S08163 REFERENCE S08163 !$#authors Chio, C.L.; Hess, G.F.; Graham, R.S.; Huff, R.M. !$#journal Nature (1990) 343:266-269 !$#title A second molecular form of D2 dopamine receptor in rat and !1bovine caudate nucleus. !$#cross-references MUID:90136899; PMID:2137198 !$#accession S08163 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-444 ##label CHI !'##cross-references GB:X51657; NID:g304; PIDN:CAA35970.1; PID:g305 CLASSIFICATION #superfamily vertebrate rhodopsin KEYWORDS alternative splicing; G protein-coupled receptor; !1glycoprotein; lipoprotein; neurotransmitter receptor; !1phosphoprotein; thiolester bond; transmembrane protein FEATURE !$1-444 #product dopamine receptor D2 (long form) #status !8predicted #label MAT1\ !$1-241,271-444 #product dopamine receptor D2 (short form) #status !8predicted #label MAT2\ !$39-59 #domain transmembrane #status predicted #label TM1\ !$71-94 #domain transmembrane #status predicted #label TM2\ !$109-130 #domain transmembrane #status predicted #label TM3\ !$152-174 #domain transmembrane #status predicted #label TM4\ !$188-210 #domain transmembrane #status predicted #label TM5\ !$211-374 #domain intracellular #status predicted #label CYT\ !$375-398 #domain transmembrane #status predicted #label TM6\ !$407-430 #domain transmembrane #status predicted #label TM7\ !$5,17,23 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$107-182 #disulfide_bonds #status predicted\ !$444 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 444 #molecular-weight 50671 #checksum 2336 SEQUENCE /// ENTRY DYMSD2 #type complete TITLE dopamine receptor D2 - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 22-Jun-1999 ACCESSIONS S13921; JH0452; JH0453 REFERENCE S13921 !$#authors Montmayeur, J.P.; Bausero, P.; Amlaiky, N.; Maroteaux, L.; !1Hen, R.; Borrelli, E. !$#journal FEBS Lett. (1991) 278:239-243 !$#title Differential expression of the mouse D(2) dopamine receptor !1isoforms. !$#cross-references MUID:91122293; PMID:1991517 !$#accession S13921 !'##molecule_type mRNA !'##residues 1-444 ##label MON !'##cross-references EMBL:X55674; NID:g50648; PIDN:CAA39209.1; !1PID:g50649 REFERENCE JH0452 !$#authors Mack, K.J.; Todd, R.D.; O'Malley, K.L. !$#journal J. Neurochem. (1991) 57:795-801 !$#title The mouse dopamine D2A receptor gene: sequence homology with !1the rat and human genes and expression of alternative !1transcripts. !$#cross-references MUID:91318281; PMID:1861151 !$#accession JH0452 !'##molecule_type DNA !'##residues 1-24,'C',26-28,'P',30-88,'R',90-103,'S',105-270,'P',252-444 !1##label MAC !'##note the authors translated the codon CAG for residue 16 as Glu CLASSIFICATION #superfamily vertebrate rhodopsin KEYWORDS alternative splicing; G protein-coupled receptor; !1glycoprotein; lipoprotein; neurotransmitter receptor; !1phosphoprotein; thiolester bond; transmembrane protein FEATURE !$1-444 #product dopamine receptor D2 (long form) #status !8predicted #label MAT1\ !$1-241,271-444 #product dopamine receptor D2 (short form) #status !8predicted #label MAT2\ !$38-59 #domain transmembrane #status predicted #label TM1\ !$71-94 #domain transmembrane #status predicted #label TM2\ !$109-130 #domain transmembrane #status predicted #label TM3\ !$152-174 #domain transmembrane #status predicted #label TM4\ !$188-210 #domain transmembrane #status predicted #label TM5\ !$211-374 #domain intracellular #status predicted #label CYT\ !$375-398 #domain transmembrane #status predicted #label TM6\ !$407-430 #domain transmembrane #status predicted #label TM7\ !$5,17,23 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$107-182 #disulfide_bonds #status predicted\ !$147,148,228,229, !$355,360,365 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$225,373 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$444 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 444 #molecular-weight 50903 #checksum 276 SEQUENCE /// ENTRY S08146 #type complete TITLE dopamine receptor D2 - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 22-Jun-1999 ACCESSIONS S08146; S19610; S07791; S09040; S09097; S19251; S08145; !1A34046; S21548; A34555 REFERENCE S08146 !$#authors Monsma Jr., F.J.; McVittie, L.D.; Gerfen, C.R.; Mahan, L.C.; !1Sibley, D.R. !$#journal Nature (1989) 342:926-929 !$#title Multiple D2 dopamine receptors produced by alternative RNA !1splicing. !$#cross-references MUID:90081873; PMID:2480527 !$#accession S08146 !'##molecule_type mRNA !'##residues 1-444 ##label MON !'##cross-references EMBL:X17458 REFERENCE S08163 !$#authors Chio, C.L.; Hess, G.F.; Graham, R.S.; Huff, R.M. !$#journal Nature (1990) 343:266-269 !$#title A second molecular form of D2 dopamine receptor in rat and !1bovine caudate nucleus. !$#cross-references MUID:90136899; PMID:2137198 !$#accession S19610 !'##molecule_type mRNA !'##residues 1-444 ##label CHI REFERENCE S07791 !$#authors Bunzow, J.R.; van Tol, H.H.M.; Grandy, D.K.; Albert, P.; !1Salon, J.; Christie, M.; Machida, C.A.; Neve, K.A.; Civelli, !1O. !$#journal Nature (1988) 336:783-787 !$#title Cloning and expression of a rat D(2) dopamine receptor cDNA. !$#cross-references MUID:89082643; PMID:2974511 !$#accession S07791 !'##molecule_type mRNA !'##residues 1-241,271-444 ##label BUN !'##cross-references EMBL:X14028 REFERENCE S09040 !$#authors Rao, D.D.; McKelvy, J.; Kebabian, J.; MacKenzie, R.G. !$#journal FEBS Lett. (1990) 263:18-22 !$#title Two forms of the rat D(2) dopamine receptor as revealed by !1the polymerase chain reaction. !$#cross-references MUID:90235966; PMID:2139615 !$#accession S09040 !'##molecule_type mRNA !'##residues 1-98,'D',100-172,'R',174-179,'G',181-444 ##label RAO !'##cross-references GB:X53278; NID:g288117; PIDN:CAA37373.1; !1PID:g288118 REFERENCE S09096 !$#authors O'Dowd, B.F.; Nguyen, T.; Tirpak, A.; Jarvie, K.R.; Israel, !1Y.; Seeman, P.; Niznik, H.B. !$#journal FEBS Lett. (1990) 262:8-12 !$#title Cloning of two additional catecholamine receptors from rat !1brain. !$#cross-references MUID:90201380; PMID:2138567 !$#accession S09097 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 126-303 ##label ODO REFERENCE S09618 !$#authors dal Toso, R.; Sommer, B.; Ewert, M.; Herb, A.; Pritchett, !1D.B.; Bach, A.; Shivers, B.D.; Seeburg, P.H. !$#journal EMBO J. (1989) 8:4025-4034 !$#title The dopamine D2 receptor: two molecular forms generated by !1alternative splicing. !$#cross-references MUID:90076122; PMID:2531656 !$#accession S19251 !'##molecule_type mRNA !'##residues 175-299 ##label DAL REFERENCE S08145 !$#authors Giros, B.; Sokoloff, P.; Martres, M.P.; Riou, J.F.; Emorine, !1L.J.; Schwartz, J.C. !$#journal Nature (1989) 342:923-926 !$#title Alternative splicing directs the expression of two D2 !1dopamine receptor isoforms. !$#cross-references MUID:90081872; PMID:2531847 !$#accession S08145 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 239-272 ##label GIR REFERENCE A34046 !$#authors Miller, J.C.; Wang, Y.; Filer, D. !$#journal Biochem. Biophys. Res. Commun. (1990) 166:109-112 !$#title Identification by sequence analysis of a second rat brain !1cDNA encoding the dopamine (D2) receptor. !$#cross-references MUID:90147685; PMID:2137336 !$#accession A34046 !'##molecule_type mRNA !'##residues 242-270 ##label MIL !'##cross-references GB:M32241; NID:g203902; PIDN:AAA41074.1; !1PID:g203904 REFERENCE S21548 !$#authors Taylor, P.L.; Inglis, J.D.; Eidne, K.A. !$#submission submitted to the EMBL Data Library, October 1990 !$#description 5' untranslated region of rat pituitary dopamine D2(B) !1receptor contains a putative CpG island. !$#accession S21548 !'##status preliminary !'##molecule_type mRNA !'##residues 1-444 ##label TAY !'##cross-references EMBL:X56065; NID:g56063; PIDN:CAA39543.1; !1PID:g56064 GENETICS !$#introns 241/3; 270/3; 381/1 !$#note the list of introns may be incomplete CLASSIFICATION #superfamily vertebrate rhodopsin KEYWORDS alternative splicing; G protein-coupled receptor; !1glycoprotein; lipoprotein; neurotransmitter receptor; !1phosphoprotein; thiolester bond; transmembrane protein FEATURE !$1-444 #product dopamine receptor D2 (long form) #status !8predicted #label MAT1\ !$1-241,271-444 #product dopamine receptor D2 (short form) #status !8predicted #label MAT2\ !$38-59 #domain transmembrane #status predicted #label TM1\ !$71-94 #domain transmembrane #status predicted #label TM2\ !$109-130 #domain transmembrane #status predicted #label TM3\ !$152-174 #domain transmembrane #status predicted #label TM4\ !$188-210 #domain transmembrane #status predicted #label TM5\ !$211-374 #domain intracellular #status predicted #label INT\ !$375-398 #domain transmembrane #status predicted #label TM6\ !$407-430 #domain transmembrane #status predicted #label TM7\ !$5,17,23 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$107-182 #disulfide_bonds #status predicted\ !$228,229 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$444 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 444 #molecular-weight 50903 #checksum 276 SEQUENCE /// ENTRY DYXLD2 #type complete TITLE dopamine receptor D2 - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 22-Jun-1999 ACCESSIONS S14827 REFERENCE S14827 !$#authors Martens, G.J.M.; Molhuizen, H.O.F.; Groeneveld, D.; Roubos, !1E.W. !$#journal FEBS Lett. (1991) 281:85-89 !$#title Cloning and sequence analysis of brain cDNA encoding a !1Xenopus D(2) dopamine receptor. !$#cross-references MUID:91200321; PMID:1826663 !$#accession S14827 !'##molecule_type mRNA !'##residues 1-442 ##label MAR !'##cross-references EMBL:X59500; NID:g64648; PIDN:CAA42088.1; !1PID:g64649 CLASSIFICATION #superfamily vertebrate rhodopsin KEYWORDS alternative splicing; G protein-coupled receptor; !1glycoprotein; neurotransmitter receptor; phosphoprotein; !1transmembrane protein FEATURE !$1-442 #product dopamine receptor D2 (long form) #status !8predicted #label MAT1\ !$1-232,266-442 #product dopamine receptor D2 (short form) #status !8predicted #label MAT2\ !$32-53 #domain transmembrane #status predicted #label TM1\ !$65-88 #domain transmembrane #status predicted #label TM2\ !$103-124 #domain transmembrane #status predicted #label TM3\ !$146-168 #domain transmembrane #status predicted #label TM4\ !$182-204 #domain transmembrane #status predicted #label TM5\ !$205-372 #domain intracellular #status predicted #label INT\ !$373-396 #domain transmembrane #status predicted #label TM6\ !$405-428 #domain transmembrane #status predicted #label TM7\ !$5,15,18,169 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$223 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 442 #molecular-weight 49738 #checksum 4349 SEQUENCE /// ENTRY DYRTD3 #type complete TITLE dopamine receptor D3 - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 22-Jun-1999 ACCESSIONS S11565; S41849; I52280 REFERENCE S11565 !$#authors Sokoloff, P.; Giros, B.; Martres, M.P.; Bouthenet, M.L.; !1Schwartz, J.C. !$#journal Nature (1990) 347:146-151 !$#title Molecular cloning and characterization of a novel dopamine !1receptor (D(3)) as a target for neuroleptics. !$#cross-references MUID:90370111; PMID:1975644 !$#accession S11565 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-446 ##label SOK !'##cross-references EMBL:X53944; NID:g56060; PIDN:CAA37887.1; !1PID:g56061 REFERENCE S41849 !$#authors Giros, B.; Martres, M.P.; Pilon, C.; Sokoloff, P.; Schwartz, !1J.C. !$#journal Biochem. Biophys. Res. Commun. (1991) 176:1584-1592 !$#title Shorter variants of the D(3) dopamine receptor produced !1through various patterns of alternative splicing. !$#cross-references MUID:91248260; PMID:2039532 !$#accession S41849 !'##molecule_type DNA !'##residues 1-138,'E',140-446 ##label GIR REFERENCE I52280 !$#authors Pagliusi, S.; Chollet-Daemerius, A.; Losberger, C.; Mills, !1A.; Kawashima, E. !$#journal Biochem. Biophys. Res. Commun. (1993) 194:465-471 !$#title Characterization of a novel exon within the D3 receptor gene !1giving rise to an mRNA isoform expressed in rat brain. !$#cross-references MUID:93326159; PMID:8333859 !$#accession I52280 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 71-106 ##label RES !'##cross-references GB:S63847; NID:g399705; PIDN:AAB27545.1; !1PID:g399707 !'##experimental_source strain Wistar, brain GENETICS !$#introns 90/3 CLASSIFICATION #superfamily vertebrate rhodopsin KEYWORDS G protein-coupled receptor; glycoprotein; lipoprotein; !1neurotransmitter receptor; phosphoprotein; thiolester bond; !1transmembrane protein FEATURE !$33-55 #domain transmembrane #status predicted #label TM1\ !$67-92 #domain transmembrane #status predicted #label TM2\ !$105-126 #domain transmembrane #status predicted #label TM3\ !$150-172 #domain transmembrane #status predicted #label TM4\ !$186-209 #domain transmembrane #status predicted #label TM5\ !$210-375 #domain intracellular #status predicted #label CYT\ !$376-399 #domain transmembrane #status predicted #label TM6\ !$413-434 #domain transmembrane #status predicted #label TM7\ !$12,19 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$103-181 #disulfide_bonds #status predicted\ !$446 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 446 #molecular-weight 49515 #checksum 9850 SEQUENCE /// ENTRY DYHUD4 #type complete TITLE dopamine receptor D4 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 02-Sep-1997 ACCESSIONS S15079 REFERENCE S15079 !$#authors van Tol, H.H.M.; Bunzow, J.R.; Guan, H.C.; Sunahara, R.K.; !1Seeman, P.; Niznik, H.B.; Civelli, O. !$#journal Nature (1991) 350:610-614 !$#title Cloning of the gene for a human dopamine D(4) receptor with !1high affinity for the antipsychotic clozapine. !$#cross-references MUID:91204054; PMID:1840645 !$#accession S15079 !'##molecule_type DNA !'##residues 1-387 ##label VAN !'##cross-references EMBL:X58497 GENETICS !$#gene GDB:DRD4 !'##cross-references GDB:127782; OMIM:126452 !$#map_position 11p15.5-11p15.5 !$#introns 95/3; 133/2; 269/2; 321/1 CLASSIFICATION #superfamily vertebrate rhodopsin KEYWORDS alternative splicing; G protein-coupled receptor; !1glycoprotein; neurotransmitter receptor; phosphoprotein; !1transmembrane protein FEATURE !$34-60 #domain transmembrane #status predicted #label TM1\ !$72-96 #domain transmembrane #status predicted #label TM2\ !$110-131 #domain transmembrane #status predicted #label TM3\ !$153-174 #domain transmembrane #status predicted #label TM4\ !$192-214 #domain transmembrane #status predicted #label TM5\ !$215-314 #domain intracellular #status predicted #label INT\ !$315-339 #domain transmembrane #status predicted #label TM6\ !$349-368 #domain transmembrane #status predicted #label TM7\ !$3 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$108-185 #disulfide_bonds #status predicted\ !$149,239 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$297,306 #binding_site phosphate (Thr) (covalent) #status !8predicted SUMMARY #length 387 #molecular-weight 40893 #checksum 1488 SEQUENCE /// ENTRY DYHUD5 #type complete TITLE dopamine receptor D5 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 22-Jun-1999 ACCESSIONS S15080; A41232 REFERENCE S15080 !$#authors Sunahara, R.K.; Guan, H.C.; O'Dowd, B.F.; Seeman, P.; !1Laurier, L.G.; Ng, G.; George, S.R.; Torchia, J.; van Tol, !1H.H.M.; Niznik, H.B. !$#journal Nature (1991) 350:614-619 !$#title Cloning of the gene for a human dopamine D(5) receptor with !1higher affinity for dopamine than D(1). !$#cross-references MUID:91204055; PMID:1826762 !$#accession S15080 !'##molecule_type DNA !'##residues 1-477 ##label SUN !'##cross-references EMBL:X58454; NID:g32048; PIDN:CAA41360.1; !1PID:g32049 REFERENCE A41232 !$#authors Grandy, D.K.; Zhang, Y.; Bouvier, C.; Zhou, Q.Y.; Johnson, !1R.A.; Allen, L.; Buck, K.; Bunzow, J.R.; Salon, J.; Civelli, !1O. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:9175-9179 !$#title Multiple human D-5 dopamine receptor genes: a functional !1receptor and two pseudogenes. !$#cross-references MUID:92021013; PMID:1833775 !$#accession A41232 !'##molecule_type DNA !'##residues 1-477 ##label GRA !'##cross-references GB:M67439; NID:g181830; PIDN:AAA52329.1; !1PID:g181831 GENETICS !$#gene GDB:DRD5; DRD1L2 !'##cross-references GDB:127548; OMIM:126453 !$#map_position 4p15.3-4p15.1 CLASSIFICATION #superfamily vertebrate rhodopsin KEYWORDS G protein-coupled receptor; glycoprotein; lipoprotein; !1neurotransmitter receptor; phosphoprotein; thiolester bond; !1transmembrane protein FEATURE !$41-66 #domain transmembrane #status predicted #label TM1\ !$78-104 #domain transmembrane #status predicted #label TM2\ !$115-136 #domain transmembrane #status predicted #label TM3\ !$157-180 #domain transmembrane #status predicted #label TM4\ !$225-245 #domain transmembrane #status predicted #label TM5\ !$246-297 #domain intracellular #status predicted #label INT\ !$298-319 #domain transmembrane #status predicted #label TM6\ !$341-361 #domain transmembrane #status predicted #label TM7\ !$7,199 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$113-217 #disulfide_bonds #status predicted\ !$153,292 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$260,271,283 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$375 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 477 #molecular-weight 52950 #checksum 7417 SEQUENCE /// ENTRY OORTB2 #type complete TITLE bradykinin receptor type B-2 - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 22-Jun-1999 ACCESSIONS A41283; A55079; S47529 REFERENCE A41283 !$#authors McEachern, A.E.; Shelton, E.R.; Bhakta, S.; Obernolte, R.; !1Bach, C.; Zuppan, P.; Fujisaki, J.; Aldrich, R.W.; Jarnagin, !1K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:7724-7728 !$#title Expression cloning of a rat B-2 bradykinin receptor. !$#cross-references MUID:91352062; PMID:1715575 !$#accession A41283 !'##molecule_type mRNA !'##residues 1-366 ##label MCE !'##cross-references GB:M59967 REFERENCE A55079 !$#authors Pesquero, J.B.; Lindsey, C.J.; Zeh, K.; Paiva, A.C.M.; !1Ganten, D.; Bader, M. !$#journal J. Biol. Chem. (1994) 269:26920-26925 !$#title Molecular structure and expression of rat bradykinin B2 !1receptor gene. Evidence for alternative splicing. !$#cross-references MUID:95014558; PMID:7929432 !$#accession A55079 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-75,'A',77-366 ##label PES !'##cross-references GB:X80187; GB:X80188; GB:X80189; GB:X80190 REFERENCE S47529 !$#authors Wang, D.; Ma, J.; Chao, L.; Chao, J. !$#journal Biochim. Biophys. Acta (1994) 1219:171-174 !$#title Molecular cloning and sequence analysis of rat bradykinin B !1(2) receptor gene. !$#cross-references MUID:94368850; PMID:8086459 !$#accession S47529 !'##status preliminary !'##molecule_type DNA !'##residues 1-366 ##label WAN !'##cross-references EMBL:L26173; NID:g476749; PIDN:AAA62492.1; !1PID:g685244 COMMENT This G protein-coupled receptor binds the nonapeptide !1bradykinin. CLASSIFICATION #superfamily vertebrate rhodopsin KEYWORDS alternative splicing; G protein-coupled receptor; !1glycoprotein; lipoprotein; receptor; thiolester bond; !1transmembrane protein FEATURE !$31-48 #domain transmembrane #status predicted #label TM1\ !$79-96 #domain transmembrane #status predicted #label TM2\ !$107-126 #domain transmembrane #status predicted #label TM3\ !$154-170 #domain transmembrane #status predicted #label TM4\ !$197-215 #domain transmembrane #status predicted #label TM5\ !$245-261 #domain transmembrane #status predicted #label TM6\ !$3,14,182 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$105-186 #disulfide_bonds #status predicted\ !$326 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 366 #molecular-weight 41696 #checksum 8326 SEQUENCE /// ENTRY A37963 #type complete TITLE complement C5a anaphylatoxin receptor - human ORGANISM #formal_name Homo sapiens #common_name man DATE 22-Jan-1993 #sequence_revision 14-Feb-1997 #text_change 21-Jul-2000 ACCESSIONS A37963; S13646; I52417; S30518 REFERENCE A37963 !$#authors Boulay, F.; Mery, L.; Tardif, M.; Brouchon, L.; Vignais, P. !$#journal Biochemistry (1991) 30:2993-2999 !$#title Expression cloning of a receptor for C5a anaphylatoxin on !1differentiated HL-60 cells. !$#cross-references MUID:91175748; PMID:2007135 !$#accession A37963 !'##molecule_type mRNA !'##residues 1-350 ##label BOU !'##cross-references GB:J05327; NID:g179699; PIDN:AAA62831.1; !1PID:g179700 REFERENCE S13646 !$#authors Gerard, N.P.; Gerard, C. !$#journal Nature (1991) 349:614-617 !$#title The chemotactic receptor for human C5a anaphylatoxin. !$#cross-references MUID:91156029; PMID:1847994 !$#accession S13646 !'##molecule_type mRNA !'##residues 1-350 ##label GER !'##cross-references EMBL:X58674; NID:g29568; PIDN:CAB37830.1; !1PID:g4467832 REFERENCE I52417 !$#authors Gerard, N.P.; Bao, L.; Xiao-Ping, H.; Eddy, R.L. !$#journal Biochemistry (1993) 32:1243-1250 !$#title Human chemotaxis receptor genes cluster at 19q13.3-13.4. !1Characterization of the human C5a receptor gene. !$#cross-references MUID:93192225; PMID:8383526 !$#accession I52417 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-3 ##label RES !'##cross-references GB:S56556; GB:S56557; NID:g298577; NID:g298578 GENETICS !$#gene GDB:C5R1; C5A; C5AR !'##cross-references GDB:128856; OMIM:113995 !$#map_position 19q13.3-19q13.4 !$#introns 1/3 !$#note the list of introns may be incomplete FUNCTION !$#description mediates the inflammatory and chemotactic responses of !1polymorphonuclear neutrophils to C5a anaphylatoxin; !1stimulates chemotaxis, granule enzyme release, and !1superoxide anion production CLASSIFICATION #superfamily vertebrate rhodopsin KEYWORDS chemotaxis; G protein-coupled receptor; glycoprotein; !1inflammation; polymorphonuclear leukocyte; transmembrane !1protein FEATURE !$1-37 #domain extracellular #status predicted #label EX1\ !$38-61 #domain transmembrane #status predicted #label TM1\ !$62-71 #domain intracellular #status predicted #label IN1\ !$72-94 #domain transmembrane #status predicted #label TM2\ !$95-110 #domain extracellular #status predicted #label EX2\ !$111-132 #domain transmembrane #status predicted #label TM3\ !$133-149 #domain intracellular #status predicted #label IN2\ !$150-174 #domain transmembrane #status predicted #label TM4\ !$175-206 #domain extracellular #status predicted #label EX3\ !$207-227 #domain transmembrane #status predicted #label TM5\ !$228-242 #domain intracellular #status predicted #label IN3\ !$243-264 #domain transmembrane #status predicted #label TM6\ !$265-283 #domain extracellular #status predicted #label EX4\ !$284-307 #domain transmembrane #status predicted #label TM7\ !$308-350 #domain intracellular #status predicted #label IN4\ !$5 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 350 #molecular-weight 39320 #checksum 3557 SEQUENCE /// ENTRY S27357 #type complete TITLE complement C5a anaphylatoxin receptor - dog ORGANISM #formal_name Canis lupus familiaris #common_name dog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S27357 REFERENCE S27357 !$#authors Perret, J.J.; Raspe, E.; Vassart, G.; Parmentier, M. !$#journal Biochem. J. (1992) 288:911-917 !$#title Cloning and functional expression of the canine !1anaphylatoxin C5a receptor. Evidence for high interspecies !1variability. !$#cross-references MUID:93111969; PMID:1472004 !$#accession S27357 !'##status preliminary !'##molecule_type mRNA !'##residues 1-352 ##label PER !'##cross-references EMBL:X65860; NID:g878; PIDN:CAA46690.1; PID:g879 FUNCTION !$#description mediates the inflammatory and chemotactic responses of !1polymorphonuclear neutrophils to C5a anaphylatoxin; !1stimulates chemotaxis, granule enzyme release, and !1superoxide anion production CLASSIFICATION #superfamily vertebrate rhodopsin KEYWORDS chemotaxis; G protein-coupled receptor; glycoprotein; !1inflammation; polymorphonuclear leukocyte; transmembrane !1protein FEATURE !$1-38 #domain extracellular #status predicted #label EX1\ !$39-62 #domain transmembrane #status predicted #label TM1\ !$63-72 #domain intracellular #status predicted #label IN1\ !$73-95 #domain transmembrane #status predicted #label TM2\ !$96-111 #domain extracellular #status predicted #label EX2\ !$112-133 #domain transmembrane #status predicted #label TM3\ !$134-150 #domain intracellular #status predicted #label IN2\ !$151-175 #domain transmembrane #status predicted #label TM4\ !$176-208 #domain extracellular #status predicted #label EX3\ !$209-229 #domain transmembrane #status predicted #label TM5\ !$230-244 #domain intracellular #status predicted #label IN3\ !$245-266 #domain transmembrane #status predicted #label TM6\ !$267-285 #domain extracellular #status predicted #label EX4\ !$286-309 #domain transmembrane #status predicted #label TM7\ !$310-352 #domain intracellular #status predicted #label IN4\ !$5 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 352 #molecular-weight 39212 #checksum 9479 SEQUENCE /// ENTRY A46525 #type complete TITLE complement C5a anaphylatoxin receptor - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A46525 REFERENCE A46525 !$#authors Gerard, C.; Bao, L.; Orozco, O.; Pearson, M.; Kunz, D.; !1Gerard, N.P. !$#journal J. Immunol. (1992) 149:2600-2606 !$#title Structural diversity in the extracellular faces of !1peptidergic G-protein-coupled receptors. Molecular cloning !1of the mouse C5a anaphylatoxin receptor. !$#cross-references MUID:93017861; PMID:1401897 !$#accession A46525 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-351 ##label GER !'##cross-references GB:S46665; GB:L05630; NID:g257519; PIDN:AAB97774.1; !1PID:g257520 !'##experimental_source BALB/C !'##note sequence extracted from NCBI backbone (NCBIP:116075) FUNCTION !$#description mediates the inflammatory and chemotactic responses of !1polymorphonuclear neutrophils to C5a anaphylatoxin; !1stimulates chemotaxis, granule enzyme release, and !1superoxide anion production CLASSIFICATION #superfamily vertebrate rhodopsin KEYWORDS chemotaxis; G protein-coupled receptor; glycoprotein; !1inflammation; polymorphonuclear leukocyte; transmembrane !1protein FEATURE !$1-37 #domain extracellular #status predicted #label EX1\ !$38-61 #domain transmembrane #status predicted #label TM1\ !$62-71 #domain intracellular #status predicted #label IN1\ !$72-94 #domain transmembrane #status predicted #label TM2\ !$95-110 #domain extracellular #status predicted #label EX2\ !$111-132 #domain transmembrane #status predicted #label TM3\ !$133-149 #domain intracellular #status predicted #label IN2\ !$150-174 #domain transmembrane #status predicted #label TM4\ !$175-207 #domain extracellular #status predicted #label EX3\ !$208-228 #domain transmembrane #status predicted #label TM5\ !$229-243 #domain intracellular #status predicted #label IN3\ !$244-265 #domain transmembrane #status predicted #label TM6\ !$266-284 #domain extracellular #status predicted #label EX4\ !$285-308 #domain transmembrane #status predicted #label TM7\ !$309-351 #domain intracellular #status predicted #label IN4\ !$6 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 351 #molecular-weight 38954 #checksum 5965 SEQUENCE /// ENTRY QQBEQ4 #type complete TITLE G protein-coupled receptor homolog ECRF3 - saimiriine herpesvirus 1 (strain 11) ORGANISM #formal_name saimiriine herpesvirus 1 #note host Saimiri sciureus (common squirrel monkey) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 22-Jun-1999 ACCESSIONS S20245; H36813 REFERENCE S20243 !$#authors Nicholas, J.; Cameron, K.R.; Honess, R.W. !$#journal Nature (1992) 355:362-365 !$#title Herpesvirus saimiri encodes homologues of G protein-coupled !1receptors and cyclins. !$#cross-references MUID:92115001; PMID:1309943 !$#accession S20245 !'##molecule_type DNA !'##residues 1-321 ##label NIC !'##cross-references GB:S76368; NID:g243351; PIDN:AAB21117.1; !1PID:g243354 REFERENCE A36806 !$#authors Albrecht, J. !$#submission submitted to the EMBL Data Library, January 1992 !$#description Primary structure of the herpesvirus saimiri genome. !$#accession H36813 !'##molecule_type DNA !'##residues 1-321 ##label ALB !'##cross-references GB:X64346; NID:g60320; PIDN:CAA45697.1; PID:g60395 REFERENCE A37309 !$#authors Albrecht, J.C.; Nicholas, J.; Biller, D.; Cameron, K.R.; !1Biesinger, B.; Newman, C.; Wittmann, S.; Craxton, M.A.; !1Coleman, H.; Fleckenstein, B.; Honess, R.W. !$#journal J. Virol. (1992) 66:5047-5058 !$#title Primary structure of the herpesvirus saimiri genome. !$#cross-references MUID:92333688; PMID:1321287 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene ECRF3; 74 CLASSIFICATION #superfamily vertebrate rhodopsin KEYWORDS G protein-coupled receptor; glycoprotein; transmembrane !1protein FEATURE !$35-51 #domain transmembrane #status predicted #label TM1\ !$77-93 #domain transmembrane #status predicted #label TM2\ !$125-141 #domain transmembrane #status predicted #label TM3\ !$150-166 #domain transmembrane #status predicted #label TM4\ !$197-215 #domain transmembrane #status predicted #label TM5\ !$235-251 #domain transmembrane #status predicted #label TM6\ !$287-303 #domain transmembrane #status predicted #label TM7\ !$14,18,117 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 321 #molecular-weight 37132 #checksum 7611 SEQUENCE /// ENTRY QQBED3 #type complete TITLE HHRF3 protein - human cytomegalovirus (strain AD169) ALTERNATE_NAMES hypothetical protein US28; probable G protein-coupled receptor ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 22-Jun-1999 ACCESSIONS C27216; S09477; S09942 REFERENCE A92935 !$#authors Weston, K.; Barrell, B.G. !$#journal J. Mol. Biol. (1986) 192:177-208 !$#title Sequence of the short unique region, short repeats, and part !1of the long repeats of human cytomegalovirus. !$#cross-references MUID:87169717; PMID:3031311 !$#accession C27216 !'##molecule_type DNA !'##residues 1-323 ##label WES !'##cross-references EMBL:X04650; NID:g59801; PIDN:CAA28338.1; !1PID:g59807 REFERENCE S09322 !$#authors Chee, M.S.; Satchwell, S.C.; Preddie, E.; Weston, K.M.; !1Barrell, B.G. !$#journal Nature (1990) 344:774-777 !$#title Human cytomegalovirus encodes three G protein-coupled !1receptor homologues. !$#cross-references MUID:90231415; PMID:2158627 !$#accession S09477 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-323 ##label CHE REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09942 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-323 ##label CH2 !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35260.1; !1PID:g1780959 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1989 GENETICS !$#gene HHRF3 CLASSIFICATION #superfamily vertebrate rhodopsin KEYWORDS G protein-coupled receptor; glycoprotein; transmembrane !1protein FEATURE !$37-60 #domain transmembrane #status predicted #label TM1\ !$70-90 #domain transmembrane #status predicted #label TM2\ !$106-127 #domain transmembrane #status predicted #label TM3\ !$144-167 #domain transmembrane #status predicted #label TM4\ !$192-209 #domain transmembrane #status predicted #label TM5\ !$229-249 #domain transmembrane #status predicted #label TM6\ !$274-295 #domain transmembrane #status predicted #label TM7\ !$30 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 323 #molecular-weight 37188 #checksum 1404 SEQUENCE /// ENTRY QQBED2 #type complete TITLE HHRF2 protein - human cytomegalovirus (strain AD169) ALTERNATE_NAMES hypothetical protein US27; probable G protein-coupled receptor ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 22-Jun-1999 ACCESSIONS B27216; S09941; S09476 REFERENCE A92935 !$#authors Weston, K.; Barrell, B.G. !$#journal J. Mol. Biol. (1986) 192:177-208 !$#title Sequence of the short unique region, short repeats, and part !1of the long repeats of human cytomegalovirus. !$#cross-references MUID:87169717; PMID:3031311 !$#accession B27216 !'##molecule_type DNA !'##residues 1-362 ##label WES !'##cross-references EMBL:X04650; NID:g59801; PIDN:CAA28337.1; !1PID:g59806 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09941 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-362 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35259.1; !1PID:g1780958 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1989 REFERENCE S09322 !$#authors Chee, M.S.; Satchwell, S.C.; Preddie, E.; Weston, K.M.; !1Barrell, B.G. !$#journal Nature (1990) 344:774-777 !$#title Human cytomegalovirus encodes three G protein-coupled !1receptor homologues. !$#cross-references MUID:90231415; PMID:2158627 !$#accession S09476 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-328 ##label CH2 GENETICS !$#gene HHRF2 CLASSIFICATION #superfamily vertebrate rhodopsin KEYWORDS G protein-coupled receptor; glycoprotein; transmembrane !1protein FEATURE !$35-57 #domain transmembrane #status predicted #label TM1\ !$68-88 #domain transmembrane #status predicted #label TM2\ !$105-126 #domain transmembrane #status predicted #label TM3\ !$147-170 #domain transmembrane #status predicted #label TM4\ !$196-213 #domain transmembrane #status predicted #label TM5\ !$233-253 #domain transmembrane #status predicted #label TM6\ !$277-298 #domain transmembrane #status predicted #label TM7\ !$7,15,18,22 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 362 #molecular-weight 41994 #checksum 852 SEQUENCE /// ENTRY QQBET9 #type complete TITLE protein UL33 - human cytomegalovirus (strain AD169) ALTERNATE_NAMES probable G protein-coupled receptor ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS S09796; S09322 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09796 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-390 ##label CHE1 !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35432.1; !1PID:g59638 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1989 REFERENCE S09322 !$#authors Chee, M.S.; Satchwell, S.C.; Preddie, E.; Weston, K.M.; !1Barrell, B.G. !$#journal Nature (1990) 344:774-777 !$#title Human cytomegalovirus encodes three G protein-coupled !1receptor homologues. !$#cross-references MUID:90231415; PMID:2158627 !$#accession S09322 !'##molecule_type DNA !'##residues 1-390 ##label CHE2 !'##cross-references EMBL:X53293; NID:g59460; PIDN:CAA37385.1; !1PID:g59461 CLASSIFICATION #superfamily vertebrate rhodopsin KEYWORDS G protein-coupled receptor; transmembrane protein FEATURE !$13-37 #domain transmembrane #status predicted #label TM1\ !$48-68 #domain transmembrane #status predicted #label TM2\ !$84-105 #domain transmembrane #status predicted #label TM3\ !$124-150 #domain transmembrane #status predicted #label TM4\ !$184-206 #domain transmembrane #status predicted #label TM5\ !$223-244 #domain transmembrane #status predicted #label TM6\ !$271-289 #domain transmembrane #status predicted #label TM7 SUMMARY #length 390 #molecular-weight 43804 #checksum 4421 SEQUENCE /// ENTRY OOOCG #type complete TITLE rhodopsin - giant octopus ORGANISM #formal_name Octopus dofleini #common_name giant octopus DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 05-Jun-1998 ACCESSIONS S00610 REFERENCE S00610 !$#authors Ovchinnikov, Y.A.; Abdulaev, N.G.; Zolotarev, A.S.; !1Artamonov, I.D.; Bespalov, I.A.; Dergachev, A.E.; Tsuda, M. !$#journal FEBS Lett. (1988) 232:69-72 !$#title Octopus rhodopsin. Amino acid sequence deduced from cDNA. !$#cross-references MUID:88211878; PMID:3366250 !$#accession S00610 !'##molecule_type mRNA !'##residues 1-455 ##label OVC !'##cross-references EMBL:X07797 !'##note the source is designated as Paroctopus defleini !'##note part of this sequence was confirmed by protein sequencing CLASSIFICATION #superfamily octopus rhodopsin KEYWORDS chromoprotein; color vision; G protein-coupled receptor; !1glycoprotein; lipoprotein; photoreceptor; retinal; !1thiolester bond; transmembrane protein FEATURE !$37-61 #domain transmembrane #status predicted #label TM1\ !$74-98 #domain transmembrane #status predicted #label TM2\ !$107-131 #domain transmembrane #status predicted #label TM3\ !$153-177 #domain transmembrane #status predicted #label TM4\ !$201-224 #domain transmembrane #status predicted #label TM5\ !$263-286 #domain transmembrane #status predicted #label TM6\ !$302-323 #domain transmembrane #status predicted #label TM7\ !$9,15 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$306 #binding_site retinal (Lys) (covalent) #status !8predicted\ !$337,338 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 455 #molecular-weight 50457 #checksum 6535 SEQUENCE /// ENTRY S60755 #type fragment TITLE rhodopsin - Alloteuthis subulata (fragment) ORGANISM #formal_name Alloteuthis subulata DATE 19-Mar-1997 #sequence_revision 01-Aug-1997 #text_change 22-Jun-1999 ACCESSIONS S60755; S60756; S71931 REFERENCE S60755 !$#authors Morris, A.; Bowmaker, J.K.; Hunt, D.M. !$#journal Proc. R. Soc. Lond. B Biol. Sci. (1993) 254:233-240 !$#title The molecular basis of a spectral shift in the rhodopsins of !1two species of squid from different photic environments. !$#cross-references MUID:94151381; PMID:8108455 !$#accession S60755 !'##molecule_type DNA !'##residues 1-440 ##label MOR !$#accession S60756 !'##molecule_type DNA !'##residues 1-113,'M',115-130,'G',132-149,'I',151-440 ##label MO2 REFERENCE S71931 !$#authors Hunt, D.M. !$#submission submitted to the EMBL Data Library, April 1995 !$#accession S71931 !'##molecule_type DNA !'##residues 1-383;385-407;409-421,'P',422-440 ##label HUN !'##cross-references EMBL:Z49108; NID:g790974; PIDN:CAA88923.1; !1PID:g793769 GENETICS !$#introns #status absent CLASSIFICATION #superfamily octopus rhodopsin KEYWORDS chromoprotein; color vision; G protein-coupled receptor; !1glycoprotein; lipoprotein; photoreceptor; retinal; !1thiolester bond; transmembrane protein FEATURE !$29-53 #domain transmembrane #status predicted #label TM1\ !$66-90 #domain transmembrane #status predicted #label TM2\ !$99-123 #domain transmembrane #status predicted #label TM3\ !$145-169 #domain transmembrane #status predicted #label TM4\ !$193-216 #domain transmembrane #status predicted #label TM5\ !$255-278 #domain transmembrane #status predicted #label TM6\ !$294-315 #domain transmembrane #status predicted #label TM7\ !$1 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$298 #binding_site retinal (Lys) (covalent) #status !8predicted\ !$329,330 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 440 #checksum 8464 SEQUENCE /// ENTRY S14332 #type complete TITLE rhodopsin - northern European squid ORGANISM #formal_name Loligo forbesi #common_name northern European squid DATE 13-Jan-1995 #sequence_revision 13-Jan-1995 #text_change 22-Jun-1999 ACCESSIONS S14332 REFERENCE S14332 !$#authors Hall, M.D.; Hoon, M.A.; Ryba, N.J.P.; Pottinger, J.D.D.; !1Keen, J.N.; Saibil, H.R.; Findlay, J.B.C. !$#journal Biochem. J. (1991) 274:35-40 !$#title Molecular cloning and primary structure of squid (Loligo !1forbesi) rhodopsin, a phospholipase C-directed !1G-protein-linked receptor. !$#cross-references MUID:91158727; PMID:1900420 !$#accession S14332 !'##status preliminary !'##molecule_type mRNA !'##residues 1-452 ##label HAL !'##cross-references EMBL:X56788; NID:g9513; PIDN:CAA40108.1; !1PID:g603851 CLASSIFICATION #superfamily octopus rhodopsin KEYWORDS chromoprotein; color vision; G protein-coupled receptor; !1glycoprotein; lipoprotein; photoreceptor; retinal; !1thiolester bond; transmembrane protein FEATURE !$36-60 #domain transmembrane #status predicted #label TM1\ !$73-97 #domain transmembrane #status predicted #label TM2\ !$106-130 #domain transmembrane #status predicted #label TM3\ !$152-176 #domain transmembrane #status predicted #label TM4\ !$200-223 #domain transmembrane #status predicted #label TM5\ !$262-285 #domain transmembrane #status predicted #label TM6\ !$301-322 #domain transmembrane #status predicted #label TM7\ !$8 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$305 #binding_site retinal (Lys) (covalent) #status !8predicted\ !$336,337 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 452 #molecular-weight 50576 #checksum 6002 SEQUENCE /// ENTRY S29483 #type complete TITLE rhodopsin [similarity] - Japanese flying squid ALTERNATE_NAMES visual pigment protein ORGANISM #formal_name Todarodes pacificus #common_name Japanese flying squid DATE 13-Jan-1995 #sequence_revision 13-Jan-1995 #text_change 21-Jul-2000 ACCESSIONS S29483; PT0063 REFERENCE S29483 !$#authors Hara-Nishimura, I.; Kondo, M.; Nishimura, M.; Hara, R.; !1Hara, T. !$#journal FEBS Lett. (1993) 317:5-11 !$#title Cloning and nucleotide sequence of cDNA for rhodopsin of the !1squid Todarodes pacificus. !$#cross-references MUID:93154520; PMID:8428633 !$#accession S29483 !'##status preliminary !'##molecule_type mRNA !'##residues 1-448 ##label HAR !'##cross-references EMBL:X70498; NID:g397389; PIDN:CAA49906.1; !1PID:g397390 REFERENCE PT0063 !$#authors Seidou, M.; Kubota, I.; Hiraki, K.; Kito, Y. !$#journal Biochim. Biophys. Acta (1988) 957:318-321 !$#title Amino acid sequence of the retinal binding site of squid !1visual pigment. !$#cross-references MUID:89051045; PMID:3191148 !$#accession PT0063 !'##molecule_type protein !'##residues 303-313 ##label SEI CLASSIFICATION #superfamily octopus rhodopsin KEYWORDS chromoprotein; color vision; G protein-coupled receptor; !1glycoprotein; lipoprotein; photoreceptor; retinal; !1thiolester bond; transmembrane protein FEATURE !$36-60 #domain transmembrane #status predicted #label TM1\ !$73-97 #domain transmembrane #status predicted #label TM2\ !$106-130 #domain transmembrane #status predicted #label TM3\ !$152-176 #domain transmembrane #status predicted #label TM4\ !$200-223 #domain transmembrane #status predicted #label TM5\ !$262-285 #domain transmembrane #status predicted #label TM6\ !$301-322 #domain transmembrane #status predicted #label TM7\ !$8,14 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$305 #binding_site retinal (Lys) (covalent) #status !8experimental\ !$336,337 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 448 #molecular-weight 49836 #checksum 3526 SEQUENCE /// ENTRY QRHUFT #type complete TITLE follitropin receptor precursor - human ALTERNATE_NAMES follicle stimulating hormone receptor (FSHR) CONTAINS follitropin receptor precursor long splice form; follitropin receptor precursor short splice form ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1991 #sequence_revision 06-Sep-1996 #text_change 22-Jun-1999 ACCESSIONS I57661; I56448; PC1147; S30560; I57672; JN0122 REFERENCE I57661 !$#authors Gromoll, J.; Dankbar, B.; Gudermann, T. !$#journal Mol. Cell. Endocrinol. (1994) 102:93-102 !$#title Characterization of the 5' flanking region of the human !1follicle-stimulating hormone receptor gene. !$#cross-references MUID:95011044; PMID:7926278 !$#accession I57661 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-51 ##label GRO !'##cross-references GB:S73199; NID:g685036; PIDN:AAB32071.1; !1PID:g685037 REFERENCE I56448 !$#authors Gromoll, J.; Ried, T.; Holtgreve-Grez, H.; Nieschlag, E.; !1Gudermann, T. !$#journal J. Mol. Endocrinol. (1994) 12:265-271 !$#title Localization of the human FSH receptor to chromosome 2 p21 !1using a genomic probe comprising exon 10. !$#cross-references MUID:95000244; PMID:7916967 !$#accession I56448 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 286-695 ##label GR2 !'##cross-references GB:S73526; NID:g688069; PIDN:AAB32225.1; !1PID:g688070 REFERENCE PC1147 !$#authors Gromoll, J.; Gudermann, T.; Nieschlag, E. !$#journal Biochem. Biophys. Res. Commun. (1992) 188:1077-1083 !$#title Molecular cloning of a truncated isoform of the human !1follicle stimulating hormone receptor. !$#cross-references MUID:93075197; PMID:1359889 !$#accession PC1147 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-223,286-294,'P',296-342 ##label GR3 !'##cross-references EMBL:X68044; NID:g31473; PIDN:CAA48179.1; !1PID:g31474 !'##experimental_source testis REFERENCE S30560 !$#authors Gromoll, J. !$#submission submitted to the EMBL Data Library, August 1992 !$#accession S30560 !'##molecule_type mRNA !'##residues 1-12,'R',14-223,286-294,'P',296-342 ##label GR4 !'##cross-references EMBL:X68044; NID:g31473; PIDN:CAA48179.1; !1PID:g31474 REFERENCE I57672 !$#authors Kelton, C.A.; Cheng, S.V.; Nugent, N.P.; Schweickhardt, !1R.L.; Rosenthal, J.L.; Overton, S.A.; Wands, G.D.; Kuzeja, !1J.B.; Luchette, C.A.; Chappel, S.C. !$#journal Mol. Cell. Endocrinol. (1992) 89:141-151 !$#title The cloning of the human follicle stimulating hormone !1receptor and its expression in COS-7, CHO, and Y-1 cells. !$#cross-references MUID:93246012; PMID:1301382 !$#accession I57672 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-679,'N',681-695 ##label KEL !'##cross-references GB:S59900; NID:g300072; PIDN:AAB26480.1; !1PID:g300073 REFERENCE JN0122 !$#authors Minegish, T.; Nakamura, K.; Takakura, Y.; Ibuki, Y.; !1Igarashi, M. !$#journal Biochem. Biophys. Res. Commun. (1991) 175:1125-1130 !$#title Cloning and sequencing of human FSH receptor cDNA. !$#cross-references MUID:91222171; PMID:1709010 !$#accession JN0122 !'##molecule_type mRNA !'##residues 1-111,'T',113-196,'AV',199-306,'A',308-695 ##label MIN !'##cross-references EMBL:M65085; NID:g182770; PIDN:AAA52477.1; !1PID:g182771 GENETICS !$#gene GDB:FSHR !'##cross-references GDB:127510; OMIM:136435 !$#map_position 2p21-2p16 !$#introns 223/3 !$#note the exact position of the intron cannot be determined from !1the experimental data FUNCTION !$#description receptor that mediates the biochemical effects of !1follitropin CLASSIFICATION #superfamily glycoprotein hormone receptor; leucine-rich !1alpha-2-glycoprotein repeat homology KEYWORDS alternative splicing; G protein-coupled receptor; !1glycoprotein; hormone receptor; phosphoprotein; !1transmembrane protein FEATURE !$1-695 #product follitropin receptor precursor, long splice !8form #status predicted #label SPL1\ !$1-223,286-695 #product follitropin receptor precursor, short splice !8form #status predicted #label SPL2\ !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-695 #product follitropin receptor #status predicted !8#label MAT\ !$16-366 #domain extracellular hormone binding #status !8predicted #label EHB\ !$56-70 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR1\ !$71-95 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR2\ !$96-120 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR3\ !$121-145 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR4\ !$146-169 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR5\ !$172-193 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR6\ !$194-218 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR7\ !$367-387 #domain transmembrane #status predicted #label TM1\ !$398-421 #domain transmembrane #status predicted #label TM2\ !$444-465 #domain transmembrane #status predicted #label TM3\ !$486-508 #domain transmembrane #status predicted #label TM4\ !$529-550 #domain transmembrane #status predicted #label TM5\ !$574-597 #domain transmembrane #status predicted #label TM6\ !$609-630 #domain transmembrane #status predicted #label TM7\ !$191,199,293,318 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$555 #binding_site phosphate (Thr) (covalent) (by protein !8kinase C) #status predicted\ !$596 #binding_site phosphate (Ser) (covalent) (by protein !8kinase C) #status predicted SUMMARY #length 695 #molecular-weight 78267 #checksum 2066 SEQUENCE /// ENTRY JN0898 #type complete TITLE follitropin receptor precursor - crab-eating macaque ALTERNATE_NAMES follicle-stimulating hormone receptor (FSHR) ORGANISM #formal_name Macaca fascicularis #common_name crab-eating macaque DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JN0898; S36452 REFERENCE JN0898 !$#authors Gromoll, J.; Dankbar, B.; Sharma, R.S.; Nieschlag, E. !$#journal Biochem. Biophys. Res. Commun. (1993) 196:1066-1072 !$#title Molecular cloning of the testicular follicle stimulating !1hormone receptor of the non human primate Macaca !1fascicularis and identification of multiple transcripts in !1the testis. !$#cross-references MUID:94071854; PMID:7504463 !$#accession JN0898 !'##molecule_type mRNA !'##residues 1-695 ##label GRO !'##cross-references EMBL:X74454; NID:g396801; PIDN:CAA52463.1; !1PID:g396802 !'##note the authors translated the codon AGT for residue 488 as Arg FUNCTION !$#description receptor that mediates the biochemical effects of !1follitropin CLASSIFICATION #superfamily glycoprotein hormone receptor; leucine-rich !1alpha-2-glycoprotein repeat homology KEYWORDS G protein-coupled receptor; glycoprotein; hormone receptor; !1phosphoprotein; pituitary; transmembrane protein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-695 #product follitropin receptor #status predicted !8#label PFH\ !$71-95 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR2\ !$96-120 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR3\ !$121-145 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR4\ !$146-169 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR5\ !$172-193 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR6\ !$194-218 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR7\ !$367-387 #domain transmembrane #status predicted #label TM1\ !$399-421 #domain transmembrane #status predicted #label TM2\ !$444-465 #domain transmembrane #status predicted #label TM3\ !$486-508 #domain transmembrane #status predicted #label TM4\ !$529-550 #domain transmembrane #status predicted #label TM5\ !$574-597 #domain transmembrane #status predicted #label TM6\ !$609-630 #domain transmembrane #status predicted #label TM7\ !$191,199,293,318 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$555 #binding_site phosphate (Thr) (covalent) (by protein !8kinase C) #status predicted\ !$596 #binding_site phosphate (Ser) (covalent) (by protein !8kinase C) #status predicted SUMMARY #length 695 #molecular-weight 78343 #checksum 1011 SEQUENCE /// ENTRY QRHUUT #type complete TITLE lutropin-choriogonadotropin receptor precursor - human ALTERNATE_NAMES luteinizing hormone-choriogonadotropin receptor CONTAINS lutropin-choriogonadotropin receptor precursor long splice form; lutropin-choriogonadotropin receptor precursor short splice form ORGANISM #formal_name Homo sapiens #common_name man DATE 22-Jan-1993 #sequence_revision 16-Feb-1996 #text_change 22-Jun-1999 ACCESSIONS A36243; B36243; A23728; B36120 REFERENCE A36243 !$#authors Minegish, T.; Nakamura, K.; Takakura, Y.; Miyamoto, K.; !1Hasegawa, Y.; Ibuki, Y.; Igarashi, M. !$#journal Biochem. Biophys. Res. Commun. (1990) 172:1049-1054 !$#title Cloning and sequencing of human LH/hCG receptor cDNA. !$#cross-references MUID:91058534; PMID:2244890 !$#accession A36243 !'##molecule_type mRNA !'##residues 1-699 ##label MIN !'##cross-references GB:M63108; NID:g187135; PIDN:AAA59515.1; !1PID:g187136 !'##experimental_source ovary !$#accession B36243 !'##molecule_type mRNA !'##residues 1-226,290-699 ##label MI2 REFERENCE A23728 !$#authors Jia, X.C.; Oikawa, M.; Bo, M.; Tanaka, T.; Ny, T.; Boime, !1I.; Hsueh, A.J.W. !$#journal Mol. Endocrinol. (1991) 5:759-768 !$#title Expression of human luteinizing hormone (LH) receptor: !1interaction with LH and chorionic gonadotropin from human !1but not equine, rat, and ovine species. !$#cross-references MUID:92017881; PMID:1922095 !$#accession A23728 !'##molecule_type mRNA !'##residues 1-123,'R',125-311,'N',313-699 ##label JIA !'##cross-references GB:S57793 !'##experimental_source ovary granulosa and luteal cells; thyroid !'##note 312-Ser was also found; the authors translated the codon UAC !1for residue 546 as Thr !'##note mRNA from the thyroid is incompletely processed compared with !1that from the ovary REFERENCE A36120 !$#authors Frazier, A.L.; Robbins, L.S.; Stork, P.J.; Sprengel, R.; !1Segaloff, D.L.; Cone, R.D. !$#journal Mol. Endocrinol. (1990) 4:1264-1276 !$#title Isolation of TSH and LH/CG receptor cDNAs from human !1thyroid: regulation by tissue specific splicing. !$#cross-references MUID:91155962; PMID:2293030 !$#accession B36120 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-6,'P',8-18,'A',20-26,'R',29-43,'A',45,'A',47,'RPS',52-67, !1'S',69-123,'R',125-261,'KQ',264-269,'R',271-273,'H',275-289, !1'L',291-310,324-447,'L',449-539,'L',541-648,'DP',650-699 !1##label FRA !'##cross-references GB:M73746; NID:g903745; PIDN:AAA70231.1; !1PID:g903746 !'##experimental_source thyroid REFERENCE A57564 !$#authors Zhu, H.; Wang, H.; Ascoli, M. !$#journal Mol. Endocrinol. (1995) 9:141-150 !$#title The lutropin/choriogonadotropin receptor is palmitoylated at !1intracellular cysteine residues. !$#cross-references MUID:95295727; PMID:7776964 !$#contents annotation; mutation analysis of palmitate binding sites GENETICS !$#gene GDB:LHCGR !'##cross-references GDB:125260; OMIM:152790 !$#map_position 2p21-2p21 !$#introns 226/3 !$#note the exact position of the intron cannot be determined from !1the experimental data CLASSIFICATION #superfamily glycoprotein hormone receptor; leucine-rich !1alpha-2-glycoprotein repeat homology KEYWORDS alternative splicing; G protein-coupled receptor; !1glycoprotein; hormone receptor; lipoprotein; phosphoprotein; !1thiolester bond; transmembrane protein FEATURE !$1-699 #product lutropin-choriogonadotropin receptor !8precursor, long splice form #status predicted #label !8SPL1\ !$1-226,290-699 #product lutropin-choriogonadotropin receptor !8precursor, short splice form #status predicted #label !8SPL2\ !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-644 #product lutropin-choriogonadotropin receptor #status !8predicted #label MAT\ !$23-363 #domain extracellular hormone binding #status !8predicted #label EHB\ !$50-73 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR1\ !$74-98 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR2\ !$99-123 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR3\ !$124-148 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR4\ !$149-173 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR5\ !$176-197 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR6\ !$198-222 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR7\ !$364-385 #domain transmembrane #status predicted #label TM1\ !$396-418 #domain transmembrane #status predicted #label TM2\ !$441-462 #domain transmembrane #status predicted #label TM3\ !$483-505 #domain transmembrane #status predicted #label TM4\ !$526-547 #domain transmembrane #status predicted #label TM5\ !$571-594 #domain transmembrane #status predicted #label TM6\ !$606-627 #domain transmembrane #status predicted #label TM7\ !$645-699 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$99,174,195,291,299, !$313 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$561,677 #binding_site phosphate (Thr) (covalent) (by protein !8kinase C) #status predicted\ !$643,644 #binding_site palmitate (Cys) (covalent) #status !8experimental\ !$670 #binding_site phosphate (Ser) (covalent) (by protein !8kinase C) #status predicted SUMMARY #length 699 #molecular-weight 78516 #checksum 6256 SEQUENCE /// ENTRY QRHURH #type complete TITLE thyrotropin receptor precursor - human ALTERNATE_NAMES thyroid stimulatory hormone receptor (TSHR) ORGANISM #formal_name Homo sapiens #common_name man DATE 22-Jan-1993 #sequence_revision 01-Mar-1996 #text_change 22-Jun-1999 ACCESSIONS A33789; A33786; A34052; A36120; S38280 REFERENCE A33789 !$#authors Libert, F.; Lefort, A.; Gerard, C.; Parmentier, M.; Perret, !1J.; Ludgate, M.; Dumont, J.E.; Vassart, G. !$#journal Biochem. Biophys. Res. Commun. (1989) 165:1250-1255 !$#title Cloning, sequencing and expression of the human thyrotropin !1(TSH) receptor: evidence for binding of autoantibodies. !$#cross-references MUID:90121232; PMID:2610690 !$#accession A33789 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type mRNA !'##residues 1-86,'L',88-764 ##label LIB REFERENCE A33786 !$#authors Nagayama, Y.; Kaufman, K.D.; Seto, P.; Rapoport, B. !$#journal Biochem. Biophys. Res. Commun. (1989) 165:1184-1190 !$#title Molecular cloning, sequence and functional expression of the !1cDNA for the human thyrotropin receptor. !$#cross-references MUID:90121223; PMID:2558651 !$#accession A33786 !'##molecule_type mRNA !'##residues 1-600,'H',602-764 ##label NAG !'##cross-references GB:M31774; NID:g340003; PIDN:AAA36783.1; !1PID:g340004 REFERENCE A34052 !$#authors Misrahi, M.; Loosfelt, H.; Atger, M.; Sar, S.; !1Guiochon-Mantel, A.; Milgrom, E. !$#journal Biochem. Biophys. Res. Commun. (1990) 166:394-403 !$#title Cloning, sequencing and expression of human TSH receptor. !$#cross-references MUID:90147730; PMID:2302212 !$#accession A34052 !'##molecule_type mRNA !'##residues 1-726,'E',728-743,'K',745-764 ##label MIS !'##cross-references GB:M32215; NID:g307524; PIDN:AAA61236.1; !1PID:g307525 !'##note 13-Pro, 260-Pro, 414-His, 500-Leu, 634-Leu, 727-Asp, and !1744-Asn were also found REFERENCE A36120 !$#authors Frazier, A.L.; Robbins, L.S.; Stork, P.J.; Sprengel, R.; !1Segaloff, D.L.; Cone, R.D. !$#journal Mol. Endocrinol. (1990) 4:1264-1276 !$#title Isolation of TSH and LH/CG receptor cDNAs from human !1thyroid: regulation by tissue specific splicing. !$#cross-references MUID:91155962; PMID:2293030 !$#accession A36120 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-129,'S',131,'AFS',135-195,'D',197,'F',199-256,'S', !1258-263,'A',265-305,'IET',309-527,'A',529-611,'H',614-634, !1'T',636-644,'V',646-668,'I',670-764 ##label FRA !'##cross-references GB:M73747; NID:g903759; PIDN:AAA70232.1; !1PID:g903760 REFERENCE S38280 !$#authors Parma, J.; Duprez, L.; van Sande, J.; Cochaux, P.; Gervy, !1C.; Mockel, J.; Dumont, J.; Vassart, G. !$#journal Nature (1993) 365:649-651 !$#title Somatic mutations in the thyrotropin receptor gene cause !1hyperfunctioning thyroid adenomas. !$#cross-references MUID:94019814; PMID:8413627 !$#accession S38280 !'##molecule_type DNA !'##residues 615-642 ##label PAR !'##experimental_source thyroid adenomas !'##note mutations to Cys-619 or to Ile-623 in hyperfunctioning thyroid !1adenomas cause constitutive activation of G protein mediated !1adenyl cyclase COMMENT See PIR:JC1319 for a splice form of thyrotropin receptor !1which lacks the seven transmembrane domains at the carboxyl !1terminal. GENETICS !$#gene GDB:TSHR !'##cross-references GDB:125313; OMIM:275200 !$#map_position 14q31-14q31 !$#introns 231/2 !$#note the list of introns is incomplete; the eighth of eight !1introns is shown FUNCTION !$#description receptor that mediates the biochemical effects of !1thyrotropin CLASSIFICATION #superfamily glycoprotein hormone receptor; leucine-rich !1alpha-2-glycoprotein repeat homology KEYWORDS alternative splicing; G protein-coupled receptor; !1glycoprotein; hormone receptor; phosphoprotein; thyroid !1gland; transmembrane protein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-764 #product thyrotropin receptor #status predicted !8#label MAT\ !$53-76 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR1\ !$77-101 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR2\ !$102-126 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR3\ !$127-151 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR4\ !$152-176 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR5\ !$179-200 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR6\ !$201-226 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR7\ !$419-440 #domain transmembrane #status predicted #label TM1\ !$451-473 #domain transmembrane #status predicted #label TM2\ !$496-517 #domain transmembrane #status predicted #label TM3\ !$538-560 #domain transmembrane #status predicted #label TM4\ !$580-602 #domain transmembrane #status predicted #label TM5\ !$626-649 #domain transmembrane #status predicted #label TM6\ !$661-682 #domain transmembrane #status predicted #label TM7\ !$77,99,113,177,198, !$302 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 764 #molecular-weight 86829 #checksum 260 SEQUENCE /// ENTRY JC1319 #type complete TITLE thyrotropin receptor precursor, short splice form - human ALTERNATE_NAMES circulating thyrotropin binding protein; thyroid stimulating hormone receptor (TSHR) V1.3 ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1993 #sequence_revision 01-Mar-1996 #text_change 21-Jul-2000 ACCESSIONS JC1319; JQ1618 REFERENCE JC1319 !$#authors Takeshita, A.; Nagayama, Y.; Fujiyama, K.; Yokoyama, N.; !1Namba, H.; Yamashita, S.; Izumi, M.; Nagataki, S. !$#journal Biochem. Biophys. Res. Commun. (1992) 188:1214-1219 !$#title Molecular cloning and sequencing of an alternatively spliced !1form of the human thyrotropin receptor transcript. !$#cross-references MUID:93075216; PMID:1445355 !$#accession JC1319 !'##molecule_type mRNA !'##residues 1-253 ##label TAK !'##cross-references GB:S49816; NID:g260246; PIDN:AAB24246.1; !1PID:g260247 REFERENCE JQ1618 !$#authors Graves, P.N.; Tomer, Y.; Davies, T.F. !$#journal Biochem. Biophys. Res. Commun. (1992) 187:1135-1143 !$#title Cloning and sequencing of a 1.3 KB variant of human !1thyrotropin receptor mRNA lacking the transmembrane domain. !$#cross-references MUID:92412080; PMID:1530609 !$#accession JQ1618 !'##molecule_type mRNA !'##residues 1-238,'L',240-247,'S',249-250,'T',252-253 ##label GRA !'##cross-references GB:S45272; NID:g256170; PIDN:AAB23390.2; !1PID:g5705928 !'##note the authors translated the codon TAT for residue 195 as Gly, !1GCT for residue 196 as Val, and omitted the translation for !1253-Ser COMMENT This splice form of thyrotropin receptor (see PIR:QRHURH) !1which lacks the seven transmembrane domains at the carboxyl !1terminal probably functions as a plasma thyrotropin binding !1protein. GENETICS !$#gene GDB:TSHR !'##cross-references GDB:125313; OMIM:275200 !$#map_position 14q31-14q31 !$#introns 231/2 !$#note the list of introns is incomplete; the eighth of eight !1introns is shown CLASSIFICATION #superfamily glycoprotein hormone receptor; leucine-rich !1alpha-2-glycoprotein repeat homology KEYWORDS alternative splicing; G protein-coupled receptor; !1glycoprotein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-253 #product thyrotropin receptor short splice form !8#status predicted #label MAT\ !$53-76 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR1\ !$77-101 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR2\ !$102-126 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR3\ !$127-151 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR4\ !$152-176 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR5\ !$179-200 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR6\ !$201-226 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR7\ !$201-211 #region thyrotropin binding #status predicted\ !$222-230 #region thyrotropin binding #status predicted\ !$77,99,113,177,198 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 253 #molecular-weight 28461 #checksum 5516 SEQUENCE /// ENTRY A35618 #type complete TITLE HDEL receptor ERD2 - yeast (Kluyveromyces marxianus var. lactis) ALTERNATE_NAMES 26K endoplasmic reticulum retention receptor ORGANISM #formal_name Kluyveromyces marxianus var. lactis, Candida sphaerica DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A35618 REFERENCE A35618 !$#authors Lewis, M.J.; Sweet, D.J.; Pelham, H.R.B. !$#journal Cell (1990) 61:1359-1363 !$#title The ERD2 gene determines the specificity of the luminal ER !1protein retention system. !$#cross-references MUID:90304894; PMID:2194671 !$#accession A35618 !'##molecule_type DNA !'##residues 1-219 ##label LEW !'##cross-references GB:M34844; NID:g173268; PIDN:AAA35253.1; !1PID:g173269 FUNCTION !$#description achieves retention of proteins specific to the lumen of the !1endoplasmic reticulum by retrieving them from the cis-Golgi; !1binding is mediated through the carboxyl-terminal !1tetrapeptide, usually KDEL in animal cells and HDEL in !1budding yeasts CLASSIFICATION #superfamily KDEL receptor KEYWORDS Golgi apparatus; protein trafficking; sorting signal !1recognition; transmembrane protein SUMMARY #length 219 #molecular-weight 25850 #checksum 4708 SEQUENCE /// ENTRY A35617 #type complete TITLE HDEL receptor ERD2 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES 26K endoplasmic reticulum retention receptor; ER lumen protein-retaining receptor ERD2; protein YBL0408; protein YBL040c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A35617; S45774; S50290; S42504 REFERENCE A35617 !$#authors Semenza, J.C.; Hardwick, K.G.; Dean, N.; Pelham, H.R.B. !$#journal Cell (1990) 61:1349-1357 !$#title ERD2, a yeast gene required for the receptor-mediated !1retrieval of luminal ER proteins from the secretory pathway. !$#cross-references MUID:90304893; PMID:2194670 !$#accession A35617 !'##molecule_type DNA !'##residues 1-219 ##label SEM !'##cross-references GB:M34777; NID:g171466; PIDN:AAA68907.1; !1PID:g171467 REFERENCE S45745 !$#authors Goffeau, A.; Jonniaux, J.L.; Purnelle, B.; Skala, J.; de !1Wergifosse, P.; van Dyck, L. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S45774 !'##molecule_type DNA !'##residues 1-219 ##label GOF !'##cross-references EMBL:Z35801; NID:g536054; PIDN:CAA84860.1; !1PID:g536055; GSPDB:GN00002; MIPS:YBL040c REFERENCE S50284 !$#authors de Wergifosse, P.; Jacques, B.; Jonniaux, J.L.; Purnelle, !1B.; Skala, J.; Goffeau, A. !$#journal Yeast (1994) 10:1489-1496 !$#title The sequence of a 22.4 kb DNA fragment from the left arm of !1yeast chromosome II reveals homologues to bacterial proline !1synthetase and murine alpha-adaptin, as well as a new !1permease and a DNA-binding protein. !$#cross-references MUID:95176707; PMID:7871888 !$#accession S50290 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 64-219 ##label DEF !'##cross-references EMBL:X78214; NID:g463261; PIDN:CAA55054.1; !1PID:g463268 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1March 1994 GENETICS !$#gene SGD:ERD2; MIPS:YBL040c !'##cross-references SGD:S0000136; MIPS:YBL040c !$#map_position 2L !$#introns 8/1 FUNCTION !$#description achieves retention of proteins specific to the lumen of the !1endoplasmic reticulum by retrieving them from the cis-Golgi; !1binding is mediated through the carboxyl-terminal !1tetrapeptide, usually KDEL in animal cells and HDEL in !1budding yeasts CLASSIFICATION #superfamily KDEL receptor KEYWORDS Golgi apparatus; protein trafficking; sorting signal !1recognition; transmembrane protein FEATURE !$4-20 #domain transmembrane #status predicted #label TM1\ !$38-54 #domain transmembrane #status predicted #label TM2\ !$61-82 #domain transmembrane #status predicted #label TM3\ !$99-115 #domain transmembrane #status predicted #label TM4\ !$122-138 #domain transmembrane #status predicted #label TM5\ !$186-202 #domain transmembrane #status predicted #label TM6 SUMMARY #length 219 #molecular-weight 25762 #checksum 3620 SEQUENCE /// ENTRY VICH #type complete TITLE avidin precursor [validated] - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 24-Apr-1984 #sequence_revision 04-Nov-1994 #text_change 15-Sep-2000 ACCESSIONS A54975; A27518; A92093; A92092; A03160 REFERENCE A54975 !$#authors Wallen, M.J.; Laukkanen, M.O.; Kulomaa, M.S. !$#submission submitted to GenBank, January 1994 !$#description Sequence of the chicken egg-white avidin gene. !$#accession A54975 !'##molecule_type DNA !'##residues 1-21,'S',23-152 ##label WAL !'##cross-references GB:L27818; NID:g450255; PID:g451889 !'##experimental_source adult oviduct, strain White Leghorn !'##note difference at position 22 may be due to PCR error in gene !1sequence REFERENCE A27518 !$#authors Gope, M.L.; Keinaenen, R.A.; Kristo, P.A.; Conneely, O.M.; !1Beattie, W.G.; Zarucki-Schulz, T.; O'Malley, B.W.; Kulomaa, !1M.S. !$#journal Nucleic Acids Res. (1987) 15:3595-3606 !$#title Molecular cloning of the chicken avidin cDNA. !$#cross-references MUID:87203384; PMID:3575102 !$#accession A27518 !'##molecule_type mRNA !'##residues 1-152 ##label GOP !'##cross-references GB:X05343; NID:g63071; PIDN:CAA28954.1; PID:g63072 REFERENCE A92093 !$#authors DeLange, R.J.; Huang, T.S. !$#journal J. Biol. Chem. (1971) 246:698-709 !$#title Egg white avidin. III. Sequence of the 78-residue middle !1cyanogen bromide peptide. Complete amino acid sequence of !1the protein subunit. !$#cross-references MUID:71107558; PMID:5100763 !$#accession A92093 !'##molecule_type protein !'##residues 25-57,'T',59-76,'E',78-152 ##label DEL !'##experimental_source egg white !'##note approximately 50% of the chains have 58-Ile REFERENCE A92092 !$#authors Huang, T.S.; DeLange, R.J. !$#journal J. Biol. Chem. (1971) 246:686-697 !$#title Egg white avidin. II. Isolation, composition, and amino acid !1sequences of the tryptic peptides. !$#cross-references MUID:71107557; PMID:5100762 !$#contents sequences of tryptic peptides !$#accession A92092 !'##molecule_type protein !'##residues 25-57,'T',59-76,'E',78-152 ##label DEL2 REFERENCE A51448 !$#authors Livnah, O.; Sussman, J. !$#submission submitted to the Brookhaven Protein Data Bank, April 1993 !$#cross-references PDB:2AVI !$#contents annotation; X-ray crystallography, 3.0 angstroms, with !1biotin, residues 27-57,'T',59-76,'E',78-147 REFERENCE A47554 !$#authors Livnah, O.; Bayer, E.A.; Wilchek, M.; Sussman, J.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:5076-5080 !$#title Three-dimensional structures of avidin and the avidin-biotin !1complex. !$#cross-references MUID:93281699; PMID:8506353 !$#contents annotation; X-ray crystallography, 3.0 angstroms REFERENCE A51622 !$#authors Pugliese, L.; Coda, A.; Malcovati, M.; Bolognesi, M. !$#submission submitted to the Brookhaven Protein Data Bank, March 1993 !$#cross-references PDB:1AVD !$#contents annotation; X-ray crystallography, 2.7 angstroms, with !1biotin, residues 27-57,'T',59-76,'E',78-149 REFERENCE A51623 !$#authors Pugliese, L.; Coda, A.; Malcovati, M.; Bolognesi, M. !$#submission submitted to the Brookhaven Protein Data Bank, March 1993 !$#cross-references PDB:1AVE !$#contents annotation; X-ray crystallography, 2.8 angstroms, without !1biotin, residues 27-57,'T',59-76,'E',78-149 REFERENCE A54974 !$#authors Pugliese, L.; Coda, A.; Malcovati, M.; Bolognesi, M. !$#journal J. Mol. Biol. (1993) 231:698-710 !$#title Three-dimensional structure of the tetragonal crystal form !1of egg-white avidin in its functional complex with biotin at !12.7 angstrom resolution. !$#cross-references MUID:93294833; PMID:8515446 !$#contents annotation; X-ray crystallography, 2.7 angstroms GENETICS !$#introns 27/3; 98/1; 138/2 CLASSIFICATION #superfamily avidin KEYWORDS glycoprotein FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-152 #product avidin #status experimental #label MAT\ !$28-107 #disulfide_bonds #status experimental\ !$41 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 152 #molecular-weight 16768 #checksum 1945 SEQUENCE /// ENTRY NZHU #type complete TITLE endozepine [validated] - human ALTERNATE_NAMES acyl-CoA-binding protein; diazepam-binding inhibitor ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1988 #sequence_revision 30-Sep-1991 #text_change 18-Aug-2000 ACCESSIONS B26448; B25832; A25049; S54341 REFERENCE A26448 !$#authors Webb, N.R.; Rose, T.M.; Malik, N.; Marquardt, H.; Shoyab, !1M.; Todaro, G.J.; Lee, D.C. !$#journal DNA (1987) 6:71-79 !$#title Bovine and human cDNA sequences encoding a putative !1benzodiazepine receptor ligand. !$#cross-references MUID:87161236; PMID:2881742 !$#accession B26448 !'##molecule_type mRNA !'##residues 1-87 ##label WEB !'##cross-references EMBL:M15886 REFERENCE A25832 !$#authors Marquardt, H.; Todaro, G.J.; Shoyab, M. !$#journal J. Biol. Chem. (1986) 261:9727-9731 !$#title Complete amino acid sequences of bovine and human !1endozepines: homology with rat diazepam binding inhibitor. !$#cross-references MUID:86278003; PMID:3525533 !$#accession B25832 !'##molecule_type protein !'##residues 2-87 ##label MAR !'##experimental_source brain REFERENCE A25049 !$#authors Gray, P.W.; Glaister, D.; Seeburg, P.H.; Guidotti, A.; !1Costa, E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:7547-7551 !$#title Cloning and expression of cDNA for human diazepam binding !1inhibitor, a natural ligand of an allosteric regulatory site !1of the gamma-aminobutyric acid type A receptor. !$#cross-references MUID:87016986; PMID:3020548 !$#accession A25049 !'##molecule_type mRNA !'##residues 'MWGDLWLLPPASANPGTGTE',4-87 ##label GRA !'##cross-references EMBL:M14200; NID:g181477; PIDN:AAA52171.1; !1PID:g181478 REFERENCE S54340 !$#authors Kolmer, M.; Rovio, A.; Alho, H. !$#journal Biochem. J. (1995) 306:327-330 !$#title The characterization of two diazepam binding inhibitor (DBI) !1transcripts in humans. !$#cross-references MUID:95194304; PMID:7534063 !$#accession S54341 !'##status preliminary !'##molecule_type mRNA !'##residues 1-11,13 ##label KOL COMMENT This endogenous protein may take part in the modulation of !1GABA-ergic transmission. GENETICS !$#gene GDB:DBI !'##cross-references GDB:119837; OMIM:125950 !$#map_position 2q12-2q21 CLASSIFICATION #superfamily endozepine; endozepine homology KEYWORDS acetylated amino end; acyl-CoA binding FEATURE !$2-87 #product endozepine #status experimental #label MAT\ !$19-75 #domain endozepine homology #label NDZ\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental SUMMARY #length 87 #molecular-weight 10044 #checksum 9521 SEQUENCE /// ENTRY NZBO #type complete TITLE endozepine - bovine ALTERNATE_NAMES acyl-CoA-binding protein; diazepam-binding inhibitor CONTAINS endozepine, short form ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Dec-1988 #sequence_revision 30-Sep-1991 #text_change 22-Jun-1999 ACCESSIONS A26448; S23127; A25832; A27886; A32944 REFERENCE A26448 !$#authors Webb, N.R.; Rose, T.M.; Malik, N.; Marquardt, H.; Shoyab, !1M.; Todaro, G.J.; Lee, D.C. !$#journal DNA (1987) 6:71-79 !$#title Bovine and human cDNA sequences encoding a putative !1benzodiazepine receptor ligand. !$#cross-references MUID:87161236; PMID:2881742 !$#accession A26448 !'##molecule_type mRNA !'##residues 1-87 ##label WEB !'##cross-references EMBL:M15886; NID:g162978; PIDN:AAA30495.1; !1PID:g162979 REFERENCE S23127 !$#authors Jensen, M.S.; Hojrup, P.; Rasmussen, J.T.; Knudsen, J. !$#journal Biochem. J. (1992) 284:809-812 !$#title Purification and characterization of variants of !1acyl-CoA-binding protein in the bovine liver. !$#cross-references MUID:92322005; PMID:1622397 !$#accession S23127 !'##molecule_type protein !'##residues 2-87 ##label JEN !'##experimental_source liver REFERENCE A25832 !$#authors Marquardt, H.; Todaro, G.J.; Shoyab, M. !$#journal J. Biol. Chem. (1986) 261:9727-9731 !$#title Complete amino acid sequences of bovine and human !1endozepines: homology with rat diazepam binding inhibitor. !$#cross-references MUID:86278003; PMID:3525533 !$#accession A25832 !'##molecule_type protein !'##residues 2-87 ##label MAR !'##experimental_source brain REFERENCE A27886 !$#authors Mikkelsen, J.; Hojrup, P.; Nielsen, P.F.; Roepstorff, P.; !1Knudsen, J. !$#journal Biochem. J. (1987) 245:857-861 !$#title Amino acid sequence of acyl-CoA-binding protein from cow !1liver. !$#cross-references MUID:88024142; PMID:3663196 !$#accession A27886 !'##molecule_type protein !'##residues 2-87 ##label MIK !'##experimental_source liver REFERENCE A32944 !$#authors Besman, M.J.; Yanagibashi, K.; Lee, T.D.; Kawamura, M.; !1Hall, P.F.; Shively, J.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:4897-4901 !$#title Identification of des-(Gly-Ile)-endozepine as an effector of !1corticotropin-dependent adrenal steroidogenesis: stimulation !1of cholesterol delivery is mediated by the peripheral !1benzodiazepine receptor. !$#cross-references MUID:89296911; PMID:2544879 !$#accession A32944 !'##molecule_type protein !'##residues 2-85 ##label BES !'##experimental_source adrenal cortex COMMENT This protein may take part in the modulation of GABA-ergic !1transmission in the brain. CLASSIFICATION #superfamily endozepine; endozepine homology KEYWORDS acetylated amino end; acyl-CoA binding FEATURE !$2-87 #product endozepine #status experimental #label MAT\ !$2-85 #product endozepine, short form #status experimental !8#label MA2\ !$19-75 #domain endozepine homology #label NDZ\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental SUMMARY #length 87 #molecular-weight 10044 #checksum 8749 SEQUENCE /// ENTRY NZPG #type complete TITLE endozepine - pig ALTERNATE_NAMES diazepam-binding inhibitor ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 26-Feb-1999 ACCESSIONS S00805; S36839 REFERENCE S00805 !$#authors Chen, Z.W.; Agerberth, B.; Gell, K.; Andersson, M.; Mutt, !1V.; Oestenson, C.G.; Efendic, S.; Barros-Soederling, J.; !1Persson, B.; Joernvall, H. !$#journal Eur. J. Biochem. (1988) 174:239-245 !$#title Isolation and characterization of porcine diazepam-binding !1inhibitor, a polypeptide not only of cerebral occurrence but !1also common in intestinal tissues and with effects on !1regulation of insulin release. !$#cross-references MUID:88254787; PMID:3289918 !$#accession S00805 !'##molecule_type protein !'##residues 1-86 ##label CHE REFERENCE S36839 !$#authors Agerberth, B.; Boman, A.; Andersson, M.; Joernvall, H.; !1Mutt, V.; Boman, H.G. !$#journal Eur. J. Biochem. (1993) 216:623-629 !$#title Isolation of three antibacterial peptides from pig !1intestine: gastric inhibitory polypeptide(7-42), !1diazepam-binding inhibitor(32-86) and a novel factor, !1peptide 3910. !$#cross-references MUID:93387315; PMID:8375398 !$#accession S36839 !'##molecule_type protein !'##residues 32-86 ##label AGE COMMENT This protein may be the endogenous ligand of the !1benzodiazepine receptor. CLASSIFICATION #superfamily endozepine; endozepine homology KEYWORDS acyl-CoA binding; antibacterial; blocked amino end; !1intestine FEATURE !$1-86 #product endozepine #status experimental #label MAT1\ !$18-74 #domain endozepine homology #label NDZ\ !$32-86 #product endozepine (32-86) #status experimental !8#label MAT2\ !$1 #modified_site blocked amino end (Ser) (probably !8acetylated) #status experimental SUMMARY #length 86 #molecular-weight 9765 #checksum 6320 SEQUENCE /// ENTRY NZRT #type complete TITLE endozepine - rat ALTERNATE_NAMES acyl-CoA-binding protein; diazepam-binding inhibitor CONTAINS triakontatetraneuropeptide (TTN) ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jun-2000 ACCESSIONS S27345; A25044; A47572; S06494; A61461; S54387 REFERENCE S27345 !$#authors Mandrup, S.; Hummel, R.; Ravn, S.; Jensen, G.; Andreasen, !1P.H.; Gregersen, N.; Knudsen, J.; Kristiansen, K. !$#journal J. Mol. Biol. (1992) 228:1011-1022 !$#title Acyl-CoA-binding protein/diazepam-binding inhibitor gene and !1pseudogenes. A typical housekeeping gene family. !$#cross-references MUID:93108436; PMID:1469708 !$#accession S27345 !'##molecule_type DNA !'##residues 1-87 ##label MAN !'##cross-references GB:X96560; EMBL:Z11991; NID:g1228088; !1PIDN:CAA65396.1; PID:g1228089 REFERENCE A25044 !$#authors Mocchetti, I.; Einstein, R.; Brosius, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:7221-7225 !$#title Putative diazepam binding inhibitor peptide: cDNA clones !1from rat. !$#cross-references MUID:87016919; PMID:3463960 !$#accession A25044 !'##molecule_type mRNA !'##residues 1-87 ##label MOC !'##cross-references EMBL:M14201; NID:g203922; PIDN:AAA41078.1; !1PID:g203923 REFERENCE A47572 !$#authors Gray, P.W. !$#journal Neuropharmacology (1987) 26:863-865 !$#title Molecular biology of diazepam binding inhibitor. !$#cross-references MUID:88014467; PMID:2821429 !$#accession A47572 !'##molecule_type mRNA !'##residues 1-87 ##label GRA !'##cross-references GB:M20268; NID:g203924; PIDN:AAA41079.1; !1PID:g203925 REFERENCE S06494 !$#authors Knudsen, J.; Hojrup, P.; Hansen, H.O.; Hansen, H.F.; !1Roepstorff, P. !$#journal Biochem. J. (1989) 262:513-519 !$#title Acyl-CoA-binding protein in the rat. Purification, binding !1characteristics, tissue concentrations and amino acid !1sequence. !$#cross-references MUID:90026317; PMID:2803267 !$#accession S06494 !'##molecule_type protein !'##residues 2-87 ##label KNU REFERENCE A61461 !$#authors Slobodyansky, E.; Guidotti, A.; Wambebe, C.; Berkovich, A.; !1Costa, E. !$#journal J. Neurochem. (1989) 53:1276-1284 !$#title Isolation and characterization of a rat brain !1triakontatetraneuropeptide, a posttranslational product of !1diazepam binding inhibitor: specific action at the Ro 5-4864 !1recognition site. !$#cross-references MUID:89361456; PMID:2769267 !$#accession A61461 !'##molecule_type protein !'##residues 18-51 ##label SLO !'##note this sequence represents a naturally occurring, biologically !1active fragment (triakontatetraneuropeptide) of diazepam !1binding inhibitor REFERENCE S54387 !$#authors Kolmer, M.; Alho, H.; Costa, E.; Pani, L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:8439-8443 !$#title Cloning and tissue-specific functional characterization of !1the promoter of the rat diazepam binding inhibitor, a !1peptide with multiple biological actions. !$#cross-references MUID:93391369; PMID:7690962 !$#accession S54387 !'##status preliminary; translation not shown !'##molecule_type DNA !'##residues 1-42 ##label KOL !'##cross-references EMBL:Z21846; NID:g296966; PIDN:CAA79894.1; !1PID:g488839 GENETICS !$#introns 3/3 CLASSIFICATION #superfamily endozepine; endozepine homology KEYWORDS acetylated amino end; acyl-CoA binding; brain FEATURE !$2-87 #product endozepine #status experimental #label MAT\ !$18-51 #domain triakontatetraneuropeptide #status !8experimental #label TTN\ !$19-75 #domain endozepine homology #label NDZ\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental SUMMARY #length 87 #molecular-weight 10027 #checksum 248 SEQUENCE /// ENTRY S48040 #type complete TITLE acyl-CoA binding protein - rape ORGANISM #formal_name Brassica napus #common_name rape DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S48040; S49102 REFERENCE S48040 !$#authors Hills, M.J.; Dann, R.; Lydiate, D.; Sharpe, A. !$#journal Plant Mol. Biol. (1994) 25:917-920 !$#title Molecular cloning of a cDNA from Brassica napus L. for a !1homologue of acyl-CoA-binding protein. !$#cross-references MUID:94355664; PMID:8075407 !$#accession S48040 !'##status preliminary !'##molecule_type mRNA !'##residues 1-92 ##label HIL !'##cross-references EMBL:X77134; NID:g509264; PIDN:CAA54390.1; !1PID:g509265 CLASSIFICATION #superfamily endozepine; endozepine homology KEYWORDS acyl-CoA binding FEATURE !$20-76 #domain endozepine homology #label NDZ SUMMARY #length 92 #molecular-weight 10171 #checksum 4946 SEQUENCE /// ENTRY NZBOR #type complete TITLE endozepine-related protein precursor - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 22-Jun-1999 ACCESSIONS C26448 REFERENCE A26448 !$#authors Webb, N.R.; Rose, T.M.; Malik, N.; Marquardt, H.; Shoyab, !1M.; Todaro, G.J.; Lee, D.C. !$#journal DNA (1987) 6:71-79 !$#title Bovine and human cDNA sequences encoding a putative !1benzodiazepine receptor ligand. !$#cross-references MUID:87161236; PMID:2881742 !$#accession C26448 !'##molecule_type mRNA !'##residues 1-533 ##label WEB !'##cross-references EMBL:M15888; NID:g162980; PIDN:AAA30496.1; !1PID:g162981 !'##note the authors translated the codon AAT for residue 238 as Asp CLASSIFICATION #superfamily endozepine-related protein; endozepine homology KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-533 #product endozepine-related protein #status predicted !8#label MAT\ !$63-119 #domain endozepine homology #label NDZ\ !$502-525 #domain transmembrane #status predicted #label TMM\ !$59,341,361 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 533 #molecular-weight 59759 #checksum 1549 SEQUENCE /// ENTRY BFBO #type complete TITLE folate-binding protein - bovine (tentative sequence) ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 17-Dec-1982 #sequence_revision 17-Mar-1987 #text_change 31-Mar-2000 ACCESSIONS A03161 REFERENCE A03161 !$#authors Svendsen, I.; Hansen, S.I.; Holm, J.; Lyngbye, J. !$#journal Carlsberg Res. Commun. (1984) 49:123-131 !$#title The complete amino acid sequence of the folate-binding !1protein from cow's milk. !$#accession A03161 !'##molecule_type protein !'##residues 1-222 ##label SVE COMMENT Eight disulfide bonds are present. COMMENT This glycoprotein was isolated from milk. CLASSIFICATION #superfamily folate-binding protein KEYWORDS folate; glycoprotein FEATURE !$49,141 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 222 #molecular-weight 25825 #checksum 9864 SEQUENCE /// ENTRY VOCH #type complete TITLE riboflavin-binding protein precursor - chicken ALTERNATE_NAMES RBP; RfBP; ribBP ORGANISM #formal_name Gallus gallus #common_name chicken DATE 28-May-1986 #sequence_revision 02-Jun-1994 #text_change 22-Jun-1999 ACCESSIONS A29228; A91978; A91993; B91993; C91993; A48871; B48871; !1A61292; S23968; A03214 REFERENCE A29228 !$#authors Zheng, D.B.; Lim, H.M.; Pene, J.J.; White III, H.B. !$#journal J. Biol. Chem. (1988) 263:11126-11129 !$#title Chicken riboflavin-binding protein. cDNA sequence and !1homology with milk folate-binding protein. !$#cross-references MUID:88298752; PMID:3403518 !$#accession A29228 !'##molecule_type mRNA !'##residues 1-238 ##label ZHE !'##cross-references GB:J03922; NID:g212630; PIDN:AAA49056.1; !1PID:g212631 REFERENCE A91978 !$#authors Hamazume, Y.; Mega, T.; Ikenaka, T. !$#journal J. Biochem. (1984) 95:1633-1644 !$#title Characterization of hen egg white- and yolk-riboflavin !1binding proteins and amino acid sequence of egg !1white-riboflavin binding protein. !$#cross-references MUID:84289341; PMID:6469943 !$#contents egg-white RBP !$#accession A91978 !'##molecule_type protein !'##residues 18-30,'N',32-236 ##label HAM !'##experimental_source White Leghorn breed !'##note 31-Lys occurs with 30% frequency in both egg-white and yolk RBP REFERENCE A91993 !$#authors Norioka, N.; Okada, T.; Hamazume, Y.; Mega, T.; Ikenaka, T. !$#journal J. Biochem. (1985) 97:19-28 !$#title Comparison of the amino acid sequences of hen plasma-, !1yolk-, and white-riboflavin binding proteins. !$#cross-references MUID:85207513; PMID:3997791 !$#contents yolk RBP, short form; yolk RBP, long form; plasma RBP !$#accession A91993 !'##molecule_type protein !'##residues 18-223 ##label NOR !$#accession B91993 !'##molecule_type protein !'##residues 18-225 ##label NO2 !$#accession C91993 !'##molecule_type protein !'##residues 212-236 ##label NO3 !'##experimental_source White Leghorn breed !'##note for the yolk RBP sequence, 70% of the molecules are of the !1short form and 30% of the molecules are of the long form REFERENCE A48871 !$#authors MacLachlan, I.; Nimpf, J.; White III, H.B.; Schneider, W.J. !$#journal J. Biol. Chem. (1993) 268:23222-23226 !$#title Riboflavinuria in the rd chicken. 5'-splice site mutation in !1the gene for riboflavin-binding protein. !$#cross-references MUID:94043110; PMID:8226844 !$#accession A48871 !'##molecule_type mRNA !'##residues 1-30,'N',32-238 ##label MA1 !'##cross-references EMBL:X74247 !'##experimental_source ssp. domesticus, White Leghorn, liver !'##note the authors translated codon TAC for residue 92 as Thr, and GAA !1for residue 181 as Gly !'##note sequence extracted from NCBI backbone (NCBIN:138908, !1NCBIP:138909) !$#accession B48871 !'##molecule_type mRNA !'##residues 1-30,'N',32-47,81-238 ##label MA3 !'##cross-references EMBL:S66387 !'##note the authors translated codon TAC for residue 92 as Thr, and GAA !1for residue 181 as Gly !'##note sequence extracted from NCBI backbone (NCBIN:138910, !1NCBIP:138911) REFERENCE A44578 !$#authors Hamazume, Y.; Mega, T.; Ikenaka, T. !$#journal J. Biochem. (1987) 101:217-223 !$#title Positions of disulfide bonds in riboflavin-binding protein !1of hen egg white. !$#cross-references MUID:87194696; PMID:3571203 !$#contents annotation; disulfide bonds REFERENCE A61292 !$#authors Fenselau, C.; Heller, D.N.; Miller, M.S.; White III, H.B. !$#journal Anal. Biochem. (1985) 150:309-314 !$#title Phosphorylation sites in riboflavin-binding protein !1characterized by fast atom bombardment mass spectrometry. !$#cross-references MUID:86128180; PMID:4091257 !$#accession A61292 !'##molecule_type protein !'##residues 199-214 ##label FEN REFERENCE S23968 !$#authors Rohrer, J.S.; White III, H.B. !$#journal Biochem. J. (1992) 285:275-280 !$#title Separation and characterization of the two Asn-linked !1glycosylation sites of chicken serum riboflavin-binding !1protein. Glycosylation differences despite similarity of !1primary structure. !$#cross-references MUID:92344583; PMID:1637312 !$#accession S23968 !'##molecule_type protein !'##residues 32-65;155-178 ##label ROH COMMENT Plasma and yolk RBPs have the same carbohydrate components, !1whereas egg-white RBP has a different, ovomucoid-type !1carbohydrate chain. COMMENT Yolk RBP is synthesized in the liver; egg-white RBP is !1synthesized in the oviduct. CLASSIFICATION #superfamily folate-binding protein KEYWORDS egg white; egg yolk; glycoprotein; phosphoprotein; !1pyroglutamic acid; vitamin carrier FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-236 #product riboflavin-binding protein, plasma and egg !8white form #status experimental #label RPW\ !$18-225 #product riboflavin-binding protein, egg yolk long !8form #status experimental #label RYL\ !$18-223 #product riboflavin-binding protein, egg yolk short !8form #status experimental #label RYS\ !$18 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$22-49,50-94 #disulfide_bonds (or 22-50, 49-77) #status !8experimental\ !$41-90,74-155, !$81-127,116-186, !$120-169,133-151, !$184-219 #disulfide_bonds #status experimental\ !$53,164 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$202 #binding_site phosphate (Ser) (covalent) #status !8absent\ !$204,205,208,209, !$210,212,213,214 #binding_site phosphate (Ser) (covalent) #status !8experimental SUMMARY #length 238 #molecular-weight 27225 #checksum 5818 SEQUENCE /// ENTRY A39904 #type complete TITLE gastric intrinsic factor precursor - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A39904; A60437; S44128 REFERENCE A39904 !$#authors Hewitt, J.E.; Gordon, M.M.; Taggart, R.T.; Mohandas, T.K.; !1Alpers, D.H. !$#journal Genomics (1991) 10:432-440 !$#title Human gastric intrinsic factor: characterization of cDNA and !1genomic clones and localization to human chromosome 11. !$#cross-references MUID:91301700; PMID:2071148 !$#accession A39904 !'##molecule_type DNA; mRNA !'##residues 1-417 ##label HEW !'##cross-references GB:M63154; NID:g806639; PIDN:AAA66354.1; !1PID:g183186 REFERENCE A60437 !$#authors Hansen, M.R.; Nexo, E.; Svendsen, I.; Bucher, D.; Olesen, H. !$#journal Scand. J. Clin. Lab. Invest. (1989) 49(Suppl.194):19-22 !$#title Human intrinsic factor. Its primary structure compared to !1the primary structure of rat intrinsic factor. !$#accession A60437 !'##molecule_type protein !'##residues 157-165,'X',167-174,'V',176-182,'V',184-187,'F',188-190, !1'X',192-211,'V',213,'X',215-216,'X',218,'XXQ',222 ##label !1HAN REFERENCE S44128 !$#authors Hannappel, M.; Kehl, M.; Winnacker, E.L. !$#submission submitted to the EMBL Data Library, December 1993 !$#description A cDNA sequence of the human intrinsic factor. !$#accession S44128 !'##status preliminary !'##molecule_type mRNA !'##residues 1-90,'Q',92-417 ##label HA2 !'##cross-references EMBL:X76562; NID:g472992; PIDN:CAA54061.1; !1PID:g472993 GENETICS !$#gene GDB:GIF !'##cross-references GDB:118800; OMIM:261000 !$#map_position 11q12-11q13 CLASSIFICATION #superfamily gastric intrinsic factor KEYWORDS glycoprotein; vitamin B12 transport; vitamin carrier FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-417 #product gastric intrinsic factor #status predicted !8#label MAT\ !$311,330,334,413 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 417 #molecular-weight 45425 #checksum 6885 SEQUENCE /// ENTRY A49684 #type complete TITLE gastric intrinsic factor precursor - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A49684 REFERENCE A49684 !$#authors Lorenz, R.G.; Gordon, J.I. !$#journal J. Biol. Chem. (1993) 268:26559-26570 !$#title Use of transgenic mice to study regulation of gene !1expression in the parietal cell lineage of gastric units. !$#cross-references MUID:94075347; PMID:8253786 !$#accession A49684 !'##status preliminary !'##molecule_type mRNA !'##residues 1-417 ##label LOR !'##cross-references GB:L24191; NID:g435091; PIDN:AAA37882.1; !1PID:g435092 CLASSIFICATION #superfamily gastric intrinsic factor KEYWORDS glycoprotein; vitamin B12 transport; vitamin carrier SUMMARY #length 417 #molecular-weight 45395 #checksum 4803 SEQUENCE /// ENTRY A34003 #type complete TITLE gastric intrinsic factor precursor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A34003; A34083 REFERENCE A34003 !$#authors Dieckgraefe, B.K.; Seetharam, B.; Banaszak, L.; Leykam, !1J.F.; Alpers, D.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:46-50 !$#title Isolation and structural characterization of a cDNA clone !1encoding rat gastric intrinsic factor. !$#cross-references MUID:88124816; PMID:3422425 !$#accession A34003 !'##molecule_type mRNA !'##residues 1-421 ##label DIE !'##cross-references GB:J03577; NID:g204683; PIDN:AAA41361.1; !1PID:g204684 !'##note part of this sequence was confirmed by protein sequencing COMMENT This protein binds the vitamin cobalamin to facilitate !1receptor-mediated endocytosis of cobalamin in the ileum. CLASSIFICATION #superfamily gastric intrinsic factor KEYWORDS glycoprotein; vitamin B12 transport; vitamin carrier FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-421 #product gastric intrinsic factor #status predicted !8#label MAT SUMMARY #length 421 #molecular-weight 46458 #checksum 1544 SEQUENCE /// ENTRY A34227 #type complete TITLE transcobalamin I precursor [validated] - human ALTERNATE_NAMES haptocorrin; vitamin B12 binding protein, R binder family ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 08-Dec-2000 ACCESSIONS A34227; A42174; A60553 REFERENCE A34227 !$#authors Johnston, J.; Bollekens, J.; Allen, R.H.; Berliner, N. !$#journal J. Biol. Chem. (1989) 264:15754-15757 !$#title Structure of the cDNA encoding transcobalamin I, a !1neutrophil granule protein. !$#cross-references MUID:89380156; PMID:2777761 !$#accession A34227 !'##molecule_type mRNA !'##residues 1-433 ##label JOH !'##cross-references GB:J05068; NID:g307478; PIDN:AAA61058.1; !1PID:g307479 REFERENCE A42174 !$#authors Johnston, J.; Yang-Feng, T.; Berliner, N. !$#journal Genomics (1992) 12:459-464 !$#title Genomic structure and mapping of the chromosomal gene for !1transcobalamin I (TCN1): comparison to human intrinsic !1factor. !$#cross-references MUID:92217966; PMID:1463480 !$#accession A42174 !'##status preliminary !'##molecule_type DNA !'##residues 1-26 ##label JO2 !'##note sequence extracted from NCBI backbone (NCBIN:95735, !1NCBIP:95736) REFERENCE A60553 !$#authors Tonnesen, P.; Thim, L.; Nexo, E. !$#journal Scand. J. Clin. Lab. Invest. (1990) 50:187-194 !$#title Epidermal growth factor and haptocorrin in nasal secretion. !$#cross-references MUID:90251988; PMID:2187240 !$#accession A60553 !'##molecule_type protein !'##residues 24-25,'X',27-32,'X',34-38,'X',40 ##label TON GENETICS !$#gene GDB:TCN1 !'##cross-references GDB:118882; OMIM:189905 !$#map_position 11q11-11q12.3 CLASSIFICATION #superfamily gastric intrinsic factor FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-433 #product transcobalamin #status experimental #label !8MAT SUMMARY #length 433 #molecular-weight 48194 #checksum 7961 SEQUENCE /// ENTRY A39744 #type complete TITLE transcobalamin II precursor - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A39744; S29812; A24598 REFERENCE A39744 !$#authors Platica, O.; Janeczko, R.; Quadros, E.V.; Regec, A.; Romain, !1R.; Rothenberg, S.P. !$#journal J. Biol. Chem. (1991) 266:7860-7863 !$#title The cDNA sequence and the deduced amino acid sequence of !1human transcobalamin II show homology with rat intrinsic !1factor and human transcobalamin I. !$#cross-references MUID:91210312; PMID:1708393 !$#accession A39744 !'##molecule_type mRNA !'##residues 1-427 ##label PLA !'##cross-references GB:M60396; NID:g339195; PIDN:AAA61054.1; !1PID:g339196 REFERENCE S29812 !$#authors Li, N.; Seetharam, S.; Lindemans, J.; Alpers, D.H.; Arwert, !1F.; Seetharam, B. !$#journal Biochim. Biophys. Acta (1993) 1172:21-30 !$#title Isolation and sequence analysis of variant forms of human !1transcobalamin II. !$#cross-references MUID:93176815; PMID:8439564 !$#accession S29812 !'##status preliminary !'##molecule_type mRNA !'##residues 1-258,'R',260-375,'L',377-427 ##label LIA !'##experimental_source clone V6 !'##note 198-Thr and 219-Ile were also found REFERENCE A24598 !$#authors Quadros, E.V.; Rothenberg, S.P.; Pan, Y.C.E.; Stein, S. !$#journal J. Biol. Chem. (1986) 261:15455-15460 !$#title Purification and molecular characterization of human !1transcobalamin II. !$#cross-references MUID:87057168; PMID:3782074 !$#accession A24598 !'##molecule_type protein !'##residues 19-37 ##label QUA !'##experimental_source plasma GENETICS !$#gene GDB:TCN2 !'##cross-references GDB:119608; OMIM:275350 !$#map_position 22q11.2-22qter CLASSIFICATION #superfamily gastric intrinsic factor KEYWORDS plasma; polymorphism; vitamin B12 transport FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-427 #product transcobalamin II #status predicted #label !8MAT SUMMARY #length 427 #molecular-weight 47449 #checksum 2190 SEQUENCE /// ENTRY XLPG2 #type complete TITLE colipase II precursor - pig ALTERNATE_NAMES procolipase II ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 24-Apr-1984 #sequence_revision 04-Dec-1986 #text_change 26-Apr-1996 ACCESSIONS A03162; A90593 REFERENCE A90652 !$#authors Sternby, B.; Engstrom, A.; Hellman, U.; Vihert, A.M.; !1Sternby, N.H.; Borgstrom, B. !$#journal Biochim. Biophys. Acta (1984) 784:75-80 !$#title The primary sequence of human pancreatic colipase. !$#cross-references MUID:84104937; PMID:6691986 !$#accession A03162 !'##molecule_type protein !'##residues 1-95 ##label STE REFERENCE A90593 !$#authors Charles, M.; Erlanson, C.; Bianchetta, J.; Joffre, J.; !1Guidoni, A.; Rovery, M. !$#journal Biochim. Biophys. Acta (1974) 359:186-197 !$#title The primary structure of porcine colipase II. I. The amino !1acid sequence. !$#cross-references MUID:74290109; PMID:4858821 !$#accession A90593 !'##molecule_type protein !'##residues 6-91 ##label CHA REFERENCE A90594 !$#authors Erlanson, C.; Charles, M.; Astier, M.; Desnuelle, P. !$#journal Biochim. Biophys. Acta (1974) 359:198-203 !$#title The primary structure of porcine colipase II. II. The !1disulfide bridges. !$#cross-references MUID:74290110; PMID:4603223 !$#contents annotation; disulfide bonds COMMENT Colipase, a cofactor of triacylglycerol lipase (EC 3.1.1.3), !1forms a 1:1 stoichiometric complex with it, enabling it to !1hydrolyze its substrate at the lipid-water interface. !1Without colipase the enzyme is washed off by bile salts, !1which are known to have an inhibitory effect on the lipase. COMMENT Residues 6-9 and Arg-92 are considered essential for the !1function of colipase in the presence of phospholipids. CLASSIFICATION #superfamily colipase KEYWORDS lipid digestion; lipid hydrolysis; pancreas FEATURE !$1-5 #domain propeptide #status experimental #label PRO\ !$6-95 #product colipase II #status experimental #label MAT\ !$17-87,23-39,27-63, !$28-61,49-69 #disulfide_bonds #status experimental\ !$52,55,58,59 #binding_site micellar substrate (Phe, Tyr, Tyr, Tyr) !8#status predicted SUMMARY #length 95 #molecular-weight 10335 #checksum 795 SEQUENCE /// ENTRY XLHU #type complete TITLE colipase precursor [validated] - human ALTERNATE_NAMES procolipase ORGANISM #formal_name Homo sapiens #common_name man DATE 04-Dec-1986 #sequence_revision 19-May-1995 #text_change 08-Dec-2000 ACCESSIONS A42568; A33949; A03163 REFERENCE A42568 !$#authors Sims, H.F.; Lowe, M.E. !$#journal Biochemistry (1992) 31:7120-7125 !$#title The human colipase gene: isolation, chromosomal location, !1and tissue-specific expression. !$#cross-references MUID:92353041; PMID:1643046 !$#accession A42568 !'##molecule_type DNA !'##residues 1-112 ##label SIM !'##cross-references GB:M95529; NID:g180842; PIDN:AAB05818.1; !1PID:g1483624 !'##note sequence extracted from NCBI backbone (NCBIN:110576, !1NCBIN:110578, NCBIP:110580) REFERENCE A33949 !$#authors Lowe, M.E.; Rosenblum, J.L.; McEwen, P.; Strauss, A.W. !$#journal Biochemistry (1990) 29:823-828 !$#title Cloning and characterization of the human colipase cDNA. !$#cross-references MUID:90248429; PMID:2337598 !$#accession A33949 !'##molecule_type mRNA !'##residues 1-112 ##label LOW !'##cross-references GB:J02883; NID:g180885; PIDN:AAA52054.1; !1PID:g180886 !'##note evidence of partial N-glycosylation, possibly at Asn-43 REFERENCE A90652 !$#authors Sternby, B.; Engstrom, A.; Hellman, U.; Vihert, A.M.; !1Sternby, N.H.; Borgstrom, B. !$#journal Biochim. Biophys. Acta (1984) 784:75-80 !$#title The primary sequence of human pancreatic colipase. !$#cross-references MUID:84104937; PMID:6691986 !$#accession A03163 !'##molecule_type protein !'##residues 23-108 ##label STE COMMENT Colipase, a cofactor of triacylglycerol lipase (EC 3.1.1.3), !1forms a 1:1 stoichiometric complex with it, enabling it to !1hydrolyze its substrate at the lipid-water interface. !1Without colipase the enzyme is washed off by bile salts, !1which are known to have an inhibitory effect on the lipase. GENETICS !$#gene GDB:CLPS !'##cross-references GDB:127277; OMIM:120105 !$#map_position 6pter-6p21.1 !$#introns 28/3; 69/3 CLASSIFICATION #superfamily colipase KEYWORDS lipid digestion; lipid hydrolysis; pancreas FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-22 #domain amino-terminal propeptide #status predicted !8#label APP\ !$23-108 #product colipase #status experimental #label MAT\ !$109-112 #domain carboxyl-terminal propeptide #status !8predicted #label CPP\ !$34-104,40-56,44-80, !$45-78,66-86 #disulfide_bonds #status predicted\ !$69,72,75,76 #binding_site micellar substrate (Lys, Tyr, Tyr, Tyr) !8#status predicted SUMMARY #length 112 #molecular-weight 11954 #checksum 9811 SEQUENCE /// ENTRY XLHOA #type complete TITLE colipase A precursor - horse ALTERNATE_NAMES procolipase A ORGANISM #formal_name Equus caballus #common_name domestic horse DATE 14-Nov-1983 #sequence_revision 04-Dec-1986 #text_change 26-Apr-1996 ACCESSIONS A03164; A91119; A90220 REFERENCE A90652 !$#authors Sternby, B.; Engstrom, A.; Hellman, U.; Vihert, A.M.; !1Sternby, N.H.; Borgstrom, B. !$#journal Biochim. Biophys. Acta (1984) 784:75-80 !$#title The primary sequence of human pancreatic colipase. !$#cross-references MUID:84104937; PMID:6691986 !$#accession A03164 !'##molecule_type protein !'##residues 1-96 ##label STE !'##note residues 56-59 were positioned by homology; no overlap was !1obtained for 65-66 REFERENCE A91119 !$#authors Pierrot, M.; Astier, J.P.; Astier, M.; Charles, M.; Drenth, !1J. !$#journal Eur. J. Biochem. (1982) 123:347-354 !$#title Pancreatic colipase: crystallographic and biochemical !1aspects. !$#cross-references MUID:82186702; PMID:7075593 !$#accession A91119 !'##molecule_type protein !'##residues 1-88,'N',90-91,'K',93 ##label PIE REFERENCE A90220 !$#authors Julien, R.; Bechis, G.; Gregoire, J.; Rathelot, J.; Rochat, !1H.; Sarda, L. !$#journal Biochem. Biophys. Res. Commun. (1980) 95:1245-1252 !$#title Evidence for the existence of two isocolipases in horse !1pancreas. !$#cross-references MUID:81021166; PMID:7417313 !$#accession A90220 !'##molecule_type protein !'##residues 1-21,'Q',23-55 ##label JUL COMMENT Colipase, a cofactor of triacylglycerol lipase (EC 3.1.1.3), !1forms a 1:1 stoichiometric complex with it, enabling it to !1hydrolyze its substrate at the lipid-water interface. !1Without colipase the enzyme is washed off by bile salts, !1which are known to have an inhibitory effect on the lipase. CLASSIFICATION #superfamily colipase KEYWORDS lipid digestion; lipid hydrolysis; pancreas FEATURE !$1-5 #domain propeptide #status experimental #label PRO\ !$6-96 #product colipase A #status experimental #label MAT\ !$17-87,23-39,27-63, !$28-61,49-69 #disulfide_bonds #status predicted\ !$52,55,58,59 #binding_site micellar substrate (Trp, Tyr, Tyr, Tyr) !8#status predicted SUMMARY #length 96 #molecular-weight 10488 #checksum 2704 SEQUENCE /// ENTRY XLHOB #type complete TITLE colipase B precursor - horse ALTERNATE_NAMES procolipase B ORGANISM #formal_name Equus caballus #common_name domestic horse DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 26-Apr-1996 ACCESSIONS A03165; B90220 REFERENCE A90637 !$#authors Bonicel, J.; Couchoud, P.; Foglizzo, E.; Desnuelle, P.; !1Chapus, C. !$#journal Biochim. Biophys. Acta (1981) 669:39-45 !$#title Amino acid sequence of horse colipase B. !$#cross-references MUID:82046794; PMID:7295770 !$#accession A03165 !'##molecule_type protein !'##residues 1-96 ##label BON REFERENCE A90220 !$#authors Julien, R.; Bechis, G.; Gregoire, J.; Rathelot, J.; Rochat, !1H.; Sarda, L. !$#journal Biochem. Biophys. Res. Commun. (1980) 95:1245-1252 !$#title Evidence for the existence of two isocolipases in horse !1pancreas. !$#cross-references MUID:81021166; PMID:7417313 !$#accession B90220 !'##molecule_type protein !'##residues 1-21,'E',23-28,'T',30-55 ##label JUL COMMENT Colipase, a cofactor of triacylglycerol lipase (EC 3.1.1.3), !1forms a 1:1 stoichiometric complex with it, enabling it to !1hydrolyze its substrate at the lipid-water interface. !1Without colipase the enzyme is washed off by bile salts, !1which are known to have an inhibitory effect on the lipase. CLASSIFICATION #superfamily colipase KEYWORDS lipid digestion; lipid hydrolysis; pancreas FEATURE !$1-5 #domain propeptide #status experimental #label PRO\ !$6-96 #product colipase B #status experimental #label MAT\ !$17-87,23-39,27-63, !$28-61,49-69 #disulfide_bonds #status predicted\ !$52,55,58,59 #binding_site micellar substrate (Trp, Tyr, Tyr, Tyr) !8#status predicted SUMMARY #length 96 #molecular-weight 10491 #checksum 3464 SEQUENCE /// ENTRY A46217 #type complete TITLE GPI-anchor biosynthesis protein PIG-A - human ALTERNATE_NAMES GlcNAc-inositol phospholipid assembly protein, class A ORGANISM #formal_name Homo sapiens #common_name man DATE 22-Sep-1993 #sequence_revision 18-Nov-1994 #text_change 21-Jul-2000 ACCESSIONS A46217; I52665; I52817 REFERENCE A46217 !$#authors Miyata, T.; Takeda, J.; Iida, Y.; Yamada, N.; Inoue, N.; !1Takahashi, M.; Maeda, K.; Kitani, T.; Kinoshita, T. !$#journal Science (1993) 259:1318-1320 !$#title The cloning of PIG-A, a component in the early step of !1GPI-anchor biosynthesis. !$#cross-references MUID:93190103; PMID:7680492 !$#accession A46217 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-484 ##label MIY !'##cross-references GB:D11466; NID:g219993; PIDN:BAA02019.1; !1PID:g219994 !'##experimental_source HeLa cells !'##note sequence extracted from NCBI backbone (NCBIP:126971) REFERENCE I52665 !$#authors Yu, J.; Nagarajan, S.; Ueda, E.; Knez, J.J.; Petersen, R.B.; !1Medof, M.E. !$#journal Braz. J. Med. Biol. Res. (1994) 27:195-201 !$#title Characterization of alternatively spliced PIG-A transcripts !1in normal and paroxysmal nocturnal hemoglobinuria cells. !$#cross-references MUID:94362532; PMID:8081230 !$#accession I52665 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-114,284-484 ##label YUJ !'##cross-references GB:S74936; NID:g797390; PIDN:AAD14160.1; !1PID:g4261860 REFERENCE I52817 !$#authors Takeda, J.; Miyata, T.; Kawagoe, K.; Iida, Y.; Endo, Y.; !1Fujita, T.; Takahashi, M.; Kitani, T.; Kinoshita, T. !$#journal Cell (1993) 73:703-711 !$#title Deficiency of the GPI anchor caused by a somatic mutation of !1the PIG-A gene in paroxysmal nocturnal hemoglobinuria. !$#cross-references MUID:93272311; PMID:8500164 !$#accession I52817 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 301-328,398-420 ##label TAK !'##cross-references GB:S61523; NID:g385677; PIDN:AAD13929.1; !1PID:g4261629 !'##note sequence with deletion mutation resulting in paroxysmal !1nocturnal hemoglobinuria COMMENT This protein is involved in GPI-anchor biosynthesis, but its !1function is uncertain. GENETICS !$#gene GDB:PIGA; PIG-A !'##cross-references GDB:138138; OMIM:311770 !$#map_position Xp22.1-Xp22.1 !$#note defects in this gene result in paroxysmal nocturnal !1hemoglobinuria CLASSIFICATION #superfamily GPI-anchor biosynthesis protein PIG-A KEYWORDS glycoprotein; transmembrane protein FEATURE !$423-442 #domain transmembrane #status predicted #label TRM\ !$99,307 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 484 #molecular-weight 54126 #checksum 7126 SEQUENCE /// ENTRY A55731 #type complete TITLE GPI-anchor biosynthesis protein PIG-A - mouse ALTERNATE_NAMES phosphatidylinositol glycan assembly protein, class A ORGANISM #formal_name Mus musculus #common_name house mouse DATE 23-Mar-1995 #sequence_revision 23-Mar-1995 #text_change 16-Jun-2000 ACCESSIONS A55731 REFERENCE A55731 !$#authors Kawagoe, K.; Takeda, J.; Endo, Y.; Kinoshita, T. !$#journal Genomics (1994) 23:566-574 !$#title Molecular cloning of murine pig-a, a gene for GPI-anchor !1biosynthesis, and demonstration of interspecies conservation !1of its structure, function, and genetic locus. !$#cross-references MUID:95154826; PMID:7851884 !$#accession A55731 !'##molecule_type mRNA !'##residues 1-485 ##label KAW !'##cross-references GB:D26047; NID:g577722; PIDN:BAA05047.1; !1PID:g577723 GENETICS !$#gene Pig-a !$#map_position X-F3/4 CLASSIFICATION #superfamily GPI-anchor biosynthesis protein PIG-A KEYWORDS glycoprotein; transmembrane protein FEATURE !$424-443 #domain transmembrane #status predicted #label TRM\ !$24,99,308 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 485 #molecular-weight 54468 #checksum 2766 SEQUENCE /// ENTRY S65187 #type complete TITLE GPI-anchor biosynthesis protein PIG-A - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES GlcNAc-inositol phospholipid assembly protein; GPI-anchor biosynthesis protein PIG-A homolog; protein P2269; protein YPL175w; transcription factor SPT14, trans-acting ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Dec-1994 #sequence_revision 31-May-1996 #text_change 16-Jun-2000 ACCESSIONS S65187; S27131; A61112; S18842; S60357 REFERENCE S65183 !$#authors Benes, V.; Rechmann, S.; Nentwich, U.; Voss, H.; Ansorge, W. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S65187 !'##molecule_type DNA !'##residues 1-461 ##label BEN !'##cross-references EMBL:Z73531; NID:g1370368; PIDN:CAA97882.1; !1PID:g1370369; GSPDB:GN00016; MIPS:YPL175w !'##experimental_source strain S288C (AB972) REFERENCE S27131 !$#authors Fassler, J. !$#submission submitted to the EMBL Data Library, January 1992 !$#accession S27131 !'##molecule_type DNA !'##residues 16-461 ##label FAS1 !'##cross-references EMBL:X63290 !$#accession A61112 !'##molecule_type DNA !'##residues 'MGF',11,'IA',16-461 ##label BAU !'##cross-references EMBL:X63290; NID:g4533; PIDN:CAA44924.1; !1PID:g441475 REFERENCE S18842 !$#authors Fassler, J.S.; Gray, W.; Lee, J.P.; Yu, G.; Gingerich, G. !$#journal Mol. Gen. Genet. (1991) 230:310-320 !$#title The Saccharomyces cerevisiae SPT14 gene is essential for !1normal expression of the yeast transposon, Ty, as well as !1for expression of the HIS4 gene and several genes in the !1mating pathway. !$#cross-references MUID:92079912; PMID:1660567 !$#accession S18842 !'##molecule_type DNA !'##residues 16-429,'S' ##label FAS2 !'##cross-references EMBL:X63290 REFERENCE S60357 !$#authors Vossen, J.H.; Ram, A.F.J.; Klis, F.M. !$#journal Biochim. Biophys. Acta (1995) 1243:549-551 !$#title Identification of SPT14/CWH6 as the yeast homologue of !1hPIG-A, a gene involved in the biosynthesis of GPI anchors. !$#cross-references MUID:95244613; PMID:7727533 !$#accession S60357 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type DNA !'##residues 16-461 ##label VOS GENETICS !$#gene SGD:SPT14; CWH6; GPI3; MIPS:YPL175w !'##cross-references SGD:S0006096; MIPS:YPL175w !$#map_position 16L !$#introns 5/2 CLASSIFICATION #superfamily GPI-anchor biosynthesis protein PIG-A KEYWORDS glycoprotein; transmembrane protein FEATURE !$416-434 #domain transmembrane #status predicted #label TMM\ !$140,386 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 461 #molecular-weight 52372 #checksum 9936 SEQUENCE /// ENTRY A40308 #type complete TITLE retinal degeneration slow protein - human ALTERNATE_NAMES rds protein ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 02-Sep-1997 ACCESSIONS A40308 REFERENCE A40308 !$#authors Travis, G.H.; Christerson, L.; Danielson, P.E.; Klisak, I.; !1Sparkes, R.S.; Hahn, L.B.; Dryja, T.P.; Sutcliffe, J.G. !$#journal Genomics (1991) 10:733-739 !$#title The human retinal degeneration slow (RDS) gene: chromosome !1assignment and structure of the mRNA. !$#cross-references MUID:91365382; PMID:1679750 !$#accession A40308 !'##molecule_type mRNA !'##residues 1-346 ##label TRA !'##cross-references GB:M62958 GENETICS !$#gene GDB:RDS; RP7 !'##cross-references GDB:118863; OMIM:179605 !$#map_position 6p21.1-6cen CLASSIFICATION #superfamily retinal degeneration slow protein KEYWORDS glycoprotein; photoreceptor; retina; transmembrane protein FEATURE !$16-39 #domain transmembrane #status predicted #label TM1\ !$59-79 #domain transmembrane #status predicted #label TM2\ !$101-122 #domain transmembrane #status predicted #label TM3\ !$261-283 #domain transmembrane #status predicted #label TM4\ !$53,229 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 346 #molecular-weight 39186 #checksum 7482 SEQUENCE /// ENTRY S10177 #type complete TITLE retinal degeneration slow protein - rat ALTERNATE_NAMES rds protein ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 22-Jun-1999 ACCESSIONS S10177 REFERENCE S10177 !$#authors Begy, C.; Bridges, C.D. !$#journal Nucleic Acids Res. (1990) 18:3058 !$#title Nucleotide and predicted protein sequence of rat retinal !1degeneration slow (rds). !$#cross-references MUID:90272424; PMID:2349107 !$#accession S10177 !'##molecule_type mRNA !'##residues 1-346 ##label BEG !'##cross-references EMBL:X52376; NID:g57840; PIDN:CAA36603.1; !1PID:g57841 GENETICS !$#gene rds CLASSIFICATION #superfamily retinal degeneration slow protein KEYWORDS glycoprotein; photoreceptor; retina; transmembrane protein FEATURE !$16-39 #domain transmembrane #status predicted #label TM1\ !$59-79 #domain transmembrane #status predicted #label TM2\ !$101-122 #domain transmembrane #status predicted #label TM3\ !$261-283 #domain transmembrane #status predicted #label TM4\ !$229 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 346 #molecular-weight 39267 #checksum 6001 SEQUENCE /// ENTRY S03347 #type complete TITLE retinal degeneration slow protein - mouse ALTERNATE_NAMES rds protein ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 22-Jun-1999 ACCESSIONS S03347; I54208 REFERENCE S03347 !$#authors Travis, G.H.; Brennan, M.B.; Danielson, P.E.; Kozak, C.A.; !1Sutcliffe, J.G. !$#journal Nature (1989) 338:70-73 !$#title Identification of a photoreceptor-specific mRNA encoded by !1the gene responsible for retinal degeneration slow (rds). !$#cross-references MUID:89143767; PMID:2918924 !$#accession S03347 !'##molecule_type mRNA !'##residues 1-346 ##label TRA !'##cross-references EMBL:X14770; NID:g53917; PIDN:CAA32878.1; !1PID:g53918 REFERENCE I54208 !$#authors Ma, J.; Norton, J.C.; Allen, A.C.; Burns, J.B.; Hasel, K.W.; !1Burns, J.L.; Sutcliffe, J.G.; Travis, G.H. !$#journal Genomics (1995) 28:212-219 !$#title Retinal degeneration slow (rds) in mouse results from simple !1insertion of a t haplotype-specific element into !1protein-coding exon II. !$#cross-references MUID:96015049; PMID:8530028 !$#accession I54208 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-229 ##label RES !'##cross-references GB:L42167; NID:g975267; PIDN:AAC37674.1; !1PID:g976161 GENETICS !$#gene rds !$#map_position 17 !$#introns 194/2 CLASSIFICATION #superfamily retinal degeneration slow protein KEYWORDS glycoprotein; photoreceptor; retina; transmembrane protein FEATURE !$16-39 #domain transmembrane #status predicted #label TM1\ !$59-79 #domain transmembrane #status predicted #label TM2\ !$101-122 #domain transmembrane #status predicted #label TM3\ !$261-283 #domain transmembrane #status predicted #label TM4\ !$53,229 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 346 #molecular-weight 39259 #checksum 7862 SEQUENCE /// ENTRY A34608 #type complete TITLE retinal degeneration slow protein - bovine ALTERNATE_NAMES rds protein; retinal peripherin ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 02-Jun-2000 ACCESSIONS A34608; B34608 REFERENCE A34608 !$#authors Connell, G.J.; Molday, R.S. !$#journal Biochemistry (1990) 29:4691-4698 !$#title Molecular cloning, primary structure, and orientation of the !1vertebrate photoreceptor cell protein peripherin in the rod !1outer segment disk membrane. !$#cross-references MUID:90321927; PMID:2372552 !$#accession A34608 !'##molecule_type mRNA !'##residues 6-345 ##label CON !'##cross-references GB:J02884; NID:g163505; PIDN:AAA30693.1; !1PID:g163506 !$#accession B34608 !'##molecule_type protein !'##residues 1-32;293-306 ##label CO2 CLASSIFICATION #superfamily retinal degeneration slow protein KEYWORDS glycoprotein; photoreceptor; retina; transmembrane protein FEATURE !$15-38 #domain transmembrane #status predicted #label TM1\ !$58-78 #domain transmembrane #status predicted #label TM2\ !$100-121 #domain transmembrane #status predicted #label TM3\ !$260-282 #domain transmembrane #status predicted #label TM4\ !$52,228 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 345 #molecular-weight 38992 #checksum 8604 SEQUENCE /// ENTRY A40402 #type complete TITLE CD9 antigen [validated] - human ALTERNATE_NAMES motility-related protein-1 ORGANISM #formal_name Homo sapiens #common_name man DATE 06-Dec-1991 #sequence_revision 07-Jul-1995 #text_change 08-Dec-2000 ACCESSIONS A46123; A40402; JH0555; A39029; S10564 REFERENCE A46123 !$#authors Rubinstein, E.; Benoit, P.; Billard, M.; Plaisance, S.; !1Prenant, M.; Uzan, G.; Boucheix, C. !$#journal Genomics (1993) 16:132-138 !$#title Organization of the human CD9 gene. !$#cross-references MUID:93252369; PMID:8486348 !$#accession A46123 !'##molecule_type DNA !'##residues 1-228 ##label RUB !'##cross-references GB:S60489; NID:g300112; PIDN:AAC60586.1; !1PID:g300115 !'##experimental_source leukocyte !'##note sequence extracted from NCBI backbone (NCBIN:131318, !1NCBIN:131326, NCBIN:131328, NCBIN:131330, NCBIN:131332, !1NCBIN:131334, NCBIN:131336, NCBIN:131339, NCBIP:131345) REFERENCE A40402 !$#authors Lanza, F.; Wolf, D.; Fox, C.F.; Kieffer, N.; Seyer, J.M.; !1Fried, V.A.; Coughlin, S.R.; Phillips, D.R.; Jennings, L.K. !$#journal J. Biol. Chem. (1991) 266:10638-10645 !$#title cDNA cloning and expression of platelet p24/CD9. Evidence !1for a new family of multiple membrane-spanning proteins. !$#cross-references MUID:91244846; PMID:2037603 !$#accession A40402 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-228 ##label LAN !'##cross-references GB:L34068; GB:M61880; NID:g508495; PIDN:AAA59982.1; !1PID:g508496 !'##note parts of this sequence, including the amino end of the mature !1protein, were confirmed by peptide sequencing REFERENCE JH0555 !$#authors Miyake, M.; Koyama, M.; Seno, M.; Ikeyama, S. !$#journal J. Exp. Med. (1991) 174:1347-1354 !$#title Identification of the motility-related protein (MRP-1), !1recognized by monoclonal antibody M31-15, which inhibits !1cell motility. !$#cross-references MUID:92078843; PMID:1720807 !$#accession JH0555 !'##molecule_type mRNA !'##residues 1-228 ##label MIY !'##cross-references GB:X60111; NID:g34768; PIDN:CAA42708.1; PID:g34769 !'##experimental_source breast carcinoma !'##note this protein has the epitope defined by cell !1motility-inhibiting monoclonal antibody REFERENCE A39029 !$#authors Boucheix, C.; Benoit, P.; Frachet, P.; Billard, M.; !1Worthington, R.E.; Gagnon, J.; Uzan, G. !$#journal J. Biol. Chem. (1991) 266:117-122 !$#title Molecular cloning of the CD9 antigen. A new family of cell !1surface proteins. !$#cross-references MUID:91093112; PMID:1840589 !$#accession A39029 !'##molecule_type mRNA !'##residues 1-8,'S',10-66,'A',68-193,195-228 ##label BOU !'##cross-references GB:M38690 !'##note parts of this sequence, including the amino end of the mature !1protein, were confirmed by peptide sequencing REFERENCE S10564 !$#authors Higashihara, M.; Takahata, K.; Yatomi, Y.; Nakahara, K.; !1Kurokawa, K. !$#journal FEBS Lett. (1990) 264:270-274 !$#title Purification and partial characterization of CD9 antigen of !1human platelets. !$#cross-references MUID:90292223; PMID:2358073 !$#accession S10564 !'##molecule_type protein !'##residues 2-8,'X',10-21 ##label HIG GENETICS !$#gene GDB:CD9; MIC3 !'##cross-references GDB:120582; OMIM:143030 !$#map_position 12p13-12p13 CLASSIFICATION #superfamily CD9 antigen KEYWORDS glycoprotein; transmembrane protein FEATURE !$2-228 #product CD9 antigen #status experimental #label MAT\ !$2-11 #domain intracellular #status predicted #label CY1\ !$12-35 #domain transmembrane #status predicted #label TM1\ !$36-55 #domain extracellular #status predicted #label EX1\ !$56-82 #domain transmembrane #status predicted #label TM2\ !$83-86 #domain intracellular #status predicted #label CY2\ !$87-111 #domain transmembrane #status predicted #label TM3\ !$112-194 #domain extracellular #status predicted #label EX2\ !$195-221 #domain transmembrane #status predicted #label TM4\ !$222-228 #domain intracellular #status predicted #label CY3\ !$53 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 228 #molecular-weight 25416 #checksum 5114 SEQUENCE /// ENTRY A42929 #type complete TITLE CD9 antigen - green monkey ALTERNATE_NAMES 27K diphtheria toxin receptor-associated protein DRAP27 ORGANISM #formal_name Cercopithecus aethiops #common_name green monkey, grivet DATE 01-Oct-1992 #sequence_revision 09-Aug-1996 #text_change 16-Jun-2000 ACCESSIONS A42929 REFERENCE A42929 !$#authors Mitamura, T.; Iwamoto, R.; Umata, T.; Yomo, T.; Urabe, I.; !1Tsuneoka, M.; Mekada, E. !$#journal J. Cell Biol. (1992) 118:1389-1399 !$#title The 27-kD diphtheria toxin receptor-associated protein !1(DRAP27) from vero cells is the monkey homologue of human !1CD9 antigen: expression of DRAP27 elevates the number of !1diphtheria toxin receptors on toxin-sensitive cells. !$#cross-references MUID:92394967; PMID:1522113 !$#accession A42929 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-228 ##label MIT !'##cross-references GB:D10726; NID:g218565; PIDN:BAA01569.1; !1PID:g218566 CLASSIFICATION #superfamily CD9 antigen KEYWORDS glycoprotein; transmembrane protein FEATURE !$2-228 #product CD9 antigen #status predicted #label MAT\ !$2-11 #domain intracellular #status predicted #label CY1\ !$12-35 #domain transmembrane #status predicted #label TM1\ !$36-55 #domain extracellular #status predicted #label EX1\ !$56-82 #domain transmembrane #status predicted #label TM2\ !$83-86 #domain intracellular #status predicted #label CY2\ !$87-111 #domain transmembrane #status predicted #label TM3\ !$112-194 #domain extracellular #status predicted #label EX2\ !$195-221 #domain transmembrane #status predicted #label TM4\ !$222-228 #domain intracellular #status predicted #label CY3\ !$52,53 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 228 #molecular-weight 25431 #checksum 4653 SEQUENCE /// ENTRY S39262 #type complete TITLE CD9 antigen - rat ALTERNATE_NAMES platelet cell surface glycoprotein ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 06-Jan-1995 #sequence_revision 09-Aug-1996 #text_change 22-Jun-1999 ACCESSIONS I56562; S39262 REFERENCE I56562 !$#authors Kaprielian, Z.; Cho, K.O.; Hadjiargyrou, M.; Patterson, P.H. !$#journal J. Neurosci. (1995) 15:562-573 !$#title CD9, a major platelet cell surface glycoprotein, is a ROCA !1antigen and is expressed in the nervous system. !$#cross-references MUID:95123481; PMID:7823164 !$#accession I56562 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-226 ##label RES !'##cross-references EMBL:X76489; NID:g434314; PIDN:CAA54027.1; !1PID:g434315 GENETICS !$#gene CD9 CLASSIFICATION #superfamily CD9 antigen KEYWORDS glycoprotein; transmembrane protein FEATURE !$2-11 #domain intracellular #status predicted #label CY1\ !$12-35 #domain transmembrane #status predicted #label TM1\ !$36-53 #domain extracellular #status predicted #label EX1\ !$54-80 #domain transmembrane #status predicted #label TM2\ !$81-84 #domain intracellular #status predicted #label CY2\ !$85-109 #domain transmembrane #status predicted #label TM3\ !$110-192 #domain extracellular #status predicted #label EX2\ !$193-219 #domain transmembrane #status predicted #label TM4\ !$220-226 #domain intracellular #status predicted #label CY3\ !$50 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 226 #molecular-weight 25215 #checksum 7514 SEQUENCE /// ENTRY JX0221 #type complete TITLE CD9 antigen - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 09-Oct-1992 #sequence_revision 09-Aug-1996 #text_change 22-Jun-1999 ACCESSIONS JX0221 REFERENCE JX0221 !$#authors Martin-Alonso, J.M.; Hernando, N.; Ghosh, S.; Coca-Prados, !1M. !$#journal J. Biochem. (1992) 112:63-67 !$#title Molecular cloning of the bovine CD9 antigen from ocular !1ciliary epithelial cells. !$#cross-references MUID:93054422; PMID:1339429 !$#accession JX0221 !'##molecule_type mRNA !'##residues 1-226 ##label MAR !'##cross-references GB:M81720; NID:g162820; PIDN:AAA30439.1; !1PID:g162821 !'##experimental_source ocular ciliary epithelial cell CLASSIFICATION #superfamily CD9 antigen KEYWORDS glycoprotein; transmembrane protein FEATURE !$2-226 #product CD9 antigen #status predicted #label MAT\ !$2-11 #domain intracellular #status predicted #label CY1\ !$12-35 #domain transmembrane #status predicted #label TM1\ !$36-53 #domain extracellular #status predicted #label EX1\ !$54-76 #domain transmembrane #status predicted #label TM2\ !$77-80 #domain intracellular #status predicted #label CY2\ !$81-109 #domain transmembrane #status predicted #label TM3\ !$110-192 #domain extracellular #status predicted #label EX2\ !$193-219 #domain transmembrane #status predicted #label TM4\ !$220-226 #domain intracellular #status predicted #label CY3\ !$50 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 226 #molecular-weight 25258 #checksum 9275 SEQUENCE /// ENTRY A35649 #type complete TITLE cell surface protein TAPA-1 - human ALTERNATE_NAMES target of antiproliferative antibody (TAPA) 1 ORGANISM #formal_name Homo sapiens #common_name man DATE 28-Sep-1990 #sequence_revision 09-Aug-1996 #text_change 22-Jun-1999 ACCESSIONS A35649 REFERENCE A35649 !$#authors Oren, R.; Takahashi, S.; Doss, C.; Levy, R.; Levy, S. !$#journal Mol. Cell. Biol. (1990) 10:4007-4015 !$#title TAPA-1, the target of an antiproliferative antibody, defines !1a new family of transmembrane proteins. !$#cross-references MUID:90318365; PMID:1695320 !$#accession A35649 !'##molecule_type mRNA !'##residues 1-236 ##label ORE !'##cross-references GB:M33680; NID:g338677; PIDN:AAA36663.1; !1PID:g338678 GENETICS !$#gene GDB:TAPA1 !'##cross-references GDB:135038; OMIM:186845 !$#map_position 11p15.5-11p15.5 CLASSIFICATION #superfamily CD9 antigen KEYWORDS transmembrane protein FEATURE !$2-11 #domain intracellular #status predicted #label CY1\ !$12-35 #domain transmembrane #status predicted #label TM1\ !$36-57 #domain extracellular #status predicted #label EX1\ !$58-84 #domain transmembrane #status predicted #label TM2\ !$85-88 #domain intracellular #status predicted #label CY2\ !$89-113 #domain transmembrane #status predicted #label TM3\ !$114-203 #domain extracellular #status predicted #label EX2\ !$204-230 #domain transmembrane #status predicted #label TM4\ !$231-236 #domain intracellular #status predicted #label CY3 SUMMARY #length 236 #molecular-weight 25809 #checksum 2159 SEQUENCE /// ENTRY A46472 #type complete TITLE cell surface protein TAPA-1 - mouse ALTERNATE_NAMES target of antiproliferative antibody (TAPA) 1 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 18-Jun-1993 #sequence_revision 09-Aug-1996 #text_change 22-Jun-1999 ACCESSIONS A46472 REFERENCE A46472 !$#authors Andria, M.L.; Hsieh, C.L.; Oren, R.; Francke, U.; Levy, S. !$#journal J. Immunol. (1991) 147:1030-1036 !$#title Genomic organization and chromosomal localization of the !1TAPA-1 gene. !$#cross-references MUID:91318144; PMID:1650385 !$#accession A46472 !'##molecule_type DNA !'##residues 1-236 ##label AND !'##cross-references GB:S45012; NID:g1679982; PIDN:AAB19417.1; !1PID:g233253 !'##experimental_source B-cell lymphoma line 38C13 !'##note sequence extracted from NCBI backbone (NCBIN:44957, !1NCBIN:44966, NCBIN:45001, NCBIN:45005, NCBIN:45008, !1NCBIN:45010, NCBIN:45012, NCBIP:45013) CLASSIFICATION #superfamily CD9 antigen KEYWORDS transmembrane protein FEATURE !$2-11 #domain intracellular #status predicted #label CY1\ !$12-35 #domain transmembrane #status predicted #label TM1\ !$36-57 #domain extracellular #status predicted #label EX1\ !$58-84 #domain transmembrane #status predicted #label TM2\ !$85-88 #domain intracellular #status predicted #label CY2\ !$89-113 #domain transmembrane #status predicted #label TM3\ !$114-203 #domain extracellular #status predicted #label EX2\ !$204-230 #domain transmembrane #status predicted #label TM4\ !$231-236 #domain intracellular #status predicted #label CY3 SUMMARY #length 236 #molecular-weight 25828 #checksum 3063 SEQUENCE /// ENTRY A37243 #type complete TITLE hemopoietic cell surface glycoprotein CD53 - human ALTERNATE_NAMES pan-leukocyte surface antigen CD53 ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Dec-1991 #sequence_revision 09-Aug-1996 #text_change 22-Jun-1999 ACCESSIONS A37243; A45872 REFERENCE A37243 !$#authors Amiot, M. !$#journal J. Immunol. (1990) 145:4322-4325 !$#title Identification and analysis of cDNA clones encoding CD53. A !1pan-leukocyte antigen related to membrane transport !1proteins. !$#cross-references MUID:91079522; PMID:2258620 !$#accession A37243 !'##molecule_type mRNA !'##residues 1-219 ##label AMI !'##cross-references GB:M60871; NID:g180140; PIDN:AAA51951.1; !1PID:g180141 REFERENCE A45872 !$#authors Angelisova, P.; Vlcek, C.; Stefanova, I.; Lipoldova, M.; !1Horejsi, V. !$#journal Immunogenetics (1990) 32:281-285 !$#title The human leucocyte surface antigen CD53 is a protein !1structurally similar to the CD37 and MRC OX-44 antigens. !$#cross-references MUID:91055810; PMID:1700763 !$#accession A45872 !'##molecule_type mRNA !'##residues 1-219 ##label ANG !'##cross-references GB:M37033; NID:g180142; PIDN:AAA35663.1; !1PID:g180143 GENETICS !$#gene GDB:CD53; MOX44 !'##cross-references GDB:127521; OMIM:151525 !$#map_position 1p21-1p13.3 CLASSIFICATION #superfamily CD9 antigen KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-10 #domain intracellular #status predicted #label CY1\ !$11-36 #domain transmembrane #status predicted #label TM1\ !$37-54 #domain extracellular #status predicted #label EX1\ !$55-75 #domain transmembrane #status predicted #label TM2\ !$76-80 #domain intracellular #status predicted #label CY2\ !$81-106 #domain transmembrane #status predicted #label TM3\ !$107-181 #domain extracellular #status predicted #label EX2\ !$182-204 #domain transmembrane #status predicted #label TM4\ !$205-219 #domain intracellular #status predicted #label CY3\ !$129,148 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 219 #molecular-weight 24341 #checksum 7618 SEQUENCE /// ENTRY A39574 #type complete TITLE leukocyte antigen OX-44 - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Aug-1991 #sequence_revision 09-Aug-1996 #text_change 22-Jun-1999 ACCESSIONS A39574 REFERENCE A39574 !$#authors Bellacosa, A.; Lazo, P.A.; Bear, S.E.; Tsichlis, P.N. !$#journal Mol. Cell. Biol. (1991) 11:2864-2872 !$#title The rat leukocyte antigen MRC OX-44 is a member of a new !1family of cell surface proteins which appear to be involved !1in growth regulation. !$#cross-references MUID:91203909; PMID:2017181 !$#accession A39574 !'##molecule_type mRNA !'##residues 1-219 ##label BEL !'##cross-references GB:M57276; NID:g205897; PIDN:AAA41775.1; !1PID:g205898 CLASSIFICATION #superfamily CD9 antigen KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-10 #domain intracellular #status predicted #label CY1\ !$11-36 #domain transmembrane #status predicted #label TM1\ !$37-54 #domain extracellular #status predicted #label EX1\ !$55-73 #domain transmembrane #status predicted #label TM2\ !$74-79 #domain intracellular #status predicted #label CY2\ !$80-106 #domain transmembrane #status predicted #label TM3\ !$107-181 #domain extracellular #status predicted #label EX2\ !$182-204 #domain transmembrane #status predicted #label TM4\ !$205-219 #domain intracellular #status predicted #label CY3\ !$119,129,148 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 219 #molecular-weight 24168 #checksum 9151 SEQUENCE /// ENTRY A36056 #type complete TITLE tumor-associated antigen CO-029 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 16-Nov-1990 #sequence_revision 09-Aug-1996 #text_change 20-Apr-2000 ACCESSIONS A36056 REFERENCE A36056 !$#authors Szala, S.; Kasai, Y.; Steplewski, Z.; Rodeck, U.; Koprowski, !1H.; Linnenbach, A.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:6833-6837 !$#title Molecular cloning of cDNA for the human tumor-associated !1antigen CO-029 and identification of related transmembrane !1antigens. !$#cross-references MUID:90370878; PMID:2395876 !$#accession A36056 !'##molecule_type mRNA !'##residues 1-237 ##label SZA !'##cross-references GB:M35252; NID:g180925; PIDN:AAA35709.1; !1PID:g180926 GENETICS !$#gene GDB:TM4SF3 !'##cross-references GDB:9113496; OMIM:600769 CLASSIFICATION #superfamily CD9 antigen KEYWORDS glycoprotein; transmembrane protein FEATURE !$2-11 #domain intracellular #status predicted #label CY1\ !$12-33 #domain transmembrane #status predicted #label TM1\ !$34-52 #domain extracellular #status predicted #label EX1\ !$53-78 #domain transmembrane #status predicted #label TM2\ !$79-82 #domain intracellular #status predicted #label CY2\ !$83-107 #domain transmembrane #status predicted #label TM3\ !$108-205 #domain extracellular #status predicted #label EX2\ !$206-232 #domain transmembrane #status predicted #label TM4\ !$233-237 #domain intracellular #status predicted #label CY3\ !$37,118 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 237 #molecular-weight 26044 #checksum 1616 SEQUENCE /// ENTRY A46493 #type complete TITLE metastasis suppressor KAI1 - human ALTERNATE_NAMES cell surface glycoprotein KAI1; membrane protein R2, inducible; type III integral membrane protein C33 ORGANISM #formal_name Homo sapiens #common_name man DATE 18-Jun-1993 #sequence_revision 09-Aug-1996 #text_change 22-Jun-1999 ACCESSIONS I38942; S16156; A46493 REFERENCE I38942 !$#authors Dong, J.T.; Lamb, P.W.; Rinker-Schaeffer, C.W.; Vukanovic, !1J.; Ichikawa, T.; Isaacs, J.T.; Barrett, J.C. !$#journal Science (1995) 268:884-886 !$#title KAI1, a metastasis suppressor gene for prostate cancer on !1human chromosome 11p11.2. !$#cross-references MUID:95273964; PMID:7754374 !$#accession I38942 !'##status nucleic acid sequence not shown; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-267 ##label RES !'##cross-references EMBL:U20770; NID:g806805; PIDN:AAC50133.1; !1PID:g806806 REFERENCE S16156 !$#authors Gaugitsch, H.W.; Hofer, E.; Huber, N.E.; Schnabl, E.; !1Baumruker, T. !$#journal Eur. J. Immunol. (1991) 21:377-383 !$#title A new superfamily of lymphoid and melanoma cell proteins !1with extensive homology to Schistosoma mansoni antigen Sm23. !$#cross-references MUID:91153380; PMID:1842498 !$#accession S16156 !'##status preliminary !'##molecule_type mRNA !'##residues 1-267 ##label GAU !'##cross-references EMBL:X53795; NID:g35832; PIDN:CAA37804.1; !1PID:g35833 !'##note the authors translated the codon AGC for residue 50 as Thr REFERENCE A46493 !$#authors Imai, T.; Fukudome, K.; Takagi, S.; Nagira, M.; Furuse, M.; !1Fukuhara, N.; Nishimura, M.; Hinuma, Y.; Yoshie, O. !$#journal J. Immunol. (1992) 149:2879-2886 !$#title C33 antigen recognized by monoclonal antibodies inhibitory !1to human T cell leukemia virus type 1-induced syncytium !1formation is a member of a new family of transmembrane !1proteins including CD9, CD37, CD53, and CD63. !$#cross-references MUID:93017900; PMID:1401919 !$#accession A46493 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-239,'MV',242-267 ##label IMA !'##cross-references GB:S48196; NID:g258294; PIDN:AAB23825.1; !1PID:g258295 !'##experimental_source T-cell line MOLT-4 !'##note sequence extracted from NCBI backbone (NCBIP:117149) GENETICS !$#gene GDB:KAI1 !'##cross-references GDB:134216; OMIM:600623 !$#map_position 11p11.2-11p11.2 CLASSIFICATION #superfamily CD9 antigen KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-10 #domain intracellular #status predicted #label CY1\ !$11-36 #domain transmembrane #status predicted #label TM1\ !$37-57 #domain extracellular #status predicted #label EX1\ !$58-78 #domain transmembrane #status predicted #label TM2\ !$79-83 #domain intracellular #status predicted #label CY2\ !$84-108 #domain transmembrane #status predicted #label TM3\ !$109-227 #domain extracellular #status predicted #label EX2\ !$228-252 #domain transmembrane #status predicted #label TM4\ !$253-265 #domain intracellular #status predicted #label CY3\ !$129,157,198 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 267 #molecular-weight 29625 #checksum 6167 SEQUENCE /// ENTRY A47629 #type complete TITLE cell surface glycoprotein CD37 - human ALTERNATE_NAMES leukocyte antigen CD37 ORGANISM #formal_name Homo sapiens #common_name man DATE 03-Feb-1994 #sequence_revision 09-Aug-1996 #text_change 22-Jun-1999 ACCESSIONS A47629; JL0093; JC1500 REFERENCE A47629 !$#authors Classon, B.J.; Williams, A.F.; Willis, A.C.; Seed, B.; !1Stamenkovic, I. !$#journal J. Exp. Med. (1990) 172:1007 !$#cross-references MUID:90354767; PMID:2388030 !$#contents erratum !$#accession A47629 !'##molecule_type mRNA !'##residues 1-281 ##label CLA !'##cross-references EMBL:X14046; NID:g29793; PIDN:CAA32204.1; !1PID:g29794 !'##note this is a revision to the sequence from reference JL0093 REFERENCE JL0093 !$#authors Classon, B.J.; Williams, A.F.; Willis, A.C.; Seed, B.; !1Stamenkovic, I. !$#journal J. Exp. Med. (1989) 169:1497-1502 !$#title The primary structure of the human leukocyte antigen CD37, a !1species homologue of the rat MRC OX-44 antigen. !$#cross-references MUID:89176904; PMID:2466944 !$#accession JL0093 !'##molecule_type mRNA !'##residues 1-228,'AARRASRSGCTTT',242,'FP' ##label CL2 !'##experimental_source patient with chronic lymphocytic leukemia COMMENT This antigen is expressed abundantly on B lymphocytes and is !1also seen at lower levels on T-cells, some thymocytes, !1neutrophils, monocytes, and macrophages. COMMENT This antigen inhibits the activation of B-cells induced by !1CD20 antibodies plus B-cell growth factor. GENETICS !$#gene GDB:CD37 !'##cross-references GDB:138750; OMIM:151523 !$#map_position 19p13-19q13.4 CLASSIFICATION #superfamily CD9 antigen KEYWORDS glycoprotein; lymphocyte; transmembrane protein FEATURE !$1-12 #domain intracellular #status predicted #label CY1\ !$13-38 #domain transmembrane #status predicted #label TM1\ !$39-59 #domain extracellular #status predicted #label EX1\ !$60-80 #domain transmembrane #status predicted #label TM2\ !$81-85 #domain intracellular #status predicted #label CY2\ !$86-110 #domain transmembrane #status predicted #label TM3\ !$111-241 #domain extracellular #status predicted #label EX2\ !$242-267 #domain transmembrane #status predicted #label TM4\ !$268-278 #domain intracellular #status predicted #label CY3\ !$170,183,188 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 281 #molecular-weight 31703 #checksum 3716 SEQUENCE /// ENTRY B47629 #type complete TITLE cell surface glycoprotein CD37 - rat ALTERNATE_NAMES leukocyte antigen CD37 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 03-Feb-1994 #sequence_revision 09-Aug-1996 #text_change 22-Jun-1999 ACCESSIONS B47629; JC1501 REFERENCE A47629 !$#authors Classon, B.J.; Williams, A.F.; Willis, A.C.; Seed, B.; !1Stamenkovic, I. !$#journal J. Exp. Med. (1990) 172:1007 !$#cross-references MUID:90354767; PMID:2388030 !$#accession B47629 !'##molecule_type mRNA !'##residues 1-281 ##label CLA !'##cross-references EMBL:X53517; NID:g55911; PIDN:CAA37596.1; !1PID:g55912 COMMENT This antigen is expressed abundantly on B lymphocytes and is !1also seen at lower levels on T-cells, some thymocytes, !1neutrophils, monocytes, and macrophages. CLASSIFICATION #superfamily CD9 antigen KEYWORDS glycoprotein; lymphocyte; transmembrane protein FEATURE !$2-12 #domain intracellular #status predicted #label CY1\ !$13-38 #domain transmembrane #status predicted #label TM1\ !$39-59 #domain extracellular #status predicted #label EX1\ !$60-80 #domain transmembrane #status predicted #label TM2\ !$81-85 #domain intracellular #status predicted #label CY2\ !$86-110 #domain transmembrane #status predicted #label TM3\ !$111-241 #domain extracellular #status predicted #label EX2\ !$242-267 #domain transmembrane #status predicted #label TM4\ !$268-278 #domain intracellular #status predicted #label CY3\ !$170,183,188 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 281 #molecular-weight 31750 #checksum 3957 SEQUENCE /// ENTRY I38016 #type complete TITLE melanoma-associated antigen CD63 [validated] - human ALTERNATE_NAMES antigen ME491; lysosomal membrane glycoprotein CD63; ME491/ CD63 antigen; ocular melanoma-associated antigen OMA81H; platelet activation antigen Pltgp40; platelet glycoprotein, 40K ORGANISM #formal_name Homo sapiens #common_name man DATE 17-May-1996 #sequence_revision 09-Aug-1996 #text_change 08-Dec-2000 ACCESSIONS I38016; S01418; A39514; B35826; A61177; A61173; A56782 REFERENCE I38016 !$#authors Hotta, H.; Miyamoto, H.; Hara, I.; Takahashi, N.; Homma, M. !$#journal Biochem. Biophys. Res. Commun. (1992) 185:436-442 !$#title Genomic structure of the ME491/CD63 antigen gene and !1functional analysis of the 5'-flanking regulatory sequences. !$#cross-references MUID:92287132; PMID:1599482 !$#accession I38016 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-238 ##label RES !'##cross-references EMBL:X62654; NID:g430755; PIDN:CAA44519.1; !1PID:g430756 REFERENCE S01418 !$#authors Hotta, H.; Ross, A.H.; Huebner, K.; Isobe, M.; Wendeborn, !1S.; Chao, M.V.; Ricciardi, R.P.; Tsujimoto, Y.; Croce, C.M.; !1Koprowski, H. !$#journal Cancer Res. (1988) 48:2955-2962 !$#title Molecular cloning and characterization of an antigen !1associated with early stages of melanoma tumor progression. !$#cross-references MUID:88210273; PMID:3365686 !$#accession S01418 !'##molecule_type mRNA !'##residues 1-238 ##label HOT !'##cross-references EMBL:X07982; NID:g34526; PIDN:CAA30792.1; !1PID:g34527 REFERENCE A39514 !$#authors Metzelaar, M.J.; Wijngaard, P.L.J.; Peters, P.J.; Sixma, !1J.J.; Nieuwenhuis, H.K.; Clevers, H.C. !$#journal J. Biol. Chem. (1991) 266:3239-3245 !$#title CD63 antigen. A novel lysosomal membrane glycoprotein, !1cloned by a screening procedure for intracellular antigens !1in eukaryotic cells. !$#cross-references MUID:91131632; PMID:1993697 !$#accession A39514 !'##molecule_type mRNA !'##residues 1-238 ##label MET !'##cross-references GB:M58485 REFERENCE A35826 !$#authors Rapp, G.; Freudenstein, J.; Klaudiny, J.; Mucha, J.; Wempe, !1F.; Zimmer, M.; Scheit, K.H. !$#journal DNA Cell Biol. (1990) 9:479-485 !$#title Characterization of three abundant mRNAs from human ovarian !1granulosa cells. !$#cross-references MUID:91025550; PMID:2171551 !$#accession B35826 !'##molecule_type mRNA !'##residues 1-238 ##label RAP !'##cross-references GB:M59907; NID:g189383; PIDN:AAA63235.1; !1PID:g189384 !'##note the authors did not translate the codons for residues 205 !1through 224 REFERENCE A61177 !$#authors Azorsa, D.O.; Hyman, J.A.; Hildreth, J.E.K. !$#journal Blood (1991) 78:280-284 !$#title CD63/Pltgp40: a platelet activation antigen identical to the !1stage-specific, melanoma-associated antigen ME491. !$#cross-references MUID:91300080; PMID:2070066 !$#accession A61177 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type mRNA !'##residues 2-68,'P',70-238 ##label AZO REFERENCE A61173 !$#authors Hildreth, J.E.K.; Derr, D.; Azorsa, D.O. !$#journal Blood (1991) 77:121-132 !$#title Characterization of a novel self-associating Mr 40,000 !1platelet glycoprotein. !$#cross-references MUID:91084576; PMID:1984792 !$#accession A61173 !'##molecule_type protein !'##residues 2-8,'X',10-16,'XX',19-21 ##label HIL REFERENCE A56782 !$#authors Wang, M.X.; Earley Jr., J.J.; Shields, J.A.; Donoso, L.A. !$#journal Arch. Ophthalmol. (1992) 110:399-404 !$#title An ocular melanoma-associated antigen. Molecular !1characterization. !$#cross-references MUID:92181348; PMID:1339263 !$#accession A56782 !'##molecule_type mRNA !'##residues 1-238 ##label WAN !'##cross-references GB:S93788; NID:g246538; PIDN:AAB21617.1; !1PID:g246539 !'##experimental_source uveal melanoma !'##note sequence extracted from NCBI backbone (NCBIN:93788, !1NCBIP:93790) GENETICS !$#gene GDB:CD63; MLA1 !'##cross-references GDB:120186; OMIM:155740 !$#map_position 12q12-12q13 !$#introns 22/3; 85/3; 110/3; 142/3; 189/3; 217/3 CLASSIFICATION #superfamily CD9 antigen KEYWORDS glycoprotein; lysosome; surface antigen; transmembrane !1protein FEATURE !$2-238 #product melanoma-associated antigen ME491 #status !8experimental #label MAT\ !$2-11 #domain intracellular #status predicted #label CY1\ !$12-35 #domain transmembrane #status predicted #label TM1\ !$36-51 #domain extracellular #status predicted #label EX1\ !$52-76 #domain transmembrane #status predicted #label TM2\ !$77-80 #domain intracellular #status predicted #label CY2\ !$81-103 #domain transmembrane #status predicted #label TM3\ !$104-202 #domain extracellular #status predicted #label EX2\ !$203-228 #domain transmembrane #status predicted #label TM4\ !$229-238 #domain intracellular #status predicted #label CY3\ !$130,150,172 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 238 #molecular-weight 25636 #checksum 2473 SEQUENCE /// ENTRY JC2297 #type complete TITLE CD63 antigen - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 28-Oct-1994 #sequence_revision 09-Aug-1996 #text_change 16-Jun-2000 ACCESSIONS JC2297 REFERENCE JC2297 !$#authors Sohma, Y.; Suzuki, T.; Sasano, H.; Nagura, H.; Nose, M.; !1Yamamoto, T. !$#journal Cell Struct. Funct. (1994) 19:219-225 !$#title Increased mRNA for CD63 antigen in atherosclerotic lesions !1of Watanable heritable hyperlipidemic rabbits. !$#cross-references MUID:95120837; PMID:7820873 !$#accession JC2297 !'##molecule_type mRNA !'##residues 1-238 ##label SOH !'##cross-references DDBJ:D21264; NID:g684973; PIDN:BAA04804.1; !1PID:g684974 !'##experimental_source aorta CLASSIFICATION #superfamily CD9 antigen KEYWORDS glycoprotein; lysosome; surface antigen; transmembrane !1protein FEATURE !$1-11 #domain intracellular #status predicted #label CY1\ !$12-35 #domain transmembrane #status predicted #label TM1\ !$36-51 #domain extracellular #status predicted #label EX1\ !$52-76 #domain transmembrane #status predicted #label TM2\ !$77-80 #domain intracellular #status predicted #label CY2\ !$81-103 #domain transmembrane #status predicted #label TM3\ !$104-202 #domain extracellular #status predicted #label EX2\ !$203-228 #domain transmembrane #status predicted #label TM4\ !$229-238 #domain intracellular #status predicted #label CY3\ !$125,130,150,172 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 238 #molecular-weight 25629 #checksum 4636 SEQUENCE /// ENTRY S43511 #type complete TITLE CD63/ME491 antigen homolog - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 13-Jan-1995 #sequence_revision 09-Aug-1996 #text_change 16-Jun-2000 ACCESSIONS S43511 REFERENCE S43511 !$#authors Miyamoto, H.; Homma, M.; Hotta, H. !$#journal Biochim. Biophys. Acta (1994) 1217:312-316 !$#title Molecular cloning of the murine homologue of CD63/ME491 and !1detection of its strong expression in the kidney and !1activated macrophages. !$#cross-references MUID:94198294; PMID:8148377 !$#accession S43511 !'##molecule_type mRNA !'##residues 1-238 ##label MIY !'##cross-references EMBL:D16432; NID:g484052; PIDN:BAA03904.1; !1PID:g976238 CLASSIFICATION #superfamily CD9 antigen KEYWORDS glycoprotein; lysosome; surface antigen; transmembrane !1protein FEATURE !$1-11 #domain intracellular #status predicted #label CY1\ !$12-35 #domain transmembrane #status predicted #label TM1\ !$36-51 #domain extracellular #status predicted #label EX1\ !$52-76 #domain transmembrane #status predicted #label TM2\ !$77-80 #domain intracellular #status predicted #label CY2\ !$81-103 #domain transmembrane #status predicted #label TM3\ !$104-202 #domain extracellular #status predicted #label EX2\ !$203-228 #domain transmembrane #status predicted #label TM4\ !$229-238 #domain intracellular #status predicted #label CY3\ !$116,130,150,172 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 238 #molecular-weight 25766 #checksum 2579 SEQUENCE /// ENTRY A46508 #type complete TITLE CD63/ME491 antigen homolog - rat ALTERNATE_NAMES mast cell antigen AD1 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 18-Jun-1993 #sequence_revision 09-Aug-1996 #text_change 22-Jun-1999 ACCESSIONS A46508; S16776 REFERENCE A46508 !$#authors Nishikata, H.; Oliver, C.; Mergenhagen, S.E.; Siraganian, !1R.P. !$#journal J. Immunol. (1992) 149:862-870 !$#title The rat mast cell antigen AD1 (homologue to human CD63 or !1melanoma antigen ME491) is expressed in other cells in !1culture. !$#cross-references MUID:92340890; PMID:1634775 !$#accession A46508 !'##molecule_type mRNA !'##residues 1-238 ##label NIS !'##cross-references EMBL:X61654; NID:g55601; PIDN:CAA43835.1; !1PID:g55602 !'##note this antigen was found localized to mast cells in tissue !1samples, but was induced in a number of cell types by tissue !1culture conditions !'##note sequence extracted from NCBI backbone (NCBIN:109346, !1NCBIP:109349) COMMENT This heavily glycosylated protein of 50-60K (27K after !1deglycosylation) is found sterically close to the high !1affinity IgE receptor. CLASSIFICATION #superfamily CD9 antigen KEYWORDS glycoprotein; lysosome; mast cell; surface antigen; !1transmembrane protein FEATURE !$1-11 #domain intracellular #status predicted #label CY1\ !$12-35 #domain transmembrane #status predicted #label TM1\ !$36-51 #domain extracellular #status predicted #label EX1\ !$52-76 #domain transmembrane #status predicted #label TM2\ !$77-80 #domain intracellular #status predicted #label CY2\ !$81-103 #domain transmembrane #status predicted #label TM3\ !$104-202 #domain extracellular #status predicted #label EX2\ !$203-228 #domain transmembrane #status predicted #label TM4\ !$229-238 #domain intracellular #status predicted #label CY3\ !$130,150,172 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 238 #molecular-weight 25698 #checksum 3181 SEQUENCE /// ENTRY I39368 #type complete TITLE T-cell acute lymphoblastic leukemia associated antigen 1 - human ALTERNATE_NAMES cell surface glycoprotein (clone A15); TALLA-1 ORGANISM #formal_name Homo sapiens #common_name man DATE 23-Feb-1996 #sequence_revision 23-Aug-1996 #text_change 22-Jun-1999 ACCESSIONS I39368; I54784 REFERENCE I39368 !$#authors Emi, N.; Kitaori, K.; Seto, M.; Ueda, R.; Saito, H.; !1Takahashi, T. !$#journal Immunogenetics (1993) 37:193-198 !$#title Isolation of a novel cDNA clone showing marked similarity to !1ME491/CD63 superfamily. !$#cross-references MUID:93131291; PMID:8420826 !$#accession I39368 !'##molecule_type mRNA !'##residues 1-244 ##label RES !'##cross-references GB:D10653; NID:g285900; PIDN:BAA01501.1; !1PID:g285901 !'##experimental_source immature T cell line HPB-ALL REFERENCE I54784 !$#authors Takagi, S.; Fujikawa, K.; Imai, T.; Fukuhara, N.; Fukudome, !1K.; Minegishi, M.; Tsuchiya, S.; Konno, T.; Hinuma, Y.; !1Yoshie, O. !$#journal Int. J. Cancer (1995) 61:706-715 !$#title Identification of a highly specific surface marker of T-cell !1acute lymphoblastic leukemia and neuroblastoma as a new !1member of the transmembrane 4 superfamily. !$#cross-references MUID:95286314; PMID:7768645 !$#accession I54784 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-244 ##label RE2 !'##cross-references GB:D29808; NID:g475005; PIDN:BAA06191.1; !1PID:g475006 GENETICS !$#gene GDB:MXS1; DXS1692E; A15; TALLA-1 !'##cross-references GDB:202921 !$#map_position Xq11-Xq11 CLASSIFICATION #superfamily CD9 antigen KEYWORDS glycoprotein; surface antigen; transmembrane protein FEATURE !$1-11 #domain intracellular #status predicted #label CY1\ !$12-35 #domain transmembrane #status predicted #label TM1\ !$36-51 #domain extracellular #status predicted #label EX1\ !$52-76 #domain transmembrane #status predicted #label TM2\ !$77-80 #domain intracellular #status predicted #label CY2\ !$81-102 #domain transmembrane #status predicted #label TM3\ !$103-207 #domain extracellular #status predicted #label EX2\ !$208-232 #domain transmembrane #status predicted #label TM4\ !$233-244 #domain intracellular #status predicted #label CY3\ !$49,150,153,172,183 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 244 #molecular-weight 26972 #checksum 5875 SEQUENCE /// ENTRY A40181 #type complete TITLE 23K integral membrane protein - fluke (Schistosoma japonicum) ALTERNATE_NAMES Sj23 ORGANISM #formal_name Schistosoma japonicum DATE 06-Nov-1992 #sequence_revision 09-Aug-1996 #text_change 22-Jun-1999 ACCESSIONS A40181 REFERENCE A40181 !$#authors Davern, K.M.; Wright, M.D.; Herrmann, V.R.; Mitchell, G.F. !$#journal Mol. Biochem. Parasitol. (1991) 48:67-76 !$#title Further characterisation of the Schistosoma japonicum !1protein Sj23, a target antigen of an immunodiagnostic !1monoclonal antibody. !$#cross-references MUID:92140457; PMID:1779990 !$#accession A40181 !'##molecule_type mRNA !'##residues 1-218 ##label DAV !'##cross-references GB:M63706; NID:g161081; PIDN:AAA29920.1; !1PID:g161082 CLASSIFICATION #superfamily CD9 antigen KEYWORDS transmembrane protein FEATURE !$1-13 #domain intracellular #status predicted #label CY1\ !$14-36 #domain transmembrane #status predicted #label TM1\ !$37-56 #domain extracellular #status predicted #label EX1\ !$57-77 #domain transmembrane #status predicted #label TM2\ !$78-82 #domain intracellular #status predicted #label CY2\ !$83-108 #domain transmembrane #status predicted #label TM3\ !$109-183 #domain extracellular #status predicted #label EX2\ !$184-206 #domain transmembrane #status predicted #label TM4\ !$207-218 #domain intracellular #status predicted #label CY3 SUMMARY #length 218 #molecular-weight 23728 #checksum 9603 SEQUENCE /// ENTRY A43522 #type complete TITLE 23K integral membrane protein - fluke (Schistosoma mansoni) ALTERNATE_NAMES Sm23 ORGANISM #formal_name Schistosoma mansoni DATE 28-Oct-1992 #sequence_revision 09-Aug-1996 #text_change 22-Jun-1999 ACCESSIONS A43522 REFERENCE A43522 !$#authors Wright, M.D.; Henkle, K.J.; Mitchell, G.F. !$#journal J. Immunol. (1990) 144:3195-3200 !$#title An immunogenic M-r 23,000 integral membrane protein of !1Schistosoma mansoni worms that closely resembles a human !1tumor-associated antigen. !$#cross-references MUID:90217533; PMID:2324498 !$#accession A43522 !'##molecule_type mRNA !'##residues 1-218 ##label WRI !'##cross-references GB:M34453; NID:g161029; PIDN:AAA29900.1; !1PID:g161030 !'##note observations of molecular weight suggest this protein is at !1most lightly glycosylated CLASSIFICATION #superfamily CD9 antigen KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-13 #domain intracellular #status predicted #label CY1\ !$14-36 #domain transmembrane #status predicted #label TM1\ !$37-56 #domain extracellular #status predicted #label EX1\ !$57-77 #domain transmembrane #status predicted #label TM2\ !$78-82 #domain intracellular #status predicted #label CY2\ !$83-108 #domain transmembrane #status predicted #label TM3\ !$109-183 #domain extracellular #status predicted #label EX2\ !$184-206 #domain transmembrane #status predicted #label TM4\ !$207-218 #domain intracellular #status predicted #label CY3\ !$165 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 218 #molecular-weight 23684 #checksum 9343 SEQUENCE /// ENTRY LNFHLS #type complete TITLE lectin precursor - flesh fly (Sarcophaga peregrina) ORGANISM #formal_name Sarcophaga peregrina DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 16-Jun-2000 ACCESSIONS S07759; S41119; A25736; B25736 REFERENCE S07759 !$#authors Kobayashi, A.; Hirai, H.; Kubo, T.; Ueno, K.; Nakanishi, Y.; !1Natori, S. !$#journal Biochim. Biophys. Acta (1989) 1009:244-250 !$#title Cloning and in vitro transcription of the Sarcophaga lectin !1gene. !$#cross-references MUID:90089397; PMID:2480809 !$#accession S07759 !'##molecule_type DNA !'##residues 1-38 ##label KOB !'##cross-references EMBL:X16659; NID:g10271; PIDN:CAA34645.1; !1PID:g10272 REFERENCE S41119 !$#authors Matsui, M.; Kobayashi, A.; Kubo, T.; Natori, S. !$#journal Eur. J. Biochem. (1994) 219:449-454 !$#title Purification and characterization of ATBP, a novel protein !1that binds to A/T stretches in three segments of the !1Sarcophaga lectin gene. !$#cross-references MUID:94139722; PMID:8307011 !$#accession S41119 !'##status preliminary; translation not shown !'##molecule_type DNA !'##residues 1-283 ##label MAT !'##cross-references EMBL:D14870; NID:g287440; PIDN:BAA03586.1; !1PID:g391905 REFERENCE A25736 !$#authors Takahashi, H.; Komano, H.; Kawaguchi, N.; Kitamura, N.; !1Nakanishi, S.; Natori, S. !$#journal J. Biol. Chem. (1985) 260:12228-12233 !$#title Cloning and sequencing of cDNA of Sarcophaga peregrina !1humoral lectin induced on injury of the body wall. !$#cross-references MUID:86008294; PMID:2413021 !$#accession A25736 !'##molecule_type mRNA !'##residues 1-283 ##label TAK !'##cross-references GB:M11673; NID:g161264; PIDN:AAA29983.1; !1PID:g161265 !$#accession B25736 !'##molecule_type protein !'##residues 24-32;164-171;209-214 ##label TAK2 !'##note the initiator Met may be either residue 1 or residue 5 COMMENT This lectin is induced in third instar larvae when the body !1wall is injured and in the pupal stage. It is synthesized in !1the fat body and secreted into the hemolymph. GENETICS !$#introns 43/3 CLASSIFICATION #superfamily Sarcophaga lectin; C-type lectin homology KEYWORDS hemolymph; lectin FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-283 #product lectin #status experimental #label LTN\ !$24-157 #domain C-type lectin homology #label LCH SUMMARY #length 283 #molecular-weight 32991 #checksum 8234 SEQUENCE /// ENTRY A34015 #type complete TITLE L-selectin precursor, long splice form - human ALTERNATE_NAMES CD62L; leucocyte cell adhesion molecule-1 (LECAM-1, LAM-1); leukocyte surface antigen Leu-8; lymph node homing receptor core glycoprotein; MEL-14 antigen homolog Leu-8/TQ1; peripheral lymph node homing receptor Leu-8 ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS I55333; S06798; JL0104; A34015; A33912 REFERENCE I55333 !$#authors Ord, D.C.; Ernst, T.J.; Zhou, L.J.; Rambaldi, A.; Spertini, !1O.; Griffin, J.; Tedder, T.F. !$#journal J. Biol. Chem. (1990) 265:7760-7767 !$#title Structure of the gene encoding the human leukocyte adhesion !1molecule-1 (TQ1, Leu-8) of lymphocytes and neutrophils. !$#cross-references MUID:90243637; PMID:1692315 !$#accession I55333 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 14-385 ##label ORD !'##cross-references GB:M32414; NID:g187259; PIDN:AAB60700.1; !1PID:g386860 REFERENCE S06798 !$#authors Camerini, D.; James, S.P.; Stamenkovic, I.; Seed, B. !$#journal Nature (1989) 342:78-82 !$#title Leu-8/TQ1 is the human equivalent of the Mel-14 lymph node !1homing receptor. !$#cross-references MUID:90044046; PMID:2509939 !$#accession S06798 !'##molecule_type mRNA !'##residues 1-225,'S',227-385 ##label CAM !'##cross-references EMBL:X17519; NID:g34344; PIDN:CAB43536.1; !1PID:g4902829 !'##note this translation is not annotated in GenBank entry HSLEU8, !1release 111.0 REFERENCE JL0104 !$#authors Tedder, T.F.; Isaacs, C.M.; Ernst, T.J.; Demetri, G.D.; !1Adler, D.A.; Disteche, C.M. !$#journal J. Exp. Med. (1989) 170:123-133 !$#title Isolation and chromosomal localization of cDNAs encoding a !1novel human lymphocyte cell surface molecule, LAM-1. !1Homology with the mouse lymphocyte homing receptor and other !1human adhesion proteins. !$#cross-references MUID:89310350; PMID:2473156 !$#accession JL0104 !'##molecule_type mRNA !'##residues 1-230,'N',232,'N',234-254,'E',256-385 ##label TED !'##cross-references GB:X16150; NID:g34428; PIDN:CAA34275.1; PID:g34429 !'##note the translated sequence in GenBank entry HSLYAM1, release !1111.0, differs from the published sequence in beginning with !114-Met REFERENCE A34015 !$#authors Bowen, B.R.; Nguyen, T.; Lasky, L.A. !$#journal J. Cell Biol. (1989) 109:421-427 !$#title Characterization of a human homologue of the murine !1peripheral lymph node homing receptor. !$#cross-references MUID:89308881; PMID:2663882 !$#accession A34015 !'##status preliminary !'##molecule_type mRNA !'##residues 14-49,'Y',51-190,'H',192-205,'L',207-226,'F',228-385 !1##label BOW !'##cross-references GB:X16070; NID:g38092; PIDN:CAA34203.1; PID:g38093 REFERENCE A33912 !$#authors Siegelman, M.H.; Weissman, I.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:5562-5566 !$#title Human homologue of mouse lymph node homing receptor: !1evolutionary conservation at tandem cell interaction !1domains. !$#cross-references MUID:89315837; PMID:2664786 !$#accession A33912 !'##status preliminary !'##molecule_type mRNA !'##residues 14-205,'L',207-385 ##label SIE !'##cross-references GB:M25280; NID:g187182; PIDN:AAC63053.1; !1PID:g307134 COMMENT For an alternative splice form, see PIR:S09702. GENETICS !$#gene GDB:SELL; GDB:LNHR; LSEL; LAM1; LYAM1; LAM-1 !'##cross-references GDB:120157; GDB:118834; OMIM:153240 !$#map_position 1q22-1q23 !$#introns 14/3; 42/1; 171/1; 207/1; 269/1; 331/1; 374/1; 380/2 FUNCTION !$#description binds with low affinity to oligosaccarides like heparan !1sulfate and sialylated Lewis x antigen; mediates the !1interaction of leucocytes with endothelial surfaces, assists !1in the recruitment of leucocytes to areas of inflammation, !1and with CD162 mediates neutrophil-neutrophil interaction CLASSIFICATION #superfamily L-selectin; C-type lectin homology; complement !1factor H repeat homology; EGF homology KEYWORDS alternative splicing; cell adhesion; duplication; !1glycoprotein; inflammation; phosphoprotein; surface antigen; !1transmembrane protein FEATURE !$1-51 #domain signal sequence #status predicted #label SIG\ !$42-168 #domain C-type lectin homology #label LCH\ !$52-385 #product L-selectin #status predicted #label MAT\ !$52-343 #domain extracellular #status predicted #label EXT\ !$173-204 #domain EGF homology #label EGF\ !$210-267 #domain complement factor H repeat homology #label !8FH1\ !$272-329 #domain complement factor H repeat homology #label !8FH2\ !$344-368 #domain transmembrane #status predicted #label TMM\ !$369-385 #domain intracellular #status predicted #label INT\ !$73,117,190,245,259 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$377,380 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 385 #molecular-weight 43617 #checksum 4539 SEQUENCE /// ENTRY S09702 #type complete TITLE L-selectin precursor, short splice form - human ALTERNATE_NAMES CD62L; leucocyte cell adhesion molecule-1 (LECAM-1, LAM-1); leukocyte surface antigen Leu-8; lymph node homing receptor core glycoprotein; MEL-14 antigen homolog Leu-8/TQ1; peripheral lymph node homing receptor Leu-8 ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 26-May-2000 ACCESSIONS S09702 REFERENCE S06798 !$#authors Camerini, D.; James, S.P.; Stamenkovic, I.; Seed, B. !$#journal Nature (1989) 342:78-82 !$#title Leu-8/TQ1 is the human equivalent of the Mel-14 lymph node !1homing receptor. !$#cross-references MUID:90044046; PMID:2509939 !$#accession S09702 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-323 ##label CAM !'##cross-references EMBL:X17519; NID:g34344 !'##note this translation is not annotated in GenBank entry HSLEU8, !1release 111.0 COMMENT For an alternative splice form, see PIR:A34015. GENETICS !$#gene GDB:SELL; GDB:LNHR; LSEL; LAM1; LYAM1; LAM-1 !'##cross-references GDB:120157; GDB:118834; OMIM:153240 !$#map_position 1q22-1q23 !$#introns 14/3; 42/1; 171/1; 207/1; 269/1; 303/2 FUNCTION !$#description binds with low affinity to oligosaccarides like heparan !1sulfate and sialylated Lewis x antigen; mediates the !1interaction of leucocytes with endothelial surfaces, assists !1in the recruitment of leucocytes to areas of inflammation, !1and with CD162 mediates neutrophil-neutrophil interaction CLASSIFICATION #superfamily L-selectin; C-type lectin homology; complement !1factor H repeat homology; EGF homology KEYWORDS alternative splicing; cell adhesion; duplication; !1glycoprotein; inflammation; phosphoprotein; surface antigen; !1transmembrane protein FEATURE !$1-51 #domain signal sequence #status predicted #label SIG\ !$42-168 #domain C-type lectin homology #label LCH\ !$52-323 #product L-selectin #status predicted #label MAT\ !$52-300 #domain extracellular #status predicted #label EXT\ !$173-204 #domain EGF homology #label EGF\ !$210-267 #domain complement factor H repeat homology #label !8FH1\ !$272-323 #domain complement factor H repeat homology #status !8atypical #label FH2\ !$301-318 #domain transmembrane #status predicted #label TRM\ !$319-323 #domain intracellular #status predicted #label INT\ !$73,117,190,245,259 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$322 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 323 #molecular-weight 36737 #checksum 4769 SEQUENCE /// ENTRY A32375 #type complete TITLE L-selectin precursor - mouse ALTERNATE_NAMES lymph node homing receptor MEL-14; lymphocyte surface antigen Ly-22 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jan-2000 ACCESSIONS A32375; A35102; A40167; A60906 REFERENCE A32375 !$#authors Lasky, L.A.; Singer, M.S.; Yednock, T.A.; Dowbenko, D.; !1Fennie, C.; Rodriguez, H.; Nguyen, T.; Stachel, S.; Rosen, !1S.D. !$#journal Cell (1989) 56:1045-1055 !$#title Cloning of a lymphocyte homing receptor reveals a lectin !1domain. !$#cross-references MUID:89168433; PMID:2647302 !$#accession A32375 !'##molecule_type mRNA !'##residues 1-372 ##label LAS !'##cross-references GB:M25324; NID:g198803; PIDN:AAA39431.1; !1PID:g198804 REFERENCE A35102 !$#authors Siegelman, M.H.; Cheng, I.C.; Weissman, I.L.; Wakeland, E.K. !$#journal Cell (1990) 61:611-622 !$#title The mouse lymph node homing receptor is identical with the !1lymphocyte cell surface marker Ly-22: role of the EGF domain !1in endothelial binding. !$#cross-references MUID:90263086; PMID:1693096 !$#accession A35102 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-372 ##label SIE1 !'##cross-references GB:M36005; NID:g199735; PIDN:AAA39722.1; !1PID:g199736; GB:M36058; NID:g199737; PIDN:AAA39723.1; !1PID:g199738 REFERENCE A40167 !$#authors Siegelman, M.H.; van de Rijn, M.; Weissman, I.L. !$#journal Science (1989) 243:1165-1172 !$#title Mouse lymph node homing receptor cDNA clone encodes a !1glycoprotein revealing tandem interaction domains. !$#cross-references MUID:89162048; PMID:2646713 !$#accession A40167 !'##molecule_type mRNA !'##residues 1-372 ##label SIE2 !'##cross-references GB:X14772; NID:g52942; PIDN:CAA32880.1; PID:g52943 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE A60906 !$#authors Siegelman, M.; Bond, M.W.; Gallatin, W.M.; St.John, T.; !1Smith, H.T.; Fried, V.A.; Weissman, I.L. !$#journal Science (1986) 231:823-829 !$#title Cell surface molecule associated with lymphocyte homing is a !1ubiquitinated branched-chain glycoprotein. !$#cross-references MUID:86122900; PMID:3003913 !$#accession A60906 !'##molecule_type protein !'##residues 'X',40,'X',42,'XXX',46,'X',48,'XXXXXX',55-56,'X',58, !1'XXXXXX',65,'V',67,'XL',70 ##label SI3 COMMENT This protein is ubiquitinated. FUNCTION !$#description binds with low affinity to oligosaccarides like heparan !1sulfate and sialylated Lewis x antigen; mediates the !1interaction of leucocytes with endothelial surfaces, assists !1in the recruitment of leucocytes to areas of inflammation, !1and with CD162 mediates neutrophil-neutrophil interaction CLASSIFICATION #superfamily L-selectin; C-type lectin homology; complement !1factor H repeat homology; EGF homology KEYWORDS cell adhesion; duplication; glycoprotein; inflammation; !1phosphoprotein; surface antigen; transmembrane protein FEATURE !$1-38 #domain signal sequence #status predicted #label SIG\ !$29-155 #domain C-type lectin homology #label LCH\ !$39-372 #product L-selectin #status experimental #label MAT\ !$39-331 #domain extracellular #status predicted #label EXT\ !$160-191 #domain EGF homology #label EGF\ !$197-254 #domain complement factor H repeat homology #label !8FH1\ !$259-316 #domain complement factor H repeat homology #label !8FH2\ !$332-355 #domain transmembrane #status predicted #label TMM\ !$356-372 #domain intracellular #status predicted #label INT\ !$60,104,216,246,278, !$308,320 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$364 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 372 #molecular-weight 42288 #checksum 8606 SEQUENCE /// ENTRY TTHUN #type complete TITLE tetranectin precursor [validated] - human ALTERNATE_NAMES plasminogen-kringle 4 binding protein ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1992 #sequence_revision 03-Aug-1995 #text_change 08-Dec-2000 ACCESSIONS S24126; A56835; A29747; I38359; S19865 REFERENCE S24126 !$#authors Berglund, L.; Petersen, T.E. !$#journal FEBS Lett. (1992) 309:15-19 !$#title The gene structure of tetranectin, a plasminogen binding !1protein. !$#cross-references MUID:92380263; PMID:1511740 !$#accession S24126 !'##molecule_type DNA !'##residues 1-202 ##label BER !'##cross-references EMBL:X70911 REFERENCE A56835 !$#authors Wewer, U.M.; Albrechtsen, R. !$#journal Lab. Invest. (1992) 67:253-262 !$#title Tetranectin, a plasminogen kringle 4-binding protein. !1Cloning and gene expression pattern in human colon cancer. !$#cross-references MUID:92365345; PMID:1354271 !$#accession A56835 !'##molecule_type mRNA !'##residues 1-202 ##label WEW !'##cross-references EMBL:X64559; NID:g37408; PIDN:CAA45860.1; !1PID:g37409 !'##experimental_source placenta REFERENCE A29747 !$#authors Fuhlendorff, J.; Clemmensen, I.; Magnusson, S. !$#journal Biochemistry (1987) 26:6757-6764 !$#title Primary structure of tetranectin, a plasminogen kringle 4 !1binding plasma protein: homology with asialoglycoprotein !1receptors and cartilage proteoglycan core protein. !$#cross-references MUID:88107595; PMID:3427041 !$#accession A29747 !'##molecule_type protein !'##residues 22-105,'G',107-202 ##label FUH !'##experimental_source plasma !'##note 55-Ser and 58-Met were also found GENETICS !$#gene GDB:TNA !'##cross-references GDB:135032; OMIM:187520 !$#map_position 3p22-3p21.3 !$#introns 37/1; 70/1 COMPLEX homotetramer CLASSIFICATION #superfamily tetranectin; C-type lectin homology KEYWORDS glycoprotein; plasma; tetramer FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-202 #product tetranectin #status experimental #label MAT\ !$71-197 #domain C-type lectin homology #label LCH\ !$25 #binding_site carbohydrate (Thr) (covalent) #status !8experimental\ !$71-81,98-197, !$173-189 #disulfide_bonds #status experimental SUMMARY #length 202 #molecular-weight 22567 #checksum 4535 SEQUENCE /// ENTRY A48689 #type complete TITLE pancreatitis-associated protein PAP-2 - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A48689 REFERENCE A48689 !$#authors Frigerio, J.M.; Dusetti, N.J.; Keim, V.; Dagorn, J.C.; !1Iovanna, J.L. !$#journal Biochemistry (1993) 32:9236-9241 !$#title Identification of a second rat pancreatitis-associated !1protein. Messenger RNA cloning, gene structure, and !1expression during acute pancreatitis. !$#cross-references MUID:93378971; PMID:8369291 !$#accession A48689 !'##status preliminary !'##molecule_type mRNA !'##residues 1-174 ##label FRI !'##cross-references GB:L10229; NID:g409014; PIDN:AAA02980.1; !1PID:g409015 CLASSIFICATION #superfamily tetranectin; C-type lectin homology FEATURE !$39-170 #domain C-type lectin homology #label LCH\ !$39-50,67-170, !$145-162 #disulfide_bonds #status predicted SUMMARY #length 174 #molecular-weight 19599 #checksum 5440 SEQUENCE /// ENTRY RGHU1A #type complete TITLE regenerating islet lectin 1-alpha precursor [validated] - human ALTERNATE_NAMES lithostathine; pancreatic thread protein (PTP); reg I protein; reg1-alpha protein CONTAINS pancreatic stone protein (PSP) ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1990 #sequence_revision 03-Aug-1995 #text_change 08-Dec-2000 ACCESSIONS A35197; B28351; S12950; S02767; S02419; S00113; S01471; !1A25246 REFERENCE A35197 !$#authors Watanabe, T.; Yonekura, H.; Terazono, K.; Yamamoto, H.; !1Okamoto, H. !$#journal J. Biol. Chem. (1990) 265:7432-7439 !$#title Complete nucleotide sequence of human reg gene and its !1expression in normal and tumoral tissues. The reg protein, !1pancreatic stone protein, and pancreatic thread protein are !1one and the same product of the gene. !$#cross-references MUID:90237042; PMID:2332435 !$#accession A35197 !'##molecule_type DNA !'##residues 1-166 ##label WAT !'##cross-references GB:J05412 REFERENCE A92704 !$#authors Terazono, K.; Yamamoto, H.; Takasawa, S.; Shiga, K.; !1Yonemura, Y.; Tochino, Y.; Okamoto, H. !$#journal J. Biol. Chem. (1988) 263:2111-2114 !$#title A novel gene activated in regenerating islets. !$#cross-references MUID:88115343; PMID:2963000 !$#accession B28351 !'##molecule_type mRNA !'##residues 1-166 ##label TER !'##cross-references GB:M18963; NID:g190978; PIDN:AAA36558.1; !1PID:g190979 REFERENCE S12950 !$#authors Itoh, T.; Tsuzuki, H.; Katoh, T.; Teraoka, H.; Matsumoto, !1K.; Yoshida, N.; Terazono, K.; Watanabe, T.; Yonekura, H.; !1Yamamoto, H.; Okamoto, H. !$#journal FEBS Lett. (1990) 272:85-88 !$#title Isolation and characterization of human reg protein produced !1in Saccharomyces cerevisiae. !$#cross-references MUID:91032149; PMID:2226837 !$#accession S12950 !'##molecule_type protein !'##residues 23-52;160-166 ##label ITO !'##note sequence determined from protein isolated after human cDNA !1sequence was cloned and expressed in Saccharomyces !1cerevisiae REFERENCE S02767 !$#authors de Caro, A.M.; Adrich, Z.; Fournet, B.; Capon, C.; Bonicel, !1J.J.; de Caro, J.D.; Rovery, M. !$#journal Biochim. Biophys. Acta (1989) 994:281-284 !$#title N-terminal sequence extension in the glycosylated forms of !1human pancreatic stone protein. The 5-oxoproline N-terminal !1chain is O-glycosylated on the 5th amino acid residue. !$#cross-references MUID:89150292; PMID:2493268 !$#accession S02767 !'##molecule_type protein !'##residues 23-47 ##label DEC REFERENCE S02419 !$#authors Rouimi, P.; de Caro, J.; Bonicel, J.; Rovery, M.; de Caro, !1A. !$#journal FEBS Lett. (1988) 229:171-174 !$#title The disulfide bridges of the immunoreactive forms of human !1pancreatic stone protein isolated from pancreatic juice. !$#cross-references MUID:88152214; PMID:3345835 !$#accession S02419 !'##molecule_type protein !'##residues 63-72;125-139;150-157;160-166 ##label ROU !'##note disulfide bonds REFERENCE S00113 !$#authors de Caro, A.M.; Bonicel, J.J.; Rouimi, P.; de Caro, J.D.; !1Sarles, H.; Rovery, M. !$#journal Eur. J. Biochem. (1987) 168:201-207 !$#title Complete amino acid sequence of an immunoreactive form of !1human pancreatic stone protein isolated from pancreatic !1juice. !$#cross-references MUID:88029417; PMID:3665916 !$#accession S00113 !'##molecule_type protein !'##residues 34-166 ##label DE1 REFERENCE S01471 !$#authors Rouimi, P.; Bonicel, J.; Rovery, M.; de Caro, A. !$#journal FEBS Lett. (1987) 216:195-199 !$#title Cleavage of the Arg-Ile bond in the native polypeptide chain !1of human pancreatic stone protein. !$#cross-references MUID:87219142; PMID:3108036 !$#accession S01471 !'##molecule_type protein !'##residues 33-48 ##label RO2 REFERENCE A25246 !$#authors Montalto, G.; Bonicel, J.; Multigner, L.; Rovery, M.; !1Sarles, H.; De Caro, A. !$#journal Biochem. J. (1986) 238:227-232 !$#title Partial amino acid sequence of human pancreatic stone !1protein, a novel pancreatic secretory protein. !$#cross-references MUID:87099950; PMID:3541906 !$#accession A25246 !'##molecule_type protein !'##residues 34-73,'X',75-87,'R',89-98 ##label MON COMMENT This protein is found in pancreatic calculi of mammals. The !1tryptic-like cleavage of an Arg-Ile bond transforms the !1soluble protein into a protein insoluble in the pH range !15.5-7.5. COMMENT Intact regenerating islet lectin 1-alpha, lithostathine, !1inhibits the growth of calcium carbonate crystals in !1pancreatic juice. GENETICS !$#gene GDB:REG1A; REG !'##cross-references GDB:132455; OMIM:167770 !$#map_position 2p12-2p12 !$#introns 22/1; 61/3; 107/3; 145/1 CLASSIFICATION #superfamily tetranectin; C-type lectin homology KEYWORDS glycoprotein; lectin; pancreas; pyroglutamic acid FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-166 #product regenerating islet lectin 1-alpha #status !8experimental #label MAT\ !$34-166 #product pancreatic stone protein #status !8experimental #label MAT2\ !$36-162 #domain C-type lectin homology #label LCH\ !$23 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$27 #binding_site carbohydrate (Thr) (covalent) #status !8experimental\ !$33-34 #cleavage_site Arg-Ile (trypsin) #status !8experimental\ !$36-47,64-162, !$137-154 #disulfide_bonds #status experimental SUMMARY #length 166 #molecular-weight 18731 #checksum 526 SEQUENCE /// ENTRY A37289 #type complete TITLE tetranectin homolog - reef shark ORGANISM #formal_name Carcharhinus springeri #common_name reef shark DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A37289; A37287 REFERENCE A37289 !$#authors Neame, P.J.; Young, C.N.; Treep, J.T. !$#journal Protein Sci. (1992) 1:161-168 !$#title Primary structure of a protein isolated from reef shark !1Carcharhinus springeri cartilage that is similar to the !1mammalian C-type lectin homolog tetranectin. !$#cross-references MUID:93284081; PMID:1304877 !$#accession A37289 !'##molecule_type protein !'##residues 1-166 ##label NE2 CLASSIFICATION #superfamily tetranectin; C-type lectin homology KEYWORDS cartilage FEATURE !$37-160 #domain C-type lectin homology #label LCH\ !$37-47,64-160, !$136-152 #disulfide_bonds #status predicted SUMMARY #length 166 #molecular-weight 18432 #checksum 149 SEQUENCE /// ENTRY JH0626 #type complete TITLE antifreeze protein II precursor - rainbow smelt ORGANISM #formal_name Osmerus mordax #common_name rainbow smelt DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JH0626; PS0361 REFERENCE JH0626 !$#authors Ewart, K.V.; Rubinsky, B.; Fletcher, G.L. !$#journal Biochem. Biophys. Res. Commun. (1992) 185:335-340 !$#title Structural and functional similarity between fish antifreeze !1proteins and calcium-dependent lectins. !$#cross-references MUID:92287116; PMID:1599470 !$#accession JH0626 !'##molecule_type mRNA !'##residues 1-175 ##label EWA !'##experimental_source liver !$#accession PS0361 !'##molecule_type protein !'##residues 145-154;162-173 ##label EWA1 COMMENT This protein lowers solution freezing points !1non-colligatively (antifreeze activity) and protects !1mammalian cells from damage at hypothermic temperatures. CLASSIFICATION #superfamily tetranectin; C-type lectin homology KEYWORDS glycoprotein FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-175 #product antifreeze protein II #status predicted !8#label ANT\ !$38-159 #domain C-type lectin homology #label LCH\ !$34 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$38-49,66-159, !$135-151 #disulfide_bonds #status predicted SUMMARY #length 175 #molecular-weight 19055 #checksum 8439 SEQUENCE /// ENTRY A34313 #type complete TITLE antifreeze protein II precursor - sea raven ALTERNATE_NAMES pro-antifreeze protein type II ORGANISM #formal_name Hemitripterus americanus #common_name sea raven DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A34313; A24602; PC2386; PC2387; S65733 REFERENCE A34313 !$#authors Hayes, P.H.; Scott, G.K.; Ng, N.F.L.; Hew, C.L.; Davies, !1P.L. !$#journal J. Biol. Chem. (1989) 264:18761-18767 !$#title Cystine-rich type II antifreeze protein precursor is !1initiated from the third AUG codon of its mRNA. !$#cross-references MUID:90036986; PMID:2572595 !$#accession A34313 !'##molecule_type DNA; mRNA !'##residues 1-37,'G',39-163 ##label HAY !'##cross-references GB:J05100; NID:g213875; PIDN:AAA49618.1; !1PID:g213876 !'##note there are 12-15 copies in the genome; the sequence of SR7 was !1determined !'##note the initiator codon was determined !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing !'##note the amino end of the mature protein is blocked REFERENCE A24602 !$#authors Ng, N.F.; Trinh, K.Y.; Hew, C.L. !$#journal J. Biol. Chem. (1986) 261:15690-15695 !$#title Structure of an antifreeze polypeptide precursor from the !1sea raven, Hemitripterus americanus. !$#cross-references MUID:87057207; PMID:3782083 !$#accession A24602 !'##molecule_type mRNA !'##residues 'MQRQQADTETREDISTAGLSIIFIVCTISTTR',1-163 ##label NGN !'##cross-references GB:J02593; NID:g213873; PIDN:AAA49617.1; !1PID:g213874 !'##note parts of this sequence were determined by protein sequencing REFERENCE PC2386 !$#authors Duncker, B.P.; Gauthier, S.Y.; Davies, P.L. !$#journal Biochem. Biophys. Res. Commun. (1994) 203:1851-1857 !$#title Cystine-rich fish antifreeze is produced as an active !1proprotein precursor in fall armyworm cells. !$#cross-references MUID:95032070; PMID:7945337 !$#accession PC2386 !'##molecule_type mRNA !'##residues 1-45 ##label DUN !$#accession PC2387 !'##molecule_type protein !'##residues 18-27 ##label DU2 REFERENCE S65733 !$#authors Duncker, B.P.; Gauthier, S.Y.; Davies, P.L. !$#journal Biochim. Biophys. Acta (1996) 1292:312-316 !$#title Evidence for a proprotein intermediate during maturation of !1type II antifreeze protein in sea raven, Hemitripterus !1americanus. !$#cross-references MUID:96176860; PMID:8597578 !$#accession S65733 !'##molecule_type protein !'##residues 18-22 ##label DUW GENETICS !$#introns 21/1; 66/3; 105/3; 142/1 CLASSIFICATION #superfamily tetranectin; C-type lectin homology KEYWORDS pyroglutamic acid FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-34 #domain propeptide #status experimental #label PRO\ !$35-163 #product antifreeze protein II #status predicted !8#label MAT\ !$41-159 #domain C-type lectin homology #label LCH\ !$35 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$41-52,69-159, !$135-151 #disulfide_bonds #status predicted SUMMARY #length 163 #molecular-weight 17509 #checksum 1944 SEQUENCE /// ENTRY RGHU1B #type complete TITLE regenerating islet lectin 1-beta precursor - human ALTERNATE_NAMES reg-related protein; reg1-beta protein CONTAINS pancreatic stone protein (PSP) ORGANISM #formal_name Homo sapiens #common_name man DATE 22-Nov-1993 #sequence_revision 03-Aug-1995 #text_change 16-Jun-2000 ACCESSIONS S34591; S42729; A44712 REFERENCE S34591 !$#authors Bartoli, C.; Gharib, B.; Giorgi, D.; Sansonetti, A.; Dagorn, !1J.C.; Berge-Lefranc, J.L. !$#journal FEBS Lett. (1993) 327:289-293 !$#title A gene homologous to the reg gene is expressed in the human !1pancreas. !$#cross-references MUID:93351647; PMID:8348956 !$#accession S34591 !'##molecule_type DNA !'##residues 1-166 ##label BAR !'##cross-references GB:L08010; NID:g307368; PIDN:AAA18204.1; !1PID:g487726 !'##note this gene appears to be expressed in pancreas and liver REFERENCE S42729 !$#authors Moriizumi, S.; Watanabe, T.; Unno, M.; Nakagawara, K.; !1Suzuki, Y.; Miyashita, H.; Yonekura, H.; Okamoto, H. !$#journal Biochim. Biophys. Acta (1994) 1217:199-202 !$#title Isolation, structural determination and expression of a !1novel reg gene, human regI-beta. !$#cross-references MUID:94153997; PMID:8110835 !$#accession S42729 !'##molecule_type mRNA !'##residues 1-166 ##label MOR !'##cross-references GB:D16816; NID:g474305; PIDN:BAA04091.1; !1PID:g474306 !$#accession A44712 !'##molecule_type DNA !'##residues 1-166 ##label MO2 !'##cross-references GB:D17291; NID:g474307; PIDN:BAA04124.1; !1PID:g474308 COMMENT This protein is found in pancreatic calculi of mammals. The !1tryptic-like cleavage of an Arg-Ile bond transforms the !1soluble protein into a protein insoluble in the pH range !15.5-7.5. GENETICS !$#gene GDB:REG1B; REG1 !'##cross-references GDB:342079 !$#map_position 2p12-2p12 !$#introns 22/1; 61/3; 107/3; 145/1 CLASSIFICATION #superfamily tetranectin; C-type lectin homology KEYWORDS glycoprotein; lectin; pancreas; pyroglutamic acid FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-166 #product regenerating islet lectin 1beta #status !8predicted #label MAT\ !$34-166 #product pancreatic stone protein #status predicted !8#label MAT2\ !$36-162 #domain C-type lectin homology #label LCH\ !$23 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status predicted\ !$27 #binding_site carbohydrate (Thr) (covalent) #status !8predicted\ !$33-34 #cleavage_site Arg-Ile (trypsin) #status predicted\ !$36-47,64-162, !$137-154 #disulfide_bonds #status predicted SUMMARY #length 166 #molecular-weight 18665 #checksum 379 SEQUENCE /// ENTRY LNRC1 #type complete TITLE lectin BRA3-1 precursor - barnacle (Megabalanus rosa) ORGANISM #formal_name Megabalanus rosa DATE 24-Feb-1994 #sequence_revision 09-Sep-1994 #text_change 16-Jul-1999 ACCESSIONS JC1503; A26094 REFERENCE JC1503 !$#authors Takamatsu, N.; Takeda, T.; Kojima, M.; Heishi, M.; Muramoto, !1K.; Kamiya, H.; Shiba, T. !$#journal Gene (1993) 128:251-255 !$#title Acorn barnacle Megabalanus rosa lectin (BRA-3): cDNA !1cloning, gene structure and seasonal changes of mRNA and !1protein levels. !$#cross-references MUID:93292994; PMID:8514190 !$#accession JC1503 !'##molecule_type DNA; mRNA !'##residues 1-162 ##label TAK !'##cross-references DDBJ:D13299 REFERENCE A26094 !$#authors Muramoto, K.; Kamiya, H. !$#journal Biochim. Biophys. Acta (1986) 874:285-295 !$#title The amino-acid sequence of a lectin of the acorn barnacle !1Megabalanus rosa. !$#accession A26094 !'##molecule_type protein !'##residues 25-145,'K',147-162 ##label MUR !'##note 146-Arg was also found COMMENT This galactose-binding lectin is isolated from the coelomic !1fluid. COMMENT This protein plays important roles in defense mechanisms and !1in development and differentiation. COMMENT The molecule is a tetramer of identical chains. GENETICS !$#introns 22/1; 47/2; 86/3 CLASSIFICATION #superfamily tetranectin; C-type lectin homology KEYWORDS hemolymph; homotetramer; lectin FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-162 #product lectin BRA3-1 #status experimental #label !8MAT\ !$26-150 #domain C-type lectin homology #label LCH\ !$26-39,56-150, !$125-142 #disulfide_bonds #status experimental\ !$157 #disulfide_bonds interchain (to 160) #status !8experimental\ !$160 #disulfide_bonds interchain (to 157) #status !8experimental SUMMARY #length 162 #molecular-weight 18342 #checksum 3137 SEQUENCE /// ENTRY LNRC3 #type complete TITLE lectin BRA3-2 precursor - barnacle (Megabalanus rosa) ORGANISM #formal_name Megabalanus rosa DATE 31-Dec-1988 #sequence_revision 09-Sep-1994 #text_change 16-Jul-1999 ACCESSIONS JC1504; A26094 REFERENCE JC1503 !$#authors Takamatsu, N.; Takeda, T.; Kojima, M.; Heishi, M.; Muramoto, !1K.; Kamiya, H.; Shiba, T. !$#journal Gene (1993) 128:251-255 !$#title Acorn barnacle Megabalanus rosa lectin (BRA-3): cDNA !1cloning, gene structure and seasonal changes of mRNA and !1protein levels. !$#cross-references MUID:93292994; PMID:8514190 !$#accession JC1504 !'##molecule_type mRNA !'##residues 1-162 ##label TAK REFERENCE A26094 !$#authors Muramoto, K.; Kamiya, H. !$#journal Biochim. Biophys. Acta (1986) 874:285-295 !$#title The amino-acid sequence of a lectin of the acorn barnacle !1Megabalanus rosa. !$#accession A26094 !'##molecule_type protein !'##residues 25-162 ##label MUR !'##note 146-Arg was also found COMMENT This three galactose-binding lectin is isolated from the !1coelomic fluid. COMMENT This protein plays important roles in defense mechanisms and !1in development and differentiation. COMMENT The molecule is a tetramer of identical chains. CLASSIFICATION #superfamily tetranectin; C-type lectin homology KEYWORDS hemolymph; homotetramer; lectin FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-162 #product lectin BRA3-2 #status experimental #label !8MAT\ !$26-150 #domain C-type lectin homology #label LCH\ !$26-39,56-150, !$125-142 #disulfide_bonds #status experimental\ !$157 #disulfide_bonds interchain (to 160) #status !8experimental\ !$160 #disulfide_bonds interchain (to 157) #status !8experimental SUMMARY #length 162 #molecular-weight 18358 #checksum 3123 SEQUENCE /// ENTRY JL0085 #type complete TITLE eosinophil major basic protein precursor [validated] - human ALTERNATE_NAMES eosinophil granule major basic protein (gMBP); immunoregulatory factor BMPG; natural killer cell-activating factor (NKAF); pregnancy-associated major basic protein (pMBP) CONTAINS bone-marrow proteoglycan (BMPG) ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1991 #sequence_revision 13-Feb-1998 #text_change 08-Dec-2000 ACCESSIONS I54055; JL0085; JL0087; I37208; S53375; A31112; A60866; !1PL0174; S33779; S43668; S37143 REFERENCE I54055 !$#authors Barker, R.L.; Loegering, D.A.; Arakawa, K.C.; Pease, L.R.; !1Gleich, G.J. !$#journal Gene (1990) 86:285-289 !$#title Cloning and sequence analysis of the human gene encoding !1eosinophil major basic protein. !$#cross-references MUID:90215311; PMID:2323577 !$#accession I54055 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-222 ##label BAR1 !'##cross-references GB:M34462; NID:g182079; PIDN:AAA35796.1; !1PID:g182080 REFERENCE JL0085 !$#authors Barker, R.L.; Gleich, G.J.; Pease, L.R. !$#journal J. Exp. Med. (1988) 168:1493-1498 !$#title Acidic precursor revealed in human eosinophil granule major !1basic protein cDNA. !$#cross-references MUID:89010545; PMID:3171483 !$#accession JL0085 !'##molecule_type mRNA !'##residues 1-222 ##label BAR2 !'##cross-references GB:M36805; NID:g187414; PIDN:AAA36203.1; !1PID:g187415 !'##note the codon given for 84-Asp (CAC) is inconsistent with the !1authors' translation REFERENCE JL0087 !$#authors McGrogan, M.; Simonsen, C.; Scott, R.; Griffith, J.; Ellis, !1N.; Kennedy, J.; Campanelli, D.; Nathan, C.; Gabay, J. !$#journal J. Exp. Med. (1988) 168:2295-2308 !$#title Isolation of a complementary DNA clone encoding a precursor !1to human eosinophil major basic protein. !$#cross-references MUID:89067833; PMID:3199069 !$#accession JL0087 !'##molecule_type mRNA !'##residues 1-222 ##label MCG !'##cross-references GB:M35670; NID:g183942; PIDN:AAA35965.1; !1PID:g306839; GB:X14088; NID:g31136; PID:g31137 REFERENCE I37208 !$#authors Yoshimatsu, K.; Ohya, Y.; Shikata, Y.; Seto, T.; Hasegawa, !1Y.; Tanaka, I.; Kawamura, T.; Kitoh, K.; Toyoshima, S.; !1Osawa, T. !$#journal Mol. Immunol. (1992) 29:537-546 !$#title Purification and cDNA cloning of a novel factor produced by !1a human T-cell hybridoma: sequence homology with animal !1lectins. !$#cross-references MUID:92227954; PMID:1565101 !$#accession I37208 !'##molecule_type mRNA !'##residues 1-222 ##label YOS !'##cross-references EMBL:X65787; NID:g312044; PIDN:CAA46670.1; !1PID:g312045 !'##note parts of this sequence, including the amino end of the mature !1protein, were confirmed by peptide sequencing REFERENCE S53375 !$#authors Li, M.S.; Sun, L.; Satoh, T.; Fisher, L.M.; Spry, C.J.F. !$#journal Biochem. J. (1995) 305:921-927 !$#title Human eosinophil major basic protein, a mediator of allergic !1inflammation, is expressed by alternative splicing from two !1promoters. !$#cross-references MUID:95151030; PMID:7531438 !$#accession S53375 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-191,'T',193-222 ##label LI2 !'##cross-references EMBL:Z26248; NID:g940510; PIDN:CAA81207.1; !1PID:g400414 REFERENCE A31112 !$#authors Wasmoen, T.L.; Bell, M.P.; Loegering, D.A.; Gleich, G.J.; !1Prendergast, F.G.; McKean, D.J. !$#journal J. Biol. Chem. (1988) 263:12559-12563 !$#title Biochemical and amino acid sequence analysis of human !1eosinophil granule major basic protein. !$#cross-references MUID:88315054; PMID:3410852 !$#accession A31112 !'##molecule_type protein !'##residues 106-222 ##label WAS1 REFERENCE A60866 !$#authors Weller, P.F.; Ackerman, S.J.; Smith, J.A. !$#journal J. Leukoc. Biol. (1988) 43:1-4 !$#title Eosinophil granule cationic proteins: major basic protein is !1distinct from the smaller subunit of eosinophil peroxidase. !$#cross-references MUID:88089268; PMID:3422083 !$#accession A60866 !'##molecule_type protein !'##residues 'XX',108-121,'X',123-124,'X' ##label WEL REFERENCE PL0174 !$#authors Wasmoen, T.L.; McKean, D.J.; Benirschke, K.; Coulam, C.B.; !1Gleich, G.J. !$#journal J. Exp. Med. (1989) 170:2051-2063 !$#title Evidence of eosinophil granule major basic protein in human !1placenta. !$#cross-references MUID:90063469; PMID:2584934 !$#accession PL0174 !'##molecule_type protein !'##residues 177-196 ##label WAS2 REFERENCE S33779 !$#authors Shikata, Y.; Hayashi, Y.; Yoshimatsu, K.; Ohya, Y.; Seto, !1T.; Fukushima, K.; Yoshida, Y. !$#journal Biochim. Biophys. Acta (1993) 1163:243-249 !$#title Pro-major basic protein has three types of sugar chains at !1the pro-portion. !$#cross-references MUID:93283419; PMID:8507662 !$#accession S33779 !'##molecule_type protein !'##residues 17-222 ##label SHI REFERENCE S43668 !$#authors Oxvig, C.; Gleich, G.J.; Sottrup-Jensen, L. !$#journal FEBS Lett. (1994) 341:213-217 !$#title Localization of disulfide bridges and free sulfhydryl groups !1in human eosinophil granule major basic protein. !$#cross-references MUID:94185797; PMID:8137941 !$#accession S43668 !'##molecule_type protein !'##residues 106-222 ##label OXV !'##note in the gMBP form cysteines 107, 128, 147, 169, and 201 probably !1have free thiols; in the pMBP form this protein may form a !1dimer involving Cys-107 and at least one other disulfide !1bond with pregnancy-associated plasma protein A COMMENT This protein is produced as a nontoxic precursor that !1constitutes the crystalloid core of the eosinophil granule. !1The glycosylated propeptide region of the precursor protects !1the eosinophil from damage by neutralizing or masking the !1toxic effects of the arginine-rich, basic region that !1becomes the mature protein. COMMENT The mature major basic protein is a potent toxin against !1Gram-negative and Gram-positive bacteria, fungi, helminths, !1and various cell types. The blood level of this protein !1increases early in gestation and plateaus by week 196 at !1concentrations more than 186 times normal. COMMENT The mature major basic protein induces histamine release !1from mast cells and basophils. GENETICS !$#gene GDB:PRG2 !'##cross-references GDB:132400 !$#map_position 10q22.1-10q22.1 !$#introns 20/1; 122/3; 166/3; 204/1 CLASSIFICATION #superfamily eosinophil major basic protein precursor; !1C-type lectin homology KEYWORDS antibiotic; chondroitin sulfate proteoglycan; cytotoxin; !1eosinophil; glycoprotein; inflammation; monomer FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-222 #product bone-marrow proteoglycan #status !8experimental #label BMPG\ !$17-105 #domain propeptide #status experimental #label PRO\ !$106-222 #product eosinophil major basic protein #status !8experimental #label MBP\ !$107-220 #domain C-type lectin homology #label LCH\ !$24 #binding_site carbohydrate (Ser) (covalent) #status !8experimental\ !$25 #binding_site carbohydrate (Thr) (covalent) #status !8experimental\ !$62 #binding_site chondroitin sulfate (Ser) (covalent) !8#status experimental\ !$86 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$125-220,197-212 #disulfide_bonds #status experimental\ !$166 #binding_site chondroitin sulfate (Ser) (covalent) !8#status absent SUMMARY #length 222 #molecular-weight 25231 #checksum 937 SEQUENCE /// ENTRY S68150 #type complete TITLE eosinophil major basic protein precursor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 14-Feb-1997 #sequence_revision 13-Mar-1997 #text_change 16-Jun-2000 ACCESSIONS S68150; S62731 REFERENCE S68150 !$#authors Nittoh, T.; Watanabe, M.; Okoyama, H.; Misawa, S.; Isobe, !1Y.; Hayashi, H.; Mue, S.; Ohuchi, K. !$#journal Biochim. Biophys. Acta (1996) 1306:115-116 !$#title Corrigendum to "Cloning of cDNA for rat eosinophil major !1basic protein". !$#cross-references MUID:96201712; PMID:8611616 !$#accession S68150 !'##molecule_type mRNA !'##residues 1-227 ##label NIT1 !'##cross-references EMBL:D50568; NID:g1127031; PIDN:BAA09129.1; !1PID:g1127032 REFERENCE S62731 !$#authors Nittoh, T.; Watanabe, M.; Okayama, H.; Misawa, S.; Isobe, !1Y.; Hayashi, H.; Mue, S.; Ohuchi, K. !$#journal Biochim. Biophys. Acta (1995) 1264:261-264 !$#title Cloning of cDNA for rat eosinophil major basic protein. !$#cross-references MUID:96138543; PMID:8547309 !$#accession S62731 !'##molecule_type mRNA !'##residues 1-7,'S',9-26,'T',28-34,'F',36-227 ##label NIT2 !'##cross-references EMBL:D50568; NID:g1127031 CLASSIFICATION #superfamily eosinophil major basic protein precursor; !1C-type lectin homology KEYWORDS antibiotic; chondroitin sulfate proteoglycan; cytotoxin; !1eosinophil; glycoprotein; inflammation; monomer FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-110 #domain propeptide #status predicted #label PRO\ !$111-227 #product eosinophil major basic protein #status !8predicted #label MBP\ !$112-225 #domain C-type lectin homology #label LCH\ !$24 #binding_site carbohydrate (Ser) (covalent) #status !8predicted\ !$70 #binding_site chondroitin sulfate (Ser) (covalent) !8#status predicted\ !$130-225,202-217 #disulfide_bonds #status predicted SUMMARY #length 227 #molecular-weight 25129 #checksum 1597 SEQUENCE /// ENTRY S13625 #type complete TITLE eosinophil major basic protein 1 precursor - guinea pig ORGANISM #formal_name Cavia porcellus #common_name guinea pig DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 21-Jul-2000 ACCESSIONS S13625; S18497; S40491 REFERENCE S13625 !$#authors Aoki, I.; Shindoh, Y.; Nishida, T.; Nakai, S.; Hong, Y.M.; !1Mio, M.; Saito, T.; Tasaka, K. !$#journal FEBS Lett. (1991) 279:330-334 !$#title Sequencing and cloning of the cDNA of guinea pig eosinophil !1major basic protein. !$#cross-references MUID:91160746; PMID:1705901 !$#accession S13625 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-233 ##label AOK !'##cross-references GB:D90251; NID:g3135096; PIDN:BAA14291.1; !1PID:g220291 !$#accession S18497 !'##molecule_type protein !'##residues 115-146,'X',148-157,'X',159-162 ##label AOK1 REFERENCE S40491 !$#authors Hashimoto, Y.; Nagaoka, I.; Yamashita, T. !$#journal Biochim. Biophys. Acta (1993) 1203:236-242 !$#title Purification of the antibacterial fragments of guinea-pig !1major basic protein. !$#cross-references MUID:94092714; PMID:8268206 !$#accession S40491 !'##molecule_type protein !'##residues 115-233 ##label HAS CLASSIFICATION #superfamily eosinophil major basic protein precursor; !1C-type lectin homology KEYWORDS antibiotic; chondroitin sulfate proteoglycan; cytotoxin; !1eosinophil; glycoprotein; inflammation; monomer FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-114 #domain propeptide #status predicted #label PRO\ !$115-233 #product eosinophil major basic protein 1 #status !8experimental #label MAT\ !$116-231 #domain C-type lectin homology #label LCH\ !$24,25 #binding_site carbohydrate (Ser) (covalent) #status !8predicted\ !$67 #binding_site chondroitin sulfate (Ser) (covalent) !8#status predicted\ !$134-231,208-223 #disulfide_bonds #status predicted SUMMARY #length 233 #molecular-weight 26268 #checksum 3816 SEQUENCE /// ENTRY S15102 #type complete TITLE eosinophil major basic protein 2 precursor - guinea pig ORGANISM #formal_name Cavia porcellus #common_name guinea pig DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 21-Jul-2000 ACCESSIONS S15102; S18501 REFERENCE S15102 !$#authors Aoki, I.; Shindoh, Y.; Nishida, T.; Nakai, S.; Hong, Y.M.; !1Mio, M.; Saito, T.; Tasaka, K. !$#journal FEBS Lett. (1991) 282:56-60 !$#title Comparison of the amino acid and nucleotide sequences !1between human and two guinea pig major basic proteins. !$#cross-references MUID:91224343; PMID:2026266 !$#accession S15102 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-234 ##label AOK !'##cross-references DDBJ:D00817; NID:g3135095; PIDN:BAA00697.1; !1PID:g220293 !$#accession S18501 !'##molecule_type protein !'##residues 116,'X',118-134,'X',136-137,'X',139-145;161-176;181-200 !1##label AOK2 CLASSIFICATION #superfamily eosinophil major basic protein precursor; !1C-type lectin homology KEYWORDS antibiotic; chondroitin sulfate proteoglycan; cytotoxin; !1eosinophil; glycoprotein; inflammation; monomer FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-115 #domain propeptide #status predicted #label PRO\ !$116-234 #product eosinophil major basic protein 2 #status !8experimental #label MAT\ !$117-232 #domain C-type lectin homology #label LCH\ !$24,25 #binding_site carbohydrate (Ser) (covalent) #status !8predicted\ !$69 #binding_site chondroitin sulfate (Ser) (covalent) !8#status predicted\ !$135-232,209-224 #disulfide_bonds #status predicted SUMMARY #length 234 #molecular-weight 26140 #checksum 4974 SEQUENCE /// ENTRY LNHU1 #type complete TITLE hepatic lectin H1 - human ALTERNATE_NAMES asialoglycoprotein receptor H1 (ASGP-H1) ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 22-Jun-1999 ACCESSIONS A22509 REFERENCE A22509 !$#authors Spiess, M.; Schwartz, A.L.; Lodish, H.F. !$#journal J. Biol. Chem. (1985) 260:1979-1982 !$#title Sequence of human asialoglycoprotein receptor cDNA: an !1internal signal sequence for membrane insertion. !$#cross-references MUID:85130911; PMID:2982798 !$#accession A22509 !'##molecule_type mRNA !'##residues 1-291 ##label SPI !'##cross-references GB:M10058; NID:g179078; PIDN:AAA51785.1; !1PID:g179079 COMMENT This receptor is expressed in mammals exclusively in hepatic !1parenchymal cells. COMMENT By homology with the R1 receptor, the initiator Met is !1removed after translation and the extracellular domain !1contains the ligand-binding site. COMMENT A cytoplasmic serine residue is phosphorylated. GENETICS !$#gene GDB:ASGR1 !'##cross-references GDB:118754; OMIM:108360 !$#map_position 17p13-17p11 CLASSIFICATION #superfamily hepatic lectin; C-type lectin homology KEYWORDS endocytosis; glycoprotein; lectin; phosphoprotein; receptor; !1transmembrane protein FEATURE !$2-291 #product hepatic lectin H1 #status predicted #label !8MAT\ !$2-40 #domain intracellular #status predicted #label INT\ !$41-59 #domain transmembrane #status predicted #label TMM\ !$60-291 #domain extracellular #status predicted #label EXT\ !$154-277 #domain C-type lectin homology #label LCH\ !$79,147 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 291 #molecular-weight 33186 #checksum 7653 SEQUENCE /// ENTRY LNRTL #type complete TITLE hepatic lectin - rat ALTERNATE_NAMES ASGP; asialoglycoprotein receptor ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 28-Feb-1986 #sequence_revision 04-Dec-1986 #text_change 22-Jun-1999 ACCESSIONS A92497; A94020; B94020; A54727; A03166 REFERENCE A92497 !$#authors Leung, J.O.; Holland, E.C.; Drickamer, K. !$#journal J. Biol. Chem. (1985) 260:12523-12527 !$#title Characterization of the gene encoding the major rat liver !1asialoglycoprotein receptor. !$#cross-references MUID:86008335; PMID:2995379 !$#accession A92497 !'##molecule_type DNA !'##residues 1-284 ##label LEU !'##cross-references GB:K02817; NID:g206646; PIDN:AAA42037.1; !1PID:g206647 REFERENCE A94020 !$#authors Holland, E.C.; Leung, J.O.; Drickamer, K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:7338-7342 !$#title Rat liver asialoglycoprotein receptor lacks a cleavable !1NH-2-terminal signal sequence. !$#cross-references MUID:85063786; PMID:6095287 !$#accession A94020 !'##molecule_type mRNA !'##residues 1-60,'R',62-210 ##label HOL !'##experimental_source clone 22; clone 1 !$#accession B94020 !'##molecule_type mRNA !'##residues 92-284 ##label HO2 !'##note clone 22 codes for a terminator at residue 210 REFERENCE A54727 !$#authors Watts, C. !$#journal Biosci. Rep. (1986) 6:527-534 !$#title Isolation and expression of cDNA clones for a rat liver !1asialoglycoprotein receptor. !$#cross-references MUID:87026895; PMID:2945599 !$#accession A54727 !'##molecule_type mRNA !'##residues 12-284 ##label WAT !'##cross-references GB:M21770; NID:g202985; PIDN:AAA40764.1; !1PID:g202988 !'##experimental_source liver COMMENT Two types of rat hepatic lectin have been identified, RHL-1 !1and RHL-2/3, having a relative abundance of 4:1. These !1receptors mediate glycoprotein endocytosis. COMMENT After removal of sialic acid monomers from the complex !1carbohydrate moieties of plasma glycoproteins, terminal !1galactose units are recognized by this hepatic receptor. COMMENT The unusual orientation of this protein across the membrane !1is postulated to occur by recognition of an internal !1transmembrane segment as a signal sequence. GENETICS !$#introns 23/1; 62/1; 94/1; 118/1; 147/1; 197/3; 233/2 CLASSIFICATION #superfamily hepatic lectin; C-type lectin homology KEYWORDS endocytosis; glycoprotein; lectin; receptor; transmembrane !1protein FEATURE !$2-284 #product hepatic lectin #status predicted #label MAT\ !$2-39 #domain intracellular #status predicted #label INT\ !$40-60 #domain transmembrane #status predicted #label TMM\ !$61-284 #domain extracellular #status predicted #label EXT\ !$153-276 #domain C-type lectin homology #label LCH\ !$75,78,146 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 284 #molecular-weight 32849 #checksum 2656 SEQUENCE /// ENTRY LNHU2A #type complete TITLE asialoglycoprotein receptor H2a - human ALTERNATE_NAMES hepatic lectin H2a CONTAINS ASGPR; asialoglycoprotein receptor H2a; asialoglycoprotein receptor H2b ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 10-Dec-1999 ACCESSIONS A25179; A39100; B39100; I37995; A49466; B49466; S14525 REFERENCE A25179 !$#authors Spiess, M.; Lodish, H.F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:6465-6469 !$#title Sequence of a second human asialoglycoprotein receptor: !1conservation of two receptor genes during evolution. !$#cross-references MUID:86016723; PMID:3863106 !$#accession A25179 !'##molecule_type mRNA !'##residues 1-311 ##label SPI !'##cross-references GB:M11025; NID:g179080; PIDN:AAB59519.1; !1PID:g179081 REFERENCE A39100 !$#authors Lederkremer, G.Z.; Lodish, H.F. !$#journal J. Biol. Chem. (1991) 266:1237-1244 !$#title An alternatively spliced miniexon alters the subcellular !1fate of the human asialoglycoprotein receptor H2 subunit. !1Endoplasmic reticulum retention and degradation or cell !1surface expression. !$#cross-references MUID:91093236; PMID:1985943 !$#accession A39100 !'##molecule_type DNA; mRNA !'##residues 69-99 ##label LED !'##cross-references GB:M38420; NID:g184395 !$#accession B39100 !'##molecule_type DNA; mRNA !'##residues 69-81,87-99 ##label LE2 !'##cross-references GB:M38420; NID:g184395 REFERENCE I37995 !$#authors Paietta, E.; Stockert, R.J.; Racevskis, J. !$#journal Hepatology (1992) 15:395-402 !$#title Differences in the abundance of variably spliced transcripts !1for the second asialoglycoprotein receptor polypeptide, H2, !1in normal and transformed human liver. !$#cross-references MUID:92184202; PMID:1371982 !$#accession I37995 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-23,43-81,87-311 ##label PAI !'##cross-references EMBL:X55283; NID:g34354; PIDN:CAA38997.1; !1PID:g34355 REFERENCE A49466 !$#authors Yuk, M.H.; Lodish, H.F. !$#journal J. Cell Biol. (1993) 123:1735-1749 !$#title Two pathways for the degradation of the H2 subunit of the !1asialoglycoprotein receptor in the endoplasmic reticulum. !$#cross-references MUID:94103329; PMID:8276894 !$#accession A49466 !'##molecule_type protein !'##residues 78-98 ##label YUK !$#accession B49466 !'##molecule_type protein !'##residues 87-98 ##label YU2 COMMENT The functioning ligand-binding unit of this receptor is !1thought to be at least a dimer. GENETICS !$#gene GDB:ASGR2; L-H2 !'##cross-references GDB:118755; OMIM:108361 !$#map_position 17p13-17p11 CLASSIFICATION #superfamily hepatic lectin; C-type lectin homology KEYWORDS alternative splicing; endocytosis; glycoprotein; lectin; !1liver; phosphoprotein; receptor; transmembrane protein FEATURE !$1-311 #product asialoglycoprotein receptor H2a #status !8predicted #label MAT1\ !$1-81,87-311 #product asialoglycoprotein receptor H2b #status !8predicted #label MAT2\ !$1-58 #domain intracellular #status predicted #label INT\ !$1-23,43-81,87-311 #product asialoglycoprotein receptor H2c #status !8predicted #label MAT3\ !$59-78 #domain transmembrane #status predicted #label TMM\ !$79-311 #domain extracellular #status predicted #label EXT\ !$177-300 #domain C-type lectin homology #label LCH\ !$102,170,305 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 311 #molecular-weight 35191 #checksum 5467 SEQUENCE /// ENTRY LNRT2 #type complete TITLE hepatic lectin 2 - rat ALTERNATE_NAMES asialoglycoprotein receptor RHL-2/3 (ASGP-R2/3) ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1988 #sequence_revision 09-Apr-1998 #text_change 22-Jun-1999 ACCESSIONS B28462; A28462; A31601; A26888; A25417 REFERENCE A28462 !$#authors Halberg, D.F.; Wager, R.E.; Farrell, D.C.; Hildreth IV, J.; !1Quesenberry, M.S.; Loeb, J.A.; Holland, E.C.; Drickamer, K. !$#journal J. Biol. Chem. (1987) 262:9828-9838 !$#title Major and minor forms of the rat liver asialoglycoprotein !1receptor are independent galactose-binding proteins. Primary !1structure and glycosylation heterogeneity of minor receptor !1forms. !$#cross-references MUID:87250656; PMID:3597443 !$#accession B28462 !'##molecule_type mRNA !'##residues 1-301 ##label HAL !'##cross-references GB:J02762; NID:g205162; PIDN:AAA41522.1; !1PID:g205163 !$#accession A28462 !'##molecule_type protein !'##residues 88-96,'X',98-118,'X',120;129-158;177-182,'X',184,'X', !1186-189;192-290,'C',292-301 ##label HA2 REFERENCE A31601 !$#authors Sanford, J.P.; Elliott, R.W.; Doyle, D. !$#journal DNA (1988) 7:721-728 !$#title Asialoglycoprotein receptor genes are linked on chromosome !111 in the mouse. !$#cross-references MUID:89170119; PMID:3234178 !$#accession A31601 !'##molecule_type mRNA !'##residues 1-301 ##label SAN !'##cross-references GB:X07636; NID:g57066; PIDN:CAA30476.1; PID:g57067 REFERENCE A26888 !$#authors McPhaul, M.; Berg, P. !$#journal Mol. Cell. Biol. (1987) 7:1841-1847 !$#title Identification and characterization of cDNA clones encoding !1two homologous proteins that are part of the !1asialoglycoprotein receptor. !$#cross-references MUID:87257885; PMID:3600647 !$#accession A26888 !'##molecule_type mRNA !'##residues 1-152,'A',154-201,'I',203-259,'C',261-301 ##label MCP !'##cross-references GB:M16347; NID:g206648; PIDN:AAA42038.1; !1PID:g206649 !'##note the authors translated the codon GCA for residue 153 as Arg and !1ATT for residue 202 as Asn REFERENCE A25417 !$#authors Drickamer, K.; Mamon, J.F.; Binns, G.; Leung, J.O. !$#journal J. Biol. Chem. (1984) 259:770-778 !$#title Primary structure of the rat liver asialoglycoprotein !1receptor: structural evidence for multiple polypeptide !1species. !$#cross-references MUID:84111554; PMID:6319386 !$#accession A25417 !'##molecule_type protein !'##residues 201-259,'C',261-281,'ND',284-301 ##label DRI COMMENT Calcium is required for ligand binding. CLASSIFICATION #superfamily hepatic lectin; C-type lectin homology KEYWORDS endocytosis; glycoprotein; lectin; liver; receptor; !1transmembrane protein FEATURE !$2-60 #domain intracellular #status predicted #label INT\ !$61-77 #domain transmembrane #status predicted #label TRN\ !$78-301 #domain extracellular #status predicted #label EXT\ !$170-293 #domain C-type lectin homology #label LCH\ !$97,119,165 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 301 #molecular-weight 35027 #checksum 5883 SEQUENCE /// ENTRY LNCHL #type complete TITLE hepatic lectin - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 08-Oct-1981 #sequence_revision 08-Oct-1981 #text_change 22-Jun-1999 ACCESSIONS A03167; A28194; A40427 REFERENCE A03167 !$#authors Drickamer, K. !$#journal J. Biol. Chem. (1981) 256:5827-5839 !$#title Complete amino acid sequence of a membrane receptor for !1glycoproteins. Sequence of the chicken hepatic lectin. !$#cross-references MUID:81215504; PMID:7240175 !$#accession A03167 !'##molecule_type protein !'##residues 1-207 ##label DRI !'##note some or all of the cysteines are involved in disulfide bonds !'##note residues 24-48 form an uncharged, hydrophobic region that may !1interact with or extend through the hepatic cell membrane REFERENCE A28194 !$#authors Mellow, T.E.; Halberg, D.; Drickamer, K. !$#journal J. Biol. Chem. (1988) 263:5468-5473 !$#title Endocytosis of N-acetylglucosamine-containing glycoproteins !1by rat fibroblasts expressing a single species of chicken !1liver glycoprotein receptor. !$#cross-references MUID:88186849; PMID:3281941 !$#accession A28194 !'##molecule_type mRNA !'##residues 1-207 ##label MEL !'##cross-references GB:J03188; NID:g212246; PIDN:AAA48937.1; !1PID:g212247 REFERENCE A40427 !$#authors Bezouska, K.; Crichlow, G.V.; Rose, J.M.; Taylor, M.E.; !1Drickamer, K. !$#journal J. Biol. Chem. (1991) 266:11604-11609 !$#title Evolutionary conservation of intron position in a subfamily !1of genes encoding carbohydrate-recognition domains. !$#cross-references MUID:91268022; PMID:2050668 !$#accession A40427 !'##molecule_type DNA !'##residues 1-207 ##label BEZ !'##cross-references GB:M63225; GB:M63226; GB:M63227; GB:M63228; !1GB:M63229; GB:M63230; NID:g211914; PIDN:AAA48814.1; !1PID:g211916 COMMENT Hepatic lectin is a membrane receptor protein that !1recognizes and binds exposed N-acetylglucosamine moieties of !1plasma glycoproteins, thus mediating their clearance (from !1the circulation) and endocytosis. GENETICS !$#introns 15/1; 50/1; 75/1; 125/3; 163/2 CLASSIFICATION #superfamily hepatic lectin; C-type lectin homology KEYWORDS acetylated amino end; glycoprotein; lectin; transmembrane !1protein FEATURE !$1-23 #domain intracellular #status predicted #label INT\ !$24-47 #domain transmembrane #status predicted #label TRA\ !$48-207 #domain extracellular #status predicted #label EXT\ !$78-201 #domain C-type lectin homology #label LCH\ !$1 #modified_site acetylated amino end (Met) #status !8experimental\ !$67 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 207 #molecular-weight 24216 #checksum 1321 SEQUENCE /// ENTRY WMVZF2 #type complete TITLE hepatic lectin homolog (BamHI-ORF2) - fowlpox virus (isolate HP-438[Munich]) ORGANISM #formal_name fowlpox virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jun-2000 ACCESSIONS B29963 REFERENCE JT0442 !$#authors Tomley, F.; Binns, M.; Campbell, J.; Boursnell, M. !$#journal J. Gen. Virol. (1988) 69:1025-1040 !$#title Sequence analysis of an 11.2 kilobase, near-terminal, BamHI !1fragment of fowlpox virus. !$#cross-references MUID:88229622; PMID:2836548 !$#accession B29963 !'##molecule_type DNA !'##residues 1-167 ##label TOM !'##cross-references GB:D00295; NID:g221380; PIDN:BAA00192.1; !1PID:g221383 CLASSIFICATION #superfamily fowlpox virus hepatic lectin homolog; C-type !1lectin homology KEYWORDS early protein FEATURE !$49-152 #domain C-type lectin homology #label LCH SUMMARY #length 167 #molecular-weight 19869 #checksum 7089 SEQUENCE /// ENTRY WMVZEL #type complete TITLE hepatic lectin homolog (BamHI-ORF11) - fowlpox virus (isolate HP-438[Munich]) ORGANISM #formal_name fowlpox virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jun-2000 ACCESSIONS B30087 REFERENCE JT0442 !$#authors Tomley, F.; Binns, M.; Campbell, J.; Boursnell, M. !$#journal J. Gen. Virol. (1988) 69:1025-1040 !$#title Sequence analysis of an 11.2 kilobase, near-terminal, BamHI !1fragment of fowlpox virus. !$#cross-references MUID:88229622; PMID:2836548 !$#accession B30087 !'##molecule_type DNA !'##residues 1-143 ##label TOM !'##cross-references GB:D00295; NID:g221380; PIDN:BAA00206.1; !1PID:g221397 CLASSIFICATION #superfamily fowlpox virus hepatic lectin homolog; C-type !1lectin homology KEYWORDS early protein FEATURE !$36-125 #domain C-type lectin homology #label LCH SUMMARY #length 143 #molecular-weight 16662 #checksum 5550 SEQUENCE /// ENTRY WMVZF8 #type complete TITLE hepatic lectin homolog (BamHI-ORF8) - fowlpox virus (isolate HP-438[Munich]) ORGANISM #formal_name fowlpox virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jun-2000 ACCESSIONS H29963 REFERENCE JT0442 !$#authors Tomley, F.; Binns, M.; Campbell, J.; Boursnell, M. !$#journal J. Gen. Virol. (1988) 69:1025-1040 !$#title Sequence analysis of an 11.2 kilobase, near-terminal, BamHI !1fragment of fowlpox virus. !$#cross-references MUID:88229622; PMID:2836548 !$#accession H29963 !'##molecule_type DNA !'##residues 1-116 ##label TOM !'##cross-references GB:D00295; NID:g221380; PIDN:BAA00203.1; !1PID:g221394 CLASSIFICATION #superfamily fowlpox virus hepatic lectin homolog; C-type !1lectin homology KEYWORDS early protein FEATURE !$48-116 #domain C-type lectin homology #status atypical !8#label LEC SUMMARY #length 116 #molecular-weight 13256 #checksum 3168 SEQUENCE /// ENTRY LNHUER #type complete TITLE IgE Fc receptor II, low-affinity [validated] - human ALTERNATE_NAMES Blast-2; CD23; Fc-epsilon-RII; lymphocyte IgE receptor CONTAINS IgE Fc receptor II, splice form a; IgE Fc receptor II, splice form a'; IgE Fc receptor II, splice form b; IgE Fc receptor II, splice form b'; soluble IgE-binding factor ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 15-Sep-2000 ACCESSIONS A26067; S03279; S39442; S39443; A26164; A26589; A31924; !1JL0132; S29107 REFERENCE A26067 !$#authors Kikutani, H.; Inui, S.; Sato, R.; Barsumian, E.L.; Owaki, !1H.; Yamasaki, K.; Kaisho, T.; Uchibayashi, N.; Hardy, R.R.; !1Hirano, T.; Tsunasawa, S.; Sakiyama, F.; Suemura, M.; !1Kishimoto, T. !$#journal Cell (1986) 47:657-665 !$#title Molecular structure of human lymphocyte receptor for !1immunoglobulin E. !$#cross-references MUID:87051737; PMID:2877743 !$#accession A26067 !'##molecule_type mRNA !'##residues 1-321 ##label KIK !'##cross-references GB:M14766; NID:g182449; PIDN:AAA52435.1; !1PID:g182450 !'##experimental_source EBV-transformed B lymphoblastoid cells RPMI-8866 REFERENCE S03279 !$#authors Suter, U.; Bastos, R.; Hofstetter, H. !$#journal Nucleic Acids Res. (1987) 15:7295-7308 !$#title Molecular structure of the gene and the 5'-flanking region !1of the human lymphocyte immunoglobulin E receptor. !$#cross-references MUID:88015596; PMID:2958779 !$#accession S03279 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type DNA !'##residues 157-284 ##label SUT !'##cross-references GB:X06049; NID:g31316 !'##note all exon sequences were determined but the complete sequence is !1not shown REFERENCE S39442 !$#authors Matsui, M.; Nunez, R.; Sachi, Y.; Lynch, R.G.; Yodoi, J. !$#journal FEBS Lett. (1993) 335:51-56 !$#title Alternative transcripts of the human CD23/Fc-epsilon-RII. A !1possible novel mechanism of generating a soluble isoform in !1the type-II cell surface receptor. !$#cross-references MUID:94063078; PMID:8243664 !$#accession S39442 !'##molecule_type DNA !'##residues 1-7,'D',47-50 ##label MAS1 !'##experimental_source splice form a' !$#accession S39443 !'##molecule_type DNA !'##residues 'MNPPSQD',47-50 ##label MAS2 !'##experimental_source splice form b' REFERENCE A26164 !$#authors Ludin, C.; Hofstetter, H.; Sarfati, M.; Levy, C.A.; Suter, !1U.; Alaimo, D.; Kilchherr, E.; Frost, H.; Delespesse, G. !$#journal EMBO J. (1987) 6:109-114 !$#title Cloning and expression of the cDNA coding for a human !1lymphocyte IgE receptor. !$#cross-references MUID:87218454; PMID:3034567 !$#accession A26164 !'##molecule_type mRNA !'##residues 1-268,'T',270-321 ##label LUD !'##cross-references GB:X04772; NID:g34002; PIDN:CAA28465.1; PID:g34003 !'##note the codon given for 269-Asn (ACC) is inconsistent with the !1authors' translation !'##note part of this sequence, including the amino end of soluble forms !1of the protein, were determined by protein sequencing REFERENCE A26589 !$#authors Ikuta, K.; Takami, M.; Kim, C.W.; Honjo, T.; Miyoshi, T.; !1Tagaya, Y.; Kawabe, T.; Yodoi, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:819-823 !$#title Human lymphocyte Fc receptor for IgE: sequence homology of !1its cloned cDNA with animal lectins. !$#cross-references MUID:87118255; PMID:2949326 !$#accession A26589 !'##molecule_type mRNA !'##residues 1-321 ##label IKU !'##cross-references GB:M15059; NID:g182447; PIDN:AAA52434.1; !1PID:g182448 !'##note part of this sequence, including the amino end of soluble forms !1of the protein, were determined by protein sequencing REFERENCE A31924 !$#authors Yokota, A.; Kikutani, H.; Tanaka, T.; Sato, R.; Barsumian, !1E.L.; Suemura, M.; Kishimoto, T. !$#journal Cell (1988) 55:611-618 !$#title Two species of human Fc-epsilon receptor II (Fc-epsilon-RII/ !1CD23): tissue-specific and IL-4-specific regulation of gene !1expression. !$#cross-references MUID:89028672; PMID:2972386 !$#accession A31924 !'##molecule_type mRNA !'##residues 'MNPPSQ',8-14 ##label YOK !'##cross-references GB:M23562; NID:g182444 !'##experimental_source splice form IIb REFERENCE JL0132 !$#authors Letellier, M.; Sarfati, M.; Delespesse, G. !$#journal Mol. Immunol. (1989) 26:1105-1112 !$#title Mechanisms of formation of IgE-binding factors (soluble !1CD23)-I. Fc epsilon R II bearing B cells generate !1IgE-binding factors of different molecular weights. !$#cross-references MUID:90220658; PMID:2534424 !$#accession JL0132 !'##molecule_type protein !'##residues 1-321 ##label LET !'##experimental_source lymphoblastoid B cell line REFERENCE S29107 !$#authors Rose, K.; Turcatti, G.; Graber, P.; Pochon, S.; Regamey, !1P.O.; Jansen, K.U.; Magnenat, E.; Aubonney, N.; Bonnefoy, !1J.Y. !$#journal Biochem. J. (1992) 286:819-824 !$#title Partial characterization of natural and recombinant human !1soluble CD23. !$#cross-references MUID:93038513; PMID:1417742 !$#accession S29107 !'##molecule_type protein !'##residues 152-166;173-179;189-212;230-263;268-306 ##label ROS REFERENCE A51791 !$#authors Padlan, E.A.; Helm, B.A. !$#submission submitted to the Brookhaven Protein Data Bank, June 1993 !$#cross-references PDB:1HLI !$#contents annotation; conformation by theoretical model, residues !1173-285 REFERENCE A65963 !$#authors Bajorath, J. !$#submission submitted to the Brookhaven Protein Data Bank, November 1995 !$#cross-references PDB:1KJE !$#contents annotation; conformation by theoretical model, residues !1173-285 COMMENT The sequence of the splice form a is shown. COMMENT This receptor for the Fc portion of IgE is expressed in !1various hematopoietic cells and has essential roles in the !1regulation of IgE production and in the growth and !1differentiation of B-cells. COMMENT Splice form a is expressed constitutively in B-cells; b is !1expressed in other cell types and in !1interleukin-4-stimulated B-cells. COMMENT Soluble IgE-binding factors are produced by proteolytic !1cleavage of IgE Fc receptor II. GENETICS !$#gene GDB:FCER2; FCE2 !'##cross-references GDB:118888; OMIM:151445 !$#map_position 19p13.3-19p13.3 !$#introns 8/1; 46/1; 64/1; 85/1; 106/1; 127/1; 157/1; 207/3; 243/2 CLASSIFICATION #superfamily IgE receptor II; C-type lectin homology KEYWORDS alternative splicing; B-cell; glycoprotein; immunoglobulin !1receptor; macrophage; tandem repeat; transmembrane protein FEATURE !$'MNPPSQD',47-321 #product IgE Fc receptor II, splice form b' #status !8predicted #label SFBI\ !$'MNPPSQ',8-321 #product IgE Fc receptor II, splice form b #status !8predicted #label SFB\ !$1-321 #product IgE Fc receptor II, splice form a #status !8predicted #label SFA\ !$1-23 #domain intracellular #status predicted #label INT\ !$1-7,'D',47-321 #product IgE Fc receptor II, splice form a' #status !8predicted #label SFAI\ !$14-20 #region stop-transfer sequence\ !$22-45 #domain transmembrane #status predicted #label TMM\ !$46-321 #domain extracellular #status predicted #label EXT\ !$64-84 #region 21-residue repeat\ !$81-321 #product soluble IgE-binding factor (37K) #status !8predicted #label IGE\ !$85-105 #region 21-residue repeat\ !$102-321 #product soluble IgE-binding factor (33K) #status !8predicted #label IGB\ !$106-126 #region 21-residue repeat\ !$125-321 #product soluble IgE-binding factor (29K) #status !8predicted #label IGI\ !$148-321 #product soluble IgE-binding factor (25-27K), long !8form #status experimental #label BF1\ !$150-321 #product soluble IgE-binding factor (25-27K), short !8form #status experimental #label BF2\ !$163-282 #domain C-type lectin homology #label LCH\ !$63 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$147-148 #cleavage_site Lys-Leu (unidentified proteinase) !8#status experimental\ !$149-150 #cleavage_site Arg-Met (unidentified proteinase) !8#status experimental\ !$191-282,259-273 #disulfide_bonds #status experimental SUMMARY #length 321 #molecular-weight 36468 #checksum 2882 SEQUENCE /// ENTRY LNMSER #type complete TITLE IgE Fc receptor, low-affinity - mouse ALTERNATE_NAMES Blast-2; CD23; Fc-epsilon-RII; lymphocyte IgE receptor ORGANISM #formal_name Mus musculus #common_name house mouse DATE 12-Feb-1993 #sequence_revision 28-Oct-1994 #text_change 22-Jun-1999 ACCESSIONS A43518; A33840 REFERENCE A43518 !$#authors Gollnick, S.O.; Trounstine, M.L.; Yamashita, L.C.; Kehry, !1M.R.; Moore, K.W. !$#journal J. Immunol. (1990) 144:1974-1982 !$#title Isolation, characterization, and expression of cDNA clones !1encoding the mouse Fc receptor for IgE (FcepsilonRII). !$#cross-references MUID:90171598; PMID:2137845 !$#accession A43518 !'##molecule_type mRNA !'##residues 1-331 ##label GOL !'##cross-references GB:M34163; NID:g193242; PIDN:AAA37603.1; !1PID:g309227 REFERENCE A33840 !$#authors Bettler, B.; Hofstetter, H.; Rao, M.; Yokoyama, W.M.; !1Kilchherr, F.; Conrad, D.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:7566-7570 !$#title Molecular structure and expression of the murine lymphocyte !1low-affinity receptor for IgE (Fc-epsilon-RII). !$#cross-references MUID:90017519; PMID:2529542 !$#accession A33840 !'##molecule_type mRNA !'##residues 1-331 ##label BET !'##cross-references GB:M99371; NID:g193245; PIDN:AAA74898.1; !1PID:g193246; GB:M27150 COMMENT This receptor for the Fc portion of IgE is expressed in !1various hematopoietic cells and has essential roles both in !1the regulation of IgE production and in the growth and !1differentiation of B-cells. CLASSIFICATION #superfamily IgE receptor II; C-type lectin homology KEYWORDS B-cell; glycoprotein; immunoglobulin receptor; macrophage; !1tandem repeat; transmembrane protein FEATURE !$1-25 #domain intracellular #status predicted #label INT\ !$14-22 #region stop-transfer sequence\ !$26-46 #domain transmembrane #status predicted #label TMM\ !$47-331 #domain extracellular #status predicted #label EXT\ !$66-86 #region 21-residue repeat\ !$87-107 #region 21-residue repeat\ !$108-128 #region 21-residue repeat\ !$129-149 #region 21-residue repeat\ !$186-305 #domain C-type lectin homology #label LCH\ !$65,114 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 331 #molecular-weight 37647 #checksum 6065 SEQUENCE /// ENTRY S34198 #type complete TITLE IgE Fc receptor II, low-affinity - rat ALTERNATE_NAMES CD23; lymphocyte IgE receptor ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 06-Jan-1995 #sequence_revision 06-Jan-1995 #text_change 22-Jun-1999 ACCESSIONS S34198 REFERENCE S34198 !$#authors Flores-Romo, L.; Shield, J.; Humbert, Y.; Graber, P.; Aubry, !1J.P.; Gauchat, J.F.; Ayala, G.; Allet, B.; Chavez, M.; !1Bazin, H.; Capron, M.; Bonnefoy, J.Y. !$#submission submitted to the EMBL Data Library, June 1993 !$#description Inhibition of an in vivo antigen-specific IgE response by !1antibodies to CD23. !$#accession S34198 !'##molecule_type mRNA !'##residues 1-309 ##label FLO !'##cross-references EMBL:X73579; NID:g313672; PIDN:CAA51981.1; !1PID:g313673 CLASSIFICATION #superfamily IgE receptor II; C-type lectin homology KEYWORDS B-cell; glycoprotein; immunoglobulin receptor; macrophage; !1tandem repeat; transmembrane protein FEATURE !$1-25 #domain intracellular #status predicted #label INT\ !$14-22 #region stop-transfer sequence\ !$24-46 #domain transmembrane #status predicted #label TMM\ !$47-309 #domain extracellular #status predicted #label EXT\ !$126-309 #product soluble IgE-binding factor (29K) #status !8predicted #label IGI\ !$149-309 #product soluble IgE-binding factor (25-27K) #status !8predicted #label BF1\ !$164-283 #domain C-type lectin homology #label LCH\ !$192-283,260-274 #disulfide_bonds #status predicted SUMMARY #length 309 #molecular-weight 35125 #checksum 5082 SEQUENCE /// ENTRY A49707 #type complete TITLE phospholipase A2 receptor precursor - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A49707 REFERENCE A49707 !$#authors Lambeau, G.; Ancian, P.; Barhanin, J.; Lazdunski, M. !$#journal J. Biol. Chem. (1994) 269:1575-1578 !$#title Cloning and expression of a membrane receptor for secretory !1phospholipases A-2. !$#cross-references MUID:94124484; PMID:8294398 !$#accession A49707 !'##status preliminary !'##molecule_type mRNA !'##residues 1-1458 ##label LAM !'##cross-references GB:U03455; NID:g456375; PIDN:AAC48402.1; !1PID:g456376 CLASSIFICATION #superfamily phospholipase A2 receptor; C-type lectin !1homology; fibronectin type II repeat homology KEYWORDS glycoprotein; receptor; skeletal muscle; tandem repeat; !1transmembrane protein FEATURE !$176-217 #domain fibronectin type II repeat homology #label !82F1\ !$376-499 #domain C-type lectin homology #label LCH1\ !$956-1094 #domain C-type lectin homology #label LCH2 SUMMARY #length 1458 #molecular-weight 167199 #checksum 6528 SEQUENCE /// ENTRY A36563 #type complete TITLE mannose receptor precursor - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A36563; A60926; A44255; B44255; C44255; D44255; E44255; !1F44255; G44255; H44255; I44255 REFERENCE A36563 !$#authors Taylor, M.E.; Conary, J.T.; Lennartz, M.R.; Stahl, P.D.; !1Drickamer, K. !$#journal J. Biol. Chem. (1990) 265:12156-12162 !$#title Primary structure of the mannose receptor contains multiple !1motifs resembling carbohydrate-recognition domains. !$#cross-references MUID:90324192; PMID:2373685 !$#accession A36563 !'##molecule_type mRNA !'##residues 1-1456 ##label TAY !'##cross-references GB:J05550; NID:g188675; PIDN:AAA59868.1; !1PID:g188676 !'##note parts of this sequence, including the amino end of the mature !1protein, were confirmed by protein sequencing REFERENCE A60926 !$#authors Ezekowitz, R.A.B.; Sastry, K.; Bailly, P.; Warner, A. !$#journal J. Exp. Med. (1990) 172:1785-1794 !$#title Molecular characterization of the human macrophage mannose !1receptor: demonstration of multiple carbohydrate !1recognition-like domains and phagocytosis of yeasts in Cos-1 !1cells. !$#cross-references MUID:91079783; PMID:2258707 !$#accession A60926 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-1333,'T',1335-1456 ##label EZE !'##cross-references GB:X55635 !'##note translation of the nucleotide sequence is incomplete !'##note in the authors' translation additional residues Pro-Glu-Ile are !1shown after 497-Ile REFERENCE A44255 !$#authors Kim, S.J.; Ruiz, N.; Bezouska, K.; Drickamer, K. !$#journal Genomics (1992) 14:721-727 !$#title Organization of the gene encoding the human macrophage !1mannose receptor (MRC1). !$#cross-references MUID:93052405; PMID:1294118 !$#accession A44255 !'##status preliminary; nucleic acid sequence not shown; not compared !1with conceptual translation !'##molecule_type DNA !'##residues 155-233,'KSAL',238-283;346-428;492-569;631-714, !1716-719;783-820,'N',822-865;'SI', !1933-1013;1085-1159;1218-1241,'A',1243-1289,1291-1300 ##label !1KIM !'##note sequence extracted from NCBI backbone (NCBIP:118415, !1NCBIP:118421, NCBIP:118428, NCBIP:118430, NCBIP:118432, !1NCBIP:118435, NCBIP:118437, NCBIP:118439, NCBIP:118441) GENETICS !$#gene GDB:MRC1 !'##cross-references GDB:133759; OMIM:153618 !$#map_position 10p13-10p13 CLASSIFICATION #superfamily phospholipase A2 receptor; C-type lectin !1homology; fibronectin type II repeat homology KEYWORDS duplication; lectin; tandem repeat; transmembrane protein FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$168-209 #domain fibronectin type II repeat homology #label !82F1\ !$223-340 #domain C-type lectin homology #label LCH1\ !$362-486 #domain C-type lectin homology #label LCH2\ !$945-1079 #domain C-type lectin homology #label LCH3 SUMMARY #length 1456 #molecular-weight 166010 #checksum 3510 SEQUENCE /// ENTRY A48925 #type complete TITLE mannose receptor precursor, macrophage - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A48925; S21320; PC2245 REFERENCE A48925 !$#authors Harris, N.; Super, M.; Rits, M.; Chang, G.; Ezekowitz, R.A. !$#journal Blood (1992) 80:2363-2373 !$#title Characterization of the murine macrophage mannose receptor: !1demonstration that the downregulation of receptor expression !1mediated by interferon-gamma occurs at the level of !1transcription. !$#cross-references MUID:93043353; PMID:1421407 !$#accession A48925 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-1455 ##label HAR !'##experimental_source peritoneal macrophage !'##note sequence extracted from NCBI backbone (NCBIP:118733) REFERENCE S21320 !$#authors Harris, N.; Super, M.; Rits, M.; Chang, G.; Ezekowitz, R.B. !$#submission submitted to the EMBL Data Library, April 1992 !$#description Characterization of the murine macrophage mannose receptor: !1Demonstration that the downregulation of receptor expression !1mediated by interferon-gamma occurs at the level of !1transcription. !$#accession S21320 !'##status preliminary !'##molecule_type mRNA !'##residues 1-302,'W',303-1117,'E',1119-1455 ##label HA2 !'##cross-references EMBL:Z11974; NID:g52997; PIDN:CAA78028.1; !1PID:g52998 REFERENCE PC2245 !$#authors Harris, N.; Peters, L.L.; Eicher, E.M.; Rits, M.; Raspberry, !1D.; Eichbaum, Q.G.; Super, M.; Ezekowitz, R.A.B. !$#journal Biochem. Biophys. Res. Commun. (1994) 198:682-692 !$#title The exon-intron structure and chromosomal localization of !1the mouse macrophage mannose receptor gene Mrc1: !1Identification of a ricin-like domain at the N-terminus of !1the receptor. !$#cross-references MUID:94128116; PMID:8297379 !$#accession PC2245 !'##molecule_type mRNA !'##residues 35-105 ##label HA3 GENETICS !$#gene Mrc1 !$#map_position 2 CLASSIFICATION #superfamily phospholipase A2 receptor; C-type lectin !1homology; fibronectin type II repeat homology KEYWORDS membrane protein; receptor FEATURE !$168-209 #domain fibronectin type II repeat homology #label !82F9\ !$361-485 #domain C-type lectin homology #label LCH1\ !$943-1077 #domain C-type lectin homology #label LCH2 SUMMARY #length 1455 #molecular-weight 164807 #checksum 9371 SEQUENCE /// ENTRY LNHUMC #type complete TITLE mannose-binding lectin precursor [validated] - human ALTERNATE_NAMES mannan-binding protein ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1989 #sequence_revision 30-Sep-1991 #text_change 08-Dec-2000 ACCESSIONS JL0115; S05641; A34978; JL0027; JX0319; PC2188; A32266 REFERENCE JL0115 !$#authors Sastry, K.; Herman, G.A.; Day, L.; Deignan, E.; Bruns, G.; !1Morton, C.C.; Ezekowitz, R.A.B. !$#journal J. Exp. Med. (1989) 170:1175-1189 !$#title The human mannose-binding protein gene. Exon structure !1reveals its evolutionary relationship to a human pulmonary !1surfactant gene and localization to chromosome 10. !$#cross-references MUID:90010778; PMID:2477486 !$#accession JL0115 !'##molecule_type DNA !'##residues 1-248 ##label SAS !'##cross-references EMBL:X15422; NID:g34486; PIDN:CAA33462.1; !1PID:g34487 REFERENCE S05641 !$#authors Taylor, M.E.; Brickell, P.M.; Craig, R.K.; Summerfield, J.A. !$#journal Biochem. J. (1989) 262:763-771 !$#title Structure and evolutionary origin of the gene encoding a !1human serum mannose-binding protein. !$#cross-references MUID:90073571; PMID:2590164 !$#accession S05641 !'##molecule_type DNA !'##residues 1-248 ##label TAY !'##cross-references EMBL:X15954; NID:g34480; PIDN:CAA34079.1; !1PID:g1212951 !$#accession A34978 !'##molecule_type protein !'##residues 'X',22-24,'X',26,'X',28-31,'X',33-34,'X',36,'XXXX',41-50 !1##label TAY2 REFERENCE JL0027 !$#authors Ezekowitz, R.A.B.; Day, L.E.; Herman, G.A. !$#journal J. Exp. Med. (1988) 167:1034-1046 !$#title A human mannose-binding protein is an acute-phase reactant !1that shares sequence homology with other vertebrate lectins. !$#cross-references MUID:88171281; PMID:2450948 !$#accession JL0027 !'##molecule_type mRNA !'##residues 1-2,'C',4,'IT',8,'S',10-57,'R',59-60,'GT',63-106,'PGCLRK', !1113,'SSANRNGTYQ',124,'C',126-159,'PLWPP',165,'GM',168-185, !1'MP',188-220,'H',222-233,'S',235-236,'FHLPS',242-248 ##label !1EZE REFERENCE JX0319 !$#authors Kurata, H.; Sannoh, T.; Kozutsumi, Y.; Yokota, Y.; Kawasaki, !1T. !$#journal J. Biochem. (1994) 115:1148-1154 !$#title Structure and function of mannan-binding proteins isolated !1from human liver and serum. !$#cross-references MUID:95073978; PMID:7982896 !$#accession JX0319 !'##molecule_type protein !'##residues 1-248 ##label KUR1 !$#accession PC2188 !'##molecule_type mRNA !'##residues 1-20 ##label KUR2 !'##experimental_source liver and serum COMMENT Mannose-binding lectins are opsonins that are important in !1host defense against pathogenic organisms with mannose-rich !1cell walls. COMMENT This protein is a Ca2+-requring animal lectin specific for !1mannose and N-acetylglucosamine. GENETICS !$#gene GDB:MBL !'##cross-references GDB:120167; OMIM:154545 !$#map_position 10q11.2-10q11.2 !$#introns 63/1; 102/1; 125/1 CLASSIFICATION #superfamily mannose-binding lectin; C-type lectin homology KEYWORDS acute phase; calcium binding; endoplasmic reticulum; Golgi !1apparatus; hydroxyproline; lectin; liver; plasma FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-248 #product mannose-binding lectin #status experimental !8#label MAT\ !$42-99 #region collagen-like\ !$128-244 #domain C-type lectin homology #label LCH\ !$47,73,79,82,88 #modified_site 4-hydroxyproline (Pro) (partial) !8#status experimental SUMMARY #length 248 #molecular-weight 26143 #checksum 3156 SEQUENCE /// ENTRY LNRTMA #type complete TITLE mannose-binding lectin A precursor - rat ALTERNATE_NAMES serum mannan-binding protein ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS B24791; A29556; A27799 REFERENCE A24791 !$#authors Drickamer, K.; Dordal, M.S.; Reynolds, L. !$#journal J. Biol. Chem. (1986) 261:6878-6887 !$#title Mannose-binding proteins isolated from rat liver contain !1carbohydrate-recognition domains linked to collagenous !1tails. Complete primary structures and homology with !1pulmonary surfactant apoprotein. !$#cross-references MUID:86196130; PMID:3009480 !$#accession B24791 !'##molecule_type mRNA !'##residues 1-238 ##label DR1 REFERENCE A29556 !$#authors Drickamer, K.; McCreary, V. !$#journal J. Biol. Chem. (1987) 262:2582-2589 !$#title Exon structure of a mannose-binding protein gene reflects !1its evolutionary relationship to the asialoglycoprotein !1receptor and nonfibrillar collagens. !$#cross-references MUID:87137502; PMID:3029088 !$#accession A29556 !'##molecule_type DNA !'##residues 1-155,'K',157-238 ##label DR2 !'##cross-references GB:M14104; GB:M14105; NID:g205259; PIDN:AAA98781.1; !1PID:g205261 !'##note the codon AAG for residue 156 is inconsistent with the authors' !1statement that the genomic and cDNA sequences are identical !1within the exons REFERENCE A27799 !$#authors Ikeda, K.; Sannoh, T.; Kawasaki, N.; Kawasaki, T.; !1Yamashina, I. !$#journal J. Biol. Chem. (1987) 262:7451-7454 !$#title Serum lectin with known structure activates complement !1through the classical pathway. !$#cross-references MUID:87222358; PMID:3584121 !$#accession A27799 !'##molecule_type protein !'##residues 18-42 ##label IKE COMMENT Mannose-binding lectins are opsonins that are important in !1host defense against pathogenic organisms with mannose-rich !1cell walls. COMMENT This plasma protein binds mannose and N-acetylglucosamine !1and can activate complement. COMMENT The molecule consists of approximately 20 identical chains !1linked by disulfide bonds. GENETICS !$#introns 51/1; 90/1; 115/1 CLASSIFICATION #superfamily mannose-binding lectin; C-type lectin homology KEYWORDS acute phase; calcium; hydroxylysine; hydroxyproline; lectin; !1liver; plasma FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-238 #product mannose-binding lectin A #status !8experimental #label MAT\ !$36-88 #region collagen-like\ !$85-87 #region cell attachment (R-G-D) motif\ !$118-234 #domain C-type lectin homology #label LCH\ !$61,67,73 #modified_site 4-hydroxyproline (Pro) #status !8experimental\ !$79,82 #modified_site lysine derivative (Lys) (probably !85-hydroxylysine) #status experimental SUMMARY #length 238 #molecular-weight 25308 #checksum 3091 SEQUENCE /// ENTRY LNMSMA #type complete TITLE mannose-binding lectin A precursor - mouse ALTERNATE_NAMES Ra-reactive factor P28b; serum mannan-binding protein ORGANISM #formal_name Mus musculus #common_name house mouse DATE 18-Jun-1993 #sequence_revision 02-Jun-1994 #text_change 16-Jun-2000 ACCESSIONS A46466; B42574; I48650 REFERENCE A46466 !$#authors Sastry, K.; Zahedi, K.; Lelias, J.M.; Whitehead, A.S.; !1Ezekowitz, R.A. !$#journal J. Immunol. (1991) 147:692-697 !$#title Molecular characterization of the mouse mannose-binding !1proteins. The mannose-binding protein A but not C is an !1acute phase reactant. !$#cross-references MUID:91302823; PMID:1712818 !$#accession A46466 !'##molecule_type mRNA !'##residues 1-239 ##label SAS1 !'##cross-references GB:S42292; NID:g1679939; PIDN:AAB19342.1; !1PID:g233016 !'##experimental_source inbred CBA/J, acute phase liver library, pTZ 19 !1vector !'##note sequence extracted from NCBI backbone (NCBIN:42292, !1NCBIP:42293) REFERENCE A42574 !$#authors Kuge, S.; Ihara, S.; Watanabe, E.; Watanabe, M.; Takishima, !1K.; Suga, T.; Mamiya, G.; Kawakami, M. !$#journal Biochemistry (1992) 31:6943-6950 !$#title cDNAs and deduced amino acid sequences of subunits in the !1binding component of mouse bactericidal factor, Ra-reactive !1factor: similarity to mannose-binding proteins. !$#cross-references MUID:92345256; PMID:1637828 !$#accession B42574 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA; protein !'##residues 1-239 ##label KUG !'##cross-references GB:D11441; NID:g220587; PIDN:BAA02006.1; !1PID:g220588 !'##experimental_source BALB/c, liver !'##note sequence extracted from NCBI backbone (NCBIP:110142) REFERENCE I48650 !$#authors Sastry, R.; Wang, J.S.; Brown, D.C.; Ezekowitz, R.A.; !1Tauber, A.I.; Sastry, K.N. !$#journal Mamm. Genome (1995) 6:103-110 !$#title Characterization of murine mannose-binding protein genes !1Mbl1 and Mbl2 reveals features common to other collectin !1genes. !$#cross-references MUID:95284466; PMID:7766991 !$#accession I48650 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-239 ##label SAS2 !'##cross-references EMBL:U09010; NID:g773278; PIDN:AAA82009.1; !1PID:g773280 COMMENT Mannose-binding lectins are opsonins that are important in !1host defense against pathogenic organisms with mannose-rich !1cell walls. GENETICS !$#gene Mbl1 !$#introns 52/1; 91/1; 116/1 CLASSIFICATION #superfamily mannose-binding lectin; C-type lectin homology KEYWORDS acute phase; calcium; hydroxyproline; lectin; liver; plasma FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-238 #product mannose-binding lectin A #status predicted !8#label MAT\ !$36-88 #region collagen-like\ !$119-235 #domain C-type lectin homology #label LCH SUMMARY #length 239 #molecular-weight 25396 #checksum 3024 SEQUENCE /// ENTRY LNRTMC #type complete TITLE mannose-binding lectin C precursor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS A24791; A38322; JX0201; A26798 REFERENCE A24791 !$#authors Drickamer, K.; Dordal, M.S.; Reynolds, L. !$#journal J. Biol. Chem. (1986) 261:6878-6887 !$#title Mannose-binding proteins isolated from rat liver contain !1carbohydrate-recognition domains linked to collagenous !1tails. Complete primary structures and homology with !1pulmonary surfactant apoprotein. !$#cross-references MUID:86196130; PMID:3009480 !$#accession A24791 !'##molecule_type mRNA !'##residues 1-244 ##label DRI !'##cross-references GB:M14103 !'##note part of the sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE A38322 !$#authors Childs, R.A.; Feizi, T.; Yuen, C.T.; Drickamer, K.; !1Quesenberry, M.S. !$#journal J. Biol. Chem. (1990) 265:20770-20777 !$#title Differential recognition of core and terminal portions of !1oligosaccharide ligands by carbohydrate-recognition domains !1of two mannose-binding proteins. !$#cross-references MUID:91065871; PMID:2249985 !$#accession A38322 !'##molecule_type mRNA !'##residues 86,'EL',89-97 ##label CHI REFERENCE JX0201 !$#authors Wada, M.; Itoh, N.; Ohta, M.; Kawasaki, T. !$#journal J. Biochem. (1992) 111:66-73 !$#title Characterization of rat liver mannan-binding protein gene. !$#cross-references MUID:92299655; PMID:1607365 !$#accession JX0201 !'##molecule_type DNA !'##residues 1-244 ##label WAD !'##experimental_source liver !'##note the authors translated the codon CCA for residue 43 as Phe REFERENCE A26798 !$#authors Oka, S.; Itoh, N.; Kawasaki, T.; Yamashina, I. !$#journal J. Biochem. (1987) 101:135-144 !$#title Primary structure of rat liver mannan-binding protein !1deduced from its cDNA sequence. !$#cross-references MUID:87194686; PMID:3032924 !$#accession A26798 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-244 ##label OKA !'##cross-references GB:X05023; NID:g56634; PIDN:CAA28687.1; PID:g56635 COMMENT The molecule contains six identical chains, occurring as !1disulfide-bonded dimers or trimers. COMMENT Mannan-binding proteins are calcium ion-dependent and are !1specific for mannose and N-acetylglucosamine. GENETICS !$#introns 59/1; 98/1; 121/1 CLASSIFICATION #superfamily mannose-binding lectin; C-type lectin homology KEYWORDS calcium; endoplasmic reticulum; Golgi apparatus; !1homohexamer; hydroxyproline; lectin; liver FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-244 #product mannose-binding lectin C #status !8experimental #label MAT\ !$38-94 #region collagen-like\ !$124-240 #domain C-type lectin homology #label LCH\ !$29,34 #disulfide_bonds interchain #status predicted\ !$69 #modified_site 4-hydroxyproline (Pro) #status !8experimental SUMMARY #length 244 #molecular-weight 26014 #checksum 180 SEQUENCE /// ENTRY LNMSMC #type complete TITLE mannose-binding lectin C precursor - mouse ALTERNATE_NAMES Ra-reactive factor P28a ORGANISM #formal_name Mus musculus #common_name house mouse DATE 18-Jun-1993 #sequence_revision 20-Feb-1998 #text_change 16-Jun-2000 ACCESSIONS I48651; B46466; A42574; C42574 REFERENCE I48650 !$#authors Sastry, R.; Wang, J.S.; Brown, D.C.; Ezekowitz, R.A.; !1Tauber, A.I.; Sastry, K.N. !$#journal Mamm. Genome (1995) 6:103-110 !$#title Characterization of murine mannose-binding protein genes !1Mbl1 and Mbl2 reveals features common to other collectin !1genes. !$#cross-references MUID:95284466; PMID:7766991 !$#accession I48651 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-244 ##label SAS1 !'##cross-references EMBL:U09016; NID:g773286; PIDN:AAA82010.1; !1PID:g773288 REFERENCE A46466 !$#authors Sastry, K.; Zahedi, K.; Lelias, J.M.; Whitehead, A.S.; !1Ezekowitz, R.A. !$#journal J. Immunol. (1991) 147:692-697 !$#title Molecular characterization of the mouse mannose-binding !1proteins. The mannose-binding protein A but not C is an !1acute phase reactant. !$#cross-references MUID:91302823; PMID:1712818 !$#accession B46466 !'##molecule_type mRNA !'##residues 1-2,'L',4-14,'A',16-244 ##label SAS2 !'##cross-references GB:S42294; NID:g233017; PIDN:AAB19343.1; !1PID:g233018 !'##experimental_source inbred CBA/J, acute phase liver library, pTZ 19 !1vector !'##note sequence extracted from NCBI backbone (NCBIN:42294, !1NCBIP:42295) REFERENCE A42574 !$#authors Kuge, S.; Ihara, S.; Watanabe, E.; Watanabe, M.; Takishima, !1K.; Suga, T.; Mamiya, G.; Kawakami, M. !$#journal Biochemistry (1992) 31:6943-6950 !$#title cDNAs and deduced amino acid sequences of subunits in the !1binding component of mouse bactericidal factor, Ra-reactive !1factor: similarity to mannose-binding proteins. !$#cross-references MUID:92345256; PMID:1637828 !$#accession A42574 !'##molecule_type mRNA; protein !'##residues 1-244 ##label KUG !'##cross-references GB:D11440; NID:g220585; PIDN:BAA02005.1; !1PID:g220586 !'##experimental_source BALB/c, liver !'##note sequence extracted from NCBI backbone (NCBIP:110137) !'##note parts of the sequence, including the amino end of the mature !1protein, were confirmed by protein sequencing !$#accession C42574 !'##molecule_type protein !'##residues 19,'X',21-28,'X',30-32;72-77,'H',79-80;'G',177-185;187-189, !1'H',191-198 ##label KU2 !'##note source is serum of ICR mice; differences may be allotypic GENETICS !$#gene Mbl2 !$#introns 59/1; 98/1; 121/1 CLASSIFICATION #superfamily mannose-binding lectin; C-type lectin homology KEYWORDS calcium; endoplasmic reticulum; Golgi apparatus; !1homohexamer; hydroxyproline; lectin; liver FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-244 #product mannose-binding lectin C #status !8experimental #label MAT\ !$38-94 #region collagen-like\ !$124-240 #domain C-type lectin homology #label LCH\ !$29,34 #disulfide_bonds interchain #status predicted\ !$69 #modified_site 4-hydroxyproline (Pro) #status !8experimental SUMMARY #length 244 #molecular-weight 25957 #checksum 9270 SEQUENCE /// ENTRY LNHUPS #type complete TITLE pulmonary surfactant protein A precursor (genomic clone) - human ALTERNATE_NAMES alveolar proteinosis protein; pulmonary surfactant 32K apoprotein; pulmonary surfactant-associated protein (PSP-A) ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS A24622; A43628 REFERENCE A24622 !$#authors White, R.T.; Damm, D.; Miller, J.; Spratt, K.; Schilling, !1J.; Hawgood, S.; Benson, B.; Cordell, B. !$#journal Nature (1985) 317:361-363 !$#title Isolation and characterization of the human pulmonary !1surfactant apoprotein gene. !$#cross-references MUID:86014366; PMID:2995821 !$#accession A24622 !'##molecule_type DNA !'##residues 1-248 ##label WHI !'##cross-references GB:M30838; NID:g190564; PIDN:AAA36510.1; !1PID:g190565 !'##note the sequence in GenBank entry HUMPSAP, release 109.0, !1(PID:g190565) has the codon CGA for 100-Pro rather than the !1published CCA !'##note four nucleotide differences, producing amino acid differences !1at positions 45, 50, and 54, were observed in a cDNA clone !1also sequenced by these authors REFERENCE A43628 !$#authors Haagsman, H.P.; White, R.T.; Schilling, J.; Lau, K.; Benson, !1B.J.; Golden, J.; Hawgood, S.; Clements, J.A. !$#journal Am. J. Physiol. (1989) 257:L421-L429 !$#title Studies of the structure of lung surfactant protein SP-A. !$#cross-references MUID:90119861; PMID:2610270 !$#accession A43628 !'##molecule_type protein !'##residues 143-150;220-240;243-248 ##label HAA COMMENT Pulmonary surfactant is a complex of phospholipids and !1proteins that lowers the surface tension at the air-liquid !1interface in the alveoli of the lung. COMMENT This protein is a sialoglycoprotein synthesized by alveolar !1type II cells. It also inhibits surfactant secretion and !1facilitates phospholipid uptake by type II cells. Its !1activities are dependent on the presence of calcium ions. GENETICS !$#gene GDB:SFTPA1; SFTP1; SP-A; SP-A1 !'##cross-references GDB:119593; OMIM:178630 !$#map_position 10q22-10q23 !$#introns 58/1; 98/1; 124/1 CLASSIFICATION #superfamily mannose-binding lectin; C-type lectin homology KEYWORDS alveolar proteinosis; calcium; gaseous exchange; !1glycoprotein; hydroxylysine; hydroxyproline; lung; pulmonary !1surfactant; respiratory distress syndrome FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-248 #product pulmonary surfactant protein A #status !8predicted #label MAT\ !$28-100 #domain collagenous #status predicted #label COL\ !$127-246 #domain C-type lectin homology #label LCH\ !$26 #disulfide_bonds interchain #status experimental\ !$30,33,36,42,57,63, !$76,79,82,91,97 #modified_site 4-hydroxyproline (Pro) #status !8predicted\ !$51,88 #modified_site 5-hydroxylysine (Lys) #status !8predicted\ !$155-246,224-238 #disulfide_bonds #status experimental\ !$207 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 248 #molecular-weight 26280 #checksum 3689 SEQUENCE /// ENTRY LNHUP6 #type complete TITLE pulmonary surfactant protein A precursor (clone 6A) - human ALTERNATE_NAMES pulmonary surfactant 32K apoprotein; pulmonary surfactant-associated protein PSP-A ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS A25720 REFERENCE A25720 !$#authors Floros, J.; Steinbrink, R.; Jacobs, K.; Phelps, D.; Kriz, !1R.; Recny, M.; Sultzman, L.; Jones, S.; Taeusch, H.W.; !1Frank, H.A.; Fritsch, E.F. !$#journal J. Biol. Chem. (1986) 261:9029-9033 !$#title Isolation and characterization of cDNA clones for the 35-kDa !1pulmonary surfactant-associated protein. !$#cross-references MUID:86250832; PMID:3755136 !$#accession A25720 !'##molecule_type mRNA !'##residues 1-248 ##label FLO !'##cross-references GB:M13686; NID:g190669; PIDN:AAA60211.1; !1PID:g190670 !'##note part of the sequence was confirmed by protein sequencing !'##note the amino end of the mature protein, which was not identified, !1is partially acetylated !'##note clones corresponding to two different proteins were sequenced. !1Cotranslational modifications of the proteins (including !1acetylation) produce multiple isoforms GENETICS !$#gene GDB:SFTPA1; SFTP1; SP-A; SP-A1 !'##cross-references GDB:119593; OMIM:178630 !$#map_position 10q22-10q23 CLASSIFICATION #superfamily mannose-binding lectin; C-type lectin homology KEYWORDS acetylated amino end; alveolar proteinosis; calcium; gaseous !1exchange; glycoprotein; hydroxyproline; lung; pulmonary !1surfactant; respiratory distress syndrome FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-248 #product pulmonary surfactant protein A #status !8predicted #label MAT\ !$127-246 #domain C-type lectin homology #label LCH\ !$21 #modified_site acetylated amino end (Glu) (in mature !8form) #status predicted\ !$30,33,36,42,54,57, !$63,76,79,82,91,97 #modified_site 4-hydroxyproline (Pro) #status !8predicted\ !$207 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 248 #molecular-weight 26214 #checksum 3326 SEQUENCE /// ENTRY LNHUP1 #type complete TITLE pulmonary surfactant protein A precursor (clone 1A) - human ALTERNATE_NAMES pulmonary surfactant 32K apoprotein; pulmonary surfactant-associated protein PSP-A ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS B25720 REFERENCE A25720 !$#authors Floros, J.; Steinbrink, R.; Jacobs, K.; Phelps, D.; Kriz, !1R.; Recny, M.; Sultzman, L.; Jones, S.; Taeusch, H.W.; !1Frank, H.A.; Fritsch, E.F. !$#journal J. Biol. Chem. (1986) 261:9029-9033 !$#title Isolation and characterization of cDNA clones for the 35-kDa !1pulmonary surfactant-associated protein. !$#cross-references MUID:86250832; PMID:3755136 !$#accession B25720 !'##molecule_type mRNA !'##residues 1-248 ##label FLO !'##cross-references GB:K03475 !'##note part of the sequence was confirmed by protein sequencing !'##note the amino end of the mature protein, which was not identified, !1is partially acetylated !'##note clones corresponding to two different proteins were sequenced. !1Cotranslational modifications of the proteins (including !1acetylation) produce multiple isoforms GENETICS !$#gene GDB:SFTPA1; SFTP1; SP-A; SP-A1 !'##cross-references GDB:119593; OMIM:178630 !$#map_position 10q22-10q23 CLASSIFICATION #superfamily mannose-binding lectin; C-type lectin homology KEYWORDS acetylated amino end; alveolar proteinosis; calcium; gaseous !1exchange; glycoprotein; hydroxyproline; lung; pulmonary !1surfactant; respiratory distress syndrome FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-248 #product pulmonary surfactant protein A #status !8predicted #label MAT\ !$127-246 #domain C-type lectin homology #label LCH\ !$21 #modified_site acetylated amino end (Glu) (in mature !8form) #status predicted\ !$30,33,36,42,54,57, !$63,76,79,82,91,97 #modified_site 4-hydroxyproline (Pro) #status !8predicted\ !$207 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 248 #molecular-weight 26209 #checksum 4335 SEQUENCE /// ENTRY LNDGPS #type complete TITLE pulmonary surfactant protein A precursor - dog ALTERNATE_NAMES pulmonary surfactant 32K apoprotein; pulmonary surfactant-associated protein PSP-A ORGANISM #formal_name Canis lupus familiaris #common_name dog DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Jul-1999 ACCESSIONS A25296; A61227; A60142 REFERENCE A25296 !$#authors Benson, B.; Hawgood, S.; Schilling, J.; Clements, J.; Damm, !1D.; Cordell, B.; White, R.T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:6379-6383 !$#title Structure of canine pulmonary surfactant apoprotein: cDNA !1and complete amino acid sequence. !$#cross-references MUID:86016705; PMID:3863100 !$#accession A25296 !'##molecule_type mRNA !'##residues 1-248 ##label BEN !'##note the authors translated the codon TTG for residue 60 as Pro !'##note part of the sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE A61227 !$#authors Liau, D.F.; Ryan, S.F. !$#journal Chem. Phys. Lipids (1991) 59:29-38 !$#title Purification of surfactant protein A from dog lung by !1reconstitution with surfactant lipids. !$#cross-references MUID:92163993; PMID:1790579 !$#accession A61227 !'##molecule_type protein !'##residues 18-32 ##label LIA REFERENCE A60142 !$#authors Ross, G.F.; Meuth, J.; Ohning, B.; Kim, Y.; Whitsett, J.A. !$#journal Biochim. Biophys. Acta (1986) 870:267-278 !$#title Purification of canine surfactant-associated glycoproteins !1A. Identification of a collagenase-resistant domain. !$#cross-references MUID:86159848; PMID:3006781 !$#accession A60142 !'##molecule_type protein !'##residues 24-34;95-101,'X',103-108 ##label ROS REFERENCE A93388 !$#authors Patthy, L. !$#journal Nature (1987) 325:490 !$#cross-references MUID:87115834; PMID:3808053 !$#contents annotation; animal lectin domain homology COMMENT Pulmonary surfactant is a complex of phospholipids and !1proteins that lowers the surface tension at the air-liquid !1interface in the alveoli of the lung. COMMENT This protein is a sialoglycoprotein synthesized by alveolar !1type II cells. It also inhibits surfactant secretion and !1facilitates phospholipid uptake by type II cells. Its !1activities are dependent on the presence of calcium ions. CLASSIFICATION #superfamily mannose-binding lectin; C-type lectin homology KEYWORDS alveolar proteinosis; calcium; disulfide bond; gaseous !1exchange; hydroxyproline; lung; pulmonary surfactant; !1respiratory distress syndrome; sialoglycoprotein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-248 #product pulmonary surfactant protein A #status !8experimental #label MPT\ !$28-102 #region collagen-like\ !$127-246 #domain C-type lectin homology #label LCH\ !$20,207 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$30 #modified_site 4-hydroxyproline (Pro) #status !8experimental SUMMARY #length 248 #molecular-weight 26211 #checksum 5767 SEQUENCE /// ENTRY LNRBPS #type complete TITLE pulmonary surfactant protein A precursor - rabbit ALTERNATE_NAMES pulmonary surfactant 32K apoprotein; pulmonary surfactant-associated protein PSP-A ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS A29931 REFERENCE A29931 !$#authors Boggaram, V.; Qing, K.; Mendelson, C.R. !$#journal J. Biol. Chem. (1988) 263:2939-2947 !$#title The major apoprotein of rabbit pulmonary surfactant. !1Elucidation of primary sequence and cyclic AMP and !1developmental regulation. !$#cross-references MUID:88139348; PMID:2830270 !$#accession A29931 !'##molecule_type mRNA !'##residues 1-247 ##label BOG !'##cross-references GB:J03542; NID:g165705; PIDN:AAA31465.1; !1PID:g165706 !'##note 12-Pro was also found !'##note two species of mRNA, which appear to be transcribed from a !1single gene, could produce proteins that are identical !1except at position 12 !'##note the amino end of the mature protein is blocked COMMENT Pulmonary surfactant is a complex of phospholipids and !1proteins that lowers the surface tension at the air-liquid !1interface in the alveoli of the lung. COMMENT This protein is a sialoglycoprotein synthesized by alveolar !1type II cells. It also inhibits surfactant secretion and !1facilitates phospholipid uptake by type II cells. Its !1activities are dependent on the presence of calcium ions. CLASSIFICATION #superfamily mannose-binding lectin; C-type lectin homology KEYWORDS acetylated amino end; alveolar proteinosis; calcium; gaseous !1exchange; glycoprotein; hydroxyproline; lung; pulmonary !1surfactant; respiratory distress syndrome FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-247 #product pulmonary surfactant protein A #status !8predicted #label MAT\ !$27-99 #region collagen-like\ !$126-245 #domain C-type lectin homology #label LCH\ !$16 #modified_site acetylated amino end (Ser) (in mature !8form) #status predicted\ !$206 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 247 #molecular-weight 26071 #checksum 4349 SEQUENCE /// ENTRY LNRTPS #type complete TITLE pulmonary surfactant protein A precursor - rat ALTERNATE_NAMES pulmonary surfactant 32K apoprotein; pulmonary surfactant-associated protein PSP-A ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS A29299; JS0034; S23183 REFERENCE A29299 !$#authors Sano, K.; Fisher, J.; Mason, R.J.; Kuroki, Y.; Schilling, !1J.; Benson, B.; Voelker, D. !$#journal Biochem. Biophys. Res. Commun. (1987) 144:367-374 !$#title Isolation and sequence of a cDNA clone for the rat pulmonary !1surfactant-associated protein (PSP-A). !$#cross-references MUID:87213191; PMID:3579914 !$#contents 0.9 kb cDNA !$#accession A29299 !'##molecule_type mRNA !'##residues 1-248 ##label SAN !'##note part of the sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE JS0034 !$#authors Fisher, J.H.; Emrie, P.A.; Shannon, J.; Sano, K.; Hattler, !1B.; Mason, R.J. !$#journal Biochim. Biophys. Acta (1988) 950:338-345 !$#title Rat pulmonary surfactant protein A is expressed as two !1differently sized mRNA species, which arise from !1differential polyadenylation of one transcript. !$#cross-references MUID:89000785; PMID:2901856 !$#contents 1.6 kb cDNA !$#accession JS0034 !'##molecule_type mRNA !'##residues 1-248 ##label FIS !'##note the codons given for residues 78, 84, and 180 are inconsistent !1with the authors' translation REFERENCE S23183 !$#authors Lacaze-Masmonteil, T.; Fraslon, C.; Bourbon, J.; !1Raymondjean, M.; Kahn, A. !$#journal Eur. J. Biochem. (1992) 206:613-623 !$#title Characterization of the rat pulmonary surfactant protein A !1promoter. !$#cross-references MUID:92298987; PMID:1606951 !$#accession S23183 !'##molecule_type DNA !'##residues 1-32 ##label LAC COMMENT Pulmonary surfactant is a complex of phospholipids and !1proteins that lowers the surface tension at the air-liquid !1interface in the alveoli of the lung. COMMENT This protein is a sialoglycoprotein synthesized by alveolar !1type II cells. It also inhibits surfactant secretion and !1facilitates phospholipid uptake by type II cells. Its !1activities are dependent on the presence of calcium ions. COMMENT Two species of mRNA, which probably are transcribed from a !1single gene, have identical coding regions. COMMENT Size heterogeneity of these proteins arises from !1posttranslational modifications, such as glycosylation, !1proline hydroxylation, sulfation, and carboxylation of !1glutamate. CLASSIFICATION #superfamily mannose-binding lectin; C-type lectin homology KEYWORDS alveolar proteinosis; calcium; gaseous exchange; !1glycoprotein; hydroxyproline; lung; pulmonary surfactant; !1respiratory distress syndrome FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-248 #product pulmonary surfactant protein A #status !8experimental #label MAT\ !$37-109 #region collagen-like\ !$127-246 #domain C-type lectin homology #label LCH\ !$21 #binding_site carbohydrate (Asn) (covalent) #status !8absent\ !$30,33,36,42,54,57, !$63,67,70,76 #modified_site 4-hydroxyproline (Pro) #status !8experimental\ !$207 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 248 #molecular-weight 26288 #checksum 6684 SEQUENCE /// ENTRY A45225 #type complete TITLE pulmonary surfactant protein D precursor - human ALTERNATE_NAMES SP-D ORGANISM #formal_name Homo sapiens #common_name man DATE 16-Apr-1999 #sequence_revision 16-Apr-1999 #text_change 22-Jun-1999 ACCESSIONS A45225; S23434; S24555; S44420; S18382; A56776 REFERENCE A45225 !$#authors Crouch, E.; Rust, K.; Veile, R.; Donis-Keller, H.; Grosso, !1L. !$#journal J. Biol. Chem. (1993) 268:2976-2983 !$#title Genomic organization of human surfactant protein D (SP-D). !1SP-D is encoded on chromosome 10q22.2-23.1. !$#cross-references MUID:93155122; PMID:8428971 !$#accession A45225 !'##molecule_type DNA !'##residues 1-375 ##label CRO !'##cross-references GB:L05483; GB:L05484; GB:L05485; NID:g292505; !1PIDN:AAB59450.1; PID:g292507 !'##experimental_source placenta !'##note sequence extracted from NCBI backbone (NCBIP:124316) REFERENCE S23434 !$#authors Lu, J.; Willis, A.C.; Reid, K.B.M. !$#journal Biochem. J. (1992) 284:795-802 !$#title Purification, characterization and cDNA cloning of human !1lung surfactant protein D. !$#cross-references MUID:92322003; PMID:1339284 !$#accession S23434 !'##molecule_type mRNA !'##residues 1-30,'T',32-121,'P',123-179,'A',181-375 ##label LUJ1 !'##cross-references EMBL:X65018; NID:g34766; PIDN:CAA46152.1; !1PID:g34767 !'##experimental_source lung !$#accession S24555 !'##molecule_type protein !'##residues 214-234,'X',236,'XX',239-241 ##label LUJ2 REFERENCE S44420 !$#authors Hoppe, H.J.; Barlow, P.N.; Reid, K.B.M. !$#journal FEBS Lett. (1994) 344:191-195 !$#title A parallel three stranded alpha-helical bundle at the !1nucleation site of collagen triple-helix formation. !$#cross-references MUID:94244769; PMID:8187882 !$#accession S44420 !'##molecule_type mRNA !'##residues 202-257 ##label HOP REFERENCE S18382 !$#authors Rust, K.; Grosso, L.; Zhang, V.; Chang, D.; Persson, A.; !1Longmore, W.; Cai, G.Z.; Crouch, E. !$#journal Arch. Biochem. Biophys. (1991) 290:116-126 !$#title Human surfactant protein D: SP-D contains a C-type lectin !1carbohydrate recognition domain. !$#cross-references MUID:91378578; PMID:1898081 !$#accession S18382 !'##status preliminary !'##molecule_type mRNA !'##residues 'F',60-205,'P',207-374,'HF' ##label RUS !'##cross-references GB:L05485; NID:g292505 !'##note corrections to this sequence are reported in reference A56776 REFERENCE A56776 !$#authors Crouch, E.; Persson, A.; Chang, D. !$#journal Am. J. Pathol. (1993) 142:241-248 !$#title Accumulation of surfactant protein D in human pulmonary !1alveolar proteinosis. !$#cross-references MUID:93142849; PMID:8424457 !$#accession A56776 !'##status preliminary !'##molecule_type protein !'##residues 46-58,'F',60-62,'E',64-72;223-227,'X',229-239,'P',241-245, !1'X',247-256,'X',258,'X',260 ##label CR2 !'##cross-references PIDN:AAB25037.1; PID:g263973; PIDN:AAB25038.1; !1PID:g263974 !'##experimental_source bronchoalveolar lavage !'##note sequence extracted from NCBI backbone (NCBIP:123024, !1NCBIP:123023); sequence modified after extraction from NCBI !1backbone COMMENT Pulmonary surfactant is a complex of phospholipids and !1proteins that lowers the surface tension at the air-liquid !1interface in the alveoli of the lung. COMMENT This protein is synthesized by alveolar type II cells. GENETICS !$#gene GDB:SFTPD; SFTP4; SP-D !'##cross-references GDB:132674; OMIM:178635 !$#map_position 10q22.2-10q23.1 CLASSIFICATION #superfamily pulmonary surfactant protein D; C-type lectin !1homology KEYWORDS blocked amino end; calcium; glycoprotein; hydroxylysine; !1hydroxyproline; lung; pulmonary surfactant FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-375 #product pulmonary surfactant protein D #status !8predicted #label MAT\ !$21-45 #domain non-collagenous #status predicted #label NC1\ !$46-222 #domain collagenous #status predicted #label COL\ !$223-375 #domain non-collagenous #status predicted #label NC2\ !$254-373 #domain C-type lectin homology #label LCH\ !$90 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$281-373,351-365 #disulfide_bonds #status predicted SUMMARY #length 375 #molecular-weight 37702 #checksum 1234 SEQUENCE /// ENTRY A42046 #type complete TITLE surfactant protein D - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A42046 REFERENCE A42046 !$#authors Shimizu, H.; Fisher, J.H.; Papst, P.; Benson, B.; Lau, K.; !1Mason, R.J.; Voelker, D.R. !$#journal J. Biol. Chem. (1992) 267:1853-1857 !$#title Primary structure of rat pulmonary surfactant protein D. !1cDNA and deduced amino acid sequence. !$#cross-references MUID:92112913; PMID:1370483 !$#accession A42046 !'##status preliminary !'##molecule_type mRNA !'##residues 1-374 ##label SHI !'##cross-references GB:M81231; NID:g207035; PIDN:AAA42170.1; !1PID:g207036 !'##experimental_source lung !'##note sequence extracted from NCBI backbone (NCBIN:76027, !1NCBIP:76031) CLASSIFICATION #superfamily pulmonary surfactant protein D; C-type lectin !1homology FEATURE !$253-372 #domain C-type lectin homology #label LCH SUMMARY #length 374 #molecular-weight 37561 #checksum 2042 SEQUENCE /// ENTRY JN0450 #type complete TITLE conglutinin precursor - bovine ALTERNATE_NAMES C3b-binding protein CONTAINS conglutinin-N ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS JN0450; JC2396; S33235; A23740; S36879; S35044; I46010; !1A29416; S34054 REFERENCE JN0450 !$#authors Suzuki, Y.; Yin, Y.P.; Makino, M.; Kurimura, T.; Wakamiya, !1N. !$#journal Biochem. Biophys. Res. Commun. (1993) 191:335-342 !$#title Cloning and sequencing of a cDNA coding for bovine !1conglutinin. !$#cross-references MUID:93213261; PMID:8460993 !$#accession JN0450 !'##molecule_type mRNA !'##residues 1-371 ##label SUZ !'##cross-references DDBJ:D14085; NID:g285643; PIDN:BAA03170.1; !1PID:g285644 !'##experimental_source liver REFERENCE JC2396 !$#authors Kawasaki, N.; Itoh, N.; Kawasaki, T. !$#journal Biochem. Biophys. Res. Commun. (1994) 198:597-604 !$#title Gene organization and 5'-flanking region sequence of !1conglutinin: A C-type mammalian lectin containing a !1collagen-like domain. !$#cross-references MUID:94128104; PMID:8297370 !$#accession JC2396 !'##molecule_type mRNA !'##residues 1-371 ##label KA2 !'##note The authors translated the codon GAT for residues 250 and 270 !1as Glu REFERENCE S33235 !$#authors Lu, J.; Laursen, S.B.; Thiel, S.; Jensenius, J.C.; Reid, !1K.B.M. !$#journal Biochem. J. (1993) 292:157-162 !$#title The cDNA cloning of conglutinin and identification of liver !1as a primary site of synthesis of conglutinin in members of !1the Bovidae. !$#cross-references MUID:93277452; PMID:7684896 !$#accession S33235 !'##molecule_type mRNA !'##residues 1-172,'H',174-217,'A',219-271,'V',273-371 ##label LUJ !'##cross-references EMBL:X71774; NID:g395267; PIDN:CAA50665.1; !1PID:g395268 !'##experimental_source liver REFERENCE A23740 !$#authors Lee, Y.M.; Leiby, K.R.; Allar, J.; Paris, K.; Lerch, B.; !1Okarma, T.B. !$#journal J. Biol. Chem. (1991) 266:2715-2723 !$#title Primary structure of bovine conglutinin, a member of the !1C-type animal lectin family. !$#cross-references MUID:91131556; PMID:1993651 !$#accession A23740 !'##molecule_type protein !'##residues 21-209,'S',211-371 ##label LEE REFERENCE S36879 !$#authors Kawasaki, N.; Yokota, Y.; Kawasaki, T. !$#journal Arch. Biochem. Biophys. (1993) 305:533-540 !$#title Differentiation of conglutination activity and sugar-binding !1activity of conglutinin after removal of NH(2)-terminal 54 !1amino acid residues by endogenous serine protease(s). !$#cross-references MUID:93384312; PMID:8373191 !$#accession S36879 !'##molecule_type protein !'##residues 21-54;75-86,'X',88-89,'X',91,'X',93-94;208-209,'X',211-227 !1##label KAW !'##experimental_source serum REFERENCE S35044 !$#authors Lu, J.; Wiedemann, H.; Holmskov, U.; Thiel, S.; Timpl, R.; !1Reid, K.B.M. !$#journal Eur. J. Biochem. (1993) 215:793-799 !$#title Structural similarity between lung surfactant protein D and !1conglutinin. Two distinct, C-type lectins containing !1collagen-like sequences. !$#cross-references MUID:93358905; PMID:8354286 !$#accession S35044 !'##molecule_type protein !'##residues 75-86,'X',88-89,'X',91,'I' ##label LUA !'##experimental_source lung REFERENCE A29416 !$#authors Young, N.M.; Leon, M.A. !$#journal Biochem. Biophys. Res. Commun. (1987) 143:645-651 !$#title The carbohydrate specificity of conglutinin and its homology !1to proteins in the hepatic lectin family. !$#cross-references MUID:87184551; PMID:3566740 !$#contents annotation REFERENCE S34054 !$#authors Malhotra, R.; Laursen, S.B.; Willis, A.C.; Sim, R.B. !$#journal Biochem. J. (1993) 293:15-19 !$#title Research Communication. Localization of the receptor-binding !1site in the collectin family of proteins. !$#cross-references MUID:93319501; PMID:8328957 !$#contents annotation REFERENCE I46010 !$#authors Liou, L.S.; Sastry, R.; Hartshorn, K.L.; Lee, Y.M.; Okarma, !1T.B.; Tauber, A.I.; Sastry, K.N. !$#journal J. Immunol. (1994) 153:173-180 !$#title Bovine conglutinin gene exon structure reveals its !1evolutionary relationship to surfactant protein-D. !$#cross-references MUID:94267222; PMID:8207234 !$#accession I46010 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-371 ##label LIO !'##cross-references EMBL:U06860; NID:g507183; PIDN:AAB60624.1; !1PID:g514256 COMMENT This protein mediates the agglutination of erythrocytes with !1antibody and complement. COMMENT This protein is a Ca2+-dependent serum lectin specific for !1N-acetylglucosamine. GENETICS !$#gene CGN1 !$#introns 67/1; 106/1; 142/1; 178/1; 217/1; 245/1 CLASSIFICATION #superfamily pulmonary surfactant protein D; C-type lectin !1homology KEYWORDS calcium binding; glycoprotein; hydroxylysine; hydroxyproline FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-371 #product conglutinin #status predicted #label MAT\ !$46-214 #region collagen-like\ !$75-371 #product conglutinin-N #status predicted #label MA2\ !$248-369 #domain C-type lectin homology #label LCH\ !$63,87,99,135,141, !$159,162,198,210 #binding_site carbohydrate (Lys) (covalent) #status !8predicted\ !$63,87,99,135,141, !$159,162,198,210 #modified_site 5-hydroxylysine (Lys) #status !8experimental\ !$78,96,108,111,129, !$132,147,153,171,195 #modified_site 4-hydroxyproline (Pro) #status !8experimental\ !$337 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 371 #molecular-weight 37994 #checksum 9074 SEQUENCE /// ENTRY LNHUB #type complete TITLE pulmonary surfactant protein B precursor [validated] - human ALTERNATE_NAMES pulmonary surfactant proteolipid SP-B; pulmonary surfactant-associated proteolipid SPL(Phe); surfactant protein 18 (SP 18) ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 08-Dec-2000 ACCESSIONS A31361; A28461; A27794; A27592; JU0162; S21134 REFERENCE A31361 !$#authors Pilot-Matias, T.J.; Kister, S.E.; Fox, J.L.; Kropp, K.; !1Glasser, S.W.; Whitsett, J.A. !$#journal DNA (1989) 8:75-86 !$#title Structure and organization of the gene encoding human !1pulmonary surfactant proteolipid SP-B. !$#cross-references MUID:89170128; PMID:2924687 !$#accession A31361 !'##molecule_type DNA !'##residues 1-381 ##label PIL !'##cross-references GB:M24461 !'##note the codon given for residue 131 (ATT) is inconsistent with the !1authors' translation !'##note this protein is encoded by a single gene REFERENCE A28461 !$#authors Jacobs, K.A.; Phelps, D.S.; Steinbrink, R.; Fisch, J.; Kriz, !1R.; Mitsock, L.; Dougherty, J.P.; Taeusch, H.W.; Floros, J. !$#journal J. Biol. Chem. (1987) 262:9808-9811 !$#title Isolation of a cDNA clone encoding a high molecular weight !1precursor to a 6-kDa pulmonary surfactant-associated !1protein. !$#cross-references MUID:87250653; PMID:3597440 !$#accession A28461 !'##molecule_type mRNA !'##residues 1-227,'A',229-381 ##label JAC !'##cross-references GB:J02761; NID:g190673; PIDN:AAA60212.1; !1PID:g190674 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE A27794 !$#authors Glasser, S.W.; Korfhagen, T.R.; Weaver, T.; Pilot-Matias, !1T.; Fox, J.L.; Whitsett, J.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:4007-4011 !$#title cDNA and deduced amino acid sequence of human pulmonary !1surfactant-associated proteolipid SPL(Phe). !$#cross-references MUID:87231940; PMID:3035561 !$#accession A27794 !'##molecule_type mRNA !'##residues 'EFR',99-317,'L',319-381 ##label GLA !'##cross-references GB:M16764; NID:g338410; PIDN:AAA88099.1; !1PID:g338411 !'##note 131-Ile was also found !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE A27592 !$#authors Revak, S.D.; Merritt, T.A.; Degryse, E.; Stefani, L.; !1Courtney, M.; Hallman, M.; Cochrane, C.G. !$#journal J. Clin. Invest. (1988) 81:826-833 !$#title Use of human surfactant low molecular weight apoproteins in !1the reconstitution of surfactant biologic activity. !$#cross-references MUID:88139786; PMID:3343343 !$#accession A27592 !'##molecule_type mRNA !'##residues 139-177,'V',179-227,'A',228-381 ##label REV !'##cross-references GB:M19097 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing !'##note the mature protein (SP 18) consists of two identical !1disulfide-bonded 9K polypeptide chains REFERENCE JU0162 !$#authors Mizumoto, M.; Adachi, H. !$#journal Sapporo Igaku Zasshi (1987) 56:731-742 !$#title Primary structure of a hydrophobic 6kDa apoprotein (SP6) of !1human pulmonary surfactant. !$#accession JU0162 !'##molecule_type protein !'##residues 201-207,'X',209-210,'X',212-227,'A',229-234,'X',236-245, !1'X',247,'L',249-253,'T',255,'L',257 ##label MIZ REFERENCE S21134 !$#authors Johansson, J.; Joernvall, H.; Curstedt, T. !$#journal FEBS Lett. (1992) 301:165-167 !$#title Human surfactant polypeptide SP-B. Disulfide bridges, !1C-terminal end, and peptide analysis of the airway form. !$#cross-references MUID:92233937; PMID:1568474 !$#accession S21134 !'##status preliminary !'##molecule_type protein !'##residues 201-227,'I',229-279 ##label JOH !'##note 228-Ala was also found COMMENT Pulmonary surfactant is a complex of phospholipids and !1proteins that lowers the surface tension at the air-liquid !1interface in the alveoli of the lung. GENETICS !$#gene GDB:SFTPB; SFTP3; SP-B !'##cross-references GDB:120374; OMIM:178640 !$#map_position 2p12-2p11.2 !$#introns 23/1; 65/3; 89/3; 131/3; 194/3; 224/3; 286/1; 334/3; 361/3 CLASSIFICATION #superfamily pulmonary surfactant protein B; saposin repeat !1homology KEYWORDS alveolar proteinosis; gaseous exchange; glycoprotein; !1lipoprotein; lung; pulmonary surfactant; respiratory !1distress syndrome FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-200 #domain propeptide #status predicted #label PRO\ !$61-153 #domain saposin repeat homology #label SAP1\ !$200-287 #domain saposin repeat homology #label SAP2\ !$201-279 #product pulmonary surfactant protein B, 9K form !8#status predicted #label SP9\ !$201-256 #product pulmonary surfactant protein B, 6K form !8#status experimental #label SP6\ !$291-376 #domain saposin repeat homology #label SAP3\ !$69-143,72-137, !$100-112,299-366, !$302-360,325-335 #disulfide_bonds #status predicted\ !$129,311 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$208-277,211-271, !$235-246 #disulfide_bonds #status experimental\ !$248 #disulfide_bonds interchain #status experimental SUMMARY #length 381 #molecular-weight 42202 #checksum 418 SEQUENCE /// ENTRY LNRBB #type complete TITLE pulmonary surfactant protein B precursor - rabbit ALTERNATE_NAMES pulmonary surfactant-associated protein-B ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Jun-1999 ACCESSIONS A32421 REFERENCE A32421 !$#authors Xu, J.; Richardson, C.; Ford, C.; Spencer, T.; Li-juan, Y.; !1Mackie, G.; Hammond, G.; Possmayer, F. !$#journal Biochem. Biophys. Res. Commun. (1989) 160:325-332 !$#title Isolation and characterization of the cDNA for pulmonary !1surfactant-associated protein-B (SP-B) in the rabbit. !$#cross-references MUID:89228033; PMID:2469419 !$#accession A32421 !'##molecule_type mRNA !'##residues 1-370 ##label XUJ !'##cross-references GB:M24901; NID:g165707; PIDN:AAA31466.1; !1PID:g165708 !'##note the authors translated the codon CCG for residue 184 as Arg and !1CAG for residue 308 as Ala COMMENT Pulmonary surfactant is a complex of phospholipids and !1proteins that lowers the surface tension at the air-liquid !1interface in the alveoli of the lung. CLASSIFICATION #superfamily pulmonary surfactant protein B; saposin repeat !1homology KEYWORDS alveolar proteinosis; gaseous exchange; glycoprotein; !1lipoprotein; lung; pulmonary surfactant; respiratory !1distress syndrome FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-184 #domain propeptide #status predicted #label PRO\ !$62-154 #domain saposin repeat homology #label SAP1\ !$184-271 #domain saposin repeat homology #label SAP2\ !$185-263 #product pulmonary surfactant protein B, 9K form !8#status predicted #label SP9\ !$185-240 #product pulmonary surfactant protein B, 6K form !8#status predicted #label SP6\ !$280-365 #domain saposin repeat homology #label SAP3\ !$300 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 370 #molecular-weight 40263 #checksum 1108 SEQUENCE /// ENTRY LNPG1 #type complete TITLE pulmonary surfactant protein 9K form - pig ALTERNATE_NAMES low molecular mass surfactant protein type 1 ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 01-Dec-1995 ACCESSIONS S00363 REFERENCE S00363 !$#authors Curstedt, T.; Johansson, J.; Barros-Soederling, J.; !1Robertson, B.; Nilsson, G.; Westberg, M.; Joernvall, H. !$#journal Eur. J. Biochem. (1988) 172:521-525 !$#title Low-molecular-mass surfactant protein type 1. The primary !1structure of a hydrophobic 8-kDa polypeptide with eight !1half-cystine residues. !$#cross-references MUID:88166729; PMID:3350011 !$#accession S00363 !'##molecule_type protein !'##residues 1-79 ##label CUR COMMENT Pulmonary surfactant protein is a phospholipid-protein !1complex, which reduces surface tension at the air-liquid !1interface of the alveoli and thus facilitates gaseous !1exchange. CLASSIFICATION #superfamily pulmonary surfactant protein B; saposin repeat !1homology KEYWORDS alveolar proteinosis; gaseous exchange; lipoprotein; lung; !1pulmonary surfactant; respiratory distress syndrome FEATURE !$1-79 #domain saposin repeat homology #label SAP SUMMARY #length 79 #molecular-weight 8714 #checksum 5695 SEQUENCE /// ENTRY SAHUP #type complete TITLE saposin precursor [validated] - human ALTERNATE_NAMES cerebroside sulfate activator protein; co-beta-glucosidase; component C activator protein; glucosylceramide activator protein A1a; proactivator protein; sphingolipid activator protein (SAP); sphingolipid activator protein A2; sulfatide sulfatase activator protein CONTAINS prosaposin; saposin A; saposin B; saposin C; saposin D ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1992 #sequence_revision 17-Nov-1995 #text_change 08-Dec-2000 ACCESSIONS JX0061; A57368; A42003; B42003; C42003; D42003; A30367; !1S34740; S36140; S36141; S36988; S36989; S36990; PS0330; !1A35985; B35985; C35985; S13196; A32784; A41240; S02289; !1S02028; S00813; S00226; I37265; I37264 REFERENCE JX0061 !$#authors Nakano, T.; Sandhoff, K.; Stuemper, J.; Christomanou, H.; !1Suzuki, K. !$#journal J. Biochem. (1989) 105:152-154 !$#title Structure of full-length cDNA coding for sulfatide !1activator, a Co-beta-glucosidase and two other homologous !1proteins: two alternate forms of the sulfatide activator. !$#cross-references MUID:89255151; PMID:2498298 !$#accession JX0061 !'##molecule_type mRNA !'##residues 1-527 ##label NAK !'##cross-references GB:D00422; NID:g220063; PIDN:BAA00321.1; !1PID:g220064 !'##note alternative splice form 1 !$#accession A57368 !'##molecule_type mRNA !'##residues 1-259,263-527 ##label NA2 !'##cross-references GB:J03015; GB:J03086; NID:g337755; PIDN:AAB59494.1; !1PID:g337756 !'##note alternative splice form 2 REFERENCE A42003 !$#authors Rorman, E.G.; Scheinker, V.; Grabowski, G.A. !$#journal Genomics (1992) 13:312-318 !$#title Structure and evolution of the human prosaposin chromosomal !1gene. !$#cross-references MUID:92307663; PMID:1612590 !$#accession A42003 !'##molecule_type DNA !'##residues 50-140 ##label ROR !'##cross-references GB:M86181 !'##note sequence extracted from NCBI backbone (NCBIN:107235, !1NCBIP:107236) !$#accession B42003 !'##molecule_type DNA !'##residues 185-259;263-276 ##label RO2 !'##note sequence extracted from NCBI backbone (NCBIN:107235, !1NCBIP:107237) !$#accession C42003 !'##molecule_type DNA !'##residues 305-393 ##label RO3 !'##note sequence extracted from NCBI backbone (NCBIN:107235, !1NCBIP:107238); sequence inconsistent with the nucleotide !1translation !$#accession D42003 !'##molecule_type DNA !'##residues 399-487 ##label RO4 !'##note sequence extracted from NCBI backbone (NCBIN:107235, !1NCBIP:107239); sequence inconsistent with the nucleotide !1translation REFERENCE A30367 !$#authors Rorman, E.G.; Grabowski, G.A. !$#journal Genomics (1989) 5:486-492 !$#title Molecular cloning of a human co-beta-glucosidase cDNA: !1evidence that four sphingolipid hydrolase activator proteins !1are encoded by single genes in humans and rats. !$#cross-references MUID:90129043; PMID:2515150 !$#accession A30367 !'##molecule_type mRNA !'##residues 1-259,263-527 ##label RO5 !'##cross-references GB:J03077; NID:g183230; PIDN:AAA52560.1; !1PID:g183231 !'##note alternative splice form 2 REFERENCE S34740 !$#authors Hiraiwa, M.; O'Brien, J.S.; Kishimoto, Y.; Galdzicka, M.; !1Fluharty, A.L.; Ginns, E.I.; Martin, B.M. !$#journal Arch. Biochem. Biophys. (1993) 304:110-116 !$#title Isolation, characterization, and proteolysis of human !1prosaposin, the precursor of saposins (sphingolipid !1activator proteins). !$#cross-references MUID:93311991; PMID:8323276 !$#accession S34740 !'##molecule_type protein !'##residues 17-24;165-172;180-189;301-305 ##label HIR REFERENCE S36140 !$#authors Tyynelae, J.; Palmer, D.N.; Baumann, M.; Haltia, M. !$#journal FEBS Lett. (1993) 330:8-12 !$#title Storage of saposins A and D in infantile neuronal !1ceroid-lipofuscinosis. !$#cross-references MUID:93380576; PMID:8370464 !$#accession S36140 !'##molecule_type protein !'##residues 'XX',62,'X',64-65,'X',67-79,'X',81-84 ##label TYY !'##note saposin A !$#accession S36141 !'##molecule_type protein !'##residues 'XXX',413-414,'X',416-428,'X',430-434 ##label TY2 !'##note saposin D REFERENCE S36988 !$#authors Holtschmidt, H.; Sandhoff, K.; Kwon, H.Y.; Harzer, K.; !1Nakano, T.; Suzuki, K. !$#journal J. Biol. Chem. (1991) 266:7556-7560 !$#title Sulfatide activator protein. Alternative splicing that !1generates three mRNAs and a newly found mutation responsible !1for a clinical disease. !$#cross-references MUID:91210267; PMID:2019586 !$#accession S36988 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type mRNA !'##residues 1-240,'S',242-527 ##label HOL !'##cross-references EMBL:M60255; NID:g337759; PIDN:AAA36594.1; !1PID:g337760 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1991 !'##note cerebroside sulfate activator protein mutant MU-9; corresponds !1to alternative splice form 1 !$#accession S36989 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type mRNA !'##residues 1-240,'S',242-259,263-527 ##label HO2 !'##cross-references EMBL:M60257; NID:g337764; PIDN:AAA36595.1; !1PID:g337765 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1991 !'##note cerebroside sulfate activator protein mutant MU-0; corresponds !1to alternative splice form 2 !$#accession S36990 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type mRNA !'##residues 1-240,'S',242-259,261-527 ##label HO3 !'##cross-references EMBL:M60258; NID:g337766; PIDN:AAA36596.1; !1PID:g337767 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1991 !'##note cerebroside sulfate activator protein mutant MU-6; corresponds !1to alternative splice form 3 REFERENCE PS0330 !$#authors Kondoh, K.; Hineno, T.; Sano, A.; Kakimoto, Y. !$#journal Biochem. Biophys. Res. Commun. (1991) 181:286-292 !$#title Isolation and characterization of prosaposin from human !1milk. !$#cross-references MUID:92068206; PMID:1958198 !$#accession PS0330 !'##molecule_type protein !'##residues 17-24,'X',26 ##label KON !'##experimental_source milk REFERENCE A35985 !$#authors Kretz, K.A.; Carson, G.S.; Morimoto, S.; Kishimoto, Y.; !1Fluharty, A.L.; O'Brien, J.S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:2541-2544 !$#title Characterization of a mutation in a family with saposin B !1deficiency: a glycosylation site defect. !$#cross-references MUID:90207231; PMID:2320574 !$#accession A35985 !'##molecule_type mRNA !'##residues 213-221 ##label KRE !'##cross-references GB:M32221 !$#accession B35985 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type mRNA !'##residues 1-259,263-527 ##label KR2 !'##cross-references GB:M32221; NID:g337761; PIDN:AAA60303.1; !1PID:g337762 !'##experimental_source lymphoblast !$#accession C35985 !'##molecule_type mRNA !'##residues 213-216,'I',218-221 ##label KR3 !'##note sequence from patients with activator-deficient metachromatic !1leukodystrophy; this mutation eliminates a glycosylation !1signal REFERENCE S13195 !$#authors Fuerst, W.; Schubert, J.; Machleidt, W.; Meyer, H.E.; !1Sandhoff, K. !$#journal Eur. J. Biochem. (1990) 192:709-714 !$#title The complete amino-acid sequences of human ganglioside GM2 !1activator protein and cerebroside sulfate activator protein. !$#cross-references MUID:91006165; PMID:2209618 !$#accession S13196 !'##molecule_type protein !'##residues 195-259,263-277 ##label FUE REFERENCE A32784 !$#authors Morimoto, S.; Martin, B.M.; Yamamoto, Y.; Kretz, K.A.; !1O'Brien, J.S.; Kishimoto, Y. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:3389-3393 !$#title Saposin A: second cerebrosidase activator protein. !$#cross-references MUID:89240739; PMID:2717620 !$#accession A32784 !'##molecule_type protein !'##residues 60-84;86-107;109-119;125-134 ##label MOR REFERENCE A41240 !$#authors O'Brien, J.S.; Kretz, K.A.; Dewji, N.; Wenger, D.A.; Esch, !1F.; Fluharty, A.L. !$#journal Science (1988) 241:1098-1101 !$#title Coding of two sphingolipid activator proteins (SAP-1 and !1SAP-2) by same genetic locus. !$#cross-references MUID:88321660; PMID:2842863 !$#accession A41240 !'##molecule_type mRNA !'##residues 'GSSR',18-259,263-299,'D',301-302,'D',304-527 ##label OAB !'##cross-references GB:J03086 REFERENCE S02289 !$#authors Dewji, N.N.; Wenger, D.A.; O'Brien, J.S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:8652-8656 !$#title Nucleotide sequence of cloned cDNA for human sphingolipid !1activator protein 1 precursor. !$#cross-references MUID:88068647; PMID:2825202 !$#accession S02289 !'##status significant sequence differences !'##molecule_type mRNA !'##cross-references EMBL:J03015 !'##note this sequence corrected by A41240 !'##note part of this sequence, including the amino end of the mature !1protein, was determined by protein sequencing REFERENCE S02028 !$#authors Kleinschmidt, T.; Christomanou, H.; Braunitzer, G. !$#journal Biol. Chem. Hoppe-Seyler (1988) 369:1361-1365 !$#title Complete amino-acid sequence of the naturally occurring A(2) !1activator protein for enzymic sphingomyelin degradation: !1identity to the sulfatide activator protein (SAP-1). !$#cross-references MUID:89207118; PMID:3242555 !$#accession S02028 !'##molecule_type protein !'##residues 195-259,263-276 ##label KLE REFERENCE S00813 !$#authors Fuerst, W.; Machleidt, W.; Sandhoff, K. !$#journal Biol. Chem. Hoppe-Seyler (1988) 369:317-328 !$#title The precursor of sulfatide activator protein is processed to !1three different proteins. !$#cross-references MUID:89000190; PMID:3048308 !$#accession S00813 !'##molecule_type protein !'##residues 410-487 ##label FU2 REFERENCE S00226 !$#authors Kleinschmidt, T.; Christomanou, H.; Braunitzer, G. !$#journal Biol. Chem. Hoppe-Seyler (1987) 368:1571-1578 !$#title Complete amino-acid sequence and carbohydrate content of the !1naturally occurring glucosylceramide activator protein (A1 !1activator) absent from a new human Gaucher disease variant. !$#cross-references MUID:88163077; PMID:3442600 !$#accession S00226 !'##molecule_type protein !'##residues 314-393 ##label KL2 REFERENCE A57297 !$#authors Vaccaro, A.M.; Salvioli, R.; Barca, A.; Tatti, M.; Ciaffoni, !1F.; Maras, B.; Siciliano, R.; Zappacosta, F.; Amoresano, A.; !1Pucci, P. !$#journal J. Biol. Chem. (1995) 270:9953-9960 !$#title Structural analysis of saposin C and B. Complete !1localization of disulfide bridges. !$#cross-references MUID:95247790; PMID:7730378 !$#contents annotation; disulfide bonds; glycosylation REFERENCE I37264 !$#authors Holtschmidt, H.; Sandhoff, K.; Fuerst, W.; Kwon, H.Y.; !1Schnabel, D.; Suzuki, K. !$#journal FEBS Lett. (1991) 280:267-270 !$#title The organization of the gene for the human cerebroside !1sulfate activator protein. !$#cross-references MUID:91192146; PMID:2013321 !$#accession I37265 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 59-125 ##label RES !'##cross-references EMBL:X57107; NID:g30234; PIDN:CAA40391.1; !1PID:g30235 !$#accession I37264 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 307-516 ##label RE2 !'##cross-references EMBL:X57108; NID:g30232; PIDN:CAA40392.1; !1PID:g1565257 !'##note sequence revised relative to PID:g30233 (corrected coding !1region) GENETICS !$#gene GDB:PSAP; GLBA !'##cross-references GDB:120366; OMIM:176801 !$#map_position 10q22.1-10q22.1 !$#introns 83/3; 338/3; 401/1; 453/3; 480/3 !$#note defects in this gene may cause variant Gaucher disease, !1variant Tay-Sachs disease, variant metachromatic !1leukodystrophy or infantile neuronal ceroid-lipofuscinosis !$#note list of introns is incomplete FUNCTION !$#description saposins bind sphingolipids, form hydrophilic complexes and !1make them accessible to sphingolipid hydrolases !$#pathway sphingolipid catabolism !$#note saposins A and C (SAP-2) activate hydrolysis of !1glucocerebroside by beta-glucosylceramidase and of !1galactocerebroside by galactosylceramidase !$#note saposin B (SAP-1) activates hydrolysis of galactocerebroside !1sulfate by arylsulfatase A, of globotriaosylceramide by !1alpha-galactosidase and of GM1 ganglioside by acid !1beta-galactosidase !$#note saposin D activates hydrolysis of sphingomyelin by !1sphingomyelin phosphodiesterase CLASSIFICATION #superfamily saposin; saposin repeat homology KEYWORDS alternative splicing; glycoprotein; lysosomal storage !1disease; lysosome; sphingolipid metabolism FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-527 #product prosaposin #status predicted #label PRO\ !$55-148 #domain saposin repeat homology #label SAP1\ !$60-143 #product saposin A #status experimental #label SAPA\ !$190-284 #domain saposin repeat homology #label SAP2\ !$195-277 #product saposin B, splice form 1 #status predicted !8#label SAB1\ !$195-259,263-277 #product saposin B, splice form 2 #status !8experimental #label SAB2\ !$195-259,261-277 #product saposin B, splice form 3 #status predicted !8#label SAB3\ !$310-401 #domain saposin repeat homology #label SAP3\ !$314-393 #product saposin C #status experimental #label SAPC\ !$404-495 #domain saposin repeat homology #label SAP4\ !$410-487 #product saposin D #status predicted #label SAPD\ !$63-138,66-132, !$94-106,412-485, !$415-479,443-454 #disulfide_bonds #status predicted\ !$80,101,215,335 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$198-274,201-268, !$230-241,318-391, !$321-385,349-360 #disulfide_bonds #status experimental\ !$429 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 527 #molecular-weight 58483 #checksum 8542 SEQUENCE /// ENTRY A28716 #type complete TITLE saposin precursor - rat ALTERNATE_NAMES cerebroside sulfate activator protein; co-beta-glucosidase; component C activator protein; glucosylceramide activator protein A1a; proactivator protein; sphingolipid activator protein (SAP); sphingolipid activator protein A2; sulfated glycoprotein 1; sulfatide sulfatase activator protein CONTAINS prosaposin; saposin A; saposin B; saposin C; saposin D ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A28716 REFERENCE A28716 !$#authors Collard, M.W.; Sylvester, S.R.; Tsuruta, J.K.; Griswold, !1M.D. !$#journal Biochemistry (1988) 27:4557-4564 !$#title Biosynthesis and molecular cloning of sulfated glycoprotein !11 secreted by rat sertoli cells: sequence similarity with !1the 70-kilodalton precursor to sulfatide/G-m1 activator. !$#cross-references MUID:89000647; PMID:3048385 !$#accession A28716 !'##molecule_type mRNA !'##residues 1-554 ##label COL !'##cross-references GB:M19936; NID:g206904; PIDN:AAA42136.1; !1PID:g206905 !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing FUNCTION !$#description saposins bind sphingolipids, form hydrophilic complexes and !1make them accessible to sphingolipid hydrolases !$#pathway sphingolipid catabolism !$#note saposins A and C (SAP-2) activate hydrolysis of !1glucocerebroside by beta-glucosylceramidase and of !1galactocerebroside by galactosylceramidase !$#note saposin B (SAP-1) activates hydrolysis of galactocerebroside !1sulfate by arylsulfatase A, of globotriaosylceramide by !1alpha-galactosidase and of GM1 ganglioside by acid !1beta-galactosidase !$#note saposin D activates hydrolysis of sphingomyelin by !1sphingomyelin phosphodiesterase CLASSIFICATION #superfamily saposin; saposin repeat homology KEYWORDS alternative splicing; glycoprotein; lysosomal storage !1disease; lysosome; sphingolipid metabolism FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-554 #product prosaposin #status predicted #label PRO\ !$55-148 #domain saposin repeat homology #label SAP1\ !$60-143 #product saposin A #status predicted #label SAPA\ !$189-280 #domain saposin repeat homology #label SAP2\ !$194-273 #product saposin B #status predicted #label SAB1\ !$306-397 #domain saposin repeat homology #label SAP3\ !$310-389 #product saposin C #status predicted #label SAPC\ !$431-522 #domain saposin repeat homology #label SAP4\ !$437-514 #product saposin D #status predicted #label SAPD\ !$63-138,66-132, !$94-106,439-512, !$442-506,470-481 #disulfide_bonds #status predicted\ !$80,214,331,456 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$197-270,200-264, !$229-240,314-387, !$317-381,345-356 #disulfide_bonds #status predicted SUMMARY #length 554 #molecular-weight 61123 #checksum 2440 SEQUENCE /// ENTRY JH0604 #type complete TITLE saposin precursor - mouse ALTERNATE_NAMES cerebroside sulfate activator protein; co-beta-glucosidase; component C activator protein; glucosylceramide activator protein A1a; proactivator protein; sphingolipid activator protein (SAP); sphingolipid activator protein A2; sulfated glycoprotein 1; sulfatide sulfatase activator protein CONTAINS prosaposin; saposin A; saposin B; saposin C; saposin D ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JH0604 REFERENCE JH0604 !$#authors Tsuda, M.; Sakiyama, T.; Endo, H.; Kitagawa, T. !$#journal Biochem. Biophys. Res. Commun. (1992) 184:1266-1272 !$#title The primary structure of mouse saposin. !$#cross-references MUID:92272718; PMID:1590788 !$#accession JH0604 !'##molecule_type mRNA !'##residues 1-557 ##label TSU !'##cross-references GB:S36200; NID:g249386; PIDN:AAB22175.1; !1PID:g249387 !'##experimental_source liver FUNCTION !$#description saposins bind sphingolipids, form hydrophilic complexes and !1make them accessible to sphingolipid hydrolases !$#pathway sphingolipid catabolism !$#note saposins A and C (SAP-2) activate hydrolysis of !1glucocerebroside by beta-glucosylceramidase and of !1galactocerebroside by galactosylceramidase !$#note saposin B (SAP-1) activates hydrolysis of galactocerebroside !1sulfate by arylsulfatase A, of globotriaosylceramide by !1alpha-galactosidase and of GM1 ganglioside by acid !1beta-galactosidase !$#note saposin D activates hydrolysis of sphingomyelin by !1sphingomyelin phosphodiesterase CLASSIFICATION #superfamily saposin; saposin repeat homology KEYWORDS alternative splicing; glycoprotein; lysosomal storage !1disease; lysosome; sphingolipid metabolism FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-557 #product prosaposin #status predicted #label PRO\ !$55-148 #domain saposin repeat homology #label SAP1\ !$60-143 #product saposin A #status predicted #label SAPA\ !$189-283 #domain saposin repeat homology #label SAP2\ !$194-276 #product saposin B #status predicted #label SAB1\ !$309-400 #domain saposin repeat homology #label SAP3\ !$313-392 #product saposin C #status predicted #label SAPC\ !$434-525 #domain saposin repeat homology #label SAP4\ !$440-517 #product saposin D #status predicted #label SAPD\ !$63-138,66-132, !$94-106,197-273, !$200-267,229-240, !$317-390,320-384, !$348-359,442-515, !$445-509,473-484 #disulfide_bonds #status predicted\ !$80,214,334,379,459 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 557 #molecular-weight 61394 #checksum 7846 SEQUENCE /// ENTRY LNHUC #type complete TITLE pulmonary surfactant protein C precursor, long splice form [validated] - human ALTERNATE_NAMES 3.7 kDa surfactant polypeptide; pulmonary surfactant protein SP5; pulmonary surfactant proteolipid SP-C; pulmonary surfactant proteolipid SPL(pVal) CONTAINS pulmonary surfactant protein C precursor, short splice form ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 08-Dec-2000 ACCESSIONS A28801; B28801; I38420; A27338; S02315; S00608; A61249 REFERENCE A28801 !$#authors Glasser, S.W.; Korfhagen, T.R.; Perme, C.M.; Pilot-Matias, !1T.J.; Kister, S.E.; Whitsett, J.A. !$#journal J. Biol. Chem. (1988) 263:10326-10331 !$#title Two SP-C genes encoding human pulmonary surfactant !1proteolipid. !$#cross-references MUID:88273133; PMID:2839484 !$#accession A28801 !'##molecule_type DNA !'##residues 1-137,'T',139-197 ##label GLA1 !'##cross-references GB:J03890; NID:g190089; PIDN:AAC32022.1; !1PID:g387029 !'##experimental_source long splice form !'##note the codon given for residue 138 (ATT) is inconsistent with the !1authors' translation, and the sequence submitted to GenBank !1which has 138-Thr (ACT) !$#accession B28801 !'##molecule_type DNA !'##residues 1-137,'T',139-145,152-197 ##label GLA2 !'##cross-references GB:J03890; NID:g190089; PIDN:AAC32023.1; !1PID:g387030 !'##experimental_source short splice form !'##note the codon given for residue 138 (ATT) is inconsistent with the !1authors' translation, and the sequence submitted to GenBank !1which has 138-Thr (ACT) !'##note identical proteins are encoded by two genes; transcripts from !1either gene can be alternatively spliced REFERENCE I38420 !$#authors Hatzis, D.; Deiter, G.; deMello, D.E.; Floros, J. !$#journal Exp. Lung Res. (1994) 20:57-72 !$#title Human surfactant protein-C: genetic homogeneity and !1expression in RDS; comparison with other species. !$#cross-references MUID:94237133; PMID:8181452 !$#accession I38420 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-14,'PCQ',15-44,'S',46-64,'FPQ',68-137,'T',139-185,'S', !1187-197 ##label HAT !'##cross-references EMBL:U02948; NID:g498319; PIDN:AAB60332.1; !1PID:g514214 !'##note there are probably errors in the presentation of the CDS splice !1boundaries in the entry prepared by NCBI REFERENCE A27338 !$#authors Glasser, S.W.; Korfhagen, T.R.; Weaver, T.E.; Clark, J.C.; !1Pilot-Matias, T.; Meuth, J.; Fox, J.L.; Whitsett, J.A. !$#journal J. Biol. Chem. (1988) 263:9-12 !$#title cDNA, deduced polypeptide structure and chromosomal !1assignment of human pulmonary surfactant proteolipid, SPL !1(pVal). !$#cross-references MUID:88087156; PMID:3335510 !$#accession A27338 !'##molecule_type mRNA !'##residues 1-197 ##label GLA3 !'##cross-references GB:J03517; NID:g338412; PIDN:AAA36634.1; !1PID:g338413 !'##note part of this sequence, including the amino end of the mature !1protein, was determined by protein sequencing; mature forms !1beginning at residues 24 and 26 were detected REFERENCE S02315 !$#authors Warr, R.G.; Hawgood, S.; Buckley, D.I.; Crisp, T.M.; !1Schilling, J.; Benson, B.J.; Ballard, P.L.; Clements, J.A.; !1White, R.T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:7915-7919 !$#title Low molecular weight human pulmonary surfactant protein !1(SP5): isolation, characterization, and cDNA and amino acid !1sequences. !$#cross-references MUID:88068508; PMID:3479771 !$#accession S02315 !'##molecule_type mRNA !'##residues 1-197 ##label WAR !'##cross-references GB:J03553; NID:g338306; PIDN:AAA36631.1; !1PID:g338307 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing !'##note 138-Thr and 186-Ser were also found REFERENCE S00608 !$#authors Johansson, J.; Joernvall, H.; Eklund, A.; Christensen, N.; !1Robertson, B.; Curstedt, T. !$#journal FEBS Lett. (1988) 232:61-64 !$#title Hydrophobic 3.7 kDa surfactant polypeptide: structural !1characterization of the human and bovine forms. !$#cross-references MUID:88211876; PMID:3366248 !$#accession S00608 !'##molecule_type protein !'##residues 24-58 ##label JOH !'##note 25-Arg was also found !'##note peptides beginning at residues 24, 25, and 26 were detected REFERENCE A61249 !$#authors Stults, J.T.; Griffin, P.R.; Lesikar, D.D.; Naidu, A.; !1Moffat, B.; Benson, B.J. !$#journal Am. J. Physiol. (1991) 261:L118-L125 !$#title Lung surfactant protein SP-C from human, bovine, and canine !1sources contains palmityl cysteine thioester linkages. !$#cross-references MUID:91336436; PMID:1872406 !$#accession A61249 !'##molecule_type protein !'##residues 24-58 ##label STU !'##note identification of palmitoyl cysteines COMMENT Pulmonary surfactant is a complex of phospholipids and !1proteins that lowers the surface tension at the air-liquid !1interface in the alveoli of the lung. COMMENT This protein is synthesized by alveolar type II cells. COMMENT The precursor of the hydrophobic proteolipid protein C lacks !1a typical signal sequence. GENETICS !$#gene GDB:SFTPC; SFTP2; SP-C !'##cross-references GDB:120373; OMIM:178620 !$#map_position 8p21-8p21 !$#introns 14/3; 67/3; 108/3; 145/3 !$#note the first intron occurs before the initiator codon CLASSIFICATION #superfamily pulmonary surfactant protein C KEYWORDS alternative splicing; gaseous exchange; lipoprotein; lung; !1pulmonary surfactant; respiratory distress syndrome; !1thiolester bond FEATURE !$1-197 #product pulmonary surfactant protein C precursor, !8short splice form #status predicted #label LSF\ !$1-145,152-197 #product pulmonary surfactant protein C precursor, !8short splice form #status predicted #label SSF\ !$1-23 #domain propeptide #status predicted #label PRO\ !$24-58 #product pulmonary surfactant protein C #status !8experimental #label MAT\ !$28,29 #binding_site palmitate (Cys) (covalent) #status !8experimental SUMMARY #length 197 #molecular-weight 21053 #checksum 8032 SEQUENCE /// ENTRY LNRTC #type complete TITLE pulmonary surfactant protein C precursor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 18-Feb-2000 ACCESSIONS S03994 REFERENCE S03994 !$#authors Fisher, J.H.; Shannon, J.M.; Hofmann, T.; Mason, R.J. !$#journal Biochim. Biophys. Acta (1989) 995:225-230 !$#title Nucleotide and deduced amino acid sequence of the !1hydrophobic surfactant protein SP-C from rat: expression in !1alveolar type II cells and homology with SP-C from other !1species. !$#cross-references MUID:89207572; PMID:2706272 !$#accession S03994 !'##molecule_type mRNA !'##residues 1-194 ##label FIS !'##cross-references GB:X14221; NID:g57286; PIDN:CAA32440.1; PID:g57287 COMMENT Pulmonary surfactant is a complex of phospholipids and !1proteins that lowers the surface tension at the air-liquid !1interface in the alveoli of the lung. COMMENT This protein is synthesized by alveolar type II cells. COMMENT The precursor of the hydrophobic proteolipid protein C lacks !1a typical signal sequence. CLASSIFICATION #superfamily pulmonary surfactant protein C KEYWORDS gaseous exchange; lipoprotein; lung; pulmonary surfactant; !1thiolester bond FEATURE !$1-23 #domain propeptide #status predicted #label PRO\ !$24-58 #product pulmonary surfactant protein C #status !8predicted #label MAT\ !$28,29 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 194 #molecular-weight 21042 #checksum 4507 SEQUENCE /// ENTRY A36534 #type complete TITLE pulmonary surfactant protein C precursor - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 12-Apr-1991 #sequence_revision 25-Apr-1997 #text_change 18-Feb-2000 ACCESSIONS A36534 REFERENCE A36534 !$#authors Glasser, S.W.; Korfhagen, T.R.; Bruno, M.D.; Dey, C.; !1Whitsett, J.A. !$#journal J. Biol. Chem. (1990) 265:21986-21991 !$#title Structure and expression of the pulmonary surfactant protein !1SP-C gene in the mouse. !$#cross-references MUID:91072410; PMID:2254341 !$#accession A36534 !'##molecule_type DNA !'##residues 1-193 ##label GLA !'##cross-references GB:M38314; NID:g200559; PIDN:AAA40010.1; !1PID:g200560 COMMENT Pulmonary surfactant is a complex of phospholipids and !1proteins that lowers the surface tension at the air-liquid !1interface in the alveoli of the lung. COMMENT This protein is synthesized by alveolar type II cells. COMMENT The precursor of the hydrophobic proteolipid protein C lacks !1a typical signal sequence. CLASSIFICATION #superfamily pulmonary surfactant protein C KEYWORDS gaseous exchange; lipoprotein; lung; pulmonary surfactant; !1thiolester bond FEATURE !$1-23 #domain propeptide #status predicted #label PRO\ !$24-58 #product pulmonary surfactant protein C #status !8predicted #label MAT\ !$28,29 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 193 #molecular-weight 21054 #checksum 2852 SEQUENCE /// ENTRY LNPGC1 #type complete TITLE pulmonary surfactant protein C [validated] - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 30-Sep-1989 #sequence_revision 25-Apr-1997 #text_change 15-Sep-2000 ACCESSIONS A28640 REFERENCE A28640 !$#authors Johansson, J.; Curstedt, T.; Robertson, B.; Joernvall, H. !$#journal Biochemistry (1988) 27:3544-3547 !$#title Size and structure of the hydrophobic low molecular weight !1surfactant-associated polypeptide. !$#cross-references MUID:88309749; PMID:3408709 !$#accession A28640 !'##molecule_type protein !'##residues 1-35 ##label JOH REFERENCE A52839 !$#authors Johansson, J.; Szyperski, T.; Curstedt, T.; Wuthrich, K. !$#submission submitted to the Brookhaven Protein Data Bank, September !11994 !$#cross-references PDB:1SPF !$#contents annotation; conformation by (1)H-NMR, residues 1-35 REFERENCE A58575 !$#authors Johansson, J.; Szyperski, T.; Curstedt, T.; Wuthrich, K. !$#journal Biochemistry (1994) 33:6015-6023 !$#title The NMR structure of the pulmonary surfactant-associated !1polypeptide sp-C in an apolar solvent contains a valyl-rich !1alpha-helix. !$#cross-references MUID:94235672; PMID:8180229 !$#contents annotation; conformation by (1)H-NMR COMMENT Pulmonary surfactant is a complex of phospholipids and !1proteins that lowers the surface tension at the air-liquid !1interface in the alveoli of the lung. COMMENT This protein is synthesized by alveolar type II cells. COMMENT The precursor of the hydrophobic proteolipid protein C lacks !1a typical signal sequence. CLASSIFICATION #superfamily pulmonary surfactant protein C KEYWORDS gaseous exchange; lipoprotein; lung; pulmonary surfactant; !1thiolester bond FEATURE !$5,6 #binding_site palmitate (Cys) (covalent) #status !8experimental SUMMARY #length 35 #molecular-weight 3710 #checksum 9814 SEQUENCE /// ENTRY LNDGC1 #type complete TITLE pulmonary surfactant protein C - dog ORGANISM #formal_name Canis lupus familiaris #common_name dog DATE 12-May-1994 #sequence_revision 25-Apr-1997 #text_change 25-Apr-1997 ACCESSIONS B61249; S14813 REFERENCE A61249 !$#authors Stults, J.T.; Griffin, P.R.; Lesikar, D.D.; Naidu, A.; !1Moffat, B.; Benson, B.J. !$#journal Am. J. Physiol. (1991) 261:L118-L125 !$#title Lung surfactant protein SP-C from human, bovine, and canine !1sources contains palmityl cysteine thioester linkages. !$#cross-references MUID:91336436; PMID:1872406 !$#accession B61249 !'##molecule_type protein !'##residues 1-35 ##label STU REFERENCE S14813 !$#authors Johansson, J.; Persson, P.; Loewenadler, B.; Robertson, B.; !1Joernvall, H.; Curstedt, T. !$#journal FEBS Lett. (1991) 281:119-122 !$#title Canine hydrophobic surfactant polypeptide SP-C. A !1lipopeptide with one thioester-linked palmitoyl group. !$#cross-references MUID:91200266; PMID:2015882 !$#accession S14813 !'##molecule_type protein !'##residues 2-35 ##label JOH COMMENT Pulmonary surfactant is a complex of phospholipids and !1proteins that lowers the surface tension at the air-liquid !1interface in the alveoli of the lung. COMMENT This protein is synthesized by alveolar type II cells. COMMENT The precursor of the hydrophobic proteolipid protein C lacks !1a typical signal sequence. CLASSIFICATION #superfamily pulmonary surfactant protein C KEYWORDS gaseous exchange; lipoprotein; lung; pulmonary surfactant; !1thiolester bond FEATURE !$5 #binding_site palmitate (Cys) (covalent) #status !8experimental SUMMARY #length 35 #molecular-weight 3658 #checksum 9168 SEQUENCE /// ENTRY LNRBC1 #type complete TITLE pulmonary surfactant protein C precursor - rabbit ALTERNATE_NAMES surfactant-associated protein SP-C ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 01-Sep-1995 #sequence_revision 25-Apr-1997 #text_change 18-Feb-2000 ACCESSIONS A56766; S14815; A56860; S19946; A56655 REFERENCE A56766 !$#authors Boggaram, V.; Margana, R.K. !$#journal Am. J. Physiol. (1992) 263:L634-L644 !$#title Rabbit surfactant protein C: cDNA cloning and regulation of !1alternatively spliced surfactant protein C mRNAs. !$#cross-references MUID:93118799; PMID:1335697 !$#accession A56766 !'##molecule_type mRNA !'##residues 1-189 ##label BOG !'##cross-references GB:S51983; NID:g262767; PIDN:AAB24761.1; !1PID:g262768; GB:S51597; NID:g262769; PID:g262770 !'##experimental_source lung !'##note sequence extracted from NCBI backbone (NCBIN:121728, !1NCBIP:121729) !'##note two types of mRNA were found differing in their 3'-untranslated !1regions because of alternative splicing REFERENCE S14813 !$#authors Johansson, J.; Persson, P.; Loewenadler, B.; Robertson, B.; !1Joernvall, H.; Curstedt, T. !$#journal FEBS Lett. (1991) 281:119-122 !$#title Canine hydrophobic surfactant polypeptide SP-C. A !1lipopeptide with one thioester-linked palmitoyl group. !$#cross-references MUID:91200266; PMID:2015882 !$#accession S14815 !'##molecule_type protein !'##residues 24-37,'XXXXXXXXXXXXXXXXXXXXX' ##label JOH REFERENCE A56860 !$#authors Connelly, I.; Possmayer, F. !$#journal Biochim. Biophys. Acta (1992) 1127:199-207 !$#title cDNA sequence and alternative mRNA splicing of !1surfactant-associated protein C (SP-C) in rabbit lung. !$#cross-references MUID:92353123; PMID:1643107 !$#accession A56860 !'##molecule_type mRNA !'##residues 24-58 ##label CON !'##cross-references EMBL:X65078; NID:g1720; PIDN:CAA46204.1; PID:g1721 !'##experimental_source fetal lung !'##note sequence extracted from NCBI backbone (NCBIN:110198, !1NCBIP:110234); the complete sequence is not shown REFERENCE S19946 !$#authors Connelly, I.; Possmayer, F. !$#submission submitted to the EMBL Data Library, March 1992 !$#description cDNA sequence and alternative splicing of !1surfactant-associated protein C (SP-C) in rabbit lung. !$#accession S19946 !'##molecule_type mRNA !'##residues 3-115,117-161,'R',163-189 ##label CO2 !'##cross-references EMBL:X65078; NID:g1720; PIDN:CAA46204.1; PID:g1721 REFERENCE A56655 !$#authors Durham, P.L.; Nanthakumar, E.J.; Snyder, J.M. !$#journal Exp. Lung Res. (1992) 18:775-793 !$#title Developmental regulation of surfactant-associated proteins !1in rabbit fetal lung in vivo. !$#cross-references MUID:93105936; PMID:1468410 !$#accession A56655 !'##status preliminary !'##molecule_type mRNA !'##residues 24-115,117-186,'Y',188-189 ##label DUR !'##cross-references GB:S51098; NID:g262066; PIDN:AAB24576.1; !1PID:g262067 !'##experimental_source fetal lung !'##note sequence extracted from NCBI backbone (NCBIN:121095, !1NCBIP:121096); sequence inconsistent with nucleotide !1translation COMMENT Pulmonary surfactant is a complex of phospholipids and !1proteins that lowers the surface tension at the air-liquid !1interface in the alveoli of the lung. COMMENT This protein is synthesized by alveolar type II cells. COMMENT The precursor of the hydrophobic proteolipid protein C lacks !1a typical signal sequence. CLASSIFICATION #superfamily pulmonary surfactant protein C KEYWORDS gaseous exchange; lipoprotein; lung; pulmonary surfactant; !1thiolester bond FEATURE !$1-23 #domain propeptide #status predicted #label PRO\ !$24-58 #product pulmonary surfactant protein C #status !8experimental #label MAT\ !$28,29 #binding_site palmitate (Cys) (covalent) #status !8experimental SUMMARY #length 189 #molecular-weight 19933 #checksum 1538 SEQUENCE /// ENTRY LNBOC1 #type complete TITLE pulmonary surfactant protein C - bovine ALTERNATE_NAMES pulmonary surfactant protein PSP-6 ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Jun-1989 #sequence_revision 25-Apr-1997 #text_change 25-Apr-1997 ACCESSIONS S00609; C61249; S02353; S02318; B29667; S14814 REFERENCE S00608 !$#authors Johansson, J.; Joernvall, H.; Eklund, A.; Christensen, N.; !1Robertson, B.; Curstedt, T. !$#journal FEBS Lett. (1988) 232:61-64 !$#title Hydrophobic 3.7 kDa surfactant polypeptide: structural !1characterization of the human and bovine forms. !$#cross-references MUID:88211876; PMID:3366248 !$#accession S00609 !'##molecule_type protein !'##residues 1-34 ##label JOH REFERENCE A61249 !$#authors Stults, J.T.; Griffin, P.R.; Lesikar, D.D.; Naidu, A.; !1Moffat, B.; Benson, B.J. !$#journal Am. J. Physiol. (1991) 261:L118-L125 !$#title Lung surfactant protein SP-C from human, bovine, and canine !1sources contains palmityl cysteine thioester linkages. !$#cross-references MUID:91336436; PMID:1872406 !$#accession C61249 !'##molecule_type protein !'##residues 1-34 ##label STU !'##note identification of palmitoyl cysteines REFERENCE S02317 !$#authors Yu, S.H.; Chung, W.; Olafson, R.W.; Harding, P.G.R.; !1Possmayer, F. !$#journal Biochim. Biophys. Acta (1987) 921:437-448 !$#title Characterization of the small hydrophobic proteins !1associated with pulmonary surfactant. !$#cross-references MUID:88025156; PMID:3663690 !$#accession S02353 !'##molecule_type protein !'##residues 1-10 ##label YU1 REFERENCE S02318 !$#authors Phelps, D.S.; Smith, L.M.; Taeusch, H.W. !$#journal Am. Rev. Respir. Dis. (1987) 135:1112-1117 !$#title Characterization and partial amino acid sequence of a low !1molecular weight surfactant protein. !$#cross-references MUID:87211387; PMID:3579010 !$#accession S02318 !'##molecule_type protein !'##residues 1-3,'XI',6-10,'L',12-15,'X',17-21,'I' ##label PHE REFERENCE A90137 !$#authors Olafson, R.W.; Rink, U.; Kielland, S.; Yu, S.H.; Chung, J.; !1Harding, P.G.R.; Possmayer, F. !$#journal Biochem. Biophys. Res. Commun. (1987) 148:1406-1411 !$#title Protein sequence analysis studies on the low molecular !1weight hydrophobic proteins associated with bovine pulmonary !1surfactant. !$#cross-references MUID:88077030; PMID:3689402 !$#accession B29667 !'##molecule_type protein !'##residues 1-20,'V',22-25,'V',27,'IGAMLAM' ##label OLA REFERENCE S14813 !$#authors Johansson, J.; Persson, P.; Loewenadler, B.; Robertson, B.; !1Joernvall, H.; Curstedt, T. !$#journal FEBS Lett. (1991) 281:119-122 !$#title Canine hydrophobic surfactant polypeptide SP-C. A !1lipopeptide with one thioester-linked palmitoyl group. !$#cross-references MUID:91200266; PMID:2015882 !$#contents annotation COMMENT Pulmonary surfactant is a complex of phospholipids and !1proteins that lowers the surface tension at the air-liquid !1interface in the alveoli of the lung. COMMENT This protein is synthesized by alveolar type II cells. COMMENT The precursor of the hydrophobic proteolipid protein C lacks !1a typical signal sequence. CLASSIFICATION #superfamily pulmonary surfactant protein C KEYWORDS gaseous exchange; lipoprotein; lung; pulmonary surfactant; !1thiolester bond FEATURE !$4,5 #binding_site palmitate (Cys) (covalent) #status !8experimental SUMMARY #length 34 #molecular-weight 3582 #checksum 6612 SEQUENCE /// ENTRY ACMSIT #type complete TITLE inositol 1,4,5-trisphosphate receptor - mouse ALTERNATE_NAMES inositol-1,4,5-triphosphate-binding protein P400; membrane-associated glycoprotein P400 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 22-Jun-1999 ACCESSIONS S04844; S06796; C34955 REFERENCE S04844 !$#authors Furuichi, T.; Yoshikawa, S.; Mikoshiba, K. !$#journal Nucleic Acids Res. (1989) 17:5385-5386 !$#title Nucleotide sequence of cDNA encoding P400 protein in the !1mouse cerebellum. !$#cross-references MUID:89345101; PMID:2762133 !$#accession S04844 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-2749 ##label FUR !'##cross-references EMBL:X15373; NID:g53568; PIDN:CAA33433.1; !1PID:g53569 !'##experimental_source strain ICR; cerebellum REFERENCE S06796 !$#authors Furuichi, T.; Yoshikawa, S.; Miyawaki, A.; Wada, K.; Maeda, !1N.; Mikoshiba, K. !$#journal Nature (1989) 342:32-38 !$#title Primary structure and functional expression of the inositol !11,4,5-trisphosphate-binding protein P(400). !$#cross-references MUID:90044039; PMID:2554142 !$#accession S06796 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-2749 ##label FU2 !'##cross-references EMBL:X15373; NID:g53568; PIDN:CAA33433.1; !1PID:g53569 !'##experimental_source strain ICR; cerebellum REFERENCE A92975 !$#authors Nordquist, D.T.; Kozak, C.A.; Orr, H.T. !$#journal J. Neurosci. (1988) 8:4780-4789 !$#title cDNA cloning and characterization of three genes uniquely !1expressed in cerebellum by Purkinje neurons. !$#cross-references MUID:89068131; PMID:3199205 !$#accession C34955 !'##molecule_type mRNA !'##residues 2250-2674,'P',2676-2749 ##label NOR CLASSIFICATION #superfamily inositol-trisphosphate receptor KEYWORDS glycoprotein; phosphoprotein; receptor; transmembrane !1protein FEATURE !$890-907 #domain transmembrane #status predicted #label TM1\ !$1960-1976 #domain transmembrane #status predicted #label TM2\ !$2276-2294 #domain transmembrane #status predicted #label TM3\ !$2308-2326 #domain transmembrane #status predicted #label TM4\ !$2334-2350 #domain transmembrane #status predicted #label TM5\ !$2352-2372 #domain transmembrane #status predicted #label TM6\ !$2391-2407 #domain transmembrane #status predicted #label TM7\ !$2440-2462 #domain transmembrane #status predicted #label TM8\ !$2570-2589 #domain transmembrane #status predicted #label TM9\ !$1588,1755 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$2475,2503,2622,2710 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 2749 #molecular-weight 313195 #checksum 2330 SEQUENCE /// ENTRY A56539 #type complete TITLE giantin - human ALTERNATE_NAMES macrogolgin ORGANISM #formal_name Homo sapiens #common_name man DATE 19-Oct-1995 #sequence_revision 26-Jan-1996 #text_change 10-Dec-1999 ACCESSIONS A56539; S37536 REFERENCE A56539 !$#authors Seelig, H.P.; Schranz, P.; Schroeter, H.; Wiemann, C.; !1Griffiths, G.; Renz, M. !$#journal Mol. Cell. Biol. (1994) 14:2564-2576 !$#title Molecular genetic analyses of a 376-kilodalton Golgi complex !1membrane protein (giantin). !$#cross-references MUID:94187728; PMID:7511208 !$#accession A56539 !'##molecule_type mRNA !'##residues 1-3259 ##label SEE !'##cross-references EMBL:X75304; NID:g405714; PIDN:CAA53052.1; !1PID:g405715 GENETICS !$#gene GDB:GOLGB1; GCP; GCP371 !'##cross-references GDB:454958 !$#map_position 3q13.31-3q13.31 CLASSIFICATION #superfamily giantin KEYWORDS coiled coil; Golgi apparatus; transmembrane protein FEATURE !$3238-3254 #domain transmembrane #status predicted #label TMN SUMMARY #length 3259 #molecular-weight 376075 #checksum 4495 SEQUENCE /// ENTRY A35041 #type complete TITLE ryanodine receptor type 1, skeletal muscle - human ALTERNATE_NAMES calcium release channel protein ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jan-2000 ACCESSIONS A35041; I84622; S66630 REFERENCE A35041 !$#authors Zorzato, F.; Fujii, J.; Otsu, K.; Phillips, M.; Green, N.M.; !1Lai, F.A.; Meissner, G.; MacLennan, D.H. !$#journal J. Biol. Chem. (1990) 265:2244-2256 !$#title Molecular cloning of cDNA encoding human and rabbit forms of !1the Ca(2+) release channel (ryanodine receptor) of skeletal !1muscle sarcoplasmic reticulum. !$#cross-references MUID:90130482; PMID:2298749 !$#accession A35041 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-5032 ##label ZOR !'##cross-references GB:J05200; NID:g337721; PIDN:AAA60294.1; !1PID:g337722 REFERENCE I46644 !$#authors Otsu, K.; Phillips, M.S.; Khanna, V.K.; de Leon, S.; !1MacLennan, D.H. !$#journal Genomics (1992) 13:835-837 !$#title Refinement of diagnostic assays for a probable causal !1mutation for porcine and human malignant hyperthermia. !$#cross-references MUID:92347887; PMID:1639409 !$#accession I84622 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 598-722 ##label RES !'##cross-references GB:M91455; NID:g337723; PIDN:AAA60295.1; !1PID:g553643 REFERENCE S66630 !$#authors Lynn, S.; Morgan, J.M.; Lamb, H.K.; Meissner, G.; Gillespie, !1J.I. !$#journal FEBS Lett. (1995) 372:6-12 !$#title Isolation and partial cloning of ryanodine-sensitive Ca(2+) !1release channel protein isoforms from human myometrial !1smooth muscle. !$#cross-references MUID:96032536; PMID:7556644 !$#accession S66630 !'##molecule_type mRNA !'##residues 4690-4968 ##label LYN !'##experimental_source myometrial smooth muscle GENETICS !$#gene GDB:RYR1 !'##cross-references GDB:120359; OMIM:180901 !$#map_position 19q13.1-19q13.1 !$#introns 642/2 CLASSIFICATION #superfamily ryanodine receptor; transcription initiation !1factor sigma region 1 homology KEYWORDS calcium channel; homotetramer; phosphoprotein; skeletal !1muscle; transmembrane protein FEATURE !$1788-1984 #domain transcription initiation factor sigma region !81 homology #label SR1 SUMMARY #length 5032 #molecular-weight 564429 #checksum 9153 SEQUENCE /// ENTRY I46646 #type complete TITLE ryanodine receptor, skeletal muscle - pig ALTERNATE_NAMES calcium release channel protein ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS I46646; I46645; S31395; I47133; S26624; A37105; I47212; !1S18135 REFERENCE I46645 !$#authors Fujii, J.; Otsu, K.; Zorzato, F.; De Leon, S.; Khanna, V.K.; !1Weiler, J.E.; O'Brien, P.J.; MacLennan, D.H. !$#journal Science (1991) 253:448-451 !$#title Identification of a mutation in porcine ryanodine receptor !1associated with malignant hypothermia. !$#cross-references MUID:91320118; PMID:1862346 !$#accession I46646 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-5035 ##label FUJ !'##cross-references GB:M91452; NID:g164647; PIDN:AAA31119.1; !1PID:g164648 !$#accession I46645 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-614,'C',616-5035 ##label FU2 !'##cross-references GB:M91451; NID:g164645; PIDN:AAA31118.1; !1PID:g164646 REFERENCE S31395 !$#authors Leeb, T.; Brem, G.; Brenig, B. !$#submission submitted to the EMBL Data Library, November 1992 !$#description Genomic organization of porcine skeletal muscle ryanodine !1receptor gene coding region 4624-7929. !$#accession S31395 !'##molecule_type DNA !'##residues 1542-2643 ##label LEE !'##cross-references EMBL:X69465 REFERENCE A48915 !$#authors Leeb, T.; Schmoelzl, S.; Brem, G.; Brenig, B. !$#journal Genomics (1993) 18:349-354 !$#title Genomic organization of the porcine skeletal muscle !1ryanodine receptor (RYR1) gene coding region 4624 to 7929. !$#cross-references MUID:94117003; PMID:8288238 !$#contents annotation REFERENCE I47133 !$#authors Harbitz, I.; Kristensen, T.; Bosnes, M.; Kran, S.; Davies, !1W. !$#journal Anim. Genet. (1992) 23:395-402 !$#title DNA sequence of the skeletal muscle calcium release channel !1cDNA and verification of the Arg615----Cys615 mutation, !1associated with porcine malignant hyperthermia, in Norwegian !1landrace pigs. !$#cross-references MUID:93036581; PMID:1329581 !$#accession I47133 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 2-2091,'A',2093-3494,'L',3496-4163,'S',4165-4182,'R', !14184-4411,'W',4413-4971,'R',4973-5035 ##label HA3 !'##cross-references EMBL:X62880; NID:g1936; PIDN:CAA44674.1; PID:g1937 REFERENCE S26624 !$#authors Harbitz, I.; Kristensen, T.; Kran, T.; Davies, W. !$#submission submitted to the EMBL Data Library, August 1992 !$#accession S26624 !'##molecule_type DNA !'##residues 482-706 ##label HAW !'##cross-references EMBL:X68247 REFERENCE A37105 !$#authors Harbitz, I.; Chowdhary, B.; Thomsen, P.D.; Davies, W.; !1Kaufmann, U.; Kran, S.; Gustavsson, I.; Christensen, K.; !1Hauge, J.G. !$#journal Genomics (1990) 8:243-248 !$#title Assignment of the porcine calcium release channel gene, a !1candidate for the malignant hyperthermia locus, to the 6p11 !1-> q21 segment of chromosome 6. !$#cross-references MUID:91065640; PMID:2174405 !$#accession A37105 !'##status preliminary !'##molecule_type mRNA !'##residues 4785-4971,'R',4973-5035 ##label HA2 !'##cross-references GB:M32501; NID:g164428; PIDN:AAA31022.1; !1PID:g164429 REFERENCE A55660 !$#authors Ledbetter, M.W.; Preiner, J.K.; Louis, C.F.; Mickelson, J.R. !$#journal J. Biol. Chem. (1994) 269:31544-31551 !$#title Tissue distribution of ryanodine receptor isoforms and !1alleles determined by reverse transcription polymerase chain !1reaction. !$#cross-references MUID:95081095; PMID:7989322 !$#accession I47212 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 516-676 ##label LED !'##cross-references EMBL:U15965; NID:g562095; PIDN:AAA60467.1; !1PID:g562096 GENETICS !$#gene RYR1 !$#introns 527/1; 559/1; 598/3; 643/2; 1570/3; 1646/2; 1850/3; 1939/3; !12006/3; 2044/1; 2093/1; 2184/2; 2222/3; 2267/2613/2 !$#note the list of introns may be incomplete CLASSIFICATION #superfamily ryanodine receptor; transcription initiation !1factor sigma region 1 homology KEYWORDS calcium channel SUMMARY #length 5035 #molecular-weight 565152 #checksum 9145 SEQUENCE /// ENTRY A54161 #type complete TITLE ryanodine-binding protein alpha form - bullfrog ORGANISM #formal_name Rana catesbeiana #common_name bullfrog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A54161 REFERENCE A54161 !$#authors Oyamada, H.; Murayama, T.; Takagi, T.; Iino, M.; Iwabe, N.; !1Miyata, T.; Ogawa, Y.; Endo, M. !$#journal J. Biol. Chem. (1994) 269:17206-17214 !$#title Primary structure and distribution of ryanodine-binding !1protein isoforms of the bullfrog skeletal muscle. !$#cross-references MUID:94274714; PMID:8006029 !$#accession A54161 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-5037 ##label OYA !'##cross-references GB:D21070; NID:g1856972; PIDN:BAA04646.1; !1PID:g538246 CLASSIFICATION #superfamily ryanodine receptor; transcription initiation !1factor sigma region 1 homology SUMMARY #length 5037 #molecular-weight 571286 #checksum 3601 SEQUENCE /// ENTRY A40399 #type complete TITLE mannose 6-phosphate receptor, cation-dependent, precursor - mouse ALTERNATE_NAMES CD-MPR ORGANISM #formal_name Mus musculus #common_name house mouse DATE 06-Dec-1991 #sequence_revision 26-Apr-1996 #text_change 15-Jun-2001 ACCESSIONS A40399; S14741; S25765; S25766; A39538 REFERENCE A40399 !$#authors Ma, Z.; Grubb, J.H.; Sly, W.S. !$#journal J. Biol. Chem. (1991) 266:10589-10595 !$#title Cloning, sequencing, and functional characterization of the !1murine 46-kDa mannose 6-phosphated receptor. !$#cross-references MUID:91244839; PMID:1645352 !$#accession A40399 !'##molecule_type mRNA !'##residues 1-278 ##label MAA !'##cross-references GB:M63286; NID:g199787; PIDN:AAA39735.1; !1PID:g199788 REFERENCE S14741 !$#authors Koester, A.; Nagel, G.; von Figura, K.; Pohlmann, R. !$#journal Biol. Chem. Hoppe-Seyler (1991) 372:297-300 !$#title Molecular cloning of the mouse 46-kDa mannose 6-phosphate !1receptor (MPR 46). !$#cross-references MUID:91282985; PMID:1647783 !$#accession S14741 !'##status preliminary !'##molecule_type mRNA !'##residues 1-278 ##label KOE !'##cross-references EMBL:X56831; NID:g53205; PIDN:CAA40162.1; !1PID:g53206 REFERENCE S25765 !$#authors Ludwig, T.; Ruether, U.; Metzger, R.; Copeland, N.G.; !1Jenkins, N.A.; Lobel, P.; Hoflack, B. !$#journal J. Biol. Chem. (1992) 267:12211-12219 !$#title Gene and pseudogene of the mouse cation-dependent mannose !16-phosphate receptor. !$#cross-references MUID:92291105; PMID:1376319 !$#accession S25765 !'##status preliminary !'##molecule_type DNA !'##residues 1-278 ##label LUD1 !'##cross-references EMBL:X64070; NID:g50361; PIDN:CAA45426.1; !1PID:g50362 !'##note the authors translated the codon CAG for residue 231 as Glu !$#accession S25766 !'##status preliminary; translation not shown !'##molecule_type mRNA !'##residues 1-278 ##label LUD2 !'##cross-references EMBL:X64068; NID:g50364; PIDN:CAA45423.1; !1PID:g50365 REFERENCE A39538 !$#authors Szebenyi, G.; Rotwein, P. !$#journal J. Biol. Chem. (1991) 266:5534-5539 !$#title Differential regulation of mannose 6-phosphate receptors and !1their ligands during the myogenic development of C2 cells. !$#cross-references MUID:91170218; PMID:1848553 !$#accession A39538 !'##molecule_type DNA !'##residues 162-195,'T',197-220,'T',222-225,'P',227 ##label SZE !'##cross-references GB:M58585 GENETICS !$#introns 60/2; 116/1; 152/3; 196/2; 238/3 FUNCTION !$#description This receptor binds the lysosomal targeting signal mannose !16-phosphate and carries enzymes modified with this group !1along to acidic pre-lysosomal compartments. CLASSIFICATION #superfamily mannose 6-phosphate receptor, cation-dependent KEYWORDS glycoprotein; Golgi apparatus; transmembrane protein FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-278 #product mannose 6-phosphate receptor, !8cation-dependent #status predicted #label MAT\ !$58,84,95,108,114 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 278 #molecular-weight 31172 #checksum 8050 SEQUENCE /// ENTRY A28372 #type complete TITLE insulin-like growth factor 2 receptor precursor - human ALTERNATE_NAMES IGF-II receptor; mannose 6-phosphate receptor precursor, cation-independent ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A28372; I37623; S58278 REFERENCE A28372 !$#authors Oshima, A.; Nolan, C.M.; Kyle, J.W.; Grubb, J.H.; Sly, W.S. !$#journal J. Biol. Chem. (1988) 263:2553-2562 !$#title The human cation-independent mannose 6-phosphate receptor. !1Cloning and sequence of the full-length cDNA and expression !1of functional receptor in COS cells. !$#cross-references MUID:88115410; PMID:2963003 !$#accession A28372 !'##molecule_type DNA !'##residues 1-2491 ##label OSH !'##cross-references GB:J03528; NID:g188671 REFERENCE I37623 !$#authors Morgan, D.O.; Edman, J.C.; Standring, D.N.; Fried, V.A.; !1Smith, M.C.; Roth, R.A.; Rutter, W.J. !$#journal Nature (1987) 329:301-307 !$#title Insulin-like growth factor II receptor as a multifunctional !1binding protein. !$#cross-references MUID:87315441; PMID:2957598 !$#accession I37623 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-179,'E',181-253,'L',255-509,'E',511-611,'R',613-844,'V', !1846-1488,'S',1490-1702,'A',1704-2025,'I',2027-2074,'T', !12076-2155,'K',2157-2159,'A',2161-2175,'Q',2177-2329,'E', !12331-2334,'V',2336-2340,'T',2342-2409,'E',2411-2491 ##label !1MOR !'##cross-references EMBL:Y00285; NID:g33054; PIDN:CAA68395.1; !1PID:g33055 REFERENCE S58277 !$#authors Smrzka, O.W.; Stoger, R.; Kurzbauer, R.; Fae, I.; Fischer, !1G.F.; Barlow, D.P. !$#submission submitted to the EMBL Data Library, January 1995 !$#description Conservation of a methylation imprint and a putative !1imprinting box at the human IGF2R locus. !$#accession S58278 !'##status preliminary !'##molecule_type DNA !'##residues 54-97,'K' ##label SMR !'##cross-references EMBL:X83700; NID:g929646; PID:g929647 GENETICS !$#gene GDB:IGF2R !'##cross-references GDB:120083; OMIM:147280 !$#map_position 6q26-6q26 CLASSIFICATION #superfamily mannose 6-phosphate receptor, !1cation-independent; fibronectin type II repeat homology KEYWORDS glycoprotein; growth factor receptor; transmembrane protein FEATURE !$1-40 #domain signal sequence #status predicted #label SIG\ !$41-2491 #product insulin-like growth factor 2 receptor !8#status predicted #label MAT\ !$1903-1942 #domain fibronectin type II repeat homology #label !82F1 SUMMARY #length 2491 #molecular-weight 274342 #checksum 4828 SEQUENCE /// ENTRY A49617 #type complete TITLE insulin-like growth factor II / cation-independent mannose 6-phosphate receptor precursor - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A49617; B39538; A48700; A46439; I52815; I65739; A57529 REFERENCE A49617 !$#authors Szebenyi, G.; Rotwein, P. !$#journal Genomics (1994) 19:120-129 !$#title The mouse insulin-like growth factor II/cation-independent !1mannose 6-phosphate (IGF-II/MPR) receptor gene: molecular !1cloning and genomic organization. !$#cross-references MUID:94245146; PMID:8188212 !$#accession A49617 !'##molecule_type DNA !'##residues 1-2483 ##label SZE !'##cross-references GB:L22143; NID:g431410; PIDN:AAA39320.1; !1PID:g431412 REFERENCE A39538 !$#authors Szebenyi, G.; Rotwein, P. !$#journal J. Biol. Chem. (1991) 266:5534-5539 !$#title Differential regulation of mannose 6-phosphate receptors and !1their ligands during the myogenic development of C2 cells. !$#cross-references MUID:91170218; PMID:1848553 !$#accession B39538 !'##molecule_type DNA !'##residues 435-488 ##label SZ2 !'##cross-references GB:M58586 REFERENCE A48700 !$#authors Chen, H.J.; Remmler, J.; Delaney, J.C.; Messner, D.J.; !1Lobel, P. !$#journal J. Biol. Chem. (1993) 268:22338-22346 !$#title Mutational analysis of the cation-independent mannose !16-phosphate/insulin-like growth factor II receptor. A !1consensus casein kinase II site followed by 2 leucines near !1the carboxyl terminus is important for intracellular !1targeting of lysosomal enzymes. !$#cross-references MUID:94042980; PMID:8226743 !$#accession A48700 !'##molecule_type mRNA !'##residues 2249-2483 ##label CHE !'##cross-references GB:L19500; NID:g407325; PIDN:AAA16037.1; !1PID:g407326 REFERENCE A46439 !$#authors Stoger, R.; Kubicka, P.; Liu, C.G.; Kafri, T.; Razin, A.; !1Cedar, H.; Barlow, D.P. !$#journal Cell (1993) 73:61-71 !$#title Maternal-specific methylation of the imprinted mouse Igf2r !1locus identifies the expressed locus as carrying the !1imprinting signal. !$#cross-references MUID:93214996; PMID:8462104 !$#accession A46439 !'##molecule_type DNA !'##residues 1-44 ##label STO !'##cross-references GB:L06445; NID:g293379; PIDN:AAA37921.1; !1PID:g553942 !'##note sequence extracted from NCBI backbone (NCBIN:128531, !1NCBIP:128532) REFERENCE I52815 !$#authors Stoeger, R.; Kubicka, P.; Liu, C. !$#journal Cell (1993) 73:1-11 !$#title Maternal-specific methylation of the imprinted mouse Igf2r !1locus identifies the expressed locus as carrying the !1imprinting signal. !$#cross-references MUID:93214982; PMID:8462093 !$#accession I52815 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-44 ##label RES !'##cross-references GB:L06445; NID:g293379; PIDN:AAA37921.1; !1PID:g553942 !$#accession I65739 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 93-106 ##label RE2 !'##cross-references GB:L06446; NID:g293381; PIDN:AAA37922.1; !1PID:g293382 REFERENCE A57529 !$#authors Liu, Z.; Mittanck, D.W.; Kim, S.; Rotwein, P. !$#journal Mol. Endocrinol. (1995) 9:1477-1487 !$#title Control of insulin-like growth factor-II/mannose 6-phosphate !1receptor gene transcription by proximal promoter elements. !$#cross-references MUID:96130821; PMID:8584025 !$#accession A57529 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-44 ##label LIU !'##cross-references GB:U26348; NID:g973191; PIDN:AAA98844.1; !1PID:g973192 GENETICS !$#gene Igf2r FUNCTION LYSO !$#description transports lysosomal enzymes marked by the presence of !1mannose 6-phosphate from the trans-Golgi to a pre-lysosomal !1compartment FUNCTION IGFR !$#description binds to, internalizes, and may play a role in transmembrane !1signalling of insulin-like growth factor II CLASSIFICATION #superfamily mannose 6-phosphate receptor, !1cation-independent; fibronectin type II repeat homology KEYWORDS duplication; growth factor receptor; transmembrane protein FEATURE !$1-35 #domain signal sequence #status predicted #label SIG\ !$36-2294 #domain extracellular #status predicted #label EXT\ !$1896-1935 #domain fibronectin type II repeat homology #label !82F1\ !$2295-2316 #domain transmembrane #status predicted #label TMM\ !$2317-2483 #domain intracellular #status predicted #label INT SUMMARY #length 2483 #molecular-weight 273813 #checksum 1431 SEQUENCE /// ENTRY A30788 #type complete TITLE mannose 6-phosphate receptor protein, cation-independent - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A25908; A30788; S09404 REFERENCE A92706 !$#authors Lobel, P.; Dahms, N.M.; Kornfeld, S. !$#journal J. Biol. Chem. (1988) 263:2563-2570 !$#title Cloning and sequence analysis of the cation-independent !1mannose 6-phosphate receptor. !$#cross-references MUID:88115411; PMID:2963004 !$#accession A25908 !'##molecule_type mRNA !'##residues 1-2499 ##label LOB !'##cross-references GB:J03527; NID:g162873; PIDN:AAA30455.1; !1PID:g162874; GB:M15869 REFERENCE S09404 !$#authors Glickman, J.N.; Conibear, E.; Pearse, B.M.F. !$#journal EMBO J. (1989) 8:1041-1047 !$#title Specificity of binding of clathrin adaptors to signals on !1the mannose-6-phosphate/insulin-like growth factor II !1receptor. !$#cross-references MUID:89305502; PMID:2545438 !$#contents annotation; HA-II adaptor binding COMMENT This protein binds phosphorylated lysosomal enzymes and !1insulin-like growth factor II. CLASSIFICATION #superfamily mannose 6-phosphate receptor, !1cation-independent; fibronectin type II repeat homology KEYWORDS Golgi apparatus; membrane protein FEATURE !$1912-1951 #domain fibronectin type II repeat homology #label !82F1\ !$2360-2363 #region HA-II adaptor binding SUMMARY #length 2499 #molecular-weight 274526 #checksum 7467 SEQUENCE /// ENTRY ACRTK1 #type complete TITLE glutamate receptor K1 precursor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 04-Nov-1994 ACCESSIONS S07059; S18184 REFERENCE S07059 !$#authors Hollmann, M.; O'Shea-Greenfield, A.; Rogers, S.W.; !1Heinemann, S. !$#journal Nature (1989) 342:643-648 !$#title Cloning by functional expression of a member of the !1glutamate receptor family. !$#cross-references MUID:90081835; PMID:2480522 !$#accession S07059 !'##molecule_type mRNA !'##residues 1-907 ##label HOL1 !'##cross-references EMBL:X17184 CLASSIFICATION #superfamily glutamate receptor; glutamate receptor homology KEYWORDS glycoprotein; ion channel; neurotransmitter receptor; !1transmembrane protein FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-907 #product glutamate receptor #status predicted #label !8MAT\ !$19-480 #domain extracellular #status predicted #label EXT1\ !$411-839 #domain glutamate receptor homology #label GRH\ !$481-498 #domain transmembrane #status predicted #label TM1\ !$539-557 #domain transmembrane #status predicted #label TM2\ !$614-632 #domain transmembrane #status predicted #label TM3\ !$633-805 #domain intracellular #status predicted #label INT\ !$806-826 #domain transmembrane #status predicted #label TM4\ !$827-907 #domain extracellular #status predicted #label EXT2\ !$63,249,257,363,401, !$406 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 907 #molecular-weight 101691 #checksum 5686 SEQUENCE /// ENTRY ACGAE #type complete TITLE glutamate receptor precursor - great pond snail ORGANISM #formal_name Lymnaea stagnalis #common_name great pond snail DATE 31-Mar-1992 #sequence_revision 28-Oct-1994 #text_change 22-Jun-1999 ACCESSIONS S18443; S15681 REFERENCE S18443 !$#authors Hutton, M.L.; Harvey, R.J.; Barnard, E.A.; Darlison, M.G. !$#journal FEBS Lett. (1991) 292:111-114 !$#title Cloning of a cDNA that encodes an invertebrate glutamate !1receptor subunit. !$#cross-references MUID:92070466; PMID:1659993 !$#accession S18443 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-917 ##label HUT !'##cross-references EMBL:X60086 REFERENCE S15681 !$#authors Hutton, M.L.; Bhandal, N.S.; Harvey, R.J.; Usherwood, !1P.N.R.; Darlison, M.G. !$#submission submitted to the EMBL Data Library, June 1991 !$#description PCR-mediated cloning of a cDNA that encodes a functional !1molluscan glutamate receptor subunit. !$#accession S15681 !'##molecule_type mRNA !'##residues 1-362,'K',364-776,'S',778-845,'R',847-886,'S',888-917 !1##label HU2 !'##cross-references EMBL:X60086; NID:g9628; PIDN:CAA42683.1; PID:g9629 CLASSIFICATION #superfamily glutamate receptor; glutamate receptor homology KEYWORDS glycoprotein; ion channel; neurotransmitter receptor; !1transmembrane protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-917 #product glutamate receptor #status predicted #label !8MAT\ !$429-853 #domain glutamate receptor homology #label GRH\ !$559-578 #domain transmembrane #status predicted #label TM1\ !$599-617 #domain transmembrane #status predicted #label TM2\ !$628-646 #domain transmembrane #status predicted #label TM3\ !$819-839 #domain transmembrane #status predicted #label TM4\ !$62,95,121,125,229, !$251,261,272,418, !$419,424,491,881 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 917 #molecular-weight 103106 #checksum 8952 SEQUENCE /// ENTRY S07062 #type complete TITLE glutamate receptor precursor - chicken ALTERNATE_NAMES kainate-binding protein ORGANISM #formal_name Gallus gallus #common_name chicken DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S07062; S27105 REFERENCE S07062 !$#authors Gregor, P.; Mano, I.; Maoz, I.; McKeown, M.; Teichberg, V.I. !$#journal Nature (1989) 342:689-692 !$#title Molecular structure of the chick cerebellar kainate-binding !1subunit of a putative glutamate receptor. !$#cross-references MUID:90081841; PMID:2480525 !$#accession S07062 !'##molecule_type DNA !'##residues 1-487 ##label GRE !'##cross-references EMBL:X17700; NID:g62786; PIDN:CAA35693.1; !1PID:g62787 !$#accession S27105 !'##molecule_type protein !'##residues 24-27,'X',29-30,'X',32-37;61,'X',63-70,'X',72-74,'XX', !177-81,'X',83-90,'X',92-94;158-161,'X',163-168;310-313,'X', !1315-319,'X',321-322;330-346 ##label GR2 CLASSIFICATION #superfamily kainate-binding protein; glutamate receptor !1homology KEYWORDS glycoprotein; ion channel; neurotransmitter receptor; !1phosphoprotein; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-487 #product glutamate receptor #status experimental !8#label MAT\ !$51-454 #domain glutamate receptor homology #label GRH\ !$172-190 #domain transmembrane #status predicted #label TM1\ !$207-225 #domain transmembrane #status predicted #label TM2\ !$236-260 #domain transmembrane #status predicted #label TM3\ !$419-440 #domain transmembrane #status predicted #label TM4\ !$104,444 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$380,408 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 487 #molecular-weight 54355 #checksum 5598 SEQUENCE /// ENTRY S07061 #type complete TITLE glutamate receptor precursor - northern leopard frog ALTERNATE_NAMES kainate receptor; kainate-binding protein ORGANISM #formal_name Rana pipiens berlandieri #common_name northern leopard frog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S07061 REFERENCE S07061 !$#authors Wada, K.; Dechesne, C.J.; Shimasaki, S.; King, R.G.; Kusano, !1K.; Buonanno, A.; Hampson, D.R.; Banner, C.; Wenthold, R.J.; !1Nakatani, Y. !$#journal Nature (1989) 342:684-689 !$#title Sequence and expression of a frog brain complementary DNA !1encoding a kainate-binding protein. !$#cross-references MUID:90081840; PMID:2556640 !$#accession S07061 !'##molecule_type mRNA !'##residues 1-487 ##label WAD !'##cross-references EMBL:X17314; NID:g64290; PIDN:CAA35193.1; !1PID:g64291 !'##note part of this sequence was confirmed by protein sequencing CLASSIFICATION #superfamily kainate-binding protein; glutamate receptor !1homology KEYWORDS glycoprotein; ion channel; neurotransmitter receptor; !1transmembrane protein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-487 #product glutamate receptor #status predicted #label !8MAT\ !$43-448 #domain glutamate receptor homology #label GRH\ !$164-183 #domain transmembrane #status predicted #label TM1\ !$200-218 #domain transmembrane #status predicted #label TM2\ !$229-253 #domain transmembrane #status predicted #label TM3\ !$414-434 #domain transmembrane #status predicted #label TM4\ !$78,97 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 487 #molecular-weight 54278 #checksum 5553 SEQUENCE /// ENTRY S29159 #type complete TITLE glutamate receptor, NMDA-sensitive, epsilon-1 chain precursor - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S29159 REFERENCE S29159 !$#authors Meguro, H.; Mori, H.; Araki, K.; Kushiya, E.; Kutsuwada, T.; !1Yamazaki, M.; Kumanishi, T.; Arakawa, M.; Sakimura, K.; !1Mishina, M. !$#journal Nature (1992) 357:70-74 !$#title Functional characterization of a heteromeric NMDA receptor !1channel expressed from cloned cDNAs. !$#cross-references MUID:92244361; PMID:1374164 !$#accession S29159 !'##molecule_type mRNA !'##residues 1-1464 ##label MEG !'##cross-references EMBL:D10217; NID:g220410; PIDN:BAA01069.1; !1PID:g220411 CLASSIFICATION #superfamily N-methyl-D-aspartate receptor 2A; glutamate !1receptor homology KEYWORDS ion channel; neurotransmitter receptor; transmembrane !1protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-1464 #product glutamate receptor epsilon-1 chain #status !8predicted #label MAT\ !$428-854 #domain glutamate receptor homology #label GRH\ !$557-576 #domain transmembrane #status predicted #label TM1\ !$599-618 #domain transmembrane #status predicted #label TM2\ !$629-647 #domain transmembrane #status predicted #label TM3\ !$817-837 #domain transmembrane #status predicted #label TM4 SUMMARY #length 1464 #molecular-weight 165489 #checksum 4046 SEQUENCE /// ENTRY B45219 #type complete TITLE N-methyl-D-aspartate receptor chain NMDAR2C - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B45219 REFERENCE A45219 !$#authors Ishii, T.; Moriyoshi, K.; Sugihara, H.; Sakurada, K.; !1Kadotani, H.; Yokoi, M.; Akazawa, C.; Shigemoto, R.; Mizuno, !1N.; Masu, M.; Nakanishi, S. !$#journal J. Biol. Chem. (1993) 268:2836-2843 !$#title Molecular characterization of the family of the !1N-methyl-D-aspartate receptor subunits. !$#cross-references MUID:93155102; PMID:8428958 !$#accession B45219 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-1250 ##label ISH !'##experimental_source brain !'##note sequence extracted from NCBI backbone (NCBIP:124263) CLASSIFICATION #superfamily N-methyl-D-aspartate receptor 2C; glutamate !1receptor homology FEATURE !$438-865 #domain glutamate receptor homology #label GRH SUMMARY #length 1250 #molecular-weight 136634 #checksum 281 SEQUENCE /// ENTRY C45219 #type complete TITLE N-methyl-D-aspartate receptor chain NMDAR2D-1 - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C45219 REFERENCE A45219 !$#authors Ishii, T.; Moriyoshi, K.; Sugihara, H.; Sakurada, K.; !1Kadotani, H.; Yokoi, M.; Akazawa, C.; Shigemoto, R.; Mizuno, !1N.; Masu, M.; Nakanishi, S. !$#journal J. Biol. Chem. (1993) 268:2836-2843 !$#title Molecular characterization of the family of the !1N-methyl-D-aspartate receptor subunits. !$#cross-references MUID:93155102; PMID:8428958 !$#accession C45219 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-1356 ##label ISH !'##experimental_source brain !'##note sequence extracted from NCBI backbone (NCBIP:124264) CLASSIFICATION #superfamily N-methyl-D-aspartate receptor 2D; glutamate !1receptor homology FEATURE !$451-879 #domain glutamate receptor homology #label GRH SUMMARY #length 1356 #molecular-weight 145973 #checksum 5329 SEQUENCE /// ENTRY ACHUA1 #type complete TITLE nicotinic acetylcholine receptor alpha-1 chain precursor, muscle - human ORGANISM #formal_name Homo sapiens #common_name man DATE 18-Apr-1984 #sequence_revision 18-Apr-1984 #text_change 22-Jun-1999 ACCESSIONS A03168; S00238; A27591 REFERENCE A03168 !$#authors Noda, M.; Furutani, Y.; Takahashi, H.; Toyosato, M.; Tanabe, !1T.; Shimizu, S.; Kikyotani, S.; Kayano, T.; Hirose, T.; !1Inayama, S.; Numa, S. !$#journal Nature (1983) 305:818-823 !$#title Cloning and sequence analysis of calf cDNA and human genomic !1DNA encoding alpha-subunit precursor of muscle acetylcholine !1receptor. !$#cross-references MUID:84039794; PMID:6688857 !$#accession A03168 !'##molecule_type DNA !'##residues 1-457 ##label NOD !'##cross-references GB:X02502; NID:g28291; PIDN:CAA26344.1; PID:g669153 REFERENCE S00238 !$#authors Schoepfer, R.; Luther, M.; Lindstrom, J. !$#journal FEBS Lett. (1988) 226:235-240 !$#title The human medulloblastoma cell line TE671 expresses a !1muscle-like acetylcholine receptor. Cloning of the !1alpha-subunit cDNA. !$#cross-references MUID:88112190; PMID:3338555 !$#accession S00238 !'##molecule_type mRNA !'##residues 1-457 ##label SCH !'##cross-references EMBL:Y00762; NID:g28308; PIDN:CAA68731.1; !1PID:g28309 REFERENCE A27591 !$#authors Hohlfeld, R.; Toyka, K.V.; Miner, L.L.; Walgrave, S.L.; !1Conti-Tronconi, B.M. !$#journal J. Clin. Invest. (1988) 81:657-660 !$#title Amphipathic segment of the nicotinic receptor alpha subunit !1contains epitopes recognized by T lymphocytes in myasthenia !1gravis. !$#cross-references MUID:88139764; PMID:2449458 !$#contents annotation GENETICS !$#gene GDB:CHRNA1; CHRNA !'##cross-references GDB:120586; OMIM:100690 !$#map_position 2q24-2q32 !$#introns 15/1; 63/3; 78/3; 115/2; 180/3; 260/1; 334/3; 414/3 COMPLEX the functional receptor molecule is a heteropentamer with !1two alpha chains and one each of beta, delta, and gamma !1chains CLASSIFICATION #superfamily acetylcholine receptor KEYWORDS alternative splicing; glycoprotein; heteropentamer; ion !1channel; neurotransmitter receptor; postsynaptic membrane; !1transmembrane protein FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-457 #product nicotinic acetylcholine receptor alpha chain !8#status predicted #label MAT\ !$231-257 #domain transmembrane #status predicted #label TM1\ !$263-281 #domain transmembrane #status predicted #label TM2\ !$297-318 #domain transmembrane #status predicted #label TM3\ !$429-447 #domain transmembrane #status predicted #label TM4\ !$148-162 #disulfide_bonds #status predicted\ !$161 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 457 #molecular-weight 51838 #checksum 1997 SEQUENCE /// ENTRY ACBOA1 #type complete TITLE nicotinic acetylcholine receptor alpha chain precursor - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 18-Apr-1984 #sequence_revision 18-Apr-1984 #text_change 22-Jun-1999 ACCESSIONS A03169 REFERENCE A03168 !$#authors Noda, M.; Furutani, Y.; Takahashi, H.; Toyosato, M.; Tanabe, !1T.; Shimizu, S.; Kikyotani, S.; Kayano, T.; Hirose, T.; !1Inayama, S.; Numa, S. !$#journal Nature (1983) 305:818-823 !$#title Cloning and sequence analysis of calf cDNA and human genomic !1DNA encoding alpha-subunit precursor of muscle acetylcholine !1receptor. !$#cross-references MUID:84039794; PMID:6688857 !$#accession A03169 !'##molecule_type mRNA !'##residues 1-457 ##label NOD !'##cross-references GB:X02509; NID:g49; PIDN:CAA26345.1; PID:g50 !'##note four hydrophobic transmembrane segments are found in each of !1the four kinds of chains in the receptor molecule; the !1authors propose that these segments comprise residues !1231-257, 263-281, 297-318, and 429-447 in the alpha chain COMMENT The functional receptor molecule has two alpha chains and !1one each of the beta, delta, and gamma chains. CLASSIFICATION #superfamily acetylcholine receptor KEYWORDS glycoprotein; ion channel; membrane protein; !1neurotransmitter receptor; postsynaptic membrane FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-457 #product nicotinic acetylcholine receptor alpha chain !8#status predicted #label MAT\ !$148-162 #disulfide_bonds #status predicted\ !$161 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 457 #molecular-weight 51947 #checksum 9445 SEQUENCE /// ENTRY ACCHAN #type complete TITLE nicotinic acetylcholine receptor alpha chain precursor - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 21-Jul-2000 ACCESSIONS S00376; A38754; I50148 REFERENCE S00376 !$#authors Nef, P.; Oneyser, C.; Alliod, C.; Couturier, S.; Ballivet, !1M. !$#journal EMBO J. (1988) 7:595-601 !$#title Genes expressed in the brain define three distinct neuronal !1nicotinic acetylcholine receptors. !$#cross-references MUID:88283624; PMID:3267226 !$#accession S00376 !'##molecule_type DNA !'##residues 1-456 ##label NEF !'##cross-references EMBL:X07330; NID:g62820; PIDN:CAA30282.1; !1PID:g1334631 !$#accession A38754 !'##molecule_type mRNA !'##residues 1-456 ##label NEF2 !'##cross-references GB:X07330; GB:Y00834; NID:g62820; PIDN:CAA30282.1; !1PID:g1334631 REFERENCE I50148 !$#authors Klarsfeld, A.; Daubas, P.; Bourachot, B.; Changeux, J.P. !$#journal Mol. Cell. Biol. (1987) 7:951-955 !$#title A 5'-flanking region of the chicken acetylcholine receptor !1alpha-subunit gene confers tissue specificity and !1developmental control of expression in transfected cells. !$#cross-references MUID:87144271; PMID:3821734 !$#accession I50148 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-12 ##label KLA !'##cross-references GB:M15307; NID:g211065; PID:g555417 GENETICS !$#introns 14/1; 62/3; 77/3; 114/2; 179/3; 259/1; 333/3; 413/3 CLASSIFICATION #superfamily acetylcholine receptor KEYWORDS glycoprotein; ion channel; neurotransmitter receptor; !1postsynaptic membrane; transmembrane protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-456 #product nicotinic acetylcholine receptor alpha chain !8#status predicted #label MAT\ !$231-254 #domain transmembrane #status predicted #label TM1\ !$262-280 #domain transmembrane #status predicted #label TM2\ !$296-317 #domain transmembrane #status predicted #label TM3\ !$428-446 #domain transmembrane #status predicted #label TM4\ !$147-161,211-212 #disulfide_bonds #status predicted\ !$160 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 456 #molecular-weight 52182 #checksum 1149 SEQUENCE /// ENTRY ACRYA1 #type complete TITLE nicotinic acetylcholine receptor alpha chain precursor - Pacific electric ray ORGANISM #formal_name Torpedo californica #common_name Pacific electric ray DATE 30-Apr-1982 #sequence_revision 05-Apr-1983 #text_change 22-Jun-1999 ACCESSIONS A03170; A20972; A33555; A41587; A54233 REFERENCE A93290 !$#authors Noda, M.; Takahashi, H.; Tanabe, T.; Toyosato, M.; Furutani, !1Y.; Hirose, T.; Asai, M.; Inayama, S.; Miyata, T.; Numa, S. !$#journal Nature (1982) 299:793-797 !$#title Primary structure of alpha-subunit precursor of Torpedo !1californica acetylcholine receptor deduced from cDNA !1sequence. !$#cross-references MUID:83036943; PMID:6182472 !$#accession A03170 !'##molecule_type mRNA !'##residues 1-461 ##label NOD !'##cross-references GB:J00963; GB:M14810; NID:g213217; PIDN:AAA96705.1; !1PID:g213218 REFERENCE A20972 !$#authors Conti-Tronconi, B.M.; Hunkapiller, M.W.; Raftery, M.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:2631-2634 !$#title Molecular weight and structural nonequivalence of the mature !1alpha subunits of Torpedo californica acetylcholine !1receptor. !$#cross-references MUID:84194060; PMID:6585820 !$#accession A20972 !'##molecule_type protein !'##residues 25-127;336-421;429-450 ##label CON REFERENCE A33555 !$#authors Moore, C.R.; Yates III, J.R.; Griffin, P.R.; Shabanowitz, !1J.; Martino, P.A.; Hunt, D.F.; Cafiso, D.S. !$#journal Biochemistry (1989) 28:9184-9191 !$#title Proteolytic fragments of the nicotinic acetylcholine !1receptor identified by mass spectrometry: implications for !1receptor topography. !$#cross-references MUID:90105466; PMID:2605252 !$#accession A33555 !'##status preliminary !'##molecule_type protein !'##residues 29-41;82-88;132-149;339-354;363-411 ##label MOO REFERENCE A41587 !$#authors Cohen, J.B.; Sharp, S.D.; Liu, W.S. !$#journal J. Biol. Chem. (1991) 266:23354-23364 !$#title Structure of the agonist-binding site of the nicotinic !1acetylcholine receptor. [(3)H]acetylcholine mustard !1identifies residues in the cation-binding subsite. !$#cross-references MUID:92078212; PMID:1744130 !$#accession A41587 !'##molecule_type protein !'##residues 104-131 ##label COH !'##note residue 117-Tyr was shown to be alkylated by [3H]-acetylcholine !1mustard, an analog of acetylcholine REFERENCE A54233 !$#authors Blanton, M.P.; Cohen, J.B. !$#journal Biochemistry (1994) 33:2859-2872 !$#title Identifying the lipid-protein interface of the Torpedo !1nicotinic acetylcholine receptor: secondary structure !1implications. !$#cross-references MUID:94176477; PMID:8130199 !$#accession A54233 !'##status preliminary !'##molecule_type protein !'##residues 234-266;287-319;423-453 ##label BLA COMPLEX heterotetramer of two alpha chains, one beta chain (see !1PIR:ACRYB1), one gamma chain (see PIR:ACRYG1), and one delta !1chain (see PIR:ACRYD1) CLASSIFICATION #superfamily acetylcholine receptor KEYWORDS ion channel; membrane protein; neurotransmitter receptor; !1postsynaptic membrane FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-461 #product nicotinic acetylcholine receptor alpha chain !8#status predicted #label MAT\ !$236-259 #domain transmembrane #status predicted #label TM1\ !$267-285 #domain transmembrane #status predicted #label TM2\ !$297-324 #domain transmembrane #status predicted #label TM3\ !$423-450 #domain transmembrane #status predicted #label TM4 SUMMARY #length 461 #molecular-weight 52740 #checksum 287 SEQUENCE /// ENTRY ACHUA7 #type complete TITLE nicotinic acetylcholine receptor alpha-7 chain precursor, neuronal - human ALTERNATE_NAMES cholinergic nicotinate receptor alpha-7 chain ORGANISM #formal_name Homo sapiens #common_name man DATE 12-Aug-1996 #sequence_revision 31-Jan-1997 #text_change 22-Jun-1999 ACCESSIONS I37185; A54194; S60309 REFERENCE I37185 !$#authors Peng, X.; Katz, M.; Gerzanich, V.; Anand, R.; Lindstrom, J. !$#journal Mol. Pharmacol. (1994) 45:546-554 !$#title Human alpha 7 acetylcholine receptor: cloning of the alpha 7 !1subunit from the SH-SY5Y cell line and determination of !1pharmacological properties of native receptors and !1functional alpha 7 homomers expressed in Xenopus oocytes. !$#cross-references MUID:94195283; PMID:8145738 !$#accession I37185 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-502 ##label PEN !'##cross-references EMBL:X70297; NID:g496606; PIDN:CAA49778.1; !1PID:g496607 !'##experimental_source brain neuroblastoma cell line SHSY-5Y REFERENCE A54194 !$#authors Chini, B.; Raimond, E.; Elgoyhen, A.B.; Moralli, D.; !1Balzaretti, M.; Heinemann, S. !$#journal Genomics (1994) 19:379-381 !$#title Molecular cloning and chromosomal localization of the human !1alpha-7-nicotinic receptor subunit gene (CHRNA7). !$#cross-references MUID:94245214; PMID:8188270 !$#accession A54194 !'##molecule_type mRNA !'##residues 24-363,'S',365-374,'A',376-408,'AWPAP',414-502 ##label CHI !'##cross-references GB:Z23141; NID:g457736; PIDN:CAA80672.1; !1PID:g457737 !'##experimental_source retina COMMENT This acetylcholine receptor is blocked by alpha-bungarotoxin !1and is localized to extrasynaptic pseudodendritic regions of !1neuron surface membranes. GENETICS !$#gene GDB:CHRNA7 !'##cross-references GDB:138751; OMIM:118511 !$#map_position 15q14-15q14 !$#note defects in this gene have been associated with mental !1retardation and schizophrenia COMPLEX the functional receptor molecule is a heteropentamer with !1two alpha chains and one each of beta, delta, and gamma !1chains CLASSIFICATION #superfamily acetylcholine receptor KEYWORDS brain; glycoprotein; heteropentamer; ion channel; !1neurotransmitter receptor; phosphoprotein; postsynaptic !1membrane; schizophrenia; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-502 #product nicotinic acetylcholine receptor alpha-7 !8chain, neuronal #status predicted #label MAT\ !$231-254 #domain transmembrane #status predicted #label TR1\ !$262-280 #domain transmembrane #status predicted #label TR2\ !$296-317 #domain transmembrane #status predicted #label TR3\ !$470-488 #domain transmembrane #status predicted #label TR4\ !$46,90,133 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$150-164 #disulfide_bonds #status predicted\ !$365,413 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$415 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$442 #binding_site phosphate (Tyr) (covalent) #status !8predicted SUMMARY #length 502 #molecular-weight 56421 #checksum 7117 SEQUENCE /// ENTRY ACCH2N #type complete TITLE nicotinic acetylcholine receptor alpha-2 chain precursor, neuronal - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 21-Jul-2000 ACCESSIONS S00377 REFERENCE S00376 !$#authors Nef, P.; Oneyser, C.; Alliod, C.; Couturier, S.; Ballivet, !1M. !$#journal EMBO J. (1988) 7:595-601 !$#title Genes expressed in the brain define three distinct neuronal !1nicotinic acetylcholine receptors. !$#cross-references MUID:88283624; PMID:3267226 !$#accession S00377 !'##molecule_type DNA !'##residues 1-528 ##label NEF !'##cross-references EMBL:X07339; NID:g62792; PIDN:CAB59645.1; !1PID:g6136914 GENETICS !$#introns 21/1; 73/3; 88/3; 125/2; 487/3 CLASSIFICATION #superfamily acetylcholine receptor KEYWORDS glycoprotein; ion channel; neurotransmitter receptor; !1postsynaptic membrane; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-528 #product nicotinic acetylcholine receptor alpha-2 !8chain #status predicted #label MAT\ !$241-264 #domain transmembrane #status predicted #label TM1\ !$272-290 #domain transmembrane #status predicted #label TM2\ !$306-327 #domain transmembrane #status predicted #label TM3\ !$502-520 #domain transmembrane #status predicted #label TM4\ !$54,104 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$158-172,222-223 #disulfide_bonds #status predicted SUMMARY #length 528 #molecular-weight 60674 #checksum 2656 SEQUENCE /// ENTRY ACCH4N #type complete TITLE nicotinic acetylcholine receptor alpha-4 chain precursor, neuronal - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 21-Jul-2000 ACCESSIONS S00379; A38756; A61186 REFERENCE S00376 !$#authors Nef, P.; Oneyser, C.; Alliod, C.; Couturier, S.; Ballivet, !1M. !$#journal EMBO J. (1988) 7:595-601 !$#title Genes expressed in the brain define three distinct neuronal !1nicotinic acetylcholine receptors. !$#cross-references MUID:88283624; PMID:3267226 !$#accession S00379 !'##molecule_type mRNA !'##residues 1-622 ##label NEF !'##cross-references GB:X07348; GB:Y00834; NID:g62809; PIDN:CAA30285.1; !1PID:g871037 !$#accession A38756 !'##molecule_type DNA !'##residues 21-622 ##label NE2 !'##cross-references EMBL:X07348 REFERENCE A61186 !$#authors Whiting, P.J.; Schoepfer, R.; Conroy, W.G.; Gore, M.J.; !1Keyser, K.T.; Shimasaki, S.; Esch, F.; Lindstrom, J.M. !$#journal Brain Res. Mol. Brain Res. (1991) 10:61-70 !$#title Expression of nicotinic acetylcholine receptor subtypes in !1brain and retina. !$#cross-references MUID:91278688; PMID:1647484 !$#accession A61186 !'##molecule_type protein !'##residues 24-29,'XX',32 ##label WHI GENETICS !$#introns 21/1; 71/3; 86/3; 123/2; 581/3 CLASSIFICATION #superfamily acetylcholine receptor KEYWORDS glycoprotein; ion channel; neurotransmitter receptor; !1postsynaptic membrane; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-622 #product nicotinic acetylcholine receptor alpha-4 !8chain #status experimental #label MAT\ !$239-262 #domain transmembrane #status predicted #label TM1\ !$270-288 #domain transmembrane #status predicted #label TM2\ !$304-325 #domain transmembrane #status predicted #label TM3\ !$596-614 #domain transmembrane #status predicted #label TM4\ !$52,102,388,472 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$156-170,220-221 #disulfide_bonds #status predicted SUMMARY #length 622 #molecular-weight 70837 #checksum 4161 SEQUENCE /// ENTRY ACCH3N #type fragment TITLE nicotinic acetylcholine receptor alpha-3 chain, neuronal - chicken (fragment) ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 22-Jun-1999 ACCESSIONS S00378; A38755 REFERENCE S00376 !$#authors Nef, P.; Oneyser, C.; Alliod, C.; Couturier, S.; Ballivet, !1M. !$#journal EMBO J. (1988) 7:595-601 !$#title Genes expressed in the brain define three distinct neuronal !1nicotinic acetylcholine receptors. !$#cross-references MUID:88283624; PMID:3267226 !$#accession S00378 !'##molecule_type DNA; mRNA !'##residues 1-416 ##label NEF !'##cross-references EMBL:X07345; NID:g62803; PIDN:CAA30284.1; !1PID:g871036 GENETICS !$#introns 37/2; 374/3 CLASSIFICATION #superfamily acetylcholine receptor KEYWORDS glycoprotein; ion channel; neurotransmitter receptor; !1postsynaptic membrane; transmembrane protein FEATURE !$153-176 #domain transmembrane #status predicted #label TM1\ !$184-202 #domain transmembrane #status predicted #label TM2\ !$218-239 #domain transmembrane #status predicted #label TM3\ !$389-407 #domain transmembrane #status predicted #label TM4\ !$70-84,134-135 #disulfide_bonds #status predicted\ !$83,295,329 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 416 #checksum 3404 SEQUENCE /// ENTRY ACCHNN #type complete TITLE nicotinic acetylcholine receptor nonalpha chain precursor, neuronal - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 21-Jul-2000 ACCESSIONS S00380; A38757; JH0175; PS0297 REFERENCE S00376 !$#authors Nef, P.; Oneyser, C.; Alliod, C.; Couturier, S.; Ballivet, !1M. !$#journal EMBO J. (1988) 7:595-601 !$#title Genes expressed in the brain define three distinct neuronal !1nicotinic acetylcholine receptors. !$#cross-references MUID:88283624; PMID:3267226 !$#accession S00380 !'##molecule_type DNA !'##residues 1-491 ##label NEF !'##cross-references GB:X07353; GB:Y00834; NID:g62945; PIDN:CAA30286.1; !1PID:g871038 !$#accession A38757 !'##molecule_type mRNA !'##residues 1-491 ##label NEF2 !'##cross-references EMBL:X07353; NID:g62945; PIDN:CAA30286.1; !1PID:g871038 REFERENCE JH0175 !$#authors Schoepfer, R.; Whiting, P.; Esch, F.; Blacher, R.; !1Shimasaki, S.; Lindstrom, J. !$#journal Neuron (1988) 1:241-248 !$#title cDNA clones coding for the structural subunit of a chicken !1brain nicotinic acetylcholine receptor. !$#cross-references MUID:90166513; PMID:3272170 !$#accession JH0175 !'##molecule_type mRNA !'##residues 1-491 ##label SCH !'##cross-references GB:X53092; GB:X53566; NID:g62957; PIDN:CAA37258.1; !1PID:g62958 !$#accession PS0297 !'##molecule_type protein !'##residues 19-58 ##label SC2 GENETICS !$#introns 15/1; 63/3; 78/3; 115/2; 435/3 CLASSIFICATION #superfamily acetylcholine receptor KEYWORDS glycoprotein; ion channel; neurotransmitter receptor; !1postsynaptic membrane; transmembrane protein FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-491 #product nicotinic acetylcholine receptor nonalpha !8chain #status experimental #label MAT\ !$228-251 #domain transmembrane #status predicted #label TM1\ !$259-277 #domain transmembrane #status predicted #label TM2\ !$293-314 #domain transmembrane #status predicted #label TM3\ !$450-468 #domain transmembrane #status predicted #label TM4\ !$44,161 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$148-162 #disulfide_bonds #status predicted SUMMARY #length 491 #molecular-weight 56032 #checksum 9040 SEQUENCE /// ENTRY ACFFA1 #type complete TITLE nicotinic acetylcholine receptor alpha-1 chain precursor - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 21-Jun-2002 ACCESSIONS S00381; A38801 REFERENCE S00381 !$#authors Bossy, B.; Ballivet, M.; Spierer, P. !$#journal EMBO J. (1988) 7:611-618 !$#title Conservation of neural nicotinic acetylcholine receptors !1from Drosophila to vertebrate central nervous systems. !$#cross-references MUID:88283626; PMID:2840281 !$#accession S00381 !'##molecule_type DNA !'##residues 1-567 ##label BOS !'##cross-references GB:X07194; NID:g7575; PIDN:CAA30172.1; PID:g7576 !$#accession A38801 !'##molecule_type mRNA !'##residues 1-567 ##label BO2 !'##cross-references EMBL:X07194; NID:g7575; PIDN:CAA30172.1; PID:g7576 !'##note 538-Tyr was also found GENETICS !$#gene FlyBase:nAcR-alpha-96Aa !'##cross-references FlyBase:FBgn0000036 !$#map_position 3R 96A !$#introns 64/3; 79/3; 116/2; 176/3; 330/2; 401/1; 499/3 CLASSIFICATION #superfamily acetylcholine receptor KEYWORDS glycoprotein; ion channel; neurotransmitter receptor; !1postsynaptic membrane; transmembrane protein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-567 #product nicotinic acetylcholine receptor alpha-like !8chain #status predicted #label MAT\ !$22-240 #domain extracellular #status predicted #label EXT\ !$240-264 #domain transmembrane #status predicted #label TM1\ !$272-290 #domain transmembrane #status predicted #label TM2\ !$306-325 #domain transmembrane #status predicted #label TM3\ !$326-513 #domain intracellular #status predicted #label INT\ !$514-532 #domain transmembrane #status predicted #label TM4\ !$45,233 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$149-163,222-223 #disulfide_bonds #status predicted SUMMARY #length 567 #molecular-weight 64016 #checksum 4428 SEQUENCE /// ENTRY ACFFA2 #type complete TITLE nicotinic acetylcholine receptor alpha-2 chain precursor - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 21-Jun-2002 ACCESSIONS S11679; S10306; S11084 REFERENCE S11679 !$#authors Sawruk, E.; Schloss, P.; Betz, H.; Schmitt, B. !$#journal EMBO J. (1990) 9:2671-2677 !$#title Heterogeneity of Drosophila nicotinic acetylcholine !1receptors: SAD, a novel developmentally regulated !1alpha-subunit. !$#cross-references MUID:90360975; PMID:1697262 !$#accession S11679 !'##molecule_type mRNA !'##residues 1-576 ##label SAW !'##cross-references EMBL:X53583; NID:g8532; PIDN:CAA37652.1; PID:g8533 !'##note 232-Ile was also found REFERENCE S10306 !$#authors Baumann, A.; Jonas, P.; Gundelfinger, E.D. !$#journal Nucleic Acids Res. (1990) 18:3640 !$#title Sequence of D-alpha-2, a novel alpha-like subunit of !1Drosophila nicotinic acetylcholine receptors. !$#cross-references MUID:90301489; PMID:2114015 !$#accession S10306 !'##molecule_type mRNA !'##residues 1-576 ##label BAU !'##cross-references EMBL:X52274; NID:g7802; PIDN:CAA36517.1; PID:g7803 REFERENCE S11084 !$#authors Jonas, P.; Baumann, A.; Merz, B.; Gundelfinger, E.D. !$#journal FEBS Lett. (1990) 269:264-268 !$#title Structure and developmental expression of the D-alpha-2 gene !1encoding a novel nicotinic acetylcholine receptor protein of !1Drosophila melanogaster. !$#cross-references MUID:90353591; PMID:2117557 !$#accession S11084 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 42-90,'I',92-576 ##label JON GENETICS !$#gene FlyBase:nAcR-alpha-96Ab !'##cross-references FlyBase:FBgn0000039 !$#map_position 3R 96A !$#introns 84/3; 136/2; 196/3; 250/1; 445/2; 512/3 CLASSIFICATION #superfamily acetylcholine receptor KEYWORDS glycoprotein; ion channel; neurotransmitter receptor; !1postsynaptic membrane; transmembrane protein FEATURE !$1-41 #domain signal sequence #status predicted #label SIG\ !$42-576 #product nicotinic acetylcholine receptor alpha-2 !8chain #status predicted #label MAT\ !$42-260 #domain extracellular #status predicted #label EXT\ !$261-287 #domain transmembrane #status predicted #label TM1\ !$293-311 #domain transmembrane #status predicted #label TM2\ !$327-348 #domain transmembrane #status predicted #label TM3\ !$349-526 #domain intracellular #status predicted #label INT\ !$527-545 #domain transmembrane #status predicted #label TM4\ !$65,254,570 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$169-183 #disulfide_bonds #status predicted SUMMARY #length 576 #molecular-weight 65506 #checksum 7983 SEQUENCE /// ENTRY ACFFNN #type complete TITLE nicotinic acetylcholine receptor nonalpha chain precursor - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 22-Jun-1999 ACCESSIONS S03012; A38064; A26313; A28126; A38759 REFERENCE S03012 !$#authors Sawruk, E.; Hermans-Borgmeyer, I.; Betz, H.; Gundelfinger, !1E.D. !$#journal FEBS Lett. (1988) 235:40-46 !$#title Characterization of an invertebrate nicotinic acetylcholine !1receptor gene: the ard gene of Drosophila melanogaster. !$#cross-references MUID:88296842; PMID:3136037 !$#accession S03012 !'##molecule_type DNA !'##residues 1-521 ##label SAW !'##cross-references EMBL:X07956; NID:g7602; PIDN:CAA30778.1; !1PID:g1065712 !$#accession A38064 !'##molecule_type mRNA !'##residues 1-55,'G',57-72,'V',74-521 ##label SAW2 REFERENCE A26313 !$#authors Hermans-Borgmeyer, I.; Zopf, D.; Ryseck, R.P.; Hovemann, B.; !1Betz, H.; Gundelfinger, E.D. !$#journal EMBO J. (1986) 5:1503-1508 !$#title Primary structure of a developmentally regulated nicotinic !1acetylcholine receptor protein from Drosophila. !$#accession A26313 !'##molecule_type mRNA !'##residues 1-72,'V',74-521 ##label HER !'##cross-references EMBL:X04016; NID:g7537; PIDN:CAA27641.1; PID:g7538 REFERENCE A28126 !$#authors Wadsworth, S.C.; Rosenthal, L.S.; Kammermeyer, K.L.; Potter, !1M.B.; Nelson, D.J. !$#journal Mol. Cell. Biol. (1988) 8:778-785 !$#title Expression of a Drosophila melanogaster acetylcholine !1receptor-related gene in the central nervous system. !$#cross-references MUID:88174720; PMID:2832736 !$#accession A28126 !'##molecule_type mRNA !'##residues 1-521 ##label WAD !'##cross-references EMBL:M20316 GENETICS !$#gene ard !'##cross-references FlyBase:FBgn0000038 !$#map_position 3L 64B/C !$#introns 22/1; 67/3; 119/2; 267/3; 467/3 CLASSIFICATION #superfamily acetylcholine receptor KEYWORDS glycoprotein; ion channel; neurotransmitter receptor; !1postsynaptic membrane; transmembrane protein FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-521 #product nicotinic acetylcholine receptor nonalpha !8chain #status predicted #label MAT\ !$25-236 #domain extracellular #status predicted #label EXT\ !$237-260 #domain transmembrane #status predicted #label TM1\ !$268-285 #domain transmembrane #status predicted #label TM2\ !$302-323 #domain transmembrane #status predicted #label TM3\ !$324-481 #domain intracellular #status predicted #label INT\ !$482-500 #domain transmembrane #status predicted #label TM4\ !$48 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$152-166 #disulfide_bonds #status predicted SUMMARY #length 521 #molecular-weight 59915 #checksum 6642 SEQUENCE /// ENTRY ACRYB1 #type complete TITLE nicotinic acetylcholine receptor beta chain precursor - Pacific electric ray ORGANISM #formal_name Torpedo californica #common_name Pacific electric ray DATE 30-Apr-1982 #sequence_revision 05-Apr-1983 #text_change 22-Jun-1999 ACCESSIONS A93294; A94250; B33555; B54233; A03171 REFERENCE A93294 !$#authors Noda, M.; Takahashi, H.; Tanabe, T.; Toyosato, M.; !1Kikyotani, S.; Hirose, T.; Asai, M.; Takashima, H.; Inayama, !1S.; Miyata, T.; Numa, S. !$#journal Nature (1983) 301:251-255 !$#title Primary structures of beta- and delta-subunit precursors of !1Torpedo californica acetylcholine receptor deduced from cDNA !1sequences. !$#cross-references MUID:83115267; PMID:6687403 !$#accession A93294 !'##molecule_type mRNA !'##residues 1-493 ##label NOD !'##cross-references GB:J00964; GB:M14811; NID:g213221; PIDN:AAA49274.1; !1PID:g213222 !'##note the sequence from a second clone differs from that shown in !1having 3-Asp and 11-Val REFERENCE A94250 !$#authors Raftery, M.A.; Hunkapiller, M.W.; Strader, C.D.; Hood, L.E. !$#journal Science (1980) 208:1454-1457 !$#title Acetylcholine receptor: complex of homologous subunits. !$#cross-references MUID:80213767; PMID:7384786 !$#accession A94250 !'##molecule_type protein !'##residues 25-74,'R',76-78 ##label RAF REFERENCE A33555 !$#authors Moore, C.R.; Yates III, J.R.; Griffin, P.R.; Shabanowitz, !1J.; Martino, P.A.; Hunt, D.F.; Cafiso, D.S. !$#journal Biochemistry (1989) 28:9184-9191 !$#title Proteolytic fragments of the nicotinic acetylcholine !1receptor identified by mass spectrometry: implications for !1receptor topography. !$#cross-references MUID:90105466; PMID:2605252 !$#accession B33555 !'##status preliminary !'##molecule_type protein !'##residues 25-42;57-70;89-100;172-191;196-206;375-433 ##label MOO REFERENCE A54233 !$#authors Blanton, M.P.; Cohen, J.B. !$#journal Biochemistry (1994) 33:2859-2872 !$#title Identifying the lipid-protein interface of the Torpedo !1nicotinic acetylcholine receptor: secondary structure !1implications. !$#cross-references MUID:94176477; PMID:8130199 !$#accession B54233 !'##status preliminary !'##molecule_type protein !'##residues 297-325;451-480 ##label BLA COMPLEX heterotetramer of two alpha chains (see PIR:ACRYA1), one !1beta chain, one gamma chain (see PIR:ACRYG1), and one delta !1chain (see PIR:ACRYD1) CLASSIFICATION #superfamily acetylcholine receptor KEYWORDS ion channel; membrane protein; neurotransmitter receptor; !1phosphoprotein; postsynaptic membrane FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-493 #product nicotinic acetylcholine receptor beta chain !8#status predicted #label MAT\ !$242-265 #domain transmembrane #status predicted #label TR1\ !$273-291 #domain transmembrane #status predicted #label TR2\ !$303-330 #domain transmembrane #status predicted #label TR3\ !$462-480 #domain transmembrane #status predicted #label TR4 SUMMARY #length 493 #molecular-weight 56156 #checksum 3569 SEQUENCE /// ENTRY ACCHG1 #type complete TITLE nicotinic acetylcholine receptor gamma chain precursor - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 23-Feb-1997 ACCESSIONS A03172 REFERENCE A94025 !$#authors Nef, P.; Mauron, A.; Stalder, R.; Alliod, C.; Ballivet, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:7975-7979 !$#title Structure, linkage, and sequence of the two genes encoding !1the delta and gamma subunits of the nicotinic acetylcholine !1receptor. !$#cross-references MUID:85088531; PMID:6096871 !$#accession A03172 !'##molecule_type DNA !'##residues 1-514 ##label NEF !'##note the authors translated the codon CGT for residue 422 as Cys GENETICS !$#introns 19/1; 65/3; 80/3; 117/2; 169/2; 202/1; 270/1; 308/2; 346/3; !1415/1; 459/3 CLASSIFICATION #superfamily acetylcholine receptor KEYWORDS glycoprotein; ion channel; neurotransmitter receptor; !1phosphoprotein; postsynaptic membrane; transmembrane protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-514 #product acetylcholine receptor gamma chain #status !8predicted #label MAT\ !$242-268 #domain transmembrane #status predicted #label TM1\ !$275-293 #domain transmembrane #status predicted #label TM2\ !$309-330 #domain transmembrane #status predicted #label TM3\ !$474-497 #domain transmembrane #status predicted #label TM4\ !$150-164 #disulfide_bonds #status predicted\ !$163,329,449 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 514 #molecular-weight 58978 #checksum 1860 SEQUENCE /// ENTRY ACRYG1 #type complete TITLE nicotinic acetylcholine receptor gamma chain precursor - Pacific electric ray ORGANISM #formal_name Torpedo californica #common_name Pacific electric ray DATE 30-Apr-1982 #sequence_revision 13-Jun-1983 #text_change 22-Jun-1999 ACCESSIONS A93300; A93940; C33555; C54233; A03173 REFERENCE A93300 !$#authors Noda, M.; Takahashi, H.; Tanabe, T.; Toyosato, M.; !1Kikyotani, S.; Furutani, Y.; Hirose, T.; Takashima, H.; !1Inayama, S.; Miyata, T.; Numa, S. !$#journal Nature (1983) 302:528-532 !$#title Structural homology of Torpedo californica acetylcholine !1receptor subunits. !$#cross-references MUID:83167514; PMID:6188060 !$#accession A93300 !'##molecule_type mRNA !'##residues 1-506 ##label NOD !'##cross-references GB:J00966; GB:M14812; NID:g213225; PIDN:AAA49276.1; !1PID:g213226 REFERENCE A93940 !$#authors Claudio, T.; Ballivet, M.; Patrick, J.; Heinemann, S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:1111-1115 !$#title Nucleotide and deduced amino acid sequences of Torpedo !1californica acetylcholine receptor gamma subunit. !$#cross-references MUID:83195044; PMID:6573658 !$#accession A93940 !'##molecule_type mRNA !'##residues 1-297,'S',299-506 ##label CLA !'##cross-references GB:V01393; NID:g64393; PIDN:CAA24682.1; PID:g64394 REFERENCE A33555 !$#authors Moore, C.R.; Yates III, J.R.; Griffin, P.R.; Shabanowitz, !1J.; Martino, P.A.; Hunt, D.F.; Cafiso, D.S. !$#journal Biochemistry (1989) 28:9184-9191 !$#title Proteolytic fragments of the nicotinic acetylcholine !1receptor identified by mass spectrometry: implications for !1receptor topography. !$#cross-references MUID:90105466; PMID:2605252 !$#accession C33555 !'##status preliminary !'##molecule_type protein !'##residues 41-51;340-367;370-389,'E',390-396;407-431 ##label MOO REFERENCE A54233 !$#authors Blanton, M.P.; Cohen, J.B. !$#journal Biochemistry (1994) 33:2859-2872 !$#title Identifying the lipid-protein interface of the Torpedo !1nicotinic acetylcholine receptor: secondary structure !1implications. !$#cross-references MUID:94176477; PMID:8130199 !$#accession C54233 !'##status preliminary !'##molecule_type protein !'##residues 293-321;456-484 ##label BLA COMPLEX heterotetramer of two alpha chains (see PIR:ACRYA1), one !1beta chain (see PIR:ACRYB1), one gamma chain, and one delta !1chain (see PIR:ACRYD1) CLASSIFICATION #superfamily acetylcholine receptor KEYWORDS glycoprotein; ion channel; membrane protein; !1neurotransmitter receptor; phosphoprotein; postsynaptic !1membrane FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-506 #product nicotinic acetylcholine receptor gamma chain !8#status predicted #label MAT\ !$236-262 #domain transmembrane #status predicted #label TM1\ !$270-287 #domain transmembrane #status predicted #label TM2\ !$303-324 #domain transmembrane #status predicted #label TM3\ !$467-490 #domain transmembrane #status predicted #label TM4\ !$85,158,323,448 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$145-159 #disulfide_bonds #status predicted SUMMARY #length 506 #molecular-weight 58164 #checksum 8566 SEQUENCE /// ENTRY ACBOE #type complete TITLE nicotinic acetylcholine receptor epsilon chain precursor - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 22-Jun-1999 ACCESSIONS A03174 REFERENCE A03174 !$#authors Takai, T.; Noda, M.; Mishina, M.; Shimizu, S.; Furutani, Y.; !1Kayano, T.; Ikeda, T.; Kubo, T.; Takahashi, H.; Takahashi, !1T.; Kuno, M.; Numa, S. !$#journal Nature (1985) 315:761-764 !$#title Cloning, sequencing and expression of cDNA for a novel !1subunit of acetylcholine receptor from calf muscle. !$#cross-references MUID:85240565; PMID:3839289 !$#accession A03174 !'##molecule_type mRNA !'##residues 1-491 ##label TAK !'##cross-references GB:X02597; NID:g56; PIDN:CAA26442.1; PID:g57 COMMENT The epsilon chain can replace the gamma chain to form a !1functional receptor molecule. CLASSIFICATION #superfamily acetylcholine receptor KEYWORDS glycoprotein; ion channel; neurotransmitter receptor; !1postsynaptic membrane; transmembrane protein FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-491 #product acetylcholine receptor epsilon chain #status !8predicted #label MAT\ !$240-266 #domain transmembrane #status predicted #label TM1\ !$273-291 #domain transmembrane #status predicted #label TM2\ !$307-328 #domain transmembrane #status predicted #label TM3\ !$420-436 #domain amphipathic helix #status predicted #label !8APH\ !$457-480 #domain transmembrane #status predicted #label TM4\ !$86,161,327 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$148-162 #disulfide_bonds #status predicted SUMMARY #length 491 #molecular-weight 54564 #checksum 7419 SEQUENCE /// ENTRY ACRTE #type complete TITLE nicotinic acetylcholine receptor epsilon chain precursor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 02-Jun-2000 ACCESSIONS S01959; S03081; S13876; I70106; S34302 REFERENCE S01959 !$#authors Criado, M.; Witzemann, V.; Koenen, M.; Sakmann, B. !$#journal Nucleic Acids Res. (1988) 16:10920 !$#title Nucleotide sequence of the rat muscle acetylcholine receptor !1epsilon-subunit. !$#cross-references MUID:89083513; PMID:3205730 !$#accession S01959 !'##molecule_type mRNA !'##residues 1-493 ##label CRI !'##cross-references EMBL:X13252; NID:g55594; PIDN:CAA31628.1; !1PID:g55595 REFERENCE S03081 !$#authors Witzemann, V.; Barg, B.; Nishikawa, Y.; Sakmann, B.; Numa, !1S. !$#journal FEBS Lett. (1987) 223:104-112 !$#title Differential regulation of muscle acetylcholine receptor !1gamma- and epsilon-subunit mRNAs. !$#cross-references MUID:88030021; PMID:3666131 !$#accession S03081 !'##molecule_type DNA !'##residues 202-305 ##label WIT !'##cross-references EMBL:X06365; NID:g55586; PIDN:CAA29663.1; !1PID:g55587 REFERENCE S13872 !$#authors Witzemann, V.; Stein, E.; Barg, B.; Konno, T.; Koenen, M.; !1Kues, W.; Criado, M.; Hofmann, M.; Sakmann, B. !$#journal Eur. J. Biochem. (1990) 194:437-448 !$#title Primary structure and functional expression of the alpha-, !1beta-, gamma-, delta- and epsilon-subunits of the !1acetylcholine receptor from rat muscle. !$#cross-references MUID:91099317; PMID:1702709 !$#accession S13876 !'##status preliminary !'##molecule_type mRNA !'##residues 1-390,'SE',392-493 ##label WI2 !'##cross-references EMBL:X74836; NID:g398939; PIDN:CAA52830.1; !1PID:g398940 REFERENCE I55406 !$#authors Walke, W.; Staple, J.; Adams, L.; Gnegy, M.; Chahine, K.; !1Goldman, D. !$#journal J. Biol. Chem. (1994) 269:19447-19456 !$#title Calcium-dependent regulation of rat and chick muscle !1nicotinic acetylcholine receptor (nAChR) gene expression. !$#cross-references MUID:94308229; PMID:8034713 !$#accession I70106 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-23 ##label WAL !'##cross-references EMBL:Z23062; NID:g312342; PIDN:CAA80597.1; !1PID:g312343 !'##note submitted to the EMBL Data Library, June 1993 GENETICS !$#gene nAChR !$#introns 201/1; 268/1; 306/2 CLASSIFICATION #superfamily acetylcholine receptor KEYWORDS glycoprotein; ion channel; muscle; neurotransmitter !1receptor; postsynaptic membrane; transmembrane protein FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-493 #product nicotinic acetylcholine receptor epsilon !8chain #status predicted #label MAT\ !$21-239 #domain extracellular #status predicted #label EXT\ !$240-266 #domain transmembrane #status predicted #label TM1\ !$273-291 #domain transmembrane #status predicted #label TM2\ !$307-328 #domain transmembrane #status predicted #label TM3\ !$329-456 #domain intracellular #status predicted #label INT\ !$457-479 #domain transmembrane #status predicted #label TM4\ !$86,161,327 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$148-162 #disulfide_bonds #status predicted SUMMARY #length 493 #molecular-weight 54888 #checksum 9606 SEQUENCE /// ENTRY ACMSE #type complete TITLE nicotinic acetylcholine receptor epsilon chain precursor - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 22-Jun-1999 ACCESSIONS S13592; B33358 REFERENCE S13592 !$#authors Gardner, P.D. !$#journal Nucleic Acids Res. (1990) 18:6714 !$#title Nucleotide sequence of the epsilon-subunit of the mouse !1muscle nicotinic acetylcholine receptor. !$#cross-references MUID:91067487; PMID:2251144 !$#accession S13592 !'##molecule_type mRNA !'##residues 1-493 ##label GAR !'##cross-references EMBL:X55718; NID:g53160; PIDN:CAA39251.1; !1PID:g53161 REFERENCE A33358 !$#authors Buonanno, A.; Mudd, J.; Merlie, J.P. !$#journal J. Biol. Chem. (1989) 264:7611-7616 !$#title Isolation and characterization of the beta-and !1epsilon-subunit genes of mouse muscle acetylcholine !1receptor. !$#cross-references MUID:89214211; PMID:2708381 !$#accession B33358 !'##molecule_type DNA !'##residues 1-493 ##label BUO !'##cross-references GB:J04698; NID:g191599; PIDN:AAA37153.1; !1PID:g387086 CLASSIFICATION #superfamily acetylcholine receptor KEYWORDS glycoprotein; ion channel; muscle; neurotransmitter !1receptor; postsynaptic membrane; transmembrane protein FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-493 #product nicotinic acetylcholine receptor epsilon !8chain #status predicted #label MAT\ !$21-239 #domain extracellular #status predicted #label EXT\ !$240-266 #domain transmembrane #status predicted #label TM1\ !$273-291 #domain transmembrane #status predicted #label TM2\ !$307-328 #domain transmembrane #status predicted #label TM3\ !$329-456 #domain intracellular #status predicted #label INT\ !$457-479 #domain transmembrane #status predicted #label TM4\ !$86,161,327 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$148-162 #disulfide_bonds #status predicted SUMMARY #length 493 #molecular-weight 54914 #checksum 1794 SEQUENCE /// ENTRY ACMSD1 #type complete TITLE nicotinic acetylcholine receptor delta chain precursor - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 22-Jun-1999 ACCESSIONS A03175; I48234 REFERENCE A03175 !$#authors LaPolla, R.J.; Mayne, K.M.; Davidson, N. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:7970-7974 !$#title Isolation and characterization of a cDNA clone for the !1complete protein coding region of the delta subunit of the !1mouse acetylcholine receptor. !$#cross-references MUID:85088530; PMID:6096870 !$#accession A03175 !'##molecule_type mRNA !'##residues 1-520 ##label LAP !'##cross-references GB:K02582; NID:g191609; PIDN:AAA37157.1; !1PID:g309087 REFERENCE I48234 !$#authors Baldwin, T.J.; Burden, S.J. !$#journal J. Cell Biol. (1988) 107:2271-2279 !$#title Isolation and characterization of the mouse acetylcholine !1receptor delta subunit gene: identification of a 148-bp !1cis-acting region that confers myotube-specific expression. !$#cross-references MUID:89066892; PMID:3198687 !$#accession I48234 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-17 ##label RES !'##cross-references EMBL:X13959; NID:g49846; PIDN:CAA32140.1; !1PID:g49847 GENETICS !$#gene AChRdelta CLASSIFICATION #superfamily acetylcholine receptor KEYWORDS glycoprotein; ion channel; neurotransmitter receptor; !1phosphoprotein; postsynaptic membrane; transmembrane protein FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-520 #product acetylcholine receptor delta chain #status !8predicted #label MAT\ !$249-275 #domain transmembrane #status predicted #label TM1\ !$281-299 #domain transmembrane #status predicted #label TM2\ !$315-336 #domain transmembrane #status predicted #label TM3\ !$475-498 #domain transmembrane #status predicted #label TM4\ !$100,167,193 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$154-168 #disulfide_bonds #status predicted SUMMARY #length 520 #molecular-weight 59143 #checksum 6367 SEQUENCE /// ENTRY ACCHD1 #type complete TITLE nicotinic acetylcholine receptor delta chain precursor - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 22-Jun-1999 ACCESSIONS A03176; I50603 REFERENCE A94025 !$#authors Nef, P.; Mauron, A.; Stalder, R.; Alliod, C.; Ballivet, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:7975-7979 !$#title Structure, linkage, and sequence of the two genes encoding !1the delta and gamma subunits of the nicotinic acetylcholine !1receptor. !$#cross-references MUID:85088531; PMID:6096871 !$#accession A03176 !'##molecule_type DNA !'##residues 1-513 ##label NEF !'##cross-references GB:K02903; NID:g211060; PIDN:AAB59944.1; !1PID:g211063 REFERENCE I50603 !$#authors Wang, X.M.; Tsay, H.J.; Schmidt, J. !$#journal EMBO J. (1990) 9:783-790 !$#title Expression of the acetylcholine receptor delta-subunit gene !1in differentiating chick muscle cells is activated by an !1element that contains two 16 bp copies of a segment of the !1alpha-subunit enhancer. !$#cross-references MUID:90183977; PMID:2311580 !$#accession I50603 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-14 ##label WAN !'##cross-references EMBL:X52010; NID:g63019; PIDN:CAA36259.1; !1PID:g63020 GENETICS !$#introns 15/1; 63/3; 78/3; 115/2; 167/2; 206/1; 273/1; 310/2; 348/3; !1416/1; 453/3 CLASSIFICATION #superfamily acetylcholine receptor KEYWORDS glycoprotein; ion channel; neurotransmitter receptor; !1phosphoprotein; postsynaptic membrane; transmembrane protein FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-513 #product acetylcholine receptor delta chain #status !8predicted #label MAT\ !$245-271 #domain transmembrane #status predicted #label TM1\ !$277-295 #domain transmembrane #status predicted #label TM2\ !$311-332 #domain transmembrane #status predicted #label TM3\ !$468-491 #domain transmembrane #status predicted #label TM4\ !$88,161 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$148-162 #disulfide_bonds #status predicted SUMMARY #length 513 #molecular-weight 59011 #checksum 2408 SEQUENCE /// ENTRY ACRYD1 #type complete TITLE nicotinic acetylcholine receptor delta chain precursor - Pacific electric ray ORGANISM #formal_name Torpedo californica #common_name Pacific electric ray DATE 30-Apr-1982 #sequence_revision 05-Apr-1983 #text_change 22-Jun-1999 ACCESSIONS A03177; A34346; B39318; D33555; D54233 REFERENCE A93294 !$#authors Noda, M.; Takahashi, H.; Tanabe, T.; Toyosato, M.; !1Kikyotani, S.; Hirose, T.; Asai, M.; Takashima, H.; Inayama, !1S.; Miyata, T.; Numa, S. !$#journal Nature (1983) 301:251-255 !$#title Primary structures of beta- and delta-subunit precursors of !1Torpedo californica acetylcholine receptor deduced from cDNA !1sequences. !$#cross-references MUID:83115267; PMID:6687403 !$#accession A03177 !'##molecule_type mRNA !'##residues 1-522 ##label NOD !'##cross-references GB:J00965; GB:M14813; NID:g213223; PIDN:AAA49275.1; !1PID:g213224 REFERENCE A34346 !$#authors DiPaola, M.; Czajkowski, C.; Karlin, A. !$#journal J. Biol. Chem. (1989) 264:15457-15463 !$#title The sidedness of the COOH terminus of the acetylcholine !1receptor delta subunit. !$#cross-references MUID:89359383; PMID:2768272 !$#accession A34346 !'##status preliminary !'##molecule_type protein !'##residues 22-213,215-522 ##label DIP REFERENCE A39318 !$#authors Czajkowski, C.; Karlin, A. !$#journal J. Biol. Chem. (1991) 266:22603-22612 !$#title Agonist binding site of Torpedo electric tissue nicotinic !1acetylcholine receptor. A negatively charged region of the !1delta subunit within 0.9 nm of the alpha subunit binding !1site disulfide. !$#cross-references MUID:92042209; PMID:1939274 !$#accession B39318 !'##status preliminary !'##molecule_type protein !'##residues 22-181,185-522 ##label CZA REFERENCE A33555 !$#authors Moore, C.R.; Yates III, J.R.; Griffin, P.R.; Shabanowitz, !1J.; Martino, P.A.; Hunt, D.F.; Cafiso, D.S. !$#journal Biochemistry (1989) 28:9184-9191 !$#title Proteolytic fragments of the nicotinic acetylcholine !1receptor identified by mass spectrometry: implications for !1receptor topography. !$#cross-references MUID:90105466; PMID:2605252 !$#accession D33555 !'##status preliminary !'##molecule_type protein !'##residues 28-37;169-191;349-354;358-368,'E', !1369-377;390-406;411-416;421-456;509-522 ##label MOO REFERENCE A54233 !$#authors Blanton, M.P.; Cohen, J.B. !$#journal Biochemistry (1994) 33:2859-2872 !$#title Identifying the lipid-protein interface of the Torpedo !1nicotinic acetylcholine receptor: secondary structure !1implications. !$#cross-references MUID:94176477; PMID:8130199 !$#accession D54233 !'##molecule_type protein !'##residues 302-330 ##label BLA !'##note the periodicity of radiolabeling by a lipid-soluble, !1photoactivatable probe strongly suggests arrangment of this !1segment as a transmembrane alpha helix REFERENCE A44744 !$#authors Yee, G.H.; Huganir, R.L. !$#journal J. Biol. Chem. (1987) 262:16748-16753 !$#title Determination of the sites of cAMP-dependent phosphorylation !1on the nicotinic acetylcholine receptor. !$#cross-references MUID:88059065; PMID:3680273 !$#contents annotation; phosphorylation site REFERENCE A30648 !$#authors Strecker, A.; Franke, P.; Weise, C.; Hucho, F. !$#journal Eur. J. Biochem. (1994) 220:1005-1011 !$#title All potential glycosylation sites of the nicotinic !1acetylcholine receptor delta subunit from Torpedo !1californica are utilized. !$#cross-references MUID:94192651; PMID:8143716 !$#contents annotation; glycosylation sites COMPLEX heterotetramer of two alpha chains (see PIR:ACRYA1), one !1beta chain (see PIR:ACRYB1), one gamma chain (see !1PIR:ACRYG1), and one delta chain CLASSIFICATION #superfamily acetylcholine receptor KEYWORDS glycoprotein; ion channel; neurotransmitter receptor; !1phosphoprotein; postsynaptic membrane; transmembrane protein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-522 #product nicotinic acetylcholine receptor delta chain !8#status experimental #label MAT\ !$247-273 #domain transmembrane #status predicted #label TM1\ !$278-294 #domain transmembrane #status predicted #label TM2\ !$312-335 #domain transmembrane #status predicted #label TM3\ !$477-496 #domain transmembrane #status predicted #label TM4\ !$91,164,229 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$151-165 #disulfide_bonds #status predicted\ !$382 #binding_site phosphate (Ser) (covalent) (by !8cAMP-dependent kinase) #status experimental SUMMARY #length 522 #molecular-weight 59890 #checksum 3427 SEQUENCE /// ENTRY CHCHA1 #type complete TITLE gamma-aminobutyric acid/benzodiazepine receptor alpha-1 chain precursor - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 22-Jun-1999 ACCESSIONS A60033; S11749 REFERENCE A60033 !$#authors Bateson, A.N.; Harvey, R.J.; Wisden, W.; Glencorse, T.A.; !1Hicks, A.A.; Hunt, S.P.; Barnard, E.A.; Darlison, M.G. !$#journal Brain Res. Mol. Brain Res. (1991) 9:333-339 !$#title The chicken GABA-A receptor alpha1 subunit: cDNA sequence !1and localization of the corresponding mRNA. !$#cross-references MUID:91245932; PMID:1710013 !$#accession A60033 !'##molecule_type mRNA !'##residues 1-455 ##label BAT !'##cross-references EMBL:X54244; NID:g62900; PIDN:CAA38148.1; !1PID:g62901 CLASSIFICATION #superfamily acetylcholine receptor KEYWORDS glycoprotein; ion channel; neurotransmitter receptor; !1transmembrane protein FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-455 #product gamma-aminobutyric acid/benzodiazepine !8receptor alpha-1 chain #status predicted #label MAT\ !$28-252 #domain extracellular #status predicted #label EXT\ !$253-274 #domain transmembrane #status predicted #label TM1\ !$283-299 #domain transmembrane #status predicted #label TM2\ !$312-337 #domain transmembrane #status predicted #label TM3\ !$338-423 #domain intracellular #status predicted #label INT\ !$424-442 #domain transmembrane #status predicted #label TM4\ !$38,138 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$166-180 #disulfide_bonds #status predicted SUMMARY #length 455 #molecular-weight 51841 #checksum 5928 SEQUENCE /// ENTRY ACBOG2 #type complete TITLE gamma-aminobutyric acid/benzodiazepine receptor alpha-2 chain precursor - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 22-Jun-1999 ACCESSIONS S12510; S05580 REFERENCE S12510 !$#authors Schofield, P.R. !$#submission submitted to the EMBL Data Library, July 1988 !$#accession S12510 !'##molecule_type mRNA !'##residues 1-451 ##label SCH !'##cross-references EMBL:X12361; NID:g368; PIDN:CAA30924.1; PID:g369 REFERENCE S05580 !$#authors Levitan, E.S.; Schofield, P.R.; Burt, D.R.; Rhee, L.M.; !1Wisden, W.; Koehler, M.; Fujita, N.; Rodriguez, H.F.; !1Stephenson, A.; Darlison, M.G.; Barnard, E.A.; Seeburg, P.H. !$#journal Nature (1988) 335:76-79 !$#title Structural and functional basis for GABA(A) receptor !1heterogeneity. !$#cross-references MUID:88318951; PMID:2842688 !$#accession S05580 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-93,'T',94-451 ##label LEV !'##cross-references EMBL:X12361 !'##note part of this sequence was confirmed by protein sequencing CLASSIFICATION #superfamily acetylcholine receptor KEYWORDS glycoprotein; ion channel; neurotransmitter receptor; !1transmembrane protein FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-451 #product gamma-aminobutyric acid/benzodiazepine !8receptor alpha-2 chain #status predicted #label MAT\ !$29-252 #domain extracellular #status predicted #label EXT\ !$253-274 #domain transmembrane #status predicted #label TM1\ !$279-300 #domain transmembrane #status predicted #label TM2\ !$315-334 #domain transmembrane #status predicted #label TM3\ !$335-422 #domain intracellular #status predicted #label INT\ !$423-441 #domain transmembrane #status predicted #label TM4\ !$38,138,201 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$166-180 #disulfide_bonds #status predicted SUMMARY #length 451 #molecular-weight 51146 #checksum 9425 SEQUENCE /// ENTRY CHBOA3 #type complete TITLE gamma-aminobutyric acid/benzodiazepine receptor alpha-3 chain precursor - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 22-Jun-1999 ACCESSIONS S12511; S05581 REFERENCE S12510 !$#authors Schofield, P.R. !$#submission submitted to the EMBL Data Library, July 1988 !$#accession S12511 !'##molecule_type mRNA !'##residues 1-492 ##label SCH !'##cross-references EMBL:X12362; NID:g372; PIDN:CAA30925.1; PID:g373 REFERENCE S05580 !$#authors Levitan, E.S.; Schofield, P.R.; Burt, D.R.; Rhee, L.M.; !1Wisden, W.; Koehler, M.; Fujita, N.; Rodriguez, H.F.; !1Stephenson, A.; Darlison, M.G.; Barnard, E.A.; Seeburg, P.H. !$#journal Nature (1988) 335:76-79 !$#title Structural and functional basis for GABA(A) receptor !1heterogeneity. !$#cross-references MUID:88318951; PMID:2842688 !$#accession S05581 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-39,'E',41-420,'KGA',421-492 ##label LEV !'##cross-references EMBL:X12362 !'##note 327-Asp was also found GENETICS !$#introns 184/2; 382/3 CLASSIFICATION #superfamily acetylcholine receptor KEYWORDS glycoprotein; ion channel; neurotransmitter receptor; !1transmembrane protein FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-492 #product gamma-aminobutyric acid/benzodiazepine !8receptor alpha-3 chain #status predicted #label MAT\ !$29-277 #domain extracellular #status predicted #label EXT\ !$278-299 #domain transmembrane #status predicted #label TM1\ !$308-325 #domain transmembrane #status predicted #label TM2\ !$340-362 #domain transmembrane #status predicted #label TM3\ !$363-460 #domain intracellular #status predicted #label INT\ !$461-479 #domain transmembrane #status predicted #label TM4\ !$63,163,176,228 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$191-205 #disulfide_bonds #status predicted SUMMARY #length 492 #molecular-weight 55283 #checksum 4750 SEQUENCE /// ENTRY ACRTGT #type complete TITLE gamma-aminobutyric acid transport protein - rat ALTERNATE_NAMES GABA transporter ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 22-Jun-1999 ACCESSIONS A35918; B35918 REFERENCE A35918 !$#authors Guastella, J.; Nelson, N.; Nelson, H.; Czyzyk, L.; Keynan, !1S.; Miedel, M.C.; Davidson, N.; Lester, H.A.; Kanner, B.I. !$#journal Science (1990) 249:1303-1306 !$#title Cloning and expression of a rat brain GABA transporter. !$#cross-references MUID:90378307; PMID:1975955 !$#accession A35918 !'##molecule_type mRNA !'##residues 1-599 ##label GUA !'##cross-references GB:M59742; NID:g204221; PIDN:AAA63487.1; !1PID:g204222 !$#accession B35918 !'##molecule_type protein !'##residues 546-551;556-562;564-566;572-583 ##label GU2 CLASSIFICATION #superfamily gamma-aminobutyric acid transporter KEYWORDS brain; glycoprotein; phosphoprotein; transmembrane protein FEATURE !$53-73 #domain transmembrane #status predicted #label TM1\ !$80-100 #domain transmembrane #status predicted #label TM2\ !$124-144 #domain transmembrane #status predicted #label TM3\ !$212-230 #domain transmembrane #status predicted #label TM4\ !$239-256 #domain transmembrane #status predicted #label TM5\ !$292-312 #domain transmembrane #status predicted #label TM6\ !$322-342 #domain transmembrane #status predicted #label TM7\ !$375-394 #domain transmembrane #status predicted #label TM8\ !$427-447 #domain transmembrane #status predicted #label TM9\ !$457-477 #domain transmembrane #status predicted #label TM10\ !$498-517 #domain transmembrane #status predicted #label TM11\ !$536-556 #domain transmembrane #status predicted #label TM12\ !$24,562 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$46 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$176,181,184 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 599 #molecular-weight 67001 #checksum 2695 SEQUENCE /// ENTRY S11175 #type complete TITLE choline transport protein - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein G3213; protein YGL077c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S11175; S64084 REFERENCE S11175 !$#authors Nikawa, J.I.; Hosaka, K.; Tsukagoshi, Y.; Yamashita, S. !$#journal J. Biol. Chem. (1990) 265:15996-16003 !$#title Primary structure of the yeast choline transport gene and !1regulation of its expression. !$#cross-references MUID:90368823; PMID:2203793 !$#accession S11175 !'##molecule_type DNA !'##residues 1-563 ##label NIK !'##cross-references EMBL:J05603; NID:g171329; PIDN:AAA34537.1; !1PID:g171330 REFERENCE S64071 !$#authors Rieger, M.; Mueller-Auer, S.; Brueckner, M.; Schaefer, M. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64084 !'##molecule_type DNA !'##residues 1-563 ##label RIE !'##cross-references EMBL:Z72599; NID:g1322592; PIDN:CAA96782.1; !1PID:g1322593; GSPDB:GN00007; MIPS:YGL077c !'##experimental_source strain S288C GENETICS !$#gene SGD:HNM1; CTR1; MIPS:YGL077c !'##cross-references MIPS:YGL077c; SGD:S0003045 !$#map_position 7L CLASSIFICATION #superfamily choline transport protein KEYWORDS transmembrane protein FEATURE !$91-107 #domain transmembrane #status predicted #label TM1\ !$185-201 #domain transmembrane #status predicted #label TM2\ !$214-230 #domain transmembrane #status predicted #label TM3\ !$257-273 #domain transmembrane #status predicted #label TM4\ !$298-314 #domain transmembrane #status predicted #label TM5\ !$345-361 #domain transmembrane #status predicted #label TM6\ !$401-417 #domain transmembrane #status predicted #label TM7\ !$428-444 #domain transmembrane #status predicted #label TM8\ !$466-482 #domain transmembrane #status predicted #label TM9 SUMMARY #length 563 #molecular-weight 62055 #checksum 3948 SEQUENCE /// ENTRY S30253 #type complete TITLE GABA transport protein - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES GABA-specific permease; protein D1037; protein YDL210w ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S30253; S67769; S25147 REFERENCE S30253 !$#authors Andre, B.; Hein, C.; Grenson, M.; Jauniaux, J.C. !$#journal Mol. Gen. Genet. (1993) 237:17-25 !$#title Cloning and expression of the UGA4 gene coding for the !1inducible GABA-specific transport protein of Saccharomyces !1cerevisiae. !$#cross-references MUID:93204891; PMID:8455553 !$#accession S30253 !'##molecule_type DNA !'##residues 1-571 ##label AND !'##cross-references EMBL:X66472; NID:g4749; PIDN:CAA47101.1; PID:g4750 !'##note the sequence from Fig. 5 is inconsistent with that from Fig. 3 !1in having 527-X REFERENCE S67756 !$#authors Schmidt, E.R.; Bahr, A.; Kraemer, C.; Hankeln, T.; !1Moeller-Rieker, S. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67769 !'##molecule_type DNA !'##residues 1-571 ##label SCH !'##cross-references EMBL:Z74258; NID:g1431349; PIDN:CAA98788.1; !1PID:g1431350; GSPDB:GN00004; MIPS:YDL210w !'##experimental_source strain S288C GENETICS !$#gene SGD:UGA4; MIPS:YDL210w !'##cross-references SGD:S0002369; MIPS:YDL210w !$#map_position 4L CLASSIFICATION #superfamily choline transport protein KEYWORDS transmembrane protein FEATURE !$79-95 #domain transmembrane #status predicted #label TM1\ !$108-124 #domain transmembrane #status predicted #label TM2\ !$154-170 #domain transmembrane #status predicted #label TM3\ !$203-219 #domain transmembrane #status predicted #label TM4\ !$229-245 #domain transmembrane #status predicted #label TM5\ !$320-336 #domain transmembrane #status predicted #label TM6\ !$365-381 #domain transmembrane #status predicted #label TM7\ !$420-436 #domain transmembrane #status predicted #label TM8\ !$485-501 #domain transmembrane #status predicted #label TM9 SUMMARY #length 571 #molecular-weight 61872 #checksum 134 SEQUENCE /// ENTRY S38004 #type complete TITLE probable transport protein YKL174c - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES probable transport protein YKL639 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S38004; S44586; S38406 REFERENCE S37976 !$#authors Vandenbol, M.; Bolle, P.A.; Dion, C.; Portetelle, D.; !1Hilger, F. !$#submission submitted to the Protein Sequence Database, March 1994 !$#accession S38004 !'##molecule_type DNA !'##residues 1-618 ##label VAN !'##cross-references EMBL:Z28174; NID:g486305; PIDN:CAA82016.1; !1PID:g486306; GSPDB:GN00011; MIPS:YKL174c !'##experimental_source strain S288C REFERENCE S44583 !$#authors Vandenbol, M.; Bolle, P.A.; Dion, C.; Portetelle, D.; !1Hilger, F. !$#journal Yeast (1994) 10:25-33 !$#title Sequencing and analysis of a 20.5 kb DNA segment located on !1the left arm of yeast chromosome XI. !$#accession S44586 !'##status translation not shown !'##molecule_type DNA !'##residues 1-618 ##label VA2 !'##cross-references EMBL:Z26878; NID:g407503; PIDN:CAA81512.1; !1PID:g407507 !'##experimental_source strain S288C GENETICS !$#gene MIPS:YKL174c !'##cross-references SGD:S0001657 !$#map_position 11L CLASSIFICATION #superfamily choline transport protein KEYWORDS transmembrane protein SUMMARY #length 618 #molecular-weight 69242 #checksum 6264 SEQUENCE /// ENTRY CHRBA2 #type complete TITLE calcium channel protein alpha-2 chain precursor - rabbit ALTERNATE_NAMES dihydropyridine-binding protein, 140K ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 22-Jun-1999 ACCESSIONS S10579; A39518; A33409 REFERENCE S10579 !$#authors Ellis, S.B.; Williams, M.E.; Ways, N.R.; Brenner, R.; Sharp, !1A.H.; Leung, A.T.; Campbell, K.P.; McKenna, E.; Koch, W.J.; !1Hui, A.; Schwartz, A.; Harpold, M.M. !$#journal Science (1988) 241:1661-1664 !$#title Sequence and expression of mRNAs encoding the alpha(1) and !1alpha(2) subunits of a DHP-sensitive calcium channel. !$#cross-references MUID:88336904; PMID:2458626 !$#accession S10579 !'##molecule_type mRNA !'##residues 1-1106 ##label ELL !'##cross-references EMBL:M21948; NID:g164762; PIDN:AAA81562.1; !1PID:g164763 !'##note 57-Asn, 106-Lys, and deletion of 620-Ser were also found REFERENCE A39518 !$#authors Jay, S.D.; Sharp, A.H.; Kahl, S.D.; Vedvick, T.S.; Harpold, !1M.M.; Campbell, K.P. !$#journal J. Biol. Chem. (1991) 266:3287-3293 !$#title Structural characterization of the dihydropyridine-sensitive !1calcium channel alpha-2-subunit and the associated delta !1peptides. !$#cross-references MUID:91131638; PMID:1847144 !$#accession A39518 !'##molecule_type protein !'##residues 961-973 ##label JAY !'##note this sequence represents the amino end of a glycosylated !1peptide that appears after reduction of disulfide bonds in !1the mature protein; several forms (25K, 22K, and 17K) have a !1common sequence at the amino end and identical molecular !1weights (17K) following deglycosylation REFERENCE A33409 !$#authors Hamilton, S.L.; Hawkes, M.J.; Brush, K.; Cook, R. !$#journal Biochemistry (1989) 28:7820-7828 !$#title Subunit composition of the purified dihydropyridine binding !1protein from skeletal muscle. !$#cross-references MUID:90122765; PMID:2558713 !$#accession A33409 !'##status preliminary !'##molecule_type protein !'##residues 27-44,'S',46-47 ##label HAM CLASSIFICATION #superfamily calcium channel alpha-2 chain KEYWORDS calcium; disulfide bond; glycoprotein; ion channel; membrane !1protein; phosphoprotein FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-1106 #product calcium channel alpha-2 chain #status !8predicted #label MAT\ !$94,138,186,326,350, !$470,477,606,615, !$678,697,784,827, !$891,898,988,1001, !$1081 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1106 #molecular-weight 125041 #checksum 5618 SEQUENCE /// ENTRY A44361 #type complete TITLE amiloride-sensitive sodium channel Apx protein - African clawed frog ALTERNATE_NAMES apical plasma membrane protein ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 30-Apr-1993 #sequence_revision 19-Oct-1995 #text_change 22-Jun-1999 ACCESSIONS A44361; S25517 REFERENCE A44361 !$#authors Staub, O.; Verrey, F.; Kleyman, T.R.; Benos, D.J.; Rossier, !1B.C.; Kraehenbuhl, J.P. !$#journal J. Cell Biol. (1992) 119:1497-1506 !$#title Primary structure of an apical protein from Xenopus laevis !1that participates in amiloride-sensitive sodium channel !1activity. !$#cross-references MUID:93107151; PMID:1334959 !$#accession A44361 !'##molecule_type mRNA !'##residues 1-1420 ##label STA !'##cross-references EMBL:Z14997; NID:g64551; PIDN:CAA78718.1; !1PID:g64552 !'##experimental_source A6 cells !'##note sequence extracted from NCBI backbone (NCBIP:121141) COMPLEX This protein is part of a large molecular complex. FUNCTION !$#description may be the amiloride-sensitive component of the !1amiloride-sensitive sodium channel CLASSIFICATION #superfamily amiloride-sensitive sodium channel Apx protein KEYWORDS glycoprotein; membrane-associated protein; sodium transport FEATURE !$119,462,481,503, !$660,664,988,1038, !$1211,1273 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1420 #molecular-weight 159467 #checksum 6152 SEQUENCE /// ENTRY CHEE #type complete TITLE sodium channel protein - electric eel ORGANISM #formal_name Electrophorus electricus #common_name electric eel DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 22-Jun-1999 ACCESSIONS A03178; I50536 REFERENCE A03178 !$#authors Noda, M.; Shimizu, S.; Tanabe, T.; Takai, T.; Kayano, T.; !1Ikeda, T.; Takahashi, H.; Nakayama, H.; Kanaoka, Y.; !1Minamino, N.; Kangawa, K.; Matsuo, H.; Raftery, M.A.; !1Hirose, T.; Inayama, S.; Hayashida, H.; Miyata, T.; Numa, S. !$#journal Nature (1984) 312:121-127 !$#title Primary structure of Electrophorus electricus sodium channel !1deduced from cDNA sequence. !$#cross-references MUID:85061498; PMID:6209577 !$#accession A03178 !'##molecule_type mRNA !'##residues 1-1820 ##label NOD !'##cross-references GB:X01119; NID:g62776; PIDN:CAA25587.1; PID:g62777 REFERENCE I50536 !$#authors Noda, M.; Numa, S. !$#journal J. Recept. Res. (1987) 7:467-497 !$#title Structure and function of sodium channel. !$#cross-references MUID:87311395; PMID:2442385 !$#accession I50536 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-1820 ##label NO2 !'##cross-references GB:M22252; NID:g1041048; PIDN:AAA79960.1; !1PID:g1041049 COMMENT This membrane glycoprotein mediates the voltage-dependent !1sodium-ion permeability of excitable membranes. Assuming !1opened or closed conformations in response to the voltage !1difference across the membrane, the protein forms a !1sodium-selective channel through which sodium ions may pass !1in accordance with their electrochemical gradient. COMMENT This sequence contains four highly homologous internal !1repeats (excluding residues 285-342, 1172-1194, and !11490-1505, the nonhomologous segments from repeats I, III, !1and IV, respectively). Each repeat has a similar overall !1structure containing six subregions located in identical !1positions. Two of these regions are highly hydrophobic (S5, !1S6), two have a net negative charge (S1,S3), one has a net !1positive charge (S4), and one is neutral (S2). COMMENT The four repeating units are thought to be oriented !1pseudosymmetrically across the membrane, surrounding the !1channel, with segments S1, S2, S5, and S6 of each repeat !1traversing the membrane. The presence of four homologous !1structures within this molecule is consistent with the !1sigmoidal kinetics characteristic of this channel. COMMENT Available data suggest that activation and inactivation !1gates are located near the cytoplasmic surface of the !1membrane. It is hypothesized that residues 802-806, 847-857, !1894-910, and 942-955 might, in conjunction with the !1positively charged residues of S4, act as a voltage sensor !1involved with the activation gate. CLASSIFICATION #superfamily sodium channel protein KEYWORDS duplication; glycoprotein; ion transport; membrane protein; !1sodium channel; voltage-gated ion channel FEATURE !$111-419,555-807, !$989-1281,1311-1587 #region duplication internal repeats I, II, III and !8IV\ !$111-141,555-585, !$989-1019,1311-1341 #region S1 of repeats I through IV\ !$150-171,597-620, !$1033-1057,1353-1376 #region S2 of repeats I through IV\ !$177-197,626-643, !$1062-1079,1381-1398 #region S3 of repeats I through IV\ !$204-224,651-671, !$1092-1112,1417-1437 #region S4 of repeats I through IV\ !$244-264,691-711, !$1132-1152,1454-1474 #region S5 of repeats I through IV\ !$379-402,767-790, !$1236-1264,1544-1567 #region S6 of repeats I through IV\ !$205,278,288,317, !$591,690,797,1160, !$1174,1806 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1820 #molecular-weight 208330 #checksum 443 SEQUENCE /// ENTRY CHRTM1 #type complete TITLE sodium channel protein mu1 alpha chain, skeletal muscle - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 22-Jun-1999 ACCESSIONS JN0007 REFERENCE JN0007 !$#authors Trimmer, J.S.; Cooperman, S.S.; Tomiko, S.A.; Zhou, J.; !1Crean, S.M.; Boyle, M.B.; Kallen, R.G.; Sheng, Z.; Barchi, !1R.L.; Sigworth, F.J.; Goodman, R.H.; Agnew, W.S.; Mandel, G. !$#journal Neuron (1989) 3:33-49 !$#title Primary structure and functional expression of a mammalian !1skeletal muscle sodium channel. !$#cross-references MUID:90148778; PMID:2559760 !$#accession JN0007 !'##molecule_type mRNA !'##residues 1-1840 ##label TRI !'##cross-references GB:M26643; NID:g205651; PIDN:AAA41682.1; !1PID:g205652 COMMENT Action potentials propagated by skeletal muscle sodium !1channels are responsible for the spread of excitation from !1the neuromuscular junction. COMMENT This heavily glycosylated protein contains four homologous !1domains, each of which is predicted to have several !1membrane-spanning segments. COMMENT This protein is distinct from but related to sodium channel !1proteins isolated from brain. CLASSIFICATION #superfamily sodium channel protein KEYWORDS duplication; glycoprotein; ion transport; neuromuscular !1junction; phosphoprotein; skeletal muscle; sodium channel; !1transmembrane protein FEATURE !$120-458,561-813, !$1013-1305,1335-1611 #region duplication\ !$56,251,1321,1504 #binding_site phosphate (Ser) (covalent) (by !8cAMP-dependent kinase) #status predicted\ !$214,288,291,297, !$303,309,315,327, !$356,502,696,954, !$1184,1198,1563,1702 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1840 #molecular-weight 208865 #checksum 5582 SEQUENCE /// ENTRY CHRTD1 #type complete TITLE potassium channel protein drk1 - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 22-Jun-1999 ACCESSIONS S05448; A44838 REFERENCE S05448 !$#authors Frech, G.C.; VanDongen, A.M.J.; Schuster, G.; Brown, A.M.; !1Joho, R.H. !$#journal Nature (1989) 340:642-645 !$#title A novel potassium channel with delayed rectifier properties !1isolated from rat brain by expression cloning. !$#cross-references MUID:89365157; PMID:2770868 !$#accession S05448 !'##molecule_type mRNA !'##residues 1-853 ##label FRE !'##cross-references EMBL:X16476; NID:g57785; PIDN:CAA34497.1; !1PID:g57786 !'##note it is uncertain whether Met-1 or Met-17 is the initiator REFERENCE A44838 !$#authors Drewe, J.A.; Verma, S.; Frech, G.; Joho, R.H. !$#journal J. Neurosci. (1992) 12:538-548 !$#title Distinct spatial and temporal expression patterns of K+ !1channel mRNAs from different subfamilies. !$#cross-references MUID:92156897; PMID:1740690 !$#accession A44838 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 'MPAG',1-571 ##label DRE !'##cross-references GB:M81783; NID:g205038 !'##experimental_source brain !'##note sequence extracted from NCBI backbone (NCBIP:81768) GENETICS !$#gene drk1 CLASSIFICATION #superfamily potassium channel protein drk1 KEYWORDS glycoprotein; ion channel; phosphoprotein; potassium !1channel; transmembrane protein FEATURE !$1-182 #domain intracellular #status predicted #label INT1\ !$183-204 #domain transmembrane #status predicted #label TM1\ !$225-245 #domain transmembrane #status predicted #label TM2\ !$256-276 #domain transmembrane #status predicted #label TM3\ !$291-312 #domain transmembrane #status predicted #label TM4\ !$327-348 #domain transmembrane #status predicted #label TM5\ !$389-410 #domain transmembrane #status predicted #label TM6\ !$411-853 #domain intracellular #status predicted #label INT2\ !$279 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 853 #molecular-weight 95280 #checksum 1721 SEQUENCE /// ENTRY PWBYH #type complete TITLE potassium transport protein TRK1, high-affinity - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein J0693; protein YJL129c ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 12-Nov-1999 ACCESSIONS S05849; S56910 REFERENCE S05849 !$#authors Gaber, R.F.; Styles, C.A.; Fink, G.R. !$#journal Mol. Cell. Biol. (1988) 8:2848-2859 !$#title TRK1 encodes a plasma membrane protein required for !1high-affinity potassium transport in Saccharomyces !1cerevisiae. !$#cross-references MUID:88302204; PMID:3043197 !$#accession S05849 !'##molecule_type DNA !'##residues 1-1235 ##label GAB !'##cross-references EMBL:M21328; NID:g171803; PIDN:AAA34728.1; !1PID:g171804 REFERENCE S56891 !$#authors Cziepluch, C.; Kordes, E.; Pujol, A.; Jauniaux, J.C. !$#submission submitted to the Protein Sequence Database, September 1995 !$#accession S56910 !'##molecule_type DNA !'##residues 1-1235 ##label CZI !'##cross-references EMBL:Z49404; NID:g1008329; PIDN:CAA89424.1; !1PID:g1008330; GSPDB:GN00010; MIPS:YJL129c GENETICS !$#gene SGD:TRK1; MIPS:YJL129c !'##cross-references SGD:S0003665; MIPS:YJL129c !$#map_position 10L CLASSIFICATION #superfamily potassium transport protein TRK1 KEYWORDS ion transport; potassium transport; transmembrane protein FEATURE !$50-70 #domain transmembrane #status predicted #label TM01\ !$72-96 #domain transmembrane #status predicted #label TM02\ !$107-127 #domain transmembrane #status predicted #label TM03\ !$778-800 #domain transmembrane #status predicted #label TM04\ !$812-834 #domain transmembrane #status predicted #label TM05\ !$839-859 #domain transmembrane #status predicted #label TM06\ !$862-882 #domain transmembrane #status predicted #label TM07\ !$898-918 #domain transmembrane #status predicted #label TM08\ !$923-943 #domain transmembrane #status predicted #label TM09\ !$972-991 #domain transmembrane #status predicted #label TM10\ !$1079-1096 #domain transmembrane #status predicted #label TM11\ !$1111-1132 #domain transmembrane #status predicted #label TM12\ !$738 #binding_site ATP (Lys) #status predicted SUMMARY #length 1235 #molecular-weight 141072 #checksum 8721 SEQUENCE /// ENTRY H64428 #type complete TITLE magnesium and cobalt transport protein homolog - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS H64428 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession H64428 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-317 ##label BUL !'##cross-references GB:U67546; GB:L77117; NID:g1591687; !1PIDN:AAB99037.1; PID:g1499876; TIGR:MJ1033 GENETICS !$#map_position FOR965089-966042 CLASSIFICATION #superfamily magnesium and cobalt transport protein SUMMARY #length 317 #molecular-weight 37141 #checksum 1677 SEQUENCE /// ENTRY EPFF #type complete TITLE zip protein precursor - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES zipper protein ORGANISM #formal_name Drosophila melanogaster DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 22-Jun-1999 ACCESSIONS S00483; A37532 REFERENCE S00483 !$#authors Zhao, D.B.; Cote, S.; Jaehnig, F.; Haller, J.; Jaeckle, H. !$#journal EMBO J. (1988) 7:1115-1119 !$#title Zipper encodes a putative integral membrane protein required !1for normal axon patterning during Drosophila neurogenesis. !$#cross-references MUID:88296414; PMID:3402433 !$#accession S00483 !'##molecule_type DNA !'##residues 1-500 ##label ZHA !'##cross-references GB:X07450; NID:g8854; PIDN:CAA30332.1; PID:g8855 !$#accession A37532 !'##molecule_type mRNA !'##residues 1-500 ##label ZHA1 !'##cross-references EMBL:X07450; NID:g8854; PIDN:CAA30332.1; PID:g8855 GENETICS !$#gene zip !'##cross-references FlyBase:FBgn0004055 !$#introns 237/1; 354/1 CLASSIFICATION #superfamily zip protein KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-500 #product zip protein #status predicted #label MAT\ !$22-470 #domain extracellular #status predicted #label EXT\ !$466-486 #domain transmembrane #status predicted #label TMM\ !$496-500 #domain intracellular #status predicted #label INT\ !$35,232,317,374,448 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 500 #molecular-weight 55814 #checksum 6533 SEQUENCE /// ENTRY EPBO #type complete TITLE phosphatidylcholine transfer protein - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Aug-1980 #sequence_revision 22-May-1981 #text_change 22-Jun-1999 ACCESSIONS A91092; A91105; A91260; S68244; A03179; S57929 REFERENCE A91092 !$#authors Moonen, P.; Akeroyd, R.; Westerman, J.; Puyk, W.C.; Smits, !1P.; Wirtz, K.W.A. !$#journal Eur. J. Biochem. (1980) 106:279-290 !$#title The primary structure of the phosphatidylcholine-exchange !1protein from bovine liver. Isolation and characterization of !1the staphylococcal protease peptides and the amino-acid !1sequence of the N-terminal half (residues 1-122). !$#cross-references MUID:82186640; PMID:7042332 !$#accession A91092 !'##molecule_type protein !'##residues 1-122 ##label MO1 REFERENCE A91105 !$#authors Akeroyd, R.; Moonen, P.; Westerman, J.; Puyk, W.C.; Wirtz, !1K.W.A. !$#journal Eur. J. Biochem. (1981) 114:385-391 !$#title The complete primary structure of the !1phosphatidylcholine-transfer protein from bovine liver. !1Isolation and characterization of the cyanogen bromide !1peptides. !$#cross-references MUID:81164528; PMID:7011810 !$#accession A91105 !'##molecule_type protein !'##residues 110-213 ##label AKE REFERENCE A91260 !$#authors Moonen, P.; Haagsman, H.P.; van Deenen, L.L.M.; Wirtz, !1K.W.A. !$#journal Eur. J. Biochem. (1979) 99:439-445 !$#title Determination of the hydrophobic binding site of !1phosphatidylcholine exchange protein with photosensitive !1phosphatidylcholine. !$#cross-references MUID:80046712; PMID:499208 !$#accession A91260 !'##molecule_type protein !'##residues 146-183 ##label MO2 !'##note residues 171-176 form part of the binding site for !1phosphatidylcholine REFERENCE S68244 !$#authors Geijtenbeek, T.B.H.; Smith, A.J.; Borst, P.; Wirtz, K.W.A. !$#journal Biochem. J. (1996) 316:49-55 !$#title cDNA cloning and tissue-specific expression of the !1phosphatidylcholine transfer protein gene. !$#cross-references MUID:96235171; PMID:8645232 !$#accession S68244 !'##molecule_type mRNA !'##residues 1-166,'K',168-213 ##label GEI !'##cross-references EMBL:Z50026; NID:g897692; PIDN:CAA90330.1; !1PID:g897693 !'##note experimental_source liver COMMENT The unique property of this protein is to extract !1phosphatidylcholine from an interface. CLASSIFICATION #superfamily phosphatidylcholine-transfer protein KEYWORDS acetylated amino end FEATURE !$1 #modified_site acetylated amino end (Met) #status !8experimental\ !$17-63,93-207 #disulfide_bonds #status experimental SUMMARY #length 213 #molecular-weight 24643 #checksum 4663 SEQUENCE /// ENTRY I53775 #type complete TITLE phosphatidylinositol transfer protein alpha - human ORGANISM #formal_name Homo sapiens #common_name man DATE 19-May-2000 #sequence_revision 19-May-2000 #text_change 19-May-2000 ACCESSIONS I53775 REFERENCE I53775 !$#authors Dickeson, S.K.; Helmkamp, G.M. !$#journal Gene (1994) 142:301-305 !$#title Sequence of a human cDNA encoding phosphatidylinositol !1transfer protein and occurrence of a related sequence in !1widely dibergent eukaryotes. !$#cross-references MUID:94252585; PMID:8194769 !$#accession I53775 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-270 ##label RES !'##cross-references GB:M73704; NID:g189938; PIDN:AAA36441.1; !1PID:g189939 GENETICS !$#gene GDB:PITPN !'##cross-references GDB:306573; OMIM:600174 !$#map_position 17p13.3-17p13.3 CLASSIFICATION #superfamily human phosphatidylinositol transfer protein KEYWORDS phospholipid binding; phospholipid transport FEATURE !$2-270 #product phosphatidylinositol transfer protein !8#status predicted #label MAT SUMMARY #length 270 #molecular-weight 31806 #checksum 2600 SEQUENCE /// ENTRY A34391 #type complete TITLE phosphatidylinositol transfer protein alpha [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 19-May-2000 #sequence_revision 19-May-2000 #text_change 19-May-2000 ACCESSIONS A34391; A29602 REFERENCE A34391 !$#authors Dickeson, S.K.; Lim, C.N.; Schuyler, G.T.; Dalton, T.P.; !1Helmkamp Jr., G.M.; Yarbrough, L.R. !$#journal J. Biol. Chem. (1989) 264:16557-16564 !$#title Isolation and sequence of cDNA clones encoding rat !1phosphatidylinositol transfer protein. !$#cross-references MUID:89380277; PMID:2777797 !$#accession A34391 !'##molecule_type mRNA !'##residues 1-271 ##label DIC !'##cross-references GB:M25758; NID:g206494; PIDN:AAA41984.1; !1PID:g206495 REFERENCE A29602 !$#authors Funkhouser, J.D. !$#journal Biochem. Biophys. Res. Commun. (1987) 145:1310-1314 !$#title Amino-terminal sequence of a phospholipid transfer protein !1from rat lung. !$#cross-references MUID:87270706; PMID:3606604 !$#accession A29602 !'##molecule_type protein !'##residues 2-13,'H',15-21 ##label FUN !'##experimental_source lung CLASSIFICATION #superfamily human phosphatidylinositol transfer protein KEYWORDS phospholipid binding; phospholipid transport FEATURE !$2-271 #product phosphatidylinositol transfer protein !8#status experimental #label MAT SUMMARY #length 271 #molecular-weight 31907 #checksum 3750 SEQUENCE /// ENTRY I52465 #type complete TITLE phosphatidylinositol transfer protein alpha - mouse ORGANISM #formal_name Mus sp. #common_name mouse DATE 19-May-2000 #sequence_revision 19-May-2000 #text_change 19-May-2000 ACCESSIONS I52465 REFERENCE I52465 !$#authors Geijtenbeek, T.B.; de Groot, E.; van Baal, J.; Brunink, F.; !1Westerman, J.; Snoek, G.T.; Wirtz, K.W. !$#journal Biochim. Biophys. Acta (1994) 1213:309-318 !$#title Characterization of mouse phosphatidylinositol transfer !1protein expressed in Escherichia coli. !$#cross-references MUID:94325324; PMID:8049244 !$#accession I52465 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-271 ##label RES !'##cross-references GB:S72681; NID:g633848; PIDN:AAC60690.1; !1PID:g633849 CLASSIFICATION #superfamily human phosphatidylinositol transfer protein KEYWORDS phospholipid binding; phospholipid transport FEATURE !$2-271 #product phosphatidylinositol transfer protein !8#status predicted #label MAT SUMMARY #length 271 #molecular-weight 31893 #checksum 4439 SEQUENCE /// ENTRY JC4854 #type complete TITLE phosphatidylinositol transfer protein alpha - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 19-May-2000 #sequence_revision 19-May-2000 #text_change 19-May-2000 ACCESSIONS JC4854 REFERENCE JC4854 !$#authors Tsao, F.H.C.; Cheng, W.; Chen, X.; Hu, J.; Chen, X. !$#journal Gene (1996) 172:299-302 !$#title Isolation and sequencing of the cDNA encoding !1phosphatidylinositol transfer protein from rabbit lung. !$#cross-references MUID:96269422; PMID:8682321 !$#contents lung !$#accession JC4854 !'##molecule_type mRNA !'##residues 1-270 ##label TSA !'##cross-references GB:U12558; NID:g534828; PIDN:AAB08971.1; !1PID:g534829 !'##experimental_source lung COMMENT This protein plays roles in cell growth, vesicular transport !1from Golgi, pulmonary surfactant biogenesis and lung !1development. CLASSIFICATION #superfamily human phosphatidylinositol transfer protein KEYWORDS phospholipid binding; phospholipid transport FEATURE !$2-270 #product phosphatidylinositol transfer protein !8#status predicted #label MAT SUMMARY #length 270 #molecular-weight 31906 #checksum 3499 SEQUENCE /// ENTRY JX0316 #type complete TITLE phosphatidylinositol transfer protein beta - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 19-May-2000 #sequence_revision 19-May-2000 #text_change 16-Jun-2000 ACCESSIONS JX0316 REFERENCE JX0316 !$#authors Tanaka, S.; Hosaka, K. !$#journal J. Biochem. (1994) 115:981-984 !$#title Cloning of a cDNA encoding a second phosphatidylinositol !1transfer protein of rat brain by complementation of the !1yeast sec14 mutation. !$#cross-references MUID:95050435; PMID:7961615 !$#accession JX0316 !'##molecule_type mRNA !'##residues 1-271 ##label TAN !'##cross-references DDBJ:D21132; NID:g516831; PIDN:BAA04669.1; !1PID:g829055 !'##experimental_source brain, cDNA RBSEC14 COMMENT This protein catalyzes the transfer of phosphatidylinositol !1and phosphatidylcholine between natural and artificial !1membranes. CLASSIFICATION #superfamily human phosphatidylinositol transfer protein KEYWORDS phospholipid binding; phospholipid transport FEATURE !$2-271 #product phosphatidylinositol transfer protein !8#status predicted #label MAT SUMMARY #length 271 #molecular-weight 31450 #checksum 5182 SEQUENCE /// ENTRY GCHUH #type complete TITLE glycine cleavage system protein H precursor - human ALTERNATE_NAMES aminomethyl carrier protein; glycine decarboxylase complex protein H ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Apr-1991 #sequence_revision 27-Jan-1995 #text_change 16-Jun-2000 ACCESSIONS A36662; JH0386 REFERENCE A36662 !$#authors Koyata, H.; Hiraga, K. !$#journal Am. J. Hum. Genet. (1991) 48:351-361 !$#title The glycine cleavage system: structure of a cDNA encoding !1human H-protein, and partial characterization of its gene in !1patients with hyperglycinemias. !$#cross-references MUID:91118944; PMID:1671321 !$#accession A36662 !'##molecule_type mRNA !'##residues 1-173 ##label KOY !'##cross-references GB:D00723; NID:g219670; PIDN:BAA00625.1; !1PID:g219671 REFERENCE JH0386 !$#authors Fujiwara, K.; Okamura-Ikeda, K.; Hayasaka, K.; Motokawa, Y. !$#journal Biochem. Biophys. Res. Commun. (1991) 176:711-716 !$#title The primary structure of human H-protein of the glycine !1cleavage system deduced by cDNA cloning. !$#cross-references MUID:91222237; PMID:2025283 !$#accession JH0386 !'##molecule_type mRNA !'##residues 1-173 ##label FUJ !'##cross-references GB:M69175; NID:g184347; PIDN:AAA36011.1; !1PID:g184348 !'##experimental_source brain COMMENT This is the lipoylprotein that serves as a substrate for the !1three enzyme components of the glycine cleavage system !1complex. GENETICS !$#gene GDB:GCSH !'##cross-references GDB:126842 !$#map_position 2p13-2p12 CLASSIFICATION #superfamily glycine cleavage system protein H; lipoyl/ !1biotin-binding homology KEYWORDS lipoamide; mitochondrion FEATURE !$1-48 #domain transit peptide (mitochondrion) #status !8predicted #label TRN\ !$49-173 #product glycine cleavage system protein H #status !8predicted #label MAT\ !$68-142 #domain lipoyl/biotin-binding homology #label LPB\ !$107 #binding_site lipoamide (Lys) (covalent) #status !8predicted SUMMARY #length 173 #molecular-weight 18910 #checksum 8536 SEQUENCE /// ENTRY GCCHH #type complete TITLE glycine cleavage system protein H precursor - chicken ALTERNATE_NAMES aminomethyl carrier protein; glycine decarboxylase complex protein H ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Dec-1991 #sequence_revision 27-Jan-1995 #text_change 22-Jun-1999 ACCESSIONS A39520; A25718 REFERENCE A39520 !$#authors Yamamoto, M.; Koyata, H.; Matsui, C.; Hiraga, K. !$#journal J. Biol. Chem. (1991) 266:3317-3322 !$#title The glycine cleavage system. Occurrence of two types of !1chicken H-protein mRNAs presumably formed by the alternative !1use of the polyadenylation consensus sequences in a single !1exon. !$#cross-references MUID:91131642; PMID:1993703 !$#accession A39520 !'##molecule_type DNA !'##residues 1-164 ##label YAM !'##cross-references GB:M64401; GB:J05741; NID:g211899; PIDN:AAA48812.1; !1PID:g211900 REFERENCE A25718 !$#authors Fujiwara, K.; Okamura-Ikeda, K.; Motokawa, Y. !$#journal J. Biol. Chem. (1986) 261:8836-8841 !$#title Chicken liver H-protein, a component of the glycine cleavage !1system: amino acid sequence and identification of the !1N-lipoyllysine residue. !$#cross-references MUID:86250806; PMID:3522581 !$#accession A25718 !'##molecule_type protein !'##residues 40-164 ##label FUJ COMMENT This is the lipoylprotein that serves as a substrate for the !1three enzyme components of the glycine cleavage system !1complex. CLASSIFICATION #superfamily glycine cleavage system protein H; lipoyl/ !1biotin-binding homology KEYWORDS lipoamide; mitochondrion FEATURE !$1-39 #domain transit peptide (mitochondrion) #status !8predicted #label TRN\ !$40-164 #product glycine cleavage system protein H #status !8experimental #label MAT\ !$59-133 #domain lipoyl/biotin-binding homology #label LPB\ !$98 #binding_site lipoamide (Lys) (covalent) #status !8experimental SUMMARY #length 164 #molecular-weight 18010 #checksum 7606 SEQUENCE /// ENTRY GCBOH #type complete TITLE glycine cleavage system protein H precursor - bovine ALTERNATE_NAMES aminomethyl carrier protein; ferredoxin, 15.3K, mitochondrial [misidentification]; glycine decarboxylase complex protein H ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 23-Aug-1991 #sequence_revision 27-Jan-1995 #text_change 04-Feb-2000 ACCESSIONS A39214; A23611; S06488 REFERENCE A39214 !$#authors Fujiwara, K.; Okamura-Ikeda, K.; Motokawa, Y. !$#journal J. Biol. Chem. (1990) 265:17463-17467 !$#title cDNA sequence, in vitro synthesis, and intramitochondrial !1lipoylation of H-protein of the glycine cleavage system. !$#cross-references MUID:91009195; PMID:2211640 !$#accession A39214 !'##molecule_type mRNA !'##residues 1-173 ##label FUJ !'##cross-references GB:M58361; GB:J05646; NID:g163158; PIDN:AAA62710.1; !1PID:g163159 REFERENCE A23611 !$#authors Waki, N.; Hiwatashi, A.; Ichikawa, Y. !$#journal FEBS Lett. (1986) 195:87-91 !$#title Purification and biochemical characterization of hepatic !1ferredoxin (hepatoredoxin) from bovine liver mitochondria. !$#cross-references MUID:86108904; PMID:3080335 !$#accession A23611 !'##molecule_type protein !'##residues 'X',50-58,'X',60-63,'D',65 ##label WAK !'##note the authors may have determined an amino-terminal sequence for !1a protein copurified with hepatic ferredoxin REFERENCE S06485 !$#authors Driscoll, W.J.; Omdahl, J.L. !$#journal Eur. J. Biochem. (1989) 185:181-187 !$#title Characterization and N-terminal amino acid sequence of !1multiple ferredoxins in kidney and adrenal mitochondria. !$#cross-references MUID:90032674; PMID:2553401 !$#accession S06488 !'##molecule_type protein !'##residues 'GXX',52-56,'X',58-63 ##label DRI COMMENT This is the lipoylprotein that serves as a substrate for the !1three enzyme components of the glycine cleavage system !1complex. CLASSIFICATION #superfamily glycine cleavage system protein H; lipoyl/ !1biotin-binding homology KEYWORDS lipoamide; mitochondrion FEATURE !$1-48 #domain transit peptide (mitochondrion) #status !8predicted #label TRN\ !$49-173 #product glycine cleavage system protein H #status !8predicted #label MAT\ !$68-142 #domain lipoyl/biotin-binding homology #label LPB\ !$107 #binding_site lipoamide (Lys) (covalent) #status !8predicted SUMMARY #length 173 #molecular-weight 18791 #checksum 6911 SEQUENCE /// ENTRY GCPMH #type complete TITLE glycine cleavage system protein H precursor [validated] - garden pea ALTERNATE_NAMES aminomethyl carrier protein; glycine decarboxylase complex protein H ORGANISM #formal_name Pisum sativum #common_name garden pea DATE 30-Jun-1992 #sequence_revision 27-Jan-1995 #text_change 23-Mar-2001 ACCESSIONS S29122; S10676; S20222; A34922; B34922 REFERENCE S29122 !$#authors Macherel, D.; Bourguignon, J.; Douce, R. !$#journal Biochem. J. (1992) 286:627-630 !$#title Cloning of the gene (gdcH) encoding H-protein, a component !1of the glycine decarboxylase complex of pea (Pisum sativum !1L.). !$#cross-references MUID:92412042; PMID:1530594 !$#accession S29122 !'##status preliminary !'##molecule_type DNA !'##residues 1-165 ##label MAC1 !'##cross-references EMBL:X64726; NID:g20736; PIDN:CAA45978.1; !1PID:g20737 REFERENCE S10676 !$#authors Macherel, D.; Lebrun, M.; Gagnon, J.; Neuburger, M.; Douce, !1R. !$#journal Biochem. J. (1990) 268:783-789 !$#title cDNA cloning, primary structure and gene expression for !1H-protein, a component of the glycine-cleavage system !1(glycine decarboxylase) of pea (Pisum sativum) leaf !1mitochondria. !$#cross-references MUID:90303277; PMID:2363710 !$#accession S10676 !'##molecule_type mRNA !'##residues 1-165 ##label MAC2 !'##cross-references GB:X53656; NID:g287814; PIDN:CAA37704.1; !1PID:g287815 !$#accession S20222 !'##molecule_type protein !'##residues 35-74;135-165 ##label MAC3 REFERENCE A34922 !$#authors Kim, Y.; Oliver, D.J. !$#journal J. Biol. Chem. (1990) 265:848-853 !$#title Molecular cloning, transcriptional characterization, and !1sequencing of cDNA encoding the H-protein of the !1mitochondrial glycine decarboxylase complex in peas. !$#cross-references MUID:90110145; PMID:1688555 !$#accession A34922 !'##molecule_type mRNA !'##residues 1-165 ##label KIM1 !'##cross-references EMBL:J05164; NID:g169092; PIDN:AAA33668.1; !1PID:g169093 !'##note the authors translated the codon GAA for residue 146 as Gly !$#accession B34922 !'##molecule_type protein !'##residues 35-41 ##label KIM2 REFERENCE A67017 !$#authors Pares, S.; Cohen-Addad, C. !$#submission submitted to the Brookhaven Protein Data Bank, January 1995 !$#cross-references PDB:1HTP !$#contents annotation; X-ray crystallography, 2.2 angstroms REFERENCE A44677 !$#authors Cohen-Addad, C.; Pares, S.; Sieker, L.; Neuburger, M.; !1Douce, R. !$#journal Nat. Struct. Biol. (1995) 2:63-68 !$#title The lipoamide arm in the glycine decarboxylase complex is !1not freely swinging. !$#cross-references MUID:95236204; PMID:7719855 !$#contents annotation; X-ray crystallography, 2.6 angstroms REFERENCE A65800 !$#authors Pares, S.; Cohen-Addad, C.; Sieker, L.; Neuburger, M.; !1Douce, R. !$#submission submitted to the Brookhaven Protein Data Bank, February 1994 !$#cross-references PDB:1HPC !$#contents annotation; X-ray crystallography, 2.6 angstroms, residues !135-165 REFERENCE A58324 !$#authors Pares, S.; Cohen-Addad, C.; Sieker, L.; Neuburger, M.; !1Douce, R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1994) 91:4850-4853 !$#title X-ray structure determination at 2.6-angstroms resolution of !1a lipoate-containing protein: the H-protein of the glycine !1decarboxylase complex from pea leaves. !$#cross-references MUID:94255425; PMID:8197146 !$#contents annotation; X-ray crystallography, 2.6 angstroms COMMENT This is the lipoylprotein that serves as a substrate for the !1three enzyme components of the glycine cleavage system !1complex. GENETICS !$#introns 37/1; 66/3; 123/3 CLASSIFICATION #superfamily glycine cleavage system protein H; lipoyl/ !1biotin-binding homology KEYWORDS lipoamide; mitochondrion FEATURE !$1-34 #domain transit peptide (mitochondrion) #status !8predicted #label TRN\ !$35-165 #product glycine cleavage system protein H #status !8experimental #label MAT\ !$58-132 #domain lipoyl/biotin-binding homology #label LPB\ !$97 #binding_site lipoamide (Lys) (covalent) #status !8experimental SUMMARY #length 165 #molecular-weight 17688 #checksum 1843 SEQUENCE /// ENTRY A56623 #type complete TITLE glycine cleavage system protein H - Escherichia coli (strain K-12) ALTERNATE_NAMES aminomethyl carrier protein; glycine decarboxylase complex protein H ORGANISM #formal_name Escherichia coli DATE 08-Jul-1995 #sequence_revision 08-Feb-1996 #text_change 01-Mar-2002 ACCESSIONS A56623; S36833; B56689; I41231; H65074 REFERENCE A56623 !$#authors Stauffer, L.T.; Steiert, P.S.; Steiert, J.G.; Stauffer, G.V. !$#journal DNA Seq. (1991) 2:13-17 !$#title An Escherichia coli protein with homology to the H-protein !1of the glycine cleavage enzyme complex from pea and chicken !1liver. !$#cross-references MUID:92199239; PMID:1802033 !$#accession A56623 !'##status preliminary !'##molecule_type DNA !'##residues 1-129 ##label STA !'##cross-references GB:M57690; NID:g146121; PIDN:AAA68887.1; !1PID:g146122 !'##note sequence extracted from NCBI backbone (NCBIN:89516, !1NCBIP:89517) REFERENCE S36832 !$#authors Okamura-Ikeda, K.; Ohmura, Y.; Fujiwara, K.; Motokawa, Y. !$#journal Eur. J. Biochem. (1993) 216:539-548 !$#title Cloning and nucleotide sequence of the gcv operon encoding !1the Escherichia coli glycine-cleavage system. !$#cross-references MUID:93387305; PMID:8375392 !$#accession S36833 !'##status preliminary !'##molecule_type DNA !'##residues 1-129 ##label OKA !'##cross-references EMBL:X73958; NID:g403342; PIDN:CAA52145.1; !1PID:g403344 REFERENCE A56689 !$#authors Stauffer, L.T.; Ghrist, A.; Stauffer, G.V. !$#journal DNA Seq. (1993) 3:339-346 !$#title The Escherichia coli gcvT gene encoding the T-protein of the !1glycine cleavage enzyme system. !$#cross-references MUID:94033619; PMID:8219277 !$#accession B56689 !'##status preliminary !'##molecule_type DNA !'##residues 1-44 ##label ST2 !'##cross-references GB:M97263; NID:g148039; PIDN:AAC36844.1; !1PID:g148041 REFERENCE I41231 !$#authors Stauffer, L.T.; Fogarty, S.J.; Stauffer, G.V. !$#journal Gene (1994) 142:17-22 !$#title Characterization of the Escherichia coli gcv operon. !$#cross-references MUID:94237484; PMID:8181752 !$#accession I41231 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 103-129 ##label RES !'##cross-references GB:L20872; NID:g304890; PIDN:AAA23866.1; !1PID:g304891 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65074 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-129 ##label BLAT !'##cross-references GB:AE000374; GB:U00096; NID:g1789270; !1PIDN:AAC75942.1; PID:g1789271; UWGP:b2904 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene gcvH !$#map_position 63 min COMPLEX the glycine cleavage system is composed of four components: !1protein P, glycine dehydrogenase (decarboxylating) (EC !11.4.4.2); protein T, aminomethyltransferase (EC 2.1.2.10); !1protein L, dihydrolipoamide dehydrogenase (EC 1.8.1.4); and !1protein H FUNCTION !$#description a lipoylprotein that serves as a substrate for the three !1enzyme components (proteins P, T, and L) of the glycine !1cleavage system that catalyzes the degradation of glycine; !1it shuttles the methylamine group of glycine from the P !1protein to the T protein CLASSIFICATION #superfamily glycine cleavage system protein H; lipoyl/ !1biotin-binding homology KEYWORDS lipoamide FEATURE !$2-129 #product glycine cleavage system protein H #status !8predicted #label MAT\ !$26-100 #domain lipoyl/biotin-binding homology #label LPB\ !$65 #binding_site lipoamide (Lys) (covalent) #status !8predicted SUMMARY #length 129 #molecular-weight 13811 #checksum 6785 SEQUENCE /// ENTRY JLBO6 #type complete TITLE coupling factor 6 precursor, mitochondrial - bovine ALTERNATE_NAMES ATP synthase coupling factor 6 ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 17-May-1985 #sequence_revision 28-Oct-1994 #text_change 22-Jun-1999 ACCESSIONS B27382; A03180; E39566 REFERENCE A90527 !$#authors Walker, J.E.; Gay, N.J.; Powell, S.J.; Kostina, M.; Dyer, !1M.R. !$#journal Biochemistry (1987) 26:8613-8619 !$#title ATP synthase from bovine mitochondria: sequences of imported !1precursors of oligomycin sensitivity conferral protein, !1factor 6, and adenosinetriphosphatase inhibitor protein. !$#cross-references MUID:88163536; PMID:2894843 !$#accession B27382 !'##molecule_type mRNA !'##residues 1-108 ##label WAL !'##cross-references GB:M19217; NID:g163035; PIDN:AAA30511.1; !1PID:g163036 REFERENCE A03180 !$#authors Fang, J.; Jacobs, J.W.; Kanner, B.I.; Racker, E.; Bradshaw, !1R.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:6603-6607 !$#title Amino acid sequence of bovine heart coupling factor 6. !$#cross-references MUID:85038563; PMID:6149548 !$#accession A03180 !'##molecule_type protein !'##residues 33-93,'F',95-108 ##label FAN !'##experimental_source heart REFERENCE A39566 !$#authors Walker, J.E.; Lutter, R.; Dupuis, A.; Runswick, M.J. !$#journal Biochemistry (1991) 30:5369-5378 !$#title Identification of the subunits of F-1F-0-ATPase from bovine !1heart mitochondria. !$#cross-references MUID:91242449; PMID:1827992 !$#accession E39566 !'##molecule_type protein !'##residues 33-37 ##label WA2 COMMENT This is one of the soluble components required for coupling !1of phosphorylation to oxidation in mitochondria. CLASSIFICATION #superfamily coupling factor 6 KEYWORDS mitochondrion; oxidative phosphorylation FEATURE !$1-32 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$33-108 #product coupling factor 6 #status experimental !8#label MAT SUMMARY #length 108 #molecular-weight 12532 #checksum 9457 SEQUENCE /// ENTRY JQ0026 #type complete TITLE ATP/ADP translocase tlc1 - Rickettsia prowazekii ALTERNATE_NAMES ADP/ATP carrier protein tlc1; RP053 ORGANISM #formal_name Rickettsia prowazekii DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 03-Nov-2000 ACCESSIONS JQ0026; E71713 REFERENCE JQ0026 !$#authors Williamson, L.R.; Plano, G.V.; Winkler, H.H.; Krause, D.C.; !1Wood, D.O. !$#journal Gene (1989) 80:269-278 !$#title Nucleotide sequence of the Rickettsia prowazekii ATP/ADP !1translocase-encoding gene. !$#cross-references MUID:90060776; PMID:2555259 !$#accession JQ0026 !'##molecule_type DNA !'##residues 1-498 ##label WIL !'##cross-references GB:M28816; NID:g152469; PIDN:AAA26382.1; !1PID:g152470 REFERENCE A71630 !$#authors Andersson, S.G.E.; Zomorodipour, A.; Andersson, J.O.; !1Sicheritz-Ponten, T.; Alsmark, U.C.M.; Podowski, R.M.; !1Naeslund, A.K.; Eriksson, A.S.; Winkler, H.H.; Kurland, C.G. !$#journal Nature (1998) 396:133-140 !$#title The genome sequence of Rickettsia prowazekii and the origin !1of mitochondria. !$#cross-references MUID:99039499; PMID:9823893 !$#accession E71713 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-498 ##label AND !'##cross-references GB:AJ235270; GB:AJ235269; NID:g3860572; !1PIDN:CAA14524.1; PID:g3860623; GSPDB:GN00081 !'##experimental_source strain Madrid E COMMENT This ATP/ADP translocase shares no detectable amino acid !1sequence homologies with its mitochondrial functional !1counterparts, but may be homologous with some plant !1sequences. GENETICS !$#gene tlc1; RP053 FUNCTION !$#description exchanges ADP in the rickettsial cell with ATP in the host !1cell CLASSIFICATION #superfamily rickettsial-type ATP/ADP translocase KEYWORDS transmembrane protein FEATURE !$28-45 #domain transmembrane #status predicted #label TR01\ !$68-84 #domain transmembrane #status predicted #label TR02\ !$93-115 #domain transmembrane #status predicted #label TR03\ !$183-206 #domain transmembrane #status predicted #label TR04\ !$219-237 #domain transmembrane #status predicted #label TR05\ !$279-297 #domain transmembrane #status predicted #label TR06\ !$346-370 #domain transmembrane #status predicted #label TR07\ !$380-399 #domain transmembrane #status predicted #label TR08\ !$445-461 #domain transmembrane #status predicted #label TR09\ !$466-482 #domain transmembrane #status predicted #label TR10 SUMMARY #length 498 #molecular-weight 56821 #checksum 9305 SEQUENCE /// ENTRY S68205 #type complete TITLE ATP/ADP translocase AATP1 precursor - Arabidopsis thaliana ALTERNATE_NAMES adenine nucleotide translocase; ATP/ADP translocator protein ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 28-Oct-1996 #sequence_revision 27-Feb-1997 #text_change 22-Jun-1999 ACCESSIONS S68205 REFERENCE S68205 !$#authors Kampfenkel, K.; Moehlmann, T.; Batz, O.; van Montagu, M.; !1Inze, D.; Neuhaus, H.E. !$#journal FEBS Lett. (1995) 374:351-355 !$#title Molecular characterization of an Arabidopsis thaliana cDNA !1encoding a novel putative adenylate translocator of higher !1plants. !$#cross-references MUID:96069943; PMID:7589569 !$#accession S68205 !'##molecule_type mRNA !'##residues 1-589 ##label KAM !'##cross-references EMBL:Z49227; NID:g1051108; PIDN:CAA89201.1; !1PID:g1051109 GENETICS !$#gene AATP1 !$#genome nuclear CLASSIFICATION #superfamily rickettsial-type ATP/ADP translocase KEYWORDS chloroplast; transmembrane protein FEATURE !$1-100 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$101-589 #product ATP/ADP translocase AATP1 #status predicted !8#label MAT SUMMARY #length 589 #molecular-weight 65257 #checksum 9984 SEQUENCE /// ENTRY QQECRS #type complete TITLE ygjE protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS E65094; C29049 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65094 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-487 ##label BLAT !'##cross-references GB:AE000388; GB:U00096; NID:g1789441; !1PIDN:AAC76099.1; PID:g1789444; UWGP:b3063 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A91573 !$#authors Nesin, M.; Lupski, J.R.; Svec, P.; Godson, G.N. !$#journal Gene (1987) 51:149-161 !$#title Possible new genes as revealed by molecular analysis of a !15-kb Escherichia coli chromosomal region 5' to the !1rpsU-dnaG-rpoD macromolecular-synthesis operon. !$#cross-references MUID:87248073; PMID:3297921 !$#accession C29049 !'##molecule_type DNA !'##residues 279-403,'P',405-411,'RWRCRKSRCRCSA' ##label NES GENETICS !$#gene ygjE !$#map_position 67 min CLASSIFICATION #superfamily 2-oxoglutarate/malate translocator KEYWORDS transmembrane protein FEATURE !$11-27 #domain transmembrane #status predicted #label TM1\ !$33-49 #domain transmembrane #status predicted #label TM2\ !$52-68 #domain transmembrane #status predicted #label TM3\ !$95-111 #domain transmembrane #status predicted #label TM4\ !$138-154 #domain transmembrane #status predicted #label TM5\ !$206-222 #domain transmembrane #status predicted #label TM6\ !$237-253 #domain transmembrane #status predicted #label TM7\ !$289-305 #domain transmembrane #status predicted #label TM8\ !$310-326 #domain transmembrane #status predicted #label TM9\ !$378-394 #domain transmembrane #status predicted #label TM10\ !$422-438 #domain transmembrane #status predicted #label TM11\ !$464-480 #domain transmembrane #status predicted #label TM12 SUMMARY #length 487 #molecular-weight 52906 #checksum 1643 SEQUENCE /// ENTRY B64043 #type complete TITLE conserved hypothetical protein HI0020 - Haemophilus influenzae ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B64043 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession B64043 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-479 ##label TIGR !'##cross-references GB:U32687; GB:L42023; NID:g1572955; !1PIDN:AAC21698.1; PID:g1572964; TIGR:HI0020 !'##experimental_source strain Rd KW20 CLASSIFICATION #superfamily 2-oxoglutarate/malate translocator SUMMARY #length 479 #molecular-weight 51353 #checksum 9765 SEQUENCE /// ENTRY B64813 #type complete TITLE ybhI protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS B64813 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64813 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-477 ##label BLAT !'##cross-references GB:AE000179; GB:U00096; NID:g1786978; !1PIDN:AAC73857.1; PID:g1786986; UWGP:b0770 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ybhI CLASSIFICATION #superfamily 2-oxoglutarate/malate translocator KEYWORDS transmembrane protein FEATURE !$6-22 #domain transmembrane #status predicted #label TM1\ !$32-48 #domain transmembrane #status predicted #label TM2\ !$55-71 #domain transmembrane #status predicted #label TM3\ !$92-108 #domain transmembrane #status predicted #label TM4\ !$125-141 #domain transmembrane #status predicted #label TM5\ !$149-165 #domain transmembrane #status predicted #label TM6\ !$224-240 #domain transmembrane #status predicted #label TM7\ !$272-288 #domain transmembrane #status predicted #label TM8\ !$297-313 #domain transmembrane #status predicted #label TM9\ !$365-381 #domain transmembrane #status predicted #label TM10\ !$388-404 #domain transmembrane #status predicted #label TM11\ !$447-463 #domain transmembrane #status predicted #label TM12 SUMMARY #length 477 #molecular-weight 51350 #checksum 6635 SEQUENCE /// ENTRY B64795 #type complete TITLE ybdS protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS B64795 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64795 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-487 ##label BLAT !'##cross-references GB:AE000166; GB:U00096; NID:g1786819; !1PIDN:AAC73713.1; PID:g1786829; UWGP:b0612 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ybdS CLASSIFICATION #superfamily 2-oxoglutarate/malate translocator KEYWORDS transmembrane protein FEATURE !$11-27 #domain transmembrane #status predicted #label TM1\ !$34-50 #domain transmembrane #status predicted #label TM2\ !$53-69 #domain transmembrane #status predicted #label TM3\ !$99-115 #domain transmembrane #status predicted #label TM4\ !$139-155 #domain transmembrane #status predicted #label TM5\ !$238-254 #domain transmembrane #status predicted #label TM6\ !$289-305 #domain transmembrane #status predicted #label TM7\ !$311-327 #domain transmembrane #status predicted #label TM8\ !$379-395 #domain transmembrane #status predicted #label TM9\ !$424-440 #domain transmembrane #status predicted #label TM10\ !$463-479 #domain transmembrane #status predicted #label TM11 SUMMARY #length 487 #molecular-weight 53092 #checksum 124 SEQUENCE /// ENTRY F69811 #type complete TITLE 2-oxoglutarate/malate translocator homolog yflS - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS F69811 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69811 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-478 ##label KUN !'##cross-references GB:Z99108; GB:AL009126; NID:g2633055; !1PIDN:CAB12586.1; PID:g2633081 !'##experimental_source strain 168 GENETICS !$#gene yflS CLASSIFICATION #superfamily 2-oxoglutarate/malate translocator SUMMARY #length 478 #molecular-weight 51431 #checksum 768 SEQUENCE /// ENTRY G64537 #type complete TITLE 2-oxoglutarate/malate translocator - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS G64537 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession G64537 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-461 ##label TOM !'##cross-references GB:AE000511; TIGR:HP0143 CLASSIFICATION #superfamily 2-oxoglutarate/malate translocator SUMMARY #length 461 #molecular-weight 50859 #checksum 4530 SEQUENCE /// ENTRY A44778 #type complete TITLE ADP,ATP carrier protein T1 - human ALTERNATE_NAMES mitochondrial ADP,ATP translocase 1 ORGANISM #formal_name Homo sapiens #common_name man DATE 17-Mar-2000 #sequence_revision 17-Mar-2000 #text_change 17-Mar-2000 ACCESSIONS A44778; S03893; A39891; A28116 REFERENCE A44778 !$#authors Li, K.; Warner, C.K.; Hodge, J.A.; Minoshima, S.; Kudoh, J.; !1Fukuyama, R.; Maekawa, M.; Shimizu, Y.; Shimizu, N.; !1Wallace, D.C. !$#journal J. Biol. Chem. (1989) 264:13998-14004 !$#title A human muscle adenine nucleotide translocator gene has four !1exons, is located on chromosome 4, and is differentially !1expressed. !$#cross-references MUID:89340499; PMID:2547778 !$#accession A44778 !'##status preliminary !'##molecule_type DNA !'##residues 1-298 ##label LIA !'##cross-references GB:J04982; NID:g178658; PIDN:AAA51736.1; !1PID:g178659 REFERENCE S03893 !$#authors Cozens, A.L.; Runswick, M.J.; Walker, J.E. !$#journal J. Mol. Biol. (1989) 206:261-280 !$#title DNA sequences of two expressed nuclear genes for human !1mitochondrial ADP/ATP translocase. !$#cross-references MUID:89236396; PMID:2541251 !$#accession S03893 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-298 ##label COZ REFERENCE A39891 !$#authors Neckelmann, N.; Li, K.; Wade, R.P.; Shuster, R.; Wallace, !1D.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:7580-7584 !$#title cDNA sequence of a human skeletal muscle ADP/ATP !1translocator: lack of a leader peptide, divergence from a !1fibroblast translocator cDNA, and coevolution with !1mitochondrial DNA genes. !$#cross-references MUID:88041149; PMID:2823266 !$#accession A39891 !'##status preliminary !'##molecule_type mRNA !'##residues 1-15,'A',17-146,'RR',149,151-226,'L',228-298 ##label NEC !'##cross-references GB:J02966; NID:g339919; PIDN:AAA61223.1; !1PID:g339920 !'##experimental_source clone pHMANT REFERENCE A94197 !$#authors Houldsworth, J.; Attardi, G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:377-381 !$#title Two distinct genes for ADP/ATP translocase are expressed at !1the mRNA level in adult human liver. !$#cross-references MUID:88124845; PMID:2829183 !$#accession A28116 !'##molecule_type mRNA !'##residues 1-37 ##label HOU !'##cross-references GB:J03593; NID:g339724; PIDN:AAA36751.1; !1PID:g339725 !'##experimental_source liver GENETICS !$#gene GDB:ANT1; T1 !'##cross-references GDB:119680; OMIM:103220 !$#map_position 4q35-4q35 CLASSIFICATION #superfamily ADP,ATP carrier protein; ADP,ATP carrier !1protein repeat homology KEYWORDS duplication; homodimer; mitochondrion; transmembrane protein FEATURE !$2-298 #product ADP,ATP carrier protein #status predicted !8#label MAT\ !$5-99 #domain ADP,ATP carrier protein repeat homology !8#label ACP1\ !$110-202 #domain ADP,ATP carrier protein repeat homology !8#label ACP2\ !$207-298 #domain ADP,ATP carrier protein repeat homology !8#label ACP3 SUMMARY #length 298 #molecular-weight 33064 #checksum 31 SEQUENCE /// ENTRY XWBO #type complete TITLE ADP,ATP carrier protein T1 - bovine ALTERNATE_NAMES ADP/ATP translocase T1 ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 14-Nov-1983 #sequence_revision 22-Jul-1994 #text_change 22-Jun-1999 ACCESSIONS A43646; A24822; A03181; A61343; S69369 REFERENCE A43646 !$#authors Powell, S.J.; Medd, S.M.; Runswick, M.J.; Walker, J.E. !$#journal Biochemistry (1989) 28:866-873 !$#title Two bovine genes for mitochondrial ADP/ATP translocase !1expressed differently in various tissues. !$#cross-references MUID:89229093; PMID:2540808 !$#accession A43646 !'##molecule_type mRNA !'##residues 1-298 ##label POW !'##cross-references GB:M24102; NID:g529414; PIDN:AAA30768.1; !1PID:g529415 REFERENCE A24822 !$#authors Rasmussen, U.B.; Wohlrab, H. !$#journal Biochem. Biophys. Res. Commun. (1986) 138:850-857 !$#title Bovine cardiac mitochondrial ADP/ATP-carrier: two distinct !1mRNAs and an unusually short 3'-noncoding sequence. !$#cross-references MUID:86295775; PMID:3017341 !$#accession A24822 !'##molecule_type mRNA !'##residues 208-298 ##label RAS !'##cross-references GB:M13783; NID:g162630; PIDN:AAA30363.1; !1PID:g162631 REFERENCE A03181 !$#authors Aquila, H.; Misra, D.; Eulitz, M.; Klingenberg, M. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1982) 363:345-349 !$#title Complete amino acid sequence of the ADP/ATP carrier from !1beef heart mitochondria. !$#cross-references MUID:82188267; PMID:7076130 !$#accession A03181 !'##molecule_type protein !'##residues 2-51,'X',53-70,'X',72-109,'X',111-298 ##label AQU !'##note residue 52 may be methyllysine REFERENCE A61343 !$#authors Babel, W.; Wachter, E.; Aquila, H.; Klingenberg, M. !$#journal Biochim. Biophys. Acta (1981) 670:176-180 !$#title Amino acid sequence determination of the ADP,ATP carrier !1from beef heart mitochondria. The sequence of the C-terminal !1acidolytic fragment. !$#cross-references MUID:82046808; PMID:6271240 !$#accession A61343 !'##molecule_type protein !'##residues 205-298 ##label BAB REFERENCE S69369 !$#authors Oettmeier, W.; Masson, K.; Kalinna, S. !$#journal Eur. J. Biochem. (1995) 227:730-733 !$#title [(3)H]7-azido-4-isopropylacridone labels Cys159 of the !1bovine mitochondrial ADP/ATP-carrier protein. !$#cross-references MUID:95172058; PMID:7867632 !$#accession S69369 !'##molecule_type protein !'##residues 49-63;154-168 ##label OET COMMENT This protein is synthesized in the cytosol and transported !1into the mitochondrion. COMPLEX homodimer FUNCTION !$#description catalyzes the exchange between cytosolic ADP and !1mitochondrial ATP generated by oxidative phosphorylation !$#note located in the inner mitochondrial membrane CLASSIFICATION #superfamily ADP,ATP carrier protein; ADP,ATP carrier !1protein repeat homology KEYWORDS acetylated amino end; duplication; homodimer; methylated !1amino acid; mitochondrion; transmembrane protein FEATURE !$5-99 #domain ADP,ATP carrier protein repeat homology !8#label ACP1\ !$110-202 #domain ADP,ATP carrier protein repeat homology !8#label ACP2\ !$207-298 #domain ADP,ATP carrier protein repeat homology !8#label ACP3\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental\ !$52 #modified_site N6-methyllysine (Lys) #status !8predicted SUMMARY #length 298 #molecular-weight 32967 #checksum 1624 SEQUENCE /// ENTRY A29132 #type complete TITLE ADP,ATP carrier protein T2 - human ALTERNATE_NAMES mitochondrial ADP,ATP translocase 2 ORGANISM #formal_name Homo sapiens #common_name man DATE 17-Mar-2000 #sequence_revision 17-Mar-2000 #text_change 17-Mar-2000 ACCESSIONS A29132; C28116 REFERENCE A29132 !$#authors Battini, R.; Ferrari, S.; Kaczmarek, L.; Calabretta, B.; !1Chen, S.; Baserga, R. !$#journal J. Biol. Chem. (1987) 262:4355-4359 !$#title Molecular cloning of a cDNA for a human ADP/ATP carrier !1which is growth-regulated. !$#cross-references MUID:87166056; PMID:3031073 !$#accession A29132 !'##molecule_type mRNA !'##residues 1-298 ##label BAT !'##cross-references GB:J02683; NID:g179246; PIDN:AAA35579.1; !1PID:g179247 REFERENCE A94197 !$#authors Houldsworth, J.; Attardi, G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:377-381 !$#title Two distinct genes for ADP/ATP translocase are expressed at !1the mRNA level in adult human liver. !$#cross-references MUID:88124845; PMID:2829183 !$#accession C28116 !'##molecule_type mRNA !'##residues 47-65,'G',67-110,'L',112-161,'G',163-298 ##label HOU !'##cross-references GB:J03591; NID:g339720; PIDN:AAA36749.1; !1PID:g339721 !'##experimental_source clone pHAT3 GENETICS !$#gene GDB:ANT2; T3; 2F1 !'##cross-references GDB:125190; OMIM:300150 !$#map_position Xq13-Xq26 !$#note there may be some confusion in the assignment of sequences !1for GDB:ANT2 and GDB:ANT3 CLASSIFICATION #superfamily ADP,ATP carrier protein; ADP,ATP carrier !1protein repeat homology KEYWORDS duplication; homodimer; mitochondrion; transmembrane protein FEATURE !$5-99 #domain ADP,ATP carrier protein repeat homology !8#label ACP1\ !$110-202 #domain ADP,ATP carrier protein repeat homology !8#label ACP2\ !$207-298 #domain ADP,ATP carrier protein repeat homology !8#label ACP3 SUMMARY #length 298 #molecular-weight 32981 #checksum 1565 SEQUENCE /// ENTRY S03894 #type complete TITLE ADP,ATP carrier protein T3 - human ALTERNATE_NAMES ADP,ATP carrier protein T2 (misidentification); mitochondrial ADP,ATP translocase 3 ORGANISM #formal_name Homo sapiens #common_name man DATE 17-Mar-2000 #sequence_revision 17-Mar-2000 #text_change 17-Mar-2000 ACCESSIONS S03894; B28116 REFERENCE S03893 !$#authors Cozens, A.L.; Runswick, M.J.; Walker, J.E. !$#journal J. Mol. Biol. (1989) 206:261-280 !$#title DNA sequences of two expressed nuclear genes for human !1mitochondrial ADP/ATP translocase. !$#cross-references MUID:89236396; PMID:2541251 !$#accession S03894 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-298 ##label COZ REFERENCE A94197 !$#authors Houldsworth, J.; Attardi, G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:377-381 !$#title Two distinct genes for ADP/ATP translocase are expressed at !1the mRNA level in adult human liver. !$#cross-references MUID:88124845; PMID:2829183 !$#accession B28116 !'##molecule_type mRNA !'##residues 36-104,'R',106,'A',109-298 ##label HOU !'##cross-references GB:J03592; NID:g339722; PIDN:AAA36750.1; !1PID:g339723 !'##experimental_source liver GENETICS !$#gene GDB:ANT3; ANT3Y !'##cross-references GDB:125184; OMIM:300151; OMIM:403000 !$#map_position Xp22.32-Xp22.32; Yp11.3-Yp11.3 !$#note there may be some confusion in the assignment of sequences !1for GDB:ANT2 and GDB:ANT3 CLASSIFICATION #superfamily ADP,ATP carrier protein; ADP,ATP carrier !1protein repeat homology KEYWORDS duplication; homodimer; mitochondrion; transmembrane protein FEATURE !$2-298 #product ADP,ATP carrier protein #status predicted !8#label MAT\ !$5-99 #domain ADP,ATP carrier protein repeat homology !8#label ACP1\ !$110-202 #domain ADP,ATP carrier protein repeat homology !8#label ACP2\ !$207-298 #domain ADP,ATP carrier protein repeat homology !8#label ACP3 SUMMARY #length 298 #molecular-weight 32866 #checksum 3645 SEQUENCE /// ENTRY S31935 #type complete TITLE ADP,ATP carrier protein - African malaria mosquito ORGANISM #formal_name Anopheles gambiae #common_name African malaria mosquito DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S31935; S31936 REFERENCE S31935 !$#authors Beard, C.B.; Crews-Oyen, A.E.; Collins, F.H. !$#submission submitted to the EMBL Data Library, February 1993 !$#description A cDNA encoding an ADP/ATP carrier from the mosquito !1Anopheles gambiae. !$#accession S31935 !'##status preliminary !'##molecule_type DNA !'##residues 1-301 ##label BEA !'##cross-references EMBL:Z21814; EMBL:Z21815 CLASSIFICATION #superfamily ADP,ATP carrier protein; ADP,ATP carrier !1protein repeat homology KEYWORDS duplication; transmembrane protein FEATURE !$7-101 #domain ADP,ATP carrier protein repeat homology !8#label ACP1\ !$112-204 #domain ADP,ATP carrier protein repeat homology !8#label ACP2\ !$209-300 #domain ADP,ATP carrier protein repeat homology !8#label ACP3 SUMMARY #length 301 #molecular-weight 32681 #checksum 8885 SEQUENCE /// ENTRY XWNC #type complete TITLE ADP,ATP carrier protein - Neurospora crassa ALTERNATE_NAMES ADP/ATP translocase ORGANISM #formal_name Neurospora crassa DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 22-Jun-1999 ACCESSIONS A03182 REFERENCE A03182 !$#authors Arends, H.; Sebald, W. !$#journal EMBO J. (1984) 3:377-382 !$#title Nucleotide sequence of the cloned mRNA and gene of the ADP/ !1ATP carrier from Neurospora crassa. !$#cross-references MUID:84182500; PMID:6325169 !$#accession A03182 !'##molecule_type DNA; mRNA !'##residues 1-313 ##label ARE !'##cross-references GB:X00363; NID:g2976; PIDN:CAA25104.1; PID:g2977 COMMENT This protein, which catalyzes the exchange of ADP and ATP !1across the mitochondrial inner membrane, is synthesized in !1the cytosol and transported into the mitochondrion. COMMENT The active protein is a dimer of identical chains. GENETICS !$#introns 11/3; 44/3 CLASSIFICATION #superfamily ADP,ATP carrier protein; ADP,ATP carrier !1protein repeat homology KEYWORDS duplication; homodimer; mitochondrion; transmembrane protein FEATURE !$10-105 #domain ADP,ATP carrier protein repeat homology !8#label ACP1\ !$115-209 #domain ADP,ATP carrier protein repeat homology !8#label ACP2\ !$215-303 #domain ADP,ATP carrier protein repeat homology !8#label ACP3 SUMMARY #length 313 #molecular-weight 33888 #checksum 7509 SEQUENCE /// ENTRY S30259 #type complete TITLE ADP,ATP carrier protein, mitochondrial - Chlamydomonas reinhardtii ALTERNATE_NAMES ADP/ATP translocator ORGANISM #formal_name Chlamydomonas reinhardtii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S30259; S20628 REFERENCE S30259 !$#authors Sharpe, J.A.; Day, A. !$#journal Mol. Gen. Genet. (1993) 237:134-144 !$#title Structure, evolution and expression of the mitochondrial !1ADP/ATP translocator gene from Chlamydomonas reinhardtii. !$#cross-references MUID:93204887; PMID:8455552 !$#accession S30259 !'##molecule_type mRNA !'##residues 1-308 ##label SHA !'##cross-references EMBL:X65194; NID:g18109; PIDN:CAA46311.1; !1PID:g18110 CLASSIFICATION #superfamily ADP,ATP carrier protein; ADP,ATP carrier !1protein repeat homology KEYWORDS duplication; homodimer; mitochondrion; transmembrane protein FEATURE !$5-100 #domain ADP,ATP carrier protein repeat homology !8#label ACP1\ !$109-204 #domain ADP,ATP carrier protein repeat homology !8#label ACP2\ !$210-298 #domain ADP,ATP carrier protein repeat homology !8#label ACP3 SUMMARY #length 308 #molecular-weight 33528 #checksum 2486 SEQUENCE /// ENTRY S29852 #type complete TITLE ADP,ATP carrier protein - Arabidopsis thaliana ALTERNATE_NAMES adenine nucleotide translocator ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S29852; S29618 REFERENCE S29852 !$#authors Schuster, W.; Kloska, S.; Brennicke, A. !$#journal Biochim. Biophys. Acta (1993) 1172:205-208 !$#title An adenine nucleotide translocator gene from Arabidopsis !1thaliana. !$#cross-references MUID:93176813; PMID:8439563 !$#accession S29852 !'##molecule_type DNA !'##residues 1-385 ##label SCH !'##cross-references EMBL:X68592; NID:g16159; PIDN:CAA48579.1; !1PID:g16160 GENETICS !$#gene ANT2 !$#introns 162/3; 287/3 CLASSIFICATION #superfamily ADP,ATP carrier protein; ADP,ATP carrier !1protein repeat homology KEYWORDS duplication; mitochondrion; transmembrane protein FEATURE !$81-176 #domain ADP,ATP carrier protein repeat homology !8#label ACP1\ !$186-281 #domain ADP,ATP carrier protein repeat homology !8#label ACP2\ !$287-375 #domain ADP,ATP carrier protein repeat homology !8#label ACP3 SUMMARY #length 385 #molecular-weight 41845 #checksum 7550 SEQUENCE /// ENTRY A31978 #type complete TITLE ADP,ATP carrier protein AAC2 precursor - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES adenine nucleotide carrier; protein YBL030c; protein YBL0421 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A31978; S36419; S45764; S50304; S42759 REFERENCE A31978 !$#authors Lawson, J.E.; Douglas, M.G. !$#journal J. Biol. Chem. (1988) 263:14812-14818 !$#title Separate genes encode functionally equivalent ADP/ATP !1carrier proteins in Saccharomyces cerevisiae. Isolation and !1analysis of AAC2. !$#cross-references MUID:89008354; PMID:2844786 !$#accession A31978 !'##molecule_type DNA !'##residues 1-318 ##label LAW !'##cross-references EMBL:J04021; NID:g170957; PIDN:AAA34381.1; !1PID:g170958 REFERENCE S36419 !$#authors Trezeguet, V.; le Saux, A.; Lauquin, J.M. !$#submission submitted to the EMBL Data Library, August 1993 !$#accession S36419 !'##molecule_type DNA !'##residues 1-318 ##label TRE !'##cross-references EMBL:X74427; NID:g396554; PIDN:CAA52446.1; !1PID:g396555 REFERENCE S45745 !$#authors Goffeau, A.; Jonniaux, J.L.; Purnelle, B.; Skala, J.; de !1Wergifosse, P.; van Dyck, L. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S45764 !'##molecule_type DNA !'##residues 1-318 ##label GOF !'##cross-references EMBL:Z35791; NID:g536034; PIDN:CAA84850.1; !1PID:g536035; GSPDB:GN00002; MIPS:YBL030c REFERENCE S50299 !$#authors van Dyck, L.; Jonniaux, J.L.; de Melo Barreiros, T.; Kleine, !1K.; Goffeau, A. !$#journal Yeast (1994) 10:1663-1673 !$#title Analysis of a 17.4 kb DNA segment of yeast chromosome II !1encompassing the ribosomal protein L19 as well as proteins !1with homologies to components of the hnRNP and snRNP !1complexes and to the human proliferation-associated p120 !1antigen. !$#cross-references MUID:95242843; PMID:7725803 !$#accession S50304 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-318 ##label VAN !'##cross-references EMBL:X77291; NID:g602888; PIDN:CAA54501.1; !1PID:g602894 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1994 REFERENCE A36582 !$#authors Kolarov, J.; Kolarova, N.; Nelson, N. !$#journal J. Biol. Chem. (1990) 265:12711-12716 !$#title A third ADP/ATP translocator gene in yeast. !$#cross-references MUID:90324269; PMID:2165073 !$#accession S42759 !'##molecule_type DNA !'##residues 1-57,'I',59-64,'K',66-67,'S',69-70,'V',72-78,'K',80-82,'L', !184-112,'L',114-123,'G',125-318 ##label KOL !'##cross-references EMBL:M34075; NID:g170961; PIDN:AAA97484.1; !1PID:g170962 GENETICS !$#gene SGD:PET9; AAC2; MIPS:YBL030c !'##cross-references MIPS:YBL030c; SGD:S0000126 !$#map_position 2L !$#genome nuclear CLASSIFICATION #superfamily ADP,ATP carrier protein; ADP,ATP carrier !1protein repeat homology KEYWORDS duplication; homodimer; mitochondrial inner membrane; !1mitochondrion; transmembrane protein FEATURE !$1-20 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$20-115 #domain ADP,ATP carrier protein repeat homology !8#label ACP1\ !$21-318 #product ADP,ATP carrier protein AAC2 #status !8predicted #label MAT\ !$21-37 #domain transmembrane #status predicted #label TM1\ !$124-218 #domain ADP,ATP carrier protein repeat homology !8#label ACP2\ !$131-147 #domain transmembrane #status predicted #label TM2\ !$186-202 #domain transmembrane #status predicted #label TM3\ !$217-233 #domain transmembrane #status predicted #label TM4\ !$224-312 #domain ADP,ATP carrier protein repeat homology !8#label ACP3 SUMMARY #length 318 #molecular-weight 34426 #checksum 8661 SEQUENCE /// ENTRY S44092 #type complete TITLE probable carrier protein c2 - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 29-Oct-1999 ACCESSIONS S44092; T24753 REFERENCE S44090 !$#authors Runswick, M.J.; Philippides, A.; Lauria, G.; Walker, J.E. !$#submission submitted to the EMBL Data Library, November 1993 !$#description Extension of the mitochondrial transport superfamily: !1sequences of five members from the nematode worm !1Caenorhabditis elegans. !$#accession S44092 !'##status preliminary !'##molecule_type mRNA !'##residues 1-384 ##label RUN !'##cross-references EMBL:X76116; NID:g472899; PIDN:CAA53722.1; !1PID:g472900 REFERENCE Z19932 !$#authors Lloyd, C. !$#submission submitted to the EMBL Data Library, April 1995 !$#accession T24753 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-384 ##label WIL !'##cross-references EMBL:Z49070; PIDN:CAA88869.1; GSPDB:GN00020; !1CESP:T09F3.2 !'##experimental_source clone T09F3 GENETICS !$#gene CESP:T09F3.2 !$#map_position 2 !$#introns 82/1; 113/1; 153/2; 179/2; 259/3; 359/3 CLASSIFICATION #superfamily Caenorhabditis probable carrier protein c2; !1ADP,ATP carrier protein repeat homology FEATURE !$4-43,141-193 #domain ADP,ATP carrier protein repeat homology !8#status atypical #label ACP1\ !$45-67 #region serine-rich\ !$201-285 #domain ADP,ATP carrier protein repeat homology !8#label ACP2\ !$296-381 #domain ADP,ATP carrier protein repeat homology !8#label ACP3 SUMMARY #length 384 #molecular-weight 42128 #checksum 3796 SEQUENCE /// ENTRY S54495 #type complete TITLE probable carrier protein YPR021c - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein YP9367.01c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S54495 REFERENCE S54059 !$#authors Badcock, K.; Churcher, C.M. !$#submission submitted to the EMBL Data Library, May 1995 !$#accession S54495 !'##molecule_type DNA !'##residues 1-902 ##label BAD !'##cross-references EMBL:Z49274; NID:g809585; PIDN:CAA89275.1; !1PID:g809586; GSPDB:GN00016; MIPS:YPR021c !'##experimental_source strain AB972 GENETICS !$#gene MIPS:YPR021c !'##cross-references SGD:S0006225 !$#map_position 16R CLASSIFICATION #superfamily probable carrier protein YPR021c; ADP,ATP !1carrier protein repeat homology KEYWORDS duplication; transmembrane protein FEATURE !$527-615 #domain ADP,ATP carrier protein repeat homology !8#label ACP1\ !$621-711 #domain ADP,ATP carrier protein repeat homology !8#label ACP2\ !$724-814 #domain ADP,ATP carrier protein repeat homology !8#label ACP3 SUMMARY #length 902 #molecular-weight 104303 #checksum 1564 SEQUENCE /// ENTRY A56509 #type complete TITLE peroxisomal membrane protein PMP27 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein AOE236; protein O0454; protein YOL147c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A56509; B56509; S60389; S62134; S62148; S66844; S57677 REFERENCE A56509 !$#authors Erdmann, R.; Blobel, G. !$#journal J. Cell Biol. (1995) 128:509-523 !$#title Giant peroxisomes in oleic acid-induced Saccharomyces !1cerevisiae lacking the peroxisomal membrane protein Pmp27p. !$#cross-references MUID:95164555; PMID:7860627 !$#accession A56509 !'##molecule_type DNA !'##residues 1-236 ##label ERD !'##cross-references GB:X81465; NID:g683700; PIDN:CAA57223.1; !1PID:g683701 !$#accession B56509 !'##molecule_type protein !'##residues 2-28 ##label ER2 REFERENCE S60385 !$#authors Casamayor, A.; Aldea, M.; Casas, C.; Herrero, E.; Gamo, !1F.J.; Lafuente, M.J.; Gancedo, C.; Arino, J. !$#journal Yeast (1995) 11:1281-1288 !$#title DNA sequence analysis of a 13 kbp fragment of the left arm !1of yeast chromosome XV containing seven new open reading !1frames. !$#cross-references MUID:96132030; PMID:8553699 !$#accession S60389 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-236 ##label CAW !'##cross-references EMBL:Z48239; NID:g1163073; PIDN:CAA88280.1; !1PID:g886949 REFERENCE S62134 !$#authors Marshall, P.A.; Krimkevich, Y.I.; Lark, R.H.; Dyer, J.M.; !1Veenhuis, M.; Goodman, J.M. !$#journal J. Cell Biol. (1995) 129:345-355 !$#title Pmp27 promotes peroxisomal proliferation. !$#cross-references MUID:95238534; PMID:7721939 !$#accession S62134 !'##molecule_type DNA !'##residues 1-236 ##label MAR !'##cross-references EMBL:Z46846; NID:g791131; PIDN:CAA86903.1; !1PID:g791132 !$#accession S62148 !'##molecule_type protein !'##residues 2-30;192-207 ##label MAW REFERENCE S66814 !$#authors Arino, J.; Casamayor, A.; Gamo, F.J.; Gancedo, C.; Lafuente, !1M.J.; Aldea, M.; Casas, C.; Herrero, E. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S66844 !'##molecule_type DNA !'##residues 1-236 ##label ARI !'##cross-references EMBL:Z74889; NID:g1420049; PIDN:CAA99168.1; !1PID:g1420050; GSPDB:GN00015; MIPS:YOL147c !'##experimental_source strain S288C GENETICS !$#gene SGD:PEX11; PMP27; MIPS:YOL147c !'##cross-references MIPS:YOL147c; SGD:S0005507 !$#map_position 15L FUNCTION !$#description promotion of peroxisomal proliferation CLASSIFICATION #superfamily peroxisomal membrane protein PMP27 KEYWORDS peroxisome; transmembrane protein FEATURE !$2-236 #product peroxisomal membrane protein PMP27 #status !8experimental #label MAT SUMMARY #length 236 #molecular-weight 26875 #checksum 9236 SEQUENCE /// ENTRY A38331 #type complete TITLE LEP100 protein precursor - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A38331; S00756 REFERENCE A38331 !$#authors Zot, A.S.; Fambrough, D.M. !$#journal J. Biol. Chem. (1990) 265:20988-20995 !$#title Structure of a gene for a lysosomal membrane glycoprotein !1(LEP100). Housekeeping gene with unexpected exon !1organization. !$#cross-references MUID:91065904; PMID:2250003 !$#accession A38331 !'##molecule_type DNA !'##residues 1-414 ##label ZOT !'##cross-references GB:M59365; GB:J05679; NID:g212252; PIDN:AAA65947.1; !1PID:g212254 !'##note the authors translated the codon GAA for residue 163 as Gln REFERENCE S00756 !$#authors Fambrough, D.M.; Takeyasu, K.; Lippincott-Schwarz, J.; !1Siegel, N.R. !$#journal J. Cell Biol. (1988) 106:61-67 !$#title Structure of LEP100, a glycoprotein that shuttles between !1lysosomes and the plasma membrane, deduced from the !1nucleotide sequence of the encoding cDNA. !$#cross-references MUID:88115569; PMID:3339090 !$#accession S00756 !'##molecule_type mRNA !'##residues 1-2,'G',4-147,'V',149-324,'S',326-368,'M',370-414 ##label !1FAM !'##cross-references EMBL:X07775; NID:g63569; PIDN:CAA30601.1; !1PID:g63570 GENETICS !$#gene LEP100 CLASSIFICATION #superfamily lysosome-associated membrane protein KEYWORDS glycoprotein; lysosome; transmembrane protein FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-414 #product LEP100 protein #status predicted #label MAT SUMMARY #length 414 #molecular-weight 44776 #checksum 568 SEQUENCE /// ENTRY B31959 #type complete TITLE lysosome-associated membrane protein 2 precursor, splice form A [validated] - human ALTERNATE_NAMES lamp-2; lysosomal membrane glycoprotein 2 ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1990 #sequence_revision 01-Dec-1995 #text_change 08-Dec-2000 ACCESSIONS JC2414; S02151; A41078; B23656; B31959; A38446; A46044; !1S34738; I55386 REFERENCE JC2414 !$#authors Konecki, D.S.; Foetisch, K.; Schlotter, M.; Lichter-Konecki, !1U. !$#journal Biochem. Biophys. Res. Commun. (1994) 205:1-5 !$#title Complete cDNA sequence of human lysosome-associated membrane !1protein-2. !$#cross-references MUID:95091708; PMID:7999007 !$#accession JC2414 !'##molecule_type mRNA !'##residues 1-410 ##label KON !'##cross-references EMBL:X77196; NID:g704462; PIDN:CAA54416.1; !1PID:g704463 REFERENCE S02150 !$#authors Mane, S.M.; Marzella, L.; Bainton, D.F.; Holt, V.K.; Cha, !1Y.; Hildreth, J.E.K.; August, J.T. !$#journal Arch. Biochem. Biophys. (1989) 268:360-378 !$#title Purification and characterization of human lysosomal !1membrane glycoproteins. !$#cross-references MUID:89104438; PMID:2912382 !$#accession S02151 !'##molecule_type protein !'##residues 29-31,'X',33-37,'X',39-40,'X',42-48,'X',50-66 ##label MAN1 REFERENCE A41078 !$#authors Guan, E.; Burgess, W.H.; Robinson, S.L.; Goodman, E.B.; !1McTigue, K.J.; Tenner, A.J. !$#journal J. Biol. Chem. (1991) 266:20345-20355 !$#title Phagocytic cell molecules that bind the collagen-like region !1of C1q. Involvement in the C1q-mediated enhancement of !1phagocytosis. !$#cross-references MUID:92041866; PMID:1939090 !$#accession A41078 !'##status preliminary !'##molecule_type protein !'##residues 87-103;144-152;280-288,'XK';297-307 ##label GUA REFERENCE A23656 !$#authors Carlsson, S.R.; Fukuda, M. !$#journal J. Biol. Chem. (1990) 265:20488-20495 !$#title The polylactosaminoglycans of human lysosomal membrane !1glycoproteins lamp-1 and lamp-2. Localization on the peptide !1backbones. !$#cross-references MUID:91056099; PMID:2243102 !$#accession B23656 !'##status preliminary !'##molecule_type protein !'##residues 29-45;304-312 ##label CAR1 REFERENCE A92699 !$#authors Fukuda, M.; Viitala, J.; Matteson, J.; Carlsson, S.R. !$#journal J. Biol. Chem. (1988) 263:18920-18928 !$#title Cloning of cDNAs encoding human lysosomal membrane !1glycoproteins, h-lamp-1 and h-lamp-2. Comparison of their !1deduced amino acid sequences. !$#cross-references MUID:89066687; PMID:3198605 !$#accession B31959 !'##molecule_type mRNA !'##residues 1-321,'MP',324,327-410 ##label FUK !'##cross-references GB:J04183; NID:g186929; PIDN:AAA60383.1; !1PID:g307110 REFERENCE A38446 !$#authors Manoni, M.; Tribioli, C.; Lazzari, B.; DeBellis, G.; !1Patrosso, C.; Pergolizzi, R.; Pellegrini, M.; Maestrini, E.; !1Rivella, S.; Vezzoni, P.; Toniolo, D. !$#journal Genomics (1991) 9:551-554 !$#title The nucleotide sequence of a CpG island demonstrates the !1presence of the first exon of the gene encoding the human !1lysosomal membrane protein lamp2 and assigns the gene to !1Xq24. !$#cross-references MUID:91236178; PMID:2032724 !$#accession A38446 !'##molecule_type DNA !'##residues 1-22 ##label MAN2 !'##note the cited accession number, M37005, is not in Genbank release !1103 REFERENCE A46044 !$#authors Sawada, R.; Jardine, K.A.; Fukuda, M. !$#journal J. Biol. Chem. (1993) 268:9014-9022 !$#title The genes of major lysosomal membrane glycoproteins, lamp-1 !1and lamp-2. 5'-flanking sequence of lamp-2 gene and !1comparison of exon organization in two genes. !$#cross-references MUID:93232065; PMID:8517882 !$#accession A46044 !'##status preliminary !'##molecule_type DNA !'##residues 1-110,'N',112-118,'D',120-219,'P',221-327,329-410 ##label !1SAW1 !'##cross-references GB:L09717; NID:g292268 !'##experimental_source placenta !'##note sequence extracted from NCBI backbone (NCBIN:129826, !1NCBIN:129828, NCBIN:129830, NCBIN:129832, NCBIN:129834, !1NCBIN:129836, NCBIN:129838, NCBIN:129840, NCBIN:129842, !1NCBIP:129823) !'##note sequence inconsistent with the nucleotide translation REFERENCE S34737 !$#authors Carlsson, S.R.; Lycksell, P.O.; Fukuda, M. !$#journal Arch. Biochem. Biophys. (1993) 304:65-73 !$#title Assignment of O-glycan attachment sites to the hinge-like !1regions of human lysosomal membrane glycoproteins lamp-1 and !1lamp-2. !$#cross-references MUID:93312023; PMID:8323299 !$#accession S34738 !'##molecule_type protein !'##residues 187-215 ##label CAR2 REFERENCE I55386 !$#authors Sawada, R.; Jardine, K.A.; Fukuda, M. !$#journal J. Biol. Chem. (1993) 268:13010 !$#title The genes of major lysosomal membrane glycoproteins lamp-1 !1and lamp-2. The 5'-flanking sequence of lamp-2 gene and !1comparison of exon organization in two genes. !$#cross-references MUID:93286154; PMID:8509432 !$#accession I55386 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 321-329 ##label SAW2 !'##cross-references GB:S62577; NID:g386154; PIDN:AAB27101.1; !1PID:g386155 COMMENT For splice form B, see PIR:JC4317. GENETICS !$#gene GDB:LAMP2 !'##cross-references GDB:125376; OMIM:309060 !$#map_position Xq24-Xq24 FUNCTION !$#description protects the lysosomal membrane from autodigestion and !1serves as adhesion molecules on activated platelets, !1cytotoxic T-cells, macrophages, embryonic cells and !1metastatic tumor cells CLASSIFICATION #superfamily lysosome-associated membrane protein KEYWORDS alternative splicing; glycoprotein; lysosome; transmembrane !1protein FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-410 #product lysosome-associated membrane protein-2, !8splice form A #status experimental #label MAT\ !$29-375 #domain lysosomal lumenal #status predicted #label !8LYS\ !$376-399 #domain transmembrane #status predicted #label TMM\ !$400-410 #domain intracellular #status predicted #label CYT\ !$32,38,307 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$49,58,75,101,123, !$179,229,242,257, !$275,300,317,356 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$195 #binding_site carbohydrate (Ser) (covalent) #status !8experimental\ !$196,200,203,204, !$210,211 #binding_site carbohydrate (Thr) (covalent) #status !8experimental\ !$207 #binding_site carbohydrate (Ser) (covalent) (partial) !8#status experimental\ !$209 #binding_site carbohydrate (Thr) (covalent) (partial) !8#status experimental SUMMARY #length 410 #molecular-weight 44960 #checksum 8437 SEQUENCE /// ENTRY JC4317 #type complete TITLE lysosome-associated membrane protein 2 precursor, splice form B - human ALTERNATE_NAMES lamp-2; lysosomal membrane glycoprotein 2 ORGANISM #formal_name Homo sapiens #common_name man DATE 18-Feb-2000 #sequence_revision 18-Feb-2000 #text_change 18-Feb-2000 ACCESSIONS JC4317; A48042; G02094 REFERENCE JC4317 !$#authors Konecki, D.S.; Foetisch, K.; Zimmer, K.P.; Schlotter, M.; !1Lichter-Konecki, U. !$#journal Biochem. Biophys. Res. Commun. (1995) 215:757-767 !$#title An alternatively spliced form of the human !1lysosome-associated membrane protein-2 gene is expressed in !1a tissue-specific manner. !$#cross-references MUID:96011842; PMID:7488019 !$#accession JC4317 !'##molecule_type mRNA !'##residues 1-410 ##label KON !'##cross-references EMBL:U36336; NID:g1209628; PIDN:AAA91149.1; !1PID:g1209629 REFERENCE A48042 !$#authors Fritz, G.; Dosch, J.; Thielmann, H.W.; Kaina, B. !$#journal J. Biol. Chem. (1993) 268:21102-21112 !$#title Molecular and cellular characterization of Mex-/ !1methylation-resistant phenotype. Gene and cDNA cloning, !1serum dependence, and tumor suppression of transfectant !1strains. !$#cross-references MUID:94012660; PMID:8407947 !$#accession A48042 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-7,'RFRS',11,'LR',14-52,'G',54-262,'AAAV',267-268,270-410 !1##label FRI !'##cross-references PIDN:AAB28483.1; PID:g435756 !'##experimental_source diploid fibroblast !'##note sequence extracted from NCBI backbone (NCBIP:138512) COMMENT For splice form A, see PIR:B31959. GENETICS !$#gene GDB:LAMP2 !'##cross-references GDB:125376; OMIM:309060 !$#map_position Xq24-Xq24 FUNCTION !$#description protects the lysosomal membrane from autodigestion and !1serves as adhesion molecules on activated platelets, !1cytotoxic T-cells, macrophages, embryonic cells and !1metastatic tumor cells CLASSIFICATION #superfamily lysosome-associated membrane protein KEYWORDS alternative splicing; glycoprotein; lysosome; transmembrane !1protein FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$29-410 #product lysosome-associated membrane protein-2, !8splice form B #status predicted #label MAT\ !$29-375 #domain lysosomal lumenal #status predicted #label !8LYS\ !$375-399 #domain transmembrane #status predicted #label TMM\ !$400-410 #domain intracellular #status predicted #label CYT\ !$32,38,307 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$49,58,75,101,123, !$179,229,242,257, !$275,300,317,356 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$195,207 #binding_site carbohydrate (Ser) (covalent) #status !8predicted\ !$196,200,203,204, !$209,210,211 #binding_site carbohydrate (Thr) (covalent) #status !8predicted SUMMARY #length 410 #molecular-weight 44955 #checksum 789 SEQUENCE /// ENTRY A31959 #type complete TITLE lysosome-associated membrane protein 1 precursor - human ALTERNATE_NAMES lysosomal-associated membrane protein lamp A; major lysosomal membrane glycoprotein lamp-1 ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1990 #sequence_revision 01-Dec-1995 #text_change 22-Jun-1999 ACCESSIONS A31959; B46044; S02150; A23656; A32685; S34737; A30210; !1B30210 REFERENCE A92699 !$#authors Fukuda, M.; Viitala, J.; Matteson, J.; Carlsson, S.R. !$#journal J. Biol. Chem. (1988) 263:18920-18928 !$#title Cloning of cDNAs encoding human lysosomal membrane !1glycoproteins, h-lamp-1 and h-lamp-2. Comparison of their !1deduced amino acid sequences. !$#cross-references MUID:89066687; PMID:3198605 !$#accession A31959 !'##molecule_type mRNA !'##residues 1-416 ##label FUK !'##cross-references GB:J04182; NID:g186927; PIDN:AAA60382.1; !1PID:g307109 REFERENCE A46044 !$#authors Sawada, R.; Jardine, K.A.; Fukuda, M. !$#journal J. Biol. Chem. (1993) 268:9014-9022 !$#title The genes of major lysosomal membrane glycoproteins, lamp-1 !1and lamp-2. 5'-flanking sequence of lamp-2 gene and !1comparison of exon organization in two genes. !$#cross-references MUID:93232065; PMID:8517882 !$#accession B46044 !'##status preliminary; nucleic acid sequence not shown; not compared !1with conceptual translation !'##molecule_type DNA !'##residues 1-416 ##label SAW !'##experimental_source placenta !'##note sequence extracted from NCBI backbone (NCBIP:129878) REFERENCE S02150 !$#authors Mane, S.M.; Marzella, L.; Bainton, D.F.; Holt, V.K.; Cha, !1Y.; Hildreth, J.E.K.; August, J.T. !$#journal Arch. Biochem. Biophys. (1989) 268:360-378 !$#title Purification and characterization of human lysosomal !1membrane glycoproteins. !$#cross-references MUID:89104438; PMID:2912382 !$#accession S02150 !'##molecule_type protein !'##residues 28-35,'X',37-39,'X',41-43,'X',45-58 ##label MAN REFERENCE A23656 !$#authors Carlsson, S.R.; Fukuda, M. !$#journal J. Biol. Chem. (1990) 265:20488-20495 !$#title The polylactosaminoglycans of human lysosomal membrane !1glycoproteins lamp-1 and lamp-2. Localization on the peptide !1backbones. !$#cross-references MUID:91056099; PMID:2243102 !$#accession A23656 !'##status preliminary !'##molecule_type protein !'##residues 57-71;116-135;215-234 ##label CAR REFERENCE A32685 !$#authors Carlsson, S.R.; Fukuda, M. !$#journal J. Biol. Chem. (1989) 264:20526-20531 !$#title Structure of human lysosomal membrane glycoprotein 1. !1Assignment of disulfide bonds and visualization of its !1domain arrangement. !$#cross-references MUID:90062189; PMID:2584229 !$#accession A32685 !'##molecule_type protein !'##residues 31-35;72-74,'X',76-77;144-153;177-179,'X', !1181-187;215-219;255-259,'X',261-265;335-339;369-375 ##label !1CA2 REFERENCE S34737 !$#authors Carlsson, S.R.; Lycksell, P.O.; Fukuda, M. !$#journal Arch. Biochem. Biophys. (1993) 304:65-73 !$#title Assignment of O-glycan attachment sites to the hinge-like !1regions of human lysosomal membrane glycoproteins lamp-1 and !1lamp-2. !$#cross-references MUID:93312023; PMID:8323299 !$#accession S34737 !'##molecule_type protein !'##residues 190-214 ##label CA3 REFERENCE A30210 !$#authors Viitala, J.; Carlsson, S.R.; Siebert, P.D.; Fukuda, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:3743-3747 !$#title Molecular cloning of cDNAs encoding lamp A, a human !1lysosomal membrane glycoprotein with apparent M-r !1approximately 120,000. !$#cross-references MUID:88234502; PMID:3131762 !$#accession A30210 !'##molecule_type mRNA !'##residues 'MARGGRVR',40-416 ##label VII !'##cross-references GB:J03263; NID:g187178; PIDN:AAA59524.1; !1PID:g307132 !$#accession B30210 !'##molecule_type protein !'##residues 116-119,'X',121-128,'X',130-131,'X',133-135;163,'X', !1165-179,'X',181-189,'X',191-195,'X',197;314-318 ##label VI2 GENETICS !$#gene GDB:LAMP1 !'##cross-references GDB:120137; OMIM:153330 !$#map_position 13q34-13q34 CLASSIFICATION #superfamily lysosome-associated membrane protein KEYWORDS glycoprotein; lysosome; transmembrane protein FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-416 #product lysosomal membrane glycoprotein 1 #status !8predicted #label MAT\ !$28-381 #domain lysosomal lumenal #status predicted #label !8LYS\ !$382-405 #domain transmembrane #status predicted #label TMM\ !$406-416 #domain intracellular #status predicted #label CYT\ !$36,44,83,102,106, !$240,248,292,321,379 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$40-79,154-190, !$230-268,337-374 #disulfide_bonds #status experimental\ !$61,75,120,129,164, !$180,222,227,260 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$196 #binding_site carbohydrate (Ser) (covalent) (partial) !8#status experimental\ !$198,199 #binding_site carbohydrate (Thr) (covalent) #status !8experimental\ !$206,208,210 #binding_site carbohydrate (Ser) (covalent) #status !8experimental SUMMARY #length 416 #molecular-weight 44773 #checksum 9968 SEQUENCE /// ENTRY A56525 #type complete TITLE lysosomal integral membrane protein II - human ALTERNATE_NAMES lgp85; LIMP II; lysosomal membrane 85K sialoglycoprotein ORGANISM #formal_name Homo sapiens #common_name man DATE 19-Oct-1995 #sequence_revision 12-Apr-1996 #text_change 21-Jul-2000 ACCESSIONS A56525; JQ1523 REFERENCE A56525 !$#authors Calvo, D.; Dopazo, J.; Vega, M.A. !$#journal Genomics (1995) 25:100-106 !$#title The CD36, CLA-1 (CD36L1), and LIMPII (CD36L2) gene family: !1cellular distribution, chromosomal location, and genetic !1evolution. !$#cross-references MUID:95293360; PMID:7539776 !$#accession A56525 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-478 ##label CAL REFERENCE JQ1523 !$#authors Fujita, H.; Takata, Y.; Kono, A.; Tanaka, Y.; Takahashi, T.; !1Himeno, M.; Kato, K. !$#journal Biochem. Biophys. Res. Commun. (1992) 184:604-611 !$#title Isolation and sequencing of a cDNA clone encoding the 85KDa !1human lysosomal sialoglycoprotein (hLGP85) in human !1metastatic pancreas islet tumor cells. !$#cross-references MUID:92246940; PMID:1374238 !$#accession JQ1523 !'##molecule_type mRNA !'##residues 1-83,'E',85-478 ##label FUJ !'##cross-references GB:D12676; NID:g219702; PIDN:BAA02177.1; !1PID:g219703 !'##experimental_source pancreatic islet REFERENCE A57905 !$#authors Sandoval, I.V.; Arredondo, J.J.; Alcalde, J.; Noriega, A.G.; !1Vandekerckhove, J.; Jimenez, M.A.; Rico, M. !$#journal J. Biol. Chem. (1994) 269:6622-6631 !$#title The residues Leu(Ile)(475)-Ile(Leu, Val, Ala)(476), !1contained in the extended carboxyl cytoplasmic tail, are !1critical for targeting of the resident lysosomal membrane !1protein LIMP II to lysosomes. !$#cross-references MUID:94165051; PMID:7509809 !$#contents annotation; sorting signal GENETICS !$#gene GDB:CD36L2 !'##cross-references GDB:383649 !$#map_position 4pter-4qter CLASSIFICATION #superfamily lysosomal integral membrane protein II KEYWORDS glycoprotein; lysosome; transmembrane protein FEATURE !$2-478 #product lysosomal membrane 85K sialoglycoprotein !8#status predicted #label LYS\ !$2-3 #domain intracellular #status predicted #label CYT1\ !$4-26 #domain transmembrane #status predicted #label TR1\ !$27-432 #domain lysosomal lumenal #status predicted #label !8LLUM\ !$433-458 #domain transmembrane #status predicted #label TR2\ !$459-478 #domain intracellular #status predicted #label CYT2\ !$475-476 #region endosomal/lysosomal sorting signal\ !$45,68,105,206,224, !$249,304,325,412,430 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 478 #molecular-weight 54289 #checksum 9884 SEQUENCE /// ENTRY JH0241 #type complete TITLE 85K lysosomal membrane sialoglycoprotein - rat ALTERNATE_NAMES 74k lysosomal membrane protein LIMP ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 23-Nov-1991 #sequence_revision 12-Apr-1996 #text_change 16-Jun-2000 ACCESSIONS JH0241; PH0212; A41180 REFERENCE JH0241 !$#authors Fujita, H.; Ezaki, J.; Noguchi, Y.; Kono, A.; Himeno, M.; !1Kato, K. !$#journal Biochem. Biophys. Res. Commun. (1991) 178:444-452 !$#title Isolation and sequencing of a cDNA clone encoding 85KDa !1sialoglycoprotein in rat liver lysosomal membranes. !$#cross-references MUID:91315465; PMID:1859403 !$#accession JH0241 !'##molecule_type mRNA !'##residues 1-478 ##label FUJ !'##cross-references GB:D10587; GB:D90532; NID:g220803; PIDN:BAA01444.1; !1PID:g220804 !'##note the authors translated the codon CCT for residue 59 as Lys, TAT !1for residue 278 as Ile, and ATA for residue 279 as Tyr !$#accession PH0212 !'##molecule_type protein !'##residues 2-9;49-67;116-121;228-234;283-294;355-373 ##label FU2 !'##experimental_source liver REFERENCE A41180 !$#authors Vega, M.A.; Segui-Real, B.; Garcia, J.A.; Cales, C.; !1Rodriguez, F.; Vanderkerckhove, J.; Sandoval, I.V. !$#journal J. Biol. Chem. (1991) 266:16818-16824 !$#title Cloning, sequencing, and expression of a cDNA encoding rat !1LIMP II, a novel 74-kDa lysosomal membrane protein related !1to the surface adhesion protein CD36. !$#cross-references MUID:91358482; PMID:1715871 !$#accession A41180 !'##molecule_type mRNA !'##residues 1-478 ##label VEG !'##cross-references GB:M68965; NID:g205206; PIDN:AAA41531.1; !1PID:g205207 !'##note parts of this sequence, including the amino end of the mature !1protein, were confirmed by peptide sequencing REFERENCE A57905 !$#authors Sandoval, I.V.; Arredondo, J.J.; Alcalde, J.; Noriega, A.G.; !1Vandekerckhove, J.; Jimenez, M.A.; Rico, M. !$#journal J. Biol. Chem. (1994) 269:6622-6631 !$#title The residues Leu(Ile)(475)-Ile(Leu, Val, Ala)(476), !1contained in the extended carboxyl cytoplasmic tail, are !1critical for targeting of the resident lysosomal membrane !1protein LIMP II to lysosomes. !$#cross-references MUID:94165051; PMID:7509809 !$#contents annotation; sorting signal CLASSIFICATION #superfamily lysosomal integral membrane protein II KEYWORDS glycoprotein; transmembrane protein FEATURE !$2-478 #product 85K lysosomal membrane sialoglycoprotein !8#status experimental #label MAT\ !$2-3 #domain intracellular #status predicted #label CYT1\ !$4-26 #domain transmembrane #status predicted #label TR1\ !$27-432 #domain lysosomal lumenal #status predicted #label !8LYS\ !$433-458 #domain transmembrane #status predicted #label TR2\ !$459-478 #domain intracellular #status predicted #label CYT2\ !$475-476 #region endosomal/lysosomal sorting signal\ !$45,68,105,122,206, !$224,249,304,325, !$412,430 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 478 #molecular-weight 54091 #checksum 1237 SEQUENCE /// ENTRY A48528 #type complete TITLE membrane glycoprotein CLA-1 protein long form precursor - human ALTERNATE_NAMES CD36 and LIMP-II analogous-1 (CLA-1) CONTAINS membrane glycoprotein CLA-1, short splice form ORGANISM #formal_name Homo sapiens #common_name man DATE 07-Apr-1994 #sequence_revision 12-Apr-1996 #text_change 22-Jun-1999 ACCESSIONS S36656; A48528 REFERENCE S36656 !$#authors Vega, M. !$#submission submitted to the EMBL Data Library, April 1993 !$#accession S36656 !'##molecule_type mRNA !'##residues 1-509 ##label VEG !'##cross-references EMBL:Z22555; NID:g397606; PIDN:CAA80277.1; !1PID:g397607 !'##note this sequence report represents the long form REFERENCE A48528 !$#authors Calvo, D.; Vega, M.A. !$#journal J. Biol. Chem. (1993) 268:18929-18935 !$#title Identification, primary structure, and distribution of !1CLA-1, a novel member of the CD36/LIMPII gene family. !$#cross-references MUID:93366811; PMID:7689561 !$#accession A48528 !'##molecule_type mRNA !'##residues 1-42,143-509 ##label CAL !'##cross-references GB:Z22555 !'##note this sequence report represents the short form; the long form !1was also sequenced GENETICS !$#gene GDB:CD36L1 !'##cross-references GDB:228074 !$#map_position 12pter-12qter CLASSIFICATION #superfamily lysosomal integral membrane protein II KEYWORDS alternative splicing; blocked amino end; glycoprotein; !1lipoprotein; myristylation; surface antigen; thiolester !1bond; transmembrane protein FEATURE !$2-509 #product membrane glycoprotein CLA-1, long splice !8form #status predicted #label LMAT\ !$2-42,143-509 #product membrane glycoprotein CLA-1, short splice !8form #status predicted #label SMAT\ !$2-8 #domain intracellular #status predicted #label CYT1\ !$9-33 #domain transmembrane #status predicted #label TM1\ !$34-442 #domain extracellular #status predicted #label EXT\ !$443-464 #domain transmembrane #status predicted #label TM2\ !$465-509 #domain intracellular #status predicted #label CYT2\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$102,108,173,212, !$227,255,310,330 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 509 #molecular-weight 56913 #checksum 4410 SEQUENCE /// ENTRY A53920 #type complete TITLE scavenger receptor SR-BI - Chinese hamster ALTERNATE_NAMES CD36-related class B scavenger receptor ORGANISM #formal_name Cricetulus griseus #common_name Chinese hamster DATE 28-Jul-1995 #sequence_revision 12-Apr-1996 #text_change 22-Jun-1999 ACCESSIONS A53920 REFERENCE A53920 !$#authors Acton, S.L.; Scherer, P.E.; Lodish, H.F.; Krieger, M. !$#journal J. Biol. Chem. (1994) 269:21003-21009 !$#title Expression cloning of SR-BI, a CD36-related class B !1scavenger receptor. !$#cross-references MUID:94342261; PMID:7520436 !$#accession A53920 !'##molecule_type mRNA !'##residues 1-509 ##label ACT !'##cross-references GB:U11453; NID:g562021; PIDN:AAA61572.1; !1PID:g562022 FUNCTION !$#description mediates the endocytosis of modified lipoprotiens such as !1oxidized or acetylated LDL CLASSIFICATION #superfamily lysosomal integral membrane protein II KEYWORDS glycoprotein; transmembrane protein FEATURE !$2-8 #domain intracellular #status predicted #label CYT1\ !$9-33 #domain transmembrane #status predicted #label TM1\ !$34-442 #domain extracellular #status predicted #label EXT\ !$443-464 #domain transmembrane #status predicted #label TM2\ !$465-509 #domain intracellular #status predicted #label CYT2\ !$102,108,173,212, !$227,255,310,330 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 509 #molecular-weight 56735 #checksum 4028 SEQUENCE /// ENTRY A54870 #type complete TITLE cell adhesion receptor CD36 - human ALTERNATE_NAMES BE111 protein; collagen type I/thrombospondin receptor; PAS IV; platelet glycoprotein GPIIIb; platelet glycoprotein IV ORGANISM #formal_name Homo sapiens #common_name man DATE 07-Jul-1995 #sequence_revision 12-Apr-1996 #text_change 21-Jul-2000 ACCESSIONS A54870; JC2017; JC2016; A30989; A47534; A33357; D56793; !1A35577; I59613; A53212; S37041 REFERENCE A54870 !$#authors Armesilla, A.L.; Vega, M.A. !$#journal J. Biol. Chem. (1994) 269:18985-18991 !$#title Structural organization of the gene for human CD36 !1glycoprotein. !$#cross-references MUID:94308159; PMID:7518447 !$#accession A54870 !'##molecule_type DNA !'##residues 1-472 ##label ARM !'##cross-references GB:Z32770; NID:g525232; PIDN:CAA83662.1; !1PID:g525233 REFERENCE JC2016 !$#authors Taylor, K.T.; Tang, Y.; Sobieski, D.A.; Lipsky, R.H. !$#journal Gene (1993) 133:205-212 !$#title Characterization of two alternatively spliced !15'-untranslated exons of the human CD36 gene in different !1cell types. !$#cross-references MUID:94040811; PMID:7693552 !$#accession JC2017 !'##molecule_type DNA !'##residues 1-40 ##label TA2 !'##cross-references GB:L06849 !$#accession JC2016 !'##molecule_type mRNA !'##residues 1-373,'Q',375-472 ##label TAY !'##cross-references GB:L06850; NID:g180116; PIDN:AAA16068.1; !1PID:g180117 !'##note the authors translated the codon CAC for residue 242 as Asn and !1CAA for residue 374 as Glu REFERENCE A30989 !$#authors Oquendo, P.; Hundt, E.; Lawler, J.; Seed, B. !$#journal Cell (1989) 58:95-101 !$#title CD36 directly mediates cytoadherence of plasmodium !1falciparum parasitized erythrocytes. !$#cross-references MUID:89324065; PMID:2473841 !$#accession A30989 !'##molecule_type mRNA !'##residues 1-472 ##label OQU !'##cross-references GB:M24795; NID:g178670; PIDN:AAA35534.1; !1PID:g178671 REFERENCE A47534 !$#authors Fernandez-Ruiz, E.; Armesilla, A.L.; Sanchez-Madrid, F.; !1Vega, M.A. !$#journal Genomics (1993) 17:759-761 !$#title Gene encoding the collagen type I and thrombospondin !1receptor CD36 is located on chromosome 7q11.2. !$#cross-references MUID:94063924; PMID:7503937 !$#accession A47534 !'##molecule_type mRNA !'##residues 144-203 ##label FER !'##cross-references EMBL:Z22924; NID:g397604; PIDN:CAA80504.1; !1PID:g397605 !'##note sequence extracted from NCBI backbone (NCBIP:139701) REFERENCE A33357 !$#authors Tandon, N.N.; Lipsky, R.H.; Burgess, W.H.; Jamieson, G.A. !$#journal J. Biol. Chem. (1989) 264:7570-7575 !$#title Isolation and characterization of platelet glycoprotein IV !1(CD36). !$#cross-references MUID:89214205; PMID:2468669 !$#accession A33357 !'##molecule_type protein !'##residues 2,'X',4-6,'X',8-32,'PX',35-36,'F' ##label TAN REFERENCE A56793 !$#authors Catimel, B.; Parmentier, S.; Leung, L.L.; McGregor, J.L. !$#journal Biochem. J. (1991) 279:419-425 !$#title Separation of important new platelet glycoproteins (GPIa, !1GPIc, GPIc*, GPIIa and GMP-140) by f.p.l.c. Characterization !1by monoclonal antibodies and gas-phase sequencing. !$#cross-references MUID:92061944; PMID:1953640 !$#accession D56793 !'##molecule_type protein !'##residues 2,'X',4-6,'X',8-23 ##label CAT !'##experimental_source platelet REFERENCE A35577 !$#authors Greenwalt, D.E.; Watt, K.W.K.; So, O.Y.; Jiwani, N. !$#journal Biochemistry (1990) 29:7054-7059 !$#title PAS IV, an integral membrane protein of mammary epithelial !1cells, is related to platelet and endothelial cell CD36 (GP !1IV). !$#cross-references MUID:91027734; PMID:1699598 !$#accession A35577 !'##molecule_type protein !'##residues 'XX',4,'X',6,'X',8-30 ##label GRE !'##experimental_source milk fat globule membrane, lactating mammary !1tissue epithelial cells REFERENCE I59613 !$#authors Wyler, B.; Daviet, L.; Bortkiewicz, H.; Bordet, J.C.; !1McGregor, J.L. !$#journal Thromb. Haemost. (1993) 70:500-505 !$#title Cloning of the cDNA encoding human platelet CD36: comparison !1to PCR amplified fragments of monocyte, endothelial and HEL !1cells. !$#cross-references MUID:94082337; PMID:7505064 !$#accession I59613 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-43,'R',45-237,'D',239-472 ##label RES !'##cross-references GB:S67532; NID:g456912; PIDN:AAD13993.1; !1PID:g4261693 REFERENCE A53212 !$#authors Tang, Y.; Taylor, K.T.; Sobieski, D.A.; Medved, E.S.; !1Lipsky, R.H. !$#journal J. Biol. Chem. (1994) 269:6011-6015 !$#title Identification of a human CD36 isoform produced by exon !1skipping. Conservation of exon organization and pre-mRNA !1splicing patterns with a CD36 gene family member, CLA-1. !$#cross-references MUID:94164961; PMID:7509795 !$#accession A53212 !'##status preliminary !'##molecule_type DNA !'##residues 1-40,144-169,'ILNSLINKSKSSM',170-185 ##label TA3 !'##cross-references GB:L06849 COMMENT This protein mediates the interaction of platelets with !1collagen and thrombospondin. GENETICS !$#gene GDB:CD36 !'##cross-references GDB:138800; OMIM:173510 !$#map_position 7q11.2-7q11.2 !$#introns 40/3; 94/2; 143/3; 185/2 CLASSIFICATION #superfamily lysosomal integral membrane protein II KEYWORDS alternative splicing; blocked amino end; cell adhesion; !1glycoprotein; lipoprotein; myristylation; platelet; !1receptor; surface antigen; thiolester bond; transmembrane !1protein FEATURE !$2-472 #product cell adhesion receptor CD36 #status !8predicted #label MAT\ !$2-6 #domain intracellular #status predicted #label CYT1\ !$7-30 #domain transmembrane #status predicted #label TM1\ !$31-439 #domain extracellular #status predicted #label EXT\ !$440-466 #domain transmembrane #status predicted #label TM2\ !$467-472 #domain intracellular #status predicted #label CYT2\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$3,7,464,466 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$79,102,134,163,205, !$220,235,247,417 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 472 #molecular-weight 53053 #checksum 6914 SEQUENCE /// ENTRY A47402 #type complete TITLE fatty acid binding/transport protein - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 19-May-1995 #sequence_revision 12-Apr-1996 #text_change 22-Jun-1999 ACCESSIONS A47402 REFERENCE A47402 !$#authors Abumrad, N.A.; El-Maghrabi, M.R.; Amri, E.Z.; Lopez, E.; !1Grimaldi, P.A. !$#journal J. Biol. Chem. (1993) 268:17665-17668 !$#title Cloning of a rat adipocyte membrane protein implicated in !1binding or transport of long-chain fatty acids that is !1induced during preadipocyte differentiation. Homology with !1human CD36. !$#cross-references MUID:93352566; PMID:7688729 !$#accession A47402 !'##molecule_type mRNA !'##residues 1-472 ##label ABU !'##cross-references GB:L19658; NID:g310112; PIDN:AAA02878.1; !1PID:g310113 CLASSIFICATION #superfamily lysosomal integral membrane protein II KEYWORDS glycoprotein; transmembrane protein FEATURE !$2-6 #domain intracellular #status predicted #label CYT1\ !$7-30 #domain transmembrane #status predicted #label TM1\ !$31-439 #domain extracellular #status predicted #label EXT\ !$440-466 #domain transmembrane #status predicted #label TM2\ !$467-472 #domain intracellular #status predicted #label CYT2\ !$79,102,134,205,220, !$235,247,417 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 472 #molecular-weight 52597 #checksum 9075 SEQUENCE /// ENTRY S43137 #type complete TITLE D-CD36 protein - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S43137; S43136 REFERENCE S43136 !$#authors Franc, N.; Dimarcq, J.; Hoffmann, J.; Lagueux, M. !$#submission submitted to the EMBL Data Library, March 1994 !$#description d-CD36 : a second Drosophila gene related to the CD36 family !1of cell adhesion molecules. !$#accession S43137 !'##status preliminary !'##molecule_type mRNA !'##residues 1-457 ##label FRA !'##cross-references EMBL:Z31583; NID:g468537; PIDN:CAA83455.1; !1PID:g468538; EMBL:Z31582; NID:g468535; PID:g468536 GENETICS !$#gene FlyBase:croquemort !'##cross-references FlyBase:FBgn0015924 CLASSIFICATION #superfamily lysosomal integral membrane protein II SUMMARY #length 457 #molecular-weight 52318 #checksum 3282 SEQUENCE /// ENTRY S38957 #type complete TITLE epithelial membrane protein - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 07-Oct-1994 #sequence_revision 12-Apr-1996 #text_change 22-Jun-1999 ACCESSIONS S38957 REFERENCE S38957 !$#authors Hart, K.; Wilcox, M. !$#journal J. Mol. Biol. (1993) 234:249-253 !$#title A Drosophila gene encoding an epithelial membrane protein !1with homology to CD36/LIMP II. !$#cross-references MUID:94047068; PMID:7693949 !$#accession S38957 !'##molecule_type mRNA !'##residues 1-519 ##label HAR !'##cross-references EMBL:X73332; NID:g429163; PIDN:CAA51759.1; !1PID:g429164 GENETICS !$#gene FlyBase:emp !'##cross-references FlyBase:FBgn0010435 CLASSIFICATION #superfamily lysosomal integral membrane protein II KEYWORDS transmembrane protein FEATURE !$2-19 #domain intracellular #status predicted #label CYT1\ !$20-39 #domain transmembrane #status predicted #label TM1\ !$460-482 #domain transmembrane #status predicted #label TM2\ !$483-519 #domain intracellular #status predicted #label CYT2 SUMMARY #length 519 #molecular-weight 58505 #checksum 729 SEQUENCE /// ENTRY A57013 #type complete TITLE early endosome antigen 1 - human ALTERNATE_NAMES endosome-associated protein ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A57013; S44243 REFERENCE A57013 !$#authors Mu, F.T.; Callaghan, J.M.; Steele-Mortimer, O.; Stenmark, !1H.; Parton, R.G.; Campbell, P.L.; McCluskey, J.; Yeo, J.P.; !1Tock, E.P.; Toh, B.H. !$#journal J. Biol. Chem. (1995) 270:13503-13511 !$#title EEA1, an early endosome-associated protein. EEA1 is a !1conserved alpha-helical peripheral membrane protein flanked !1by cysteine 'fingers' and contains a calmodulin-binding IQ !1motif. !$#cross-references MUID:95286647; PMID:7768953 !$#accession A57013 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-1410 ##label RES !'##cross-references GB:L40157; NID:g1016367; PIDN:AAA79121.1; !1PID:g1016368 REFERENCE S44243 !$#authors Seelig, H.P. !$#submission submitted to the EMBL Data Library, April 1994 !$#accession S44243 !'##status preliminary !'##molecule_type mRNA !'##residues 1-254,'C',256-257,'LQ',260-276,'A',278-283,'A',285-519,'D', !1521-574,'EQ',577-582,'KL',585-679,'Q',681-1325,'A',1326-1410 !1##label SEE !'##cross-references EMBL:X78998; NID:g475933; PIDN:CAA55632.1; !1PID:g475934 GENETICS !$#gene GDB:EEA1 !'##cross-references GDB:1369996 CLASSIFICATION #superfamily human early endosome antigen 1 KEYWORDS calmodulin binding; endocytosis; metal binding; peripheral !1membrane protein; zinc finger SUMMARY #length 1410 #molecular-weight 162496 #checksum 7251 SEQUENCE /// ENTRY A64545 #type complete TITLE fatty acid/phospholipid synthesis protein - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A64545 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession A64545 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-338 ##label TOM !'##cross-references GB:AE000540; GB:AE000511; NID:g2313287; !1PIDN:AAD07269.1; PID:g2313290; TIGR:HP0201 CLASSIFICATION #superfamily phospholipid synthesis protein SUMMARY #length 338 #molecular-weight 36483 #checksum 3523 SEQUENCE /// ENTRY S75456 #type complete TITLE protein plsX - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein slr1510 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S75456 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75456 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-348 ##label KAN !'##cross-references EMBL:D90911; GB:AB001339; NID:g1653083; !1PIDN:BAA18017.1; PID:g1653101 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene plsX CLASSIFICATION #superfamily phospholipid synthesis protein SUMMARY #length 348 #molecular-weight 37285 #checksum 1704 SEQUENCE /// ENTRY G64852 #type complete TITLE fatty acid/phospholipid synthesis protein plsX homolog - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS G64852 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64852 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-346 ##label BLAT !'##cross-references GB:AE000209; GB:U00096; NID:g1787322; !1PIDN:AAC74174.1; PID:g1787331; UWGP:b1090 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene plsX CLASSIFICATION #superfamily phospholipid synthesis protein KEYWORDS fatty acid biosynthesis; phospholipid biosynthesis SUMMARY #length 346 #molecular-weight 37100 #checksum 5298 SEQUENCE /// ENTRY B41608 #type complete TITLE hypothetical protein 2 - Rhodobacter capsulatus ORGANISM #formal_name Rhodobacter capsulatus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B41608 REFERENCE A41608 !$#authors Toussaint, B.; Bosc, C.; Richaud, P.; Colbeau, A.; Vignais, !1P.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:10749-10753 !$#title A mutation in a Rhodobacter capsulatus gene encoding an !1integration host factor-like protein impairs in vivo !1hydrogenase expression. !$#cross-references MUID:92073365; PMID:1961742 !$#accession B41608 !'##status preliminary !'##molecule_type DNA !'##residues 1-399 ##label TOU !'##cross-references GB:M84030; GB:M62764; NID:g151940; PIDN:AAA26126.1; !1PID:g151942 CLASSIFICATION #superfamily phospholipid synthesis protein SUMMARY #length 399 #molecular-weight 41052 #checksum 713 SEQUENCE /// ENTRY G64240 #type complete TITLE fatty acid/phospholipid synthesis protein plsX homolog - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 07-Dec-1999 ACCESSIONS G64240 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession G64240 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-328 ##label TIGR !'##cross-references GB:U39721; GB:L43967; NID:g1046072; PID:g1046077; !1TIGR:MG368 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily phospholipid synthesis protein SUMMARY #length 328 #molecular-weight 36502 #checksum 4270 SEQUENCE /// ENTRY S73622 #type complete TITLE fatty acid/phospholipid synthesis protein plsX - Mycoplasma pneumoniae (strain ATCC 29342) ALTERNATE_NAMES hypothetical protein G12_orf328a ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Dec-1999 ACCESSIONS S73622 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73622 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-328 ##label HIM !'##cross-references EMBL:AE000027; GB:U00089; NID:g1673941; !1PIDN:AAB95944.1; PID:g1673967 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#gene plsX !$#genetic_code SGC3 CLASSIFICATION #superfamily phospholipid synthesis protein SUMMARY #length 328 #molecular-weight 36664 #checksum 7438 SEQUENCE /// ENTRY GFHUE #type complete TITLE glycophorin A precursor, blood group N allele [validated] - human ALTERNATE_NAMES glycoprotein alpha; MN-glycoprotein; PAS-2; sialoglycoprotein alpha CONTAINS glycophorin Erik I-IV ORGANISM #formal_name Homo sapiens #common_name man DATE 24-Apr-1984 #sequence_revision 23-Mar-1995 #text_change 08-Dec-2000 ACCESSIONS S01304; A93801; A94584; B39785; I82987; A49566; A03183 REFERENCE S01304 !$#authors Tate, C.G.; Tanner, M.J.A. !$#journal Biochem. J. (1988) 254:743-750 !$#title Isolation of cDNA clones for human erythrocyte membrane !1sialoglycoproteins alpha and delta. !$#cross-references MUID:89061610; PMID:3196288 !$#accession S01304 !'##molecule_type mRNA !'##residues 1-150 ##label TAT !'##cross-references EMBL:X08054; NID:g31834; PIDN:CAA30843.1; !1PID:g31835 REFERENCE A93801 !$#authors Tomita, M.; Marchesi, V.T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1975) 72:2964-2968 !$#title Amino-acid sequence and oligosaccharide attachment sites of !1human erythrocyte glycophorin. !$#cross-references MUID:76053044; PMID:1059087 !$#accession A93801 !'##molecule_type protein !'##residues 20-29,'T',31-35,'S',37-89,'I',91-95,'V',97-150 ##label TOM !'##note this sequence has been revised in A94584 REFERENCE A94584 !$#authors Furthmayr, H.; Galardy, R.; Tomita, M.; Marchesi, V.T. !$#submission submitted to the Atlas, June 1977 !$#accession A94584 !'##molecule_type protein !'##residues 81-120 ##label FUR REFERENCE A39785 !$#authors Huang, C.H.; Blumenfeld, O.O. !$#journal J. Biol. Chem. (1991) 266:7248-7255 !$#title Molecular genetics of human erythrocyte MiIII and MiVI !1glycophorins. Use of a pseudoexon in construction of two !1delta-alpha-delta hybrid genes resulting in antigenic !1diversification. !$#cross-references MUID:91201388; PMID:2016325 !$#accession B39785 !'##molecule_type DNA !'##residues 20-90 ##label HUA1 !'##cross-references GB:M60707 REFERENCE I60083 !$#authors DuPont, B.R.; Grant, S.G.; Oto, S.H.; Bigbee, W.L.; Jensen, !1R.H.; Langlois, R.G. !$#journal Vox Sang. (1995) 68:121-129 !$#title Molecular characterization of glycophorin A transcripts in !1human erythroid cells using RT-PCR, allele-specific !1restriction, and sequencing. !$#cross-references MUID:95282423; PMID:7762218 !$#accession I82987 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 10-12,'A',14-34 ##label DUP !'##cross-references GB:S77082; NID:g913056; PIDN:AAB34408.1; !1PID:g913057 REFERENCE A49566 !$#authors Huang, C.; Reid, M.E.; Daniels, G.; Blumenfeld, O.O. !$#journal J. Biol. Chem. (1993) 268:25902-25908 !$#title Alteration of splice site selection by an exon mutation in !1the human glycophorin A gene. !$#cross-references MUID:94064669; PMID:8245024 !$#accession A49566 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-12,78-150 ##label HUA2 !'##cross-references EMBL:U00179; NID:g392432; PIDN:AAA18258.1; !1PID:g392433 !'##experimental_source glycophorin Erik I-IV !'##note this sequence has a mutation causing abnormal splicing COMMENT Glycophorin A is the major intrinsic membrane protein of the !1erythrocyte. COMMENT The MN blood group antigen system reflects allelic variation !1of this protein (see PIR:A25131). GENETICS !$#gene GDB:GYPA !'##cross-references GDB:118890; OMIM:111300 !$#map_position 4q28-4q31 CLASSIFICATION #superfamily glycophorin KEYWORDS blood group; erythrocyte; sialoglycoprotein; transmembrane !1protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-150 #product glycophorin A #status experimental #label !8MAT\ !$20-91 #domain extracellular #status predicted #label EXT\ !$92-114 #domain transmembrane #status predicted #label MEM\ !$115-150 #domain intracellular #status predicted #label INT\ !$21,30,32,33,34,41, !$63,66 #binding_site carbohydrate (Ser) (covalent) #status !8experimental\ !$22,23,29,31,44,56, !$69 #binding_site carbohydrate (Thr) (covalent) #status !8experimental\ !$36,47,52 #binding_site carbohydrate (Thr) (covalent) #status !8predicted\ !$38,42 #binding_site carbohydrate (Ser) (covalent) #status !8predicted\ !$45 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 150 #molecular-weight 16429 #checksum 7379 SEQUENCE /// ENTRY A25131 #type complete TITLE glycophorin A precursor, blood group M allele [validated] - human ALTERNATE_NAMES glycoprotein alpha; MN-glycoprotein; PAS-2; sialoglycoprotein alpha CONTAINS glycophorin Mz II-IV; glycophorin Mz II-V ORGANISM #formal_name Homo sapiens #common_name man DATE 25-Oct-1987 #sequence_revision 23-Mar-1995 #text_change 08-Dec-2000 ACCESSIONS A33931; I54065; S06254; I59456; A25131; S00333; JX0337; !1S11567; A54468; B54468; S09683; S05425; S18490; I60853; !1I60852 REFERENCE A33931 !$#authors Kudo, S.; Fukuda, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:4619-4623 !$#title Structural organization of glycophorin A and B genes: !1glycophorin B gene evolved by homologous recombination at !1Alu repeat sequences. !$#cross-references MUID:89282822; PMID:2734312 !$#accession A33931 !'##molecule_type DNA !'##residues 1-150 ##label KUD !'##cross-references GB:M24123; GB:M24134; GB:M24124; GB:M24125; !1GB:M24126; GB:M24127; GB:M24128; NID:g183720; !1PIDN:AAA52768.1; PID:g386760 REFERENCE I54065 !$#authors Vignal, A.; London, J.; Rahuel, C.; Cartron, J. !$#journal Gene (1990) 95:289-293 !$#title Promoter sequence and chromosomal organization of the genes !1encoding glycophorins A, B and E. !$#cross-references MUID:91065544; PMID:2249783 !$#accession I54065 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-12 ##label VIG !'##cross-references GB:M57232; NID:g183471; PIDN:AAA35923.1; !1PID:g553311 REFERENCE S06254 !$#authors Siebert, P.D.; Fukuda, M. !$#journal Rev. Fr. Transfus. Immunohematol. (1986) 29:251-266 !$#title Molecular biological study of the structure and expression !1of human glycophorin A. !$#cross-references MUID:87119742; PMID:3809885 !$#accession S06254 !'##molecule_type mRNA !'##residues 1-150 ##label SIE1 !$#accession I59456 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 'DLR',1-145 ##label SIE2 !'##cross-references GB:M36281; NID:g183724; PIDN:AAA52624.1; !1PID:g183725 !'##note in GenBank HUMGYPAA the citation is incorrect and the !1translation begins before the initiation codon REFERENCE A25131 !$#authors Siebert, P.D.; Fukuda, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:1665-1669 !$#title Isolation and characterization of human glycophorin A cDNA !1clones by a synthetic oligonucleotide approach: nucleotide !1sequence and mRNA structure. !$#cross-references MUID:86149364; PMID:3456608 !$#accession A25131 !'##molecule_type mRNA !'##residues 1-150 ##label SIE3 !'##cross-references GB:M12857; GB:J02578; NID:g183304; PIDN:AAA88044.1; !1PID:g183305 REFERENCE S00333 !$#authors Rahuel, C.; London, J.; d'Auriol, L.; Mattei, M.G.; !1Tournamille, C.; Skrzynia, C.; Lebouc, Y.; Galibert, F.; !1Cartron, J.P. !$#journal Eur. J. Biochem. (1988) 172:147-153 !$#title Characterization of cDNA clones for human glycophorin A. Use !1for gene localization and for analysis of normal of !1glycophorin-A-deficient (Finnish type) genomic DNA. !$#cross-references MUID:88151980; PMID:3345758 !$#accession S00333 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 23-150 ##label RAH REFERENCE JX0337 !$#authors Kudo, S.; Onda, M.; Fukuda, M. !$#journal J. Biochem. (1994) 116:183-192 !$#title Characterization of glycophorin A transcripts: Control by !1the common erythroid-specific promoter and alternative usage !1of different polyadenylation signals. !$#cross-references MUID:95096015; PMID:7798177 !$#accession JX0337 !'##molecule_type mRNA !'##residues 1-150 ##label KU2 !'##cross-references GB:L31863 !'##experimental_source cell line K562 REFERENCE S11567 !$#authors Hamid, J.; Burness, A.T.H. !$#journal Nucleic Acids Res. (1990) 18:5829-5836 !$#title The mechanism of production of multiple mRNAs for human !1glycophorin A. !$#cross-references MUID:91016923; PMID:2216775 !$#accession S11567 !'##molecule_type mRNA !'##residues 1-150 ##label HAM !'##cross-references EMBL:X51798; NID:g31842; PIDN:CAA36095.1; !1PID:g31843 !'##note the different classes of mRNA described differ in their !1non-coding regions REFERENCE A54468 !$#authors Challou, N.; Goormaghtigh, E.; Cabiaux, V.; Conrath, K.; !1Ruysschaert, J.M. !$#journal Biochemistry (1994) 33:6902-6910 !$#title Sequence and structure of the membrane-associated peptide of !1glycophorin A. !$#cross-references MUID:94264006; PMID:8204624 !$#accession A54468 !'##molecule_type protein !'##residues 20-38 ##label CHA1 !$#accession B54468 !'##molecule_type protein !'##residues 77-82,84-114 ##label CHA2 REFERENCE S09683 !$#authors Dahr, W.; Blanchard, D.; Chevalier, C.; Cartron, J.P.; !1Beyreuther, K.; Fournet, B. !$#journal Biol. Chem. Hoppe-Seyler (1990) 371:403-410 !$#title The Mz variety of the St(a+) phenotype-a variant of !1glycophorin A exhibiting a deletion. !$#cross-references MUID:90334743; PMID:2378678 !$#accession S09683 !'##status preliminary !'##molecule_type protein !'##residues 20-29,'XXX',33-35,'X',37,'X',39-45;78-94,'XX',97-98,'X', !1100-133;138-150 ##label DAH1 REFERENCE S05425 !$#authors Dahr, W.; Vengelen-Tyler, V.; Dybkjaer, E.; Beyreuther, K. !$#journal Biol. Chem. Hoppe-Seyler (1989) 370:855-859 !$#title Structural analysis of glycophorin A from Miltenberger class !1VIII erythrocytes. !$#cross-references MUID:90074183; PMID:2590469 !$#accession S05425 !'##molecule_type protein !'##residues 59-80 ##label DAH2 !'##experimental_source glycophorin Mi-VIII REFERENCE S18490 !$#authors Barton, P.; Collins, A.; Hoogenraad, N. !$#journal Biochim. Biophys. Acta (1991) 1090:265-266 !$#title A variant of glycophorin A resulting from the deletion of !1exon 4. !$#cross-references MUID:92031706; PMID:1932122 !$#accession S18490 !'##status preliminary; translation not shown !'##molecule_type mRNA !'##residues 1-77,91-150 ##label BAR !'##cross-references EMBL:X57023; NID:g31838; PIDN:CAA40340.1; !1PID:g31839 !'##note this sequence has a mutation causing abnormal splicing REFERENCE A45420 !$#authors Huang, C.H.; Reid, M.E.; Blumenfeld, O.O. !$#journal J. Biol. Chem. (1993) 268:4945-4952 !$#title Exon skipping caused by DNA recombination that introduces a !1defective donor splice site into the human glycophorin A !1gene. !$#cross-references MUID:93186803; PMID:8444872 !$#accession I60853 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-45,91-149,'P' ##label HUA1 !'##cross-references GB:L07253; NID:g183324; PIDN:AAC46258.1; !1PID:g183325 !'##experimental_source glycophorin Mz II-V !'##note in GenBank HUMGLYCMZC the translation in PID:g183325 has a !1mistranslation of the residue caused by reading through the !1splice junction !'##note this sequence has a mutation causing abnormal splicing !$#accession I60852 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-45,78-150 ##label HUA2 !'##cross-references GB:L07251; NID:g183322; PIDN:AAC46257.1; !1PID:g183323 !'##experimental_source glycophorin Mz II-IV !'##note this sequence has a mutation causing abnormal splicing COMMENT Glycophorin A is the major intrinsic membrane protein of the !1erythrocyte. COMMENT The MN blood group antigen system reflects allelic variation !1of this erythrocyte-specific protein (see PIR:GFHUE). GENETICS !$#gene GDB:GYPA !'##cross-references GDB:118890; OMIM:111300 !$#map_position 4q28-4q31 CLASSIFICATION #superfamily glycophorin KEYWORDS blood group; erythrocyte; sialoglycoprotein; transmembrane !1protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-150 #product glycophorin A #status experimental #label !8MAT\ !$20-91 #domain extracellular #status predicted #label EXT\ !$92-114 #domain transmembrane #status predicted #label MEM\ !$115-150 #domain intracellular #status predicted #label INT\ !$21,30,32,33,34,41, !$63,66 #binding_site carbohydrate (Ser) (covalent) #status !8experimental\ !$22,23,29,31,44,56, !$69 #binding_site carbohydrate (Thr) (covalent) #status !8experimental\ !$36,47,52 #binding_site carbohydrate (Thr) (covalent) #status !8predicted\ !$38,42 #binding_site carbohydrate (Ser) (covalent) #status !8predicted\ !$45 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 150 #molecular-weight 16273 #checksum 7515 SEQUENCE /// ENTRY B33931 #type complete TITLE glycophorin B precursor - human ALTERNATE_NAMES GPB; sialoglycoprotein delta; Ss-active sialoglycoprotein ORGANISM #formal_name Homo sapiens #common_name man DATE 04-Dec-1992 #sequence_revision 04-Dec-1992 #text_change 16-Jun-2000 ACCESSIONS B33931; A28400; S01305; S00074; A26729; A25717; I68187 REFERENCE A33931 !$#authors Kudo, S.; Fukuda, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:4619-4623 !$#title Structural organization of glycophorin A and B genes: !1glycophorin B gene evolved by homologous recombination at !1Alu repeat sequences. !$#cross-references MUID:89282822; PMID:2734312 !$#accession B33931 !'##molecule_type DNA !'##residues 1-91 ##label KUD !'##cross-references GB:M24130; NID:g183728 !'##note blood group s allele; this translation is not annotated in !1GenBank entry HUMGYPB01, release 113.0 REFERENCE A28400 !$#authors Siebert, P.D.; Fukuda, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:6735-6739 !$#title Molecular cloning of a human glycophorin B cDNA: nucleotide !1sequence and genomic relationship to glycophorin A. !$#cross-references MUID:88016166; PMID:3477806 !$#accession A28400 !'##molecule_type mRNA !'##residues 1-91 ##label SIE !'##cross-references GB:J02982; NID:g183312; PIDN:AAA52573.1; !1PID:g183313 REFERENCE S01304 !$#authors Tate, C.G.; Tanner, M.J.A. !$#journal Biochem. J. (1988) 254:743-750 !$#title Isolation of cDNA clones for human erythrocyte membrane !1sialoglycoproteins alpha and delta. !$#cross-references MUID:89061610; PMID:3196288 !$#accession S01305 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-83,'S',85-91 ##label TAT !'##cross-references EMBL:X08055; NID:g31840; PIDN:CAB42645.1; !1PID:g4803699 REFERENCE S00072 !$#authors Dahr, W.; Beyreuther, K.; Moulds, J.; Unger, P. !$#journal Eur. J. Biochem. (1987) 166:31-36 !$#title Hybrid glycophorins from human erythrocyte membranes. I. !1Isolation and complete structural analysis of the hybrid !1sialoglycoprotein from Dantu-positive red cells of the N.E. !1variety. !$#cross-references MUID:87246688; PMID:3595615 !$#accession S00074 !'##molecule_type protein !'##residues 20-68,'S',70-83,'S',85-90 ##label DAH REFERENCE A92641 !$#authors Blanchard, D.; Dahr, W.; Hummel, M.; Latron, F.; Beyreuther, !1K.; Cartron, J.P. !$#journal J. Biol. Chem. (1987) 262:5808-5811 !$#title Glycophorins B and C from human erythrocyte membranes. !1Purification and sequence analysis. !$#cross-references MUID:87194779; PMID:3571235 !$#accession A26729 !'##molecule_type protein !'##residues 20-47,'M',49-68,'S',70-83,'S',85-90 ##label BLA !'##note blood group S allele REFERENCE A25717 !$#authors Hummel, M.; Dahr, W.; Blanchard, D.; Beyreuther, K.; !1Cartron, J. !$#journal Biol. Chem. Hoppe-Seyler (1985) 366:805 !$#accession A25717 !'##molecule_type protein !'##residues 'M',49-68,'F',70-83,'X',85-88,'X',90,'K' ##label HUM !'##note Thr-48 was also found REFERENCE I54065 !$#authors Vignal, A.; London, J.; Rahuel, C.; Cartron, J. !$#journal Gene (1990) 95:289-293 !$#title Promoter sequence and chromosomal organization of the genes !1encoding glycophorins A, B and E. !$#cross-references MUID:91065544; PMID:2249783 !$#accession I68187 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-12 ##label RES !'##cross-references GB:M57233; NID:g183477; PIDN:AAA63179.1; !1PID:g183478 COMMENT The glycophorins are intrinsic membrane proteins of the !1erythrocyte. COMMENT The Ss blood group antigen system reflects allelic variation !1of this erythrocyte-specific protein. GENETICS !$#gene GDB:GYPB !'##cross-references GDB:118891; OMIM:111740 !$#map_position 4q28-4q31 !$#introns 13/1; 46/1; 59/1; 90/3 CLASSIFICATION #superfamily glycophorin KEYWORDS blood group; erythrocyte; polymorphism; sialoglycoprotein; !1transmembrane protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-91 #product glycophorin B #status predicted #label MAT\ !$20-60 #domain extracellular #status predicted #label EXT\ !$61-81 #domain transmembrane #status predicted #label MEM\ !$82-91 #domain intracellular #status predicted #label INT\ !$21,30,32,33,34,38, !$41,42 #binding_site carbohydrate (Ser) (covalent) #status !8predicted\ !$22,23,29,31,36,44 #binding_site carbohydrate (Thr) (covalent) #status !8predicted SUMMARY #length 91 #molecular-weight 9796 #checksum 6283 SEQUENCE /// ENTRY A34931 #type complete TITLE glycophorin E precursor - human ORGANISM #formal_name Homo sapiens #common_name man DATE 20-Jul-1990 #sequence_revision 20-Jul-1990 #text_change 22-Jun-1999 ACCESSIONS A34931; S11030; S20664 REFERENCE A34931 !$#authors Kudo, S.; Fukuda, M. !$#journal J. Biol. Chem. (1990) 265:1102-1110 !$#title Identification of a novel human glycophorin, glycophorin E, !1by isolation of genomic clones and complementary DNA clones !1utilizing polymerase chain reaction. !$#cross-references MUID:90110092; PMID:2295603 !$#accession A34931 !'##status preliminary !'##molecule_type mRNA !'##residues 1-78 ##label KUD !'##cross-references GB:M29610; NID:g183335; PIDN:AAA52575.1; !1PID:g183336; GB:J05183; GB:M29620 !'##note 13-Gly was also found REFERENCE S11030 !$#authors Vignal, A.; Rahuel, C.; London, J.; Cherif Zahar, B.; !1Schaff, S.; Hattab, C.; Okubo, Y.; Cartron, J.P. !$#journal Eur. J. Biochem. (1990) 191:619-625 !$#title A novel gene member of the human glycophorin A and B gene !1family. Molecular cloning and expression. !$#cross-references MUID:90361045; PMID:2390989 !$#accession S11030 !'##status preliminary !'##molecule_type DNA !'##residues 1-12,'G',14-78 ##label VI2 !'##cross-references EMBL:X53010; NID:g31878; PIDN:CAA37191.1; !1PID:g31879 COMMENT The glycophorins are intrinsic membrane proteins of the !1erythrocyte. GENETICS !$#gene GDB:GYPE !'##cross-references GDB:125418; OMIM:138590 !$#map_position 4q28-4q31 CLASSIFICATION #superfamily glycophorin KEYWORDS erythrocyte; sialoglycoprotein; transmembrane protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-78 #product glycophorin E #status predicted #label MAT\ !$20-61 #domain extracellular #status predicted #label EXT\ !$62-77 #domain transmembrane #status predicted #label MEM\ !$20,21,30,32,33,34, !$38,41,42 #binding_site carbohydrate (Ser) (covalent) #status !8predicted\ !$22,23,29,31,36,44 #binding_site carbohydrate (Thr) (covalent) #status !8predicted SUMMARY #length 78 #molecular-weight 8535 #checksum 8224 SEQUENCE /// ENTRY GFPGE #type complete TITLE glycophorin - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 30-Apr-1981 #sequence_revision 30-Apr-1981 #text_change 31-Dec-1993 ACCESSIONS A91958; A90631; A03184 REFERENCE A91958 !$#authors Honma, K.; Tomita, M.; Hamada, A. !$#journal J. Biochem. (1980) 88:1679-1691 !$#title Amino acid sequence and attachment sites of oligosaccharide !1units of porcine erythrocyte glycophorin. !$#cross-references MUID:81117185; PMID:7462200 !$#accession A91958 !'##molecule_type protein !'##residues 1-43;47-106 ##label HO1 REFERENCE A90631 !$#authors Honma, K.; Tomita, M.; Hamada, A. !$#journal Biochim. Biophys. Acta (1979) 580:210-215 !$#title Partial amino acid sequence of glycophorin from porcine !1erythrocyte membranes. !$#cross-references MUID:80198362; PMID:546438 !$#accession A90631 !'##molecule_type protein !'##residues 36-54;98-133 ##label HO2 CLASSIFICATION #superfamily glycophorin KEYWORDS erythrocyte; sialoglycoprotein; transmembrane protein FEATURE !$1-62 #domain extracellular #status predicted #label EXT\ !$63-85 #domain transmembrane #status predicted #label MEM\ !$86-133 #domain intracellular #status predicted #label INT\ !$1,6,13,21,23,30,41, !$48 #binding_site carbohydrate (Thr) (covalent) #status !8experimental\ !$11,31 #binding_site carbohydrate (Ser) (covalent) #status !8experimental\ !$19,39 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 133 #molecular-weight 14000 #checksum 9033 SEQUENCE /// ENTRY GFHOE #type complete TITLE glycophorin HA - horse ORGANISM #formal_name Equus caballus #common_name domestic horse DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 05-Aug-1994 ACCESSIONS A03185 REFERENCE A03185 !$#authors Murayama, J.I.; Tomita, M.; Hamada, A. !$#journal J. Membr. Biol. (1982) 64:205-215 !$#title Primary structure of horse erythrocyte glycophorin HA. Its !1amino acid sequence has a unique homology with those of !1human and porcine erythrocyte glycophorins. !$#cross-references MUID:82122516; PMID:7057453 !$#accession A03185 !'##molecule_type protein !'##residues 1-120 ##label MUR COMMENT Glycophorin HA is the major intrinsic membrane protein of !1horse erythrocytes. CLASSIFICATION #superfamily glycophorin KEYWORDS erythrocyte; glycoprotein; pyroglutamic acid; transmembrane !1protein FEATURE !$1-49 #domain extracellular #status predicted #label EXT\ !$50-73 #domain transmembrane #status predicted #label TMN\ !$74-120 #domain intracellular #status predicted #label INT\ !$1 #modified_site pyrrolidone carboxylic acid (Gln) !8#status experimental\ !$2,5,13,18,20,24,28 #binding_site carbohydrate (Thr) (covalent) #status !8experimental\ !$7,17,21 #binding_site carbohydrate (Ser) (covalent) #status !8experimental SUMMARY #length 120 #molecular-weight 12440 #checksum 5169 SEQUENCE /// ENTRY GFHUC #type complete TITLE glycophorin C - human ALTERNATE_NAMES component D; glycoconnectin; glycophorin D; PAS-2'; sialoglycoprotein beta CONTAINS glycophorin C short splice form ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 22-Jun-1999 ACCESSIONS A92573; A37269; A29155; A90693; B26729; S06585; S10169; !1I37440; S05529; I59457; S05539; I55302; A03186; S04823 REFERENCE A92573 !$#authors Colin, Y.; Rahuel, C.; London, J.; Romeo, P.H.; d'Auriol, !1L.; Galibert, F.; Cartron, J.P. !$#journal J. Biol. Chem. (1986) 261:229-233 !$#title Isolation of cDNA clones and complete amino acid sequence of !1human erythrocyte glycophorin C. !$#cross-references MUID:86085813; PMID:2416746 !$#accession A92573 !'##molecule_type mRNA !'##residues 1-128 ##label COL !'##cross-references GB:M11802; NID:g189622; PIDN:AAA60023.1; !1PID:g189623 REFERENCE A37269 !$#authors Le Van Kim, C.; Colin, Y.; Blanchard, D.; Dahr, W.; London, !1J.; Cartron, J.P. !$#journal Eur. J. Biochem. (1987) 165:571-579 !$#title Gerbich blood group deficiency of the Ge:-1,-2,-3 and Ge:-1, !1-2,3 types. Immunochemical study and genomic analysis with !1cDNA probes. !$#cross-references MUID:87246642; PMID:3595602 !$#accession A37269 !'##molecule_type mRNA !'##residues 1-128 ##label LEV !'##cross-references GB:M28335 REFERENCE A29155 !$#authors High, S.; Tanner, M.J.A. !$#journal Biochem. J. (1987) 243:277-280 !$#title Human erythrocyte membrane sialoglycoprotein-beta. The cDNA !1sequence suggests the absence of a cleaved N-terminal signal !1sequence. !$#cross-references MUID:87270634; PMID:3606576 !$#accession A29155 !'##molecule_type mRNA !'##residues 1-128 ##label HIG !'##cross-references GB:X12496; NID:g36459; PIDN:CAA31016.1; PID:g36460 REFERENCE A90693 !$#authors Dahr, W.; Hummel, M.; Blanchard, D.; Beyreuther, K.; !1Cartron, J. !$#journal Biol. Chem. Hoppe-Seyler (1985) 366:777-778 !$#title Divergence of chloroplast gene organization in three !1legumes: pea, broad bean and common bean. !$#accession A90693 !'##molecule_type protein !'##residues 1-87 ##label DAH REFERENCE A92641 !$#authors Blanchard, D.; Dahr, W.; Hummel, M.; Latron, F.; Beyreuther, !1K.; Cartron, J.P. !$#journal J. Biol. Chem. (1987) 262:5808-5811 !$#title Glycophorins B and C from human erythrocyte membranes. !1Purification and sequence analysis. !$#cross-references MUID:87194779; PMID:3571235 !$#accession B26729 !'##molecule_type protein !'##residues 1-128 ##label BLA REFERENCE S06585 !$#authors Cartron, J.P.; Colin, Y.; Le Van Kim, C.; Rahuel, C.; !1Blanchard, D.; Bloy, C.; London, J. !$#journal Rev. Fr. Transfus. Immunohematol. (1986) 29:267-285 !$#title Structure of human erythrocyte glycophorin C deduced from !1cDNA analysis. !$#cross-references MUID:87119743; PMID:3544149 !$#accession S06585 !'##status preliminary !'##molecule_type mRNA !'##residues 3-128 ##label CAR REFERENCE S10169 !$#authors Le Van Kim, C.; Mitjavila, M.T.; Clerget, M.; Cartron, J.P.; !1Colin, Y. !$#journal Nucleic Acids Res. (1990) 18:3076 !$#title An ubiquitous isoform of glycophorin C is produced by !1alternative splicing. !$#cross-references MUID:90272439; PMID:2349119 !$#accession S10169 !'##molecule_type mRNA !'##residues 1-22,42-128 ##label LE2 !'##cross-references EMBL:X51973; NID:g31672; PIDN:CAA36235.1; !1PID:g31673 REFERENCE I37440 !$#authors Le Van Kim, C.; Colin, Y.; Mitjavila, M.T.; Clerget, M.; !1Dubart, A.; Nakazawa, M.; Vainchenker, W.; Cartron, J.P. !$#journal J. Biol. Chem. (1989) 264:20407-20414 !$#title Structure of the promoter region and tissue specificity of !1the human glycophorin C gene. !$#cross-references MUID:90062172; PMID:2584223 !$#accession I37440 !'##molecule_type DNA !'##residues 1-16 ##label RES !'##cross-references EMBL:X14242; NID:g31962; PIDN:CAA32458.1; !1PID:g31963 REFERENCE S05529 !$#authors El-Maliki, B.; Blanchard, D.; Dahr, W.; Beyreuther, K.; !1Cartron, J.P. !$#journal Eur. J. Biochem. (1989) 183:639-643 !$#title Structural homology between glycophorins C and D of human !1erythrocytes. !$#cross-references MUID:89377831; PMID:2776757 !$#accession S05529 !'##molecule_type protein !'##residues 30,'XXX',34-41,'X',43-74,'X',76,'X',78-79;81,'A',83;85-98, !1'XX',101-102,'XX',105-106;107,'X',110-123,'X',125-126 !1##label ELM REFERENCE I59457 !$#authors Cartron, J. !$#journal Rev. Fr. Transfus. Immunohematol. (1986) 24:267-285 !$#title Structure of human erythrocyte glycophorin C deduced from !1cDNA analysis. !$#accession I59457 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-128 ##label RE2 !'##cross-references GB:M36284; NID:g183736; PIDN:AAA52625.1; !1PID:g306825 REFERENCE S05539 !$#authors High, S.; Tanner, M.J.A.; Macdonald, E.B.; Anstee, D.J. !$#journal Biochem. J. (1989) 262:47-54 !$#title Rearrangements of the red-cell membrane glycophorin C !1(sialoglycoprotein beta) gene. A further study of !1alterations in the glycophorin C gene. !$#cross-references MUID:90056445; PMID:2818576 !$#accession S05539 !'##molecule_type DNA !'##residues 18-128 ##label HIW !'##cross-references EMBL:X13890 REFERENCE I55302 !$#authors Colin, Y.; Le Van Kim, C.; Tsapis, A.; Clerget, M.; !1d'Auriol, L.; London, J.; Galibert, F.; Cartron, J.P. !$#journal J. Biol. Chem. (1989) 264:3773-3780 !$#title Human erythrocyte glycophorin C. Gene structure and !1rearrangement in genetic variants. !$#cross-references MUID:89139429; PMID:2917976 !$#accession I55302 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-16 ##label RE3 !'##cross-references GB:M29662; NID:g183741; PIDN:AAA52626.1; !1PID:g553327 COMMENT A minor sialoglycoprotein in human erythrocyte membranes, !1this protein binds an average of 12 sialotetrasaccharides !1(O-glycosidically) and one asparagine-linked carbohydrate !1chain. The blood group Gerbich antigens and receptors for !1Plasmodium falciparum merozoites are most likely located !1within the extracellular domain. GENETICS !$#gene GDB:GYPC !'##cross-references GDB:120027; OMIM:110750 !$#map_position 2q14-2q21 !$#introns 17/1; 36/1; 64/1 CLASSIFICATION #superfamily glycophorin KEYWORDS alternative splicing; blood group; erythrocyte; !1sialoglycoprotein; transmembrane protein FEATURE !$1-128 #product glycophorin C #status predicted #label MAT\ !$1-57 #domain extracellular #status predicted #label EXT\ !$1-22,42-128 #product glycophorin C short splice form #status !8predicted #label MA2\ !$58-81 #domain transmembrane #status predicted #label TMM\ !$82-128 #domain intracellular #status predicted #label INT\ !$3,6,15,24,26,42 #binding_site carbohydrate (Ser) (covalent) #status !8experimental\ !$4,27,28,31,32,33 #binding_site carbohydrate (Thr) (covalent) #status !8experimental\ !$8 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 128 #molecular-weight 13810 #checksum 8817 SEQUENCE /// ENTRY B3HU #type complete TITLE band 3 anion transport protein, erythrocyte - human ALTERNATE_NAMES carrier family 4, anion exchanger, member 1; erythroid anion exchange protein ORGANISM #formal_name Homo sapiens #common_name man DATE 03-Aug-1984 #sequence_revision 03-Oct-1995 #text_change 22-Jun-1999 ACCESSIONS A36218; S03074; I39408; I39409; A92237; A26507; A92430; !1A90323; A28079; S05523; A35835; A44933; A44116; A49717; !1PC4403; A03189 REFERENCE A36218 !$#authors Lux, S.E.; John, K.M.; Kopito, R.R.; Lodish, H.F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:9089-9093 !$#title Cloning and characterization of band 3, the human !1erythrocyte anion-exchange protein (AE1). !$#cross-references MUID:90083213; PMID:2594752 !$#accession A36218 !'##status preliminary !'##molecule_type mRNA !'##residues 1-911 ##label LUX !'##cross-references GB:M27819; NID:g178215; PIDN:AAA35514.1; !1PID:g178216 REFERENCE S03074 !$#authors Tanner, M.J.A.; Martin, P.G.; High, S. !$#journal Biochem. J. (1988) 256:703-712 !$#title The complete amino acid sequence of the human erythrocyte !1membrane anion-transport protein deduced from the cDNA !1sequence. !$#cross-references MUID:89134172; PMID:3223947 !$#accession S03074 !'##molecule_type mRNA !'##residues 1-55,'E',57-911 ##label TAN !'##cross-references EMBL:X12609; NID:g28713; PIDN:CAA31128.1; !1PID:g28714 REFERENCE I39408 !$#authors Showe, L.C.; Ballantine, M.; Huebner, K. !$#journal Genomics (1987) 1:71-76 !$#title Localization of the gene for the erythroid anion exchange !1protein, band 3 (EMPB3), to human chromosome 17. !$#cross-references MUID:88031311; PMID:3478298 !$#accession I39408 !'##molecule_type DNA !'##residues 37-56 ##label SHO1 !'##cross-references GB:M16978; NID:g178217; PIDN:AAA51670.1; !1PID:g178220 !$#accession I39409 !'##molecule_type DNA !'##residues 118-161 ##label SHO2 !'##cross-references GB:M16979; NID:g178218; PIDN:AAA51671.1; !1PID:g553169 REFERENCE A92237 !$#authors Drickamer, L.K. !$#journal J. Biol. Chem. (1978) 253:7242-7248 !$#title Orientation of the band 3 polypeptide from human erythrocyte !1membranes. Identification of NH-2-terminal sequence and site !1of carbohydrate attachment. !$#cross-references MUID:79027186; PMID:701248 !$#accession A92237 !'##molecule_type protein !'##residues 1-3 ##label DRI REFERENCE A26507 !$#authors Mawby, W.J.; Findlay, J.B.C. !$#journal Biochem. J. (1982) 205:465-475 !$#title Characterization and partial sequence of di-iodosulphophenyl !1isothiocyanate-binding peptide from human erythrocyte !1anion-transport protein. !$#cross-references MUID:83074521; PMID:7150226 !$#accession A26507 !'##molecule_type protein !'##residues 437-473;360-364,'D',366-369 ##label MAW REFERENCE A92430 !$#authors Kaul, R.K.; Murthy, S.N.P.; Reddy, A.G.; Steck, T.L.; !1Kohler, H. !$#journal J. Biol. Chem. (1983) 258:7981-7990 !$#title Amino acid sequence of the N(alpha)-terminal 201 residues of !1human erythrocyte membrane band 3. !$#cross-references MUID:83238395; PMID:6345535 !$#accession A92430 !'##molecule_type protein !'##residues 1-10,'D',12-68,'E',69-200 ##label KAU REFERENCE A90323 !$#authors Brock, C.J.; Tanner, M.J.A.; Kempf, C. !$#journal Biochem. J. (1983) 213:577-586 !$#title The human erythrocyte anion-transport protein. !$#cross-references MUID:83308584; PMID:6615451 !$#accession A90323 !'##molecule_type protein !'##residues 559-630 ##label BRO !'##note Lys-590 was shown to bind phenyl isothiocyanate, an inhibitor !1of anion transport REFERENCE A28079 !$#authors Kawano, Y.; Okubo, K.; Tokunaga, F.; Miyata, T.; Iwanaga, !1S.; Hamasaki, N. !$#journal J. Biol. Chem. (1988) 263:8232-8238 !$#title Localization of the pyridoxal phosphate binding site at the !1COOH-terminal region of erythrocyte band 3 protein. !$#cross-references MUID:88228050; PMID:3372523 !$#accession A28079 !'##molecule_type protein !'##residues 834-842,'X',844-911 ##label KAW !'##note Lys-851 was shown to bind the affinity label pyridoxal !1phosphate, a substrate for anion transport REFERENCE S05523 !$#authors Yannoukakos, D.; Vasseur, C.; Blouquit, Y.; Bursaux, E.; !1Wajcman, H. !$#journal Biochim. Biophys. Acta (1989) 998:43-49 !$#title Primary structure of the cytoplasmic domain of human !1erythrocyte protein band 3. Comparison with its sequence in !1the mouse. !$#cross-references MUID:90001294; PMID:2790053 !$#accession S05523 !'##molecule_type protein !'##residues 1-201;220-292;307-308,'R',310-312,'S',314-329,'K', !1331-333;347-370 ##label YAN1 REFERENCE A35835 !$#authors Cobb, C.E.; Beth, A.H. !$#journal Biochemistry (1990) 29:8283-8290 !$#title Identification of the eosinyl-5-maleimide reaction site on !1the human erythrocyte anion-exchange protein: overlap with !1the reaction sites of other chemical probes. !$#cross-references MUID:91070049; PMID:1701324 !$#accession A35835 !'##status preliminary !'##molecule_type protein !'##residues 361-364,'X',366-372;424-429,'X',431-434 ##label COB !'##note Lys-430 is labeled by eosinyl-5-maleimide (EMA) in intact !1erythrocytes REFERENCE A44933 !$#authors Yannoukakos, D.; Vasseur, C.; Driancourt, C.; Blouquit, Y.; !1Delaunay, J.; Wajcman, H.; Bursaux, E. !$#journal Blood (1991) 78:1117-1120 !$#title Human erythrocyte band 3 polymorphism (band 3 Memphis): !1characterization of the structural modification (Lys !156->Glu) by protein chemistry methods. !$#cross-references MUID:91329825; PMID:1678289 !$#accession A44933 !'##molecule_type protein !'##residues 1-55,'E',57-69 ##label YAN2 !'##note sequence extracted from NCBI backbone (NCBIP:49829) !'##note sequence of a common polymorphic form designated band 3 Memphis REFERENCE A44116 !$#authors Kang, D.; Okubo, K.; Hamasaki, N.; Kuroda, N.; Shiraki, H. !$#journal J. Biol. Chem. (1992) 267:19211-19217 !$#title A structural study of the membrane domain of band 3 by !1tryptic digestion. Conformational change of band 3 in situ !1induced by alkali treatment. !$#cross-references MUID:92406862; PMID:1527044 !$#accession A44116 !'##status preliminary !'##molecule_type protein !'##residues !1361-372;390-399;604-613;632-639;647-656;699-729;731-743; !1761-781;818-826 ##label KAN !'##experimental_source erythrocyte !'##note sequence extracted from NCBI backbone (NCBIP:113819, !1NCBIP:113821, NCBIP:113823, NCBIP:113825, NCBIP:113827, !1NCBIP:113829, NCBIP:113831, NCBIP:113833, NCBIP:113835) !'##note a histidine residue essential for anion transport is suggested !1to be His-651, His-734, or His-819 REFERENCE A49717 !$#authors Okubo, K.; Kang, D.; Hamasaki, N.; Jennings, M.L. !$#journal J. Biol. Chem. (1994) 269:1918-1926 !$#title Red blood cell band 3. Lysine 539 and lysine 851 react with !1the same H-2DIDS (4,4'-diisothiocyanodihydrostilbene-2, !12'-disulfonic acid) molecule. !$#cross-references MUID:94124538; PMID:8294441 !$#accession A49717 !'##molecule_type protein !'##residues 427-436;479-519;538-540;559-566;809-817;825-841;849-857 !1##label OKU !'##note Lys-539 and Lys-851 were shown to bind the same molecule of the !1anion transport inhibitor 4,4'-diisothiocyanostilbene-2, !12'-disulfonic acid (H-2DIDS) REFERENCE PC4403 !$#authors Hamasaki, N.; Okubo, K.; Kuma, H.; Kang, D.; Yae, Y. !$#journal J. Biochem. (1997) 122:577-585 !$#title Proteolytic cleavage sites of band 3 protein in !1alkali-treated membranes: Fidelity of hydropathy prediction !1for band 3 protein. !$#cross-references MUID:98006310; PMID:9348087 !$#accession PC4403 !'##molecule_type protein !'##residues 361-911 ##label HAM COMMENT Band 3 is the major integral glycoprotein of the erythrocyte !1membrane. A dimer in solution, it spans the membrane !1asymmetrically and appears to be tetrameric. COMMENT Band 3 has at least two functional domains. Its integral !1domain mediates a 1:1 exchange of chloride and bicarbonate !1anions across the membrane, whereas its cytoplasmic domain !1provides binding sites for cytoskeletal proteins, glycolytic !1enzymes, and hemoglobin. GENETICS !$#gene GDB:SLC4A1; EPB3 !'##cross-references GDB:119874; OMIM:109270 !$#map_position 17q21-17q22 CLASSIFICATION #superfamily band 3 anion transport protein KEYWORDS acetylated amino end; glycoprotein; ion transport; !1phosphoprotein; transmembrane protein FEATURE !$1-403 #region cytoskeletal protein binding\ !$404-911 #region anion antiporter\ !$405-427 #domain transmembrane #status predicted #label TM01\ !$435-457 #domain transmembrane #status predicted #label TM02\ !$459-479 #domain transmembrane #status predicted #label TM03\ !$491-507 #domain transmembrane #status predicted #label TM04\ !$522-542 #domain transmembrane #status predicted #label TM05\ !$568-588 #domain transmembrane #status predicted #label TM06\ !$604-624 #domain transmembrane #status predicted #label TM07\ !$659-680 #domain transmembrane #status predicted #label TM08\ !$701-721 #domain transmembrane #status predicted #label TM09\ !$723-743 #domain transmembrane #status predicted #label TM10\ !$764-780 #domain transmembrane #status predicted #label TM11\ !$785-806 #domain transmembrane #status predicted #label TM12\ !$839-859 #domain transmembrane #status predicted #label TM13\ !$861-881 #domain transmembrane #status predicted #label TM14\ !$1 #modified_site acetylated amino end (Met) #status !8experimental\ !$539,590,851 #binding_site anion (Lys) #status experimental\ !$642 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 911 #molecular-weight 101791 #checksum 1140 SEQUENCE /// ENTRY ETHUL #type complete TITLE lymphotactin precursor - human ALTERNATE_NAMES activation-induced chemokine-related protein (ATAC); single cysteine motif-1 chemokine (SCM-1); small inducible cytokine subfamily C, member 1 CONTAINS eosinophilotactic peptide ORGANISM #formal_name Homo sapiens #common_name man DATE 23-Oct-1981 #sequence_revision 07-Jun-1996 #text_change 22-Jun-1999 ACCESSIONS S60650; I38978; A03190; I53506 REFERENCE S60650 !$#authors Mueller, S.; Dorner, B.; Korthaeuer, U.; Mages, H.W.; !1D'Apuzzo, M.; Senger, G.; Kroczek, R.A. !$#journal Eur. J. Immunol. (1995) 25:1744-1748 !$#title Cloning of ATAC, an activation-induced, chemokine-related !1molecule exclusively expressed in CD8(+) T lymphocytes. !$#cross-references MUID:95339892; PMID:7615002 !$#accession S60650 !'##molecule_type mRNA !'##residues 1-114 ##label MUE !'##cross-references EMBL:X86474; NID:g895846; PIDN:CAA60198.1; !1PID:g895847 REFERENCE I38978 !$#authors Kennedy, J.; Kelner, G.S.; Kleyensteuber, S.; Schall, T.J.; !1Weiss, M.C.; Yssel, H.; Schneider, P.V.; Cocks, B.G.; Bacon, !1K.B.; Zlotnik, A. !$#journal J. Immunol. (1995) 155:203-209 !$#title Molecular cloning and functional characterization of human !1lymphotactin. !$#cross-references MUID:95325590; PMID:7602097 !$#accession I38978 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-114 ##label KEN !'##cross-references EMBL:U23772; NID:g902001; PIDN:AAC50164.1; !1PID:g902002 REFERENCE A03190 !$#authors Goetzl, E.J.; Austen, K.F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1975) 72:4123-4127 !$#title Purification and synthesis of eosinophilotactic !1tetrapeptides of human lung tissue: identification as !1eosinophil chemotactic factor of anaphylaxis. !$#cross-references MUID:76078412; PMID:1060093 !$#accession A03190 !'##molecule_type protein !'##residues 22-25 ##label GOE !'##note 22-Ala was also seen REFERENCE I53506 !$#authors Yoshida, T.; Imai, T.; Kakizaki, M.; Nishimura, M.; Yoshie, !1O. !$#journal FEBS Lett. (1995) 360:155-159 !$#title Molecular cloning of a novel C or gamma type chemokine, !1SCM-1. !$#cross-references MUID:95180438; PMID:7875320 !$#accession I53506 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-114 ##label YOS !'##cross-references GB:D43768; NID:g927650; PIDN:BAA07825.1; !1PID:g927651 COMMENT Lymphotactin is produced by activated T-cells and is !1chemotactic for some lymphocytes. COMMENT Eosinophilotactic peptide is released from mast cells in !1lung and other tissues during anaphylaxis (hypersensitivity !1reactions). The activities of the eosinophilotactic !1peptides, preferentially affecting eosinophils, include !1chemotaxis, chemotactic deactivation, release of enzymes, !1and stimulation of the hexose monophosphate shunt. COMMENT It has not yet been shown that the previously detected !1eosinophilotactic peptide actually arises from lymphotactin. GENETICS !$#gene GDB:SCYC1; LTN; LPTN; ATAC !'##cross-references GDB:682094 !$#map_position 1q23-1q25 CLASSIFICATION #superfamily lymphotactin KEYWORDS chemotaxis; cytokine; lymphokine; mast cell; T-cell FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-21 #domain propeptide #status predicted #label PRO\ !$22-114 #product lymphotactin #status predicted #label MAT\ !$22-25 #product eosinophilotactic peptide #status predicted !8#label EOP\ !$32-69 #disulfide_bonds #status predicted SUMMARY #length 114 #molecular-weight 12516 #checksum 365 SEQUENCE /// ENTRY ETMSL #type complete TITLE lymphotactin precursor - mouse ALTERNATE_NAMES single cysteine motif-1, SCM-1 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 23-Mar-1995 #sequence_revision 07-Jun-1996 #text_change 22-Jun-1999 ACCESSIONS A55248; I67635 REFERENCE A55248 !$#authors Kelner, G.S.; Kennedy, J.; Bacon, K.B.; Kleyensteuber, S.; !1Largaespada, D.A.; Jenkins, N.A.; Copeland, N.G.; Bazan, !1J.F.; Moore, K.W.; Schall, T.J.; Zlotnik, A. !$#journal Science (1994) 266:1395-1399 !$#title Lymphotactin: a cytokine that represents a new class of !1chemokine. !$#cross-references MUID:95064019; PMID:7973732 !$#accession A55248 !'##molecule_type mRNA !'##residues 1-114 ##label KEL !'##cross-references GB:U15607; NID:g595908; PIDN:AAA56752.1; !1PID:g595909 !'##note authors translated the codon AAA for residue 98 as Leu, GTA for !1residue 110 as Ile, and also inserted an additional Gly !1after residue 99 REFERENCE I53506 !$#authors Yoshida, T.; Imai, T.; Kakizaki, M.; Nishimura, M.; Yoshie, !1O. !$#journal FEBS Lett. (1995) 360:155-159 !$#title Molecular cloning of a novel C or gamma type chemokine, !1SCM-1. !$#cross-references MUID:95180438; PMID:7875320 !$#accession I67635 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-109,'I',111-114 ##label RES !'##cross-references GB:D43769; NID:g927656; PIDN:BAA07826.1; !1PID:g927657 COMMENT Lymphotactin is produced by activated T-cells and is a !1chemotactin for monocytes and neutrophils. CLASSIFICATION #superfamily lymphotactin KEYWORDS chemotaxis; cytokine; lymphokine; mast cell; T-cell FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-21 #domain propeptide #status predicted #label PRO\ !$22-114 #product lymphotactin #status predicted #label MAT SUMMARY #length 114 #molecular-weight 12453 #checksum 5703 SEQUENCE /// ENTRY FDFI5G #type complete TITLE antifreeze protein GS-5 - grubby sculpin ORGANISM #formal_name Myoxocephalus aenaeus #common_name grubby sculpin DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 24-Nov-1999 ACCESSIONS S06417 REFERENCE S06417 !$#authors Chakrabartty, A.; Hew, C.L.; Shears, M.; Fletcher, G. !$#journal Can. J. Zool. (1988) 66:403-408 !$#title Primary structures of the alanine-rich antifreeze !1polypeptides from grubby sculpin, Myoxocephalus aenaeus. !$#accession S06417 !'##molecule_type protein !'##residues 1-33 ##label CHA CLASSIFICATION #superfamily antifreeze protein KEYWORDS antifreeze; blocked amino end FEATURE !$1 #modified_site blocked amino end (Met) #status !8experimental SUMMARY #length 33 #molecular-weight 2980 #checksum 8836 SEQUENCE /// ENTRY FDFL4W #type complete TITLE antifreeze protein 4 precursor - winter flounder ORGANISM #formal_name Pseudopleuronectes americanus #common_name winter flounder DATE 01-Sep-1981 #sequence_revision 01-Sep-1981 #text_change 25-Apr-1997 ACCESSIONS A03193 REFERENCE A03193 !$#authors Lin, Y.; Gross, J.K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:2825-2829 !$#title Molecular cloning and characterization of winter flounder !1antifreeze cDNA. !$#cross-references MUID:81247379; PMID:6265915 !$#accession A03193 !'##molecule_type mRNA !'##residues 1-85 ##label LIN CLASSIFICATION #superfamily antifreeze protein KEYWORDS antifreeze FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-85 #product antifreeze protein 4 #status predicted !8#label MAT SUMMARY #length 85 #molecular-weight 7243 #checksum 2205 SEQUENCE /// ENTRY FDFLAW #type complete TITLE antifreeze protein A precursor - winter flounder ORGANISM #formal_name Pseudopleuronectes americanus #common_name winter flounder DATE 13-Aug-1986 #sequence_revision 13-Aug-1986 #text_change 22-Jun-1999 ACCESSIONS JS0704; A03194 REFERENCE JH0627 !$#authors Davies, P.L. !$#journal Gene (1992) 112:163-170 !$#title Conservation of antifreeze protein-encoding genes in tandem !1repeats. !$#cross-references MUID:92209995; PMID:1555765 !$#accession JS0704 !'##molecule_type DNA !'##residues 1-82 ##label DA1 !'##cross-references GB:M62412; GB:M62416; NID:g213592; PIDN:AAA49471.1; !1PID:g213593 REFERENCE A03194 !$#authors Davies, P.L.; Roach, A.H.; Hew, C.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:335-339 !$#title DNA sequence coding for an antifreeze protein precursor from !1winter flounder. !$#cross-references MUID:82197490; PMID:6952188 !$#accession A03194 !'##molecule_type mRNA !'##residues 1-82 ##label DA2 !'##experimental_source clones 4-2b and 2A-7c !'##note the authors translated the codon AGC for residue 24 as Arg GENETICS !$#introns 19/2 CLASSIFICATION #superfamily antifreeze protein KEYWORDS antifreeze; plasma; tandem repeat FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-44 #domain propeptide #status predicted #label PRO\ !$45-82 #product antifreeze protein A #status predicted !8#label MAT SUMMARY #length 82 #molecular-weight 7711 #checksum 310 SEQUENCE /// ENTRY FDFL3W #type complete TITLE antifreeze protein 3 - winter flounder ORGANISM #formal_name Pseudopleuronectes americanus #common_name winter flounder DATE 01-Sep-1981 #sequence_revision 01-Sep-1981 #text_change 23-Aug-1996 ACCESSIONS A03192 REFERENCE A03192 !$#authors DeVries, A.L.; Lin, Y. !$#journal Biochim. Biophys. Acta (1977) 495:388-392 !$#title Structure of a peptide antifreeze and mechanism of !1adsorption to ice. !$#cross-references MUID:78060969; PMID:588591 !$#accession A03192 !'##molecule_type protein !'##residues 1-37 ##label DEV CLASSIFICATION #superfamily antifreeze protein KEYWORDS antifreeze SUMMARY #length 37 #molecular-weight 3144 #checksum 7865 SEQUENCE /// ENTRY FDFI8G #type complete TITLE antifreeze protein GS-8 - grubby sculpin ORGANISM #formal_name Myoxocephalus aenaeus #common_name grubby sculpin DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 24-Nov-1999 ACCESSIONS S07046 REFERENCE S06417 !$#authors Chakrabartty, A.; Hew, C.L.; Shears, M.; Fletcher, G. !$#journal Can. J. Zool. (1988) 66:403-408 !$#title Primary structures of the alanine-rich antifreeze !1polypeptides from grubby sculpin, Myoxocephalus aenaeus. !$#accession S07046 !'##molecule_type protein !'##residues 1-40 ##label CHA CLASSIFICATION #superfamily antifreeze protein KEYWORDS antifreeze; blocked amino end FEATURE !$1 #modified_site blocked amino end (Met) #status !8experimental SUMMARY #length 40 #molecular-weight 3579 #checksum 5679 SEQUENCE /// ENTRY FDFICP #type complete TITLE antifreeze protein SP1-C precursor - ocean pout ORGANISM #formal_name Macrozoarces americanus #common_name ocean pout DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 22-Jun-1999 ACCESSIONS A24081; F31075 REFERENCE A24081 !$#authors Li, X.M.; Trinh, K.Y.; Hew, C.L.; Buettner, B.; Baenziger, !1J.; Davies, P.L. !$#journal J. Biol. Chem. (1985) 260:12904-12909 !$#title Structure of an antifreeze polypeptide and its precursor !1from the ocean pout, Macrozoarces americanus. !$#cross-references MUID:86033715; PMID:3840475 !$#accession A24081 !'##molecule_type mRNA !'##residues 1-87 ##label LIX !'##cross-references GB:M11790; NID:g213362; PIDN:AAA49347.1; !1PID:g213363 REFERENCE A31075 !$#authors Hew, C.L.; Wang, N.C.; Joshi, S.; Fletcher, G.L.; Scott, !1G.K.; Hayes, P.H.; Buettner, B.; Davies, P.L. !$#journal J. Biol. Chem. (1988) 263:12049-12055 !$#title Multiple genes provide the basis for antifreeze protein !1diversity and dosage in the ocean pout, Macrozoarces !1americanus. !$#cross-references MUID:88298890; PMID:3403560 !$#accession F31075 !'##molecule_type protein !'##residues 23-86 ##label HEW COMMENT Ocean pout AFP has at least 12 components, which separate !1into SP1, SP2, SP3, and SP4 in ion-exchange chromatography. !1SP1 has 3 components; SP1-A, SP1-B and SP1-C. SP1-A differs !1from that shown at least in having 75-Ile and 84-Ala. SP1-B !1may be a posttranslational modification of SP1-C. CLASSIFICATION #superfamily antifreeze protein SP1 KEYWORDS antifreeze; plasma; pyroglutamic acid FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-87 #product antifreeze protein SP1-C #status !8experimental #label AFC\ !$23 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental SUMMARY #length 87 #molecular-weight 9229 #checksum 1879 SEQUENCE /// ENTRY FDFIRE #type complete TITLE antifreeze protein RD2 - eelpout (Lycodichthys dearborni) ORGANISM #formal_name Lycodichthys dearborni DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 26-Feb-1999 ACCESSIONS S08561; S53513 REFERENCE S07150 !$#authors Schrag, J.D.; Cheng, C.H.C.; Panico, M.; Morris, H.R.; !1DeVries, A.L. !$#journal Biochim. Biophys. Acta (1987) 915:357-370 !$#title Primary and secondary structure of antifreeze peptides from !1arctic and antarctic zoarcid fishes. !$#cross-references MUID:88000728; PMID:3477289 !$#accession S08561 !'##molecule_type protein !'##residues 1-64 ##label SCH !'##note the source is designated as Rhigophila dearborni REFERENCE S53512 !$#authors Wang, X.; DeVries, A.L.; Cheng, C.H.C. !$#journal Biochim. Biophys. Acta (1995) 1247:163-172 !$#title Antifreeze peptide heterogeneity in an antarctic eel pout !1includes an unusually large major variant comprised of two 7 !1kDa type III AFPs linked in tandem. !$#cross-references MUID:95210308; PMID:7696304 !$#accession S53513 !'##status preliminary !'##molecule_type protein !'##residues 1-64 ##label WAN CLASSIFICATION #superfamily antifreeze protein SP1 KEYWORDS antifreeze SUMMARY #length 64 #molecular-weight 6934 #checksum 9342 SEQUENCE /// ENTRY FDFILC #type complete TITLE antifreeze protein LP - Canadian eelpout ORGANISM #formal_name Lycodes polaris #common_name Canadian eelpout DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 30-Jun-1993 ACCESSIONS S07150 REFERENCE S07150 !$#authors Schrag, J.D.; Cheng, C.H.C.; Panico, M.; Morris, H.R.; !1DeVries, A.L. !$#journal Biochim. Biophys. Acta (1987) 915:357-370 !$#title Primary and secondary structure of antifreeze peptides from !1arctic and antarctic zoarcid fishes. !$#cross-references MUID:88000728; PMID:3477289 !$#accession S07150 !'##molecule_type protein !'##residues 1-66 ##label SCH CLASSIFICATION #superfamily antifreeze protein SP1 KEYWORDS antifreeze SUMMARY #length 66 #molecular-weight 6982 #checksum 966 SEQUENCE /// ENTRY YLHUS #type complete TITLE serum amyloid A1 protein precursor [validated] - human ALTERNATE_NAMES amyloid-related serum protein SAA CONTAINS amyloid protein AA ORGANISM #formal_name Homo sapiens #common_name man DATE 15-Oct-1982 #sequence_revision 08-Feb-1996 #text_change 08-Dec-2000 ACCESSIONS A22342; S09972; S09974; S09977; S09978; S12491; S12492; !1S20103; A60863; A90461; A91711; A29419; A60431; S21261; !1S21260; S33864; A56867; A94234; A91215; A90195; B30323; !1I39454; A03195; A03196 REFERENCE A22342 !$#authors Sipe, J.D.; Colten, H.R.; Goldberger, G.; Edge, M.D.; Tack, !1B.F.; Cohen, A.S.; Whitehead, A.S. !$#journal Biochemistry (1985) 24:2931-2936 !$#title Human serum amyloid A (SAA): biosynthesis and postsynthetic !1processing of preSAA and structural variants defined by !1complementary DNA. !$#cross-references MUID:85252712; PMID:3839415 !$#contents allele SAA1*1 (SAA1-alpha) !$#accession A22342 !'##molecule_type mRNA !'##residues 1-118,'S',120-122 ##label SIP !'##cross-references GB:M10906; NID:g337747; PIDN:AAA60297.1; !1PID:g337748 REFERENCE S09972 !$#authors Steinkasserer, A.; Weiss, E.H.; Schwaeble, W.; Linke, R.P. !$#journal Biochem. J. (1990) 268:187-193 !$#title Heterogeneity of human serum amyloid A protein: five !1different variants from one individual demonstrated by cDNA !1sequence analysis. !$#cross-references MUID:90262544; PMID:1971508 !$#accession S09972 !'##molecule_type mRNA !'##residues 8-72 ##label STE !'##cross-references EMBL:X51443 !'##experimental_source clone pAS4 !'##note allele SAA1*1 (SAA1-alpha) !$#accession S09974 !'##molecule_type mRNA !'##residues 73-122 ##label ST2 !'##cross-references EMBL:X51439; NID:g36311; PIDN:CAA35804.1; !1PID:g825714 !'##experimental_source clone pAS1 !'##note allele SAA1*1 (SAA1-alpha) !$#accession S09977 !'##molecule_type mRNA !'##residues 73-74,'V',76-77,'N',79-122 ##label ST3 !'##cross-references EMBL:X51442; NID:g36314; PIDN:CAA35807.1; !1PID:g825717 !'##experimental_source clone pAS3-beta !'##note a variant of allele SAA1-beta !$#accession S09978 !'##molecule_type mRNA !'##residues 73-77,'N',79-122 ##label ST4 !'##cross-references EMBL:X51441 !'##experimental_source clone pAS3-alpha REFERENCE S12491 !$#authors Linke, R.P. !$#submission submitted to the EMBL Data Library, January 1990 !$#accession S12491 !'##molecule_type mRNA !'##residues 8-69,'LG' ##label LIN !'##cross-references EMBL:X51443; NID:g36315; PIDN:CAA35808.1; !1PID:g939926 !'##experimental_source clone pAS4 !'##note allele SAA1*1 (SAA1-alpha) !$#accession S12492 !'##molecule_type mRNA !'##residues 73-74,'V',76-77,'N',79-122 ##label LI2 !'##cross-references EMBL:X51441; NID:g36313; PIDN:CAA35806.1; !1PID:g825716 !'##experimental_source clone pAS3-alpha REFERENCE S20103 !$#authors Betts, J.C.; Edbrooke, M.R.; Thakker, R.V.; Woo, P. !$#journal Scand. J. Immunol. (1991) 34:471-482 !$#title The human acute-phase serum amyloid A gene family: !1structure, evolution and expression in hepatoma cells. !$#cross-references MUID:92022342; PMID:1656519 !$#contents allele SAA1*2b (SAA1-beta) !$#accession S20103 !'##status translation not shown !'##molecule_type DNA !'##residues 1-69,'A',71-74,'V',76-122 ##label BET !'##cross-references EMBL:X56652; NID:g36307; PIDN:CAA39974.1; !1PID:g36308 REFERENCE A60863 !$#authors Skinner, M.; Pinnette, A.; Travis, W.D.; Shwachman, H.; !1Cohen, A.S. !$#journal J. Lab. Clin. Med. (1988) 112:413-417 !$#title Isolation and sequence analysis of amyloid protein AA from a !1patient with cystic fibrosis. !$#cross-references MUID:89010280; PMID:3171350 !$#contents allele SAA1*1 (SAA1-alpha) !$#accession A60863 !'##molecule_type protein !'##residues 19-94 ##label SKI REFERENCE A90461 !$#authors Parmelee, D.C.; Titani, K.; Ericsson, L.H.; Eriksen, N.; !1Benditt, E.P.; Walsh, K.A. !$#journal Biochemistry (1982) 21:3298-3303 !$#title Amino acid sequence of amyloid-related apoprotein (apoSAA-1) !1from human high-density lipoprotein. !$#cross-references MUID:83000248; PMID:7115671 !$#contents allele SAA1*1 (SAA1-alpha) !$#accession A90461 !'##molecule_type protein !'##residues 19-122 ##label PAR !'##note 70-Ala and 75-Val were also found !'##note this protein was isolated from the high-density lipoprotein !1fraction of serum REFERENCE A91711 !$#authors Sletten, K.; Marhaug, G.; Husby, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1983) 364:1039-1046 !$#title The covalent structure of amyloid-related serum protein SAA !1from two patients with inflammatory disease. !$#cross-references MUID:84030495; PMID:6629328 !$#contents allele SAA1*1 (SAA1-alpha) !$#accession A91711 !'##molecule_type protein !'##residues 19-40,'N',42-77,'N',79-92,'N',94-122 ##label SLE !'##note at least three polymorphic forms of this protein have been !1found in a patient with chronic inflammatory disease; both !1alanine and valine occur at positions 70 and 75, and both !1isoleucine and leucine are found at position 76 REFERENCE A29419 !$#authors Prelli, F.; Pras, M.; Frangione, B. !$#journal Biochemistry (1987) 26:8251-8256 !$#title Degradation and deposition of amyloid AA fibrils are tissue !1specific. !$#cross-references MUID:88163487; PMID:3442653 !$#contents allele SAA1*1 (SAA1-alpha) !$#accession A29419 !'##molecule_type protein !'##residues 20-100 ##label PRE REFERENCE A60431 !$#authors Westermark, G.T.; Sletten, K.; Westermark, P. !$#journal Scand. J. Immunol. (1989) 30:605-613 !$#title Massive vascular AA-amyloidosis: a histologically and !1biochemically distinctive subtype of reactive systemic !1amyloidosis. !$#cross-references MUID:90069444; PMID:2587936 !$#contents allele SAA1*1 (SAA1-alpha) !$#accession A60431 !'##molecule_type protein !'##residues 19-98,'XXXX',103-105,'X',107 ##label WES REFERENCE S21260 !$#authors Beach, C.M.; de Beer, M.C.; Sipe, J.D.; Loose, L.D.; de !1Beer, F.C. !$#journal Biochem. J. (1992) 282:615-620 !$#title Human serum amyloid A protein. Complete amino acid sequence !1of a new variant. !$#cross-references MUID:92189607; PMID:1546977 !$#contents allele SAA1*2a (SAA1-beta) !$#accession S21261 !'##molecule_type protein !'##residues 19-69,'A',71-74,'V',76-89,'D',91-122 ##label BEA !$#accession S21260 !'##molecule_type protein !'##residues 20-69,'A',71-74,'V',76-89,'D',91-122 ##label BE2 REFERENCE S33864 !$#authors Baba, S.; Takahashi, T.; Kasama, T.; Fujie, M.; Shirasawa, !1H. !$#journal Arch. Biochem. Biophys. (1993) 303:361-366 !$#title A novel polymorphism of human serum amyloid A protein, !1SAA1gamma, is characterized by alanines at both residues 52 !1and 57. !$#cross-references MUID:93290347; PMID:8512321 !$#contents allele SAA1-gamma !$#accession S33864 !'##molecule_type protein !'##residues 19-69,'A',71-122 ##label BAB REFERENCE A56867 !$#authors Baba, S.; Takahashi, T.; Kasama, T.; Shirasawa, H. !$#journal Biochim. Biophys. Acta (1992) 1180:195-200 !$#title Identification of two novel amyloid A protein subsets !1coexisting in an individual patient of AA-amyloidosis. !$#cross-references MUID:93099171; PMID:1463770 !$#contents allele SAA1-gamma (allele 52,57-Ala) !$#accession A56867 !'##molecule_type protein !'##residues 65-69,'A',71-80 ##label BA2 !'##experimental_source amyloid fibrils, thyroid gland of rheumatoid !1arthritis patient !'##note sequence extracted from NCBI backbone (NCBIP:121042) REFERENCE A94234 !$#authors Moyner, K.; Sletten, K.; Husby, G.; Natvig, J.B. !$#journal Scand. J. Immunol. (1980) 11:549-554 !$#title An unusually large (83 amino acid residues) amyloid fibril !1protein AA from a patient with Waldenstroem's !1macroglobulinaemia and amyloidosis. !$#cross-references MUID:80213686; PMID:6155694 !$#contents Bol !$#accession A94234 !'##molecule_type protein !'##residues 19-40,'N',42-83,'E',85-92,'N',94-95,'SEATVK' ##label MOY !'##note 70-Ala and 71-Arg were also found !'##note this protein is from a patient with Waldenstrom's !1macroglobulinemia REFERENCE A91215 !$#authors Sletten, K.; Husby, G. !$#journal Eur. J. Biochem. (1974) 41:117-125 !$#title The complete amino-acid sequence of non-immunoglobulin !1amyloid fibril protein AS in rheumatoid arthritis. !$#cross-references MUID:74120351; PMID:4816450 !$#contents Th !$#accession A91215 !'##molecule_type protein !'##residues 19-40,'N',42-92,'N',94 ##label SL3 !'##note this protein is from a patient with juvenile rheumatoid !1arthritis REFERENCE A90195 !$#authors Sletten, K.; Husby, G.; Natvig, J.B. !$#journal Biochem. Biophys. Res. Commun. (1976) 69:19-25 !$#title The complete amino acid sequence of an amyloid fibril !1protein AA of unusual size (64 residues). !$#cross-references MUID:76160745; PMID:1259755 !$#contents Jl !$#accession A90195 !'##molecule_type protein !'##residues 19-40,'N',42-77,'N',79-82 ##label SL2 !'##note 19-Arg is missing from some of the molecules !'##note this protein is from a patient with ankylosing spondylitis REFERENCE A30323 !$#authors Gorevic, P.D.; Prelli, F.C.; Wright, J.; Pras, M.; !1Frangione, B. !$#journal J. Clin. Invest. (1989) 83:836-843 !$#title Systemic senile amyloidosis. Identification of a new !1prealbumin (transthyretin) variant in cardiac tissue: !1immunologic and biochemical similarity to one form of !1familial amyloidotic polyneuropathy. !$#cross-references MUID:89155805; PMID:2646319 !$#accession B30323 !'##molecule_type protein !'##residues 19-29 ##label GOR REFERENCE A38975 !$#authors Uhlar, C.M.; Burgess, C.J.; Sharp, P.M.; Whitehead, A.S. !$#journal Genomics (1994) 19:228-235 !$#title Evolution of the serum amyloid A (SAA) protein superfamily. !$#cross-references MUID:94245191; PMID:8188253 !$#contents annotation REFERENCE I39454 !$#authors Kluve-Beckerman, B.; Dwulet, F.E.; Benson, M.D. !$#journal J. Clin. Invest. (1988) 82:1670-1675 !$#title Human serum amyloid A. Three hepatic mRNAs and the !1corresponding proteins in one person. !$#cross-references MUID:89034862; PMID:3183061 !$#accession I39454 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-122 ##label RES !'##cross-references GB:M23698; NID:g758678; PIDN:AAA64799.1; !1PID:g758679 GENETICS !$#gene GDB:SAA1; SAA !'##cross-references GDB:120364; OMIM:104750 !$#map_position 11p15.1-11p15.1 !$#introns 31/1; 77/2 CLASSIFICATION #superfamily amyloid protein KEYWORDS acute phase; amyloid; HDL; polymorphism FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-122 #product (or 20-122) serum amyloid A1 protein #status !8experimental #label APA\ !$19-94 #product (or 20-94) amyloid protein AA #status !8experimental #label AP3 SUMMARY #length 122 #molecular-weight 13532 #checksum 9658 SEQUENCE /// ENTRY YLHUA #type complete TITLE serum amyloid A2 protein precursor [validated] - human ALTERNATE_NAMES amyloid IV; amyloid protein AA (FMF); amyloid-related serum protein SAA ORGANISM #formal_name Homo sapiens #common_name man DATE 24-Apr-1984 #sequence_revision 08-Feb-1996 #text_change 08-Dec-2000 ACCESSIONS A27902; S20104; S09975; S09976; S09973; B38974; A28445; !1A92763; A92112; A91345; B56867; I39455; A03197 REFERENCE A27902 !$#authors Kluve-Beckerman, B.; Long, G.L.; Benson, M.D. !$#journal Biochem. Genet. (1986) 24:795-803 !$#title DNA sequence evidence for polymorphic forms of human serum !1amyloid A (SAA). !$#cross-references MUID:87099785; PMID:3800865 !$#contents allele SAA2*1 (SAA2-alpha) !$#accession A27902 !'##molecule_type mRNA !'##residues 1-122 ##label KLU !'##cross-references GB:M26152; NID:g1160968; PIDN:AAA85338.1; !1PID:g1160969 REFERENCE S20103 !$#authors Betts, J.C.; Edbrooke, M.R.; Thakker, R.V.; Woo, P. !$#journal Scand. J. Immunol. (1991) 34:471-482 !$#title The human acute-phase serum amyloid A gene family: !1structure, evolution and expression in hepatoma cells. !$#cross-references MUID:92022342; PMID:1656519 !$#contents allele SAA2*1 (SAA2-alpha) !$#accession S20104 !'##status translation not shown !'##molecule_type DNA !'##residues 32-122 ##label BET !'##cross-references EMBL:X56653; NID:g36309; PIDN:CAA39975.1; !1PID:g36310 REFERENCE S09972 !$#authors Steinkasserer, A.; Weiss, E.H.; Schwaeble, W.; Linke, R.P. !$#journal Biochem. J. (1990) 268:187-193 !$#title Heterogeneity of human serum amyloid A protein: five !1different variants from one individual demonstrated by cDNA !1sequence analysis. !$#cross-references MUID:90262544; PMID:1971508 !$#accession S09975 !'##molecule_type mRNA !'##residues 1-55 ##label STE !'##cross-references EMBL:X51444; NID:g36316; PIDN:CAA35809.1; !1PID:g36317 !'##experimental_source clone pAS6 !'##note allele SAA2*1 (SAA2-alpha) !$#accession S09976 !'##molecule_type mRNA !'##residues 4-122 ##label ST2 !'##cross-references EMBL:X51445; NID:g36320; PIDN:CAA35810.1; !1PID:g36321 !'##experimental_source clone pAS8 !'##note allele SAA2*1 (SAA2-alpha) !$#accession S09973 !'##molecule_type mRNA !'##residues 73-88,'R',90-122 ##label ST3 !'##cross-references EMBL:X51440; NID:g36312; PIDN:CAA35805.1; !1PID:g825715 !'##experimental_source clone pAS2 !'##note allele SAA2*2 (SAA2-beta) REFERENCE A38974 !$#authors Steel, D.M.; Sellar, G.C.; Uhlar, C.M.; Simon, S.; DeBeer, !1F.C.; Whitehead, A.S. !$#journal Genomics (1993) 16:447-454 !$#title A constitutively expressed serum amyloid A protein gene !1(SAA4) is closely linked to, and shares structural !1similarities with, an acute-phase serum amyloid A protein !1gene (SAA2). !$#cross-references MUID:93300520; PMID:7686132 !$#contents allele SAA2*2 (SAA2-beta) !$#accession B38974 !'##molecule_type DNA !'##residues 1-88,'R',90-122 ##label ST4 !'##cross-references GB:L05921 REFERENCE A28445 !$#authors Woo, P.; Sipe, J.; Dinarello, C.A.; Colten, H.R. !$#journal J. Biol. Chem. (1987) 262:15790-15795 !$#title Structure of a human serum amyloid A gene and modulation of !1its expression in transfected L cells. !$#cross-references MUID:88058926; PMID:2890635 !$#contents allele SAA2*2 (SAA2-beta) !$#accession A28445 !'##molecule_type DNA !'##residues 1-14,'G',16-88,'R',90-122 ##label WOO !'##cross-references GB:J03474; NID:g337742; PIDN:AAB59539.1; !1PID:g337743 REFERENCE A92763 !$#authors Levin, M.; Franklin, E.C.; Frangione, B.; Pras, M. !$#journal J. Clin. Invest. (1972) 51:2773-2776 !$#title The amino acid sequence of a major nonimmunoglobulin !1component of some amyloid fibrils. !$#cross-references MUID:72268653; PMID:5056669 !$#contents allele SAA2*2 (SAA2-beta) !$#accession A92763 !'##molecule_type protein !'##residues 19-70,'R',72-88,'R',90-94 ##label LEV !'##note this protein is from a patient with familial Mediterranean !1fever !'##note the sequence of residues 19-72 of amyloid protein AA from a !1patient with tuberculosis was identical except in having !170-Val REFERENCE A92112 !$#authors Ein, D.; Kimura, S.; Terry, W.D.; Magnotta, J.; Glenner, !1G.G. !$#journal J. Biol. Chem. (1972) 247:5653-5655 !$#title Amino acid sequence of an amyloid fibril protein of unknown !1origin. !$#cross-references MUID:72266694; PMID:5055786 !$#accession A92112 !'##molecule_type protein !'##residues 19-63 ##label EIN !'##note this amyloid IV was isolated from a patient with rheumatoid !1arthritis REFERENCE A91345 !$#authors Benditt, E.P.; Eriksen, N.; Hermodson, M.A.; Ericsson, L.H. !$#journal FEBS Lett. (1971) 19:169-173 !$#title The major proteins of human and monkey amyloid substance: !1common properties including unusual N-terminal amino acid !1sequences. !$#accession A91345 !'##molecule_type protein !'##residues 19-42 ##label BEN !'##note the amino-terminal tripeptide is sometimes missing !'##note this protein is from a patient with generalized amyloidosis !1associated with tuberculosis REFERENCE A56867 !$#authors Baba, S.; Takahashi, T.; Kasama, T.; Shirasawa, H. !$#journal Biochim. Biophys. Acta (1992) 1180:195-200 !$#title Identification of two novel amyloid A protein subsets !1coexisting in an individual patient of AA-amyloidosis. !$#cross-references MUID:93099171; PMID:1463770 !$#contents allele SAA2*1 (SAA2-alpha) !$#accession B56867 !'##molecule_type protein !'##residues 65-80 ##label BAB !'##experimental_source amyloid fibrils, thyroid gland of rhematoid !1arthritis patient !'##note sequence extracted from NCBI backbone (NCBIP:121046) REFERENCE I39454 !$#authors Kluve-Beckerman, B.; Dwulet, F.E.; Benson, M.D. !$#journal J. Clin. Invest. (1988) 82:1670-1675 !$#title Human serum amyloid A. Three hepatic mRNAs and the !1corresponding proteins in one person. !$#cross-references MUID:89034862; PMID:3183061 !$#accession I39455 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-122 ##label RES !'##cross-references GB:M23699; NID:g758680; PIDN:AAA64800.1; !1PID:g758681 GENETICS !$#gene GDB:SAA2 !'##cross-references GDB:132592; OMIM:104751 !$#map_position 11p15.1-11p15.1 !$#introns 31/1; 77/2 CLASSIFICATION #superfamily amyloid protein KEYWORDS acute phase; amyloid; polymorphism FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-94 #product serum amyloid A2 protein #status !8experimental #label MAT SUMMARY #length 122 #molecular-weight 13508 #checksum 1374 SEQUENCE /// ENTRY YLMQAR #type complete TITLE amyloid protein AA - rhesus macaque ORGANISM #formal_name Macaca mulatta #common_name rhesus macaque DATE 07-May-1981 #sequence_revision 07-May-1981 #text_change 31-Dec-1993 ACCESSIONS A03198 REFERENCE A03198 !$#authors Hermodson, M.A.; Kuhn, R.W.; Walsh, K.A.; Neurath, H.; !1Eriksen, N.; Benditt, E.P. !$#journal Biochemistry (1972) 11:2934-2938 !$#title Amino acid sequence of monkey amyloid protein A. !$#cross-references MUID:72230069; PMID:4625315 !$#accession A03198 !'##molecule_type protein !'##residues 1-76 ##label HER CLASSIFICATION #superfamily amyloid protein KEYWORDS amyloid SUMMARY #length 76 #molecular-weight 8620 #checksum 8466 SEQUENCE /// ENTRY YLCTA #type complete TITLE amyloid protein AA - cat ORGANISM #formal_name Felis silvestris catus #common_name domestic cat DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 11-May-2000 ACCESSIONS JL0111 REFERENCE JL0110 !$#authors Kluve-Beckerman, B.; Dwulet, F.E.; DiBartola, S.P.; Benson, !1M.D. !$#journal Comp. Biochem. Physiol. B (1989) 94:175-183 !$#title Primary structures of dog and cat amyloid A proteins: !1comparison to human AA. !$#cross-references MUID:90091422; PMID:2598632 !$#accession JL0111 !'##molecule_type protein !'##residues 1-90 ##label KLU !'##note no overlap was shown between residues 88 and 89 COMMENT This protein is the main constituent of reactive amyloid !1fibrils in man and in several other species affected by !1amyloidosis, whether spontaneous or induced by chronic !1inflammatory stimuli. COMMENT The extracellular deposits formed by this protein are highly !1insoluble and resistant to proteolysis; they disrupt tissue !1structure and compromise function. CLASSIFICATION #superfamily amyloid protein KEYWORDS amyloid SUMMARY #length 90 #molecular-weight 10122 #checksum 4619 SEQUENCE /// ENTRY YLDGA #type fragment TITLE amyloid protein AA precursor (clone DSAA15) - dog (fragment) ORGANISM #formal_name Canis lupus familiaris #common_name dog DATE 30-Sep-1990 #sequence_revision 12-Apr-1996 #text_change 11-May-2000 ACCESSIONS A38645; JL0110 REFERENCE A38645 !$#authors Sellar, G.C.; DeBeer, M.C.; Lelias, J.M.; Snyder, P.W.; !1Glickman, L.T.; Felsburg, P.J.; Whitehead, A.S. !$#journal J. Biol. Chem. (1991) 266:3505-3510 !$#title Dog serum amyloid A protein. Identification of multiple !1isoforms defined by cDNA and protein analyses. !$#cross-references MUID:91139635; PMID:1995613 !$#accession A38645 !'##molecule_type mRNA !'##residues 1-119 ##label SEL !'##cross-references GB:M59171; NID:g164059; PIDN:AAA62762.1; !1PID:g164060 REFERENCE JL0110 !$#authors Kluve-Beckerman, B.; Dwulet, F.E.; DiBartola, S.P.; Benson, !1M.D. !$#journal Comp. Biochem. Physiol. B (1989) 94:175-183 !$#title Primary structures of dog and cat amyloid A proteins: !1comparison to human AA. !$#cross-references MUID:90091422; PMID:2598632 !$#accession JL0110 !'##molecule_type protein !'##residues 9-101 ##label KLU !'##note 25-Trp was also found COMMENT This protein is the main constituent of reactive amyloid !1fibrils in man and in several other species affected by !1amyloidosis, whether spontaneous or induced by chronic !1inflammatory stimuli. COMMENT The extracellular deposits formed by this protein are highly !1insoluble and resistant to proteolysis; they disrupt tissue !1structure and compromise function. CLASSIFICATION #superfamily amyloid protein KEYWORDS amyloid; pyroglutamic acid FEATURE !$1-8 #domain signal sequence (fragment) #status predicted !8#label SIG\ !$9-101 #product amyloid protein AA #status experimental !8#label MAT\ !$9 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental SUMMARY #length 119 #checksum 8511 SEQUENCE /// ENTRY A60952 #type complete TITLE amyloid protein AA - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 03-Mar-1994 #sequence_revision 03-Mar-1994 #text_change 11-May-2000 ACCESSIONS A60952; A60910; A61108 REFERENCE A60952 !$#authors Benson, M.D.; DiBartola, S.P.; Dwulet, F.E. !$#journal J. Lab. Clin. Med. (1989) 113:67-72 !$#title A unique insertion in the primary structure of bovine !1amyloid AA protein. !$#cross-references MUID:89080450; PMID:2909653 !$#accession A60952 !'##molecule_type protein !'##residues 1-90 ##label BEN REFERENCE A60910 !$#authors Husebekk, A.; Husby, G.; Sletten, K.; Skogen, B.; Nordstoga, !1K. !$#journal Scand. J. Immunol. (1988) 27:739-743 !$#title Characterization of bovine amyloid proteins SAA and AA. !$#cross-references MUID:88277778; PMID:3393848 !$#accession A60910 !'##molecule_type protein !'##residues 4-16 ##label HUS !'##experimental_source amyloid fibrils, kidney !'##note An identical fragment was sequenced from its precursor molecule !1serum amyloid A found in complex with HDL in acute phase !1serum REFERENCE A61108 !$#authors Westermark, P.; Johnson, K.H.; Westermark, G.T.; Sletten, !1K.; Hayden, D.W. !$#journal Comp. Biochem. Physiol. B (1986) 85:609-614 !$#title Bovine amyloid protein AA: isolation and amino acid sequence !1analysis. !$#cross-references MUID:87079535; PMID:3791962 !$#accession A61108 !'##molecule_type protein !'##residues 3,'X',5-9,'X',11-13,17-20,'X',22-23,'X',25-28,'Y',30-32, !1'X',34-48 ##label WES COMMENT This protein is derived from the acute phase protein serum !1amyloid A (SAA). COMMENT This protein is the main constituent of reactive amyloid !1fibrils in man and in several other species affected by !1amyloidosis, whether spontaneous or induced by chronic !1inflammatory stimuli. COMMENT The extracellular deposits formed by this protein are highly !1insoluble and resistant to proteolysis; they disrupt tissue !1structure and compromise function. CLASSIFICATION #superfamily amyloid protein KEYWORDS acute phase; amyloid; pyroglutamic acid FEATURE !$1 #modified_site pyrrolidone carboxylic acid (Gln) !8#status experimental SUMMARY #length 90 #molecular-weight 10079 #checksum 4721 SEQUENCE /// ENTRY YLMNA #type complete TITLE amyloid protein AA - American mink ORGANISM #formal_name Mustela vison #common_name American mink DATE 23-Oct-1981 #sequence_revision 23-Oct-1981 #text_change 05-Aug-1994 ACCESSIONS A03199; B03199 REFERENCE A03199 !$#authors Waalen, K.; Sletten, K.; Husby, G.; Nordstoga, K. !$#journal Eur. J. Biochem. (1980) 104:407-412 !$#title The primary structure of amyloid fibril protein AA in !1endotoxin-induced amyloidosis of the mink. !$#cross-references MUID:80156813; PMID:6767608 !$#accession A03199 !'##molecule_type protein !'##residues 1-64 ##label WA1 !$#accession B03199 !'##molecule_type protein !'##residues 1-53 ##label WA2 CLASSIFICATION #superfamily amyloid protein KEYWORDS amyloid; pyroglutamic acid FEATURE !$1-64 #product amyloid protein AA1 #status experimental !8#label AP1\ !$1-53 #product amyloid protein AA2 #status experimental !8#label AP2\ !$1 #modified_site pyrrolidone carboxylic acid (Gln) !8#status experimental SUMMARY #length 64 #molecular-weight 7418 #checksum 6276 SEQUENCE /// ENTRY A38974 #type complete TITLE serum amyloid A4 protein precursor [validated] - human ALTERNATE_NAMES constitutive serum amyloid A protein; serum amyloid A protein, C-SAA ORGANISM #formal_name Homo sapiens #common_name man DATE 08-Feb-1996 #sequence_revision 08-Mar-1996 #text_change 08-Dec-2000 ACCESSIONS A38974; A42258; I59470 REFERENCE A38974 !$#authors Steel, D.M.; Sellar, G.C.; Uhlar, C.M.; Simon, S.; DeBeer, !1F.C.; Whitehead, A.S. !$#journal Genomics (1993) 16:447-454 !$#title A constitutively expressed serum amyloid A protein gene !1(SAA4) is closely linked to, and shares structural !1similarities with, an acute-phase serum amyloid A protein !1gene (SAA2). !$#cross-references MUID:93300520; PMID:7686132 !$#accession A38974 !'##molecule_type DNA !'##residues 1-130 ##label STE !'##cross-references GB:L05920 REFERENCE A42258 !$#authors Whitehead, A.S.; de Beer, M.C.; Steel, D.M.; Rits, M.; !1Lelias, J.M.; Lane, W.S.; de Beer, F.C. !$#journal J. Biol. Chem. (1992) 267:3862-3867 !$#title Identification of novel members of the serum amyloid A !1protein superfamily as constitutive apolipoproteins of high !1density lipoprotein. !$#cross-references MUID:92156125; PMID:1740433 !$#accession A42258 !'##molecule_type mRNA !'##residues 1-130 ##label WHI !'##cross-references GB:M81349; NID:g337749; PIDN:AAA60298.1; !1PID:g337750 !'##experimental_source liver !'##note sequence extracted from NCBI backbone (NCBIP:82631) !'##note parts of this sequence, including the amino and carboxyl ends !1of the mature protein, were determined by protein sequencing REFERENCE I59470 !$#authors Watson, G.; Coade, S.; Woo, P. !$#journal Scand. J. Immunol. (1992) 36:703-712 !$#title Analysis of the genomic and derived protein structure of a !1novel human serum amyloid A gene, SAA4. !$#cross-references MUID:93068025; PMID:1439582 !$#accession I59470 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-130 ##label RES !'##cross-references GB:S48983; NID:g259351; PIDN:AAB24060.1; !1PID:g259352 GENETICS !$#gene GDB:SAA4 !'##cross-references GDB:132594; OMIM:104752 !$#map_position 11p15.1-11p15.1 !$#introns 31/1; 77/2 CLASSIFICATION #superfamily amyloid protein KEYWORDS acute phase; amyloid; glycoprotein FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-130 #product serum amyloid A4 protein #status !8experimental #label MAT\ !$94 #binding_site carbohydrate (Asn) (covalent) (partial) !8#status experimental SUMMARY #length 130 #molecular-weight 14807 #checksum 6000 SEQUENCE /// ENTRY YLDKA #type fragment TITLE amyloid protein AA - duck (tentative sequence) (fragment) ORGANISM #formal_name Anas platyrhynchos #common_name domestic duck DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 31-Mar-2000 ACCESSIONS A03200 REFERENCE A03200 !$#authors Gorevic, P.D.; Greenwald, M.; Frangione, B.; Pras, M.; !1Franklin, E.C. !$#journal J. Immunol. (1977) 118:1113-1118 !$#title The amino acid sequence of duck amyloid A (AA) protein. !$#cross-references MUID:77142518; PMID:845435 !$#accession A03200 !'##molecule_type protein !'##residues 1-80 ##label GOR !'##experimental_source Pekin breed !'##note 33-Tyr, 34-Val, and 63-Ser were also found !'##note although the sequence shown is homologous with other amyloid AA !1proteins, the authors suggest that an extension of the !1carboxyl end is likely; the molecular weight of the isolated !1protein appeared to be 12,000, and several additional !1tryptic peptides were found in low yield CLASSIFICATION #superfamily amyloid protein KEYWORDS amyloid SUMMARY #length 80 #checksum 3572 SEQUENCE /// ENTRY CJHU #type complete TITLE C-reactive protein precursor [validated] - human ALTERNATE_NAMES CRP ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1980 #sequence_revision 31-Dec-1992 #text_change 08-Dec-2000 ACCESSIONS A24515; A24514; B24514; A05292; A93808; S21385; I55945; !1S21516; I59496 REFERENCE A92499 !$#authors Lei, K.J.; Liu, T.; Zon, G.; Soravia, E.; Liu, T.Y.; !1Goldman, N.D. !$#journal J. Biol. Chem. (1985) 260:13377-13383 !$#title Genomic DNA sequence for human C-reactive protein. !$#cross-references MUID:86033784; PMID:2997165 !$#accession A24515 !'##molecule_type DNA !'##residues 1-224 ##label LEI !'##cross-references GB:M11725; NID:g181067; PIDN:AAA52075.1; !1PID:g181068 REFERENCE A24514 !$#authors Woo, P.; Korenberg, J.R.; Whitehead, A.S. !$#journal J. Biol. Chem. (1985) 260:13384-13388 !$#title Characterization of genomic and complementary DNA sequence !1of human C-reactive protein, and comparison with the !1complementary DNA sequence of serum amyloid P component. !$#cross-references MUID:86033785; PMID:3840479 !$#accession A24514 !'##molecule_type DNA !'##residues 1-224 ##label WOO !'##cross-references GB:M11880; GB:M11881; GB:M11882; NID:g181065; !1PIDN:AAB59526.1; PID:g181066 !$#accession B24514 !'##molecule_type mRNA !'##residues 1-224 ##label WOO2 !'##cross-references GB:M11880; GB:M11881; GB:M11882; NID:g181065; !1PIDN:AAB59526.1; PID:g181066 REFERENCE A94674 !$#authors Oliveira, E.B.; Gotschlich, E.C.; Liu, T.Y. !$#journal J. Biol. Chem. (1979) 254:489-502 !$#title Primary structure of human C-reactive protein. !$#cross-references MUID:79109592; PMID:762075 !$#accession A05292 !'##molecule_type protein !'##residues 19-82;102-224 ##label OLI REFERENCE A93808 !$#authors Osmand, A.P.; Gewurz, H.; Friedenson, B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1977) 74:1214-1218 !$#title Partial amino-acid sequences of human and rabbit C-reactive !1protein: homology with immunoglobulins and !1histocompatibility antigens. !$#cross-references MUID:77148979; PMID:403526 !$#accession A93808 !'##molecule_type protein !'##residues 22-48,'G',50-51,'G',53,'X',55 ##label OSM REFERENCE S21385 !$#authors Murphy, T.M.; Baum, L.; Beaman, K. !$#submission submitted to the EMBL Data Library, November 1990 !$#description Extrahepetic transcription of human C-reactive protein. !$#accession S21385 !'##status preliminary !'##molecule_type mRNA !'##residues 1-224 ##label MUR !'##cross-references EMBL:X56692; NID:g30212; PIDN:CAA40020.1; !1PID:g30213 REFERENCE I55945 !$#authors Tucci, A.; Goldberger, G.; Whitehead, A.S.; Kay, R.M.; !1Woods, D.E.; Colten, H.R. !$#journal J. Immunol. (1983) 131:2416-2419 !$#title Biosynthesis and postsynthetic processing of human !1C-reactive protein. !$#cross-references MUID:84034218; PMID:6685157 !$#accession I55945 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-26 ##label RES !'##cross-references GB:M35163; NID:g181072; PIDN:AAA52076.1; !1PID:g181073 REFERENCE S21516 !$#authors Tenchini, M.L.; Marchetti, L.; Bossi, E.; Malcovati, M.; !1Lorenzetti, R. !$#submission submitted to the EMBL Data Library, December 1990 !$#accession S21516 !'##molecule_type mRNA !'##residues 1-66,'TVFSRMPPRDKTMRFF',83-224 ##label TEN !'##cross-references EMBL:X56214; NID:g30223; PIDN:CAA39671.1; !1PID:g30224 !'##note the region of difference likely results from frameshift errors REFERENCE I59496 !$#authors Whitehead, A.S.; Bruns, G.A.; Markham, A.F.; Colten, H.R.; !1Woods, D.E. !$#journal Science (1983) 221:69-71 !$#title Isolation of human C-reactive protein complementary DNA and !1localization of the gene to chromosome 1. !$#cross-references MUID:83223601; PMID:6857266 !$#accession I59496 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 144-169,'V',171-175 ##label RE2 !'##cross-references GB:K00518; NID:g181060; PIDN:AAA52074.1; !1PID:g181061 COMMENT The CRP molecule is a cyclic pentamer of identical chains. COMMENT The concentration of CRP in plasma increases greatly (up to !1over 1000-fold) after acute infection. CRP may act as an !1addtional initiator of complement system. COMMENT CRP binds phosphorylcholine. COMMENT CRP is synthesized mainly in hepatocytes. Its synthesis is !1possibly induced by interleukin I. GENETICS !$#gene GDB:CRP !'##cross-references GDB:119071; OMIM:123260 !$#map_position 1q21-1q23 !$#introns 21/1 !$#note the list of introns is incomplete CLASSIFICATION #superfamily C-reactive protein KEYWORDS acute phase; liver; pentamer; pentraxin; plasma; !1pyroglutamic acid FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-224 #product C-reactive protein #status experimental !8#label MAT\ !$19 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$54-115 #disulfide_bonds #status experimental SUMMARY #length 224 #molecular-weight 25038 #checksum 1038 SEQUENCE /// ENTRY CJRB #type complete TITLE C-reactive protein precursor - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 05-Apr-1983 #sequence_revision 18-Jul-1997 #text_change 22-Jun-1999 ACCESSIONS A25605; A25583; A03202 REFERENCE A25605 !$#authors Syin, C.; Gotschlich, E.C.; Liu, T.Y. !$#journal J. Biol. Chem. (1986) 261:5473-5479 !$#title Rabbit C-reactive protein. Biosynthesis and characterization !1of cDNA clones. !$#cross-references MUID:86168292; PMID:3007506 !$#accession A25605 !'##molecule_type mRNA !'##residues 1-225 ##label SYI !'##cross-references GB:M13497; NID:g164901; PIDN:AAA31206.1; !1PID:g164902 REFERENCE A25583 !$#authors Hu, S.I.; Miller, S.M.; Samols, D. !$#journal Biochemistry (1986) 25:7834-7839 !$#title Cloning and characterization of the gene for rabbit !1C-reactive protein. !$#cross-references MUID:87101075; PMID:3026463 !$#accession A25583 !'##molecule_type DNA !'##residues 1-9,'T',11-107,'I',109-192,'I',194-225 ##label HUS !'##cross-references GB:M14538; NID:g164899; PIDN:AAA75403.1; !1PID:g164900 REFERENCE A03202 !$#authors Wang, C.M.; Nguyen, N.Y.; Yonaha, K.; Robey, F.; Liu, T.Y. !$#journal J. Biol. Chem. (1982) 257:13610-13615 !$#title Primary structure of rabbit C-reactive protein. !$#cross-references MUID:83056861; PMID:6754715 !$#accession A03202 !'##molecule_type protein !'##residues 21-45,'T',47-49,'L',51-83,'F',85,105,'KE',108,'I',110,'Y', !1112-166,'W',168-176,'D',178-225 ##label WAN !'##note 62-Lys and 108-Asp were also found !'##note Asp-61, Arg-76, Arg-77, and Glu-81 may be involved in the !1calcium-dependent binding of phosphorylcholine, a property !1that may be important for the biological function of this !1protein GENETICS !$#introns 22/1 CLASSIFICATION #superfamily C-reactive protein KEYWORDS acute phase; pentamer; plasma FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-225 #product C-reactive protein #status experimental !8#label MAT\ !$55-116 #disulfide_bonds #status experimental SUMMARY #length 225 #molecular-weight 25477 #checksum 5987 SEQUENCE /// ENTRY YLHUP #type complete TITLE serum amyloid P-component precursor [validated] - human ALTERNATE_NAMES SAP ORGANISM #formal_name Homo sapiens #common_name man DATE 13-Jun-1983 #sequence_revision 10-May-1996 #text_change 08-Dec-2000 ACCESSIONS A25503; A92539; A24080; A94632; A90418; A03203 REFERENCE A25503 !$#authors Ohnishi, S.; Maeda, S.; Shimada, K.; Arao, T. !$#journal J. Biochem. (1986) 100:849-858 !$#title Isolation and characterization of the complete complementary !1and genomic DNA sequences of human serum amyloid P !1component. !$#cross-references MUID:87137351; PMID:3029048 !$#accession A25503 !'##molecule_type mRNA !'##residues 1-223 ##label OHN !'##cross-references GB:X04608; NID:g36330; PIDN:CAA28275.1; PID:g36331 REFERENCE A92539 !$#authors Mantzouranis, E.C.; Dowton, S.B.; Whitehead, A.S.; Edge, !1M.D.; Bruns, G.A.P.; Colten, H.R. !$#journal J. Biol. Chem. (1985) 260:7752-7756 !$#title Human serum amyloid P component. cDNA isolation, complete !1sequence of pre-serum amyloid P component, and localization !1of the gene to chromosome 1. !$#cross-references MUID:85207828; PMID:2987268 !$#accession A92539 !'##molecule_type mRNA !'##residues 1-100,'P',102-223 ##label MAN !'##cross-references GB:M10944; NID:g337757; PIDN:AAA60302.1; !1PID:g337758 REFERENCE A24080 !$#authors Prelli, F.; Pras, M.; Frangione, B. !$#journal J. Biol. Chem. (1985) 260:12895-12898 !$#title The primary structure of human tissue amyloid P component !1from a patient with primary idiopathic amyloidosis. !$#cross-references MUID:86033713; PMID:4055725 !$#accession A24080 !'##molecule_type protein !'##residues 20-100,'P',102-223 ##label PRE REFERENCE A94632 !$#authors Frangione, B. !$#submission submitted to the Protein Sequence Database, June 1985 !$#accession A94632 !'##molecule_type protein !'##residues 20-100,'P',102-223 ##label FRA REFERENCE A90418 !$#authors Thompson, A.R.; Enfield, D.L. !$#journal Biochemistry (1978) 17:4304-4311 !$#title Human plasma P component: isolation and characterization. !$#cross-references MUID:79042150; PMID:81686 !$#accession A90418 !'##molecule_type protein !'##residues 20-49 ##label THO COMMENT SAP is a decamer of identical chains. The molecule consists !1of two pentameric discs of protomers connected by their !1ends, as is characteristic of pentraxins. GENETICS !$#gene GDB:APCS !'##cross-references GDB:118999; OMIM:104770 !$#map_position 1q21-1q23 CLASSIFICATION #superfamily C-reactive protein KEYWORDS amyloid; glycoprotein; pentraxin; plasma FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-223 #product serum amyloid P-component #status !8experimental #label MPT\ !$51 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$55-114 #disulfide_bonds #status experimental SUMMARY #length 223 #molecular-weight 25387 #checksum 8840 SEQUENCE /// ENTRY LSHC #type fragment TITLE limulin - Atlantic horseshoe crab (tentative sequence) (fragment) ORGANISM #formal_name Limulus polyphemus #common_name Atlantic horseshoe crab DATE 31-May-1979 #sequence_revision 08-Oct-1981 #text_change 31-Mar-2000 ACCESSIONS A03204 REFERENCE A03204 !$#authors Kaplan, R.; Li, S.S.L.; Kehoe, J.M. !$#journal Biochemistry (1977) 16:4297-4303 !$#title Molecular characterization of limulin, a sialic acid binding !1lectin from the hemolymph of the horseshoe crab, Limulus !1polyphemus. !$#cross-references MUID:78000308; PMID:409430 !$#accession A03204 !'##molecule_type protein !'##residues 1-84 ##label KAP !'##note a disulfide bond links Cys-38 to a Cys in the carboxyl half of !1the chain of 163 residues !'##note a possible carbohydrate binding site is located between !1positions 14 and 20; this lectin binds sialic acid COMMENT This protein is distantly related to mammalian C-reactive !1protein. CLASSIFICATION #superfamily C-reactive protein KEYWORDS lectin; pentamer SUMMARY #length 84 #checksum 6505 SEQUENCE /// ENTRY KGHUH1 #type complete TITLE kininogen, HMW precursor [validated] - human ALTERNATE_NAMES alpha-2-thiol proteinase inhibitor; preprokininogen; prokininogen CONTAINS bradykinin (kallidin I); HMW kininogen I; HMW kininogen II; low molecular weight growth promoting factor; lysyl-bradykinin (kallidin II) ORGANISM #formal_name Homo sapiens #common_name man DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 08-Dec-2000 ACCESSIONS A01279; A25276; S32422; A91153; A24871; A27899; A27699; !1A31905; A34030; S02482; A61495; B61495; C61495; S14447; !1S55239; S68059 REFERENCE A90490 !$#authors Ohkubo, I.; Kurachi, K.; Takasawa, T.; Shiokawa, H.; Sasaki, !1M. !$#journal Biochemistry (1984) 23:5691-5697 !$#title Isolation of a human cDNA for alpha-2-thiol proteinase !1inhibitor and its identity with low molecular weight !1kininogen. !$#cross-references MUID:85122621; PMID:6441591 !$#accession A01279 !'##molecule_type mRNA !'##residues 1-389 ##label OHK !'##cross-references GB:K02566; NID:g177889 REFERENCE A92544 !$#authors Takagaki, Y.; Kitamura, N.; Nakanishi, S. !$#journal J. Biol. Chem. (1985) 260:8601-8609 !$#title Cloning and sequence analysis of cDNAs for human high !1molecular weight and low molecular weight prekininogens. !$#cross-references MUID:85234582; PMID:2989293 !$#accession A25276 !'##molecule_type mRNA !'##residues 1-592,'I',594-644 ##label TAK !'##cross-references GB:M11437; NID:g186751; PIDN:AAB59550.1; !1PID:g386852 REFERENCE S32422 !$#authors Auerswald, E.A.; Roessler, D.; Mentele, R.; !1Assfalg-Machleidt, I. !$#journal FEBS Lett. (1993) 321:93-97 !$#title Cloning, expression and characterization of human kininogen !1domain 3. !$#cross-references MUID:93223854; PMID:8467916 !$#accession S32422 !'##molecule_type mRNA !'##residues 'ANSM',253-377 ##label AUE !'##note differences are due to known cloning artifacts REFERENCE A91153 !$#authors Lottspeich, F.; Kellermann, J.; Henschen, A.; Foertsch, B.; !1Muller-Esterl, W. !$#journal Eur. J. Biochem. (1985) 152:307-314 !$#title The amino acid sequence of the light chain of human !1high-molecular-mass kininogen. !$#cross-references MUID:86030270; PMID:4054110 !$#accession A91153 !'##molecule_type protein !'##residues 379-644 ##label LOT !'##note the bradykinin sequence preceding the light chain sequence was !1not determined in this work REFERENCE A24871 !$#authors Kellermann, J.; Lottspeich, F.; Henschen, A.; !1Mueller-Esterl, W. !$#journal Eur. J. Biochem. (1986) 154:471-478 !$#title Completion of the primary structure of human !1high-molecular-mass kininogen. The amino acid sequence of !1the entire heavy chain and evidence for its evolution by !1gene triplication. !$#cross-references MUID:86108361; PMID:3484703 !$#accession A24871 !'##molecule_type protein !'##residues 'Z',20-380 ##label KEL1 REFERENCE A27899 !$#authors Kellermann, J.; Lottspeich, F.; Henschen, A.; !1Mueller-Esterl, W. !$#book Kinins IV, Greenbaum, L.M., and Margolius, H.S., ed., !1pp.85-89, Plenum Press, New York, 1986 !$#title Amino acid sequence of the light chain of human high !1molecular mass kininogen. !$#accession A27899 !'##molecule_type protein !'##residues 379-389,'K',390-407,'Q',409-644 ##label KEL2 REFERENCE A27699 !$#authors Mindroiu, T.; Carretero, O.A.; Proud, D.; Walz, D.; Scicli, !1A.G. !$#journal Biochem. Biophys. Res. Commun. (1988) 152:519-526 !$#title A new kinin moiety in human plasma kininogens. !$#cross-references MUID:88209021; PMID:3365237 !$#accession A27699 !'##molecule_type protein !'##residues 380-389 ##label MIN REFERENCE A31905 !$#authors Maeda, H.; Matsumura, Y.; Kato, H. !$#journal J. Biol. Chem. (1988) 263:16051-16054 !$#title Purification and identification of [hydroxyprolyl(3)] !1bradykinin in ascitic fluid from a patient with gastric !1cancer. !$#cross-references MUID:89034061; PMID:3182782 !$#accession A31905 !'##molecule_type protein !'##residues 381-389 ##label MAE REFERENCE A34030 !$#authors Sasaguri, M.; Ikeda, M.; Ideishi, M.; Arakawa, K. !$#journal Biochem. Biophys. Res. Commun. (1988) 150:511-516 !$#title Identification of [hydroxyproline(3)]-lysyl-bradykinin !1released from human plasma protein by kallikrein. !$#cross-references MUID:88106632; PMID:3337729 !$#accession A34030 !'##molecule_type protein !'##residues 380-389 ##label SAS REFERENCE S02482 !$#authors Lenarcic, B.; Gabrijelcic, D.; Rozman, B.; Drobnic-Kosorok, !1M.; Turk, V. !$#journal Biol. Chem. Hoppe-Seyler (1988) 369:257-261 !$#title Human cathepsin B and cysteine proteinase inhibitors (CPIs) !1in inflammatory and metabolic joint diseases. !$#cross-references MUID:89076517; PMID:3264507 !$#accession S02482 !'##molecule_type protein !'##residues 1-19;189-192;310-314;381-389 ##label LEN1 REFERENCE A61495 !$#authors Kato, H.; Matsumura, Y.; Maeda, H. !$#journal FEBS Lett. (1988) 232:252-254 !$#title Isolation and identification of hydroxyproline analogues of !1bradykinin in human urine. !$#cross-references MUID:88211869; PMID:3366244 !$#accession A61495 !'##molecule_type protein !'##residues 380-389 ##label KAT1 !'##experimental_source urine !'##note this peptide had Pro-383 modified to 4-hydroxyproline !$#accession B61495 !'##molecule_type protein !'##residues 381-389 ##label KAT2 !'##experimental_source urine !'##note this peptide had Pro-383 modified to 4-hydroxyproline !$#accession C61495 !'##molecule_type protein !'##residues 380-389 ##label KAT3 REFERENCE S14303 !$#authors Lenarcic, B.; Krasovec, M.; Ritonja, A.; Olafsson, I.; Turk, !1V. !$#journal FEBS Lett. (1991) 280:211-215 !$#title Inactivation of human cystatin C and kininogen by human !1cathepsin D. !$#cross-references MUID:91192133; PMID:2013314 !$#accession S14447 !'##molecule_type protein !'##residues 264-359,'N',361-375 ##label LEN2 REFERENCE S55239 !$#authors Little, S.S.; Johnson, D.A. !$#journal Biochem. J. (1995) 307:341-346 !$#title Human mast cell tryptase isoforms: separation and !1examination of substrate-specificity differences. !$#cross-references MUID:95251593; PMID:7733867 !$#accession S55239 !'##molecule_type protein !'##residues 450-452,'X',454,'X',456 ##label LIT REFERENCE S68059 !$#authors Straczek, J.; Maachi, F.; le Nguyen, D.; Becchi, M.; Heulin, !1M.H.; Nabet, P.; Belleville, F. !$#journal FEBS Lett. (1995) 373:207-211 !$#title Purification from human plasma of a tetrapeptide that !1potentiates insulin-like growth factor-I activity in chick !1embryo cartilage. !$#cross-references MUID:96033974; PMID:7589467 !$#accession S68059 !'##molecule_type protein !'##residues 431-434 ##label STR REFERENCE A92545 !$#authors Kitamura, N.; Kitagawa, H.; Fukushima, D.; Takagaki, Y.; !1Miyata, T.; Nakanishi, S. !$#journal J. Biol. Chem. (1985) 260:8610-8617 !$#title Structural organization of the human kininogen gene and a !1model for its evolution. !$#cross-references MUID:85234583; PMID:2989294 !$#contents annotation; gene organization REFERENCE A91455 !$#authors Pierce, J.V. !$#journal Fed. Proc. (1968) 27:52-57 !$#title Structural features of plasma kinins and kininogens. !$#cross-references MUID:90255622; PMID:4952632 !$#contents annotation; bradykinin COMMENT The HMW kininogen precursor and the LMW form are produced !1from the same gene through alternative splicing. COMMENT Kininogen is a cysteine proteinase inhibitor, takes part in !1initiation of the intrinsic pathway of blood coagulation, !1and binds both kallikrein and coagulation factor XI. COMMENT The glycine/histidine/lysine-rich region of HMW kininogen !1light chain is important in mediating clotting activity. COMMENT Bradykinin, released from kininogen by kallikrein, is a !1potent vasodilator, increases capillary permeability, !1mediates inflamation, and causes visceral smooth muscle !1contraction. The hydroxyproline residue is present in the !1kininogen prior to the release of bradykinin. GENETICS !$#gene GDB:KNG !'##cross-references GDB:125256; OMIM:228960 !$#map_position 3q27-3q27 !$#introns 65/3; 102/3; 131/1; 188/3; 224/3; 253/1; 310/3; 346/3; 375/3 CLASSIFICATION #superfamily kininogen; cystatin homology KEYWORDS alternative splicing; blood coagulation; cysteine proteinase !1inhibitor; duplication; glycoprotein; hydroxyproline; !1plasma; pyroglutamic acid; tandem repeat FEATURE !$1-18 #domain signal sequence #status experimental #label !8SIG\ !$19-644 #product HMW kininogen I (prokininogen) #status !8experimental #label MAT1\ !$19-379,390-644 #product HMW kininogen II #status experimental #label !8MAT2\ !$19-379 #domain HMW kininogen heavy chain #status !8experimental #label HCH\ !$19-131 #domain cystatin homology #label CY1\ !$142-253 #domain cystatin homology #label CY2\ !$264-375 #domain cystatin homology #label CY3\ !$380-389 #product lysyl-bradykinin (kallidin II) #status !8experimental #label KBDY\ !$381-389 #product bradykinin (kallidin I) #status experimental !8#label BDY\ !$390-644 #domain HMW kininogen light chain #status !8experimental #label LCH\ !$421-510 #region glycine/histidine/lysine-rich 30-residue !8repeats\ !$431-434 #product low molecular weight growth promoting factor !8#status experimental #label GPF\ !$19 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$28-614,83-94, !$107-126,142-145, !$206-218,229-248, !$264-267,328-340, !$351-370 #disulfide_bonds #status predicted\ !$48 #binding_site carbohydrate (Asn) (covalent) #status !8absent\ !$169,205,294 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$379-380 #cleavage_site Met-Lys (kallikrein) #status !8experimental\ !$383 #modified_site 4-hydroxyproline (Pro) (partial) !8#status experimental\ !$389-390 #cleavage_site Arg-Ser (kallikrein) #status !8experimental\ !$401,533,542,546, !$557,571,593,628 #binding_site carbohydrate (Thr) (covalent) #status !8experimental\ !$577 #binding_site carbohydrate (Ser) (covalent) #status !8experimental SUMMARY #length 644 #molecular-weight 71945 #checksum 3755 SEQUENCE /// ENTRY KGHUL1 #type complete TITLE kininogen, LMW precursor [validated] - human ALTERNATE_NAMES alpha-2-thiol proteinase inhibitor; preprokininogen CONTAINS bradykinin (kallidin); kininogen I; kininogen II; prokininogen ORGANISM #formal_name Homo sapiens #common_name man DATE 06-Jul-1982 #sequence_revision 27-Nov-1985 #text_change 08-Dec-2000 ACCESSIONS A01280; B25276; A27900; A27699; A31905; A34030 REFERENCE A90490 !$#authors Ohkubo, I.; Kurachi, K.; Takasawa, T.; Shiokawa, H.; Sasaki, !1M. !$#journal Biochemistry (1984) 23:5691-5697 !$#title Isolation of a human cDNA for alpha-2-thiol proteinase !1inhibitor and its identity with low molecular weight !1kininogen. !$#cross-references MUID:85122621; PMID:6441591 !$#accession A01280 !'##molecule_type mRNA !'##residues 1-427 ##label OHK !'##cross-references GB:K02566; NID:g177889; PIDN:AAA35497.1; !1PID:g177890 REFERENCE A92544 !$#authors Takagaki, Y.; Kitamura, N.; Nakanishi, S. !$#journal J. Biol. Chem. (1985) 260:8601-8609 !$#title Cloning and sequence analysis of cDNAs for human high !1molecular weight and low molecular weight prekininogens. !$#cross-references MUID:85234582; PMID:2989293 !$#accession B25276 !'##molecule_type mRNA !'##residues 1-427 ##label TAK !'##cross-references GB:M11437; NID:g186751; PIDN:AAB59551.1; !1PID:g386853 REFERENCE A27900 !$#authors Lottspeich, F.; Kellermann, J.; Henschen, A.; Rauth, G.; !1Mueller-Esterl, W. !$#book Kinins IV, part A, Greenbaum, L.M., and Margolius, H.S., !1eds., pp.91-95, Plenum, New York and London, 1986 !$#title Amino acid sequence of the light chain of human low !1molecular mass kininogen. !$#accession A27900 !'##molecule_type protein !'##residues 390-427 ##label LOT REFERENCE A27699 !$#authors Mindroiu, T.; Carretero, O.A.; Proud, D.; Walz, D.; Scicli, !1A.G. !$#journal Biochem. Biophys. Res. Commun. (1988) 152:519-526 !$#title A new kinin moiety in human plasma kininogens. !$#cross-references MUID:88209021; PMID:3365237 !$#accession A27699 !'##molecule_type protein !'##residues 380-389 ##label MIN REFERENCE A31905 !$#authors Maeda, H.; Matsumura, Y.; Kato, H. !$#journal J. Biol. Chem. (1988) 263:16051-16054 !$#title Purification and identification of [hydroxyprolyl(3)] !1bradykinin in ascitic fluid from a patient with gastric !1cancer. !$#cross-references MUID:89034061; PMID:3182782 !$#accession A31905 !'##molecule_type protein !'##residues 381-389 ##label MAE REFERENCE A34030 !$#authors Sasaguri, M.; Ikeda, M.; Ideishi, M.; Arakawa, K. !$#journal Biochem. Biophys. Res. Commun. (1988) 150:511-516 !$#title Identification of [hydroxyproline(3)]-lysyl-bradykinin !1released from human plasma protein by kallikrein. !$#cross-references MUID:88106632; PMID:3337729 !$#accession A34030 !'##molecule_type protein !'##residues 380-389 ##label SAS REFERENCE A92545 !$#authors Kitamura, N.; Kitagawa, H.; Fukushima, D.; Takagaki, Y.; !1Miyata, T.; Nakanishi, S. !$#journal J. Biol. Chem. (1985) 260:8610-8617 !$#title Structural organization of the human kininogen gene and a !1model for its evolution. !$#cross-references MUID:85234583; PMID:2989294 !$#contents annotation; gene organization REFERENCE A91455 !$#authors Pierce, J.V. !$#journal Fed. Proc. (1968) 27:52-57 !$#title Structural features of plasma kinins and kininogens. !$#cross-references MUID:90255622; PMID:4952632 !$#contents annotation; bradykinin COMMENT The LMW kininogen precursor is produced from the same gene !1as the HMW form (see PIR:HGHUH1) as the result of using the !1alternative last mRNA splicing junction. COMMENT Kininogen is a cysteine proteinase inhibitor, takes part in !1initiation of the intrinsic pathway of blood coagulation, !1and binds both kallikrein and coagulation factor XI. COMMENT Bradykinin, released from kininogen by kallikrein, is a !1potent vasodilator, increases capillary permeability, !1mediates inflamation, and causes visceral smooth muscle !1contraction. The hydroxyproline residue is present in the !1kininogen prior to the release of bradykinin. GENETICS !$#gene GDB:KNG !'##cross-references GDB:125256; OMIM:228960 !$#map_position 3q27-3q27 !$#introns 65/3; 102/3; 131/1; 188/3; 224/3; 253/1; 310/3; 346/3; 375/ !13; 401/3 CLASSIFICATION #superfamily kininogen; cystatin homology KEYWORDS alternative splicing; blood coagulation; cysteine proteinase !1inhibitor; glycoprotein; hydroxyproline; plasma; !1pyroglutamic acid FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-427 #product LMW prokininogen (kininogen I) #status !8predicted #label MAT\ !$19-389,390-427 #product LMW kininogen II #status predicted #label !8MAT2\ !$19-379 #product LMW kininogen heavy chain #status predicted !8#label HCH\ !$19-131 #domain cystatin homology #label CY1\ !$142-253 #domain cystatin homology #label CY2\ !$264-375 #domain cystatin homology #label CY3\ !$380-389 #product lysyl-bradykinin (kallidin II) #status !8experimental #label KBDY\ !$381-389 #product bradykinin (kallidin I) #status experimental !8#label BDY\ !$390-427 #product LMW kininogen light chain #status !8experimental #label LCH\ !$19 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status predicted\ !$28-407,83-94, !$107-126,142-145, !$206-218,229-248, !$264-267,328-340, !$351-370 #disulfide_bonds #status predicted\ !$48,169,205,294 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$379-380 #cleavage_site Met-Lys (kallikrein) #status !8experimental\ !$383 #modified_site 4-hydroxyproline (Pro) (partial) !8#status experimental\ !$389-390 #cleavage_site Arg-Ser (kallikrein) #status !8experimental\ !$401 #binding_site carbohydrate (Thr) (covalent) #status !8absent SUMMARY #length 427 #molecular-weight 47883 #checksum 3881 SEQUENCE /// ENTRY KGBOH1 #type complete TITLE kininogen, HMW I precursor - bovine ALTERNATE_NAMES alpha-2-thiol proteinase inhibitor; preprokininogen CONTAINS bradykinin (kallidin); kininogen I; kininogen II; prokininogen ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 22-Jun-1999 ACCESSIONS A01281; A91923; A91938; A29559 REFERENCE A93317 !$#authors Kitamura, N.; Takagaki, Y.; Furuto, S.; Tanaka, T.; Nawa, !1H.; Nakanishi, S. !$#journal Nature (1983) 305:545-549 !$#title A single gene for bovine high molecular weight and low !1molecular weight kininogens. !$#cross-references MUID:84014106; PMID:6571699 !$#accession A01281 !'##molecule_type mRNA !'##residues 1-621 ##label KIT !'##cross-references GB:V01491; GB:K01757; NID:g491; PIDN:CAA24735.1; !1PID:g492 REFERENCE A91923 !$#authors Kato, H.; Nagasawa, S.; Suzuki, T. !$#journal J. Biochem. (1970) 67:313-323 !$#title Studies on the structure of bovine kininogen: cleavages of !1disulfide bonds and of methionyl bonds in kininogen-II. !$#cross-references MUID:70180420; PMID:4986212 !$#accession A91923 !'##molecule_type protein !'##residues 378-393 ##label KAT REFERENCE A91938 !$#authors Han, Y.N.; Komiya, M.; Iwanaga, S.; Suzuki, T. !$#journal J. Biochem. (1975) 77:55-68 !$#title Studies on the primary structure of bovine !1high-molecular-weight kininogen. Amino acid sequence of a !1fragment ("histidine-rich peptide") released by plasma !1kallikrein. !$#cross-references MUID:75170265; PMID:1169237 !$#accession A91938 !'##molecule_type protein !'##residues 458-498 ##label HAN REFERENCE A92627 !$#authors Sueyoshi, T.; Miyata, T.; Hashimoto, N.; Kato, H.; !1Hayashida, H.; Miyata, T.; Iwanaga, S. !$#journal J. Biol. Chem. (1987) 262:2768-2779 !$#title Bovine high molecular weight kininogen. The amino acid !1sequence, positions of carbohydrate chains and disulfide !1bridges in the heavy chain portion. !$#cross-references MUID:87137530; PMID:3546295 !$#accession A29559 !'##molecule_type protein !'##residues 'Z',20-123,'I',125-127,'I',129-378 ##label SUE REFERENCE A91153 !$#authors Lottspeich, F.; Kellermann, J.; Henschen, A.; Foertsch, B.; !1Muller-Esterl, W. !$#journal Eur. J. Biochem. (1985) 152:307-314 !$#title The amino acid sequence of the light chain of human !1high-molecular-mass kininogen. !$#cross-references MUID:86030270; PMID:4054110 !$#contents annotation; bovine cleavage sites; bovine carbohydrate !1binding sites REFERENCE A94300 !$#authors Sueyoshi, T.; Miyata, T.; Kato, H.; Iwanaga, S. !$#journal Seikagaku (1984) 56:808 !$#title Disulfide bonds in bovine HMW kininogens. !$#contents annotation; disulfide bonds !$#note article in Japanese COMMENT The HMW kininogen precursor is produced from the same gene !1as the LMW form as the result of reading through an !1alternative mRNA splicing junction. COMMENT Kininogen is a cysteine proteinase inhibitor, takes part in !1initiation of the intrinsic pathway of blood coagulation, !1and binds both kallikrein and coagulation factor XI. COMMENT The glycine/histidine/lysine-rich region of HMW kininogen !1light chain is important in mediating clotting activity. COMMENT Bradykinin, released from kininogen by kallikrein, is a !1potent vasodilator, increases capillary permeability, !1mediates inflamation, and causes visceral smooth muscle !1contraction. The hydroxyproline residue is present in the !1kininogen prior to the release of bradykinin. CLASSIFICATION #superfamily kininogen; cystatin homology KEYWORDS alternative splicing; blood coagulation; cysteine proteinase !1inhibitor; duplication; glycoprotein; hydroxyproline; !1plasma; pyroglutamic acid; tandem repeat FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-621 #product HMW prokininogen I #status predicted #label !8MAT\ !$19-379 #product HMW kininogen I heavy chain #status !8experimental #label HCH\ !$19-130 #domain cystatin homology #label CY1\ !$141-252 #domain cystatin homology #label CY2\ !$263-374 #domain cystatin homology #label CY3\ !$379-388 #product lysyl-bradykinin (kallidin II) #status !8experimental #label KBDY\ !$380-388 #product bradykinin (kallidin I) #status experimental !8#label BDY\ !$389-621 #product HMW kininogen I light chain #status !8experimental #label LCH\ !$417-488 #region glycine/histidine/lysine-rich\ !$19 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$27-591,82-93, !$106-125,141-144, !$205-217,228-247, !$263-266,327-339, !$350-369 #disulfide_bonds #status experimental\ !$87,168,169,204 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$136 #binding_site carbohydrate (Thr) (covalent) (partial) !8#status experimental\ !$197 #binding_site carbohydrate (Asn) (covalent) (partial) !8#status experimental\ !$378-379 #cleavage_site Met-Lys (kallikrein) #status !8experimental\ !$382 #modified_site 4-hydroxyproline (Pro) #status !8predicted\ !$388-389 #cleavage_site Arg-Ser (kallikrein) #status !8experimental\ !$398,406,512 #binding_site carbohydrate (Ser) (covalent) #status !8experimental\ !$399,400,520,524, !$536,548,553,570 #binding_site carbohydrate (Thr) (covalent) #status !8experimental\ !$498-499 #cleavage_site Arg-Thr (kallikrein) #status !8experimental SUMMARY #length 621 #molecular-weight 68890 #checksum 5316 SEQUENCE /// ENTRY KGBOH2 #type complete TITLE kininogen, HMW II precursor - bovine ALTERNATE_NAMES alpha-2-thiol proteinase inhibitor; preprokininogen CONTAINS bradykinin (kallidin); kininogen I; kininogen II; prokininogen ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 22-Jun-1999 ACCESSIONS A01282; A91923; A91941; A91938; B29559 REFERENCE A93317 !$#authors Kitamura, N.; Takagaki, Y.; Furuto, S.; Tanaka, T.; Nawa, !1H.; Nakanishi, S. !$#journal Nature (1983) 305:545-549 !$#title A single gene for bovine high molecular weight and low !1molecular weight kininogens. !$#cross-references MUID:84014106; PMID:6571699 !$#accession A01282 !'##molecule_type mRNA !'##residues 1-619 ##label KIT !'##cross-references GB:V01492; GB:K01758; NID:g493; PIDN:CAA24736.1; !1PID:g494 REFERENCE A91923 !$#authors Kato, H.; Nagasawa, S.; Suzuki, T. !$#journal J. Biochem. (1970) 67:313-323 !$#title Studies on the structure of bovine kininogen: cleavages of !1disulfide bonds and of methionyl bonds in kininogen-II. !$#cross-references MUID:70180420; PMID:4986212 !$#accession A91923 !'##molecule_type protein !'##residues 376-391 ##label KAT REFERENCE A91941 !$#authors Han, Y.N.; Kato, H.; Iwanaga, S.; Suzuki, T. !$#journal J. Biochem. (1976) 79:1201-1222 !$#title Primary structure of bovine plasma high-molecular-weight !1kininogen. The amino acid sequence of a glycopeptide portion !1(fragment 1) following the C-terminus of the bradykinin !1moiety. !$#cross-references MUID:76260155; PMID:956151 !$#accession A91941 !'##molecule_type protein !'##residues 387-455 ##label HAN !'##note 398-Pro, 401-Val, and 455-Lys were also found REFERENCE A91938 !$#authors Han, Y.N.; Komiya, M.; Iwanaga, S.; Suzuki, T. !$#journal J. Biochem. (1975) 77:55-68 !$#title Studies on the primary structure of bovine !1high-molecular-weight kininogen. Amino acid sequence of a !1fragment ("histidine-rich peptide") released by plasma !1kallikrein. !$#cross-references MUID:75170265; PMID:1169237 !$#accession A91938 !'##molecule_type protein !'##residues 456-496 ##label HA2 REFERENCE A92627 !$#authors Sueyoshi, T.; Miyata, T.; Hashimoto, N.; Kato, H.; !1Hayashida, H.; Miyata, T.; Iwanaga, S. !$#journal J. Biol. Chem. (1987) 262:2768-2779 !$#title Bovine high molecular weight kininogen. The amino acid !1sequence, positions of carbohydrate chains and disulfide !1bridges in the heavy chain portion. !$#cross-references MUID:87137530; PMID:3546295 !$#accession B29559 !'##molecule_type protein !'##residues 'Z',20-104,'E',106-256,'XX',257-376 ##label SUE REFERENCE A91153 !$#authors Lottspeich, F.; Kellermann, J.; Henschen, A.; Foertsch, B.; !1Muller-Esterl, W. !$#journal Eur. J. Biochem. (1985) 152:307-314 !$#title The amino acid sequence of the light chain of human !1high-molecular-mass kininogen. !$#cross-references MUID:86030270; PMID:4054110 !$#contents annotation; bovine cleavage sites; bovine carbohydrate !1binding sites REFERENCE A94300 !$#authors Sueyoshi, T.; Miyata, T.; Kato, H.; Iwanaga, S. !$#journal Seikagaku (1984) 56:808 !$#title Disulfide bonds in bovine HMW kininogens. !$#contents annotation; disulfide bonds !$#note article in Japanese COMMENT The HMW kininogen precursor is produced from the same gene !1as the LMW form as the result of reading through an !1alternative mRNA splicing junction. COMMENT Kininogen is a cysteine proteinase inhibitor, takes part in !1initiation of the intrinsic pathway of blood coagulation, !1and binds both kallikrein and coagulation factor XI. COMMENT The glycine/histidine/lysine-rich region of HMW kininogen !1light chain is important in mediating clotting activity. COMMENT Bradykinin, released from kininogen by kallikrein, is a !1potent vasodilator, increases capillary permeability, !1mediates inflamation, and causes visceral smooth muscle !1contraction. The hydroxyproline residue is present in the !1kininogen prior to the release of bradykinin. CLASSIFICATION #superfamily kininogen; cystatin homology KEYWORDS alternative splicing; blood coagulation; cysteine proteinase !1inhibitor; duplication; glycoprotein; hydroxyproline; !1plasma; pyroglutamic acid; tandem repeat FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-619 #product HMW kininogen II #status predicted #label !8MAT\ !$19-376 #product HMW kininogen II heavy chain #status !8experimental #label HCH\ !$19-130 #domain cystatin homology #label CY1\ !$141-252 #domain cystatin homology #label CY2\ !$261-372 #domain cystatin homology #label CY3\ !$377-386 #product lysyl-bradykinin (kallidin II) #status !8experimental #label KBDY\ !$378-386 #product bradykinin (kallidin I) #status experimental !8#label BDY\ !$387-619 #product HMW kininogen II light chain #status !8experimental #label LCH\ !$418-488 #region glycine/histidine/lysine-rich\ !$19 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$27-589,82-93, !$106-125,141-144, !$205-217,228-247, !$261-264,325-337, !$348-367 #disulfide_bonds #status experimental\ !$47 #binding_site carbohydrate (Asn) (covalent) #status !8absent\ !$87,168,169,204,280 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$136 #binding_site carbohydrate (Thr) (covalent) (partial) !8#status experimental\ !$197 #binding_site carbohydrate (Asn) (covalent) (partial) !8#status experimental\ !$376-377 #cleavage_site Met-Lys (kallikrein) #status !8experimental\ !$380 #modified_site 4-hydroxyproline (Pro) #status !8predicted\ !$386-387 #cleavage_site Arg-Ser (kallikrein) #status !8experimental\ !$396,400,404,510 #binding_site carbohydrate (Ser) (covalent) #status !8experimental\ !$397,398,518,522, !$534,546,551,568 #binding_site carbohydrate (Thr) (covalent) #status !8experimental\ !$496-497 #cleavage_site Arg-Thr (kallikrein) #status !8experimental SUMMARY #length 619 #molecular-weight 68710 #checksum 7111 SEQUENCE /// ENTRY KGBOL1 #type complete TITLE kininogen, LMW I precursor - bovine ALTERNATE_NAMES alpha-2-thiol proteinase inhibitor; preprokininogen CONTAINS bradykinin (kallidin); kininogen I; kininogen II; prokininogen ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 22-Jun-1999 ACCESSIONS A01283 REFERENCE A93984 !$#authors Nawa, H.; Kitamura, N.; Hirose, T.; Asai, M.; Inayama, S.; !1Nakanishi, S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:90-94 !$#title Primary structures of bovine liver low molecular weight !1kininogen precursors and their two mRNAs. !$#cross-references MUID:83117859; PMID:6572010 !$#accession A01283 !'##molecule_type mRNA !'##residues 1-436 ##label NAW !'##cross-references GB:J00010; GB:V00426; NID:g163256; PIDN:AAA30604.1; !1PID:g163257 COMMENT The LMW kininogen precursor is produced from the same gene !1as the HMW form as the result of using the alternative last !1mRNA splicing junction. COMMENT Kininogen is a cysteine proteinase inhibitor, takes part in !1initiation of the intrinsic pathway of blood coagulation, !1and binds both kallikrein and coagulation factor XI. COMMENT Bradykinin, released from kininogen by kallikrein, is a !1potent vasodilator, increases capillary permeability, !1mediates inflamation, and causes visceral smooth muscle !1contraction. The hydroxyproline residue is present in the !1kininogen prior to the release of bradykinin. CLASSIFICATION #superfamily kininogen; cystatin homology KEYWORDS alternative splicing; blood coagulation; cysteine proteinase !1inhibitor; glycoprotein; hydroxyproline; plasma; !1pyroglutamic acid FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-436 #product LMW kininogen I #status predicted #label !8MAT\ !$19-378 #product LMW kininogen I heavy chain #status !8predicted #label HCH\ !$19-130 #domain cystatin homology #label CY1\ !$141-252 #domain cystatin homology #label CY2\ !$263-374 #domain cystatin homology #label CY3\ !$379-388 #product lysyl-bradykinin (kallidin II) #status !8predicted #label KBDY\ !$380-388 #product bradykinin (kallidin I) #status predicted !8#label BDY\ !$389-436 #product LMW kininogen I light chain #status !8experimental #label LCH\ !$19 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status predicted\ !$27-406,82-93, !$106-125,141-144, !$205-217,228-247, !$263-266,327-339, !$350-369 #disulfide_bonds #status predicted\ !$47,87,168,169,197, !$204 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$378-379 #cleavage_site Met-Lys (kallikrein) #status !8predicted\ !$382 #modified_site 4-hydroxyproline (Pro) #status !8predicted\ !$388-389 #cleavage_site Arg-Ser (kallikrein) #status predicted SUMMARY #length 436 #molecular-weight 48427 #checksum 870 SEQUENCE /// ENTRY KGBOL2 #type complete TITLE kininogen, LMW II precursor - bovine ALTERNATE_NAMES alpha-2-thiol proteinase inhibitor; preprokininogen CONTAINS bradykinin (kallidin); kininogen I; kininogen II; prokininogen ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 28-May-1999 ACCESSIONS A01284 REFERENCE A93984 !$#authors Nawa, H.; Kitamura, N.; Hirose, T.; Asai, M.; Inayama, S.; !1Nakanishi, S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:90-94 !$#title Primary structures of bovine liver low molecular weight !1kininogen precursors and their two mRNAs. !$#cross-references MUID:83117859; PMID:6572010 !$#accession A01284 !'##molecule_type mRNA !'##residues 1-434 ##label NAW !'##cross-references GB:V00427; GB:J00011; NID:g489; PIDN:CAA23710.1; !1PID:g490 COMMENT The LMW kininogen precursor is produced from the same gene !1as the HMW form as the result of using the alternative last !1mRNA splicing junction. COMMENT Kininogen is a cysteine proteinase inhibitor, takes part in !1initiation of the intrinsic pathway of blood coagulation, !1and binds both kallikrein and coagulation factor XI. COMMENT Bradykinin, released from kininogen by kallikrein, is a !1potent vasodilator, increases capillary permeability, !1mediates inflamation, and causes visceral smooth muscle !1contraction. The hydroxyproline residue is present in the !1kininogen prior to the release of bradykinin. CLASSIFICATION #superfamily kininogen; cystatin homology KEYWORDS alternative splicing; blood coagulation; cysteine proteinase !1inhibitor; glycoprotein; hydroxyproline; plasma; !1pyroglutamic acid FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-434 #product LMW kininogen II #status predicted #label !8MAT\ !$19-377 #product LMW kininogen I heavy chain #status !8predicted #label HCH\ !$19-130 #domain cystatin homology #label CY1\ !$141-252 #domain cystatin homology #label CY2\ !$261-372 #domain cystatin homology #label CY3\ !$377-386 #product lysyl-bradykinin (kallidin II) #status !8predicted #label KBDY\ !$378-386 #product bradykinin (kallidin I) #status predicted !8#label BDY\ !$387-434 #product LMW kininogen I light chain #status !8experimental #label LCH\ !$19 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status predicted\ !$27-404,82-93, !$106-125,141-144, !$205-217,228-247, !$261-264,325-337, !$348-367 #disulfide_bonds #status predicted\ !$47,87,168,169,197, !$204,280 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$376-377 #cleavage_site Met-Lys (kallikrein) #status !8predicted\ !$380 #modified_site 4-hydroxyproline (Pro) #status !8predicted\ !$386-387 #cleavage_site Arg-Ser (kallikrein) #status predicted SUMMARY #length 434 #molecular-weight 48148 #checksum 4452 SEQUENCE /// ENTRY KGRTM #type fragment TITLE major acute phase alpha-1 protein precursor - rat (fragment) CONTAINS bradykinin ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 12-Apr-1996 ACCESSIONS A01285 REFERENCE A01285 !$#authors Cole, T.; Inglis, A.S.; Roxburgh, C.M.; Howlett, G.J.; !1Schreiber, G. !$#journal FEBS Lett. (1985) 182:57-61 !$#title Major acute phase alpha1-protein of the rat is homologous to !1bovine kininogen and contains the sequence for bradykinin: !1its synthesis is regulated at the mRNA level. !$#cross-references MUID:85127561; PMID:2578992 !$#accession A01285 !'##molecule_type mRNA !'##residues 1-423 ##label COL COMMENT This plasma glycoprotein inhibits cysteine proteinases. !1During acute inflammation its plasma concentration increases !1approximately 20-fold due to an increased rate of synthesis !1by the liver. CLASSIFICATION #superfamily kininogen; cystatin homology KEYWORDS bradykinin; cysteine proteinase inhibitor; duplication; !1glycoprotein; inflammation; plasma; pyroglutamic acid FEATURE !$1-11 #domain signal sequence (fragment) #status predicted !8#label SIG\ !$12-423 #product major acute phase alpha-1 protein #status !8predicted #label MAT\ !$12-123 #domain cystatin homology #label CY1\ !$134-245 #domain cystatin homology #label CY2\ !$256-367 #domain cystatin homology #label CY3\ !$371-379 #product bradykinin #status predicted #label BDY\ !$12 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status predicted\ !$161,197 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 423 #checksum 657 SEQUENCE /// ENTRY KGRTT1 #type complete TITLE T-kininogen I precursor - rat ALTERNATE_NAMES 73K protein; LMW kininogen T-I CONTAINS bradykinin; T-kinin ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 22-Jun-1999 ACCESSIONS A01286; D25486; A28526; PL0193; JQ0027; B25488; A28525; !1S68036 REFERENCE A92496 !$#authors Furuto-Kato, S.; Matsumoto, A.; Kitamura, N.; Nakanishi, S. !$#journal J. Biol. Chem. (1985) 260:12054-12059 !$#title Primary structures of the mRNAs encoding the rat precursors !1for bradykinin and T-kinin. Structural relationship of !1kininogens with major acute phase protein and !1alpha-1-cysteine proteinase inhibitor. !$#cross-references MUID:86008264; PMID:2413018 !$#accession A01286 !'##molecule_type mRNA !'##residues 1-430 ##label FUR !'##cross-references GB:M11883; NID:g205084; PIDN:AAA41489.1; !1PID:g205085 REFERENCE A92625 !$#authors Kitagawa, H.; Kitamura, N.; Hayashida, H.; Miyata, T.; !1Nakanishi, S. !$#journal J. Biol. Chem. (1987) 262:2190-2198 !$#title Differing expression patterns and evolution of the rat !1kininogen gene family. !$#cross-references MUID:87137443; PMID:3029068 !$#accession D25486 !'##molecule_type DNA !'##residues 375-430 ##label KIT REFERENCE A92729 !$#authors Enjyoji, K.; Kato, H.; Hayashi, I.; Oh-ishi, S.; Iwanaga, S. !$#journal J. Biol. Chem. (1988) 263:973-979 !$#title Purification and characterization of rat T-kininogens !1isolated from plasma of adjuvant-treated rats. !1Identification of three kinds of T-kininogens. !$#cross-references MUID:88087226; PMID:3121623 !$#accession A28526 !'##molecule_type protein !'##residues 'E',20-48;376-430 ##label ENJ REFERENCE PL0193 !$#authors Kanda, S.; Sugiyama, K.; Takahashi, M.; Shumiya, S.; Tomino, !1S.; Nagase, S. !$#journal Jpn. J. Cancer Res. (1990) 81:63-68 !$#title Identification of a protein increasing in serum of Nagase !1analbuminemic rats bearing intestinal tumors as an isotype !1of T-kininogen. !$#cross-references MUID:90216390; PMID:2108948 !$#accession PL0193 !'##molecule_type mRNA !'##residues 330-420,'R',422-429,'P' ##label KAN REFERENCE JQ0027 !$#authors Anderson, K.P.; Croyle, M.L.; Lingrel, J.B. !$#journal Gene (1989) 81:119-128 !$#title Primary structure of a gene encoding rat T-kininogen. !$#cross-references MUID:90034172; PMID:2806908 !$#accession JQ0027 !'##molecule_type DNA !'##residues 1-60,'E',62-113,'R',115-165,'F',167-178,'TKI',182-211,'F', !1213-256,'S',258-388,'Q',390-413,'G',415-429,'P' ##label AND !'##experimental_source strain Sprague-Dawley REFERENCE A25488 !$#authors Kageyama, R.; Kitamura, N.; Ohkubo, H.; Nakanishi, S. !$#journal J. Biol. Chem. (1987) 262:2345-2351 !$#title Differing utilization of homologous transcription initiation !1sites of rat K and T kininogen genes under inflammation !1condition. !$#cross-references MUID:87137465; PMID:3818598 !$#accession B25488 !'##status preliminary !'##molecule_type DNA !'##residues 1-48 ##label KAG !'##cross-references GB:M14356; NID:g205090; PIDN:AAA41492.1; !1PID:g205091 REFERENCE A28525 !$#authors Enjyoji, K.; Kato, H.; Hayashi, I.; Oh-ishi, S.; Iwanaga, S. !$#journal J. Biol. Chem. (1988) 263:965-972 !$#title Purification and characterization of two kinds of low !1molecular weight kininogens from rat (non-inflamed) plasma. !1One resistant and the second sensitive to rat glandular !1kallikreins. !$#cross-references MUID:88087225; PMID:3335530 !$#accession A28525 !'##molecule_type protein !'##residues 376-430 ##label EN2 REFERENCE S68034 !$#authors Sierra, F.; Walter, R.; Vautravers, P.; Guigoz, Y. !$#journal Arch. Biochem. Biophys. (1995) 322:333-338 !$#title Identification of several isoforms of T-kininogen expressed !1in the liver of aging rats. !$#cross-references MUID:96032652; PMID:7574705 !$#accession S68036 !'##molecule_type mRNA !'##residues 340-430 ##label SIE !'##experimental_source clone pSG17 COMMENT At least three types of LMW kininogen precursors are present !1in rat plasma, the K (LMW splice form), T-I, and T-II !1kininogens. Although homologous, their sequences differ in !1the region preceding bradykinin. COMMENT T-kininogens contain T-kinin (I-S-bradykinin), a novel kinin !1isolated after the treatment of rat plasma with high !1concentrations of trypsin. Inasmuch as T-kinin is preceded !1by a Met instead of an Arg or Lys, it is probably not !1released from its precursor by either tissue or plasma !1kallikrein. COMMENT The T-kininogens are produced in response to an inflammatory !1stimulant. GENETICS !$#introns 65/3; 102/3; 130/1; 187/3; 223/2; 252/1; 309/3; 345/3; 374/ !13; 398/3 CLASSIFICATION #superfamily kininogen; cystatin homology KEYWORDS acute phase; bradykinin; cysteine proteinase inhibitor; !1duplication; glycoprotein; inflammation; plasma; !1pyroglutamic acid FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-430 #product T-kininogen I #status experimental #label !8MAT\ !$19-130 #domain cystatin homology #label CY1\ !$141-252 #domain cystatin homology #label CY2\ !$263-374 #domain cystatin homology #label CY3\ !$378-386 #product bradykinin #status predicted #label BDY\ !$19 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$82,126,168,204,326 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$83-94,107-125, !$141-144,205-217, !$228-247,263-266, !$327-339,350-369 #disulfide_bonds #status predicted SUMMARY #length 430 #molecular-weight 47704 #checksum 6101 SEQUENCE /// ENTRY KGHUGH #type complete TITLE histidine-rich glycoprotein precursor - human ALTERNATE_NAMES HRG ORGANISM #formal_name Homo sapiens #common_name man DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 16-Jun-2000 ACCESSIONS A01287; S29669 REFERENCE A01287 !$#authors Koide, T.; Foster, D.; Yoshitake, S.; Davie, E.W. !$#journal Biochemistry (1986) 25:2220-2225 !$#title Amino acid sequence of human histidine-rich glycoprotein !1derived from the nucleotide sequence of its cDNA. !$#cross-references MUID:86216149; PMID:3011081 !$#accession A01287 !'##molecule_type mRNA !'##residues 1-525 ##label KOI !'##cross-references GB:AB005803; NID:g2280513; PIDN:BAA21613.1; !1PID:g2280514 REFERENCE S29669 !$#authors Hennis, B.; Havelaar, A.; Kluft, C. !$#submission submitted to the EMBL Data Library, October 1991 !$#description PCR detection of a dinucleotide repeat in the human !1histidine-rich glycoprotein (HRG) gene. !$#accession S29669 !'##status preliminary !'##molecule_type DNA !'##residues 214-247 ##label HEN !'##cross-references EMBL:Z17218; NID:g32453; PIDN:CAA78925.1; !1PID:g32454 COMMENT Although its physiological function is not yet known, HRG !1does bind heme, dyes, and divalent metal ions. It can !1inhibit rosette formation and is known to interact with !1heparin, thrombospondin, and the lysine-binding site of !1plasminogen. On the basis of its homology with HMW !1kininogen, the histidine-rich region of this protein may !1mediate the contact activation phase of the intrinsic blood !1coagulation cascade. COMMENT The amino half of this protein is homologous to the first !1two cystatin-like domains of kininogen, but the sequence of !1the reactive site in both domains has changed to the extent !1that HGR would not have inhibitory activity. COMMENT In addition to having a high histidine and proline content, !1this protein has many internal repeats. Twelve tandem !1repetitions of a five-residue sequence (GHHPH, consensus) !1form a 'histidine-rich' region. GENETICS !$#gene GDB:HRG !'##cross-references GDB:120055; OMIM:142640 !$#map_position 3q27-3q27 CLASSIFICATION #superfamily histidine-rich glycoprotein; cystatin homology KEYWORDS duplication; glycoprotein; heparin binding; tandem repeat FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-525 #product histidine-rich glycoprotein #status !8predicted #label MAT\ !$19-131 #domain cystatin homology #label CY1\ !$140-246 #domain cystatin homology #label CY2\ !$276-321 #region proline-rich\ !$348-437 #region histidine-rich\ !$351-497 #region proline-rich\ !$63,125,344,345 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$78-89,105-126, !$218-241 #disulfide_bonds #status predicted SUMMARY #length 525 #molecular-weight 59578 #checksum 9896 SEQUENCE /// ENTRY WOHU #type complete TITLE alpha-2-HS-glycoprotein precursor [validated] - human ALTERNATE_NAMES bone resorptive protein BRP-2 CONTAINS alpha-2-HS-glycoprotein chain A; alpha-2-HS-glycoprotein chain B ORGANISM #formal_name Homo sapiens #common_name man DATE 03-Aug-1984 #sequence_revision 28-Dec-1987 #text_change 08-Dec-2000 ACCESSIONS A29081; A26296; A03228; A60795; A44779; S04467; S02765; !1S51074; S55686 REFERENCE A94162 !$#authors Lee, C.C.; Bowman, B.H.; Yang, F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:4403-4407 !$#title Human alpha-2-HS-glycoprotein: the A and B chains with a !1connecting sequence are encoded by a single mRNA transcript. !$#cross-references MUID:87260816; PMID:3474608 !$#accession A29081 !'##molecule_type mRNA !'##residues 1-367 ##label LEE !'##cross-references GB:M16961; NID:g178283; PIDN:AAA51683.1; !1PID:g178284 REFERENCE A92567 !$#authors Yoshioka, Y.; Gejyo, F.; Marti, T.; Rickli, E.E.; Burgi, W.; !1Offner, G.D.; Troxler, R.F.; Schmid, K. !$#journal J. Biol. Chem. (1986) 261:1665-1676 !$#title The complete amino acid sequence of the A-chain of human !1plasma alpha-2-HS-glycoprotein. !$#cross-references MUID:86111834; PMID:3944104 !$#accession A26296 !'##molecule_type protein !'##residues 19-53,'K',55-300 ##label YOS REFERENCE A92422 !$#authors Gejyo, F.; Chang, J.L.; Burgi, W.; Schmid, K.; Offner, G.D.; !1Troxler, R.F.; Van Halbeek, H.; Dorland, L.; Gerwig, G.J.; !1Vliegenthart, F.G. !$#journal J. Biol. Chem. (1983) 258:4966-4971 !$#title Characterization of the B-chain of human plasma !1alpha-2HS-glycoprotein. The complete amino acid sequence and !1primary structure of its heteroglycan. !$#cross-references MUID:83161108; PMID:6833285 !$#accession A03228 !'##molecule_type protein !'##residues 341-367 ##label GEJ REFERENCE A60795 !$#authors Lamkin, M.S.; Colclasure, C.; Rodrick, M.; Troxler, R.F.; !1Offner, G.D.; Lloyd, W.S.; Schmid, K.; Nimberg, R.B. !$#journal Calcif. Tissue Int. (1987) 41:171-175 !$#title Three forms of BRP-2 (bone resorptive proteins) from human !1cancer ascites fluid and their relationship to human serum !1alpha-2 HS-glycoprotein. !$#cross-references MUID:88026479; PMID:3117344 !$#accession A60795 !'##molecule_type protein !'##residues 19-28;341-350 ##label LAM REFERENCE A44779 !$#authors Kellermann, J.; Haupt, H.; Auerswald, E.A.; Mueller-Esterl, !1W. !$#journal J. Biol. Chem. (1989) 264:14121-14128 !$#title The arrangement of disulfide loops in human alpha-2-HS !1glycoprotein. Similarity to the disulfide bridge structures !1of cystatins and kininogens. !$#cross-references MUID:89340518; PMID:2760061 !$#accession A44779 !'##molecule_type protein !'##residues 19-103;107-120;125-143;145-339;341-361;364-367 ##label KEL REFERENCE S02765 !$#authors Araki, T.; Yoshioka, Y.; Schmid, K. !$#journal Biochim. Biophys. Acta (1989) 994:195-199 !$#title The position of the disulfide bonds in human plasma alpha(2) !1HS-glycoprotein and the repeating double disulfide bonds in !1the domain structure. !$#cross-references MUID:89150282; PMID:2645941 !$#accession S04467 !'##molecule_type protein !'##residues 19-53,'K',55-300 ##label ARA !$#accession S02765 !'##molecule_type protein !'##residues 341-367 ##label AR2 REFERENCE S51074 !$#authors Jahnen-Dechent, W.; Trindl, A.; Godovac-Zimmermann, J.; !1Mueller-Esterl, W. !$#journal Eur. J. Biochem. (1994) 226:59-69 !$#title Posttranslational processing of human alpha(2)-HS !1glycoprotein (human fetuin). Evidence for the production of !1a phosphorylated single-chain form by hepatoma cells. !$#cross-references MUID:95045601; PMID:7525288 !$#accession S51074 !'##molecule_type protein !'##residues 19-23,25-28 ##label JAH REFERENCE S55686 !$#authors To, W.Y.; Leung, J.C.K.; Lai, K.N. !$#journal Biochim. Biophys. Acta (1995) 1249:58-64 !$#title Identification and characterization of human serum alpha2-HS !1glycoprotein as a jacalin-bound protein. !$#cross-references MUID:95284111; PMID:7766684 !$#accession S55686 !'##molecule_type protein !'##residues 19-20,'LP',23-29,'S',31 ##label TOW COMMENT The purified protein stimulates calcium release from bone in !1studies in vitro. COMMENT Alpha-2-HS shows affinity for calcium and barium ions. It is !1found in the matrix of bone and dentin in much larger !1quantities than other plasma proteins. GENETICS !$#gene GDB:AHSG !'##cross-references GDB:118985; OMIM:138680 !$#map_position 3q27-3q27 CLASSIFICATION #superfamily alpha-2-HS-glycoprotein; cystatin homology KEYWORDS acute-phase negative reactant; duplication; glycoprotein; !1liver; plasma FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-300 #product alpha-2-HS-glycoprotein chain A #status !8experimental #label ACH\ !$23-137 #domain cystatin homology #label CY1\ !$146-252 #domain cystatin homology #label CY2\ !$254-300 #region collagen-like\ !$341-367 #product alpha-2-HS-glycoprotein chain B #status !8experimental #label BCH\ !$32-358,89-100, !$114-132,146-149, !$208-219,230-247 #disulfide_bonds #status experimental\ !$156,176 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$256,270 #binding_site carbohydrate (Thr) (covalent) #status !8experimental\ !$346 #binding_site carbohydrate (Ser) (covalent) #status !8experimental SUMMARY #length 367 #molecular-weight 39324 #checksum 8182 SEQUENCE /// ENTRY C1HUQA #type complete TITLE complement subcomponent C1q chain A precursor [validated] - human ALTERNATE_NAMES complement subcomponent C1q alpha chain ORGANISM #formal_name Homo sapiens #common_name man DATE 24-Apr-1984 #sequence_revision 31-May-1996 #text_change 08-Dec-2000 ACCESSIONS S14350; A90304; A90315; A03205 REFERENCE S14350 !$#authors Sellar, G.C.; Blake, D.J.; Reid, K.B.M. !$#journal Biochem. J. (1991) 274:481-490 !$#title Characterization and organization of the genes encoding the !1A-, B- and C-chains of human complement subcomponent C1q. !1The complete derived amino acid sequence of human C1q. !$#cross-references MUID:91174759; PMID:1706597 !$#accession S14350 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-245 ##label SEL REFERENCE A90304 !$#authors Reid, K.B.M. !$#journal Biochem. J. (1979) 179:367-371 !$#title Complete amino acid sequences of the three collagen-like !1regions present in subcomponent C1q of the first component !1of human complement. !$#cross-references MUID:80020137; PMID:486087 !$#accession A90304 !'##molecule_type protein !'##residues 23-96,'K',98-102,'P',104-130 ##label REI REFERENCE A90315 !$#authors Reid, K.B.M.; Gagnon, J.; Frampton, J. !$#journal Biochem. J. (1982) 203:559-569 !$#title Completion of the amino acid sequences of the A and B chains !1of subcomponent C1q of the first component of human !1complement. !$#cross-references MUID:82283890; PMID:6981411 !$#accession A90315 !'##molecule_type protein !'##residues 131-171,'N',173-177,'W',179-239,'ILPGFSA' ##label RE2 COMMENT The first component of complement is a calcium-dependent !1complex of the three subcomponents C1q, C1r, and C1s. !1Subcomponent C1q binds to immunoglobulin complexes, with !1resulting serial activation of C1r (enzyme), C1s !1(proenzyme), and the other eight components of complement. COMMENT The C1q subcomponent is composed of nine subunits, six of !1which are disulfide-linked dimers of the A and B (see !1PIR:C1HUQB) chains, and three of which are disulfide-linked !1dimers of the C (see PIR:C1HUQC) chain. Equimolar amounts of !1the A, B, and C chains are found after reduction of the !1disulfide bonds. GENETICS !$#gene GDB:C1QA !'##cross-references GDB:119042; OMIM:120550 !$#map_position 1p36.3-1p34.1 !$#introns 55/1 CLASSIFICATION #superfamily complement subcomponent C1q chain A; complement !1C1q carboxyl-terminal homology KEYWORDS complement pathway; glycoprotein; heterodimer; !1hydroxylysine; hydroxyproline; plasma; triple helix FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-245 #product complement subcomponent C1q chain A #status !8experimental #label MAT\ !$31-109 #domain collagenous, triple helix #status predicted !8#label COL\ !$116-243 #domain complement C1q carboxyl-terminal homology !8#label C1Q\ !$26 #disulfide_bonds interchain (to chain B-31) #status !8experimental\ !$33,48,67,100,103 #modified_site 5-hydroxylysine (Lys) #status !8experimental\ !$33,48,67,100,103 #binding_site carbohydrate (Lys) (covalent) #status !8experimental\ !$39,45,54,57,73,85, !$97 #modified_site 4-hydroxyproline (Pro) #status !8experimental\ !$146 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 245 #molecular-weight 26016 #checksum 8846 SEQUENCE /// ENTRY C1HUQB #type complete TITLE complement subcomponent C1q chain B precursor [validated] - human ALTERNATE_NAMES complement subcomponent C1q beta chain ORGANISM #formal_name Homo sapiens #common_name man DATE 22-May-1981 #sequence_revision 31-May-1996 #text_change 08-Dec-2000 ACCESSIONS B23422; A23422; B90304; A90301; B90315; A03206 REFERENCE A23422 !$#authors Reid, K.B.M. !$#journal Biochem. J. (1985) 231:729-735 !$#title Molecular cloning and characterization of the complementary !1DNA and gene coding for the B-chain of subcomponent C1q of !1the human complement system. !$#cross-references MUID:86076906; PMID:3000358 !$#accession B23422 !'##molecule_type DNA !'##residues 'HS',1-32 ##label REI !'##note the authors translated the codon AGT for the second position as !1Arg; they were uncertain about the location of the !1initiation codon !$#accession A23422 !'##molecule_type mRNA !'##residues 28-253 ##label RE1 !'##cross-references EMBL:X03084 !'##note the authors translated the codon ACA for residue 46 as Ile REFERENCE A90304 !$#authors Reid, K.B.M. !$#journal Biochem. J. (1979) 179:367-371 !$#title Complete amino acid sequences of the three collagen-like !1regions present in subcomponent C1q of the first component !1of human complement. !$#cross-references MUID:80020137; PMID:486087 !$#accession B90304 !'##molecule_type protein !'##residues 'E',29-84,'D',86-99,'P',101-135 ##label RE5 REFERENCE A90301 !$#authors Reid, K.B.M.; Thompson, E.O.P. !$#journal Biochem. J. (1978) 173:863-868 !$#title Amino acid sequence of the N-terminal 108 amino acid !1residues of the B chain of subcomponent C1q of the first !1component of human complement. !$#cross-references MUID:79041552; PMID:708376 !$#accession A90301 !'##molecule_type protein !'##residues 28-99,'P',101-195 ##label RE3 REFERENCE A90315 !$#authors Reid, K.B.M.; Gagnon, J.; Frampton, J. !$#journal Biochem. J. (1982) 203:559-569 !$#title Completion of the amino acid sequences of the A and B chains !1of subcomponent C1q of the first component of human !1complement. !$#cross-references MUID:82283890; PMID:6981411 !$#accession B90315 !'##molecule_type protein !'##residues 136-253 ##label RE4 !'##note 176-Glx may also be present COMMENT The first component of complement is a calcium-dependent !1complex of the three subcomponents C1q, C1r, and C1s. !1Subcomponent C1q binds to immunoglobulin complexes, with !1resulting serial activation of C1r (enzyme), C1s !1(proenzyme), and the other eight components of complement. COMMENT The C1q subcomponent is composed of nine subunits, six of !1which are disulfide-linked dimers of the A (see PIR:C1HUQA) !1and B chains, and three of which are disulfide-linked dimers !1of the C (see PIR:C1HUQC) chain. Equimolar amounts of the A, !1B, and C chains are found after reduction of the disulfide !1bonds. GENETICS !$#gene GDB:C1QB !'##cross-references GDB:119043; OMIM:120570 !$#map_position 1p36.3-1p34.1 CLASSIFICATION #superfamily complement subcomponent C1q chain A; complement !1C1q carboxyl-terminal homology KEYWORDS complement pathway; glycoprotein; heterodimer; !1hydroxylysine; hydroxyproline; plasma; pyroglutamic acid; !1triple helix FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-253 #product complement subcomponent C1q chain B #status !8experimental #label MAT\ !$33-116 #domain collagenous, triple helix #label COL\ !$123-249 #domain complement C1q carboxyl-terminal homology !8#label C1Q\ !$28 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$31 #disulfide_bonds interchain (to chain A-26) #status !8experimental\ !$35,38,41,53,56,65, !$83,86,101,104,107 #modified_site 4-hydroxyproline (Pro) #status !8experimental\ !$59,62,77,92,98,110 #modified_site 5-hydroxylysine (Lys) #status !8experimental\ !$59,62,98,110 #binding_site carbohydrate (Lys) (covalent) #status !8experimental SUMMARY #length 253 #molecular-weight 26722 #checksum 7399 SEQUENCE /// ENTRY C1HUQC #type complete TITLE complement subcomponent C1q chain C precursor - human ALTERNATE_NAMES complement subcomponent C1q gamma chain ORGANISM #formal_name Homo sapiens #common_name man DATE 22-May-1981 #sequence_revision 31-May-1996 #text_change 22-May-1998 ACCESSIONS S14351; A03207 REFERENCE S14350 !$#authors Sellar, G.C.; Blake, D.J.; Reid, K.B.M. !$#journal Biochem. J. (1991) 274:481-490 !$#title Characterization and organization of the genes encoding the !1A-, B- and C-chains of human complement subcomponent C1q. !1The complete derived amino acid sequence of human C1q. !$#cross-references MUID:91174759; PMID:1706597 !$#accession S14351 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-245 ##label SEL REFERENCE A90304 !$#authors Reid, K.B.M. !$#journal Biochem. J. (1979) 179:367-371 !$#title Complete amino acid sequences of the three collagen-like !1regions present in subcomponent C1q of the first component !1of human complement. !$#cross-references MUID:80020137; PMID:486087 !$#accession A03207 !'##molecule_type protein !'##residues 29-56,'P',58-65,'K',67-71,'P',73-83,'K',85-86,'D',88-89, !1'N',91-122 ##label REI COMMENT The first component of complement is a calcium-dependent !1complex of the three subcomponents C1q, C1r, and C1s. !1Subcomponent C1q binds to immunoglobulin complexes, with !1resulting serial activation of C1r (enzyme), C1s !1(proenzyme), and the other eight components of complement. COMMENT The C1q subcomponent is composed of nine subunits, six of !1which are disulfide-linked dimers of the A (see PIR:C1HUQA) !1and B (see PIR:C1HUQB) chains, and three of which are !1disulfide-linked dimers of the C chain. Equimolar amounts of !1the A, B, and C chains are found after reduction of the !1disulfide bonds. GENETICS !$#gene GDB:C1QG !'##cross-references GDB:128132; OMIM:120575 !$#map_position 1p36.3-1p34.1 !$#introns 60/3 CLASSIFICATION #superfamily complement subcomponent C1q chain A; complement !1C1q carboxyl-terminal homology KEYWORDS complement pathway; glycoprotein; homodimer; hydroxylysine; !1hydroxyproline; plasma; triple helix FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-245 #product complement subcomponent C1q chain B #status !8predicted #label MAT\ !$31-114 #domain collagenous, triple helix #label COL\ !$121-244 #domain complement C1q carboxyl-terminal homology !8#label C1Q\ !$32 #disulfide_bonds interchain #status experimental\ !$36,39,42,45,54,63, !$81,93,96,99,105 #modified_site 4-hydroxyproline (Pro) #status !8experimental\ !$57,72,75 #modified_site 5-hydroxylysine (Lys) #status !8experimental\ !$75 #binding_site carbohydrate (Lys) (covalent) #status !8experimental SUMMARY #length 245 #molecular-weight 25748 #checksum 9528 SEQUENCE /// ENTRY TSHUP1 #type complete TITLE thrombospondin 1 precursor - human ORGANISM #formal_name Homo sapiens #common_name man DATE 23-Aug-1987 #sequence_revision 03-Aug-1995 #text_change 17-Nov-2000 ACCESSIONS A26155; A34274; A30140; A25812; A05172; A42927 REFERENCE A26155 !$#authors Lawler, J.; Hynes, R.O. !$#journal J. Cell Biol. (1986) 103:1635-1648 !$#title The structure of human thrombospondin, an adhesive !1glycoprotein with multiple calcium-binding sites and !1homologies with several different proteins. !$#cross-references MUID:87057617; PMID:2430973 !$#accession A26155 !'##molecule_type mRNA !'##residues 1-1170 ##label LAW !'##cross-references GB:X04665; NID:g37137; PIDN:CAA28370.1; PID:g37138 !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing REFERENCE A34274 !$#authors Laherty, C.D.; Gierman, T.M.; Dixit, V.M. !$#journal J. Biol. Chem. (1989) 264:11222-11227 !$#title Characterization of the promoter region of the human !1thrombospondin gene. DNA sequences within the first intron !1increase transcription. !$#cross-references MUID:89291870; PMID:2544587 !$#accession A34274 !'##molecule_type DNA !'##residues 1-166 ##label LAH !'##cross-references GB:J04835 REFERENCE A30140 !$#authors Hennessy, S.W.; Frazier, B.A.; Kim, D.D.; Deckwerth, T.L.; !1Baumgartel, D.M.; Rotwein, P.; Frazier, W.A. !$#journal J. Cell Biol. (1989) 108:729-736 !$#title Complete thrombospondin mRNA sequence includes potential !1regulatory sites in the 3' untranslated region. !$#cross-references MUID:89139590; PMID:2918029 !$#accession A30140 !'##molecule_type mRNA !'##residues 1-83,'A',85-522,'A',524-1170 ##label HEN !'##cross-references EMBL:X14787; NID:g37464; PIDN:CAA32889.1; !1PID:g37465 !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing REFERENCE A25812 !$#authors Kobayashi, S.; Eden-McCutchan, F.; Framson, P.; Bornstein, !1P. !$#journal Biochemistry (1986) 25:8418-8425 !$#title Partial amino acid sequence of human thrombospondin as !1determined by analysis of cDNA clones: homology to malarial !1circumsporozoite proteins. !$#cross-references MUID:87157592; PMID:3030396 !$#accession A25812 !'##molecule_type mRNA !'##residues 1-83,'A',85-397 ##label KOB !'##cross-references GB:M25631; NID:g538353; PIDN:AAA36741.1; !1PID:g538354 REFERENCE A05172 !$#authors Dixit, V.M.; Hennessy, S.W.; Grant, G.A.; Rotwein, P.; !1Frazier, W.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:5449-5453 !$#cross-references MUID:86287276; PMID:3461443 !$#accession A05172 !'##molecule_type mRNA !'##residues 1-83,'A',85-374,'RC' ##label DIX !'##cross-references GB:M14326; NID:g340005; PIDN:AAA61237.1; !1PID:g553801 !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing REFERENCE A42927 !$#authors Sun, X.; Skorstengaard, K.; Mosher, D.F. !$#journal J. Cell Biol. (1992) 118:693-701 !$#title Disulfides modulate RGD-inhibitable cell adhesive activity !1of thrombospondin. !$#cross-references MUID:92348511; PMID:1379247 !$#accession A42927 !'##molecule_type protein !'##residues 987-1003 ##label SUN !'##note Cys-992 is shown to have a free sulfhydryl GENETICS !$#gene GDB:THBS1; TSP1; TSP !'##cross-references GDB:120438; OMIM:188060 !$#map_position 15q15-15q15 !$#introns 23/1 !$#note the list of introns may be incomplete COMPLEX homotrimer, disulfide linked FUNCTION !$#description participates in cell migration and adhesion, and in platelet !1aggregation CLASSIFICATION #superfamily thrombospondin 1; EGF homology; thrombospondin !1type 1 repeat homology; von Willebrand factor type C repeat !1homology KEYWORDS beta-hydroxyasparagine; calcium binding; cell adhesion; !1glycoprotein; trimer FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-1170 #product thrombospondin 1 #status predicted #label !8MAT\ !$317-375 #domain von Willebrand factor type C repeat homology !8#label VWC\ !$378-429 #domain thrombospondin type 1 repeat homology #label !8THR1\ !$434-490 #domain thrombospondin type 1 repeat homology #label !8THR2\ !$491-547 #domain thrombospondin type 1 repeat homology #label !8THR3\ !$551-586 #domain EGF homology #label EGF1\ !$650-689 #domain EGF homology #label EGF2\ !$926-928 #region cell attachment (R-G-D) motif\ !$171-232 #disulfide_bonds #status predicted\ !$248,360,708,1067 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$270,274 #disulfide_bonds interchain #status predicted\ !$610 #modified_site erythro-beta-hydroxyasparagine (Asn) !8#status predicted\ !$1051 #binding_site carbohydrate (Asn) (covalent) #status !8absent SUMMARY #length 1170 #molecular-weight 129412 #checksum 6656 SEQUENCE /// ENTRY TSHUP2 #type complete TITLE thrombospondin 2 precursor - human ORGANISM #formal_name Homo sapiens #common_name man DATE 19-May-1995 #sequence_revision 03-Aug-1995 #text_change 13-Aug-1999 ACCESSIONS A47379; A42173 REFERENCE A47379 !$#authors LaBell, T.L.; Byers, P.H. !$#journal Genomics (1993) 17:225-229 !$#title Sequence and characterization of the complete human !1thrombospondin 2 cDNA: potential regulatory role for the 3' !1untranslated region. !$#cross-references MUID:94010892; PMID:8406456 !$#accession A47379 !'##molecule_type mRNA !'##residues 1-1172 ##label LAB !'##cross-references GB:L12350; NID:g307505; PIDN:AAA03703.1; !1PID:g307506 REFERENCE A42173 !$#authors LaBell, T.L.; Milewicz, D.J.; Disteche, C.M.; Byers, P.H. !$#journal Genomics (1992) 12:421-429 !$#title Thrombospondin II: partial cDNA sequence, chromosome !1location, and expression of a second member of the !1thrombospondin gene family in humans. !$#cross-references MUID:92217961; PMID:1559694 !$#accession A42173 !'##molecule_type mRNA !'##residues 560-1172 ##label LA2 !'##cross-references GB:M81339 !'##experimental_source fibroblast !'##note sequence extracted from NCBI backbone (NCBIN:95091, !1NCBIP:95096) GENETICS !$#gene GDB:THBS2; TSP2 !'##cross-references GDB:128789; OMIM:188061 !$#map_position 6q27-6q27 COMPLEX homotrimer, disulfide linked FUNCTION !$#description participates in cell migration and adhesion, and in platelet !1aggregation CLASSIFICATION #superfamily thrombospondin 1; EGF homology; thrombospondin !1type 1 repeat homology; von Willebrand factor type C repeat !1homology KEYWORDS beta-hydroxyasparagine; calcium binding; cell adhesion; !1glycoprotein; trimer FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-1172 #product thrombospondin 2 #status predicted #label !8MAT\ !$319-377 #domain von Willebrand factor type C repeat homology !8#label VWC\ !$380-431 #domain thrombospondin type 1 repeat homology #label !8THR1\ !$436-492 #domain thrombospondin type 1 repeat homology #label !8THR2\ !$493-549 #domain thrombospondin type 1 repeat homology #label !8THR3\ !$553-588 #domain EGF homology #label EGF1\ !$652-691 #domain EGF homology #label EGF\ !$928-930 #region cell attachment (R-G-D) motif\ !$151,316,330,457, !$584,710,1069 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$167-226 #disulfide_bonds #status predicted\ !$266,270 #disulfide_bonds interchain #status predicted\ !$612 #modified_site erythro-beta-hydroxyasparagine (Asn) !8#status predicted SUMMARY #length 1172 #molecular-weight 129954 #checksum 9989 SEQUENCE /// ENTRY A39804 #type complete TITLE thrombospondin precursor - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A39804 REFERENCE A39804 !$#authors Lawler, J.; Duquette, M.; Ferro, P. !$#journal J. Biol. Chem. (1991) 266:8039-8043 !$#title Cloning and sequencing of chicken thrombospondin. !$#cross-references MUID:91217026; PMID:2022631 !$#accession A39804 !'##status preliminary !'##molecule_type mRNA !'##residues 1-1178 ##label LAW !'##cross-references GB:M60853; NID:g212763; PIDN:AAA51437.1; !1PID:g212764 CLASSIFICATION #superfamily thrombospondin 1; EGF homology; thrombospondin !1type 1 repeat homology; von Willebrand factor type C repeat !1homology FEATURE !$325-383 #domain von Willebrand factor type C repeat homology !8#label VWC\ !$386-437 #domain thrombospondin type 1 repeat homology #label !8THR1\ !$442-498 #domain thrombospondin type 1 repeat homology #label !8THR2\ !$499-555 #domain thrombospondin type 1 repeat homology #label !8THR3\ !$658-697 #domain EGF homology #label EGF SUMMARY #length 1178 #molecular-weight 131816 #checksum 3042 SEQUENCE /// ENTRY S29126 #type complete TITLE properdin precursor [validated] - human ALTERNATE_NAMES factor P ORGANISM #formal_name Homo sapiens #common_name man DATE 17-Nov-2000 #sequence_revision 17-Nov-2000 #text_change 17-Nov-2000 ACCESSIONS S29126; S16150; A05319; T45112; T45113 REFERENCE S29126 !$#authors Nolan, K.F.; Kaluz, S.; Higgins, J.M.G.; Goundis, D.; Reid, !1K.B.M. !$#journal Biochem. J. (1992) 287:291-297 !$#title Characterization of the human properdin gene. !$#cross-references MUID:93038568; PMID:1417780 !$#accession S29126 !'##molecule_type DNA !'##residues 1-469 ##label NOL1 !'##cross-references EMBL:X70872; NID:g35679; PIDN:CAA50220.1; !1PID:g35680 REFERENCE S16150 !$#authors Nolan, K.F.; Schwaeble, W.; Kaluz, S.; Dierich, M.P.; Reid, !1K.B.M. !$#journal Eur. J. Immunol. (1991) 21:771-776 !$#title Molecular cloning of the cDNA coding for properdin, a !1positive regulator of the alternative pathway of human !1complement. !$#cross-references MUID:91184288; PMID:2009915 !$#accession S16150 !'##molecule_type mRNA !'##residues 1-456,'R',458-469 ##label NOL2 !'##cross-references EMBL:X57748 REFERENCE A05319 !$#authors Reid, K.B.M.; Gagnon, J. !$#journal Mol. Immunol. (1981) 18:949-959 !$#cross-references MUID:82195224; PMID:7341961 !$#accession A05319 !'##molecule_type protein !'##residues 28-53,'Q',55-59,'G',61,'I',63;137-138,'P',140-141,'P', !1143-144,'X',146-148,'Y',150,'S',152,'Y',154-156, !1'XSXGXA';162-163,'E',165-172,'X',174-176,'X',178,'V', !1180;223-228,'X',230-232,'GX',235-238,'GH',241-245;248-251, !1'X',253-257,'P',259,'G',261,'XPP',265-266,'X', !1268-269;280-285,'X',287-290,'X',292,'H',294-300,'SXXX', !1305-307,'X',309-315,'K',317;333-341,343-357,'X',359-362, !1'EXE';393-404,'QK',407;421-427,'R',429-443,'TKV',447-448, !1'XX',451,'RX',454-455 ##label REI REFERENCE Z22914 !$#authors Westberg, J.; Nordin-Fredrikson, G.; Truedsson, L.; Sjoholm, !1A.G.; Uhlen, M. !$#submission submitted to the EMBL Data Library, May 1997 !$#accession T45112 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-54,'X',56-73,'X',75-99,'W',101-469 ##label WES1 !'##cross-references EMBL:AF005665; PIDN:AAB63280.1 !'##experimental_source genomic DNA from individual with properdin !1deficiency type II !$#accession T45113 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-60,'X',62-413,'D',415-452,'XX',455-469 ##label WE2 !'##cross-references EMBL:AF005666; PIDN:AAC51626.1 !'##experimental_source genomic DNA from individual with properdin !1deficiency type III REFERENCE A59360 !$#authors Hartmann, S.; Hofsteenge, J. !$#journal J. Biol. Chem. (2000) 275:28569-28574 !$#title Properdin, the positive regulator of complement, is highly !1C-mannosylated. !$#cross-references MUID:20435812; PMID:10878002 !$#contents annotation !$#note identification and location of C-mannosylation sites by !1mass-spectroscopy GENETICS !$#gene GDB:PFC !'##cross-references GDB:120275; OMIM:312060 !$#map_position Xp11.3-Xp11.23 !$#introns 26/1; 76/2; 135/1; 192/1; 256/1; 314/1; 378/1; 415/2 COMPLEX a mixture of homodimers, homotrimers and homotetramers FUNCTION !$#description protects C3 convertase (C3bBb) from rapid inactivation !$#pathway complement alternate pathway CLASSIFICATION #superfamily human properdin precursor; thrombospondin type !11 repeat homology KEYWORDS complement alternate pathway; glycoprotein; homodimer; !1homotetramer; homotrimer; plasma FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-469 #product properdin #status experimental #label MAT\ !$76-128 #domain thrombospondin type 1 repeat homology #label !8THR1\ !$135-191 #domain thrombospondin type 1 repeat homology #label !8THR2\ !$192-255 #domain thrombospondin type 1 repeat homology #label !8THR3\ !$256-313 #domain thrombospondin type 1 repeat homology #label !8THR4\ !$314-377 #domain thrombospondin type 1 repeat homology #label !8THR5\ !$378-440 #domain thrombospondin type 1 repeat homology #label !8THR6\ !$83,86,139,142,145, !$196,199,260,263, !$321,324,382,385,388 #modified_site 2'-mannosyl-tryptophan (Trp) #status !8experimental\ !$428 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 469 #molecular-weight 51276 #checksum 8782 SEQUENCE /// ENTRY A46016 #type complete TITLE thrombospondin 3 - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jan-2000 ACCESSIONS A46016; A44124; I55398; S68788; S72433 REFERENCE A46016 !$#authors Bornstein, P.; Devarayalu, S.; Edelhoff, S.; Disteche, C.M. !$#journal Genomics (1993) 15:607-613 !$#title Isolation and characterization of the mouse thrombospondin 3 !1(Thbs3) gene. !$#cross-references MUID:93224149; PMID:8468055 !$#accession A46016 !'##status preliminary !'##molecule_type mRNA !'##residues 1-956 ##label BOR !'##cross-references GB:L04302; NID:g202200; PIDN:AAA40497.1; !1PID:g202201 !'##note sequence extracted from NCBI backbone (NCBIN:129415, !1NCBIP:129416) REFERENCE A44124 !$#authors Vos, H.L.; Devarayalu, S.; de Vries, Y.; Bornstein, P. !$#journal J. Biol. Chem. (1992) 267:12192-12196 !$#title Thrombospondin 3 (Thbs3), a new member of the thrombospondin !1gene family. !$#cross-references MUID:92291102; PMID:1601886 !$#accession A44124 !'##status preliminary !'##molecule_type DNA !'##residues 517-956 ##label VOS !'##cross-references GB:M86620; NID:g201987; PIDN:AAA40430.1; !1PID:g201989 !'##experimental_source BALB/c !'##note sequence extracted from NCBI backbone (NCBIN:106634, !1NCBIN:106636, NCBIN:106639, NCBIN:106642, NCBIN:106644, !1NCBIN:106646, NCBIN:106648, NCBIN:106650, NCBIN:106652, !1NCBIN:106654, NCBIP:106655) REFERENCE I55398 !$#authors Qabar, A.N.; Lin, Z.; Wolf, F.W.; O'Shea, K.S.; Lawler, J.; !1Dixit, V.M. !$#journal J. Biol. Chem. (1994) 269:1262-1269 !$#title Thrombospondin 3 is a developmentally regulated heparin !1binding protein. !$#cross-references MUID:94117438; PMID:8288588 !$#accession I55398 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-432,'F',434-562,'D',564-719,'E',721-870,'W',872-956 !1##label RES !'##cross-references GB:L24434; NID:g402718; PIDN:AAA40433.1; !1PID:g402719 REFERENCE S68787 !$#authors Chen, H.; Aeschlimann, D.; Nowlen, J.; Mosher, D.F. !$#journal FEBS Lett. (1996) 387:36-41 !$#title Expression and initial characterization of recombinant mouse !1thrombospondin 1 and thrombospondin 3. !$#cross-references MUID:96234006; PMID:8654563 !$#accession S68788 !'##molecule_type protein !'##residues 'X',23-28,'X',30,'X',32 ##label CHE REFERENCE S72433 !$#authors Collins, M.; Bornstein, P. !$#journal Nucleic Acids Res. (1996) 24:3661-3669 !$#title SP1-binding elements, within the common !1metaxin-thrombospondin 3 intergenic region, participate in !1the regulation of the metaxin gene. !$#cross-references MUID:97025352; PMID:8871542 !$#accession S72433 !'##molecule_type DNA !'##residues 1-26 ##label COL !'##cross-references EMBL:U66257; NID:g1575552; PIDN:AAC52819.1; !1PID:g1575554 GENETICS !$#gene Thbs-3 COMPLEX homopentamer, disulfide linked CLASSIFICATION #superfamily thrombospondin 3; EGF homology KEYWORDS calcium binding; glycoprotein; homopentamer FEATURE !$374-412 #domain EGF homology #label EGF\ !$310,407,644,937 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 956 #molecular-weight 103972 #checksum 2709 SEQUENCE /// ENTRY TSHUP4 #type complete TITLE thrombospondin 4 precursor - human ORGANISM #formal_name Homo sapiens #common_name man DATE 06-Jan-1995 #sequence_revision 11-Aug-1995 #text_change 13-Aug-1999 ACCESSIONS A55710; S36069 REFERENCE A55710 !$#authors Lawler, J.; McHenry, K.; Duquette, M.; Derick, L. !$#journal J. Biol. Chem. (1995) 270:2809-2814 !$#title Characterization of human thrombospondin-4. !$#cross-references MUID:95155352; PMID:7852353 !$#accession A55710 !'##molecule_type mRNA !'##residues 1-961 ##label LAW !'##cross-references EMBL:Z19585; NID:g311625; PIDN:CAA79635.1; !1PID:g311626 !'##note authors translated the codon GTG for residue 616 as Ser GENETICS !$#gene GDB:THBS4 !'##cross-references GDB:463011; OMIM:600715 !$#map_position 1q21-1q23 COMPLEX homotrimer, disulfide linked FUNCTION !$#description participates in cell migration and adhesion, and in platelet !1aggregation CLASSIFICATION #superfamily thrombospondin 3; EGF homology KEYWORDS beta-hydroxyasparagine; beta-hydroxyaspartic acid; calcium !1binding; cell adhesion; glycoprotein; trimer FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-961 #product thrombospondin 4 #status predicted #label !8MAT\ !$290-324 #domain EGF homology #label EGF1\ !$330-362 #domain EGF homology #label EGF\ !$562-564 #region cell attachment (R-G-D) motif\ !$303 #modified_site erythro-beta-hydroxyaspartic acid !8(Asp) #status predicted\ !$343 #modified_site erythro-beta-hydroxyasparagine (Asn) !8#status predicted\ !$612,941 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 961 #molecular-weight 105801 #checksum 3426 SEQUENCE /// ENTRY A34372 #type complete TITLE complement C6 precursor [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 17-Nov-2000 ACCESSIONS A34372; A34235; A32109; A31894; A53072 REFERENCE A34372 !$#authors Haefliger, J.A.; Tschopp, J.; Vial, N.; Jenne, D.E. !$#journal J. Biol. Chem. (1989) 264:18041-18051 !$#title Complete primary structure and functional characterization !1of the sixth component of the human complement system. !1Identification of the C5b-binding domain in complement C6. !$#cross-references MUID:90036879; PMID:2808363 !$#accession A34372 !'##status preliminary !'##molecule_type mRNA !'##residues 1-934 ##label HAE !'##cross-references GB:J05064; NID:g179703; PIDN:AAA51860.1; !1PID:g179704 REFERENCE A34235 !$#authors DiScipio, R.G.; Hugli, T.E. !$#journal J. Biol. Chem. (1989) 264:16197-16206 !$#title The molecular architecture of human complement component C6. !$#cross-references MUID:89380223; PMID:2789218 !$#accession A34235 !'##status preliminary !'##molecule_type mRNA !'##residues 1-118,'E',120-934 ##label DIS !'##cross-references GB:J05024; NID:g187824; PIDN:AAA59668.1; !1PID:g307228 REFERENCE A32109 !$#authors Chakravarti, D.N.; Chakravarti, B.; Parra, C.A.; !1Muller-Eberhard, H.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:2799-2803 !$#title Structural homology of complement protein C6 with other !1channel-forming proteins of complement. !$#cross-references MUID:89202413; PMID:2468158 !$#accession A32109 !'##molecule_type mRNA !'##residues 1-118,'E',120-491 ##label CH2 !'##cross-references GB:J04506; NID:g618465; PIDN:AAB59433.1; !1PID:g618466 REFERENCE A31894 !$#authors Chakravarti, D.N.; Muller-Eberhard, H.J. !$#journal J. Biol. Chem. (1988) 263:18306-18312 !$#title Biochemical characterization of the human complement protein !1C6. Association with alpha-thrombin-like enzyme and absence !1of serine protease activity in cytolytically active C6. !$#cross-references MUID:89054009; PMID:3192535 !$#accession A31894 !'##molecule_type protein !'##residues 22-41 ##label CHA REFERENCE A53072 !$#authors Hobart, M.J.; Fernie, B.; DiScipio, R.G. !$#journal Biochemistry (1993) 32:6198-6205 !$#title Structure of the human C6 gene. !$#cross-references MUID:93291175; PMID:8512929 !$#accession A53072 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type DNA !'##residues 'GPGGSQG',1-47,'A',49-118,'E',120-561,'A',563-618,'A', !1620-700,'A',702-763,'A',765-934 ##label HOB !'##cross-references GB:X72177; NID:g312783; PIDN:CAA50994.1; !1PID:g825633 !'##note sequence extracted from NCBI backbone (NCBIP:134071); this !1sequence was incorrectly processed by NCBI from Figure 3 and !1includes a translation of sequence preceeding the initiation !1codon and single-letter code interpreted splice boundary !1codons written in three-letter code REFERENCE A59362 !$#authors Hofsteenge, J.; Blommers, M.; Hess, D.; Furmanek, A.; !1Miroshnichenko, O. !$#journal J. Biol. Chem. (1999) 274:32786-32794 !$#title The four terminal components of the complement system are !1C-mannosylated on multiple tryptophan residues. !$#cross-references MUID:20020247; PMID:10551839 !$#contents annotation !$#note identification and location of C-mannosylation sites by !1mass-spectroscopy GENETICS !$#gene GDB:C6 !'##cross-references GDB:119045; OMIM:217050 !$#map_position 5p13-5p13 COMPLEX combines with C5b to form the complement C5b-6 complex FUNCTION !$#description as a component of the complement C5b-8 complex, assists in !1the polymerization of complement component C9 !$#pathway complement pathway CLASSIFICATION #superfamily complement c6; complement factor H repeat !1homology; EGF homology; LDL receptor ligand-binding repeat !1homology; thrombospondin type 1 repeat homology KEYWORDS complement alternate pathway; complement pathway; cytolysis; !1glycoprotein; membrane attack complex; membrane protein; !1membrane-associated complex FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-934 #product complement C6 #status experimental #label !8MAT\ !$22-79 #domain thrombospondin type 1 repeat homology #label !8THR1\ !$80-134 #domain thrombospondin type 1 repeat homology #label !8THR2\ !$140-173 #domain LDL receptor ligand-binding repeat homology !8#label LDL\ !$521-552 #domain EGF homology #label EGF\ !$564-612 #domain thrombospondin type 1 repeat homology #label !8THR3\ !$644-699 #domain complement factor H repeat homology #label !8FH01\ !$704-761 #domain complement factor H repeat homology #label !8FH02\ !$29,571 #modified_site 2'-mannosyl-tryptophan (Trp) #status !8experimental\ !$32,90,568,574 #modified_site 2'-mannosyl-tryptophan (Trp) (partial) !8#status experimental\ !$324,855 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 934 #molecular-weight 104785 #checksum 8217 SEQUENCE /// ENTRY A27340 #type complete TITLE complement C7 precursor [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 31-Dec-2000 ACCESSIONS A27340; B53072; C53072 REFERENCE A27340 !$#authors DiScipio, R.G.; Chakravarti, D.N.; Muller-Eberhard, H.J.; !1Fey, G.H. !$#journal J. Biol. Chem. (1988) 263:549-560 !$#title The structure of human complement component C7 and the C5b-7 !1complex. !$#cross-references MUID:88087145; PMID:3335508 !$#accession A27340 !'##molecule_type mRNA !'##residues 1-843 ##label DIS !'##cross-references GB:J03507; NID:g179715; PIDN:AAA51861.1; !1PID:g179716 REFERENCE A53072 !$#authors Hobart, M.J.; Fernie, B.; DiScipio, R.G. !$#journal Biochemistry (1993) 32:6198-6205 !$#title Structure of the human C6 gene. !$#cross-references MUID:93291175; PMID:8512929 !$#accession B53072 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type DNA !'##residues 1-15,'P',17-21,'R',22-143 ##label HOB1 !'##cross-references GB:X72190; NID:g312799; GB:X72191; NID:g312800; !1GB:X72192; NID:g312801 !'##note sequence extracted from NCBI backbone (NCBIP:134085) !'##note this translation is not annotated in GenBank entries HSC7X2, !1HSC7X3, and HSC7X4, release 117.0 !$#accession C53072 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type DNA !'##residues 584-596,'TY',599-624,'N',626-627,'L',629-690,'L' ##label !1HOB2 !'##cross-references GB:X72193; NID:g312797; GB:X72194; NID:g312798 !'##note sequence extracted from NCBI backbone (NCBIP:134087) !'##note this translation is not annotated in GenBank entries HSC7X13, !1and HSC7X14, release 117.0 REFERENCE A59362 !$#authors Hofsteenge, J.; Blommers, M.; Hess, D.; Furmanek, A.; !1Miroshnichenko, O. !$#journal J. Biol. Chem. (1999) 274:32786-32794 !$#title The four terminal components of the complement system are !1C-mannosylated on multiple tryptophan residues. !$#cross-references MUID:20020247; PMID:10551839 !$#contents annotation !$#note identification and location of C-mannosylation sites by !1mass-spectroscopy GENETICS !$#gene GDB:C7 !'##cross-references GDB:119046; OMIM:217070 !$#map_position 5p13-5p13 COMPLEX combines with complement C5b-6 complex to form the !1complement C5b-7 complex FUNCTION !$#description as a component of the complement C5b-8 complex, assists in !1the polymerization of complement component C9 !$#pathway complement pathway CLASSIFICATION #superfamily complement c6; complement factor H repeat !1homology; EGF homology; LDL receptor ligand-binding repeat !1homology; thrombospondin type 1 repeat homology KEYWORDS complement alternate pathway; complement pathway; cytolysis; !1glycoprotein; membrane attack complex; membrane protein; !1membrane-associated complex FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-843 #product complement component C7 #status predicted !8#label MAT\ !$26-80 #domain thrombospondin type 1 repeat homology #label !8THR1\ !$85-119 #domain LDL receptor ligand-binding repeat homology !8#label LDL\ !$455-486 #domain EGF homology #label EGF\ !$499-546 #domain thrombospondin type 1 repeat homology #label !8THR2\ !$571-626 #domain complement factor H repeat homology #label !8FH01\ !$631-688 #domain complement factor H repeat homology #label !8FH02\ !$36 #modified_site 2'-mannosyl-tryptophan (Trp) #status !8experimental\ !$202,754 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$503,506,509 #modified_site 2'-mannosyl-tryptophan (Trp) (partial) !8#status experimental SUMMARY #length 843 #molecular-weight 93514 #checksum 4079 SEQUENCE /// ENTRY C9HU #type complete TITLE complement C9 precursor [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 27-Nov-1985 #sequence_revision 17-Nov-2000 #text_change 17-Nov-2000 ACCESSIONS A59363; I52400; A91029; A94019; S68647; A59364; A03208 REFERENCE A59363 !$#authors Marazitti, D.; Eggertsen, G.; Fey, G.H.; Stanley, K.K. !$#citation unpublished results, 1988, cited by GenBank !$#description Relationships between the gene and protein structure in !1human complement component C9. !$#accession A59363 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-559 ##label MAR1 !'##cross-references GB:X02176; NID:g29580; PIDN:CAA26117.1; PID:g29581 REFERENCE I52400 !$#authors Marazziti, D.; Eggertsen, G.; Fey, G.H.; Stanley, K.K. !$#journal Biochemistry (1988) 27:6529-6534 !$#title Relationships between the gene and protein structure in !1human complement component C9. !$#cross-references MUID:89118250; PMID:3219351 !$#accession I52400 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 62-159 ##label MAR2 !'##cross-references GB:J02833; NID:g179727; PIDN:AAA51890.1; !1PID:g179728 REFERENCE A91029 !$#authors Stanley, K.K.; Kocher, H.P.; Luzio, J.P.; Jackson, P.; !1Tschopp, J. !$#journal EMBO J. (1985) 4:375-382 !$#title The sequence and topology of human complement component C9. !$#cross-references MUID:85257464; PMID:4018030 !$#accession A91029 !'##molecule_type mRNA !'##residues 'S',1-313,315-559 ##label STA !'##cross-references GB:X02176; NID:g29580 REFERENCE A94019 !$#authors DiScipio, R.G.; Gehring, M.R.; Podack, E.R.; Kan, C.C.; !1Hugli, T.E.; Fey, G.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:7298-7302 !$#title Nucleotide sequence of cDNA and derived amino acid sequence !1of human complement component C9. !$#cross-references MUID:85063778; PMID:6095282 !$#accession A94019 !'##molecule_type mRNA !'##residues 2-12,'X',14-16,'X',18-42,'R',44-313,315-416,'P',418-559 !1##label DIS !'##cross-references GB:K02766; NID:g179725; PIDN:AAA51889.1; !1PID:g179726 REFERENCE S68647 !$#authors Lengweiler, S.; Schaller, J.; Rickli, E.E. !$#journal FEBS Lett. (1996) 380:8-12 !$#title Identification of disulfide bonds in the ninth component !1(C9) of human complement. !$#cross-references MUID:96181657; PMID:8603752 !$#accession S68647 !'##molecule_type protein !'##residues 34-47;52-59;69-87,'X',89-93,'T', !194-98;106-113;118-131;136-145;180-181,'X',183-187;252-253, !1'X',255-258;377-379,'X',381;401-406;505-514;523-525,'X',527, !1'X',529,'X',531-532;536-540 ##label LEN REFERENCE A59364 !$#authors Witze.Schlomp, K.; Hobart, M.J.; Fernie, B.A.; Orren, A.; !1Wurzner, R.; Rittner, C.; Kaufmann, T.; Schneider, P.M. !$#journal Immunogenetics (1998) 48:144-147 !$#title Heterogeneity in the genetic basis of human complement C9 !1deficiency. !$#cross-references MUID:98298010; PMID:9634479 !$#note submitted to GenBank, September 1996 !$#accession A59364 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 27-559 ##label WIT !'##cross-references GB:Y08545; NID:g1834472; PIDN:CAA69849.1; !1PID:g2258128 !'##experimental_source macronuclear; tissue type blood; cell type !1lymphocyte REFERENCE A59362 !$#authors Hofsteenge, J.; Blommers, M.; Hess, D.; Furmanek, A.; !1Miroshnichenko, O. !$#journal J. Biol. Chem. (1999) 274:32786-32794 !$#title The four terminal components of the complement system are !1C-mannosylated on multiple tryptophan residues. !$#cross-references MUID:20020247; PMID:10551839 !$#contents annotation !$#note identification and location of C-mannosylation sites by !1mass-spectroscopy and (1)H-NMR GENETICS !$#gene GDB:C9 !'##cross-references GDB:119738; OMIM:120940 !$#map_position 5p13-5p13 COMPLEX monomer in plasma; 10 to 16 chain multimer in transmembrane !1form FUNCTION !$#description in association with complement C5b-8 complex polymerizes to !1form a transmembrane channel !$#pathway complement pathway CLASSIFICATION #superfamily complement C9; EGF homology; LDL receptor !1ligand-binding repeat homology; thrombospondin type 1 repeat !1homology KEYWORDS complement pathway; cytolysis; glycoprotein; inflammation; !1membrane attack complex; multimer; plasma; transmembrane !1protein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-265,266-559 #product complement C9 #status predicted #label MAT\ !$22-265 #domain complement C9a #status predicted #label C9A\ !$41-95 #domain thrombospondin type 1 repeat homology #label !8THR\ !$101-134 #domain LDL receptor ligand-binding repeat homology !8#label LDL\ !$266-559 #domain complement C9b #status predicted #label C9B\ !$510-539 #domain EGF homology #label EGF\ !$43-78,54-57,88-94, !$142-181,254-255, !$380-405,510-526, !$513-528,530-539 #disulfide_bonds #status experimental\ !$48 #modified_site 2'-mannosyl-tryptophan (Trp) #status !8experimental\ !$51 #modified_site 2'-mannosyl-tryptophan (Trp) (partial) !8#status experimental\ !$265-266 #cleavage_site His-Gly (thrombin) #status predicted\ !$277,415 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 559 #molecular-weight 63173 #checksum 9684 SEQUENCE /// ENTRY C8HUA #type complete TITLE complement C8 alpha chain precursor [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 28-Dec-1987 #sequence_revision 17-Nov-2000 #text_change 17-Nov-2000 ACCESSIONS I37213; A26704 REFERENCE I37213 !$#authors Michelotti, G.A.; Snider, J.V.; Sodetz, J.M. !$#journal Hum. Genet. (1995) 95:513-518 !$#title Genomic organization of human complement protein C8 alpha !1and further examination of its linkage to C8 beta. !$#cross-references MUID:95278905; PMID:7759071 !$#accession I37213 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-584 ##label MIC !'##cross-references EMBL:U08006; NID:g901862; PIDN:AAA82124.1; !1PID:g901864 REFERENCE A26704 !$#authors Rao, A.G.; Howard, O.M.Z.; Ng, S.C.; Whitehead, A.S.; !1Colten, H.R.; Sodetz, J.M. !$#journal Biochemistry (1987) 26:3556-3564 !$#title Complementary DNA and derived amino acid sequence of the !1alpha subunit of human complement protein C8: evidence for !1the existence of a separate alpha subunit messenger RNA. !$#cross-references MUID:88000560; PMID:2820471 !$#accession A26704 !'##molecule_type mRNA !'##residues 1-92,'Q',94-466,'CCGTQAWASGGQ',480-574,'P',576-584 ##label !1RAO !'##note part of the sequence was confirmed by protein sequencing REFERENCE A59362 !$#authors Hofsteenge, J.; Blommers, M.; Hess, D.; Furmanek, A.; !1Miroshnichenko, O. !$#journal J. Biol. Chem. (1999) 274:32786-32794 !$#title The four terminal components of the complement system are !1C-mannosylated on multiple tryptophan residues. !$#cross-references MUID:20020247; PMID:10551839 !$#contents annotation !$#note identification and location of C-mannosylation sites by !1mass-spectroscopy GENETICS !$#gene GDB:C8A !'##cross-references GDB:119735; OMIM:120950 !$#map_position 1p32-1p32 !$#introns 26/2; 57/3; 106/1; 155/2; 218/3; 285/3; 366/1; 408/1; 460/3; !1535/1 COMPLEX heterotrimer of C8 alpha chain (PIR:C8HUA), C8 beta chain !1(PIR:C8HUB), and C8 gamma chain (PIR:C8HUG); the trimer !1associates with the C5b-7 complex FUNCTION !$#description combines with complement C5b-7 complex to polymerize !1complement component C9 !$#pathway complement pathway CLASSIFICATION #superfamily complement C9; EGF homology; LDL receptor !1ligand-binding repeat homology; thrombospondin type 1 repeat !1homology KEYWORDS complement pathway; cytolysis; glycoprotein; membrane attack !1complex; plasma FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-30 #domain propeptide #status predicted #label PRO\ !$31-584 #product complement C8 alpha chain #status predicted !8#label MPT\ !$37-91 #domain thrombospondin type 1 repeat homology #label !8THR1\ !$96-130 #domain LDL receptor ligand-binding repeat homology !8#label LDL\ !$497-528 #domain EGF homology #label EGF\ !$538-584 #domain thrombospondin type 1 repeat homology #label !8THR2\ !$43 #binding_site carbohydrate (Asn) (covalent) #status !8absent\ !$44,542,545,548 #modified_site 2'-mannosyl-tryptophan (Trp) #status !8experimental\ !$437 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 584 #molecular-weight 65153 #checksum 7933 SEQUENCE /// ENTRY C8HUB #type complete TITLE complement C8 beta chain precursor [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 28-Dec-1987 #sequence_revision 15-Oct-1994 #text_change 17-Nov-2000 ACCESSIONS A43071; A94618; A90517; A27208; A26705 REFERENCE A43071 !$#authors Sodetz, J.M. !$#submission submitted to GenBank, June 1988 !$#accession A43071 !'##molecule_type mRNA !'##residues 1-591 ##label SOD1 !'##cross-references GB:M16973; NID:g179719; PIDN:AAA51862.1; !1PID:g179720 REFERENCE A94618 !$#authors Sodetz, J.M. !$#submission submitted to the Protein Sequence Database, August 1987 !$#accession A94618 !'##molecule_type mRNA !'##residues 'SQCD',5-591 ##label SOD2 REFERENCE A90517 !$#authors Howard, O.M.Z.; Rao, A.G.; Sodetz, J.M. !$#journal Biochemistry (1987) 26:3565-3570 !$#title Complementary DNA and derived amino acid sequence of the !1beta subunit of human complement protein C8: identification !1of a close structural and ancestral relationship to the !1alpha subunit and C9. !$#cross-references MUID:88000561; PMID:2820472 !$#accession A90517 !'##molecule_type mRNA !'##residues 'SQCD',5-436,'PGIPGAAD',446-591 ##label HOW !'##cross-references GB:M16973; NID:g179719 !'##note parts of this sequence, including the amino and carboxyl ends !1of the mature protein, were confirmed by protein sequencing REFERENCE A27208 !$#authors Haefliger, J.A.; Tschopp, J.; Nardelli, D.; Wahli, W.; !1Kocher, H.P.; Tosi, M.; Stanley, K.K. !$#journal Biochemistry (1987) 26:3551-3556 !$#title Complementary DNA cloning of complement C8-beta-and its !1sequence homology to C9. !$#cross-references MUID:88000559; PMID:3651397 !$#accession A27208 !'##molecule_type mRNA !'##residues 47-116,'R',118-591 ##label HAE !'##cross-references GB:X04393; NID:g29574; PIDN:CAA27981.1; PID:g29575 REFERENCE A59362 !$#authors Hofsteenge, J.; Blommers, M.; Hess, D.; Furmanek, A.; !1Miroshnichenko, O. !$#journal J. Biol. Chem. (1999) 274:32786-32794 !$#title The four terminal components of the complement system are !1C-mannosylated on multiple tryptophan residues. !$#cross-references MUID:20020247; PMID:10551839 !$#contents annotation !$#note identification and location of C-mannosylation sites by !1mass-spectroscopy GENETICS !$#gene GDB:C8B !'##cross-references GDB:119736; OMIM:120960 !$#map_position 1p32-1p32 COMPLEX heterotrimer of C8 alpha chain (PIR:C8HUA), C8 beta chain !1(PIR:C8HUB), and C8 gamma chain (PIR:C8HUG); the trimer !1associates with the C5b-7 complex FUNCTION !$#description combines with complement C5b-7 complex to polymerize !1complement component C9 !$#pathway complement pathway CLASSIFICATION #superfamily complement C9; EGF homology; LDL receptor !1ligand-binding repeat homology; thrombospondin type 1 repeat !1homology KEYWORDS complement alternate pathway; complement pathway; cytolysis; !1glycoprotein; membrane attack complex; membrane protein; !1membrane-associated complex; plasma FEATURE !$1-32 #domain signal sequence #status predicted #label SIG\ !$33-54 #domain propeptide #status predicted #label PRO\ !$55-591 #product complement C8 beta chain #status !8experimental #label MPT\ !$63-117 #domain thrombospondin type 1 repeat homology #label !8THR1\ !$122-155 #domain LDL receptor ligand-binding repeat homology !8#label LDL3\ !$503-534 #domain EGF homology #label EGF\ !$544-591 #domain thrombospondin type 1 repeat homology #label !8THR2\ !$70,73,551,554 #modified_site 2'-mannosyl-tryptophan (Trp) #status !8experimental\ !$243 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$553 #binding_site carbohydrate (Asn) (covalent) #status !8absent SUMMARY #length 591 #molecular-weight 66947 #checksum 5079 SEQUENCE /// ENTRY NBHUH #type complete TITLE complement factor H precursor, long splice form [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 08-Dec-2000 ACCESSIONS S00254; A60238; A54726; A61565; A26505; I72654; S66298 REFERENCE S00254 !$#authors Ripoche, J.; Day, A.J.; Harris, T.J.R.; Sim, R.B. !$#journal Biochem. J. (1988) 249:593-602 !$#title The complete amino acid sequence of human complement factor !1H. !$#cross-references MUID:88134059; PMID:2963625 !$#accession S00254 !'##molecule_type mRNA !'##residues 1-1231 ##label RIP !'##cross-references EMBL:Y00716; NID:g31964; PIDN:CAA68704.1; !1PID:g31965 !'##note 402-Tyr was also found !'##note parts of this sequence, including the amino and carboxyl ends !1of the mature protein, were confirmed by protein sequencing REFERENCE A60238 !$#authors Estaller, C.; Schwaeble, W.; Dierich, M.; Weiss, E.H. !$#journal Eur. J. Immunol. (1991) 21:799-802 !$#title Human complement factor H: two factor H proteins are derived !1from alternatively spliced transcripts. !$#cross-references MUID:91184292; PMID:1826264 !$#accession A60238 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-56;1177-1231 ##label EST !'##note only portions of this 4.3 kilobase mRNA were sequenced REFERENCE A54726 !$#authors Day, A.J.; Ripoche, J.; Lyons, A.; McIntosh, B.; Harris, !1T.J.R.; Sim, R.B. !$#journal Biosci. Rep. (1987) 7:201-207 !$#title Sequence analysis of a cDNA clone encoding the C-terminal !1end of human complement factor H. !$#cross-references MUID:88025472; PMID:2889480 !$#accession A54726 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 'DFRN',579-1231 ##label DAY !'##cross-references GB:M17517; NID:g180497; PIDN:AAA52016.1; !1PID:g180498 !'##note parts of this sequence were determined by protein sequencing REFERENCE A61565 !$#authors Ripoche, J.; Day, A.J.; Willis, A.C.; Belt, K.T.; Campbell, !1R.D.; Sim, R.B. !$#journal Biosci. Rep. (1986) 6:65-72 !$#title Partial characterization of human complement factor H by !1protein and cDNA sequencing: homology with other complement !1and non-complement proteins. !$#cross-references MUID:86188123; PMID:2938641 !$#accession A61565 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 'METGRNHLNAKI',1050-1057,'T',1059-1102 ##label RI2 REFERENCE A26505 !$#authors Sim, R.B.; DiScipio, R.G. !$#journal Biochem. J. (1982) 205:285-293 !$#title Purification and structural studies on the complement-system !1control protein beta-1-H (factor H). !$#cross-references MUID:83048213; PMID:6215918 !$#accession A26505 !'##molecule_type protein !'##residues 19-20,'Q',22-29,'V',31-33,'Q',35 ##label SIM REFERENCE A44551 !$#authors Barlow, P.N.; Norman, D.G.; Steinkasserer, A.; Horne, T.J.; !1Pearce, J.; Driscoll, P.C.; Sim, R.B.; Campbell, I.D. !$#journal Biochemistry (1992) 31:3626-3634 !$#title Solution structure of the fifth repeat of factor H: A second !1example of the complement control protein module. !$#cross-references MUID:92232649; PMID:1533152 !$#contents annotation; NMR structure determination, residues 264-292 REFERENCE A49224 !$#authors Norman, D.G.; Barlow, P.N.; Baron, M.; Day, A.J.; Sim, R.B.; !1Campbell, I.D. !$#journal J. Mol. Biol. (1991) 219:717-725 !$#title Three-dimensional structure of a complement control protein !1module in solution. !$#cross-references MUID:91278097; PMID:1829116 !$#contents annotation; NMR structure determination, residues 927-985 REFERENCE I56100 !$#authors Estaller, C.; Koistinen, V.; Schwaeble, W.; Dierich, M.P.; !1Weiss, E.H. !$#journal J. Immunol. (1991) 146:3190-3196 !$#title Cloning of the 1.4-kb mRNA species of human complement !1factor H reveals a novel member of the short consensus !1repeat family related to the carboxy terminal of the !1classical 150-kDa molecule. !$#cross-references MUID:91201892; PMID:1826708 !$#accession I72654 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1047-1231 ##label RES !'##cross-references GB:M65294; NID:g183766; PIDN:AAA35948.1; !1PID:g183767 REFERENCE S66298 !$#authors Carron, J.A.; Bates, R.C.; Smith, A.I.; Tetoz, T.; Arellano, !1A.; Gordon, D.L.; Burns, G.F. !$#journal Biochim. Biophys. Acta (1996) 1289:305-311 !$#title Factor H co-purifies with thrombospondin isolated from !1platelet secretate. !$#cross-references MUID:96205365; PMID:8620012 !$#accession S66298 !'##status preliminary !'##molecule_type protein !'##residues 411-419;574-578,580-582 ##label CAR COMMENT Factor H has also been found bound to cell membranes in an !1unknown manner. However, it has at least one cell attachment !1site motif in repeat 4. COMMENT Alternative transcipts of 4.3, 1.8, and 1.4 kilobases are !1expressed in liver. See also PIR:NBHUHS. GENETICS HF1 !$#gene GDB:HF1; HF !'##cross-references GDB:120041; OMIM:134370 !$#map_position 1q32-1q32 GENETICS HF2 !$#gene GDB:HF2; HF !'##cross-references GDB:129095 !$#map_position 1q32-1q32 !$#note the correspondence between the two loci and the sequences !1indicated is unclear; factor H has been reported to have !1several allelic forms FUNCTION !$#description a cofactor in the inactivation of C3b by serine proteinase !1I; also increases the rate of dissociation of the C3bBb !1complex (C3 convertase) and the (C3b)nBb complex (C5 !1convertase) in the alternative complement pathway !$#pathway complement alternate pathway CLASSIFICATION #superfamily complement factor H; complement factor H repeat !1homology KEYWORDS alternative splicing; complement alternate pathway; !1glycoprotein; plasma FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-1229 #product complement factor H #status experimental !8#label MPT\ !$19-449 #product complement factor H, short splice form !8#status experimental #label MAT\ !$21-80 #domain complement factor H repeat homology #label !8FH01\ !$85-141 #domain complement factor H repeat homology #label !8FH02\ !$146-205 #domain complement factor H repeat homology #label !8FH03\ !$210-262 #domain complement factor H repeat homology #label !8FH04\ !$246-248 #region cell attachment (R-G-D) motif\ !$267-320 #domain complement factor H repeat homology #label !8FH05\ !$325-385 #domain complement factor H repeat homology #label !8FH06\ !$389-442 #domain complement factor H repeat homology #label !8FH07\ !$448-505 #domain complement factor H repeat homology #label !8FH08\ !$509-564 #domain complement factor H repeat homology #label !8FH09\ !$569-623 #domain complement factor H repeat homology #label !8FH10\ !$630-684 #domain complement factor H repeat homology #label !8FH11\ !$691-744 #domain complement factor H repeat homology #label !8FH12\ !$753-803 #domain complement factor H repeat homology #label !8FH13\ !$811-864 #domain complement factor H repeat homology #label !8FH14\ !$870-926 #domain complement factor H repeat homology #label !8FH15\ !$931-984 #domain complement factor H repeat homology #label !8FH16\ !$989-1043 #domain complement factor H repeat homology #label !8FH17\ !$1048-1102 #domain complement factor H repeat homology #label !8FH18\ !$1109-1163 #domain complement factor H repeat homology #label !8FH19\ !$1167-1228 #domain complement factor H repeat homology #label !8FH20\ !$21-66,52-80,85-129, !$114-141,146-192, !$178-205,210-251, !$237-262,267-309, !$294-320,325-374, !$357-385,389-431, !$416-442,448-494, !$477-505,509-553, !$536-564,569-611, !$597-623,630-673, !$659-684,691-733, !$719-744,753-792, !$781-803,811-853, !$839-864,870-915, !$901-926,931-973, !$959-984,989-1032, !$1018-1043, !$1048-1091, !$1077-1102, !$1109-1152, !$1138-1163, !$1167-1218,1201-1228 #disulfide_bonds #status predicted\ !$217 #binding_site carbohydrate (Asn) (covalent) #status !8absent\ !$529,802,822,882,911 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$718,1029,1095 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1231 #molecular-weight 139124 #checksum 9625 SEQUENCE /// ENTRY NBHUHS #type complete TITLE complement factor H precursor, short splice form [validated] - human ALTERNATE_NAMES complement factor H-related protein; complement protein H ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1993 #sequence_revision 23-Feb-1996 #text_change 08-Dec-2000 ACCESSIONS S03013; B60238; A27877; A61103; A26505; S10479 REFERENCE S00254 !$#authors Ripoche, J.; Day, A.J.; Harris, T.J.R.; Sim, R.B. !$#journal Biochem. J. (1988) 249:593-602 !$#title The complete amino acid sequence of human complement factor !1H. !$#cross-references MUID:88134059; PMID:2963625 !$#accession S03013 !'##molecule_type mRNA !'##residues 1-449 ##label RIP !'##cross-references EMBL:X07523; EMBL:Y00716; NID:g32492; !1PIDN:CAA30403.1; PID:g758073 !'##note part of this sequence, including the amino end of the mature !1protein was confirmed by protein sequencing !'##note 402-Tyr was also found REFERENCE A60238 !$#authors Estaller, C.; Schwaeble, W.; Dierich, M.; Weiss, E.H. !$#journal Eur. J. Immunol. (1991) 21:799-802 !$#title Human complement factor H: two factor H proteins are derived !1from alternatively spliced transcripts. !$#cross-references MUID:91184292; PMID:1826264 !$#accession B60238 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-33;434-449 ##label EST !'##note only portions of this 1.8 kilobase mRNA were sequenced REFERENCE A27877 !$#authors Schulz, T.F.; Schwaeble, W.; Stanley, K.K.; Weiss, E.; !1Dierich, M.P. !$#journal Eur. J. Immunol. (1986) 16:1351-1355 !$#title Human complement factor H: isolation of cDNA clones and !1partial cDNA sequence of the 38-kDa tryptic fragment !1containing the binding site for C3b. !$#cross-references MUID:87054207; PMID:2946589 !$#accession A27877 !'##molecule_type mRNA !'##residues 'IL',55-401,'Y',403-449 ##label SCH !'##cross-references GB:X04697; NID:g31991; PIDN:CAB41739.1; !1PID:g4725976 !'##note an additional nucleotide present within the codon for Glu-310 !1was thought to be a cloning artifact and was ignored in !1translation REFERENCE A61103 !$#authors Schwaeble, W.; Zwirner, J.; Schulz, T.F.; Linke, R.P.; !1Dierich, M.P.; Weiss, E.H. !$#journal Eur. J. Immunol. (1987) 17:1485-1489 !$#title Human complement factor H: expression of an additional !1truncated gene product of 43 kDa in human liver. !$#cross-references MUID:88055295; PMID:2445583 !$#accession A61103 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 27-76 ##label SC2 !'##note this is a partial sequence of an alternatively spliced 1.8 !1kilobase mRNA that is translated to yield a 43 K form !1related to factor H REFERENCE A26505 !$#authors Sim, R.B.; DiScipio, R.G. !$#journal Biochem. J. (1982) 205:285-293 !$#title Purification and structural studies on the complement-system !1control protein beta-1-H (factor H). !$#cross-references MUID:83048213; PMID:6215918 !$#accession A26505 !'##molecule_type protein !'##residues 19-20,'Q',22-29,'V',31-33,'Q',35 ##label SIM REFERENCE A44551 !$#authors Barlow, P.N.; Norman, D.G.; Steinkasserer, A.; Horne, T.J.; !1Pearce, J.; Driscoll, P.C.; Sim, R.B.; Campbell, I.D. !$#journal Biochemistry (1992) 31:3626-3634 !$#title Solution structure of the fifth repeat of factor H: A second !1example of the complement control protein module. !$#cross-references MUID:92232649; PMID:1533152 !$#contents annotation; NMR structure determination, residues 264-292 REFERENCE S10479 !$#authors Kristensen, T.; Wetsel, R.A.; Tack, B.F. !$#journal J. Immunol. (1986) 136:3407-3411 !$#title Structural analysis of human complement protein H: homology !1with C4b binding protein, beta(2)-glycoprotein I, and the Ba !1fragment of B. !$#cross-references MUID:86169701; PMID:2937845 !$#accession S10479 !'##molecule_type mRNA !'##residues 226-401,'Y',403-449 ##label KRI !'##cross-references GB:M12383; NID:g180472; PIDN:AAA52013.1; !1PID:g180473 COMMENT Factor H has also been found bound to cell membranes in an !1unknown manner. However, it has at least one cell attachment !1site motif in repeat 4. COMMENT Alternative transcipts of 4.3, 1.8, and 1.4 kilobases are !1expressed in liver. See also PIR:NBHUH. GENETICS HF1 !$#gene GDB:HF1; HF !'##cross-references GDB:120041; OMIM:134370 !$#map_position 1q32-1q32 GENETICS HF2 !$#gene GDB:HF2; HF !'##cross-references GDB:129095 !$#map_position 1q32-1q32 !$#note the correspondence between the two loci and the sequences !1indicated is unclear; factor H has been reported to have !1several allelic forms FUNCTION !$#description a cofactor in the inactivation of C3b by serine proteinase !1I; also increases the rate of dissociation of the C3bBb !1complex (C3 convertase) and the (C3b)nBb complex (C5 !1convertase) in the alternative complement pathway !$#pathway complement alternate pathway CLASSIFICATION #superfamily complement factor H; complement factor H repeat !1homology KEYWORDS alternative splicing; complement alternate pathway; !1glycoprotein; plasma FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-449 #product complement factor H, short splice form !8#status experimental #label MAT\ !$21-80 #domain complement factor H repeat homology #label !8FH01\ !$85-141 #domain complement factor H repeat homology #label !8FH02\ !$146-205 #domain complement factor H repeat homology #label !8FH03\ !$210-262 #domain complement factor H repeat homology #label !8FH04\ !$246-248 #region cell attachment (R-G-D) motif\ !$267-320 #domain complement factor H repeat homology #label !8FH05\ !$325-385 #domain complement factor H repeat homology #label !8FH06\ !$389-442 #domain complement factor H repeat homology #label !8FH07\ !$21-66,52-80,85-129, !$114-141,146-192, !$178-205,210-251, !$237-262,267-309, !$294-320,325-374, !$357-385,389-431, !$416-442 #disulfide_bonds #status predicted\ !$217 #binding_site carbohydrate (Asn) (covalent) #status !8absent SUMMARY #length 449 #molecular-weight 51007 #checksum 6077 SEQUENCE /// ENTRY NBMSH #type complete TITLE complement factor H precursor - mouse ALTERNATE_NAMES protein beta-1-H ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 22-Jun-1999 ACCESSIONS A26154; I49711; I49728 REFERENCE A26154 !$#authors Kristensen, T.; Tack, B.F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:3963-3967 !$#title Murine protein H is comprised of 20 repeating units, 61 !1amino acids in length. !$#cross-references MUID:86233353; PMID:2940596 !$#accession A26154 !'##molecule_type mRNA !'##residues 1-1234 ##label KRI !'##cross-references GB:M12660; NID:g193724; PIDN:AAA37759.1; !1PID:g387181 REFERENCE I49711 !$#authors Natsuume-Sakai, S.; Nonaka, M.; Nonaka, M.; Harada, Y. !$#journal J. Immunol. (1990) 144:358-362 !$#title Demonstration of an unusual allelic variation of mouse !1factor H by the complete cDNA sequence of the H.2 allotype. !$#cross-references MUID:90111033; PMID:2136885 !$#accession I49711 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-18 ##label RES !'##cross-references GB:M31979; NID:g193726; PIDN:AAA37762.1; !1PID:g193729 REFERENCE I49728 !$#authors Munoz-Canoves, P.; Tack, B.F.; Vik, D.P. !$#journal Biochemistry (1989) 28:9891-9897 !$#title Analysis of complement factor H mRNA expression: !1Dexamethasone and IFN-gamma increase the level of H in L !1cells. !$#cross-references MUID:90148935; PMID:2533512 !$#accession I49728 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-19 ##label RE2 !'##cross-references GB:J02891; NID:g193805; PIDN:AAA37795.1; !1PID:g553926 COMMENT Two codominant alleles of factor H are present in mice. COMMENT Factor H functions as a cofactor in the inactivation of C3b !1by serine proteinase I and also increases the rate of !1dissociation of the C3bBb complex (C3 convertase) and the !1(C3b)nBb complex (C5 convertase) in the alternative !1complement pathway. GENETICS !$#map_position 1 CLASSIFICATION #superfamily complement factor H; complement factor H repeat !1homology KEYWORDS complement alternate pathway; duplication; glycoprotein; !1plasma FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-1234 #product complement factor H #status predicted #label !8MPT\ !$21-80 #domain complement factor H repeat homology #label !8FH01\ !$85-141 #domain complement factor H repeat homology #label !8FH02\ !$146-205 #domain complement factor H repeat homology #label !8FH03\ !$210-262 #domain complement factor H repeat homology #label !8FH04\ !$246-248 #region cell attachment (R-G-D) motif\ !$267-320 #domain complement factor H repeat homology #label !8FH05\ !$325-385 #domain complement factor H repeat homology #label !8FH06\ !$389-442 #domain complement factor H repeat homology #label !8FH07\ !$448-505 #domain complement factor H repeat homology #label !8FH08\ !$509-564 #domain complement factor H repeat homology #label !8FH09\ !$569-622 #domain complement factor H repeat homology #label !8FH10\ !$629-683 #domain complement factor H repeat homology #label !8FH11\ !$690-743 #domain complement factor H repeat homology #label !8FH12\ !$752-802 #domain complement factor H repeat homology #label !8FH13\ !$808-861 #domain complement factor H repeat homology #label !8FH14\ !$867-931 #domain complement factor H repeat homology #label !8FH15\ !$936-989 #domain complement factor H repeat homology #label !8FH16\ !$994-1048 #domain complement factor H repeat homology #label !8FH17\ !$1053-1107 #domain complement factor H repeat homology #label !8FH18\ !$1114-1168 #domain complement factor H repeat homology #label !8FH19\ !$1172-1233 #domain complement factor H repeat homology #label !8FH20\ !$21-66,52-80,85-129, !$114-141,146-192, !$178-205,210-251, !$237-262,267-309, !$294-320,325-374, !$357-385,389-431, !$416-442,448-494, !$477-505,509-553, !$536-564,569-610, !$597-622,629-672, !$658-683,690-732, !$718-743,752-791, !$780-802,808-850, !$836-861,867-920, !$906-931,936-978, !$964-989,994-1037, !$1023-1048, !$1053-1096, !$1082-1107, !$1114-1157, !$1143-1168, !$1172-1223,1206-1233 #disulfide_bonds #status predicted\ !$676,721,773,801, !$1030,1061,1225 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1234 #molecular-weight 139081 #checksum 3676 SEQUENCE /// ENTRY JC1195 #type complete TITLE plasminogen-related protein precursor - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS JC1195 REFERENCE JC1195 !$#authors Weissbach, L.; Treadwell, B.V. !$#journal Biochem. Biophys. Res. Commun. (1992) 186:1108-1114 !$#title A plasminogen-related gene is expressed in cancer cells. !$#cross-references MUID:92359990; PMID:1379800 !$#accession JC1195 !'##molecule_type mRNA !'##residues 1-96 ##label WEI !'##cross-references GB:M93143; NID:g4481742; PIDN:AAB06491.1; !1PID:g190072 COMMENT This protein is expressed most prominently in malignent !1cells. GENETICS !$#gene GDB:PLGL !'##cross-references GDB:120300; OMIM:173340 !$#map_position 2p11-2q11 CLASSIFICATION #superfamily plasminogen-related protein; !1plasminogen-related protein precursor homology FEATURE !$1-96 #domain plasminogen-related protein precursor !8homology #label PLPH\ !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-96 #product plasminogen-related protein #status !8predicted #label MAT\ !$49-73,53-61 #disulfide_bonds #status predicted SUMMARY #length 96 #molecular-weight 10971 #checksum 1773 SEQUENCE /// ENTRY PL0009 #type complete TITLE complement C3d/Epstein-Barr virus receptor precursor - human ALTERNATE_NAMES complement receptor 2; CR2/CD21 ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1992 #sequence_revision 07-Jul-1995 #text_change 22-Jun-1999 ACCESSIONS JL0028; A39958; A32036; A24319; B24319; C24319; D24319; !1E24319; F24319; PL0009 REFERENCE JL0028 !$#authors Weis, J.J.; Toothaker, L.E.; Smith, J.A.; Weis, J.H.; !1Fearon, D.T. !$#journal J. Exp. Med. (1988) 167:1047-1066 !$#title Structure of the human B lymphocyte receptor for C3d and the !1Epstein-Barr virus and relatedness to other members of the !1family of C3/C4 binding proteins. !$#cross-references MUID:88171282; PMID:2832506 !$#accession JL0028 !'##molecule_type mRNA !'##residues 1-1091 ##label WEI !'##note nucleotides 1566-1625 are missing from Figure 1; therefore, !1residues 522-542 have not been compared to nucleotide !1translation REFERENCE A39958 !$#authors Moore, M.D.; Cooper, N.R.; Tack, B.F.; Nemerow, G.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:9194-9198 !$#title Molecular cloning of the cDNA encoding the Epstein-Barr !1virus/C3d receptor (complement receptor type 2) of human B !1lymphocytes. !$#cross-references MUID:88097454; PMID:2827171 !$#accession A39958 !'##molecule_type mRNA !'##residues 1-456,'G',457-644,'R',646-669,'R',671-816, !1'NCSAEVILKAWILERAF',835-840,'L',846-943,'V',945-947,'P', !1949-1050,'I',1052-1060,'E',1062-1091 ##label MOO !'##cross-references GB:J03565; NID:g181919; PIDN:AAA35784.1; !1PID:g181920 REFERENCE A32036 !$#authors Fujisaku, A.; Harley, J.B.; Frank, M.B.; Gruner, B.A.; !1Frazier, B.; Holers, V.M. !$#journal J. Biol. Chem. (1989) 264:2118-2125 !$#title Genomic organization and polymorphisms of the human C3d/ !1Epstein-Barr virus receptor. !$#cross-references MUID:89123277; PMID:2563370 !$#accession A32036 !'##molecule_type mRNA !'##residues 1-456,'G',457-658,718-1050,'I',1052-1060,'E',1062-1091 !1##label FUJ !'##cross-references GB:J04463 REFERENCE A94114 !$#authors Weis, J.J.; Fearon, D.T.; Klickstein, L.B.; Wong, W.W.; !1Richards, S.A.; De Bruyn Kops, A.; Smith, J.A.; Weis, J.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:5639-5643 !$#title Identification of a partial cDNA clone for the C3d/ !1Epstein-Barr virus receptor of human B lymphocytes: homology !1with the receptor for fragments C3b and C4b of the third and !1fourth components of complement. !$#cross-references MUID:86287311; PMID:3016712 !$#accession A24319 !'##molecule_type protein !'##residues 226-230,'XILQ';257-267;332-341;583-591,'Q',593,'D', !1595-596;728-735 ##label WE2 !'##experimental_source B-lymphoblastoid cell lines SB and Raji GENETICS !$#gene GDB:CR2 !'##cross-references GDB:119802; OMIM:120650 !$#map_position 1q32-1q32 CLASSIFICATION #superfamily complement C3d/Epstein-Barr virus receptor; !1complement factor H repeat homology KEYWORDS alternative splicing; duplication; glycoprotein; !1transmembrane protein FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-1091 #product complement receptor 2 (16-repeat form) !8#status predicted #label MAT1\ !$21-658,718-1091 #product complement receptor 2 (15-repeat form) !8#status predicted #label MAT2\ !$23-82 #domain complement factor H repeat homology #label !8FH01\ !$91-146 #domain complement factor H repeat homology #label !8FH02\ !$154-210 #domain complement factor H repeat homology #label !8FH03\ !$215-271 #domain complement factor H repeat homology #label !8FH04\ !$276-342 #domain complement factor H repeat homology #label !8FH05\ !$351-406 #domain complement factor H repeat homology #label !8FH06\ !$410-465 #domain complement factor H repeat homology #label !8FH07\ !$470-521 #domain complement factor H repeat homology #label !8FH08\ !$526-592 #domain complement factor H repeat homology #label !8FH09\ !$601-656 #domain complement factor H repeat homology #label !8FH10\ !$660-716 #domain complement factor H repeat homology #label !8FH11\ !$720-772 #domain complement factor H repeat homology #label !8FH12\ !$777-837 #domain complement factor H repeat homology #label !8FH13\ !$846-901 #domain complement factor H repeat homology #label !8FH14\ !$909-965 #domain complement factor H repeat homology #label !8FH15\ !$970-1026 #domain complement factor H repeat homology #label !8FH16\ !$1034-1056 #domain transmembrane #status predicted #label TMM\ !$1057-1091 #domain intracellular #status predicted #label INT\ !$121,127,294,372, !$622,698,858,881,919 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1091 #molecular-weight 119079 #checksum 5314 SEQUENCE /// ENTRY A43526 #type complete TITLE complement C3d/Epstein-Barr virus receptor 2 precursor - mouse ALTERNATE_NAMES complement receptor type 2 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A43526; A43538; A32215; A45802; B32215 REFERENCE A43526 !$#authors Fingeroth, J.D. !$#journal J. Immunol. (1990) 144:3458-3467 !$#title Comparative structure and evolution of murine CR2. The !1homolog of the human C3d/EBV receptor (CD21). !$#cross-references MUID:90229735; PMID:2139457 !$#accession A43526 !'##molecule_type mRNA !'##residues 1-1025 ##label FIN !'##cross-references GB:M35684; EMBL:J04153; NID:g192687; !1PIDN:AAA37448.1; PID:g192688 REFERENCE A43538 !$#authors Molina, H.; Kinoshita, T.; Inoue, K.; Carel, J.C.; Holers, !1V.M. !$#journal J. Immunol. (1990) 145:2974-2983 !$#title A molecular and immunochemical characterization of mouse !1CR2. Evidence for a single gene model of mouse complement !1receptors 1 and 2. !$#cross-references MUID:91010789; PMID:2145366 !$#accession A43538 !'##molecule_type mRNA !'##residues 12-305,'T',307-519,'A',521-1025 ##label MOL !'##cross-references GB:M61132; NID:g192692; PIDN:AAA63295.1; !1PID:g192693 REFERENCE A32215 !$#authors Fingeroth, J.D.; Benedict, M.A.; Levy, D.N.; Strominger, !1J.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:242-246 !$#title Identification of murine complement receptor type 2. !$#cross-references MUID:89098890; PMID:2783485 !$#accession A32215 !'##molecule_type mRNA !'##residues 343-401;991-1025 ##label FI2 !'##cross-references GB:J04153 REFERENCE A45802 !$#authors Kurtz, C.B.; Paul, M.S.; Aegerter, M.; Weis, J.J.; Weis, !1J.H. !$#journal J. Immunol. (1989) 143:2058-2067 !$#title Murine complement receptor gene family. Identification and !1characterization of the murine homolog (Cr2) to human CR2 !1and its molecular linkage to Crry. !$#cross-references MUID:89381350; PMID:2528587 !$#accession A45802 !'##status preliminary !'##molecule_type mRNA !'##residues 'E',100-101,292-961,964-1025 ##label KUR !'##cross-references GB:M29281; NID:g192685; PIDN:AAA37447.1; !1PID:g387131 !'##note the authors failed to translate GGA for residue 421 as Gly, and !1CCA for residue 552 as Pro !'##note the authors translated the codon CAC for residue 727 as Asn CLASSIFICATION #superfamily complement C3d/Epstein-Barr virus receptor; !1complement factor H repeat homology KEYWORDS alternative splicing; duplication; glycoprotein; receptor; !1transmembrane protein FEATURE !$1-11 #domain signal sequence #status predicted #label SIG\ !$12-1025 #product complement C3d/Epstein-Barr virus receptor 2 !8(15-repeat form) #status predicted #label MAT1\ !$12-973 #domain extracellular #status predicted #label EXT\ !$14-73 #domain complement factor H repeat homology #label !8FH01\ !$82-138 #domain complement factor H repeat homology #label !8FH02\ !$146-202 #domain complement factor H repeat homology #label !8FH03\ !$207-263 #domain complement factor H repeat homology #label !8FH04\ !$268-334 #domain complement factor H repeat homology #label !8FH05\ !$343-398 #domain complement factor H repeat homology #label !8FH06\ !$402-458 #domain complement factor H repeat homology #label !8FH07\ !$463-514 #domain complement factor H repeat homology #label !8FH08\ !$519-585 #domain complement factor H repeat homology #label !8FH09\ !$594-649 #domain complement factor H repeat homology #label !8FH10\ !$654-704 #domain complement factor H repeat homology #label !8FH12\ !$709-769 #domain complement factor H repeat homology #label !8FH13\ !$778-833 #domain complement factor H repeat homology #label !8FH14\ !$841-897 #domain complement factor H repeat homology #label !8FH15\ !$902-958 #domain complement factor H repeat homology #label !8FH16\ !$968-989 #domain transmembrane #status predicted #label TMM\ !$990-1025 #domain intracellular #status predicted #label INT SUMMARY #length 1025 #molecular-weight 112994 #checksum 6190 SEQUENCE /// ENTRY NBHUC4 #type complete TITLE C4b-binding protein alpha chain precursor - human ALTERNATE_NAMES C4BP; proline-rich protein ORGANISM #formal_name Homo sapiens #common_name man DATE 13-Aug-1986 #sequence_revision 30-Jun-1993 #text_change 22-Jun-1999 ACCESSIONS A33568; S02372; A90326; A24182; A93134; S29492; A31785; !1I52244; A03210 REFERENCE A33568 !$#authors Matsuguchi, T.; Okamura, S.; Aso, T.; Sata, T.; Niho, Y. !$#journal Biochem. Biophys. Res. Commun. (1989) 165:138-144 !$#title Molecular cloning of the cDNA coding for proline-rich !1protein (PRP): identity of PRP as C4b-binding protein. !$#cross-references MUID:90073699; PMID:2590215 !$#accession A33568 !'##molecule_type mRNA !'##residues 1-597 ##label MA1 !'##cross-references GB:M31452; NID:g190501; PIDN:AAA36507.1; !1PID:g190502 !'##note the authors translated the codon GGA for residue 492 as Glu REFERENCE S02372 !$#authors Lintin, S.J.; Lewin, A.R.; Reid, K.B.M. !$#journal FEBS Lett. (1988) 232:328-332 !$#title Derivation of the sequence of the signal peptide in human !1C4b-binding protein and interspecies cross-hybridisation of !1the C4bp cDNA sequence. !$#cross-references MUID:88242821; PMID:3378624 !$#accession S02372 !'##molecule_type mRNA !'##residues 17-81 ##label LI2 !'##cross-references EMBL:X07853 !'##note although the sequence determined extends to residue 9 above, !1these authors assign Met-17 as the initiator REFERENCE A90326 !$#authors Chung, L.P.; Bentley, D.R.; Reid, K.B.M. !$#journal Biochem. J. (1985) 230:133-141 !$#title Molecular cloning and characterization of the cDNA coding !1for C4b-binding protein, a regulatory protein of the !1classical pathway of the human complement system. !$#cross-references MUID:86025405; PMID:3840370 !$#accession A90326 !'##molecule_type mRNA !'##residues 80-597 ##label CH2 !'##cross-references GB:X02865; NID:g29564; PIDN:CAA26617.1; PID:g29565 !'##note 92-Thr and 357-His were also found REFERENCE A24182 !$#authors Lintin, S.J.; Reid, K.B.M. !$#journal FEBS Lett. (1986) 204:77-81 !$#title Studies on the structure of the human C4b-binding protein !1gene. !$#cross-references MUID:86301119; PMID:3017751 !$#accession A24182 !'##molecule_type DNA !'##residues 203-288 ##label LIN !'##cross-references EMBL:X04284; EMBL:X04296 REFERENCE A43023 !$#authors Rodriguez de Cordoba, S.; Sanchez-Corral, P.; Rey-Campos, J. !$#journal J. Exp. Med. (1991) 173:1073-1082 !$#title Structure of the gene coding for the alpha polypeptide chain !1of the human complement component C4b-binding protein. !$#cross-references MUID:91217619; PMID:2022920 !$#contents annotation; exon-intron boundaries REFERENCE A93134 !$#authors Chung, L.P.; Gagnon, J.; Reid, K.B.M. !$#journal Mol. Immunol. (1985) 22:427-435 !$#title Amino acid sequence studies of human C4b-binding protein: !1N-terminal sequence analysis and alignment of the fragments !1produced by limited proteolysis with chymotrypsin and the !1peptides produced by cyanogen bromide treatment. !$#cross-references MUID:85296001; PMID:4033666 !$#accession A93134 !'##molecule_type protein !'##residues 49-81 ##label CH1 !'##note this paper reports amino-terminal sequences of the intact !1protein and of a number of proteolytic peptides REFERENCE S29492 !$#authors Hessing, M.; Kanters, D.; Takeya, H.; van't Veer, C.; !1Hackeng, T.M.; Iwanaga, S.; Bouma, B.N. !$#journal FEBS Lett. (1993) 317:228-232 !$#title The region Ser(333)-Arg(356) of the alpha-chain of human !1C4b-binding protein is involved in the binding of complement !1C4b. !$#cross-references MUID:93146164; PMID:8425609 !$#accession S29492 !'##status preliminary !'##molecule_type protein !'##residues 381-404 ##label HES REFERENCE A31785 !$#authors Suzuki, K.; Nishioka, J. !$#journal J. Biol. Chem. (1988) 263:17034-17039 !$#title Binding site for vitamin K-dependent protein S on complement !1C4b-binding protein. !$#cross-references MUID:89034204; PMID:2460456 !$#accession A31785 !'##molecule_type protein !'##residues 495-505,'X',507-510,'X',512-515 ##label SUZ !'##note this peptide appears to bind protein S REFERENCE A93950 !$#authors Dahlback, B.; Smith, C.A.; Muller-Eberhard, H.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:3461-3465 !$#title Visualization of human C4b-binding protein and its complexes !1with vitamin K-dependent protein S and complement protein !1C4b. !$#cross-references MUID:83221615; PMID:6222381 !$#contents annotation; electron microscopy; three-dimensional !1structure; ligand binding REFERENCE I52244 !$#authors Aso, T.; Okamura, S.; Matsuguchi, T.; Sakamoto, N.; Sata, !1T.; Niho, Y. !$#journal Biochem. Biophys. Res. Commun. (1991) 174:222-227 !$#title Genomic organization of the alpha chain of the human !1C4b-binding protein gene. !$#cross-references MUID:91113199; PMID:1989602 !$#accession I52244 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-597 ##label ASO !'##cross-references GB:M62486; NID:g190498; PIDN:AAA36506.1; !1PID:g190500 COMMENT C4BP controls the classical pathway of complement !1activation. It binds as a cofactor to C3b/C4b inactivator !1(C3bINA), which then hydrolyzes the complement fragment C4b. !1It also accelerates the degradation of the C4bC2a complex !1(C3 convertase) by dissociating the complement fragment C2a. COMMENT C4BP occurs in plasma in two forms, both of which bind !1complement fragment C4b. The prevalent higher molecular !1weight form contains 7 alpha chains and one beta chain, !1which are linked by disulfide bonds. The beta chain binds !1the vitamin K-dependent plasma protein S. A minor form lacks !1the beta chain. Bound protein S is inactive as a cofactor !1for protein C inactivation of coagulation factors V and !1VIII. COMMENT The molecule has a central body supporting seven tentacles !1(alpha chains), each with the binding site for C4b at the !1peripheral end. GENETICS !$#gene GDB:C4BPA !'##cross-references GDB:120568; OMIM:120830 !$#map_position 1q32-1q32 !$#introns 48/1; 110/1; 143/2; 172/1; 236/1; 297/1; 362/1; 425/1; 482/ !11; 540/3 COMPLEX octamer of seven alpha chains and one beta chain CLASSIFICATION #superfamily C4b-binding protein alpha chain; complement !1factor H repeat homology KEYWORDS acute phase; chylomicron; complement pathway; duplication; !1glycoprotein; plasma FEATURE !$1-48 #domain signal sequence #status predicted #label SIG\ !$49-597 #product C4b-binding protein alpha chain #status !8predicted #label MAT\ !$50-108 #domain complement factor H repeat homology #label !8FH1\ !$113-170 #domain complement factor H repeat homology #label !8FH2\ !$175-234 #domain complement factor H repeat homology #label !8FH3\ !$239-294 #domain complement factor H repeat homology #label !8FH4\ !$299-360 #domain complement factor H repeat homology #label !8FH5\ !$364-422 #domain complement factor H repeat homology #label !8FH6\ !$381-404 #region complement C4b binding #status predicted\ !$426-480 #domain complement factor H repeat homology #label !8FH7\ !$484-538 #domain complement factor H repeat homology #label !8FH8\ !$221,506,528 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 597 #molecular-weight 67033 #checksum 6374 SEQUENCE /// ENTRY I46001 #type complete TITLE C4b-binding protein alpha chain - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS I46001; S43190 REFERENCE I46001 !$#authors Hillarp, A.; Thern, A.; Dahlback, B. !$#journal J. Immunol. (1994) 153:4190-4199 !$#title Bovine C4b binding protein. Molecular cloning of the alpha- !1and beta-chains provides structural background for lack of !1complex formation with protein S. !$#cross-references MUID:95015909; PMID:7930621 !$#accession I46001 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-610 ##label HIL !'##cross-references EMBL:Z31693; NID:g469117; PIDN:CAA83498.1; !1PID:g469118 CLASSIFICATION #superfamily C4b-binding protein alpha chain; complement !1factor H repeat homology FEATURE !$50-107 #domain complement factor H repeat homology #label !8FH1\ !$112-169 #domain complement factor H repeat homology #label !8FH2\ !$174-234 #domain complement factor H repeat homology #label !8FH3\ !$239-294 #domain complement factor H repeat homology #label !8FH4\ !$299-362 #domain complement factor H repeat homology #label !8FH5\ !$366-425 #domain complement factor H repeat homology #label !8FH6\ !$429-483 #domain complement factor H repeat homology #label !8FHR\ !$487-541 #domain complement factor H repeat homology #label !8FH8 SUMMARY #length 610 #molecular-weight 68886 #checksum 2096 SEQUENCE /// ENTRY S53711 #type complete TITLE C4BP alpha chain precursor - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S53711 REFERENCE S53711 !$#authors de Frutos, P.G.; Dahlbaeck, B. !$#journal Biochim. Biophys. Acta (1995) 1261:285-289 !$#title cDNA structure of rabbit C4b-binding protein alpha-chain. !1Preserved sequence motive in complement regulatory protein !1modules which bind C4b. !$#cross-references MUID:95226458; PMID:7711074 !$#accession S53711 !'##status preliminary; nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-597 ##label DEF !'##cross-references EMBL:Z35490 CLASSIFICATION #superfamily C4b-binding protein alpha chain; complement !1factor H repeat homology FEATURE !$50-107 #domain complement factor H repeat homology #label !8FH1\ !$112-169 #domain complement factor H repeat homology #label !8FH2\ !$174-234 #domain complement factor H repeat homology #label !8FH3\ !$239-294 #domain complement factor H repeat homology #label !8FH4\ !$299-360 #domain complement factor H repeat homology #label !8FH5\ !$364-422 #domain complement factor H repeat homology #label !8FH6\ !$426-480 #domain complement factor H repeat homology #label !8FH7\ !$484-538 #domain complement factor H repeat homology #label !8FH8 SUMMARY #length 597 #molecular-weight 66130 #checksum 6473 SEQUENCE /// ENTRY A44247 #type complete TITLE C4b-binding protein alpha-chain homolog - pig ALTERNATE_NAMES apolipoprotein R ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A44247; JS0773 REFERENCE A44247 !$#authors Cooper, S.T.; Attie, A.D. !$#journal Biochemistry (1992) 31:12328-12336 !$#title Pig apolipoprotein R: a new member of the short consensus !1repeat family of proteins. !$#cross-references MUID:93099101; PMID:1463721 !$#accession A44247 !'##status preliminary !'##molecule_type mRNA; protein !'##residues 1-202 ##label COO !'##cross-references GB:L06820; NID:g164362; PIDN:AAA30994.1; !1PID:g164363 !'##experimental_source liver !'##note sequence inconsistent with the nucleotide translation !'##note sequence extracted from NCBI backbone (NCBIN:120912, !1NCBIP:120913) REFERENCE JS0773 !$#authors Cooper, S.T.; Attie, A.D. !$#submission submitted to JIPID, November 1992 !$#description Pig Apolipoprotein R, a new member of the short consensus !1repeat (SCR) family of proteins. !$#accession JS0773 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-202 ##label CO2 CLASSIFICATION #superfamily C4b-binding protein alpha chain; complement !1factor H repeat homology KEYWORDS lipid binding; lipoprotein FEATURE !$30-85 #domain complement factor H repeat homology #label !8FH1\ !$89-143 #domain complement factor H repeat homology #label !8FH2 SUMMARY #length 202 #molecular-weight 22724 #checksum 3207 SEQUENCE /// ENTRY NBMSC4 #type complete TITLE C4b-binding protein alpha chain precursor - mouse ALTERNATE_NAMES C4BP; proline-rich protein ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 18-Jul-1997 ACCESSIONS A27117 REFERENCE A27117 !$#authors Kristensen, T.; Ogata, R.T.; Chung, L.P.; Reid, K.B.M.; !1Tack, B.F. !$#journal Biochemistry (1987) 26:4668-4674 !$#title cDNA structure of murine C4b-binding protein, a regulatory !1component of the serum complement system. !$#cross-references MUID:88024997; PMID:3663616 !$#accession A27117 !'##molecule_type mRNA !'##residues 1-469 ##label KRI !'##note the authors translated the codon GCT for residue 25 as Val COMMENT C4BP controls the classical pathway of complement !1activation. It binds as a cofactor to C3b/C4b inactivator !1(C3bINA), which then hydrolyzes the complement fragment C4b. !1It also accelerates the degradation of the C4bC2a complex !1(C3 convertase) by dissociating the complement fragment C2a. COMMENT In mouse, C4BP is a multimeric protein of noncovalently !1associated chains. CLASSIFICATION #superfamily C4b-binding protein alpha chain; complement !1factor H repeat homology KEYWORDS acute phase; chylomicron; complement pathway; duplication; !1glycoprotein; plasma FEATURE !$1-56 #domain signal sequence #status predicted #label SIG\ !$57-469 #product C4b-binding protein alpha chain #status !8predicted #label MAT\ !$58-115 #domain complement factor H repeat homology #label !8FH1\ !$120-176 #domain complement factor H repeat homology #label !8FH2\ !$181-240 #domain complement factor H repeat homology #label !8FH3\ !$245-299 #domain complement factor H repeat homology #label !8FH4\ !$303-355 #domain complement factor H repeat homology #label !8FH5\ !$359-413 #domain complement factor H repeat homology #label !8FH6\ !$74,227,275,292,366, !$381,428 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 469 #molecular-weight 51523 #checksum 5359 SEQUENCE /// ENTRY WMBE1E #type complete TITLE secretory complement control protein homolog precursor - saimiriine herpesvirus 1 (strain 11) ALTERNATE_NAMES sCCPH protein ORGANISM #formal_name saimiriine herpesvirus 1 DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 01-Dec-2000 ACCESSIONS A42534; E36806; S24566 REFERENCE A42534 !$#authors Albrecht, J.C.; Fleckenstein, B. !$#journal J. Virol. (1992) 66:3937-3940 !$#title New member of the multigene family of complement control !1proteins in herpesvirus saimiri. !$#cross-references MUID:92260674; PMID:1316492 !$#accession A42534 !'##molecule_type DNA !'##residues 1-302 ##label ALB !'##cross-references EMBL:X60283; NID:g60315; PIDN:CAA42822.1; !1PID:g60316 GENETICS !$#introns 288/1 CLASSIFICATION #superfamily herpesvirus complement control protein; !1complement factor H repeat homology KEYWORDS alternative splicing; duplication; extracellular protein; !1glycoprotein FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-302 #product secretory complement control protein homolog !8#status predicted #label SCC\ !$23-79 #domain complement factor H repeat homology #label !8FH1\ !$84-142 #domain complement factor H repeat homology #label !8FH2\ !$147-205 #domain complement factor H repeat homology #label !8FH3\ !$210-264 #domain complement factor H repeat homology #label !8FH4\ !$36,39,46,72,155 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 302 #molecular-weight 33392 #checksum 5963 SEQUENCE /// ENTRY WMBE2E #type complete TITLE membrane-bound complement control protein homolog precursor - saimiriine herpesvirus 1 (strain 11) ALTERNATE_NAMES mCCPH protein ORGANISM #formal_name saimiriine herpesvirus 1 DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 22-Jun-1999 ACCESSIONS B42534; D36806; S24567 REFERENCE A42534 !$#authors Albrecht, J.C.; Fleckenstein, B. !$#journal J. Virol. (1992) 66:3937-3940 !$#title New member of the multigene family of complement control !1proteins in herpesvirus saimiri. !$#cross-references MUID:92260674; PMID:1316492 !$#accession B42534 !'##molecule_type DNA !'##residues 1-360 ##label ALB !'##cross-references EMBL:X60283; NID:g60315; PIDN:CAA42823.1; !1PID:g60317 CLASSIFICATION #superfamily herpesvirus complement control protein; !1complement factor H repeat homology KEYWORDS duplication; glycoprotein; transmembrane protein FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-302 #product membrane-bound complement control protein !8homolog #status predicted #label SCC\ !$23-79 #domain complement factor H repeat homology #label !8FH1\ !$84-142 #domain complement factor H repeat homology #label !8FH2\ !$147-205 #domain complement factor H repeat homology #label !8FH3\ !$210-264 #domain complement factor H repeat homology #label !8FH4\ !$329-345 #domain transmembrane #status predicted #label TMN\ !$36,39,46,72,155,294 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 360 #molecular-weight 40006 #checksum 6371 SEQUENCE /// ENTRY WMVZSP #type complete TITLE apolipoprotein H homolog precursor - vaccinia virus ALTERNATE_NAMES 35K secretory protein; C3L protein; virokine ORGANISM #formal_name vaccinia virus #note host Homo sapiens (man) DATE 31-Dec-1989 #sequence_revision 30-Jun-1990 #text_change 22-Jun-1999 ACCESSIONS A31005; B42504 REFERENCE A31005 !$#authors Kotwal, G.J.; Moss, B. !$#journal Nature (1988) 335:176-178 !$#title Vaccinia virus encodes a secretory polypeptide structurally !1related to complement control proteins. !$#cross-references MUID:88318974; PMID:3412473 !$#accession A31005 !'##molecule_type DNA !'##residues 1-263 ##label KOT !'##cross-references GB:X13166; NID:g60690; PIDN:CAA31564.1; PID:g60691 !'##experimental_source strain WR REFERENCE A42501 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:517-563 !$#title Appendix to "The complete DNA sequence of vaccinia virus". !$#accession B42504 !'##molecule_type DNA !'##residues 1-263 ##label GOE !'##cross-references GB:M35027; NID:g335317; PIDN:AAA47997.1; !1PID:g335345 !'##experimental_source strain Copenhagen REFERENCE A42531 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:247-266 !$#title The complete DNA sequence of vaccinia virus. !$#cross-references MUID:91021027; PMID:2219722 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given CLASSIFICATION #superfamily herpesvirus complement control protein; !1complement factor H repeat homology KEYWORDS duplication; extracellular protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-263 #product C4b-binding protein homolog #status !8predicted #label MAT\ !$21-81 #domain complement factor H repeat homology #label !8FH1\ !$86-143 #domain complement factor H repeat homology #label !8FH2\ !$148-201 #domain complement factor H repeat homology #label !8FH3\ !$206-261 #domain complement factor H repeat homology #label !8FH4 SUMMARY #length 263 #molecular-weight 28629 #checksum 8152 SEQUENCE /// ENTRY C36838 #type complete TITLE complement control protein homolog - variola virus (strain India-1967) ALTERNATE_NAMES D12L protein ORGANISM #formal_name variola virus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 23-Mar-2001 ACCESSIONS C36838 REFERENCE A36859 !$#authors Blinov, V.M. !$#submission submitted to GenBank, November 1992 !$#accession C36838 !'##molecule_type DNA !'##residues 1-263 ##label BLI !'##cross-references GB:X69198; NID:g456758; PIDN:CAA48953.1; !1PID:g297195 CLASSIFICATION #superfamily herpesvirus complement control protein; !1complement factor H repeat homology FEATURE !$21-81 #domain complement factor H repeat homology #label !8FH1\ !$86-143 #domain complement factor H repeat homology #label !8FH2\ !$148-201 #domain complement factor H repeat homology #label !8FH3\ !$206-261 #domain complement factor H repeat homology #label !8FH4 SUMMARY #length 263 #molecular-weight 28789 #checksum 8771 SEQUENCE /// ENTRY KFHU13 #type complete TITLE coagulation factor XIII chain b precursor - human ALTERNATE_NAMES fibrin-stabilizing factor; plasma transglutaminase b chain; protein-glutamine gamma-glutamyltransferase b chain ORGANISM #formal_name Homo sapiens #common_name man DATE 19-Apr-1991 #sequence_revision 26-May-1994 #text_change 22-Jun-1999 ACCESSIONS A36397; A23830; S09980 REFERENCE A36397 !$#authors Bottenus, R.E.; Ichinose, A.; Davie, E.W. !$#journal Biochemistry (1990) 29:11195-11209 !$#title Nucleotide sequence of the gene for the b subunit of human !1factor XIII. !$#cross-references MUID:91105054; PMID:2271707 !$#accession A36397 !'##molecule_type DNA !'##residues 1-661 ##label BOT !'##cross-references GB:J05294 REFERENCE A23830 !$#authors Ichinose, A.; McMullen, B.A.; Fujikawa, K.; Davie, E.W. !$#journal Biochemistry (1986) 25:4633-4638 !$#title Title: Amino acid sequence of the b subunit of human factor !1XIII, a protein composed of ten repetitive segments. !$#cross-references MUID:87026535; PMID:3021194 !$#accession A23830 !'##molecule_type mRNA !'##residues 2-661 ##label ICH !'##cross-references GB:M14057; NID:g182838; PIDN:AAA88042.1; !1PID:g182839 !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing REFERENCE S09980 !$#authors Grundmann, U.; Nerlich, C.; Rein, T.; Zettlmeissl, G. !$#journal Nucleic Acids Res. (1990) 18:2817-2818 !$#title Complete cDNA sequence encoding the B subunit of human !1factor XIII. !$#cross-references MUID:90251467; PMID:2339067 !$#accession S09980 !'##molecule_type mRNA !'##residues 1-661 ##label GRU !'##cross-references EMBL:X51823 COMMENT This protein is noncatalytic. GENETICS !$#gene GDB:F13B !'##cross-references GDB:119893; OMIM:134580 !$#map_position 1q31-1q32.1 !$#introns 2/1; 69/1; 131/1; 190/1; 249/1; 309/1; 371/1; 432/1; 499/1; !1560/1; 631/2 COMPLEX heterotetramer in plasma with coagulation factor XIII chain !1a, the plasma transglutaminase CLASSIFICATION #superfamily coagulation factor XIII chain b; complement !1factor H repeat homology KEYWORDS blood coagulation; duplication; glycoprotein; plasma FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-661 #product coagulation factor XIII chain b #status !8predicted #label MAT\ !$25-87 #domain complement factor H repeat homology #label !8FH01\ !$91-146 #domain complement factor H repeat homology #label !8FH02\ !$153-208 #domain complement factor H repeat homology #label !8FH03\ !$213-267 #domain complement factor H repeat homology #label !8FH04\ !$274-327 #domain complement factor H repeat homology #label !8FH05\ !$336-389 #domain complement factor H repeat homology #label !8FH06\ !$396-450 #domain complement factor H repeat homology #label !8FH07\ !$454-515 #domain complement factor H repeat homology #label !8FH08\ !$524-578 #domain complement factor H repeat homology #label !8FH09\ !$582-646 #domain complement factor H repeat homology #label !8FH10\ !$617-619 #region cell attachment (R-G-D) motif\ !$25-76,59-87,91-135, !$118-146,153-197, !$180-208,213-255, !$241-267,274-316, !$302-327,336-378, !$364-389,396-439, !$425-450,454-505, !$486-515,524-567, !$553-578,582-636, !$616-646 #disulfide_bonds #status predicted\ !$162,545 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 661 #molecular-weight 75491 #checksum 7401 SEQUENCE /// ENTRY NBHU #type complete TITLE apolipoprotein H precursor [validated] - human ALTERNATE_NAMES activated protein C-binding protein; anticardiolipin cofactor; beta-2-glycoprotein I ORGANISM #formal_name Homo sapiens #common_name man DATE 17-May-1985 #sequence_revision 30-Jun-1993 #text_change 08-Dec-2000 ACCESSIONS S17178; S17668; JQ1379; B43286; A03209; A35786; A46464; !1I54745; S15499; S20110 REFERENCE S17178 !$#authors Steinkasserer, A.; Estaller, C.; Weiss, E.H.; Sim, R.B.; !1Day, A.J. !$#journal Biochem. J. (1991) 277:387-391 !$#title Complete nucleotide and deduced amino acid sequence of human !1beta(2)-glycoprotein I. !$#cross-references MUID:91315408; PMID:1650181 !$#accession S17178 !'##molecule_type mRNA !'##residues 1-345 ##label STE !'##cross-references EMBL:X58100; NID:g28809; PIDN:CAA41113.1; !1PID:g28810 REFERENCE S17668 !$#authors Kristensen, T.; Schousboe, I.; Boel, E.; Mulvihill, E.M.; !1Rosendahl Hansen, R.; Bach Moller, K.; Hundahl Moller, N.P.; !1Sottrup-Jensen, L. !$#journal FEBS Lett. (1991) 289:183-186 !$#title Molecular cloning and mammalian expression of human beta !1(2)-glycoprotein I cDNA. !$#cross-references MUID:92008618; PMID:1655523 !$#accession S17668 !'##molecule_type mRNA !'##residues 1-345 ##label KRI !'##cross-references EMBL:X53595; NID:g28811; PIDN:CAA37664.1; !1PID:g28812 REFERENCE JQ1379 !$#authors Mehdi, H.; Nunn, M.; Steel, D.M.; Whitehead, A.S.; Perez, !1M.; Walker, L.; Peeples, M.E. !$#journal Gene (1991) 108:293-298 !$#title Nucleotide sequence and expression of the human gene !1encoding apolipoprotein H (beta2-glycoprotein I). !$#cross-references MUID:92084151; PMID:1748314 !$#accession JQ1379 !'##molecule_type mRNA !'##residues 1-265,'V',267-345 ##label MEH !'##cross-references EMBL:X57847; NID:g28813; PIDN:CAA40977.1; !1PID:g28814 !'##experimental_source liver REFERENCE A43286 !$#authors Nonaka, M.; Matsuda, Y.; Shiroishi, T.; Moriwaki, K.; !1Nonaka, M.; Natsuume-Sakai, S. !$#journal Genomics (1992) 13:1082-1087 !$#title Molecular cloning of mouse beta-2-glycoprotein I and mapping !1of the gene to chromosome 11. !$#cross-references MUID:92372000; PMID:1339387 !$#accession B43286 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-265,'V',267-345 ##label NON REFERENCE A03209 !$#authors Lozier, J.; Takahashi, N.; Putnam, F.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:3640-3644 !$#title Complete amino acid sequence of human plasma !1beta2-glycoprotein I. !$#cross-references MUID:84222015; PMID:6587378 !$#accession A03209 !'##molecule_type protein !'##residues 20-120,'C',122-187,'N',189-265,'V',267-345 ##label LOZ REFERENCE A35786 !$#authors McNeil, H.P.; Simpson, R.J.; Chesterman, C.N.; Krilis, S.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:4120-4124 !$#title Anti-phospholipid antibodies are directed against a complex !1antigen that includes a lipid-binding inhibitor of !1coagulation: beta-2-glycoprotein I (apolipoprotein H). !$#cross-references MUID:90272666; PMID:2349221 !$#accession A35786 !'##molecule_type protein !'##residues 20-22,'X',24-37,'X',39-43 ##label MCN REFERENCE A46464 !$#authors Matsuura, E.; Igarashi, Y.; Fujimoto, M.; Ichikawa, K.; !1Suzuki, T.; Sumida, T.; Yasuda, T.; Koike, T. !$#journal J. Immunol. (1992) 148:3885-3891 !$#title Heterogeneity of anticardiolipin antibodies defined by the !1anticardiolipin cofactor. !$#cross-references MUID:92291509; PMID:1602135 !$#accession A46464 !'##molecule_type protein !'##residues 20-44 ##label MA2 !'##note sequence extracted from NCBI backbone (NCBIP:105524) REFERENCE I54745 !$#authors Matsuura, E.; Igarashi, M.; Igarashi, Y.; Nagae, H.; !1Ichikawa, K.; Yasuda, T.; Koike, T. !$#journal Int. Immunol. (1991) 3:1217-1221 !$#title Molecular definition of human beta 2-glycoprotein I (beta !12-GPI) by cDNA cloning and inter-species differences of beta !12-GPI in alternation of anticardiolipin binding. !$#cross-references MUID:92135065; PMID:1777418 !$#accession I54745 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-265,'V',267-345 ##label RES !'##cross-references GB:S80305; NID:g244677; PIDN:AAB21330.1; !1PID:g244678 COMMENT This plasma glycoprotein is a constituent of chylomicrons, !1VLDL, and HDL. It binds to lipoproteins, anionic !1phospholipids, platelets, heparin, DNA, and mitochondria. It !1inhibits the intrinsic blood coagulation cascade and !1ADP-mediated platelet aggregation. COMMENT The physiological role of this protein is uncertain. It may !1diminish unwanted activation of blood coagulation by binding !1and neutralizing negatively charged macromolecules. GENETICS !$#gene GDB:APOH !'##cross-references GDB:118887; OMIM:138700 !$#map_position 17q23-17qter CLASSIFICATION #superfamily apolipoprotein H; complement factor H repeat !1homology KEYWORDS chylomicron; duplication; glycoprotein; HDL; heparin !1binding; lipid binding; monomer; plasma; polymorphism; VLDL FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-345 #product apolipoprotein H #status experimental #label !8MAT\ !$23-79 #domain complement factor H repeat homology #label !8FH1\ !$84-137 #domain complement factor H repeat homology #label !8FH2\ !$142-200 #domain complement factor H repeat homology #label !8FH3\ !$205-260 #domain complement factor H repeat homology #label !8FH4\ !$264-325 #domain complement factor H repeat homology #label !8FH5\ !$23-66,51-79, !$110-137,174-200, !$205-248,300-307 #disulfide_bonds #status experimental\ !$84-124,142-188, !$234-260,264-315, !$325-345 #disulfide_bonds #status predicted\ !$162,183,193,253 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 345 #molecular-weight 38312 #checksum 1754 SEQUENCE /// ENTRY NBBO #type complete TITLE apolipoprotein H precursor - bovine ALTERNATE_NAMES beta-2-glycoprotein I; heparin-binding protein, 46K ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Jun-1993 #sequence_revision 19-May-1995 #text_change 21-Jul-2000 ACCESSIONS JN0502; PN0465; S23597; A43209; A39300; S09032 REFERENCE JN0502 !$#authors Gao, B.; Virmani, M.; Romm, E.; Lazar-Wesley, E.; Sakaguchi, !1K.; Appela, E.; Kunos, G.; Takacs, L. !$#journal Gene (1993) 126:287-288 !$#title Sequence of a cDNA encoding bovine apolipoprotein H. !$#cross-references MUID:93246260; PMID:8482546 !$#accession JN0502 !'##molecule_type mRNA !'##residues 1-100,'G',102-107,'S',109-176,'R',178-193,'C',195-258,'N', !1260-301,'N',303-304,'R',306-328,'R',330-345 ##label GAO !'##cross-references GB:L07303; NID:g162679; PIDN:AAA30382.1; !1PID:g162680 !$#accession PN0465 !'##molecule_type protein !'##residues 20-49 ##label GA1 REFERENCE S23597 !$#authors Bendixen, E.; Halkier, T.; Magnusson, S.; Sottrup-Jensen, !1L.; Kristensen, T. !$#journal Biochemistry (1992) 31:3611-3617 !$#title Complete primary structure of bovine beta(2)-glycoprotein I: !1localization of the disulfide bridges. !$#cross-references MUID:92232647; PMID:1567819 !$#accession S23597 !'##molecule_type mRNA !'##residues 4-345 ##label BE2 !'##cross-references EMBL:X60065; NID:g5; PIDN:CAA42669.1; PID:g6 !$#accession A43209 !'##molecule_type protein !'##residues !120-58;63-100;108-110;124-145;150-163;174-201;203-217; !1228-253,'X',255-256,'M',258-265;271-279;299-325;337-345 !1##label BE3 !'##note 186-Glu was also found REFERENCE A39300 !$#authors Kato, H.; Enjyoji, K. !$#journal Biochemistry (1991) 30:11687-11694 !$#title Amino acid sequence and location of the disulfide bonds in !1bovine beta2 glycoprotein I: the presence of five sushi !1domains. !$#cross-references MUID:92089075; PMID:1751487 !$#accession A39300 !'##molecule_type protein !'##residues 20-301,'N',303-345 ##label KAT REFERENCE S09032 !$#authors Li, Q.; Blacher, R.; Esch, F.; Congote, L.F. !$#journal Biochem. J. (1990) 267:261-264 !$#title Isolation from fetal bovine serum of an !1apolipoprotein-H-like protein which inhibits thymidine !1incorporation in fetal calf erythroid cells. !$#cross-references MUID:90226328; PMID:2327984 !$#accession S09032 !'##molecule_type protein !'##residues 20-22,'X',24-41 ##label LIQ COMMENT This plasma glycoprotein is a constituent of chylomicrons, !1VLDL, and HDL and may be an activator of lipoprotein lipase. !1It binds specifically to platelet membranes, modulates !1adenylate cyclase activity, and binds heparin. It may !1prevent activation of the intrinsic blood coagulation !1cascade by binding to phospholipids on the surface of !1damaged cells. CLASSIFICATION #superfamily apolipoprotein H; complement factor H repeat !1homology KEYWORDS chylomicron; duplication; glycoprotein; HDL; heparin !1binding; lipid binding; monomer; plasma; VLDL FEATURE !$1-19 #domain signal sequence (fragment) #status predicted !8#label SIG\ !$20-345 #product apolipoprotein H #status experimental #label !8MAT\ !$23-79 #domain complement factor H repeat homology #label !8FH1\ !$84-137 #domain complement factor H repeat homology #label !8FH2\ !$142-200 #domain complement factor H repeat homology #label !8FH3\ !$205-260 #domain complement factor H repeat homology #label !8FH4\ !$264-325 #domain complement factor H repeat homology #label !8FH5\ !$23-66,51-79,84-124, !$110-137,142-188, !$174-200,205-248, !$234-260,264-315, !$300-325,307-345 #disulfide_bonds #status experimental\ !$92,162,183,193,253 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 345 #molecular-weight 38252 #checksum 9783 SEQUENCE /// ENTRY JN0465 #type complete TITLE apolipoprotein H precursor - dog ALTERNATE_NAMES beta 2 glycoprotein I ORGANISM #formal_name Canis lupus familiaris #common_name dog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JN0465; S32693 REFERENCE JN0465 !$#authors Sellar, G.C.; Keane, J.; Mehdi, H.; Peeples, M.E.; Browne, !1N.; Whitehead, A.S. !$#journal Biochem. Biophys. Res. Commun. (1993) 191:1288-1293 !$#title Characterization and acute phase modulation of canine !1apolipoprotein H (beta2-glycoprotein I). !$#cross-references MUID:93221500; PMID:7682067 !$#accession JN0465 !'##molecule_type mRNA !'##residues 1-345 ##label SEL !'##cross-references EMBL:X72933; NID:g296088; PIDN:CAA51438.1; !1PID:g296089 !'##experimental_source liver COMMENT This plasma glycoprotein is a constituent of chylomicrons, !1VLDL, and HDL. It binds to lipoproteins, anionic !1phospholipids, platelets, heparin, DNA, and mitochondria. It !1inhibits the intrinsic blood coagulation cascade and !1ADP-mediated platelet aggregation. CLASSIFICATION #superfamily apolipoprotein H; complement factor H repeat !1homology KEYWORDS chylomicron; duplication; glycoprotein; HDL; heparin !1binding; lipid binding; lipoprotein; monomer; plasma; VLDL FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-345 #product apolipoprotein H #status predicted #label !8MAT\ !$23-79 #domain complement factor H repeat homology #label !8FH1\ !$84-137 #domain complement factor H repeat homology #label !8FH2\ !$142-200 #domain complement factor H repeat homology #label !8FH3\ !$205-260 #domain complement factor H repeat homology #label !8FH4\ !$264-325 #domain complement factor H repeat homology #label !8FH5\ !$301-306 #region phospholipid binding #status predicted\ !$23-66,51-79,84-124, !$110-137,142-188, !$174-200,205-248, !$234-260,264-315, !$300-307,325-345 #disulfide_bonds #status predicted\ !$117,162,183,193,253 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 345 #molecular-weight 38403 #checksum 100 SEQUENCE /// ENTRY NBRT #type complete TITLE apolipoprotein H precursor - rat ALTERNATE_NAMES beta-2-glycoprotein I ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 22-Jun-1999 ACCESSIONS S05310 REFERENCE S05310 !$#authors Aoyama, Y.; Chan, Y.L.; Wool, I.G. !$#journal Nucleic Acids Res. (1989) 17:6401 !$#title The primary structure of rat beta(2)-glycoprotein I. !$#cross-references MUID:89366680; PMID:2771654 !$#accession S05310 !'##molecule_type mRNA !'##residues 1-297 ##label AOY !'##cross-references EMBL:X15551; NID:g57524; PIDN:CAA33556.1; !1PID:g57525 !'##note the authors translated the codon CAA for residue 148 as Glu and !1GAA for residue 151 as Gln COMMENT This plasma glycoprotein is a constituent of chylomicrons, !1VLDL, and HDL and may be an activator of lipoprotein lipase. !1It binds specifically to platelet membranes, modulates !1adenylate cyclase activity, and binds heparin. It may !1prevent activation of the intrinsic blood coagulation !1cascade by binding to phospholipids on the surface of !1damaged cells. CLASSIFICATION #superfamily apolipoprotein H; complement factor H repeat !1homology KEYWORDS chylomicron; duplication; glycoprotein; HDL; heparin !1binding; lipid binding; plasma; VLDL FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-297 #product apolipoprotein H #status predicted #label !8MAT\ !$36-89 #domain complement factor H repeat homology #label !8FH1\ !$94-152 #domain complement factor H repeat homology #label !8FH2\ !$157-212 #domain complement factor H repeat homology #label !8FH3\ !$216-277 #domain complement factor H repeat homology #label !8FH4\ !$36-76,62-89,94-140, !$126-152,157-200, !$186-212,216-267, !$252-259,277-297 #disulfide_bonds #status predicted\ !$114,135,145,205 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 297 #molecular-weight 33197 #checksum 7513 SEQUENCE /// ENTRY NBMS #type complete TITLE apolipoprotein H precursor - mouse ALTERNATE_NAMES 50K serum glycoprotein; activated protein C-binding protein; beta-2-glycoprotein I ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 28-May-1999 ACCESSIONS A43286; JC2243 REFERENCE A43286 !$#authors Nonaka, M.; Matsuda, Y.; Shiroishi, T.; Moriwaki, K.; !1Nonaka, M.; Natsuume-Sakai, S. !$#journal Genomics (1992) 13:1082-1087 !$#title Molecular cloning of mouse beta-2-glycoprotein I and mapping !1of the gene to chromosome 11. !$#cross-references MUID:92372000; PMID:1339387 !$#accession A43286 !'##molecule_type mRNA !'##residues 1-252,'A',254-277,'N',279-345 ##label NON !'##cross-references GB:D10056 !'##note the authors translated the codon ACT for residue 253 as Ala and !1ATG for residue 278 as Asn !'##note sequence extracted from NCBI backbone (NCBIN:111791, !1NCBIP:111794) and corrected to correspond with the !1nucleotide translation REFERENCE JC2243 !$#authors Sellar, G.C.; Steel, D.M.; Zafiropoulos, A.; Seery, L.T.; !1Whitehead, A.S. !$#journal Biochem. Biophys. Res. Commun. (1994) 200:1521-1528 !$#title Characterization, expression and evolution of mouse !1beta2-glycoprotein I (apolipoprotein H). !$#cross-references MUID:94242017; PMID:7514402 !$#accession JC2243 !'##molecule_type mRNA !'##residues 1-251,'R',253-345 ##label SEL !'##cross-references GB:S70439; NID:g546780; PIDN:AAB30789.1; !1PID:g546781 !'##experimental_source liver GENETICS !$#gene B2gp1 !$#map_position 11 CLASSIFICATION #superfamily apolipoprotein H; complement factor H repeat !1homology KEYWORDS chylomicron; duplication; glycoprotein; HDL; heparin !1binding; lipid binding; monomer; plasma; VLDL FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-345 #product apolipoprotein H #status predicted #label !8MAT\ !$23-79 #domain complement factor H repeat homology #label !8FH1\ !$84-137 #domain complement factor H repeat homology #label !8FH2\ !$142-200 #domain complement factor H repeat homology #label !8FH3\ !$205-260 #domain complement factor H repeat homology #label !8FH4\ !$264-325 #domain complement factor H repeat homology #label !8FH5\ !$23-66,51-79,84-124, !$110-137,142-188, !$174-200,205-248, !$234-260,264-315, !$300-307,325-345 #disulfide_bonds #status predicted\ !$105,117,162,183,193 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 345 #molecular-weight 38618 #checksum 2016 SEQUENCE /// ENTRY B26359 #type complete TITLE decay-accelerating factor, GPI-anchored splice form precursor - human ALTERNATE_NAMES CD55; DAF splice form 2; decay-accelerating factor membrane-bound form ORGANISM #formal_name Homo sapiens #common_name man DATE 05-Oct-1988 #sequence_revision 16-Aug-1996 #text_change 19-Jan-2001 ACCESSIONS B26359; A27666; A39101; I52594; I52564 REFERENCE A26359 !$#authors Caras, I.W.; Davitz, M.A.; Rhee, L.; Weddell, G.; Martin !1Jr., D.W.; Nussenzweig, V. !$#journal Nature (1987) 325:545-549 !$#title Cloning of decay-accelerating factor suggests novel use of !1splicing to generate two proteins. !$#cross-references MUID:87115845; PMID:2433596 !$#accession B26359 !'##molecule_type mRNA !'##residues 1-381 ##label CAR !'##cross-references GB:M30142; NID:g181464; PIDN:AAA52168.1; !1PID:g181465 REFERENCE A27666 !$#authors Medof, M.E.; Lublin, D.M.; Holers, V.M.; Ayers, D.J.; Getty, !1R.R.; Leykam, J.F.; Atkinson, J.P.; Tykocinski, M.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:2007-2011 !$#title Cloning and characterization of cDNAs encoding the complete !1sequence of decay-accelerating factor of human complement. !$#cross-references MUID:87175602; PMID:2436222 !$#accession A27666 !'##molecule_type mRNA !'##residues 6-79,'T',81-84,'M',86-381 ##label MED !'##cross-references GB:M15799; NID:g181462; PIDN:AAA52167.1; !1PID:g181463 REFERENCE A39101 !$#authors Moran, P.; Raab, H.; Kohr, W.J.; Caras, I.W. !$#journal J. Biol. Chem. (1991) 266:1250-1257 !$#title Glycophospholipid membrane anchor attachment. Molecular !1analysis of the cleavage/attachment site. !$#cross-references MUID:91093238; PMID:1824699 !$#accession A39101 !'##molecule_type protein !'##residues 338-352 ##label MOR REFERENCE I52594 !$#authors Lublin, D.M.; Mallinson, G.; Poole, J.; Reid, M.E.; !1Thompson, E.S.; Ferdman, B.R.; Telen, M.J.; Anstee, D.J.; !1Tanner, M.J. !$#journal Blood (1994) 84:1276-1282 !$#title Molecular basis of reduced or absent expression of !1decay-accelerating factor in Cromer blood group phenotypes. !$#cross-references MUID:94325573; PMID:7519480 !$#accession I52594 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 194-198,'L',200-209 ##label LUB !'##cross-references GB:S72858; NID:g639599; PIDN:AAC60633.1; !1PID:g639600 !'##experimental_source individual KW, Cromer blood group phenotype Dr !1(a-) !'##note the single nucleotide difference in this allele, which changes !1Ser-199 to Leu, leads also to use of a downstream cryptic !1splice acceptor side with a reading frame shift and !1premature stop codon (see reference I52564), and thus !1reduced DAF expression REFERENCE I52564 !$#authors Reid, M.E.; Mallinson, G.; Sim, R.B.; Poole, J.; Pausch, V.; !1Merry, A.H.; Liew, Y.W.; Tanner, M.J. !$#journal Blood (1991) 78:3291-3297 !$#title Biochemical studies on red blood cells from a patient with !1the Inab phenotype (decay-accelerating factor deficiency). !$#cross-references MUID:92075980; PMID:1720702 !$#accession I52564 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 190-193,'QLCPVE' ##label RE2 !'##cross-references GB:S70688; NID:g240301; PIDN:AAB20576.1; !1PID:g240302 !'##experimental_source individual KW, Cromer blood group phenotype Dr !1(a-) (described incorrectly as phenotype Inab in this paper. !1see reference I52594) COMMENT Cromer blood group system antigens reside on this protein. COMMENT For an alternative splice form, see PIR:A26359. GENETICS !$#gene GDB:DAF !'##cross-references GDB:119088; OMIM:125240 !$#map_position 1q32-1q32 FUNCTION !$#description protects tissues from damage by regulating complement !1activation on cell surfaces at the C3 convertase step CLASSIFICATION #superfamily decay-accelerating factor; complement factor H !1repeat homology KEYWORDS alternative splicing; blocked carboxyl end; complement !1inhibitor; glycoprotein; lipoprotein; phosphatidylinositol !1linkage; phosphoprotein FEATURE !$1-34 #domain signal sequence #status predicted #label SIG\ !$35-353 #product decay-accelerating factor 2 #status !8predicted #label MAT\ !$36-94 #domain complement factor H repeat homology #label !8FH01\ !$98-158 #domain complement factor H repeat homology #label !8FH02\ !$163-220 #domain complement factor H repeat homology #label !8FH03\ !$225-283 #domain complement factor H repeat homology #label !8FH04\ !$354-381 #domain carboxyl-terminal propeptide #status !8predicted #label PRO\ !$95 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$353 #modified_site GPI-anchor ethanolamine amidated !8carboxyl end (Ser) (in mature form) #status predicted SUMMARY #length 381 #molecular-weight 41400 #checksum 4027 SEQUENCE /// ENTRY NBHUC8 #type complete TITLE decorin precursor - human ALTERNATE_NAMES cartilage proteoglycan protein II; DS-PG II; PG40 core protein; proteoglycan 38K core protein ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 21-Jan-2000 ACCESSIONS A45016; A45015; B45015; A26476; S05640 REFERENCE A45016 !$#authors Vetter, U.; Vogel, W.; Just, W.; Young, M.F.; Fisher, L.W. !$#journal Genomics (1993) 15:161-168 !$#title Human decorin gene: intron-exon junctions and chromosomal !1localization. !$#cross-references MUID:93162643; PMID:8432527 !$#accession A45016 !'##molecule_type DNA !'##residues 1-359 ##label VET !'##cross-references GB:L01125; GB:L01126; GB:L01127; GB:L01128; !1GB:L01129; GB:L01130; GB:L01131 !'##note sequence extracted from NCBI backbone (NCBIP:125061) REFERENCE A45015 !$#authors Danielson, K.G.; Fazzio, A.; Cohen, I.; Cannizzaro, L.A.; !1Eichstetter, I.; Iozzo, R.V. !$#journal Genomics (1993) 15:146-160 !$#title The human decorin gene: intron-exon organization, discovery !1of two alternatively spliced exons in the 5' untranslated !1region, and mapping of the gene to chromosome 12q23. !$#cross-references MUID:93162642; PMID:8432526 !$#accession A45015 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 28-70 ##label DA2 !'##cross-references GB:M98262 !'##note sequence extracted from NCBI backbone (NCBIP:125013) !$#accession B45015 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 296-359 ##label DAN !'##note sequence extracted from NCBI backbone (NCBIP:125017) REFERENCE A26476 !$#authors Krusius, T.; Ruoslahti, E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:7683-7687 !$#title Primary structure of an extracellular matrix proteoglycan !1core protein deduced from cloned cDNA. !$#cross-references MUID:87017013; PMID:3484330 !$#accession A26476 !'##molecule_type mRNA !'##residues 1-359 ##label KRU !'##cross-references GB:M14219; NID:g181169; PIDN:AAB00774.1; !1PID:g181170 REFERENCE S05639 !$#authors Roughley, P.J.; White, R.J. !$#journal Biochem. J. (1989) 262:823-827 !$#title Dermatan sulphate proteoglycans of human articular !1cartilage. The properties of dermatan sulphate proteoglycans !1I and II. !$#cross-references MUID:90073579; PMID:2590169 !$#accession S05640 !'##molecule_type protein !'##residues 31-33,'X',35-50 ##label ROU COMMENT This protein binds type I collagen. GENETICS !$#gene GDB:DCN !'##cross-references GDB:119839; OMIM:125255 !$#map_position 12q21.3-12q23 !$#introns 71/1; 108/3; 180/1; 218/1; 249/2; 295/3 !$#note the first two introns occur before the initiator codon CLASSIFICATION #superfamily decorin; leucine-rich alpha-2-glycoprotein !1repeat homology; proteoglycan amino-terminal homology; !1proteoglycan carboxyl-terminal homology KEYWORDS chondroitin sulfate proteoglycan; collagen binding; dermatan !1sulfate; duplication; extracellular matrix; fibroblast; !1glycoprotein; tandem repeat FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-30 #domain propeptide #status predicted #label PRO\ !$31-359 #product decorin #status predicted #label MPT\ !$48-72 #domain proteoglycan amino-terminal homology #label !8PAH\ !$82-105 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR1\ !$106-129 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR2\ !$130-150 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR3\ !$151-174 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR4\ !$175-200 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR5\ !$201-221 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR6\ !$222-245 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR7\ !$246-269 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR8\ !$270-292 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR9\ !$293-316 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR10\ !$308-359 #domain proteoglycan carboxyl-terminal homology !8#label PRC\ !$34 #binding_site dermatan sulfate (Ser) (covalent) !8#status experimental\ !$189,325 #binding_site dermatan sulfate (Ser) (covalent) !8#status predicted\ !$211,262,303 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 359 #molecular-weight 39746 #checksum 835 SEQUENCE /// ENTRY BGHUN #type complete TITLE biglycan precursor - human ALTERNATE_NAMES cartilage proteoglycan I; dermatan sulfate proteoglycan I (DS-PGI); proteoglycan I core protein (PG-I) ORGANISM #formal_name Homo sapiens #common_name man DATE 21-Apr-1992 #sequence_revision 26-May-1995 #text_change 28-Jan-2000 ACCESSIONS A40757; I38706; A32458; S14349; S05639; A28457 REFERENCE A40757 !$#authors Fisher, L.W.; Heegaard, A.M.; Vetter, U.; Vogel, W.; Just, !1W.; Termine, J.D.; Young, M.F. !$#journal J. Biol. Chem. (1991) 266:14371-14377 !$#title Human biglycan gene. Putative promoter, intron-exon !1junctions, and chromosomal localization. !$#cross-references MUID:91317791; PMID:1860845 !$#accession A40757 !'##molecule_type DNA !'##residues 1-368 ##label FIS1 !'##cross-references GB:M65151; NID:g179428; GB:M65152; NID:g179429; !1GB:M65153; NID:g179430 !'##note the translated sequence in GenBank entry HUMBGN3, release !1113.0, (PIDN:AAA52287.1; PID:g179433) differs from the !1published sequence in having 139-Asn, 140-Val (residues !1present in the mRNA and not the DNA) and 26 residues !1inserted after residue 80 (apparently from a misread !1splicing) REFERENCE I38706 !$#authors Just, W.; Rau, W.; Muller, R.; Geerkens, C.; Vogel, W. !$#journal Hum. Mol. Genet. (1994) 3:2268 !$#title Dinucleotide repeat polymorphism at the human biglycan (BGN) !1locus. !$#cross-references MUID:95187185; PMID:7881444 !$#accession I38706 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 361-368 ##label JUS !'##cross-references EMBL:U11686; NID:g607862; PIDN:AAC50117.1; !1PID:g619663 REFERENCE A32458 !$#authors Fisher, L.W.; Termine, J.D.; Young, M.F. !$#journal J. Biol. Chem. (1989) 264:4571-4576 !$#title Deduced protein sequence of bone small proteoglycan I !1(Biglycan) shows homology with proteoglycan II (Decorin) and !1several nonconnective tissue proteins in a variety of !1species. !$#cross-references MUID:89174714; PMID:2647739 !$#accession A32458 !'##molecule_type mRNA !'##residues 1-138,'NV',141-162,'DV',165-368 ##label FIS2 !'##cross-references GB:J04599; NID:g184339 !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing !'##note the translated sequence in GenBank entry HUMHPGI, release !1113.0, (PIDN:AAA36009.1; PID:g306884) differs from the !1published sequence in having 139-Lys, 140-Leu, 163-Glu, and !1164-Leu REFERENCE S14349 !$#authors Stoecker, G.; Meyer, H.E.; Wagener, C.; Greiling, H. !$#journal Biochem. J. (1991) 274:415-420 !$#title Purification and N-terminal amino acid sequence of a !1chondroitin sulphate/dermatan sulphate proteoglycan isolated !1from intima/media preparations of human aorta. !$#cross-references MUID:91174749; PMID:1848758 !$#accession S14349 !'##molecule_type protein !'##residues 38-57 ##label STO !'##experimental_source aorta REFERENCE S05639 !$#authors Roughley, P.J.; White, R.J. !$#journal Biochem. J. (1989) 262:823-827 !$#title Dermatan sulphate proteoglycans of human articular !1cartilage. The properties of dermatan sulphate proteoglycans !1I and II. !$#cross-references MUID:90073579; PMID:2590169 !$#accession S05639 !'##molecule_type protein !'##residues 38-41,'X',43-46,'X',48-57 ##label ROU REFERENCE A92656 !$#authors Fisher, L.W.; Hawkins, G.R.; Tuross, N.; Termine, J.D. !$#journal J. Biol. Chem. (1987) 262:9702-9708 !$#title Purification and partial characterization of small !1proteoglycans I and II, bone sialoproteins I and II, and !1osteonectin from the mineral compartment of developing human !1bone. !$#cross-references MUID:87250639; PMID:3597437 !$#accession A28457 !'##molecule_type protein !'##residues 38-41,'X',43-62,'X',64-66 ##label FIS3 !'##experimental_source bone GENETICS !$#gene GDB:BGN !'##cross-references GDB:119727; OMIM:301870 !$#map_position Xq28-Xq28 !$#introns 80/1; 117/3; 189/1; 226/1; 257/2; 303/3 CLASSIFICATION #superfamily decorin; leucine-rich alpha-2-glycoprotein !1repeat homology; proteoglycan amino-terminal homology; !1proteoglycan carboxyl-terminal homology KEYWORDS chondroitin sulfate proteoglycan; dermatan sulfate; !1duplication; extracellular matrix; glycoprotein; tandem !1repeat FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-37 #domain propeptide #status predicted #label PRO\ !$38-368 #product biglycan #status predicted #label MAT\ !$57-81 #domain proteoglycan amino-terminal homology #label !8PAH\ !$91-114 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR1\ !$115-138 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR2\ !$139-159 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR3\ !$160-183 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR4\ !$184-207 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR5\ !$209-229 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR6\ !$230-253 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR7\ !$254-277 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR8\ !$278-300 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR9\ !$301-315 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #status atypical #label LR10\ !$316-368 #domain proteoglycan carboxyl-terminal homology !8#label PCH\ !$42,47 #binding_site dermatan sulfate (Ser) (covalent) !8#status experimental\ !$180,198 #binding_site dermatan sulfate (Ser) (covalent) !8#status predicted\ !$270,311 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 368 #molecular-weight 41654 #checksum 1684 SEQUENCE /// ENTRY NBHUA2 #type complete TITLE leucine-rich alpha-2-glycoprotein - human ORGANISM #formal_name Homo sapiens #common_name man DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 05-Dec-1998 ACCESSIONS A03211 REFERENCE A03211 !$#authors Takahashi, N.; Takahashi, Y.; Putnam, F.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:1906-1910 !$#title Periodicity of leucine and tandem repetition of a 24-amino !1acid segment in the primary structure of leucine-rich !1alpha-2-glycoprotein of human serum. !$#cross-references MUID:85166241; PMID:3856868 !$#accession A03211 !'##molecule_type protein !'##residues 1-312 ##label TAK COMMENT The function of this plasma protein is not known. CLASSIFICATION #superfamily leucine-rich alpha-2-glycoprotein; leucine-rich !1alpha-2-glycoprotein repeat homology; proteoglycan !1carboxyl-terminal homology KEYWORDS duplication; glycoprotein; plasma; tandem repeat FEATURE !$58-81 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR1\ !$82-105 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR2\ !$106-129 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR3\ !$130-153 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR4\ !$154-177 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR5\ !$178-201 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR6\ !$202-225 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR7\ !$226-249 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR8\ !$262-309 #domain proteoglycan carboxyl-terminal homology !8#label PCH\ !$2 #binding_site carbohydrate (Thr) (covalent) #status !8experimental\ !$8-21,268-294 #disulfide_bonds #status experimental\ !$44,151,234,290 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$271 #binding_site carbohydrate (Asn) (covalent) #status !8absent SUMMARY #length 312 #molecular-weight 34346 #checksum 6045 SEQUENCE /// ENTRY A29944 #type complete TITLE chaoptin precursor - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES photoreceptor cell-specific membrane protein ORGANISM #formal_name Drosophila melanogaster DATE 15-Dec-1988 #sequence_revision 15-Dec-1988 #text_change 22-Jun-1999 ACCESSIONS A29944; A21123 REFERENCE A29944 !$#authors Reinke, R.; Krantz, D.E.; Yen, D.; Zipursky, S.L. !$#journal Cell (1988) 52:291-301 !$#title Chaoptin, a cell surface glycoprotein required for !1Drosophila photoreceptor cell morphogenesis, contains a !1repeat motif found in yeast and human. !$#cross-references MUID:88135762; PMID:3124963 !$#accession A29944 !'##molecule_type DNA !'##residues 1-1134 ##label REI !'##cross-references GB:M19008; GB:M19009; GB:M19010; GB:M19011; !1GB:M19012; GB:M19013; GB:M19014; GB:M19015; GB:M19016; !1GB:M19017; NID:g157094; PIDN:AAA28425.1; PID:g157098 REFERENCE A21123 !$#authors Zipursky, S.L.; Venkatesh, T.R.; Teplow, D.B.; Benzer, S. !$#journal Cell (1984) 36:15-26 !$#title Neuronal development in the Drosophila retina: monoclonal !1antibodies as molecular probes. !$#cross-references MUID:84106810; PMID:6420071 !$#accession A21123 !'##molecule_type protein !'##residues 31-43,'HX',46-49,'H' ##label ZIP GENETICS !$#gene FlyBase:chp !'##cross-references FlyBase:FBgn0000313 !$#introns 1/3 80/3; 318/3; 377/2 422/2; 702/1 745/3; 831/2; 998/2 CLASSIFICATION #superfamily chaoptin; leucine-rich alpha-2-glycoprotein !1repeat homology KEYWORDS cell adhesion; glycoprotein; membrane protein FEATURE !$1-29 #domain signal sequence #status predicted #label SIG\ !$30-1134 #product chaoptin #status predicted #label MAT\ !$80-102 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #status atypical #label LRR1\ !$103-126 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR2\ !$128-151 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR3\ !$152-175 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR4\ !$177-200 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR5\ !$201-224 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR6\ !$226-249 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR7\ !$250-273 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR8\ !$279-302 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR9\ !$303-325 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR10\ !$326-349 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR11\ !$351-374 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR12\ !$375-399 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR13\ !$401-424 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR14\ !$428-451 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR15\ !$453-476 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR16\ !$477-500 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR17\ !$502-526 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR18\ !$527-550 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR19\ !$551-574 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR20\ !$577-600 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR21\ !$601-624 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR22\ !$625-648 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR23\ !$649-672 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR24\ !$673-696 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR25\ !$708-731 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR26\ !$733-756 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR27\ !$757-780 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR28\ !$781-804 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR29\ !$805-827 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR30\ !$828-851 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR31\ !$854-877 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR32\ !$879-902 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR33\ !$903-926 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR34\ !$928-948 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #status atypical #label LR35\ !$949-972 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR36\ !$973-995 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR37\ !$996-1019 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR38\ !$1021-1044 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR39\ !$1056-1080 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LR40 SUMMARY #length 1134 #molecular-weight 130719 #checksum 332 SEQUENCE /// ENTRY NBHUIA #type complete TITLE platelet glycoprotein Ib alpha chain precursor - human ALTERNATE_NAMES membrane glycoprotein Ib alpha chain CONTAINS glycocalicin ORGANISM #formal_name Homo sapiens #common_name man DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 22-Jun-1999 ACCESSIONS A94174; A60435; A94173; S16945; I55355; A27075; A27102 REFERENCE A94174 !$#authors Lopez, J.A.; Chung, D.W.; Fujikawa, K.; Hagen, F.S.; !1Papayannopoulou, T.; Roth, G.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:5615-5619 !$#title Cloning of the alpha-chain of human platelet glycoprotein !1Ib: a transmembrane protein with homology to leucine-rich !1alpha-2-glycoprotein. !$#cross-references MUID:87289655; PMID:3303030 !$#accession A94174 !'##molecule_type mRNA !'##residues 1-626 ##label LOP !'##cross-references GB:J02940; NID:g183499; PIDN:AAA52595.1; !1PID:g306793 REFERENCE A60435 !$#authors Wicki, A.N.; Walz, A.; Gerber-Huber, S.N.; Wenger, R.H.; !1Vornhagen, R.; Clemetson, K.J. !$#journal Thromb. Haemost. (1989) 61:448-453 !$#title Isolation and characterization of human blood platelet mRNA !1and construction of a cDNA library in lambdagt11. !1Confirmation of the platelet derivation by identification of !1GPIb coding mRNA and cloning of a GPIb coding cDNA insert. !$#cross-references MUID:90020160; PMID:2799758 !$#accession A60435 !'##molecule_type mRNA !'##residues 207-467 ##label WIC REFERENCE A94173 !$#authors Titani, K.; Takio, K.; Handa, M.; Ruggeri, Z.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:5610-5614 !$#title Amino acid sequence of the von Willebrand factor-binding !1domain of platelet membrane glycoprotein Ib. !$#cross-references MUID:87289654; PMID:3497398 !$#accession A94173 !'##molecule_type protein !'##residues 17-315 ##label TIT REFERENCE S16945 !$#authors Hess, D.; Schaller, J.; Rickli, E.E.; Clemetson, K.J. !$#journal Eur. J. Biochem. (1991) 199:389-393 !$#title Identification of the disulphide bonds in human platelet !1glycocalicin. !$#cross-references MUID:91301149; PMID:2070794 !$#accession S16945 !'##status preliminary !'##molecule_type protein !'##residues 224-227;262-270;277-282 ##label HES REFERENCE I55355 !$#authors Lopez, J.A.; Ludwig, E.H.; McCarthy, B.J. !$#journal J. Biol. Chem. (1992) 267:10055-10061 !$#title Polymorphism of human glycoprotein Ib alpha results from a !1variable number of tandem repeats of a 13-amino acid !1sequence in the mucin-like macroglycopeptide region. !1Structure/function implications. !$#cross-references MUID:92250564; PMID:1577776 !$#accession I55355 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 412-427 ##label RES !'##cross-references GB:S34436; NID:g249176; PIDN:AAB22152.1; !1PID:g249177 !'##note variant D COMMENT Glycoprotein Ib (GPIb), a surface membrane protein of !1platelets, participates in the formation of platelet plugs !1by binding to von Willebrand factor, bound to the !1subendothelium. COMMENT Platelet activation apparently involves disruption of the !1macromolecular complex of GPIb with the platelet !1glycoprotein IX and dissociation of GPIb from the !1actin-binding protein. COMMENT Binding sites for von Willebrand factor and thrombin (the !1latter site with unknown function) are in the amino-terminal !1part of the molecule. COMMENT Glycocalicin, which is approximately coextensive with the !1extracellular part of the molecule, is cleaved off by !1calpain during platelet lysis. GENETICS !$#gene GDB:GP1BA; GP1B !'##cross-references GDB:118806; OMIM:231200 !$#map_position 17pter-17p12 COMPLEX heterodimer with platelet glycoprotein Ib beta chain !1(NBHUIB) CLASSIFICATION #superfamily platelet glycoprotein Ib alpha chain; !1leucine-rich alpha-2-glycoprotein repeat homology KEYWORDS blood coagulation; duplication; glycoprotein; platelet !1membrane; tandem repeat; thrombin binding; transmembrane !1protein; von Willebrand factor binding FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-626 #product platelet glycoprotein Ib alpha chain #status !8predicted #label MPT\ !$48-71 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR1\ !$72-93 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR2\ !$94-116 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR3\ !$117-140 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR4\ !$141-164 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR5\ !$165-188 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR6\ !$189-212 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR7\ !$379-430 #region proline/threonine-rich 9-residue repeats\ !$502-540 #domain transmembrane #status predicted #label TRM\ !$541-626 #domain intracellular #status predicted #label INT\ !$37,175 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$308 #binding_site carbohydrate (Thr) (covalent) #status !8experimental SUMMARY #length 626 #molecular-weight 68955 #checksum 2140 SEQUENCE /// ENTRY NBHUIB #type complete TITLE platelet glycoprotein Ib beta chain precursor - human ALTERNATE_NAMES membrane glycoprotein Ib beta chain (GPIb) ORGANISM #formal_name Homo sapiens #common_name man DATE 21-May-1990 #sequence_revision 05-Apr-1995 #text_change 21-Jul-2000 ACCESSIONS A54137; A31929; B26864 REFERENCE A54137 !$#authors Yagi, M.; Edelhoff, S.; Disteche, C.M.; Roth, G.J. !$#journal J. Biol. Chem. (1994) 269:17424-17427 !$#title Structural characterization and chromosomal location of the !1gene encoding human platelet glycoprotein Ibbeta. !$#cross-references MUID:94292494; PMID:8021244 !$#accession A54137 !'##molecule_type DNA !'##residues 1-206 ##label YAG !'##cross-references GB:U07983; NID:g2978509; PIDN:AAC39781.1; !1PID:g2978512 REFERENCE A31929 !$#authors Lopez, J.A.; Chung, D.W.; Fujikawa, K.; Hagen, F.S.; Davie, !1E.W.; Roth, G.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:2135-2139 !$#title The alpha and beta chains of human platelet glycoprotein Ib !1are both transmembrane proteins containing a leucine-rich !1amino acid sequence. !$#cross-references MUID:88176901; PMID:3353370 !$#accession A31929 !'##molecule_type mRNA !'##residues 1-206 ##label LOP !'##cross-references GB:J03259; NID:g183497; PIDN:AAA52594.1; !1PID:g306792 !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing REFERENCE A26864 !$#authors Canfield, V.A.; Ozols, J.; Nugent, D.; Roth, G.J. !$#journal Biochem. Biophys. Res. Commun. (1987) 147:526-534 !$#title Isolation and characterization of the alpha and beta chains !1of human platelet glycoprotein Ib. !$#cross-references MUID:87326405; PMID:3632685 !$#accession B26864 !'##molecule_type protein !'##residues 27-29,'Q',31,'Q',33-38,'Q',40 ##label CAN !'##note cysteine and glutamine could not be distinquished by the !1authors' methodology COMMENT Glycoprotein Ib, a surface membrane protein of platelets, !1participates in the formation of platelet plugs by binding !1to von Willebrand factor, which is already bound to the !1subendothelium. COMMENT Platelet activation apparently involves disruption of the !1macromolecular complex of GPIb with the platelet !1glycoprotein IX and dissociation of GPIb from the !1actin-binding protein. GENETICS !$#gene GDB:GP1BB !'##cross-references GDB:128731; OMIM:138720 !$#map_position 22q11.21-22q11.23 !$#introns 4/1 COMPLEX heterodimer with platelet glycoprotein Ib alpha chain !1(PIR:NBHUIA) CLASSIFICATION #superfamily platelet glycoprotein Ib beta chain; !1leucine-rich alpha-2-glycoprotein repeat homology; !1proteoglycan amino-terminal homology; proteoglycan !1carboxyl-terminal homology KEYWORDS alternative splicing; blood coagulation; duplication; !1glycoprotein; heterodimer; phosphoprotein; platelet !1membrane; thrombin binding; transmembrane protein; von !1Willebrand factor binding FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$19-44 #domain proteoglycan amino-terminal homology #label !8PAH\ !$26-206 #product platelet glycoprotein Ib beta chain #status !8predicted #label MAT\ !$56-79 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR\ !$87-133 #domain proteoglycan carboxyl-terminal homology !8#label PCH\ !$148-172 #domain transmembrane #status predicted #label TRM\ !$66 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$191 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 206 #molecular-weight 21717 #checksum 470 SEQUENCE /// ENTRY I55604 #type complete TITLE platelet glycoprotein Ib beta chain precursor, endothelial splice form - human ALTERNATE_NAMES membrane glycoprotein Ib beta chain (GPIb) ORGANISM #formal_name Homo sapiens #common_name man DATE 02-Jul-1996 #sequence_revision 02-Jul-1996 #text_change 22-Jun-1999 ACCESSIONS I55604 REFERENCE I55604 !$#authors Kelly, M.D.; Essex, D.W.; Shapiro, S.S.; Meloni, F.J.; !1Druck, T.; Huebner, K.; Konkle, B.A. !$#journal J. Clin. Invest. (1994) 93:2417-2424 !$#title Complementary DNA cloning of the alternatively expressed !1endothelial cell glycoprotein Ib beta (GPIb beta) and !1localization of the GPIb beta gene to chromosome 22. !$#cross-references MUID:94259799; PMID:8200976 !$#accession I55604 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-411 ##label KEL !'##cross-references GB:L20860; NID:g438627; PIDN:AAA20398.1; !1PID:g517494 GENETICS !$#gene GDB:GP1BB !'##cross-references GDB:128731; OMIM:138720 !$#map_position 22q11.21-22q11.23 !$#introns 209/1 COMPLEX heterodimer with platelet glycoprotein Ib alpha chain !1(PIR:NBHUIA) CLASSIFICATION #superfamily platelet glycoprotein Ib beta chain; !1leucine-rich alpha-2-glycoprotein repeat homology; !1proteoglycan amino-terminal homology; proteoglycan !1carboxyl-terminal homology KEYWORDS alternative splicing; blood coagulation; duplication; !1glycoprotein; heterodimer; phosphoprotein; platelet !1membrane; thrombin binding; transmembrane protein; von !1Willebrand factor binding FEATURE !$224-249 #domain proteoglycan amino-terminal homology #label !8PAH\ !$261-284 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR\ !$292-338 #domain proteoglycan carboxyl-terminal homology !8#label PCH\ !$353-377 #domain transmembrane #status predicted #label TRM\ !$271 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$396 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 411 #molecular-weight 43157 #checksum 4750 SEQUENCE /// ENTRY A46606 #type complete TITLE platelet glycoprotein IX precursor - human ORGANISM #formal_name Homo sapiens #common_name man DATE 21-Sep-1993 #sequence_revision 06-Sep-1996 #text_change 22-Jun-1999 ACCESSIONS A46606; S12952; A33731; A31586; S11723 REFERENCE A46606 !$#authors Hickey, M.J.; Roth, G.J. !$#journal J. Biol. Chem. (1993) 268:3438-3443 !$#title Characterization of the gene encoding human platelet !1glycoprotein IX. !$#cross-references MUID:93155192; PMID:8429020 !$#accession A46606 !'##molecule_type DNA !'##residues 1-176 ##label HIC !'##experimental_source liver cell !'##note sequence extracted from NCBI backbone (NCBIN:124405, !1NCBIP:124406) REFERENCE S12952 !$#authors Hickey, M.J.; Deaven, L.L.; Roth, G.J. !$#journal FEBS Lett. (1990) 274:189-192 !$#title Human platelet glycoprotein IX. Characterization of cDNA and !1localization of the gene to chromosome 3. !$#cross-references MUID:91071429; PMID:2253772 !$#accession S12952 !'##molecule_type mRNA !'##residues 1-121,'GPL',125-176 ##label HI2 !'##cross-references EMBL:X52997 REFERENCE A33731 !$#authors Hickey, M.J.; Williams, S.A.; Roth, G.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:6773-6777 !$#title Human platelet glycoprotein IX: an adhesive prototype of !1leucine-rich glycoproteins with flank-center-flank !1structures. !$#cross-references MUID:89367331; PMID:2771955 !$#accession A33731 !'##molecule_type mRNA !'##residues 12-121,'GPL',125-176 ##label HI3 !'##cross-references GB:M25827; NID:g340362; PIDN:AAA36809.1; !1PID:g340363 REFERENCE A31586 !$#authors Roth, G.J.; Ozols, J.; Nugent, D.J.; Williams, S.A. !$#journal Biochem. Biophys. Res. Commun. (1988) 156:931-939 !$#title Isolation and characterization of human platelet !1glycoprotein IX. !$#cross-references MUID:89050128; PMID:3056407 !$#accession A31586 !'##molecule_type protein !'##residues 17-19,'X',21-22,'XL',25,'T',27-30,'X',32-33 ##label ROT GENETICS !$#gene GDB:GP9; CD42a !'##cross-references GDB:126370; OMIM:173515 !$#map_position 3pter-3qter COMPLEX With platelet glycoproteins Ia, Ib, and V, forms the von !1Willebrand factor receptor. FUNCTION !$#description von Willebrand factor receptor mediates platelet adhesion to !1injured arterial surfaces, a critical step in the initiation !1of blood coagulation CLASSIFICATION #superfamily platelet glycoprotein Ib beta chain; !1leucine-rich alpha-2-glycoprotein repeat homology; !1proteoglycan amino-terminal homology; proteoglycan !1carboxyl-terminal homology KEYWORDS blood coagulation; duplication; glycoprotein; platelet !1membrane; thrombin binding; transmembrane protein; von !1Willebrand factor binding FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$13-43 #domain proteoglycan amino-terminal homology #status !8atypical #label PAH\ !$17-176 #product platelet glycoprotein IX #status predicted !8#label MAT\ !$52-75 #domain leucine-rich alpha-2-glycoprotein repeat !8homology #label LRR1\ !$83-131 #domain proteoglycan carboxyl-terminal homology !8#label PCH\ !$146-170 #domain transmembrane #status predicted #label TMM\ !$60 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 176 #molecular-weight 18963 #checksum 6652 SEQUENCE /// ENTRY VWHU #type complete TITLE von Willebrand factor precursor - human ORGANISM #formal_name Homo sapiens #common_name man DATE 04-Dec-1986 #sequence_revision 30-Jun-1993 #text_change 22-Jun-1999 ACCESSIONS A34480; S02377; A37139; S23676; A25298; A25469; A25366; !1S23618; S23645; A94060; A90504; A44178; S07363; S23678; !1A90505; A23464; A36013; A60913; A03212; S23677 REFERENCE A34480 !$#authors Mancuso, D.J.; Tuley, E.A.; Westfield, L.A.; Worrall, N.K.; !1Shelton-Inloes, B.B.; Sorace, J.M.; Alevy, Y.G.; Sadler, !1J.E. !$#journal J. Biol. Chem. (1989) 264:19514-19527 !$#title Structure of the gene for human von Willebrand factor. !$#cross-references MUID:90062044; PMID:2584182 !$#accession A34480 !'##molecule_type DNA !'##residues 1-2813 ##label MAN !'##cross-references EMBL:M25864 REFERENCE S02377 !$#authors Bonthron, D.; Orkin, S.H. !$#journal Eur. J. Biochem. (1988) 171:51-57 !$#title The human von Willebrand factor gene. Structure of the 5' !1region. !$#cross-references MUID:88111704; PMID:2828057 !$#accession S02377 !'##molecule_type DNA !'##residues 1-177 ##label BO2 !'##cross-references EMBL:X06828 REFERENCE A37139 !$#authors Mancuso, D.J.; Tuley, E.A.; Westfield, L.A.; Lester-Mancuso, !1T.L.; Le Beau, M.M.; Sorace, J.M.; Sadler, J.E. !$#journal Biochemistry (1991) 30:253-269 !$#title Human von Willebrand factor gene and pseudogene: structural !1analysis and differentiation by polymerase chain reaction. !$#cross-references MUID:91105089; PMID:1988024 !$#accession A37139 !'##molecule_type DNA !'##residues 990-1947 ##label MAD !'##cross-references GB:M60675; NID:g340357; PIDN:AAA61295.1; !1PID:g553810 !'##note the authors translated the codon CGC for residue 156 as Gln REFERENCE S23676 !$#authors Collins, C.J.; Underdahl, J.P.; Levene, R.B.; Ravera, C.P.; !1Morin, M.J.; Dombalagian, M.J.; Ricca, G.; Livingston, D.M.; !1Lynch, D.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:4393-4397 !$#title Molecular cloning of the human gene for von Willebrand !1factor and identification of the transcription initiation !1site. !$#cross-references MUID:87260814; PMID:3496594 !$#accession S23676 !'##molecule_type DNA !'##residues 2731-2813 ##label COL !'##cross-references EMBL:M16945 REFERENCE A25298 !$#authors Bonthron, D.; Orr, E.C.; Mitsock, L.M.; Ginsburg, D.; !1Handin, R.I.; Orkin, S.H. !$#journal Nucleic Acids Res. (1986) 14:7125-7127 !$#title Nucleotide sequence of pre-pro-von Willebrand factor cDNA. !$#cross-references MUID:87016349; PMID:3489923 !$#accession A25298 !'##molecule_type mRNA !'##residues 1-470,'V',472-2813 ##label BON !'##cross-references EMBL:X04385 REFERENCE A91044 !$#authors Verweij, C.L.; Diergaarde, P.J.; Hart, M.; Pannekoek, H. !$#journal EMBO J. (1986) 5:1839-1847 !$#title Full-length von Willebrand factor (vWF) cDNA encodes a !1highly repetitive protein considerably larger than the !1mature vWF subunit. !$#cross-references MUID:87004550; PMID:3019665 !$#accession A25469 !'##molecule_type mRNA !'##residues 1-470,'V',472-483,'R',485-1022,'K',1024-1025,'E',1027-1400 !1##label VER !'##cross-references EMBL:X04146 !'##note this sequence has been revised in reference A91056 REFERENCE A91056 !$#authors Verweij, C.L.; Diergaarde, P.J.; Hart, M.; Pannekoek, H. !$#journal EMBO J. (1986) 5:3074 !$#accession A25366 !'##molecule_type mRNA !'##residues 1021-1030 ##label VE2 !'##note this is a revision to the sequence from reference A91044 REFERENCE S23618 !$#authors Shelton-Inloes, B.B.; Broze Jr., G.J.; Miletich, J.P.; !1Sadler, J.E. !$#journal Biochem. Biophys. Res. Commun. (1987) 144:657-665 !$#title Evolution of human von Willebrand factor: cDNA sequence !1polymorphisms, repeated domains, and relationship to von !1Willebrand antigen II. !$#cross-references MUID:87213253; PMID:3495266 !$#accession S23618 !'##molecule_type mRNA !'##residues 1-120 ##label SH2 !'##cross-references EMBL:M17588; NID:g799330; PIDN:AAA65940.1; !1PID:g340316 !$#accession S23645 !'##molecule_type protein !'##residues 23-56 ##label SH3 REFERENCE A94060 !$#authors Sadler, J.E.; Shelton-Inloes, B.B.; Sorace, J.M.; Harlan, !1J.M.; Titani, K.; Davie, E.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:6394-6398 !$#title Cloning and characterization of two cDNAs coding for human !1von Willebrand factor. !$#cross-references MUID:86016708; PMID:2864688 !$#accession A94060 !'##molecule_type mRNA !'##residues 'WA',739,'C',744-769,'H',771-788,'A',790-803,'S', !1805-873;1289-1471,'D',1473-2167,'S',2169-2813 ##label SAD !'##note the authors translated the codon TCG for residue 2168 as Cys REFERENCE A90504 !$#authors Shelton-Inloes, B.B.; Titani, K.; Sadler, J.E. !$#journal Biochemistry (1986) 25:3164-3171 !$#title cDNA sequences for human von Willebrand factor reveal five !1types of repeated domains and five possible protein sequence !1polymorphisms. !$#cross-references MUID:86269894; PMID:3488076 !$#accession A90504 !'##molecule_type mRNA !'##residues 781-788,'A',790-1424 ##label SHE !'##note 852-Gln, 857-Asp, and 1381-Thr were also found REFERENCE A44178 !$#authors Ginsburg, D.; Handin, R.I.; Bonthron, D.T.; Donlon, T.A.; !1Bruns, G.A.P.; Latt, S.A.; Orkin, S.H. !$#journal Science (1985) 228:1401-1406 !$#title Human von Willebrand factor (vWF): isolation of !1complementary DNA (cDNA) clones and chromosomal !1localization. !$#cross-references MUID:85244588; PMID:3874428 !$#accession A44178 !'##molecule_type mRNA !'##residues 2621-2813 ##label GIN !'##cross-references EMBL:K03028; NID:g340308; PIDN:AAA61293.1; !1PID:g340309 REFERENCE S07363 !$#authors Verweij, C.L.; de Vries, C.J.M.; Distel, B.; van Zonneveld, !1A.J.; van Kessel, A.G.; van Mourik, J.A.; Pannekoek, H. !$#journal Nucleic Acids Res. (1985) 13:4699-4717 !$#title Construction of cDNA coding for human von Willebrand factor !1using antibody probes for colony-screening and mapping of !1the chromosomal gene. !$#cross-references MUID:85269603; PMID:3875078 !$#accession S07363 !'##molecule_type mRNA !'##residues 2731-2813 ##label VE3 !'##cross-references EMBL:X02672; NID:g37939; PIDN:CAA26503.1; !1PID:g37940 REFERENCE S23678 !$#authors Lynch, D.C.; Zimmerman, T.S.; Collins, C.J.; Brown, M.; !1Morin, M.J.; Ling, E.H.; Livingston, D.M. !$#journal Cell (1985) 41:49-56 !$#title Molecular cloning of cDNA for human von Willebrand factor: !1authentication by a new method. !$#cross-references MUID:85201687; PMID:3873280 !$#accession S23678 !'##molecule_type mRNA !'##residues 2731-2813 ##label LYN !'##cross-references EMBL:K03028 REFERENCE A90505 !$#authors Titani, K.; Kumar, S.; Takio, K.; Ericsson, L.H.; Wade, !1R.D.; Ashida, K.; Walsh, K.A.; Chopek, M.W.; Sadler, J.E.; !1Fujikawa, K. !$#journal Biochemistry (1986) 25:3171-3184 !$#title Amino acid sequences of human von Willebrand factor. !$#cross-references MUID:86269895; PMID:3524673 !$#accession A90505 !'##molecule_type protein !'##residues 764-788,'A',790-1471,'D',1473-2813 ##label TIT !'##note 789-Thr was also found REFERENCE A23464 !$#authors Chopek, M.W.; Girma, J.P.; Fujikawa, K.; Davie, E.W.; !1Titani, K. !$#journal Biochemistry (1986) 25:3146-3155 !$#title Human von Willebrand factor: a multivalent protein composed !1of identical subunits. !$#cross-references MUID:86269892; PMID:3015199 !$#accession A23464 !'##molecule_type protein !'##residues 764-773;2803-2813 ##label CHO REFERENCE A36013 !$#authors Dent, J.A.; Berkowitz, S.D.; Ware, J.; Kasper, C.K.; !1Ruggeri, Z.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:6306-6310 !$#title Identification of a cleavage site directing the !1immunochemical detection of molecular abnormalities in type !1IIA von Willebrand factor. !$#cross-references MUID:90349604; PMID:2385594 !$#accession A36013 !'##molecule_type protein !'##residues 1606-1617 ##label DEN REFERENCE A60913 !$#authors Fay, P.J.; Kawai, Y.; Wagner, D.D.; Ginsburg, D.; Bonthron, !1D.; Ohlsson-Wilhelm, B.M.; Chavin, S.I.; Abraham, G.N.; !1Handin, R.I.; Orkin, S.H.; Montgomery, R.R.; Marder, V.J. !$#journal Science (1986) 232:995-998 !$#title Propolypeptide of von Willebrand factor circulates in blood !1and is identical to von Willebrand antigen II. !$#cross-references MUID:86208144; PMID:3486471 !$#accession A60913 !'##molecule_type protein !'##residues 576-590 ##label FAY GENETICS !$#gene GDB:VWF !'##cross-references GDB:119125; OMIM:193400 !$#map_position 12p13.3-12p13.2 !$#introns 19/1; 74/1; 108/2; 178/1; 219/3; 292/1; 333/1; 370/2; 386/1; !1431/3; 478/1; 511/3; 577/1; 649/1; 729/2; 761/1; 814/3; 849/ !12; 895/3; 940/3; 989/3; 1036/3; 1074/3; 1127/1; 1180/1; !11225/2; 1685/1; 1724/1; 1771/1; 1819/1; 1874/1; 1888/3; !11948/1; 2021/3; 2086/1; 2200/1; 2266/3; 2301/1; 2326/1; !12361/1; 2429/3; 2479/3; 2516/3; 2577/1; 2590/3; 2629/3; !12662/3; 2705/3; 2719/1; 2751/3 CLASSIFICATION #superfamily von Willebrand factor; von Willebrand factor !1type A repeat homology; von Willebrand factor type C repeat !1homology KEYWORDS blood coagulation; cell binding; connective tissue; !1disulfide bond; duplication; extracellular matrix; !1glycoprotein; homomultimer; plasma; von Willebrand disease FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-763 #product von Willebrand antigen II #status predicted !8#label MA1\ !$34-386 #domain type D repeat 1 #label DD1\ !$387-745 #domain type D repeat 2 #label DD2\ !$698-700 #region cell attachment (R-G-D) motif\ !$764-2813 #product von Willebrand factor #status predicted !8#label MA2\ !$784-865 #domain D' #label DDD\ !$788-833,2216-2261 #region duplication\ !$826-853,2400-2515, !$2544-2662 #region duplication\ !$842-1130,1934-2203 #region duplication\ !$866-1241 #domain type D repeat 3 #label DD3\ !$1275-1443 #domain von Willebrand factor type A repeat homology !8#label VWA1\ !$1496-1654 #domain von Willebrand factor type A repeat homology !8#label VWA2\ !$1689-1854 #domain von Willebrand factor type A repeat homology !8#label VWA3\ !$1947-2295 #domain type D repeat 4 #label DD4\ !$2296-2330 #domain type B repeat 1 #label VB1\ !$2340-2365 #domain type B repeat 2 #label VB2\ !$2375-2399 #domain type B repeat 3 #label VB3\ !$2430-2497 #domain von Willebrand factor type C repeat homology !8#label VWC1\ !$2507-2509 #region cell attachment (R-G-D) motif\ !$2581-2647 #domain von Willebrand factor type C repeat homology !8#label VWC2\ !$857,1231,1515,1574, !$2223,2290,2357, !$2400,2546,2585,2790 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$1147 #binding_site carbohydrate (Asn) (covalent) #status !8atypical\ !$1248,1255,1256, !$1468,1477,1487, !$1679,2298 #binding_site carbohydrate (Thr) (covalent) #status !8experimental\ !$1263,1486 #binding_site carbohydrate (Ser) (covalent) #status !8experimental SUMMARY #length 2813 #molecular-weight 309296 #checksum 4996 SEQUENCE /// ENTRY A55195 #type complete TITLE chordin precursor - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A55195 REFERENCE A55195 !$#authors Sasai, Y.; Lu, B.; Steinbeisser, H.; Geissert, D.; Gont, !1L.K.; De Robertis, E.M. !$#journal Cell (1994) 79:779-790 !$#title Xenopus chordin: a novel dorsalizing factor activated by !1organizer-specific homeobox genes. !$#cross-references MUID:95094250; PMID:8001117 !$#accession A55195 !'##status preliminary !'##molecule_type mRNA !'##residues 1-941 ##label SAS !'##cross-references GB:L35764; NID:g603944; PIDN:AAC42222.1; !1PID:g603945 CLASSIFICATION #superfamily chordin; von Willebrand factor type C repeat !1homology FEATURE !$42-119 #domain von Willebrand factor type C repeat homology !8#label VWC1\ !$692-753 #domain von Willebrand factor type C repeat homology !8#label VWC2\ !$770-840 #domain von Willebrand factor type C repeat homology !8#label VWC3\ !$858-922 #domain von Willebrand factor type C repeat homology !8#label VWC4 SUMMARY #length 941 #molecular-weight 104946 #checksum 9276 SEQUENCE /// ENTRY RWHU1B #type complete TITLE cell surface glycoprotein CD11b precursor [validated] - human ALTERNATE_NAMES complement receptor type 3 alpha chain; leukocyte adhesion protein Mac-1 alpha chain; leukocyte differentiation antigen Mo1 alpha chain; leukocyte glycoprotein alpha chain (Mo1); leukocyte integrin alpha chain; neutrophil adherence receptor alphaM chain ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 31-Dec-2000 ACCESSIONS A31108; A28915; A41600; A30892; A32218; A46526; A26091; !1I52567 REFERENCE A31108 !$#authors Corbi, A.L.; Kishimoto, T.K.; Miller, L.J.; Springer, T.A. !$#journal J. Biol. Chem. (1988) 263:12403-12411 !$#title The human leukocyte adhesion glycoprotein Mac-1 (complement !1receptor type 3, CD11b) alpha-subunit. Cloning, primary !1structure, and relation to the integrins, Von Willebrand !1factor and factor B. !$#cross-references MUID:88315033; PMID:2457584 !$#accession A31108 !'##molecule_type mRNA !'##residues 1-1153 ##label COR !'##cross-references GB:J03925; NID:g187284; PIDN:AAA59544.1; !1PID:g307148 !'##note part of this sequence was confirmed by protein sequencing REFERENCE A28915 !$#authors Arnaout, M.A.; Gupta, S.K.; Pierce, M.W.; Tenen, D.G. !$#journal J. Cell Biol. (1988) 106:2153-2158 !$#title Amino acid sequence of the alpha subunit of human leukocyte !1adhesion receptor Mo1 (complement receptor type 3). !$#cross-references MUID:88257215; PMID:2454931 !$#accession A28915 !'##molecule_type mRNA !'##residues 1-499,501-965,'P',967-1153 ##label ARN !'##cross-references GB:M18044; GB:J03270; GB:M19664; GB:X07421; !1NID:g186935; PIDN:AAA59491.1; PID:g307114 !'##note the authors translated the codon TAC for residue 1129 as Thr !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE A41600 !$#authors Shelley, C.S.; Arnaout, M.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:10525-10529 !$#title The promoter of the CD11b gene directs myeloid-specific and !1developmentally regulated expression. !$#cross-references MUID:92073318; PMID:1683702 !$#accession A41600 !'##molecule_type DNA !'##residues 1-9 ##label SHE !'##cross-references GB:M76724; NID:g180018; PIDN:AAA58410.1; !1PID:g553215 REFERENCE A94193 !$#authors Arnaout, M.A.; Remold-O'Donnell, E.; Pierce, M.W.; Harris, !1P.; Tenen, D.G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:2776-2780 !$#title Molecular cloning of the alpha-subunit of human and guinea !1pig leukocyte adhesion glycoprotein Mo1: chromosomal !1localization and homology to the alpha-subunits of !1integrins. !$#cross-references MUID:88190151; PMID:2833753 !$#accession A30892 !'##molecule_type mRNA !'##residues 917-1042 ##label AR2 !'##cross-references GB:M18044 REFERENCE A32218 !$#authors Hickstein, D.D.; Hickey, M.J.; Ozols, J.; Baker, D.M.; Back, !1A.L.; Roth, G.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:257-261 !$#title cDNA sequence for the alphaM subunit of the human neutrophil !1adherence receptor indicates homology to integrin alpha !1subunits. !$#cross-references MUID:89098893; PMID:2563162 !$#accession A32218 !'##molecule_type mRNA !'##residues 9-1153 ##label HIC !'##cross-references GB:J04145; NID:g189068; PIDN:AAA59903.1; !1PID:g386975 !'##note part of this sequence was confirmed by protein sequencing REFERENCE A46526 !$#authors Fleming, J.C.; Pahl, H.L.; Gonzalez, D.A.; Smith, T.F.; !1Tenen, D.G. !$#journal J. Immunol. (1993) 150:480-490 !$#title Structural analysis of the CD11b gene and phylogenetic !1analysis of the alpha-integrin gene family demonstrate !1remarkable conservation of genomic organization and suggest !1early diversification during evolution. !$#cross-references MUID:93123748; PMID:8419480 !$#accession A46526 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-499,501-1153 ##label FLE !'##cross-references GB:S52227; NID:g263047; PIDN:AAB24821.1; !1PID:g263049 !'##note the last three bases of intron 13, CAG, are included in some !1but not all mature mRNA species and encode 500-Gln when !1present !'##note sequence extracted from NCBI backbone (NCBIP:121963) REFERENCE A90664 !$#authors Pierce, M.W.; Remold-O'Donnell, E.; Todd III, R.F.; Arnaout, !1M.A. !$#journal Biochim. Biophys. Acta (1986) 874:368-371 !$#title N-terminal sequence of human leukocyte glycoprotein Mo1: !1conservation across species and homology to platelet IIb/ !1IIIa. !$#cross-references MUID:87076671; PMID:3539202 !$#accession A26091 !'##molecule_type protein !'##residues 17-31 ##label PIE !'##experimental_source granulocytes REFERENCE I52567 !$#authors Pahl, H.L.; Rosmarin, A.G.; Tenen, D.G. !$#journal Blood (1992) 79:865-870 !$#title Characterization of the myeloid-specific CD11b promoter. !$#cross-references MUID:92144986; PMID:1346576 !$#accession I52567 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-9 ##label RES !'##cross-references GB:M84477; NID:g180184; PIDN:AAA51960.1; !1PID:g553219 COMMENT A common beta chain (CD18) forms a heterodimer with this !1chain to form Mac-1 on myeloid cells, with CD11c to form !1p150,95 on myeloid cells, and with CD11a to form LFA-1 on !1all leukocytes. GENETICS !$#gene GDB:ITGAM; CR3A !'##cross-references GDB:120599; OMIM:120980 !$#map_position 16p11.2-16p11.2 !$#note promoter contains a GATA motif and two Sp1 consensus binding !1sites CLASSIFICATION #superfamily cell surface glycoprotein CD11b; von Willebrand !1factor type A repeat homology KEYWORDS alternative splicing; calcium; cell adhesion; glycoprotein; !1heterodimer; magnesium; transmembrane protein FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-1153 #product cell surface glycoprotein CD11b #status !8experimental #label MAT\ !$17-1108 #domain extracellular #status predicted #label EXT\ !$148-318 #domain von Willebrand factor type A repeat homology !8#label VWA2\ !$465-473 #region calcium/magnesium binding #status predicted\ !$530-538 #region calcium/magnesium binding #status predicted\ !$593-601 #region calcium/magnesium binding #status predicted\ !$1109-1134 #domain transmembrane #status predicted #label TMM\ !$1135-1153 #domain intracellular #status predicted #label INT\ !$86,240,391,469,693, !$697,735,802,881, !$901,912,941,947, !$979,994,1022,1045, !$1051,1076 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1153 #molecular-weight 127306 #checksum 5196 SEQUENCE /// ENTRY RWHU1C #type complete TITLE cell surface glycoprotein CD11c precursor - human ALTERNATE_NAMES leukocyte adhesion receptor p150,95 alpha chain ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 22-Jun-1999 ACCESSIONS A36584; A35543; S00864 REFERENCE A36584 !$#authors Corbi, A.L.; Garcia-Aguilar, J.; Springer, T.A. !$#journal J. Biol. Chem. (1990) 265:12750-12751 !$#contents erratum !$#accession A36584 !'##molecule_type DNA !'##residues 1-1163 ##label COR !'##note this revision to the sequence from reference A35543 includes !1the carboxyl end REFERENCE A35543 !$#authors Corbi, A.L.; Garcia-Aguilar, J.; Springer, T.A. !$#journal J. Biol. Chem. (1990) 265:2782-2788 !$#title Genomic structure of an integrin alpha subunit, the !1leukocyte p150,95 molecule. !$#cross-references MUID:90153906; PMID:2303426 !$#accession A35543 !'##molecule_type DNA !'##residues 1-834 ##label CO2 !'##note this sequence has been revised in reference A36584 REFERENCE S00864 !$#authors Corbi, A.L.; Miller, L.J.; O'Connor, K.; Larson, R.S.; !1Springer, T.A. !$#journal EMBO J. (1987) 6:4023-4028 !$#title cDNA cloning and complete primary structure of the alpha !1subunit of a leukocyte adhesion glycoprotein, p150,95. !$#cross-references MUID:88166645; PMID:3327687 !$#accession S00864 !'##molecule_type mRNA !'##residues 1-755,'L',757-1163 ##label CO3 !'##cross-references GB:M81695; EMBL:Y00093; NID:g487829; !1PIDN:AAA59180.1; PID:g487830 !'##note part of this sequence was confirmed by protein sequencing COMMENT A common beta chain (CD18) forms a heterodimer with CD11b to !1form Mac-1 on myeloid cells, with this chain to form p150,95 !1on myeloid cells, and with CD11a to form LFA-1 on all !1leukocytes. GENETICS !$#gene GDB:ITGAX; CD11C !'##cross-references GDB:119758; OMIM:151510 !$#map_position 16p11.2-16p11.2 CLASSIFICATION #superfamily cell surface glycoprotein CD11b; von Willebrand !1factor type A repeat homology KEYWORDS calcium; cell adhesion; glycoprotein; heterodimer; !1magnesium; tandem repeat; transmembrane protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-1163 #product cell surface glycoprotein CD11c #status !8predicted #label MAT\ !$20-1107 #domain extracellular #status predicted #label EXT\ !$149-319 #domain von Willebrand factor type A repeat homology !8#label VWA4\ !$1108-1133 #domain transmembrane #status predicted #label TMM\ !$1134-1163 #domain intracellular #status predicted #label INT\ !$61,89,392,697,735, !$899,939,1050 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1163 #molecular-weight 127886 #checksum 3725 SEQUENCE /// ENTRY KFHU3 #type complete TITLE tissue factor precursor [validated] - human ALTERNATE_NAMES coagulation factor III ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 08-Dec-2000 ACCESSIONS A43645; A47574; A28320; A29062; A29672; A29008 REFERENCE A43645 !$#authors Mackman, N.; Morrissey, J.H.; Fowler, B.; Edgington, T.S. !$#journal Biochemistry (1989) 28:1755-1762 !$#title Complete sequence of the human tissue factor gene, a highly !1regulated cellular receptor that initiates the coagulation !1protease cascade. !$#cross-references MUID:89247359; PMID:2719931 !$#accession A43645 !'##molecule_type DNA !'##residues 1-295 ##label MAC !'##cross-references GB:J02846; NID:g339505; PIDN:AAA61152.1; !1PID:g339506 REFERENCE A47574 !$#authors Fisher, K.L.; Gorman, C.M.; Vehar, G.A.; O'Brien, D.P.; !1Lawn, R.M. !$#journal Thromb. Res. (1987) 48:89-99 !$#title Cloning and expression of human tissue factor cDNA. !$#cross-references MUID:88100453; PMID:3424286 !$#accession A47574 !'##molecule_type mRNA !'##residues 1-295 ##label FIS !'##cross-references GB:M27436; NID:g339507; PIDN:AAA36734.1; !1PID:g339508 REFERENCE A94171 !$#authors Spicer, E.K.; Horton, R.; Bloem, L.; Bach, R.; Williams, !1K.R.; Guha, A.; Kraus, J.; Lin, T.C.; Nemerson, Y.; !1Konigsberg, W.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:5148-5152 !$#title Isolation of cDNA clones coding for human tissue factor: !1primary structure of the protein and cDNA. !$#cross-references MUID:87260946; PMID:3037536 !$#accession A28320 !'##molecule_type mRNA !'##residues 1-295 ##label SPI !'##cross-references GB:J02931; NID:g339501; PIDN:AAA61150.1; !1PID:g339502 REFERENCE A29062 !$#authors Morrissey, J.H.; Fakhrai, H.; Edgington, T.S. !$#journal Cell (1987) 50:129-135 !$#title Molecular cloning of the cDNA for tissue factor, the !1cellular receptor for the initiation of the coagulation !1protease cascade. !$#cross-references MUID:87244317; PMID:3297348 !$#accession A29062 !'##molecule_type mRNA !'##residues 1-295 ##label MOR !'##cross-references GB:J02931; NID:g339501; PIDN:AAA61150.1; !1PID:g339502 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE A29672 !$#authors Scarpati, E.M.; Wen, D.; Broze Jr., G.J.; Miletich, J.P.; !1Flandermeyer, R.R.; Siegel, N.R.; Sadler, J.E. !$#journal Biochemistry (1987) 26:5234-5238 !$#title Human tissue factor: cDNA sequence and chromosome !1localization of the gene. !$#cross-references MUID:88050796; PMID:2823875 !$#accession A29672 !'##molecule_type mRNA !'##residues 1-259,'A',261-295 ##label SCA !'##cross-references GB:M16553; NID:g339503; PIDN:AAA61151.1; !1PID:g339504 REFERENCE A37422 !$#authors Bach, R.; Konigsberg, W.H.; Nemerson, Y. !$#journal Biochemistry (1988) 27:4227-4231 !$#title Human tissue factor contains thioester-linked palmitate and !1stearate on the cytoplasmic half-cystine. !$#cross-references MUID:89000604; PMID:3166978 !$#contents annotation; disulfide bonds and fatty acid binding site COMMENT Tissue factor is an integral membrane glycoprotein that !1serves as a receptor for plasma coagulation factor VIIa. The !1complex initiates the extrinsic coagulation pathway. COMMENT Expression of tissue factor can be induced in a variety of !1tissues by certain growth factors and inflammatory stimuli. GENETICS !$#gene GDB:F3 !'##cross-references GDB:119895; OMIM:134390 !$#map_position 1p22-1p21 !$#introns 34/1; 71/2; 138/1; 197/3; 251/1 CLASSIFICATION #superfamily tissue factor KEYWORDS blood coagulation; glycoprotein; lipoprotein; thiolester !1bond; transmembrane protein FEATURE !$1-32 #domain signal sequence #status predicted #label SIG\ !$33-295 #product tissue factor #status experimental #label !8MAT\ !$33-251 #domain extracellular #status predicted #label EXT\ !$252-274 #domain transmembrane #status predicted #label TMM\ !$275-295 #domain intracellular #status predicted #label INT\ !$43 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$81-89,218-241 #disulfide_bonds #status experimental\ !$156,169 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$277 #binding_site palmitate (Cys) (covalent) #status !8experimental SUMMARY #length 295 #molecular-weight 33067 #checksum 4014 SEQUENCE /// ENTRY KFBO3 #type complete TITLE tissue factor precursor - bovine ALTERNATE_NAMES coagulation factor III ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 22-Jun-1999 ACCESSIONS JQ1319 REFERENCE JQ1319 !$#authors Takayenoki, Y.; Muta, T.; Miyata, T.; Iwanaga, S. !$#journal Biochem. Biophys. Res. Commun. (1991) 181:1145-1150 !$#title cDNA and amino acid sequences of bovine tissue factor. !$#cross-references MUID:92109720; PMID:1764065 !$#accession JQ1319 !'##molecule_type mRNA !'##residues 1-292 ##label TAK !'##cross-references GB:S74147; NID:g241438; PIDN:AAB20755.1; !1PID:g241439 !'##experimental_source adrenal gland !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing COMMENT Tissue factor is an integral membrane glycoprotein that !1serves as a receptor for plasma coagulation factor VIIa. The !1complex initiates the extrinsic coagulation pathway. COMMENT Expression of tissue factor can be induced in a variety of !1tissues by certain growth factors and inflammatory stimuli. CLASSIFICATION #superfamily tissue factor KEYWORDS blood coagulation; glycoprotein; lipoprotein; thiolester !1bond; transmembrane protein FEATURE !$1-35 #domain signal sequence #status predicted #label SIG\ !$36-292 #product tissue factor #status experimental #label !8MAT\ !$36-248 #domain extracellular #status predicted #label EXT\ !$249-271 #domain transmembrane #status predicted #label TMM\ !$272-292 #domain intracellular #status predicted #label INT\ !$43,153,181 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$81-89,215-238 #disulfide_bonds #status predicted\ !$118,124 #binding_site carbohydrate (Thr) (covalent) #status !8predicted\ !$274 #binding_site palmitate (Cys) (covalent) #status !8experimental SUMMARY #length 292 #molecular-weight 32475 #checksum 1836 SEQUENCE /// ENTRY KFRB3 #type complete TITLE tissue factor precursor - rabbit ALTERNATE_NAMES coagulation factor III ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 21-Jul-2000 ACCESSIONS JU0441; S23681 REFERENCE JU0441 !$#authors Andrews, B.S.; Rehemtulla, A.; Fowler, B.J.; Edgington, !1T.S.; Mackman, N. !$#journal Gene (1991) 98:265-269 !$#title Conservation of tissue factor primary sequence among three !1mammalian species. !$#cross-references MUID:91200676; PMID:1840552 !$#accession JU0441 !'##molecule_type mRNA !'##residues 1-292 ##label AND !'##cross-references GB:M55390; NID:g165696; PIDN:AAA63469.1; !1PID:g165697 !'##experimental_source brain REFERENCE S23681 !$#authors Pawashe, A.; Ezekowitz, M.; Lin, T.C.; Horton, R.; Bach, R.; !1Konigsberg, W. !$#journal Thromb. Haemost. (1991) 66:315-320 !$#title Molecular cloning, characterization and expression of cDNA !1for rabbit brain tissue factor. !$#cross-references MUID:92081032; PMID:1746002 !$#accession S23681 !'##status preliminary !'##molecule_type mRNA !'##residues 33-292 ##label PAW !'##cross-references EMBL:X53521; NID:g1495; PIDN:CAA37597.1; !1PID:g3980170 COMMENT Tissue factor is an integral membrane glycoprotein that !1serves as a receptor for plasma coagulation factor VIIa. The !1complex initiates the extrinsic coagulation pathway. COMMENT Expression of tissue factor can be induced in a variety of !1tissues by certain growth factors and inflammatory stimuli. CLASSIFICATION #superfamily tissue factor KEYWORDS blood coagulation; glycoprotein; lipoprotein; thiolester !1bond; transmembrane protein FEATURE !$1-32 #domain signal sequence #status predicted #label SIG\ !$33-292 #product tissue factor #status predicted #label MAT\ !$33-249 #domain extracellular #status predicted #label EXT\ !$250-271 #domain transmembrane #status predicted #label TMM\ !$272-292 #domain intracellular #status predicted #label INT\ !$41,114,154,167,182 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$79-87,216-239 #disulfide_bonds #status predicted\ !$274 #binding_site palmitate (Cys) (covalent) #status !8experimental SUMMARY #length 292 #molecular-weight 32738 #checksum 1871 SEQUENCE /// ENTRY KFMS3 #type complete TITLE tissue factor precursor - mouse ALTERNATE_NAMES coagulation factor III ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 22-Jun-1999 ACCESSIONS A32318; A39046 REFERENCE A32318 !$#authors Hartzell, S.; Ryder, K.; Lanahan, A.; Lau, L.F.; Nathans, D. !$#journal Mol. Cell. Biol. (1989) 9:2567-2573 !$#title A growth factor-responsive gene of murine BALB/c 3T3 cells !1encodes a protein homologous to human tissue factor. !$#cross-references MUID:89343974; PMID:2761539 !$#accession A32318 !'##molecule_type mRNA !'##residues 1-294 ##label HAR !'##cross-references GB:M26071; NID:g201924; PIDN:AAA40414.1; !1PID:g201925 REFERENCE A39046 !$#authors Ranganathan, G.; Blatti, S.P.; Subramaniam, M.; Fass, D.N.; !1Maihle, N.J.; Getz, M.J. !$#journal J. Biol. Chem. (1991) 266:496-501 !$#title Cloning of murine tissue factor and regulation of gene !1expression by transforming growth factor type beta1. !$#cross-references MUID:91093171; PMID:1985911 !$#accession A39046 !'##molecule_type mRNA !'##residues 1-25,'I',27-294 ##label RAN !'##cross-references GB:M57896; GB:J05713; NID:g201926; PIDN:AAA63400.1; !1PID:g201927 !'##note 26-Thr was also found COMMENT Tissue factor is an integral membrane glycoprotein that !1serves as a receptor for plasma coagulation factor VIIa. The !1complex initiates the extrinsic coagulation pathway. COMMENT Expression of tissue factor can be induced in a variety of !1tissues by certain growth factors and inflammatory stimuli. CLASSIFICATION #superfamily tissue factor KEYWORDS blood coagulation; glycoprotein; lipoprotein; thiolester !1bond; transmembrane protein FEATURE !$1-29 #domain signal sequence #status predicted #label SIG\ !$30-294 #product tissue factor #status predicted #label MAT\ !$30-251 #domain extracellular #status predicted #label EXT\ !$252-274 #domain transmembrane #status predicted #label TMM\ !$37,57,169,200 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$75-83,218-241 #disulfide_bonds #status predicted\ !$275 #binding_site palmitate (Cys) (covalent) #status !8experimental SUMMARY #length 294 #molecular-weight 32923 #checksum 9197 SEQUENCE /// ENTRY FNHU #type complete TITLE fibronectin precursor [validated] - human ALTERNATE_NAMES fibronectin splice form ED-A ORGANISM #formal_name Homo sapiens #common_name man DATE 27-Nov-1985 #sequence_revision 31-Mar-1993 #text_change 08-Dec-2000 ACCESSIONS A26460; A26284; S03917; A24854; A24476; A91008; A93529; !1A21011; A90495; A22245; B22245; I65273; A21165; A92398; !1S34791; A60904; A23901; A92386; A32517; S14357; A23891; !1A03213; S10592 REFERENCE A26460 !$#authors Dean, D.C.; Bowlus, C.L.; Bourgeois, S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:1876-1880 !$#title Cloning and analysis of the promoter region of the human !1fibronectin gene. !$#cross-references MUID:87175578; PMID:3031656 !$#accession A26460 !'##molecule_type DNA !'##residues 1-49 ##label DEA !'##cross-references GB:M15801; NID:g182686; PIDN:AAA53376.1; !1PID:g553293 REFERENCE A26284 !$#authors Oldberg, A.; Ruoslahti, E. !$#journal J. Biol. Chem. (1986) 261:2113-2116 !$#title Evolution of the fibronectin gene. !$#cross-references MUID:86111901; PMID:3003095 !$#accession A26284 !'##molecule_type DNA !'##residues 1447-1540 ##label OLD !'##cross-references GB:M12549; NID:g182688 !'##note the authors translated the codon TTC for residue 1494 as Glu REFERENCE S00848 !$#authors Paolella, G.; Henchcliffe, C.; Sebastio, G.; Baralle, F.E. !$#journal Nucleic Acids Res. (1988) 16:3545-3557 !$#title Sequence analysis and in vivo expression show that !1alternative splicing of ED-B and ED-A regions of the human !1fibronectin gene are independent events. !$#cross-references MUID:88233940; PMID:3375063 !$#accession S03917 !'##molecule_type DNA !'##residues 1594-1767,'V',1769-1783 ##label PAO !'##cross-references EMBL:X07718; NID:g31402 !'##note the authors translated the codon AAC for residue 1631 as Asp REFERENCE A24854 !$#authors Vibe-Pedersen, K.; Magnusson, S.; Baralle, F.E. !$#journal FEBS Lett. (1986) 207:287-291 !$#title Donor and acceptor splice signals within an exon of the !1human fibronectin gene: a new type of differential splicing. !$#cross-references MUID:87030929; PMID:3770201 !$#accession A24854 !'##molecule_type DNA !'##residues 1992-2147 ##label VIB !'##cross-references GB:X04530; NID:g31436 REFERENCE A24476 !$#authors Gutman, A.; Yamada, K.M.; Kornblihtt, A. !$#journal FEBS Lett. (1986) 207:145-148 !$#title Human fibronectin is synthesized as a pre-propolypeptide. !$#cross-references MUID:87030890; PMID:3770189 !$#accession A24476 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-14,'Q',16-38 ##label GUT REFERENCE A91008 !$#authors Kornblihtt, A.R.; Umezawa, K.; Vibe-Pedersen, K.; Baralle, !1F.E. !$#journal EMBO J. (1985) 4:1755-1759 !$#title Primary structure of human fibronectin: differential !1splicing may generate at least 10 polypeptides from a single !1gene. !$#cross-references MUID:85284965; PMID:2992939 !$#accession A91008 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 32-1344,1346-2080;2112-2386 ##label KOR !'##cross-references GB:X02761 REFERENCE A93529 !$#authors Kornblihtt, A.R.; Vibe-Pedersen, K.; Baralle, F.E. !$#journal Nucleic Acids Res. (1984) 12:5853-5868 !$#title Human fibronectin: cell specific alternative mRNA splicing !1generates polypeptide chains differing in the number of !1internal repeats. !$#cross-references MUID:84272258; PMID:6462919 !$#accession A93529 !'##molecule_type mRNA !'##residues 973-2080;2112-2386 ##label KO2 !'##cross-references GB:X00739 REFERENCE A21011 !$#authors Oldberg, A.; Linney, E.; Ruoslahti, E. !$#journal J. Biol. Chem. (1983) 258:10193-10196 !$#title Molecular cloning and nucleotide sequence of a cDNA clone !1coding for the cell attachment domain in human fibronectin. !$#cross-references MUID:83290929; PMID:6688418 !$#accession A21011 !'##molecule_type mRNA !'##residues 1434-1537 ##label OL2 !'##cross-references GB:K00055; NID:g182680; PIDN:AAA52459.1; !1PID:g182683 REFERENCE A90495 !$#authors Bernard, M.P.; Kolbe, M.; Weil, D.; Chu, M.L. !$#journal Biochemistry (1985) 24:2698-2704 !$#title Human cellular fibronectin: comparison of the !1carboxyl-terminal portion with rat identifies primary !1structural domains separated by hypervariable regions. !$#cross-references MUID:85280409; PMID:2992573 !$#accession A90495 !'##molecule_type mRNA !'##residues 1594-2386 ##label BER !'##cross-references GB:M10905; NID:g182696; PIDN:AAA52462.1; !1PID:g182697 REFERENCE A22245 !$#authors Umezawa, K.; Kornblihtt, A.R.; Baralle, F.E. !$#journal FEBS Lett. (1985) 186:31-34 !$#title Isolation and characterization of cDNA clones for human !1liver fibronectin. !$#cross-references MUID:85231203; PMID:2989004 !$#accession A22245 !'##molecule_type mRNA !'##residues 1948-2067 ##label UME !'##cross-references GB:M27589; NID:g182705; PIDN:AAA52465.1; !1PID:g182706 !$#accession B22245 !'##molecule_type mRNA !'##residues 1975-1991;2017-2039 ##label UM2 !'##cross-references GB:M27590 REFERENCE I52394 !$#authors Sekiguchi, K.; Klos, A.M.; Kurachi, K.; Yoshitake, S.; !1Hakomori, S. !$#journal Biochemistry (1986) 25:4936-4941 !$#title Human liver fibronectin complementary DNAs: identification !1of two different messenger RNAs possibly encoding the alpha !1and beta subunits of plasma fibronectin. !$#cross-references MUID:87026578; PMID:3021206 !$#accession I65273 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1978-1990,2016-2018,'N',2020-2081,2113-2127 ##label SEK !'##cross-references GB:M14060; NID:g182701; PIDN:AAA52464.1; !1PID:g182704 REFERENCE A21165 !$#authors Kornblihtt, A.R.; Vibe-Pedersen, K.; Baralle, F.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:3218-3222 !$#title Isolation and characterization of cDNA clones for human and !1bovine fibronectins. !$#cross-references MUID:83221567; PMID:6304699 !$#accession A21165 !'##molecule_type mRNA !'##residues 2291-2386 ##label KO3 !'##cross-references GB:K00799; NID:g182681; PIDN:AAA52460.1; !1PID:g182684 REFERENCE A92398 !$#authors Garcia-Pardo, A.; Pearlstein, E.; Frangione, B. !$#journal J. Biol. Chem. (1983) 258:12670-12674 !$#title Primary structure of human plasma fibronectin. !$#cross-references MUID:84032463; PMID:6630202 !$#accession A92398 !'##molecule_type protein !'##residues 32-47,'C',49-51,'S',53-72,'A',74-290 ##label GAR1 REFERENCE S34791 !$#authors Garcia-Pardo, A.; Gold, L.I. !$#journal Arch. Biochem. Biophys. (1993) 304:181-188 !$#title Further characterization of the binding of fibronectin to !1gelatin reveals the presence of different binding !1interactions. !$#cross-references MUID:93312001; PMID:8323285 !$#accession S34791 !'##molecule_type protein !'##residues 291-300;551-560 ##label GAR2 REFERENCE A60904 !$#authors Griffin, C.A.; Calaycay, J.; Shively, J.E.; Smith, R.L. !$#journal Thromb. Res. (1986) 43:469-477 !$#title Two plasma fibronectin fragments with different !1gelatin-binding properties. !$#cross-references MUID:87019725; PMID:3532418 !$#accession A60904 !'##molecule_type protein !'##residues 293-301 ##label GRI REFERENCE A23901 !$#authors Calaycay, J.; Pande, H.; Lee, T.; Borsi, L.; Siri, A.; !1Shively, J.E.; Zardi, L. !$#journal J. Biol. Chem. (1985) 260:12136-12141 !$#title Primary structure of a DNA- and heparin-binding domain !1(domain III) in human plasma fibronectin. !$#cross-references MUID:86008277; PMID:3900070 !$#accession A23901 !'##molecule_type protein !'##residues 616-677,'Q',679-703,'PT' ##label CAL REFERENCE A92386 !$#authors Pierschbacher, M.D.; Ruoslahti, E.; Sundelin, J.; Lind, P.; !1Peterson, P.A. !$#journal J. Biol. Chem. (1982) 257:9593-9597 !$#title The cell attachment domain of fibronectin. Determination of !1the primary structure. !$#cross-references MUID:82265604; PMID:7050098 !$#accession A92386 !'##molecule_type protein !'##residues 1441-1548 ##label PIE !'##note residues 1524-1527 are responsible for the cell-binding !1activity REFERENCE A32517 !$#authors Garcia-Pardo, A.; Rostagno, A.; Frangione, B. !$#journal Biochem. J. (1987) 241:923-928 !$#title Primary structure of human plasma fibronectin. !1Characterization of a 38 kDa domain containing the !1C-terminal heparin-binding site (Hep III site) and a region !1of molecular heterogeneity. !$#cross-references MUID:87241275; PMID:3593230 !$#accession A32517 !'##molecule_type protein !'##residues 1589-1630,'T',1722-2058 ##label GAR3 REFERENCE S14357 !$#authors Tressel, T.; McCarthy, J.B.; Calaycay, J.; Lee, T.D.; !1Legesse, K.; Shively, J.E.; Pande, H. !$#journal Biochem. J. (1991) 274:731-738 !$#title Human plasma fibronectin. Demonstration of structural !1differences between the A- and B-chains in the III CS !1region. !$#cross-references MUID:91190085; PMID:2012601 !$#accession S14357 !'##molecule_type protein !'##residues 1614-1630,'T',1722-2081,2113-2244 ##label TRE REFERENCE A23891 !$#authors Garcia-Pardo, A.; Pearlstein, E.; Frangione, B. !$#journal J. Biol. Chem. (1985) 260:10320-10325 !$#title Primary structure of human plasma fibronectin. !1Characterization of a 31,000-dalton fragment from the !1COOH-terminal region containing a free sulfhydryl group and !1a fibrin-binding site. !$#cross-references MUID:85261459; PMID:4019516 !$#accession A23891 !'##molecule_type protein !'##residues 2071-2080;2112-2356 ##label GAR4 COMMENT The extra domain and connecting strand 3 are subject to !1developmental and tissue-specific alternative splicing. COMMENT The cellular and plasma fibronectins are high molecular !1weight glycoproteins, heterodimers of similar polypeptides, !1that are involved with processes of cell contact, !1morphology, differentiation, and transformation. GENETICS !$#gene GDB:FN1 !'##cross-references GDB:119135; OMIM:135600 !$#map_position 2q34-2q34 !$#introns 49/3; 1266/1; 1357/1; 1447/1; 1487/1; 1541/1; 1631/1; 1721/ !11; 1991/1; 2145/1 CLASSIFICATION #superfamily fibronectin; fibronectin type I repeat !1homology; fibronectin type II repeat homology; fibronectin !1type III repeat homology KEYWORDS acute phase; alternative splicing; cell adhesion; collagen !1binding; duplication; extracellular matrix; glycoprotein; !1heparin binding; heterodimer; plasma; pyroglutamic acid FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-31 #domain propeptide #status predicted #label PRO\ !$32-2386 #product fibronectin #status experimental #label MAT\ !$52-272 #domain fibrin and heparin binding #label FHB\ !$52-87 #domain fibronectin type I repeat homology #label !81F1\ !$97-135 #domain fibronectin type I repeat homology #label !81F2\ !$141-179 #domain fibronectin type I repeat homology #label !81F3\ !$186-225 #domain fibronectin type I repeat homology #label !81F4\ !$231-270 #domain fibronectin type I repeat homology #label !81F5\ !$308-608 #domain collagen binding #label CBR\ !$308-342 #domain fibronectin type I repeat homology #label !81F6\ !$360-401 #domain fibronectin type II repeat homology #label !82F1\ !$420-461 #domain fibronectin type II repeat homology #label !82F2\ !$470-508 #domain fibronectin type I repeat homology #label !81F7\ !$518-555 #domain fibronectin type I repeat homology #label !81F8\ !$561-599 #domain fibronectin type I repeat homology #label !81F9\ !$609-692 #domain fibronectin type III repeat homology #label !83FA\ !$616-706 #domain heparin binding #label HPB\ !$719-801 #domain fibronectin type III repeat homology #label !83FB\ !$810-891 #domain fibronectin type III repeat homology #label !83FC\ !$906-988 #domain fibronectin type III repeat homology #label !83FD\ !$996-1077 #domain fibronectin type III repeat homology #label !83FE\ !$1086-1164 #domain fibronectin type III repeat homology #label !83FF\ !$1173-1258 #domain fibronectin type III repeat homology #label !83FG\ !$1266-1349 #domain fibronectin type III repeat homology #label !83FH\ !$1357-1439 #domain fibronectin type III repeat homology #label !83FI\ !$1447-1529 #domain fibronectin type III repeat homology #label !83FJ\ !$1524-1526 #region cell attachment (R-G-D) motif\ !$1541-1623 #domain fibronectin type III repeat homology #label !83FK\ !$1631-1720 #domain extra #label EXD\ !$1631-1713 #domain fibronectin type III repeat homology #label !83FL\ !$1721-1991 #domain heparin binding #label HB2\ !$1721-1803 #domain fibronectin type III repeat homology #label !83FM\ !$1813-1894 #domain fibronectin type III repeat homology #label !83FN\ !$1902-1984 #domain fibronectin type III repeat homology #label !83FO\ !$1992-2102 #domain connecting strand 3 #label CS3\ !$2103-2183 #domain fibronectin type III repeat homology #label !83FP\ !$2206-2337 #domain fibrin binding #label FB2\ !$2206-2245 #domain fibronectin type I repeat homology #label !81F10\ !$2251-2288 #domain fibronectin type I repeat homology #label !81F11\ !$2295-2330 #domain fibronectin type I repeat homology #label !81F12\ !$32 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$34 #cross-link isopeptide (Gln) (interchain to Lys !8N6-amino of fibrin) #status predicted\ !$52-78,76-87,97-125, !$123-135,141-169, !$167-179,186-215, !$213-225,231-260, !$258-270,308-335, !$333-342,360-386, !$374-401,420-461, !$434-446,470-498, !$496-508,518-545, !$543-555,561-589, !$587-599,2206-2235, !$2233-2245, !$2251-2278, !$2276-2288, !$2295-2321,2319-2330 #disulfide_bonds #status predicted\ !$430,528,877,1007, !$1244,2108 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$2064 #binding_site carbohydrate (Thr) (covalent) #status !8experimental\ !$2367 #disulfide_bonds interchain (to 2371) #status !8predicted\ !$2371 #disulfide_bonds interchain (to 2367) #status !8predicted SUMMARY #length 2386 #molecular-weight 262668 #checksum 7947 SEQUENCE /// ENTRY FNBO #type complete TITLE fibronectin - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 20-Oct-2000 ACCESSIONS A26452; B21165; A23292 REFERENCE A26452 !$#authors Skorstengaard, K.; Jensen, M.S.; Sahl, P.; Petersen, T.E.; !1Magnusson, S. !$#journal Eur. J. Biochem. (1986) 161:441-453 !$#title Complete primary structure of bovine plasma fibronectin. !$#cross-references MUID:87054047; PMID:3780752 !$#accession A26452 !'##molecule_type protein !'##residues 1-2265 ##label SKO REFERENCE A21165 !$#authors Kornblihtt, A.R.; Vibe-Pedersen, K.; Baralle, F.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:3218-3222 !$#title Isolation and characterization of cDNA clones for human and !1bovine fibronectins. !$#cross-references MUID:83221567; PMID:6304699 !$#accession B21165 !'##molecule_type mRNA !'##residues 2170-2265 ##label KOR !'##cross-references GB:K00800; NID:g163055; PIDN:AAA30521.2; !1PID:g5713323 REFERENCE A23292 !$#authors Petersen, T.E.; Thogersen, H.C.; Skorstengaard, K.; !1Vibe-Pedersen, K.; Sahl, P.; Sottrup-Jensen, L.; Magnusson, !1S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:137-141 !$#title Partial primary structure of bovine plasma fibronectin: !1three types of internal homology. !$#cross-references MUID:83117805; PMID:6218503 !$#accession A23292 !'##molecule_type protein !'##residues 1-16,'C',18-20,'S', !122-432;447-463;1367-1517;1567-1673;2062-2176,'N',2178-2265 !1##label PET COMMENT Cys-1201 and Cys-2015 have free sulfhydryl groups. COMMENT The plasma fibronectin molecule consists of two chains, !1which are connected by disulfide bonds near the carboxyl !1ends. The chains partly differ due to the alternate splicing !1of mRNA. COMMENT Fibronectins bind cell surfaces and various compounds !1including collagen, fibrin, heparin, DNA, and actin. !1Fibronectins are involved in cell adhesion, cell motility, !1opsonization, wound healing, and maintenance of cell shape. COMMENT Plasma fibronectin is synthesized by hepatocytes. CLASSIFICATION #superfamily fibronectin; fibronectin type I repeat !1homology; fibronectin type II repeat homology; fibronectin !1type III repeat homology KEYWORDS acute phase; alternative splicing; collagen binding; !1duplication; extracellular matrix; glycoprotein; heparin !1binding; heterodimer; liver; phosphoprotein; plasma; !1pyroglutamic acid FEATURE !$21-241 #domain fibrin and heparin binding #label FBR\ !$21-56 #domain fibronectin type I repeat homology #label !81F1\ !$66-104 #domain fibronectin type I repeat homology #label !81F2\ !$110-148 #domain fibronectin type I repeat homology #label !81F3\ !$155-194 #domain fibronectin type I repeat homology #label !81F4\ !$200-239 #domain fibronectin type I repeat homology #label !81F5\ !$277-577 #domain collagen binding #label CBR\ !$277-311 #domain fibronectin type I repeat homology #label !81F6\ !$329-370 #domain fibronectin type II repeat homology #label !82F1\ !$389-430 #domain fibronectin type II repeat homology #label !82F2\ !$439-477 #domain fibronectin type I repeat homology #label !81F7\ !$487-524 #domain fibronectin type I repeat homology #label !81F8\ !$530-568 #domain fibronectin type I repeat homology #label !81F9\ !$578-661 #domain fibronectin type III repeat homology #label !8FN3A\ !$688-770 #domain fibronectin type III repeat homology #label !8FN3B\ !$779-860 #domain fibronectin type III repeat homology #label !8FN3C\ !$875-957 #domain fibronectin type III repeat homology #label !8FN3D\ !$965-1046 #domain fibronectin type III repeat homology #label !8FN3E\ !$1055-1134 #domain fibronectin type III repeat homology #label !8FN3F\ !$1142-1227 #domain fibronectin type III repeat homology #label !8FN3G\ !$1235-1318 #domain fibronectin type III repeat homology #label !8FN3H\ !$1326-1404 #domain fibronectin type III repeat homology #label !8GN3I\ !$1410-1517 #domain cell attachment #label CAD\ !$1416-1502 #domain fibronectin type III repeat homology #label !8FN3J\ !$1493-1495 #region cell attachment (R-G-D) motif\ !$1510-1592 #domain fibronectin type III repeat homology #label !8FN3K\ !$1600-1870 #domain heparin binding #label HB2\ !$1600-1682 #domain fibronectin type III repeat homology #label !8FN3L\ !$1692-1773 #domain fibronectin type III repeat homology #label !8FN3M\ !$1781-1863 #domain fibronectin type III repeat homology #label !8FN3N\ !$1970-1972 #region cell attachment (R-G-D) motif\ !$1982-2062 #domain fibronectin type III repeat homology #label !8FN3O\ !$1985-2216 #domain fibrin binding #label FB2\ !$2085-2124 #domain fibronectin type I repeat homology #label !81F10\ !$2130-2167 #domain fibronectin type I repeat homology #label !81F11\ !$2174-2209 #domain fibronectin type I repeat homology #label !81F12\ !$1 #modified_site pyrrolidone carboxylic acid (Gln) !8#status experimental\ !$3 #cross-link isopeptide (Gln) (interchain to Lys !8N6-amino of fibrin) #status experimental\ !$21-47,45-56,66-94, !$92-104,110-138, !$136-148,155-184, !$182-194,200-229, !$227-239,277-304, !$302-311,329-355, !$343-370,389-415, !$403-430,439-467, !$465-477,487-514, !$512-524,530-558, !$556-568,2085-2114, !$2112-2124, !$2130-2157, !$2155-2167, !$2174-2200,2198-2209 #disulfide_bonds #status predicted\ !$399,497,511,846, !$976,1213,1987 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$1205,1692 #binding_site carbohydrate (Asn) (covalent) #status !8absent\ !$1943,1944 #binding_site carbohydrate (Thr) (covalent) #status !8experimental\ !$2246 #disulfide_bonds interchain (to 2250) #status !8predicted\ !$2250 #disulfide_bonds interchain (to 2246) #status !8predicted\ !$2263 #binding_site phosphate (Ser) (covalent) #status !8experimental SUMMARY #length 2265 #molecular-weight 249556 #checksum 6613 SEQUENCE /// ENTRY A40701 #type complete TITLE tenascin-X precursor - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Dec-1999 ACCESSIONS A40701; A33725; C42175 REFERENCE A40701 !$#authors Bristow, J.; Tee, M.K.; Gitelman, S.E.; Mellon, S.H.; !1Miller, W.L. !$#journal J. Cell Biol. (1993) 122:265-278 !$#title Tenascin-X: a novel extracellular matrix protein encoded by !1the human XB gene overlapping P450c21B. !$#cross-references MUID:93300909; PMID:7686164 !$#accession A40701 !'##status preliminary !'##molecule_type DNA !'##residues 1-3566 ##label BRI !'##cross-references EMBL:X71937 REFERENCE A33725 !$#authors Morel, Y.; Bristow, J.; Gitelman, S.E.; Miller, W.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:6582-6586 !$#title Transcript encoded on the opposite strand of the human !1steroid 21-hydroxylase/complement component C4 gene locus. !$#cross-references MUID:89367293; PMID:2475872 !$#accession A33725 !'##molecule_type mRNA !'##residues 2748-3199,'V',3201-3298,'E',3299-3314,'G',3316-3566 ##label !1MOR !'##cross-references GB:M25813; NID:g183069; PIDN:AAA35884.1; !1PID:g183070 REFERENCE A42175 !$#authors Matsumoto, K.; Arai, M.; Ishihara, N.; Ando, A.; Inoko, H.; !1Ikemura, T. !$#journal Genomics (1992) 12:485-491 !$#title Cluster of fibronectin type III repeats found in the human !1major histocompatibility complex class III region shows the !1highest homology with the repeats in an extracellular matrix !1protein, tenascin. !$#cross-references MUID:92217969; PMID:1373119 !$#accession C42175 !'##molecule_type DNA !'##residues 1849-1936 ##label MAT !'##experimental_source clone 3.9kF3-1 !'##note sequence extracted from NCBI backbone (NCBIP:95694) GENETICS !$#gene GDB:TNXA; D6S103E; TNX; XA; XB !'##cross-references GDB:568487; OMIM:600261 !$#map_position 6p21.3-6p21.3 CLASSIFICATION #superfamily tenascin-X; EGF homology; fibrinogen beta/gamma !1homology; fibronectin type III repeat homology KEYWORDS extracellular matrix; glycoprotein FEATURE !$435-461 #domain EGF homology #label EGF\ !$748-828 #domain fibronectin type III repeat homology #label !83F1\ !$829-856 #domain fibronectin type III repeat homology #status !8atypical #label 3F2\ !$873-953 #domain fibronectin type III repeat homology #label !83F3\ !$975-1055 #domain fibronectin type III repeat homology #label !83F4\ !$1078-1158 #domain fibronectin type III repeat homology #label !83F5\ !$1167-1247 #domain fibronectin type III repeat homology #label !83F6\ !$1248-1317 #domain fibronectin type III repeat homology #status !8atypical #label 3F7\ !$1323-1403 #domain fibronectin type III repeat homology #label !83F8\ !$1412-1492 #domain fibronectin type III repeat homology #label !83F9\ !$1510-1590 #domain fibronectin type III repeat homology #label !83F10\ !$1618-1676 #domain fibronectin type III repeat homology #status !8atypical #label 3F11\ !$1678-1749 #domain fibronectin type III repeat homology #status !8atypical #label 3F12\ !$1751-1831 #domain fibronectin type III repeat homology #label !83F13\ !$1849-1929 #domain fibronectin type III repeat homology #label !83F14\ !$1955-2035 #domain fibronectin type III repeat homology #label !83F15\ !$2061-2141 #domain fibronectin type III repeat homology #label !83F16\ !$2167-2246 #domain fibronectin type III repeat homology #label !83F17\ !$2274-2354 #domain fibronectin type III repeat homology #label !83F18\ !$2382-2462 #domain fibronectin type III repeat homology #label !83F19\ !$2488-2568 #domain fibronectin type III repeat homology #label !83F20\ !$2584-2664 #domain fibronectin type III repeat homology #label !83F21\ !$2677-2757 #domain fibronectin type III repeat homology #label !83F22\ !$2771-2851 #domain fibronectin type III repeat homology #label !83F23\ !$2878-2958 #domain fibronectin type III repeat homology #label !83F24\ !$2977-3067 #domain fibronectin type III repeat homology #status !8atypical #label 3F25\ !$3078-3159 #domain fibronectin type III repeat homology #label !83F26\ !$3167-3247 #domain fibronectin type III repeat homology #label !83F27\ !$3255-3334 #domain fibronectin type III repeat homology #label !83F28\ !$3349-3557 #domain fibrinogen beta/gamma homology #label FBG SUMMARY #length 3566 #molecular-weight 385617 #checksum 7433 SEQUENCE /// ENTRY JH0675 #type complete TITLE restrictin precursor - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JH0675; PS0385; S23254 REFERENCE JH0675 !$#authors Noerenberg, U.; Wille, H.; Wolff, J.M.; Frank, R.; Rathjen, !1F.G. !$#journal Neuron (1992) 8:849-863 !$#title The chicken neural extracellular matrix molecule restrictin: !1similarity with EGF-, fibronectin type III-, and !1fibrinogen-like motifs. !$#cross-references MUID:92265298; PMID:1375037 !$#accession JH0675 !'##molecule_type mRNA !'##residues 1-1353 ##label NOE !'##cross-references GB:X64649; NID:g63613; PIDN:CAA45920.1; PID:g63614 !'##experimental_source brain !$#accession PS0385 !'##molecule_type protein !'##residues 579-586;827-840 ##label NOE1 COMMENT This protein is a neural extracellular matrix protein !1implicated in neural cell attachment. CLASSIFICATION #superfamily restrictin; EGF homology; fibrinogen beta/gamma !1homology; fibronectin type III repeat homology KEYWORDS calcium binding; cell adhesion; duplication; extracellular !1matrix; glycoprotein; homotrimer; tandem repeat FEATURE !$1-33 #domain signal sequence #status predicted #label SIG\ !$34-1353 #product restrictin #status predicted #label MAT\ !$203-229 #domain EGF homology #label EG1\ !$234-260 #domain EGF homology #label EG2\ !$265-291 #domain EGF homology #label EG3\ !$296-322 #domain EGF homology #label EG4\ !$324-405 #domain fibronectin type III repeat homology #label !8FN1\ !$413-494 #domain fibronectin type III repeat homology #label !8FN2\ !$502-584 #domain fibronectin type III repeat homology #label !8FN3\ !$592-676 #domain fibronectin type III repeat homology #label !8FN4\ !$684-764 #domain fibronectin type III repeat homology #label !8FN5\ !$772-853 #domain fibronectin type III repeat homology #label !8FN6\ !$861-941 #domain fibronectin type III repeat homology #label !8FN7\ !$949-1027 #domain fibronectin type III repeat homology #label !8FN8\ !$1035-1115 #domain fibronectin type III repeat homology #label !8FN9\ !$1130-1338 #domain fibrinogen beta/gamma homology #label FBG\ !$1272-1286 #region calcium binding #status predicted\ !$53,197,277,391,469, !$580,734,790,960, !$1031,1041,1256,1342 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1353 #molecular-weight 148278 #checksum 975 SEQUENCE /// ENTRY JQ1322 #type complete TITLE tenascin precursor - mouse ALTERNATE_NAMES contactin; hexabrachion ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS JQ1322; A37936; B37936; S14571; S50209 REFERENCE JQ1322 !$#authors Saga, Y.; Tsukamoto, T.; Jing, N.; Kusakabe, M.; Sakakura, !1T. !$#journal Gene (1991) 104:177-185 !$#title Murine tenascin: cDNA cloning, structure and temporal !1expression of isoforms. !$#cross-references MUID:92009211; PMID:1717349 !$#accession JQ1322 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-2019 ##label SAG !'##cross-references GB:D90343; NID:g220609; PIDN:BAA14355.1; !1PID:g220610 !'##experimental_source cell line 2H6GR !'##note the authors translated the codon ATG for residue 60 as Trp REFERENCE A37936 !$#authors Weller, A.; Beck, S.; Ekblom, P. !$#journal J. Cell Biol. (1991) 112:355-362 !$#title Amino acid sequence of mouse tenascin and differential !1expression of two tenascin isoforms during embryogenesis. !$#cross-references MUID:91107734; PMID:1703162 !$#accession A37936 !'##status preliminary !'##molecule_type mRNA !'##residues 1-201,'E',203-317,'S',319-620,622-1010,'N',1012-1018,'S', !11020-1024,'H',1026-1305,'S',1307-2019 ##label WEL !'##cross-references GB:X56304 !$#accession B37936 !'##status preliminary; nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-201,'E',203-317,'S',319-620,622-1010,'N',1012-1018,'S', !11020-1024,'H',1026-1071,1527-2019 ##label WE2 !'##cross-references GB:X56304 REFERENCE S14571 !$#authors Weller, A.; Beck, S.; Ekblom, P. !$#submission submitted to the EMBL Data Library, August 1990 !$#description Aminoacid sequence of mouse tenascin and differential !1expression of two tenascin isoforms during embryogenesis. !$#accession S14571 !'##status preliminary !'##molecule_type mRNA !'##residues 1-201,'E',203-317,'S',319-1018,'S',1020-1024,'H',1026-1305, !1'S',1307-2019 ##label WE3 !'##cross-references EMBL:X56304; NID:g54768; PIDN:CAA39751.1; !1PID:g54769 REFERENCE S50206 !$#authors Glumoff, V.; Savontaus, M.; Vehanen, J.; Vuorio, E. !$#journal Biochim. Biophys. Acta (1994) 1219:613-622 !$#title Analysis of aggrecan and tenascin gene expression in mouse !1skeletal tissues by Northern and in situ hybridization using !1species specific cDNA probes. !$#cross-references MUID:95035091; PMID:7524681 !$#accession S50209 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type mRNA !'##residues 46-146 ##label GLU !'##cross-references EMBL:X80281 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1994 CLASSIFICATION #superfamily tenascin; EGF homology; fibrinogen beta/gamma !1homology; fibronectin type III repeat homology KEYWORDS alternative splicing; calcium binding; cell adhesion; !1duplication; extracellular matrix; glycoprotein; hexamer; !1tandem repeat FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-2019 #product tenascin, long splice form #status predicted !8#label MAT\ !$23-1071,1527-2019 #product tenascin, short splice form #status !8predicted #label MAT2\ !$408-434 #domain EGF homology #label EGF\ !$622-703 #domain fibronectin type III repeat homology #label !8FN3A\ !$711-793 #domain fibronectin type III repeat homology #label !8FN3B\ !$802-884 #domain fibronectin type III repeat homology #label !8FN3C\ !$892-976 #domain fibronectin type III repeat homology #label !8FN3D\ !$984-1064 #domain fibronectin type III repeat homology #label !8FN3E\ !$1073-1155 #domain fibronectin type III repeat homology #label !8FN3F\ !$1346-1428 #domain fibronectin type III repeat homology #label !8FN3G\ !$1437-1519 #domain fibronectin type III repeat homology #label !8FN3H\ !$1527-1608 #domain fibronectin type III repeat homology #label !8FN3I\ !$1616-1696 #domain fibronectin type III repeat homology #label !8FN3J\ !$1704-1784 #domain fibronectin type III repeat homology #label !8FN3K\ !$1799-2007 #domain fibrinogen beta/gamma homology #label FBG\ !$38,166,184,327,788, !$1018,1079,1093, !$1119,1184,1210, !$1275,1301,1354, !$1364,1394,1627, !$1878,1980 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 2019 #molecular-weight 221877 #checksum 8219 SEQUENCE /// ENTRY S19694 #type complete TITLE tenascin precursor - pig ALTERNATE_NAMES contactin; hexabrachion ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S19694 REFERENCE S19694 !$#authors Nishi, T.; Weinstein, J.; Gillespie, W.M.; Paulson, J.C. !$#journal Eur. J. Biochem. (1991) 202:643-648 !$#title Complete primary structure of porcine tenascin. Detection of !1tenascin transcripts in adult submaxillary glands. !$#cross-references MUID:92104189; PMID:1722152 !$#accession S19694 !'##molecule_type mRNA !'##residues 1-1746 ##label NIS !'##cross-references EMBL:X61599; NID:g2124; PIDN:CAA43796.1; PID:g2125 CLASSIFICATION #superfamily tenascin; EGF homology; fibrinogen beta/gamma !1homology; fibronectin type III repeat homology KEYWORDS alternative splicing; calcium binding; cell adhesion; !1duplication; extracellular matrix; glycoprotein; hexamer; !1tandem repeat FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-1746 #product tenascin #status predicted #label MAT\ !$346-372 #domain EGF homology #label EGF\ !$377-403 #domain EGF homology #label EGF2\ !$622-703 #domain fibronectin type III repeat homology #label !8FN3A\ !$711-793 #domain fibronectin type III repeat homology #label !8FN3B\ !$802-884 #domain fibronectin type III repeat homology #label !8FN3C\ !$892-976 #domain fibronectin type III repeat homology #label !8FN3D\ !$984-1064 #domain fibronectin type III repeat homology #label !8FN3E\ !$1073-1155 #domain fibronectin type III repeat homology #label !8FN3F\ !$1164-1246 #domain fibronectin type III repeat homology #label !8FN3G\ !$1254-1335 #domain fibronectin type III repeat homology #label !8FN3H\ !$1343-1423 #domain fibronectin type III repeat homology #label !8FN3I\ !$1431-1511 #domain fibronectin type III repeat homology #label !8FN3J\ !$1526-1734 #domain fibrinogen beta/gamma homology #label FBG\ !$38,166,184,327,788, !$1034,1079,1121,1354 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1746 #molecular-weight 191398 #checksum 8396 SEQUENCE /// ENTRY A32230 #type complete TITLE tenascin precursor - chicken ALTERNATE_NAMES cytotactin; hexabrachion CONTAINS tenascin 190K; tenascin 200K ORGANISM #formal_name Gallus gallus #common_name chicken DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A32230; B32230; A33379; B33379; C33379; S01292; A30903 REFERENCE A32230 !$#authors Jones, F.S.; Hoffman, S.; Cunningham, B.A.; Edelman, G.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:1905-1909 !$#title A detailed structural model of cytotactin: protein !1homologies, alternative RNA splicing, and binding regions. !$#cross-references MUID:89184536; PMID:2467292 !$#accession A32230 !'##status preliminary !'##molecule_type DNA !'##residues 1-1810 ##label JON !'##cross-references GB:J04519; NID:g211717; PIDN:AAA48745.1; !1PID:g211718 !$#accession B32230 !'##status preliminary !'##molecule_type mRNA !'##residues 1-1044,1318-1810 ##label JO2 !'##cross-references GB:J04519 REFERENCE A33379 !$#authors Spring, J.; Beck, K.; Chiquet-Ehrismann, R. !$#journal Cell (1989) 59:325-334 !$#title Two contrary functions of tenascin: dissection of the active !1sites by recombinant tenascin fragments. !$#cross-references MUID:90030407; PMID:2478295 !$#accession A33379 !'##status preliminary; nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-204,'G',206-221,'A',223-380,'D',382-386,'H',388-444,'HN', !1447-450,'V',452-597,'E',599-841,844-887,'N',889-1247,'S', !11249-1335,'T',1337-1810 ##label SPR !'##cross-references GB:M23121; NID:g212746; PIDN:AAA49086.1; !1PID:g212749 !$#accession B33379 !'##status preliminary; nucleic acid sequence not shown; not compared !1with conceptual translation !'##molecule_type mRNA !'##residues 1-204,'G',206-221,'A',223-380,'D',382-386,'H',388-444,'HN', !1447-450,'V',452-597,'E',599-841,844-887,'N',889-1045, !11228-1247,'S',1249-1335,'T',1337-1810 ##label SP2 !$#accession C33379 !'##status preliminary; nucleic acid sequence not shown; not compared !1with conceptual translation !'##molecule_type mRNA !'##residues 1-204,'G',206-221,'A',223-380,'D',382-386,'H',388-444,'HN', !1447-450,'V',452-597,'E',599-841,844-887,'N',889-1044, !11318-1335,'T',1337-1810 ##label SP3 !'##cross-references GB:M23121 REFERENCE S01292 !$#authors Pearson, C.A.; Pearson, D.; Shibahara, S.; Hofsteenge, J.; !1Chiquet-Ehrismann, R. !$#journal EMBO J. (1988) 7:2977-2982 !$#title Tenascin: cDNA cloning and induction by TGF-beta. !$#cross-references MUID:89030589; PMID:2460335 !$#accession S01292 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 27-181,'R',183-204,'G',206-221,'A',223-380,'D',382-386,'H', !1388-444,'HN',447-450,'V',452-597,'E',599-722,'K' ##label PEA !'##cross-references EMBL:X08030 !'##note part of this sequence was confirmed by protein sequencing CLASSIFICATION #superfamily tenascin; EGF homology; fibrinogen beta/gamma !1homology; fibronectin type III repeat homology KEYWORDS alternative splicing; calcium binding; cell adhesion; !1duplication; extracellular matrix; glycoprotein; hexamer; !1tandem repeat FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-33 #domain propeptide #status predicted #label PRO\ !$34-1810 #product tenascin 230K #status predicted #label MAT\ !$223-249 #domain EGF homology #label EGF1\ !$316-342 #domain EGF homology #label EGF\ !$592-673 #domain fibronectin type III repeat homology #label !8FN3A\ !$681-765 #domain fibronectin type III repeat homology #label !8FN3B\ !$773-857 #domain fibronectin type III repeat homology #label !8FN3C\ !$865-949 #domain fibronectin type III repeat homology #label !8FN3D\ !$957-1037 #domain fibronectin type III repeat homology #label !8FN3E\ !$1046-1128 #domain fibronectin type III repeat homology #label !8FN3F\ !$1137-1219 #domain fibronectin type III repeat homology #label !8FN3G\ !$1228-1310 #domain fibronectin type III repeat homology #label !8FN3H\ !$1318-1399 #domain fibronectin type III repeat homology #label !8FN3I\ !$1407-1487 #domain fibronectin type III repeat homology #label !8FN3J\ !$1495-1575 #domain fibronectin type III repeat homology #label !8FN3K\ !$1590-1798 #domain fibrinogen beta/gamma homology #label FBG\ !$1734-1747 #domain calcium binding #status predicted #label CAB SUMMARY #length 1810 #molecular-weight 199304 #checksum 4155 SEQUENCE /// ENTRY IJFFTM #type complete TITLE cadherin-related tumor suppressor precursor - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Feb-1997 ACCESSIONS A41087; B41087 REFERENCE A41087 !$#authors Mahoney, P.A.; Weber, U.; Onofrechuk, P.; Biessmann, H.; !1Bryant, P.J.; Goodman, C.S. !$#journal Cell (1991) 67:853-868 !$#title The fat tumor suppressor gene in Drosophila encodes a novel !1member of the cadherin gene superfamily. !$#cross-references MUID:92069752; PMID:1959133 !$#accession A41087 !'##molecule_type mRNA !'##residues 143-485;1279-5147 ##label MAH !'##cross-references GB:M80537 !$#accession B41087 !'##molecule_type DNA !'##residues 1-142;487-1278 ##label MA2 !'##cross-references GB:M80537 !'##note 1229-Gly and 1233-Ser were also found GENETICS !$#gene fat !'##cross-references FlyBase:FBgn0001075 CLASSIFICATION #superfamily cadherin-related tumor suppressor; cadherin !1repeat homology; EGF homology KEYWORDS calcium binding; cell adhesion; duplication; transmembrane !1protein FEATURE !$1-35 #domain signal sequence #status predicted #label SIG\ !$36-5147 #product cadherin-related tumor suppressor #status !8predicted #label MAT\ !$36-4583 #domain extracellular #status predicted #label EXT\ !$51-156 #domain cadherin repeat homology #label CR1\ !$159-270 #domain cadherin repeat homology #label CR2\ !$271-382 #domain cadherin repeat homology #label CR3\ !$390-494 #domain cadherin repeat homology #label CR4\ !$497-599 #domain cadherin repeat homology #label CR5\ !$602-708 #domain cadherin repeat homology #label CR6\ !$718-822 #domain cadherin repeat homology #label CR7\ !$831-942 #domain cadherin repeat homology #label CR8\ !$948-1049 #domain cadherin repeat homology #label CR9\ !$1052-1153 #domain cadherin repeat homology #label C10\ !$1156-1278 #domain cadherin repeat homology #label C11\ !$1281-1384 #domain cadherin repeat homology #label C12\ !$1387-1489 #domain cadherin repeat homology #label C13\ !$1492-1601 #domain cadherin repeat homology #label C14\ !$1607-1713 #domain cadherin repeat homology #label C15\ !$1717-1823 #domain cadherin repeat homology #label C16\ !$1826-1922 #domain cadherin repeat homology #label C17\ !$1925-2027 #domain cadherin repeat homology #label C18\ !$2028-2167 #domain cadherin repeat homology #label C19\ !$2169-2278 #domain cadherin repeat homology #label C20\ !$2281-2384 #domain cadherin repeat homology #label C99\ !$2387-2491 #domain cadherin repeat homology #label C21\ !$2494-2596 #domain cadherin repeat homology #label C22\ !$2599-2703 #domain cadherin repeat homology #label C23\ !$2707-2810 #domain cadherin repeat homology #label C24\ !$2813-2913 #domain cadherin repeat homology #label C25\ !$2915-3013 #domain cadherin repeat homology #label C26\ !$3014-3124 #domain cadherin repeat homology #label C27\ !$3127-3229 #domain cadherin repeat homology #label C28\ !$3232-3334 #domain cadherin repeat homology #label C29\ !$3337-3439 #domain cadherin repeat homology #label C30\ !$3442-3545 #domain cadherin repeat homology #label C31\ !$3548-3651 #domain cadherin repeat homology #label C32\ !$3654-3756 #domain cadherin repeat homology #label C33\ !$3954-4010 #domain EGF homology #label EG1\ !$4017-4048 #domain EGF homology #label EG2\ !$4056-4089 #domain EGF homology #label EG3\ !$4096-4127 #domain EGF homology #label EG4\ !$4584-4609 #domain transmembrane #status predicted #label TMM\ !$4610-5147 #domain intracellular #status predicted #label INT SUMMARY #length 5147 #molecular-weight 564895 #checksum 6994 SEQUENCE /// ENTRY IJHUCN #type complete TITLE cadherin 2 precursor - human ALTERNATE_NAMES N-cadherin; neuronal cadherin ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 22-Jun-1999 ACCESSIONS A38870; S11487; JQ0751; S13799 REFERENCE A38870 !$#authors Reid, R.A. !$#submission submitted to the EMBL Data Library, November 1990 !$#accession A38870 !'##molecule_type mRNA !'##residues 1-906 ##label REI !'##cross-references EMBL:X54315; NID:g34998; PIDN:CAA38213.1; !1PID:g34999 REFERENCE S11487 !$#authors Reid, R.A.; Hemperly, J.J. !$#journal Nucleic Acids Res. (1990) 18:5896 !$#title Human N-cadherin: nucleotide and deduced amino acid !1sequence. !$#cross-references MUID:91016946; PMID:2216790 !$#accession S11487 !'##molecule_type mRNA !'##residues 1-340,'N',342-698,'R',700-704,'F',706-906 ##label RE2 !'##cross-references EMBL:X54315 !'##note this sequence has been revised in reference A38870 REFERENCE JQ0751 !$#authors Walsh, F.S.; Barton, C.H.; Putt, W.; Moore, S.E.; Kelsell, !1D.; Spurr, N.; Goodfellow, P.N. !$#journal J. Neurochem. (1990) 55:805-812 !$#title N-cadherin gene maps to human chromosome 18 and is not !1linked to the E-cadherin gene. !$#cross-references MUID:90347462; PMID:2384753 !$#accession JQ0751 !'##molecule_type mRNA !'##residues 160-194,'IR',197-211,'L',213-227,'Q',229,'N',231-235,'G', !1237-248,'T',250-356,'N',358-530,'KYL',533-906 ##label WAL !'##cross-references GB:M34064 COMMENT Cadherins mediate calcium-dependent intercellular adhesion !1and are thought to be involved in the sorting of different !1cell types during morphogenesis. GENETICS !$#gene GDB:CDH2; NCAD !'##cross-references GDB:128185; OMIM:114020 !$#map_position 18q12.1-18q12.1 CLASSIFICATION #superfamily cadherin; cadherin repeat homology KEYWORDS calcium binding; cell adhesion; duplication; glycoprotein; !1transmembrane protein FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-159 #domain propeptide #status predicted #label PRO\ !$160-906 #product N-cadherin #status predicted #label MAT\ !$160-714 #domain extracellular #status predicted #label EXT\ !$162-267 #domain cadherin repeat homology #label CR1\ !$237-242 #region cadherin binding #status predicted\ !$270-382 #domain cadherin repeat homology #label CR2\ !$385-497 #domain cadherin repeat homology #label CR3\ !$500-605 #domain cadherin repeat homology #label CR4\ !$606-712 #domain cadherin repeat homology #label CR5\ !$715-746 #domain transmembrane #status predicted #label TMM\ !$747-906 #domain intracellular #status predicted #label INT\ !$865-878 #region serine-rich\ !$190,273,325,402, !$572,622,651,692 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 906 #molecular-weight 99864 #checksum 9191 SEQUENCE /// ENTRY IJBOCN #type fragment TITLE N-cadherin precursor - bovine (fragment) ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 22-Jun-1999 ACCESSIONS S11693 REFERENCE S11693 !$#authors Liaw, C.W.; Cannon, C.; Power, M.D.; Kiboneka, P.K.; Rubin, !1L.L. !$#journal EMBO J. (1990) 9:2701-2708 !$#title Identification and cloning of two species of cadherins in !1bovine endothelial cells. !$#cross-references MUID:90360979; PMID:2390969 !$#accession S11693 !'##molecule_type mRNA !'##residues 1-877 ##label LIA !'##cross-references EMBL:X53615; NID:g164; PIDN:CAA37677.1; PID:g664894 COMMENT Cadherins mediate calcium-dependent intercellular adhesion, !1and are thought to be involved in the sorting of different !1cell types during morphogenesis. CLASSIFICATION #superfamily cadherin; cadherin repeat homology KEYWORDS calcium binding; cell adhesion; duplication; glycoprotein; !1transmembrane protein FEATURE !$1-130 #domain propeptide (fragment) #status predicted !8#label PRO\ !$131-877 #product N-cadherin #status predicted #label MAT\ !$131-685 #domain extracellular #status predicted #label EXT\ !$133-238 #domain cadherin repeat homology #label CR1\ !$208-213 #region cadherin binding #status predicted\ !$241-353 #domain cadherin repeat homology #label CR2\ !$356-468 #domain cadherin repeat homology #label CR3\ !$471-576 #domain cadherin repeat homology #label CR4\ !$577-685 #domain cadherin repeat homology #label CR5\ !$686-717 #domain transmembrane #status predicted #label TMM\ !$718-877 #domain intracellular #status predicted #label INT\ !$836-849 #region serine-rich\ !$161,244,296,373, !$543,593,622,663 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 877 #checksum 8685 SEQUENCE /// ENTRY IJMSCN #type complete TITLE N-cadherin precursor, neuronal - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 22-Jun-1999 ACCESSIONS A32759; A46163 REFERENCE A32759 !$#authors Miyatani, S.; Shimamura, K.; Hatta, M.; Nagafuchi, A.; Nose, !1A.; Matsunaga, M.; Hatta, K.; Takeichi, M. !$#journal Science (1989) 245:631-635 !$#title Neural cadherin: role in selective cell-cell adhesion. !$#cross-references MUID:89346748; PMID:2762814 !$#accession A32759 !'##molecule_type mRNA !'##residues 1-906 ##label MIY !'##cross-references GB:M31131; NID:g192327; PIDN:AAA37353.1; !1PID:g309125 REFERENCE A46163 !$#authors Miyatani, S.; Copeland, N.G.; Gilbert, D.J.; Jenkins, N.A.; !1Takeichi, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:8443-8447 !$#title Genomic structure and chromosomal mapping of the mouse !1N-cadherin gene. !$#cross-references MUID:92409532; PMID:1528849 !$#accession A46163 !'##status preliminary !'##molecule_type DNA !'##residues 839-906 ##label MI2 !'##cross-references GB:S45011; NID:g256010; PIDN:AAB23356.1; !1PID:g256011 !'##note sequence extracted from NCBI backbone (NCBIN:113759, !1NCBIP:113760) COMMENT Cadherins mediate calcium-dependent intercellular adhesion, !1and are thought to be involved in the sorting of different !1cell types during morphogenesis. CLASSIFICATION #superfamily cadherin; cadherin repeat homology KEYWORDS calcium binding; cell adhesion; duplication; glycoprotein; !1transmembrane protein FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-159 #domain propeptide #status predicted #label PRO\ !$160-906 #product N-cadherin #status predicted #label MAT\ !$160-714 #domain extracellular #status predicted #label EXT\ !$162-267 #domain cadherin repeat homology #label CR1\ !$237-242 #region cadherin binding #status predicted\ !$270-382 #domain cadherin repeat homology #label CR2\ !$385-497 #domain cadherin repeat homology #label CR3\ !$500-605 #domain cadherin repeat homology #label CR4\ !$606-714 #domain cadherin repeat homology #label CR5\ !$715-746 #domain transmembrane #status predicted #label TMM\ !$747-906 #domain intracellular #status predicted #label INT\ !$865-878 #region serine-rich\ !$190,273,325,402, !$572,651,692 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 906 #molecular-weight 99760 #checksum 7386 SEQUENCE /// ENTRY IJCHCN #type complete TITLE N-cadherin precursor, neuronal - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 22-Jun-1999 ACCESSIONS A29964 REFERENCE A29964 !$#authors Hatta, K.; Nose, A.; Nagafuchi, A.; Takeichi, M. !$#journal J. Cell Biol. (1988) 106:873-881 !$#title Cloning and expression of cDNA encoding a neural !1calcium-dependent cell adhesion molecule: its identity in !1the cadherin gene family. !$#cross-references MUID:88153917; PMID:2831236 !$#accession A29964 !'##molecule_type mRNA !'##residues 1-912 ##label HAT !'##cross-references GB:X07277; NID:g63649; PIDN:CAA30258.1; PID:g63650 COMMENT Cadherins mediate calcium-dependent intercellular adhesion, !1and are thought to be involved in the sorting of different !1cell types during morphogenesis. CLASSIFICATION #superfamily cadherin; cadherin repeat homology KEYWORDS calcium binding; cell adhesion; duplication; glycoprotein; !1transmembrane protein FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-164 #domain propeptide #status predicted #label PRO\ !$165-912 #product N-cadherin #status predicted #label MAT\ !$165-720 #domain extracellular #status predicted #label EXT\ !$167-272 #domain cadherin repeat homology #label CR1\ !$242-247 #region cadherin binding #status predicted\ !$275-387 #domain cadherin repeat homology #label CR2\ !$390-502 #domain cadherin repeat homology #label CR3\ !$505-611 #domain cadherin repeat homology #label CR4\ !$612-720 #domain cadherin repeat homology #label CR5\ !$721-752 #domain transmembrane #status predicted #label TMM\ !$753-912 #domain intracellular #status predicted #label INT\ !$869-884 #region serine-rich\ !$278,330,407,578, !$628,657 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 912 #molecular-weight 100464 #checksum 7687 SEQUENCE /// ENTRY IJXLC2 #type complete TITLE N-cadherin 2 precursor - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 22-Jun-1999 ACCESSIONS A43785 REFERENCE A43785 !$#authors Ginsberg, D.; DeSimone, D.; Geiger, B. !$#journal Development (1991) 111:315-325 !$#title Expression of a novel cadherin (EP-cadherin) in unfertilized !1eggs and early Xenopus embryos. !$#cross-references MUID:91372132; PMID:1893866 !$#accession A43785 !'##molecule_type mRNA !'##residues 1-906 ##label GIN !'##cross-references GB:X57675; NID:g64910; PIDN:CAA40867.1; PID:g64911 COMMENT Cadherins mediate calcium-dependent intercellular adhesion, !1and are thought to be involved in the sorting of different !1cell types during morphogenesis. CLASSIFICATION #superfamily cadherin; cadherin repeat homology KEYWORDS calcium binding; cell adhesion; duplication; glycoprotein; !1transmembrane protein FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-160 #domain propeptide #status predicted #label PRO\ !$161-906 #product N-cadherin 2 #status predicted #label MAT\ !$161-714 #domain extracellular #status predicted #label EXT\ !$163-268 #domain cadherin repeat homology #label CR1\ !$238-243 #region cadherin binding #status predicted\ !$271-383 #domain cadherin repeat homology #label CR2\ !$386-498 #domain cadherin repeat homology #label CR3\ !$501-606 #domain cadherin repeat homology #label CR4\ !$607-714 #domain cadherin repeat homology #label CR5\ !$715-746 #domain transmembrane #status predicted #label TMM\ !$747-906 #domain intracellular #status predicted #label INT\ !$863-878 #region serine-rich\ !$274,326,403,573, !$623,652,693 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 906 #molecular-weight 100392 #checksum 5038 SEQUENCE /// ENTRY IJXLC1 #type complete TITLE N-cadherin 1 precursor - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 19-Jan-1996 ACCESSIONS JQ0442 REFERENCE JQ0442 !$#authors Detrick, R.J.; Dickey, D.; Kintner, C.R. !$#journal Neuron (1990) 4:493-506 !$#title The effects of N-cadherin misexpression on morphogenesis in !1Xenopus embryos. !$#cross-references MUID:90211966; PMID:2322458 !$#accession JQ0442 !'##molecule_type mRNA !'##residues 1-905 ##label DET COMMENT Cadherins mediate calcium-dependent intercellular adhesion, !1and are thought to be involved in the sorting of different !1cell types during morphogenesis. CLASSIFICATION #superfamily cadherin; cadherin repeat homology KEYWORDS calcium binding; cell adhesion; duplication; glycoprotein; !1transmembrane protein FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-160 #domain propeptide #status predicted #label PRO\ !$161-905 #product N-cadherin 1 #status predicted #label MAT\ !$161-713 #domain extracellular #status predicted #label EXT\ !$163-268 #domain cadherin repeat homology #label CR1\ !$238-243 #region cadherin binding #status predicted\ !$271-383 #domain cadherin repeat homology #label CR2\ !$386-498 #domain cadherin repeat homology #label CR3\ !$501-606 #domain cadherin repeat homology #label CR4\ !$607-713 #domain cadherin repeat homology #label CR5\ !$714-745 #domain transmembrane #status predicted #label TMM\ !$746-905 #domain intracellular #status predicted #label INT\ !$862-877 #region serine-rich\ !$191,274,326,403, !$573,623,651,692 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 905 #molecular-weight 100548 #checksum 9373 SEQUENCE /// ENTRY A47543 #type complete TITLE R-cadherin precursor - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 03-May-1994 #sequence_revision 26-May-1994 #text_change 22-Jun-1999 ACCESSIONS A47543; I55501 REFERENCE A47543 !$#authors Hutton, J.C.; Christofori, G.; Chi, W.Y.; Edman, U.; Guest, !1P.C.; Hanahan, D.; Kelly, R.B. !$#journal Mol. Endocrinol. (1993) 7:1151-1160 !$#title Molecular cloning of mouse pancreatic islet R-cadherin: !1differential expression in endocrine and exocrine tissue. !$#cross-references MUID:94067164; PMID:8247017 !$#accession A47543 !'##molecule_type mRNA !'##residues 1-913 ##label HUT !'##cross-references EMBL:X69966; NID:g429111; PIDN:CAA49589.1; !1PID:g429112 REFERENCE I55501 !$#authors Matsunami, H.; Miyatani, S.; Inoue, T.; Copeland, N.; !1Gilbert, D.; Jenkins, N.; Takeichi, M. !$#journal J. Cell Sci. (1993) 106:401-409 !$#title Cell binding specificity of mouse R-cadherin and chromosomal !1mapping of the gene. !$#cross-references MUID:94095672; PMID:8270638 !$#accession I55501 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-913 ##label RES !'##cross-references GB:D14888; NID:g457658; PIDN:BAA03605.1; !1PID:g457659 COMMENT Cadherins mediate calcium-dependent intercellular adhesion !1and are thought to be involved in the sorting of different !1cell types during morphogenesis. CLASSIFICATION #superfamily cadherin; cadherin repeat homology KEYWORDS calcium binding; cell adhesion; duplication; glycoprotein; !1transmembrane protein FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-166 #domain propeptide #status predicted #label PRO\ !$167-913 #product R-cadherin #status predicted #label MAT\ !$167-721 #domain extracellular #status predicted #label EXT\ !$169-274 #domain cadherin repeat homology #label CR1\ !$244-249 #region cadherin binding #status predicted\ !$277-389 #domain cadherin repeat homology #label CR2\ !$300-304 #domain calcium binding #status predicted #label CAB\ !$392-504 #domain cadherin repeat homology #label CR3\ !$507-612 #domain cadherin repeat homology #label CR4\ !$613-721 #domain cadherin repeat homology #label CR5\ !$722-753 #domain transmembrane #status predicted #label TMM\ !$754-913 #domain intracellular #status predicted #label INT\ !$870-885 #region serine-rich\ !$280,409,554,629, !$658,699 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 913 #molecular-weight 100029 #checksum 4483 SEQUENCE /// ENTRY IJCHCR #type complete TITLE R-cadherin precursor - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jun-2000 ACCESSIONS JH0424 REFERENCE JH0424 !$#authors Inuzuka, H.; Miyatani, S.; Takeichi, M. !$#journal Neuron (1991) 7:69-79 !$#title R-cadherin: a novel Ca2+-dependent cell-cell adhesion !1molecule expressed in the retina. !$#cross-references MUID:91299341; PMID:1712604 !$#accession JH0424 !'##molecule_type mRNA !'##residues 1-913 ##label INU !'##cross-references GB:D14459; GB:D00849; NID:g222854; PIDN:BAA03356.1; !1PID:g222855 !'##experimental_source retina COMMENT Cadherins mediate calcium-dependent intercellular adhesion, !1and are thought to be involved in the sorting of different !1cell types during morphogenesis. CLASSIFICATION #superfamily cadherin; cadherin repeat homology KEYWORDS calcium binding; cell adhesion; duplication; glycoprotein; !1retina; transmembrane protein FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-166 #domain propeptide #status predicted #label PRO\ !$167-913 #product R-cadherin #status predicted #label MAT\ !$167-721 #domain extracellular #status predicted #label EXT\ !$169-274 #domain cadherin repeat homology #label CR1\ !$244-249 #region cadherin binding #status predicted\ !$277-389 #domain cadherin repeat homology #label CR2\ !$392-504 #domain cadherin repeat homology #label CR3\ !$507-612 #domain cadherin repeat homology #label CR4\ !$613-721 #domain cadherin repeat homology #label CR5\ !$722-753 #domain transmembrane #status predicted #label TMM\ !$754-913 #domain intracellular #status predicted #label INT\ !$870-885 #region serine-rich\ !$280,409,554,629, !$658,699 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 913 #molecular-weight 100885 #checksum 5917 SEQUENCE /// ENTRY IJHUCE #type complete TITLE cadherin 1 precursor [validated] - human ALTERNATE_NAMES ARC-1; cell CAM 120/80; E-cadherin; epithelial cadherin; L-CAM; uvomorulin ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 08-Dec-2000 ACCESSIONS S37654; S31430; S05475; S31460; S06716; A57171; JC2230; !1I52294; I52704; S25141 REFERENCE S37654 !$#authors Bussemakers, M.J.G.; van Bokhoven, A.; Mees, S.G.M.; Kemler, !1R.; Schalken, J.A. !$#journal Mol. Biol. Rep. (1993) 17:123-128 !$#title Molecular cloning and characterization of the human !1E-cadherin cDNA. !$#cross-references MUID:93211394; PMID:8459805 !$#accession S37654 !'##molecule_type mRNA !'##residues 1-882 ##label BUS !'##cross-references EMBL:Z13009; NID:g31072; PIDN:CAA78353.1; !1PID:g31073 REFERENCE S31430 !$#authors Kelker, W.; Warda, A.; Oda, T.; Hirohashi, S.; Kemler, R.; !1Birchmeier, W. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Sequence of human E-cadherin cDNA. !$#accession S31430 !'##molecule_type mRNA !'##residues 1-542,'F',544-882 ##label KEL !'##cross-references EMBL:Z18923; NID:g31074; PIDN:CAA79356.1; !1PID:g31075 REFERENCE S05475 !$#authors Mansouri, A.; Spurr, N.; Goodfellow, P.N.; Kemler, R. !$#journal Differentiation (1988) 38:67-71 !$#title Characterization and chromosomal localization of the gene !1encoding the human cell adhesion molecule uvomorulin. !$#cross-references MUID:89031725; PMID:3263290 !$#accession S05475 !'##molecule_type mRNA !'##residues 157-311 ##label MAN !'##cross-references EMBL:X12790 !'##note nucleotide sequence is not complete REFERENCE S31460 !$#authors Frixen, U.H. !$#submission submitted to the EMBL Data Library, March 1990 !$#accession S31460 !'##molecule_type mRNA !'##residues 265-392 ##label FRI !'##cross-references EMBL:X52279; NID:g28821; PIDN:CAA36522.1; !1PID:g28822 REFERENCE S06716 !$#authors Wheelock, M.J.; Buck, C.A.; Bechtol, K.B.; Damsky, C.H. !$#journal J. Cell. Biochem. (1987) 34:187-202 !$#title Soluble 80-kd fragment of cell-CAM 120/80 disrupts cell-cell !1adhesion. !$#cross-references MUID:87280410; PMID:3611200 !$#accession S06716 !'##molecule_type protein !'##residues 'XQ',157-162,'V',164-179 ##label WHE REFERENCE A57171 !$#authors Berx, G.; Staes, K.; van Hengel, J.; Molemans, F.; !1Bussemakers, M.J.G.; van Bokhoven, A.; van Roy, F. !$#journal Genomics (1995) 26:281-289 !$#title Cloning and characterization of the human invasion !1suppressor gene E-cadherin (CDH1). !$#cross-references MUID:95324920; PMID:7601454 !$#accession A57171 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type DNA !'##residues 1-30,32-882 ##label BER !'##cross-references GB:L34784 REFERENCE JC2230 !$#authors Rimm, D.L.; Morrow, J.S. !$#journal Biochem. Biophys. Res. Commun. (1994) 200:1754-1761 !$#title Molecular cloning of human E-cadherin suggests a novel !1subdivision of the cadherin superfamily. !$#cross-references MUID:94242050; PMID:8185635 !$#accession JC2230 !'##molecule_type mRNA !'##residues 1-9,'G',11-15,'RSPLGSQERSPPPCLTRELHVHGAPAPPEKRPR',52-67, !1'I',69,'LTPIP',76-94,'TDP',98-99,'GLR',103-482,'G',484-529, !1'R',531-614,'H',616-633,'RVP',637-867,'P',869-881,'H' !1##label RIM !'##cross-references GB:L08599; NID:g340184; PIDN:AAA61259.1; !1PID:g340185 !'##note the majority of differences between this and other reports !1represent apparant frameshift errors !'##note the authors translated the codon CCG for residue 868 as Arg REFERENCE I52294 !$#authors Bussemakers, M.J.G.; Giroldi, L.A.; van Bokhoven, A.; !1Schalken, J.A. !$#journal Biochem. Biophys. Res. Commun. (1994) 203:1284-1290 !$#title Transcriptional regulation of the human E-cadherin gene in !1human prostate cancer cell lines. !$#cross-references MUID:94380041; PMID:8093045 !$#accession I52294 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-16 ##label RES !'##cross-references GB:L34545; NID:g509604; PIDN:AAA21764.1; !1PID:g509605 REFERENCE I52704 !$#authors Becker, K.F.; Atkinson, M.J.; Reich, U.; Becker, I.; !1Nekarda, H.; Siewert, J.R.; Hofler, H. !$#journal Cancer Res. (1994) 54:3845-3852 !$#title E-cadherin gene mutations provide clues to diffuse type !1gastric carcinomas. !$#cross-references MUID:94306394; PMID:8033105 !$#accession I52704 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 337-476 ##label RE2 !'##cross-references GB:S72492; NID:g632756; PIDN:AAD14108.1; !1PID:g4261808 COMMENT Cadherins mediate calcium-dependent intercellular adhesion !1and are thought to be involved in the sorting of different !1cell types during morphogenesis. GENETICS !$#gene GDB:CDH1; UVO !'##cross-references GDB:120484; OMIM:192090 !$#map_position 16q22.1-16q22.1 !$#introns 379/3; 440/3 CLASSIFICATION #superfamily cadherin; cadherin repeat homology KEYWORDS calcium binding; cell adhesion; duplication; glycoprotein; !1transmembrane protein FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-154 #domain propeptide #status predicted #label PRO\ !$155-882 #product E-cadherin #status experimental #label MAT\ !$155-697 #domain extracellular #status predicted #label EXT\ !$157-262 #domain cadherin repeat homology #label CR1\ !$232-237 #region cadherin binding #status predicted\ !$265-375 #domain cadherin repeat homology #label CR2\ !$378-486 #domain cadherin repeat homology #label CR3\ !$487-595 #domain cadherin repeat homology #label CR4\ !$596-700 #domain cadherin repeat homology #label CR5\ !$698-731 #domain transmembrane #status predicted #label TMM\ !$732-882 #domain intracellular #status predicted #label INT\ !$840-853 #region serine-rich\ !$376,558,570,622, !$637,849 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 882 #molecular-weight 97455 #checksum 5112 SEQUENCE /// ENTRY IJMSCE #type complete TITLE E-cadherin precursor, epithelial - mouse ALTERNATE_NAMES uvomorulin ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 22-Jun-1999 ACCESSIONS S04528; S03160; I49565; S48735 REFERENCE S04528 !$#authors Nagafuchi, A.; Shirayoshi, Y.; Okazaki, K.; Yasuda, K.; !1Takeichi, M. !$#journal Nature (1987) 329:341-343 !$#title Transformation of cell adhesion properties by exogenously !1introduced E-cadherin cDNA. !$#cross-references MUID:87315445; PMID:3498123 !$#accession S04528 !'##molecule_type mRNA !'##residues 1-412,'V',414-884 ##label NAG !'##cross-references EMBL:X06115 REFERENCE S03160 !$#authors Ringwald, M.; Schuh, R.; Vestweber, D.; Eistetter, H.; !1Lottspeich, F.; Engel, J.; Doelz, R.; Jaehnig, F.; Epplen, !1J.; Mayer, S.; Mueller, C.; Kemler, R. !$#journal EMBO J. (1987) 6:3647-3653 !$#title The structure of cell adhesion molecule uvomorulin. Insights !1into the molecular mechanism of Ca(2+)-dependent cell !1adhesion. !$#cross-references MUID:88111553; PMID:3501370 !$#accession S03160 !'##molecule_type mRNA !'##residues 157-884 ##label RIN !'##cross-references EMBL:X06339 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE I49565 !$#authors Behrens, J.; Loewrick, O.; Klein-Hitpass, L.; Birchmeier, W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:11495-11499 !$#title The E-cadherin promoter: Functional analysis of a G-C-rich !1region and an epithelial cell-specific palindromic !1regulatory element. !$#cross-references MUID:92107977; PMID:1763063 !$#accession I49565 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-15 ##label RES !'##cross-references GB:M81449; NID:g192325; PIDN:AAA37352.1; !1PID:g192326 REFERENCE S48735 !$#authors Tong, K.I.; Yau, P.; Overduin, M.; Bagby, S.; Porumb, T.; !1Takeichi, M.; Ikura, M. !$#journal FEBS Lett. (1994) 352:318-322 !$#title Purification and spectroscopic characterization of a !1recombinant amino-terminal polypeptide fragment of mouse !1epithelial cadherin. !$#cross-references MUID:95010732; PMID:7925993 !$#accession S48735 !'##status preliminary !'##molecule_type protein !'##residues 156-300 ##label TON COMMENT Cadherins mediate calcium-dependent intercellular adhesion, !1and are thought to be involved in the sorting of different !1cell types during morphogenesis. GENETICS !$#gene E-cadherin CLASSIFICATION #superfamily cadherin; cadherin repeat homology KEYWORDS calcium binding; cell adhesion; duplication; glycoprotein; !1transmembrane protein FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-156 #domain propeptide #status predicted #label PRO\ !$157-884 #product E-cadherin, epithelial #status experimental !8#label MAT\ !$157-699 #domain extracellular #status predicted #label EXT\ !$159-264 #domain cadherin repeat homology #label CR1\ !$234-239 #region cadherin binding #status predicted\ !$267-377 #domain cadherin repeat homology #label CR2\ !$380-488 #domain cadherin repeat homology #label CR3\ !$489-597 #domain cadherin repeat homology #label CR4\ !$598-702 #domain cadherin repeat homology #label CR5\ !$702-733 #domain transmembrane #status predicted #label TMM\ !$734-884 #domain intracellular #status predicted #label INT\ !$842-855 #region serine-rich\ !$560,639 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 884 #molecular-weight 98255 #checksum 2268 SEQUENCE /// ENTRY IJCHCL #type complete TITLE E-cadherin precursor, hepatic - chicken ALTERNATE_NAMES L-CAM; liver cell adhesion molecule ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 25-Oct-1996 ACCESSIONS A30201; A29866; B29866 REFERENCE A30201 !$#authors Sorkin, B.C.; Hemperly, J.J.; Edelman, G.M.; Cunningham, !1B.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:7617-7621 !$#title Structure of the gene for the liver cell adhesion molecule, !1L-CAM. !$#cross-references MUID:89017248; PMID:3174655 !$#accession A30201 !'##molecule_type mRNA !'##residues 1-81 ##label SOR !'##cross-references EMBL:J04074 REFERENCE A29866 !$#authors Gallin, W.J.; Sorkin, B.C.; Edelman, G.M.; Cunningham, B.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:2808-2812 !$#title Sequence analysis of a cDNA clone encoding the liver cell !1adhesion molecule, L-CAM. !$#cross-references MUID:87204217; PMID:3472238 !$#accession A29866 !'##molecule_type mRNA !'##residues 51-887 ##label GA1 !'##cross-references EMBL:M16260 !$#accession B29866 !'##molecule_type protein !'##residues 161-172;323-336;386-407;533-551 ##label GA2 COMMENT Cadherins mediate calcium-dependent intercellular adhesion, !1and are thought to be involved in the sorting of different !1cell types during morphogenesis. GENETICS !$#introns 23/3; 62/1; 138/1 183/3; 235/3; 284/1; 342/3; 385/3; 447/3; !1529/2; 577/1; 652/1; 726/1; 769/3; 817/3 CLASSIFICATION #superfamily cadherin; cadherin repeat homology KEYWORDS calcium binding; cell adhesion; duplication; glycoprotein; !1liver; transmembrane protein FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-160 #domain propeptide #status predicted #label PRO\ !$161-887 #product E-cadherin, hepatic #status experimental !8#label MAT\ !$161-704 #domain extracellular #status predicted #label EXT\ !$163-268 #domain cadherin repeat homology #label CR1\ !$238-243 #region cadherin binding #status predicted\ !$271-381 #domain cadherin repeat homology #label CR2\ !$384-493 #domain cadherin repeat homology #label CR3\ !$494-601 #domain cadherin repeat homology #label CR4\ !$602-704 #domain cadherin repeat homology #label CR5\ !$705-735 #domain transmembrane #status predicted #label TMM\ !$736-887 #domain intracellular #status predicted #label INT\ !$844-857 #region serine-rich\ !$291,346,564,643 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 887 #molecular-weight 97782 #checksum 4351 SEQUENCE /// ENTRY IJHUCP #type complete TITLE cadherin 3 precursor - human ALTERNATE_NAMES P-cadherin; placental cadherin ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 22-Jun-1999 ACCESSIONS A33659 REFERENCE A33659 !$#authors Shimoyama, Y.; Yoshida, T.; Terada, M.; Shimosato, Y.; Abe, !1O.; Hirohashi, S. !$#journal J. Cell Biol. (1989) 109:1787-1794 !$#title Molecular cloning of a human Ca(2+)-dependent cell-cell !1adhesion molecule homologous to mouse placental cadherin: !1its low expression in human placental tissues. !$#cross-references MUID:90009051; PMID:2793940 !$#accession A33659 !'##molecule_type mRNA !'##residues 1-829 ##label SHI !'##cross-references GB:X63629; NID:g35322; PIDN:CAA45177.1; PID:g35323 COMMENT Cadherins mediate calcium-dependent intercellular adhesion, !1and are thought to be involved in the sorting of different !1cell types during morphogenesis. GENETICS !$#gene GDB:CDH3 !'##cross-references GDB:132860; OMIM:114021 !$#map_position 16q24.1-16qter CLASSIFICATION #superfamily cadherin; cadherin repeat homology KEYWORDS calcium binding; cell adhesion; duplication; glycoprotein; !1transmembrane protein FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-107 #domain propeptide #status predicted #label PRO\ !$108-829 #product P-cadherin #status predicted #label MAT\ !$108-650 #domain extracellular #status predicted #label EXT\ !$110-215 #domain cadherin repeat homology #label CR1\ !$185-190 #region cadherin binding #status predicted\ !$218-328 #domain cadherin repeat homology #label CR2\ !$331-440 #domain cadherin repeat homology #label CR3\ !$441-548 #domain cadherin repeat homology #label CR4\ !$549-652 #domain cadherin repeat homology #label CR5\ !$653-677 #domain transmembrane #status predicted #label TMM\ !$678-829 #domain intracellular #status predicted #label INT\ !$785-800 #region serine-rich\ !$200,566 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 829 #molecular-weight 91427 #checksum 4901 SEQUENCE /// ENTRY IJMSCP #type complete TITLE P-cadherin precursor - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 07-May-1999 ACCESSIONS S03163; S34458 REFERENCE S03163 !$#authors Nose, A.; Nagafuchi, A.; Takeichi, M. !$#journal EMBO J. (1987) 6:3655-3661 !$#title Isolation of placental cadherin cDNA: identification of a !1novel gene family of cell-cell adhesion molecules. !$#cross-references MUID:88111554; PMID:3428270 !$#accession S03163 !'##molecule_type mRNA !'##residues 1-822 ##label NOS !'##cross-references EMBL:X06340 REFERENCE S34458 !$#authors Faraldo, M.L.M.; Cano, A. !$#journal J. Mol. Biol. (1993) 231:935-941 !$#title The 5' flanking sequences of the mouse P-cadherin gene. !1Homologies to 5' sequences of the E-cadherin gene and !1identification of a first 215 base-pair intron. !$#cross-references MUID:93294853; PMID:8515462 !$#accession S34458 !'##molecule_type DNA !'##residues 1-55 ##label FAR !'##cross-references EMBL:X68057 COMMENT Cadherins mediate calcium-dependent intercellular adhesion, !1and are thought to be involved in the sorting of different !1cell types during morphogenesis. GENETICS !$#introns 16/3 CLASSIFICATION #superfamily cadherin; cadherin repeat homology KEYWORDS calcium binding; cell adhesion; duplication; glycoprotein; !1placenta; transmembrane protein FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-99 #domain propeptide #status predicted #label PRO\ !$100-822 #product P-cadherin #status predicted #label MAT\ !$100-645 #domain extracellular #status predicted #label EXT\ !$102-207 #domain cadherin repeat homology #label CR1\ !$210-320 #domain cadherin repeat homology #label CR2\ !$323-432 #domain cadherin repeat homology #label CR3\ !$433-540 #domain cadherin repeat homology #label CR4\ !$541-645 #domain cadherin repeat homology #label CR5\ !$646-670 #domain transmembrane #status predicted #label TMM\ !$671-822 #domain intracellular #status predicted #label INT\ !$778-793 #region serine-rich\ !$192,558 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 822 #molecular-weight 90728 #checksum 5860 SEQUENCE /// ENTRY IJBOCP #type fragment TITLE P-cadherin - bovine (fragment) ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 22-Jun-1999 ACCESSIONS S11694 REFERENCE S11693 !$#authors Liaw, C.W.; Cannon, C.; Power, M.D.; Kiboneka, P.K.; Rubin, !1L.L. !$#journal EMBO J. (1990) 9:2701-2708 !$#title Identification and cloning of two species of cadherins in !1bovine endothelial cells. !$#cross-references MUID:90360979; PMID:2390969 !$#accession S11694 !'##molecule_type mRNA !'##residues 1-491 ##label LIA !'##cross-references EMBL:X53614; NID:g166; PIDN:CAA37676.1; PID:g833777 COMMENT Cadherins mediate calcium-dependent intercellular adhesion, !1and are thought to be involved in the sorting of different !1cell types during morphogenesis. CLASSIFICATION #superfamily cadherin; cadherin repeat homology KEYWORDS calcium binding; cell adhesion; duplication; glycoprotein; !1transmembrane protein FEATURE !$1-491 #product P-cadherin (fragment) #status predicted !8#label MAT\ !$1-314 #domain extracellular (fragment) #status predicted !8#label EXT\ !$1-102 #domain cadherin repeat homology (fragment) #label !8CR3\ !$103-210 #domain cadherin repeat homology #label CR4\ !$211-314 #domain cadherin repeat homology #label CR5\ !$315-339 #domain transmembrane #status predicted #label TMM\ !$340-491 #domain intracellular #status predicted #label INT\ !$447-462 #region serine-rich\ !$228 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 491 #checksum 9011 SEQUENCE /// ENTRY IJXLCP #type complete TITLE EP-cadherin precursor - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 22-Jun-1999 ACCESSIONS B43785; A60128 REFERENCE A43785 !$#authors Ginsberg, D.; DeSimone, D.; Geiger, B. !$#journal Development (1991) 111:315-325 !$#title Expression of a novel cadherin (EP-cadherin) in unfertilized !1eggs and early Xenopus embryos. !$#cross-references MUID:91372132; PMID:1893866 !$#accession B43785 !'##molecule_type mRNA !'##residues 1-895 ##label GIN !'##cross-references GB:X63720; NID:g64681; PIDN:CAA45252.1; PID:g64682 !'##note it is uncertain whether Met-1 or Met-16 is the initiator REFERENCE A60128 !$#authors Angres, B.; Mueller, A.H.J.; Kellermann, J.; Hausen, P. !$#journal Development (1991) 111:829-844 !$#title Differential expression of two cadherins in Xenopus laevis. !$#cross-references MUID:91347911; PMID:1879345 !$#accession A60128 !'##molecule_type protein !'##residues 171-177,'I',179-183,'K',185-189,'XI' ##label ANG !'##note the material sequenced may have contained U-cadherin as well as !1E-cadherin COMMENT Cadherins mediate calcium-dependent intercellular adhesion, !1and are thought to be involved in the sorting of different !1cell types during morphogenesis. CLASSIFICATION #superfamily cadherin; cadherin repeat homology KEYWORDS calcium binding; cell adhesion; duplication; embryo; !1glycoprotein; transmembrane protein FEATURE !$1-43 #domain signal sequence #status predicted #label SIG\ !$44-170 #domain propeptide #status predicted #label PRO\ !$171-895 #product EP-cadherin #status predicted #label MAT\ !$171-718 #domain extracellular #status predicted #label EXT\ !$173-278 #domain cadherin repeat homology #label CR1\ !$248-253 #region cadherin binding #status predicted\ !$281-391 #domain cadherin repeat homology #label CR2\ !$394-502 #domain cadherin repeat homology #label CR3\ !$503-610 #domain cadherin repeat homology #label CR4\ !$611-714 #domain cadherin repeat homology #label CR5\ !$719-743 #domain transmembrane #status predicted #label TMM\ !$744-895 #domain intracellular #status predicted #label INT\ !$852-865 #region serine-rich\ !$440,696 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 895 #molecular-weight 99368 #checksum 116 SEQUENCE /// ENTRY IJCHCB #type fragment TITLE B-cadherin precursor - chicken (fragment) ALTERNATE_NAMES K-CAM protein ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 22-Jun-1999 ACCESSIONS A41634; A38715; S16160 REFERENCE A41634 !$#authors Sorkin, B.C.; Gallin, W.J.; Edelman, G.M.; Cunningham, B.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:11545-11549 !$#title Genes for two calcium-dependent cell adhesion molecules have !1similar structures and are arranged in tandem in the chicken !1genome. !$#cross-references MUID:92107987; PMID:1763068 !$#accession A41634 !'##molecule_type DNA !'##residues 1-732 ##label SOR !'##cross-references GB:M81894; NID:g212226; PIDN:AAA48929.1; !1PID:g212227 REFERENCE A38715 !$#authors Napolitano, E.W.; Venstrom, K.; Wheeler, E.F.; Reichardt, !1L.F. !$#journal J. Cell Biol. (1991) 113:893-905 !$#title Molecular cloning and characterization of B-cadherin, a !1novel chick cadherin. !$#cross-references MUID:91225083; PMID:2026653 !$#accession A38715 !'##molecule_type mRNA !'##residues 7-413,'V',415-732 ##label NAP !'##cross-references GB:X58518; NID:g63113; PIDN:CAA41408.1; PID:g63114 COMMENT Cadherins mediate calcium-dependent intercellular adhesion, !1and are thought to be involved in the sorting of different !1cell types during morphogenesis. GENETICS !$#gene K-CAM !$#introns 29/3; 81/3; 130/1; 188/3; 231/3; 293/3; 375/2; 423/1; 498/1; !1571/1; 614/3; 662/3 CLASSIFICATION #superfamily cadherin; cadherin repeat homology KEYWORDS calcium binding; cell adhesion; duplication; glycoprotein; !1transmembrane protein FEATURE !$1-6 #domain propeptide (fragment) #status predicted !8#label PRO\ !$6-554 #domain extracellular #status predicted #label EXT\ !$7-732 #product B-cadherin #status predicted #label MAT\ !$9-114 #domain cadherin repeat homology #label CR1\ !$84-89 #region cadherin binding #status predicted\ !$117-227 #domain cadherin repeat homology #label CR2\ !$230-339 #domain cadherin repeat homology #label CR3\ !$340-447 #domain cadherin repeat homology #label CR4\ !$448-552 #domain cadherin repeat homology #label CR5\ !$555-580 #domain transmembrane #status predicted #label TMM\ !$581-732 #domain intracellular #status predicted #label INT\ !$689-702 #region serine-rich\ !$137,410 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 732 #checksum 4720 SEQUENCE /// ENTRY IJMSCM #type fragment TITLE M-cadherin - mouse (fragment) ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 19-Jan-1996 ACCESSIONS A40986 REFERENCE A40986 !$#authors Donalies, M.; Cramer, M.; Ringwald, M.; Starzinski-Powitz, !1A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:8024-8028 !$#title Expression of M-cadherin, a member of the cadherin multigene !1family, correlates with differentiation of skeletal muscle !1cells. !$#cross-references MUID:91376079; PMID:1840697 !$#accession A40986 !'##molecule_type mRNA !'##residues 1-730 ##label DON !'##cross-references GB:M74541 COMMENT Cadherins mediate calcium-dependent intercellular adhesion, !1and are thought to be involved in the sorting of different !1cell types during morphogenesis. CLASSIFICATION #superfamily cadherin; cadherin repeat homology KEYWORDS calcium binding; cell adhesion; duplication; glycoprotein; !1skeletal muscle; transmembrane protein FEATURE !$1-730 #product M-cadherin (fragment) #status predicted !8#label MAT\ !$1-535 #domain extracellular (fragment) #status predicted !8#label EXT\ !$1-97 #domain cadherin repeat homology (fragment) #label !8CR1\ !$67-72 #region cadherin binding #status predicted\ !$100-205 #domain cadherin repeat homology #label CR2\ !$206-320 #domain cadherin repeat homology #label CR3\ !$321-428 #domain cadherin repeat homology #label CR4\ !$430-538 #domain cadherin repeat homology #label CR5\ !$552-568 #domain transmembrane #status predicted #label TMM\ !$574-730 #domain intracellular #status predicted #label INT\ !$691-702 #region serine-rich\ !$52,172,476,483,521 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 730 #checksum 4160 SEQUENCE /// ENTRY IJMSCT #type complete TITLE T-cadherin precursor - chicken ALTERNATE_NAMES truncated cadherin ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 20-Apr-2000 ACCESSIONS JU0279; S33272 REFERENCE JU0279 !$#authors Ranscht, B.; Dours-Zimmermann, M.T. !$#journal Neuron (1991) 7:391-402 !$#title T-cadherin, a novel cadherin cell adhesion molecule in the !1nervous system lacks the conserved cytoplasmic region. !$#cross-references MUID:92000685; PMID:1654948 !$#accession JU0279 !'##molecule_type mRNA !'##residues 1-712 ##label RAN !'##cross-references GB:M81779; NID:g212708; PIDN:AAA49079.1; !1PID:g212709 !'##experimental_source embryonic brain !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE S33272 !$#authors Cunningham, H.B.; Yazaki, P.J.; Domingo, R.C.; Oades, K.V.; !1Bohlen, H.; Sabbadini, R.A.; Dahms, A.S. !$#journal Arch. Biochem. Biophys. (1993) 303:32-43 !$#title The skeletal muscle transverse tubular Mg-ATPase: identity !1with Mg-ATPases of smooth muscle and brain. !$#cross-references MUID:93256569; PMID:8489264 !$#accession S33272 !'##molecule_type protein !'##residues 139-153 ##label CUN COMMENT Cadherins mediate calcium-dependent intercellular adhesion, !1and are thought to be involved in the sorting of different !1cell types during morphogenesis. COMMENT This protein is attached to the neuronal plasma membrane !1through a glycosyl phosphotidylinositol anchor; however, the !1attachment site is uncertain. CLASSIFICATION #superfamily cadherin; cadherin repeat homology KEYWORDS blocked carboxyl end; calcium binding; cell adhesion; !1duplication; glycoprotein; lipoprotein; membrane bound; !1phosphatidylinositol linkage; phosphoprotein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-138 #domain amino-terminal propeptide #status predicted !8#label PRO\ !$139-693 #product T-cadherin #status predicted #label MAT\ !$141-245 #domain cadherin repeat homology #label CR1\ !$248-363 #domain cadherin repeat homology #label CR2\ !$366-477 #domain cadherin repeat homology #label CR3\ !$480-585 #domain cadherin repeat homology #label CR4\ !$586-691 #domain cadherin repeat homology #label CR5\ !$694-712 #domain carboxyl-terminal propeptide #status !8predicted #label CPR\ !$382,500,530,638,671 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$693 #modified_site GPI-anchor ethanolamine amidated !8carboxyl end (Asp) (in mature form) #status predicted SUMMARY #length 712 #molecular-weight 78380 #checksum 8552 SEQUENCE /// ENTRY IJHUC5 #type complete TITLE cadherin 5 precursor - human ALTERNATE_NAMES 7B4 antigen; cadherin, endothelial-specific; VE-cadherin ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1993 #sequence_revision 13-Sep-1996 #text_change 22-Jun-1999 ACCESSIONS S49893; S24305; A43418 REFERENCE S49893 !$#authors Breviario, F.; Caveda, L.; Corada, M.; Martin-Padura, I.; !1Golay, J.; Introna, M.; Lampugnani, M.G.; Dejana, E. !$#submission submitted to the EMBL Data Library, June 1994 !$#description Molecular and functional properties of VE-cadherin (7B4/ !1cadherin-5) a novel endothelial specific cadherin. !$#accession S49893 !'##status preliminary !'##molecule_type mRNA !'##residues 1-784 ##label BRE !'##cross-references EMBL:X79981; NID:g599833; PIDN:CAA56306.1; !1PID:g599834 REFERENCE S24305 !$#authors Suzuki, S.; Sano, K.; Tanihara, H. !$#journal Cell Regul. (1991) 2:261-270 !$#title Diversity of the cadherin family: evidence for eight new !1cadherins in nervous tissue. !$#cross-references MUID:91283540; PMID:2059658 !$#accession S24305 !'##molecule_type mRNA !'##residues 5-516,'I',518-784 ##label SUZ !'##cross-references EMBL:X59796; NID:g639976; PIDN:CAA42468.1; !1PID:g29593 REFERENCE A43418 !$#authors Lampugnani, M.G.; Resnati, M.; Raiteri, M.; Pigott, R.; !1Pisacane, A.; Houen, G.; Ruco, L.P.; Dejana, E. !$#journal J. Cell Biol. (1992) 118:1511-1522 !$#title A novel endothelial-specific membrane protein is a marker of !1cell-cell contacts. !$#cross-references MUID:92394977; PMID:1522121 !$#accession A43418 !'##molecule_type protein !'##residues 48-60,'X',62,'X',64;108-116,'X',118-123;237-238,'X',240, !1'X',242-252,'X',254-256;263-275,'X',277-283,'X', !1285;348-355;'X',425-429 ##label LAM !'##experimental_source cultured endothelial cells !'##note sequence extracted from NCBI backbone (NCBIP:113040, !1NCBIP:113045, NCBIP:113047, NCBIP:113049, NCBIP:113051, !1NCBIP:113054) COMMENT Cadherins mediate calcium-dependent intercellular adhesion, !1and are thought to be involved in the sorting of different !1cell types during morphogenesis. GENETICS !$#gene GDB:CDH5 !'##cross-references GDB:134230; OMIM:601120 !$#map_position 16q22.1-16q22.1 CLASSIFICATION #superfamily cadherin; cadherin repeat homology KEYWORDS calcium binding; cell adhesion; duplication; glycoprotein; !1transmembrane protein FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-47 #domain propeptide #status predicted #label PRO\ !$48-784 #product cadherin 5 #status predicted #label MAT\ !$48-593 #domain extracellular #status predicted #label EXT\ !$50-151 #domain cadherin repeat homology #label CR1\ !$154-258 #domain cadherin repeat homology #label CR2\ !$261-372 #domain cadherin repeat homology #label CR3\ !$375-479 #domain cadherin repeat homology #label CR4\ !$481-587 #domain cadherin repeat homology #label CR5\ !$594-620 #domain transmembrane #status predicted #label TMM\ !$621-784 #domain intracellular #status predicted #label INT\ !$736-753 #region serine-rich\ !$61,112,157,362,442, !$523,535 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 784 #molecular-weight 87516 #checksum 7459 SEQUENCE /// ENTRY IJHUDA #type complete TITLE desmocollin 3a precursor - human ALTERNATE_NAMES desmosomal glycoprotein II ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 07-May-1999 ACCESSIONS B40390; S16465 REFERENCE A40390 !$#authors Parker, A.E.; Wheeler, G.N.; Arnemann, J.; Pidsley, S.C.; !1Ataliotis, P.; Thomas, C.L.; Rees, D.A.; Magee, A.I.; !1Buxton, R.S. !$#journal J. Biol. Chem. (1991) 266:10438-10445 !$#title Desmosomal glycoproteins II and III. Cadherin-like !1junctional molecules generated by alternative splicing. !$#cross-references MUID:91244819; PMID:2037591 !$#accession B40390 !'##molecule_type mRNA !'##residues 1-901 ##label PAR !'##cross-references GB:X56807 !'##note it is uncertain whether Met-1 is the initiator or whether !1translation is initiated upstream to the sequenced region REFERENCE A43032 !$#authors Buxton, R.S.; Cowin, P.; Franke, W.W.; Garrod, D.R.; Green, !1K.J.; King, I.A.; Koch, P.J.; Magee, A.I.; Rees, D.A.; !1Stanley, J.R.; Steinberg, M.S. !$#journal J. Cell Biol. (1993) 121:481-483 !$#title Nomenclature of the desmosomal cadherins. !$#cross-references MUID:93252984; PMID:8486729 !$#contents annotation; nomenclature GENETICS !$#gene GDB:DSC3; DSC2; DSC1; DS !'##cross-references GDB:126552; OMIM:600271 !$#map_position 18q12.1-18q12.1 CLASSIFICATION #superfamily cadherin; cadherin repeat homology KEYWORDS alternative splicing; calcium binding; cell adhesion; !1duplication; glycoprotein; phosphoprotein; transmembrane !1protein FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-135 #domain propeptide #status predicted #label PRO\ !$136-901 #product desmocollin 3a #status predicted #label MAT\ !$136-695 #domain extracellular #status predicted #label EXT\ !$138-243 #domain cadherin repeat homology #label CR1\ !$246-355 #domain cadherin repeat homology #label CR2\ !$358-471 #domain cadherin repeat homology #label CR3\ !$474-577 #domain cadherin repeat homology #label CR4\ !$578-680 #domain cadherin repeat homology #label CR5\ !$696-718 #domain transmembrane #status predicted #label TMM\ !$719-901 #domain intracellular #status predicted #label INT\ !$166,392,546,629 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$864 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 901 #molecular-weight 99961 #checksum 5906 SEQUENCE /// ENTRY IJHUDB #type complete TITLE desmocollin 3b precursor - human ALTERNATE_NAMES desmosomal glycoprotein III ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 07-May-1999 ACCESSIONS A40390; S16464 REFERENCE A40390 !$#authors Parker, A.E.; Wheeler, G.N.; Arnemann, J.; Pidsley, S.C.; !1Ataliotis, P.; Thomas, C.L.; Rees, D.A.; Magee, A.I.; !1Buxton, R.S. !$#journal J. Biol. Chem. (1991) 266:10438-10445 !$#title Desmosomal glycoproteins II and III. Cadherin-like !1junctional molecules generated by alternative splicing. !$#cross-references MUID:91244819; PMID:2037591 !$#accession A40390 !'##molecule_type mRNA !'##residues 1-847 ##label PAR !'##cross-references GB:X56807 !'##note it is uncertain whether Met-1 is the initiator or whether !1translation is initiated upstream to the sequenced region REFERENCE A43032 !$#authors Buxton, R.S.; Cowin, P.; Franke, W.W.; Garrod, D.R.; Green, !1K.J.; King, I.A.; Koch, P.J.; Magee, A.I.; Rees, D.A.; !1Stanley, J.R.; Steinberg, M.S. !$#journal J. Cell Biol. (1993) 121:481-483 !$#title Nomenclature of the desmosomal cadherins. !$#cross-references MUID:93252984; PMID:8486729 !$#contents annotation; nomenclature GENETICS !$#gene GDB:DSC3; DSC2; DSC1; DS !'##cross-references GDB:126552; OMIM:600271 !$#map_position 18q12.1-18q12.1 CLASSIFICATION #superfamily cadherin; cadherin repeat homology KEYWORDS alternative splicing; calcium binding; cell adhesion; !1duplication; glycoprotein; phosphoprotein; transmembrane !1protein FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-135 #domain propeptide #status predicted #label PRO\ !$136-847 #product desmocollin 3b #status predicted #label MAT\ !$136-695 #domain extracellular #status predicted #label EXT\ !$138-243 #domain cadherin repeat homology #label CR1\ !$246-355 #domain cadherin repeat homology #label CR2\ !$358-471 #domain cadherin repeat homology #label CR3\ !$474-577 #domain cadherin repeat homology #label CR4\ !$578-680 #domain cadherin repeat homology #label CR5\ !$696-718 #domain transmembrane #status predicted #label TMM\ !$719-847 #domain intracellular #status predicted #label INT\ !$166,392,546,629 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 847 #molecular-weight 93768 #checksum 3131 SEQUENCE /// ENTRY IJBODC #type fragment TITLE desmocollin 2a precursor - bovine (fragment) ALTERNATE_NAMES epithelial type 2 desmocollin subform I ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 22-Jun-1999 ACCESSIONS A41799 REFERENCE A41799 !$#authors Koch, P.J.; Goldschmidt, M.D.; Zimbelmann, R.; Troyanovsky, !1R.; Franke, W.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:353-357 !$#title Complexity and expression patterns of the desmosomal !1cadherins. !$#cross-references MUID:92108053; PMID:1729705 !$#accession A41799 !'##molecule_type mRNA !'##residues 1-863 ##label KOC !'##cross-references GB:M81190; NID:g163757; PIDN:AAA30782.1; !1PID:g163758 !'##experimental_source muzzle !'##note sequence extracted from NCBI backbone !'##note 264-Gln and 333-Gln were also found GENETICS !$#gene DSC2 CLASSIFICATION #superfamily cadherin; cadherin repeat homology KEYWORDS alternative splicing; calcium binding; cell adhesion; !1duplication; glycoprotein; phosphoprotein; transmembrane !1protein FEATURE !$1-89 #domain propeptide #status predicted #label PRO\ !$90-863 #product desmocollin 2a #status predicted #label MAT\ !$90-645 #domain extracellular #status predicted #label EXT\ !$92-197 #domain cadherin repeat homology #label CR1\ !$200-309 #domain cadherin repeat homology #label CR2\ !$312-423 #domain cadherin repeat homology #label CR3\ !$426-526 #domain cadherin repeat homology #label CR4\ !$527-634 #domain cadherin repeat homology #label CR5\ !$646-672 #domain transmembrane #status predicted #label TMM\ !$673-863 #domain intracellular #status predicted #label INT\ !$120,346,495,579 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$826 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 863 #checksum 1299 SEQUENCE /// ENTRY IJBODD #type fragment TITLE desmocollin 2b precursor - bovine (fragment) ALTERNATE_NAMES epithelial type 2 desmocollin subform II ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 22-Jun-1999 ACCESSIONS B41799 REFERENCE A41799 !$#authors Koch, P.J.; Goldschmidt, M.D.; Zimbelmann, R.; Troyanovsky, !1R.; Franke, W.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:353-357 !$#title Complexity and expression patterns of the desmosomal !1cadherins. !$#cross-references MUID:92108053; PMID:1729705 !$#accession B41799 !'##molecule_type mRNA !'##residues 1-809 ##label KOC !'##cross-references GB:M81190; NID:g163757; PIDN:AAA30783.1; !1PID:g163759 !'##experimental_source muzzle !'##note sequence extracted from NCBI backbone !'##note 264-Gln and 333-Gln were also found GENETICS !$#gene DSC2 CLASSIFICATION #superfamily cadherin; cadherin repeat homology KEYWORDS alternative splicing; calcium binding; cell adhesion; !1duplication; glycoprotein; transmembrane protein FEATURE !$1-89 #domain propeptide #status predicted #label PRO\ !$90-809 #product desmocollin 2b #status predicted #label MAT\ !$90-645 #domain extracellular #status predicted #label EXT\ !$92-197 #domain cadherin repeat homology #label CR1\ !$200-309 #domain cadherin repeat homology #label CR2\ !$312-423 #domain cadherin repeat homology #label CR3\ !$426-526 #domain cadherin repeat homology #label CR4\ !$527-634 #domain cadherin repeat homology #label CR5\ !$646-672 #domain transmembrane #status predicted #label TMM\ !$673-809 #domain intracellular #status predicted #label INT\ !$120,346,495,579 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 809 #checksum 9747 SEQUENCE /// ENTRY IJBODE #type complete TITLE desmocollin 1a - bovine ALTERNATE_NAMES desmocollin BDCM; desmosomal glycoprotein 2 ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 22-Jun-1999 ACCESSIONS A43838; B43838; A38456; A60714; S14542 REFERENCE A43838 !$#authors Koch, P.J.; Goldschmidt, M.D.; Walsh, M.J.; Zimbelmann, R.; !1Schmelz, M.; Franke, W.W. !$#journal Differentiation (1991) 47:29-36 !$#title Amino acid sequence of bovine muzzle epithelial desmocollin !1derived from cloned cDNA: a novel subtype of desmosomal !1cadherins. !$#cross-references MUID:92008912; PMID:1916068 !$#accession A43838 !'##molecule_type mRNA !'##residues 1-761 ##label KOC !'##cross-references GB:X58029; GB:S57985; NID:g453583; PIDN:CAA41088.1; !1PID:g453584 !$#accession B43838 !'##molecule_type protein !'##residues !11-32;65-76;148-159;164-176;190-205;208-219;238-256;361-375; !1377-388;478-486 ##label KO2 !'##experimental_source muzzle epithelium !'##note sequence extracted from NCBI backbone REFERENCE A38456 !$#authors Collins, J.E.; Legan, P.K.; Kenny, T.P.; MacGarvie, J.; !1Holton, J.L.; Garrod, D.R. !$#journal J. Cell Biol. (1991) 113:381-391 !$#title Cloning and sequence analysis of desmosomal glycoproteins 2 !1and 3 (desmocollins): cadherin-like desmosomal adhesion !1molecules with heterogeneous cytoplasmic domains. !$#cross-references MUID:91185414; PMID:2010468 !$#accession A38456 !'##molecule_type mRNA !'##residues 606-761 ##label COL !'##cross-references EMBL:X56967; NID:g310; PIDN:CAA40287.1; PID:g311 REFERENCE A60714 !$#authors Holton, J.L.; Kenny, T.P.; Legan, P.K.; Collins, J.E.; Keen, !1J.N.; Sharma, R.; Garrod, D.R. !$#journal J. Cell Sci. (1990) 97:239-246 !$#title Desmosomal glycoproteins 2 and 3 (desmocollins) show !1N-terminal similarity to calcium-dependent cell-cell !1adhesion molecules. !$#cross-references MUID:91115997; PMID:2277091 !$#accession A60714 !'##molecule_type protein !'##residues 1-6,'A',8-9,'R',11-17,'RCE',21-23 ##label HOL !'##experimental_source nasal epidermis GENETICS !$#gene DSC1 CLASSIFICATION #superfamily cadherin; cadherin repeat homology KEYWORDS alternative splicing; calcium binding; cell adhesion; !1duplication; glycoprotein; phosphoprotein; transmembrane !1protein FEATURE !$1-761 #product desmocollin 1a #status experimental #label !8MAT\ !$1-561 #domain extracellular #status predicted #label EXT\ !$3-108 #domain cadherin repeat homology #label CR1\ !$111-220 #domain cadherin repeat homology #label CR2\ !$223-338 #domain cadherin repeat homology #label CR3\ !$339-444 #domain cadherin repeat homology #label CR4\ !$445-561 #domain cadherin repeat homology #label CR5\ !$562-582 #domain transmembrane #status predicted #label TMM\ !$583-761 #domain intracellular #status predicted #label INT\ !$31,266,413 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$584,588,678 #binding_site phosphate (Thr) (covalent) (by protein !8kinase C) #status predicted\ !$605 #binding_site phosphate (Ser) (covalent) (by casein !8kinase II) #status predicted\ !$671 #binding_site phosphate (Ser) (covalent) (by protein !8kinase C) #status predicted\ !$681 #binding_site phosphate (Tyr) (covalent) #status !8predicted\ !$682 #binding_site phosphate (Thr) (covalent) (by casein !8kinase II) #status predicted SUMMARY #length 761 #molecular-weight 85170 #checksum 3508 SEQUENCE /// ENTRY IJBODF #type complete TITLE desmocollin 1b precursor - bovine ALTERNATE_NAMES desmosomal glycoprotein 3 ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 22-Jun-1999 ACCESSIONS B38456; A39377; S14567 REFERENCE A38456 !$#authors Collins, J.E.; Legan, P.K.; Kenny, T.P.; MacGarvie, J.; !1Holton, J.L.; Garrod, D.R. !$#journal J. Cell Biol. (1991) 113:381-391 !$#title Cloning and sequence analysis of desmosomal glycoproteins 2 !1and 3 (desmocollins): cadherin-like desmosomal adhesion !1molecules with heterogeneous cytoplasmic domains. !$#cross-references MUID:91185414; PMID:2010468 !$#accession B38456 !'##molecule_type mRNA !'##residues 1-839 ##label COL !'##cross-references GB:X56966; NID:g315; PIDN:CAA40286.1; PID:g316 REFERENCE A39377 !$#authors Mechanic, S.; Raynor, K.; Hill, J.E.; Cowin, P. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:4476-4480 !$#title Desmocollins form a distinct subset of the cadherin family !1of cell adhesion molecules. !$#cross-references MUID:91239591; PMID:2034686 !$#accession A39377 !'##molecule_type mRNA !'##residues 1-484,'A',486-839 ##label MEC !'##cross-references GB:M67489; GB:M61750; NID:g162970; PIDN:AAA30492.1; !1PID:g162971 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing GENETICS !$#gene DSC1 CLASSIFICATION #superfamily cadherin; cadherin repeat homology KEYWORDS alternative splicing; calcium binding; cell adhesion; !1duplication; glycoprotein; phosphoprotein; transmembrane !1protein FEATURE !$1-29 #domain signal sequence #status predicted #label SIG\ !$30-132 #domain propeptide #status predicted #label PRO\ !$133-839 #product desmocollin 1b #status experimental #label !8MAT\ !$133-682 #domain extracellular #status predicted #label EXT\ !$135-240 #domain cadherin repeat homology #label CR1\ !$243-352 #domain cadherin repeat homology #label CR2\ !$355-470 #domain cadherin repeat homology #label CR3\ !$471-576 #domain cadherin repeat homology #label CR4\ !$577-682 #domain cadherin repeat homology #label CR5\ !$694-714 #domain transmembrane #status predicted #label TMM\ !$718-839 #domain intracellular #status predicted #label INT\ !$163,398,545 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$716,720,810 #binding_site phosphate (Thr) (covalent) (by protein !8kinase C) #status predicted\ !$737 #binding_site phosphate (Ser) (covalent) (by casein !8kinase II) #status predicted\ !$803,830 #binding_site phosphate (Ser) (covalent) (by protein !8kinase C) #status predicted\ !$813 #binding_site phosphate (Tyr) (covalent) #status !8predicted\ !$814 #binding_site phosphate (Thr) (covalent) (by casein !8kinase II) #status predicted SUMMARY #length 839 #molecular-weight 93521 #checksum 6365 SEQUENCE /// ENTRY IJHUG1 #type complete TITLE desmoglein 1 precursor - human ALTERNATE_NAMES desmosomal glycoprotein I ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 22-Jun-1999 ACCESSIONS S16906; A39706; A61254; A61279; S16158 REFERENCE S16906 !$#authors Buxton, R.S. !$#submission submitted to the EMBL Data Library, November 1990 !$#accession S16906 !'##molecule_type mRNA !'##residues 1-1049 ##label BUX !'##cross-references EMBL:X56654; NID:g30505; PIDN:CAA39976.1; !1PID:g30506 REFERENCE A39706 !$#authors Wheeler, G.N.; Parker, A.E.; Thomas, C.L.; Ataliotis, P.; !1Poynter, D.; Arnemann, J.; Rutman, A.J.; Pidsley, S.C.; !1Watt, F.M.; Rees, D.A.; Buxton, R.S.; Magee, A.I. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:4796-4800 !$#title Desmosomal glycoprotein DGI, a component of intercellular !1desmosome junctions, is related to the cadherin family of !1cell adhesion molecules. !$#cross-references MUID:91271279; PMID:1711210 !$#accession A39706 !'##molecule_type mRNA !'##residues 24-1049 ##label WHE !'##cross-references GB:X56654 REFERENCE A61254 !$#authors Nilles, L.A.; Parry, D.A.D.; Powers, E.E.; Angst, B.D.; !1Wagner, R.M.; Green, K.J. !$#journal J. Cell Sci. (1991) 99:809-821 !$#title Structural analysis and expression of human desmoglein: a !1cadherin-like component of the desmosome. !$#cross-references MUID:92121251; PMID:1770008 !$#accession A61254 !'##molecule_type mRNA !'##residues 26-1049 ##label NIL REFERENCE A61279 !$#authors Wheeler, G.N.; Buxton, R.S.; Parker, A.E.; Arnemann, J.; !1Rees, D.A.; King, I.A.; Magee, A.I. !$#journal Biochem. Soc. Trans. (1991) 19:1060-1064 !$#title Desmosomal glycoproteins I, II and III: novel members of the !1cadherin superfamily. !$#cross-references MUID:92175187; PMID:1794462 !$#accession A61279 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-55 ##label WH3 GENETICS !$#gene GDB:DSG1 !'##cross-references GDB:126563; OMIM:125670 !$#map_position 18q12.1-18q12.2 CLASSIFICATION #superfamily cadherin; cadherin repeat homology KEYWORDS calcium binding; cell adhesion; duplication; glycoprotein; !1transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-49 #domain propeptide #status predicted #label PRO\ !$50-1049 #product desmoglein #status predicted #label MAT\ !$50-548 #domain extracellular #status predicted #label EXT\ !$52-157 #domain cadherin repeat homology #label CR1\ !$160-269 #domain cadherin repeat homology #label CR2\ !$272-385 #domain cadherin repeat homology #label CR3\ !$392-493 #domain cadherin repeat homology #label CR4\ !$509-530 #region serine/threonine-rich\ !$549-569 #domain transmembrane #status predicted #label TMM\ !$572-1049 #domain intracellular #status predicted #label INT\ !$840-869 #domain desmoglein repeat #label DG1\ !$870-899 #domain desmoglein repeat #label DG2\ !$900-927 #domain desmoglein repeat #label DG3\ !$928-956 #domain desmoglein repeat #label DG4\ !$969-1019 #region glycine/serine-rich\ !$110,180 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1049 #molecular-weight 113715 #checksum 4482 SEQUENCE /// ENTRY IJBOG1 #type complete TITLE desmoglein 1 precursor - bovine ALTERNATE_NAMES desmoglein BDGM ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 22-Jun-1999 ACCESSIONS S14603; A38872; A37785; S38721; A48173; S24412 REFERENCE S14603 !$#authors Koch, P.J.; Goldschmidt, M.D.; Zimbelmann, R.; Franke, W.W. !$#submission submitted to the EMBL Data Library, March 1991 !$#description Complete sequence of the desmoglein precursor and evidence !1for the existence of different desmoglein genes expressed in !1cell type-specific patterns. !$#accession S14603 !'##molecule_type mRNA !'##residues 1-1043 ##label KOC !'##cross-references EMBL:X58466; NID:g306; PIDN:CAA41380.1; PID:g307 REFERENCE A38872 !$#authors Koch, P.J.; Goldschmidt, M.D.; Walsh, M.J.; Zimbelmann, R.; !1Franke, W.W. !$#journal Eur. J. Cell Biol. (1991) 55:200-208 !$#title Complete amino acid sequence of the epidermal desmoglein !1precursor polypeptide and identification of a second type of !1desmoglein gene. !$#cross-references MUID:92037656; PMID:1935985 !$#accession A38872 !'##molecule_type mRNA !'##residues 1-87;968-1043 ##label KO2 !'##cross-references GB:S64268; GB:S64270 REFERENCE A37785 !$#authors Goodwin, L.; Hill, J.E.; Raynor, K.; Raszi, L.; Manabe, M.; !1Cowin, P. !$#journal Biochem. Biophys. Res. Commun. (1990) 173:1224-1230 !$#title Desmoglein shows extensive homology to the cadherin family !1of cell adhesion molecules. !$#cross-references MUID:91097553; PMID:1702628 !$#accession A37785 !'##molecule_type mRNA !'##residues 44-123,'V',125-493 ##label GOO !'##cross-references GB:M58165; NID:g162966; PIDN:AAA62709.1; !1PID:g552318 REFERENCE S38721 !$#authors Zimbelmann, R. !$#submission submitted to the EMBL Data Library, February 1991 !$#accession S38721 !'##molecule_type mRNA !'##residues 44-1043 ##label ZIM !'##cross-references EMBL:X57784; NID:g436061; PIDN:CAA40930.1; !1PID:g436062 REFERENCE A48173 !$#authors Koch, P.J.; Walsh, M.J.; Schmelz, M.; Goldschmidt, M.D.; !1Zimbelmann, R.; Franke, W.W. !$#journal Eur. J. Cell Biol. (1990) 53:1-12 !$#title Identification of desmoglein, a constitutive desmosomal !1glycoprotein, as a member of the cadherin family of cell !1adhesion molecules. !$#cross-references MUID:91168965; PMID:1706270 !$#accession A48173 !'##molecule_type mRNA !'##residues 44-1001,'AQPPSAT' ##label KO3 !'##cross-references GB:X57784 !'##note this sequence has been revised in references A38872 and S38721 GENETICS !$#gene DSG1 CLASSIFICATION #superfamily cadherin; cadherin repeat homology KEYWORDS calcium binding; cell adhesion; duplication; glycoprotein; !1transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-49 #domain propeptide #status predicted #label PRO\ !$50-1043 #product desmoglein #status predicted #label MAT\ !$50-548 #domain extracellular #status predicted #label EXT\ !$52-157 #domain cadherin repeat homology #label CR1\ !$160-269 #domain cadherin repeat homology #label CR2\ !$272-385 #domain cadherin repeat homology #label CR3\ !$392-491 #domain cadherin repeat homology #label CR4\ !$549-574 #domain transmembrane #status predicted #label TMM\ !$575-1043 #domain intracellular #status predicted #label INT\ !$846-875 #domain desmoglein repeat #label DG1\ !$876-905 #domain desmoglein repeat #label DG2\ !$906-933 #domain desmoglein repeat #label DG3\ !$934-962 #domain desmoglein repeat #label DG4\ !$963-1012 #region glycine/serine-rich\ !$110 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$180,496 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1043 #molecular-weight 112242 #checksum 6897 SEQUENCE /// ENTRY IJHUG3 #type complete TITLE desmoglein 3 precursor - human ALTERNATE_NAMES pemphigus vulgaris antigen ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 22-Jun-1999 ACCESSIONS A41088 REFERENCE A41088 !$#authors Amagai, M.; Klaus-Kovtun, V.; Stanley, J.R. !$#journal Cell (1991) 67:869-877 !$#title Autoantibodies against a novel epithelial cadherin in !1pemphigus vulgaris, a disease of cell adhesion. !$#cross-references MUID:92069753; PMID:1720352 !$#accession A41088 !'##molecule_type mRNA !'##residues 1-999 ##label AMA !'##cross-references GB:M76482; NID:g190751; PIDN:AAA60230.1; !1PID:g190752 GENETICS !$#gene GDB:DSG3 !'##cross-references GDB:134030; OMIM:169615 !$#map_position 18q12.1-18q12.2 CLASSIFICATION #superfamily cadherin; cadherin repeat homology KEYWORDS calcium binding; cell adhesion; duplication; glycoprotein; !1transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-49 #domain propeptide #status predicted #label PRO\ !$50-999 #product desmoglein homolog #status predicted #label !8MAT\ !$50-615 #domain extracellular #status predicted #label EXT\ !$52-157 #domain cadherin repeat homology #label CR1\ !$160-267 #domain cadherin repeat homology #label CR2\ !$270-383 #domain cadherin repeat homology #label CR3\ !$390-495 #domain cadherin repeat homology #label CR4\ !$496-598 #domain cadherin repeat homology #label CR5\ !$616-639 #domain transmembrane #status predicted #label TMM\ !$640-999 #domain intracellular #status predicted #label INT\ !$910-938 #domain desmoglein repeat #label DG1\ !$937-966 #domain desmoglein repeat #label DG2\ !$110,180,545 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 999 #molecular-weight 107502 #checksum 8311 SEQUENCE /// ENTRY JQ0948 #type complete TITLE A5 antigen precursor - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS JH0466; JQ0948 REFERENCE JH0466 !$#authors Takagi, S.; Hirata, T.; Agata, K.; Mochii, M.; Eguchi, G.; !1Fujisawa, H. !$#journal Neuron (1991) 7:295-307 !$#title The A5 antigen, a candidate for the neuronal recognition !1molecule, has homologies to complement components and !1coagulation factors. !$#cross-references MUID:91337458; PMID:1908252 !$#accession JH0466 !'##molecule_type mRNA !'##residues 1-927 ##label TAK !'##cross-references GB:D10467; GB:D01077; NID:g222962; PIDN:BAA01260.1; !1PID:g222963 !'##experimental_source tadpole, brain !'##note this protein has motifs homologous to complement components C1r !1and C1s and to coagulation factors VIII and V COMMENT This protein is a neuronal cell surface molecule involved in !1the neuronal recognition between the optic nerve fibers and !1the visual centers. CLASSIFICATION #superfamily Xenopus A5 antigen; C1r/C1s repeat homology; !1discoidin I amino-terminal homology; EGF homology; MAM !1homology KEYWORDS duplication; glycoprotein; transmembrane protein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-927 #product A5 antigen #status predicted #label A5A\ !$27-138 #domain C1r/C1s repeat homology #label C1R1\ !$147-262 #domain C1r/C1s repeat homology #label C1R2\ !$274-424 #domain discoidin I amino-terminal homology #label !8DN1\ !$430-584 #domain discoidin I amino-terminal homology #label !8DN2\ !$646-812 #domain MAM homology #label MAM\ !$861-883 #domain transmembrane #status predicted #label TMM\ !$150,261,300,523,844 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 927 #molecular-weight 103328 #checksum 714 SEQUENCE /// ENTRY A36479 #type complete TITLE milk fat globule membrane protein - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A36479 REFERENCE A36479 !$#authors Stubbs, J.D.; Lekutis, C.; Singer, K.L.; Bui, A.; Yuzuki, !1D.; Srinivasan, U.; Parry, G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:8417-8421 !$#title cDNA cloning of a mouse mammary epithelial cell surface !1protein reveals the existence of epidermal growth !1factor-like domains linked to factor VIII-like sequences. !$#cross-references MUID:91046008; PMID:2122462 !$#accession A36479 !'##status preliminary !'##molecule_type mRNA !'##residues 1-463 ##label STU !'##cross-references GB:M38337; NID:g199142; PIDN:AAA39534.1; !1PID:g199143 CLASSIFICATION #superfamily milk fat globule protein; discoidin I !1amino-terminal homology; EGF homology KEYWORDS membrane protein FEATURE !$28-60 #domain EGF homology #label EG1\ !$68-107 #domain EGF homology #label EG2\ !$147-303 #domain discoidin I amino-terminal homology #label !8DN1\ !$307-463 #domain discoidin I amino-terminal homology #label !8DN2 SUMMARY #length 463 #molecular-weight 51465 #checksum 8337 SEQUENCE /// ENTRY IJHUNG #type complete TITLE neural cell adhesion molecule 1 GPI-anchored splice form precursor, muscle-specific - human ALTERNATE_NAMES CD56; NCAM-120 ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 28-Jan-2000 ACCESSIONS S07784; A26883 REFERENCE S07784 !$#authors Barton, C.H.; Dickson, G.; Gower, H.J.; Rowett, L.H.; Putt, !1W.; Elsom, V.; Moore, S.E.; Goridis, C.; Walsh, F.S. !$#journal Development (1988) 104:165-173 !$#title Complete sequence and in vitro expression of a !1tissue-specific phosphatidylinositol-linked N-CAM isoform !1from skeletal muscle. !$#cross-references MUID:89305258; PMID:3253057 !$#accession S07784 !'##molecule_type mRNA !'##residues 1-761 ##label BAR !'##cross-references EMBL:X16841; NID:g35005; PIDN:CAA34739.1; !1PID:g35006 REFERENCE A90895 !$#authors Dickson, G.; Gower, H.J.; Barton, C.H.; Prentice, H.M.; !1Elsom, V.L.; Moore, S.E.; Cox, R.D.; Quinn, C.; Putt, W.; !1Walsh, F.S. !$#journal Cell (1987) 50:1119-1130 !$#title Human muscle neural cell adhesion molecule (N-CAM): !1identification of a muscle-specific sequence in the !1extracellular domain. !$#cross-references MUID:87301755; PMID:2887295 !$#accession A26883 !'##molecule_type mRNA !'##residues 491-761 ##label DIC !'##cross-references GB:M17409; NID:g189097; PIDN:AAA59912.1; !1PID:g386979 COMMENT NCAM mediates cell-cell adhesion via homophilic binding with !1another NCAM molecule. COMMENT Various forms of NCAM are produced by alternative splicing. GENETICS !$#gene GDB:NCAM1; NCAM; CD56 !'##cross-references GDB:119448; OMIM:116930 !$#map_position 11q22.2-11q22.3 CLASSIFICATION #superfamily neural cell adhesion molecule; fibronectin type !1III repeat homology; immunoglobulin homology KEYWORDS alternative splicing; cell adhesion; duplication; heparin !1binding; membrane protein; phosphatidylinositol linkage; !1sialoglycoprotein; skeletal muscle FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-761 #product neural cell adhesion molecule !8phosphatidylinositol-linked form, muscle-specific !8#status predicted #label MAT\ !$34-98 #domain immunoglobulin homology #label IMM1\ !$132-191 #domain immunoglobulin homology #label IMM2\ !$152-156 #region heparin binding #status predicted\ !$161-165 #region heparin binding #status predicted\ !$228-289 #domain immunoglobulin homology #label IMM3\ !$263-272 #region NCAM binding #status predicted\ !$322-387 #domain immunoglobulin homology #label IMM4\ !$419-481 #domain immunoglobulin homology #label IMM5\ !$499-587 #domain fibronectin type III repeat homology #status !8atypical #label FN3A\ !$633-720 #domain fibronectin type III repeat homology #status !8atypical #label FN3B\ !$41-96,139-189, !$235-287,329-385, !$426-479 #disulfide_bonds #status predicted\ !$222,315,347,423, !$449,478 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 761 #molecular-weight 83769 #checksum 6158 SEQUENCE /// ENTRY IJMSNL #type complete TITLE neural cell adhesion molecule 1 precursor, long domain splice form - mouse ALTERNATE_NAMES NCAM-180 CONTAINS neural cell adhesion molecule, short domain splice form (NCAM-140) ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 31-Dec-2000 ACCESSIONS A29673; S00844; S00384; A28281; A44290; S00383 REFERENCE A29673 !$#authors Barthels, D.; Santoni, M.J.; Wille, W.; Ruppert, C.; Chaix, !1J.C.; Hirsch, M.R.; Fontecilla-Camps, J.C.; Goridis, C. !$#journal EMBO J. (1987) 6:907-914 !$#title Isolation and nucleotide sequence of mouse NCAM cDNA that !1codes for a Mr 79,000 polypeptide without a !1membrane-spanning region. !$#cross-references MUID:87246524; PMID:3595563 !$#accession A29673 !'##molecule_type mRNA !'##residues 1-548,'T',550-571,'T',573-574,'D',576-588,'MQPS',593,'S', !1595-599,'P',601,'L',603-656,'H',658-701, !1'TLGGSSTSYTLVSLLFSAVTLLLL' ##label BA2 !'##cross-references EMBL:Y00051; NID:g53342; PIDN:CAA68263.1; !1PID:g53343 REFERENCE S00844 !$#authors Santoni, M.J.; Barthels, D.; Barbas, J.A.; Hirsch, M.R.; !1Steinmetz, M.; Goridis, C.; Wille, W. !$#journal Nucleic Acids Res. (1987) 15:8621-8641 !$#title Analysis of cDNA clones that code for the transmembrane !1forms of the mouse neural cell adhesion molecule (NCAM) and !1are generated by alternative RNA splicing. !$#cross-references MUID:88067687; PMID:3684567 !$#accession S00844 !'##molecule_type mRNA !'##residues 529-809,1077-1115 ##label SAN !'##cross-references EMBL:X06328; NID:g53322; PIDN:CAA29641.1; !1PID:g817984 REFERENCE S00382 !$#authors Barbas, J.A.; Chaix, J.C.; Steinmetz, M.; Goridis, C. !$#journal EMBO J. (1988) 7:625-632 !$#title Differential splicing and alternative polyadenylation !1generates distinct NCAM transcripts and proteins in the !1mouse. !$#cross-references MUID:88283628; PMID:3396534 !$#accession S00384 !'##molecule_type DNA !'##residues 642-1115 ##label BAR !'##cross-references EMBL:X07195 REFERENCE A28281 !$#authors Barthels, D.; Vopper, G.; Wille, W. !$#journal Nucleic Acids Res. (1988) 16:4217-4225 !$#title NCAM-180, the large isoform of the neural cell adhesion !1molecule of the mouse, is encoded by an alternatively !1spliced transcript. !$#cross-references MUID:88247737; PMID:2454455 !$#accession A28281 !'##molecule_type mRNA !'##residues 804-1081 ##label BA3 !'##cross-references EMBL:X07244; NID:g53321; PIDN:CAA30230.1; !1PID:g929720 REFERENCE A44290 !$#authors Rougon, G.; Marshak, D.R. !$#journal J. Biol. Chem. (1986) 261:3396-3401 !$#title Structural and immunological characterization of the !1amino-terminal domain of mammalian neural cell adhesion !1molecules. !$#cross-references MUID:86140120; PMID:3512556 !$#accession A44290 !'##molecule_type protein !'##residues 20-36 ##label ROU COMMENT NCAM mediates cell-cell adhesion via homophilic binding with !1another NCAM molecule. COMMENT Several forms of NCAM are produced by alternative splicing. !1See also PIR:IJMSNG. GENETICS !$#gene NCAM !$#map_position 9 !$#introns 643/3; 701/1; 770/2; 809/2; 1076/2 CLASSIFICATION #superfamily neural cell adhesion molecule; fibronectin type !1III repeat homology; immunoglobulin homology KEYWORDS alternative splicing; brain; cell adhesion; duplication; !1heparin binding; sialoglycoprotein; transmembrane protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-1115 #product neural cell adhesion molecule, long domain !8splice form #status experimental #label LDF\ !$20-809,1077-1115 #product neural cell adhesion molecule, short domain !8splice form #status experimental #label SDF\ !$20-711 #domain extracellular #status predicted #label EXT\ !$34-98 #domain immunoglobulin homology #label IMM1\ !$132-191 #domain immunoglobulin homology #label IMM2\ !$152-156 #region heparin binding #status predicted\ !$161-165 #region heparin binding #status predicted\ !$228-290 #domain immunoglobulin homology #label IMM3\ !$262-272 #region NCAM binding #status predicted\ !$323-388 #domain immunoglobulin homology #label IMM4\ !$420-482 #domain immunoglobulin homology #label IMM5\ !$519-596 #domain fibronectin type III repeat homology #label !8FN3A\ !$625-685 #domain fibronectin type III repeat homology #label !8FN3B\ !$712-729 #domain transmembrane #status predicted #label TMM\ !$730-1115 #domain intracellular #status predicted #label INT\ !$41-96,139-189, !$235-288,330-386, !$427-480 #disulfide_bonds #status predicted\ !$222,316,348,424, !$450,479 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1115 #molecular-weight 119350 #checksum 7901 SEQUENCE /// ENTRY IJMSNG #type complete TITLE neural cell adhesion molecule 1 precursor, GPI-anchored splice form - mouse ALTERNATE_NAMES NCAM-120 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 31-Dec-2000 ACCESSIONS A29673; S00382; A44290 REFERENCE A29673 !$#authors Barthels, D.; Santoni, M.J.; Wille, W.; Ruppert, C.; Chaix, !1J.C.; Hirsch, M.R.; Fontecilla-Camps, J.C.; Goridis, C. !$#journal EMBO J. (1987) 6:907-914 !$#title Isolation and nucleotide sequence of mouse NCAM cDNA that !1codes for a Mr 79,000 polypeptide without a !1membrane-spanning region. !$#cross-references MUID:87246524; PMID:3595563 !$#accession A29673 !'##molecule_type mRNA !'##residues 1-725 ##label BAR !'##cross-references EMBL:Y00051; NID:g53342; PIDN:CAA68263.1; !1PID:g53343 REFERENCE S00382 !$#authors Barbas, J.A.; Chaix, J.C.; Steinmetz, M.; Goridis, C. !$#journal EMBO J. (1988) 7:625-632 !$#title Differential splicing and alternative polyadenylation !1generates distinct NCAM transcripts and proteins in the !1mouse. !$#cross-references MUID:88283628; PMID:3396534 !$#accession S00382 !'##molecule_type DNA !'##residues 642-656,'D',658-725 ##label BA2 !'##cross-references EMBL:X07195 REFERENCE A44290 !$#authors Rougon, G.; Marshak, D.R. !$#journal J. Biol. Chem. (1986) 261:3396-3401 !$#title Structural and immunological characterization of the !1amino-terminal domain of mammalian neural cell adhesion !1molecules. !$#cross-references MUID:86140120; PMID:3512556 !$#accession A44290 !'##molecule_type protein !'##residues 20-36 ##label ROU COMMENT NCAM mediates cell-cell adhesion via homophilic binding with !1another NCAM molecule. COMMENT Several forms of NCAM are produced by alternative splicing. !1See also PIR:IJMSNL. GENETICS !$#gene NCAM !$#map_position 9 !$#introns 701/1 CLASSIFICATION #superfamily neural cell adhesion molecule; fibronectin type !1III repeat homology; immunoglobulin homology KEYWORDS alternative splicing; cell adhesion; duplication; heparin !1binding; membrane protein; phosphatidylinositol linkage; !1sialoglycoprotein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$34-98 #domain immunoglobulin homology #label IMM1\ !$132-191 #domain immunoglobulin homology #label IMM2\ !$152-156 #region heparin binding #status predicted\ !$161-165 #region heparin binding #status predicted\ !$228-290 #domain immunoglobulin homology #label IMM3\ !$263-272 #region NCAM binding #status predicted\ !$323-388 #domain immunoglobulin homology #label IMM4\ !$420-482 #domain immunoglobulin homology #label IMM5\ !$519-596 #domain fibronectin type III repeat homology #label !8FN3A\ !$625-685 #domain fibronectin type III repeat homology #label !8FN3B\ !$41-96,139-189, !$235-288,330-386, !$427-480 #disulfide_bonds #status predicted\ !$222,316,348,424, !$450,479 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 725 #molecular-weight 80295 #checksum 6952 SEQUENCE /// ENTRY IJRTNC #type complete TITLE neural cell adhesion molecule short domain form precursor - rat ALTERNATE_NAMES NCAM-140 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 22-Jun-1999 ACCESSIONS S00846; B37795; I58136 REFERENCE S00846 !$#authors Small, S.J.; Shull, G.E.; Santoni, M.J.; Akeson, R. !$#journal J. Cell Biol. (1987) 105:2335-2345 !$#title Identification of a cDNA clone that contains the complete !1coding sequence for a 140-kD rat NCAM polypeptide. !$#cross-references MUID:88059265; PMID:3680385 !$#accession S00846 !'##molecule_type mRNA !'##residues 1-858 ##label SMA !'##cross-references EMBL:X06564 REFERENCE A37795 !$#authors Small, S.J.; Akeson, R. !$#journal J. Cell Biol. (1990) 111:2089-2096 !$#title Expression of the unique NCAM VASE exon is independently !1regulated in distinct tissues during development. !$#cross-references MUID:91035620; PMID:1699951 !$#accession B37795 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 340-381 ##label SM2 REFERENCE I58136 !$#authors Small, S.J.; Haines, S.L.; Akeson, R.A. !$#journal Neuron (1988) 1:1007-1017 !$#title Polypeptide variation in an N-CAM extracellular !1immunoglobulin-like fold is developmentally regulated !1through alternative splicing. !$#cross-references MUID:90166485; PMID:2483093 !$#accession I58136 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 355-364 ##label RES !'##cross-references GB:M32611; NID:g205643; PIDN:AAA41679.1; !1PID:g205644 COMMENT NCAM mediates cell-cell adhesion via homophilic binding with !1another NCAM molecule. COMMENT Various forms of NCAM are produced by alternative splicing. GENETICS !$#gene NCAM CLASSIFICATION #superfamily neural cell adhesion molecule; fibronectin type !1III repeat homology; immunoglobulin homology KEYWORDS alternative splicing; brain; cell adhesion; duplication; !1heparin binding; sialoglycoprotein; transmembrane protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-858 #product neural cell adhesion molecule, short domain !8form #status predicted #label MAT\ !$20-721 #domain extracellular #status predicted #label EXT\ !$34-98 #domain immunoglobulin homology #label IMM1\ !$132-191 #domain immunoglobulin homology #label IMM2\ !$152-156 #region heparin binding #status predicted\ !$161-165 #region heparin binding #status predicted\ !$228-290 #domain immunoglobulin homology #label IMM3\ !$263-272 #region NCAM binding #status predicted\ !$323-398 #domain immunoglobulin homology #label IMM4\ !$430-492 #domain immunoglobulin homology #label IMM5\ !$529-606 #domain fibronectin type III repeat homology #label !8FN3A\ !$635-695 #domain fibronectin type III repeat homology #label !8FN3B\ !$722-739 #domain transmembrane #status predicted #label TMM\ !$740-858 #domain intracellular #status predicted #label INT\ !$41-96,139-189, !$235-288,330-396, !$437-490 #disulfide_bonds #status predicted\ !$222,316,348,434, !$460,489 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 858 #molecular-weight 94615 #checksum 9480 SEQUENCE /// ENTRY IJBONC #type complete TITLE neural cell adhesion molecule short domain form precursor - bovine ALTERNATE_NAMES NCAM-140 ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 22-Jun-1999 ACCESSIONS A32976; A38778; B44290; S05402 REFERENCE A32976 !$#authors Lipkin, V.M.; Khramtsov, N.V.; Andreeva, S.G.; Moshnyakov, !1M.V.; Petukhova, G.V.; Rakitina, T.V.; Feshchenko, E.A.; !1Ishchenko, K.A.; Mirzoeva, S.F.; Chernova, M.N.; Dranytsyna, !1S.M. !$#journal FEBS Lett. (1989) 254:69-73 !$#title Calmodulin-independent bovine brain adenylate cyclase. Amino !1acid sequence and nucleotide sequence of the corresponding !1cDNA. !$#cross-references MUID:89378239; PMID:2776887 !$#accession A32976 !'##molecule_type mRNA !'##residues 1-853 ##label LIP !'##cross-references GB:X16451; NID:g60; PIDN:CAA34470.1; PID:g61 !$#accession A38778 !'##molecule_type protein !'##residues !120-35;51-61;113-117;122-147;155-161;262-275;279-302;353-360; !1369-382;544-562;592-614;633-646;671-690;819-845 ##label LI2 !'##note the authors identified this protein as calmodulin-independent !1adenylate cyclase REFERENCE A44290 !$#authors Rougon, G.; Marshak, D.R. !$#journal J. Biol. Chem. (1986) 261:3396-3401 !$#title Structural and immunological characterization of the !1amino-terminal domain of mammalian neural cell adhesion !1molecules. !$#cross-references MUID:86140120; PMID:3512556 !$#accession B44290 !'##molecule_type protein !'##residues 20-36 ##label ROU !'##note 23-Glu was also found COMMENT NCAM mediates cell-cell adhesion via homophilic binding with !1another NCAM molecule. COMMENT Various forms of NCAM are produced by alternative splicing. CLASSIFICATION #superfamily neural cell adhesion molecule; fibronectin type !1III repeat homology; immunoglobulin homology KEYWORDS alternative splicing; brain; cell adhesion; duplication; !1heparin binding; sialoglycoprotein; transmembrane protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-853 #product neural cell adhesion molecule, short domain !8form #status experimental #label MAT\ !$20-719 #domain extracellular #status predicted #label EXT\ !$34-98 #domain immunoglobulin homology #label IMM1\ !$132-191 #domain immunoglobulin homology #label IMM2\ !$152-156 #region heparin binding #status predicted\ !$161-165 #region heparin binding #status predicted\ !$228-288 #domain immunoglobulin homology #label IMM3\ !$261-270 #region NCAM binding #status predicted\ !$321-396 #domain immunoglobulin homology #label IMM4\ !$428-490 #domain immunoglobulin homology #label IMM5\ !$527-604 #domain fibronectin type III repeat homology #label !8FN3A\ !$633-693 #domain fibronectin type III repeat homology #label !8FN3B\ !$720-737 #domain transmembrane #status predicted #label TMM\ !$738-853 #domain intracellular #status predicted #label INT\ !$41-96,139-189, !$235-286,328-394, !$435-488 #disulfide_bonds #status predicted\ !$222,314,346,432, !$458,487 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 853 #molecular-weight 93893 #checksum 9582 SEQUENCE /// ENTRY JN0635 #type complete TITLE neural cell adhesion molecule 2 precursor - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 03-Feb-1994 #sequence_revision 03-Feb-1994 #text_change 22-Jun-1999 ACCESSIONS JN0635 REFERENCE JN0635 !$#authors Tonissen, K.F.; Krieg, P.A. !$#journal Gene (1993) 127:243-247 !$#title Two neural-cell adhesion molecule(NCAM)-encoding genes in !1Xenopus laevis are expressed during development and in adult !1tissues. !$#cross-references MUID:93273239; PMID:7684721 !$#accession JN0635 !'##molecule_type mRNA !'##residues 1-1092 ##label TON !'##cross-references GB:M76710; NID:g214611; PIDN:AAA49910.1; !1PID:g214612 COMMENT NCAM mediates cell-cell adhesion via homophilic binding with !1another NCAM molecule. GENETICS !$#gene NCAM2 CLASSIFICATION #superfamily neural cell adhesion molecule; fibronectin type !1III repeat homology; immunoglobulin homology KEYWORDS alternative splicing; cell adhesion; duplication; heparin !1binding; sialoglycoprotein; transmembrane protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-1092 #product neural cell adhesion molecule 2 #status !8predicted #label NCA\ !$20-705 #domain extracellular #status predicted #label EXT\ !$34-95 #domain immunoglobulin homology #label IMM1\ !$129-188 #domain immunoglobulin homology #label IMM2\ !$149-153 #region heparin binding #status predicted\ !$158-162 #region heparin binding #status predicted\ !$317-381 #domain immunoglobulin homology #label IMM3\ !$413-475 #domain immunoglobulin homology #label IMM4\ !$512-589 #domain fibronectin type III repeat homology #label !8FN3A\ !$619-680 #domain fibronectin type III repeat homology #label !8FN3B\ !$706-723 #domain transmembrane #status predicted #label TMM\ !$724-1092 #domain intracellular #status predicted #label INT\ !$41-93,136-186, !$232-282,323-379, !$420-473 #disulfide_bonds #status predicted\ !$219,310,341,417, !$443,472 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1092 #molecular-weight 118081 #checksum 5154 SEQUENCE /// ENTRY IJCHNL #type complete TITLE neural cell adhesion molecule long domain form precursor - chicken ALTERNATE_NAMES NCAM-180 CONTAINS neural cell adhesion molecule, short domain form (NCAM-140) ORGANISM #formal_name Gallus gallus #common_name chicken DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 22-Jun-1999 ACCESSIONS A43613; B43613; A25435; B25435; A46550; S36950; A44369; !1A60852; S29668 REFERENCE A43613 !$#authors Cunningham, B.A.; Hemperly, J.J.; Murray, B.A.; Prediger, !1E.A.; Brackenbury, R.; Edelman, G.M. !$#journal Science (1987) 236:799-806 !$#title Neural cell adhesion molecule: structure, !1immunoglobulin-like domains, cell surface modulation, and !1alternative RNA splicing. !$#cross-references MUID:87206190; PMID:3576199 !$#accession A43613 !'##molecule_type mRNA !'##residues 1-175 ##label CU2 !'##cross-references GB:M15860 !$#accession B43613 !'##molecule_type protein !'##residues 20-44;120-127;202-221;320-342;399-415;640-659;822-828 !1##label CUN !'##note Asn-222 probably binds carbohydrate; Asn-226 probably does not REFERENCE A25435 !$#authors Hemperly, J.J.; Murray, B.A.; Edelman, G.M.; Cunningham, !1B.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:3037-3041 !$#title Sequence of a cDNA clone encoding the polysialic acid-rich !1and cytoplasmic domains of the neural cell adhesion molecule !1N-CAM. !$#cross-references MUID:86206089; PMID:3458261 !$#accession A25435 !'##molecule_type mRNA !'##residues 128-1091 ##label HEM !'##cross-references GB:M13210 !$#accession B25435 !'##molecule_type protein !'##residues 128-140;222-240;428-439;611-631;744-760;763-781;1080-1084 !1##label HE2 REFERENCE A46550 !$#authors Murray, B.A.; Owens, G.C.; Prediger, E.A.; Crossin, K.L.; !1Cunningham, B.A.; Edelman, G.M. !$#journal J. Cell Biol. (1986) 103:1431-1439 !$#title Cell surface modulation of the neural cell adhesion molecule !1resulting from alternative mRNA splicing in a !1tissue-specific developmental sequence. !$#cross-references MUID:87033934; PMID:3771645 !$#accession A46550 !'##molecule_type DNA !'##residues 810-1070 ##label MUR !'##cross-references GB:X04479 REFERENCE S36950 !$#authors Sasner, M.; Covault, J. !$#submission submitted to the EMBL Data Library, February 1993 !$#accession S36950 !'##molecule_type DNA !'##residues 1-17 ##label SAS !'##cross-references EMBL:X70342; NID:g417631; PIDN:CAA49807.1; !1PID:g417632 REFERENCE A44369 !$#authors Colwell, G.; Li, B.; Forrest, D.; Brackenbury, R. !$#journal Genomics (1992) 14:875-882 !$#title Conserved regulatory elements in the promoter region of the !1N-CAM gene. !$#cross-references MUID:93122797; PMID:1478668 !$#accession A44369 !'##molecule_type DNA !'##residues 1-17 ##label COF !'##cross-references EMBL:Z12128; NID:g63653; PIDN:CAA78113.1; !1PID:g63654 !'##experimental_source White Leghorn REFERENCE A60852 !$#authors Cole, G.J.; Loewy, A.; Cross, N.V.; Akeson, R.; Glaser, L. !$#journal J. Cell Biol. (1986) 103:1739-1744 !$#title Topographic localization of the heparin-binding domain of !1the neural cell adhesion molecule N-CAM. !$#cross-references MUID:87057627; PMID:2430978 !$#accession A60852 !'##molecule_type protein !'##residues 20-29 ##label COL REFERENCE A43280 !$#authors Rao, Y.; Wu, X.F.; Gariepy, J.; Rutishauser, U.; Siu, C.H. !$#journal J. Cell Biol. (1992) 118:937-949 !$#title Identification of a peptide sequence involved in homophilic !1binding in the neural cell adhesion molecule NCAM. !$#cross-references MUID:92363934; PMID:1380002 !$#contents annotation; homophilic binding region COMMENT NCAM mediates cell-cell adhesion via homophilic binding with !1another NCAM molecule. COMMENT Various forms of NCAM are produced by alternative splicing. CLASSIFICATION #superfamily neural cell adhesion molecule; fibronectin type !1III repeat homology; immunoglobulin homology KEYWORDS alternative splicing; brain; cell adhesion; duplication; !1heparin binding; sialoglycoprotein; transmembrane protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-1091 #product neural cell adhesion molecule, long domain !8form #status experimental #label MAT\ !$20-809,1071-1091 #product neural cell adhesion molecule, short domain !8form #status experimental #label SDF\ !$20-711 #domain extracellular #status predicted #label EXT\ !$34-98 #domain immunoglobulin homology #label IMM1\ !$132-191 #domain immunoglobulin homology #label IMM2\ !$152-156 #region heparin binding #status predicted\ !$161-165 #region heparin binding #status predicted\ !$228-289 #domain immunoglobulin homology #label IMM3\ !$262-271 #region NCAM binding #status experimental\ !$322-387 #domain immunoglobulin homology #label IMM4\ !$419-481 #domain immunoglobulin homology #label IMM5\ !$518-595 #domain fibronectin type III repeat homology #label !8FN3A\ !$624-685 #domain fibronectin type III repeat homology #label !8FN3B\ !$712-729 #domain transmembrane #status predicted #label TMM\ !$730-1091 #domain intracellular #status predicted #label INT\ !$41-96,139-189, !$235-287,329-385, !$426-479 #disulfide_bonds #status predicted\ !$222 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$315,347,423,449,478 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1091 #molecular-weight 117396 #checksum 7449 SEQUENCE /// ENTRY IJXLNL #type complete TITLE neural cell adhesion molecule long domain form precursor - African clawed frog ALTERNATE_NAMES NCAM-180 CONTAINS neural cell adhesion molecule, short domain form (NCAM-140) ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 22-Jun-1999 ACCESSIONS S09600 REFERENCE S09600 !$#authors Krieg, P.A.; Sakaguchi, D.S.; Kintner, C.R. !$#journal Nucleic Acids Res. (1989) 17:10321-10335 !$#title Primary structure and developmental expression of a large !1cytoplasmic domain form of Xenopus laevis neural cell !1adhesion molecule (NCAM). !$#cross-references MUID:90098871; PMID:2481269 !$#accession S09600 !'##molecule_type mRNA !'##residues 1-1088 ##label KRI !'##cross-references EMBL:M25696; NID:g214609; PIDN:AAA49909.1; !1PID:g214610 !'##note the authors translated the codon AAA for residue 970 as Leu COMMENT NCAM mediates cell-cell adhesion via homophilic binding with !1another NCAM molecule. COMMENT Several forms of NCAM are produced by alternative splicing. GENETICS !$#gene NCAM CLASSIFICATION #superfamily neural cell adhesion molecule; fibronectin type !1III repeat homology; immunoglobulin homology KEYWORDS alternative splicing; brain; cell adhesion; duplication; !1heparin binding; sialoglycoprotein; transmembrane protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-1088 #product neural cell adhesion molecule, long domain !8form #status predicted #label LDF\ !$20-803,1050-1088 #product neural cell adhesion molecule, short domain !8form #status predicted #label SDF\ !$20-705 #domain extracellular #status predicted #label EXT\ !$34-95 #domain immunoglobulin homology #label IMM1\ !$129-188 #domain immunoglobulin homology #label IMM2\ !$149-153 #region heparin binding #status predicted\ !$158-162 #region heparin binding #status predicted\ !$225-284 #domain immunoglobulin homology #label IMM3\ !$317-381 #domain immunoglobulin homology #label IMM4\ !$413-475 #domain immunoglobulin homology #label IMM5\ !$512-589 #domain fibronectin type III repeat homology #label !8FN3A\ !$618-679 #domain fibronectin type III repeat homology #label !8FN3B\ !$706-723 #domain transmembrane #status predicted #label TMM\ !$724-1088 #domain intracellular #status predicted #label INT\ !$41-93,136-186, !$232-282,323-379, !$420-473 #disulfide_bonds #status predicted\ !$219,310,341,417, !$443,472 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1088 #molecular-weight 117777 #checksum 8545 SEQUENCE /// ENTRY A41060 #type complete TITLE neural cell adhesion molecule L1 precursor - human ALTERNATE_NAMES L1CAM ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A41060; S18454; A35331; S21971; S21972; A60223; A31072; !1G02506 REFERENCE A41060 !$#authors Hlavin, M.L.; Lemmon, V. !$#journal Genomics (1991) 11:416-423 !$#title Molecular structure and functional testing of human L1CAM: !1an interspecies comparison. !$#cross-references MUID:92120663; PMID:1769655 !$#accession A41060 !'##molecule_type mRNA !'##residues 1-1257 ##label HLA !'##cross-references GB:M64296; NID:g186053; PIDN:AAC14352.1; !1PID:g3068548 REFERENCE S18454 !$#authors Kobayashi, M.; Miura, M.; Asou, H.; Uyemura, K. !$#journal Biochim. Biophys. Acta (1991) 1090:238-240 !$#title Molecular cloning of cell adhesion molecule L1 from human !1nervous tissue: a comparison of the primary sequences of L1 !1molecules of different origin. !$#cross-references MUID:92031698; PMID:1932117 !$#accession S18454 !'##molecule_type mRNA !'##residues 1-3,'V',5-215,'I',217-249,'T',251-275,'SV',278-356,'E', !1358-625,'V',627-1257 ##label KOB !'##cross-references EMBL:X59847; NID:g35009; PIDN:CAA42508.1; !1PID:g35010 !'##note the authors translated the codon GAA for residue 27 as Gly REFERENCE A35331 !$#authors Djabali, M.; Mattei, M.G.; Nguyen, C.; Roux, D.; Demengeot, !1J.; Denizot, F.; Moos, M.; Schachner, M.; Goridis, C.; !1Jordan, B.R. !$#journal Genomics (1990) 7:587-593 !$#title The gene encoding L1, a neural adhesion molecule of the !1immunoglobulin family, is located on the X chromosome in !1mouse and man. !$#cross-references MUID:90353957; PMID:2387585 !$#accession A35331 !'##molecule_type DNA !'##residues 332-371 ##label DJA !'##cross-references GB:M55271 REFERENCE S21971 !$#authors Rosenthal, A.; MacKinnon, R.N.; Jones, D.S.C. !$#journal Nucleic Acids Res. (1991) 19:5395-5401 !$#title PCR walking from microdissection clone M54 identifies three !1exons from the human gene for the neural cell adhesion !1molecule L1 (CAM-L1). !$#cross-references MUID:92020233; PMID:1923824 !$#accession S21971 !'##molecule_type DNA !'##residues 1082-1176 ##label ROS !'##cross-references EMBL:X58775; NID:g29642; PIDN:CAA41576.1; !1PID:g29643 !$#accession S21972 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type mRNA !'##residues 353-935,'V',937-1176 ##label RO2 !'##cross-references EMBL:X58776; NID:g29644; PIDN:CAB37831.1; !1PID:g4467833 REFERENCE A60223 !$#authors Harper, J.R.; Prince, J.T.; Healy, P.A.; Stuart, J.K.; !1Nauman, S.J.; Stallcup, W.B. !$#journal J. Neurochem. (1991) 56:797-804 !$#title Isolation and sequence of partial cDNA clones of human L1: !1homology of human and rodent L1 in the cytoplasmic region. !$#cross-references MUID:91132183; PMID:1993895 !$#accession A60223 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1030-1115,'WLC',1118-1176,1181-1257 ##label HAR REFERENCE A31072 !$#authors Wolff, J.M.; Frank, R.; Mujoo, K.; Spiro, R.C.; Reisfeld, !1R.A.; Rathjen, F.G. !$#journal J. Biol. Chem. (1988) 263:11943-11947 !$#title A human brain glycoprotein related to the mouse cell !1adhesion molecule L1. !$#cross-references MUID:88298876; PMID:3136168 !$#accession A31072 !'##molecule_type protein !'##residues 'Q',21-36 ##label WOL REFERENCE H01368 !$#authors Platzer, M.; Bauer, D.; Drescher, B. !$#submission submitted to the EMBL Data Library, March 1995 !$#accession G02506 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-1257 ##label PLA !'##cross-references EMBL:U52112; NID:g1302657; PIDN:AAC51746.1; !1PID:g1302658 GENETICS !$#gene GDB:L1CAM !'##cross-references GDB:120133; OMIM:303350; OMIM:308840 !$#map_position Xq28-Xq28 !$#introns 26/1; 31/1; 66/2; 134/1; 175/1; 232/1; 269/2; 331/1; 375/1; !1423/1; 460/2; 516/1; 568/2; 610/1; 647/1; 713/1; 736/3; 811/ !11; 849/3; 917/1; 958/1; 1016/1; 1056/1; 1108/1; 1153/1; !11177/2; 1181/2 CLASSIFICATION #superfamily neural cell adhesion molecule L1; fibronectin !1type III repeat homology; immunoglobulin homology KEYWORDS alternative splicing; cell adhesion; duplication; !1glycoprotein; transmembrane protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-1257 #product neural cell adhesion molecule L1 #status !8predicted #label MAT\ !$257-314 #domain immunoglobulin homology #label IMM1\ !$532-593 #domain immunoglobulin homology #label IMM2 SUMMARY #length 1257 #molecular-weight 140002 #checksum 8098 SEQUENCE /// ENTRY S05479 #type complete TITLE neural cell adhesion molecule L1 precursor - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S05479; B60850; S22167 REFERENCE S05479 !$#authors Moos, M.; Tacke, R.; Scherer, H.; Teplow, D.; Frueh, K.; !1Schachner, M. !$#journal Nature (1988) 334:701-703 !$#title Neural adhesion molecule L1 as a member of the !1immunoglobulin superfamily with binding domains similar to !1fibronectin. !$#cross-references MUID:88318924; PMID:3412448 !$#accession S05479 !'##molecule_type mRNA !'##residues 1-1260 ##label MOO !'##cross-references EMBL:X12875; NID:g53336; PIDN:CAA31368.1; !1PID:g53337 !'##note the authors translated the codon CCT for residue 166 as Leu, !1ACT for residue 396 as Ser, and AGT for residue 705 as Thr !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE A60850 !$#authors Rathjen, F.G.; Wolff, J.M.; Frank, R.; Bonhoeffer, F.; !1Rutishauser, U. !$#journal J. Cell Biol. (1987) 104:343-353 !$#title Membrane glycoproteins involved in neurite fasciculation. !$#cross-references MUID:87109457; PMID:3805123 !$#accession B60850 !'##molecule_type protein !'##residues 20-28,'XX',31-36 ##label RAT REFERENCE S22167 !$#authors Kohl, A.; Giese, K.P.; Mohajeri, M.H.; Montag, D.; Moos, M.; !1Schachner, M. !$#submission submitted to the EMBL Data Library, December 1991 !$#description Analysis of promoter activity and 5' genomic structure of !1the neural cell adhesion molecule L1. !$#accession S22167 !'##molecule_type DNA !'##residues 1-165,'L',167-189,'E',191-281,'S',283-395,'S',397-514, !1'APEKNPVDV',524,'GEGNETNNM',534,550-552,'K' ##label KOH !'##cross-references EMBL:X63511 GENETICS !$#introns 26/1; 31/1; 66/2; 133/1; 174/1; 231/1; 268/2; 330/1; 374/1; !1422/1; 459/2 !$#note the list of introns may be incomplete CLASSIFICATION #superfamily neural cell adhesion molecule L1; fibronectin !1type III repeat homology; immunoglobulin homology KEYWORDS alternative splicing; cell adhesion; duplication; !1glycoprotein; transmembrane protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-1260 #product neural cell adhesion molecule #status !8experimental #label MAT\ !$256-313 #domain immunoglobulin homology #label IMM1\ !$440-498 #domain immunoglobulin homology #label IMM2\ !$531-592 #domain immunoglobulin homology #label IMM3 SUMMARY #length 1260 #molecular-weight 140968 #checksum 2327 SEQUENCE /// ENTRY A37967 #type complete TITLE neural cell adhesion molecule Ng-CAM precursor - chicken ALTERNATE_NAMES neural glycoprotein G4 ORGANISM #formal_name Gallus gallus #common_name chicken DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A37967; A60850; S16452 REFERENCE A37967 !$#authors Burgoon, M.P.; Grumet, M.; Mauro, V.; Edelman, G.M.; !1Cunningham, B.A. !$#journal J. Cell Biol. (1991) 112:1017-1029 !$#title Structure of the chicken neuron-glia cell adhesion molecule, !1Ng-CAM: origin of the polypeptides and relation to the Ig !1superfamily. !$#cross-references MUID:91154306; PMID:1705558 !$#accession A37967 !'##molecule_type mRNA !'##residues 1-1265 ##label BUR !'##cross-references GB:X56969 REFERENCE A60850 !$#authors Rathjen, F.G.; Wolff, J.M.; Frank, R.; Bonhoeffer, F.; !1Rutishauser, U. !$#journal J. Cell Biol. (1987) 104:343-353 !$#title Membrane glycoproteins involved in neurite fasciculation. !$#cross-references MUID:87109457; PMID:3805123 !$#accession A60850 !'##molecule_type protein !'##residues 21-29,'X',31-37 ##label RAT CLASSIFICATION #superfamily neural cell adhesion molecule L1; fibronectin !1type III repeat homology; immunoglobulin homology KEYWORDS cell adhesion; duplication; glycoprotein; membrane protein FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-1265 #product neural cell adhesion molecule Ng-CAM #status !8predicted #label MAT\ !$340-398 #domain immunoglobulin homology #label IMM1\ !$433-491 #domain immunoglobulin homology #label IMM2\ !$524-582 #domain immunoglobulin homology #label IMM3 SUMMARY #length 1265 #molecular-weight 136641 #checksum 5562 SEQUENCE /// ENTRY A39640 #type complete TITLE neural cell adhesion molecule Nr-CAM precursor - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A39640; S16451 REFERENCE A39640 !$#authors Grumet, M.; Mauro, V.; Burgoon, M.P.; Edelman, G.M.; !1Cunningham, B.A. !$#journal J. Cell Biol. (1991) 113:1399-1412 !$#title Structure of a new nervous system glycoprotein, Nr-CAM, and !1its relationship to subgroups of neural cell adhesion !1molecules. !$#cross-references MUID:91258407; PMID:2045418 !$#accession A39640 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-1268 ##label GRU !'##cross-references GB:X58482; NID:g63706; PIDN:CAA41391.1; PID:g63707 CLASSIFICATION #superfamily neural cell adhesion molecule L1; fibronectin !1type III repeat homology; immunoglobulin homology KEYWORDS alternative splicing; cell adhesion; duplication; !1glycoprotein; membrane protein FEATURE !$261-318 #domain immunoglobulin homology #label IMM SUMMARY #length 1268 #molecular-weight 140274 #checksum 2695 SEQUENCE /// ENTRY A32579 #type complete TITLE neuroglian - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A32579 REFERENCE A32579 !$#authors Bieber, A.J.; Snow, P.M.; Hortsch, M.; Patel, N.H.; Jacobs, !1J.R.; Traquina, Z.R.; Schilling, J.; Goodman, C.S. !$#journal Cell (1989) 59:447-460 !$#title Drosophila neuroglian: a member of the immunoglobulin !1superfamily with extensive homology to the vertebrate neural !1adhesion molecule L1. !$#cross-references MUID:90030418; PMID:2805067 !$#accession A32579 !'##status preliminary !'##molecule_type mRNA !'##residues 1-1239 ##label BIE !'##cross-references GB:M28231; NID:g157998; PIDN:AAA28728.1; !1PID:g157999 !'##note the authors translated the codon TAT for residue 1234 as Thr !1and AAA for residue 1237 as Leu; codons for residues 192-199 !1and 232-239 were mistranslated GENETICS !$#gene FlyBase:Nrg !'##cross-references FlyBase:FBgn0002968 CLASSIFICATION #superfamily neural cell adhesion molecule L1; fibronectin !1type III repeat homology; immunoglobulin homology KEYWORDS alternative splicing; cell adhesion; duplication; membrane !1protein FEATURE !$353-412 #domain immunoglobulin homology #label IMM1\ !$446-502 #domain immunoglobulin homology #label IMM2\ !$535-596 #domain immunoglobulin homology #label IMM3 SUMMARY #length 1239 #molecular-weight 138361 #checksum 7663 SEQUENCE /// ENTRY I61596 #type complete TITLE advanced glycosylation end-products receptor precursor - human ALTERNATE_NAMES advanced glycosylation end product-binding protein, 35K; glycoprotein receptor RAGE ORGANISM #formal_name Homo sapiens #common_name man DATE 24-May-1996 #sequence_revision 07-Feb-1997 #text_change 16-Jul-1999 ACCESSIONS I61596; B42879; S27968 REFERENCE A55562 !$#authors Sugaya, K.; Fukagawa, T.; Matsumoto, K.; Mita, K.; !1Takahashi, E.; Ando, A.; Inoko, H.; Ikemura, T. !$#journal Genomics (1994) 23:408-419 !$#title Three genes in the human MHC class III region near the !1junction with the class II: gene for receptor of advanced !1glycosylation end products, PBX2 homeobox gene and a notch !1homolog, human counterpart of mouse mammary tumor gene !1int-3. !$#cross-references MUID:95137587; PMID:7835890 !$#accession I61596 !'##status nucleic acid sequence not shown; translation not shown; !1translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-404 ##label RES !'##cross-references GB:D28769; NID:g561657; PIDN:BAA05958.1; !1PID:g561659 REFERENCE A42879 !$#authors Neeper, M.; Schmidt, A.M.; Brett, J.; Yan, S.D.; Wang, F.; !1Pan, Y.C.; Elliston, K.; Stern, D.; Shaw, A. !$#journal J. Biol. Chem. (1992) 267:14998-15004 !$#title Cloning and expression of a cell surface receptor for !1advanced glycosylation end products of proteins. !$#cross-references MUID:92340547; PMID:1378843 !$#accession B42879 !'##molecule_type mRNA !'##residues 'G',2-99,'R',101-404 ##label NEE !'##cross-references EMBL:M91211; NID:g190845; PIDN:AAA03574.1; !1PID:g190846 !'##experimental_source lung !'##note sequence extracted from NCBI backbone (NCBIP:109438) COMMENT Advanced glycosylation end products are heterogeneous !1nonenzymatically glycosylated proteins that accumulate in !1hyperglycemia; they bind to endothelial cells, causing toxic !1alterations in cellular function, thus contributing to !1tissue lesions in diabetes. COMMENT This receptor appears also to mediate the effects of amyloid !1beta peptide on neurons, resulting in oxidant stress, and on !1microglia, resulting in cytokine production; thus it !1probably operates in the neurotoxic pathway that produces !1dementia in Alzheimer's disease. GENETICS !$#gene GDB:AGER !'##cross-references GDB:306354; OMIM:600214 !$#map_position 6p21.3-6p21.3 !$#introns 18/1; 53/3; 119/1; 140/3; 170/1; 231/1; 274/3; 322/1; 331/1; !1373/2 FUNCTION !$#description neuronal receptor for amphoterin, a DNA-binding protein !1involved in neurite outgrowth CLASSIFICATION #superfamily advanced glycosylation end products receptor; !1immunoglobulin homology KEYWORDS Alzheimer's disease; glycoprotein; receptor; transmembrane !1protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-404 #product advanced glycosylation end products receptor !8#status predicted #label MAT\ !$23-344 #domain extracellular #status predicted #label EXT\ !$31-101 #domain immunoglobulin homology #label IM1\ !$137-210 #domain immunoglobulin homology #label IM2\ !$252-303 #domain immunoglobulin homology #label IM3\ !$345-362 #domain transmembrane #status predicted #label TMM\ !$363-404 #domain intracellular #status predicted #label INT\ !$25,81 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$38-99,144-208, !$259-301 #disulfide_bonds #status predicted SUMMARY #length 404 #molecular-weight 42802 #checksum 5865 SEQUENCE /// ENTRY A42879 #type complete TITLE advanced glycosylation end-products receptor precursor - bovine ALTERNATE_NAMES advanced glycosylation end product-binding protein, 35K; glycoprotein receptor RAGE ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 04-Mar-1993 #sequence_revision 07-Feb-1997 #text_change 16-Jul-1999 ACCESSIONS A42879; A42878; S27949 REFERENCE A42879 !$#authors Neeper, M.; Schmidt, A.M.; Brett, J.; Yan, S.D.; Wang, F.; !1Pan, Y.C.; Elliston, K.; Stern, D.; Shaw, A. !$#journal J. Biol. Chem. (1992) 267:14998-15004 !$#title Cloning and expression of a cell surface receptor for !1advanced glycosylation end products of proteins. !$#cross-references MUID:92340547; PMID:1378843 !$#accession A42879 !'##molecule_type mRNA !'##residues 1-416 ##label NEE !'##cross-references GB:M91212; NID:g163650; PIDN:AAA03575.1; !1PID:g163651 !'##experimental_source lung !'##note sequence extracted from NCBI backbone (NCBIP:109436) !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing REFERENCE A42878 !$#authors Schmidt, A.M.; Vianna, M.; Gerlach, M.; Brett, J.; Ryan, J.; !1Kao, J.; Esposito, C.; Hegarty, H.; Hurley, W.; Clauss, M.; !1Wang, F.; Pan, Y.C.E.; Tsang, T.C.; Stern, D. !$#journal J. Biol. Chem. (1992) 267:14987-14997 !$#title Isolation and characterization of two binding proteins for !1advanced glycosylation end products from bovine lung which !1are present on the endothelial cell surface. !$#cross-references MUID:92340546; PMID:1321822 !$#accession A42878 !'##molecule_type protein !'##residues 23-24,'X',26-37,'X',39-49,'XX',52-54 ##label SCH !'##experimental_source endothelial cells !'##note sequence extracted from NCBI backbone (NCBIP:109434) COMMENT Advanced glycosylation end products are heterogeneous !1nonenzymatically glycosylated proteins that accumulate in !1hyperglycemia; they bind to endothelial cells, causing toxic !1alterations in cellular function, thus contributing to !1tissue lesions in diabetes. COMMENT This receptor appears also to mediate the effects of amyloid !1beta peptide on neurons, resulting in oxidant stress, and on !1microglia, resulting in cytokine production; thus it !1probably operates in the neurotoxic pathway that produces !1dementia in Alzheimer's disease. FUNCTION !$#description neuronal receptor for amphoterin, a DNA-binding protein !1involved in neurite outgrowth CLASSIFICATION #superfamily advanced glycosylation end products receptor; !1immunoglobulin homology KEYWORDS Alzheimer's disease; glycoprotein; receptor; transmembrane !1protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-416 #product advanced glycosylation end-products receptor !8RAGE #status predicted #label MAT\ !$23-354 #domain extracellular #status predicted #label EXT\ !$31-100 #domain immunoglobulin homology #label IM1\ !$136-209 #domain immunoglobulin homology #label IM2\ !$262-313 #domain immunoglobulin homology #label IM3\ !$355-372 #domain transmembrane #status predicted #label TMM\ !$373-416 #domain intracellular #status predicted #label INT\ !$25,80 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$38-98,143-207, !$269-311 #disulfide_bonds #status predicted SUMMARY #length 416 #molecular-weight 44182 #checksum 6608 SEQUENCE /// ENTRY A29849 #type complete TITLE intercellular adhesion molecule ICAM-1 precursor - human ALTERNATE_NAMES CD54 antigen; rhinovirus receptor ORGANISM #formal_name Homo sapiens #common_name man DATE 18-Oct-1989 #sequence_revision 07-Jul-1995 #text_change 19-Jan-2001 ACCESSIONS A29849; S00573; A32943; A32191; A39471; A46470; S22876; !1I37578; A31495 REFERENCE A29849 !$#authors Staunton, D.E.; Marlin, S.D.; Stratowa, C.; Dustin, M.L.; !1Springer, T.A. !$#journal Cell (1988) 52:925-933 !$#title Primary structure of ICAM-1 demonstrates interaction between !1members of the immunoglobulin and integrin supergene !1families. !$#cross-references MUID:88165043; PMID:3349522 !$#accession A29849 !'##molecule_type mRNA !'##residues 1-532 ##label STA !'##cross-references GB:J03132; NID:g184534; PIDN:AAA52709.1; !1PID:g306896 REFERENCE S00573 !$#authors Simmons, D.; Makgoba, M.W.; Seed, B. !$#journal Nature (1988) 331:624-627 !$#title ICAM, an adhesion ligand of LFA-1, is homologous to the !1neural cell adhesion molecule NCAM. !$#cross-references MUID:88122667; PMID:3340213 !$#accession S00573 !'##molecule_type mRNA !'##residues 1-532 ##label SIM !'##cross-references EMBL:X06990; NID:g32614; PIDN:CAA30051.1; !1PID:g758074 REFERENCE A32943 !$#authors Tomassini, J.E.; Graham, D.; DeWitt, C.M.; Lineberger, D.W.; !1Rodkey, J.A.; Colonno, R.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:4907-4911 !$#title cDNA cloning reveals that the major group rhinovirus !1receptor on HeLa cells is intercellular adhesion molecule 1. !$#cross-references MUID:89296913; PMID:2544880 !$#accession A32943 !'##molecule_type mRNA !'##residues 1-468,'K',470-532 ##label TOM !'##cross-references GB:M24283; NID:g184532; PIDN:AAA52708.1; !1PID:g306895 REFERENCE A32191 !$#authors Johnson, J.P.; Stade, B.G.; Holzmann, B.; Schwaeble, W.; !1Riethmueller, G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:641-644 !$#title De novo expression of intercellular-adhesion molecule 1 in !1melanoma correlates with increased risk of metastasis. !$#cross-references MUID:89098986; PMID:2643120 !$#accession A32191 !'##status preliminary; nucleic acid sequence not shown; not compared !1with conceptual translation !'##molecule_type mRNA !'##residues 368-431 ##label JOH REFERENCE A39471 !$#authors Degitz, K.; Lian-Jie, L.; Caughman, S.W. !$#journal J. Biol. Chem. (1991) 266:14024-14030 !$#title Cloning and characterization of the 5'-transcriptional !1regulatory region of the human intercellular adhesion !1molecule 1 gene. !$#cross-references MUID:91310692; PMID:1677359 !$#accession A39471 !'##molecule_type DNA !'##residues 1-22 ##label DEG !'##cross-references GB:M65001 REFERENCE A46470 !$#authors Voraberger, G.; Schafer, R.; Stratowa, C. !$#journal J. Immunol. (1991) 147:2777-2786 !$#title Cloning of the human gene for intercellular adhesion !1molecule 1 and analysis of its 5'-regulatory region. !1Induction by cytokines and phorbol ester. !$#cross-references MUID:92013093; PMID:1680919 !$#accession A46470 !'##molecule_type DNA !'##residues 1-22 ##label VOR !'##note sequence extracted from NCBI backbone (NCBIN:59007, !1NCBIP:59009) REFERENCE S22876 !$#authors Stade, B.G.; Messer, G.; Riethmueller, G.; Johnson, J.P. !$#journal Immunobiology (1990) 182:79-87 !$#title Structural characteristics of the 5' region of the human !1ICAM-1 gene. !$#cross-references MUID:91276491; PMID:1983003 !$#accession S22876 !'##status preliminary !'##molecule_type DNA !'##residues 1-8,'PV',11-22 ##label STD1 !'##cross-references EMBL:X57151; NID:g32621; PIDN:CAA40441.1; !1PID:g32622 REFERENCE I37578 !$#authors Stade, B.G.; Messer, G.; Riethmueller, G.; Johnson, J.P. !$#journal Immunobiology (1990) 181:851-856 !$#title Structural characteristics of the 5' region of the Human !1ICAM-1 gene. !$#accession I37578 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-8,'PV',11-22 ##label STD2 !'##cross-references EMBL:X57151; NID:g32621; PIDN:CAA40441.1; !1PID:g32622 REFERENCE A31495 !$#authors Greve, J.M.; Davis, G.; Meyer, A.M.; Forte, C.P.; Yost, !1S.C.; Marlor, C.W.; Kamarck, M.E.; McClelland, A. !$#journal Cell (1989) 56:839-847 !$#title The major human rhinovirus receptor is ICAM-1. !$#cross-references MUID:89168424; PMID:2538243 !$#accession A31495 !'##molecule_type protein !'##residues 35-40;67-91,'X',93-95,'X',97,'I',99-100,'XX',103;155,'X', !1157-171,'R',173-178,'X',180-182,'X',184;225,'T',227-236,'X', !1238-248,'X',250,'XIXI';433-453,'X',455-456,'I', !1458-460;510-529 ##label GRE COMMENT ICAM mediates cell-cell adhesion primarily via heterophilic !1binding with the lymphocyte function-associated antigen. GENETICS !$#gene GDB:ICAM1 !'##cross-references GDB:120076; OMIM:147840 !$#map_position 19p13.2-19p13.2 CLASSIFICATION #superfamily intercellular adhesion molecule; immunoglobulin !1homology KEYWORDS blocked amino end; cell adhesion; glycoprotein; !1transmembrane protein FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-532 #product intercellular adhesion molecule ICAM-1 !8#status predicted #label MAT\ !$28-480 #domain extracellular #status predicted #label EXT\ !$41-98 #domain immunoglobulin homology #label IM1\ !$128-188 #domain immunoglobulin homology #label IM2\ !$152-154 #region cell adhesion #status predicted\ !$230-292 #domain immunoglobulin homology #label IM3\ !$325-373 #domain immunoglobulin homology #label IM4\ !$481-504 #domain transmembrane #status predicted #label TMM\ !$505-532 #domain intracellular #status predicted #label INT\ !$28 #modified_site blocked amino end (Gln) (in mature !8form) (probably pyrrolidone carboxylic acid) #status !8experimental\ !$48-96,135-186, !$237-290,332-371 #disulfide_bonds #status predicted\ !$130,145,183,202, !$267,296,385,406 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 532 #molecular-weight 57826 #checksum 6460 SEQUENCE /// ENTRY S28904 #type complete TITLE intercellular adhesion molecule ICAM-3 precursor - human ALTERNATE_NAMES intercellular adhesion molecule ICAM-R ORGANISM #formal_name Homo sapiens #common_name man DATE 07-Apr-1994 #sequence_revision 07-Jul-1995 #text_change 24-Nov-1999 ACCESSIONS S28904; S37703; S28905; S31520; PH1576 REFERENCE S28904 !$#authors Fawcett, J.; Holness, C.L.L.; Needham, L.A.; Turley, H.; !1Gatter, K.C.; Mason, D.Y.; Simmons, D.L. !$#journal Nature (1992) 360:481-484 !$#title Molecular cloning of ICAM-3, a third ligand for LFA-1, !1constitutively expressed on resting leukocytes. !$#cross-references MUID:93078881; PMID:1448173 !$#accession S28904 !'##molecule_type mRNA !'##residues 1-547 ##label FAW !'##cross-references EMBL:S50015; NID:g260878; PIDN:AAB24331.1; !1PID:g260879 REFERENCE S37703 !$#authors Fawcett, J.; Holness, C.L.; Needham, L.A.; Turley, H.; !1Gatter, K.C.; Mason, D.Y.; Simmons, D.L. !$#submission submitted to the EMBL Data Library, February 1993 !$#accession S37703 !'##molecule_type mRNA !'##residues 1-59,'F',61-547 ##label FA2 !'##cross-references EMBL:S50015 REFERENCE S28905 !$#authors Vazeux, R.; Hoffman, P.A.; Tomita, J.K.; Dickinson, E.S.; !1Jasman, R.L.; John, T.S.; Gallatin, W.M. !$#journal Nature (1992) 360:485-488 !$#title Cloning and characterization of a new intercellular adhesion !1molecule ICAM-R. !$#cross-references MUID:93078882; PMID:1448174 !$#accession S28905 !'##molecule_type mRNA !'##residues 1-547 ##label VAZ !'##cross-references EMBL:X69711; NID:g296534; PIDN:CAA49369.1; !1PID:g296535 REFERENCE S31520 !$#authors de Fougerolles, A.R.; Klickstein, L.B.; Springer, T.A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Cloning and expression of ICAM-3 reveals strong homology to !1other Ig family counter receptors for LFA1. !$#accession S31520 !'##molecule_type mRNA !'##residues 1-547 ##label DEF !'##cross-references EMBL:X69819; NID:g32627; PIDN:CAA49473.1; !1PID:g32628 REFERENCE PH1576 !$#authors de Fougerolles, A.R.; Klickstein, L.B.; Springer, T.A. !$#journal J. Exp. Med. (1993) 177:1187-1192 !$#title Cloning and expression of intercellular adhesion molecule 3 !1reveals strong homology to other immunoglobulin family !1counter-receptors for lymphocyte function-associated antigen !11. !$#cross-references MUID:93210474; PMID:8459213 !$#accession PH1576 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 30-547 ##label DE2 COMMENT ICAM mediates cell-cell adhesion primarily via heterophilic !1binding with the lymphocyte function-associated antigen. GENETICS !$#gene GDB:ICAM3 !'##cross-references GDB:136236; OMIM:146631 !$#map_position 19p13.3-19p13.2 CLASSIFICATION #superfamily intercellular adhesion molecule; immunoglobulin !1homology KEYWORDS blocked amino end; cell adhesion; glycoprotein; !1transmembrane protein FEATURE !$1-29 #domain signal sequence #status predicted #label SIG\ !$30-547 #product intercellular adhesion molecule ICAM-3 !8#status predicted #label MAT\ !$30-485 #domain extracellular #status predicted #label EXT\ !$46-102 #domain immunoglobulin homology #label IM1\ !$132-192 #domain immunoglobulin homology #label IM2\ !$234-296 #domain immunoglobulin homology #label IM3\ !$329-377 #domain immunoglobulin homology #label IM4\ !$486-510 #domain transmembrane #status predicted #label TMM\ !$511-547 #domain intracellular #status predicted #label INT\ !$30 #modified_site blocked amino end (Gln) (in mature !8form) (probably pyrrolidone carboxylic acid) #status !8experimental\ !$52,84,87,101,110, !$134,206,264,295, !$308,320,363,389, !$453,457 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$53-100,139-190, !$241-294,336-375 #disulfide_bonds #status predicted SUMMARY #length 547 #molecular-weight 59383 #checksum 2498 SEQUENCE /// ENTRY B44294 #type complete TITLE unc-5 protein, long form - Caenorhabditis elegans CONTAINS unc-5 protein, short form ORGANISM #formal_name Caenorhabditis elegans DATE 30-Apr-1993 #sequence_revision 28-Jul-1995 #text_change 05-Nov-1999 ACCESSIONS B44294; T32540; A44294 REFERENCE A44294 !$#authors Leung-Hagesteijn, C.; Spence, A.M.; Stern, B.D.; Zhou, Y.; !1Su, M.W.; Hedgecock, E.M.; Culotti, J.G. !$#journal Cell (1992) 71:289-299 !$#title UNC-5, a transmembrane protein with immunoglobulin and !1thrombospondin type 1 domains, guides cell and pioneer axon !1migrations in C. elegans. !$#cross-references MUID:93046629; PMID:1384987 !$#contents variety Bergerac !$#accession B44294 !'##molecule_type DNA !'##residues 1-947 ##label LEU !'##cross-references GB:S47168; NID:g258527; PIDN:AAB23867.1; !1PID:g258529 !'##note sequence extracted from NCBI backbone (NCBIN:116668, !1NCBIN:116670, NCBIN:116672, NCBIN:116674, NCBIN:116676, !1NCBIN:116678, NCBIN:116680, NCBIN:116682, NCBIN:116685, !1NCBIP:118648) !'##note authors translated the codon CTA for residue 642 as Val; !1sequence shown follows the authors' translation !'##note mRNA lacking the first exon is equally prevalent REFERENCE Z21187 !$#authors Latreille, P. !$#submission submitted to the EMBL Data Library, December 1997 !$#description The sequence of C. elegans cosmid B0273. !$#accession T32540 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-947 ##label LAT !'##cross-references EMBL:AF036698; PIDN:AAB88356.1; GSPDB:GN00022; !1CESP:B0273.4b !'##experimental_source strain Bristol N2; clone B0273 GENETICS !$#gene unc-5 !$#map_position 4 !$#introns 28/1; 69/3; 136/1; 170/3; 229/1; 351/2; 581/1; 886/3 FUNCTION !$#description required for guidance of pioneering axons and cells !1migrating dorsally along the body wall; proposed to be a !1receptor on the surface of the motile cells CLASSIFICATION #superfamily unc-5 protein; immunoglobulin homology; SH3 !1homology; thrombospondin type 1 repeat homology KEYWORDS alternative splicing; duplication; glycoprotein; receptor; !1transmembrane protein FEATURE !$30-947 #product unc-5 protein, short form #status predicted !8#label ALT\ !$46-116 #domain immunoglobulin homology #label IM1\ !$153-211 #domain immunoglobulin homology #label IM2\ !$229-300 #domain thrombospondin type 1 repeat homology #status !8atypical #label THR1\ !$301-354 #domain thrombospondin type 1 repeat homology #label !8THR2\ !$365-390 #domain transmembrane #status predicted #label TMM\ !$512-559 #domain SH3 homology #label SH3\ !$53-114,65-112, !$160-209 #disulfide_bonds #status predicted\ !$206 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 947 #molecular-weight 104728 #checksum 1023 SEQUENCE /// ENTRY IJHULM #type complete TITLE leukocyte adhesion protein beta chain (CD18) precursor - human ALTERNATE_NAMES integrin beta-2; LFA-1 beta chain; Mac-1 beta chain; p150,95 beta chain ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 23-Jul-1999 ACCESSIONS A25967; A91084; S19324; I70090; I70091; A29265; A94497 REFERENCE A25967 !$#authors Kishimoto, T.K.; O'Connor, K.; Lee, A.; Roberts, T.M.; !1Springer, T.A. !$#journal Cell (1987) 48:681-690 !$#title Cloning of the beta subunit of the leukocyte adhesion !1proteins: homology to an extracellular matrix receptor !1defines a novel supergene family. !$#cross-references MUID:87131080; PMID:3028646 !$#accession A25967 !'##molecule_type mRNA !'##residues 1-769 ##label KIS !'##cross-references GB:M15395; NID:g186933; PIDN:AAA59490.1; !1PID:g307113 !'##note source of LFA-1 was the SKW3 T-cell line; source of Mac-1 was !1pooled leukocytes; source of p150,95 was hairy cell leukemia !1spleens REFERENCE A91084 !$#authors Law, S.K.A.; Gagnon, J.; Hildreth, J.E.; Wells, C.E.; !1Willis, A.C.; Wong, A.J. !$#journal EMBO J. (1987) 6:915-919 !$#title The primary structure of the B-subunit of the cell surface !1adhesion glycoproteins LFA-1, CR3 and p150,95 and its !1relationship to the fibronectin receptor. !$#cross-references MUID:87246525; PMID:2954816 !$#accession A91084 !'##molecule_type mRNA !'##residues 9-198,'P',200-769 ##label LA2 !'##cross-references GB:Y00057; NID:g30228; PIDN:CAA68266.1; PID:g762939 REFERENCE S19324 !$#authors Weitzman, J.B.; Wells, C.E.; Wright, A.H.; Clark, P.A.; Law, !1S.K.A. !$#journal FEBS Lett. (1991) 294:97-103 !$#title The gene organisation of the human beta2 integrin subunit !1(CD18). !$#cross-references MUID:92077153; PMID:1683838 !$#accession S19324 !'##molecule_type DNA !'##residues !11-3;16-23;46-53;106-113;163-170;244-251;296-303;328-335; !1358-365;405-412;468-475;549-556;623-630;690-697;746-769 !1##label WEI REFERENCE I55376 !$#authors Nelson, C.; Rabb, H.; Arnaout, M.A. !$#journal J. Biol. Chem. (1992) 267:3351-3357 !$#title Genetic cause of leukocyte adhesion molecule deficiency. !1Abnormal splicing and a missense mutation in a conserved !1region of CD18 impair cell surface expression of beta 2 !1integrins. !$#cross-references MUID:92147694; PMID:1346613 !$#accession I70090 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 347-350,'S',352-355 ##label NEL !'##cross-references GB:S81234; NID:g245294; PIDN:AAB21404.1; !1PID:g245295 !'##note mutant form !$#accession I70091 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 246-247,'PSSQ',248-249 ##label RES !'##cross-references GB:S81252; NID:g245289; PIDN:AAB21402.1; !1PID:g245290 !'##note mutant splice form COMMENT The leukocyte adhesion proteins are noncovalently linked !1heterodimers of distinct alpha and identical beta chains. !1These structurally related glycoproteins mediate !1cell-adhesion reactions, and a deficiency of them is !1attributed to a genetic defect in the expression or !1structure of their common beta chain. COMMENT The cysteine residues are involved in intrachain disulfide !1bonds. GENETICS !$#gene GDB:ITGB2 !'##cross-references GDB:120574; OMIM:600065 !$#map_position 21q22.3-21q22.3 CLASSIFICATION #superfamily integrin beta chain; laminin-type EGF-like !1homology KEYWORDS cell adhesion; cytoskeleton; duplication; glycoprotein; !1heterodimer; leukocyte; pyroglutamic acid; transmembrane !1protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-769 #product leukocyte adhesion protein beta chain !8#status predicted #label MAT\ !$23-670 #domain extracellular #status predicted #label EXT\ !$445-631 #region cysteine-rich\ !$459-540 #region duplication\ !$541-627 #region duplication\ !$701-723 #domain transmembrane #status predicted #label MEM\ !$724-769 #domain intracellular #status predicted #label CYT\ !$23 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status predicted\ !$50,116,212,254,501 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 769 #molecular-weight 84790 #checksum 9238 SEQUENCE /// ENTRY JC1121 #type complete TITLE leukocyte adhesion protein beta chain precursor - bovine ALTERNATE_NAMES surface glycoprotein CD18 ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 23-Jul-1999 ACCESSIONS JC1121 REFERENCE JC1121 !$#authors Shuster, D.E.; Bosworth, B.T.; Kehrli Jr., M.E. !$#journal Gene (1992) 114:267-271 !$#title Sequence of the bovine CD18-encoding cDNA: Comparison with !1the human and murine glycoproteins. !$#cross-references MUID:92290287; PMID:1351021 !$#accession JC1121 !'##molecule_type mRNA !'##residues 1-769 ##label SHU !'##cross-references GB:M81233; NID:g162818; PIDN:AAA30438.1; !1PID:g162819 COMMENT The leukocyte adhesion proteins are noncovalently linked !1heterodimers of distinct alpha and identical beta chains. !1These structurally related glycoproteins mediate !1cell-adhesion reactions, and a deficiency of them is !1attributed to a genetic defect in the expression or !1structure of their common beta chain. CLASSIFICATION #superfamily integrin beta chain; laminin-type EGF-like !1homology KEYWORDS cell adhesion; cytoskeleton; duplication; glycoprotein; !1heterodimer; leukocyte; pyroglutamic acid; transmembrane !1protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-769 #product leukocyte adhesion protein beta chain !8#status predicted #label MAT\ !$23-670 #domain extracellular #status predicted #label EXT\ !$445-631 #region cysteine-rich\ !$701-723 #domain transmembrane #status predicted #label TMM\ !$724-769 #domain intracellular #status predicted #label CYT\ !$23 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status predicted\ !$50,116,254,501,642 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 769 #molecular-weight 84399 #checksum 9562 SEQUENCE /// ENTRY IJCH3 #type complete TITLE integrin, band 3 precursor - chicken ALTERNATE_NAMES CSAT antigen; JG22 antigen; RGD-receptor ORGANISM #formal_name Gallus gallus #common_name chicken DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 23-Jul-1999 ACCESSIONS A23947 REFERENCE A23947 !$#authors Tamkun, J.W.; DeSimone, D.W.; Fonda, D.; Patel, R.S.; Buck, !1C.; Horwitz, A.F.; Hynes, R.O. !$#journal Cell (1986) 46:271-282 !$#title Structure of integrin, a glycoprotein involved in the !1transmembrane linkage between fibronectin and actin. !$#cross-references MUID:86245073; PMID:3487386 !$#accession A23947 !'##molecule_type mRNA !'##residues 1-803 ##label TAM !'##cross-references GB:M14049; NID:g212213; PIDN:AAA48926.1; !1PID:g212214 !'##experimental_source embryonic fibroblasts !'##note the amino end of the mature protein is blocked COMMENT Integrin, an integral plasma membrane complex of three (two !1in mammalian cells) noncovalently associated glycoproteins, !1links the extracellular matrix with the intracellular !1cytoskeleton. COMMENT This transmembrane complex may be the target of oncogenic !1transformation that results in loss of fibronectin, !1disruption of normal cell-substrata adhesion, and !1disorganization of the cytoskeleton. The cytoplasmic domain !1of this subunit contains a potential tyrosine-kinase !1phosphorylation site. COMMENT The extracellular domain of this protein, like many membrane !1receptors, contains a cysteine-rich region, and the cysteine !1residues are presumed to be disulfide-bonded. CLASSIFICATION #superfamily integrin beta chain; laminin-type EGF-like !1homology KEYWORDS cell adhesion; cytoskeleton; duplication; extracellular !1matrix; glycoprotein; heterodimer; phosphoprotein; !1transmembrane protein FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-803 #product integrin, band 3 #status predicted #label !8MAT\ !$25-733 #domain extracellular #status predicted #label EXT\ !$467-654 #region cysteine-rich\ !$482-564,565-650 #region duplication\ !$734-756 #domain transmembrane #status predicted #label MEM\ !$757-803 #domain intracellular #status predicted #label INT\ !$216,273,367,410, !$421,433,445,486, !$525,589,624,674 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$788 #binding_site phosphate (Tyr) (covalent) #status !8predicted SUMMARY #length 803 #molecular-weight 88553 #checksum 4487 SEQUENCE /// ENTRY IJMSFB #type complete TITLE fibronectin receptor beta chain precursor - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 23-Jul-1999 ACCESSIONS PL0104; B60597 REFERENCE PL0103 !$#authors Holers, V.M.; Ruff, T.G.; Parks, D.L.; McDonald, J.A.; !1Ballard, L.L.; Brown, E.J. !$#journal J. Exp. Med. (1989) 169:1589-1605 !$#title Molecular cloning of a murine fibronectin receptor and its !1expression during inflammation. Expression of VLA-5 is !1increased in activated peritoneal macrophages in a manner !1discordant from major histocompatibility complex class II. !$#cross-references MUID:89235580; PMID:2523953 !$#accession PL0104 !'##molecule_type mRNA !'##residues 1-799 ##label HOL !'##cross-references GB:X15202; GB:Y00818; NID:g50986; PIDN:CAA33272.1; !1PID:g762977 !'##experimental_source strain BALB/c !'##note the cDNA clone was missing the first nucleotide of Met-1 REFERENCE A60597 !$#authors Ryseck, R.P.; Macdonald-Bravo, H.; Zerial, M.; Bravo, R. !$#journal Exp. Cell Res. (1989) 180:537-545 !$#title Coordinate induction of fibronectin, fibronectin receptor, !1tropomyosin, and actin genes in serum-stimulated !1fibroblasts. !$#cross-references MUID:89121031; PMID:2521606 !$#accession B60597 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type mRNA !'##residues 596-799 ##label RYS COMMENT The receptor is a heterodimer of alpha and beta chains. CLASSIFICATION #superfamily integrin beta chain; laminin-type EGF-like !1homology KEYWORDS cell adhesion; duplication; glycoprotein; heterodimer; !1receptor; transmembrane protein FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-799 #product fibronectin receptor beta chain #status !8predicted #label MAT\ !$21-729 #domain extracellular #status predicted #label EXT\ !$730-752 #domain transmembrane #status predicted #label TRA\ !$753-799 #domain intracellular #status predicted #label INT\ !$50,94,97,212,269, !$363,406,417,482, !$521,585,670 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 799 #molecular-weight 88324 #checksum 5760 SEQUENCE /// ENTRY JN0786 #type complete TITLE integrin beta-4 chain precursor - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jan-2000 ACCESSIONS JN0786 REFERENCE JN0786 !$#authors Kennel, S.J.; Foote, L.J.; Cimino, L.; Rizzo, M.G.; Chang, !1L.Y.; Sacchi, A. !$#journal Gene (1993) 130:209-216 !$#title Sequence of a cDNA encoding the beta 4 subunit of murine !1integrin. !$#cross-references MUID:93366176; PMID:8359687 !$#accession JN0786 !'##molecule_type mRNA !'##residues 1-1748 ##label KEN !'##experimental_source lung carcinoma CLASSIFICATION #superfamily integrin beta-4 chain; EGF homology; !1fibronectin type III repeat homology KEYWORDS cell adhesion; chondroitin sulfate proteoglycan; !1duplication; glycoprotein; heterodimer; transmembrane !1protein FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-1748 #product integrin beta 4 chain #status predicted !8#label MAT\ !$545-575 #domain EGF homology #label EGF\ !$711-733 #domain transmembrane #status predicted #label TMM\ !$328,493,581,619,695 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$515 #binding_site chondroitin sulfate (Ser) (covalent) !8#status predicted SUMMARY #length 1748 #molecular-weight 194336 #checksum 3816 SEQUENCE /// ENTRY LCHUL #type complete TITLE lacrimal lipocalin precursor - human ALTERNATE_NAMES lipocalin 1; PMFA; tear prealbumin; von Ebner's gland protein ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Jun-1993 #sequence_revision 02-Jun-1995 #text_change 22-Jun-1999 ACCESSIONS A44029; A49186; S29842; I53728; S18929; S34277 REFERENCE A44029 !$#authors Redl, B.; Holzfeind, P.; Lottspeich, F. !$#journal J. Biol. Chem. (1992) 267:20282-20287 !$#title cDNA cloning and sequencing reveals human tear prealbumin to !1be a member of the lipophilic-ligand carrier protein !1superfamily. !$#cross-references MUID:93015903; PMID:1400345 !$#accession A44029 !'##molecule_type mRNA; protein !'##residues 1-176 ##label RED !'##cross-references GB:M90424; NID:g642380; PIDN:AAA61845.1; !1PID:g184458 !'##experimental_source lacrimal gland, tears !'##note sequence extracted from NCBI backbone (NCBIN:115716, !1NCBIP:115717) !'##note part of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing !'##note 22-Leu and 24-Ser were also observed as amino-terminal residues REFERENCE A49186 !$#authors Lassagne, H.; Gachon, A.M. !$#journal Exp. Eye Res. (1993) 56:605-609 !$#title Cloning of a human lacrimal lipocalin secreted in tears. !$#cross-references MUID:93272888; PMID:8500570 !$#accession A49186 !'##molecule_type mRNA; protein !'##residues 1-176 ##label LAS !'##cross-references EMBL:X67647; NID:g313855; PIDN:CAA47889.1; !1PID:g313856 !'##experimental_source lacrimal gland !'##note sequence extracted from NCBI backbone (NCBIN:133186, !1NCBIP:133187) REFERENCE S29842 !$#authors Blaeker, M.; Kock, K.; Ahlers, C.; Buck, F.; Schmale, H. !$#journal Biochim. Biophys. Acta (1993) 1172:131-137 !$#title Molecular cloning of human von Ebner's gland protein, a !1member of the lipocalin superfamily highly expressed in !1lingual salivary glands. !$#cross-references MUID:93176795; PMID:7679926 !$#accession S29842 !'##status preliminary !'##molecule_type mRNA !'##residues 1-176 ##label BL2 !'##cross-references EMBL:X62418; NID:g37660; PIDN:CAA44284.1; !1PID:g37661 REFERENCE I53728 !$#authors Holzfeind, P.; Redl, B. !$#journal Gene (1994) 139:177-183 !$#title Structural organization of the gene encoding the human !1lipocalin tear prealbumin and synthesis of the recombinant !1protein in Escherichia coli. !$#cross-references MUID:94156196; PMID:8112601 !$#accession I53728 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-176 ##label RE2 !'##cross-references GB:L14927; NID:g307517; PIDN:AAA18633.1; !1PID:g307518 GENETICS !$#gene GDB:LCN1; TP !'##cross-references GDB:138345; OMIM:151675 !$#map_position 9q34-9q34 !$#introns 30/3; 74/2; 98/1; 135/1; 169/1 CLASSIFICATION #superfamily lipocalin; lipocalin homology KEYWORDS extracellular protein; von Ebner's gland FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$21-176 #product lacrimal lipocalin #status predicted #label !8MAT\ !$26-171 #domain lipocalin homology #label LIP\ !$79-171 #disulfide_bonds #status predicted SUMMARY #length 176 #molecular-weight 19250 #checksum 6917 SEQUENCE /// ENTRY UART #type complete TITLE alpha-2u-globulin precursor - rat ALTERNATE_NAMES fatty acid-binding protein; major urinary protein; MUP ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 23-Oct-1981 #sequence_revision 23-Oct-1981 #text_change 21-Jul-2000 ACCESSIONS A92317; A92354; S05245; A45666; B45666; S03887; B39551; !1I58973; I65318; I65320; I54049; I83302; I52212; S68545; !1A03215; I68182 REFERENCE A92317 !$#authors Drickamer, K.; Kwoh, T.J.; Kurtz, D.T. !$#journal J. Biol. Chem. (1981) 256:3634-3636 !$#title Amino acid sequence of the precursor of rat liver !1alpha-2u-globulin. !$#cross-references MUID:81168119; PMID:6163771 !$#accession A92317 !'##molecule_type mRNA !'##residues 1-65 ##label DRI REFERENCE A92354 !$#authors Dolan, K.P.; Unterman, R.; McLaughlin, M.; Nakhasi, H.L.; !1Lynch, K.R.; Feigelson, P. !$#journal J. Biol. Chem. (1982) 257:13527-13534 !$#title The structure and expression of very closely related members !1of the alpha 2u globulin gene family. !$#cross-references MUID:83056849; PMID:6183262 !$#accession A92354 !'##molecule_type mRNA !'##residues 34-181 ##label DOL REFERENCE S05244 !$#authors Yamamoto, M.; Gao, F.; Furuichi, M.; Ichiyoshi, Y.; Endo, H. !$#journal Biochim. Biophys. Acta (1989) 1008:322-328 !$#title A LINE 1 sequence interrupts the rat alpha2u globulin gene. !$#cross-references MUID:89335733; PMID:2474324 !$#accession S05245 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-8,'S',10-20,'D',22-31,'D',33-131,'A',133-134,'A',136-181 !1##label YAM !'##cross-references EMBL:X14435 !'##experimental_source clone 43 REFERENCE A45666 !$#authors Roy, A.K.; Chatterjee, B.; Rao, K.V.S.; Murty, C.V.R.; !1Sarkar, F.H.; Majumdar, D. !$#journal J. Steroid Biochem. (1987) 27:1129-1134 !$#title Androgenic regulation of hepatic gene expression. !$#cross-references MUID:88092566; PMID:2447393 !$#accession A45666 !'##molecule_type mRNA !'##residues 5-10,'R',12-89,'S',91-116,'YI',119-181 ##label ROY !'##cross-references GB:M27434 !'##experimental_source liver !$#accession B45666 !'##molecule_type mRNA !'##residues 5-10,'R',12-181 ##label RO2 !'##experimental_source liver REFERENCE S03887 !$#authors Kimura, H.; Odani, S.; Suzuki, J.I.; Arakawa, M.; Ono, T. !$#journal FEBS Lett. (1989) 246:101-104 !$#title Kidney fatty acid-binding protein: identification as alpha !1(2U)-globulin. !$#cross-references MUID:89211378; PMID:2468522 !$#accession S03887 !'##molecule_type protein !'##residues 29-48 ##label KIM !'##experimental_source renal REFERENCE A39551 !$#authors Kimura, H.; Odani, S.; Nishi, S.; Sato, H.; Arakawa, M.; !1Ono, T. !$#journal J. Biol. Chem. (1991) 266:5963-5972 !$#title Primary structure and cellular distribution of two fatty !1acid-binding proteins in adult rat kidneys. !$#cross-references MUID:91170283; PMID:2005132 !$#accession B39551 !'##status preliminary !'##molecule_type protein !'##residues 29-179 ##label KI2 REFERENCE A91963 !$#authors Ikehara, Y.; Oda, K.; Rosenfeld, M.G.; Bar-Nun, S.; !1Kreibich, G. !$#journal J. Biochem. (1981) 90:1833-1836 !$#title Precursor of rat liver alpha-2u-globulin: partial amino acid !1sequence determination of its signal peptide. !$#cross-references MUID:82142269; PMID:6174503 !$#contents annotation; signal sequence cleavage site REFERENCE I58973 !$#authors Unterman, R.D.; Lynch, K.R.; Nakhasi, H.L.; Dolan, K.P.; !1Hamilton, J.W.; Cohn, D.V.; Feigelson, P. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:3478-3482 !$#title Cloning and sequence of several alpha-2u-glodulin cDNAs. !$#cross-references MUID:81273082; PMID:6167987 !$#accession I58973 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 5-25,'S',27-181 ##label RES !'##cross-references GB:J00737; NID:g204260; PIDN:AAA41198.1; !1PID:g204261 !'##experimental_source liver !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing REFERENCE I52504 !$#authors Ichiyoshi, Y.; Endo, H.; Yamamoto, M. !$#journal Biochim. Biophys. Acta (1987) 910:43-51 !$#title Length polymorphism in the 3' noncoding region of rat !1hepatic alpha-2u-globulin mRNAs. !$#cross-references MUID:88000701; PMID:2443176 !$#accession I65318 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-181 ##label RE2 !'##cross-references GB:M26837; NID:g202607; PIDN:AAA40641.1; !1PID:g202608 !$#accession I65320 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-181 ##label RE3 !'##cross-references GB:M26835; NID:g202611; PIDN:AAA40643.1; !1PID:g202612 REFERENCE I54049 !$#authors Shaw, P.H.; Walter-Sierra, R.; Tamone, F.; Schibler, U. !$#journal Gene (1989) 84:371-381 !$#title Rapid identification of DNA fragments containing promoters !1for RNA polymerase II. !$#cross-references MUID:90128281; PMID:2558970 !$#accession I54049 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-23 ##label RE4 !'##cross-references GB:M33690; EMBL:X51820; NID:g55541; !1PIDN:CAA36120.1; PID:g55542 REFERENCE I60231 !$#authors Winderickx, J.; van Dijck, P.; Dirckx, L.; Volckaert, G.; !1Rombauts, W.; Heyns, W.; Verhoeven, G. !$#journal Eur. J. Biochem. (1987) 165:521-529 !$#title Comparison of the 5' upstream putative regulatory sequences !1of three members of the alpha 2u-globulin gene family. !$#cross-references MUID:87246634; PMID:2439333 !$#accession I83302 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-70 ##label RE5 !'##cross-references EMBL:X05614; NID:g56249; PIDN:CAA29103.1; !1PID:g56250 REFERENCE I52212 !$#authors Osorio, M.L.; Sinogas, M.; Ludovice, M.; Lechner, M.C. !$#journal Biochem. Biophys. Res. Commun. (1986) 134:1182-1189 !$#title Induction of alpha-2u globulin mRNA by phenobarbital in rat !1liver: characterization of a cDNA clone. !$#cross-references MUID:86130615; PMID:2418834 !$#accession I52212 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 23-57,'K',59-171 ##label REF !'##cross-references GB:M12155; NID:g204263; PIDN:AAA41199.1; !1PID:g204264 REFERENCE S68545 !$#authors Uchida, K.; Fukuda, A.; Kawakishi, S.; Toyokuni, S.; Hiai, !1H.; Ikeda, S.; Horio, F. !$#journal FEBS Lett. (1995) 357:165-167 !$#title Acute nephrotoxicity of a carcinogenic iron chelate. !1Selective inhibition of a proteolytic conversion of alpha !1(2U)-globulin to the kidney fatty acid-binding protein. !$#cross-references MUID:95104464; PMID:7528688 !$#accession S68545 !'##molecule_type protein !'##residues 29-44 ##label UCH COMMENT Alpha-2u-globulin is abundant in the urine of adult male !1rats but absent from that of females. COMMENT Synthesis of this protein in the hepatic parenchymal cells !1is induced in vivo by androgens, glucocorticoids, growth !1hormone, and insulin, and inhibited by estrogens. GENETICS !$#introns 33/3 CLASSIFICATION #superfamily lipocalin; lipocalin homology KEYWORDS glycoprotein; lipid binding; liver; plasma; urine FEATURE !$1-19 #domain signal sequence #status experimental #label !8SIG\ !$20-181 #product alpha-2u-globulin #status experimental !8#label MAT\ !$29-176 #domain lipocalin homology #label LIP\ !$54 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 181 #molecular-weight 20737 #checksum 8409 SEQUENCE /// ENTRY UAMS #type complete TITLE alpha-2u-globulin I precursor - mouse ALTERNATE_NAMES group I major urinary protein; major urinary protein; MUP ORGANISM #formal_name Mus musculus #common_name house mouse DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 22-Jun-1999 ACCESSIONS A03216; B26890; A26890; I55495; I55493; I49097; S07186; !1I57627; I77449; I77450; I59031; S50107 REFERENCE A03216 !$#authors Clark, A.J.; Clissold, P.M.; Al-Shawi, R.; Beattie, P.; !1Bishop, J. !$#journal EMBO J. (1984) 3:1045-1052 !$#title Structure of mouse major urinary protein genes: different !1splicing configurations in the 3'-non-coding region. !$#cross-references MUID:84236099; PMID:6329733 !$#accession A03216 !'##molecule_type DNA !'##residues 1-180 ##label CLA !'##note the authors translated the codons AAC and AAT for residues 55 !1and 173 as Asp and TTA for residue 85 as Tyr REFERENCE A93091 !$#authors Shahan, K.; Gilmartin, M.; Derman, E. !$#journal Mol. Cell. Biol. (1987) 7:1938-1946 !$#title Nucleotide sequences of liver, lachrymal, and submaxillary !1gland mouse major urinary protein mRNAs: mosaic structure !1and construction of panels of gene-specific synthetic !1oligonucleotide probes. !$#cross-references MUID:87257897; PMID:3600652 !$#accession B26890 !'##molecule_type mRNA !'##residues 1-67,'K',69-153,'K',155-180 ##label SHA !'##cross-references GB:M16356; NID:g199880; PIDN:AAA39768.1; !1PID:g199881 !'##experimental_source strain BALB/c, female liver !$#accession A26890 !'##molecule_type mRNA !'##residues 1-157,'K',159-180 ##label SH2 !'##cross-references GB:M16355; NID:g199878; PIDN:AAA39767.1; !1PID:g199879 !'##experimental_source strain BALB/c, male liver REFERENCE I55495 !$#authors Krauter, K.; Leinwand, L.; D'Eustachio, P.; Ruddle, F.; !1Darnell, J.E. !$#journal J. Cell Biol. (1982) 94:414-417 !$#title structural genes of the mouse major urinary protein are on !1chromosome 4. !$#cross-references MUID:82265923; PMID:7107707 !$#accession I55495 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 20-41 ##label RES !'##cross-references GB:J00607; NID:g199860; PIDN:AAA39760.1; !1PID:g199861 REFERENCE I55493 !$#authors Bennett, A.L.; Paulson, K.E.; Miller, R.E.; Darnell, J.E. !$#journal J. Cell Biol. (1987) 105:1073-1085 !$#title Aquisition of antigens characteristic of adult pericentral !1hepatocytes by differentiating fetal hepatoblasts in vitro. !$#cross-references MUID:88007832; PMID:2888770 !$#accession I55493 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 3-43,'F',45-126,'N',128-157,'K',159-180 ##label RE2 !'##cross-references GB:M28649; NID:g199868; PIDN:AAA39764.1; !1PID:g199869 REFERENCE I49097 !$#authors Belgrader, P.; Maquat, L.E. !$#journal Mol. Cell. Biol. (1994) 14:6326-6336 !$#title Nonsense but not missense mutations can decrease the !1abundance of nuclear mRNA for the mouse major urinary !1protein, while both types of mutations can facilitate exon !1skipping. !$#cross-references MUID:94344143; PMID:8065364 !$#accession I49097 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 134-157,'K',159-180 ##label RE3 !'##cross-references EMBL:U12201; NID:g1305451; PIDN:AAA99109.1; !1PID:g520548 REFERENCE S07186 !$#authors Clark, A.J.; Chave-Cox, A.; Ma, X.; Bishop, J.O. !$#journal EMBO J. (1985) 4:3167-3171 !$#title Analysis of mouse major urinary protein genes: variation !1between the exonic sequences of Group 1 genes and a !1comparison with an active gene outwith Group 1 both suggest !1that gene conversion has occurred between MUP genes. !$#cross-references MUID:86135943; PMID:3004936 !$#accession S07186 !'##status translation not shown !'##molecule_type mRNA !'##residues 'R',31-180 ##label CL2 !'##cross-references EMBL:X03524; NID:g53270; PIDN:CAA27227.1; !1PID:g53271 !'##experimental_source clone pMUP11 REFERENCE I57627 !$#authors Held, W.A.; Gallagher, J.F.; Hohman, C.M.; Kuhn, N.J.; !1Sampsell, B.M.; Hughes, R.G. !$#journal Mol. Cell. Biol. (1987) 7:3705-3712 !$#title Identification and characterization of functional genes !1encoding the mouse major urinary proteins. !$#cross-references MUID:88065510; PMID:2824995 !$#accession I57627 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-10 ##label RE4 !'##cross-references GB:M17814; NID:g202299; PIDN:AAA40540.1; !1PID:g202300 !$#accession I77449 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-10 ##label RE5 !'##cross-references GB:M17818; NID:g202305; PIDN:AAA40543.1; !1PID:g202306 !$#accession I77450 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-10 ##label RE6 !'##cross-references GB:M17817; NID:g202307; PIDN:AAA40544.1; !1PID:g202308 REFERENCE I59031 !$#authors Ghazal, P.; Clark, J.A.; Bishop, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:4182-4185 !$#title Evolutionary amplification of a pseudogene. !$#cross-references MUID:85216655; PMID:3858875 !$#accession I59031 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-32 ##label RE8 !'##cross-references GB:M17759; NID:g199866; PIDN:AAA39763.1; !1PID:g199867 REFERENCE S50102 !$#authors Caubin, J.; Iglesias, T.; Bernal, J.; Munoz, A.; Marquez, !1G.; Barbero, J.L.; Zaballos, A. !$#journal Nucleic Acids Res. (1994) 22:4132-4138 !$#title Isolation of genomic DNA fragments corresponding to genes !1modulated in vivo by a transcription factor. !$#cross-references MUID:95023181; PMID:7937138 !$#accession S50107 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 'SXPRSQERXGPDRQTILFPYL',1-32 ##label CAU !'##cross-references EMBL:Z32546 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1March 1994 GENETICS !$#introns 139/1; 173/1 CLASSIFICATION #superfamily lipocalin; lipocalin homology KEYWORDS lipid binding; liver; plasma; urine FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-180 #product alpha-2u-globulin #status predicted #label !8MAT\ !$28-175 #domain lipocalin homology #label LIP SUMMARY #length 180 #molecular-weight 20649 #checksum 6344 SEQUENCE /// ENTRY OVFGP #type complete TITLE olfactory protein precursor - northern leopard frog ORGANISM #formal_name Rana pipiens #common_name northern leopard frog DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 22-Jun-1999 ACCESSIONS A25837 REFERENCE A25837 !$#authors Lee, K.H.; Wells, R.G.; Reed, R.R. !$#journal Science (1987) 235:1053-1056 !$#title Isolation of an olfactory cDNA: similarity to !1retinol-binding protein suggests a role in olfaction. !$#cross-references MUID:87149013; PMID:3493528 !$#accession A25837 !'##molecule_type mRNA !'##residues 1-177 ##label LEE !'##cross-references GB:M15531; NID:g213685; PIDN:AAA49529.1; !1PID:g213686 COMMENT This protein is synthesized in the Bowman's glands, which !1secrete the mucus that bathes the cilia of the olfactory !1neuroepithelium. CLASSIFICATION #superfamily lipocalin; lipocalin homology KEYWORDS Bowman's gland; olfaction FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-177 #product olfactory protein #status predicted #label !8MAT\ !$26-174 #domain lipocalin homology #label LIP SUMMARY #length 177 #molecular-weight 20191 #checksum 8562 SEQUENCE /// ENTRY SQRTAD #type complete TITLE androgen-dependent epididymal 18.5K protein precursor - rat ALTERNATE_NAMES epididymal secretory protein I ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1987 #sequence_revision 08-Feb-1996 #text_change 22-Jun-1999 ACCESSIONS A43801; S19654; A23870; S18742 REFERENCE A43801 !$#authors Moore, A.; Hall, L.; Hamilton, D.W. !$#journal Biol. Reprod. (1990) 43:497-506 !$#title An 18-kDa androgen-regulated protein that modifies !1galactosyltransferase activity is synthesized by the rat !1caput epididymidis, but has no structural similarity to rat !1milk alphalactalbumin. !$#cross-references MUID:91105233; PMID:2125511 !$#accession A43801 !'##molecule_type mRNA !'##residues 1-188 ##label MOO !'##cross-references GB:X59832; NID:g56118; PIDN:CAA42494.1; PID:g56119 REFERENCE S19654 !$#authors Girotti, M.; Jones, R.; Emery, D.C.; Chia, W.; Hall, L. !$#journal Biochem. J. (1992) 281:203-210 !$#title Structure and expression of the rat epididymal secretory !1protein I gene. An androgen-regulated member of the !1lipocalin superfamily with a rare splice donor site. !$#cross-references MUID:92117973; PMID:1731756 !$#accession S19654 !'##status preliminary !'##molecule_type DNA !'##residues 1-188 ##label GIR !'##cross-references EMBL:X59831; NID:g56116; PIDN:CAA42493.1; !1PID:g56117 REFERENCE A23870 !$#authors Brooks, D.E.; Means, A.R.; Wright, E.J.; Singh, S.P.; Tiver, !1K.K. !$#journal J. Biol. Chem. (1986) 261:4956-4961 !$#title Molecular cloning of the cDNA for two major !1androgen-dependent secretory proteins of 18.5 kilodaltons !1synthesized by the rat epididymis. !$#cross-references MUID:86168213; PMID:2420796 !$#accession A23870 !'##molecule_type mRNA !'##residues 5-188 ##label BRO !'##cross-references GB:M12790; NID:g204062; PIDN:AAA41127.1; !1PID:g204063 !'##note amino-terminal sequence of a form designated protein B began at !1residue 23; the form designated protein C could not be !1sequenced and is probably blocked !'##note the sequences of all (six) separate cDNA clones were identical !1and the tryptic peptide maps of the two forms B and C !1"failed to reveal any obvious differences" COMMENT There are two similar, immunologically cross-reacting forms !1of this protein, designated B and C, which probably result !1from different processing of the amino end. COMMENT This protein is synthesized exclusively in the proximal part !1(caput epididymidis) of the epididymis. It makes up a !1substantial part of the total protein in the epididymal !1luminal fluid and binds to the sperm membrane. GENETICS !$#introns 32/3; 78/2; 105/1; 140/1; 174/1; 182/3 CLASSIFICATION #superfamily lipocalin; lipocalin homology KEYWORDS epididymis; sperm FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-188 #product androgen-dependent epididymal 18.5K protein !8#status predicted #label MPT\ !$28-176 #domain lipocalin homology #label LIP SUMMARY #length 188 #molecular-weight 20670 #checksum 6469 SEQUENCE /// ENTRY C8HUG #type complete TITLE complement C8 gamma chain precursor [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 28-Dec-1987 #sequence_revision 27-Jun-1994 #text_change 17-Nov-2000 ACCESSIONS A27487; A29772; A54254 REFERENCE A27487 !$#authors Haefliger, J.A.; Jenne, D.; Stanley, K.K.; Tschopp, J. !$#journal Biochem. Biophys. Res. Commun. (1987) 149:750-754 !$#title Structural homology of human complement component C8-gamma !1and plasma protein HC: identity of the cysteine bond !1pattern. !$#cross-references MUID:88106501; PMID:2447883 !$#contents sequence and disulfide bonds !$#accession A27487 !'##molecule_type mRNA !'##residues 1-202 ##label HAE !'##cross-references GB:X06465; NID:g29576; PIDN:CAA29773.1; PID:g29577 REFERENCE A29772 !$#authors Ng, S.C.; Rao, A.G.; Howard, O.M.Z.; Sodetz, J.M. !$#journal Biochemistry (1987) 26:5229-5233 !$#title The eighth component of human complement: evidence that it !1is an oligomeric serum protein assembled from products of !1three different genes. !$#cross-references MUID:88050795; PMID:3676249 !$#accession A29772 !'##molecule_type mRNA !'##residues 1-44,'H',46-202 ##label NGS !'##note part of the sequence was confirmed by protein sequencing !'##note the authors translated the codon CAT for residue 45 as Gln REFERENCE A54254 !$#authors Kaufman, K.M.; Sodetz, J.M. !$#journal Biochemistry (1994) 33:5162-5166 !$#title Genomic structure of the human complement protein C8gamma: !1homology to the lipocalin gene family. !$#cross-references MUID:94227046; PMID:8172891 !$#accession A54254 !'##molecule_type DNA !'##residues 1-198,'G',200-202 ##label KAU !'##cross-references GB:U08198 !'##note authors translated the codon GAA for residue 199 as Gly GENETICS !$#gene GDB:C8G !'##cross-references GDB:119737; OMIM:120930 !$#map_position 9q22.3-9q32 !$#introns 46/3; 92/2; 116/1; 152/1; 186/1; 199/1 COMPLEX heterotrimer of C8 alpha chain (PIR:C8HUA), C8 beta chain !1(PIR:C8HUB), and C8 gamma chain (PIR:C8HUG); the trimer !1associates with the C5b-7 complex FUNCTION !$#description combines with complement C5b-7 complex to polymerize !1complement component C9 !$#pathway complement pathway CLASSIFICATION #superfamily lipocalin; lipocalin homology KEYWORDS membrane attack complex; plasma FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-202 #product complement C8 gamma chain #status predicted !8#label MAT\ !$42-188 #domain lipocalin homology #label LIP\ !$60 #disulfide_bonds interchain (to alpha chain) #status !8experimental\ !$96-188 #disulfide_bonds #status experimental SUMMARY #length 202 #molecular-weight 22219 #checksum 8853 SEQUENCE /// ENTRY LGBO #type complete TITLE beta-lactoglobulin precursor [validated] - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 24-Apr-1984 #sequence_revision 05-Apr-1995 #text_change 15-Sep-2000 ACCESSIONS S10179; S05505; A27359; S02483; A91659; B91659; A91682; !1A91393; A94567; D60808; S09001; A03218; A26193; S14721 REFERENCE S10179 !$#authors Silva, M.C.; Wong, D.W.S.; Batt, C.A. !$#journal Nucleic Acids Res. (1990) 18:3051 !$#title Cloning and partial nucleotide sequence of the genomic !1bovine beta-lactoglobulin gene. !$#cross-references MUID:90272417; PMID:2349102 !$#accession S10179 !'##molecule_type DNA !'##residues 1-20 ##label SIL !'##cross-references EMBL:X52581; NID:g125; PIDN:CAA36812.1; PID:g126 REFERENCE S05505 !$#authors Alexander, L.J.; Hayes, G.; Pearse, M.J.; Beattie, C.W.; !1Stewart, A.F.; Willis, I.M.; Mackinlay, A.G. !$#journal Nucleic Acids Res. (1989) 17:6739 !$#title Complete sequence of the bovine beta-lactoglobulin cDNA. !$#cross-references MUID:89386012; PMID:2701948 !$#contents variant A !$#accession S05505 !'##molecule_type mRNA !'##residues 1-79,'D',81-120,'V',122-133,'V',135-178 ##label AL2 !'##cross-references EMBL:X14712; NID:g519; PIDN:CAA32835.1; PID:g520 REFERENCE A27359 !$#authors Jamieson, A.C.; Vandeyar, M.A.; Kang, Y.C.; Kinsella, J.E.; !1Batt, C.A. !$#journal Gene (1987) 61:85-90 !$#title Cloning and nucleotide sequence of the bovine !1beta-lactoglobulin gene. !$#cross-references MUID:88167846; PMID:3443305 !$#contents variant A !$#accession A27359 !'##molecule_type mRNA !'##residues 28-79,'D',81-133,'V',135-178 ##label JAM !'##cross-references GB:M19088; NID:g162747; PIDN:AAA30411.1; !1PID:g162748 !'##experimental_source mammary gland REFERENCE S02483 !$#authors Ivanov, V.N.; Judinkova, E.S.; Gorodetsky, S.I. !$#journal Biol. Chem. Hoppe-Seyler (1988) 369:425-429 !$#title Molecular cloning of bovine beta-lactoglobulin cDNA. !$#cross-references MUID:89076475; PMID:3202951 !$#accession S02483 !'##molecule_type mRNA !'##residues 122-178 ##label IVA !'##cross-references GB:M27732; NID:g530872; PIDN:AAA30412.1; !1PID:g530873 !'##experimental_source mammary gland REFERENCE A91659 !$#authors Braunitzer, G.; Chen, R.; Schrank, B.; Stangl, A. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1973) 354:867-878 !$#title Die Sequenzanalyse des beta-Lactoglobulins. !$#cross-references MUID:75059155; PMID:4611888 !$#accession A91659 !'##molecule_type protein !'##residues 17-79,'D',81-99,'L',101-102,'I',104-133,'V',135-170,'LQ', !1173-178 ##label BRA !'##experimental_source variant A !$#accession B91659 !'##molecule_type protein !'##residues 17-99,'L',101-102,'I',104-170,'LQ',173-178 ##label BR2 !'##experimental_source variant B REFERENCE A91682 !$#authors Preaux, G.; Braunitzer, G.; Schrank, B.; Stangl, A. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1979) 360:1595-1604 !$#title The amino acid sequence of goat beta-lactoglobulin. !$#cross-references MUID:80070611; PMID:511095 !$#contents revisions to residues 100, 103, 171, and 172 !$#accession A91682 !'##molecule_type protein !'##residues 17-178 ##label PRE REFERENCE A91393 !$#authors Brignon, G.; Ribadeau-Dumas, B. !$#journal FEBS Lett. (1973) 33:73-76 !$#title Localisation dans la chaine peptidique de la beta !1lactoglobuline bovine de la substitution Glu/Gln !1differenciant les variants genetiques B et D. !$#cross-references MUID:73229270; PMID:4737332 !$#accession A91393 !'##molecule_type protein !'##residues 59-60,'Q',62-73 ##label BRI !'##experimental_source variant D REFERENCE A94567 !$#authors Shaw, D.C. !$#submission submitted to the Atlas, January 1973 !$#accession A94567 !'##molecule_type protein !'##residues 17-74,'H',76-178 ##label SHA !'##experimental_source variant C, Jersey breed REFERENCE A60808 !$#authors Hsieh, J.C.; Lin, F.P.; Tam, M.F. !$#journal Anal. Biochem. (1988) 170:1-8 !$#title Electroblotting onto glass-fiber filter from an analytical !1isoelectrofocusing gel: a preparative method for isolating !1proteins for N-terminal microsequencing. !$#cross-references MUID:88267456; PMID:3389500 !$#accession D60808 !'##molecule_type protein !'##residues 17-34,'X',36 ##label HSI REFERENCE S09001 !$#authors Godovac-Zimmermann, J.; Krause, I.; Buchberger, J.; Weiss, !1G.; Klostermeyer, H. !$#journal Biol. Chem. Hoppe-Seyler (1990) 371:255-260 !$#title Genetic variants of bovine beta-lactoglobulin. A novel !1wild-type beta-lactoglobulin W and its primary sequence. !$#cross-references MUID:90253648; PMID:2340107 !$#contents variant W !$#accession S09001 !'##molecule_type protein !'##residues 17-71,'L',73-178 ##label GOD !'##experimental_source Murnau-Werdenfelser breed REFERENCE A90364 !$#authors McKenzie, H.A.; Ralston, G.B.; Shaw, D.C. !$#journal Biochemistry (1972) 11:4539-4547 !$#title Location of sulfhydryl and disulfide groups in bovine !1beta-lactoglobulins and effects of urea. !$#cross-references MUID:73123377; PMID:4569282 !$#contents annotation; disulfide bonds REFERENCE A65151 !$#authors Brownlow, S.; Morais-cabral, J.H.; Sawyer, L. !$#submission submitted to the Brookhaven Protein Data Bank, December 1996 !$#cross-references PDB:1BEB !$#contents annotation; X-ray crystallography, 1.8 angstroms, residues !121-113,'V',115-176 REFERENCE A92856 !$#authors Green, D.W.; Aschaffenburg, R.; Camerman, A.; Coppola, J.C.; !1Dunnill, P.; Simmons, R.M.; Komorowski, E.S.; Sawyer, L.; !1Turner, E.M.C.; Woods, K.F. !$#journal J. Mol. Biol. (1979) 131:375-397 !$#title Structure of bovine beta-lactoglobulin at 6 angstrom !1resolution. !$#cross-references MUID:80029719; PMID:40037 !$#contents annotation; X-ray crystallography, 6 angstroms REFERENCE A93385 !$#authors Papiz, M.Z.; Sawyer, L.; Eliopoulos, E.E.; North, A.C.T.; !1Findlay, J.B.C.; Sivaprasadarao, R.; Jones, T.A.; Newcomer, !1M.E.; Kraulis, P.J. !$#journal Nature (1986) 324:383-385 !$#title The structure of beta-lactoglobulin and its similarity to !1plasma retinol-binding protein. !$#cross-references MUID:87065093; PMID:3785406 !$#contents annotation; X-ray crystallography, 2.8 angstroms; disulfide !1bonds COMMENT The sequence of variant B is shown. COMMENT Under physiological conditions beta-lactoglobulin exists as !1an equilibrium mixture of monomeric and dimeric forms. The !1monomeric molecule, similar to that of plasma !1retinol-binding protein (see PIR:VAHU) has a beta-sheet core !1and an alpha-helix; the core forms a hydrophobic pocket, !1which can bind retinol. COMMENT Beta-lactoglobulin is a major component of whey in ruminants !1and some other mammals. CLASSIFICATION #superfamily lipocalin; lipocalin homology KEYWORDS homodimer; mammary gland; milk; polymorphism FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-178 #product beta-lactoglobulin #status predicted #label !8MAT\ !$26-176 #domain lipocalin homology #label LIP\ !$82-176,122-135 #disulfide_bonds #status experimental SUMMARY #length 178 #molecular-weight 19883 #checksum 5237 SEQUENCE /// ENTRY LGBUI #type complete TITLE beta-lactoglobulin - water buffalo ORGANISM #formal_name Bubalus arnee #common_name water buffalo DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 08-May-1998 ACCESSIONS A03219; B12267 REFERENCE A03219 !$#authors Kolde, H.J.; Liberatori, J.; Braunitzer, G. !$#journal Milchwissenschaft (1981) 36:83-86 !$#title The amino acid sequence of the water buffalo !1beta-lactoglobulin. !$#accession A03219 !'##molecule_type protein !'##residues 1-162 ##label KOL REFERENCE A91428 !$#authors Addeo, F.; Mercier, J.C.; Ribadeau Dumas, B. !$#journal FEBS Lett. (1976) 63:255-259 !$#title Elements de structure primaire de l'alpha-lactalbumine et de !1la beta-lactoglobuline de buffle. !$#cross-references MUID:76165595; PMID:1261697 !$#accession B12267 !'##molecule_type protein !'##residues 1-4;7-10,'N',12-19,'Q';161-162 ##label ADD COMMENT Under physiological conditions beta-lactoglobulin exists as !1an equilibrium mixture of monomeric and dimeric forms. The !1monomeric molecule, similar to that of plasma !1retinol-binding protein (see PIR:VAHU) has a beta-sheet core !1and an alpha-helix; the core forms a hydrophobic pocket, !1which can bind retinol. CLASSIFICATION #superfamily lipocalin; lipocalin homology KEYWORDS homodimer; mammary gland; milk FEATURE !$10-160 #domain lipocalin homology #label LIP\ !$66-160,106-119 #disulfide_bonds #status predicted SUMMARY #length 162 #molecular-weight 18267 #checksum 7550 SEQUENCE /// ENTRY LGGT #type complete TITLE beta-lactoglobulin precursor - goat ORGANISM #formal_name Capra aegagrus hircus #common_name domestic goat DATE 17-May-1985 #sequence_revision 12-Apr-1996 #text_change 22-Jun-1999 ACCESSIONS A03220; S14507; S42800; S42801 REFERENCE A91682 !$#authors Preaux, G.; Braunitzer, G.; Schrank, B.; Stangl, A. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1979) 360:1595-1604 !$#title The amino acid sequence of goat beta-lactoglobulin. !$#cross-references MUID:80070611; PMID:511095 !$#accession A03220 !'##molecule_type protein !'##residues 19-180 ##label PRE REFERENCE S14507 !$#authors Folch, J.M.; Coll, A.; Sanchez, A. !$#submission submitted to the EMBL Data Library, March 1991 !$#accession S14507 !'##molecule_type mRNA !'##residues 1-180 ##label FOL !'##cross-references EMBL:X58471; NID:g967; PIDN:CAA41385.1; PID:g968 REFERENCE S42800 !$#authors Kim, J. !$#submission submitted to the EMBL Data Library, January 1993 !$#accession S42800 !'##molecule_type mRNA !'##residues 1-180 ##label KIM !'##cross-references EMBL:Z19569; NID:g437751; PIDN:CAA79623.1; !1PID:g437752 !$#accession S42801 !'##molecule_type mRNA !'##residues 1-32 ##label KI2 !'##cross-references EMBL:Z19570; NID:g437753; PIDN:CAA79624.1; !1PID:g437754 COMMENT Under physiological conditions beta-lactoglobulin exists as !1an equilibrium mixture of monomeric and dimeric forms. CLASSIFICATION #superfamily lipocalin; lipocalin homology KEYWORDS milk FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-180 #product beta-lactoglobulin #status predicted #label !8MAT\ !$28-178 #domain lipocalin homology #label LIP\ !$84-178,124-137 #disulfide_bonds #status predicted SUMMARY #length 180 #molecular-weight 19975 #checksum 3894 SEQUENCE /// ENTRY LGSH #type complete TITLE beta-lactoglobulin precursor - sheep ALTERNATE_NAMES beta-lactoglobulin A; beta-lactoglobulin B; beta-lactoglobulin C; beta-lactoglobulin I; beta-lactoglobulin II ORGANISM #formal_name Ovis orientalis aries, Ovis ammon aries #common_name domestic sheep DATE 17-May-1985 #sequence_revision 19-Apr-1996 #text_change 22-Jun-1999 ACCESSIONS JQ0749; JQ0748; A30011; B30011; S02136; A25136; A03221; !1S04955 REFERENCE JQ0748 !$#authors Ali, S.; McClenaghan, M.; Simons, J.P.; Clark, A.J. !$#journal Gene (1990) 91:201-207 !$#title Characterisation of the alleles encoding ovine !1beta-lactoglobulins A and B. !$#cross-references MUID:91007276; PMID:1976573 !$#accession JQ0749 !'##molecule_type DNA !'##residues 1-180 ##label ALIB !'##cross-references GB:M32232 !'##experimental_source beta-lactoglobulin B !$#accession JQ0748 !'##molecule_type DNA !'##residues 1-37,'Y',39-180 ##label ALIA !'##cross-references GB:M32232 !'##experimental_source beta-lactoglobulin A REFERENCE A92942 !$#authors Ali, S.; Clark, A.J. !$#journal J. Mol. Biol. (1988) 199:415-426 !$#title Characterization of the gene encoding ovine !1beta-lactoglobulin. Similarity to the genes for retinol !1binding protein and other secretory proteins. !$#cross-references MUID:88172489; PMID:3351935 !$#accession A30011 !'##molecule_type DNA !'##residues 1-180 ##label ALI1 !'##cross-references GB:X14971 !'##experimental_source beta-lactoglobulin I !$#accession B30011 !'##molecule_type DNA !'##residues 1-37,'Y',39-102,'N',104-180 ##label ALI2 !'##cross-references GB:X07009 !'##experimental_source beta-lactoglobulin II REFERENCE S02136 !$#authors Harris, S.; Ali, S.; Anderson, S.; Archibald, A.L.; Clark, !1A.J. !$#journal Nucleic Acids Res. (1988) 16:10379-10380 !$#title Complete nucleotide sequence of the genomic ovine !1beta-lactoglobulin gene. !$#cross-references MUID:89057492; PMID:3194215 !$#accession S02136 !'##status translation not shown !'##molecule_type DNA !'##residues 1-180 ##label HAR !'##cross-references EMBL:X12817; NID:g1313; PIDN:CAA31305.1; PID:g1314 REFERENCE A25136 !$#authors Gaye, P.; Hue-Delahaie, D.; Mercier, J.C.; Soulier, S.; !1Vilotte, J.L.; Furet, J.P. !$#journal Biochimie (1986) 68:1097-1107 !$#title Ovine beta-lactoglobulin messenger RNA: nucleotide sequence !1and mRNA levels during functional differentiation of the !1mammary gland. !$#cross-references MUID:87049827; PMID:3096387 !$#accession A25136 !'##molecule_type mRNA !'##residues 1-180 ##label GAY !'##cross-references GB:X04520; NID:g1315; PIDN:CAA28204.1; PID:g1316 REFERENCE A03221 !$#authors Preaux, G.; Braunitzer, G.; Kolde, H.J. !$#journal Arch. Int. Physiol. Biochim. (1980) 88:B45-B46 !$#title Primary structure of ovine beta-lactoglobulin. !$#cross-references MUID:80219294; PMID:6155855 !$#accession A03221 !'##molecule_type protein !'##residues 19-37,'Y',39-180 ##label PRE REFERENCE S04955 !$#authors Erhardt, G.; Godovac-Zimmermann, J.; Conti, A. !$#journal Biol. Chem. Hoppe-Seyler (1989) 370:757-762 !$#title Isolation and complete primary sequence of a new ovine !1wild-type beta-lactoglobulin C. !$#cross-references MUID:89374823; PMID:2775495 !$#accession S04955 !'##molecule_type protein !'##residues 19-37,'Y',39-165,'Q',167-180 ##label ERH !'##experimental_source beta-lactoglobulin C COMMENT This protein is the major milk whey protein of ruminants and !1is produced in the mammary gland during pregnancy and !1lactation. COMMENT Under physiological conditions beta-lactoglobulin exists as !1an equilibrium mixture of monomeric and dimeric forms. GENETICS !$#gene BLG !$#introns 32/3; 79/2; 104/1; 141/1; 176/1 CLASSIFICATION #superfamily lipocalin; lipocalin homology KEYWORDS milk; polymorphism FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-180 #product beta-lactoglobulin #status experimental !8#label MAT\ !$28-178 #domain lipocalin homology #label LIP\ !$84-178,124-137 #disulfide_bonds #status predicted SUMMARY #length 180 #molecular-weight 19921 #checksum 3558 SEQUENCE /// ENTRY LGHO #type complete TITLE beta-lactoglobulin I - horse ORGANISM #formal_name Equus caballus #common_name domestic horse DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 06-Dec-1996 ACCESSIONS A03222 REFERENCE A03222 !$#authors Conti, A.; Godovac-Zimmermann, J.; Liberatori, J.; !1Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1984) 365:1393-1399 !$#title The primary structure of monomeric beta-lactoglobulin I from !1horse colostrum (Equus caballus, Perissodactyla). !$#cross-references MUID:85128970; PMID:6526379 !$#accession A03222 !'##molecule_type protein !'##residues 1-162 ##label CON COMMENT This protein is a monomer. CLASSIFICATION #superfamily lipocalin; lipocalin homology KEYWORDS colostrum; milk FEATURE !$10-160 #domain lipocalin homology #label LIP\ !$66-160,106-119 #disulfide_bonds #status predicted SUMMARY #length 162 #molecular-weight 18540 #checksum 8989 SEQUENCE /// ENTRY LGHOD #type complete TITLE beta-lactoglobulin I - donkey ORGANISM #formal_name Equus asinus #common_name donkey DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 06-Dec-1996 ACCESSIONS S00372 REFERENCE S00372 !$#authors Godovac-Zimmermann, J.; Conti, A.; James, L.; Napolitano, L. !$#journal Biol. Chem. Hoppe-Seyler (1988) 369:171-179 !$#title Microanalysis of the amino-acid sequence of monomeric !1beta-lactoglobulin I from donkey (Equus asinus) milk. The !1primary structure and its homology with a superfamily of !1hydrophobic molecule transporters. !$#cross-references MUID:88221842; PMID:3370127 !$#accession S00372 !'##molecule_type protein !'##residues 1-162 ##label GOD COMMENT This is a monomeric beta-lactoglobulin. CLASSIFICATION #superfamily lipocalin; lipocalin homology KEYWORDS colostrum; milk; retinol binding FEATURE !$10-160 #domain lipocalin homology #label LIP\ !$66-160,106-119 #disulfide_bonds #status predicted SUMMARY #length 162 #molecular-weight 18528 #checksum 8229 SEQUENCE /// ENTRY LGHO2 #type complete TITLE beta-lactoglobulin II - horse ORGANISM #formal_name Equus caballus #common_name domestic horse DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 08-May-1998 ACCESSIONS A24654 REFERENCE A24654 !$#authors Godovac-Zimmermann, J.; Conti, A.; Liberatori, J.; !1Braunitzer, G. !$#journal Biol. Chem. Hoppe-Seyler (1985) 366:601-608 !$#title The amino-acid sequence of beta-lactoglobulin II from horse !1colostrum (Equus caballus, Perissodactyla): !1beta-lactoglobulins are retinol-binding proteins. !$#cross-references MUID:85279907; PMID:4040766 !$#accession A24654 !'##molecule_type protein !'##residues 1-166 ##label GOD COMMENT The equine beta-lactoglobulins are monomeric. COMMENT Under physiological conditions beta-lactoglobulin exists as !1an equilibrium mixture of monomeric and dimeric forms. The !1monomeric molecule, similar to that of plasma !1retinol-binding protein (see PIR:VAHU) has a beta-sheet core !1and an alpha-helix; the core forms a hydrophobic pocket that !1can bind retinol. CLASSIFICATION #superfamily lipocalin; lipocalin homology KEYWORDS mammary gland; milk FEATURE !$10-164 #domain lipocalin homology #label LIP SUMMARY #length 166 #molecular-weight 18580 #checksum 6590 SEQUENCE /// ENTRY A39167 #type complete TITLE placental protein 14 precursor [validated] - human ALTERNATE_NAMES alpha uterine protein (AUP); chorionic alpha2-microglobulin (CAG-2); endometrial protein 14; placenta-specific alpha2-microglobulin (PAMG-2); PP14; pregnancy-associated endometrial alpha2-globulin (alpha2-PEG), long splice form; progestagen-associated endometrial protein (PEP); protein DKFZp586D0922.1 CONTAINS alpha2-PEG, medium splice form; alpha2-PEG, short splice form ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Jan-1992 #sequence_revision 19-Apr-1996 #text_change 08-Dec-2000 ACCESSIONS A35570; A39167; B39167; C39167; A31242; A29773; A60874; !1A61064; S07444; T08791 REFERENCE A35570 !$#authors Vaisse, C.; Atger, M.; Potier, B.; Milgrom, E. !$#journal DNA Cell Biol. (1990) 9:401-413 !$#title Human placental protein 14 gene: sequence and !1characterization of a short duplication. !$#cross-references MUID:91000355; PMID:2206398 !$#accession A35570 !'##molecule_type DNA !'##residues 1-180 ##label VAI !'##cross-references GB:M34046; NID:g190216; PIDN:AAA60148.1; !1PID:g190217 REFERENCE A39167 !$#authors Garde, J.; Bell, S.C.; Eperon, I.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:2456-2460 !$#title Multiple forms of mRNA encoding human pregnancy-associated !1endometrial alpha-2-globulin, a beta-lactoglobulin !1homologue. !$#cross-references MUID:91172827; PMID:2006183 !$#accession A39167 !'##molecule_type mRNA !'##residues 1-180 ##label GAR1 !'##cross-references GB:M61886; NID:g182092; PIDN:AAA35801.1; !1PID:g182094 !$#accession B39167 !'##molecule_type mRNA !'##residues 1-32,55-180 ##label GAR2 !'##cross-references GB:M61886; NID:g182092; PIDN:AAA35802.1; !1PID:g182093 !$#accession C39167 !'##molecule_type mRNA !'##residues 1-32,127-180 ##label GAR3 !'##cross-references GB:M61886 REFERENCE A31242 !$#authors Julkunen, M.; Seppaelae, M.; Jaenne, O.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:8845-8849 !$#title Complete amino acid sequence of human placental protein 14: !1a progesterone-regulated uterine protein homologous to !1beta-lactoglobulins. !$#cross-references MUID:89057835; PMID:3194393 !$#accession A31242 !'##molecule_type mRNA !'##residues 1-94,'G',96-180 ##label JUL !'##cross-references GB:J04129; NID:g190214; PIDN:AAA60147.1; !1PID:g190215 !'##note the translated sequence in GenBank entry HUMPP14A, release !1111.0, (PID:g190215) differs from the published sequence in !1beginning with Met-19 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE A29773 !$#authors Huhtala, M.L.; Seppala, M.; Narvanen, A.; Palomaki, P.; !1Julkunen, M.; Bohn, H. !$#journal Endocrinology (1987) 120:2620-2622 !$#title Amino acid sequence homology between human placental protein !114 and beta-lactoglobulins from various species. !$#cross-references MUID:87190171; PMID:3569148 !$#accession A29773 !'##molecule_type protein !'##residues 19-40 ##label HUH !'##experimental_source placenta REFERENCE A60874 !$#authors Westwood, O.M.R.; Chapman, M.G.; Totty, N.; Philip, R.; !1Bolton, A.E.; Lazarus, N.R. !$#journal J. Reprod. Fertil. (1988) 82:493-500 !$#title N-terminal sequence analysis of human placental protein 14, !1purified in high yield from decidual cytosol. !$#cross-references MUID:88200074; PMID:3361484 !$#accession A60874 !'##molecule_type protein !'##residues 19-36,'E',38,'E',40-42 ##label WES !'##experimental_source decidual endometrium REFERENCE A61064 !$#authors Riittinen, L.; Julkunen, M.; Seppaelae, M.; Koistinen, R.; !1Huhtala, M.L. !$#journal Clin. Chim. Acta (1989) 184:19-30 !$#title Purification and characterization of endometrial protein !1PP14 from mid-trimester amniotic fluid. !$#cross-references MUID:90091009; PMID:2688994 !$#accession A61064 !'##molecule_type protein !'##residues 19-41 ##label RII REFERENCE S07444 !$#authors Bell, S.C.; Keyte, J.W.; Waites, G.T. !$#journal J. Clin. Endocrinol. Metab. (1987) 65:1067-1071 !$#title Pregnancy-associated endometrial alpha(2)-globulin, the !1major secretory protein of the luteal phase and first !1trimester pregnancy endometrium, is not glycosylated !1prolactin but related to beta-lactoglobulins. !$#cross-references MUID:88033578; PMID:3667877 !$#accession S07444 !'##molecule_type protein !'##residues 19-35,'K',37-45,'X',47-56 ##label BEL REFERENCE Z16473 !$#authors Koehrer, K.; Beyer, A.; Mewes, H.W.; Gassenhuber, J.; !1Wiemann, S. !$#submission submitted to the Protein Sequence Database, March 1999 !$#accession T08791 !'##molecule_type mRNA !'##residues 'SEPPTAAA',1-180 ##label KOE !'##cross-references EMBL:AL050169 !'##experimental_source adult uterus; clone DKFZp586D0922 COMMENT Placental protein 14, the major secretory protein in the !1endometrium during the mid- to late luteal phase of !1menstruation and the first trimester of pregnancy, is !1secreted by the glandular surface epithelium of the !1endometrium. It may have immunosuppressive activity during !1implantation and early placentation. GENETICS !$#gene GDB:PAEP; DKFZp586D0922.1 !'##cross-references GDB:127516; OMIM:173310 !$#map_position 9q34.2-9q34.3 !$#introns 32/3; 79/2; 104/1; 140/1; 176/1 COMPLEX homodimer CLASSIFICATION #superfamily lipocalin; lipocalin homology KEYWORDS alternative splicing; glycoprotein; homodimer; uterus FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-180 #product placental protein 14 #status experimental !8#label MAT\ !$19-32,55-180 #product alpha2-PEG, medium splice form #status !8predicted #label MA2\ !$19-32,127-180 #product alpha2-PEG, short splice form #status !8predicted #label MA3\ !$28-178 #domain lipocalin homology #label LIP\ !$46 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$81,103 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$84-178,124-137 #disulfide_bonds #status predicted SUMMARY #length 180 #molecular-weight 20624 #checksum 556 SEQUENCE /// ENTRY VAHU #type complete TITLE plasma retinol-binding protein precursor [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Nov-1979 #sequence_revision 28-Aug-1985 #text_change 08-Dec-2000 ACCESSIONS A93494; A91011; S06278; A91270; A27786; A03223 REFERENCE A93494 !$#authors Colantuoni, V.; Romano, V.; Bensi, G.; Santoro, C.; !1Costanzo, F.; Raugei, G.; Cortese, R. !$#journal Nucleic Acids Res. (1983) 11:7769-7776 !$#title Cloning and sequencing of a full length cDNA coding for !1human retinol-binding protein. !$#cross-references MUID:84069802; PMID:6316270 !$#accession A93494 !'##molecule_type mRNA !'##residues 1-199 ##label COL !'##cross-references EMBL:X00129; NID:g35896; PIDN:CAA24959.1; !1PID:g35897 REFERENCE A91011 !$#authors D'Onofrio, C.; Colantuoni, V.; Cortese, R. !$#journal EMBO J. (1985) 4:1981-1989 !$#title Structure and cell-specific expression of a cloned human !1retinol binding protein gene: the 5'-flanking region !1contains hepatoma specific transcriptional signals. !$#cross-references MUID:86055755; PMID:2998779 !$#accession A91011 !'##molecule_type DNA !'##residues 1-187 ##label DON !'##cross-references EMBL:X02775 REFERENCE S06278 !$#authors Rask, L.; Anundi, H.; Fohlman, J.; Peterson, P.A. !$#journal Ups. J. Med. Sci. (1987) 92:115-146 !$#title The complete amino acid sequence of human serum !1retinol-binding protein. !$#cross-references MUID:88019004; PMID:2444024 !$#accession S06278 !'##molecule_type protein !'##residues 17-198 ##label RA2 REFERENCE A91270 !$#authors Rask, L.; Anundi, H.; Peterson, P.A. !$#journal FEBS Lett. (1979) 104:55-58 !$#title The primary structure of the human retinol-binding protein. !$#cross-references MUID:80004132; PMID:573217 !$#accession A91270 !'##molecule_type protein !'##residues 17-162,'Q',164-181 ##label RAS REFERENCE A90985 !$#authors Newcomer, M.E.; Jones, T.A.; Aqvist, J.; Sundelin, J.; !1Eriksson, U.; Rask, L.; Peterson, P.A. !$#journal EMBO J. (1984) 3:1451-1454 !$#title The three-dimensional structure of retinol-binding protein. !$#cross-references MUID:84261439; PMID:6540172 !$#contents annotation; X-ray crystallography, 3.1 angstroms, and !1disulfide bonds REFERENCE A27786 !$#authors Rask, L.; Anundi, H.; Bohme, J.; Eriksson, U.; Ronne, H.; !1Sege, K.; Peterson, P.A. !$#journal Ann. N. Y. Acad. Sci. (1981) 359:79-90 !$#title Structural and functional studies of vitamin A-binding !1proteins. !$#cross-references MUID:81254137; PMID:6942701 !$#accession A27786 !'##molecule_type protein !'##residues 17-162,'Q',164-198 ##label RA3 COMMENT The pRBP molecule consists of an amino-terminal coil, a !1beta-sheet core composed of eight antiparallel strands, an !1alpha-helix, and a carboxyl-terminal coil. The core forms a !1hydrophobic pocket that completely encloses the retinol !1molecule, which is buried with the beta-ionone ring lying !1deepest and the isoprene tail stretching out almost to the !1surface of the molecule. COMMENT The pRBP transports retinol (the alcohol form of vitamin A) !1from the liver to the peripheral tissues. In plasma, the !1pRBP binds to transthyretin (prealbumin) in a 1:1 molar !1ratio, which prevents its loss via the kidney. The pRBP !1binds to the receptors of target cells, releases retinol, !1and loses its affinity for transthyretin. COMMENT The pRBP precursor is synthesized in the hepatocytes, where, !1after cleavage of the signal sequence, the apoprotein is !1saturated with retinol. GENETICS !$#gene GDB:RBP4 !'##cross-references GDB:120342; OMIM:180250 !$#map_position 10q23-10q24 !$#introns 35/3; 81/2; 117/1 CLASSIFICATION #superfamily lipocalin; lipocalin homology KEYWORDS extracellular protein; liver; plasma; retinol binding; !1vitamin A; vitamin carrier FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-198 #product plasma retinol-binding protein #status !8experimental #label MAT\ !$31-190 #domain lipocalin homology #label LIP\ !$20-176,86-190, !$136-145 #disulfide_bonds #status experimental SUMMARY #length 199 #molecular-weight 22868 #checksum 8315 SEQUENCE /// ENTRY VARB #type complete TITLE retinol-binding protein precursor - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 30-Sep-1987 #sequence_revision 01-Mar-1996 #text_change 22-Jun-1999 ACCESSIONS A49178; A22620 REFERENCE A49178 !$#authors Lee, S.Y.; Ubels, J.L.; Soprano, D.R. !$#journal Exp. Eye Res. (1992) 55:163-171 !$#title The lacrimal gland synthesizes retinol-binding protein. !$#cross-references MUID:93011736; PMID:1339354 !$#accession A49178 !'##molecule_type mRNA !'##residues 1-201 ##label LEE !'##cross-references GB:S45958; NID:g257202; PIDN:AAB23582.1; !1PID:g257203 !'##experimental_source liver !'##note sequence extracted from NCBI backbone (NCBIN:115099, !1NCBIP:115101) REFERENCE A92525 !$#authors Sundelin, J.; Laurent, B.C.; Anundi, H.; Tragardh, L.; !1Larhammar, D.; Bjorck, L.; Eriksson, U.; Akerstrom, B.; !1Jones, A.; Newcomer, M.; Peterson, P.A.; Rask, L. !$#journal J. Biol. Chem. (1985) 260:6472-6480 !$#title Amino acid sequence homologies between rabbit, rat, and !1human serum retinol-binding proteins. !$#cross-references MUID:85207643; PMID:3838985 !$#accession A22620 !'##molecule_type protein !'##residues 19-200 ##label SUN COMMENT For general comments see the entry for the human protein !1(PIR:VAHU). CLASSIFICATION #superfamily lipocalin; lipocalin homology KEYWORDS liver; plasma; retinol binding; vitamin A FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-201 #product retinol-binding protein #status experimental !8#label MAT\ !$33-192 #domain lipocalin homology #label LIP\ !$22-178,88-192, !$138-147 #disulfide_bonds #status predicted SUMMARY #length 201 #molecular-weight 23102 #checksum 2179 SEQUENCE /// ENTRY VART #type complete TITLE plasma retinol-binding protein precursor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 22-Jun-1999 ACCESSIONS A92493; A92525; B92525; A23916 REFERENCE A92493 !$#authors Laurent, B.C.; Nilsson, M.H.L.; Bavik, C.O.; Jones, T.A.; !1Sundelin, J.; Peterson, P.A. !$#journal J. Biol. Chem. (1985) 260:11476-11480 !$#title Characterization of the rat retinol-binding protein gene and !1its comparison to the three-dimensional structure of the !1protein. !$#cross-references MUID:86008182; PMID:4044565 !$#accession A92493 !'##molecule_type DNA !'##residues 1-201 ##label LAU !'##cross-references GB:K03046; NID:g206583; PIDN:AAA42018.1; !1PID:g206585 REFERENCE A92525 !$#authors Sundelin, J.; Laurent, B.C.; Anundi, H.; Tragardh, L.; !1Larhammar, D.; Bjorck, L.; Eriksson, U.; Akerstrom, B.; !1Jones, A.; Newcomer, M.; Peterson, P.A.; Rask, L. !$#journal J. Biol. Chem. (1985) 260:6472-6480 !$#title Amino acid sequence homologies between rabbit, rat, and !1human serum retinol-binding proteins. !$#cross-references MUID:85207643; PMID:3838985 !$#accession A92525 !'##molecule_type mRNA !'##residues 30-201 ##label SUN !'##cross-references GB:M10934; NID:g206588; PIDN:AAA42020.1; !1PID:g206589 !$#accession B92525 !'##molecule_type protein !'##residues 19-59 ##label SU2 COMMENT For general comments see the entry for the human protein !1(PIR:VAHU). GENETICS !$#introns 37/3; 83/2; 119/1; 190/1 CLASSIFICATION #superfamily lipocalin; lipocalin homology KEYWORDS liver; plasma; retinol binding; vitamin A FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-201 #product plasma retinol-binding protein #status !8predicted #label MPT\ !$33-192 #domain lipocalin homology #label LIP\ !$22-178,88-192, !$138-147 #disulfide_bonds #status predicted SUMMARY #length 201 #molecular-weight 23220 #checksum 3753 SEQUENCE /// ENTRY LPHUD #type complete TITLE apolipoprotein D precursor [validated] - human ALTERNATE_NAMES apoD; gross cystic disease fluid protein 24 (GCDFP-24) ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 15-Sep-2000 ACCESSIONS A26958; A03224; S13050 REFERENCE A26958 !$#authors Drayna, D.T.; McLean, J.W.; Wion, K.L.; Trent, J.M.; !1Drabkin, H.A.; Lawn, R.M. !$#journal DNA (1987) 6:199-204 !$#title Human apolipoprotein D gene: gene sequence, chromosome !1localization, and homology to the alpha-2u-globulin !1superfamily. !$#cross-references MUID:87246069; PMID:2439269 !$#accession A26958 !'##molecule_type DNA !'##residues 1-189 ##label DRA1 !'##cross-references GB:M16648; GB:M16649; GB:M16695; GB:M16696; !1NID:g178845; PIDN:AAA51764.1; PID:g178847 REFERENCE A03224 !$#authors Drayna, D.; Fielding, C.; McLean, J.; Baer, B.; Castro, G.; !1Chen, E.; Comstock, L.; Henzel, W.; Kohr, W.; Rhee, L.; !1Wion, K.; Lawn, R. !$#journal J. Biol. Chem. (1986) 261:16535-16539 !$#title Cloning and expression of human apolipoprotein D cDNA. !$#cross-references MUID:87057347; PMID:3453108 !$#accession A03224 !'##molecule_type mRNA !'##residues 1-189 ##label DRA2 !'##cross-references GB:J02611; NID:g178840; PIDN:AAB59517.1; !1PID:g178841 !'##note part of the sequence was confirmed by protein sequencing REFERENCE S13050 !$#authors Balbin, M.; Freije, J.M.P.; Fueyo, A.; Sanchez, L.M.; !1Lopez-Otin, C. !$#journal Biochem. J. (1990) 271:803-807 !$#title Apolipoprotein D is the major protein component in cyst !1fluid from women with human breast gross cystic disease. !$#cross-references MUID:91058519; PMID:2244881 !$#accession S13050 !'##molecule_type protein !'##residues 28-41;42-45;'X',47-51;52-60;61-64,'X',66-73;76-82;83-97, !1'X',99-104;109-110,'X',112-118,'X',120-141,'X',143-146,'X', !1148-150;152-164;165-175;176-187 ##label BAL !'##experimental_source mammary cyst fluid !'##note carbohydrate binding sites determined; the sequence of the !1amino-terminal pyroglutamyl peptide of the mature protein is !1also reported REFERENCE A50026 !$#authors Peitsch, M.C.; Boguski, M.S. !$#submission submitted to the Brookhaven Protein Data Bank, April 1992 !$#cross-references PDB:2APD !$#contents annotation; theoretical model, residues 21-189 REFERENCE A55901 !$#authors Yang, C.Y.; Gu, Z.W.; Blanco-Vaca, F.; Gaskell, S.J.; Yang, !1M.; Massey, J.B.; Gotto Jr., A.M.; Pownall, H.J. !$#journal Biochemistry (1994) 33:12451-12455 !$#title Structure of human apolipoprotein D: locations of the !1intermolecular and intramolecular disulfide links. !$#cross-references MUID:95001965; PMID:7918467 !$#contents annotation; confirmation of peptide sequence overlap; !1disulfide bonds; N-glycosylation REFERENCE A57914 !$#authors Schindler, P.A.; Settineri, C.A.; Collet, X.; Fielding, !1C.J.; Burlingame, A.L. !$#journal Protein Sci. (1995) 4:791-803 !$#title Site-specific detection and structural characterization of !1the glycosylation of human plasma proteins !1lecithin:cholesterol acyltransferase and apolipoprotein D !1using HPLC/electrospray mass spectrometry and sequential !1glycosidase digestion. !$#cross-references MUID:95338133; PMID:7613477 !$#contents annotation; N-glycosylation COMMENT ApoD occurs in the macromolecular complex with !1lecithin-cholesterol acyltransferase. COMMENT ApoD is primarily localized in HDL (60-65%), with most of !1the remainder in VHDL and only trace amounts in VLDL and !1LDL. COMMENT ApoD has been found in liver, intestine, pancreas, kidney, !1placenta, adrenal, spleen, and fetal brain tissue. GENETICS !$#gene GDB:APOD !'##cross-references GDB:119690; OMIM:107740 !$#map_position 3q27-3qter !$#introns 41/3; 82/2; 112/1 !$#note the first intron occurs before the initiator codon CLASSIFICATION #superfamily lipocalin; lipocalin homology KEYWORDS glycoprotein; lipid binding; lipid transport; lipoprotein; !1plasma; pyroglutamic acid FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-189 #product apolipoprotein D #status experimental #label !8MAT\ !$37-185 #domain lipocalin homology #label LIP\ !$21 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$28-134,61-185 #disulfide_bonds #status experimental\ !$65,98 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$136 #disulfide_bonds interchain (to apolipoprotein A-II !829) #status experimental SUMMARY #length 189 #molecular-weight 21275 #checksum 2438 SEQUENCE /// ENTRY CUWOI #type complete TITLE insecticyanin - tobacco hornworm ORGANISM #formal_name Manduca sexta #common_name tobacco hornworm DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 18-Jul-1997 ACCESSIONS A03225 REFERENCE A92449 !$#authors Riley, C.T.; Barbeau, B.K.; Keim, P.S.; Kezdy, F.J.; !1Heinrikson, R.L.; Law, J.H. !$#journal J. Biol. Chem. (1984) 259:13159-13165 !$#title The covalent protein structure of insecticyanin, a blue !1biliprotein from the hemolymph of the tobacco hornworm, !1Manduca sexta L. !$#cross-references MUID:85030430; PMID:6386809 !$#accession A03225 !'##molecule_type protein !'##residues 1-189 ##label RIL !'##experimental_source fifth instar larvae REFERENCE A91070 !$#authors Holden, H.M.; Rypniewski, W.R.; Law, J.H.; Rayment, I. !$#journal EMBO J. (1987) 6:1565-1570 !$#title The molecular structure of insecticyanin from the tobacco !1hornworm Manduca sexta L. at 2.6 angstrom resolution. !$#cross-references MUID:87275848; PMID:3608987 !$#contents annotation; X-ray crystallography, 2.6 angstroms REFERENCE A90492 !$#authors Goodman, W.G.; Adams, B.; Trost, J.T. !$#journal Biochemistry (1985) 24:1168-1175 !$#title Purification and characterization of a biliverdin-associated !1protein from the hemolymph of Manduca sexta. !$#cross-references MUID:86159655; PMID:4096898 !$#contents annotation; identification of chromophore COMMENT Insecticyanin is a homotetramer. The protomers consist !1primarily of eight antiparallel beta-pleated strands, which !1enclose a hydrophobic pocket, and an alpha-helix. The !1hydrophobic pocket binds a chromophore identified as !1biliverdin IX, isomer gamma. The biliverdin molecule remains !1in closed conformation, with the two propionate chains !1directed outwards. COMMENT Insecticyanin is synthesized only in the caterpillars, !1apparently by the epidermis, and secreted into the !1hemolymph. The protein is passed over from the larval !1hemolymph to that of pupae and adults and is sequestered in !1the eggs. COMMENT Mixed with lipoprotein-bound carotenes, this blue protein !1provides hornworms with their green cryptic coloration !1(camouflage). CLASSIFICATION #superfamily lipocalin; lipocalin homology KEYWORDS hemolymph; integument coloration; pigment binding FEATURE !$18-173 #domain lipocalin homology #label LIP\ !$9-119,43-175 #disulfide_bonds #status experimental SUMMARY #length 189 #molecular-weight 21379 #checksum 1457 SEQUENCE /// ENTRY OMHU1 #type complete TITLE alpha-1-acid glycoprotein 1 precursor [validated] - human ALTERNATE_NAMES alpha-1-acid glycoprotein A; alpha-1-AGP; orosomucoid 1 ORGANISM #formal_name Homo sapiens #common_name man DATE 24-Apr-1984 #sequence_revision 30-Sep-1987 #text_change 08-Dec-2000 ACCESSIONS A28346; A93567; A91553; A90367; A03226; A23805 REFERENCE A28346 !$#authors Dente, L.; Pizza, M.G.; Metspalu, A.; Cortese, R. !$#journal EMBO J. (1987) 6:2289-2296 !$#title Structure and expression of the genes coding for human !1alpha-1-acid glycoprotein. !$#cross-references MUID:88029318; PMID:2822385 !$#accession A28346 !'##molecule_type DNA !'##residues 1-201 ##label DEN !'##cross-references GB:X05779 REFERENCE A93567 !$#authors Dente, L.; Ciliberto, G.; Cortese, R. !$#journal Nucleic Acids Res. (1985) 13:3941-3952 !$#title Structure of the human alpha-1-acid glycoprotein gene: !1sequence homology with other human acute phase protein !1genes. !$#cross-references MUID:85242080; PMID:2409529 !$#accession A93567 !'##molecule_type mRNA !'##residues 1-201 ##label DE2 !'##cross-references GB:X02544; NID:g24444; PIDN:CAA26397.1; PID:g757907 REFERENCE A91553 !$#authors Board, P.G.; Jones, I.M.; Bentley, A.K. !$#journal Gene (1986) 44:127-131 !$#title Molecular cloning and nucleotide sequence of human alpha-1 !1acid glycoprotein cDNA. !$#cross-references MUID:87031577; PMID:3770479 !$#accession A91553 !'##molecule_type mRNA !'##residues 1-201 ##label BOA !'##cross-references GB:M13692; NID:g178256; PIDN:AAA35515.1; !1PID:g178257 REFERENCE A90367 !$#authors Schmid, K.; Kaufmann, H.; Isemura, S.; Bauer, F.; Emura, J.; !1Motoyama, T.; Ishiguro, M.; Nanno, S. !$#journal Biochemistry (1973) 12:2711-2724 !$#title Structure of alpha-1-acid glycoprotein. The complete amino !1acid sequence, multiple amino acid substitutions, and !1homology with the immunoglobulins. !$#cross-references MUID:73197484; PMID:4711474 !$#accession A90367 !'##molecule_type protein !'##residues 19-181,183-192,194-201 ##label SCH !'##note 38-Arg, 50-Ala, 65-Ala, 91-Phe, 94-Ser, 95-Ser, 106-Val, !1110-Glu, 113-Arg, 116-Val, 128-Leu, 130-Phe, 131-Gly, !1132-Ser, 133-Tyr, 134-Leu, 135-Asp, 144-Phe, 158-Gln, !1167-Cys, 170-Arg, and 174-Met were also found REFERENCE A90378 !$#authors Schmid, K.; Buergi, W.; Collins, J.H.; Nanno, S. !$#journal Biochemistry (1974) 13:2694-2697 !$#title The disulfide bonds of alpha-1-acid glycoprotein. !$#cross-references MUID:74290014; PMID:4603214 !$#contents annotation; disulfide bonds COMMENT Alpha-1-AGP, synthesized in the liver and leucocytes, !1appears to function in modulating the activity of the immune !1system during the acute-phase reaction. COMMENT See also PIR:OMHU2. GENETICS !$#gene GDB:ORM1 !'##cross-references GDB:120250; OMIM:138600 !$#map_position 9q32-9q32 !$#introns 38/3; 86/2; 110/1; 146/1; 180/3 CLASSIFICATION #superfamily lipocalin; lipocalin homology KEYWORDS acute phase; glycoprotein; leukocyte; liver; plasma; !1pyroglutamic acid FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-201 #product alpha-1-acid glycoprotein 1 #status !8experimental #label MAT\ !$34-183 #domain lipocalin homology #label LIP\ !$19 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$23-165,90-183 #disulfide_bonds #status experimental\ !$33,56,72,93,103 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 201 #molecular-weight 23511 #checksum 5478 SEQUENCE /// ENTRY OMHU2 #type complete TITLE alpha-1-acid glycoprotein 2 precursor - human ALTERNATE_NAMES alpha-1-acid glycoprotein B; orosomucoid 2 ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1992 #sequence_revision 07-Jun-1996 #text_change 22-Jun-1999 ACCESSIONS JT0326; B28346 REFERENCE JT0326 !$#authors Merritt, C.M.; Board, P.G. !$#journal Gene (1988) 66:97-106 !$#title Structure and characterisation of a duplicated human alpha 1 !1acid-glycoprotein gene. !$#cross-references MUID:88329732; PMID:2970990 !$#accession JT0326 !'##molecule_type DNA !'##residues 1-201 ##label MER !'##cross-references GB:M21540; NID:g177839; PIDN:AAA51549.1; !1PID:g177840 REFERENCE A28346 !$#authors Dente, L.; Pizza, M.G.; Metspalu, A.; Cortese, R. !$#journal EMBO J. (1987) 6:2289-2296 !$#title Structure and expression of the genes coding for human !1alpha-1-acid glycoprotein. !$#cross-references MUID:88029318; PMID:2822385 !$#accession B28346 !'##molecule_type DNA !'##residues 1-118,'N',120-201 ##label DEN !'##cross-references GB:X06674 COMMENT Alpha-1-AGP, synthesized in the liver and leucocytes, !1appears to function in modulating the activity of the immune !1system during the acute-phase reaction. COMMENT See also PIR:OMHU1. GENETICS !$#gene GDB:ORM2 !'##cross-references GDB:120251; OMIM:138610 !$#map_position 9q32-9q32 !$#introns 38/3; 86/2; 110/1; 146/1; 180/3 CLASSIFICATION #superfamily lipocalin; lipocalin homology KEYWORDS acute phase; glycoprotein; leukocyte; liver; plasma; !1pyroglutamic acid FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-201 #product alpha-1-acid glycoprotein 2 #status !8predicted #label MAT\ !$34-183 #domain lipocalin homology #label LIP\ !$19 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status predicted\ !$23-165,90-183 #disulfide_bonds #status predicted\ !$33,56,72,93,103 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 201 #molecular-weight 23602 #checksum 4589 SEQUENCE /// ENTRY OMRT1 #type complete TITLE alpha-1-acid glycoprotein precursor - rat ALTERNATE_NAMES orosomucoid ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 24-Sep-1999 ACCESSIONS A93069; A92517; A92293; A03227; A22279; A23449 REFERENCE A93069 !$#authors Liao, Y.C.J.; Taylor, J.M.; Vannice, J.L.; Clawson, G.A.; !1Smuckler, E.A. !$#journal Mol. Cell. Biol. (1985) 5:3634-3639 !$#title Structure of the rat alpha-1-acid glycoprotein gene. !$#cross-references MUID:86310846; PMID:2943986 !$#accession A93069 !'##molecule_type DNA !'##residues 1-205 ##label LIA !'##cross-references GB:M11329; NID:g202794; PIDN:AAA40700.1; !1PID:g202795 REFERENCE A92517 !$#authors Reinke, R.; Feigelson, P. !$#journal J. Biol. Chem. (1985) 260:4397-4403 !$#title Rat alpha-1-acid glycoprotein. Gene sequence and regulation !1by glucocorticoids in transfected L-cells. !$#cross-references MUID:85157606; PMID:3838547 !$#accession A92517 !'##molecule_type DNA !'##residues 1-205 ##label REI !'##cross-references GB:M10614; NID:g202796; PIDN:AAA40701.1; !1PID:g202797 REFERENCE A92293 !$#authors Ricca, G.A.; Taylor, J.M. !$#journal J. Biol. Chem. (1981) 256:11199-11202 !$#title Nucleotide sequence of rat alpha-1-acid glycoprotein !1messenger RNA. !$#cross-references MUID:82030935; PMID:6270146 !$#accession A92293 !'##molecule_type mRNA !'##residues 1-205 ##label RIC !'##cross-references GB:J00696; GB:M25466; NID:g202792; PIDN:AAA40699.1; !1PID:g202793 COMMENT Alpha-1-AGP appears to function in modulating the activity !1of the immune system during the acute-phase reaction. COMMENT The synthesis of alpha-1-AGP, which occurs in the liver, is !1strongly induced by glucocorticoids. GENETICS !$#introns 39/3; 87/2; 111/1; 146/1; 180/3 CLASSIFICATION #superfamily lipocalin; lipocalin homology KEYWORDS acute phase; glycoprotein; liver; plasma FEATURE !$1-18 #domain (or 5-18) signal sequence #status predicted !8#label SIG\ !$19-205 #product alpha-1-acid glycoprotein #status predicted !8#label MPT\ !$35-183 #domain lipocalin homology #label LIP\ !$76,94,104,134 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$91-183 #disulfide_bonds #status predicted SUMMARY #length 205 #molecular-weight 23575 #checksum 1453 SEQUENCE /// ENTRY OMMS1 #type complete TITLE alpha-1-acid glycoprotein 1 precursor - mouse ALTERNATE_NAMES orosomucoid ORGANISM #formal_name Mus musculus #common_name house mouse DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 22-Jun-1999 ACCESSIONS A29294; A26300; C32476 REFERENCE A29294 !$#authors Cooper, R.; Eckley, D.M.; Papaconstantinou, J. !$#journal Biochemistry (1987) 26:5244-5250 !$#title Nucleotide sequence of the mouse alpha-1-acid glycoprotein !1gene 1. !$#cross-references MUID:88050798; PMID:3676251 !$#accession A29294 !'##molecule_type DNA !'##residues 1-207 ##label CO1 !'##cross-references GB:M17376; NID:g191777; PIDN:AAA37193.1; !1PID:g387095 REFERENCE A26300 !$#authors Cooper, R.; Papaconstantinou, J. !$#journal J. Biol. Chem. (1986) 261:1849-1853 !$#title Evidence for the existence of multiple alpha-1-acid !1glycoprotein genes in the mouse. !$#cross-references MUID:86111861; PMID:3003086 !$#accession A26300 !'##molecule_type mRNA !'##residues 70-207 ##label CO2 !'##cross-references GB:M12566; NID:g193595; PIDN:AAA91744.1; !1PID:g387176 REFERENCE A32476 !$#authors Lee, S.C.; Chang, C.J.; Lee, Y.M.; Lei, H.Y.; Lai, M.Y.; !1Chen, D.S. !$#journal DNA (1989) 8:245-251 !$#title Molecular cloning of cDNAs corresponding to two genes of !1alpha-1-acid glycoprotein and characterization of two !1alleles of AGP-1 in the mouse. !$#cross-references MUID:89356252; PMID:2475311 !$#accession C32476 !'##molecule_type mRNA !'##residues 1-207 ##label LEE !'##cross-references GB:M27009; NID:g531208; PIDN:AAA37196.1; !1PID:g531209 COMMENT Three genes coding for different forms of alpha-1-AGP are !1present in the mouse. COMMENT Alpha-1-AGP is synthesized in the liver, the synthesis being !1controlled by glucocorticoids. GENETICS !$#gene AGP-1 !$#introns 39/3; 87/2; 111/1; 147/1; 181/3 CLASSIFICATION #superfamily lipocalin; lipocalin homology KEYWORDS acute phase; glycoprotein; liver; plasma FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-207 #product alpha-1-acid glycoprotein 1 #status !8predicted #label MPT\ !$35-184 #domain lipocalin homology #label LIP\ !$25,34,69,76,94,104 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$91-184 #disulfide_bonds #status predicted SUMMARY #length 207 #molecular-weight 23843 #checksum 8339 SEQUENCE /// ENTRY B31955 #type complete TITLE cellular retinaldehyde-binding protein - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B31955; A55013 REFERENCE A92697 !$#authors Crabb, J.W.; Goldflam, S.; Harris, S.E.; Saari, J.C. !$#journal J. Biol. Chem. (1988) 263:18688-18692 !$#title Cloning of the cDNAs encoding the cellular !1retinaldehyde-binding protein from bovine and human retina !1and comparison of the protein structures. !$#cross-references MUID:89066656; PMID:3198595 !$#accession B31955 !'##molecule_type mRNA !'##residues 1-317 ##label CRA !'##cross-references GB:J04213; NID:g190853; PIDN:AAA60251.1; !1PID:g190854 REFERENCE A55013 !$#authors Intres, R.; Goldflam, S.; Cook, J.R.; Crabb, J.W. !$#journal J. Biol. Chem. (1994) 269:25411-25418 !$#title Molecular cloning and structural analysis of the human gene !1encoding cellular retinaldehyde-binding protein. !$#cross-references MUID:95014337; PMID:7929238 !$#accession A55013 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-317 ##label RES !'##cross-references GB:L34219; NID:g598228; PIDN:AAA65123.1; !1PID:g598229 GENETICS !$#gene GDB:RLBP1 !'##cross-references GDB:127341; OMIM:180090 !$#map_position 15q26-15q26 !$#introns 4/3; 47/3; 116/1; 175/3; 228/3; 265/3 CLASSIFICATION #superfamily cellular retinaldehyde-binding protein; !1cellular retinaldehyde-binding protein homology FEATURE !$97-291 #domain cellular retinaldehyde-binding protein !8homology #label CRB SUMMARY #length 317 #molecular-weight 36474 #checksum 6687 SEQUENCE /// ENTRY A31955 #type complete TITLE cellular retinaldehyde-binding protein - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A31955; A30052 REFERENCE A92697 !$#authors Crabb, J.W.; Goldflam, S.; Harris, S.E.; Saari, J.C. !$#journal J. Biol. Chem. (1988) 263:18688-18692 !$#title Cloning of the cDNAs encoding the cellular !1retinaldehyde-binding protein from bovine and human retina !1and comparison of the protein structures. !$#cross-references MUID:89066656; PMID:3198595 !$#accession A31955 !'##molecule_type mRNA !'##residues 1-317 ##label CRA !'##cross-references GB:J04214; NID:g163652; PIDN:AAA30751.1; !1PID:g163653 !'##note the authors translated the codon ATT for residue 162 as Asn and !1GAA for residue 272 as Asp REFERENCE A30052 !$#authors Crabb, J.W.; Johnson, C.M.; Carr, S.A.; Armes, L.G.; Saari, !1J.C. !$#journal J. Biol. Chem. (1988) 263:18678-18687 !$#title The complete primary structure of the cellular !1retinaldehyde-binding protein from bovine retina. !$#cross-references MUID:89066655; PMID:3198594 !$#accession A30052 !'##molecule_type protein !'##residues 2-161,'N',163-271,'D',273-317 ##label CR2 CLASSIFICATION #superfamily cellular retinaldehyde-binding protein; !1cellular retinaldehyde-binding protein homology KEYWORDS acetylated amino end FEATURE !$2-317 #product cellular retinaldehyde-binding protein !8#status predicted #label MAT\ !$97-291 #domain cellular retinaldehyde-binding protein !8homology #label CRB\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental SUMMARY #length 317 #molecular-weight 36518 #checksum 5307 SEQUENCE /// ENTRY A37766 #type complete TITLE SEC14 protein - yeast (Kluyveromyces marxianus var. lactis) ORGANISM #formal_name Kluyveromyces marxianus var. lactis, Candida sphaerica DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A37766 REFERENCE A37766 !$#authors Salama, S.R.; Cleves, A.E.; Malehorn, D.E.; Whitters, E.A.; !1Bankaitis, V.A. !$#journal J. Bacteriol. (1990) 172:4510-4521 !$#title Cloning and characterization of Kluyveromyces lactis SEC14, !1a gene whose product stimulates Golgi secretory function in !1Saccharomyces cerevisiae. !$#cross-references MUID:90330560; PMID:2198263 !$#accession A37766 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-301 ##label SAL CLASSIFICATION #superfamily cellular retinaldehyde-binding protein; !1cellular retinaldehyde-binding protein homology FEATURE !$57-264 #domain cellular retinaldehyde-binding protein !8homology #label CRB SUMMARY #length 301 #molecular-weight 34529 #checksum 3455 SEQUENCE /// ENTRY A47404 #type complete TITLE alpha-tocopherol transfer protein isoform II cellular retinaldehyde-binding protein homolog - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A47404 REFERENCE A47404 !$#authors Sato, Y.; Arai, H.; Miyata, A.; Tokita, S.; Yamamoto, K.; !1Tanabe, T.; Inoue, K. !$#journal J. Biol. Chem. (1993) 268:17705-17710 !$#title Primary structure of alpha-tocopherol transfer protein from !1rat liver. Homology with cellular retinaldehyde-binding !1protein. !$#cross-references MUID:93352574; PMID:8349655 !$#accession A47404 !'##status preliminary !'##molecule_type mRNA; protein !'##residues 1-278 ##label SAT !'##cross-references GB:D16339; NID:g436049; PIDN:BAA03843.1; !1PID:g436050 !'##experimental_source liver !'##note sequence extracted from NCBI backbone (NCBIN:136429, !1NCBIP:136430) CLASSIFICATION #superfamily cellular retinaldehyde-binding protein; !1cellular retinaldehyde-binding protein homology FEATURE !$53-247 #domain cellular retinaldehyde-binding protein !8homology #label CRB SUMMARY #length 278 #molecular-weight 31845 #checksum 1857 SEQUENCE /// ENTRY A47327 #type complete TITLE selenoprotein P precursor [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 21-Sep-1993 #sequence_revision 01-Dec-1995 #text_change 15-Sep-2000 ACCESSIONS A47327; S42752 REFERENCE A47327 !$#authors Hill, K.E.; Lloyd, R.S.; Burk, R.F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:537-541 !$#title Conserved nucleotide sequences in the open reading frame and !13' untranslated region of selenoprotein P mRNA. !$#cross-references MUID:93133823; PMID:8421687 !$#accession A47327 !'##molecule_type mRNA !'##residues 1-381 ##label HIL !'##cross-references GB:Z11793; NID:g36425; PIDN:CAA77836.1; !1PID:g2654365 !'##experimental_source heart and liver !'##note in Genbank entry HSSELPM, release 117.0, PIDN:CAA77836.1, the !1selenocysteine UGA codons are translated as 'X' REFERENCE S42752 !$#authors Akesson, B.; Bellew, T.; Burk, R.F. !$#journal Biochim. Biophys. Acta (1994) 1204:243-249 !$#title Purification of selenoprotein P from human plasma. !$#cross-references MUID:94191007; PMID:8142465 !$#accession S42752 !'##molecule_type protein !'##residues 20-27,'X',29-33 ##label AKE !'##note mature forms of 55K and 61K were detected in plasma; the !1protein was shown to contain selenocysteine but individual !1sites were not identified directly GENETICS !$#gene GDB:SEPP1; SLNP !'##cross-references GDB:138278; OMIM:601484 !$#map_position 5q31-5q31 FUNCTION !$#description may act as a free-radical scavenger CLASSIFICATION #superfamily selenoprotein P KEYWORDS extracellular protein; glycoprotein; heparin binding; liver; !1plasma; selenocysteine FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-381 #product selenoprotein P #status experimental #label !8MAT\ !$46,83,119,128,338 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$59,300,318,330,345, !$352,367,369,376,378 #modified_site selenocysteine #status predicted SUMMARY #length 381 #molecular-weight 42705 #checksum 4477 SEQUENCE /// ENTRY OMRTSP #type complete TITLE selenoprotein P precursor [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 15-Sep-2000 ACCESSIONS A40380; B40380; S68322 REFERENCE A40380 !$#authors Hill, K.E.; Lloyd, R.S.; Yang, J.G.; Read, R.; Burk, R.F. !$#journal J. Biol. Chem. (1991) 266:10050-10053 !$#title The cDNA for rat selenoprotein P contains 10 TGA codons in !1the open reading frame. !$#cross-references MUID:91244760; PMID:2037562 !$#accession A40380 !'##molecule_type mRNA !'##residues 1-385 ##label HIL !'##cross-references GB:M63574; NID:g206893; PIDN:AAA42129.1; !1PID:g206894 !$#accession B40380 !'##molecule_type protein !'##residues 20-41;267-287;316-327 ##label HI2 REFERENCE S68322 !$#authors Chittum, H.S.; Himeno, S.; Hill, K.E.; Burk, R.F. !$#journal Arch. Biochem. Biophys. (1996) 325:124-128 !$#title Multiple forms of selenoprotein P in rat plasma. !$#cross-references MUID:96140605; PMID:8554336 !$#accession S68322 !'##molecule_type protein !'##residues 20-27 ##label CHI CLASSIFICATION #superfamily selenoprotein P KEYWORDS extracellular protein; glycoprotein; heparin binding; liver; !1plasma; selenocysteine FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-385 #product selenoprotein P #status experimental #label !8MAT\ !$59,264,335,357,371, !$373,380,382 #modified_site selenocysteine #status predicted\ !$83,174,188,370,375 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$282,323 #modified_site selenocysteine #status experimental SUMMARY #length 385 #molecular-weight 42614 #checksum 1647 SEQUENCE /// ENTRY IYHU2 #type complete TITLE inter-alpha-trypsin inhibitor heavy chain 2 precursor - human ALTERNATE_NAMES inter-alpha-trypsin inhibitor complex component II ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 04-Feb-2000 ACCESSIONS S00346; S09064; B39967; S00632; B34245; S28929; C53642 REFERENCE S00346 !$#authors Gebhard, W.; Schreitmueller, T.; Hochstrasser, K.; Wachter, !1E. !$#journal FEBS Lett. (1988) 229:63-67 !$#title Complementary DNA and derived amino acid sequence of the !1precursor of one of the three protein components of the !1inter-alpha-trypsin inhibitor complex. !$#cross-references MUID:88152237; PMID:2450046 !$#accession S00346 !'##molecule_type mRNA !'##residues 1-946 ##label GEB !'##cross-references EMBL:X07173 !'##experimental_source liver !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing; however, no !1peptides beyond 698-Arg were isolated, suggesting that !1proteolytic processing occurs at the carboxyl as well as the !1amino end to produce the mature protein !'##note due to a double frameshift, the nucleic acid sequence of codons !1363-372 is inconsistent with the protein translation !'##note in one clone, a T is lacking from codon 716; this clone could !1code for a protein of 738 amino acids with the carboxyl end !1VSILTQNLEKSSTWFLTQNQEL starting at position 717 REFERENCE S09064 !$#authors Schreitmueller, T.; Hochstrasser, K.; Reisinger, P.W.M.; !1Wachter, E.; Gebhard, W. !$#journal Biol. Chem. Hoppe-Seyler (1987) 368:963-970 !$#title cDNA cloning of human inter-alpha-trypsin inhibitor !1discloses three different proteins. !$#cross-references MUID:88024442; PMID:3663330 !$#accession S09064 !'##molecule_type mRNA !'##residues 265,'RR',268-284,'D',286-946 ##label SCH !'##note this sequence has been revised in reference S00346 REFERENCE A39967 !$#authors Salier, J.P.; Diarra-Mehrpour, M.; Sesboue, R.; Bourguignon, !1J.; Benarous, R.; Ohkubo, I.; Kurachi, S.; Kurachi, K.; !1Martin, J.P. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:8272-8276 !$#title Isolation and characterization of cDNAs encoding the heavy !1chain of human inter-alpha-trypsin inhibitor (IalphaTI): !1unambiguous evidence for multipolypeptide chain structure of !1IalphaTI. !$#cross-references MUID:88068576; PMID:2446322 !$#accession B39967 !'##molecule_type mRNA !'##residues 384-673,'A',675-704,'S',706-728,'D',730,'A',732-865 ##label !1SAL !'##cross-references GB:M18193; GB:J03013; NID:g338222; PIDN:AAA60558.1; !1PID:g553647 !'##experimental_source liver REFERENCE S00632 !$#authors Salier, J.P.; Diarra-Mehrpour, M.; Sesbouee, R.; !1Bourguignon, J.; Martin, J.P. !$#journal Biol. Chem. Hoppe-Seyler (1988) 369(Suppl.):15-18 !$#title Human inter-alpha-trypsin inhibitor. Isolation and !1characterization of heavy (H) chain cDNA clones coding for a !1383 amino-acid sequence of the H chain. !$#cross-references MUID:89076497; PMID:2462430 !$#accession S00632 !'##molecule_type mRNA !'##residues 384-673,'A',675-704,'S',706-728,'D',730,'A',732-766 ##label !1SA2 !'##cross-references GB:M33033; NID:g186589; PIDN:AAA59195.1; !1PID:g186590 REFERENCE A92736 !$#authors Enghild, J.J.; Thogersen, I.B.; Pizzo, S.V.; Salvesen, G. !$#journal J. Biol. Chem. (1989) 264:15975-15981 !$#title Analysis of inter-alpha-trypsin inhibitor and a novel !1trypsin inhibitor, pre-alpha-trypsin inhibitor, from human !1plasma. Polypeptide chain stoichiometry and assembly by !1glycan. !$#cross-references MUID:89380192; PMID:2476436 !$#accession B34245 !'##molecule_type protein !'##residues 55-74 ##label ENG REFERENCE S28928 !$#authors Malki, N.; Balduyck, M.; Maes, P.; Capon, C.; Mizon, C.; !1Han, K.K.; Tartar, A.; Fournet, B.; Mizon, J. !$#journal Biol. Chem. Hoppe-Seyler (1992) 373:1009-1018 !$#title The heavy chains of human plasma inter-alpha-trypsin !1inhibitor: their isolation, their identification by !1electrophoresis and partial sequencing. Differential !1reactivity with Concanavalin A. !$#cross-references MUID:93039735; PMID:1384548 !$#accession S28929 !'##molecule_type protein !'##residues 55-64 ##label MAL REFERENCE A53642 !$#authors Wisniewski, H.G.; Burgess, W.H.; Oppenheim, J.D.; Vilcek, J. !$#journal Biochemistry (1994) 33:7423-7429 !$#title TSG-6, an arthritis-associated hyaluronan binding protein, !1forms a stable complex with the serum protein !1inter-alpha-inhibitor. !$#cross-references MUID:94271799; PMID:7516184 !$#accession C53642 !'##molecule_type protein !'##residues 55-64 ##label WIS COMMENT Inter-alpha-trypsin inhibitor is a complex of three !1proteins, each deriving from a different precursor. The !1inhibitory activity is with component I. COMMENT This protein is a heterodimer of heavy and light chains. GENETICS !$#gene GDB:ITIH2 !'##cross-references GDB:120108; OMIM:146640 !$#map_position 10p15-10p15 CLASSIFICATION #superfamily inter-alpha-trypsin inhibitor complex component !1II KEYWORDS carboxyglutamic acid; glycoprotein; heterodimer; serine !1proteinase inhibitor FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-54 #domain propeptide #status predicted #label PRO\ !$55-698 #product inter-alpha-trypsin inhibitor heavy chain 2 !8#status predicted #label MAT\ !$96,445 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$118,671 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$282,283 #modified_site gamma-carboxyglutamic acid (Glu) !8#status predicted\ !$421,422,423 #binding_site calcium (Asp, Gly, Asp) #status !8predicted SUMMARY #length 946 #molecular-weight 106436 #checksum 9519 SEQUENCE /// ENTRY A40668 #type complete TITLE hemolymph juvenile hormone-binding protein precursor - tobacco hornworm ALTERNATE_NAMES juvenile hormone carrier protein ORGANISM #formal_name Manduca sexta #common_name tobacco hornworm DATE 21-Sep-1993 #sequence_revision 01-Dec-1995 #text_change 22-Jun-1999 ACCESSIONS A40668; A37985; S00312; S03201; A56774 REFERENCE A40668 !$#authors Touhara, K.; Lerro, K.A.; Bonning, B.C.; Hammock, B.D.; !1Prestwich, G.D. !$#journal Biochemistry (1993) 32:2068-2075 !$#title Ligand binding by a recombinant insect juvenile hormone !1binding protein. !$#cross-references MUID:93192269; PMID:8448166 !$#accession A40668 !'##molecule_type mRNA !'##residues 1-244 ##label TOU !'##cross-references GB:S56567; NID:g299272; PIDN:AAB25736.1; !1PID:g299273 !'##experimental_source larva !'##note sequence inconsistent with the nucleotide translation !'##note sequence extracted from NCBI backbone (NCBIN:127016, !1NCBIP:127017) !'##note authors designate this clone JHBP cDNA 2; differences from JHBP !1cDNA 1 may represent polymorphism REFERENCE A37985 !$#authors Lerro, K.A.; Prestwich, G.D. !$#journal J. Biol. Chem. (1990) 265:19800-19806 !$#title Cloning and sequencing of a cDNA for the hemolymph juvenile !1hormone binding protein of larval Manduca sexta. !$#cross-references MUID:91060594; PMID:2246263 !$#accession A37985 !'##molecule_type mRNA !'##residues 16-63,'S',65-84,'I',86-205,'S',207-244 ##label LER !'##cross-references GB:M59436; GB:M37657; NID:g159517; PIDN:AAA29317.1; !1PID:g159518 !'##note authors designate this clone JHBP cDNA 1 REFERENCE S00312 !$#authors Kulcsar, P.; Prestwich, G.D. !$#journal FEBS Lett. (1988) 228:49-52 !$#title Detection and microsequencing of juvenile hormone-binding !1proteins of an insect by the use of an iodinated juvenile !1hormone analog. !$#cross-references MUID:88137602; PMID:3342877 !$#accession S00312 !'##molecule_type protein !'##residues 19-36,'T',38-43,'D',45-51,'N',55 ##label KUL REFERENCE S03201 !$#authors Peterson, R.C.; Dunn, P.E.; Seballos, H.L.; Barbeau, B.K.; !1Keim, P.S.; Riley, C.T.; Heinrikson, R.L.; Law, J.H. !$#journal Insect Biochem. (1982) 12:643-650 !$#title Juvenile hormone carrier protein of Manduca sexta !1haemolymph. Improved purification procedure; protein !1modification studies and sequence of the amino terminus of !1the protein. !$#accession S03201 !'##molecule_type protein !'##residues 19-36,'X',38 ##label PET REFERENCE A56774 !$#authors Touhara, K.; Prestwich, G.D. !$#journal Biochem. Biophys. Res. Commun. (1992) 182:466-473 !$#title Binding site mapping of a photoaffinity-labeled juvenile !1hormone binding protein. !$#cross-references MUID:92134256; PMID:1734862 !$#accession A56774 !'##molecule_type protein !'##residues 135-145;199-205,'P',207-210,'DN' ##label TO2 !'##note sequence modified after extraction from NCBI backbone !'##note the juvenile hormone photoaffinity analog used was [3H] !1epoxyhomofarnesyl diazoacetate CLASSIFICATION #superfamily hemolymph juvenile hormone-binding protein KEYWORDS hemolymph; lipid binding FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-244 #product hemolymph juvenile hormone-binding protein !8#status experimental #label MAT\ !$19-52,202-244 #region hormone-binding pocket SUMMARY #length 244 #molecular-weight 27137 #checksum 3791 SEQUENCE /// ENTRY VBHU #type complete TITLE transthyretin precursor [validated] - human ALTERNATE_NAMES prealbumin; TBPA CONTAINS transthyretin-derived amyloid fibril protein ORGANISM #formal_name Homo sapiens #common_name man DATE 24-Apr-1984 #sequence_revision 04-Dec-1986 #text_change 20-Apr-2001 ACCESSIONS A91532; I55234; S14818; S20217; JC1011; A94015; B94015; !1A92162; S36215; A35998; A28892; C30323; A19827; I52207; !1I55187; I55233; I55558; I77345; A03229 REFERENCE A91532 !$#authors Sasaki, H.; Yoshioka, N.; Takagi, Y.; Sakaki, Y. !$#journal Gene (1985) 37:191-197 !$#title Structure of the chromosomal gene for human serum !1prealbumin. !$#cross-references MUID:86031352; PMID:4054629 !$#accession A91532 !'##molecule_type DNA !'##residues 1-147 ##label SAS REFERENCE I55234 !$#authors Tsuzuki, T.; Mita, S.; Maeda, S.; Araki, S.; Shimada, K. !$#journal J. Biol. Chem. (1985) 260:12224-12227 !$#title Structure of the human prealbumin gene. !$#cross-references MUID:86008293; PMID:2995367 !$#accession I55234 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-147 ##label RES !'##cross-references GB:M11844; NID:g189587; PIDN:AAA60013.1; !1PID:g386999 REFERENCE S14818 !$#authors Christmanson, L.; Betsholtz, C.; Gustavsson, A.; Johansson, !1B.; Sletten, K.; Westermark, P. !$#journal FEBS Lett. (1991) 281:177-180 !$#title The transthyretin cDNA sequence is normal in !1transthyretin-derived senile systemic amyloidosis. !$#cross-references MUID:91200280; PMID:2015890 !$#accession S14818 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-147 ##label CHR !'##cross-references GB:X59498; NID:g37482; PIDN:CAA42087.1; PID:g37483 !$#accession S20217 !'##molecule_type protein !'##residues 'X',22-28 ##label CH2 REFERENCE JC1011 !$#authors Gu, J.R.; Jiang, H.Q.; He, L.P.; Li, D.Z.; Zhou, X.M.; Dai, !1W.L.; Qian, L.F.; Chen, Y.Q. !$#journal Sci. Sin. B Chem. Biol. Agric. Med. Earth Sci. (1991) !134:1312-1318 !$#title Transthyretin (prealbumin) gene in human primary hepatic !1cancer. !$#accession JC1011 !'##molecule_type mRNA !'##residues 1-147 ##label GUJ !'##experimental_source liver REFERENCE A94015 !$#authors Dwulet, F.E.; Merrill, D.B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:694-698 !$#title Primary structure of an amyloid prealbumin and its plasma !1precursor in a heredofamilial polyneuropathy of Swedish !1origin. !$#cross-references MUID:84144770; PMID:6583672 !$#contents amyloid fibrils and plasma from a patient with !1polyneuropathic amyloidosis, normal transthyretin and GRO !1variant !$#accession A94015 !'##molecule_type protein !'##residues 21-147 ##label DWU !$#accession B94015 !'##molecule_type protein !'##residues 21-49,'M',51-147 ##label DW2 !'##note this variant, GRO, constitutes a third of the transthyretin in !1plasma and two-thirds in the amyloid fibrils REFERENCE A92162 !$#authors Kanda, Y.; Goodman, D.S.; Canfield, R.E.; Morgan, F.J. !$#journal J. Biol. Chem. (1974) 249:6796-6805 !$#title The amino acid sequence of human plasma prealbumin. !$#cross-references MUID:75019190; PMID:4607556 !$#accession A92162 !'##molecule_type protein !'##residues 21-147 ##label KAN REFERENCE S36215 !$#authors Thylen, C.; Wahlqvist, J.; Haettner, E.; Sandgren, O.; !1Holmgren, G.; Lundgren, E. !$#journal EMBO J. (1993) 12:743-748 !$#title Modifications of transthyretin in amyloid fibrils: analysis !1of amyloid from homozygous and heterozygous individuals with !1the Met30 mutation. !$#cross-references MUID:93178450; PMID:8095018 !$#accession S36215 !'##molecule_type protein !'##residues 21-34,69-78 ##label THY REFERENCE A92851 !$#authors Blake, C.C.F.; Geisow, M.J.; Oatley, S.J.; Rerat, B.; Rerat, !1C. !$#journal J. Mol. Biol. (1978) 121:339-356 !$#title Structure of prealbumin: secondary, tertiary and quaternary !1interactions determined by Fourier refinement at 1.8 !1angstroms. !$#cross-references MUID:78220687; PMID:671542 !$#contents annotation; X-ray crystallography, 1.8 angstroms REFERENCE A93188 !$#authors Blake, C.C.F.; Oatley, S.J. !$#journal Nature (1977) 268:115-120 !$#title Protein-DNA and protein-hormone interactions in prealbumin: !1a model of the thyroid hormone nuclear receptor? !$#cross-references MUID:78071636; PMID:201845 !$#contents annotation; binding sites for thyroid hormones REFERENCE A35998 !$#authors Westermark, P.; Sletten, K.; Johansson, B.; Cornwell III, !1G.G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:2843-2845 !$#title Fibril in senile systemic amyloidosis is derived from normal !1transthyretin. !$#cross-references MUID:90207293; PMID:2320592 !$#accession A35998 !'##molecule_type protein !'##residues 21-82,'Q',84-147 ##label WES REFERENCE A28892 !$#authors Cornwell III, G.G.; Sletten, K.; Johansson, B.; Westermark, !1P. !$#journal Biochem. Biophys. Res. Commun. (1988) 154:648-653 !$#title Evidence that the amyloid fibril protein in senile systemic !1amyloidosis is derived from normal prealbumin. !$#cross-references MUID:88293495; PMID:3135807 !$#accession A28892 !'##molecule_type protein !'##residues 21-82,'Q',84-147 ##label COR REFERENCE A30323 !$#authors Gorevic, P.D.; Prelli, F.C.; Wright, J.; Pras, M.; !1Frangione, B. !$#journal J. Clin. Invest. (1989) 83:836-843 !$#title Systemic senile amyloidosis. Identification of a new !1prealbumin (transthyretin) variant in cardiac tissue: !1immunologic and biochemical similarity to one form of !1familial amyloidotic polyneuropathy. !$#cross-references MUID:89155805; PMID:2646319 !$#accession C30323 !'##molecule_type protein !'##residues 21-24,'I',26-82,'Q',84-141,'I',143-147 ##label GOR !'##experimental_source senile systemic amyloidosis patient heart tissue REFERENCE A19827 !$#authors Benson, M.D. !$#journal J. Clin. Invest. (1981) 67:1035-1041 !$#title Partial amino acid sequence homology between an !1heredofamilial amyloid protein and human plasma prealbumin. !$#cross-references MUID:81142690; PMID:6782125 !$#accession A19827 !'##molecule_type protein !'##residues 34,'V',36-42,'T',44 ##label BEN !'##experimental_source amyloid fibrils, kidney, autosomal dominant !1heredofamilial amyloidosis REFERENCE I52207 !$#authors Wallace, M.R.; Naylor, S.L.; Kluve-Beckerman, B.; Long, !1G.L.; McDonald, L.; Shows, T.B.; Benson, M.D. !$#journal Biochem. Biophys. Res. Commun. (1985) 129:753-758 !$#title Localization of the human prealbumin gene to chromosome 18. !$#cross-references MUID:85251684; PMID:2990465 !$#accession I52207 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-147 ##label RE2 !'##cross-references GB:M10605; NID:g189583; PIDN:AAA60012.1; !1PID:g189584 REFERENCE I55187 !$#authors Mita, S.; Maeda, S.; Shimada, K.; Araki, S. !$#journal J. Biochem. (1986) 100:1215-1222 !$#title Analyses of prealbumin mRNAs in individuals with familial !1amyloidotic polyneuropathy. !$#cross-references MUID:87137380; PMID:3818577 !$#accession I55187 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-49,'M',51-147 ##label RE3 !'##cross-references GB:D00096; NID:g219977; PIDN:BAA00059.1; !1PID:g219978 !'##experimental_source liver from a patient with polyneuropathic !1amyloidosis REFERENCE I55233 !$#authors Soprano, D.R.; Herbert, J.; Soprano, K.J.; Schon, E.A.; !1Goodman, D.S. !$#journal J. Biol. Chem. (1985) 260:11793-11798 !$#title Demonstration of transthyretin mRNA in the brain and other !1extrahepatic tissues in the rat. !$#cross-references MUID:86008229; PMID:4044580 !$#accession I55233 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 31-147 ##label RE4 !'##cross-references GB:M11714; NID:g339684; PIDN:AAA61181.1; !1PID:g339685 REFERENCE I55558 !$#authors Moses, A.C.; Rosen, H.N.; Moller, D.E.; Tsuzaki, S.; Haddow, !1J.E.; Lawlor, J.; Liepnieks, J.J.; Nichols, W.C.; Benson, !1M.D. !$#journal J. Clin. Invest. (1990) 86:2025-2033 !$#title A point mutation in transthyretin increases affinity for !1thyroxine and produces euthroid hyperthyroxinemia. !$#cross-references MUID:91072680; PMID:1979335 !$#accession I55558 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 113-129 ##label RE5 !'##cross-references GB:M63285; NID:g340014; PIDN:AAA36784.1; !1PID:g340015 REFERENCE I57456 !$#authors Maeda, S.; Mita, S.; Araki, S.; Shimada, K. !$#journal Mol. Biol. Med. (1986) 3:329-338 !$#title Structure and expression of the mutant prealbumin gene !1associated with familial amyloidotic polyneuropathy. !$#cross-references MUID:87038739; PMID:3022108 !$#accession I77345 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-49,'M',51-147 ##label RE6 !'##cross-references GB:M15517; NID:g189591; PIDN:AAA60018.1; !1PID:g387000 COMMENT Two dimer pairs each form internal channels that are the !1binding sites for thyroxine. Transthyretin binds L-thyroxine !1an order of magnitude more strongly than it binds !1triiodo-L-thyronine. Less than 1% of plasma prealbumin !1molecules are normally involved in thyroxine transport. COMMENT About 40% of plasma transthyretin circulates in a tight !1complex with plasma retinol-binding protein (RBP). The !1formation of the complex stabilizes the binding of retinol !1to RBP and decreases the glomerular filtration and renal !1catabolism of the relatively small RBP molecule. COMMENT Transthyretin is synthesized in the liver. COMMENT At least three sequence variants have been identified in !1amyloid fibrils from patients with polyneuropathic !1amyloidosis (FAP). GENETICS !$#gene GDB:TTR; PALB !'##cross-references GDB:119471; OMIM:176300 !$#map_position 18q11.2-18q12.1 !$#introns 23/3; 67/2; 112/3 COMPLEX homotetramer with two subunits of plasma retinol-binding !1protein (VAHU) CLASSIFICATION #superfamily transthyretin KEYWORDS albumin; amyloid; homotetramer; liver; plasma; !1polyneuropathy; retinol binding; thyroid hormone binding; !1vitamin A FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-147 #product transthyretin #status experimental #label !8MAT\ !$35,74 #binding_site thyroxine (Lys, Glu) #status !8experimental SUMMARY #length 147 #molecular-weight 15887 #checksum 4763 SEQUENCE /// ENTRY VBRB #type complete TITLE transthyretin - rabbit ALTERNATE_NAMES prealbumin ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 30-Sep-1993 ACCESSIONS B22621 REFERENCE A92526 !$#authors Sundelin, J.; Melhus, H.; Das, S.; Eriksson, U.; Lind, P.; !1Tragardh, L.; Peterson, P.A.; Rask, L. !$#journal J. Biol. Chem. (1985) 260:6481-6487 !$#title The primary structure of rabbit and rat prealbumin and a !1comparison with the tertiary structure of human prealbumin. !$#cross-references MUID:85207644; PMID:3922975 !$#accession B22621 !'##molecule_type protein !'##residues 1-127 ##label SUN COMMENT The protein is a tetramer of identical chains. CLASSIFICATION #superfamily transthyretin KEYWORDS albumin; liver; plasma; retinol binding; thyroid hormone; !1transport protein; vitamin A FEATURE !$15,54 #binding_site thyroxine (Lys, Glu) #status !8experimental SUMMARY #length 127 #molecular-weight 13657 #checksum 8455 SEQUENCE /// ENTRY VBMS #type complete TITLE transthyretin precursor - mouse ALTERNATE_NAMES prealbumin ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 22-Jun-1999 ACCESSIONS A24132; I55188 REFERENCE A24132 !$#authors Wakasugi, S.; Maeda, S.; Shimada, K.; Nakashima, H.; Migita, !1S. !$#journal J. Biochem. (1985) 98:1707-1714 !$#title Structural comparisons between mouse and human prealbumin. !$#cross-references MUID:86139970; PMID:3005251 !$#accession A24132 !'##molecule_type mRNA !'##residues 1-147 ##label WAK !'##cross-references GB:X03351; NID:g49911; PIDN:CAA27057.1; PID:g736256 REFERENCE I55188 !$#authors Wakasugi, S.; Maeda, S.; Shimada, K. !$#journal J. Biochem. (1986) 100:49-58 !$#title Structure and expression of the mouse prealbumin gene. !$#cross-references MUID:87008480; PMID:3020014 !$#accession I55188 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-147 ##label RES !'##cross-references GB:D00073; NID:g220560; PIDN:BAA00050.1; !1PID:g220562 COMMENT The protein is a tetramer of identical chains. COMMENT A variant of transthyretin differs from the above in having !150-Met, which is associated with a familial amyloidotic !1polyneuropathy. COMMENT The protein is synthesized in the liver. GENETICS !$#gene Pre-1; Pre-2 !$#map_position 12 !$#introns 23/3; 67/2; 112/3 CLASSIFICATION #superfamily transthyretin KEYWORDS albumin; liver; plasma; retinol binding; thyroid hormone; !1transport protein; vitamin A FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-147 #product transthyretin #status predicted #label MPT\ !$35,74 #binding_site thyroxine (Lys, Glu) #status !8experimental SUMMARY #length 147 #molecular-weight 15776 #checksum 7433 SEQUENCE /// ENTRY VBRT #type complete TITLE transthyretin precursor - rat ALTERNATE_NAMES prealbumin precursor; TBPA precursor ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 22-Jun-1999 ACCESSIONS A92542; S04357; A92205; A22621; I55279; I70054; A03230 REFERENCE A92542 !$#authors Dickson, P.W.; Howlett, G.J.; Schreiber, G. !$#journal J. Biol. Chem. (1985) 260:8214-8219 !$#title Rat transthyretin (prealbumin). Molecular cloning, !1nucleotide sequence, and gene expression in liver and brain. !$#cross-references MUID:85234523; PMID:3839240 !$#accession A92542 !'##molecule_type mRNA !'##residues 1-147 ##label DIC !'##cross-references GB:K03251; NID:g205983; PIDN:AAA41802.1; !1PID:g205984 REFERENCE S04357 !$#authors Duan, W.; Cole, T.; Schreiber, G. !$#journal Nucleic Acids Res. (1989) 17:3979 !$#title Cloning and nucleotide sequencing of transthyretin !1(prealbumin) cDNA from rat choroid plexus and liver. !$#cross-references MUID:89282405; PMID:2734110 !$#accession S04357 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-147 ##label DUA !'##cross-references EMBL:X14876; NID:g57424; PIDN:CAA33017.1; !1PID:g57425 REFERENCE A92205 !$#authors Navab, M.; Mallia, A.K.; Kanda, Y.; Goodman, D.S. !$#journal J. Biol. Chem. (1977) 252:5100-5106 !$#title Rat plasma prealbumin. Isolation and partial !1characterization. !$#cross-references MUID:77207131; PMID:873934 !$#accession A92205 !'##molecule_type protein !'##residues 21-35;38-50 ##label NAV REFERENCE A92526 !$#authors Sundelin, J.; Melhus, H.; Das, S.; Eriksson, U.; Lind, P.; !1Tragardh, L.; Peterson, P.A.; Rask, L. !$#journal J. Biol. Chem. (1985) 260:6481-6487 !$#title The primary structure of rabbit and rat prealbumin and a !1comparison with the tertiary structure of human prealbumin. !$#cross-references MUID:85207644; PMID:3922975 !$#accession A22621 !'##molecule_type mRNA !'##residues 1-54,'R',56-147 ##label SUN !'##cross-references GB:K03252; NID:g205981; PIDN:AAA41801.1; !1PID:g205982 REFERENCE I55279 !$#authors Fung, W. !$#journal J. Biol. Chem. (1988) 263:480-488 !$#title Structure and expression of the rat transthyretin !1(prealbumin) gene. !$#cross-references MUID:88087134; PMID:2891699 !$#accession I55279 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-23 ##label RES !'##cross-references GB:M18685; NID:g202817; PIDN:AAA40708.1; !1PID:g202821 !$#accession I70054 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 113-147 ##label RE2 !'##cross-references GB:M20246; NID:g202819; PIDN:AAA40709.1; !1PID:g202822 COMMENT Transthyretin is synthesized in the liver and the choroid !1plexus (of the brain); the concentration in the choroid !1plexus was 25 times greater than that in the liver. COMMENT The molecule of rat transthyretin is a tetramer of identical !1chains and can be assumed to have a three-dimensional !1structure similar to that of the human protein. COMMENT This protein binds retinol-binding protein at levels similar !1to, and the thyroid hormones at levels much higher than, the !1human protein. GENETICS !$#gene TT CLASSIFICATION #superfamily transthyretin KEYWORDS albumin; brain; choroid plexus; liver; plasma; retinol !1binding; thyroid hormone binding; vitamin A FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-147 #product transthyretin #status experimental #label !8MAT SUMMARY #length 147 #molecular-weight 15720 #checksum 6162 SEQUENCE /// ENTRY F64961 #type complete TITLE hypothetical protein b1970 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS F64961 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64961 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-137 ##label BLAT !'##cross-references GB:AE000288; GB:U00096; NID:g2367124; !1PIDN:AAC75036.1; PID:g1788281; UWGP:b1970 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily transthyretin SUMMARY #length 137 #molecular-weight 15460 #checksum 4079 SEQUENCE /// ENTRY H70016 #type complete TITLE conserved hypothetical protein yunM - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS H70016 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H70016 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-121 ##label KUN !'##cross-references GB:Z99120; GB:AL009126; NID:g2635613; !1PIDN:CAB15236.1; PID:g2635743 !'##experimental_source strain 168 GENETICS !$#gene yunM CLASSIFICATION #superfamily transthyretin SUMMARY #length 121 #molecular-weight 13408 #checksum 2787 SEQUENCE /// ENTRY ABHUS #type complete TITLE serum albumin precursor [validated] - human ALTERNATE_NAMES preproalbumin CONTAINS kinetensin ORGANISM #formal_name Homo sapiens #common_name man DATE 29-Jul-1981 #sequence_revision 31-Jan-1997 #text_change 17-Mar-2000 ACCESSIONS A93743; A93936; I39427; I59286; I59313; G01747; S55314; !1A91420; S06422; S36882; S17599; A45800; A03239; C38255; !1B38255; A38255; S33298; S21078; A03231 REFERENCE A93743 !$#authors Lawn, R.M.; Adelman, J.; Bock, S.C.; Franke, A.E.; Houck, !1C.M.; Najarian, R.C.; Seeburg, P.H.; Wion, K.L. !$#journal Nucleic Acids Res. (1981) 9:6103-6114 !$#title The sequence of human serum albumin cDNA and its expression !1in Escherichia coli. !$#cross-references MUID:82081882; PMID:6171778 !$#accession A93743 !'##molecule_type mRNA !'##residues 1-419,'K',421-609 ##label LAW !'##cross-references EMBL:V00495; GB:J00078; GB:L00132; GB:L00133; !1NID:g28591; PIDN:CAA23754.1; PID:g28592 REFERENCE A93936 !$#authors Dugaiczyk, A.; Law, S.W.; Dennison, O.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:71-75 !$#title Nucleotide sequence and the encoded amino acids of human !1serum albumin mRNA. !$#cross-references MUID:82105994; PMID:6275391 !$#accession A93936 !'##molecule_type mRNA !'##residues 1-120,'G',122-609 ##label DUG !'##cross-references EMBL:V00494; NID:g28589; PIDN:CAA23753.1; !1PID:g28590 REFERENCE I39427 !$#authors Urano, Y.; Watanabe, K.; Sakai, M.; Tamaoki, T. !$#journal J. Biol. Chem. (1986) 261:3244-3251 !$#title The human albumin gene. Characterization of the 5' and 3' !1flanking regions and the polymorphic gene transcripts. !$#cross-references MUID:86140099; PMID:2419329 !$#accession I39427 !'##status translation not shown !'##molecule_type DNA !'##residues 1-26 ##label URA !'##cross-references GB:M13075; NID:g178330; PIDN:AAA51688.1; !1PID:g553173 REFERENCE I59286 !$#authors Watkins, S.; Madison, J.; Galliano, M.; Minchiotti, L.; !1Putnam, F.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1994) 91:2275-2279 !$#title A nucleotide insertion and frameshift cause analbuminemia in !1an Italian family. !$#cross-references MUID:94181575; PMID:8134387 !$#accession I59286 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 282-290,'KSRFDLQ' ##label WAT !'##cross-references GB:S69192; NID:g546032; PIDN:AAB30282.1; !1PID:g546033 !'##note this frame-shift variant, designated albumin Roma, leads to !1analbuminemia REFERENCE I59313 !$#authors Madison, J.; Galliano, M.; Watkins, S.; Minchiotti, L.; !1Porta, F.; Rossi, A.; Putnam, F.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1994) 91:6476-6480 !$#title Genetic variants of human serum albumin in Italy: point !1mutants and a carboxyl-terminal variant. !$#cross-references MUID:94294404; PMID:8022807 !$#accession I59313 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 589-590,'ALPRRVKNLLLQVKLP' ##label MAD !'##cross-references GB:S70799; NID:g547231; PIDN:AAB31177.1; !1PID:g547232 !'##note this frame-shift variant is designated albumin Bazzano; four !1additional variants are reported, and a table of 47 variants !1is presented REFERENCE G08292 !$#authors Menaya, J.; Parrilla, R.; Ayuso, M.S. !$#submission submitted to the EMBL Data Library, March 1995 !$#accession G01747 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-120,'G',122-455 ##label MEN !'##cross-references EMBL:U22961; NID:g763428; PIDN:AAA64922.1; !1PID:g763431 REFERENCE S55314 !$#authors Ledgerwood, E.C.; George, P.M.; Peach, R.J.; Brennan, S.O. !$#journal Biochem. J. (1995) 308:321-325 !$#title Endoproteolytic processing of recombinant proalbumin !1variants by the yeast Kex2 protease. !$#cross-references MUID:95275251; PMID:7755581 !$#accession S55314 !'##molecule_type protein !'##residues 19-27 ##label LED REFERENCE A91420 !$#authors Meloun, B.; Moravek, L.; Kostka, V. !$#journal FEBS Lett. (1975) 58:134-137 !$#title Complete amino acid sequence of human serum albumin. !$#cross-references MUID:76187907; PMID:1225573 !$#accession A91420 !'##molecule_type protein !'##residues 25-117,'EQ',120-154,'Q',156-193,'E',195-387,'H',389-390, !1'Y',392-393,'A',395-487,'EH',490-524,'Q',526-609 ##label MEL REFERENCE S06422 !$#authors Roehr, U.; Spiteller, G.; Tripier, D. !$#journal Justus Liebigs Ann. Chem. (1988) 9:881-884 !$#title Isolation and structure elucidation of middle-molecular !1weight peptides from uremic hemofiltrates. !$#note this paper is in German, with an English abstract !$#accession S06422 !'##molecule_type protein !'##residues 25-48 ##label ROE REFERENCE S36882 !$#authors Finch, J.W.; Crouch, R.K.; Knapp, D.R.; Schey, K.L. !$#journal Arch. Biochem. Biophys. (1993) 305:595-599 !$#title Mass spectrometric identification of modifications to human !1serum albumin treated with hydrogen peroxide. !$#cross-references MUID:93384321; PMID:8373198 !$#accession S36882 !'##molecule_type protein !'##residues 45-67;141-160;311-337;469-490;570-581 ##label FIN REFERENCE S17599 !$#authors Kausler, E.; Spiteller, G. !$#journal Biol. Chem. Hoppe-Seyler (1991) 372:849-855 !$#title Bruchstuecke aus Albumin und beta(2)-Mikroglobulin - !1Bestandteile der Mittelmolekuelfraktion in Haemofiltrat. !$#cross-references MUID:92126241; PMID:1772598 !$#accession S17599 !'##molecule_type protein !'##residues 25-54;354-357;431-447 ##label KAU !'##note 49-Leu was also found REFERENCE A45800 !$#authors Carraway, R.E.; Cochrane, D.E.; Boucher, W.; Mitra, S.P. !$#journal J. Immunol. (1989) 143:1680-1684 !$#title Structures of histamine-releasing peptides formed by the !1action of acid proteases on mammalian albumin(s). !$#cross-references MUID:89341406; PMID:2474609 !$#accession A45800 !'##molecule_type protein !'##residues 166-173 ##label CAR REFERENCE A03239 !$#authors Mogard, M.H.; Kobayashi, R.; Chen, C.F.; Lee, T.D.; Reeve !1Jr., J.R.; Shively, J.E.; Walsh, J.H. !$#journal Biochem. Biophys. Res. Commun. (1986) 136:983-988 !$#title The amino acid sequence of kinetensin, a novel peptide !1isolated from pepsin-treated human plasma: homology with !1human serum albumin, neurotensin and angiotensin. !$#cross-references MUID:86242180; PMID:3087352 !$#accession A03239 !'##molecule_type protein !'##residues 166-173,'L' ##label MOG REFERENCE A38255 !$#authors Galliano, M.; Minchiotti, L.; Porta, F.; Rossi, A.; Ferri, !1G.; Madison, J.; Watkins, S.; Putnam, F.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:8721-8725 !$#title Mutations in genetic variants of human serum albumin found !1in Italy. !$#cross-references MUID:91062352; PMID:2247440 !$#accession C38255 !'##molecule_type protein !'##residues 76-111 ##label GAL1 !$#accession B38255 !'##molecule_type protein !'##residues 82-105,'K',107-110 ##label GAL2 !'##note this variant is designated albumin Vibo Valentia !$#accession A38255 !'##molecule_type protein !'##residues 76-83,'K',85-106 ##label GAL3 !'##note this variant is designated albumin Torino REFERENCE S33298 !$#authors Minchiotti, L.; Galliano, M.; Zapponi, M.C.; Tenni, R. !$#journal Eur. J. Biochem. (1993) 214:437-444 !$#title The structural characterization and bilirubin-binding !1properties of albumin Herborn, a [Lys240->Glu] albumin !1mutant. !$#cross-references MUID:93292504; PMID:8513793 !$#accession S33298 !'##molecule_type protein !'##residues 255-263,'E',265-281 ##label MIN1 !'##note this variant is designated albumin Herborn REFERENCE S21078 !$#authors Minchiotti, L.; Galliano, M.; Stoppini, M.; Ferri, G.; !1Crespeau, H.; Rochu, D.; Porta, F. !$#journal Biochim. Biophys. Acta (1992) 1119:232-238 !$#title Two alloalbumins with identical electrophoretic mobility are !1produced by differently charged amino acid substitutions. !$#cross-references MUID:92190239; PMID:1347703 !$#accession S21078 !'##molecule_type protein !'##residues 354-356,'K',358-378 ##label MIN2 !'##note this variant is designated albumin Sondrio; another variant !1Paris-2 is reported, 587-Asn REFERENCE A46756 !$#authors He, X.M.; Carter, D.C. !$#journal Nature (1992) 358:209-215 !$#title Atomic structure and chemistry of human serum albumin. !$#cross-references MUID:92334427; PMID:1630489 !$#contents annotation; X-ray crystallography, 2.8 angstroms REFERENCE A94442 !$#authors Brown, J.R.; Shockley, P.; Behrens, P.Q. !$#book The Chemistry and Physiology of the Human Plasma Proteins, !1Bing, D.H., ed., pp.23-40, Pergamon Press, New York, 1979 !$#contents annotation; three-dimensional structure and disulfide bonds REFERENCE A90930 !$#authors Saber, M.A.; Stockbauer, P.; Moravek, L.; Meloun, B. !$#journal Collect. Czech. Chem. Commun. (1977) 42:564-579 !$#title Disulfide bonds in human serum albumin. !$#contents annotation; disulfide bonds REFERENCE A90299 !$#authors Jacobsen, C. !$#journal Biochem. J. (1978) 171:453-459 !$#title Lysine residue 240 of human serum albumin is involved in !1high-affinity binding of bilirubin. !$#cross-references MUID:78186630; PMID:656055 !$#contents annotation; bilirubin-binding site REFERENCE A94408 !$#authors Peters, T.; Reed, R.G. !$#book Albumin: Structure, Biosynthesis, Function, Peters, J., and !1Sjoholm, I., eds., 11-20, 1977 !$#title Serum albumin: conformation and active sites. !$#contents annotation; binding sites REFERENCE A90028 !$#authors Harper, M.E.; Dugaiczyk, A. !$#journal Am. J. Hum. Genet. (1983) 35:565-572 !$#title Linkage of the evolutionarily-related serum albumin and !1alpha-fetoprotein genes within q11-22 of human chromosome 4. !$#cross-references MUID:83279982; PMID:6192711 !$#contents annotation; gene position REFERENCE A46755 !$#authors Walker, J.E. !$#journal FEBS Lett. (1976) 66:173-175 !$#title Lysine residue 199 of human serum albumin is modified by !1acetylsalicyclic acid. !$#cross-references MUID:76257808; PMID:955075 !$#contents annotation !$#note the nonenzymatic transfer of an acetyl group from aspirin !1(acetylsalicyclic acid) to lysine-223 is described; this !1modification affects the binding of anionic drugs REFERENCE A56294 !$#authors Bohney, J.P.; Fonda, M.L.; Feldhoff, R.C. !$#journal FEBS Lett. (1992) 298:266-268 !$#title Identification of Lys(190) as the primary binding site for !1pyridoxal 5'-phosphate in human serum albumin. !$#cross-references MUID:92183881; PMID:1544460 !$#contents annotation !$#note the nonenzymatic binding of pyridoxal phosphate to !1lysine-214 is described; in plasma, 95% of circulating !1pyridoxal phosphate is covalently bound to serum albumin and !1is protected from phosphatase activity COMMENT Serum albumin, a predominant protein in the plasma of !1adults, is synthesized in the liver as preproalbumin. It !1binds copper, nickel, calcium (weakly, at 2-3 sites), !1pyridoxal phosphate, bilirubin, protoporphyrin, long-chain !1fatty acids, prostaglandins, steroid hormones (weak bonds !1with these hormones promote their transfer across the !1membranes), thyroxine, and triiodothyronine. COMMENT A large number of variants of human serum albumin have been !1described. GENETICS !$#gene GDB:ALB !'##cross-references GDB:118990; OMIM:103600 !$#map_position 4q11-4q13 CLASSIFICATION #superfamily serum albumin; serum albumin repeat homology KEYWORDS carrier protein; duplication; metal binding; phosphoprotein; !1plasma; pyridoxal phosphate FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-24 #domain propeptide #status experimental #label PRO\ !$25-609 #product serum albumin #status experimental #label !8MPT\ !$29-202 #domain serum albumin repeat homology #label SA1\ !$166-174 #product kinetensin #status experimental #label KIP\ !$221-394 #domain serum albumin repeat homology #label SA2\ !$413-592 #domain serum albumin repeat homology #label SA3\ !$27 #binding_site copper (His) #status predicted\ !$77-86,99-115, !$114-125,148-193, !$192-201,224-270, !$269-277,289-303, !$302-313,340-385, !$384-393,416-462, !$461-472,485-501, !$500-511,538-583, !$582-591 #disulfide_bonds #status experimental\ !$214 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status experimental\ !$264 #binding_site bilirubin (Lys) #status predicted SUMMARY #length 609 #molecular-weight 69366 #checksum 9276 SEQUENCE /// ENTRY ABBOS #type complete TITLE serum albumin precursor [validated] - bovine ALTERNATE_NAMES 67K protein; preproalbumin ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 24-Apr-1984 #sequence_revision 30-Sep-1993 #text_change 18-Aug-2000 ACCESSIONS A38885; A36401; A91258; B60808; S10780; D45800; A26693; !1A90309; A91458; A94551; S55232; A03232 REFERENCE A38885 !$#authors Holowachuk, E.W.; Stoltenborg, J.K.; Reed, R.G.; Peters Jr., !1T. !$#submission submitted to the EMBL Data Library, August 1991 !$#description Bovine serum albumin: cDNA sequence and expression. !$#accession A38885 !'##molecule_type mRNA !'##residues 1-607 ##label HOL !'##cross-references EMBL:M73215 REFERENCE A36401 !$#authors Hirayama, K.; Akashi, S.; Furuya, M.; Fukuhara, K. !$#journal Biochem. Biophys. Res. Commun. (1990) 173:639-646 !$#title Rapid confirmation and revision of the primary structure of !1bovine serum albumin by ESIMS and Frit-FAB LC/MS. !$#cross-references MUID:91083649; PMID:2260975 !$#accession A36401 !'##molecule_type protein !'##residues 25-41,'H',43-189,'E',191-213,'T',215-323,'D',325-393,'TS', !1396-607 ##label HIR REFERENCE A91258 !$#authors MacGillivray, R.T.A.; Chung, D.W.; Davie, E.W. !$#journal Eur. J. Biochem. (1979) 98:477-485 !$#title Biosynthesis of bovine plasma proteins in a cell-free !1system. !$#cross-references MUID:80024278; PMID:488109 !$#accession A91258 !'##molecule_type protein !'##residues 1-32 ##label MAG REFERENCE A60808 !$#authors Hsieh, J.C.; Lin, F.P.; Tam, M.F. !$#journal Anal. Biochem. (1988) 170:1-8 !$#title Electroblotting onto glass-fiber filter from an analytical !1isoelectrofocusing gel: a preparative method for isolating !1proteins for N-terminal microsequencing. !$#cross-references MUID:88267456; PMID:3389500 !$#accession B60808 !'##molecule_type protein !'##residues 25-41 ##label HSI REFERENCE S10780 !$#authors Strawich, E.; Glimcher, M.J. !$#journal Eur. J. Biochem. (1990) 191:47-56 !$#title Tooth 'enamelins' identified mainly as serum proteins. Major !1'enamelin' is albumin. !$#cross-references MUID:90336641; PMID:2379503 !$#accession S10780 !'##molecule_type protein !'##residues 25-41,'H',43-57,59-64 ##label STR REFERENCE A45800 !$#authors Carraway, R.E.; Cochrane, D.E.; Boucher, W.; Mitra, S.P. !$#journal J. Immunol. (1989) 143:1680-1684 !$#title Structures of histamine-releasing peptides formed by the !1action of acid proteases on mammalian albumin(s). !$#cross-references MUID:89341406; PMID:2474609 !$#accession D45800 !'##molecule_type protein !'##residues 163-172 ##label CAR REFERENCE A26693 !$#authors Carraway, R.E.; Mitra, S.P.; Cochrane, D.E. !$#journal J. Biol. Chem. (1987) 262:5968-5973 !$#title Structure of a biologically active neurotensin-related !1peptide obtained from pepsin-treated albumin(s). !$#cross-references MUID:87194805; PMID:2437111 !$#accession A26693 !'##molecule_type protein !'##residues 165-172,'L' ##label CA2 REFERENCE A90309 !$#authors Reed, R.G.; Putnam, F.W.; Peters Jr., T. !$#journal Biochem. J. (1980) 191:867-868 !$#title Sequence of residues 400-403 of bovine serum albumin. !$#cross-references MUID:82023364; PMID:7283978 !$#accession A90309 !'##molecule_type protein !'##residues 402-433 ##label REE REFERENCE A91458 !$#authors Brown, J.R. !$#journal Fed. Proc. (1975) 34:591 !$#title Structure of bovine serum albumin. !$#accession A91458 !'##molecule_type protein !'##residues 25-41,'H',43-117,'EQ',120-179,181-189,'E',191-194,'A', !1196-213,'T',215-288,'BBZB',293-301,'K',303,'PC',306-323,'D', !1325-393,'TS',396-412,'ZB',415,'BZ',418-424;429-492,'ES', !1495-607 ##label BRO REFERENCE A94551 !$#authors Brown, J.R. !$#submission submitted to the Atlas, April 1975 !$#accession A94551 !'##molecule_type protein !'##residues 190-195 ##label BR2 REFERENCE A91457 !$#authors Brown, J.R. !$#journal Fed. Proc. (1974) 33:1389 !$#contents annotation; disulfide bonds REFERENCE S55232 !$#authors Werlen, R.C.; Offord, R.E.; Rose, K. !$#journal Biochem. J. (1994) 302:907-911 !$#title Preparation and characterization of novel substrates of !1insulin proteinase (EC 3.4.99.45). !$#cross-references MUID:95031935; PMID:7945219 !$#accession S55232 !'##status preliminary !'##molecule_type protein !'##residues 529-536;569-572 ##label WER CLASSIFICATION #superfamily serum albumin; serum albumin repeat homology KEYWORDS carrier protein; copper binding; duplication; plasma FEATURE !$1-18 #domain signal sequence #status experimental #label !8SIG\ !$19-24 #domain propeptide #status experimental #label PRO\ !$25-607 #product serum albumin #status experimental #label !8MPT\ !$29-201 #domain serum albumin repeat homology #label SA1\ !$220-393 #domain serum albumin repeat homology #label SA2\ !$412-591 #domain serum albumin repeat homology #label SA3\ !$27 #binding_site copper (His) #status predicted\ !$77-86,99-115, !$114-125,147-192, !$191-200,223-269, !$268-276,288-302, !$301-312,339-384, !$383-392,415-461, !$460-471,484-500, !$499-510,537-582, !$581-590 #disulfide_bonds #status experimental SUMMARY #length 607 #molecular-weight 69270 #checksum 9616 SEQUENCE /// ENTRY ABSHS #type complete TITLE serum albumin precursor - sheep ORGANISM #formal_name Ovis orientalis aries, Ovis ammon aries #common_name domestic sheep DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 22-Jun-1999 ACCESSIONS S06936 REFERENCE S06936 !$#authors Brown, W.M.; Dziegielewska, K.M.; Foreman, R.C.; Saunders, !1N.R. !$#journal Nucleic Acids Res. (1989) 17:10495 !$#title Nucleotide and deduced amino acid sequence of sheep serum !1albumin. !$#cross-references MUID:90098888; PMID:2602160 !$#accession S06936 !'##molecule_type mRNA !'##residues 1-607 ##label BRO !'##cross-references EMBL:X17055; NID:g1386; PIDN:CAA34903.1; PID:g1387 COMMENT Serum albumin is synthesized in the liver as preproalbumin. !1It binds copper, nickel, calcium (weakly, at 2-3 sites), !1bilirubin and protoporphyrin, long-chain fatty acids, !1prostaglandins, steroid hormones (weak bonds with these !1hormones promote their transfer across the membranes), !1thyroxine, and triiodothyronine. CLASSIFICATION #superfamily serum albumin; serum albumin repeat homology KEYWORDS carrier protein; duplication; metal binding; plasma FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-24 #domain propeptide #status predicted #label PRO\ !$25-607 #product serum albumin #status predicted #label MAT\ !$29-201 #domain serum albumin repeat homology #label SA1\ !$220-393 #domain serum albumin repeat homology #label SA2\ !$412-591 #domain serum albumin repeat homology #label SA3\ !$27 #binding_site copper (His) #status predicted\ !$77-86,99-115, !$114-125,147-192, !$191-200,223-269, !$268-276,288-302, !$301-312,339-384, !$383-392,415-461, !$460-471,484-500, !$499-510,537-582, !$581-590 #disulfide_bonds #status predicted\ !$263 #binding_site bilirubin (Lys) #status predicted SUMMARY #length 607 #molecular-weight 69188 #checksum 6318 SEQUENCE /// ENTRY ABPGS #type fragment TITLE serum albumin precursor - pig (fragment) ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 22-Jun-1999 ACCESSIONS S01382; A61006 REFERENCE S01382 !$#authors Weinstock, J.; Baldwin, G.S. !$#journal Nucleic Acids Res. (1988) 16:9045 !$#title Nucleotide sequence of porcine liver albumin. !$#cross-references MUID:89016582; PMID:3174440 !$#accession S01382 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-605 ##label WEI !'##cross-references EMBL:X12422; NID:g1875; PIDN:CAA30970.1; !1PID:g833798 REFERENCE A61006 !$#authors Limeback, H.; Sakarya, H.; Chu, W.; Mackinnon, M. !$#journal J. Bone Miner. Res. (1989) 4:235-241 !$#title Serum albumin and its acid hydrolysis peptides dominate !1preparations of mineral-bound enamel proteins. !$#cross-references MUID:89269769; PMID:2728927 !$#accession A61006 !'##molecule_type protein !'##residues 23-51,'X',53-54;'XXXGY',146,'E',148,'E',150-151,'XVN',155 !1##label LIM !'##experimental_source dental enamel !'##note albumin and other serum proteins are also found in bone COMMENT Serum albumin is synthesized in the liver as preproalbumin. !1It binds copper, nickel, calcium (weakly, at 2-3 sites), !1bilirubin and protoporphyrin, long-chain fatty acids, !1prostaglandins, steroid hormones (weak bonds with these !1hormones promote their transfer across the membranes), !1thyroxine, and triiodothyronine. CLASSIFICATION #superfamily serum albumin; serum albumin repeat homology KEYWORDS carrier protein; duplication; metal binding; plasma FEATURE !$1-16 #domain signal sequence (fragment) #status predicted !8#label SIG\ !$17-22 #domain propeptide #status predicted #label PRO\ !$23-605 #product serum albumin #status predicted #label MAT\ !$27-199 #domain serum albumin repeat homology #label SA1\ !$218-391 #domain serum albumin repeat homology #label SA2\ !$410-589 #domain serum albumin repeat homology #label SA3\ !$75-84,97-113, !$112-123,145-190, !$189-198,221-267, !$266-274,286-300, !$299-310,337-382, !$381-390,413-459, !$458-469,482-498, !$497-508,535-580, !$579-588 #disulfide_bonds #status predicted\ !$261 #binding_site bilirubin (Lys) #status predicted SUMMARY #length 605 #checksum 8205 SEQUENCE /// ENTRY ABHOS #type complete TITLE serum albumin precursor - horse ORGANISM #formal_name Equus caballus #common_name domestic horse DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 22-Jun-1999 ACCESSIONS S34053 REFERENCE S34053 !$#authors Ho, J.X.; Holowachuk, E.W.; Norton, E.J.; Twigg, P.D.; !1Carter, D.C. !$#journal Eur. J. Biochem. (1993) 215:205-212 !$#title X-ray and primary structure of horse serum albumin (Equus !1caballus) at 0.27-nm resolution. !$#cross-references MUID:93345495; PMID:8344282 !$#accession S34053 !'##molecule_type mRNA !'##residues 1-607 ##label HOA !'##cross-references GB:X74045; NID:g399671; PIDN:CAA52194.1; !1PID:g399672 COMMENT Serum albumin is synthesized in the liver as preproalbumin. !1It binds copper, nickel, calcium (weakly, at 2-3 sites), !1bilirubin and protoporphyrin, long-chain fatty acids, !1prostaglandins, steroid hormones (weak bonds with these !1hormones promote their transfer across the membranes), !1thyroxine, and triiodothyronine. CLASSIFICATION #superfamily serum albumin; serum albumin repeat homology KEYWORDS carrier protein; duplication; metal binding; plasma FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-24 #domain propeptide #status predicted #label PRO\ !$25-607 #product serum albumin #status predicted #label MAT\ !$29-201 #domain serum albumin repeat homology #label SA1\ !$220-393 #domain serum albumin repeat homology #label SA2\ !$412-591 #domain serum albumin repeat homology #label SA3\ !$27 #binding_site copper (His) #status predicted\ !$77-86,99-115, !$114-125,147-192, !$191-200,223-269, !$268-276,288-302, !$301-312,339-384, !$383-392,415-461, !$460-471,484-500, !$499-510,537-582, !$581-590 #disulfide_bonds #status predicted\ !$263 #binding_site bilirubin (Lys) #status predicted SUMMARY #length 607 #molecular-weight 68598 #checksum 307 SEQUENCE /// ENTRY ABRTS #type complete TITLE serum albumin precursor - rat ALTERNATE_NAMES preproalbumin ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-May-1979 #sequence_revision 31-May-1979 #text_change 22-Jun-1999 ACCESSIONS A93872; A92211; A91946; A91940; C45800; I57621; A03233 REFERENCE A93872 !$#authors Sargent, T.D.; Yang, M.; Bonner, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:243-246 !$#title Nucleotide sequence of cloned rat serum albumin messenger !1RNA. !$#cross-references MUID:81223722; PMID:7017712 !$#accession A93872 !'##molecule_type mRNA !'##residues 1-608 ##label SAR !'##cross-references GB:V01222; GB:J00698; NID:g55627; PIDN:CAA24532.1; !1PID:g55628 REFERENCE A92211 !$#authors Strauss, A.W.; Bennett, C.D.; Donohue, A.M.; Rodkey, J.A.; !1Alberts, A.W. !$#journal J. Biol. Chem. (1977) 252:6846-6855 !$#title Rat liver pre-proalbumin: complete amino acid sequence of !1the pre-piece. Analysis of the direct translation product of !1albumin messenger RNA. !$#cross-references MUID:77249657; PMID:893447 !$#note cleavages during protein maturation !$#accession A92211 !'##molecule_type protein !'##residues 1-38 ##label STR REFERENCE A91946 !$#authors Isemura, S.; Ikenaka, T. !$#journal J. Biochem. (1978) 83:35-48 !$#title Amino acid sequences of fragments I and II obtained by !1cyanogen bromide cleavage of rat serum albumin. !$#cross-references MUID:78109429; PMID:564345 !$#accession A91946 !'##molecule_type protein !'##residues 25-222 ##label IS1 REFERENCE A91940 !$#authors Isemura, S.; Ikenaka, T. !$#journal J. Biochem. (1976) 79:1183-1196 !$#title Fragmentation of rat serum albumin by cyanogen bromide !1cleavage and the amino acid sequences of four fragments. !$#cross-references MUID:76260153; PMID:956149 !$#accession A91940 !'##molecule_type protein !'##residues 223-288;572-608 ##label IS2 !'##note 262-Leu was also found REFERENCE A90758 !$#authors Aoyagi, Y.; Ikenaka, T.; Ichida, F. !$#journal Cancer Res. (1978) 38:3483-3486 !$#title Copper(II)-binding ability of human alpha-fetoprotein. !$#cross-references MUID:79001617; PMID:80265 !$#contents annotation; copper binding REFERENCE A45800 !$#authors Carraway, R.E.; Cochrane, D.E.; Boucher, W.; Mitra, S.P. !$#journal J. Immunol. (1989) 143:1680-1684 !$#title Structures of histamine-releasing peptides formed by the !1action of acid proteases on mammalian albumin(s). !$#cross-references MUID:89341406; PMID:2474609 !$#accession C45800 !'##status preliminary !'##molecule_type protein !'##residues 166-173 ##label CAR REFERENCE I57621 !$#authors Heard, J. !$#journal Mol. Cell. Biol. (1987) 7:2425-2434 !$#title Determinants of rat albumin promoter tissue specificity !1analyzed by an improved transient expression system. !$#cross-references MUID:87286876; PMID:3475566 !$#accession I57621 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-5 ##label RES !'##cross-references GB:M16825; NID:g202828; PIDN:AAA40712.1; !1PID:g554412 CLASSIFICATION #superfamily serum albumin; serum albumin repeat homology KEYWORDS carrier protein; duplication; metal binding; plasma FEATURE !$1-18 #domain signal sequence #status experimental #label !8SIG\ !$19-24 #domain propeptide #status experimental #label PRO\ !$25-608 #product serum albumin #status experimental #label !8MAT\ !$29-202 #domain serum albumin repeat homology #label SA1\ !$221-394 #domain serum albumin repeat homology #label SA2\ !$413-592 #domain serum albumin repeat homology #label SA3\ !$27 #binding_site copper (His) #status experimental\ !$77-86,99-115, !$114-125,148-193, !$192-201,224-270, !$269-277,289-303, !$302-313,340-385, !$384-393,416-462, !$461-472,485-501, !$500-511,538-583, !$582-591 #disulfide_bonds #status predicted SUMMARY #length 608 #molecular-weight 68718 #checksum 6355 SEQUENCE /// ENTRY ABCHS #type complete TITLE serum albumin precursor - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 22-Jun-1999 ACCESSIONS S15571; A05078; A13451 REFERENCE S15571 !$#authors Cassady, A.I.; Salklld, C.K.; Baverstock, P.; Wallace, J.C. !$#submission submitted to the EMBL Data Library, July 1991 !$#accession S15571 !'##molecule_type mRNA !'##residues 1-615 ##label CAS !'##cross-references EMBL:X60688; NID:g63747; PIDN:CAA43098.1; !1PID:g63748 REFERENCE A05078 !$#authors Hache, R.J.G.; Wiskocil, R.; Vasa, M.; Roy, R.N.; Lau, !1P.C.K.; Deeley, R.G. !$#journal J. Biol. Chem. (1983) 258:4556-4564 !$#title The 5' noncoding and flanking regions of the avian very low !1density apolipoprotein II and serum albumin genes. !1Homologies with the egg white protein genes. !$#cross-references MUID:83161037; PMID:6187737 !$#accession A05078 !'##molecule_type DNA !'##residues 1-28 ##label HAC !'##cross-references GB:V00381; NID:g63038; PIDN:CAA23680.1; PID:g63039 REFERENCE A13451 !$#authors Rosen, A.M.; Geller, D.M. !$#journal Biochem. Biophys. Res. Commun. (1977) 78:1060-1066 !$#title Chicken microsomal albumin: amino terminal sequence of !1chicken proalbumin. !$#cross-references MUID:78019943; PMID:911327 !$#accession A13451 !'##molecule_type protein !'##residues 19-23,'M',25-30 ##label ROS COMMENT Serum albumin is synthesized in the liver as preproalbumin. !1It binds copper, nickel, calcium (weakly, at 2-3 sites), and !1protoporphyrin, long-chain fatty acids, prostaglandins, !1steroid hormones (weak bonds with these hormones promote !1their transfer across the membranes), thyroxine, and !1triiodothyronine. CLASSIFICATION #superfamily serum albumin; serum albumin repeat homology KEYWORDS carrier protein; duplication; metal binding; plasma FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-26 #domain propeptide #status predicted #label PRO\ !$27-613 #product serum albumin #status predicted #label MAT\ !$32-206 #domain serum albumin repeat homology #label SA1\ !$225-398 #domain serum albumin repeat homology #label SA2\ !$417-596 #domain serum albumin repeat homology #label SA3\ !$30 #binding_site copper (His) #status predicted\ !$80-89,102-118, !$117-128,152-197, !$196-205,228-274, !$273-281,293-307, !$306-317,344-389, !$388-397,420-466, !$465-476,489-505, !$504-515,542-587, !$586-595 #disulfide_bonds #status predicted SUMMARY #length 615 #molecular-weight 69918 #checksum 4822 SEQUENCE /// ENTRY ABXL68 #type complete TITLE 68K serum albumin precursor - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 28-Apr-1995 ACCESSIONS A41682; S02692 REFERENCE A41682 !$#authors Moskaitis, J.E.; Sargent, T.D.; Smith Jr., L.H.; Pastori, !1R.L.; Schoenberg, D.R. !$#journal Mol. Endocrinol. (1989) 3:464-473 !$#title Xenopus laevis serum albumin: sequence of the complementary !1deoxyribonucleic acids encoding the 68- and 74-kilodalton !1peptides and the regulation of albumin gene expression by !1thyroid hormone during development. !$#cross-references MUID:89313788; PMID:2747653 !$#accession A41682 !'##molecule_type mRNA !'##residues 1-608 ##label MOS !'##cross-references GB:M18350 REFERENCE S02692 !$#authors Schorpp, M.; Doebbeling, U.; Wagner, U.; Ryffel, G.U. !$#journal J. Mol. Biol. (1988) 199:83-93 !$#title 5'-flanking and 5'-proximal exon regions of the two Xenopus !1albumin genes. Deletion analysis of constitutive promoter !1function. !$#cross-references MUID:88172470; PMID:2451026 !$#accession S02692 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-48 ##label SCH !'##cross-references EMBL:Z26825 COMMENT Serum albumin is synthesized in the liver as preproalbumin. !1It binds copper, nickel, calcium (weakly, at 2-3 sites), and !1protoporphyrin, long-chain fatty acids, prostaglandins, !1steroid hormones (weak bonds with these hormones promote !1their transfer across the membranes), thyroxine, and !1triiodothyronine. GENETICS !$#introns 27/1 CLASSIFICATION #superfamily serum albumin; serum albumin repeat homology KEYWORDS carrier protein; duplication; metal binding; plasma FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-24 #domain propeptide #status predicted #label PRO\ !$25-608 #product 68K serum albumin #status predicted #label !8MAT\ !$32-202 #domain serum albumin repeat homology #label SA1\ !$221-394 #domain serum albumin repeat homology #label SA2\ !$413-592 #domain serum albumin repeat homology #label SA3\ !$30 #binding_site copper (His) #status predicted\ !$80-89,102-118, !$117-128,148-193, !$192-201,224-270, !$269-277,289-303, !$302-313,340-385, !$384-393,416-462, !$461-472,485-501, !$500-511,538-583, !$582-591 #disulfide_bonds #status predicted SUMMARY #length 608 #molecular-weight 70784 #checksum 5756 SEQUENCE /// ENTRY ABXL72 #type complete TITLE 74K albumin precursor - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 22-Jun-1999 ACCESSIONS B41682; S02693; A05288 REFERENCE A41682 !$#authors Moskaitis, J.E.; Sargent, T.D.; Smith Jr., L.H.; Pastori, !1R.L.; Schoenberg, D.R. !$#journal Mol. Endocrinol. (1989) 3:464-473 !$#title Xenopus laevis serum albumin: sequence of the complementary !1deoxyribonucleic acids encoding the 68- and 74-kilodalton !1peptides and the regulation of albumin gene expression by !1thyroid hormone during development. !$#cross-references MUID:89313788; PMID:2747653 !$#accession B41682 !'##molecule_type mRNA !'##residues 3-607 ##label MOS !'##cross-references GB:M21442; NID:g213930; PIDN:AAA49637.1; !1PID:g213931 REFERENCE S02692 !$#authors Schorpp, M.; Doebbeling, U.; Wagner, U.; Ryffel, G.U. !$#journal J. Mol. Biol. (1988) 199:83-93 !$#title 5'-flanking and 5'-proximal exon regions of the two Xenopus !1albumin genes. Deletion analysis of constitutive promoter !1function. !$#cross-references MUID:88172470; PMID:2451026 !$#accession S02693 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-48 ##label SCH !'##cross-references EMBL:Z26826 REFERENCE A05288 !$#authors Wolffe, A.P.; Glover, J.F.; Martin, S.C.; Tenniswood, !1M.P.R.; Williams, J.L.; Tata, J.R. !$#journal Eur. J. Biochem. (1985) 146:489-496 !$#title Deinduction of transcription of Xenopus 74-kDa albumin genes !1and destabilization of mRNA by estrogen in vivo and in !1hepatocyte cultures. !$#cross-references MUID:85126974; PMID:3971963 !$#accession A05288 !'##molecule_type mRNA !'##residues 459-502,'L',504-557 ##label WOL !'##cross-references GB:M28276 !'##note the authors translated the codon TAT for residue 63 as Thr COMMENT Serum albumin is synthesized in the liver as preproalbumin. !1It binds copper, nickel, calcium (weakly, at 2-3 sites), and !1protoporphyrin, long-chain fatty acids, prostaglandins, !1steroid hormones (weak bonds with these hormones promote !1their transfer across the membranes), thyroxine, and !1triiodothyronine. GENETICS !$#introns 27/1 CLASSIFICATION #superfamily serum albumin; serum albumin repeat homology KEYWORDS carrier protein; duplication; glycoprotein; metal binding; !1plasma FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-24 #domain propeptide #status predicted #label PRO\ !$25-607 #product 74K serum albumin #status predicted #label !8MAT\ !$32-201 #domain serum albumin repeat homology #label SA1\ !$220-393 #domain serum albumin repeat homology #label SA2\ !$412-591 #domain serum albumin repeat homology #label SA3\ !$30 #binding_site copper (His) #status predicted\ !$80-88,101-117, !$116-127,147-192, !$191-200,223-269, !$268-276,288-302, !$301-312,339-384, !$383-392,415-461, !$460-471,484-500, !$499-510,537-582, !$581-590 #disulfide_bonds #status predicted\ !$256 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 607 #molecular-weight 70382 #checksum 91 SEQUENCE /// ENTRY ABONS1 #type complete TITLE serum albumin 1 precursor - Atlantic salmon ORGANISM #formal_name Salmo salar #common_name Atlantic salmon DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 22-Jun-1999 ACCESSIONS A36238; S13079 REFERENCE A36238 !$#authors Byrnes, L.; Gannon, F. !$#journal DNA Cell Biol. (1990) 9:647-655 !$#title Atlantic salmon (Salmo salar) serum albumin: cDNA sequence, !1evolution, and tissue expression. !$#cross-references MUID:91083837; PMID:2261082 !$#accession A36238 !'##molecule_type mRNA !'##residues 1-608 ##label BYR !'##cross-references GB:X52397; NID:g64375; PIDN:CAA36643.1; PID:g64376 COMMENT Serum albumin is synthesized in the liver as preproalbumin. !1It binds copper, nickel, calcium (weakly, at 2-3 sites), and !1protoporphyrin, long-chain fatty acids, prostaglandins, !1steroid hormones (weak bonds with these hormones promote !1their transfer across the membranes), thyroxine, and !1triiodothyronine. CLASSIFICATION #superfamily serum albumin; serum albumin repeat homology KEYWORDS carrier protein; duplication; plasma FEATURE !$1-14 #domain signal sequence #status predicted #label SIG\ !$15-18 #domain propeptide #status predicted #label PRO\ !$19-608 #product serum albumin #status predicted #label MAT\ !$23-196 #domain serum albumin repeat homology #label SA1\ !$215-390 #domain serum albumin repeat homology #label SA2\ !$411-591 #domain serum albumin repeat homology #label SA3\ !$26-72,71-80,93-108, !$107-118,142-187, !$186-195,218-264, !$263-271,283-299, !$298-309,336-381, !$380-389,414-460, !$459-471,484-500, !$499-510,537-582, !$581-590 #disulfide_bonds #status predicted SUMMARY #length 608 #molecular-weight 67151 #checksum 8004 SEQUENCE /// ENTRY ABONS2 #type complete TITLE serum albumin 2 precursor - Atlantic salmon ORGANISM #formal_name Salmo salar #common_name Atlantic salmon DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 22-Jun-1999 ACCESSIONS A46757; S30594 REFERENCE A46757 !$#authors Byrnes, L. !$#submission submitted to the EMBL Data Library, June 1991 !$#accession A46757 !'##molecule_type mRNA !'##residues 1-608 ##label BYR !'##cross-references EMBL:X60776; NID:g64349; PIDN:CAA43187.1; !1PID:g64350 REFERENCE S30594 !$#authors Byrnes, L.; Gannon, F. !$#journal Gene (1992) 120:319-320 !$#title Sequence analysis of a second cDNA encoding Atlantic salmon !1(Salmo salar) serum albumin. !$#cross-references MUID:93013056; PMID:1398147 !$#contents annotation !$#note only a list of differences from sequence A36238 is shown COMMENT Serum albumin is synthesized in the liver as preproalbumin. !1It binds copper, nickel, calcium (weakly, at 2-3 sites), and !1protoporphyrin, long-chain fatty acids, prostaglandins, !1steroid hormones (weak bonds with these hormones promote !1their transfer across the membranes), thyroxine, and !1triiodothyronine. CLASSIFICATION #superfamily serum albumin; serum albumin repeat homology KEYWORDS carrier protein; duplication; plasma FEATURE !$1-14 #domain signal sequence #status predicted #label SIG\ !$15-18 #domain propeptide #status predicted #label PRO\ !$19-608 #product serum albumin #status predicted #label MAT\ !$23-196 #domain serum albumin repeat homology #label SA1\ !$215-390 #domain serum albumin repeat homology #label SA2\ !$411-591 #domain serum albumin repeat homology #label SA3\ !$26-72,71-80,93-108, !$107-118,142-187, !$186-195,218-264, !$263-271,283-299, !$298-309,336-381, !$380-389,414-460, !$459-471,484-500, !$499-510,537-582, !$581-590 #disulfide_bonds #status predicted SUMMARY #length 608 #molecular-weight 67058 #checksum 7069 SEQUENCE /// ENTRY A54906 #type complete TITLE afamin precursor - human ALTERNATE_NAMES alpha-albumin ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 17-Mar-2000 ACCESSIONS A54906; JC6143; S68554; S78082; I39425 REFERENCE A54906 !$#authors Lichenstein, H.S.; Lyons, D.E.; Wurfel, M.M.; Johnson, D.A.; !1McGinley, M.D.; Leidli, J.C.; Trollinger, D.B.; Mayer, J.P.; !1Wright, S.D.; Zukowski, M.M. !$#journal J. Biol. Chem. (1994) 269:18149-18154 !$#title Afamin is a new member of the albumin, alpha-fetoprotein, !1and vitamin D-binding protein gene family. !$#cross-references MUID:94299534; PMID:7517938 !$#accession A54906 !'##status preliminary !'##molecule_type mRNA !'##residues 1-599 ##label LIC !'##cross-references GB:L32140; NID:g533885; PIDN:AAA21612.1; !1PID:g547402 REFERENCE JC6143 !$#authors Mishio, H.; Dugaiczyk, A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1996) 93:7557-7561 !$#title Complete structure of the human alpha-albumin gene, a new !1member of the serum albumin multigene family. !$#cross-references MUID:96353855; PMID:8755513 !$#accession JC6143 !'##molecule_type DNA !'##residues 1-599 ##label MIS !'##cross-references GB:U51243; NID:g1418261; PIDN:AAC50720.1; !1PID:g1418262 REFERENCE S68554 !$#authors Nishio, H.; Heiskanen, M.; Palotie, A.; Belanger, L.; !1Dugaiczyk, A. !$#journal J. Mol. Biol. (1996) 259:113-119 !$#title Tandem arrangement of the human serum albumin multigene !1family in the sub-centromeric region of 4q: evolution and !1chromosomal direction of transcription. !$#cross-references MUID:96240683; PMID:8648639 !$#accession S68554 !'##molecule_type DNA !'##residues 1-29 ##label NIW !'##cross-references GB:U51243; NID:g1418261 !'##note neither the complete nucleic acid sequence nor the complete !1translation are shown REFERENCE S78082 !$#authors Nishio, H.; Heiskanen, M.; Palotie, A.; Belanger, L.; !1Dugaiczyk, A. !$#submission submitted to the EMBL Data Library, March 1996 !$#description Tandem arrangement of the human serum albumin multigene !1family in the sub-centromeric region of 4q: evolution and !1chromosomal direction of transcription. !$#accession S78082 !'##molecule_type DNA !'##residues 1-599 ##label NIS !'##cross-references EMBL:U51243; NID:g1418261; PIDN:AAC50720.1; !1PID:g1418262 REFERENCE I39424 !$#authors Allard, D.; Gilbert, S.; Lamontagne, A.; Hamel, D.; !1Belanger, L. !$#journal Gene (1995) 153:287-288 !$#title Identification of rat alpha-albumin and cDNA cloning of its !1human ortholog. !$#cross-references MUID:95180738; PMID:7875606 !$#accession I39425 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 105-207 ##label ALL !'##cross-references GB:L35497; NID:g530131; PIDN:AAA68198.1; !1PID:g857676 GENETICS !$#gene GDB:AFM !'##cross-references GDB:376475; OMIM:104145 !$#map_position 4q11-4q13 !$#introns 30/1; 46/2; 90/3; 161/2; 205/3; 238/2; 281/3; 353/2; 397/3; !1430/2; 474/3; 549/2; 593/3 CLASSIFICATION #superfamily serum albumin; serum albumin repeat homology KEYWORDS extracellular protein; glycoprotein; plasma FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-599 #product afamin #status predicted #label MAT\ !$29-202 #domain serum albumin repeat homology #label SA1\ !$221-394 #domain serum albumin repeat homology #label SA2\ !$413-590 #domain serum albumin repeat homology #label SA3\ !$33,109,402,488 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 599 #molecular-weight 69068 #checksum 5918 SEQUENCE /// ENTRY FPHU #type complete TITLE alpha-fetoprotein precursor [validated] - human ALTERNATE_NAMES AFP; alpha-1-fetoprotein; alpha-fetoglobulin ORGANISM #formal_name Homo sapiens #common_name man DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 08-Dec-2000 ACCESSIONS A26624; S37655; A93961; A91497; A23699; A61480; A90624; !1A90757; A93042; A03234; S31499 REFERENCE A26624 !$#authors Gibbs, P.E.M.; Zielinski, R.; Boyd, C.; Dugaiczyk, A. !$#journal Biochemistry (1987) 26:1332-1343 !$#title Structure, polymorphism, and novel repeated DNA elements !1revealed by a complete sequence of the human !1alpha-fetoprotein gene. !$#cross-references MUID:87185438; PMID:2436661 !$#accession A26624 !'##molecule_type DNA !'##residues 1-609 ##label GIB !'##cross-references GB:M16110; NID:g773678; PIDN:AAB58754.1; !1PID:g178236 REFERENCE S37655 !$#authors McVey, J.H.; Michaelides, K.; Hansen, L.P.; Ferguson-Smith, !1M.; Tilghman, S.; Krumlauf, R.; Tuddenham, E.G.D. !$#journal Hum. Mol. Genet. (1993) 2:379-384 !$#title A G->A substitution in an HNF I binding site in the human !1alpha-fetoprotein gene is associated with hereditary !1persistence of alpha-fetoprotein (HPAFP). !$#cross-references MUID:93278385; PMID:7684942 !$#accession S37655 !'##molecule_type DNA !'##residues 1-28 ##label MCV !'##cross-references EMBL:Z19532; NID:g28527; PIDN:CAA79592.1; !1PID:g28528 !'##note the authors translated the codon TAT for residue 26 as Thr REFERENCE A93961 !$#authors Morinaga, T.; Sakai, M.; Wegmann, T.G.; Tamaoki, T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:4604-4608 !$#title Primary structures of human alpha-fetoprotein and its mRNA. !$#cross-references MUID:83273664; PMID:6192439 !$#accession A93961 !'##molecule_type mRNA !'##residues 1-609 ##label MOR !'##cross-references GB:J00077; NID:g311348; PIDN:CAA24758.1; PID:g31351 REFERENCE A91497 !$#authors Beattie, W.G.; Dugaiczyk, A. !$#journal Gene (1982) 20:415-422 !$#title Structure and evolution of human alpha-fetoprotein deduced !1from partial sequence of cloned cDNA. !$#cross-references MUID:83158778; PMID:6187626 !$#accession A91497 !'##molecule_type mRNA !'##residues 429-556 ##label BEA !'##cross-references GB:J00076 REFERENCE A23699 !$#authors Pucci, P.; Siciliano, R.; Malorni, A.; Marino, G.; Tecce, !1M.F.; Ceccarini, C.; Terrana, B. !$#journal Biochemistry (1991) 30:5061-5066 !$#title Human alpha-fetoprotein primary structure: a mass !1spectrometric study. !$#cross-references MUID:91242409; PMID:1709810 !$#accession A23699 !'##molecule_type protein !'##residues 19-45;60-97;102-107;122-184;187-249;255-489;507-609 ##label !1PUC REFERENCE A61480 !$#authors Tecce, M.F.; Terrana, B.; Giuliani, M.M.; Ceccarini, C. !$#journal J. Nucl. Med. Allied Sci. (1990) 34:213-216 !$#title Characterization of in vitro expressed human !1alpha-fetoprotein as highly reproducible reference material !1for clinical immunoassays. !$#cross-references MUID:91225826; PMID:1709209 !$#accession A61480 !'##molecule_type protein !'##residues 19-45;63-97;102-107;122-184;187-249;255-489;507-609 ##label !1TEC REFERENCE A90624 !$#authors Yachnin, S.; Hsu, R.; Heinrikson, R.L.; Miller, J.B. !$#journal Biochim. Biophys. Acta (1977) 493:418-428 !$#title Studies on human alpha-fetoprotein. Isolation and !1characterization of monomeric and polymeric forms and !1amino-terminal sequence analysis. !$#cross-references MUID:77242506; PMID:70228 !$#accession A90624 !'##molecule_type protein !'##residues 'S',20-22,'S',24-35 ##label YAC !'##note dimeric and trimeric forms have been found in addition to the !1monomeric form REFERENCE A90757 !$#authors Aoyagi, Y.; Ikenaka, T.; Ichida, F. !$#journal Cancer Res. (1977) 37:3663-3667 !$#title Comparative chemical structure of human alpha-fetoproteins !1from fetal serum and from ascites fluid of a patient with !1hepatoma. !$#cross-references MUID:78001760; PMID:71198 !$#accession A90757 !'##molecule_type protein !'##residues 'S',20-30,'A',32-37,'A' ##label AOY REFERENCE A93042 !$#authors Ruoslahti, E.; Pihko, H.; Vaheri, A.; Seppala, M.; !1Virolainen, M.; Konttinen, A. !$#journal Johns Hopkins Med. J. Suppl. (1974) 3:249-255 !$#title 20. Alpha fetoprotein: structure and expression in man and !1inbred mouse strains under normal conditions and liver !1injury. !$#cross-references MUID:75018719; PMID:4138095 !$#accession A93042 !'##molecule_type protein !'##residues 'S',20-24,'Q',26-30,'A',32-35,'E',37-39 ##label RUO REFERENCE A92520 !$#authors Sakai, M.; Morinaga, T.; Urano, Y.; Watanabe, K.; Wegmann, !1T.G.; Tamaoki, T. !$#journal J. Biol. Chem. (1985) 260:5055-5060 !$#title The human alpha-fetoprotein gene. Sequence organization and !1the 5' flanking region. !$#cross-references MUID:85182629; PMID:2580830 !$#contents annotation; gene, exons and introns REFERENCE A90758 !$#authors Aoyagi, Y.; Ikenaka, T.; Ichida, F. !$#journal Cancer Res. (1978) 38:3483-3486 !$#title Copper(II)-binding ability of human alpha-fetoprotein. !$#cross-references MUID:79001617; PMID:80265 !$#contents annotation; metal binding REFERENCE A90759 !$#authors Aoyagi, Y.; Ikenaka, T.; Ichida, F. !$#journal Cancer Res. (1979) 39:3571-3574 !$#title alpha-Fetoprotein as a carrier protein in plasma and its !1bilirubin-binding ability. !$#cross-references MUID:80001710; PMID:89900 !$#contents annotation; bilirubin binding COMMENT AFP is synthesized by the fetal liver and yolk sac. It !1occurs in the plasma of fetuses more than 4 weeks old, !1reaches the highest levels during the 12th-16th week of !1gestation, and drops to trace amounts after birth. The serum !1level in adults is usually less than 40 ng/ml. AFP occurs !1also at high levels in the plasma and ascitic fluid of !1adults with hepatoma. COMMENT Human AFP binds copper, nickel, and fatty acids as well as, !1and the bilirubin less well than, serum albumin. Only a !1small percentage (less than 2%) of the human AFP shows !1estrogen-binding properties. GENETICS !$#gene GDB:AFP !'##cross-references GDB:119660; OMIM:104150 !$#map_position 4q11-4q13 !$#introns 29/1; 46/2; 90/3; 161/2; 205/3; 238/2; 281/3; 353/2; 397/3; !1430/2; 476/3; 551/2; 595/3 CLASSIFICATION #superfamily serum albumin; serum albumin repeat homology KEYWORDS embryo; fetus; globulin; glycoprotein; metal binding; plasma FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-609 #product alpha-fetoprotein #status experimental !8#label MAT\ !$29-202 #domain serum albumin repeat homology #label SA1\ !$221-394 #domain serum albumin repeat homology #label SA2\ !$413-592 #domain serum albumin repeat homology #label SA3\ !$22 #binding_site copper (His) #status experimental\ !$99-114,113-124, !$148-193,192-201, !$224-270,269-277, !$289-303,302-313, !$384-393,416-462, !$461-472,485-501, !$500-511,538-583, !$582-591 #disulfide_bonds #status predicted\ !$249 #binding_site bilirubin (Lys) #status predicted\ !$251 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 609 #molecular-weight 68677 #checksum 9196 SEQUENCE /// ENTRY FPGO #type complete TITLE alpha-fetoprotein precursor - gorilla ORGANISM #formal_name Gorilla gorilla #common_name gorilla DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 22-Jun-1999 ACCESSIONS A37970 REFERENCE A37970 !$#authors Ryan, S.C.; Zielinski, R.; Dugaiczyk, A. !$#journal Genomics (1991) 9:60-72 !$#title Structure of the gorilla alpha-fetoprotein gene and the !1divergence of primates. !$#cross-references MUID:91169517; PMID:1706310 !$#accession A37970 !'##molecule_type DNA !'##residues 1-609 ##label RYA !'##cross-references GB:M38272; NID:g817963; PIDN:AAA73520.1; !1PID:g177041 GENETICS !$#map_position 4q11-12 !$#introns 29/1; 46/2; 90/3; 161/2; 205/3; 238/2; 281/3; 353/2; 397/3; !1430/2; 476/3; 551/2; 595/3 CLASSIFICATION #superfamily serum albumin; serum albumin repeat homology KEYWORDS embryo; fetus; globulin; glycoprotein; metal binding; plasma FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-609 #product alpha-fetoprotein #status predicted #label !8MAT\ !$29-202 #domain serum albumin repeat homology #label SA1\ !$221-394 #domain serum albumin repeat homology #label SA2\ !$413-592 #domain serum albumin repeat homology #label SA3\ !$22 #binding_site copper (His) #status predicted\ !$99-114,113-124, !$148-193,192-201, !$224-270,269-277, !$289-303,302-313, !$384-393,416-462, !$461-472,485-501, !$500-511,538-583, !$582-591 #disulfide_bonds #status predicted\ !$249 #binding_site bilirubin (Lys) #status predicted\ !$251 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 609 #molecular-weight 68697 #checksum 670 SEQUENCE /// ENTRY FPMS #type complete TITLE alpha-fetoprotein precursor - mouse ALTERNATE_NAMES AFP; alpha-1-fetoprotein precursor; alpha-fetoglobulin precursor ORGANISM #formal_name Mus musculus #common_name house mouse DATE 01-Sep-1981 #sequence_revision 28-May-1986 #text_change 12-Jun-1998 ACCESSIONS A93254; A92305; A03235 REFERENCE A93254 !$#authors Law, S.W.; Dugaiczyk, A. !$#journal Nature (1981) 291:201-205 !$#title Homology between the primary structure of alpha-fetoprotein, !1deduced from a complete cDNA sequence, and serum albumin. !$#cross-references MUID:81197641; PMID:6164927 !$#accession A93254 !'##molecule_type mRNA !'##residues 1-597,'E',599-605 ##label LAW !'##cross-references GB:V00743 REFERENCE A93055 !$#authors Minghetti, P.P.; Law, S.W.; Dugaiczyk, A. !$#journal Mol. Biol. Evol. (1985) 2:347-358 !$#title The rate of molecular evolution of alpha-fetoprotein !1approaches that of pseudogenes. !$#cross-references MUID:88216123; PMID:2452956 !$#contents annotation; revision to residue 598 !$#note residue 598, reported in reference A93254 as Glu, should !1have been reported as Lys REFERENCE A92305 !$#authors Gorin, M.B.; Cooper, D.L.; Eiferman, F.; van de Rijn, P.; !1Tilghman, S.M. !$#journal J. Biol. Chem. (1981) 256:1954-1959 !$#title The evolution of alpha-fetoprotein and albumin: I. A !1comparison of the primary amino acid sequences of mammalian !1alpha-fetoprotein and albumin. !$#cross-references MUID:81117287; PMID:6161929 !$#accession A92305 !'##molecule_type mRNA !'##residues 15-532,'RAKL',538-605 ##label GOR !'##cross-references GB:M16381 !'##note the beginning of the mature protein was placed at residue 21 REFERENCE A93271 !$#authors Eiferman, F.A.; Young, P.R.; Scott, R.W.; Tilghman, S.M. !$#journal Nature (1981) 294:713-718 !$#title Intragenic amplification and divergence in the mouse !1alpha-fetoprotein gene. !$#cross-references MUID:82103990; PMID:6172714 !$#contents annotation; exon-intron junctions COMMENT Mouse AFP has two carbohydrate chains and was found to bind !1estrogens and copper. GENETICS !$#map_position 5 !$#introns 29/1; 46/2; 86/3; 157/2; 201/3; 234/2; 277/3; 349/2; 393/3; !1426/2; 472/3; 547/2; 591/3 CLASSIFICATION #superfamily serum albumin; serum albumin repeat homology KEYWORDS embryo; fetus; globulin; glycoprotein; metal binding; plasma FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-605 #product alpha-fetoprotein #status predicted #label !8MPT\ !$29-198 #domain serum albumin repeat homology #label SA1\ !$217-390 #domain serum albumin repeat homology #label SA2\ !$409-588 #domain serum albumin repeat homology #label SA3\ !$22 #binding_site copper (His) #status predicted\ !$95-110,109-120, !$144-189,188-197, !$220-266,265-273, !$285-299,298-309, !$380-389,412-458, !$457-468,481-497, !$496-507,534-579, !$578-587 #disulfide_bonds #status predicted\ !$247,498 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 605 #molecular-weight 67336 #checksum 7876 SEQUENCE /// ENTRY FPRT #type complete TITLE alpha-fetoprotein precursor - rat ALTERNATE_NAMES AFP precursor; alpha-1-fetoprotein precursor; alpha-fetoglobulin precursor ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 08-Oct-1981 #sequence_revision 28-May-1986 #text_change 21-Jul-2000 ACCESSIONS A93561; A93876; JN0247; I53048; I55253; I55217; I55218; !1I69969; I58260; A03236 REFERENCE A93561 !$#authors Turcotte, B.; Guertin, M.; Chevrette, M.; Belanger, L. !$#journal Nucleic Acids Res. (1985) 13:2387-2398 !$#title Rat alpha 1-fetoprotein messenger RNA: 5'-end sequence and !1glucocorticoid-suppressed liver transcription in an improved !1nuclear run-off assay. !$#cross-references MUID:85215621; PMID:2582363 !$#accession A93561 !'##molecule_type mRNA !'##residues 1-106 ##label TUR !'##cross-references GB:X02361 REFERENCE A93876 !$#authors Jagodzinski, L.L.; Sargent, T.D.; Yang, M.; Glackin, C.; !1Bonner, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:3521-3525 !$#title Sequence homology between RNAs encoding rat !1alpha-fetoprotein and rat serum albumin. !$#cross-references MUID:81273091; PMID:6167988 !$#accession A93876 !'##molecule_type mRNA !'##residues 91-611 ##label JAG !'##cross-references GB:V01254; NID:g56781; PIDN:CAA24567.1; PID:g809077 REFERENCE JN0247 !$#authors Watanabe, T.; Jimenez-Molina, J.L.; Chou, J.Y. !$#journal Biochem. Biophys. Res. Commun. (1992) 185:648-656 !$#title Characterization of a rat variant alpha-fetoprotein. !$#cross-references MUID:92304289; PMID:1376990 !$#accession JN0247 !'##molecule_type mRNA !'##residues 287-611 ##label WAT !'##experimental_source liver !'##note an mRNA encoding a variant alpha-fetoprotein lacking the !1amino-terminal 286 residues was isolated from adult liver REFERENCE I53048 !$#authors Buzard, G.; Locker, J. !$#journal DNA Seq. (1990) 1:33-48 !$#title The transcription control region of the rat !1alpha-fetoprotein gene. DNA sequence and homology studies. !$#cross-references MUID:92119318; PMID:1722723 !$#accession I53048 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 7-52 ##label RES !'##cross-references GB:M18351; NID:g202783; PIDN:AAA68903.1; !1PID:g202784 REFERENCE I55253 !$#authors Nahon, J. !$#journal J. Biol. Chem. (1987) 262:12479-12487 !$#title The rat alpha-fetoprotein and albumin genes: Transcriptional !1control and comparison of the sequence organization and !1promoter region. !$#cross-references MUID:87308273; PMID:2442163 !$#accession I55253 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 7-19 ##label RE2 !'##cross-references GB:J02816; NID:g202778; PIDN:AAA40695.1; !1PID:g202779 REFERENCE I55217 !$#authors Liao, W.S.L.; Hamilton, R.W.; Taylor, J.M. !$#journal J. Biol. Chem. (1980) 255:8046-8049 !$#title Amino acid sequence homology between rat alpha-fetoprotein !1and albumin at the COOH-terminal regions. !$#cross-references MUID:81006806; PMID:6157681 !$#accession I55217 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 'VG',558-611 ##label RE3 !'##cross-references GB:J00694; NID:g202776; PIDN:AAA40694.1; !1PID:g202777 REFERENCE I55218 !$#authors Innis, M.A.; Miller, D.L. !$#journal J. Biol. Chem. (1980) 255:8994-8996 !$#title Alpha-fetoprotein gene expression. Partial DNA sequence and !1COOH-terminal homology to albumin. !$#cross-references MUID:81006964; PMID:6157690 !$#accession I55218 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 476-525,'L',527-529,'ATNSSSTRN',539-546,'P',548-597, !1'VQVDFQ',605-611 ##label RE4 !'##cross-references GB:J00693; NID:g56141; PIDN:CAA24546.1; PID:g56142 !$#accession I69969 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 476-525,'L',527-529,'ATNSSSTRN',539-546,'P',548-597, !1'VQVDFQ',605-611 ##label RE5 !'##cross-references EMBL:V01236; NID:g56141; PIDN:CAA24546.1; !1PID:g56142 REFERENCE I58260 !$#authors Chevrette, M.; Guertin, M.; Turcotte, B.; Belanger, L. !$#journal Nucleic Acids Res. (1987) 15:1338-1339 !$#title The rat alpha 1-fetoprotein gene: characterization of the !15'-flanking region and tandem organization with the albumin !1gene. !$#cross-references MUID:87146445; PMID:2434929 !$#accession I58260 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-34 ##label RE6 !'##cross-references EMBL:X05093; NID:g55610; PIDN:CAA28744.1; !1PID:g55611 !'##experimental_source Sprague-Dawley COMMENT The rat AFP strongly binds estrogens. GENETICS !$#introns 35/1 CLASSIFICATION #superfamily serum albumin; serum albumin repeat homology KEYWORDS duplication; embryo; fetus; globulin; glycoprotein; metal !1binding; plasma FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-611 #product alpha-fetoprotein #status predicted #label !8MAT\ !$35-204 #domain serum albumin repeat homology #label SA1\ !$223-396 #domain serum albumin repeat homology #label SA2\ !$287-611 #product alpha-fetoprotein variant #status predicted !8#label MVT\ !$415-594 #domain serum albumin repeat homology #label SA3\ !$28 #binding_site copper (His) #status predicted\ !$101-116,115-126, !$150-195,194-203, !$226-272,271-279, !$291-305,304-315, !$386-395,418-464, !$463-474,487-503, !$502-513,540-585, !$584-593 #disulfide_bonds #status predicted\ !$253 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 611 #molecular-weight 68385 #checksum 2407 SEQUENCE /// ENTRY VYHUD #type complete TITLE vitamin D-binding protein precursor [validated] - human ALTERNATE_NAMES DBP; Gc-globulin; group-specific component ORGANISM #formal_name Homo sapiens #common_name man DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 17-Mar-2000 ACCESSIONS A94076; A46759; A29096; A92765; S39787; A24066; A90427; !1A03237 REFERENCE A94076 !$#authors Yang, F.; Brune, J.L.; Naylor, S.L.; Cupples, R.L.; !1Naberhaus, K.H.; Bowman, B.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:7994-7998 !$#title Human group-specific component (Ge) is a member of the !1albumin family. !$#cross-references MUID:86068030; PMID:2415977 !$#accession A94076 !'##molecule_type mRNA !'##residues 1-474 ##label YAN1 !'##cross-references GB:X03178; GB:M11321; NID:g31675; PIDN:CAA26938.1; !1PID:g31676 !'##experimental_source allele Gc2 REFERENCE A46759 !$#authors Witke, W.F.; Gibbs, P.E.M.; Zielinski, R.; Yang, F.; Bowman, !1B.H.; Dugaiczyk, A. !$#journal Genomics (1993) 16:751-754 !$#title Complete structure of the human Gc gene: differences and !1similarities between members of the albumin gene family. !$#cross-references MUID:93315171; PMID:8325650 !$#accession A46759 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-431,'E',433-435,'T',437-474 ##label WIT !'##cross-references GB:L10641; NID:g340281; PIDN:AAA61704.1; !1PID:g639896 !'##experimental_source allele Gc1 REFERENCE A29096 !$#authors Yang, F.; Naberhaus, K.H.; Adrian, G.S.; Gardella, J.M.; !1Brissenden, J.E.; Bowman, B.H. !$#journal Gene (1987) 54:285-290 !$#title The vitamin D-binding protein gene contains conserved !1nucleotide sequences that respond to heavy metal, adipocyte !1and mitotic signals. !$#cross-references MUID:88005794; PMID:2958390 !$#accession A29096 !'##status translation not shown !'##molecule_type DNA !'##residues 1-19 ##label YAN2 !'##cross-references GB:M17156; NID:g181489; PIDN:AAA19662.1; !1PID:g463096 REFERENCE A92765 !$#authors Cooke, N.E.; David, E.V. !$#journal J. Clin. Invest. (1985) 76:2420-2424 !$#title Serum vitamin D-binding protein is a third member of the !1albumin and alpha fetoprotein gene family. !$#cross-references MUID:86086396; PMID:2416779 !$#accession A92765 !'##molecule_type mRNA !'##residues 1-167,'E',169-326,'R',328-431,'E',433-435,'T',437-474 !1##label COO !'##cross-references GB:M12654; NID:g181481; PIDN:AAA52173.1; !1PID:g181482 !'##experimental_source allele Gc1 REFERENCE S39787 !$#authors Braun, A.; Kofler, A.; Morawietz, S.; Cleve, H. !$#journal Biochim. Biophys. Acta (1993) 1216:385-394 !$#title Sequence and organization of the human vitamin D-binding !1protein gene. !$#cross-references MUID:94092730; PMID:7505619 !$#accession S39787 !'##status preliminary !'##molecule_type DNA !'##residues 1-431,'E',433-435,'T',437-474 ##label BRA !'##cross-references GB:S67480; NID:g455967; PIDN:AAB29423.1; !1PID:g455970 REFERENCE A24066 !$#authors Schoentgen, F.; Metz-Boutigue, M.H.; Jolles, J.; Constans, !1J.; Jolles, P. !$#journal Biochim. Biophys. Acta (1986) 871:189-198 !$#title Complete amino acid sequence of human vitamin D-binding !1protein (group-specific component): evidence of a three-fold !1internal homology as in serum albumin and alpha-fetoprotein. !$#cross-references MUID:86216223; PMID:2423133 !$#accession A24066 !'##molecule_type protein !'##residues 17-474 ##label SCH REFERENCE A90427 !$#authors Svasti, J.; Kurosky, A.; Bennett, A.; Bowman, B.H. !$#journal Biochemistry (1979) 18:1611-1617 !$#title Molecular basis for the three major forms of human serum !1vitamin D binding protein (group-specific component). !$#cross-references MUID:79145448; PMID:218624 !$#accession A90427 !'##molecule_type protein !'##residues 17,'Q',19-21,'N',23-36,'XXX',40-41;472-474 ##label SVA COMMENT DBP is a multifunctional protein found in plasma, ascitic !1fluid, cerebrospinal fluid, and urine and on the surface of !1many cell types. In plasma, it carries the vitamin D sterols !1and prevents polymerization of actin by binding its !1monomers. DBP associates with membrane-bound immunoglobulin !1on the surface of B-lymphocytes and with IgG Fc receptor on !1the membranes of T-lymphocytes. COMMENT Over 80 variants of human DBP have been identified. The !1three most common alleles are called Gc1f, Gc1s, and Gc2. GENETICS !$#gene GDB:GC !'##cross-references GDB:119263; OMIM:139200 !$#map_position 4q12-4q13 !$#introns 20/1; 43/2; 87/3; 158/2; 202/3; 234/2; 277/3; 345/2; 388/3; !1421/2; 465/3 CLASSIFICATION #superfamily serum albumin; serum albumin repeat homology KEYWORDS actin binding; duplication; globulin; glycoprotein; liver; !1plasma; polymorphism; vitamin D FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-474 #product vitamin D-binding protein (allele Gc2) !8#status experimental #label MAL2\ !$17-431,'E',433-435, !$'T',437-474 #product vitamin D-binding protein (allele Gc1) !8#status predicted #label MAL1\ !$26-199 #domain serum albumin repeat homology #label SA1\ !$217-385 #domain serum albumin repeat homology #label SA2\ !$404-474 #domain serum albumin repeat homology #status !8atypical #label SA3\ !$29-75,74-83,96-112, !$111-122,145-190, !$189-198,220-266, !$265-273,286-300, !$299-311,335-376, !$375-384,407-453, !$452-462 #disulfide_bonds #status predicted\ !$288 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 474 #molecular-weight 52963 #checksum 5462 SEQUENCE /// ENTRY VYRTD #type complete TITLE vitamin D-binding protein precursor - rat ALTERNATE_NAMES DBP; Gc-globulin; group-specific component ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 04-Dec-1986 #sequence_revision 31-Dec-1993 #text_change 22-Jun-1999 ACCESSIONS A38726; A34161; A92576; A93050; A03238 REFERENCE A38726 !$#authors Ray, K.; Wang, X.; Zhao, M.; Cooke, N.E. !$#journal J. Biol. Chem. (1991) 266:6221-6229 !$#title The rat vitamin D binding protein (Gc-globulin) gene. !1Structural analysis, functional and evolutionary !1correlations. !$#cross-references MUID:91177870; PMID:2007578 !$#accession A38726 !'##molecule_type DNA !'##residues 1-476 ##label RAY !'##cross-references GB:M60197 !'##experimental_source liver !'##note the authors translated the codon CAG for residue 129 as Gly, !1CTT for residue 174 as Pro, and CAG for residue 337 as Gly REFERENCE A34161 !$#authors Mc Leod, J.F.; Cooke, N.E. !$#journal J. Biol. Chem. (1989) 264:21760-21769 !$#title The vitamin D-binding protein, alpha-fetoprotein, albumin !1multigene family: detection of transcripts in multiple !1tissues. !$#cross-references MUID:90094352; PMID:2480956 !$#accession A34161 !'##molecule_type mRNA !'##residues 1-131,'Q',133-476 ##label MCL !'##cross-references GB:J05148; NID:g203940; PIDN:AAA41082.1; !1PID:g203941 !'##experimental_source kidney REFERENCE A92576 !$#authors Cooke, N.E. !$#journal J. Biol. Chem. (1986) 261:3441-3450 !$#title Rat vitamin D binding protein. Determination of the !1full-length primary structure from cloned cDNA. !$#cross-references MUID:86140127; PMID:2419332 !$#accession A92576 !'##molecule_type mRNA !'##residues 1-173,'P',175-209,'L',211-476 ##label COO !'##cross-references GB:M12450; NID:g203926; PIDN:AAA41080.1; !1PID:g203927 !'##experimental_source liver REFERENCE A93050 !$#authors Litwiller, R.; Fass, D.; Kumar, R. !$#journal Life Sci. (1986) 38:2179-2184 !$#title The amino acid sequence of the NH-2-terminal portion of rat !1and human vitamin D binding protein: evidence for a high !1degree of homology between rat and human vitamin D binding !1protein. !$#cross-references MUID:86229807; PMID:3713442 !$#accession A93050 !'##molecule_type protein !'##residues 17-40 ##label LIT COMMENT DBP is a multifunctional protein found in plasma, ascitic !1fluid, cerebrospinal fluid, and urine and on the surface of !1many cell types. In plasma, it carries the vitamin D sterols !1and prevents polymerization of actin by binding its !1monomers. DBP associates with membrane-bound immunoglobulin !1on the surface of B-lymphocytes and with IgG Fc receptor on !1the membranes of T-lymphocytes. GENETICS !$#introns 20/1; 43/2; 87/3; 158/2; 202/3; 234/2; 277/3; 345/2; 388/3; !1421/2; 465/3 CLASSIFICATION #superfamily serum albumin; serum albumin repeat homology KEYWORDS actin binding; duplication; globulin; glycoprotein; liver; !1plasma; polymorphism; vitamin D FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-476 #product vitamin D-binding protein #status !8experimental #label MPT\ !$26-199 #domain serum albumin repeat homology #label SA1\ !$217-385 #domain serum albumin repeat homology #label SA2\ !$404-476 #domain serum albumin repeat homology #status !8atypical #label SA3\ !$29-75,74-83,96-112, !$111-122,145-190, !$189-198,220-266, !$265-273,286-300, !$299-311,335-376, !$375-384,407-453, !$452-462 #disulfide_bonds #status predicted\ !$288 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 476 #molecular-weight 53518 #checksum 1592 SEQUENCE /// ENTRY A35327 #type fragment TITLE vitamin D-binding protein precursor - mouse (fragment) ALTERNATE_NAMES DBP; Gc-globulin; group-specific component ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 22-Jun-1999 ACCESSIONS A35327 REFERENCE A35327 !$#authors Yang, F.; Bergeron, J.M.; Linehan, L.A.; Lalley, P.A.; !1Sakaguchi, A.Y.; Bowman, B.H. !$#journal Genomics (1990) 7:509-516 !$#title Mapping and conservation of the group-specific component !1gene in mouse. !$#cross-references MUID:90353947; PMID:1696927 !$#accession A35327 !'##molecule_type mRNA !'##residues 1-472 ##label YAN !'##cross-references GB:M55413; GB:J04762; NID:g193445; PIDN:AAA37669.1; !1PID:g193446 COMMENT DBP is a multifunctional protein found in plasma, ascitic !1fluid, cerebrospinal fluid, and urine and on the surface of !1many cell types. In plasma, it carries the vitamin D sterols !1and prevents polymerization of actin by binding its !1monomers. DBP associates with membrane-bound immunoglobulin !1on the surface of B-lymphocytes and with IgG Fc receptor on !1the membranes of T-lymphocytes. GENETICS !$#gene GC !$#map_position 5 CLASSIFICATION #superfamily serum albumin; serum albumin repeat homology KEYWORDS actin binding; duplication; globulin; glycoprotein; liver; !1plasma; polymorphism; vitamin D FEATURE !$1-12 #domain signal sequence (fragment) #status predicted !8#label SIG\ !$13-472 #product vitamin D-binding protein #status predicted !8#label MAT\ !$22-195 #domain serum albumin repeat homology #label SA1\ !$213-381 #domain serum albumin repeat homology #label SA2\ !$400-472 #domain serum albumin repeat homology #status !8atypical #label SA3\ !$25-71,70-79,92-108, !$107-118,141-186, !$185-194,216-262, !$261-269,282-296, !$295-307,331-372, !$371-380,403-449, !$448-458 #disulfide_bonds #status predicted\ !$284 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 472 #checksum 7326 SEQUENCE /// ENTRY S27941 #type complete TITLE serum albumin - sea lamprey ALTERNATE_NAMES plasma albumin ORGANISM #formal_name Petromyzon marinus #common_name sea lamprey DATE 17-Apr-1993 #sequence_revision 17-Apr-1993 #text_change 22-Jun-1999 ACCESSIONS S27941 REFERENCE S27941 !$#authors Doolittle, R.F.; Gray, J.E. !$#submission submitted to the EMBL Data Library, January 1992 !$#description Characterization, primary structure and evolution of Lamprey !1plasma albumin. !$#accession S27941 !'##molecule_type mRNA !'##residues 1-1423 ##label DOO !'##cross-references EMBL:M74193; NID:g213213; PIDN:AAA49271.1; !1PID:g213214 CLASSIFICATION #superfamily sea lamprey serum albumin; serum albumin repeat !1homology FEATURE !$39-222 #domain serum albumin repeat homology #label SA1\ !$241-417 #domain serum albumin repeat homology #label SA2\ !$436-610 #domain serum albumin repeat homology #label SA3\ !$619-803 #domain serum albumin repeat homology #label SA4\ !$822-911,942-1023 #domain serum albumin repeat homology #status !8atypical #label SA5\ !$912-939 #region 4-residue repeats (T-S-T-T)\ !$1042-1217 #domain serum albumin repeat homology #label SA6\ !$1236-1413 #domain serum albumin repeat homology #label SA7 SUMMARY #length 1423 #molecular-weight 159092 #checksum 8943 SEQUENCE /// ENTRY TGHU #type complete TITLE beta-thromboglobulin precursor [validated] - human CONTAINS connective-tissue activating peptide III; CTAP-III; histamine-releasing factor; neutrophil-activating peptide 2; platelet basic protein ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Apr-1979 #sequence_revision 31-Dec-1992 #text_change 08-Dec-2000 ACCESSIONS A39546; A37382; A24448; PL0222; A93982; A90411; A60709; !1A61240; B61240; A03240; A30159; A33516; S46247 REFERENCE A39546 !$#authors Majumdar, S.; Gonder, D.; Koutsis, B.; Poncz, M. !$#journal J. Biol. Chem. (1991) 266:5785-5789 !$#title Characterization of the human beta-thromboglobulin gene. !1Comparison with the gene for platelet factor 4. !$#cross-references MUID:91170256; PMID:1826003 !$#accession A39546 !'##molecule_type DNA !'##residues 1-128 ##label MAJ !'##cross-references GB:M54995; NID:g181175; PIDN:AAA62836.1; !1PID:g181176 !'##note the authors translated the codon GAT for residue 109 as Pro REFERENCE A37382 !$#authors Wenger, R.H.; Wicki, A.N.; Walz, A.; Kieffer, N.; Clemetson, !1K.J. !$#journal Blood (1989) 73:1498-1503 !$#title Cloning of cDNA coding for connective tissue activating !1peptide III from a human platelet-derived lambdagtII !1expression library. !$#cross-references MUID:89229374; PMID:2713489 !$#accession A37382 !'##molecule_type mRNA !'##residues 1-128 ##label WEN !'##cross-references GB:M54995; NID:g181175; PIDN:AAA62836.1; !1PID:g181176; GB:M38441 REFERENCE A24448 !$#authors Holt, J.C.; Harris, M.E.; Holt, A.M.; Lange, E.; Henschen, !1A.; Niewiarowski, S. !$#journal Biochemistry (1986) 25:1988-1996 !$#title Characterization of human platelet basic protein, a !1precursor form of low-affinity platelet factor 4 and !1beta-thromboglobulin. !$#cross-references MUID:86216117; PMID:2423119 !$#accession A24448 !'##molecule_type protein !'##residues 35-53 ##label HOL REFERENCE PL0222 !$#authors Walz, A.; Baggiolini, M. !$#journal J. Exp. Med. (1990) 171:449-454 !$#title Generation of the neutrophil-activating peptide NAP-2 from !1platelet basic protein or connective tissue-activating !1peptide III through monocyte proteases. !$#cross-references MUID:90155110; PMID:2406364 !$#accession PL0222 !'##molecule_type protein !'##residues 54-67 ##label WAL REFERENCE A93982 !$#authors Castor, C.W.; Miller, J.W.; Walz, D.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:765-769 !$#title Structural and biological characteristics of connective !1tissue activating peptide (CTAP-III), a major human !1platelet-derived growth factor. !$#cross-references MUID:83144010; PMID:6572368 !$#accession A93982 !'##molecule_type protein !'##residues 44-66;125-128 ##label CAS REFERENCE A90411 !$#authors Begg, G.S.; Pepper, D.S.; Chesterman, C.N.; Morgan, F.J. !$#journal Biochemistry (1978) 17:1739-1744 !$#title Complete covalent structure of human beta-thromboglobulin. !$#cross-references MUID:78187279; PMID:77677 !$#accession A90411 !'##molecule_type protein !'##residues 48-128 ##label BEG REFERENCE A60709 !$#authors Baeza, M.L.; Reddigari, S.R.; Kornfeld, D.; Ramani, N.; !1Smith, E.M.; Hossler, P.A.; Fischer, T.; Castor, C.W.; !1Gorevic, P.G.; Kaplan, A.P. !$#journal J. Clin. Invest. (1990) 85:1516-1521 !$#title Relationship of one form of human histamine-releasing factor !1to connective tissue activating peptide-III. !$#cross-references MUID:90237229; PMID:1692035 !$#accession A60709 !'##molecule_type protein !'##residues 44-62,'X',64-79 ##label BAE REFERENCE A61240 !$#authors Kaplan, A.P.; Baeza, M.; Reddigari, S.; Kuna, P. !$#journal Int. Arch. Allergy Appl. Immunol. (1991) 94:148-153 !$#title Histamine-releasing factors. !$#cross-references MUID:92040226; PMID:1718884 !$#accession A61240 !'##molecule_type protein !'##residues 44-61,'XX',64 ##label KAP !$#accession B61240 !'##molecule_type protein !'##residues 59-62,'X',64-79 ##label KA2 REFERENCE S46247 !$#authors Kungl, A.J.; Machius, M.; Huber, R.; Schwer, C.; Lam, C.; !1Aschauer, H.; Ehn, G.; Lindley, I.J.D.; Auer, M. !$#journal FEBS Lett. (1994) 347:300-303 !$#title Purification, crystallization and preliminary X-ray !1diffraction analysis of recombinant human !1neutrophil-activating peptide 2 (rhNAP-2). !$#cross-references MUID:94307404; PMID:8034022 !$#contents annotation COMMENT There appears to be a second beta-thromboglobulin-like human !1gene. COMMENT Connective-tissue activating peptides (CTAP) are a group of !1proteins capable of activating connective tissue cells. !1CTAP-I, -II, -III and -P2, and -PMN are of lymphoid, tumor !1cell, human platelet, and polymorphonuclear leukocyte !1origin, respectively. COMMENT CTAP-III, a monomer isolated from platelets, stimulates DNA !1synthesis, mitosis, glycolysis, intracellular cAMP !1accumulation, prostaglandin E2 secretion, and synthesis of !1hyaluronic acid and sulfated glycosaminoglycan. It also !1stimulates the formation and secretion of plasminogen !1activator by human synovial cells. COMMENT Proteolytic removal of the first four residues of CTAP-III !1produces the active peptide beta-thromboglobulin, which is !1released from platelets along with platelet factor 4 and !1platelet-derived growth factor. GENETICS !$#gene GDB:PPBP; THBGB1 !'##cross-references GDB:127391; OMIM:121010 !$#map_position 4p12-4q13 !$#introns 50/1; 95/2 CLASSIFICATION #superfamily beta-thromboglobulin KEYWORDS growth factor; homotetramer; platelet FEATURE !$1-34 #domain signal sequence #status predicted #label SIG\ !$35-43 #domain propeptide #status predicted #label PRO\ !$44-128 #product connective-tissue activating peptide III !8#status experimental #label CTAP\ !$48-128 #product beta-thromboglobulin #status experimental !8#label BTG\ !$59-128 #product neutrophil-activating peptide 2 #status !8experimental #label NAP2\ !$63-89,65-105 #disulfide_bonds #status experimental SUMMARY #length 128 #molecular-weight 13894 #checksum 6910 SEQUENCE /// ENTRY PFHU4 #type complete TITLE platelet factor 4 precursor [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1979 #sequence_revision 03-Nov-1995 #text_change 20-Apr-2001 ACCESSIONS A60161; S07159; A94305; A92208; A93810; A94307; A03241 REFERENCE A60161 !$#authors Eisman, R.; Surrey, S.; Ramachandran, B.; Schwartz, E.; !1Poncz, M. !$#journal Blood (1990) 76:336-344 !$#title Structural and functional comparison of the genes for human !1platelet factor 4 and PF4-alt. !$#cross-references MUID:90315431; PMID:1695112 !$#accession A60161 !'##molecule_type DNA !'##residues 1-101 ##label EIS REFERENCE S07159 !$#authors Poncz, M.; Surrey, S.; LaRocco, P.; Weiss, M.J.; Rappaport, !1E.F.; Conway, T.M.; Schwartz, E. !$#journal Blood (1987) 69:219-223 !$#title Cloning and characterization of platelet factor 4 cDNA !1derived from a human erythroleukemic cell line. !$#cross-references MUID:87076954; PMID:3098319 !$#accession S07159 !'##molecule_type DNA; mRNA !'##residues 1-101 ##label PON !'##cross-references EMBL:M25897; NID:g189850; PIDN:AAA60066.1; !1PID:g189851 REFERENCE A94305 !$#authors Morgan, F.J.; Begg, G.S.; Chesterman, C.N. !$#journal Thromb. Haemost. (1980) 42:1652-1660 !$#title Complete covalent structure of human platelet factor 4. !$#cross-references MUID:80169663; PMID:6445090 !$#accession A94305 !'##molecule_type protein !'##residues 32-101 ##label MOR REFERENCE A92208 !$#authors Hermodson, M.; Schmer, G.; Kurachi, K. !$#journal J. Biol. Chem. (1977) 252:6276-6279 !$#title Isolation, crystallization, and primary amino acid sequence !1of human platelet factor 4. !$#cross-references MUID:77249569; PMID:893407 !$#accession A92208 !'##molecule_type protein !'##residues 32-101 ##label HER REFERENCE A93810 !$#authors Deuel, T.F.; Keim, P.S.; Farmer, M.; Heinrikson, R.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1977) 74:2256-2258 !$#title Amino acid sequence of human platelet factor 4. !$#cross-references MUID:77234634; PMID:267922 !$#accession A93810 !'##molecule_type protein !'##residues 32-77,'D',79-101 ##label DEU REFERENCE A94307 !$#authors Walz, D.A.; Wu, V.Y.; de Lamo, R.; Dene, H.; McCoy, L.E. !$#journal Thromb. Res. (1977) 11:893-898 !$#title Primary structure of human platelet factor-4. !$#cross-references MUID:78097310; PMID:601757 !$#accession A94307 !'##molecule_type protein !'##residues 32-77,'D',79-101 ##label WAL REFERENCE A52834 !$#authors Chen, L.; Zhang, X. !$#submission submitted to the Brookhaven Protein Data Bank, September !11994 !$#cross-references PDB:1RHP !$#contents annotation; X-ray crystallography, 2.4 angstroms, residues !138-101 !$#note recombinant form expressed in Escherichia coli REFERENCE A54206 !$#authors Zhang, X.; Chen, L.; Bancroft, D.P.; Lai, C.K.; Maione, T.E. !$#journal Biochemistry (1994) 33:8361-8366 !$#title Crystal structure of recombinant human platelet factor 4. !$#cross-references MUID:94304848; PMID:8031770 !$#contents annotation; X-ray crystallography, 2.4 angstroms COMMENT Tetrameric platelet factor 4 is made in megakaryocytes, !1noncovalently bound to one proteoglycan molecule, and !1packaged into alpha granules for release during platelet !1aggregation. GENETICS !$#gene GDB:PF4 !'##cross-references GDB:119479; OMIM:173460 !$#map_position 4q12-4q21 !$#introns 31/1; 73/2 COMPLEX homotetramer FUNCTION !$#description binds strongly to heparin and related glycosaminoglycans, !1more strongly than to the chondroitin-4-sulfate chains of !1its carrier molecule; by binding it neutralizes the !1anticoagulant effect of heparin !$#pathway blood coagulation CLASSIFICATION #superfamily beta-thromboglobulin KEYWORDS blood coagulation; heparin binding; homotetramer; platelet FEATURE !$1-31 #domain signal sequence #status predicted #label SIG\ !$32-101 #product platelet factor 4 #status experimental !8#label MAT\ !$41-67,43-83 #disulfide_bonds #status experimental SUMMARY #length 101 #molecular-weight 10845 #checksum 581 SEQUENCE /// ENTRY PFHU4A #type complete TITLE platelet factor 4 variant 1 precursor - human ALTERNATE_NAMES platelet factor 4-alt ORGANISM #formal_name Homo sapiens #common_name man DATE 08-Dec-1989 #sequence_revision 03-Nov-1995 #text_change 22-Jun-1999 ACCESSIONS A31941; B60161 REFERENCE A31941 !$#authors Green, C.J.; St. Charles, R.; Edwards, B.F.P.; Johnson, P.H. !$#journal Mol. Cell. Biol. (1989) 9:1445-1451 !$#title Identification and characterization of PF4var1, a human gene !1variant of platelet factor 4. !$#cross-references MUID:89261772; PMID:2725510 !$#accession A31941 !'##molecule_type DNA !'##residues 1-104 ##label GRE !'##cross-references EMBL:M26167; NID:g292389; PIDN:AAA60067.1; !1PID:g292390 REFERENCE A60161 !$#authors Eisman, R.; Surrey, S.; Ramachandran, B.; Schwartz, E.; !1Poncz, M. !$#journal Blood (1990) 76:336-344 !$#title Structural and functional comparison of the genes for human !1platelet factor 4 and PF4-alt. !$#cross-references MUID:90315431; PMID:1695112 !$#accession B60161 !'##status translation not shown !'##molecule_type DNA !'##residues 1-104 ##label EIS COMMENT Modeling studies suggest that the function of platelet !1factor 4 variant may differ significantly from platelet !1factor 4 (see PIR:PFHU4). GENETICS !$#gene GDB:PF4V1 !'##cross-references GDB:125382; OMIM:173461 !$#map_position 4q12-4q21 !$#introns 34/1; 76/2 CLASSIFICATION #superfamily beta-thromboglobulin FEATURE !$1-34 #domain signal sequence #status predicted #label SIG\ !$35-104 #product platelet factor 4 variant 1 #status !8predicted #label MAT\ !$44-70,46-86 #disulfide_bonds #status predicted SUMMARY #length 104 #molecular-weight 11553 #checksum 187 SEQUENCE /// ENTRY PFBO4 #type complete TITLE platelet factor 4 - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 18-Apr-1984 #sequence_revision 18-Apr-1984 #text_change 18-Oct-1996 ACCESSIONS A03242; A26144 REFERENCE A94611 !$#authors Walz, D.A. !$#submission submitted to the Atlas, October 1982 !$#accession A03242 !'##molecule_type protein !'##residues 1-88 ##label WAL REFERENCE A26144 !$#authors Ciaglowski, R.E.; Snow, J.; Walz, D.A. !$#journal Arch. Biochem. Biophys. (1986) 250:249-256 !$#title Isolation and amino acid sequence of bovine platelet factor !14. !$#cross-references MUID:87024614; PMID:3767377 !$#accession A26144 !'##molecule_type protein !'##residues 1-88 ##label CIA CLASSIFICATION #superfamily beta-thromboglobulin KEYWORDS heparin binding; homotetramer; platelet FEATURE !$25-51,27-67 #disulfide_bonds #status predicted SUMMARY #length 88 #molecular-weight 9523 #checksum 2919 SEQUENCE /// ENTRY TGHUGI #type complete TITLE interferon gamma-induced protein precursor - human ALTERNATE_NAMES gamma-IP-10 ORGANISM #formal_name Homo sapiens #common_name man DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 22-Jun-1999 ACCESSIONS A03243 REFERENCE A03243 !$#authors Luster, A.D.; Unkeless, J.C.; Ravetch, J.V. !$#journal Nature (1985) 315:672-676 !$#title gamma-Interferon transcriptionally regulates an !1early-response gene containing homology to platelet !1proteins. !$#cross-references MUID:85240552; PMID:3925348 !$#accession A03243 !'##molecule_type mRNA !'##residues 1-98 ##label LUS !'##cross-references EMBL:X02530; GB:M17752; NID:g33917; !1PIDN:CAA26370.1; PID:g33918 COMMENT In response to interferon gamma treatment, a diverse !1population of cell types rapidly increases transcription of !1mRNA encoding this protein. This suggests that gamma-induced !1protein may be a key mediator of the interferon gamma !1response. Sequence similarities to beta-thromboglobulin and !1platelet factor 4 suggest that it may also be involved in !1inflammation. GENETICS !$#gene GDB:INP10 !'##cross-references GDB:119348; OMIM:147310 !$#map_position 4q21-4q21 CLASSIFICATION #superfamily beta-thromboglobulin KEYWORDS inflammation FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-98 #product interferon gamma-induced protein #status !8predicted #label MAT\ !$30-57,32-74 #disulfide_bonds #status predicted SUMMARY #length 98 #molecular-weight 10856 #checksum 2500 SEQUENCE /// ENTRY BVFFSL #type complete TITLE sol protein, large splice form - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 22-Jun-1999 ACCESSIONS A41146 REFERENCE A41146 !$#authors Delaney, S.J.; Hayward, D.C.; Barleben, F.; Fischbach, K.F.; !1Miklos, G.L.G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:7214-7218 !$#title Molecular cloning and analysis of small optic lobes, a !1structural brain gene of Drosophila melanogaster. !$#cross-references MUID:91334436; PMID:1714593 !$#accession A41146 !'##molecule_type mRNA !'##residues 1-1597 ##label DEL !'##cross-references GB:M64084; NID:g2760822; PIDN:AAB95431.1; !1PID:g158483 COMMENT The sol (small optic lobes) mutation eliminates certain !1classes of columnar neurons. COMMENT An alternate splice form of 395 amino acids is observed, in !1which the first 393 are identical to the large sol protein. GENETICS !$#gene sol !'##cross-references FlyBase:FBgn0003464 !$#map_position 19F4 CLASSIFICATION #superfamily sol protein; calpain catalytic domain homology KEYWORDS alternative splicing; brain; zinc finger FEATURE !$12-29 #region zinc finger CCCC motif\ !$141-158 #region zinc finger CCCC motif\ !$649-667 #region zinc finger CCCC motif\ !$673-702 #region glutamine/histidine-rich\ !$713-730 #region zinc finger CCCC motif\ !$754-771 #region zinc finger CCCC motif\ !$936-953 #region zinc finger CCCC motif\ !$1047-1307 #domain calpain catalytic domain homology #label !8CALP\ !$1082,1248,1268 #active_site Cys, His, Asn #status predicted SUMMARY #length 1597 #molecular-weight 174713 #checksum 8253 SEQUENCE /// ENTRY QRMSN1 #type complete TITLE probable hormone receptor N10, nuclear - mouse ALTERNATE_NAMES steroid hormone receptor homolog nur/77 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 22-Jun-1999 ACCESSIONS S06953; A30059; A31344 REFERENCE S06953 !$#authors Ryseck, R.P.; Macdonald-Bravo, H.; Mattei, M.G.; Ruppert, !1S.; Bravo, R. !$#journal EMBO J. (1989) 8:3327-3335 !$#title Structure, mapping and expression of a growth factor !1inducible gene encoding a putative nuclear hormonal binding !1receptor. !$#cross-references MUID:90059925; PMID:2555161 !$#accession S06953 !'##molecule_type DNA !'##residues 1-601 ##label RYS !'##cross-references EMBL:X16995; NID:g53312; PIDN:CAA34862.1; !1PID:g53313 REFERENCE A94211 !$#authors Hazel, T.G.; Nathans, D.; Lau, L.F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:8444-8448 !$#title A gene inducible by serum growth factors encodes a member of !1the steroid and thyroid hormone receptor superfamily. !$#cross-references MUID:89042200; PMID:3186734 !$#accession A30059 !'##molecule_type mRNA !'##residues 1-601 ##label HAZ !'##cross-references GB:J04113; NID:g200115; PIDN:AAA39843.1; !1PID:g200116 GENETICS !$#map_position 15F !$#introns 295/3; 339/1; 389/3; 457/2; 517/1 CLASSIFICATION #superfamily probable hormone receptor N10, nuclear; erbA !1transforming protein homology KEYWORDS DNA binding; nucleus; steroid hormone receptor; !1transcription factor; zinc finger FEATURE !$268-517 #domain erbA transforming protein homology #label !8ERBA\ !$270-290 #region zinc finger CCCC motif\ !$276-335 #domain DNA binding #status predicted #label DNA\ !$306-330 #region zinc finger CCCC motif SUMMARY #length 601 #molecular-weight 64738 #checksum 8700 SEQUENCE /// ENTRY T43348 #type complete TITLE nuclear steroid hormone receptor NHR-6 - Caenorhabditis elegans ALTERNATE_NAMES protein C48D5.1; steroid hormone receptor family member CNR8 ORGANISM #formal_name Caenorhabditis elegans DATE 03-Mar-2000 #sequence_revision 03-Mar-2000 #text_change 21-Jul-2000 ACCESSIONS T43348; T20039; I45068 REFERENCE Z22443 !$#authors Sluder, A.E.; Mathews, S.W.; Hough, D.; Yin, V.P.; Maina, !1C.V. !$#journal Genome Res. (1999) 9:103-120 !$#title The nuclear receptor superfamily has undergone extensive !1proliferation and diversification in nematodes. !$#cross-references MUID:99148134; PMID:10022975 !$#accession T43348 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-619 ##label SLU !'##cross-references EMBL:AF083224; NID:g4139073; PIDN:AAD03682.1; !1PID:g4139074 REFERENCE Z19215 !$#authors Lightning, J. !$#submission submitted to the EMBL Data Library, August 1994 !$#accession T20039 !'##molecule_type DNA !'##residues 58-619 ##label WIL !'##cross-references EMBL:Z36237; PIDN:CAA85271.1; GSPDB:GN00021; !1CESP:C48D5.1 !'##experimental_source clone C48D5 REFERENCE A55595 !$#authors Kostrouch, Z.; Kostrouchova, M.; Rall, J.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1995) 92:156-159 !$#title Steroid/thyroid hormone receptor genes in Caenorhabditis !1elegans. !$#cross-references MUID:95116514; PMID:7816808 !$#accession I45068 !'##status preliminary !'##molecule_type mRNA !'##residues 157-187,'T',189-619 ##label RES !'##cross-references EMBL:U13076; NID:g538372; PIDN:AAA96984.1; !1PID:g538373 GENETICS !$#gene nhr-6; cnr8; CESP:C48D5.1 !$#map_position 3 !$#introns 71/1; 98/3; 124/3; 175/2; 240/2; 337/1; 389/3; 510/1; 550/3 CLASSIFICATION #superfamily Caenorhabditis elegans nuclear steroid hormone !1receptor NHR-6; erbA transforming protein homology KEYWORDS steroid hormone receptor; zinc finger FEATURE !$266-507 #domain erbA transforming protein homology #label !8ERBA SUMMARY #length 619 #molecular-weight 68622 #checksum 3599 SEQUENCE /// ENTRY B36738 #type complete TITLE orphan receptor TR2, splice form TR2-11 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 15-Oct-1999 ACCESSIONS B36738 REFERENCE A36738 !$#authors Chang, C.; Kokontis, J.; Acakpo-Satchivi, L.; Liao, S.; !1Takeda, H.; Chang, Y. !$#journal Biochem. Biophys. Res. Commun. (1989) 165:735-741 !$#title Molecular cloning of new human TR2 receptors: a class of !1steroid receptor with multiple ligand-binding domains. !$#cross-references MUID:90088487; PMID:2597158 !$#accession B36738 !'##molecule_type mRNA !'##residues 1-603 ##label CHA !'##cross-references GB:M29960; NID:g339886; PIDN:AAA36761.1; !1PID:g339887 GENETICS !$#gene GDB:TR2-11 !'##cross-references GDB:5875387 CLASSIFICATION #superfamily orphan receptor TR2; erbA transforming protein !1homology KEYWORDS alternative splicing; DNA binding; nucleus; receptor; !1transcription regulation; zinc finger FEATURE !$111-510 #domain erbA transforming protein homology #label !8ERBA\ !$113-133 #region zinc finger CCCC motif\ !$149-168 #region zinc finger CCCC motif SUMMARY #length 603 #molecular-weight 67299 #checksum 7688 SEQUENCE /// ENTRY A31521 #type complete TITLE orphan receptor TR2, splice form TR2-5 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 21-Jul-2000 ACCESSIONS A31521 REFERENCE A31521 !$#authors Chang, C.; Kokontis, J. !$#journal Biochem. Biophys. Res. Commun. (1988) 155:971-977 !$#title Identification of a new member of the steroid receptor !1super-family by cloning and sequence analysis. !$#cross-references MUID:88339993; PMID:3421977 !$#accession A31521 !'##molecule_type mRNA !'##residues 1-483 ##label CHA !'##cross-references GB:M21985; NID:g338485; PIDN:AAA36650.1; !1PID:g338486 GENETICS !$#gene GDB:TR2-11 !'##cross-references GDB:5875387 CLASSIFICATION #superfamily orphan receptor TR2; erbA transforming protein !1homology KEYWORDS alternative splicing; DNA binding; nucleus; receptor; !1transcription regulation; zinc finger FEATURE !$111-465 #domain erbA transforming protein homology #status !8atypical #label ERBA\ !$113-133 #region zinc finger CCCC motif\ !$149-168 #region zinc finger CCCC motif SUMMARY #length 483 #molecular-weight 53042 #checksum 2057 SEQUENCE /// ENTRY A36738 #type complete TITLE orphan receptor TR2, splice form TR2-9 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 21-Jul-2000 ACCESSIONS A36738 REFERENCE A36738 !$#authors Chang, C.; Kokontis, J.; Acakpo-Satchivi, L.; Liao, S.; !1Takeda, H.; Chang, Y. !$#journal Biochem. Biophys. Res. Commun. (1989) 165:735-741 !$#title Molecular cloning of new human TR2 receptors: a class of !1steroid receptor with multiple ligand-binding domains. !$#cross-references MUID:90088487; PMID:2597158 !$#accession A36738 !'##status preliminary !'##molecule_type mRNA !'##residues 1-467 ##label CHA !'##cross-references GB:M29959; NID:g339888; PIDN:AAA36762.1; !1PID:g339889 GENETICS !$#gene GDB:TR2-11 !'##cross-references GDB:5875387 CLASSIFICATION #superfamily orphan receptor TR2; erbA transforming protein !1homology KEYWORDS alternative splicing; DNA binding; nucleus; receptor; !1transcription regulation; zinc finger FEATURE !$111-464 #domain erbA transforming protein homology #status !8atypical #label ERBA\ !$113-133 #region zinc finger CCCC motif\ !$149-168 #region zinc finger CCCC motif SUMMARY #length 467 #molecular-weight 51192 #checksum 8704 SEQUENCE /// ENTRY QRHUE #type complete TITLE estrogen receptor 1 - human ALTERNATE_NAMES ER1; estrogen receptor alpha ORGANISM #formal_name Homo sapiens #common_name man DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 22-Jun-1999 ACCESSIONS A94284; A93376; A43021; S27143; S34000; A41925; B41925; !1A03244; C41925; D41925 REFERENCE A94284 !$#authors Greene, G.L.; Gilna, P.; Waterfield, M.; Baker, A.; Hort, !1Y.; Shine, J. !$#journal Science (1986) 231:1150-1154 !$#title Sequence and expression of human estrogen receptor !1complementary DNA. !$#cross-references MUID:86122927; PMID:3753802 !$#accession A94284 !'##molecule_type mRNA !'##residues 1-595 ##label GR1 !'##cross-references GB:M12674; NID:g182192; PIDN:AAA52399.1; !1PID:g182193 REFERENCE A93376 !$#authors Green, S.; Walter, P.; Kumar, V.; Krust, A.; Bornert, J.M.; !1Argos, P.; Chambon, P. !$#journal Nature (1986) 320:134-139 !$#title Human oestrogen receptor cDNA: sequence, expression and !1homology to v-erb-A. !$#cross-references MUID:86146892; PMID:3754034 !$#accession A93376 !'##molecule_type mRNA !'##residues 1-595 ##label GR2 !'##cross-references GB:X03635; NID:g31233; PIDN:CAA27284.1; PID:g31234 REFERENCE A43021 !$#authors Ponglikitmongkol, M.; Green, S.; Chambon, P. !$#journal EMBO J. (1988) 7:3385-3388 !$#title Genomic organization of the human oestrogen receptor gene. !$#cross-references MUID:89091079; PMID:3145193 !$#accession A43021 !'##molecule_type DNA !'##residues 143-161;205-225;244-264;356-374,'G',376;402-422;447-460, !1'P',462-467;508-528 ##label PON REFERENCE S27140 !$#authors Keaveney, M.; Klug, J.; Gannon, F. !$#journal DNA Seq. (1992) 2:347-358 !$#title Sequence analysis of the 5' flanking region of the human !1estrogen receptor gene. !$#cross-references MUID:93075998; PMID:1476547 !$#accession S27143 !'##status preliminary; translation not shown !'##molecule_type DNA !'##residues 1-115 ##label KEA !'##cross-references EMBL:X62462; NID:g31201; PIDN:CAA44322.1; !1PID:g31205 REFERENCE S34000 !$#authors Pfeffer, U.; Fecarotta, E.; Castagnetta, L.; Vidali, G. !$#journal Cancer Res. (1993) 53:741-743 !$#title Estrogen receptor variant messenger RNA lacking exon 4 in !1estrogen-responsive human breast cancer cell lines. !$#cross-references MUID:93153765; PMID:7916651 !$#accession S34000 !'##status preliminary !'##molecule_type mRNA !'##residues 216-254,367-399,'G',401-434 ##label PFE !'##cross-references EMBL:X73067; NID:g579865; PIDN:CAA51528.1; !1PID:g939886 !'##note the authors translated the codon GGG for residue 400 as Val REFERENCE A41925 !$#authors Dotzlaw, H.; Alkhalaf, M.; Murphy, L.C. !$#journal Mol. Endocrinol. (1992) 6:773-785 !$#title Characterization of estrogen receptor variant mRNAs from !1human breast cancers. !$#cross-references MUID:92293154; PMID:1603086 !$#accession A41925 !'##molecule_type mRNA !'##residues 1-214,'ELPTLC' ##label DOT !'##cross-references GB:M69297; NID:g182218; PIDN:AAA58462.1; !1PID:g182219 !'##experimental_source clone 4; breast cancer !'##note sequence has been revised after extraction from NCBI backbone !'##note the complete sequence of neither the nucleotide nor the protein !1is shown in this paper !'##note sequence extracted from NCBI backbone (NCBIN:106580) !$#accession B41925 !'##status significant sequence differences !'##molecule_type mRNA !'##cross-references GB:M69296 !'##experimental_source clone 24; breast cancer !'##note sequence extracted from NCBI backbone (NCBIN:106597) COMMENT The steroid hormones and their receptors are involved in the !1regulation of eukaryotic gene expression and affect cellular !1proliferation and differentiation in target tissues. COMMENT In the absence of ligand, steroid hormone receptors are !1thought to be weakly associated with nuclear components; !1hormone binding greatly increases receptor affinity. The !1hormone-receptor complex appears to recognize discrete DNA !1sequences upstream of transcriptional start sites. GENETICS !$#gene GDB:ESR1; ESR !'##cross-references GDB:119120; OMIM:133430 !$#map_position 6q25.1-6q25.1 !$#introns 151/2; 215/1; 254/1; 366/1; 412/2; 457/1; 518/2 CLASSIFICATION #superfamily estrogen receptor; erbA transforming protein !1homology KEYWORDS DNA binding; nucleus; phosphoprotein; steroid hormone !1receptor; transcription regulation; zinc finger FEATURE !$1-120 #domain amino-terminal #label NH2\ !$121-299 #domain DNA binding #status predicted #label DNA\ !$183-456 #domain erbA transforming protein homology #label !8ERBA\ !$185-205 #region zinc finger CCCC motif\ !$221-245 #region zinc finger CCCC motif\ !$300-595 #domain steroid binding #status predicted #label STB\ !$236,305 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 595 #molecular-weight 66258 #checksum 4317 SEQUENCE /// ENTRY QRMSE #type complete TITLE estrogen receptor - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 06-Mar-1992 #sequence_revision 14-Jul-1994 #text_change 22-Jun-1999 ACCESSIONS A40061 REFERENCE A40061 !$#authors White, R.; Lees, J.A.; Needham, M.; Ham, J.; Parker, M. !$#journal Mol. Endocrinol. (1987) 1:735-744 !$#title Structural organization and expression of the mouse estrogen !1receptor. !$#cross-references MUID:91042558; PMID:2484714 !$#accession A40061 !'##molecule_type mRNA !'##residues 1-599 ##label WHI !'##cross-references GB:M38651; NID:g193179; PIDN:AAA37580.1; !1PID:g193180 COMMENT The steroid hormones and their receptors are involved in the !1regulation of eukaryotic gene expression and affect cellular !1proliferation and differentiation in target tissues. COMMENT In the absence of ligand, steroid hormone receptors are !1thought to be weakly associated with nuclear components; !1hormone binding greatly increases receptor affinity. The !1hormone-receptor complex appears to recognize discrete DNA !1sequences upstream of transcriptional start sites. CLASSIFICATION #superfamily estrogen receptor; erbA transforming protein !1homology KEYWORDS DNA binding; nucleus; phosphoprotein; steroid binding; !1steroid hormone receptor; transcription regulation; zinc !1finger FEATURE !$1-183 #domain amino-terminal #label NH2\ !$184-275 #domain DNA binding #status predicted #label DNA\ !$187-460 #domain erbA transforming protein homology #label !8ERBA\ !$187-210 #region zinc finger CCCC motif\ !$223-245 #region zinc finger CCCC motif\ !$260-275 #region nuclear location signal\ !$304-556 #domain steroid binding #status predicted #label STB\ !$189,192,206,209 #binding_site zinc (Cys) #status predicted\ !$225,231,241,244 #binding_site zinc (Cys) #status predicted\ !$240,309 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 599 #molecular-weight 66954 #checksum 4749 SEQUENCE /// ENTRY QRRTE #type complete TITLE estrogen receptor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1991 #sequence_revision 14-Jul-1994 #text_change 22-Jun-1999 ACCESSIONS S07379; S16731 REFERENCE S07379 !$#authors Koike, S.; Sakai, M.; Muramatsu, M. !$#journal Nucleic Acids Res. (1987) 15:2499-2513 !$#title Molecular cloning and characterization of rat estrogen !1receptor cDNA. !$#cross-references MUID:87174780; PMID:3031601 !$#accession S07379 !'##molecule_type mRNA !'##residues 1-600 ##label KOI !'##cross-references EMBL:Y00102; NID:g56110; PIDN:CAA68287.1; !1PID:g56111 REFERENCE S16731 !$#authors Maggi, A.M.A. !$#submission submitted to the EMBL Data Library, June 1991 !$#accession S16731 !'##molecule_type mRNA !'##residues 1-487,'T',489-600 ##label MAG !'##cross-references EMBL:X61098; NID:g56120; PIDN:CAA43411.1; !1PID:g56121 COMMENT The steroid hormones and their receptors are involved in the !1regulation of eukaryotic gene expression and affect cellular !1proliferation and differentiation in target tissues. COMMENT In the absence of ligand, steroid hormone receptors are !1thought to be weakly associated with nuclear components; !1hormone binding greatly increases receptor affinity. The !1hormone-receptor complex appears to recognize discrete DNA !1sequences upstream of transcriptional start sites. CLASSIFICATION #superfamily estrogen receptor; erbA transforming protein !1homology KEYWORDS DNA binding; nucleus; phosphoprotein; steroid binding; !1steroid hormone receptor; transcription regulation; zinc !1finger FEATURE !$1-184 #domain amino-terminal #label NH2\ !$185-276 #domain DNA binding #status predicted #label DNA\ !$188-461 #domain erbA transforming protein homology #label !8ERBA\ !$188-211 #region zinc finger CCCC motif\ !$224-246 #region zinc finger CCCC motif\ !$261-276 #region nuclear location signal\ !$305-557 #domain steroid binding #status predicted #label STB\ !$190,193,207,210 #binding_site zinc (Cys) #status predicted\ !$226,232,242,245 #binding_site zinc (Cys) #status predicted\ !$241,310 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 600 #molecular-weight 67029 #checksum 4599 SEQUENCE /// ENTRY QRCHE #type complete TITLE estrogen receptor - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 06-Mar-1992 #sequence_revision 14-Jul-1994 #text_change 22-Jun-1999 ACCESSIONS A40914; S07192 REFERENCE A40914 !$#authors Maxwell, B.L.; McDonnell, D.P.; Conneely, O.M.; Schulz, !1T.Z.; Greene, G.L.; O'Malley, B.W. !$#journal Mol. Endocrinol. (1987) 1:25-35 !$#title Structural organization and regulation of the chicken !1estrogen receptor. !$#cross-references MUID:88318621; PMID:2901032 !$#accession A40914 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-589 ##label MAX REFERENCE S07192 !$#authors Krust, A.; Green, S.; Argos, P.; Kumar, V.; Walter, P.; !1Bornert, J.M.; Chambon, P. !$#journal EMBO J. (1986) 5:891-897 !$#title The chicken oestrogen receptor sequence: homology with !1v-erbA and the human oestrogen and glucocorticoid receptors. !$#cross-references MUID:86247578; PMID:3755102 !$#accession S07192 !'##status preliminary !'##molecule_type mRNA !'##residues 1-256,'E',258-589 ##label KRU !'##cross-references EMBL:X03805; NID:g63378; PIDN:CAA27433.1; !1PID:g63380 COMMENT The steroid hormones and their receptors are involved in the !1regulation of eukaryotic gene expression and affect cellular !1proliferation and differentiation in target tissues. COMMENT In the absence of ligand, steroid hormone receptors are !1thought to be weakly associated with nuclear components; !1hormone binding greatly increases receptor affinity. The !1hormone-receptor complex appears to recognize discrete DNA !1sequences upstream of transcriptional start sites. CLASSIFICATION #superfamily estrogen receptor; erbA transforming protein !1homology KEYWORDS DNA binding; nucleus; phosphoprotein; steroid binding; !1steroid hormone receptor; transcription regulation; zinc !1finger FEATURE !$1-173 #domain amino-terminal #label NH2\ !$174-265 #domain DNA binding #status predicted #label DNA\ !$177-450 #domain erbA transforming protein homology #label !8ERBA\ !$177-200 #region zinc finger CCCC motif\ !$213-235 #region zinc finger CCCC motif\ !$250-265 #region nuclear location signal\ !$294-546 #domain steroid binding #status predicted #label STB\ !$179,182,196,199 #binding_site zinc (Cys) #status predicted\ !$215,221,231,234 #binding_site zinc (Cys) #status predicted\ !$230,299 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 589 #molecular-weight 66773 #checksum 793 SEQUENCE /// ENTRY QRXLE #type complete TITLE estrogen receptor - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 28-Feb-1992 #sequence_revision 14-Jul-1994 #text_change 15-Jun-1996 ACCESSIONS A40907 REFERENCE A40907 !$#authors Weiler, I.J.; Lew, D.; Shapiro, D.J. !$#journal Mol. Endocrinol. (1987) 1:355-362 !$#title The Xenopus laevis estrogen receptor: sequence homology with !1human and avian receptors and identification of multiple !1estrogen receptor messenger ribonucleic acids. !$#cross-references MUID:90331927; PMID:3274894 !$#accession A40907 !'##molecule_type mRNA !'##residues 1-586 ##label WEI !'##cross-references GB:L20735 COMMENT The steroid hormones and their receptors are involved in the !1regulation of eukaryotic gene expression and affect cellular !1proliferation and differentiation in target tissues. COMMENT In the absence of ligand, steroid hormone receptors are !1thought to be weakly associated with nuclear components; !1hormone binding greatly increases receptor affinity. The !1hormone-receptor complex appears to recognize discrete DNA !1sequences upstream of transcriptional start sites. CLASSIFICATION #superfamily estrogen receptor; erbA transforming protein !1homology KEYWORDS DNA binding; nucleus; phosphoprotein; steroid binding; !1steroid hormone receptor; transcription regulation; zinc !1finger FEATURE !$1-174 #domain amino-terminal #label NH2\ !$175-266 #domain DNA binding #status predicted #label DNA\ !$178-448 #domain erbA transforming protein homology #label !8ERBA\ !$178-201 #region zinc finger CCCC motif\ !$214-237 #region zinc finger CCCC motif\ !$251-266 #region nuclear location signal\ !$292-544 #domain steroid binding #status predicted #label STB\ !$180,183,197,200 #binding_site zinc (Cys) #status predicted\ !$216,222,232,235 #binding_site zinc (Cys) #status predicted\ !$231 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 586 #molecular-weight 66080 #checksum 9991 SEQUENCE /// ENTRY QRHUP #type complete TITLE progesterone receptor form B - human ALTERNATE_NAMES hPR CONTAINS progesterone receptor form A ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1987 #sequence_revision 18-Nov-1994 #text_change 22-Jun-1999 ACCESSIONS S09971; S12464; A03245 REFERENCE S09971 !$#authors Kastner, P.; Krust, A.; Turcotte, B.; Stropp, U.; Tora, L.; !1Gronemeyer, H.; Chambon, P. !$#journal EMBO J. (1990) 9:1603-1614 !$#title Two distinct estrogen-regulated promoters generate !1transcripts encoding the two functionally different human !1progesterone receptor forms A and B. !$#cross-references MUID:90228361; PMID:2328727 !$#accession S09971 !'##molecule_type mRNA !'##residues 1-933 ##label KAS !'##cross-references EMBL:X51730 REFERENCE S12464 !$#authors Kastner, P. !$#submission submitted to the EMBL Data Library, February 1990 !$#accession S12464 !'##molecule_type mRNA !'##residues 1-343,'T',345-933 ##label KA2 !'##cross-references EMBL:X51730; NID:g35651; PIDN:CAA36018.1; !1PID:g35652 REFERENCE A03245 !$#authors Misrahi, M.; Atger, M.; D'Auriol, L.; Loosfelt, H.; Meriel, !1C.; Fridlansky, F.; Guiochon-Mantel, A.; Galibert, F.; !1Milgrom, E. !$#journal Biochem. Biophys. Res. Commun. (1987) 143:740-748 !$#title Complete amino acid sequence of the human progesterone !1receptor deduced from cloned cDNA. !$#cross-references MUID:87184565; PMID:3551956 !$#accession A03245 !'##molecule_type mRNA !'##residues 1-225,'G',227-255,'V',257-659,'V',661-933 ##label MIS !'##cross-references GB:M15716; NID:g189934; PIDN:AAA60081.1; !1PID:g189935 GENETICS !$#gene GDB:PGR !'##cross-references GDB:119493; OMIM:264080 !$#map_position 11q22.1-11q22.3 CLASSIFICATION #superfamily progesterone receptor; erbA transforming !1protein homology KEYWORDS alternative splicing; DNA binding; nucleus; phosphoprotein; !1steroid hormone receptor; transcription regulation; zinc !1finger FEATURE !$1-933 #product progesterone receptor form B #status !8predicted #label MA1\ !$165-933 #product progesterone receptor form A #status !8predicted #label MA2\ !$565-829 #domain erbA transforming protein homology #label !8ERBA\ !$567-587 #region zinc finger CCCC motif\ !$603-627 #region zinc finger CCCC motif\ !$681-933 #domain steroid binding #status predicted #label STB\ !$41 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$227,232,552,793 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$329,374,601 #binding_site phosphate (Tyr) (covalent) #status !8predicted SUMMARY #length 933 #molecular-weight 99028 #checksum 5865 SEQUENCE /// ENTRY QRHUGA #type complete TITLE glucocorticoid receptor, alpha splice form - human ALTERNATE_NAMES hGR ORGANISM #formal_name Homo sapiens #common_name man DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 21-Jul-2000 ACCESSIONS A93370; A39837; A39779; I56596; A03246; A32196 REFERENCE A93370 !$#authors Hollenberg, S.M.; Weinberger, C.; Ong, E.S.; Cerelli, G.; !1Oro, A.; Lebo, R.; Thompson, E.B.; Rosenfeld, M.G.; Evans, !1R.M. !$#journal Nature (1985) 318:635-641 !$#title Primary structure and expression of a functional human !1glucocorticoid receptor cDNA. !$#cross-references MUID:86092206; PMID:2867473 !$#accession A93370 !'##molecule_type mRNA !'##residues 1-777 ##label HOL !'##cross-references EMBL:X03225; GB:M10901; NID:g31679; !1PIDN:CAA26976.1; PID:g31680 REFERENCE A39837 !$#authors Leclerc, S.; Xie, B.; Roy, R.; Govindan, M.V. !$#journal J. Biol. Chem. (1991) 266:8711-8719 !$#title Purification of a human glucocorticoid receptor gene !1promoter-binding protein. Production of polyclonal !1antibodies against the purified factor. !$#cross-references MUID:91224961; PMID:2026589 !$#accession A39837 !'##molecule_type DNA !'##residues 1-394 ##label LEC !'##cross-references GB:M69104; NID:g183605; PIDN:AAA88049.1; !1PID:g553322 REFERENCE A39779 !$#authors Encio, I.J.; Detera-Wadleigh, S.D. !$#journal J. Biol. Chem. (1991) 266:7182-7188 !$#title The genomic structure of the human glucocorticoid receptor. !$#cross-references MUID:91201378; PMID:1707881 !$#accession A39779 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type DNA !'##residues 385-404;441-459;480-498;573-593;621-640;665-685;718-737 !1##label ENC !'##cross-references GB:M60597 !'##experimental_source placenta REFERENCE A93373 !$#authors Weinberger, C.; Hollenberg, S.M.; Rosenfeld, M.G.; Evans, !1R.M. !$#journal Nature (1985) 318:670-672 !$#title Domain structure of human glucocorticoid receptor and its !1relationship to the v-erb-A oncogene product. !$#cross-references MUID:86092211; PMID:3841189 !$#contents annotation; domains REFERENCE A32196 !$#authors Dahlman, K.; Stroemstedt, P.E.; Rae, C.; Joernvall, H.; !1Flock, J.I.; Carlstedt-Duke, J.; Gustafsson, J.A. !$#journal J. Biol. Chem. (1989) 264:804-809 !$#title High level expression in Escherichia coli of the DNA-binding !1domain of the glucocorticoid receptor in a functional form !1utilizing domain-specific cleavage of a fusion protein. !$#cross-references MUID:89093147; PMID:2642905 !$#contents annotation; domains !$#note engineered sequence expressed in Escherichia coli REFERENCE I56596 !$#authors Govindan, M.V.; Pothier, F.; Leclerc, S.; Palaniswami, R.; !1Xie, B. !$#journal J. Steroid Biochem. Mol. Biol. (1991) 40:317-323 !$#title Human glucocorticoid receptor gene promotor-homologous down !1regulation. !$#cross-references MUID:92068829; PMID:1958537 !$#accession I56596 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-394 ##label RES !'##cross-references GB:S68378; NID:g239757; PIDN:AAB20466.1; !1PID:g239758 COMMENT Alpha and beta (see PIR:QRUGB) splice forms differ in their !1carboxyl-terminal sequences. This protein is the predominant !1physiological form. GENETICS !$#gene GDB:GRL !'##cross-references GDB:120017; OMIM:138040 !$#map_position 5q31-5q31 !$#introns 395/2; 451/1; 490/1; 583/1; 631/2; 675/1; 727/3 !$#note the first intron occurs before the initiator codon CLASSIFICATION #superfamily glucocorticoid receptor; erbA transforming !1protein homology KEYWORDS alternative splicing; DNA binding; nucleus; steroid hormone !1receptor; transcription regulation; zinc finger FEATURE !$419-674 #domain erbA transforming protein homology #label !8ERBA\ !$421-441 #region zinc finger CCCC motif\ !$457-481 #region zinc finger CCCC motif\ !$728-777 #domain steroid binding #status predicted #label STB SUMMARY #length 777 #molecular-weight 85659 #checksum 6124 SEQUENCE /// ENTRY QRHUGB #type complete TITLE glucocorticoid receptor, beta splice form - human ALTERNATE_NAMES hGR ORGANISM #formal_name Homo sapiens #common_name man DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 21-Jul-2000 ACCESSIONS B93370; B39779; A03247 REFERENCE A93370 !$#authors Hollenberg, S.M.; Weinberger, C.; Ong, E.S.; Cerelli, G.; !1Oro, A.; Lebo, R.; Thompson, E.B.; Rosenfeld, M.G.; Evans, !1R.M. !$#journal Nature (1985) 318:635-641 !$#title Primary structure and expression of a functional human !1glucocorticoid receptor cDNA. !$#cross-references MUID:86092206; PMID:2867473 !$#accession B93370 !'##molecule_type mRNA !'##residues 1-742 ##label HOL !'##cross-references EMBL:X03348; GB:M11050; NID:g31681; !1PIDN:CAA27054.1; PID:g31682 REFERENCE A39779 !$#authors Encio, I.J.; Detera-Wadleigh, S.D. !$#journal J. Biol. Chem. (1991) 266:7182-7188 !$#title The genomic structure of the human glucocorticoid receptor. !$#cross-references MUID:91201378; PMID:1707881 !$#accession B39779 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type DNA !'##residues 385-404;441-459;480-498;573-593;621-640;665-685;718-737 !1##label ENC !'##cross-references GB:M60597 !'##experimental_source placenta REFERENCE A93373 !$#authors Weinberger, C.; Hollenberg, S.M.; Rosenfeld, M.G.; Evans, !1R.M. !$#journal Nature (1985) 318:670-672 !$#title Domain structure of human glucocorticoid receptor and its !1relationship to the v-erb-A oncogene product. !$#cross-references MUID:86092211; PMID:3841189 !$#contents annotation; domains COMMENT Alpha (see PIR:QRHUGA) and beta splice forms differ in their !1carboxyl-terminal sequences. The in vitro translation !1product of the beta form does not bind steroid. Its function !1is unclear; however, it is possible that variant receptors !1perform tissue-specific functions. GENETICS !$#gene GDB:GRL !'##cross-references GDB:120017; OMIM:138040 !$#map_position 5q31-5q31 !$#introns 395/2; 451/1; 490/1; 583/1; 631/2; 675/1; 727/3 !$#note the first intron occurs before the initiator codon CLASSIFICATION #superfamily glucocorticoid receptor; erbA transforming !1protein homology KEYWORDS alternative splicing; DNA binding; nucleus; steroid hormone !1receptor; transcription regulation; zinc finger FEATURE !$419-674 #domain erbA transforming protein homology #label !8ERBA\ !$421-441 #region zinc finger CCCC motif\ !$457-481 #region zinc finger CCCC motif SUMMARY #length 742 #molecular-weight 81509 #checksum 6904 SEQUENCE /// ENTRY QRRTG #type complete TITLE glucocorticoid receptor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 22-Jun-1999 ACCESSIONS A24194; S02475; A27284; S33888; S33891 REFERENCE A24194 !$#authors Miesfeld, R.; Rusconi, S.; Godowski, P.J.; Maler, B.A.; !1Okret, S.; Wikstrom, A.C.; Gustafsson, J.A.; Yamamoto, K.R. !$#journal Cell (1986) 46:389-399 !$#title Genetic complementation of a glucocorticoid receptor !1deficiency by expression of cloned receptor cDNA. !$#cross-references MUID:86272086; PMID:3755378 !$#accession A24194 !'##molecule_type mRNA !'##residues 1-795 ##label MIE !'##cross-references GB:M14053; NID:g204271; PIDN:AAA41203.1; !1PID:g204272 REFERENCE S02475 !$#authors Severne, Y.; Wieland, S.; Schaffner, W.; Rusconi, S. !$#journal EMBO J. (1988) 7:2503-2508 !$#title Metal binding 'finger' structures in the glucocorticoid !1receptor defined by site-directed mutagenesis. !$#cross-references MUID:89052664; PMID:3191912 !$#accession S02475 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 440-539 ##label SEV REFERENCE A27284 !$#authors Chang, C.; Kokontis, J.; Chang, C.T.; Liao, S. !$#journal Nucleic Acids Res. (1987) 15:9603 !$#title Cloning and sequence analysis of the rat ventral prostate !1glucocorticoid receptor cDNA. !$#cross-references MUID:88067783; PMID:3684608 !$#accession A27284 !'##molecule_type mRNA !'##residues 1-97,'D',99-225,'G',227-259,'D',261-344,'T',346-515 ##label !1CHA !'##cross-references GB:Y00489; NID:g56324; PIDN:CAA68545.1; PID:g56325 REFERENCE S33888 !$#authors Gearing, K.L.; Gustafsson, J.A.; Okret, S. !$#journal Nucleic Acids Res. (1993) 21:2014 !$#title Heterogeneity in the polyglutamine tract of the !1glucocorticoid receptor from different rat strains. !$#cross-references MUID:93261843; PMID:8493115 !$#accession S33888 !'##status preliminary !'##molecule_type DNA !'##residues 68-97,'D',99-104 ##label GEA !'##cross-references EMBL:X69666 !$#accession S33891 !'##status preliminary !'##molecule_type DNA !'##residues 68-92,97,'D',99-104 ##label GE2 !'##cross-references EMBL:X69669 COMMENT This sequence contains five potential translation !1initiators: 1-Met, 28-Met, 107-Met, 111-Met, and 119-Met. !1Multiple receptors are observed in vivo and in vitro, but !1the major species found is initiated from 1-Met. CLASSIFICATION #superfamily glucocorticoid receptor; erbA transforming !1protein homology KEYWORDS DNA binding; nucleus; steroid hormone receptor; !1transcription regulation; zinc finger FEATURE !$75-96 #region glutamine-rich\ !$438-692 #domain erbA transforming protein homology #label !8ERBA\ !$440-460 #region zinc finger CCCC motif\ !$476-500 #region zinc finger CCCC motif SUMMARY #length 795 #molecular-weight 87498 #checksum 1049 SEQUENCE /// ENTRY A25691 #type complete TITLE glucocorticoid receptor - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 05-Jun-1988 #sequence_revision 18-Nov-1994 #text_change 22-Jun-1999 ACCESSIONS A25691; S02212; S02214 REFERENCE A25691 !$#authors Danielsen, M.; Northrop, J.P.; Ringold, G.M. !$#journal EMBO J. (1986) 5:2513-2522 !$#title The mouse glucocorticoid receptor: mapping of functional !1domains by cloning, sequencing and expression of wild-type !1and mutant receptor proteins. !$#cross-references MUID:87053816; PMID:3780669 !$#accession A25691 !'##molecule_type mRNA !'##residues 1-783 ##label DAN !'##cross-references GB:X04435; NID:g51057; PIDN:CAA28031.1; PID:g51058 REFERENCE S02212 !$#authors Nohno, T.; Kasai, Y.; Saito, T. !$#journal Nucleic Acids Res. (1989) 17:445 !$#title Novel cDNA sequence possibly generated by alternative !1splicing of a mouse glucocorticoid receptor gene transcript !1from Shionogi carcinoma 115. !$#cross-references MUID:89098404; PMID:2911477 !$#accession S02212 !'##molecule_type mRNA !'##residues 1-436,'G',438-755 ##label NOH !'##cross-references EMBL:X13358; NID:g51117; PIDN:CAA31738.1; !1PID:g51118 !'##note neither the complete nucleic acid sequence nor the complete !1translation are shown !$#accession S02214 !'##molecule_type mRNA !'##residues 1-436,'G',438-458,'R',459-755 ##label NO2 !'##cross-references EMBL:X13359; NID:g51119; PIDN:CAA31739.1; !1PID:g51120 !'##note neither the complete nucleic acid sequence nor the complete !1translation are shown CLASSIFICATION #superfamily glucocorticoid receptor; erbA transforming !1protein homology KEYWORDS alternative splicing; DNA binding; nucleus; steroid hormone !1receptor; transcription regulation; zinc finger FEATURE !$75-82 #region glutamine-rich\ !$426-680 #domain erbA transforming protein homology #label !8ERBA\ !$428-448 #region zinc finger CCCC motif\ !$464-488 #region zinc finger CCCC motif\ !$734-783 #domain steroid binding #status predicted #label STB SUMMARY #length 783 #molecular-weight 86052 #checksum 779 SEQUENCE /// ENTRY S44047 #type complete TITLE glucocorticoid receptor - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 13-Jan-1995 #sequence_revision 27-Oct-1995 #text_change 22-Jun-1999 ACCESSIONS S45348; S44047; S42083 REFERENCE S45348 !$#authors Gao, X.; Kalkhoven, E.; Peterson-Maduro, J.; van der Burg, !1B.; Destree, O.H.J. !$#journal Biochim. Biophys. Acta (1994) 1218:194-198 !$#title Expression of the glucocorticoid receptor gene is regulated !1during early embryogenesis of Xenopus laevis. !$#cross-references MUID:94289478; PMID:8018720 !$#accession S45348 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-776 ##label GAO !'##cross-references EMBL:X72211 !'##experimental_source embryonic stage 17 REFERENCE S44047 !$#authors Gao, X.; Kalkhoven, E.; Peterson-Maduro, J.; van der Burg, !1B.; Destree, O.H.J. !$#submission submitted to the EMBL Data Library, May 1993 !$#description The expression of glucocorticoid receptor gene is regulated !1during early Xenopus laevis embryonic development. !$#accession S44047 !'##molecule_type mRNA !'##residues 1-271,'R',273-776 ##label GAW !'##cross-references EMBL:X72211; NID:g444042; PIDN:CAA51010.1; !1PID:g444043 !'##experimental_source embryonic stage 17 REFERENCE S42083 !$#authors Picard, D. !$#submission submitted to the EMBL Data Library, February 1994 !$#accession S42083 !'##molecule_type mRNA !'##residues 452-501,'P',503,'A',505,'A',507-510,'N',512-518,'M', !1520-543,'F',545-550,'M',552-653,'R',655-739,'M',741-767,'I', !1769-776 ##label PIC !'##cross-references EMBL:X77764; NID:g456373; PIDN:CAA54804.1; !1PID:g456374 !'##experimental_source liver CLASSIFICATION #superfamily glucocorticoid receptor; erbA transforming !1protein homology KEYWORDS DNA binding; nucleus; steroid hormone receptor; !1transcription regulation; zinc finger FEATURE !$418-673 #domain erbA transforming protein homology #label !8ERBA\ !$420-440 #region zinc finger CCCC motif\ !$456-480 #region zinc finger CCCC motif SUMMARY #length 776 #molecular-weight 84917 #checksum 2612 SEQUENCE /// ENTRY A46077 #type complete TITLE steroid hormone receptor Ad4BP - bovine ALTERNATE_NAMES steroid hydroxylase positive regulator; steroidogenic factor 1; transcription factor ad4bp; transcription factor SF-1 ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A46077 REFERENCE A46077 !$#authors Honda, S.; Morohashi, K.; Nomura, M.; Takeya, H.; Kitajima, !1M.; Omura, T. !$#journal J. Biol. Chem. (1993) 268:7494-7502 !$#title Ad4BP regulating steroidogenic P-450 gene is a member of !1steroid hormone receptor superfamily. !$#cross-references MUID:93216698; PMID:8463279 !$#accession A46077 !'##molecule_type mRNA !'##residues 1-461 ##label HON !'##cross-references GB:D13569; NID:g217431; PIDN:BAA02764.1; !1PID:g217432 FUNCTION !$#description transcription activator for CYP11B and other steroidogenic !1cytochrome P-450 genes with an Ad4 element in the promoter !1region CLASSIFICATION #superfamily steroid hormone receptor Ad4BP; erbA !1transforming protein homology KEYWORDS DNA binding; nucleus; steroid hormone receptor; !1transcription factor; zinc finger FEATURE !$11-379 #domain erbA transforming protein homology #label !8ERBA\ !$13-33 #region zinc finger CCCC motif\ !$49-73 #region zinc finger CCCC motif SUMMARY #length 461 #molecular-weight 51612 #checksum 5196 SEQUENCE /// ENTRY A56120 #type complete TITLE steroid hormone receptor Ad4BP - rat ALTERNATE_NAMES steroid hydroxylase positive regulator; steroidogenic factor 1; transcription factor ad4bp; transcription factor SF-1 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A56120; A40704 REFERENCE A56120 !$#authors Nomura, M.; Baertsch, S.; Nawata, H.; Omura, T.; Morohashi, !1K. !$#journal J. Biol. Chem. (1995) 270:7453-7461 !$#title An E box element is required for the expression of the ad4bp !1gene, a mammalian homologue of ftz-f1 gene, which is !1essential for adrenal and gonadal development. !$#cross-references MUID:95221406; PMID:7706291 !$#accession A56120 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-462 ##label NOM !'##cross-references GB:D42151 REFERENCE A40704 !$#authors Lynch, J.P.; Lala, D.S.; Peluso, J.J.; Luo, W.; Parker, !1K.L.; White, B.A. !$#journal Mol. Endocrinol. (1993) 7:776-786 !$#title Steroidogenic factor 1, an orphan nuclear receptor, !1regulates the expression of the rat aromatase gene in !1gonadal tissues. !$#cross-references MUID:93368604; PMID:8395654 !$#accession A40704 !'##status preliminary !'##molecule_type DNA !'##residues 20-149,'R',151-293 ##label LYN !'##experimental_source R2C Leydig tumor cells !'##note sequence inconsistent with nucleotide translation !'##note sequence extracted from NCBI backbone (NCBIN:136880, !1NCBIP:136881) GENETICS !$#gene ad4bp FUNCTION !$#description transcription activator for CYP11B and other steroidogenic !1cytochrome P-450 genes with an Ad4 element in the promoter !1region CLASSIFICATION #superfamily steroid hormone receptor Ad4BP; erbA !1transforming protein homology KEYWORDS DNA binding; nucleus; steroid hormone receptor; !1transcription factor; zinc finger FEATURE !$11-380 #domain erbA transforming protein homology #label !8ERBA\ !$13-33 #region zinc finger CCCC motif\ !$49-73 #region zinc finger CCCC motif SUMMARY #length 462 #molecular-weight 52087 #checksum 2031 SEQUENCE /// ENTRY A56543 #type complete TITLE Ftz-F1-related orphan receptor A - African clawed frog ALTERNATE_NAMES xFF1rA protein ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A56543 REFERENCE A56543 !$#authors Ellinger-Ziegelbauer, H.; Hihi, A.K.; Laudet, V.; Keller, !1H.; Wahli, W.; Dreyer, C. !$#journal Mol. Cell. Biol. (1994) 14:2786-2797 !$#title FTZ-F1-related orphan receptors in Xenopus laevis: !1transcriptional regulators differentially expressed during !1early embryogenesis. !$#cross-references MUID:94187748; PMID:8139576 !$#accession A56543 !'##status preliminary !'##molecule_type mRNA !'##residues 1-501 ##label ELL !'##cross-references GB:U05001; NID:g451660; PIDN:AAA18356.1; !1PID:g451661 GENETICS !$#gene xFF1rA FUNCTION !$#description transcription regulation; probably a steroid hormone !1receptor CLASSIFICATION #superfamily steroid hormone receptor Ad4BP; erbA !1transforming protein homology KEYWORDS DNA binding; nucleus; steroid hormone receptor; !1transcription factor; zinc finger FEATURE !$44-419 #domain erbA transforming protein homology #label !8ERBA\ !$46-66 #region zinc finger CCCC motif\ !$82-106 #region zinc finger CCCC motif SUMMARY #length 501 #molecular-weight 56986 #checksum 2256 SEQUENCE /// ENTRY S33708 #type complete TITLE nuclear steroid/thyroid hormone receptor beta protein FTZ-F1beta - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES DHR39 protein ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S33708; A56562 REFERENCE S33708 !$#authors Ayer, S.; Walker, N.; Mosammaparast, M.; Nelson, J.P.; !1Shilo, B.; Benyajati, C. !$#journal Nucleic Acids Res. (1993) 21:1619-1627 !$#title Activation and repression of Drosophila alcohol !1dehydrogenase distal transcription by two steroid hormone !1receptor superfamily members binding to a common response !1element. !$#cross-references MUID:93241944; PMID:8479913 !$#accession S33708 !'##status preliminary !'##molecule_type mRNA !'##residues 1-808 ##label AYE !'##cross-references EMBL:L07549; NID:g157231; PID:g157232 REFERENCE A56562 !$#authors Ohno, C.K.; Petkovich, M. !$#journal Mech. Dev. (1993) 40:13-24 !$#title FTZ-F1 beta, a novel member of the Drosophila nuclear !1receptor family. !$#cross-references MUID:93183764; PMID:8382937 !$#accession A56562 !'##status preliminary !'##molecule_type DNA !'##residues 1-202,'L',204-388,'G',390-762,'P',764-808 ##label OHN !'##cross-references GB:L06423; NID:g290225; PID:g290226 !'##note sequence extracted from NCBI backbone (NCBIN:126878, !1NCBIP:126879) GENETICS !$#gene FlyBase:Hr39; FlyBase:ftz-f1 !'##cross-references FlyBase:FBgn0010229; FlyBase:FBgn0001078 CLASSIFICATION #superfamily nuclear steroid/thyroid hormone receptor beta !1protein FTZ-F1beta; erbA transforming protein homology KEYWORDS DNA binding; steroid hormone receptor; transcription factor; !1zinc finger FEATURE !$374-729 #domain erbA transforming protein homology #label !8ERBA SUMMARY #length 808 #molecular-weight 87362 #checksum 2493 SEQUENCE /// ENTRY S33709 #type complete TITLE DHR39-short protein - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S33709 REFERENCE S33708 !$#authors Ayer, S.; Walker, N.; Mosammaparast, M.; Nelson, J.P.; !1Shilo, B.; Benyajati, C. !$#journal Nucleic Acids Res. (1993) 21:1619-1627 !$#title Activation and repression of Drosophila alcohol !1dehydrogenase distal transcription by two steroid hormone !1receptor superfamily members binding to a common response !1element. !$#cross-references MUID:93241944; PMID:8479913 !$#accession S33709 !'##status preliminary !'##molecule_type mRNA !'##residues 1-701 ##label AYE !'##cross-references EMBL:L07550; NID:g157233; PID:g157234 GENETICS !$#gene FlyBase:Hr39 !'##cross-references FlyBase:FBgn0010229 CLASSIFICATION #superfamily fruit fly DHR39-short protein; erbA !1transforming protein homology FEATURE !$374-701 #domain erbA transforming protein homology #status !8atypical #label ERBA SUMMARY #length 701 #molecular-weight 74802 #checksum 6652 SEQUENCE /// ENTRY TVHUAR #type complete TITLE thyroid hormone receptor beta - human ALTERNATE_NAMES erbA transforming protein ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 22-Jun-1999 ACCESSIONS A25237; I52900 REFERENCE A25237 !$#authors Weinberger, C.; Thompson, C.C.; Ong, E.S.; Lebo, R.; Gruol, !1D.J.; Evans, R.M. !$#journal Nature (1986) 324:641-646 !$#title The c-erb-A gene encodes a thyroid hormone receptor. !$#cross-references MUID:87090375; PMID:2879243 !$#accession A25237 !'##molecule_type mRNA !'##residues 1-456 ##label WEI !'##cross-references EMBL:X04707; NID:g31206; PIDN:CAA28412.1; !1PID:g31207 REFERENCE I52900 !$#authors Weinberger, C.; Giguere, V.; Hollenberg, S.; Rosenfeld, !1M.G.; Evans, R.M. !$#journal Cold Spring Harb. Symp. Quant. Biol. (1988) 51:759-772 !$#title Human steroid receptors and erbA proto-oncogene products: !1Members of a new superfamily of enhancer binding proteins. !$#cross-references MUID:87217099; PMID:3034496 !$#accession I52900 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-456 ##label WE2 !'##cross-references GB:M26747; NID:g180252; PIDN:AAA35677.1; !1PID:g180253 GENETICS !$#gene GDB:THRB; ERBA2 !'##cross-references GDB:120731; OMIM:190160 !$#map_position 3p24.1-3p22 CLASSIFICATION #superfamily thyroid hormone receptor; erbA transforming !1protein homology KEYWORDS DNA binding; nucleus; proto-oncogene; thyroid hormone !1receptor; transcription regulation; zinc finger FEATURE !$100-376 #domain erbA transforming protein homology #label !8ERBA\ !$102-122 #region zinc finger CCCC motif\ !$140-164 #region zinc finger CCCC motif\ !$239-456 #domain hormone binding #status predicted #label HRB SUMMARY #length 456 #molecular-weight 52176 #checksum 1688 SEQUENCE /// ENTRY TVCHTB #type complete TITLE thyroid hormone receptor beta - chicken ALTERNATE_NAMES erbA transforming protein ORGANISM #formal_name Gallus gallus #common_name chicken DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 22-Jun-1999 ACCESSIONS S09625; A38460 REFERENCE S09625 !$#authors Forrest, D.; Sjoeberg, M.; Vennstroem, B. !$#journal EMBO J. (1990) 9:1519-1528 !$#title Contrasting developmental and tissue-specific expression of !1alpha and beta thyroid hormone receptor genes. !$#cross-references MUID:90228351; PMID:1970296 !$#accession S09625 !'##molecule_type mRNA !'##residues 1-369 ##label FOR !'##cross-references EMBL:X17504 !'##experimental_source kidney REFERENCE A38460 !$#authors Showers, M.O.; Darling, D.S.; Kieffer, G.D.; Chin, W.W. !$#journal DNA Cell Biol. (1991) 10:211-221 !$#title Isolation and characterization of a cDNA encoding a chicken !1beta thyroid hormone receptor. !$#cross-references MUID:91190272; PMID:1707280 !$#accession A38460 !'##molecule_type mRNA !'##residues 1-116,'V',118-143,'V',145-201,'L',203-214,'V',216-369 !1##label SHO !'##cross-references GB:M65207; NID:g212801; PIDN:AAA49107.1; !1PID:g212802 !'##experimental_source liver !'##note the authors translated the codon GTT for residue 117 as Gly, !1GTA for residue 144 as Gly, TTG for residue 202 as Cys, and !1GTC for residue 215 as Gly CLASSIFICATION #superfamily thyroid hormone receptor; erbA transforming !1protein homology KEYWORDS DNA binding; nucleus; proto-oncogene; thyroid hormone !1receptor; transcription regulation; zinc finger FEATURE !$13-289 #domain erbA transforming protein homology #label !8ERBA\ !$14-82 #domain DNA binding #status predicted #label DNA\ !$15-35 #region zinc finger CCCC motif\ !$53-77 #region zinc finger CCCC motif\ !$132-369 #domain hormone binding #status predicted #label HRB SUMMARY #length 369 #molecular-weight 42115 #checksum 5182 SEQUENCE /// ENTRY TVRTAR #type complete TITLE thyroid hormone receptor alpha-2 - rat ALTERNATE_NAMES transforming protein (erbA) homolog ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 22-Jun-1999 ACCESSIONS A36752; A40923; S00927; A35581 REFERENCE A36752 !$#authors Nikodem, V. !$#submission submitted to the EMBL Data Library, April 1988 !$#accession A36752 !'##molecule_type mRNA !'##residues 1-454 ##label NIK !'##cross-references EMBL:X07409; NID:g57390; PIDN:CAA30307.1; !1PID:g57391 REFERENCE A40923 !$#authors Lazar, M.A.; Chin, W.W. !$#journal Mol. Endocrinol. (1988) 2:479-484 !$#title Regulation of two c-erbA messenger ribonucleic acids in rat !1GH-3 cells by thyroid hormone. !$#cross-references MUID:88334548; PMID:2901667 !$#accession A40923 !'##molecule_type mRNA !'##residues 82-443,'C',445-454 ##label LAZ !'##cross-references GB:M31177; NID:g204049; PIDN:AAA41122.1; !1PID:g204050 REFERENCE S00927 !$#authors Mitsuhashi, T.; Tennyson, G.; Nikodem, V. !$#journal Nucleic Acids Res. (1988) 16:5697 !$#title Nucleotide sequence of novel cDNAs generated by alternative !1splicing of a rat thyroid hormone receptor gene transcript. !$#cross-references MUID:88262581; PMID:3387247 !$#accession S00927 !'##status translation not shown !'##molecule_type mRNA !'##residues 333-454 ##label MIT REFERENCE A35581 !$#authors Mitsuhashi, T.; Tennyson, G.E.; Nikodem, V.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:5804-5808 !$#title Alternative splicing generates messages encoding rat c-erbA !1proteins that do not bind thyroid hormone. !$#cross-references MUID:88320332; PMID:2901090 !$#accession A35581 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type mRNA !'##residues 333-454 ##label MI2 CLASSIFICATION #superfamily thyroid hormone receptor; erbA transforming !1protein homology KEYWORDS alternative splicing; DNA binding; nucleus; proto-oncogene; !1thyroid hormone receptor; transcription regulation; zinc !1finger FEATURE !$13-289 #domain erbA transforming protein homology #label !8ERBA\ !$15-35 #region zinc finger CCCC motif\ !$53-77 #region zinc finger CCCC motif SUMMARY #length 454 #molecular-weight 50900 #checksum 5434 SEQUENCE /// ENTRY QRMSA1 #type complete TITLE thyroid hormone receptor alpha-1 - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 22-Jun-1999 ACCESSIONS S14690; S08690 REFERENCE S14690 !$#authors Masuda, M.; Yasuhara, S.; Yamashita, M.; Shibuya, M.; Odaka, !1T. !$#journal Nucleic Acids Res. (1990) 18:3055 !$#title Nucleotide sequence of the murine thyroid hormone receptor !1(alpha-1) cDNA. !$#cross-references MUID:90272421; PMID:2349106 !$#accession S14690 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-410 ##label MAS !'##cross-references EMBL:X51983; NID:g50385; PIDN:CAA36241.1; !1PID:g50386 GENETICS !$#gene erbA-alpha CLASSIFICATION #superfamily thyroid hormone receptor; erbA transforming !1protein homology KEYWORDS alternative splicing; DNA binding; proto-oncogene; thyroid !1hormone receptor; transcription regulation; zinc finger FEATURE !$51-327 #domain erbA transforming protein homology #label !8ERBA\ !$53-73 #region zinc finger CCCC motif\ !$91-115 #region zinc finger CCCC motif\ !$190-410 #domain hormone binding #status predicted #label HRB SUMMARY #length 410 #molecular-weight 46804 #checksum 3176 SEQUENCE /// ENTRY TVXLTA #type complete TITLE thyroid hormone receptor alpha-1 - African clawed frog ALTERNATE_NAMES thyroid hormone receptor alpha-A ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 22-Jun-1999 ACCESSIONS S09605; A36067 REFERENCE S09605 !$#authors Brooks, A.R.; Sweeney, G.; Old, R.W. !$#journal Nucleic Acids Res. (1989) 17:9395-9405 !$#title Structure and functional expression of a cloned Xenopus !1thyroid hormone receptor. !$#cross-references MUID:90067936; PMID:2587261 !$#accession S09605 !'##molecule_type mRNA !'##residues 1-418 ##label BRO !'##cross-references EMBL:X17385; NID:g65141; PIDN:CAA35252.1; !1PID:g65142 REFERENCE A36067 !$#authors Yaoita, Y.; Shi, Y.; Brown, D.D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:7090-7094 !$#title Xenopus laevis alpha and beta thyroid hormone receptors. !$#cross-references MUID:90384953; PMID:2402492 !$#accession A36067 !'##molecule_type mRNA !'##residues 1-53,'Y',55-136,'G',138-418 ##label YAO !'##cross-references GB:M35343; NID:g214829; PIDN:AAA49969.1; !1PID:g214830 CLASSIFICATION #superfamily thyroid hormone receptor; erbA transforming !1protein homology KEYWORDS DNA binding; nucleus; thyroid hormone receptor; !1transcription regulation; zinc finger FEATURE !$59-335 #domain erbA transforming protein homology #label !8ERBA\ !$60-128 #domain DNA binding #status predicted #label DNA\ !$61-81 #region zinc finger CCCC motif\ !$99-123 #region zinc finger CCCC motif\ !$178-415 #domain hormone binding #status predicted #label HRB SUMMARY #length 418 #molecular-weight 47676 #checksum 1663 SEQUENCE /// ENTRY TVCHVR #type complete TITLE thyroid hormone receptor alpha - chicken ALTERNATE_NAMES erbA transforming protein ORGANISM #formal_name Gallus gallus #common_name chicken DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 22-Jun-1999 ACCESSIONS A25236; S00029 REFERENCE A25236 !$#authors Sap, J.; Munoz, A.; Damm, K.; Goldberg, Y.; Ghysdael, J.; !1Leutz, A.; Beug, H.; Vennstrom, B. !$#journal Nature (1986) 324:635-640 !$#title The c-erb-A protein is a high-affinity receptor for thyroid !1hormone. !$#cross-references MUID:87090374; PMID:2879242 !$#accession A25236 !'##molecule_type mRNA !'##residues 1-408 ##label SAP !'##cross-references GB:Y00987; NID:g63177; PIDN:CAA68792.1; PID:g63178 REFERENCE S00029 !$#authors Zahraoui, A.; Cuny, G. !$#journal Eur. J. Biochem. (1987) 166:63-69 !$#title Nucleotide sequence of the chicken proto-oncogene c-erbA !1corresponding to domain 1 of v-erbA. !$#cross-references MUID:87246693; PMID:3036525 !$#accession S00029 !'##molecule_type DNA !'##residues 1-239 ##label ZAH !'##cross-references GB:X04858 GENETICS !$#gene erbA CLASSIFICATION #superfamily thyroid hormone receptor; erbA transforming !1protein homology KEYWORDS DNA binding; nucleus; phosphoprotein; proto-oncogene; !1thyroid hormone receptor; transcription regulation; zinc !1finger FEATURE !$49-325 #domain erbA transforming protein homology #label !8ERBA\ !$51-118 #domain DNA binding #status predicted #label DNA\ !$51-71 #region zinc finger CCCC motif\ !$89-113 #region zinc finger CCCC motif\ !$168-408 #domain hormone binding #status predicted #label HRB SUMMARY #length 408 #molecular-weight 46757 #checksum 1498 SEQUENCE /// ENTRY TVFVVR #type complete TITLE transforming protein erbA - avian erythroblastosis virus ORGANISM #formal_name avian erythroblastosis virus #note host Gallus gallus (chicken) DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 29-Oct-1999 ACCESSIONS A03248; S35744 REFERENCE A38022 !$#authors Debuire, B.; Henry, C.; Benaissa, M.; Biserte, G.; Claverie, !1J.M.; Saule, S.; Martin, P.; Stehelin, D. !$#journal Science (1984) 224:1456-1459 !$#title Sequencing the erbA gene of avian erythroblastosis virus !1reveals a new type of oncogene. !$#cross-references MUID:84223957; PMID:6328658 !$#accession A03248 !'##molecule_type genomic RNA !'##residues 1-398 ##label DEB !'##cross-references GB:K02006 REFERENCE S35743 !$#authors Vennstroem, B. !$#submission submitted to the EMBL Data Library, March 1993 !$#accession S35744 !'##status preliminary !'##molecule_type DNA !'##residues 'EP',1-380,'S',382,'QEV' ##label VEN !'##cross-references EMBL:X12707 COMMENT This protein is synthesized as a gag-erbA polyprotein. GENETICS !$#gene erbA CLASSIFICATION #superfamily thyroid hormone receptor; erbA transforming !1protein homology KEYWORDS DNA binding; oncogene; polyprotein; transcription !1regulation; transforming protein; zinc finger FEATURE !$35-311 #domain erbA transforming protein homology #label !8ERBA\ !$37-57 #region zinc finger CCCC motif\ !$75-99 #region zinc finger CCCC motif SUMMARY #length 398 #molecular-weight 45506 #checksum 2528 SEQUENCE /// ENTRY A29491 #type complete TITLE retinoic acid receptor alpha - human ORGANISM #formal_name Homo sapiens #common_name man DATE 04-Jun-1999 #sequence_revision 04-Jun-1999 #text_change 16-Jun-2000 ACCESSIONS A29491; S07272; S06224; S15598; A58975; A29740; S15599 REFERENCE A29491 !$#authors Giguere, V.; Ong, E.S.; Segui, P.; Evans, R.M. !$#journal Nature (1987) 330:624-629 !$#title Identification of a receptor for the morphogen retinoic !1acid. !$#cross-references MUID:88065922; PMID:2825036 !$#accession A29491 !'##molecule_type mRNA !'##residues 1-462 ##label GIG !'##cross-references GB:X06614; NID:g36156; PIDN:CAA29829.1; PID:g36157 REFERENCE S07272 !$#authors Chambon, P. !$#submission submitted to the EMBL Data Library, December 1988 !$#accession S07272 !'##molecule_type mRNA !'##residues 31-462 ##label CHA !'##cross-references EMBL:X06538; NID:g35873; PIDN:CAA29787.1; !1PID:g35874 REFERENCE S06224 !$#authors Petkovich, M.; Brand, N.J.; Krust, A.; Chambon, P. !$#journal Nature (1987) 330:444-450 !$#title A human retinoic acid receptor which belongs to the family !1of nuclear receptors. !$#cross-references MUID:88065872; PMID:2825025 !$#accession S06224 !'##molecule_type mRNA !'##residues 31-179,'V',181-462 ##label PET !'##cross-references EMBL:X06538 !'##note this sequence has been revised in reference S07272 !'##note the authors translated the codon AAC for residue 360 as Lys; !1the sequence shown follows the authors' translation REFERENCE S15594 !$#authors Brand, N.J.; Petkovich, M.; Chambon, P. !$#journal Nucleic Acids Res. (1990) 18:6799-6806 !$#title Characterization of a functional promoter for the human !1retinoic acid receptor-alpha (hRAR-alpha). !$#cross-references MUID:91088249; PMID:2175878 !$#accession S15598 !'##molecule_type DNA !'##residues 1-80 ##label BRA1 !'##cross-references EMBL:X56058; NID:g35876; PIDN:CAA39533.1; !1PID:g825712 !$#accession A58975 !'##molecule_type DNA !'##residues 61-80 ##label BRA2 !'##cross-references GB:X58685; NID:g35878; PIDN:CAA41532.1; !1PID:g1335286 GENETICS !$#gene GDB:RARA !'##cross-references GDB:120337; OMIM:180240 !$#map_position 17q12-17q12 !$#introns 60/1 !$#note the first intron occurs before the initiator codon; the list !1of introns is incomplete CLASSIFICATION #superfamily retinoic acid receptor alpha; erbA transforming !1protein homology KEYWORDS DNA binding; nucleus; transcription regulation; zinc finger FEATURE !$86-337 #domain erbA transforming protein homology #label !8ERBA\ !$88-108 #region zinc finger\ !$124-148 #region zinc finger SUMMARY #length 462 #molecular-weight 50771 #checksum 3439 SEQUENCE /// ENTRY A33903 #type complete TITLE retinoic acid receptor gamma, splice form 1 - human ALTERNATE_NAMES retinoic acid receptor gamma-A ORGANISM #formal_name Homo sapiens #common_name man DATE 04-Jun-1999 #sequence_revision 04-Jun-1999 #text_change 22-Jun-1999 ACCESSIONS A33903; A35573; S26848 REFERENCE A33903 !$#authors Krust, A.; Kastner, P.; Petkovich, M.; Zelent, A.; Chambon, !1P. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:5310-5314 !$#title A third human retinoic acid receptor, hRAR-gamma. !$#cross-references MUID:89315787; PMID:2546152 !$#accession A33903 !'##molecule_type mRNA !'##residues 1-454 ##label KRU !'##cross-references GB:M24857; NID:g184385; PIDN:AAA52692.1; !1PID:g306887 REFERENCE A35573 !$#authors Ishikawa, T.; Umesono, K.; Mangelsdorf, D.J.; Aburatani, H.; !1Stanger, B.Z.; Shibasaki, Y.; Imawari, M.; Evans, R.M.; !1Takaku, F. !$#journal Mol. Endocrinol. (1990) 4:837-844 !$#title A functional retinoic acid receptor encoded by the gene on !1human chromosome 12. !$#cross-references MUID:91042616; PMID:2172793 !$#accession A35573 !'##molecule_type mRNA !'##residues 1-454 ##label ISH !'##cross-references GB:M57707; NID:g190867; PIDN:AAA63254.1; !1PID:g190868 REFERENCE S26848 !$#authors Lehmann, J.M.; Hoffmann, B.; Pfahl, M. !$#journal Nucleic Acids Res. (1991) 19:573-578 !$#title Genomic organization of the retinoic acid receptor gamma !1gene. !$#cross-references MUID:91187677; PMID:1849262 !$#accession S26848 !'##molecule_type mRNA !'##residues 1-454 ##label LEH !'##cross-references EMBL:M38258; NID:g190871; PIDN:AAA60254.1; !1PID:g190872 COMMENT For the alternative splice form, see PIR:C35991. GENETICS !$#gene GDB:RARG !'##cross-references GDB:126426; OMIM:180190 !$#map_position 12q13-12q13 CLASSIFICATION #superfamily retinoic acid receptor alpha; erbA transforming !1protein homology KEYWORDS alternative splicing; DNA binding; nucleus; transcription !1regulation; zinc finger FEATURE !$88-339 #domain erbA transforming protein homology #label !8ERBA\ !$90-110 #region zinc finger\ !$126-150 #region zinc finger SUMMARY #length 454 #molecular-weight 50341 #checksum 4152 SEQUENCE /// ENTRY C35991 #type complete TITLE retinoic acid receptor gamma, splice form 2 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 04-Jun-1999 #sequence_revision 04-Jun-1999 #text_change 22-Jun-1999 ACCESSIONS C35991; I38147; S26848 REFERENCE A35991 !$#authors Kastner, P.; Krust, A.; Mendelsohn, C.; Garnier, J.M.; !1Zelent, A.; Leroy, P.; Staub, A.; Chambon, P. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:2700-2704 !$#title Murine isoforms of retinoic acid receptor gamma with !1specific patterns of expression. !$#cross-references MUID:90207264; PMID:2157210 !$#accession C35991 !'##status preliminary !'##molecule_type mRNA !'##residues 1-63 ##label KAS !'##cross-references GB:M32074; NID:g190869; PIDN:AAA60253.1; !1PID:g190870 REFERENCE I38147 !$#authors Lehmann, J.M.; Zhang, X.K.; Pfahl, M. !$#journal Mol. Cell. Biol. (1992) 12:2976-2985 !$#title RAR gamma 2 expression is regulated through a retinoic acid !1response element embedded in Sp1 sites. !$#cross-references MUID:92318914; PMID:1320193 !$#accession I38147 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-50,'VGTGV' ##label LEH1 !'##cross-references EMBL:X57280; NID:g297145; PIDN:CAA40548.1; !1PID:g297146 REFERENCE S26848 !$#authors Lehmann, J.M.; Hoffmann, B.; Pfahl, M. !$#journal Nucleic Acids Res. (1991) 19:573-578 !$#title Genomic organization of the retinoic acid receptor gamma !1gene. !$#cross-references MUID:91187677; PMID:1849262 !$#accession S26848 !'##molecule_type mRNA !'##residues 'MATNKERLFAAGALGPGSGYPGAGFPFAF', !1'PGALRGSPPFEMLSPSFRGLGQPDLPKEMASL',51-443 ##label LEH2 !'##cross-references EMBL:M38258; NID:g190871; PIDN:AAA60254.1; !1PID:g190872 !'##note this sequence for an alternative splice form provides the !1missing coding regions COMMENT For the alternative splice form, see PIR:A33903. GENETICS !$#gene GDB:RARG !'##cross-references GDB:126426; OMIM:180190 !$#map_position 12q13-12q13 CLASSIFICATION #superfamily retinoic acid receptor alpha; erbA transforming !1protein homology KEYWORDS alternative splicing; DNA binding; nucleus; transcription !1regulation; zinc finger FEATURE !$77-328 #domain erbA transforming protein homology #label !8ERBA\ !$79-99 #region zinc finger\ !$115-139 #region zinc finger SUMMARY #length 443 #molecular-weight 49307 #checksum 5034 SEQUENCE /// ENTRY S09592 #type complete TITLE retinoid X receptor alpha [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 04-Jun-1999 #sequence_revision 04-Jun-1999 #text_change 15-Sep-2000 ACCESSIONS S09592; S48153 REFERENCE S09592 !$#authors Mangelsdorf, D.J.; Ong, E.S.; Dyck, J.A.; Evans, R.M. !$#journal Nature (1990) 345:224-229 !$#title Nuclear receptor that identifies a novel retinoic acid !1response pathway. !$#cross-references MUID:90238542; PMID:2159111 !$#accession S09592 !'##molecule_type mRNA !'##residues 1-462 ##label MAN !'##cross-references EMBL:X52773; NID:g35884; PIDN:CAA36982.1; !1PID:g35885 REFERENCE S48153 !$#authors Lee, M.S.; Sem, D.S.; Kliewer, S.A.; Provencal, J.; Evans, !1R.M.; Wright, P.E. !$#journal Eur. J. Biochem. (1994) 224:639-650 !$#title NMR assignments and secondary structure of the retinoid X !1receptor alpha DNA-binding domain. Evidence for the novel !1C-terminal helix. !$#cross-references MUID:95010044; PMID:7925381 !$#contents annotation; NMR study REFERENCE A66009 !$#authors Bourguet, W.; Moras, D. !$#submission submitted to the Brookhaven Protein Data Bank, May 1996 !$#cross-references PDB:1LBD !$#contents annotation; X-ray crystallography, 2.7 angstroms, residues !1225-462 REFERENCE A58541 !$#authors Bourguet, W.; Ruff, M.; Chambon, P.; Gronemeyer, H.; Moras, !1D. !$#journal Nature (1995) 375:377-382 !$#title Crystal structure of the ligand-binding domain of the human !1nuclear receptor RXR-alpha. !$#cross-references MUID:95281048; PMID:7760929 !$#contents annotation; X-ray crystallography, 2.7 angstroms REFERENCE A67262 !$#authors Rastinejad, F.; Perlmann, T.; Evans, R.M.; Sigler, P.B. !$#submission submitted to the Brookhaven Protein Data Bank, November 1996 !$#cross-references PDB:2NLL !$#contents annotation; X-ray crystallography, 1.9 angstroms, residues !1135-200 GENETICS !$#gene GDB:RXRA !'##cross-references GDB:127878; OMIM:180245 !$#map_position 9q34-9q34 CLASSIFICATION #superfamily retinoic acid receptor alpha; erbA transforming !1protein homology KEYWORDS DNA binding; transcription factor; zinc finger FEATURE !$133-378 #domain erbA transforming protein homology #label !8ERBA\ !$135-200 #domain DNA binding #status predicted #label DNA SUMMARY #length 462 #molecular-weight 50811 #checksum 858 SEQUENCE /// ENTRY B49070 #type complete TITLE ecdysone-inducible protein E78B - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B49070 REFERENCE A49070 !$#authors Stone, B.L.; Thummel, C.S. !$#journal Cell (1993) 75:307-320 !$#title The Drosophila 78C early late puff contains E78, an !1ecdysone-inducible gene that encodes a novel member of the !1nuclear hormone receptor superfamily. !$#cross-references MUID:94006562; PMID:8402914 !$#accession B49070 !'##status preliminary !'##molecule_type mRNA !'##residues 1-390 ##label STO !'##cross-references GB:U01088 GENETICS !$#gene FlyBase:Eip78C !'##cross-references FlyBase:FBgn0004865 !$#start_codon CTG CLASSIFICATION #superfamily fruit fly ecdysone-inducible protein E78B; erbA !1transforming protein homology KEYWORDS alternative splicing FEATURE !$1-300 #domain erbA transforming protein homology #status !8atypical #label ERBA SUMMARY #length 390 #molecular-weight 43800 #checksum 2010 SEQUENCE /// ENTRY UGRB #type complete TITLE uteroglobin precursor [validated] - rabbit ALTERNATE_NAMES blastokinin ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 28-Feb-1980 #sequence_revision 15-Oct-1982 #text_change 15-Sep-2000 ACCESSIONS A92391; A93461; A90935; A24217; A90303; A90417; A93824; !1A94608; I46904; I46905; I46907; I46906; A03249 REFERENCE A92391 !$#authors Bailly, A.; Atger, M.; Atger, P.; Cerbon, M.A.; Alizon, M.; !1Vu Hai, M.T.; Logeat, F.; Milgrom, E. !$#journal J. Biol. Chem. (1983) 258:10384-10389 !$#title The rabbit uteroglobin gene. Structure and interaction with !1the progesterone receptor. !$#cross-references MUID:83290960; PMID:6309802 !$#accession A92391 !'##molecule_type DNA !'##residues 1-91 ##label BAI !'##cross-references GB:K00049; NID:g165789 REFERENCE A93461 !$#authors Suske, G.; Wenz, M.; Cato, A.C.B.; Beato, M. !$#journal Nucleic Acids Res. (1983) 11:2257-2271 !$#title The uteroglobin gene region: hormonal regulation, repetitive !1elements and complete nucleotide sequence of the gene. !$#cross-references MUID:83220783; PMID:6304644 !$#accession A93461 !'##molecule_type DNA !'##residues 1-91 ##label SUS !'##cross-references GB:J00687; NID:g1772; PIDN:CAA25669.1; PID:g313668 REFERENCE A90935 !$#authors Chandra, T.; Bullock, D.W.; Woo, S.L.C. !$#journal DNA (1981) 1:19-26 !$#title Hormonally regulated mammalian gene expression: steady-state !1level and nucleotide sequence of rabbit uteroglobin mRNA. !$#cross-references MUID:83157105; PMID:6299663 !$#accession A90935 !'##molecule_type mRNA !'##residues 1-91 ##label CHA !'##cross-references GB:K01657; NID:g165794; PIDN:AAA31497.1; !1PID:g165795 REFERENCE A24217 !$#authors Lopez de Haro, M.S.; Nieto, A. !$#journal FEBS Lett. (1985) 193:247-249 !$#title Primary structure of rabbit lung uteroglobin as deduced from !1the nucleotide sequence of a cDNA. !$#cross-references MUID:86056319; PMID:2415398 !$#accession A24217 !'##molecule_type mRNA !'##residues 22-91 ##label LOP !'##cross-references GB:M27564; NID:g165792; PIDN:AAA31496.1; !1PID:g165793 !'##experimental_source lung REFERENCE A90303 !$#authors Atger, M.; Mercier, J.C.; Haze, G.; Fridlansky, F.; Milgrom, !1E. !$#journal Biochem. J. (1979) 177:985-988 !$#title N-terminal sequences of uteroglobin and its precursor. !$#cross-references MUID:79187160; PMID:571719 !$#accession A90303 !'##molecule_type protein !'##residues 1-5,'F',7-10,'X',15,'G',17-54,'X',56,'B',58-66,'B',68-70, !1'XX',73 ##label ATG REFERENCE A90417 !$#authors Ponstingl, H.; Nieto, A.; Beato, M. !$#journal Biochemistry (1978) 17:3908-3912 !$#title Amino acid sequence of progesterone-induced rabbit !1uteroglobin. !$#cross-references MUID:79042086; PMID:568483 !$#accession A90417 !'##molecule_type protein !'##residues 22-81,'Q',83-91 ##label PON REFERENCE A93824 !$#authors Popp, R.A.; Foresman, K.R.; Wise, L.D.; Daniel Jr., J.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1978) 75:5516-5519 !$#title Amino acid sequence of a progesterone-binding protein. !$#cross-references MUID:79074850; PMID:281700 !$#accession A93824 !'##molecule_type protein !'##residues 22-49,'D',51,'EN',54-59,61-66,'NEPSL',72-91 ##label POP REFERENCE A94608 !$#authors Popp, R.A.; Foresman, K.R.; Wise, L.D.; Daniel Jr., J.C. !$#submission submitted to the Atlas, October 1982 !$#accession A94608 !'##molecule_type protein !'##residues 50-62;67-71 ##label PO2 REFERENCE A50025 !$#authors Morize, I.; Surcouf, E.; Vaney, M.C.; Buehner, M.; Mornon, !1J.P. !$#submission submitted to the Brookhaven Protein Data Bank, April 1989 !$#cross-references PDB:1UTG !$#contents annotation; X-ray crystallography, 1.34 angstroms, residues !122-91 REFERENCE A44652 !$#authors Morize, I.; Surcouf, E.; Vaney, M.C.; Epelboin, Y.; Buehner, !1M.; Fridlansky, F.; Milgrom, E.; Mornon, J.P. !$#journal J. Mol. Biol. (1987) 194:725-739 !$#title Refinement of the C222-1 crystal form of oxidized !1uteroglobin at 1.34 angstroms resolution. !$#cross-references MUID:88011213; PMID:3656405 !$#contents annotation; X-ray crystallography, 1.34 angstroms REFERENCE A50553 !$#authors Bally, R.; Delettre, J. !$#submission submitted to the Brookhaven Protein Data Bank, May 1989 !$#cross-references PDB:2UTG !$#contents annotation; X-ray crystallography, 1.64 angstroms, residues !122-91 REFERENCE A44653 !$#authors Bally, R.; Delettre, J. !$#journal J. Mol. Biol. (1989) 206:153-170 !$#title Structure and refinement of the oxidized P2-1 form of !1uteroglobin at 1.64 angstroms resolution. !$#cross-references MUID:89199637; PMID:2704039 !$#contents annotation; X-ray crystallography, 1.64 angstroms; disulfide !1bonds REFERENCE I46904 !$#authors Menne, C.; Suske, G.; Arnemann, J.; Wenz, M.; Cato, A.C.B.; !1Beato, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:4853-4857 !$#title Isolation and structure of the gene for the !1progesterone-inducible protein uteroglobin. !$#cross-references MUID:83014990; PMID:6956897 !$#accession I46904 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-91 ##label MEN !'##cross-references GB:J00689; NID:g165786; PIDN:AAA31495.1; !1PID:g165788 REFERENCE I46905 !$#authors Chandra, T.; Woo, S.L.C.; Bullock, D.W. !$#journal Biochem. Biophys. Res. Commun. (1980) 95:197-204 !$#title Cloning of the rabbit uteroglobin structural gene. !$#cross-references MUID:81021016; PMID:7417250 !$#accession I46905 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 39-77 ##label CH2 !'##cross-references GB:M25057; NID:g165802; PIDN:AAA31498.1; !1PID:g165803 REFERENCE I46907 !$#authors Suske, G.; Menne, C.; Cato, A.; Wenz, M.; Beato, M. !$#journal Prog. Clin. Biol. Res. (1982) 85:139-146 !$#title Structure and regulated expression of the uteroglobin gene. !$#cross-references MUID:82275176; PMID:6287481 !$#accession I46907 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-45,'V',47-91 ##label SU2 !'##cross-references GB:M32012; NID:g165807; PIDN:AAA31500.1; !1PID:g165809 REFERENCE I46906 !$#authors Atger, M.; Perricaudet, M.; Tiollais, P.; Milgrom, E. !$#journal Biochem. Biophys. Res. Commun. (1980) 93:1082-1088 !$#title Bacterial cloning of the rabbit uteroglobin structural gene. !$#cross-references MUID:80241888; PMID:6156676 !$#accession I46906 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 53-66,'NT',69-72 ##label AT2 !'##cross-references GB:M25038; NID:g165804; PIDN:AAA31499.1; !1PID:g165805 COMMENT Uteroglobin is secreted by the uterus upon induction by !1progesterone. It binds progesterone specifically and with !1high affinity. GENETICS !$#introns 19/1; 81/3 COMPLEX homodimer linked by two disulfide bonds CLASSIFICATION #superfamily uteroglobin KEYWORDS homodimer; steroid binding; uterus FEATURE !$1-21 #domain signal sequence #status experimental #label !8SIG\ !$22-91 #product uteroglobin #status experimental #label MAT\ !$24 #disulfide_bonds interchain (to 90) #status !8experimental\ !$90 #disulfide_bonds interchain (to 24) #status !8experimental SUMMARY #length 91 #molecular-weight 9983 #checksum 556 SEQUENCE /// ENTRY UGRBL #type complete TITLE uteroglobin precursor - brown hare ALTERNATE_NAMES blastokinin ORGANISM #formal_name Lepus capensis #common_name brown hare DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 22-Jun-1999 ACCESSIONS A23825 REFERENCE A23825 !$#authors Lopez de Haro, M.S.; Nieto, A. !$#journal Biochem. J. (1986) 235:895-898 !$#title Nucleotide and derived amino acid sequences of a cDNA coding !1for pre-uteroglobin from the lung of the hare (Lepus !1capensis). !$#cross-references MUID:86323069; PMID:3019311 !$#accession A23825 !'##molecule_type mRNA !'##residues 1-91 ##label LOP !'##cross-references GB:M25609; NID:g164246; PIDN:AAA30960.1; !1PID:g164247 !'##experimental_source lung COMMENT Uteroglobin, synthesized in the uterus and lung, is secreted !1by the uterus upon induction by progesterone. It binds !1progesterone specifically and with high affinity. COMPLEX homodimer linked by two disulfide bonds CLASSIFICATION #superfamily uteroglobin KEYWORDS lung; steroid binding; uterus FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-91 #product uteroglobin #status predicted #label MAT\ !$24 #disulfide_bonds interchain (to 90) #status !8predicted\ !$90 #disulfide_bonds interchain (to 24) #status predicted SUMMARY #length 91 #molecular-weight 9807 #checksum 9933 SEQUENCE /// ENTRY UGMS #type complete TITLE uteroglobin precursor - mouse ALTERNATE_NAMES CC10; Clara cell 10K protein precursor; Clara cell secretory protein ORGANISM #formal_name Mus musculus #common_name house mouse DATE 03-May-1994 #sequence_revision 21-Jan-1997 #text_change 22-Jun-1999 ACCESSIONS A53025; A56656; I51925; S24783 REFERENCE A53025 !$#authors Stripp, B.R.; Huffman, J.A.; Bohinski, R.J. !$#journal Genomics (1994) 20:27-35 !$#title Structure and regulation of the murine Clara cell secretory !1protein gene. !$#cross-references MUID:94292183; PMID:8020953 !$#accession A53025 !'##status preliminary !'##molecule_type DNA !'##residues 1-96 ##label STR !'##cross-references GB:L24372; NID:g461147; PIDN:AAA65446.1; !1PID:g785054 REFERENCE A56656 !$#authors Singh, G.; Katyal, S.L.; Brown, W.E.; Kennedy, A.L. !$#journal Exp. Lung Res. (1993) 19:67-75 !$#title Mouse Clara cell 10-kDa (CC10) protein: cDNA nucleotide !1sequence and molecular basis for the variation in !1progesterone binding of CC10 from different species. !$#cross-references MUID:93178380; PMID:8440203 !$#accession A56656 !'##molecule_type mRNA; protein !'##residues 1-96 ##label SIN !'##cross-references EMBL:X67702; NID:g49690; PIDN:CAA47936.1; !1PID:g49691 !'##experimental_source lung !'##note sequence extracted from NCBI backbone (NCBIP:126148) !'##note parts of this sequence, including the amino end of the mature !1protein, were confirmed by peptide sequencing REFERENCE I51925 !$#authors Margraf, L.R.; Finegold, M.J.; Stanley, L.A.; Major, A.; !1Nawkins, H.K.; DeMayo, F.J. !$#journal Am. J. Respir. Cell Mol. Biol. (1993) 9:231-238 !$#title Cloning and tissue-specific expression of the cDNA for the !1mouse Clara cell 10kD protein: comparison of endogenous !1expression to rabbit uteroglobin promoter-driven transgene !1expression. !$#cross-references MUID:94000840; PMID:8398159 !$#accession I51925 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-96 ##label RES !'##cross-references GB:L04503; NID:g202313; PIDN:AAA03625.1; !1PID:g433093 GENETICS !$#introns 19/1; 81/3 COMPLEX homodimer linked by two disulfide bonds CLASSIFICATION #superfamily uteroglobin KEYWORDS lung; steroid binding; uterus FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-96 #product uteroglobin #status predicted #label MAT\ !$24 #disulfide_bonds interchain (to 90) #status !8predicted\ !$90 #disulfide_bonds interchain (to 24) #status predicted SUMMARY #length 96 #molecular-weight 10519 #checksum 5662 SEQUENCE /// ENTRY BORT3 #type complete TITLE prostatic steroid-binding protein chain C3 precursor - rat ALTERNATE_NAMES prostatein ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 17-Dec-1982 #sequence_revision 14-Nov-1983 #text_change 28-May-1999 ACCESSIONS A92395; A92433; A91108; A42392; A03250 REFERENCE A92395 !$#authors Parker, M.G.; White, R.; Hurst, H.; Needham, M.; Tilly, R. !$#journal J. Biol. Chem. (1983) 258:12-15 !$#title Prostatic steroid-binding protein. Isolation and !1characterization of C3 genes. !$#cross-references MUID:83082848; PMID:6294095 !$#accession A92395 !'##molecule_type mRNA !'##residues 1-95 ##label PAR !'##cross-references GB:V01263; GB:J00777; NID:g56993; PIDN:CAA24577.1; !1PID:g56994 REFERENCE A92433 !$#authors Viskochil, D.H.; Perry, S.T.; Lea, O.A.; Stafford, D.W.; !1Wilson, E.M.; French, F.S. !$#journal J. Biol. Chem. (1983) 258:8861-8866 !$#title Isolation of two genomic sequences encoding the M-r = 14,000 !1subunit of rat prostatein. !$#cross-references MUID:83238526; PMID:6190812 !$#accession A92433 !'##molecule_type mRNA !'##residues 1-78,'S',80-95 ##label VIS REFERENCE A91108 !$#authors Peeters, B.; Rombauts, W.; Mous, J.; Heyns, W. !$#journal Eur. J. Biochem. (1981) 115:115-121 !$#title Structural studies on rat prostatic binding protein. The !1primary structure of its glycosylated component C3. !$#cross-references MUID:81188769; PMID:7014218 !$#accession A91108 !'##molecule_type protein !'##residues 19-95 ##label PEE REFERENCE A42392 !$#authors Tan, J.A.; Marschke, K.B.; Ho, K.C.; Perry, S.T.; Wilson, !1E.M.; French, F.S. !$#journal J. Biol. Chem. (1992) 267:4456-4466 !$#title Response elements of the androgen-regulated C3 gene. !$#cross-references MUID:92165796; PMID:1537831 !$#accession A42392 !'##status preliminary !'##molecule_type DNA !'##residues 1-16,'T',18-95 ##label TAN !'##note sequence inconsistent with the nucleotide translation !'##note sequence extracted from NCBI backbone (NCBIN:83851, !1NCBIP:83856) COMMENT C3 is encoded by two unique genes that differ from each !1other only in their intron regions. Only one protein product !1has been identified in vivo, but both genes may in fact be !1transcribed. COMMENT Steroid-binding protein, the principal androgen-dependent !1secretory protein in rat prostatic fluid, consists of two !1dimeric subunits, one containing C1 and C3 chains and the !1other containing C2 and C3 chains. The chains of each dimer !1are linked by disulfide bonds. This protein is encoded by at !1least four genes whose expression is concomitant and !1stimulated by androgen. CLASSIFICATION #superfamily uteroglobin KEYWORDS glycoprotein FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-95 #product prostatic steroid-binding protein C3 chain !8#status experimental #label MAT\ !$35 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 95 #molecular-weight 10730 #checksum 4495 SEQUENCE /// ENTRY BORT2 #type complete TITLE prostatic steroid-binding protein chain C2 precursor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 15-Oct-1982 #sequence_revision 15-Oct-1982 #text_change 24-Sep-1999 ACCESSIONS A03251; A26671 REFERENCE A93286 !$#authors Parker, M.; Needham, M.; White, R. !$#journal Nature (1982) 298:92-94 !$#title Prostatic steroid binding protein: gene duplication and !1steroid binding. !$#cross-references MUID:82220075; PMID:6896362 !$#accession A03251 !'##molecule_type mRNA !'##residues 1-98 ##label PAR !'##cross-references GB:J00776; NID:g206448; PIDN:AAA51641.1; !1PID:g206450 REFERENCE A26671 !$#authors Delaey, B.; Dirckx, L.; Decourt, J.L.; Claessens, F.; !1Peeters, B.; Rombauts, W. !$#journal Nucleic Acids Res. (1987) 15:1627-1641 !$#title Rat prostatic binding protein: the complete sequence of the !1C2 gene and its flanking regions. !$#cross-references MUID:87146484; PMID:2881277 !$#accession A26671 !'##molecule_type DNA !'##residues 1-25,'Q',26-86,'I',88-94,'VWLQINFPRGRWFSEIN' ##label DEL !'##cross-references GB:X05034; NID:g56857; PIDN:CAA28708.1; PID:g56858 COMMENT Steroid-binding protein, the principal secretory protein in !1rat prostatic fluid, consists of two dimeric subunits, one !1containing C1 and C3 chains and the other containing C2 and !1C3 chains. The chains of each dimer are linked by disulfide !1bonds. CLASSIFICATION #superfamily uteroglobin KEYWORDS heterotetramer; prostate; steroid binding FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-98 #product prostatic steroid-binding protein chain C2 !8#status predicted #label MAT SUMMARY #length 98 #molecular-weight 11055 #checksum 9675 SEQUENCE /// ENTRY BORT1 #type complete TITLE prostatic steroid-binding protein chain C1 precursor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 15-Oct-1982 #sequence_revision 15-Oct-1982 #text_change 22-Jun-1999 ACCESSIONS A93286; A92348; A90348; S42615; A03252 REFERENCE A93286 !$#authors Parker, M.; Needham, M.; White, R. !$#journal Nature (1982) 298:92-94 !$#title Prostatic steroid binding protein: gene duplication and !1steroid binding. !$#cross-references MUID:82220075; PMID:6896362 !$#accession A93286 !'##molecule_type mRNA !'##residues 1-111 ##label PAR REFERENCE A92348 !$#authors Liao, S.; Chen, C.; Huang, I.Y. !$#journal J. Biol. Chem. (1982) 257:122-125 !$#title Prostate alpha-protein. Complete amino acid sequence of the !1component that inhibits nuclear retention of the !1androgen-receptor complex. !$#cross-references MUID:82075873; PMID:7198120 !$#accession A92348 !'##molecule_type protein !'##residues 24-73,'D',75-89,'E',91,'G',93-111 ##label LIA REFERENCE A90348 !$#authors Delaey, B.; Rombauts, W.; Volckaert, G.; Peeters, B.; Mous, !1J.; Heyns, W. !$#journal Biochem. Soc. Trans. (1982) 10:51 !$#title Identification of a complementary-DNA clone containing part !1of the sequence information for the C-1-polypeptide of rat !1prostatic binding protein. !$#accession A90348 !'##molecule_type mRNA !'##residues 13-14,'S',16,'GG',19-65 ##label DEL REFERENCE S42615 !$#authors Delaey, B.; Dirckx, L.; Peeters, B.; Volckaert, G.; Mous, !1J.; Heyns, W.; Rombauts, W. !$#journal Eur. J. Biochem. (1983) 133:645-649 !$#title The nucleotide sequence of cDNA complementary to the C(1) !1component of rat prostatic binding protein. !$#cross-references MUID:83234456; PMID:6688048 !$#accession S42615 !'##molecule_type mRNA !'##residues 1-3,'IK',6-89,'E',91,'G',93-111 ##label DE2 !'##cross-references EMBL:V01545; NID:g57108; PIDN:CAA24787.1; !1PID:g57109 COMMENT Steroid-binding protein, the principal secretory protein in !1rat prostatic fluid, consists of two dimeric subunits, one !1containing C1 and C3 chains and the other containing C2 and !1C3 chains. The chains of each dimer are linked by disulfide !1bonds. CLASSIFICATION #superfamily uteroglobin KEYWORDS heterotetramer; prostate; steroid binding FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-111 #product prostatic steroid-binding protein chain C1 !8#status experimental #label MAT SUMMARY #length 111 #molecular-weight 12807 #checksum 8704 SEQUENCE /// ENTRY BOHUS #type complete TITLE sex steroid-binding globulin precursor [validated] - human ALTERNATE_NAMES SBP; sex steroid-binding protein; testosterone-estradiol binding globulin ORGANISM #formal_name Homo sapiens #common_name man DATE 04-Dec-1986 #sequence_revision 24-Feb-1994 #text_change 08-Dec-2000 ACCESSIONS S09606; A41402; A60876; A26339; S00077; S00065; A03253; !1A60875; A36093 REFERENCE S09606 !$#authors Gershagen, S.; Lundwall, A.; Fernlund, P. !$#journal Nucleic Acids Res. (1989) 17:9245-9258 !$#title Characterization of the human sex hormone binding globulin !1(SHBG) gene and demonstration of two transcripts in both !1liver and testis. !$#cross-references MUID:90067924; PMID:2587256 !$#accession S09606 !'##molecule_type DNA !'##residues 1-402 ##label GER1 !'##cross-references EMBL:X16349; NID:g36442; PIDN:CAA34398.1; !1PID:g296673 REFERENCE A41402 !$#authors Hammond, G.L.; Underhill, D.A.; Rykse, H.M.; Smith, C.L. !$#journal Mol. Endocrinol. (1989) 3:1869-1876 !$#title The human sex hormone-binding globulin gene contains exons !1for androgen-binding protein and two other testicular !1messenger RNAs. !$#cross-references MUID:90114193; PMID:2608061 !$#accession A41402 !'##molecule_type DNA !'##residues 1-333,'L',335,'S',337-402 ##label HAM1 !'##cross-references GB:M31651; NID:g2979502; PIDN:AAC18778.1; !1PID:g338075 !'##note the authors translated the codon CTC for residue 334 as Ala and !1TCC for residue 336 as Leu REFERENCE A60876 !$#authors Bardin, C.W.; Gunsalus, G.L.; Musto, N.A.; Cheng, C.Y.; !1Reventos, J.; Smith, C.; Underhill, D.A.; Hammond, G. !$#journal J. Steroid Biochem. (1988) 30:131-139 !$#title Corticosteroid binding globulin, testosterone-estradiol !1binding globulin, and androgen binding protein belong to !1protein families distinct from steroid receptors. !$#cross-references MUID:88260097; PMID:3386241 !$#accession A60876 !'##molecule_type mRNA !'##residues 'PQ',23-287,'F',289-402 ##label BAR !'##note the steroid-binding domain assigned by sequencing a fragment !1photolabelled with a testosterone derivative REFERENCE A26339 !$#authors Hammond, G.L.; Underhill, D.A.; Smith, C.L.; Goping, I.S.; !1Harley, M.J.; Musto, N.A.; Cheng, C.Y.; Bardin, C.W. !$#journal FEBS Lett. (1987) 215:100-104 !$#title The cDNA-deduced primary structure of human sex !1hormone-binding globulin and location of its steroid-binding !1domain. !$#cross-references MUID:87190990; PMID:3569533 !$#accession A26339 !'##molecule_type mRNA !'##residues 'Q',23-287,'F',289-402 ##label HAM2 !'##cross-references GB:X05403; NID:g36447; PIDN:CAA28987.1; PID:g36448 REFERENCE S00077 !$#authors Gershagen, S.; Fernlund, P.; Lundwall, A. !$#journal FEBS Lett. (1987) 220:129-135 !$#title A cDNA coding for human sex hormone binding globulin. !1Homology to vitamin K-dependent protein S. !$#cross-references MUID:87276542; PMID:2956126 !$#accession S00077 !'##molecule_type mRNA !'##residues 'VHSAAQTTL',56-402 ##label GER2 !'##cross-references EMBL:X05885; NID:g36450; PIDN:CAA29309.1; !1PID:g1335306 !'##note part of this sequence was confirmed by protein sequencing REFERENCE S00065 !$#authors Que, B.G.; Petra, P.H. !$#journal FEBS Lett. (1987) 219:405-409 !$#title Characterization of a cDNA coding for sex steroid-binding !1protein of human plasma. !$#cross-references MUID:87276521; PMID:2956125 !$#accession S00065 !'##molecule_type mRNA !'##residues 121-402 ##label QUE !'##cross-references GB:X05792; NID:g36416; PIDN:CAA29234.1; PID:g825718 REFERENCE A03253 !$#authors Walsh, K.A.; Titani, K.; Takio, K.; Kumar, S.; Hayes, R.; !1Petra, P.H. !$#journal Biochemistry (1986) 25:7584-7590 !$#title Amino acid sequence of the sex steroid binding protein of !1human plasma. !$#cross-references MUID:87101042; PMID:3542030 !$#accession A03253 !'##molecule_type protein !'##residues 30-402 ##label WAL REFERENCE A60875 !$#authors Petra, P.H.; Kumar, S.; Hayes, R.; Ericsson, L.H.; Titani, !1K. !$#journal J. Steroid Biochem. (1986) 24:45-49 !$#title Molecular organization of the sex steroid-binding protein !1(SBP) of human plasma. !$#cross-references MUID:86201744; PMID:3702428 !$#accession A60875 !'##molecule_type protein !'##residues 192-195;216-219;361-364;389-392 ##label PET REFERENCE A36093 !$#authors Khan, M.S.; Hryb, D.J.; Hashim, G.A.; Romas, N.A.; Rosner, !1W. !$#journal J. Biol. Chem. (1990) 265:18362-18365 !$#title Delineation and synthesis of the membrane receptor-binding !1domain of sex hormone-binding globulin. !$#cross-references MUID:91009329; PMID:2170408 !$#accession A36093 !'##molecule_type protein !'##residues 77-86 ##label KHA !'##note membrane receptor-binding region assigned by the binding !1proteolytic fragments of the protein to receptor and !1confirmed by inhibition of binding with synthetic peptides GENETICS !$#gene GDB:SHBG !'##cross-references GDB:125280; OMIM:182205 !$#map_position 17pter-17p12 !$#introns 37/3; 68/2; 131/3; 185/3; 239/1; 284/3; 354/1 COMPLEX homodimer CLASSIFICATION #superfamily sex steroid-binding protein; laminin G repeat !1homology; sex hormone-binding globulin homology KEYWORDS alternative splicing; glycoprotein; homodimer; plasma; !1steroid binding FEATURE !$1-29 #domain signal sequence #status predicted #label SIG\ !$30-402 #product (or 31-402 or 33-402) sex hormone-binding !8globulin #status experimental #label MAT\ !$61-391 #domain sex hormone-binding globulin homology #label !8SHB\ !$71-220 #domain laminin G repeat homology #label LGR\ !$77-86 #region receptor binding #status experimental\ !$325-402 #region steroid binding #status experimental\ !$36 #binding_site carbohydrate (Thr) (covalent) #status !8experimental\ !$193-217,362-390 #disulfide_bonds #status experimental\ !$193-217,362-390 #disulfide_bonds #status predicted\ !$273 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$380,396 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 402 #molecular-weight 43779 #checksum 3065 SEQUENCE /// ENTRY WTHUB #type complete TITLE semenogelin I precursor [validated] - human CONTAINS seminal basic protein ORGANISM #formal_name Homo sapiens #common_name man DATE 04-Dec-1986 #sequence_revision 03-Oct-1995 #text_change 08-Dec-2000 ACCESSIONS B43412; A31489; A91335; S29155; A43500; A91320; S29380; !1S68761; A03254 REFERENCE A43412 !$#authors Ulvsback, M.; Lazure, C.; Lilja, H.; Spurr, N.K.; Rao, V.V.; !1Loffler, C.; Hansmann, I.; Lundwall, A. !$#journal J. Biol. Chem. (1992) 267:18080-18084 !$#title Gene structure of semenogelin I and II. The predominant !1proteins in human semen are encoded by two homologous genes !1on chromosome 20. !$#cross-references MUID:92388176; PMID:1517240 !$#accession B43412 !'##molecule_type DNA !'##residues 1-462 ##label ULV !'##cross-references GB:M81650; NID:g307416; PIDN:AAA18168.1; !1PID:g487420 REFERENCE A31489 !$#authors Lilja, H.; Abrahamsson, P.A.; Lundwall, A. !$#journal J. Biol. Chem. (1989) 264:1894-1900 !$#title Semenogelin, the predominant protein in human semen. Primary !1structure and identification of closely related proteins in !1the male accessory sex glands and on the spermatozoa. !$#cross-references MUID:89109215; PMID:2912989 !$#accession A31489 !'##molecule_type mRNA !'##residues 1-78,'T',80-422,'K',424-462 ##label LIL !'##cross-references GB:J04440 !'##note Ser-79 was also found REFERENCE A91335 !$#authors Lilja, H.; Jeppsson, J.O. !$#journal FEBS Lett. (1985) 182:181-184 !$#title Amino acid sequence of the predominant basic protein in !1human seminal plasma. !$#cross-references MUID:85127550; PMID:3972122 !$#accession A91335 !'##molecule_type protein !'##residues 108-159 ##label LI2 !'##note this sequence represents a naturally occurring fragment from !1proteolytic cleavage of semenogelin during liquefaction of !1semen REFERENCE S29155 !$#authors Schneider, K.; Kausler, W.; Tripier, D.; Jouvenal, K.; !1Spiteller, G. !$#journal Biol. Chem. Hoppe-Seyler (1989) 370:353-356 !$#title Isolation and structure determination of two peptides !1occurring in human seminal plasma. !$#cross-references MUID:89335265; PMID:2757795 !$#accession S29155 !'##molecule_type protein !'##residues 316-320,'L',322-344 ##label SCH !'##note this sequence represents the amino end of a naturally occurring !1fragment from proteolytic cleavage of semenogelin during !1liquefaction of semen REFERENCE A43500 !$#authors Ramasharma, K.; Sairam, M.R.; Seidah, N.G.; Chretien, M.; !1Manjunath, P.; Schiller, P.W.; Yamashiro, D.; Li, C.H. !$#journal Science (1984) 223:1199-1202 !$#title Isolation, structure, and synthesis of a human seminal !1plasma peptide with inhibin-like activity. !$#cross-references MUID:84146751; PMID:6422553 !$#accession A43500 !'##molecule_type protein !'##residues 108-138 ##label RAM !'##note this sequence represents a naturally occurring fragment from !1proteolytic cleavage of semenogelin during liquefaction of !1semen REFERENCE A91320 !$#authors Seidah, N.G.; Ramasharma, K.; Sairam, M.R.; Chretien, M. !$#journal FEBS Lett. (1984) 167:98-102 !$#title Partial amino acid sequence of a human seminal plasma !1peptide with inhibin-like activity. !$#cross-references MUID:84132557; PMID:6698208 !$#accession A91320 !'##molecule_type protein !'##residues 108-138 ##label SEI !'##note this sequence represents a naturally occurring fragment from !1proteolytic cleavage of semenogelin during liquefaction of !1semen REFERENCE S29380 !$#authors Khan, Z.; Smyth, D.G. !$#journal Eur. J. Biochem. (1993) 212:35-40 !$#title Isolation and identification of N-terminally extended forms !1of 5-oxoprolylglutamylprolinamide (Glp-Glu-Pro-NH(2)), a !1thyrotropin-releasing-hormone(TRH)-like peptide present in !1human semen. !$#cross-references MUID:93185635; PMID:8444163 !$#accession S29380 !'##molecule_type protein !'##residues 373-397 ##label KHA !'##note the authors' suggestion that this peptide is amidated is !1consistent with radioimmunoassay results but has not been !1proven !'##note the amidated tripeptide Glp-Glu-Pro-NH2 (where Glp is !1pyroglutamic acid) is present in human semen; although the !1sequence reported here is consistent with an !1amino-terminally extended form derived from semenogelin, the !1sequence is followed in semenogelin by Trp, which (unlike !1Gly) probably cannot become the source of an amide moiety; !1the authors conclude the peptide must be derived from a !1closely related protein REFERENCE S68761 !$#authors Malm, J.; Hellman, J.; Magnusson, H.; Laurell, C.B.; Lilja, !1H. !$#journal Eur. J. Biochem. (1996) 238:48-53 !$#title Isolation and characterization of the major gel proteins in !1human semen, semenogelin I and semenogelin II. !$#cross-references MUID:96248420; PMID:8665951 !$#accession S68761 !'##molecule_type protein !'##residues 49-50,'G',52-53 ##label MAL COMMENT This abundant protein from seminal vesicle secretions !1maintains a gel-like environment for the sperm cells. At !1ejaculation, kallikrein-like enzymes in prostatic secretions !1cleave this protein, resulting in liquefaction of the !1seminal gel and allowing increased sperm motility. GENETICS !$#gene GDB:SEMG1 !'##cross-references GDB:128167; OMIM:182140 !$#map_position 20q12-20q13.1 !$#introns 26/1 CLASSIFICATION #superfamily semenogelin KEYWORDS duplication; glycoprotein; semen; seminal vesicle FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$108-138 #product seminal basic protein #status experimental !8#label MAT\ !$174-215 #region semenogelin short repeat 1\ !$234-275 #region semenogelin short repeat 2\ !$282-339 #region semenogelin long repeat 1\ !$342-399 #region semenogelin long repeat 2\ !$414-455 #region semenogelin short repeat 3\ !$141 #binding_site carbohydrate (Asn) (covalent) #status !8absent\ !$239 #disulfide_bonds interchain #status experimental SUMMARY #length 462 #molecular-weight 52117 #checksum 9901 SEQUENCE /// ENTRY SQRTSV #type complete TITLE seminal vesicle secretory protein IV precursor - rat ALTERNATE_NAMES seminal vesicle secretory protein S; SVS IV protein ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Jul-1980 #sequence_revision 27-Nov-1985 #text_change 22-Jun-1999 ACCESSIONS A93975; S07181; A91761; A61349; I58208; A03255 REFERENCE A93975 !$#authors Harris, S.E.; Mansson, P.E.; Tully, D.B.; Burkhart, B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:6460-6464 !$#title Seminal vesicle secretion IV gene: allelic difference due to !1a series of 20-base-pair direct tandem repeats within an !1intron. !$#cross-references MUID:84042491; PMID:6579532 !$#accession A93975 !'##molecule_type DNA !'##residues 1-112 ##label HAR !'##cross-references GB:X01114; NID:g57317; PIDN:CAA25584.1; PID:g57318 REFERENCE S07181 !$#authors McDonald, C.J.; Eliopoulos, E.; Higgins, S.J. !$#journal EMBO J. (1984) 3:2517-2521 !$#title Divergent protein coding regions in otherwise closely !1related androgen-regulated mRNAs. !$#cross-references MUID:85076571; PMID:6548962 !$#accession S07181 !'##molecule_type mRNA !'##residues 1-112 ##label MCD !'##cross-references EMBL:X01114; NID:g57317; PIDN:CAA25584.1; !1PID:g57318 REFERENCE A91761 !$#authors Pan, Y.C.E.; Li, S.S.L. !$#journal Int. J. Pept. Protein Res. (1982) 20:177-187 !$#title Structure of secretory protein IV from rat seminal vesicles. !$#cross-references MUID:83029971; PMID:6752062 !$#accession A91761 !'##molecule_type protein !'##residues 22-112 ##label PAN REFERENCE A61349 !$#authors Pan, Y.C.E.; Silverberg, A.B.; Harris, S.E.; Li, S.S.L. !$#journal Int. J. Pept. Protein Res. (1980) 16:143-146 !$#title Complete amino acid sequence of a major secretory protein !1from rat seminal vesicle. !$#cross-references MUID:81116479; PMID:7007263 !$#accession A61349 !'##molecule_type protein !'##residues 22-49,51-112 ##label PA2 REFERENCE I58208 !$#authors Kandala, J.C.; Kistler, M.K.; Lawther, R.P.; Kistler, W.S. !$#journal Nucleic Acids Res. (1983) 11:3169-3186 !$#title Characterization of a genomic clone for rat seminal vesicle !1secretory protein IV. !$#cross-references MUID:83220735; PMID:6304626 !$#accession I58208 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-25 ##label RES !'##cross-references EMBL:X01575; NID:g57314; PIDN:CAA25730.1; !1PID:g736293 COMMENT This is one of several small basic polypeptides secreted by !1the seminal vesicle under the influence of testosterone. !1Although its function is unknown, it is a marker for the !1hormonal regulation of protein synthesis. GENETICS !$#introns 26/1 CLASSIFICATION #superfamily seminal vesicle secretory protein KEYWORDS extracellular protein; seminal vesicle FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-112 #product seminal vesicle secretory protein IV #status !8experimental #label MAT SUMMARY #length 112 #molecular-weight 12046 #checksum 5162 SEQUENCE /// ENTRY WTBO #type complete TITLE seminal fluid protein PDC-109 precursor - bovine ALTERNATE_NAMES seminal vesicle secretory protein 109 (SVSP109) ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 14-Nov-1983 #sequence_revision 05-May-1995 #text_change 22-Jun-1999 ACCESSIONS S18404; S45010; A31852; A61564; A03256; S59518; S48674 REFERENCE S18404 !$#authors Braeuer, C.; Scheit, K.H. !$#journal Biochim. Biophys. Acta (1991) 1090:259-260 !$#title Characterization of the gene for the bovine seminal vesicle !1secretory protein SVSP109. !$#cross-references MUID:92031704; PMID:1932121 !$#accession S18404 !'##molecule_type DNA !'##residues 1-134 ##label BRA !'##cross-references GB:X60495; NID:g29; PIDN:CAA43021.1; PID:g833775 REFERENCE S45010 !$#authors Braeuer, C.C.; Kleine Kuhlmann, J.J.; Hanes, J.J.; Scheit, !1K.K. !$#submission submitted to the EMBL Data Library, May 1994 !$#description Structure and promoter analysis of the genes for bovine !1SVSP109 and seminalplasmin. !$#accession S45010 !'##molecule_type DNA !'##residues 1-134 ##label BR2 !'##cross-references EMBL:Z33621; NID:g488602; PIDN:CAA83915.1; !1PID:g488603 REFERENCE A31852 !$#authors Kemme, M.; Scheit, K.H. !$#journal DNA (1988) 7:595-599 !$#title Cloning and sequence analysis of a cDNA from seminal vesicle !1tissue encoding the precursor of the major protein of bull !1semen. !$#cross-references MUID:89152746; PMID:3229283 !$#accession A31852 !'##molecule_type mRNA !'##residues 1-134 ##label KEM !'##cross-references GB:M22244; NID:g163734; PIDN:AAA30766.1; !1PID:g163735 REFERENCE A61564 !$#authors Scheit, K.H.; Kemme, M.; Aumueller, G.; Seitz, J.; !1Hagendorff, G.; Zimmer, M. !$#journal Biosci. Rep. (1988) 8:589-608 !$#title The major protein of bull seminal plasma: biosynthesis and !1biological function. !$#cross-references MUID:89207711; PMID:2468369 !$#accession A61564 !'##molecule_type mRNA !'##residues 7-134 ##label SCH REFERENCE A03256 !$#authors Esch, F.S.; Ling, N.C.; Bohlen, P.; Ying, S.Y.; Guillemin, !1R. !$#journal Biochem. Biophys. Res. Commun. (1983) 113:861-867 !$#title Primary structure of PDC-109, a major protein constituent of !1bovine seminal plasma. !$#cross-references MUID:83256590; PMID:6870895 !$#accession A03256 !'##molecule_type protein !'##residues 26-134 ##label ESC !'##note residues 49-86 and 94-134 form two structurally similar !1domains, A and B, each containing two disulfide bonds !'##note the function of this protein is not known REFERENCE S59518 !$#authors Braeuer, C.; Hanes, J.; Scheit, K.H. !$#journal Biol. Chem. Hoppe-Seyler (1995) 376:631-636 !$#title The gene for the major protein (SVSP109) of bovine semen: !1structure and promoter analysis. !$#cross-references MUID:96145730; PMID:8590633 !$#accession S59518 !'##molecule_type DNA !'##residues 1-134 ##label BR3 !'##cross-references EMBL:Z33621; NID:g488602; PIDN:CAA83915.1; !1PID:g488603 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1May 1994 !'##note only a part of the nucleic acid sequence is shown; only a part !1of the translation is shown REFERENCE S48674 !$#authors Calvete, J.J.; Raida, M.; Sanz, L.; Wempe, F.; Scheit, K.H.; !1Romero, A.; Toepfer-Petersen, E. !$#journal FEBS Lett. (1994) 350:203-206 !$#title Localization and structural characterization of an !1oligosaccharide O-linked to bovine PDC-109. Quantitation of !1the glycoprotein in seminal plasma and on the surface of !1ejaculated and capacitated spermatozoa. !$#cross-references MUID:94350099; PMID:8070564 !$#accession S48674 !'##molecule_type protein !'##residues 26-35,'X',37-56;60-89 ##label CAL GENETICS !$#introns 26/1; 46/1; 90/1 CLASSIFICATION #superfamily seminal fluid protein PDC-109; fibronectin type !1II repeat homology KEYWORDS duplication; glycoprotein; plasma; semen FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-134 #product seminal fluid protein SVSP109 #status !8experimental #label MAT\ !$49-86 #domain fibronectin type II repeat homology #label !82F0\ !$94-134 #domain fibronectin type II repeat homology #label !82F1\ !$36 #binding_site carbohydrate (Thr) (covalent) (partial) !8#status experimental\ !$49-73,63-86,94-119, !$108-134 #disulfide_bonds #status experimental SUMMARY #length 134 #molecular-weight 15480 #checksum 7856 SEQUENCE /// ENTRY WTFF #type complete TITLE testis-specific protein (clone mst(3)gl-9) - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 22-Jun-1999 ACCESSIONS S00340 REFERENCE S00340 !$#authors Kuhn, R.; Schaefer, U.; Schaefer, M. !$#journal EMBO J. (1988) 7:447-454 !$#title Cis-acting regions sufficient for spermatocyte-specific !1transcriptional and spermatid-specific translational control !1of the Drosophila melanogaster gene mst(3)gl-9. !$#cross-references MUID:88211557; PMID:2835228 !$#accession S00340 !'##molecule_type DNA !'##residues 1-56 ##label KUH !'##cross-references EMBL:Y00831; NID:g8650; PIDN:CAA68761.1; PID:g8651 GENETICS !$#gene FlyBase:Mst87F !'##cross-references FlyBase:FBgn0002862 CLASSIFICATION #superfamily fruit fly testis-specific protein KEYWORDS sex-specific protein; testis SUMMARY #length 56 #molecular-weight 5233 #checksum 7305 SEQUENCE /// ENTRY EYNKHR #type complete TITLE egg-lysin precursor [validated] - California red abalone ORGANISM #formal_name Haliotis rufescens #common_name California red abalone DATE 30-Jun-1987 #sequence_revision 19-Oct-1995 #text_change 15-Sep-2000 ACCESSIONS A35960; A03257 REFERENCE A35960 !$#authors Vacquier, V.D.; Carner, K.R.; Stout, C.D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:5792-5796 !$#title Species-specific sequences of abalone lysin, the sperm !1protein that creates a hole in the egg envelope. !$#cross-references MUID:90332668; PMID:2377618 !$#accession A35960 !'##molecule_type mRNA !'##residues 1-154 ##label VAC !'##cross-references GB:M34388; NID:g159228; PIDN:AAA29196.1; !1PID:g159229 REFERENCE A03257 !$#authors Fridberger, A.; Sundelin, J.; Vacquier, V.D.; Peterson, P.A. !$#journal J. Biol. Chem. (1985) 260:9092-9099 !$#title Amino acid sequence of an egg-lysin protein from abalone !1spermatozoa that solubilizes the vitelline layer. !$#cross-references MUID:85261286; PMID:3894351 !$#accession A03257 !'##molecule_type protein !'##residues 19-38,'K',40,'F',42-84,'I',86-90,'L',92-108,'D',110-136, !1'Q',138-152 ##label FRI !'##experimental_source spermatozoa !'##note carboxy-terminal analysis gave an extremely low yield !1suggesting it is blocked REFERENCE A51283 !$#authors Shaw, A.; McRee, D.E.; Vacquier, V.D.; Stout, C.D. !$#submission submitted to the Brookhaven Protein Data Bank, June 1993 !$#cross-references PDB:1LIS !$#contents annotation; X-ray crystallography, 1.9 angstroms, residues !122-152 !$#note monomer REFERENCE A49386 !$#authors Shaw, A.; McRee, D.E.; Vacquier, V.D.; Stout, C.D. !$#journal Science (1993) 262:1864-1867 !$#title The crystal structure of lysin, a fertilization protein. !$#cross-references MUID:94090312; PMID:8266073 !$#contents annotation; X-ray crystallography, 1.9 angstroms REFERENCE A66089 !$#authors Shaw, A.; Vacquier, V.D.; Stout, C.D. !$#submission submitted to the Brookhaven Protein Data Bank, March 1995 !$#cross-references PDB:1LYN !$#contents annotation; X-ray crystallography, 2.75 angstroms, residues !128-152 !$#note dimer REFERENCE A57052 !$#authors Shaw, A.; Fortes, P.A.G.; Stout, C.D.; Vacquier, V.D. !$#journal J. Cell Biol. (1995) 130:1117-1125 !$#title Crystal structure and subunit dynamics of the abalone sperm !1lysin dimer: egg envelopes dissociate dimers, the monomer is !1the active species. !$#cross-references MUID:95386571; PMID:7657696 !$#contents annotation; X-ray crystallography, 2.75 angstroms COMPLEX homodimer; dissociates to monomer in egg envelope lipid FUNCTION !$#description dissolves the egg vitelline layer nonenzymatically during !1fertilization CLASSIFICATION #superfamily egg-lysin KEYWORDS amidated carboxyl end; fertilization; sperm FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-152 #product egg-lysin #status experimental #label MAT\ !$152 #modified_site amidated carboxyl end (Met) (amide in !8mature form from following glycine) #status predicted SUMMARY #length 154 #molecular-weight 18237 #checksum 6435 SEQUENCE /// ENTRY IZWS #type complete TITLE cygnin - black swan ORGANISM #formal_name Cygnus atratus #common_name black swan DATE 18-Apr-1984 #sequence_revision 28-Feb-1986 #text_change 24-Nov-1999 ACCESSIONS A03258 REFERENCE A94600 !$#authors Simpson, R.J.; Morgan, F.J. !$#submission submitted to the Atlas, November 1982 !$#accession A03258 !'##molecule_type protein !'##residues 1-39 ##label SIM COMMENT Cygnin shows some similarity to the amino-terminal fragment !1of the carboxyl-terminal domain of the chicken !1ovotransferrin. CLASSIFICATION #superfamily cygnin KEYWORDS blocked amino end; egg white FEATURE !$1 #modified_site blocked amino end (Gln) (probably !8pyrrolidone carboxylic acid) #status experimental SUMMARY #length 39 #molecular-weight 4452 #checksum 9776 SEQUENCE /// ENTRY JXHU #type complete TITLE transferrin receptor - human ALTERNATE_NAMES CD71; p90 CONTAINS 85K serum transferrin receptor ORGANISM #formal_name Homo sapiens #common_name man DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 22-Jun-1999 ACCESSIONS A93343; A90856; A36597; S54327; S09039; A03259 REFERENCE A93343 !$#authors Schneider, C.; Owen, M.J.; Banville, D.; Williams, J.G. !$#journal Nature (1984) 311:675-678 !$#title Primary structure of human transferrin receptor deduced from !1the mRNA sequence. !$#cross-references MUID:85012743; PMID:6090955 !$#accession A93343 !'##molecule_type mRNA !'##residues 1-760 ##label SCH !'##cross-references GB:X01060; NID:g37432; PIDN:CAA25527.1; PID:g37433 REFERENCE A90856 !$#authors McClelland, A.; Kuhn, L.C.; Ruddle, F.H. !$#journal Cell (1984) 39:267-274 !$#title The human transferrin receptor gene: genomic organization, !1and the complete primary structure of the receptor deduced !1from a cDNA sequence. !$#cross-references MUID:85048936; PMID:6094009 !$#accession A90856 !'##molecule_type mRNA !'##residues 1-760 ##label MCC !'##cross-references GB:M11507; NID:g339515; PIDN:AAA61153.1; !1PID:g339516 REFERENCE A36597 !$#authors Shih, Y.J.; Baynes, R.D.; Hudson, B.G.; Flowers, C.H.; !1Skikne, B.S.; Cook, J.D. !$#journal J. Biol. Chem. (1990) 265:19077-19081 !$#title Serum transferrin receptor is a truncated form of tissue !1receptor. !$#cross-references MUID:91035436; PMID:2229063 !$#accession A36597 !'##molecule_type protein !'##residues 101-103,'X',105-108,'X',110-119 ##label SHI !'##experimental_source serum REFERENCE S54327 !$#authors Coppolino, M.; Migliorini, M.; Argraves, W.S.; Dedhar, S. !$#journal Biochem. J. (1995) 306:129-134 !$#title Identification of a novel form of the alpha(3) integrin !1subunit: covalent association with transferrin receptor. !$#cross-references MUID:95169043; PMID:7864799 !$#accession S54327 !'##molecule_type protein !'##residues 288-302;694-708;721-730 ##label COP REFERENCE S09039 !$#authors Alvarez, E.; Girones, N.; Davis, R.J. !$#journal Biochem. J. (1990) 267:31-35 !$#title A point mutation in the cytoplasmic domain of the !1transferrin receptor inhibits endocytosis. !$#cross-references MUID:90226333; PMID:2327986 !$#accession S09039 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-19,'C',21-61 ##label ALV !'##note mutant defective in endocytosis COMMENT This transmembrane glycoprotein exists as a dimer of similar !1or identical chains linked by a disulfide bond involving !1Cys-67, Cys-89, or Cys-98. Each chain binds glycans, !1phosphate, and fatty acyl groups. The amino end of each !1chain lies within the cytoplasm and a stop-transfer sequence !1(K-P-K-R) precedes the transmembrane segment, which, in !1addition to anchoring the molecule to the membrane, may also !1serve as an internal signal sequence. COMMENT The expression of this receptor, involved in the regulation !1of cell growth, on cell surfaces directly correlates with !1cellular proliferation. GENETICS !$#gene GDB:TFRC !'##cross-references GDB:120433; OMIM:190010 !$#map_position 3q26.2-3q26.2 FUNCTION !$#description mediates cell iron uptake by binding, internalizing, and !1recycling the iron-binding plasma protein transferrin CLASSIFICATION #superfamily transferrin receptor KEYWORDS glycoprotein; iron transport; receptor; transmembrane !1protein FEATURE !$1-57 #domain intracellular #status predicted #label INT\ !$20-24 #region tyrosine-based endosomal/lysosomal sorting !8signal\ !$58-61 #region stop-transfer sequence\ !$62-89 #domain transmembrane #status predicted #label TMS\ !$89-760 #domain extracellular #status predicted #label EXT\ !$101-760 #product 85K serum transferrin receptor #status !8predicted #label MAT\ !$251,317,727 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 760 #molecular-weight 84901 #checksum 7264 SEQUENCE /// ENTRY S29548 #type complete TITLE transferrin receptor - mouse ALTERNATE_NAMES CD71; p90 CONTAINS 85K serum transferrin receptor ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S29548; A26735; D24550; I49662 REFERENCE S29548 !$#authors Trowbridge, I.S.; Domingo, D.L.; Thomas, M.L.; Chain, A. !$#submission submitted to the EMBL Data Library, January 1991 !$#accession S29548 !'##status preliminary !'##molecule_type mRNA !'##residues 1-763 ##label TRO !'##cross-references EMBL:X57349; NID:g54914; PIDN:CAA40624.1; !1PID:g54915 REFERENCE A26735 !$#authors Rothenberger, S.; Iacopetta, B.J.; Kuhn, L.C. !$#journal Cell (1987) 49:423-431 !$#title Endocytosis of the transferrin receptor requires the !1cytoplasmic domain but not its phosphorylation site. !$#cross-references MUID:87187639; PMID:3568132 !$#accession A26735 !'##molecule_type protein !'##residues 1-82 ##label ROT REFERENCE A24550 !$#authors Grego, B.; Van Driel, I.R.; Stearne, P.A.; Goding, J.W.; !1Nice, E.C.; Simpson, R.J. !$#journal Eur. J. Biochem. (1985) 148:485-491 !$#cross-references MUID:85203852; PMID:2986964 !$#accession D24550 !'##molecule_type protein !'##residues 7-19;158-175,'X',177-179;'DESL','AY',189,'IEN',193,'FXEF', !1195;196,197-208;450-468;736-742,'X',744-756,'I',758 ##label !1GRE !'##note these tryptic fragments have been ordered by homology with the !1human sequence REFERENCE I49662 !$#authors Stearne, P.A.; Pietersz, G.A.; Goding, J.W. !$#journal J. Immunol. (1985) 134:3474-3479 !$#title cDNA cloning of the murine transferrin receptor: Sequence of !1trans-membrane and adjacent regions. !$#cross-references MUID:85159078; PMID:2984291 !$#accession I49662 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 'AL',27-149,'Q',151-301 ##label RES !'##cross-references GB:M29618; NID:g193272; PIDN:AAA37616.1; !1PID:g193273 COMMENT This transmembrane glycoprotein exists as a dimer of similar !1or identical chains linked by a disulfide bond involving !1Cys-67, Cys-89, or Cys-98. Each chain binds glycans, !1phosphate, and fatty acyl groups. The amino end of each !1chain lies within the cytoplasm and a stop-transfer sequence !1(K-P-K-R) precedes the transmembrane segment, which, in !1addition to anchoring the molecule to the membrane, may also !1serve as an internal signal sequence. COMMENT The expression of this receptor, involved in the regulation !1of cell growth, on cell surfaces directly correlates with !1cellular proliferation. FUNCTION !$#description mediates cell iron uptake by binding, internalizing, and !1recycling the iron-binding plasma protein transferrin CLASSIFICATION #superfamily transferrin receptor KEYWORDS glycoprotein; iron transport; receptor; transmembrane !1protein FEATURE !$1-57 #domain intracellular #status predicted #label INT\ !$58-61 #region stop-transfer sequence\ !$62-89 #domain transmembrane #status predicted #label TMS\ !$89-763 #domain extracellular #status predicted #label EXT\ !$101-763 #product 85K serum transferrin receptor #status !8predicted #label MAT\ !$253,319,730 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 763 #molecular-weight 85731 #checksum 9532 SEQUENCE /// ENTRY JH0570 #type complete TITLE transferrin receptor - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JH0570; S16855 REFERENCE JH0570 !$#authors Gerhardt, E.M.; Chan, L.N.L.; Jing, S.; Qi, M.; Trowbridge, !1I.S. !$#journal Gene (1991) 102:249-254 !$#title The cDNA sequence and primary structure of the chicken !1transferrin receptor. !$#cross-references MUID:91340160; PMID:1874449 !$#accession JH0570 !'##molecule_type mRNA !'##residues 1-776 ##label GER !'##cross-references EMBL:X55348 !'##note 581-His and 736-Gln were also found as the result of !1polymorphism COMMENT This protein mediates the endocytosis of the iron !1transferrin complex. CLASSIFICATION #superfamily transferrin receptor KEYWORDS glycoprotein; lipoprotein; phosphoprotein; receptor; !1thiolester bond; transmembrane protein FEATURE !$19-22 #region coated-pit mediated internalization signal\ !$70-88 #domain transmembrane #status predicted #label TRM\ !$23 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$70 #binding_site palmitate (Cys) (covalent) #status !8predicted\ !$261,326,391,738 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 776 #molecular-weight 85731 #checksum 1113 SEQUENCE /// ENTRY TFHUP #type complete TITLE transferrin precursor [validated] - human ALTERNATE_NAMES siderophilin ORGANISM #formal_name Homo sapiens #common_name man DATE 15-Oct-1982 #sequence_revision 30-Sep-1993 #text_change 08-Dec-2000 ACCESSIONS A20981; A92417; A94044; A29090; A32739; I51959; I63133; !1I54011; I68160; A03260 REFERENCE A20981 !$#authors Yang, F.; Lum, J.B.; McGill, J.R.; Moore, C.M.; Naylor, !1S.L.; van Bragt, P.H.; Baldwin, W.D.; Bowman, B.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:2752-2756 !$#title Human transferrin: cDNA characterization and chromosomal !1localization. !$#cross-references MUID:84194084; PMID:6585826 !$#contents variant C !$#accession A20981 !'##molecule_type mRNA !'##residues 1-698 ##label YAN !'##cross-references EMBL:M12530; NID:g339452; PIDN:AAA61140.1; !1PID:g339453 !'##note the authors translated the codon CAA for residue 203 as Glu REFERENCE A92417 !$#authors MacGillivray, R.T.A.; Mendez, E.; Shewale, J.G.; Sinha, !1S.K.; Lineback-Zins, J.; Brew, K. !$#journal J. Biol. Chem. (1983) 258:3543-3553 !$#title The primary structure of human serum transferrin. The !1structures of seven cyanogen bromide fragments and the !1assembly of the complete structure. !$#cross-references MUID:83160878; PMID:6833213 !$#accession A92417 !'##molecule_type protein !'##residues 20-263,'E',265-328,'N',330-379,'SD',382-435,'D',437-557, !1'T',559-560,'P',562-590,'Q',592-671,'Q',673-698 ##label MAC !'##note the sequence shown is the predominant electrophoretic genetic !1variant (C or TfC) of transferrin; the D1 and Dchi variants !1differ from this sequence in having 277-Gly and 300-Arg, !1respectively REFERENCE A94044 !$#authors Park, I.; Schaeffer, E.; Sidoli, A.; Baralle, F.E.; Cohen, !1G.N.; Zakin, M.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:3149-3153 !$#title Organization of the human transferrin gene: direct evidence !1that it originated by gene duplication. !$#cross-references MUID:85216459; PMID:3858812 !$#accession A94044 !'##molecule_type DNA !'##residues 73-263,'E',265-328,'N',330-562 ##label PAR !'##cross-references EMBL:M11361 REFERENCE A29090 !$#authors Adrian, G.S.; Korinek, B.W.; Bowman, B.H.; Yang, F. !$#journal Gene (1986) 49:167-175 !$#title The human transferrin gene: 5' region contains conserved !1sequences which match the control elements regulated by !1heavy metals, glucocorticoids and acute phase reaction. !$#cross-references MUID:87192006; PMID:3106157 !$#accession A29090 !'##molecule_type DNA !'##residues 1-72;291-300 ##label ADR !'##cross-references EMBL:M15673 REFERENCE A32739 !$#authors Uzan, G.; Frain, M.; Park, I.; Besmond, C.; Maessen, G.; !1Trepat, J.S.; Zakin, M.M.; Kahn, A. !$#journal Biochem. Biophys. Res. Commun. (1984) 119:273-281 !$#title Molecular cloning and sequence analysis of cDNA for human !1transferrin. !$#cross-references MUID:84153910; PMID:6322780 !$#accession A32739 !'##molecule_type mRNA !'##residues 422-690,'G',692-698 ##label UZA !'##cross-references EMBL:M12525; NID:g339468; PIDN:AAA61142.1; !1PID:g339469 REFERENCE A93911 !$#authors MacGillivray, R.T.A.; Mendez, E.; Sinha, S.K.; Sutton, M.R.; !1Lineback-Zins, J.; Brew, K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:2504-2508 !$#title The complete amino acid sequence of human serum transferrin. !$#cross-references MUID:82222166; PMID:6953407 !$#contents annotation; disulfide bonds REFERENCE I51959 !$#authors Hershberger, C.L.; Larson, J.L.; Arnold, B.; Rosteck, P.R. !$#journal Ann. N. Y. Acad. Sci. (1991) 646:140-154 !$#title A cloned gene for human transferrin. !$#cross-references MUID:92231399; PMID:1809186 !$#accession I51959 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-698 ##label RES !'##cross-references GB:S95936; NID:g248647; PIDN:AAB22049.1; !1PID:g248648 REFERENCE I48174 !$#authors Duguid, J.R.; Bohmont, C.W.; Liu, N.G.; Tourtellotte, W.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:7260-7264 !$#title Changes in brain gene expression shared by scrapie and !1Alzheimer disease. !$#cross-references MUID:89386721; PMID:2780570 !$#accession I63133 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 636-696 ##label RE2 !'##cross-references GB:M26641; NID:g339988; PIDN:AAA61233.1; !1PID:g339989 REFERENCE I54011 !$#authors Schaeffer, E.; Lucero, M.A.; Jeltsch, J.M.; Py, M.C.; Levin, !1M.J.; Chambon, P.; Cohen, G.N.; Zakin, M.M. !$#journal Gene (1987) 56:109-116 !$#title Complete structure of the human transferrin gene. Comparison !1with analogous chicken gene and human pseudogene. !$#cross-references MUID:88056305; PMID:3678832 !$#accession I54011 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-72 ##label RE3 !'##cross-references GB:M17611; NID:g339480; PIDN:AAA61147.1; !1PID:g339485 !$#accession I68160 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 564-698 ##label RE4 !'##cross-references GB:M17614; NID:g339483; PIDN:AAA61148.1; !1PID:g339486 COMMENT Each of the two repetitive domains binds a ferric ion and a !1bicarbonate anion. Concomitant binding of the anion is !1essential for metal binding at each site. GENETICS !$#gene GDB:TF !'##cross-references GDB:120432; OMIM:190000 !$#map_position 3q21-3q21 !$#introns 15/1; 72/3; 119/1; 168/1; 212/2; 231/1; 290/3; 350/1; 401/3; !1433/1; 444/1; 496/1; 541/2; 563/1; 624/3; 688/1 FUNCTION !$#description binds iron for delivery into cells CLASSIFICATION #superfamily transferrin; transferrin repeat homology KEYWORDS duplication; glycoprotein; iron transport; metal binding; !1plasma FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-698 #product transferrin #status experimental #label MAT\ !$20-350 #domain transferrin repeat homology #label TRH1\ !$356-686 #domain transferrin repeat homology #label TRH2\ !$28-67,38-58, !$137-213,156-350, !$177-193,180-196, !$190-198,246-260, !$358-615,364-396, !$374-387,421-693, !$437-656,469-542, !$493-684,503-517, !$514-525,582-596, !$634-639 #disulfide_bonds #status experimental\ !$432,630 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 698 #molecular-weight 77049 #checksum 8374 SEQUENCE /// ENTRY S01384 #type complete TITLE transferrin - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 11-May-2000 ACCESSIONS S01384; A60520; A61573 REFERENCE S01384 !$#authors Baldwin, G.S.; Weinstock, J. !$#journal Nucleic Acids Res. (1988) 16:8720 !$#title Nucleotide sequence of porcine liver transferrin. !$#cross-references MUID:88335629; PMID:3419934 !$#accession S01384 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-696 ##label BAL !'##cross-references EMBL:X12386; NID:g2126; PIDN:CAA30943.1; !1PID:g833800 !'##note 308-Arg was also found REFERENCE A60520 !$#authors Baldwin, G.S.; Bacic, T.; Chandler, R.; Grego, B.; Pedersen, !1J.; Simpson, R.J.; Toh, B.H.; Weinstock, J. !$#journal Comp. Biochem. Physiol. B (1990) 95:261-268 !$#title Isolation of transferrin from porcine gastric mucosa: !1comparison with porcine serum transferrin. !$#cross-references MUID:90227903; PMID:2328566 !$#accession A60520 !'##molecule_type protein !'##residues 1-8,'X',10-11,'X',13-15 ##label BA2 !'##experimental_source gastric mucosa !'##note the authors suggest transferrin from gastric mucosa may act in !1dietary iron uptake REFERENCE A61573 !$#authors Chung, M.C.M.; Chan, S.L.; Shimizu, S. !$#journal Int. J. Biochem. (1991) 23:609-616 !$#title Purification of transferrins and lactoferrin using DEAE !1Affi-Gel Blue. !$#cross-references MUID:91293379; PMID:2065820 !$#accession A61573 !'##molecule_type protein !'##residues 1-8,'X',10-18,'XE' ##label CHU CLASSIFICATION #superfamily transferrin; transferrin repeat homology KEYWORDS duplication; glycoprotein; iron transport; plasma FEATURE !$1-696 #product transferrin #status predicted #label MAT\ !$1-335 #domain transferrin repeat homology #label TRH1 SUMMARY #length 696 #molecular-weight 76967 #checksum 6767 SEQUENCE /// ENTRY TFHUL #type complete TITLE lactotransferrin precursor [validated] - human ALTERNATE_NAMES lactoferrin ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1992 #sequence_revision 21-Nov-1997 #text_change 08-Dec-2000 ACCESSIONS G01394; S11228; A45401; S10324; S15853; S20841; S07160; !1A61169; A31000; S74119; A03261; A38029 REFERENCE G06820 !$#authors Cho, Y. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession G01394 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-711 ##label CHO !'##cross-references EMBL:U07643; NID:g467236; PIDN:AAB60324.1; !1PID:g467237 REFERENCE S11228 !$#authors Rey, M.W.; Woloshuk, S.L.; deBoer, H.A.; Pieper, F.R. !$#journal Nucleic Acids Res. (1990) 18:5288 !$#title Complete nucleotide sequence of human mammary gland !1lactoferrin. !$#cross-references MUID:90384839; PMID:2402455 !$#accession S11228 !'##molecule_type mRNA !'##residues 1-148,'T',150-422,'C',424-711 ##label REY !'##cross-references EMBL:X53961; NID:g34415; PIDN:CAA37914.1; !1PID:g34416 REFERENCE A45401 !$#authors Teng, C.T.; Liu, Y.; Yang, N.; Walmer, D.; Panella, T. !$#journal Mol. Endocrinol. (1992) 6:1969-1981 !$#title Differential molecular mechanism of the estrogen action that !1regulates lactoferrin gene in human and mouse. !$#cross-references MUID:93125571; PMID:1480183 !$#accession A45401 !'##molecule_type DNA !'##residues 1-15 ##label TEN !'##cross-references GB:S52659; NID:g263311; PIDN:AAB24877.1; !1PID:g263312 !'##experimental_source placenta !'##note sequence extracted from NCBI backbone (NCBIP:122202) REFERENCE S10324 !$#authors Powell, M.J.; Ogden, J.E. !$#journal Nucleic Acids Res. (1990) 18:4013 !$#title Nucleotide sequence of human lactoferrin cDNA. !$#cross-references MUID:90326549; PMID:2374734 !$#accession S10324 !'##molecule_type mRNA !'##residues 3-711 ##label POW !'##cross-references EMBL:X52941; NID:g34411; PIDN:CAA37116.1; !1PID:g34412 REFERENCE S15853 !$#authors Stowell, K.M.; Rado, T.A.; Funk, W.D.; Tweedie, J.W. !$#journal Biochem. J. (1991) 276:349-355 !$#title Expression of cloned human lactoferrin in baby-hamster !1kidney cells. !$#cross-references MUID:91264786; PMID:2049066 !$#accession S15853 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type mRNA !'##residues 20-31 ##label ST1 !$#accession S20841 !'##molecule_type protein !'##residues 20-28,'X',30-31 ##label ST2 REFERENCE S07160 !$#authors Rado, T.A.; Wei, X.; Benz Jr., E.J. !$#journal Blood (1987) 70:989-993 !$#title Isolation of lactoferrin cDNA from a human myeloid library !1and expression of mRNA during normal and leukemic !1myelopoiesis. !$#cross-references MUID:88001031; PMID:3477300 !$#accession S07160 !'##molecule_type mRNA !'##residues 436-487,'A',489-711 ##label RAD !'##cross-references EMBL:M18642; NID:g186815; PIDN:AAA86665.1; !1PID:g386855 REFERENCE A61169 !$#authors Panella, T.J.; Liu, Y.; Huang, A.T.; Teng, C.T. !$#journal Cancer Res. (1991) 51:3037-3043 !$#title Polymorphism and altered methylation of the lactoferrin gene !1in normal leukocytes, leukemic cells, and breast cancer. !$#cross-references MUID:91235214; PMID:1674448 !$#accession A61169 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 3-701,'SWKPVN' ##label PAN !'##experimental_source normal breast tissue REFERENCE A31000 !$#authors Metz-Boutigue, M.H.; Jolles, J.; Mazurier, J.; Schoentgen, !1F.; Legrand, D.; Spik, G.; Montreuil, J.; Jolles, P. !$#journal Eur. J. Biochem. (1984) 145:659-666 !$#title Human lactotransferrin: amino acid sequence and structural !1comparisons with other transferrins. !$#cross-references MUID:85076667; PMID:6510420 !$#accession A31000 !'##molecule_type protein !'##residues 20-140,142-169,171-203,'L',205,'K',207-208,'K',210-385,'Q', !1387-391,'W',393-409,'N',411,'SVLMDSEGGFLAR',412-531,'E', !1533-694,'R',696-711 ##label MET !'##note this is the final paper in a series REFERENCE S74119 !$#authors Houen, G.; Hoegdall, E.V.; Barkholt, V.; Norskov, L. !$#journal Eur. J. Biochem. (1996) 241:303-308 !$#title Lactoferrin: similarity to diamine oxidase and purification !1by aminohexyl affinity chromatography. !$#cross-references MUID:97054624; PMID:8898921 !$#accession S74119 !'##molecule_type protein !'##residues 'G',23-24,'R',26-27,'XX',30-32 ##label HOU !'##experimental_source neutrophil granulocytes GENETICS !$#gene GDB:LTF !'##cross-references GDB:119368; OMIM:150210 !$#map_position 3q21-3q23 CLASSIFICATION #superfamily transferrin; transferrin repeat homology KEYWORDS duplication; glycoprotein; iron binding; milk FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-711 #product lactotransferrin #status experimental #label !8MAT\ !$21-356 #domain transferrin repeat homology #label TRH1\ !$360-699 #domain transferrin repeat homology #label TRH2\ !$29-65,39-56, !$135-218,177-193, !$190-201,251-265, !$503-697,595-609 #disulfide_bonds #status experimental\ !$157,498 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$368-400,378-391, !$425-706,447-669, !$479-554,513-527, !$524-537,647-652 #disulfide_bonds #status predicted SUMMARY #length 711 #molecular-weight 78337 #checksum 8418 SEQUENCE /// ENTRY TFBOL #type complete TITLE lactotransferrin precursor - bovine ALTERNATE_NAMES lactoferrin ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Mar-1992 #sequence_revision 21-Nov-1997 #text_change 11-May-2000 ACCESSIONS I45919; S14674; S14110; S18517; JT0595; S13097; S18518; !1S13881; PL0148; S21756; A56659 REFERENCE I45919 !$#authors Tsang, T.C.; Burns, D.K.; Wang, F.; Pan, Y. !$#journal FASEB J. (1991) 6:233 !$#title Cloning of a 80-kD advanced glycosylation end product (AGE) !1binding protein from bovine lung. !$#accession I45919 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-708 ##label TSA !'##cross-references GB:L08604; NID:g163269; PIDN:AAA30609.1; !1PID:g163270 REFERENCE S14674 !$#authors Pierce, A. !$#submission submitted to the EMBL Data Library, November 1990 !$#accession S14674 !'##molecule_type mRNA !'##residues 1-144,'V',146-163,'PP',166-339,'A',341-438,'Y',440-513,'R', !1515-708 ##label PI1 !'##cross-references EMBL:X57084; NID:g505; PIDN:CAA40366.1; PID:g506 REFERENCE S14110 !$#authors Pierce, A.; Colavizza, D.; Benaissa, M.; Maes, P.; Tartar, !1A.; Montreuil, J.; Spik, G. !$#journal Eur. J. Biochem. (1991) 196:177-184 !$#title Molecular cloning and sequence analysis of bovine !1lactotransferrin. !$#cross-references MUID:91160550; PMID:2001696 !$#accession S14110 !'##molecule_type mRNA !'##residues 3-144,'V',146-339,'A',341-438,'Y',440-513,'R',515-708 !1##label PI2 !'##cross-references EMBL:X57084 !$#accession S18517 !'##molecule_type protein !'##residues 20-35;82-114;148-163,'PP',166-178,'V', !1'P';183-190;205-212;230-239;304-339;598-619;670-692 ##label !1PIE REFERENCE JT0595 !$#authors Goodman, R.E.; Schanbacher, F.L. !$#journal Biochem. Biophys. Res. Commun. (1991) 180:75-84 !$#title Bovine lactoferrin mRNA: sequence, analysis, and expression !1in the mammary gland. !$#cross-references MUID:92028986; PMID:1718281 !$#accession JT0595 !'##molecule_type mRNA !'##residues 1-65,'PG',68-296,'S',298-339,'A',341-708 ##label GOO !'##cross-references GB:M63502 !'##note the authors translated the codon CCG for residue 66 as Arg and !1TCT for residue 297 as Phe REFERENCE S13097 !$#authors Mead, P.E.; Tweedie, J.W. !$#journal Nucleic Acids Res. (1990) 18:7167 !$#title cDNA and protein sequence of bovine lactoferrin. !$#cross-references MUID:91088328; PMID:2263492 !$#accession S13097 !'##molecule_type mRNA !'##residues 28-33,'DS',36-38,'P',40-708 ##label MEA !'##cross-references EMBL:X54801 !$#accession S18518 !'##molecule_type protein !'##residues 20-47;59-66;132-139;256-277;278, !1305-332;343-351;361-363;586,587-589;598-619 ##label ME2 REFERENCE S13881 !$#authors Mead, P.E. !$#submission submitted to the EMBL Data Library, October 1990 !$#accession S13881 !'##molecule_type mRNA !'##residues 28-38,'P',40-86,'C',88-708 ##label ME3 !'##cross-references EMBL:X54801 REFERENCE PL0148 !$#authors Rejman, J.J.; Hegarty, H.M.; Hurley, W.L. !$#journal Comp. Biochem. Physiol. B (1989) 93:929-934 !$#title Purification and characterization of bovine lactoferrin from !1secretions of the involuting mammary gland: identification !1of multiple molecular weight forms. !$#cross-references MUID:90031466; PMID:2805645 !$#accession PL0148 !'##molecule_type protein !'##residues 20-27,'X',29-37,'X',39-54,'X',56-59 ##label REJ REFERENCE S21756 !$#authors Bellamy, W.; Takase, M.; Yamauchi, K.; Wakabayashi, H.; !1Kawase, K.; Tomita, M. !$#journal Biochim. Biophys. Acta (1992) 1121:130-136 !$#title Identification of the bactericidal domain of lactoferrin. !$#cross-references MUID:92287941; PMID:1599934 !$#accession S21756 !'##molecule_type protein !'##residues 36-60 ##label BEL REFERENCE A56659 !$#authors Shimazaki, K.; Tanaka, T.; Kon, H.; Oota, K.; Kawaguchi, A.; !1Maki, Y.; Sato, T. !$#journal J. Dairy Sci. (1993) 76:946-955 !$#title Separation and characterization of the C-terminal half !1molecule of bovine lactoferrin. !$#cross-references MUID:93253156; PMID:8486845 !$#accession A56659 !'##molecule_type protein !'##residues 20-25;302-308;359-366,'X',368-376,'X',378 ##label SHI CLASSIFICATION #superfamily transferrin; transferrin repeat homology KEYWORDS duplication; glycoprotein; iron; iron binding; !1metalloprotein; milk FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-708 #product lactotransferrin #status experimental #label !8MAT\ !$20-355 #domain transferrin repeat homology #label TRH1\ !$36-60 #region antimicrobial\ !$359-696 #domain transferrin repeat homology #label TRH2\ !$28-64,134-217, !$176-192,179-200, !$189-202,250-264, !$367-399,377-390, !$424-703,444-666, !$476-551,500-694, !$510-524,521-534, !$592-606,644-649 #disulfide_bonds #status predicted\ !$38-55 #disulfide_bonds #status predicted\ !$79,111,211,272 #binding_site iron (Asp, Tyr, Tyr, His) #status !8experimental\ !$140 #binding_site carbonate (Arg) #status experimental\ !$252,300,387,495,564 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$414,452,545,614 #binding_site iron (Asp, Tyr, Tyr, His) #status !8experimental\ !$482 #binding_site carbonate (Arg) #status experimental SUMMARY #length 708 #molecular-weight 78056 #checksum 9805 SEQUENCE /// ENTRY A28438 #type complete TITLE lactoferrin precursor - mouse ALTERNATE_NAMES lactotransferrin ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A28438; A41205 REFERENCE A92596 !$#authors Pentecost, B.T.; Teng, C.T. !$#journal J. Biol. Chem. (1987) 262:10134-10139 !$#title Lactotransferrin is the major estrogen inducible protein of !1mouse uterine secretions. !$#cross-references MUID:87280033; PMID:3611056 !$#accession A28438 !'##molecule_type mRNA !'##residues 3-707 ##label PEN !'##cross-references EMBL:J03298 REFERENCE A41205 !$#authors Liu, Y.; Teng, C.T. !$#journal J. Biol. Chem. (1991) 266:21880-21885 !$#title Characterization of estrogen-responsive mouse lactoferrin !1promoter. !$#cross-references MUID:92042099; PMID:1939212 !$#accession A41205 !'##molecule_type DNA !'##residues 1-15 ##label LIU !'##cross-references GB:M74778 CLASSIFICATION #superfamily transferrin; transferrin repeat homology KEYWORDS duplication; glycoprotein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-707 #product lactotransferrin #status predicted #label !8MAT\ !$358-695 #domain transferrin repeat homology #label TRH2\ !$494 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 707 #molecular-weight 77895 #checksum 1594 SEQUENCE /// ENTRY A36500 #type complete TITLE transferrin precursor - tobacco hornworm ORGANISM #formal_name Manduca sexta #common_name tobacco hornworm DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A36500 REFERENCE A36500 !$#authors Bartfeld, N.S.; Law, J.H. !$#journal J. Biol. Chem. (1990) 265:21684-21691 !$#title Isolation and molecular cloning of transferrin from the !1tobacco hornworm, Manduca sexta. Sequence similarity to the !1vertebrate transferrins. !$#cross-references MUID:91072368; PMID:2254322 !$#accession A36500 !'##status preliminary !'##molecule_type mRNA !'##residues 1-681 ##label BAR !'##cross-references GB:M62802; GB:M36296; NID:g159543; PIDN:AAA29338.1; !1PID:g159544 CLASSIFICATION #superfamily transferrin; transferrin repeat homology KEYWORDS duplication SUMMARY #length 681 #molecular-weight 75222 #checksum 9579 SEQUENCE /// ENTRY TFRBP #type complete TITLE transferrin precursor - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 22-Jun-1999 ACCESSIONS S16246; A61239; C61573; S00335; S02694; A26504; S14853 REFERENCE S16246 !$#authors Banfield, D.K.; Chow, B.K.C.; Funk, W.D.; Robertson, K.A.; !1Umelas, T.M.; Woodworth, R.C.; MacGillivray, R.T.A. !$#journal Biochim. Biophys. Acta (1991) 1089:262-265 !$#title The nucleotide sequence of rabbit liver transferrin cDNA. !$#cross-references MUID:91274362; PMID:2054387 !$#accession S16246 !'##molecule_type mRNA !'##residues 1-694 ##label BAN !'##cross-references EMBL:X58533; NID:g1750; PIDN:CAA41424.1; PID:g1751 REFERENCE A61239 !$#authors Pierpaoli, W.; Dall'Ara, A.; Yi, C.; Neri, P.; Santucci, A.; !1Choay, J. !$#journal Cell. Immunol. (1991) 134:225-234 !$#title Iron carrier proteins facilitate engraftment of allogeneic !1bone marrow and enduring hemopoietic chimerism in the !1lethally irradiated host. !$#cross-references MUID:91191584; PMID:2013104 !$#accession A61239 !'##molecule_type protein !'##residues 19-36 ##label PIE REFERENCE A61573 !$#authors Chung, M.C.M.; Chan, S.L.; Shimizu, S. !$#journal Int. J. Biochem. (1991) 23:609-616 !$#title Purification of transferrins and lactoferrin using DEAE !1Affi-Gel Blue. !$#cross-references MUID:91293379; PMID:2065820 !$#accession C61573 !'##molecule_type protein !'##residues 19-26,'X',28-36,'X',38-53 ##label CHU REFERENCE S00335 !$#authors Godovac-Zimmermann, J. !$#journal Biol. Chem. Hoppe-Seyler (1988) 369:93-96 !$#title Isolation, characterization and N-terminal amino-acid !1sequence of rabbit transferrin. !$#cross-references MUID:88209278; PMID:3365331 !$#accession S00335 !'##molecule_type protein !'##residues 19-45,'S',47-48,'Y',50 ##label GOD REFERENCE S02694 !$#authors Evans, R.W.; Aitken, A.; Patel, K.J. !$#journal FEBS Lett. (1988) 238:39-42 !$#title Evidence for a single glycan moiety in rabbit serum !1transferrin and location of the glycan within the !1polypeptide chain. !$#cross-references MUID:89005676; PMID:3169252 !$#accession S02694 !'##molecule_type protein !'##residues 482-515,'V',517-544 ##label EVA !'##note 516-Ile was also found REFERENCE A26504 !$#authors Heaphy, S.; Williams, J. !$#journal Biochem. J. (1982) 205:611-617 !$#title The preparation and partial characterization of N-terminal !1and C-terminal iron-binding fragments from rabbit serum !1transferrin. !$#cross-references MUID:83074540; PMID:6816218 !$#accession A26504 !'##molecule_type protein !'##residues 19-24,'N',26,'X',28-29,'S' ##label HEA CLASSIFICATION #superfamily transferrin; transferrin repeat homology KEYWORDS duplication; glycoprotein; iron transport; metal binding; !1plasma FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-694 #product transferrin #status experimental #label MAT\ !$19-349 #domain transferrin repeat homology #label TRH1\ !$355-682 #domain transferrin repeat homology #label TRH2\ !$27-66,37-57, !$136-212,155-349, !$176-192,179-195, !$189-197,245-259, !$357-611,363-395, !$373-386,420-689, !$435-652,467-538, !$491-680,501-515, !$512-521,578-592, !$630-635 #disulfide_bonds #status predicted\ !$508 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 694 #molecular-weight 76613 #checksum 7323 SEQUENCE /// ENTRY TFCHE #type complete TITLE ovotransferrin precursor - chicken ALTERNATE_NAMES conalbumin; transferrin ORGANISM #formal_name Gallus gallus #common_name chicken DATE 24-Apr-1984 #sequence_revision 30-Sep-1993 #text_change 22-Jun-1999 ACCESSIONS A26845; A91115; A92229; A91116; A40674; B61573; A90282; !1S02476; A03262 REFERENCE A26845 !$#authors Jeltsch, J.M.; Hen, R.; Maroteaux, L.; Garnier, J.M.; !1Chambon, P. !$#journal Nucleic Acids Res. (1987) 15:7643-7645 !$#title Sequence of the chicken ovotransferrin gene. !$#cross-references MUID:88015626; PMID:3658709 !$#accession A26845 !'##molecule_type DNA !'##residues 1-705 ##label JE1 !'##cross-references GB:Y00407; NID:g63131; PIDN:CAA68468.1; PID:g295721 REFERENCE A91115 !$#authors Jeltsch, J.M.; Chambon, P. !$#journal Eur. J. Biochem. (1982) 122:291-295 !$#title The complete nucleotide sequence of the chicken !1ovotransferrin mRNA. !$#cross-references MUID:82138851; PMID:7060577 !$#accession A91115 !'##molecule_type mRNA !'##residues 1-82,'V',84-99,'I',101-153,'W',155-238,'LN',241-685,'N', !1687-705 ##label JE2 !'##cross-references EMBL:X02009 !'##note the codons given for residues 132 (AAC) and 317 (UUC) are !1inconsistent with the authors' translation and with the !1protein sequencing results REFERENCE A92229 !$#authors Thibodeau, S.N.; Lee, D.C.; Palmiter, R.D. !$#journal J. Biol. Chem. (1978) 253:3771-3774 !$#title Identical precursors for serum transferrin and egg white !1conalbumin. !$#cross-references MUID:78171533; PMID:649604 !$#accession A92229 !'##molecule_type protein !'##residues 1-23 ##label THI REFERENCE A91116 !$#authors Williams, J.; Elleman, T.C.; Kingston, I.B.; Wilkins, A.G.; !1Kuhn, K.A. !$#journal Eur. J. Biochem. (1982) 122:297-303 !$#title The primary structure of hen ovotransferrin. !$#cross-references MUID:82138852; PMID:6895872 !$#accession A91116 !'##molecule_type protein !'##residues 1-50;54-82,'V', !184-92;102-146;162-168;170-228;241-283;289-333;338-344; !1350-351;361-373;381-464;471-612;625-629;634-641;645-685,'N', !1687-705 ##label WIL REFERENCE A40674 !$#authors Gentili, C.; Bianco, P.; Neri, M.; Malpeli, M.; Campanile, !1G.; Castagnola, P.; Cancedda, R.; Descalzi Cancedda, F. !$#journal J. Cell Biol. (1993) 122:703-712 !$#title Cell proliferation, extracellular matrix mineralization, and !1ovotransferrin transient expression during in vitro !1differentiation of chick hypertrophic chondrocytes into !1osteoblast-like cells. !$#cross-references MUID:93328771; PMID:8393014 !$#accession A40674 !'##molecule_type protein !'##residues 20-28,'X',30-38,'X',40-44 ##label GEN REFERENCE A61573 !$#authors Chung, M.C.M.; Chan, S.L.; Shimizu, S. !$#journal Int. J. Biochem. (1991) 23:609-616 !$#title Purification of transferrins and lactoferrin using DEAE !1Affi-Gel Blue. !$#cross-references MUID:91293379; PMID:2065820 !$#accession B61573 !'##molecule_type protein !'##residues 20-28,'X',30-38,'X',40-43,'S' ##label CHU REFERENCE A90282 !$#authors Kingston, I.B.; Williams, J. !$#journal Biochem. J. (1975) 147:463-472 !$#title The amino acid sequence of a carbohydrate-containing !1fragment of hen ovotransferrin. !$#cross-references MUID:76039467; PMID:1172663 !$#accession A90282 !'##molecule_type protein !'##residues 480-582 ##label KIN REFERENCE A90246 !$#authors Elleman, T.C.; Williams, J. !$#journal Biochem. J. (1970) 116:515-532 !$#title The amino acid sequences of cysteic acid-containing peptides !1from performic acid-oxidized ovotransferrin. !$#cross-references MUID:70141846; PMID:4907959 !$#contents annotation; disulfide bonds REFERENCE S02476 !$#authors Williams, J.; Moreton, K. !$#journal Biochem. J. (1988) 251:849-855 !$#title The dimerization of half-molecule fragments of transferrin. !$#cross-references MUID:88326225; PMID:3415649 !$#accession S02476 !'##molecule_type protein !'##residues 20-23;295-302;336-366;674-679,'T',681,'F',683-685,'N', !1687-705 ##label WI2 COMMENT Ovotransferrin (conalbumin) and transferrin have identical !1protein components (apotransferrin) and differ only in their !1glycan chains. Ovotransferrin is synthesized in the oviduct. !1Transferrin is synthesized in the liver. COMMENT Ovotransferrin has a bacteriostatic function. Its !1concentration in avian egg white is the highest !1concentration of any transferrin in vivo. COMMENT Plasma apotransferrin promotes the oxidation of ferrous !1ions, which would otherwise catalyze the production of toxic !1hydroxyl radicals. COMMENT In electrophoretic and genetic studies, transferrin shows !1strong polymorphism, which is controlled by codominant !1alleles. GENETICS !$#introns 15/1; 69/3; 106/1; 170/1; 215/2; 234/1; 290/3; 353/1; 404/3; !1436/1; 448/1; 500/1; 548/2; 570/1; 631/3; 694/1 CLASSIFICATION #superfamily transferrin; transferrin repeat homology KEYWORDS duplication; egg white; glycoprotein; iron binding; plasma FEATURE !$1-19 #domain signal sequence #status experimental #label !8SIG\ !$20-705 #product transferrin #status experimental #label MAT\ !$21-355 #domain transferrin repeat homology #label TRH1\ !$359-692 #domain transferrin repeat homology #label TRH2\ !$29-64,134-216, !$179-193,190-201, !$247-261,367-399, !$424-699,440-662, !$473-549,497-690 #disulfide_bonds #status experimental\ !$39-55,377-390, !$589-603 #disulfide_bonds #status predicted\ !$492 #binding_site carbohydrate (Asn) (covalent) (partial) !8#status experimental\ !$507-521,518-532 #disulfide_bonds (or 507-518, 521-532) #status !8predicted SUMMARY #length 705 #molecular-weight 77776 #checksum 1985 SEQUENCE /// ENTRY TFHUM #type complete TITLE melanotransferrin precursor - human ALTERNATE_NAMES melanoma-associated antigen gp95/p97 ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 28-Jan-2000 ACCESSIONS A23814; A60925 REFERENCE A23814 !$#authors Rose, T.M.; Plowman, G.D.; Teplow, D.B.; Dreyer, W.J.; !1Hellstrom, K.E.; Brown, J.P. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:1261-1265 !$#title Primary structure of the human melanoma-associated antigen !1p97 (melanotransferrin) deduced from the mRNA sequence. !$#cross-references MUID:86149285; PMID:2419904 !$#accession A23814 !'##molecule_type mRNA !'##residues 1-738 ##label ROS !'##cross-references EMBL:M12154; NID:g189515; PIDN:AAA59992.1; !1PID:g189518 !'##experimental_source melanoma REFERENCE A60925 !$#authors Furukawa, K.S.; Furukawa, K.; Real, F.X.; Old, L.J.; Lloyd, !1K.O. !$#journal J. Exp. Med. (1989) 169:585-590 !$#title A unique antigenic epitope of human melanoma is carried on !1the common melanoma glycoprotein gp95/p97. !$#cross-references MUID:89094252; PMID:2463331 !$#accession A60925 !'##molecule_type protein !'##residues 20-25,'X',27-28,'X',30 ##label FUR COMMENT This protein is found predominantly in human melanomas and !1in certain fetal tissues; it is found in only trace amounts !1in normal adult tissues. COMMENT Seven disulfide bonds are predicted in each domain. GENETICS !$#gene GDB:MFI2 !'##cross-references GDB:119387; OMIM:155750 !$#map_position 3q28-3q29 CLASSIFICATION #superfamily transferrin; transferrin repeat homology KEYWORDS blocked carboxyl end; duplication; glycoprotein; !1lipoprotein; membrane protein; metal binding; !1phosphatidylinositol linkage; phosphoprotein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$18-360 #domain transferrin repeat homology #label TRH1\ !$20-710 #product melanotransferrin #status predicted #label !8MTF\ !$361-709 #domain transferrin repeat homology #label TRH2\ !$711-738 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$38,135,515 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$710 #modified_site GPI-anchor ethanolamine amidated !8carboxyl end (Ser) (in mature form) #status predicted SUMMARY #length 738 #molecular-weight 80241 #checksum 9466 SEQUENCE /// ENTRY A39684 #type complete TITLE hemiferrin - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A39684 REFERENCE A39684 !$#authors Stallard, B.J.; Collard, M.W.; Griswold, M.D. !$#journal Mol. Cell. Biol. (1991) 11:1448-1453 !$#title A transferrinlike (hemiferrin) mRNA is expressed in the germ !1cells of rat testis. !$#cross-references MUID:91141493; PMID:1996102 !$#accession A39684 !'##molecule_type mRNA !'##residues 1-216 ##label STA !'##cross-references GB:M60388 CLASSIFICATION #superfamily hemiferrin; transferrin repeat homology KEYWORDS glycoprotein; testis FEATURE !$1-204 #domain transferrin repeat homology #status atypical !8#label TRH2 SUMMARY #length 216 #molecular-weight 24091 #checksum 5095 SEQUENCE /// ENTRY OQHU #type complete TITLE hemopexin precursor [validated] - human ALTERNATE_NAMES beta-1B-glycoprotein ORGANISM #formal_name Homo sapiens #common_name man DATE 28-Aug-1985 #sequence_revision 02-Jul-1996 #text_change 08-Dec-2000 ACCESSIONS I56456; I54212; A93566; A94069; A91328; A43791; A03263 REFERENCE I56456 !$#authors Altruda, F.; Poli, V.; Restagno, G.; Silengo, L. !$#journal J. Mol. Evol. (1988) 27:102-108 !$#title Structure of the human hemopexin gene and evidence for !1intron-mediated evolution. !$#cross-references MUID:88316972; PMID:2842511 !$#accession I56456 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-462 ##label RES !'##cross-references GB:M36803; NID:g184495; PIDN:AAA58678.1; !1PID:g184497 REFERENCE I54212 !$#authors Law, M.L.; Cai, G.Y.; Hartz, J.A.; Jones, C.; Kao, F.T. !$#journal Genomics (1988) 3:48-52 !$#title The hemopexin gene maps to the same location as the !1beta-globin gene cluster on human chromosome 11. !$#cross-references MUID:89122012; PMID:3220477 !$#accession I54212 !'##status nucleic acid sequence not shown; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 2-462 ##label RE2 !'##cross-references GB:J03048; NID:g184487; PIDN:AAA52704.1; !1PID:g386789 REFERENCE A93566 !$#authors Altruda, F.; Poli, V.; Restagno, G.; Argos, P.; Cortese, R.; !1Silengo, L. !$#journal Nucleic Acids Res. (1985) 13:3841-3859 !$#title The primary structure of human hemopexin deduced from cDNA !1sequence: evidence for internal, repeating homology. !$#cross-references MUID:85242073; PMID:2989777 !$#accession A93566 !'##molecule_type mRNA !'##residues 22-462 ##label ALT REFERENCE A94069 !$#authors Takahashi, N.; Takahashi, Y.; Putnam, F.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:73-77 !$#title Complete amino acid sequence of human hemopexin, the !1heme-binding protein of serum. !$#cross-references MUID:85113173; PMID:3855550 !$#accession A94069 !'##molecule_type protein !'##residues 24-462 ##label TAK REFERENCE A91328 !$#authors Frantikova, V.; Borvak, J.; Kluh, I.; Moravek, L. !$#journal FEBS Lett. (1984) 178:213-216 !$#title Amino acid sequence of the N-terminal region of human !1hemopexin. !$#cross-references MUID:85076955; PMID:6510521 !$#accession A91328 !'##molecule_type protein !'##residues 24-255 ##label FRA REFERENCE A43791 !$#authors Takahashi, N.; Takahashi, Y.; Putnam, F.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:2021-2025 !$#title Structure of human hemopexin: O-glycosyl and N-glycosyl !1sites and unusual clustering of tryptophan residues. !$#cross-references MUID:84193947; PMID:6371807 !$#accession A43791 !'##molecule_type protein !'##residues 24-49;62-67;178-192;236-250;443-457 ##label TA2 COMMENT Hemopexin is a serum glycoprotein that binds heme and !1transports it to the liver for breakdown and iron recovery, !1after which the free hemopexin returns to the circulation. GENETICS !$#gene GDB:HPX !'##cross-references GDB:120054; OMIM:142290 !$#map_position 11p15.4-11p15.4 !$#introns 28/2; 48/1; 72/1; 112/3; 164/1; 235/1; 279/1; 322/3; 377/1 CLASSIFICATION #superfamily hemopexin; hemopexin repeat homology KEYWORDS acute phase; duplication; glycoprotein; heme binding; plasma FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-462 #product hemopexin #status experimental #label HPX\ !$44-231 #domain hemopexin repeat homology #label PX1\ !$252-460 #domain hemopexin repeat homology #label PX2\ !$24 #binding_site carbohydrate (Thr) (covalent) #status !8experimental\ !$50-231,149-154, !$188-200,257-460, !$366-408,418-435 #disulfide_bonds #status experimental\ !$64,187,240,246,453 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 462 #molecular-weight 51676 #checksum 5322 SEQUENCE /// ENTRY OQRB #type complete TITLE hemopexin precursor - rabbit ALTERNATE_NAMES beta-1B-glycoprotein ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 21-Sep-1993 #sequence_revision 13-Jan-1995 #text_change 03-Mar-2000 ACCESSIONS A46006; B46006; A61426; B31514 REFERENCE A46006 !$#authors Morgan, W.T.; Muster, P.; Tatum, F.; Kao, S.M.; Alam, J.; !1Smith, A. !$#journal J. Biol. Chem. (1993) 268:6256-6262 !$#title Identification of the histidine residues of hemopexin that !1coordinate with heme-iron and of a receptor-binding region. !$#cross-references MUID:93203213; PMID:7681064 !$#accession A46006 !'##molecule_type mRNA !'##residues 1-459 ##label MOR !'##note sequence extracted from NCBI backbone (NCBIN:127918, !1NCBIP:127919) !$#accession B46006 !'##molecule_type protein !'##residues 26-32;104-108;239-242,'X',243-244 ##label MO2 !'##note residues 42-46 are shown as 'TKPEA' in the Fig. 2 alignment, !1with no explanation of this discrepancy (between their !1mRNA-derived sequence and that they reported also in !1reference A61426) REFERENCE A61426 !$#authors Muster, P.; Tatum, F.; Smith, A.; Morgan, W.T. !$#journal J. Protein Chem. (1991) 10:123-128 !$#title Further characterization of structural determinants of !1rabbit hemopexin function. !$#cross-references MUID:91273754; PMID:2054057 !$#accession A61426 !'##molecule_type protein !'##residues 26-41,'TKPEA',47-51 ##label MUS REFERENCE A90148 !$#authors Wellner, D.; Cheng, K.C.; Muller-Eberhard, U. !$#journal Biochem. Biophys. Res. Commun. (1988) 155:622-625 !$#title N-terminal amino acid sequences of the hemopexins from !1chicken, rat and rabbit. !$#cross-references MUID:88339942; PMID:3421961 !$#accession B31514 !'##molecule_type protein !'##residues 26-33,'X',35-41,'TKPEA',47-51,'W',53 ##label WEL COMMENT Hemopexin is a serum glycoprotein that binds heme and !1transports it to the liver for breakdown and iron recovery, !1after which the free hemopexin returns to the circulation. COMMENT The JEN-14 monoclonal antibody, which blocks the interaction !1of hemopexin with its receptor, recognizes an epitope !1located between Ala-147 and Arg-167. CLASSIFICATION #superfamily hemopexin; hemopexin repeat homology KEYWORDS acute phase; chromoprotein; duplication; glycoprotein; heme; !1iron; metalloprotein; plasma FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-459 #product hemopexin #status experimental #label HPX\ !$46-232 #domain hemopexin repeat homology #label PX1\ !$249-457 #domain hemopexin repeat homology #label PX2\ !$34 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$52-232,150-155, !$189-201,254-457, !$363-405,415-432 #disulfide_bonds #status predicted\ !$66,188,243 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$81,151 #binding_site heme iron (His) (axial ligands) #status !8experimental SUMMARY #length 459 #molecular-weight 51728 #checksum 8702 SEQUENCE /// ENTRY OQRT #type complete TITLE hemopexin precursor - rat ALTERNATE_NAMES beta-1B-glycoprotein ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 28-Jun-1991 #sequence_revision 13-Jan-1995 #text_change 03-Mar-2000 ACCESSIONS A43079; A38399; A31514; A38139 REFERENCE A43079 !$#authors Nagae, Y.; Muller-Eberhard, U. !$#journal Biochem. Biophys. Res. Commun. (1992) 185:420-429 !$#title Identification of an interleukin-6 responsive element and !1characterization of the proximal promoter region of the rat !1hemopexin gene. !$#cross-references MUID:92287130; PMID:1599480 !$#accession A43079 !'##molecule_type DNA !'##residues 1-14 ##label NAG !'##cross-references GB:X60006; NID:g416183; PIDN:CAA42621.1; !1PID:g416184 REFERENCE A38399 !$#authors Nikkilae, H.; Gitlin, J.D.; Muller-Eberhard, U. !$#journal Biochemistry (1991) 30:823-829 !$#title Rat hemopexin. Molecular cloning, primary structural !1characterization, and analysis of gene expression. !$#cross-references MUID:91105180; PMID:1988069 !$#accession A38399 !'##molecule_type mRNA !'##residues 15-460 ##label NIK !'##cross-references GB:J05306 REFERENCE A90148 !$#authors Wellner, D.; Cheng, K.C.; Muller-Eberhard, U. !$#journal Biochem. Biophys. Res. Commun. (1988) 155:622-625 !$#title N-terminal amino acid sequences of the hemopexins from !1chicken, rat and rabbit. !$#cross-references MUID:88339942; PMID:3421961 !$#accession A31514 !'##molecule_type protein !'##residues 24-37,'C',39-48,'KW',51,'X',53 ##label WEL REFERENCE A38139 !$#authors Swerts, J.P.; Soula, C.; Sagot, Y.; Guinaudy, M.J.; !1Guillemot, J.C.; Ferrara, P.; Duprat, A.M.; Cochard, P. !$#journal J. Biol. Chem. (1992) 267:10596-10600 !$#title Hemopexin is synthesized in peripheral nerves but not in !1central nervous system and accumulates after axotomy. !$#cross-references MUID:92268104; PMID:1587840 !$#accession A38139 !'##molecule_type protein !'##residues 24-35,'X',37,'X',39-43 ##label SWE !'##experimental_source sciatic nerve; skeletal muscle !'##note the amino-terminal sequence of the mature protein was !1determined COMMENT Hemopexin is a serum glycoprotein that binds heme and !1transports it to the liver for breakdown and iron recovery, !1after which the free hemopexin returns to the circulation. CLASSIFICATION #superfamily hemopexin; hemopexin repeat homology KEYWORDS acute phase; chromoprotein; duplication; glycoprotein; heme; !1iron; metalloprotein; plasma FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-460 #product hemopexin #status predicted #label HPX\ !$44-230 #domain hemopexin repeat homology #label PX1\ !$250-458 #domain hemopexin repeat homology #label PX2\ !$38,64,186,240,246 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$50-230,148-153, !$187-199,255-458, !$364-406,416-433 #disulfide_bonds #status predicted\ !$79,149 #binding_site heme iron (His) (axial ligands) #status !8predicted SUMMARY #length 460 #molecular-weight 51290 #checksum 1124 SEQUENCE /// ENTRY SGHU1V #type complete TITLE vitronectin precursor [validated] - human ALTERNATE_NAMES complement S protein; serum spreading factor CONTAINS somatomedin B ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 08-Dec-2000 ACCESSIONS A29744; A03265; A91014; A94633; A01402; A41373; B61142; !1A23744; S47561; S62642; A03264 REFERENCE A29744 !$#authors Jenne, D.; Stanley, K.K. !$#journal Biochemistry (1987) 26:6735-6742 !$#title Nucleotide sequence and organization of the human S-protein !1gene: repeating peptide motifs in the "pexin" family and a !1model for their evolution. !$#cross-references MUID:88107592; PMID:2447940 !$#accession A29744 !'##molecule_type DNA !'##residues 1-478 ##label JE1 !'##cross-references EMBL:X05006; NID:g36572; PIDN:CAA28659.1; !1PID:g36573 REFERENCE A03265 !$#authors Jenne, D.; Stanley, K.K. !$#journal EMBO J. (1985) 4:3153-3157 !$#title Molecular cloning of S-protein, a link between complement, !1coagulation and cell-substrate adhesion. !$#cross-references MUID:86135941; PMID:3004934 !$#accession A03265 !'##molecule_type mRNA !'##residues 1-365,'T',367-478 ##label JE2 !'##cross-references EMBL:X03168 REFERENCE A91014 !$#authors Suzuki, S.; Oldberg, A.; Hayman, E.G.; Pierschbacher, M.D.; !1Ruoslahti, E. !$#journal EMBO J. (1985) 4:2519-2524 !$#title Complete amino acid sequence of human vitronectin deduced !1from cDNA. Similarity of cell attachment sites in !1vitronectin and fibronectin. !$#cross-references MUID:86030229; PMID:2414098 !$#accession A91014 !'##molecule_type mRNA !'##residues 4-160;'STLHR',167-224,'S',226-365,'A',367-399,'T',401-441, !1'E',443-478 ##label SU1 !'##cross-references EMBL:X03168 REFERENCE A94633 !$#authors Suzuki, S.; Oldberg, A.; Hayman, E.G.; Pierschbacher, M.D.; !1Ruoslahti, E. !$#submission submitted to the Protein Sequence Database, June 1986 !$#contents revisions !$#accession A94633 !'##molecule_type mRNA !'##residues 1-224,'S',226-399,'T',401-478 ##label SU2 REFERENCE A01402 !$#authors Fryklund, L.; Sievertsson, H. !$#journal FEBS Lett. (1978) 87:55-60 !$#title Primary structure of somatomedin B. A growth !1hormone-dependent serum factor with protease inhibiting !1activity. !$#cross-references MUID:78127267; PMID:631332 !$#accession A01402 !'##molecule_type protein !'##residues 20-49,'N',51-52,'C',54-63 ##label FRY REFERENCE A41372 !$#authors Jenne, D.; Hille, A.; Stanley, K.K.; Huttner, W.B. !$#journal Eur. J. Biochem. (1989) 185:391-395 !$#title Sulfation of two tyrosine-residues in human complement !1S-protein (vitronectin). !$#cross-references MUID:90060125; PMID:2479556 !$#contents annotation REFERENCE A41373 !$#authors McGuire, E.A.; Peacock, M.E.; Inhorn, R.C.; Siegel, N.R.; !1Tollefsen, D.M. !$#journal J. Biol. Chem. (1988) 263:1942-1945 !$#title Phosphorylation of vitronectin by a protein kinase in human !1plasma. Identification of a unique phosphorylation site in !1the heparin-binding domain. !$#cross-references MUID:88115321; PMID:2448300 !$#accession A41373 !'##molecule_type protein !'##residues 393-399,'T' ##label MCG REFERENCE A61142 !$#authors Yaoi, Y.; Hashimoto, K.; Takahara, K.; Kato, I. !$#journal Exp. Cell Res. (1991) 194:180-185 !$#title Insulin binds to type V collagen with retention of mitogenic !1activity. !$#cross-references MUID:91224163; PMID:1709100 !$#accession B61142 !'##molecule_type protein !'##residues 360-368 ##label YAO REFERENCE A41374 !$#authors Chain, D.; Korc-Grodzicki, B.; Kreizman, T.; Shaltiel, S. !$#journal FEBS Lett. (1990) 269:221-225 !$#title The phosphorylation of the two-chain form of vitronectin by !1protein kinase A is heparin dependent. !$#cross-references MUID:90353578; PMID:1696913 !$#contents annotation REFERENCE A23744 !$#authors Seiffert, D.; Loskutoff, D.J. !$#journal J. Biol. Chem. (1991) 266:2824-2830 !$#title Evidence that type 1 plasminogen activator inhibitor binds !1to the somatomedin B domain of vitronectin. !$#cross-references MUID:91131573; PMID:1704366 !$#accession A23744 !'##molecule_type protein !'##residues 20-23,'X',25-26;71-76 ##label SEI REFERENCE S47561 !$#authors Sigurdardottir, O.; Wiman, B. !$#journal Biochim. Biophys. Acta (1994) 1208:104-110 !$#title Identification of a PAI-1 binding site in vitronectin. !$#cross-references MUID:94368811; PMID:7522053 !$#accession S47561 !'##molecule_type protein !'##residues 20-39,'X',41-44 ##label SGU REFERENCE S62642 !$#authors Kost, C.; Benner, K.; Stockmann, A.; Linder, D.; Preissner, !1K.T. !$#journal Eur. J. Biochem. (1996) 236:682-688 !$#title Limited plasmin proteolysis of vitronectin. Characterization !1of the adhesion protein as morpho-regulatory and !1angiostatin-binding factor. !$#cross-references MUID:96195681; PMID:8612645 !$#accession S62642 !'##molecule_type protein !'##residues 20-23,'X',25;108-113 ##label KOS COMMENT Seven disulfide bonds are present. Four are predicted to be !1in the somatomedin domain. In addition to the known bond, !1two more are predicted to be in the hemopexin-like domains. COMMENT Somatomedin B was named when it was thought to have growth !1promoting activity; it is now known not to have that !1activity, and its function as a circulating peptide is still !1uncertain. GENETICS !$#gene GDB:VTN !'##cross-references GDB:132366; OMIM:193190 !$#map_position 17q11-17q11 !$#introns 22/1; 62/1; 177/1; 223/3; 276/1; 327/1; 442/1 FUNCTION !$#description vitronectin sequestered in extracellular matrix binds and !1stabilizes plasminogen activator inhibitor 1 (PAI1); !1cleavage of vitronectin by plasmin reduces the binding of !1PAI1, releasing it to inhibit plasminogen activation !$#pathway fibrinolysis CLASSIFICATION #superfamily vitronectin; hemopexin repeat homology; !1somatomedin B homology KEYWORDS cell adhesion; fibrinolysis; glycoprotein; heparin binding; !1phosphoprotein; sulfoprotein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-478 #product vitronectin #status predicted #label MAT\ !$20-71 #region plasminogen-activator-inhibitor-1 binding\ !$20-63 #product somatomedin B #status experimental #label !8ACT\ !$20-62 #domain somatomedin B homology #label SBH\ !$64-66 #region cell attachment (R-G-D) motif\ !$65-83 #region PEST sequence\ !$91-106 #region PEST sequence\ !$118-131 #region PEST sequence\ !$147-159 #region PEST sequence\ !$150-287 #domain hemopexin repeat homology #status atypical !8#label PX1\ !$288-472 #domain hemopexin repeat homology #label PX2\ !$367-398 #region heparin binding\ !$75,78 #binding_site sulfate (Tyr) (covalent) #status !8predicted\ !$86,169,242 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$293-430 #disulfide_bonds #status experimental\ !$380-381 #cleavage_site Arg-Ser (plasmin) #status !8experimental\ !$397 #binding_site phosphate (Ser) (covalent) (by !8cAMP-dependent kinase) #status experimental\ !$398-399 #cleavage_site Arg-Ala (unidentified proteinase) !8#status experimental SUMMARY #length 478 #molecular-weight 54362 #checksum 3083 SEQUENCE /// ENTRY SGMSV #type complete TITLE vitronectin precursor - mouse ALTERNATE_NAMES complement protein S CONTAINS somatomedin B ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 22-Jun-1999 ACCESSIONS S19894; JT0662; S22224; A56398 REFERENCE S19894 !$#authors Ehrlich, H.J.; Richter, B.; von der Ahe, D.; Preissner, K.T. !$#submission submitted to the EMBL Data Library, November 1991 !$#description Molecular cloning and expression in E. coli of mouse !1vitronectin. !$#accession S19894 !'##molecule_type mRNA !'##residues 1-476 ##label EHR !'##cross-references EMBL:X63003 REFERENCE JT0662 !$#authors Seiffert, D.; Poenninger, J.; Binder, B.R. !$#journal Gene (1993) 134:303-304 !$#title Organization of the gene encoding mouse vitronectin. !$#cross-references MUID:94085797; PMID:7505250 !$#accession JT0662 !'##molecule_type DNA !'##residues 1-255,'A',256-434,'S',435-476 ##label SEI !'##cross-references GB:X72091; NID:g441465; PIDN:CAA50981.1; !1PID:g441466 REFERENCE S21768 !$#authors Nakashima, N.; Miyazaki, K.; Ishikawa, M.; Yatohgo, T.; !1Ogawa, H.; Uchibori, H.; Matsumoto, I.; Seno, N.; Hayashi, !1M. !$#journal Biochim. Biophys. Acta (1992) 1120:1-10 !$#title Vitronectin diversity in evolution but uniformity in ligand !1binding and size of the core polypeptide. !$#cross-references MUID:92207982; PMID:1372829 !$#accession S22224 !'##status preliminary !'##molecule_type protein !'##residues 20,'XXXF',25-27,'X',29-34,'X',36-37,'X',39,'X',41,'X',43, !1'X' ##label NAK REFERENCE A56398 !$#authors Seiffert, D.; Keeton, M.; Eguchi, Y.; Sawdey, M.; Loskutoff, !1D.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:9402-9406 !$#title Detection of vitronectin mRNA in tissues and cells of the !1mouse. !$#cross-references MUID:92052101; PMID:1719529 !$#accession A56398 !'##molecule_type mRNA !'##residues 1-255,'A',256-382,385-414,'K',416-434,'S',435-476 ##label !1SE2 !'##cross-references GB:M77123; NID:g202371; PIDN:AAA40558.1; !1PID:g202372 GENETICS !$#introns 22/1; 62/1; 176/1; 222/3; 273/1; 324/1; 439/1 CLASSIFICATION #superfamily vitronectin; hemopexin repeat homology; !1somatomedin B homology KEYWORDS cell adhesion; glycoprotein; heparin binding; !1phosphoprotein; sulfoprotein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-476 #product vitronectin #status predicted #label MAT\ !$20-63 #product somatomedin B #status predicted #label SOM\ !$20-62 #domain somatomedin B homology #label SBH\ !$64-66 #region cell attachment (R-G-D) motif\ !$150-285 #domain hemopexin repeat homology #status atypical !8#label PX1\ !$286-471 #domain hemopexin repeat homology #label PX2\ !$365-398 #region heparin binding #status predicted\ !$75,78 #binding_site sulfate (Tyr) (covalent) #status !8predicted\ !$86,168,241 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$291-430 #disulfide_bonds #status predicted\ !$397 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 476 #molecular-weight 54690 #checksum 7058 SEQUENCE /// ENTRY A36000 #type complete TITLE sperm-binding glycoprotein ZP3 precursor - human ALTERNATE_NAMES sperm receptor ZP3; zona pellucida glycoprotein ZP3 ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A36000; A44365 REFERENCE A36000 !$#authors Chamberlin, M.E.; Dean, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:6014-6018 !$#title Human homolog of the mouse sperm receptor. !$#cross-references MUID:90349545; PMID:2385582 !$#accession A36000 !'##molecule_type mRNA; DNA !'##residues 1-424 ##label CHA !'##cross-references GB:M60504; GB:M35109; NID:g340491; PIDN:AAA61336.1; !1PID:g340492 REFERENCE A44365 !$#authors van Duin, M.; Polman, J.E.; Verkoelen, C.C.; Bunschoten, H.; !1Meyerink, J.H.; Olijve, W.; Aitken, R.J. !$#journal Genomics (1992) 14:1064-1070 !$#title Cloning and characterization of the human sperm receptor !1ligand ZP3: evidence for a second polymorphic allele with a !1different frequency in the Caucasian and Japanese !1populations. !$#cross-references MUID:93122771; PMID:1478648 !$#accession A44365 !'##status preliminary !'##molecule_type mRNA !'##residues 329-370,'S',372-424 ##label VAN !'##experimental_source ovary !'##note sequence inconsistent with the nucleotide translation !'##note sequence extracted from NCBI backbone (NCBIN:122391, !1NCBIP:122392) COMMENT This sulfated glycoprotein in the zona pellucida of the !1oocyte is a receptor for sperm binding. It has O-linked as !1well as N-linked carbohydrate. GENETICS !$#gene GDB:ZP3A !'##cross-references GDB:128007; OMIM:182889 !$#map_position 7pter-7qter CLASSIFICATION #superfamily sperm-binding glycoprotein ZP3; ZP domain !1homology KEYWORDS glycoprotein; oocyte; receptor; sulfoprotein; transmembrane !1protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-424 #product sperm-binding glycoprotein ZP3 #status !8predicted #label MAT\ !$45-301 #domain ZP domain homology #label ZPH SUMMARY #length 424 #molecular-weight 47028 #checksum 5505 SEQUENCE /// ENTRY A60503 #type complete TITLE sperm-binding glycoprotein ZP3 precursor - golden hamster ALTERNATE_NAMES sperm receptor; zona pellucida glycoprotein ZP3 ORGANISM #formal_name Mesocricetus auratus #common_name golden hamster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A60503 REFERENCE A60503 !$#authors Kinloch, R.A.; Ruiz-Seiler, B.; Wassarman, P.M. !$#journal Dev. Biol. (1990) 142:414-421 !$#title Genomic organization and polypeptide primary structure of !1zona pellucida glycoprotein hZP3, the hamster sperm !1receptor. !$#cross-references MUID:91078540; PMID:2257975 !$#accession A60503 !'##molecule_type DNA !'##residues 1-422 ##label KIN !'##cross-references GB:M63629 !'##note the authors translated the codon CAA for residue 251 as Glu, !1and AGG for residue 303 as Lys COMMENT This sulfated glycoprotein in the zona pellucida of the !1oocyte is a receptor for sperm binding. It has O-linked as !1well as N-linked carbohydrate. CLASSIFICATION #superfamily sperm-binding glycoprotein ZP3; ZP domain !1homology KEYWORDS glycoprotein; oocyte FEATURE !$45-300 #domain ZP domain homology #label ZPH SUMMARY #length 422 #molecular-weight 45801 #checksum 6117 SEQUENCE /// ENTRY A30334 #type complete TITLE sperm-binding glycoprotein ZP3 precursor - mouse ALTERNATE_NAMES sperm receptor; zona pellucida glycoprotein ZP3; ZP3 glycoprotein ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A30334; S04189; A31232; A48823 REFERENCE A30334 !$#authors Ringuette, M.J.; Chamberlin, M.E.; Baur, A.W.; Sobieski, !1D.A.; Dean, J. !$#journal Dev. Biol. (1988) 127:287-295 !$#title Molecular analysis of cDNA coding for ZP3, a sperm binding !1protein of the mouse zona pellucida. !$#cross-references MUID:88242926; PMID:3378665 !$#accession A30334 !'##molecule_type DNA; mRNA !'##residues 1-424 ##label RIN !'##cross-references GB:M20026; NID:g1663713; PIDN:AAB18629.1; !1PID:g1663714 REFERENCE S04189 !$#authors Kinloch, R.A.; Wassarman, P.M. !$#journal Nucleic Acids Res. (1989) 17:2861-2863 !$#title Nucleotide sequence of the gene encoding zona pellucida !1glycoprotein ZP3 - the mouse sperm receptor. !$#cross-references MUID:89240048; PMID:2541416 !$#accession S04189 !'##status translation not shown !'##molecule_type DNA !'##residues 1-423 ##label KIN !'##cross-references EMBL:X14376 REFERENCE A31232 !$#authors Kinloch, R.A.; Roller, R.J.; Fimiani, C.M.; Wassarman, D.A.; !1Wassarman, P.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:6409-6413 !$#title Primary structure of the mouse sperm receptor polypeptide !1determined by genomic cloning. !$#cross-references MUID:88320451; PMID:2842770 !$#accession A31232 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-152,'E',154-252,'E',254-424 ##label KI2 !'##cross-references EMBL:J03851 REFERENCE A48823 !$#authors Rosiere, T.K.; Wassarman, P.M. !$#journal Dev. Biol. (1992) 154:309-317 !$#title Identification of a region of mouse zona pellucida !1glycoprotein mZP3 that possesses sperm receptor activity. !$#cross-references MUID:93050795; PMID:1330788 !$#accession A48823 !'##status preliminary !'##molecule_type protein !'##residues 1-152,'E',154-252,'E',254-424 ##label ROS !'##experimental_source ovary !'##note sequence extracted from NCBI backbone (NCBIP:119137) COMMENT This sulfated glycoprotein in the zona pellucida of the !1oocyte is a receptor for sperm binding. It has O-linked as !1well as N-linked carbohydrate. GENETICS !$#introns 103/3; 143/2; 178/1; 239/2; 278/3; 309/2; 355/1 CLASSIFICATION #superfamily sperm-binding glycoprotein ZP3; ZP domain !1homology KEYWORDS glycoprotein; oocyte; sulfoprotein; transmembrane protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-424 #product sperm-binding glycoprotein ZP3 #status !8predicted #label MAT\ !$45-302 #domain ZP domain homology #label ZPH\ !$146,304,327,330 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$273 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 424 #molecular-weight 46303 #checksum 7302 SEQUENCE /// ENTRY S70433 #type complete TITLE zona pellucida glycoprotein C - pig ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S70433 REFERENCE S70396 !$#authors Harris, J.D.; Hibler, D.W.; Fontenot, G.K.; Hsu, K.T.; !1Yurewicz, E.C.; Sacco, A.G. !$#journal DNA Seq. (1994) 4:361-393 !$#title Cloning and characterization of zona pellucida genes and !1cDNAs from a variety of mammalian species: the ZPA, ZPB and !1ZPC gene families. !$#cross-references MUID:95143578; PMID:7841460 !$#accession S70433 !'##status preliminary !'##molecule_type mRNA !'##residues 1-421 ##label HAR CLASSIFICATION #superfamily sperm-binding glycoprotein ZP3; ZP domain !1homology FEATURE !$44-300 #domain ZP domain homology #label ZPH SUMMARY #length 421 #molecular-weight 46239 #checksum 4652 SEQUENCE /// ENTRY S70402 #type complete TITLE zona pellucida glycoprotein C - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S70402 REFERENCE S70396 !$#authors Harris, J.D.; Hibler, D.W.; Fontenot, G.K.; Hsu, K.T.; !1Yurewicz, E.C.; Sacco, A.G. !$#journal DNA Seq. (1994) 4:361-393 !$#title Cloning and characterization of zona pellucida genes and !1cDNAs from a variety of mammalian species: the ZPA, ZPB and !1ZPC gene families. !$#cross-references MUID:95143578; PMID:7841460 !$#accession S70402 !'##status preliminary !'##molecule_type mRNA !'##residues 1-421 ##label HAR !'##cross-references EMBL:U05775; NID:g458266; PIDN:AAA74385.1; !1PID:g458267 CLASSIFICATION #superfamily sperm-binding glycoprotein ZP3; ZP domain !1homology FEATURE !$44-300 #domain ZP domain homology #label ZPH SUMMARY #length 421 #molecular-weight 46545 #checksum 9197 SEQUENCE /// ENTRY S52845 #type complete TITLE ZP3 protein - goldfish ORGANISM #formal_name Carassius auratus #common_name goldfish DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S52845 REFERENCE S52845 !$#authors Chang, Y.; Wang, S.; Tsao, C.; Huang, F. !$#submission submitted to the EMBL Data Library, April 1995 !$#description Structural analysis and expression of carp ZP3 gene. !$#accession S52845 !'##status preliminary !'##molecule_type mRNA !'##residues 1-428 ##label CHA !'##cross-references EMBL:Z48974; NID:g763072; PIDN:CAA88838.1; !1PID:g763073 CLASSIFICATION #superfamily sperm-binding glycoprotein ZP3; ZP domain !1homology FEATURE !$121-375 #domain ZP domain homology #label ZPH SUMMARY #length 428 #molecular-weight 46651 #checksum 1919 SEQUENCE /// ENTRY A39783 #type complete TITLE sperm-binding glycoprotein ZP3-alpha precursor - rabbit ALTERNATE_NAMES zona pellucida glycoprotein ZP3-alpha ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A39783 REFERENCE A39783 !$#authors Schwoebel, E.; Prasad, S.; Timmons, T.M.; Cook, R.; Kimura, !1H.; Niu, E.M.; Cheung, P.; Skinner, S.; Avery, S.E.; !1Wilkins, B.; Dunbar, B.S. !$#journal J. Biol. Chem. (1991) 266:7214-7219 !$#title Isolation and characterization of a full-length cDNA !1encoding the 55-kDa rabbit zona pellucida protein. !$#cross-references MUID:91201383; PMID:1707882 !$#accession A39783 !'##status preliminary !'##molecule_type mRNA !'##residues 1-540 ##label SCH !'##cross-references GB:M58160; NID:g165815; PIDN:AAA31501.1; !1PID:g165816 CLASSIFICATION #superfamily sperm-binding glycoprotein ZP3-alpha; trefoil !1homology; ZP domain homology KEYWORDS glycoprotein; oocyte; transmembrane protein FEATURE !$147-186 #domain trefoil homology #label TRF\ !$192-460 #domain ZP domain homology #label ZPH SUMMARY #length 540 #molecular-weight 59835 #checksum 8748 SEQUENCE /// ENTRY S35712 #type complete TITLE sperm-binding glycoprotein ZP3-alpha precursor - pig ALTERNATE_NAMES zona pellucida glycoprotein ZP3-alpha ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S35712 REFERENCE S35712 !$#authors Yurewicz, E.C.; Hibler, D.; Fontenot, G.K.; Sacco, A.G.; !1Harris, J. !$#journal Biochim. Biophys. Acta (1993) 1174:211-214 !$#title Nucleotide sequence of cDNA encoding ZP3-alpha, a !1sperm-binding glycoprotein from zona pellucida of pig !1oocyte. !$#cross-references MUID:93363643; PMID:8357839 !$#accession S35712 !'##status preliminary !'##molecule_type mRNA !'##residues 1-536 ##label YUR !'##cross-references EMBL:L11000; NID:g294237; PIDN:AAA50164.1; !1PID:g294238 !'##note the authors translated the codon TTC for residue 41 as Pro CLASSIFICATION #superfamily sperm-binding glycoprotein ZP3-alpha; trefoil !1homology; ZP domain homology KEYWORDS glycoprotein; oocyte; transmembrane protein FEATURE !$144-183 #domain trefoil homology #label TRF\ !$189-456 #domain ZP domain homology #label ZPH SUMMARY #length 536 #molecular-weight 59333 #checksum 6789 SEQUENCE /// ENTRY A48833 #type complete TITLE sperm-binding glycoprotein ZP2 precursor - human ALTERNATE_NAMES 75K zona pellucida glycoprotein; zona pellucida protein 2; zona pellucida secondary sperm receptor ZP2 ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 29-Sep-1999 ACCESSIONS A48833 REFERENCE A48833 !$#authors Liang, L.F.; Dean, J. !$#journal Dev. Biol. (1993) 156:399-408 !$#title Conservation of mammalian secondary sperm receptor genes !1enables the promoter of the human gene to function in mouse !1oocytes. !$#cross-references MUID:93215931; PMID:8385033 !$#accession A48833 !'##status preliminary !'##molecule_type mRNA !'##residues 1-745 ##label LIA !'##cross-references GB:M90366; NID:g292939; PIDN:AAA61335.1; !1PID:g292940 !'##experimental_source ovary !'##note sequence extracted from NCBI backbone (NCBIN:129165, !1NCBIP:129166) GENETICS !$#gene GDB:ZP2 !'##cross-references GDB:6278878; OMIM:182888 CLASSIFICATION #superfamily sperm-binding glycoprotein ZP2; ZP domain !1homology KEYWORDS glycoprotein; oocyte; transmembrane protein FEATURE !$371-631 #domain ZP domain homology #label ZPH SUMMARY #length 745 #molecular-weight 82356 #checksum 7498 SEQUENCE /// ENTRY A34782 #type complete TITLE sperm-binding glycoprotein ZP2 precursor - mouse ALTERNATE_NAMES 75K zona pellucida glycoprotein; zona pellucida protein 2; zona pellucida secondary sperm receptor ZP2 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A34782 REFERENCE A34782 !$#authors Liang, L.F.; Chamow, S.M.; Dean, J. !$#journal Mol. Cell. Biol. (1990) 10:1507-1515 !$#title Oocyte-specific expression of mouse Zp-2: developmental !1regulation of the zona pellucida genes. !$#cross-references MUID:90205829; PMID:1690843 !$#accession A34782 !'##status preliminary !'##molecule_type mRNA !'##residues 1-713 ##label LIA !'##cross-references GB:M34148; NID:g202460; PIDN:AAA40586.1; !1PID:g202461 CLASSIFICATION #superfamily sperm-binding glycoprotein ZP2; ZP domain !1homology KEYWORDS glycoprotein; oocyte; transmembrane protein FEATURE !$364-624 #domain ZP domain homology #label ZPH SUMMARY #length 713 #molecular-weight 80209 #checksum 6452 SEQUENCE /// ENTRY A30452 #type complete TITLE uromodulin precursor - human ALTERNATE_NAMES Tamm-Horsfall urinary glycoprotein; uromucoid ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A30452; A30453 REFERENCE A30452 !$#authors Pennica, D.; Kohr, W.J.; Kuang, W.J.; Glaister, D.; !1Aggarwal, B.B.; Chen, E.Y.; Goeddel, D.V. !$#journal Science (1987) 236:83-88 !$#title Identification of human uromodulin as the Tamm-Horsfall !1urinary glycoprotein. !$#cross-references MUID:87177970; PMID:3453112 !$#accession A30452 !'##molecule_type DNA; mRNA !'##residues 1-640 ##label PEN !'##cross-references GB:M15881; NID:g340163; PIDN:AAA36798.1; !1PID:g340164 !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing REFERENCE A30453 !$#authors Hesion, C.; Decker, J.M.; Sherblom, A.P.; Kumar, S.; Yue, !1C.C.; Mattaliano, R.J.; Tizard, R.; Kawashima, E.; !1Schmeissner, U.; Heletky, S.; Chow, E.P.; Burne, C.A.; Shaw, !1A.; Muchmore, A.V. !$#journal Science (1987) 237:1479-1484 !$#title Uromodulin (Tamm-Horsfall glycoprotein): A renal ligand for !1lymphokines. !$#cross-references MUID:87319675; PMID:3498215 !$#accession A30453 !'##molecule_type mRNA !'##residues 1-640 ##label HES !'##cross-references GB:M17778 !'##note the authors translated the codon GTG for residue 381 as Asp !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing REFERENCE A30454 !$#authors Rindler, M.J.; Naik, S.S.; Li, N.; Hoops, T.C.; Peraldi, !1M.N. !$#journal J. Biol. Chem. (1990) 265:20784-20789 !$#title Uromodulin (Tamm-Horsfall Glycoprotein/Uromucoid) is a !1phosphatidylinositol-linked membrane protein. !$#cross-references MUID:91065873; PMID:2249987 !$#contents annotation; GPI-anchor COMMENT The protein is anchored to the cell membrane by a !1phosphatidylinositol linkage at its carboxyl end. There is !1no direct evidence as to the identity of the !1carboxyl-terminal amino acid in the membrane-bound form. GENETICS !$#gene GDB:UMOD !'##cross-references GDB:133729; OMIM:191845 !$#map_position 16p13.11-16p12.3 !$#introns 30/1; 289/1; 325/1; 394/3; 444/2; 526/2; 580/3; 608/1; 621/1 !$#note the first intron occurs before the initiator codon CLASSIFICATION #superfamily uromodulin; EGF homology; membrane glycoprotein !12 homology; ZP domain homology KEYWORDS duplication; glycoprotein; lipoprotein; phosphatidylinositol !1linkage; phosphoprotein; transmembrane protein; urine FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-640 #product uromodulin #status predicted #label MAT\ !$69-106 #domain EGF homology #label EGF\ !$170-639 #domain membrane glycoprotein 2 homology #label MGH\ !$334-583 #domain ZP domain homology #label ZPH\ !$625-640 #domain transmembrane #status predicted #label TRM\ !$38,76,80,275,322, !$513 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$232,396 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 640 #molecular-weight 69760 #checksum 346 SEQUENCE /// ENTRY A40212 #type complete TITLE uromodulin precursor - rat ALTERNATE_NAMES Tamm-Horsfall urinary glycoprotein; uromucoid ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A40212 REFERENCE A40212 !$#authors Fukuoka, S.; Freedman, S.D.; Yu, H.; Sukhatme, V.P.; !1Scheele, G.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:1189-1193 !$#title GP-2/THP gene family encodes self-binding !1glycosylphosphatidylinositol-anchored proteins in apical !1secretory compartments of pancreas and kidney. !$#cross-references MUID:92159014; PMID:1531535 !$#accession A40212 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-644 ##label FUK !'##cross-references GB:M63510; NID:g207620; PIDN:AAA42319.1; !1PID:g207621 !'##experimental_source kidney !'##note sequence extracted from NCBI backbone (NCBIP:82042) CLASSIFICATION #superfamily uromodulin; EGF homology; membrane glycoprotein !12 homology; ZP domain homology KEYWORDS duplication; glycoprotein; lipoprotein; membrane protein; !1phosphatidylinositol linkage; phosphoprotein; urine FEATURE !$71-107 #domain EGF homology #label EG1\ !$113-149 #domain EGF homology #label EGF\ !$173-643 #domain membrane glycoprotein 2 homology #label MGH\ !$337-586 #domain ZP domain homology #label ZPH SUMMARY #length 644 #molecular-weight 71062 #checksum 512 SEQUENCE /// ENTRY S52111 #type complete TITLE uromodulin precursor - mouse ALTERNATE_NAMES Tamm-Horsfall urinary glycoprotein; uromucoid ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S52111 REFERENCE S52111 !$#authors Prasadan, K.; Bates, J.; Badgett, A.; Dell, M.; Sukhatme, !1V.; Yu, H.; Kumar, S. !$#journal Biochim. Biophys. Acta (1995) 1260:328-332 !$#title Nucleotide sequence and peptide motifs of mouse uromodulin !1(Tamm-Horsfall protein) - the most abundant protein in !1mammalian urine. !$#cross-references MUID:95178555; PMID:7873609 !$#accession S52111 !'##status preliminary !'##molecule_type mRNA !'##residues 1-642 ##label PRA CLASSIFICATION #superfamily uromodulin; EGF homology; membrane glycoprotein !12 homology; ZP domain homology KEYWORDS duplication; glycoprotein; lipoprotein; membrane protein; !1phosphatidylinositol linkage; phosphoprotein; urine FEATURE !$69-105 #domain EGF homology #label EG1\ !$111-147 #domain EGF homology #label EG2\ !$171-641 #domain membrane glycoprotein 2 homology #label MGH\ !$335-584 #domain ZP domain homology #label ZPH SUMMARY #length 642 #molecular-weight 70754 #checksum 638 SEQUENCE /// ENTRY A38690 #type complete TITLE membrane glycoprotein 2 precursor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A38690; S11503; PN0573 REFERENCE A38690 !$#authors Hoops, T.C.; Rindler, M.J. !$#journal J. Biol. Chem. (1991) 266:4257-4263 !$#title Isolation of the cDNA encoding glycoprotein-2 (GP-2), the !1major zymogen granule membrane protein. Homology to !1uromodulin/Tamm-Horsfall protein. !$#cross-references MUID:91154223; PMID:1999417 !$#accession A38690 !'##status preliminary !'##molecule_type mRNA !'##residues 1-530 ##label HOO !'##cross-references GB:M58716; NID:g204453; PIDN:AAA41268.1; !1PID:g204454 REFERENCE S11503 !$#authors Fukuoka, S.I.; Scheele, G. !$#journal Nucleic Acids Res. (1990) 18:5900 !$#title Nucleotide sequence encoding the major glycoprotein (GP2) of !1rat pancreatic secretory (zymogen) granule membranes. !$#cross-references MUID:91016950; PMID:2216794 !$#accession S11503 !'##molecule_type DNA !'##residues 1-286,'Q',288-376,'A',378-530 ##label FUK !'##cross-references EMBL:X53935; NID:g57246; PIDN:CAA37882.1; !1PID:g57247 REFERENCE PN0573 !$#authors Withiam-Leitch, M.; Aletta, J.M.; Koshlukova, S.E.; Rupp, !1G.; Beaudoin, A.R.; Rubin, R.P. !$#journal Biochem. Biophys. Res. Commun. (1993) 194:1167-1174 !$#title Glycoprotein 2 of zymogen granule membranes shares !1immunological cross-reactivity and sequence similarity with !1phospholipase A2. !$#cross-references MUID:93356784; PMID:8352773 !$#accession PN0573 !'##molecule_type protein !'##residues 327-376,'A',378-512 ##label WIT !'##experimental_source pancreas COMMENT This protein is a major protein of rat pancreatic zymogen !1granule membranes, and plays a fundamental role in the !1secretory cycle. CLASSIFICATION #superfamily membrane glycoprotein 2; membrane glycoprotein !12 homology; ZP domain homology KEYWORDS calcium binding; glycoprotein; lipoprotein; membrane !1protein; pancreas; phospholipid binding FEATURE !$52-530 #domain membrane glycoprotein 2 homology #label MGH\ !$221-471 #domain ZP domain homology #label ZPH\ !$350,366,367,378 #binding_site phospholipid (Leu) #status predicted\ !$375,377,397,420 #binding_site calcium (Val, Val, Thr, Asp) #status !8predicted SUMMARY #length 530 #molecular-weight 58745 #checksum 3928 SEQUENCE /// ENTRY A37259 #type complete TITLE membrane glycoprotein 2 precursor - dog ALTERNATE_NAMES zymogen granule membrane associated protein ZAP75 ORGANISM #formal_name Canis lupus familiaris #common_name dog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A37259; PC2195 REFERENCE A37259 !$#authors Fukuoka, S.I.; Freedman, S.D.; Scheele, G.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:2898-2902 !$#title A single gene encodes membrane-bound and free forms of GP-2, !1the major glycoprotein in pancreatic secretory (zymogen) !1granule membranes. !$#cross-references MUID:91187898; PMID:2011597 !$#accession A37259 !'##status preliminary !'##molecule_type mRNA !'##residues 1-509 ##label FUK !'##cross-references GB:M64083; GB:M37032; NID:g164102; PIDN:AAA30904.1; !1PID:g164103 REFERENCE PC2195 !$#authors Fukuoka, S. !$#journal Biosci. Biotechnol. Biochem. (1994) 58:1282-1285 !$#title Analysis of ZAPs, zymogen granule membrane associated !1proteins, in the regulated exocytosis of the pancreas. !$#cross-references MUID:94362286; PMID:7765250 !$#accession PC2195 !'##molecule_type protein !'##residues 22-32 ##label FU2 !'##experimental_source pancreas !'##note This sequence is identical to that of glycophosphatidylinositol !1(GPI)-anchored protein GP2 COMMENT This protein localizes in the zymogen granule membrane and !1has important functions at each stage of the exocytotic !1pathways. CLASSIFICATION #superfamily membrane glycoprotein 2; membrane glycoprotein !12 homology; ZP domain homology KEYWORDS calcium binding; glycoprotein; lipoprotein; membrane !1protein; pancreas; phospholipid binding FEATURE !$34-509 #domain membrane glycoprotein 2 homology #label MGH\ !$200-450 #domain ZP domain homology #label ZPH SUMMARY #length 509 #molecular-weight 56772 #checksum 6538 SEQUENCE /// ENTRY JC1350 #type complete TITLE transforming growth factor beta receptor type III precursor - human ALTERNATE_NAMES betaglycan ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Dec-1999 ACCESSIONS JC1350 REFERENCE JC1350 !$#authors Moren, A.; Ichijo, H.; Miyazono, K. !$#journal Biochem. Biophys. Res. Commun. (1992) 189:356-362 !$#title Molecular cloning and characterization of the human and !1porcine transforming growth factor-beta type III receptors. !$#cross-references MUID:93080582; PMID:1333192 !$#accession JC1350 !'##molecule_type mRNA !'##residues 1-849 ##label MOR !'##cross-references GB:L07594; NID:g818001; PIDN:AAA67061.1; !1PID:g339556 GENETICS !$#gene GDB:TGFBR3 !'##cross-references GDB:136737; OMIM:600742 !$#map_position 1p33-1p32 CLASSIFICATION #superfamily transforming growth factor beta receptor type !1III; ZP domain homology KEYWORDS chondroitin sulfate proteoglycan; glycoprotein; receptor; !1transmembrane protein FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-849 #product transforming growth factor beta-3 receptor !8#status predicted #label MAT\ !$453-722 #domain ZP domain homology #label ZPH\ !$782-806 #domain transmembrane #status predicted #label TMM\ !$532,543 #binding_site chondroitin sulfate (Ser) (covalent) !8#status predicted SUMMARY #length 849 #molecular-weight 93385 #checksum 9179 SEQUENCE /// ENTRY JC1351 #type complete TITLE transforming growth factor beta receptor type III precursor - pig ALTERNATE_NAMES betaglycan ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Dec-1999 ACCESSIONS JC1351 REFERENCE JC1350 !$#authors Moren, A.; Ichijo, H.; Miyazono, K. !$#journal Biochem. Biophys. Res. Commun. (1992) 189:356-362 !$#title Molecular cloning and characterization of the human and !1porcine transforming growth factor-beta type III receptors. !$#cross-references MUID:93080582; PMID:1333192 !$#accession JC1351 !'##molecule_type mRNA !'##residues 1-848 ##label MOR !'##cross-references GB:L07595; NID:g164690; PIDN:AAA31126.1; !1PID:g164691 CLASSIFICATION #superfamily transforming growth factor beta receptor type !1III; ZP domain homology KEYWORDS chondroitin sulfate proteoglycan; glycoprotein; receptor; !1transmembrane protein FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-848 #product transforming growth factor beta-3 receptor !8#status predicted #label MAT\ !$454-723 #domain ZP domain homology #label ZPH\ !$781-805 #domain transmembrane #status predicted #label TMM\ !$533,544 #binding_site chondroitin sulfate (Ser) (covalent) !8#status predicted SUMMARY #length 848 #molecular-weight 93004 #checksum 6624 SEQUENCE /// ENTRY A41220 #type complete TITLE transforming growth factor beta receptor type III precursor - rat ALTERNATE_NAMES betaglycan ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Dec-1999 ACCESSIONS A41220; A41219 REFERENCE A41220 !$#authors Wang, X.F.; Lin, H.Y.; Ng-Eaton, E.; Downward, J.; Lodish, !1H.F.; Weinberg, R.A. !$#journal Cell (1991) 67:797-805 !$#title Expression cloning and characterization of the TGF-beta type !1III receptor. !$#cross-references MUID:92035000; PMID:1657407 !$#accession A41220 !'##status preliminary !'##molecule_type mRNA !'##residues 1-853 ##label WAN !'##cross-references GB:M80784; NID:g207287; PIDN:AAA42236.1; !1PID:g207288 REFERENCE A41219 !$#authors Lopez-Casillas, F.; Cheifetz, S.; Doody, J.; Andres, J.L.; !1Lane, W.S.; Massague, J. !$#journal Cell (1991) 67:785-795 !$#title Structure and expression of the membrane proteoglycan !1betaglycan, a component of the TGF-beta receptor system. !$#cross-references MUID:92034999; PMID:1657406 !$#accession A41219 !'##status preliminary !'##molecule_type mRNA !'##residues 1-163,'L',165-853 ##label LOP !'##cross-references GB:M77809; NID:g203137; PIDN:AAA40813.1; !1PID:g203138 CLASSIFICATION #superfamily transforming growth factor beta receptor type !1III; ZP domain homology KEYWORDS chondroitin sulfate proteoglycan; glycoprotein; receptor; !1transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-853 #product transforming growth factor beta-3 receptor !8#status predicted #label MAT\ !$456-724 #domain ZP domain homology #label ZPH\ !$787-811 #domain transmembrane #status predicted #label TMM\ !$535,546 #binding_site chondroitin sulfate (Ser) (covalent) !8#status predicted SUMMARY #length 853 #molecular-weight 94088 #checksum 4139 SEQUENCE /// ENTRY FRHUL #type complete TITLE ferritin light chain - human ORGANISM #formal_name Homo sapiens #common_name man DATE 13-Jun-1983 #sequence_revision 03-May-1996 #text_change 03-Mar-2000 ACCESSIONS B23920; B24844; A94043; A91317; A91308; I37137; S68943; !1A03266 REFERENCE A92494 !$#authors Boyd, D.; Vecoli, C.; Belcher, D.M.; Jain, S.K.; Drysdale, !1J.W. !$#journal J. Biol. Chem. (1985) 260:11755-11761 !$#title Structural and functional relationships of human ferritin H !1and L chains deduced from cDNA clones. !$#cross-references MUID:86008223; PMID:3840162 !$#accession B23920 !'##molecule_type mRNA !'##residues 1-175 ##label BOY !'##cross-references GB:M11147; NID:g182513; PIDN:AAA52439.1; !1PID:g182514 REFERENCE A93087 !$#authors Chou, C.C.; Gatti, R.A.; Fuller, M.L.; Concannon, P.; Wong, !1A.; Chada, S.; Davis, R.C.; Salser, W.A. !$#journal Mol. Cell. Biol. (1986) 6:566-573 !$#title Structure and expression of ferritin genes in a human !1promyelocytic cell line that differentiates in vitro. !$#cross-references MUID:87064341; PMID:3023856 !$#accession B24844 !'##molecule_type mRNA !'##residues 33-175 ##label CHO !'##cross-references GB:M12938; NID:g182515; PIDN:AAA52440.1; !1PID:g182516 REFERENCE A94043 !$#authors Dorner, M.H.; Salfeld, J.; Will, H.; Leibold, E.A.; Vass, !1J.K.; Munro, H.N. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:3139-3143 !$#title Structure of human ferritin light subunit messenger RNA: !1comparison with heavy subunit message and functional !1implications. !$#cross-references MUID:85216457; PMID:3858810 !$#accession A94043 !'##molecule_type mRNA !'##residues 1-101,'T',103-175 ##label DOR !'##cross-references GB:M10119; NID:g182517; PIDN:AAA35831.1; !1PID:g182518 !'##experimental_source monocyte-like leukemia cell line U937 REFERENCE A91317 !$#authors Addison, J.M.; Fitton, J.E.; Lewis, W.G.; May, K.; Harrison, !1P.M. !$#journal FEBS Lett. (1983) 164:139-144 !$#title The amino acid sequence of human liver apoferritin. !$#cross-references MUID:84085077; PMID:6653779 !$#accession A91317 !'##molecule_type protein !'##residues 2-36;41-53,'Q',55-86,'Q',88-174,'ND' ##label ADD !'##experimental_source liver !'##note some peptides were positioned by homology REFERENCE A91308 !$#authors Wustefeld, C.; Crichton, R.R. !$#journal FEBS Lett. (1982) 150:43-48 !$#title The amino acid sequence of human spleen apoferritin. !$#accession A91308 !'##molecule_type protein !'##residues 2-18,'Y',20-25,'Y',27-39,'BY',42-152,'RK',155-175 ##label !1WUS !'##experimental_source spleen !'##note the order of residues 2-7, 40-41, and 153-154 was not !1determined. Some peptides were positioned by homology REFERENCE I37137 !$#authors Santoro, C.; Marone, M.; Ferrone, M.; Costanzo, F.; Colombo, !1M.; Minganti, C.; Cortese, R.; Silengo, L. !$#journal Nucleic Acids Res. (1986) 14:2863-2876 !$#title Cloning of the gene coding for human L apoferritin. !$#cross-references MUID:86176772; PMID:3754330 !$#accession I37137 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-83 ##label RES !'##cross-references EMBL:X03742; NID:g28518; PIDN:CAA27382.1; !1PID:g28519 REFERENCE S68911 !$#authors Vladimirov, S.N.; Ivanov, A.V.; Karpova, G.G.; Musolyamov, !1A.K.; Egorov, T.A.; Thiede, B.; Wittmann-Liebold, B.; Otto, !1A. !$#journal Eur. J. Biochem. (1996) 239:144-149 !$#title Characterization of the human small-ribosomal-subunit !1proteins by N-terminal and internal sequencing, and mass !1spectrometry. !$#cross-references MUID:96305378; PMID:8706699 !$#accession S68943 !'##molecule_type protein !'##residues 84-89,'E',91;145-153,'A',155 ##label VLA !'##note ferritin light chain 1 !'##note 90-Gly was also found COMMENT Ferritin stores iron after its oxidation to the ferric form. !1It is present in virtually all cells and, at low !1concentrations, in plasma. GENETICS !$#gene GDB:FTL !'##cross-references GDB:119234; OMIM:134790 !$#map_position 19q13.3-19q13.4 !$#introns 34/3 !$#note the list of introns may not be complete COMPLEX the functional molecule, composed of 24 chains, is roughly !1spherical with a central cavity in which polymeric ferric !1iron core is deposited; there are two types of ferritin !1subunits, heavy (H) chain (see PIR:FEHUH) and light (L) !1chain. The predominant chain can be light or heavy, !1depending on the species and tissue type. CLASSIFICATION #superfamily ferritin KEYWORDS acetylated amino end; iron; metalloprotein; multimer; !1storage protein FEATURE !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental\ !$54,57,58,61,64 #binding_site iron (Glu) #status predicted SUMMARY #length 175 #molecular-weight 20019 #checksum 1205 SEQUENCE /// ENTRY FRHOL #type complete TITLE ferritin light chain - horse ORGANISM #formal_name Equus caballus #common_name domestic horse DATE 01-Sep-1981 #sequence_revision 08-May-1998 #text_change 16-Jun-2000 ACCESSIONS S36118; A03267 REFERENCE S36118 !$#authors Takeda, S.; Ohta, M.; Ebina, S.; Nagayama, K. !$#journal Biochim. Biophys. Acta (1993) 1174:218-220 !$#title Cloning, expression and characterization of horse L-ferritin !1in Escherichia coli. !$#cross-references MUID:93363645; PMID:8357841 !$#accession S36118 !'##molecule_type mRNA !'##residues 1-175 ##label TAK !'##cross-references GB:D14523; NID:g406208; PIDN:BAA03396.1; !1PID:g406209 !'##experimental_source liver REFERENCE A91294 !$#authors Heusterspreute, M.; Crichton, R.R. !$#journal FEBS Lett. (1981) 129:322-327 !$#title Amino acid sequence of horse spleen apoferritin. !$#cross-references MUID:82027739; PMID:7026284 !$#accession A03267 !'##molecule_type protein !'##residues 2-93,'L',95-175 ##label HEU !'##experimental_source spleen REFERENCE A93239 !$#authors Clegg, G.A.; Stansfield, R.F.D.; Bourne, P.E.; Harrison, !1P.M. !$#journal Nature (1980) 288:298-300 !$#title Helix packing and subunit conformation in horse spleen !1apoferritin. !$#cross-references MUID:81052459; PMID:7432529 !$#contents annotation; X-ray crystallography, 2.8 angstroms COMMENT Ferritin is an intracellular molecule that stores iron in a !1soluble, nontoxic, readily available form. The functional !1molecule, which is composed of 24 chains, is roughly !1spherical and contains a central cavity in which the !1polymeric ferric iron core is deposited. COMMENT There are two types of ferritin subunits: L (light) chain !1and H (heavy) chain. The major chain can be light or heavy, !1depending on the species and tissue type. COMMENT In horse spleen the light chain is the major chain. CLASSIFICATION #superfamily ferritin KEYWORDS acetylated amino end; iron; iron storage; liver; !1metalloprotein; multimer; spleen FEATURE !$2-175 #product ferritin light chain #status experimental !8#label MAT\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental\ !$54,57,58,61,64 #binding_site iron (Glu) #status predicted SUMMARY #length 175 #molecular-weight 19961 #checksum 4247 SEQUENCE /// ENTRY FRRTL #type complete TITLE ferritin light chain - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 28-Aug-1985 #sequence_revision 01-Dec-1995 #text_change 22-Jun-1999 ACCESSIONS A29575; A03268 REFERENCE A29575 !$#authors Leibold, E.A.; Munro, H.N. !$#journal J. Biol. Chem. (1987) 262:7335-7341 !$#title Characterization and evolution of the expressed rat ferritin !1light subunit gene and its pseudogene family. Conservation !1of sequences within noncoding regions of ferritin genes. !$#cross-references MUID:87222340; PMID:3584116 !$#accession A29575 !'##molecule_type DNA !'##residues 1-183 ##label LEI !'##cross-references GB:J02741; NID:g204132; PIDN:AAA41155.1; !1PID:g204133 REFERENCE A92474 !$#authors Leibold, E.A.; Aziz, N.; Brown, A.J.P.; Munro, H.N. !$#journal J. Biol. Chem. (1984) 259:4327-4334 !$#title Conservation in rat liver of light and heavy subunit !1sequences of mammalian ferritin. Presence of unique !1octopeptide in the light subunit. !$#cross-references MUID:84162134; PMID:6546756 !$#accession A03268 !'##molecule_type mRNA !'##residues 2-97,'K',99-120,'QA',123-154,'W',156-183 ##label LE2 !'##cross-references GB:K01930; NID:g204130; PIDN:AAA41154.1; !1PID:g204131 !'##note initiator Met not shown COMMENT This ferritin mRNA was isolated from liver parenchymal !1cells. COMMENT The rat light chain has an octopeptide insertion after !1residue 158 compared with other light chains. COMMENT Ferritin is an intracellular molecule that stores iron in a !1soluble, nontoxic, readily available form. The functional !1molecule, which is composed of 24 chains, is roughly !1spherical and contains a central cavity in which the !1polymeric ferric iron core is deposited. COMMENT There are two types of ferritin subunits: L (light) chain !1and H (heavy) chain. The major chain can be light or heavy, !1depending on the species and tissue type. COMMENT In rat liver the light chain is the major chain. CLASSIFICATION #superfamily ferritin KEYWORDS iron storage; liver; multimer SUMMARY #length 183 #molecular-weight 20805 #checksum 7976 SEQUENCE /// ENTRY FRFGL #type complete TITLE ferritin, tadpole - bullfrog ORGANISM #formal_name Rana catesbeiana #common_name bullfrog DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 22-Jun-1999 ACCESSIONS A25627 REFERENCE A25627 !$#authors Didsbury, J.R.; Theil, E.C.; Kaufman, R.E.; Dickey, L.F. !$#journal J. Biol. Chem. (1986) 261:949-955 !$#title Multiple red cell ferritin mRNAs, which code for an abundant !1protein in the embryonic cell type, analyzed by cDNA !1sequence and by primer extension of the 5'-untranslated !1regions. !$#cross-references MUID:86085940; PMID:3484480 !$#accession A25627 !'##molecule_type mRNA !'##residues 1-176 ##label DID !'##cross-references GB:M12120; NID:g213691; PIDN:AAA49532.1; !1PID:g213692 !'##experimental_source reticulocytes COMMENT The sequence of this ferritin is more similar to mammalian H !1chains than to L chains; however, the mass of the protein !1coincides more with that of the mammalian L chains. CLASSIFICATION #superfamily ferritin KEYWORDS erythrocyte; iron storage SUMMARY #length 176 #molecular-weight 20534 #checksum 5737 SEQUENCE /// ENTRY FRXL #type complete TITLE ferritin heavy chain - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 30-Sep-1991 #sequence_revision 03-Nov-1995 #text_change 17-Mar-2000 ACCESSIONS A37959; S12463; S09499; A40408 REFERENCE A37959 !$#authors Holland, L.J.; Wall, A.A.; Bhattacharya, A. !$#journal Biochemistry (1991) 30:1965-1972 !$#title Xenopus liver ferritin H subunit: cDNA sequence and mRNA !1production in the liver following estrogen treatment. !$#cross-references MUID:91129281; PMID:1993207 !$#accession A37959 !'##molecule_type mRNA !'##residues 1-176 ##label HOL !'##cross-references GB:M55010; NID:g214135; PIDN:AAA49708.1; !1PID:g214136 !'##experimental_source liver REFERENCE S12463 !$#authors Schoenberg, D. !$#submission submitted to the EMBL Data Library, January 1990 !$#accession S12463 !'##molecule_type mRNA !'##residues 1-5,'L',7-14,'I',16-156,'A',159-176 ##label SCH !'##cross-references EMBL:X51395; NID:g64690; PIDN:CAA35760.1; !1PID:g64691 REFERENCE S09499 !$#authors Moskaitis, J.E.; Pastori, R.L.; Schoenberg, D.R. !$#journal Nucleic Acids Res. (1990) 18:2184 !$#title Sequence of Xenopus laevis ferritin mRNA. !$#cross-references MUID:90245677; PMID:2336402 !$#accession S09499 !'##molecule_type mRNA !'##residues 1-5,'L',7-14,'I',16-64,70-86,'KFLKY',87-156,'A',159-176 !1##label MOS !'##cross-references EMBL:X51395 !'##note the sequence shown in the alignment is inconsistent with the !1nucleotide sequence and its translation, but consistent with !1the nucleotide sequence in reference S12463 REFERENCE A40408 !$#authors Muller, J.P.; Vedel, M.; Monnot, M.J.; Touzet, N.; Wegnez, !1M. !$#journal DNA Cell Biol. (1991) 10:571-579 !$#title Molecular cloning and expression of ferritin mRNA in heavy !1metal-poisoned Xenopus laevis cells. !$#cross-references MUID:92029619; PMID:1718317 !$#accession A40408 !'##molecule_type mRNA !'##residues 1-9,'H',11-22,'M',24-90,'G',92-96,'T',98-123,'AH',126-143, !1'Q',145-176 ##label MUL !'##cross-references EMBL:X64727 !'##experimental_source cadmium-poisoned XL2 embryonic cell line COMPLEX The functional molecule is composed of 24 chains, is roughly !1spherical and contains a central cavity in which the !1polymeric ferric iron core is deposited. FUNCTION !$#description intracellular protein that stores and transports iron in a !1soluble, nontoxic, readily available form CLASSIFICATION #superfamily ferritin KEYWORDS iron; iron binding; iron storage; iron transport; !1metalloprotein; multimer FEATURE !$24,58,59,61,62,104 #binding_site iron (Glu, Glu, Glu, Glu, His, Glu) !8#status predicted\ !$81 #binding_site iron (Asp) (shared with tetrameric !8partners) #status predicted\ !$83 #binding_site iron (Lys) (shared with tetrameric !8partners) #status predicted SUMMARY #length 176 #molecular-weight 20563 #checksum 7896 SEQUENCE /// ENTRY FRHUH #type complete TITLE ferritin heavy chain - human ALTERNATE_NAMES apoferritin H; ferritin heavy polypeptide 1 ORGANISM #formal_name Homo sapiens #common_name man DATE 28-Aug-1985 #sequence_revision 31-Dec-1993 #text_change 03-Mar-2000 ACCESSIONS A23517; A25045; JN0571; A23920; A24844; A03269; A05250; !1PN0562 REFERENCE A23517 !$#authors Costanzo, F.; Colombo, M.; Staempfli, S.; Santoro, C.; !1Marone, M.; Frank, R.; Delius, H.; Cortese, R. !$#journal Nucleic Acids Res. (1986) 14:721-736 !$#title Structure of gene and pseudogenes of human apoferritin H. !$#cross-references MUID:86120367; PMID:3003694 !$#accession A23517 !'##molecule_type DNA !'##residues 1-183 ##label COS !'##cross-references GB:X03487; NID:g31340; PIDN:CAA27205.1; !1PID:g762940; GB:X03488 REFERENCE A25045 !$#authors Hentze, M.W.; Keim, S.; Papadopoulos, P.; O'Brien, S.; Modi, !1W.; Drysdale, J.; Leonard, W.J.; Harford, J.B.; Klausner, !1R.D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:7226-7230 !$#title Cloning, characterization, expression, and chromosomal !1localization of a human ferritin heavy-chain gene. !$#cross-references MUID:87016920; PMID:3020541 !$#accession A25045 !'##molecule_type DNA !'##residues 1-183 ##label HEN !'##cross-references GB:M14211; GB:M14212; NID:g182509; PIDN:AAA52438.1; !1PID:g182511; GB:M18522 REFERENCE JN0571 !$#authors Dhar, M.; Chauthaiwale, V.; Joshi, J.G. !$#journal Gene (1993) 126:275-278 !$#title Sequence of a cDNA encoding the ferritin H-chain from an !111-week-old human fetal brain. !$#cross-references MUID:93246257; PMID:7916709 !$#accession JN0571 !'##molecule_type mRNA !'##residues 1-183 ##label DHA !'##cross-references GB:M97164; NID:g306743; PIDN:AAA35832.1; !1PID:g306744 REFERENCE A92494 !$#authors Boyd, D.; Vecoli, C.; Belcher, D.M.; Jain, S.K.; Drysdale, !1J.W. !$#journal J. Biol. Chem. (1985) 260:11755-11761 !$#title Structural and functional relationships of human ferritin H !1and L chains deduced from cDNA clones. !$#cross-references MUID:86008223; PMID:3840162 !$#accession A23920 !'##molecule_type mRNA !'##residues 1-183 ##label BOY !'##cross-references GB:M11146; NID:g182504; PIDN:AAA52437.1; !1PID:g182505 REFERENCE A93087 !$#authors Chou, C.C.; Gatti, R.A.; Fuller, M.L.; Concannon, P.; Wong, !1A.; Chada, S.; Davis, R.C.; Salser, W.A. !$#journal Mol. Cell. Biol. (1986) 6:566-573 !$#title Structure and expression of ferritin genes in a human !1promyelocytic cell line that differentiates in vitro. !$#cross-references MUID:87064341; PMID:3023856 !$#accession A24844 !'##molecule_type mRNA !'##residues 1-183 ##label CHO !'##cross-references GB:M12937; NID:g182506; PIDN:AAA35830.1; !1PID:g182507 !'##note the authors translated the codon CAG for residue 113 as Glu REFERENCE A03269 !$#authors Costanzo, F.; Santoro, C.; Colantuoni, V.; Bensi, G.; !1Raugei, G.; Romano, V.; Cortese, R. !$#journal EMBO J. (1984) 3:23-27 !$#title Cloning and sequencing of a full length cDNA coding for a !1human apoferritin H chain: evidence for a multigene family. !$#cross-references MUID:84158535; PMID:6323167 !$#accession A03269 !'##molecule_type mRNA !'##residues 1-175,'WETVIMKAKPRANFP' ##label CO2 !'##cross-references GB:X00318; NID:g28434; PIDN:CAA25086.1; PID:g28435 !'##note this sequence has been revised in reference A23517 REFERENCE PN0562 !$#authors Luzzago, A.; Felici, F.; Tramontano, A.; Pessi, A.; Cortese, !1R. !$#journal Gene (1993) 128:51-57 !$#title Mimicking of discontinuous epitopes by phage-displayed !1peptides, I. Epitope mapping of human H ferritin using a !1phage library of constrained peptides. !$#cross-references MUID:93285469; PMID:7685301 !$#contents annotation; artificial epitopes REFERENCE A57130 !$#authors Lawson, D.M.; Artymiuk, P.J.; Yewdall, S.J.; Smith, J.M.A.; !1Livingstone, J.C.; Treffry, A.; Luzzago, A.; Levi, S.; !1Arosio, P.; Cesarini, G.; Thomas, C.D.; Shaw, W.V.; !1Harrison, P.M. !$#journal Nature (1991) 349:541-544 !$#title Solving the structure of human H ferritin by genetically !1engineering intermolecular crystal contacts. !$#cross-references MUID:91125486; PMID:1992356 !$#contents annotation; X-ray crystallography, 2.4 angstroms, residues !16-86,'Q',88-177 COMMENT There are several distinct binding sites for iron. Two sites !1each consist of two aspartic acid and two lysine residues !1from four different chains. Another interior site within !1each chain may bind several iron atoms and possess !1feroxidase activity. GENETICS !$#gene GDB:FTH1; FTHL6 !'##cross-references GDB:120617; OMIM:134770 !$#map_position 11q12-11q13 !$#introns 38/3; 87/3; 129/3 COMPLEX the functional molecule, composed of 24 chains, is roughly !1spherical with a central cavity in which polymeric ferric !1iron core is deposited; there are two types of ferritin !1subunits, heavy (H) chain and light (L) chain (see !1PIR:FEHUL). The predominant chain can be light or heavy, !1depending on the species and tissue type. FUNCTION !$#description intracellular protein that stores and transports iron in a !1soluble, nontoxic, readily available form !$#note tissues containing high levels of iron and involved in !1long-term storage tend to be rich in light chains, whereas !1heavy chain-rich ferritins may be more involved in iron !1metabolism CLASSIFICATION #superfamily ferritin KEYWORDS iron; iron binding; iron storage; iron transport; !1metalloprotein; multimer FEATURE !$28,62,63,65,66,108 #binding_site iron (Glu, Glu, Glu, Glu, His, Glu) !8#status predicted\ !$85 #binding_site iron (Asp) (shared with tetrameric !8partners) #status experimental\ !$87 #binding_site iron (Lys) (shared with tetrameric !8partners) #status experimental SUMMARY #length 183 #molecular-weight 21225 #checksum 327 SEQUENCE /// ENTRY B45628 #type complete TITLE ferritin heavy chain 1 - fluke (Schistosoma mansoni) ORGANISM #formal_name Schistosoma mansoni DATE 22-Apr-1993 #sequence_revision 02-Jun-1994 #text_change 03-Mar-2000 ACCESSIONS B45628 REFERENCE A45628 !$#authors Dietzel, J.; Hirzmann, J.; Preis, D.; Symmons, P.; Kunz, W. !$#journal Mol. Biochem. Parasitol. (1992) 50:245-254 !$#title Ferritins of Schistosoma mansoni: sequence comparison and !1expression in female and male worms. !$#cross-references MUID:92158004; PMID:1741011 !$#accession B45628 !'##molecule_type mRNA !'##residues 1-173 ##label DIE !'##cross-references GB:M64538; NID:g160985; PIDN:AAA29880.1; !1PID:g160986 !'##note sequence extracted from NCBI backbone (NCBIN:82751, !1NCBIP:82752) CLASSIFICATION #superfamily ferritin KEYWORDS iron; iron storage; metalloprotein FEATURE !$23,57,58,60,61,103 #binding_site iron (Glu, Glu, Glu, Gln, His, Glu) !8#status predicted SUMMARY #length 173 #molecular-weight 20173 #checksum 6578 SEQUENCE /// ENTRY A45628 #type complete TITLE ferritin heavy chain 2 - fluke (Schistosoma mansoni) ORGANISM #formal_name Schistosoma mansoni DATE 22-Apr-1993 #sequence_revision 02-Jun-1994 #text_change 03-Mar-2000 ACCESSIONS A45628 REFERENCE A45628 !$#authors Dietzel, J.; Hirzmann, J.; Preis, D.; Symmons, P.; Kunz, W. !$#journal Mol. Biochem. Parasitol. (1992) 50:245-254 !$#title Ferritins of Schistosoma mansoni: sequence comparison and !1expression in female and male worms. !$#cross-references MUID:92158004; PMID:1741011 !$#accession A45628 !'##molecule_type mRNA !'##residues 1-172 ##label DIE !'##cross-references GB:M64539; NID:g160987; PIDN:AAA29881.1; !1PID:g160988 !'##note sequence extracted from NCBI backbone (NCBIN:82753, !1NCBIP:82754) CLASSIFICATION #superfamily ferritin KEYWORDS iron; iron storage; metalloprotein FEATURE !$25,59,60,62,63,105 #binding_site iron (Glu, Glu, Glu, Glu, His, Glu) !8#status predicted SUMMARY #length 172 #molecular-weight 19688 #checksum 2871 SEQUENCE /// ENTRY FRFBH #type complete TITLE ferritin heavy chain precursor - kidney bean ORGANISM #formal_name Phaseolus vulgaris #common_name kidney bean DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 03-Mar-2000 ACCESSIONS S17426; S14868 REFERENCE S17426 !$#authors Spence, M.J.; Henzl, M.T.; Lammers, P.J. !$#journal Plant Mol. Biol. (1991) 17:499-504 !$#title The structure of a Phaseolus vulgaris cDNA encoding the iron !1storage protein ferritin. !$#cross-references MUID:91355941; PMID:1884000 !$#accession S17426 !'##molecule_type mRNA !'##residues 1-254 ##label SPE !'##cross-references EMBL:X58274; NID:g21026; PIDN:CAA41213.1; !1PID:g21027 REFERENCE S14868 !$#authors Spence, M.J.; Sengupta-Gopalan, C.; Henzl, M.T.; Lammers, !1P.J. !$#submission submitted to the EMBL Data Library, March 1991 !$#description A Phaseolus vulgaris cDNA encoding an iron storage protein !1with sequence similarity to vertebrate ferritins. !$#accession S14868 !'##molecule_type mRNA !'##residues 1-69,'X',71-125,'X',127-254 ##label SP2 !'##cross-references EMBL:X58274; NID:g21026; PIDN:CAA41213.1; !1PID:g21027 GENETICS !$#gene pfe CLASSIFICATION #superfamily ferritin KEYWORDS chloroplast; iron; iron storage; metalloprotein FEATURE !$1-48 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$49-254 #product ferritin heavy chain #status predicted !8#label MAT\ !$99,133,134,136,137, !$183 #binding_site iron (Glu, Glu, Glu, Glu, His, Glu) !8#status predicted SUMMARY #length 254 #molecular-weight 28304 #checksum 2208 SEQUENCE /// ENTRY FREC #type complete TITLE bacterioferritin - Escherichia coli (strain K-12) ALTERNATE_NAMES cytochrome b1 ORGANISM #formal_name Escherichia coli DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 01-Mar-2002 ACCESSIONS JV0032; A31297; C65127 REFERENCE JV0032 !$#authors Andrews, S.C.; Harrison, P.M.; Guest, J.R. !$#journal J. Bacteriol. (1989) 171:3940-3947 !$#title Cloning, sequencing, and mapping of the bacterioferritin !1gene (bfr) of Escherichia coli K-12. !$#cross-references MUID:89291745; PMID:2661540 !$#accession JV0032 !'##molecule_type DNA !'##residues 1-158 ##label AN1 !'##cross-references GB:M27176; NID:g145406; PIDN:AAC13987.1; !1PID:g145409 !'##experimental_source strain K12 REFERENCE A31297 !$#authors Andrews, S.C.; Smith, J.M.A.; Guest, J.R.; Harrison, P.M. !$#journal Biochem. Biophys. Res. Commun. (1989) 158:489-496 !$#title Amino acid sequence of the bacterioferritin (cytochrome b-1) !1of Escherichia coli-K12. !$#cross-references MUID:89134252; PMID:2644932 !$#accession A31297 !'##molecule_type protein !'##residues 1-12,'X',14-38,'X',40-47,'X',49-52,'M',54-56,'X',58-70,'X', !172,'X',74-75 ##label AN2 !'##experimental_source strain K12 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65127 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-158 ##label BLAT !'##cross-references GB:AE000409; GB:U00096; NID:g1789718; !1PIDN:AAC76361.1; PID:g1789733; UWGP:b3336 !'##experimental_source strain K-12, substrain MG1655 COMMENT The active enzyme comprises twenty-four identical chains and !112 heme moities; there is predicted to be a bundle of four !1helices each having about 30 amino acids, with adjacent !1helices lying antiparallel. This feature is also the most !1prominent in the structures of mammalian ferritins. GENETICS !$#gene bfr !$#map_position 73 min CLASSIFICATION #superfamily bacterioferritin KEYWORDS heme; iron storage SUMMARY #length 158 #molecular-weight 18495 #checksum 1759 SEQUENCE /// ENTRY GYRTI #type complete TITLE cysteine-rich intestinal protein - rat ALTERNATE_NAMES CRIP ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 13-Aug-1986 #sequence_revision 13-Aug-1986 #text_change 22-Jun-1999 ACCESSIONS A03270; A56412 REFERENCE A03270 !$#authors Birkenmeier, E.H.; Gordon, J.I. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:2516-2520 !$#title Developmental regulation of a gene that encodes a !1cysteine-rich intestinal protein and maps near the murine !1immunoglobulin heavy chain locus. !$#cross-references MUID:86205983; PMID:3085096 !$#accession A03270 !'##molecule_type mRNA !'##residues 1-77 ##label BIR !'##cross-references GB:M13018; NID:g192725; PIDN:AAA37458.1; !1PID:g309189 !'##experimental_source strain Sprague-Dawley REFERENCE A56412 !$#authors Hempe, J.M.; Cousins, R.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:9671-9674 !$#title Cysteine-rich intestinal protein binds zinc during !1transmucosal zinc transport. !$#cross-references MUID:92052153; PMID:1946385 !$#accession A56412 !'##status preliminary !'##molecule_type protein !'##residues 4-56 ##label HEM COMMENT The authors report two short internal duplications, residues !13-27 with 30-54 and residues 25-47 with 53-75. COMMENT The authors report that the sequence of residues 28-72 is !1similar to the iron-binding region of ferredoxins. COMMENT The concentration in intestinal tissues of the mRNA encoding !1this protein undergoes an abrupt increase during the !1animal's transition from suckling to weaning. COMMENT Homologous genes for this protein are present in human, !1bird, fish, and sea squirt genomes. CLASSIFICATION #superfamily cysteine-rich intestinal protein; LIM !1metal-binding repeat homology KEYWORDS duplication; intestine; zinc FEATURE !$4-55 #domain LIM metal-binding repeat homology #label LIM SUMMARY #length 77 #molecular-weight 8550 #checksum 9610 SEQUENCE /// ENTRY GYHU #type complete TITLE granulin precursor [validated] - human ALTERNATE_NAMES epithelin CONTAINS granulin A; granulin B; granulin C; granulin D; granulin E; granulin F; granulin G; paragranulin ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1992 #sequence_revision 03-May-1996 #text_change 08-Dec-2000 ACCESSIONS JC1284; A38128; A38118; A36698; B36698; C36698; D36698; !1A56873 REFERENCE JC1284 !$#authors Bhandari, V.; Bateman, A. !$#journal Biochem. Biophys. Res. Commun. (1992) 188:57-63 !$#title Structure and chromosomal location of the human granulin !1gene. !$#cross-references MUID:93038704; PMID:1417868 !$#accession JC1284 !'##molecule_type DNA !'##residues 1-593 ##label BHA REFERENCE A38128 !$#authors Plowman, G.D.; Green, J.M.; Neubauer, M.G.; Buckley, S.D.; !1McDonald, V.L.; Todaro, G.J.; Shoyab, M. !$#journal J. Biol. Chem. (1992) 267:13073-13078 !$#title The epithelin precursor encodes two proteins with opposing !1activities on epithelial cell growth. !$#cross-references MUID:92317004; PMID:1618805 !$#accession A38128 !'##status preliminary !'##molecule_type mRNA !'##residues 1-593 ##label PLO !'##cross-references GB:X62320; NID:g31192; PIDN:CAA44196.1; PID:g31193 REFERENCE A38118 !$#authors Bhandari, V.; Palfree, R.G.E.; Bateman, A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:1715-1719 !$#title Isolation and sequence of the granulin precursor cDNA from !1human bone marrow reveals tandem cysteine-rich granulin !1domains. !$#cross-references MUID:92179253; PMID:1542665 !$#accession A38118 !'##molecule_type mRNA !'##residues 1-406,'R',408-433,'G',435-453,'G',455-459,'Q',461-546,'A', !1548-566,'R',568-593 ##label BH2 !'##cross-references GB:M75161; NID:g183612; PIDN:AAA58617.1; !1PID:g183613 !'##note this sequence has been revised in reference JC1284 REFERENCE A36698 !$#authors Bateman, A.; Belcourt, D.; Bennett, H.; Lazure, C.; Solomon, !1S. !$#journal Biochem. Biophys. Res. Commun. (1990) 173:1161-1168 !$#title Granulins, a novel class of peptide from leukocytes. !$#cross-references MUID:91097544; PMID:2268320 !$#accession A36698 !'##molecule_type protein !'##residues 281-336 ##label BAT !'##note this protein was purified and characterized as granulin A !$#accession B36698 !'##molecule_type protein !'##residues 206-218,'H',220-233 ##label BA2 !'##note this protein was purified and characterized as granulin B !$#accession C36698 !'##molecule_type protein !'##residues 364-367,'X',369-385,'H',387-396 ##label BA3 !'##note this protein was purified and characterized as granulin C !$#accession D36698 !'##molecule_type protein !'##residues 442-446,'XDTSS',456-458,'DG' ##label BA4 REFERENCE A56873 !$#authors Kardana, A.; Bagshawe, K.D.; Coles, B.; Read, D.; Taylor, M. !$#journal Br. J. Cancer (1993) 67:686-692 !$#title Characterisation of UGP and its relationship with beta-core !1fragment. !$#cross-references MUID:93229246; PMID:8471426 !$#accession A56873 !'##molecule_type protein !'##residues 281-283,'X',285-289,'S',291-295 ##label KAR !'##experimental_source urine !'##note sequence extracted from NCBI backbone (NCBIP:129524) GENETICS !$#gene GDB:GRN !'##cross-references GDB:136006; OMIM:138945 !$#map_position 17pter-17qter !$#introns 46/3; 88/3; 117/1; 154/3; 200/1; 236/3; 279/1; 311/3; 393/3; !1471/3; 548/3 CLASSIFICATION #superfamily granulin KEYWORDS glycoprotein; tandem repeat FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-593 #product granulin #status predicted #label MAT\ !$18-593 #product progranulin #status predicted #label PRO\ !$18-44 #product paragranulin #status experimental #label !8PGR\ !$58-113 #product granulin G #status predicted #label GRG\ !$123-179 #product granulin F #status predicted #label GRF\ !$206-261 #product granulin B #status experimental #label GRB\ !$281-336 #product granulin A #status experimental #label GRA\ !$364-417 #product granulin C #status experimental #label GRC\ !$442-496 #product granulin D #status predicted #label GRD\ !$518-573 #product granulin E #status predicted #label GRE\ !$368 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 593 #molecular-weight 63544 #checksum 9486 SEQUENCE /// ENTRY S23075 #type complete TITLE protein PMP-D1 - migratory locust ALTERNATE_NAMES pars intercerebralis major peptide D1 ORGANISM #formal_name Locusta migratoria #common_name migratory locust DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S23075 REFERENCE S23074 !$#authors Nakakura, N.; Hietter, H.; van Dorsselaer, A.; Luu, B. !$#journal Eur. J. Biochem. (1992) 204:147-153 !$#title Isolation and structural determination of three peptides !1from the insect Locusta migratoria. Identification of a !1deoxyhexose-linked peptide. !$#cross-references MUID:92155197; PMID:1740125 !$#accession S23075 !'##molecule_type protein !'##residues 1-54 ##label NAK !'##experimental_source brain CLASSIFICATION #superfamily migratory locust protein PMP-D1 KEYWORDS brain; disulfide bond; hemolymph SUMMARY #length 54 #molecular-weight 5788 #checksum 154 SEQUENCE /// ENTRY SMHU2 #type complete TITLE metallothionein 2 [validated] - human ALTERNATE_NAMES metallothionein II ORGANISM #formal_name Homo sapiens #common_name man DATE 31-May-1979 #sequence_revision 29-Jul-1981 #text_change 15-Sep-2000 ACCESSIONS A03271; A93425; I52344; S69276; A91444 REFERENCE A93291 !$#authors Karin, M.; Richards, R.I. !$#journal Nature (1982) 299:797-802 !$#title Human metallothionein genes - primary structure of the !1metallothionein-II gene and a related processed gene. !$#cross-references MUID:83036944; PMID:7133118 !$#accession A03271 !'##molecule_type DNA !'##residues 1-61 ##label KA1 !'##cross-references GB:J00271; NID:g467308; PIDN:AAA59583.1; !1PID:g386863 REFERENCE A93425 !$#authors Karin, M.; Richards, R.I. !$#journal Nucleic Acids Res. (1982) 10:3165-3173 !$#title Human metallothionein genes: molecular cloning and sequence !1analysis of the mRNA. !$#cross-references MUID:82247198; PMID:6896577 !$#accession A93425 !'##molecule_type mRNA !'##residues 1-61 ##label KA2 !'##cross-references GB:V00594; NID:g37120; PIDN:CAA23841.1; PID:g37121 REFERENCE I52344 !$#authors Yamazaki, S.; Nakanishi, M.; Hamamoto, T.; Hirata, H.; !1Ebihara, A.; Tokue, A.; Kagawa, Y. !$#journal Biochem. Int. (1992) 28:451-460 !$#title Expression of human metallothionein-II fusion protein in !1Escherichia coli. !$#cross-references MUID:93129264; PMID:1339282 !$#accession I52344 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-61 ##label YAM !'##cross-references GB:S52379; NID:g263506; PIDN:AAB24908.1; !1PID:g263507 REFERENCE S69276 !$#authors Lambert, E.; Kille, P.; Swaminathan, R. !$#journal FEBS Lett. (1996) 389:210-212 !$#title Cloning and sequencing a novel metallothionein I isoform !1expressed in human reticulocytes. !$#cross-references MUID:96338109; PMID:8766831 !$#accession S69276 !'##molecule_type mRNA !'##residues 1-61 ##label LAM REFERENCE A91444 !$#authors Kissling, M.M.; Kagi, J.H.R. !$#journal FEBS Lett. (1977) 82:247-250 !$#title Primary structure of human hepatic metallothionein. !$#cross-references MUID:78024269; PMID:913597 !$#accession A91444 !'##molecule_type protein !'##residues 1-57,'CS',60-61 ##label KIS REFERENCE A50495 !$#authors Braun, W.; Messerle, B.A.; Schaeffer, A.; Vasak, M.; Kaegi, !1J.H.R.; Wuthrich, K. !$#submission submitted to the Brookhaven Protein Data Bank, May 1990 !$#cross-references PDB:2MHU !$#contents annotation; conformation by (1)H-NMR, residues 1-30 REFERENCE A50280 !$#authors Braun, W.; Messerle, B.A.; Schaeffer, A.; Vasak, M.; Kaegi, !1J.H.R.; Wuthrich, K. !$#submission submitted to the Brookhaven Protein Data Bank, May 1990 !$#cross-references PDB:1MHU !$#contents annotation; conformation by (1)H-NMR, residues 31-61 REFERENCE A58799 !$#authors Messerle, B.A.; Schaeffer, A.; Vasak, M.; Kaegi, J.H.R.; !1Wuethrich, K. !$#journal J. Mol. Biol. (1990) 214:765-779 !$#title Three-dimensional structure of human [(113)Cd-7] !1metallothionein-2 in solution determined by nuclear magnetic !1resonance spectroscopy. !$#cross-references MUID:90355190; PMID:2388267 !$#contents annotation; conformation by (1)H-NMR COMMENT Metallothioneins have a high content of cysteine residues !1that bind various heavy metals; they lack leucine and !1aromatic amino acids. These proteins are transcriptionally !1regulated by both heavy metals and glucocorticoids and may !1be involved in heavy metal detoxification and homeostasis. GENETICS !$#gene GDB:MT2A; MT2 !'##cross-references GDB:120199; OMIM:156360 !$#map_position 16q13-16q13 !$#introns 10/1; 32/1 CLASSIFICATION #superfamily metallothionein KEYWORDS acetylated amino end; chelation; metal binding; !1metal-thiolate cluster FEATURE !$1-29 #domain beta #label NH2\ !$30-61 #domain alpha #label ALP\ !$1 #modified_site acetylated amino end (Met) #status !8experimental\ !$5,7,13,15,19,21,24, !$26,29 #binding_site transition metal ions (Cys) #status !8experimental\ !$33,34,36,37,41,44, !$48,50,57,59,60 #binding_site transition metal ions (Cys) #status !8experimental SUMMARY #length 61 #molecular-weight 6042 #checksum 8 SEQUENCE /// ENTRY SMMK2 #type complete TITLE metallothionein 2 - green monkey ALTERNATE_NAMES metallothionein II; MT-II ORGANISM #formal_name Cercopithecus aethiops #common_name green monkey, grivet DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 28-May-1999 ACCESSIONS A03272 REFERENCE A91501 !$#authors Schmidt, C.J.; Hamer, D.H. !$#journal Gene (1983) 24:137-146 !$#title Cloning and sequence analysis of two monkey metallothionein !1cDNAs. !$#cross-references MUID:84029892; PMID:6414888 !$#accession A03272 !'##molecule_type mRNA !'##residues 1-61 ##label SCH !'##cross-references GB:V01532; GB:K00485; NID:g38121; PIDN:CAA24771.1; !1PID:g38122 !'##experimental_source cadmium-resistant line of kidney BS-C-1 cells COMMENT The vertebrate metallothioneins contain two metal-binding !1domains. Clusters of cysteines within each domain chelate !1the metal ions. CLASSIFICATION #superfamily metallothionein KEYWORDS chelation; metal binding; metal-thiolate cluster FEATURE !$1-29 #domain beta #label NH2\ !$30-61 #domain alpha #label ALP\ !$5,7,13,15,19,21,24, !$26,29 #binding_site transition metal ions (Cys) #status !8predicted\ !$33,34,36,37,41,44, !$48,50,57,59,60 #binding_site transition metal ions (Cys) #status !8predicted SUMMARY #length 61 #molecular-weight 6097 #checksum 171 SEQUENCE /// ENTRY SMHU1E #type complete TITLE metallothionein 1E - human ALTERNATE_NAMES MT-1E ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1987 #sequence_revision 09-Sep-1994 #text_change 22-Jun-1999 ACCESSIONS A22634; S77696 REFERENCE A92538 !$#authors Schmidt, C.J.; Jubier, M.F.; Hamer, D.H. !$#journal J. Biol. Chem. (1985) 260:7731-7737 !$#title Structure and expression of two human metallothionein-I !1isoform genes and a related pseudogene. !$#cross-references MUID:85207825; PMID:2581970 !$#accession A22634 !'##molecule_type DNA !'##residues 1-61 ##label SCH !'##cross-references GB:M10942; NID:g187538; PIDN:AAA59587.1; !1PID:g386865 REFERENCE S41203 !$#authors Pauwels, M.; van Weyenbergh, J.; Soumillion, A.; Proost, P.; !1de Ley, M. !$#journal Eur. J. Biochem. (1994) 220:105-110 !$#title Induction by zinc of specific metallothionein isoforms in !1human monocytes. !$#cross-references MUID:94164148; PMID:8119276 !$#accession S77696 !'##molecule_type mRNA !'##residues 1-31 ##label PAU !'##cross-references EMBL:S68949; NID:g545716; PIDN:AAB30082.1; !1PID:g545717 !'##note N-terminal sequencing was done after deblocking the acylated !1N-terminal methionine residue by acid cleavage GENETICS !$#gene GDB:MT1E; MT1 !'##cross-references GDB:125569; OMIM:156351 !$#map_position 16q13-16q13 !$#introns 10/1; 32/1 CLASSIFICATION #superfamily metallothionein KEYWORDS acetylated amino end; chelation; metal binding; !1metal-thiolate cluster FEATURE !$1-29 #domain beta #label NH2\ !$30-61 #domain alpha #label ALP\ !$1 #modified_site acetylated amino end (Met) #status !8predicted\ !$5,7,13,15,19,21,24, !$26,29 #binding_site transition metal ions (Cys) #status !8predicted\ !$33,34,36,37,41,44, !$48,50,57,59,60 #binding_site transition metal ions (Cys) #status !8predicted SUMMARY #length 61 #molecular-weight 6014 #checksum 904 SEQUENCE /// ENTRY SMHU1A #type complete TITLE metallothionein 1A - human ORGANISM #formal_name Homo sapiens #common_name man DATE 24-Jun-1987 #sequence_revision 09-Sep-1994 #text_change 22-Jun-1999 ACCESSIONS A24502 REFERENCE A24502 !$#authors Richards, R.I.; Heguy, A.; Karin, M. !$#journal Cell (1984) 37:263-272 !$#title Structural and functional analysis of the human !1metallothionein-IA gene: differential induction by metal !1ions and glucocorticoids. !$#cross-references MUID:84205649; PMID:6327055 !$#accession A24502 !'##molecule_type DNA !'##residues 1-61 ##label RIC !'##cross-references GB:K01383; NID:g187536; PIDN:AAA59586.1; !1PID:g386864 GENETICS !$#gene GDB:MT1A; MT1 !'##cross-references GDB:125559; OMIM:156350 !$#map_position 16q13-16q13 !$#introns 10/1; 32/1 CLASSIFICATION #superfamily metallothionein KEYWORDS acetylated amino end; chelation; metal binding; !1metal-thiolate cluster FEATURE !$1-29 #domain beta #label NH2\ !$30-61 #domain alpha #label ALP\ !$1 #modified_site acetylated amino end (Met) #status !8predicted\ !$5,7,13,15,19,21,24, !$26,29 #binding_site transition metal ions (Cys) #status !8predicted\ !$33,34,36,37,41,44, !$48,50,57,59,60 #binding_site transition metal ions (Cys) #status !8predicted SUMMARY #length 61 #molecular-weight 6133 #checksum 538 SEQUENCE /// ENTRY SMHU1B #type complete TITLE metallothionein 1B - human ORGANISM #formal_name Homo sapiens #common_name man DATE 25-Oct-1987 #sequence_revision 09-Sep-1994 #text_change 22-Jun-1999 ACCESSIONS A25244 REFERENCE A25244 !$#authors Heguy, A.; West, A.; Richards, R.I.; Karin, M. !$#journal Mol. Cell. Biol. (1986) 6:2149-2157 !$#title Structure and tissue-specific expression of the human !1metallothionein IB gene. !$#cross-references MUID:87064506; PMID:3785191 !$#accession A25244 !'##molecule_type DNA !'##residues 1-61 ##label HEG !'##cross-references GB:M13484; GB:M13485; NID:g188709; PIDN:AAA36331.1; !1PID:g386962 GENETICS !$#gene GDB:MT1B; MT1 !'##cross-references GDB:125564; OMIM:156349 !$#map_position 16q13-16q13 !$#introns 10/1; 32/1 CLASSIFICATION #superfamily metallothionein KEYWORDS acetylated amino end; chelation; metal binding; !1metal-thiolate cluster FEATURE !$1-29 #domain beta #label NH2\ !$30-61 #domain alpha #label ALP\ !$1 #modified_site acetylated amino end (Met) #status !8predicted\ !$5,7,13,15,19,21,24, !$26,29 #binding_site transition metal ions (Cys) #status !8predicted\ !$33,34,36,37,41,44, !$48,50,57,59,60 #binding_site transition metal ions (Cys) #status !8predicted SUMMARY #length 61 #molecular-weight 6115 #checksum 1231 SEQUENCE /// ENTRY SMMK1 #type complete TITLE metallothionein 1 - green monkey ORGANISM #formal_name Cercopithecus aethiops #common_name green monkey, grivet DATE 15-Nov-1984 #sequence_revision 15-Nov-1984 #text_change 28-May-1999 ACCESSIONS A03273 REFERENCE A91501 !$#authors Schmidt, C.J.; Hamer, D.H. !$#journal Gene (1983) 24:137-146 !$#title Cloning and sequence analysis of two monkey metallothionein !1cDNAs. !$#cross-references MUID:84029892; PMID:6414888 !$#accession A03273 !'##molecule_type mRNA !'##residues 1-61 ##label SCH !'##cross-references GB:V01533; GB:K00484; NID:g38123; PIDN:CAA24772.1; !1PID:g38124 !'##experimental_source kidney BS-C-1 cells CLASSIFICATION #superfamily metallothionein KEYWORDS chelation; metal binding; metal-thiolate cluster FEATURE !$1-29 #domain beta #label NH2\ !$30-61 #domain alpha #label ALP\ !$5,7,13,15,19,21,24, !$26,29 #binding_site transition metal ions (Cys) #status !8predicted\ !$33,34,36,37,41,44, !$48,50,57,59,60 #binding_site transition metal ions (Cys) #status !8predicted SUMMARY #length 61 #molecular-weight 6141 #checksum 1013 SEQUENCE /// ENTRY SMHU1F #type complete TITLE metallothionein 1F - human ALTERNATE_NAMES MT-IF ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 22-Jun-1999 ACCESSIONS B22634; A24905; A61560 REFERENCE A92538 !$#authors Schmidt, C.J.; Jubier, M.F.; Hamer, D.H. !$#journal J. Biol. Chem. (1985) 260:7731-7737 !$#title Structure and expression of two human metallothionein-I !1isoform genes and a related pseudogene. !$#cross-references MUID:85207825; PMID:2581970 !$#accession B22634 !'##molecule_type DNA !'##residues 1-61 ##label SCH !'##cross-references GB:M10943; NID:g187540; PIDN:AAA59588.1; !1PID:g386866 REFERENCE A24905 !$#authors Varshney, U.; Jahroudi, N.; Foster, R.; Gedamu, L. !$#journal Mol. Cell. Biol. (1986) 6:26-37 !$#title Structure, organization, and regulation of human !1metallothionein I-F gene: differential and !1cell-type-specific expression in response to heavy metals !1and glucocorticoids. !$#cross-references MUID:87064295; PMID:3023827 !$#accession A24905 !'##molecule_type DNA !'##residues 1-61 ##label VAR !'##cross-references GB:M13003; NID:g187542; PIDN:AAA36213.1; !1PID:g386867 REFERENCE A61560 !$#authors Gedamu, L.; Varshney, U.; Jahroudi, N.; Foster, R.; Shworak, !1N.W. !$#journal Experientia Suppl. (1987) 52:361-372 !$#title Structure and expression of the human metallothionein genes. !$#cross-references MUID:88029905; PMID:2444457 !$#accession A61560 !'##molecule_type DNA !'##residues 1-61 ##label GED COMMENT Expression of this protein appears to be tissue-specific and !1differentially regulated by heavy metals (cadmium, zinc, and !1copper) but not by glucocorticoids. GENETICS !$#gene GDB:MT1F; MT1 !'##cross-references GDB:125571; OMIM:156352 !$#map_position 16q13-16q13 !$#introns 10/1; 32/1 CLASSIFICATION #superfamily metallothionein KEYWORDS acetylated amino end; chelation; metal binding; !1metal-thiolate cluster FEATURE !$1-29 #domain beta #label NH2\ !$30-61 #domain alpha #label ALP\ !$1 #modified_site acetylated amino end (Met) #status !8predicted\ !$5,7,13,15,19,21,24, !$26,29 #binding_site transition metal ions (Cys) #status !8predicted\ !$33,34,36,37,41,44, !$48,50,57,59,60 #binding_site transition metal ions (Cys) #status !8predicted SUMMARY #length 61 #molecular-weight 6086 #checksum 1666 SEQUENCE /// ENTRY SMRT2 #type complete TITLE metallothionein II - rat ALTERNATE_NAMES MT-II ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 18-Mar-1997 ACCESSIONS B61561; S02630; A03274; S65713 REFERENCE A61561 !$#authors Andersen, R.D.; Taplitz, S.J.; Birren, B.W.; Bristol, G.; !1Herschman, H.R. !$#journal Experientia Suppl. (1987) 52:373-384 !$#title Rat metallothionein multigene family. !$#cross-references MUID:88029906; PMID:2959527 !$#accession B61561 !'##molecule_type DNA !'##residues 1-61 ##label AND REFERENCE S02630 !$#authors Woergoetter, E.; Wagner, G.; Vasak, M.; Kaegi, J.H.R.; !1Wuethrich, K. !$#journal Eur. J. Biochem. (1987) 167:457-466 !$#title Sequence-specific (1)H-NMR assignments in rat-liver !1metallothionein-2. !$#cross-references MUID:88004467; PMID:3653102 !$#accession S02630 !'##molecule_type protein !'##residues 1-61 ##label WOE REFERENCE A92445 !$#authors Winge, D.R.; Nielson, K.B.; Zeikus, R.D.; Gray, W.R. !$#journal J. Biol. Chem. (1984) 259:11419-11425 !$#title Structural characterization of the isoforms of neonatal and !1adult rat liver metallothionein. !$#cross-references MUID:84289593; PMID:6470004 !$#accession A03274 !'##molecule_type protein !'##residues 1-61 ##label WIN !'##experimental_source neonatal and adult liver REFERENCE S65712 !$#authors Saito, S.; Hunziker, P.E. !$#journal Biochim. Biophys. Acta (1996) 1289:65-70 !$#title Differential sensitivity of metallothionein-1 and -2 in !1liver of zinc-injected rat toward proteolysis. !$#cross-references MUID:96195842; PMID:8605234 !$#accession S65713 !'##molecule_type protein !'##residues 3-61 ##label SAI COMMENT The vertebrate metallothioneins contain two metal-binding !1domains. Clusters of cysteines within each domain chelate !1the metal ions. CLASSIFICATION #superfamily metallothionein KEYWORDS blocked amino end; chelation; metal binding; metal-thiolate !1cluster FEATURE !$1-29 #domain beta #status predicted #label NH2\ !$30-61 #domain alpha #status predicted #label ALP\ !$1 #modified_site blocked amino end (Met) (probably !8acetylated) #status experimental\ !$5,7,13,15,19,21,24, !$26,29 #binding_site transition metal ions (Cys) #status !8predicted\ !$33,34,36,37,41,44, !$48,50,57,59,60 #binding_site transition metal ions (Cys) #status !8predicted SUMMARY #length 61 #molecular-weight 6145 #checksum 1150 SEQUENCE /// ENTRY SMMS2 #type complete TITLE metallothionein II - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 05-Apr-1983 #sequence_revision 05-Apr-1983 #text_change 13-Sep-1996 ACCESSIONS A03275 REFERENCE A03275 !$#authors Huang, I.Y.; Kimura, M.; Hata, A.; Tsunoo, H.; Yoshida, A. !$#journal J. Biochem. (1981) 89:1839-1845 !$#title Complete amino acid sequence of mouse liver !1metallothionein-II. !$#cross-references MUID:82030651; PMID:7287658 !$#accession A03275 !'##molecule_type protein !'##residues 1-61 ##label HUA CLASSIFICATION #superfamily metallothionein KEYWORDS acetylated amino end; metal binding FEATURE !$1 #modified_site acetylated amino end (Met) #status !8experimental\ !$5,7,13,15,19,21,24, !$26,29 #binding_site transition metal ions (Cys) #status !8predicted\ !$33,34,36,37,41,44, !$48,50,57,59,60 #binding_site transition metal ions (Cys) #status !8predicted SUMMARY #length 61 #molecular-weight 6114 #checksum 1441 SEQUENCE /// ENTRY SMHY2C #type complete TITLE metallothionein II - Chinese hamster ORGANISM #formal_name Cricetulus griseus #common_name Chinese hamster DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 16-Jun-2000 ACCESSIONS A03276; S50199 REFERENCE A93501 !$#authors Griffith, B.B.; Walters, R.A.; Enger, M.D.; Hildebrand, !1C.E.; Griffith, J.K. !$#journal Nucleic Acids Res. (1983) 11:901-910 !$#title cDNA cloning and nucleotide sequence comparison of Chinese !1hamster metallothionein I and II mRNAs. !$#cross-references MUID:83168910; PMID:6687636 !$#accession A03276 !'##molecule_type mRNA !'##residues 1-61 ##label GRI !'##cross-references GB:J00062; NID:g191139; PIDN:AAA36997.1; !1PID:g304523 REFERENCE S50198 !$#authors Yamada, K.; Kato, H.; Kanda, N.; Fujii-Kuriyama, Y.; !1Utakoji, T.; Itoh, R. !$#journal Biochim. Biophys. Acta (1994) 1219:581-591 !$#title Sequence homology of Chinese hamster metallothionein genes I !1and II to those of the mouse and rat, and their !1amplification in Cd-resistant cells. !$#cross-references MUID:95035087; PMID:7948015 !$#accession S50199 !'##status preliminary !'##molecule_type DNA !'##residues 1-61 ##label YAM !'##cross-references GB:D10552; GB:D90510; NID:g633057; PIDN:BAA01409.1; !1PID:g633058 CLASSIFICATION #superfamily metallothionein KEYWORDS metal binding FEATURE !$5,7,13,15,19,21,24, !$26,29 #binding_site transition metal ions (Cys) #status !8predicted\ !$33,34,36,37,41,44, !$48,50,57,59,60 #binding_site transition metal ions (Cys) #status !8predicted SUMMARY #length 61 #molecular-weight 6146 #checksum 1539 SEQUENCE /// ENTRY SMHO1A #type complete TITLE metallothionein 1A - horse ORGANISM #formal_name Equus caballus #common_name domestic horse DATE 31-May-1979 #sequence_revision 31-May-1979 #text_change 13-Sep-1996 ACCESSIONS A03277 REFERENCE A03277 !$#authors Kojima, Y.; Kagi, J.H.R. !$#journal Trends Biochem. Sci. (1978) 3:90-93 !$#title Metallothionein. !$#accession A03277 !'##molecule_type protein !'##residues 1-60 ##label KOJ !'##experimental_source liver and kidney !'##note both Ser and Leu occur at position 54 CLASSIFICATION #superfamily metallothionein KEYWORDS acetylated amino end; metal binding FEATURE !$1 #modified_site acetylated amino end (Met) #status !8experimental\ !$5,7,13,15,19,21,24, !$26,29 #binding_site transition metal ions (Cys) #status !8predicted\ !$33,34,36,37,41,44, !$48,50,57,59 #binding_site transition metal ions (Cys) #status !8predicted SUMMARY #length 60 #molecular-weight 5937 #checksum 594 SEQUENCE /// ENTRY SMHOB #type complete TITLE metallothionein 1B - horse ORGANISM #formal_name Equus caballus #common_name domestic horse DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 13-Sep-1996 ACCESSIONS A03278 REFERENCE A03278 !$#authors Kojima, Y.; Berger, C.; Vallee, B.L.; Kagi, J.H.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1976) 73:3413-3417 !$#title Amino-acid sequence of equine renal metallothionein-1B. !$#cross-references MUID:77036758; PMID:1068454 !$#accession A03278 !'##molecule_type protein !'##residues 1-61 ##label KOJ !'##experimental_source kidney COMMENT Metallothioneins are found in many tissues, especially !1kidney and liver, in multiple molecular forms. They can bind !1up to seven metal ions (mainly cadmium and/or zinc) through !1mercaptide linkages, in which all Cys residues participate. CLASSIFICATION #superfamily metallothionein KEYWORDS acetylated amino end; metal binding FEATURE !$1 #modified_site acetylated amino end (Met) #status !8experimental\ !$5,7,13,15,19,21,24, !$26,29 #binding_site transition metal ions (Cys) #status !8predicted\ !$33,34,36,37,41,44, !$48,50,57,58,60 #binding_site transition metal ions (Cys) #status !8predicted SUMMARY #length 61 #molecular-weight 6067 #checksum 778 SEQUENCE /// ENTRY SMBO2 #type complete TITLE metallothionein II - bovine ALTERNATE_NAMES MT-II ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 05-Jan-1996 ACCESSIONS A03279 REFERENCE A03279 !$#authors Winge, D.R.; Gray, W.R.; Zelazowski, A.; Garvey, J.S. !$#journal Arch. Biochem. Biophys. (1986) 245:254-262 !$#title Sequence and antigenicity of calf metallothionein II. !$#cross-references MUID:86129456; PMID:3947100 !$#accession A03279 !'##molecule_type protein !'##residues 1-61 ##label WIN !'##experimental_source calf liver !'##note 49-Ile was also found COMMENT The vertebrate metallothioneins contain two metal-binding !1domains. Clusters of cysteines within each domain chelate !1the metal ions. COMMENT Cysteine clusters can also chelate univalent metal ions. As !1many as 18 different metals are known to associate with this !1protein in vitro. CLASSIFICATION #superfamily metallothionein KEYWORDS acetylated amino end; chelation; metal binding; !1metal-thiolate cluster FEATURE !$1-29 #domain beta #label NH2\ !$30-61 #domain alpha #label ALP\ !$1 #modified_site acetylated amino end (Met) #status !8experimental\ !$5,7,13,15,19,21,24, !$26,29 #binding_site transition metal ions (Cys) #status !8predicted\ !$33,34,36,37,41,44, !$48,50,57,59,60 #binding_site transition metal ions (Cys) #status !8predicted SUMMARY #length 61 #molecular-weight 5951 #checksum 1110 SEQUENCE /// ENTRY SMHU1G #type complete TITLE metallothionein 1G - human ALTERNATE_NAMES MT-IG ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1989 #sequence_revision 09-Sep-1994 #text_change 22-Jun-1999 ACCESSIONS A29236; B61560; S77697 REFERENCE A29236 !$#authors Foster, R.; Jahroudi, N.; Varshney, U.; Gedamu, L. !$#journal J. Biol. Chem. (1988) 263:11528-11535 !$#title Structure and expression of the human metallothionein-IG !1gene. Differential promoter activity of two linked !1metallothionein-I genes in response to heavy metals. !$#cross-references MUID:88298811; PMID:3403543 !$#accession A29236 !'##molecule_type DNA !'##residues 1-61 ##label FOS !'##cross-references GB:J03910; NID:g188712; PIDN:AAA59873.1; !1PID:g188713 !'##note the authors translated the codon GGC for residues 40 and 47 as !1Cys REFERENCE A61560 !$#authors Gedamu, L.; Varshney, U.; Jahroudi, N.; Foster, R.; Shworak, !1N.W. !$#journal Experientia Suppl. (1987) 52:361-372 !$#title Structure and expression of the human metallothionein genes. !$#cross-references MUID:88029905; PMID:2444457 !$#accession B61560 !'##molecule_type DNA !'##residues 1-61 ##label GED REFERENCE S41203 !$#authors Pauwels, M.; van Weyenbergh, J.; Soumillion, A.; Proost, P.; !1de Ley, M. !$#journal Eur. J. Biochem. (1994) 220:105-110 !$#title Induction by zinc of specific metallothionein isoforms in !1human monocytes. !$#cross-references MUID:94164148; PMID:8119276 !$#accession S77697 !'##molecule_type mRNA !'##residues 1-31 ##label PAU !'##cross-references EMBL:S68954; NID:g545718; PIDN:AAB30083.1; !1PID:g545719 !'##note N-terminal sequencing was done after deblocking the acylated !1N-terminal methionine residue by acid cleavage GENETICS !$#gene GDB:MT1G; MT1 !'##cross-references GDB:125572; OMIM:156353 !$#map_position 16q13-16q13 !$#introns 10/1; 32/1 CLASSIFICATION #superfamily metallothionein KEYWORDS acetylated amino end; chelation; metal binding; !1metal-thiolate cluster FEATURE !$1-29 #domain beta #label NH2\ !$30-61 #domain alpha #label ALP\ !$1 #modified_site acetylated amino end (Met) #status !8predicted\ !$5,7,13,15,19,21,24, !$26,29 #binding_site transition metal ions (Cys) #status !8predicted\ !$33,34,36,37,41,44, !$48,50,57,59,60 #binding_site transition metal ions (Cys) #status !8predicted SUMMARY #length 61 #molecular-weight 6070 #checksum 465 SEQUENCE /// ENTRY SMMSI #type complete TITLE metallothionein I - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Apr-1979 #sequence_revision 24-Sep-1981 #text_change 22-Jun-1999 ACCESSIONS A93261; A93863; A90105; A92216; JC5586; PC4480; A03280 REFERENCE A93261 !$#authors Glanville, N.; Durnam, D.M.; Palmiter, R.D. !$#journal Nature (1981) 292:267-269 !$#title Structure of mouse metallothionein-I gene and its mRNA. !$#cross-references MUID:81245168; PMID:7254320 !$#accession A93261 !'##molecule_type DNA !'##residues 1-61 ##label GLA !'##cross-references GB:V00835; GB:J00605; NID:g53247; PIDN:CAA24220.1; !1PID:g53248 REFERENCE A93863 !$#authors Durnam, D.M.; Perrin, F.; Gannon, F.; Palmiter, R.D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1980) 77:6511-6515 !$#title Isolation and characterization of the mouse !1metallothionein-I gene. !$#cross-references MUID:81101080; PMID:6935664 !$#accession A93863 !'##molecule_type mRNA !'##residues 1-61 ##label DUR !'##experimental_source liver REFERENCE A90105 !$#authors Mbikay, M.; Maiti, I.B.; Thirion, J.P. !$#journal Biochem. Biophys. Res. Commun. (1981) 103:825-832 !$#title Cloning and sequencing of cDNA for mouse liver !1metallothionein-I. !$#cross-references MUID:82134842; PMID:6277322 !$#accession A90105 !'##molecule_type mRNA !'##residues 1-61 ##label MBI REFERENCE A92216 !$#authors Huang, I.Y.; Yoshida, A.; Tsunoo, H.; Nakajima, H. !$#journal J. Biol. Chem. (1977) 252:8217-8221 !$#title Mouse liver metallothioneins. Comlete amino acid sequence of !1metallothionein-I. !$#cross-references MUID:78026596; PMID:914867 !$#accession A92216 !'##molecule_type protein !'##residues 1-22,'D',24-61 ##label HUA !'##experimental_source liver REFERENCE JC5586 !$#authors Xiong, Y.; Ru, B. !$#journal J. Biochem. (1997) 121:1102-1106 !$#title Purification and characterization of recombinant mouse !1metallothionein-I from Escherichia coli. !$#cross-references MUID:98014474; PMID:9354383 !$#accession JC5586 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-61 ##label XIO !$#accession PC4480 !'##molecule_type protein !'##residues 1-4 ##label XI1 COMMENT The vertebrate metallothioneins contain two metal-binding !1domains. Clusters of cysteines within each domain chelate !1the metal ions. This protein is involved in cellular !1detoxification of heavy metal such as cadmium and mercury as !1well as in the homeostasis of essential metal ions, zinc and !1copper. It is also in mammalian UV response, serving as !1scavengers of free hydroxyl radicals or sources of zinc for !1DNA repair enzymes. GENETICS !$#introns 10/1; 32/1 CLASSIFICATION #superfamily metallothionein KEYWORDS acetylated amino end; chelation; metal binding; !1metal-thiolate cluster FEATURE !$1 #modified_site acetylated amino end (Met) #status !8experimental\ !$5,7,13,15,19,21,24, !$26,29 #binding_site transition metal ions (Cys) #status !8predicted\ !$33,34,36,37,41,44, !$48,50,57,59,60 #binding_site transition metal ions (Cys) #status !8predicted SUMMARY #length 61 #molecular-weight 6018 #checksum 1293 SEQUENCE /// ENTRY SMRT1 #type complete TITLE metallothionein I - rat ALTERNATE_NAMES MT-I ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 22-Jun-1999 ACCESSIONS A93079; A61561; A90943; A92445; I52549; A03281 REFERENCE A93079 !$#authors Andersen, R.D.; Birren, B.W.; Taplitz, S.J.; Herschman, H.R. !$#journal Mol. Cell. Biol. (1986) 6:302-314 !$#title Rat metallothionein-1 structural gene and three pseudogenes, !1one of which contains 5'-regulatory sequences. !$#cross-references MUID:87064300; PMID:3023830 !$#accession A93079 !'##molecule_type DNA !'##residues 1-61 ##label AND !'##cross-references GB:M11794; NID:g205531; PIDN:AAA41641.1; !1PID:g205533 REFERENCE A61561 !$#authors Andersen, R.D.; Taplitz, S.J.; Birren, B.W.; Bristol, G.; !1Herschman, H.R. !$#journal Experientia Suppl. (1987) 52:373-384 !$#title Rat metallothionein multigene family. !$#cross-references MUID:88029906; PMID:2959527 !$#accession A61561 !'##molecule_type DNA !'##residues 1-61 ##label AN1 REFERENCE A90943 !$#authors Andersen, R.D.; Birren, B.W.; Ganz, T.; Piletz, J.E.; !1Herschman, H.R. !$#journal DNA (1983) 2:15-22 !$#title Molecular cloning of the rat metallothionein 1 (MT-1) mRNA !1sequence. !$#cross-references MUID:83209120; PMID:6687866 !$#accession A90943 !'##molecule_type mRNA !'##residues 1-61 ##label AN2 !'##cross-references GB:J00750; GB:K01196; NID:g205381; PIDN:AAA41590.1; !1PID:g205382 !'##experimental_source liver REFERENCE A92445 !$#authors Winge, D.R.; Nielson, K.B.; Zeikus, R.D.; Gray, W.R. !$#journal J. Biol. Chem. (1984) 259:11419-11425 !$#title Structural characterization of the isoforms of neonatal and !1adult rat liver metallothionein. !$#cross-references MUID:84289593; PMID:6470004 !$#accession A92445 !'##molecule_type protein !'##residues 1-61 ##label WIN !'##experimental_source neonatal and adult liver REFERENCE I52549 !$#authors Mercer, J.F.B.; Hudson, P.J. !$#journal Biosci. Rep. (1982) 2:761-768 !$#title Cloning of metallothionein cDNA from neonatal rat liver. !$#cross-references MUID:83075694; PMID:6184083 !$#accession I52549 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 44-61 ##label RES !'##cross-references GB:M24327; NID:g205379; PIDN:AAA41589.1; !1PID:g205380 COMMENT The vertebrate metallothioneins contain two metal-binding !1domains. Clusters of cysteines within each domain chelate !1the metal ions. COMMENT It is estimated that more than 50% of the total fetal zinc !1content is in the liver and most is associated with MT. This !1coupled with an enhanced fetal/neonatal expression of MT has !1led to the postulate that this protein may serve as a major !1reservoir of metal ions during development. GENETICS !$#introns 10/1; 32/1 CLASSIFICATION #superfamily metallothionein KEYWORDS blocked amino end; chelation; metal binding; metal-thiolate !1cluster FEATURE !$1-29 #domain beta #status predicted #label NH2\ !$30-61 #domain alpha #status predicted #label ALP\ !$1 #modified_site blocked amino end (Met) (probably !8acetylated) #status experimental\ !$5,7,13,15,19,21,24, !$26,29 #binding_site transition metal ions (Cys) #status !8predicted\ !$33,34,36,37,41,44, !$48,50,57,59,60 #binding_site transition metal ions (Cys) #status !8predicted SUMMARY #length 61 #molecular-weight 6006 #checksum 2369 SEQUENCE /// ENTRY SMHY1C #type complete TITLE metallothionein I - Chinese hamster ORGANISM #formal_name Cricetulus griseus #common_name Chinese hamster DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 16-Jun-2000 ACCESSIONS A03282; S13737; S50198 REFERENCE A93501 !$#authors Griffith, B.B.; Walters, R.A.; Enger, M.D.; Hildebrand, !1C.E.; Griffith, J.K. !$#journal Nucleic Acids Res. (1983) 11:901-910 !$#title cDNA cloning and nucleotide sequence comparison of Chinese !1hamster metallothionein I and II mRNAs. !$#cross-references MUID:83168910; PMID:6687636 !$#accession A03282 !'##molecule_type mRNA !'##residues 1-61 ##label GRI !'##cross-references GB:J00061; NID:g191135; PIDN:AAA36996.1; !1PID:g304522 REFERENCE S13737 !$#authors Grady, D.L.; Robinson, D.L.; Hildebrand, C.E. !$#journal Nucleic Acids Res. (1990) 18:7149 !$#title Genomic sequence of the Chinese hamster MT I gene. !$#cross-references MUID:91088310; PMID:2263484 !$#accession S13737 !'##molecule_type DNA !'##residues 1-61 ##label GRA !'##cross-references EMBL:X55064; NID:g49468; PIDN:CAA38897.1; !1PID:g49469 REFERENCE S50198 !$#authors Yamada, K.; Kato, H.; Kanda, N.; Fujii-Kuriyama, Y.; !1Utakoji, T.; Itoh, R. !$#journal Biochim. Biophys. Acta (1994) 1219:581-591 !$#title Sequence homology of Chinese hamster metallothionein genes I !1and II to those of the mouse and rat, and their !1amplification in Cd-resistant cells. !$#cross-references MUID:95035087; PMID:7948015 !$#accession S50198 !'##molecule_type DNA !'##residues 1-61 ##label YAM !'##cross-references GB:D10551; GB:D90509; NID:g633055; PIDN:BAA01408.1; !1PID:g633056 GENETICS !$#gene MT-I !$#introns 10/1; 32/1 CLASSIFICATION #superfamily metallothionein KEYWORDS metal binding FEATURE !$5,7,13,15,19,21,24, !$26,29 #binding_site transition metal ions (Cys) #status !8predicted\ !$33,34,36,37,41,44, !$48,50,57,59,60 #binding_site transition metal ions (Cys) #status !8predicted SUMMARY #length 61 #molecular-weight 6051 #checksum 2283 SEQUENCE /// ENTRY SMKD1S #type complete TITLE metallothionein 1 - mud crab ORGANISM #formal_name Scylla serrata #common_name mud crab DATE 29-Jul-1981 #sequence_revision 29-Jul-1981 #text_change 13-Sep-1996 ACCESSIONS A03283 REFERENCE A92363 !$#authors Lerch, K.; Ammer, D.; Olafson, R.W. !$#journal J. Biol. Chem. (1982) 257:2420-2426 !$#title Crab metallothionein. Primary structures of metallothioneins !11 and 2. !$#cross-references MUID:82142340; PMID:7061431 !$#accession A03283 !'##molecule_type protein !'##residues 1-58 ##label LER !'##note the five Cys-X-Cys sequences are believed to be the principal !1metal-binding sites of this protein CLASSIFICATION #superfamily metallothionein KEYWORDS metal binding SUMMARY #length 58 #molecular-weight 6001 #checksum 1380 SEQUENCE /// ENTRY SMKD2S #type complete TITLE metallothionein 2 - mud crab ORGANISM #formal_name Scylla serrata #common_name mud crab DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 13-Sep-1996 ACCESSIONS A03284 REFERENCE A92363 !$#authors Lerch, K.; Ammer, D.; Olafson, R.W. !$#journal J. Biol. Chem. (1982) 257:2420-2426 !$#title Crab metallothionein. Primary structures of metallothioneins !11 and 2. !$#cross-references MUID:82142340; PMID:7061431 !$#accession A03284 !'##molecule_type protein !'##residues 1-57 ##label LER CLASSIFICATION #superfamily metallothionein KEYWORDS metal binding SUMMARY #length 57 #molecular-weight 6109 #checksum 2022 SEQUENCE /// ENTRY SMFF #type complete TITLE metallothionein Mtn - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES MT ORGANISM #formal_name Drosophila melanogaster DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 22-Jun-1999 ACCESSIONS A25294; A03285; A48734; A61194 REFERENCE A25294 !$#authors Maroni, G.; Otto, E.; Lastowski-Perry, D. !$#journal Genetics (1986) 112:493-504 !$#title Molecular and cytogenetic characterization of a !1metallothionein gene of Drosophila. !$#cross-references MUID:86165787; PMID:3007277 !$#accession A25294 !'##molecule_type DNA !'##residues 1-40 ##label MAR !'##cross-references GB:X03758; GB:M12964; NID:g8272; PIDN:CAA27391.1; !1PID:g8273 REFERENCE A03285 !$#authors Lastowski-Perry, D.; Otto, E.; Maroni, G. !$#journal J. Biol. Chem. (1985) 260:1527-1530 !$#title Nucleotide sequence and expression of a Drosophila !1metallothionein. !$#cross-references MUID:85105016; PMID:2578462 !$#accession A03285 !'##molecule_type mRNA !'##residues 1-40 ##label LAS !'##cross-references GB:K02314; GB:M35390; NID:g157876; PIDN:AAA28681.1; !1PID:g157877 !'##experimental_source Samarkand stock, larva !'##note this allele is designated Mtn-1 REFERENCE A48734 !$#authors Maroni, G.; Lastowski-Perry, D.; Otto, E.; Watson, D. !$#journal Environ. Health Perspect. (1986) 65:107-116 !$#title Effects of heavy metals on Drosophila larvae and a !1metallothionein cDNA. !$#cross-references MUID:86219988; PMID:3086075 !$#accession A48734 !'##molecule_type mRNA !'##residues 1-40 ##label MA2 !'##cross-references GB:K02314; NID:g157876; PIDN:AAA28681.1; !1PID:g157877 REFERENCE A61194 !$#authors Theodore, L.; Ho, A.S.; Maroni, G. !$#journal Genet. Res. (1991) 58:203-210 !$#title Recent evolutionary history of the metallothionein gene Mtn !1in Drosophila. !$#cross-references MUID:92201681; PMID:1802803 !$#accession A61194 !'##molecule_type DNA !'##residues 1-39,'K' ##label THE !'##cross-references GB:M69015; NID:g157915; PIDN:AAB41334.1; !1PID:g157916 !'##note this allele is designated Mtn-3 COMMENT This protein binds cations of several transition elements. COMMENT All cysteine residues are arranged in C-X-C groups. These !1are thought to be the metal-binding sites. GENETICS !$#gene Mtn !'##cross-references FlyBase:FBgn0002868 !$#map_position 3R 85E10-15 !$#introns 8/1 !$#note several alleles of Mtn are known; the metallothionein gene !1Mto is very distantly related CLASSIFICATION #superfamily metallothionein KEYWORDS chelation; metal binding SUMMARY #length 40 #molecular-weight 3853 #checksum 9471 SEQUENCE /// ENTRY SMFF2 #type complete TITLE metallothionein 2 - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 24-Nov-1999 ACCESSIONS S14706; A38808; A29863; S10476 REFERENCE S14706 !$#authors Silar, P.; Theodore, L.; Mokdad, R.; Erraiss, N.E.; Cadic, !1A.; Wegnez, M. !$#journal J. Mol. Biol. (1990) 215:217-224 !$#title Metallothionein Mto gene of Drosophila melanogaster: !1structure and regulation. !$#cross-references MUID:91012582; PMID:1976815 !$#accession S14706 !'##molecule_type DNA !'##residues 1-43 ##label SIL1 !'##cross-references EMBL:X52098; NID:g8274; PIDN:CAA36318.1; !1PID:g295751 !$#accession A38808 !'##molecule_type protein !'##residues 'X',3-24,'X',26-27 ##label SIL2 !'##note 15-Thr was also found REFERENCE A29863 !$#authors Mokdad, R.; Debec, A.; Wegnez, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:2658-2662 !$#title Metallothionein genes in Drosophila melanogaster constitute !1a dual system. !$#cross-references MUID:87204190; PMID:3106973 !$#accession A29863 !'##molecule_type mRNA !'##residues 1-43 ##label MOK !'##cross-references GB:M16250; NID:g157884; PIDN:AAA28683.1; !1PID:g157885 GENETICS !$#gene Mto !'##cross-references FlyBase:FBgn0002869 !$#map_position 3R 92E !$#introns 9/1 CLASSIFICATION #superfamily metallothionein KEYWORDS blocked amino end; chelation; metal binding FEATURE !$1 #modified_site blocked amino end (Met) #status !8experimental SUMMARY #length 43 #molecular-weight 4525 #checksum 9665 SEQUENCE /// ENTRY SMMR #type complete TITLE metallothionein - cultivated mushroom ORGANISM #formal_name Agaricus bisporus #common_name cultivated mushroom DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 13-Sep-1996 ACCESSIONS A03286 REFERENCE A03286 !$#authors Munger, K.; Lerch, K. !$#journal Biochemistry (1985) 24:6751-6756 !$#title Copper metallothionein from the fungus Agaricus bisporus: !1chemical and spectroscopic properties. !$#accession A03286 !'##molecule_type protein !'##residues 1-25 ##label MUN !'##experimental_source mycelium; strain A-32 COMMENT In contrast to the vertebrate metallothioneins, the fungal !1proteins bind copper exclusively. This protein binds six !1copper ions. COMMENT The absorptive, luminescent, and stereoptical properties of !1the copper MT are attributed to the metal-thiolate complex !1because they are not present in the apoprotein. CLASSIFICATION #superfamily metallothionein KEYWORDS chelation; metal binding; metal-thiolate cluster SUMMARY #length 25 #molecular-weight 2233 #checksum 3970 SEQUENCE /// ENTRY SMNC #type complete TITLE metallothionein - Neurospora crassa ORGANISM #formal_name Neurospora crassa DATE 31-May-1980 #sequence_revision 31-Mar-1993 #text_change 22-Jun-1999 ACCESSIONS A24641; A03287 REFERENCE A24641 !$#authors Muenger, K.; Germann, U.A.; Lerch, K. !$#journal EMBO J. (1985) 4:2665-2668 !$#title Isolation and structural organization of the Neurospora !1crassa copper metallothionein gene. !$#cross-references MUID:86030247; PMID:2932331 !$#accession A24641 !'##molecule_type DNA !'##residues 1-26 ##label MUE !'##cross-references GB:X03009; NID:g2986; PIDN:CAA26793.1; PID:g2987 REFERENCE A03287 !$#authors Lerch, K. !$#journal Nature (1980) 284:368-370 !$#title Copper metallothionein, a copper-binding protein from !1Neurospora crassa. !$#cross-references MUID:80143244; PMID:6444697 !$#accession A03287 !'##molecule_type protein !'##residues 2-26 ##label LER GENETICS !$#introns 18/1 CLASSIFICATION #superfamily metallothionein KEYWORDS chelation; metal binding; metal-thiolate cluster FEATURE !$4,6,12,14,18,20,23 #binding_site transition metal ions (Cys) #status !8experimental SUMMARY #length 26 #molecular-weight 2366 #checksum 6133 SEQUENCE /// ENTRY SMBH1 #type complete TITLE metallothionein - barley ORGANISM #formal_name Hordeum vulgare #common_name barley DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 22-Jun-1999 ACCESSIONS S17299; S15558 REFERENCE S17299 !$#authors Okumura, N.; Nishizawa, N.K.; Umehara, Y.; Mori, S. !$#journal Plant Mol. Biol. (1991) 17:531-533 !$#title An iron deficiency-specific cDNA from barley roots having !1two homologous cysteine-rich MT domains. !$#cross-references MUID:91355948; PMID:1832055 !$#accession S17299 !'##molecule_type mRNA !'##residues 1-74 ##label OKU !'##cross-references EMBL:X58540; NID:g19006; PIDN:CAA41432.1; !1PID:g19007 GENETICS !$#gene ids-1 CLASSIFICATION #superfamily metallothionein KEYWORDS metal binding SUMMARY #length 74 #molecular-weight 7469 #checksum 3781 SEQUENCE /// ENTRY SMMUL #type complete TITLE metallothionein-like protein - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jun-2000 ACCESSIONS S18069; S57897 REFERENCE S18069 !$#authors Takahashi, K. !$#submission submitted to the EMBL Data Library, October 1991 !$#accession S18069 !'##molecule_type mRNA !'##residues 1-81 ##label TAK !'##cross-references EMBL:X62818; NID:g16183; PIDN:CAA44630.1; !1PID:g16184 !'##experimental_source strain Columbia REFERENCE S57897 !$#authors Takahashi, K. !$#submission submitted to the EMBL Data Library, July 1992 !$#accession S57897 !'##molecule_type DNA !'##residues 1-81 ##label TAW !'##cross-references EMBL:D11394; NID:g217856; PIDN:BAA01990.1; !1PID:g217857 GENETICS !$#introns 22/2 CLASSIFICATION #superfamily metallothionein KEYWORDS metal binding SUMMARY #length 81 #molecular-weight 8136 #checksum 6595 SEQUENCE /// ENTRY SBHUP #type complete TITLE statherin precursor [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 24-Apr-1984 #sequence_revision 30-Jun-1993 #text_change 08-Dec-2000 ACCESSIONS JH0153; A27308; B27489; A03288; A32524 REFERENCE JH0153 !$#authors Sabatini, L.M.; He, Y.Z.; Azen, E.A. !$#journal Gene (1990) 89:245-251 !$#title Structure and sequence determination of the gene encoding !1human salivary statherin. !$#cross-references MUID:90323623; PMID:2373369 !$#accession JH0153 !'##molecule_type DNA !'##residues 1-62 ##label SA2 !'##cross-references GB:M31077 REFERENCE A27308 !$#authors Sabatini, L.M.; Carlock, L.R.; Johnson, G.W.; Azen, E.A. !$#journal Am. J. Hum. Genet. (1987) 41:1048-1060 !$#title cDNA cloning and chromosomal localization (4q11-13) of a !1gene for statherin, a regulator of calcium in saliva. !$#cross-references MUID:88074310; PMID:3502720 !$#accession A27308 !'##molecule_type mRNA !'##residues 1-62 ##label SAB !'##cross-references GB:M32639; NID:g338504; PIDN:AAA60593.1; !1PID:g338506 REFERENCE A27489 !$#authors Dickinson, D.P.; Ridall, A.L.; Levine, M.J. !$#journal Biochem. Biophys. Res. Commun. (1987) 149:784-790 !$#title Human submandibular gland statherin and basic histidine-rich !1peptide are encoded by highly abundant mRNA's derived from a !1common ancestral sequence. !$#cross-references MUID:88106506; PMID:3426601 !$#accession B27489 !'##molecule_type mRNA !'##residues 1-62 ##label DIC !'##cross-references GB:M18371; NID:g338610; PIDN:AAA60600.1; !1PID:g338611 REFERENCE A03288 !$#authors Schlesinger, D.H.; Hay, D.I. !$#journal J. Biol. Chem. (1977) 252:1689-1695 !$#title Complete covalent structure of statherin, a tyrosine-rich !1acidic peptide which inhibits calcium phosphate !1precipitation from human parotid saliva. !$#cross-references MUID:77118656; PMID:838735 !$#accession A03288 !'##molecule_type protein !'##residues 20-62 ##label SCH REFERENCE A92773 !$#authors Oppenheim, F.G.; Hay, D.I.; Smith, D.J.; Offner, G.D.; !1Troxler, R.F. !$#journal J. Dent. Res. (1987) 66:462-466 !$#title Molecular basis of salivary proline-rich protein and peptide !1synthesis: cell-free translations and processing of human !1and macaque statherin mRNAs and partial amino acid sequence !1of their signal peptides. !$#cross-references MUID:87309161; PMID:3476566 !$#accession A32524 !'##molecule_type protein !'##residues 1,'X',3-4,'X',6,'X',8,'X',10,'X',12-13,'XX',16 ##label OPP !'##note radiosequencing of precursor after cell-free translation COMMENT Statherin is one of the salivary proteins that stabilize !1saliva supersaturated with calcium salts by inhibiting !1calcium phosphate precipitation and that adsorb onto apatite !1surfaces (possibly being precursors of enamel pellicle). !1These inhibitors thus promote enamel stabilization and !1recalcification and prevent formation of accretions on the !1tooth surface. GENETICS !$#gene GDB:STATH !'##cross-references GDB:120391; OMIM:184470 !$#map_position 4q11-4q13 !$#introns 17/3; 24/3; 34/3 CLASSIFICATION #superfamily statherin precursor; statherin/histatin signal !1sequence homology KEYWORDS phosphoprotein; saliva FEATURE !$1-25 #domain statherin/histatin signal sequence homology !8#label SHH\ !$1-19 #domain signal sequence #status experimental #label !8SIG\ !$20-62 #product statherin #status experimental #label MAT\ !$21,22 #binding_site phosphate (Ser) (covalent) #status !8experimental SUMMARY #length 62 #molecular-weight 7304 #checksum 1846 SEQUENCE /// ENTRY SBMQPI #type complete TITLE statherin precursor - crab-eating macaque ORGANISM #formal_name Macaca fascicularis #common_name crab-eating macaque DATE 17-Dec-1982 #sequence_revision 21-Jul-1995 #text_change 21-Jan-2000 ACCESSIONS B32524; A03289 REFERENCE A92773 !$#authors Oppenheim, F.G.; Hay, D.I.; Smith, D.J.; Offner, G.D.; !1Troxler, R.F. !$#journal J. Dent. Res. (1987) 66:462-466 !$#title Molecular basis of salivary proline-rich protein and peptide !1synthesis: cell-free translations and processing of human !1and macaque statherin mRNAs and partial amino acid sequence !1of their signal peptides. !$#cross-references MUID:87309161; PMID:3476566 !$#accession B32524 !'##molecule_type protein !'##residues 1-19 ##label OP1 !'##note 6-Leu was also found REFERENCE A03289 !$#authors Oppenheim, F.G.; Offner, G.D.; Troxler, R.F. !$#journal J. Biol. Chem. (1982) 257:9271-9282 !$#title Phosphoproteins in the parotid saliva from the subhuman !1primate Macaca fascicularis. Isolation and characterization !1of a proline-rich phosphoglycoprotein and the complete !1covalent structure of a proline-rich phosphopeptide. !$#cross-references MUID:82265555; PMID:7107568 !$#accession A03289 !'##molecule_type protein !'##residues 20-61 ##label OP2 CLASSIFICATION #superfamily statherin precursor; statherin/histatin signal !1sequence homology KEYWORDS phosphoprotein; saliva FEATURE !$1-25 #domain statherin/histatin signal sequence homology !8#label SHH\ !$1-19 #domain signal sequence #status experimental #label !8SIG\ !$20-61 #product statherin #status experimental #label MAT\ !$21,22 #binding_site phosphate (Ser) (covalent) #status !8experimental SUMMARY #length 61 #molecular-weight 7452 #checksum 2032 SEQUENCE /// ENTRY A32541 #type complete TITLE histatin 1 precursor [validated] - human ALTERNATE_NAMES histidine-rich protein 1 CONTAINS histatin 2 ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 08-Dec-2000 ACCESSIONS I57425; A32541; A32987; A25661; A60664; A28164; A60742; !1A60659 REFERENCE I57425 !$#authors Sabatini, L.M.; Ota, T.; Azen, E.A. !$#journal Mol. Biol. Evol. (1993) 10:497-511 !$#title Nucleotide sequence analysis of the human salivary protein !1genes HIS1 and HIS2, and evolution of the STATH/HIS gene !1family. !$#cross-references MUID:93330039; PMID:8336540 !$#accession I57425 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-57 ##label SA1 !'##cross-references GB:L04132; NID:g184051; PIDN:AAA02745.1; !1PID:g184054 REFERENCE A90156 !$#authors Sabatini, L.M.; Azen, E.A. !$#journal Biochem. Biophys. Res. Commun. (1989) 160:495-502 !$#title Histatins, a family of salivary histidine-rich proteins, are !1encoded by at least two loci (HIS1 and HIS2). !$#cross-references MUID:89246491; PMID:2719677 !$#accession A32541 !'##molecule_type mRNA !'##residues 1-57 ##label SAB !'##cross-references GB:M26664; NID:g292143; PIDN:AAA58645.1; !1PID:g292144 REFERENCE A32987 !$#authors vanderSpek, J.C.; Wyandt, H.E.; Skare, J.C.; Milunsky, A.; !1Oppenheim, F.G.; Troxler, R.F. !$#journal Am. J. Hum. Genet. (1989) 45:381-387 !$#title Localization of the genes for histatins to human chromosome !14q13 and tissue distribution of the mRNAs. !$#cross-references MUID:89371745; PMID:2773933 !$#accession A32987 !'##molecule_type mRNA !'##residues 14-57 ##label VAN REFERENCE A25661 !$#authors Oppenheim, F.G.; Yang, Y.C.; Diamond, R.D.; Hyslop, D.; !1Offner, G.D.; Troxler, R.F. !$#journal J. Biol. Chem. (1986) 261:1177-1182 !$#title The primary structure and functional characterization of the !1neutral histidine-rich polypeptide from human parotid !1secretion. !$#cross-references MUID:86111755; PMID:3944083 !$#accession A25661 !'##molecule_type protein !'##residues 20-57 ##label OPP REFERENCE A60664 !$#authors Sugiyama, K.; Ogino, T.; Ogata, K. !$#journal Arch. Oral Biol. (1990) 35:415-419 !$#title Rapid purification and characterization of histatins !1(histidine-rich polypeptides) from human whole saliva. !$#cross-references MUID:90321151; PMID:2372245 !$#accession A60664 !'##molecule_type protein !'##residues 20-57 ##label SUG REFERENCE A94685 !$#authors Oppenheim, F.G.; Xu, T.; McMillian, F.M.; Levitz, S.M.; !1Diamond, R.D.; Offner, G.D.; Troxler, R.F. !$#journal J. Biol. Chem. (1988) 263:7472-7477 !$#title Histatins, a novel family of histidine-rich proteins in !1human parotid secretion. Isolation, characterization, !1primary structure, and fungistatic effects of Candida !1albicans. !$#cross-references MUID:88227937; PMID:3286634 !$#accession A28164 !'##molecule_type protein !'##residues 20-57 ##label OP2 REFERENCE A60742 !$#authors Troxler, R.F.; Offner, G.D.; Xu, T.; Vanderspek, J.C.; !1Oppenheim, F.G. !$#journal J. Dent. Res. (1990) 69:2-6 !$#title Structural relationship between human salivary histatins. !$#cross-references MUID:90154430; PMID:2303595 !$#accession A60742 !'##molecule_type protein !'##residues 31-57 ##label TRO REFERENCE A60659 !$#authors vanderSpek, J.C.; Offner, G.D.; Troxler, R.F.; Oppenheim, !1F.G. !$#journal Arch. Oral Biol. (1990) 35:137-143 !$#title Molecular cloning of human submandibular histatins. !$#cross-references MUID:90262442; PMID:2344289 !$#accession A60659 !'##molecule_type mRNA !'##residues 'VML',14-57 ##label VA2 GENETICS !$#gene GDB:HTN1 !'##cross-references GDB:120068; OMIM:142701 !$#map_position 4q13-4q13 !$#introns 17/3; 24/3; 34/3 CLASSIFICATION #superfamily histatin precursor; statherin/histatin signal !1sequence homology KEYWORDS phosphoprotein; saliva FEATURE !$1-25 #domain statherin/histatin signal sequence homology !8#label SHH\ !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-57 #product histatin 1 #status experimental #label MA1\ !$31-57 #product histatin 2 #status experimental #label MA2\ !$21 #binding_site phosphate (Ser) (covalent) #status !8experimental SUMMARY #length 57 #molecular-weight 6963 #checksum 6367 SEQUENCE /// ENTRY B32541 #type complete TITLE histatin 3 precursor [validated] - human ALTERNATE_NAMES histidine-rich protein 3 CONTAINS histatin 10; histatin 11; histatin 12; histatin 4; histatin 5; histatin 6; histatin 7; histatin 8; histatin 9 ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 08-Dec-2000 ACCESSIONS B32541; A27489; B60659; B60664; C60664; B28164; C28164; !1B60742; C60742; D60742; H60742; A60675; A61000; I77213; !1E60742; F60742; G60742; I60742 REFERENCE A90156 !$#authors Sabatini, L.M.; Azen, E.A. !$#journal Biochem. Biophys. Res. Commun. (1989) 160:495-502 !$#title Histatins, a family of salivary histidine-rich proteins, are !1encoded by at least two loci (HIS1 and HIS2). !$#cross-references MUID:89246491; PMID:2719677 !$#accession B32541 !'##molecule_type mRNA !'##residues 1-51 ##label SAB !'##cross-references GB:M26665; NID:g292145; PIDN:AAA58646.1; !1PID:g292146 REFERENCE A27489 !$#authors Dickinson, D.P.; Ridall, A.L.; Levine, M.J. !$#journal Biochem. Biophys. Res. Commun. (1987) 149:784-790 !$#title Human submandibular gland statherin and basic histidine-rich !1peptide are encoded by highly abundant mRNA's derived from a !1common ancestral sequence. !$#cross-references MUID:88106506; PMID:3426601 !$#accession A27489 !'##molecule_type mRNA !'##residues 1-51 ##label DIC !'##cross-references GB:M18372; NID:g179465; PIDN:AAA51830.1; !1PID:g179466 REFERENCE A60659 !$#authors vanderSpek, J.C.; Offner, G.D.; Troxler, R.F.; Oppenheim, !1F.G. !$#journal Arch. Oral Biol. (1990) 35:137-143 !$#title Molecular cloning of human submandibular histatins. !$#cross-references MUID:90262442; PMID:2344289 !$#accession B60659 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-51 ##label VAN REFERENCE A60664 !$#authors Sugiyama, K.; Ogino, T.; Ogata, K. !$#journal Arch. Oral Biol. (1990) 35:415-419 !$#title Rapid purification and characterization of histatins !1(histidine-rich polypeptides) from human whole saliva. !$#cross-references MUID:90321151; PMID:2372245 !$#accession B60664 !'##molecule_type protein !'##residues 20-43 ##label SUG !$#accession C60664 !'##molecule_type protein !'##residues 20-51 ##label SU2 REFERENCE A94685 !$#authors Oppenheim, F.G.; Xu, T.; McMillian, F.M.; Levitz, S.M.; !1Diamond, R.D.; Offner, G.D.; Troxler, R.F. !$#journal J. Biol. Chem. (1988) 263:7472-7477 !$#title Histatins, a novel family of histidine-rich proteins in !1human parotid secretion. Isolation, characterization, !1primary structure, and fungistatic effects of Candida !1albicans. !$#cross-references MUID:88227937; PMID:3286634 !$#accession B28164 !'##molecule_type protein !'##residues 20-51 ##label OPP !$#accession C28164 !'##molecule_type protein !'##residues 20-43 ##label OP2 REFERENCE A60742 !$#authors Troxler, R.F.; Offner, G.D.; Xu, T.; Vanderspek, J.C.; !1Oppenheim, F.G. !$#journal J. Dent. Res. (1990) 69:2-6 !$#title Structural relationship between human salivary histatins. !$#cross-references MUID:90154430; PMID:2303595 !$#accession B60742 !'##molecule_type protein !'##residues 31-51 ##label TRO !$#accession C60742 !'##molecule_type protein !'##residues 20-44 ##label TR2 !$#accession D60742 !'##molecule_type protein !'##residues 31-43 ##label TR3 !$#accession H60742 !'##molecule_type protein !'##residues 24-31 ##label TR7 REFERENCE A60675 !$#authors Xu, L.; Fischer, T.; Pollock, J.J. !$#journal Pept. Res. (1989) 2:373-375 !$#title Sequence determination of low molecular weight salivary !1histidine-rich polypeptides from electroblots. !$#cross-references MUID:92273931; PMID:2520776 !$#accession A60675 !'##molecule_type protein !'##residues 25-43 ##label XUA REFERENCE A61000 !$#authors Murakami, Y.; Amano, A.; Takagaki, M.; Shizukuishi, S.; !1Tsunemitsu, A.; Aimoto, S. !$#journal FEMS Microbiol. Lett. (1990) 72:275-280 !$#title Purification and characterization from human parotid !1secretion of a peptide which inhibits hemagglutination of !1Bacteroides gingivalis 381. !$#accession A61000 !'##molecule_type protein !'##residues 32-43 ##label MUR !'##note this salivary histidine-rich peptide was shown to inhibit !1hemagglutination by Bacteroides gingivalis 381 REFERENCE I57425 !$#authors Sabatini, L.M.; Ota, T.; Azen, E.A. !$#journal Mol. Biol. Evol. (1993) 10:497-511 !$#title Nucleotide sequence analysis of the human salivary protein !1genes HIS1 and HIS2, and evolution of the STATH/HIS gene !1family. !$#cross-references MUID:93330039; PMID:8336540 !$#accession I77213 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-51 ##label RES !'##cross-references GB:L05514; NID:g184056; PIDN:AAA02746.1; !1PID:g184058 GENETICS !$#gene GDB:HTN3 !'##cross-references GDB:125601; OMIM:142702 !$#map_position 4q12-4q21 !$#introns 17/3; 24/3; 34/3 CLASSIFICATION #superfamily histatin precursor; statherin/histatin signal !1sequence homology KEYWORDS saliva FEATURE !$1-25 #domain statherin/histatin signal sequence homology !8#label SHH\ !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-51 #product histatin 3 #status experimental #label MA3\ !$20-44 #product histatin 6 #status experimental #label MA6\ !$20-43 #product histatin 5 #status experimental #label MA5\ !$24-31 #product histatin 11 #status experimental #label M11\ !$24-30 #product histatin 12 #status experimental #label M12\ !$31-51 #product histatin 4 #status experimental #label MA4\ !$31-44 #product histatin 9 #status experimental #label MA9\ !$31-43 #product histatin 7 #status experimental #label MA7\ !$32-44 #product histatin 10 #status experimental #label M10\ !$32-43 #product histatin 8 #status experimental #label MA8 SUMMARY #length 51 #molecular-weight 6149 #checksum 1828 SEQUENCE /// ENTRY PIHUSC #type complete TITLE salivary proline-rich phosphoprotein precursor PRH2 [validated] - human ALTERNATE_NAMES salivary acidic proline-rich protein PRH2 CONTAINS peptide P-C (basic proline-rich peptide IB-8b); proline-rich phosphoprotein A (PRP-4); proline-rich phosphoprotein C (PRP-1); PRP-2; PRP-3 ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1981 #sequence_revision 12-Apr-1996 #text_change 08-Dec-2000 ACCESSIONS A25372; A19803; B57868; A92277; A92254; A94425; A91954; !1S02564; S02563; JP0106; G38355; S06153; A03290 REFERENCE A92492 !$#authors Maeda, N.; Kim, H.S.; Azen, E.A.; Smithies, O. !$#journal J. Biol. Chem. (1985) 260:11123-11130 !$#title Differential RNA splicing and post-translational cleavages !1in the human salivary proline-rich protein gene system. !$#cross-references MUID:85289325; PMID:2993301 !$#accession A25372 !'##molecule_type mRNA !'##residues 1-166 ##label MAE !'##cross-references GB:K03202; NID:g190481; PIDN:AAA60183.1; !1PID:g190482 REFERENCE A91757 !$#authors Schlesinger, D.H.; Hay, D.I. !$#journal Int. J. Pept. Protein Res. (1981) 17:34-41 !$#title Primary structure of the active tryptic fragments of human !1and monkey salivary anionic proline-rich proteins. !$#cross-references MUID:81191179; PMID:7228490 !$#accession A19803 !'##molecule_type protein !'##residues 17-46 ##label SCH REFERENCE A57868 !$#authors Kim, H.S.; Maeda, N. !$#journal J. Biol. Chem. (1986) 261:6712-6718 !$#title Structures of two HaeIII-type genes in the human salivary !1proline-rich protein multigene family. !$#cross-references MUID:86196106; PMID:3009472 !$#accession B57868 !'##molecule_type DNA !'##residues 1-166 ##label KIM !'##cross-references GB:M13058; NID:g190513; PIDN:AAA98808.1; !1PID:g190514 REFERENCE A92277 !$#authors Wong, R.S.C.; Bennick, A. !$#journal J. Biol. Chem. (1980) 255:5943-5948 !$#title The primary structure of a salivary calcium-binding !1proline-rich phosphoprotein (protein C), a possible !1precursor of a related salivary protein A. !$#cross-references MUID:80204368; PMID:7380845 !$#contents protein C !$#accession A92277 !'##molecule_type protein !'##residues 17-19,'N',21-166 ##label WON !'##note the amino-terminal 46 residues are involved with inhibiting !1hydroxyapatite formation, binding to hydroxyapatite, and !1calcium binding REFERENCE A92254 !$#authors Wong, R.S.C.; Hofmann, T.; Bennick, A. !$#journal J. Biol. Chem. (1979) 254:4800-4808 !$#title The complete primary structure of a proline-rich !1phosphoprotein from human saliva. !$#cross-references MUID:79173237; PMID:438215 !$#contents protein A !$#accession A92254 !'##molecule_type protein !'##residues 17-19,'N',21-122 ##label WO2 REFERENCE A94425 !$#authors Schlesinger, D.H.; Hay, D.I. !$#book Peptides: Structure and Biological Function (Proc. Sixth !1Amer. Peptide Symp.), Gross, E., and Meienhofer, J., eds., !1pp.133-136, Pierce Chemical Co., Rockford, Ill., 1979 !$#title Complete primary structure of a proline-rich phosphoprotein !1(PRP-4), a potent inhibitor of calcium phosphate !1precipitation in human parotid saliva. !$#accession A94425 !'##molecule_type protein !'##residues 17-122 ##label SC2 !'##note the authors call this protein PRP-4 REFERENCE A91954 !$#authors Isemura, S.; Saitoh, E.; Sanada, K. !$#journal J. Biochem. (1980) 87:1071-1077 !$#title The amino acid sequence of a salivary proline-rich peptide, !1P-C, and its relation to a salivary proline-rich !1phosphoprotein, protein C. !$#cross-references MUID:80227634; PMID:7390979 !$#contents peptide P-C !$#accession A91954 !'##molecule_type protein !'##residues 123-166 ##label ISE REFERENCE S02562 !$#authors Hay, D.I.; Bennick, A.; Schlesinger, D.H.; Minaguchi, K.; !1Madapallimattam, G.; Schluckebier, S.K. !$#journal Biochem. J. (1988) 255:15-21 !$#title The primary structures of six human salivary acidic !1proline-rich proteins (PRP-1, PRP-2, PRP-3, PRP-4, PIF-s and !1PIF-f). !$#cross-references MUID:89061650; PMID:3196309 !$#accession S02564 !'##molecule_type protein !'##residues 17-166 ##label HAY !$#accession S02563 !'##molecule_type protein !'##residues 47-71 ##label HA2 REFERENCE JP0106 !$#authors Schlesinger, D.H.; Hay, D.I. !$#journal Int. J. Pept. Protein Res. (1986) 27:373-379 !$#title Complete covalent structure of a proline-rich !1phosphoprotein, PRP-2, an inhibitor of calcium phosphate !1crystal growth from human parotid saliva. !$#cross-references MUID:86222916; PMID:3710693 !$#accession JP0106 !'##molecule_type protein !'##residues 17-161,'Q',163-166 ##label SC3 !'##experimental_source parotid gland REFERENCE A38355 !$#authors Kauffman, D.L.; Bennick, A.; Blum, M.; Keller, P.J. !$#journal Biochemistry (1991) 30:3351-3356 !$#title Basic proline-rich proteins from human parotid saliva: !1relationships of the covalent structures of ten proteins !1from a single individual. !$#cross-references MUID:91190884; PMID:1849422 !$#accession G38355 !'##status preliminary !'##molecule_type protein !'##residues 123-166 ##label KAU REFERENCE S06153 !$#authors Robinson, R.; Kauffman, D.L.; Waye, M.M.Y.; Blum, M.; !1Bennick, A.; Keller, P.J. !$#journal Biochem. J. (1989) 263:497-503 !$#title Primary structure and possible origin of the !1non-glycosylated basic proline-rich protein of human !1submandibular/sublingual saliva. !$#cross-references MUID:90088384; PMID:2688632 !$#accession S06153 !'##molecule_type protein !'##residues 123-166 ##label ROB COMMENT The proposed biological functions are a highly potent !1inhibitor of crystal growth of calcium phosphates, and a !1reservior of calcium ions. GENETICS !$#gene GDB:PRH2 !'##cross-references GDB:119516; OMIM:168790 !$#map_position 12p13.2-12p13.2 !$#introns 22/1; 34/1 CLASSIFICATION #superfamily proline-rich protein KEYWORDS calcium binding; phosphoprotein; pyroglutamic acid; saliva FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-166 #product protein C #status experimental #label PRC\ !$17-122 #product protein A #status experimental #label PRA\ !$17-46 #region apatitic mineral binding\ !$47-71 #product PRP-3 #status experimental #label PRP3\ !$123-166 #product peptide P-C #status experimental #label PPC\ !$17 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$24,38 #binding_site phosphate (Ser) (covalent) #status !8experimental SUMMARY #length 166 #molecular-weight 17016 #checksum 1732 SEQUENCE /// ENTRY PIHUB6 #type complete TITLE salivary proline-rich phosphoprotein precursor PRB1 (large allele) [validated] - human CONTAINS peptide IB-1; peptide P-E (peptide IB-9); peptide P-F; peptide P-H ORGANISM #formal_name Homo sapiens #common_name man DATE 04-Dec-1986 #sequence_revision 12-Apr-1996 #text_change 08-Dec-2000 ACCESSIONS B40750; C40750; A40750; C25372; S02128; S02127; A03293; !1A90502; A91974; A05261; A05262; A90464; A91966; A03291; !1A03292 REFERENCE A40750 !$#authors Azen, E.A.; Latreille, P.; Niece, R.L. !$#journal Am. J. Hum. Genet. (1993) 53:264-278 !$#title PRBI gene variants coding for length and null polymorphisms !1among human salivary Ps, PmF, PmS, and Pe proline-rich !1proteins (PRPs). !$#cross-references MUID:93304421; PMID:8317492 !$#accession B40750 !'##molecule_type DNA !'##residues 35-392 ##label AZE !'##cross-references GB:S62941 !'##experimental_source subject C.J. (large allele) !$#accession C40750 !'##molecule_type DNA !'##residues 35-127,'R',129-148,'R',150-151,153-187,'K',189-272,'S', !1274-336,'S',338-392 ##label AZ2 !'##cross-references GB:S62929 !'##experimental_source subject M.V.O. (large allele) !$#accession A40750 !'##molecule_type DNA !'##residues 35-183,245-270,'Q',272-392 ##label AZ3 !'##cross-references GB:S62928 !'##experimental_source subject C.J. (medium allele) !'##note authors translated the codon CAA for residue 272 as Arg REFERENCE A92492 !$#authors Maeda, N.; Kim, H.S.; Azen, E.A.; Smithies, O. !$#journal J. Biol. Chem. (1985) 260:11123-11130 !$#title Differential RNA splicing and post-translational cleavages !1in the human salivary proline-rich protein gene system. !$#cross-references MUID:85289325; PMID:2993301 !$#accession C25372 !'##molecule_type mRNA !'##residues 1-183,245-392 ##label MAE !'##cross-references GB:K03204; NID:g190485; PIDN:AAA60185.1; !1PID:g190486 !'##note alternatively splice forms lacking portions of the repeat !1region were also found REFERENCE S02127 !$#authors Lyons, K.M.; Stein, J.H.; Smithies, O. !$#journal Genetics (1988) 120:267-278 !$#title Length polymorphisms in human proline-rich protein genes !1generated by intragenic unequal crossing over. !$#cross-references MUID:89121440; PMID:2851479 !$#accession S02128 !'##status translation not shown !'##molecule_type DNA !'##residues 35-127,250-273,'R',275-277,'R',279-336,'S',338-392 ##label !1LYO !'##cross-references EMBL:X07517 !$#accession S02127 !'##status translation not shown !'##molecule_type DNA !'##residues 35-183,245-392 ##label LY2 !'##cross-references EMBL:X07516 REFERENCE A90502 !$#authors Kauffman, D.; Hofmann, T.; Bennick, A.; Keller, P. !$#journal Biochemistry (1986) 25:2387-2392 !$#title Basic proline-rich proteins from human parotid saliva: !1complete covalent structures of proteins IB-1 and IB-6. !$#cross-references MUID:86243355; PMID:3521730 !$#accession A03293 !'##molecule_type protein !'##residues 17-38,'AP',41-51,92-148,'R',150-152 ##label KA2 !'##note among nine basic proline-rich peptides isolated from the !1saliva, this peptide is designated IB-1 !$#accession A90502 !'##molecule_type protein !'##residues 275-336,'S',338-392 ##label KAU REFERENCE A91974 !$#authors Saitoh, E.; Isemura, S.; Sanada, K. !$#journal J. Biochem. (1983) 94:1991-1999 !$#title Further fractionation of basic proline-rich peptides from !1human parotid saliva and complete amino acid sequence of !1basic proline-rich peptide P-H. !$#cross-references MUID:84161824; PMID:6671974 !$#contents P-H !$#accession A91974 !'##molecule_type protein !'##residues 'S',338-392 ##label SAI REFERENCE A94005 !$#authors Azen, E.; Lyons, K.M.; McGonigal, T.; Barrett, N.L.; !1Clements, L.S.; Maeda, N.; Vanin, E.F.; Carlson, D.M.; !1Smithies, O. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:5561-5565 !$#cross-references MUID:84298176; PMID:6089212 !$#accession A05261 !'##molecule_type DNA !'##residues 35-39,'P',41-84,'G',86,'R',87-154,'R',218-246;300-306,'T', !1308-329,'C',331-384,'DK',387-392 ##label AZ4 !$#accession A05262 !'##molecule_type DNA !'##residues 'N',57-59,'A',61-69;334-336,'S',338-339,'R',341-392 ##label !1AZ5 REFERENCE A90464 !$#authors Kauffman, D.; Wong, R.; Bennick, A.; Keller, P. !$#journal Biochemistry (1982) 21:6558-6562 !$#title Basic proline-rich proteins from human parotid saliva: !1complete covalent structure of protein IB-9 and partial !1structure of protein IB-6, members of a polymorphic pair. !$#cross-references MUID:83101329; PMID:6924859 !$#contents IB-9 !$#accession A90464 !'##molecule_type protein !'##residues 92-127,'R',129-148,'R',150-152 ##label KA3 REFERENCE A91966 !$#authors Isemura, S.; Saitoh, E.; Sanada, K. !$#journal J. Biochem. (1982) 91:2067-2075 !$#title Fractionation and characterization of basic proline-rich !1peptides of human parotid saliva and the amino acid sequence !1of proline-rich peptide P-E. !$#cross-references MUID:83007119; PMID:7118863 !$#contents P-E !$#accession A91966 !'##molecule_type protein !'##residues 92-127,'R',129-148,'R',150-152 ##label ISE COMMENT This peptide contains 21-residue repeats, two of which have !1internal 7-residue repeats. GENETICS !$#gene GDB:PRB1 !'##cross-references GDB:119511; OMIM:180989 !$#map_position 12p13.2-12p13.2 !$#note each of the tandem repeats contains a candidate splice !1acceptor site, and several mRNAs with variable numbers of !1repeats have been found CLASSIFICATION #superfamily proline-rich protein KEYWORDS alternative splicing; duplication; parotid gland; !1phosphoprotein; pyroglutamic acid; saliva; tandem repeat FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-51,92-152 #product basic proline-rich peptide IB-1 #status !8experimental #label IB1\ !$92-152 #product basic proline-rich peptide P-E #status !8experimental #label PPE\ !$275-392 #product basic proline-rich peptide IB-6 #status !8experimental #label PIB6\ !$275-335 #product basic proline-rich peptide P-F #status !8experimental #label PPF\ !$337-392 #product basic proline-rich peptide P-H #status !8experimental #label PPH\ !$17 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$24 #binding_site phosphate (Ser) (covalent) #status !8experimental SUMMARY #length 392 #molecular-weight 38546 #checksum 8553 SEQUENCE /// ENTRY PIHUPF #type fragment TITLE salivary proline-rich glycoprotein precursor PRB2 [validated] - human (fragment) ALTERNATE_NAMES basic proline-rich peptide IB-8c precursor; proline-rich protein (clone cP7); PRP EO27 CONTAINS basic proline-rich peptide IB-4; basic proline-rich peptide P-F ORGANISM #formal_name Homo sapiens #common_name man DATE 15-Nov-1984 #sequence_revision 12-Apr-1996 #text_change 08-Dec-2000 ACCESSIONS E25372; A60827; A03294; B38355; A38355; F38355 REFERENCE A92492 !$#authors Maeda, N.; Kim, H.S.; Azen, E.A.; Smithies, O. !$#journal J. Biol. Chem. (1985) 260:11123-11130 !$#title Differential RNA splicing and post-translational cleavages !1in the human salivary proline-rich protein gene system. !$#cross-references MUID:85289325; PMID:2993301 !$#accession E25372 !'##molecule_type mRNA !'##residues 1-251 ##label MAE !'##cross-references GB:K03208; NID:g190509; PIDN:AAA60189.1; !1PID:g190510 REFERENCE A60827 !$#authors Mamula, P.W.; Morley, D.J.; Larsen, S.H.; Karn, R.C. !$#journal Biochem. Genet. (1988) 26:165-175 !$#title Expression of human salivary protein genes. !$#cross-references MUID:88240287; PMID:3288192 !$#accession A60827 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 175-251 ##label MAM REFERENCE A03294 !$#authors Saitoh, E.; Isemura, S.; Sanada, K. !$#journal J. Biochem. (1983) 93:883-888 !$#title Complete amino acid sequence of a basic proline-rich !1peptide, P-F, from human parotid saliva. !$#cross-references MUID:83265674; PMID:6874669 !$#accession A03294 !'##molecule_type protein !'##residues 134-194 ##label SAI !'##experimental_source saliva REFERENCE A38355 !$#authors Kauffman, D.L.; Bennick, A.; Blum, M.; Keller, P.J. !$#journal Biochemistry (1991) 30:3351-3356 !$#title Basic proline-rich proteins from human parotid saliva: !1relationships of the covalent structures of ten proteins !1from a single individual. !$#cross-references MUID:91190884; PMID:1849422 !$#accession B38355 !'##molecule_type protein !'##residues 134-194 ##label KAU !'##experimental_source saliva !'##note this peptide, which is closely related to that of peptide P-E, !1contains three 21-residue internal repeats (residues !1134-154, 155-175, and 176-194) !$#accession A38355 !'##molecule_type protein !'##residues 10-67,'R' ##label KA2 !$#accession F38355 !'##molecule_type protein !'##residues 196-251 ##label KA3 GENETICS !$#gene GDB:PRB2 !'##cross-references GDB:119512; OMIM:168810 !$#map_position 12p13.2-12p13.2 CLASSIFICATION #superfamily proline-rich protein KEYWORDS glycoprotein; saliva; tandem repeat FEATURE !$134-194 #product basic proline-rich peptide P-F #status !8experimental #label MAT1\ !$196-251 #product basic proline-rich peptide IB-4 #status !8experimental #label MAT2\ !$3,65,107 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 251 #checksum 4427 SEQUENCE /// ENTRY PIHUSD #type complete TITLE salivary proline-rich glycoprotein precursor PRB4 (large allele) [validated] - human CONTAINS basic proline-rich protein IB-5; proline-rich peptide P-D ORGANISM #formal_name Homo sapiens #common_name man DATE 19-Feb-1984 #sequence_revision 12-Apr-1996 #text_change 08-Dec-2000 ACCESSIONS S03176; S03175; S10890; D25372; E38355; A03295; A61294; !1S62891 REFERENCE S02127 !$#authors Lyons, K.M.; Stein, J.H.; Smithies, O. !$#journal Genetics (1988) 120:267-278 !$#title Length polymorphisms in human proline-rich protein genes !1generated by intragenic unequal crossing over. !$#cross-references MUID:89121440; PMID:2851479 !$#accession S03176 !'##status translation not shown !'##molecule_type DNA !'##residues 35-310 ##label LY1 !'##cross-references EMBL:X07715 !'##note large allele !$#accession S03175 !'##status translation not shown !'##molecule_type DNA !'##residues 35-36,'E',38-112,155-310 ##label LY2 !'##cross-references EMBL:X07704 !'##note medium allele !$#accession S10890 !'##status preliminary; translation not shown !'##molecule_type DNA !'##residues 1-38,60-112,'T',114-115,'P',117-121,185-271,'A',273-310 !1##label LY3 !'##cross-references EMBL:X07882; NID:g35647; PIDN:CAA30729.1; !1PID:g296670 REFERENCE A92492 !$#authors Maeda, N.; Kim, H.S.; Azen, E.A.; Smithies, O. !$#journal J. Biol. Chem. (1985) 260:11123-11130 !$#title Differential RNA splicing and post-translational cleavages !1in the human salivary proline-rich protein gene system. !$#cross-references MUID:85289325; PMID:2993301 !$#accession D25372 !'##molecule_type mRNA !'##residues 1-36,'E',38-112,'T',114-115,'P',117-121,185-271,'A',273-310 !1##label MAE REFERENCE A38355 !$#authors Kauffman, D.L.; Bennick, A.; Blum, M.; Keller, P.J. !$#journal Biochemistry (1991) 30:3351-3356 !$#title Basic proline-rich proteins from human parotid saliva: !1relationships of the covalent structures of ten proteins !1from a single individual. !$#cross-references MUID:91190884; PMID:1849422 !$#accession E38355 !'##molecule_type protein !'##residues 241-254,'KN',257-310 ##label KAU REFERENCE A03295 !$#authors Saitoh, E.; Isemura, S.; Sanada, K. !$#journal J. Biochem. (1983) 93:495-502 !$#title Complete amino acid sequence of a basic proline-rich !1peptide, P-D, from human parotid saliva. !$#cross-references MUID:83186122; PMID:6841349 !$#accession A03295 !'##molecule_type protein !'##residues 241-310 ##label SAI REFERENCE A61294 !$#authors Shimomura, H.; Kanai, Y.; Sanada, K. !$#journal J. Biochem. (1983) 93:857-863 !$#title Amino acid sequences of glycopeptides obtained from basic !1proline-rich glycoprotein of human parotid saliva. !$#cross-references MUID:83265671; PMID:6874667 !$#accession A61294 !'##molecule_type protein !'##residues 54-57,'E',59-73,'R';82-101 ##label SHI REFERENCE S62891 !$#authors Charlton, A.J.; Baxter, N.J.; Lilley, T.H.; Haslam, E.; !1McDonald, C.J.; Williamson, M.P. !$#journal FEBS Lett. (1996) 382:289-292 !$#title Tannin interactions with a full-length human salivary !1proline-rich protein display a stronger affinity than with !1single proline-rich repeats. !$#cross-references MUID:96184506; PMID:8605987 !$#accession S62891 !'##molecule_type protein !'##residues 241-252 ##label CHA !'##note amino end of peptide designated basic proline-rich protein IB-5 !'##note it is unclear from the peptide sequence whether this is a !1product of the PRB2 (PIR:PIHUPF) or PRB4 (this entry) gene GENETICS !$#gene GDB:PRB4 !'##cross-references GDB:119514; OMIM:180990 !$#map_position 12p13.2-12p13.2 !$#introns 22/1; 34/1 !$#note the list of introns may be incomplete CLASSIFICATION #superfamily proline-rich protein KEYWORDS glycoprotein; saliva; tandem repeat FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$241-310 #product proline-rich peptide P-D #status !8experimental #label MAT\ !$66,87,171 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$108,150,192,213,234 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 310 #molecular-weight 31351 #checksum 3960 SEQUENCE /// ENTRY PIRT3 #type complete TITLE acidic proline-rich protein precursor - rat ALTERNATE_NAMES PRP ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 22-Jun-1999 ACCESSIONS A03296 REFERENCE A03296 !$#authors Ziemer, M.A.; Swain, W.F.; Rutter, W.J.; Clements, S.; Ann, !1D.K.; Carlson, D.M. !$#journal J. Biol. Chem. (1984) 259:10475-10480 !$#title Nucleotide sequence analysis of a proline-rich protein cDNA !1and peptide homologies of rat and human proline-rich !1proteins. !$#cross-references MUID:84289443; PMID:6547951 !$#accession A03296 !'##molecule_type mRNA !'##residues 1-206 ##label ZIE !'##cross-references GB:K02247; NID:g206395; PIDN:AAA41949.1; !1PID:g206396 COMMENT This protein contains six 18- to 19-residue repeats. COMMENT This protein may protect teeth by binding to tannins. CLASSIFICATION #superfamily proline-rich protein KEYWORDS duplication; parotid gland; saliva; tandem repeat FEATURE !$1-13 #domain signal sequence #status predicted #label SIG\ !$14-206 #product acidic proline-rich protein #status !8predicted #label MAT\ !$80-189 #region 18-residue repeats SUMMARY #length 206 #molecular-weight 21403 #checksum 841 SEQUENCE /// ENTRY PJHUSB #type complete TITLE proline-rich peptide P-B precursor [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Nov-1979 #sequence_revision 03-Aug-1995 #text_change 21-Jul-2000 ACCESSIONS JX0321; A03297; S19281; JC7215 REFERENCE JX0321 !$#authors Isemura, S.; Saitoh, E. !$#journal J. Biochem. (1994) 115:1101-1106 !$#title Molecular cloning and sequence analysis of cDNA coding for !1the precursor of the human salivary proline-rich peptide !1P-B. !$#cross-references MUID:95073971; PMID:7982889 !$#accession JX0321 !'##molecule_type mRNA !'##residues 1-79 ##label ISE !'##cross-references DDBJ:D29833; NID:g6630614; PIDN:BAA06213.1; !1PID:g705389 !'##experimental_source salivary gland REFERENCE A03297 !$#authors Isemura, S.; Saitoh, E.; Sanada, K. !$#journal J. Biochem. (1979) 86:79-86 !$#title Isolation and amino acid sequences of proline-rich peptides !1of human whole saliva. !$#cross-references MUID:80006513; PMID:479131 !$#accession A03297 !'##molecule_type protein !'##residues 23-79 ##label IS2 !'##experimental_source saliva !'##note the sequence of another peptide, designated P-A, corresponded !1to the carboxyl-terminal 38 residues of P-B and was probably !1a degradation product REFERENCE S19279 !$#authors Ramasubbu, N.; Reddy, M.S.; Bergey, E.J.; Haraszthy, G.G.; !1Soni, S.D.; Levine, M.J. !$#journal Biochem. J. (1991) 280:341-352 !$#title Large-scale purification and characterization of the major !1phosphoproteins and mucins of human submandibular-sublingual !1saliva. !$#cross-references MUID:92082469; PMID:1747107 !$#accession S19281 !'##molecule_type protein !'##residues 30-43 ##label RAM REFERENCE JC7215 !$#authors Isemura, S. !$#journal J. Biochem. (2000) 127:393-398 !$#title Nucleotide sequence of gene PBII encoding salivary !1proline-rich protein P-B. !$#cross-references MUID:20198251; PMID:10731710 !$#accession JC7215 !'##status preliminary !'##molecule_type DNA !'##residues 1-79 ##label IS3 !'##cross-references DDBJ:AB031740; PIDN:BAA88517.1 GENETICS !$#gene GDB:P-B !'##cross-references GDB:9958441 CLASSIFICATION #superfamily proline-rich peptide P-B KEYWORDS pyroglutamic acid FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-79 #product proline-rich peptide P-B #status !8experimental #label MAT\ !$23 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental SUMMARY #length 79 #molecular-weight 8188 #checksum 7694 SEQUENCE /// ENTRY SQMS #type complete TITLE parotid secretory protein precursor - mouse ALTERNATE_NAMES PSP ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 22-Jun-1999 ACCESSIONS A23031; I53236 REFERENCE A23031 !$#authors Madsen, H.O.; Hjorth, J.P. !$#journal Nucleic Acids Res. (1985) 13:1-13 !$#title Molecular cloning of mouse PSP mRNA. !$#cross-references MUID:85215456; PMID:2582349 !$#accession A23031 !'##molecule_type mRNA !'##residues 1-235 ##label MAD !'##cross-references GB:X01697; NID:g53810; PIDN:CAA25846.1; PID:g758163 REFERENCE I53236 !$#authors Poulsen, K.; Jakobsen, B.K.; Mikkelsen, B.M.; Harmark, K.; !1Nielsen, J.T.; Hjorth, J.P. !$#journal EMBO J. (1986) 5:1891-1896 !$#title Coordination of murine parotid secretory protein and !1salivary amylase expression. !$#cross-references MUID:87004556; PMID:2428613 !$#accession I53236 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-87 ##label RES !'##cross-references GB:M26807; NID:g200556; PIDN:AAA40009.1; !1PID:g554264 COMMENT PSP is the most abundant protein in the parotid gland. Its !1function is not known; however, its production is !1coordinated with that of salivary amylase. GENETICS !$#gene Psp !$#map_position 2 !$#introns 41/1 !$#note list of introns may be incomplete CLASSIFICATION #superfamily parotid secretory protein KEYWORDS parotid gland; saliva FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-235 #product parotid secretory protein #status predicted !8#label MAT SUMMARY #length 235 #molecular-weight 24753 #checksum 1500 SEQUENCE /// ENTRY WMMS16 #type complete TITLE submandibular gland 16.5K protein - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 22-Jun-1999 ACCESSIONS A03298 REFERENCE A93503 !$#authors Windass, J.D.; Mullins, J.J.; Beecroft, L.J.; George, H.; !1Meacock, P.A.; Williams, B.R.G.; Brammar, W.J. !$#journal Nucleic Acids Res. (1984) 12:1361-1376 !$#title Molecular cloning of cDNAs from androgen-independent mRNA !1species of DBA/2 mouse sub-maxillary glands. !$#cross-references MUID:84144035; PMID:6546617 !$#accession A03298 !'##molecule_type mRNA !'##residues 1-138 ##label WIN !'##cross-references GB:X00349; NID:g51367; PIDN:CAA25098.1; PID:g51368 COMMENT This protein contains a hydrophobic amino-terminal sequence !1that is similar to a signal sequence. It is probably !1secreted as an acidic, hydrophilic glycoprotein. CLASSIFICATION #superfamily submandibular gland 16.5K protein KEYWORDS glycoprotein; submandibular gland FEATURE !$25,72,89,94 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 138 #molecular-weight 14896 #checksum 4558 SEQUENCE /// ENTRY WMMS14 #type complete TITLE submandibular gland 14K protein - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 28-May-1999 ACCESSIONS A03299 REFERENCE A93503 !$#authors Windass, J.D.; Mullins, J.J.; Beecroft, L.J.; George, H.; !1Meacock, P.A.; Williams, B.R.G.; Brammar, W.J. !$#journal Nucleic Acids Res. (1984) 12:1361-1376 !$#title Molecular cloning of cDNAs from androgen-independent mRNA !1species of DBA/2 mouse sub-maxillary glands. !$#cross-references MUID:84144035; PMID:6546617 !$#accession A03299 !'##molecule_type mRNA !'##residues 1-129 ##label WIN !'##cross-references GB:X02510; GB:K02296; NID:g51369; PIDN:CAA26346.1; !1PID:g51370 !'##note the authors translated the codon AAT for residues 104 and 124 !1as Asp COMMENT Lack of a hydrophobic region at the amino end may indicate !1that this protein is intracellular. However, similary to a !1related human sequence in entry SQHUAC suggests that the !1amino end shown here may not be exact. CLASSIFICATION #superfamily submandibular gland 14K protein KEYWORDS submandibular gland FEATURE !$48-74,72-106 #disulfide_bonds #status predicted SUMMARY #length 129 #molecular-weight 14870 #checksum 5481 SEQUENCE /// ENTRY SQHUAC #type complete TITLE secretory actin-binding protein precursor [validated] - human ALTERNATE_NAMES gross cystic fluid protein 15; prolactin-induced protein; SABP ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 08-Dec-2000 ACCESSIONS I37432; A29469; S14770; A40177; S53792 REFERENCE I37432 !$#authors Myal, Y.; Robinson, D.B.; Iwasiow, B.; Tsuyuki, D.; Wong, !1P.; Shiu, R.P. !$#journal Mol. Cell. Endocrinol. (1991) 80:165-175 !$#title The prolactin-inducible protein (PIP/GCDFP-15) gene: !1cloning, structure and regulation. !$#cross-references MUID:92064134; PMID:1955075 !$#accession I37432 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-146 ##label RES !'##cross-references EMBL:X51501; NID:g31889; PIDN:CAA35870.1; !1PID:g825666 !'##note nucleic acid sequence not complete REFERENCE A29469 !$#authors Murphy, L.C.; Tsuyuki, D.; Myal, Y.; Shiu, R.P.C. !$#journal J. Biol. Chem. (1987) 262:15236-15241 !$#title Isolation and sequencing of a cDNA clone for a !1prolactin-inducible protein (PIP). Regulation of PIP gene !1expression in the human breast cancer cell line, T-47D. !$#cross-references MUID:88033111; PMID:3667631 !$#accession A29469 !'##molecule_type mRNA !'##residues 1-146 ##label MUR !'##cross-references GB:J03460; NID:g189963; PIDN:AAA60091.1; !1PID:g189964 REFERENCE S14770 !$#authors Schaller, J.; Akiyama, K.; Kimura, H.; Hess, D.; Affolter, !1M.; Rickli, E.E. !$#journal Eur. J. Biochem. (1991) 196:743-750 !$#title Primary structure of a new actin-binding protein from human !1seminal plasma. !$#cross-references MUID:91192048; PMID:2013294 !$#accession S14770 !'##molecule_type protein !'##residues 29-146 ##label SCH REFERENCE A40177 !$#authors Schaller, J.; Hess, D.; Affolter, M.; Rickli, E.E.; Akiyama, !1K.; Kimura, H. !$#journal J. Protein Chem. (1990) 9:360 !$#title Primary structure of a new actin-binding protein from human !1seminal plasma. !$#accession A40177 !'##molecule_type protein !'##residues 31-146 ##label SC2 !'##experimental_source seminal plasma REFERENCE S53792 !$#authors Schenkels, L.C.P.M.; Schaller, J.; Walgreen-Weterings, E.; !1Schadee-Eestermans, I.L.; Veerman, E.C.I.; Amerongen, A.V.N. !$#journal Biol. Chem. Hoppe-Seyler (1994) 375:609-615 !$#title Identity of human extra parotid glycoprotein (EP-GP) with !1secretory actin binding protein (SABP) and its biological !1properties. !$#cross-references MUID:95142939; PMID:7840903 !$#accession S53792 !'##molecule_type protein !'##residues 39-44;137-146 ##label SC3 GENETICS !$#gene GDB:PIP !'##cross-references GDB:120292; OMIM:176720 !$#map_position 7q32-7qter !$#introns 32/2; 67/3; 106/1 CLASSIFICATION #superfamily submandibular gland 14K protein KEYWORDS actin binding; glycoprotein; pyroglutamic acid FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-146 #product secretory actin-binding protein #status !8experimental #label MAT\ !$29 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$65-91,89-123 #disulfide_bonds #status experimental\ !$105 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 146 #molecular-weight 16572 #checksum 3681 SEQUENCE /// ENTRY JMBO #type complete TITLE amelogenin I precursor - bovine CONTAINS leucine-rich amelogenin peptide, LRAP-43; leucine-rich amelogenin peptide, LRAP-48; leucine-rich amelogenin peptide, LRAP-59; tyrosine-rich amelogenin peptide, TRAP-43; tyrosine-rich amelogenin peptide, TRAP-45 ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 28-May-1986 #sequence_revision 06-Feb-1995 #text_change 22-Jun-1999 ACCESSIONS A37998; JN0123; A26549; A03300; PC2005; PC2007 REFERENCE A37998 !$#authors Gibson, C.; Golub, E.; Herold, R.; Risser, M.; Ding, W.; !1Shimokawa, H.; Young, M.; Termine, J.; Rosenbloom, J. !$#journal Biochemistry (1991) 30:1075-1079 !$#title Structure and expression of the bovine amelogenin gene. !$#cross-references MUID:91113686; PMID:1989679 !$#accession A37998 !'##molecule_type mRNA !'##residues 1-213 ##label GI2 !'##cross-references GB:M63499; NID:g162659; PIDN:AAA30372.1; !1PID:g162660 REFERENCE JN0123 !$#authors Gibson, C.W.; Golub, E.; Ding, W.; Shimokawa, H.; Young, M.; !1Termine, J.; Rosenbloom, J. !$#journal Biochem. Biophys. Res. Commun. (1991) 174:1306-1312 !$#title Identification of the leucine-rich amelogenin peptide (LRAP) !1as the translation product of an alternatively spliced !1transcript. !$#cross-references MUID:91144612; PMID:1996994 !$#accession JN0123 !'##molecule_type mRNA !'##residues 7-49,188-211 ##label GIB !'##cross-references GB:M63631; NID:g163308; PIDN:AAA30625.1; !1PID:g163309 !'##experimental_source tooth REFERENCE A26549 !$#authors Shimokawa, H.; Sobel, M.E.; Sasaki, M.; Termine, J.D.; !1Young, M.F. !$#journal J. Biol. Chem. (1987) 262:4042-4047 !$#title Heterogeneity of amelogenin mRNA in the bovine tooth germ. !$#cross-references MUID:87166009; PMID:3549722 !$#accession A26549 !'##molecule_type mRNA !'##residues 49-65,'Y',67-108,116-143,153-179,'V',181-183,'L',185-188, !1'M',190-192,'I',194-213 ##label SHI !'##cross-references GB:J02696 REFERENCE A03300 !$#authors Takagi, T.; Suzuki, M.; Baba, T.; Minegishi, K.; Sasaki, S. !$#journal Biochem. Biophys. Res. Commun. (1984) 121:592-597 !$#title Complete amino acid sequence of amelogenin in developing !1bovine enamel. !$#cross-references MUID:84231410; PMID:6732825 !$#accession A03300 !'##molecule_type protein !'##residues 17-33,'Q',35-55,'Q',57-76,'D',78-82,'P',84-108,117-125,'T', !1127-152,'L',154-162,'H',164,'P',165-166,'I',168,'Q',170-171, !1176,'F',178-182,187-194,'N',196-198,'Q',200-201 ##label TAK REFERENCE PC2005 !$#authors Fincham, A.G.; Moradian-Oldak, J. !$#journal Biochem. Biophys. Res. Commun. (1993) 197:248-255 !$#title Amelogenin post-translational modifications: !1carboxy-terminal processing and the phosphorylation of !1bovine and porcine "TRAP" and "LRAP" amelogenins. !$#cross-references MUID:94071951; PMID:8250931 !$#accession PC2005 !'##molecule_type protein !'##residues 17-61 ##label FI2 !$#accession PC2007 !'##molecule_type protein !'##residues 17-40;48-49,188-202 ##label FIN COMMENT Amelogenin is the predominant protein in developing dental !1enamel. GENETICS !$#map_position X CLASSIFICATION #superfamily amelogenin KEYWORDS alternative splicing; enamel; phosphoprotein; tandem repeat; !1tooth FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-213 #product amelogenin #status predicted #label MAT\ !$17-61 #product tyrosine-rich amelogenin peptide, TRAP-45 !8#status experimental #label MA2\ !$17-59 #product tyrosine-rich amelogenin peptide, TRAP-43 !8#status experimental #label MA3\ !$17-49,188-213 #product leucine-rich amelogenin peptide, LRAP-59 !8#status experimental #label MA4\ !$17-49,188-202 #product leucine-rich amelogenin peptide, LRAP-48 !8#status experimental #label MA5\ !$17-49,188-196 #product leucine-rich amelogenin peptide, LRAP-43 !8#status experimental #label MA6\ !$136-165 #region 3-residue repeats (Q-P-X)\ !$32 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 213 #molecular-weight 24119 #checksum 90 SEQUENCE /// ENTRY GERTX1 #type complete TITLE matrix glycoprotein SC1 precursor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 17-Nov-2000 ACCESSIONS I58173; JQ0593 REFERENCE I58173 !$#authors Johnston, I.G.; Paladino, T.; Gurd, J.W.; Brown, I.R. !$#journal Neuron (1990) 4:165-176 !$#title Molecular cloning of SC1: a putative brain extracellular !1matrix glycoprotein showing partial similarity to !1osteonectin/BM40/SPARC. !$#cross-references MUID:90180492; PMID:1690015 !$#accession I58173 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-634 ##label JOH !'##cross-references EMBL:U27562; NID:g868164; PIDN:AAA68708.1; !1PID:g868165 CLASSIFICATION #superfamily matrix glycoprotein SC1; calmodulin repeat !1homology; Kazal proteinase inhibitor homology; osteonectin !1homology KEYWORDS calcium binding; EF hand; extracellular matrix; glycoprotein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-634 #product matrix glycoprotein SC1 #status predicted !8#label MAT\ !$81-113 #domain calmodulin repeat homology #label EF1\ !$318-350 #domain calmodulin repeat homology #label EF2\ !$401-634 #domain osteonectin homology #label OST\ !$422-479 #domain Kazal proteinase inhibitor homology #label !8KPI\ !$592-624 #domain calmodulin repeat homology #label EF4\ !$144,368,446 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$424-460,432-453, !$442-479,485-596, !$604-620 #disulfide_bonds #status predicted SUMMARY #length 634 #molecular-weight 70633 #checksum 1474 SEQUENCE /// ENTRY A39379 #type complete TITLE hatching-suppressed osteonectin-like retinal protein precursor - Japanese quail ORGANISM #formal_name Coturnix coturnix japonica #common_name Japanese quail DATE 20-Mar-1992 #sequence_revision 20-Mar-1992 #text_change 17-Nov-2000 ACCESSIONS A39379 REFERENCE A39379 !$#authors Guermah, M.; Crisanti, P.; Laugier, D.; Dezelee, P.; Bidou, !1L.; Pessac, B.; Calothy, G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:4503-4507 !$#title Transcription of a quail gene expressed in embryonic retinal !1cells is shut off sharply at hatching. !$#cross-references MUID:91239596; PMID:2034690 !$#accession A39379 !'##status preliminary !'##molecule_type mRNA !'##residues 1-676 ##label GUE !'##cross-references GB:M61908; NID:g213614; PIDN:AAA49499.1; !1PID:g213615 CLASSIFICATION #superfamily hatching-suppressed osteonectin-like retinal !1protein; calmodulin repeat homology; Kazal proteinase !1inhibitor homology; osteonectin homology KEYWORDS EF hand; embryo; retina FEATURE !$443-676 #domain osteonectin homology #label OST\ !$464-521 #domain Kazal proteinase inhibitor homology #label !8KPI\ !$634-666 #domain calmodulin repeat homology #label EFH SUMMARY #length 676 #molecular-weight 78142 #checksum 6459 SEQUENCE /// ENTRY GEHUN #type complete TITLE osteonectin precursor [validated] - human ALTERNATE_NAMES basesment membrane protein BM-40; secreted protein acidic and rich in cysteine; SPARC ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1991 #sequence_revision 31-Dec-1993 #text_change 08-Dec-2000 ACCESSIONS A32821; A60968; S01334; A29974; E28457; S16168; S16315; !1A60162; S68324 REFERENCE A32821 !$#authors Villarreal, X.C.; Mann, K.G.; Long, G.L. !$#journal Biochemistry (1989) 28:6483-6491 !$#title Structure of human osteonectin based upon analysis of cDNA !1and genomic sequences. !$#cross-references MUID:90001202; PMID:2790009 !$#accession A32821 !'##molecule_type DNA !'##residues 1-204,'L',206-268,'L',270-303 ##label VIL !'##cross-references EMBL:M25738 REFERENCE A60968 !$#authors Young, M.F.; Day, A.A.; Dominquez, P.; McQuillan, C.I.; !1Fisher, L.W.; Termine, J.D. !$#journal Connect. Tissue Res. (1990) 24:17-28 !$#title Structure and expression of osteonectin mRNA in human !1tissue. !$#cross-references MUID:90249219; PMID:2338025 !$#accession A60968 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-303 ##label YOU REFERENCE S01334 !$#authors Lankat-Buttgereit, B.; Mann, K.; Deutzmann, R.; Timpl, R.; !1Krieg, T. !$#journal FEBS Lett. (1988) 236:352-356 !$#title Cloning and complete amino acid sequences of human and !1murine basement membrane protein BM-40 (SPARC, osteonectin). !$#cross-references MUID:88312997; PMID:3410046 !$#accession S01334 !'##molecule_type mRNA !'##residues 1-303 ##label LAN !'##cross-references EMBL:Y00755; NID:g29461; PIDN:CAA68724.1; !1PID:g29462 REFERENCE A29974 !$#authors Swaroop, A.; Hogan, B.L.M.; Francke, U. !$#journal Genomics (1988) 2:37-47 !$#title Molecular analysis of the cDNA for human SPARC/osteonectin/ !1BM-40: sequence, expression, and localization of the gene to !1chromosome 5q31-q33. !$#cross-references MUID:88256150; PMID:2838412 !$#accession A29974 !'##molecule_type mRNA !'##residues 1-303 ##label SWA !'##cross-references EMBL:J03040; NID:g338312; PIDN:AAA60570.1; !1PID:g338313 REFERENCE A92656 !$#authors Fisher, L.W.; Hawkins, G.R.; Tuross, N.; Termine, J.D. !$#journal J. Biol. Chem. (1987) 262:9702-9708 !$#title Purification and partial characterization of small !1proteoglycans I and II, bone sialoproteins I and II, and !1osteonectin from the mineral compartment of developing human !1bone. !$#cross-references MUID:87250639; PMID:3597437 !$#accession E28457 !'##molecule_type protein !'##residues 18-41,'PT',44-53 ##label FIS REFERENCE A27690 !$#authors Findlay, D.M.; Fisher, L.W.; McQuillan, C.I.; Termine, J.D.; !1Young, M.F. !$#journal Biochemistry (1988) 27:1483-1489 !$#title Isolation of the osteonectin gene: evidence that a variable !1region of the osteonectin molecule is encoded within one !1exon. !$#cross-references MUID:88209512; PMID:2835093 !$#accession S16168 !'##molecule_type protein !'##residues 18-41,'PT',44-54 ##label FIN REFERENCE S16315 !$#authors Nischt, R.; Pottgiesser, J.; Krieg, T.; Mayer, U.; !1Aumailley, M.; Timpl, R. !$#journal Eur. J. Biochem. (1991) 200:529-536 !$#title Recombinant expression and properties of the human !1calcium-binding extracellular matrix protein BM-40. !$#cross-references MUID:91364705; PMID:1653704 !$#accession S16315 !'##molecule_type protein !'##residues 18-31 ##label NIS REFERENCE A60162 !$#authors Kelm Jr., R.J.; Mann, K.G. !$#journal Blood (1990) 75:1105-1113 !$#title Human platelet osteonectin: release, surface expression, and !1partial characterization. !$#cross-references MUID:90167274; PMID:2306517 !$#accession A60162 !'##molecule_type protein !'##residues 18-38,'X',40-41 ##label KEL !'##note this protein was purified from platelets rather than from bone; !1it had an identical sequence near the amino end but !1different physical properties from bone osteonectin REFERENCE S68324 !$#authors Bassuk, J.A.; Baneyx, F.; Vernon, R.B.; Funk, S.E.; Sage, !1E.H. !$#journal Arch. Biochem. Biophys. (1996) 325:8-19 !$#title Expression of biologically active human SPARC in Escherichia !1coli. !$#cross-references MUID:96140592; PMID:8554346 !$#accession S68324 !'##molecule_type protein !'##residues 19-33 ##label BAS GENETICS !$#gene GDB:SPARC !'##cross-references GDB:118733; OMIM:182120 !$#map_position 5q31.3-5q32 !$#introns 19/3; 40/3; 70/1; 81/3; 151/1; 195/3; 245/2; 295/1 CLASSIFICATION #superfamily osteonectin; calmodulin repeat homology; Kazal !1proteinase inhibitor homology; osteonectin homology KEYWORDS calcium binding; collagen binding; duplication; EF hand; !1extracellular matrix; glycoprotein; hydroxyapatite binding; !1phosphoprotein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-303 #product osteonectin #status experimental #label MAT\ !$18-69 #domain I #label DOM1\ !$18-39 #domain repeat #label RP1\ !$45-67 #domain repeat #label RP2\ !$70-303 #domain osteonectin homology #label OST\ !$70-155 #domain II #label DOM2\ !$91-149 #domain Kazal proteinase inhibitor homology #label !8KPI\ !$156-229 #domain III #label DOM3\ !$182-193 #domain calcium binding #status predicted #label CA1\ !$226-259 #domain calmodulin repeat homology #label EF1\ !$230-303 #domain IV #label DOM4\ !$261-293 #domain calmodulin repeat homology #label EF2\ !$93-130,101-123, !$112-149,155-265, !$273-289 #disulfide_bonds #status predicted\ !$116 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$121,158 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 303 #molecular-weight 34632 #checksum 4602 SEQUENCE /// ENTRY GEBON #type complete TITLE osteonectin precursor - bovine ALTERNATE_NAMES basesment membrane protein BM-40; SPARC ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 17-Nov-2000 ACCESSIONS A31333; A27690; S02294; A22292; S16171; S00999 REFERENCE A31333 !$#authors Bolander, M.E.; Young, M.F.; Fisher, L.W.; Yamada, Y.; !1Termine, J.D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:2919-2923 !$#title Osteonectin cDNA sequence reveals potential binding regions !1for calcium and hydroxyapatite and shows homologies with !1both a basement membrane protein (SPARC) and a serine !1proteinase inhibitor (ovomucoid). !$#cross-references MUID:88203612; PMID:2834720 !$#accession A31333 !'##molecule_type mRNA !'##residues 1-304 ##label BOL !'##cross-references EMBL:J03233; NID:g163460; PIDN:AAA30678.1; !1PID:g163461 REFERENCE A27690 !$#authors Findlay, D.M.; Fisher, L.W.; McQuillan, C.I.; Termine, J.D.; !1Young, M.F. !$#journal Biochemistry (1988) 27:1483-1489 !$#title Isolation of the osteonectin gene: evidence that a variable !1region of the osteonectin molecule is encoded within one !1exon. !$#cross-references MUID:88209512; PMID:2835093 !$#accession A27690 !'##molecule_type DNA !'##residues 1-69 ##label FIN !'##cross-references EMBL:M18874 REFERENCE S02294 !$#authors Young, M.F.; Bolander, M.E.; Day, A.A.; Ramis, C.I.; Robey, !1P.G.; Yamada, Y.; Termine, J.D. !$#journal Nucleic Acids Res. (1986) 14:4483-4497 !$#title Osteonectin mRNA: distribution in normal and transformed !1cells. !$#cross-references MUID:86232586; PMID:3012473 !$#accession S02294 !'##molecule_type mRNA !'##residues 18-36 ##label YOU !'##cross-references EMBL:M31318; NID:g163452; PIDN:AAA30677.1; !1PID:g163453 REFERENCE A22292 !$#authors Romberg, R.W.; Werness, P.G.; Lollar, P.; Riggs, B.L.; Mann, !1K.G. !$#journal J. Biol. Chem. (1985) 260:2728-2736 !$#title Isolation and characterization of native adult osteonectin. !$#cross-references MUID:85131033; PMID:2982834 !$#accession A22292 !'##molecule_type protein !'##residues 19,'ZX',22-26,'Z',28,'Z',30,'E',32-33,'L',35-36 ##label ROM REFERENCE A26309 !$#authors Mason, I.J.; Taylor, A.; Williams, J.G.; Sage, H.; Hogan, !1B.L.M. !$#journal EMBO J. (1986) 5:1465-1472 !$#title Evidence from molecular cloning that SPARC, a major product !1of mouse embryo parietal endoderm, is related to an !1endothelial cell 'culture shock' glycoprotein of M(r) 43 !1000. !$#cross-references MUID:86300644; PMID:3755680 !$#accession S16171 !'##molecule_type protein !'##residues 18-27,'CX',30-31 ##label MAS REFERENCE S00998 !$#authors Domenicucci, C.; Goldberg, H.A.; Hofmann, T.; Isenman, D.; !1Wasi, S.; Sodek, J. !$#journal Biochem. J. (1988) 253:139-151 !$#title Characterization of porcine osteonectin extracted from !1foetal calvariae. !$#cross-references MUID:88339880; PMID:3421938 !$#accession S00999 !'##molecule_type protein !'##residues 18-49,'X',51-55 ##label DOM !'##note 21-Ser and 28-Lys were also found GENETICS !$#gene SPARC !$#map_position U22 !$#introns 19/3; 40/3 CLASSIFICATION #superfamily osteonectin; calmodulin repeat homology; Kazal !1proteinase inhibitor homology; osteonectin homology KEYWORDS calcium binding; collagen binding; EF hand; extracellular !1matrix; glycoprotein; hydroxyapatite binding; phosphoprotein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-304 #product osteonectin #status experimental #label MAT\ !$70-304 #domain osteonectin homology #label OST\ !$91-149 #domain Kazal proteinase inhibitor homology #label !8KPI\ !$262-294 #domain calmodulin repeat homology #label EFH\ !$93-130,101-123, !$112-149,155-266, !$274-290 #disulfide_bonds #status predicted\ !$116 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$121,158 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 304 #molecular-weight 34716 #checksum 5177 SEQUENCE /// ENTRY GEMSN #type complete TITLE osteonectin precursor - mouse ALTERNATE_NAMES basement membrane protein BM-40; SPARC ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 17-Nov-2000 ACCESSIONS A29227; A26309; S01335; A37579; S16167; A27029; S16079; !1B27029; C27029 REFERENCE A29227 !$#authors McVey, J.H.; Nomura, S.; Kelly, P.; Mason, I.J.; Hogan, !1B.L.M. !$#journal J. Biol. Chem. (1988) 263:11111-11116 !$#title Characterization of the mouse SPARC/osteonectin gene. !1Intron/exon organization and an unusual promoter region. !$#cross-references MUID:88298750; PMID:3165375 !$#accession A29227 !'##molecule_type DNA !'##residues 1-302 ##label MCV !'##cross-references EMBL:M20684 REFERENCE A26309 !$#authors Mason, I.J.; Taylor, A.; Williams, J.G.; Sage, H.; Hogan, !1B.L.M. !$#journal EMBO J. (1986) 5:1465-1472 !$#title Evidence from molecular cloning that SPARC, a major product !1of mouse embryo parietal endoderm, is related to an !1endothelial cell 'culture shock' glycoprotein of M(r) 43 !1000. !$#cross-references MUID:86300644; PMID:3755680 !$#accession A26309 !'##molecule_type mRNA !'##residues 1-302 ##label MAS !'##cross-references EMBL:X04017; NID:g54168; PIDN:CAA27642.1; !1PID:g54169 REFERENCE S01334 !$#authors Lankat-Buttgereit, B.; Mann, K.; Deutzmann, R.; Timpl, R.; !1Krieg, T. !$#journal FEBS Lett. (1988) 236:352-356 !$#title Cloning and complete amino acid sequences of human and !1murine basement membrane protein BM-40 (SPARC, osteonectin). !$#cross-references MUID:88312997; PMID:3410046 !$#accession S01335 !'##molecule_type mRNA !'##residues 1-302 ##label LAN1 !$#accession A37579 !'##molecule_type protein !'##residues 18-32;65-75;117-165;168-171;192-200;215-234;239-302 ##label !1LAN2 !'##note 287-Ser was also found REFERENCE S16167 !$#authors Howe, C.C.; Overton, G.C.; Sawicki, J.; Solter, D.; Stein, !1P.; Strickland, S. !$#journal Differentiation (1988) 37:20-25 !$#title Expression of SPARC/osteonectin transcript in murine embryos !1and gonads. !$#cross-references MUID:88255622; PMID:3384223 !$#accession S16167 !'##status translation not shown !'##molecule_type mRNA !'##residues 122-165,'IG',168-209;211-302 ##label HOW !'##cross-references EMBL:X12697 !'##note the codon for residue 210 is incomplete (-AC) REFERENCE A27029 !$#authors Mann, K.; Deutzmann, R.; Paulsson, M.; Timpl, R. !$#journal FEBS Lett. (1987) 218:167-172 !$#title Solubilization of protein BM-40 from a basement membrane !1tumor with chelating agents and evidence for its identity !1with osteonectin and SPARC. !$#cross-references MUID:87247250; PMID:3109947 !$#accession A27029 !'##molecule_type protein !'##residues 18-37;65-70,'X',72-75;133-165;168-171;190-200;215-216,'X', !1218-234;239-262;271-283;285-302 ##label MAN REFERENCE S16079 !$#authors Mayer, U.; Aumailley, M.; Mann, K.; Timpl, R.; Engel, J. !$#journal Eur. J. Biochem. (1991) 198:141-150 !$#title Calcium-dependent binding of basement membrane protein BM-40 !1(osteonectin, SPARC) to basement membrane collagen type IV. !$#cross-references MUID:91249793; PMID:2040276 !$#accession S16079 !'##molecule_type protein !'##residues 18-35;65-75;140-165;172-180;208-211;217-246;256-292 ##label !1MAY REFERENCE S16172 !$#authors Engel, J.; Taylor, W.; Paulsson, M.; Sage, H.; Hogan, B. !$#journal Biochemistry (1987) 26:6958-6965 !$#title Calcium binding domains and calcium-induced conformational !1transition of SPARC/BM-40/osteonectin, an extracellular !1glycoprotein expressed in mineralized and nonmineralized !1tissues. !$#cross-references MUID:88107625; PMID:3427055 !$#contents annotation GENETICS !$#gene SPARC !$#map_position 11 1D !$#introns 19/3; 39/3; 69/1; 109/3; 150/1; 194/3; 244/2; 294/1 CLASSIFICATION #superfamily osteonectin; calmodulin repeat homology; Kazal !1proteinase inhibitor homology; osteonectin homology KEYWORDS calcium binding; collagen binding; EF hand; extracellular !1matrix; glycoprotein; hydroxyapatite binding; phosphoprotein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-302 #product osteonectin #status experimental #label MAT\ !$69-302 #domain osteonectin homology #label OST\ !$90-148 #domain Kazal proteinase inhibitor homology #label !8KPI\ !$260-292 #domain calmodulin repeat homology #label EFH\ !$92-129,100-122, !$111-148,154-264, !$272-288 #disulfide_bonds #status predicted\ !$115 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$120,157 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 302 #molecular-weight 34450 #checksum 2103 SEQUENCE /// ENTRY A47737 #type complete TITLE osteonectin precursor - Caenorhabditis elegans ALTERNATE_NAMES BM-40 precursor; SPARC precursor ORGANISM #formal_name Caenorhabditis elegans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 17-Nov-2000 ACCESSIONS A47737; T32511 REFERENCE A47737 !$#authors Schwarzbauer, J.E.; Spencer, C.S. !$#journal Mol. Biol. Cell (1993) 4:941-952 !$#title The Caenorhabditis elegans homologue of the extracellular !1calcium binding protein SPARC/osteonectin affects nematode !1body morphology and mobility. !$#cross-references MUID:94080020; PMID:8257796 !$#accession A47737 !'##status preliminary !'##molecule_type mRNA !'##residues 1-264 ##label SCH !'##cross-references GB:L21758; NID:g304333; PIDN:AAA16827.1; !1PID:g304334 REFERENCE Z21183 !$#authors Tin-Wollam, A. !$#submission submitted to the EMBL Data Library, December 1997 !$#description The sequence of C. elegans cosmid C44B12. !$#accession T32511 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-264 ##label TIN !'##cross-references EMBL:AF036692; PIDN:AAB88325.1; GSPDB:GN00022; !1CESP:C44B12.2 !'##experimental_source strain Bristol N2; clone C44B12 GENETICS !$#gene SPARC; ost-1 !$#map_position 4 !$#introns 21/3; 46/1; 90/3; 159/3; 208/3 CLASSIFICATION #superfamily osteonectin; calmodulin repeat homology; Kazal !1proteinase inhibitor homology; osteonectin homology KEYWORDS calcium binding; cell adhesion; EF hand; extracellular !1protein; glycoprotein; phosphoprotein FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-264 #product osteonectin #status predicted #label MAT\ !$51-264 #domain osteonectin homology #label OST\ !$72-135 #domain Kazal proteinase inhibitor homology #label !8KPI\ !$224-256 #domain calmodulin repeat homology #label EFH\ !$74-110,80-103, !$92-135,141-228, !$236-252 #disulfide_bonds #status predicted\ !$96 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$101 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 264 #molecular-weight 30172 #checksum 2894 SEQUENCE /// ENTRY GEHU #type complete TITLE osteocalcin precursor [validated] - human ALTERNATE_NAMES BGP; bone Gla protein; gamma-carboxyglutamic acid-containing protein ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1980 #sequence_revision 07-Apr-1994 #text_change 08-Dec-2000 ACCESSIONS S12652; C25471; A03301; S08694 REFERENCE S12652 !$#authors Kiefer, M.C.; Saphire, A.C.S.; Bauer, D.M.; Barr, P.J. !$#journal Nucleic Acids Res. (1990) 18:1909 !$#title The cDNA and derived amino acid sequences of human and !1bovine bone Gla protein. !$#cross-references MUID:90245603; PMID:2336375 !$#accession S12652 !'##molecule_type mRNA !'##residues 1-100 ##label KIE !'##cross-references EMBL:X53698; NID:g36092; PIDN:CAA37736.1; !1PID:g36093 REFERENCE A91045 !$#authors Celeste, A.J.; Rosen, V.; Buecker, J.L.; Kriz, R.; Wang, !1E.A.; Wozney, J.M. !$#journal EMBO J. (1986) 5:1885-1890 !$#title Isolation of the human gene for bone gla protein utilizing !1mouse and rat cDNA clones. !$#cross-references MUID:87004555; PMID:3019668 !$#accession C25471 !'##molecule_type DNA !'##residues 1-32,35-100 ##label CEL !'##cross-references EMBL:X04143; NID:g29449; PIDN:CAA27763.1; !1PID:g29450 REFERENCE A03301 !$#authors Poser, J.W.; Esch, F.S.; Ling, N.C.; Price, P.A. !$#journal J. Biol. Chem. (1980) 255:8685-8691 !$#title Isolation and sequence of the vitamin K-dependent protein !1from human bone. Undercarboxylation of the first glutamic !1acid residue. !$#cross-references MUID:81006914; PMID:6967872 !$#accession A03301 !'##molecule_type protein !'##residues 52-100 ##label POS REFERENCE A44566 !$#authors Cairns, J.R.; Williamson, M.K.; Price, P.A. !$#journal Anal. Biochem. (1991) 199:93-97 !$#title Direct identification of gamma-carboxyglutamic acid in the !1sequencing of vitamin K-dependent proteins. !$#cross-references MUID:92222128; PMID:1807167 !$#contents annotation COMMENT This protein, isolated from bone, binds strongly to apatite. COMMENT Alternative splicing may produce the sequence presented in !1reference A91045. COMMENT Glu-68 is gamma-carboxylated in 9-50% of the molecules. GENETICS !$#gene GDB:BGLAP !'##cross-references GDB:118760; OMIM:112260 !$#map_position 1q25-1q31 !$#introns 22/1; 35/1; 58/2 CLASSIFICATION #superfamily osteocalcin KEYWORDS bone; calcium binding; carboxyglutamic acid; extracellular !1matrix FEATURE !$1-51 #domain signal sequence #status predicted #label SIG\ !$52-100 #product osteocalcin #status experimental #label MAT\ !$60 #modified_site 4-hydroxyproline (Pro) #status absent\ !$68 #modified_site gamma-carboxyglutamic acid (Glu) !8(partial) #status experimental\ !$72,75 #modified_site gamma-carboxyglutamic acid (Glu) !8#status experimental\ !$74-80 #disulfide_bonds #status experimental SUMMARY #length 100 #molecular-weight 10962 #checksum 8909 SEQUENCE /// ENTRY GEMKI #type complete TITLE osteocalcin - crab-eating macaque ALTERNATE_NAMES BGP; bone Gla protein; gamma-carboxyglutamic acid-containing protein ORGANISM #formal_name Macaca fascicularis #common_name crab-eating macaque DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 06-Sep-1996 ACCESSIONS A03302 REFERENCE A03302 !$#authors Hauschka, P.V.; Carr, S.A.; Biemann, K. !$#journal Biochemistry (1982) 21:638-642 !$#title Primary structure of monkey osteocalcin. !$#cross-references MUID:82182842; PMID:6978733 !$#accession A03302 !'##molecule_type protein !'##residues 1-49 ##label HAU COMMENT This protein, isolated from bone, binds strongly to apatite. CLASSIFICATION #superfamily osteocalcin KEYWORDS bone; calcium binding; carboxyglutamic acid; hydroxyproline FEATURE !$9 #modified_site 4-hydroxyproline (Pro) #status !8experimental\ !$17,21,24 #modified_site gamma-carboxyglutamic acid (Glu) !8#status experimental\ !$23-29 #disulfide_bonds #status experimental SUMMARY #length 49 #molecular-weight 5743 #checksum 2211 SEQUENCE /// ENTRY GEBO #type complete TITLE osteocalcin precursor - bovine ALTERNATE_NAMES BGP; bone Gla protein; gamma-carboxyglutamic acid-containing protein ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 24-Apr-1984 #sequence_revision 07-Apr-1994 #text_change 22-Jun-1999 ACCESSIONS S12653; A03303; S08693 REFERENCE S12652 !$#authors Kiefer, M.C.; Saphire, A.C.S.; Bauer, D.M.; Barr, P.J. !$#journal Nucleic Acids Res. (1990) 18:1909 !$#title The cDNA and derived amino acid sequences of human and !1bovine bone Gla protein. !$#cross-references MUID:90245603; PMID:2336375 !$#accession S12653 !'##molecule_type mRNA !'##residues 1-100 ##label KIE !'##cross-references EMBL:X53699; NID:g719; PIDN:CAA37737.1; PID:g720 !'##note alternative splicing may produce a sequence lacking residues !133-34 REFERENCE A03303 !$#authors Price, P.A.; Poser, J.W.; Raman, N. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1976) 73:3374-3375 !$#title Primary structure of the gamma-carboxyglutamic !1acid-containing protein from bovine bone. !$#cross-references MUID:77036749; PMID:1068450 !$#accession A03303 !'##molecule_type protein !'##residues 52-100 ##label PRI COMMENT This protein, isolated from bone, binds strongly to apatite. CLASSIFICATION #superfamily osteocalcin KEYWORDS bone; calcium binding; carboxyglutamic acid; hydroxyproline FEATURE !$1-51 #domain signal sequence #status predicted #label SIG\ !$52-100 #product osteocalcin #status experimental #label MAT\ !$60 #modified_site 4-hydroxyproline (Pro) #status !8experimental\ !$68,72,75 #modified_site gamma-carboxyglutamic acid (Glu) !8#status experimental\ !$74-80 #disulfide_bonds #status experimental SUMMARY #length 100 #molecular-weight 11042 #checksum 6453 SEQUENCE /// ENTRY GECT #type complete TITLE osteocalcin - cat ALTERNATE_NAMES BGP; bone Gla protein; gamma-carboxyglutamic acid-containing protein ORGANISM #formal_name Felis silvestris catus #common_name domestic cat DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 06-Sep-1996 ACCESSIONS A03304 REFERENCE A03304 !$#authors Shimomura, H.; Kanai, Y.; Sanada, K. !$#journal J. Biochem. (1984) 96:405-411 !$#title Primary structure of cat osteocalcin. !$#cross-references MUID:85054706; PMID:6334077 !$#accession A03304 !'##molecule_type protein !'##residues 1-49 ##label SHI CLASSIFICATION #superfamily osteocalcin KEYWORDS bone; calcium binding; carboxyglutamic acid; hydroxyproline FEATURE !$9 #modified_site 4-hydroxyproline (Pro) #status !8experimental\ !$17,21,24 #modified_site gamma-carboxyglutamic acid (Glu) !8#status experimental\ !$23-29 #disulfide_bonds #status experimental SUMMARY #length 49 #molecular-weight 5495 #checksum 1921 SEQUENCE /// ENTRY GERT #type complete TITLE osteocalcin precursor - rat ALTERNATE_NAMES BGP; bone Gla protein; gamma-carboxyglutamic acid-containing protein ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 22-Jun-1999 ACCESSIONS A31856; A31419; A32324; A25167; A25471 REFERENCE A31856 !$#authors Yoon, K.; Rutledge, S.J.C.; Buenaga, R.F.; Rodan, G.A. !$#journal Biochemistry (1988) 27:8521-8526 !$#title Characterization of the rat osteocalcin gene: stimulation of !1promoter activity by 1,25-dihydroxyvitamin D-3. !$#cross-references MUID:89118266; PMID:3265336 !$#accession A31856 !'##molecule_type DNA !'##residues 1-99 ##label YOO !'##cross-references GB:M23637; NID:g340986; PIDN:AAA41761.1; !1PID:g514962 REFERENCE A31419 !$#authors Theofan, G.; Haberstroh, L.M.; Price, P.A. !$#journal DNA (1989) 8:213-221 !$#title Molecular structure of the rat bone Gla protein gene and !1identification of putative regulatory elements. !$#cross-references MUID:89251082; PMID:2785907 !$#accession A31419 !'##molecule_type DNA !'##residues 1-99 ##label THE !'##cross-references GB:M25490; NID:g576530; PIDN:AAA53280.1; !1PID:g576531 REFERENCE A32324 !$#authors Lian, J.; Stewart, C.; Puchacz, E.; Mackowiak, S.; Shalhoub, !1V.; Collart, D.; Zambetti, G.; Stein, G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:1143-1147 !$#title Structure of the rat osteocalcin gene and regulation of !1vitamin D-dependent expression. !$#cross-references MUID:89145200; PMID:2784002 !$#accession A32324 !'##molecule_type DNA !'##residues 1-99 ##label LIA !'##cross-references GB:J04500; NID:g205863; PIDN:AAA41764.1; !1PID:g205864 REFERENCE A25167 !$#authors Pan, L.C.; Price, P.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:6109-6113 !$#title The propeptide of rat bone gamma-carboxyglutamic acid !1protein shares homology with other vitamin K-dependent !1protein precursors. !$#cross-references MUID:85298305; PMID:3875856 !$#accession A25167 !'##molecule_type mRNA !'##residues 1-99 ##label PAN !'##cross-references GB:M11777; NID:g203147; PIDN:AAA40816.1; !1PID:g203148 REFERENCE A91045 !$#authors Celeste, A.J.; Rosen, V.; Buecker, J.L.; Kriz, R.; Wang, !1E.A.; Wozney, J.M. !$#journal EMBO J. (1986) 5:1885-1890 !$#title Isolation of the human gene for bone gla protein utilizing !1mouse and rat cDNA clones. !$#cross-references MUID:87004555; PMID:3019668 !$#accession A25471 !'##molecule_type mRNA !'##residues 1-99 ##label CEL !'##cross-references GB:X04141; NID:g55826; PIDN:CAA27761.1; PID:g55827 GENETICS !$#introns 22/1; 33/1; 56/2 CLASSIFICATION #superfamily osteocalcin KEYWORDS bone; calcium binding; carboxyglutamic acid; hydroxyproline FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-49 #domain propeptide #status predicted #label PRO\ !$50-99 #product osteocalcin #status predicted #label OCN\ !$58 #modified_site 4-hydroxyproline (Pro) #status !8predicted\ !$66,70,73 #modified_site gamma-carboxyglutamic acid (Glu) !8#status predicted\ !$72-78 #disulfide_bonds #status predicted SUMMARY #length 99 #molecular-weight 10927 #checksum 4372 SEQUENCE /// ENTRY A61280 #type complete TITLE osteocalcin - rabbit ALTERNATE_NAMES BGP; bone Gla protein; gamma-carboxyglutamic acid-containing protein ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 12-May-1994 #sequence_revision 02-Jun-1994 #text_change 06-Sep-1996 ACCESSIONS A61280 REFERENCE A61280 !$#authors Virdi, A.S.; Willis, A.C.; Hauschka, P.V.; Triffitt, J.T. !$#journal Biochem. Soc. Trans. (1991) 19:373S !$#title Primary aminoacid sequence of rabbit osteocalcin. !$#cross-references MUID:92175242; PMID:1794506 !$#accession A61280 !'##molecule_type protein !'##residues 1-49 ##label VIR CLASSIFICATION #superfamily osteocalcin KEYWORDS bone; calcium binding; carboxyglutamic acid; hydroxyproline; !1pyroglutamic acid FEATURE !$1 #modified_site pyrrolidone carboxylic acid (Gln) !8#status experimental\ !$9 #modified_site 4-hydroxyproline (Pro) #status !8experimental\ !$17,21,24 #modified_site gamma-carboxyglutamic acid (Glu) !8#status experimental\ !$23-29 #disulfide_bonds #status predicted SUMMARY #length 49 #molecular-weight 5431 #checksum 3021 SEQUENCE /// ENTRY GECH #type complete TITLE osteocalcin precursor - chicken ALTERNATE_NAMES BGP; bone Gla protein; gamma-carboxyglutamic acid-containing protein ORGANISM #formal_name Gallus gallus #common_name chicken DATE 15-Oct-1982 #sequence_revision 15-Aug-1997 #text_change 22-Jun-1999 ACCESSIONS I50700; A03305 REFERENCE I50700 !$#authors Neugebauer, B.M.; Moore, M.A.; Broess, M.; Gerstenfeld, !1L.C.; Hauschka, P.V. !$#journal J. Bone Miner. Res. (1995) 10:157-163 !$#title Characterization of structural sequences in the chicken !1osteocalcin gene: expression of osteocalcin by maturing !1osteoblasts and by hypertrophic chondrocytes in vitro. !$#cross-references MUID:95266465; PMID:7747623 !$#accession I50700 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-97 ##label NEU !'##cross-references EMBL:U10578; NID:g1008455; PIDN:AAA78809.1; !1PID:g595408 REFERENCE A03305 !$#authors Carr, S.A.; Hauschka, P.V.; Biemann, K. !$#journal J. Biol. Chem. (1981) 256:9944-9950 !$#title Gas chromatographic mass spectrometric sequence !1determination of osteocalcin, a gamma-carboxyglutamic !1acid-containing protein from chicken bone. !$#cross-references MUID:82007831; PMID:6792200 !$#accession A03305 !'##molecule_type protein !'##residues 49-63,'I',65-77,'N',79-82,'EL',85-90,'Q',91-97 ##label CAR COMMENT The gamma-carboxyglutamic acid residues formed by vitamin !1K-dependent posttranslational carboxylation are essential !1for the binding of calcium. CLASSIFICATION #superfamily osteocalcin KEYWORDS bone; calcium binding; carboxyglutamic acid FEATURE !$49-97 #product osteocalcin #status experimental #label MAT\ !$65,69,72 #modified_site gamma-carboxyglutamic acid (Glu) !8#status experimental\ !$71-77 #disulfide_bonds #status predicted SUMMARY #length 97 #molecular-weight 10707 #checksum 7327 SEQUENCE /// ENTRY GEWF #type complete TITLE osteocalcin - swordfish ALTERNATE_NAMES BGP; bone Gla protein; gamma-carboxyglutamic acid-containing protein ORGANISM #formal_name Xiphias gladius #common_name swordfish DATE 30-Apr-1979 #sequence_revision 27-Nov-1985 #text_change 06-Sep-1996 ACCESSIONS A03306 REFERENCE A03306 !$#authors Price, P.A.; Otsuka, A.S.; Poser, J.W. !$#book Calcium-binding Proteins and Calcium Function, Wasserman, !1R.H., Corradino, R.A., Carafoli, E., Kretsinger, R.H., !1MacLennan, D.H., and Siegel, F.L., eds., pp.333-337, !1North-Holland, New York, 1977 !$#title Comparison of gamma-carboxyglutamic acid-containing proteins !1from bovine and swordfish bone: primary structure and Ca++ !1binding. !$#accession A03306 !'##molecule_type protein !'##residues 1-47 ##label PRI !'##note residues 14, 24, and 37 were not positively identified CLASSIFICATION #superfamily osteocalcin KEYWORDS bone; calcium binding; carboxyglutamic acid FEATURE !$13,17,20 #modified_site gamma-carboxyglutamic acid (Glu) !8#status experimental\ !$19-25 #disulfide_bonds #status predicted SUMMARY #length 47 #molecular-weight 5080 #checksum 4897 SEQUENCE /// ENTRY A42794 #type complete TITLE osteocalcin - bluegill ALTERNATE_NAMES BGP; bone Gla protein; gamma-carboxyglutamic acid-containing protein ORGANISM #formal_name Lepomis macrochirus #common_name bluegill DATE 31-Dec-1993 #sequence_revision 06-Sep-1996 #text_change 06-Sep-1996 ACCESSIONS A42794 REFERENCE A42794 !$#authors Nishimoto, S.K.; Araki, N.; Robinson, F.D.; Waite, J.H. !$#journal J. Biol. Chem. (1992) 267:11600-11605 !$#title Discovery of bone gamma-carboxyglutamic acid protein in !1mineralized scales. The abundance and structure of Lepomis !1macrochirus bone gamma-carboxyglutamic acid protein. !$#cross-references MUID:92283881; PMID:1597487 !$#accession A42794 !'##molecule_type protein !'##residues 1-45 ##label NIS !'##experimental_source bone; mineralized scale !'##note sequence extracted from NCBI backbone (NCBIP:104759) CLASSIFICATION #superfamily osteocalcin KEYWORDS bone; calcium binding; carboxyglutamic acid; vitamin K FEATURE !$4 #modified_site gamma-carboxyglutamic acid (Glu) !8#status absent\ !$11,15,18 #modified_site gamma-carboxyglutamic acid (Glu) !8#status experimental\ !$17-23 #disulfide_bonds #status predicted SUMMARY #length 45 #molecular-weight 4870 #checksum 8141 SEQUENCE /// ENTRY GEHUM #type complete TITLE matrix Gla protein precursor [validated] - human ALTERNATE_NAMES MGP ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1992 #sequence_revision 30-Sep-1992 #text_change 08-Dec-2000 ACCESSIONS A35811; B35811; S01231; I38018; B40844; S11741 REFERENCE A35811 !$#authors Cancela, L.; Hsieh, C.L.; Francke, U.; Price, P.A. !$#journal J. Biol. Chem. (1990) 265:15040-15048 !$#title Molecular structure, chromosome assignment, and promoter !1organization of the human matrix Gla protein gene. !$#cross-references MUID:90368682; PMID:2394711 !$#accession A35811 !'##molecule_type DNA !'##residues 1-103 ##label CA1 !'##cross-references EMBL:M55270; EMBL:J05572; NID:g187590; !1PIDN:AAB53765.1; PID:g187591 !$#accession B35811 !'##molecule_type mRNA !'##residues 1-103 ##label CA2 !'##cross-references EMBL:M58549; EMBL:J05572; NID:g187592; !1PIDN:AAB53766.1; PID:g187593 REFERENCE S01231 !$#authors Kiefer, M.C.; Bauer, D.M.; Young, D.; Hermsen, K.M.; !1Masiarz, F.R.; Barr, P.J. !$#journal Nucleic Acids Res. (1988) 16:5213 !$#title The cDNA and derived amino acid sequences for human and !1bovine matrix Gla protein. !$#cross-references MUID:88262527; PMID:3387234 !$#accession S01231 !'##molecule_type mRNA !'##residues 1-101,'A',103 ##label KIE !'##cross-references EMBL:X07362; NID:g3928268; PIDN:CAA30287.1; !1PID:g34618 REFERENCE I38018 !$#authors Chen, L.; O'Bryan, J.P.; Smith, H.S.; Liu, E. !$#journal Oncogene (1990) 5:1391-1395 !$#title Overexpression of matrix Gla protein mRNA in malignant human !1breast cells: isolation by differential cDNA hybridization. !$#cross-references MUID:91016442; PMID:2216462 !$#accession I38018 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-101,'A',103 ##label CHE !'##cross-references EMBL:X53331; NID:g34613; PIDN:CAA37418.1; !1PID:g34614 !'##note submitted to the EMBL Data Library, May 1990 REFERENCE A40844 !$#authors Hale, J.E.; Williamson, M.K.; Price, P.A. !$#journal J. Biol. Chem. (1991) 266:21145-21149 !$#title Carboxyl-terminal proteolytic processing of matrix Gla !1protein. !$#cross-references MUID:92041989; PMID:1939157 !$#accession B40844 !'##molecule_type protein !'##residues 20-48;85-96 ##label HAL !'##note the final 7 residues are absent in the secreted form REFERENCE A58570 !$#authors Price, P.A.; Rice, J.S.; Williamson, M.K. !$#journal Protein Sci. (1994) 3:822-830 !$#title Conserved phosphorylation of serines in the Ser-X-Glu/Ser(P) !1sequences of the vitamin K-dependent matrix Gla protein from !1shark, lamb, rat, cow, and human. !$#cross-references MUID:94339842; PMID:8061611 !$#contents annotation; sequence; identification of phosphoserine and !1carboxyglutamic acid in amino-terminal peptide COMMENT This vitamin K-dependent calcium binding protein is secreted !1by most known cell types, but is deposited only in bone, !1cartilage and dentine. During bone development it is !1deposited earlier than osteocalcin. GENETICS !$#gene GDB:MGP !'##cross-references GDB:126860; OMIM:154870 !$#map_position 12pter-12cen !$#introns 21/1; 32/1; 57/2 CLASSIFICATION #superfamily osteocalcin KEYWORDS bone; calcium binding; carboxyglutamic acid; cartilage; !1phosphoprotein; vitamin K FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-96 #product matrix Gla protein #status experimental !8#label MAT\ !$21 #modified_site gamma-carboxyglutamic acid (Glu) !8#status experimental\ !$22,25,28 #binding_site phosphate (Ser) (covalent) (by casein !8kinase II) #status experimental\ !$56,60,67,71 #modified_site gamma-carboxyglutamic acid (Glu) !8#status predicted\ !$73-79 #disulfide_bonds #status predicted SUMMARY #length 103 #molecular-weight 12353 #checksum 1988 SEQUENCE /// ENTRY GEBOM #type complete TITLE matrix Gla protein precursor - bovine ALTERNATE_NAMES MGP ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Dec-1988 #sequence_revision 07-Apr-1994 #text_change 22-Jun-1999 ACCESSIONS S01232; A24237; A40844 REFERENCE S01231 !$#authors Kiefer, M.C.; Bauer, D.M.; Young, D.; Hermsen, K.M.; !1Masiarz, F.R.; Barr, P.J. !$#journal Nucleic Acids Res. (1988) 16:5213 !$#title The cDNA and derived amino acid sequences for human and !1bovine matrix Gla protein. !$#cross-references MUID:88262527; PMID:3387234 !$#accession S01232 !'##molecule_type mRNA !'##residues 1-103 ##label KIE !'##cross-references EMBL:X07363; NID:g528; PIDN:CAA30288.1; PID:g529 REFERENCE A24237 !$#authors Price, P.A.; Williamson, M.K. !$#journal J. Biol. Chem. (1985) 260:14971-14975 !$#title Primary structure of bovine matrix Gla protein, a new !1vitamin K-dependent bone protein. !$#cross-references MUID:86059338; PMID:3877721 !$#accession A24237 !'##molecule_type protein !'##residues 20-98 ##label PRI REFERENCE A40844 !$#authors Hale, J.E.; Williamson, M.K.; Price, P.A. !$#journal J. Biol. Chem. (1991) 266:21145-21149 !$#title Carboxyl-terminal proteolytic processing of matrix Gla !1protein. !$#cross-references MUID:92041989; PMID:1939157 !$#accession A40844 !'##molecule_type protein !'##residues 85-102 ##label HAL !'##note about 50% of the molecules in the secreted form lack the final !1residue; the remainder lack the final 5 residues REFERENCE A44566 !$#authors Cairns, J.R.; Williamson, M.K.; Price, P.A. !$#journal Anal. Biochem. (1991) 199:93-97 !$#title Direct identification of gamma-carboxyglutamic acid in the !1sequencing of vitamin K-dependent proteins. !$#cross-references MUID:92222128; PMID:1807167 !$#contents annotation !$#note Glu-21 is gamma-carboxylated in about 80% of the molecules REFERENCE A58570 !$#authors Price, P.A.; Rice, J.S.; Williamson, M.K. !$#journal Protein Sci. (1994) 3:822-830 !$#title Conserved phosphorylation of serines in the Ser-X-Glu/Ser(P) !1sequences of the vitamin K-dependent matrix Gla protein from !1shark, lamb, rat, cow, and human. !$#cross-references MUID:94339842; PMID:8061611 !$#contents annotation; sequence; identification of phosphoserine and !1carboxyglutamic acid in amino-terminal peptide COMMENT This vitamin K-dependent calcium binding protein is secreted !1by most known cell types, but is deposited only in bone, !1cartilage and dentine. During bone development it is !1deposited earlier than osteocalcin. CLASSIFICATION #superfamily osteocalcin KEYWORDS bone; calcium binding; carboxyglutamic acid; cartilage; !1phosphoprotein; vitamin K FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-102 #product matrix Gla protein, long form #status !8experimental #label MAT1\ !$20-98 #product matrix Gla protein, short form #status !8experimental #label MAT2\ !$21 #modified_site gamma-carboxyglutamic acid (Glu) !8(partial) #status experimental\ !$22,25,28 #binding_site phosphate (Ser) (covalent) (by casein !8kinase II) #status experimental\ !$56,60,67,71 #modified_site gamma-carboxyglutamic acid (Glu) !8#status experimental\ !$73-79 #disulfide_bonds #status experimental SUMMARY #length 103 #molecular-weight 12217 #checksum 8787 SEQUENCE /// ENTRY GEMSM1 #type complete TITLE matrix Gla protein precursor - mouse ALTERNATE_NAMES MGP ORGANISM #formal_name Mus musculus #common_name house mouse DATE 07-Sep-1990 #sequence_revision 25-Apr-1997 #text_change 22-Jun-1999 ACCESSIONS JQ0455; I55484 REFERENCE JQ0455 !$#authors Ikeda, T. !$#submission submitted to JIPID, May 1990 !$#accession JQ0455 !'##molecule_type mRNA !'##residues 1-104 ##label IKE !'##cross-references DDBJ:D00613; NID:g220478; PIDN:BAA00488.1; !1PID:g220479 !'##experimental_source strain C57BL/6, cell type osteoblast REFERENCE I55484 !$#authors Luo, G.; D'Souza, R.; Hogue, D.; Karsenty, G. !$#journal J. Bone Miner. Res. (1995) 10:325-334 !$#title The matrix Gla protein gene is a marker of the !1chondrogenesis cell lineage during mouse development. !$#cross-references MUID:95274434; PMID:7754814 !$#accession I55484 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-24,'I',26-104 ##label LUO !'##cross-references GB:S77350; NID:g998473 !'##experimental_source 129 SvEv !'##note the source is designated as mouse and classified as Mus sp. by !1NCBI COMMENT This vitamin K-dependent calcium binding protein is secreted !1by most known cell types, but is deposited only in bone, !1cartilage and dentine. During bone development it is !1deposited earlier than osteocalcin. GENETICS !$#introns 21/1; 32/1; 57/2 CLASSIFICATION #superfamily osteocalcin KEYWORDS bone; calcium binding; carboxyglutamic acid; cartilage; !1phosphoprotein; vitamin K FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-104 #product matrix Gla protein #status predicted #label !8MAT\ !$21,60,67,71 #modified_site gamma-carboxyglutamic acid (Glu) !8#status predicted\ !$22,25,28 #binding_site phosphate (Ser) (covalent) (by casein !8kinase II) #status predicted\ !$73-79 #disulfide_bonds #status predicted SUMMARY #length 104 #molecular-weight 12359 #checksum 4508 SEQUENCE /// ENTRY GERTM1 #type complete TITLE matrix Gla protein precursor - rat ALTERNATE_NAMES MGP ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 08-Nov-1991 #sequence_revision 25-Apr-1997 #text_change 22-Jun-1999 ACCESSIONS A39974 REFERENCE A39974 !$#authors Price, P.A.; Fraser, J.D.; Metz-Virca, G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:8335-8339 !$#title Molecular cloning of matrix Gla protein: implications for !1substrate recognition by the vitamin K-dependent !1gamma-carboxylase. !$#cross-references MUID:88068589; PMID:3317405 !$#accession A39974 !'##molecule_type mRNA !'##residues 1-103 ##label PRI !'##cross-references GB:J03026; NID:g205405; PIDN:AAA41597.1; !1PID:g205406 REFERENCE A58570 !$#authors Price, P.A.; Rice, J.S.; Williamson, M.K. !$#journal Protein Sci. (1994) 3:822-830 !$#title Conserved phosphorylation of serines in the Ser-X-Glu/Ser(P) !1sequences of the vitamin K-dependent matrix Gla protein from !1shark, lamb, rat, cow, and human. !$#cross-references MUID:94339842; PMID:8061611 !$#contents annotation; sequence; identification of phosphoserine and !1carboxyglutamic acid in amino-terminal peptide COMMENT This vitamin K-dependent calcium binding protein is secreted !1by most known cell types, but is deposited only in bone, !1cartilage and dentine. During bone development it is !1deposited earlier than osteocalcin. CLASSIFICATION #superfamily osteocalcin KEYWORDS bone; calcium binding; carboxyglutamic acid; cartilage; !1phosphoprotein; vitamin K FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-103 #product matrix Gla protein #status predicted #label !8MAT\ !$21 #modified_site gamma-carboxyglutamic acid (Glu) !8#status experimental\ !$22,25,28 #binding_site phosphate (Ser) (covalent) (by casein !8kinase II) #status experimental\ !$56,60,67,71 #modified_site gamma-carboxyglutamic acid (Glu) !8#status predicted\ !$73-79 #disulfide_bonds #status predicted SUMMARY #length 103 #molecular-weight 12050 #checksum 9283 SEQUENCE /// ENTRY GERBM1 #type complete TITLE matrix Gla protein precursor - rabbit ALTERNATE_NAMES MGP ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 22-Apr-1995 #sequence_revision 25-Apr-1997 #text_change 22-Jun-1999 ACCESSIONS JX0354; PC2379 REFERENCE JX0354 !$#authors Sohma, Y.; Suzuki, T.; Sasano, H.; Nagura, H.; Nose, M.; !1Yamamoto, T. !$#journal J. Biochem. (1994) 116:747-751 !$#title Expression of mRNA for matrix gamma-carboxyglutamic acid !1protein during progression of atherosclerosis in aortae of !1Watanabe heritable hyperlipidemic rabbits. !$#cross-references MUID:95189771; PMID:7883748 !$#accession JX0354 !'##molecule_type mRNA !'##residues 1-103 ##label SOH !'##cross-references DDBJ:D21265; NID:g624912; PIDN:BAA04805.1; !1PID:g624913 COMMENT This vitamin K-dependent calcium binding protein is secreted !1by most known cell types, but is deposited only in bone, !1cartilage and dentine. During bone development it is !1deposited earlier than osteocalcin. CLASSIFICATION #superfamily osteocalcin KEYWORDS bone; calcium binding; carboxyglutamic acid; cartilage; !1phosphoprotein; vitamin K FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-103 #product matrix Gla protein #status predicted #label !8MAT\ !$21,56,60,67,71 #modified_site gamma-carboxyglutamic acid (Glu) !8#status predicted\ !$22,25,28 #binding_site phosphate (Ser) (covalent) (by casein !8kinase II) #status predicted\ !$73-79 #disulfide_bonds #status predicted SUMMARY #length 103 #molecular-weight 12441 #checksum 199 SEQUENCE /// ENTRY S09575 #type complete TITLE osteopontin precursor, splice form A - human ALTERNATE_NAMES bone sialoprotein I; lactopontin; milk protein, 75K; secreted phosphoprotein I; urinary stone protein; uropontin CONTAINS osteopontin, splice form B; osteopontin, splice form C ORGANISM #formal_name Homo sapiens #common_name man DATE 20-May-1994 #sequence_revision 27-Jun-1994 #text_change 16-Jun-2000 ACCESSIONS S50028; S09575; A35326; JQ1529; I56986; I76601; I76602; !1A41802; S04505 REFERENCE S50028 !$#authors Hijiya, N.; Setoguchi, M.; Matsuura, K.; Higuchi, Y.; !1Akizuki, S.; Yamamoto, S. !$#journal Biochem. J. (1994) 303:255-262 !$#title Cloning and characterization of the human osteopontin gene !1and its promoter. !$#cross-references MUID:95031968; PMID:7945249 !$#accession S50028 !'##status preliminary !'##molecule_type DNA !'##residues 1-314 ##label HIJ !'##cross-references EMBL:D14813; NID:g506341; PIDN:BAA03554.1; !1PID:g506342 !'##note the authors translated the codon GTG for residue 5 as Tyr REFERENCE S09575 !$#authors Kiefer, M.C.; Bauer, D.M.; Barr, P.J. !$#journal Nucleic Acids Res. (1989) 17:3306 !$#title The cDNA and derived amino acid sequence for human !1osteopontin. !$#cross-references MUID:89263749; PMID:2726470 !$#accession S09575 !'##molecule_type mRNA !'##residues 1-314 ##label KIE !'##cross-references EMBL:X13694; NID:g35147; PIDN:CAA31984.1; !1PID:g35148 REFERENCE A35326 !$#authors Young, M.F.; Kerr, J.M.; Termine, J.D.; Wewer, U.M.; Ge !1Wang, M.; McBride, O.W.; Fisher, L.W. !$#journal Genomics (1990) 7:491-502 !$#title cDNA cloning, mRNA distribution and heterogeneity, !1chromosomal location, and RFLP analysis of human osteopontin !1(OPN). !$#cross-references MUID:90353945; PMID:1974876 !$#accession A35326 !'##molecule_type mRNA !'##residues 1-58,73-314 ##label YOU !'##cross-references GB:J04765; NID:g189404; PIDN:AAA59974.1; !1PID:g189405 REFERENCE JQ1529 !$#authors Kohri, K.; Suzuki, Y.; Yoshida, K.; Yamamoto, K.; Amasaki, !1N.; Yamate, T.; Umekawa, T.; Iguchi, M.; Sinohara, H.; !1Kurita, T. !$#journal Biochem. Biophys. Res. Commun. (1992) 184:859-864 !$#title Molecular cloning and sequencing of cDNA encoding urinary !1stone protein, which is identical to osteopontin. !$#cross-references MUID:92246977; PMID:1575754 !$#accession JQ1529 !'##status translation not shown !'##molecule_type mRNA !'##residues 67-273 ##label KOH !'##experimental_source kidney REFERENCE I56986 !$#authors Saitoh, Y.; Kuratsu, J.; Takeshima, H.; Yamamoto, S.; Ushio, !1Y. !$#journal Lab. Invest. (1995) 72:55-63 !$#title Expression of osteopontin in human glioma. Its correlation !1with the malignancy. !$#cross-references MUID:95139605; PMID:7837791 !$#accession I56986 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-187,'H',189-236,'A',238-314 ##label SAI1 !'##cross-references GB:D28759; NID:g633074; PIDN:BAA05949.1; !1PID:g992948 !$#accession I76601 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-57,72-187,'H',189-236,'A',238-314 ##label SAI2 !'##cross-references GB:D28760; NID:g633075; PIDN:BAA05950.1; !1PID:g992949 !$#accession I76602 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-31,59-187,'H',189-236,'A',238-314 ##label SAI3 !'##cross-references GB:D28761; NID:g633076; PIDN:BAA05951.1; !1PID:g992950 REFERENCE A41802 !$#authors Shiraga, H.; Min, W.; VanDusen, W.J.; Clayman, M.D.; Miner, !1D.; Terrell, C.H.; Sherbotie, J.R.; Foreman, J.W.; !1Przysiecki, C.; Neilson, E.G.; Hoyer, J.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:426-430 !$#title Inhibition of calcium oxalate crystal growth in vitro by !1uropontin: another member of the aspartic acid-rich protein !1superfamily. !$#cross-references MUID:92108068; PMID:1729712 !$#accession A41802 !'##molecule_type protein !'##residues 19-62 ##label SHI REFERENCE S04505 !$#authors Senger, D.R.; Perruzzi, C.A.; Papadopoulos, A.; Tenen, D.G. !$#journal Biochim. Biophys. Acta (1989) 996:43-48 !$#title Purification of a human milk protein closely similar to !1tumor-secreted phosphoproteins and osteopontin. !$#cross-references MUID:89287357; PMID:2736258 !$#accession S04505 !'##status preliminary !'##molecule_type protein !'##residues 17-23;169-182 ##label SEN COMMENT This protein is an acidic glycoprotein rich in aspartic !1acid, glutamic acid, and serine and is the major inhibitor !1of precipitation of calcium salts, especially calcium !1oxalate. GENETICS !$#gene GDB:SPP1; BNSP; OPN !'##cross-references GDB:118889; OMIM:166490 !$#map_position 4q21-4q25 CLASSIFICATION #superfamily osteopontin KEYWORDS alternative splicing; bone; cell binding; extracellular !1matrix; phosphoprotein; sialoglycoprotein FEATURE !$1-314 #product osteopontin precursor, splice form A #status !8predicted #label PRA\ !$1-57,72-314 #product osteopontin precursor, splice form B #status !8predicted #label PRB\ !$1-31,59-314 #product osteopontin precursor, splice form C #status !8predicted #label PRC\ !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-314 #product osteopontin #status predicted #label MAT\ !$86-95 #region aspartic acid-rich\ !$159-161 #region cell attachment (R-G-D) motif\ !$24,26,27,62,63,191, !$195,234,303,308,310 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$79,106 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$185 #binding_site phosphate (Thr) (covalent) #status !8predicted SUMMARY #length 314 #molecular-weight 35422 #checksum 2944 SEQUENCE /// ENTRY GEPGO #type complete TITLE osteopontin precursor - pig ALTERNATE_NAMES bone sialoprotein I; phosphoprotein I, secreted CONTAINS 20K glycoprotein; 23K glycoprotein ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 10-Sep-1999 ACCESSIONS S14903; A35204; S24372; S06690 REFERENCE S14903 !$#authors Wrana, J.L.; Zhang, Q.; Sodek, J. !$#journal Nucleic Acids Res. (1989) 17:10119 !$#title Full length cDNA sequence of porcine secreted !1phosphoprotein-I (SPP-I, osteopontin). !$#cross-references MUID:90098793; PMID:2602123 !$#accession S14903 !'##molecule_type mRNA !'##residues 1-303 ##label WRA !'##cross-references EMBL:X16575; NID:g2120; PIDN:CAA34594.1; PID:g2121 REFERENCE A35204 !$#authors Zhang, Q.; Domenicucci, C.; Goldberg, H.A.; Wrana, J.L.; !1Sodek, J. !$#journal J. Biol. Chem. (1990) 265:7583-7589 !$#title Characterization of fetal porcine bone sialoproteins, !1secreted phosphoprotein I (SPPI, osteopontin), bone !1sialoprotein, and a 23-kDa glycoprotein. Demonstration that !1the 23-kDa glycoprotein is derived from the carboxyl !1terminus of SPPI. !$#cross-references MUID:90237064; PMID:2332443 !$#accession A35204 !'##molecule_type protein !'##residues 17-36;172-211 ##label ZHA REFERENCE S24372 !$#authors Zhang, Q.; Wrana, J.L.; Sodek, J. !$#journal Eur. J. Biochem. (1992) 207:649-659 !$#title Characterization of the promoter region of the porcine opn !1(osteopontin, secreted phosphoprotein 1) gene. !1Identification of positive and negative regulatory elements !1and a 'silent' second promoter. !$#cross-references MUID:92339454; PMID:1633816 !$#accession S24372 !'##molecule_type DNA !'##residues 1-18 ##label ZH2 !'##cross-references EMBL:M84121; NID:g164599; PIDN:AAA31094.1; !1PID:g164600 COMMENT This protein is an acidic glycoprotein rich in aspartic !1acid, glutamic acid, and serine and is the major inhibitor !1of precipitation of calcium salts, especially calcium !1oxalate. CLASSIFICATION #superfamily osteopontin KEYWORDS bone; cell binding; extracellular matrix; phosphoprotein; !1sialoglycoprotein FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-303 #product osteopontin #status experimental #label MAT\ !$86-93 #region aspartic acid-rich\ !$154-156 #region cell attachment (R-G-D) motif\ !$172-303 #product 23K glycoprotein #status experimental #label !823K\ !$199-303 #product 20K glycoprotein #status experimental #label !820K\ !$79 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 303 #molecular-weight 33668 #checksum 9444 SEQUENCE /// ENTRY JC1191 #type complete TITLE osteopontin precursor - rabbit ALTERNATE_NAMES bone sialoprotein I; secreted phosphoprotein I ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jun-2000 ACCESSIONS JC1191; S54977; S54976 REFERENCE JC1191 !$#authors Tezuka, K.; Sato, T.; Kamioka, H.; Nijweide, P.J.; Tanaka, !1K.; Matsuo, T.; Ohta, M.; Kurihara, N.; Hakeda, Y.; !1Kumegawa, M. !$#journal Biochem. Biophys. Res. Commun. (1992) 186:911-917 !$#title Identification of osteopontin in isolated rabbit !1osteoclasts. !$#cross-references MUID:92360044; PMID:1379809 !$#accession JC1191 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-311 ##label TEZ !'##cross-references DDBJ:D11411; NID:g217735; PIDN:BAA01993.1; !1PID:g217736 !'##note the authors translated the codon TCT for residue 126 as Glu and !1GAC for residue 185 as Ser REFERENCE S54977 !$#authors Nasu, K.; Ishida, T.; Setoguchi, M.; Higuchi, Y.; Akizuki, !1S.; Yamamoto, S. !$#journal Biochem. J. (1995) 307:257-265 !$#title Expression of wild-type and mutated rabbit osteopontin in !1Escherichia coli, and their effects on adhesion and !1migration of P388D1 cells. !$#cross-references MUID:95234045; PMID:7717985 !$#accession S54977 !'##status preliminary; nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 78-84,'V',86-99,'Q',101-128,'SDE',129-150,'I',152-166 !1##label NAS !'##cross-references EMBL:D16544 REFERENCE S54976 !$#authors Nasu, K.; Ishida, T.; Hijiya, N.; Setoguchi, M.; Akizuki, !1S.; Higuchi, Y.; Yamamoto, S. !$#submission submitted to the EMBL Data Library, September 1994 !$#description Molecular cloning of rabbit osteopontin cDNA and its !1expression. !$#accession S54976 !'##status preliminary !'##molecule_type mRNA !'##residues 1-84,'V',86-99,'Q',101-128,'SDE',129-150,'I',152-311 !1##label NA2 !'##cross-references EMBL:D16544; NID:g538244; PIDN:BAA03980.1; !1PID:g538245 COMMENT This protein is an acidic glycoprotein rich in aspartic !1acid, glutamic acid, and serine and is the major inhibitor !1of precipitation of calcium salts, especially calcium !1oxalate. GENETICS !$#gene OC-1 CLASSIFICATION #superfamily osteopontin KEYWORDS bone; cell binding; extracellular matrix; phosphoprotein; !1sialoglycoprotein FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-311 #product osteopontin #status predicted #label MAT\ !$86-95 #region aspartic acid-rich\ !$155-157 #region cell attachment (R-G-D) motif\ !$103 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 311 #molecular-weight 35172 #checksum 5959 SEQUENCE /// ENTRY JS0638 #type complete TITLE osteopontin precursor - bovine ALTERNATE_NAMES bone sialoprotein I; phosphoprotein I, secreted ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Jun-1992 #sequence_revision 27-Jun-1994 #text_change 10-Sep-1999 ACCESSIONS JS0638; PC2024; PQ0160 REFERENCE JS0638 !$#authors Kerr, J.M.; Fisher, L.W.; Termine, J.D.; Young, M.F. !$#journal Gene (1991) 108:237-243 !$#title The cDNA cloning and RNA distribution of bovine osteopontin. !$#cross-references MUID:92084141; PMID:1721033 !$#accession JS0638 !'##molecule_type mRNA !'##residues 1-278 ##label KER !'##cross-references GB:M66236 !'##note the authors translated the codon CGG for residue 221 as Ala REFERENCE JC2050 !$#authors Sorensen, E.S.; Petersen, T.E. !$#journal Biochem. Biophys. Res. Commun. (1994) 198:200-205 !$#title Identification of two phosphorylation motifs in bovine !1osteopontin. !$#cross-references MUID:94121631; PMID:8292023 !$#accession PC2024 !'##molecule_type protein !'##residues 17-30;36-55,'A',57-70;153-161;167-215;250-278 ##label SOR REFERENCE PQ0160 !$#authors Prince, C.W.; Dickie, D.; Krumdieck, C.L. !$#journal Biochem. Biophys. Res. Commun. (1991) 177:1205-1210 !$#title Osteopontin, a substrate for transglutaminase and factor !1XIII activity. !$#cross-references MUID:91282766; PMID:1676261 !$#accession PQ0160 !'##molecule_type protein !'##residues 17-21,'LTF' ##label PRI !'##experimental_source bone !'##note 22-Thr and 23-Ser were also found COMMENT This protein is an acidic glycoprotein rich in aspartic !1acid, glutamic acid, and serine and is the major inhibitor !1of precipitation of calcium salts, especially calcium !1oxalate. COMMENT This protein is thought to anchor osteoclasts to bone. CLASSIFICATION #superfamily osteopontin KEYWORDS bone; cell binding; extracellular matrix; phosphoprotein; !1sialoglycoprotein FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-278 #product osteopontin #status experimental #label MAT\ !$86-93 #region aspartic acid-rich\ !$152-154 #region cell attachment (R-G-D) motif\ !$23,24,26,27,60,62, !$63,184,188,205,210, !$267,272,274 #binding_site phosphate (Ser) (covalent) #status !8experimental\ !$79 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$178 #binding_site phosphate (Thr) (covalent) #status !8experimental SUMMARY #length 278 #molecular-weight 31031 #checksum 159 SEQUENCE /// ENTRY A37818 #type complete TITLE osteopontin precursor - mouse ALTERNATE_NAMES bone sialoprotein I; early T lymphocyte activation 1 protein; phosphoprotein I, secreted ORGANISM #formal_name Mus musculus #common_name house mouse DATE 12-Feb-1993 #sequence_revision 27-Jun-1994 #text_change 10-Sep-1999 ACCESSIONS A37818; S04078; S12064; A33853; JL0105; A60931; S11677 REFERENCE A37818 !$#authors Miyazaki, Y.; Setoguchi, M.; Yoshida, S.; Higuchi, Y.; !1Akizuki, S.; Yamamoto, S. !$#journal J. Biol. Chem. (1990) 265:14432-14438 !$#title The mouse osteopontin gene. Expression in monocytic lineages !1and complete nucleotide sequence. !$#cross-references MUID:90354433; PMID:2387863 !$#accession A37818 !'##molecule_type DNA !'##residues 1-294 ##label MIY !'##cross-references EMBL:X51834 REFERENCE S04078 !$#authors Miyazaki, Y.; Setoguchi, M.; Yoshida, S.; Higuchi, Y.; !1Akizuki, S.; Yamamoto, S. !$#journal Nucleic Acids Res. (1989) 17:3298 !$#title Nucleotide sequence of cDNA for mouse osteopontin-like !1protein. !$#cross-references MUID:89263742; PMID:2726465 !$#accession S04078 !'##molecule_type mRNA !'##residues 1-294 ##label MI2 !'##cross-references EMBL:X13986; NID:g53755; PIDN:CAA32165.1; !1PID:g53756 REFERENCE S12064 !$#authors Yamamoto, S. !$#submission submitted to the EMBL Data Library, January 1990 !$#accession S12064 !'##molecule_type DNA !'##residues 1-121,'F',123-294 ##label YAM !'##cross-references EMBL:X51834; NID:g53520; PIDN:CAA36132.1; !1PID:g297546 REFERENCE A33853 !$#authors Craig, A.M.; Smith, J.H.; Denhardt, D.T. !$#journal J. Biol. Chem. (1989) 264:9682-9689 !$#title Osteopontin, a transformation-associated cell adhesion !1phosphoprotein, is induced by 12-O-tetradecanoylphorbol !113-acetate in mouse epidermis. !$#cross-references MUID:89255479; PMID:2722855 !$#accession A33853 !'##molecule_type mRNA !'##residues 1-98,'G',100-294 ##label CRA !'##cross-references GB:J04806; NID:g200157; PIDN:AAA57265.1; !1PID:g200158 REFERENCE JL0105 !$#authors Patarca, R.; Freeman, G.J.; Singh, R.P.; Wei, F.Y.; Durfee, !1T.; Blattner, F.; Regnier, D.C.; Kozak, C.A.; Mock, B.A.; !1Morse III, H.C.; Jerrells, T.R.; Cantor, H. !$#journal J. Exp. Med. (1989) 170:145-161 !$#title Structural and functional studies of the early T lymphocyte !1activation 1 (Eta-1) gene. Definition of a novel T !1cell-dependent response associated with genetic resistance !1to bacterial infection. !$#cross-references MUID:89310352; PMID:2787378 !$#accession JL0105 !'##molecule_type mRNA !'##residues 1-42,'P',44-294 ##label PAT !'##cross-references EMBL:X16151; NID:g50863; PIDN:CAA34276.1; !1PID:g50864 REFERENCE A60931 !$#authors Singh, R.P.; Patarca, R.; Schwartz, J.; Singh, P.; Cantor, !1H. !$#journal J. Exp. Med. (1990) 171:1931-1942 !$#title Definition of a specific interaction between the early T !1lymphocyte activation 1 (Eta-1) protein and murine !1macrophages in vitro and its effect upon macrophages in !1vivo. !$#cross-references MUID:90278349; PMID:2351930 !$#accession A60931 !'##molecule_type protein !'##residues 158-176 ##label SIN COMMENT This protein is an acidic glycoprotein rich in aspartic !1acid, glutamic acid, and serine and is the major inhibitor !1of precipitation of calcium salts, especially calcium !1oxalate. GENETICS !$#gene Eta-1 !$#map_position 5 !$#introns 18/3; 30/3; 57/3; 71/3; 165/3 CLASSIFICATION #superfamily osteopontin KEYWORDS bone; cell binding; extracellular matrix; phosphoprotein; !1sialoglycoprotein FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-294 #product osteopontin #status predicted #label MAT\ !$85-96 #region aspartic acid-rich\ !$144-146 #region cell attachment (R-G-D) motif\ !$78 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 294 #molecular-weight 32459 #checksum 929 SEQUENCE /// ENTRY A25917 #type complete TITLE osteopontin precursor - rat ALTERNATE_NAMES bone sialoprotein I; phosphoprotein I, secreted; tumor-secreted phosphoprotein ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 18-Dec-1987 #sequence_revision 27-Jun-1994 #text_change 10-Sep-1999 ACCESSIONS A25917; A45132; B45132; S28772; S04506; A45925 REFERENCE A25917 !$#authors Oldberg, A.; Franzen, A.; Heinegard, D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:8819-8823 !$#title Cloning and sequence analysis of rat bone sialoprotein !1(osteopontin) cDNA reveals an Arg-Gly-Asp cell-binding !1sequence. !$#cross-references MUID:87067405; PMID:3024151 !$#accession A25917 !'##molecule_type mRNA !'##residues 1-317 ##label OLD !'##cross-references GB:M14656; NID:g205859; PIDN:AAA41762.1; !1PID:g205860 REFERENCE A45132 !$#authors Singh, K.; Mukherjee, A.B.; De Vouge, M.W.; Mukherjee, B.B. !$#journal J. Biol. Chem. (1992) 267:23847-23851 !$#title Differential processing of osteopontin transcripts in rat !1kidney- and osteoblast-derived cell lines. !$#cross-references MUID:93054745; PMID:1429723 !$#accession A45132 !'##molecule_type protein !'##residues 36-51 ##label SIN1 !'##experimental_source kidney !'##note sequence extracted from NCBI backbone (NCBIP:118869) !$#accession B45132 !'##molecule_type protein !'##residues 272-282 ##label SIN2 !'##note sequence extracted from NCBI backbone (NCBIP:118871) REFERENCE S28772 !$#authors Prince, C.W.; Oosawa, T.; Butler, W.T.; Tomana, M.; Bhown, !1A.S.; Bhown, M.; Schrohenloher, R.E. !$#journal J. Biol. Chem. (1987) 262:2900-2907 !$#title Isolation, characterization, and biosynthesis of a !1phosphorylated glycoprotein from rat bone. !$#cross-references MUID:87137549; PMID:3469201 !$#accession S28772 !'##status preliminary !'##molecule_type protein !'##residues 17-26,'X' ##label PRI REFERENCE S04505 !$#authors Senger, D.R.; Perruzzi, C.A.; Papadopoulos, A.; Tenen, D.G. !$#journal Biochim. Biophys. Acta (1989) 996:43-48 !$#title Purification of a human milk protein closely similar to !1tumor-secreted phosphoproteins and osteopontin. !$#cross-references MUID:89287357; PMID:2736258 !$#accession S04506 !'##status preliminary !'##molecule_type protein !'##residues 17-26;155-167 ##label SEN REFERENCE A45925 !$#authors Senger, D.R.; Perruzzi, C.A.; Gracey, C.F.; Papadopoulos, !1A.; Tenen, D.G. !$#journal Cancer Res. (1988) 48:5770-5774 !$#title Secreted phosphoproteins associated with neoplastic !1transformation: close homology with plasma proteins cleaved !1during blood coagulation. !$#cross-references MUID:89002730; PMID:3167835 !$#accession A45925 !'##molecule_type protein !'##residues 17-25 ##label SE2 COMMENT This protein is an acidic glycoprotein rich in aspartic !1acid, glutamic acid, and serine and is the major inhibitor !1of precipitation of calcium salts, especially calcium !1oxalate. CLASSIFICATION #superfamily osteopontin KEYWORDS bone; cell binding; extracellular matrix; phosphoprotein; !1sialoglycoprotein FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-317 #product osteopontin #status predicted #label MAT\ !$86-96 #region aspartic acid-rich\ !$144-146 #region cell attachment (R-G-D) motif\ !$79 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 317 #molecular-weight 34929 #checksum 5754 SEQUENCE /// ENTRY A40019 #type complete TITLE osteopontin precursor - chicken ALTERNATE_NAMES bone sialoprotein I; phosphoprotein I, secreted ORGANISM #formal_name Gallus gallus #common_name chicken DATE 20-Mar-1992 #sequence_revision 15-Aug-1997 #text_change 21-Jul-2000 ACCESSIONS I51384; A40019; A37962; S16462 REFERENCE I51384 !$#authors Rafidi, K.; Simikina, I.; Johnson, E.; Moore, M.A.; !1Gerstenfeld, L.C. !$#journal Gene (1994) 140:163-169 !$#title Characterization of the chicken osteopontin-encoding gene. !$#cross-references MUID:94192994; PMID:8144023 !$#accession I51384 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-264 ##label RAF !'##cross-references EMBL:U01844; NID:g404635; PIDN:AAA18584.1; !1PID:g404636 REFERENCE A40019 !$#authors Castagnola, P.; Bet, P.; Quarto, R.; Gennari, M.; Cancedda, !1R. !$#journal J. Biol. Chem. (1991) 266:9944-9949 !$#title cDNA cloning and gene expression of chicken osteopontin. !1Expression of osteopontin mRNA in chondrocytes is enhanced !1by trypsin treatment of cells. !$#cross-references MUID:91236779; PMID:2033080 !$#accession A40019 !'##molecule_type mRNA !'##residues 1-215,'D',217-234,'A',236-239,'A',241-264 ##label CAS !'##cross-references GB:X56772; NID:g58344; PIDN:CAA40091.1; !1PID:g4493384 REFERENCE A37962 !$#authors Moore, M.A.; Gotoh, Y.; Rafidi, K.; Gerstenfeld, L.C. !$#journal Biochemistry (1991) 30:2501-2508 !$#title Characterization of a cDNA for chicken osteopontin: !1expression during bone development, osteoblast !1differentiation, and tissue distribution. !$#cross-references MUID:91159433; PMID:2001376 !$#accession A37962 !'##molecule_type mRNA !'##residues 1-103,'G',105-264 ##label MOO !'##cross-references GB:M59182; GB:J05323; NID:g211276; PIDN:AAA62729.1; !1PID:g211277 COMMENT This protein is an acidic glycoprotein rich in aspartic !1acid, glutamic acid, and serine and is the major inhibitor !1of precipitation of calcium salts, especially calcium !1oxalate. GENETICS !$#introns 18/3; 35/3; 70/3; 85/3; 164/3 CLASSIFICATION #superfamily osteopontin KEYWORDS bone; cell binding; extracellular matrix; phosphoprotein; !1sialoglycoprotein FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-264 #product osteopontin #status predicted #label MAT\ !$100-106 #region aspartic acid-rich\ !$138-140 #region cell attachment (R-G-D) motif\ !$106,109,204,242 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 264 #molecular-weight 29162 #checksum 8806 SEQUENCE /// ENTRY GEHUS #type complete TITLE bone sialoprotein precursor [validated] - human ALTERNATE_NAMES bone sialoprotein II; cell-binding sialoprotein ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 08-Dec-2000 ACCESSIONS A35043; D28457; A47217; S42619 REFERENCE A35043 !$#authors Fisher, L.W.; McBride, O.W.; Termine, J.D.; Young, M.F. !$#journal J. Biol. Chem. (1990) 265:2347-2351 !$#title Human bone sialoprotein. Deduced protein sequence and !1chromosomal localization. !$#cross-references MUID:90130496; PMID:2404984 !$#accession A35043 !'##molecule_type mRNA !'##residues 1-317 ##label FIS !'##cross-references GB:J05213; NID:g338083; PIDN:AAC95490.1; !1PID:g338084 REFERENCE A92656 !$#authors Fisher, L.W.; Hawkins, G.R.; Tuross, N.; Termine, J.D. !$#journal J. Biol. Chem. (1987) 262:9702-9708 !$#title Purification and partial characterization of small !1proteoglycans I and II, bone sialoproteins I and II, and !1osteonectin from the mineral compartment of developing human !1bone. !$#cross-references MUID:87250639; PMID:3597437 !$#accession D28457 !'##molecule_type protein !'##residues 17-41,'X',43-45,'X',47,'X',49-51,'X',53,'X',55 ##label FI2 REFERENCE A47217 !$#authors Kerr, J.M.; Fisher, L.W.; Termine, J.D.; Wang, M.G.; !1McBride, O.W.; Young, M.F. !$#journal Genomics (1993) 17:408-415 !$#title The human bone sialoprotein gene (IBSP): genomic !1localization and characterization. !$#cross-references MUID:94010937; PMID:8406493 !$#accession A47217 !'##molecule_type DNA !'##residues 1-194,'V',196-267,'A',269,'D',271-317 ##label KER !'##cross-references GB:L09554 REFERENCE S42619 !$#authors Kim, R.H.; Shapiro, H.S.; Li, J.J.; Wrana, J.L.; Sodek, J. !$#journal Matrix Biol. (1994) 14:31-40 !$#title Characterization of the human bone sialoprotein (BSP) gene !1and its promoter sequence. !$#cross-references MUID:94340202; PMID:8061918 !$#accession S42619 !'##molecule_type DNA !'##residues 1-93,'L',95-108,110-194,'E',196-215,'G',217-218,'R', !1220-267,'A',269,'D',271-302,'E',304-317 ##label KIM GENETICS !$#gene GDB:IBSP !'##cross-references GDB:138129; OMIM:147563 !$#map_position 4q28-4q31 CLASSIFICATION #superfamily bone sialoprotein KEYWORDS bone; cell adhesion; hydroxyapatite binding; !1sialoglycoprotein; sulfoprotein FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-317 #product bone sialoprotein #status experimental !8#label MAT\ !$286-288 #region cell attachment (R-G-D) motif\ !$104,177,182,190 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$259,263,265,271, !$275,278,293,297 #binding_site sulfate (Tyr) (covalent) #status !8predicted SUMMARY #length 317 #molecular-weight 35018 #checksum 6703 SEQUENCE /// ENTRY GERTS #type complete TITLE bone sialoprotein precursor - rat ALTERNATE_NAMES bone sialoprotein II; cell-binding sialoprotein ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 22-Jun-1999 ACCESSIONS A30058; A61207 REFERENCE A30058 !$#authors Oldberg, A.; Franzen, A.; Heinegard, D. !$#journal J. Biol. Chem. (1988) 263:19430-19432 !$#title The primary structure of a cell-binding bone sialoprotein. !$#cross-references MUID:89066760; PMID:3198635 !$#accession A30058 !'##molecule_type mRNA !'##residues 1-320 ##label OLD !'##cross-references EMBL:J04215; NID:g205861; PIDN:AAA41763.1; !1PID:g205862 REFERENCE A61207 !$#authors Chopra, R.K.; Anastassiades, T.P.; Lohnes, D.; Jones, G. !$#journal Biochem. Cell Biol. (1991) 69:523-530 !$#title Further purification and characterization of newly !1synthesized anionic glycoconjugates secreted by cultured !1UMR-106 cells: evidence that the major anionic !1glycoconjugate secreted by these cells is similar to bone !1sialoprotein II. !$#cross-references MUID:92102651; PMID:1760156 !$#accession A61207 !'##molecule_type protein !'##residues 17-22 ##label CHO COMMENT This protein contains about 50% carbohydrate, both N- and !1O-linked. CLASSIFICATION #superfamily bone sialoprotein KEYWORDS bone; cell adhesion; hydroxyapatite binding; !1sialoglycoprotein; sulfoprotein FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-320 #product bone sialoprotein #status experimental !8#label MAT\ !$289-291 #region cell attachment (R-G-D) motif\ !$108,180,185 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$263,267,274,278, !$281,296,300,308, !$311,316 #binding_site sulfate (Tyr) (covalent) #status !8predicted SUMMARY #length 320 #molecular-weight 35251 #checksum 9104 SEQUENCE /// ENTRY A35175 #type complete TITLE mucin 1 precursor, repetitive splice form A [validated] - human ALTERNATE_NAMES breast carcinoma-associated DF3 antigen; core protein KP39; episialin; epithelial tumor antigen precursor, membrane-bound splice form; H23 antigen; MUC1 protein; NCRC11 antigen; pancreatic mucin; polymorphic epithelial mucin (PEM) CONTAINS mucin 1 precursor, epithelial tumor antigen splice form; mucin 1 precursor, splice form B ORGANISM #formal_name Homo sapiens #common_name man DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 02-Jun-2000 ACCESSIONS A35175; B35175; A35886; A35887; S10572; S40293; A36735; !1PX0066; S10218; S51026 REFERENCE A35175 !$#authors Ligtenberg, M.J.L.; Vos, H.L.; Gennissen, A.M.C.; Hilkens, !1J. !$#journal J. Biol. Chem. (1990) 265:5573-5578 !$#title Episialin, a carcinoma-associated mucin, is generated by a !1polymorphic gene encoding splice variants with alternative !1amino termini. !$#cross-references MUID:90202794; PMID:2318825 !$#accession A35175 !'##molecule_type mRNA !'##residues 1-952,1033-1344 ##label LIG1 !'##cross-references GB:M32738; GB:J05288; NID:g182121; PIDN:AAA35804.1; !1PID:g182124; GB:M34088; NID:g182122; PIDN:AAA35805.1; !1PID:g182125 !'##experimental_source splice form A !'##note GenBank entries HUMEPISIA1 and HUMEPISIA2 present only the !1amino-and carboxyl-ends of the translation !$#accession B35175 !'##molecule_type mRNA !'##residues 1-19,29-952,1033-1344 ##label LIG2 !'##cross-references GB:M32739; GB:J05288; NID:g182126; PIDN:AAA35806.1; !1PID:g182129; GB:M34089; NID:g182127; PIDN:AAA35807.1; !1PID:g182130 !'##experimental_source splice form B !'##note GenBank entries HUMEPISIB1 and HUMEPISIB2 present only the !1amino-and carboxyl-ends of the translation REFERENCE A35886 !$#authors Gendler, S.J.; Lancaster, C.A.; Taylor-Papadimitriou, J.; !1Duhig, T.; Peat, N.; Burchell, J.; Pemberton, L.; Lalani, !1E.N.; Wilson, D. !$#journal J. Biol. Chem. (1990) 265:15286-15293 !$#title Molecular cloning and expression of human tumor-associated !1polymorphic epithelial mucin. !$#cross-references MUID:90368715; PMID:1697589 !$#accession A35886 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-19,29-992,1033-1344 ##label GEN !'##cross-references GB:J05581; NID:g188869; PIDN:AAA59876.1; !1PID:g188870 !'##note GenBank entry HUMMUCAB includes one copy of the tandemly !1repeated sequence REFERENCE A35887 !$#authors Lan, M.S.; Batra, S.K.; Qi, W.N.; Metzgar, R.S.; !1Hollingsworth, M.A. !$#journal J. Biol. Chem. (1990) 265:15294-15299 !$#title Cloning and sequencing of a human pancreatic tumor mucin !1cDNA. !$#cross-references MUID:90368716; PMID:2394722 !$#accession A35887 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-19,29-1109,'S',1111-1339,'A',1341-1344 ##label LAN !'##cross-references GB:J05582; NID:g189598; PIDN:AAA60019.1; !1PID:g189599 !'##note GenBank entry HUMPANMU contains four fewer copies of the !1tandemly repeated sequence REFERENCE S10571 !$#authors Wreschner, D.H.; Hareuveni, M.; Tsarfaty, I.; Smorodinsky, !1N.; Horev, J.; Zaretsky, J.; Kotkes, P.; Weiss, M.; Lathe, !1R.; Dion, A.; Keydar, I. !$#journal Eur. J. Biochem. (1990) 189:463-473 !$#title Human epithelial tumor antigen cDNA sequences. Differential !1splicing may generate multiple protein forms. !$#cross-references MUID:90276413; PMID:2351132 !$#accession S10572 !'##molecule_type mRNA !'##residues 1-19,29-155,'P',157-175,'P',177-182,'A',184-212,1033-1344 !1##label WRE !'##cross-references EMBL:X52229; NID:g37053 REFERENCE S40293 !$#authors Wreschner, D.H. !$#submission submitted to the EMBL Data Library, March 1990 !$#accession S40293 !'##molecule_type mRNA !'##residues 1-19,29-155,'P',157-175,'P',177-182,'A',184-212,1033-1037, !1'A',1039-1344 ##label WR2 !'##cross-references EMBL:X52229; NID:g37053; PIDN:CAA36478.1; !1PID:g37054 REFERENCE A36735 !$#authors Abe, M.; Siddiqui, J.; Kufe, D. !$#journal Biochem. Biophys. Res. Commun. (1989) 165:644-649 !$#title Sequence analysis of the 5' region of the human DF3 breast !1carcinoma-associated antigen gene. !$#cross-references MUID:90088473; PMID:2597151 !$#accession A36735 !'##molecule_type mRNA !'##residues 1-142,'Q',144-162,'Q',164-168 ##label ABE !'##cross-references EMBL:M31823; NID:g181542; PIDN:AAA35757.1; !1PID:g181543 REFERENCE JX0235 !$#authors Masuzawa, Y.; Miyauchi, T.; Hamanoue, M.; Ando, S.; Yoshida, !1J.; Takao, S.; Shimazu, H.; Adachi, M.; Muramatsu, T. !$#journal J. Biochem. (1992) 112:609-615 !$#title A novel core protein as well as polymorphic epithelial mucin !1carry peanut agglutinin binding sites in human gastric !1carcinoma cells: sequence analysis and examination of gene !1expression. !$#cross-references MUID:93123189; PMID:1478919 !$#accession PX0066 !'##molecule_type mRNA !'##residues 998-1011,'ES',1014-1017;1018-1032,'T',1034-1037;1038-1057 !1##label MAS !'##experimental_source gastric carcinoma cell REFERENCE S51026 !$#authors Zrihan-Licht, S.; Baruch, A.; Elroy-Stein, O.; Keydar, I.; !1Wreschner, D.H. !$#journal FEBS Lett. (1994) 356:130-136 !$#title Tyrosine phosphorylation of the MUC1 breast cancer membrane !1proteins cytokine receptor-like molecules. !$#cross-references MUID:95080414; PMID:7988707 !$#contents annotation !$#note undetermined tyrosine residues in the carboxyl-terminal !1non-repetitive region are phosphorylated COMMENT This protein is length polymorphic. Individuals may have !1between 21 and 125 copies of the tandem repeat, with 41 and !185 copies being most commonly observed. There are flanking !1imperfect or partial repeats. The repeat shown is defined by !1SmaI nuclease sites. COMMENT Serine and threonine residues in the tandem repeat domain !1are extensively glycosylated. COMMENT For an alternative splice form without a tandem repeat !1domain, see PIR:S48146. GENETICS !$#gene GDB:MUC1; PUM !'##cross-references GDB:120705; OMIM:158340 !$#map_position 1q21-1q23 !$#introns 20/1; 62/3; 1165/3; 1184/2; 1230/1; 1270/3; 1320/3 CLASSIFICATION #superfamily polymorphic epithelial mucin KEYWORDS alternative splicing; duplication; glycoprotein; !1phosphoprotein; polymorphism; surface antigen; tandem !1repeat; transmembrane protein FEATURE !$1-1344 #product mucin 1 precursor, splice form A #status !8predicted #label PREA\ !$1-62 #region mucin 1 amino-terminal non-repetitive\ !$1-23 #domain signal sequence #link PREA #status predicted !8#label SIGA\ !$1-19,29-32 #domain signal sequence #link PREB #status predicted !8#label SIGB\ !$1-19,29-1344 #product mucin 1 precursor, splice form B #status !8predicted #label PREB\ !$1-19,29-212, !$1033-1344 #product mucin 1 precursor, epithelial tumor antigen !8splice form #status predicted #label PRE3\ !$138-1017 #region 20-residue repeats (GSTAPPAHGVTSAPDTRPAP)\ !$1143-1344 #region mucin 1 carboxyl-terminal non-repetitive\ !$1245-1272 #domain transmembrane #status predicted #label TRM\ !$1046,1064,1118, !$1144,1222 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$1213 #binding_site phosphate (Tyr) (covalent) #status !8predicted SUMMARY #length 1344 #molecular-weight 130430 #checksum 4143 SEQUENCE /// ENTRY S48146 #type complete TITLE mucin 1 precursor, non-repetitive splice form Y [validated] - human ALTERNATE_NAMES breast carcinoma-associated DF3 antigen; episialin; MUC1/Y protein; polymorphic epithelial mucin (PEM) ORGANISM #formal_name Homo sapiens #common_name man DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS S48146 REFERENCE S48146 !$#authors Zrihan-Licht, S.; Vos, H.L.; Baruch, A.; Elroy-Stein, O.; !1Sagiv, D.; Keydar, I.; Hilkens, J.; Wreschner, D.H. !$#journal Eur. J. Biochem. (1994) 224:787-795 !$#title Characterization and molecular cloning of a novel MUC1 !1protein, devoid of tandem repeats, expressed in human breast !1cancer tissue. !$#cross-references MUID:95010060; PMID:7925397 !$#accession S48146 !'##molecule_type mRNA !'##residues 1-255 ##label ZRI !'##cross-references EMBL:X80761; NID:g541679; PIDN:CAA56734.1; !1PID:g541680 COMMENT For alternative splice forms with a tandem repeat domain, !1see PIR:A35175. GENETICS !$#gene GDB:MUC1; PUM !'##cross-references GDB:120705; OMIM:158340 !$#map_position 1q21-1q23 !$#introns 20/1; 53/3; 73/3; 95/2; 141/1; 181/3; 231/3 CLASSIFICATION #superfamily polymorphic epithelial mucin KEYWORDS glycoprotein; phosphoprotein; polymorphism; transmembrane !1protein FEATURE !$1-53 #region mucin 1 amino-terminal non-repetitive\ !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-255 #product mucin 1, non-repetitive splice form Y !8#status predicted #label MAT\ !$54-255 #region mucin 1 carboxyl-terminal non-repetitive\ !$156-183 #domain transmembrane #status predicted #label TRM\ !$55,133 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 255 #molecular-weight 27566 #checksum 4227 SEQUENCE /// ENTRY TVHUBR #type complete TITLE bcr (breakpoint cluster region) protein, splice form 1 - human ALTERNATE_NAMES Mbcr protein CONTAINS bcr (breakpoint cluster region) protein, splice form 2 ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 24-Nov-1999 ACCESSIONS A91064; A93362; S14195; S14196; S10113; A28765; A43798; !1I57512; A26172; A29387 REFERENCE A91064 !$#authors Hariharan, I.K.; Adams, J.M. !$#journal EMBO J. (1987) 6:115-119 !$#title cDNA sequence for human bcr, the gene that translocates to !1the abl oncogene in chronic myeloid leukaemia. !$#cross-references MUID:87218455; PMID:3107980 !$#accession A91064 !'##molecule_type mRNA !'##residues 1-872 ##label HAR !'##cross-references EMBL:X02596 REFERENCE A93362 !$#authors Heisterkamp, N.; Stam, K.; Groffen, J.; de Klein, A.; !1Grosveld, G. !$#journal Nature (1985) 315:758-761 !$#title Structural organization of the bcr gene and its role in the !1Ph' translocation. !$#cross-references MUID:85240564; PMID:2989703 !$#accession A93362 !'##molecule_type mRNA !'##residues 683-1271 ##label HEI !'##cross-references GB:M24603 REFERENCE S14193 !$#authors Zhu, Q.S.; Heisterkamp, N.; Groffen, J. !$#journal Nucleic Acids Res. (1990) 18:7119-7125 !$#title Unique organization of the human BCR gene promoter. !$#cross-references MUID:91088292; PMID:2263470 !$#accession S14195 !'##status preliminary !'##molecule_type DNA !'##residues 1-46 ##label ZHU !'##cross-references EMBL:X52828; NID:g23890; PIDN:CAA37010.1; !1PID:g23891 !$#accession S14196 !'##status preliminary !'##molecule_type DNA !'##residues 275-426 ##label ZH2 !'##cross-references EMBL:X52829; NID:g23863; PIDN:CAA37011.1; !1PID:g23864 REFERENCE S10113 !$#authors Romero, P.; Beran, M.; Shtalrid, M.; Andersson, B.; Talpaz, !1M.; Blick, M. !$#journal Oncogene (1989) 4:93-98 !$#title Alternative 5'end of the bcr-abl transcript in chronic !1myelogenous leukemia. !$#cross-references MUID:89128203; PMID:2915904 !$#accession S10113 !'##status preliminary !'##molecule_type mRNA !'##residues 362-438 ##label ROM !'##cross-references EMBL:X14676; NID:g29413; PIDN:CAA32806.1; !1PID:g930043 REFERENCE A28765 !$#authors Lifshitz, B.; Fainstein, E.; Marcelle, C.; Shtivelman, E.; !1Amson, R.; Gale, R.P.; Canaani, E. !$#journal Oncogene (1988) 2:113-117 !$#title bcr genes and transcripts. !$#cross-references MUID:88217290; PMID:3285291 !$#accession A28765 !'##molecule_type mRNA !'##residues 1-417,'D',419-482,'K',484-559,'S',561-732,'D',734-960, !11005-1271 ##label LIF !'##cross-references GB:Y00661; NID:g29411 REFERENCE A43798 !$#authors Selleri, L.; von Lindern, M.; Hermans, A.; Meijer, D.; !1Torelli, G.; Grosveld, G. !$#journal Blood (1990) 75:1146-1153 !$#title Chronic myeloid leukemia may be associated with several !1bcr-abl transcripts including the acute lymphoid !1leukemia-type 7 kb transcript. !$#cross-references MUID:90167280; PMID:2407300 !$#accession A43798 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 670-689,'D',691-732,'D',734-842 ##label SEL REFERENCE I57512 !$#authors Shah, N.P.; Witte, O.N.; Denny, C.T. !$#journal Mol. Cell. Biol. (1991) 11:1854-1860 !$#title Characterization of the BCR promoter in Philadelphia !1chromosome-positive and -negative cell lines. !$#cross-references MUID:91172169; PMID:1900918 !$#accession I57512 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-4 ##label SHA !'##cross-references GB:M64437; NID:g179386 !'##note this translation is not annotated in GenBank entry HUMBCRAA, !1release 112.0 GENETICS !$#gene GDB:BCR !'##cross-references GDB:120562; OMIM:151410 !$#map_position 22q11.2-22q11.2 CLASSIFICATION #superfamily bcr protein; CDC24 homology KEYWORDS alternative splicing; breakpoint cluster region FEATURE !$1-1271 #product bcr (breakpoint cluster region) protein, !8splice form 1 #status predicted #label MAT1\ !$1-960,1005-1271 #product bcr (breakpoint cluster region) protein, !8splice form 2 #status predicted #label MAT2\ !$498-691 #domain CDC24 homology #label CD24 SUMMARY #length 1271 #molecular-weight 142805 #checksum 5214 SEQUENCE /// ENTRY TVHUA2 #type fragment TITLE bcr (breakpoint cluster region) protein, splice form 3 - human (fragment) ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 02-Sep-1997 ACCESSIONS A26664 REFERENCE A26664 !$#authors Mes-Masson, A.M.; McLaughlin, J.; Daley, G.Q.; Paskind, M.; !1Witte, O.N. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:9768-9772 !$#title Overlapping cDNA clones define the complete coding region !1for the P210c-abl gene product associated with chronic !1myelogenous leukemia cells containing the Philadelphia !1chromosome. !$#cross-references MUID:87092329; PMID:3540951 !$#accession A26664 !'##molecule_type mRNA !'##residues 1-693 ##label MES GENETICS !$#gene GDB:BCR !'##cross-references GDB:120562; OMIM:151410 !$#map_position 22q11.2-22q11.2 CLASSIFICATION #superfamily bcr protein; CDC24 homology KEYWORDS breakpoint cluster region FEATURE !$498-691 #domain CDC24 homology #label CD24 SUMMARY #length 693 #checksum 8433 SEQUENCE /// ENTRY HHFF72 #type complete TITLE dnaK-type molecular chaperone Hsp70Bc - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES major heat shock protein 70 2 ORGANISM #formal_name Drosophila melanogaster DATE 31-Dec-1980 #sequence_revision 31-Dec-1980 #text_change 22-Jun-1999 ACCESSIONS A03307 REFERENCE A03307 !$#authors Ingolia, T.D.; Craig, E.A.; McCarthy, B.J. !$#journal Cell (1980) 21:669-679 !$#title Sequence of three copies of the gene for the major !1Drosophila heat shock induced protein and their flanking !1regions. !$#cross-references MUID:81064669; PMID:6777045 !$#accession A03307 !'##molecule_type DNA !'##residues 1-641 ##label ING !'##cross-references GB:J01104; GB:J01105; NID:g157720; PIDN:AAD15226.1; !1PID:g157723 COMMENT Heat shock induces the synthesis of seven proteins at five !1otherwise inactive sites in the polytene chromosomes of !1fruit fly larvae. Two separate sites, producing two and !1three copies, respectively, code for the 70K protein. The !1function of heat shock proteins is unknown. GENETICS !$#gene FlyBase:Hsp70Bc !'##cross-references FlyBase:FBgn0013279 FUNCTION !$#description involved in protein folding and assembling/disassembling of !1protein complexes CLASSIFICATION #superfamily heat shock protein 70 KEYWORDS ATP; heat shock; molecular chaperone; stress-induced protein SUMMARY #length 641 #molecular-weight 70258 #checksum 1785 SEQUENCE /// ENTRY HHXL70 #type complete TITLE dnaK-type molecular chaperone - African clawed frog ALTERNATE_NAMES heat shock protein 70; heat shock protein X16 ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 22-Jun-1999 ACCESSIONS A03310; A22175 REFERENCE A90993 !$#authors Bienz, M. !$#journal EMBO J. (1984) 3:2477-2483 !$#title Xenopus hsp 70 genes are constitutively expressed in !1injected oocytes. !$#cross-references MUID:85076567; PMID:6510409 !$#accession A03310 !'##molecule_type DNA !'##residues 1-647 ##label BIE !'##cross-references GB:X01102; GB:M11915; NID:g64795; PIDN:CAA25576.1; !1PID:g64796 REFERENCE A22175 !$#authors Bienz, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:3138-3142 !$#title Developmental control of the heat shock response in Xenopus. !$#cross-references MUID:84221917; PMID:6203112 !$#accession A22175 !'##molecule_type mRNA !'##residues 81-120 ##label BI2 !'##cross-references GB:K02307; NID:g214271; PIDN:AAA49759.1; !1PID:g214272 COMMENT This protein is expressed constitutively in oocytes, !1disappears after fertilization, and is induced by heat shock !1in somatic cells from the gastrula stage onward. FUNCTION !$#description involved in protein folding and assembling/disassembling of !1protein complexes CLASSIFICATION #superfamily heat shock protein 70 KEYWORDS ATP; heat shock; molecular chaperone; stress-induced protein SUMMARY #length 647 #molecular-weight 70915 #checksum 3965 SEQUENCE /// ENTRY HHKW7A #type complete TITLE dnaK-type molecular chaperone hsp70A - Caenorhabditis elegans ALTERNATE_NAMES heat shock protein 70 A ORGANISM #formal_name Caenorhabditis elegans DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 22-Jun-1999 ACCESSIONS JT0285 REFERENCE JT0285 !$#authors Snutch, T.P.; Heschl, M.F.P.; Baillie, D.L. !$#journal Gene (1988) 64:241-255 !$#title The Caenorhabditis elegans hsp70 gene family: a molecular !1genetic characterization. !$#cross-references MUID:88297155; PMID:2841196 !$#accession JT0285 !'##molecule_type DNA; mRNA !'##residues 1-640 ##label SNU !'##cross-references GB:M18540; NID:g156351; PIDN:AAA28078.1; !1PID:g156352 !'##note genomic clones representing six distinct members of the hsp70 !1gene family were isolated !'##note transcripts of hsp70A are abundant in control worms and also !1increase two- to sixfold upon heat shock !'##note one of the three introns in hsp70A is in a position similar to !1an intron in Drosophila hsc1 and hsc2 genes GENETICS !$#gene hsp70A !$#map_position IV !$#introns 69/1; 331/3; 558/3 FUNCTION !$#description involved in protein folding and assembling/disassembling of !1protein complexes CLASSIFICATION #superfamily heat shock protein 70 KEYWORDS ATP; heat shock; molecular chaperone; stress-induced protein SUMMARY #length 640 #molecular-weight 69823 #checksum 6630 SEQUENCE /// ENTRY HHUM7B #type complete TITLE dnaK-type molecular chaperone - lettuce downy mildew ALTERNATE_NAMES heat shock protein 70 ORGANISM #formal_name Bremia lactucae #common_name lettuce downy mildew DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 13-Mar-1998 ACCESSIONS JU0062 REFERENCE JU0062 !$#authors Judelson, H.S.; Michelmore, R.W. !$#journal Gene (1989) 79:207-217 !$#title Structure and expression of a gene encoding heat-shock !1protein Hsp70 from the oomycete fungus Bremia lactucae. !$#cross-references MUID:90006750; PMID:2792764 !$#accession JU0062 !'##molecule_type DNA !'##residues 1-675 ##label JUD COMMENT This fungus causes downy mildew disease in lettuce. FUNCTION !$#description involved in protein folding and assembling/disassembling of !1protein complexes CLASSIFICATION #superfamily heat shock protein 70 KEYWORDS ATP; heat shock; molecular chaperone; stress-induced protein SUMMARY #length 675 #molecular-weight 73986 #checksum 9064 SEQUENCE /// ENTRY HHBYA1 #type complete TITLE dnaK-type molecular chaperone SSA1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES heat shock protein 70-related protein SSA1; heat shock protein YG100; protein YAL005c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 05-Nov-1999 ACCESSIONS S43449; S25438; S42164; S25231; S40897 REFERENCE S43441 !$#authors Clark, M.W.; Keng, T.; Storms, R.K.; Zhong, W.; Fortin, N.; !1Zeng, B.; Delaney, S.; Ouellette, B.F.F.; Barton, A.B.; !1Kaback, D.B.; Bussey, H. !$#journal Yeast (1994) 10:535-541 !$#title Sequencing of chromosome I of Saccharomyces cerevisiae: !1analysis of the 42 kbp SPO7-CENI-CDC15 region. !$#cross-references MUID:95028152; PMID:7941740 !$#accession S43449 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-642 ##label CLA !'##cross-references EMBL:L22015; NID:g1339990; PIDN:AAC04952.1; !1PID:g349747; GSPDB:GN00001; MIPS:YAL005c !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1993 REFERENCE S20139 !$#authors Slater, M.R.; Craig, E.A. !$#journal Nucleic Acids Res. (1989) 17:805-806 !$#title The SSA1 and SSA2 genes of the yeast Saccharomyces !1cerevisiae. !$#cross-references MUID:89128457; PMID:2644626 !$#accession S25438 !'##status translation not shown !'##molecule_type DNA !'##residues 1-642 ##label SLA !'##cross-references EMBL:X12926 !'##note this sequence has been revised in reference S42164 REFERENCE S42164 !$#authors Slater, M.R. !$#submission submitted to the EMBL Data Library, June 1993 !$#accession S42164 !'##molecule_type DNA !'##residues 1-207,'S',209-417,'P',419-421,'S',423-642 ##label SL2 !'##cross-references EMBL:X12926; NID:g312351; PIDN:CAA31393.1; !1PID:g312352 !'##note this is a revision to the sequence from reference S20139 GENETICS !$#gene SGD:SSA1; YG100; MIPS:YAL005c !'##cross-references SGD:S0000004; MIPS:YAL005c !$#map_position 1L FUNCTION !$#description involved in protein folding and assembling/disassembling of !1protein complexes CLASSIFICATION #superfamily heat shock protein 70 KEYWORDS ATP; heat shock; molecular chaperone; stress-induced !1protein; transmembrane protein FEATURE !$193-209 #domain transmembrane #status predicted #label TMM SUMMARY #length 642 #molecular-weight 69767 #checksum 6411 SEQUENCE /// ENTRY HHBYK2 #type complete TITLE dnaK-type molecular chaperone KAR2 precursor - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES heat shock protein BiP/GRP78 homolog; nuclear fusion protein KAR2; protein J1248; protein YJL034w ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 21-Jul-2000 ACCESSIONS A32366; A34875; A32367; B32367; S56806; A30943; S05776; !1S05777 REFERENCE A32366 !$#authors Rose, M.D.; Misra, L.M.; Vogel, J.P. !$#journal Cell (1989) 57:1211-1221 !$#title KAR2, a karyogamy gene, is the yeast homolog of the !1mammalian BiP/GRP78 gene. !$#cross-references MUID:89288322; PMID:2661018 !$#accession A32366 !'##molecule_type DNA !'##residues 1-682 ##label ROS !'##cross-references EMBL:M25064; NID:g171772; PIDN:AAA34714.1; !1PID:g171773 REFERENCE A34875 !$#authors Nicholson, R.C.; Williams, D.B.; Moran, L.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:1159-1163 !$#title An essential member of the HSP70 gene family of !1Saccharomyces cerevisiae is homologous to immunoglobulin !1heavy chain binding protein. !$#cross-references MUID:90138957; PMID:2105497 !$#accession A34875 !'##molecule_type DNA !'##residues 1-682 ##label NIC !'##cross-references EMBL:M31006; NID:g171129; PIDN:AAA34454.1; !1PID:g171130 !'##note the authors translated the codon TTG for residue 119 as Val and !1GGT for residue 121 as Val REFERENCE A32367 !$#authors Normington, K.; Kohno, K.; Kozutsumi, Y.; Gething, M.J.; !1Sambrook, J. !$#journal Cell (1989) 57:1223-1236 !$#title S. cerevisiae encodes an essential protein homologous in !1sequence and function to mammalian BiP. !$#cross-references MUID:89288323; PMID:2661019 !$#accession A32367 !'##molecule_type DNA !'##residues 1-682 ##label NOR1 !'##cross-references EMBL:M25394; NID:g171770; PIDN:AAA34713.1; !1PID:g171771 !$#accession B32367 !'##molecule_type mRNA !'##residues 31-388 ##label NOR2 !'##note the authors translated the codon ACT for residue 161 as Pro REFERENCE S56793 !$#authors Pohl, T.M.; Aljinovic, G. !$#submission submitted to the Protein Sequence Database, September 1995 !$#accession S56806 !'##molecule_type DNA !'##residues 1-682 ##label TOV !'##cross-references EMBL:Z49309; NID:g1008156; PIDN:CAA89325.1; !1PID:g1008157; GSPDB:GN00010; MIPS:YJL034w GENETICS !$#gene SGD:KAR2; MIPS:YJL034w !'##cross-references SGD:S0003571; MIPS:YJL034w !$#map_position 10L FUNCTION !$#description involved in protein folding and assembling/disassembling of !1protein complexes; required for both co-translational import !1and post-translational import of proteins into the ER; !1required for fusion of ER-nuclear membranes during !1karyogamy; can participate in refolding of heat-denatured !1proteins in the ER CLASSIFICATION #superfamily heat shock protein 70 KEYWORDS ATP; endoplasmic reticulum; heat shock; molecular chaperone; !1stress-induced protein FEATURE !$1-42 #domain signal sequence #status predicted #label SIG\ !$43-682 #product dnaK-type molecular chaperone KAR2 #status !8predicted #label MAT\ !$679-682 #region endoplasmic reticulum retention signal SUMMARY #length 682 #molecular-weight 74467 #checksum 7408 SEQUENCE /// ENTRY HHRTGB #type complete TITLE dnaK-type molecular chaperone precursor - rat ALTERNATE_NAMES BiP; glucose-regulated 78K protein; Ig heavy chain-binding protein CONTAINS steroidogenesis-activator polypeptide ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 22-Jun-1999 ACCESSIONS A23948; A60134; A26257 REFERENCE A23948 !$#authors Munro, S.; Pelham, H.R.B. !$#journal Cell (1986) 46:291-300 !$#title An Hsp70-like protein in the ER: identity with the 78 kd !1glucose-regulated protein and immunoglobulin heavy chain !1binding protein. !$#cross-references MUID:86245075; PMID:3087629 !$#accession A23948 !'##molecule_type mRNA !'##residues 1-654 ##label MUN !'##cross-references GB:M14050; NID:g203150; PIDN:AAA40817.1; !1PID:g203151 REFERENCE A60134 !$#authors Pedersen, R.C.; Brownie, A.C. !$#journal Science (1987) 236:188-190 !$#title Steroidogenesis-activator polypeptide isolated from a rat !1leydig cell tumor. !$#cross-references MUID:87177981; PMID:3563495 !$#accession A60134 !'##molecule_type protein !'##residues 626-648,'D',650,'K',651-654 ##label PED REFERENCE A26257 !$#authors Chang, S.C.; Wooden, S.K.; Nakaki, T.; Kim, Y.K.; Lin, A.Y.; !1Kung, L.; Attenello, J.W.; Lee, A.S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:680-684 !$#title Rat gene encoding the 78-KDa glucose-regulated protein !1GRP78: its regulatory sequences and the effect of protein !1glycosylation on its expression. !$#cross-references MUID:87118232; PMID:3468506 !$#accession A26257 !'##molecule_type DNA !'##residues 1-28,'M',30-40 ##label CHA !'##cross-references GB:M14866; NID:g204478; PIDN:AAA41277.1; !1PID:g554440 FUNCTION !$#description involved in protein folding and assembling/disassembling of !1protein complexes CLASSIFICATION #superfamily heat shock protein 70 KEYWORDS ATP; endoplasmic reticulum; glycoprotein; molecular !1chaperone FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-654 #product Ig heavy chain binding protein #status !8predicted #label MAT\ !$651-654 #region endoplasmic reticulum retention signal SUMMARY #length 654 #molecular-weight 72346 #checksum 2743 SEQUENCE /// ENTRY B48127 #type complete TITLE dnaK-type molecular chaperone precursor, mitochondrial - human ALTERNATE_NAMES heat shock protein 70 homolog; PBP74; peptide-binding protein 74 ORGANISM #formal_name Homo sapiens #common_name man DATE 21-Jan-1994 #sequence_revision 26-May-1995 #text_change 20-Apr-2000 ACCESSIONS B48127; A55623 REFERENCE A48127 !$#authors Domanico, S.Z.; DeNagel, D.C.; Dahlseid, J.N.; Green, J.M.; !1Pierce, S.K. !$#journal Mol. Cell. Biol. (1993) 13:3598-3610 !$#title Cloning of the gene encoding peptide-binding protein 74 !1shows that it is a new member of the heat shock protein 70 !1family. !$#cross-references MUID:93268309; PMID:7684501 !$#accession B48127 !'##molecule_type mRNA !'##residues 1-679 ##label DOM !'##cross-references GB:L11066; NID:g307322 !'##note sequence extracted from NCBI backbone (NCBIN:132585, !1NCBIP:132586) !'##note this ORF is not annotated in GenBank entry HUMPBP, release 106 REFERENCE A55623 !$#authors Bhattacharyya, T.; Karnezis, A.N.; Murphy, S.P.; Hoang, T.; !1Freeman, B.C.; Phillips, B.; Morimoto, R.I. !$#journal J. Biol. Chem. (1995) 270:1705-1710 !$#title Cloning and subcellular localization of human mitochondrial !1hsp70. !$#cross-references MUID:95130547; PMID:7829505 !$#accession A55623 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-539,'R',541-679 ##label BHA !'##cross-references GB:L15189; NID:g292058; PIDN:AAA67526.1; !1PID:g292059 !'##note authors definitively demonstrate mitochondrial localization GENETICS !$#gene GDB:HSPA9B; HSPA9; GRP75; PBP74; MOT2; MTHSP75 !'##cross-references GDB:626151; OMIM:600548 !$#map_position 5q31.1-5q31.1 FUNCTION !$#description involved in protein folding and assembling/disassembling of !1protein complexes CLASSIFICATION #superfamily heat shock protein 70 KEYWORDS ATP; heat shock; mitochondrion; molecular chaperone; !1stress-induced protein FEATURE !$1-46 #domain transit peptide (mitochondrion) #status !8predicted #label TPP\ !$47-679 #product mitochondrial hsp70 #status predicted #label !8MAT SUMMARY #length 679 #molecular-weight 73680 #checksum 303 SEQUENCE /// ENTRY I56581 #type complete TITLE dnaK-type molecular chaperone grp75 precursor - rat ALTERNATE_NAMES glucose regulated protein 75; grp75; heat shock protein 70 homolog; PBP74; peptide-binding protein 74 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 26-Jul-1996 #sequence_revision 11-Apr-1997 #text_change 16-Jul-1999 ACCESSIONS I56581; B35488; I53019 REFERENCE I56581 !$#authors Massa, S.M.; Longo, F.M.; Zuo, J.; Wang, S.; Chen, J.; !1Sharp, F.R. !$#journal J. Neurosci. Res. (1995) 40:807-819 !$#title Cloning of rat grp75, an hsp70-family member, and its !1expression in normal and ischemic brain. !$#cross-references MUID:95356254; PMID:7629893 !$#accession I56581 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-679 ##label RES !'##cross-references GB:S78556; NID:g1000438; PIDN:AAB34982.1; !1PID:g1000439 !'##experimental_source strain Sprague-Dawley, brain REFERENCE A35488 !$#authors Akamizu, T.; Saji, M.; Kohn, L.D. !$#journal Biochem. Biophys. Res. Commun. (1990) 170:351-358 !$#title A microsequencing approach to identify proteins which appear !1to interact with thyrotropin in rat FRTL-5 thyroid cells. !$#cross-references MUID:90321251; PMID:2372296 !$#accession B35488 !'##molecule_type protein !'##residues 80-98;484-486,'T',488-492,'Q',494-503 ##label AKA REFERENCE I53019 !$#authors Webster, T.J.; Naylor, D.J.; Hartman, D.J.; Hoj, P.B.; !1Hoogenraad, N.J. !$#journal DNA Cell Biol. (1994) 13:1213-1220 !$#title cDNA cloning and efficient mitochondrial import of !1pre-mtHSP70 from rat liver. !$#cross-references MUID:95110439; PMID:7811387 !$#accession I53019 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-36,'V',38-80,'S',82-372,'R',374-588,'V',590-679 ##label !1RE2 !'##cross-references GB:S75280; NID:g896231; PIDN:AAB33049.1; !1PID:g896232 FUNCTION !$#description involved in protein folding and assembling/disassembling of !1protein complexes CLASSIFICATION #superfamily heat shock protein 70 KEYWORDS ATP; mitochondrion; molecular chaperone; stress-induced !1protein FEATURE !$1-46 #domain transit peptide (mitochondrion) #status !8predicted #label TPP\ !$47-679 #product mitochondrial heat shock protein 70 homolog !8#status predicted #label MAT SUMMARY #length 679 #molecular-weight 73744 #checksum 373 SEQUENCE /// ENTRY HHBYS1 #type complete TITLE dnaK-type molecular chaperone SSC1 precursor, mitochondrial - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES endonuclease SceI 75K chain; endonuclease SceI large chain; heat shock protein 70-related protein SSC1; protein GTF654; protein J1639; protein YJR045c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 21-Jul-2000 ACCESSIONS A32493; S11176; S20238; S12497; S57064; S63769 REFERENCE A32493 !$#authors Craig, E.A.; Kramer, J.; Shilling, J.; Werner-Washburne, M.; !1Holmes, S.; Kosic-Smithers, J.; Nicolet, C.M. !$#journal Mol. Cell. Biol. (1989) 9:3000-3008 !$#title SSC1, an essential member of the yeast HSP70 multigene !1family, encodes a mitochondrial protein. !$#cross-references MUID:89384560; PMID:2674677 !$#accession A32493 !'##molecule_type DNA !'##residues 1-654 ##label CRA !'##cross-references EMBL:M27229; NID:g341653; PIDN:AAA63792.1; !1PID:g717089 REFERENCE S11176 !$#authors Morishima, N.; Nakagawa, K.; Yamamoto, E.; Shibata, T. !$#journal J. Biol. Chem. (1990) 265:15189-15197 !$#title A subunit of yeast site-specific endonuclease SceI is a !1mitochondrial version of the 70-kDa heat shock protein. !$#cross-references MUID:90368701; PMID:2203771 !$#accession S11176 !'##molecule_type DNA !'##residues 1-643,'N',644-649,'D',651-654 ##label MOR !'##cross-references GB:M55275; GB:J05574; NID:g171462; PIDN:AAA34590.1; !1PID:g171463 !$#accession S20238 !'##molecule_type protein !'##residues 24-41 ##label MOR2 REFERENCE S12497 !$#authors Scherer, P.E.; Krieg, U.C.; Hwang, S.T.; Vestweber, D.; !1Schatz, G. !$#journal EMBO J. (1990) 9:4315-4322 !$#title A precursor protein partly translocated into yeast !1mitochondria is bound to a 70 kd mitochondrial stress !1protein. !$#cross-references MUID:91092254; PMID:2265609 !$#accession S12497 !'##molecule_type protein !'##residues 'E',25-38 ##label SCHE REFERENCE S57052 !$#authors Huang, M.E.; Chuat, J.C.; Galibert, F. !$#submission submitted to the Protein Sequence Database, September 1995 !$#accession S57064 !'##molecule_type DNA !'##residues 1-654 ##label MAN !'##cross-references EMBL:Z49545; NID:g1015700; PIDN:CAA89573.1; !1PID:g1015701; GSPDB:GN00010; MIPS:YJR045c REFERENCE S63757 !$#authors Huang, M.E.; Chuat, J.C.; Galibert, F. !$#journal Yeast (1995) 11:775-781 !$#title Analysis of a 42.5 kb DNA sequence of chromosome X reveals !1three tRNA genes and 14 new open reading frames including a !1gene most probably belonging to the family of !1ubiquitin-protein ligases. !$#cross-references MUID:95397595; PMID:7668047 !$#accession S63769 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-654 ##label HUA !'##cross-references EMBL:L36344; NID:g1197060; PIDN:AAA88747.1; !1PID:g1197073 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1February 1996 GENETICS !$#gene SGD:SSC1; ENS1; MIPS:YJR045c !'##cross-references SGD:S0003806; MIPS:YJR045c !$#map_position 10R !$#genome nuclear FUNCTION !$#description involved in protein folding and assembling/disassembling of !1protein complexes CLASSIFICATION #superfamily heat shock protein 70 KEYWORDS ATP; endonuclease; heat shock; mitochondrion; molecular !1chaperone; stress-induced protein FEATURE !$1-23 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$24-654 #product dnaK-type molecular chaperone SSC1 #status !8experimental #label MAT\ !$634-646 #region asparagine-rich SUMMARY #length 654 #molecular-weight 70627 #checksum 6160 SEQUENCE /// ENTRY IQECDK #type complete TITLE dnaK-type molecular chaperone dnaK - Escherichia coli (strain K-12) ALTERNATE_NAMES heat shock protein, 70K; hsp70 protein ORGANISM #formal_name Escherichia coli DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 01-Mar-2002 ACCESSIONS A03311; S40536; B26298; S29261; S61285; F64721 REFERENCE A03311 !$#authors Bardwell, J.C.A.; Craig, E.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:848-852 !$#title Major heat shock gene of Drosophila and the Escherichia coli !1heat-inducible dnaK gene are homologous. !$#cross-references MUID:84144800; PMID:6322174 !$#accession A03311 !'##molecule_type DNA !'##residues 1-638 ##label BAR !'##cross-references GB:D10483; GB:J01597; GB:J01683; GB:J01706; !1GB:K01298; GB:K01990; GB:M10420; GB:M10611; GB:M12544; !1GB:V00259; GB:X04711; GB:X54847; GB:X54945; GB:X55034; !1GB:X56742; NID:g216434; PIDN:BAA01291.1; PID:g216440 REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40536 !'##molecule_type DNA !'##residues 1-638 ##label YUR !'##cross-references EMBL:D10483; NID:g216434; PIDN:BAA01291.1; !1PID:g216440 REFERENCE A56405 !$#authors McCarty, J.S.; Walker, G.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:9513-9517 !$#title DnaK as a thermometer: threonine-199 is site of !1autophosphorylation and is critical for ATPase activity. !$#cross-references MUID:92052123; PMID:1835085 !$#contents annotation REFERENCE A26298 !$#authors Ohki, M.; Tamura, F.; Nishimura, S.; Uchida, H. !$#journal J. Biol. Chem. (1986) 261:1778-1781 !$#title Nucleotide sequence of the Escherichia coli dnaJ gene and !1purification of the gene product. !$#cross-references MUID:86111849; PMID:3003084 !$#accession B26298 !'##status preliminary !'##molecule_type DNA !'##residues 590-638 ##label OHK !'##experimental_source strain K12 !'##note the authors translated the codon CAG for residue 593 as Glu REFERENCE S29260 !$#authors Schmid, D.; Jaussi, R.; Christen, P. !$#journal Eur. J. Biochem. (1992) 208:699-704 !$#title Precursor of mitochondrial aspartate aminotransferase !1synthesized in Escherichia coli is complexed with heat-shock !1protein DnaK. !$#cross-references MUID:93011098; PMID:1396676 !$#accession S29261 !'##molecule_type protein !'##residues 2-9,11-14,'VI' ##label SCH REFERENCE S61284 !$#authors Freestone, P.; Grant, S.; Toth, I.; Norris, V. !$#journal Mol. Microbiol. (1995) 15:573-580 !$#title Identification of phosphoproteins in Escherichia coli. !$#cross-references MUID:95302968; PMID:7783627 !$#accession S61285 !'##molecule_type protein !'##residues 2-11 ##label FRE REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64721 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-638 ##label BLAT !'##cross-references GB:AE000112; GB:U00096; NID:g1786192; !1PIDN:AAC73125.1; PID:g1786196; UWGP:b0014 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene dnaK !$#map_position 0 min FUNCTION !$#description involved in protein folding and assembling/disassembling of !1protein complexes CLASSIFICATION #superfamily heat shock protein 70 KEYWORDS ATP; autophosphorylation; calcium; DNA replication; heat !1shock; molecular chaperone; phosphoprotein; stress-induced !1protein FEATURE !$2-638 #product dnaK-type molecular chaperone dnaK #status !8experimental #label MAT\ !$199 #binding_site phosphate (Thr) (covalent) (by !8autophosphorylation) (partial) #status experimental SUMMARY #length 638 #molecular-weight 69114 #checksum 4735 SEQUENCE /// ENTRY HHHU86 #type complete TITLE heat shock protein 90-alpha - human ALTERNATE_NAMES heat shock protein 86; heat shock protein 89 alpha ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 22-Jun-1999 ACCESSIONS A32319; JQ0128; PS0020; S06898; JQ0724; B31420; S67961 REFERENCE A32319 !$#authors Hickey, E.; Brandon, S.E.; Smale, G.; Lloyd, D.; Weber, L.A. !$#journal Mol. Cell. Biol. (1989) 9:2615-2626 !$#title Sequence and regulation of a gene encoding a human !189-kilodalton heat shock protein. !$#cross-references MUID:89343979; PMID:2527334 !$#accession A32319 !'##molecule_type DNA !'##residues 1-732 ##label HIC !'##cross-references GB:M27024; NID:g341598; PIDN:AAA63194.1; !1PID:g703087 !'##note the authors translated the codon AAC for residue 383 as Asp REFERENCE JQ0128 !$#authors Walter, T.; Drabent, B.; Krebs, H.; Tomalak, M.; Heiss, S.; !1Benecke, B.J. !$#journal Gene (1989) 83:105-115 !$#title Cloning and analysis of a human 86-kDa !1heat-shock-protein-encoding gene. !$#cross-references MUID:90076956; PMID:2591742 !$#accession JQ0128 !'##molecule_type DNA !'##residues 1-312 ##label WAL !'##cross-references GB:M30626; NID:g184418; PIDN:AAA36023.1; !1PID:g184419 !'##note the authors translated the codon AAA for residue 58 as Leu and !1AAC for residue 83 as Ser REFERENCE PS0020 !$#authors Hoffmann, T.; Hovemann, B. !$#journal Gene (1988) 74:491-501 !$#title Heat-shock proteins, Hsp84 and Hsp86, of mice and men: two !1related genes encode formerly identified tumour-specific !1transplantation antigens. !$#cross-references MUID:89232740; PMID:2469626 !$#accession PS0020 !'##molecule_type mRNA !'##residues 1-312 ##label HOF !'##cross-references GB:X07270; NID:g32485; PIDN:CAA30255.1; PID:g32486 REFERENCE S06898 !$#authors Yamazaki, M.; Akaogi, K.; Miwa, T.; Imai, T.; Soeda, E.; !1Yokoyama, K. !$#journal Nucleic Acids Res. (1989) 17:7108 !$#title Nucleotide sequence of a full-length cDNA for 90 kDa !1heat-shock protein from human peripheral blood lymphocytes. !$#cross-references MUID:89386066; PMID:2780322 !$#accession S06898 !'##molecule_type mRNA !'##residues 1-20,'LSG',25-62,'T',64-161,'GVLSR',168-732 ##label YAM !'##experimental_source peripheral blood lymphocytes REFERENCE JQ0724 !$#authors Yamazaki, M.; Tashiro, H.; Yokoyama, K.; Soeda, E. !$#journal Agric. Biol. Chem. (1990) 54:3163-3170 !$#title Molecular cloning of cDNA encoding a human heat-shock !1protein whose expression is induced by adenovirus type 12 !1E1A in HeLa cells. !$#cross-references MUID:91242090; PMID:1368637 !$#accession JQ0724 !'##molecule_type mRNA !'##residues 1-62,'T',64-732 ##label YA2 !'##experimental_source adenovirus type 12 E1A-transfected HeLa cells REFERENCE A92741 !$#authors Lees-Miller, S.P.; Anderson, C.W. !$#journal J. Biol. Chem. (1989) 264:2431-2437 !$#title Two human 90-kDa heat shock proteins are phosphorylated in !1vivo at conserved serines that are phosphorylated in vitro !1by casein kinase II. !$#cross-references MUID:89123325; PMID:2492519 !$#accession B31420 !'##molecule_type protein !'##residues 2-21;225-274 ##label LEE !'##experimental_source HeLa cells in exponential growth !'##note phosphorylation sites were determined by metabolic labelling !1with [32-P]orthophosphate; phosphate content was ~1.7 mol !1phosphate/mol protein REFERENCE S67961 !$#authors Nemoto, T.; Ohara-Nemoto, Y.; Ota, M.; Takagi, T.; Yokoyama, !1K. !$#journal Eur. J. Biochem. (1995) 233:1-8 !$#title Mechanism of dimer formation of the 90-kDa heat-shock !1protein. !$#cross-references MUID:96061925; PMID:7588731 !$#accession S67961 !'##molecule_type protein !'##residues 533-539;542-551;'AQ',619-634 ##label NEM COMMENT In response to temperature stress, to treatment with certain !1chemicals and amino acid analogs, or following viral !1infections, heat shock proteins are synthesized as a set of !1low- and high-molecular-weight proteins. GENETICS !$#gene GDB:HSPCA; HSPC1 !'##cross-references GDB:118813; OMIM:140571 !$#map_position Xpter-Xq22 !$#introns 54/3; 177/1; 221/3; 327/3; 383/1; 446/3; 496/1; 585/3; 697/1 CLASSIFICATION #superfamily heat shock protein 90 KEYWORDS estrogen-induced protein; heat shock; phosphoprotein; !1steroid receptor complex; stress-induced protein FEATURE !$223-322 #region highly charged\ !$534-569 #region highly charged\ !$231,263 #binding_site phosphate (Ser) (covalent) #status !8experimental SUMMARY #length 732 #molecular-weight 84659 #checksum 8926 SEQUENCE /// ENTRY HHMS86 #type complete TITLE heat shock protein 86 - mouse ALTERNATE_NAMES HSP86 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 22-Jun-1999 ACCESSIONS B32848; PS0021; A40338; A37345 REFERENCE A32848 !$#authors Moore, S.K.; Kozak, C.; Robinson, E.A.; Ullrich, S.J.; !1Appella, E. !$#journal J. Biol. Chem. (1989) 264:5343-5351 !$#title Murine 86- and 84-kDa heat shock proteins, cDNA sequences, !1chromosome assignments, and evolutionary origins. !$#cross-references MUID:89174568; PMID:2925609 !$#accession B32848 !'##molecule_type mRNA !'##residues 1-733 ##label MR1 !'##cross-references GB:J04633; NID:g194030; PIDN:AAA53068.1; !1PID:g309318 REFERENCE PS0020 !$#authors Hoffmann, T.; Hovemann, B. !$#journal Gene (1988) 74:491-501 !$#title Heat-shock proteins, Hsp84 and Hsp86, of mice and men: two !1related genes encode formerly identified tumour-specific !1transplantation antigens. !$#cross-references MUID:89232740; PMID:2469626 !$#accession PS0021 !'##molecule_type mRNA !'##residues 6,'A',8-242,247-355,'K' ##label HOF !'##cross-references GB:M36830; NID:g194032; PIDN:AAA37868.1; !1PID:g194033 REFERENCE A40338 !$#authors Moore, S.K.; Appella, E.; Villar, C.J.; Kozak, C.A. !$#journal Genomics (1991) 10:1019-1029 !$#title Mapping of the mouse 86-kDa heat-shock protein expressed !1gene (Hsp86-1) on chromosome 12 and related genes on !1chromosomes 3, 4, 9, and 11. !$#cross-references MUID:92009901; PMID:1916807 !$#accession A40338 !'##molecule_type DNA !'##residues 556-634 ##label MR2 !'##cross-references GB:M57673; NID:g194028; PIDN:AAA37867.1; !1PID:g194029 REFERENCE A37345 !$#authors Legagneux, V.; Mezger, V.; Quelard, C.; Barnier, J.V.; !1Bensaude, O.; Morange, M. !$#journal Differentiation (1989) 41:42-48 !$#title High constitutive transcription of HSP86 gene in murine !1embryonal carcinoma cells. !$#cross-references MUID:90033873; PMID:2806771 !$#accession A37345 !'##molecule_type mRNA !'##residues 460-733 ##label LEG !'##cross-references GB:X16857; NID:g51456; PIDN:CAA34748.1; PID:g51457 COMMENT In response to temperature stress, to treatment with certain !1chemicals and amino acid analogs, or following viral !1infections, heat shock proteins are synthesized as a set of !1low- and high-molecular-weight proteins. COMMENT This protein is one of two forms of 80-90 kDa heat shock !1proteins found in mice. These are abundant in the cytoplasm !1of unstressed cells and are moderately induced by heat !1shock. GENETICS !$#gene HSP86 !$#introns 586/3 !$#note the list of introns may be incomplete CLASSIFICATION #superfamily heat shock protein 90 KEYWORDS estrogen-induced protein; heat shock; phosphoprotein; !1steroid receptor complex; stress-induced protein; !1transplantation antigen FEATURE !$2-733 #product heat shock protein 86 #status experimental !8#label MAT\ !$223-323 #region highly charged\ !$535-570 #region highly charged SUMMARY #length 733 #molecular-weight 84787 #checksum 1396 SEQUENCE /// ENTRY HHCH90 #type complete TITLE heat shock protein 90 - chicken ALTERNATE_NAMES heat shock protein, 90K ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 22-Jun-1999 ACCESSIONS A32298; S12472; S05435; A23779; S10880 REFERENCE A32298 !$#authors Binart, N.; Chambraud, B.; Dumas, B.; Rowlands, D.A.; !1Bigogne, C.; Levin, J.M.; Garnier, J.; Baulieu, E.E.; !1Catelli, M.G. !$#journal Biochem. Biophys. Res. Commun. (1989) 159:140-147 !$#title The cDNA-derived amino acid sequence of chick heat shock !1protein Mr 90,000 (HSP 90) reveals a "DNA like" structure: !1potential site of interaction with steroid receptors. !$#cross-references MUID:89165846; PMID:2923621 !$#accession A32298 !'##molecule_type mRNA !'##residues 1-728 ##label BIN !'##cross-references EMBL:X07265 REFERENCE S12472 !$#authors Binart, N. !$#submission submitted to the EMBL Data Library, March 1988 !$#accession S12472 !'##molecule_type mRNA !'##residues 1-136,'S',138-728 ##label BI2 !'##cross-references EMBL:X07265; NID:g63515; PIDN:CAA30251.1; !1PID:g63516 REFERENCE S05435 !$#authors Vourc'h, C.; Binart, N.; Chambraud, B.; David, J.P.; Jerome, !1V.; Baulieu, E.E.; Catelli, M.G. !$#journal Nucleic Acids Res. (1989) 17:5259-5272 !$#title Isolation and functional analysis of chicken 90-kDa heat !1shock protein gene promoter. !$#cross-references MUID:89345085; PMID:2762125 !$#accession S05435 !'##status translation not shown !'##molecule_type DNA !'##residues 1-85 ##label VOU !'##cross-references EMBL:X15028; NID:g63512; PIDN:CAA33132.1; !1PID:g295722 GENETICS !$#introns 53/3 CLASSIFICATION #superfamily heat shock protein 90 KEYWORDS heat shock; phosphoprotein; stress-induced protein SUMMARY #length 728 #molecular-weight 84119 #checksum 2960 SEQUENCE /// ENTRY HHHU84 #type complete TITLE heat shock protein 90-beta [validated] - human ALTERNATE_NAMES heat shock protein 84 ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 08-Dec-2000 ACCESSIONS A29461; A31420 REFERENCE A29461 !$#authors Rebbe, N.F.; Ware, J.; Bertina, R.M.; Modrich, P.; Stafford, !1D.W. !$#journal Gene (1987) 53:235-245 !$#title Nucleotide sequence of a cDNA for a member of the human !190-kDa heat-shock protein family. !$#cross-references MUID:87277414; PMID:3301534 !$#accession A29461 !'##molecule_type mRNA !'##residues 1-724 ##label REB !'##cross-references GB:M16660; NID:g184420; PIDN:AAA36025.1; !1PID:g306891 REFERENCE A92741 !$#authors Lees-Miller, S.P.; Anderson, C.W. !$#journal J. Biol. Chem. (1989) 264:2431-2437 !$#title Two human 90-kDa heat shock proteins are phosphorylated in !1vivo at conserved serines that are phosphorylated in vitro !1by casein kinase II. !$#cross-references MUID:89123325; PMID:2492519 !$#accession A31420 !'##molecule_type protein !'##residues 2-21;220-265 ##label LEE !'##experimental_source HeLa cells (exponential growth) !'##note phosphorylation sites were determined by metabolic labelling !1with [32-P]orthophosphate; phosphate content was ~1.7 mol !1phosphate/mol protein GENETICS !$#gene GDB:HSPCB; HSPC2 !'##cross-references GDB:118814; OMIM:140572 !$#map_position 6p12-6p12 CLASSIFICATION #superfamily heat shock protein 90 KEYWORDS estrogen-induced protein; heat shock; phosphoprotein; !1steroid receptor complex; stress-induced protein FEATURE !$2-724 #product heat shock protein 90-beta #status !8experimental #label MAT\ !$226,255 #binding_site phosphate (Ser) (covalent) #status !8experimental SUMMARY #length 724 #molecular-weight 83294 #checksum 3214 SEQUENCE /// ENTRY HHMS84 #type complete TITLE heat shock protein 84 - mouse ALTERNATE_NAMES HSP84 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 15-Nov-1996 ACCESSIONS A35569; A32848; JS0099; A28809 REFERENCE A35569 !$#authors Moore, S.K.; Rijli, F.; Appella, E. !$#journal DNA Cell Biol. (1990) 9:387-400 !$#title Characterization of the mouse 84-kD heat shock protein gene !1family. !$#cross-references MUID:91000354; PMID:1976316 !$#accession A35569 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-724 ##label MO2 REFERENCE A32848 !$#authors Moore, S.K.; Kozak, C.; Robinson, E.A.; Ullrich, S.J.; !1Appella, E. !$#journal J. Biol. Chem. (1989) 264:5343-5351 !$#title Murine 86- and 84-kDa heat shock proteins, cDNA sequences, !1chromosome assignments, and evolutionary origins. !$#cross-references MUID:89174568; PMID:2925609 !$#accession A32848 !'##molecule_type mRNA !'##residues 1-724 ##label MOO REFERENCE PS0020 !$#authors Hoffmann, T.; Hovemann, B. !$#journal Gene (1988) 74:491-501 !$#title Heat-shock proteins, Hsp84 and Hsp86, of mice and men: two !1related genes encode formerly identified tumour-specific !1transplantation antigens. !$#cross-references MUID:89232740; PMID:2469626 !$#accession JS0099 !'##molecule_type mRNA !'##residues 1-496,'P',498-724 ##label HOF COMMENT This protein is one of two forms of 80-90 kDa heat shock !1proteins found in mice. These are abundant in the cytoplasm !1of unstressed cells and are moderately induced by heat !1shock. GENETICS !$#gene hsp84 CLASSIFICATION #superfamily heat shock protein 90 KEYWORDS estrogen-induced protein; heat shock; phosphoprotein; !1steroid receptor complex; stress-induced protein SUMMARY #length 724 #molecular-weight 83281 #checksum 3638 SEQUENCE /// ENTRY HHCH08 #type complete TITLE heat shock protein 108 precursor - chicken ALTERNATE_NAMES transferrin-binding protein ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 22-Jun-1999 ACCESSIONS A24461; JC2205; PC2135; A31964 REFERENCE A24461 !$#authors Kulomaa, M.S.; Weigel, N.L.; Kleinsek, D.A.; Beattie, W.G.; !1Conneely, O.M.; March, C.; Zarucki-Schulz, T.; Schrader, !1W.T.; O'Malley, B.W. !$#journal Biochemistry (1986) 25:6244-6251 !$#title Amino acid sequence of a chicken heat shock protein derived !1from the complementary DNA nucleotide sequence. !$#cross-references MUID:87076542; PMID:3024703 !$#accession A24461 !'##molecule_type mRNA !'##residues 1-795 ##label KUL !'##cross-references GB:M14772; NID:g211942; PIDN:AAA48826.1; !1PID:g211943 REFERENCE JC2205 !$#authors Hayes, G.R.; Himpler, B.S.; Weiner, K.X.B.; Lucas, J.J. !$#journal Biochem. Biophys. Res. Commun. (1994) 200:65-70 !$#title A chicken transferrin binding protein is heat shock protein !1108. !$#cross-references MUID:94220155; PMID:8166742 !$#accession JC2205 !'##molecule_type mRNA !'##residues 1-795 ##label HAY !$#accession PC2135 !'##molecule_type protein !'##residues !124-34;75-83;101-109;142-151;213-214;216-229;259-262;272-280; !1285-294;479-483;502-508;608-619;684-687;700-707;709;724-730 !1##label HA2 !'##note failure of the protein to react with an anti-KDEL monoclonal !1antibody suggests the KDEL sequence is removed or modified REFERENCE A31964 !$#authors Poola, I.; Lucas, J.J. !$#journal J. Biol. Chem. (1988) 263:19137-19146 !$#title Purification and characterization of an estrogen-inducible !1membrane glycoprotein. Evidence that it is a transferrin !1receptor. !$#cross-references MUID:89066718; PMID:3198616 !$#accession A31964 !'##molecule_type protein !'##residues 'XX',24-33,'E' ##label POO COMMENT This protein is a disulfide-linked homodimer and is tightly !1membrane bound. It contains both N- and O-linked !1carbohydrate. CLASSIFICATION #superfamily heat shock protein 90 KEYWORDS estrogen-induced protein; glycoprotein; heat shock; !1homodimer; membrane protein; stress-induced protein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$792-795 #region endoplasmic reticulum retention signal\ !$216 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 795 #molecular-weight 91554 #checksum 4431 SEQUENCE /// ENTRY HHBY90 #type complete TITLE heat shock protein 90 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein P1045; protein YPL240c ORGANISM #formal_name Saccharomyces cerevisiae DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 21-Jul-2000 ACCESSIONS A03313; S61024; S65269 REFERENCE A03313 !$#authors Farrelly, F.W.; Finkelstein, D.B. !$#journal J. Biol. Chem. (1984) 259:5745-5751 !$#title Complete sequence of the heat shock-inducible HSP90 gene of !1Saccharomyces cerevisiae. !$#cross-references MUID:84185722; PMID:6325446 !$#accession A03313 !'##molecule_type DNA !'##residues 1-709 ##label FAR !'##cross-references EMBL:K01387; NID:g171724; PIDN:AAA02743.1; !1PID:g171725 REFERENCE S61010 !$#authors Pohl, T.M. !$#submission submitted to the EMBL Data Library, November 1995 !$#accession S61024 !'##molecule_type DNA !'##residues 1-709 ##label POH !'##cross-references EMBL:Z67751; NID:g1061234; PIDN:CAA91604.1; !1PID:g1061249 REFERENCE S64899 !$#authors Pohl, T.M. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S65269 !'##molecule_type DNA !'##residues 1-709 ##label POW !'##cross-references EMBL:Z73596; NID:g1370494; PIDN:CAA97961.1; !1PID:g1370495; GSPDB:GN00016; MIPS:YPL240c !'##experimental_source strain S288C (AB972) GENETICS !$#gene SGD:HSP82; HSP90; MIPS:YPL240c !'##cross-references SGD:S0006161; MIPS:YPL240c !$#map_position 16L CLASSIFICATION #superfamily heat shock protein 90 KEYWORDS heat shock; stress-induced protein SUMMARY #length 709 #molecular-weight 81406 #checksum 9780 SEQUENCE /// ENTRY HHFF83 #type complete TITLE heat shock protein 83 - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 25-Feb-1985 #sequence_revision 13-Mar-1997 #text_change 24-Sep-1999 ACCESSIONS A24827; A03312 REFERENCE A92925 !$#authors Blackman, R.K.; Meselson, M. !$#journal J. Mol. Biol. (1986) 188:499-515 !$#title Interspecific nucleotide sequence comparisons used to !1identify regulatory and structural features of the !1Drosophila hsp82 gene. !$#cross-references MUID:86281707; PMID:2426456 !$#accession A24827 !'##molecule_type DNA !'##residues 1-717 ##label BLA !'##cross-references GB:X03810; NID:g8125; PIDN:CAA27435.1; PID:g8127 REFERENCE A03312 !$#authors Hackett, R.W.; Lis, J.T. !$#journal Nucleic Acids Res. (1983) 11:7011-7030 !$#title Localization of the hsp83 transcript within a 3292 !1nucleotide sequence from the 63B heat shock locus of !1Drosophila melanogaster. !$#cross-references MUID:84041500; PMID:6314271 !$#accession A03312 !'##molecule_type mRNA !'##residues 1-375 ##label HAC !'##cross-references GB:X00065; GB:K01685; NID:g8101; PIDN:CAA24938.1; !1PID:g8102 COMMENT In contrast to other major heat shock proteins, this one is !1also expressed at normal growth temperatures. GENETICS !$#gene FlyBase:Hsp83 !'##cross-references FlyBase:FBgn0001233 !$#map_position 3L (63B) CLASSIFICATION #superfamily heat shock protein 90 KEYWORDS heat shock; stress-induced protein SUMMARY #length 717 #molecular-weight 81865 #checksum 1730 SEQUENCE /// ENTRY HHEC62 #type complete TITLE heat shock protein C62.5 - Escherichia coli (strain K-12) ALTERNATE_NAMES high temperature protein G ORGANISM #formal_name Escherichia coli DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 01-Mar-2002 ACCESSIONS A28324; H64777 REFERENCE A28324 !$#authors Bardwell, J.C.A.; Craig, E.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:5177-5181 !$#title Eukaryotic Mr 83,000 heat shock protein has a homologue in !1Escherichia coli. !$#cross-references MUID:87260952; PMID:3299380 !$#accession A28324 !'##molecule_type DNA !'##residues 1-624 ##label BAR !'##cross-references GB:M38777; NID:g145295; PIDN:AAA23460.1; !1PID:g145300 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64777 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-624 ##label BLAT !'##cross-references GB:AE000153; GB:U00096; NID:g1786671; !1PIDN:AAC73575.1; PID:g1786679; UWGP:b0473 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene htpG !$#map_position 11 min FUNCTION !$#description has ATPase activity CLASSIFICATION #superfamily heat shock protein 90 KEYWORDS ATP binding; heat shock; molecular chaperone; stress-induced !1protein SUMMARY #length 624 #molecular-weight 71422 #checksum 1630 SEQUENCE /// ENTRY S19647 #type complete TITLE T-complex protein 1 homolog - Sulfolobus shibatae ALTERNATE_NAMES thermophilic factor 55 ORGANISM #formal_name Sulfolobus shibatae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S19647 REFERENCE S19647 !$#authors Trent, J.D.; Nimmesgern, E.; Wall, J.S.; Hartl, F.U.; !1Horwich, A.L. !$#journal Nature (1991) 354:490-493 !$#title A molecular chaperone from a thermophilic archaebacterium is !1related to the eukaryotic protein t-complex polypeptide-1. !$#cross-references MUID:92086050; PMID:1836250 !$#accession S19647 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-552 ##label TRE !'##cross-references GB:X63834; GB:S70432; NID:g49043; PIDN:CAA45326.1; !1PID:g49044 CLASSIFICATION #superfamily molecular chaperone t-complex-type SUMMARY #length 552 #molecular-weight 59682 #checksum 7700 SEQUENCE /// ENTRY HHECDJ #type complete TITLE heat shock protein dnaJ - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 01-Mar-2002 ACCESSIONS A92572; A26298; S40537; G64721; A26299 REFERENCE A92572 !$#authors Bardwell, J.C.A.; Tilly, K.; Craig, E.; King, J.; Zylicz, !1M.; Georgopoulos, C. !$#journal J. Biol. Chem. (1986) 261:1782-1785 !$#title The nucleotide sequence of the Escherichia coli K12 dnaJ !1gene. !$#cross-references MUID:86111850; PMID:3003085 !$#accession A92572 !'##molecule_type DNA !'##residues 1-376 ##label BAR !'##cross-references GB:M12565; NID:g145767; PIDN:AAA23693.1; !1PID:g145769 !'##experimental_source strain K12 REFERENCE A26298 !$#authors Ohki, M.; Tamura, F.; Nishimura, S.; Uchida, H. !$#journal J. Biol. Chem. (1986) 261:1778-1781 !$#title Nucleotide sequence of the Escherichia coli dnaJ gene and !1purification of the gene product. !$#cross-references MUID:86111849; PMID:3003084 !$#accession A26298 !'##molecule_type DNA !'##residues 1-376 ##label OHK !'##cross-references GB:D10483; GB:J01597; GB:J01683; GB:J01706; !1GB:K01298; GB:K01990; GB:M10420; GB:M10611; GB:M12544; !1NID:g216434; PIDN:BAA01292.1; PID:g216441 REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40537 !'##molecule_type DNA !'##residues 1-376 ##label YUR !'##cross-references EMBL:D10483; NID:g216434; PIDN:BAA01292.1; !1PID:g216441 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64721 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-376 ##label BLAT !'##cross-references GB:AE000112; GB:U00096; NID:g1786192; !1PIDN:AAC73126.1; PID:g1786197; UWGP:b0015 !'##experimental_source strain K-12, substrain MG1655 COMMENT This protein is induced by heat shock under the control of !1the htpR gene product, heat shock regulatory protein. It is !1required for lambda DNA replication at all temperatures. GENETICS !$#gene dnaJ !$#map_position 0 min CLASSIFICATION #superfamily heat shock protein dnaJ; dnaJ amino-terminal !1homology KEYWORDS DNA replication; heat shock; molecular chaperone; !1stress-induced protein FEATURE !$5-70 #domain dnaJ amino-terminal homology #label DNJ\ !$77-106 #region G/F motif\ !$144-151 #region CXXCXGXG repeat\ !$161-168 #region CXXCXGXG repeat\ !$183-190 #region CXXCXGXG repeat\ !$197-204 #region CXXCXGXG repeat SUMMARY #length 376 #molecular-weight 41100 #checksum 2314 SEQUENCE /// ENTRY JT0761 #type complete TITLE heat shock protein hslU - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS JT0761; S40874; F65199 REFERENCE JT0760 !$#authors Chuang, S.E.; Burland, V.; Plunkett III, G.; Daniels, D.L.; !1Blattner, F.R. !$#journal Gene (1993) 134:1-6 !$#title Sequence analysis of four new heat-shock genes constituting !1the hslTS/ibpAB and hslVU operons in Escherichia coli. !$#cross-references MUID:94063501; PMID:8244018 !$#accession JT0761 !'##molecule_type DNA !'##residues 1-443 ##label CHU REFERENCE S40802 !$#authors Plunkett III, G.; Burland, V.; Daniels, D.L.; Blattner, F.R. !$#journal Nucleic Acids Res. (1993) 21:3391-3398 !$#title Analysis of the Escherichia coli genome. III. DNA sequence !1of the region from 87.2 to 89.2 minutes. !$#cross-references MUID:93347969; PMID:8346018 !$#accession S40874 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-443 ##label PLU !'##cross-references EMBL:L19201; NID:g304961; PIDN:AAB03063.1; !1PID:g305034 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1993 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65199 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-443 ##label BLAT !'##cross-references GB:AE000467; GB:U00096; NID:g1790356; !1PIDN:AAC76913.1; PID:g1790366; UWGP:b3931 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene hslU CLASSIFICATION #superfamily heat shock protein hslU; FtsH/SEC18/CDC48-type !1ATP-binding domain homology; shikimate kinase homology KEYWORDS ATP; GTP binding; heat shock; nucleotide binding; P-loop; !1stress-induced protein FEATURE !$57-64 #region nucleotide-binding motif A (P-loop) SUMMARY #length 443 #molecular-weight 49593 #checksum 548 SEQUENCE /// ENTRY D64072 #type complete TITLE probable heat shock protein HI0497 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS D64072 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession D64072 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-466 ##label TIGR !'##cross-references GB:L42023; TIGR:HI0497 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily heat shock protein hslU; FtsH/SEC18/CDC48-type !1ATP-binding domain homology; shikimate kinase homology KEYWORDS nucleotide binding; P-loop FEATURE !$79-86 #region nucleotide-binding motif A (P-loop) SUMMARY #length 466 #molecular-weight 51920 #checksum 8571 SEQUENCE /// ENTRY S27609 #type complete TITLE hypothetical protein 1 - Pasteurella haemolytica ORGANISM #formal_name Pasteurella haemolytica DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S27609 REFERENCE S27609 !$#authors Highlander, S.K.; Wickersham, E.A.; Weinstock, G.M. !$#submission submitted to the EMBL Data Library, February 1992 !$#accession S27609 !'##molecule_type DNA !'##residues 1-387 ##label HIG !'##cross-references EMBL:M59210 CLASSIFICATION #superfamily heat shock protein hslU; FtsH/SEC18/CDC48-type !1ATP-binding domain homology; shikimate kinase homology KEYWORDS nucleotide binding; P-loop FEATURE !$3-10 #region nucleotide-binding motif A (P-loop) SUMMARY #length 387 #molecular-weight 43514 #checksum 35 SEQUENCE /// ENTRY D64584 #type complete TITLE heat shock protein - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS D64584 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession D64584 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-443 ##label TOM !'##cross-references GB:AE000566; GB:AE000511; NID:g2313628; !1PIDN:AAD07584.1; PID:g2313631; TIGR:HP0516 CLASSIFICATION #superfamily heat shock protein hslU; FtsH/SEC18/CDC48-type !1ATP-binding domain homology; shikimate kinase homology KEYWORDS nucleotide binding; P-loop FEATURE !$59-66 #region nucleotide-binding motif A (P-loop) SUMMARY #length 443 #molecular-weight 50190 #checksum 3835 SEQUENCE /// ENTRY G69862 #type complete TITLE heat-shock protein homolog ykrL - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS G69862 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69862 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-298 ##label KUN !'##cross-references GB:Z99111; GB:AL009126; NID:g2633699; !1PIDN:CAB13222.1; PID:g2633720 !'##experimental_source strain 168 GENETICS !$#gene ykrL CLASSIFICATION #superfamily heat-shock protein htpX SUMMARY #length 298 #molecular-weight 32865 #checksum 1223 SEQUENCE /// ENTRY A43659 #type complete TITLE heat shock protein htpX - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS A43659; E64944 REFERENCE A43659 !$#authors Kornitzer, D.; Teff, D.; Altuvia, S.; Oppenheim, A.B. !$#journal J. Bacteriol. (1991) 173:2944-2953 !$#title Isolation, characterization, and sequence of an Escherichia !1coli heat shock gene, htpX. !$#cross-references MUID:91210186; PMID:1826904 !$#accession A43659 !'##status preliminary !'##molecule_type DNA !'##residues 1-293 ##label KOR !'##cross-references GB:M58470; NID:g146411; PIDN:AAA62779.1; !1PID:g146412 !'##note induced by temperature upshift; overexpression of a truncated !1form of the protein display a higher rate of degradation of !1puromycyl peptides REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64944 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-293 ##label BLAT !'##cross-references GB:AE000277; GB:U00096; NID:g1788129; !1PIDN:AAC74899.1; PID:g1788133; UWGP:b1829 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene htpX CLASSIFICATION #superfamily heat-shock protein htpX KEYWORDS ATP; heat shock; metalloproteinase; nucleotide binding; !1P-loop; transmembrane protein; zinc FEATURE !$6-22 #domain transmembrane #status predicted #label TM1\ !$36-52 #domain transmembrane #status predicted #label TM2\ !$150-166 #domain transmembrane #status predicted #label TM3\ !$197-213 #domain transmembrane #status predicted #label TM4\ !$259-266 #region nucleotide-binding motif A (P-loop)\ !$139,143 #binding_site zinc (His) #status predicted\ !$140 #active_site Glu #status predicted SUMMARY #length 293 #molecular-weight 31923 #checksum 8018 SEQUENCE /// ENTRY H64088 #type complete TITLE heat shock protein htpX - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS H64088 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession H64088 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-283 ##label TIGR !'##cross-references GB:U32755; GB:L42023; NID:g3212203; !1PIDN:AAC22378.1; PID:g1573723; TIGR:HI0720 GENETICS !$#gene htpX CLASSIFICATION #superfamily heat-shock protein htpX KEYWORDS ATP; heat shock; metalloproteinase; P-loop; transmembrane !1protein; zinc FEATURE !$12-28 #domain transmembrane #status predicted #label TM1\ !$35-51 #domain transmembrane #status predicted #label TM2\ !$150-166 #domain transmembrane #status predicted #label TM3\ !$193-209 #domain transmembrane #status predicted #label TM4\ !$139,143 #binding_site zinc (His) #status predicted\ !$140 #active_site Glu #status predicted SUMMARY #length 283 #molecular-weight 30780 #checksum 8145 SEQUENCE /// ENTRY H64509 #type complete TITLE heat shock protein X - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H64509 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession H64509 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-284 ##label BUL !'##cross-references GB:U67608; GB:L77117; NID:g1592245; !1PIDN:AAB99703.1; PID:g1592249; TIGR:MJ1682 GENETICS !$#map_position REV1664869-1664015 CLASSIFICATION #superfamily heat-shock protein htpX SUMMARY #length 284 #molecular-weight 31972 #checksum 8768 SEQUENCE /// ENTRY C69175 #type complete TITLE heat shock protein X - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C69175 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession C69175 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-258 ##label MTH !'##cross-references GB:AE000839; GB:AE000666; NID:g2621637; !1PIDN:AAB85075.1; PID:g2621646 !'##experimental_source strain Delta H GENETICS !$#gene MTH569 CLASSIFICATION #superfamily heat-shock protein htpX SUMMARY #length 258 #molecular-weight 28605 #checksum 5777 SEQUENCE /// ENTRY G64635 #type complete TITLE heat shock protein - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS G64635 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession G64635 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-326 ##label TOM !'##cross-references GB:AE000602; GB:AE000511; NID:g2314060; !1PIDN:AAD07972.1; PID:g2314064; TIGR:HP0927 CLASSIFICATION #superfamily heat-shock protein htpX SUMMARY #length 326 #molecular-weight 37353 #checksum 5743 SEQUENCE /// ENTRY HHGQ60 #type complete TITLE heat shock protein 60 - Giardia lamblia ORGANISM #formal_name Giardia lamblia DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 22-Jun-1999 ACCESSIONS S10237 REFERENCE S10237 !$#authors Aggarwal, A.; de la Cruz, V.F.; Nash, T.E. !$#journal Nucleic Acids Res. (1990) 18:3409 !$#title A heat shock protein gene in Giardia lamblia unrelated to !1HSP70. !$#cross-references MUID:90287732; PMID:2356135 !$#accession S10237 !'##molecule_type DNA !'##residues 1-529 ##label AGG !'##cross-references EMBL:X16738; NID:g9360; PIDN:CAA34711.1; PID:g9361 !'##note the authors translated the codon AGC for residue 422 as Leu, !1GCA for residue 423 as Ser, and CTT for residue 424 as Ala CLASSIFICATION #superfamily heat shock protein 60 KEYWORDS heat shock; stress-induced protein SUMMARY #length 529 #molecular-weight 60251 #checksum 5988 SEQUENCE /// ENTRY HHBYD8 #type complete TITLE heat shock protein DDR48 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES DNA damage-responsive protein 48; flocculent-specific protein; protein YM8010.03; protein YMR173w ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1991 #sequence_revision 17-Nov-1995 #text_change 21-Jul-2000 ACCESSIONS S55120; A36331; JC2263; S46652; A45429; S22874; PC2182; !1S12203 REFERENCE S55118 !$#authors Churcher, C.M. !$#submission submitted to the EMBL Data Library, June 1995 !$#accession S55120 !'##molecule_type DNA !'##residues 1-430 ##label CHU !'##cross-references EMBL:Z49808; NID:g854440; PIDN:CAA89906.1; !1PID:g854443; GSPDB:GN00013; MIPS:YMR173w !'##experimental_source strain AB972 REFERENCE A36331 !$#authors Treger, J.M.; McEntee, K. !$#journal Mol. Cell. Biol. (1990) 10:3174-3184 !$#title Structure of the DNA damage-inducible gene DDR48 and !1evidence for its role in mutagenesis in Saccharomyces !1cerevisiae. !$#cross-references MUID:90258909; PMID:2111448 !$#accession A36331 !'##molecule_type DNA !'##residues 1-37,'Q',39-430 ##label TRE !'##cross-references EMBL:M36110; NID:g171387; PIDN:AAA34563.1; !1PID:g171388 REFERENCE JC2263 !$#authors Tonouchi, A.; Fujita, A.; Kuhara, S. !$#journal J. Biochem. (1994) 115:683-688 !$#title Molecular cloning of the gene encoding a highly expressed !1protein in SFL1 gene-disrupted flocculating yeast. !$#cross-references MUID:94375413; PMID:8089083 !$#accession JC2263 !'##molecule_type DNA !'##residues 1-430 ##label TON !'##cross-references GB:S73336; NID:g685014; PIDN:AAB31954.1; !1PID:g685015 !$#accession S46652 !'##molecule_type protein !'##residues 2-11 ##label TO2 REFERENCE A45429 !$#authors Sheng, S.; Schuster, S.M. !$#journal J. Biol. Chem. (1993) 268:4752-4758 !$#title Purification and characterization of Saccharomyces !1cerevisiae DNA damage-responsive protein 48 (DDRP 48). !$#cross-references MUID:93186777; PMID:8444852 !$#accession A45429 !'##molecule_type protein !'##residues 2-31 ##label SHE !'##note sequence modified after extraction from NCBI backbone REFERENCE S22874 !$#authors Carabaza, A.; Arino, J.; Fox, J.W.; Villar-Palasi, C.; !1Guinovart, J.J. !$#journal Biochem. J. (1990) 268:401-407 !$#title Purification, characterization and partial amino acid !1sequence of glycogen synthase from Saccharomyces cerevisiae. !$#cross-references MUID:90303218; PMID:2114092 !$#accession S22874 !'##molecule_type protein !'##residues 2-8,'E',10-12 ##label CAR !'##experimental_source strain ABYS-minus !'##note this protein was identified as UDPglucose-starch !1glucosyltransferase (EC 2.4.1.11) GENETICS !$#gene SGD:DDR48; MIPS:YMR173w !'##cross-references SGD:S0004784; MIPS:YMR173w !$#map_position 13R CLASSIFICATION #superfamily heat shock protein DDR48 KEYWORDS glycoprotein; heat shock; stress-induced protein; tandem !1repeat FEATURE !$2-430 #product heat shock protein DDR48 #status !8experimental #label MAT\ !$74-414 #region 8-residue repeats\ !$18,66,72,77,85,93, !$101,109,144,152, !$160,177,212,228, !$263,280,343,378 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 430 #molecular-weight 46233 #checksum 1429 SEQUENCE /// ENTRY HHBY12 #type complete TITLE heat shock protein 12 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YFL014w ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jun-2000 ACCESSIONS S11179; S20215; JQ0889; S20216; S48318; S56240; S62299; !1S12949 REFERENCE S11179 !$#authors Praekelt, U.M.; Meacock, P.A. !$#journal Mol. Gen. Genet. (1990) 223:97-106 !$#title HSP12, a new small heat shock gene of Saccharomyces !1cerevisiae: analysis of structure, regulation and function. !$#cross-references MUID:91080870; PMID:2175390 !$#accession S11179 !'##molecule_type DNA !'##residues 1-109 ##label PRA1 !'##cross-references EMBL:X55785; NID:g3799; PIDN:CAA39306.1; PID:g3800 !$#accession S20215 !'##molecule_type mRNA !'##residues 1-109 ##label PRA2 !'##cross-references GB:X55785; NID:g3799; PIDN:CAA39306.1; PID:g3800 REFERENCE JQ0889 !$#authors Stone, R.L.; Matarese, V.; Magee, B.B.; Magee, P.T.; !1Bernlohr, D.A. !$#journal Gene (1990) 96:171-176 !$#title Cloning, sequencing and chromosomal assignment of a gene !1from Saccharomyces cerevisiae which is negatively regulated !1by glucose and positively by lipids. !$#cross-references MUID:91099672; PMID:2129531 !$#accession JQ0889 !'##molecule_type DNA !'##residues 1-109 ##label STO !'##cross-references GB:M60827; NID:g171606; PIDN:AAA34647.1; !1PID:g171607 !'##note the authors translated the codon AAG for residue 23 as Arg !$#accession S20216 !'##molecule_type protein !'##residues 25-30;45-50 ##label STO2 REFERENCE S48310 !$#authors Churcher, C. !$#submission submitted to the EMBL Data Library, September 1994 !$#accession S48318 !'##molecule_type DNA !'##residues 1-109 ##label CHU !'##cross-references EMBL:Z46255; NID:g559925; PIDN:CAA86349.1; !1PID:g559934; GSPDB:GN00006; MIPS:YFL014w REFERENCE S56186 !$#authors Murakami, Y.; Naitou, M.; Hagiwara, H.; Shibata, T.; Ozawa, !1M.; Sasanuma, S.I.; Sasanuma, M.; Tsuchiya, Y.; Soeda, E.; !1Yokoyama, K.; Yamazaki, M.; Tashiro, H.; Eki, T. !$#submission submitted to the EMBL Data Library, May 1995 !$#description Analysis of the nucleotide sequence of chromosome VI from !1Saccaromyces cerevisiae. !$#accession S56240 !'##molecule_type DNA !'##residues 1-109 ##label MUR !'##cross-references EMBL:D50617; NID:g836685; PIDN:BAA09224.1; !1PID:g836740; GSPDB:GN00006; MIPS:YFL014w REFERENCE S62230 !$#authors Murakami, Y. !$#submission submitted to the EMBL Data Library, December 1994 !$#accession S62299 !'##molecule_type DNA !'##residues 1-109 ##label MUW !'##cross-references EMBL:D44596; NID:g1100783; PIDN:BAA08003.1; !1PID:g1100790 GENETICS !$#gene SGD:HSP12; GLP1; MIPS:YFL014w !'##cross-references SGD:S0001880; MIPS:YFL014w !$#map_position 6L CLASSIFICATION #superfamily heat shock protein 12 KEYWORDS heat shock; stress-induced protein SUMMARY #length 109 #molecular-weight 11693 #checksum 8362 SEQUENCE /// ENTRY S25478 #type complete TITLE heat shock transcription factor HSF8 - tomato ORGANISM #formal_name Lycopersicon esculentum #common_name tomato DATE 20-Feb-1995 #sequence_revision 20-Feb-1995 #text_change 22-Jun-1999 ACCESSIONS S25478 REFERENCE S25478 !$#authors Scharf, K.D. !$#submission submitted to the EMBL Data Library, July 1992 !$#accession S25478 !'##molecule_type DNA !'##residues 1-527 ##label SCH !'##cross-references EMBL:X67599; NID:g19259; PIDN:CAA47868.1; !1PID:g19260 GENETICS !$#gene hsf8 !$#introns 98/3 FUNCTION !$#description transcription factor that binds to heat shock promoter !1elements CLASSIFICATION #superfamily tomato heat shock transcription factor HSF8; !1HSF DNA-binding domain homology KEYWORDS DNA binding; heat shock; leucine zipper; nucleus; !1stress-induced protein; transcription regulation FEATURE !$40-135 #domain HSF DNA-binding domain homology #label HSF\ !$170-191 #region leucine zipper SUMMARY #length 527 #molecular-weight 57700 #checksum 2274 SEQUENCE /// ENTRY S25481 #type complete TITLE heat shock transcription factor HSF8 - Peruvian tomato ORGANISM #formal_name Lycopersicon peruvianum #common_name Peruvian tomato DATE 20-Feb-1995 #sequence_revision 20-Feb-1995 #text_change 22-Jun-1999 ACCESSIONS S25481 REFERENCE S25480 !$#authors Scharf, K.D.; Materna, T.; Rose, S.; Thierfelder, J.; !1Treuter, E.; Nover, L. !$#submission submitted to the EMBL Data Library, July 1992 !$#description Sequence expression and functional analysis of tomato heat !1stress transcription factors. !$#accession S25481 !'##molecule_type mRNA !'##residues 1-527 ##label SCH !'##cross-references EMBL:X67600; NID:g19491; PIDN:CAA47869.1; !1PID:g19492 GENETICS !$#gene hsf8 FUNCTION !$#description transcription factor that binds to heat shock promoter !1elements CLASSIFICATION #superfamily tomato heat shock transcription factor HSF8; !1HSF DNA-binding domain homology KEYWORDS DNA binding; heat shock; leucine zipper; nucleus; !1stress-induced protein; transcription regulation FEATURE !$42-137 #domain HSF DNA-binding domain homology #label HSF\ !$172-193 #region leucine zipper SUMMARY #length 527 #molecular-weight 57519 #checksum 3975 SEQUENCE /// ENTRY S52641 #type complete TITLE heat shock transcription factor HSF1 - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress #variety columbia DATE 01-Aug-1995 #sequence_revision 24-Mar-1999 #text_change 16-Jun-2000 ACCESSIONS F71447; S52641; S62227; S38873 REFERENCE A71400 !$#authors Bevan, M.; Bancroft, I.; Bent, E.; Love, K.; Goodman, H.; !1Dean, C.; Bergkamp, R.; Dirkse, W.; Van Staveren, M.; !1Stiekema, W.; Drost, L.; Ridley, P.; Hudson, S.A.; Patel, !1K.; Murphy, G.; Piffanelli, P.; Wedler, H.; Wedler, E.; !1Wambutt, R.; Weitzenegger, T.; Pohl, T.M.; Terryn, N.; !1Gielen, J.; Villarroel, R.; De Clerck, R.; Van Montagu, M.; !1Lecharny, A.; Auborg, S.; Gy, I.; Kreis, M.; Lao, N.; !1Kavanagh, T.; Hempel, S.; Kotter, P.; Entian, K.D.; Rieger, !1M.; Schaeffer, M.; Funk, B.; Mueller-Auer, S.; Silvey, M.; !1James, R.; Montfort, A.; Pons, A.; Puigdomenech, P.; Douka, !1A.; Voukelatou, E.; Milioni, D.; Hatzopoulos, P.; Piravandi, !1E.; Obermaier, B.; Hilbert, H.; Duesterhoft, A.; Moores, T.; !1Jones, J.D.G.; Eneva, T.; Palme, K.; Benes, V.; Rechman, S.; !1Ansorge, W.; Cooke, R.; Berger, C.; Delseny, M.; Voet, M.; !1Volckaert, G.; Mewes, H.W.; Klosterman, S.; Schueller, C.; !1Chalwatzis, N. !$#journal Nature (1998) 391:485-488 !$#title Analysis of 1.9 Mb of contiguous sequence from chromosome 4 !1of Arabidopsis thaliana. !$#cross-references MUID:98121113; PMID:9461215 !$#accession F71447 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-495 ##label BEV !'##cross-references GB:Z97344; NID:g2245126; PIDN:CAB10555.1; !1PID:g2245134 REFERENCE S52641 !$#authors Huebel, A.; Schoeffl, F. !$#journal Plant Mol. Biol. (1994) 26:353-362 !$#title Arabidopsis heat shock factor: isolation and !1characterization of the gene and the recombinant protein. !$#cross-references MUID:95036006; PMID:7948881 !$#accession S52641 !'##molecule_type DNA !'##residues 1-215,'M',217-284,'D',286-335,'T',337-389,'Y',391-469, !1474-495 ##label HUE !'##cross-references EMBL:X76167 !$#accession S62227 !'##molecule_type mRNA !'##residues 31-215,'M',217-284,'D',286-335,'T',337-389,'Y',391-469, !1474-495 ##label HUW REFERENCE S38873 !$#authors Huebel, A.; Schoeffl, F. !$#submission submitted to the EMBL Data Library, November 1993 !$#description Arabidopsis heat shock factor: isolation and !1characterization of the gene and the recombinant protein. !$#accession S38873 !'##molecule_type DNA !'##residues 1-215,'M',217-284,'D',286-335,'T',337-389,'Y',391-461, !1474-495 ##label HUF !'##cross-references EMBL:X76167; NID:g429154; PIDN:CAA53761.1; !1PID:g429155 GENETICS !$#gene HSF1 !$#map_position 4COP9-4G3845 !$#introns 111/3 FUNCTION TFC !$#description transcription factor that binds to heat shock promoter !1elements CLASSIFICATION #superfamily tomato heat shock transcription factor HSF8; !1HSF DNA-binding domain homology KEYWORDS DNA binding; heat shock; leucine zipper; nucleus; !1stress-induced protein; transcription regulation FEATURE !$53-148 #domain HSF DNA-binding domain homology #label HSF\ !$181-202 #region leucine zipper SUMMARY #length 495 #molecular-weight 55744 #checksum 774 SEQUENCE /// ENTRY S12361 #type complete TITLE heat shock transcription factor HSF24 - Peruvian tomato ORGANISM #formal_name Lycopersicon peruvianum #common_name Peruvian tomato DATE 07-Oct-1994 #sequence_revision 07-Oct-1994 #text_change 22-Jun-1999 ACCESSIONS S12361 REFERENCE S12361 !$#authors Scharf, K.D.; Rose, S.; Zott, W.; Schoeff, F.; Nover, L. !$#journal EMBO J. (1990) 9:4495-4501 !$#title Three tomato genes code for heat stress transcription !1factors with a region of remarkable homology to the !1DNA-binding domain of the yeast HSF. !$#cross-references MUID:91092274; PMID:2148291 !$#accession S12361 !'##molecule_type mRNA !'##residues 1-301 ##label SCH !'##cross-references EMBL:X55347; NID:g19487; PIDN:CAA39034.1; !1PID:g19488 GENETICS !$#gene hsf24 FUNCTION !$#description binding of HSF to heat shock promoter elements activates !1transcription of heat shock genes CLASSIFICATION #superfamily tomato heat shock transcription factor HSF24; !1HSF DNA-binding domain homology KEYWORDS DNA binding; heat shock; nucleus; stress-induced protein; !1transcription regulation FEATURE !$10-105 #domain HSF DNA-binding domain homology #label HSF SUMMARY #length 301 #molecular-weight 33195 #checksum 364 SEQUENCE /// ENTRY S59538 #type complete TITLE heat shock transcription factor HSF34 - soybean ORGANISM #formal_name Glycine max #common_name soybean DATE 15-Feb-1996 #sequence_revision 01-Mar-1996 #text_change 22-Jun-1999 ACCESSIONS S59538; S52304 REFERENCE S59537 !$#authors Czarnecka-Verner, E.; Yuan, C.X.; Fox, P.C.; Gurley, W.B. !$#journal Plant Mol. Biol. (1995) 29:37-51 !$#title Isolation and characterization of six heat shock !1transcription factor cDNA clones from soybean. !$#cross-references MUID:96017612; PMID:7579166 !$#accession S59538 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-282 ##label CZA !'##cross-references EMBL:Z46953; NID:g662929; PIDN:CAA87077.1; !1PID:g662930 GENETICS !$#gene HSF34 FUNCTION !$#description binding of HSF to heat shock promoter elements activates !1transcription of heat shock genes CLASSIFICATION #superfamily tomato heat shock transcription factor HSF24; !1HSF DNA-binding domain homology KEYWORDS DNA binding; heat shock; leucine zipper; nucleus; !1stress-induced protein; transcription regulation FEATURE !$10-105 #domain HSF DNA-binding domain homology #label HSF\ !$252-280 #region leucine zipper SUMMARY #length 282 #molecular-weight 31194 #checksum 6777 SEQUENCE /// ENTRY S71851 #type complete TITLE heat shock transcription factor HSF4 - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 05-Dec-1996 #sequence_revision 13-Mar-1997 #text_change 22-Jun-1999 ACCESSIONS S71851 REFERENCE S71851 !$#authors Barros, D.; Czarnecka-Verner, E.; Yuan, C.X.; Baldwin, D.; !1Gurley, W. !$#submission submitted to the EMBL Data Library, August 1996 !$#description Cloning of two cDNAs encoding heat shock transcription !1factors from Arabidopsis. !$#accession S71851 !'##molecule_type mRNA !'##residues 1-284 ##label BAR !'##cross-references EMBL:U68017; NID:g1619920; PIDN:AAC31756.1; !1PID:g1619921 GENETICS !$#gene HSF4 FUNCTION !$#description binding of HSF to heat shock promoter elements activates !1transcription of heat shock genes CLASSIFICATION #superfamily tomato heat shock transcription factor HSF24; !1HSF DNA-binding domain homology KEYWORDS DNA binding; heat shock; leucine zipper; nucleus; !1stress-induced protein; transcription regulation FEATURE !$15-110 #domain HSF DNA-binding domain homology #label HSF\ !$149-170 #region leucine zipper SUMMARY #length 284 #molecular-weight 31397 #checksum 3534 SEQUENCE /// ENTRY A31593 #type complete TITLE heat shock transcription factor HSF1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein G3257; protein YGL073w ORGANISM #formal_name Saccharomyces cerevisiae DATE 28-Feb-1990 #sequence_revision 28-Feb-1990 #text_change 21-Jul-2000 ACCESSIONS A31593; S64080; A31592; S26253 REFERENCE A31593 !$#authors Sorger, P.K.; Pelham, H.R.B. !$#journal Cell (1988) 54:855-864 !$#title Yeast heat shock factor is an essential DNA-binding protein !1that exhibits temperature-dependent phosphorylation. !$#cross-references MUID:88311088; PMID:3044613 !$#accession A31593 !'##molecule_type DNA !'##residues 1-833 ##label SOR !'##cross-references GB:J03139; NID:g171707; PIDN:AAA34688.1; !1PID:g171708 !'##experimental_source strain BJ2168 !'##note parts of this sequence were determined by protein sequencing REFERENCE S64071 !$#authors Rieger, M.; Mueller-Auer, S.; Brueckner, M.; Schaefer, M. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64080 !'##molecule_type DNA !'##residues 1-833 ##label RIE !'##cross-references EMBL:Z72596; NID:g1322584; PIDN:CAA96777.1; !1PID:g1322586; GSPDB:GN00007; MIPS:YGL073w !'##experimental_source strain S288C REFERENCE A31592 !$#authors Wiederrecht, G.; Seto, D.; Parker, C.S. !$#journal Cell (1988) 54:841-853 !$#title Isolation of the gene encoding the S. cerevisiae heat shock !1transcription factor. !$#cross-references MUID:88311087; PMID:3044612 !$#accession A31592 !'##molecule_type DNA !'##residues 1-521,'F',523-556,'LISNLIMTA',566,'FQKFLLMTKKKKKP',581-830, !1'V',832-833 ##label WIE !'##cross-references GB:M22040; GB:J03140; NID:g171709; PIDN:AAA34689.1; !1PID:g171710 !'##experimental_source strain EJ926 GENETICS !$#gene SGD:HSF1; EXA3; MAS3; MIPS:YGL073w !'##cross-references SGD:S0003041; MIPS:YGL073w !$#map_position 7L COMPLEX homotrimer FUNCTION !$#description binding of HSF to heat shock promoter elements activates !1transcription of heat shock genes !$#note essential for viability at normal temperatures; increase in !1activity after heat shock is correlated with increased !1phosphorylation of existing protein CLASSIFICATION #superfamily Saccharomyces heat shock transcription factor !1HSF1; HSF DNA-binding domain homology KEYWORDS DNA binding; heat shock; homotrimer; leucine zipper; !1nucleus; phosphoprotein; stress-induced protein; !1transcription regulation FEATURE !$175-281 #domain HSF DNA-binding domain homology #label HSF\ !$347-375 #region leucine zipper\ !$536-542 #region regulatory heptapeptide SUMMARY #length 833 #molecular-weight 93281 #checksum 5278 SEQUENCE /// ENTRY S13365 #type complete TITLE heat shock transcription factor HSF - yeast (Kluyveromyces marxianus var. lactis) ORGANISM #formal_name Kluyveromyces marxianus var. lactis, Candida sphaerica DATE 07-Oct-1994 #sequence_revision 07-Oct-1994 #text_change 22-Jun-1999 ACCESSIONS S13365 REFERENCE S13365 !$#authors Jakobsen, B.K.; Pelham, H.R.B. !$#journal EMBO J. (1991) 10:369-375 !$#title A conserved heptapeptide restrains the activity of the yeast !1heat shock transcription factor. !$#cross-references MUID:91122044; PMID:1899375 !$#accession S13365 !'##molecule_type DNA !'##residues 1-677 ##label EMB !'##cross-references EMBL:X55149; NID:g2825; PIDN:CAA38950.1; PID:g2826 COMPLEX homotrimer FUNCTION !$#description binding of HSF to heat shock promoter elements activates !1transcription of heat shock genes CLASSIFICATION #superfamily Kluyveromyces heat shock transcription factor !1HSF; HSF DNA-binding domain homology KEYWORDS DNA binding; homotrimer; leucine zipper; nucleus; !1transcription factor FEATURE !$197-303 #domain HSF DNA-binding domain homology #label HSF\ !$317-345 #region leucine zipper\ !$451-457 #region regulatory heptapeptide\ !$485-551 #region glutamine-rich SUMMARY #length 677 #molecular-weight 75420 #checksum 8385 SEQUENCE /// ENTRY A49344 #type complete TITLE cell wall assembly regulatory protein SKN7 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES oxidative stress response regulator POS9; protein YHR206w ORGANISM #formal_name Saccharomyces cerevisiae DATE 07-Apr-1994 #sequence_revision 07-Apr-1994 #text_change 21-Jul-2000 ACCESSIONS A49344; S48987; S49986; S68114 REFERENCE A49344 !$#authors Brown, J.L.; North, S.; Bussey, H. !$#journal J. Bacteriol. (1993) 175:6908-6915 !$#title SKN7, a yeast multicopy suppressor of a mutation affecting !1cell wall beta-glucan assembly, encodes a product with !1domains homologous to prokaryotic two-component regulators !1and to heat shock transcription factors. !$#cross-references MUID:94042854; PMID:8226633 !$#accession A49344 !'##molecule_type DNA !'##residues 1-622 ##label BRO !'##cross-references GB:U00485; NID:g414418; PIDN:AAC48911.1; !1PID:g414419 REFERENCE S46671 !$#authors Macri, C. !$#submission submitted to the EMBL Data Library, February 1994 !$#description The sequence of S. cerevisiae cosmid 9177. !$#accession S48987 !'##molecule_type DNA !'##residues 1-622 ##label MAC !'##cross-references EMBL:U00029; NID:g551322; PIDN:AAB69734.1; !1PID:g458922; GSPDB:GN00008; MIPS:YHR206w REFERENCE S49986 !$#authors Krems, B.; Charizanis, C.; Entian, K.D. !$#submission submitted to the EMBL Data Library, November 1994 !$#description A protein (Pos9) similar to prokaryotic response regulators !1is involved in oxidative stress in yeast. !$#accession S49986 !'##molecule_type DNA !'##residues 1-622 ##label KRE !'##cross-references EMBL:X83031; NID:g600027; PIDN:CAA58143.1; !1PID:g600028 REFERENCE S68114 !$#authors Krems, B.; Charizanis, C.; Entian, K.D. !$#journal Curr. Genet. (1996) 29:327-334 !$#title The response regulator-like protein Pos9/Skn7 of !1Saccharomyces cerevisiae is involved in oxidative stress !1resistance. !$#cross-references MUID:96171515; PMID:8598053 !$#accession S68114 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-622 ##label KRW !'##cross-references EMBL:X83031; NID:g600027; PIDN:CAA58143.1; !1PID:g600028 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1994 GENETICS !$#gene SGD:SKN7; POS9; MIPS:YHR206w !'##cross-references SGD:S0001249; MIPS:YHR206w !$#map_position 8R CLASSIFICATION #superfamily cell wall assembly regulatory protein SKN7; HSF !1DNA-binding domain homology; response regulator homology KEYWORDS DNA binding; leucine zipper; nucleus; phosphoprotein; !1transcription regulation FEATURE !$87-194 #domain HSF DNA-binding domain homology #label HSF\ !$379-488 #domain response regulator homology #label RRH\ !$382-410 #region leucine zipper\ !$555-576 #region glutamine-rich\ !$427 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 622 #molecular-weight 69202 #checksum 256 SEQUENCE /// ENTRY A48070 #type complete TITLE heat shock transcription factor HSF - fission yeast (Schizosaccharomyces pombe) ORGANISM #formal_name Schizosaccharomyces pombe DATE 21-Jan-1994 #sequence_revision 07-Oct-1994 #text_change 10-Dec-1999 ACCESSIONS A48070; S27472; T38531 REFERENCE A48070 !$#authors Gallo, G.J.; Prentice, H.; Kingston, R.E. !$#journal Mol. Cell. Biol. (1993) 13:749-761 !$#title Heat shock factor is required for growth at normal !1temperatures in the fission yeast Schizosaccharomyces pombe. !$#cross-references MUID:93140772; PMID:8423799 !$#accession A48070 !'##molecule_type mRNA !'##residues 1-609 ##label GAL !'##note sequence extracted from NCBI backbone (NCBIN:123352, !1NCBIP:123353) REFERENCE S27472 !$#authors Gallo, G.J.; Prentice, H.; Kingston, R.E. !$#submission submitted to the EMBL Data Library, June 1992 !$#accession S27472 !'##molecule_type mRNA !'##residues 1-28,'H',30-609 ##label GA2 !'##cross-references EMBL:M94683; NID:g173406; PIDN:AAA35313.1; !1PID:g295687 REFERENCE Z21750 !$#authors Devlin, K.; Churcher, C.M.; Barrell, B.G.; Rajandream, M.A.; !1Walsh, S.V. !$#submission submitted to the EMBL Data Library, February 1996 !$#accession T38531 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-609 ##label DEV !'##cross-references EMBL:Z69726; PIDN:CAA93546.1; GSPDB:GN00066; !1SPDB:SPAC2E12.02.02 !'##experimental_source strain 972h-; cosmid c2E12 GENETICS !$#gene SPAC2E12.02.02 !$#map_position 1 !$#introns 110/1 FUNCTION !$#description binding of HSF to heat shock promoter elements activates !1transcription of heat shock genes !$#note essential for viability at normal temperatures; increases in !1activity after heat shock CLASSIFICATION #superfamily Schizosaccharomyces heat shock transcription !1factor HSF; HSF DNA-binding domain homology KEYWORDS DNA binding; heat shock; leucine zipper; nucleus; !1stress-induced protein; transcription regulation FEATURE !$53-160 #domain HSF DNA-binding domain homology #label HSF\ !$173-201 #region leucine zipper\ !$480-501 #region leucine zipper\ !$543-564 #region leucine zipper SUMMARY #length 609 #molecular-weight 66947 #checksum 6003 SEQUENCE /// ENTRY S61694 #type complete TITLE flocculation suppression protein SFL1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein O3339; protein YOR140w; protein YOR3339w ORGANISM #formal_name Saccharomyces cerevisiae DATE 09-Mar-1996 #sequence_revision 12-Apr-1996 #text_change 16-Jun-2000 ACCESSIONS S61694; JQ0384; S67025 REFERENCE S61643 !$#authors Benes, V.; Andrade, M.A.; Rechmann, S.; Teodoru, C.; !1Banrevi, A.; Sander, C.; Valencia, A.; Ansorge, W.; Voss, H. !$#submission submitted to the EMBL Data Library, December 1995 !$#description Nucleotide sequence and analysis of a 130 kb fragment of !1yeast chromosome XV. !$#accession S61694 !'##molecule_type DNA !'##residues 1-766 ##label BEN !'##cross-references EMBL:X94335; NID:g1262139; PIDN:CAA64057.1; !1PID:g1164982 REFERENCE JQ0384 !$#authors Fujita, A.; Kikuchi, Y.; Kuhara, S.; Misumi, Y.; Matsumoto, !1S.; Kobayashi, H. !$#journal Gene (1989) 85:321-328 !$#title Domains of the SFL1 protein of yeasts are homologous to Myc !1oncoproteins or yeast heat-shock transcription factor. !$#cross-references MUID:90185205; PMID:2697640 !$#accession JQ0384 !'##molecule_type DNA !'##residues 1-445,'FVQYQPQSQ',455-460,'KQ',463-766 ##label FUJ REFERENCE S66965 !$#authors Voss, H.; Benes, V.; Rechmann, S.; Teodoru, C.; Schwager, !1C.; Paces, V.; Ansorge, W. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67025 !'##molecule_type DNA !'##residues 1-766 ##label VOS !'##cross-references EMBL:Z75047; NID:g1420352; PIDN:CAA99338.1; !1PID:g1420354; GSPDB:GN00015; MIPS:YOR140w !'##experimental_source strain S288C COMMENT This protein is involved in cell surface assembly and !1regulation of the gene related to flocculation (asexual cell !1aggregation). GENETICS !$#gene SGD:SFL1; MIPS:YOR140w !'##cross-references MIPS:YOR140w; SGD:S0005666 !$#map_position 15R CLASSIFICATION #superfamily flocculation suppression protein SFL1; HSF !1DNA-binding domain homology KEYWORDS DNA binding; nucleus; transcription regulation FEATURE !$65-170 #domain HSF DNA-binding domain homology #label HSF SUMMARY #length 766 #molecular-weight 83317 #checksum 2259 SEQUENCE /// ENTRY A36295 #type complete TITLE heat shock transcription factor HSF - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 08-Mar-1991 #sequence_revision 08-Mar-1991 #text_change 22-Jun-1999 ACCESSIONS A36295 REFERENCE A36295 !$#authors Clos, J.; Westwood, J.T.; Becker, P.B.; Wilson, S.; Lambert, !1K.; Wu, C. !$#journal Cell (1990) 63:1085-1097 !$#title Molecular cloning and expression of a hexameric Drosophila !1heat shock factor subject to negative regulation. !$#cross-references MUID:91077922; PMID:2257625 !$#accession A36295 !'##molecule_type mRNA !'##residues 1-691 ##label CLO !'##cross-references GB:M60070; GB:M38668; NID:g157741; PIDN:AAA28642.1; !1PID:g157742 GENETICS !$#gene FlyBase:Hsf !'##cross-references FlyBase:FBgn0001222 COMPLEX homohexamer FUNCTION !$#description binding of HSF to heat shock promoter elements activates !1transcription of heat shock genes CLASSIFICATION #superfamily Drosophila heat shock transcription factor HSF; !1HSF DNA-binding domain homology KEYWORDS DNA binding; heat shock; homohexamer; leucine zipper; !1nucleus; phosphoprotein; stress-induced protein; !1transcription regulation FEATURE !$49-154 #domain HSF DNA-binding domain homology #label HSF\ !$169-204 #region leucine zipper\ !$218-239 #region leucine zipper\ !$581-609 #region leucine zipper SUMMARY #length 691 #molecular-weight 76933 #checksum 6177 SEQUENCE /// ENTRY OCECJ #type complete TITLE major cold shock protein cspA - Escherichia coli (strain K-12) ALTERNATE_NAMES 7.4 kda cytoplasmic protein CS7.4 ORGANISM #formal_name Escherichia coli DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 01-Mar-2002 ACCESSIONS JH0201; A44911; S47777; F65154 REFERENCE JH0201 !$#authors Goldstein, J.; Pollitt, N.S.; Inouye, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:283-287 !$#title Major cold shock protein of Escherichia coli. !$#cross-references MUID:90115858; PMID:2404279 !$#accession JH0201 !'##molecule_type DNA !'##residues 1-70 ##label GOL !'##cross-references GB:M30139; NID:g409136; PIDN:AAA23617.1; !1PID:g145633 REFERENCE A44911 !$#authors Tanabe, H.; Goldstein, J.; Yang, M.; Inouye, M. !$#journal J. Bacteriol. (1992) 174:3867-3873 !$#title Identification of the promoter region of the Escherichia !1coli major cold shock gene, cspA. !$#cross-references MUID:92283739; PMID:1597410 !$#accession A44911 !'##molecule_type DNA !'##residues 1-70 ##label TAN !'##cross-references GB:M30139; NID:g409136; PIDN:AAA23617.1; !1PID:g145633 !'##experimental_source strain SB221 !'##note sequence extracted from NCBI backbone (NCBIN:107427, !1NCBIP:107430) REFERENCE S47666 !$#authors Plunkett, G. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S47777 !'##molecule_type DNA !'##residues 1-70 ##label PLU !'##cross-references EMBL:U00039; NID:g466582; PIDN:AAB18533.1; !1PID:g466694 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65154 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-70 ##label BLAT !'##cross-references GB:AE000433; GB:U00096; NID:g1789977; !1PIDN:AAC76580.1; PID:g1789979; UWGP:b3556 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene cspA !$#map_position 79 min CLASSIFICATION #superfamily major cold shock protein; cold shock domain !1homology KEYWORDS cold shock; DNA binding; stress-induced protein; !1transcription regulation FEATURE !$2-70 #product major cold shock protein #status predicted !8#label MAT\ !$7-67 #domain cold shock domain homology #label CSD SUMMARY #length 70 #molecular-weight 7403 #checksum 2158 SEQUENCE /// ENTRY I39382 #type complete TITLE Y box-binding protein 1 - human ALTERNATE_NAMES DNA binding protein B; transcription enhancer factor EF1a; transcription factor YB-1 ORGANISM #formal_name Homo sapiens #common_name man DATE 16-Feb-1996 #sequence_revision 16-Feb-1996 #text_change 22-Jun-1999 ACCESSIONS I39382; PS0015; A40498 REFERENCE A54085 !$#authors Horwitz, E.M.; Maloney, K.A.; Ley, T.J. !$#journal J. Biol. Chem. (1994) 269:14130-14139 !$#title A human protein containing a 'cold shock' domain binds !1specifically to H-DNA upstream from the human gamma-globin !1genes. !$#cross-references MUID:94245734; PMID:8188694 !$#accession I39382 !'##molecule_type mRNA !'##residues 1-324 ##label RES !'##cross-references GB:L28809; NID:g454151; PIDN:AAA20871.1; !1PID:g454152 REFERENCE PS0014 !$#authors Sakura, H.; Maekawa, T.; Imamoto, F.; Yasuda, K.; Ishii, S. !$#journal Gene (1988) 73:499-507 !$#title Two human genes isolated by a novel method encode !1DNA-binding proteins containing a common region of homology. !$#cross-references MUID:89211987; PMID:2977358 !$#accession PS0015 !'##molecule_type mRNA !'##residues 'EFGGPQRALSSPTAAAGLVTITPREEPQLPQPAPVTITAT',1-324 ##label !1SAK !'##cross-references GB:M24070; NID:g181485; PIDN:AAA35750.1; !1PID:g181486 REFERENCE A40498 !$#authors Didier, D.K.; Schiffenbauer, J.; Woulfe, S.L.; Zacheis, M.; !1Schwartz, B.D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:7322-7326 !$#title Characterization of the cDNA encoding a protein binding to !1the major histocompatibility complex class II Y box. !$#cross-references MUID:89017190; PMID:3174636 !$#accession A40498 !'##molecule_type mRNA !'##residues 1-119,'E',121-313,'RSRG' ##label DID !'##cross-references GB:J03827; NID:g340418; PIDN:AAA61308.1; !1PID:g340419 GENETICS !$#gene GDB:YB1 !'##cross-references GDB:5577123; OMIM:154030 !$#map_position 1p34-1p34 CLASSIFICATION #superfamily Y box-binding protein 1; cold shock domain !1homology KEYWORDS DNA binding; nucleus; transcription regulation FEATURE !$61-125 #domain cold shock domain homology #label CSD SUMMARY #length 324 #molecular-weight 35924 #checksum 3263 SEQUENCE /// ENTRY JQ2292 #type complete TITLE Y box-binding protein 1 - bovine ALTERNATE_NAMES DNA binding protein B; transcription enhancer factor EF1a; transcription factor YB-1 ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 30-Sep-1993 #sequence_revision 20-Aug-1994 #text_change 22-Jun-1999 ACCESSIONS JQ2292 REFERENCE JQ2292 !$#authors Ozer, J.; Chalkley, R.; Sealy, L. !$#journal Gene (1993) 124:223-230 !$#title Isolation of the CCAAT transcription factor subunit EFIA !1cDNA and a potentially functional EFIA processed pseudogene !1from Bos taurus: Insights into the evolution of the EFIA/ !1dbpB/YB-1 gene family. !$#cross-references MUID:93185927; PMID:8444345 !$#accession JQ2292 !'##molecule_type mRNA !'##residues 1-324 ##label OZE !'##cross-references GB:M95793; NID:g162982; PIDN:AAA30497.1; !1PID:g162983 COMMENT This protein is a multi-subunit trans-acting complex that !1binds to CCAAT box cis-element and is essential for Rous !1sarcoma viral long terminal repeat enhancer function. CLASSIFICATION #superfamily Y box-binding protein 1; cold shock domain !1homology KEYWORDS DNA binding; nucleus; transcription regulation FEATURE !$61-125 #domain cold shock domain homology #label CSD SUMMARY #length 324 #molecular-weight 35924 #checksum 3263 SEQUENCE /// ENTRY A55971 #type complete TITLE Y box-binding protein 1 - rabbit ALTERNATE_NAMES DNA binding protein B; transcription enhancer factor EF1a; transcription factor YB-1 ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 03-Oct-1995 #sequence_revision 03-Oct-1995 #text_change 22-Jun-1999 ACCESSIONS A55971 REFERENCE A55971 !$#authors Evdokimova, V.M.; Wei, C.L.; Sitikov, A.S.; Simonenko, P.N.; !1Lazarev, O.A.; Vasilenko, K.S.; Ustinov, V.A.; Hershey, !1J.W.B.; Ovchinnikov, L.P. !$#journal J. Biol. Chem. (1995) 270:3186-3192 !$#title The major protein of messenger ribonucleoprotein particles !1in somatic cells is a member of the Y-box binding !1transcription factor family. !$#cross-references MUID:95155408; PMID:7852402 !$#accession A55971 !'##molecule_type mRNA !'##residues 1-324 ##label EVD !'##cross-references GB:U16821; NID:g608517; PIDN:AAA66069.1; !1PID:g608518 CLASSIFICATION #superfamily Y box-binding protein 1; cold shock domain !1homology KEYWORDS DNA binding; phosphoprotein; RNA binding; transcription !1regulation; translation regulation FEATURE !$61-125 #domain cold shock domain homology #label CSD SUMMARY #length 324 #molecular-weight 35824 #checksum 3280 SEQUENCE /// ENTRY I58195 #type complete TITLE Y box-binding protein 1 - mouse ALTERNATE_NAMES DNA binding protein B; MSY1 protein; transcription enhancer factor EF1a; transcription factor YB-1 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 26-Jul-1996 #sequence_revision 26-Jul-1996 #text_change 22-Jun-1999 ACCESSIONS I58195; A45976; I52910; S22822 REFERENCE I58195 !$#authors Wolffe, A.P.; Tafuri, S.; Ranjan, M.; Familari, M. !$#journal New Biol. (1992) 4:290-298 !$#title The Y-box factors: a family of nucleic acid binding proteins !1conserved from Escherichia coli to man. !$#cross-references MUID:92322631; PMID:1622927 !$#accession I58195 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-322 ##label RES !'##cross-references GB:M62867; NID:g199820; PIDN:AAA63390.1; !1PID:g199821 REFERENCE A45976 !$#authors Tafuri, S.R.; Familari, M.; Wolffe, A.P. !$#journal J. Biol. Chem. (1993) 268:12213-12220 !$#title A mouse Y box protein, MSY1, is associated with paternal !1mRNA in spermatocytes. !$#cross-references MUID:93280200; PMID:8505341 !$#accession A45976 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-322 ##label TAF REFERENCE I52910 !$#authors Shaughnessy, M.; Lee, D.; Wistow, G.J. !$#journal Curr. Eye Res. (1992) 11:171-181 !$#title Absense of MHC expression in lens and cloning of dbpB/YB-1, !1a DNA-binding protein expressed in mouse lens. !$#accession I52910 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-28,'G',30-322 ##label RE2 !'##cross-references GB:M60419; NID:g202434; PIDN:AAA40577.1; !1PID:g202435 !'##experimental_source lens REFERENCE S22822 !$#authors Gai, X.; Lipson, K.E.; Prystowsky, M.B. !$#journal Nucleic Acids Res. (1992) 20:601-606 !$#title Unusual DNA binding characteristics of an in vitro !1translation product of the CCAAT binding protein mYB-1. !$#cross-references MUID:92158671; PMID:1741293 !$#accession S22822 !'##status nucleic acid sequence not shown; translation not shown; !1translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-28,'G',30-42,'RR',46-237,'P',239-322 ##label GAI !'##cross-references EMBL:X57621; NID:g55450; PIDN:CAA40847.1; !1PID:g55451 !'##experimental_source strain C57BL/6 GENETICS !$#gene MSY-1; YB-1 CLASSIFICATION #superfamily Y box-binding protein 1; cold shock domain !1homology KEYWORDS DNA binding; eye lens; nucleus; RNA binding; testis; !1transcription regulation; translation regulation FEATURE !$59-123 #domain cold shock domain homology #label CSD SUMMARY #length 322 #molecular-weight 35744 #checksum 6396 SEQUENCE /// ENTRY A23677 #type complete TITLE Y box-binding protein 1 - rat ALTERNATE_NAMES DNA binding protein B; transcription enhancer factor EF1a; transcription factor YB-1 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 04-Oct-1991 #sequence_revision 31-Jul-1992 #text_change 22-Jun-1999 ACCESSIONS A23677 REFERENCE A23677 !$#authors Ozer, J.; Faber, M.; Chalkley, R.; Sealy, L. !$#journal J. Biol. Chem. (1990) 265:22143-22152 !$#title Isolation and characterization of a cDNA clone for the CCAAT !1transcription factor EFI-A reveals a novel structural motif. !$#cross-references MUID:91093048; PMID:1967130 !$#accession A23677 !'##molecule_type DNA !'##residues 1-322 ##label OZE !'##cross-references GB:M57299; GB:J05704; NID:g203998; PIDN:AAA41108.1; !1PID:g203999 CLASSIFICATION #superfamily Y box-binding protein 1; cold shock domain !1homology KEYWORDS DNA binding; nucleus; transcription regulation FEATURE !$59-123 #domain cold shock domain homology #label CSD SUMMARY #length 322 #molecular-weight 35720 #checksum 6633 SEQUENCE /// ENTRY A48136 #type complete TITLE Y box-binding protein 1 - chicken ALTERNATE_NAMES DNA binding protein B; transcription factor EF1a; transcription factor YB-1 ORGANISM #formal_name Gallus gallus #common_name chicken DATE 30-Jun-1995 #sequence_revision 30-Jun-1995 #text_change 22-Jun-1999 ACCESSIONS A48136 REFERENCE A48136 !$#authors Grant, C.E.; Deeley, R.G. !$#journal Mol. Cell. Biol. (1993) 13:4186-4196 !$#title Cloning and characterization of chicken YB-1: regulation of !1expression in the liver. !$#cross-references MUID:93309452; PMID:8321222 !$#accession A48136 !'##molecule_type mRNA !'##residues 1-321 ##label GRA !'##cross-references GB:L13032; NID:g289796; PIDN:AAA02573.1; !1PID:g289797 CLASSIFICATION #superfamily Y box-binding protein 1; cold shock domain !1homology KEYWORDS DNA binding; nucleus; transcription regulation FEATURE !$58-122 #domain cold shock domain homology #label CSD SUMMARY #length 321 #molecular-weight 35799 #checksum 3891 SEQUENCE /// ENTRY S34426 #type complete TITLE nuclease sensitive element-binding protein 1 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 02-Dec-1993 #sequence_revision 26-May-1995 #text_change 07-May-1999 ACCESSIONS S34426 REFERENCE S34426 !$#authors Kolluri, R.; Kinniburgh, A.J. !$#journal Nucleic Acids Res. (1991) 19:4771 !$#title Full length cDNA sequence encoding a nuclease-sensitive !1element DNA binding protein. !$#cross-references MUID:91367681; PMID:1891370 !$#accession S34426 !'##status nucleic acid sequence not shown; translation not shown; !1translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-321 ##label KOL !'##cross-references EMBL:M85234 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1992 GENETICS !$#gene GDB:NSEP1 !'##cross-references GDB:128796 CLASSIFICATION #superfamily Y box-binding protein 1; cold shock domain !1homology KEYWORDS DNA binding; nucleus; transcription regulation FEATURE !$60-124 #domain cold shock domain homology #label CSD SUMMARY #length 321 #molecular-weight 34541 #checksum 7508 SEQUENCE /// ENTRY A38274 #type complete TITLE Y box-binding protein 1 - African clawed frog ALTERNATE_NAMES DNA binding protein B; transcription enhancer factor EF1a; transcription factor YB-1 ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 21-Jun-1991 #sequence_revision 21-Jun-1991 #text_change 22-Jun-1999 ACCESSIONS A38274 REFERENCE A38274 !$#authors Tafuri, S.R.; Wolffe, A.P. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:9028-9032 !$#title Xenopus Y-box transcription factors: molecular cloning, !1functional analysis, and developmental regulation. !$#cross-references MUID:91062413; PMID:2247479 !$#accession A38274 !'##molecule_type mRNA !'##residues 1-303 ##label TAF !'##cross-references GB:M59453; GB:M38382; NID:g214154; PIDN:AAA49715.1; !1PID:g214155 CLASSIFICATION #superfamily Y box-binding protein 1; cold shock domain !1homology KEYWORDS DNA binding; nucleus; transcription regulation FEATURE !$39-103 #domain cold shock domain homology #label CSD SUMMARY #length 303 #molecular-weight 34633 #checksum 7069 SEQUENCE /// ENTRY S22313 #type complete TITLE B box-binding protein - African clawed frog ALTERNATE_NAMES YB3 protein ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 22-Nov-1993 #sequence_revision 10-Nov-1995 #text_change 22-Jun-1999 ACCESSIONS S22313 REFERENCE S22313 !$#authors Cohen, I.; Reynolds, W.F. !$#journal Nucleic Acids Res. (1991) 19:4753-4759 !$#title The Xenopus YB3 protein binds the B box element of the class !1III promoter. !$#cross-references MUID:91367675; PMID:1891365 !$#accession S22313 !'##molecule_type mRNA !'##residues 1-305 ##label COH !'##cross-references EMBL:X60217; NID:g65270; PIDN:CAA42778.1; !1PID:g65271 !'##experimental_source oocyte FUNCTION !$#description binds to the B-box promoter element; may be involved in !1class III gene regulation !$#note expressed in a variety of adult tissues CLASSIFICATION #superfamily Y box-binding protein 1; cold shock domain !1homology KEYWORDS DNA binding; nucleus; transcription regulation FEATURE !$39-103 #domain cold shock domain homology #label CSD SUMMARY #length 305 #molecular-weight 34484 #checksum 755 SEQUENCE /// ENTRY I53354 #type complete TITLE DNA-binding protein A - human ORGANISM #formal_name Homo sapiens #common_name man DATE 02-Jul-1996 #sequence_revision 02-Jul-1996 #text_change 20-Apr-2000 ACCESSIONS I53354; PS0014; S65945 REFERENCE I53354 !$#authors Kudo, S.; Mattei, M.G.; Fukuda, M. !$#journal Eur. J. Biochem. (1995) 231:72-82 !$#title Characterization of the gene for dbpA, a family member of !1the nucleic-acid-binding proteins containing a cold-shock !1domain. !$#cross-references MUID:95354705; PMID:7628487 !$#accession I53354 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-342 ##label KUD !'##cross-references GB:L29071; NID:g950337; PIDN:AAA79243.1; !1PID:g950340 !'##experimental_source placenta !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1995 REFERENCE PS0014 !$#authors Sakura, H.; Maekawa, T.; Imamoto, F.; Yasuda, K.; Ishii, S. !$#journal Gene (1988) 73:499-507 !$#title Two human genes isolated by a novel method encode !1DNA-binding proteins containing a common region of homology. !$#cross-references MUID:89211987; PMID:2977358 !$#accession PS0014 !'##molecule_type mRNA !'##residues !1'EFGRGSPRSERARRSSSRLRQRDPTSAAGLRREIRPGLPESEPRPPRPPAALTADQPPP !1RRLSESRGGGG',1-342 ##label SAK !'##cross-references GB:M24069; NID:g181483; PIDN:AAA35749.1; !1PID:g181484 GENETICS !$#gene GDB:CSDA; dbpA !'##cross-references GDB:9865772; OMIM:603437 !$#map_position 12p13.1-12p13.1 !$#introns 88/1; 109/2; 120/3; 150/3; 191/3; 260/3; 293/2 CLASSIFICATION #superfamily Y box-binding protein 1; cold shock domain !1homology KEYWORDS DNA binding; nucleus; transcription regulation FEATURE !$93-157 #domain cold shock domain homology #label CSD SUMMARY #length 342 #molecular-weight 36990 #checksum 7906 SEQUENCE /// ENTRY A35667 #type complete TITLE Ty transcription activator TEC1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YBR0750; protein YBR083w ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A35667; S45950 REFERENCE A35667 !$#authors Laloux, I.; Dubois, E.; Dewerchin, M.; Jacobs, E. !$#journal Mol. Cell. Biol. (1990) 10:3541-3550 !$#title TEC1, a gene involved in the activation of Ty1 and !1Ty1-mediated gene expression in Saccharomyces cerevisiae: !1cloning and molecular analysis. !$#cross-references MUID:90287143; PMID:2192259 !$#accession A35667 !'##molecule_type DNA !'##residues 1-486 ##label LAL !'##cross-references GB:M32797; NID:g172881; PIDN:AAA35141.1; !1PID:g172882 REFERENCE S45893 !$#authors Andre, B.; Cziepluch, C.; Hein, C.; Jauniaux, J.C.; !1Urrestarazu, A.; Vissers, S. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S45950 !'##molecule_type DNA !'##residues 1-486 ##label AND !'##cross-references EMBL:Z35952; NID:g536345; PIDN:CAA85028.1; !1PID:g536346; GSPDB:GN00002; MIPS:YBR083w GENETICS !$#gene SGD:TEC1; MIPS:YBR083w !'##cross-references SGD:S0000287; MIPS:YBR083w !$#map_position 2R CLASSIFICATION #superfamily Ty transcription activator TEC1; TEA !1DNA-binding domain homology KEYWORDS DNA binding; nucleus; transcription regulation FEATURE !$123-193 #domain TEA DNA-binding domain homology #label TEA SUMMARY #length 486 #molecular-weight 55157 #checksum 3867 SEQUENCE /// ENTRY A32434 #type complete TITLE abaA protein - Emericella nidulans ORGANISM #formal_name Emericella nidulans, Aspergillus nidulans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A32434 REFERENCE A32434 !$#authors Mirabito, P.M.; Adams, T.H.; Timberlake, W.E. !$#journal Cell (1989) 57:859-868 !$#title Interactions of three sequentially expressed genes control !1temporal and spatial specificity in Aspergillus development. !$#cross-references MUID:89249350; PMID:2655931 !$#accession A32434 !'##status preliminary !'##molecule_type DNA !'##residues 1-796 ##label MIR !'##cross-references GB:J04850; NID:g167997; PIDN:AAA33286.1; !1PID:g167998 !'##note the authors translated the codon ATC for residue 641 as Thr CLASSIFICATION #superfamily abaA protein; TEA DNA-binding domain homology KEYWORDS DNA binding; nucleus; transcription regulation FEATURE !$131-201 #domain TEA DNA-binding domain homology #label TEA SUMMARY #length 796 #molecular-weight 89170 #checksum 6986 SEQUENCE /// ENTRY A40032 #type complete TITLE transcription enhancer factor TEF1 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A40032 REFERENCE A40032 !$#authors Xiao, J.H.; Davidson, I.; Matthes, H.; Garnier, J.M.; !1Chambon, P. !$#journal Cell (1991) 65:551-568 !$#title Cloning, expression, and transcriptional properties of the !1human enhancer factor TEF-1. !$#cross-references MUID:91235292; PMID:1851669 !$#accession A40032 !'##molecule_type mRNA !'##residues 1-426 ##label XIA !'##cross-references GB:M63896 GENETICS !$#gene GDB:TCF13; TEF-1 !'##cross-references GDB:128990; OMIM:189967 !$#map_position 15q21-15q21 !$#start_codon ATT CLASSIFICATION #superfamily transcription enhancer factor TEF1; TEA !1DNA-binding domain homology KEYWORDS DNA binding; transcription factor; zinc finger FEATURE !$26-98 #domain TEA DNA-binding domain homology #label TEA\ !$402-419 #region zinc finger SUMMARY #length 426 #molecular-weight 47945 #checksum 3722 SEQUENCE /// ENTRY B38274 #type complete TITLE Y box-binding protein 2 - African clawed frog ALTERNATE_NAMES cytoplasmic mRNA-binding protein p54 ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 21-Jun-1991 #sequence_revision 21-Jun-1991 #text_change 22-Jun-1999 ACCESSIONS B38274; B41786 REFERENCE A38274 !$#authors Tafuri, S.R.; Wolffe, A.P. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:9028-9032 !$#title Xenopus Y-box transcription factors: molecular cloning, !1functional analysis, and developmental regulation. !$#cross-references MUID:91062413; PMID:2247479 !$#accession B38274 !'##status preliminary !'##molecule_type mRNA !'##residues 1-336 ##label TAF !'##cross-references GB:M59454; GB:M38382; NID:g214156; PIDN:AAA49716.1; !1PID:g214157; GB:M38383 REFERENCE A41786 !$#authors Murray, M.T.; Schiller, D.L.; Franke, W.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:11-15 !$#title Sequence analysis of cytoplasmic mRNA-binding proteins of !1Xenopus oocytes identifies a family of RNA-binding proteins. !$#cross-references MUID:92107999; PMID:1729676 !$#accession B41786 !'##molecule_type protein !'##residues 56-82;95-105,'XXX',109-113;234-253,'A',255 ##label MUR CLASSIFICATION #superfamily Xenopus Y box-binding protein 2; cold shock !1domain homology KEYWORDS DNA binding; nucleus; oocyte; RNA binding; testis; !1transcription regulation FEATURE !$44-108 #domain cold shock domain homology #label CSD SUMMARY #length 336 #molecular-weight 37233 #checksum 4798 SEQUENCE /// ENTRY A41786 #type complete TITLE mRNA-binding protein p54 - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 04-Mar-1993 #sequence_revision 03-Nov-1995 #text_change 22-Jun-1999 ACCESSIONS A41786; A36348 REFERENCE A41786 !$#authors Murray, M.T.; Schiller, D.L.; Franke, W.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:11-15 !$#title Sequence analysis of cytoplasmic mRNA-binding proteins of !1Xenopus oocytes identifies a family of RNA-binding proteins. !$#cross-references MUID:92107999; PMID:1729676 !$#accession A41786 !'##molecule_type mRNA !'##residues 1-324 ##label MUR !'##cross-references GB:M80257; NID:g214641; PIDN:AAA49924.1; !1PID:g214642 !'##note sequence extracted from NCBI backbone (NCBIN:74686, !1NCBIP:74687) REFERENCE A36348 !$#authors Murray, M.T.; Krohne, G.; Franke, W.W. !$#journal J. Cell Biol. (1991) 112:1-11 !$#title Different forms of soluble cytoplasmic mRNA binding proteins !1and particles in Xenopus laevis oocytes and embryos. !$#cross-references MUID:91093331; PMID:1670777 !$#accession A36348 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type mRNA !'##residues 221-233 ##label MU2 !'##note authors say this sequence was found in the similar p56 molecule !1but there are two sequence differences from the !1corresponding region of that protein (see accession B38274) CLASSIFICATION #superfamily Xenopus Y box-binding protein 2; cold shock !1domain homology KEYWORDS DNA binding; nucleus; oocyte; RNA binding; transcription !1regulation FEATURE !$44-108 #domain cold shock domain homology #label CSD SUMMARY #length 324 #molecular-weight 35952 #checksum 3672 SEQUENCE /// ENTRY UMMS #type fragment TITLE period clock protein - mouse (fragment) ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jun-2000 ACCESSIONS A24403 REFERENCE A24403 !$#authors Shin, H.S.; Bargiello, T.A.; Clark, B.T.; Jackson, F.R.; !1Young, M.W. !$#journal Nature (1985) 317:445-448 !$#title An unusual coding sequence from a Drosophila clock gene is !1conserved in vertebrates. !$#cross-references MUID:86014384; PMID:2413365 !$#accession A24403 !'##molecule_type DNA !'##residues 1-713 ##label SHI !'##cross-references GB:X02966; GB:M12039; NID:g55125; PIDN:CAA26710.1; !1PID:g1334150 COMMENT Mutations within the per locus of the fruit fly affect a !1variety of natural biological rhythms (from long-term !1circadian to short-period behaviors). The genome of the !1mouse contains a homologous locus with multiple tandem !1repeats of nucleic acid hexamers (ACNGGN, TCAGGC) that !1encode poly(T/S-G) tracts up to 48 residues long. COMMENT The serine residues of the S-G repeats found in certain !1proteoglycans are attachment sites for glycosaminoglycans, !1although it is not known whether this protein binds !1proteoglycan. CLASSIFICATION #superfamily period clock protein; EGF homology KEYWORDS circadian rhythm; tandem repeat FEATURE !$41-77 #domain EGF homology #label EGF SUMMARY #length 713 #checksum 3504 SEQUENCE /// ENTRY UMFF #type fragment TITLE period clock protein - fruit fly (Drosophila melanogaster) (fragment) ORGANISM #formal_name Drosophila melanogaster DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 23-Jul-1999 ACCESSIONS A23932 REFERENCE A23932 !$#authors Reddy, P.; Jacquier, A.C.; Abovich, N.; Petersen, G.; !1Rosbash, M. !$#journal Cell (1986) 46:53-61 !$#title The period clock locus of D. melanogaster codes for a !1proteoglycan. !$#cross-references MUID:86245055; PMID:3087625 !$#accession A23932 !'##molecule_type DNA !'##residues 1-571 ##label RED !'##note the authors translated the codon GCG for residue 140 as Glu, !1GTT for residue 525 as Leu, and TAC for residue 570 as Thr COMMENT Mutations within the per locus (period clock gene) can !1disrupt or modify a variety of natural biological rhythms, !1from long-term circadian to short-period behaviors (rhythm !1of courtship song). COMMENT Biochemically, this protein is thought to be a neuronal !1heparan/heparan sulfate type of proteoglycan; however, its !1multiple, tandemly repeated G-T residues have not yet been !1shown to have covalently bound chondroitin sulfate. GENETICS !$#gene per !'##cross-references FlyBase:FBgn0003068 !$#map_position 3B1-2 CLASSIFICATION #superfamily period clock protein; EGF homology KEYWORDS chondroitin sulfate proteoglycan; circadian rhythm; !1glycoprotein; heparan sulfate; tandem repeat FEATURE !$201-239 #region heparan sulfate attachment (T-G repeats) !8#status predicted\ !$178,192,241,302,566 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$245,311,372,388 #binding_site heparan sulfate (Ser) (covalent) !8#status predicted SUMMARY #length 571 #checksum 8460 SEQUENCE /// ENTRY WJMSX3 #type complete TITLE homeotic protein Hox C8 - mouse ALTERNATE_NAMES homeotic protein Hox 3.1 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 22-Jun-1999 ACCESSIONS B36023; S00548; A29980 REFERENCE A36023 !$#authors Awgulewitsch, A.; Bieberich, C.; Bogarad, L.; Shashikant, !1C.; Ruddle, F.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:6428-6432 !$#title Structural analysis of the Hox-3.1 transcription unit and !1the Hox-3.2-Hox-3.1 intergenic region. !$#cross-references MUID:90349629; PMID:1696731 !$#accession B36023 !'##molecule_type DNA !'##residues 1-242 ##label AWG !'##cross-references GB:M35603; NID:g193977; PIDN:AAA37857.1; !1PID:g193979 REFERENCE S00548 !$#authors Breier, G.; Dressler, G.R.; Gruss, P. !$#journal EMBO J. (1988) 7:1329-1336 !$#title Primary structure and developmental expression pattern of !1Hox 3.1, a member of the murine Hox 3 homeobox gene cluster. !$#cross-references MUID:88312579; PMID:2900757 !$#accession S00548 !'##molecule_type mRNA !'##residues 1-242 ##label BRE !'##cross-references EMBL:X07646; NID:g51402; PIDN:CAA30486.1; !1PID:g51403 REFERENCE A29980 !$#authors Le Mouellic, H.; Condamine, H.; Brulet, P. !$#journal Genes Dev. (1988) 2:125-135 !$#title Pattern of transcription of the homeo gene Hox-3.1 in the !1mouse embryo. !$#cross-references MUID:88185818; PMID:2895723 !$#accession A29980 !'##molecule_type mRNA !'##residues 1-242 ##label LEM !'##cross-references EMBL:X07439; NID:g51406; PIDN:CAA30319.1; !1PID:g51407 GENETICS !$#gene Hox 3.1 !$#map_position 15 !$#introns 146/1 CLASSIFICATION #superfamily homeotic protein Hox A7; homeobox homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$150-206 #domain homeobox homology #label HOX SUMMARY #length 242 #molecular-weight 27740 #checksum 3282 SEQUENCE /// ENTRY WJMS24 #type complete TITLE homeotic protein Hox B8 - mouse ALTERNATE_NAMES homeotic protein Hox 2.4 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 22-Jun-1999 ACCESSIONS S03712; S16691; S02015; A27176 REFERENCE S03712 !$#authors Kongsuwan, K.; Allen, J.; Adams, J.M. !$#journal Nucleic Acids Res. (1989) 17:1881-1892 !$#title Expression of Hox-2.4 homeobox gene directed by proviral !1insertion in a myeloid leukemia. !$#cross-references MUID:89183599; PMID:2564662 !$#accession S03712 !'##molecule_type mRNA !'##residues 1-243 ##label KON !'##cross-references EMBL:X13721 REFERENCE S16691 !$#authors Blatt, C. !$#submission submitted to the EMBL Data Library, July 1989 !$#accession S16691 !'##molecule_type DNA !'##residues 1-88,'D',90-243 ##label BLA1 !'##cross-references EMBL:X13961; NID:g51393; PIDN:CAA32141.1; !1PID:g295919 REFERENCE S02015 !$#authors Blatt, C.; Aberdam, D.; Schwartz, R.; Sachs, L. !$#journal EMBO J. (1988) 7:4283-4290 !$#title DNA rearrangement of a homeobox gene in myeloid leukaemic !1cells. !$#cross-references MUID:89210815; PMID:2907477 !$#accession S02015 !'##molecule_type DNA !'##residues 1-29,'HDLAPTHRGVRSQQRRHVPAPFANPGVLPRAIVAVHSSLPAEPVRRGCN', !182-88,'D',90-114,'RS',116-122,'RGLSRARR',131-141,143-243 !1##label BLA2 !'##cross-references EMBL:X13961 !'##note this sequence has been revised in reference S16691 REFERENCE A27176 !$#authors Hart, C.P.; Fainsod, A.; Ruddle, F.H. !$#journal Genomics (1987) 1:182-195 !$#title Sequence analysis of the murine Hox-2.2, -2.3, and -2.4 !1homeo boxes: evolutionary and structural comparisons. !$#cross-references MUID:88085193; PMID:2891608 !$#accession A27176 !'##molecule_type DNA !'##residues 143-243 ##label HAR !'##cross-references EMBL:M18399 GENETICS !$#gene Hox-2.4 !$#map_position 11 !$#introns 142/1 CLASSIFICATION #superfamily homeotic protein Hox A7; homeobox homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$147-203 #domain homeobox homology #label HOX SUMMARY #length 243 #molecular-weight 27640 #checksum 2568 SEQUENCE /// ENTRY WJHU2C #type complete TITLE homeotic protein Hox B7 - human ALTERNATE_NAMES homeotic protein c1; homeotic protein Hox 2C; TATAA binding protein ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 22-Jun-1999 ACCESSIONS A28030; S15535; A44934 REFERENCE A28030 !$#authors Simeone, A.; Mavilio, F.; Acampora, D.; Giampaolo, A.; !1Faiella, A.; Zappavigna, V.; D'Esposito, M.; Pannese, M.; !1Russo, G.; Boncinelli, E.; Peschle, C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:4914-4918 !$#title Two human homeobox genes, c1 and c8: structure analysis and !1expression in embryonic development. !$#cross-references MUID:87260899; PMID:2885844 !$#accession A28030 !'##molecule_type mRNA !'##residues 1-217 ##label SIM !'##cross-references GB:M16937 !'##note the authors translated the codon GGC for residue 53 as Ala REFERENCE S15036 !$#authors Boncinelli, E.; Acampora, D.; Pannese, M.; d'Esposito, M.; !1Somma, R.; Gaudino, G.; Stornaiuolo, A.; Cafiero, M.; !1Faiella, A.; Simeone, A. !$#journal Genome (1989) 31:745-756 !$#title Organization of human class I homeobox genes. !$#cross-references MUID:90215256; PMID:2576652 !$#accession S15535 !'##molecule_type DNA !'##residues 137-202 ##label BON REFERENCE A44934 !$#authors Baier, L.J.; Hannibal, M.C.; Hanley, E.W.; Nabel, G.J. !$#journal Blood (1991) 78:1047-1055 !$#title Lymphoid expression and TATAA binding of a human protein !1containing an Antennapedia homeodomain. !$#cross-references MUID:91329816; PMID:1678287 !$#accession A44934 !'##molecule_type mRNA !'##residues 98-217 ##label BAI !'##cross-references GB:S49765; NID:g233572; PIDN:AAB19469.1; !1PID:g233573 !'##note this sequence is inconsistent with the nucleotide translation !'##note sequence extracted from NCBI backbone (NCBIN:49765, !1NCBIP:49769) GENETICS !$#gene GDB:HOXB7 !'##cross-references GDB:120660; OMIM:142962 !$#map_position 17q21.3-17q21.3 !$#introns 134/1 CLASSIFICATION #superfamily homeotic protein Hox A7; homeobox homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$138-194 #domain homeobox homology #label HOX SUMMARY #length 217 #molecular-weight 23940 #checksum 5602 SEQUENCE /// ENTRY WJMSX2 #type complete TITLE homeotic protein Hox B7 - mouse ALTERNATE_NAMES homeotic protein Hox 2.3 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 22-Jun-1999 ACCESSIONS A26846; B26846; B27176; A29585; S00988; I48411; S01887 REFERENCE A26846 !$#authors Meijlink, F.; de Laaf, R.; Verrijzer, P.; Destree, O.; !1Kroezen, V.; Hilkens, J.; Deschamps, J. !$#journal Nucleic Acids Res. (1987) 15:6773-6786 !$#title A mouse homeobox containing gene on chromosome 11: sequence !1and tissue-specific expression. !$#cross-references MUID:88015526; PMID:2889183 !$#accession A26846 !'##molecule_type DNA !'##residues 1-217 ##label MEI !'##cross-references GB:Y00436; NID:g51387; PIDN:CAA68494.1; PID:g861031 !$#accession B26846 !'##molecule_type mRNA !'##residues 1-217 ##label ME2 !'##cross-references EMBL:Y00436; NID:g51387; PIDN:CAA68494.1; !1PID:g861031 REFERENCE A27176 !$#authors Hart, C.P.; Fainsod, A.; Ruddle, F.H. !$#journal Genomics (1987) 1:182-195 !$#title Sequence analysis of the murine Hox-2.2, -2.3, and -2.4 !1homeo boxes: evolutionary and structural comparisons. !$#cross-references MUID:88085193; PMID:2891608 !$#accession B27176 !'##molecule_type DNA !'##residues 134-210,'R',212-217 ##label HAR !'##cross-references EMBL:M18400 REFERENCE A29585 !$#authors Lonai, P.; Arman, E.; Czosnek, H.; Ruddle, F.H.; Blatt, C. !$#journal DNA (1987) 6:409-418 !$#title New murine homeoboxes: structure, chromosomal assignment, !1and differential expression in adult erythropoiesis. !$#cross-references MUID:88054465; PMID:2890503 !$#accession A29585 !'##molecule_type DNA !'##residues 'LCV',134-185,'G',187-205,'H',207-210,'A',212-217 ##label !1LON !'##cross-references EMBL:M18167 !'##note the authors translated the codon CAG for residue 186 as Gly REFERENCE S00987 !$#authors Kongsuwan, K.; Webb, E.; Housiaux, P.; Adams, J.M. !$#journal EMBO J. (1988) 7:2131-2138 !$#title Expression of multiple homeobox genes within diverse !1mammalian haemopoietic lineages. !$#cross-references MUID:88329001; PMID:2901346 !$#accession S00988 !'##molecule_type mRNA !'##residues 137-196 ##label KON !'##cross-references EMBL:X14570; NID:g51388; PIDN:CAA32708.1; !1PID:g930147 REFERENCE I48411 !$#authors Verrijzer, P.; de Graaff, W.; Deschamps, J.; Meijlink, F. !$#journal Nucleic Acids Res. (1988) 16:2729 !$#title Nucleotide sequence of the Hox2.3 gene region. !$#cross-references MUID:88203221; PMID:2896332 !$#accession I48411 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-217 ##label RES !'##cross-references EMBL:X06762; NID:g51389; PIDN:CAA29934.1; !1PID:g51390 GENETICS !$#gene Hox-2.3 !$#map_position 11 CLASSIFICATION #superfamily homeotic protein Hox A7; homeobox homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$138-194 #domain homeobox homology #label HOX SUMMARY #length 217 #molecular-weight 23912 #checksum 5892 SEQUENCE /// ENTRY A39164 #type complete TITLE homeotic protein Hox A7 - quail ALTERNATE_NAMES homeotic protein Quox-1 ORGANISM #formal_name Phasianidae gen. sp. #common_name quail DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A39164 REFERENCE A39164 !$#authors Xue, Z.G.; Gehring, W.J.; Le Douarin, N.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:2427-2431 !$#title Quox-1, a quail homeobox gene expressed in the embryonic !1central nervous system, including the forebrain. !$#cross-references MUID:91172821; PMID:1672453 !$#accession A39164 !'##status preliminary !'##molecule_type DNA !'##residues 1-242 ##label XUE !'##cross-references GB:M59714 CLASSIFICATION #superfamily homeotic protein Hox A7; homeobox homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$130-186 #domain homeobox homology #label HOX SUMMARY #length 242 #molecular-weight 28190 #checksum 6110 SEQUENCE /// ENTRY WJHU3C #type complete TITLE homeotic protein Hox C6 - human ALTERNATE_NAMES homeotic protein c8; homeotic protein cp25; homeotic protein Hox 3C ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 14-Nov-1997 ACCESSIONS B28030; S15539; S06165 REFERENCE A28030 !$#authors Simeone, A.; Mavilio, F.; Acampora, D.; Giampaolo, A.; !1Faiella, A.; Zappavigna, V.; D'Esposito, M.; Pannese, M.; !1Russo, G.; Boncinelli, E.; Peschle, C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:4914-4918 !$#title Two human homeobox genes, c1 and c8: structure analysis and !1expression in embryonic development. !$#cross-references MUID:87260899; PMID:2885844 !$#accession B28030 !'##molecule_type mRNA !'##residues 1-153 ##label SIM !'##cross-references GB:M16937 REFERENCE S15036 !$#authors Boncinelli, E.; Acampora, D.; Pannese, M.; d'Esposito, M.; !1Somma, R.; Gaudino, G.; Stornaiuolo, A.; Cafiero, M.; !1Faiella, A.; Simeone, A. !$#journal Genome (1989) 31:745-756 !$#title Organization of human class I homeobox genes. !$#cross-references MUID:90215256; PMID:2576652 !$#accession S15539 !'##molecule_type DNA !'##residues 59-124 ##label BON GENETICS !$#gene GDB:HOXC6 !'##cross-references GDB:120670; OMIM:142972 !$#map_position 12q13.3-12q13.3 !$#introns 52/1 CLASSIFICATION #superfamily homeotic protein Hox C6; homeobox homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$60-116 #domain homeobox homology #label HOX SUMMARY #length 153 #molecular-weight 17852 #checksum 3008 SEQUENCE /// ENTRY WJMSX6 #type complete TITLE homeotic protein Hox 6.1 - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 22-Jun-1999 ACCESSIONS S00987; S07810 REFERENCE S00987 !$#authors Kongsuwan, K.; Webb, E.; Housiaux, P.; Adams, J.M. !$#journal EMBO J. (1988) 7:2131-2138 !$#title Expression of multiple homeobox genes within diverse !1mammalian haemopoietic lineages. !$#cross-references MUID:88329001; PMID:2901346 !$#accession S00987 !'##molecule_type mRNA !'##residues 1-153 ##label KON !'##cross-references EMBL:X12504; NID:g51410; PIDN:CAA31023.1; !1PID:g51412 REFERENCE S07810 !$#authors Sharpe, P.T.; Miller, J.R.; Evans, E.P.; Burtenshaw, M.D.; !1Gaunt, S.J. !$#journal Development (1988) 102:397-407 !$#title Isolation and expression of a new mouse homeobox gene. !$#cross-references MUID:88328811; PMID:2458223 !$#accession S07810 !'##molecule_type DNA !'##residues 'N',50-109,'A',111-153 ##label SHA !'##cross-references EMBL:X16838; NID:g54097; PIDN:CAA34737.1; !1PID:g930199 !'##note the authors translated the codon GCG for residue 110 as Arg and !1GAA for residue 144 as Gly GENETICS !$#gene Hox 6.1 !$#map_position 14E2 CLASSIFICATION #superfamily homeotic protein Hox C6; homeobox homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$60-116 #domain homeobox homology #label HOX SUMMARY #length 153 #molecular-weight 17834 #checksum 2986 SEQUENCE /// ENTRY S02014 #type complete TITLE homeotic protein Hox 1 - eastern newt ORGANISM #formal_name Notophthalmus viridescens, Triturus viridescens #common_name eastern newt DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Dec-1999 ACCESSIONS S02014; S07819 REFERENCE S02014 !$#authors Savard, P.; Gates, P.B.; Brockes, J.P. !$#journal EMBO J. (1988) 7:4275-4282 !$#title Position dependent expression of a homeobox gene transcript !1in relation to amphibian limb regeneration. !$#cross-references MUID:89210814; PMID:2907476 !$#accession S02014 !'##molecule_type DNA !'##residues 1-234 ##label SAV !'##cross-references EMBL:X13957; NID:g64117; PIDN:CAA32139.1; !1PID:g64118 REFERENCE S07819 !$#authors Tabin, C.J. !$#journal Development (1989) 105:813-820 !$#title Isolation of potential vertebrate limb-identity genes. !$#cross-references MUID:90091821; PMID:2574663 !$#accession S07819 !'##molecule_type mRNA !'##residues 131-234 ##label TAB !'##cross-references EMBL:X16848; NID:g64115; PIDN:CAA34745.1; !1PID:g64116 GENETICS !$#gene Hox 1 CLASSIFICATION #superfamily homeotic protein Hox C6; homeobox homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$142-198 #domain homeobox homology #label HOX SUMMARY #length 234 #molecular-weight 26901 #checksum 2709 SEQUENCE /// ENTRY WJHU2I #type complete TITLE homeotic protein Hox B1 - human ALTERNATE_NAMES homeotic protein Hox 2I ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 22-Jun-1999 ACCESSIONS S07541; S15550 REFERENCE S07541 !$#authors Acampora, D.; d'Esposito, M.; Faiella, A.; Pannese, M.; !1Migliaccio, E.; Morelli, F.; Stornaiuolo, A.; Nigro, V.; !1Simeone, A.; Boncinelli, E. !$#journal Nucleic Acids Res. (1989) 17:10385-10402 !$#title The human HOX gene family. !$#cross-references MUID:90098876; PMID:2574852 !$#accession S07541 !'##molecule_type mRNA !'##residues 1-301 ##label ACA !'##cross-references EMBL:X16666; NID:g32383; PIDN:CAA34656.1; !1PID:g32384 REFERENCE S15036 !$#authors Boncinelli, E.; Acampora, D.; Pannese, M.; d'Esposito, M.; !1Somma, R.; Gaudino, G.; Stornaiuolo, A.; Cafiero, M.; !1Faiella, A.; Simeone, A. !$#journal Genome (1989) 31:745-756 !$#title Organization of human class I homeobox genes. !$#cross-references MUID:90215256; PMID:2576652 !$#accession S15550 !'##molecule_type DNA !'##residues 203-268 ##label BON GENETICS !$#gene GDB:HOXB1 !'##cross-references GDB:120666; OMIM:142968 !$#map_position 17q21.3-17q21.3 !$#introns 193/1 CLASSIFICATION #superfamily homeotic protein Hox B1; homeobox homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$204-260 #domain homeobox homology #label HOX SUMMARY #length 301 #molecular-weight 32121 #checksum 532 SEQUENCE /// ENTRY WJMS29 #type complete TITLE homeotic protein Hox 2.9 - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 22-Jun-1999 ACCESSIONS A60082; B35511; A43780; S11732 REFERENCE A60082 !$#authors Frohman, M.A.; Boyle, M.; Martin, G.R. !$#journal Development (1990) 110:589-607 !$#title Isolation of the mouse Hox-2.9 gene; analysis of embryonic !1expression suggests that positional information along the !1anterior-posterior axis is specified by mesoderm. !$#cross-references MUID:92155114; PMID:1983472 !$#accession A60082 !'##molecule_type mRNA; DNA !'##residues 1-297 ##label FRO !'##cross-references EMBL:X53063; NID:g51398; PIDN:CAA37238.1; !1PID:g297528 REFERENCE A35511 !$#authors Rubock, M.J.; Larin, Z.; Cook, M.; Papalopulu, N.; Krumlauf, !1R.; Lehrach, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:4751-4755 !$#title A yeast artificial chromosome containing the mouse homeobox !1cluster Hox-2. !$#cross-references MUID:90280453; PMID:1972280 !$#accession B35511 !'##molecule_type DNA !'##residues 199-259 ##label RUB !'##cross-references GB:M34005; NID:g193947; PIDN:AAA37850.1; !1PID:g193948 REFERENCE A43780 !$#authors Murphy, P.; Hill, R.E. !$#journal Development (1991) 111:61-74 !$#title Expression of the mouse labial-like homeobox-containing !1genes, Hox 2.9 and Hox 1.6, during segmentation of the !1hindbrain. !$#cross-references MUID:91199959; PMID:1673098 !$#accession A43780 !'##status preliminary !'##molecule_type mRNA !'##residues 1-37,'T',39-161,'C',163-197,'P',199,'R',201-233,'P',235-297 !1##label MUR !'##cross-references GB:X59474; NID:g51433; PIDN:CAA42078.1; PID:g51434 GENETICS !$#introns 188/2 CLASSIFICATION #superfamily homeotic protein Hox B1; homeobox homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$200-256 #domain homeobox homology #label HOX SUMMARY #length 297 #molecular-weight 31672 #checksum 8906 SEQUENCE /// ENTRY A60096 #type complete TITLE homeotic protein homolog Ghox-lab - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A60096 REFERENCE A60096 !$#authors Sundin, O.H.; Busse, H.G.; Rogers, M.B.; Gudas, L.J.; !1Eichele, G. !$#journal Development (1990) 108:47-58 !$#title Region-specific expression in early chick and mouse embryos !1of Ghox-lab and Hox 1.6, vertebrate homeobox-containing !1genes related to Drosophila labial. !$#cross-references MUID:90276239; PMID:1693558 !$#accession A60096 !'##molecule_type DNA !'##residues 1-309 ##label SUN !'##cross-references GB:X68352; NID:g63502; PIDN:CAA48418.1; !1PID:g833615; GB:X68353 !'##note the authors translated the codon GCG for residue 49 as Arg, and !1GCG for residue 111 as Gly GENETICS !$#introns 202/1 CLASSIFICATION #superfamily homeotic protein Hox B1; homeobox homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$214-270 #domain homeobox homology #label HOX SUMMARY #length 309 #molecular-weight 33832 #checksum 8717 SEQUENCE /// ENTRY WJHU4B #type complete TITLE homeotic protein Hox D4 - human ALTERNATE_NAMES homeotic protein c13; homeotic protein Hox 4B; homeotic protein Hox 5.1 ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 22-Jun-1999 ACCESSIONS S10985; A38787; A25238; S15546 REFERENCE S10985 !$#authors Cianetti, L.; di Cristofaro, A.; Zappavigna, V.; Bottero, !1L.; Boccoli, G.; Testa, U.; Russo, G.; Boncinelli, E.; !1Peschle, C. !$#journal Nucleic Acids Res. (1990) 18:4361-4368 !$#title Molecular mechanisms underlying the expression of the human !1HOX-5.1 gene. !$#cross-references MUID:90356367; PMID:1975093 !$#accession S10985 !'##molecule_type DNA !'##residues 1-255 ##label CIA !'##cross-references EMBL:X17360; NID:g32394; PIDN:CAA35237.1; !1PID:g296652 !$#accession A38787 !'##molecule_type mRNA !'##residues 1-122,'S',124-255 ##label CIA2 REFERENCE A25238 !$#authors Mavilio, F.; Simeone, A.; Giampaolo, A.; Faiella, A.; !1Zappavigna, V.; Acampora, D.; Poiana, G.; Russo, G.; !1Peschle, C.; Boncinelli, E. !$#journal Nature (1986) 324:664-668 !$#title Differential and stage-related expression in embryonic !1tissues of a new human homoeobox gene. !$#cross-references MUID:87090377; PMID:2879245 !$#accession A25238 !'##molecule_type mRNA !'##residues 1-122,'S',124-141,'A',143-255 ##label MAV !'##cross-references EMBL:X04706; NID:g32366; PIDN:CAA28411.1; !1PID:g32367 REFERENCE S15036 !$#authors Boncinelli, E.; Acampora, D.; Pannese, M.; d'Esposito, M.; !1Somma, R.; Gaudino, G.; Stornaiuolo, A.; Cafiero, M.; !1Faiella, A.; Simeone, A. !$#journal Genome (1989) 31:745-756 !$#title Organization of human class I homeobox genes. !$#cross-references MUID:90215256; PMID:2576652 !$#accession S15546 !'##molecule_type DNA !'##residues 154-219 ##label BON GENETICS !$#gene GDB:HOXD4 !'##cross-references GDB:120677; OMIM:142981 !$#map_position 2q31-2q31 !$#introns 145/1 FUNCTION !$#description control of embryonic development by tissue- and !1stage-specific regulation of transcription CLASSIFICATION #superfamily homeotic protein Hox D4; homeobox homology KEYWORDS DNA binding; embryo; homeobox; nucleus; transcription !1regulation FEATURE !$155-211 #domain homeobox homology #label HOX SUMMARY #length 255 #molecular-weight 27895 #checksum 7490 SEQUENCE /// ENTRY A36170 #type complete TITLE homeotic protein Hox D4 - mouse ALTERNATE_NAMES homeotic protein Hox 4.2; homeotic protein Hox 5.1 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 14-Dec-1990 #sequence_revision 14-Dec-1990 #text_change 24-Jul-1997 ACCESSIONS A36170 REFERENCE A36170 !$#authors Featherstone, M.S.; Baron, A.; Gaunt, S.J.; Mattei, M.G.; !1Duboule, D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:4760-4764 !$#title Hox-5.1 defines a homeobox-containing gene locus on mouse !1chromosome 2. !$#cross-references MUID:88263027; PMID:2898782 !$#accession A36170 !'##status preliminary !'##molecule_type DNA !'##residues 1-250 ##label FEA !'##cross-references GB:J03770 GENETICS !$#gene Hoxd-4 !$#map_position 2 FUNCTION !$#description control of embryonic development by tissue- and !1stage-specific regulation of transcription CLASSIFICATION #superfamily homeotic protein Hox D4; homeobox homology KEYWORDS DNA binding; embryo; homeobox; nucleus; transcription !1regulation FEATURE !$153-209 #domain homeobox homology #label HOX SUMMARY #length 250 #molecular-weight 27323 #checksum 6629 SEQUENCE /// ENTRY S09256 #type complete TITLE homeotic protein Hox D4 - chicken ALTERNATE_NAMES homeotic protein Chox-4.2; homeotic protein Chox-a ORGANISM #formal_name Gallus gallus #common_name chicken DATE 29-Jan-1993 #sequence_revision 29-Jan-1993 #text_change 24-Jul-1997 ACCESSIONS S09256 REFERENCE S09256 !$#authors Sasaki, H.; Yokoyama, E.; Kuroiwa, A. !$#journal Nucleic Acids Res. (1990) 18:1739-1747 !$#title Specific DNA binding of the two chicken deformed family !1homeodomain proteins, Chox-1.4 and Chox-a. !$#cross-references MUID:90245562; PMID:1970866 !$#accession S09256 !'##molecule_type mRNA !'##residues 1-236 ##label SAS !'##cross-references EMBL:X52671; EMBL:X52672 GENETICS !$#gene hoxd-4 FUNCTION !$#description control of embryonic development by tissue- and !1stage-specific regulation of transcription CLASSIFICATION #superfamily homeotic protein Hox D4; homeobox homology KEYWORDS DNA binding; embryo; homeobox; nucleus; transcription !1regulation FEATURE !$146-202 #domain homeobox homology #label HOX SUMMARY #length 236 #molecular-weight 26790 #checksum 3830 SEQUENCE /// ENTRY WJHU3E #type complete TITLE homeotic protein Hox C4 - human ALTERNATE_NAMES homeotic protein cp19; homeotic protein cp8; homeotic protein Hox 3E ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 22-Jun-1999 ACCESSIONS S01030; S15545 REFERENCE S01030 !$#authors Simeone, A.; Pannese, M.; Acampora, D.; d'Esposito, M.; !1Boncinelli, E. !$#journal Nucleic Acids Res. (1988) 16:5379-5390 !$#title At least three human homeoboxes on chromosome 12 belong to !1the same transcription unit. !$#cross-references MUID:88262550; PMID:2898768 !$#accession S01030 !'##molecule_type mRNA !'##residues 1-264 ##label SIM !'##cross-references EMBL:X07495; NID:g32385; PIDN:CAA30376.1; !1PID:g32386 !'##note the sequence from Fig. 4 is inconsistent with that from Fig. 3 !1in lacking 108-Ala and 109-Ser and in having 259-Gly REFERENCE S15036 !$#authors Boncinelli, E.; Acampora, D.; Pannese, M.; d'Esposito, M.; !1Somma, R.; Gaudino, G.; Stornaiuolo, A.; Cafiero, M.; !1Faiella, A.; Simeone, A. !$#journal Genome (1989) 31:745-756 !$#title Organization of human class I homeobox genes. !$#cross-references MUID:90215256; PMID:2576652 !$#accession S15545 !'##molecule_type DNA !'##residues 156-221 ##label BON GENETICS !$#gene GDB:HOXC4 !'##cross-references GDB:120672; OMIM:142974 !$#map_position 12q13.3-12q13.3 FUNCTION !$#description control of embryonic development by tissue- and !1stage-specific regulation of transcription CLASSIFICATION #superfamily homeotic protein Hox D4; homeobox homology KEYWORDS alternative splicing; DNA binding; embryo; homeobox; !1nucleus; transcription regulation FEATURE !$157-213 #domain homeobox homology #label HOX SUMMARY #length 264 #molecular-weight 29781 #checksum 1680 SEQUENCE /// ENTRY B60492 #type complete TITLE homeotic protein Hox B4 - human ALTERNATE_NAMES homeotic protein Hox 2.6; homeotic protein Hox 2F ORGANISM #formal_name Homo sapiens #common_name man DATE 19-Mar-1993 #sequence_revision 19-Mar-1993 #text_change 22-Jun-1999 ACCESSIONS B60492; C37042; S15543 REFERENCE A60492 !$#authors Peverali, F.A.; D'Esposito, M.; Acampora, D.; Bunone, G.; !1Negri, M.; Faiella, A.; Stornaiuolo, A.; Pannese, M.; !1Migliaccio, E.; Simeone, A.; Valle, G.D.; Boncinelli, E. !$#journal Differentiation (1990) 45:61-69 !$#title Expression of HOX homeogenes in human neuroblastoma cell !1culture lines. !$#cross-references MUID:91153613; PMID:1981366 !$#accession B60492 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-251 ##label PEV REFERENCE A37042 !$#authors Giampaolo, A.; Acampora, D.; Zappavigna, V.; Pannese, M.; !1D'Esposito, M.; Care, A.; Faiella, A.; Stornaiuolo, A.; !1Russo, G.; Simeone, A.; Boncinelli, E.; Peschle, C. !$#journal Differentiation (1989) 40:191-197 !$#title Differential expression of human HOX-2 genes along the !1anterior-posterior axis in embryonic central nervous system. !$#cross-references MUID:89378558; PMID:2570724 !$#accession C37042 !'##status preliminary !'##molecule_type DNA !'##residues 160-227 ##label GIA !'##cross-references GB:X16174; NID:g32376; PIDN:CAA34296.1; PID:g939889 REFERENCE S15036 !$#authors Boncinelli, E.; Acampora, D.; Pannese, M.; d'Esposito, M.; !1Somma, R.; Gaudino, G.; Stornaiuolo, A.; Cafiero, M.; !1Faiella, A.; Simeone, A. !$#journal Genome (1989) 31:745-756 !$#title Organization of human class I homeobox genes. !$#cross-references MUID:90215256; PMID:2576652 !$#accession S15543 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 162-227 ##label BON GENETICS !$#gene GDB:HOXB4 !'##cross-references GDB:120663; OMIM:142965 !$#map_position 17q21.3-17q21.3 FUNCTION !$#description control of embryonic development by tissue- and !1stage-specific regulation of transcription CLASSIFICATION #superfamily homeotic protein Hox D4; homeobox homology KEYWORDS DNA binding; embryo; homeobox; nucleus; transcription !1regulation FEATURE !$163-219 #domain homeobox homology #label HOX SUMMARY #length 251 #molecular-weight 27604 #checksum 841 SEQUENCE /// ENTRY A31757 #type complete TITLE homeotic protein Hox B4 - mouse ALTERNATE_NAMES homeotic protein Hox 2.6 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 07-Jun-1990 #sequence_revision 07-Jun-1990 #text_change 22-Jun-1999 ACCESSIONS A31757 REFERENCE A31757 !$#authors Graham, A.; Papalopulu, N.; Lorimer, J.; McVey, J.H.; !1Tuddenham, E.G.D.; Krumlauf, R. !$#journal Genes Dev. (1988) 2:1424-1438 !$#title Characterization of a murine homeo box gene, Hox-2.6, !1related to the Drosophila deformed gene. !$#cross-references MUID:89091992; PMID:2463210 !$#accession A31757 !'##molecule_type DNA !'##residues 1-250 ##label GRA !'##cross-references EMBL:M36654; NID:g193943; PIDN:AAA37848.1; !1PID:g193944 GENETICS !$#gene Hoxb-4 !$#map_position 11 !$#introns 151/3 FUNCTION !$#description control of embryonic development by tissue- and !1stage-specific regulation of transcription CLASSIFICATION #superfamily homeotic protein Hox D4; homeobox homology KEYWORDS DNA binding; embryo; homeobox; nucleus; transcription !1regulation FEATURE !$162-218 #domain homeobox homology #label HOX SUMMARY #length 250 #molecular-weight 27519 #checksum 713 SEQUENCE /// ENTRY S10092 #type complete TITLE homeotic protein Hox B4 - chicken ALTERNATE_NAMES homeotic protein Chox-2.6; homeotic protein Chox-Z ORGANISM #formal_name Gallus gallus #common_name chicken DATE 02-Dec-1993 #sequence_revision 03-Aug-1995 #text_change 22-Jun-1999 ACCESSIONS S10092 REFERENCE S10092 !$#authors Sasaki, H.; Kuroiwa, A. !$#journal Nucleic Acids Res. (1990) 18:184 !$#title The nucleotide sequence of the cDNA encoding a chicken !1deformed family homeobox gene, Chox-Z. !$#cross-references MUID:90174917; PMID:1968620 !$#accession S10092 !'##status preliminary !'##molecule_type mRNA !'##residues 1-245 ##label SAS !'##cross-references EMBL:X17612; NID:g63504; PIDN:CAA35614.1; !1PID:g63505 FUNCTION !$#description control of embryonic development by tissue- and !1stage-specific regulation of transcription CLASSIFICATION #superfamily homeotic protein Hox D4; homeobox homology KEYWORDS DNA binding; embryo; homeobox; nucleus; transcription !1regulation FEATURE !$151-207 #domain homeobox homology #label HOX SUMMARY #length 245 #molecular-weight 27782 #checksum 7772 SEQUENCE /// ENTRY A25108 #type complete TITLE homeotic protein Hox B4 - African clawed frog ALTERNATE_NAMES homeotic protein Hox-1A ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 22-Jun-1999 ACCESSIONS A25108 REFERENCE A25108 !$#authors Harvey, R.P.; Tabin, C.J.; Melton, D.A. !$#journal EMBO J. (1986) 5:1237-1244 !$#title Embryonic expression and nuclear localization of Xenopus !1homeobox (Xhox) gene products. !$#cross-references MUID:86274626; PMID:3015593 !$#accession A25108 !'##molecule_type mRNA !'##residues 1-232 ##label HAR !'##cross-references GB:M26884; NID:g214262; PIDN:AAA49756.1; !1PID:g214265 FUNCTION !$#description control of embryonic development by tissue- and !1stage-specific regulation of transcription CLASSIFICATION #superfamily homeotic protein Hox D4; homeobox homology KEYWORDS DNA binding; embryo; homeobox; nucleus; transcription !1regulation FEATURE !$142-198 #domain homeobox homology #label HOX SUMMARY #length 232 #molecular-weight 26467 #checksum 6431 SEQUENCE /// ENTRY S35219 #type complete TITLE homeotic protein Hox C4 - mouse ALTERNATE_NAMES homeotic protein Hox 3.5; homeotic protein MAB87 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Dec-1993 #sequence_revision 03-Aug-1995 #text_change 22-Jun-1999 ACCESSIONS S35219; A49153; C41606; I49752 REFERENCE S35219 !$#authors Goto, J.; Miyabayashi, T.; Wakamatsu, Y.; Takahashi, N.; !1Muramatsu, M. !$#journal Mol. Gen. Genet. (1993) 239:41-48 !$#title Organization and expression of mouse Hox3 cluster genes. !$#cross-references MUID:93288004; PMID:8099712 !$#accession S35219 !'##status preliminary !'##molecule_type DNA !'##residues 1-264 ##label GOT !'##cross-references GB:S62287; NID:g385749; PIDN:AAB27153.1; !1PID:g385750; GB:D11328; NID:g406212; PID:g416420 !'##note entry MUSHOX35A in GenBank release 103 duplicates GenBank entry !1S62287 except for an incorrect reference citation REFERENCE A49153 !$#authors Geada, A.M.; Gaunt, S.J.; Azzawi, M.; Shimeld, S.M.; Pearce, !1J.; Sharpe, P.T. !$#journal Development (1992) 116:497-506 !$#title Sequence and embryonic expression of the murine Hox-3.5 !1gene. !$#cross-references MUID:93161956; PMID:1363091 !$#accession A49153 !'##status preliminary !'##molecule_type mRNA !'##residues 1-79,'G',81-95,'S',97-264 ##label GEA !'##cross-references GB:X69019; NID:g396183; PIDN:CAA48784.1; !1PID:g396184 !'##note sequence extracted from NCBI backbone (NCBIN:124829, !1NCBIP:124830) REFERENCE A41606 !$#authors Murtha, M.T.; Leckman, J.F.; Ruddle, F.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:10711-10715 !$#title Detection of homeobox genes in development and evolution. !$#cross-references MUID:92073357; PMID:1720547 !$#accession C41606 !'##status preliminary !'##molecule_type DNA !'##residues 177-201 ##label MUR !'##cross-references GB:M81660; NID:g193975; PIDN:AAA63313.1; !1PID:g193976 GENETICS !$#gene Hoxc-4; Hox 3.5 !$#map_position 15 !$#introns 147/1 FUNCTION !$#description control of embryonic development by tissue- and !1stage-specific regulation of transcription CLASSIFICATION #superfamily homeotic protein Hox D4; homeobox homology KEYWORDS DNA binding; embryo; homeobox; nucleus; transcription !1regulation FEATURE !$157-213 #domain homeobox homology #label HOX SUMMARY #length 264 #molecular-weight 29865 #checksum 3249 SEQUENCE /// ENTRY A39724 #type complete TITLE homeotic protein Hox A4 - human ALTERNATE_NAMES homeotic protein Hox 1.4; homeotic protein Hox 1D ORGANISM #formal_name Homo sapiens #common_name man DATE 14-Feb-1992 #sequence_revision 14-Feb-1992 #text_change 26-Feb-1999 ACCESSIONS A39724; A60492; S15544; A32468 REFERENCE A39724 !$#authors Buettner, R.; Yim, S.O.; Hong, Y.S.; Boncinelli, E.; !1Tainsky, M.A. !$#journal Mol. Cell. Biol. (1991) 11:3573-3583 !$#title Alteration of homeobox gene expression by N-ras !1transformation of PA-1 human teratocarcinoma cells. !$#cross-references MUID:91260707; PMID:1675427 !$#accession A39724 !'##status preliminary !'##molecule_type mRNA !'##residues 1-320 ##label BUE !'##cross-references GB:M39724 REFERENCE A60492 !$#authors Peverali, F.A.; D'Esposito, M.; Acampora, D.; Bunone, G.; !1Negri, M.; Faiella, A.; Stornaiuolo, A.; Pannese, M.; !1Migliaccio, E.; Simeone, A.; Valle, G.D.; Boncinelli, E. !$#journal Differentiation (1990) 45:61-69 !$#title Expression of HOX homeogenes in human neuroblastoma cell !1culture lines. !$#cross-references MUID:91153613; PMID:1981366 !$#accession A60492 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-107,'A',109-320 ##label PEV REFERENCE S15036 !$#authors Boncinelli, E.; Acampora, D.; Pannese, M.; d'Esposito, M.; !1Somma, R.; Gaudino, G.; Stornaiuolo, A.; Cafiero, M.; !1Faiella, A.; Simeone, A. !$#journal Genome (1989) 31:745-756 !$#title Organization of human class I homeobox genes. !$#cross-references MUID:90215256; PMID:2576652 !$#accession S15544 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 215-280 ##label BON REFERENCE A32468 !$#authors Ferguson-Smith, A.C.; Fienberg, A.; Ruddle, F.H. !$#journal Genomics (1989) 5:250-258 !$#title Isolation, chromosomal localization, and nucleotide sequence !1of the human HOX 1.4 homeobox. !$#cross-references MUID:90007544; PMID:2571574 !$#accession A32468 !'##molecule_type DNA !'##residues 215-275 ##label FER !'##cross-references EMBL:M28199 COMMENT This homeotic protein is expressed in embryonic nervous !1system. GENETICS !$#gene GDB:HOXA4 !'##cross-references GDB:120650; OMIM:142953 !$#map_position 7p15.3-7p15.3 FUNCTION !$#description control of embryonic development by tissue- and !1stage-specific regulation of transcription CLASSIFICATION #superfamily homeotic protein Hox D4; homeobox homology KEYWORDS DNA binding; embryo; homeobox; nucleus; transcription !1regulation FEATURE !$216-272 #domain homeobox homology #label HOX SUMMARY #length 320 #molecular-weight 34505 #checksum 6579 SEQUENCE /// ENTRY A43556 #type complete TITLE homeotic protein Hox A4 - mouse ALTERNATE_NAMES homeotic protein 1.3; homeotic protein HBT-1; homeotic protein Hox 1.4; homeotic protein MH3 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 11-Dec-1992 #sequence_revision 11-Dec-1992 #text_change 22-Jun-1999 ACCESSIONS A43556; B43556; A25311; A25107; I49753; S26147 REFERENCE A43556 !$#authors Galliot, B.; Dolle, P.; Vigneron, M.; Featherstone, M.S.; !1Baron, A.; Duboule, D. !$#journal Development (1989) 107:343-359 !$#title The mouse Hox-1.4 gene: primary structure, evidence for !1promoter activity and expression during development. !$#cross-references MUID:90214520; PMID:2576648 !$#accession A43556 !'##molecule_type DNA !'##residues 1-285 ##label GAL !'##cross-references EMBL:X66861 !$#accession B43556 !'##molecule_type mRNA !'##residues 1-285 ##label GA2 REFERENCE A25311 !$#authors Rubin, M.R.; Toth, L.E.; Patel, M.D.; D'Eustachio, P.; !1Nguyen-Huu, M.C. !$#journal Science (1986) 233:663-667 !$#title A mouse homeo box gene is expressed in spermatocytes and !1embryos. !$#cross-references MUID:86261825; PMID:3726554 !$#accession A25311 !'##molecule_type mRNA !'##residues 180,'E',182-209,211-268,'H',270-271 ##label RUB !'##cross-references GB:M13813 REFERENCE A25107 !$#authors Wolgemuth, D.J.; Engelmyer, E.; Duggal, R.N.; !1Gizang-Ginsberg, E.; Mutter, G.L.; Ponzetto, C.; Viviano, !1C.; Zakeri, Z.F. !$#journal EMBO J. (1986) 5:1229-1235 !$#title Isolation of a mouse cDNA coding for a developmentally !1regulated, testis-specific transcript containing homeo box !1homology. !$#cross-references MUID:86274625; PMID:2426103 !$#accession A25107 !'##molecule_type mRNA !'##residues 198-268,'H',270-271 ##label WOL !'##cross-references GB:M27432 REFERENCE I49753 !$#authors Duggal, R.N.; Zakeri, Z.F.; Ponzetto, C.; Wolgemuth, D.J. !$#journal Ann. N. Y. Acad. Sci. (1987) 513:112-127 !$#title Differential expression of the c-abl proto-oncogene and the !1homeo box-containing gene Hox 1.4 during mouse !1spermatogenesis. !$#cross-references MUID:88181884; PMID:2895600 !$#accession I49753 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 180-268,'H',270-285 ##label RES !'##cross-references GB:M27432; NID:g193957; PIDN:AAA16440.1; !1PID:g193958 GENETICS !$#gene Hoxa-4; Hox 1.4; MH-3 !$#map_position 6 !$#introns 171/1 FUNCTION !$#description control of embryonic development by tissue- and !1stage-specific regulation of transcription CLASSIFICATION #superfamily homeotic protein Hox D4; homeobox homology KEYWORDS DNA binding; embryo; homeobox; nucleus; transcription !1regulation FEATURE !$181-237 #domain homeobox homology #label HOX SUMMARY #length 285 #molecular-weight 30441 #checksum 221 SEQUENCE /// ENTRY S09257 #type complete TITLE homeotic protein Hox A4 - chicken ALTERNATE_NAMES homeotic protein Chox1-4 ORGANISM #formal_name Gallus gallus #common_name chicken DATE 29-Jan-1993 #sequence_revision 29-Jan-1993 #text_change 21-Jul-2000 ACCESSIONS S09257; S10883 REFERENCE S09256 !$#authors Sasaki, H.; Yokoyama, E.; Kuroiwa, A. !$#journal Nucleic Acids Res. (1990) 18:1739-1747 !$#title Specific DNA binding of the two chicken deformed family !1homeodomain proteins, Chox-1.4 and Chox-a. !$#cross-references MUID:90245562; PMID:1970866 !$#accession S09257 !'##molecule_type mRNA !'##residues 1-309 ##label SAS !'##cross-references EMBL:X52670; NID:g63218; PIDN:CAA36896.1; !1PID:g63219 REFERENCE S10883 !$#authors Scotting, P.J.; Hewitt, M.; Keynes, R.J. !$#journal Nucleic Acids Res. (1990) 18:3999 !$#title Isolation and analysis of chick homeobox cDNA clones. !$#cross-references MUID:90326535; PMID:1973835 !$#accession S10883 !'##molecule_type mRNA !'##residues 207-273 ##label SCO !'##cross-references EMBL:X52747; NID:g63223; PIDN:CAB57949.1; !1PID:g6018426 FUNCTION !$#description control of embryonic development by tissue- and !1stage-specific regulation of transcription CLASSIFICATION #superfamily homeotic protein Hox D4; homeobox homology KEYWORDS DNA binding; embryo; homeobox; nucleus; transcription !1regulation FEATURE !$210-266 #domain homeobox homology #label HOX SUMMARY #length 309 #molecular-weight 33478 #checksum 6580 SEQUENCE /// ENTRY WJHU2H #type complete TITLE homeotic protein Hox B2 - human ALTERNATE_NAMES homeotic protein Hox 2.8; homeotic protein Hox 2H; homeotic protein K8 ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 22-Jun-1999 ACCESSIONS S07542; S00989; S15549; A56093; E37042; S44216 REFERENCE S07541 !$#authors Acampora, D.; d'Esposito, M.; Faiella, A.; Pannese, M.; !1Migliaccio, E.; Morelli, F.; Stornaiuolo, A.; Nigro, V.; !1Simeone, A.; Boncinelli, E. !$#journal Nucleic Acids Res. (1989) 17:10385-10402 !$#title The human HOX gene family. !$#cross-references MUID:90098876; PMID:2574852 !$#accession S07542 !'##molecule_type mRNA !'##residues 1-356 ##label ACA !'##cross-references EMBL:X16665; NID:g32381; PIDN:CAA34655.1; !1PID:g32382 REFERENCE S00987 !$#authors Kongsuwan, K.; Webb, E.; Housiaux, P.; Adams, J.M. !$#journal EMBO J. (1988) 7:2131-2138 !$#title Expression of multiple homeobox genes within diverse !1mammalian haemopoietic lineages. !$#cross-references MUID:88329001; PMID:2901346 !$#accession S00989 !'##molecule_type mRNA !'##residues 143-202 ##label KON !'##cross-references EMBL:X14571; NID:g32034; PIDN:CAA32709.1; !1PID:g930065 REFERENCE S15036 !$#authors Boncinelli, E.; Acampora, D.; Pannese, M.; d'Esposito, M.; !1Somma, R.; Gaudino, G.; Stornaiuolo, A.; Cafiero, M.; !1Faiella, A.; Simeone, A. !$#journal Genome (1989) 31:745-756 !$#title Organization of human class I homeobox genes. !$#cross-references MUID:90215256; PMID:2576652 !$#accession S15549 !'##molecule_type DNA !'##residues 143-208 ##label BON REFERENCE A56093 !$#authors Vieille-Grosjean, I.; Huber, P. !$#journal J. Biol. Chem. (1995) 270:4544-4550 !$#title Transcription factor GATA-1 regulates human HOXB2 gene !1expression in erythroid cells. !$#cross-references MUID:95181447; PMID:7876223 !$#accession A56093 !'##molecule_type DNA !'##residues 1-42 ##label VI2 !'##cross-references GB:X78978; NID:g475199; PIDN:CAA55581.1; !1PID:g475200 REFERENCE A37042 !$#authors Giampaolo, A.; Acampora, D.; Zappavigna, V.; Pannese, M.; !1D'Esposito, M.; Care, A.; Faiella, A.; Stornaiuolo, A.; !1Russo, G.; Simeone, A.; Boncinelli, E.; Peschle, C. !$#journal Differentiation (1989) 40:191-197 !$#title Differential expression of human HOX-2 genes along the !1anterior-posterior axis in embryonic central nervous system. !$#cross-references MUID:89378558; PMID:2570724 !$#accession E37042 !'##molecule_type DNA !'##residues 132-135,'RRL',139-208 ##label GIA !'##cross-references GB:X16176; NID:g32378; PIDN:CAA34298.1; PID:g930069 GENETICS !$#gene GDB:HOXB2 !'##cross-references GDB:120665; OMIM:142967 !$#map_position 17q21.3-17q21.3 !$#introns 131/1 CLASSIFICATION #superfamily homeotic protein Hox B2; homeobox homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$76-96 #region proline-rich\ !$144-200 #domain homeobox homology #label HOX SUMMARY #length 356 #molecular-weight 37913 #checksum 6644 SEQUENCE /// ENTRY WJHU2G #type complete TITLE homeotic protein Hox B3 - human ALTERNATE_NAMES homeotic protein Hox 2.7; homeotic protein Hox 2G ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 22-Jun-1999 ACCESSIONS S07543; S15547; D37042 REFERENCE S07541 !$#authors Acampora, D.; d'Esposito, M.; Faiella, A.; Pannese, M.; !1Migliaccio, E.; Morelli, F.; Stornaiuolo, A.; Nigro, V.; !1Simeone, A.; Boncinelli, E. !$#journal Nucleic Acids Res. (1989) 17:10385-10402 !$#title The human HOX gene family. !$#cross-references MUID:90098876; PMID:2574852 !$#accession S07543 !'##molecule_type mRNA !'##residues 1-431 ##label ACA !'##cross-references EMBL:X16667; NID:g32379; PIDN:CAA34657.1; !1PID:g32380 REFERENCE S15036 !$#authors Boncinelli, E.; Acampora, D.; Pannese, M.; d'Esposito, M.; !1Somma, R.; Gaudino, G.; Stornaiuolo, A.; Cafiero, M.; !1Faiella, A.; Simeone, A. !$#journal Genome (1989) 31:745-756 !$#title Organization of human class I homeobox genes. !$#cross-references MUID:90215256; PMID:2576652 !$#accession S15547 !'##molecule_type DNA !'##residues 188-253 ##label BON REFERENCE A37042 !$#authors Giampaolo, A.; Acampora, D.; Zappavigna, V.; Pannese, M.; !1D'Esposito, M.; Care, A.; Faiella, A.; Stornaiuolo, A.; !1Russo, G.; Simeone, A.; Boncinelli, E.; Peschle, C. !$#journal Differentiation (1989) 40:191-197 !$#title Differential expression of human HOX-2 genes along the !1anterior-posterior axis in embryonic central nervous system. !$#cross-references MUID:89378558; PMID:2570724 !$#accession D37042 !'##molecule_type DNA !'##residues 188-253 ##label GIA !'##cross-references GB:X16175; NID:g32377; PIDN:CAA34297.1; PID:g930068 GENETICS !$#gene GDB:HOXB3 !'##cross-references GDB:120664; OMIM:142966 !$#map_position 17q21.3-17q21.3 !$#introns 150/1 CLASSIFICATION #superfamily homeotic protein Hox B3; homeobox homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$152-178 #region glycine-rich\ !$189-245 #domain homeobox homology #label HOX SUMMARY #length 431 #molecular-weight 44344 #checksum 2117 SEQUENCE /// ENTRY S71480 #type complete TITLE homeotic protein Hox B3 - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S71480 REFERENCE S71480 !$#authors Scotting, P.J.; Rex, M. !$#submission submitted to the EMBL Data Library, August 1993 !$#accession S71480 !'##status preliminary !'##molecule_type mRNA !'##residues 1-399 ##label SCO !'##cross-references EMBL:X74506; NID:g398704; PIDN:CAA52613.1; !1PID:g443794 GENETICS !$#gene Hox-B3 CLASSIFICATION #superfamily homeotic protein Hox B3; homeobox homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$160-216 #domain homeobox homology #label HOX SUMMARY #length 399 #molecular-weight 43504 #checksum 1861 SEQUENCE /// ENTRY WJHU1C #type complete TITLE homeotic protein Hox A5 - human ALTERNATE_NAMES homeotic protein Hox 1.3; homeotic protein Hox 1C ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 22-Jun-1999 ACCESSIONS A32799; S15541 REFERENCE A32799 !$#authors Tournier-Lasserve, E.; Odenwald, W.F.; Garbern, J.; !1Trojanowski, J.; Lazzarini, R.A. !$#journal Mol. Cell. Biol. (1989) 9:2273-2278 !$#title Remarkable intron and exon sequence conservation in human !1and mouse homeobox Hox 1.3 genes. !$#cross-references MUID:89313782; PMID:2568583 !$#accession A32799 !'##molecule_type DNA !'##residues 1-270 ##label TOU !'##cross-references EMBL:M26679; NID:g341517; PIDN:AAA58663.1; !1PID:g387668 REFERENCE S15036 !$#authors Boncinelli, E.; Acampora, D.; Pannese, M.; d'Esposito, M.; !1Somma, R.; Gaudino, G.; Stornaiuolo, A.; Cafiero, M.; !1Faiella, A.; Simeone, A. !$#journal Genome (1989) 31:745-756 !$#title Organization of human class I homeobox genes. !$#cross-references MUID:90215256; PMID:2576652 !$#accession S15541 !'##molecule_type DNA !'##residues 195-260 ##label BON GENETICS !$#gene GDB:HOXA5 !'##cross-references GDB:120649; OMIM:142952 !$#map_position 7p15.3-7p15.3 !$#introns 188/1 CLASSIFICATION #superfamily homeotic protein Hox A5; homeobox homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$196-252 #domain homeobox homology #label HOX SUMMARY #length 270 #molecular-weight 29359 #checksum 4744 SEQUENCE /// ENTRY WJMS13 #type complete TITLE homeotic protein Hox A5 - mouse ALTERNATE_NAMES homeotic protein Hox 1.3; homeotic protein m2 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 24-Sep-1999 ACCESSIONS S07812; A27051; A38763 REFERENCE A30340 !$#authors Fibi, M.; Zink, B.; Kessel, M.; Colberg-Poley, A.M.; Labeit, !1S.; Lehrach, H.; Gruss, P. !$#journal Development (1988) 102:349-359 !$#title Coding sequence and expression of the homeobox gene Hox 1.3. !$#cross-references MUID:88328807; PMID:2901335 !$#accession S07812 !'##molecule_type mRNA !'##residues 1-270 ##label FIB !'##cross-references EMBL:X16840; NID:g51470; PIDN:CAA34738.1; !1PID:g51471 REFERENCE A27051 !$#authors Odenwald, W.F.; Taylor, C.F.; Palmer-Hill, F.J.; Friedrich !1Jr., V.; Tani, M.; Lazzarini, R.A. !$#journal Genes Dev. (1987) 1:482-496 !$#title Expression of a homeo domain protein in noncontact-inhibited !1cultured cells and postmitotic neurons. !$#cross-references MUID:88056292; PMID:2890554 !$#accession A27051 !'##molecule_type DNA !'##residues 1-270 ##label ODE !'##cross-references GB:Y00208; NID:g51371; PIDN:CAA68364.1; PID:g51372 !'##experimental_source strain Balb/c !$#accession A38763 !'##molecule_type mRNA !'##residues 1-270 ##label ODE2 !'##cross-references GB:Y00208; NID:g51371; PIDN:CAA68364.1; PID:g51372 GENETICS !$#gene Hox 1.3 !$#map_position 6 !$#introns 187/3 CLASSIFICATION #superfamily homeotic protein Hox A5; homeobox homology KEYWORDS DNA binding; homeobox; nucleus; phosphoprotein; !1transcription regulation FEATURE !$196-252 #domain homeobox homology #label HOX SUMMARY #length 270 #molecular-weight 29237 #checksum 3713 SEQUENCE /// ENTRY WJZFX2 #type complete TITLE homeotic protein Hox B5 - zebra fish ALTERNATE_NAMES homeotic protein Hox 2.1; homeotic protein ZF-21 ORGANISM #formal_name Brachydanio rerio #common_name zebra fish DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 22-Jun-1999 ACCESSIONS S03671; S00395; S32564; S25595 REFERENCE S03671 !$#authors Njolstad, P.R.; Molven, A.; Hordvik, I.; Apold, J.; Fjose, !1A. !$#journal Nucleic Acids Res. (1988) 16:9097-9111 !$#title Primary structure, developmentally regulated expression and !1potential duplication of the zebrafish homeobox gene ZF-21. !$#cross-references MUID:89016617; PMID:2902580 !$#accession S03671 !'##molecule_type mRNA !'##residues 1-275 ##label NJO !'##cross-references EMBL:X12802; NID:g62554; PIDN:CAA31290.1; !1PID:g62555 !'##note the authors translated the codon ACG for residue 212 as Tyr REFERENCE S00395 !$#authors Njolstad, P.R.; Molven, A.; Fjose, A. !$#journal FEBS Lett. (1988) 230:25-30 !$#title A zebrafish homologue of the murine Hox-2.1 gene. !$#cross-references MUID:88167192; PMID:2895022 !$#accession S00395 !'##molecule_type DNA !'##residues 195-275 ##label NJ2 !'##cross-references EMBL:X07381; NID:g62527; PIDN:CAA30293.1; !1PID:g62528 REFERENCE S32563 !$#authors Molven, A.; Hordvik, I.; Njolstad, P.R. !$#journal Biochim. Biophys. Acta (1993) 1173:102-106 !$#title Sequence analysis of the zebrafish hox-B5/B6 region. !$#cross-references MUID:93250038; PMID:8097929 !$#accession S32564 !'##status preliminary !'##molecule_type DNA !'##residues 1-275 ##label MOL !'##cross-references EMBL:X68248; NID:g62535; PIDN:CAA48320.1; !1PID:g62537 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1992 !'##note only a small part of the coding sequence is given !'##note only a small part of the translation is shown GENETICS !$#gene Hox-B5; Hox 2.1 !$#introns 194/1 CLASSIFICATION #superfamily homeotic protein Hox A5; homeobox homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$201-257 #domain homeobox homology #label HOX SUMMARY #length 275 #molecular-weight 30754 #checksum 7940 SEQUENCE /// ENTRY A43551 #type complete TITLE homeotic protein Hox B5 - mouse ALTERNATE_NAMES homeotic protein Hox 2.1 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 01-Dec-1992 #sequence_revision 23-May-1997 #text_change 21-Jul-2000 ACCESSIONS A43551; A26508 REFERENCE A43551 !$#authors Krumlauf, R.; Holland, P.W.H.; McVey, J.H.; Hogan, B.L.M. !$#journal Development (1987) 99:603-617 !$#title Developmental and spatial patterns of expression of the !1mouse homeobox gene, Hox 2.1. !$#cross-references MUID:88029099; PMID:2889591 !$#accession A43551 !'##status preliminary !'##molecule_type mRNA !'##residues 1-269 ##label KRU !'##cross-references GB:M26283; NID:g522334; PIDN:AAA37842.1; !1PID:g522335 REFERENCE A26508 !$#authors Jackson, I.J.; Schofield, P.; Hogan, B. !$#journal Nature (1985) 317:745-748 !$#title A mouse homoeo box gene is expressed during embryogenesis !1and in adult kidney. !$#cross-references MUID:86040438; PMID:4058581 !$#accession A26508 !'##molecule_type DNA !'##residues 192-259 ##label JAC !'##cross-references GB:X03033; NID:g51360; PIDN:CAB57812.1; !1PID:g6015585 CLASSIFICATION #superfamily homeotic protein Hox A5; homeobox homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$195-251 #domain homeobox homology #label HOX SUMMARY #length 269 #molecular-weight 29464 #checksum 1157 SEQUENCE /// ENTRY S03631 #type complete TITLE homeotic protein Scr - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES sex combs reduced protein ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S03631 REFERENCE S03631 !$#authors LeMotte, P.K.; Kuroiwa, A.; Fessler, L.I.; Gehring, W.J. !$#journal EMBO J. (1989) 8:219-227 !$#title The homeotic gene sex combs reduced of Drosophila: gene !1structure and embryonic expression. !$#cross-references MUID:89231621; PMID:2565809 !$#accession S03631 !'##molecule_type DNA !'##residues 1-413 ##label LEM !'##cross-references EMBL:X14475 GENETICS !$#gene Scr !'##cross-references FlyBase:FBgn0003339 CLASSIFICATION #superfamily homeotic protein Scr; homeobox homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$321-377 #domain homeobox homology #label HOX SUMMARY #length 413 #molecular-weight 44993 #checksum 1499 SEQUENCE /// ENTRY WJFFBC #type complete TITLE homeotic protein bicoid - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES bcd homeotic protein ORGANISM #formal_name Drosophila melanogaster DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 22-Jun-1999 ACCESSIONS S00835 REFERENCE S00835 !$#authors Berleth, T.; Burri, M.; Thoma, G.; Bopp, D.; Richstein, S.; !1Frigerio, G.; Noll, M.; Nuesslein-Volhard, C. !$#journal EMBO J. (1988) 7:1749-1756 !$#title The role of localization of bicoid RNA in organizing the !1anterior pattern of the Drosophila embryo. !$#cross-references MUID:89005064; PMID:2901954 !$#accession S00835 !'##molecule_type DNA !'##residues 1-494 ##label BER !'##cross-references EMBL:X07870; NID:g7648; PIDN:CAA30720.1; !1PID:g311722 !'##note 247-Ala, 298-Ser, and 460-Met were also found GENETICS !$#gene FlyBase:bcd !'##cross-references FlyBase:FBgn0000166 !$#map_position 3R 84A !$#introns 55/3; 81/1; 400/3 FUNCTION !$#description controls anterior pattern (development of head and thorax) !1in the Drosophila embryo; activates transcription of target !1genes; binds to and represses translation of the homeodomain !1protein caudal mRNA CLASSIFICATION #superfamily homeotic protein bicoid; homeobox homology KEYWORDS alternative splicing; DNA binding; homeobox; nucleus; RNA !1binding; transcription regulation; translation repressor FEATURE !$1-494 #product homeotic protein bicoid (transcript 1) !8#status predicted #label MAT1\ !$1-80,86-494 #product homeotic protein bicoid (transcript 2) !8#status predicted #label MAT2\ !$1-55,401-494 #product homeotic protein bicoid (transcript 3) !8#status predicted #label MAT3\ !$12-40 #region histidine-rich\ !$98-154 #domain homeobox homology #label HOX\ !$258-304 #region glutamine-rich SUMMARY #length 494 #molecular-weight 54493 #checksum 8832 SEQUENCE /// ENTRY S12570 #type complete TITLE homeotic protein bicoid - fruit fly (Drosophila pseudoobscura) ALTERNATE_NAMES homeotic protein bcd ORGANISM #formal_name Drosophila pseudoobscura DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S12570 REFERENCE S12570 !$#authors Seeger, M.A.; Kaufman, T.C. !$#journal EMBO J. (1990) 9:2977-2987 !$#title Molecular analysis of the bicoid gene from Drosophila !1pseudoobscura: identification of conserved domains within !1coding and noncoding regions of the bicoid mRNA. !$#cross-references MUID:90361013; PMID:1975239 !$#accession S12570 !'##molecule_type DNA !'##residues 1-538 ##label SEE !'##cross-references EMBL:X55735; NID:g9048; PIDN:CAA39267.1; PID:g9049 GENETICS !$#gene bcd !'##cross-references FlyBase:FBgn0012719 !$#introns 54/3; 80/1; 444/3 CLASSIFICATION #superfamily homeotic protein bicoid; homeobox homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$92-148 #domain homeobox homology #label HOX SUMMARY #length 538 #molecular-weight 59476 #checksum 4951 SEQUENCE /// ENTRY S03170 #type complete TITLE homeotic protein cut - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S03170 REFERENCE S03170 !$#authors Blochlinger, K.; Bodmer, R.; Jack, J.; Jan, L.Y.; Jan, Y.N. !$#journal Nature (1988) 333:629-635 !$#title Primary structure and expression of a product from cut, a !1locus involved in specifying sensory organ identity in !1Drosophila. !$#cross-references MUID:88232956; PMID:2897632 !$#accession S03170 !'##molecule_type mRNA !'##residues 1-2175 ##label BLO !'##cross-references EMBL:X07985; NID:g7767; PIDN:CAA30794.1; PID:g7768 GENETICS !$#gene cut !'##cross-references FlyBase:FBgn0004198 CLASSIFICATION #superfamily homeotic protein cut; cut repeat homology; !1homeobox homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$886-958 #domain cut repeat homology #label CU1\ !$1339-1411 #domain cut repeat homology #label CU2\ !$1617-1689 #domain cut repeat homology #label CU3\ !$1746-1802 #domain homeobox homology #label HOX SUMMARY #length 2175 #molecular-weight 233627 #checksum 2025 SEQUENCE /// ENTRY I48314 #type complete TITLE homeotic protein CDP - mouse ALTERNATE_NAMES CCAAT displacement protein; homeotic protein Cux ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS I48314 REFERENCE I48314 !$#authors Valarche, I.; Tissier-Seta, J.P.; Hirsch, M.R.; Martinez, !1S.; Goridis, C.; Brunet, J.F. !$#journal Development (1993) 119:881-896 !$#title The mouse homeodomain protein Phox2 regulates Ncam promoter !1activity in concert with Cux/CDP and is a putative !1determinant of neurotransmitter phenotype. !$#cross-references MUID:94244481; PMID:7910552 !$#accession I48314 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-1332 ##label RES !'##cross-references EMBL:X75013; NID:g402589; PIDN:CAA52922.1; !1PID:g402590 GENETICS !$#gene Cux CLASSIFICATION #superfamily homeotic protein CDP; cut repeat homology; !1homeobox homology KEYWORDS DNA binding; duplication; homeobox; nucleus; transcription !1regulation FEATURE !$366-438 #domain cut repeat homology #label CU1\ !$755-827 #domain cut repeat homology #label CU2\ !$938-1010 #domain cut repeat homology #label CU3\ !$1057-1113 #domain homeobox homology #label HOX SUMMARY #length 1332 #molecular-weight 144274 #checksum 2323 SEQUENCE /// ENTRY WJFFFT #type complete TITLE fushi tarazu segmentation protein - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES ftz segmentation protein ORGANISM #formal_name Drosophila melanogaster DATE 28-May-1986 #sequence_revision 17-Mar-1987 #text_change 22-Jun-1999 ACCESSIONS A93334; A90847; A03320 REFERENCE A93334 !$#authors Laughon, A.; Scott, M.P. !$#journal Nature (1984) 310:25-31 !$#title Sequence of a Drosophila segmentation gene: protein !1structure homology with DNA-binding proteins. !$#cross-references MUID:84245843; PMID:6330566 !$#accession A93334 !'##molecule_type DNA !'##residues 1-413 ##label LAU !'##cross-references GB:X00854; GB:K01951; NID:g7984; PIDN:CAA25408.1; !1PID:g7986 !'##note the authors translated the codon AAT for residue 228 as Asp REFERENCE A90847 !$#authors McGinnis, W.; Garber, R.L.; Wirz, J.; Kuroiwa, A.; Gehring, !1W.J. !$#journal Cell (1984) 37:403-408 !$#title A homologous protein-coding sequence in Drosophila homeotic !1genes and its conservation in other metazoans. !$#cross-references MUID:84205674; PMID:6327065 !$#contents homeo box !$#accession A90847 !'##molecule_type DNA !'##residues 253-323 ##label MCG COMMENT This homeotic protein, required in alternating segment !1primordia, specifies the correct number of segments. GENETICS !$#gene ftz !'##cross-references FlyBase:FBgn0001077 !$#map_position 3R,47.8 (84B1-2) !$#introns 253/1 CLASSIFICATION #superfamily fushi tarazu segmentation protein; homeobox !1homology KEYWORDS DNA binding; embryo; homeobox; nucleus; transcription !1regulation FEATURE !$258-314 #domain homeobox homology #label HOX\ !$285-317 #region DNA binding #status predicted SUMMARY #length 413 #molecular-weight 46871 #checksum 925 SEQUENCE /// ENTRY WJFFEN #type complete TITLE homeotic protein engrailed - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES specific body pattern development protein ORGANISM #formal_name Drosophila melanogaster DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 16-Jun-2000 ACCESSIONS A90862; A93354; A03321; A03322; A25682; S03667 REFERENCE A90862 !$#authors Poole, S.J.; Kauvar, L.M.; Drees, B.; Kornberg, T. !$#journal Cell (1985) 40:37-43 !$#title The engrailed locus of Drosophila: structural analysis of an !1embryonic transcript. !$#cross-references MUID:85099327; PMID:3917855 !$#accession A90862 !'##molecule_type mRNA !'##residues 1-552 ##label POO !'##cross-references GB:M10017; NID:g157363; PIDN:AAA65478.1; !1PID:g763443 REFERENCE A93354 !$#authors Fjose, A.; McGinnis, W.J.; Gehring, W.J. !$#journal Nature (1985) 313:284-289 !$#title Isolation of a homoeo box-containing gene from the engrailed !1region of Drosophila and the spatial distribution of its !1transcripts. !$#cross-references MUID:90114393; PMID:2481829 !$#accession A93354 !'##molecule_type DNA !'##residues 447-485,'E',487-518,'WH' ##label FJO !'##cross-references GB:X01765; GB:K03059; NID:g8084; PIDN:CAA25906.1; !1PID:g1345472 !'##note the translation of the nucleotide sequence from Fig. 5 is !1shown, not the translation in Fig. 6; GenBank entry !1DMHOB48A, release 116.0, differs in translating only the !1single exon portion shown in Fig. 6 REFERENCE A91059 !$#authors Kassis, J.A.; Poole, S.J.; Wright, D.K.; O'Farrell, P.H. !$#journal EMBO J. (1986) 5:3583-3589 !$#title Sequence conservation in the protein coding and intron !1regions of the engrailed transcription unit. !$#cross-references MUID:87161768; PMID:2881781 !$#contents annotation; intron locations and sequences REFERENCE S03667 !$#authors Gay, N.J.; Poole, S.J.; Kornberg, T.B. !$#journal Nucleic Acids Res. (1988) 16:6637-6647 !$#title The Drosophila engrailed protein is phosphorylated by a !1serine-specific protein kinase. !$#cross-references MUID:88289425; PMID:2899884 !$#contents annotation; potential phosphorylation sites; homeobox domain COMMENT This protein specifies the body segmentation pattern. GENETICS !$#gene en !'##cross-references FlyBase:FBgn0000577 !$#map_position 2R,62.0 (48A1-4) !$#introns 438/1; 470/3 CLASSIFICATION #superfamily engrailed homeotic protein; homeobox homology KEYWORDS DNA binding; embryo; homeobox; nucleus; segmentation; !1transcription regulation FEATURE !$26-53 #region glutamine-rich\ !$68-87 #region alanine-rich\ !$232-240 #region alanine-rich\ !$320-368 #region serine-rich\ !$455-511 #domain homeobox homology #label HOX SUMMARY #length 552 #molecular-weight 59419 #checksum 1543 SEQUENCE /// ENTRY A54677 #type complete TITLE homeotic protein goosecoid [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Sep-2000 ACCESSIONS A54677 REFERENCE A54677 !$#authors Blum, M.; De Robertis, E.M.; Kojis, T.; Heinzmann, C.; !1Klisak, I.; Geissert, D.; Sparkes, R.S. !$#journal Genomics (1994) 21:388-393 !$#title Molecular cloning of the human homeobox gene goosecoid (GSC) !1and mapping of the gene to human chromosome 14q32.1. !$#cross-references MUID:94375063; PMID:7916327 !$#accession A54677 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-252 ##label BLU GENETICS !$#gene GDB:GSC !'##cross-references GDB:251683; OMIM:138890 !$#map_position 14q32.1-14q32.1 CLASSIFICATION #superfamily homeotic protein goosecoid; homeobox homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$156-212 #domain homeobox homology #label HOX SUMMARY #length 252 #molecular-weight 27853 #checksum 8768 SEQUENCE /// ENTRY A42768 #type complete TITLE homeotic protein goosecoid [similarity] - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Sep-2000 ACCESSIONS A42768 REFERENCE A42768 !$#authors Blum, M.; Gaunt, S.J.; Cho, K.W.Y.; Steinbeisser, H.; !1Blumberg, B.; Bittner, D.; De Robertis, E.M. !$#journal Cell (1992) 69:1097-1106 !$#title Gastrulation in the mouse: the role of the homeobox gene !1goosecoid. !$#cross-references MUID:92315328; PMID:1352187 !$#accession A42768 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-256 ##label BLU !'##cross-references GB:M85271; NID:g193895; PIDN:AAA37826.1; !1PID:g193896 !'##note sequence extracted from NCBI backbone (NCBIP:108110) CLASSIFICATION #superfamily homeotic protein goosecoid; homeobox homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$161-217 #domain homeobox homology #label HOX SUMMARY #length 256 #molecular-weight 27979 #checksum 6332 SEQUENCE /// ENTRY A47539 #type complete TITLE homeotic protein goosecoid [similarity] - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Sep-2000 ACCESSIONS A47539 REFERENCE A47539 !$#authors Izpisua-Belmonte, J.C.; De Robertis, E.M.; Storey, K.G.; !1Stern, C.D. !$#journal Cell (1993) 74:645-659 !$#title The homeobox gene goosecoid and the origin of organizer !1cells in the early chick blastoderm. !$#cross-references MUID:93364981; PMID:7916659 !$#accession A47539 !'##status preliminary !'##molecule_type mRNA !'##residues 1-245 ##label IZP !'##cross-references EMBL:X70471; NID:g402580; PIDN:CAA49897.1; !1PID:g402581 CLASSIFICATION #superfamily homeotic protein goosecoid; homeobox homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$151-207 #domain homeobox homology #label HOX SUMMARY #length 245 #molecular-weight 27269 #checksum 6936 SEQUENCE /// ENTRY B42768 #type complete TITLE homeotic protein goosecoid - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B42768; D40856 REFERENCE A42768 !$#authors Blum, M.; Gaunt, S.J.; Cho, K.W.Y.; Steinbeisser, H.; !1Blumberg, B.; Bittner, D.; De Robertis, E.M. !$#journal Cell (1992) 69:1097-1106 !$#title Gastrulation in the mouse: the role of the homeobox gene !1goosecoid. !$#cross-references MUID:92315328; PMID:1352187 !$#accession B42768 !'##status preliminary !'##molecule_type mRNA !'##residues 1-243 ##label BLU !'##cross-references GB:M63872 REFERENCE A40856 !$#authors Blumberg, B.; Wright, C.V.E.; De Robertis, E.M.; Cho, K.W.Y. !$#journal Science (1991) 253:194-196 !$#title Organizer-specific homeobox genes in Xenopus laevis embryos. !$#cross-references MUID:91305940; PMID:1677215 !$#accession D40856 !'##status preliminary !'##molecule_type mRNA !'##residues 148-207 ##label BL2 !'##cross-references GB:M63872 CLASSIFICATION #superfamily homeotic protein goosecoid; homeobox homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$149-205 #domain homeobox homology #label HOX SUMMARY #length 243 #molecular-weight 27424 #checksum 8793 SEQUENCE /// ENTRY S70617 #type complete TITLE homeotic protein goosecoid - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES homeobox protein goosecoid ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 17-Nov-2000 ACCESSIONS S70617 REFERENCE S70617 !$#authors Hahn, M.; Jaeckle, H. !$#journal EMBO J. (1996) 15:3077-3084 !$#title Drosophila goosecoid participates in neural development but !1not in body axis formation. !$#cross-references MUID:96272167; PMID:8670808 !$#accession S70617 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-419 ##label HAH !'##cross-references EMBL:U52968; NID:g1399586; PIDN:AAB17948.1; !1PID:g1399587 GENETICS !$#gene gsc !'##cross-references FlyBase:FBgn0010323 !$#map_position 2 FUNCTION !$#description plays a role in neurogenesis in post-gastrula Drosophila !1embryos !$#note not required for gastrulation like Xenopus goosecoid; !1expressed most strongly in the foregut anlage CLASSIFICATION #superfamily fruit fly homeotic protein goosecoid; homeobox !1homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$287-343 #domain homeobox homology #label HOX SUMMARY #length 419 #molecular-weight 44949 #checksum 8390 SEQUENCE /// ENTRY I58311 #type complete TITLE HMG-box containing protein 1 - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 08-Oct-1999 ACCESSIONS I58311 REFERENCE I58311 !$#authors Lesage, F.; Hugnot, J.P.; Amri, E.Z.; Grimaldi, P.; !1Barhanin, J.; Lazdunski, M. !$#journal Nucleic Acids Res. (1994) 22:3685-3688 !$#title Expression cloning in K+ transport defective yeast and !1distribution of HBP1, a new putative HMG transcriptional !1regulator. !$#cross-references MUID:95023111; PMID:7937077 !$#accession I58311 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-513 ##label RES !'##cross-references EMBL:U09551; NID:g576448; PIDN:AAA53240.1; !1PID:g576449 GENETICS !$#gene HBP1 CLASSIFICATION #superfamily rat HMG-box containing protein 1; HMG box !1homology FEATURE !$430-505 #domain HMG box homology #label HMG1 SUMMARY #length 513 #molecular-weight 57429 #checksum 9173 SEQUENCE /// ENTRY JC6540 #type complete TITLE placenta specific-homeobox protein - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 15-Oct-1999 ACCESSIONS JC6540 REFERENCE JC6540 !$#authors Han, Y.J.; Park, A.R.; Sung, D.Y.; Chun, J.Y. !$#journal Gene (1998) 207:159-166 !$#title Psx, a novel murine homeobox gene expressed in placenta. !$#cross-references MUID:98172748; PMID:9511757 !$#accession JC6540 !'##molecule_type mRNA !'##residues 1-247 ##label HAN !'##cross-references GB:AF017453 COMMENT This protein is involved in controlling cell fate during !1embryonic development. GENETICS !$#gene Psx CLASSIFICATION #superfamily mouse placenta-specific homeobox protein; !1homeobox homology KEYWORDS DNA binding; homeobox; nucleus; placenta; transcription !1regulation FEATURE !$151-207 #domain homeobox homology #label HOX SUMMARY #length 247 #molecular-weight 28180 #checksum 5116 SEQUENCE /// ENTRY WJFFH2 #type complete TITLE homeotic protein H2.0 - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 14-Nov-1997 ACCESSIONS S00994 REFERENCE S00994 !$#authors Barad, M.; Jack, T.; Chadwick, R.; McGinnis, W. !$#journal EMBO J. (1988) 7:2151-2161 !$#title A novel, tissue-specific, Drosophila homeobox gene. !$#cross-references MUID:88329003; PMID:2901348 !$#accession S00994 !'##molecule_type mRNA !'##residues 1-419 ##label BAR !'##cross-references EMBL:Y00843 !'##note it is uncertain whether Met-1 or Met-10 is the initiator COMMENT This homeotic protein is expressed in the visceral !1musculature and its anlagen. GENETICS !$#gene FlyBase:H2.0 !'##cross-references FlyBase:FBgn0001170 !$#map_position 2L 26B1-3 CLASSIFICATION #superfamily homeotic protein H2.0; homeobox homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$189-212 #region glutamine/histidine-rich\ !$297-353 #domain homeobox homology #label HOX SUMMARY #length 419 #molecular-weight 45890 #checksum 7564 SEQUENCE /// ENTRY A41948 #type complete TITLE alpha-fetoprotein enhancer-binding protein - human ALTERNATE_NAMES ATBF1 protein ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 15-Oct-1999 ACCESSIONS A41948 REFERENCE A41948 !$#authors Morinaga, T.; Yasuda, H.; Hashimoto, T.; Higashio, K.; !1Tamaoki, T. !$#journal Mol. Cell. Biol. (1991) 11:6041-6049 !$#title A human alpha-fetoprotein enhancer-binding protein, ATBF1, !1contains four homeodomains and seventeen zinc fingers. !$#cross-references MUID:92049333; PMID:1719379 !$#accession A41948 !'##molecule_type mRNA !'##residues 1-2783 ##label MOR !'##cross-references GB:D10250; GB:D90395; NID:g219429; PIDN:BAA01095.1; !1PID:g219430 !'##note sequence extracted from NCBI backbone (NCBIN:66271, !1NCBIP:66276) GENETICS !$#gene GDB:ATBF1 !'##cross-references GDB:392090; OMIM:104155 !$#map_position 16q22.3-16q23.1 CLASSIFICATION #superfamily alpha-fetoprotein enhancer-binding protein; !1homeobox homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation; !1zinc finger FEATURE !$72-94 #region zinc finger CCHH motif\ !$128-150 #region zinc finger CCHH motif\ !$176-198 #region zinc finger CCHH motif\ !$311-332 #region zinc finger CCHH motif\ !$340-361 #region zinc finger CCHH motif\ !$448-471 #region zinc finger CCHH motif\ !$489-509 #region zinc finger CCHH motif\ !$517-538 #region zinc finger CCHH motif\ !$633-655 #region zinc finger CCHH motif\ !$684-706 #region zinc finger CCHH motif\ !$719-773 #region serine/threonine-rich\ !$809-958 #region glutamine-rich\ !$1071-1092 #region zinc finger CCHH motif\ !$1117-1211 #region proline-rich\ !$1232-1288 #domain homeobox homology #label HOX1\ !$1329-1385 #domain homeobox homology #label HOX2\ !$1416-1437 #region zinc finger CCHC motif\ !$1618-1638 #region zinc finger CCHH motif\ !$1728-1784 #domain homeobox homology #label HOX3\ !$1799-1820 #region zinc finger CCHH motif\ !$2033-2089 #domain homeobox homology #label HOX4\ !$2112-2134 #region zinc finger CCHH motif\ !$2545-2566 #region zinc finger CCHC motif\ !$2585-2607 #region glycine-rich\ !$2611-2633 #region zinc finger CCHH motif\ !$2650-2737 #region serine/threonine-rich SUMMARY #length 2783 #molecular-weight 305737 #checksum 5097 SEQUENCE /// ENTRY A47001 #type complete TITLE transcription factor Oct-1 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 29-Sep-1999 ACCESSIONS A47001; A31754 REFERENCE A47001 !$#authors Sturm, R.A.; Cassady, J.L.; Das, G.; Romo, A.; Evans, G.A. !$#journal Genomics (1993) 16:333-341 !$#title Chromosomal structure and expression of the human OTF1 locus !1encoding the oct-1 protein. !$#cross-references MUID:93300505; PMID:8314572 !$#accession A47001 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-766 ##label STU !'##note the sequence in GenBank entry HSOCT1, release 111.0, begins !1with Met-24 REFERENCE A31754 !$#authors Sturm, R.A.; Das, G.; Herr, W. !$#journal Genes Dev. (1988) 2:1582-1599 !$#title The ubiquitous octamer-binding protein Oct-1 contains a POU !1domain with a homeo box subdomain. !$#cross-references MUID:89107993; PMID:2905684 !$#accession A31754 !'##molecule_type mRNA !'##residues 'P',8-400,'R',402-766 ##label ST2 !'##cross-references GB:X13403; NID:g35126; PIDN:CAA31767.1; PID:g35127 GENETICS !$#gene GDB:POU2F1; OTF1; OCT1 !'##cross-references GDB:120254; OMIM:164175 !$#map_position 1q22-1q23 CLASSIFICATION #superfamily transcription factor Oct-1; homeobox homology; !1POU domain homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$310-377 #domain POU domain homology #label POU\ !$403-459 #domain homeobox homology #label HOX SUMMARY #length 766 #molecular-weight 78522 #checksum 4954 SEQUENCE /// ENTRY S30293 #type complete TITLE transcription factor Oct-1, splice form Oct-1A - mouse ALTERNATE_NAMES NF-A1; NFIII; OBP100; OTF-1 CONTAINS transcription factor Oct-1B ORGANISM #formal_name Mus musculus #common_name house mouse DATE 13-Jan-1995 #sequence_revision 13-Jan-1995 #text_change 22-Jun-1999 ACCESSIONS S30293; S30294; S30295; S31873; S31870; S09238; S53721; !1S53720; S22645; S26569; S26570; S26571 REFERENCE S30293 !$#authors Suzuki, N.; Peter, W.; Ciesiolka, T.; Gruss, P.; Schoeler, !1H.R. !$#journal Nucleic Acids Res. (1993) 21:245-252 !$#title Mouse Oct-1 contains a composite homeodomain of human Oct-1 !1and Oct-2. !$#cross-references MUID:93181198; PMID:8441632 !$#accession S30293 !'##status preliminary !'##molecule_type mRNA !'##residues 1-770 ##label SUZ !'##cross-references EMBL:X68362; NID:g53465; PIDN:CAA48422.1; !1PID:g53466 !$#accession S30294 !'##status preliminary !'##molecule_type mRNA !'##residues 1-498,523-770 ##label SU2 !'##cross-references EMBL:X68363; NID:g53471; PIDN:CAA48423.1; !1PID:g53472 !$#accession S30295 !'##status preliminary !'##molecule_type mRNA !'##residues 1-498,523-716,'DCFMDWRTF' ##label SU3 !'##cross-references EMBL:X68364; NID:g53473; PIDN:CAA48424.1; !1PID:g53474 !'##note splice form Oct-1C REFERENCE S31870 !$#authors Jaffe, J.; Hochberg, M.; Reich, L.; Ben-neriah, Y.; Bergman, !1Y.; Laskov, R. !$#submission submitted to the EMBL Data Library, February 1993 !$#description Expression of different isoforms of murine oct-1 gene in !1various tissues. !$#accession S31873 !'##status preliminary !'##molecule_type mRNA !'##residues 30-128,'P',130-607,'A',609-667,692-770 ##label JAF !'##cross-references EMBL:X70324; NID:g53467; PIDN:CAA49791.1; !1PID:g53468 !$#accession S31870 !'##status preliminary !'##molecule_type mRNA !'##residues 371-498,523-607,'A',609-770 ##label JA2 !'##cross-references EMBL:X70325 REFERENCE S09237 !$#authors Goldsborough, A.; Ashworth, A.; Willison, K. !$#journal Nucleic Acids Res. (1990) 18:1634 !$#title Cloning and sequencing of POU-boxes expressed in mouse !1testis. !$#cross-references MUID:90221898; PMID:1970171 !$#accession S09238 !'##molecule_type DNA !'##residues 305-367,'D',369-426 ##label GOL !'##cross-references EMBL:X51958; NID:g53475; PIDN:CAA36217.1; !1PID:g930193 REFERENCE S53720 !$#authors Jaffe, J.; Hochberg, M.; Riss, J.; Hasin, T.; Reich, L.; !1Laskov, R. !$#journal Biochim. Biophys. Acta (1995) 1261:201-209 !$#title Cloning, sequencing and expression of two isoforms of the !1murine oct-1 transcription factor. !$#cross-references MUID:95226446; PMID:7711063 !$#accession S53721 !'##status preliminary; nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 30-128,'P',130-607,'A',609-667,692-770 ##label JA3 !'##cross-references EMBL:X70324; NID:g53467; PIDN:CAA49791.1; !1PID:g53468 !$#accession S53720 !'##status preliminary; nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 370-498,523-607,'A',609-770 ##label JA4 !'##cross-references EMBL:X70325; NID:g53469; PIDN:CAA49792.1; !1PID:g53470 REFERENCE S22645 !$#authors Stepchenko, A.G. !$#journal Nucleic Acids Res. (1992) 20:1419 !$#title The nucleotide sequence of mouse OCT-1 cDNA. !$#cross-references MUID:92220620; PMID:1561098 !$#accession S22645 !'##status preliminary !'##molecule_type mRNA !'##residues 'MLDCSDCVLDSR',1-42,'L',44-53,72-498,523-607,'A',609-638 !1##label STE !'##cross-references EMBL:X56230; NID:g53476; PIDN:CAA39679.1; !1PID:g53477 GENETICS !$#gene Oct-1 !$#map_position 1 CLASSIFICATION #superfamily transcription factor Oct-1; homeobox homology; !1POU domain homology KEYWORDS alternative splicing; DNA binding; homeobox; nucleus; !1transcription regulation FEATURE !$1-770 #product transcription factor Oct-1A #status !8predicted #label OC1A\ !$1-498,523-770 #product transcription factor Oct-1B #status !8predicted #label OC1B\ !$288-355 #domain POU domain homology #label POU\ !$383-439 #domain homeobox homology #label HOX SUMMARY #length 770 #molecular-weight 79532 #checksum 3401 SEQUENCE /// ENTRY A34873 #type complete TITLE transcription factor Oct-1, octamer-binding - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A34873 REFERENCE A34873 !$#authors Petryniak, B.; Staudt, L.M.; Postema, C.E.; McCormack, W.T.; !1Thompson, C.B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:1099-1103 !$#title Characterization of chicken octamer-binding proteins !1demonstrates that POU domain-containing homeobox !1transcription factors have been highly conserved during !1vertebrate evolution. !$#cross-references MUID:90138945; PMID:1967834 !$#accession A34873 !'##status preliminary !'##molecule_type mRNA !'##residues 1-739 ##label PET !'##cross-references GB:M29972; NID:g212466; PIDN:AAA48993.1; !1PID:g212467 CLASSIFICATION #superfamily transcription factor Oct-1; homeobox homology; !1POU domain homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$281-348 #domain POU domain homology #label POU\ !$376-432 #domain homeobox homology #label HOX SUMMARY #length 739 #molecular-weight 75981 #checksum 2743 SEQUENCE /// ENTRY S07896 #type complete TITLE transcription factor Oct-1.32 - African clawed frog ALTERNATE_NAMES maternal transcription factor; pou homeobox protein oct-1.32 ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 15-Oct-1999 ACCESSIONS S07896; S40642; S08673; S14554; S12186 REFERENCE S07896 !$#authors Smith, D.P.; Old, R.W. !$#journal Nucleic Acids Res. (1990) 18:369 !$#title Nucleotide sequence of Xenopus laevis Oct-1 cDNA. !$#cross-references MUID:90221827; PMID:2326173 !$#accession S07896 !'##molecule_type mRNA !'##residues 1-760 ##label SMI !'##cross-references EMBL:X17190; NID:g64942; PIDN:CAA35051.1; !1PID:g671665 REFERENCE S40642 !$#authors Smith, D.P.; Old, R.W. !$#journal Nucleic Acids Res. (1991) 19:815-821 !$#title Xenopus laevis Oct-1 does not bind to certain histone H2B !1gene promoter octamer motifs for which a novel !1octamer-binding factor has high affinity. !$#cross-references MUID:91204435; PMID:2017364 !$#accession S40642 !'##status preliminary !'##molecule_type mRNA !'##residues 1-7,'L',9-760 ##label SM2 REFERENCE S08673 !$#authors Schilthuis, J.G.; Baarends, W.M.; Peterson-Maduro, J.; !1Destre, O.H.J. !$#submission submitted to the EMBL Data Library, February 1990 !$#accession S08673 !'##molecule_type DNA !'##residues 'LVCCSFLLIQYSV',261-335 ##label SCH !'##cross-references EMBL:X51819; NID:g65249; PIDN:CAA36119.1; !1PID:g295726 REFERENCE S14554 !$#authors Hinkley, C.; Leibham, D.; Perry, M. !$#submission submitted to the EMBL Data Library, January 1991 !$#description Regulated binding specificity of Xenopus OCT-1, a maternal !1transcription factor. !$#accession S14554 !'##status preliminary !'##molecule_type mRNA !'##residues 1-156,'S',158-367,370-760 ##label HIN !'##cross-references EMBL:X57165; NID:g64951; PIDN:CAA40454.1; !1PID:g64952 REFERENCE S12179 !$#authors Baltzinger, M.; Stiegler, P.; Remy, P. !$#journal Nucleic Acids Res. (1990) 18:6131 !$#title Cloning and sequencing of POU-boxes expressed in Xenopus !1laevis neurula embryos. !$#cross-references MUID:91045083; PMID:2235499 !$#accession S12186 !'##molecule_type mRNA !'##residues 320-435 ##label BAL !'##cross-references EMBL:X54683; NID:g64947; PIDN:CAA38497.1; !1PID:g930281 GENETICS !$#gene Oct-1 !$#introns 320/3 CLASSIFICATION #superfamily transcription factor Oct-1; homeobox homology; !1POU domain homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$301-368 #domain POU domain homology #label POU\ !$398-454 #domain homeobox homology #label HOX SUMMARY #length 760 #molecular-weight 79096 #checksum 3237 SEQUENCE /// ENTRY S47575 #type complete TITLE EGD1 protein - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein P7102.13c; protein YPL037c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Dec-1999 ACCESSIONS S47575; S62038; A45037; S31295 REFERENCE S47574 !$#authors Hu, G.Z.; Ronne, H. !$#journal Nucleic Acids Res. (1994) 22:2740-2743 !$#title Yeast BTF3 protein is encoded by duplicated genes and !1inhibits the expression of some genes in vivo. !$#cross-references MUID:94329431; PMID:8052529 !$#accession S47575 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-157 ##label HUG !'##cross-references EMBL:X78725; NID:g547459; PIDN:CAA55371.1; !1PID:g547460 REFERENCE S62026 !$#authors Dietrich, F.S.; Allen, E.; Araujo, R.; Aparicio, A.; !1Carpenter, J.; Cherry, J.M.; Chung, E.; Davis, K.; Duncan, !1M.; Hunicke-Smith, S.; Hyman, R.; Kalman, S.; Komp, C.; !1Kurdi, O.; Lashkari, D.; Lew, H.; Lin, A.; Lin, D.; Marathe, !1R.; Mirtipati, S.; Namath, A.; Oefner, P.; Petel, F.X.; !1Roberts, D.; Schramm, S.; Schroeder, M.; Botstein, D.; !1Davis, R.W. !$#submission submitted to the EMBL Data Library, December 1995 !$#accession S62038 !'##molecule_type DNA !'##residues 1-157 ##label DIE !'##cross-references EMBL:U44030; NID:g1171408; PIDN:AAB68183.1; !1PID:g1171421; GSPDB:GN00016; MIPS:YPL037c REFERENCE A45037 !$#authors Parthun, M.R.; Mangus, D.A.; Jaehning, J.A. !$#journal Mol. Cell. Biol. (1992) 12:5683-5689 !$#title The EGD1 product, a yeast homolog of human BTF3, may be !1involved in GAL4 DNA binding. !$#cross-references MUID:93078770; PMID:1448098 !$#accession A45037 !'##molecule_type DNA !'##residues 1-79,'KLLV',86-87,'TLL',91,'STVYHRKRTCKICSQVLS',110, !1'NWALKPSKPCLNWL',112,'KWKSTKPR',121,'QLMLKRRMKLFQS' ##label !1PAR !'##cross-references EMBL:S49596; NID:g260583; PIDN:AAB24290.1; !1PID:g260584 GENETICS !$#gene SGD:EGD1; MIPS:YPL037c !'##cross-references SGD:S0005958; MIPS:YPL037c !$#map_position 16L CLASSIFICATION #superfamily transcription factor BTF3 SUMMARY #length 157 #molecular-weight 17020 #checksum 8212 SEQUENCE /// ENTRY A31753 #type complete TITLE transcription factor Oct-2 - human ALTERNATE_NAMES NF-A2; OTF-2 ORGANISM #formal_name Homo sapiens #common_name man DATE 07-Jun-1990 #sequence_revision 26-Apr-1996 #text_change 21-Jul-2000 ACCESSIONS A31753; C31753; S06452; A31213; S47513; S06453; S50016; !1S12535 REFERENCE A91621 !$#authors Clerc, R.G.; Corcoran, L.M.; LeBowitz, J.H.; Baltimore, D.; !1Sharp, P.A. !$#journal Genes Dev. (1988) 2:1570-1581 !$#title The B-cell-specific Oct-2 protein contains POU box- and !1homeo box-type domains. !$#cross-references MUID:89107992; PMID:3265124 !$#accession A31753 !'##molecule_type mRNA !'##residues 1-467 ##label CLE !'##cross-references EMBL:X53468; NID:g35128; PIDN:CAA37562.1; !1PID:g35129; EMBL:Y00227 !$#accession C31753 !'##molecule_type mRNA !'##residues 450-479 ##label CL2 !'##cross-references EMBL:X53469; NID:g35131; PIDN:CAA37565.1; !1PID:g35132; EMBL:Y00227 REFERENCE S06452 !$#authors Mueller, M.M.; Ruppert, S.; Schaffner, W.; Matthias, P. !$#journal Nature (1988) 336:544-551 !$#title A cloned octamer transcription factor stimulates !1transcription from lymphoid-specific promoters in non-B !1cells. !$#cross-references MUID:89070674; PMID:2904653 !$#accession S06452 !'##status preliminary !'##molecule_type mRNA !'##residues 2-479 ##label MUE !'##cross-references EMBL:X13809 !'##note it is uncertain whether Met-6 or Met-13 is the initiator or !1whether translation is initiated 5' to the sequenced region REFERENCE A31213 !$#authors Ko, H.S.; Fast, P.; McBride, W.; Staudt, L.M. !$#journal Cell (1988) 55:135-144 !$#title A human protein specific for the immunoglobulin octamer DNA !1motif contains a functional homeobox domain. !$#cross-references MUID:89003042; PMID:2901913 !$#accession A31213 !'##molecule_type mRNA !'##residues 255-402 ##label KOH !'##cross-references GB:M22596; NID:g727159; PIDN:AAA64232.1; !1PID:g727160 REFERENCE S47215 !$#authors Matsuo, K.; Clay, O.; Kuenzler, P.; Georgiev, O.; Urbanek, !1P.; Schaffner, W. !$#submission submitted to the EMBL Data Library, August 1994 !$#accession S47513 !'##status preliminary !'##molecule_type DNA !'##residues 168-377 ##label MAT !'##cross-references EMBL:X81030 REFERENCE S06453 !$#authors Scheidereit, C.; Cromlish, J.A.; Gerster, T.; Kawakami, K.; !1Balmaceda, C.G.; Currie, R.A.; Roeder, R.G. !$#journal Nature (1988) 336:551-557 !$#title A human lymphoid-specific transcription factor that !1activates immunoglobulin genes is a homoeobox protein. !$#cross-references MUID:89070675; PMID:2904654 !$#accession S06453 !'##status preliminary !'##molecule_type mRNA !'##residues 1-167,184-479 ##label SCH !'##cross-references EMBL:X13810; NID:g35166; PIDN:CAA32040.1; !1PID:g35167 REFERENCE S50016 !$#authors Matsuo, K.; Clay, O.; Kuenzler, P.; Georgiev, O.; Urbanek, !1P.; Schaffner, W. !$#journal Biol. Chem. Hoppe-Seyler (1994) 375:675-683 !$#title Short introns interrupting the Oct-2 POU domain may prevent !1recombination between POU family genes without interfering !1with potential POU domain 'shuffling' in evolution. !$#cross-references MUID:95194574; PMID:7888080 !$#accession S50016 !'##status preliminary; translation not shown !'##molecule_type DNA !'##residues 168-377 ##label MA2 !'##cross-references EMBL:X81030; NID:g532054; PIDN:CAA56933.1; !1PID:g4379032 REFERENCE S12535 !$#authors Mueller-Immerglueck, M.M.; Schaffner, W.; Matthias, P. !$#journal EMBO J. (1990) 9:1625-1634 !$#title Transcription factor Oct-2A contains functionally redundant !1activating domains and works selectively from a promoter but !1not from a remote enhancer position in non-lymphoid (HeLa) !1cells. !$#cross-references MUID:90228363; PMID:2328728 !$#accession S12535 !'##status preliminary !'##molecule_type mRNA !'##residues 99-161 ##label MU2 COMMENT This protein is a tissue-specific transcriptional !1trans-activator. In humans it is found mainly in B-cells !1where it is involved in the regulation of immunoglobulin !1gene transcription. GENETICS !$#gene GDB:POU2F2; OCT2; OTF2 !'##cross-references GDB:120255; OMIM:164176 !$#map_position 19pter-19qter !$#introns 221/3; 269/1; 318/3 CLASSIFICATION #superfamily transcription factor Oct-2; homeobox homology; !1POU domain homology KEYWORDS alternative splicing; B-cell; DNA binding; homeobox; !1nucleus; transcription regulation FEATURE !$202-269 #domain POU domain homology #label POU\ !$298-354 #domain homeobox homology #label HOX SUMMARY #length 479 #molecular-weight 51209 #checksum 958 SEQUENCE /// ENTRY S22543 #type complete TITLE transcription factor Oct-2 splice form Oct-2.3 - mouse ALTERNATE_NAMES NF-A2 protein; OTF-2 protein CONTAINS transcription factor Oct-2 splice form Oct-2.1; transcription factor Oct-2 splice form Oct-2.6; transcription factor Oct-2 splice form Oct-2c ORGANISM #formal_name Mus musculus #common_name house mouse DATE 22-Nov-1993 #sequence_revision 10-Nov-1995 #text_change 15-Oct-1999 ACCESSIONS S22543; S22541; S22540; JH0596; I48698; S47215 REFERENCE S22539 !$#authors Wirth, T.; Priess, A.; Annweiler, A.; Zwilling, S.; Oeler, !1B. !$#journal Nucleic Acids Res. (1991) 19:43-51 !$#title Multiple Oct2 isoforms are generated by alternative !1splicing. !$#cross-references MUID:91187647; PMID:2011512 !$#accession S22543 !'##status preliminary !'##molecule_type mRNA !'##residues 1-485 ##label WIR !'##cross-references EMBL:X57938; NID:g53485; PIDN:CAA41006.1; !1PID:g53486 !'##note splice form Oct-2.3 !$#accession S22541 !'##status preliminary !'##molecule_type mRNA !'##residues 1-62,85-485 ##label WI3 !'##cross-references EMBL:X57936; NID:g53481; PIDN:CAA41004.1; !1PID:g53482 !'##note splice form Oct-2.1 !$#accession S22540 !'##status preliminary !'##molecule_type mRNA !'##residues 1-62,124-485 ##label WI4 !'##cross-references EMBL:X57941; NID:g53491; PIDN:CAA41009.1; !1PID:g53492 !'##note splice form Oct-2.6 REFERENCE JH0596 !$#authors Stoykova, A.S.; Sterrer, S.; Erselius, J.R.; Hatzopoulos, !1A.K.; Gruss, P. !$#journal Neuron (1992) 8:541-558 !$#title Mini-Oct and Oct-2c: two novel, functionally diverse murine !1Oct-2 gene products are differentially expressed in the CNS. !$#cross-references MUID:92198662; PMID:1550677 !$#accession JH0596 !'##molecule_type mRNA !'##residues 1-62,85-430,'A',432,'P',434-473 ##label STO !'##experimental_source brain !'##note splice form Oct-2c REFERENCE I48698 !$#authors Stepchenko, A.G. !$#journal Dokl. Akad. Nauk SSSR (1992) 325:175-178 !$#title [Interaction of Oct-binding transcription factors with a !1large series of 'noncanonical' oct-sequences. Primary !1sequence of murine Oct-2B cDNA]. !$#accession I48698 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 'PHP',189-430,'A',432,'P',434-464,'W',466-485 ##label RES !'##cross-references EMBL:X57089; NID:g53493; PIDN:CAA40369.1; !1PID:g53494 COMMENT This protein is a tissue-specific transcriptional !1trans-activator. GENETICS !$#gene Oct-2 !$#map_position 7 CLASSIFICATION #superfamily transcription factor Oct-2; homeobox homology; !1POU domain homology KEYWORDS alternative splicing; DNA binding; homeobox; nucleus; !1transcription regulation FEATURE !$208-275 #domain POU domain homology #label POU\ !$304-360 #domain homeobox homology #label HOX SUMMARY #length 485 #molecular-weight 51798 #checksum 9495 SEQUENCE /// ENTRY S22542 #type complete TITLE transcription factor Oct-2, splice form Oct-2.2 - mouse ALTERNATE_NAMES NF-A2; OTF-2 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 22-Nov-1993 #sequence_revision 10-Nov-1995 #text_change 22-Jun-1999 ACCESSIONS S22542; S50017; S47215 REFERENCE S22539 !$#authors Wirth, T.; Priess, A.; Annweiler, A.; Zwilling, S.; Oeler, !1B. !$#journal Nucleic Acids Res. (1991) 19:43-51 !$#title Multiple Oct2 isoforms are generated by alternative !1splicing. !$#cross-references MUID:91187647; PMID:2011512 !$#accession S22542 !'##status preliminary !'##molecule_type mRNA !'##residues 1-479 ##label WIR !'##cross-references EMBL:X57937; NID:g53483; PIDN:CAA41005.1; !1PID:g53484 REFERENCE S50016 !$#authors Matsuo, K.; Clay, O.; Kuenzler, P.; Georgiev, O.; Urbanek, !1P.; Schaffner, W. !$#journal Biol. Chem. Hoppe-Seyler (1994) 375:675-683 !$#title Short introns interrupting the Oct-2 POU domain may prevent !1recombination between POU family genes without interfering !1with potential POU domain 'shuffling' in evolution. !$#cross-references MUID:95194574; PMID:7888080 !$#accession S50017 !'##status translation not shown !'##molecule_type DNA !'##residues 168-377 ##label MAT !'##cross-references EMBL:X81031; NID:g534039; PIDN:CAA56934.1; !1PID:g536781 COMMENT This protein is a tissue-specific transcriptional !1trans-activator. GENETICS !$#gene Oct-2 !$#map_position 7 !$#introns 221/3; 269/1; 318/3 CLASSIFICATION #superfamily transcription factor Oct-2; homeobox homology; !1POU domain homology KEYWORDS alternative splicing; DNA binding; homeobox; nucleus; !1transcription regulation FEATURE !$202-269 #domain POU domain homology #label POU\ !$298-354 #domain homeobox homology #label HOX SUMMARY #length 479 #molecular-weight 51320 #checksum 108 SEQUENCE /// ENTRY S22539 #type complete TITLE transcription factor Oct-2, splice form Oct-2.4 - mouse ALTERNATE_NAMES NF-A2; OTF-2 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 22-Nov-1993 #sequence_revision 10-Nov-1995 #text_change 22-Jun-1999 ACCESSIONS S22539 REFERENCE S22539 !$#authors Wirth, T.; Priess, A.; Annweiler, A.; Zwilling, S.; Oeler, !1B. !$#journal Nucleic Acids Res. (1991) 19:43-51 !$#title Multiple Oct2 isoforms are generated by alternative !1splicing. !$#cross-references MUID:91187647; PMID:2011512 !$#accession S22539 !'##status preliminary !'##molecule_type mRNA !'##residues 1-400 ##label WIR !'##cross-references EMBL:X57939; NID:g53487; PIDN:CAA41007.1; !1PID:g53488 COMMENT This protein is a tissue-specific transcriptional !1trans-activator. GENETICS !$#gene Oct-2 !$#map_position 7 CLASSIFICATION #superfamily transcription factor Oct-2; homeobox homology; !1POU domain homology KEYWORDS alternative splicing; DNA binding; homeobox; nucleus; !1transcription regulation FEATURE !$186-253 #domain POU domain homology #label POU\ !$282-338 #domain homeobox homology #label HOX SUMMARY #length 400 #molecular-weight 43648 #checksum 8739 SEQUENCE /// ENTRY JH0597 #type complete TITLE transcription factor Oct-2, splice form Oct-2d - mouse ALTERNATE_NAMES NF-A2; OTF-2 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 17-Jul-1992 #sequence_revision 17-Jul-1992 #text_change 24-Oct-1997 ACCESSIONS JH0597 REFERENCE JH0596 !$#authors Stoykova, A.S.; Sterrer, S.; Erselius, J.R.; Hatzopoulos, !1A.K.; Gruss, P. !$#journal Neuron (1992) 8:541-558 !$#title Mini-Oct and Oct-2c: two novel, functionally diverse murine !1Oct-2 gene products are differentially expressed in the CNS. !$#cross-references MUID:92198662; PMID:1550677 !$#accession JH0597 !'##molecule_type mRNA !'##residues 1-232 ##label STO !'##experimental_source brain COMMENT This protein is a tissue-specific transcriptional !1trans-activator. GENETICS !$#gene Oct-2 CLASSIFICATION #superfamily transcription factor Oct-2; homeobox homology; !1POU domain homology KEYWORDS alternative splicing; DNA binding; homeobox; nucleus; !1transcription regulation FEATURE !$34-101 #domain POU domain homology #label POU\ !$130-186 #domain homeobox homology #label HOX SUMMARY #length 232 #molecular-weight 25851 #checksum 5808 SEQUENCE /// ENTRY S22544 #type complete TITLE transcription factor Oct-2, splice form Oct-2.5 - mouse ALTERNATE_NAMES NF-A2; OTF-2; transcription factor Oct-2b ORGANISM #formal_name Mus musculus #common_name house mouse DATE 03-Feb-1994 #sequence_revision 03-Feb-1994 #text_change 22-Jun-1999 ACCESSIONS S22544; A60085; S09240 REFERENCE S22539 !$#authors Wirth, T.; Priess, A.; Annweiler, A.; Zwilling, S.; Oeler, !1B. !$#journal Nucleic Acids Res. (1991) 19:43-51 !$#title Multiple Oct2 isoforms are generated by alternative !1splicing. !$#cross-references MUID:91187647; PMID:2011512 !$#accession S22544 !'##molecule_type mRNA !'##residues 1-583 ##label WIR !'##cross-references EMBL:X57940; NID:g53489; PIDN:CAA41008.1; !1PID:g53490 REFERENCE A60085 !$#authors Hatzopoulos, A.K.; Stoykova, A.S.; Erselius, J.R.; Goulding, !1M.; Neuman, T.; Gruss, P. !$#journal Development (1990) 109:349-362 !$#title Structure and expression of the mouse Oct2a and Oct2b, two !1differentially spliced products of the same gene. !$#cross-references MUID:90382251; PMID:1976089 !$#accession A60085 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-408,'A',410,'P',412-583 ##label HAT !'##cross-references EMBL:X53654; NID:g288173; PIDN:CAA37702.1; !1PID:g288174 REFERENCE S09237 !$#authors Goldsborough, A.; Ashworth, A.; Willison, K. !$#journal Nucleic Acids Res. (1990) 18:1634 !$#title Cloning and sequencing of POU-boxes expressed in mouse !1testis. !$#cross-references MUID:90221898; PMID:1970171 !$#accession S09240 !'##molecule_type DNA !'##residues 203-325 ##label GOL !'##cross-references EMBL:X51961; NID:g53495; PIDN:CAA36220.1; !1PID:g930194 COMMENT This protein is a tissue-specific transcriptional !1trans-activator. GENETICS !$#gene Oct-2 !$#map_position 7 CLASSIFICATION #superfamily transcription factor Oct-2; homeobox homology; !1POU domain homology KEYWORDS alternative splicing; DNA binding; homeobox; nucleus; !1transcription regulation FEATURE !$186-253 #domain POU domain homology #label POU\ !$282-338 #domain homeobox homology #label HOX SUMMARY #length 583 #molecular-weight 60241 #checksum 2410 SEQUENCE /// ENTRY I47154 #type complete TITLE transcription factor Oct-2 - pig ALTERNATE_NAMES NF-A2; OTF-2 ORGANISM #formal_name Sus scrofa domestica #common_name domestic pig DATE 21-Feb-1997 #sequence_revision 21-Feb-1997 #text_change 22-Jun-1999 ACCESSIONS I47154 REFERENCE I47154 !$#authors Tuggle, C.K.; Helm, J.; Rothschild, M.F. !$#journal Anim. Genet. (1994) 25:141-145 !$#title Cloning, sequencing and restriction fragment length !1polymorphism analysis of a porcine cDNA for OCT2. !$#cross-references MUID:95030552; PMID:7943947 !$#accession I47154 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-478 ##label TUG !'##cross-references EMBL:U00794; NID:g451313; PIDN:AAA80148.1; !1PID:g451314 COMMENT This protein is a tissue-specific transcriptional !1trans-activator. GENETICS !$#gene OCT2 CLASSIFICATION #superfamily transcription factor Oct-2; homeobox homology; !1POU domain homology KEYWORDS alternative splicing; DNA binding; homeobox; nucleus; !1transcription regulation FEATURE !$202-269 #domain POU domain homology #label POU\ !$298-354 #domain homeobox homology #label HOX SUMMARY #length 478 #molecular-weight 51098 #checksum 8833 SEQUENCE /// ENTRY JC2002 #type complete TITLE transcription factor Oct-11, long splice form - mouse ALTERNATE_NAMES Epoc-1 protein; POU domain protein Oct-11; POU-domain transcription factor ORGANISM #formal_name Mus musculus #common_name house mouse DATE 14-Jul-1994 #sequence_revision 14-Jul-1994 #text_change 22-Jun-1999 ACCESSIONS JC2002; S09239 REFERENCE JC2002 !$#authors Yukawa, K.; Yasui, T.; Yamamoto, A.; Shiku, H.; Kishimoto, !1T.; Kikutani, H. !$#journal Gene (1993) 133:163-169 !$#title Epoc-1: A POU-domain gene expressed in murine epidermal !1basal cells and thymic stromal cells. !$#cross-references MUID:94040806; PMID:8224904 !$#accession JC2002 !'##molecule_type mRNA !'##residues 1-431 ##label YUK !'##cross-references GB:L14677; NID:g388913; PIDN:AAA16855.1; !1PID:g388914 REFERENCE S09237 !$#authors Goldsborough, A.; Ashworth, A.; Willison, K. !$#journal Nucleic Acids Res. (1990) 18:1634 !$#title Cloning and sequencing of POU-boxes expressed in mouse !1testis. !$#cross-references MUID:90221898; PMID:1970171 !$#accession S09239 !'##molecule_type DNA !'##residues 200-318 ##label GOL !'##cross-references EMBL:X51960; NID:g53464; PIDN:CAA36219.1; !1PID:g930192 COMMENT This protein is a developmental regulator that controls !1organ development and cell phenotype. GENETICS !$#gene Oct-11 CLASSIFICATION #superfamily transcription factor Oct-2; homeobox homology; !1POU domain homology KEYWORDS alternative splicing; DNA binding; homeobox; nucleus; !1transcription regulation FEATURE !$183-250 #domain POU domain homology #label POU\ !$275-331 #domain homeobox homology #label HOX SUMMARY #length 431 #molecular-weight 47045 #checksum 5374 SEQUENCE /// ENTRY S35541 #type complete TITLE transcription factor Oct-11, short splice form - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 09-Dec-1993 #sequence_revision 01-Sep-1995 #text_change 22-Jun-1999 ACCESSIONS S35541 REFERENCE S35541 !$#authors Goldsborough, A.S.; Healy, L.E.; Copeland, N.G.; Gilbert, !1D.J.; Jenkins, N.A.; Willison, K.R.; Ashworth, A. !$#journal Nucleic Acids Res. (1993) 21:127-134 !$#title Cloning, chromosomal localization and expression pattern of !1the POU domain gene Oct-11. !$#cross-references MUID:93181164; PMID:8441607 !$#accession S35541 !'##status preliminary !'##molecule_type mRNA !'##residues 1-403 ##label GOL !'##cross-references EMBL:Z18537; NID:g53514; PIDN:CAA79222.1; !1PID:g53515 CLASSIFICATION #superfamily transcription factor Oct-2; homeobox homology; !1POU domain homology KEYWORDS alternative splicing; DNA binding; homeobox; nucleus; !1transcription regulation FEATURE !$183-250 #domain POU domain homology #label POU\ !$275-331 #domain homeobox homology #label HOX SUMMARY #length 403 #molecular-weight 43886 #checksum 4803 SEQUENCE /// ENTRY A46216 #type complete TITLE transcription factor Skn-1, splice form a - rat ALTERNATE_NAMES Skn-1a ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 19-Nov-1993 #sequence_revision 18-Nov-1994 #text_change 05-Dec-1997 ACCESSIONS A46216 REFERENCE A46216 !$#authors Andersen, B.; Schonemann, M.D.; Flynn, S.E.; Pearse II, !1R.V.; Singh, H.; Rosenfeld, M.G. !$#journal Science (1993) 260:78-82 !$#title Skn-1a and Skn-1i: two functionally distinct Oct-2-related !1factors expressed in epidermis. !$#cross-references MUID:93219836; PMID:7682011 !$#accession A46216 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-430 ##label AND !'##cross-references GB:L23862; NID:g393220 !'##note sequence extracted from NCBI backbone (NCBIP:128572) CLASSIFICATION #superfamily transcription factor Oct-2; homeobox homology; !1POU domain homology KEYWORDS alternative splicing; DNA binding; homeobox; nucleus; !1transcription regulation FEATURE !$183-250 #domain POU domain homology #label POU\ !$275-331 #domain homeobox homology #label HOX SUMMARY #length 430 #molecular-weight 46775 #checksum 9929 SEQUENCE /// ENTRY B46216 #type complete TITLE transcription factor Skn-1, splice form i - rat ALTERNATE_NAMES Skn-1i ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 19-Nov-1993 #sequence_revision 18-Nov-1994 #text_change 05-Feb-1999 ACCESSIONS B46216 REFERENCE A46216 !$#authors Andersen, B.; Schonemann, M.D.; Flynn, S.E.; Pearse II, !1R.V.; Singh, H.; Rosenfeld, M.G. !$#journal Science (1993) 260:78-82 !$#title Skn-1a and Skn-1i: two functionally distinct Oct-2-related !1factors expressed in epidermis. !$#cross-references MUID:93219836; PMID:7682011 !$#accession B46216 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-348 ##label AND !'##cross-references GB:L23863; NID:g393221 !'##note sequence extracted from NCBI backbone (NCBIP:128574) CLASSIFICATION #superfamily transcription factor Oct-2; homeobox homology; !1POU domain homology KEYWORDS alternative splicing; DNA binding; homeobox; nucleus; !1transcription regulation FEATURE !$101-168 #domain POU domain homology #label POU\ !$193-249 #domain homeobox homology #label HOX SUMMARY #length 348 #molecular-weight 37990 #checksum 5977 SEQUENCE /// ENTRY S31223 #type complete TITLE transcription factor Brn-1 - mouse ALTERNATE_NAMES class III POU domain protein brain-1 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 02-Dec-1993 #sequence_revision 01-Sep-1995 #text_change 22-Jun-1999 ACCESSIONS S31223 REFERENCE S31223 !$#authors Hara, Y.; Rovescalli, A.C.; Kim, Y.; Nirenberg, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:3280-3284 !$#title Structure and evolution of four POU domain genes expressed !1in mouse brain. !$#cross-references MUID:92228768; PMID:1565620 !$#accession S31223 !'##status preliminary !'##molecule_type DNA !'##residues 1-495 ##label HAR !'##cross-references EMBL:M88299; NID:g200444; PIDN:AAA39960.1; !1PID:g200445 CLASSIFICATION #superfamily transcription factor Brn-1; homeobox homology; !1POU domain homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$27-49 #region glycine-rich\ !$101-112 #region alanine-rich\ !$162-180 #region histidine/proline-rich\ !$186-201 #region alanine-rich\ !$236-247 #region glycine-rich\ !$267-291 #region histidine/proline-rich\ !$316-383 #domain POU domain homology #label POU\ !$402-458 #domain homeobox homology #label HOX SUMMARY #length 495 #molecular-weight 50012 #checksum 6953 SEQUENCE /// ENTRY JH0710 #type complete TITLE transcription factor Brn-1 - zebra fish ALTERNATE_NAMES ZFPOU 1 protein ORGANISM #formal_name Brachydanio rerio #common_name zebra fish DATE 17-Apr-1993 #sequence_revision 17-Apr-1993 #text_change 16-Jun-2000 ACCESSIONS JH0710 REFERENCE JH0710 !$#authors Matsuzaki, T.; Amanuma, H.; Takeda, H. !$#journal Biochem. Biophys. Res. Commun. (1992) 187:1446-1453 !$#title A pou-domain gene of zebrafish, ZFPOU1, specifically !1expressed in the developing neural tissues. !$#cross-references MUID:93038620; PMID:1417821 !$#accession JH0710 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-425 ##label MAT !'##cross-references DDBJ:D13045; NID:g222975; PIDN:BAA02377.1; !1PID:g222976 CLASSIFICATION #superfamily transcription factor Brn-1; homeobox homology; !1POU domain homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$12-26 #region serine-rich\ !$84-98 #region alanine-rich\ !$165-169 #region glutamine-rich\ !$208-227 #region glutamine/histidine-rich\ !$245-312 #domain POU domain homology #label POU\ !$331-387 #domain homeobox homology #label HOX SUMMARY #length 425 #molecular-weight 45626 #checksum 2056 SEQUENCE /// ENTRY S29334 #type complete TITLE transcription factor Brn-2 [validated] - human ALTERNATE_NAMES class III POU domain protein brain-2; transcription factor Oct-3 CONTAINS transcription factor Brn-2; transcription factor Oct-5a; transcription factor Oct-5b ORGANISM #formal_name Homo sapiens #common_name man DATE 13-Jan-1995 #sequence_revision 13-Jan-1995 #text_change 08-Dec-2000 ACCESSIONS S29334; S05043; S30296 REFERENCE S29334 !$#authors Schreiber, E.; Tobler, A.; Malipiero, U.; Fontana, A. !$#submission submitted to the EMBL Data Library, April 1992 !$#description The human N-Oct 3 cDNA encodes three neuroectodermal cell !1lineage restricted POU proteins with converse transcription !1activation functions. !$#accession S29334 !'##molecule_type mRNA !'##residues 1-443 ##label SCH !'##cross-references EMBL:Z11933; NID:g35084; PIDN:CAA77990.1; !1PID:g35085 !'##experimental_source tissue-type brain REFERENCE S05042 !$#authors He, X.; Treacy, M.N.; Simmons, D.M.; Ingraham, H.A.; !1Swanson, L.W.; Rosenfeld, M.G. !$#journal Nature (1989) 340:35-42 !$#title Expression of a large family of POU-domain regulatory genes !1in mammalian brain development. !$#cross-references MUID:89295573; PMID:2739723 !$#accession S05043 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 280-350;351-404 ##label HEX !'##cross-references GB:Z11933; NID:g35084 REFERENCE S30296 !$#authors Schreiber, E.; Tobler, A.; Malipiero, U.; Schaffner, W.; !1Fontana, A. !$#journal Nucleic Acids Res. (1993) 21:253-258 !$#title cDNA cloning of human N-Oct 3, a nervous-system specific POU !1domain transcription factor binding to the octamer DNA !1motif. !$#cross-references MUID:93181199; PMID:8441633 !$#accession S30296 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-25,'G',27-443 ##label SCW !'##cross-references EMBL:Z11933 !'##experimental_source tissue-type brain GENETICS !$#gene GDB:POU3F2; OTF7 !'##cross-references GDB:222816; OMIM:600494 !$#map_position 6q16-6q16 CLASSIFICATION #superfamily transcription factor Brn-1; homeobox homology; !1POU domain homology KEYWORDS alternative initiators; DNA binding; homeobox; nucleus; !1transcription regulation FEATURE !$1-443 #product transcription factor Brn-2 #status !8experimental #label MAT1\ !$68-90 #region glycine-rich\ !$125-149 #region glutamine-rich\ !$151-165 #region histidine/proline-rich\ !$181-443 #product transcription factor Oct-5a #status !8experimental #label MAT2\ !$200-443 #product transcription factor Oct-5b #status !8experimental #label MAT3\ !$211-259 #region histidine/proline-rich\ !$269-336 #domain POU domain homology #label POU\ !$355-411 #domain homeobox homology #label HOX SUMMARY #length 443 #molecular-weight 46921 #checksum 5058 SEQUENCE /// ENTRY S31224 #type complete TITLE transcription factor Brn-2 - mouse ALTERNATE_NAMES class III POU domain protein brain-2 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 02-Dec-1993 #sequence_revision 01-Sep-1995 #text_change 22-Jun-1999 ACCESSIONS S31224 REFERENCE S31223 !$#authors Hara, Y.; Rovescalli, A.C.; Kim, Y.; Nirenberg, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:3280-3284 !$#title Structure and evolution of four POU domain genes expressed !1in mouse brain. !$#cross-references MUID:92228768; PMID:1565620 !$#accession S31224 !'##status preliminary !'##molecule_type DNA !'##residues 1-445 ##label HAR !'##cross-references EMBL:M88300; NID:g200446; PIDN:AAA39961.1; !1PID:g200447 CLASSIFICATION #superfamily transcription factor Brn-1; homeobox homology; !1POU domain homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$68-90 #region glycine-rich\ !$125-151 #region glutamine-rich\ !$153-165 #region histidine/proline-rich\ !$213-261 #region histidine/proline-rich\ !$271-338 #domain POU domain homology #label POU\ !$357-413 #domain homeobox homology #label HOX SUMMARY #length 445 #molecular-weight 47149 #checksum 1755 SEQUENCE /// ENTRY A49447 #type complete TITLE transcription factor Brn-2 - rat ALTERNATE_NAMES class III POU domain protein brain-2 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 07-Apr-1994 #sequence_revision 18-Nov-1994 #text_change 20-Feb-1998 ACCESSIONS A49447 REFERENCE A49447 !$#authors Li, P.; He, X.; Gerrero, M.R.; Mok, M.; Aggarwal, A.; !1Rosenfeld, M.G. !$#journal Genes Dev. (1993) 7:2483-2496 !$#title Spacing and orientation of bipartite DNA-binding motifs as !1potential functional determinants for POU domain factors. !$#cross-references MUID:94102531; PMID:8276233 !$#accession A49447 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-445 ##label LI1 !'##cross-references GB:L27663; NID:g443687 !'##experimental_source brain !'##note sequence extracted from NCBI backbone (NCBIP:141696) CLASSIFICATION #superfamily transcription factor Brn-1; homeobox homology; !1POU domain homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$68-90 #region glycine-rich\ !$125-151 #region glutamine-rich\ !$153-165 #region histidine/proline-rich\ !$213-261 #region histidine/proline-rich\ !$271-338 #domain POU domain homology #label POU\ !$357-413 #domain homeobox homology #label HOX SUMMARY #length 445 #molecular-weight 47165 #checksum 1923 SEQUENCE /// ENTRY S22652 #type complete TITLE transcription factor Brn-2 - African clawed frog ALTERNATE_NAMES class III POU domain protein brain-2; transcription factor POU3 ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 22-Nov-1993 #sequence_revision 10-Nov-1995 #text_change 22-Jun-1999 ACCESSIONS S22652 REFERENCE S22652 !$#authors Baltzinger, M.; Payen, E.; Remy, P. !$#journal Nucleic Acids Res. (1992) 20:1993 !$#title Nucleotide sequence of XLPOU3 cDNA, a member of the POU !1domain gene family expressed in Xenopus laevis embryos. !$#cross-references MUID:92253425; PMID:1579504 !$#accession S22652 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type mRNA !'##residues 1-382 ##label BAL !'##cross-references EMBL:X64835; NID:g65020; PIDN:CAA46047.1; !1PID:g65021 !'##note this sequence was submitted to the EMBL Data Library, March !11991 CLASSIFICATION #superfamily transcription factor Brn-1; homeobox homology; !1POU domain homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$103-115 #region histidine/proline-rich\ !$208-275 #domain POU domain homology #label POU\ !$294-350 #domain homeobox homology #label HOX SUMMARY #length 382 #molecular-weight 41543 #checksum 638 SEQUENCE /// ENTRY A55557 #type complete TITLE transcription factor Brn-4 - human ALTERNATE_NAMES class III POU domain protein brain-4; transcription factor POU3F4 ORGANISM #formal_name Homo sapiens #common_name man DATE 20-Feb-1995 #sequence_revision 20-Feb-1995 #text_change 07-May-1999 ACCESSIONS A55557 REFERENCE A55557 !$#authors de Kok, Y.J.M.; van der Maarel, S.M.; Bitner-Glindzicz, M.; !1Huber, I.; Monaco, A.P.; Malcolm, S.; Pembrey, M.E.; Ropers, !1H.H.; Cremers, F.P.M. !$#journal Science (1995) 267:685-688 !$#title Association between X-linked mixed deafness and mutations in !1the POU domain gene POU3F4. !$#cross-references MUID:95141074; PMID:7839145 !$#accession A55557 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-361 ##label DEA !'##cross-references EMBL:X82324 GENETICS !$#gene GDB:POU3F4; BRN4; OTF9 !'##cross-references GDB:351386; OMIM:600420 !$#map_position Xq21.1-Xq21.1 CLASSIFICATION #superfamily transcription factor Brn-1; homeobox homology; !1POU domain homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$95-111 #region histidine/proline-rich\ !$193-260 #domain POU domain homology #label POU\ !$279-335 #domain homeobox homology #label HOX SUMMARY #length 361 #molecular-weight 39418 #checksum 3891 SEQUENCE /// ENTRY S31225 #type complete TITLE transcription factor Brn-4 - mouse ALTERNATE_NAMES class III POU domain protein brain-4 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 02-Dec-1993 #sequence_revision 01-Sep-1995 #text_change 22-Jun-1999 ACCESSIONS S31225 REFERENCE S31223 !$#authors Hara, Y.; Rovescalli, A.C.; Kim, Y.; Nirenberg, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:3280-3284 !$#title Structure and evolution of four POU domain genes expressed !1in mouse brain. !$#cross-references MUID:92228768; PMID:1565620 !$#accession S31225 !'##status preliminary !'##molecule_type DNA !'##residues 1-361 ##label HAR !'##cross-references EMBL:M88301; NID:g200448; PIDN:AAA39962.1; !1PID:g200449 CLASSIFICATION #superfamily transcription factor Brn-1; homeobox homology; !1POU domain homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$95-111 #region histidine/proline-rich\ !$193-260 #domain POU domain homology #label POU\ !$279-335 #domain homeobox homology #label HOX SUMMARY #length 361 #molecular-weight 39417 #checksum 4441 SEQUENCE /// ENTRY A44144 #type fragment TITLE transcription factor Brn-4 - rat (fragment) ALTERNATE_NAMES class III POU domain protein brain-4; transcription factor RHS2 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 27-Jun-1994 #sequence_revision 27-Jun-1994 #text_change 22-Jun-1999 ACCESSIONS A44144; S22698; S19889 REFERENCE A44144 !$#authors Le Moine, C.; Young III, W.S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:3285-3289 !$#title RHS2, a POU domain-containing gene, and its expression in !1developing and adult rat. !$#cross-references MUID:92228769; PMID:1348858 !$#accession A44144 !'##status preliminary !'##molecule_type mRNA !'##residues 1-371 ##label LEA !'##cross-references GB:M84645 REFERENCE S22698 !$#authors Mathis, J.M.; Simmons, D.M.; He, X.; Swanson, L.W.; !1Rosenfeld, M.G. !$#journal EMBO J. (1992) 11:2551-2561 !$#title Brain 4: a novel mammalian POU domain transcription factor !1exhibiting restricted brain-specific expression. !$#cross-references MUID:92331607; PMID:1628619 !$#accession S22698 !'##molecule_type mRNA !'##residues 11-371 ##label MAT !'##cross-references EMBL:Z11834; NID:g55833; PIDN:CAA77855.1; !1PID:g55834 !'##experimental_source brain GENETICS !$#gene brn-4 CLASSIFICATION #superfamily transcription factor Brn-1; homeobox homology; !1POU domain homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$105-121 #region histidine/proline-rich\ !$203-270 #domain POU domain homology #label POU\ !$289-345 #domain homeobox homology #label HOX SUMMARY #length 371 #checksum 691 SEQUENCE /// ENTRY S23248 #type fragment TITLE transcription factor POU1 - African clawed frog (fragment) ALTERNATE_NAMES pou homeobox protein nrl-22 ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 20-Feb-1995 #sequence_revision 20-Feb-1995 #text_change 22-Jun-1999 ACCESSIONS S23248; S12182 REFERENCE S23248 !$#authors Agarwal, V.R.; Sato, S.M. !$#journal Dev. Biol. (1991) 147:363-373 !$#title XLPOU 1 and XLPOU 2, two novel POU domain genes expressed in !1the dorsoanterior region of Xenopus embryos. !$#cross-references MUID:92008841; PMID:1717323 !$#accession S23248 !'##status preliminary !'##molecule_type mRNA !'##residues 1-369 ##label AGA !'##cross-references EMBL:X59056 REFERENCE S12179 !$#authors Baltzinger, M.; Stiegler, P.; Remy, P. !$#journal Nucleic Acids Res. (1990) 18:6131 !$#title Cloning and sequencing of POU-boxes expressed in Xenopus !1laevis neurula embryos. !$#cross-references MUID:91045083; PMID:2235499 !$#accession S12182 !'##molecule_type mRNA !'##residues 214-318 ##label BAL !'##cross-references EMBL:X54682; NID:g64932; PIDN:CAA38496.1; !1PID:g930277 GENETICS !$#gene POU1 CLASSIFICATION #superfamily transcription factor Brn-1; homeobox homology; !1POU domain homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$195-262 #domain POU domain homology #label POU\ !$281-337 #domain homeobox homology #label HOX SUMMARY #length 369 #checksum 306 SEQUENCE /// ENTRY A56018 #type complete TITLE transcription factor Oct-6 - human ALTERNATE_NAMES transcription factor SCIP ORGANISM #formal_name Homo sapiens #common_name man DATE 05-May-1995 #sequence_revision 05-May-1995 #text_change 22-Jun-1999 ACCESSIONS A56018; S30218 REFERENCE A56018 !$#authors Faus, I.; Hsu, H.J.; Fuchs, E. !$#journal Mol. Cell. Biol. (1994) 14:3263-3275 !$#title Oct-6: a regulator of keratinocyte gene expression in !1stratified squamous epithelia. !$#cross-references MUID:94217723; PMID:7909356 !$#accession A56018 !'##status preliminary !'##molecule_type mRNA !'##residues 1-448 ##label FAU !'##cross-references GB:L26494; NID:g508989; PIDN:AAA59965.1; !1PID:g508990 !'##note it is uncertain whether Met-1 or Met-51 is the initiator REFERENCE S30218 !$#authors Tobler, A.; Schreiber, E.; Fontana, A. !$#journal Nucleic Acids Res. (1993) 21:1043 !$#title The human Oct-6 POU transcription factor lacks the first 50 !1amino acids of its murine counterpart. !$#cross-references MUID:93197134; PMID:8451175 !$#accession S30218 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type mRNA !'##residues 51-448 ##label TOB !'##cross-references EMBL:Z18284; NID:g35133; PIDN:CAA79158.1; !1PID:g35134 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1992 GENETICS !$#gene GDB:POU3F1; OCT-6; OTF6 !'##cross-references GDB:138779 !$#map_position 19pter-19qter CLASSIFICATION #superfamily transcription factor Brn-1; homeobox homology; !1POU domain homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$251-318 #domain POU domain homology #label POU\ !$337-393 #domain homeobox homology #label HOX SUMMARY #length 448 #molecular-weight 45270 #checksum 2016 SEQUENCE /// ENTRY S30205 #type complete TITLE transcription factor Oct-6 - mouse ALTERNATE_NAMES class III POU domain protein SCIP ORGANISM #formal_name Mus musculus #common_name house mouse DATE 02-Dec-1993 #sequence_revision 26-May-1995 #text_change 22-Jun-1999 ACCESSIONS S30205; S31226; S13083; S11999 REFERENCE S30205 !$#authors Zimmerman, E.C.; Jones, C.M.; Fet, V.; Hogan, B.L.M.; !1Magnuson, M.A. !$#journal Nucleic Acids Res. (1991) 19:956 !$#title Nucleotide sequence of mouse SCIP cDNA, a POU-domain !1transcription factor. !$#cross-references MUID:91204458; PMID:1840678 !$#accession S30205 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type mRNA !'##residues 1-449 ##label ZIM !'##cross-references EMBL:X56959; NID:g49681; PIDN:CAA40280.1; !1PID:g49682 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1990 REFERENCE S31223 !$#authors Hara, Y.; Rovescalli, A.C.; Kim, Y.; Nirenberg, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:3280-3284 !$#title Structure and evolution of four POU domain genes expressed !1in mouse brain. !$#cross-references MUID:92228768; PMID:1565620 !$#accession S31226 !'##molecule_type DNA !'##residues 1-449 ##label HAR !'##cross-references EMBL:M88302; NID:g200450; PIDN:AAA39963.1; !1PID:g200451 REFERENCE S13083 !$#authors Meijer, D.; Graus, A.; Kraay, R.; Langeveld, A.; Mulder, !1M.P.; Grosveld, G. !$#journal Nucleic Acids Res. (1990) 18:7357-7365 !$#title The octamer binding factor Oct6: cDNA cloning and expression !1in early embryonic cells. !$#cross-references MUID:91081324; PMID:1979677 !$#accession S13083 !'##molecule_type mRNA !'##residues 1-449 ##label MEI !'##cross-references EMBL:X54628; NID:g53505; PIDN:CAA38445.1; !1PID:g53506 REFERENCE S11999 !$#authors Suzuki, N.; Rohdewohld, H.; Neuman, T.; Gruss, P.; Schoeler, !1H.R. !$#journal EMBO J. (1990) 9:3723-3732 !$#title Oct-6: a POU transcription factor expressed in embryonal !1stem cells and in the developing brain. !$#cross-references MUID:91006074; PMID:1976514 !$#accession S11999 !'##molecule_type mRNA !'##residues 1-26,28-449 ##label SUZ !'##cross-references EMBL:X57482; NID:g53507; PIDN:CAA40720.1; !1PID:g53508 CLASSIFICATION #superfamily transcription factor Brn-1; homeobox homology; !1POU domain homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$252-319 #domain POU domain homology #label POU\ !$338-394 #domain homeobox homology #label HOX SUMMARY #length 449 #molecular-weight 45323 #checksum 5389 SEQUENCE /// ENTRY A40168 #type complete TITLE transcription factor Oct-6 - rat ALTERNATE_NAMES POU domain protein Tst-1; transcription factor SCIP ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 05-Jun-1992 #sequence_revision 05-Jun-1992 #text_change 22-Jun-1999 ACCESSIONS A40168; A39694; S05449; S05044 REFERENCE A40168 !$#authors Monuki, E.S.; Kuhn, R.; Weinmaster, G.; Trapp, B.D.; Lemke, !1G. !$#journal Science (1990) 249:1300-1303 !$#title Expression and activity of the POU transcription factor !1SCIP. !$#cross-references MUID:90378306; PMID:1975954 !$#accession A40168 !'##status preliminary !'##molecule_type mRNA !'##residues 1-451 ##label MON !'##cross-references GB:M72711; GB:M35205; NID:g206866; PIDN:AAA42118.1; !1PID:g206867 REFERENCE A39694 !$#authors He, X.; Gerrero, R.; Simmons, D.M.; Park, R.E.; Lin, C.R.; !1Swanson, L.W.; Rosenfeld, M.G. !$#journal Mol. Cell. Biol. (1991) 11:1739-1744 !$#title Tst-1, a member of the POU domain gene family, binds the !1promoter of the gene encoding the cell surface adhesion !1molecule Po. !$#cross-references MUID:91141528; PMID:1705013 !$#accession A39694 !'##molecule_type mRNA !'##residues 35-451 ##label HEA !'##cross-references GB:M63712; NID:g207539; PIDN:AAA42303.1; !1PID:g207540 !'##note the authors translated the codon GCT for residue 249 as Pro REFERENCE S05449 !$#authors He, X.; Treacy, M.N.; Simmons, D.M.; Ingraham, H.A.; !1Swanson, L.W.; Rosenfeld, M.G. !$#journal Nature (1989) 340:662 !$#title Correction. Expression of a large family of POU-domain !1regulatory genes in mammalian brain development. !$#accession S05449 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 265-389 ##label HEX !'##note this is a revision to the sequence from reference S05042 REFERENCE S05042 !$#authors He, X.; Treacy, M.N.; Simmons, D.M.; Ingraham, H.A.; !1Swanson, L.W.; Rosenfeld, M.G. !$#journal Nature (1989) 340:35-42 !$#title Expression of a large family of POU-domain regulatory genes !1in mammalian brain development. !$#cross-references MUID:89295573; PMID:2739723 !$#accession S05044 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 265-319,'A',321-335;336-389 ##label HEF !'##note this sequence has been revised in reference S05449 GENETICS !$#gene tst-1 CLASSIFICATION #superfamily transcription factor Brn-1; homeobox homology; !1POU domain homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$254-321 #domain POU domain homology #label POU\ !$340-396 #domain homeobox homology #label HOX SUMMARY #length 451 #molecular-weight 45465 #checksum 1878 SEQUENCE /// ENTRY A54687 #type complete TITLE transcription factor Brn-5 - human ALTERNATE_NAMES homeobox protein mPOU; TCR beta enhancer binding protein TCFbeta1 ORGANISM #formal_name Homo sapiens #common_name man DATE 23-Mar-1995 #sequence_revision 23-Mar-1995 #text_change 22-Jun-1999 ACCESSIONS A54687; S42575; S40151 REFERENCE A54687 !$#authors Messier, H.; Brickner, H.; Gaikwad, J.; Fotedar, A. !$#journal Mol. Cell. Biol. (1993) 13:5450-5460 !$#title A novel POU domain protein which binds to the T-cell !1receptor beta enhancer. !$#cross-references MUID:93360980; PMID:8102789 !$#accession A54687 !'##molecule_type mRNA !'##residues 1-301 ##label MES !'##cross-references GB:L14482 REFERENCE S42575 !$#authors Wey, E.; Lyons, G.E.; Schaefer, B.W. !$#journal Eur. J. Biochem. (1994) 220:753-762 !$#title A human POU domain gene, mPOU, is expressed in developing !1brain and specific adult tissues. !$#cross-references MUID:94192665; PMID:7908264 !$#accession S42575 !'##molecule_type mRNA !'##residues 1-301 ##label WEY !'##cross-references EMBL:Z21966; NID:g437806; PIDN:CAA79977.1; !1PID:g437807 GENETICS !$#gene GDB:POU6F1; BRN5; MPOU; TCFB1 !'##cross-references GDB:361078 !$#map_position 12pter-12qter CLASSIFICATION #superfamily transcription factor Brn-5; homeobox homology; !1POU domain homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$146-213 #domain POU domain homology #label POU\ !$235-291 #domain homeobox homology #label HOX SUMMARY #length 301 #molecular-weight 32645 #checksum 3743 SEQUENCE /// ENTRY A48880 #type complete TITLE transcription factor Brn-5 - rat ALTERNATE_NAMES homeobox protein mPOU; TCR beta enhancer binding protein TCFbeta1 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 07-Apr-1994 #sequence_revision 18-Nov-1994 #text_change 24-Oct-1997 ACCESSIONS A48880 REFERENCE A48880 !$#authors Andersen, B.; Schonemann, M.D.; Pearse II, R.V.; Jenne, K.; !1Sugarman, J.; Rosenfeld, M.G. !$#journal J. Biol. Chem. (1993) 268:23390-23398 !$#title Brn-5 is a divergent POU domain factor highly expressed in !1layer IV of the neocortex. !$#cross-references MUID:94043133; PMID:7901208 !$#accession A48880 !'##status preliminary !'##molecule_type mRNA !'##residues 1-301 ##label AND !'##cross-references GB:L23204; NID:g349723 !'##experimental_source anterior pituitary !'##note sequence extracted from NCBI backbone (NCBIN:138920, !1NCBIP:138921) CLASSIFICATION #superfamily transcription factor Brn-5; homeobox homology; !1POU domain homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$146-213 #domain POU domain homology #label POU\ !$235-291 #domain homeobox homology #label HOX SUMMARY #length 301 #molecular-weight 32701 #checksum 4273 SEQUENCE /// ENTRY I56543 #type complete TITLE transcription factor Brn-5 - mouse ALTERNATE_NAMES homeobox protein mPOU; TCR beta enhancer binding protein TCFbeta1 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 26-Jul-1996 #sequence_revision 26-Jul-1996 #text_change 23-Mar-2001 ACCESSIONS I56543; A46078; S40160 REFERENCE I56543 !$#authors Bulleit, R.F.; Cui, H.; Wang, J.; Lin, X. !$#journal J. Neurosci. (1994) 14:1584-1595 !$#title NMDA receptor activation in differentiating cerebellar cell !1cultures regulates the expression of a new POU gene, Cns-1. !$#cross-references MUID:94172446; PMID:7907365 !$#accession I56543 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-301 ##label RES !'##cross-references GB:L13763; NID:g293726; PIDN:AAA53044.1; !1PID:g567227 REFERENCE A46078 !$#authors Okamoto, K.; Wakamiya, M.; Noji, S.; Koyama, E.; Taniguchi, !1S.; Takemura, R.; Copeland, N.G.; Gilbert, D.J.; Jenkins, !1N.A.; Muramatsu, M.; Hamada, H. !$#journal J. Biol. Chem. (1993) 268:7449-7457 !$#title A novel class of murine POU gene predominantly expressed in !1central nervous system. !$#cross-references MUID:93216691; PMID:8463278 !$#accession A46078 !'##status preliminary !'##molecule_type mRNA !'##residues 1-130,'SLE',132-301 ##label OKA !'##cross-references GB:D13801 !'##note authors translated the codon ATC for residue 263 as Glu REFERENCE S40151 !$#authors Wey, E.; Lyons, G.E.; Schafer, B.W. !$#submission submitted to the EMBL Data Library, March 1993 !$#description mPOU: A novel human POU domain gene expressed in specific !1adult tissues. !$#accession S40160 !'##status preliminary !'##molecule_type mRNA !'##residues 197-301 ##label WEY !'##cross-references EMBL:Z21967; NID:g437875; PIDN:CAA79978.1; !1PID:g437876 GENETICS !$#gene POU 1 CLASSIFICATION #superfamily transcription factor Brn-5; homeobox homology; !1POU domain homology KEYWORDS alternative splicing; DNA binding; homeobox; nucleus; !1transcription regulation FEATURE !$146-213 #domain POU domain homology #label POU\ !$235-291 #domain homeobox homology #label HOX SUMMARY #length 301 #molecular-weight 32851 #checksum 5161 SEQUENCE /// ENTRY S30234 #type complete TITLE transcription factor POU-C - zebra fish ORGANISM #formal_name Brachydanio rerio #common_name zebra fish DATE 13-Jan-1995 #sequence_revision 13-Jan-1995 #text_change 22-Jun-1999 ACCESSIONS S30234 REFERENCE S30234 !$#authors Johansen, T.; Moens, U.; Holm, T.; Fjose, A.; Krauss, S. !$#journal Nucleic Acids Res. (1993) 21:475-483 !$#title Zebrafish pou[c]: a divergent POU family gene ubiquitously !1expressed during embryogenesis. !$#cross-references MUID:93181237; PMID:8441661 !$#accession S30234 !'##status preliminary !'##molecule_type mRNA !'##residues 1-610 ##label JOH !'##cross-references EMBL:X68432; NID:g62552; PIDN:CAA48481.1; !1PID:g62553 CLASSIFICATION #superfamily zebra fish transciption factor POU-C; homeobox !1homology; POU domain homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$1-82 #region acidic\ !$86-91 #region serine/threonine-rich\ !$214-239 #region glutamiine-rich\ !$238-245 #region threonine-rich\ !$287-292 #region serine/threonine-rich\ !$388-394 #region threonine-rich\ !$455-522 #domain POU domain homology #label POU\ !$542-547 #region nuclear location signal\ !$544-600 #domain homeobox homology #label HOX SUMMARY #length 610 #molecular-weight 63124 #checksum 1118 SEQUENCE /// ENTRY JQ2010 #type complete TITLE transcription factor POU-1 - planarian (Dugesia japonica) ORGANISM #formal_name Dugesia japonica DATE 03-Feb-1994 #sequence_revision 03-Feb-1994 #text_change 16-Jun-2000 ACCESSIONS JQ2010 REFERENCE JQ2010 !$#authors Orii, H.; Agata, K.; Watanabe, K. !$#journal Biochem. Biophys. Res. Commun. (1993) 192:1395-1402 !$#title POU-domain genes in planarian Dugesia japonica: the !1structure and expression. !$#cross-references MUID:93282851; PMID:8099480 !$#accession JQ2010 !'##molecule_type mRNA !'##residues 1-559 ##label ORI !'##cross-references DDBJ:D12924; NID:g217311; PIDN:BAA02308.1; !1PID:g217312 !'##experimental_source strain GI GENETICS !$#gene DjPOU1 CLASSIFICATION #superfamily planarian transcription factor POU-1; homeobox !1homology; POU domain homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$266-333 #domain POU domain homology #label POU\ !$352-408 #domain homeobox homology #label HOX SUMMARY #length 559 #molecular-weight 63999 #checksum 4885 SEQUENCE /// ENTRY A48763 #type complete TITLE transcription factor SGF-3 - silkworm ALTERNATE_NAMES POU-M1; silk gland factor 3 ORGANISM #formal_name Bombyx mori #common_name silkworm DATE 19-May-1995 #sequence_revision 19-May-1995 #text_change 22-Jun-1999 ACCESSIONS A48763 REFERENCE A48763 !$#authors Fukuta, M.; Matsuno, K.; Hui, C.; Nagata, T.; Takiya, S.; !1Xu, P.X.; Ueno, K.; Suzuki, Y. !$#journal J. Biol. Chem. (1993) 268:19471-19475 !$#title Molecular cloning of a POU domain-containing factor involved !1in the regulation of the Bombyx sericin-1 gene. !$#cross-references MUID:93374935; PMID:7690034 !$#accession A48763 !'##molecule_type mRNA !'##residues 1-351 ##label FUK !'##cross-references GB:M64781; NID:g156009; PIDN:AAA27841.1; !1PID:g156010 COMMENT This protein is expressed in the middle silk gland during !1the fifth intermolt; it is believed to be involved in the !1regulation of silk protein genes, particularly sericin-1. CLASSIFICATION #superfamily transcription factor SGF-3; homeobox homology; !1POU domain homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$156-223 #domain POU domain homology #label POU\ !$242-298 #domain homeobox homology #label HOX SUMMARY #length 351 #molecular-weight 38591 #checksum 6879 SEQUENCE /// ENTRY A54963 #type complete TITLE transcription factor ceh-18 - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 12-Apr-1995 #sequence_revision 12-Apr-1995 #text_change 22-Jun-1999 ACCESSIONS A54963 REFERENCE A54963 !$#authors Greenstein, D.; Hird, S.; Plasterk, R.H.A.; Andachi, Y.; !1Kohara, Y.; Wang, B.; Finney, M.; Ruvkun, G. !$#journal Genes Dev. (1994) 8:1935-1948 !$#title Targeted mutations in the Caenorhabditis elegans POU homeo !1box gene ceh-18 cause defects in oocyte cell cycle arrest, !1gonad migration, and epidermal differentiation. !$#cross-references MUID:95047345; PMID:7958868 !$#accession A54963 !'##status preliminary !'##molecule_type DNA !'##residues 1-542 ##label GRE !'##cross-references GB:U16367; NID:g564040; PIDN:AAA52203.1; !1PID:g564041 GENETICS !$#gene ceh-18 CLASSIFICATION #superfamily transcription factor ceh-18; homeobox homology; !1POU domain homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$297-364 #domain POU domain homology #label POU\ !$422-478 #domain homeobox homology #label HOX SUMMARY #length 542 #molecular-weight 59480 #checksum 1749 SEQUENCE /// ENTRY A49836 #type complete TITLE transcription factor POU-2, long splice form - zebra fish ORGANISM #formal_name Brachydanio rerio #common_name zebra fish DATE 06-Jan-1995 #sequence_revision 06-Jan-1995 #text_change 16-Jun-2000 ACCESSIONS A49836; S58867 REFERENCE A49836 !$#authors Takeda, H.; Matsuzaki, T.; Oki, T.; Miyagawa, T.; Amanuma, !1H. !$#journal Genes Dev. (1994) 8:45-59 !$#title A novel POU domain gene, zebrafish pou2: expression and !1roles of two alternatively spliced twin products in early !1development. !$#cross-references MUID:94116858; PMID:8288127 !$#accession A49836 !'##molecule_type mRNA !'##residues 1-472 ##label TAK !'##cross-references GB:D28548; NID:g461302; PIDN:BAA05901.1; !1PID:g461303 REFERENCE S58867 !$#authors Hauptmann, G.; Gerster, T. !$#journal Mech. Dev. (1995) 51:127-138 !$#title Pou-2 - a zebrafish gene active during cleavage stages and !1in the early hindbrain. !$#cross-references MUID:95399309; PMID:7669688 !$#accession S58867 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type mRNA !'##residues 1-159,'V',161-244,'D',246-461,'L',463-470,'T',472 ##label !1HAU !'##cross-references EMBL:X84224; NID:g871002; PIDN:CAA59006.1; !1PID:g871003 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1995 COMMENT In zebra fish, POU-2 is maternally expressed; transcripts !1are present from the one-cell to the gastrula stages. GENETICS !$#gene pou2 CLASSIFICATION #superfamily zebra fish transcription factor POU-2; homeobox !1homology; POU domain homology KEYWORDS alternative splicing; DNA binding; homeobox; nucleus; !1transcription regulation FEATURE !$256-323 #domain POU domain homology #label POU\ !$344-400 #domain homeobox homology #label HOX SUMMARY #length 472 #molecular-weight 51504 #checksum 8241 SEQUENCE /// ENTRY B49836 #type complete TITLE transcription factor POU-2, short splice form - zebra fish ORGANISM #formal_name Brachydanio rerio #common_name zebra fish DATE 06-Jan-1995 #sequence_revision 06-Jan-1995 #text_change 15-Oct-1999 ACCESSIONS B49836 REFERENCE A49836 !$#authors Takeda, H.; Matsuzaki, T.; Oki, T.; Miyagawa, T.; Amanuma, !1H. !$#journal Genes Dev. (1994) 8:45-59 !$#title A novel POU domain gene, zebrafish pou2: expression and !1roles of two alternatively spliced twin products in early !1development. !$#cross-references MUID:94116858; PMID:8288127 !$#accession B49836 !'##molecule_type mRNA !'##residues 1-399 ##label TAK !'##cross-references GB:D28548 COMMENT Because the homeobox sequence is incomplete, this protein !1does not bind to DNA. Overexpression of this form produced !1developmental defects. GENETICS !$#gene pou2 CLASSIFICATION #superfamily zebra fish transcription factor POU-2; homeobox !1homology; POU domain homology KEYWORDS alternative splicing; DNA binding; homeobox; nucleus; !1transcription regulation FEATURE !$256-323 #domain POU domain homology #label POU\ !$344-387 #domain homeobox homology #status atypical #label HOX SUMMARY #length 399 #molecular-weight 43502 #checksum 1388 SEQUENCE /// ENTRY C42022 #type complete TITLE transcription factor Oct-91 - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 04-Mar-1993 #sequence_revision 18-Nov-1994 #text_change 22-Jun-1999 ACCESSIONS C42022; A49145 REFERENCE A42022 !$#authors Hinkley, C.S.; Martin, J.F.; Leibham, D.; Perry, M. !$#journal Mol. Cell. Biol. (1992) 12:638-649 !$#title Sequential expression of multiple POU proteins during !1amphibian early development. !$#cross-references MUID:92123189; PMID:1732736 !$#accession C42022 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-445 ##label HIN !'##cross-references GB:M60077; NID:g214922; PIDN:AAA49999.1; !1PID:g214923 !'##note sequence extracted from NCBI backbone (NCBIP:76554) REFERENCE A49145 !$#authors Frank, D.; Harland, R.M. !$#journal Development (1992) 115:439-448 !$#title Localized expression of a Xenopus POU gene depends on !1cell-autonomous transcriptional activation and !1induction-dependent inactivation. !$#cross-references MUID:93048808; PMID:1358592 !$#accession A49145 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 236-247,'A',249-294,'E',296-332,'G',334-362 ##label FRA !'##experimental_source stage 11 embryos !'##note sequence extracted from NCBI backbone (NCBIP:117108) CLASSIFICATION #superfamily Xenopus transcription factor Oct-91; homeobox !1homology; POU domain homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$225-292 #domain POU domain homology #label POU\ !$313-369 #domain homeobox homology #label HOX SUMMARY #length 445 #molecular-weight 49034 #checksum 9442 SEQUENCE /// ENTRY B42022 #type complete TITLE transcription factor Oct-25 - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 04-Mar-1993 #sequence_revision 18-Nov-1994 #text_change 22-Jun-1999 ACCESSIONS B42022 REFERENCE A42022 !$#authors Hinkley, C.S.; Martin, J.F.; Leibham, D.; Perry, M. !$#journal Mol. Cell. Biol. (1992) 12:638-649 !$#title Sequential expression of multiple POU proteins during !1amphibian early development. !$#cross-references MUID:92123189; PMID:1732736 !$#accession B42022 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-448 ##label HIN !'##cross-references GB:M60074; NID:g214916; PIDN:AAA49996.1; !1PID:g214917 !'##note sequence extracted from NCBI backbone (NCBIP:76556) CLASSIFICATION #superfamily Xenopus transcription factor Oct-91; homeobox !1homology; POU domain homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$234-301 #domain POU domain homology #label POU\ !$322-378 #domain homeobox homology #label HOX SUMMARY #length 448 #molecular-weight 49543 #checksum 443 SEQUENCE /// ENTRY A48829 #type complete TITLE transcription factor Oct-60 - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 01-Dec-1993 #sequence_revision 18-Nov-1994 #text_change 22-Jun-1999 ACCESSIONS A48829; A42022 REFERENCE A48829 !$#authors Whitfield, T.; Heasman, J.; Wylie, C. !$#journal Dev. Biol. (1993) 155:361-370 !$#title XLPOU-60, a Xenopus POU-domain mRNA, is oocyte-specific from !1very early stages of oogenesis, and localised to presumptive !1mesoderm and ectoderm in the blastula. !$#cross-references MUID:93162302; PMID:8432392 !$#accession A48829 !'##molecule_type mRNA !'##residues 1-426 ##label WHI !'##cross-references GB:X86377; NID:g785051; PIDN:CAA60136.1; !1PID:g785052 !'##experimental_source oocyte !'##note sequence extracted from NCBI backbone (NCBIN:124758, !1NCBIP:124759) REFERENCE A42022 !$#authors Hinkley, C.S.; Martin, J.F.; Leibham, D.; Perry, M. !$#journal Mol. Cell. Biol. (1992) 12:638-649 !$#title Sequential expression of multiple POU proteins during !1amphibian early development. !$#cross-references MUID:92123189; PMID:1732736 !$#accession A42022 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-139,'P',141-426 ##label HIN !'##cross-references GB:M60075; NID:g214918; PIDN:AAA49997.1; !1PID:g214919 !'##note sequence extracted from NCBI backbone (NCBIP:76557) and !1corrected to correspond with the published sequence CLASSIFICATION #superfamily Xenopus transcription factor Oct-91; homeobox !1homology; POU domain homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$209-276 #domain POU domain homology #label POU\ !$297-353 #domain homeobox homology #label HOX SUMMARY #length 426 #molecular-weight 47253 #checksum 381 SEQUENCE /// ENTRY S18718 #type complete TITLE transcription factor Pit-1 - human ALTERNATE_NAMES transcription factor GHF-1 ORGANISM #formal_name Homo sapiens #common_name man DATE 22-Nov-1993 #sequence_revision 03-Nov-1995 #text_change 16-Jun-2000 ACCESSIONS S18718; S20315; PN0442; S34855; S34259 REFERENCE S18718 !$#authors Lew, A.M.; Elsholtz, H.P. !$#journal Nucleic Acids Res. (1991) 19:6329 !$#title Cloning of the human cDNA for transcription factor Pit-1. !$#cross-references MUID:92066490; PMID:1956794 !$#accession S18718 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type mRNA !'##residues 1-291 ##label LEW !'##cross-references EMBL:X62429; NID:g35474; PIDN:CAA44295.1; !1PID:g35475 !'##note this sequence was submitted to the EMBL Data Library, October !11991 REFERENCE S20315 !$#authors Tatsumi, K.; Notomi, T.; Amino, N.; Miyai, K. !$#journal Biochim. Biophys. Acta (1992) 1129:231-234 !$#title Nucleotide sequence of the complementary DNA for human !1Pit-1/GHF-1. !$#cross-references MUID:92110389; PMID:1370379 !$#accession S20315 !'##molecule_type mRNA !'##residues 1-291 ##label TAT !'##cross-references EMBL:D10216; NID:g219997; PIDN:BAA01068.1; !1PID:g219998; EMBL:D01114 REFERENCE PN0442 !$#authors Ohta, K.; Nobukuni, Y.; Mitsubuchi, H.; Ohta, T.; Tohma, T.; !1Jinno, Y.; Endo, F.; Matsuda, I. !$#journal Gene (1992) 122:387-388 !$#title Characterization of the gene encoding human pituitary !1transcription factor, Pit-1. !$#cross-references MUID:93138415; PMID:1487156 !$#accession PN0442 !'##molecule_type DNA !'##residues 1-47 ##label OHT !'##cross-references DDBJ:D11333 !'##note translation of the nucleotide sequence is not complete REFERENCE S34855 !$#authors Pernasetti, F.; Wera, S.; Belayew, A.; Martial, J.A. !$#journal Nucleic Acids Res. (1993) 21:3584 !$#title Cloning of a human GHF-1/Pit-1 cDNA variant. !$#cross-references MUID:93348003; PMID:8346040 !$#accession S34855 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type mRNA !'##residues 1-3,'R',5-226,'Y',228-291 ##label PER !'##cross-references EMBL:X72215; NID:g311925; PIDN:CAA51017.1; !1PID:g311926 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1May 1993 GENETICS !$#gene GDB:POU1F1; PIT1; GHF-1 !'##cross-references GDB:129070; OMIM:173110 !$#map_position 3p11-3p11 CLASSIFICATION #superfamily transcription factor Pit-1; homeobox homology; !1POU domain homology KEYWORDS DNA binding; homeobox; nucleus; pituitary; transcription !1regulation FEATURE !$131-198 #domain POU domain homology #label POU\ !$215-271 #domain homeobox homology #label HOX SUMMARY #length 291 #molecular-weight 32912 #checksum 1447 SEQUENCE /// ENTRY A31305 #type complete TITLE transcription factor Pit-1 - bovine ALTERNATE_NAMES transcription factor GHF-1 ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 22-Jun-1999 ACCESSIONS A31305 REFERENCE A90906 !$#authors Bodner, M.; Castrillo, J.L.; Theill, L.E.; Deerinck, T.; !1Ellisman, M.; Karin, M. !$#journal Cell (1988) 55:505-518 !$#title The pituitary-specific transcription factor GHF-1 is a !1homeobox-containing protein. !$#cross-references MUID:89028660; PMID:2902927 !$#accession A31305 !'##molecule_type mRNA !'##residues 1-291 ##label BOD !'##cross-references GB:X12657; NID:g388; PIDN:CAA31184.1; PID:g389 CLASSIFICATION #superfamily transcription factor Pit-1; homeobox homology; !1POU domain homology KEYWORDS DNA binding; homeobox; nucleus; pituitary; transcription !1regulation FEATURE !$131-198 #domain POU domain homology #label POU\ !$215-271 #domain homeobox homology #label HOX SUMMARY #length 291 #molecular-weight 33038 #checksum 2502 SEQUENCE /// ENTRY S11663 #type complete TITLE transcription factor pit-1, thyrotrope-specific splice form - mouse ALTERNATE_NAMES transcription factor GHF-1 CONTAINS transcription factor Pit-1, pituitary-specific splice form; transcription factor pit-1, thyrotrope-specific splice form ORGANISM #formal_name Mus musculus #common_name house mouse DATE 19-Mar-1997 #sequence_revision 17-Oct-1997 #text_change 16-Jun-2000 ACCESSIONS S11663; JC2182; A48032; S41454 REFERENCE S11663 !$#authors Li, S.; Crenshaw III, E.B.; Rawson, E.J.; Simmons, D.M.; !1Swanson, L.W.; Rosenfeld, M.G. !$#journal Nature (1990) 347:528-533 !$#title Dwarf locus mutants lacking three pituitary cell types !1result from mutations in the POU-domain gene pit-1. !$#cross-references MUID:91015356; PMID:1977085 !$#accession S11663 !'##status preliminary !'##molecule_type DNA; mRNA !'##residues 1-47,62-305 ##label LIS !'##cross-references GB:X57512; NID:g53690; PIDN:CAA40737.1; PID:g53691; !1GB:D12885; NID:g493685; PID:g493686 REFERENCE JC2182 !$#authors Jehn, B.; Chicaiza, G.; Martin, F.; Jaggi, R. !$#journal Biochem. Biophys. Res. Commun. (1994) 200:156-162 !$#title Isolation of three novel POU-domain containing cDNA clones !1from lactating mouse mammary gland. !$#cross-references MUID:94220079; PMID:8166682 !$#accession JC2182 !'##molecule_type mRNA !'##residues 180-236,'I',238-247,'R',249-257 ##label JEH !'##cross-references EMBL:Z29628; NID:g452413; PIDN:CAA82735.1; !1PID:g452414 !'##experimental_source mammary gland REFERENCE A48032 !$#authors Haugen, B.R.; Wood, W.M.; Gordon, D.F.; Ridgway, E.C. !$#journal J. Biol. Chem. (1993) 268:20818-20824 !$#title A thyrotrope-specific variant of Pit-1 transactivates the !1thyrotropin beta promoter. !$#cross-references MUID:94012619; PMID:8407911 !$#accession A48032 !'##status preliminary !'##molecule_type mRNA !'##residues 1-80 ##label HAU GENETICS !$#gene pit-1 CLASSIFICATION #superfamily transcription factor Pit-1; homeobox homology; !1POU domain homology KEYWORDS alternative splicing; DNA binding; homeobox; nucleus; !1pituitary; transcription regulation FEATURE !$1-305 #product transcription factor pit-1, !8thyrotrope-specific splice form #status predicted !8#label MAT2\ !$1-47,62-305 #product transcription factor Pit-1, !8pituitary-specific splice form #status predicted !8#label MAT1\ !$145-212 #domain POU domain homology #label POU\ !$229-285 #domain homeobox homology #label HOX SUMMARY #length 305 #molecular-weight 34428 #checksum 5379 SEQUENCE /// ENTRY S22705 #type complete TITLE transcription factor GHF-1, splice form GHF-2 - rat ALTERNATE_NAMES transcription factor Pit-1, splice form Pit-1a ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 13-Jan-1995 #sequence_revision 13-Jan-1995 #text_change 22-Jun-1999 ACCESSIONS S22705; S22706; A41813; B31305; A31306; S22642 REFERENCE S22705 !$#authors Theill, L.E.; Hattori, K.; Lazzaro, D.; Castrillo, J.L.; !1Karin, M. !$#journal EMBO J. (1992) 11:2261-2269 !$#title Differential splicing of the GHF1 primary transcript gives !1rise to two functionally distinct homeodomain proteins. !$#cross-references MUID:92289691; PMID:1600947 !$#accession S22705 !'##molecule_type DNA !'##residues 1-317 ##label THE !'##cross-references EMBL:X65367 !$#accession S22706 !'##molecule_type DNA !'##residues 1-47,74-317 ##label TH2 !'##cross-references EMBL:X65367 REFERENCE A41813 !$#authors Konzak, K.E.; Moore, D.D. !$#journal Mol. Endocrinol. (1992) 6:241-247 !$#title Functional isoforms of Pit-1 generated by alternative !1messenger RNA splicing. !$#cross-references MUID:92236631; PMID:1569967 !$#accession A41813 !'##status preliminary !'##molecule_type mRNA !'##residues 1-99 ##label KON !'##cross-references GB:S97398; NID:g248783; PIDN:AAC60656.1; !1PID:g248784 !'##experimental_source GH3 pituitary cell line !'##note sequence extracted from NCBI backbone (NCBIN:97398, !1NCBIP:97399) REFERENCE A90906 !$#authors Bodner, M.; Castrillo, J.L.; Theill, L.E.; Deerinck, T.; !1Ellisman, M.; Karin, M. !$#journal Cell (1988) 55:505-518 !$#title The pituitary-specific transcription factor GHF-1 is a !1homeobox-containing protein. !$#cross-references MUID:89028660; PMID:2902927 !$#accession B31305 !'##molecule_type mRNA !'##residues 1-47,74-317 ##label BOD !'##cross-references GB:X12658; NID:g56218; PIDN:CAA31185.1; PID:g56219 REFERENCE A31306 !$#authors Ingraham, H.A.; Chen, R.; Mangalam, H.J.; Elsholtz, H.P.; !1Flynn, S.E.; Lin, C.R.; Simmons, D.M.; Swanson, L.; !1Rosenfeld, M.G. !$#journal Cell (1988) 55:519-529 !$#title A tissue-specific transcription factor containing a !1homeodomain specifies a pituitary phenotype. !$#cross-references MUID:89028661; PMID:2902928 !$#accession A31306 !'##molecule_type mRNA !'##residues 1-47,74-317 ##label ING !'##cross-references GB:M23253; NID:g511882; PIDN:AAA41854.1; !1PID:g511883 REFERENCE S22642 !$#authors Morris, A.E.; Kloss, B.; McChesney, R.E.; Bancroft, C.; !1Chasin, L.A. !$#journal Nucleic Acids Res. (1992) 20:1355-1361 !$#title An alternatively spliced Pit-1 isoform altered in its !1ability to trans-activate. !$#cross-references MUID:92220611; PMID:1561093 !$#accession S22642 !'##molecule_type mRNA !'##residues 49-73 ##label MOR !'##cross-references EMBL:X63089 GENETICS !$#gene GHF-1; Pit-1 !$#map_position 16 !$#introns 74/1; 98/1; 173/1; 228/1; 248/2 CLASSIFICATION #superfamily transcription factor Pit-1; homeobox homology; !1POU domain homology KEYWORDS alternative splicing; DNA binding; homeobox; nucleus; !1pituitary; transcription regulation FEATURE !$1-317 #product transcription factor GHF-2/Pit-1a #status !8predicted #label TF2\ !$1-47,74-317 #product transcription factor GHF-1/Pit-1 #status !8predicted #label TF1\ !$157-224 #domain POU domain homology #label POU\ !$241-297 #domain homeobox homology #label HOX SUMMARY #length 317 #molecular-weight 35769 #checksum 8465 SEQUENCE /// ENTRY S26693 #type complete TITLE transcription factor Pit-1 - turkey ALTERNATE_NAMES transcription factor GHF-1 ORGANISM #formal_name Meleagris gallopavo #common_name common turkey DATE 25-Feb-1994 #sequence_revision 26-May-1995 #text_change 22-Jun-1999 ACCESSIONS S26693 REFERENCE S26693 !$#authors Wong, E.A.; Silsby, J.L.; El Halawani, M.E. !$#journal DNA Cell Biol. (1992) 11:651-660 !$#title Complementary DNA cloning and expression of Pit-1/GHF-1 from !1the domestic turkey. !$#cross-references MUID:93039671; PMID:1418622 !$#accession S26693 !'##status preliminary !'##molecule_type mRNA !'##residues 1-327 ##label WON !'##cross-references EMBL:X69471; NID:g64077; PIDN:CAA49229.1; !1PID:g64078 !'##note the authors translated the codon ATT for residue 319 as Phe CLASSIFICATION #superfamily transcription factor Pit-1; homeobox homology; !1POU domain homology KEYWORDS DNA binding; homeobox; nucleus; pituitary; transcription !1regulation FEATURE !$166-233 #domain POU domain homology #label POU\ !$250-306 #domain homeobox homology #label HOX SUMMARY #length 327 #molecular-weight 36790 #checksum 1450 SEQUENCE /// ENTRY A49511 #type complete TITLE transcription factor Pit-1 - rainbow trout ALTERNATE_NAMES transcription factor GHF-1 ORGANISM #formal_name Oncorhynchus mykiss #common_name rainbow trout DATE 10-Nov-1995 #sequence_revision 10-Nov-1995 #text_change 16-Jun-2000 ACCESSIONS A49511 REFERENCE A49511 !$#authors Yamada, S.; Hata, J.; Yamashita, S. !$#journal J. Biol. Chem. (1993) 268:24361-24366 !$#title Molecular cloning of fish Pit-1 cDNA and its functional !1binding to promoter of gene expressed in the pituitary. !$#cross-references MUID:94043275; PMID:8226986 !$#accession A49511 !'##status preliminary !'##molecule_type mRNA !'##residues 1-358 ##label YAM !'##cross-references GB:D16513; NID:g416067; PIDN:BAA03964.1; !1PID:g416068 !'##note authors translated the codon TAT for residue 89 as Thr CLASSIFICATION #superfamily transcription factor Pit-1; homeobox homology; !1POU domain homology KEYWORDS DNA binding; homeobox; nucleus; pituitary; transcription !1regulation FEATURE !$199-266 #domain POU domain homology #label POU\ !$283-339 #domain homeobox homology #label HOX SUMMARY #length 358 #molecular-weight 39375 #checksum 8348 SEQUENCE /// ENTRY JC6121 #type complete TITLE transcription factor Pit-1 - chinook salmon ALTERNATE_NAMES transcription factor GHF-1 ORGANISM #formal_name Oncorhynchus tschawytscha #common_name chinook salmon DATE 23-Mar-1997 #sequence_revision 09-May-1997 #text_change 22-Jun-1999 ACCESSIONS JC6121; A41928 REFERENCE JC6121 !$#authors Majumdar, S.; Irwin, D.M.; Elsholtz, H.P. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1996) 93:10256-10261 !$#title Selective constraints on the activation domain of !1transcription factor Pit-1. !$#cross-references MUID:96413633; PMID:8816787 !$#accession JC6121 !'##molecule_type mRNA !'##residues 1-358 ##label MAJ !'##cross-references GB:U55045; NID:g1621540; PIDN:AAB17254.1; !1PID:g1621541 REFERENCE A41928 !$#authors Elsholtz, H.P.; Majumdar-Sonnylal, S.; Xiong, F.; Gong, Z.; !1Hew, C.L. !$#journal Mol. Endocrinol. (1992) 6:515-522 !$#title Phylogenetic specificity of prolactin gene expression to !1conservation of Pit-1 function. !$#cross-references MUID:92261606; PMID:1350055 !$#accession A41928 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type mRNA !'##residues 198-341 ##label ELS GENETICS !$#gene pit-1 CLASSIFICATION #superfamily transcription factor Pit-1; homeobox homology; !1POU domain homology KEYWORDS DNA binding; homeobox; nucleus; pituitary; transcription !1regulation FEATURE !$199-266 #domain POU domain homology #label POU\ !$283-339 #domain homeobox homology #label HOX SUMMARY #length 358 #molecular-weight 39408 #checksum 8719 SEQUENCE /// ENTRY JC1168 #type complete TITLE transcription factor Pit-1 - chum salmon ALTERNATE_NAMES transcription factor GHF-1 ORGANISM #formal_name Oncorhynchus keta #common_name chum salmon DATE 05-Mar-1993 #sequence_revision 05-Mar-1993 #text_change 22-Jun-1999 ACCESSIONS JC1168; I51076 REFERENCE JC1168 !$#authors Ono, M.; Takayama, Y. !$#journal Gene (1992) 116:275-279 !$#title Structures of cDNAs encoding chum salmon pituitary-specific !1transcription factor, Pit-1/GHF-1. !$#cross-references MUID:92339901; PMID:1634120 !$#accession JC1168 !'##molecule_type mRNA !'##residues 1-365 ##label ONO !'##cross-references GB:D10444; NID:g222901; PIDN:BAA01234.1; !1PID:g222902 CLASSIFICATION #superfamily transcription factor Pit-1; homeobox homology; !1POU domain homology KEYWORDS DNA binding; homeobox; nucleus; pituitary; transcription !1regulation FEATURE !$195-262 #domain POU domain homology #label POU\ !$279-335 #domain homeobox homology #label HOX SUMMARY #length 365 #molecular-weight 40333 #checksum 9858 SEQUENCE /// ENTRY S25464 #type complete TITLE transcription factor Pit-1 - Atlantic salmon ALTERNATE_NAMES transcription factor GHF-1 ORGANISM #formal_name Salmo salar #common_name Atlantic salmon DATE 20-Feb-1995 #sequence_revision 20-Feb-1995 #text_change 22-Jun-1999 ACCESSIONS S25464 REFERENCE S25464 !$#authors Lorens, J.B.; Male, R.; Aasland, R. !$#submission submitted to the EMBL Data Library, August 1992 !$#description Molecular characterization of Pit-1/GHF-1 from Atlantic !1salmon. !$#accession S25464 !'##status preliminary !'##molecule_type mRNA !'##residues 1-358 ##label LOR !'##cross-references EMBL:X68039; NID:g64377; PIDN:CAA48175.1; !1PID:g64378 CLASSIFICATION #superfamily transcription factor Pit-1; homeobox homology; !1POU domain homology KEYWORDS DNA binding; homeobox; nucleus; pituitary; transcription !1regulation FEATURE !$199-266 #domain POU domain homology #label POU\ !$283-339 #domain homeobox homology #label HOX SUMMARY #length 358 #molecular-weight 39494 #checksum 9716 SEQUENCE /// ENTRY JC6186 #type complete TITLE transcription factor Pit-1 - gilthead sea bream ALTERNATE_NAMES transcription factor GHF-1 ORGANISM #formal_name Sparus aurata #common_name gilthead sea bream DATE 11-Apr-1997 #sequence_revision 09-May-1997 #text_change 22-Jun-1999 ACCESSIONS JC6186 REFERENCE JC6186 !$#authors Martinez-Barbera, J.P.; Vila, V.; Valdivia, M.M.; Castrillo, !1J.L. !$#journal Gene (1997) 185:87-93 !$#title Molecular cloning of gilthead seabream (Sparus aurata) !1pituitary transcription factor GHF-1/Pit-1. !$#cross-references MUID:97186701; PMID:9034317 !$#contents Pituitary glands !$#accession JC6186 !'##molecule_type mRNA !'##residues 1-371 ##label MAR !'##cross-references EMBL:X81646; NID:g1004292; PIDN:CAA57306.1; !1PID:g1004293 GENETICS !$#gene GHF-1/Pit-1 CLASSIFICATION #superfamily transcription factor Pit-1; homeobox homology; !1POU domain homology KEYWORDS DNA binding; homeobox; nucleus; pituitary; transcription !1regulation FEATURE !$201-268 #domain POU domain homology #label POU\ !$285-341 #domain homeobox homology #label HOX SUMMARY #length 371 #molecular-weight 40483 #checksum 472 SEQUENCE /// ENTRY A30042 #type complete TITLE transcription factor unc-86, long splice form - Caenorhabditis elegans ALTERNATE_NAMES C30A5.7 protein ORGANISM #formal_name Caenorhabditis elegans DATE 28-Feb-1990 #sequence_revision 28-Feb-1990 #text_change 22-Jun-1999 ACCESSIONS A30042; S44779 REFERENCE A30042 !$#authors Finney, M.; Ruvkun, G.; Horvitz, H.R. !$#journal Cell (1988) 55:757-769 !$#title The C. elegans cell lineage and differentiation gene unc-86 !1encodes a protein with a homeodomain and extended similarity !1to transcription factors. !$#cross-references MUID:89051866; PMID:2903797 !$#accession A30042 !'##molecule_type DNA !'##residues 1-467 ##label FIN !'##cross-references GB:L10990; NID:g156211; PIDN:AAB59176.1; !1PID:g156217; GB:M22363; NID:g156485; PID:g156486 REFERENCE S44774 !$#authors Anderson, K. !$#submission submitted to the EMBL Data Library, February 1993 !$#description Sequence of the C. elegans cosmid C30A5. !$#accession S44779 !'##status preliminary !'##molecule_type DNA !'##residues 1-467 ##label AND !'##cross-references EMBL:L10990; NID:g156211; PIDN:AAB59176.1; !1PID:g156217 GENETICS !$#gene unc-86 !$#introns 128/3; 174/2; 291/3; 383/2; 420/2 CLASSIFICATION #superfamily transcription factor unc-86; homeobox homology; !1POU domain homology KEYWORDS alternative splicing; DNA binding; homeobox; nucleus; !1transcription regulation FEATURE !$272-342 #domain POU domain homology #label POU\ !$364-420 #domain homeobox homology #label HOX SUMMARY #length 467 #molecular-weight 52314 #checksum 9063 SEQUENCE /// ENTRY S44778 #type complete TITLE transcription factor unc-86, short splice form - Caenorhabditis elegans ALTERNATE_NAMES C30A5.6 protein ORGANISM #formal_name Caenorhabditis elegans DATE 20-Feb-1995 #sequence_revision 20-Feb-1995 #text_change 22-Jun-1999 ACCESSIONS S44778 REFERENCE S44774 !$#authors Anderson, K. !$#submission submitted to the EMBL Data Library, February 1993 !$#description Sequence of the C. elegans cosmid C30A5. !$#accession S44778 !'##molecule_type DNA !'##residues 1-429 ##label AND !'##cross-references EMBL:L10990; NID:g156211; PIDN:AAB59175.1; !1PID:g156216 GENETICS !$#introns 128/3; 253/3; 345/2; 382/2 CLASSIFICATION #superfamily transcription factor unc-86; homeobox homology; !1POU domain homology KEYWORDS alternative splicing; DNA binding; homeobox; nucleus; !1transcription regulation FEATURE !$234-304 #domain POU domain homology #label POU\ !$326-382 #domain homeobox homology #label HOX SUMMARY #length 429 #molecular-weight 48214 #checksum 4214 SEQUENCE /// ENTRY B56564 #type complete TITLE transcription factor nubbin - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES transcription factor dPOU-19 ORGANISM #formal_name Drosophila melanogaster DATE 21-Jul-1995 #sequence_revision 21-Jul-1995 #text_change 22-Jun-1999 ACCESSIONS B56564; A41277 REFERENCE A56564 !$#authors Lloyd, A.; Sakonju, S. !$#journal Mech. Dev. (1991) 36:87-102 !$#title Characterization of two Drosophila POU domain genes, related !1to oct-1 and oct-2, and the regulation of their expression !1patterns. !$#cross-references MUID:92144419; PMID:1685891 !$#accession B56564 !'##status preliminary !'##molecule_type mRNA !'##residues 1-601 ##label LLO !'##cross-references GB:S80561; NID:g245323; PIDN:AAB21409.1; !1PID:g245324 !'##note sequence extracted from NCBI backbone (NCBIN:80561, !1NCBIP:80562) REFERENCE A41277 !$#authors Dick, T.; Yang, X.; Yeo, S.; Chia, W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:7645-7649 !$#title Two closely linked Drosophila POU domain genes are expressed !1in neuroblasts and sensory elements. !$#cross-references MUID:91352045; PMID:1881906 !$#accession A41277 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-70,'D',72-107,'M',109-419,'P',421-600 ##label DIC !'##cross-references GB:M65015 !'##note the sequence shown follows the authors' translation at !1positions 71 and 108 GENETICS !$#gene FlyBase:nub !'##cross-references FlyBase:FBgn0002970 CLASSIFICATION #superfamily Drosophila transcription factor nubbin; !1homeobox homology; POU domain homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$428-495 #domain POU domain homology #label POU\ !$524-580 #domain homeobox homology #label HOX SUMMARY #length 601 #molecular-weight 65261 #checksum 7240 SEQUENCE /// ENTRY A56564 #type complete TITLE transcription factor pdm2 - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES POU domain protein 2; transcription factor dOct2; transcription factor dPOU-28 ORGANISM #formal_name Drosophila melanogaster DATE 21-Jul-1995 #sequence_revision 21-Jul-1995 #text_change 15-Oct-1999 ACCESSIONS A56564; A46196; B41277 REFERENCE A56564 !$#authors Lloyd, A.; Sakonju, S. !$#journal Mech. Dev. (1991) 36:87-102 !$#title Characterization of two Drosophila POU domain genes, related !1to oct-1 and oct-2, and the regulation of their expression !1patterns. !$#cross-references MUID:92144419; PMID:1685891 !$#accession A56564 !'##status preliminary !'##molecule_type mRNA !'##residues 1-498 ##label LLO !'##cross-references GB:S80559; NID:g245321; PIDN:AAB21408.1; !1PID:g245322 !'##note sequence extracted from NCBI backbone (NCBIN:80559, !1NCBIP:80560) REFERENCE A46196 !$#authors Prakash, K.; Fang, X.D.; Engelberg, D.; Behal, A.; Parker, !1C.S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:7080-7084 !$#title dOct2, a Drosophila Oct transcription factor that functions !1in yeast. !$#cross-references MUID:92357775; PMID:1496003 !$#accession A46196 !'##status preliminary !'##molecule_type mRNA !'##residues 1-247,'S',249-446,'N',448-498 ##label PRA !'##cross-references GB:M93149; NID:g158004; PIDN:AAA28732.1; !1PID:g158005 !'##note sequence extracted from NCBI backbone (NCBIN:113522, !1NCBIP:113523) REFERENCE A41277 !$#authors Dick, T.; Yang, X.; Yeo, S.; Chia, W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:7645-7649 !$#title Two closely linked Drosophila POU domain genes are expressed !1in neuroblasts and sensory elements. !$#cross-references MUID:91352045; PMID:1881906 !$#accession B41277 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-155,'N',157-220,'GA',222,'AR',225-471,'RRL' ##label DIC !'##cross-references GB:M65016; NID:g157289 !'##note the sequence shown follows the authors' translation at position !1156 GENETICS !$#gene FlyBase:pdm2 !'##cross-references FlyBase:FBgn0004394 CLASSIFICATION #superfamily Drosophila transcription factor pdm2; homeobox !1homology; POU domain homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$293-360 #domain POU domain homology #label POU\ !$392-448 #domain homeobox homology #label HOX SUMMARY #length 498 #molecular-weight 55462 #checksum 6645 SEQUENCE /// ENTRY S19095 #type complete TITLE transcription factor Cf1a - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES POU domain protein Cf1-a ORGANISM #formal_name Drosophila melanogaster DATE 22-Nov-1993 #sequence_revision 12-Apr-1996 #text_change 21-Jan-2000 ACCESSIONS S19095; S14796; S08143 REFERENCE S19095 !$#authors Treacy, M.N. !$#submission submitted to the EMBL Data Library, March 1991 !$#accession S19095 !'##molecule_type mRNA !'##residues 1-549 ##label TRE !'##cross-references EMBL:X58435; NID:g7717; PIDN:CAA41341.1; PID:g7718 REFERENCE S14795 !$#authors Treacy, M.N.; He, X.; Rosenfeld, M.G. !$#journal Nature (1991) 350:577-584 !$#title I-POU: a POU-domain protein that inhibits neuron-specific !1gene activation. !$#cross-references MUID:91204052; PMID:1673230 !$#accession S14796 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-166,'GG',169-549 ##label TRE1 !'##cross-references EMBL:X58435 REFERENCE S08143 !$#authors Johnson, W.A.; Hirsh, J. !$#journal Nature (1990) 343:467-470 !$#title Binding of a Drosophila POU-domain protein to a sequence !1element regulating gene expression in specific dopaminergic !1neurons. !$#cross-references MUID:90136944; PMID:1967821 !$#accession S08143 !'##molecule_type DNA !'##residues 122-168,'ACLA',173,'CRLAC',180-185,'G',187-402,'AKYARRRHD', !1'GR',415-458,'AAHQLAAH' ##label JOH !'##cross-references EMBL:X52252; NID:g7715; PIDN:CAA36496.1; PID:g7716 GENETICS !$#gene FlyBase:vvl !'##cross-references FlyBase:FBgn0003995 CLASSIFICATION #superfamily Drosophila transcription factor Cf1a; homeobox !1homology; POU domain homology KEYWORDS DNA binding; homeobox; nucleus; transcription regulation FEATURE !$258-325 #domain POU domain homology #label POU\ !$344-400 #domain homeobox homology #label HOX SUMMARY #length 549 #molecular-weight 59101 #checksum 4376 SEQUENCE /// ENTRY I53277 #type complete TITLE transcription factor isl-1 - human ALTERNATE_NAMES insulin enhancer-binding protein isl-1; islet-1 protein ORGANISM #formal_name Homo sapiens #common_name man DATE 01-Nov-1996 #sequence_revision 01-Nov-1996 #text_change 21-Jul-2000 ACCESSIONS I53277; I38522 REFERENCE I53277 !$#authors Wang, M.; Drucker, D.J. !$#journal Endocrinology (1994) 134:1416-1422 !$#title The LIM domain homeobox gene isl-1: conservation of human, !1hamster, and rat complementary deoxyribonucleic acid !1sequences and expression in cell types of nonneuroendocrine !1lineage. !$#cross-references MUID:94164048; PMID:7907017 !$#accession I53277 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-349 ##label RES !'##cross-references GB:S70721; NID:g545789; PIDN:AAD14064.1; !1PID:g4261764 REFERENCE I38522 !$#authors Riggs, A.C.; Tanizawa, Y.; Aoki, M.; Wasson, J.; Ferrer, J.; !1Rabin, D.U.; Vaxillaire, M.; Froguel, P.; Permutt, M.A. !$#journal Diabetes (1995) 44:689-694 !$#title Characterization of the LIM/homeodomain gene islet-1 and !1single nucleotide screening in NIDDM. !$#cross-references MUID:95309532; PMID:7789634 !$#accession I38522 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 4-349 ##label RE2 !'##cross-references EMBL:U07559; NID:g533418; PIDN:AAA81946.1; !1PID:g533419 GENETICS !$#gene GDB:ISL1; ISL-1 !'##cross-references GDB:376478; OMIM:600366 !$#map_position 5q-5q CLASSIFICATION #superfamily transcription factor isl-1; homeobox homology; !1LIM metal-binding repeat homology KEYWORDS DNA binding; duplication; homeobox; nucleus; transcription !1regulation; zinc FEATURE !$17-70 #domain LIM metal-binding repeat homology #label !8LIM1\ !$79-132 #domain LIM metal-binding repeat homology #label !8LIM2\ !$182-238 #domain homeobox homology #label HOX SUMMARY #length 349 #molecular-weight 39035 #checksum 8930 SEQUENCE /// ENTRY I67417 #type complete TITLE transcription factor isl-1 - rat ALTERNATE_NAMES insulin enhancer-binding protein isl-1; islet-1 protein ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 26-Jul-1996 #sequence_revision 26-Jul-1996 #text_change 22-Jun-1999 ACCESSIONS I67417; S09321 REFERENCE I53277 !$#authors Wang, M.; Drucker, D.J. !$#journal Endocrinology (1994) 134:1416-1422 !$#title The LIM domain homeobox gene isl-1: conservation of human, !1hamster, and rat complementary deoxyribonucleic acid !1sequences and expression in cell types of nonneuroendocrine !1lineage. !$#cross-references MUID:94164048; PMID:7907017 !$#accession I67417 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-349 ##label RES !'##cross-references GB:S69329; NID:g545786; PIDN:AAB30128.1; !1PID:g545787 REFERENCE S09321 !$#authors Karlsson, O.; Thor, S.; Norberg, T.; Ohlsson, H.; Edlund, T. !$#journal Nature (1990) 344:879-882 !$#title Insulin gene enhancer binding protein Isl-1 is a member of a !1novel class of proteins containing both a homeo- and a !1Cys-His domain. !$#cross-references MUID:90231441; PMID:1691825 !$#accession S09321 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-349 ##label KAR !'##cross-references EMBL:X53258 GENETICS !$#gene isl-1 CLASSIFICATION #superfamily transcription factor isl-1; homeobox homology; !1LIM metal-binding repeat homology KEYWORDS DNA binding; duplication; homeobox; nucleus; transcription !1regulation; zinc FEATURE !$17-70 #domain LIM metal-binding repeat homology #label !8LIM1\ !$79-132 #domain LIM metal-binding repeat homology #label !8LIM2\ !$182-238 #domain homeobox homology #label HOX SUMMARY #length 349 #molecular-weight 39035 #checksum 8930 SEQUENCE /// ENTRY I67418 #type complete TITLE transcription factor isl-1 - hamster ALTERNATE_NAMES insulin enhancer-binding protein isl-1; islet-1 protein ORGANISM #formal_name Cricetinae gen. sp. #common_name hamster DATE 02-Aug-1996 #sequence_revision 02-Aug-1996 #text_change 24-Jul-1997 ACCESSIONS I67418 REFERENCE I53277 !$#authors Wang, M.; Drucker, D.J. !$#journal Endocrinology (1994) 134:1416-1422 !$#title The LIM domain homeobox gene isl-1: conservation of human, !1hamster, and rat complementary deoxyribonucleic acid !1sequences and expression in cell types of nonneuroendocrine !1lineage. !$#cross-references MUID:94164048; PMID:7907017 !$#accession I67418 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-349 ##label RES !'##cross-references GB:S70720; NID:g545788 GENETICS !$#gene isl-1 CLASSIFICATION #superfamily transcription factor isl-1; homeobox homology; !1LIM metal-binding repeat homology KEYWORDS DNA binding; duplication; homeobox; nucleus; transcription !1regulation; zinc FEATURE !$17-70 #domain LIM metal-binding repeat homology #label !8LIM1\ !$79-132 #domain LIM metal-binding repeat homology #label !8LIM2\ !$182-238 #domain homeobox homology #label HOX SUMMARY #length 349 #molecular-weight 39035 #checksum 8930 SEQUENCE /// ENTRY I50369 #type complete TITLE transcription factor isl-1 - chicken ALTERNATE_NAMES insulin enhancer-binding protein isl-1; islet-1 protein ORGANISM #formal_name Gallus gallus #common_name chicken DATE 13-Sep-1996 #sequence_revision 13-Sep-1996 #text_change 16-Jul-1999 ACCESSIONS I50369 REFERENCE A55198 !$#authors Tsuchida, T.; Ensini, M.; Morton, S.B.; Baldassare, M.; !1Edlund, T.; Jessell, T.M.; Pfaff, S.L. !$#journal Cell (1994) 79:957-970 !$#title Topographic organization of embryonic motor neurons defined !1by expression of LIM homeobox genes [see comments]. !$#cross-references MUID:95094281; PMID:7528105 !$#accession I50369 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-349 ##label TSU !'##cross-references GB:L35567; NID:g531178; PIDN:AAA62171.1; !1PID:g531179 GENETICS !$#gene islet-1; isl-1 CLASSIFICATION #superfamily transcription factor isl-1; homeobox homology; !1LIM metal-binding repeat homology KEYWORDS DNA binding; duplication; homeobox; nucleus; transcription !1regulation; zinc FEATURE !$17-70 #domain LIM metal-binding repeat homology #label !8LIM1\ !$79-132 #domain LIM metal-binding repeat homology #label !8LIM2\ !$182-238 #domain homeobox homology #label HOX SUMMARY #length 349 #molecular-weight 39033 #checksum 8265 SEQUENCE /// ENTRY I51739 #type complete TITLE transcription factor isl-1 - zebra fish ALTERNATE_NAMES insulin enhancer-binding protein isl-1; islet-1 protein ORGANISM #formal_name Brachydanio rerio #common_name zebra fish DATE 13-Mar-1997 #sequence_revision 13-Mar-1997 #text_change 16-Jul-1999 ACCESSIONS I51739 REFERENCE I51739 !$#authors Inoue, A.; Takahashi, M.; Hatta, K.; Hotta, Y.; Okamoto, H. !$#journal Dev. Dyn. (1994) 199:1-11 !$#title Developmental regulation of islet-1 mRNA expression during !1neuronal differentiation in embryonic zebrafish. !$#cross-references MUID:94220748; PMID:8167375 !$#accession I51739 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-349 ##label INO !'##cross-references GB:D21135; NID:g497897; PIDN:BAA04670.1; !1PID:g497898 CLASSIFICATION #superfamily transcription factor isl-1; homeobox homology; !1LIM metal-binding repeat homology KEYWORDS DNA binding; duplication; homeobox; nucleus; transcription !1regulation; zinc FEATURE !$17-70 #domain LIM metal-binding repeat homology #label !8LIM1\ !$79-132 #domain LIM metal-binding repeat homology #label !8LIM2\ !$182-238 #domain homeobox homology #label HOX SUMMARY #length 349 #molecular-weight 39181 #checksum 42 SEQUENCE /// ENTRY A55198 #type complete TITLE transcription factor isl-2 - rat ALTERNATE_NAMES insulin enhancer-binding protein isl-2; islet-2 protein ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 02-Jul-1996 #sequence_revision 02-Jul-1996 #text_change 16-Jul-1999 ACCESSIONS A55198 REFERENCE A55198 !$#authors Tsuchida, T.; Ensini, M.; Morton, S.B.; Baldassare, M.; !1Edlund, T.; Jessell, T.M.; Pfaff, S.L. !$#journal Cell (1994) 79:957-970 !$#title Topographic organization of embryonic motor neurons defined !1by expression of LIM homeobox genes [see comments]. !$#cross-references MUID:95094281; PMID:7528105 !$#accession A55198 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-360 ##label RES !'##cross-references GB:L35571; NID:g531217; PIDN:AAA62161.1; !1PID:g531218 GENETICS !$#gene islet-2; isl-2 CLASSIFICATION #superfamily transcription factor isl-1; homeobox homology; !1LIM metal-binding repeat homology KEYWORDS DNA binding; duplication; homeobox; nucleus; transcription !1regulation; zinc FEATURE !$27-80 #domain LIM metal-binding repeat homology #label !8LIM1\ !$89-142 #domain LIM metal-binding repeat homology #label !8LIM2\ !$193-249 #domain homeobox homology #label HOX SUMMARY #length 360 #molecular-weight 39675 #checksum 7614 SEQUENCE /// ENTRY I50370 #type fragment TITLE transcription factor isl-2 - chicken (fragment) ALTERNATE_NAMES insulin enhancer-binding protein isl-2; islet-2 protein ORGANISM #formal_name Gallus gallus #common_name chicken DATE 21-Feb-1997 #sequence_revision 21-Feb-1997 #text_change 16-Jul-1999 ACCESSIONS I50370 REFERENCE A55198 !$#authors Tsuchida, T.; Ensini, M.; Morton, S.B.; Baldassare, M.; !1Edlund, T.; Jessell, T.M.; Pfaff, S.L. !$#journal Cell (1994) 79:957-970 !$#title Topographic organization of embryonic motor neurons defined !1by expression of LIM homeobox genes [see comments]. !$#cross-references MUID:95094281; PMID:7528105 !$#accession I50370 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-319 ##label TSU !'##cross-references GB:L35568; NID:g531180; PIDN:AAA62172.1; !1PID:g531181 GENETICS !$#gene islet-2; isl-2 CLASSIFICATION #superfamily transcription factor isl-1; homeobox homology; !1LIM metal-binding repeat homology KEYWORDS DNA binding; duplication; homeobox; nucleus; transcription !1regulation; zinc FEATURE !$1-43 #domain LIM metal-binding repeat homology (fragment) !8#label LIM1\ !$52-105 #domain LIM metal-binding repeat homology #label !8LIM2\ !$151-207 #domain homeobox homology #label HOX SUMMARY #length 319 #checksum 2119 SEQUENCE /// ENTRY I51734 #type complete TITLE transcription factor isl-2 - zebra fish ALTERNATE_NAMES insulin enhancer-binding protein isl-2; islet-2 protein ORGANISM #formal_name Brachydanio rerio #common_name zebra fish DATE 13-Mar-1997 #sequence_revision 13-Mar-1997 #text_change 16-Jul-1999 ACCESSIONS I51734; S57407 REFERENCE I51734 !$#authors Tokumoto, M.; Gong, Z.; Tsubokawa, T.; Hew, C.L.; Uyemura, !1K.; Hotta, Y.; Okamoto, H. !$#journal Dev. Biol. (1995) 171:578-589 !$#title Molecular heterogeneity among primary motoneurons and within !1myotomes revealed by the differential mRNA expression of !1novel islet-1 homologs in embryonic zebrafish. !$#cross-references MUID:96005022; PMID:7556938 !$#accession I51734 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-359 ##label TOK !'##cross-references GB:D38453; NID:g1037165; PIDN:BAA07484.1; !1PID:g1037166 REFERENCE S57407 !$#authors Appel, B.; Korzh, V.; Glasgow, E.; Thor, S.; Edlund, T.; !1Dawid, L.; Eisen, J. !$#submission submitted to the EMBL Data Library, June 1995 !$#description Motoneuron fate specification and patterned LIM homeobox !1gene expression in embryonic zebrafish. !$#accession S57407 !'##status preliminary !'##molecule_type mRNA !'##residues 1-359 ##label APP !'##cross-references EMBL:X88805; NID:g871000; PIDN:CAA61283.1; !1PID:g871001 GENETICS !$#gene isl-2 CLASSIFICATION #superfamily transcription factor isl-1; homeobox homology; !1LIM metal-binding repeat homology KEYWORDS DNA binding; duplication; homeobox; nucleus; transcription !1regulation; zinc FEATURE !$27-80 #domain LIM metal-binding repeat homology #label !8LIM1\ !$89-142 #domain LIM metal-binding repeat homology #label !8LIM2\ !$192-248 #domain homeobox homology #label HOX SUMMARY #length 359 #molecular-weight 40227 #checksum 7994 SEQUENCE /// ENTRY A55973 #type complete TITLE transcription factor isl-2a, long form - chinook salmon ALTERNATE_NAMES insulin enhancer-binding protein isl-2a; islet-2a protein ORGANISM #formal_name Oncorhynchus tschawytscha #common_name chinook salmon DATE 03-Oct-1995 #sequence_revision 03-Oct-1995 #text_change 07-May-1999 ACCESSIONS A55973; S52092; S19957 REFERENCE A55973 !$#authors Gong, Z.; Hui, C.; Hew, C.L. !$#journal J. Biol. Chem. (1995) 270:3335-3345 !$#title Presence of isl-1-related LIM domain homeobox genes in !1teleost and their similar patterns of expression in brain !1and spinal cord. !$#cross-references MUID:95155429; PMID:7852419 !$#accession A55973 !'##molecule_type mRNA !'##residues 1-358 ##label GON !'##cross-references EMBL:X64885 REFERENCE S52089 !$#authors Gong, Z.; Hew, C.L. !$#journal Biochim. Biophys. Acta (1995) 1260:349-354 !$#title Several splicing variants of isl-1 like genes in the chinook !1salmon (Oncorhynchus tschawytscha) encode truncated !1transcription factors containing a complete LIM domain. !$#cross-references MUID:95178560; PMID:7873614 !$#accession S52092 !'##status preliminary !'##molecule_type mRNA !'##residues 1-358 ##label GO2 !'##cross-references EMBL:X64885 !'##note the authors translated the codon GAG for residue 135 as Asp GENETICS !$#gene isl-2a !$#introns 83/2 CLASSIFICATION #superfamily transcription factor isl-1; homeobox homology; !1LIM metal-binding repeat homology KEYWORDS alternative splicing; DNA binding; duplication; homeobox; !1nucleus; transcription regulation; zinc FEATURE !$27-80 #domain LIM metal-binding repeat homology #label !8LIM1\ !$89-142 #domain LIM metal-binding repeat homology #label !8LIM2\ !$191-247 #domain homeobox homology #label HOX SUMMARY #length 358 #molecular-weight 40072 #checksum 4636 SEQUENCE /// ENTRY B55973 #type fragment TITLE transcription factor isl-2b - chinook salmon (fragment) ALTERNATE_NAMES insulin enhancer-binding protein isl-2b; islet-2b protein ORGANISM #formal_name Oncorhynchus tschawytscha #common_name chinook salmon DATE 03-Oct-1995 #sequence_revision 03-Oct-1995 #text_change 16-Jul-1999 ACCESSIONS B55973; S52091; S19956 REFERENCE A55973 !$#authors Gong, Z.; Hui, C.; Hew, C.L. !$#journal J. Biol. Chem. (1995) 270:3335-3345 !$#title Presence of isl-1-related LIM domain homeobox genes in !1teleost and their similar patterns of expression in brain !1and spinal cord. !$#cross-references MUID:95155429; PMID:7852419 !$#accession B55973 !'##molecule_type mRNA !'##residues 1-340 ##label GON !'##cross-references EMBL:X64884; NID:g64208; PIDN:CAA46102.1; !1PID:g64209 !'##note authors translated the codon CTG for residue 251 as Met, and !1ATG for residue 256 as Leu REFERENCE S52089 !$#authors Gong, Z.; Hew, C.L. !$#journal Biochim. Biophys. Acta (1995) 1260:349-354 !$#title Several splicing variants of isl-1 like genes in the chinook !1salmon (Oncorhynchus tschawytscha) encode truncated !1transcription factors containing a complete LIM domain. !$#cross-references MUID:95178560; PMID:7873614 !$#accession S52091 !'##status preliminary !'##molecule_type mRNA !'##residues 1-340 ##label GO2 !'##cross-references EMBL:X64884; NID:g64208; PIDN:CAA46102.1; !1PID:g64209 !'##note the authors translated the codon CAG for residue 105 as His, !1GTG for residue 107 as Leu, CTG for residue 251 as Met, and !1ATG for residue 256 as Leu GENETICS !$#gene isl-2b CLASSIFICATION #superfamily transcription factor isl-1; homeobox homology; !1LIM metal-binding repeat homology KEYWORDS DNA binding; duplication; homeobox; nucleus; transcription !1regulation; zinc FEATURE !$9-62 #domain LIM metal-binding repeat homology #label !8LIM1\ !$71-124 #domain LIM metal-binding repeat homology #label !8LIM2\ !$173-229 #domain homeobox homology #label HOX SUMMARY #length 340 #checksum 5243 SEQUENCE /// ENTRY C55973 #type complete TITLE transcription factor isl-3 - chinook salmon ALTERNATE_NAMES insulin enhancer-binding protein isl-3; islet-3 protein ORGANISM #formal_name Oncorhynchus tschawytscha #common_name chinook salmon DATE 03-Oct-1995 #sequence_revision 03-Oct-1995 #text_change 07-May-1999 ACCESSIONS C55973; S52090 REFERENCE A55973 !$#authors Gong, Z.; Hui, C.; Hew, C.L. !$#journal J. Biol. Chem. (1995) 270:3335-3345 !$#title Presence of isl-1-related LIM domain homeobox genes in !1teleost and their similar patterns of expression in brain !1and spinal cord. !$#cross-references MUID:95155429; PMID:7852419 !$#accession C55973 !'##molecule_type mRNA !'##residues 1-363 ##label GON !'##cross-references GB:X64883 REFERENCE S52089 !$#authors Gong, Z.; Hew, C.L. !$#journal Biochim. Biophys. Acta (1995) 1260:349-354 !$#title Several splicing variants of isl-1 like genes in the chinook !1salmon (Oncorhynchus tschawytscha) encode truncated !1transcription factors containing a complete LIM domain. !$#cross-references MUID:95178560; PMID:7873614 !$#accession S52090 !'##status preliminary !'##molecule_type mRNA !'##residues 1-82,'IWNKMCKMQPGIQQQ' ##label GO2 !'##cross-references EMBL:X64883 !'##note alternative splice form GENETICS !$#gene isl-3 CLASSIFICATION #superfamily transcription factor isl-1; homeobox homology; !1LIM metal-binding repeat homology KEYWORDS alternative splicing; DNA binding; duplication; homeobox; !1nucleus; transcription regulation; zinc FEATURE !$27-80 #domain LIM metal-binding repeat homology #label !8LIM1\ !$89-142 #domain LIM metal-binding repeat homology #label !8LIM2\ !$192-248 #domain homeobox homology #label HOX SUMMARY #length 363 #molecular-weight 40799 #checksum 5148 SEQUENCE /// ENTRY I51735 #type complete TITLE transcription factor isl-3 - zebra fish ALTERNATE_NAMES insulin enhancer-binding protein isl-3; islet-3 protein ORGANISM #formal_name Brachydanio rerio #common_name zebra fish DATE 13-Mar-1997 #sequence_revision 13-Mar-1997 #text_change 16-Jul-1999 ACCESSIONS I51735 REFERENCE I51734 !$#authors Tokumoto, M.; Gong, Z.; Tsubokawa, T.; Hew, C.L.; Uyemura, !1K.; Hotta, Y.; Okamoto, H. !$#journal Dev. Biol. (1995) 171:578-589 !$#title Molecular heterogeneity among primary motoneurons and within !1myotomes revealed by the differential mRNA expression of !1novel islet-1 homologs in embryonic zebrafish. !$#cross-references MUID:96005022; PMID:7556938 !$#accession I51735 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-358 ##label TOK !'##cross-references GB:D38454; NID:g1037167; PIDN:BAA07485.1; !1PID:g1037168 GENETICS !$#gene isl-3 CLASSIFICATION #superfamily transcription factor isl-1; homeobox homology; !1LIM metal-binding repeat homology KEYWORDS DNA binding; duplication; homeobox; nucleus; transcription !1regulation; zinc FEATURE !$27-80 #domain LIM metal-binding repeat homology #label !8LIM1\ !$89-142 #domain LIM metal-binding repeat homology #label !8LIM2\ !$192-248 #domain homeobox homology #label HOX SUMMARY #length 358 #molecular-weight 39848 #checksum 7081 SEQUENCE /// ENTRY B46233 #type complete TITLE transcription factor lmx-1 - golden hamster ORGANISM #formal_name Mesocricetus auratus #common_name golden hamster DATE 21-Sep-1993 #sequence_revision 18-Nov-1994 #text_change 16-Jul-1999 ACCESSIONS B46233 REFERENCE A46233 !$#authors German, M.S.; Wang, J.; Chadwick, R.B.; Rutter, W.J. !$#journal Genes Dev. (1992) 6:2165-2176 !$#title Synergistic activation of the insulin gene by a LIM-homeo !1domain protein and a basic helix-loop-helix protein: !1building a functional insulin minienhancer complex. !$#cross-references MUID:93051335; PMID:1358758 !$#accession B46233 !'##status preliminary !'##molecule_type mRNA !'##residues 1-382 ##label GER !'##cross-references GB:X81406; NID:g587460; PIDN:CAA57163.1; !1PID:g587461 !'##experimental_source insulinoma cell line HIT T-15 M2.2.2 !'##note sequence extracted from NCBI backbone (NCBIN:117927, !1NCBIP:117928) GENETICS !$#gene lmx-1 CLASSIFICATION #superfamily transcription factor isl-1; homeobox homology; !1LIM metal-binding repeat homology KEYWORDS DNA binding; duplication; homeobox; nucleus; transcription !1regulation; zinc FEATURE !$35-85 #domain LIM metal-binding repeat homology #label !8LIM1\ !$94-147 #domain LIM metal-binding repeat homology #label !8LIM2\ !$196-252 #domain homeobox homology #label HOX SUMMARY #length 382 #molecular-weight 42802 #checksum 6563 SEQUENCE /// ENTRY I58187 #type complete TITLE homeotic protein lim-1 - rat ORGANISM #formal_name Rattus sp. #common_name rat DATE 26-Jul-1996 #sequence_revision 26-Jul-1996 #text_change 16-Jul-1999 ACCESSIONS I58187 REFERENCE I58187 !$#authors Furuyama, T.; Inagaki, S.; Iwahashi, Y.; Takagi, H. !$#journal Neurosci. Lett. (1994) 170:266-268 !$#title Distribution of Rlim, an LIM homeodomain gene, in the rat !1brain. !$#cross-references MUID:94336075; PMID:7914684 !$#accession I58187 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-406 ##label RES !'##cross-references GB:S71523; NID:g559635; PIDN:AAC60696.1; !1PID:g559636 GENETICS !$#gene lim-1 CLASSIFICATION #superfamily homeotic protein lim-1; homeobox homology; LIM !1metal-binding repeat homology KEYWORDS DNA binding; duplication; embryo; homeobox; nucleus; !1transcription regulation; zinc FEATURE !$4-54 #domain LIM metal-binding repeat homology #label !8LIM1\ !$63-117 #domain LIM metal-binding repeat homology #label !8LIM2\ !$181-237 #domain homeobox homology #label HOX SUMMARY #length 406 #molecular-weight 44780 #checksum 2535 SEQUENCE /// ENTRY I48637 #type complete TITLE homeotic protein lim-1 - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 02-Jul-1996 #sequence_revision 02-Jul-1996 #text_change 16-Jul-1999 ACCESSIONS I48637; S42788 REFERENCE I48637 !$#authors Fujii, T.; Pichel, J.G.; Taira, M.; Toyama, R.; Dawid, I.B.; !1Westphal, H. !$#journal Dev. Dyn. (1994) 199:73-83 !$#title Expression patterns of the murine LIM class homeobox gene !1lim1 in the developing brain and excretory system. !$#cross-references MUID:94220754; PMID:7909459 !$#accession I48637 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-406 ##label RES !'##cross-references EMBL:Z27410; NID:g425216; PIDN:CAA81797.1; !1PID:g425217 REFERENCE S42788 !$#authors Fujii, T. !$#submission submitted to the EMBL Data Library, November 1993 !$#accession S42788 !'##status preliminary !'##molecule_type mRNA !'##residues 1-406 ##label FUJ !'##cross-references EMBL:Z27410; NID:g425216; PIDN:CAA81797.1; !1PID:g425217 GENETICS !$#gene Lhx1 CLASSIFICATION #superfamily homeotic protein lim-1; homeobox homology; LIM !1metal-binding repeat homology KEYWORDS DNA binding; duplication; embryo; homeobox; nucleus; !1transcription regulation; zinc FEATURE !$4-54 #domain LIM metal-binding repeat homology #label !8LIM1\ !$63-117 #domain LIM metal-binding repeat homology #label !8LIM2\ !$181-237 #domain homeobox homology #label HOX SUMMARY #length 406 #molecular-weight 44780 #checksum 2535 SEQUENCE /// ENTRY I48186 #type complete TITLE homeotic protein lim-1 - golden hamster ALTERNATE_NAMES homeotic protein lmx2 ORGANISM #formal_name Mesocricetus auratus #common_name golden hamster DATE 02-Jul-1996 #sequence_revision 02-Jul-1996 #text_change 16-Jul-1999 ACCESSIONS I48186 REFERENCE I48185 !$#authors Rudnick, A.; Ling, T.Y.; Odagiri, H.; Rutter, W.J.; German, !1M.S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1994) 91:12203-12207 !$#title Pancreatic beta cells express a diverse set of homeobox !1genes. !$#cross-references MUID:95083670; PMID:7991607 !$#accession I48186 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-406 ##label RES !'##cross-references EMBL:X81407; NID:g587462; PIDN:CAA57164.1; !1PID:g587463 GENETICS !$#gene lmx2 CLASSIFICATION #superfamily homeotic protein lim-1; homeobox homology; LIM !1metal-binding repeat homology KEYWORDS DNA binding; duplication; embryo; homeobox; nucleus; !1transcription regulation; zinc FEATURE !$4-54 #domain LIM metal-binding repeat homology #label !8LIM1\ !$63-117 #domain LIM metal-binding repeat homology #label !8LIM2\ !$181-237 #domain homeobox homology #label HOX SUMMARY #length 406 #molecular-weight 44780 #checksum 2535 SEQUENCE /// ENTRY I50375 #type complete TITLE homeotic protein lim-1 - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 13-Sep-1996 #sequence_revision 13-Sep-1996 #text_change 16-Jul-1999 ACCESSIONS I50375 REFERENCE A55198 !$#authors Tsuchida, T.; Ensini, M.; Morton, S.B.; Baldassare, M.; !1Edlund, T.; Jessell, T.M.; Pfaff, S.L. !$#journal Cell (1994) 79:957-970 !$#title Topographic organization of embryonic motor neurons defined !1by expression of LIM homeobox genes [see comments]. !$#cross-references MUID:95094281; PMID:7528105 !$#accession I50375 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-406 ##label TSU !'##cross-references GB:L35569; NID:g531182; PIDN:AAA62173.1; !1PID:g531183 GENETICS !$#gene lim-1 CLASSIFICATION #superfamily homeotic protein lim-1; homeobox homology; LIM !1metal-binding repeat homology KEYWORDS DNA binding; duplication; embryo; homeobox; nucleus; !1transcription regulation; zinc FEATURE !$4-54 #domain LIM metal-binding repeat homology #label !8LIM1\ !$63-117 #domain LIM metal-binding repeat homology #label !8LIM2\ !$181-237 #domain homeobox homology #label HOX SUMMARY #length 406 #molecular-weight 44845 #checksum 9918 SEQUENCE /// ENTRY S23802 #type complete TITLE homeotic protein lim-1 - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 22-Nov-1993 #sequence_revision 03-Nov-1995 #text_change 16-Jul-1999 ACCESSIONS S23802 REFERENCE S23802 !$#authors Taira, M.; Jamrich, M.; Good, P.J.; Dawid, I.B. !$#journal Genes Dev. (1992) 6:356-366 !$#title The LIM domain-containing homeo box gene Xlim-1 is expressed !1specifically in the organizer region of Xenopus gastrula !1embryos. !$#cross-references MUID:92192449; PMID:1347750 !$#accession S23802 !'##molecule_type mRNA !'##residues 1-403 ##label TAI !'##cross-references EMBL:X63889; NID:g64829; PIDN:CAA45353.1; !1PID:g64830 GENETICS !$#gene lim-1 CLASSIFICATION #superfamily homeotic protein lim-1; homeobox homology; LIM !1metal-binding repeat homology KEYWORDS DNA binding; duplication; embryo; homeobox; nucleus; !1transcription regulation; zinc FEATURE !$4-54 #domain LIM metal-binding repeat homology #label !8LIM1\ !$63-117 #domain LIM metal-binding repeat homology #label !8LIM2\ !$180-236 #domain homeobox homology #label HOX SUMMARY #length 403 #molecular-weight 44934 #checksum 8769 SEQUENCE /// ENTRY I61573 #type complete TITLE homeotic protein lim-2 - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 02-Aug-1996 #sequence_revision 02-Aug-1996 #text_change 16-Jul-1999 ACCESSIONS I61573 REFERENCE A55198 !$#authors Tsuchida, T.; Ensini, M.; Morton, S.B.; Baldassare, M.; !1Edlund, T.; Jessell, T.M.; Pfaff, S.L. !$#journal Cell (1994) 79:957-970 !$#title Topographic organization of embryonic motor neurons defined !1by expression of LIM homeobox genes [see comments]. !$#cross-references MUID:95094281; PMID:7528105 !$#accession I61573 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-402 ##label RES !'##cross-references GB:L35572; NID:g531219; PIDN:AAA62162.1; !1PID:g531220 GENETICS !$#gene lim-2 CLASSIFICATION #superfamily homeotic protein lim-1; homeobox homology; LIM !1metal-binding repeat homology KEYWORDS DNA binding; duplication; embryo; homeobox; nucleus; !1transcription regulation; zinc FEATURE !$5-55 #domain LIM metal-binding repeat homology #label !8LIM1\ !$64-118 #domain LIM metal-binding repeat homology #label !8LIM2\ !$181-237 #domain homeobox homology #label HOX SUMMARY #length 402 #molecular-weight 44387 #checksum 1768 SEQUENCE /// ENTRY I59360 #type complete TITLE homeotic protein lim-3 - mouse ALTERNATE_NAMES homeotic protein Plim ORGANISM #formal_name Mus musculus #common_name house mouse DATE 02-Jul-1996 #sequence_revision 02-Jul-1996 #text_change 16-Jul-1999 ACCESSIONS I59360 REFERENCE I59360 !$#authors Bach, I.; Rhodes, S.J.; Pearse, R.V. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1995) 92:2720-2724 !$#title P-Lim, a LIM homeodomain factor, is expressed during !1pituitary organ and cell commitment and synergizes with !1Pit-1. !$#cross-references MUID:95224012; PMID:7708713 !$#accession I59360 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-400 ##label RES !'##cross-references GB:L38857; NID:g780313; PIDN:AAA73902.1; !1PID:g780314 GENETICS !$#gene Lhx3 !$#map_position 16.0 CLASSIFICATION #superfamily homeotic protein lim-3; homeobox homology; LIM !1metal-binding repeat homology KEYWORDS DNA binding; duplication; embryo; homeobox; nucleus; !1transcription regulation; zinc FEATURE !$34-84 #domain LIM metal-binding repeat homology #label !8LIM1\ !$93-147 #domain LIM metal-binding repeat homology #label !8LIM2\ !$161-217 #domain homeobox homology #label HOX SUMMARY #length 400 #molecular-weight 44467 #checksum 808 SEQUENCE /// ENTRY I50376 #type complete TITLE homeotic protein lim-3 - chicken ORGANISM #formal_name Gallus gallus #common_name chicken DATE 13-Sep-1996 #sequence_revision 13-Sep-1996 #text_change 16-Jul-1999 ACCESSIONS I50376 REFERENCE A55198 !$#authors Tsuchida, T.; Ensini, M.; Morton, S.B.; Baldassare, M.; !1Edlund, T.; Jessell, T.M.; Pfaff, S.L. !$#journal Cell (1994) 79:957-970 !$#title Topographic organization of embryonic motor neurons defined !1by expression of LIM homeobox genes [see comments]. !$#cross-references MUID:95094281; PMID:7528105 !$#accession I50376 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-395 ##label TSU !'##cross-references GB:L35570; NID:g531184; PIDN:AAA62174.1; !1PID:g531185 GENETICS !$#gene lim-3 CLASSIFICATION #superfamily homeotic protein lim-3; homeobox homology; LIM !1metal-binding repeat homology KEYWORDS DNA binding; duplication; embryo; homeobox; nucleus; !1transcription regulation; zinc FEATURE !$28-78 #domain LIM metal-binding repeat homology #label !8LIM1\ !$87-141 #domain LIM metal-binding repeat homology #label !8LIM2\ !$155-211 #domain homeobox homology #label HOX SUMMARY #length 395 #molecular-weight 43805 #checksum 4995 SEQUENCE /// ENTRY S38821 #type complete TITLE homeotic protein lim-3 - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 27-Jan-1995 #sequence_revision 27-Jan-1995 #text_change 16-Jul-1999 ACCESSIONS S38821; S23805 REFERENCE S38821 !$#authors Taira, M.; Hayes, W.P.; Otani, H.; Dawid, I.B. !$#journal Dev. Biol. (1993) 159:245-256 !$#title Expression of LIM class homeobox gene Xlim-3 in Xenopus !1development is limited to neural and neuroendocrine tissues. !$#cross-references MUID:93374177; PMID:8103491 !$#accession S38821 !'##status preliminary !'##molecule_type mRNA !'##residues 1-395 ##label TAI !'##cross-references EMBL:Z22702; NID:g407071; PIDN:CAA80402.1; !1PID:g407072 REFERENCE S23802 !$#authors Taira, M.; Jamrich, M.; Good, P.J.; Dawid, I.B. !$#journal Genes Dev. (1992) 6:356-366 !$#title The LIM domain-containing homeo box gene Xlim-1 is expressed !1specifically in the organizer region of Xenopus gastrula !1embryos. !$#cross-references MUID:92192449; PMID:1347750 !$#accession S23805 !'##molecule_type mRNA !'##residues 162-173,'D',175-200 ##label TA2 !'##cross-references EMBL:Z11589; NID:g64833; PIDN:CAA77674.1; !1PID:g388552 GENETICS !$#gene lim-3 CLASSIFICATION #superfamily homeotic protein lim-3; homeobox homology; LIM !1metal-binding repeat homology KEYWORDS DNA binding; duplication; embryo; homeobox; nucleus; !1transcription regulation; zinc FEATURE !$28-78 #domain LIM metal-binding repeat homology #label !8LIM1\ !$87-141 #domain LIM metal-binding repeat homology #label !8LIM2\ !$155-211 #domain homeobox homology #label HOX SUMMARY #length 395 #molecular-weight 44031 #checksum 8467 SEQUENCE /// ENTRY S28390 #type complete TITLE homeotic protein mec-3 - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 17-Apr-1993 #sequence_revision 17-Apr-1993 #text_change 16-Jul-1999 ACCESSIONS S28390; A27662 REFERENCE S28390 !$#authors Xue, D.; Finney, M.; Ruvkun, G.; Chalfie, M. !$#journal EMBO J. (1992) 11:4969-4979 !$#title Regulation of the mec-3 gene by the C. elegans homeoproteins !1UNC-86 and MEC-3. !$#cross-references MUID:93099872; PMID:1361171 !$#accession S28390 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-321 ##label XUE !'##cross-references EMBL:L02877; NID:g156488; PIDN:AAA50614.1; !1PID:g156489 REFERENCE A27662 !$#authors Way, J.C.; Chalfie, M. !$#journal Cell (1988) 54:5-16 !$#title mec-3, a homeobox-containing gene that specifies !1differentiation of the touch receptor neurons in C. elegans. !$#cross-references MUID:88253425; PMID:2898300 !$#accession A27662 !'##molecule_type DNA !'##residues 'MPRLHDIWLLT',20,'DLLQESS',28,'ITASSKNSETIIYFQ',44-321 !1##label WAY !'##cross-references GB:M20244; NID:g156363; PIDN:AAA28108.1; !1PID:g156364 GENETICS !$#gene mec-3 !$#introns 82/3; 106/3; 190/3; 228/3; 300/1 CLASSIFICATION #superfamily homeotic protein mec-3; homeobox homology; LIM !1metal-binding repeat homology KEYWORDS DNA binding; duplication; homeobox; nucleus; transcription !1regulation; zinc FEATURE !$29-79 #domain LIM metal-binding repeat homology #label !8LIM1\ !$89-145 #domain LIM metal-binding repeat homology #label !8LIM2\ !$218-274 #domain homeobox homology #label HOX SUMMARY #length 321 #molecular-weight 37088 #checksum 1652 SEQUENCE /// ENTRY A39479 #type complete TITLE homeotic protein mec-3 - Caenorhabditis vulgaris ORGANISM #formal_name Caenorhabditis vulgaris DATE 17-Jul-1992 #sequence_revision 17-Jul-1992 #text_change 16-Jul-1999 ACCESSIONS A39479; S24225 REFERENCE A39479 !$#authors Way, J.C.; Wang, L.; Run, J.Q.; Wang, A. !$#journal Genes Dev. (1991) 5:2199-2211 !$#title The mec-3 gene contains cis-acting elements mediating !1positive and negative regulation in cells produced by !1asymmetric cell division in Caenorhabditis elegans. !$#cross-references MUID:92084094; PMID:1684166 !$#accession A39479 !'##molecule_type DNA !'##residues 1-320 ##label WAY !'##cross-references GB:X63956; NID:g11059; PIDN:CAA45377.1; PID:g11060 !'##note the authors translated the codon CAC for residue 47 as Arg, GCA !1for residue 171 as Ser, AAG for residue 249 as Leu, and CAT !1for residue 295 as Asp !'##note the source is designated as Caenorhabditis vulgarensis GENETICS !$#gene mec-3 !$#introns 26/3; 43/3; 82/3; 106/3; 189/3; 298/3 CLASSIFICATION #superfamily homeotic protein mec-3; homeobox homology; LIM !1metal-binding repeat homology KEYWORDS DNA binding; duplication; homeobox; nucleus; transcription !1regulation; zinc FEATURE !$29-79 #domain LIM metal-binding repeat homology #label !8LIM1\ !$89-145 #domain LIM metal-binding repeat homology #label !8LIM2\ !$217-273 #domain homeobox homology #label HOX SUMMARY #length 320 #molecular-weight 36849 #checksum 9204 SEQUENCE /// ENTRY S29399 #type fragment TITLE homeotic protein mec-3 - Caenorhabditis briggsae (fragment) ORGANISM #formal_name Caenorhabditis briggsae DATE 07-May-1993 #sequence_revision 07-May-1993 #text_change 07-May-1999 ACCESSIONS S29399; S29475 REFERENCE S28390 !$#authors Xue, D.; Finney, M.; Ruvkun, G.; Chalfie, M. !$#journal EMBO J. (1992) 11:4969-4979 !$#title Regulation of the mec-3 gene by the C. elegans homeoproteins !1UNC-86 and MEC-3. !$#cross-references MUID:93099872; PMID:1361171 !$#accession S29399 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-295 ##label XUE1 !'##cross-references EMBL:L02878 REFERENCE S29475 !$#authors Xue, D.; Finney, M.; Ruvkun, G.; Chalfie, M. !$#submission submitted to the EMBL Data Library, September 1992 !$#accession S29475 !'##molecule_type DNA !'##residues 1-39,'F',41-100,'M',102-194,'F',196-215,'PWK',219-220,'R', !1222-228,'N',230-295 ##label XUE2 !'##cross-references EMBL:L02878 GENETICS !$#gene mec-3 !$#introns 26/3; 43/3; 82/2; 106/3; 186/3 CLASSIFICATION #superfamily homeotic protein mec-3; homeobox homology; LIM !1metal-binding repeat homology KEYWORDS DNA binding; duplication; homeobox; nucleus; transcription !1regulation; zinc FEATURE !$29-79 #domain LIM metal-binding repeat homology #label !8LIM1\ !$89-145 #domain LIM metal-binding repeat homology #label !8LIM2\ !$214-270 #domain homeobox homology #label HOX SUMMARY #length 295 #checksum 7071 SEQUENCE /// ENTRY JH0718 #type complete TITLE homeotic protein apterous - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 10-Jun-1993 #sequence_revision 10-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS JH0718; S24568; A42616 REFERENCE JH0718 !$#authors Bourgouin, C.; Lundgren, S.E.; Thomas, J.B. !$#journal Neuron (1992) 9:549-561 !$#title Apterous is a Drosophila LIM domain gene required for the !1development of a subset of embryonic muscles. !$#cross-references MUID:92398973; PMID:1524829 !$#accession JH0718 !'##molecule_type mRNA !'##residues 1-469 ##label BOU !'##cross-references GB:M92841; NID:g157821; PIDN:AAA28673.1; !1PID:g157822 !'##experimental_source embryo REFERENCE S24568 !$#authors Cohen, S.M. !$#submission submitted to the EMBL Data Library, March 1992 !$#accession S24568 !'##status preliminary !'##molecule_type DNA !'##residues 1-469 ##label COH !'##cross-references EMBL:X65158; NID:g7600; PIDN:CAA46276.1; PID:g7601 REFERENCE A42616 !$#authors Cohen, B.; McGuffin, M.E.; Pfeifle, C.; Segal, D.; Cohen, !1S.M. !$#journal Genes Dev. (1992) 6:715-729 !$#title apterous, a gene required for imaginal disc development in !1Drosophila encodes a member of the LIM family of !1developmental regulatory proteins. !$#cross-references MUID:92249766; PMID:1349545 !$#accession A42616 !'##status preliminary !'##molecule_type mRNA !'##residues 1-457,'R',459-469 ##label CO2 !'##cross-references GB:X65158 GENETICS !$#gene FlyBase:ap !'##cross-references FlyBase:FBgn0000099 CLASSIFICATION #superfamily homeotic protein apterous; homeobox homology; !1LIM metal-binding repeat homology KEYWORDS DNA binding; duplication; homeobox; nucleus; transcription !1regulation; zinc FEATURE !$148-200 #domain LIM metal-binding repeat homology #label !8LIM1\ !$210-263 #domain LIM metal-binding repeat homology #label !8LIM2\ !$368-424 #domain homeobox homology #label HOX SUMMARY #length 469 #molecular-weight 52053 #checksum 6108 SEQUENCE /// ENTRY A47179 #type complete TITLE homeotic protein LH-2 - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 21-Sep-1993 #sequence_revision 18-Nov-1994 #text_change 24-Jul-1997 ACCESSIONS A47179 REFERENCE A47179 !$#authors Xu, Y.; Baldassare, M.; Fisher, P.; Rathbun, G.; Oltz, E.M.; !1Yancopoulos, G.D.; Jessell, T.M.; Alt, F.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:227-231 !$#title LH-2: a LIM/homeodomain gene expressed in developing !1lymphocytes and neural cells. !$#cross-references MUID:93126348; PMID:7678338 !$#accession A47179 !'##status preliminary !'##molecule_type mRNA !'##residues 1-426 ##label XU1 !'##cross-references GB:L06804 !'##experimental_source brain !'##note sequence inconsistent with the nucleotide translation !'##note sequence extracted from NCBI backbone (NCBIN:122101, !1NCBIP:122102) CLASSIFICATION #superfamily homeotic protein LH-2; homeobox homology; LIM !1metal-binding repeat homology KEYWORDS DNA binding; duplication; homeobox; nucleus; transcription !1regulation; zinc FEATURE !$52-104 #domain LIM metal-binding repeat homology #label !8LIM1\ !$114-167 #domain LIM metal-binding repeat homology #label !8LIM2\ !$265-321 #domain homeobox homology #label HOX SUMMARY #length 426 #molecular-weight 47416 #checksum 5860 SEQUENCE /// ENTRY BWMSV4 #type complete TITLE Mov-34 protein - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS A40556; B40556 REFERENCE A40556 !$#authors Gridley, T.; Jaenisch, R.; Gendron-Maguire, M. !$#journal Genomics (1991) 11:501-507 !$#title The murine Mov-34 gene: full-length cDNA and genomic !1organization. !$#cross-references MUID:92128931; PMID:1837787 !$#accession A40556 !'##molecule_type DNA !'##residues 1-321 ##label GRI !'##cross-references GB:M64634 !$#accession B40556 !'##molecule_type mRNA !'##residues 1-321 ##label GR2 !'##cross-references GB:M64641; NID:g199770; PIDN:AAA39730.1; !1PID:g199771 COMMENT The function of this protein is unknown but disruption of !1the Mov-34 locus is a recessive embryonic lethal mutation. GENETICS !$#gene Mov-34 !$#map_position 8 !$#introns 25/2; 56/1; 87/1; 119/3; 146/3; 177/2 CLASSIFICATION #superfamily mov-34 protein SUMMARY #length 321 #molecular-weight 36540 #checksum 723 SEQUENCE /// ENTRY JC4154 #type complete TITLE 26S proteasome regulatory chain, p40 - human ALTERNATE_NAMES mov-34 homolog ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS JC4154; PC4037 REFERENCE JC4154 !$#authors Tsurumi, C.; DeMartino, G.N.; Slaughter, C.A.; Shimbara, N.; !1Tanaka, K. !$#journal Biochem. Biophys. Res. Commun. (1995) 210:600-608 !$#title cDNA cloning of p40, a regulatory subunit of the human 26S !1proteasome, and a homolog of the Mov-34 gene product. !$#cross-references MUID:95275316; PMID:7755639 !$#accession JC4154 !'##molecule_type mRNA !'##residues 1-324 ##label TSU !'##cross-references DDBJ:D50063; NID:g971269; PIDN:BAA08780.1; !1PID:g971270 !$#accession PC4037 !'##molecule_type protein !'##residues 35-45;94-100;130-143;154-173;181-199;205-214 ##label TS2 COMMENT This protein is a novel essential regulatory subunit of the !1human 26S proteasome. GENETICS !$#gene GDB:PSMD7; MOV34; P40; S12 !'##cross-references GDB:127564; OMIM:157970 !$#map_position 16q22.2-16q22.2 CLASSIFICATION #superfamily mov-34 protein KEYWORDS proteasome; protein degradation FEATURE !$286-324 #region KEKE motif SUMMARY #length 324 #molecular-weight 37060 #checksum 452 SEQUENCE /// ENTRY BVKWZ1 #type complete TITLE zyg11 protein - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 29-Oct-1999 ACCESSIONS S14908; T19066; S06702 REFERENCE S14908 !$#authors Carter, P.W.; Roos, J.M.; Kemphues, K.J. !$#journal Mol. Gen. Genet. (1990) 221:72-80 !$#title Molecular analysis of zyg-11, a maternal-effect gene !1required for early embryogenesis of Caenorhabditis elegans. !$#cross-references MUID:90220522; PMID:2325632 !$#accession S14908 !'##molecule_type DNA !'##residues 1-799 ##label CAR !'##cross-references EMBL:X16473; NID:g6975; PIDN:CAA34493.1; PID:g6976 REFERENCE Z19069 !$#authors Sims, M. !$#submission submitted to the EMBL Data Library, November 1994 !$#accession T19066 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-799 ##label WIL !'##cross-references EMBL:Z46676; PIDN:CAA86661.1; GSPDB:GN00020; !1CESP:C08B11.1 !'##experimental_source clone C08B11 COMMENT This protein is required for early embryogenesis; one-cell !1embryos lacking it become arrested in meiosis and exhibit !1various other abnormalities. GENETICS !$#gene zyg11 !$#map_position 2 !$#introns 33/1; 112/1; 319/1; 417/2; 627/2; 740/2 CLASSIFICATION #superfamily zyg11 protein KEYWORDS meiosis; phosphoprotein SUMMARY #length 799 #molecular-weight 90779 #checksum 9770 SEQUENCE /// ENTRY UCLQ38 #type complete TITLE cuticle protein 38 - migratory locust ORGANISM #formal_name Locusta migratoria #common_name migratory locust DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 13-Mar-1998 ACCESSIONS A03327; F24802 REFERENCE A03327 !$#authors Hojrup, P.; Andersen, S.O.; Roepstorff, P. !$#journal Biochem. J. (1986) 236:713-720 !$#title Primary structure of a structural protein from the cuticle !1of the migratory locust, Locusta migratoria. !$#cross-references MUID:87075646; PMID:3790088 !$#accession A03327 !'##molecule_type protein !'##residues 1-163 ##label HOJ REFERENCE A91157 !$#authors Hojrup, P.; Andersen, S.O.; Roepstorff, P. !$#journal Eur. J. Biochem. (1986) 154:153-159 !$#cross-references MUID:86108304; PMID:3943519 !$#accession F24802 !'##molecule_type protein !'##residues 1-14,'V',16-30 ##label HO2 COMMENT There are tetrapeptide (A-A-P-A/V) repeats throughout the !1protein. CLASSIFICATION #superfamily cuticle protein 38 KEYWORDS duplication; structural protein FEATURE !$1-163 #product cuticle protein 38 #status experimental !8#label MAT\ !$7-74,75-147 #region duplication SUMMARY #length 163 #molecular-weight 15320 #checksum 7909 SEQUENCE /// ENTRY UCFF1L #type complete TITLE cuticle protein LCP1 precursor - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 18-Dec-1981 #sequence_revision 18-Dec-1981 #text_change 16-Feb-1997 ACCESSIONS A03328 REFERENCE A03328 !$#authors Snyder, M.; Davidson, N. !$#submission submitted to the Atlas, October 1981 !$#accession A03328 !'##molecule_type mRNA !'##residues 1-129 ##label SNY !'##experimental_source larva COMMENT This protein is one of several expressed by a gene cluster !1in epidermal cells of late third instar larvae. GENETICS !$#gene FlyBase:Lcp1 !'##cross-references FlyBase:FBgn0002531 CLASSIFICATION #superfamily cuticle protein LCP1 KEYWORDS structural protein FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-129 #product cuticle protein LCP1 #status predicted !8#label MAT SUMMARY #length 129 #molecular-weight 13818 #checksum 9694 SEQUENCE /// ENTRY UCFFPM #type complete TITLE cuticle protein precursor, pupal - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Feb-1997 ACCESSIONS B24787; S02251 REFERENCE A90876 !$#authors Henikoff, S.; Keene, M.A.; Fechtel, K.; Fristrom, J.W. !$#journal Cell (1986) 44:33-42 !$#title Gene within a gene: nested Drosophila genes encode unrelated !1proteins on opposite DNA strands. !$#cross-references MUID:86079579; PMID:3079672 !$#accession B24787 !'##molecule_type DNA !'##residues 1-184 ##label HEN !'##cross-references GB:J02527 GENETICS !$#gene FlyBase:Pcp !'##cross-references FlyBase:FBgn0003046 !$#map_position 2L 27C !$#introns 4/3 CLASSIFICATION #superfamily cuticle protein LCP1 KEYWORDS structural protein FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-184 #product cuticle protein, pupal #status predicted !8#label MAT SUMMARY #length 184 #molecular-weight 20633 #checksum 4412 SEQUENCE /// ENTRY UCFFPP #type complete TITLE cuticle protein precursor, pupal - fruit fly (Drosophila pseudoobscura) ORGANISM #formal_name Drosophila pseudoobscura DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jul-1999 ACCESSIONS S01205 REFERENCE S01204 !$#authors Henikoff, S.; Eghtedarzadeh, M.K. !$#journal Genetics (1987) 117:711-725 !$#title Conserved arrangement of nested genes at the Drosophila Gart !1locus. !$#cross-references MUID:88112752; PMID:3123310 !$#accession S01205 !'##molecule_type DNA !'##residues 1-192 ##label HEN !'##cross-references EMBL:X06285; NID:g9055; PIDN:CAA29610.1; !1PID:g435017 !'##note the authors translated the codon TTT for residue 20 as Val GENETICS !$#gene FlyBase:Dpse/Pcp !'##cross-references FlyBase:FBgn0012707 !$#map_position 4 88 !$#introns 4/3 CLASSIFICATION #superfamily cuticle protein LCP1 KEYWORDS structural protein FEATURE !$1-12 #domain signal sequence #status predicted #label SIG\ !$13-192 #product cuticle protein, pupal #status predicted !8#label MAT SUMMARY #length 192 #molecular-weight 21524 #checksum 4364 SEQUENCE /// ENTRY S05638 #type complete TITLE cuticle protein 8 - migratory locust ORGANISM #formal_name Locusta migratoria #common_name migratory locust DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Dec-1999 ACCESSIONS S05638; B24802 REFERENCE S05638 !$#authors Klarskov, K.; Hojrup, P.; Andersen, S.O.; Roepstorff, P. !$#journal Biochem. J. (1989) 262:923-930 !$#title Plasma-desorption mass spectrometry as an aid in protein !1sequence determination. Application of the method on a !1cuticular protein from the migratory locust (Locusta !1migratoria). !$#cross-references MUID:90073593; PMID:2590176 !$#accession S05638 !'##molecule_type protein !'##residues 1-148 ##label KLA REFERENCE A91157 !$#authors Hojrup, P.; Andersen, S.O.; Roepstorff, P. !$#journal Eur. J. Biochem. (1986) 154:153-159 !$#cross-references MUID:86108304; PMID:3943519 !$#accession B24802 !'##molecule_type protein !'##residues 1-53,'X',55-56 ##label HOJ CLASSIFICATION #superfamily migratory locust cuticle protein 8 KEYWORDS structural protein FEATURE !$16-19 #region 4-residue repeat (A-A-P-[AV])\ !$22-25 #region 4-residue repeat (A-A-P-[AV])\ !$28-31 #region 4-residue repeat (A-A-P-[AV])\ !$37-40 #region 4-residue repeat (A-A-P-[AV])\ !$44-47 #region 4-residue repeat (A-A-P-[AV]) SUMMARY #length 148 #molecular-weight 15224 #checksum 3784 SEQUENCE /// ENTRY GSFF3 #type complete TITLE salivary glue protein sgs-3 - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 16-Jul-1999 ACCESSIONS A03329 REFERENCE A92904 !$#authors Garfinkel, M.D.; Pruitt, R.E.; Meyerowitz, E.M. !$#journal J. Mol. Biol. (1983) 168:765-789 !$#title DNA sequences, gene regulation and modular protein evolution !1in the Drosophila 68C glue gene cluster. !$#cross-references MUID:83294545; PMID:6411930 !$#accession A03329 !'##molecule_type DNA !'##residues 1-307 ##label GAR !'##cross-references GB:X01918; NID:g8581; PIDN:CAA25994.1; PID:g603989 COMMENT This protein is produced by third-instar larvae. GENETICS !$#gene sgs-3 !'##cross-references FlyBase:FBgn0003373 !$#map_position 3L (68C) !$#introns 10/1 CLASSIFICATION #superfamily salivary glue protein KEYWORDS salivary gland; tandem repeat SUMMARY #length 307 #molecular-weight 32196 #checksum 3175 SEQUENCE /// ENTRY GSFF7 #type complete TITLE salivary glue protein sgs-7 - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 16-Jul-1999 ACCESSIONS A03330 REFERENCE A92904 !$#authors Garfinkel, M.D.; Pruitt, R.E.; Meyerowitz, E.M. !$#journal J. Mol. Biol. (1983) 168:765-789 !$#title DNA sequences, gene regulation and modular protein evolution !1in the Drosophila 68C glue gene cluster. !$#cross-references MUID:83294545; PMID:6411930 !$#accession A03330 !'##molecule_type DNA !'##residues 1-74 ##label GAR !'##cross-references GB:X01918; NID:g8581; PIDN:CAA25993.1; PID:g603988 COMMENT This protein is produced by third-instar larvae. GENETICS !$#gene sgs-7 !'##cross-references FlyBase:FBgn0003377 !$#map_position 3L (68C) !$#introns 10/1 CLASSIFICATION #superfamily salivary glue protein KEYWORDS salivary gland SUMMARY #length 74 #molecular-weight 7919 #checksum 4350 SEQUENCE /// ENTRY GSFF8 #type complete TITLE salivary glue protein sgs-8 - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 16-Feb-1997 ACCESSIONS A03331 REFERENCE A92904 !$#authors Garfinkel, M.D.; Pruitt, R.E.; Meyerowitz, E.M. !$#journal J. Mol. Biol. (1983) 168:765-789 !$#title DNA sequences, gene regulation and modular protein evolution !1in the Drosophila 68C glue gene cluster. !$#cross-references MUID:83294545; PMID:6411930 !$#accession A03331 !'##molecule_type DNA !'##residues 1-75 ##label GAR COMMENT This protein is produced by third-instar larvae. GENETICS !$#gene sgs-8 !'##cross-references FlyBase:FBgn0003378 !$#map_position 3L (68C) !$#introns 10/1 CLASSIFICATION #superfamily salivary glue protein KEYWORDS salivary gland SUMMARY #length 75 #molecular-weight 7917 #checksum 5454 SEQUENCE /// ENTRY VJFF1 #type complete TITLE vitellogenin I precursor - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 06-Apr-1982 #sequence_revision 06-Apr-1982 #text_change 16-Jul-1999 ACCESSIONS A93744; A93738; A03332 REFERENCE A93744 !$#authors Hung, M.C.; Wensink, P.C. !$#journal Nucleic Acids Res. (1981) 9:6407-6419 !$#title The sequence of the Drosophila melanogaster gene for yolk !1protein 1. !$#cross-references MUID:82105554; PMID:6275360 !$#accession A93744 !'##molecule_type DNA !'##residues 1-439 ##label HUN REFERENCE A93738 !$#authors Hovemann, B.; Galler, R.; Walldorf, U.; Kupper, H.; Bautz, !1E.K.F. !$#journal Nucleic Acids Res. (1981) 9:4721-4734 !$#title Vitellogenin in Drosophila melanogaster: sequence of the !1yolk protein I gene and its flanking regions. !$#cross-references MUID:82059495; PMID:6272212 !$#accession A93738 !'##molecule_type DNA !'##residues 1-439 ##label HOV !'##cross-references GB:V00248; NID:g8839; PIDN:CAA23502.1; PID:g8840 !'##experimental_source strain Canton S GENETICS !$#gene ypI !'##cross-references FlyBase:FBgn0004045 !$#map_position 1,29 (9A1-9B1) CLASSIFICATION #superfamily insect vitellogenin KEYWORDS egg yolk; glycoprotein; phosphoprotein; sulfoprotein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-439 #product vitellogenin I #status predicted #label MAT SUMMARY #length 439 #molecular-weight 48711 #checksum 7946 SEQUENCE /// ENTRY VJFF2 #type complete TITLE vitellogenin II precursor - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES yolk protein 2 ORGANISM #formal_name Drosophila melanogaster DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 05-Sep-1997 ACCESSIONS A03333; A31980 REFERENCE A03333 !$#authors Hung, M.C.; Wensink, P.C. !$#journal J. Mol. Biol. (1983) 164:481-492 !$#title Sequence and structure conservation in yolk proteins and !1their genes. !$#cross-references MUID:83189120; PMID:6405043 !$#accession A03333 !'##molecule_type DNA !'##residues 1-442 ##label HUN REFERENCE A31980 !$#authors Baeuerle, P.A.; Lottspeich, F.; Huttner, W.B. !$#journal J. Biol. Chem. (1988) 263:14925-14929 !$#title Purification of yolk protein 2 of Drosophila melanogaster !1and identification of its site of tyrosine sulfation. !$#cross-references MUID:89008370; PMID:3139663 !$#accession A31980 !'##molecule_type protein !'##residues 162-191 ##label BAE !'##note Tyr-172 is sulfated stoichiometrically, and exclusively GENETICS !$#gene ypII !'##cross-references FlyBase:FBgn0005391 !$#map_position 1,29 (9A1-9B1) CLASSIFICATION #superfamily insect vitellogenin KEYWORDS glycoprotein; phosphoprotein; sulfoprotein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-442 #product vitellogenin II #status predicted #label !8MAT\ !$25 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$172 #binding_site sulfate (Tyr) (covalent) #status !8experimental SUMMARY #length 442 #molecular-weight 49678 #checksum 2099 SEQUENCE /// ENTRY S27772 #type complete TITLE vitellogenin precursor - boll weevil ORGANISM #formal_name Anthonomus grandis #common_name boll weevil DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S27772 REFERENCE S27772 !$#authors Trewitt, P.M.; Heilmann, L.J.; Kumaran, A.K. !$#submission submitted to the EMBL Data Library, October 1991 !$#description Nucleotide sequence and structure of the vitellogenin gene !1from the boll weevil, Anthonomus grandis. !$#accession S27772 !'##molecule_type DNA !'##residues 1-1790 ##label TRE !'##cross-references EMBL:M72980; NID:g155707; PIDN:AAA27740.1; !1PID:g155708 GENETICS !$#introns 11/1; 678/3; 744/2; 845/2; 902/1; 1466/1 CLASSIFICATION #superfamily boll weevil vitellogenin FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-1790 #product vitellogenin #status predicted #label MAT SUMMARY #length 1790 #molecular-weight 205857 #checksum 2621 SEQUENCE /// ENTRY VJCH2 #type complete TITLE vitellogenin II precursor [validated] - chicken CONTAINS 40K yolk glycoprotein; lipovitellin; phosvitin ORGANISM #formal_name Gallus gallus #common_name chicken DATE 28-Aug-1985 #sequence_revision 18-Aug-2000 #text_change 18-Aug-2000 ACCESSIONS I50441; S55680; A92941; A93502; C29184; I50440; S07788; !1E23876; A03335; A23177; A27869 REFERENCE I50441 !$#authors Nardelli, D.; van het Schip, F.D.; Gerber-Huber, S.; !1Haefliger, J. !$#journal J. Biol. Chem. (1987) 262:15377-15385 !$#title Comparison of the organization and fine structure of a !1chicken and a Xenopus laevis vitellogenin gene. !$#cross-references MUID:88058863; PMID:3680202 !$#accession I50441 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-1852 ##label NAR !'##cross-references GB:M18060; NID:g212880; PIDN:AAA49139.1; !1PID:g212881 REFERENCE S55680 !$#authors Yamamura, J.; Adachi, T.; Aoki, N.; Nakajima, H.; Nakamura, !1R.; Matsuda, T. !$#journal Biochim. Biophys. Acta (1995) 1244:384-394 !$#title Precursor-product relationship between chicken vitellogenin !1and the yolk proteins: the 40 kDa yolk plasma glycoprotein !1is derived from the C-terminal cysteine-rich domain of !1vitellogenin II. !$#cross-references MUID:95322425; PMID:7599159 !$#accession S55680 !'##status preliminary !'##molecule_type protein !'##residues 1569-1582 ##label YAM REFERENCE A92941 !$#authors van het Schip, F.D.; Samallo, J.; Broos, J.; Ophuis, J.; !1Mojet, M.; Gruber, M.; AB, G. !$#journal J. Mol. Biol. (1987) 196:245-260 !$#title Nucleotide sequence of a chicken vitellogenin gene and !1derived amino acid sequence of the encoded yolk precursor !1protein. !$#cross-references MUID:88011328; PMID:3477646 !$#accession A92941 !'##molecule_type DNA !'##residues 1-579,582-774,'R',776-1138,'S',1140-1437,'HK',1440-1852 !1##label VAN !'##cross-references GB:X13607; NID:g63886; PIDN:CAA31942.1; PID:g63887 !'##note 1842-Ala was also found REFERENCE A93502 !$#authors Burch, J.B.E. !$#journal Nucleic Acids Res. (1984) 12:1117-1135 !$#title Identification and sequence analysis of the 5' end of the !1major chicken vitellogenin gene. !$#cross-references MUID:84118805; PMID:6694908 !$#accession A93502 !'##molecule_type DNA !'##residues 1-71 ##label BUR !'##cross-references GB:X00345; NID:g63872; PIDN:CAA25096.1; PID:g63873 REFERENCE A91754 !$#authors Clark, R.C. !$#journal Int. J. Biochem. (1985) 17:983-988 !$#title The primary structure of avian phosvitins. Contributions !1through the Edman degradation of methylmercaptovitins !1prepared from the constituent phosphoproteins. !$#cross-references MUID:86056531; PMID:4065410 !$#accession C29184 !'##molecule_type protein !'##residues 1114-1138,'S',1140-1190 ##label CLA REFERENCE I50440 !$#authors Byrne, B.M.; van Het Schip, A.D.; van de Klundert, J.A. !$#journal Biochemistry (1984) 23:4275-4279 !$#title Amino acid sequence of phosvitin derived from the nucleotide !1sequence of part of the chicken vitellogenin gene. !$#cross-references MUID:85023316; PMID:6091745 !$#accession I50440 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1094-1138,'S',1140-1340 ##label BYR !'##cross-references GB:K02113; NID:g212878; PIDN:AAA98791.1; !1PID:g212879 REFERENCE S07788 !$#authors Philipsen, J.N.J.; de Vries, J.E.; Samallo, J.; van Dijk, !1C.; Arnberg, A.C.; AB, G. !$#journal J. Mol. Evol. (1989) 28:185-190 !$#title Characterization of a polymorphism in the 3' part of the !1chicken vitellogenin gene. !$#cross-references MUID:89178745; PMID:2494348 !$#accession S07788 !'##status translation not shown !'##molecule_type DNA !'##residues 1707-1759 ##label ABG !'##cross-references EMBL:X14729; NID:g63881; PIDN:CAA32851.1; !1PID:g1334751 !'##note the source is designated as Gallus domesticus REFERENCE A23876 !$#authors Walker, P.; Brown-Luedi, M.; Germond, J.E.; Wahli, W.; !1Meijlink, F.C.P.W.; van het Schip, A.D.; Roelink, H.; !1Gruber, M.; Ab, G. !$#journal EMBO J. (1983) 2:2271-2279 !$#title Sequence homologies within the 5' end region of the !1estrogen-controlled d vitellogenin gene in Xenopus and !1chicken. !$#cross-references MUID:84131940; PMID:6199194 !$#accession E23876 !'##status preliminary !'##molecule_type DNA !'##residues 1-71 ##label WAL COMMENT Vitellogenin is synthesized in the liver of oviparous !1vertebrates in response to steroid (estrogen) induction. COMMENT Phosvitin, an egg yolk storage protein, is one of the most !1highly phosphorylated (10%) proteins in nature. GENETICS !$#gene VtgII !$#introns 14/1; 21/1; 71/3; 155/3; 209/3; 259/2; 309/3; 362/2; 417/3; !1459/3; 532/3; 607/2; 640/1; 681/3; 715/3; 755/3; 819/1; 850/ !12; 912/2; 960/3; 1035/1; 1093/3; 1323/3; 1340/3; 1370/3; !11441/3; 1489/2; 1535/3; 1581/1; 1643/2; 1674/1; 1706/3; !11760/1; 1814/1 CLASSIFICATION #superfamily vitellogenin KEYWORDS egg yolk; glycoprotein; liver; phosphoprotein FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$1114-1330 #product phosvitin B #status experimental #label MPT\ !$1125,1126,1127, !$1128,1129,1130, !$1132,1133,1137, !$1138,1140,1141, !$1142,1144,1145, !$1169,1170,1171, !$1172,1174,1175, !$1177,1178,1180, !$1181,1184,1185, !$1186,1188,1189 #binding_site phosphate (Ser) (covalent) #status !8experimental\ !$1191,1192,1195, !$1196,1197,1198, !$1199,1200,1201, !$1202,1203,1204, !$1205,1206,1208, !$1209,1210,1211, !$1212,1213,1214, !$1215,1216,1217, !$1219,1221,1222, !$1223,1224,1225, !$1226,1228,1229, !$1230,1231,1232, !$1233,1235,1237, !$1238,1239,1241, !$1242,1243,1244, !$1245,1246,1247, !$1248,1249,1250, !$1251,1252,1253, !$1254,1256,1257, !$1258,1259,1261, !$1262,1263,1264, !$1265,1266,1268, !$1269,1270,1273, !$1275,1278,1284, !$1285,1286,1287, !$1288,1289,1290, !$1291,1293,1295,1298 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$1282 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$1303,1310,1311, !$1312,1313,1314, !$1315,1316,1317 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 1852 #molecular-weight 204936 #checksum 5344 SEQUENCE /// ENTRY VJKW5 #type complete TITLE vitellogenin vit-5 precursor - Caenorhabditis elegans ALTERNATE_NAMES vitellogenin yp170A ORGANISM #formal_name Caenorhabditis elegans DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 01-Dec-2000 ACCESSIONS A03334; C27271; B93576; T15409 REFERENCE A03334 !$#authors Spieth, J.; Denison, K.; Zucker, E.; Blumenthal, T. !$#journal Nucleic Acids Res. (1985) 13:7129-7138 !$#title The nucleotide sequence of a nematode vitellogenin gene. !$#cross-references MUID:86041902; PMID:3855245 !$#accession A03334 !'##molecule_type DNA !'##residues 1-1603 ##label SPI1 !'##cross-references GB:X03044; NID:g6919; PIDN:CAA26849.1; PID:g6920 !'##note the authors translated the codon TTT for residue 1318 as Thr REFERENCE A93067 !$#authors Spieth, J.; Blumenthal, T. !$#journal Mol. Cell. Biol. (1985) 5:2495-2501 !$#title The Caenorhabditis elegans vitellogenin gene family includes !1a gene encoding a distantly related protein. !$#cross-references MUID:86284606; PMID:3841791 !$#accession C27271 !'##molecule_type DNA !'##residues 1-99 ##label SPI2 !'##cross-references GB:M11497 REFERENCE A93576 !$#authors Spieth, J.; Denison, K.; Kirtland, S.; Cane, J.; Blumenthal, !1T. !$#journal Nucleic Acids Res. (1985) 13:5283-5295 !$#title The C. elegans vitellogenin genes: short sequence repeats in !1the promoter regions and homology to the vertebrate genes. !$#cross-references MUID:85269643; PMID:4022780 !$#accession B93576 !'##molecule_type DNA !'##residues 1-71 ##label SPI3 !'##cross-references GB:X02755 REFERENCE Z18346 !$#authors Nhan, M. !$#submission submitted to the EMBL Data Library, December 1995 !$#description The sequence of C. elegans cosmid C04F6. !$#accession T15409 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-44,'A',46-168,'L',170-182,'EVAYT',188-390,'TL',393-613, !1'N',615-688,'F',690-882,'RFW',886-1263,'YMNMTI',1270-1280, !1'V',1282-1318,'D',1320-1475,'V',1477,'N',1479-1516,'K', !11518-1564,'SKNAR',1570-1572,'KEAR',1577-1603 ##label NHA !'##cross-references EMBL:U42835; NID:g1125760; PID:g1125763; !1PIDN:AAA83587.1; CESP:vit-5 COMMENT In Caenorhabditis, vitellogenins are synthesized by 32 cells !1building the intestine of adult hermaphroditic individuals; !1they are cotranslationally secreted into the body cavity and !1subsequently taken up by the gonad. Vitellogenin 5 undergoes !1little if any processing before being packaged into yolk !1platelets. GENETICS !$#gene CESP:vit-5 !$#introns 288/3; 383/3; 1396/2; 1472/3; 1518/1 CLASSIFICATION #superfamily vitellogenin KEYWORDS egg yolk; glycoprotein; intestine; oocyte FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-1603 #product vitellogenin vit-5 #status predicted #label !8MAT\ !$602,812,1052 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1603 #molecular-weight 186443 #checksum 7339 SEQUENCE /// ENTRY JAAO92 #type fragment TITLE chorion class A protein pc292 precursor - polyphemus moth (fragment) ORGANISM #formal_name Antheraea polyphemus #common_name polyphemus moth DATE 31-Aug-1980 #sequence_revision 31-Aug-1980 #text_change 15-Oct-1999 ACCESSIONS A03336 REFERENCE A03336 !$#authors Tsitilou, S.G.; Regier, J.C.; Kafatos, F.C. !$#journal Nucleic Acids Res. (1980) 8:1987-1997 !$#title Selection and sequence analysis of a cDNA clone encoding a !1known chorion protein of the A family. !$#cross-references MUID:81053859; PMID:7433133 !$#accession A03336 !'##molecule_type mRNA !'##residues 1-119 ##label TSI !'##cross-references GB:V00078; NID:g5632; PIDN:CAA23420.1; PID:g5633 !'##note partial direct sequencing of the protein revealed one !1difference from the above, Leu at position 118, probably due !1to polymorphism CLASSIFICATION #superfamily chorion class A protein pc292 KEYWORDS egg shell; structural protein FEATURE !$1-6 #domain signal sequence (fragment) #status predicted !8#label SIG\ !$7-119 #product chorion class A protein pc292 #status !8predicted #label MAT SUMMARY #length 119 #checksum 4568 SEQUENCE /// ENTRY JBAO41 #type complete TITLE chorion class B protein pc401 precursor - polyphemus moth ORGANISM #formal_name Antheraea polyphemus #common_name polyphemus moth DATE 28-Feb-1980 #sequence_revision 28-Feb-1980 #text_change 15-Oct-1999 ACCESSIONS A03337 REFERENCE A90786 !$#authors Jones, C.W.; Rosenthal, N.; Rodakis, G.C.; Kafatos, F.C. !$#journal Cell (1979) 18:1317-1332 !$#title Evolution of two major chorion multigene families as !1inferred from cloned cDNA and protein sequences. !$#cross-references MUID:80090072; PMID:519771 !$#accession A03337 !'##molecule_type mRNA !'##residues 1-171 ##label JON !'##cross-references GB:V00077; GB:J01162; NID:g5630; PIDN:CAA23419.1; !1PID:g5631 COMMENT This protein is one of many from the eggshell of the !1polyphemus moth. CLASSIFICATION #superfamily chorion class A protein pc292 KEYWORDS egg shell; structural protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-171 #product chorion class B protein pc401 #status !8predicted #label MAT SUMMARY #length 171 #molecular-weight 16081 #checksum 9895 SEQUENCE /// ENTRY JBAO10 #type complete TITLE chorion class B protein pc10 - polyphemus moth ORGANISM #formal_name Antheraea polyphemus #common_name polyphemus moth DATE 28-Feb-1980 #sequence_revision 28-Feb-1980 #text_change 15-Oct-1999 ACCESSIONS A03338 REFERENCE A90786 !$#authors Jones, C.W.; Rosenthal, N.; Rodakis, G.C.; Kafatos, F.C. !$#journal Cell (1979) 18:1317-1332 !$#title Evolution of two major chorion multigene families as !1inferred from cloned cDNA and protein sequences. !$#cross-references MUID:80090072; PMID:519771 !$#accession A03338 !'##molecule_type mRNA !'##residues 1-130 ##label JON !'##cross-references GB:J01161; NID:g155833; PIDN:AAA27781.1; !1PID:g155834 COMMENT This protein is one of many from the eggshell of the !1polyphemus moth. CLASSIFICATION #superfamily chorion class A protein pc292 KEYWORDS egg shell; structural protein FEATURE !$1-130 #product chorion class B protein pc10 (fragment) !8#status predicted #label MAT SUMMARY #length 130 #molecular-weight 12084 #checksum 4707 SEQUENCE /// ENTRY EMAOE1 #type complete TITLE E1 protein precursor - polyphemus moth ORGANISM #formal_name Antheraea polyphemus #common_name polyphemus moth DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 16-Jul-1999 ACCESSIONS A25163 REFERENCE A25163 !$#authors Regier, J.C.; Pacholski, P. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:6035-6039 !$#title Nucleotide sequence of an unusual regionally expressed !1silkmoth chorion RNA: predicted primary and secondary !1structures of an architectural protein. !$#cross-references MUID:85298291; PMID:3862116 !$#accession A25163 !'##molecule_type mRNA !'##residues 1-169 ##label REG !'##cross-references GB:M10789; NID:g155848; PIDN:AAB59217.1; !1PID:g155849 !'##note the exact signal sequence was not determined !'##note 34-Asn and 46-Cys were also found COMMENT This protein is produced during the very late period of !1choriogenesis by follicle cells in the aeropyle crown !1region. With the E2 protein, it forms a spongy material !1called "filler". CLASSIFICATION #superfamily silkworm E1 protein KEYWORDS choriogenesis; duplication FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-169 #product E1 protein #status predicted #label E1P\ !$114-127,128-141 #region duplication SUMMARY #length 169 #molecular-weight 17360 #checksum 1156 SEQUENCE /// ENTRY A39638 #type complete TITLE plectin - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A39638; S21876 REFERENCE A39638 !$#authors Wiche, G.; Becker, B.; Luber, K.; Weitzer, G.; Castanon, !1M.J.; Hauptmann, R.; Stratowa, C.; Stewart, M. !$#journal J. Cell Biol. (1991) 114:83-99 !$#title Cloning and sequencing of rat plectin indicates a 466-kD !1polypeptide chain with a three-domain structure based on a !1central alpha-helical coiled coil. !$#cross-references MUID:91268156; PMID:2050743 !$#accession A39638 !'##status preliminary !'##molecule_type mRNA !'##residues 1-4687 ##label WIC !'##cross-references EMBL:X59601; NID:g1292885; PIDN:CAA42169.1; !1PID:g1561642 CLASSIFICATION #superfamily plectin; alpha-actinin actin-binding domain !1homology; ribosomal protein S10 homology KEYWORDS cytoskeleton; transmembrane protein FEATURE !$6-103 #domain ribosomal protein S10 homology #label RS10\ !$184-399 #domain alpha-actinin actin-binding domain homology !8#label ACT SUMMARY #length 4687 #molecular-weight 533535 #checksum 3612 SEQUENCE /// ENTRY WSHB #type complete TITLE secapin precursor - honeybee ORGANISM #formal_name Apis mellifera #common_name honeybee DATE 31-May-1979 #sequence_revision 28-May-1986 #text_change 02-May-1994 ACCESSIONS A91139; A91253; A03341 REFERENCE A91139 !$#authors Vlasak, R.; Kreil, G. !$#journal Eur. J. Biochem. (1984) 145:279-282 !$#title Nucleotide sequence of cloned cDNAs coding for !1preprosecapin, a major product of queen-bee venom glands. !$#cross-references MUID:85051353; PMID:6548708 !$#accession A91139 !'##molecule_type mRNA !'##residues 1-77 ##label VLA REFERENCE A91253 !$#authors Gauldie, J.; Hanson, J.M.; Shipolini, R.A.; Vernon, C.A. !$#journal Eur. J. Biochem. (1978) 83:405-410 !$#title The structures of some peptides from bee venom. !$#cross-references MUID:78126868; PMID:631126 !$#accession A91253 !'##molecule_type protein !'##residues 53-74,77 ##label GAU COMMENT Secapin is a basic, nontoxic component of honeybee venom. CLASSIFICATION #superfamily secapin KEYWORDS venom FEATURE !$1-32 #domain signal sequence #status predicted #label SIG\ !$53-77 #product secapin #status experimental #label SCP\ !$61-72 #disulfide_bonds #status experimental SUMMARY #length 77 #molecular-weight 8689 #checksum 2977 SEQUENCE /// ENTRY PJBYS #type complete TITLE cold shock protein TIR1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES 25K protein; protein YER011w; serine-rich protein SRP1 ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 23-Mar-2001 ACCESSIONS S05803; S50469 REFERENCE S05803 !$#authors Marguet, D.; Guo, X.J.; Lauquin, G.J.M. !$#journal J. Mol. Biol. (1988) 202:455-470 !$#title Yeast gene SRP1 (serine-rich protein). Intragenic repeat !1structure and identification of a family of SRP1-related DNA !1sequences. !$#cross-references MUID:89011972; PMID:3139887 !$#accession S05803 !'##molecule_type DNA !'##residues 1-254 ##label MAR !'##cross-references EMBL:X12775; NID:g4539; PIDN:CAA31262.1; PID:g4540 REFERENCE S50433 !$#authors Dietrich, F.S. !$#submission submitted to the EMBL Data Library, December 1994 !$#description The sequence of S. cerevisiae cosmids 9537, 9581, 9495, !19867, and lambda clone 5898. !$#accession S50469 !'##molecule_type DNA !'##residues 1-254 ##label DIE !'##cross-references EMBL:U18778; NID:g603592; PIDN:AAB64544.1; !1PID:g603603; GSPDB:GN00005; MIPS:YER011w GENETICS !$#gene SGD:TIR1; SRP1; MIPS:YER011w !'##cross-references SGD:S0000813; MIPS:YER011w !$#map_position 5R CLASSIFICATION #superfamily serine-rich protein KEYWORDS cell wall; tandem repeat; transmembrane protein FEATURE !$114-209 #region 12-residue repeats\ !$238-254 #domain transmembrane #status predicted #label TMM SUMMARY #length 254 #molecular-weight 24906 #checksum 2927 SEQUENCE /// ENTRY S17936 #type complete TITLE oleosin (clone P24/91) - soybean ORGANISM #formal_name Glycine max #common_name soybean DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S17936; S18749 REFERENCE S17935 !$#authors Kalinski, A.; Loer, D.S.; Weisemann, J.M.; Matthews, B.F.; !1Herman, E.M. !$#journal Plant Mol. Biol. (1991) 17:1095-1098 !$#title Isoforms of soybean seed oil body membrane protein 24 kDa !1oleosin are encoded by closely related cDNAs. !$#cross-references MUID:92032770; PMID:1932682 !$#accession S17936 !'##molecule_type mRNA !'##residues 1-223 ##label KAL !'##cross-references EMBL:X60773; NID:g944829; PIDN:CAA43183.1; !1PID:g944830 REFERENCE S18749 !$#authors Herman, E.M. !$#submission submitted to the EMBL Data Library, July 1991 !$#accession S18749 !'##molecule_type mRNA !'##residues 1-24;26-223 ##label HER !'##cross-references EMBL:X60773 CLASSIFICATION #superfamily oleosin KEYWORDS seed; tandem repeat FEATURE !$158-171 #region 7-residue repeats\ !$183-204 #region 11-residue repeats SUMMARY #length 223 #molecular-weight 23392 #checksum 1051 SEQUENCE /// ENTRY JQ0986 #type complete TITLE lipid body-associated membrane protein - carrot ORGANISM #formal_name Daucus carota #common_name carrot DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JQ0986 REFERENCE JQ0986 !$#authors Hatzopoulos, P.; Franz, G.; Choy, L.; Sung, R.Z. !$#journal Plant Cell (1990) 2:457-467 !$#title Interaction of nuclear factors with upstream sequences of a !1lipid body membrane protein gene from carrot. !$#cross-references MUID:93044488; PMID:2152171 !$#accession JQ0986 !'##molecule_type DNA !'##residues 1-180 ##label HAT !'##cross-references GB:S47635; NID:g259452; PIDN:AAB24078.1; !1PID:g259453 !'##experimental_source var. juwarot GENETICS !$#gene DC59 CLASSIFICATION #superfamily oleosin KEYWORDS membrane protein SUMMARY #length 180 #molecular-weight 18779 #checksum 4657 SEQUENCE /// ENTRY S22475 #type complete TITLE oleosin BN-III - rape ORGANISM #formal_name Brassica napus #common_name rape DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S22475; S17082 REFERENCE S22475 !$#authors Keddie, J.S.; Huebner, G.; Slocombe, S.P.; Jarvis, R.P.; !1Cummins, I.; Edwards, E.; Shaw, C.H.; Murphy, D.J. !$#journal Plant Mol. Biol. (1992) 19:443-453 !$#title Cloning and characterisation of an oleosin gene from !1Brassica napus. !$#cross-references MUID:92322976; PMID:1377966 !$#accession S22475 !'##molecule_type DNA !'##residues 1-195 ##label KED !'##cross-references EMBL:X61937; NID:g17838; PIDN:CAA43941.1; !1PID:g17839 !'##note the authors did not translate the codon AAG for residues 132 GENETICS !$#introns 132/2 CLASSIFICATION #superfamily oleosin SUMMARY #length 195 #molecular-weight 21540 #checksum 6737 SEQUENCE /// ENTRY S22538 #type complete TITLE oleosin, 18.5K - Arabidopsis thaliana ALTERNATE_NAMES protein F13M23.280 ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S22538; T05535; S22143 REFERENCE S22538 !$#authors van Rooijen, G.J.H.; Terning, L.I.; Moloney, M.M. !$#journal Plant Mol. Biol. (1992) 18:1177-1179 !$#title Nucleotide sequence of an Arabidopsis thaliana oleosin gene. !$#cross-references MUID:92288310; PMID:1600152 !$#accession S22538 !'##molecule_type DNA !'##residues 1-173 ##label ROO !'##cross-references EMBL:X62353; NID:g16404; PIDN:CAA44225.1; !1PID:g16405 !'##experimental_source cv. Columbia REFERENCE Z15419 !$#authors Bevan, M.; Wedler, H.; Wedler, E.; Wambutt, R.; Hoheisel, !1J.; Mewes, H.W.; Mayer, K.F.X.; Schueller, C. !$#submission submitted to the Protein Sequence Database, February 1999 !$#accession T05535 !'##molecule_type DNA !'##residues 1-173 ##label BEV !'##cross-references EMBL:AL035523 !'##experimental_source cultivar Columbia; BAC clone F13M23 GENETICS !$#map_position 4 !$#introns 118/2 !$#note F13M23.280 CLASSIFICATION #superfamily oleosin KEYWORDS seed SUMMARY #length 173 #molecular-weight 18569 #checksum 6991 SEQUENCE /// ENTRY S16262 #type complete TITLE auxin-binding protein precursor - maize ORGANISM #formal_name Zea mays #common_name maize DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jul-1999 ACCESSIONS S16262; A43033; S05387; A43034; S05388; A32559; B32559 REFERENCE S16262 !$#authors Yu, L.X.; Lazarus, C.M. !$#journal Plant Mol. Biol. (1991) 16:925-930 !$#title Structure and sequence of an auxin-binding protein gene from !1maize (Zea mays L.). !$#cross-references MUID:91316232; PMID:1650260 !$#accession S16262 !'##molecule_type DNA !'##residues 1-201 ##label YUA !'##cross-references EMBL:X56737; NID:g22174; PIDN:CAA40061.1; !1PID:g22175 !'##experimental_source clone lambda AuxIII REFERENCE A43033 !$#authors Schwob, E.; Choi, S.Y.; Simmons, C.; Migliaccio, F.; Illag, !1L.; Hesse, T.; Palme, K.; Soll, D. !$#submission submitted to GenBank, February 1993 !$#description Molecular analysis of three maize 22 kDa auxin binding !1protein genes - transient promoter expression and regulatory !1regions. !$#accession A43033 !'##molecule_type DNA !'##residues 1-12,'G',14-201 ##label SCH REFERENCE S05387 !$#authors Hesse, T.; Feldwisch, J.; Balshuesemann, D.; Bauw, G.; !1Puype, M.; Vandekerckhove, J.; Loebler, M.; Klaembt, D.; !1Schell, J.; Palme, K. !$#journal EMBO J. (1989) 8:2453-2461 !$#title Molecular cloning and structural analysis of a gene from Zea !1mays (L.) coding for a putative receptor for the plant !1hormone auxin. !$#cross-references MUID:90060001; PMID:2555179 !$#accession S05387 !'##molecule_type mRNA !'##residues 1-201 ##label HES !'##cross-references EMBL:X16309; NID:g22106; PIDN:CAA34376.1; !1PID:g22107 !$#accession A43034 !'##molecule_type protein !'##residues 39-67;78-91;110-119;185-194 ##label HE2 !'##note two minor components, totaling less than 5% of the major !1component, were found; their amino-terminal sequences, !1corresponding to residues 39-67, were determined and 41-Pro, !154-Gln, 57-Asn, 60-Gly and 63-Phe were found REFERENCE S05388 !$#authors Tillmann, U.; Viola, G.; Kayser, B.; Siemeister, G.; Hesse, !1T.; Palme, K.; Loebler, M.; Klaembt, D. !$#journal EMBO J. (1989) 8:2463-2467 !$#title cDNA clones of the auxin-binding protein from corn !1coleoptiles (Zea mays L.): isolation and characterization by !1immunological methods. !$#cross-references MUID:90060002; PMID:2555180 !$#accession S05388 !'##molecule_type mRNA !'##residues 1-201 ##label TIL !'##cross-references EMBL:X16308; NID:g22108; PIDN:CAA34375.1; !1PID:g22109 !'##note immunological evidence indicated that one form of this protein !1lacks the carboxyl-terminal KDEL and may be secreted REFERENCE A32559 !$#authors Inohara, N.; Shimomura, S.; Fukui, T.; Futai, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:3564-3568 !$#title Auxin-binding protein located in the endoplasmic reticulum !1of maize shoots: molecular cloning and complete primary !1structure. !$#cross-references MUID:89264464; PMID:2542939 !$#accession A32559 !'##molecule_type mRNA !'##residues 1-12,'P',14-140,'S',142-201 ##label IN1 !'##cross-references EMBL:J04550; NID:g168421; PIDN:AAA33436.1; !1PID:g168422 !'##experimental_source clone pABP420 !$#accession B32559 !'##molecule_type protein !'##residues 39-68 ##label IN2 !'##note 13-Ala (3 clones) and 141-Asn (6 clones) were also found !'##note the cDNA sequence of one clone (pABP370) lacked codons encoding !1residues 79-84 GENETICS !$#gene ERabp; Aux311 !$#introns 43/1; 78/3; 145/3; 168/2 CLASSIFICATION #superfamily auxin-binding protein KEYWORDS endoplasmic reticulum; glycoprotein FEATURE !$1-38 #domain signal sequence #status predicted #label SIG\ !$39-201 #product auxin-binding protein #status experimental !8#label MAT\ !$198-201 #region endoplasmic reticulum retention signal\ !$133 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 201 #molecular-weight 21977 #checksum 5270 SEQUENCE /// ENTRY B43033 #type complete TITLE auxin-binding protein 4 precursor - maize ORGANISM #formal_name Zea mays #common_name maize DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jul-1999 ACCESSIONS B43033; S39500 REFERENCE A43033 !$#authors Schwob, E.; Choi, S.Y.; Simmons, C.; Migliaccio, F.; Illag, !1L.; Hesse, T.; Palme, K.; Soll, D. !$#submission submitted to GenBank, February 1993 !$#description Molecular analysis of three maize 22 kDa auxin binding !1protein genes - transient promoter expression and regulatory !1regions. !$#accession B43033 !'##molecule_type DNA !'##residues 1-204 ##label SCH !'##cross-references GB:L08426; NID:g168398; PIDN:AAA33431.1; !1PID:g168399 REFERENCE S39500 !$#authors Hesse, T.; Garbers, C.; Brzobohaty, B.; Kreimer, G.; Soell, !1D.; Melkonian, M.; Schell, J.; Palme, K. !$#journal Plant Mol. Biol. (1993) 23:57-66 !$#title Two members of the ERabp gene family are expressed !1differentially in reproductive organs but to similar levels !1in the coleoptile of maize. !$#cross-references MUID:94033297; PMID:8219056 !$#accession S39500 !'##status preliminary !'##molecule_type mRNA !'##residues 1-204 ##label HES !'##cross-references GB:S66813; NID:g442525; PIDN:AAB28589.1; !1PID:g442526 GENETICS !$#gene abp4 CLASSIFICATION #superfamily auxin-binding protein KEYWORDS endoplasmic reticulum; glycoprotein FEATURE !$1-41 #domain signal sequence #status predicted #label SIG\ !$42-204 #product auxin-binding protein #status predicted !8#label MAT\ !$201-204 #region endoplasmic reticulum retention signal\ !$136 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 204 #molecular-weight 22628 #checksum 3473 SEQUENCE /// ENTRY C43033 #type fragment TITLE auxin-binding protein 5 precursor - maize (fragment) ORGANISM #formal_name Zea mays #common_name maize DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jul-1999 ACCESSIONS C43033 REFERENCE A43033 !$#authors Schwob, E.; Choi, S.Y.; Simmons, C.; Migliaccio, F.; Illag, !1L.; Hesse, T.; Palme, K.; Soll, D. !$#submission submitted to GenBank, February 1993 !$#description Molecular analysis of three maize 22 kDa auxin binding !1protein genes - transient promoter expression and regulatory !1regions. !$#accession C43033 !'##molecule_type DNA !'##residues 1-150 ##label SCH !'##cross-references GB:L08427; NID:g168400; PIDN:AAA33432.1; !1PID:g168401 GENETICS !$#gene abp5 CLASSIFICATION #superfamily auxin-binding protein KEYWORDS endoplasmic reticulum; glycoprotein FEATURE !$1-41 #domain signal sequence #status predicted #label SIG\ !$42-150 #product auxin-binding protein (fragment) #status !8predicted #label MAT\ !$136 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 150 #checksum 5505 SEQUENCE /// ENTRY S31835 #type complete TITLE auxin-binding protein T85 precursor - common tobacco ORGANISM #formal_name Nicotiana tabacum #common_name common tobacco DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jul-1999 ACCESSIONS S31835 REFERENCE S31835 !$#authors Shimomura, S. !$#submission submitted to GenBank, January 1993 !$#accession S31835 !'##molecule_type DNA !'##residues 1-187 ##label SHI !'##cross-references GB:X70902; NID:g20033; PIDN:CAA50259.1; PID:g20034 GENETICS !$#gene T85 !$#introns 26/1; 61/3; 129/3; 152/2 CLASSIFICATION #superfamily auxin-binding protein KEYWORDS endoplasmic reticulum; glycoprotein FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-187 #product auxin-binding protein #status predicted !8#label MAT\ !$184-187 #region endoplasmic reticulum retention signal\ !$32,117 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 187 #molecular-weight 21256 #checksum 3373 SEQUENCE /// ENTRY S31837 #type complete TITLE auxin-binding protein T92 precursor - common tobacco ORGANISM #formal_name Nicotiana tabacum #common_name common tobacco DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jul-1999 ACCESSIONS S31837 REFERENCE S31835 !$#authors Shimomura, S. !$#submission submitted to GenBank, January 1993 !$#accession S31837 !'##molecule_type DNA !'##residues 1-187 ##label SHI !'##cross-references GB:X70903; NID:g21946; PIDN:CAA50260.1; PID:g21947 GENETICS !$#gene T92 !$#introns 26/1; 61/3; 129/3; 152/2 CLASSIFICATION #superfamily auxin-binding protein KEYWORDS endoplasmic reticulum; glycoprotein FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-187 #product auxin-binding protein #status predicted !8#label MAT\ !$184-187 #region endoplasmic reticulum retention signal\ !$32,117 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 187 #molecular-weight 21453 #checksum 2426 SEQUENCE /// ENTRY S31584 #type complete TITLE auxin-binding protein T4I9.14 precursor - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jul-1999 ACCESSIONS S31584; JQ1598; A43037; S14524; T01395 REFERENCE S31584 !$#authors Shimomura, S. !$#submission submitted to GenBank, December 1992 !$#accession S31584 !'##molecule_type DNA !'##residues 1-198 ##label SHI !'##cross-references GB:X69901; NID:g16200; PIDN:CAA49526.1; PID:g16201 !'##experimental_source strain Columbia REFERENCE JQ1598 !$#authors Palme, K.; Hesse, T.; Campos, N.; Garbers, C.; Yanofsky, !1M.F.; Schell, J. !$#journal Plant Cell (1992) 4:193-201 !$#title Molecular analysis of an auxin binding protein gene located !1on chromosome 4 of Arabidopsis. !$#cross-references MUID:92338848; PMID:1321684 !$#accession JQ1598 !'##molecule_type mRNA !'##residues 1-198 ##label PAL !'##cross-references GB:S40550; NID:g251898; PIDN:AAB22612.1; !1PID:g251899 !$#accession A43037 !'##molecule_type protein !'##residues 34-68 ##label PA2 REFERENCE S14524 !$#authors Shimomura, S. !$#submission submitted to the EMBL Data Library, October 1990 !$#accession S14524 !'##molecule_type DNA !'##residues 172-198 ##label SH2 !'##cross-references EMBL:X55111; NID:g16141; PIDN:CAA38909.1; !1PID:g16142 REFERENCE Z14314 !$#authors Parnell, L.D.; Gnoj, L.; de la Bastide, M.; Hameed, A.; !1Habermann, K.; Schutz, K.; Huang, E.; Gottesman, T.; Dedhia, !1N.N.; McCombie, W.R. !$#submission submitted to the EMBL Data Library, May 1998 !$#description Genomic sequence of BAC T4I9 from Arabidopsis thaliana, !1chromosome IV, near 16.6 cM. !$#accession T01395 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-198 ##label PAR !'##cross-references EMBL:AF069442; NID:g3242970; PIDN:AAC79108.1; !1PID:g3924607 !'##experimental_source cultivar Columbia GENETICS !$#gene ERabp !$#map_position 4 !$#introns 40/1; 75/3; 142/3; 164/2 !$#note T4I9.14 CLASSIFICATION #superfamily auxin-binding protein KEYWORDS endoplasmic reticulum; glycoprotein FEATURE !$1-33 #domain signal sequence #status predicted #label SIG\ !$34-198 #product auxin-binding protein #status experimental !8#label MAT\ !$195-198 #region endoplasmic reticulum retention signal\ !$46,130 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 198 #molecular-weight 22044 #checksum 8480 SEQUENCE /// ENTRY ZZSYN2 #type complete TITLE nodulin-24 - soybean ORGANISM #formal_name Glycine max #common_name soybean DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 22-Nov-1996 ACCESSIONS A03342 REFERENCE A03342 !$#authors Katinakis, P.; Verma, D.P.S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:4157-4161 !$#title Nodulin-24 gene of soybean codes for a peptide of the !1peribacteroid membrane and was generated by tandem !1duplication of a sequence resembling an insertion element. !$#accession A03342 !'##molecule_type DNA !'##residues 1-147 ##label KAT COMMENT Nodulins are plant proteins induced during nodulation in !1legume roots after Rhizobium infection. Nodulin-24 may be !1cotranslated into a smaller polypeptide that appears to be !1an integral part of the peribacteroid membrane, a !1compartment essential for effective symbiotic nitrogen !1fixation. GENETICS !$#introns 31/1; 49/1; 67/1; 85/1 CLASSIFICATION #superfamily nodulin-24 KEYWORDS membrane protein; nodulation; tandem repeat FEATURE !$31-84 #region 18-residue repeats !8(A-G-E-A-V-Q-E-T-N-E-V-A-D-[TA]-K-L-V-[AG]) SUMMARY #length 147 #molecular-weight 15177 #checksum 2732 SEQUENCE /// ENTRY ZZAACD #type complete TITLE nodulin-25 precursor (clone 910) - alfalfa (cv. Cardinal) ORGANISM #formal_name Medicago sativa #common_name alfalfa DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS S11873; S04895 REFERENCE S11873 !$#authors Kiss, G.B.; Vincze, E.; Vegh, Z.; Toth, G.; Soos, J. !$#journal Plant Mol. Biol. (1990) 14:467-475 !$#title Identification and cDNA cloning of a new nodule-specific !1gene, Nms-25 (nodulin-25) of Medicago sativa. !$#cross-references MUID:91346636; PMID:2102828 !$#accession S11873 !'##molecule_type mRNA !'##residues 1-246 ##label KIS !'##cross-references EMBL:X13289; NID:g19645; PIDN:CAA31646.1; !1PID:g19646 GENETICS !$#gene Nms-25 CLASSIFICATION #superfamily nodulin-25 KEYWORDS nodulation FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-246 #product nodulin-25 #status predicted #label MAT SUMMARY #length 246 #molecular-weight 27431 #checksum 5974 SEQUENCE /// ENTRY ZZAAGY #type complete TITLE nodulin-25 precursor (clone pBRC4,pBRC5) - alfalfa (cv. Nagyszenasi) ORGANISM #formal_name Medicago sativa #common_name alfalfa DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS S14710; S04893 REFERENCE S14710 !$#authors Vegh, Z.; Vincze, E.; Kadirov, R.; Toth, G.; Kiss, G.B. !$#journal Plant Mol. Biol. (1990) 15:295-306 !$#title The nucleotide sequence of a nodule-specific gene, Nms-25 of !1Medicago sativa: its primary evolution via exon-shuffling !1and retrotransposon-mediated DNA rearrangements. !$#cross-references MUID:91355876; PMID:1966488 !$#accession S14710 !'##molecule_type DNA !'##residues 1-246 ##label VEG !'##cross-references EMBL:X13287; NID:g19642; PIDN:CAA31644.1; !1PID:g19643 GENETICS !$#gene Nms-25 !$#introns 35/1; 53/1; 67/1; 85/1; 101/1; 120/1; 138/1; 156/1; 174/1; !1192/1; 210/1; 244/1 CLASSIFICATION #superfamily nodulin-25 KEYWORDS nodulation FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-246 #product nodulin-25 #status predicted #label MAT SUMMARY #length 246 #molecular-weight 27529 #checksum 6181 SEQUENCE /// ENTRY FSFB #type fragment TITLE phaseolin - kidney bean (fragment) ALTERNATE_NAMES G1-globulin ORGANISM #formal_name Phaseolus vulgaris #common_name kidney bean DATE 24-Sep-1981 #sequence_revision 24-Sep-1981 #text_change 11-Nov-1996 ACCESSIONS A03343 REFERENCE A03343 !$#authors Sun, S.M.; Slightom, J.L.; Hall, T.C. !$#journal Nature (1981) 289:37-41 !$#title Intervening sequences in a plant gene - comparison of the !1partial sequence of cDNA and genomic DNA of French bean !1phaseolin. !$#accession A03343 !'##molecule_type DNA !'##residues 1-184 ##label SUN COMMENT This protein, the major storage protein of French bean, is !1also called G1-globulin. CLASSIFICATION #superfamily glycinin KEYWORDS glycoprotein; seed; storage protein FEATURE !$114 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 184 #checksum 3878 SEQUENCE /// ENTRY FWCNAB #type complete TITLE alpha-globulin B precursor (clone C72) - upland cotton ALTERNATE_NAMES seed storage protein; vicilin precursor ORGANISM #formal_name Gossypium hirsutum #common_name upland cotton DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jul-1999 ACCESSIONS A30838; S06911 REFERENCE A30838 !$#authors Chlan, C.A.; Pyle, J.B.; Legocki, A.B.; Dure III, L. !$#journal Plant Mol. Biol. (1986) 7:475-489 !$#title Developmental biochemistry of cottonseed embryogenesis and !1germination XVIII cDNA and amino acid sequences of members !1of the storage protein families. !$#accession A30838 !'##molecule_type mRNA !'##residues 1-588 ##label CHL !'##cross-references GB:M16891; NID:g167374; PIDN:AAA33071.1; !1PID:g167375 !'##experimental_source var. Coker 201 REFERENCE S06398 !$#authors Chlan, C.A.; Borroto, K.; Kamalay, J.A.; Dure III, L. !$#journal Plant Mol. Biol. (1987) 9:533-546 !$#title Developmental biochemistry of cottonseed embryogenesis and !1germination. XIX. Sequences and genomic organization of the !1alpha globulin (vicilin) genes of cottonseed. !$#accession S06911 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-81 ##label CH2 COMMENT This is a seed storage protein. CLASSIFICATION #superfamily glycinin KEYWORDS glycoprotein; seed; storage protein FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-588 #product alpha-globulin storage proprotein #status !8predicted #label MAT\ !$417 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 588 #molecular-weight 69729 #checksum 941 SEQUENCE /// ENTRY FWCNBA #type fragment TITLE beta-globulin A precursor (clone 94) - upland cotton (fragment) ALTERNATE_NAMES legumin precursor ORGANISM #formal_name Gossypium hirsutum #common_name upland cotton DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 20-Mar-1998 ACCESSIONS B30838 REFERENCE A30838 !$#authors Chlan, C.A.; Pyle, J.B.; Legocki, A.B.; Dure III, L. !$#journal Plant Mol. Biol. (1986) 7:475-489 !$#title Developmental biochemistry of cottonseed embryogenesis and !1germination XVIII cDNA and amino acid sequences of members !1of the storage protein families. !$#accession B30838 !'##molecule_type mRNA !'##residues 1-507 ##label CHL !'##experimental_source var. Coker 201 COMPLEX homohexamer of heterodimer disulfide linked acidic and basic !1chains CLASSIFICATION #superfamily glycinin KEYWORDS homohexamer; seed; storage protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-322,323-507 #product beta-globulin A #status predicted #label !8MAT\ !$20-322 #domain acidic chain #status predicted #label ACD\ !$323-507 #domain basic chain #status predicted #label BAS\ !$108-329 #disulfide_bonds #status predicted SUMMARY #length 507 #checksum 7420 SEQUENCE /// ENTRY FWCNBB #type complete TITLE beta-globulin B precursor (clone 134) - upland cotton ALTERNATE_NAMES legumin precursor ORGANISM #formal_name Gossypium hirsutum #common_name upland cotton DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 08-Dec-1995 ACCESSIONS C30838 REFERENCE A30838 !$#authors Chlan, C.A.; Pyle, J.B.; Legocki, A.B.; Dure III, L. !$#journal Plant Mol. Biol. (1986) 7:475-489 !$#title Developmental biochemistry of cottonseed embryogenesis and !1germination XVIII cDNA and amino acid sequences of members !1of the storage protein families. !$#accession C30838 !'##molecule_type mRNA !'##residues 1-516 ##label CHL !'##experimental_source var. Coker 201 COMMENT This cottonseed storage protein is a hexamer of identical !1subunits; each subunit is composed of an acidic and a basic !1chain linked by a disulfide bond and derived from the single !1preprotein chain. CLASSIFICATION #superfamily glycinin KEYWORDS seed; storage protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-516 #product beta-globulin B proprotein #status predicted !8#label MAT\ !$23-335 #domain beta-globulin B acidic chain #status !8predicted #label ACD\ !$336-516 #domain beta-globulin B basic chain #status predicted !8#label BAS\ !$126-342 #disulfide_bonds #status predicted SUMMARY #length 516 #molecular-weight 58709 #checksum 8098 SEQUENCE /// ENTRY FWSYBA #type complete TITLE beta-conglycinin alpha chain precursor - soybean ORGANISM #formal_name Glycine max #common_name soybean DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jul-1999 ACCESSIONS S14681; S74124; S06714 REFERENCE S14681 !$#authors Sebastiani, F.L.; Farrell, L.B.; Schuler, M.A.; Beachy, R.N. !$#journal Plant Mol. Biol. (1990) 15:197-201 !$#title Complete sequence of a cDNA of alpha subunit of soybean !1beta-conglycinin. !$#cross-references MUID:91355860; PMID:2103438 !$#accession S14681 !'##molecule_type mRNA !'##residues 1-605 ##label SEB !'##cross-references EMBL:X17698; NID:g18535; PIDN:CAA35691.1; !1PID:g18536 REFERENCE S74123 !$#authors Shutov, A.D.; Kakhovskaya, I.A.; Bastrygina, A.S.; Bulmaga, !1V.P.; Horstmann, C.; Muentz, K. !$#journal Eur. J. Biochem. (1996) 241:221-228 !$#title Limited proteolysis of beta-conglycinin and glycinin, the 7S !1and 11S storage globulins from soybean [Glycine max (L.) !1Merr.]. Structural and evolutionary implications. !$#cross-references MUID:97054613; PMID:8898910 !$#accession S74124 !'##molecule_type protein !'##residues 189-196,'H',198,'N',200,'X',202-203;397-408,'X',410,'X', !1412-417,'X',419-420,'X';484-501,'Y',503 ##label SHU !'##experimental_source seed CLASSIFICATION #superfamily glycinin KEYWORDS glycoprotein; seed; storage protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-62 #domain propeptide #status predicted #label PRO\ !$63-605 #product beta-conglycinin alpha chain #status !8predicted #label MAT\ !$261,517 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 605 #molecular-weight 70293 #checksum 6280 SEQUENCE /// ENTRY FWSYCB #type complete TITLE beta-conglycinin beta chain - soybean ORGANISM #formal_name Glycine max #common_name soybean DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jul-1999 ACCESSIONS JQ0969 REFERENCE JQ0969 !$#authors Harada, J.J.; Barker, S.J.; Goldberg, R.B. !$#journal Plant Cell (1989) 1:415-425 !$#title Soybean beta-conglycinin genes are clustered in several DNA !1regions and are regulated by transcriptional and !1posttranscriptional processes. !$#cross-references MUID:93005638; PMID:2562562 !$#accession JQ0969 !'##molecule_type DNA !'##residues 1-439 ##label HAR !'##cross-references GB:S44893; NID:g256426; PIDN:AAB23463.1; !1PID:g256427 COMMENT This protein accumulates during seed development and is !1hydrolyzed after germination to provide a carbon and !1nitrogen source for the developing seedling. GENETICS !$#gene CG-4 !$#introns 101/1; 159/3; 186/3; 281/3; 375/1 CLASSIFICATION #superfamily glycinin KEYWORDS seed; storage protein SUMMARY #length 439 #molecular-weight 50552 #checksum 4649 SEQUENCE /// ENTRY FWPMVB #type fragment TITLE vicilin B precursor - garden pea (fragment) ORGANISM #formal_name Pisum sativum #common_name garden pea DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 02-Jul-1998 ACCESSIONS A03344 REFERENCE A93462 !$#authors Lycett, G.W.; Delauney, A.J.; Gatehouse, J.A.; Gilroy, J.; !1Croy, R.R.D.; Boulter, D. !$#journal Nucleic Acids Res. (1983) 11:2367-2380 !$#title The vicilin gene family of pea (Pisum sativum L.): a !1complete cDNA coding sequence for preprovicilin. !$#cross-references MUID:83220791; PMID:6687941 !$#accession A03344 !'##molecule_type mRNA !'##residues 1-410 ##label LYC !'##experimental_source cv. Feltham First, clones pDUB7 and pDUB4 !'##note parts of this sequence, including the amino end of the mature !1protein, were determined by protein sequencing COMMENT The gene that codes for this protein is part of a multigene !1family coding for at least four major types of seed storage !1proteins. CLASSIFICATION #superfamily glycinin KEYWORDS glycoprotein FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-410 #product vicilin type B (fragment) #status predicted !8#label MAT\ !$321-322 #cleavage_site Asn-Asp (unidentified proteinase) !8#status experimental\ !$359 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 410 #checksum 5995 SEQUENCE /// ENTRY FWPMVA #type fragment TITLE vicilin A precursor - garden pea (fragment) ORGANISM #formal_name Pisum sativum #common_name garden pea DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 02-Jul-1998 ACCESSIONS A03345 REFERENCE A93462 !$#authors Lycett, G.W.; Delauney, A.J.; Gatehouse, J.A.; Gilroy, J.; !1Croy, R.R.D.; Boulter, D. !$#journal Nucleic Acids Res. (1983) 11:2367-2380 !$#title The vicilin gene family of pea (Pisum sativum L.): a !1complete cDNA coding sequence for preprovicilin. !$#cross-references MUID:83220791; PMID:6687941 !$#accession A03345 !'##molecule_type mRNA !'##residues 1-275 ##label LYC !'##experimental_source cv. Feltham First, clone pDUB2 CLASSIFICATION #superfamily glycinin KEYWORDS seed; storage protein FEATURE !$1-263 #product vicilin type A (fragment) #status predicted !8#label MAT\ !$264-275 #domain carboxyl-terminal propeptide #status !8predicted #label CTP SUMMARY #length 275 #checksum 182 SEQUENCE /// ENTRY FWPMV4 #type complete TITLE vicilin, 14K component - garden pea (tentative sequence) ORGANISM #formal_name Pisum sativum #common_name garden pea DATE 15-Oct-1982 #sequence_revision 15-Oct-1982 #text_change 31-Mar-2000 ACCESSIONS A03346 REFERENCE A03346 !$#authors Hirano, H.; Gatehouse, J.A.; Boulter, D. !$#journal FEBS Lett. (1982) 145:99-102 !$#title The complete amino acid sequence of a subunit of the vicilin !1seed storage protein of pea (Pisum sativum L.). !$#accession A03346 !'##molecule_type protein !'##residues 1-124 ##label HIR !'##experimental_source cv. Feltham First !'##note the microsequencing technique did not distinguish Leu from Ile; !1however, residues at positions 6, 23, 44, 86, 87, 97, and !1112 are most likely to be Leu as these are points of !1chymotryptic cleavage !'##note 18-Glu, 39-Asn, 47-Ser, 47-Arg, and 48-Asn were also found COMMENT This seed storage protein contains several components of !1different molecular weights. CLASSIFICATION #superfamily glycinin KEYWORDS seed; storage protein SUMMARY #length 124 #molecular-weight 14039 #checksum 22 SEQUENCE /// ENTRY FWPMLA #type complete TITLE legumin A precursor - garden pea ORGANISM #formal_name Pisum sativum #common_name garden pea DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 08-Dec-1995 ACCESSIONS A22866 REFERENCE A22866 !$#authors Lycett, G.W.; Croy, R.R.D.; Shirsat, A.H.; Boulter, D. !$#journal Nucleic Acids Res. (1984) 12:4493-4506 !$#title The complete nucleotide sequence of a legumin gene from pea !1(Pisum sativum L.). !$#cross-references MUID:84247316; PMID:6330672 !$#accession A22866 !'##molecule_type DNA !'##residues 1-517 ##label LYC !'##experimental_source cv. Feltham First COMMENT This protein, found in the seeds of many leguminous and !1nonleguminous plants, is the source of sulfur-containing !1amino acids in seed meals. GENETICS !$#gene leg A !$#introns 96/1; 179/3; 388/3 CLASSIFICATION #superfamily glycinin KEYWORDS seed; storage protein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-332 #product legumin A, alpha chain #status predicted !8#label ALP\ !$333-517 #product legumin A, beta chain #status predicted !8#label BET SUMMARY #length 517 #molecular-weight 58805 #checksum 1829 SEQUENCE /// ENTRY FWSYG1 #type complete TITLE glycinin chain A2B1a precursor - soybean ALTERNATE_NAMES 11S globulin CONTAINS glycinin chain A2; glycinin chain B1a ORGANISM #formal_name Glycine max #common_name soybean DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jul-1999 ACCESSIONS A91341; A92454; B92454; A90024; A92452; S10503; S74123; !1A05082; A05164; A05165; A24005; B91341; B92452; C92454; !1D92454; JS0285 REFERENCE A91341 !$#authors Momma, T.; Negoro, T.; Udaka, K.; Fukazawa, C. !$#journal FEBS Lett. (1985) 188:117-122 !$#title A complete cDNA coding for the sequence of glycinin A2B1a !1subunit precursor. !$#accession A91341 !'##molecule_type mRNA !'##residues 1-485 ##label MOM !'##experimental_source strain Bonmimori !'##note the source of this mRNA was cotyledon tissue taken from seeds !1at the middle stage of development REFERENCE A92454 !$#authors Marco, Y.A.; Thanh, V.H.; Tumer, N.E.; Scallon, B.J.; !1Nielsen, N.C. !$#journal J. Biol. Chem. (1984) 259:13436-13441 !$#title Cloning and structural analysis of DNA encoding an A2B1a !1subunit of glycinin. !$#cross-references MUID:85030472; PMID:6092376 !$#accession A92454 !'##molecule_type mRNA !'##residues 262-446 ##label MA1 !$#accession B92454 !'##molecule_type DNA !'##residues 318-485 ##label MA2 !'##experimental_source strain CX635-1-1-1 REFERENCE A90024 !$#authors Utsumi, S.; Kim, C.S.; Kohno, M.; Kito, M. !$#journal Agric. Biol. Chem. (1987) 51:3267-3273 !$#title Polymorphism and expression of cDNAs encoding glycinin !1subunits. !$#accession A90024 !'##molecule_type mRNA !'##residues 1-38,'D',40-485 ##label UTS !'##experimental_source strain Shirotsurunoko REFERENCE A92452 !$#authors Staswick, P.E.; Hermodson, M.A.; Nielsen, N.C. !$#journal J. Biol. Chem. (1984) 259:13424-13430 !$#title The amino acid sequence of the A2B1a subunit of glycinin. !$#cross-references MUID:85030470; PMID:6541652 !$#accession A92452 !'##molecule_type protein !'##residues 19-38,'D',40-60,'S',62-116,'C',118-192,'E',194-296;301-342, !1'S',344-463,'I',465-480 ##label STA !'##experimental_source strain CX635-1-1-1 !'##note residues 94-Gly, 103-Asp, 195-Glu, 318-Thr, 331-Val, 400-Asp !1and 400-Arg, 409-Val, 413-Arg, 431-Met, and 434-Thr were !1also found; this heterogeneity is attributed to the presence !1of multiple polypeptides differing slightly in their primary !1sequences REFERENCE A92453 !$#authors Staswick, P.E.; Hermodson, M.A.; Nielsen, N.C. !$#journal J. Biol. Chem. (1984) 259:13431-13435 !$#title Identification of the cystines which link the acidic and !1basic components of the glycinin subunits. !$#cross-references MUID:85030471; PMID:6541653 !$#contents annotation; disulfide bond REFERENCE S10502 !$#authors Kitamura, Y.; Arahira, M.; Itoh, Y.; Fukazawa, C. !$#journal Nucleic Acids Res. (1990) 18:4245 !$#title The complete nucleotide sequence of soybean glycinin A2B1a !1gene spanning to another glycinin gene A1aB1b. !$#cross-references MUID:90332420; PMID:2377465 !$#accession S10503 !'##status translation not shown !'##molecule_type DNA !'##residues 1-36 ##label KIT !'##cross-references EMBL:X53404; NID:g18522; PIDN:CAA37480.1; !1PID:g18524 REFERENCE S74123 !$#authors Shutov, A.D.; Kakhovskaya, I.A.; Bastrygina, A.S.; Bulmaga, !1V.P.; Horstmann, C.; Muentz, K. !$#journal Eur. J. Biochem. (1996) 241:221-228 !$#title Limited proteolysis of beta-conglycinin and glycinin, the 7S !1and 11S storage globulins from soybean [Glycine max (L.) !1Merr.]. Structural and evolutionary implications. !$#cross-references MUID:97054613; PMID:8898910 !$#accession S74123 !'##molecule_type protein !'##residues 118-132;205-215 ##label SHU !'##experimental_source seed COMMENT Both acidic (A2) and basic (B1a) components of this glycinin !1subunit (A2B1a) are synthesized as a single precursor that !1is modified after translation to form a dimer covalently !1linked by a disulfide bond. COMMENT Residues 297-300 and 481-485 are removed from the precursor !1during processing after translation. GENETICS !$#introns 356/3 CLASSIFICATION #superfamily glycinin KEYWORDS seed; storage protein FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-296 #product glycinin chain A2 #status experimental !8#label GLA\ !$301-480 #product glycinin chain B1a #status experimental !8#label GLB\ !$104-307 #disulfide_bonds #status experimental SUMMARY #length 485 #molecular-weight 54332 #checksum 9795 SEQUENCE /// ENTRY FWSYG2 #type complete TITLE glycinin chain A1aBx precursor - soybean ALTERNATE_NAMES 11S globulin; glycinin A1aB1b ORGANISM #formal_name Glycine max #common_name soybean DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jul-1999 ACCESSIONS A23497; S10502 REFERENCE A23497 !$#authors Negoro, T.; Momma, T.; Fukazawa, C. !$#journal Nucleic Acids Res. (1985) 13:6719-6731 !$#title A cDNA clone encoding a glycinin A-1a subunit precursor of !1soybean. !$#cross-references MUID:86041867; PMID:2997720 !$#accession A23497 !'##molecule_type mRNA !'##residues 1-495 ##label NEG !'##cross-references GB:X02985; NID:g18614; PIDN:CAA26723.1; PID:g18615 !'##experimental_source cv. Bonminori !'##note the authors translated the codon AAC for residue 449 as Lys !'##note because of current nomenclature ambiguities, the authors choose !1to designate the basic chain as Bx REFERENCE S10502 !$#authors Kitamura, Y.; Arahira, M.; Itoh, Y.; Fukazawa, C. !$#journal Nucleic Acids Res. (1990) 18:4245 !$#title The complete nucleotide sequence of soybean glycinin A2B1a !1gene spanning to another glycinin gene A1aB1b. !$#cross-references MUID:90332420; PMID:2377465 !$#accession S10502 !'##status preliminary; translation not shown !'##molecule_type DNA !'##residues 481-495 ##label KIT !'##cross-references EMBL:X53404; NID:g18522; PIDN:CAA37479.1; !1PID:g18523 COMMENT The source of this protein was cotyledon tissue taken 38 !1days after flowering. COMMENT By homology with the A2B1a component, residues 307-310, and !1491-495 are removed from the precursor during !1posttranslational processing. CLASSIFICATION #superfamily glycinin KEYWORDS seed; storage protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-306 #product glycinin chain A1a #status predicted #label !8GLA\ !$311-490 #product glycinin chain Bx #status predicted #label !8GLB\ !$107-317 #disulfide_bonds #status predicted SUMMARY #length 495 #molecular-weight 55506 #checksum 8518 SEQUENCE /// ENTRY FWSYG5 #type complete TITLE glycinin chain A5A4B3 precursor - soybean ALTERNATE_NAMES 11S globulin ORGANISM #formal_name Glycine max #common_name soybean DATE 28-Feb-1986 #sequence_revision 31-Mar-1988 #text_change 16-Jul-1999 ACCESSIONS A91145; A91333; A03348; A25207; A27253 REFERENCE A91145 !$#authors Momma, T.; Negoro, T.; Hirano, H.; Matsumoto, A.; Udaka, K.; !1Fukazawa, C. !$#journal Eur. J. Biochem. (1985) 149:491-496 !$#title Glycinin A5A4B3 mRNA: cDNA cloning and nucleotide sequencing !1of a splitting storage protein subunit of soybean. !$#cross-references MUID:85230642; PMID:2988947 !$#accession A91145 !'##molecule_type mRNA !'##residues 1-562 ##label MOM !'##cross-references GB:X02626; NID:g18628; PIDN:CAA26478.1; PID:g732706 !'##experimental_source cv. Bonminori !'##note the authors translated the codon TCA for residue 86 as Leu, GAC !1for residue 145 as Glu, and CTT for residue 473 as Ile REFERENCE A91333 !$#authors Hirano, H.; Fukazawa, C.; Harada, K. !$#journal FEBS Lett. (1985) 181:124-128 !$#title The primary structures of the A4 and A5 subunits are highly !1homologous to that of the A3 subunit in the glycinin seed !1storage protein of soybean. !$#accession A91333 !'##molecule_type protein !'##residues 24-28,'F',30-81,'L',83-85,'L',87-93,'V',95-100,'I',102,'M', !1104,'F',106-116,'Q',118-120 ##label HIR !'##experimental_source cv. Bonminori !'##note parts of the A4 chain, including the amino end, were sequenced COMMENT The source of this protein was cotyledon tissue taken from !1seeds at the middle stage of development. COMMENT The glycinin molecule, the major seed storage protein of !1soybean, is composed of six dimers, each dimer consisting of !1acidic and basic chains. Seven acidic and five basic chains !1have been identified. COMMENT Acidic (A5 and A4) and basic (B3) components of this !1glycinin subunit are synthesized as a single precursor. !1Posttranslational modifications form a dimer (A5-B3), !1covalently linked by a disulfide bond, that is thought to be !1noncovalently associated with the A4 chain. CLASSIFICATION #superfamily glycinin KEYWORDS seed; storage protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-120 #product glycinin, A5 chain #status experimental !8#label GA5\ !$121-377 #product glycinin, A4 chain #status predicted #label !8GA4\ !$378-562 #product glycinin, B3 chain #status predicted #label !8GB3\ !$108-384 #disulfide_bonds #status predicted SUMMARY #length 562 #molecular-weight 63587 #checksum 2559 SEQUENCE /// ENTRY FWSYG3 #type complete TITLE glycinin G5 precursor - soybean ALTERNATE_NAMES 11S globulin; glycinin A3B4 ORGANISM #formal_name Glycine max #common_name soybean DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jul-1999 ACCESSIONS A92524; S11005; A05083; A22615 REFERENCE A92524 !$#authors Fukazawa, C.; Momma, T.; Hirano, H.; Harada, K.; Udaka, K. !$#journal J. Biol. Chem. (1985) 260:6234-6239 !$#title Glycinin A3B4 mRNA: cloning and sequencing of !1double-stranded cDNA complementary to a soybean storage !1protein. !$#cross-references MUID:85207609; PMID:3838983 !$#accession A92524 !'##molecule_type mRNA !'##residues 1-516 ##label FUK !'##cross-references GB:M10962; NID:g169968; PIDN:AAA33964.1; !1PID:g169969 !'##experimental_source cv. Bonminori REFERENCE A92465 !$#authors Hirano, H.; Fukazawa, C.; Harada, K. !$#journal J. Biol. Chem. (1984) 259:14371-14377 !$#title The complete amino acid sequence of the A-3 subunit of the !1glycinin seed storage protein of the soybean (Glycine max !1(L.) Merrill). !$#cross-references MUID:85054904; PMID:6542104 !$#contents annotation !$#note the sequence reported is very different from that shown REFERENCE S10851 !$#authors Nielsen, N.C.; Dickinson, C.D.; Cho, T.J.; Thanh, V.H.; !1Scallon, B.J.; Fischer, R.L.; Sims, T.L.; Drews, G.N.; !1Goldberg, R.B. !$#journal Plant Cell (1989) 1:313-328 !$#title Characterization of the glycinin gene family in soybean. !$#cross-references MUID:92393391; PMID:2485233 !$#accession S11005 !'##molecule_type DNA !'##residues 1-516 ##label NIE !'##experimental_source variety Forrest GENETICS !$#gene Gy5 CLASSIFICATION #superfamily glycinin KEYWORDS seed; storage protein FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-344 #product glycinin chain A3 #status predicted #label !8GLA\ !$345-516 #product glycinin chain B4 #status predicted #label !8GLB\ !$109-351 #disulfide_bonds #status predicted SUMMARY #length 516 #molecular-weight 57956 #checksum 3503 SEQUENCE /// ENTRY FWPU1B #type complete TITLE 11S globulin beta subunit precursor - cucurbita cv. Kurokawa Amakuri ALTERNATE_NAMES globulin IV beta subunit ORGANISM #formal_name Cucurbita cv. Kurokawa Amakuri #variety cv. Kurokawa Amakuri Nankin DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 23-Sep-2002 ACCESSIONS S00366; S09480 REFERENCE S00366 !$#authors Hayashi, M.; Mori, H.; Nishimura, M.; Akazawa, T.; !1Hara-Nishimura, I. !$#journal Eur. J. Biochem. (1988) 172:627-632 !$#title Nucleotide sequence of cloned cDNA coding for pumpkin 11-S !1globulin beta subunit. !$#cross-references MUID:88166744; PMID:2450746 !$#accession S00366 !'##molecule_type mRNA !'##residues 1-480 ##label HAY !'##cross-references EMBL:M36407; NID:g167491; PIDN:AAA33110.1; !1PID:g167492 !'##experimental_source Cucurbita sp. cv. Kurokawa Amakuri Nankin; !1cotyledon mRNA REFERENCE S09066 !$#authors Ohmiya, M.; Hara, I.; Matsubara, H. !$#journal Plant Cell Physiol. (1980) 21:157-167 !$#title Pumpkin (Cucurbita sp.) seed globulin IV. Terminal sequences !1of the acidic and basic peptide chains and identification of !1a pyroglutamyl peptide chain. !$#accession S09480 !'##molecule_type protein !'##residues 22-26,'E',28-29,'S';297-302 ##label OHM !'##experimental_source Cucurbita sp. hybrid, Tetsukabuto-Nankin !'##note the carboxyl end of the gamma' chain is Leu or Val; the !1carboxyl end of the delta 2 chain is Arg COMPLEX heterohexamer; hexamer of alpha and beta subunits; beta !1subunit composed of disulfide-linked gamma and delta chain CLASSIFICATION #superfamily glycinin KEYWORDS pyroglutamic acid; seed; storage protein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-274 #product (or 22-272) 11S globulin gamma' chain !8#status experimental #label GCH\ !$297-479 #product (or 297-478) 11S globulin delta-2 chain !8#status experimental #label DCH\ !$22 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$124-303 #disulfide_bonds #status predicted SUMMARY #length 480 #molecular-weight 54625 #checksum 6954 SEQUENCE /// ENTRY FWRZ2 #type complete TITLE glutelin II precursor - rice ORGANISM #formal_name Oryza sativa #common_name rice DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 07-Jun-1996 ACCESSIONS JQ0112 REFERENCE JQ0112 !$#authors Abe, K.; Emori, Y.; Kawasaki, H.; Kondo, H.; Suzuki, K.; !1Arai, S. !$#journal Agric. Biol. Chem. (1989) 53:2969-2973 !$#title Organization and primary sequence of multiple genes encoding !1type II mRNA species of rice prepro-glutelin. !$#accession JQ0112 !'##molecule_type DNA !'##residues 1-499 ##label ABE !'##experimental_source cv. Nipponbare !'##note four independent genomic clones (OGg1, OGg11, OGg15, and OGg17) !1were sequenced; the translation of OGg1 differs from that of !1OGg15 (shown) in having 320-Ile. That of OGg11 differs in !1having 320-Ile and 454-Ala COMMENT Glutelin, the major storage protein of rice, is synthesized !1as a precursor, which undergoes posttranslational processing !1to produce a mature protein with acidic and basic chains !1linked by disulfide bonds. GENETICS !$#introns 111/1; 202/3; 362/3 CLASSIFICATION #superfamily glycinin KEYWORDS pyroglutamic acid; seed; storage protein FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-306 #product glutelin II acidic chain #status predicted !8#label ACH\ !$307-499 #product glutelin II basic chain #status predicted !8#label BCH\ !$25 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status predicted SUMMARY #length 499 #molecular-weight 56320 #checksum 2368 SEQUENCE /// ENTRY FWOAG1 #type complete TITLE 12S seed storage globulin precursor (clone pOG2) - oat CONTAINS acidic polypeptide; basic polypeptide ORGANISM #formal_name Avena sativa #common_name oat DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 08-Dec-1995 ACCESSIONS JA0141; JA0160 REFERENCE JA0141 !$#authors Shotwell, M.A.; Afonso, C.; Davies, E.; Chesnut, R.S.; !1Larkins, B.A. !$#journal Plant Physiol. (1988) 87:698-704 !$#title Molecular characterization of oat seed globulins. !$#accession JA0141 !'##molecule_type mRNA !'##residues 1-518 ##label SHO !'##cross-references GB:M21405 !'##experimental_source strain Merr. cv Williams !'##note the authors translated the codon AAA for residue 46 as Arg; the !1sequence shown in Fig. 5 of this paper also differs from the !1nucleic acid translation in having 46-Arg and 47-Lys COMMENT Most of oat storage protein is a 11-12S globulin that is !1synthesized in the endosperm. COMMENT The protein is a hexamer of subunits, each consisting of an !1acidic chain and a basic chain linked by disulfide bonds. !1These chains are formed by proteolytic cleavage of a single !1precursor. CLASSIFICATION #superfamily glycinin KEYWORDS seed; storage protein; tandem repeat FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-317 #product acidic polypeptide #status predicted #label !8ACP\ !$281-312 #region 8-residue repeats\ !$318-518 #product basic polypeptide #status predicted #label !8BAP\ !$121-324 #disulfide_bonds #status predicted SUMMARY #length 518 #molecular-weight 58513 #checksum 4573 SEQUENCE /// ENTRY S14762 #type complete TITLE cruciferin 4 precursor - rape ALTERNATE_NAMES 11S globulin cru4; 12S globulin alpha-4 chain/beta-4 chain ORGANISM #formal_name Brassica napus #common_name rape DATE 30-Jun-1993 #sequence_revision 22-Apr-1995 #text_change 10-Dec-1999 ACCESSIONS S14762; S30036; S30028; D35540 REFERENCE S14762 !$#authors Sjoedahl, S.; Roedin, J.; Rask, L. !$#journal Eur. J. Biochem. (1991) 196:617-621 !$#title Characterization of the 12S globulin complex of Brassica !1napus. Evolutionary relationship to other 11-12S storage !1globulins. !$#cross-references MUID:91192032; PMID:2013284 !$#accession S14762 !'##molecule_type mRNA !'##residues 1-109,'N',111-358,'N',360-465 ##label SJO !'##cross-references EMBL:X57851 !$#accession S30036 !'##molecule_type mRNA !'##residues 282-373,'Q',375-465 ##label SJ2 !'##cross-references EMBL:X57848; NID:g17806; PIDN:CAA40978.1; !1PID:g17807 REFERENCE S30028 !$#authors Roedin, J. !$#submission submitted to the EMBL Data Library, February 1991 !$#accession S30028 !'##status preliminary !'##molecule_type mRNA !'##residues 53-465 ##label RO2 !'##cross-references EMBL:X57850; NID:g17804; PIDN:CAA40980.1; !1PID:g17805 REFERENCE A35540 !$#authors Roedin, J.; Ericson, M.L.; Josefsson, L.G.; Rask, L. !$#journal J. Biol. Chem. (1990) 265:2720-2723 !$#title Characterization of a cDNA clone encoding a Brassica napus !112 S protein (cruciferin) subunit. Relationship between !1precursors and mature chains. !$#cross-references MUID:90153897; PMID:2303422 !$#accession D35540 !'##molecule_type protein !'##residues 108-119;123-125,'E',128-135;139-143,'X',145-146,'H', !1148-153;277-302,'X',304-307;336-351,'X',353,'X',355,'X', !1357-360;372-373,'Q',375-377,'X',379-395 ##label ROE GENETICS !$#gene cru4 !$#introns 60/3 CLASSIFICATION #superfamily glycinin KEYWORDS seed; storage protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-276 #product cruciferin alpha-4 chain #status predicted !8#label ACH\ !$116-134 #region glutamine/glycine-rich\ !$277-465 #product cruciferin beta-4 chain #status predicted !8#label BCH\ !$105-283 #disulfide_bonds #status predicted SUMMARY #length 465 #molecular-weight 51411 #checksum 7012 SEQUENCE /// ENTRY S08510 #type complete TITLE cruciferin precursor (CRB) - Arabidopsis thaliana ALTERNATE_NAMES 12S globulin; 12S seed storage protein; seed storage protein beta-chain 1 ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 30-Jun-1992 #sequence_revision 27-Feb-1997 #text_change 16-Jul-1999 ACCESSIONS S08510; B38925 REFERENCE S08509 !$#authors Pang, P.P.; Pruitt, R.E.; Meyerowitz, E.M. !$#journal Plant Mol. Biol. (1988) 11:805-820 !$#title Molecular cloning, genomic organization, expression and !1evolution of 12S seed storage protein genes of Arabidopsis !1thaliana. !$#accession S08510 !'##molecule_type DNA !'##residues 1-455 ##label PAN !'##cross-references EMBL:X14313; NID:g16236; PIDN:CAA32494.1; !1PID:g808937 !'##note the authors translated the codon CTA for residue 330 as Thr REFERENCE PA0001 !$#authors Kamo, M.; Kawakami, T.; Miyatake, N.; Tsugita, A. !$#submission submitted to JIPID, July 1994 !$#description Separation and characterization of Arabidopsis proteins by !1two-dimensional gel electrophoresis. !$#accession B38925 !'##molecule_type protein !'##residues 270-275,'X',277 ##label KAM !'##experimental_source seed GENETICS !$#gene CRB !$#introns 95/1; 182/3; 325/3 CLASSIFICATION #superfamily glycinin KEYWORDS seed; storage protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-455 #product cruciferin #status predicted #label MAT\ !$24-269 #domain cruciferin alpha chain #status predicted !8#label ACH\ !$270-455 #domain cruciferin beta chain #status experimental !8#label BCH SUMMARY #length 455 #molecular-weight 50643 #checksum 314 SEQUENCE /// ENTRY S21426 #type complete TITLE conglutin gamma precursor - narrow-leaved blue lupine ORGANISM #formal_name Lupinus angustifolius #common_name narrow-leaved blue lupine DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S21426; S31092 REFERENCE S21426 !$#authors Kolivas, S.; Gayler, K.R. !$#submission submitted to the EMBL Data Library, April 1992 !$#accession S21426 !'##molecule_type mRNA !'##residues 1-448 ##label KOL1 !'##cross-references EMBL:X65601 !'##note it is uncertain whether Met-1 or Met-5 is the initiator REFERENCE S31092 !$#authors Kolivas, S.; Gayler, K.R. !$#journal Plant Mol. Biol. (1993) 21:397-401 !$#title Structure of the cDNA coding for conglutin gamma, a !1sulphur-rich protein from Lupinus angustifolius. !$#cross-references MUID:93144715; PMID:8425065 !$#accession S31092 !'##molecule_type mRNA !'##residues 5-448 ##label KOL2 !'##cross-references EMBL:X65601 CLASSIFICATION #superfamily conglutin gamma KEYWORDS disulfide bond; seed; storage protein FEATURE !$1-33 #domain signal sequence #status predicted #label SIG\ !$34-294 #product conglutin gamma large chain #status !8predicted #label MA1\ !$295-448 #product conglutin gamma small chain #status !8predicted #label MA2 SUMMARY #length 448 #molecular-weight 48885 #checksum 9435 SEQUENCE /// ENTRY S06750 #type complete TITLE basic 7S globulin precursor - soybean ALTERNATE_NAMES insulin-binding protein ORGANISM #formal_name Glycine max #common_name soybean DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S06750; S00218; A61003; JN0311; JN0312 REFERENCE S06750 !$#authors Kagawa, H.; Hirano, H. !$#journal Nucleic Acids Res. (1989) 17:8868 !$#title Sequence of a cDNA encoding soybean basic 7S globulin. !$#cross-references MUID:90067863; PMID:2587227 !$#accession S06750 !'##molecule_type mRNA !'##residues 1-427 ##label KA1 !'##cross-references EMBL:X16469; NID:g18542; PIDN:CAA34489.1; !1PID:g18543 REFERENCE S00218 !$#authors Kagawa, H.; Yamauchi, F.; Hirano, H. !$#journal FEBS Lett. (1987) 226:145-149 !$#title Soybean basic 7S globulin represents a protein widely !1distributed in legume species. !$#accession S00218 !'##molecule_type protein !'##residues 276-293,'X';295-304,'FX';423-427, !1'X';'IVGPFGLCPNQNGVTSLGPMXXMQPAR';'QL',356,'LN',359-368,'X', !1370-380;381-388;334-336,'PV',339-342,'E',344-345,'L', !1347-349,'X';326-327,'S',329-339,'F',341-342,'AX' ##label KAG REFERENCE A61003 !$#authors Hirano, H.; Watanabe, T. !$#journal Electrophoresis (1990) 11:573-580 !$#title Microsequencing of proteins electrotransferred onto !1immobilizing matrices from polyacrylamide gel !1electrophoresis: application to an insoluble protein. !$#cross-references MUID:91031409; PMID:2226413 !$#accession A61003 !'##molecule_type protein !'##residues 25-57;135-150;276-304,'X',306-308,'X',310-311;383-417 !1##label HIR REFERENCE JN0309 !$#authors Barbashov, S.F.; Egorov, T.A.; Kochkina, V.M. !$#journal Bioorg. Khim. (1991) 17:421-423 !$#title Isolation and characterization of soybean insulin-binding !1protein. !$#cross-references MUID:91291181; PMID:2064630 !$#accession JN0311 !'##molecule_type protein !'##residues 'VPIPQHKTN',27-33,'X',35-42,'XX',45,'X',47,'X',49,'AX',52 !1##label BAR !'##note 20-Thr, 21-Asn, 25-Pro and 50-Asn were also found !$#accession JN0312 !'##molecule_type protein !'##residues 'S',99,'IV',102,'SX',105,'C',286-299,'XX',302,'XX',305 !1##label BA2 !'##note 102-Gly and 296-Lys were also found COMMENT This protein specifically binds to bovine insulin. CLASSIFICATION #superfamily conglutin gamma KEYWORDS heterodimer; seed; storage protein FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-275 #product basic 7S globulin heavy chain #status !8experimental #label MAT1\ !$276-427 #product basic 7S globulin light chain #status !8experimental #label MAT2 SUMMARY #length 427 #molecular-weight 46292 #checksum 9342 SEQUENCE /// ENTRY S24756 #type complete TITLE vicilin-like storage protein precursor - white spruce ORGANISM #formal_name Picea glauca #common_name white spruce DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S24756; S18873 REFERENCE S24756 !$#authors Newton, C.H.; Flinn, B.S.; Sutton, B.C.S. !$#journal Plant Mol. Biol. (1992) 20:315-322 !$#title Vicilin-like seed storage proteins in the gymnosperm !1interior spruce (Picea glauca/engelmanii). !$#cross-references MUID:93004485; PMID:1391775 !$#accession S24756 !'##molecule_type mRNA !'##residues 1-448 ##label NEW !'##cross-references EMBL:X63191; NID:g20500; PIDN:CAA44873.1; !1PID:g20501 CLASSIFICATION #superfamily vicilin SUMMARY #length 448 #molecular-weight 50200 #checksum 6346 SEQUENCE /// ENTRY FWRZP7 #type complete TITLE prolamin 7 precursor - rice ORGANISM #formal_name Oryza sativa #common_name rice DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jul-1999 ACCESSIONS S00557; JA0165 REFERENCE S00557 !$#authors Kim, W.T.; Okita, T.W. !$#journal FEBS Lett. (1988) 231:308-310 !$#title Nucleotide and primary sequence of a major rice prolamine. !$#cross-references MUID:88196415; PMID:3360138 !$#accession S00557 !'##molecule_type mRNA !'##residues 1-149 ##label KI1 !'##cross-references EMBL:Y00747; NID:g20297; PIDN:CAA68715.1; !1PID:g20298 REFERENCE JA0165 !$#authors Kim, W.T.; Okita, T.W. !$#journal Plant Physiol. (1988) 88:649-655 !$#title Structure, expression, and heterogeneity of the rice seed !1prolamines. !$#accession JA0165 !'##molecule_type mRNA !'##residues 1-149 ##label KI2 !'##experimental_source seed, clone 7 !'##note the authors translated the codon UAU for residue 55 as Thr COMMENT Prolamin is the major seed storage protein in most of the !1cereals. CLASSIFICATION #superfamily prolamin KEYWORDS prolamin; seed; storage protein FEATURE !$1-14 #domain signal sequence #status predicted #label SIG\ !$15-149 #product prolamin #status predicted #label MAT SUMMARY #length 149 #molecular-weight 16930 #checksum 7109 SEQUENCE /// ENTRY UESY27 #type complete TITLE vegetative storage protein, 27K, precursor - soybean ALTERNATE_NAMES 31K glycoprotein precursor ORGANISM #formal_name Glycine max #common_name soybean DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 17-Mar-2000 ACCESSIONS JN0697; JA0139; S08512; B45504; JA0158 REFERENCE JN0697 !$#authors Rapp, W.D.; Lilley, G.G.; Nielsen, N.C. !$#journal Theor. Appl. Genet. (1990) 79:785-792 !$#title Characterization of soybean vegetative storage proteins and !1genes. !$#accession JN0697 !'##molecule_type DNA !'##residues 1-254 ##label RAP REFERENCE JA0139 !$#authors Staswick, P.E. !$#journal Plant Physiol. (1988) 87:250-254 !$#title Soybean vegetative storage protein structure and gene !1expression. !$#accession JA0139 !'##molecule_type mRNA !'##residues 1-254 ##label STA !'##experimental_source strain Merr. cv Williams !'##note the cDNA clones corresponding to two different vegetative !1storage proteins were isolated and sequenced; the predicted !1sequences for the mature proteins agree with the known !1amino-terminal sequences REFERENCE S08511 !$#authors Mason, H.S.; Guerrero, F.D.; Boyer, J.S.; Mullet, J.E. !$#journal Plant Mol. Biol. (1988) 11:845-856 !$#title Proteins homologous to leaf glycoproteins are abundant in !1stems of darkgrown soybean seedlings. Analysis of proteins !1and cDNAs. !$#accession S08512 !'##status preliminary !'##molecule_type mRNA !'##residues 1-254 ##label MAS !'##cross-references EMBL:X17414; NID:g18761; PIDN:CAA35464.1; !1PID:g18762 REFERENCE A45504 !$#authors Staswick, P.E. !$#journal Plant Physiol. (1989) 89:717 !$#contents erratum !$#accession B45504 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 207-254 ##label ST2 COMMENT Vegetative storage protein is found in vegetative tissues !1but not in seeds. GENETICS !$#gene VSP27 CLASSIFICATION #superfamily vegetative storage protein; !1glucose-6-phosphatase catalytic domain homology KEYWORDS glycoprotein; storage protein FEATURE !$1-35 #domain signal sequence #status predicted #label SIG\ !$36-254 #product 27K vegetative storage protein #status !8predicted #label MAP\ !$130 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 254 #molecular-weight 29280 #checksum 306 SEQUENCE /// ENTRY UESY25 #type fragment TITLE vegetative storage protein, 25K, precursor - soybean (fragment) ORGANISM #formal_name Glycine max #common_name soybean DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 17-Mar-2000 ACCESSIONS JA0140; JA0157 REFERENCE JA0139 !$#authors Staswick, P.E. !$#journal Plant Physiol. (1988) 87:250-254 !$#title Soybean vegetative storage protein structure and gene !1expression. !$#accession JA0140 !'##molecule_type mRNA !'##residues 1-244 ##label STA !'##experimental_source strain Merr. cv Williams !'##note the cDNA clones corresponding to two different vegetative !1storage proteins were isolated and sequenced; the predicted !1sequences for the mature proteins agree with the known !1amino-terminal sequences COMMENT Vegetative storage protein is found in vegetative tissues !1but not in seeds. GENETICS !$#gene VSP25 CLASSIFICATION #superfamily vegetative storage protein; !1glucose-6-phosphatase catalytic domain homology KEYWORDS glycoprotein; storage protein FEATURE !$1-31 #domain signal sequence (fragment) #status predicted !8#label SIG\ !$32-244 #product 25K vegetative storage protein #status !8predicted #label MAP\ !$126 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 244 #checksum 6470 SEQUENCE /// ENTRY ZIZM21 #type complete TITLE 22K zein precursor (clone pZ22.1) - maize ORGANISM #formal_name Zea mays #common_name maize DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 28-May-1999 ACCESSIONS A26564 REFERENCE A92387 !$#authors Marks, M.D.; Larkins, B.A. !$#journal J. Biol. Chem. (1982) 257:9976-9983 !$#title Analysis of sequence microheterogeneity among zein messenger !1RNAs. !$#cross-references MUID:82265740; PMID:6286660 !$#accession A26564 !'##molecule_type mRNA !'##residues 1-263 ##label MAR !'##cross-references GB:V01478; GB:J01245; NID:g22531; PIDN:CAA24725.1; !1PID:g22532 !'##experimental_source inbred line W64A REFERENCE A92509 !$#authors Marks, M.D.; Lindell, J.S.; Larkins, B.A. !$#journal J. Biol. Chem. (1985) 260:16445-16450 !$#title Quantitative analysis of the accumulation of zein mRNA !1during maize endosperm development. !$#cross-references MUID:86059562; PMID:2999156 !$#contents annotation; classification and localization REFERENCE A92388 !$#authors Argos, P.; Pedersen, K.; Marks, M.D.; Larkins, B.A. !$#journal J. Biol. Chem. (1982) 257:9984-9990 !$#title A structural model for maize zein proteins. !$#cross-references MUID:82265741; PMID:7107620 !$#contents annotation; structure COMMENT Zeins, which compose approximately 50% of the total !1endosperm protein in maize, are deposited as protein bodies !1within the rough reticulum. The zeins can be divided into !1five groups based on molecular weight: 27K (glutelin), 22K, !119K, 15K, and 10K. Structurally, 22K and 19K zeins are !1composed of nine adjacent, topologically antiparallel !1helices clustered within a distorted cylinder. CLASSIFICATION #superfamily zein KEYWORDS seed; storage protein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-263 #product 22K zein #status predicted #label MAT SUMMARY #length 263 #molecular-weight 28484 #checksum 1354 SEQUENCE /// ENTRY ZIZMC2 #type fragment TITLE 22K zein precursor (clone cZ22C2) - maize (fragment) ORGANISM #formal_name Zea mays #common_name maize DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 16-Jul-1999 ACCESSIONS C24557 REFERENCE A92510 !$#authors Marks, M.D.; Lindell, J.S.; Larkins, B.A. !$#journal J. Biol. Chem. (1985) 260:16451-16459 !$#title Nucleotide sequence analysis of zein mRNAs from maize !1endosperm. !$#cross-references MUID:86059563; PMID:2999157 !$#accession C24557 !'##molecule_type mRNA !'##residues 1-261 ##label MAR !'##cross-references GB:M12141; NID:g168687; PIDN:AAA33534.1; !1PID:g168688 !'##experimental_source inbred line W64A !'##note the authors translated the codon TCA for residue 92 as Ala, GTG !1for residue 93 as Leu, and GGC for residue 229 as Ala CLASSIFICATION #superfamily zein KEYWORDS seed; storage protein FEATURE !$1-16 #domain signal sequence (fragment) #status predicted !8#label SIG\ !$17-261 #product 22K zein #status predicted #label MAT SUMMARY #length 261 #checksum 6218 SEQUENCE /// ENTRY ZIZM23 #type complete TITLE 22K zein precursor (clone pZ22.3) - maize ORGANISM #formal_name Zea mays #common_name maize DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 16-Jul-1999 ACCESSIONS B26564 REFERENCE A92387 !$#authors Marks, M.D.; Larkins, B.A. !$#journal J. Biol. Chem. (1982) 257:9976-9983 !$#title Analysis of sequence microheterogeneity among zein messenger !1RNAs. !$#cross-references MUID:82265740; PMID:6286660 !$#accession B26564 !'##molecule_type mRNA !'##residues 1-266 ##label MAR !'##cross-references GB:J01246; NID:g168685; PIDN:AAA33533.1; !1PID:g168686 !'##experimental_source inbred line W64A !'##note the authors translated the codon GTT for residue 212 as Ala CLASSIFICATION #superfamily zein KEYWORDS seed; storage protein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-266 #product 22K zein #status predicted #label MAT SUMMARY #length 266 #molecular-weight 28935 #checksum 8438 SEQUENCE /// ENTRY ZIZM49 #type fragment TITLE 22K zein (clone B49) - maize (fragment) ORGANISM #formal_name Zea mays #common_name maize DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 21-Jul-2000 ACCESSIONS B22762 REFERENCE A90967 !$#authors Geraghty, D.E.; Messing, J.; Rubenstein, I. !$#journal EMBO J. (1982) 1:1329-1335 !$#title Sequence analysis and comparison of cDNAs of the zein !1multigene family. !$#cross-references MUID:84207881; PMID:6897917 !$#accession B22762 !'##molecule_type mRNA !'##residues 1-122 ##label GER !'##cross-references GB:V01477; NID:g22530; PIDN:CAB56172.1; !1PID:g5912522 CLASSIFICATION #superfamily zein KEYWORDS seed; storage protein SUMMARY #length 122 #checksum 9641 SEQUENCE /// ENTRY ZIZMD1 #type complete TITLE 19K zein precursor (clone cZ19D1) - maize ORGANISM #formal_name Zea mays #common_name maize DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 16-Jul-1999 ACCESSIONS G24557 REFERENCE A92510 !$#authors Marks, M.D.; Lindell, J.S.; Larkins, B.A. !$#journal J. Biol. Chem. (1985) 260:16451-16459 !$#title Nucleotide sequence analysis of zein mRNAs from maize !1endosperm. !$#cross-references MUID:86059563; PMID:2999157 !$#accession G24557 !'##molecule_type mRNA !'##residues 1-240 ##label MAR !'##cross-references GB:M12144; NID:g168681; PIDN:AAA33531.1; !1PID:g168682 !'##experimental_source inbred line W64A !'##note the authors translated the codon CAG for residue 52 as Glu CLASSIFICATION #superfamily zein KEYWORDS seed; storage protein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-240 #product 19K zein #status predicted #label MAT SUMMARY #length 240 #molecular-weight 26633 #checksum 6110 SEQUENCE /// ENTRY ZIZM91 #type complete TITLE 19K zein precursor (clone cZ19C1) - maize ORGANISM #formal_name Zea mays #common_name maize DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 16-Jul-1999 ACCESSIONS I24557 REFERENCE A92510 !$#authors Marks, M.D.; Lindell, J.S.; Larkins, B.A. !$#journal J. Biol. Chem. (1985) 260:16451-16459 !$#title Nucleotide sequence analysis of zein mRNAs from maize !1endosperm. !$#cross-references MUID:86059563; PMID:2999157 !$#accession I24557 !'##molecule_type mRNA !'##residues 1-240 ##label MAR !'##cross-references GB:M12146; NID:g168677; PIDN:AAA33529.1; !1PID:g168678 !'##experimental_source inbred line W64A CLASSIFICATION #superfamily zein KEYWORDS seed; storage protein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-240 #product 19K zein #status predicted #label MAT SUMMARY #length 240 #molecular-weight 26254 #checksum 3946 SEQUENCE /// ENTRY ZIZM2 #type complete TITLE 19K zein precursor (clone A20) - maize ORGANISM #formal_name Zea mays #common_name maize DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 16-Jul-1999 ACCESSIONS A22762; D22831 REFERENCE A90967 !$#authors Geraghty, D.E.; Messing, J.; Rubenstein, I. !$#journal EMBO J. (1982) 1:1329-1335 !$#title Sequence analysis and comparison of cDNAs of the zein !1multigene family. !$#cross-references MUID:84207881; PMID:6897917 !$#accession A22762 !'##molecule_type mRNA !'##residues 1-240 ##label GER !'##cross-references GB:V01476; NID:g22528; PIDN:CAA24723.1; PID:g22529 !'##experimental_source clone A20 REFERENCE A91003 !$#authors Viotti, A.; Cairo, G.; Vitale, A.; Sala, E. !$#journal EMBO J. (1985) 4:1103-1110 !$#title Each zein gene class can produce polypeptides of different !1sizes. !$#accession D22831 !'##molecule_type mRNA !'##residues 1-73 ##label VIO !'##experimental_source clone M8 CLASSIFICATION #superfamily zein KEYWORDS seed; storage protein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-240 #product 19K zein #status predicted #label MAT SUMMARY #length 240 #molecular-weight 26240 #checksum 4396 SEQUENCE /// ENTRY ZIZM92 #type complete TITLE 19K zein precursor (clone cZ19C2) - maize ORGANISM #formal_name Zea mays #common_name maize DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 16-Jul-1999 ACCESSIONS H24557 REFERENCE A92510 !$#authors Marks, M.D.; Lindell, J.S.; Larkins, B.A. !$#journal J. Biol. Chem. (1985) 260:16451-16459 !$#title Nucleotide sequence analysis of zein mRNAs from maize !1endosperm. !$#cross-references MUID:86059563; PMID:2999157 !$#accession H24557 !'##molecule_type mRNA !'##residues 1-240 ##label MAR !'##cross-references GB:M12145; NID:g168679; PIDN:AAA33530.1; !1PID:g168680 !'##experimental_source inbred line W64A CLASSIFICATION #superfamily zein KEYWORDS seed; storage protein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-240 #product 19K zein #status predicted #label MAT SUMMARY #length 240 #molecular-weight 26280 #checksum 3467 SEQUENCE /// ENTRY ZIZM99 #type complete TITLE 19K zein precursor (clone ZG99) - maize ORGANISM #formal_name Zea mays #common_name maize DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 28-May-1999 ACCESSIONS A29288; F24557 REFERENCE A90820 !$#authors Pedersen, K.; Devereux, J.; Wilson, D.R.; Sheldon, E.; !1Larkins, B.A. !$#journal Cell (1982) 29:1015-1026 !$#title Cloning and sequence analysis reveal structural variation !1among related zein genes in maize. !$#cross-references MUID:83103094; PMID:7151164 !$#accession A29288 !'##molecule_type DNA !'##residues 1-235 ##label PED !'##cross-references GB:V01470; GB:J01243; NID:g22518; PIDN:CAA24717.1; !1PID:g22519 !'##experimental_source inbred line W64A !'##note the authors translated the codon GGC for residue 202 as Gln REFERENCE A92510 !$#authors Marks, M.D.; Lindell, J.S.; Larkins, B.A. !$#journal J. Biol. Chem. (1985) 260:16451-16459 !$#title Nucleotide sequence analysis of zein mRNAs from maize !1endosperm. !$#cross-references MUID:86059563; PMID:2999157 !$#accession F24557 !'##molecule_type mRNA !'##residues 1-235 ##label MAR !'##experimental_source inbred line W64A CLASSIFICATION #superfamily zein KEYWORDS seed; storage protein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-235 #product 19K zein #status predicted #label MAT SUMMARY #length 235 #molecular-weight 25575 #checksum 745 SEQUENCE /// ENTRY ZIZM3 #type complete TITLE 19K zein precursor (clone A30) - maize ORGANISM #formal_name Zea mays #common_name maize DATE 18-Dec-1981 #sequence_revision 30-Jun-1988 #text_change 16-Jul-1999 ACCESSIONS A90967; A93741; S21970; A03349; C22762 REFERENCE A90967 !$#authors Geraghty, D.E.; Messing, J.; Rubenstein, I. !$#journal EMBO J. (1982) 1:1329-1335 !$#title Sequence analysis and comparison of cDNAs of the zein !1multigene family. !$#cross-references MUID:84207881; PMID:6897917 !$#accession A90967 !'##molecule_type mRNA !'##residues 1-234 ##label GER REFERENCE A93741 !$#authors Geraghty, D.; Peifer, M.A.; Rubenstein, I.; Messing, J. !$#journal Nucleic Acids Res. (1981) 9:5163-5174 !$#title The primary structure of a plant protein: zein. !$#cross-references MUID:82081837; PMID:6895552 !$#accession A93741 !'##molecule_type mRNA !'##residues 10-234 ##label GE2 REFERENCE S07172 !$#authors Hu, N.T.; Peifer, M.A.; Heidecker, G.; Messing, J.; !1Rubenstein, I. !$#journal EMBO J. (1982) 1:1337-1342 !$#title Primary structure of a genomic zein sequence of maize. !$#cross-references MUID:84207882; PMID:6233138 !$#accession S21970 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-234 ##label HUN !'##cross-references EMBL:V01481; NID:g22544; PIDN:CAA24728.1; !1PID:g22545 CLASSIFICATION #superfamily zein KEYWORDS seed; storage protein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-234 #product 19K zein #status predicted #label MAT SUMMARY #length 234 #molecular-weight 25403 #checksum 977 SEQUENCE /// ENTRY ZIZMB1 #type complete TITLE 19K zein precursor (clone cZ19B1) - maize ORGANISM #formal_name Zea mays #common_name maize DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 16-Jul-1999 ACCESSIONS E24557 REFERENCE A92510 !$#authors Marks, M.D.; Lindell, J.S.; Larkins, B.A. !$#journal J. Biol. Chem. (1985) 260:16451-16459 !$#title Nucleotide sequence analysis of zein mRNAs from maize !1endosperm. !$#cross-references MUID:86059563; PMID:2999157 !$#accession E24557 !'##molecule_type mRNA !'##residues 1-234 ##label MAR !'##cross-references GB:M12143; NID:g168673; PIDN:AAA33527.1; !1PID:g168674 !'##experimental_source inbred line W64A CLASSIFICATION #superfamily zein KEYWORDS seed; storage protein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-234 #product 19K zein #status predicted #label MAT SUMMARY #length 234 #molecular-weight 25435 #checksum 3129 SEQUENCE /// ENTRY ZIZMA2 #type fragment TITLE 19K zein precursor (clone cZ19A2) - maize (fragment) ORGANISM #formal_name Zea mays #common_name maize DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 16-Jul-1999 ACCESSIONS D24557 REFERENCE A92510 !$#authors Marks, M.D.; Lindell, J.S.; Larkins, B.A. !$#journal J. Biol. Chem. (1985) 260:16451-16459 !$#title Nucleotide sequence analysis of zein mRNAs from maize !1endosperm. !$#cross-references MUID:86059563; PMID:2999157 !$#accession D24557 !'##molecule_type mRNA !'##residues 1-230 ##label MAR !'##cross-references GB:M12142; NID:g168669; PIDN:AAA33525.1; !1PID:g168670 !'##experimental_source inbred line W64A !'##note the authors translated the codon GAC for residue 209 as Asn CLASSIFICATION #superfamily zein KEYWORDS seed; storage protein FEATURE !$1-18 #domain signal sequence (fragment) #status predicted !8#label SIG\ !$19-230 #product 19K zein #status predicted #label MAT SUMMARY #length 230 #checksum 8546 SEQUENCE /// ENTRY S04740 #type complete TITLE 39K protein - maize mitochondrion plasmid ORGANISM #formal_name mitochondrion Zea mays #common_name maize DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS S04740; S26989 REFERENCE S04740 !$#authors Leon, P.; Walbot, V.; Bedinger, P. !$#journal Nucleic Acids Res. (1989) 17:4089-4099 !$#title Molecular analysis of the linear 2.3 kb plasmid of maize !1mitochondria: apparent capture of tRNA genes. !$#cross-references MUID:89296459; PMID:2472603 !$#accession S04740 !'##status translation not shown !'##molecule_type DNA !'##residues 1-294 ##label LEO !'##cross-references EMBL:X13704; NID:g14304; PIDN:CAA31989.1; !1PID:g14305 GENETICS !$#genome mitochondrion CLASSIFICATION #superfamily maize mitochondrion 39K protein KEYWORDS mitochondrion SUMMARY #length 294 #molecular-weight 33870 #checksum 5290 SEQUENCE /// ENTRY KNPMP4 #type complete TITLE protein P4 - garden pea ORGANISM #formal_name Pisum sativum #common_name garden pea DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jul-1999 ACCESSIONS S11874 REFERENCE S11874 !$#authors Williams, M.E.; Mundy, J.; Kay, S.A.; Chua, N.H. !$#journal Plant Mol. Biol. (1990) 14:765-774 !$#title Differential expression of two related organ-specific genes !1in pea. !$#cross-references MUID:91346667; PMID:2102854 !$#accession S11874 !'##molecule_type DNA !'##residues 1-130 ##label WIL !'##cross-references EMBL:X51594; NID:g20820; PIDN:CAA35943.1; !1PID:g295829 !'##note the protein sequence from Fig. 8 is inconsistent with the !1nucleotide sequence from Fig. 4 in having an additional Ser !1after 52-Ser !'##note the authors translated the codon GGT for residue 103 as Ala GENETICS !$#introns 17/3 CLASSIFICATION #superfamily pea protein S2 KEYWORDS duplication FEATURE !$60-85,86-111 #region duplication SUMMARY #length 130 #molecular-weight 14421 #checksum 6746 SEQUENCE /// ENTRY KNPMS2 #type complete TITLE protein S2 - garden pea ORGANISM #formal_name Pisum sativum #common_name garden pea DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jul-1999 ACCESSIONS S11875 REFERENCE S11874 !$#authors Williams, M.E.; Mundy, J.; Kay, S.A.; Chua, N.H. !$#journal Plant Mol. Biol. (1990) 14:765-774 !$#title Differential expression of two related organ-specific genes !1in pea. !$#cross-references MUID:91346667; PMID:2102854 !$#accession S11875 !'##molecule_type DNA !'##residues 1-181 ##label WIL !'##cross-references EMBL:X51595; NID:g20886; PIDN:CAA35944.1; !1PID:g295831 !'##note the protein sequence from Fig. 8 is inconsistent with the !1nucleotide sequence from Fig. 5 in having an additional Ser !1after 51-Ser and an additional Asn after 101-Asn !'##note the authors translated the codon GCT for residue 154 as Gly GENETICS !$#introns 16/3 CLASSIFICATION #superfamily pea protein S2 KEYWORDS duplication FEATURE !$59-84,85-110, !$111-136,137-162 #region duplication SUMMARY #length 181 #molecular-weight 19974 #checksum 1359 SEQUENCE /// ENTRY KNMUHY #type complete TITLE dehydrin-like protein - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS S22485; S22193 REFERENCE S22485 !$#authors Rouse, D.; Gehring, C.A.; Parish, R.W. !$#journal Plant Mol. Biol. (1992) 19:531-532 !$#title Structure and sequence of a dehydrin-like gene in !1Arabidopsis thaliana. !$#cross-references MUID:92322990; PMID:1623199 !$#accession S22485 !'##molecule_type DNA !'##residues 1-127 ##label ROU !'##cross-references EMBL:X64199; NID:g17683; PIDN:CAA45524.1; !1PID:g17684 GENETICS !$#introns 60/3 CLASSIFICATION #superfamily dehydrin-like protein SUMMARY #length 127 #molecular-weight 13378 #checksum 8780 SEQUENCE /// ENTRY KNRZG1 #type complete TITLE glycine-rich cell wall structural protein 1 precursor (clone lambda-313) - rice ORGANISM #formal_name Oryza sativa #common_name rice DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jul-1999 ACCESSIONS S13385 REFERENCE S13385 !$#authors Lei, M.; Wu, R. !$#journal Plant Mol. Biol. (1991) 16:187-198 !$#title A novel glycine-rich cell wall protein gene in rice. !$#cross-references MUID:91370862; PMID:1716496 !$#accession S13385 !'##molecule_type DNA !'##residues 1-165 ##label LEI !'##cross-references EMBL:X53596; NID:g20246; PIDN:CAA37665.1; !1PID:g20247 GENETICS !$#gene grp-1 CLASSIFICATION #superfamily glycine-rich cell wall structural protein 1 KEYWORDS cell wall; duplication; structural protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-165 #product glycine-rich cell wall structural protein 1 !8#status predicted #label MAT\ !$30-55 #region repeat R1\ !$56-62 #region repeat R2\ !$62-92 #region repeat R1\ !$93-99 #region repeat R2\ !$100-131 #region repeat R1\ !$132-138 #region repeat R2\ !$139-160 #region repeat R1 SUMMARY #length 165 #molecular-weight 13536 #checksum 5738 SEQUENCE /// ENTRY KNRZG2 #type complete TITLE glycine-rich cell wall structural protein 2 precursor - rice ORGANISM #formal_name Oryza sativa #common_name rice DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS S18567 REFERENCE S18567 !$#authors Fang, R.X.; Pang, Z.; Gao, D.M.; Mang, K.Q.; Chua, N.H. !$#journal Plant Mol. Biol. (1991) 17:1255-1257 !$#title cDNA sequence of a virus-inducible, glycine-rich protein !1gene from rice. !$#cross-references MUID:92032791; PMID:1840687 !$#accession S18567 !'##molecule_type mRNA !'##residues 1-183 ##label FAN !'##cross-references EMBL:X54449; NID:g20244; PIDN:CAA38315.1; !1PID:g20245 CLASSIFICATION #superfamily glycine-rich cell wall structural protein 1 KEYWORDS cell wall; structural protein FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-183 #product glycine-rich cell wall structural protein 2 !8#status predicted #label MAT SUMMARY #length 183 #molecular-weight 14920 #checksum 6894 SEQUENCE /// ENTRY S01820 #type complete TITLE glycine-rich cell wall protein 1.8 precursor - kidney bean ORGANISM #formal_name Phaseolus vulgaris #common_name kidney bean DATE 30-Sep-1989 #sequence_revision 19-May-1994 #text_change 16-Jul-1999 ACCESSIONS S01820 REFERENCE S01820 !$#authors Keller, B.; Sauer, N.; Lamb, C.J. !$#journal EMBO J. (1988) 7:3625-3633 !$#title Glycine-rich cell wall proteins in bean: gene structure and !1association of the protein with the vascular system. !$#cross-references MUID:89091109; PMID:3208742 !$#accession S01820 !'##molecule_type DNA !'##residues 1-465 ##label KEL !'##cross-references EMBL:X13596; NID:g21002; PIDN:CAA31932.1; !1PID:g21003 COMMENT This protein is enriched in the cell wall fraction of young !1hypocotyls and ovary tissue, apparently associated with the !1vascular system, and is transiently induced in wounded !1mature hypocotyls. COMMENT Much of the sequence consists of tandemly repeated !122-residue segments with the consensus sequence !1HGGGYGGGQGGGAGGGYGAGGE. CLASSIFICATION #superfamily Phaseolus glycine-rich cell wall protein 1.8 KEYWORDS cell wall; structural protein; tandem repeat FEATURE !$1-30 #domain signal sequence #status predicted #label SIG\ !$31-465 #product glycine-rich cell wall protein 1.8 #status !8predicted #label MAT SUMMARY #length 465 #molecular-weight 36683 #checksum 5623 SEQUENCE /// ENTRY KNMU #type complete TITLE glycine-rich cell wall protein precursor - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS S17732 REFERENCE S17732 !$#authors Quigley, F.; Villiot, M.L.; Mache, R. !$#journal Plant Mol. Biol. (1991) 17:949-952 !$#title Nucleotide sequence and expression of a novel glycine-rich !1protein gene from Arabidopsis thaliana. !$#cross-references MUID:92003708; PMID:1912511 !$#accession S17732 !'##molecule_type DNA !'##residues 1-338 ##label QUI !'##cross-references EMBL:X58338; NID:g16292; PIDN:CAA41249.1; !1PID:g16293 GENETICS !$#introns 203/1 CLASSIFICATION #superfamily Phaseolus glycine-rich cell wall protein 1.8 KEYWORDS cell wall; structural protein FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-338 #product glycine-rich cell wall protein #status !8predicted #label MAT SUMMARY #length 338 #molecular-weight 23891 #checksum 6121 SEQUENCE /// ENTRY A26099 #type complete TITLE glycine-rich cell wall structural protein - garden petunia ORGANISM #formal_name Petunia x hybrida #common_name garden petunia DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A26099 REFERENCE A26099 !$#authors Condit, C.M.; Meagher, R.B. !$#journal Nature (1986) 323:178-181 !$#title A gene encoding a novel glycine-rich structural protein of !1petunia. !$#accession A26099 !'##molecule_type mRNA !'##residues 1-384 ##label CON CLASSIFICATION #superfamily Phaseolus glycine-rich cell wall protein 1.8 SUMMARY #length 384 #molecular-weight 28777 #checksum 1852 SEQUENCE /// ENTRY S31415 #type complete TITLE glycine-rich protein GRP22 - rape ORGANISM #formal_name Brassica napus #common_name rape DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S31415 REFERENCE S31415 !$#authors Bergeron, D.; Boivin, R.; Baszczynski, C.L.; Bellemare, G. !$#submission submitted to the EMBL Data Library, August 1992 !$#description Characterization and expression of a gene family encoding !1glycine-rich proteins in Brassica napus. !$#accession S31415 !'##status preliminary !'##molecule_type DNA !'##residues 1-291 ##label BER !'##cross-references EMBL:Z15045; NID:g17820; PIDN:CAA78762.1; !1PID:g17821 CLASSIFICATION #superfamily Phaseolus glycine-rich cell wall protein 1.8 SUMMARY #length 291 #molecular-weight 22659 #checksum 9301 SEQUENCE /// ENTRY S01821 #type complete TITLE glycine-rich protein 1.0 precursor - kidney bean ORGANISM #formal_name Phaseolus vulgaris #common_name kidney bean DATE 30-Sep-1989 #sequence_revision 19-May-1994 #text_change 16-Jul-1999 ACCESSIONS S01821 REFERENCE S01820 !$#authors Keller, B.; Sauer, N.; Lamb, C.J. !$#journal EMBO J. (1988) 7:3625-3633 !$#title Glycine-rich cell wall proteins in bean: gene structure and !1association of the protein with the vascular system. !$#cross-references MUID:89091109; PMID:3208742 !$#accession S01821 !'##molecule_type DNA !'##residues 1-252 ##label KEL !'##cross-references EMBL:X13595; NID:g21000; PIDN:CAA31931.1; !1PID:g21001 CLASSIFICATION #superfamily Phaseolus glycine-rich protein 1.0 KEYWORDS cell wall; structural protein FEATURE !$1-30 #domain signal sequence #status predicted #label SIG\ !$31-252 #product glycine-rich protein 1.0 #status predicted !8#label MAT SUMMARY #length 252 #molecular-weight 19958 #checksum 4254 SEQUENCE /// ENTRY JQ1062 #type complete TITLE glycine-rich protein 3 precursor - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 31-Dec-1991 #sequence_revision 19-May-1994 #text_change 13-Jun-1997 ACCESSIONS JQ1062 REFERENCE JQ1060 !$#authors de Oliveira, D.E.; Seurinck, J.; Inze, D.; Van Montagu, M.; !1Botterman, J. !$#journal Plant Cell (1990) 2:427-436 !$#title Differential expression of five Arabidopsis genes encoding !1glycine-rich proteins. !$#cross-references MUID:93044485; PMID:2152168 !$#accession JQ1062 !'##molecule_type mRNA !'##residues 1-145 ##label DEO !'##cross-references GB:S47409 !'##experimental_source strain C24 CLASSIFICATION #superfamily Arabidopsis glycine-rich protein 3 KEYWORDS tandem repeat FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-145 #product glycine-rich protein 3 #status predicted !8#label MAT\ !$59-100 #region 7-residue repeats (G-G-G-G-[NR]-Y-Q) SUMMARY #length 145 #molecular-weight 14370 #checksum 675 SEQUENCE /// ENTRY JQ1061 #type complete TITLE glycine-rich protein 2 - Arabidopsis thaliana ALTERNATE_NAMES protein F20M13.240 ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 31-Dec-1991 #sequence_revision 19-May-1994 #text_change 23-Jul-1999 ACCESSIONS JQ1061; T05696 REFERENCE JQ1060 !$#authors de Oliveira, D.E.; Seurinck, J.; Inze, D.; Van Montagu, M.; !1Botterman, J. !$#journal Plant Cell (1990) 2:427-436 !$#title Differential expression of five Arabidopsis genes encoding !1glycine-rich proteins. !$#cross-references MUID:93044485; PMID:2152168 !$#accession JQ1061 !'##molecule_type mRNA !'##residues 1-203 ##label DEO !'##cross-references GB:S47408; NID:g259444; PIDN:AAB24074.1; !1PID:g259445 !'##experimental_source strain C24 REFERENCE Z15420 !$#authors Bevan, M.; Wedler, H.; Kutzner, M.; Wambutt, R.; Bancroft, !1I.; Mewes, H.W.; Mayer, K.F.X.; Schueller, C. !$#submission submitted to the Protein Sequence Database, February 1999 !$#accession T05696 !'##molecule_type DNA !'##residues 1-203 ##label BEV !'##cross-references EMBL:AL035540 !'##experimental_source cultivar Columbia; BAC clone F20M13 COMMENT This protein is expressed in roots, stems, leaves, and seed !1pods. GENETICS !$#map_position 4 !$#note F20M13.240 CLASSIFICATION #superfamily Arabidopsis glycine-rich protein 2; cold shock !1domain homology KEYWORDS zinc finger FEATURE !$13-73 #domain cold shock domain homology #label CSD\ !$87-129 #region glycine-rich\ !$131-144 #region zinc finger CCHC motif\ !$147-183 #region glycine-rich\ !$185-198 #region zinc finger CCHC motif SUMMARY #length 203 #molecular-weight 19153 #checksum 7923 SEQUENCE /// ENTRY KNNT2S #type complete TITLE glycine-rich protein 2 - wood tobacco ORGANISM #formal_name Nicotiana sylvestris #common_name wood tobacco DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS S17731 REFERENCE S17731 !$#authors Obokata, J.; Ohme, M.; Hayashida, N. !$#journal Plant Mol. Biol. (1991) 17:953-955 !$#title Nucleotide sequence of a cDNA clone encoding a putative !1glycine-rich protein of 19.7 kDa in Nicotiana sylvestris. !$#cross-references MUID:92003709; PMID:1912512 !$#accession S17731 !'##molecule_type mRNA !'##residues 1-214 ##label OBO !'##cross-references EMBL:X60007; NID:g19742; PIDN:CAA42622.1; !1PID:g19743 CLASSIFICATION #superfamily Arabidopsis glycine-rich protein 2; cold shock !1domain homology KEYWORDS zinc finger FEATURE !$11-71 #domain cold shock domain homology #label CSD\ !$82-158 #region glycine-rich\ !$159-172 #region zinc finger CCHC motif\ !$176-195 #region glycine-rich\ !$196-209 #region zinc finger CCHC motif SUMMARY #length 214 #molecular-weight 19746 #checksum 7019 SEQUENCE /// ENTRY KNNP #type complete TITLE arachin 25K chain - peanut ORGANISM #formal_name Arachis hypogaea #common_name peanut DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 04-Nov-1994 ACCESSIONS A03350; A61464 REFERENCE A03350 !$#authors Bhushan, R.; Goyal, R.N.; Agarwal, A. !$#journal Biochem. Int. (1985) 11:477-490 !$#title Complete amino acid sequence of an arachin sub-unit. !$#accession A03350 !'##molecule_type protein !'##residues 1-201 ##label BHU REFERENCE A61464 !$#authors Bhushan, R.; Goyal, R.N.; Agarwal, A. !$#journal J. Protein Chem. (1984) 3:395-401 !$#title Amino-terminal sequence analysis of arachin. !$#accession A61464 !'##molecule_type protein !'##residues 'CM',1-16,'P',18-58 ##label BH2 COMMENT This is one of six apparently different protein chains that !1constitute the peanut protein arachin. CLASSIFICATION #superfamily arachin KEYWORDS seed; storage protein SUMMARY #length 201 #molecular-weight 22219 #checksum 2474 SEQUENCE /// ENTRY PJSY3 #type complete TITLE proline-rich protein 3 precursor - soybean ALTERNATE_NAMES proline-rich protein 2; repetitive proline-rich protein 3 ORGANISM #formal_name Glycine max #common_name soybean DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 21-Jan-2000 ACCESSIONS S14912; JQ1103; A35532; S06774 REFERENCE S14912 !$#authors Datta, K.; Marcus, A. !$#journal Plant Mol. Biol. (1990) 14:285-286 !$#title Nucleotide sequence of a gene encoding soybean repetitive !1proline-rich protein 3. !$#cross-references MUID:91329684; PMID:2101695 !$#accession S14912 !'##molecule_type DNA !'##residues 1-230 ##label DAT !'##cross-references EMBL:X16574; NID:g18737; PIDN:CAA34593.1; !1PID:g18738 !'##experimental_source cv. Wayne REFERENCE JQ1103 !$#authors Datta, K.; Schmidt, A.; Marcus, A. !$#journal Plant Cell (1989) 1:945-952 !$#title Characterization of two soybean repetitive proline-rich !1proteins and a cognate cDNA from germinated axes. !$#cross-references MUID:92393424; PMID:2535534 !$#accession JQ1103 !'##molecule_type mRNA !'##residues 1-230 ##label DA2 !'##cross-references GB:S44202; NID:g255407; PIDN:AAD13836.1; !1PID:g4261542 !'##experimental_source var. Hobbit, var. Corsoy REFERENCE A35532 !$#authors Hong, J.C.; Nagao, R.T.; Key, J.L. !$#journal J. Biol. Chem. (1990) 265:2470-2475 !$#title Characterization of a proline-rich cell wall protein gene !1family of soybean. A comparative analysis. !$#cross-references MUID:90153859; PMID:2303411 !$#accession A35532 !'##molecule_type DNA !'##residues 1-230 ##label HON !'##cross-references GB:J05208; NID:g170065; PIDN:AAA34011.1; !1PID:g170066 !'##note the authors designate this protein as proline-rich protein 2 GENETICS !$#gene RPRP3 CLASSIFICATION #superfamily proline-rich protein 3 KEYWORDS cell wall; hydroxyproline; tandem repeat FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-230 #product proline-rich protein 3 #status predicted !8#label MAT\ !$25-214 #region 10-residue repeats (E-[KN]-P-P-[VI] !8-Y-K-P-P-[VTY]) SUMMARY #length 230 #molecular-weight 25981 #checksum 7878 SEQUENCE /// ENTRY S11880 #type complete TITLE S-locus-specific glycoprotein precursor - cabbage ALTERNATE_NAMES S-locus-related glycoprotein ORGANISM #formal_name Brassica oleracea var. capitata #common_name cabbage DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S11880; S10474 REFERENCE S11880 !$#authors Trick, M. !$#journal Plant Mol. Biol. (1990) 15:203-205 !$#title Genomic sequence of a Brassica S locus-related gene. !$#cross-references MUID:91355861; PMID:2103439 !$#accession S11880 !'##molecule_type DNA !'##residues 1-444 ##label TRI !'##cross-references EMBL:X52089; NID:g17896; PIDN:CAA36307.1; !1PID:g17897 CLASSIFICATION #superfamily S-locus-specific glycoprotein; S-locus-specific !1glycoprotein homology KEYWORDS glycoprotein FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-444 #product S-locus-specific glycoprotein #status !8predicted #label MAT\ !$37-440 #domain S-locus-specific glycoprotein homology #label !8SSG SUMMARY #length 444 #molecular-weight 50358 #checksum 8256 SEQUENCE /// ENTRY JC2251 #type complete TITLE S-locus-specific glycoprotein S8 precursor - field mustard ALTERNATE_NAMES S8-glycoprotein ORGANISM #formal_name Brassica campestris #common_name field mustard DATE 28-Aug-1985 #sequence_revision 23-Mar-1995 #text_change 26-Feb-1999 ACCESSIONS JC2251; B26424 REFERENCE JC2250 !$#authors Yamakawa, S.; Shiba, H.; Watanabe, M.; Shiozawa, H.; !1Takayama, S.; Hinata, K.; Isogai, A.; Suzuki, A. !$#journal Biosci. Biotechnol. Biochem. (1994) 58:921-925 !$#title The sequences of S-glycoproteins involved in !1self-incompatibility of Brassica campestris and their !1distribution among Brassicaceae. !$#cross-references MUID:94289867; PMID:7764979 !$#accession JC2251 !'##molecule_type mRNA !'##residues 1-435 ##label YAM REFERENCE A93390 !$#authors Takayama, S.; Isogai, A.; Tsukamoto, C.; Ueda, Y.; Hinata, !1K.; Okazaki, K.; Suzuki, A. !$#journal Nature (1987) 326:102-105 !$#title Sequences of S-glycoproteins, products of the Brassica !1campestris self-incompatibility locus. !$#accession B26424 !'##molecule_type protein !'##residues 32-45,'X',47-63,'X',65-72,'Y',74-85,'N',87-98,'X', !1100;102-113,'X',115;116-120,'X',122-149,'X',151-158,'F', !1160-238,'L',240-244,'X',246-259,'XX',262-263,'X',265,'XX', !1270-278,'XXX',282-287,'X',290-291,'X',293-296,'X',298-300, !1304-325;329-358;366-435 ##label TAK COMMENT This protein plays a role in self-incompatibility in !1Brassica plants. The self-incompatibility system is under !1control of a single locus with multiple alleles. CLASSIFICATION #superfamily S-locus-specific glycoprotein; S-locus-specific !1glycoprotein homology KEYWORDS glycoprotein FEATURE !$1-31 #domain signal sequence #status predicted #label SIG\ !$32-435 #product S-locus-specific glycoprotein S8 #status !8experimental #label MAT\ !$40-433 #domain S-locus-specific glycoprotein homology #label !8SSG\ !$46,64,114,121,150, !$245,261 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 435 #molecular-weight 49825 #checksum 4924 SEQUENCE /// ENTRY JC2250 #type complete TITLE S-locus-specific glycoprotein S12 precursor - field mustard ALTERNATE_NAMES S12-glycoprotein; stylar glycoprotein 12 ORGANISM #formal_name Brassica campestris #common_name field mustard DATE 28-Aug-1985 #sequence_revision 23-Mar-1995 #text_change 26-Feb-1999 ACCESSIONS JC2250; PC2166; D26424 REFERENCE JC2250 !$#authors Yamakawa, S.; Shiba, H.; Watanabe, M.; Shiozawa, H.; !1Takayama, S.; Hinata, K.; Isogai, A.; Suzuki, A. !$#journal Biosci. Biotechnol. Biochem. (1994) 58:921-925 !$#title The sequences of S-glycoproteins involved in !1self-incompatibility of Brassica campestris and their !1distribution among Brassicaceae. !$#cross-references MUID:94289867; PMID:7764979 !$#accession JC2250 !'##molecule_type mRNA !'##residues 1-436 ##label YAM !$#accession PC2166 !'##molecule_type protein !'##residues 32-60;78-100;102-152;172-198;202-261;305-346;364-399 !1##label YA2 REFERENCE A93390 !$#authors Takayama, S.; Isogai, A.; Tsukamoto, C.; Ueda, Y.; Hinata, !1K.; Okazaki, K.; Suzuki, A. !$#journal Nature (1987) 326:102-105 !$#title Sequences of S-glycoproteins, products of the Brassica !1campestris self-incompatibility locus. !$#accession D26424 !'##molecule_type protein !'##residues 32-45,'X',47-60;78-100;102-110,'X',112-113,'X',115;114-120, !1'XI',123-152;172-177,179-184,'X',186,'XX',189-190,'X', !1192-198;202-225,'X',227-238;240-245,'X', !1247-261;305-346;370-399 ##label TAK COMMENT This protein plays a role in self-incompatibility in !1Brassica plants. The self-incompatibility system is under !1control of a single locus with multiple alleles. CLASSIFICATION #superfamily S-locus-specific glycoprotein; S-locus-specific !1glycoprotein homology KEYWORDS glycoprotein FEATURE !$1-31 #domain signal sequence #status predicted #label SIG\ !$32-436 #product S-locus-specific glycoprotein S12 #status !8experimental #label MAT\ !$40-434 #domain S-locus-specific glycoprotein homology #label !8SSG\ !$46,121,246 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 436 #molecular-weight 49534 #checksum 3781 SEQUENCE /// ENTRY ZMZM19 #type complete TITLE glutelin 2 precursor (clone pME119) - maize ALTERNATE_NAMES 27K zein; alcohol-soluble reduced glutelin; Zc2 protein ORGANISM #formal_name Zea mays #common_name maize DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 16-Jul-1999 ACCESSIONS A93557; A29017; S12144; A23014 REFERENCE A93557 !$#authors Prat, S.; Cortadas, J.; Puigdomenech, P.; Palau, J. !$#journal Nucleic Acids Res. (1985) 13:1493-1504 !$#title Nucleic acid (cDNA) and amino acid sequences of the maize !1endosperm protein glutelin-2. !$#cross-references MUID:85215560; PMID:3839076 !$#accession A93557 !'##molecule_type mRNA !'##residues 1-223 ##label PR1 !'##cross-references GB:X02230; NID:g22288; PIDN:CAA26149.1; PID:g22289 !'##experimental_source inbred line E-10 REFERENCE A29017 !$#authors Prat, S.; Perez-Grau, L.; Puigdomenech, P. !$#journal Gene (1987) 52:41-49 !$#title Multiple variability in the sequence of a family of maize !1endosperm proteins. !$#cross-references MUID:87248094; PMID:3596247 !$#accession A29017 !'##molecule_type mRNA !'##residues 1-223 ##label PR2 !'##experimental_source inbred lines W64 and W64O2 !'##note the authors called this clone pME125 REFERENCE S12144 !$#authors Reina, M.; Ponte, I.; Guillen, P.; Boronat, A.; Palau, J. !$#journal Nucleic Acids Res. (1990) 18:6426 !$#title Sequence analysis of a genomic clone encoding a Zc2 protein !1from Zea mays W64 A. !$#cross-references MUID:91057132; PMID:2243788 !$#accession S12144 !'##status translation not shown !'##molecule_type DNA !'##residues 1-223 ##label REI !'##cross-references EMBL:X53514; NID:g22516; PIDN:CAA37594.1; !1PID:g22517 !'##experimental_source strain W64A, clone p268c COMMENT Glutelin 2 accounts for about 15% of the total endosperm !1protein and is located on the border of the inner part of !1the membrane of endosperm protein bodies. CLASSIFICATION #superfamily glutelin KEYWORDS duplication; seed; storage protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-223 #product glutelin 2 #status predicted #label MAT\ !$31-36,37-42,43-48, !$49-54,55-60,61-66, !$73-78 #region duplication SUMMARY #length 223 #molecular-weight 23689 #checksum 433 SEQUENCE /// ENTRY ZMZM5 #type complete TITLE glutelin 5 - maize ALTERNATE_NAMES alcohol-soluble reduced glutelin (ASG) ORGANISM #formal_name Zea mays #common_name maize DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 23-Aug-1996 ACCESSIONS A03351 REFERENCE A03351 !$#authors Esen, A.; Bietz, J.A.; Paulis, J.W.; Wall, J.S. !$#journal Nature (1982) 296:678-679 !$#title Tandem repeats in the N-terminal sequence of a proline-rich !1protein from corn endosperm. !$#accession A03351 !'##molecule_type protein !'##residues 1-58 ##label ESE !'##note 9-Cys was found in approximately one-third of the molecules !'##note glutelins are major seed storage proteins CLASSIFICATION #superfamily glutelin KEYWORDS duplication; seed; storage protein SUMMARY #length 58 #molecular-weight 6041 #checksum 1579 SEQUENCE /// ENTRY EEWTHW #type complete TITLE glutenin, high molecular weight chain precursor - wheat ORGANISM #formal_name Triticum aestivum #common_name common wheat DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 16-Jul-1999 ACCESSIONS A24107 REFERENCE A24107 !$#authors Sugiyama, T.; Rafalski, A.; Peterson, D.; Soll, D. !$#journal Nucleic Acids Res. (1985) 13:8729-8737 !$#title A wheat HMW glutenin subunit gene reveals a highly repeated !1structure. !$#cross-references MUID:86093674; PMID:3001648 !$#accession A24107 !'##molecule_type DNA !'##residues 1-838 ##label SUG !'##cross-references GB:X03346; NID:g21784; PIDN:CAA27052.1; PID:g736319 !'##experimental_source cv. Yamhill COMMENT Glutenins, like gliadins, are high in glutamine and proline !1but differ in containing up to 20% glycine. CLASSIFICATION #superfamily glutenin KEYWORDS seed; storage protein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-838 #product glutenin, HMW chain #status predicted #label !8MAT SUMMARY #length 838 #molecular-weight 89175 #checksum 9906 SEQUENCE /// ENTRY EEWT1 #type fragment TITLE glutenin 1 - wheat (fragment) ORGANISM #formal_name Triticum aestivum #common_name common wheat DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 23-Aug-1996 ACCESSIONS A03352 REFERENCE A03353 !$#authors Forde, J.; Forde, B.G.; Fry, R.P.; Kreis, M.; Shewry, P.R.; !1Miflin, B.J. !$#journal FEBS Lett. (1983) 162:360-366 !$#title Identification of barley and wheat cDNA clones related to !1the high-M-r polypeptides of wheat gluten. !$#accession A03352 !'##molecule_type mRNA !'##residues 1-101 ##label FOR CLASSIFICATION #superfamily glutenin KEYWORDS seed; storage protein SUMMARY #length 101 #checksum 4217 SEQUENCE /// ENTRY EEWTA #type complete TITLE alpha/beta-gliadin precursor - wheat ALTERNATE_NAMES prolamin ORGANISM #formal_name Triticum aestivum #common_name common wheat DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 16-Jul-1999 ACCESSIONS A03354 REFERENCE A03354 !$#authors Rafalski, J.A.; Scheets, K.; Metzler, M.; Peterson, D.M.; !1Hedgcoth, C.; Soll, D.G. !$#journal EMBO J. (1984) 3:1409-1415 !$#title Developmentally regulated plant genes: the nucleotide !1sequence of a wheat gliadin genomic clone. !$#cross-references MUID:84261434; PMID:6204862 !$#accession A03354 !'##molecule_type DNA !'##residues 1-286 ##label RAF !'##cross-references GB:X00627; GB:K03076; NID:g21752; PIDN:CAA25261.1; !1PID:g21753 !'##experimental_source cv. Newton COMMENT Gliadin is the major seed storage protein in wheat. CLASSIFICATION #superfamily gliadin KEYWORDS storage protein; tandem repeat FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$16-108 #region 6-residue repeats ([QP]-Q-Q-P-[FY]-P)\ !$21-286 #product gliadin #status predicted #label GLN\ !$116-133 #region glutamine-rich SUMMARY #length 286 #molecular-weight 32948 #checksum 9619 SEQUENCE /// ENTRY EEWTG #type complete TITLE gamma-gliadin B precursor - wheat ORGANISM #formal_name Triticum aestivum #common_name common wheat DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 16-Jul-1999 ACCESSIONS A25632 REFERENCE A25632 !$#authors Rafalski, J.A. !$#journal Gene (1986) 43:221-229 !$#title Structure of wheat gamma-gliadin genes. !$#cross-references MUID:86301876; PMID:3017812 !$#accession A25632 !'##molecule_type DNA !'##residues 1-291 ##label RAF !'##cross-references GB:M13713; NID:g170707; PIDN:AAA34274.1; !1PID:g170708 COMMENT Gliadin, a glutamine and proline rich protein, is a major !1storage protein found in wheat endosperm. CLASSIFICATION #superfamily gliadin KEYWORDS seed; storage protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-291 #product gamma-gliadin B #status predicted #label MAT SUMMARY #length 291 #molecular-weight 32967 #checksum 351 SEQUENCE /// ENTRY JN0696 #type complete TITLE glutenin low molecular weight chain precursor (clone pTdUCD1) - durum wheat ORGANISM #formal_name Triticum durum #common_name durum wheat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JN0696; S08683 REFERENCE JN0696 !$#authors Cassidy, B.G.; Dvorak, J. !$#journal Theor. Appl. Genet. (1991) 81:653-660 !$#title Molecular characterization of a low-molecular-weight !1glutenin cDNA clone from Triticum durum. !$#accession JN0696 !'##molecule_type mRNA !'##residues 1-295 ##label CAS !'##cross-references EMBL:X51759; NID:g21925; PIDN:CAA36063.1; !1PID:g21926 CLASSIFICATION #superfamily gliadin KEYWORDS seed; storage protein FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-295 #product glutenin low molecular weight chain #status !8predicted #label MAT\ !$34-101 #region glutamine/proline-rich SUMMARY #length 295 #molecular-weight 33379 #checksum 4981 SEQUENCE /// ENTRY CVJBP #type complete TITLE concanavalin A precursor - jack bean ORGANISM #formal_name Canavalia ensiformis #common_name jack bean DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 28-May-1999 ACCESSIONS A03357; A60780; A60848 REFERENCE A03357 !$#authors Carrington, D.M.; Auffret, A.; Hanke, D.E. !$#journal Nature (1985) 313:64-67 !$#title Polypeptide ligation occurs during post-translational !1modification of concanavalin A. !$#cross-references MUID:85086270; PMID:3965973 !$#accession A03357 !'##molecule_type mRNA !'##residues 1-290 ##label CAR !'##cross-references GB:X01632; NID:g312382; PIDN:CAA25787.1; PID:g17979 REFERENCE A60780 !$#authors Chrispeels, M.J.; Hartl, P.M.; Sturm, A.; Faye, L. !$#journal J. Biol. Chem. (1986) 261:10021-10024 !$#title Characterization of the endoplasmic reticulum-associated !1precursor of concanavalin A. Partial amino acid sequence and !1lectin activity. !$#cross-references MUID:86278043; PMID:3733700 !$#accession A60780 !'##molecule_type protein !'##residues 30-41;153-169 ##label CHR REFERENCE A60848 !$#authors Bowles, D.J.; Marcus, S.E.; Pappin, D.J.C.; Findlay, J.B.C.; !1Eliopoulos, E.; Maycox, P.R.; Burgess, J. !$#journal J. Cell Biol. (1986) 102:1284-1297 !$#title Posttranslational processing of concanavalin A precursors in !1jackbean cotyledons. !$#cross-references MUID:86168475; PMID:3958046 !$#accession A60848 !'##molecule_type protein !'##residues 30-41;160-173 ##label BOW COMMENT The mature chain (see PIR:CVJB) consists of residues 164-281 !1followed by 30-148. To form a mature ConA chain the !1precursor undergoes further posttranslational modification !1after removal of the signal sequence; cleavage after !1asparagines at positions 148, 163, and 281 is followed by !1transposition and ligation (by formation of a new peptide !1bond) of residues 164-281 and 30-148. CLASSIFICATION #superfamily plant lectin KEYWORDS glycoprotein FEATURE !$1-29 #domain signal sequence #status predicted #label SIG\ !$149-163 #domain glycopeptide #status predicted #label GLP\ !$148-149 #cleavage_site Asn-Val (unidentified proteinase) !8#status experimental\ !$152 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$163-164 #cleavage_site Asn-Ala (unidentified proteinase) !8#status experimental\ !$281-282 #cleavage_site Asn-Glu (unidentified proteinase) !8#status experimental SUMMARY #length 290 #molecular-weight 31521 #checksum 4638 SEQUENCE /// ENTRY CVJB #type complete TITLE concanavalin A - jack bean ORGANISM #formal_name Canavalia ensiformis #common_name jack bean DATE 22-Jun-1981 #sequence_revision 22-Jun-1981 #text_change 08-May-1998 ACCESSIONS A92166; A92167; A44427; A03358 REFERENCE A92166 !$#authors Wang, J.L.; Cunningham, B.A.; Waxdal, M.J.; Edelman, G.M. !$#journal J. Biol. Chem. (1975) 250:1490-1502 !$#title The covalent and three-dimensional structure of concanavalin !1A. I. Amino acid sequence of cyanogen bromide fragments F-1 !1and F-2. !$#cross-references MUID:75095622; PMID:1112813 !$#accession A92166 !'##molecule_type protein !'##residues 1-129 ##label WAN REFERENCE A92167 !$#authors Cunningham, B.A.; Wang, J.L.; Waxdal, M.J.; Edelman, G.M. !$#journal J. Biol. Chem. (1975) 250:1503-1512 !$#title The covalent and three-dimensional structure of concanavalin !1A. II. Amino acid sequence of cyanogen bromide fragment F-3. !$#cross-references MUID:75095623; PMID:1112814 !$#accession A92167 !'##molecule_type protein !'##residues 130-237 ##label CUN REFERENCE A92168 !$#authors Becker, J.W.; Reeke Jr., G.N.; Wang, J.L.; Cunningham, B.A.; !1Edelman, G.M. !$#journal J. Biol. Chem. (1975) 250:1513-1524 !$#title The covalent and three-dimensional structure of concanavalin !1A. III. Structure of the monomer and its interactions with !1metals and saccharides. !$#cross-references MUID:75095624; PMID:1112815 !$#contents annotation; X-ray crystallography, 2.0 angstroms !$#note the molecule is a tetramer of identical chains, each binding !1one manganese (or other transition metal) ion and one !1calcium ion; the metal ions are essential for the !1saccharide-binding and cell-agglutinating activities of !1concanavalin A REFERENCE A44427 !$#authors Machida, S.; Saito, M. !$#journal J. Biol. Chem. (1993) 268:1702-1707 !$#title Purification and characterization of membrane-bound chitin !1synthase. !$#cross-references MUID:93131910; PMID:8420947 !$#accession A44427 !'##molecule_type protein !'##residues 1-20 ##label MAC !'##note although this protein was reported to be chitin synthase (EC !12.4.1.16) from the pin mould Absidia glauca, purification !1included use of ConA-Sepharose and this material is !1undoubtedly concanavalin A itself REFERENCE A92169 !$#authors Reeke Jr., G.N.; Becker, J.W.; Edelman, G.M. !$#journal J. Biol. Chem. (1975) 250:1525-1547 !$#title The covalent and three-dimensional structure of concanavalin !1A. IV. Atomic coordinates, hydrogen bonding, and quaternary !1structure. !$#cross-references MUID:75095625; PMID:1112816 !$#contents annotation !$#note the X-ray crystallographic coordinates are presented and the !1intersubunit interactions are described COMMENT Concanavalin A is derived from its precursor by cleavage, !1transposition of the products, and formation of a new !1peptide bond between Asn-118 and Ser-119. Residues 1-118 and !1119-237 correspond to residues 164-281 and 30-148, !1respectively, in the precursor. COMMENT See the entry for concanavalin A precursor (PIR:CVJBP). CLASSIFICATION #superfamily plant lectin KEYWORDS calcium; glycoprotein; homotetramer; lectin; manganese FEATURE !$118-119 #cross-link peptide (Asn-Ser) #status experimental\ !$118 #binding_site carbohydrate (Asn) (covalent) #status !8absent SUMMARY #length 237 #molecular-weight 25572 #checksum 2912 SEQUENCE /// ENTRY LNLD #type complete TITLE lectin - spring vetchling ORGANISM #formal_name Lathyrus sphaericus #common_name spring vetchling DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 01-May-1998 ACCESSIONS S00002 REFERENCE S00002 !$#authors Richardson, M.; Yarwood, A.; Rouge, P. !$#journal FEBS Lett. (1987) 216:145-150 !$#title The amino acid sequence of an atypical single-chain lectin !1from seeds of Lathyrus sphaericus (Retz). !$#accession S00002 !'##molecule_type protein !'##residues 1-244 ##label RIC !'##note 57-Gly and 98-Ser were also found CLASSIFICATION #superfamily plant lectin KEYWORDS calcium; homodimer; lectin; metalloprotein; seed FEATURE !$1-191 #domain beta chain homolog #label BCH\ !$192-244 #domain alpha chain homolog #label ACH\ !$132,134,136,140 #binding_site calcium (Asp, Phe, Asn, Asp) #status !8predicted SUMMARY #length 244 #molecular-weight 27313 #checksum 2321 SEQUENCE /// ENTRY LNPM #type complete TITLE lectin precursor - garden pea ORGANISM #formal_name Pisum sativum #common_name garden pea DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 16-Jul-1999 ACCESSIONS A26844; A92438; A90627; S22074; S42645; A03359 REFERENCE A26844 !$#authors Gatehouse, J.A.; Bown, D.; Evans, I.M.; Gatehouse, L.N.; !1Jobes, D.; Preston, P.; Croy, R.R.D. !$#journal Nucleic Acids Res. (1987) 15:7642 !$#title Sequence of the seed lectin gene from pea (Pisum sativum !1L.). !$#cross-references MUID:88015625; PMID:3658708 !$#accession A26844 !'##molecule_type DNA !'##residues 1-275 ##label GAT !'##cross-references GB:Y00440; NID:g20769; PIDN:CAA68497.1; PID:g20770 REFERENCE A92438 !$#authors Higgins, T.J.V.; Chandler, P.M.; Zurawski, G.; Button, S.C.; !1Spencer, D. !$#journal J. Biol. Chem. (1983) 258:9544-9549 !$#title The biosynthesis and primary structure of pea seed lectin. !$#cross-references MUID:83265760; PMID:6688253 !$#accession A92438 !'##molecule_type mRNA !'##residues 1-275 ##label HIG !'##experimental_source cv. P1/G 086 !'##note the authors translated the codon CAA for residues 5 and 7 as !1Glu REFERENCE A90627 !$#authors Richardson, C.; Behnke, W.D.; Freisheim, J.H.; Blumenthal, !1K.M. !$#journal Biochim. Biophys. Acta (1978) 537:310-319 !$#title The complete amino acid sequence of the alpha-subunit of pea !1lectin, Pisum sativum. !$#cross-references MUID:79082912; PMID:728447 !$#accession A90627 !'##molecule_type protein !'##residues 218-268,270-271 ##label RIC REFERENCE S22074 !$#authors de Pater, B.S.; Pham, K.T.; Katagiri, F.; Chua, N.H.; Kijne, !1J.W. !$#submission submitted to the EMBL Data Library, May 1992 !$#description Seed-specific and developmental regulated expression. !$#accession S22074 !'##molecule_type DNA !'##residues 1-275 ##label DEP !'##cross-references EMBL:X66368; NID:g562782; PIDN:CAA47011.1; !1PID:g20804 !'##experimental_source var. Feldham First REFERENCE S42645 !$#authors Hoedemaeker, F.J.; Richardson, M.; Diaz, C.L.; de Pater, !1B.S.; Kijne, J.W. !$#journal Plant Mol. Biol. (1994) 24:75-81 !$#title Pea (Pisum sativum L.) seed isolectins 1 and 2 and pea root !1lectin result from carboxypeptidase-like processing of a !1single gene product. !$#cross-references MUID:94154245; PMID:8111028 !$#accession S42645 !'##molecule_type mRNA !'##residues !131-54;56-91;100-113;116-129;135-149;154-163;166-183;185-187; !1197-200;204-211 ##label HOE GENETICS !$#gene LecA !$#introns #status absent CLASSIFICATION #superfamily plant lectin KEYWORDS calcium; glycoprotein; lectin; metalloprotein; seed FEATURE !$1-30 #domain signal sequence #status predicted #label SIG\ !$31-217 #domain beta chain #status predicted #label BCH\ !$31-217,218-275 #product lectin #status predicted #label MAT\ !$218-275 #domain alpha chain #status experimental #label ACH\ !$29,217 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$151,153,155,159 #binding_site calcium (Asp, Phe, Asn, Asp) #status !8predicted SUMMARY #length 275 #molecular-weight 30270 #checksum 7300 SEQUENCE /// ENTRY LNVTAC #type complete TITLE lectin alpha chain, mannose/glucose-specific - bird vetch ORGANISM #formal_name Vicia cracca #common_name bird vetch DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 23-Aug-1996 ACCESSIONS A03360 REFERENCE A03360 !$#authors Baumann, C.M.; Strosberg, A.D.; Rudiger, H. !$#journal Eur. J. Biochem. (1982) 122:105-110 !$#title Purification and characterization of a mannose/ !1glucose-specific lectin from Vicia cracca. !$#cross-references MUID:82138814; PMID:7060560 !$#accession A03360 !'##molecule_type protein !'##residues 1-53 ##label BAU CLASSIFICATION #superfamily plant lectin KEYWORDS lectin SUMMARY #length 53 #molecular-weight 5767 #checksum 603 SEQUENCE /// ENTRY LNLDAO #type complete TITLE lectin alpha chain - sweet pea ORGANISM #formal_name Lathyrus odoratus #common_name sweet pea DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 23-Aug-1996 ACCESSIONS A03361 REFERENCE A03361 !$#authors Sletten, K.; Kolberg, J.; Michaelsen, T.E. !$#journal FEBS Lett. (1983) 156:253-256 !$#title The amino acid sequence of the alpha-subunit of a mitogenic !1lectin from seeds of Lathyrus odoratus. !$#accession A03361 !'##molecule_type protein !'##residues 1-54 ##label SLE CLASSIFICATION #superfamily plant lectin KEYWORDS lectin SUMMARY #length 54 #molecular-weight 5823 #checksum 3370 SEQUENCE /// ENTRY LNLD2C #type complete TITLE lectin alpha-2 chain - flat-pod pea ORGANISM #formal_name Lathyrus cicera #common_name flat-pod pea DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 23-Aug-1996 ACCESSIONS B26148 REFERENCE A93761 !$#authors Sousa-Cavada, B.; Richardson, M.; Yarwood, A.; Pere, D.; !1Rouge, P. !$#journal Phytochemistry (1986) 25:115-118 !$#title The amino acid sequences of the alpha subunits of the !1lectins from Lathyrus cicera, L. alphaca and L. articulatus. !$#accession B26148 !'##molecule_type protein !'##residues 1-53 ##label SOU CLASSIFICATION #superfamily plant lectin KEYWORDS lectin; seed; storage protein SUMMARY #length 53 #molecular-weight 5781 #checksum 8918 SEQUENCE /// ENTRY LNLD2H #type complete TITLE lectin alpha-2 chain - rough pea ALTERNATE_NAMES alpha lectin; LhL2 isolectin; light chain lectin ORGANISM #formal_name Lathyrus hirsutus #common_name rough pea, hairy vetchling DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 23-Aug-1996 ACCESSIONS JA0003 REFERENCE A93762 !$#authors Yarwood, A.; Richardson, M.; Sousa-Cavada, B.; Pere, D.; !1Rouge, P. !$#journal Phytochemistry (1986) 25:2109-2112 !$#title The amino acid sequences of the alpha subunits of the !1lectins from the seeds of Lathyrus hirsutus and Lathyrus !1tingitanus. !$#accession JA0003 !'##molecule_type protein !'##residues 1-53 ##label YAR CLASSIFICATION #superfamily plant lectin KEYWORDS lectin; seed; storage protein SUMMARY #length 53 #molecular-weight 5709 #checksum 9014 SEQUENCE /// ENTRY LNLD1H #type complete TITLE lectin alpha-1 chain - rough pea ALTERNATE_NAMES alpha lectin; LhL1 isolectin; light chain lectin ORGANISM #formal_name Lathyrus hirsutus #common_name rough pea, hairy vetchling DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 23-Aug-1996 ACCESSIONS JA0002 REFERENCE A93762 !$#authors Yarwood, A.; Richardson, M.; Sousa-Cavada, B.; Pere, D.; !1Rouge, P. !$#journal Phytochemistry (1986) 25:2109-2112 !$#title The amino acid sequences of the alpha subunits of the !1lectins from the seeds of Lathyrus hirsutus and Lathyrus !1tingitanus. !$#accession JA0002 !'##molecule_type protein !'##residues 1-54 ##label YAR COMMENT The two-chain legume lectins contain three domains and are !1highly conserved. CLASSIFICATION #superfamily plant lectin KEYWORDS lectin; seed; storage protein SUMMARY #length 54 #molecular-weight 5837 #checksum 3070 SEQUENCE /// ENTRY LNLD1C #type complete TITLE lectin alpha-1 chain - flat-pod pea ORGANISM #formal_name Lathyrus cicera #common_name flat-pod pea DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 23-Aug-1996 ACCESSIONS A26148 REFERENCE A93761 !$#authors Sousa-Cavada, B.; Richardson, M.; Yarwood, A.; Pere, D.; !1Rouge, P. !$#journal Phytochemistry (1986) 25:115-118 !$#title The amino acid sequences of the alpha subunits of the !1lectins from Lathyrus cicera, L. alphaca and L. articulatus. !$#accession A26148 !'##molecule_type protein !'##residues 1-54 ##label SOU !'##note 53-Val was also found CLASSIFICATION #superfamily plant lectin KEYWORDS lectin; seed; storage protein SUMMARY #length 54 #molecular-weight 5910 #checksum 2974 SEQUENCE /// ENTRY LNLDAT #type complete TITLE lectin alpha chain - Tangier pea ALTERNATE_NAMES light chain lectin ORGANISM #formal_name Lathyrus tingitanus #common_name Tangier pea DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 23-Aug-1996 ACCESSIONS JA0004 REFERENCE A93762 !$#authors Yarwood, A.; Richardson, M.; Sousa-Cavada, B.; Pere, D.; !1Rouge, P. !$#journal Phytochemistry (1986) 25:2109-2112 !$#title The amino acid sequences of the alpha subunits of the !1lectins from the seeds of Lathyrus hirsutus and Lathyrus !1tingitanus. !$#accession JA0004 !'##molecule_type protein !'##residues 1-54 ##label YAR CLASSIFICATION #superfamily plant lectin KEYWORDS lectin; seed; storage protein SUMMARY #length 54 #molecular-weight 5996 #checksum 2763 SEQUENCE /// ENTRY LNLDAF #type complete TITLE lectin alpha chain - yellow vetchling ORGANISM #formal_name Lathyrus aphaca #common_name yellow vetchling DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 23-Aug-1996 ACCESSIONS C26148 REFERENCE A93761 !$#authors Sousa-Cavada, B.; Richardson, M.; Yarwood, A.; Pere, D.; !1Rouge, P. !$#journal Phytochemistry (1986) 25:115-118 !$#title The amino acid sequences of the alpha subunits of the !1lectins from Lathyrus cicera, L. alphaca and L. articulatus. !$#accession C26148 !'##molecule_type protein !'##residues 1-53 ##label SOU CLASSIFICATION #superfamily plant lectin KEYWORDS lectin; seed; storage protein SUMMARY #length 53 #molecular-weight 5634 #checksum 212 SEQUENCE /// ENTRY LNLDAA #type complete TITLE lectin alpha chain - Lathyrus clymenum ORGANISM #formal_name Lathyrus clymenum DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 23-Aug-1996 ACCESSIONS D26148 REFERENCE A93761 !$#authors Sousa-Cavada, B.; Richardson, M.; Yarwood, A.; Pere, D.; !1Rouge, P. !$#journal Phytochemistry (1986) 25:115-118 !$#title The amino acid sequences of the alpha subunits of the !1lectins from Lathyrus cicera, L. alphaca and L. articulatus. !$#accession D26148 !'##molecule_type protein !'##residues 1-53 ##label SOU CLASSIFICATION #superfamily plant lectin KEYWORDS lectin; seed; storage protein SUMMARY #length 53 #molecular-weight 5759 #checksum 9244 SEQUENCE /// ENTRY LNLWBA #type fragments TITLE lectin precursor [validated] - lentil (fragments) ORGANISM #formal_name Lens culinaris #common_name lentil DATE 25-Feb-1985 #sequence_revision 01-May-1998 #text_change 15-Sep-2000 ACCESSIONS A48694; A92324; A93817; A03362 REFERENCE A48694 !$#authors Loris, R.; Steyaert, J.; Maes, D.; Lisgarten, J.; !1Pickersgill, R.; Wyns, L. !$#journal Biochemistry (1993) 32:8772-8781 !$#title Crystal structure determination and refinement at !12.3-angstrom resolution of the lentil lectin. !$#cross-references MUID:93372081; PMID:8364026 !$#accession A48694 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type DNA !'##residues 20-181;182-202 ##label LOR !'##note this sequence has been corrected in A58806 REFERENCE A58806 !$#authors Loris, R.; Steyaert, J.; Maes, D.; Lisgarten, J.; !1Pickersgill, R.; Wyns, L. !$#journal Biochemistry (1993) 32:14229 !$#cross-references MUID:94083431; PMID:8260509 !$#contents annotation; erratum REFERENCE A92324 !$#authors Foriers, A.; Lebrun, E.; Van Rapenbusch, R.; de Neve, R.; !1Strosberg, A.D. !$#journal J. Biol. Chem. (1981) 256:5550-5560 !$#title The structure of the lentil (Lens culinaris) lectin. Amino !1acid sequence determination and prediction of the secondary !1structure. !$#cross-references MUID:81215459; PMID:7240155 !$#accession A92324 !'##molecule_type protein !'##residues 1-26,'GKEG',31-35,'VSKETG',42-57,'V',59-65,'NGSQVFRESPNG', !177-104,'Y',105,'G',107-157 ##label FO1 REFERENCE A93817 !$#authors Foriers, A.; de Neve, R.; Kanarek, L.; Strosberg, A.D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1978) 75:1136-1139 !$#title Common ancestor for concanavalin A and lentil lectin? !$#cross-references MUID:78178992; PMID:274705 !$#accession A93817 !'##molecule_type protein !'##residues 182-233 ##label FO2 REFERENCE A51479 !$#authors Loris, R.; Steyaert, J.; Maes, D.; Lisgarten, J.; !1Pickersgill, R.; Wyns, L. !$#submission submitted to the Brookhaven Protein Data Bank, June 1993 !$#cross-references PDB:2LAL !$#contents annotation; X-ray crystallography, 1.8 angstroms, residues !11-181;182-228 REFERENCE A51820 !$#authors Loris, R.; Wyns, L. !$#submission submitted to the Brookhaven Protein Data Bank, November 1993 !$#cross-references PDB:1LEM !$#contents annotation; X-ray crystallography, 3.0 angstroms, residues !11-181;182-228 REFERENCE A51821 !$#authors Van Overberge, D.; Loris, R.; Wyns, L. !$#submission submitted to the Brookhaven Protein Data Bank, November 1993 !$#cross-references PDB:1LEN !$#contents annotation; X-ray crystallography, 1.8 angstroms, residues !11-181;182-228 REFERENCE A66034 !$#authors Hamelryck, T.; Loris, R. !$#submission submitted to the Brookhaven Protein Data Bank, August 1995 !$#cross-references PDB:1LES !$#contents annotation; X-ray crystallography, 1.9 angstroms, residues !11-181;182-228 COMPLEX heterotetramer of two alpha and two beta chains CLASSIFICATION #superfamily plant lectin KEYWORDS calcium; glycoprotein; heterotetramer; lectin; manganese; !1metalloprotein FEATURE !$1-181 #domain beta chain #status experimental #label BCH\ !$1-181,182-233 #product lectin #status experimental #label MAT\ !$182-233 #domain alpha chain #status experimental #label ACH\ !$119,121,129,136 #binding_site manganese (Glu, Asp, Asp, His) #status !8experimental\ !$121,123,125,129 #binding_site calcium (Asp, Phe, Asn, Asp) #status !8experimental SUMMARY #length 233 #checksum 628 SEQUENCE /// ENTRY FVVFBA #type fragments TITLE favin precursor - fava bean (fragments) ORGANISM #formal_name Vicia faba #common_name fava bean DATE 25-Feb-1985 #sequence_revision 08-May-1998 #text_change 08-May-1998 ACCESSIONS A92369; A92257; A03363 REFERENCE A92369 !$#authors Hopp, T.P.; Hemperly, J.J.; Cunningham, B.A. !$#journal J. Biol. Chem. (1982) 257:4473-4483 !$#title Amino acid sequence and variant forms of favin, a lectin !1from Vicia faba. !$#cross-references MUID:82167535; PMID:7068646 !$#accession A92369 !'##molecule_type protein !'##residues 1-182 ##label HOP REFERENCE A92257 !$#authors Hemperly, J.J.; Hopp, T.P.; Becker, J.W.; Cunningham, B.A. !$#journal J. Biol. Chem. (1979) 254:6803-6810 !$#title The chemical characterization of favin, a lectin isolated !1from Vicia faba. !$#cross-references MUID:79194284; PMID:447749 !$#accession A92257 !'##molecule_type protein !'##residues 183-233 ##label HEM COMPLEX heterodimer of alpha and beta chains CLASSIFICATION #superfamily plant lectin KEYWORDS calcium; glycoprotein; heterodimer; metalloprotein FEATURE !$1-182 #domain beta chain #status experimental #label BCH\ !$1-182,183-233 #product lectin #status experimental #label MAT\ !$183-233 #domain alpha chain #status experimental #label ACH\ !$122,124,126,130 #binding_site calcium (Asp, Phe, Asn, Asp) #status !8predicted\ !$168 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 233 #checksum 7876 SEQUENCE /// ENTRY LNNPG #type complete TITLE lectin - peanut (tentative sequence) ALTERNATE_NAMES agglutinin ORGANISM #formal_name Arachis hypogaea #common_name peanut DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 23-Aug-1996 ACCESSIONS A03364 REFERENCE A03364 !$#authors Lauwereys, M.; Foriers, A.; Sharon, N.; Strosberg, A.D. !$#journal FEBS Lett. (1985) 181:241-244 !$#title Sequence studies of peanut agglutinin. !$#contents var. Shulamit, compositions of tryptic peptides and sequence !1of residues 1-40 !$#accession A03364 !'##molecule_type protein !'##residues 1-161 ##label LAU !'##note the tryptic peptides were positioned by homology with the !1lectins of soybean and broad bean CLASSIFICATION #superfamily plant lectin KEYWORDS lectin; seed; storage protein SUMMARY #length 161 #molecular-weight 17392 #checksum 3592 SEQUENCE /// ENTRY LNFB #type complete TITLE lectin precursor - kidney bean ALTERNATE_NAMES heat-labile alpha-amylase inhibitor ORGANISM #formal_name Phaseolus vulgaris #common_name kidney bean DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 16-Jul-1999 ACCESSIONS A03365; A27350; PQ0539; PQ0541; PQ0540 REFERENCE A03365 !$#authors Hoffman, L.M. !$#journal J. Mol. Appl. Genet. (1984) 2:447-453 !$#title Structure of a chromosomal Phaseolus vulgaris lectin gene !1and its transcript. !$#cross-references MUID:85008540; PMID:6090563 !$#accession A03365 !'##molecule_type DNA !'##residues 1-246 ##label HOF !'##cross-references GB:J01261; NID:g169354; PIDN:AAA33769.1; !1PID:g169355 !'##experimental_source cv. Tendergreen REFERENCE A27350 !$#authors Hoffman, L.M.; Ma, Y.; Barker, R.F. !$#journal Nucleic Acids Res. (1982) 10:7819-7828 !$#title Molecular cloning of Phaseolus vulgaris lectin mRNA and use !1of cDNA as a probe to estimate lectin transcript levels in !1various tissues. !$#cross-references MUID:83116994; PMID:6897567 !$#accession A27350 !'##molecule_type mRNA !'##residues 1-246 ##label HO2 !'##cross-references GB:J01261; NID:g169354; PIDN:AAA33769.1; !1PID:g169355 !'##experimental_source cv. Tendergreen !'##note the authors translated the codon GAG for residue 157 as Val !'##note translation of residues 1-2 not shown REFERENCE PQ0539 !$#authors Yamaguchi, H. !$#journal Biosci. Biotechnol. Biochem. (1993) 57:297-302 !$#title Isolation and characterization of the subunits of a !1heat-labile alpha-amylase inhibitor from Phaseolus vulgaris !1white kidney bean. !$#cross-references MUID:93214116; PMID:7763497 !$#accession PQ0539 !'##molecule_type protein !'##residues 24-29,'N',31-32 ##label YA1 !'##experimental_source seed, strain Tebo !'##note amino end of gamma chain; gamma chain has composition similar !1to alpha and beta chains together !$#accession PQ0541 !'##molecule_type protein !'##residues 24-29,'N',31-32 ##label YA2 !'##experimental_source seed, strain Tebo !'##note amino end of alpha chain !$#accession PQ0540 !'##molecule_type protein !'##residues 101-109 ##label YA3 !'##experimental_source seed, strain Tebo !'##note amino end of beta chain CLASSIFICATION #superfamily plant lectin KEYWORDS glycoprotein; heterotetramer; lectin; seed; storage protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-246 #product lectin #status predicted #label LEC\ !$35,88,163,183 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 246 #molecular-weight 27207 #checksum 7910 SEQUENCE /// ENTRY LNOJ #type complete TITLE lectin - common sainfoin ORGANISM #formal_name Onobrychis viciifolia #common_name common sainfoin DATE 15-Nov-1984 #sequence_revision 15-Nov-1984 #text_change 01-May-1998 ACCESSIONS A03366 REFERENCE A03366 !$#authors Kouchalakos, R.N.; Bates, O.J.; Bradshaw, R.A.; Hapner, K.D. !$#journal Biochemistry (1984) 23:1824-1830 !$#title Lectin from sainfoin (Onobrychis viciifolia Scop.). Complete !1amino acid sequence. !$#cross-references MUID:84203555; PMID:6722125 !$#accession A03366 !'##molecule_type protein !'##residues 1-236 ##label KOU !'##note half of the chains have 49-Ile COMMENT This lectin has D-mannose (D-glucose) binding activity. The !1active molecule consists of two identical, noncovalently !1associated chains. CLASSIFICATION #superfamily plant lectin KEYWORDS calcium; glycoprotein; lectin; metalloprotein FEATURE !$118 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$127,129,131,134 #binding_site calcium (Asp, Phe, Asn, Asp) #status !8predicted SUMMARY #length 236 #molecular-weight 26499 #checksum 4432 SEQUENCE /// ENTRY LNHUGB #type complete TITLE galectin 1 [validated] - human ALTERNATE_NAMES 14K lectin; brain lectin; galaptin; laminin-binding protein HLBP14; soluble beta-galactoside-binding lectin 1 ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 08-Dec-2000 ACCESSIONS A37134; S04330; S03866; A40299; I55292; A31038; JC1092; !1S04998; S24167; C26495; A26761 REFERENCE A37134 !$#authors Gitt, M.A.; Barondes, S.H. !$#journal Biochemistry (1991) 30:82-89 !$#title Genomic sequence and organization of two members of a human !1lectin gene family. !$#cross-references MUID:91105104; PMID:1988031 !$#accession A37134 !'##molecule_type DNA !'##residues 1-135 ##label GIT !'##cross-references GB:J05303; GB:M57678; NID:g184227; PIDN:AAB00777.1; !1PID:g184228 !'##experimental_source clone 182 REFERENCE S04330 !$#authors Hirabayashi, J.; Ayaki, H.; Soma, G.I.; Kasai, K.I. !$#journal Biochim. Biophys. Acta (1989) 1008:85-91 !$#title Cloning and nucleotide sequence of a full-length cDNA for !1human 14 kDa beta-galactoside-binding lectin. !$#cross-references MUID:89247452; PMID:2719964 !$#accession S04330 !'##molecule_type mRNA !'##residues 1-135 ##label HIR1 !'##cross-references EMBL:X14829; NID:g34342; PIDN:CAA32938.1; !1PID:g34343 REFERENCE S03866 !$#authors Abbott, W.M.; Feizi, T. !$#journal Biochem. J. (1989) 259:291-294 !$#title Evidence that the 14 kDa soluble beta-galactoside-binding !1lectin in man is encoded by a single gene. !$#cross-references MUID:89246318; PMID:2719646 !$#accession S03866 !'##molecule_type mRNA !'##residues 1-135 ##label ABB !'##cross-references EMBL:X15256; NID:g23238; PIDN:CAA33328.1; !1PID:g4377694 REFERENCE A40299 !$#authors Allen, H.J.; Gottstine, S.; Sharma, A.; DiCioccio, R.A.; !1Swank, R.T.; Li, H. !$#journal Biochemistry (1991) 30:8904-8910 !$#title Synthesis, isolation, and characterization of endogenous !1beta-galactoside-binding lectins in human leukocytes. !$#cross-references MUID:91363388; PMID:1888747 !$#accession A40299 !'##molecule_type mRNA !'##residues 7-66;85-115;119-127 ##label ALL !'##cross-references GB:J05338 REFERENCE I55292 !$#authors Couraud, P. !$#journal J. Biol. Chem. (1989) 264:1310-1316 !$#title Molecular cloning, characterization, and expression of a !1human 14-kDa lectin. !$#cross-references MUID:89093123; PMID:2910856 !$#accession I55292 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-135 ##label RES !'##cross-references GB:J04456; NID:g187109; PIDN:AAA36170.1; !1PID:g307122 REFERENCE A31038 !$#authors Hirabayashi, J.; Kasai, K. !$#journal J. Biochem. (1988) 104:1-4 !$#title Complete amino acid sequence of a beta-galactoside-binding !1lectin from human placenta. !$#cross-references MUID:89123203; PMID:3065332 !$#accession A31038 !'##molecule_type protein !'##residues 2-135 ##label HIR2 !'##experimental_source placenta REFERENCE JC1092 !$#authors Wang, Y.J. !$#journal Prog. Biochem. Biophys. (1993) 20:435-436 !$#title Human brain lectin (HBL). !$#accession JC1092 !'##molecule_type protein !'##residues 2-135 ##label WAN !'##experimental_source brain REFERENCE S04998 !$#authors Hirabayashi, J.; Ayaki, H.; Soma, G.I.; Kasai, K.I. !$#journal FEBS Lett. (1989) 250:161-165 !$#title Production and purification of a recombinant human 14 kDa !1beta-galactoside-binding lectin. !$#cross-references MUID:89325559; PMID:2666155 !$#accession S04998 !'##molecule_type protein !'##residues 2,'X',4-16,'X',18-40 ##label HIR !'##experimental_source recombinant protein expressed in E. coli REFERENCE S24167 !$#authors Castronovo, V.; Luyten, F.; van den Brule, F.; Sobel, M.E. !$#journal Arch. Biochem. Biophys. (1992) 297:132-138 !$#title Identification of a 14-kDa laminin binding protein (HLBP14) !1in human melanoma cells that is identical to the 14-kDa !1galactoside binding lectin. !$#cross-references MUID:92344405; PMID:1386213 !$#accession S24167 !'##status preliminary !'##molecule_type protein !'##residues 20-29;50-64;65-74;132-135 ##label CAS REFERENCE A94130 !$#authors Gitt, M.A.; Barondes, S.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:7603-7607 !$#title Evidence that a human soluble beta-galactoside-binding !1lectin is encoded by a family of genes. !$#cross-references MUID:87016997; PMID:3020551 !$#accession C26495 !'##molecule_type protein !'##residues 22-42,'X',44;66-70,'XX',73,75-78,'Y',80,'X',82;101-102,'X', !1104-105,'Q',107-120 ##label GI2 REFERENCE A26761 !$#authors Hirabayashi, J.; Kawasaki, H.; Suzuki, K.; Kasai, K. !$#journal J. Biochem. (1987) 101:987-995 !$#title Further characterization and structural studies on human !1placenta lectin. !$#cross-references MUID:87279994; PMID:3611046 !$#accession A26761 !'##molecule_type protein !'##residues 70-84,'X',86-87;122-135 ##label HI2 !'##experimental_source placenta COMMENT The lectin is inactivated upon the formation of disulfide !1bonds. GENETICS !$#gene GDB:LGALS1 !'##cross-references GDB:126889; OMIM:150570 !$#map_position 22q12-22q13.1 CLASSIFICATION #superfamily beta-galactoside-binding lectin KEYWORDS acetylated amino end; glycoprotein; lectin FEATURE !$2-135 #product beta-galactoside-binding lectin #status !8experimental #label MAT\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status predicted\ !$96 #binding_site carbohydrate (Asn) (covalent) #status !8absent SUMMARY #length 135 #molecular-weight 14716 #checksum 5017 SEQUENCE /// ENTRY LNMSGB #type complete TITLE beta-galactoside-binding lectin - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS S11718; S05412; A44883; S15894; A34675; A38438 REFERENCE S11718 !$#authors Wilson, T.J.G.; Harrison, F.L. !$#submission submitted to the EMBL Data Library, May 1990 !$#accession S11718 !'##molecule_type mRNA !'##residues 1-135 ##label EMB !'##cross-references EMBL:X53067; NID:g49697; PIDN:CAA37242.1; !1PID:g49698 REFERENCE S05412 !$#authors Wilson, T.J.G.; Firth, M.N.; Powell, J.T.; Harrison, F.L. !$#journal Biochem. J. (1989) 261:847-852 !$#title The sequence of the mouse 14 kDa beta-galactoside-binding !1lectin and evidence for its synthesis on free cytoplasmic !1ribosomes. !$#cross-references MUID:90026277; PMID:2803247 !$#accession S05412 !'##molecule_type mRNA !'##residues 21-135 ##label WIL !'##cross-references EMBL:X15986 REFERENCE A44883 !$#authors Poirier, F.; Timmons, P.M.; Chan, C.T.; Guenet, J.L.; Rigby, !1P.W. !$#journal Development (1992) 115:143-155 !$#title Expression of the L14 lectin during mouse embryogenesis !1suggests multiple roles during pre- and post-implantation !1development. !$#cross-references MUID:92347174; PMID:1638977 !$#accession A44883 !'##molecule_type mRNA !'##residues 1-135 ##label POI !'##cross-references GB:X66532; GB:S41202; NID:g395927; PIDN:CAA47143.1; !1PID:g395928 !'##experimental_source embryo !'##note sequence extracted from NCBI backbone (NCBIN:109808, !1NCBIP:109809) REFERENCE S15894 !$#authors Chiariotti, L.; Wells, V.; Bruni, C.B.; Mallucci, L. !$#journal Biochim. Biophys. Acta (1991) 1089:54-60 !$#title Structure and expression of the negative growth factor mouse !1beta-galactoside binding protein gene. !$#cross-references MUID:91223098; PMID:2025648 !$#accession S15894 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-135 ##label BIO !'##cross-references GB:X51577; NID:g50149; PIDN:CAA35930.1; PID:g817944 REFERENCE A34675 !$#authors Cooper, D.N.W.; Barondes, S.H. !$#journal J. Cell Biol. (1990) 110:1681-1691 !$#title Evidence for export of a muscle lectin from cytosol to !1extracellular matrix and for a novel secretory mechanism. !$#cross-references MUID:90243778; PMID:2335567 !$#accession A34675 !'##molecule_type mRNA !'##residues 1-135 ##label COO !'##cross-references GB:X51903 REFERENCE A38438 !$#authors Wells, V.; Mallucci, L. !$#journal Cell (1991) 64:91-97 !$#title Identification of an autocrine negative growth factor: mouse !1beta-galactoside-binding protein is a cytostatic factor and !1cell growth regulator. !$#cross-references MUID:91098658; PMID:1986871 !$#accession A38438 !'##molecule_type mRNA !'##residues 1-77,'S',79-135 ##label WEL !'##cross-references GB:M57470; NID:g193441; PIDN:AAA37667.1; !1PID:g193442 !'##note the authors translated the codon TCC for residue 78 as Phe COMMENT The lectin is inactivated upon the formation of disulfide !1bonds. GENETICS !$#introns 3/3; 30/2; 87/3 CLASSIFICATION #superfamily beta-galactoside-binding lectin KEYWORDS acetylated amino end; lectin FEATURE !$2-135 #product beta-galactoside-binding lectin #status !8predicted #label MAT\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status predicted SUMMARY #length 135 #molecular-weight 14866 #checksum 3336 SEQUENCE /// ENTRY LNRTGB #type complete TITLE beta-galactoside-binding lectin - rat ALTERNATE_NAMES 14K lectin ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS A28703; A37025 REFERENCE A28703 !$#authors Clerch, L.B.; Whitney, P.; Hass, M.; Brew, K.; Miller, T.; !1Werner, R.; Massaro, D. !$#journal Biochemistry (1988) 27:692-699 !$#title Sequence of a full-length cDNA for rat lung !1beta-galactoside-binding protein: primary and secondary !1structure of the lectin. !$#cross-references MUID:88163654; PMID:3349058 !$#accession A28703 !'##molecule_type mRNA !'##residues 1-135 ##label CLE !'##cross-references GB:M19036; NID:g203161; PIDN:AAA40822.1; !1PID:g203162 REFERENCE A37025 !$#authors Hynes, M.A.; Gitt, M.; Barondes, S.H.; Jessell, T.M.; Buck, !1L.B. !$#journal J. Neurosci. (1990) 10:1004-1013 !$#title Selective expression of an endogenous lactose-binding lectin !1gene in subsets of central and peripheral neurons. !$#cross-references MUID:90203973; PMID:2319298 !$#accession A37025 !'##molecule_type mRNA !'##residues 1-135 ##label HYN !'##experimental_source brain COMMENT The lectin is inactivated upon the formation of disulfide !1bonds. CLASSIFICATION #superfamily beta-galactoside-binding lectin KEYWORDS acetylated amino end; lectin FEATURE !$2-135 #product beta-galactoside-binding lectin #status !8predicted #label MAT\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status predicted SUMMARY #length 135 #molecular-weight 14857 #checksum 3224 SEQUENCE /// ENTRY LNBOGB #type complete TITLE beta-galactoside-binding lectin - bovine ALTERNATE_NAMES 14K lectin ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS S03865; A38132; A26756 REFERENCE S03865 !$#authors Abbott, W.M.; Mellor, A.; Edwards, Y.; Feizi, T. !$#journal Biochem. J. (1989) 259:283-290 !$#title Soluble bovine galactose-binding lectin: cDNA cloning !1reveals the complete amino acid sequence and an antigenic !1relationship with the major encephalitogenic domain of !1myelin basic protein. !$#cross-references MUID:89246317; PMID:2470348 !$#accession S03865 !'##molecule_type mRNA !'##residues 1-135 ##label ABB !'##cross-references EMBL:X14330; NID:g517; PIDN:CAA32508.1; PID:g518 REFERENCE A38132 !$#authors Tracey, B.M.; Feizi, T.; Abbott, W.M.; Carruthers, R.A.; !1Green, B.N.; Lawson, A.M. !$#journal J. Biol. Chem. (1992) 267:10342-10347 !$#title Subunit molecular mass assignment of 14,654 Da to the !1soluble beta-galactoside-binding lectin from bovine heart !1muscle and demonstration of intramolecular disulfide bonding !1associated with oxidative inactivation. !$#cross-references MUID:92268070; PMID:1587821 !$#accession A38132 !'##molecule_type protein !'##residues 2-135 ##label TRA !'##experimental_source heart !'##note sequence extracted from NCBI backbone (NCBIP:103655) REFERENCE A26756 !$#authors Southan, C.; Aitken, A.; Childs, R.A.; Abbott, W.M.; Feizi, !1T. !$#journal FEBS Lett. (1987) 214:301-304 !$#title Amino acid sequence of beta-galactoside-binding bovine heart !1lectin. Member of a novel class of vertebrate proteins. !$#cross-references MUID:87190976; PMID:3569527 !$#accession A26756 !'##molecule_type protein !'##residues 'L',12-16,'E',18-42,'Y',44-57,'L',59-60,'S',62-64,'K', !166-88,'E',90-91,'S',93-130,'E',132-134 ##label SOU !'##experimental_source heart !'##note residues 17, 43, 61, 65, 89, 92, and 131 have been revised in !1reference S03865 CLASSIFICATION #superfamily beta-galactoside-binding lectin KEYWORDS acetylated amino end; lectin FEATURE !$2-135 #product beta-galactoside-binding lectin #status !8experimental #label MAT\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental\ !$3-131,17-89,43-61 #disulfide_bonds (in inactive form) #status !8experimental SUMMARY #length 135 #molecular-weight 14744 #checksum 5409 SEQUENCE /// ENTRY LNCH14 #type complete TITLE 14K beta-galactoside-binding lectin - chicken ALTERNATE_NAMES 14K lectin ORGANISM #formal_name Gallus gallus #common_name chicken DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jun-2000 ACCESSIONS JX0042; JT0009; A24062 REFERENCE JX0042 !$#authors Ohyama, Y.; Kasai, K. !$#journal J. Biochem. (1988) 104:173-177 !$#title Isolation and characterization of the chick 14K !1beta-galactoside-binding lectin gene. !$#cross-references MUID:89033999; PMID:3182759 !$#accession JX0042 !'##molecule_type DNA !'##residues 1-135 ##label OHY !'##cross-references GB:D00311; NID:g222798; PIDN:BAA00214.1; !1PID:g222800 REFERENCE JT0009 !$#authors Hirabayashi, J.; Kawasaki, H.; Suzuki, K.; Kasai, K.I. !$#journal J. Biochem. (1987) 101:775-783 !$#title Complete amino acid sequence of 14 kDa !1beta-galactoside-binding lectin of chick embryo. !$#cross-references MUID:87250364; PMID:3597352 !$#accession JT0009 !'##molecule_type protein !'##residues 2-110,112-135 ##label HIR REFERENCE A24062 !$#authors Ohyama, Y.; Hirabayashi, J.; Oda, Y.; Ohno, S.; Kawasaki, !1H.; Suzuki, K.; Kasai, K. !$#journal Biochem. Biophys. Res. Commun. (1986) 134:51-56 !$#title Nucleotide sequence of chick 14K beta-galactoside-binding !1lectin mRNA. !$#cross-references MUID:86130505; PMID:3004444 !$#accession A24062 !'##molecule_type mRNA !'##residues 12-135 ##label OH2 GENETICS !$#introns 3/3; 30/2; 118/3 CLASSIFICATION #superfamily beta-galactoside-binding lectin KEYWORDS acetylated amino end; lectin FEATURE !$2-135 #product beta-galactoside-binding lectin #status !8experimental #label MAT\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental SUMMARY #length 135 #molecular-weight 15063 #checksum 8342 SEQUENCE /// ENTRY LNCH16 #type complete TITLE 16K galactose-binding lectin - chicken ALTERNATE_NAMES 16K lectin ORGANISM #formal_name Gallus gallus #common_name chicken DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 13-Sep-1996 ACCESSIONS A36496 REFERENCE A36496 !$#authors Sakakura, Y.; Hirabayashi, J.; Oda, Y.; Ohyama, Y.; Kasai, !1K. !$#journal J. Biol. Chem. (1990) 265:21573-21579 !$#title Structure of chicken 16-kDa beta-galactoside-binding lectin. !1Complete amino acid sequence, cloning of cDNA, and !1production of recombinant lectin. !$#cross-references MUID:91072353; PMID:2254315 !$#accession A36496 !'##molecule_type mRNA !'##residues 1-134 ##label SAK !'##cross-references GB:J05687 CLASSIFICATION #superfamily beta-galactoside-binding lectin KEYWORDS lectin SUMMARY #length 134 #molecular-weight 14934 #checksum 4441 SEQUENCE /// ENTRY LNRZ #type complete TITLE lectin precursor - rice CONTAINS lectin 10K chain; lectin 8K chain ORGANISM #formal_name Oryza sativa #common_name rice DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jul-1999 ACCESSIONS JQ1102 REFERENCE JQ1102 !$#authors Wilkins, T.A.; Raikhel, N.V. !$#journal Plant Cell (1989) 1:541-549 !$#title Expression of rice lectin is governed by two temporally and !1spatially regulated mRNAs in developing embryos. !$#cross-references MUID:92404719; PMID:2535550 !$#accession JQ1102 !'##molecule_type mRNA !'##residues 1-227 ##label WIL !'##cross-references GB:M24504; NID:g530789; PIDN:AAA20873.1; !1PID:g530790 !'##experimental_source embryo, cv. Lemont !'##note part of this sequence, including the amino and carboxyl ends of !1both the 10K and 8K peptides, was confirmed by protein !1sequencing CLASSIFICATION #superfamily wheat agglutinin; hevein chitin-binding domain !1homology KEYWORDS duplication; glycoprotein; lectin; pyroglutamic acid FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-227 #product lectin proprotein #status experimental !8#label LEP\ !$29-201 #product lectin #status experimental #label LEC\ !$29-122 #product lectin 10K chain #status experimental #label !810K\ !$29-71 #domain hevein chitin-binding domain homology #label !8HCB1\ !$72-114 #domain hevein chitin-binding domain homology #label !8HCB2\ !$115-157 #domain hevein chitin-binding domain homology #label !8HCB3\ !$123-201 #product lectin 8K chain #status experimental #label !88KD\ !$158-200 #domain hevein chitin-binding domain homology #label !8HCB4\ !$202-227 #domain carboxyl-terminal propeptide #status !8predicted #label CAR\ !$29 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status predicted\ !$31-46,40-52,45-59, !$63-68,74-89,83-95, !$88-102,106-111, !$117-132,126-138, !$131-145,149-154, !$160-175,169-181, !$174-188,192-197 #disulfide_bonds #status predicted\ !$211 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 227 #molecular-weight 22795 #checksum 6530 SEQUENCE /// ENTRY AEWT2 #type complete TITLE agglutinin isolectin 2 precursor - wheat ALTERNATE_NAMES agglutinin isolectin D ORGANISM #formal_name Triticum aestivum #common_name common wheat DATE 03-Aug-1984 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS S09624; S10044; A03369 REFERENCE S09623 !$#authors Smith, J.J.; Raikhel, N.V. !$#journal Plant Mol. Biol. (1989) 13:601-603 !$#title Nucleotide sequences of cDNA clones encoding wheat germ !1agglutinin isolectins A and D. !$#cross-references MUID:91370843; PMID:2491677 !$#accession S09624 !'##molecule_type mRNA !'##residues 1-213 ##label SMI !'##cross-references EMBL:M25537; NID:g170669; PIDN:AAA34258.1; !1PID:g170670 REFERENCE S07289 !$#authors Wright, C.S.; Raikhel, N. !$#journal J. Mol. Evol. (1989) 28:327-336 !$#title Sequence variability in three wheat germ agglutinin !1isolectins: products of multiple genes in polyploid wheat. !$#cross-references MUID:89279931; PMID:2499688 !$#accession S10044 !'##molecule_type protein !'##residues 28-63,'D',65-198 ##label WR2 REFERENCE A90485 !$#authors Wright, C.S.; Gavilanes, F.; Peterson, D.L. !$#journal Biochemistry (1984) 23:280-287 !$#title Primary structure of wheat germ agglutinin isolectin 2. !1Peptide order deduced from X-ray structure. !$#cross-references MUID:84128547; PMID:6546522 !$#accession A03369 !'##molecule_type protein !'##residues 28-63,'D',65-67,'S',69-135,'S',137-160,'G',162-176,'G', !1178-198 ##label WRI !'##note this sequence has been revised in reference S07289 COMMENT The three isolectins associate randomly into dimers in vivo. COMMENT Wheat isolectins bind specifically to N-acetylglucosamine !1and N-acetylneuraminic acid. CLASSIFICATION #superfamily wheat agglutinin; hevein chitin-binding domain !1homology KEYWORDS dimer; duplication; glycoprotein; lectin; pyroglutamic acid FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-213 #product agglutinin isolectin 2 proprotein #status !8experimental #label PRO\ !$28-198 #product agglutinin isolectin 2 #status experimental !8#label MAT\ !$28-70 #domain hevein chitin-binding domain homology #label !8HCB1\ !$71-113 #domain hevein chitin-binding domain homology #label !8HCB2\ !$114-156 #domain hevein chitin-binding domain homology #label !8HCB3\ !$157-199 #domain hevein chitin-binding domain homology #label !8HCB4\ !$199-213 #domain carboxyl-terminal propeptide #status !8experimental #label CPRO\ !$28 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$30-45,39-51,44-58, !$62-67,73-88,82-94, !$87-101,105-110, !$116-131,125-137, !$130-144,148-153, !$159-174,168-180, !$173-187,191-196 #disulfide_bonds #status experimental\ !$207 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 213 #molecular-weight 21356 #checksum 3216 SEQUENCE /// ENTRY HVHV #type complete TITLE hevein precursor - Para rubber tree ORGANISM #formal_name Hevea brasiliensis #common_name Para rubber tree DATE 24-Apr-1984 #sequence_revision 23-Mar-1995 #text_change 16-Jul-1999 ACCESSIONS A38288; A94426; A94583; A03370 REFERENCE A38288 !$#authors Broekaert, W.; Lee, H.; Kush, A.; Chua, N.H.; Raikhel, N. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:7633-7637 !$#title Wound-induced accumulation of mRNA containing a hevein !1sequence in laticifers of rubber tree (Hevea brasiliensis). !$#cross-references MUID:91017559; PMID:2217194 !$#accession A38288 !'##molecule_type mRNA !'##residues 1-204 ##label BRO !'##cross-references GB:M36986; NID:g168208; PIDN:AAA33357.1; !1PID:g168209 REFERENCE A94426 !$#authors Walujono, K.; Scholma, R.A.; Beintema, J.J.; Mariono, A.; !1Hahn, A.M. !$#book Proceedings of the International Rubber Conference, vol.2, !1pp.518-531, Rubber Research Institute of Malaysia, Kuala !1Lumpur, 1975 !$#title Amino acid sequence of hevein. !$#accession A94426 !'##molecule_type protein !'##residues 18-50,'HD',53-60 ##label WAL REFERENCE A94583 !$#authors Beintema, J.J. !$#submission submitted to the Atlas, June 1977 !$#accession A94583 !'##molecule_type protein !'##residues 51-52 ##label BEI REFERENCE A46380 !$#authors Andersen, N.H.; Cao, B.; Rodriguez-Romero, A.; Arreguin, B. !$#journal Biochemistry (1993) 32:1407-1422 !$#title Hevein: NMR assignment and assessment of solution-state !1folding for the agglutinin-toxin motif. !$#cross-references MUID:93160177; PMID:8431421 !$#contents annotation; conformation and disulfide bond assignments of !1hevein by (1)H-NMR COMMENT Hevein binds chitin and inhibits growth of some !1chitin-binding fungi. It may protect wound sites from fungal !1attack. CLASSIFICATION #superfamily hevein precursor; barwin homology; hevein !1chitin-binding domain homology KEYWORDS antifungal; lectin FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-61 #domain hevein chitin-binding domain homology #label !8HCB\ !$18-60 #product hevein #status experimental #label MAT\ !$68-189 #domain barwin homology #label BAR\ !$20-35,29-41,34-48, !$54-58 #disulfide_bonds #status experimental\ !$96-128,117-151, !$131-187 #disulfide_bonds #status predicted SUMMARY #length 204 #molecular-weight 21859 #checksum 4463 SEQUENCE /// ENTRY S18598 #type complete TITLE pathogenesis-related protein 4 - common tobacco ORGANISM #formal_name Nicotiana tabacum #common_name common tobacco DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S18598 REFERENCE S18598 !$#authors Friedrich, L.; Moyer, M.; Ward, E.; Ryals, J. !$#journal Mol. Gen. Genet. (1991) 230:113-119 !$#title Pathogenesis-related protein 4 is structurally homologous to !1the carboxy-terminal domains of hevein, Win-1 and Win-2. !$#cross-references MUID:92079884; PMID:1745223 !$#accession S18598 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-147 ##label FRI !'##cross-references GB:X60281; NID:g19963; PIDN:CAA42820.1; PID:g19964 CLASSIFICATION #superfamily pathogenesis-related protein 4A; barwin !1homology FEATURE !$26-147 #domain barwin homology #label BAR SUMMARY #length 147 #molecular-weight 16221 #checksum 7383 SEQUENCE /// ENTRY S18838 #type complete TITLE a-agglutinin precursor - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein G3646; protein YGL032c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jun-2000 ACCESSIONS S18838; S18839; S52575; S64034 REFERENCE S18838 !$#authors Cappellaro, C.; Hauser, K.; Mrsa, V.; Watzele, M.; Watzele, !1G.; Gruber, C.; Tanner, W. !$#journal EMBO J. (1991) 10:4081-4088 !$#title Saccharomyces cerevisiae a- and alpha-agglutinin: !1characterization of their molecular interaction. !$#cross-references MUID:92097526; PMID:1756718 !$#accession S18838 !'##molecule_type mRNA; DNA !'##residues 1-87 ##label CAP1 !'##cross-references EMBL:X62877; NID:g3350; PIDN:CAA44670.1; PID:g3351 !$#accession S18839 !'##molecule_type protein !'##residues 19-21,'ES',24,'S',26-29,'X',31,'D',33-38,'X', !140-41;51-60;'X',62-67,'Y',69-74,'X',76-83,'GT',86 ##label !1CAP2 REFERENCE S52575 !$#authors Cappellaro, C.; Baldermann, C.; Rachel, R.; Tanner, W. !$#journal EMBO J. (1994) 13:4737-4744 !$#title Mating type-specific cell-cell recognition of Saccharomyces !1cerevisiae: cell wall attachment and active sites of a- and !1alpha-agglutinin. !$#cross-references MUID:95045364; PMID:7957044 !$#accession S52575 !'##molecule_type protein !'##residues 19-87 ##label CAP REFERENCE S64003 !$#authors Hebling, U.; Hofmann, B.; Delius, H. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64034 !'##molecule_type DNA !'##residues 1-87 ##label HEB !'##cross-references EMBL:Z72554; NID:g1322507; PIDN:CAA96733.1; !1PID:g1322508; GSPDB:GN00007; MIPS:YGL032c !'##experimental_source strain S288C GENETICS !$#gene SGD:AGA2; MIPS:YGL032c !'##cross-references SGD:S0003000; MIPS:YGL032c !$#map_position 7L FUNCTION !$#description involved in agglutination of a and alpha cells !$#note a-agglutinin forms a 1:1 complex with alpha-agglutinin CLASSIFICATION #superfamily a-agglutinin KEYWORDS disulfide bond; glycoprotein FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-87 #product a-agglutinin #status experimental #label !8MAT\ !$22,23,32,75 #binding_site carbohydrate (Thr) (covalent) #status !8predicted\ !$30,39 #binding_site carbohydrate (Ser) (covalent) #status !8predicted\ !$63 #binding_site carbohydrate (Thr) (covalent) #status !8experimental\ !$66 #binding_site carbohydrate (Ser) (covalent) #status !8experimental SUMMARY #length 87 #molecular-weight 9464 #checksum 4185 SEQUENCE /// ENTRY ARRA5 #type complete TITLE allergen Ra5 - common ragweed ORGANISM #formal_name Ambrosia artemisiifolia var. elatior #common_name common ragweed DATE 08-Oct-1981 #sequence_revision 08-Oct-1981 #text_change 16-Jul-1999 ACCESSIONS A03371 REFERENCE A03371 !$#authors Mole, L.E.; Goodfriend, L.; Lapkoff, C.B.; Kehoe, J.M.; !1Capra, J.D. !$#journal Biochemistry (1975) 14:1216-1220 !$#title The amino acid sequence of ragweed pollen allergen Ra5. !$#cross-references MUID:75127948; PMID:1122277 !$#accession A03371 !'##molecule_type protein !'##residues 1-45 ##label MOL !'##note 2-Val and 2-Leu were found in a ratio of 2:1 CLASSIFICATION #superfamily allergen Ra5; hevein chitin-binding domain !1homology KEYWORDS pollen FEATURE !$2-45 #domain hevein chitin-binding domain homology #label !8HCB\ !$4-39,11-26,18-32, !$19-43 #disulfide_bonds #status predicted SUMMARY #length 45 #molecular-weight 4979 #checksum 8778 SEQUENCE /// ENTRY ARRA5G #type complete TITLE allergen Ra5G precursor - giant ragweed ALTERNATE_NAMES allergen Amb t V ORGANISM #formal_name Ambrosia trifida #common_name giant ragweed DATE 31-Dec-1988 #sequence_revision 31-May-1996 #text_change 16-Jul-1999 ACCESSIONS JQ1001; A23859; S21509 REFERENCE JQ1001 !$#authors Ghosh, B.; Perry, M.P.; Marsh, D.G. !$#journal Gene (1991) 101:231-238 !$#title Cloning the cDNA encoding the AmbtV allergen from giant !1ragweed (Ambrosia trifida) pollen. !$#cross-references MUID:91276276; PMID:1711499 !$#accession JQ1001 !'##status preliminary !'##molecule_type mRNA !'##residues 1-73 ##label GHO !'##cross-references GB:M38782; NID:g1184266; PIDN:AAB02877.1; !1PID:g1184267; EMBL:X56279; NID:g17679; PID:g17680 REFERENCE A23859 !$#authors Goodfriend, L.; Choudhury, A.M.; Klapper, D.G.; Coulter, !1K.M.; Dorval, G.; del Carpio, J.; Osterland, C.K. !$#journal Mol. Immunol. (1985) 22:899-906 !$#title Ra5G, a homologue of Ra5 in giant ragweed pollen: isolation, !1HLA-DR-associated activity and amino acid sequence. !$#cross-references MUID:86014019; PMID:3862954 !$#accession A23859 !'##molecule_type protein !'##residues 34-73 ##label GOO REFERENCE A44521 !$#authors Metzler, W.J.; Valentine, K.; Roebber, M.; Friedrichs, M.S.; !1Marsh, D.G.; Mueller, L. !$#journal Biochemistry (1992) 31:5117-5127 !$#title Determination of the three-dimensional solution structure of !1ragweed allergen Amb t V by nuclear magnetic resonance !1spectroscopy. !$#cross-references MUID:92297618; PMID:1606135 !$#contents annotation CLASSIFICATION #superfamily allergen Ra5; hevein chitin-binding domain !1homology KEYWORDS pollen FEATURE !$34-73 #product allergen Ra5G #status experimental #label !8MAT\ !$36-73 #domain hevein chitin-binding domain homology #label !8HCB\ !$38-68,44-59,51-61, !$52-72 #disulfide_bonds #status experimental SUMMARY #length 73 #molecular-weight 8058 #checksum 4140 SEQUENCE /// ENTRY JT0756 #type complete TITLE group-V allergen isoform, Lol p VB precursor (clone 19R) - perennial ryegrass ALTERNATE_NAMES 34K allergen ORGANISM #formal_name Lolium perenne #common_name perennial ryegrass DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JT0756; S38289 REFERENCE JT0756 !$#authors Ong, E.K.; Griffith, I.J.; Knox, R.B.; Singh, M.B. !$#journal Gene (1993) 134:235-240 !$#title Cloning of a cDNA encoding a group-V (group-IX) allergen !1isoform from rye-grass pollen that demonstrates specific !1antigenic immunoreactivity. !$#cross-references MUID:94085783; PMID:8262382 !$#accession JT0756 !'##molecule_type mRNA !'##residues 1-339 ##label ONG !'##cross-references GB:L13083; NID:g455287; PIDN:AAA33405.1; !1PID:g455288 REFERENCE S38288 !$#authors Petersen, A.; Schramm, G.; Becker, W.M.; Schlaak, M. !$#journal Biol. Chem. Hoppe-Seyler (1993) 374:855-861 !$#title Comparison of four grass pollen species concerning their !1allergens of grass group V by 2D immunoblotting and !1microsequencing. !$#cross-references MUID:94092339; PMID:7505588 !$#accession S38289 !'##molecule_type protein !'##residues 26-44 ##label PET CLASSIFICATION #superfamily grass pollen allergen IX KEYWORDS pollen FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-339 #product group-V allergen isoform, Lol p VB #status !8experimental #label MAT SUMMARY #length 339 #molecular-weight 33750 #checksum 5903 SEQUENCE /// ENTRY RLQHG2 #type complete TITLE rRNA N-glycosidase (EC 3.2.2.22) Sap2 precursor - common soapwort ALTERNATE_NAMES ribosome-inactivating protein; saporin 2; saporin S5 ORGANISM #formal_name Saponaria officinalis #common_name common soapwort DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS S17933; S28540; S38526; S15459 REFERENCE S17932 !$#authors Fordham-Skelton, A.P.; Taylor, P.N.; Hartley, M.R.; Croy, !1R.R.D. !$#journal Mol. Gen. Genet. (1991) 229:460-466 !$#title Characterisation of saporin genes: in vitro expression and !1ribosome inactivation. !$#cross-references MUID:92049247; PMID:1719367 !$#accession S17933 !'##molecule_type DNA !'##residues 1-292 ##label FOR !'##cross-references EMBL:X59255; GB:S63902; NID:g2094853; !1PIDN:CAA41948.1; PID:g21321 REFERENCE S28539 !$#authors Soria, M.R. !$#submission submitted to the EMBL Data Library, October 1992 !$#accession S28540 !'##molecule_type DNA !'##residues 25-283 ##label SOR !'##cross-references EMBL:X69132; NID:g21330; PIDN:CAA48886.1; !1PID:g938284 REFERENCE S38521 !$#authors Ferreras, J.M.; Barbieri, L.; Girbes, T.; Battelli, M.G.; !1Rojo, M.A.; Arias, F.J.; Rocher, M.A.; Soriano, F.; Mendez, !1E.; Stirpe, F. !$#journal Biochim. Biophys. Acta (1993) 1216:31-42 !$#title Distribution and properties of major ribosome-inactivating !1proteins (28 S rRNA N-glycosidases) of the plant Saponaria !1officinalis L. (Caryophyllaceae). !$#cross-references MUID:94032486; PMID:8218413 !$#accession S38526 !'##molecule_type protein !'##residues 25-54 ##label FER GENETICS !$#gene SAP2 CLASSIFICATION #superfamily rRNA N-glycosidase; rRNA N-glycosidase homology KEYWORDS glycosidase; hydrolase; monomer; toxin FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-292 #product rRNA N-glycosidase Sap2 #status predicted !8#label MAT\ !$30-273 #domain rRNA N-glycosidase homology #label RNG SUMMARY #length 292 #molecular-weight 32810 #checksum 6849 SEQUENCE /// ENTRY RLPUGG #type complete TITLE rRNA N-glycosidase (EC 3.2.2.22) alpha-momorcharin precursor [validated] - balsam pear ALTERNATE_NAMES agglutinin; momordin-A; ribosome-inactivating protein momorcharin alpha ORGANISM #formal_name Momordica charantia #common_name balsam pear, bitter gourd DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 15-Sep-2000 ACCESSIONS S14273; A61318; S16490; JN0628; S01670 REFERENCE S14273 !$#authors Ho, W.K.K.; Liu, S.C.; Shaw, P.C.; Yeung, H.W.; Ng, T.B.; !1Chan, W.Y. !$#journal Biochim. Biophys. Acta (1991) 1088:311-314 !$#title Cloning of the cDNA of alpha-momorcharin: a ribosome !1inactivating protein. !$#cross-references MUID:91159486; PMID:2001404 !$#accession S14273 !'##molecule_type mRNA !'##residues 1-286 ##label HOW !'##cross-references EMBL:X57682; NID:g19527; PIDN:CAA40869.1; !1PID:g19528 REFERENCE A61318 !$#authors Li, S.S.L. !$#journal Experientia (1980) 36:524-527 !$#title Purification and partial characterization of two lectins !1from Momordica charantia. !$#cross-references MUID:80201763; PMID:7379938 !$#accession A61318 !'##molecule_type protein !'##residues 24-50 ##label LIA !'##note as a lectin shows agglutinating activity for type-O red blood !1cells REFERENCE S16331 !$#authors Montecucchi, P.C.; Lazzarini, A.M.; Barbieri, L.; Stirpe, !1F.; Soria, M.; Lappi, D. !$#journal Int. J. Pept. Protein Res. (1989) 33:263-267 !$#title N-terminal sequence of some ribosome-inactivating proteins. !$#cross-references MUID:89326691; PMID:2753596 !$#accession S16490 !'##molecule_type protein !'##residues 24-68,'X',70 ##label MON REFERENCE JN0628 !$#authors Minami, Y.; Funatsu, G. !$#journal Biosci. Biotechnol. Biochem. (1993) 57:1141-1144 !$#title The complete amino acid sequence of momordin-a, a !1ribosome-inactivating protein from the seeds of bitter gourd !1(Momordica charantia). !$#cross-references MUID:93372485; PMID:7763984 !$#accession JN0628 !'##molecule_type protein !'##residues 24-107,'Q',109-123,125-147,'L',149-154,'I',156-205,'I', !1207-208,'L',210-214,'L',215-273 ##label MIN !'##experimental_source seed REFERENCE A52272 !$#authors Ren, J.; Wang, Y.; Dong, Y.; Stuart, D.I. !$#submission submitted to the Brookhaven Protein Data Bank, January 1994 !$#cross-references PDB:1AHC !$#contents annotation; X-ray crystallography, 2.0 angstroms, residues !124-269 REFERENCE A52385 !$#authors Husain, J.; Tickle, I.J.; Wood, S.P. !$#submission submitted to the Brookhaven Protein Data Bank, March 1994 !$#cross-references PDB:1MOM !$#contents annotation; X-ray crystallography, 2.16 angstroms, residues !124-86,'L',88-269 REFERENCE A67089 !$#authors Huang, Q.; Liu, S.; Tang, Y.; Jin, S.; Wang, Y. !$#submission submitted to the Brookhaven Protein Data Bank, July 1994 !$#cross-references PDB:1MRH !$#contents annotation; X-ray crystallography, 2.0 angstroms, residues !124-77,'R',79-132,'D',134-269 FUNCTION !$#description hydrolyzes the N-glycosidic bond of a specific adenosine in !128S rRNA thereby inactivating the ribosome CLASSIFICATION #superfamily rRNA N-glycosidase; rRNA N-glycosidase homology KEYWORDS glycoprotein; glycosidase; hydrolase; lectin; seed; toxin FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-23 #domain amino-terminal propeptide #status predicted !8#label PRO\ !$24-269 #product rRNA N-glycosidase alpha-momorcharin #status !8experimental #label MAT\ !$27-266 #domain rRNA N-glycosidase homology #label RNG\ !$270-286 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$93,183,186 #active_site Tyr, Glu, Arg #status predicted\ !$250 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 286 #molecular-weight 31532 #checksum 1384 SEQUENCE /// ENTRY RLTZT #type complete TITLE rRNA N-glycosidase (EC 3.2.2.22) alpha-trichosanthin precursor [validated] - Mongolian snake-gourd ALTERNATE_NAMES alpha-TCS; type I ribosome-inactivating protein ORGANISM #formal_name Trichosanthes kirilowii #common_name Mongolian snake-gourd DATE 30-Sep-1988 #sequence_revision 26-Jan-1996 #text_change 23-Mar-2001 ACCESSIONS JT0566; A36274; JC1093; A36273; JT0003 REFERENCE JT0566 !$#authors Shaw, P.C.; Yung, M.H.; Zhu, R.H.; Ho, W.K.K.; Ng, T.B.; !1Yeung, H.W. !$#journal Gene (1991) 97:267-272 !$#title Cloning of trichosanthin cDNA and its expression in !1Escherichia coli. !$#cross-references MUID:91153657; PMID:1999291 !$#accession JT0566 !'##molecule_type mRNA !'##residues 1-289 ##label SHA !'##cross-references GB:M34858; NID:g170536; PIDN:AAA34207.1; !1PID:g170537 !'##experimental_source tuber REFERENCE A36274 !$#authors Chow, T.P.; Feldman, R.A.; Lovett, M.; Piatak, M. !$#journal J. Biol. Chem. (1990) 265:8670-8674 !$#title Isolation and DNA sequence of a gene encoding !1alpha-trichosanthin, a type I ribosome-inactivating protein. !$#cross-references MUID:90256790; PMID:2341400 !$#accession A36274 !'##molecule_type DNA !'##residues 1-233,'T',235-246,'M',248-289 ##label CHO !'##cross-references GB:J05434; NID:g170534; PIDN:AAA34206.1; !1PID:g170535 REFERENCE JC1093 !$#authors Zheng, H.G.; Wang, B.; Shao, P.Z.; Yang, X.R. !$#journal Acta Genet. Sin. (1994) 21:42-51 !$#title Cloning and DNA sequencing of the gene encoding !1Trichosanthin. !$#cross-references MUID:94271613; PMID:8003348 !$#accession JC1093 !'##molecule_type DNA !'##residues 1-72,'V',74-90,'S',92-233,'T',235-267,'D',269-289 ##label !1ZHE !'##cross-references GB:S70176; NID:g547148; PIDN:AAB31048.1; !1PID:g547149 REFERENCE A36273 !$#authors Collins, E.J.; Robertus, J.D.; LoPresti, M.; Stone, K.L.; !1Williams, K.R.; Wu, P.; Hwang, K.; Piatak, M. !$#journal J. Biol. Chem. (1990) 265:8665-8669 !$#title Primary amino acid sequence of alpha-trichosanthin and !1molecular models for abrin A-chain and alpha-trichosanthin. !$#cross-references MUID:90256789; PMID:2341399 !$#accession A36273 !'##molecule_type protein !'##residues 24-270 ##label COL REFERENCE JT0003 !$#authors Wang, Y.; Qian, R.Q.; Gu, Z.W.; Jin, S.W.; Zhang, L.Q.; Xia, !1Z.X.; Tian, G.Y.; Ni, C.Z. !$#journal Pure Appl. Chem. (1986) 58:789-798 !$#title Scientific evaluation of Tian Hua Fen (THF): history, !1chemistry and application. !$#accession JT0003 !'##molecule_type protein !'##residues 24-56,'L',58-59,'I',61-71,'I',73-81,85-86,'L',88-92, !1'DAGLPRNAVL',93-142,'GL',145-195,'S',197-214,'L',215,'L', !1217-230,'T',232-245,267-270 ##label WAN !'##experimental_source tuber REFERENCE A67091 !$#authors Huang, Q.; Liu, S.; Tang, Y.; Jin, S.; Wang, Y. !$#submission submitted to the Brookhaven Protein Data Bank, July 1994 !$#cross-references PDB:1MRJ !$#contents annotation; X-ray crystallography, 1.6 angstroms, with !1adenine, residues 24-270 REFERENCE A67092 !$#authors Huang, Q.; Liu, S.; Tang, Y.; Jin, S.; Wang, Y. !$#submission submitted to the Brookhaven Protein Data Bank, July 1994 !$#cross-references PDB:1MRK !$#contents annotation; X-ray crystallography, 1.6 angstroms, with !1formycin, residues 24-270 REFERENCE A66711 !$#authors Xiong, J.P.; Xia, Z.X.; Wang, Y. !$#submission submitted to the Brookhaven Protein Data Bank, December 1994 !$#cross-references PDB:1TCS !$#contents annotation; X-ray crystallography, 1.7 angstroms, with !1NADPH, residues 24-270 REFERENCE A58622 !$#authors Xiong, J.P.; Xia, Z.X.; Wang, Y. !$#journal Nat. Struct. Biol. (1994) 1:695-700 !$#title Crystal structure of trichosanthin-NADPH complex at 1.7 !1Angstroms resolution reveals active-site architecture. !$#cross-references MUID:95360714; PMID:7634073 !$#contents annotation; X-ray crystallography, 1.7 angstroms COMMENT Alpha-trichosanthin has been used to induce abortions. GENETICS !$#gene tcs FUNCTION !$#description hydrolyzes the N-glycosidic bond of a specific adenosine in !128S rRNA thereby inactivating the ribosome CLASSIFICATION #superfamily rRNA N-glycosidase; rRNA N-glycosidase homology KEYWORDS abortifacient; glycosidase; hydrolase; root; toxin FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-270 #product trichosanthin alpha #status experimental !8#label MAT\ !$27-266 #domain rRNA N-glycosidase homology #label RNG\ !$271-289 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$93,183,186 #active_site Tyr, Glu, Arg #status predicted SUMMARY #length 289 #molecular-weight 31676 #checksum 1678 SEQUENCE /// ENTRY RLBH #type complete TITLE rRNA N-glycosidase (EC 3.2.2.22) 2 - barley ALTERNATE_NAMES 30K ribosome-inactivating protein 2; protein synthesis inhibitor II ORGANISM #formal_name Hordeum vulgare #common_name barley DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 16-Jul-1999 ACCESSIONS A03373; C38664 REFERENCE A90767 !$#authors Asano, K.; Svensson, B.; Svendsen, I.; Poulsen, F.M.; !1Roepstorff, P. !$#journal Carlsberg Res. Commun. (1986) 51:129-141 !$#title The complete primary structure of protein synthesis !1inhibitor II from barley seeds. !$#accession A03373 !'##molecule_type protein !'##residues 1-280 ##label ASA REFERENCE A90665 !$#authors Roberts, W.K.; Selitrennikoff, C.P. !$#journal Biochim. Biophys. Acta (1986) 880:161-170 !$#title Isolation and partial characterization of two antifungal !1proteins from barley. !$#cross-references MUID:86104412; PMID:3942788 !$#contents annotation; antifungal activity REFERENCE A38664 !$#authors Leah, R.; Tommerup, H.; Svendsen, I.; Mundy, J. !$#journal J. Biol. Chem. (1991) 266:1564-1573 !$#title Biochemical and molecular characterization of three barley !1seed proteins with antifungal properties. !$#cross-references MUID:91107649; PMID:1899089 !$#accession C38664 !'##molecule_type mRNA !'##residues 164-280 ##label LEA !'##cross-references GB:M62906; GB:M36991; NID:g167033; PIDN:AAA32951.1; !1PID:g167034 COMMENT Catalytic amounts of this protein, which is homologous to !1the A chain of ricin D, inhibit the elongation phase of !1protein synthesis. It inactivates fungal ribosomes even more !1effectively than mammalian ribosomes and is thought to !1function as a constitutive antifungal agent in plants. CLASSIFICATION #superfamily rRNA N-glycosidase; rRNA N-glycosidase homology KEYWORDS acetylated amino end; antifungal; glycosidase; hydrolase FEATURE !$16-259 #domain rRNA N-glycosidase homology #label RNG\ !$1 #modified_site acetylated amino end (Ala) #status !8experimental SUMMARY #length 280 #molecular-weight 29863 #checksum 6523 SEQUENCE /// ENTRY RLZMRI #type complete TITLE rRNA N-glycosidase (EC 3.2.2.22) precursor - maize ALTERNATE_NAMES ribosome-inactivating protein precursor ORGANISM #formal_name Zea mays #common_name maize DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS A41590; B41590 REFERENCE A41590 !$#authors Walsh, T.A.; Morgan, A.E.; Hey, T.D. !$#journal J. Biol. Chem. (1991) 266:23422-23427 !$#title Characterization and molecular cloning of a proenzyme form !1of a ribosome-inactivating protein from maize. Novel !1mechanism of proenzyme activation by proteolytic removal of !1a 2.8-kilodalton internal peptide segment. !$#cross-references MUID:92078221; PMID:1744135 !$#accession A41590 !'##molecule_type mRNA !'##residues 1-301 ##label WAL !'##cross-references GB:M77122; NID:g168609; PIDN:AAA33508.1; !1PID:g168610 !$#accession B41590 !'##molecule_type protein !'##residues 14-49;155-161;187-215 ##label WA2 !'##note the first four residues of the alpha chain were detected in !1only 10% of the sequenced material COMMENT The position of the alanine residue identified as the !1carboxyl end of the processed beta chain was not determined !1but is estimated here from the reported molecular weight of !18.5 (+/- 1.5) kilodaltons. COMMENT This enzyme inhibits protein synthesis by cleaving the !1N-glycosyl bond of a specific adenine residue in the !1ribosomal 28 S RNA of eukaryotic ribosomes. COMMENT This enzyme differs from the ricin A chain and most other !1type 1 ribosome-inactivating proteins in that the protein is !1stored as a zymogen, its active form is created by !1processing into two chains, and it is not associated with a !1lectin-like moeity. CLASSIFICATION #superfamily rRNA N-glycosidase; rRNA N-glycosidase homology KEYWORDS glycosidase; hydrolase; zymogen FEATURE !$2-13 #domain propeptide #status predicted #label PRO\ !$14-161 #product rRNA N-glycosidase #status predicted #label !8MAT\ !$14-161 #domain rRNA N-glycosidase alpha chain #status !8predicted #label ACH\ !$26-283 #domain rRNA N-glycosidase homology #label RNG\ !$162-186 #domain activation peptide #status experimental !8#label ACT\ !$187-273 #domain rRNA N-glycosidase beta chain #status !8predicted #label BCH SUMMARY #length 301 #molecular-weight 33330 #checksum 7133 SEQUENCE /// ENTRY RLCSD #type complete TITLE ricin D precursor - castor bean CONTAINS rRNA N-glycosidase (EC 3.2.2.22) ORGANISM #formal_name Ricinus communis #common_name castor bean DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS A24041; S20513; A24614; A03372; A24010; A03374; S10903 REFERENCE A24041 !$#authors Halling, K.C.; Halling, A.C.; Murray, E.E.; Ladin, B.F.; !1Houston, L.L.; Weaver, R.F. !$#journal Nucleic Acids Res. (1985) 13:8019-8033 !$#title Genomic cloning and characterization of a ricin gene from !1Ricinus communis. !$#cross-references MUID:86067214; PMID:2999712 !$#accession A24041 !'##molecule_type DNA !'##residues 1-576 ##label HAL !'##cross-references GB:X03179; NID:g21082; PIDN:CAA26939.1; PID:g21083 REFERENCE S20513 !$#authors Tregear, J.W.; Roberts, L.M. !$#journal Plant Mol. Biol. (1992) 18:515-525 !$#title The lectin gene family of Ricinus communis: cloning of a !1functional ricin gene and three lectin pseudogenes. !$#cross-references MUID:92163016; PMID:1371405 !$#accession S20513 !'##molecule_type DNA !'##residues 1-576 ##label TRE !'##cross-references EMBL:X52908; NID:g21084; PIDN:CAA37095.1; !1PID:g21085 REFERENCE A24614 !$#authors Lamb, F.I.; Roberts, L.M.; Lord, J.M. !$#journal Eur. J. Biochem. (1985) 148:265-270 !$#title Nucleotide sequence of cloned cDNA coding for preproricin. !$#cross-references MUID:85179479; PMID:3838723 !$#accession A24614 !'##molecule_type mRNA !'##residues 12-75,'D',77-550,'R',552-576 ##label LAM !'##cross-references GB:X02388; NID:g21077; PIDN:CAA26230.1; PID:g21078 REFERENCE A03372 !$#authors Yoshitake, S.; Funatsu, G.; Funatsu, M. !$#journal Agric. Biol. Chem. (1978) 42:1267-1274 !$#title Isolation and sequences of peptic peptides, and the complete !1sequence of Ile chain of ricin-D. !$#accession A03372 !'##molecule_type protein !'##residues 36-97,'Q',99-109,'S',111-269,'D',272-283,'L',285-288, !1290-302 ##label YOS !'##note this paper cites the others in the series providing !1experimental details for the determination of the complete !1sequence REFERENCE A24010 !$#authors Araki, T.; Funatsu, G. !$#journal FEBS Lett. (1985) 191:121-124 !$#title Revised amino acid sequence of the B-chain of ricin D due to !1loss of tryptophan in the cyanogen bromide cleavage. !$#accession A24010 !'##molecule_type protein !'##residues 315-383,'PS',386-576 ##label ARA REFERENCE A03374 !$#authors Funatsu, G.; Kimura, M.; Funatsu, M. !$#journal Agric. Biol. Chem. (1979) 43:2221-2224 !$#title Primary structure of Ala chain of ricin D. !$#accession A03374 !'##molecule_type protein !'##residues 315-335,'N',337-342,'NH',345-362,364-383,'PS',386-399,'T', !1401,'D',403,'E',406-407,'N',409-444,'P',446,'F',448-453,'W', !1455-473,'V',475-477,'SC',480-491,'S',493,'N',495,'N', !1497-499,'R',501-527,'E',529-564,'W',566,'H',567-570,'LI', !1573-574,'F' ##label FUN !'##note this paper, one of a series, summarizes the experimental !1details for the determination of the complete sequence REFERENCE A48237 !$#authors Ready, M.P.; Kim, Y.; Robertus, J.D. !$#journal Proteins (1991) 10:270-278 !$#title Site-directed mutagenesis of ricin A-chain and implications !1for the mechanism of action. !$#cross-references MUID:91352006; PMID:1881883 !$#contents annotation; active site REFERENCE A48238 !$#authors Rutenber, E.; Robertus, J.D. !$#journal Proteins (1991) 10:260-269 !$#title Structure of ricin B-chain at 2.5 angstrom resolution. !$#cross-references MUID:91352005; PMID:1881882 !$#contents annotation; X-ray crystallography, 2.5 angstroms REFERENCE A48239 !$#authors Katzin, B.J.; Collins, E.J.; Robertus, J.D. !$#journal Proteins (1991) 10:251-259 !$#title Structure of ricin A-chain at 2.5 angstroms. !$#cross-references MUID:91352004; PMID:1881881 !$#contents annotation; X-ray crystallography, 2.5 angstroms COMMENT The functional molecule is a disulfide-linked dimer of A and !1B chains, which are derived from the same precursor !1molecule. COMMENT The A chain inhibits protein synthesis; it inactivates the !160S ribosomal subunit by cleaving at a specific site in 28S !1rRNA. The B chain binds to cell receptors and facilitates !1the entry into the cell of the A chain; B chains are also !1responsible for cell agglutination (lectin activity). COMMENT This protein is cytotoxic and very poisonous to animals. CLASSIFICATION #superfamily ricin; rRNA N-glycosidase homology KEYWORDS duplication; glycoprotein; glycosidase; hydrolase; lectin; !1RNA binding; seed; tandem repeat; toxin FEATURE !$1-35 #domain signal sequence #status predicted #label SIG\ !$36-302 #product ricin D chain A #status experimental #label !8ACH\ !$46-293 #domain rRNA N-glycosidase homology #label RNG\ !$315-576 #product ricin D chain B #status experimental #label !8BCH\ !$331-373,374-414, !$417-455,462-497, !$501-540,543-576 #region 40-residue repeats\ !$45,409,449 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$115,158,243,244 #binding_site substrate (Tyr, Tyr, Glu, Asn) #status !8predicted\ !$212 #active_site Glu #status experimental\ !$215 #active_site Arg #status predicted\ !$294-318,334-353, !$377-394,465-478, !$504-521 #disulfide_bonds #status experimental\ !$336,349,360 #binding_site N-acetylgalactosamine (Asp, Gln, Asn) !8#status experimental\ !$548,569 #binding_site N-acetylgalactosamine (Asp, Asn) !8#status experimental SUMMARY #length 576 #molecular-weight 64090 #checksum 6082 SEQUENCE /// ENTRY RLCSAG #type complete TITLE agglutinin precursor - castor bean CONTAINS rRNA N-glycosidase (EC 3.2.2.22) ORGANISM #formal_name Ricinus communis #common_name castor bean DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS A24261; A24210 REFERENCE A24261 !$#authors Roberts, L.M.; Lamb, I.F.; Pappin, D.J.C.; Lord, J.M. !$#journal J. Biol. Chem. (1985) 260:15682-15686 !$#title The primary sequence of Ricinus communis agglutinin. !1Comparison with ricin. !$#cross-references MUID:86059449; PMID:2999130 !$#accession A24261 !'##molecule_type mRNA !'##residues 1-564 ##label ROB !'##cross-references GB:M12089; NID:g169700; PIDN:AAA33869.1; !1PID:g169701 REFERENCE A24210 !$#authors Araki, T.; Yoshioka, Y.; Funatsu, G. !$#journal Biochim. Biophys. Acta (1986) 872:277-285 !$#title The complete amino acid sequence of the B-chain of the !1Ricinus communis agglutinin isolated from large-grain castor !1bean seeds. !$#accession A24210 !'##molecule_type protein !'##residues 303-325,'F',327-330,'T',332-361,'D',363-373,'G',375-403, !1'T',405-551,'V',553-564 ##label ARA COMMENT This protein has strong agglutinating activity and weak !1cytotoxicity compared with ricin D. CLASSIFICATION #superfamily ricin; rRNA N-glycosidase homology KEYWORDS duplication; glycoprotein; glycosidase; hydrolase; lectin; !1RNA binding; seed; tandem repeat; toxin FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-290 #product agglutinin chain A #status predicted #label !8ACH\ !$35-281 #domain rRNA N-glycosidase homology #label RNG\ !$303-564 #product agglutinin chain B #status experimental !8#label BCH\ !$319-361,362-402, !$405-443,450-485, !$489-528,531-564 #region 40-residue repeats\ !$34,259 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$104,147,231,232 #binding_site substrate (Tyr, Tyr, Glu, Asn) #status !8predicted\ !$200,203 #active_site Glu, Arg #status predicted\ !$282-306,322-341, !$365-382,453-466, !$492-509 #disulfide_bonds #status predicted\ !$324,337,348 #binding_site N-acetylgalactosamine (Asp, Gln, Asn) !8#status predicted\ !$397,437 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$536,557 #binding_site N-acetylgalactosamine (Asp, Asn) !8#status predicted SUMMARY #length 564 #molecular-weight 62851 #checksum 5861 SEQUENCE /// ENTRY TZLSA #type fragment TITLE abrin-a precursor - Indian licorice (fragment) CONTAINS rRNA N-glycosidase (EC 3.2.2.22) ORGANISM #formal_name Abrus precatorius #common_name Indian licorice DATE 31-Dec-1993 #sequence_revision 01-Aug-1997 #text_change 16-Jul-1999 ACCESSIONS S32429; JT0202; A39761; JC1398; S14472; S24133; S74110; !1S74111 REFERENCE S32429 !$#authors Hung, C.H.; Lee, M.C.; Lee, T.C.; Lin, J.Y. !$#journal J. Mol. Biol. (1993) 229:263-267 !$#title Primary structure of three distinct isoabrins determined by !1cDNA sequencing. Conservation and significance. !$#cross-references MUID:93132798; PMID:8421313 !$#accession S32429 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 'E',2-528 ##label HUN !'##cross-references GB:M98344; NID:g166294; PIDN:AAA32624.1; !1PID:g166295 !'##note the coding region for the sequence shown is preceded by an ATG !1codon !'##note residues 1-8 were derived from the synthesized primer REFERENCE JT0202 !$#authors Funatsu, G.; Taguchi, Y.; Kamenosono, M.; Yanaka, M. !$#journal Agric. Biol. Chem. (1988) 52:1095-1097 !$#title The complete amino acid sequence of the A-chain of abrin-a, !1a toxic protein from the seeds of Abrus precatorius. !$#accession JT0202 !'##molecule_type protein !'##residues 1-201,203-251 ##label FUN !'##note the amino-terminal residue forms pyrrolidone carboxylic acid; !1therefore, we have shown it as Gln REFERENCE A39761 !$#authors Evensen, G.; Mathiesen, A.; Sundan, A. !$#journal J. Biol. Chem. (1991) 266:6848-6852 !$#title Direct molecular cloning and expression of two distinct !1abrin A-chains. !$#cross-references MUID:91201329; PMID:2016300 !$#accession A39761 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 'E',2-251 ##label EVE !'##cross-references GB:X54872 !'##note residues 1-8 were derived from the synthesized primer REFERENCE JC1398 !$#authors Kimura, M.; Sumizawa, T.; Funatsu, G. !$#journal Biosci. Biotechnol. Biochem. (1993) 57:166-169 !$#title The complete amino acid sequences of the B-chains of Abrin-a !1and Abrin-b, toxic proteins from the seeds of Abrus !1precatorius. !$#cross-references MUID:93169023; PMID:7763422 !$#contents seeds !$#accession JC1398 !'##molecule_type protein !'##residues 261-347,'T',349-351,'A',353-357,'L',359-528 ##label KIM !'##experimental_source seed REFERENCE S14471 !$#authors Evensen, G.; Mathiesen, A.; Sundan, A. !$#submission submitted to the EMBL Data Library, October 1990 !$#description Direct molecular cloning of two distinct abrin A-chains. !$#accession S14472 !'##status preliminary !'##molecule_type DNA !'##residues 'ME',2-251 ##label EV2 !'##cross-references EMBL:X54873; NID:g16090; PIDN:CAA38655.1; !1PID:g16091 REFERENCE S24133 !$#authors Chen, Y.L.; Chow, L.P.; Tsugita, A.; Lin, J.Y. !$#journal FEBS Lett. (1992) 309:115-118 !$#title The complete primary structure of abrin-a B chain. !$#cross-references MUID:92371656; PMID:1505674 !$#accession S24133 !'##molecule_type protein !'##residues 262-297,'Y',299-426,'L',428-466,'P',468-482,'L',484-528 !1##label CHE REFERENCE S74110 !$#authors Lin, S.H.; Chow, L.P.; Chen, Y.L.; Liaw, Y.C.; Chen, J.K.; !1Lin, J.Y. !$#journal Eur. J. Biochem. (1996) 240:564-569 !$#title Probing the domain structure of abrin-a by tryptic !1digestion. !$#cross-references MUID:97008945; PMID:8856055 !$#accession S74110 !'##molecule_type protein !'##residues 89-108;154-172 ##label LIN !'##experimental_source seed !$#accession S74111 !'##molecule_type protein !'##residues 262-276,'X',278-280;329-348;369-388;399-418 ##label LIW !'##experimental_source seed COMMENT Abrin-a is more toxic than ricin. The toxin consists of an A !1chain, which inhibits protein synthesis by inactivating 60S !1ribosomal subunits, and a B chain, which binds to the !1galactose-containing receptors on the cell surface. The A !1and B chains are linked by a single disulfide bond, which is !1essential for toxicity. CLASSIFICATION #superfamily ricin; rRNA N-glycosidase homology KEYWORDS duplication; glycoprotein; glycosidase; hydrolase; lectin; !1pyroglutamic acid; RNA binding; seed; tandem repeat; toxin FEATURE !$1-251 #product abrin-a chain A #status experimental #label !8ACH\ !$7-246 #domain rRNA N-glycosidase homology #label RNG\ !$261-528 #product abrin-a chain B #status experimental #label !8BCH\ !$283-325,326-366, !$369-407,414-449, !$453-492,495-528 #region 40-residue repeats\ !$1 #modified_site pyrrolidone carboxylic acid (Gln) !8#status experimental\ !$74,113,195,196 #binding_site substrate (Tyr, Tyr, Glu, Asn) #status !8predicted\ !$164,167 #active_site Glu, Arg #status predicted\ !$247-269,286-305, !$329-346,417-430, !$456-473 #disulfide_bonds #status predicted\ !$288,312 #binding_site N-acetylgalactosamine (Asp, Asn) !8#status predicted\ !$361,401 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$500,521 #binding_site N-acetylgalactosamine (Asp, Asn) !8#status predicted SUMMARY #length 528 #checksum 1325 SEQUENCE /// ENTRY MLDIA #type complete TITLE monellin chain A [validated] - serendipity berry ALTERNATE_NAMES monellin chain I ORGANISM #formal_name Dioscoreophyllum cumminsii #common_name serendipity berry DATE 24-Apr-1984 #sequence_revision 25-Oct-1996 #text_change 15-Sep-2000 ACCESSIONS JH0209; A91670; A90197; A90607; A03375 REFERENCE JH0209 !$#authors Kohmura, M.; Nio, N.; Ariyoshi, Y. !$#journal Agric. Biol. Chem. (1990) 54:2219-2224 !$#title Complete amino acid sequence of the sweet protein monellin. !$#cross-references MUID:91136778; PMID:1368575 !$#accession JH0209 !'##molecule_type protein !'##residues 1-45 ##label KOH !'##experimental_source strain [Stapf] Diels !'##note the ratio of monellin A, and Phe-A was 90:10 REFERENCE A91670 !$#authors Frank, G.; Zuber, H. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1976) 357:585-592 !$#title The complete amino acid sequences of both subunits of the !1sweet protein monellin. !$#cross-references MUID:77004858; PMID:964918 !$#accession A91670 !'##molecule_type protein !'##residues 2-45 ##label FRA !'##note in approximately 10% of the chains, a Phe preceded 1-Arg REFERENCE A90197 !$#authors Hudson, G.; Biemann, K. !$#journal Biochem. Biophys. Res. Commun. (1976) 71:212-220 !$#title Mass spectrometric sequencing of proteins. The structure of !1subunit I of monellin. !$#cross-references MUID:76277941; PMID:962914 !$#accession A90197 !'##molecule_type protein !'##residues 2-45 ##label HUD REFERENCE A90607 !$#authors Bohak, Z.; Li, S.L. !$#journal Biochim. Biophys. Acta (1976) 427:153-170 !$#title The structure of monellin and its relation to the sweetness !1of the protein. !$#cross-references MUID:76161292; PMID:4107 !$#contents amides !$#accession A90607 !'##molecule_type protein !'##residues 2-22,'N',24-25,'QN',28 ##label BOH !'##note this sequence is called chain I by the authors REFERENCE A51514 !$#authors Jiang, F.; Tong, L.; Kim, S.H. !$#submission submitted to the Brookhaven Protein Data Bank, August 1992 !$#cross-references PDB:3MON !$#contents annotation; X-ray crystallography, 2.8 angstroms, residues !12-45 REFERENCE A58205 !$#authors Ogata, C.; Hatada, M.; Tomlinson, G.; Shin, W.C.; Kim, S.H. !$#journal Nature (1987) 328:739-742 !$#title Crystal structure of the intensely sweet protein monellin. !$#cross-references MUID:87287292; PMID:3614382 !$#contents annotation; X-ray crystallography, 3.0 angstroms, residues !12-45 COMMENT It is possible that both chains are derived from a single !1precursor chain. COMPLEX heterodimer (see PIR:MLDIB) CLASSIFICATION #superfamily monellin chain A KEYWORDS heterodimer; sweet taste FEATURE !$1-45 #product monellin chain Phe-A #status experimental !8#label MAT2\ !$2-45 #product monellin chain A #status experimental #label !8MAT1 SUMMARY #length 45 #molecular-weight 5398 #checksum 95 SEQUENCE /// ENTRY MLDIB #type complete TITLE monellin chain B [validated] - serendipity berry ALTERNATE_NAMES monellin chain II ORGANISM #formal_name Dioscoreophyllum cumminsii #common_name serendipity berry DATE 24-Apr-1984 #sequence_revision 25-Oct-1996 #text_change 15-Sep-2000 ACCESSIONS JH0210; B91670; B90607; A03376 REFERENCE JH0209 !$#authors Kohmura, M.; Nio, N.; Ariyoshi, Y. !$#journal Agric. Biol. Chem. (1990) 54:2219-2224 !$#title Complete amino acid sequence of the sweet protein monellin. !$#cross-references MUID:91136778; PMID:1368575 !$#accession JH0210 !'##molecule_type protein !'##residues 1-51 ##label KOH !'##experimental_source strain [Stapf] Diels !'##note the ratio of monellin B, des-Gly-B and Thr-B was 57:24:19 REFERENCE A91670 !$#authors Frank, G.; Zuber, H. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1976) 357:585-592 !$#title The complete amino acid sequences of both subunits of the !1sweet protein monellin. !$#cross-references MUID:77004858; PMID:964918 !$#accession B91670 !'##molecule_type protein !'##residues 2-49,'NE' ##label FRA REFERENCE A90607 !$#authors Bohak, Z.; Li, S.L. !$#journal Biochim. Biophys. Acta (1976) 427:153-170 !$#title The structure of monellin and its relation to the sweetness !1of the protein. !$#cross-references MUID:76161292; PMID:4107 !$#accession B90607 !'##molecule_type protein !'##residues 2-51 ##label BOH !'##note this sequence is called chain II by the authors REFERENCE A51514 !$#authors Jiang, F.; Tong, L.; Kim, S.H. !$#submission submitted to the Brookhaven Protein Data Bank, August 1992 !$#cross-references PDB:3MON !$#contents annotation; X-ray crystallography, 2.8 angstroms, residues !12-49,'NE' REFERENCE A58205 !$#authors Ogata, C.; Hatada, M.; Tomlinson, G.; Shin, W.C.; Kim, S.H. !$#journal Nature (1987) 328:739-742 !$#title Crystal structure of the intensely sweet protein monellin. !$#cross-references MUID:87287292; PMID:3614382 !$#contents annotation; X-ray crystallography, 3.0 angstroms, residues !12-49,'NE' COMMENT It is possible that both chains are derived from a single !1precursor chain. COMMENT Blocking of the active site cysteine abolishes the sweet !1taste. COMPLEX heterodimer (see PIR:MLDIA) CLASSIFICATION #superfamily monellin chain B KEYWORDS heterodimer; sweet taste FEATURE !$1-51 #product monellin chain Thr-B #status experimental !8#label MAT3\ !$2-51 #product monellin chain B #status experimental #label !8MAT1\ !$3-51 #product monellin chain des-Gly-B #status !8experimental #label MAT2\ !$42 #active_site Cys #status experimental SUMMARY #length 51 #molecular-weight 5936 #checksum 1001 SEQUENCE /// ENTRY QTTC1 #type complete TITLE thaumatin I [validated] - miracle fruit ORGANISM #formal_name Thaumatococcus daniellii #common_name miracle fruit DATE 30-Nov-1979 #sequence_revision 30-Nov-1979 #text_change 15-Sep-2000 ACCESSIONS A03377 REFERENCE A03377 !$#authors Iyengar, R.B.; Smits, P.; van der Ouderaa, F.; van der Wel, !1H.; van Brouwershaven, J.; Ravestein, P.; Richters, G.; van !1Wassenaar, P.D. !$#journal Eur. J. Biochem. (1979) 96:193-204 !$#title The complete amino-acid sequence of the sweet protein !1thaumatin I. !$#cross-references MUID:79213425; PMID:456365 !$#accession A03377 !'##molecule_type protein !'##residues 1-207 ##label IYE REFERENCE A50367 !$#authors Kim, S.H. !$#submission submitted to the Brookhaven Protein Data Bank, May 1989 !$#cross-references PDB:1THI !$#contents annotation; X-ray crystallography, 3.2 angstroms REFERENCE A58204 !$#authors de Vos, A.M.; Hatada, M.; van der Wel, H.; Krabbendam, H.; !1Peerdeman, A.F.; Kim, S.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:1406-1409 !$#title Three-dimensional structure of thaumatin I, an intensely !1sweet protein. !$#cross-references MUID:85140305; PMID:3856268 !$#contents annotation; X-ray crystallography, 3.1 angstroms, residues !11-207 COMMENT Thaumatin I is one of two intensely sweet-tasting proteins !1from the aril (the seed coat) of this plant, a member of the !1monocotyledonous arrowroot family. CLASSIFICATION #superfamily thaumatin I KEYWORDS seed; sweet taste FEATURE !$9-204,56-66,71-77, !$121-193,126-177, !$134-145,149-158, !$159-164 #disulfide_bonds #status experimental SUMMARY #length 207 #molecular-weight 22204 #checksum 8953 SEQUENCE /// ENTRY QTTC2 #type complete TITLE thaumatin II precursor - miracle fruit ORGANISM #formal_name Thaumatococcus daniellii #common_name miracle fruit DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 16-Jul-1999 ACCESSIONS A03378 REFERENCE A03378 !$#authors Edens, L.; Heslinga, L.; Klok, R.; Ledeboer, A.M.; Maat, J.; !1Toonen, M.Y.; Visser, C.; Verrips, C.T. !$#journal Gene (1982) 18:1-12 !$#title Cloning of cDNA encoding the sweet-tasting plant protein !1thaumatin and its expression in Escherichia coli. !$#cross-references MUID:82262799; PMID:7049841 !$#accession A03378 !'##molecule_type mRNA !'##residues 1-235 ##label EDE !'##cross-references GB:J01209; NID:g170190; PIDN:AAA93095.1; !1PID:g170191 COMMENT Thaumatin II is one of two intensely sweet-tasting proteins !1from the aril (the seed coat) of this plant, a member of the !1monocotyledonous arrowroot family. CLASSIFICATION #superfamily thaumatin I KEYWORDS seed; sweet taste FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-229 #product thaumatin II #status predicted #label MAT\ !$230-235 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$31-226,78-88,93-99, !$143-215,148-199, !$156-167,171-180, !$181-186 #disulfide_bonds #status predicted SUMMARY #length 235 #molecular-weight 25523 #checksum 621 SEQUENCE /// ENTRY VCTO14 #type complete TITLE pathogenesis-related protein P6 precursor - tomato ALTERNATE_NAMES ethylene-induced protein P1; ethylene-induced protein p14; PR protein P6 ORGANISM #formal_name Lycopersicon esculentum #common_name tomato DATE 04-Dec-1986 #sequence_revision 21-Jan-1997 #text_change 16-Jul-1999 ACCESSIONS S26239; S61709; S29628; A03379 REFERENCE S26238 !$#authors van Kan, J.A.L.; Joosten, M.H.A.J.; Wagemakers, C.A.M.; van !1den Berg-Velthuis, G.C.M.; de Wit, P.J.G.M. !$#journal Plant Mol. Biol. (1992) 20:513-527 !$#title Differential accumulation of mRNAs encoding extracellular !1and intracellular PR proteins in tomato induced by virulent !1and avirulent races of Cladosporium fulvum. !$#cross-references MUID:93043041; PMID:1421154 !$#accession S26239 !'##molecule_type mRNA !'##residues 1-159 ##label KAN !'##cross-references EMBL:M69248; NID:g170489; PIDN:AAA03616.1; !1PID:g170490 !$#accession S61709 !'##molecule_type protein !'##residues 40-56;65-78;90-106;117-121 ##label KAW REFERENCE S29628 !$#authors Vera, P.; Tornero, P. !$#submission submitted to the EMBL Data Library, September 1992 !$#description Isolation of a cDNA clone encoding "pathogenesis-related". !$#accession S29628 !'##molecule_type mRNA !'##residues 1-159 ##label VER !'##cross-references EMBL:X68738; NID:g19284; PIDN:CAA48672.1; !1PID:g19285 REFERENCE A91019 !$#authors Lucas, J.; Camacho Henriquez, A.; Lottspeich, F.; Henschen, !1A.; Sanger, H.L. !$#journal EMBO J. (1985) 4:2745-2749 !$#title Amino acid sequence of the 'pathogenesis-related' leaf !1protein p14 from viroid-infected tomato reveals a new type !1of structurally unfamiliar proteins. !$#accession A03379 !'##molecule_type protein !'##residues 25-122,128-159 ##label LUC !'##experimental_source cv. Rutgers COMMENT Three disulfide bonds are present. CLASSIFICATION #superfamily pathogenesis-related leaf protein KEYWORDS pyroglutamic acid; viroid-induced protein FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-159 #product pathogenesis-related protein isomer P6 !8#status experimental #label MAT\ !$25 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental SUMMARY #length 159 #molecular-weight 17520 #checksum 2513 SEQUENCE /// ENTRY SNFB1 #type complete TITLE pathogenesis-related protein PvPR1 - kidney bean (cv. Canadian Wonder and cv. Saxa) ALTERNATE_NAMES pathogenesis-related protein PR2 ORGANISM #formal_name Phaseolus vulgaris #common_name kidney bean #variety cv. Canadian Wonder; cv. Saxa DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS S11929; S14730 REFERENCE S11929 !$#authors Walter, M.H.; Liu, J.W.; Grand, C.; Lamb, C.J.; Hess, D. !$#journal Mol. Gen. Genet. (1990) 222:353-360 !$#title Bean pathogenesis-related (PR) proteins deduced from !1elicitor-induced transcripts are members of a ubiquitous new !1class of conserved PR proteins including pollen allergens. !$#cross-references MUID:91109723; PMID:2274036 !$#accession S11929 !'##molecule_type mRNA !'##residues 1-156 ##label MOL !'##cross-references EMBL:X61365; NID:g21043; PIDN:CAA43637.1; !1PID:g21044 !'##experimental_source cv. Canadian Wonder REFERENCE S14730 !$#authors Awade, A.; Metz-Boutigue, M.H.; le Ret, M.; Genot, G.; !1Amiri, I.; Burkard, G. !$#journal Biochim. Biophys. Acta (1991) 1077:241-244 !$#title The complete amino acid sequence of the pathogenesis-related !1(PR2) protein induced in chemically stressed bean leaves. !$#cross-references MUID:91198134; PMID:2015296 !$#accession S14730 !'##molecule_type protein !'##residues 2-156 ##label AWA !'##experimental_source cv. Saxa CLASSIFICATION #superfamily pathogenesis-related protein KEYWORDS stress-induced protein FEATURE !$2-156 #product pathogenesis-related protein PvPR1 #status !8experimental #label MAT SUMMARY #length 156 #molecular-weight 16528 #checksum 6326 SEQUENCE /// ENTRY SNFB2 #type complete TITLE pathogenesis-related protein 2 - kidney bean ORGANISM #formal_name Phaseolus vulgaris #common_name kidney bean DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS S11930 REFERENCE S11929 !$#authors Walter, M.H.; Liu, J.W.; Grand, C.; Lamb, C.J.; Hess, D. !$#journal Mol. Gen. Genet. (1990) 222:353-360 !$#title Bean pathogenesis-related (PR) proteins deduced from !1elicitor-induced transcripts are members of a ubiquitous new !1class of conserved PR proteins including pollen allergens. !$#cross-references MUID:91109723; PMID:2274036 !$#accession S11930 !'##molecule_type mRNA !'##residues 1-155 ##label WAL !'##cross-references EMBL:X61364; NID:g21047; PIDN:CAA43636.1; !1PID:g21048 CLASSIFICATION #superfamily pathogenesis-related protein SUMMARY #length 155 #molecular-weight 16402 #checksum 4572 SEQUENCE /// ENTRY SNUMP #type complete TITLE sillucin - Rhizomucor pusillus ORGANISM #formal_name Rhizomucor pusillus DATE 30-Jun-1979 #sequence_revision 30-Jun-1979 #text_change 18-Oct-1996 ACCESSIONS A03380 REFERENCE A03380 !$#authors Bradley, W.A.; Somkuti, G.A. !$#journal FEBS Lett. (1979) 97:81-83 !$#title The primary structure of sillucin and antimicrobial peptide !1from Mucor pusillus. !$#cross-references MUID:79107453; PMID:761621 !$#accession A03380 !'##molecule_type protein !'##residues 1-30 ##label BRA !'##note four disulfide bonds are present COMMENT Sillucin is an antimicrobial agent produced by the !1thermophilic fungus Rhizomucor pusillus in liquid culture; !1it is effective against gram-positive bacteria at the level !1of RNA metabolism. CLASSIFICATION #superfamily sillucin KEYWORDS antibiotic SUMMARY #length 30 #molecular-weight 3209 #checksum 5242 SEQUENCE /// ENTRY DLDOIA #type complete TITLE discoidin I chain A - slime mold (Dictyostelium discoideum) ORGANISM #formal_name Dictyostelium discoideum DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 31-Oct-1997 ACCESSIONS A03381 REFERENCE A92876 !$#authors Poole, S.; Firtel, R.A.; Lamar, E.; Rowekamp, W. !$#journal J. Mol. Biol. (1981) 153:273-289 !$#title Sequence and expression of the discoidin I gene family in !1Dictyostelium discoideum. !$#cross-references MUID:82170475; PMID:6279874 !$#accession A03381 !'##molecule_type DNA !'##residues 1-253 ##label POO COMMENT The authors translated the codon CAA for residue 152 as Glu. COMMENT The A chain is the product of one of the four genes in the !1discoidin I family. COMMENT Discoidin I is a tetrameric lectin that appears on the cell !1surface during aggregation of amoebae (to form fruiting !1structures) and that is involved in cell-cell cohesion. It !1binds to galactose and modified galactose residues. CLASSIFICATION #superfamily discoidin I chain A; discoidin I amino-terminal !1homology KEYWORDS cell adhesion; lectin FEATURE !$1-152 #domain discoidin I amino-terminal homology #label !8DN1 SUMMARY #length 253 #molecular-weight 28258 #checksum 5211 SEQUENCE /// ENTRY DLDOIC #type complete TITLE discoidin I chain C - slime mold (Dictyostelium discoideum) ORGANISM #formal_name Dictyostelium discoideum DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 16-Jul-1999 ACCESSIONS A03382 REFERENCE A92876 !$#authors Poole, S.; Firtel, R.A.; Lamar, E.; Rowekamp, W. !$#journal J. Mol. Biol. (1981) 153:273-289 !$#title Sequence and expression of the discoidin I gene family in !1Dictyostelium discoideum. !$#cross-references MUID:82170475; PMID:6279874 !$#accession A03382 !'##molecule_type DNA !'##residues 1-253 ##label POO !'##cross-references GB:J01284; NID:g167760; PIDN:AAA33199.1; !1PID:g167763 !'##note the authors translated the codon CAA for residue 152 as Glu COMMENT The C chain is the product of one of the four genes in the !1discoidin I family. CLASSIFICATION #superfamily discoidin I chain A; discoidin I amino-terminal !1homology KEYWORDS cell adhesion; lectin FEATURE !$1-152 #domain discoidin I amino-terminal homology #label !8DN1 SUMMARY #length 253 #molecular-weight 28392 #checksum 5570 SEQUENCE /// ENTRY DLDOID #type fragment TITLE discoidin I chain D - slime mold (Dictyostelium discoideum) (fragment) ORGANISM #formal_name Dictyostelium discoideum DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 16-Jul-1999 ACCESSIONS A03383 REFERENCE A92876 !$#authors Poole, S.; Firtel, R.A.; Lamar, E.; Rowekamp, W. !$#journal J. Mol. Biol. (1981) 153:273-289 !$#title Sequence and expression of the discoidin I gene family in !1Dictyostelium discoideum. !$#cross-references MUID:82170475; PMID:6279874 !$#accession A03383 !'##molecule_type DNA !'##residues 1-149 ##label POO !'##cross-references GB:J01285; NID:g167761; PIDN:AAA33200.1; !1PID:g167764 COMMENT The D chain is the product of one of the four genes in the !1discoidin I family. CLASSIFICATION #superfamily discoidin I chain A; discoidin I amino-terminal !1homology KEYWORDS cell adhesion; lectin FEATURE !$1-149 #domain discoidin I amino-terminal homology !8(fragment) #label DN1 SUMMARY #length 149 #checksum 3432 SEQUENCE /// ENTRY YPDOD1 #type complete TITLE prestalk D11 protein precursor - slime mold (Dictyostelium discoideum) ORGANISM #formal_name Dictyostelium discoideum DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 12-Apr-1996 ACCESSIONS A23754 REFERENCE A23754 !$#authors Barklis, E.; Pontius, B.; Lodish, H.F. !$#journal Mol. Cell. Biol. (1985) 5:1473-1479 !$#title Structure of the Dictyostelium discoideum prestalk D11 gene !1and protein. !$#cross-references MUID:85295982; PMID:4033661 !$#accession A23754 !'##molecule_type DNA !'##residues 1-282 ##label BAR !'##note the authors translated the codon GAA for residue 54 as Val, CAA !1for residue 69 as Asp, GAA for residue 116 as Val, CAA for !1residue 146 as Glu, and CAA for residue 164 as Asn COMMENT The D11 mRNA is present at low levels in the amoeboid and !1early developing cells and reaches up to 20-fold higher !1levels during later stages of development of the fruiting !1bodies. COMMENT This protein has many features in common with the !1phosphodiesterase inhibitor, which is active during the !1aggregation phase of development. CLASSIFICATION #superfamily prestalk D11 protein FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$25-64,88-126 #region duplication type A repeats\ !$26-282 #product prestalk D11 protein #status predicted !8#label MPT\ !$65-82,127-144, !$160-177,193-210, !$227-244,261-276 #region duplication type B repeats\ !$145-159,178-192, !$211-226,245-260 #region duplication type C repeats SUMMARY #length 282 #molecular-weight 31073 #checksum 6017 SEQUENCE /// ENTRY VUWTEM #type complete TITLE embryonic abundant protein Em - wheat ALTERNATE_NAMES ABA-regulated major embryo protein ORGANISM #formal_name Triticum aestivum #common_name common wheat DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS A56626; S11747 REFERENCE A56626 !$#authors Litts, J.C.; Colwell, G.W.; Chakerian, R.L.; Quatrano, R.S. !$#journal DNA Seq. (1991) 1:263-274 !$#title Sequence analysis of a functional member of the Em gene !1family from wheat. !$#cross-references MUID:92216128; PMID:1806042 !$#contents var. Chinese Spring !$#accession A56626 !'##molecule_type DNA !'##residues 1-94 ##label LIT !'##cross-references EMBL:X52103; NID:g21729; PIDN:CAA36323.1; !1PID:g295844 GENETICS !$#introns 41/1 CLASSIFICATION #superfamily embryonic abundant protein Em KEYWORDS seed; stress-induced protein FEATURE !$2-94 #product embryonic abundant protein Em #status !8predicted #label MAT SUMMARY #length 94 #molecular-weight 9987 #checksum 6870 SEQUENCE /// ENTRY VUQB1B #type complete TITLE BabR protein 1 - Babesia bovis ORGANISM #formal_name Babesia bovis DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 31-Dec-1993 ACCESSIONS A03385 REFERENCE A90849 !$#authors Cowman, A.F.; Bernard, O.; Stewart, N.; Kemp, D.J. !$#journal Cell (1984) 37:653-660 !$#title Genes of the protozoan parasite Babesia bovis that rearrange !1to produce RNA species with different sequences. !$#cross-references MUID:84205701; PMID:6327081 !$#accession A03385 !'##molecule_type mRNA !'##residues 1-191 ##label COW COMMENT The sequences of the BabR proteins are nearly identical, !1differing only at their carboxyl ends. COMMENT Babesia bovis is a protozoan. CLASSIFICATION #superfamily BabR protein SUMMARY #length 191 #molecular-weight 22193 #checksum 3908 SEQUENCE /// ENTRY VUQB2B #type complete TITLE BabR protein 2 - Babesia bovis ORGANISM #formal_name Babesia bovis DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 31-Dec-1993 ACCESSIONS A03386 REFERENCE A90849 !$#authors Cowman, A.F.; Bernard, O.; Stewart, N.; Kemp, D.J. !$#journal Cell (1984) 37:653-660 !$#title Genes of the protozoan parasite Babesia bovis that rearrange !1to produce RNA species with different sequences. !$#cross-references MUID:84205701; PMID:6327081 !$#accession A03386 !'##molecule_type mRNA !'##residues 1-200 ##label COW COMMENT The sequences of the BabR proteins are nearly identical, !1differing only at their carboxyl ends. CLASSIFICATION #superfamily BabR protein SUMMARY #length 200 #molecular-weight 22948 #checksum 820 SEQUENCE /// ENTRY VUQB3B #type complete TITLE BabR protein 3 - Babesia bovis ORGANISM #formal_name Babesia bovis DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 31-Dec-1993 ACCESSIONS A03387 REFERENCE A90849 !$#authors Cowman, A.F.; Bernard, O.; Stewart, N.; Kemp, D.J. !$#journal Cell (1984) 37:653-660 !$#title Genes of the protozoan parasite Babesia bovis that rearrange !1to produce RNA species with different sequences. !$#cross-references MUID:84205701; PMID:6327081 !$#accession A03387 !'##molecule_type mRNA !'##residues 1-212 ##label COW COMMENT The sequences of the BabR proteins are nearly identical, !1differing only at their carboxyl ends. CLASSIFICATION #superfamily BabR protein SUMMARY #length 212 #molecular-weight 24338 #checksum 3013 SEQUENCE /// ENTRY OZZQAF #type complete TITLE circumsporozoite protein - malaria parasite (Plasmodium falciparum) (isolate IMTM22) ORGANISM #formal_name Plasmodium falciparum DATE 15-Nov-1984 #sequence_revision 15-Nov-1984 #text_change 09-Jun-2000 ACCESSIONS A03388 REFERENCE A03388 !$#authors Dame, J.B.; Williams, J.L.; McCutchan, T.F.; Weber, J.L.; !1Wirtz, R.A.; Hochmeyer, W.T.; Maloy, W.L.; Haynes, J.D.; !1Schneider, I.; Roberts, D.; Sanders, G.S.; Reddy, E.P.; !1Diggs, C.L.; Miller, L.H. !$#journal Science (1984) 225:593-599 !$#title Structure of the gene encoding the immunodominant surface !1antigen on the sporozoite of the human malaria parasite !1Plasmodium falciparum. !$#cross-references MUID:84250215; PMID:6204383 !$#accession A03388 !'##molecule_type DNA !'##residues 1-412 ##label DAM !'##cross-references GB:K02194; NID:g160160; PIDN:AAA29524.1; !1PID:g160161 !'##experimental_source clone 7G8 COMMENT Residues 1-16 are the probable signal sequence. COMMENT There are 41 copies of a 4-residue repeating unit in the !1middle domain of the protein. CLASSIFICATION #superfamily circumsporozoite protein; thrombospondin type 1 !1repeat homology FEATURE !$336-390 #domain thrombospondin type 1 repeat homology #label !8THR1 SUMMARY #length 412 #molecular-weight 44420 #checksum 4667 SEQUENCE /// ENTRY OZZQMY #type complete TITLE circumsporozoite protein precursor - Plasmodium yoelii ALTERNATE_NAMES sporozoite surface antigen ORGANISM #formal_name Plasmodium yoelii DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Jul-1999 ACCESSIONS A26271 REFERENCE A26271 !$#authors Lal, A.A.; de la Cruz, V.F.; Welsh, J.A.; Charoenvit, Y.; !1Maloy, W.L.; McCutchan, T.F. !$#journal J. Biol. Chem. (1987) 262:2937-2940 !$#title Structure of the gene encoding the circumsporozoite protein !1of Plasmodium yoelli. !$#cross-references MUID:87137555; PMID:3102479 !$#accession A26271 !'##molecule_type DNA !'##residues 1-367 ##label LAL !'##cross-references GB:J02695; NID:g160222; PIDN:AAA29558.1; !1PID:g160223 COMMENT There are three distinct regions in the mature !1circumsporozoite protein, the amino-terminal region, the !1middle repeat region, and the carboxyl-terminal conserved !1region ending in a hydrophobic membrane-anchoring sequence. COMMENT There are 15 copies of a 6-residue repeat and 8 copies of a !14-residue repeat. CLASSIFICATION #superfamily circumsporozoite protein; thrombospondin type 1 !1repeat homology KEYWORDS sporozoite; surface antigen; tandem repeat FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-367 #product circumsporozoite protein #status predicted !8#label MAT\ !$139-228 #region 6-residue repeats (Q-G-P-G-A-P)\ !$229-260 #region 4-residue repeats (Q-Q-P-P)\ !$293-345 #domain thrombospondin type 1 repeat homology #label !8THR1 SUMMARY #length 367 #molecular-weight 38888 #checksum 6918 SEQUENCE /// ENTRY OZZQBK #type complete TITLE circumsporozoite protein precursor - Plasmodium berghei (strain ANKA clone 2.34L) ALTERNATE_NAMES sporozoite surface antigen ORGANISM #formal_name Plasmodium berghei DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS S07873; S12571 REFERENCE S07873 !$#authors Lockyer, M.J.; Davies, C.S.; Suhrbier, A.; Sinden, R.E. !$#journal Nucleic Acids Res. (1990) 18:376 !$#title Nucleotide sequence of the Plasmodium berghei !1circumsporozoite protein gene from the ANKA clone 2.34L. !$#cross-references MUID:90221834; PMID:2183186 !$#accession S07873 !'##molecule_type DNA !'##residues 1-348 ##label LOC !'##cross-references EMBL:X17606 REFERENCE S12571 !$#authors Lockyer, M.J. !$#submission submitted to the EMBL Data Library, November 1989 !$#accession S12571 !'##molecule_type DNA !'##residues 1-59,'I',61-81,83-348 ##label LOC2 !'##cross-references EMBL:X17606; NID:g9784; PIDN:CAA35608.1; PID:g9785 CLASSIFICATION #superfamily circumsporozoite protein; thrombospondin type 1 !1repeat homology KEYWORDS tandem repeat FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-348 #product circumsporozoite protein #status predicted !8#label MAT\ !$94-205 #region 8-residue repeats\ !$215-247 #region 2-residue repeats\ !$274-326 #domain thrombospondin type 1 repeat homology #label !8THR1 SUMMARY #length 348 #molecular-weight 37906 #checksum 1626 SEQUENCE /// ENTRY OZZQMB #type complete TITLE circumsporozoite protein precursor - Plasmodium berghei (strain NK65) ALTERNATE_NAMES sporozoite surface antigen ORGANISM #formal_name Plasmodium berghei DATE 30-Sep-1987 #sequence_revision 28-Jul-1995 #text_change 16-Jul-1999 ACCESSIONS A44948; A25083; S13446 REFERENCE A44948 !$#authors Lanar, D.E. !$#journal Mol. Biochem. Parasitol. (1990) 39:151-154 !$#title Sequence of the circumsporozoite gene of Plasmodium berghei !1ANKA clone and NK65 strain. !$#cross-references MUID:90158693; PMID:2406593 !$#accession A44948 !'##molecule_type DNA !'##residues 1-332 ##label LAN !'##cross-references GB:M28887 REFERENCE A25083 !$#authors Eichinger, D.J.; Arnot, D.E.; Tam, J.P.; Nussenzweig, V.; !1Enea, V. !$#journal Mol. Cell. Biol. (1986) 6:3965-3972 !$#title Circumsporozoite protein of Plasmodium berghei: gene cloning !1and identification of the immunodominant epitopes. !$#cross-references MUID:87089740; PMID:2432395 !$#accession A25083 !'##molecule_type DNA !'##residues 1-26,'I',28-68,'PMLRR',75-126,'P',128-134,'PPPNANDP', !1135-332 ##label EIC !'##cross-references GB:M14135; NID:g160245; PIDN:AAA29577.1; !1PID:g160246 REFERENCE S13446 !$#authors Weber, J.L.; Egan, J.E.; Lyon, J.A.; Wirtz, R.A.; !1Charoenvit, Y.; Maloy, W.L.; Hockmeyer, W.T. !$#journal Exp. Parasitol. (1987) 63:295-300 !$#title Plasmodium berghei: cloning of the circumsporozoite protein !1gene. !$#cross-references MUID:87218962; PMID:3556207 !$#accession S13446 !'##status preliminary !'##molecule_type DNA !'##residues 61-122,'A',124-332 ##label WEB !'##cross-references GB:M25445; NID:g160177; PIDN:AAA29531.1; !1PID:g160178 COMMENT There are three distinct regions in the mature !1circumsporozoite protein, the amino-terminal region, the !1middle repeat region, and the carboxyl-terminal conserved !1region ending in a hydrophobic membrane-anchoring sequence. CLASSIFICATION #superfamily circumsporozoite protein; thrombospondin type 1 !1repeat homology KEYWORDS sporozoite; surface antigen; tandem repeat FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-332 #product circumsporozoite protein #status predicted !8#label MAT\ !$94-189 #region 8-residue repeats\ !$199-230 #region 2-residue repeats\ !$258-310 #domain thrombospondin type 1 repeat homology #label !8THR1 SUMMARY #length 332 #molecular-weight 36170 #checksum 2552 SEQUENCE /// ENTRY OZZQAK #type complete TITLE circumsporozoite protein - Plasmodium knowlesi (strain H) ORGANISM #formal_name Plasmodium knowlesi DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 16-Jul-1999 ACCESSIONS A90841; A93315; A03389 REFERENCE A90841 !$#authors Ozaki, L.S.; Svec, P.; Nussenzweig, R.S.; Nussenzweig, V.; !1Godson, G.N. !$#journal Cell (1983) 34:815-822 !$#title Structure of the Plasmodium knowlesi gene coding for the !1circumsporozoite protein. !$#cross-references MUID:84026486; PMID:6313209 !$#accession A90841 !'##molecule_type DNA !'##residues 1-363 ##label OZA !'##cross-references GB:K00822; NID:g160195; PIDN:AAA19699.1; !1PID:g160196 REFERENCE A93315 !$#authors Godson, G.N.; Ellis, J.; Svec, P.; Schlesinger, D.H.; !1Nussenzweig, V. !$#journal Nature (1983) 305:29-33 !$#title Identification and chemical synthesis of a tandemly repeated !1immunogenic region of Plasmodium knowlesi circumsporozoite !1protein. !$#cross-references MUID:83297689; PMID:6193427 !$#accession A93315 !'##molecule_type mRNA !'##residues 107-208 ##label GOD !'##cross-references GB:K00772 COMMENT At least 12 copies of a 12-residue repeating unit occur in !1this surface protein of the sporozoite. The sporozoite is !1the infective stage of the malaria parasite that is !1transmitted from the mosquito to the vertebrate host. CLASSIFICATION #superfamily circumsporozoite protein; thrombospondin type 1 !1repeat homology FEATURE !$288-341 #domain thrombospondin type 1 repeat homology #label !8THR1 SUMMARY #length 363 #molecular-weight 36793 #checksum 5476 SEQUENCE /// ENTRY OZZQKU #type complete TITLE circumsporozoite protein precursor - Plasmodium knowlesi (strain Nuri) ALTERNATE_NAMES sporozoite surface protein ORGANISM #formal_name Plasmodium knowlesi DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Jul-1999 ACCESSIONS A26253 REFERENCE A26253 !$#authors Sharma, S.; Svec, P.; Mitchell, G.H.; Godson, G.N. !$#journal Science (1985) 229:779-782 !$#title Diversity of circumsporozoite antigen genes from two strains !1of the malarial parasite Plasmodium knowlesi. !$#cross-references MUID:85272582; PMID:4023712 !$#accession A26253 !'##molecule_type DNA !'##residues 1-351 ##label SHA !'##cross-references GB:M11031; NID:g160197; PIDN:AAA29540.1; !1PID:g160198 COMMENT There are three distinct regions in the mature !1circumsporozoite protein, the amino-terminal region, the !1middle repeat region, and the carboxyl-terminal conserved !1region ending in a hydrophobic membrane-anchoring sequence. COMMENT There are 14 tandem copies of the 9-residue repeat !1E-Q-P-A-A-G-A-G/R-G (plus two less conserved copies). CLASSIFICATION #superfamily circumsporozoite protein; thrombospondin type 1 !1repeat homology KEYWORDS sporozoite; surface antigen; tandem repeat FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-351 #product circumsporozoite protein #status predicted !8#label MAT\ !$98-223 #region 9-residue repeats\ !$224-241 #region 9-residue repeats\ !$276-329 #domain thrombospondin type 1 repeat homology #label !8THR1 SUMMARY #length 351 #molecular-weight 34782 #checksum 8689 SEQUENCE /// ENTRY OZZQAV #type complete TITLE circumsporozoite protein precursor - Plasmodium vivax (strain Belem) ORGANISM #formal_name Plasmodium vivax DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 07-Nov-1997 ACCESSIONS A26256 REFERENCE A94283 !$#authors Arnot, D.E.; Barnwell, J.W.; Tam, J.P.; Nussenzweig, V.; !1Nussenzweig, R.S.; Enea, V. !$#journal Science (1985) 230:815-818 !$#title Circumsporozoite protein of Plasmodium vivax: gene cloning !1and characterization of the immunodominant epitope. !$#cross-references MUID:86044510; PMID:2414847 !$#accession A26256 !'##molecule_type DNA !'##residues 1-378 ##label ARN REFERENCE A94617 !$#authors Nussenzweig, V. !$#submission submitted to the Protein Sequence Database, April 1987 !$#contents annotation; revisions COMMENT There are three distinct regions in the mature !1circumsporozoite protein, the amino-terminal region, the !1middle repeat region, and the carboxyl-terminal conserved !1region ending in a hydrophobic membrane-anchoring sequence. COMMENT There are 19 tandem copies of the 9-residue repeat D-R-A-D/ !1A-G-Q-P-A-G. CLASSIFICATION #superfamily circumsporozoite protein; thrombospondin type 1 !1repeat homology KEYWORDS sporozoite; surface antigen; tandem repeat FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-378 #product circumsporozoite protein #status predicted !8#label MAT\ !$97-267 #region 9-residue repeats\ !$303-356 #domain thrombospondin type 1 repeat homology #label !8THR1 SUMMARY #length 378 #molecular-weight 37844 #checksum 3295 SEQUENCE /// ENTRY OZZQAB #type complete TITLE circumsporozoite protein precursor - Plasmodium cynomolgi (strain Berok) ALTERNATE_NAMES major sporozoite surface antigen ORGANISM #formal_name Plasmodium cynomolgi DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 07-Nov-1997 ACCESSIONS D26255 REFERENCE A90889 !$#authors Galinski, M.R.; Arnot, D.E.; Cochrane, A.H.; Barnwell, J.W.; !1Nussenzweig, R.S.; Enea, V. !$#journal Cell (1987) 48:311-319 !$#title The circumsporozoite gene of the Plasmodium cynomolgi !1complex. !$#cross-references MUID:87102878; PMID:3802196 !$#accession D26255 !'##molecule_type DNA !'##residues 1-378 ##label GAL COMMENT There are three distinct regions in the mature !1circumsporozoite protein, the amino-terminal region, the !1middle repeat region, and the carboxyl-terminal conserved !1region ending in a hydrophobic membrane-anchoring sequence. COMMENT There are 10 tandem copies of a 9-residue repeat (preceded !1by a 6-residue incomplete repeat) and 3 tandem copies of a !116-residue repeat (followed by 3 shorter, incomplete !1copies). CLASSIFICATION #superfamily circumsporozoite protein; thrombospondin type 1 !1repeat homology KEYWORDS sporozoite; surface antigen; tandem repeat FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-378 #product circumsporozoite protein #status predicted !8#label MAT\ !$97-192 #region 9-residue repeats\ !$193-268 #region 16-residue repeats\ !$303-356 #domain thrombospondin type 1 repeat homology #label !8THR1 SUMMARY #length 378 #molecular-weight 36150 #checksum 8251 SEQUENCE /// ENTRY OZZQAL #type complete TITLE circumsporozoite protein precursor - Plasmodium cynomolgi (strain London) ALTERNATE_NAMES major sporozoite surface antigen ORGANISM #formal_name Plasmodium cynomolgi DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 07-Nov-1997 ACCESSIONS A26255 REFERENCE A90889 !$#authors Galinski, M.R.; Arnot, D.E.; Cochrane, A.H.; Barnwell, J.W.; !1Nussenzweig, R.S.; Enea, V. !$#journal Cell (1987) 48:311-319 !$#title The circumsporozoite gene of the Plasmodium cynomolgi !1complex. !$#cross-references MUID:87102878; PMID:3802196 !$#accession A26255 !'##molecule_type DNA !'##residues 1-378 ##label GAL COMMENT There are three distinct regions in the mature !1circumsporozoite protein, the amino-terminal region, the !1middle repeat region, and the carboxyl-terminal conserved !1region ending in a hydrophobic membrane-anchoring sequence. COMMENT There are 19 tandem copies of a 6-residue repeat and 6 !1copies of an 11-residue repeat. CLASSIFICATION #superfamily circumsporozoite protein; thrombospondin type 1 !1repeat homology KEYWORDS sporozoite; surface antigen; tandem repeat FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-378 #product circumsporozoite protein #status predicted !8#label MAT\ !$98-211 #region 6-residue repeats\ !$212-277 #region 11-residue repeats\ !$303-356 #domain thrombospondin type 1 repeat homology #label !8THR1 SUMMARY #length 378 #molecular-weight 37424 #checksum 5084 SEQUENCE /// ENTRY OZZQAC #type complete TITLE circumsporozoite protein precursor - Plasmodium cynomolgi (strain Gombak) ALTERNATE_NAMES major sporozoite surface antigen ORGANISM #formal_name Plasmodium cynomolgi DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 07-Nov-1997 ACCESSIONS E26255 REFERENCE A90889 !$#authors Galinski, M.R.; Arnot, D.E.; Cochrane, A.H.; Barnwell, J.W.; !1Nussenzweig, R.S.; Enea, V. !$#journal Cell (1987) 48:311-319 !$#title The circumsporozoite gene of the Plasmodium cynomolgi !1complex. !$#cross-references MUID:87102878; PMID:3802196 !$#accession E26255 !'##molecule_type DNA !'##residues 1-401 ##label GAL COMMENT There are three distinct regions in the mature !1circumsporozoite protein, the amino-terminal region, the !1middle repeat region, and the carboxyl-terminal conserved !1region ending in a hydrophobic membrane-anchoring sequence. COMMENT There are 17 tandem copies of the 11-residue repeat D/ !1G-G-A-A-A-A-G-G-G-G-N. CLASSIFICATION #superfamily circumsporozoite protein; thrombospondin type 1 !1repeat homology KEYWORDS sporozoite; surface antigen; tandem repeat FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-401 #product circumsporozoite protein #status predicted !8#label MAT\ !$98-278 #region 11-residue repeats\ !$326-379 #domain thrombospondin type 1 repeat homology #label !8THR1 SUMMARY #length 401 #molecular-weight 36523 #checksum 2996 SEQUENCE /// ENTRY OZZQAM #type complete TITLE circumsporozoite protein precursor - Plasmodium cynomolgi (strain Mulligan/NIH) ALTERNATE_NAMES major sporozoite surface antigen ORGANISM #formal_name Plasmodium cynomolgi DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 07-Nov-1997 ACCESSIONS B26255 REFERENCE A90889 !$#authors Galinski, M.R.; Arnot, D.E.; Cochrane, A.H.; Barnwell, J.W.; !1Nussenzweig, R.S.; Enea, V. !$#journal Cell (1987) 48:311-319 !$#title The circumsporozoite gene of the Plasmodium cynomolgi !1complex. !$#cross-references MUID:87102878; PMID:3802196 !$#accession B26255 !'##molecule_type DNA !'##residues 1-419 ##label GAL COMMENT There are three distinct regions in the mature !1circumsporozoite protein, the amino-terminal region, the !1middle repeat region, and the carboxyl-terminal conserved !1region ending in a hydrophobic membrane-anchoring sequence. COMMENT There are 53 tandem copies of a 4-residue repeat. CLASSIFICATION #superfamily circumsporozoite protein; thrombospondin type 1 !1repeat homology KEYWORDS sporozoite; surface antigen; tandem repeat FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-419 #product circumsporozoite protein #status predicted !8#label MAT\ !$99-310 #region 4-residue repeats\ !$344-397 #domain thrombospondin type 1 repeat homology #label !8THR1 SUMMARY #length 419 #molecular-weight 38824 #checksum 3487 SEQUENCE /// ENTRY OZZQAS #type complete TITLE circumsporozoite protein precursor - Plasmodium cynomolgi (strain Ceylon) ALTERNATE_NAMES major sporozoite surface antigen ORGANISM #formal_name Plasmodium cynomolgi DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 07-Nov-1997 ACCESSIONS C26255 REFERENCE A90889 !$#authors Galinski, M.R.; Arnot, D.E.; Cochrane, A.H.; Barnwell, J.W.; !1Nussenzweig, R.S.; Enea, V. !$#journal Cell (1987) 48:311-319 !$#title The circumsporozoite gene of the Plasmodium cynomolgi !1complex. !$#cross-references MUID:87102878; PMID:3802196 !$#accession C26255 !'##molecule_type DNA !'##residues 1-398 ##label GAL COMMENT There are three distinct regions in the mature !1circumsporozoite protein, the amino-terminal region, the !1middle repeat region, and the carboxyl-terminal conserved !1region ending in a hydrophobic membrane-anchoring sequence. COMMENT There are 16 tandem copies of a 9-residue repeat and 3 !1copies of a 17-residue repeat. CLASSIFICATION #superfamily circumsporozoite protein; thrombospondin type 1 !1repeat homology KEYWORDS sporozoite; surface antigen; tandem repeat FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-398 #product circumsporozoite protein #status predicted !8#label MAT\ !$97-240 #region 9-residue repeats\ !$241-291 #region 17-residue repeats\ !$323-376 #domain thrombospondin type 1 repeat homology #label !8THR1 SUMMARY #length 398 #molecular-weight 37652 #checksum 11 SEQUENCE /// ENTRY S50820 #type complete TITLE surface protein type 51B - Paramecium tetraurelia ORGANISM #formal_name Paramecium tetraurelia DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 07-Dec-1999 ACCESSIONS S50820 REFERENCE S50820 !$#authors Scott, J.; Leeck, C.; Forney, J. !$#journal Nucleic Acids Res. (1994) 22:5079-5084 !$#title Analysis of the micronuclear B type surface protein gene in !1Paramecium tetraurelia. !$#cross-references MUID:95098630; PMID:7800503 !$#accession S50820 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-2395 ##label SCO !'##cross-references EMBL:U07603; NID:g467226; PIDN:AAA81947.1; !1PID:g467227 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1March 1994 GENETICS !$#genetic_code SGC5 !$#introns 472/3; 1310/3; 1821/3 CLASSIFICATION #superfamily G surface protein SUMMARY #length 2395 #molecular-weight 246430 #checksum 5587 SEQUENCE /// ENTRY SAZQK1 #type complete TITLE major merozoite surface antigen precursor - malaria parasite (Plasmodium falciparum) (strain K1/Thai) ORGANISM #formal_name Plasmodium falciparum DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 09-Jun-2000 ACCESSIONS A25120 REFERENCE A91030 !$#authors Mackay, M.; Goman, M.; Bone, N.; Hyde, J.E.; Scaife, J.; !1Certa, U.; Stunnenberg, H.; Bujard, H. !$#journal EMBO J. (1985) 4:3823-3829 !$#title Polymorphism of the precursor for the major surface antigens !1of Plasmodium falciparum merozoites: studies at the genetic !1level. !$#cross-references MUID:86136024; PMID:3004972 !$#accession A25120 !'##molecule_type DNA !'##residues 1-1631 ##label MAC COMMENT The merozoite stages of different strains have !1strain-specific surface antigens that are involved in !1strain-specific immunity. COMMENT P. falciparum has three stages: sporozoite, merozoite, and !1gametocyte. The merozoite stage can be recovered from the !1blood. CLASSIFICATION #superfamily major merozoite surface antigen KEYWORDS glycoprotein; merozoite; surface antigen; tandem repeat; !1transmembrane protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-1631 #product major merozoite surface antigen #status !8predicted #label MAT\ !$67-84 #region 3-residue repeats (S-G-T/P)\ !$1614-1631 #domain membrane anchor #status predicted #label MBN\ !$97,259,755,759,835, !$911,955,1049,1156, !$1165,1436,1563 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1631 #molecular-weight 187806 #checksum 2237 SEQUENCE /// ENTRY SAZQGM #type complete TITLE major merozoite surface antigen precursor - malaria parasite (Plasmodium falciparum) (strain CAMP/Malaysia) ALTERNATE_NAMES 195K glycoprotein ORGANISM #formal_name Plasmodium falciparum DATE 30-Sep-1987 #sequence_revision 31-Mar-1991 #text_change 09-Jun-2000 ACCESSIONS A23386; S06361 REFERENCE A23386 !$#authors Weber, J.L.; Leininger, W.M.; Lyon, J.A. !$#journal Nucleic Acids Res. (1986) 14:3311-3323 !$#title Variation in the gene encoding a major merozoite surface !1antigen of the human malaria parasite Plasmodium falciparum. !$#cross-references MUID:86205236; PMID:3517809 !$#accession A23386 !'##molecule_type DNA !'##residues 1-1104 ##label WEB1 !'##cross-references EMBL:X03831 REFERENCE S06361 !$#authors Weber, J.L.; Sim, B.K.L.; Lyon, J.A.; Wolff, R. !$#journal Nucleic Acids Res. (1988) 16:1206 !$#title Merozoite surface protein sequence from the Camp strain of !1the human malaria parasite Plasmodium falciparum. !$#cross-references MUID:88143999; PMID:3278296 !$#accession S06361 !'##molecule_type DNA !'##residues 1104-1726 ##label WEB2 !'##cross-references EMBL:X03831 COMMENT The merozoite stages of different strains have !1strain-specific surface antigens that are involved in !1strain-specific immunity. COMMENT P. falciparum has three stages: sporozoite, merozoite, and !1gametocyte. The merozoite stage can be recovered from the !1blood. CLASSIFICATION #superfamily major merozoite surface antigen KEYWORDS glycoprotein; merozoite; surface antigen; tandem repeat FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-1726 #product major merozoite surface antigen #status !8predicted #label MAT\ !$67-87,91-96, !$100-105,109-120 #region 3-residue repeats (S-G-T)\ !$757-765 #region 3-residue repeats (T-E-E)\ !$133,272,501,567, !$638,827,839,924, !$944,990,1016,1114, !$1221,1613,1658 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1726 #molecular-weight 196197 #checksum 4970 SEQUENCE /// ENTRY A25526 #type complete TITLE ring-infected erythrocyte surface antigen precursor - malaria parasite (Plasmodium falciparum) (strain FC27/Papua New Guinea) ORGANISM #formal_name Plasmodium falciparum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS A25526 REFERENCE A25526 !$#authors Favaloro, J.M.; Coppel, R.L.; Corcoran, L.M.; Foote, S.J.; !1Brown, G.V.; Anders, R.F.; Kemp, D.J. !$#journal Nucleic Acids Res. (1986) 14:8265-8277 !$#title Structure of the RESA gene of Plasmodium falciparum. !$#cross-references MUID:87066710; PMID:3537955 !$#accession A25526 !'##molecule_type DNA !'##residues 1-1073 ##label FAV GENETICS !$#gene RESA CLASSIFICATION #superfamily ring-infected erythrocyte surface antigen; dnaJ !1amino-terminal homology KEYWORDS surface antigen; tandem repeat FEATURE !$1-65 #domain signal sequence #status predicted #label SIG\ !$66-1073 #product ring-infected erythrocyte surface antigen !8#status predicted #label MAT\ !$523-587 #domain dnaJ amino-terminal homology #label DNJ\ !$891-1073 #region 4-residue repeats SUMMARY #length 1073 #molecular-weight 124906 #checksum 6757 SEQUENCE /// ENTRY A45614 #type complete TITLE merozoite surface antigen p58 - Babesia bigemina ORGANISM #formal_name Babesia bigemina DATE 22-Apr-1993 #sequence_revision 02-Jun-1994 #text_change 16-Jul-1999 ACCESSIONS A45614; A45561; S27775 REFERENCE A45614 !$#authors Mishra, V.S.; Stephens, E.B.; Dame, J.B.; Perryman, L.E.; !1McGuire, T.C.; McElwain, T.F. !$#journal Mol. Biochem. Parasitol. (1991) 47:207-212 !$#title Immunogenicity and sequence analysis of recombinant p58: a !1neutralization-sensitive, antigenically conserved Babesia !1bigemina merozoite surface protein. !$#cross-references MUID:92049553; PMID:1944417 !$#accession A45614 !'##molecule_type DNA !'##residues 1-480 ##label MIS1 !'##cross-references EMBL:M60878; NID:g155860; PIDN:AAA65583.1; !1PID:g155861 !'##experimental_source merozoite !'##note sequence extracted from NCBI backbone (NCBIN:65037, !1NCBIP:65038) REFERENCE A45561 !$#authors Mishra, V.S.; McElwain, T.F.; Dame, J.B.; Stephens, E.B. !$#journal Mol. Biochem. Parasitol. (1992) 53:149-158 !$#title Isolation, sequence and differential expression of the p58 !1gene family of Babesia bigemina. !$#cross-references MUID:92365724; PMID:1501634 !$#accession A45561 !'##molecule_type DNA !'##residues 1-281,'G',283-480 ##label MIS2 !'##note sequence extracted from NCBI backbone (NCBIN:111161, !1NCBIP:111164) GENETICS !$#gene p58 CLASSIFICATION #superfamily merozoite surface antigen p58 KEYWORDS surface antigen SUMMARY #length 480 #molecular-weight 53794 #checksum 7442 SEQUENCE /// ENTRY YAZQN7 #type complete TITLE S-antigen precursor - malaria parasite (Plasmodium falciparum) (strain NF7/Ghana) ORGANISM #formal_name Plasmodium falciparum DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 09-Jun-2000 ACCESSIONS B22011 REFERENCE A90863 !$#authors Cowman, A.F.; Saint, R.B.; Coppel, R.L.; Brown, G.V.; !1Anders, R.F.; Kemp, D.J. !$#journal Cell (1985) 40:775-783 !$#title Conserved sequences flank variable tandem repeats in two !1S-antigen gnes of Plasmodium falciparum. !$#cross-references MUID:85176931; PMID:3886159 !$#accession B22011 !'##molecule_type DNA !'##residues 1-309 ##label COW !'##cross-references GB:M10130; NID:g160670; PIDN:AAA29758.1; !1PID:g160671 !'##experimental_source clone NF7.S !'##note the intact NF7 S-antigen contains about 35 more of the !18-residue repeats COMMENT The S-antigen is secreted by the parasite. CLASSIFICATION #superfamily plasmodium S-antigen KEYWORDS malaria; surface antigen; tandem repeat FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-309 #product S-antigen #status predicted #label MAT\ !$97-256 #region 8-residue repeats (S-D-E-A-E-A-L/R-K)\ !$257-271,272-286 #region 15-residue repeats SUMMARY #length 309 #molecular-weight 33694 #checksum 473 SEQUENCE /// ENTRY YAZQF7 #type complete TITLE S-antigen precursor - malaria parasite (Plasmodium falciparum) (strain FC27/Papua New Guinea) ORGANISM #formal_name Plasmodium falciparum DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 09-Jun-2000 ACCESSIONS A22011 REFERENCE A90863 !$#authors Cowman, A.F.; Saint, R.B.; Coppel, R.L.; Brown, G.V.; !1Anders, R.F.; Kemp, D.J. !$#journal Cell (1985) 40:775-783 !$#title Conserved sequences flank variable tandem repeats in two !1S-antigen gnes of Plasmodium falciparum. !$#cross-references MUID:85176931; PMID:3886159 !$#accession A22011 !'##molecule_type DNA !'##residues 1-265 ##label COW !'##cross-references GB:M10129; NID:g160668; PIDN:AAA29757.1; !1PID:g160669 !'##experimental_source clone FC27.4.S !'##note the native FC27 S-antigen contains about 100 more of the !111-residue repeats COMMENT The S-antigen is secreted by the parasite. CLASSIFICATION #superfamily plasmodium S-antigen KEYWORDS malaria; surface antigen; tandem repeat FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-265 #product S-antigen #status predicted #label MAT\ !$96-238 #region 11-residue repeats (D-P-A-K-A-S-Q-G-G-L-E) SUMMARY #length 265 #molecular-weight 27934 #checksum 2893 SEQUENCE /// ENTRY YAZQ51 #type complete TITLE antigen 5.1 precursor - malaria parasite (Plasmodium falciparum) ORGANISM #formal_name Plasmodium falciparum DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 09-Jun-2000 ACCESSIONS A23052 REFERENCE A23052 !$#authors Hope, I.A.; Mackay, M.; Hyde, J.E.; Goman, M.; Scaife, J. !$#journal Nucleic Acids Res. (1985) 13:369-379 !$#title The gene for an exported antigen of the malaria parasite !1Plasmodium falciparum cloned and expressed in Escherichia !1coli. !$#cross-references MUID:85215483; PMID:2582354 !$#accession A23052 !'##molecule_type mRNA !'##residues 1-162 ##label HOP !'##cross-references GB:X01745; NID:g9858; PIDN:CAA25881.1; PID:g758218 COMMENT This antigen may be secreted by the intraerythrocyte stage !1into the cytoplasm of the host cell or may be trapped in the !1parasite membrane if the hydrophobic region (76-101) !1prevents the entire protein from being secreted. COMMENT This antigen and the circumsporozoite protein appear to have !1a common epitope. CLASSIFICATION #superfamily plasmodium S-antigen KEYWORDS sporozoite; surface antigen; transmembrane protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-162 #product antigen 5.1 #status predicted #label MAT\ !$76-101 #domain transmembrane #status predicted #label TMM SUMMARY #length 162 #molecular-weight 17422 #checksum 1672 SEQUENCE /// ENTRY YAZQ31 #type fragment TITLE 300K antigen Ag231 - malaria parasite (Plasmodium falciparum) (strain FCQ27/Papua New Guinea) (fragment) ALTERNATE_NAMES FIRA ORGANISM #formal_name Plasmodium falciparum DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 09-Jun-2000 ACCESSIONS A21890 REFERENCE A21890 !$#authors Stahl, H.D.; Crewther, P.E.; Anders, R.F.; Brown, G.V.; !1Coppel, R.L.; Bianco, A.E.; Mitchell, G.F.; Kemp, D.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:543-547 !$#title Interspersed blocks of repetitive and charged amino acids in !1a dominant immunogen of Plasmodium falciparum. !$#cross-references MUID:85113233; PMID:3881769 !$#accession A21890 !'##molecule_type mRNA !'##residues 1-310 ##label STA !'##cross-references GB:M10236; NID:g160058; PIDN:AAA29468.1; !1PID:g552169 COMMENT There are three distinct regions of repeats. The first !1region is four 6-residue repeats, the second is thirteen !16-residue repeats, and the third is thirteen 6-residue !1repeats. CLASSIFICATION #superfamily plasmodium S-antigen KEYWORDS merozoite; surface antigen; tandem repeat; trophozoite FEATURE !$1-23 #region 6-residue repeats (V-T-G-S-C-V)\ !$29-106 #region 6-residue repeats (V-T-T/I-Q/E-E-P)\ !$107-152,266-310 #region 45-residue repeats\ !$188-265 #region 6-residue repeats SUMMARY #length 310 #checksum 4807 SEQUENCE /// ENTRY A58938 #type complete TITLE surface protein rhoptry ROP1 precursor - Toxoplasma gondii ORGANISM #formal_name Toxoplasma gondii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A58938; A45644; S37697 REFERENCE A58938 !$#authors Boothroyd, J.C. !$#submission submitted to GenBank, July 1995 !$#accession A58938 !'##status preliminary !'##molecule_type mRNA !'##residues 1-396 ##label BOO !'##cross-references GB:M71274; NID:g897822; PIDN:AAA69859.1; !1PID:g897823 !'##note revision to sequence reported in A45644 REFERENCE A45644 !$#authors Ossorio, P.N.; Schwartzman, J.D.; Boothroyd, J.C. !$#journal Mol. Biochem. Parasitol. (1992) 50:1-15 !$#title A Toxoplasma gondii rhoptry protein associated with host !1cell penetration has unusual charge asymmetry. !$#cross-references MUID:92178277; PMID:1542304 !$#accession A45644 !'##molecule_type mRNA !'##residues 'MACRQLLCSVQNLLFFFLRDIYCTDFDT',1-352,'FPQR',358-364,'R', !1366,'I',393,'SP',396, !1'AAELMARRAGPYWAKEESRMMDRNNTGSMLLDSAKTTVSRKRGSGVLRS' ##label !1OSS !'##cross-references EMBL:M71274; NID:g897822 !'##note sequence extracted from NCBI backbone (NCBIN:85178, !1NCBIP:85179) CLASSIFICATION #superfamily surface protein rhoptry KEYWORDS surface antigen FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-396 #product surface protein rhoptry #status predicted !8#label MAT SUMMARY #length 396 #molecular-weight 42670 #checksum 2217 SEQUENCE /// ENTRY S06839 #type complete TITLE surface antigen spaP precursor - Streptococcus mutans ALTERNATE_NAMES antigen I/II ORGANISM #formal_name Streptococcus mutans DATE 03-Mar-1994 #sequence_revision 03-Mar-1994 #text_change 16-Jul-1999 ACCESSIONS S06839; A60339; A60661 REFERENCE S06839 !$#authors Kelly, C.; Evans, P.; Bergmeier, L.; Lee, S.F.; !1Progulske-Fox, A.; Harris, A.C.; Aitken, A.; Bleiweis, A.S.; !1Lehner, T. !$#journal FEBS Lett. (1989) 258:127-132 !$#title Sequence analysis of the cloned streptococcal cell surface !1antigen I/II. !$#cross-references MUID:90076473; PMID:2687020 !$#accession S06839 !'##molecule_type DNA !'##residues 1-1561 ##label KEL !'##cross-references EMBL:X17390; NID:g47266; PIDN:CAA35253.1; !1PID:g47267 !'##experimental_source serotype c !'##note parts of this sequence, including the amino ends of the mature !1proteins, were confirmed by amino acid sequencing REFERENCE A60661 !$#authors Kelly, C.; Evans, P.; Ma, J.K.C.; Bergmeier, L.A.; Taylor, !1W.; Brady, L.J.; Lee, S.F.; Bleiweis, A.S.; Lehner, T. !$#journal Arch. Oral Biol. (1990) 35(Suppl.):33S-38S !$#title Sequencing and characterization of the 185 kDa cell surface !1antigen of Streptococcus mutans. !$#cross-references MUID:91207143; PMID:1982405 !$#contents annotation REFERENCE A60339 !$#authors Ma, J.K.C.; Kelly, C.G.; Munro, G.; Whiley, R.A.; Lehner, T. !$#journal Infect. Immun. (1991) 59:2686-2694 !$#title Conservation of the gene encoding streptococcal antigen I/II !1in oral streptococci. !$#cross-references MUID:91310321; PMID:1855988 !$#accession A60339 !'##status preliminary !'##molecule_type DNA !'##residues 1084-1189 ##label MAA GENETICS !$#gene spaP FUNCTION !$#description probably plays a role in adherence to the tooth surface. CLASSIFICATION #superfamily surface antigen spaP KEYWORDS duplication; glycoprotein; transmembrane protein FEATURE !$1-38 #domain signal sequence #status predicted #label SIG\ !$39-1561 #product surface antigen spaP.I #status predicted !8#label MAT1\ !$169-193 #domain spaP alanine-rich repeat #label AR1\ !$194-218 #domain spaP alanine-rich repeat #label AR2\ !$219-243 #domain spaP alanine-rich repeat #label AR3\ !$244-268 #domain spaP alanine-rich repeat #label AR4\ !$276-300 #domain spaP alanine-rich repeat #label AR5\ !$301-325 #domain spaP alanine-rich repeat #label AR6\ !$326-350 #domain spaP alanine-rich repeat #label AR7\ !$358-382 #domain spaP alanine-rich repeat #label AR8\ !$383-407 #domain spaP alanine-rich repeat #label AR9\ !$408-426 #domain spaP alanine-rich repeat #label AR10\ !$440-464 #domain spaP alanine-rich repeat #label AR11\ !$847-885 #domain spaP proline-rich repeat #label PR1\ !$886-924 #domain spaP proline-rich repeat #label PR2\ !$925-963 #domain spaP proline-rich repeat #label PR3\ !$997-1561 #product surface antigen spaP.II #status predicted !8#label MAT2 SUMMARY #length 1561 #molecular-weight 170059 #checksum 5218 SEQUENCE /// ENTRY KGZQHF #type complete TITLE histidine/alanine-rich protein - malaria parasite (Plasmodium falciparum) ALTERNATE_NAMES antigen 57 ORGANISM #formal_name Plasmodium falciparum DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 09-Jun-2000 ACCESSIONS A24117 REFERENCE A24117 !$#authors Stahl, H.D.; Kemp, D.J.; Crewther, P.E.; Scanlon, D.B.; !1Woodrow, G.; Brown, G.V.; Bianco, A.E.; Anders, R.F.; !1Coppel, R.L. !$#journal Nucleic Acids Res. (1985) 13:7837-7846 !$#title Sequence of a cDNA encoding a small polymorphic histidine- !1and alanine-rich protein from Plasmodium falciparum. !$#cross-references MUID:86067201; PMID:2415925 !$#accession A24117 !'##molecule_type mRNA !'##residues 1-221 ##label STA !'##cross-references GB:X03144; NID:g9970; PIDN:CAA26916.1; PID:g9971 !'##experimental_source strain Papua New Guinea COMMENT There are 3 copies of 3-residue repeats, 13 copies of !16-residue repeats, and 7 copies of 5-residue repeats in this !1small, polymorphic protein. CLASSIFICATION #superfamily plasmodium histidine-rich protein KEYWORDS tandem repeat; trophozoite FEATURE !$57-59,60-62,66-68 #region 3-residue repeats (A-H-H)\ !$69-146 #region 6-residue repeats (A-H-H-A-A-N)\ !$176-210 #region 5-residue repeats (H-H-D-D/G-A) SUMMARY #length 221 #molecular-weight 23580 #checksum 7326 SEQUENCE /// ENTRY KGZQHL #type complete TITLE histidine-rich glycoprotein precursor - Plasmodium lophurae ORGANISM #formal_name Plasmodium lophurae DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Jul-1999 ACCESSIONS A22692 REFERENCE A22692 !$#authors Ravetch, J.V.; Feder, R.; Pavlovec, A.; Blobel, G. !$#journal Nature (1984) 312:616-620 !$#title Primary structure and genomic organization of the !1histidine-rich protein of the malaria parasite Plasmodium !1lophurae. !$#cross-references MUID:85061618; PMID:6095114 !$#accession A22692 !'##molecule_type DNA !'##residues 1-351 ##label RAV !'##cross-references GB:X01469; NID:g9997; PIDN:CAA25698.1; PID:g9999 COMMENT There are two copies of 16-residue repeats, two copies of !117-residue repeats, two copies of 15-residue repeats, and 17 !1copies of 10-residue repeats (plus one lacking the tenth !1His). GENETICS !$#introns 23/3 CLASSIFICATION #superfamily plasmodium histidine-rich protein KEYWORDS glycoprotein; tandem repeat FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-47 #domain propeptide #status predicted #label PRO\ !$48-351 #product histidine-rich glycoprotein #status !8predicted #label MAT\ !$59-74,75-90 #region 16-residue repeats\ !$91-107,108-123 #region 17-residue repeats\ !$124-138,139-153 #region 15-residue repeats\ !$173-301,312-331 #region 10-residue repeats\ !$40 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 351 #molecular-weight 44032 #checksum 5469 SEQUENCE /// ENTRY A31429 #type complete TITLE hisactophilin [validated] - slime mold (Dictyostelium discoideum) ALTERNATE_NAMES histidine-rich actin-binding protein ORGANISM #formal_name Dictyostelium discoideum DATE 31-Jul-1989 #sequence_revision 02-Aug-1994 #text_change 15-Sep-2000 ACCESSIONS A31429; A30787 REFERENCE A31429 !$#authors Scheel, J.; Ziegelbauer, K.; Kupke, T.; Humbel, B.M.; !1Noegel, A.A.; Gerisch, G.; Schleicher, M. !$#journal J. Biol. Chem. (1989) 264:2832-2839 !$#title Hisactophilin, a histidine-rich actin-binding protein from !1Dictyostelium discoideum. !$#cross-references MUID:89123382; PMID:2914932 !$#accession A31429 !'##molecule_type mRNA !'##residues 1-118 ##label SCH !'##cross-references GB:J04472; NID:g167812; PIDN:AAA33218.1; !1PID:g167813 REFERENCE A52585 !$#authors Habazettl, J.; Gondol, D.; Wiltscheck, R.; Otlewski, J.; !1Schleicher, M.; Holak, T.A. !$#submission submitted to the Brookhaven Protein Data Bank, May 1994 !$#cross-references PDB:1HCD !$#contents annotation; conformation by (1)H-, (13)C-, and (15)N-NMR, !1residues 1-118 !$#note recombinant form expressed in Escherichia coli includes !1Met-1 and lacks post-translational modifications of the !1mature protein REFERENCE A59170 !$#authors Habazettl, J.; Gondol, D.; Wiltscheck, R.; Otlewski, J.; !1Schleicher, M.; Holak, T.A. !$#journal Nature (1992) 359:855-858 !$#title Structure of hisactophilin is similar to interleukin-1beta !1and fibroblast growth factor. !$#cross-references MUID:93063300; PMID:1436061 !$#contents annotation; conformation by (1)H-, (13)C-, and (15)N-NMR REFERENCE A59169 !$#authors Hanakam, F.; Gerisch, G.; Lotz, S.; Alt, T.; Seelig, A. !$#journal Biochemistry (1996) 35:11036-11044 !$#title Binding of hisactophilin I and II to lipid membranes is !1controlled by a pH-dependent myristoyl-histidine switch. !$#cross-references MUID:96374214; PMID:8780505 !$#contents annotation REFERENCE A59171 !$#authors Hanakam, F.; Eckerskorn, C.; Lottspeich, F.; !1Mueller-Taubenberger, A.; Schaefer, W.; Gerisch, G. !$#journal J. Biol. Chem. (1995) 270:596-602 !$#title The pH-sensitive actin-binding protein hisactophilin of !1Dictyostelium exists in two isoforms which both are !1myristoylated and distributed between plasma membrane and !1cytoplasm. !$#cross-references MUID:95122497; PMID:7822284 !$#contents annotation REFERENCE A38915 !$#authors Urban, M.; Gerisch, G. !$#citation unpublished results, cited by Schleicher, M., in Guidebook !1to the Cytoskeletal and Motor Proteins, Kreis. T. and Vale, !1R., eds., pp.54-55, Oxford University Press, Oxford, 1993 !$#contents annotation; palmitate binding !$#note one or more of the serines is phosphorylated COMMENT Hisactophilin binds to F-actin in a pH-dependent manner, !1inducing actin polymerization. It is suggested to act as an !1intracellular pH sensor that links chemotactic signals to !1responses in the microfilament system. CLASSIFICATION #superfamily hisactophilin KEYWORDS actin binding; blocked amino end; duplication; lipoprotein; !1myristylation; tandem repeat; thiolester bond FEATURE !$2-118 #product hisactophilin #status experimental #label !8MAT\ !$34-86 #region 13-residue repeats !8(F-H-V-E-N-H-G-G-K-V-A-L-K)\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status experimental\ !$3 #modified_site aspartic acid (Asn) #status predicted\ !$49 #binding_site palmitate (Cys) (covalent) (partial) !8#status experimental SUMMARY #length 118 #molecular-weight 13456 #checksum 6737 SEQUENCE /// ENTRY A36614 #type complete TITLE actobindin - Acanthamoeba castellanii ORGANISM #formal_name Acanthamoeba castellanii DATE 28-Mar-1991 #sequence_revision 05-Apr-1995 #text_change 06-Sep-1996 ACCESSIONS A36614 REFERENCE A36614 !$#authors Vandekerckhove, J.; Van Damme, J.; Vancompernolle, K.; Bubb, !1M.R.; Lambooy, P.K.; Korn, E.D. !$#journal J. Biol. Chem. (1990) 265:12801-12805 !$#title The covalent structure of Acanthamoeba actobindin. !$#cross-references MUID:90330610; PMID:2376577 !$#accession A36614 !'##molecule_type protein !'##residues 1-88 ##label VAN REFERENCE A39422 !$#authors Vancompernolle, K.; Vandekerckhove, J.; Bubb, M.R.; Korn, !1E.D. !$#journal J. Biol. Chem. (1991) 266:15427-15431 !$#title The interfaces of actin and Acanthamoeba actobindin. !1Identification of a new actin-binding motif. !$#cross-references MUID:91332070; PMID:1869561 !$#contents annotation !$#note Lys-16 and Lys-52 were identified by chemical cross-linking !1to actin as residues within actin-binding regions COMMENT This protein can bind two actin monomers. CLASSIFICATION #superfamily actobindin KEYWORDS acetylated amino end; actin binding; duplication; methylated !1amino acid; monomer FEATURE !$15-47 #domain actobindin repeat #label AB1\ !$15-20 #region actin binding #status experimental\ !$51-84 #domain actobindin repeat #label AB2\ !$51-56 #region actin binding #status experimental\ !$1 #modified_site acetylated amino end (Met) #status !8experimental\ !$35,72 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental SUMMARY #length 88 #molecular-weight 9554 #checksum 1595 SEQUENCE /// ENTRY ZOZQMF #type fragment TITLE glycophorin-binding protein, merozoite - Plasmodium falciparum (fragment) ORGANISM #formal_name Plasmodium falciparum DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 16-Jul-1999 ACCESSIONS A03390 REFERENCE A03390 !$#authors Ravetch, J.V.; Kochan, J.; Perkins, M. !$#journal Science (1985) 227:1593-1597 !$#title Isolation of the gene for a glycophorin-binding protein !1implicated in erythrocyte invasion by a malaria parasite. !$#cross-references MUID:85142172; PMID:3883491 !$#accession A03390 !'##molecule_type mRNA !'##residues 1-219 ##label RAV !'##cross-references GB:M10985; NID:g160302; PIDN:AAA29607.1; !1PID:g160303 COMMENT The mRNA for this protein was isolated from the merozoite !1stage. COMMENT There are four copies of a 50-residue repeating unit. COMMENT P. falciparum undergoes three cycles of development in its !1vertebrate host: the hepatic cyle; the asexual blood cycle, !1which includes the extracellular merozoite and the !1intraerythrocytic schizont; and the sexual gametocyte cycle. !1It elicits stage-specific immune responses. CLASSIFICATION #superfamily glycophorin-binding protein KEYWORDS duplication FEATURE !$20-69,70-119, !$120-169,170-219 #region duplication SUMMARY #length 219 #checksum 2456 SEQUENCE /// ENTRY VMUT1B #type complete TITLE variant surface glycoprotein AnTat 1.1 precursor - Trypanosoma brucei brucei ORGANISM #formal_name Trypanosoma brucei brucei DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 28-Jan-2000 ACCESSIONS S07174; S18522; S09253; S10844 REFERENCE S07174 !$#authors Michiels, F.; Matthyssens, G.; Kronenberger, P.; Pays, E.; !1Dero, B.; van Assel, S.; Darville, M.; Cravador, A.; !1Steinert, M.; Hamers, R. !$#journal EMBO J. (1983) 2:1185-1192 !$#title Gene activation and re-expression of a Trypanosoma brucei !1variant surface glycoprotein. !$#cross-references MUID:84028590; PMID:6313354 !$#accession S07174 !'##molecule_type DNA !'##residues 1-503 ##label MIC !'##cross-references EMBL:X01843; NID:g10429; PIDN:CAA25971.1; !1PID:g10430 !$#accession S18522 !'##molecule_type mRNA !'##residues 1-503 ##label MIC2 !'##cross-references GB:X01843; NID:g10429; PIDN:CAA25971.1; PID:g10430 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE S09252 !$#authors van der Werf, A.; van Assel, S.; Aerts, D.; Steinert, M.; !1Pays, E. !$#journal EMBO J. (1990) 9:1035-1040 !$#title Telomere interactions may condition the programming of !1antigen expression in Trypanosoma brucei. !$#cross-references MUID:90214610; PMID:2323332 !$#accession S09253 !'##status translation not shown !'##molecule_type DNA !'##residues 1-333,'P',335-345,'V',347-416 ##label VAN !'##cross-references EMBL:X15817; NID:g10381; PIDN:CAA33809.1; !1PID:g10382 REFERENCE A17609 !$#authors Matthyssens, G.; Michiels, F.; Hamers, R.; Pays, E.; !1Steinert, M. !$#journal Nature (1981) 293:230-233 !$#title Two variant surface glycoproteins of Trypanosoma brucei have !1a conserved C-terminus. !$#cross-references MUID:82013622; PMID:7278981 !$#accession S10844 !'##molecule_type mRNA !'##residues 391-418,'K',420-503 ##label MATH !'##cross-references EMBL:J01213; NID:g162361; PIDN:AAA30280.1; !1PID:g162362 !'##note the authors translated the codon AAG for residue 419 as Asn and !1TTC for residue 503 as Leu CLASSIFICATION #superfamily variant surface glycoprotein KEYWORDS blocked carboxyl end; glycoprotein; lipoprotein; membrane !1protein; phosphatidylinositol linkage; phosphoprotein FEATURE !$1-30 #domain signal sequence #status predicted #label SIG\ !$31-480 #product variant surface glycoprotein AnTat 1.1 !8#status experimental #label MAT\ !$481-503 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$113,419,432 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$480 #modified_site GPI-anchor ethanolamine amidated !8carboxyl end (Asp) (in mature form) #status predicted SUMMARY #length 503 #molecular-weight 52814 #checksum 5761 SEQUENCE /// ENTRY VMUT8B #type complete TITLE variant surface glycoprotein 117 precursor - Trypanosoma brucei ALTERNATE_NAMES VSG ORGANISM #formal_name Trypanosoma brucei DATE 29-Jun-1981 #sequence_revision 28-May-1986 #text_change 28-Jan-2000 ACCESSIONS A92883; A45908; B17609; A92882; A03391 REFERENCE A92883 !$#authors Boothroyd, J.C.; Paynter, C.A.; Coleman, S.L.; Cross, G.A.M. !$#journal J. Mol. Biol. (1982) 157:547-556 !$#title Complete nucleotide sequence of complementary DNA coding for !1a variant surface glycoprotein from Trypanosoma brucei. !$#cross-references MUID:83010278; PMID:7120401 !$#accession A92883 !'##molecule_type mRNA !'##residues 1-526 ##label BOO !'##cross-references GB:V01387; NID:g10416; PIDN:CAA24677.1; PID:g10417 REFERENCE A45908 !$#authors Boothroyd, J.C.; Paynter, C.A.; Cross, G.A.M.; Bernards, A.; !1Borst, P. !$#journal Nucleic Acids Res. (1981) 9:4735-4743 !$#title Variant surface glycoproteins of Trypanosoma brucei are !1synthesised with cleavable hydrophobic sequences at the !1carboxy and amino termini. !$#cross-references MUID:82059496; PMID:6272213 !$#accession A45908 !'##molecule_type mRNA !'##residues 1-53 ##label BO2 !'##cross-references GB:J01214; NID:g162389; PIDN:AAA30290.1; !1PID:g162392 !'##note the modification to residue 503-Asp was described as !1glycosylation but is now recognized as a !1glycosylphosphatidylinositol (GPI) anchor REFERENCE A17609 !$#authors Matthyssens, G.; Michiels, F.; Hamers, R.; Pays, E.; !1Steinert, M. !$#journal Nature (1981) 293:230-233 !$#title Two variant surface glycoproteins of Trypanosoma brucei have !1a conserved C-terminus. !$#cross-references MUID:82013622; PMID:7278981 !$#accession B17609 !'##molecule_type mRNA !'##residues 412-526 ##label MAT REFERENCE A92882 !$#authors Allen, G.; Gurnett, L.P.; Cross, G.A.M. !$#journal J. Mol. Biol. (1982) 157:527-546 !$#title Complete amino acid sequence of a variant surface !1glycoprotein (VSG 117) from Trypanosoma brucei. !$#cross-references MUID:83010277; PMID:7120400 !$#accession A92882 !'##molecule_type protein !'##residues 34-503 ##label ALL COMMENT All cysteine residues except Cys-277 form disulfide bonds. CLASSIFICATION #superfamily variant surface glycoprotein KEYWORDS blocked carboxyl end; glycoprotein; lipoprotein; !1phosphatidylinositol linkage; phosphoprotein FEATURE !$1-33 #domain signal sequence #status predicted #label SIG\ !$34-503 #product variant surface glycoprotein 117 #status !8experimental #label VSG\ !$504-526 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$453 #binding_site carbohydrate (Asn) (covalent) #status !8experimental\ !$503 #modified_site GPI-anchor ethanolamine amidated !8carboxyl end (Asp) (in mature form) #status !8experimental SUMMARY #length 526 #molecular-weight 56317 #checksum 6346 SEQUENCE /// ENTRY VMUT4R #type fragment TITLE variant surface glycoprotein 4 precursor - Trypanosoma brucei rhodesiense (fragment) ALTERNATE_NAMES metacyclic variable antigen; VSG ORGANISM #formal_name Trypanosoma brucei rhodesiense DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 28-Jan-2000 ACCESSIONS A03392 REFERENCE A94011 !$#authors Lenardo, M.J.; Rice-Ficht, A.C.; Kelly, G.; Esser, K.M.; !1Donelson, J.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:6642-6646 !$#title Characterization of the genes specifying two metacyclic !1variable antigen types in Trypanosoma brucei rhodesiense. !$#cross-references MUID:85038570; PMID:6593722 !$#accession A03392 !'##molecule_type mRNA !'##residues 1-476 ##label LEN COMMENT VSGs expressed during metacyclic and bloodstream stages of !1the trypanosome life cycle appear to share certain sequence !1characteristics: amino-terminal heterogeneity, !1carboxyl-terminal homogeneity, hydrophobic tails, and !1potential glycosylation sites. CLASSIFICATION #superfamily variant surface glycoprotein KEYWORDS blocked carboxyl end; glycoprotein; lipoprotein; !1phosphatidylinositol linkage; phosphoprotein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-457 #product variant surface glycoprotein 4 #status !8predicted #label MAT\ !$458-476 #domain carboxyl-terminal propeptide (fragment) !8#status predicted #label CTP\ !$38-160,144-203 #disulfide_bonds #status predicted\ !$356 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$457 #modified_site GPI-anchor ethanolamine amidated !8carboxyl end (Asp) (in mature form) #status predicted SUMMARY #length 476 #checksum 376 SEQUENCE /// ENTRY VMUT7R #type fragments TITLE variant surface glycoprotein 7 precursor - Trypanosoma brucei rhodesiense (fragments) ALTERNATE_NAMES metacyclic variable antigen; VSG ORGANISM #formal_name Trypanosoma brucei rhodesiense DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 17-Nov-2000 ACCESSIONS A03393 REFERENCE A94011 !$#authors Lenardo, M.J.; Rice-Ficht, A.C.; Kelly, G.; Esser, K.M.; !1Donelson, J.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:6642-6646 !$#title Characterization of the genes specifying two metacyclic !1variable antigen types in Trypanosoma brucei rhodesiense. !$#cross-references MUID:85038570; PMID:6593722 !$#accession A03393 !'##molecule_type mRNA !'##residues 1-467 ##label LEN CLASSIFICATION #superfamily variant surface glycoprotein KEYWORDS blocked carboxyl end; glycoprotein; lipoprotein; !1phosphatidylinositol linkage; phosphoprotein FEATURE !$1-27 #domain signal sequence (fragment) #status predicted !8#label SIG\ !$28-444 #product variant surface glycoprotein 7 (fragment) !8#status predicted #label MAT\ !$445-467 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$108,252,416 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$444 #modified_site GPI-anchor ethanolamine amidated !8carboxyl end (Asp) (in mature form) #status predicted SUMMARY #length 467 #checksum 7279 SEQUENCE /// ENTRY A45596 #type complete TITLE trypomastigote-specific surface antigen precursor - Trypanosoma cruzi ORGANISM #formal_name Trypanosoma cruzi DATE 22-Apr-1993 #sequence_revision 02-Jun-1994 #text_change 16-Jul-1999 ACCESSIONS A45596; S27857 REFERENCE A45596 !$#authors Fouts, D.L.; Ruef, B.J.; Ridley, P.T.; Wrightsman, R.A.; !1Peterson, D.S.; Manning, J.E. !$#journal Mol. Biochem. Parasitol. (1991) 46:189-200 !$#title Nucleotide sequence and transcription of a trypomastigote !1surface antigen gene of Trypanosoma cruzi. !$#cross-references MUID:92018016; PMID:1717846 !$#accession A45596 !'##molecule_type DNA !'##residues 1-835 ##label FOU !'##cross-references EMBL:M58466; NID:g162314; PIDN:AAA30259.1; !1PID:g162315 !'##experimental_source strain Peru !'##note sequence extracted from NCBI backbone (NCBIN:61039, !1NCBIP:61041) GENETICS !$#gene TSA-1 CLASSIFICATION #superfamily trypomastigote-specific surface antigen KEYWORDS surface antigen FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-835 #product trypomastigote-specific surface antigen !8#status predicted #label MAT SUMMARY #length 835 #molecular-weight 90436 #checksum 6434 SEQUENCE /// ENTRY VMUT17 #type complete TITLE VSG expression site-associated protein 117a precursor - Trypanosoma brucei ALTERNATE_NAMES ESAG protein ORGANISM #formal_name Trypanosoma brucei DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 16-Jul-1999 ACCESSIONS A03394 REFERENCE A90868 !$#authors Cully, D.F.; Ip, H.S.; Cross, G.A.M. !$#journal Cell (1985) 42:173-182 !$#title Coordinate transcription of variant surface glycoprotein !1genes and an expression site associated gene family in !1Trypanosoma brucei. !$#cross-references MUID:85254917; PMID:2861910 !$#accession A03394 !'##molecule_type mRNA !'##residues 1-325 ##label CUL !'##cross-references GB:M11451; NID:g162070; PIDN:AAA30190.1; !1PID:g162071 COMMENT The function of the ESAG proteins is not known but may be !1related to activation of the variant surface glycoprotein !1genes. CLASSIFICATION #superfamily VSG expression-site associated protein KEYWORDS glycoprotein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-325 #product VSG expression site-associated protein 117a !8#status predicted #label MAT\ !$72,290,313 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 325 #molecular-weight 35992 #checksum 6689 SEQUENCE /// ENTRY VMUT21 #type complete TITLE VSG expression site-associated protein 221a precursor - Trypanosoma brucei ALTERNATE_NAMES ESAG protein ORGANISM #formal_name Trypanosoma brucei DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 16-Jul-1999 ACCESSIONS A03395 REFERENCE A90868 !$#authors Cully, D.F.; Ip, H.S.; Cross, G.A.M. !$#journal Cell (1985) 42:173-182 !$#title Coordinate transcription of variant surface glycoprotein !1genes and an expression site associated gene family in !1Trypanosoma brucei. !$#cross-references MUID:85254917; PMID:2861910 !$#accession A03395 !'##molecule_type mRNA !'##residues 1-329 ##label CUL !'##cross-references GB:M11452; NID:g162072; PIDN:AAA30191.1; !1PID:g162073 COMMENT The function of the ESAG proteins is not known but may be !1related to activation of the variant surface glycoprotein !1genes. CLASSIFICATION #superfamily VSG expression-site associated protein KEYWORDS glycoprotein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-329 #product VSG expression site-associated protein 221a !8#status predicted #label MAT\ !$73,294,308 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 329 #molecular-weight 36603 #checksum 7855 SEQUENCE /// ENTRY MKUT5B #type complete TITLE kinetoplast minicircle 51 polypeptide - Trypanosoma brucei mitochondrion ORGANISM #formal_name mitochondrion Trypanosoma brucei DATE 31-Dec-1980 #sequence_revision 31-Dec-1980 #text_change 07-Dec-1999 ACCESSIONS A03396 REFERENCE A93843 !$#authors Chen, K.K.; Donelson, J.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1980) 77:2445-2449 !$#title Sequences of two kinetoplast DNA minicircles of Trypanosoma !1brucei. !$#cross-references MUID:80234638; PMID:6930643 !$#accession A03396 !'##molecule_type DNA !'##residues 1-71 ##label CHE !'##cross-references GB:V01389; GB:J01455; NID:g10517; PIDN:CAA24679.1; !1PID:g671657 !'##note the sequence was determined from the 0.98-kb kinetoplast DNA GENETICS !$#genome mitochondrion !$#genetic_code SGC6 CLASSIFICATION #superfamily kinetoplast minicircle 51 polypeptide KEYWORDS mitochondrion SUMMARY #length 71 #molecular-weight 8286 #checksum 8449 SEQUENCE /// ENTRY MKUT2B #type complete TITLE kinetoplast minicircle 201 polypeptide - Trypanosoma brucei mitochondrion ORGANISM #formal_name mitochondrion Trypanosoma brucei DATE 31-Dec-1980 #sequence_revision 31-Dec-1980 #text_change 07-Dec-1999 ACCESSIONS A03397 REFERENCE A93843 !$#authors Chen, K.K.; Donelson, J.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1980) 77:2445-2449 !$#title Sequences of two kinetoplast DNA minicircles of Trypanosoma !1brucei. !$#cross-references MUID:80234638; PMID:6930643 !$#accession A03397 !'##molecule_type DNA !'##residues 1-52 ##label CHE !'##note the sequence was determined from the 1.0-kb kinetoplast DNA GENETICS !$#genome mitochondrion !$#genetic_code SGC6 CLASSIFICATION #superfamily kinetoplast minicircle 201 polypeptide KEYWORDS mitochondrion SUMMARY #length 52 #molecular-weight 5916 #checksum 5208 SEQUENCE /// ENTRY A44937 #type complete TITLE kinetoplast-associated protein - Trypanosoma cruzi ALTERNATE_NAMES probable structural protein KAP ORGANISM #formal_name Trypanosoma cruzi DATE 28-Apr-1993 #sequence_revision 02-Dec-1994 #text_change 16-Jul-1999 ACCESSIONS A44937; S27855 REFERENCE A44937 !$#authors Gonzalez, A.; Rosales, J.L.; Ley, V.; Diaz, C. !$#journal Mol. Biochem. Parasitol. (1990) 40:233-244 !$#title Cloning and characterization of a gene coding for a protein !1(KAP) associated with the kinetoplast of epimastigotes and !1amastigotes of Trypanosoma cruzi. !$#cross-references MUID:90301144; PMID:1694571 !$#accession A44937 !'##molecule_type DNA !'##residues 1-1052 ##label GON !'##cross-references EMBL:M25364; NID:g162141; PIDN:AAA30209.1; !1PID:g162142 COMMENT This protein was detected only in kinetoplasts of !1replicative stages of the parasite. The protein appears to !1be encoded by a single copy gene located in the chromosome !1rather than in the kinetoplast. COMMENT This protein is translocated to the mitochondrion without !1the loss of an amino-terminal region. CLASSIFICATION #superfamily kinetoplast-associated protein KEYWORDS duplication; mitochondrion; tandem repeat FEATURE !$424-563,582-705, !$724-862 #region 9-residue repeats (A-A-R-K-Q-A-E-E-E) SUMMARY #length 1052 #molecular-weight 118110 #checksum 5291 SEQUENCE /// ENTRY A34309 #type complete TITLE rubber elongation factor - Para rubber tree ORGANISM #formal_name Hevea brasiliensis #common_name Para rubber tree DATE 08-Jun-1990 #sequence_revision 13-Mar-1997 #text_change 03-Dec-1999 ACCESSIONS S16258; A34309 REFERENCE S16258 !$#authors Attanyaka, D.P.S.T.G.; Kekwick, R.G.O.; Franklin, F.C.H. !$#journal Plant Mol. Biol. (1991) 16:1079-1081 !$#title Molecular cloning and nucleotide sequencing of the rubber !1elongation factor gene from Hevea brasiliensis. !$#cross-references MUID:91322500; PMID:1863760 !$#accession S16258 !'##molecule_type mRNA !'##residues 1-138 ##label ATT !'##cross-references EMBL:X56535; NID:g18838; PIDN:CAA39880.1; !1PID:g18839 REFERENCE A34309 !$#authors Dennis, M.S.; Henzel, W.J.; Bell, J.; Kohr, W.; Light, D.R. !$#journal J. Biol. Chem. (1989) 264:18618-18626 !$#title Amino acid sequence of rubber elongation factor protein !1associated with rubber particles in Hevea latex. !$#cross-references MUID:90036965; PMID:2808390 !$#accession A34309 !'##molecule_type protein !'##residues 2-138 ##label DEN COMMENT This protein is found associated with growing rubber !1molecules and may play a structural role necessary for !1docking the prenyltransferase to the rubber particle. GENETICS !$#gene REF CLASSIFICATION #superfamily rubber elongation factor KEYWORDS acetylated amino end FEATURE !$2-138 #product rubber elongation factor #status !8experimental #label MAT\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental SUMMARY #length 138 #molecular-weight 14722 #checksum 5786 SEQUENCE /// ENTRY AYEC #type complete TITLE acyl carrier protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 24-Apr-1984 #sequence_revision 20-Aug-1994 #text_change 01-Mar-2002 ACCESSIONS C42147; A92042; A26935; C64853; S28389; A03398 REFERENCE A42147 !$#authors Rawlings, M.; Cronan Jr., J.E. !$#journal J. Biol. Chem. (1992) 267:5751-5754 !$#title The gene encoding Escherichia coli acyl carrier protein lies !1within a cluster of fatty acid biosynthetic genes. !$#cross-references MUID:92210530; PMID:1556094 !$#accession C42147 !'##molecule_type DNA !'##residues 1-78 ##label RAW !'##cross-references GB:M84991; NID:g145879; PIDN:AAA23740.1; !1PID:g145882 !'##experimental_source strain E-26 REFERENCE A92042 !$#authors Vanaman, T.C.; Wakil, S.J.; Hill, R.L. !$#journal J. Biol. Chem. (1968) 243:6420-6431 !$#title The complete amino acid sequence of the acyl carrier protein !1of Escherichia coli. !$#cross-references MUID:69063911; PMID:4882207 !$#accession A92042 !'##molecule_type protein !'##residues 2-24,'D',26-78 ##label VAN REFERENCE A92041 !$#authors Vanaman, T.C.; Wakil, S.J.; Hill, R.L. !$#journal J. Biol. Chem. (1968) 243:6409-6419 !$#title The preparation of tryptic, peptic, thermolysin, and !1cyanogen bromide peptides from the acyl carrier protein of !1Escherichia coli. !$#cross-references MUID:69063910; PMID:4882206 !$#contents annotation; partial sequence REFERENCE A26935 !$#authors Jackowski, S.; Rock, C.O. !$#journal J. Bacteriol. (1987) 169:1469-1473 !$#title Altered molecular form of acyl carrier protein associated !1with beta-ketoacyl-acyl carrier protein synthase II (fabF) !1mutants. !$#cross-references MUID:87165751; PMID:3549687 !$#accession A26935 !'##molecule_type protein !'##residues 2-43,'I',45-78 ##label JAC !'##experimental_source strain K-12 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64853 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-78 ##label BLAT !'##cross-references GB:AE000210; GB:U00096; NID:g1787332; !1PIDN:AAC74178.1; PID:g1787336; UWGP:b1094 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S28389 !$#authors Niki, H.; Imamura, R.; Kitaoka, M.; Yamanaka, K.; Ogura, T.; !1Hiraga, S. !$#journal EMBO J. (1992) 11:5101-5109 !$#title E. coli MukB protein involved in chromosome partition forms !1a homodimer with a rod-and-hinge structure having DNA !1binding and ATP/GTP binding activities. !$#cross-references MUID:93099885; PMID:1464330 !$#accession S28389 !'##molecule_type protein !'##residues 2-25,'X',27-35,'XX',38-41 ##label NIK GENETICS !$#gene acpP !$#map_position 24 min FUNCTION !$#description carrier of the growing fatty acid chain; growing fatty acid !1chain is covalently bound to 4'-phosphopantetheine !1prosthetic group !$#pathway fatty acid biosynthesis CLASSIFICATION #superfamily acyl carrier protein; acyl carrier protein !1homology KEYWORDS carrier protein; fatty acid biosynthesis; !1phosphopantetheine; phosphoprotein FEATURE !$2-73 #domain acyl carrier protein homology #label ACP\ !$37 #binding_site phosphopantetheine (Ser) (covalent) !8#status experimental SUMMARY #length 78 #molecular-weight 8639 #checksum 83 SEQUENCE /// ENTRY AYBH #type complete TITLE acyl carrier protein I precursor - barley ORGANISM #formal_name Hordeum vulgare #common_name barley DATE 03-Aug-1984 #sequence_revision 28-Oct-1994 #text_change 26-May-2000 ACCESSIONS S17927; A29638; A03399 REFERENCE S17927 !$#authors Hansen, L.; von Wettstein-Knowles, P. !$#journal Mol. Gen. Genet. (1991) 229:467-478 !$#title The barley genes Acl1 and Acl3 encoding acyl carrier !1proteins I and III are located on different chromosomes. !$#cross-references MUID:92049248; PMID:1944232 !$#accession S17927 !'##status preliminary !'##molecule_type DNA !'##residues 1-149 ##label HAN1 !'##cross-references EMBL:M58753; NID:g166966; PIDN:AAA32920.1; !1PID:g166967 REFERENCE A29638 !$#authors Hansen, L. !$#journal Carlsberg Res. Commun. (1987) 52:381-392 !$#title Three cDNA clones for barley leaf acyl carrier proteins I !1and III. !$#accession A29638 !'##molecule_type mRNA !'##residues 1-149 ##label HAN2 !'##cross-references GB:M24425; NID:g166972; PIDN:AAA32923.1; !1PID:g166973 REFERENCE A03399 !$#authors Hoj, P.B.; Svendsen, I. !$#journal Carlsberg Res. Commun. (1983) 48:285-305 !$#title Barley ACYL carrier protein: its amino acid sequence and !1assay using purified malonyl-CoA:ACP transacylase. !$#accession A03399 !'##molecule_type protein !'##residues 60-131 ##label HOJ COMMENT This protein is the carrier of the growing fatty acid chain !1in fatty acid biosynthesis; the sequence of residues 40-59 !1is well conserved and functionally essential. GENETICS !$#introns 23/3; 60/3; 107/3 CLASSIFICATION #superfamily acyl carrier protein; acyl carrier protein !1homology KEYWORDS carrier protein; chloroplast; fatty acid biosynthesis; !1phosphopantetheine; phosphoprotein FEATURE !$1-59 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$60-149 #product acyl carrier protein I #status experimental !8#label MAT\ !$69-140 #domain acyl carrier protein homology #label ACP\ !$104 #binding_site phosphopantetheine (Ser) (covalent) !8#status predicted SUMMARY #length 149 #molecular-weight 15974 #checksum 3818 SEQUENCE /// ENTRY AYSP #type complete TITLE acyl carrier protein I precursor - spinach ORGANISM #formal_name Spinacia oleracea #common_name spinach DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 26-May-2000 ACCESSIONS A28052 REFERENCE A28052 !$#authors Scherer, D.E.; Knauf, V.C. !$#journal Plant Mol. Biol. (1987) 9:127-134 !$#title Isolation of a cDNA clone for the acyl carrier protein-I of !1spinach. !$#accession A28052 !'##molecule_type DNA !'##residues 1-137 ##label SCH CLASSIFICATION #superfamily acyl carrier protein; acyl carrier protein !1homology KEYWORDS carrier protein; chloroplast; fatty acid biosynthesis; !1phosphopantetheine; phosphoprotein FEATURE !$1-56 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$57-137 #product acyl carrier protein #status predicted !8#label MAT\ !$59-130 #domain acyl carrier protein homology #label ACP\ !$94 #binding_site phosphopantetheine (Ser) (covalent) !8#status predicted SUMMARY #length 137 #molecular-weight 14838 #checksum 2358 SEQUENCE /// ENTRY A24706 #type complete TITLE nodulation protein nodF - Rhizobium meliloti plasmid ALTERNATE_NAMES hsnA protein ORGANISM #formal_name Rhizobium meliloti DATE 30-Jun-1988 #sequence_revision 13-Jan-1995 #text_change 26-May-2000 ACCESSIONS A24706; S06395; A24193 REFERENCE A93638 !$#authors Debelle, F.; Sharma, S.B. !$#journal Nucleic Acids Res. (1986) 14:7453-7472 !$#title Nucleotide sequence of Rhizobium meliloti RCR2011 genes !1involved in host specificity of nodulation. !$#cross-references MUID:87016382; PMID:3020515 !$#accession A24706 !'##molecule_type DNA !'##residues 1-93 ##label DEB !'##cross-references GB:X04379; NID:g46305; PIDN:CAA27960.1; PID:g46306 !'##experimental_source strain RCR2011 symbiotic plasmid REFERENCE S06395 !$#authors Fisher, R.F.; Swanson, J.A.; Mulligan, J.T.; Long, S.R. !$#journal Genetics (1987) 117:191-201 !$#title Extended region of nodulation genes in Rhizobium meliloti !11021. II. Nucleotide sequence, transcription start sites and !1protein products. !$#accession S06395 !'##molecule_type DNA !'##residues 1-93 ##label FIS !'##experimental_source strain 1021 REFERENCE A94655 !$#authors Horvath, B.; Kondorosi, E.; John, M.; Schmidt, J.; Toeroek, !1I.; Gyoergypal, Z.; Barabas, I.; Wieneke, U.; Schell, J.; !1Kondorosi, A. !$#journal Cell (1986) 46:335-343 !$#title Organization, structure and symbiotic function of Rhizobium !1meliloti nodulation genes determining host specificity for !1alfalfa. !$#cross-references MUID:86272081; PMID:3731273 !$#accession A24193 !'##status significant sequence differences !'##molecule_type DNA !'##cross-references GB:M14052 !'##experimental_source strain AK631 (a variant of strain 41) !'##note the sequence reported in this reference is incorrect due to !1frameshift errors COMMENT This is one of several proteins that control host !1specificity of root hair infection and nodulation. GENETICS !$#gene nodF; hsnA !$#genome plasmid CLASSIFICATION #superfamily acyl carrier protein; acyl carrier protein !1homology KEYWORDS carrier protein; host range; nodulation; phosphopantetheine; !1phosphoprotein FEATURE !$11-82 #domain acyl carrier protein homology #label ACP\ !$46 #binding_site phosphopantetheine (Ser) (covalent) !8#status predicted SUMMARY #length 93 #molecular-weight 9771 #checksum 2800 SEQUENCE /// ENTRY F23766 #type complete TITLE nodulation protein nodF - Rhizobium leguminosarum bv. trifolii ORGANISM #formal_name Rhizobium leguminosarum bv. trifolii DATE 21-May-1988 #sequence_revision 13-Jan-1995 #text_change 26-May-2000 ACCESSIONS F23766; S06020 REFERENCE A93614 !$#authors Schofield, P.R.; Watson, J.M. !$#journal Nucleic Acids Res. (1986) 14:2891-2903 !$#title DNA sequence of Rhizobium trifolii nodulation genes reveals !1a reiterated and potentially regulatory sequence preceding !1nodABC and nodFE. !$#cross-references MUID:86176774; PMID:3008100 !$#accession F23766 !'##molecule_type DNA !'##residues 1-92 ##label SCH !'##cross-references GB:X03721; NID:g46461; PIDN:CAA27355.1; PID:g46466 !'##experimental_source strain ANU843 REFERENCE S06020 !$#authors Spaink, H.P.; Weinman, J.; Djordjevic, M.A.; Wijffelman, !1C.A.; Okker, R.J.H.; Lugtenberg, B.J.J. !$#journal EMBO J. (1989) 8:2811-2818 !$#title Genetic analysis and cellular localization of the Rhizobium !1host specificity-determining NodE protein. !$#cross-references MUID:90059862; PMID:2684629 !$#accession S06020 !'##molecule_type DNA !'##residues 43-92 ##label SPA COMMENT This is one of several proteins that control host !1specificity of root hair infection and nodulation. GENETICS !$#gene nodF CLASSIFICATION #superfamily acyl carrier protein; acyl carrier protein !1homology KEYWORDS carrier protein; host range; nodulation; phosphopantetheine; !1phosphoprotein FEATURE !$11-81 #domain acyl carrier protein homology #label ACP\ !$45 #binding_site phosphopantetheine (Ser) (covalent) !8#status predicted SUMMARY #length 92 #molecular-weight 9791 #checksum 105 SEQUENCE /// ENTRY C25095 #type complete TITLE nodulation protein nodF - Rhizobium leguminosarum ORGANISM #formal_name Rhizobium leguminosarum DATE 05-Oct-1988 #sequence_revision 13-Jan-1995 #text_change 26-May-2000 ACCESSIONS C25095; S02060 REFERENCE A25095 !$#authors Shearman, C.A.; Rossen, L.; Johnston, A.W.B.; Downie, J.A. !$#journal EMBO J. (1986) 5:647-652 !$#title The Rhizobium leguminosarum nodulation gene nodF encodes a !1polypeptide similar to acyl-carrier protein and is regulated !1by nodD plus a factor in pea root exudate. !$#accession C25095 !'##molecule_type DNA !'##residues 1-92 ##label SHE !'##cross-references EMBL:Y00548 REFERENCE S02059 !$#authors Downie, J.A. !$#submission submitted to the EMBL Data Library, April 1988 !$#accession S02060 !'##molecule_type DNA !'##residues 1-44,'L',46-92 ##label DOW !'##cross-references EMBL:Y00548; NID:g46212; PIDN:CAA68623.1; !1PID:g599962 COMMENT This is one of several proteins that control host !1specificity of root hair infection and nodulation. GENETICS !$#gene nodF CLASSIFICATION #superfamily acyl carrier protein; acyl carrier protein !1homology KEYWORDS carrier protein; host range; nodulation; phosphopantetheine; !1phosphoprotein FEATURE !$11-81 #domain acyl carrier protein homology #label ACP\ !$45 #binding_site phosphopantetheine (Ser) (covalent) !8#status predicted SUMMARY #length 92 #molecular-weight 9945 #checksum 3151 SEQUENCE /// ENTRY D24706 #type complete TITLE nodulation protein nodH - Rhizobium meliloti plasmid ALTERNATE_NAMES hsnD protein ORGANISM #formal_name Rhizobium meliloti DATE 30-Jun-1988 #sequence_revision 13-Jan-1995 #text_change 16-Jul-1999 ACCESSIONS D24706; S07676; D24193 REFERENCE A93638 !$#authors Debelle, F.; Sharma, S.B. !$#journal Nucleic Acids Res. (1986) 14:7453-7472 !$#title Nucleotide sequence of Rhizobium meliloti RCR2011 genes !1involved in host specificity of nodulation. !$#cross-references MUID:87016382; PMID:3020515 !$#accession D24706 !'##molecule_type DNA !'##residues 1-247 ##label DEB !'##cross-references GB:X04380; NID:g46309; PIDN:CAA27963.1; PID:g46310 !'##experimental_source strain RCR2011 symbiotic plasmid REFERENCE S06395 !$#authors Fisher, R.F.; Swanson, J.A.; Mulligan, J.T.; Long, S.R. !$#journal Genetics (1987) 117:191-201 !$#title Extended region of nodulation genes in Rhizobium meliloti !11021. II. Nucleotide sequence, transcription start sites and !1protein products. !$#accession S07676 !'##molecule_type DNA !'##residues 1-247 ##label FIS !'##experimental_source strain 1021 REFERENCE A94655 !$#authors Horvath, B.; Kondorosi, E.; John, M.; Schmidt, J.; Toeroek, !1I.; Gyoergypal, Z.; Barabas, I.; Wieneke, U.; Schell, J.; !1Kondorosi, A. !$#journal Cell (1986) 46:335-343 !$#title Organization, structure and symbiotic function of Rhizobium !1meliloti nodulation genes determining host specificity for !1alfalfa. !$#cross-references MUID:86272081; PMID:3731273 !$#accession D24193 !'##molecule_type DNA !'##residues 1-8,'R',10-16,'R',18-65,'CW',68-132,'Q',134-167,'N',169-247 !1##label HOR !'##cross-references GB:M14052; NID:g152239; PIDN:AAA26291.1; !1PID:g152243 !'##experimental_source strain AK631 (a variant of strain 41) COMMENT This is one of several proteins that control host !1specificity of root hair infection and nodulation. GENETICS !$#gene nodH; hsnD !$#genome plasmid CLASSIFICATION #superfamily nodulation protein nodH KEYWORDS host range; nodulation SUMMARY #length 247 #molecular-weight 28584 #checksum 8440 SEQUENCE /// ENTRY AYKBL #type complete TITLE citrate (pro-3S)-lyase (EC 4.1.3.6) gamma chain - Klebsiella pneumoniae ALTERNATE_NAMES citrate lyase acyl carrier protein ORGANISM #formal_name Klebsiella pneumoniae DATE 31-Jan-1980 #sequence_revision 06-Jun-1997 #text_change 05-May-2000 ACCESSIONS S60774; A03400 REFERENCE S60773 !$#authors Bott, M.; Dimroth, P. !$#journal Mol. Microbiol. (1994) 14:347-356 !$#title Klebsiella pneumoniae genes for citrate lyase and citrate !1lyase ligase: localization, sequencing and expression. !$#cross-references MUID:95131756; PMID:7830578 !$#accession S60774 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-97 ##label BOT !'##cross-references EMBL:X79817; NID:g565615; PIDN:CAA56215.1; !1PID:g565617 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1994 REFERENCE A03400 !$#authors Beyreuther, K.; Bohmer, H.; Dimroth, P. !$#journal Eur. J. Biochem. (1978) 87:101-110 !$#title Amino-acid sequence of citrate-lyase acyl-carrier protein !1from Klebsiella aerogenes. !$#cross-references MUID:78214604; PMID:352686 !$#note K. aerogenes !$#accession A03400 !'##molecule_type protein !'##residues 1-39,'E',41-45,'Q',47-59,'ECDN',74,'QL',77-85,'WQ',88 !1##label BEY !'##experimental_source ATCC 13882 GENETICS !$#gene citD CLASSIFICATION #superfamily citrate lyase acyl carrier protein KEYWORDS carbon-carbon lyase; coenzyme A; oxo-acid-lyase; !1phosphoprotein FEATURE !$14 #binding_site phosphoribosyl dephospho-coenzyme A !8(Ser) (covalent) #status experimental SUMMARY #length 97 #molecular-weight 10427 #checksum 7715 SEQUENCE /// ENTRY E64043 #type complete TITLE citrate (pro-3S)-lyase (EC 4.1.3.6) gamma chain - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES citrate lyase acyl carrier protein; citrate lyase, acyl lyase chain CitD ORGANISM #formal_name Haemophilus influenzae DATE 18-Aug-1995 #sequence_revision 14-Feb-1997 #text_change 05-May-2000 ACCESSIONS E64043 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession E64043 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-95 ##label TIGR !'##cross-references GB:U32688; GB:L42023; NID:g1572966; !1PIDN:AAC21702.1; PID:g1572969; TIGR:HI0024 !'##note named as homolog to a protein from Klebsiella pneumoniae CLASSIFICATION #superfamily citrate lyase acyl carrier protein KEYWORDS carbon-carbon lyase; coenzyme A; oxo-acid-lyase; !1phosphoprotein FEATURE !$14 #binding_site phosphoribosyl dephospho-coenzyme A !8(Ser) (covalent) #status predicted SUMMARY #length 95 #molecular-weight 10184 #checksum 534 SEQUENCE /// ENTRY G64795 #type complete TITLE citrate (pro-3S)-lyase (EC 4.1.3.6) gamma chain [similarity] - Escherichia coli (strain K-12) ALTERNATE_NAMES citrate lyase acyl carrier protein ORGANISM #formal_name Escherichia coli DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 01-Mar-2002 ACCESSIONS G64795 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64795 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-98 ##label BLAT !'##cross-references GB:AE000166; GB:U00096; NID:g1786819; !1PIDN:AAC73718.1; PID:g1786834; UWGP:b0617 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene citD CLASSIFICATION #superfamily citrate lyase acyl carrier protein KEYWORDS carbon-carbon lyase; coenzyme A; oxo-acid-lyase; !1phosphoprotein FEATURE !$14 #binding_site phosphoribosyl dephospho-coenzyme A !8(Ser) (covalent) #status predicted SUMMARY #length 98 #molecular-weight 10689 #checksum 9705 SEQUENCE /// ENTRY T46729 #type complete TITLE citrate (pro-3S)-lyase (EC 4.1.3.6) gamma chain [similarity] - Weissella paramesenteroides plasmid ORGANISM #formal_name Weissella paramesenteroides DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 21-Jul-2000 ACCESSIONS T46729 REFERENCE Z23138 !$#authors Martin, M.; Corrales, M.; de Mendoza, D.; Lopez, P.; Magni, !1C. !$#journal FEMS Microbiol. Lett. (1999) 174:231-238 !$#title Cloning and molecular characterization of the citrate !1utilisation citMCDEFGRP cluster of Leuconostoc !1paramesenteroides. !$#cross-references MUID:99271171; PMID:10339813 !$#accession T46729 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-146 ##label MAR !'##cross-references EMBL:AJ132782; NID:g6249489; PIDN:CAB60041.1; !1PID:g6249492 !'##experimental_source strain J1 !'##note the correct initiation codon is probably Met-50 GENETICS !$#gene citD !$#genome plasmid CLASSIFICATION #superfamily citrate lyase acyl carrier protein KEYWORDS carbon-carbon lyase; coenzyme A; oxo-acid-lyase; !1phosphoprotein FEATURE !$63 #binding_site phosphoribosyl dephospho-coenzyme A !8(Ser) (covalent) #status predicted SUMMARY #length 146 #molecular-weight 16291 #checksum 4361 SEQUENCE /// ENTRY BKIP #type complete TITLE biotin carboxyl carrier protein [validated] - Propionibacterium freudenreichii subsp. shermanii ALTERNATE_NAMES methylmalonyl-CoA carboxyltransferase biotin carboxyl carrier protein (BCCP) ORGANISM #formal_name Propionibacterium freudenreichii subsp. shermanii DATE 31-Mar-1980 #sequence_revision 31-Mar-1980 #text_change 01-Feb-2002 ACCESSIONS A03401 REFERENCE A03401 !$#authors Maloy, W.L.; Bowien, B.U.; Zwolinski, G.K.; Kumar, K.G.; !1Wood, H.G.; Ericsson, L.H.; Walsh, K.A. !$#journal J. Biol. Chem. (1979) 254:11615-11622 !$#title Amino acid sequence of the biotinyl subunit from !1transcarboxylase. !$#cross-references MUID:80049796; PMID:40985 !$#accession A03401 !'##molecule_type protein !'##residues 1-123 ##label MAL COMMENT Six or 12 chains of biotin carboxyl carrier protein (BCCP) !1are found in the transcarboxylase complex. Two other types !1of chains catalyze the transfer of a carboxyl group (1) from !1methylmalonyl coenzyme A to BCCP and (2) from BCCP to !1pyruvate, forming oxalacetate. COMMENT See PIR:A48665 and PIR:S36808. CLASSIFICATION #superfamily biotin carboxyl carrier protein; lipoyl/ !1biotin-binding homology KEYWORDS biotin binding FEATURE !$50-123 #domain lipoyl/biotin-binding homology #label LPB\ !$89 #binding_site biotin (Lys) (covalent) #status !8experimental SUMMARY #length 123 #molecular-weight 12367 #checksum 8869 SEQUENCE /// ENTRY BKEC9 #type complete TITLE acetyl-CoA carboxylase (EC 6.4.1.2) biotin carboxyl carrier protein [validated] - Escherichia coli (strain K-12) CONTAINS biotin carboxyl carrier protein ORGANISM #formal_name Escherichia coli DATE 30-Nov-1980 #sequence_revision 31-Dec-1989 #text_change 01-Mar-2002 ACCESSIONS A93687; A92204; JS0686; PS0357; A33643; C40637; PS0272; !1A65118; S78777; A03402; JU0027 REFERENCE A93687 !$#authors Muramatsu, S.; Mizuno, T. !$#journal Nucleic Acids Res. (1989) 17:3982 !$#title Nucleotide sequence of the fabE gene and flanking regions !1containing a bent DNA sequence of Escherichia coli. !$#cross-references MUID:89282408; PMID:2660106 !$#accession A93687 !'##molecule_type DNA !'##residues 1-156 ##label MUR !'##cross-references GB:X14825; NID:g41361; PIDN:CAA32933.1; PID:g41362 !'##experimental_source strain LA2-22 REFERENCE A92204 !$#authors Sutton, M.R.; Fall, R.R.; Nervi, A.M.; Alberts, A.W.; !1Vagelos, P.R.; Bradshaw, R.A. !$#journal J. Biol. Chem. (1977) 252:3934-3940 !$#title Amino acid sequence of Escherichia coli biotin carboxyl !1carrier protein (9100). !$#cross-references MUID:77187896; PMID:324999 !$#accession A92204 !'##molecule_type protein !'##residues 75-156 ##label SUT REFERENCE JS0686 !$#authors Li, S.J.; Cronan Jr., J.E. !$#journal J. Biol. Chem. (1992) 267:855-863 !$#title The gene encoding the biotin carboxylase subunit of !1Escherichia coli acetyl-CoA carboxylase. !$#cross-references MUID:92112819; PMID:1370469 !$#accession JS0686 !'##molecule_type DNA !'##residues 1-156 ##label LIS !'##cross-references GB:M80458; NID:g145172; PIDN:AAA23408.1; !1PID:g145174 !'##experimental_source strain K12 !$#accession PS0357 !'##molecule_type protein !'##residues 1-23 ##label LIS1 REFERENCE A33643 !$#authors Alix, J.H. !$#journal DNA (1989) 8:779-789 !$#title A rapid procedure for cloning genes from lambda libraries by !1complementation of E. coli defective mutants: application to !1the fabE region of the E. coli chromosome. !$#cross-references MUID:90126231; PMID:2575489 !$#accession A33643 !'##molecule_type DNA !'##residues 1-156 ##label ALI !'##cross-references GB:M32214; NID:g145889; PIDN:AAA23744.1; !1PID:g145890 REFERENCE A40637 !$#authors Li, S.J.; Cronan Jr., J.E. !$#journal J. Bacteriol. (1993) 175:332-340 !$#title Growth rate regulation of Escherichia coli acetyl coenzyme A !1carboxylase, which catalyzes the first committed step of !1lipid biosynthesis. !$#cross-references MUID:93123150; PMID:7678242 !$#accession C40637 !'##status preliminary !'##molecule_type DNA !'##residues 1-25 ##label LI1 !'##cross-references GB:S52932; NID:g263399; PIDN:AAB24892.1; !1PID:g263401 !'##note sequence extracted from NCBI backbone (NCBIN:122315, !1NCBIP:122319) REFERENCE JS0632 !$#authors Kondo, H.; Shiratsuchi, K.; Yoshimoto, T.; Masuda, T.; !1Kitazono, A.; Tsuru, D.; Anai, M.; Sekiguchi, M.; Tanabe, T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:9730-9733 !$#title Acetyl-CoA carboxylase from Escherichia coli: gene !1organization and nucleotide sequence of the biotin !1carboxylase subunit. !$#cross-references MUID:92052166; PMID:1682920 !$#accession PS0272 !'##molecule_type DNA !'##residues 133-156 ##label KON !'##cross-references GB:M79446 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65118 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-156 ##label BLAT !'##cross-references GB:AE000404; GB:U00096; NID:g2367207; !1PIDN:AAC76287.1; PID:g1789653; UWGP:b3255 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S78777 !$#authors Chapman-Smith, A.; Turner, D.L.; Cronan Jr., J.E.; Morris, !1T.W.; Wallace, J.C. !$#journal Biochem. J. (1994) 302:881-887 !$#title Expression, biotinylation and purification of a !1biotin-domain peptide from the biotin carboxy carrier !1protein of Escherichia coli acetyl-CoA carboxylase. !$#cross-references MUID:95031932; PMID:7945216 !$#accession S78777 !'##molecule_type protein !'##residues 2-20 ##label CHA GENETICS !$#gene accB; fabE !$#map_position 72 min COMPLEX in E. coli, acetyl-CoA carboxylase is composed of biotin !1carboxylase (EC 6.3.4.14) (PIR:JS0362), carboxyltransferase !1(heterodimer of alpha (PIR:A43452) and beta (PIR:XMECBD) !1chains), and biotin carboxyl carrier protein (BCCP, !1homodimer) (PIR:BKEC9) FUNCTION ACO !$#description EC 6.4.1.2 [validated; MUID:75035569]; the acetyl-CoA !1carboxylase complex catalyzes the synthesis of malonyl-CoA !1from acetyl-CoA !$#pathway fatty acid biosynthesis FUNCTION BCC !$#description a specific lysine residue within the biotin carboxyl carrier !1protein (BCCP) is recognized and biotinylated by the biotin !1protein ligase birA [validated; MUID:99400973] !$#note the C-terminal 87 amino acids of the biotin carboxyl carrier !1protein (BCCP87) form a domain that can be independently !1expressed, biotinylated, and purified [validated; !1MUID:20011362] CLASSIFICATION #superfamily biotin carboxyl carrier protein; lipoyl/ !1biotin-binding homology KEYWORDS biotin binding; fatty acid biosynthesis; homodimer; ligase FEATURE !$1-156 #product biotin carboxyl carrier protein BCCP, long !8form #status experimental #label MAT1\ !$2-156 #product biotin carboxyl carrier protein #status !8experimental #label MAT\ !$70-156 #product biotin carboxyl carrier protein BCCP87, !8short form #status experimental #label MAT2\ !$76-156 #domain lipoyl/biotin-binding homology #label LPB\ !$122 #binding_site biotin (Lys) (covalent) #status !8experimental SUMMARY #length 156 #molecular-weight 16687 #checksum 9714 SEQUENCE /// ENTRY A49342 #type complete TITLE acetyl-CoA carboxylase (EC 6.4.1.2), biotin carboxyl carrier protein - Pseudomonas aeruginosa ORGANISM #formal_name Pseudomonas aeruginosa DATE 07-Apr-1994 #sequence_revision 26-May-1994 #text_change 01-Feb-2002 ACCESSIONS A49342; G83039 REFERENCE A49342 !$#authors Best, E.A.; Knauf, V.C. !$#journal J. Bacteriol. (1993) 175:6881-6889 !$#title Organization and nucleotide sequences of the genes encoding !1the biotin carboxyl carrier protein and biotin carboxylase !1protein of Pseudomonas aeruginosa acetyl coenzyme A !1carboxylase. !$#cross-references MUID:94042851; PMID:7693652 !$#accession A49342 !'##molecule_type DNA !'##residues 1-156 ##label BES !'##cross-references GB:L14612; NID:g405539; PIDN:AAA16040.1; !1PID:g405540 REFERENCE A82950 !$#authors Stover, C.K.; Pham, X.Q.; Erwin, A.L.; Mizoguchi, S.D.; !1Warrener, P.; Hickey, M.J.; Brinkman, F.S.L.; Hufnagle, !1W.O.; Kowalik, D.J.; Lagrou, M.; Garber, R.L.; Goltry, L.; !1Tolentino, E.; Westbrook-Wadman, S.; Yuan, Y.; Brody, L.L.; !1Coulter, S.N.; Folger, K.R.; Kas, A.; Larbig, K.; Lim, R.M.; !1Smith, K.A.; Spencer, D.H.; Wong, G.K.S.; Wu, Z.; Paulsen, !1I.T.; Reizer, J.; Saier, M.H.; Hancock, R.E.W.; Lory, S.; !1Olson, M.V. !$#journal Nature (2000) 406:959-964 !$#title Complete genome sequence of Pseudomonas aeruginosa PA01, an !1opportunistic pathogen. !$#cross-references MUID:20437337; PMID:10984043 !$#accession G83039 !'##status preliminary !'##molecule_type DNA !'##residues 1-156 ##label STO !'##cross-references GB:AE004898; GB:AE004091; NID:g9951115; !1PIDN:AAG08232.1; GSPDB:GN00131; PASP:PA4847 !'##experimental_source strain PAO1 GENETICS !$#gene accB; PA4847 CLASSIFICATION #superfamily biotin carboxyl carrier protein; lipoyl/ !1biotin-binding homology KEYWORDS biotin binding; fatty acid biosynthesis; homodimer; ligase FEATURE !$76-156 #domain lipoyl/biotin-binding homology #label LPB\ !$122 #binding_site biotin (Lys) (covalent) #status !8predicted SUMMARY #length 156 #molecular-weight 16455 #checksum 8724 SEQUENCE /// ENTRY BYEC #type complete TITLE sulfate binding protein precursor, periplasmic - Escherichia coli (strain K-12) ALTERNATE_NAMES sulfate starvation-induced protein SSI2 ORGANISM #formal_name Escherichia coli DATE 31-Dec-1988 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS S40860; H65197; B25206; A94501; A23719; S78618 REFERENCE S40802 !$#authors Plunkett III, G.; Burland, V.; Daniels, D.L.; Blattner, F.R. !$#journal Nucleic Acids Res. (1993) 21:3391-3398 !$#title Analysis of the Escherichia coli genome. III. DNA sequence !1of the region from 87.2 to 89.2 minutes. !$#cross-references MUID:93347969; PMID:8346018 !$#accession S40860 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-329 ##label PLU !'##cross-references EMBL:L19201; NID:g304961; PIDN:AAB03049.1; !1PID:g305020 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1993 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65197 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-329 ##label BLAT !'##cross-references GB:AE000466; GB:U00096; NID:g2367328; !1PIDN:AAC76899.1; PID:g1790351; UWGP:b3917 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A91144 !$#authors Hellinga, H.W.; Evans, P.R. !$#journal Eur. J. Biochem. (1985) 149:363-373 !$#title Nucleotide sequence and high-level expression of the major !1Escherichia coli phosphofructokinase. !$#cross-references MUID:85203917; PMID:3158524 !$#accession B25206 !'##molecule_type DNA !'##residues 1-177,'X',179-184,'E',186-201,'P',203-329 ##label HEL !'##cross-references GB:X02519; NID:g42365; PIDN:CAA26357.1; PID:g42367 !'##note this sequence has since been corrected REFERENCE A94501 !$#authors Evans, P.R. !$#submission submitted to the EMBL Data Library, October 1986 !$#contents correction !$#accession A94501 !'##molecule_type DNA !'##residues 153-160 ##label EVA !'##note this entry is a correction to residues 153-160 REFERENCE A23719 !$#authors Jacobson, B.L.; He, J.J.; Vermersch, P.S.; Lemon, D.D.; !1Quiocho, F.A. !$#journal J. Biol. Chem. (1991) 266:5220-5225 !$#title Engineered interdomain disulfide in the periplasmic receptor !1for sulfate transport reduces flexibility. Site-directed !1mutagenesis and ligand-binding studies. !$#cross-references MUID:91161616; PMID:2002055 !$#accession A23719 !'##molecule_type DNA !'##residues 152-164;'D',199-200;201-203 ##label JAC !'##note the authors show only portions of sequences that correct the !1previously published sequence REFERENCE S78617 !$#authors Quadroni, M.; Staudenmann, W.; Kertesz, M.; James, P. !$#journal Eur. J. Biochem. (1996) 239:773-781 !$#title Analysis of global responses by protein and peptide !1fingerprinting of proteins isolated by two-dimensional gel !1electrophoresis. Application to the sulfate-starvation !1response of Escherichia coli. !$#cross-references MUID:96370830; PMID:8774726 !$#accession S78618 !'##molecule_type protein !'##residues 20-29;42-48;256-261,'X',263;'X',266-272,'X';277-282 ##label !1QUA GENETICS !$#gene sbp !$#map_position 88 min CLASSIFICATION #superfamily sulfate-binding protein KEYWORDS periplasmic space; sulfate transport FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-329 #product sulfate-binding protein #status experimental !8#label MAT SUMMARY #length 329 #molecular-weight 36659 #checksum 2807 SEQUENCE /// ENTRY BYEBT #type complete TITLE sulfate-binding protein - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 24-Sep-1981 #sequence_revision 09-Aug-1997 #text_change 09-Aug-1997 ACCESSIONS A03403; S09675 REFERENCE A03403 !$#authors Isihara, H.; Hogg, R.W. !$#journal J. Biol. Chem. (1980) 255:4614-4618 !$#title Amino acid sequence of the sulfate-binding protein from !1Salmonella typhimurium LT2. !$#cross-references MUID:80182123; PMID:6989815 !$#accession A03403 !'##molecule_type protein !'##residues 1-230,232-300,'D',302-311 ##label ISI !'##experimental_source strain LT2 REFERENCE S04172 !$#authors Garrett, A.R.; Johnson, L.A.; Beacham, I.R. !$#journal Mol. Microbiol. (1989) 3:177-186 !$#title Isolation, molecular characterization and expression of the !1ushB gene of Salmonella typhimurium which encodes a !1membrane-bound UDP-sugar hydrolase. !$#cross-references MUID:89343621; PMID:2548058 !$#accession S09675 !'##status translation not shown !'##molecule_type DNA !'##residues 228-311 ##label GAR !'##cross-references EMBL:X13380 COMMENT This protein, isolated from the periplasmic space of the !1cell, specifically binds sulfate and is involved in its !1transmembrane transport. CLASSIFICATION #superfamily sulfate-binding protein KEYWORDS periplasmic space; sulfate transport SUMMARY #length 311 #molecular-weight 34604 #checksum 5418 SEQUENCE /// ENTRY JGECT #type complete TITLE thiosulfate-binding protein cysP precursor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 01-Mar-2002 ACCESSIONS A35403; H65016 REFERENCE A35403 !$#authors Hryniewicz, M.; Sirko, A.; Palucha, A.; Boeck, A.; !1Hulanicka, D. !$#journal J. Bacteriol. (1990) 172:3358-3366 !$#title Sulfate and thiosulfate transport in Escherichia coli K-12: !1identification of a gene encoding a novel protein involved !1in thiosulfate binding. !$#cross-references MUID:90264335; PMID:2188959 !$#accession A35403 !'##molecule_type DNA !'##residues 1-338 ##label HRY !'##cross-references GB:M32101; NID:g145657; PIDN:AAA23636.1; !1PID:g145658 !'##experimental_source strain K12 !'##note the authors translated the codon CCG for residue 247 as Thr and !1ACC for residue 321 as Pro REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65016 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-338 ##label BLAT !'##cross-references GB:AE000330; GB:U00096; NID:g1788763; !1PIDN:AAC75478.1; PID:g1788765; UWGP:b2425 !'##experimental_source strain K-12, substrain MG1655 COMMENT This protein may be a component of the sulfate and !1thiosulfate binding-protein-dependent transport system; it !1specifically binds thiosulfates. GENETICS !$#gene cysP !$#map_position 52 min CLASSIFICATION #superfamily sulfate-binding protein KEYWORDS binding protein-dependent transport system; sulfate !1transport; thiosulfate transport FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-338 #product thiosulfate-binding protein cysP #status !8predicted #label MAT SUMMARY #length 338 #molecular-weight 37614 #checksum 477 SEQUENCE /// ENTRY WQECPH #type complete TITLE phosphotransferase system phosphohistidine-containing protein [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES phosphotransferase system HPr ORGANISM #formal_name Escherichia coli DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 01-Mar-2002 ACCESSIONS A29785; A24035; A32345; G28181; F65015 REFERENCE A29785 !$#authors Saffen, D.W.; Presper, K.A.; Doering, T.L.; Roseman, S. !$#journal J. Biol. Chem. (1987) 262:16241-16253 !$#title Sugar transport by the bacterial phosphotransferase system. !1Molecular cloning and structural analysis of the Escherichia !1coli ptsH, ptsI, and crr genes. !$#cross-references MUID:88058992; PMID:2960675 !$#accession A29785 !'##molecule_type DNA !'##residues 1-85 ##label SAF !'##cross-references GB:J02796; NID:g147397; PIDN:AAA24440.1; !1PID:g147398 REFERENCE A24035 !$#authors De Reuse, H.; Roy, A.; Danchin, A. !$#journal Gene (1985) 35:199-207 !$#title Analysis of the ptsH-ptsI-crr region in Escherichia coli !1K-12: nucleotide sequence of the ptsH gene. !$#cross-references MUID:85286351; PMID:2411636 !$#accession A24035 !'##molecule_type DNA !'##residues 1-85 ##label DER1 !'##cross-references GB:M10425; NID:g147394; PIDN:AAA24438.1; !1PID:g147395 REFERENCE A32345 !$#authors De Reuse, H.; Danchin, A. !$#journal J. Bacteriol. (1988) 170:3827-3837 !$#title The ptsH, ptsI, and crr genes of the Escherichia coli !1phosphoenolpyruvate-dependent phosphotransferase system: a !1complex operon with several modes of transcription. !$#cross-references MUID:88314869; PMID:2457575 !$#accession A32345 !'##molecule_type DNA !'##residues 1-85 ##label DER2 !'##cross-references GB:M21994; NID:g147261; PIDN:AAA24384.1; !1PID:g147263 REFERENCE A28181 !$#authors Byrne, C.R.; Monroe, R.S.; Ward, K.A.; Kredich, N.M. !$#journal J. Bacteriol. (1988) 170:3150-3157 !$#title DNA sequences of the cysK regions of Salmonella typhimurium !1and Escherichia coli and linkage of the cysK regions to !1ptsH. !$#cross-references MUID:88257033; PMID:3290198 !$#accession G28181 !'##molecule_type DNA !'##residues 1-85 ##label BYR !'##cross-references GB:M21451; NID:g145684; PIDN:AAA23655.1; !1PID:g145687 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65015 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-85 ##label BLAT !'##cross-references GB:AE000329; GB:U00096; NID:g2367137; !1PIDN:AAC75468.1; PID:g1788755; UWGP:b2415 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A52379 !$#authors Prasad, L.; Delbaere, L.T.J.; Quail, J.W.; Vandonselaar, M. !$#submission submitted to the Brookhaven Protein Data Bank, April 1993 !$#cross-references PDB:1JEL !$#contents annotation; X-ray crystallography, 2.8 angstroms, residues !11-2,'E',4-85 REFERENCE A39710 !$#authors Sharma, S.; Georges, F.; Delbaere, L.T.J.; Lee, J.S.; !1Klevit, R.E.; Waygood, E.B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:4877-4881 !$#title Epitope mapping by mutagenesis distinguishes between the two !1tertiary structures of the histidine-containing protein HPr. !$#cross-references MUID:91271296; PMID:1711212 !$#contents annotation; site-directed mutagenesis REFERENCE A51916 !$#authors Jia, Z.; Quail, W.; Delbaere, L. !$#submission submitted to the Brookhaven Protein Data Bank, October 1993 !$#cross-references PDB:1POH !$#contents annotation; X-ray crystallography, 2.0 angstroms, residues !11-85 REFERENCE A52354 !$#authors Van Nuland, N.A.J.; Scheek, R.M.; Robillard, G.T. !$#submission submitted to the Brookhaven Protein Data Bank, February 1994 !$#cross-references PDB:1HDN !$#contents annotation; conformation by (1)H-, (13)C-, and (15)N-NMR, !1residues 1-85 REFERENCE A58916 !$#authors van Nuland, N.A.J.; Hangyi, I.W.; van Schaik, R.C.; !1Berendsen, H.J.C.; van Gunsteren, W.F.; Scheek, R.M.; !1Robillard, G.T. !$#journal J. Mol. Biol. (1994) 237:544-559 !$#title The high-resolution structure of the histidine-containing !1phosphocarrier protein HPr from Escherichia coli determined !1by restrained molecular dynamics from nuclear magnetic !1resonance nuclear Overhauser effect data. !$#cross-references MUID:94210480; PMID:8158637 !$#contents annotation; conformation by (1)H-, (13)C-, and (15)N-NMR REFERENCE A58912 !$#authors van Nuland, N.A.J.; Groetzinger, J.; Dijkstra, K.; Scheek, !1R.M.; Robillard, G.T. !$#journal Eur. J. Biochem. (1992) 210:881-891 !$#title Determination of the three-dimensional solution structure of !1the histidine-containing phosphocarrier protein HPr from !1Escherichia coli using multidimensional NMR spectroscopy. !$#cross-references MUID:93130914; PMID:1483471 !$#contents annotation; conformation by (1)H-, (13)C-, and (15)N-NMR REFERENCE A66357 !$#authors Van Nuland, N.A.J.; Scheek, R.M.; Robillard, G.T. !$#submission submitted to the Brookhaven Protein Data Bank, August 1995 !$#cross-references PDB:1PFH !$#contents annotation; conformation by (1)H-, (13)C-, and (15)N-NMR, !1residues 1-85 REFERENCE A58913 !$#authors van Nuland, N.A.J.; Boelens, R.; Scheek, R.M.; Robillard, !1G.T. !$#journal J. Mol. Biol. (1995) 246:180-193 !$#title High-resolution structure of the phosphorylated form of the !1histidine-containing phosphocarrier protein HPr from !1Escherichia coli determined by restrained molecular dynamics !1from NMR-NOE data. !$#cross-references MUID:95156481; PMID:7853396 !$#contents annotation; conformation by (1)H-, (13)C-, and (15)N-NMR REFERENCE A67665 !$#authors Napper, S.; Delbaere, L.; Waygood, B. !$#submission submitted to the Brookhaven Protein Data Bank, August 1996 !$#cross-references PDB:1OPD !$#contents annotation; X-ray crystallography, 1.5 angstroms, residues !11-2,'E',4-45,'D',47-85 REFERENCE A58915 !$#authors Napper, S.; Anderson, J.W.; Georges, F.; Quail, J.W.; !1Delbaere, L.T.J.; Waygood, E.B. !$#journal Biochemistry (1996) 35:11260-11267 !$#title Mutation of serine-46 to aspartate in the !1histidine-containing protein of Escherichia coli mimics the !1inactivation by phosphorylation of serine-46 in HPrs from !1Gram-positive bacteria. !$#cross-references MUID:96378616; PMID:8784179 !$#contents annotation; X-ray crystallography, 1.5 angstroms COMMENT This protein is phosphorylated by the phosphotransferase !1system enzyme I (see PIR:WQECPI), and serves as the !1phosphate donor for various sugar-specific !1phosphotransferase system enzyme II systems. GENETICS !$#gene ptsH !$#map_position 52 min CLASSIFICATION #superfamily phosphotransferase system !1phosphohistidine-containing protein; phosphotransferase !1system phosphohistidine-containing protein homology KEYWORDS phosphocarrier protein; phosphohistidine; phosphoprotein; !1phosphotransferase system; sugar transport system FEATURE !$8-84 #domain phosphotransferase system !8phosphohistidine-containing protein homology #label !8HPR\ !$15 #binding_site phosphate (His) (covalent) (by !8phosphotransferase system enzyme I) #status !8experimental\ !$46 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 85 #molecular-weight 9119 #checksum 6673 SEQUENCE /// ENTRY WQEBPH #type complete TITLE phosphotransferase system phosphohistidine-containing protein - Salmonella typhimurium ALTERNATE_NAMES phosphocarrier protein HPr ORGANISM #formal_name Salmonella typhimurium DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jul-1999 ACCESSIONS C28181; S04159; A22849 REFERENCE A28181 !$#authors Byrne, C.R.; Monroe, R.S.; Ward, K.A.; Kredich, N.M. !$#journal J. Bacteriol. (1988) 170:3150-3157 !$#title DNA sequences of the cysK regions of Salmonella typhimurium !1and Escherichia coli and linkage of the cysK regions to !1ptsH. !$#cross-references MUID:88257033; PMID:3290198 !$#accession C28181 !'##molecule_type DNA !'##residues 1-85 ##label BYR !'##cross-references GB:M21450; NID:g153933; PIDN:AAA27052.1; !1PID:g153936 REFERENCE S04159 !$#authors Schnierow, B.J.; Yamada, M.; Saier Jr., M.H. !$#journal Mol. Microbiol. (1989) 3:113-118 !$#title Partial nucleotide sequence of the pts operon in Salmonella !1typhimurium: comparative analyses in five bacterial genera. !$#cross-references MUID:89237892; PMID:2497295 !$#accession S04159 !'##molecule_type DNA !'##residues 1-85 ##label SCH !'##cross-references EMBL:X14737; NID:g47844; PIDN:CAA32865.1; !1PID:g47845 REFERENCE A22849 !$#authors Powers, D.A.; Roseman, S. !$#journal J. Biol. Chem. (1984) 259:15212-15214 !$#title The primary structure of Salmonella typhimurium HPr, a !1phosphocarrier protein of the phosphoenolpyruvate:glycose !1phosphotransferase system. !$#cross-references MUID:85080006; PMID:6392295 !$#accession A22849 !'##molecule_type protein !'##residues 1-20,'G',22-84,'Z' ##label POW COMMENT The phosphoenolpyruvate-glycose phosphotransferase system !1(PTS) comprises two general proteins (Hpr and enzyme I) and !1a sugar-specific complex (enzyme II), which consists of a !1pair of factors (II-A/II-B or III/II), lipid, and divalent !1cation. The phosphoryl group is transferred from !1phosphoenolpyruvate to enzyme I, to Hpr, to II-A (or III), !1to II-B (or II), and finally to the sugar substrate as it !1crosses the cell membrane. GENETICS !$#gene ptsH !$#map_position 49 min CLASSIFICATION #superfamily phosphotransferase system !1phosphohistidine-containing protein; phosphotransferase !1system phosphohistidine-containing protein homology KEYWORDS phosphocarrier protein; phosphohistidine; phosphoprotein; !1sugar transport system FEATURE !$8-84 #domain phosphotransferase system !8phosphohistidine-containing protein homology #label !8HPR\ !$15 #binding_site phosphate (His) (covalent) (by !8phosphotransferase system enzyme I) #status !8predicted\ !$46 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 85 #molecular-weight 9119 #checksum 6673 SEQUENCE /// ENTRY S12749 #type complete TITLE phosphotransferase system phosphohistidine-containing protein - Klebsiella pneumoniae ORGANISM #formal_name Klebsiella pneumoniae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S12749 REFERENCE S12749 !$#authors Titgemeyer, F.; Eisermann, R.; Hengstenberg, W.; Lengeler, !1J.W. !$#journal Nucleic Acids Res. (1990) 18:1898 !$#title The nucleotide sequence of ptsH gene from Klebsiella !1pneumoniae. !$#cross-references MUID:90245592; PMID:2186369 !$#accession S12749 !'##molecule_type DNA !'##residues 1-85 ##label TIT !'##cross-references EMBL:X51452; NID:g43910; PIDN:CAA35818.1; !1PID:g43911 GENETICS !$#gene ptsH CLASSIFICATION #superfamily phosphotransferase system !1phosphohistidine-containing protein; phosphotransferase !1system phosphohistidine-containing protein homology KEYWORDS phosphocarrier protein; phosphohistidine; phosphoprotein; !1sugar transport system FEATURE !$8-84 #domain phosphotransferase system !8phosphohistidine-containing protein homology #label !8HPR\ !$15 #binding_site phosphate (His) (covalent) (by !8phosphotransferase system enzyme I) #status !8predicted\ !$46 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 85 #molecular-weight 9119 #checksum 6691 SEQUENCE /// ENTRY I64137 #type complete TITLE phosphotransferase system phosphohistidine-containing protein - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS I64137 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession I64137 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-85 ##label TIGR !'##cross-references GB:U32844; GB:L42023; NID:g1574563; !1PIDN:AAC23358.1; PID:g1574568; TIGR:HI1713 CLASSIFICATION #superfamily phosphotransferase system !1phosphohistidine-containing protein; phosphotransferase !1system phosphohistidine-containing protein homology KEYWORDS phosphocarrier protein; phosphohistidine; phosphoprotein; !1sugar transport system FEATURE !$8-84 #domain phosphotransferase system !8phosphohistidine-containing protein homology #label !8HPR\ !$15 #binding_site phosphate (His) (covalent) (by !8phosphotransferase system enzyme I) #status !8predicted\ !$46 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 85 #molecular-weight 9004 #checksum 6180 SEQUENCE /// ENTRY WQBSPH #type complete TITLE phosphotransferase system phosphohistidine-containing protein [validated] - Bacillus subtilis ALTERNATE_NAMES phosphocarrier protein HPr; PtsH ORGANISM #formal_name Bacillus subtilis DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 15-Sep-2000 ACCESSIONS S04177; A46238; G41835; F69683 REFERENCE S04174 !$#authors Gonzy-Treboul, G.; Zagorec, M.; Rain-Guion, M.C.; Steinmetz, !1M. !$#journal Mol. Microbiol. (1989) 3:103-112 !$#title Phosphoenolpyruvate:sugar phosphotransferase system of !1Bacillus subtilis: nucleotide sequence of ptsX, ptsH and the !15'-end of ptsI and evidence for a ptsHI operon. !$#cross-references MUID:89237891; PMID:2497294 !$#accession S04177 !'##molecule_type DNA !'##residues 1-88 ##label GON !'##cross-references EMBL:X12832; NID:g48679; PIDN:CAA31317.1; !1PID:g48682 REFERENCE A46238 !$#authors Reizer, J.; Hoischen, C.; Reizer, A.; Pham, T.N.; Saier Jr., !1M.H. !$#journal Protein Sci. (1993) 2:506-521 !$#title Sequence analyses and evolutionary relationships among the !1energy-coupling proteins Enzyme I and HPr of the bacterial !1phosphoenolpyruvate: sugar phosphotransferase system. !$#cross-references MUID:93299364; PMID:7686067 !$#accession A46238 !'##molecule_type DNA !'##residues 1-88 ##label REI !'##cross-references GB:M98359; NID:g1943574 !'##note sequence extracted from NCBI backbone (NCBIN:134327, !1NCBIP:134328) !'##note this ORF is not annotated in GenBank entry BACPTSI in release !1103.0 REFERENCE A41835 !$#authors Mitchell, C.; Morris, P.W.; Vary, J.C. !$#journal J. Bacteriol. (1992) 174:2474-2477 !$#title Identification of proteins phosphorylated by ATP during !1sporulation of Bacillus subtilis. !$#cross-references MUID:92210489; PMID:1556067 !$#accession G41835 !'##molecule_type protein !'##residues 1-20 ##label MIT !'##note studies on phosporylation in vitro by extracts of Bacillus !1subtilis at various stages of growth showed that !1phosphorylation occurred after glucose in the medium was !1depleted REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69683 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-88 ##label KUN !'##cross-references GB:Z99111; GB:AL009126; NID:g2633699; !1PIDN:CAB13263.1; PID:g2633761 !'##experimental_source strain 168 REFERENCE A67240 !$#authors Jones, B.E.; Rajagopal, P.; Klevit, R.E. !$#submission submitted to the Brookhaven Protein Data Bank, May 1996 !$#cross-references PDB:2HID !$#contents annotation; conformation by (1)H-NMR, residues 2-50,'V', !152-88 REFERENCE A56289 !$#authors Rajagopal, P.; Waygood, E.B.; Klevit, R.E. !$#journal Biochemistry (1994) 33:15271-15282 !$#title Structural consequences of histidine phosphorylation: NMR !1characterization of the phosphohistidine form of !1histidine-containing protein from Bacillus subtilis and !1Escherichia coli. !$#cross-references MUID:95101620; PMID:7803390 !$#contents annotation; conformation by (1)H-NMR REFERENCE A58682 !$#authors Wittekind, M.; Rajagopal, P.; Branchini, B.R.; Reizer, J.; !1Saier Jr., M.H.; Klevit, R.E. !$#journal Protein Sci. (1992) 1:1363-1376 !$#title Solution structure of the phosphocarrier protein HPr from !1Bacillus subtilis by two-dimensional NMR spectroscopy. !$#cross-references MUID:93271883; PMID:1303754 !$#contents annotation; conformation by (1)H-NMR REFERENCE A50888 !$#authors Herzberg, O. !$#submission submitted to the Brookhaven Protein Data Bank, September !11992 !$#cross-references PDB:2HPR !$#contents annotation; X-ray crystallography, 2.0 angstroms, residues !12-50,'V',52-82,'C',84-88 REFERENCE A41987 !$#authors Herzberg, O.; Reddy, P.; Sutrina, S.; Saier Jr., M.H.; !1Reizer, J.; Kapadia, G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:2499-2503 !$#title Structure of the histidine-containing phosphocarrier protein !1HPr from Bacillus subtilis at 2.0-angstrom resolution. !$#cross-references MUID:92196146; PMID:1549615 !$#contents annotation; X-ray crystallography, 2.0 angstroms COMMENT Phosphorylation of Ser-46 inhibits the ability of this !1protein to accept phosphate on His-15. The phosphorylation !1of Ser-46 is regulated by specific kinase and phosphatase !1activities. GENETICS !$#gene ptsH FUNCTION !$#description a histidine of this protein is phosphorylated by !1phosphotransferase system enzyme I and the phosphoryl group !1is subsequently removed by a metabolite-specific !1phosphotransferase system enzyme II !$#pathway sugar transport CLASSIFICATION #superfamily phosphotransferase system !1phosphohistidine-containing protein; phosphotransferase !1system phosphohistidine-containing protein homology KEYWORDS phosphocarrier protein; phosphohistidine; phosphoprotein; !1sugar transport system FEATURE !$8-85 #domain phosphotransferase system !8phosphohistidine-containing protein homology #label !8HPR\ !$15 #binding_site phosphate (His) (covalent) (by !8phosphotransferase system enzyme I) #status !8experimental\ !$46 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 88 #molecular-weight 9189 #checksum 2909 SEQUENCE /// ENTRY WQSOHP #type complete TITLE phosphotransferase system phosphohistidine-containing protein - Enterococcus faecalis ALTERNATE_NAMES phosphotransferase system HPr ORGANISM #formal_name Enterococcus faecalis DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jul-1999 ACCESSIONS A25053; S32115 REFERENCE A25053 !$#authors Deutscher, J.; Pevec, B.; Beyreuther, K.; Kiltz, H.H.; !1Hengstenberg, W. !$#journal Biochemistry (1986) 25:6543-6551 !$#title Streptococcal phosphoenolpyruvate-sugar phosphotransferase !1system: amino acid sequence and site of ATP-dependent !1phosphorylation of HPr. !$#cross-references MUID:87076587; PMID:3098288 !$#accession A25053 !'##molecule_type protein !'##residues 1-89 ##label DEU REFERENCE S32115 !$#authors Reizer, J.; Mitchell, W.J.; Romano, A.H.; Mirkov, E.T.; !1Saier, M.H. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Cloning and nucleotide sequence of the ptsH gene of !1Enterococcus faecalis. !$#accession S32115 !'##status preliminary !'##molecule_type DNA !'##residues 1-88 ##label REI !'##cross-references EMBL:Z19137; NID:g287946; PIDN:CAA79533.1; !1PID:g287947 CLASSIFICATION #superfamily phosphotransferase system !1phosphohistidine-containing protein; phosphotransferase !1system phosphohistidine-containing protein homology KEYWORDS phosphocarrier protein; phosphohistidine; phosphoprotein; !1sugar transport system FEATURE !$8-85 #domain phosphotransferase system !8phosphohistidine-containing protein homology #label !8HPR\ !$15 #binding_site phosphate (His) (covalent) (by !8phosphotransferase system enzyme I) #status !8predicted\ !$46 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 89 #molecular-weight 9449 #checksum 6110 SEQUENCE /// ENTRY A42374 #type complete TITLE phosphotransferase system phosphohistidine-containing protein - Staphylococcus carnosus ALTERNATE_NAMES phosphotransferase system HPr ORGANISM #formal_name Staphylococcus carnosus DATE 10-Jul-1992 #sequence_revision 31-Jan-1997 #text_change 03-Dec-1999 ACCESSIONS S15367; A42374 REFERENCE S15367 !$#authors Eisermann, R.; Fischer, R.; Kessler, U.; Neubauer, A.; !1Hengstenberg, W. !$#journal Eur. J. Biochem. (1991) 197:9-14 !$#title Staphylococcal phosphoenolpyruvate-dependent !1phosphotransferase system. Purification and protein !1sequencing of the Staphylococcus carnosus !1histidine-containing protein, and cloning and DNA sequencing !1of the ptsH gene. !$#cross-references MUID:91200066; PMID:1901791 !$#accession S15367 !'##status preliminary !'##molecule_type DNA !'##residues 1-88 ##label EIS !'##cross-references EMBL:X60766; NID:g46907; PIDN:CAA43175.1; !1PID:g46908 REFERENCE A42374 !$#authors Kohlbrecher, D.; Eisermann, R.; Hengstenberg, W. !$#journal J. Bacteriol. (1992) 174:2208-2214 !$#title Staphylococcal phosphoenolpyruvate-dependent !1phosphotransferase system: molecular cloning and nucleotide !1sequence of the Staphylococcus carnosus ptsI gene and !1expression and complementation studies of the gene product. !$#cross-references MUID:92202148; PMID:1551842 !$#accession A42374 !'##status preliminary !'##molecule_type DNA !'##residues 43-88 ##label KOH !'##cross-references GB:M69050; NID:g153073; PIDN:AAA26663.1; !1PID:g153074 GENETICS !$#gene ptsH CLASSIFICATION #superfamily phosphotransferase system !1phosphohistidine-containing protein; phosphotransferase !1system phosphohistidine-containing protein homology KEYWORDS phosphocarrier protein; phosphohistidine; phosphoprotein; !1sugar transport system FEATURE !$8-85 #domain phosphotransferase system !8phosphohistidine-containing protein homology #label !8HPR\ !$15 #binding_site phosphate (His) (covalent) (by !8phosphotransferase system enzyme I) #status !8predicted\ !$46 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 88 #molecular-weight 9511 #checksum 3696 SEQUENCE /// ENTRY A44562 #type complete TITLE phosphotransferase system phosphohistidine-containing protein - Streptococcus mutans ALTERNATE_NAMES phosphocarrier protein HPr ORGANISM #formal_name Streptococcus mutans DATE 10-Mar-1994 #sequence_revision 31-Jan-1997 #text_change 26-Feb-1999 ACCESSIONS A44562; JC2114 REFERENCE A44562 !$#authors Reynolds, E.C. !$#submission submitted to the Protein Sequence Database, February 1994 !$#accession A44562 !'##molecule_type protein !'##residues 1-87 ##label REY !'##experimental_source strain Ingbritt !'##note the initial Met was found in 14% of the molecules REFERENCE JC2114 !$#authors Dashper, S.G.; Kirszbaum, L.; Huq, N.L.; Riley, P.F.; !1Reynolds, E.C. !$#journal Biochem. Biophys. Res. Commun. (1994) 199:1297-1304 !$#title Complete amino acid sequence and comparative molecular !1modelling of HPr from Streptococcus mutans ingbritt. !$#cross-references MUID:94197719; PMID:8147873 !$#accession JC2114 !'##molecule_type protein !'##residues 2-87 ##label DAS !'##note initiator Met was present in 14% of the molecules COMMENT This protein is a heat stable regulatory protein of the !1phosphotransferase system. CLASSIFICATION #superfamily phosphotransferase system !1phosphohistidine-containing protein; phosphotransferase !1system phosphohistidine-containing protein homology KEYWORDS phosphocarrier protein; phosphohistidine; phosphoprotein; !1sugar transport system FEATURE !$8-85 #domain phosphotransferase system !8phosphohistidine-containing protein homology #label !8HPR\ !$1 #modified_site N-formylmethionine (partial) #status !8experimental\ !$15 #binding_site phosphate (His) (covalent) (by !8phosphotransferase system enzyme I) #status !8predicted\ !$46 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 87 #molecular-weight 8936 #checksum 9977 SEQUENCE /// ENTRY S37585 #type complete TITLE phosphotransferase system phosphohistidine-containing protein - Streptococcus salivarius ALTERNATE_NAMES phosphocarrier protein HPr ORGANISM #formal_name Streptococcus salivarius DATE 06-Jan-1995 #sequence_revision 31-Jan-1997 #text_change 16-Jul-1999 ACCESSIONS S37585; PC1176 REFERENCE S37585 !$#authors Gagnon, G.; Vadeboncoeur, C.; Frenette, M. !$#submission submitted to the EMBL Data Library, October 1992 !$#description The Streptococcus salivarius pts operon: cloning, sequence !1and expression of the ptsH gene. !$#accession S37585 !'##status preliminary !'##molecule_type DNA !'##residues 1-87 ##label GAG !'##cross-references EMBL:Z17217; NID:g406778; PIDN:CAA78923.1; !1PID:g406779 REFERENCE JC1375 !$#authors Gagnon, G.; Vadeboncoeur, C.; Levesque, R.C.; Frenette, M. !$#journal Gene (1992) 121:71-78 !$#title Cloning, sequencing and expression in Escherichia coli of !1the ptsI gene encoding enzyme I of the !1phosphoenolpyruvate:sugar phosphotransferase transport !1system from Streptococcus salivarius. !$#cross-references MUID:93051364; PMID:1427100 !$#accession PC1176 !'##molecule_type DNA !'##residues 65-87 ##label GA2 !'##cross-references GB:M81756 CLASSIFICATION #superfamily phosphotransferase system !1phosphohistidine-containing protein; phosphotransferase !1system phosphohistidine-containing protein homology KEYWORDS phosphocarrier protein; phosphohistidine; phosphoprotein; !1phosphotransferase system; sugar transport system FEATURE !$8-85 #domain phosphotransferase system !8phosphohistidine-containing protein homology #label !8HPR\ !$15 #binding_site phosphate (His) (covalent) (by !8phosphotransferase system enzyme I) #status !8predicted\ !$46 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 87 #molecular-weight 8907 #checksum 75 SEQUENCE /// ENTRY WPSAHP #type complete TITLE phosphotransferase system phosphohistidine-containing protein - Staphylococcus aureus ALTERNATE_NAMES phosphotransferase system HPr ORGANISM #formal_name Staphylococcus aureus DATE 30-Apr-1979 #sequence_revision 30-Apr-1979 #text_change 20-Feb-1998 ACCESSIONS A03404 REFERENCE A03404 !$#authors Beyreuther, K.; Raufuss, H.; Schrecker, O.; Hengstenberg, W. !$#journal Eur. J. Biochem. (1977) 75:275-286 !$#title The phosphoenolpyruvate-dependent phosphotransferase system !1of Staphylococcus aureus. 1. Amino-acid sequence of the !1phosphocarrier protein HPr. !$#cross-references MUID:77185012; PMID:862621 !$#accession A03404 !'##molecule_type protein !'##residues 1-70 ##label BEY COMMENT This protein participates in the active transport of !1galactosides into the cell by a !1phosphoenolpyruvate-dependent phosphotransferase system that !1phosphorylates the galactoside at the inner surface of the !1cell membrane. CLASSIFICATION #superfamily phosphotransferase system !1phosphohistidine-containing protein; phosphotransferase !1system phosphohistidine-containing protein homology KEYWORDS phosphocarrier protein; phosphohistidine; phosphoprotein; !1sugar transport system FEATURE !$8-70 #domain phosphotransferase system !8phosphohistidine-containing protein homology #label !8HPR\ !$15 #binding_site phosphate (His) (covalent) (by !8phosphotransferase system enzyme I) #status !8experimental\ !$44 #binding_site phosphate (Ser) (covalent) #status !8experimental SUMMARY #length 70 #molecular-weight 7685 #checksum 3273 SEQUENCE /// ENTRY A49683 #type complete TITLE phosphotransferase system phosphohistidine-containing protein - Mycoplasma capricolum ALTERNATE_NAMES phosphocarrier protein HPr ORGANISM #formal_name Mycoplasma capricolum DATE 26-May-1995 #sequence_revision 31-Jan-1997 #text_change 07-Dec-1999 ACCESSIONS A49683 REFERENCE A49683 !$#authors Zhu, P.P.; Reizer, J.; Reizer, A.; Peterkofsky, A. !$#journal J. Biol. Chem. (1993) 268:26531-26540 !$#title Unique monocistronic operon (ptsH) in Mycoplasma capricolum !1encoding the phosphocarrier protein, HPr, of the !1phosphoenolpyruvate:sugar phosphotransferase system. !1Cloning, sequencing, and characterization of ptsH. !$#cross-references MUID:94075343; PMID:8253782 !$#accession A49683 !'##status preliminary !'##molecule_type DNA !'##residues 1-89 ##label ZHU !'##cross-references GB:L22432; NID:g435095; PIDN:AAA16213.1; !1PID:g435097 !'##note monocistronic operon GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily phosphotransferase system !1phosphohistidine-containing protein; phosphotransferase !1system phosphohistidine-containing protein homology KEYWORDS phosphocarrier protein; phosphohistidine; phosphoprotein; !1phosphotransferase system; sugar transport system FEATURE !$8-85 #domain phosphotransferase system !8phosphohistidine-containing protein homology #label !8HPR\ !$15 #binding_site phosphate (His) (covalent) (by !8phosphotransferase system enzyme I) #status !8predicted\ !$46 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 89 #molecular-weight 9418 #checksum 3831 SEQUENCE /// ENTRY S60667 #type complete TITLE phosphotransferase system phosphohistidine-containing protein - Klebsiella pneumoniae ALTERNATE_NAMES phosphotransferase protein HPr ORGANISM #formal_name Klebsiella pneumoniae DATE 19-Jul-1996 #sequence_revision 31-Jan-1997 #text_change 16-Jul-1999 ACCESSIONS S60667 REFERENCE S60666 !$#authors Merrick, M.J.; Taylor, M. !$#submission submitted to the EMBL Data Library, August 1995 !$#description Sequence and characterisation of distal genes in the !1Klebsiella pneumoniae rpoN operon. !$#accession S60667 !'##status preliminary !'##molecule_type DNA !'##residues 1-90 ##label MER !'##cross-references EMBL:Z50803; NID:g950054; PIDN:CAA90685.1; !1PID:g950056 CLASSIFICATION #superfamily phosphotransferase system !1phosphohistidine-containing protein; phosphotransferase !1system phosphohistidine-containing protein homology KEYWORDS phosphocarrier protein; phosphohistidine; phosphoprotein; !1phosphotransferase system; sugar transport system FEATURE !$9-86 #domain phosphotransferase system !8phosphohistidine-containing protein homology #label !8HPR\ !$16 #binding_site phosphate (His) (covalent) (by !8phosphotransferase system enzyme I) #status !8predicted\ !$48 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 90 #molecular-weight 9820 #checksum 4629 SEQUENCE /// ENTRY JHEBT #type complete TITLE histidine-binding protein J precursor - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 29-Jun-1981 #sequence_revision 17-Dec-1982 #text_change 24-Sep-1999 ACCESSIONS A93893; A92304; A03407 REFERENCE A93893 !$#authors Higgins, C.F.; Ames, G.F.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:6038-6042 !$#title Two periplasmic transport proteins which interact with a !1common membrane receptor show extensive homology: complete !1nucleotide sequences. !$#cross-references MUID:82082392; PMID:6273842 !$#accession A93893 !'##molecule_type DNA !'##residues 1-260 ##label HIG !'##cross-references GB:V01372; NID:g47717; PIDN:CAA24658.1; PID:g47718 REFERENCE A92304 !$#authors Hogg, R.W. !$#journal J. Biol. Chem. (1981) 256:1935-1939 !$#title The amino acid sequence of the histidine binding protein of !1Salmonella typhimurium. !$#cross-references MUID:81117284; PMID:7007375 !$#accession A92304 !'##molecule_type protein !'##residues 23-172,'N',174-260 ##label HOG COMMENT This periplasmic binding protein is one of the components of !1the high-affinity histidine permease, a !1binding-protein-dependent transport system. The other !1components are proteins Q, M, and P. The P protein is a !1common receptor for two independent binding proteins, J and !1LAO, the sequences of which are 70% identical. GENETICS !$#gene hisJ !$#map_position 48.5 CLASSIFICATION #superfamily lysine-arginine-ornithine-binding protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-260 #product histidine-binding protein J #status !8experimental #label MAT\ !$60-67 #disulfide_bonds #status experimental SUMMARY #length 260 #molecular-weight 28379 #checksum 6194 SEQUENCE /// ENTRY JKEBT #type complete TITLE lysine/arginine/ornithine-binding protein LAO precursor - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 24-Sep-1999 ACCESSIONS A03408 REFERENCE A93893 !$#authors Higgins, C.F.; Ames, G.F.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:6038-6042 !$#title Two periplasmic transport proteins which interact with a !1common membrane receptor show extensive homology: complete !1nucleotide sequences. !$#cross-references MUID:82082392; PMID:6273842 !$#accession A03408 !'##molecule_type DNA !'##residues 1-260 ##label HIG !'##cross-references GB:V01368; NID:g47639; PIDN:CAA24651.1; PID:g47640 COMMENT This periplasmic binding protein is involved in an arginine !1transport system. Its sequence is 70% identical with that of !1histidine-binding protein J; the two proteins interact with !1a common membrane-bound receptor, protein P. GENETICS !$#gene argT !$#map_position 48.5 CLASSIFICATION #superfamily lysine-arginine-ornithine-binding protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-260 #product lysine/arginine/ornithine-binding protein !8LAO #status predicted #label MAT\ !$60-67 #disulfide_bonds #status predicted SUMMARY #length 260 #molecular-weight 28186 #checksum 7669 SEQUENCE /// ENTRY JKECT #type complete TITLE lysine-arginine-ornithine-binding periplasmic protein precursor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1988 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS D65003; I29803 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65003 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-260 ##label BLAT !'##cross-references GB:AE000320; GB:U00096; NID:g1788647; !1PIDN:AAC75370.1; PID:g1788649; UWGP:b2310 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A29803 !$#authors Nonet, M.L.; Marvel, C.C.; Tolan, D.R. !$#journal J. Biol. Chem. (1987) 262:12209-12217 !$#title The hisT-purF region of the Escherichia coli K-12 !1chromosome. Identification of additional genes of the hisT !1and purF operons. !$#cross-references MUID:87308226; PMID:3040734 !$#accession I29803 !'##molecule_type DNA !'##residues 1-22,'P',24-85,'ST',88-94,'V',96-146 ##label NON !'##cross-references GB:M68935; GB:J02800; NID:g146360; PIDN:AAA23971.1; !1PID:g551811 COMMENT This periplasmic binding protein is involved in an arginine !1transport system. GENETICS !$#gene argT !$#map_position 50 min CLASSIFICATION #superfamily lysine-arginine-ornithine-binding protein KEYWORDS arginine transport FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-146 #product lysine/arginine/ornithine-binding protein !8LAO (fragment) #status predicted #label MAT\ !$60-67 #disulfide_bonds #status predicted SUMMARY #length 260 #molecular-weight 27991 #checksum 7694 SEQUENCE /// ENTRY JKECQ #type complete TITLE ABC-type transport system glutamine-binding protein precursor [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES glutamine-binding periplasmic protein ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 01-Mar-2002 ACCESSIONS S03181; C64818 REFERENCE S03181 !$#authors Nohno, T.; Saito, T.; Hong, J. !$#journal Mol. Gen. Genet. (1986) 205:260-269 !$#title Cloning and complete nucleotide sequence of the Escherichia !1coli glutamine permease operon (glnHPQ). !$#cross-references MUID:87115160; PMID:3027504 !$#accession S03181 !'##molecule_type DNA !'##residues 1-248 ##label NOH !'##cross-references EMBL:X14180; NID:g41568; PIDN:CAA32382.1; !1PID:g41569 !'##experimental_source strain K-12, substrain PSM2 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64818 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-248 ##label BLAT !'##cross-references GB:AE000183; GB:U00096; NID:g1787025; !1PIDN:AAC73898.1; PID:g1787031; UWGP:b0811 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene glnH !$#map_position 18 min FUNCTION ABC !$#description the ABC-type glutamine transport system glnHPQ is a highly !1specific binding protein-dependent transport system for !1glutamine FUNCTION PER !$#description periplasmic glutamine-binding component of the ABC-type !1glutamine transport system glnHPQ [validated, MUID:87115160] !$#note induction by lack of glutamine CLASSIFICATION #superfamily lysine-arginine-ornithine-binding protein KEYWORDS binding protein-dependent transport system; glutamine !1transport; periplasmic space FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-248 #product glutamine-binding protein #status !8experimental #label MAT SUMMARY #length 248 #molecular-weight 27190 #checksum 4561 SEQUENCE /// ENTRY A39194 #type complete TITLE periplasmic dipeptide transport protein precursor dppA - Escherichia coli (strain K-12) ALTERNATE_NAMES dipeptide transport protein dppA; dipeptide-binding protein dppA ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS A39194; S15292; S47766; S61403; C65153; S61431 REFERENCE A39194 !$#authors Olson, E.R.; Dunyak, D.S.; Jurss, L.M.; Poorman, R.A. !$#journal J. Bacteriol. (1991) 173:234-244 !$#title Identification and characterization of dppA, an Escherichia !1coli gene encoding a periplasmic dipeptide transport !1protein. !$#cross-references MUID:91100289; PMID:1702779 !$#accession A39194 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-535 ##label OLS !'##cross-references GB:M35045; NID:g145796; PIDN:AAA23707.1; !1PID:g145797 REFERENCE S15292 !$#authors Abouhamad, W.N.; Manson, M.; Gibson, M.M.; Higgins, C.F. !$#journal Mol. Microbiol. (1991) 5:1035-1047 !$#title Peptide transport and chemotaxis in Escherichia coli and !1Salmonella typhimurium: characterization of the dipeptide !1permease (Dpp) and the dipeptide-binding protein. !$#cross-references MUID:92065799; PMID:1956284 !$#accession S15292 !'##status preliminary !'##molecule_type DNA !'##residues 1-535 ##label ABO !'##cross-references EMBL:X58051; NID:g42474; PIDN:CAA41090.1; !1PID:g42475 REFERENCE S47666 !$#authors Plunkett, G. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S47766 !'##status preliminary !'##molecule_type DNA !'##residues 1-535 ##label PLU !'##cross-references EMBL:U00039; NID:g466582; PIDN:AAB18522.1; !1PID:g466683 REFERENCE S61403 !$#authors Abouhamad, W.N.; Manson, M.D. !$#submission submitted to the EMBL Data Library, November 1993 !$#description The dipeptide permease (dpp) operon of Escherichia coli !1resembles the oligopeptide permease (opp) but exhibits !1unique features. !$#accession S61403 !'##status preliminary !'##molecule_type DNA !'##residues 1-535 ##label AB2 !'##cross-references EMBL:L08399; NID:g349224; PIDN:AAA23702.1; !1PID:g349225 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65153 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-535 ##label BLAT !'##cross-references GB:AE000431; GB:U00096; NID:g1789957; !1PIDN:AAC76569.1; PID:g1789966; UWGP:b3544 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S61431 !$#authors Abouhamad, W.N.; Manson, M.D. !$#journal Mol. Microbiol. (1994) 14:1077-1092 !$#title The dipeptide permease of Escherichia coli closely resembles !1other bacterial transport systems and shows !1growth-phase-dependent expression. !$#cross-references MUID:95231288; PMID:7536291 !$#accession S61431 !'##molecule_type DNA !'##residues 1-33;534-535 ##label AB3 !'##cross-references EMBL:L08399 GENETICS !$#gene dppA CLASSIFICATION #superfamily dipeptide transport protein FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-535 #product dipeptide-binding protein dppA #status !8predicted #label MAT SUMMARY #length 535 #molecular-weight 60293 #checksum 4717 SEQUENCE /// ENTRY B64557 #type complete TITLE dipeptide ABC transporter, periplasmic dipeptide-binding protein - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B64557 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession B64557 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-549 ##label TOM !'##cross-references GB:AE000548; GB:AE000511; NID:g2313391; !1PIDN:AAD07367.1; PID:g2313396; TIGR:HP0298 CLASSIFICATION #superfamily dipeptide transport protein SUMMARY #length 549 #molecular-weight 62467 #checksum 4223 SEQUENCE /// ENTRY S39594 #type complete TITLE nickel-binding periplasmic protein precursor - Escherichia coli (strain K-12) ALTERNATE_NAMES nikA protein ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS S39594; S47695; G65144 REFERENCE S39594 !$#authors Navarro, C.; Wu, L.F.; Mandrand-Berthelot, M.A. !$#journal Mol. Microbiol. (1993) 9:1181-1191 !$#title The nik operon of Escherichia coli encodes a periplasmic !1binding-protein-dependent transport system for nickel. !$#cross-references MUID:95020649; PMID:7934931 !$#accession S39594 !'##status preliminary !'##molecule_type DNA !'##residues 1-524 ##label NAV !'##cross-references EMBL:X73143; NID:g404844; PIDN:CAA51659.1; !1PID:g404845 REFERENCE S47666 !$#authors Plunkett, G. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S47695 !'##status preliminary !'##molecule_type DNA !'##residues 1-524 ##label PLU !'##cross-references EMBL:U00039; NID:g466582; PIDN:AAB18451.1; !1PID:g466612 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65144 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-524 ##label BLAT !'##cross-references GB:AE000423; GB:U00096; NID:g1789880; !1PIDN:AAC76501.1; PID:g1789887; UWGP:b3476 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene nikA CLASSIFICATION #superfamily dipeptide transport protein SUMMARY #length 524 #molecular-weight 58718 #checksum 5088 SEQUENCE /// ENTRY A64134 #type complete TITLE periplasmic dipeptide transport protein dppA homolog - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A64134 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession A64134 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-565 ##label TIGR !'##cross-references GB:U32837; GB:L42023; NID:g1574485; !1PIDN:AAC23285.1; PID:g1574486; TIGR:HI1638 CLASSIFICATION #superfamily dipeptide transport protein SUMMARY #length 565 #molecular-weight 64504 #checksum 4824 SEQUENCE /// ENTRY F64871 #type complete TITLE oligopeptide-binding protein precursor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS F64871; A36263 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64871 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-543 ##label BLAT !'##cross-references GB:AE000222; GB:U00096; NID:g1787486; !1PIDN:AAC74325.1; PID:g1787495; UWGP:b1243 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A36263 !$#authors Kashiwagi, K.; Yamaguchi, Y.; Sakai, Y.; Kobayashi, H.; !1Igarashi, K. !$#journal J. Biol. Chem. (1990) 265:8387-8391 !$#title Identification of the polyamine-induced protein as a !1periplasmic oligopeptide binding protein. !$#cross-references MUID:90256748; PMID:2187863 !$#accession A36263 !'##status preliminary !'##molecule_type DNA !'##residues 1-270,'Y',272-313,'LW',316-486,'HG',489-543 ##label KAS !'##cross-references GB:J05433; NID:g147013; PIDN:AAA21302.1; !1PID:g147014 GENETICS !$#gene oppA CLASSIFICATION #superfamily dipeptide transport protein KEYWORDS binding protein-dependent transport system; oligopeptide !1transport; periplasmic space FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-543 #product oligopeptide-binding protein #status !8predicted #label MAT SUMMARY #length 543 #molecular-weight 60898 #checksum 5109 SEQUENCE /// ENTRY QREBOA #type complete TITLE oligopeptide-binding protein precursor - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS A25011 REFERENCE A25011 !$#authors Hiles, I.D.; Higgins, C.F. !$#journal Eur. J. Biochem. (1986) 158:561-567 !$#title Peptide uptake by Salmonella typhimurium. The periplasmic !1oligopeptide-binding protein. !$#cross-references MUID:86274740; PMID:3525163 !$#accession A25011 !'##molecule_type DNA !'##residues 1-542 ##label HIL !'##cross-references GB:X04194; NID:g47807; PIDN:CAA27785.1; PID:g47808 COMMENT This protein binds peptides up to five amino acids long with !1high affinity, serving as the primary receptor for !1oligopeptides in the oligopeptide permease transport system. GENETICS !$#gene oppA !$#map_position 34 min CLASSIFICATION #superfamily dipeptide transport protein KEYWORDS binding protein-dependent transport system; oligopeptide !1transport; periplasmic space FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-542 #product oligopeptide-binding protein #status !8predicted #label MAT SUMMARY #length 542 #molecular-weight 61261 #checksum 1904 SEQUENCE /// ENTRY QRBYPR #type complete TITLE arginine transport protein - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES arginine permease; protein YEL063c ORGANISM #formal_name Saccharomyces cerevisiae DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 23-Mar-2001 ACCESSIONS A23922; S50526; S05825 REFERENCE A23922 !$#authors Hoffmann, W. !$#journal J. Biol. Chem. (1985) 260:11831-11837 !$#title Molecular characterization of the CAN1 locus in !1Saccharomyces cerevisiae. A transmembrane protein without !1N-terminal hydrophobic signal sequence. !$#cross-references MUID:86008235; PMID:3900064 !$#accession A23922 !'##molecule_type DNA !'##residues 1-590 ##label HOF !'##cross-references EMBL:M11724; NID:g171154; PIDN:AAA34467.1; !1PID:g171155 REFERENCE S50434 !$#authors Dietrich, F.S. !$#submission submitted to the EMBL Data Library, December 1994 !$#description The sequence of S. cerevisiae cosmids 9669, 8334, 8199, and !1lambda clone 1160. !$#accession S50526 !'##molecule_type DNA !'##residues 1-590 ##label DIE !'##cross-references EMBL:U18795; NID:g603241; PIDN:AAB65024.1; !1PID:g603255; GSPDB:GN00005; MIPS:YEL063c REFERENCE S05825 !$#authors Ahmad, M.; Bussey, H. !$#journal Curr. Genet. (1986) 10:587-592 !$#title Yeast arginine permease: nucleotide sequence of the CAN1 !1gene. !$#cross-references MUID:88165106; PMID:3327612 !$#accession S05825 !'##molecule_type DNA !'##residues 1-533,'V',535-590 ##label AHM !'##cross-references EMBL:X03784; NID:g3441; PIDN:CAA27416.1; PID:g3442 GENETICS !$#gene SGD:CAN1; MIPS:YEL063c !'##cross-references SGD:S0000789; MIPS:YEL063c !$#map_position 5L CLASSIFICATION #superfamily arginine permease KEYWORDS amino acid transport; arginine transport; transmembrane !1protein SUMMARY #length 590 #molecular-weight 65785 #checksum 3603 SEQUENCE /// ENTRY S50711 #type complete TITLE basic-amino-acid permease - yeast (Candida albicans) ORGANISM #formal_name Candida albicans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S50711 REFERENCE S50711 !$#authors Sychrova, H.; Souciet, J.L. !$#journal Yeast (1994) 10:1647-1651 !$#title CAN1, a gene encoding a permease for basic amino acids in !1Candida albicans. !$#cross-references MUID:95242840; PMID:7725800 !$#accession S50711 !'##status preliminary !'##molecule_type DNA !'##residues 1-571 ##label SYC !'##cross-references EMBL:X76689 CLASSIFICATION #superfamily arginine permease KEYWORDS amino acid transport; glycoprotein; transmembrane protein FEATURE !$69-85 #domain transmembrane #status predicted #label TM1\ !$96-112 #domain transmembrane #status predicted #label TM2\ !$175-191 #domain transmembrane #status predicted #label TM3\ !$211-227 #domain transmembrane #status predicted #label TM4\ !$301-317 #domain transmembrane #status predicted #label TM5\ !$323-339 #domain transmembrane #status predicted #label TM6\ !$346-362 #domain transmembrane #status predicted #label TM7\ !$398-414 #domain transmembrane #status predicted #label TM8\ !$425-441 #domain transmembrane #status predicted #label TM9\ !$476-492 #domain transmembrane #status predicted #label TM10\ !$499-515 #domain transmembrane #status predicted #label TM11 SUMMARY #length 571 #molecular-weight 63343 #checksum 1444 SEQUENCE /// ENTRY QRECAA #type complete TITLE aromatic amino acid transport protein aroP - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1991 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS H64733; JS0447; S10720; S45191 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64733 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-457 ##label BLAT !'##cross-references GB:AE000120; GB:U00096; NID:g1786298; !1PIDN:AAC73223.1; PID:g1786302; UWGP:b0112 !'##experimental_source strain K-12, substrain MG1655 REFERENCE JS0447 !$#authors Honore, N.; Cole, S.T. !$#journal Nucleic Acids Res. (1990) 18:653 !$#title Nucleotide sequence of the aroP gene encoding the general !1aromatic amino acid transport protein of Escherichia coli !1K-12: homology with yeast transport proteins. !$#cross-references MUID:90174991; PMID:2408019 !$#accession JS0447 !'##molecule_type DNA !'##residues 1-27,'S',29-198,'A',200-397,'L',400-457 ##label HON !'##cross-references EMBL:X17333 !'##experimental_source strain K12 REFERENCE S10720 !$#authors Cole, S.T. !$#submission submitted to the EMBL Data Library, December 1989 !$#accession S10720 !'##molecule_type DNA !'##residues 1-27,'S',29-198,'A',200-397,'L',400-423,'R',425-426,'G', !1428,'W',430-457 ##label COL !'##cross-references EMBL:X17333; NID:g40985; PIDN:CAA35211.1; !1PID:g40986 !'##experimental_source strain K-12 REFERENCE S45181 !$#authors Fujita, N. !$#submission submitted to the EMBL Data Library, January 1994 !$#accession S45191 !'##molecule_type DNA !'##residues 1-27,'S',29-198,'A',200-397,'L',400-423,'R',425-426,'G', !1428,'W',430-457 ##label FUJ !'##cross-references EMBL:D26562; NID:g473770; PIDN:BAA05570.1; !1PID:g473781 !'##experimental_source strain K-12 substrain W3110 GENETICS !$#gene aroP !$#map_position 2.6 min FUNCTION !$#description transports tryptophan, phenylalanine, and tyrosine CLASSIFICATION #superfamily arginine permease KEYWORDS amino acid transport; transmembrane protein FEATURE !$20-36 #domain transmembrane #status predicted #label TM1\ !$47-63 #domain transmembrane #status predicted #label TM2\ !$99-115 #domain transmembrane #status predicted #label TM3\ !$125-141 #domain transmembrane #status predicted #label TM4\ !$154-170 #domain transmembrane #status predicted #label TM5\ !$204-220 #domain transmembrane #status predicted #label TM6\ !$245-261 #domain transmembrane #status predicted #label TM7\ !$283-299 #domain transmembrane #status predicted #label TM8\ !$334-350 #domain transmembrane #status predicted #label TM9\ !$361-377 #domain transmembrane #status predicted #label TM10\ !$407-423 #domain transmembrane #status predicted #label TM11\ !$426-442 #domain transmembrane #status predicted #label TM12 SUMMARY #length 457 #molecular-weight 49690 #checksum 2440 SEQUENCE /// ENTRY S38111 #type complete TITLE amino acid transport protein GAP1 [validated] - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES general amino acid permease GAP1; protein YKR039w ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 20-Apr-2000 ACCESSIONS S38111; S13036 REFERENCE S38097 !$#authors Urrestarazu, L.A.; Jauniaux, J.C. !$#submission submitted to the Protein Sequence Database, March 1994 !$#accession S38111 !'##molecule_type DNA !'##residues 1-602 ##label URR !'##cross-references EMBL:Z28264; NID:g486478; PIDN:CAA82113.1; !1PID:g486479; GSPDB:GN00011; MIPS:YKR039w !'##experimental_source strain S288C REFERENCE S13036 !$#authors Jauniaux, J.C.; Grenson, M. !$#journal Eur. J. Biochem. (1990) 190:39-44 !$#title GAP1, the general amino acid permease gene of Saccharomyces !1cerevisiae. Nucleotide sequence, protein similarity with the !1other bakers yeast amino acid permeases, and nitrogen !1catabolite repression. !$#cross-references MUID:90306009; PMID:2194797 !$#accession S13036 !'##molecule_type DNA !'##residues 1-121,123-188,'A',190-337,'V',339-517,'L',519-602 ##label !1JAU !'##cross-references EMBL:X52633; NID:g3721; PIDN:CAA36858.1; PID:g3722 GENETICS !$#gene SGD:GAP1; MIPS:YKR039w !'##cross-references SGD:S0001747; MIPS:YKR039w !$#map_position 11R FUNCTION !$#description transports several amino acids through the plasma membrane !1[validated, MUID:97344270] !$#note permease GAP1 activity is regulated according to nitrogen !1source, activity being high on urea and low on glutamate; !1this regulation is due to differential protein sorting from !1the Golgi complex to either the plasma membrane or the !1vacuole !$#note citrulline transport is mediated exclusively by permease !1GAP1 which permits to specifically measure activity of this !1transport protein CLASSIFICATION #superfamily arginine permease KEYWORDS amino acid transport; glycoprotein; membrane protein SUMMARY #length 602 #molecular-weight 65655 #checksum 5058 SEQUENCE /// ENTRY A64647 #type complete TITLE amino acid permease (rocE) - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A64647 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession A64647 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-519 ##label TOM !'##cross-references GB:AE000610; GB:AE000511; NID:g2314160; !1PIDN:AAD08062.1; PID:g2314162; TIGR:HP1017 CLASSIFICATION #superfamily arginine permease KEYWORDS amino acid transport; glycoprotein; transmembrane protein SUMMARY #length 519 #molecular-weight 57876 #checksum 6982 SEQUENCE /// ENTRY C64984 #type complete TITLE lysine-specific permease - Escherichia coli (strain K-12) ALTERNATE_NAMES lysine transport protein ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS C64984; A41871; S24560 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64984 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-489 ##label BLAT !'##cross-references GB:AE000305; GB:U00096; NID:g1788479; !1PIDN:AAC75217.1; PID:g1788480; UWGP:b2156 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A41871 !$#authors Steffes, C.; Ellis, J.; Wu, J.; Rosen, B.P. !$#journal J. Bacteriol. (1992) 174:3242-3249 !$#title The lysP gene encodes the lysine-specific permease. !$#cross-references MUID:92250419; PMID:1315732 !$#accession A41871 !'##status preliminary !'##molecule_type DNA !'##residues 1-73,'R',75-489 ##label STE !'##cross-references GB:M89774 REFERENCE S24560 !$#authors Rosen, B.P. !$#submission submitted to the EMBL Data Library, November 1991 !$#accession S24560 !'##status preliminary !'##molecule_type DNA !'##residues 1-73,'R',75-346,'K',348,'AVC',352-489 ##label ROS !'##cross-references EMBL:X65029 GENETICS !$#gene lysP CLASSIFICATION #superfamily arginine permease KEYWORDS amino acid transport; glycoprotein; transmembrane protein SUMMARY #length 489 #molecular-weight 53575 #checksum 9158 SEQUENCE /// ENTRY S33212 #type complete TITLE INDA1 protein - fungus (Trichoderma harzianum) ORGANISM #formal_name Trichoderma harzianum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S33212 REFERENCE S33212 !$#authors Vasseur, V.V.; van Montagu, M.M.; Goldman, G.G.H. !$#submission submitted to the EMBL Data Library, April 1993 !$#description Molecular characterization of mycoparasitic-related genes of !1Trichoderma harzianum: cloning and sequencing of an amino !1acid transporter gene induced during mycoparasitism. !$#accession S33212 !'##status preliminary !'##molecule_type DNA !'##residues 1-573 ##label VAS !'##cross-references EMBL:Z22594; NID:g296569; PIDN:CAA80308.1; !1PID:g296570 CLASSIFICATION #superfamily arginine permease KEYWORDS amino acid transport; glycoprotein; transmembrane protein SUMMARY #length 573 #molecular-weight 62849 #checksum 4058 SEQUENCE /// ENTRY A64822 #type complete TITLE probable bacitracin transport permease ybjG - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 28-Jan-2000 #sequence_revision 28-Jan-2000 #text_change 01-Mar-2002 ACCESSIONS A64822 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64822 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-198 ##label BLAT !'##cross-references GB:AE000186; GB:U00096; NID:g1787058; !1PIDN:AAC73928.1; PID:g1787064; UWGP:b0841 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ybjG CLASSIFICATION #superfamily bacitracin transport permease; !1glucose-6-phosphatase catalytic domain homology KEYWORDS antibiotic resistance; transmembrane protein FEATURE !$34-50 #domain transmembrane #status predicted #label TM1\ !$51-160 #domain glucose-6-phosphatase catalytic domain !8homology #label GPH\ !$56-72 #domain transmembrane #status predicted #label TM2\ !$128-144 #domain transmembrane #status predicted #label TM3\ !$151-167 #domain transmembrane #status predicted #label TM4 SUMMARY #length 198 #molecular-weight 22398 #checksum 6925 SEQUENCE /// ENTRY T31684 #type complete TITLE probable bacitracin transport permease bcrC protein - Bacillus licheniformis ORGANISM #formal_name Bacillus licheniformis DATE 28-Jan-2000 #sequence_revision 28-Jan-2000 #text_change 21-Jul-2000 ACCESSIONS T31684; S77629 REFERENCE Z21058 !$#authors Konz, D.; Klens, A.; Schorgendorfer, K.; Marahiel, M.A. !$#journal Chem. Biol. (1997) 4:927-937 !$#title The bacitracin biosynthesis operon of Bacillus licheniformis !1ATCC 10716: molecular characterization of three !1multi-modular peptide synthetases. !$#cross-references MUID:98089193; PMID:9427658 !$#accession T31684 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-203 ##label KON !'##cross-references EMBL:AF007865; NID:g4464275; PID:g4464280; !1PIDN:AAD21215.1 REFERENCE S77627 !$#authors Podlesek, Z.; Comino, A.; Herzog-Velikonja, B.; Zgur-Bertok, !1D.; Komel, R.; Grabnar, M. !$#journal Mol. Microbiol. (1995) 16:969-976 !$#title Bacillus licheniformis bacitracin-resistance ABC !1transporter: relationship to mammalian multidrug resistance. !$#cross-references MUID:96059642; PMID:7476193 !$#accession S77629 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-203 ##label POD !'##cross-references EMBL:L20573; NID:g466477; PIDN:AAA99503.1; !1PID:g466478 !'##experimental_source strain ATCC 9945A !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1993 GENETICS !$#gene bcrC FUNCTION !$#description may function as a membrane component of bacitracin transport !1permease CLASSIFICATION #superfamily bacitracin transport permease; !1glucose-6-phosphatase catalytic domain homology KEYWORDS antibiotic resistance; transmembrane protein FEATURE !$52-161 #domain glucose-6-phosphatase catalytic domain !8homology #label GPH SUMMARY #length 203 #molecular-weight 23274 #checksum 1539 SEQUENCE /// ENTRY D70064 #type complete TITLE bacitracin transport permease homolog ywoA - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 28-Jan-2000 #sequence_revision 28-Jan-2000 #text_change 16-Jun-2000 ACCESSIONS D70064 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D70064 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-193 ##label KUN !'##cross-references GB:Z99122; GB:AL009126; NID:g2636029; !1PIDN:CAB15670.1; PID:g2636178 !'##experimental_source strain 168 GENETICS !$#gene ywoA CLASSIFICATION #superfamily bacitracin transport permease; !1glucose-6-phosphatase catalytic domain homology KEYWORDS antibiotic resistance; transmembrane protein FEATURE !$47-155 #domain glucose-6-phosphatase catalytic domain !8homology #label GPH SUMMARY #length 193 #molecular-weight 21722 #checksum 5248 SEQUENCE /// ENTRY T29447 #type complete TITLE probable bacitracin transport permease - Streptomyces coelicolor ORGANISM #formal_name Streptomyces coelicolor DATE 28-Jan-2000 #sequence_revision 28-Jan-2000 #text_change 16-Jun-2000 ACCESSIONS T29447 REFERENCE Z20619 !$#authors Parkhill, J.; Barrell, B.G.; Rajandream, M.A. !$#submission submitted to the EMBL Data Library, July 1998 !$#accession T29447 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-201 ##label PAR !'##cross-references EMBL:AL031155; PIDN:CAA20087.1 GENETICS !$#note SC3A7.24c CLASSIFICATION #superfamily bacitracin transport permease; !1glucose-6-phosphatase catalytic domain homology KEYWORDS antibiotic resistance; transmembrane protein FEATURE !$57-170 #domain glucose-6-phosphatase catalytic domain !8homology #label GPH SUMMARY #length 201 #molecular-weight 21016 #checksum 6917 SEQUENCE /// ENTRY D69206 #type complete TITLE conserved hypothetical protein MTH798 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 28-Jan-2000 #sequence_revision 28-Jan-2000 #text_change 03-Mar-2000 ACCESSIONS D69206 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession D69206 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-186 ##label MTH !'##cross-references GB:AE000858; GB:AE000666; NID:g2621885; !1PIDN:AAB85298.1; PID:g2621888 !'##experimental_source strain Delta H GENETICS !$#gene MTH798 CLASSIFICATION #superfamily bacitracin transport permease; !1glucose-6-phosphatase catalytic domain homology KEYWORDS antibiotic resistance; transmembrane protein FEATURE !$55-161 #domain glucose-6-phosphatase catalytic domain !8homology #label GPH SUMMARY #length 186 #molecular-weight 20561 #checksum 3126 SEQUENCE /// ENTRY GRBYCP #type complete TITLE cytosine/purine transport protein - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES cytosine/purine permease; protein YER056c ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Dec-1992 #sequence_revision 19-May-1995 #text_change 05-Nov-1999 ACCESSIONS S50559; S20153 REFERENCE S50557 !$#authors Dietrich, F.S. !$#submission submitted to the EMBL Data Library, December 1994 !$#description The sequence of S. cerevisiae lambda clones 6592, 4678, !14742, and 3612. !$#accession S50559 !'##molecule_type DNA !'##residues 1-533 ##label DIE !'##cross-references EMBL:U18813; NID:g1381127; PIDN:AAB64592.1; !1PID:g603292; GSPDB:GN00005; MIPS:YER056c !'##experimental_source strain S288c (AB972) REFERENCE S20153 !$#authors Weber, E.; Rodriguez, C.; Chevallier, M.R.; Jund, R. !$#journal Mol. Microbiol. (1990) 4:585-596 !$#title The purine-cytosine permease gene of Saccharomyces !1cerevisiae: primary structure and deduced protein sequence !1of the FCY2 gene product. !$#cross-references MUID:90279501; PMID:2191181 !$#accession S20153 !'##molecule_type DNA !'##residues 1-191,'M',193-260,'G',262-533 ##label WEB !'##cross-references EMBL:X51751; NID:g3699; PIDN:CAA36040.1; PID:g3700 !'##experimental_source strain FL100 GENETICS !$#gene SGD:FCY2; MIPS:YER056c !'##cross-references SGD:S0000858; MIPS:YER056c !$#map_position 5R CLASSIFICATION #superfamily cytosine/purine transport protein KEYWORDS glycoprotein; transmembrane protein FEATURE !$99-119 #domain transmembrane #status predicted #label TM1\ !$122-142 #domain transmembrane #status predicted #label TM2\ !$143-198 #domain extracellular #status predicted #label EXT\ !$199-221 #domain transmembrane #status predicted #label TM3\ !$257-277 #domain transmembrane #status predicted #label TM4\ !$301-320 #domain transmembrane #status predicted #label TM5\ !$345-368 #domain transmembrane #status predicted #label TM6\ !$398-419 #domain transmembrane #status predicted #label TM7\ !$466-485 #domain transmembrane #status predicted #label TM8\ !$160,181 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 533 #molecular-weight 58201 #checksum 5327 SEQUENCE /// ENTRY GRECY #type complete TITLE tyrosine-specific transport protein - Escherichia coli (strain K-12) ALTERNATE_NAMES tyrosine permease ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS C64954; JS0146 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64954 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-403 ##label BLAT !'##cross-references GB:AE000284; GB:U00096; NID:g1788214; !1PIDN:AAC74977.1; PID:g1788218; UWGP:b1907 !'##experimental_source strain K-12, substrain MG1655 REFERENCE JS0146 !$#authors Wookey, P.J.; Pittard, A.J. !$#journal J. Bacteriol. (1988) 170:4946-4949 !$#title DNA sequence of the gene (tyrP) encoding the !1tyrosine-specific transport system of Escherichia coli. !$#cross-references MUID:89008121; PMID:3049553 !$#accession JS0146 !'##molecule_type DNA !'##residues 1-130,'RRVAWL',136-221,'ECD',225-403 ##label WOO !'##cross-references GB:M23240; NID:g148088; PIDN:AAA24705.1; !1PID:g148089 GENETICS !$#gene tyrP !$#map_position 42 min !$#start_codon GTG FUNCTION !$#description involved in transporting tyrosine across the cytoplasmic !1membrane !$#note repressed by tyrosine and induced by phenylalanine under the !1control of regulatory protein tyrR CLASSIFICATION #superfamily tyrosine-specific transport protein KEYWORDS amino acid transport; inner membrane; transmembrane protein; !1transport protein FEATURE !$8-24 #domain transmembrane #status predicted #label TM1\ !$37-53 #domain transmembrane #status predicted #label TM2\ !$122-138 #domain transmembrane #status predicted #label TM3\ !$149-165 #domain transmembrane #status predicted #label TM4\ !$216-232 #domain transmembrane #status predicted #label TM5\ !$277-293 #domain transmembrane #status predicted #label TM6\ !$335-351 #domain transmembrane #status predicted #label TM7\ !$378-394 #domain transmembrane #status predicted #label TM8 SUMMARY #length 403 #molecular-weight 42819 #checksum 8497 SEQUENCE /// ENTRY S54140 #type complete TITLE D-serine permease - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 08-Jul-1995 #sequence_revision 19-Oct-1995 #text_change 01-Mar-2002 ACCESSIONS S54140; A26949; B65010; S15281 REFERENCE S54140 !$#authors Brannigan, J.A. !$#submission submitted to the EMBL Data Library, April 1995 !$#description DNA sequence and gene organisation of hte E.coli dsd operon. !$#accession S54140 !'##molecule_type DNA !'##residues 1-445 ##label BRA !'##cross-references EMBL:X86379; NID:g784979; PIDN:CAA60138.1; !1PID:g784980 REFERENCE A26949 !$#authors Bornstein-Forst, S.M.; McFall, E.; Palchaudhuri, S. !$#journal J. Bacteriol. (1987) 169:1056-1060 !$#title In vivo D-serine deaminase transcription start sites in !1wild-type Escherichia coli and in dsdA promoter mutants. !$#cross-references MUID:87137257; PMID:3029015 !$#accession A26949 !'##molecule_type DNA !'##residues 338-445 ##label BOR !'##cross-references GB:J01603; GB:M15237; GB:M22415; NID:g145804; !1PIDN:AAA87974.1; PID:g145805 !'##note the authors translated the codon GCC for residue 9 as Val, TGG !1for residue 10 as Tyr, TCC for residue 22 as Leu, GCT for !1residue 23 as Pro, GCA for residue 35 as Arg, GAC for !1residue 65 as Thr, TGG for residue 69 as Tyr, and AAG for !1residue 72 as Asn REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65010 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-445 ##label BLAT !'##cross-references GB:AE000324; GB:U00096; NID:g1788694; !1PIDN:AAC75424.1; PID:g1788707; UWGP:b2365 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene dsdX; dsdC !$#map_position 51 min CLASSIFICATION #superfamily D-serine permease KEYWORDS D-serine catabolism SUMMARY #length 445 #molecular-weight 47163 #checksum 6906 SEQUENCE /// ENTRY YOECNQ #type complete TITLE sodium-glutamate symport carrier protein - Escherichia coli (strain K-12) ALTERNATE_NAMES glutamate permease ORGANISM #formal_name Escherichia coli DATE 30-Jun-1991 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS G65166; A36524; S14031; JQ0489 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65166 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-401 ##label BLAT !'##cross-references GB:AE000442; GB:U00096; NID:g2367253; !1PIDN:AAC76677.1; PID:g1790085; UWGP:b3653 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A36524 !$#authors Deguchi, Y.; Yamato, I.; Anraku, Y. !$#journal J. Biol. Chem. (1990) 265:21704-21708 !$#title Nucleotide sequence of gltS, the Na(+)/glutamate symport !1carrier gene of Escherichia coli B. !$#cross-references MUID:91072371; PMID:2254324 !$#accession A36524 !'##molecule_type DNA !'##residues 1-377,'S',379-401 ##label DEG !'##cross-references GB:D00626; NID:g216540; PIDN:BAA00517.1; !1PID:g216541 !'##experimental_source strain B29-78 REFERENCE S14031 !$#authors Kalman, M.; Gentry, D.R.; Cashel, M. !$#journal Mol. Gen. Genet. (1991) 225:379-386 !$#title Characterization of the Escherichia coli K12 gltS glutamate !1permease gene. !$#cross-references MUID:91203811; PMID:2017136 !$#accession S14031 !'##molecule_type DNA !'##residues 1-401 ##label KAL !'##cross-references EMBL:X17499; NID:g41592; PIDN:CAA35540.1; !1PID:g41593 GENETICS !$#gene gltS !$#map_position 82 min CLASSIFICATION #superfamily sodium-glutamate symport carrier protein KEYWORDS glutamate transport; transmembrane protein SUMMARY #length 401 #molecular-weight 42425 #checksum 7766 SEQUENCE /// ENTRY MMEBMT #type complete TITLE histidine permease protein M - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 24-Sep-1999 ACCESSIONS A03409 REFERENCE A94697 !$#authors Higgins, C.F.; Haag, P.D.; Nikaido, K.; Ardeshir, F.; !1Garcia, G.; Ames, G.F.L. !$#journal Nature (1982) 298:723-727 !$#title Complete nucleotide sequence and identification of membrane !1components of the histidine transport operon of Salmonella !1typhimurium. !$#cross-references MUID:82272316; PMID:7050725 !$#accession A03409 !'##molecule_type DNA !'##residues 1-235 ##label HIG !'##cross-references GB:V01373; NID:g47730; PIDN:CAA24661.1; !1PID:g1000516 !'##note this protein is one of the membrane-bound components of the !1high-affinity histidine permease, a !1binding-protein-dependent transport system; the other !1components are proteins Q, P, and J; the M, Q, and P !1proteins are also essential for an arginine transport system !1that requires lysine-arginine-ornithine-binding protein !1(LAO) GENETICS !$#gene hisM !$#map_position 48.5 !$#start_codon GTG CLASSIFICATION #superfamily histidine permease protein M KEYWORDS transmembrane protein SUMMARY #length 235 #molecular-weight 26453 #checksum 9922 SEQUENCE /// ENTRY MMEBQT #type complete TITLE histidine permease protein Q - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 24-Sep-1999 ACCESSIONS A03410 REFERENCE A94697 !$#authors Higgins, C.F.; Haag, P.D.; Nikaido, K.; Ardeshir, F.; !1Garcia, G.; Ames, G.F.L. !$#journal Nature (1982) 298:723-727 !$#title Complete nucleotide sequence and identification of membrane !1components of the histidine transport operon of Salmonella !1typhimurium. !$#cross-references MUID:82272316; PMID:7050725 !$#accession A03410 !'##molecule_type DNA !'##residues 1-228 ##label HIG !'##cross-references GB:V01373; NID:g47730; PIDN:CAA24660.1; PID:g47732 !'##note this protein is one of the membrane-bound components of the !1high-affinity histidine permease, a !1binding-protein-dependent transport system; the other !1components are proteins M, P, and J; the Q, M, and P !1proteins are also essential for an arginine transport system !1that requires lysine-arginine-ornithine-binding protein !1(LAO) GENETICS !$#gene hisQ !$#map_position 48.5 CLASSIFICATION #superfamily histidine permease protein M KEYWORDS transmembrane protein SUMMARY #length 228 #molecular-weight 24620 #checksum 7028 SEQUENCE /// ENTRY QRECGP #type complete TITLE glutamine transport system permease protein glnP - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 01-Mar-2002 ACCESSIONS S03182; B64818 REFERENCE S03181 !$#authors Nohno, T.; Saito, T.; Hong, J. !$#journal Mol. Gen. Genet. (1986) 205:260-269 !$#title Cloning and complete nucleotide sequence of the Escherichia !1coli glutamine permease operon (glnHPQ). !$#cross-references MUID:87115160; PMID:3027504 !$#accession S03182 !'##molecule_type DNA !'##residues 1-219 ##label NOH !'##cross-references EMBL:X14180; NID:g41568; PIDN:CAA32383.1; !1PID:g41572 !'##experimental_source strain K-12, substrain PSM2 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64818 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-219 ##label BLAT !'##cross-references GB:AE000183; GB:U00096; NID:g1787025; !1PIDN:AAC73897.1; PID:g1787030; UWGP:b0810 !'##experimental_source strain K-12, substrain MG1655 COMMENT This protein is the binding protein component of the !1glutamine permease system, a highly specific binding !1protein-dependent transport system for glutamine. GENETICS !$#gene glnP !$#map_position 18 min FUNCTION !$#description translocates substrate across the membrane !$#note induction by glutamine lack CLASSIFICATION #superfamily histidine permease protein M KEYWORDS binding protein-dependent transport system; glutamine !1transport; transmembrane protein FEATURE !$23-39 #domain transmembrane #status predicted #label TM1\ !$46-62 #domain transmembrane #status predicted #label TM2\ !$66-82 #domain transmembrane #status predicted #label TM3\ !$155-171 #domain transmembrane #status predicted #label TM4\ !$193-209 #domain transmembrane #status predicted #label TM5 SUMMARY #length 219 #molecular-weight 24364 #checksum 6203 SEQUENCE /// ENTRY GRECNK #type complete TITLE nitrite extrusion protein - Escherichia coli (strain K-12) ALTERNATE_NAMES nitrite facilitator ORGANISM #formal_name Escherichia coli DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 01-Mar-2002 ACCESSIONS S05239; D64869 REFERENCE S05239 !$#authors Noji, S.; Nohno, T.; Saito, T.; Taniguchi, S. !$#journal FEBS Lett. (1989) 252:139-143 !$#title The narK gene product participates in nitrate transport !1induced in Escherichia coli nitrate-respiring cells. !$#cross-references MUID:89338707; PMID:2668029 !$#accession S05239 !'##molecule_type DNA !'##residues 1-463 ##label NOJ !'##cross-references EMBL:X15996; NID:g42089; PIDN:CAA34126.1; !1PID:g42091 !'##experimental_source strain K-12 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64869 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-463 ##label BLAT !'##cross-references GB:AE000220; GB:U00096; NID:g1787467; !1PIDN:AAC74307.1; PID:g1787475; UWGP:b1223 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene narK !$#map_position 27 min FUNCTION !$#description promotes a rapid rate of anaerobic nitrate reduction and the !1continuous excretion of the nitrite formed !$#note induction by nitrate CLASSIFICATION #superfamily nitrate transport protein narK KEYWORDS nitrate assimilation; nitrate transport; transmembrane !1protein FEATURE !$44-60 #domain transmembrane #status predicted #label TM1\ !$74-90 #domain transmembrane #status predicted #label TM2\ !$107-123 #domain transmembrane #status predicted #label TM3\ !$132-148 #domain transmembrane #status predicted #label TM4\ !$180-196 #domain transmembrane #status predicted #label TM5\ !$218-234 #domain transmembrane #status predicted #label TM6\ !$256-272 #domain transmembrane #status predicted #label TM7\ !$320-336 #domain transmembrane #status predicted #label TM8\ !$348-364 #domain transmembrane #status predicted #label TM9\ !$405-421 #domain transmembrane #status predicted #label TM10\ !$436-452 #domain transmembrane #status predicted #label TM11 SUMMARY #length 463 #molecular-weight 49693 #checksum 4671 SEQUENCE /// ENTRY QREBOB #type complete TITLE oligopeptide transport system permease protein oppB - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS B29333 REFERENCE A29333 !$#authors Hiles, I.D.; Gallagher, M.P.; Jamieson, D.J.; Higgins, C.F. !$#journal J. Mol. Biol. (1987) 195:125-142 !$#title Molecular characterization of the oligopeptide permease of !1Salmonella typhimurium. !$#cross-references MUID:88011222; PMID:2821267 !$#accession B29333 !'##molecule_type DNA !'##residues 1-306 ##label HIL !'##cross-references GB:X05491; NID:g47801; PIDN:CAA29040.1; PID:g47803 COMMENT This is one of the highly hydrophobic membrane-associated !1components of the periplasmic binding protein-dependent !1transport system for peptides that are two to five amino !1acids long. This transport system is of importance to the !1nutrition of the organism; it is also essential for !1recycling of cell wall peptides. GENETICS !$#gene oppB !$#map_position 34 min FUNCTION !$#description probably responsible for mediating passage of peptides !1across the cytoplasmic membrane CLASSIFICATION #superfamily oligopeptide permease protein oppB KEYWORDS binding protein-dependent transport system; oligopeptide !1transport; transmembrane protein FEATURE !$9-25 #domain transmembrane #status predicted #label TM1\ !$105-121 #domain transmembrane #status predicted #label TM2\ !$140-156 #domain transmembrane #status predicted #label TM3\ !$173-189 #domain transmembrane #status predicted #label TM4\ !$228-244 #domain transmembrane #status predicted #label TM5\ !$273-289 #domain transmembrane #status predicted #label TM6 SUMMARY #length 306 #molecular-weight 33420 #checksum 4920 SEQUENCE /// ENTRY QREBOC #type complete TITLE oligopeptide transport system permease protein oppC - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS C29333 REFERENCE A29333 !$#authors Hiles, I.D.; Gallagher, M.P.; Jamieson, D.J.; Higgins, C.F. !$#journal J. Mol. Biol. (1987) 195:125-142 !$#title Molecular characterization of the oligopeptide permease of !1Salmonella typhimurium. !$#cross-references MUID:88011222; PMID:2821267 !$#accession C29333 !'##molecule_type DNA !'##residues 1-302 ##label HIL !'##cross-references GB:X05491; NID:g47801; PIDN:CAA29041.1; PID:g47804 COMMENT This is one of the highly hydrophobic membrane-associated !1components of the periplasmic binding protein-dependent !1transport system for peptides that are two to five amino !1acids long. This transport system is of importance to the !1nutrition of the organism; it is also essential for !1recycling of cell wall peptides. GENETICS !$#gene oppC !$#map_position 34 min FUNCTION !$#description probably responsible for mediating passage of peptides !1across the cytoplasmic membrane CLASSIFICATION #superfamily oligopeptide permease protein oppB KEYWORDS binding protein-dependent transport system; oligopeptide !1transport; transmembrane protein FEATURE !$39-55 #domain transmembrane #status predicted #label TM1\ !$103-119 #domain transmembrane #status predicted #label TM2\ !$153-169 #domain transmembrane #status predicted #label TM3\ !$218-234 #domain transmembrane #status predicted #label TM4\ !$270-286 #domain transmembrane #status predicted #label TM5 SUMMARY #length 302 #molecular-weight 33090 #checksum 2675 SEQUENCE /// ENTRY S27616 #type complete TITLE probable glucarate transporter - Pseudomonas putida ORGANISM #formal_name Pseudomonas putida DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S27616 REFERENCE S27612 !$#authors Burlingame, R.P.; Maruya, A.; Ally, A.; Ally, D.; Backman, !1K.C. !$#submission submitted to the EMBL Data Library, June 1992 !$#description Nucleotide sequences of hydroxyproline-specific !1alpha-ketoglutarate semialdehyde dehydrogenase genes from !1two strains of pseudomonas putida. !$#accession S27616 !'##status preliminary !'##molecule_type DNA !'##residues 1-456 ##label BUR !'##cross-references EMBL:M69160; NID:g151313; PIDN:AAA25867.1; !1PID:g151314 CLASSIFICATION #superfamily hexuronate transporter KEYWORDS membrane protein SUMMARY #length 456 #molecular-weight 49779 #checksum 5657 SEQUENCE /// ENTRY H69752 #type complete TITLE probalble glucarate transporter - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS H69752 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69752 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-455 ##label KUN !'##cross-references GB:Z99105; GB:AL009126; NID:g2632457; !1PIDN:CAB12042.1; PID:g2632534 !'##experimental_source strain 168 GENETICS !$#gene ycbE CLASSIFICATION #superfamily hexuronate transporter SUMMARY #length 455 #molecular-weight 49253 #checksum 2897 SEQUENCE /// ENTRY S65982 #type complete TITLE transport protein homolog yybO - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S65982; B70088 REFERENCE S65967 !$#authors Ogasawara, N.; Nakai, S.; Yoshikawa, H. !$#journal DNA Res. (1994) 1:1-14 !$#title Systematic sequencing of the 180 kilobase region of the !1Bacillus subtilis chromosome containing the replication !1origin. !$#cross-references MUID:96051385; PMID:7584024 !$#accession S65982 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-435 ##label OGA !'##cross-references EMBL:D26185; NID:g467326; PIDN:BAA05188.1; !1PID:g467342 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1993 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B70088 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-435 ##label KUN !'##cross-references GB:Z99124; GB:AL009126; NID:g2636442; !1PIDN:CAB16094.1; PID:g2636604 !'##experimental_source strain 168 GENETICS !$#gene yybO CLASSIFICATION #superfamily hexuronate transporter SUMMARY #length 435 #molecular-weight 48247 #checksum 8779 SEQUENCE /// ENTRY D65171 #type complete TITLE hypothetical 48.8 kD protein in ibpA-gyrB intergenic region - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS D65171 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65171 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-445 ##label BLAT !'##cross-references GB:AE000446; GB:U00096; NID:g2367261; !1PIDN:AAC76714.1; PID:g1790126; UWGP:b3691 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yidT CLASSIFICATION #superfamily hexuronate transporter SUMMARY #length 445 #molecular-weight 48793 #checksum 5051 SEQUENCE /// ENTRY B65098 #type complete TITLE hexuronate transporter - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS B65098 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65098 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-472 ##label BLAT !'##cross-references GB:AE000391; GB:U00096; NID:g2367191; !1PIDN:AAC76128.1; PID:g2367193; UWGP:b3093 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene exuT CLASSIFICATION #superfamily hexuronate transporter SUMMARY #length 472 #molecular-weight 51571 #checksum 7204 SEQUENCE /// ENTRY F65250 #type complete TITLE hypothetical 49.4 kD protein in tsr-mdoB intergenic region - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS F65250; S56582 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65250 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-453 ##label BLAT !'##cross-references GB:AE000506; GB:U00096; NID:g2367377; !1PIDN:AAC77312.1; PID:g2367379; UWGP:b4356 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56582 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 262-453 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97253.1; !1PID:g537198 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 CLASSIFICATION #superfamily hexuronate transporter SUMMARY #length 453 #molecular-weight 49440 #checksum 2337 SEQUENCE /// ENTRY A69853 #type complete TITLE hexuronate transporter homolog yjmG - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A69853 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69853 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-422 ##label KUN !'##cross-references GB:Z99110; GB:AL009126; NID:g2633472; !1PIDN:CAB13093.1; PID:g2633590 !'##experimental_source strain 168 GENETICS !$#gene yjmG CLASSIFICATION #superfamily hexuronate transporter SUMMARY #length 422 #molecular-weight 45313 #checksum 8902 SEQUENCE /// ENTRY G1YC #type complete TITLE gene 1 protein - Synechococcus sp. (strain PCC 6301) ORGANISM #formal_name Synechococcus sp. DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jul-1999 ACCESSIONS S10825 REFERENCE S07286 !$#authors Cozens, A.L.; Walker, J.E. !$#journal J. Mol. Biol. (1987) 194:359-383 !$#title The organization and sequence of the genes for ATP synthase !1subunits in the cyanobacterium Synechococcus 6301. Support !1for an endosymbiotic origin of chloroplasts. !$#cross-references MUID:87311713; PMID:3041005 !$#accession S10825 !'##molecule_type DNA !'##residues 1-118 ##label COZ !'##cross-references EMBL:X05302; NID:g48009; PIDN:CAA28922.1; !1PID:g48011 CLASSIFICATION #superfamily gene 1 protein KEYWORDS membrane protein SUMMARY #length 118 #molecular-weight 13455 #checksum 5424 SEQUENCE /// ENTRY BVECCZ #type complete TITLE probable sulfate transport protein CysZ - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 30-Sep-1997 #text_change 01-Mar-2002 ACCESSIONS D65015; E28181; S03093 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65015 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-253 ##label BLAT !'##cross-references GB:AE000329; GB:U00096; NID:g2367137; !1PIDN:AAC75466.1; PID:g1788753; UWGP:b2413 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A28181 !$#authors Byrne, C.R.; Monroe, R.S.; Ward, K.A.; Kredich, N.M. !$#journal J. Bacteriol. (1988) 170:3150-3157 !$#title DNA sequences of the cysK regions of Salmonella typhimurium !1and Escherichia coli and linkage of the cysK regions to !1ptsH. !$#cross-references MUID:88257033; PMID:3290198 !$#accession E28181 !'##molecule_type DNA !'##residues 58-253 ##label BYR !'##cross-references GB:M21451; NID:g145684; PIDN:AAA23653.1; !1PID:g145685 REFERENCE S03093 !$#authors Levy, S.; Danchin, A. !$#journal Mol. Microbiol. (1988) 2:777-783 !$#title Phylogeny of metabolic pathways: O-acetylserine !1sulphydrylase A is homologous to the tryptophan synthase !1beta subunit. !$#cross-references MUID:89096499; PMID:3062311 !$#accession S03093 !'##status preliminary !'##molecule_type DNA !'##residues 58-253 ##label LEV !'##cross-references EMBL:X12615; NID:g41199; PIDN:CAA31136.1; !1PID:g809674 GENETICS !$#gene cysZ !$#map_position 52 min FUNCTION !$#description probably involved in sulfate transport !$#pathway cysteine biosynthesis CLASSIFICATION #superfamily cysZ protein KEYWORDS cysteine biosynthesis; membrane protein; sulfate transport SUMMARY #length 253 #molecular-weight 29305 #checksum 2505 SEQUENCE /// ENTRY BVEBCZ #type complete TITLE cysZ protein - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jul-1999 ACCESSIONS A28181 REFERENCE A28181 !$#authors Byrne, C.R.; Monroe, R.S.; Ward, K.A.; Kredich, N.M. !$#journal J. Bacteriol. (1988) 170:3150-3157 !$#title DNA sequences of the cysK regions of Salmonella typhimurium !1and Escherichia coli and linkage of the cysK regions to !1ptsH. !$#cross-references MUID:88257033; PMID:3290198 !$#accession A28181 !'##molecule_type DNA !'##residues 1-290 ##label BYR !'##cross-references GB:M21450; NID:g153933; PIDN:AAA27050.1; !1PID:g153934 COMMENT This protein is probably involved in sulfate transport. GENETICS !$#gene cysZ !$#map_position 49 min CLASSIFICATION #superfamily cysZ protein KEYWORDS cysteine biosynthesis; membrane protein; sulfate transport SUMMARY #length 290 #molecular-weight 33455 #checksum 225 SEQUENCE /// ENTRY QRECD3 #type complete TITLE citrate-dependent iron transport protein fecB precursor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS S56515; D65242; JS0112 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56515 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-302 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97186.1; !1PID:g537131 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65242 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-302 ##label BLAT !'##cross-references GB:AE000499; GB:U00096; NID:g1790732; !1PIDN:AAC77246.1; PID:g1790742; UWGP:b4290 !'##experimental_source strain K-12, substrain MG1655 REFERENCE PS0029 !$#authors Staudenmaier, H.; Van Hove, B.; Yaraghi, Z.; Braun, V. !$#journal J. Bacteriol. (1989) 171:2626-2633 !$#title Nucleotide sequences of the fecBCDE genes and locations of !1the proteins suggest a periplasmic-binding-protein-dependent !1transport mechanism for iron(III) dicitrate in Escherichia !1coli. !$#cross-references MUID:89213950; PMID:2651410 !$#accession JS0112 !'##molecule_type DNA !'##residues 3-24,'M',26-58,'S',60-302 ##label STA !'##cross-references GB:M26397; NID:g145923; PIDN:AAA23762.1; !1PID:g145925 !'##experimental_source strain K12 COMMENT The sequence from strain B differs from that shown in having !1Val-10 and Thr-25. COMMENT This protein is one of five, encoded by the fec operon, !1constituting a citrate-dependent iron(III) transport system. GENETICS !$#gene fecB !$#map_position 7 min !$#start_codon GTG CLASSIFICATION #superfamily ferrichrome-iron transport protein fecB KEYWORDS iron transport FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-302 #product iron(III) dicitrate transport protein fecB !8#status predicted #label MAT SUMMARY #length 302 #molecular-weight 33390 #checksum 4739 SEQUENCE /// ENTRY QRECFD #type complete TITLE ferrichrome-iron transport protein fhuD precursor - Escherichia coli (strain K-12) ALTERNATE_NAMES ferrichrome-binding periplasmic protein ORGANISM #formal_name Escherichia coli DATE 30-Sep-1988 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS H64738; B26977; S07037; S45221; S57324 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64738 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-296 ##label BLAT !'##cross-references GB:AE000124; GB:U00096; NID:g1786339; !1PIDN:AAC73263.1; PID:g1786346; UWGP:b0152 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A30394 !$#authors Coulton, J.W.; Mason, P.; Allatt, D.D. !$#journal J. Bacteriol. (1987) 169:3844-3849 !$#title fhuC and fhuD genes for iron(III)-ferrichrome transport into !1Escherichia coli K-12. !$#cross-references MUID:87279948; PMID:3301821 !$#accession B26977 !'##molecule_type DNA !'##residues 1-153,'D',155-296 ##label COU !'##cross-references GB:D26562; NID:g473770; PIDN:BAA05600.1; !1PID:g473811 REFERENCE A32650 !$#authors Burkhardt, R.; Braun, V. !$#journal Mol. Gen. Genet. (1987) 209:49-55 !$#title Nucleotide sequence of the fhuC and fhuD genes involved in !1iron (III) hydroxamate transport: domains in FhuC homologous !1to ATP-binding proteins. !$#cross-references MUID:88038363; PMID:2823072 !$#accession S07037 !'##molecule_type DNA !'##residues 1-47,'V',49-296 ##label BUR !'##cross-references EMBL:X05810; NID:g41438; PIDN:CAA29255.1; !1PID:g41441 !'##note the authors translated the codon GTA for residue 48 as Leu !'##note it is uncertain whether Met-1 is the initiator or whether !1translation is initiated at 46-Val (GTG) REFERENCE S45181 !$#authors Fujita, N. !$#submission submitted to the EMBL Data Library, January 1994 !$#accession S45221 !'##molecule_type DNA !'##residues 1-153,'D',155-296 ##label FUJ !'##cross-references EMBL:D26562; NID:g473770; PIDN:BAA05600.1; !1PID:g473811 !'##experimental_source strain K-12, substrain W3110 REFERENCE S57324 !$#authors Rohrbach, M.R.; Paul, S.; Koester, W. !$#journal Mol. Gen. Genet. (1995) 248:33-42 !$#title In vivo reconstitution of an active siderophore transport !1system by a binding protein derivative lacking a signal !1sequence. !$#cross-references MUID:95379747; PMID:7651325 !$#accession S57324 !'##molecule_type protein !'##residues 32-39 ##label ROH COMMENT It is a soluble protein and may be exported into the !1periplasm. GENETICS !$#gene fhuD !$#map_position 4 min FUNCTION !$#description involved in the high-affinity transport of iron !1(III)-ferrichrome into the E. coli cell CLASSIFICATION #superfamily ferrichrome-iron transport protein fhuD KEYWORDS iron transport; membrane protein FEATURE !$1-30 #domain signal sequence #status predicted #label SIG\ !$31-296 #product ferrichrome-iron transport protein fhuD !8#status predicted #label MAT SUMMARY #length 296 #molecular-weight 32998 #checksum 5353 SEQUENCE /// ENTRY BYECPR #type complete TITLE phosphate-repressible phosphate-binding protein precursor [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 01-Mar-2002 ACCESSIONS A30277; A65176 REFERENCE A30277 !$#authors Surin, B.P.; Jans, D.A.; Fimmel, A.L.; Shaw, D.C.; Cox, !1G.B.; Rosenberg, H. !$#journal J. Bacteriol. (1984) 157:772-778 !$#title Structural gene for the phosphate-repressible !1phosphate-binding protein of Escherichia coli has its own !1promoter: complete nucleotide sequence of the phoS gene. !$#cross-references MUID:84135579; PMID:6321434 !$#accession A30277 !'##molecule_type DNA !'##residues 1-346 ##label SUR !'##cross-references GB:K01992; NID:g147255; PIDN:AAA24378.1; !1PID:g147256 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65176 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-346 ##label BLAT !'##cross-references GB:AE000449; GB:U00096; NID:g2367269; !1PIDN:AAC76751.1; PID:g2367271; UWGP:b3728 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A68487 !$#authors Wang, Z.; Luecke, H.; Quiocho, F.A. !$#submission submitted to the Brookhaven Protein Data Bank, August 1996 !$#cross-references PDB:1IXH !$#contents annotation; X-ray crystallography, 0.98 angstroms, residues !126-346 REFERENCE A67875 !$#authors Yao, N.; Choudhary, A.; Ledvina, P.S.; Quiocho, F.A. !$#submission submitted to the Brookhaven Protein Data Bank, November 1995 !$#cross-references PDB:2ABH !$#contents annotation; X-ray crystallography, 1.70 angstroms, residues !126-346 REFERENCE A51014 !$#authors Luecke, H.; Quiocho, F.A. !$#submission submitted to the Brookhaven Protein Data Bank, April 1992 !$#cross-references PDB:1ABH !$#contents annotation; X-ray crystallography, 1.7 angstroms, residues !126-110,'G',112-202,'E',204-346 REFERENCE A30645 !$#authors Luecke, H.; Quiocho, F.A. !$#journal Nature (1990) 347:402-406 !$#title High specificity of a phosphate transport protein determined !1by hydrogen bonds. !$#cross-references MUID:91015319; PMID:2215649 !$#contents annotation; X-ray crystallography, 1.7 angstroms COMMENT This protein is a component of the inducible, high-affinity, !1phosphate-specific transport (Pst) system. The Pst system is !1part of the phosphate regulon induced by phosphate !1starvation. GENETICS !$#gene pstS; phoS !$#map_position 84 min CLASSIFICATION #superfamily phosphate-repressible phosphate-binding protein KEYWORDS phosphate transport FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-346 #product phosphate-repressible phosphate-binding !8protein #status experimental #label MAT\ !$35,63,81,160,164, !$166 #binding_site phosphate (Thr, Ser, Asp, Arg, Ser, !8Thr) #status experimental SUMMARY #length 346 #molecular-weight 37024 #checksum 5310 SEQUENCE /// ENTRY C70473 #type complete TITLE phosphate-binding periplasmic protein - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C70473 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession C70473 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-337 ##label AQF !'##cross-references GB:AE000768; NID:g2984249; PIDN:AAC07783.1; !1PID:g2984256; GB:AE000657 !'##experimental_source strain VF5 GENETICS !$#gene pstS CLASSIFICATION #superfamily phosphate-repressible phosphate-binding protein SUMMARY #length 337 #molecular-weight 37798 #checksum 8760 SEQUENCE /// ENTRY S74423 #type complete TITLE phosphate-binding periplasmic protein pstS-1 - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein sll0680 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S74423 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74423 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-383 ##label KAN !'##cross-references EMBL:D64001; GB:AB001339; NID:g1001102; !1PIDN:BAA10341.1; PID:g1001197 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene pstS-1 CLASSIFICATION #superfamily phosphate-repressible phosphate-binding protein SUMMARY #length 383 #molecular-weight 40023 #checksum 6509 SEQUENCE /// ENTRY S74876 #type complete TITLE phosphate-binding periplasmic protein pstS-2 - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein slr1247 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S74876 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74876 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-333 ##label KAN !'##cross-references EMBL:D90909; GB:AB001339; NID:g1652844; !1PIDN:BAA17837.1; PID:g1652919 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene pstS-2 CLASSIFICATION #superfamily phosphate-repressible phosphate-binding protein SUMMARY #length 333 #molecular-weight 35289 #checksum 4605 SEQUENCE /// ENTRY F64426 #type complete TITLE phosphate-binding protein - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F64426 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession F64426 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-389 ##label BUL !'##cross-references GB:U67544; GB:L77117; NID:g1591671; !1PIDN:AAB99019.1; PID:g1591675; TIGR:MJ1015 GENETICS !$#map_position REV945831-944662 !$#start_codon TTG CLASSIFICATION #superfamily phosphate-repressible phosphate-binding protein SUMMARY #length 389 #molecular-weight 42413 #checksum 2761 SEQUENCE /// ENTRY F70584 #type complete TITLE phosphate specific transporter S precursor - Mycobacterium tuberculosis (strain H37RV) ALTERNATE_NAMES antigen b ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS F70584; JC5103; A42930; A49721; A45820 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession F70584 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-374 ##label COL !'##cross-references GB:Z95209; GB:AL123456; NID:g3261750; !1PIDN:CAB08484.1; PID:g2078049 !'##experimental_source strain H37Rv REFERENCE JC5100 !$#authors Braibant, M.; Lefevre, P.; de Wit, L.; Peirs, P.; Ooms, J.; !1Huygen, K.; Andersen, A.B.; Content, J. !$#journal Gene (1996) 176:171-176 !$#title A Mycobacterium tuberculosis gene cluster encoding proteins !1of a phosphate transporter homologous to the Escherichia !1coli Pst system. !$#cross-references MUID:97075926; PMID:8918249 !$#accession JC5103 !'##molecule_type DNA !'##residues 1-374 ##label BRA !'##cross-references GB:M30046; NID:g149987; PIDN:AAA25374.1; !1PID:g149988 !'##note neither the complete nucleic acid sequence nor the complete !1translation are shown !'##note the authors translated the initiation codon GTG for residue 1 !1as Met REFERENCE A42930 !$#authors Andersen, A.B.; Hansen, E.B. !$#journal Infect. Immun. (1989) 57:2481-2488 !$#title Structure and mapping of antigenic domains of protein !1antigen b, a 38,000-molecular-weight protein of !1Mycobacterium tuberculosis. !$#cross-references MUID:89307568; PMID:2545626 !$#accession A42930 !'##status preliminary !'##molecule_type DNA !'##residues 1-374 ##label AND1 !'##cross-references GB:M30046; NID:g149987; PIDN:AAA25374.1; !1PID:g149988 REFERENCE A49721 !$#authors Chang, Z.; Choudhary, A.; Lathigra, R.; Quiocho, F.A. !$#journal J. Biol. Chem. (1994) 269:1956-1958 !$#title The immunodominant 38-kDa lipoprotein antigen of !1Mycobacterium tuberculosis is a phosphate-binding protein. !$#cross-references MUID:94124544; PMID:8294447 !$#accession A49721 !'##molecule_type protein !'##residues 25-34 ##label CHA REFERENCE A45820 !$#authors Andersen, A.B.; Ljungqvist, L.; Olsen, M. !$#journal J. Gen. Microbiol. (1990) 136:477-480 !$#title Evidence that protein antigen b of Mycobacterium !1tuberculosis is involved in phosphate metabolism. !$#cross-references MUID:90362031; PMID:2118164 !$#accession A45820 !'##molecule_type protein !'##residues 'X',27-28,'X',30-34,'XX',37 ##label AND2 !'##note confirmed presence of normal signal and absence of lipoprotein !1attachment GENETICS !$#gene phoS1; pstS !$#start_codon GTG CLASSIFICATION #superfamily phosphate-repressible phosphate-binding protein KEYWORDS surface antigen FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-374 #product phosphate specific transporter S #status !8experimental #label MAT SUMMARY #length 374 #molecular-weight 38243 #checksum 7348 SEQUENCE /// ENTRY S39852 #type complete TITLE phosphate-binding protein, periplasmic - Synechococcus sp. ORGANISM #formal_name Synechococcus sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S39852; S33208 REFERENCE S39852 !$#authors Scanlan, D.J.; Mann, N.H.; Carr, N.G. !$#journal Mol. Microbiol. (1993) 10:181-191 !$#title The response of the picoplanktonic marine cyanobacterium !1Synechococcus species WH7803 to phosphate starvation !1involves a protein homologous to the periplasmic !1phosphate-binding protein of Escherichia coli. !$#cross-references MUID:95058176; PMID:7968514 !$#accession S39852 !'##status preliminary !'##molecule_type DNA !'##residues 1-326 ##label SCA !'##cross-references EMBL:X71359; NID:g296205; PIDN:CAA50495.1; !1PID:g296206 CLASSIFICATION #superfamily phosphate-repressible phosphate-binding protein SUMMARY #length 326 #molecular-weight 33758 #checksum 2468 SEQUENCE /// ENTRY I64120 #type complete TITLE phosphate-binding protein, phosphate-repressible - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS I64120 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession I64120 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-258 ##label TIGR !'##cross-references GB:U32818; GB:L42023; NID:g1574209; !1PIDN:AAC23028.1; PID:g1574216; TIGR:HI1383 CLASSIFICATION #superfamily phosphate-repressible phosphate-binding protein KEYWORDS phosphate transport SUMMARY #length 258 #molecular-weight 28542 #checksum 1493 SEQUENCE /// ENTRY QRECBC #type complete TITLE vitamin B12 transport permease protein btuC precursor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS G64929; A24498; S04777 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64929 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-326 ##label BLAT !'##cross-references GB:AE000266; GB:U00096; NID:g1787997; !1PIDN:AAC74781.1; PID:g1788004; UWGP:b1711 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A24498 !$#authors Friedrich, M.J.; DeVeaux, L.C.; Kadner, R.J. !$#journal J. Bacteriol. (1986) 167:928-934 !$#title Nucleotide sequence of the btuCED genes involved in vitamin !1B12 transport in Escherichia coli and homology with !1components of periplasmic-binding-protein-dependent !1transport systems. !$#cross-references MUID:86304184; PMID:3528129 !$#accession A24498 !'##molecule_type DNA !'##residues 1-110,'LT',113-122,'R',124-285,'DCCWPIL' ##label FRI !'##note this sequence has been revised in reference S04777 REFERENCE S04777 !$#authors Rioux, C.R.; Kadner, R.J. !$#journal Mol. Gen. Genet. (1989) 217:301-308 !$#title Vitamin B(12) transport in Escherichia coli K12 does not !1require the btuE gene of the btuCED operon. !$#cross-references MUID:89364713; PMID:2671656 !$#accession S04777 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 280-326 ##label RIO COMMENT This membrane-associated protein is required for vitamin B12 !1transport across the cytoplasmic membrane; however, its !1exact role is not clear. GENETICS !$#gene btuC !$#map_position 37 min CLASSIFICATION #superfamily vitamin B12 transport protein btuC KEYWORDS transmembrane protein; vitamin B12 transport FEATURE !$1-35 #domain signal sequence #status predicted #label SIG\ !$36-326 #product vitamin B12 transport permease protein btuC !8#status predicted #label MAT\ !$61-77 #domain transmembrane #status predicted #label TM01\ !$90-106 #domain transmembrane #status predicted #label TM02\ !$117-133 #domain transmembrane #status predicted #label TM03\ !$145-161 #domain transmembrane #status predicted #label TM04\ !$190-206 #domain transmembrane #status predicted #label TM05\ !$244-260 #domain transmembrane #status predicted #label TM06\ !$274-290 #domain transmembrane #status predicted #label TM07\ !$305-321 #domain transmembrane #status predicted #label TM08 SUMMARY #length 326 #molecular-weight 34949 #checksum 1332 SEQUENCE /// ENTRY QRECD2 #type complete TITLE iron(III) dicitrate transport protein 2, cytosolic - Escherichia coli (strain K-12) ALTERNATE_NAMES citrate-dependent iron transport protein fecD ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS S56513; B65242; JS0114 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56513 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-318 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97184.1; !1PID:g537129 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65242 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-318 ##label BLAT !'##cross-references GB:AE000499; GB:U00096; NID:g1790732; !1PIDN:AAC77244.1; PID:g1790740; UWGP:b4288 !'##experimental_source strain K-12, substrain MG1655 REFERENCE PS0029 !$#authors Staudenmaier, H.; Van Hove, B.; Yaraghi, Z.; Braun, V. !$#journal J. Bacteriol. (1989) 171:2626-2633 !$#title Nucleotide sequences of the fecBCDE genes and locations of !1the proteins suggest a periplasmic-binding-protein-dependent !1transport mechanism for iron(III) dicitrate in Escherichia !1coli. !$#cross-references MUID:89213950; PMID:2651410 !$#accession JS0114 !'##molecule_type DNA !'##residues 1-40,'R',42-318 ##label STA !'##cross-references GB:M26397; NID:g145923; PIDN:AAA23764.1; !1PID:g145927 !'##experimental_source strain K12 COMMENT This protein is one of five, encoded by the fec operon, !1constituting a citrate-dependent iron(III) transport system. !1It is also one of two nonpolar integral membrane proteins in !1the system. GENETICS !$#gene fecD !$#map_position 7 min CLASSIFICATION #superfamily vitamin B12 transport protein btuC KEYWORDS iron transport; transmembrane protein SUMMARY #length 318 #molecular-weight 34131 #checksum 7621 SEQUENCE /// ENTRY QRECD1 #type complete TITLE iron(III) dicitrate transport protein 1, cytosolic - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS S56514; C65242; JS0113 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56514 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-332 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97185.1; !1PID:g537130 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65242 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-332 ##label BLAT !'##cross-references GB:AE000499; GB:U00096; NID:g1790732; !1PIDN:AAC77245.1; PID:g1790741; UWGP:b4289 !'##experimental_source strain K-12, substrain MG1655 REFERENCE PS0029 !$#authors Staudenmaier, H.; Van Hove, B.; Yaraghi, Z.; Braun, V. !$#journal J. Bacteriol. (1989) 171:2626-2633 !$#title Nucleotide sequences of the fecBCDE genes and locations of !1the proteins suggest a periplasmic-binding-protein-dependent !1transport mechanism for iron(III) dicitrate in Escherichia !1coli. !$#cross-references MUID:89213950; PMID:2651410 !$#accession JS0113 !'##molecule_type DNA !'##residues 1-102,'WLWRYQR',110,'E',112,'DADCRLF',120,'V','V',124-178, !1'S',179-332 ##label STA !'##cross-references GB:M26397; NID:g145923; PIDN:AAA23763.1; !1PID:g145926 !'##experimental_source strain K12 COMMENT This protein is one of five, encoded by the fec operon, !1constituting a citrate-dependent iron(III) transport system. !1It is also one of two nonpolar integral membrane proteins in !1the system. GENETICS !$#gene fecC !$#map_position 7 min CLASSIFICATION #superfamily vitamin B12 transport protein btuC KEYWORDS iron transport; transmembrane protein FEATURE !$106-117 #region hydrophilic\ !$144-151 #region hydrophilic SUMMARY #length 332 #molecular-weight 34892 #checksum 5889 SEQUENCE /// ENTRY D69812 #type complete TITLE ferrichrome ABC transporter (permease) homolog yfmE - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS D69812 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D69812 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-333 ##label KUN !'##cross-references GB:Z99108; GB:AL009126; NID:g2633055; !1PIDN:CAB12579.1; PID:g2633074 !'##experimental_source strain 168 GENETICS !$#gene yfmE CLASSIFICATION #superfamily vitamin B12 transport protein btuC SUMMARY #length 333 #molecular-weight 35218 #checksum 9321 SEQUENCE /// ENTRY G64310 #type complete TITLE hemin permease homolog - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G64310 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession G64310 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-349 ##label BUL !'##cross-references GB:U67466; GB:L77117; NID:g1590867; !1PIDN:AAB98069.1; PID:g1590869; TIGR:MJ0087 GENETICS !$#map_position FOR81930-82979 CLASSIFICATION #superfamily vitamin B12 transport protein btuC SUMMARY #length 349 #molecular-weight 38201 #checksum 1553 SEQUENCE /// ENTRY B69763 #type complete TITLE ferrichrome ABC transporter (permease) homolog yclN - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS B69763 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69763 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-316 ##label KUN !'##cross-references GB:Z99106; GB:AL009126; NID:g2632653; !1PIDN:CAB12188.1; PID:g2632681 !'##experimental_source strain 168 GENETICS !$#gene yclN CLASSIFICATION #superfamily vitamin B12 transport protein btuC SUMMARY #length 316 #molecular-weight 34899 #checksum 8904 SEQUENCE /// ENTRY A41671 #type complete TITLE iron transport protein fatD - Vibrio anguillarum ORGANISM #formal_name Vibrio anguillarum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A41671 REFERENCE A41671 !$#authors Koester, W.L.; Actis, L.A.; Waldbeser, L.S.; Tolmasky, M.E.; !1Crosa, J.H. !$#journal J. Biol. Chem. (1991) 266:23829-23833 !$#title Molecular characterization of the iron transport system !1mediated by the pJM1 plasmid in Vibrio anguillarum 775. !$#cross-references MUID:92084677; PMID:1748657 !$#accession A41671 !'##status preliminary !'##molecule_type DNA !'##residues 1-314 ##label KOE !'##cross-references GB:M74068; NID:g150758; PIDN:AAA25641.1; !1PID:g150759 CLASSIFICATION #superfamily vitamin B12 transport protein btuC KEYWORDS transmembrane protein SUMMARY #length 314 #molecular-weight 33922 #checksum 134 SEQUENCE /// ENTRY C69763 #type complete TITLE ferrichrome ABC transporter (permease) homolog yclO - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS C69763 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69763 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-315 ##label KUN !'##cross-references GB:Z99106; GB:AL009126; NID:g2632653; !1PIDN:CAB12189.1; PID:g2632682 !'##experimental_source strain 168 GENETICS !$#gene yclO CLASSIFICATION #superfamily ferrichrome ABC transporter SUMMARY #length 315 #molecular-weight 35473 #checksum 6084 SEQUENCE /// ENTRY B41671 #type complete TITLE iron transport protein fatC - Vibrio anguillarum ORGANISM #formal_name Vibrio anguillarum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B41671 REFERENCE A41671 !$#authors Koester, W.L.; Actis, L.A.; Waldbeser, L.S.; Tolmasky, M.E.; !1Crosa, J.H. !$#journal J. Biol. Chem. (1991) 266:23829-23833 !$#title Molecular characterization of the iron transport system !1mediated by the pJM1 plasmid in Vibrio anguillarum 775. !$#cross-references MUID:92084677; PMID:1748657 !$#accession B41671 !'##status preliminary !'##molecule_type DNA !'##residues 1-317 ##label KOE !'##cross-references GB:M74068; NID:g150758; PIDN:AAA25642.1; !1PID:g150760 CLASSIFICATION #superfamily ferrichrome ABC transporter KEYWORDS transmembrane protein SUMMARY #length 317 #molecular-weight 34929 #checksum 5436 SEQUENCE /// ENTRY C69812 #type complete TITLE ferrichrome ABC transporter (permease) homolog yfmD - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS C69812 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69812 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-333 ##label KUN !'##cross-references GB:Z99108; GB:AL009126; NID:g2633055; !1PIDN:CAB12580.1; PID:g2633075 !'##experimental_source strain 168 GENETICS !$#gene yfmD CLASSIFICATION #superfamily ferrichrome ABC transporter SUMMARY #length 333 #molecular-weight 35098 #checksum 8217 SEQUENCE /// ENTRY G64125 #type complete TITLE hemin transport protein homolog HI1471 - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES hemin permease homolog HI1471 ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS G64125 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession G64125 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-337 ##label TIGR !'##cross-references GB:U32825; GB:L42023; NID:g3212226; !1PIDN:AAC23119.1; PID:g1574312; TIGR:HI1471 CLASSIFICATION #superfamily ferrichrome ABC transporter SUMMARY #length 337 #molecular-weight 36530 #checksum 5512 SEQUENCE /// ENTRY QRECBD #type complete TITLE vitamin b12 transport ATP-binding protein btuD - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 01-Mar-2002 ACCESSIONS C24498; E64929 REFERENCE A24498 !$#authors Friedrich, M.J.; DeVeaux, L.C.; Kadner, R.J. !$#journal J. Bacteriol. (1986) 167:928-934 !$#title Nucleotide sequence of the btuCED genes involved in vitamin !1B12 transport in Escherichia coli and homology with !1components of periplasmic-binding-protein-dependent !1transport systems. !$#cross-references MUID:86304184; PMID:3528129 !$#accession C24498 !'##molecule_type DNA !'##residues 1-249 ##label FRI !'##cross-references GB:M14031; NID:g145441; PIDN:AAA23528.1; !1PID:g145445 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64929 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-249 ##label BLAT !'##cross-references GB:AE000266; GB:U00096; NID:g1787997; !1PIDN:AAC74779.1; PID:g1788002; UWGP:b1709 !'##experimental_source strain K-12, substrain MG1655 COMMENT This is one of the components required for transporting !1vitamin B12 across the cytoplasmic membrane. This active !1transport system is very similar to binding !1protein-dependent systems; however, the exact role of this !1protein has not been determined. GENETICS !$#gene btuD !$#map_position 37 min FUNCTION !$#description involved in vitamin B12 transport CLASSIFICATION #superfamily inner membrane protein malK; ATP-binding !1cassette homology KEYWORDS ATP; membrane protein; nucleotide binding; P-loop; vitamin !1B12 transport FEATURE !$16-209 #domain ATP-binding cassette homology #label ABC\ !$33-40 #region nucleotide-binding motif A (P-loop) SUMMARY #length 249 #molecular-weight 27081 #checksum 1339 SEQUENCE /// ENTRY MMECMK #type complete TITLE inner membrane protein malK - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 05-Apr-1983 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS B65211; A03411; S06707 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65211 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-371 ##label BLAT !'##cross-references GB:AE000476; GB:U00096; NID:g1790456; !1PIDN:AAC77005.1; PID:g1790467; UWGP:b4035 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A03411 !$#authors Gilson, E.; Nikaido, H.; Hofnung, M. !$#journal Nucleic Acids Res. (1982) 10:7449-7458 !$#title Sequence of the malK gene in Escherichia coli K12. !$#cross-references MUID:83116968; PMID:6296778 !$#accession A03411 !'##molecule_type DNA !'##residues 1-101,'P',103-219,'AVPLSGRPFCRRI',222,'RFAK',227,'EL', !1242-371 ##label GIL !'##cross-references GB:J01648; GB:J01639; GB:K02117; GB:M24344; !1GB:M24345; NID:g146697; PIDN:AAB59057.1; PID:g146701 !'##experimental_source strain K12 REFERENCE S05328 !$#authors Dahl, M.K.; Francoz, E.; Saurin, W.; Boos, W.; Manson, M.D.; !1Hofnung, M. !$#journal Mol. Gen. Genet. (1989) 218:199-207 !$#title Comparison of sequences from the malB regions of Salmonella !1typhimurium and Enterobacter aerogenes with Escherichia coli !1K12: a potential new regulatory site in the interoperonic !1region. !$#cross-references MUID:89384443; PMID:2674653 !$#accession S06707 !'##molecule_type DNA !'##residues 1-101,'P',103-371 ##label DAH COMMENT This is one of the five or more proteins involved in the !1transport system of maltose and maltodextrin; its exact !1function is not yet known. GENETICS !$#gene malK !$#map_position 92 min CLASSIFICATION #superfamily inner membrane protein malK; ATP-binding !1cassette homology KEYWORDS ATP; inner membrane; nucleotide binding; P-loop FEATURE !$19-210 #domain ATP-binding cassette homology #label ABC\ !$36-43 #region nucleotide-binding motif A (P-loop) SUMMARY #length 371 #molecular-weight 40990 #checksum 3806 SEQUENCE /// ENTRY QRECM3 #type complete TITLE membrane-bound iron(III) dicitrate transport protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 01-Mar-2002 ACCESSIONS JS0115; S56512; A65242 REFERENCE PS0029 !$#authors Staudenmaier, H.; Van Hove, B.; Yaraghi, Z.; Braun, V. !$#journal J. Bacteriol. (1989) 171:2626-2633 !$#title Nucleotide sequences of the fecBCDE genes and locations of !1the proteins suggest a periplasmic-binding-protein-dependent !1transport mechanism for iron(III) dicitrate in Escherichia !1coli. !$#cross-references MUID:89213950; PMID:2651410 !$#accession JS0115 !'##molecule_type DNA !'##residues 1-255 ##label STA !'##cross-references GB:M26397; NID:g145923; PIDN:AAA23765.1; !1PID:g145928 !'##experimental_source strain K12 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56512 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-255 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97183.1; !1PID:g537128 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65242 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-255 ##label BLAT !'##cross-references GB:AE000499; GB:U00096; NID:g1790732; !1PIDN:AAC77243.1; PID:g1790739; UWGP:b4287 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene fecE !$#map_position 7 min FUNCTION !$#description one of five, encoded by the fec operon, constituting a !1citrate-dependent iron(III) transport system CLASSIFICATION #superfamily inner membrane protein malK; ATP-binding !1cassette homology KEYWORDS ATP; iron transport; membrane protein; nucleotide binding; !1P-loop FEATURE !$18-214 #domain ATP-binding cassette homology #label ABC\ !$35-42 #region nucleotide-binding motif A (P-loop) SUMMARY #length 255 #molecular-weight 28190 #checksum 283 SEQUENCE /// ENTRY QREBOT #type complete TITLE oligopeptide transport protein oppD - Salmonella typhimurium ALTERNATE_NAMES oligopeptide permease membrane protein oppD ORGANISM #formal_name Salmonella typhimurium DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 23-Apr-1999 ACCESSIONS A03413; E29333 REFERENCE A03413 !$#authors Higgins, C.F.; Hiles, I.D.; Whalley, K.; Jamieson, D.J. !$#journal EMBO J. (1985) 4:1033-1039 !$#title Nucleotide binding by membrane components of bacterial !1periplasmic binding protein-dependent transport systems. !$#cross-references MUID:85257495; PMID:3926486 !$#accession A03413 !'##molecule_type DNA !'##residues 1-335 ##label HIG !'##note the DNA sequence of oppD gene (Hiles and Higgins, unpublished !1data) was not shown in the above paper REFERENCE A29333 !$#authors Hiles, I.D.; Gallagher, M.P.; Jamieson, D.J.; Higgins, C.F. !$#journal J. Mol. Biol. (1987) 195:125-142 !$#title Molecular characterization of the oligopeptide permease of !1Salmonella typhimurium. !$#cross-references MUID:88011222; PMID:2821267 !$#accession E29333 !'##molecule_type DNA !'##residues 1-335 ##label HIL COMMENT This protein is one of the membrane-bound components of !1oligopeptide permease, a binding protein-dependent transport !1system that requires a periplasmic protein, in addition to !1several cytoplasmic membrane proteins, for substrate !1binding. It may be responsible for energy coupling to the !1transport system. GENETICS !$#gene oppD !$#map_position 34 min FUNCTION !$#description probably responsible for energy-coupling to the transport !1system CLASSIFICATION #superfamily inner membrane protein malK; ATP-binding !1cassette homology KEYWORDS ATP; binding protein-dependent transport system; membrane !1protein; nucleotide binding; oligopeptide transport; P-loop FEATURE !$37-243 #domain ATP-binding cassette homology #label ABC\ !$54-61 #region nucleotide-binding motif A (P-loop)\ !$187-191 #region nucleotide-binding motif B SUMMARY #length 335 #molecular-weight 37029 #checksum 1766 SEQUENCE /// ENTRY QREBOF #type complete TITLE oligopeptide transport protein oppF - Salmonella typhimurium ALTERNATE_NAMES oligopeptide permease membrane protein oppF ORGANISM #formal_name Salmonella typhimurium DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS D29333 REFERENCE A29333 !$#authors Hiles, I.D.; Gallagher, M.P.; Jamieson, D.J.; Higgins, C.F. !$#journal J. Mol. Biol. (1987) 195:125-142 !$#title Molecular characterization of the oligopeptide permease of !1Salmonella typhimurium. !$#cross-references MUID:88011222; PMID:2821267 !$#accession D29333 !'##molecule_type DNA !'##residues 1-334 ##label HIL !'##cross-references GB:X05491; NID:g47801; PIDN:CAA29043.1; PID:g47806 !'##experimental_source strain LT2 COMMENT This protein is one of the membrane-bound components of !1oligopeptide permease, a binding protein-dependent transport !1system that requires a periplasmic protein, in addition to !1several cytoplasmic membrane proteins, for substrate !1binding. GENETICS !$#gene oppF !$#map_position 34 min FUNCTION !$#description probably responsible for energy-coupling to the transport !1system CLASSIFICATION #superfamily inner membrane protein malK; ATP-binding !1cassette homology KEYWORDS ATP; binding protein-dependent transport system; membrane !1protein; nucleotide binding; oligopeptide transport; P-loop FEATURE !$40-241 #domain ATP-binding cassette homology #label ABC\ !$57-64 #region nucleotide-binding motif A (P-loop)\ !$185-189 #region nucleotide-binding motif B SUMMARY #length 334 #molecular-weight 37214 #checksum 2722 SEQUENCE /// ENTRY BVECZB #type complete TITLE ABC-type phosphate transport system ATP-binding protein pstB [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 01-Mar-2002 ACCESSIONS A30382; F65175; Q00616 REFERENCE A30382 !$#authors Amemura, M.; Makino, K.; Shinagawa, H.; Kobayashi, A.; !1Nakata, A. !$#journal J. Mol. Biol. (1985) 184:241-250 !$#title Nucleotide sequence of the genes involved in phosphate !1transport and regulation of the phosphate regulon in !1Escherichia coli. !$#cross-references MUID:85293094; PMID:2993631 !$#accession A30382 !'##molecule_type DNA !'##residues 1-257 ##label AME !'##cross-references GB:X02723; NID:g42395; PIDN:CAA26509.1; PID:g42398 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65175 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-257 ##label BLAT !'##cross-references GB:AE000449; GB:U00096; NID:g2367269; !1PIDN:AAC76748.1; PID:g1790162; UWGP:b3725 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene pstB !$#map_position 84 min FUNCTION !$#description required for the binding protein-mediated, highly specific !1phosphate transport [validated, MUID:85293094] CLASSIFICATION #superfamily inner membrane protein malK; ATP-binding !1cassette homology KEYWORDS ATP; binding protein-dependent transport system; nucleotide !1binding; P-loop; phosphate transport FEATURE !$26-228 #domain ATP-binding cassette homology #label ABC\ !$43-50 #region nucleotide-binding motif A (P-loop)\ !$174-179 #region nucleotide-binding motif B SUMMARY #length 257 #molecular-weight 29027 #checksum 5492 SEQUENCE /// ENTRY QRECFH #type complete TITLE ferrichrome transport ATP-binding protein fhuC - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1990 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS G64738; A30394; A32650; S45220; Q00049 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64738 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-265 ##label BLAT !'##cross-references GB:AE000124; GB:U00096; NID:g1786339; !1PIDN:AAC73262.1; PID:g1786345; UWGP:b0151 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A30394 !$#authors Coulton, J.W.; Mason, P.; Allatt, D.D. !$#journal J. Bacteriol. (1987) 169:3844-3849 !$#title fhuC and fhuD genes for iron(III)-ferrichrome transport into !1Escherichia coli K-12. !$#cross-references MUID:87279948; PMID:3301821 !$#accession A30394 !'##molecule_type DNA !'##residues 1-225,'SDCS',230,'NACGNYARRNPRNDLWH',248,'D',250-265 !1##label COU !'##cross-references GB:D26562; NID:g473770; PIDN:BAA05599.1; !1PID:g473810 REFERENCE A32650 !$#authors Burkhardt, R.; Braun, V. !$#journal Mol. Gen. Genet. (1987) 209:49-55 !$#title Nucleotide sequence of the fhuC and fhuD genes involved in !1iron (III) hydroxamate transport: domains in FhuC homologous !1to ATP-binding proteins. !$#cross-references MUID:88038363; PMID:2823072 !$#accession A32650 !'##molecule_type DNA !'##residues 1-265 ##label BUR REFERENCE S45181 !$#authors Fujita, N. !$#submission submitted to the EMBL Data Library, January 1994 !$#accession S45220 !'##molecule_type DNA !'##residues 1-225,'SDCS',230,'NACGNYARRNPRNDLWH',248,'D',250-265 !1##label FUJ !'##cross-references EMBL:D26562; NID:g473770; PIDN:BAA05599.1; !1PID:g473810 !'##experimental_source strain K-12, substrain W3110 COMMENT This is one of the proteins involved in the high-affinity !1transport of iron(III)-ferrichrome into the E. coli cell. It !1may function as an ATP-binding protein in the Fe(III) uptake !1process. GENETICS !$#gene fhuC !$#map_position 4 min CLASSIFICATION #superfamily inner membrane protein malK; ATP-binding !1cassette homology KEYWORDS ATP; iron transport; membrane protein; nucleotide binding; !1P-loop FEATURE !$27-224 #domain ATP-binding cassette homology #label ABC\ !$44-51 #region nucleotide-binding motif A (P-loop)\ !$168-173 #region nucleotide-binding motif B SUMMARY #length 265 #molecular-weight 28886 #checksum 7315 SEQUENCE /// ENTRY QRECSA #type complete TITLE sulfate transport ATP-binding protein cysA - Escherichia coli (strain K-12) ALTERNATE_NAMES nucleotide-binding protein cysA ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS E65016; C35402 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65016 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-365 ##label BLAT !'##cross-references GB:AE000329; GB:U00096; NID:g2367137; !1PIDN:AAC75475.1; PID:g1788761; UWGP:b2422 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A35402 !$#authors Sirko, A.; Hryniewicz, M.; Hulanicka, D.; Boeck, A. !$#journal J. Bacteriol. (1990) 172:3351-3357 !$#title Sulfate and thiosulfate transport in Escherichia coli K-12: !1nucleotide sequence and expression of the cysTWAM gene !1cluster. !$#cross-references MUID:90264334; PMID:2188958 !$#accession C35402 !'##molecule_type DNA !'##residues 1-135,'HV',138-365 ##label SIR !'##cross-references GB:M32101; GB:M38050; NID:g145657; PIDN:AAA23639.1; !1PID:g145661 !'##experimental_source strain K12 COMMENT This protein is the hydrophilic nucleotide-binding component !1of the binding protein-dependent transport system for !1sulfates and thiosulfates. GENETICS !$#gene cysA !$#map_position 52 min CLASSIFICATION #superfamily inner membrane protein malK; ATP-binding !1cassette homology KEYWORDS ATP; binding protein-dependent transport system; inner !1membrane; nucleotide binding; P-loop; sulfate transport; !1thiosulfate transport FEATURE !$18-213 #domain ATP-binding cassette homology #label ABC\ !$35-42 #region nucleotide-binding motif A (P-loop)\ !$157-161 #region nucleotide-binding motif B SUMMARY #length 365 #molecular-weight 41059 #checksum 6740 SEQUENCE /// ENTRY BVECMF #type complete TITLE mcbF protein - Escherichia coli plasmid MccB17 ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS S01228 REFERENCE S00836 !$#authors Garrido, M.C.; Herrero, M.; Kolter, R.; Moreno, F. !$#journal EMBO J. (1988) 7:1853-1862 !$#title The export of the DNA replication inhibitor microcin B17 !1provides immunity for the host cell. !$#cross-references MUID:89005078; PMID:3049078 !$#accession S01228 !'##molecule_type DNA !'##residues 1-247 ##label DEL !'##cross-references EMBL:X07875; NID:g41980; PIDN:CAA30723.1; !1PID:g41982 !'##note the authors translated the codon GAC for residue 109 as Glu and !1GTT for residue 110 as Leu COMMENT The immunity to the peptide antibiotic microcin B17 !1(MccB17), which inhibits DNA replication in enterobacteria, !1is mediated by mcbF, mcbE, and mcbG proteins. mcbF protein, !1a nucleotide-binding protein, together with mcbE protein, !1may be involved in the export of active MccB17 from the !1cytoplasm to the periplasmic space. GENETICS !$#gene mcbF !$#genome plasmid CLASSIFICATION #superfamily inner membrane protein malK; ATP-binding !1cassette homology KEYWORDS antibiotic resistance; ATP; membrane protein; nucleotide !1binding; P-loop FEATURE !$23-210 #domain ATP-binding cassette homology #label ABC\ !$40-47 #region nucleotide-binding motif A (P-loop)\ !$155-159 #region nucleotide-binding motif B SUMMARY #length 247 #molecular-weight 28819 #checksum 2124 SEQUENCE /// ENTRY BVLVMX #type complete TITLE mbpX protein - liverwort (Marchantia polymorpha) chloroplast ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS S01592; A05038 REFERENCE S01567 !$#authors Umesono, K.; Inokuchi, H.; Shiki, Y.; Takeuchi, M.; Chang, !1Z.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Ohyama, K.; Ozeki, !1H. !$#journal J. Mol. Biol. (1988) 203:299-331 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. II. Gene organization of the large !1single copy region from rps'12 to atpB. !$#cross-references MUID:89068686; PMID:2974085 !$#accession S01592 !'##molecule_type DNA !'##residues 1-370 ##label UME !'##cross-references GB:X04465; GB:Y00686; NID:g11640; PIDN:CAA28079.1; !1PID:g11666 COMMENT This protein is homologous with E. coli malK protein and !1thus may be involved in a binding protein-dependent !1transport system in the chloroplast. GENETICS !$#gene mbpX !$#genome chloroplast CLASSIFICATION #superfamily inner membrane protein malK; ATP-binding !1cassette homology KEYWORDS ATP; chloroplast; nucleotide binding; P-loop FEATURE !$18-209 #domain ATP-binding cassette homology #label ABC\ !$35-42 #region nucleotide-binding motif A (P-loop)\ !$153-157 #region nucleotide-binding motif B SUMMARY #length 370 #molecular-weight 42799 #checksum 7349 SEQUENCE /// ENTRY QRSEUC #type complete TITLE nucleotide-binding protein sfuC - Serratia marcescens ORGANISM #formal_name Serratia marcescens DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS C35108 REFERENCE A35108 !$#authors Angerer, A.; Gaisser, S.; Braun, V. !$#journal J. Bacteriol. (1990) 172:572-578 !$#title Nucleotide sequences of the sfuA, sfuB, and sfuC genes of !1Serratia marcescens suggest a !1periplasmic-binding-protein-dependent iron transport !1mechanism. !$#cross-references MUID:90130288; PMID:2404942 !$#accession C35108 !'##molecule_type DNA !'##residues 1-345 ##label ANG !'##cross-references GB:M33815; NID:g152859; PIDN:AAA26575.1; !1PID:g152862 COMMENT This protein is the nucleotide-binding protein component of !1the binding protein-dependent transport system for Fe(III). !1However, it is not clear how Fe(III) is solubilized and !1taken up across the outer membrane. GENETICS !$#gene sfuC CLASSIFICATION #superfamily inner membrane protein malK; ATP-binding !1cassette homology KEYWORDS ATP; binding protein-dependent transport system; inner !1membrane; nucleotide binding; P-loop; sulfate transport; !1thiosulfate transport FEATURE !$19-212 #domain ATP-binding cassette homology #label ABC\ !$36-43 #region nucleotide-binding motif A (P-loop)\ !$156-160 #region nucleotide-binding motif B SUMMARY #length 345 #molecular-weight 36692 #checksum 1574 SEQUENCE /// ENTRY QRECUC #type complete TITLE sn-Glycerol-3-phosphate transport ATP-binding protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 01-Mar-1996 #text_change 01-Mar-2002 ACCESSIONS S47669; S03783; E65141 REFERENCE S47666 !$#authors Plunkett, G. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S47669 !'##status preliminary !'##molecule_type DNA !'##residues 1-369 ##label PLU !'##cross-references EMBL:U00039; NID:g466582; PIDN:AAB18425.1; !1PID:g912455 REFERENCE S03780 !$#authors Overduin, P.; Boos, W.; Tommassen, J. !$#journal Mol. Microbiol. (1988) 2:767-775 !$#title Nucleotide sequence of the ugp genes of Escherichia coli !1K-12: homology to the maltose system. !$#cross-references MUID:89096498; PMID:3062310 !$#accession S03783 !'##molecule_type DNA !'##residues 14-369 ##label OVE !'##cross-references EMBL:X13141; NID:g43243; PIDN:CAA31534.1; !1PID:g43249 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65141 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-369 ##label BLAT !'##cross-references GB:AE000421; GB:U00096; NID:g1789854; !1PIDN:AAC76475.1; PID:g1789859; UWGP:b3450 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ugpC !$#map_position 76 min !$#start_codon GTG FUNCTION !$#description the hydrophilic nucleotide-binding component of the !1phosphate limitation-induced binding protein-dependent !1transport system for glycerol-3-phosphate and !1glycerophosphoryl diesters CLASSIFICATION #superfamily inner membrane protein malK; ATP-binding !1cassette homology KEYWORDS ATP; binding protein-dependent transport system; !1glycerol-3-phosphate transport; inner membrane; nucleotide !1binding; P-loop FEATURE !$33-224 #domain ATP-binding cassette homology #label ABC\ !$50-57 #region nucleotide-binding motif A (P-loop)\ !$168-172 #region nucleotide-binding motif B SUMMARY #length 369 #molecular-weight 40968 #checksum 4634 SEQUENCE /// ENTRY GRYCS7 #type complete TITLE sulfate transport protein - Synechococcus sp. (strain PCC 7942) ALTERNATE_NAMES sulfate permease ORGANISM #formal_name Synechococcus sp. DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 28-May-1999 ACCESSIONS A30301; A43670; JQ0123 REFERENCE A30301 !$#authors Green, L.S.; Laudenbach, D.E.; Grossman, A.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:1949-1953 !$#title A region of a cyanobacterial genome required for sulfate !1transport. !$#cross-references MUID:89184544; PMID:2538823 !$#accession A30301 !'##molecule_type DNA !'##residues 1-344 ##label GRE !'##cross-references GB:J04512; NID:g142151; PIDN:AAA22056.1; !1PID:g142152 REFERENCE A43670 !$#authors Laudenbach, D.E.; Grossman, A.R. !$#journal J. Bacteriol. (1991) 173:2739-2750 !$#title Characterization and mutagenesis of sulfur-regulated genes !1in a cyanobacterium: evidence for function in sulfate !1transport. !$#cross-references MUID:91210162; PMID:1708375 !$#accession A43670 !'##status preliminary !'##molecule_type DNA !'##residues 1-11 ##label LAU !'##cross-references GB:M65247 GENETICS !$#gene cysA !$#start_codon GTG FUNCTION !$#description this protein is the hydrophilic nucleotide-binding component !1of the binding protein-dependent transport system for !1sulfates CLASSIFICATION #superfamily inner membrane protein malK; ATP-binding !1cassette homology KEYWORDS ATP; binding protein-dependent transport system; inner !1membrane; nucleotide binding; P-loop; sulfate transport FEATURE !$24-215 #domain ATP-binding cassette homology #label ABC\ !$41-48 #region nucleotide-binding motif A (P-loop)\ !$159-163 #region nucleotide-binding motif B SUMMARY #length 344 #molecular-weight 38476 #checksum 4957 SEQUENCE /// ENTRY E70046 #type complete TITLE iron transport system homolog yvrA - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS E70046 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E70046 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-442 ##label KUN !'##cross-references GB:Z99120; GB:Z99121; GB:AL009126; NID:g2635827; !1PIDN:CAB15321.1; PID:g2635829; NID:g2635613; PID:g2635813 !'##experimental_source strain 168 GENETICS !$#gene yvrA CLASSIFICATION #superfamily Bacillus subtilis probable iron transport !1system yvrA; ATP-binding cassette homology KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$16-214 #domain ATP-binding cassette homology #label ABC\ !$33-40 #region nucleotide-binding motif A (P-loop) SUMMARY #length 442 #molecular-weight 48631 #checksum 4084 SEQUENCE /// ENTRY QREBVT #type complete TITLE glycine betaine/proline transport protein proV - Salmonella typhimurium ALTERNATE_NAMES nucleotide-binding protein proV ORGANISM #formal_name Salmonella typhimurium DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS S05374; B45917; S34273 REFERENCE S05374 !$#authors Stirling, D.A.; Hulton, C.S.J.; Waddell, L.; Park, S.F.; !1Stewart, G.S.A.B.; Booth, I.R.; Higgins, C.F. !$#journal Mol. Microbiol. (1989) 3:1025-1038 !$#title Molecular characterization of the proU loci of Salmonella !1typhimurium and Escherichia coli encoding osmoregulated !1glycine betaine transport systems. !$#cross-references MUID:90113884; PMID:2691838 !$#accession S05374 !'##molecule_type DNA !'##residues 1-400 ##label STI !'##cross-references GB:X52693; NID:g47829; PIDN:CAA36921.1; PID:g47831 REFERENCE A45917 !$#authors Overdier, D.G.; Olson, E.R.; Erickson, B.D.; Ederer, M.M.; !1Csonka, L.N. !$#journal J. Bacteriol. (1989) 171:4694-4706 !$#title Nucleotide sequence of the transcriptional control region of !1the osmotically regulated proU operon of Salmonella !1typhimurium and identification of the 5' endpoint of the !1proU mRNA. !$#cross-references MUID:89359099; PMID:2548994 !$#accession B45917 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-157,'A',159-290 ##label OVE !'##cross-references GB:M26063; NID:g154278; PIDN:AAA88621.1; !1PID:g552022 REFERENCE S34271 !$#authors Jordan Valles, A. !$#submission submitted to the EMBL Data Library, June 1993 !$#accession S34273 !'##status preliminary !'##molecule_type DNA !'##residues 1-157,'A',159-196 ##label JOR !'##cross-references EMBL:X73226 COMMENT This protein is the hydrophilic nucleotide-binding component !1of the binding protein-dependent osmoregulated transport !1system for glycine betaine and proline. GENETICS !$#gene proV !$#map_position 57 min CLASSIFICATION #superfamily glycine betaine/proline transport protein proV; !1ATP-binding cassette homology; CBS homology KEYWORDS ATP; binding protein-dependent transport system; glycine !1betaine transport; inner membrane; nucleotide binding; !1P-loop; proline transport FEATURE !$44-241 #domain ATP-binding cassette homology #label ABC\ !$61-68 #region nucleotide-binding motif A (P-loop)\ !$185-189 #region nucleotide-binding motif B\ !$286-334 #domain CBS homology #label CBS1\ !$346-393 #domain CBS homology #label CBS2 SUMMARY #length 400 #molecular-weight 44210 #checksum 2802 SEQUENCE /// ENTRY BVECPV #type complete TITLE glycine betaine/L-proline transport ATP-binding protein proV - Escherichia coli (strain K-12) ALTERNATE_NAMES nucleotide-binding protein proV ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 01-Mar-2002 ACCESSIONS JS0128; F65047 REFERENCE JS0128 !$#authors Gowrishankar, J. !$#journal J. Bacteriol. (1989) 171:1923-1931 !$#title Nucleotide sequence of the osmoregulatory proU operon of !1Escherichia coli. !$#cross-references MUID:89197759; PMID:2649479 !$#accession JS0128 !'##molecule_type DNA !'##residues 1-400 ##label GOW !'##cross-references GB:M24856; NID:g147372; PIDN:AAA24427.1; !1PID:g147373 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65047 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-400 ##label BLAT !'##cross-references GB:AE000352; GB:U00096; NID:g1789024; !1PIDN:AAC75724.1; PID:g1789032; UWGP:b2677 !'##experimental_source strain K-12, substrain MG1655 COMMENT This is one of the three components of the transport system !1for glycine betaine and L-proline. GENETICS !$#gene proV !$#map_position 57 min CLASSIFICATION #superfamily glycine betaine/proline transport protein proV; !1ATP-binding cassette homology; CBS homology KEYWORDS ATP; binding protein-dependent transport system; glycine !1betaine transport; inner membrane; nucleotide binding; !1P-loop; proline transport FEATURE !$44-241 #domain ATP-binding cassette homology #label ABC\ !$61-68 #region nucleotide-binding motif A (P-loop)\ !$185-189 #region nucleotide-binding motif B\ !$286-334 #domain CBS homology #label CBS1\ !$346-393 #domain CBS homology #label CBS2 SUMMARY #length 400 #molecular-weight 44162 #checksum 4110 SEQUENCE /// ENTRY I40535 #type complete TITLE probable glycine betaine/proline ABC transporter - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS I40535; D69669 REFERENCE A57322 !$#authors Kempf, B.; Bremer, E. !$#journal J. Biol. Chem. (1995) 270:16701-16713 !$#title OpuA, an osmotically regulated binding protein-dependent !1transport system for the osmoprotectant glycine betaine in !1Bacillus subtilis. !$#cross-references MUID:95348093; PMID:7622480 !$#accession I40535 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-418 ##label RES !'##cross-references EMBL:U17292; NID:g984802; PIDN:AAC43455.1; !1PID:g984803 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D69669 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-34,'A',36-418 ##label KUN !'##cross-references GB:Z99105; GB:AL009126; NID:g2632457; !1PIDN:CAB12092.1; PID:g2632584 !'##experimental_source strain 168 GENETICS !$#gene opuAA CLASSIFICATION #superfamily glycine betaine/proline transport protein proV; !1ATP-binding cassette homology; CBS homology KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$49-246 #domain ATP-binding cassette homology #label ABC\ !$66-73 #region nucleotide-binding motif A (P-loop)\ !$289-335 #domain CBS homology #label CBS SUMMARY #length 418 #molecular-weight 46468 #checksum 1729 SEQUENCE /// ENTRY E69372 #type complete TITLE osmoprotection protein (proV) homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS E69372 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession E69372 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-361 ##label KLE !'##cross-references GB:AE001036; GB:AE000782; NID:g2689359; !1PIDN:AAB90260.1; PID:g2649615; TIGR:AF0981 CLASSIFICATION #superfamily glycine betaine/proline transport protein proV; !1ATP-binding cassette homology; CBS homology KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$24-218 #domain ATP-binding cassette homology #label ABC\ !$41-48 #region nucleotide-binding motif A (P-loop) SUMMARY #length 361 #molecular-weight 40891 #checksum 4681 SEQUENCE /// ENTRY A39741 #type complete TITLE cytochrome c biogenesis protein CycV - Bradyrhizobium japonicum ORGANISM #formal_name Bradyrhizobium japonicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS A39741 REFERENCE A39741 !$#authors Ramseier, T.M.; Winteler, H.V.; Hennecke, H. !$#journal J. Biol. Chem. (1991) 266:7793-7803 !$#title Discovery and sequence analysis of bacterial genes involved !1in the biogenesis of c-type cytochromes. !$#cross-references MUID:91210304; PMID:1850420 !$#accession A39741 !'##status preliminary !'##molecule_type DNA !'##residues 1-200 ##label RAM !'##cross-references GB:M60874; NID:g152073; PIDN:AAA26192.1; !1PID:g152074 CLASSIFICATION #superfamily short-chain ATP-binding cassette proteins; !1ATP-binding cassette homology KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$18-199 #domain ATP-binding cassette homology #label ABC\ !$35-42 #region nucleotide-binding motif A (P-loop) SUMMARY #length 200 #molecular-weight 21132 #checksum 4031 SEQUENCE /// ENTRY S23663 #type complete TITLE helA protein - Rhodobacter capsulatus ORGANISM #formal_name Rhodobacter capsulatus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S23663 REFERENCE S23662 !$#authors Beckman, D.L.; Trawick, D.R.; Kranz, R.G. !$#journal Genes Dev. (1992) 6:268-283 !$#title Bacterial cytochromes c biogenesis. !$#cross-references MUID:92146961; PMID:1310666 !$#accession S23663 !'##status preliminary !'##molecule_type DNA !'##residues 1-214 ##label BEC !'##cross-references EMBL:X63462; NID:g46022; PIDN:CAA45061.1; !1PID:g46024 CLASSIFICATION #superfamily short-chain ATP-binding cassette proteins; !1ATP-binding cassette homology KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$19-189 #domain ATP-binding cassette homology #label ABC\ !$36-43 #region nucleotide-binding motif A (P-loop) SUMMARY #length 214 #molecular-weight 22168 #checksum 8604 SEQUENCE /// ENTRY E64166 #type complete TITLE cytochrome c biogenesis protein CycV homolog - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES hypothetical protein HI1089 ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS E64166 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession E64166 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-212 ##label TIGR !'##cross-references GB:U32789; GB:L42023; NID:g1574642; !1PIDN:AAC22746.1; PID:g1574644; TIGR:HI1089 !'##note best homolog was a hypothetical protein from Escherichia coli CLASSIFICATION #superfamily short-chain ATP-binding cassette proteins; !1ATP-binding cassette homology KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$22-207 #domain ATP-binding cassette homology #label ABC\ !$39-46 #region nucleotide-binding motif A (P-loop) SUMMARY #length 212 #molecular-weight 24009 #checksum 2130 SEQUENCE /// ENTRY E71024 #type complete TITLE probable transport protein - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Sep-2000 ACCESSIONS E71024 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession E71024 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-222 ##label KAW !'##cross-references GB:AP000006; NID:g3236133; PIDN:BAA30597.1; !1PID:g3257914 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1490 CLASSIFICATION #superfamily short-chain ATP-binding cassette proteins; !1ATP-binding cassette homology KEYWORDS ATP FEATURE !$18-202 #domain ATP-binding cassette homology #label ABC SUMMARY #length 222 #molecular-weight 24762 #checksum 8589 SEQUENCE /// ENTRY S74028 #type complete TITLE sulfate transport protein homolog c0210 - Sulfolobus solfataricus ORGANISM #formal_name Sulfolobus solfataricus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S74028 REFERENCE S73076 !$#authors Sensen, C.W.; Klenk, H.P.; Singh, R.K.; Allard, G.; Chan, !1C.C.Y.; Liu, Q.Y.; Penny, S.L.; Young, F.; Schenk, M.E.; !1Gaasterland, T.; Doolittle, W.F.; Ragan, M.A.; Charlebois, !1R.L. !$#journal Mol. Microbiol. (1996) 22:175-191 !$#title Organizational characteristics and information content of an !1archaeal genome: 156 kb of sequence from Sulfolobus !1solfataricus P2. !$#cross-references MUID:97055432; PMID:8899719 !$#accession S74028 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-257 ##label SEN !'##cross-references EMBL:Y08256; NID:g1707679; PIDN:CAA69488.1; !1PID:g1707722 !'##experimental_source strain P2 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1September 1996 CLASSIFICATION #superfamily short-chain ATP-binding cassette proteins; !1ATP-binding cassette homology KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$16-197 #domain ATP-binding cassette homology #label ABC\ !$31-38 #region nucleotide-binding motif A (P-loop) SUMMARY #length 257 #molecular-weight 29158 #checksum 5954 SEQUENCE /// ENTRY A64780 #type complete TITLE probable ABC ransport protein ybbL - Escherichia coli (strain K-12) ALTERNATE_NAMES probable ABC transporter, ATP-binding protein ybbL ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS A64780 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64780 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-225 ##label BLAT !'##cross-references GB:AE000155; GB:U00096; NID:g1786692; !1PIDN:AAC73592.1; PID:g1786698; UWGP:b0490 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ybbL CLASSIFICATION #superfamily short-chain ATP-binding cassette proteins; !1ATP-binding cassette homology KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$23-213 #domain ATP-binding cassette homology #label ABC\ !$40-47 #region nucleotide-binding motif A (P-loop) SUMMARY #length 225 #molecular-weight 25382 #checksum 56 SEQUENCE /// ENTRY D64935 #type complete TITLE hypothetical protein b1756 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS D64935 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64935 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-217 ##label BLAT !'##cross-references GB:AE000270; GB:U00096; NID:g1788045; !1PIDN:AAC74826.1; PID:g1788053; UWGP:b1756 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily short-chain ATP-binding cassette proteins; !1ATP-binding cassette homology KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$17-207 #domain ATP-binding cassette homology #label ABC\ !$34-41 #region nucleotide-binding motif A (P-loop) SUMMARY #length 217 #molecular-weight 24016 #checksum 7949 SEQUENCE /// ENTRY B71694 #type complete TITLE ABC transporter potG - Rickettsia prowazekii ORGANISM #formal_name Rickettsia prowazekii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Nov-2000 ACCESSIONS B71694 REFERENCE A71630 !$#authors Andersson, S.G.E.; Zomorodipour, A.; Andersson, J.O.; !1Sicheritz-Ponten, T.; Alsmark, U.C.M.; Podowski, R.M.; !1Naeslund, A.K.; Eriksson, A.S.; Winkler, H.H.; Kurland, C.G. !$#journal Nature (1998) 396:133-140 !$#title The genome sequence of Rickettsia prowazekii and the origin !1of mitochondria. !$#cross-references MUID:99039499; PMID:9823893 !$#accession B71694 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-247 ##label AND !'##cross-references GB:AJ235271; GB:AJ235269; NID:g3868717; !1PIDN:CAA14828.1; PID:g3860928; GSPDB:GN00081 !'##experimental_source strain Madrid E GENETICS !$#gene potG; RP369 CLASSIFICATION #superfamily short-chain ATP-binding cassette proteins; !1ATP-binding cassette homology KEYWORDS ATP FEATURE !$22-217 #domain ATP-binding cassette homology #label ABC SUMMARY #length 247 #molecular-weight 27732 #checksum 5780 SEQUENCE /// ENTRY QREBPT #type complete TITLE histidine transport protein hisP - Salmonella typhimurium ALTERNATE_NAMES histidine permease inner membrane receptor protein P ORGANISM #formal_name Salmonella typhimurium DATE 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 08-Sep-2000 ACCESSIONS A03412 REFERENCE A94697 !$#authors Higgins, C.F.; Haag, P.D.; Nikaido, K.; Ardeshir, F.; !1Garcia, G.; Ames, G.F.L. !$#journal Nature (1982) 298:723-727 !$#title Complete nucleotide sequence and identification of membrane !1components of the histidine transport operon of Salmonella !1typhimurium. !$#cross-references MUID:82272316; PMID:7050725 !$#accession A03412 !'##molecule_type DNA !'##residues 1-258 ##label HIG !'##cross-references GB:V01373; NID:g47730; PIDN:CAA24662.1; PID:g47734 !'##note this protein, the receptor for histidine-binding protein J and !1lysine-arginine-ornithine-binding protein (LAO), is one of !1the membrane-bound components of the high-affinity histidine !1permease, a binding-protein-dependent transport system; the !1other components are proteins Q, M, and J GENETICS !$#gene hisP !$#map_position 48.5 CLASSIFICATION #superfamily short-chain ATP-binding cassette proteins; !1ATP-binding cassette homology KEYWORDS ATP; histidine transport; nucleotide binding; P-loop FEATURE !$22-229 #domain ATP-binding cassette homology #label ABC\ !$39-46 #region nucleotide-binding motif A (P-loop)\ !$174-178 #region nucleotide-binding motif B SUMMARY #length 258 #molecular-weight 28771 #checksum 1098 SEQUENCE /// ENTRY BVHIXA #type complete TITLE capsulation protein bexA - Haemophilus influenzae ORGANISM #formal_name Haemophilus influenzae DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 08-Sep-2000 ACCESSIONS S12235; A28781; C41654 REFERENCE S12232 !$#authors Kroll, J.S.; Loynds, B.; Brophy, L.N.; Moxon, E.R. !$#journal Mol. Microbiol. (1990) 4:1853-1862 !$#title The bex locus in encapsulated Haemophilus influenzae: a !1chromosomal region involved in capsule polysaccharide !1export. !$#cross-references MUID:91186821; PMID:2082145 !$#accession S12235 !'##molecule_type DNA !'##residues 1-217 ##label KR1 !'##cross-references EMBL:X54987; NID:g45295; PIDN:CAA38734.1; !1PID:g45300 !'##experimental_source serotype B REFERENCE A28781 !$#authors Kroll, J.S.; Hopkins, I.; Moxon, E.R. !$#journal Cell (1988) 53:347-356 !$#title Capsule loss in H. influenzae type b occurs by !1recombination-mediated disruption of a gene essential for !1polysaccharide export. !$#cross-references MUID:88210460; PMID:3284653 !$#accession A28781 !'##molecule_type DNA !'##residues 1-217 ##label KR2 !'##cross-references EMBL:M19995; NID:g148866; PIDN:AAA24944.1; !1PID:g148867 REFERENCE A41654 !$#authors Kroll, J.S.; Langford, P.R.; Loynds, B.M. !$#journal J. Bacteriol. (1991) 173:7449-7457 !$#title Copper-zinc superoxide dismutase of Haemophilus influenzae !1and Haemophilus parainfluenzae. !$#cross-references MUID:92041655; PMID:1938942 !$#accession C41654 !'##status preliminary !'##molecule_type DNA !'##residues 'DQ',215-217 ##label KRO GENETICS !$#gene bexA CLASSIFICATION #superfamily short-chain ATP-binding cassette proteins; !1ATP-binding cassette homology KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$21-197 #domain ATP-binding cassette homology #label ABC\ !$38-45 #region nucleotide-binding motif A (P-loop)\ !$150-154 #region nucleotide-binding motif B\ !$44 #binding_site ATP/GTP (Lys) #status predicted SUMMARY #length 217 #molecular-weight 24746 #checksum 7525 SEQUENCE /// ENTRY CEECFE #type complete TITLE cell division ATP-binding protein ftsE - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 01-Mar-2002 ACCESSIONS S03131; S47682; B65143 REFERENCE S03129 !$#authors Gill, D.R.; Hatfull, G.F.; Salmond, G.P.C. !$#journal Mol. Gen. Genet. (1986) 205:134-145 !$#title A new cell division operon in Escherichia coli. !$#cross-references MUID:87089083; PMID:3025556 !$#accession S03131 !'##molecule_type DNA !'##residues 1-222 ##label GIL !'##cross-references EMBL:X04398; NID:g41496; PIDN:CAA27985.1; !1PID:g41499 REFERENCE S47666 !$#authors Plunkett, G. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S47682 !'##molecule_type DNA !'##residues 1-222 ##label PLU !'##cross-references EMBL:U00039; NID:g466582; PIDN:AAB18438.1; !1PID:g466599 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65143 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-222 ##label BLAT !'##cross-references GB:AE000422; GB:U00096; NID:g1789868; !1PIDN:AAC76488.1; PID:g1789873; UWGP:b3463 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ftsE !$#map_position 76 min CLASSIFICATION #superfamily short-chain ATP-binding cassette proteins; !1ATP-binding cassette homology KEYWORDS ATP; cell division; inner membrane; nucleotide binding; !1P-loop FEATURE !$18-213 #domain ATP-binding cassette homology #label ABC\ !$35-42 #region nucleotide-binding motif A (P-loop)\ !$158-163 #region nucleotide-binding motif B SUMMARY #length 222 #molecular-weight 24439 #checksum 2169 SEQUENCE /// ENTRY QRECGQ #type complete TITLE glutamine transport protein glnQ - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 01-Mar-2002 ACCESSIONS S03183; A64818 REFERENCE S03181 !$#authors Nohno, T.; Saito, T.; Hong, J. !$#journal Mol. Gen. Genet. (1986) 205:260-269 !$#title Cloning and complete nucleotide sequence of the Escherichia !1coli glutamine permease operon (glnHPQ). !$#cross-references MUID:87115160; PMID:3027504 !$#accession S03183 !'##molecule_type DNA !'##residues 1-240 ##label NOH !'##cross-references EMBL:X14180; NID:g41568; PIDN:CAA32384.1; !1PID:g581098 !'##experimental_source strain K12 PSM2 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64818 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-240 ##label BLAT !'##cross-references GB:AE000183; GB:U00096; NID:g1787025; !1PIDN:AAC73896.1; PID:g1787029; UWGP:b0809 !'##experimental_source strain K-12, substrain MG1655 COMMENT This protein is the hydrophilic nucleotide-binding component !1of the binding protein-dependent transport system for !1glutamine. GENETICS !$#gene glnQ !$#map_position 18 min !$#start_codon GTG CLASSIFICATION #superfamily short-chain ATP-binding cassette proteins; !1ATP-binding cassette homology KEYWORDS ATP; glutamine transport; inner membrane; nucleotide !1binding; P-loop FEATURE !$17-212 #domain ATP-binding cassette homology #label ABC\ !$34-41 #region nucleotide-binding motif A (P-loop)\ !$157-161 #region nucleotide-binding motif B SUMMARY #length 240 #molecular-weight 26731 #checksum 4153 SEQUENCE /// ENTRY B39741 #type complete TITLE cytochrome c biogenesis protein CycW - Bradyrhizobium japonicum ORGANISM #formal_name Bradyrhizobium japonicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B39741 REFERENCE A39741 !$#authors Ramseier, T.M.; Winteler, H.V.; Hennecke, H. !$#journal J. Biol. Chem. (1991) 266:7793-7803 !$#title Discovery and sequence analysis of bacterial genes involved !1in the biogenesis of c-type cytochromes. !$#cross-references MUID:91210304; PMID:1850420 !$#accession B39741 !'##status preliminary !'##molecule_type DNA !'##residues 1-222 ##label RAM !'##cross-references GB:M60874; NID:g152073; PIDN:AAA26193.1; !1PID:g152075 CLASSIFICATION #superfamily cytochrome c biogenesis protein CycW KEYWORDS transmembrane protein SUMMARY #length 222 #molecular-weight 22667 #checksum 2055 SEQUENCE /// ENTRY S23664 #type complete TITLE helB protein - Rhodobacter capsulatus ORGANISM #formal_name Rhodobacter capsulatus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S23664 REFERENCE S23662 !$#authors Beckman, D.L.; Trawick, D.R.; Kranz, R.G. !$#journal Genes Dev. (1992) 6:268-283 !$#title Bacterial cytochromes c biogenesis. !$#cross-references MUID:92146961; PMID:1310666 !$#accession S23664 !'##status preliminary !'##molecule_type DNA !'##residues 1-218 ##label BEC !'##cross-references EMBL:X63462; NID:g46022; PIDN:CAA45062.1; !1PID:g46025 CLASSIFICATION #superfamily cytochrome c biogenesis protein CycW KEYWORDS transmembrane protein SUMMARY #length 218 #molecular-weight 22611 #checksum 9931 SEQUENCE /// ENTRY F64166 #type complete TITLE heme export protein B - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS F64166 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession F64166 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-221 ##label TIGR !'##cross-references GB:U32789; GB:L42023; NID:g1574642; !1PIDN:AAC22747.1; PID:g1574645; TIGR:HI1090 CLASSIFICATION #superfamily cytochrome c biogenesis protein CycW KEYWORDS transmembrane protein SUMMARY #length 221 #molecular-weight 23643 #checksum 4067 SEQUENCE /// ENTRY C39741 #type complete TITLE hypothetical 29K protein (cycW-cycX intergenic region) - Bradyrhizobium japonicum ORGANISM #formal_name Bradyrhizobium japonicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C39741 REFERENCE A39741 !$#authors Ramseier, T.M.; Winteler, H.V.; Hennecke, H. !$#journal J. Biol. Chem. (1991) 266:7793-7803 !$#title Discovery and sequence analysis of bacterial genes involved !1in the biogenesis of c-type cytochromes. !$#cross-references MUID:91210304; PMID:1850420 !$#accession C39741 !'##status preliminary !'##molecule_type DNA !'##residues 1-263 ##label RAM !'##cross-references GB:M60874; NID:g152073; PIDN:AAA26194.1; !1PID:g152076 CLASSIFICATION #superfamily helC protein KEYWORDS transmembrane protein SUMMARY #length 263 #molecular-weight 28831 #checksum 6315 SEQUENCE /// ENTRY S23665 #type complete TITLE helC protein - Rhodobacter capsulatus ORGANISM #formal_name Rhodobacter capsulatus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S23665 REFERENCE S23662 !$#authors Beckman, D.L.; Trawick, D.R.; Kranz, R.G. !$#journal Genes Dev. (1992) 6:268-283 !$#title Bacterial cytochromes c biogenesis. !$#cross-references MUID:92146961; PMID:1310666 !$#accession S23665 !'##status preliminary !'##molecule_type DNA !'##residues 1-242 ##label BEC !'##cross-references EMBL:X63462; NID:g46022; PIDN:CAA45063.1; !1PID:g46026 CLASSIFICATION #superfamily helC protein KEYWORDS transmembrane protein SUMMARY #length 242 #molecular-weight 27196 #checksum 1868 SEQUENCE /// ENTRY S70854 #type complete TITLE probable heme transport protein chain 2 - evening primrose mitochondrion ALTERNATE_NAMES probable ABC-type heme transporter chain 2 ORGANISM #formal_name mitochondrion Oenothera villaricae #common_name evening primrose DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S70854; S51482; S42983 REFERENCE S51482 !$#authors Jekabsons, W.; Schuster, W. !$#journal Mol. Gen. Genet. (1995) 246:166-173 !$#title orf250 encodes a second subunit of an ABC-type heme !1transporter in Oenothera mitochondria. !$#cross-references MUID:95166173; PMID:7862087 !$#accession S70854 !'##molecule_type mRNA !'##residues 1-250 ##label JEK !'##cross-references EMBL:X78037 !'##note the source is designated as Oenothera berteriana !$#accession S51482 !'##molecule_type DNA !'##residues 1-25,'R',27-34,'H',36-38,'R',40-44,'L',46-53,'P',55-59,'A', !161,'R',63-110,'R',112-131,'S',133,'L',135-145,'P',147-148, !1'P',150-152,'S',154,'RA',157,'P',159-165,'S',167-173,'P', !1175-182,'S',184-189,'P',191,'P',193-202,'P',204,'S',206,'R', !1208-216,'P',218-221,'P',223-250 ##label JEW !'##cross-references EMBL:X78037; NID:g459534; PIDN:CAA54967.1; !1PID:g459535 !'##note the source is designated as Oenothera berteriana !'##note the differences are due to RNA editing GENETICS !$#genome mitochondrion CLASSIFICATION #superfamily helC protein KEYWORDS mitochondrion; RNA editing; transmembrane protein SUMMARY #length 250 #molecular-weight 28239 #checksum 4265 SEQUENCE /// ENTRY G64166 #type complete TITLE heme export protein C - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS G64166 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession G64166 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-246 ##label TIGR !'##cross-references GB:U32789; GB:L42023; NID:g1574642; !1PIDN:AAC22748.1; PID:g1574646; TIGR:HI1091 CLASSIFICATION #superfamily helC protein KEYWORDS transmembrane protein SUMMARY #length 246 #molecular-weight 27716 #checksum 6214 SEQUENCE /// ENTRY D39741 #type complete TITLE cytochrome c biogenesis protein CycX - Bradyrhizobium japonicum ORGANISM #formal_name Bradyrhizobium japonicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS D39741 REFERENCE A39741 !$#authors Ramseier, T.M.; Winteler, H.V.; Hennecke, H. !$#journal J. Biol. Chem. (1991) 266:7793-7803 !$#title Discovery and sequence analysis of bacterial genes involved !1in the biogenesis of c-type cytochromes. !$#cross-references MUID:91210304; PMID:1850420 !$#accession D39741 !'##status preliminary !'##molecule_type DNA !'##residues 1-132 ##label RAM !'##cross-references GB:M60874; NID:g152073; PIDN:AAA26196.1; !1PID:g551962 CLASSIFICATION #superfamily cytochrome c biogenesis protein CycX KEYWORDS redox-active disulfide FEATURE !$30-33 #disulfide_bonds redox-active #status predicted SUMMARY #length 132 #molecular-weight 14457 #checksum 7246 SEQUENCE /// ENTRY A47384 #type complete TITLE cytochrome c biogenesis protein CycX homolog HelX [similarity] - Rhodobacter capsulatus ORGANISM #formal_name Rhodobacter capsulatus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A47384 REFERENCE A47384 !$#authors Beckman, D.L.; Kranz, R.G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:2179-2183 !$#title Cytochromes c biogenesis in a photosynthetic bacterium !1requires a periplasmic thioredoxin-like protein. !$#cross-references MUID:93211925; PMID:8384715 !$#accession A47384 !'##status preliminary !'##molecule_type DNA !'##residues 1-176 ##label BEC !'##cross-references GB:M96013; NID:g294657; PIDN:AAA03178.1; !1PID:g294659 !'##experimental_source SB1003 !'##note sequence extracted from NCBI backbone (NCBIN:128013, !1NCBIP:128015) CLASSIFICATION #superfamily cytochrome c biogenesis protein CycX KEYWORDS redox-active disulfide FEATURE !$75-78 #disulfide_bonds redox-active #status predicted SUMMARY #length 176 #molecular-weight 18736 #checksum 1881 SEQUENCE /// ENTRY B64167 #type complete TITLE cytochrome c biogenesis protein CycX homolog ccmG precursor [similarity] - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES disulfide interchange protein dsbE; thiol-disulfide interchange protein dsbE ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS B64167 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession B64167 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-181 ##label TIGR !'##cross-references GB:U32789; GB:L42023; NID:g1574642; !1PIDN:AAC22752.1; PID:g1574650; TIGR:HI1095 GENETICS !$#gene dsbE CLASSIFICATION #superfamily cytochrome c biogenesis protein CycX KEYWORDS redox-active disulfide FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-181 #product cytochrome c biogenesis protein cycX homolog !8ccmG #status predicted #label MAT\ !$78-81 #disulfide_bonds redox-active #status predicted SUMMARY #length 181 #molecular-weight 20535 #checksum 2253 SEQUENCE /// ENTRY I64161 #type complete TITLE cytochrome c biogenesis protein CycX homolog HI0935 [similarity] - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS I64161 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession I64161 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-176 ##label TIGR !'##cross-references GB:U32775; GB:L42023; NID:g1573951; !1PIDN:AAC22593.1; PID:g1573956; TIGR:HI0935 !'##note best homolog was a hypothetical protein from Escherichia coli CLASSIFICATION #superfamily cytochrome c biogenesis protein CycX KEYWORDS redox-active disulfide FEATURE !$75-78 #disulfide_bonds redox-active #status predicted SUMMARY #length 176 #molecular-weight 19926 #checksum 9829 SEQUENCE /// ENTRY S77665 #type complete TITLE integral membrane protein HP0228 homolog - Mycobacterium smegmatis ORGANISM #formal_name Mycobacterium smegmatis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JC6190; S77664; S77665 REFERENCE JC6190 !$#authors Barsom, E.K.; Hatfull, G.F. !$#journal Gene (1997) 185:127-132 !$#title A putative ABC-transport operon of Mycobacterium smegmatis. !$#cross-references MUID:97186707; PMID:9034323 !$#accession JC6190 !'##status preliminary !'##molecule_type DNA !'##residues 1-498 ##label BA2 !'##cross-references GB:U50335; NID:g1477566; PIDN:AAB41652.1; !1PID:g1477568 REFERENCE S77663 !$#authors Barsom, E.K.; Hatfull, G.F. !$#journal Mol. Microbiol. (1996) 21:159-170 !$#title Characterization of a Mycobacterium smegmatis gene that !1confers resistance to phages L5 and D29 when overexpressed. !$#cross-references MUID:97000357; PMID:8843442 !$#accession S77664 !'##molecule_type DNA !'##residues 477-498 ##label BAR !'##cross-references EMBL:U50335 CLASSIFICATION #superfamily integral membrane protein HP0228 KEYWORDS membrane protein SUMMARY #length 498 #molecular-weight 51835 #checksum 926 SEQUENCE /// ENTRY S77411 #type complete TITLE integral membrane protein HP0228 homolog 1 - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein slr1229 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S77411 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S77411 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-498 ##label KAN !'##cross-references EMBL:D90906; GB:AB001339; NID:g1652492; !1PIDN:BAA17514.1; PID:g1652593 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily integral membrane protein HP0228 SUMMARY #length 498 #molecular-weight 54495 #checksum 5215 SEQUENCE /// ENTRY D64548 #type complete TITLE integral membrane protein HP0228 - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS D64548 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession D64548 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-390 ##label TOM !'##cross-references GB:AE000542; GB:AE000511; NID:g2313310; !1PIDN:AAD07294.1; PID:g2313317; TIGR:HP0228 CLASSIFICATION #superfamily integral membrane protein HP0228 SUMMARY #length 390 #molecular-weight 42124 #checksum 5081 SEQUENCE /// ENTRY F64614 #type complete TITLE conserved hypothetical integral membrane protein HP0758 - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS F64614 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession F64614 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-437 ##label TOM !'##cross-references GB:AE000588; GB:AE000511; NID:g2313880; !1PIDN:AAD07806.1; PID:g2313884; TIGR:HP0758 CLASSIFICATION #superfamily conserved integral membrane protein HP0758 SUMMARY #length 437 #molecular-weight 46720 #checksum 8883 SEQUENCE /// ENTRY A64148 #type complete TITLE hypothetical protein HI0325 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A64148 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession A64148 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-450 ##label TIGR !'##cross-references GB:U32717; GB:L42023; NID:g1573283; !1PIDN:AAC21988.1; PID:g1573294; TIGR:HI0325 !'##note best homolog was a hypothetical protein from Vibrio !1parahaemolyticus CLASSIFICATION #superfamily conserved integral membrane protein HP0758 SUMMARY #length 450 #molecular-weight 47439 #checksum 9316 SEQUENCE /// ENTRY B25937 #type complete TITLE arsenical pump membrane protein - Escherichia coli plasmid R773 ORGANISM #formal_name Escherichia coli DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS B25937; S09409 REFERENCE A92563 !$#authors Chen, C.M.; Misra, T.K.; Silver, S.; Rosen, B.P. !$#journal J. Biol. Chem. (1986) 261:15030-15038 !$#title Nucleotide sequence of the structural genes for an anion !1pump. !$#cross-references MUID:87033737; PMID:3021763 !$#accession B25937 !'##molecule_type DNA !'##residues 1-429 ##label CHE !'##cross-references GB:J02591; NID:g151856; PIDN:AAA21095.1; !1PID:g151858 REFERENCE S09409 !$#authors San Francisco, M.J.D.; Tisa, L.S.; Rosen, B.P. !$#journal Mol. Microbiol. (1989) 3:15-21 !$#title Identification of the membrane component of the anion pump !1encoded by the arsenical resistance operon of R-factor R773. !$#cross-references MUID:89237894; PMID:2523997 !$#accession S09409 !'##molecule_type DNA !'##residues 272-280 ##label SAN GENETICS !$#gene arsB !$#genome plasmid R773 CLASSIFICATION #superfamily arsenical pump membrane protein KEYWORDS toxic oxyanion resistance; transmembrane protein SUMMARY #length 429 #molecular-weight 45598 #checksum 4183 SEQUENCE /// ENTRY B41902 #type complete TITLE arsenical pump membrane protein - Staphylococcus xylosus ORGANISM #formal_name Staphylococcus xylosus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 28-May-1999 ACCESSIONS B41902 REFERENCE A41902 !$#authors Rosenstein, R.; Peschel, A.; Wieland, B.; Gotz, F. !$#journal J. Bacteriol. (1992) 174:3676-3683 !$#title Expression and regulation of the antimonite, arsenite, and !1arsenate resistance operon of Staphylococcus xylosus plasmid !1pSX267. !$#cross-references MUID:92276350; PMID:1534327 !$#contents pSX267 !$#accession B41902 !'##molecule_type DNA !'##residues 1-429 ##label ROS !'##cross-references GB:M80565; NID:g155343; PIDN:AAA27588.1; !1PID:g155345 !'##note sequence extracted from NCBI backbone (NCBIN:104639, !1NCBIP:104644) GENETICS !$#gene arsB CLASSIFICATION #superfamily arsenical pump membrane protein KEYWORDS toxic oxyanion resistance; transmembrane protein SUMMARY #length 429 #molecular-weight 46561 #checksum 8227 SEQUENCE /// ENTRY C41903 #type complete TITLE arsenical pump membrane protein - Staphylococcus aureus ORGANISM #formal_name Staphylococcus aureus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 28-May-1999 ACCESSIONS C41903 REFERENCE A41903 !$#authors Ji, G.; Silver, S. !$#journal J. Bacteriol. (1992) 174:3684-3694 !$#title Regulation and expression of the arsenic resistance operon !1from Staphylococcus aureus plasmid pI258. !$#cross-references MUID:92276351; PMID:1534328 !$#contents pI258 !$#accession C41903 !'##molecule_type DNA !'##residues 1-429 ##label JI1 !'##cross-references GB:M86824; NID:g150725; PIDN:AAA25637.1; !1PID:g150728 !'##note sequence extracted from NCBI backbone (NCBIN:104669, !1NCBIP:104672) GENETICS !$#gene arsB CLASSIFICATION #superfamily arsenical pump membrane protein KEYWORDS toxic oxyanion resistance; transmembrane protein SUMMARY #length 429 #molecular-weight 46483 #checksum 7851 SEQUENCE /// ENTRY BWHIXD #type complete TITLE bexD protein - Haemophilus influenzae ORGANISM #formal_name Haemophilus influenzae DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS S12232 REFERENCE S12232 !$#authors Kroll, J.S.; Loynds, B.; Brophy, L.N.; Moxon, E.R. !$#journal Mol. Microbiol. (1990) 4:1853-1862 !$#title The bex locus in encapsulated Haemophilus influenzae: a !1chromosomal region involved in capsule polysaccharide !1export. !$#cross-references MUID:91186821; PMID:2082145 !$#accession S12232 !'##molecule_type DNA !'##residues 1-394 ##label KRO !'##cross-references EMBL:X54987; NID:g45295; PIDN:CAA38730.1; !1PID:g45296 GENETICS !$#gene bexD CLASSIFICATION #superfamily bexD protein SUMMARY #length 394 #molecular-weight 41973 #checksum 7096 SEQUENCE /// ENTRY BWHIXC #type complete TITLE polysaccharide export protein bexC - Haemophilus influenzae ORGANISM #formal_name Haemophilus influenzae DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 05-May-2000 ACCESSIONS S12233 REFERENCE S12232 !$#authors Kroll, J.S.; Loynds, B.; Brophy, L.N.; Moxon, E.R. !$#journal Mol. Microbiol. (1990) 4:1853-1862 !$#title The bex locus in encapsulated Haemophilus influenzae: a !1chromosomal region involved in capsule polysaccharide !1export. !$#cross-references MUID:91186821; PMID:2082145 !$#accession S12233 !'##molecule_type DNA !'##residues 1-377 ##label KRO !'##cross-references EMBL:X54987; NID:g45295; PIDN:CAA38731.1; !1PID:g45297 !'##note it is uncertain whether Met-1 or Met-20 is the initiator GENETICS !$#gene bexC CLASSIFICATION #superfamily bexC protein KEYWORDS transmembrane protein SUMMARY #length 377 #molecular-weight 42292 #checksum 8132 SEQUENCE /// ENTRY BWHIXB #type complete TITLE bexB protein - Haemophilus influenzae ORGANISM #formal_name Haemophilus influenzae DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS S12234 REFERENCE S12232 !$#authors Kroll, J.S.; Loynds, B.; Brophy, L.N.; Moxon, E.R. !$#journal Mol. Microbiol. (1990) 4:1853-1862 !$#title The bex locus in encapsulated Haemophilus influenzae: a !1chromosomal region involved in capsule polysaccharide !1export. !$#cross-references MUID:91186821; PMID:2082145 !$#accession S12234 !'##molecule_type DNA !'##residues 1-265 ##label KRO !'##cross-references EMBL:X54987; NID:g45295; PIDN:CAA38733.1; !1PID:g45299 GENETICS !$#gene bexB CLASSIFICATION #superfamily bexB protein KEYWORDS transmembrane protein SUMMARY #length 265 #molecular-weight 30195 #checksum 4508 SEQUENCE /// ENTRY DVHU1 #type complete TITLE multidrug resistance protein 1 - human ALTERNATE_NAMES P-glycoprotein 1 ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1990 #sequence_revision 18-Aug-1995 #text_change 19-Jan-2001 ACCESSIONS A34914; PS0162; S15500; A25059; S43838; I52238; I65204 REFERENCE A34914 !$#authors Chen, C.; Clark, D.; Ueda, K.; Pastan, I.; Gottesman, M.M.; !1Roninson, I.B. !$#journal J. Biol. Chem. (1990) 265:506-514 !$#title Genomic organization of the human multidrug resistance !1(MDR1) gene and origin of P-glycoproteins. !$#cross-references MUID:90094448; PMID:1967175 !$#accession A34914 !'##molecule_type DNA !'##residues 1-1280 ##label CHE !'##cross-references GB:M29447; GB:J05168; NID:g187496; PIDN:AAA59576.1; !1PID:g386862 REFERENCE PS0162 !$#authors Kioka, N.; Yamano, Y.; Komano, T.; Ueda, K. !$#submission submitted to JIPID, April 1991 !$#accession PS0162 !'##molecule_type DNA !'##residues 1-22 ##label KIO REFERENCE S15500 !$#authors Kioka, N.; Yamano, Y.; Komano, T.; Ueda, K. !$#submission submitted to the EMBL Data Library, April 1991 !$#description Transcriptional regulation of multidrug resistance gene !1(MDR1) expression in response to arsenite treatment. !$#accession S15500 !'##molecule_type DNA !'##residues 1-22,'R' ##label KI2 !'##cross-references EMBL:X58723; NID:g34522; PIDN:CAA41558.1; !1PID:g34523 REFERENCE A25059 !$#authors Chen, C.; Chin, J.E.; Ueda, K.; Clark, D.P.; Pastan, I.; !1Gottesman, M.M.; Roninson, I.B. !$#journal Cell (1986) 47:381-389 !$#title Internal duplication and homology with bacterial transport !1proteins in the mdr1 (P-Glycoprotein) gene from !1multidrug-resistant human cells. !$#cross-references MUID:87028230; PMID:2876781 !$#accession A25059 !'##molecule_type mRNA !'##residues 1-184,'V',186-1280 ##label CH2 !'##cross-references GB:M14758; NID:g187468; PIDN:AAA59575.1; !1PID:g307180 REFERENCE S43838 !$#authors Chambers, T.C.; Pohl, J.; Glass, D.B.; Kuo, J.F. !$#journal Biochem. J. (1994) 299:309-315 !$#title Phosphorylation by protein kinase C and cyclic AMP-dependent !1protein kinase of synthetic peptides derived from the linker !1region of human P-glycoprotein. !$#cross-references MUID:94220047; PMID:7909431 !$#accession S43838 !'##molecule_type protein !'##residues 656-689 ##label CHA REFERENCE I52238 !$#authors Gekeler, V.; Weger, S.; Probst, H. !$#journal Biochem. Biophys. Res. Commun. (1990) 169:796-802 !$#title mdr1/P-glycoprotein gene segments analyzed from various !1human leukemic cell lines exhibiting different multidrug !1resistance profiles. !$#cross-references MUID:90290529; PMID:1972623 !$#accession I52238 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 178-215 ##label RES !'##cross-references GB:M37724; NID:g183537; PIDN:AAA88047.1; !1PID:g553314 !$#accession I65204 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 800-856 ##label RE2 !'##cross-references GB:M37725; NID:g183538; PIDN:AAA88048.1; !1PID:g553315 COMMENT This is an integral membrane protein overproduced in !1multidrug-resistant cells. It decreases drug accumulation by !1acting as an energy-dependent efflux pump that has broad !1specificity for structurally and functionally unrelated !1lipophilic antitumor drugs. GENETICS !$#gene GDB:PGY1; MDR1 !'##cross-references GDB:120712; OMIM:171050 !$#map_position 7q21-7q21 CLASSIFICATION #superfamily multidrug resistance protein; ATP-binding !1cassette homology KEYWORDS ATP; duplication; glycoprotein; nucleotide binding; P-loop; !1phosphoprotein; transmembrane protein FEATURE !$1-638,653-1280 #region duplication\ !$49-350 #domain hydrophobic #label HB1\ !$351-637 #domain hydrophilic #label HL1\ !$410-604 #domain ATP-binding cassette homology #label ABC1\ !$427-434 #region nucleotide-binding motif A (P-loop)\ !$551-555 #region nucleotide-binding motif B\ !$638-708 #domain linker #label LIN\ !$709-993 #domain hydrophobic #label HB2\ !$994-1280 #domain hydrophilic #label HL2\ !$1053-1249 #domain ATP-binding cassette homology #label ABC2\ !$1070-1077 #region nucleotide-binding motif A (P-loop)\ !$1196-1200 #region nucleotide-binding motif B\ !$91,94,99 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$433 #binding_site ATP (Lys) #status predicted\ !$661,667,671 #binding_site phosphate (Ser) (covalent) (by protein !8kinase C) #status experimental\ !$667,671,683 #binding_site phosphate (Ser) (covalent) (by !8cAMP-dependent kinase) #status experimental\ !$1076 #binding_site ATP (Lys) #status predicted SUMMARY #length 1280 #molecular-weight 141461 #checksum 3889 SEQUENCE /// ENTRY DVHU3 #type complete TITLE multidrug resistance protein 3 - human ALTERNATE_NAMES P-glycoprotein MDR3 ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 19-Jan-2001 ACCESSIONS JS0051; S01346; A42213; I38015 REFERENCE JS0051 !$#authors van der Bliek, A.M.; Kooiman, P.M.; Schneider, C.; Borst, P. !$#journal Gene (1988) 71:401-411 !$#title Sequence of mdr3 cDNA encoding a human P-glycoprotein. !$#cross-references MUID:89138016; PMID:2906314 !$#accession JS0051 !'##molecule_type mRNA !'##residues 1-1279 ##label VA1 !'##cross-references GB:M23234; NID:g187501; PIDN:AAA36207.1; !1PID:g307181 REFERENCE S01346 !$#authors van der Bliek, A.M.; Baas, F.; ten Houte de Lange, T.; !1Kooiman, P.M.; van der Velde-Koerts, T.; Borst, P. !$#journal EMBO J. (1987) 6:3325-3331 !$#title The human mdr3 gene encodes a novel P-glycoprotein homologue !1and gives rise to alternatively spliced mRNAs in liver. !$#cross-references MUID:88111519; PMID:2892668 !$#accession S01346 !'##molecule_type mRNA !'##residues 856-1093,'FVDFGFQ',1094-1279 ##label VA2 !'##cross-references EMBL:X06181; NID:g34524; PIDN:CAA29547.1; !1PID:g34525 REFERENCE A42213 !$#authors Lincke, C.R.; Smit, J.J.M.; van der Velde-Koerts, T.; Borst, !1P. !$#journal J. Biol. Chem. (1991) 266:5303-5310 !$#title Structure of the human MDR3 gene and physical mapping of the !1human MDR locus. !$#cross-references MUID:91161629; PMID:2002063 !$#accession A42213 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-1279 ##label LIN REFERENCE I38015 !$#authors Smit, J.J.; Mol, C.A.; van Deemter, L.; Wagenaar, E.; !1Schinkel, A.H.; Borst, P. !$#journal Biochim. Biophys. Acta (1995) 1261:44-56 !$#title Characterization of the promoter region of the human MDR3 !1P-glycoprotein gene. !$#cross-references MUID:95200972; PMID:7893760 !$#accession I38015 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-61,'RGSSRVDLQAC' ##label RES !'##cross-references EMBL:Z35284; NID:g1006662; PIDN:CAA84542.1; !1PID:g1006663 COMMENT This is an integral membrane protein overproduced in !1multidrug-resistant cells. It decreases drug accumulation by !1acting as an energy-dependent efflux pump that has broad !1specificity for structurally and functionally unrelated !1lipophilic antitumor drugs. GENETICS !$#gene GDB:PGY3; MDR3 !'##cross-references GDB:120713; OMIM:171060 !$#map_position 7q21-7q21 CLASSIFICATION #superfamily multidrug resistance protein; ATP-binding !1cassette homology KEYWORDS ATP; duplication; glycoprotein; nucleotide binding; P-loop; !1transmembrane protein FEATURE !$1-640,653-1279 #region duplication\ !$412-606 #domain ATP-binding cassette homology #label ABC1\ !$429-436 #region nucleotide-binding motif A (P-loop)\ !$553-557 #region nucleotide-binding motif B\ !$638-694 #domain linker #label LINK\ !$1052-1248 #domain ATP-binding cassette homology #label ABC2\ !$1069-1076 #region nucleotide-binding motif A (P-loop)\ !$1195-1199 #region nucleotide-binding motif B\ !$91,97 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$435 #binding_site ATP (Lys) #status predicted\ !$1075 #binding_site ATP (Lys) #status predicted SUMMARY #length 1279 #molecular-weight 140681 #checksum 9907 SEQUENCE /// ENTRY DVMS1 #type complete TITLE multidrug resistance protein 1 - mouse ALTERNATE_NAMES P-glycoprotein 1 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 19-Jan-2001 ACCESSIONS A33719; A25057; I57510 REFERENCE A33719 !$#authors Raymond, M.; Gros, P. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:6488-6492 !$#title Mammalian multidrug-resistance gene: correlation of exon !1organization with structural domains and duplication of an !1ancestral gene. !$#cross-references MUID:89367274; PMID:2570420 !$#accession A33719 !'##molecule_type DNA !'##residues 1-1276 ##label RAY REFERENCE A25057 !$#authors Gros, P.; Croop, J.; Housman, D. !$#journal Cell (1986) 47:371-380 !$#title Mammalian multidrug resistance gene: complete cDNA sequence !1indicates strong homology to bacterial transport proteins. !$#cross-references MUID:87028229; PMID:3768958 !$#accession A25057 !'##molecule_type mRNA !'##residues 1-1276 ##label GRO !'##cross-references GB:M14757; NID:g199100; PIDN:AAA79005.1; !1PID:g387426 REFERENCE I57510 !$#authors Raymond, M.; Gros, P. !$#journal Mol. Cell. Biol. (1990) 10:6036-6040 !$#title Cell-specific activity of cis-acting regulatory elements in !1the promoter of the mouse multidrug resistance gene mdr1. !$#cross-references MUID:91042535; PMID:2248681 !$#accession I57510 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-21 ##label RES !'##cross-references GB:M60348; NID:g199102; PIDN:AAA39513.1; !1PID:g554199 COMMENT This is an integral membrane protein overproduced in !1multidrug-resistant cells. It decreases drug accumulation by !1acting as an energy-dependent efflux pump that has broad !1specificity for structurally and functionally unrelated !1lipophilic antitumor drugs. GENETICS !$#gene mdr1 (pgp1) !$#introns 21/2; 38/3; 92/1; 111/2; 175/2; 233/3; 274/2; 332/3; 370/3; !1407/3; 449/3; 517/3; 574/3; 628/3; 686/3; 735/3; 771/3; 797/ !13; 821/3; 893/3; 926/2; 973/2; 1026/3; 1092/3; 1161/3; 1210/ !13 CLASSIFICATION #superfamily multidrug resistance protein; ATP-binding !1cassette homology KEYWORDS ATP; duplication; glycoprotein; nucleotide binding; P-loop; !1transmembrane protein FEATURE !$1-637,653-1276 #region duplication\ !$409-603 #domain ATP-binding cassette homology #label ABC1\ !$426-433 #region nucleotide-binding motif A (P-loop)\ !$550-554 #region nucleotide-binding motif B\ !$1051-1247 #domain ATP-binding cassette homology #label ABC2\ !$1068-1075 #region nucleotide-binding motif A (P-loop)\ !$1194-1198 #region nucleotide-binding motif B\ !$73,91,96,103 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$432 #binding_site ATP (Lys) #status predicted\ !$1074 #binding_site ATP (Lys) #status predicted SUMMARY #length 1276 #molecular-weight 140993 #checksum 6711 SEQUENCE /// ENTRY DVMS1A #type fragment TITLE multidrug resistance protein 1a - mouse (fragment) ALTERNATE_NAMES P-glycoprotein 1a ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 19-Jan-2001 ACCESSIONS A34175 REFERENCE A34175 !$#authors Hsu, S.I.H.; Lothstein, L.; Horwitz, S.B. !$#journal J. Biol. Chem. (1989) 264:12053-12062 !$#title Differential overexpression of three mdr gene family members !1in multidrug-resistant J774.2 mouse cells. Evidence that !1distinct P-glycoprotein precursors are encoded by unique mdr !1genes. !$#cross-references MUID:89308614; PMID:2473069 !$#accession A34175 !'##molecule_type mRNA !'##residues 1-1104 ##label HSU !'##cross-references GB:M24417; GB:J04839; NID:g200329; PIDN:AAA03243.1; !1PID:g200330 COMMENT This is an integral membrane protein overproduced in !1multidrug-resistant cells. It decreases drug accumulation by !1acting as an energy-dependent efflux pump that has broad !1specificity for structurally and functionally unrelated !1lipophilic antitumor drugs. CLASSIFICATION #superfamily multidrug resistance protein; ATP-binding !1cassette homology KEYWORDS ATP; duplication; glycoprotein; nucleotide binding; P-loop; !1transmembrane protein FEATURE !$234-428 #domain ATP-binding cassette homology #label ABC1\ !$251-258 #region nucleotide-binding motif A (P-loop)\ !$375-379 #region nucleotide-binding motif B\ !$877-1073 #domain ATP-binding cassette homology #label ABC2\ !$894-901 #region nucleotide-binding motif A (P-loop)\ !$1020-1024 #region nucleotide-binding motif B\ !$257 #binding_site ATP (Lys) #status predicted\ !$900 #binding_site ATP (Lys) #status predicted SUMMARY #length 1104 #checksum 7525 SEQUENCE /// ENTRY DVMS2 #type complete TITLE multidrug resistance protein 2 - mouse ALTERNATE_NAMES P-glycoprotein MDR2 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 19-Jan-2001 ACCESSIONS A30409; S70711 REFERENCE A30409 !$#authors Gros, P.; Raymond, M.; Bell, J.; Housman, D. !$#journal Mol. Cell. Biol. (1988) 8:2770-2778 !$#title Cloning and characterization of a second member of the mouse !1mdr gene family. !$#cross-references MUID:88302195; PMID:3405218 !$#accession A30409 !'##molecule_type mRNA !'##residues 1-1276 ##label HSU !'##cross-references GB:J03398; NID:g199109; PIDN:AAA39516.1; !1PID:g387428 REFERENCE S70711 !$#authors Kirschner, L.S. !$#journal Nucleic Acids Res. (1996) 24:2829-2834 !$#title De novo generation of simple sequence during gene !1amplification. !$#cross-references MUID:96313253; PMID:8759018 !$#accession S70711 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 43-92 ##label KIR !'##cross-references EMBL:U46839; NID:g1228142; PIDN:AAC52722.1; !1PID:g1228143 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1996 COMMENT This is an integral membrane protein overproduced in !1multidrug-resistant cells. It decreases drug accumulation by !1acting as an energy-dependent efflux pump that has broad !1specificity for structurally and functionally unrelated !1lipophilic antitumor drugs. GENETICS !$#gene mdr2 CLASSIFICATION #superfamily multidrug resistance protein; ATP-binding !1cassette homology KEYWORDS ATP; duplication; glycoprotein; nucleotide binding; P-loop; !1transmembrane protein FEATURE !$1-637,653-1276 #region duplication\ !$409-603 #domain ATP-binding cassette homology #label ABC1\ !$426-433 #region nucleotide-binding motif A (P-loop)\ !$550-554 #region nucleotide-binding motif B\ !$1049-1245 #domain ATP-binding cassette homology #label ABC2\ !$1067-1074 #region nucleotide-binding motif A (P-loop)\ !$1192-1196 #region nucleotide-binding motif B\ !$88,94 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$432 #binding_site ATP (Lys) #status predicted\ !$1072 #binding_site ATP (Lys) #status predicted SUMMARY #length 1276 #molecular-weight 140332 #checksum 2095 SEQUENCE /// ENTRY DVHY1C #type complete TITLE multidrug resistance protein 1 - Chinese hamster ALTERNATE_NAMES P-glycoprotein pgp1 ORGANISM #formal_name Cricetulus griseus #common_name Chinese hamster DATE 31-Dec-1990 #sequence_revision 30-Sep-1992 #text_change 19-Jan-2001 ACCESSIONS A38696; C38696; B38696; A27126; S33768; I52823 REFERENCE A38696 !$#authors Devine, S.E.; Hussain, A.; Davide, J.P.; Melera, P.W. !$#journal J. Biol. Chem. (1991) 266:4545-4555 !$#title Full length and alternatively spliced pgp-1 transcripts in !1multidrug-resistant Chinese hamster lung cells. !$#cross-references MUID:91154265; PMID:1671863 !$#accession A38696 !'##molecule_type mRNA !'##residues 1-1276 ##label DEV !'##cross-references GB:M59253; NID:g191154; PIDN:AAA37004.1; !1PID:g191155 !$#accession C38696 !'##molecule_type mRNA !'##residues 108-1276 ##label DE1 !'##cross-references GB:M59254; NID:g191156; PIDN:AAA37005.1; !1PID:g191157 !'##experimental_source clone ADX185 !$#accession B38696 !'##molecule_type mRNA !'##residues 1-32,771-1276 ##label DE2 !'##cross-references GB:M59252; NID:g191152; PIDN:AAA37003.1; !1PID:g191153 !'##experimental_source clone ADX124 REFERENCE A27126 !$#authors Endicott, J.A.; Juranka, P.F.; Sarangi, F.; Gerlach, J.H.; !1Deuchars, K.L.; Ling, V. !$#journal Mol. Cell. Biol. (1987) 7:4075-4081 !$#title Simultaneous expression of two P-glycoprotein genes in !1drug-sensitive Chinese hamster ovary cells. !$#cross-references MUID:88122132; PMID:2893255 !$#accession A27126 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 706-1276 ##label END !'##cross-references GB:M17897; NID:g191158; PIDN:AAA37006.1; !1PID:g191159 REFERENCE S33768 !$#authors Zastawny, R.L.; Ling, V. !$#journal Biochim. Biophys. Acta (1993) 1173:303-313 !$#title Structural and functional analysis of 5' flanking and intron !11 sequences of the hamster P-glycoprotein pgp1 and pgp2 !1genes. !$#cross-references MUID:93305724; PMID:8100449 !$#accession S33768 !'##status translation not shown !'##molecule_type DNA !'##residues 1-21 ##label ZAS !'##cross-references EMBL:L03286 REFERENCE I52823 !$#authors Teeter, L.D.; Eckersberg, T.; Tsai, Y.; Kuo, M.T. !$#journal Cell Growth Differ. (1991) 2:429-437 !$#title Analysis of the Chinese hamster P-glycoprotein/multidrug !1resistance gene pgp1 reveals that the AP-1 site is essential !1for full promoter activity. !$#cross-references MUID:92088970; PMID:1661134 !$#accession I52823 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-21 ##label RES !'##cross-references GB:S81975; NID:g240862 COMMENT This is an integral membrane protein overproduced in !1multidrug-resistant cells. It decreases drug accumulation by !1acting as an energy-dependent efflux pump that has broad !1specificity for structurally and functionally unrelated !1lipophilic antitumor drugs. GENETICS !$#gene pgp1 CLASSIFICATION #superfamily multidrug resistance protein; ATP-binding !1cassette homology KEYWORDS alternative splicing; ATP; duplication; glycoprotein; !1nucleotide binding; P-loop; transmembrane protein FEATURE !$407-601 #domain ATP-binding cassette homology #label ABC1\ !$424-431 #region nucleotide-binding motif A (P-loop)\ !$548-552 #region nucleotide-binding motif B\ !$1050-1246 #domain ATP-binding cassette homology #label ABC2\ !$1067-1074 #region nucleotide-binding motif A (P-loop)\ !$1193-1197 #region nucleotide-binding motif B\ !$87,91,96 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$430 #binding_site ATP (Lys) #status predicted\ !$1073 #binding_site ATP (Lys) #status predicted SUMMARY #length 1276 #molecular-weight 140964 #checksum 6954 SEQUENCE /// ENTRY DVHY2C #type fragment TITLE multidrug resistance protein 2 - Chinese hamster (fragment) ALTERNATE_NAMES P-glycoprotein pgp2 ORGANISM #formal_name Cricetulus griseus #common_name Chinese hamster DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 19-Jan-2001 ACCESSIONS B27126 REFERENCE A27126 !$#authors Endicott, J.A.; Juranka, P.F.; Sarangi, F.; Gerlach, J.H.; !1Deuchars, K.L.; Ling, V. !$#journal Mol. Cell. Biol. (1987) 7:4075-4081 !$#title Simultaneous expression of two P-glycoprotein genes in !1drug-sensitive Chinese hamster ovary cells. !$#cross-references MUID:88122132; PMID:2893255 !$#accession B27126 !'##molecule_type mRNA !'##residues 1-655 ##label END !'##cross-references GB:M17896; NID:g191161; PIDN:AAA37007.1; !1PID:g387054 COMMENT This is an integral membrane protein overproduced in !1multidrug-resistant cells. It decreases drug accumulation by !1acting as an energy-dependent efflux pump that has broad !1specificity for structurally and functionally unrelated !1lipophilic antitumor drugs. GENETICS !$#gene pgp2 CLASSIFICATION #superfamily multidrug resistance protein; ATP-binding !1cassette homology KEYWORDS ATP; duplication; glycoprotein; nucleotide binding; P-loop; !1transmembrane protein FEATURE !$430-626 #domain ATP-binding cassette homology #label ABC2\ !$447-454 #region nucleotide-binding motif A (P-loop)\ !$573-577 #region nucleotide-binding motif B\ !$453 #binding_site ATP (Lys) #status predicted SUMMARY #length 655 #checksum 4409 SEQUENCE /// ENTRY DVZQF #type complete TITLE multidrug resistance protein - malaria parasite (Plasmodium falciparum) ALTERNATE_NAMES P-glycoprotein ORGANISM #formal_name Plasmodium falciparum DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 19-Jan-2001 ACCESSIONS S18204; A32547 REFERENCE S18204 !$#authors Triglia, T.; Foote, S.J.; Kemp, D.J.; Cowman, A.F. !$#journal Mol. Cell. Biol. (1991) 11:5244-5250 !$#title Amplification of the multidrug resistance gene pfmdr1 in !1Plasmodium falciparum has arisen as multiple independent !1events. !$#cross-references MUID:92017800; PMID:1922044 !$#accession S18204 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-1419 ##label TRI !'##cross-references EMBL:X56851; NID:g9935; PIDN:CAA40180.1; PID:g9936 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1990 REFERENCE A32547 !$#authors Foote, S.J.; Thompson, J.K.; Cowman, A.F.; Kemp, D.J. !$#journal Cell (1989) 57:921-930 !$#title Amplification of the multidrug resistance gene in some !1chloroquine-resistant isolates of P. falciparum. !$#cross-references MUID:89288297; PMID:2701941 !$#accession A32547 !'##molecule_type mRNA !'##residues 1-1419 ##label FOO !'##cross-references GB:M29154; GB:M24322; NID:g160398; PIDN:AAA29646.1; !1PID:g160399 CLASSIFICATION #superfamily multidrug resistance protein; ATP-binding !1cassette homology KEYWORDS ATP; duplication; glycoprotein; nucleotide binding; P-loop; !1transmembrane protein FEATURE !$1-632,655-1276 #region duplication\ !$396-638 #domain ATP-binding cassette homology #label ABC1\ !$413-420 #region nucleotide-binding motif A (P-loop)\ !$583-587 #region nucleotide-binding motif B\ !$1144-1387 #domain ATP-binding cassette homology #label ABC2\ !$1161-1168 #region nucleotide-binding motif A (P-loop)\ !$1332-1336 #region nucleotide-binding motif B SUMMARY #length 1419 #molecular-weight 162251 #checksum 2697 SEQUENCE /// ENTRY DVBYS6 #type complete TITLE mating pheromone a secretion protein STE6 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES mating factor a secretion protein STE6; mating hormone a secretion protein STE6; multidrug resistance protein homolog STE6; P-glycoprotein homolog STE6; protein YKL209c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 19-Jan-2001 ACCESSIONS S05789; S14174; S38047; S05872 REFERENCE S05789 !$#authors McGrath, J.P.; Varshavsky, A. !$#journal Nature (1989) 340:400-404 !$#title The yeast STE6 gene encodes a homologue of the mammalian !1multidrug resistance P-glycoprotein. !$#cross-references MUID:89330565; PMID:2569166 !$#accession S05789 !'##molecule_type DNA !'##residues 1-1290 ##label MCG !'##cross-references EMBL:X15428; NID:g4563; PIDN:CAA33467.1; PID:g4564 !'##experimental_source strain S288C REFERENCE S14174 !$#authors Kuchler, K.; Sterne, R.E.; Thorner, J. !$#journal EMBO J. (1989) 8:3973-3984 !$#title Saccharomyces cerevisiae STE6 gene product: a novel pathway !1for protein export in eukaryotic cells. !$#cross-references MUID:90076117; PMID:2686977 !$#accession S14174 !'##molecule_type DNA !'##residues 1-1290 ##label KUC !'##cross-references EMBL:M26376; NID:g172757; PIDN:AAA35116.1; !1PID:g172758 REFERENCE S37897 !$#authors Pohl, T.M.; Pohl, F.M. !$#submission submitted to the Protein Sequence Database, March 1994 !$#accession S38047 !'##molecule_type DNA !'##residues 1-1290 ##label POH !'##cross-references EMBL:Z28209; NID:g486372; PIDN:CAA82054.1; !1PID:g486373; GSPDB:GN00011; MIPS:YKL209c REFERENCE S05872 !$#authors Wilson, K.L.; Herskowitz, I. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:2536-2540 !$#title Sequences upstream of the STE6 gene required for its !1expression and regulation by the mating type locus in !1Saccharomyces cerevisiae. !$#cross-references MUID:86205986; PMID:3517872 !$#accession S05872 !'##molecule_type DNA !'##residues 1-41 ##label WIL !'##cross-references EMBL:M12842; NID:g172759; PIDN:AAA35117.1; !1PID:g553144 GENETICS !$#gene SGD:STE6; MIPS:YKL209c !'##cross-references SGD:S0001692; MIPS:YKL209c !$#map_position 11L FUNCTION !$#description responsible for export of mating pheromone a CLASSIFICATION #superfamily multidrug resistance protein; ATP-binding !1cassette homology KEYWORDS ATP; duplication; glycoprotein; nucleotide binding; P-loop; !1transmembrane protein FEATURE !$26-48 #domain transmembrane #status predicted #label TM01\ !$49-75 #domain extracellular #status predicted #label EXT\ !$76-97 #domain transmembrane #status predicted #label TM02\ !$151-170 #domain transmembrane #status predicted #label TM03\ !$176-194 #domain transmembrane #status predicted #label TM04\ !$242-264 #domain transmembrane #status predicted #label TM05\ !$293-317 #domain transmembrane #status predicted #label TM06\ !$318-715 #domain intracellular #status predicted #label INT1\ !$375-579 #domain ATP-binding cassette homology #label ABC1\ !$392-399 #region nucleotide-binding motif A (P-loop)\ !$526-530 #region nucleotide-binding motif B\ !$716-742 #domain transmembrane #status predicted #label TM07\ !$762-779 #domain transmembrane #status predicted #label TM08\ !$839-859 #domain transmembrane #status predicted #label TM09\ !$864-886 #domain transmembrane #status predicted #label TM10\ !$947-963 #domain transmembrane #status predicted #label TM11\ !$981-999 #domain transmembrane #status predicted #label TM12\ !$1000-1290 #domain intracellular #status predicted #label INT2\ !$1070-1263 #domain ATP-binding cassette homology #label ABC2\ !$1087-1094 #region nucleotide-binding motif A (P-loop)\ !$1210-1214 #region nucleotide-binding motif B\ !$398 #binding_site ATP (Lys) #status predicted\ !$1093 #binding_site ATP (Lys) #status predicted SUMMARY #length 1290 #molecular-weight 144764 #checksum 6516 SEQUENCE /// ENTRY T00558 #type complete TITLE probable ABC transporter [imported] - Arabidopsis thaliana ALTERNATE_NAMES protein F12L6.14; probable P-glycoprotein pgp1 ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 02-Mar-2001 ACCESSIONS T00558; H84817 REFERENCE Z14168 !$#authors Rounsley, S.D.; Lin, X.; Ketchum, K.A.; Crosby, M.L.; !1Brandon, R.C.; Sykes, S.M.; Kaul, S.; Mason, T.M.; !1Kerlavage, A.R.; Adams, M.D.; Somerville, C.R.; Venter, J.C. !$#submission submitted to the EMBL Data Library, July 1998 !$#description Arabidopsis thaliana chromosome II BAC F12L6 genomic !1sequence. !$#accession T00558 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-1407 ##label ROU !'##cross-references EMBL:AC004218; NID:g3355463; PIDN:AAC27839.1; !1PID:g3355477 !'##experimental_source cultivar Columbia REFERENCE A84420 !$#authors Lin, X.; Kaul, S.; Rounsley, S.D.; Shea, T.P.; Benito, M.I.; !1Town, C.D.; Fujii, C.Y.; Mason, T.M.; Bowman, C.L.; !1Barnstead, M.E.; Feldblyum, T.V.; Buell, C.R.; Ketchum, !1K.A.; Lee, J.J.; Ronning, C.M.; Koo, H.; Moffat, K.S.; !1Cronin, L.A.; Shen, M.; VanAken, S.E.; Umayam, L.; Tallon, !1L.J.; Gill, J.E.; Adams, M.D.; Carrera, A.J.; Creasy, T.H.; !1Goodman, H.M.; Somerville, C.R.; Copenhaver, G.P.; Preuss, !1D.; Nierman, W.C.; White, O.; Eisen, J.A.; Salzberg, S.L.; !1Fraser, C.M.; Venter, J.C. !$#journal Nature (1999) 402:761-768 !$#title Sequence and analysis of chromosome 2 of the plant !1Arabidopsis thaliana. !$#cross-references MUID:20083487; PMID:10617197 !$#accession H84817 !'##status preliminary !'##molecule_type DNA !'##residues 1-1407 ##label STO !'##cross-references GB:AE002093; NID:g3355477; PIDN:AAC27839.1; !1GSPDB:GN00139 GENETICS !$#gene pgp1; F12L6.14; At2g39480 !$#map_position 2 !$#introns 134/3; 153/1; 211/3; 278/3; 365/2; 469/1; 542/3; 656/2; 918/ !11; 998/3 CLASSIFICATION #superfamily Arabidopsis thaliana probable multidrug !1resistance protein pgp1; ATP-binding cassette homology KEYWORDS ATP FEATURE !$430-623 #domain ATP-binding cassette homology #label ABC1\ !$1176-1371 #domain ATP-binding cassette homology #label ABC2 SUMMARY #length 1407 #molecular-weight 155874 #checksum 1697 SEQUENCE /// ENTRY DVLNS #type complete TITLE multidrug resistance protein - Leishmania tarentolae ALTERNATE_NAMES P-glycoprotein ORGANISM #formal_name Leishmania tarentolae DATE 31-Dec-1990 #sequence_revision 26-Feb-1998 #text_change 19-Jan-2001 ACCESSIONS S09248; S12457; A34207 REFERENCE A34207 !$#authors Ouellette, M.; Fase-Fowler, F.; Borst, P. !$#journal EMBO J. (1990) 9:1027-1033 !$#title The amplified H circle of methotrexate-resistant Leishmania !1tarentolae contains a novel P-glycoprotein gene. !$#cross-references MUID:90214609; PMID:1969794 !$#accession S09248 !'##molecule_type DNA !'##residues 1-1548 ##label OUE !'##cross-references EMBL:X17154 !'##note the source is designated as Leishmania tarentolae REFERENCE S12457 !$#authors Ouellette, M. !$#submission submitted to the EMBL Data Library, November 1989 !$#accession S12457 !'##status preliminary !'##molecule_type DNA !'##residues 1-1357,'DV',1360-1548 ##label OU2 !'##cross-references EMBL:X17154; NID:g9658; PIDN:CAA35038.1; PID:g9659 !'##note the source is designated as Leishmania tarentolae GENETICS !$#gene itpgpA CLASSIFICATION #superfamily human multidrug resistance protein cMOAT2; !1ATP-binding cassette homology KEYWORDS antibiotic resistance; ATP; duplication; glycoprotein; !1nucleotide binding; P-loop; transmembrane protein FEATURE !$650-831 #domain ATP-binding cassette homology #label ABC1\ !$667-674 #region nucleotide-binding motif A (P-loop)\ !$777-781 #region nucleotide-binding motif B\ !$1303-1497 #domain ATP-binding cassette homology #label ABC2\ !$1320-1327 #region nucleotide-binding motif A (P-loop)\ !$1444-1448 #region nucleotide-binding motif B SUMMARY #length 1548 #molecular-weight 172262 #checksum 1864 SEQUENCE /// ENTRY DVHUAR #type complete TITLE multidrug resistance protein (cell line H69AR) - human ALTERNATE_NAMES multidrug resistance-associated protein (MRP) ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1993 #sequence_revision 05-Dec-1998 #text_change 19-Jan-2001 ACCESSIONS A44231; A37495 REFERENCE A44231 !$#authors Cole, S.P.C.; Bhardwaj, G.; Gerlach, J.H.; Mackie, J.E.; !1Grant, C.E.; Almquist, K.C.; Stewart, A.J.; Kurz, E.U.; !1Duncan, A.M.V.; Deeley, R.G. !$#journal Science (1992) 258:1650-1654 !$#title Overexpression of a transporter gene in a !1multidrug-resistant human lung cancer cell line. !$#cross-references MUID:93088080; PMID:1360704 !$#accession A44231 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 'MAPTRSGTGMSRGIPATPTSPSAFRTRSSCGCLVFTSGPV',50-1531 ##label !1CO1 !'##cross-references GB:L05628; NID:g1835658 !'##experimental_source small cell lung carcinoma cell line H69AR !'##note sequence extracted from NCBI backbone (NCBIP:119851); this !1sequence has been corrected in reference A37495 REFERENCE A37495 !$#authors Cole, S.P.C.; Deeley, R.G. !$#journal Science (1993) 260:879 !$#title Multidrug resistance-associated protein: sequence !1correction. !$#cross-references MUID:93262415; PMID:8098549 !$#accession A37495 !'##status not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-60 ##label CO2 !'##cross-references GB:L05628; NID:g1835658 !'##note sequence extracted from NCBI backbone (NCBIP:131929) GENETICS !$#gene GDB:MRP !'##cross-references GDB:136335; OMIM:158343 !$#map_position 16p13.1-16p13.1 CLASSIFICATION #superfamily human multidrug resistance protein cMOAT2; !1ATP-binding cassette homology KEYWORDS antibiotic resistance; ATP; duplication; nucleotide binding; !1P-loop; transmembrane protein; transport protein FEATURE !$661-844 #domain ATP-binding cassette homology #label ABC1\ !$678-685 #region nucleotide-binding motif A (P-loop)\ !$788-792 #region nucleotide-binding motif B\ !$1310-1503 #domain ATP-binding cassette homology #label ABC2\ !$1327-1334 #region nucleotide-binding motif A (P-loop)\ !$1450-1454 #region nucleotide-binding motif B SUMMARY #length 1531 #molecular-weight 171671 #checksum 2048 SEQUENCE /// ENTRY S71839 #type complete TITLE canalicular multidrug resistance protein - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S71839 REFERENCE S71839 !$#authors Buechler, M.; Koenig, J.; Brom, M.; Kartenbeck, J.; Spring, !1H.; Horie, T.; Keppler, D. !$#journal J. Biol. Chem. (1996) 271:15091-15098 !$#title cDNA cloning of the hepatocyte canalicular isoform of the !1multidrug resistance protein, cMrp, reveals a novel !1conjugate export pump deficient in hyperbilirubinemic mutant !1rats. !$#cross-references MUID:96279006; PMID:8662992 !$#accession S71839 !'##status preliminary; nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-1541 ##label BUE !'##cross-references EMBL:X96393; NID:g1292881; PIDN:CAA65257.1; !1PID:g1617207 CLASSIFICATION #superfamily human multidrug resistance protein cMOAT2; !1ATP-binding cassette homology KEYWORDS ATP; glycoprotein; nucleotide binding; P-loop; transmembrane !1protein FEATURE !$100-124 #domain transmembrane #status predicted #label TM01\ !$127-151 #domain transmembrane #status predicted #label TM02\ !$160-187 #domain transmembrane #status predicted #label TM03\ !$305-329 #domain transmembrane #status predicted #label TM04\ !$354-381 #domain transmembrane #status predicted #label TM05\ !$431-451 #domain transmembrane #status predicted #label TM06\ !$456-476 #domain transmembrane #status predicted #label TM07\ !$536-564 #domain transmembrane #status predicted #label TM08\ !$574-602 #domain transmembrane #status predicted #label TM09\ !$650-833 #domain ATP-binding cassette homology #label ABC1\ !$667-674 #region nucleotide-binding motif A (P-loop)\ !$966-994 #domain transmembrane #status predicted #label TM10\ !$1018-1046 #domain transmembrane #status predicted #label TM11\ !$1104-1132 #domain transmembrane #status predicted #label TM12\ !$1203-1228 #domain transmembrane #status predicted #label TM13\ !$1313-1506 #domain ATP-binding cassette homology #label ABC2\ !$1330-1337 #region nucleotide-binding motif A (P-loop)\ !$6,1007,1010,1011 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1541 #molecular-weight 173382 #checksum 1315 SEQUENCE /// ENTRY S71841 #type complete TITLE multidrug resistance protein, canalicular - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S71841; S71840 REFERENCE S71841 !$#authors Koenig, J.; Keppler, D. !$#submission submitted to the EMBL Data Library, August 1996 !$#accession S71841 !'##molecule_type mRNA !'##residues 1-1545 ##label KOE !'##cross-references EMBL:X96395; NID:g1507819; PIDN:CAA65259.1; !1PID:g1514568 REFERENCE S71839 !$#authors Buechler, M.; Koenig, J.; Brom, M.; Kartenbeck, J.; Spring, !1H.; Horie, T.; Keppler, D. !$#journal J. Biol. Chem. (1996) 271:15091-15098 !$#title cDNA cloning of the hepatocyte canalicular isoform of the !1multidrug resistance protein, cMrp, reveals a novel !1conjugate export pump deficient in hyperbilirubinemic mutant !1rats. !$#cross-references MUID:96279006; PMID:8662992 !$#accession S71840 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1415-1429,'VP',1432-1455,'E',1457-1545 ##label BUE !'##cross-references EMBL:X96395 GENETICS !$#gene GDB:ABCC2; CMOAT; ABC; MRP2; cMRP; DJS !'##cross-references GDB:6089489; OMIM:601107 !$#map_position 10q24-10q24 CLASSIFICATION #superfamily human multidrug resistance protein cMOAT2; !1ATP-binding cassette homology KEYWORDS ATP; glycoprotein; nucleotide binding; P-loop; transmembrane !1protein FEATURE !$654-837 #domain ATP-binding cassette homology #label ABC1\ !$671-678 #region nucleotide-binding motif A (P-loop)\ !$1317-1510 #domain ATP-binding cassette homology #label ABC2\ !$1334-1341 #region nucleotide-binding motif A (P-loop) SUMMARY #length 1545 #molecular-weight 174090 #checksum 5562 SEQUENCE /// ENTRY S64757 #type complete TITLE probable membrane protein YLL015w - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein A255; hypothetical protein L1313 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S64757; S64763; PS0041; S69391; S70560 REFERENCE S64743 !$#authors Miosga, T.; Zimmermann, F.K. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64757 !'##molecule_type DNA !'##residues 1-1559 ##label MIO !'##cross-references EMBL:Z73120; NID:g1360184; PIDN:CAA97460.1; !1PID:g1360185; GSPDB:GN00012; MIPS:YLL015w !'##experimental_source strain S288C REFERENCE S64761 !$#authors Goffeau, A.; Purnelle, B. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64763 !'##molecule_type DNA !'##residues 1-1559 ##label GOF !'##cross-references EMBL:Z73120; NID:g1360184; PIDN:CAA97460.1; !1PID:g1360185; GSPDB:GN00012; MIPS:YLL015w !'##experimental_source strain S288C REFERENCE PS0041 !$#authors Boy-Marcotte, E.; Damak, F.; Camonis, J.; Garreau, H.; !1Jacquet, M. !$#journal Gene (1989) 77:21-30 !$#title The C-terminal part of a gene partially homologous to CDC25 !1gene suppresses the cdc25-5 mutation in Saccharomyces !1cerevisiae. !$#cross-references MUID:89306677; PMID:2545538 !$#accession PS0041 !'##molecule_type DNA !'##residues 1-255 ##label BOY !'##note the authors translated the codon CAG for residue 248 as His REFERENCE S69380 !$#authors Purnelle, B.; Goffeau, A. !$#submission submitted to the EMBL Data Library, April 1996 !$#description The sequence of 32 kb on the left arm of yeast chromosome !1XII reveals 14 open reading frames among which HSP104, SSA2, !1SPA2, KNS1, DPS1/APS, SDC25, a new member of the !1seripauperins family and a new ABC transporter homologous to !1the human multidrug resistance protein. !$#accession S69391 !'##molecule_type DNA !'##residues 1-1559 ##label PUR !'##cross-references EMBL:X97560; NID:g1297003; PIDN:CAA66162.1; !1PID:g1297015 REFERENCE S70557 !$#authors Miosga, T.; Zimmermann, F.K. !$#journal Yeast (1996) 12:693-708 !$#title Sequence analysis of the CEN12 region of Saccharomyces !1cerevisiae on a 43.7 kb fragment of chromosome XII including !1an open reading frame homologous to the human cystic !1fibrosis transmembrane conductance regulator protein CFTR. !$#cross-references MUID:96405918; PMID:8810043 !$#accession S70560 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1559 ##label MIW !'##cross-references EMBL:X91488; NID:g1495203; PIDN:CAA62776.1; !1PID:g1495208 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1September 1995 GENETICS !$#gene SGD:BPT1; MIPS:YLL015w !'##cross-references SGD:S0003938 !$#map_position 12L CLASSIFICATION #superfamily human multidrug resistance protein cMOAT2; !1ATP-binding cassette homology KEYWORDS ATP; nucleotide binding; P-loop; transmembrane protein FEATURE !$28-44 #domain transmembrane #status predicted #label TM1\ !$143-159 #domain transmembrane #status predicted #label TM2\ !$178-194 #domain transmembrane #status predicted #label TM3\ !$334-350 #domain transmembrane #status predicted #label TM4\ !$421-437 #domain transmembrane #status predicted #label TM5\ !$526-542 #domain transmembrane #status predicted #label TM6\ !$550-566 #domain transmembrane #status predicted #label TM7\ !$654-847 #domain ATP-binding cassette homology #label ABC1\ !$672-679 #region nucleotide-binding motif A (P-loop)\ !$974-990 #domain transmembrane #status predicted #label TM8\ !$1017-1033 #domain transmembrane #status predicted #label TM9\ !$1099-1115 #domain transmembrane #status predicted #label TM10\ !$1118-1134 #domain transmembrane #status predicted #label TM11\ !$1212-1228 #domain transmembrane #status predicted #label TM12\ !$1319-1529 #domain ATP-binding cassette homology #label ABC2\ !$1336-1343 #region nucleotide-binding motif A (P-loop) SUMMARY #length 1559 #molecular-weight 176872 #checksum 4310 SEQUENCE /// ENTRY S51863 #type complete TITLE cadmium resistance protein YCF1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YD9302.11c; protein YDR135c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S51863; A55352; S50233 REFERENCE S51853 !$#authors Oliver, K.; Harris, D. !$#submission submitted to the EMBL Data Library, February 1995 !$#accession S51863 !'##molecule_type DNA !'##residues 1-1515 ##label OLI !'##cross-references EMBL:Z48179; NID:g665657; PIDN:CAA88217.1; !1PID:g665668; GSPDB:GN00004; MIPS:YDR135c REFERENCE A55352 !$#authors Szczypka, M.S.; Wemmie, J.A.; Moye-Rowley, W.S.; Thiele, !1D.J. !$#journal J. Biol. Chem. (1994) 269:22853-22857 !$#title A yeast metal resistance protein similar to human cystic !1fibrosis transmembrane conductance regulator (CFTR) and !1multidrug resistance-associated protein. !$#cross-references MUID:94357936; PMID:7521334 !$#accession A55352 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-679,'R',681-1515 ##label SZC !'##cross-references GB:L35237; NID:g556464; PIDN:AAA50353.1; !1PID:g556465 GENETICS !$#gene SGD:YCF1; MIPS:YDR135c !'##cross-references SGD:S0002542; MIPS:YDR135c !$#map_position 4R FUNCTION !$#description required for cadmium resistance CLASSIFICATION #superfamily human multidrug resistance protein cMOAT2; !1ATP-binding cassette homology KEYWORDS ATP; nucleotide binding; P-loop; transmembrane protein; !1yeast vacuole FEATURE !$287-308 #domain transmembrane #status predicted #label TM1\ !$345-366 #domain transmembrane #status predicted #label TM2\ !$421-442 #domain transmembrane #status predicted #label TM3\ !$446-467 #domain transmembrane #status predicted #label TM4\ !$534-555 #domain transmembrane #status predicted #label TM5\ !$558-580 #domain transmembrane #status predicted #label TM6\ !$646-829 #domain ATP-binding cassette homology #label ABC1\ !$663-670 #region nucleotide-binding motif A (P-loop)\ !$951-972 #domain transmembrane #status predicted #label TM7\ !$995-1016 #domain transmembrane #status predicted #label TM8\ !$1068-1088 #domain transmembrane #status predicted #label TM9\ !$1092-1113 #domain transmembrane #status predicted #label TM10\ !$1179-1200 #domain transmembrane #status predicted #label TM11\ !$1208-1229 #domain transmembrane #status predicted #label TM12\ !$1289-1483 #domain ATP-binding cassette homology #label ABC2\ !$1306-1313 #region nucleotide-binding motif A (P-loop) SUMMARY #length 1515 #molecular-weight 171120 #checksum 6651 SEQUENCE /// ENTRY JC5667 #type complete TITLE multidrug resistance protein, short type - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS JC5667 REFERENCE JC5667 !$#authors Suzuki, T.; Nishio, K.; Sasaki, H.; Kurokawa, H.; !1Saito-Ohara, F.; Ikeuchi, T.; Tanabe, S.; Terada, M.; Saijo, !1N. !$#journal Biochem. Biophys. Res. Commun. (1997) 238:790-794 !$#title cDNA cloning of a short type of multidrug resistance protein !1homologue, SMRP, from a human lung cancer cell line. !$#cross-references MUID:97472289; PMID:9325169 !$#accession JC5667 !'##molecule_type mRNA !'##residues 1-946 ##label SUZ !'##cross-references DDBJ:AB005659; NID:g2554609; PIDN:BAA22887.1; !1PID:g2554610 GENETICS !$#gene GDB:ABCC5; MRP5; sMRP; ABC33; MOAT-C !'##cross-references GDB:9954943 !$#map_position 3q25-3q27 CLASSIFICATION #superfamily human multidrug resistance protein, short type; !1ATP-binding cassette homology KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$87-268 #domain ATP-binding cassette homology #label ABC1\ !$104-111 #region walker A motif\ !$104-111 #region nucleotide-binding motif A (P-loop)\ !$214-219 #region walker B motif\ !$719-912 #domain ATP-binding cassette homology #label ABC2\ !$736-743 #region nucleotide-binding motif A (P-loop)\ !$736-743 #region walker A motif\ !$859-863 #region walker B motif SUMMARY #length 946 #molecular-weight 105509 #checksum 2244 SEQUENCE /// ENTRY DVHUCF #type complete TITLE cystic fibrosis transmembrane conductance regulator - human ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1990 #sequence_revision 28-Oct-1994 #text_change 16-Jul-1999 ACCESSIONS A39069; A30300; A42805; S10943; I55354; S10951 REFERENCE A39069 !$#authors Zielenski, J.; Rozmahel, R.; Bozon, D.; Kerem, B.; !1Grzelczak, Z.; Riordan, J.R.; Rommens, J.; Tsui, L.C. !$#journal Genomics (1991) 10:214-228 !$#title Genomic DNA sequence of the cystic fibrosis transmembrane !1conductance regulator (CFTR) gene. !$#cross-references MUID:91257831; PMID:1710598 !$#accession A39069 !'##molecule_type DNA !'##residues 1-1480 ##label ZIE !'##cross-references GB:M55131; NID:g306536; PIDN:AAC13657.1; !1PID:g306538 REFERENCE A30300 !$#authors Riordan, J.R.; Rommens, J.M.; Kerem, B.; Alon, N.; Rozmahel, !1R.; Grzelczak, Z.; Zielenski, J.; Lok, S.; Plavsic, N.; !1Chou, J.L.; Drumm, M.L.; Iannuzzi, M.C.; Collins, F.S.; !1Tsui, L.C. !$#journal Science (1989) 245:1066-1073 !$#title Identification of the cystic fibrosis gene: cloning and !1characterization of complementary DNA. !$#cross-references MUID:89368940; PMID:2475911 !$#accession A30300 !'##molecule_type mRNA !'##residues 1-619,'N',621-832,'L',834-1149,'I',1151-1480 ##label RIO !'##cross-references GB:M28668; NID:g180331 !'##note this sequence has been revised in reference A39069 !'##note 75-Gln and 470-Val were also found REFERENCE A42805 !$#authors Picciotto, M.R.; Cohn, J.A.; Bertuzzi, G.; Greengard, P.; !1Nairn, A.C. !$#journal J. Biol. Chem. (1992) 267:12742-12752 !$#title Phosphorylation of the cystic fibrosis transmembrane !1conductance regulator. !$#cross-references MUID:92316961; PMID:1377674 !$#accession A42805 !'##molecule_type protein !'##residues 682-690,'E';693-725;727-743;747-815 ##label PIC REFERENCE S10943 !$#authors Cutting, G.R.; Kasch, L.M.; Rosenstein, B.J.; Zielenski, J.; !1Tsui, L.C.; Antonarakis, S.E.; Kazazian Jr., H.H. !$#journal Nature (1990) 346:366-369 !$#title A cluster of cystic fibrosis mutations in the first !1nucleotide-binding fold of the cystic fibrosis conductance !1regulator protein. !$#cross-references MUID:90326187; PMID:1695717 !$#accession S10943 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 542-560;1340-1358 ##label CUT !'##note Four mutations between residues 549-559 were identified in CF !1patients REFERENCE I55354 !$#authors Yoshimura, K.; Nakamura, H.; Trapnell, B.C.; Dalemans, W.; !1Pavirani, A.; Lecocq, J.P.; Crystal, R.G. !$#journal J. Biol. Chem. (1991) 266:9140-9144 !$#title The cystic fibrosis gene has a 'housekeeping'-type promoter !1and is expressed at low levels in cells of epithelial !1origin. !$#cross-references MUID:91225019; PMID:1709163 !$#accession I55354 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-17 ##label RES !'##cross-references GB:M58478; NID:g180291; PIDN:AAA51982.1; !1PID:g180292 !'##note neither the complete nucleic acid sequence nor the complete !1translation are shown COMMENT This protein (CFTR) is directly responsible for cystic !1fibrosis (CF), a disorder characterized by abnormally high !1electrical potential differences across the epithelial !1surfaces of the respiratory tract. A single residue deletion !1(Phe-508) is detected in most CF patients; however, the !1exact function of CFTR is not clear. It may be involved in !1anion transport and regulation of ion conductance across the !1apical membrane of epithelial cells. GENETICS !$#gene GDB:CFTR; CF !'##cross-references GDB:120584; OMIM:219700 !$#map_position 7q31.2-7q31.2 !$#introns 18/2; 55/2; 91/3; 163/3; 193/3; 248/2; 290/2; 372/3; 403/3; !1464/3; 528/3; 560/2; 589/2; 830/3; 873/3; 886/2; 970/1; 996/ !13; 1047/1; 1123/1; 1156/3; 1239/3; 1291/3; 1321/3; 1379/2; !11414/3 CLASSIFICATION #superfamily cystic fibrosis transmembrane conductance !1regulator; ATP-binding cassette homology KEYWORDS ATP; duplication; glycoprotein; nucleotide binding; P-loop; !1phosphoprotein; transmembrane protein FEATURE !$81-102 #domain transmembrane #status predicted #label TM1\ !$118-138 #domain transmembrane #status predicted #label TM2\ !$195-215 #domain transmembrane #status predicted #label TM3\ !$221-241 #domain transmembrane #status predicted #label TM4\ !$308-328 #domain transmembrane #status predicted #label TM5\ !$331-350 #domain transmembrane #status predicted #label TM6\ !$441-622 #domain ATP-binding cassette homology #label ABC1\ !$458-465 #region nucleotide-binding motif A (P-loop)\ !$568-572 #region nucleotide-binding motif B\ !$590-830 #region R domain\ !$860-880 #domain transmembrane #status predicted #label TM7\ !$912-932 #domain transmembrane #status predicted #label TM8\ !$991-1011 #domain transmembrane #status predicted #label TM9\ !$1103-1123 #domain transmembrane #status predicted #label TM10\ !$1129-1150 #domain transmembrane #status predicted #label TM11\ !$1227-1419 #domain ATP-binding cassette homology #label ABC2\ !$1244-1251 #region nucleotide-binding motif A (P-loop)\ !$1366-1370 #region nucleotide-binding motif B\ !$464 #binding_site ATP (Lys) #status predicted\ !$660,700,737,813 #binding_site phosphate (Ser) (covalent) (by cAMP- !8and cGMP-dependent kinases) #status experimental\ !$686,790 #binding_site phosphate (Ser) (covalent) (by protein !8kinase C) #status experimental\ !$768,795 #binding_site phosphate (Ser) (covalent) (by cAMP- !8and cGMP-dependent kinases) #status predicted\ !$894,900 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$1250 #binding_site ATP (Lys) #status predicted SUMMARY #length 1480 #molecular-weight 168172 #checksum 1238 SEQUENCE /// ENTRY A39323 #type complete TITLE cystic fibrosis transmembrane conductance regulator - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 19-Jun-1992 #sequence_revision 28-Oct-1994 #text_change 16-Jul-1999 ACCESSIONS A39323 REFERENCE A39323 !$#authors Diamond, G.; Scanlin, T.F.; Zasloff, M.A.; Bevins, C.L. !$#journal J. Biol. Chem. (1991) 266:22761-22769 !$#title A cross-species analysis of the cystic fibrosis !1transmembrane conductance regulator. Potential functional !1domains and regulatory sites. !$#cross-references MUID:92042228; PMID:1719001 !$#accession A39323 !'##molecule_type mRNA !'##residues 1-1481 ##label DIA !'##cross-references GB:M76128; NID:g163741; PIDN:AAA30772.1; !1PID:g163742 !'##note the authors translated the codon GGA for residue 725 as Phe and !1AGA for residue 1260 as Ala CLASSIFICATION #superfamily cystic fibrosis transmembrane conductance !1regulator; ATP-binding cassette homology KEYWORDS ATP; duplication; glycoprotein; nucleotide binding; P-loop; !1phosphoprotein; transmembrane protein FEATURE !$81-102 #domain transmembrane #status predicted #label TM1\ !$118-138 #domain transmembrane #status predicted #label TM2\ !$195-215 #domain transmembrane #status predicted #label TM3\ !$221-241 #domain transmembrane #status predicted #label TM4\ !$308-328 #domain transmembrane #status predicted #label TM5\ !$331-350 #domain transmembrane #status predicted #label TM6\ !$440-621 #domain ATP-binding cassette homology #label ABC1\ !$457-464 #region nucleotide-binding motif A (P-loop)\ !$567-571 #region nucleotide-binding motif B\ !$589-830 #region R domain\ !$860-880 #domain transmembrane #status predicted #label TM7\ !$912-932 #domain transmembrane #status predicted #label TM8\ !$991-1011 #domain transmembrane #status predicted #label TM9\ !$1103-1123 #domain transmembrane #status predicted #label TM10\ !$1129-1150 #domain transmembrane #status predicted #label TM11\ !$1228-1420 #domain ATP-binding cassette homology #label ABC2\ !$1245-1252 #region nucleotide-binding motif A (P-loop)\ !$1367-1371 #region nucleotide-binding motif B\ !$463 #binding_site ATP (Lys) #status predicted\ !$659,699,736,813 #binding_site phosphate (Ser) (covalent) (by cAMP- !8and cGMP-dependent kinases) #status experimental\ !$685,790 #binding_site phosphate (Ser) (covalent) (by protein !8kinase C) #status experimental\ !$767,795 #binding_site phosphate (Ser) (covalent) (by cAMP- !8and cGMP-dependent kinases) #status predicted\ !$894,900 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$1251 #binding_site ATP (Lys) #status predicted SUMMARY #length 1481 #molecular-weight 167758 #checksum 7909 SEQUENCE /// ENTRY A39901 #type complete TITLE cystic fibrosis transmembrane conductance regulator - mouse (strain C57/Bl/6J) ORGANISM #formal_name Mus musculus domesticus #common_name western European house mouse DATE 20-Mar-1992 #sequence_revision 28-Oct-1994 #text_change 16-Jul-1999 ACCESSIONS A39901; A42007 REFERENCE A39901 !$#authors Tata, F.; Stanier, P.; Wicking, C.; Halford, S.; Kruyer, H.; !1Lench, N.J.; Scambler, P.J.; Hansen, C.; Braman, J.C.; !1Williamson, R.; Wainwright, B.J. !$#journal Genomics (1991) 10:301-307 !$#title Cloning the mouse homolog of the human cystic fibrosis !1transmembrane conductance regulator gene. !$#cross-references MUID:91301683; PMID:1712752 !$#accession A39901 !'##molecule_type mRNA !'##residues 1-1476 ##label TAT !'##cross-references GB:M69298; NID:g192566; PIDN:AAA37417.1; !1PID:g192567 REFERENCE A42007 !$#authors Kelley, K.A.; Stamm, S.; Kozak, C.A. !$#journal Genomics (1992) 13:381-388 !$#title Expression and chromosome localization of the murine cystic !1fibrosis transmembrane conductance regulator. !$#cross-references MUID:92307673; PMID:1377165 !$#accession A42007 !'##molecule_type DNA !'##residues 465-528 ##label KEL !'##cross-references GB:M84614 GENETICS !$#gene CFTR !$#map_position 6 CLASSIFICATION #superfamily cystic fibrosis transmembrane conductance !1regulator; ATP-binding cassette homology KEYWORDS ATP; duplication; glycoprotein; nucleotide binding; P-loop; !1phosphoprotein; transmembrane protein FEATURE !$81-102 #domain transmembrane #status predicted #label TM1\ !$118-138 #domain transmembrane #status predicted #label TM2\ !$195-215 #domain transmembrane #status predicted #label TM3\ !$221-241 #domain transmembrane #status predicted #label TM4\ !$308-328 #domain transmembrane #status predicted #label TM5\ !$331-350 #domain transmembrane #status predicted #label TM6\ !$441-622 #domain ATP-binding cassette homology #label ABC1\ !$458-465 #region nucleotide-binding motif A (P-loop)\ !$568-572 #region nucleotide-binding motif B\ !$590-825 #region R domain\ !$855-875 #domain transmembrane #status predicted #label TM7\ !$907-927 #domain transmembrane #status predicted #label TM8\ !$986-1006 #domain transmembrane #status predicted #label TM9\ !$1098-1118 #domain transmembrane #status predicted #label TM10\ !$1124-1145 #domain transmembrane #status predicted #label TM11\ !$1223-1415 #domain ATP-binding cassette homology #label ABC2\ !$1240-1247 #region nucleotide-binding motif A (P-loop)\ !$1362-1366 #region nucleotide-binding motif B\ !$464 #binding_site ATP (Lys) #status predicted\ !$660,698,732,808 #binding_site phosphate (Ser) (covalent) (by cAMP- !8and cGMP-dependent kinases) #status experimental\ !$684,785 #binding_site phosphate (Ser) (covalent) (by protein !8kinase C) #status experimental\ !$763,790 #binding_site phosphate (Ser) (covalent) (by cAMP- !8and cGMP-dependent kinases) #status predicted\ !$889,895 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$1246 #binding_site ATP (Lys) #status predicted SUMMARY #length 1476 #molecular-weight 167852 #checksum 9487 SEQUENCE /// ENTRY A40303 #type complete TITLE cystic fibrosis transmembrane conductance regulator - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 03-Apr-1992 #sequence_revision 28-Oct-1994 #text_change 16-Jul-1999 ACCESSIONS A40303; I78528 REFERENCE A40303 !$#authors Yorifuji, T.; Lemna, W.K.; Ballard, C.F.; Rosenbloom, C.L.; !1Rozmahel, R.; Plavsic, N.; Tsui, L.C.; Beaudet, A.L. !$#journal Genomics (1991) 10:547-550 !$#title Molecular cloning and sequence analysis of the murine cDNA !1for the cystic fibrosis transmembrane conductance regulator. !$#cross-references MUID:91365359; PMID:1716243 !$#accession A40303 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-1476 ##label YOR !'##cross-references GB:M60493; NID:g192831; PIDN:AAA18903.1; !1PID:g192832 !'##experimental_source lung, strain BALB/cBy REFERENCE I58115 !$#authors Delaney, S.J.; Rich, D.P.; Thomson, S.A.; Hargrave, M.R.; !1Lovelock, P.K.; Welsh, M.J.; Wainwright, B.J. !$#journal Nature Genet. (1993) 4:426-431 !$#title Cystic fibrosis transmembrane conductance regulator splice !1variants are not conserved and fail to produce chloride !1channels. !$#cross-references MUID:94004974; PMID:7691356 !$#accession I78528 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 549-571 ##label RES !'##cross-references GB:S65942; NID:g430810; PIDN:AAB28391.1; !1PID:g430811 GENETICS !$#gene CFTR !$#map_position 6 !$#introns 560/2 !$#note the list of introns is incomplete CLASSIFICATION #superfamily cystic fibrosis transmembrane conductance !1regulator; ATP-binding cassette homology KEYWORDS ATP; duplication; glycoprotein; nucleotide binding; P-loop; !1phosphoprotein; transmembrane protein FEATURE !$81-102 #domain transmembrane #status predicted #label TM1\ !$118-138 #domain transmembrane #status predicted #label TM2\ !$195-215 #domain transmembrane #status predicted #label TM3\ !$221-241 #domain transmembrane #status predicted #label TM4\ !$308-328 #domain transmembrane #status predicted #label TM5\ !$331-350 #domain transmembrane #status predicted #label TM6\ !$441-622 #domain ATP-binding cassette homology #label ABC1\ !$458-465 #region nucleotide-binding motif A (P-loop)\ !$568-572 #region nucleotide-binding motif B\ !$590-825 #region R domain\ !$855-875 #domain transmembrane #status predicted #label TM7\ !$907-927 #domain transmembrane #status predicted #label TM8\ !$986-1006 #domain transmembrane #status predicted #label TM9\ !$1098-1118 #domain transmembrane #status predicted #label TM10\ !$1124-1145 #domain transmembrane #status predicted #label TM11\ !$1223-1415 #domain ATP-binding cassette homology #label ABC2\ !$1240-1247 #region nucleotide-binding motif A (P-loop)\ !$1362-1366 #region nucleotide-binding motif B\ !$464 #binding_site ATP (Lys) #status predicted\ !$660,698,732,808 #binding_site phosphate (Ser) (covalent) (by cAMP- !8and cGMP-dependent kinases) #status experimental\ !$684,785 #binding_site phosphate (Ser) (covalent) (by protein !8kinase C) #status experimental\ !$763,790 #binding_site phosphate (Ser) (covalent) (by cAMP- !8and cGMP-dependent kinases) #status predicted\ !$889,895 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$1246 #binding_site ATP (Lys) #status predicted SUMMARY #length 1476 #molecular-weight 167869 #checksum 9437 SEQUENCE /// ENTRY S19421 #type complete TITLE ATP-dependent permease ADP1 precursor - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YCR011c; protein YCR105 ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 19-Jan-2001 ACCESSIONS S19421; S40914 REFERENCE S19420 !$#authors Goffeau, A.; Purnelle, B.; Skala, J. !$#submission submitted to the Protein Sequence Database, March 1992 !$#accession S19421 !'##molecule_type DNA !'##residues 1-1049 ##label GOF !'##cross-references EMBL:X59720; NID:g1907116; PIDN:CAA42328.1; !1PID:g1907154; GSPDB:GN00003; MIPS:YCR011c REFERENCE S40914 !$#authors Purnelle, B.; Skala, J.; Goffeau, A. !$#journal Yeast (1991) 7:867-872 !$#title The product of the YCR105 gene located on the chromosome III !1from Saccharomyces cerevisiae presents homologies to !1ATP-dependent permeases. !$#cross-references MUID:92160395; PMID:1789009 !$#accession S40914 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-1049 ##label PUR REFERENCE S25353 !$#authors Skala, J.; Purnelle, B.; Goffeau, A. !$#journal Yeast (1992) 8:409-417 !$#title The complete sequence of a 10.8 kb segment distal of SUF2 on !1the right arm of chromosome III from Saccharomyces !1cerevisiae reveals seven open reading frames including the !1RVS161, ADP1 and PGK genes. !$#cross-references MUID:92327849; PMID:1626432 !$#contents annotation GENETICS !$#gene SGD:ADP1; MIPS:YCR011c !'##cross-references SGD:S0000604; MIPS:YCR011c !$#map_position 3R CLASSIFICATION #superfamily ATP-dependent permease ADP1; ATP-binding !1cassette homology KEYWORDS ATP; glycoprotein; nucleotide binding; P-loop; transmembrane !1protein FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-1049 #product ATP-dependent permease ADP1 #status !8predicted #label MAT\ !$26-324 #domain extracellular #status predicted #label EXT\ !$325-341 #domain transmembrane #status predicted #label TM1\ !$406-607 #domain ATP-binding cassette homology #label ABC\ !$423-430 #region nucleotide-binding motif A (P-loop)\ !$550-557 #region nucleotide-binding motif B\ !$794-810 #domain transmembrane #status predicted #label TM2\ !$829-845 #domain transmembrane #status predicted #label TM3\ !$878-894 #domain transmembrane #status predicted #label TM4\ !$909-925 #domain transmembrane #status predicted #label TM5\ !$938-954 #domain transmembrane #status predicted #label TM6\ !$1025-1041 #domain transmembrane #status predicted #label TM7\ !$50,114,165,221 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$429 #binding_site ATP (Lys) #status predicted SUMMARY #length 1049 #molecular-weight 117231 #checksum 6386 SEQUENCE /// ENTRY DVBYE3 #type complete TITLE translation elongation factor eEF-3 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein L9672.5; protein YLR249w ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Dec-1990 #sequence_revision 23-Feb-1996 #text_change 19-Jan-2001 ACCESSIONS S59395; A35027; S11174; A38376 REFERENCE S59386 !$#authors Johnson, D. !$#submission submitted to the EMBL Data Library, February 1995 !$#description The sequence of S. cerevisiae cosmid 9672. !$#accession S59395 !'##molecule_type DNA !'##residues 1-1044 ##label JOH !'##cross-references EMBL:U20865; NID:g662330; PIDN:AAB67391.1; !1PID:g662335; GSPDB:GN00012; MIPS:YLR249w !'##experimental_source strain S288C (AB972) REFERENCE A35027 !$#authors Qin, S.; Xie, A.; Bonato, M.C.M.; McLaughlin, C.S. !$#journal J. Biol. Chem. (1990) 265:1903-1912 !$#title Sequence analysis of the translational elongation factor 3 !1from Saccharomyces cerevisiae. !$#cross-references MUID:90130430; PMID:2404974 !$#accession A35027 !'##molecule_type DNA !'##residues 1-152,'F',154-331,'L',333-1044 ##label QIN !'##cross-references EMBL:J05197; NID:g173213; PIDN:AAA35232.1; !1PID:g173214 REFERENCE A38376 !$#authors Sandbaken, M.G.; Lupisella, J.A.; DiDomenico, B.; !1Chakraburtty, K. !$#journal J. Biol. Chem. (1990) 265:15838-15844 !$#title Protein synthesis in yeast. Structural and functional !1analysis of the gene encoding elongation factor 3. !$#cross-references MUID:90368801; PMID:2203789 !$#accession S11174 !'##molecule_type DNA !'##residues 1-152,'F',154-331,'L',333-1044 ##label SAN !'##cross-references GB:J05583; NID:g173215; PIDN:AAA35233.1; !1PID:g173216 !'##note the sequences of residues 101-110 and 111-120 are interchanged !1in the authors' translation !'##note the authors translated the codon TTG for residues 290 and 291 !1as Lys GENETICS !$#gene SGD:YEF3; MIPS:YLR249w !'##cross-references SGD:S0004239; MIPS:YLR249w !$#map_position 12R CLASSIFICATION #superfamily translation elongation factor 3; ATP-binding !1cassette homology KEYWORDS ATP; duplication; nucleotide binding; P-loop; protein !1biosynthesis FEATURE !$446-616 #domain ATP-binding cassette homology #label ABC1\ !$463-470 #region nucleotide-binding motif A (P-loop)\ !$564-568 #region nucleotide-binding motif B\ !$684-969 #domain ATP-binding cassette homology #label ABC2\ !$701-708 #region nucleotide-binding motif A (P-loop)\ !$917-921 #region nucleotide-binding motif B\ !$469 #binding_site ATP (Lys) #status predicted\ !$707 #binding_site ATP (Lys) #status predicted SUMMARY #length 1044 #molecular-weight 115944 #checksum 9415 SEQUENCE /// ENTRY SKPSXR #type complete TITLE general secretion pathway protein E PA3103 [imported] - Pseudomonas aeruginosa (strain PAO1) ORGANISM #formal_name Pseudomonas aeruginosa DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 06-Oct-2000 ACCESSIONS S25384; G83258; S22729 REFERENCE S25384 !$#authors Bally, M.; Filloux, A.; Akrim, M.; Ball, G.; Lazdunski, A.; !1Tommassen, J. !$#journal Mol. Microbiol. (1992) 6:1121-1131 !$#title Protein secretion in Pseudomonas aeruginosa: !1characterization of seven xcp genes and processing of !1secretory apparatus components by prepilin peptidase. !$#cross-references MUID:92269572; PMID:1588814 !$#accession S25384 !'##molecule_type DNA !'##residues 1-502 ##label BAL !'##cross-references EMBL:X62666; NID:g45433; PIDN:CAA44533.1; !1PID:g45434 REFERENCE A82950 !$#authors Stover, C.K.; Pham, X.Q.; Erwin, A.L.; Mizoguchi, S.D.; !1Warrener, P.; Hickey, M.J.; Brinkman, F.S.L.; Hufnagle, !1W.O.; Kowalik, D.J.; Lagrou, M.; Garber, R.L.; Goltry, L.; !1Tolentino, E.; Westbrook-Wadman, S.; Yuan, Y.; Brody, L.L.; !1Coulter, S.N.; Folger, K.R.; Kas, A.; Larbig, K.; Lim, R.M.; !1Smith, K.A.; Spencer, D.H.; Wong, G.K.S.; Wu, Z.; Paulsen, !1I.T.; Reizer, J.; Saier, M.H.; Hancock, R.E.W.; Lory, S.; !1Olson, M.V. !$#journal Nature (2000) 406:959-964 !$#title Complete genome sequence of Pseudomonas aeruginosa PA01, an !1opportunistic pathogen. !$#cross-references MUID:20437337; PMID:10984043 !$#accession G83258 !'##status preliminary !'##molecule_type DNA !'##residues 1-502 ##label STO !'##cross-references GB:AE004734; GB:AE004091; NID:g9949204; !1PIDN:AAG06491.1; GSPDB:GN00131; PASP:PA3103 !'##experimental_source strain PAO1 GENETICS !$#gene xcpR; PA3103 CLASSIFICATION #superfamily secretion protein xcpR SUMMARY #length 502 #molecular-weight 55524 #checksum 6737 SEQUENCE /// ENTRY SKPSXS #type complete TITLE secretion protein xcpS - Pseudomonas aeruginosa ORGANISM #formal_name Pseudomonas aeruginosa DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 31-Dec-2000 ACCESSIONS S25385; F83258; S22730 REFERENCE S25384 !$#authors Bally, M.; Filloux, A.; Akrim, M.; Ball, G.; Lazdunski, A.; !1Tommassen, J. !$#journal Mol. Microbiol. (1992) 6:1121-1131 !$#title Protein secretion in Pseudomonas aeruginosa: !1characterization of seven xcp genes and processing of !1secretory apparatus components by prepilin peptidase. !$#cross-references MUID:92269572; PMID:1588814 !$#accession S25385 !'##molecule_type DNA !'##residues 1-405 ##label BAL !'##cross-references EMBL:X62666; NID:g45433; PIDN:CAA44534.1; !1PID:g45435 REFERENCE A82950 !$#authors Stover, C.K.; Pham, X.Q.; Erwin, A.L.; Mizoguchi, S.D.; !1Warrener, P.; Hickey, M.J.; Brinkman, F.S.L.; Hufnagle, !1W.O.; Kowalik, D.J.; Lagrou, M.; Garber, R.L.; Goltry, L.; !1Tolentino, E.; Westbrook-Wadman, S.; Yuan, Y.; Brody, L.L.; !1Coulter, S.N.; Folger, K.R.; Kas, A.; Larbig, K.; Lim, R.M.; !1Smith, K.A.; Spencer, D.H.; Wong, G.K.S.; Wu, Z.; Paulsen, !1I.T.; Reizer, J.; Saier, M.H.; Hancock, R.E.W.; Lory, S.; !1Olson, M.V. !$#journal Nature (2000) 406:959-964 !$#title Complete genome sequence of Pseudomonas aeruginosa PA01, an !1opportunistic pathogen. !$#cross-references MUID:20437337; PMID:10984043 !$#accession F83258 !'##status preliminary !'##molecule_type DNA !'##residues 1-405 ##label STO !'##cross-references GB:AE004734; GB:AE004091; NID:g9949204; !1PIDN:AAG06490.1; GSPDB:GN00131; PASP:PA3102 !'##experimental_source strain PAO1 GENETICS !$#gene xcpS; PA3102 CLASSIFICATION #superfamily secretion protein xcpS KEYWORDS transmembrane protein SUMMARY #length 405 #molecular-weight 44061 #checksum 5063 SEQUENCE /// ENTRY D47021 #type complete TITLE pectic enzyme secretion protein OutF - Erwinia chrysanthemi ORGANISM #formal_name Erwinia chrysanthemi DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS D47021 REFERENCE A47021 !$#authors Lindeberg, M.; Collmer, A. !$#journal J. Bacteriol. (1992) 174:7385-7397 !$#title Analysis of eight out genes in a cluster required for pectic !1enzyme secretion by Erwinia chrysanthemi: sequence !1comparison with secretion genes from other gram-negative !1bacteria. !$#cross-references MUID:93054355; PMID:1429461 !$#accession D47021 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-404 ##label LIN !'##note sequence extracted from NCBI backbone (NCBIP:118273) CLASSIFICATION #superfamily secretion protein xcpS KEYWORDS transmembrane protein FEATURE !$167-193 #domain transmembrane #status predicted #label TM1\ !$223-239 #domain transmembrane #status predicted #label TM2\ !$375-393 #domain transmembrane #status predicted #label TM3 SUMMARY #length 404 #molecular-weight 44751 #checksum 3381 SEQUENCE /// ENTRY S32860 #type complete TITLE outF protein - Erwinia carotovora subsp. carotovora ALTERNATE_NAMES probable polytopic inner membrane protein ORGANISM #formal_name Erwinia carotovora subsp. carotovora DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S32860; S31749 REFERENCE S32857 !$#authors Reeves, P.J.; Whitcombe, D.; Wharam, S.; Gibson, M.; !1Allison, G.; Bunce, N.; Barallon, R.; Douglas, P.; !1Mulholland, V.; Stevens, S.; Walker, D.; Salmond, G.P.C. !$#journal Mol. Microbiol. (1993) 8:443-456 !$#title Molecular cloning and characterization of 13 out genes from !1Erwinia carotovora subspecies carotovora: genes encoding !1members of a general secretion pathway (GSP) widespread in !1gram-negative bacteria. !$#cross-references MUID:93316842; PMID:8326859 !$#accession S32860 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-408 ##label REE !'##cross-references EMBL:X70049; NID:g42184; PIDN:CAA49647.1; !1PID:g42188 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1992 GENETICS !$#gene outF CLASSIFICATION #superfamily secretion protein xcpS KEYWORDS transmembrane protein FEATURE !$169-195 #domain transmembrane #status predicted #label TM1\ !$225-241 #domain transmembrane #status predicted #label TM2\ !$379-397 #domain transmembrane #status predicted #label TM3 SUMMARY #length 408 #molecular-weight 45161 #checksum 8022 SEQUENCE /// ENTRY S22670 #type complete TITLE hypothetical protein 3 - Aeromonas hydrophila ORGANISM #formal_name Aeromonas hydrophila DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S22670 REFERENCE S22668 !$#authors Jiang, B.; Howard, S.P. !$#journal Mol. Microbiol. (1992) 6:1351-1361 !$#title The Aeromonas hydrophila exeE gene, required both for !1protein secretion and normal outer membrane biogenesis, is a !1member of a general secretion pathway. !$#cross-references MUID:92349963; PMID:1640836 !$#accession S22670 !'##status preliminary !'##molecule_type DNA !'##residues 1-388 ##label JIA !'##cross-references EMBL:X66504; NID:g551420; PIDN:CAA47127.1; !1PID:g809648 !'##note the authors translated the initiation codon GTG for residue 1 !1as Val GENETICS !$#start_codon GTG CLASSIFICATION #superfamily secretion protein xcpS KEYWORDS transmembrane protein FEATURE !$149-175 #domain transmembrane #status predicted #label TM1\ !$205-221 #domain transmembrane #status predicted #label TM2\ !$359-377 #domain transmembrane #status predicted #label TM3 SUMMARY #length 388 #molecular-weight 43463 #checksum 9122 SEQUENCE /// ENTRY B65126 #type complete TITLE probable general secretion pathway protein f - Escherichia coli (strain K-12) ALTERNATE_NAMES hopF protein ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS B65126; A56150 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65126 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-398 ##label BLAT !'##cross-references GB:AE000409; GB:U00096; NID:g1789718; !1PIDN:AAC76352.1; PID:g1789724; UWGP:b3327 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A56150 !$#authors Stojiljkovic, I.; Schoenherr, R.; Kusters, J.G. !$#journal J. Bacteriol. (1995) 177:1892-1895 !$#title Identification of the hopG gene, a component of Escherichia !1coli K-12 type II export system, and its conservation among !1different pathogenic Escherichia coli and Shigella isolates. !$#cross-references MUID:95204361; PMID:7896718 !$#accession A56150 !'##status preliminary !'##molecule_type DNA !'##residues 195-269,'P',271-398 ##label STO !'##cross-references GB:U20786; NID:g693704; PIDN:AAA69030.1; !1PID:g693705 !'##note authors translated the codon ATG for residue 396 as Gly, ATT !1for residue 397 as Lys, and AAT for residue 398 as His GENETICS !$#gene hofF; hopF CLASSIFICATION #superfamily secretion protein xcpS KEYWORDS transmembrane protein SUMMARY #length 398 #molecular-weight 44339 #checksum 4905 SEQUENCE /// ENTRY B35384 #type complete TITLE pilC protein - Pseudomonas aeruginosa ORGANISM #formal_name Pseudomonas aeruginosa DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B35384 REFERENCE A35384 !$#authors Nunn, D.; Bergman, S.; Lory, S. !$#journal J. Bacteriol. (1990) 172:2911-2919 !$#title Products of three accessory genes, pilB, pilC, and pilD, are !1required for biogenesis of Pseudomonas aeruginosa pili. !$#cross-references MUID:90264276; PMID:1971619 !$#accession B35384 !'##status preliminary !'##molecule_type DNA !'##residues 1-406 ##label NUN !'##cross-references GB:M32066; NID:g151064; PIDN:AAA25733.1; !1PID:g151066 CLASSIFICATION #superfamily secretion protein xcpS KEYWORDS transmembrane protein SUMMARY #length 406 #molecular-weight 44549 #checksum 3647 SEQUENCE /// ENTRY A36961 #type complete TITLE pilin biogenesis protein pilC - Pseudomonas putida ORGANISM #formal_name Pseudomonas putida DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A36961; S35952 REFERENCE A36961 !$#authors de Groot, A.; Heijnen, I.; de Cock, H.; Filloux, A.; !1Tommassen, J. !$#journal J. Bacteriol. (1994) 176:642-650 !$#title Characterization of type IV pilus genes in plant !1growth-promoting Pseudomonas putida WCS358. !$#cross-references MUID:94131942; PMID:7905475 !$#accession A36961 !'##status preliminary !'##molecule_type DNA !'##residues 1-401 ##label DEA !'##cross-references EMBL:X74276; NID:g396262; PIDN:CAA52333.1; !1PID:g396264 GENETICS !$#gene pilC CLASSIFICATION #superfamily secretion protein xcpS KEYWORDS transmembrane protein SUMMARY #length 401 #molecular-weight 43084 #checksum 8884 SEQUENCE /// ENTRY S17938 #type complete TITLE xpsF protein - Xanthomonas campestris pv. campestris ORGANISM #formal_name Xanthomonas campestris pv. campestris DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S17938 REFERENCE S17937 !$#authors Dums, F.; Dow, J.M.; Daniels, M.J. !$#journal Mol. Gen. Genet. (1991) 229:357-364 !$#title Structural characterization of protein secretion genes of !1the bacterial phytopathogen Xanthomonas campestris pathovar !1campestris: relatedness to secretion systems of other !1gram-negative bacteria. !$#cross-references MUID:92049233; PMID:1944223 !$#accession S17938 !'##molecule_type DNA !'##residues 1-390 ##label DUM !'##cross-references EMBL:X59079; NID:g48896; PIDN:CAA41804.1; !1PID:g48898 GENETICS !$#gene xpsF CLASSIFICATION #superfamily secretion protein xcpS KEYWORDS transmembrane protein SUMMARY #length 390 #molecular-weight 42348 #checksum 4061 SEQUENCE /// ENTRY D64060 #type complete TITLE pilus assembly protein pilG homolog - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS D64060 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession D64060 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-406 ##label TIGR !'##cross-references GB:U32715; GB:L42023; NID:g1573254; !1PIDN:AAC21961.1; PID:g1573265; TIGR:HI0297 CLASSIFICATION #superfamily secretion protein xcpS KEYWORDS transmembrane protein SUMMARY #length 406 #molecular-weight 46290 #checksum 8172 SEQUENCE /// ENTRY SKPSXT #type complete TITLE secretion protein xcpT - Pseudomonas aeruginosa ORGANISM #formal_name Pseudomonas aeruginosa DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS S25386; S22731 REFERENCE S25384 !$#authors Bally, M.; Filloux, A.; Akrim, M.; Ball, G.; Lazdunski, A.; !1Tommassen, J. !$#journal Mol. Microbiol. (1992) 6:1121-1131 !$#title Protein secretion in Pseudomonas aeruginosa: !1characterization of seven xcp genes and processing of !1secretory apparatus components by prepilin peptidase. !$#cross-references MUID:92269572; PMID:1588814 !$#accession S25386 !'##molecule_type DNA !'##residues 1-142 ##label BAL !'##cross-references EMBL:X62666; NID:g45433; PIDN:CAA44535.1; !1PID:g581440 GENETICS !$#gene xcpT !$#start_codon TTG CLASSIFICATION #superfamily secretion protein xcpT SUMMARY #length 142 #molecular-weight 15449 #checksum 2410 SEQUENCE /// ENTRY SKPSXU #type complete TITLE secretion protein xcpU - Pseudomonas aeruginosa ORGANISM #formal_name Pseudomonas aeruginosa DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 06-Oct-2000 ACCESSIONS S25387; D83258; S22732 REFERENCE S25384 !$#authors Bally, M.; Filloux, A.; Akrim, M.; Ball, G.; Lazdunski, A.; !1Tommassen, J. !$#journal Mol. Microbiol. (1992) 6:1121-1131 !$#title Protein secretion in Pseudomonas aeruginosa: !1characterization of seven xcp genes and processing of !1secretory apparatus components by prepilin peptidase. !$#cross-references MUID:92269572; PMID:1588814 !$#accession S25387 !'##molecule_type DNA !'##residues 1-172 ##label BAL !'##cross-references EMBL:X62666; NID:g45433; PIDN:CAA44536.1; !1PID:g45437 REFERENCE A82950 !$#authors Stover, C.K.; Pham, X.Q.; Erwin, A.L.; Mizoguchi, S.D.; !1Warrener, P.; Hickey, M.J.; Brinkman, F.S.L.; Hufnagle, !1W.O.; Kowalik, D.J.; Lagrou, M.; Garber, R.L.; Goltry, L.; !1Tolentino, E.; Westbrook-Wadman, S.; Yuan, Y.; Brody, L.L.; !1Coulter, S.N.; Folger, K.R.; Kas, A.; Larbig, K.; Lim, R.M.; !1Smith, K.A.; Spencer, D.H.; Wong, G.K.S.; Wu, Z.; Paulsen, !1I.T.; Reizer, J.; Saier, M.H.; Hancock, R.E.W.; Lory, S.; !1Olson, M.V. !$#journal Nature (2000) 406:959-964 !$#title Complete genome sequence of Pseudomonas aeruginosa PA01, an !1opportunistic pathogen. !$#cross-references MUID:20437337; PMID:10984043 !$#accession D83258 !'##status preliminary !'##molecule_type DNA !'##residues 1-172 ##label STO !'##cross-references GB:AE004734; GB:AE004091; NID:g9949204; !1PIDN:AAG06488.1; GSPDB:GN00131; PASP:PA3100 !'##experimental_source strain PAO1 GENETICS !$#gene xcpU; PA3100 CLASSIFICATION #superfamily secretion protein xcpU SUMMARY #length 172 #molecular-weight 19148 #checksum 5401 SEQUENCE /// ENTRY SKPSXV #type complete TITLE secretion protein xcpV - Pseudomonas aeruginosa ALTERNATE_NAMES general secretion pathway protein I ORGANISM #formal_name Pseudomonas aeruginosa DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 31-Dec-2000 ACCESSIONS S25388; C83258; S22733 REFERENCE S25384 !$#authors Bally, M.; Filloux, A.; Akrim, M.; Ball, G.; Lazdunski, A.; !1Tommassen, J. !$#journal Mol. Microbiol. (1992) 6:1121-1131 !$#title Protein secretion in Pseudomonas aeruginosa: !1characterization of seven xcp genes and processing of !1secretory apparatus components by prepilin peptidase. !$#cross-references MUID:92269572; PMID:1588814 !$#accession S25388 !'##molecule_type DNA !'##residues 1-129 ##label BAL !'##cross-references EMBL:X62666; NID:g45433; PIDN:CAA44537.1; !1PID:g45438 REFERENCE A82950 !$#authors Stover, C.K.; Pham, X.Q.; Erwin, A.L.; Mizoguchi, S.D.; !1Warrener, P.; Hickey, M.J.; Brinkman, F.S.L.; Hufnagle, !1W.O.; Kowalik, D.J.; Lagrou, M.; Garber, R.L.; Goltry, L.; !1Tolentino, E.; Westbrook-Wadman, S.; Yuan, Y.; Brody, L.L.; !1Coulter, S.N.; Folger, K.R.; Kas, A.; Larbig, K.; Lim, R.M.; !1Smith, K.A.; Spencer, D.H.; Wong, G.K.S.; Wu, Z.; Paulsen, !1I.T.; Reizer, J.; Saier, M.H.; Hancock, R.E.W.; Lory, S.; !1Olson, M.V. !$#journal Nature (2000) 406:959-964 !$#title Complete genome sequence of Pseudomonas aeruginosa PA01, an !1opportunistic pathogen. !$#cross-references MUID:20437337; PMID:10984043 !$#accession C83258 !'##status preliminary !'##molecule_type DNA !'##residues 1-129 ##label STO !'##cross-references GB:AE004734; GB:AE004091; NID:g9949204; !1PIDN:AAG06487.1; GSPDB:GN00131; PASP:PA3099 !'##experimental_source strain PAO1 GENETICS !$#gene xcpV; PA3099 CLASSIFICATION #superfamily secretion protein xcpV SUMMARY #length 129 #molecular-weight 14380 #checksum 676 SEQUENCE /// ENTRY SKPSXW #type complete TITLE general secretion pathway protein J PA3098 [imported] - Pseudomonas aeruginosa ORGANISM #formal_name Pseudomonas aeruginosa DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 31-Dec-2000 ACCESSIONS S25389; B83258; S22734 REFERENCE S25384 !$#authors Bally, M.; Filloux, A.; Akrim, M.; Ball, G.; Lazdunski, A.; !1Tommassen, J. !$#journal Mol. Microbiol. (1992) 6:1121-1131 !$#title Protein secretion in Pseudomonas aeruginosa: !1characterization of seven xcp genes and processing of !1secretory apparatus components by prepilin peptidase. !$#cross-references MUID:92269572; PMID:1588814 !$#accession S25389 !'##molecule_type DNA !'##residues 1-237 ##label BAL !'##cross-references EMBL:X62666; NID:g45433; PIDN:CAA44538.1; !1PID:g45439 REFERENCE A82950 !$#authors Stover, C.K.; Pham, X.Q.; Erwin, A.L.; Mizoguchi, S.D.; !1Warrener, P.; Hickey, M.J.; Brinkman, F.S.L.; Hufnagle, !1W.O.; Kowalik, D.J.; Lagrou, M.; Garber, R.L.; Goltry, L.; !1Tolentino, E.; Westbrook-Wadman, S.; Yuan, Y.; Brody, L.L.; !1Coulter, S.N.; Folger, K.R.; Kas, A.; Larbig, K.; Lim, R.M.; !1Smith, K.A.; Spencer, D.H.; Wong, G.K.S.; Wu, Z.; Paulsen, !1I.T.; Reizer, J.; Saier, M.H.; Hancock, R.E.W.; Lory, S.; !1Olson, M.V. !$#journal Nature (2000) 406:959-964 !$#title Complete genome sequence of Pseudomonas aeruginosa PA01, an !1opportunistic pathogen. !$#cross-references MUID:20437337; PMID:10984043 !$#accession B83258 !'##status preliminary !'##molecule_type DNA !'##residues 1-237 ##label STO !'##cross-references GB:AE004734; GB:AE004091; NID:g9949204; !1PIDN:AAG06486.1; GSPDB:GN00131; PASP:PA3098 !'##experimental_source strain PAO1 GENETICS !$#gene xcpW; PA3098 CLASSIFICATION #superfamily secretion protein xcpW SUMMARY #length 237 #molecular-weight 27130 #checksum 630 SEQUENCE /// ENTRY SKPSXX #type complete TITLE secretion protein xcpX - Pseudomonas aeruginosa ORGANISM #formal_name Pseudomonas aeruginosa DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 31-Dec-2000 ACCESSIONS S25390; A83258; S22735 REFERENCE S25384 !$#authors Bally, M.; Filloux, A.; Akrim, M.; Ball, G.; Lazdunski, A.; !1Tommassen, J. !$#journal Mol. Microbiol. (1992) 6:1121-1131 !$#title Protein secretion in Pseudomonas aeruginosa: !1characterization of seven xcp genes and processing of !1secretory apparatus components by prepilin peptidase. !$#cross-references MUID:92269572; PMID:1588814 !$#accession S25390 !'##molecule_type DNA !'##residues 1-333 ##label BAL !'##cross-references EMBL:X62666; NID:g45433; PIDN:CAA44539.1; !1PID:g45440 REFERENCE A82950 !$#authors Stover, C.K.; Pham, X.Q.; Erwin, A.L.; Mizoguchi, S.D.; !1Warrener, P.; Hickey, M.J.; Brinkman, F.S.L.; Hufnagle, !1W.O.; Kowalik, D.J.; Lagrou, M.; Garber, R.L.; Goltry, L.; !1Tolentino, E.; Westbrook-Wadman, S.; Yuan, Y.; Brody, L.L.; !1Coulter, S.N.; Folger, K.R.; Kas, A.; Larbig, K.; Lim, R.M.; !1Smith, K.A.; Spencer, D.H.; Wong, G.K.S.; Wu, Z.; Paulsen, !1I.T.; Reizer, J.; Saier, M.H.; Hancock, R.E.W.; Lory, S.; !1Olson, M.V. !$#journal Nature (2000) 406:959-964 !$#title Complete genome sequence of Pseudomonas aeruginosa PA01, an !1opportunistic pathogen. !$#cross-references MUID:20437337; PMID:10984043 !$#accession A83258 !'##status preliminary !'##molecule_type DNA !'##residues 1-333 ##label STO !'##cross-references GB:AE004734; GB:AE004091; NID:g9949204; !1PIDN:AAG06485.1; GSPDB:GN00131; PASP:PA3097 !'##experimental_source strain PAO1 GENETICS !$#gene xcpX; PA3097 CLASSIFICATION #superfamily secretion protein xcpX KEYWORDS transmembrane protein SUMMARY #length 333 #molecular-weight 37000 #checksum 9789 SEQUENCE /// ENTRY IKEC5B #type complete TITLE colicin V secretion protein cvaB - Escherichia coli plasmid ColV ORGANISM #formal_name Escherichia coli DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 19-Jan-2001 ACCESSIONS S12272 REFERENCE S12271 !$#authors Gilson, L.; Mahanty, H.K.; Kolter, R. !$#journal EMBO J. (1990) 9:3875-3884 !$#title Genetic analysis of an MDR-like export system: the secretion !1of colicin V. !$#cross-references MUID:91065315; PMID:2249654 !$#accession S12272 !'##molecule_type DNA !'##residues 1-698 ##label GIL !'##cross-references EMBL:X57524; NID:g41174; PIDN:CAA40744.1; !1PID:g41176 GENETICS !$#gene cvaB !$#genome plasmid CLASSIFICATION #superfamily hemolysin secretion protein B; ATP-binding !1cassette homology KEYWORDS ATP; nucleotide binding; P-loop; transmembrane protein FEATURE !$179-200 #domain transmembrane #status predicted #label TM1\ !$212-233 #domain transmembrane #status predicted #label TM2\ !$285-304 #domain transmembrane #status predicted #label TM3\ !$309-329 #domain transmembrane #status predicted #label TM4\ !$397-417 #domain transmembrane #status predicted #label TM5\ !$421-438 #domain transmembrane #status predicted #label TM6\ !$439-698 #domain intracellular #status predicted #label INT\ !$509-698 #domain ATP-binding cassette homology #label ABC\ !$526-533 #region nucleotide-binding motif A (P-loop)\ !$650-655 #region nucleotide-binding motif B\ !$532 #binding_site ATP (Lys) #status predicted SUMMARY #length 698 #molecular-weight 78245 #checksum 6574 SEQUENCE /// ENTRY LEECB #type complete TITLE hemolysin secretion protein hlyB - Escherichia coli ALTERNATE_NAMES hemolysin transporter hlyB ORGANISM #formal_name Escherichia coli DATE 30-Sep-1988 #sequence_revision 03-Oct-1995 #text_change 19-Jan-2001 ACCESSIONS A42255; B24433 REFERENCE A42255 !$#authors Juranka, P.; Zhang, F.; Kulpa, J.; Endicott, J.; Blight, M.; !1Holland, I.B.; Ling, V. !$#journal J. Biol. Chem. (1992) 267:3764-3770 !$#title Characterization of the hemolysin transporter, HlyB, using !1an epitope insertion. !$#cross-references MUID:92156111; PMID:1371277 !$#accession A42255 !'##molecule_type DNA !'##residues 1-707 ##label JUR !'##cross-references GB:M81823; NID:g146382; PIDN:AAA23978.1; !1PID:g146383 !'##experimental_source cell line LE2001 !'##note sequence extracted from NCBI backbone (NCBIN:82595, !1NCBIP:82597) REFERENCE A24433 !$#authors Felmlee, T.; Pellett, S.; Welch, R.A. !$#journal J. Bacteriol. (1985) 163:94-105 !$#title Nucleotide sequence of an Escherichia coli chromosomal !1hemolysin. !$#cross-references MUID:85234404; PMID:3891743 !$#accession B24433 !'##molecule_type DNA !'##residues 1-81,'C',83-131,'T',133-151,'K',153-188,'QP',191, !1'MLLLSHYLLWWCLRL',207-642,'V',644-707 ##label FEL !'##experimental_source strain J96, O4 serotype GENETICS !$#gene hylB CLASSIFICATION #superfamily hemolysin secretion protein B; ATP-binding !1cassette homology KEYWORDS ATP; nucleotide binding; P-loop; transmembrane protein FEATURE !$485-679 #domain ATP-binding cassette homology #label ABC\ !$502-509 #region nucleotide-binding motif A (P-loop)\ !$626-630 #region nucleotide-binding motif B\ !$508 #binding_site ATP (Lys) #status predicted SUMMARY #length 707 #molecular-weight 79528 #checksum 96 SEQUENCE /// ENTRY LEEBBV #type complete TITLE hemolysin secretion protein hlyB - Proteus vulgaris ORGANISM #formal_name Proteus vulgaris DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 19-Jan-2001 ACCESSIONS S05477 REFERENCE S05477 !$#authors Koronakis, V.; Koronakis, E.; Hughes, C. !$#journal Mol. Gen. Genet. (1988) 213:551-555 !$#title Comparison of the haemolysin secretion protein HlyB from !1Proteus vulgaris and Escherichia coli; site-directed !1mutagenesis causing impairment of export function. !$#cross-references MUID:89039746; PMID:3054490 !$#accession S05477 !'##molecule_type DNA !'##residues 1-707 ##label KOR !'##cross-references EMBL:X12852; NID:g45903; PIDN:CAA31330.1; !1PID:g45904 !'##note the authors translated the codon GTT for residue 39 as Thr, CAA !1for residue 456 as His, AAT for residue 491 as Ser, and GAT !1for residue 693 as Glu GENETICS !$#gene hlyB CLASSIFICATION #superfamily hemolysin secretion protein B; ATP-binding !1cassette homology KEYWORDS ATP; nucleotide binding; P-loop; transmembrane protein FEATURE !$158-179 #domain transmembrane #status predicted #label TM1\ !$187-204 #domain transmembrane #status predicted #label TM2\ !$269-289 #domain transmembrane #status predicted #label TM3\ !$293-311 #domain transmembrane #status predicted #label TM4\ !$360-377 #domain transmembrane #status predicted #label TM5\ !$387-403 #domain transmembrane #status predicted #label TM6\ !$407-425 #domain transmembrane #status predicted #label TM7\ !$485-679 #domain ATP-binding cassette homology #label ABC\ !$502-509 #region nucleotide-binding motif A (P-loop)\ !$626-630 #region nucleotide-binding motif B\ !$656-660 #region nucleotide-binding motif B\ !$508 #binding_site ATP (Lys) #status predicted\ !$625 #binding_site ATP (Lys) #status predicted SUMMARY #length 707 #molecular-weight 79939 #checksum 4068 SEQUENCE /// ENTRY BVBRCB #type complete TITLE cyaB protein - Bordetella pertussis ORGANISM #formal_name Bordetella pertussis DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 19-Jan-2001 ACCESSIONS S02386 REFERENCE S02386 !$#authors Glaser, P.; Sakamoto, H.; Bellalou, J.; Ullmann, A.; !1Danchin, A. !$#journal EMBO J. (1988) 7:3997-4004 !$#title Secretion of cyclolysin, the calmodulin-sensitive adenylate !1cyclase--haemolysin bifunctional protein of Bordetella !1pertussis. !$#cross-references MUID:89091151; PMID:2905265 !$#accession S02386 !'##molecule_type DNA !'##residues 1-712 ##label GLA !'##cross-references GB:X14199; NID:g39731; PIDN:CAA32412.1; PID:g39733 COMMENT This protein is required for the transport of cyclolysin (or !1calmodulin-sensitive adenylate cyclase-hemolysin !1bifunctional protein, encoded by cyaA) across the cell !1envelope and for its release into the external medium. This !1secretion process is very similar to that of the E. coli !1alpha-hemolysin. GENETICS !$#gene cyaB CLASSIFICATION #superfamily hemolysin secretion protein B; ATP-binding !1cassette homology KEYWORDS ATP; cyclolysin transport; membrane protein; nucleotide !1binding; P-loop FEATURE !$488-682 #domain ATP-binding cassette homology #label ABC\ !$505-512 #region nucleotide-binding motif A (P-loop)\ !$629-633 #region nucleotide-binding motif B\ !$511 #binding_site ATP (Lys) #status predicted SUMMARY #length 712 #molecular-weight 77969 #checksum 2892 SEQUENCE /// ENTRY VXAGCA #type complete TITLE beta-1,2-glucan export protein chvA - Agrobacterium tumefaciens ORGANISM #formal_name Agrobacterium tumefaciens DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS A32810 REFERENCE A32810 !$#authors Cangelosi, G.A.; Martinetti, G.; Leigh, J.A.; Lee, C.C.; !1Theines, C.; Nester, E.W. !$#journal J. Bacteriol. (1989) 171:1609-1615 !$#title Role of Agrobacterium tumefaciens chvA protein in export of !1beta-1,2-glucan. !$#cross-references MUID:89155469; PMID:2921245 !$#accession A32810 !'##molecule_type DNA !'##residues 1-588 ##label CAN !'##cross-references GB:M24198; NID:g142223; PIDN:AAA22083.1; !1PID:g142224 COMMENT This protein is required for the export (transport across !1the inner membrane) of a cyclic extracellular !1polysaccharide, beta-1,2-glucan, that is essential for !1attachment of A. tumefaciens to plant cells. GENETICS !$#gene chvA !$#start_codon GTG CLASSIFICATION #superfamily beta-1,2-glucan export protein chvA; !1ATP-binding cassette homology KEYWORDS ATP; inner membrane; nucleotide binding; P-loop; !1polysaccharide export FEATURE !$351-545 #domain ATP-binding cassette homology #label ABC\ !$368-375 #region nucleotide-binding motif A (P-loop)\ !$492-496 #region nucleotide-binding motif B SUMMARY #length 588 #molecular-weight 64651 #checksum 5322 SEQUENCE /// ENTRY VXZRNA #type complete TITLE beta-1,2-glucan export protein ndvA - Rhizobium meliloti ORGANISM #formal_name Rhizobium meliloti DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS A31094 REFERENCE A31094 !$#authors Stanfield, S.W.; Ielpi, L.; O'Brochta, D.; Helinski, D.R.; !1Ditta, G.S. !$#journal J. Bacteriol. (1988) 170:3523-3530 !$#title The ndvA gene product of Rhizobium meliloti is required for !1beta-(1->2) glucan production and has homology to the !1ATP-binding export protein HlyB. !$#cross-references MUID:88298659; PMID:3042754 !$#accession A31094 !'##molecule_type DNA !'##residues 1-616 ##label STA !'##cross-references GB:M20726; NID:g152268; PIDN:AAA26304.1; !1PID:g152269 COMMENT This protein is required for the export (transport across !1the inner membrane) of a cyclic extracellular !1polysaccharide, beta-(1,2)glucan, that is essential for !1inducing normal nitrogen-fixing nodules on the roots of !1legumes. GENETICS !$#gene ndvA CLASSIFICATION #superfamily beta-1,2-glucan export protein chvA; !1ATP-binding cassette homology KEYWORDS ATP; inner membrane; nucleotide binding; P-loop; !1polysaccharide export FEATURE !$382-576 #domain ATP-binding cassette homology #label ABC\ !$399-406 #region nucleotide-binding motif A (P-loop)\ !$523-527 #region nucleotide-binding motif B SUMMARY #length 616 #molecular-weight 67238 #checksum 3846 SEQUENCE /// ENTRY FYFFW #type complete TITLE white protein - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 31-Dec-1990 #sequence_revision 17-Feb-1995 #text_change 19-Jan-2001 ACCESSIONS S08635; S07263; S10240 REFERENCE S08635 !$#authors Pepling, M.; Mount, S.M. !$#journal Nucleic Acids Res. (1990) 18:1633 !$#title Sequence of a cDNA from the Drosophila melanogaster white !1gene. !$#cross-references MUID:90221897; PMID:2109311 !$#accession S08635 !'##molecule_type mRNA !'##residues 1-687 ##label PEP !'##cross-references EMBL:X51749; NID:g8825; PIDN:CAA36038.1; PID:g8826 REFERENCE S07263 !$#authors O'Hare, K.; Murphy, C.; Levis, R.; Rubin, G.M. !$#journal J. Mol. Biol. (1984) 180:437-455 !$#title DNA sequence of the white locus of Drosophila melanogaster. !$#cross-references MUID:85134865; PMID:6084717 !$#accession S07263 !'##molecule_type DNA !'##residues 1-24,'LIFEIPYHCRVTAD',30-334, !1'ITLHLNSYPAWVPSVLPTTIRRTFTYRCWPLCPDGRSSPVIGSPRYG',372-687 !1##label OHA1 !'##cross-references EMBL:X02974 !'##experimental_source strain Canton S REFERENCE S10240 !$#authors O'Hare, K. !$#submission submitted to the EMBL Data Library, June 1985 !$#accession S10240 !'##molecule_type DNA !'##residues 1-24,'LIFEIPYHCRVTAD',30-687 ##label OHA2 !'##cross-references EMBL:X02974; NID:g10873; PIDN:CAA26716.1; !1PID:g10874 !'##experimental_source strain Canton S GENETICS !$#gene white; w !'##cross-references FlyBase:FBgn0003996 !$#introns 24/3; 116/1; 334/2; 439/3; 483/3 CLASSIFICATION #superfamily fruit fly white protein; ATP-binding cassette !1homology KEYWORDS ATP; glycoprotein; nucleotide binding; P-loop; transmembrane !1protein FEATURE !$113-317 #domain ATP-binding cassette homology #label ABC\ !$130-137 #region nucleotide-binding motif A (P-loop)\ !$261-265 #region nucleotide-binding motif B\ !$67,93,472,554,651 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 687 #molecular-weight 75672 #checksum 9163 SEQUENCE /// ENTRY FYFFB #type complete TITLE brown protein - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 19-Jan-2001 ACCESSIONS A31399 REFERENCE A31399 !$#authors Dreesen, T.D.; Johnson, D.H.; Henikoff, S. !$#journal Mol. Cell. Biol. (1988) 8:5206-5215 !$#title The brown protein of Drosophila melanogaster is similar to !1the white protein and to components of active transport !1complexes. !$#cross-references MUID:89218981; PMID:3149712 !$#accession A31399 !'##molecule_type mRNA !'##residues 1-675 ##label DRE !'##cross-references GB:M20630; NID:g157013; PIDN:AAA28397.1; !1PID:g157014 COMMENT This is one of the proteins involved in deposition and !1transport of screening pigments of the Drosophila compound !1eye. GENETICS !$#gene brown !'##cross-references FlyBase:FBgn0000241 CLASSIFICATION #superfamily fruit fly white protein; ATP-binding cassette !1homology KEYWORDS ATP; glycoprotein; membrane protein; nucleotide binding; !1P-loop FEATURE !$49-243 #domain ATP-binding cassette homology #label ABC\ !$66-73 #region nucleotide-binding motif A (P-loop)\ !$187-191 #region nucleotide-binding motif B\ !$72 #binding_site ATP (Lys) #status predicted SUMMARY #length 675 #molecular-weight 75942 #checksum 1090 SEQUENCE /// ENTRY T02567 #type complete TITLE probable ATP-binding cassette protein T16B24.1 - Arabidopsis thaliana ALTERNATE_NAMES protein F12L6.1 ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 02-Mar-2001 ACCESSIONS T02567; T00545; C84816 REFERENCE Z14679 !$#authors Rounsley, S.D.; Kaul, S.; Lin, X.; Ketchum, K.A.; Crosby, !1M.L.; Brandon, R.C.; Sykes, S.M.; Mason, T.M.; Kerlavage, !1A.R.; Adams, M.D.; Somerville, C.R.; Venter, J.C. !$#submission submitted to the EMBL Data Library, August 1998 !$#description Arabidopsis thaliana chromosome II BAC T16B24 genomic !1sequence. !$#accession T02567 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-740 ##label ROU !'##cross-references EMBL:AC004697; NID:g3402671; PIDN:AAC28975.1; !1PID:g3402672 !'##experimental_source cultivar Columbia REFERENCE Z14168 !$#authors Rounsley, S.D.; Lin, X.; Ketchum, K.A.; Crosby, M.L.; !1Brandon, R.C.; Sykes, S.M.; Kaul, S.; Mason, T.M.; !1Kerlavage, A.R.; Adams, M.D.; Somerville, C.R.; Venter, J.C. !$#submission submitted to the EMBL Data Library, July 1998 !$#description Arabidopsis thaliana chromosome II BAC F12L6 genomic !1sequence. !$#accession T00545 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-362 ##label ROW !'##cross-references EMBL:AC004218; NID:g3355463; PIDN:AAC27826.1; !1PID:g3355464 !'##experimental_source cultivar Columbia REFERENCE A84420 !$#authors Lin, X.; Kaul, S.; Rounsley, S.D.; Shea, T.P.; Benito, M.I.; !1Town, C.D.; Fujii, C.Y.; Mason, T.M.; Bowman, C.L.; !1Barnstead, M.E.; Feldblyum, T.V.; Buell, C.R.; Ketchum, !1K.A.; Lee, J.J.; Ronning, C.M.; Koo, H.; Moffat, K.S.; !1Cronin, L.A.; Shen, M.; VanAken, S.E.; Umayam, L.; Tallon, !1L.J.; Gill, J.E.; Adams, M.D.; Carrera, A.J.; Creasy, T.H.; !1Goodman, H.M.; Somerville, C.R.; Copenhaver, G.P.; Preuss, !1D.; Nierman, W.C.; White, O.; Eisen, J.A.; Salzberg, S.L.; !1Fraser, C.M.; Venter, J.C. !$#journal Nature (1999) 402:761-768 !$#title Sequence and analysis of chromosome 2 of the plant !1Arabidopsis thaliana. !$#cross-references MUID:20083487; PMID:10617197 !$#accession C84816 !'##status preliminary !'##molecule_type DNA !'##residues 1-740 ##label STO !'##cross-references GB:AE002093; NID:g3402672; PIDN:AAC28975.1; !1GSPDB:GN00139 GENETICS !$#gene At2g39350; T16B24.1; F12L6.1 !$#map_position 2 CLASSIFICATION #superfamily Arabidopsis thaliana probable ATP-binding !1cassette protein F12L6.1; ATP-binding cassette homology KEYWORDS ATP FEATURE !$110-310 #domain ATP-binding cassette homology #label ABC SUMMARY #length 740 #molecular-weight 82331 #checksum 274 SEQUENCE /// ENTRY BVECUA #type complete TITLE excinuclease ABC chain A - Escherichia coli (strain K-12) ALTERNATE_NAMES uvrA protein CONTAINS excision endonuclease ABC (EC 3.1.-.-) chain A ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 01-Mar-2002 ACCESSIONS A23869; I78011; A65214 REFERENCE A23869 !$#authors Husain, I.; Van Houten, B.; Thomas, D.C.; Sancar, A. !$#journal J. Biol. Chem. (1986) 261:4895-4901 !$#title Sequences of Escherichia coli uvrA gene and protein reveal !1two potential ATP binding sites. !$#cross-references MUID:86168204; PMID:3007478 !$#accession A23869 !'##molecule_type DNA !'##residues 1-940 ##label HUS !'##cross-references GB:M13495; NID:g148164; PIDN:AAA24754.1; !1PID:g148165 REFERENCE I58044 !$#authors Sancar, A.; Sancar, G.B.; Rupp, W.D.; Little, J.W.; Mount, !1D.W. !$#journal Nature (1982) 298:96-98 !$#title LexA protein inhibits transcription of the E. coli uvrA gene !1in vitro. !$#cross-references MUID:82220077; PMID:6283374 !$#accession I78011 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-14 ##label RES !'##cross-references GB:J01721; NID:g148161; PIDN:AAA24753.1; !1PID:g551847 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65214 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-940 ##label BLAT !'##cross-references GB:AE000479; GB:U00096; NID:g2367340; !1PIDN:AAC77028.1; PID:g2367343; UWGP:b4058 !'##experimental_source strain K-12, substrain MG1655 COMMENT This protein is an ATPase and a DNA-binding protein that !1preferentially binds single-stranded or UV-irradiated !1double-stranded DNA. It is one of the three components of !1the ABC excinuclease, an ATP-dependent DNA repair enzyme !1that catalyzes the excision reaction of UV-damaged !1nucleotide segments producing oligomers (12-13 nucleotides !1long) having the modified base(s). GENETICS !$#gene uvrA !$#map_position 92 min CLASSIFICATION #superfamily excinuclease ABC chain A; ATP-binding cassette !1homology KEYWORDS ATP; DNA binding; DNA repair; duplication; hydrolase; !1nucleotide binding; P-loop FEATURE !$31-38 #region nucleotide-binding motif A (P-loop)\ !$623-907 #domain ATP-binding cassette homology #label ABCE\ !$640-647 #region nucleotide-binding motif A (P-loop) SUMMARY #length 940 #molecular-weight 103867 #checksum 6883 SEQUENCE /// ENTRY T46550 #type complete TITLE excinuclease ABC chain A [validated] - Thermus aquaticus ALTERNATE_NAMES nucleotide excision repair system protein uvrA CONTAINS excision endonuclease ABC (EC 3.1.-.-) chain A ORGANISM #formal_name Thermus aquaticus DATE 18-Feb-2000 #sequence_revision 18-Feb-2000 #text_change 19-Jan-2001 ACCESSIONS T46550 REFERENCE Z23060 !$#authors Yamamoto, N.; Kato, R.; Kuramitsu, S. !$#journal Gene (1996) 171:103-106 !$#title Cloning, sequencing and expression of the uvrA gene from an !1extremely thermophilic bacterium, Thermus thermophilus HB8. !$#cross-references MUID:96257202; PMID:8675016 !$#accession T46550 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-952 ##label YAM !'##cross-references EMBL:D49911; PIDN:BAA08652.1 !'##experimental_source strain HB8 !'##note the source is designated as Thermus thermophilus COMMENT This protein is an ATPase and a DNA-binding protein that !1preferentially binds single-stranded or UV-irradiated !1double-stranded DNA. It is one of the three components of !1the ABC excinuclease, an ATP-dependent DNA repair enzyme !1that catalyzes the excision reaction of UV-damaged !1nucleotide segments producing oligomers (12-13 nucleotides !1long) having the modified base(s). GENETICS !$#gene uvrA FUNCTION !$#description plays an essential role in excision repair system !1[validated, MUID:96257202] !$#note one of the most important DNA repair systems CLASSIFICATION #superfamily excinuclease ABC chain A; ATP-binding cassette !1homology KEYWORDS ATP; DNA binding; DNA repair; duplication; hydrolase; !1nucleotide binding; P-loop FEATURE !$31-38 #region nucleotide-binding motif A (P-loop)\ !$626-909 #domain ATP-binding cassette homology #label ABCE\ !$643-650 #region nucleotide-binding motif A (P-loop) SUMMARY #length 952 #molecular-weight 105232 #checksum 1361 SEQUENCE /// ENTRY MMECMF #type complete TITLE maltose transport inner membrane protein malF - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 01-Mar-2002 ACCESSIONS A03414; H65210; S17305 REFERENCE A03414 !$#authors Froshauer, S.; Beckwith, J. !$#journal J. Biol. Chem. (1984) 259:10896-10903 !$#title The nucleotide sequence of the gene for malF protein, an !1inner membrane component of the maltose transport system of !1Escherichia coli. Repeated DNA sequences are found in the !1malE-malF intercistronic region. !$#cross-references MUID:84289514; PMID:6088520 !$#accession A03414 !'##molecule_type DNA !'##residues 1-514 ##label FRO !'##cross-references GB:J01648; GB:J01639; GB:K02117; GB:M24344; !1GB:M24345; NID:g146697; PIDN:AAB59055.1; PID:g455175 REFERENCE S17305 !$#authors McGovern, K.; Ehrmann, M.; Beckwith, J. !$#journal EMBO J. (1991) 10:2773-2782 !$#title Decoding signals for membrane protein assembly using !1alkaline phosphatase fusions. !$#cross-references MUID:92007720; PMID:1915262 !$#contents annotation REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65210 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-514 ##label BLAT !'##cross-references GB:AE000476; GB:U00096; NID:g1790456; !1PIDN:AAC77003.1; PID:g1790465; UWGP:b4033 !'##experimental_source strain K-12, substrain MG1655 COMMENT This protein is an inner-membrane-bound component of the !1maltose transport system; a substantial portion of it !1protrudes into the periplasmic space. GENETICS !$#gene malF !$#map_position 92 min CLASSIFICATION #superfamily inner membrane protein malF KEYWORDS transmembrane protein SUMMARY #length 514 #molecular-weight 57013 #checksum 6076 SEQUENCE /// ENTRY S63615 #type complete TITLE malF protein homolog cymF - Klebsiella oxytoca ORGANISM #formal_name Klebsiella oxytoca DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S63615; S55408 REFERENCE S63612 !$#authors Fiedler, G.; Pajatsch, M.; Boeck, A. !$#journal J. Mol. Biol. (1996) 256:279-291 !$#title Genetics of a novel starch utilisation pathway present in !1Klebsiella oxytoca. !$#cross-references MUID:96174475; PMID:8594196 !$#accession S63615 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-427 ##label FIE !'##cross-references EMBL:X86014; NID:g854227; PIDN:CAA60005.1; !1PID:g854233 GENETICS !$#gene cymF CLASSIFICATION #superfamily inner membrane protein malF KEYWORDS transmembrane protein SUMMARY #length 427 #molecular-weight 48061 #checksum 1641 SEQUENCE /// ENTRY S32570 #type complete TITLE malC protein - Streptococcus pneumoniae ORGANISM #formal_name Streptococcus pneumoniae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S32570 REFERENCE S32569 !$#authors Puyet, A.; Espinosa, M. !$#journal J. Mol. Biol. (1993) 230:800-811 !$#title Structure of the maltodextrin-uptake locus of Streptococcus !1pneumoniae. Correlation to the Escherichia coli maltose !1regulon. !$#cross-references MUID:93240534; PMID:8478935 !$#accession S32570 !'##status preliminary !'##molecule_type DNA !'##residues 1-430 ##label PUY !'##cross-references EMBL:L08611; NID:g153722; PIDN:AAA26926.1; !1PID:g153724 CLASSIFICATION #superfamily inner membrane protein malF KEYWORDS transmembrane protein SUMMARY #length 430 #molecular-weight 47661 #checksum 2891 SEQUENCE /// ENTRY MMECUA #type complete TITLE sn-Glycerol-3-phosphate transport system permease protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 01-Mar-2002 ACCESSIONS S03781; S47671; G65141 REFERENCE S03780 !$#authors Overduin, P.; Boos, W.; Tommassen, J. !$#journal Mol. Microbiol. (1988) 2:767-775 !$#title Nucleotide sequence of the ugp genes of Escherichia coli !1K-12: homology to the maltose system. !$#cross-references MUID:89096498; PMID:3062310 !$#accession S03781 !'##molecule_type DNA !'##residues 1-295 ##label OVE !'##cross-references EMBL:X13141; NID:g43243; PIDN:CAA31532.1; !1PID:g43247 REFERENCE S47666 !$#authors Plunkett, G. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S47671 !'##molecule_type DNA !'##residues 1-295 ##label PLU !'##cross-references EMBL:U00039; NID:g466582; PIDN:AAB18427.1; !1PID:g466588 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65141 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-295 ##label BLAT !'##cross-references GB:AE000421; GB:U00096; NID:g1789854; !1PIDN:AAC76477.1; PID:g1789861; UWGP:b3452 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ugpA !$#map_position 76 min FUNCTION !$#description one of the membrane protein components of a phosphate !1limitation-induced transport system for glycerol-3-phosphate !1and glycerophosphoryl diesters CLASSIFICATION #superfamily inner membrane protein ugpA KEYWORDS binding protein-dependent transport system; !1glycerol-3-phosphate transport; membrane protein SUMMARY #length 295 #molecular-weight 33264 #checksum 639 SEQUENCE /// ENTRY MMAGCF #type complete TITLE membrane protein lacF - Agrobacterium radiobacter ORGANISM #formal_name Agrobacterium radiobacter DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS S25248; S22740 REFERENCE S25247 !$#authors Williams, S.G.; Greenwood, J.A.; Jones, C.W. !$#journal Mol. Microbiol. (1992) 6:1755-1768 !$#title Molecular analysis of the lac operon encoding the !1binding-protein-dependent lactose transport system and !1beta-galactosidase in Agrobacterium radiobacter. !$#cross-references MUID:92334152; PMID:1630315 !$#accession S25248 !'##molecule_type DNA !'##residues 1-298 ##label WIL !'##cross-references EMBL:X66596; NID:g38967; PIDN:CAA47162.1; !1PID:g38969 GENETICS !$#gene lacF CLASSIFICATION #superfamily inner membrane protein ugpA KEYWORDS binding protein-dependent transport system; lactose !1transport; membrane protein SUMMARY #length 298 #molecular-weight 33618 #checksum 5973 SEQUENCE /// ENTRY BVECMM #type complete TITLE maltose operon periplasmic protein malM - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 01-Mar-2002 ACCESSIONS A25787; I64879; D65211; A04469 REFERENCE A92930 !$#authors Gilson, E.; Rousset, J.P.; Charbit, A.; Perrin, D.; Hofnung, !1M. !$#journal J. Mol. Biol. (1986) 191:303-311 !$#title malM, a new gene of the maltose regulon in Escherichia coli !1K12. I. malM is the last gene of the malK-lamB operon and !1encodes a periplasmic protein. !$#cross-references MUID:87141161; PMID:2434655 !$#accession A25787 !'##molecule_type DNA !'##residues 1-306 ##label GIL !'##cross-references GB:X04477; NID:g41960; PIDN:CAA28166.1; PID:g41961 !'##experimental_source strain K12 REFERENCE I51944 !$#authors Clement, J. !$#journal Ann. Inst. Pasteur Microbiol. (1982) 133:9-20 !$#title A system for genetic analysis in gene lamB: First results !1with lambda-resistant tight mutants. !$#accession I64879 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-131 ##label RES !'##cross-references GB:M26131; NID:g146593; PIDN:AAA24061.1; !1PID:g146595 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65211 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-306 ##label BLAT !'##cross-references GB:AE000477; GB:U00096; NID:g2367338; !1PIDN:AAC77007.1; PID:g1790470; UWGP:b4037 !'##experimental_source strain K-12, substrain MG1655 COMMENT This is presumably a periplasmic protein with a signal !1sequence (residues 1-22 or 1-26); it is encoded by the last !1gene of the malK-lamB operon. GENETICS !$#gene malM; molA !$#map_position 92 min CLASSIFICATION #superfamily malM protein KEYWORDS periplasmic space SUMMARY #length 306 #molecular-weight 31943 #checksum 4084 SEQUENCE /// ENTRY BLEC #type complete TITLE leucine/isoleucine/valine-binding protein precursor - Escherichia coli (strain K-12) ALTERNATE_NAMES leucine transport protein livJ precursor; LIV-binding protein ORGANISM #formal_name Escherichia coli DATE 31-May-1979 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS G65142; A23576; A37074; A03415; S47679; I55524 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65142 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-386 ##label BLAT !'##cross-references GB:AE000422; GB:U00096; NID:g1789868; !1PIDN:AAC76485.1; PID:g1789870; UWGP:b3460 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A94677 !$#authors Landick, R.; Oxender, D.L. !$#journal J. Biol. Chem. (1985) 260:8257-8261 !$#title The complete nucleotide sequences of the Escherichia coli !1LIV-BP and LS-BP genes. Implications for the mechanism of !1high-affinity branched-chain amino acid transport. !$#cross-references MUID:85234531; PMID:3891753 !$#accession A23576 !'##molecule_type DNA !'##residues 20-21,'T',23-30,'L',32-88,'A',90-386 ##label LAN !'##cross-references GB:J05516; GB:K02178; GB:M10426; GB:M10427; !1GB:M13166; NID:g146630; PIDN:AAA83881.1; PID:g146631 REFERENCE A37074 !$#authors Adams, M.D.; Wagner, L.M.; Graddis, T.J.; Landick, R.; !1Antonucci, T.K.; Gibson, A.L.; Oxender, D.L. !$#journal J. Biol. Chem. (1990) 265:11436-11443 !$#title Nucleotide sequence and genetic characterization reveal six !1essential genes for the LIV-I and LS transport systems of !1Escherichia coli. !$#cross-references MUID:90307651; PMID:2195019 !$#accession A37074 !'##molecule_type DNA !'##residues 20-21,'T',23-30,'L',32-88,'A',90-386 ##label ADA !'##cross-references GB:J05516; NID:g146630; PIDN:AAA83881.1; !1PID:g146631 REFERENCE A03415 !$#authors Ovchinnikov, Y.A.; Aldanova, N.A.; Grinkevich, V.A.; !1Arzamazova, N.M.; Moroz, I.N. !$#journal FEBS Lett. (1977) 78:313-316 !$#title The primary structure of a Leu, Ile and Val (LIV)-binding !1protein from Escherichia coli. !$#cross-references MUID:77225636; PMID:328304 !$#accession A03415 !'##molecule_type protein !'##residues 43-304,'AD',307-383,'AD',386 ##label OVC !'##experimental_source strain K12 !'##note this protein was isolated from the periplasmic space of the !1cell REFERENCE S47666 !$#authors Plunkett, G. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S47679 !'##status preliminary !'##molecule_type DNA !'##residues 1-386 ##label PLU !'##cross-references EMBL:U00039; NID:g466582; PIDN:AAB18435.1; !1PID:g912457 !'##note this reported protein translation starts with a GTG codon; it !1has an extra 23-residue segment compare to the sequences in !1the other reports REFERENCE I55524 !$#authors Antonucci, T.K.; Landick, R.; Oxender, D.L. !$#journal J. Cell. Biochem. (1985) 29:209-216 !$#title The leucine binding proteins of Escherichia coli as models !1for studying the relationships between protein structure and !1function. !$#cross-references MUID:86086153; PMID:4077929 !$#accession I55524 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 20-21,'T',23-30,'L',32-88,'A',90-386 ##label RES !'##cross-references GB:M29377; NID:g146628; PIDN:AAA24075.1; !1PID:g146629 GENETICS !$#gene livJ !$#map_position 76 min FUNCTION !$#description specifically binds Leu, Ile, and Val and may be involved in !1their transmembrane transport CLASSIFICATION #superfamily LIV-binding protein FEATURE !$1-42 #domain (or 20-42) signal sequence #status predicted !8#label SIG\ !$43-386 #product leucine/isoleucine/valine-binding protein !8#status experimental #label MAT\ !$95-120 #disulfide_bonds #status experimental SUMMARY #length 386 #molecular-weight 41326 #checksum 8607 SEQUENCE /// ENTRY BLECL #type complete TITLE leucine-specific binding protein precursor - Escherichia coli (strain K-12) ALTERNATE_NAMES LS-binding protein precursor ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS E65142; B23576; C37074; S47677; I70187; I41096; I84545 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65142 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-369 ##label BLAT !'##cross-references GB:AE000421; GB:U00096; NID:g1789854; !1PIDN:AAC76483.1; PID:g1789867; UWGP:b3458 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A94677 !$#authors Landick, R.; Oxender, D.L. !$#journal J. Biol. Chem. (1985) 260:8257-8261 !$#title The complete nucleotide sequences of the Escherichia coli !1LIV-BP and LS-BP genes. Implications for the mechanism of !1high-affinity branched-chain amino acid transport. !$#cross-references MUID:85234531; PMID:3891753 !$#accession B23576 !'##molecule_type DNA !'##residues 1-42,'I',44-49,'E',51-125,'A',127-369 ##label LAN !'##cross-references GB:J05516; GB:K02178; GB:M10426; GB:M10427; !1GB:M13166; NID:g146630; PIDN:AAA83883.1; PID:g146632 REFERENCE A37074 !$#authors Adams, M.D.; Wagner, L.M.; Graddis, T.J.; Landick, R.; !1Antonucci, T.K.; Gibson, A.L.; Oxender, D.L. !$#journal J. Biol. Chem. (1990) 265:11436-11443 !$#title Nucleotide sequence and genetic characterization reveal six !1essential genes for the LIV-I and LS transport systems of !1Escherichia coli. !$#cross-references MUID:90307651; PMID:2195019 !$#accession C37074 !'##molecule_type DNA !'##residues 1-42,'I',44-49,'E',51-125,'A',127-369 ##label ADA !'##cross-references GB:J05516; NID:g146630; PIDN:AAA83883.1; !1PID:g146632 REFERENCE S47666 !$#authors Plunkett, G. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S47677 !'##molecule_type DNA !'##residues 1-369 ##label PLU !'##cross-references EMBL:U00039; NID:g466582; PIDN:AAB18433.1; !1PID:g466594 REFERENCE I55524 !$#authors Antonucci, T.K.; Landick, R.; Oxender, D.L. !$#journal J. Cell. Biochem. (1985) 29:209-216 !$#title The leucine binding proteins of Escherichia coli as models !1for studying the relationships between protein structure and !1function. !$#cross-references MUID:86086153; PMID:4077929 !$#accession I70187 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-42,'I',44-49,'E',51-125,'A',127-369 ##label RES !'##cross-references GB:M29378; NID:g146666; PIDN:AAA24090.1; !1PID:g146667 REFERENCE I41096 !$#authors Oxender, D.L.; Anderson, J.J.; Daniels, C.J.; Landick, R.; !1Gunsalus, R.P.; Zurawski, G.; Yanofsky, C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1980) 77:2005-2009 !$#title Amino-terminal sequence and processing of the precursor of !1the leucine-specific binding protein, and evidence for !1conformational differences between the precursor and the !1mature form. !$#cross-references MUID:80190173; PMID:6990419 !$#accession I41096 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-2,'A',4-36 ##label RE2 !'##cross-references EMBL:V00301; GB:J01644; NID:g41924; !1PIDN:CAA23579.1; PID:g41925 GENETICS !$#gene livK !$#map_position 76 min FUNCTION !$#description one of the two binding proteins (LIV-BP and LS-BP) that !1interact with a common set of membrane proteins to transport !1branched-chain amino acids into the cytoplasm; it is part of !1a high-affinity periplasmic binding protein-dependent !1transport system for amino acids CLASSIFICATION #superfamily LIV-binding protein KEYWORDS branched-chain amino acid transport FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-369 #product leucine-specific binding protein #status !8predicted #label MAT SUMMARY #length 369 #molecular-weight 39378 #checksum 6736 SEQUENCE /// ENTRY BLECGP #type complete TITLE glycine betaine/proline transport system binding protein proX precursor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 01-Mar-2002 ACCESSIONS JS0130; A92608; H65047; A33002 REFERENCE JS0128 !$#authors Gowrishankar, J. !$#journal J. Bacteriol. (1989) 171:1923-1931 !$#title Nucleotide sequence of the osmoregulatory proU operon of !1Escherichia coli. !$#cross-references MUID:89197759; PMID:2649479 !$#accession JS0130 !'##molecule_type DNA !'##residues 1-330 ##label GOW !'##cross-references GB:M24856; NID:g147372; PIDN:AAA24429.1; !1PID:g147375 REFERENCE A92608 !$#authors Barron, A.; Jung, J.U.; Villarejo, M. !$#journal J. Biol. Chem. (1987) 262:11841-11846 !$#title Purification and characterization of a glycine betaine !1binding protein from Escherichia coli. !$#cross-references MUID:87308168; PMID:3305496 !$#accession A92608 !'##molecule_type protein !'##residues 22-33 ##label BAR REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65047 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-330 ##label BLAT !'##cross-references GB:AE000352; GB:U00096; NID:g1789024; !1PIDN:AAC75726.1; PID:g1789034; UWGP:b2679 !'##experimental_source strain K-12, substrain MG1655 COMMENT This periplasmic protein is one of the three components of !1the transport system for glycine betaine and L-proline; it !1is the binding protein component. GENETICS !$#gene proX CLASSIFICATION #superfamily glycine betaine and proline transport system !1binding protein proX KEYWORDS glycine betaine transport; proline transport FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-330 #product glycine betaine and proline transport system !8binding protein proX #status experimental #label MAT SUMMARY #length 330 #molecular-weight 36022 #checksum 4408 SEQUENCE /// ENTRY ZPECPA #type complete TITLE penicillin-binding protein 1A - Escherichia coli (strain K-12) CONTAINS aminoacyltransferase (EC 2.3.2.-); glycosyltransferase (EC 2.4.-.-) ORGANISM #formal_name Escherichia coli DATE 28-May-1986 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS G65134; A03416; A22950 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65134 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-858 ##label BLAT !'##cross-references GB:AE000415; GB:U00096; NID:g1789798; !1PIDN:AAC76421.1; PID:g1789799; UWGP:b3396 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A91143 !$#authors Broome-Smith, J.K.; Edelman, A.; Yousif, S.; Spratt, B.G. !$#journal Eur. J. Biochem. (1985) 147:437-446 !$#title The nucleotide sequences of the ponA and ponB genes encoding !1penicillin-binding proteins 1A and 1B of Escherichia coli !1K12. !$#cross-references MUID:85127060; PMID:3882429 !$#accession A03416 !'##molecule_type DNA !'##residues 'M',10-858 ##label BRO !'##cross-references GB:X02164; NID:g42465; PIDN:CAA26100.1; PID:g581194 !'##experimental_source strain K12 REFERENCE A94031 !$#authors Keck, W.; Glauner, B.; Schwarz, U.; Broome-Smith, J.K.; !1Spratt, B.G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:1999-2003 !$#title Sequences of the active-site peptides of three of the !1high-Mr penicillin-binding proteins of Escherichia coli !1K-12. !$#cross-references MUID:85166260; PMID:3920658 !$#contents K12 !$#accession A22950 !'##molecule_type protein !'##residues 460-488 ##label KEC GENETICS !$#gene mrcA; ponA FUNCTION !$#description penicillin-binding proteins (PBP), located in the !1cytoplasmic membrane, catalyze the final stages in !1peptidoglycan synthesis; in E. coli, seven PBPs have been !1well characterized; PBP 1A is a major bifunctional protein !1that catalyzes the penicillin-sensitive transglycosylation !1(formation of linear glycan strands) and transpeptidation !1(cross-linking of the peptide subunits) CLASSIFICATION #superfamily penicillin-binding protein KEYWORDS aminoacyltransferase; antibiotic resistance; cell wall !1synthesis; glycosyltransferase FEATURE !$473 #active_site Ser (covalent penicillin-binding) !8#status predicted SUMMARY #length 858 #molecular-weight 94520 #checksum 2908 SEQUENCE /// ENTRY ZPECPB #type complete TITLE penicillin-binding protein 1B - Escherichia coli (strain K-12) ALTERNATE_NAMES peptidoglycan synthetase CONTAINS aminoacyltransferase (EC 2.3.2.-); glycosyltransferase (EC 2.4.-.-) ORGANISM #formal_name Escherichia coli DATE 28-May-1986 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS E64738; A03417; S45218; B22950 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64738 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-844 ##label BLAT !'##cross-references GB:AE000124; GB:U00096; NID:g1786339; !1PIDN:AAC73260.1; PID:g1786343; UWGP:b0149 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A91143 !$#authors Broome-Smith, J.K.; Edelman, A.; Yousif, S.; Spratt, B.G. !$#journal Eur. J. Biochem. (1985) 147:437-446 !$#title The nucleotide sequences of the ponA and ponB genes encoding !1penicillin-binding proteins 1A and 1B of Escherichia coli !1K12. !$#cross-references MUID:85127060; PMID:3882429 !$#accession A03417 !'##molecule_type DNA !'##residues 1-102,'A',104-844 ##label BRO !'##cross-references GB:X02163; NID:g42467; PIDN:CAA26098.1; PID:g42468 !'##experimental_source strain K12, large isozyme REFERENCE S45181 !$#authors Fujita, N. !$#submission submitted to the EMBL Data Library, January 1994 !$#accession S45218 !'##status preliminary !'##molecule_type DNA !'##residues 1-102,'A',104-754,'TP',755-844 ##label FUJ !'##cross-references EMBL:D26562; NID:g473770; PIDN:BAA05597.1; !1PID:g473808 !'##experimental_source strain K-12, substrain W3110 REFERENCE A94031 !$#authors Keck, W.; Glauner, B.; Schwarz, U.; Broome-Smith, J.K.; !1Spratt, B.G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:1999-2003 !$#title Sequences of the active-site peptides of three of the !1high-Mr penicillin-binding proteins of Escherichia coli !1K-12. !$#cross-references MUID:85166260; PMID:3920658 !$#accession B22950 !'##molecule_type protein !'##residues 497-525 ##label KEC !'##experimental_source K12 COMMENT Penicillin-binding proteins (PBP), located in the !1cytoplasmic membrane, catalyze the final stages in !1peptidoglycan synthesis. In E. coli, seven PBPs have been !1well characterized. PBP 1B is a major bifunctional protein !1that catalyzes the penicillin-insensitive transglycosylation !1(formation of linear glycan strands) and the !1penicillin-sensitive transpeptidation (cross-linking of the !1peptide subunits). COMMENT Using alternative initiation codons in the same reading !1frame, the gene translates into two isozymes having !1different amino ends. GENETICS !$#gene mrcB; ponB FUNCTION TGL !$#description catalyzes transglycosylation to form linear glycan strands !$#pathway peptidoglycan synthesis !$#note this reaction is penicillin-insensitive FUNCTION TPT !$#description catalyzes transpeptidation to cross-link peptide subunits !$#pathway peptidoglycan synthesis !$#note this reaction is penicillin-sensitive CLASSIFICATION #superfamily penicillin-binding protein 1B KEYWORDS alternative initiators; aminoacyltransferase; antibiotic !1resistance; cell wall synthesis; glycosyltransferase; !1multifunctional enzyme FEATURE !$1-844 #product penicillin-binding protein 1B, long form !8#status predicted #label LRG\ !$46-844 #product penicillin-binding protein 1B, short form !8#status predicted #label SML\ !$510 #active_site Ser (covalent penicillin-binding) !8#status predicted SUMMARY #length 844 #molecular-weight 94292 #checksum 9798 SEQUENCE /// ENTRY ZPECP3 #type complete TITLE penicillin-binding protein 3 precursor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 01-Mar-2002 ACCESSIONS A93123; A94446; S40594; B45274; B45278; S10690; D64730; !1A03419; A23345 REFERENCE A93123 !$#authors Nakamura, M.; Maruyama, I.N.; Soma, M.; Kato, J.; Suzuki, !1H.; Horota, Y. !$#journal Mol. Gen. Genet. (1983) 191:1-9 !$#title On the process of cellular division in Escherichia coli: !1nucleotide sequence of the gene for penicillin-binding !1protein 3. !$#cross-references MUID:83296957; PMID:6350821 !$#accession A93123 !'##molecule_type DNA !'##residues 1-588 ##label NAK !'##cross-references GB:X55034; GB:M10429; NID:g40841; PIDN:CAA38861.1; !1PID:g40852 REFERENCE A94446 !$#authors Maruyama, I.N.; Yamamoto, A.; Maruyama, T.; Hirota, Y. !$#book The Target of Penicillin, Hakenbeck, R., Holtje, J.V., and !1Labischinski, H., eds., pp.393-402, Walter de Gruyter, !1Berlin and New York, 1983 !$#title The fine architecture and function of the gene coding for !1PBP-3 of Escherichia coli. !$#accession A94446 !'##molecule_type DNA !'##residues 1-328,'I',330-588 ##label MAR REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40594 !'##status preliminary !'##molecule_type DNA !'##residues 1-588 ##label YUR !'##cross-references EMBL:D10483; NID:g216434; PIDN:BAA01349.1; !1PID:g216498 REFERENCE A45274 !$#authors Guzman, L.M.; Barondess, J.J.; Beckwith, J. !$#journal J. Bacteriol. (1992) 174:7716-7728 !$#title FtsL, an essential cytoplasmic membrane protein involved in !1cell division in Escherichia coli. !$#cross-references MUID:93077455; PMID:1332942 !$#accession B45274 !'##status preliminary !'##molecule_type DNA !'##residues 1-20 ##label GUZ !'##note sequence extracted from NCBI backbone REFERENCE A45278 !$#authors Ueki, M.; Wachi, M.; Jung, H.K.; Ishino, F.; Matsuhashi, M. !$#journal J. Bacteriol. (1992) 174:7841-7843 !$#title Escherichia coli mraR gene involved in cell growth and !1division. !$#cross-references MUID:93077472; PMID:1447153 !$#accession B45278 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-71 ##label UEK !'##cross-references GB:S49802; NID:g260729; PIDN:AAB24312.1; !1PID:g260731 !'##note sequence extracted from NCBI backbone (NCBIP:119214) REFERENCE S10690 !$#authors Michaud, C.; Parquet, C.; Flouret, B.; Blanot, D.; van !1Heijenoort, J. !$#journal Biochem. J. (1990) 269:277-278 !$#title Revised interpretation of the sequence containing the murE !1gene encoding the UDP-N-acetylmuramyl-tripeptide synthetase !1of Escherichia coli. !$#cross-references MUID:90328986; PMID:2198024 !$#accession S10690 !'##molecule_type DNA !'##residues 550-588 ##label MIC !'##cross-references GB:X55814; NID:g296013; PIDN:CAA39333.1; !1PID:g296014 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64730 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-588 ##label BLAT !'##cross-references GB:AE000118; GB:U00096; NID:g1786262; !1PIDN:AAC73195.1; PID:g1786272; UWGP:b0084 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ftsI; pbpB !$#map_position 2 min FUNCTION !$#pathway peptidoglycan biosynthesis CLASSIFICATION #superfamily penicillin-binding protein 3 KEYWORDS antibiotic resistance; cell division; cell wall; inner !1membrane; peptidoglycan biosynthesis; transmembrane protein FEATURE !$1-40 #domain (or 1-43 or 1-49) signal sequence #status !8predicted #label SIG\ !$24-40 #domain transmembrane #status predicted #label TMM\ !$41-588 #product (or 44-588 or 50-588) penicillin-binding !8protein 3 #status predicted #label MAT\ !$307 #active_site Ser (covalent penicillin-binding) !8#status predicted SUMMARY #length 588 #molecular-weight 63877 #checksum 899 SEQUENCE /// ENTRY ZPECP2 #type complete TITLE penicillin-binding protein 2 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 01-Mar-2002 ACCESSIONS C24995; A32257; A64798 REFERENCE A91176 !$#authors Asoh, S.; Matsuzawa, H.; Ishino, F.; Strominger, J.L.; !1Matsuhashi, M.; Ohta, T. !$#journal Eur. J. Biochem. (1986) 160:231-238 !$#title Nucleotide sequence of the pbpA gene and characteristics of !1the deduced amino acid sequence of penicillin-binding !1protein 2 of Escherichia coli K12. !$#cross-references MUID:87030266; PMID:3533535 !$#accession C24995 !'##molecule_type DNA !'##residues 1-633 ##label ASO !'##cross-references GB:X04516; GB:D00001; GB:N00001; NID:g42313; !1PIDN:CAA28201.1; PID:g42316 REFERENCE A32257 !$#authors Matsuzawa, H.; Asoh, S.; Kunai, K.; Muraiso, K.; Takasuga, !1A.; Ohta, T. !$#journal J. Bacteriol. (1989) 171:558-560 !$#title Nucleotide sequence of the rodA gene, responsible for the !1rod shape of Escherichia coli: rodA and the pbpA gene, !1encoding penicillin-binding protein 2, constitute the rodA !1operon. !$#cross-references MUID:89123070; PMID:2644207 !$#accession A32257 !'##status preliminary !'##molecule_type DNA !'##residues 606-633 ##label MAT !'##cross-references GB:M22857; NID:g147693; PIDN:AAA24570.1; !1PID:g147694 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64798 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-633 ##label BLAT !'##cross-references GB:AE000168; GB:U00096; NID:g1786849; !1PIDN:AAC73736.1; PID:g1786854; UWGP:b0635 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene mrdA; pbpA !$#map_position 15 min FUNCTION !$#description penicillin-binding proteins (PBP), located in the !1cytoplasmic membrane, catalyze the final stages in !1peptidoglycan synthesis; in E. coli, seven PBPs have been !1well characterized; PBP2 is responsible for the !1determination of the rod shape of the cell CLASSIFICATION #superfamily penicillin-binding protein 3 KEYWORDS antibiotic resistance; peptidoglycan biosynthesis SUMMARY #length 633 #molecular-weight 70856 #checksum 9867 SEQUENCE /// ENTRY ZPECP5 #type complete TITLE serine-type D-Ala-D-Ala carboxypeptidase (EC 3.4.16.4) dacA precursor - Escherichia coli (strain K-12) ALTERNATE_NAMES DD-carboxypeptidase; penicillin-binding protein 5 ORGANISM #formal_name Escherichia coli DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 19-Jul-2002 ACCESSIONS A28536; A91319; D28387; F64797; A03420; A94463 REFERENCE A93682 !$#authors Broome-Smith, J.K.; Ioannidis, I.; Edelman, A.; Spratt, B.G. !$#journal Nucleic Acids Res. (1988) 16:1617 !$#title Nucleotide sequences of the penicillin-binding protein 5 and !16 genes of Escherichia coli. !$#cross-references MUID:88157719; PMID:3279397 !$#accession A28536 !'##molecule_type DNA !'##residues 1-403 ##label BRO !'##cross-references GB:X06479; GB:X00273; NID:g41211; PIDN:CAA29774.1; !1PID:g41212 REFERENCE A91319 !$#authors Broome-Smith, J.; Spratt, B.G. !$#journal FEBS Lett. (1984) 165:185-189 !$#title An amino acid substitution that blocks the deacylation step !1in the enzyme mechanism of penicillin-binding protein 5 of !1Escherichia coli. !$#cross-references MUID:84108878; PMID:6319180 !$#accession A91319 !'##molecule_type DNA !'##residues 108-133,'D',135-336 ##label BR2 !'##experimental_source mutant dacA11191 !'##note this mutation, caused by a single nucleotide substitution, !1alters both the acylation and deacylation steps of the !1enzyme mechanism; the overall effect is that the protein is !1capable of binding penicillin but is unable to catalyze the !1release of the bound penicilloyl moiety REFERENCE A91853 !$#authors Takase, I.; Ishino, F.; Wachi, M.; Kamata, H.; Doi, M.; !1Asoh, S.; Matsuzawa, H.; Ohta, T.; Matsuhashi, M. !$#journal J. Bacteriol. (1987) 169:5692-5699 !$#title Genes encoding two lipoproteins in the leuS-dacA region of !1the Escherichia coli chromosome. !$#cross-references MUID:88058785; PMID:3316191 !$#accession D28387 !'##molecule_type DNA !'##residues 1-39 ##label TAK REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64797 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-403 ##label BLAT !'##cross-references GB:AE000168; GB:U00096; NID:g1786849; !1PIDN:AAC73733.1; PID:g1786851; UWGP:b0632 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene dacA; pfv !$#map_position 15 min FUNCTION !$#description penicillin-binding proteins (PBP), located in the !1cytoplasmic membrane, catalyze the final stages in !1peptidoglycan synthesis; in E. coli, seven PBPs have been !1well characterized; PBP5, which is not essential for !1bacterial growth, is a major D-alanine carboxypeptidase; !1however, the precise function of this enzyme in !1peptidoglycan synthesis is not known CLASSIFICATION #superfamily penicillin-binding protein 5 KEYWORDS cell wall synthesis; hydrolase; membrane protein; !1peptidoglycan biosynthesis; serine carboxypeptidase FEATURE !$1-29 #domain signal sequence #status predicted #label SIG\ !$30-403 #product serine-type D-Ala-D-Ala carboxypeptidase !8dacA #status predicted #label MAT SUMMARY #length 403 #molecular-weight 44444 #checksum 7496 SEQUENCE /// ENTRY JN0801 #type complete TITLE serine-type D-Ala-D-Ala carboxypeptidase (EC 3.4.16.4) precursor - Bacillus stearothermophilus ORGANISM #formal_name Bacillus stearothermophilus DATE 03-May-1994 #sequence_revision 22-Jul-1994 #text_change 16-Jul-1999 ACCESSIONS JN0801; A61335; A16374; S26433 REFERENCE JN0801 !$#authors Despreaux, C.W.; Manning, R.F. !$#journal Gene (1993) 131:35-41 !$#title The dacA gene of Bacillus stearothermophilus coding for !1D-alanine carboxypeptidase: Cloning, structure and !1expression in Escherichia coli and Pichia pastoris. !$#cross-references MUID:93380671; PMID:8370539 !$#accession JN0801 !'##molecule_type DNA !'##residues 1-452 ##label DES !'##cross-references EMBL:X68587; NID:g49167; PIDN:CAA48577.1; !1PID:g580849 REFERENCE A61335 !$#authors Yocum, R.R.; Waxman, D.J.; Rasmussen, J.R.; Strominger, J.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1979) 76:2730-2734 !$#title Mechanism of penicillin action: penicillin and substrate !1bind covalently to the same active site serine in two !1bacterial D-alanine carboxypeptidases. !$#cross-references MUID:79223865; PMID:111240 !$#accession A61335 !'##molecule_type protein !'##residues 31-50,'K',52-70 ##label YOC REFERENCE A92307 !$#authors Waxman, D.J.; Strominger, J.L. !$#journal J. Biol. Chem. (1981) 256:2067-2077 !$#title Primary structure of the COOH-terminal membranous segment of !1a penicillin-sensitive enzyme purified from two Bacilli. !$#cross-references MUID:81117303; PMID:6780559 !$#accession A16374 !'##molecule_type protein !'##residues 29-30;425-452 ##label WAX COMMENT This enzyme removes the D-alanyl termini from cell wall !1precursors in vitro, limiting their ability to form !1cross-links, and catalyzes O-acyl transferase reactions. GENETICS !$#gene dacA !$#start_codon GTG CLASSIFICATION #superfamily penicillin-binding protein 5 KEYWORDS cell wall synthesis; hydrolase; serine carboxypeptidase FEATURE !$1-30 #domain signal sequence #status predicted #label SIG\ !$31-452 #product D-alanine carboxypeptidase #status !8experimental #label MAT\ !$429-452 #region membrane attachment\ !$66 #active_site Ser #status experimental SUMMARY #length 452 #molecular-weight 51002 #checksum 4942 SEQUENCE /// ENTRY JGECPP #type complete TITLE sodium/proline symporter - Escherichia coli (strain K-12) ALTERNATE_NAMES proline carrier protein; proline permease; proline transport protein ORGANISM #formal_name Escherichia coli DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 01-Mar-2002 ACCESSIONS A30258; I54981; E64843 REFERENCE A30258 !$#authors Nakao, T.; Yamato, I.; Anraku, Y. !$#journal Mol. Gen. Genet. (1987) 208:70-75 !$#title Nucleotide sequence of putP, the proline carrier gene of !1Escherichia coli K12. !$#cross-references MUID:87286425; PMID:3302614 !$#accession A30258 !'##molecule_type DNA !'##residues 1-502 ##label NAK !'##cross-references GB:X05653; GB:X06415; NID:g42599; PIDN:CAA29143.1; !1PID:g42602 REFERENCE I54981 !$#authors Nelson, K.; Selander, R.K. !$#journal J. Bacteriol. (1992) 174:6886-6895 !$#title Evolutionary genetics of proline permease gene (putP) and !1the control region of the proline utilization operon in !1populations of Salmonella and Escherichia coli. !$#cross-references MUID:93015751; PMID:1400239 !$#accession I54981 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-297,'E',299-301,'V',303-364,'Q',366-489 ##label RES !'##cross-references GB:L01132; NID:g147434; PIDN:AAA24461.1; !1PID:g147435 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64843 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-502 ##label BLAT !'##cross-references GB:AE000203; GB:U00096; NID:g1787248; !1PIDN:AAC74100.1; PID:g1787251; UWGP:b1015 !'##experimental_source strain K-12, substrain MG1655 COMMENT Amino acid substition analysis indicates that the N-terminal !1part of PutP is important for ion binding. GENETICS !$#gene putP !$#map_position 23 min FUNCTION !$#description responsible for the sodium-dependent transport of proline !1into the cell CLASSIFICATION #superfamily proline carrier protein KEYWORDS proline transport; sodium transport; symport system; !1transmembrane protein FEATURE !$2-26 #domain transmembrane #status predicted #label TM01\ !$46-73 #domain transmembrane #status predicted #label TM02\ !$128-147 #domain transmembrane #status predicted #label TM03\ !$163-185 #domain transmembrane #status predicted #label TM04\ !$191-210 #domain transmembrane #status predicted #label TM05\ !$233-255 #domain transmembrane #status predicted #label TM06\ !$274-297 #domain transmembrane #status predicted #label TM07\ !$317-353 #domain transmembrane #status predicted #label TM08\ !$372-392 #domain transmembrane #status predicted #label TM09\ !$397-423 #domain transmembrane #status predicted #label TM10\ !$428-444 #domain transmembrane #status predicted #label TM11\ !$455-473 #domain transmembrane #status predicted #label TM12\ !$55 #binding_site sodium (Asp) #status predicted\ !$344 #active_site Cys #status predicted SUMMARY #length 502 #molecular-weight 54344 #checksum 3370 SEQUENCE /// ENTRY BDEC #type complete TITLE melibiose carrier protein - Escherichia coli (strain K-12) ALTERNATE_NAMES thiomethylgalactoside permease II ORGANISM #formal_name Escherichia coli DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 01-Mar-2002 ACCESSIONS A03421; S56349; G65221 REFERENCE A03421 !$#authors Yazyu, H.; Shiota-Niiya, S.; Shimamoto, T.; Kanazawa, H.; !1Futai, M.; Tsuchiya, T. !$#journal J. Biol. Chem. (1984) 259:4320-4326 !$#title Nucleotide sequence of the melB gene and characteristics of !1deduced amino acid sequence of the melibiose carrier in !1Escherichia coli. !$#cross-references MUID:84162133; PMID:6323466 !$#accession A03421 !'##molecule_type DNA !'##residues 1-469 ##label YAZ !'##cross-references GB:K01991; NID:g146802; PIDN:AAA24148.1; !1PID:g146804 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56349 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-469 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97020.1; !1PID:g536965 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65221 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-469 ##label BLAT !'##cross-references GB:AE000484; GB:U00096; NID:g2367352; !1PIDN:AAC77081.1; PID:g1790561; UWGP:b4120 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene melB !$#map_position 93 min FUNCTION !$#description is the only protein responsible for melibiose transport; !1capable of using hydrogen, sodium, and lithium cations as !1coupling cations for cotransport, depending on the !1particular sugar transported CLASSIFICATION #superfamily melibiose carrier protein KEYWORDS membrane protein; sugar transport SUMMARY #length 469 #molecular-weight 52217 #checksum 5322 SEQUENCE /// ENTRY MMBY61 #type complete TITLE maltose transport protein MAL61 - yeast (Saccharomyces cerevisiae) (strain carlsbergensis) ALTERNATE_NAMES maltose permease MAL61; maltose transport protein MAL6T ORGANISM #formal_name Saccharomyces cerevisiae #variety strain carlsbergensis DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Jul-1999 ACCESSIONS S07686; JU0063 REFERENCE S07686 !$#authors Cheng, Q.; Michels, C.A. !$#journal Genetics (1989) 123:477-484 !$#title The maltose permease encoded by the MAL61 gene of !1Saccharomyces cerevisiae exhibits both sequence and !1structural homology to other sugar transporters. !$#cross-references MUID:90092960; PMID:2689282 !$#accession S07686 !'##molecule_type DNA !'##residues 1-614 ##label CHE !'##cross-references GB:X17391; GB:X59049; NID:g3882; PIDN:CAA35254.1; !1PID:g3883 REFERENCE JU0063 !$#authors Yao, B.; Sollitti, P.; Marmur, J. !$#journal Gene (1989) 79:189-197 !$#title Primary structure of the maltose-permease-encoding gene of !1Saccharomyces carlsbergensis. !$#cross-references MUID:90006748; PMID:2507395 !$#accession JU0063 !'##molecule_type DNA !'##residues 1-614 ##label YAO !'##experimental_source Saccharomyces carlsbergensis !'##note the source is designated as Saccharomyces carlsbergensis GENETICS !$#gene MAL61; MAL6T !$#map_position 8 CLASSIFICATION #superfamily maltose transport protein MAL61 KEYWORDS sugar transport; transmembrane protein FEATURE !$104-124 #domain transmembrane #status predicted #label TM01\ !$151-170 #domain transmembrane #status predicted #label TM02\ !$179-198 #domain transmembrane #status predicted #label TM03\ !$201-223 #domain transmembrane #status predicted #label TM04\ !$236-257 #domain transmembrane #status predicted #label TM05\ !$273-293 #domain transmembrane #status predicted #label TM06\ !$365-388 #domain transmembrane #status predicted #label TM07\ !$399-419 #domain transmembrane #status predicted #label TM08\ !$428-448 #domain transmembrane #status predicted #label TM09\ !$459-481 #domain transmembrane #status predicted #label TM10\ !$500-516 #domain transmembrane #status predicted #label TM11\ !$528-544 #domain transmembrane #status predicted #label TM12 SUMMARY #length 614 #molecular-weight 68225 #checksum 2577 SEQUENCE /// ENTRY MMBYH2 #type complete TITLE glucose transport protein HXT2 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES petite-specific protein rho-11; protein YM8270.15; protein YMR011w ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 21-Jul-2000 ACCESSIONS A36380; S53042; A47586; S12200 REFERENCE A36380 !$#authors Kruckeberg, A.L.; Bisson, L.F. !$#journal Mol. Cell. Biol. (1990) 10:5903-5913 !$#title The HXT2 gene of Saccharomyces cerevisiae is required for !1high-affinity glucose transport. !$#cross-references MUID:91042520; PMID:2233722 !$#accession A36380 !'##molecule_type DNA !'##residues 1-541 ##label KRU !'##cross-references EMBL:M33270; NID:g171742; PIDN:AAA34701.1; !1PID:g171743 REFERENCE S53028 !$#authors Devlin, K.; Churcher, C.M. !$#submission submitted to the EMBL Data Library, March 1995 !$#accession S53042 !'##molecule_type DNA !'##residues 1-541 ##label DEV !'##cross-references EMBL:Z48613; NID:g728645; PIDN:CAA88528.1; !1PID:g728660; GSPDB:GN00013; MIPS:YMR011w !'##experimental_source strain AB972 REFERENCE A47586 !$#authors Parikh, V.S.; Morgan, M.M.; Scott, R.; Clements, L.S.; !1Butow, R.A. !$#journal Science (1987) 235:576-580 !$#title The mitochondrial genotype can influence nuclear gene !1expression in yeast. !$#cross-references MUID:87120291; PMID:3027892 !$#accession A47586 !'##molecule_type mRNA !'##residues 'DTT',9-10,'KITK',15,'MAMEAE',22,'PNRH',27,'RRPNLSTVY',37, !1'ATKVIG',44,'VDYTKR',54,'SLED',59,'SYDAL';303,'A',305-307, !1'H',310-322,'H',324,'TH',333,'CTLLSICTTIHAS',347,'RSHSSC' !1##label PAR !'##cross-references GB:M15166; GB:M15167 !'##note the authors translated the codon TGT for residue 353 as Val GENETICS !$#gene SGD:HXT2; MIPS:YMR011w !'##cross-references SGD:S0004613; MIPS:YMR011w !$#map_position 13R CLASSIFICATION #superfamily maltose transport protein MAL61 KEYWORDS glycoprotein; phosphoprotein; sugar transport; transmembrane !1protein FEATURE !$50-70 #domain transmembrane #status predicted #label TM01\ !$106-125 #domain transmembrane #status predicted #label TM02\ !$135-153 #domain transmembrane #status predicted #label TM03\ !$166-183 #domain transmembrane #status predicted #label TM04\ !$195-215 #domain transmembrane #status predicted #label TM05\ !$228-248 #domain transmembrane #status predicted #label TM06\ !$317-337 #domain transmembrane #status predicted #label TM07\ !$351-372 #domain transmembrane #status predicted #label TM08\ !$380-400 #domain transmembrane #status predicted #label TM09\ !$420-440 #domain transmembrane #status predicted #label TM10\ !$456-477 #domain transmembrane #status predicted #label TM11\ !$485-505 #domain transmembrane #status predicted #label TM12\ !$82 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 541 #molecular-weight 59840 #checksum 5167 SEQUENCE /// ENTRY A43344 #type complete TITLE synaptic vesicle protein SV2 - rat ALTERNATE_NAMES transporter-like protein p87 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Sep-2000 ACCESSIONS A43344; A43267; A58948 REFERENCE A43344 !$#authors Feany, M.B.; Lee, S.; Edwards, R.H.; Buckley, K.M. !$#journal Cell (1992) 70:861-867 !$#title The synaptic vesicle protein SV2 is a novel type of !1transmembrane transporter. !$#cross-references MUID:92386605; PMID:1355409 !$#accession A43344 !'##molecule_type mRNA !'##residues 1-742 ##label FEA !'##cross-references GB:L01788; NID:g207090 !'##experimental_source pheochromocytoma cell line PC12 !'##note sequence extracted from NCBI backbone (NCBIN:112840, !1NCBIP:112842) !'##note this ORF is not annotated in GenBank entry RATSV2A, release !1109.0 REFERENCE A43267 !$#authors Bajjalieh, S.M.; Peterson, K.; Shinghal, R.; Scheller, R.H. !$#journal Science (1992) 257:1271-1273 !$#title SV2, a brain synaptic vesicle protein homologous to !1bacterial transporters. !$#cross-references MUID:92390722; PMID:1519064 !$#accession A43267 !'##molecule_type mRNA !'##residues 1-339,'F',341-742 ##label BAJ !'##cross-references GB:L05435; NID:g207091; PIDN:AAA42188.1; !1PID:g207092 !'##experimental_source brain !'##note sequence extracted from NCBI backbone (NCBIP:112489) REFERENCE S27263 !$#authors Gingrich, J.A.; Andersen, P.H.; Tiberi, M.; El Mestikawy, !1S.; Jorgensen, P.N.; Fremeau Jr., R.T.; Caron, M.G. !$#journal FEBS Lett. (1992) 312:115-122 !$#title Identification, characterization, and molecular cloning of a !1novel transporter-like protein localized to the central !1nervous system. !$#cross-references MUID:93050176; PMID:1426240 !$#accession A58948 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-120,'E',122-249,'W',251-684,'P',686-742 ##label GIN !'##note only differences from the bovine translation are shown in Fig. !12 CLASSIFICATION #superfamily synaptic vesicle protein SV2 KEYWORDS transport protein SUMMARY #length 742 #molecular-weight 82661 #checksum 6646 SEQUENCE /// ENTRY MMECMG #type complete TITLE maltose transport inner membrane protein malG - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 01-Mar-2002 ACCESSIONS A24361; S11908; G65210 REFERENCE A24361 !$#authors Dassa, E.; Hofnung, M. !$#journal EMBO J. (1985) 4:2287-2293 !$#title Sequence of gene malG in E. coli K12: homologies between !1integral membrane components from binding protein-dependent !1transport systems. !$#cross-references MUID:86081738; PMID:3000770 !$#accession A24361 !'##molecule_type DNA !'##residues 1-296 ##label DAS !'##cross-references GB:X02871; NID:g41949; PIDN:CAA26628.1; PID:g41951 !'##experimental_source strain K12 REFERENCE S11908 !$#authors Dassa, E. !$#journal Mol. Gen. Genet. (1990) 222:33-36 !$#title Cellular localization of the MalG protein from the maltose !1transport system in Escherichia coli K12. !$#cross-references MUID:91042423; PMID:2233678 !$#accession S11908 !'##status preliminary !'##molecule_type DNA !'##residues 190-209 ##label DA2 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65210 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-296 ##label BLAT !'##cross-references GB:AE000476; GB:U00096; NID:g1790456; !1PIDN:AAC77002.1; PID:g1790464; UWGP:b4032 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene malG !$#map_position 92 min FUNCTION !$#description one of the five proteins essential to the active binding !1protein-dependent transport system for maltose and !1maltodextrin; an inner membrane protein associated with, and !1distantly related to, the malK protein CLASSIFICATION #superfamily maltose transport protein malG KEYWORDS maltodextrin transport; maltose transport; membrane protein SUMMARY #length 296 #molecular-weight 32225 #checksum 2003 SEQUENCE /// ENTRY QRECST #type complete TITLE sulfate/thiosulfate transport protein cysT - Escherichia coli (strain K-12) ALTERNATE_NAMES sulfate transport system permease protein cysT ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 01-Mar-2002 ACCESSIONS A35402; G65016; B35403 REFERENCE A35402 !$#authors Sirko, A.; Hryniewicz, M.; Hulanicka, D.; Boeck, A. !$#journal J. Bacteriol. (1990) 172:3351-3357 !$#title Sulfate and thiosulfate transport in Escherichia coli K-12: !1nucleotide sequence and expression of the cysTWAM gene !1cluster. !$#cross-references MUID:90264334; PMID:2188958 !$#accession A35402 !'##molecule_type DNA !'##residues 1-277 ##label SIR !'##cross-references GB:M32101; GB:M38050; NID:g145657; PIDN:AAA23637.1; !1PID:g145659 !'##experimental_source strain K12 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65016 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-277 ##label BLAT !'##cross-references GB:AE000330; GB:U00096; NID:g1788763; !1PIDN:AAC75477.1; PID:g1788764; UWGP:b2424 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A35403 !$#authors Hryniewicz, M.; Sirko, A.; Palucha, A.; Boeck, A.; !1Hulanicka, D. !$#journal J. Bacteriol. (1990) 172:3358-3366 !$#title Sulfate and thiosulfate transport in Escherichia coli K-12: !1identification of a gene encoding a novel protein involved !1in thiosulfate binding. !$#cross-references MUID:90264335; PMID:2188959 !$#accession B35403 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-126,'F',128-133 ##label HRY COMMENT This is one of the membrane-associated components of the !1binding protein-dependent transport system for sulfates and !1thiosulfates. GENETICS !$#gene cysU; cysT !$#map_position 52 min CLASSIFICATION #superfamily maltose transport protein malG KEYWORDS binding protein-dependent transport system; inner membrane; !1membrane protein; sulfate transport; thiosulfate transport SUMMARY #length 277 #molecular-weight 30291 #checksum 1625 SEQUENCE /// ENTRY QRECSW #type complete TITLE sulfate/thiosulfate transport protein cysW - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS F65016; B35402 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65016 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-149 ##label BLAT !'##cross-references GB:AE000329; GB:U00096; NID:g2367137; !1PIDN:AAC75476.1; PID:g1788762; UWGP:b2423 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A35402 !$#authors Sirko, A.; Hryniewicz, M.; Hulanicka, D.; Boeck, A. !$#journal J. Bacteriol. (1990) 172:3351-3357 !$#title Sulfate and thiosulfate transport in Escherichia coli K-12: !1nucleotide sequence and expression of the cysTWAM gene !1cluster. !$#cross-references MUID:90264334; PMID:2188958 !$#accession B35402 !'##molecule_type DNA !'##residues !1'MAEVTQLKRYDARPINWGKWFLIGIGMLVSAFILLVPMIYIFVQAFSKGLMPVLQNLAD !1PDMLHAIWLTVMIALIAVPVNLVFGILLAWLVTRFNFPGRQLLLTLLDIPFAVSPVVAGL !1VYLLFYGSNGPLGGWLDEHNLQI',1-149 ##label SIR !'##cross-references GB:M32101; GB:M38050; NID:g145657; PIDN:AAA23638.1; !1PID:g145660 !'##experimental_source strain K12 COMMENT This is one of the membrane-associated components of the !1binding protein-dependent transport system for sulfates and !1thiosulfates. GENETICS !$#gene cysW !$#map_position 52 min CLASSIFICATION #superfamily maltose transport protein malG KEYWORDS binding protein-dependent transport system; inner membrane; !1sulfate transport; thiosulfate transport SUMMARY #length 149 #molecular-weight 16675 #checksum 394 SEQUENCE /// ENTRY BVECHJ #type complete TITLE molybdenum transport protein modB - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS D64812; A26871 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64812 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-229 ##label BLAT !'##cross-references GB:AE000179; GB:U00096; NID:g1786978; !1PIDN:AAC73851.1; PID:g1786980; UWGP:b0764 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A26871 !$#authors Johann, S.; Hinton, S.M. !$#journal J. Bacteriol. (1987) 169:1911-1916 !$#title Cloning and nucleotide sequence of the chlD locus. !$#cross-references MUID:87194564; PMID:3553151 !$#accession A26871 !'##molecule_type DNA !'##residues 30-39,'S',41-229 ##label JOH !'##cross-references EMBL:X07875 !'##experimental_source strain K12 COMMENT This protein is one of the components of the binding !1protein-dependent transport system for molybdenum. GENETICS !$#gene modB; chlJ !$#map_position 17 min FUNCTION !$#description molybdenum transport CLASSIFICATION #superfamily maltose transport protein malG KEYWORDS inner membrane; molybdenum transport; transmembrane protein FEATURE !$21-37 #domain transmembrane #status predicted #label TM1\ !$53-69 #domain transmembrane #status predicted #label TM2\ !$95-111 #domain transmembrane #status predicted #label TM3\ !$142-158 #domain transmembrane #status predicted #label TM4\ !$199-215 #domain transmembrane #status predicted #label TM5 SUMMARY #length 229 #molecular-weight 24938 #checksum 1412 SEQUENCE /// ENTRY MMECUE #type complete TITLE sn-Glycerol-3-phosphate transport system permease protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 01-Mar-2002 ACCESSIONS S03782; S47670; F65141 REFERENCE S03780 !$#authors Overduin, P.; Boos, W.; Tommassen, J. !$#journal Mol. Microbiol. (1988) 2:767-775 !$#title Nucleotide sequence of the ugp genes of Escherichia coli !1K-12: homology to the maltose system. !$#cross-references MUID:89096498; PMID:3062310 !$#accession S03782 !'##molecule_type DNA !'##residues 1-281 ##label OVE !'##cross-references EMBL:X13141; NID:g43243; PIDN:CAA31533.1; !1PID:g43248 REFERENCE S47666 !$#authors Plunkett, G. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S47670 !'##molecule_type DNA !'##residues 1-281 ##label PLU !'##cross-references EMBL:U00039; NID:g466582; PIDN:AAB18426.1; !1PID:g466587 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65141 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-281 ##label BLAT !'##cross-references GB:AE000421; GB:U00096; NID:g1789854; !1PIDN:AAC76476.1; PID:g1789860; UWGP:b3451 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ugpE !$#map_position 76 min FUNCTION !$#description one of the membrane protein components of a phosphate !1limitation-induced transport system for glycerol-3-phosphate !1and glycerophosphoryl diesters CLASSIFICATION #superfamily maltose transport protein malG KEYWORDS binding protein-dependent transport system; !1glycerol-3-phosphate transport; membrane protein SUMMARY #length 281 #molecular-weight 31499 #checksum 5393 SEQUENCE /// ENTRY MMAGCG #type complete TITLE membrane protein lacG - Agrobacterium radiobacter ORGANISM #formal_name Agrobacterium radiobacter DATE 31-Dec-1992 #sequence_revision 30-Sep-1993 #text_change 16-Jul-1999 ACCESSIONS S25249; S22741 REFERENCE S25247 !$#authors Williams, S.G.; Greenwood, J.A.; Jones, C.W. !$#journal Mol. Microbiol. (1992) 6:1755-1768 !$#title Molecular analysis of the lac operon encoding the !1binding-protein-dependent lactose transport system and !1beta-galactosidase in Agrobacterium radiobacter. !$#cross-references MUID:92334152; PMID:1630315 !$#accession S25249 !'##molecule_type DNA !'##residues 1-273 ##label WIL !'##cross-references EMBL:X66596; NID:g38967; PIDN:CAA47163.1; !1PID:g38970 GENETICS !$#gene lacG CLASSIFICATION #superfamily maltose transport protein malG KEYWORDS binding protein-dependent transport system; lactose !1transport; membrane protein SUMMARY #length 273 #molecular-weight 30651 #checksum 9455 SEQUENCE /// ENTRY MMECHP #type complete TITLE hexose phosphate transport protein uhpT - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 01-Mar-2002 ACCESSIONS A30395; H41853; C65168; Q00500; S30079 REFERENCE A30395 !$#authors Friedrich, M.J.; Kadner, R.J. !$#journal J. Bacteriol. (1987) 169:3556-3563 !$#title Nucleotide sequence of the uhp region of Escherichia coli. !$#cross-references MUID:87279903; PMID:3301805 !$#accession A30395 !'##molecule_type DNA !'##residues 1-463 ##label FRI !'##cross-references GB:M17102; NID:g148110; PIDN:AAA24723.1; !1PID:g148115 REFERENCE A41853 !$#authors Island, M.D.; Wei, B.Y.; Kadner, R.J. !$#journal J. Bacteriol. (1992) 174:2754-2762 !$#title Structure and function of the uhp genes for the sugar !1phosphate transport system in Escherichia coli and !1Salmonella typhimurium. !$#cross-references MUID:92234930; PMID:1569007 !$#accession H41853 !'##molecule_type DNA !'##residues 1-463 ##label ISL !'##cross-references EMBL:M89479; NID:g148116; PIDN:AAA24727.1; !1PID:g148120 !'##note in the authors' translation residues 385 and 386 are displaced !1one codon to the right REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65168 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-463 ##label BLAT !'##cross-references GB:AE000444; GB:U00096; NID:g2367258; !1PIDN:AAC76689.1; PID:g2367259; UWGP:b3666 !'##experimental_source strain K-12, substrain MG1655 COMMENT This protein, a cytoplasmic membrane protein with potential !1transmembrane segments, is the transporter for a sugar !1phosphate transport system. The gene expression of this !1system is induced by external glucose-6-phosphate. GENETICS !$#gene uhpT !$#map_position 82 min CLASSIFICATION #superfamily hexose phosphate transport protein uhpT KEYWORDS membrane protein; sugar phosphate transport system SUMMARY #length 463 #molecular-weight 50606 #checksum 3111 SEQUENCE /// ENTRY RGECUC #type complete TITLE regulatory protein uhpC - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1991 #sequence_revision 14-Nov-1997 #text_change 01-Mar-2002 ACCESSIONS D65168; G41853; C26925; S30078 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65168 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-440 ##label BLAT !'##cross-references GB:AE000444; GB:U00096; NID:g2367258; !1PIDN:AAC76690.1; PID:g2367260; UWGP:b3667 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A41853 !$#authors Island, M.D.; Wei, B.Y.; Kadner, R.J. !$#journal J. Bacteriol. (1992) 174:2754-2762 !$#title Structure and function of the uhp genes for the sugar !1phosphate transport system in Escherichia coli and !1Salmonella typhimurium. !$#cross-references MUID:92234930; PMID:1569007 !$#accession G41853 !'##molecule_type DNA !'##residues 2-440 ##label ISL !'##cross-references GB:M89479; NID:g148116; PIDN:AAA24726.1; !1PID:g148119 !'##note this is a revision to the sequence from reference A30395 REFERENCE A30395 !$#authors Friedrich, M.J.; Kadner, R.J. !$#journal J. Bacteriol. (1987) 169:3556-3563 !$#title Nucleotide sequence of the uhp region of Escherichia coli. !$#cross-references MUID:87279903; PMID:3301805 !$#accession C26925 !'##molecule_type DNA !'##residues 'M',87,'VCRALGAE',96,'L',98,'P',100,'L',102,'FTG',139-141, !1'SVNGLVFTYRA',153,'R',156-337,'C' ##label FRI !'##note this sequence has been revised in reference A41853 COMMENT This is one of the proteins involved in the expression of !1uhpT, a gene for hexose phosphate transport. It may also !1have a role in transmembrane signaling involving !1sugar-phosphate-binding NAD transmembrane orientation. GENETICS !$#gene uhpC !$#map_position 82 min CLASSIFICATION #superfamily hexose phosphate transport protein uhpT KEYWORDS membrane protein; sugar phosphate transport system SUMMARY #length 440 #molecular-weight 48387 #checksum 1829 SEQUENCE /// ENTRY JNEBPT #type complete TITLE phosphoglycerate transport protein - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS A31089 REFERENCE A31089 !$#authors Goldrick, D.; Yu, G.Q.; Jiang, S.Q.; Hong, J.S. !$#journal J. Bacteriol. (1988) 170:3421-3426 !$#title Nucleotide sequence and transcription start point of the !1phosphoglycerate transporter gene of Salmonella typhimurium. !$#cross-references MUID:88298646; PMID:3042749 !$#accession A31089 !'##molecule_type DNA !'##residues 1-406 ##label GOL !'##cross-references GB:M21278; NID:g154261; PIDN:AAA27186.1; !1PID:g154262 !'##note the authors translated the codon TTG for residues 59 and 206 as !1Phe, GAA for residues 182 and 214 as Gln and Asp, !1respectively, and GGC for residue 274 as Glu GENETICS !$#gene pgtP CLASSIFICATION #superfamily hexose phosphate transport protein uhpT KEYWORDS membrane bound; sugar phosphate transport system; !1transmembrane protein FEATURE !$28-44 #domain transmembrane #status predicted #label TM1\ !$95-113 #domain transmembrane #status predicted #label TM2\ !$116-133 #domain transmembrane #status predicted #label TM3\ !$163-180 #domain transmembrane #status predicted #label TM4\ !$189-207 #domain transmembrane #status predicted #label TM5\ !$265-286 #domain transmembrane #status predicted #label TM6\ !$296-315 #domain transmembrane #status predicted #label TM7\ !$325-343 #domain transmembrane #status predicted #label TM8\ !$348-369 #domain transmembrane #status predicted #label TM9 SUMMARY #length 406 #molecular-weight 44853 #checksum 685 SEQUENCE /// ENTRY JNECGT #type complete TITLE glycerol-3-phosphate transport protein - Escherichia coli (strain K-12) ALTERNATE_NAMES glycerol-3-phosphate permease ORGANISM #formal_name Escherichia coli DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 01-Mar-2002 ACCESSIONS S00868; F64994 REFERENCE S00868 !$#authors Eiglmeier, K.; Boos, W.; Cole, S.T. !$#journal Mol. Microbiol. (1987) 1:251-258 !$#title Nucleotide sequence and transcriptional startpoint of the !1glpT gene of Escherichia coli: extensive sequence homology !1of the glycerol-3-phosphate transport protein with !1components of the hexose-6-phosphate transport system. !$#cross-references MUID:88201663; PMID:3329281 !$#accession S00868 !'##molecule_type DNA !'##residues 1-452 ##label EIG !'##cross-references EMBL:Y00536; NID:g41586; PIDN:CAA68598.1; !1PID:g41587 !'##experimental_source strain K12 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64994 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-452 ##label BLAT !'##cross-references GB:AE000314; GB:U00096; NID:g1788570; !1PIDN:AAC75300.1; PID:g1788573; UWGP:b2240 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene glpT !$#map_position 49 min CLASSIFICATION #superfamily hexose phosphate transport protein uhpT KEYWORDS sugar phosphate transport system; transmembrane protein FEATURE !$94-117 #domain transmembrane #status predicted #label TM1\ !$120-138 #domain transmembrane #status predicted #label TM2\ !$167-183 #domain transmembrane #status predicted #label TM3\ !$186-208 #domain transmembrane #status predicted #label TM4\ !$254-273 #domain transmembrane #status predicted #label TM5\ !$322-341 #domain transmembrane #status predicted #label TM6\ !$351-373 #domain transmembrane #status predicted #label TM7\ !$382-406 #domain transmembrane #status predicted #label TM8\ !$415-437 #domain transmembrane #status predicted #label TM9 SUMMARY #length 452 #molecular-weight 50310 #checksum 816 SEQUENCE /// ENTRY GREC #type complete TITLE lactose permease - Escherichia coli (strain K-12) ALTERNATE_NAMES lactose transport protein; lactose-proton symport protein ORGANISM #formal_name Escherichia coli DATE 31-Mar-1980 #sequence_revision 31-Mar-1980 #text_change 01-Mar-2002 ACCESSIONS A03418; S21314; A61352; G64761 REFERENCE A03418 !$#authors Buchel, D.E.; Gronenborn, B.; Muller-Hill, B. !$#journal Nature (1980) 283:541-545 !$#title Sequence of the lactose permease gene. !$#cross-references MUID:80120651; PMID:6444453 !$#accession A03418 !'##molecule_type DNA !'##residues 1-417 ##label BUC !'##cross-references GB:V00295; NID:g41897; PIDN:CAA23571.1; PID:g41899 REFERENCE S21314 !$#authors Pastore, J.C.; Larigan, J.D.; Consler, T.G.; Kaback, H.R. !$#submission submitted to the EMBL Data Library, September 1990 !$#accession S21314 !'##molecule_type DNA !'##residues 1-417 ##label PAS !'##cross-references EMBL:X56095; NID:g42417; PIDN:CAA39575.1; !1PID:g42418 REFERENCE A61352 !$#authors Ehring, R.; Beyreuther, K.; Wright, J.K.; Overath, P. !$#journal Nature (1980) 283:537-540 !$#title In vitro and in vivo products of Escherichia coli lactose !1permease gene are identical. !$#cross-references MUID:80120650; PMID:6986561 !$#accession A61352 !'##molecule_type protein !'##residues 1-5,'X',7,'X',9,'X',11-32,'X',34,'X',36-37,'XX',40,'X',42 !1##label EHR REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64761 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-417 ##label BLAT !'##cross-references GB:AE000141; GB:U00096; NID:g1786532; !1PIDN:AAC73446.1; PID:g1786538; UWGP:b0343 !'##experimental_source strain K-12, substrain MG1655 COMMENT This protein is processed by a fairly efficient !1deformylation of the amino-terminal N-formylmethionine and !1not by proteolytic cleavage. GENETICS !$#gene lacY !$#map_position 8 min FUNCTION !$#description responsible for the transport of galactosides into the cell !$#note located in the inner membrane CLASSIFICATION #superfamily lactose permease KEYWORDS inner membrane; sugar transport; symport system; !1transmembrane protein FEATURE !$9-25 #domain transmembrane #status predicted #label TM1\ !$47-63 #domain transmembrane #status predicted #label TM2\ !$79-95 #domain transmembrane #status predicted #label TM3\ !$103-119 #domain transmembrane #status predicted #label TM4\ !$148-164 #domain transmembrane #status predicted #label TM5\ !$168-184 #domain transmembrane #status predicted #label TM6\ !$267-283 #domain transmembrane #status predicted #label TM7\ !$292-308 #domain transmembrane #status predicted #label TM8\ !$315-331 #domain transmembrane #status predicted #label TM9\ !$352-368 #domain transmembrane #status predicted #label TM10\ !$383-399 #domain transmembrane #status predicted #label TM11\ !$1 #modified_site N-formylmethionine (partial) #status !8experimental SUMMARY #length 417 #molecular-weight 46503 #checksum 1268 SEQUENCE /// ENTRY GRECST #type complete TITLE sucrose transport protein - Escherichia coli ALTERNATE_NAMES sucrose permease ORGANISM #formal_name Escherichia coli DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS S30107; S52160; S19880 REFERENCE S30107 !$#authors Bockmann, J.; Heuel, H.; Lengeler, J.W. !$#journal Mol. Gen. Genet. (1992) 235:22-32 !$#title Characterization of a chromosomally encoded, non-PTS !1metabolic pathway for sucrose utilization in Escherichia !1coli EC3132. !$#cross-references MUID:93062804; PMID:1435727 !$#accession S30107 !'##molecule_type DNA !'##residues 1-415 ##label BOC1 !'##cross-references EMBL:X63740; NID:g41167; PIDN:CAA45274.1; !1PID:g41168 REFERENCE S52160 !$#authors Bockmann, J. !$#submission submitted to the EMBL Data Library, September 1994 !$#accession S52160 !'##molecule_type DNA !'##residues 1-415 ##label BOC2 !'##cross-references EMBL:X81461; NID:g608705; PIDN:CAA57217.1; !1PID:g608706 GENETICS !$#gene cscB CLASSIFICATION #superfamily lactose permease KEYWORDS sugar transport; transmembrane protein FEATURE !$1-13 #domain intracellular #status predicted #label INT1\ !$14-37 #domain transmembrane #status predicted #label TM01\ !$51-69 #domain transmembrane #status predicted #label TM02\ !$78-102 #domain transmembrane #status predicted #label TM03\ !$106-128 #domain transmembrane #status predicted #label TM04\ !$148-165 #domain transmembrane #status predicted #label TM05\ !$171-188 #domain transmembrane #status predicted #label TM06\ !$189-218 #domain intracellular #status predicted #label INT2\ !$219-249 #domain transmembrane #status predicted #label TM07\ !$258-281 #domain transmembrane #status predicted #label TM08\ !$289-308 #domain transmembrane #status predicted #label TM09\ !$311-332 #domain transmembrane #status predicted #label TM10\ !$347-363 #domain transmembrane #status predicted #label TM11\ !$379-398 #domain transmembrane #status predicted #label TM12 SUMMARY #length 415 #molecular-weight 46923 #checksum 9180 SEQUENCE /// ENTRY WQECFP #type complete TITLE L-fucose permease - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 01-Mar-2002 ACCESSIONS JS0184; C33495; S49565; E65062 REFERENCE S04702 !$#authors Lu, Z.; Lin, E.C.C. !$#journal Nucleic Acids Res. (1989) 17:4883-4884 !$#title The nucleotide sequence of Escherichia coli genes for !1L-fucose dissimilation. !$#cross-references MUID:89315234; PMID:2664711 !$#accession JS0184 !'##molecule_type DNA !'##residues 1-438 ##label LUZ !'##cross-references EMBL:X15025; NID:g41501; PIDN:CAA33126.1; !1PID:g41504 REFERENCE A33495 !$#authors Chen, Y.M.; Lu, Z.; Lin, E.C.C. !$#journal J. Bacteriol. (1989) 171:6097-6105 !$#title Constitutive activation of the fucAO operon and silencing of !1the divergently transcribed fucPIK operon by an IS5 element !1in Escherichia coli mutants selected for growth on L-1, !12-propanediol. !$#cross-references MUID:90036697; PMID:2553671 !$#accession C33495 !'##status preliminary !'##molecule_type DNA !'##residues 1-31 ##label CHE !'##cross-references GB:M31059; NID:g146040; PIDN:AAA23822.1; !1PID:g146041 REFERENCE S49564 !$#authors Gunn, F.J.; Tate, C.G.; Henderson, P.J.F. !$#journal Mol. Microbiol. (1994) 12:799-809 !$#title Identification of a novel sugar-H(+) symport protein, FucP, !1for transport of L-fucose into Escherichia coli. !$#cross-references MUID:94328931; PMID:8052131 !$#accession S49565 !'##molecule_type protein !'##residues 2-21 ##label GUN REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65062 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-438 ##label BLAT !'##cross-references GB:AE000364; GB:U00096; NID:g2367162; !1PIDN:AAC75843.1; PID:g1789166; UWGP:b2801 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene fucP !$#map_position 60 min FUNCTION !$#description this protein is a permease involved in an inducible !1catabolic pathway for L-fucose CLASSIFICATION #superfamily fucose permease KEYWORDS L-fucose catabolism; L-fucose utilization; transmembrane !1protein SUMMARY #length 438 #molecular-weight 47544 #checksum 7007 SEQUENCE /// ENTRY RYEC2 #type complete TITLE DNA primase (EC 2.7.7.-) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 20-Sep-1984 #sequence_revision 20-Sep-1984 #text_change 01-Mar-2002 ACCESSIONS A03423; H65094; A03422; I77532 REFERENCE A02749 !$#authors Burton, Z.F.; Gross, C.A.; Watanabe, K.K.; Burgess, R.R. !$#journal Cell (1983) 32:335-349 !$#title The operon that encodes the sigma subunit of RNA polymerse !1also encodes ribosomal protein S21 and DNA primase in !1Escherichia coli K12. !$#cross-references MUID:83129424; PMID:6186393 !$#accession A03423 !'##molecule_type DNA !'##residues 1-581 ##label BUR !'##cross-references GB:J01687; NID:g147753; PIDN:AAA24600.1; !1PID:g147755 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65094 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-581 ##label BLAT !'##cross-references GB:AE000388; GB:U00096; NID:g1789441; !1PIDN:AAC76102.1; PID:g1789447; UWGP:b3066 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A03422 !$#authors Smiley, B.L.; Lupski, J.R.; Svec, P.S.; McMacken, R.; !1Godson, G.N. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:4550-4554 !$#title Sequences of the Escherichia coli dnaG primase gene and !1regulation of its expression. !$#cross-references MUID:83014926; PMID:6750604 !$#accession A03422 !'##molecule_type DNA !'##residues 1-23,'N',25-105,'XPDRAPSEANALSVDGRSEYVLPTIFTTTCCHVCAPVSG', !1145-156,'GLVLR',162-163,'AGQR',169-272,'V',274-581 ##label !1SMI REFERENCE I57721 !$#authors Lupski, J.R.; Smiley, B.L.; Godson, G.N. !$#journal Mol. Gen. Genet. (1983) 189:48-57 !$#title Regulation of the rpsU-dnaG-rpoD macromolecular synthesis !1operon and the initiation of DNA replication in Escherichia !1coli K-12. !$#cross-references MUID:83218520; PMID:6222240 !$#accession I77532 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-23,'N',25-81 ##label RES !'##cross-references EMBL:V00346; NID:g42867; PIDN:CAA23636.1; !1PID:g42869 COMMENT This enzyme, an RNA polymerase, interacts with DNA to !1synthesize the primer RNA that initiates DNA replication. GENETICS !$#gene dnaG !$#map_position 67 min CLASSIFICATION #superfamily DNA primase KEYWORDS DNA replication; nucleotidyltransferase SUMMARY #length 581 #molecular-weight 65564 #checksum 1758 SEQUENCE /// ENTRY RYEBT #type complete TITLE DNA primase (EC 2.7.7.-) - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 16-Jul-1999 ACCESSIONS B23985 REFERENCE A91542 !$#authors Erickson, B.D.; Burton, Z.F.; Watanabe, K.K.; Burgess, R.R. !$#journal Gene (1985) 40:67-78 !$#title Nucleotide sequence of the rpsU-dnaG-rpoD operon from !1Salmonella typhimurium and a comparison of this sequence !1with the homologous operon of Escherichia coli. !$#cross-references MUID:86137422; PMID:3005129 !$#accession B23985 !'##molecule_type DNA !'##residues 1-581 ##label ERI !'##cross-references GB:M14427; NID:g154402; PIDN:AAA27241.1; !1PID:g154405 GENETICS !$#gene dnaG CLASSIFICATION #superfamily DNA primase KEYWORDS DNA replication; nucleotidyltransferase SUMMARY #length 581 #molecular-weight 65362 #checksum 587 SEQUENCE /// ENTRY RPECEG #type complete TITLE ebg repressor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 01-Mar-2002 ACCESSIONS A25752; S09205; H65095 REFERENCE A25752 !$#authors Stokes, H.W.; Hall, B.G. !$#journal Mol. Biol. Evol. (1985) 2:478-483 !$#title Sequence of the ebgR gene of Escherichia coli: evidence that !1the EBG and LAC operons are descended from a common !1ancestor. !$#cross-references MUID:88216134; PMID:3939708 !$#accession A25752 !'##molecule_type DNA !'##residues 1-327 ##label STO !'##cross-references GB:M64441; GB:M13700; GB:M13796; GB:M66835; !1GB:M66836; GB:X03228; NID:g145819; PIDN:AAA61970.1; !1PID:g145820 !'##note the authors translated the codon GAA for residue 255 as Gly REFERENCE S09205 !$#authors Hall, B.G.; Betts, P.W.; Wootton, J.C. !$#journal Genetics (1989) 123:635-648 !$#title DNA sequence analysis of artificially evolved ebg enzyme and !1ebg repressor genes. !$#cross-references MUID:90128218; PMID:2515108 !$#accession S09205 !'##molecule_type DNA !'##residues 1-327 ##label HAL !'##cross-references EMBL:X52031; NID:g41307; PIDN:CAA36273.1; !1PID:g41308 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65095 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-327 ##label BLAT !'##cross-references GB:AE000389; GB:U00096; NID:g1789451; !1PIDN:AAC76110.1; PID:g1789456; UWGP:b3075 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ebgR !$#map_position 68 min CLASSIFICATION #superfamily lac repressor KEYWORDS DNA binding; transcription regulation FEATURE !$3-23 #region helix-turn-helix motif SUMMARY #length 327 #molecular-weight 36210 #checksum 6597 SEQUENCE /// ENTRY RPECL #type complete TITLE lactose operon repressor - Escherichia coli (strain K-12) ALTERNATE_NAMES lac repressor ORGANISM #formal_name Escherichia coli DATE 30-Apr-1982 #sequence_revision 30-Apr-1982 #text_change 01-Mar-2002 ACCESSIONS A93198; A91234; A92122; A93785; S40661; S02540; A64762; !1S68009; S14614; A03558 REFERENCE A93198 !$#authors Farabaugh, P.J. !$#journal Nature (1978) 274:765-769 !$#title Sequence of the lacI gene. !$#cross-references MUID:78246991; PMID:355891 !$#accession A93198 !'##molecule_type DNA !'##residues 1-360 ##label FAR REFERENCE A91234 !$#authors Beyreuther, K.; Adler, K.; Fanning, E.; Murray, C.; Klemm, !1A.; Geisler, N. !$#journal Eur. J. Biochem. (1975) 59:491-509 !$#title Amino-acid sequence of lac repressor from Escherichia coli. !1Isolation, sequence analysis and sequence assembly of !1tryptic peptides and cyanogen-bromide fragments. !$#cross-references MUID:76091932; PMID:1107032 !$#accession A91234 !'##molecule_type protein !'##residues 1-147;159-163,'Q',165-230;233-360 ##label BEY !'##note the active repressor is a tetramer of identical chains !'##note this protein was obtained from a strain with the I-SQ mutation, !1which leads to an overproduction of wild-type repressor, !1probably by affecting the promoter for the lac repressor !1gene !'##note this sequence has since been revised REFERENCE A93199 !$#authors Beyreuther, K. !$#journal Nature (1978) 274:767 !$#contents annotation; revision !$#note the revised sequence is identical with that shown REFERENCE A92122 !$#authors Platt, T.; Files, J.G.; Weber, K. !$#journal J. Biol. Chem. (1973) 248:110-121 !$#cross-references MUID:73143730; PMID:4571224 !$#accession A92122 !'##molecule_type protein !'##residues 1-59;96-101;206-215;328-347 ##label PLA !'##note removal of residues 1-59 and 328-347 results in the molecule !1losing its DNA-binding activity while maintaining its !1inducer-binding activity and its tetrameric structure REFERENCE A93785 !$#authors Ganem, D.; Miller, J.H.; Files, J.G.; Platt, T.; Weber, K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1973) 70:3165-3169 !$#title Reinitiation of a lac repressor fragment at a codon other !1than ATG. !$#cross-references MUID:74126378; PMID:4594037 !$#accession A93785 !'##molecule_type protein !'##residues 60-70;73-78;83-86 ##label GAN REFERENCE S40661 !$#authors Shin, J.A.; Ebright, R.H.; Dervan, P.B. !$#journal Nucleic Acids Res. (1991) 19:5233-5236 !$#title Orientation of the Lac repressor DNA binding domain in !1complex with the left lac operator half site characterized !1by affinity cleaving. !$#cross-references MUID:92020210; PMID:1923807 !$#accession S40661 !'##molecule_type DNA !'##residues 1-56 ##label SHI REFERENCE S02540 !$#authors Gordon, A.J.E.; Burns, P.A.; Fix, D.F.; Yatagai, F.; Allen, !1F.L.; Horsfall, M.J.; Halliday, J.A.; Gray, J.; !1Bernelot-Moens, C.; Glickman, B.W. !$#journal J. Mol. Biol. (1988) 200:239-251 !$#title Missense mutation in the lacI gene of Escherichia coli. !1Inferences on the structure of the repressor protein. !$#cross-references MUID:88230449; PMID:3286877 !$#accession S02540 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-60 ##label GOR REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64762 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-360 ##label BLAT !'##cross-references GB:AE000141; GB:U00096; NID:g1786532; !1PIDN:AAC73448.1; PID:g1786540; UWGP:b0345 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S68009 !$#authors Kamashev, D.E.; Esipova, N.G.; Ebralidse, K.K.; Mirzabekov, !1A.D. !$#journal FEBS Lett. (1995) 375:27-30 !$#title Mechanism of Lac repressor switch-off: orientation of the !1Lac repressor DNA-binding domain is reversed upon inducer !1binding. !$#cross-references MUID:96087076; PMID:7498473 !$#accession S68009 !'##molecule_type protein !'##residues 'X',2-22;23-32,'X',34-35 ##label KAM REFERENCE S14614 !$#authors Chen, J.; Matthews, K.K.S.M. !$#submission submitted to the EMBL Data Library, March 1991 !$#description T41 mutation in lac repressor is Tyr282Asp. !$#accession S14614 !'##molecule_type DNA !'##residues 'V',2-108,'T',110-281,'D',283-285,'S',287-360 ##label CHE !'##cross-references EMBL:X58469 !'##experimental_source T41 mutant GENETICS !$#gene lacI !$#map_position 8 min !$#start_codon GTG COMPLEX homotetramer CLASSIFICATION #superfamily lac repressor KEYWORDS DNA binding; homotetramer; transcription regulation FEATURE !$5-25 #region helix-turn-helix motif SUMMARY #length 360 #molecular-weight 38590 #checksum 1939 SEQUENCE /// ENTRY RPECCT #type complete TITLE transcription regulator cytR [similarity] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 01-Mar-2002 ACCESSIONS A24963; S40877; A65200 REFERENCE A24963 !$#authors Valentin-Hansen, P.; Larsen, J.E.L.; Hojrup, P.; Short, !1S.A.; Barbier, C.S. !$#journal Nucleic Acids Res. (1986) 14:2215-2228 !$#title Nucleotide sequence of the cytR regulatory gene of E. coli !1K-12. !$#cross-references MUID:86176724; PMID:3515317 !$#accession A24963 !'##molecule_type DNA !'##residues 1-341 ##label VAL !'##cross-references GB:X03683; NID:g41207; PIDN:CAA27318.1; PID:g581060 !'##experimental_source strain K12 REFERENCE S40802 !$#authors Plunkett III, G.; Burland, V.; Daniels, D.L.; Blattner, F.R. !$#journal Nucleic Acids Res. (1993) 21:3391-3398 !$#title Analysis of the Escherichia coli genome. III. DNA sequence !1of the region from 87.2 to 89.2 minutes. !$#cross-references MUID:93347969; PMID:8346018 !$#accession S40877 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-341 ##label PLU !'##cross-references EMBL:L19201; NID:g304961; PIDN:AAB03066.1; !1PID:g305037 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1993 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65200 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-341 ##label BLAT !'##cross-references GB:AE000467; GB:U00096; NID:g1790356; !1PIDN:AAC76916.1; PID:g1790369; UWGP:b3934 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene cytR !$#map_position 88.8 min !$#start_codon GTG FUNCTION !$#description negatively controls the transcription initiation of genes !1such as deoCABD, udp, and cdd encoding catabolizing enzymes !1and nupC, nupG, and tsx encoding transporting and !1pore-forming proteins CLASSIFICATION #superfamily lac repressor KEYWORDS DNA binding; transcription regulation FEATURE !$11-31 #region helix-turn-helix motif SUMMARY #length 341 #molecular-weight 37819 #checksum 7254 SEQUENCE /// ENTRY RPECG #type complete TITLE gal operon repressor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 15-Oct-1982 #sequence_revision 15-Oct-1982 #text_change 01-Mar-2002 ACCESSIONS A93910; A92900; F65066; A03559 REFERENCE A93910 !$#authors von Wilcken-Bergmann, B.; Muller-Hill, B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:2427-2431 !$#title Sequence of galR gene indicates a common evolutionary origin !1of lac and gal repressor in Escherichia coli. !$#cross-references MUID:82222151; PMID:6283521 !$#accession A93910 !'##molecule_type DNA !'##residues 1-343 ##label VON !'##cross-references GB:V00280; NID:g41533; PIDN:CAA23543.1; PID:g41534 REFERENCE A92900 !$#authors Stragier, P.; Danos, O.; Patte, J.C. !$#journal J. Mol. Biol. (1983) 168:321-331 !$#title Regulation of diaminopimelate decarboxylase synthesis in !1Escherichia coli. II. Nucleotide sequence of the lysA gene !1and its regulatory region. !$#cross-references MUID:83294516; PMID:6350601 !$#accession A92900 !'##molecule_type DNA !'##residues 31-343 ##label STR REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65066 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-343 ##label BLAT !'##cross-references GB:AE000367; GB:U00096; NID:g1789195; !1PIDN:AAC75876.1; PID:g1789202; UWGP:b2837 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene galR !$#map_position 62 min CLASSIFICATION #superfamily lac repressor KEYWORDS DNA binding; transcription regulation FEATURE !$5-22 #region helix-turn-helix motif SUMMARY #length 343 #molecular-weight 37094 #checksum 2506 SEQUENCE /// ENTRY RPECML #type complete TITLE maltose regulon repressor malI - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1991 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS F64918; JV0031; A42477 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64918 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-342 ##label BLAT !'##cross-references GB:AE000257; GB:U00096; NID:g1787898; !1PIDN:AAC74692.1; PID:g1787906; UWGP:b1620 !'##experimental_source strain K-12, substrain MG1655 REFERENCE JV0031 !$#authors Reidl, J.; Roemisch, K.; Ehrmann, M.; Boos, W. !$#journal J. Bacteriol. (1989) 171:4888-4899 !$#title MalI, a novel protein involved in regulation of the maltose !1system of Escherichia coli, is highly homologous to the !1repressor proteins GalR, CytR, and LacI. !$#cross-references MUID:89359124; PMID:2670898 !$#accession JV0031 !'##molecule_type DNA !'##residues 1-286,'IYRCD',291,'NH',294,'CMH',298-316,'SHDA',321,'NHP' !1##label LEV !'##cross-references GB:M28539; NID:g146707; PIDN:AAA24104.1; !1PID:g146709 REFERENCE A42477 !$#authors Reidl, J.; Boos, W. !$#journal J. Bacteriol. (1991) 173:4862-4876 !$#title The malX malY operon of Escherichia coli encodes a novel !1enzyme II of the phosphotransferase system recognizing !1glucose and maltose and an enzyme abolishing the endogenous !1induction of the maltose system. !$#cross-references MUID:91310596; PMID:1856179 !$#accession A42477 !'##status preliminary !'##molecule_type DNA !'##residues 1-52 ##label REI !'##cross-references GB:M60722 GENETICS !$#gene malI !$#map_position 36 min FUNCTION !$#description transcriptional repressor for malX-malY operon !$#note autoregulation; maltose acts as inducer CLASSIFICATION #superfamily lac repressor KEYWORDS DNA binding; repressor; transcription regulation FEATURE !$8-28 #region helix-turn-helix motif SUMMARY #length 342 #molecular-weight 36624 #checksum 1503 SEQUENCE /// ENTRY RPECDU #type complete TITLE pur operon repressor purR - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 01-Mar-2002 ACCESSIONS A32027; S08477; D64923; JS0138 REFERENCE A32027 !$#authors Rolfes, R.J.; Zalkin, H. !$#journal J. Biol. Chem. (1988) 263:19653-19661 !$#title Escherichia coli gene purR encoding a repressor protein for !1purine nucleotide synthesis. Cloning, nucleotide sequence, !1and interaction with the purF operator. !$#cross-references MUID:89066795; PMID:3058704 !$#accession A32027 !'##molecule_type DNA !'##residues 1-341 ##label ROL !'##cross-references GB:J04212; NID:g147427; PIDN:AAA24457.1; !1PID:g147428 REFERENCE S08477 !$#authors Meng, L.M.; Kilstrup, M.; Nygaard, P. !$#journal Eur. J. Biochem. (1990) 187:373-379 !$#title Autoregulation of PurR repressor synthesis and involvement !1of purR in the regulation of purB, purC, purL, purMN and !1guaBA expression in Escherichia coli. !$#cross-references MUID:90126847; PMID:2404765 !$#accession S08477 !'##status translation not shown !'##molecule_type DNA !'##residues 1-341 ##label MEN !'##cross-references EMBL:X51368; NID:g42597; PIDN:CAA35753.1; !1PID:g42598 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64923 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-341 ##label BLAT !'##cross-references GB:AE000261; GB:U00096; NID:g1787945; !1PIDN:AAC74730.1; PID:g1787948; UWGP:b1658 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene purR !$#map_position 36 min FUNCTION !$#description binds to the purF operator and coregulates other genes for !1de novo purine nucleotide synthesis CLASSIFICATION #superfamily lac repressor KEYWORDS DNA binding; transcription regulation FEATURE !$5-23 #region helix-turn-helix motif SUMMARY #length 341 #molecular-weight 38174 #checksum 9364 SEQUENCE /// ENTRY JGECR #type complete TITLE periplasmic ribose-binding protein precursor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 01-Mar-2002 ACCESSIONS A03425; H65178; S72655 REFERENCE A03425 !$#authors Groarke, J.M.; Mahoney, W.C.; Hope, J.N.; Furlong, C.E.; !1Robb, F.T.; Zalkin, H.; Hermodson, M.A. !$#journal J. Biol. Chem. (1983) 258:12952-12956 !$#title The amino acid sequence of D-ribose-binding protein from !1Escherichia coli K12. !$#cross-references MUID:84032513; PMID:6313683 !$#accession A03425 !'##molecule_type DNA !'##residues 1-296 ##label GRO !'##cross-references GB:M13169; GB:M13517; NID:g147511; PIDN:AAA51475.1; !1PID:g147515 !'##experimental_source strain K12 DG50-3 !'##note most of the primary structure was confirmed by protein !1sequencing REFERENCE A44680 !$#authors Mowbray, S.L.; Cole, L.B. !$#journal J. Mol. Biol. (1992) 225:155-175 !$#title 1.7 angstroms x-ray structure of the periplasmic ribose !1receptor from escherichia coli. !$#cross-references MUID:92260530; PMID:1583688 !$#contents annotation; X-ray crystallography, 1.7 angstroms REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65178 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-296 ##label BLAT !'##cross-references GB:AE000452; GB:U00096; NID:g1790188; !1PIDN:AAC76774.1; PID:g1790192; UWGP:b3751 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S72651 !$#authors Gonzalez-Gil, G.; Bringmann, P.; Kahmann, R. !$#journal Mol. Microbiol. (1996) 22:21-29 !$#title FIS is a regulator of metabolism in Escherichia coli. !$#cross-references MUID:97055418; PMID:8899705 !$#accession S72655 !'##molecule_type protein !'##residues 26-39 ##label GON COMMENT This periplasmic binding protein is involved in the !1high-affinity D-ribose membrane transport system and also !1serves as the primary chemoreceptor for chemotaxis. GENETICS !$#gene rbsB CLASSIFICATION #superfamily lac repressor KEYWORDS chemotaxis; periplasmic space; sugar transport FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-296 #product D-ribose-binding protein #status !8experimental #label MAT\ !$26-128,261-289 #domain 1 #status experimental #label TOP\ !$129-260,290-296 #domain 2 #status experimental #label BOT\ !$38,114,115,166,215, !$240,260 #binding_site beta-D-ribopyranose (Asn, Asp, Arg, !8Arg, Asn, Asp, Gln) #status experimental SUMMARY #length 296 #molecular-weight 30950 #checksum 3926 SEQUENCE /// ENTRY JGEBRT #type complete TITLE D-ribose-binding protein - Salmonella typhimurium (tentative sequence) ORGANISM #formal_name Salmonella typhimurium DATE 25-Feb-1985 #sequence_revision 10-Feb-1995 #text_change 22-Nov-1996 ACCESSIONS A03426 REFERENCE A03426 !$#authors Buckenmeyer, G.K.; Hermodson, M.A. !$#journal J. Biol. Chem. (1983) 258:12957 !$#title The amino acid sequence of D-ribose-binding protein from !1Salmonella typhimurium ST1. !$#cross-references MUID:84032514; PMID:6415058 !$#accession A03426 !'##molecule_type protein !'##residues 1-271 ##label BUC !'##experimental_source strain ST1 !'##note only cyanogen bromide peptides differing in composition from !1the Escherichia coli K12 protein (see A03425) were !1sequenced; the determined positions were 1-35, 78-97, !1194-208, 211-244 in the sequence shown COMMENT This periplasmic binding protein is involved in the !1high-affinity D-ribose membrane transport system and also !1serves as the primary chemoreceptor for chemotaxis. CLASSIFICATION #superfamily lac repressor KEYWORDS chemotaxis; periplasmic space; sugar transport FEATURE !$1-271 #product D-ribose-binding protein #status !8experimental #label MAT\ !$13,89,90,141,190, !$215,235 #binding_site beta-D-ribopyranose (Asn, Asp, Arg, !8Arg, Asn, Asp, Gln) #status predicted SUMMARY #length 271 #molecular-weight 28530 #checksum 8021 SEQUENCE /// ENTRY A36940 #type complete TITLE sporulation-specific degradation regulator protein DegA - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 11-Nov-1994 #sequence_revision 02-Jul-1998 #text_change 16-Jun-2000 ACCESSIONS G69613; A36940 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69613 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-337 ##label KUN !'##cross-references GB:Z99109; GB:AL009126; NID:g2633260; !1PIDN:CAB12923.1; PID:g2633419 !'##experimental_source strain 168 REFERENCE A36940 !$#authors Bussey, L.B.; Switzer, R.L. !$#journal J. Bacteriol. (1993) 175:6348-6353 !$#title The degA gene product accelerates degradation of Bacillus !1subtilis phosphoribosylpyrophosphate amidotransferase in !1Escherichia coli. !$#cross-references MUID:94012500; PMID:8407808 !$#accession A36940 !'##molecule_type DNA !'##residues 1-299,'AERHRTAGRSNR',312-337 ##label BUS !'##cross-references GB:L08822; NID:g142835; PIDN:AAA03541.1; !1PID:g142836 COMMENT In nutrient-deprived cells, this protein, probably acting as !1regulatory protein rather than a proteinase, stimulates the !1specific, energy-requiring inactivation and degradation of !1several biosynthetic enzymes. GENETICS !$#gene degA CLASSIFICATION #superfamily lac repressor KEYWORDS DNA binding; sporulation; transcription regulation FEATURE !$5-24 #region helix-turn-helix SUMMARY #length 337 #molecular-weight 36595 #checksum 9032 SEQUENCE /// ENTRY E69690 #type complete TITLE transcription repressor of ribose operon - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS E69690; I40462; S42710 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69690 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-326 ##label KUN !'##cross-references GB:Z99122; GB:AL009126; NID:g2636029; !1PIDN:CAB15608.1; PID:g2636116 !'##experimental_source strain 168 REFERENCE I40462 !$#authors Woodson, K.; Devine, K.M. !$#journal Microbiology (1994) 140:1829-1838 !$#title Analysis of a ribose transport operon from Bacillus !1subtilis. !$#cross-references MUID:95005437; PMID:7921236 !$#accession I40462 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-121,'QRITRISR',130-251,'AK',254,'RAG',259-326 ##label RES !'##cross-references EMBL:Z25798; NID:g397493; PIDN:CAA81048.1; !1PID:g580917 !'##experimental_source strain 168 GENETICS !$#gene rbsR !$#start_codon TTG CLASSIFICATION #superfamily lac repressor KEYWORDS DNA binding; transcription regulation SUMMARY #length 326 #molecular-weight 35855 #checksum 3843 SEQUENCE /// ENTRY S44259 #type complete TITLE sucrose operon regulatory protein scrR - Pediococcus pentosaceus ORGANISM #formal_name Pediococcus pentosaceus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S44259 REFERENCE S44252 !$#authors Leenhouts, K.K.J.; Bolhuis, A.A.; Kok, J.J.; Venema, G.G. !$#submission submitted to the EMBL Data Library, April 1994 !$#description The sucrose and raffinose operons of Pediococcus pentosaceus !1PPE1.0. !$#accession S44259 !'##molecule_type DNA !'##residues 1-326 ##label LEE !'##cross-references EMBL:Z32771; NID:g493728; PIDN:CAA83670.1; !1PID:g475970 GENETICS !$#gene scrR CLASSIFICATION #superfamily lac repressor KEYWORDS DNA binding; transcription regulation SUMMARY #length 326 #molecular-weight 36207 #checksum 9069 SEQUENCE /// ENTRY S15318 #type complete TITLE transcription regulator for carbon catabolite control ccpA - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S15318; E69597 REFERENCE S15318 !$#authors Henkin, T.M.; Grundy, F.J.; Nicholson, W.L.; Chambliss, G.H. !$#journal Mol. Microbiol. (1991) 5:575-584 !$#title Catabolite repression of alpha-amylase gene expression in !1Bacillus subtilis involves a trans-acting gene product !1homologous to the Escherichia coli lacI and galR repressors. !$#cross-references MUID:91260441; PMID:1904524 !$#accession S15318 !'##status preliminary !'##molecule_type DNA !'##residues 1-334 ##label MOL !'##cross-references GB:AF008220; NID:g2293135; PIDN:AAC00299.1; !1PID:g2293221 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69597 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-334 ##label KUN !'##cross-references GB:Z99119; GB:AL009126; NID:g2635411; !1PIDN:CAB14952.1; PID:g2635458 !'##experimental_source strain 168 GENETICS !$#gene ccpA CLASSIFICATION #superfamily lac repressor KEYWORDS DNA binding; transcription regulation SUMMARY #length 334 #molecular-weight 36940 #checksum 1871 SEQUENCE /// ENTRY A32885 #type complete TITLE xylose operon repressor protein xylR - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A32885; E69735 REFERENCE A32885 !$#authors Kreuzer, P.; Gaertner, D.; Allmansberger, R.; Hillen, W. !$#journal J. Bacteriol. (1989) 171:3840-3845 !$#title Identification and sequence analysis of the Bacillus !1subtilis W23 xylR gene and xyl operator. !$#cross-references MUID:89291732; PMID:2544559 !$#accession A32885 !'##molecule_type DNA !'##residues 1-384 ##label KRE !'##cross-references GB:M27248; NID:g143840; PIDN:AAA22896.1; !1PID:g143841 !'##experimental_source strain W23 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69735 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 35-53,'SM',56-82,'V',84-92,'N',94-103,'V',105-107,'YR', !1110-132,'Q',134-140,'F',142-154,'D',156-173,'S',175-178,'Y', !1180-181,'S',183-197,'L',199-205,'D',207-210,'V',212-277,'L', !1279-284,'N',286-320,'V',322-337,'M',339-347,'S',349-362,'Q', !1364-375,'D',377-380,'MIT',384 ##label KUN !'##cross-references GB:Z99113; GB:AL009126; NID:g2634090; !1PIDN:CAB13643.1; PID:g2634143 !'##experimental_source strain 168 GENETICS !$#gene xylR !$#start_codon GTG CLASSIFICATION #superfamily xylose repressor; glucose kinase homology KEYWORDS DNA binding; transcription regulation FEATURE !$141-269 #domain glucose kinase homology #label GKH SUMMARY #length 384 #molecular-weight 42295 #checksum 6179 SEQUENCE /// ENTRY S16529 #type complete TITLE xylR protein - Staphylococcus xylosus ORGANISM #formal_name Staphylococcus xylosus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S16529 REFERENCE S16529 !$#authors Sizemore, C.; Buchner, E.; Rygus, T.; Witke, C.; Goetz, F.; !1Hillen, W. !$#journal Mol. Gen. Genet. (1991) 227:377-384 !$#title Organization, promoter analysis and transcriptional !1regulation of the Staphylococcus xylosus xylose utilization !1operon. !$#cross-references MUID:91326026; PMID:1714034 !$#accession S16529 !'##status preliminary !'##molecule_type DNA !'##residues 1-383 ##label SIZ !'##cross-references EMBL:X57599; NID:g48833; PIDN:CAA40823.1; !1PID:g48834 GENETICS !$#gene xylR CLASSIFICATION #superfamily xylose repressor; glucose kinase homology KEYWORDS DNA binding; transcription regulation FEATURE !$138-265 #domain glucose kinase homology #label GKH SUMMARY #length 383 #molecular-weight 43376 #checksum 3480 SEQUENCE /// ENTRY S41787 #type complete TITLE xylose repressor xylR - thermophilic bacterium RT8.B4 ORGANISM #formal_name thermophilic bacterium RT8.B4 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S41787 REFERENCE S41785 !$#authors Dwivedi, P.P.; Gibbs, M.D.; Bergquist, P.L. !$#submission submitted to the EMBL Data Library, October 1993 !$#description Cloning, sequencing and over expression of a multifunctional !1xylanase gene (xynA) from the thermophilic bacterium Rt8.B4 !1in Escherichia coli. !$#accession S41787 !'##molecule_type DNA !'##residues 1-399 ##label DWI !'##cross-references EMBL:L18965; NID:g311185; PIDN:AAB42043.1; !1PID:g311188 GENETICS !$#gene xylR CLASSIFICATION #superfamily xylose repressor; glucose kinase homology FEATURE !$140-269 #domain glucose kinase homology #label GKH SUMMARY #length 399 #molecular-weight 43725 #checksum 6497 SEQUENCE /// ENTRY B69632 #type complete TITLE glucose kinase glcK - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69632 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69632 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-321 ##label KUN !'##cross-references GB:Z99116; GB:AL009126; NID:g2634723; !1PIDN:CAB14416.1; PID:g2634919 !'##experimental_source strain 168 GENETICS !$#gene glcK CLASSIFICATION #superfamily glucose kinase; glucose kinase homology FEATURE !$64-194 #domain glucose kinase homology #label GKH SUMMARY #length 321 #molecular-weight 33545 #checksum 7790 SEQUENCE /// ENTRY S52352 #type complete TITLE glucose kinase - Staphylococcus xylosus ORGANISM #formal_name Staphylococcus xylosus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S52352 REFERENCE S52351 !$#authors Wagner, E. !$#submission submitted to the EMBL Data Library, February 1995 !$#accession S52352 !'##status preliminary !'##molecule_type DNA !'##residues 1-328 ##label WAG !'##cross-references EMBL:X84332; NID:g666114; PIDN:CAA59069.1; !1PID:g666116 CLASSIFICATION #superfamily glucose kinase; glucose kinase homology FEATURE !$66-197 #domain glucose kinase homology #label GKH SUMMARY #length 328 #molecular-weight 35032 #checksum 830 SEQUENCE /// ENTRY S26208 #type complete TITLE glucose kinase - Streptomyces coelicolor ORGANISM #formal_name Streptomyces coelicolor DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 12-Nov-1999 ACCESSIONS S26208; T35507; S21459 REFERENCE S26206 !$#authors Angell, S.; Schwarz, E.; Bibb, M.J. !$#journal Mol. Microbiol. (1992) 6:2833-2844 !$#title The glucose kinase gene of Streptomyces coelicolor A3(2): !1its nucleotide sequence, transcriptional analysis and role !1in glucose repression. !$#cross-references MUID:93062017; PMID:1435260 !$#accession S26208 !'##molecule_type DNA !'##residues 1-317 ##label ANG !'##cross-references EMBL:X65932; NID:g46848; PIDN:CAA46727.1; !1PID:g46851 REFERENCE Z21580 !$#authors Seeger, K.; Harris, D.; James, K.D.; Parkhill, J.; Barrell, !1B.G.; Rajandream, M.A. !$#submission submitted to the EMBL Data Library, August 1999 !$#accession T35507 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-317 ##label SEE !'##cross-references EMBL:AL109661; PIDN:CAB51974.1; GSPDB:GN00070; !1SCOEDB:glk !'##experimental_source strain A3(2) GENETICS !$#gene glk CLASSIFICATION #superfamily glucose kinase; glucose kinase homology FEATURE !$57-186 #domain glucose kinase homology #label GKH SUMMARY #length 317 #molecular-weight 33061 #checksum 24 SEQUENCE /// ENTRY S76053 #type complete TITLE hypothetical protein - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S76053 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76053 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-327 ##label KAN !'##cross-references EMBL:D63999; GB:AB001339; NID:g1001396; !1PIDN:BAA10031.1; PID:g1001409 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily glucose kinase; glucose kinase homology FEATURE !$86-216 #domain glucose kinase homology #label GKH SUMMARY #length 327 #molecular-weight 34607 #checksum 2453 SEQUENCE /// ENTRY S58290 #type complete TITLE invasion-associated protein - Renibacterium salmoninarum ORGANISM #formal_name Renibacterium salmoninarum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S58290 REFERENCE S58290 !$#authors Maulen, N.; Morales, P.; Aruti, D.; Figueroa, J.; Concha, !1M.; Krauskopf, M.; Leon, G. !$#submission submitted to the EMBL Data Library, July 1995 !$#description Identification of a Renibacterium salmoninarum DNA fragment !1associated with bacterial internalization into CHSE cultured !1cells. !$#accession S58290 !'##status preliminary !'##molecule_type DNA !'##residues 1-272 ##label MAU !'##cross-references EMBL:X89964 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily glucose kinase; glucose kinase homology FEATURE !$13-142 #domain glucose kinase homology #label GKH SUMMARY #length 272 #molecular-weight 28512 #checksum 5741 SEQUENCE /// ENTRY RPECIR #type complete TITLE acetate operon repressor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 14-Nov-1997 #text_change 01-Mar-2002 ACCESSIONS A65209; A35267; JQ0871 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65209 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-287 ##label BLAT !'##cross-references GB:AE000475; GB:U00096; NID:g1790448; !1PIDN:AAC76988.1; PID:g1790449; UWGP:b4018 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A35267 !$#authors Sunnarborg, A.; Klumpp, D.; Chung, T.; LaPorte, D.C. !$#journal J. Bacteriol. (1990) 172:2642-2649 !$#title Regulation of the glyoxylate bypass operon: cloning and !1characterization of iclR. !$#cross-references MUID:90236928; PMID:2185227 !$#accession A35267 !'##molecule_type DNA !'##residues 14-287 ##label SUN !'##cross-references GB:M31761; NID:g146437; PIDN:AAA24008.1; !1PID:g146438 REFERENCE JQ0871 !$#authors Negre, D.; Cortay, J.C.; Old, I.G.; Galinier, A.; Richaud, !1C.; Saint Girons, I.; Cozzone, A.J. !$#journal Gene (1991) 97:29-37 !$#title Overproduction and characterization of the iclR gene product !1of Escherichia coli K-12 and comparison with that of !1Salmonella typhimurium LT2. !$#cross-references MUID:91138983; PMID:1995431 !$#accession JQ0871 !'##molecule_type DNA !'##residues 14-287 ##label NEG !'##cross-references GB:M34937 COMMENT This repressor protein regulates expression of the enzymes !1of the glyoxylate bypass, a metabolic pathway induced by !1growing E. coli on acetate. GENETICS !$#gene iclR !$#map_position 91 min CLASSIFICATION #superfamily acetate operon repressor KEYWORDS DNA binding; transcription regulation SUMMARY #length 287 #molecular-weight 31258 #checksum 6636 SEQUENCE /// ENTRY JGECA #type complete TITLE L-arabinose-binding protein precursor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-May-1979 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS E64953; S03711; A92206; A03424 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64953 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-329 ##label BLAT !'##cross-references GB:AE000283; GB:U00096; NID:g1788200; !1PIDN:AAC74971.1; PID:g1788211; UWGP:b1901 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S01074 !$#authors Scripture, J.B.; Voelker, C.; Miller, S.; O'Donnell, R.T.; !1Polgar, L.; Rade, J.; Horazdovsky, B.F.; Hogg, R.W. !$#journal J. Mol. Biol. (1987) 197:37-46 !$#title High-affinity L-arabinose transport operon: nucleotide !1sequence and analysis of gene products. !$#cross-references MUID:88062741; PMID:2445996 !$#accession S03711 !'##molecule_type DNA !'##residues 1-193,'E',195-280,'L',282-329 ##label SCR !'##cross-references EMBL:X06091; NID:g40943; PIDN:CAA29476.1; !1PID:g40944 REFERENCE A92206 !$#authors Hogg, R.W.; Hermodson, M.A. !$#journal J. Biol. Chem. (1977) 252:5135-5141 !$#cross-references MUID:77207135; PMID:326784 !$#accession A92206 !'##molecule_type protein !'##residues 24-329 ##label HOG !'##experimental_source strain B/R REFERENCE A92207 !$#authors Quiocho, F.A.; Gilliland, G.L.; Phillips Jr., G.N. !$#journal J. Biol. Chem. (1977) 252:5142-5149 !$#title The 2.8-angstrom resolution structure of the !1L-arabinose-binding protein from Escherichia coli. !1Polypeptide chain folding, domain similarity, and probable !1location of sugar-binding site. !$#cross-references MUID:77207136; PMID:326785 !$#contents annotation; X-ray crystallography, 2.8 angstroms !$#note the binding site for the sugar molecule has not yet been !1established, but Cys-64 may be involved GENETICS !$#gene araF !$#map_position 45 min FUNCTION !$#description involved in the high-affinity L-arabinose membrane transport !1system. CLASSIFICATION #superfamily L-arabinose-binding protein KEYWORDS periplasmic space; sugar transport FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-329 #product L-arabinose-binding protein #status !8predicted #label MAT SUMMARY #length 329 #molecular-weight 35541 #checksum 5979 SEQUENCE /// ENTRY JGECG #type complete TITLE D-galactose-binding periplasmic protein precursor - Escherichia coli (strain K-12) ALTERNATE_NAMES mglB protein ORGANISM #formal_name Escherichia coli DATE 02-Apr-1982 #sequence_revision 18-Nov-1994 #text_change 01-Mar-2002 ACCESSIONS A37277; A92319; A94599; A30384; A32653; E64983; A03427; !1Q00294 REFERENCE A37277 !$#authors Hogg, R.W.; Voelker, C.; Von Carlowitz, I. !$#journal Mol. Gen. Genet. (1991) 229:453-459 !$#title Nucleotide sequence and analysis of the mgl operon of !1Escherichia coli K12. !$#cross-references MUID:92049246; PMID:1719366 !$#accession A37277 !'##molecule_type DNA !'##residues 1-332 ##label HOG !'##cross-references GB:M59444; NID:g146852; PIDN:AAA24169.1; !1PID:g146853 !'##experimental_source strain K12 REFERENCE A92319 !$#authors Mahoney, W.C.; Hogg, R.W.; Hermodson, M.A. !$#journal J. Biol. Chem. (1981) 256:4350-4356 !$#title The amino acid sequence of the D-galactose-binding protein !1from Escherichia coli B/r. !$#cross-references MUID:81168234; PMID:7012152 !$#accession A92319 !'##molecule_type protein !'##residues 24-178,'KE',181-332 ##label MA1 !'##experimental_source strain B/r !'##note this sequence revised in reference A94599 REFERENCE A94599 !$#authors Mahoney, W.C.; Hogg, R.W.; Hermodson, M.A. !$#submission submitted to the Atlas, November 1982 !$#contents revisions !$#accession A94599 !'##molecule_type protein !'##residues 24-332 ##label MA2 REFERENCE A30384 !$#authors Scholle, A.; Vreemann, J.; Blank, V.; Nold, A.; Boos, W.; !1Manson, M.D. !$#journal Mol. Gen. Genet. (1987) 208:247-253 !$#title Sequence of the mglB gene from Escherichia coli K12: !1comparison of wild-type and mutant galactose chemoreceptors. !$#cross-references MUID:87286407; PMID:3302609 !$#accession A30384 !'##molecule_type DNA !'##residues 1-15 ##label SCH REFERENCE A32653 !$#authors Scripture, J.B.; Hogg, R.W. !$#journal J. Biol. Chem. (1983) 258:10853-10855 !$#title The nucleotide sequences defining the signal peptides of the !1galactose-binding protein and the arabinose-binding protein. !$#cross-references MUID:83291030; PMID:6885805 !$#accession A32653 !'##molecule_type DNA !'##residues 1-15 ##label SCR REFERENCE A93942 !$#authors Vyas, N.K.; Vyas, M.N.; Quiocho, F.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:1792-1796 !$#title The 3 angstrom resolution structure of a D-galactose-binding !1protein for transport and chemotaxis in Escherichia coli. !$#cross-references MUID:83169767; PMID:6340108 !$#contents annotation; X-ray crystallography, 3.0 angstroms REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64983 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-332 ##label BLAT !'##cross-references GB:AE000304; GB:U00096; NID:g1788470; !1PIDN:AAC75211.1; PID:g1788473; UWGP:b2150 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene mglB; mglM !$#map_position 46 min CLASSIFICATION #superfamily D-galactose-binding protein KEYWORDS calcium binding; chemotaxis; periplasmic space; sugar !1transport FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-332 #product D-galactose-binding protein #status !8experimental #label MAT\ !$37,114,175,177,181, !$234,259,279 #binding_site galactose (Asp, Asn, His, Asp, Arg, !8Asn, Asp, Asn) #status experimental\ !$157,159,161,163, !$165,228 #binding_site calcium (Asp, Asn, Asp, Gln, Gln, Glu) !8#status experimental SUMMARY #length 332 #molecular-weight 35712 #checksum 5207 SEQUENCE /// ENTRY S15554 #type complete TITLE D-galactose-binding protein - Citrobacter freundii ORGANISM #formal_name Citrobacter freundii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S15554 REFERENCE S15554 !$#authors Galindo, R.L.; Dagget Garvin, L.; Hardies, S.C. !$#submission submitted to the EMBL Data Library, May 1991 !$#accession S15554 !'##status preliminary !'##molecule_type DNA !'##residues 1-332 ##label GAL !'##cross-references EMBL:X59389; NID:g40472; PIDN:CAA42032.1; !1PID:g40473 GENETICS !$#gene mglB CLASSIFICATION #superfamily D-galactose-binding protein KEYWORDS calcium binding; chemotaxis; periplasmic space; sugar !1transport FEATURE !$37,114,175,177,181, !$234,259,279 #binding_site galactose (Asp, Asn, His, Asp, Arg, !8Asn, Asp, Asn) #status predicted SUMMARY #length 332 #molecular-weight 35817 #checksum 4462 SEQUENCE /// ENTRY S29390 #type complete TITLE galactose-binding protein - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S29390 REFERENCE S29389 !$#authors Benner-Luger, D.; Boos, W. !$#journal Mol. Gen. Genet. (1988) 214:579-587 !$#title The mglB sequence of Salmonella typhimurium LT2; promoter !1analysis by gene fusions and evidence for a divergently !1oriented gene coding for the mgl repressor. !$#cross-references MUID:89112167; PMID:3146019 !$#accession S29390 !'##status preliminary !'##molecule_type DNA !'##residues 1-332 ##label BEN CLASSIFICATION #superfamily D-galactose-binding protein SUMMARY #length 332 #molecular-weight 35747 #checksum 8669 SEQUENCE /// ENTRY G64096 #type complete TITLE D-galactose-binding protein - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS G64096 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession G64096 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-349 ##label TIGR !'##cross-references GB:U32764; GB:L42023; NID:g1573827; !1PIDN:AAC22481.1; PID:g1573835; TIGR:HI0822 CLASSIFICATION #superfamily D-galactose-binding protein KEYWORDS calcium binding; chemotaxis; periplasmic space; sugar !1transport FEATURE !$56,133,194,196,200, !$253,277,297 #binding_site galactose (Asp, Asn, His, Asp, Arg, !8Asn, Asp, Asn) #status predicted SUMMARY #length 349 #molecular-weight 37603 #checksum 9055 SEQUENCE /// ENTRY JGECM #type complete TITLE periplasmic maltose-binding protein precursor - Escherichia coli (strain K-12) ALTERNATE_NAMES maltose binding protein 16-1 ORGANISM #formal_name Escherichia coli DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 01-Mar-2002 ACCESSIONS A03428; I54874; A65211; I54911 REFERENCE A03428 !$#authors Duplay, P.; Bedouelle, H.; Fowler, A.; Zabin, I.; Saurin, !1W.; Hofnung, M. !$#journal J. Biol. Chem. (1984) 259:10606-10613 !$#title Sequences of the malE gene and of its product, the !1maltose-binding protein of Escherichia coli K12. !$#cross-references MUID:84289460; PMID:6088507 !$#accession A03428 !'##molecule_type DNA !'##residues 1-396 ##label DUP !'##cross-references GB:J01648; GB:J01639; GB:K02117; GB:M24344; !1GB:M24345; NID:g146697; PIDN:AAB59056.1; PID:g457109 !'##experimental_source strain K12 !'##note most of the primary structure was confirmed by protein !1sequencing REFERENCE I54874 !$#authors Cover, W.H.; Ryan, J.P.; Bassford, P.J. !$#journal J. Bacteriol. (1987) 169:1794-1800 !$#title Suppresion of a signal sequence mutation by an amino acid !1substitution in the mature portion of the maltose-binding !1protein. !$#cross-references MUID:87194547; PMID:3553148 !$#accession I54874 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-28 ##label RES !'##cross-references GB:M16181; NID:g146704; PIDN:AAA24102.1; !1PID:g146705 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65211 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-396 ##label BLAT !'##cross-references GB:AE000476; GB:U00096; NID:g1790456; !1PIDN:AAC77004.1; PID:g1790466; UWGP:b4034 !'##experimental_source strain K-12, substrain MG1655 REFERENCE I54911 !$#authors Collier, D.N.; Bassford, P.J. !$#journal J. Bacteriol. (1989) 171:4640-4647 !$#title Mutations that improve export of maltose-binding protein in !1SecB- cells of Escherichia coli. !$#cross-references MUID:89359092; PMID:2670890 !$#accession I54911 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-15,'K',17-29 ##label RE2 !'##cross-references GB:M29860; NID:g146885; PIDN:AAA24179.1; !1PID:g146886 COMMENT This periplasmic binding protein is involved in the !1high-affinity maltose membrane transport system. GENETICS !$#gene malE !$#map_position 92 min CLASSIFICATION #superfamily maltose-binding protein KEYWORDS periplasmic space; sugar transport FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-396 #product maltose-binding protein #status experimental !8#label MAT SUMMARY #length 396 #molecular-weight 43387 #checksum 7912 SEQUENCE /// ENTRY JGECGP #type complete TITLE glycerol-3-phosphate-binding protein precursor - Escherichia coli (strain K-12) ALTERNATE_NAMES ugpB protein ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS S47672; H65141; S03780 REFERENCE S47666 !$#authors Plunkett, G. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S47672 !'##molecule_type DNA !'##residues 1-438 ##label PLU !'##cross-references EMBL:U00039; NID:g466582; PIDN:AAB18428.1; !1PID:g466589 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65141 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-438 ##label BLAT !'##cross-references GB:AE000421; GB:U00096; NID:g1789854; !1PIDN:AAC76478.1; PID:g1789862; UWGP:b3453 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S03780 !$#authors Overduin, P.; Boos, W.; Tommassen, J. !$#journal Mol. Microbiol. (1988) 2:767-775 !$#title Nucleotide sequence of the ugp genes of Escherichia coli !1K-12: homology to the maltose system. !$#cross-references MUID:89096498; PMID:3062310 !$#accession S03780 !'##molecule_type DNA !'##residues 1-333,'T',335-438 ##label OVE !'##cross-references EMBL:X13141; NID:g43243; PIDN:CAA31531.1; !1PID:g43244 COMMENT This is the periplasmic binding protein component of a !1phosphate limitation-induced transport system for !1glycerol-3-phosphate and glycerophosphoryl diesters. GENETICS !$#gene ugpB !$#map_position 76 min CLASSIFICATION #superfamily glycerol-3-phosphate-binding protein KEYWORDS binding protein-dependent transport system; !1glycerol-3-phosphate transport FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-438 #product glycerol-3-phosphate-binding protein #status !8predicted #label MAT SUMMARY #length 438 #molecular-weight 48448 #checksum 7013 SEQUENCE /// ENTRY JGAGLR #type complete TITLE lactose-binding protein precursor - Agrobacterium radiobacter ORGANISM #formal_name Agrobacterium radiobacter DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS S25247; S22739 REFERENCE S25247 !$#authors Williams, S.G.; Greenwood, J.A.; Jones, C.W. !$#journal Mol. Microbiol. (1992) 6:1755-1768 !$#title Molecular analysis of the lac operon encoding the !1binding-protein-dependent lactose transport system and !1beta-galactosidase in Agrobacterium radiobacter. !$#cross-references MUID:92334152; PMID:1630315 !$#accession S25247 !'##molecule_type DNA !'##residues 1-422 ##label WIL !'##cross-references EMBL:X66596; NID:g38967; PIDN:CAA47161.1; !1PID:g38968 GENETICS !$#gene lacE CLASSIFICATION #superfamily glycerol-3-phosphate-binding protein KEYWORDS binding protein-dependent transport system; lactose !1transport; membrane protein FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-422 #product lactose-binding protein #status predicted !8#label MAT SUMMARY #length 422 #molecular-weight 45903 #checksum 5428 SEQUENCE /// ENTRY A69956 #type complete TITLE phosphate ABC transporter (binding protein) homolog yqgG - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A69956 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69956 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-300 ##label KUN !'##cross-references GB:Z99116; GB:AL009126; NID:g2634723; !1PIDN:CAB14429.1; PID:g2634932 !'##experimental_source strain 168 GENETICS !$#gene yqgG CLASSIFICATION #superfamily Methanobacterium phosphate-binding protein pstS SUMMARY #length 300 #molecular-weight 31684 #checksum 3003 SEQUENCE /// ENTRY S75769 #type complete TITLE hypothetical protein sll0540 - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S75769 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75769 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-307 ##label KAN !'##cross-references EMBL:D64003; GB:AB001339; NID:g1001200; !1PIDN:BAA10504.1; PID:g1001260 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily Methanobacterium phosphate-binding protein pstS SUMMARY #length 307 #molecular-weight 32534 #checksum 5409 SEQUENCE /// ENTRY G70126 #type complete TITLE phosphate ABC transporter, periplasmic phosphate-binding protein (pstS) homolog - Lyme disease spirochete ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS G70126 REFERENCE A70100 !$#authors Fraser, C.M.; Casjens, S.; Huang, W.M.; Sutton, G.G.; !1Clayton, R.; Lathigra, R.; White, O.; Ketchum, K.A.; Dodson, !1R.; Hickey, E.K.; Gwinn, M.; Dougherty, B.; Tomb, J.F.; !1Fleischmann, R.D.; Richardson, D.; Peterson, J.; Kerlavage, !1A.R.; Quackenbush, J.; Salzberg, S.; Hanson, M.; Vugt, R.V.; !1Palmer, N.; Adams, M.D.; Gocayne, J.; Weidman, J.; !1Utterback, T.; Watthey, L.; McDonald, L.; Artiach, P.; !1Bowman, C.; Garland, S.; Fujii, C.; Cotton, M.D.; Horst, K.; !1Roberts, K.; Hatch, B.; Smith, H.O.; Venter, J.C. !$#journal Nature (1997) 390:580-586 !$#title Genomic sequence of a Lyme disease spirochaete, Borrelia !1burgdorferi. !$#cross-references MUID:98065943; PMID:9403685 !$#accession G70126 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-280 ##label KLE !'##cross-references GB:AE001132; GB:AE000783; NID:g2688107; !1PIDN:AAC66609.1; PID:g2688115; TIGR:BB0215 !'##experimental_source strain B31 CLASSIFICATION #superfamily Methanobacterium phosphate-binding protein pstS SUMMARY #length 280 #molecular-weight 31249 #checksum 1660 SEQUENCE /// ENTRY BVEC #type complete TITLE tonB protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 14-Nov-1983 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS G64872; A03429 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64872 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-239 ##label BLAT !'##cross-references GB:AE000223; GB:U00096; NID:g1787496; !1PIDN:AAC74334.1; PID:g1787505; UWGP:b1252 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A03429 !$#authors Postle, K.; Good, R.F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:5235-5239 !$#title DNA sequence of the Escherichia coli tonB gene. !$#cross-references MUID:83299947; PMID:6310567 !$#accession A03429 !'##molecule_type DNA !'##residues 'MIMTS',1-239 ##label POS !'##cross-references GB:K00431; NID:g148022; PIDN:AAB59066.1; !1PID:g148023 !'##note the authors translated the codons GAT, AAT, and GGT for !1residues 113, 159, and 186 as Gln, Asp, and Glu, !1respectively GENETICS !$#gene tonB; exbA !$#map_position 28 min FUNCTION !$#description essential for high-affinity iron transport systems, for the !1energy-dependent phase of vitamin B-12 transport, and in the !1energy-dependent, irreversible steps of bacteriophages !1phi-80 and T1 infection !$#note interaction with the ExbBD proteins CLASSIFICATION #superfamily tonB protein KEYWORDS iron transport; periplasmic space FEATURE !$1-32 #domain membrane-anchoring #status predicted #label !8MAC SUMMARY #length 239 #molecular-weight 26094 #checksum 6662 SEQUENCE /// ENTRY BVECES #type complete TITLE enterochelin esterase (EC 3.1.-.-) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 01-Mar-2002 ACCESSIONS A31958; G64791 REFERENCE A31958 !$#authors Pettis, G.S.; Brickman, T.J.; McIntosh, M.A. !$#journal J. Biol. Chem. (1988) 263:18857-18863 !$#title Transcriptional mapping and nucleotide sequence of the !1Escherichia coli fepA-fes enterobactin region. !1Identification of a unique iron-regulated bidirectional !1promoter. !$#cross-references MUID:89066678; PMID:2974033 !$#accession A31958 !'##molecule_type DNA !'##residues 1-374 ##label PET !'##cross-references GB:J04216; NID:g145916; PIDN:AAA23757.1; !1PID:g145918 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64791 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-374 ##label BLAT !'##cross-references GB:AE000163; GB:U00096; NID:g1786790; !1PIDN:AAC73686.1; PID:g1786799; UWGP:b0585 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene fes !$#map_position 14 min FUNCTION !$#description enterochelin esterase is required for hydrolysis of !1ferrienterobactin and for the release of iron for metabolic !1use CLASSIFICATION #superfamily fes protein KEYWORDS hydrolase SUMMARY #length 374 #molecular-weight 42569 #checksum 343 SEQUENCE /// ENTRY BVECCA #type complete TITLE preprotein translocase secA - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1988 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS B64732; A31088; S40608; C28381 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64732 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-901 ##label BLAT !'##cross-references GB:AE000119; GB:U00096; NID:g1786283; !1PIDN:AAC73209.1; PID:g1786287; UWGP:b0098 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A31088 !$#authors Schmidt, M.G.; Rollo, E.E.; Grodberg, J.; Oliver, D.B. !$#journal J. Bacteriol. (1988) 170:3404-3414 !$#title Nucleotide sequence of the secA gene and secA(Ts) mutations !1preventing protein export in Escherichia coli. !$#cross-references MUID:88298644; PMID:2841285 !$#accession A31088 !'##molecule_type DNA !'##residues 1-736,'DG',739-901 ##label SCH !'##cross-references GB:X55034; GB:M10429; NID:g40841; PIDN:CAA38875.1; !1PID:g40866 REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40608 !'##status preliminary !'##molecule_type DNA !'##residues 1-736,'DG',739-901 ##label YUR !'##cross-references EMBL:D10483; NID:g216434; PIDN:BAA01363.1; !1PID:g216512 REFERENCE A91852 !$#authors Beall, B.; Lutkenhaus, J. !$#journal J. Bacteriol. (1987) 169:5408-5415 !$#title Sequence analysis, transcriptional organization, and !1insertional mutagenesis of the envA gene of Escherichia !1coli. !$#cross-references MUID:88058745; PMID:2824434 !$#accession C28381 !'##molecule_type DNA !'##residues 1-67 ##label BEA !'##cross-references GB:M19211; NID:g145846; PIDN:AAA83851.1; !1PID:g551802 REFERENCE A58822 !$#authors Park, S.K.; Kim, D.W.; Choe, J.; Kim, H. !$#journal Biochem. Biophys. Res. Commun. (1997) 235:593-597 !$#title RNA helicase activity of Escherichia coli SecA protein. !$#cross-references MUID:97350826; PMID:9207202 !$#contents annotation !$#note disscussion of helicase activity COMMENT The "nucleotide-binding motif B" and "DEAD motif" features !1as annotated are consistant with what has been identified in !1the literature. However, an equaly good, and better !1conserved motif is adjacent to the identified motif and a !1third conserved motif is approximatly 120-140 residues !1closer to the C-terminus and closer to the TAT motif !1associated with helicase activity. GENETICS !$#gene secA !$#map_position 2 min FUNCTION PPS !$#description involved in the secretion process of envelope proteins FUNCTION HEL !$#description RNA helicase activity CLASSIFICATION #superfamily preprotein translocase secA KEYWORDS ATP; membrane-associated complex; P-loop; protein export FEATURE !$102-109 #region nucleotide-binding motif A (P-loop) #status !8atypical\ !$205-210 #region nucleotide-binding motif B\ !$209-212 #region DEAD motif SUMMARY #length 901 #molecular-weight 102022 #checksum 3606 SEQUENCE /// ENTRY QRSEUA #type complete TITLE sfuA protein precursor - Serratia marcescens ORGANISM #formal_name Serratia marcescens DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS A35108 REFERENCE A35108 !$#authors Angerer, A.; Gaisser, S.; Braun, V. !$#journal J. Bacteriol. (1990) 172:572-578 !$#title Nucleotide sequences of the sfuA, sfuB, and sfuC genes of !1Serratia marcescens suggest a !1periplasmic-binding-protein-dependent iron transport !1mechanism. !$#cross-references MUID:90130288; PMID:2404942 !$#accession A35108 !'##molecule_type DNA !'##residues 1-338 ##label ANG !'##cross-references GB:M33815; NID:g152859; PIDN:AAA26573.1; !1PID:g152860 COMMENT The mature protein can be further processed to smaller a !1peptide. This periplasmic protein is involved in an unusual !1periplasmic binding-protein-dependent iron transport system, !1which is independent of tonB, exbB, siderophore, or any !1outer membrane protein. GENETICS !$#gene sfuA CLASSIFICATION #superfamily sfuA protein KEYWORDS binding protein-dependent transport system; iron transport; !1membrane protein FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-338 #product sfuA protein #status predicted #label MAT SUMMARY #length 338 #molecular-weight 36157 #checksum 5172 SEQUENCE /// ENTRY IJYMAP #type complete TITLE adhesin P1 precursor - Mycoplasma pneumoniae ALTERNATE_NAMES cytadhesin P1; hypothetical protein 116a ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 31-Mar-1989 #sequence_revision 30-Sep-1991 #text_change 07-Dec-1999 ACCESSIONS S03725; A38791; JT0288; S04516; S62807; S73339; A60102; !1A27597; PL0008 REFERENCE S03725 !$#authors Su, C.J.; Tryon, V.V.; Baseman, J.B. !$#journal Infect. Immun. (1987) 55:3023-3029 !$#title Cloning and sequence analysis of cytadhesin P1 gene from !1Mycoplasma pneumoniae. !$#cross-references MUID:88057593; PMID:3119495 !$#accession S03725 !'##molecule_type DNA !'##residues 1-1627 ##label SU1 !'##cross-references EMBL:M18639; NID:g150166; PIDN:AAA25424.1; !1PID:g150167 !'##experimental_source strain M129-B16 !$#accession A38791 !'##molecule_type protein !'##residues 60-77 ##label SU2 !'##note it is uncertain whether Met-1 is the initiator or whether !1translation is initiated at 31-Val (GTG) REFERENCE JT0288 !$#authors Inamine, J.M.; Denny, T.P.; Loechel, S.; Schaper, U.; Huang, !1C.H.; Bott, K.F.; Hu, P.C. !$#journal Gene (1988) 64:217-229 !$#title Nucleotide sequence of the P 1 attachment-protein gene of !1Mycoplasma pneumoniae. !$#cross-references MUID:88297153; PMID:2841195 !$#accession JT0288 !'##molecule_type DNA !'##residues 1-1627 ##label INA !'##cross-references GB:M21519; NID:g150138; PIDN:AAA88325.1; !1PID:g150139 !'##experimental_source strain M-129, ATCC 29342 REFERENCE S04516 !$#authors Wenzel, R.; Herrmann, R. !$#journal Nucleic Acids Res. (1988) 16:8337-8350 !$#title Repetitive DNA sequences in Mycoplasma pneumoniae. !$#cross-references MUID:88335593; PMID:3138660 !$#accession S04516 !'##status translation not shown !'##molecule_type DNA !'##residues 1187-1413 ##label WEN !'##cross-references EMBL:X13087 REFERENCE S62797 !$#authors Hilbert, H.; Himmelreich, R.; Plagens, H.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:628-639 !$#title Sequence analysis of 56 kb from the genome of the bacterium !1Mycoplasma pneumoniae comprising the dnaA region, the atp !1operon and a cluster of ribosomal protein genes. !$#cross-references MUID:96177562; PMID:8604303 !$#accession S62807 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 'MQVMRRSAPSFGP',1156-1199,'GAT',1203-1253,'VRRRS' ##label !1HIL !'##cross-references EMBL:U34795; NID:g1215683; PIDN:AAC43678.1; !1PID:g1215685 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1995 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73339 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1627 ##label HIM !'##cross-references EMBL:AE000002; GB:U00089; NID:g1673651; !1PIDN:AAB95661.1; PID:g1673659 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 REFERENCE A60102 !$#authors Jacobs, E.; Gerstenecker, B.; Mader, B.; Huang, C.H.; Hu, !1P.C.; Halter, R.; Bredt, W. !$#journal Infect. Immun. (1989) 57:685-688 !$#title Binding sites of attachment-inhibiting monoclonal antibodies !1and antibodies from patients on peptide fragments of the !1Mycoplasma pneumoniae adhesin. !$#cross-references MUID:89138634; PMID:2465270 !$#accession A60102 !'##molecule_type protein !'##residues 237-246;702-708 ##label JAC COMMENT The protein is the major adhesin mediating the attachment of !1the mycoplasma to respiratory epithelium. GENETICS !$#gene P1 !$#genetic_code SGC3 CLASSIFICATION #superfamily adhesin P1 KEYWORDS cell adhesion; membrane protein FEATURE !$1-59 #domain signal sequence #status predicted #label SIG\ !$60-1627 #product adhesin P1 #status experimental #label MAT SUMMARY #length 1627 #molecular-weight 176269 #checksum 9273 SEQUENCE /// ENTRY A30588 #type complete TITLE 140K adhesin precursor - Mycoplasma genitalium ALTERNATE_NAMES attachment protein MgPa ORGANISM #formal_name Mycoplasma genitalium DATE 08-Jun-1989 #sequence_revision 01-Dec-1995 #text_change 20-Apr-2001 ACCESSIONS A30588; JQ0090; B64221; A61605; S18721 REFERENCE A30588 !$#authors Dallo, S.F.; Chavoya, A.; Su, C.J.; Baseman, J.B. !$#journal Infect. Immun. (1989) 57:1059-1065 !$#title DNA and protein sequence homologies between the adhesins of !1Mycoplasma genitalium and Mycoplasma pneumoniae. !$#cross-references MUID:89173298; PMID:2925238 !$#accession A30588 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-1444 ##label DAL REFERENCE JQ0090 !$#authors Inamine, J.M.; Loechel, S.; Collier, A.M.; Barile, M.F.; Hu, !1P.C. !$#journal Gene (1989) 82:259-267 !$#title Nucleotide sequence of the MgPa (mgp) operon of Mycoplasma !1genitalium and comparison to the P1 (mpp) operon of !1Mycoplasma pneumoniae. !$#cross-references MUID:90060815; PMID:2583522 !$#accession JQ0090 !'##molecule_type DNA !'##residues 1-1444 ##label INA !'##cross-references GB:M31431; NID:g150157; PIDN:AAA25420.1; !1PID:g150159 !'##experimental_source strain G-37 (ATCC 33530) REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession B64221 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-1444 ##label TIGR !'##cross-references GB:U39696; GB:L43967; NID:g1045869; PID:g1045876; !1TIGR:MG191 !'##experimental_source strain G-37 REFERENCE A61605 !$#authors Mader, B.; Hu, P.C.; Huang, C.H.; Schilz, E.; Jacobs, E. !$#journal Zentralbl. Bakteriol. (1991) 274:507-513 !$#title The mature MgPa-adhesin of mycoplasma genitalium. !$#cross-references MUID:91321682; PMID:1863319 !$#accession A61605 !'##molecule_type protein !'##residues 59-68 ##label MAD REFERENCE S18693 !$#authors Peterson, S.N.; Schramm, N.; Hu, P.; Bott, K.F.; Hutchison !1III, C.A. !$#journal Nucleic Acids Res. (1991) 19:6027-6031 !$#title A random sequencing approach for placing markers on the !1physical map of Mycoplasma genitalium. !$#cross-references MUID:92051396; PMID:1945886 !$#accession S18721 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 106-176 ##label PET !'##cross-references EMBL:X61522 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1September 1991 GENETICS !$#gene MgPa !$#genetic_code SGC3 FUNCTION !$#description this protein plays an important role in the attachment of !1the respective organism to natural target cells CLASSIFICATION #superfamily adhesin P1 KEYWORDS membrane protein FEATURE !$59-1444 #product 140K adhesin #status experimental #label MAT SUMMARY #length 1444 #molecular-weight 159650 #checksum 4632 SEQUENCE /// ENTRY MMLYAZ #type complete TITLE outer surface protein A precursor - Lyme disease spirochete ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jul-1999 ACCESSIONS S14906; A61408; S06694 REFERENCE S14906 !$#authors Wallich, R.; Schaible, U.E.; Simon, M.M.; Heiberger, A.; !1Kramer, M.D. !$#journal Nucleic Acids Res. (1989) 17:8864 !$#title Cloning and sequencing of the gene encoding the outer !1surface protein A (OspA) of a European Borrelia burgdorferi !1isolate. !$#cross-references MUID:90067859; PMID:2587225 !$#accession S14906 !'##molecule_type DNA !'##residues 1-273 ##label WAL !'##cross-references EMBL:X16467; NID:g39381; PIDN:CAA34487.1; !1PID:g39382 !'##experimental_source strain ZS7 REFERENCE A61408 !$#authors Simon, M.M.; Schaible, U.E.; Kramer, M.D.; Eckerskorn, C.; !1Museteanu, C.; Mueller-Hermelink, H.K.; Wallich, R. !$#journal J. Infect. Dis. (1991) 164:123-132 !$#title Recombinant outer surface protein A from Borrelia !1burgdorferi induces antibodies protective against !1spirochetal infection in mice. !$#cross-references MUID:91277462; PMID:1829104 !$#accession A61408 !'##status preliminary !'##molecule_type protein !'##residues 118-135 ##label SIM GENETICS !$#gene ospA CLASSIFICATION #superfamily outer surface protein A KEYWORDS blocked amino end; lipoprotein; membrane protein FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-273 #product outer surface protein A #status predicted !8#label MAT\ !$17 #binding_site sn-2,3-diacylglycerol (Cys) (covalent) !8#status predicted\ !$17 #modified_site fatty acylated amino end (Cys) (in !8mature form) #status predicted SUMMARY #length 273 #molecular-weight 29455 #checksum 5886 SEQUENCE /// ENTRY A46460 #type complete TITLE outer surface protein A precursor - Lyme disease spirochete (strain 25015) ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 18-Jun-1993 #sequence_revision 02-Jun-1994 #text_change 16-Jul-1999 ACCESSIONS A46460 REFERENCE A46460 !$#authors Fikrig, E.; Barthold, S.W.; Persing, D.H.; Sun, X.; Kantor, !1F.S.; Flavell, R.A. !$#journal J. Immunol. (1992) 148:2256-2260 !$#title Borrelia burgdorferi strain 25015: characterization of outer !1surface protein A and vaccination against infection. !$#cross-references MUID:92185237; PMID:1545130 !$#accession A46460 !'##molecule_type DNA !'##residues 1-273 ##label FIK !'##cross-references GB:S88693; NID:g247092; PIDN:AAB21761.1; !1PID:g247093 !'##experimental_source strain 25015 !'##note sequence extracted from NCBI backbone (NCBIN:88693, !1NCBIP:88694) GENETICS !$#gene ospA CLASSIFICATION #superfamily outer surface protein A KEYWORDS blocked amino end; lipoprotein; membrane protein FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-273 #product outer surface protein A #status predicted !8#label MAT\ !$17 #binding_site sn-2,3-diacylglycerol (Cys) (covalent) !8#status predicted\ !$17 #modified_site fatty acylated amino end (Cys) (in !8mature form) #status predicted SUMMARY #length 273 #molecular-weight 29448 #checksum 5476 SEQUENCE /// ENTRY MMBY7C #type complete TITLE probable membrane protein YCR037c - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YCR524 ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jun-2000 ACCESSIONS S12919; S19449 REFERENCE S12916 !$#authors Thierry, A.; Fairhead, C.; Dujon, B. !$#journal Yeast (1990) 6:521-534 !$#title The complete sequence of the 8.2 kb segment left of MAT on !1chromosome III reveals five ORFs, including a gene for a !1yeast ribokinase. !$#cross-references MUID:91181345; PMID:1964349 !$#accession S12919 !'##molecule_type DNA !'##residues 1-923 ##label THI !'##cross-references EMBL:X56909; NID:g4489; PIDN:CAA40229.1; PID:g4493 REFERENCE S19445 !$#authors Herbert, C.J.; Jia, Y.; Slonimski, P.P. !$#submission submitted to the Protein Sequence Database, March 1992 !$#accession S19449 !'##molecule_type DNA !'##residues 1-923 ##label DUJ !'##cross-references EMBL:X59720; NID:g1907116; PIDN:CAA42304.1; !1PID:g1907179; GSPDB:GN00003; MIPS:YCR037c GENETICS !$#gene SGD:PHO87; MIPS:YCR037c !'##cross-references SGD:S0000633; MIPS:YCR037c !$#map_position 3R CLASSIFICATION #superfamily probable membrane protein YCR037C KEYWORDS transmembrane protein FEATURE !$458-479 #domain transmembrane #status predicted #label TM1\ !$501-518 #domain transmembrane #status predicted #label TM2\ !$538-554 #domain transmembrane #status predicted #label TM3\ !$583-603 #domain transmembrane #status predicted #label TM4\ !$628-644 #domain transmembrane #status predicted #label TM5\ !$675-694 #domain transmembrane #status predicted #label TM6\ !$708-732 #domain transmembrane #status predicted #label TM7\ !$739-759 #domain transmembrane #status predicted #label TM8\ !$766-784 #domain transmembrane #status predicted #label TM9\ !$799-836 #domain transmembrane #status predicted #label TM10\ !$846-868 #domain transmembrane #status predicted #label TM11\ !$891-919 #domain transmembrane #status predicted #label TM12 SUMMARY #length 923 #molecular-weight 102549 #checksum 858 SEQUENCE /// ENTRY BWDOP8 #type complete TITLE development-specific membrane protein P8A7 - slime mold (Dictyostelium discoideum) ORGANISM #formal_name Dictyostelium discoideum DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jul-1999 ACCESSIONS S14689; A27673; S12794 REFERENCE S14689 !$#authors Maniak, M.; Nellen, W. !$#journal Nucleic Acids Res. (1990) 18:3211-3217 !$#title Two separable promoters control different aspects of !1expression of a Dictyostelium gene. !$#cross-references MUID:90287695; PMID:2356118 !$#accession S14689 !'##molecule_type DNA !'##residues 1-138 ##label MAN1 !'##cross-references EMBL:X51947; NID:g7309; PIDN:CAA36209.1; !1PID:g295732 REFERENCE A27673 !$#authors Maniak, M.; Nellen, W. !$#journal Mol. Cell. Biol. (1988) 8:153-159 !$#title A developmentally regulated membrane protein gene in !1Dictyostelium discoideum is also induced by heat shock and !1cold shock. !$#cross-references MUID:88094381; PMID:3336356 !$#accession A27673 !'##molecule_type mRNA !'##residues 1-138 ##label MAN2 !'##cross-references GB:M19416; NID:g167830; PIDN:AAA33225.1; !1PID:g167831 GENETICS !$#gene P8A7 !$#introns 83/2 CLASSIFICATION #superfamily development-specific membrane protein P8A7 KEYWORDS membrane protein SUMMARY #length 138 #molecular-weight 15056 #checksum 156 SEQUENCE /// ENTRY S67566 #type complete TITLE probable membrane protein YDL033c - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein D2761 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S67566 REFERENCE S67560 !$#authors Paulin, L.; Saren, A.M.; Laamanen, P. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67566 !'##molecule_type DNA !'##residues 1-417 ##label PAU !'##cross-references EMBL:Z74081; NID:g1431011; PIDN:CAA98591.1; !1PID:g1431012; GSPDB:GN00004; MIPS:YDL033c !'##experimental_source strain S288C GENETICS !$#gene MIPS:YDL033c !'##cross-references SGD:S0002191 !$#map_position 4L CLASSIFICATION #superfamily probable membrane protein YDL033c KEYWORDS transmembrane protein FEATURE !$29-45 #domain transmembrane #status predicted #label TMM SUMMARY #length 417 #molecular-weight 47049 #checksum 8415 SEQUENCE /// ENTRY S73745 #type complete TITLE hypothetical protein A05_orf370 - Mycoplasma pneumoniae (strain ATCC 29342) ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Dec-1999 ACCESSIONS S73745 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73745 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-370 ##label HIM !'##cross-references EMBL:AE000040; GB:U00089; NID:g1674091; !1PIDN:AAB96067.1; PID:g1674103 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily probable membrane protein YDL033c SUMMARY #length 370 #molecular-weight 41773 #checksum 50 SEQUENCE /// ENTRY F64232 #type complete TITLE hypothetical protein homolog MG295 - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 07-Dec-1999 ACCESSIONS F64232 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession F64232 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-367 ##label TIGR !'##cross-references GB:U39710; GB:L43967; NID:g1045989; PID:g1045993; !1TIGR:MG295 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily probable membrane protein YDL033c SUMMARY #length 367 #molecular-weight 41887 #checksum 8491 SEQUENCE /// ENTRY D64144 #type complete TITLE probable ATPase HI0174 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS D64144 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession D64144 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-418 ##label TIGR !'##cross-references GB:U32702; GB:L42023; NID:g1573118; !1PIDN:AAC21843.1; PID:g1573129; TIGR:HI0174 CLASSIFICATION #superfamily probable membrane protein YDL033c SUMMARY #length 418 #molecular-weight 46957 #checksum 8682 SEQUENCE /// ENTRY S74846 #type complete TITLE hypothetical protein sll0844 - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S74846 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74846 !'##status preliminary !'##molecule_type DNA !'##residues 1-358 ##label KAN !'##cross-references EMBL:D90909; GB:AB001339; NID:g1652844; !1PIDN:BAA17807.1; PID:g1652889 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily probable membrane protein YDL033c SUMMARY #length 358 #molecular-weight 39096 #checksum 5079 SEQUENCE /// ENTRY BVECAD #type complete TITLE membrane protein traD - Escherichia coli plasmid F ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 28-May-1999 ACCESSIONS JS0293; S01758 REFERENCE JS0293 !$#authors Jalajakumari, M.B.; Manning, P.A. !$#journal Gene (1989) 81:195-202 !$#title Nucleotide sequence of the traD region in the Escherichia !1coli F sex factor. !$#cross-references MUID:90034191; PMID:2680768 !$#accession JS0293 !'##molecule_type DNA !'##residues 1-716 ##label JAL !'##cross-references GB:M29254; NID:g148618; PIDN:AAA83928.1; !1PID:g148620 !'##experimental_source strain K12 REFERENCE S01756 !$#authors Jalajakumari, M.B.; Guidolin, A.; Buhk, H.J.; Manning, P.A.; !1Ham, L.M.; Hodgson, A.L.M.; Cheah, K.C.; Skurray, R.A. !$#journal J. Mol. Biol. (1987) 198:1-11 !$#title Surface exclusion genes traS and traT of the F sex factor of !1Escherichia coli K-12. Determination of the nucleotide !1sequence and promoter and terminator activities. !$#cross-references MUID:88118903; PMID:3323526 !$#accession S01758 !'##molecule_type DNA !'##residues 8-34 ##label JA2 !'##cross-references EMBL:X06915 GENETICS !$#gene traD !$#genome plasmid FUNCTION !$#description this cytoplasmic membrane protein is one of the proteins !1that control the transfer of F plasmid. CLASSIFICATION #superfamily membrane protein traD KEYWORDS F pilin formation; transmembrane protein SUMMARY #length 716 #molecular-weight 81366 #checksum 6312 SEQUENCE /// ENTRY A43829 #type complete TITLE muramidase-released protein precursor - Streptococcus suis (type 2, strain D282) ORGANISM #formal_name Streptococcus suis DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS A43829; S21549 REFERENCE A43829 !$#authors Smith, H.E.; Vecht, U.; Gielkens, A.L.; Smits, M.A. !$#journal Infect. Immun. (1992) 60:2361-2367 !$#title Cloning and nucleotide sequence of the gene encoding the !1136-kilodalton surface protein (muramidase-released protein) !1of Streptococcus suis type 2. !$#cross-references MUID:92267650; PMID:1587602 !$#accession A43829 !'##molecule_type DNA !'##residues 1-1256 ##label SMI !'##cross-references EMBL:X64450; NID:g47550; PIDN:CAA45781.1; !1PID:g47551 CLASSIFICATION #superfamily muramidase-released protein KEYWORDS tandem repeat; transmembrane protein FEATURE !$1-47 #domain signal sequence #status predicted #label SIG\ !$48-1256 #product muramidase-released protein #status !8predicted #label MAT\ !$663-681 #domain small repeat #label RP1\ !$839-861 #domain small repeat #label RP2\ !$953-1006 #domain large repeat #label RPT1\ !$1064-1084 #domain small repeat #label RP3\ !$1089-1142 #domain large repeat #label RPT2\ !$1143-1195 #domain large repeat #label RPT3\ !$1232-1248 #domain transmembrane #status predicted #label TM1 SUMMARY #length 1256 #molecular-weight 135795 #checksum 1571 SEQUENCE /// ENTRY C64834 #type complete TITLE probable outer membrane usher protein ycbS - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS C64834 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64834 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-866 ##label BLAT !'##cross-references GB:AE000196; GB:U00096; NID:g1787169; !1PIDN:AAC74026.1; PID:g1787172; UWGP:b0940 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ycbS CLASSIFICATION #superfamily outer membrane usher protein fimD KEYWORDS ATP; fimbria; membrane protein; nucleotide binding; P-loop; !1transport protein FEATURE !$15-31 #domain transmembrane #status predicted #label TMM\ !$642-649 #region nucleotide-binding motif A (P-loop) SUMMARY #length 866 #molecular-weight 95241 #checksum 1115 SEQUENCE /// ENTRY C64785 #type complete TITLE outer membrane usher protein sfmD precursor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS C64785 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64785 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-867 ##label BLAT !'##cross-references GB:AE000159; GB:U00096; NID:g1786739; !1PIDN:AAC73634.1; PID:g1786744; UWGP:b0532 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene smfD CLASSIFICATION #superfamily outer membrane usher protein fimD KEYWORDS membrane protein SUMMARY #length 867 #molecular-weight 95676 #checksum 5139 SEQUENCE /// ENTRY C56271 #type complete TITLE outer membrane usher protein lpfC precursor - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C56271 REFERENCE A56271 !$#authors Baeumler, A.J.; Heffron, F. !$#journal J. Bacteriol. (1995) 177:2087-2097 !$#title Identification and sequence analysis of lpfABCDE, a putative !1fimbrial operon of Salmonella typhimurium. !$#cross-references MUID:95238281; PMID:7721701 !$#accession C56271 !'##status preliminary !'##molecule_type DNA !'##residues 1-842 ##label BAE !'##cross-references GB:U18559; NID:g829370; PIDN:AAA73968.1; !1PID:g829373 GENETICS !$#gene lpfC CLASSIFICATION #superfamily outer membrane usher protein fimD KEYWORDS membrane protein SUMMARY #length 842 #molecular-weight 92506 #checksum 9937 SEQUENCE /// ENTRY D65104 #type complete TITLE probable outer membrane usher protein precursor (agaL-mtr intergenic region) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS D65104 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65104 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-838 ##label BLAT !'##cross-references GB:AE000395; GB:U00096; NID:g1789524; !1PIDN:AAC76178.1; PID:g1789533; UWGP:b3144 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yraJ CLASSIFICATION #superfamily outer membrane usher protein fimD KEYWORDS membrane protein SUMMARY #length 838 #molecular-weight 93616 #checksum 8557 SEQUENCE /// ENTRY S20387 #type complete TITLE outer membrane protein caf1A precursor - Yersinia pestis ORGANISM #formal_name Yersinia pestis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S20387; S23726 REFERENCE S20387 !$#authors Karlyshev, A.V.; Galyov, E.E.; Smirnov, O.Y.; Guzayev, A.P.; !1Abramov, V.M.; Zav'yalov, V.P. !$#journal FEBS Lett. (1992) 297:77-80 !$#title A new gene of the f1 operon of Y. pestis involved in the !1capsule biogenesis. !$#cross-references MUID:92201398; PMID:1551441 !$#accession S20387 !'##molecule_type DNA !'##residues 1-833 ##label KAR !'##cross-references GB:X61996; GB:S40525; GB:S90405; GB:X57773; !1NID:g48620; PIDN:CAA43968.1; PID:g48622 REFERENCE S13008 !$#authors Galyov, E.E.; Smirnov, O.Y.; Karlishev, A.V.; Volkovoy, !1K.I.; Denesyuk, A.I.; Nazimov, I.V.; Rubtsov, K.S.; Abramov, !1V.M.; Dalvadyanz, S.M.; Zav'yalov, V.P. !$#journal FEBS Lett. (1990) 277:230-232 !$#title Nucleotide sequence of the Yersinia pestis gene encoding F1 !1antigen and the primary structure of the protein. Putative T !1and B cell epitopes. !$#cross-references MUID:91099503; PMID:1702734 !$#accession S23726 !'##status translation not shown !'##molecule_type DNA !'##residues 1-833 ##label GAL !'##cross-references EMBL:X61996; NID:g48620; PIDN:CAA43968.1; !1PID:g48622 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1992 GENETICS !$#gene caf1A CLASSIFICATION #superfamily outer membrane usher protein fimD KEYWORDS membrane protein FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-833 #domain outer membrane protein caf1A #status !8predicted #label MAT SUMMARY #length 833 #molecular-weight 93205 #checksum 9774 SEQUENCE /// ENTRY S39365 #type complete TITLE outer membrane usher protein myfC precursor - Yersinia enterocolitica ORGANISM #formal_name Yersinia enterocolitica DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S39365; S39363 REFERENCE S39364 !$#authors Iriarte, M. !$#submission submitted to the EMBL Data Library, March 1993 !$#accession S39365 !'##molecule_type DNA !'##residues 1-841 ##label IRI1 !'##cross-references EMBL:Z21953; NID:g402169; PIDN:CAA79953.1; !1PID:g402172 REFERENCE S36206 !$#authors Iriarte, M.; Vanooteghem, J.C.; Delor, I.; Diaz, R.; !1Knutton, S.; Cornelis, G.R. !$#journal Mol. Microbiol. (1993) 9:507-520 !$#title The Myf fibrillae of Yersinia enterocolitica. !$#cross-references MUID:94018646; PMID:8105362 !$#accession S39363 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 165-182;236-330;703-776 ##label IRI2 !'##cross-references EMBL:Z21953 GENETICS !$#gene myfC CLASSIFICATION #superfamily outer membrane usher protein fimD KEYWORDS membrane protein SUMMARY #length 841 #molecular-weight 93414 #checksum 1019 SEQUENCE /// ENTRY C40618 #type complete TITLE fimbrial outer membrane protein homolog SefC - Salmonella enteritidis ORGANISM #formal_name Salmonella enteritidis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C40618 REFERENCE A40618 !$#authors Clouthier, S.C.; Muller, K.H.; Doran, J.L.; Collinson, S.K.; !1Kay, W.W. !$#journal J. Bacteriol. (1993) 175:2523-2533 !$#title Characterization of three fimbrial genes, sefABC, of !1Salmonella enteritidis. !$#cross-references MUID:93239677; PMID:8097515 !$#contents 27655-3b !$#accession C40618 !'##status preliminary !'##molecule_type DNA !'##residues 1-814 ##label CLO !'##cross-references GB:L11010; NID:g310649; PIDN:AAA27221.1; !1PID:g310650 !'##note sequence extracted from NCBI backbone (NCBIN:130387, !1NCBIP:130397) CLASSIFICATION #superfamily outer membrane usher protein fimD KEYWORDS membrane protein SUMMARY #length 814 #molecular-weight 90324 #checksum 2189 SEQUENCE /// ENTRY C64737 #type complete TITLE outer membrane usher protein htrE precursor - Escherichia coli (strain K-12) ALTERNATE_NAMES fimbriae biogenesis protein homolog; pilin porin homolog htrE precursor ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS C64737; B53303; S45208; S45207 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64737 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-865 ##label BLAT !'##cross-references GB:AE000123; GB:U00096; NID:g1786327; !1PIDN:AAC73250.1; PID:g1786332; UWGP:b0139 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A53303 !$#authors Raina, S.; Missiakas, D.; Baird, L.; Kumar, S.; !1Georgopoulos, C. !$#journal J. Bacteriol. (1993) 175:5009-5021 !$#title Identification and transcriptional analysis of the !1Escherichia coli htrE operon which is homologous to pap and !1related pilin operons. !$#cross-references MUID:93352405; PMID:8102362 !$#accession B53303 !'##status preliminary !'##molecule_type DNA !'##residues 1-50,'T',52-809,'HR',812-848,'P',850-860,'LFI' ##label RAI !'##cross-references GB:L00680; NID:g385210; PIDN:AAA23721.1; !1PID:g385212 REFERENCE S45181 !$#authors Fujita, N. !$#submission submitted to the EMBL Data Library, January 1994 !$#accession S45208 !'##molecule_type DNA !'##residues 41-480,'LMK' ##label FUW !'##cross-references EMBL:D26562; NID:g473770; PIDN:BAA05587.1; !1PID:g473798 !$#accession S45207 !'##molecule_type DNA !'##residues 496-865 ##label FUJ !'##cross-references EMBL:D26562; NID:g473770; PIDN:BAA05586.1; !1PID:g473797 GENETICS !$#gene htrE !$#start_codon GTG FUNCTION !$#description biogenesis of fimbriae CLASSIFICATION #superfamily outer membrane usher protein fimD KEYWORDS membrane protein SUMMARY #length 865 #molecular-weight 95499 #checksum 1486 SEQUENCE /// ENTRY S54429 #type complete TITLE outer membrane usher protein hifC precursor - Haemophilus influenzae (strain AM30) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S54429 REFERENCE S54428 !$#authors van Ham, S.M.; van Alphen, L.; Mooi, F.R.; van Putten, !1J.P.M. !$#journal Mol. Microbiol. (1994) 13:673-684 !$#title The fimbrial gene cluster of Haemophilus influenzae type b. !$#cross-references MUID:95089703; PMID:7997179 !$#accession S54429 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-837 ##label VAN !'##cross-references EMBL:Z33502; NID:g535165; PIDN:CAA83902.1; !1PID:g581263 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1May 1994 GENETICS !$#gene hifC !$#start_codon GTG CLASSIFICATION #superfamily outer membrane usher protein fimD KEYWORDS membrane protein SUMMARY #length 837 #molecular-weight 92640 #checksum 7336 SEQUENCE /// ENTRY D64978 #type complete TITLE probable outer membrane usher protein precursor (mrp 5' region) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS D64978 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64978 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-826 ##label BLAT !'##cross-references GB:AE000300; GB:U00096; NID:g1788425; !1PIDN:AAC75170.1; PID:g1788427; UWGP:b2109 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yehB CLASSIFICATION #superfamily outer membrane usher protein fimD KEYWORDS membrane protein SUMMARY #length 826 #molecular-weight 92282 #checksum 7428 SEQUENCE /// ENTRY D39142 #type complete TITLE outer membrane usher protein mrkC precursor - Klebsiella pneumoniae ORGANISM #formal_name Klebsiella pneumoniae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS D39142 REFERENCE A39142 !$#authors Allen, B.L.; Gerlach, G.F.; Clegg, S. !$#journal J. Bacteriol. (1991) 173:916-920 !$#title Nucleotide sequence and functions of mrk determinants !1necessary for expression of type 3 fimbriae in Klebsiella !1pneumoniae. !$#cross-references MUID:91100388; PMID:1670938 !$#accession D39142 !'##status preliminary !'##molecule_type DNA !'##residues 1-828 ##label ALL !'##cross-references GB:M55912; NID:g149234; PIDN:AAA25095.1; !1PID:g149238 CLASSIFICATION #superfamily outer membrane usher protein fimD KEYWORDS membrane protein SUMMARY #length 828 #molecular-weight 91049 #checksum 429 SEQUENCE /// ENTRY S25193 #type complete TITLE outer membrane usher protein fimC precursor - Bordetella pertussis ALTERNATE_NAMES filamentous hemagglutinin A; outer membrane protein fimC ORGANISM #formal_name Bordetella pertussis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S25193; S36246; S22870; S23564; S21574 REFERENCE S25191 !$#authors Willems, R.J.L.; van der Heide, H.G.J.; Mooi, F.R. !$#journal Mol. Microbiol. (1992) 6:2661-2671 !$#title Characterization of a Bordetella pertussis fimbrial gene !1cluster which is located directly downstream of the !1filamentous haemagglutinin gene. !$#cross-references MUID:93078620; PMID:1360139 !$#accession S25193 !'##molecule_type DNA !'##residues 1-873 ##label WIL !'##cross-references EMBL:X64876; NID:g313839; PIDN:CAA46090.1; !1PID:g39748 REFERENCE S36244 !$#authors Willems, R.J.L.; Geuijen, C.; van der Heide, H.G.J.; !1Matheson, M.; Robinson, A.; Versluis, L.F.; Ebberink, R.; !1Theelen, J.; Mooi, F.R. !$#journal Mol. Microbiol. (1993) 9:623-634 !$#title Isolation of a putative fimbrial adhesin from Bordetella !1pertussis and the identification of its gene. !$#cross-references MUID:94018656; PMID:8105363 !$#accession S36246 !'##status preliminary; translation not shown !'##molecule_type DNA !'##residues 1-873 ##label WIW !'##cross-references EMBL:X64876; NID:g313839; PIDN:CAA46090.1; !1PID:g39748 REFERENCE S22869 !$#authors Locht, C.; Geoffroy, M.; Renauld, G. !$#submission submitted to the EMBL Data Library, June 1992 !$#description Common accessory genes for the Bordetella pertussis !1filamentous hemagglutinin and fimbriae share sequence !1similarites with the PAP C and PAP D gene families. !$#accession S22870 !'##molecule_type DNA !'##residues 1-743,'A',745-873 ##label LOC !'##cross-references EMBL:X66729; NID:g39716; PIDN:CAA47266.1; !1PID:g39718 REFERENCE S23563 !$#authors Locht, C.; Geoffroy, M.C.; Renauld, G. !$#journal EMBO J. (1992) 11:3175-3183 !$#title Common accessory genes for the Bordetella pertussis !1filamentous hemagglutinin and fimbriae share sequence !1similarities with the papC and papD gene families. !$#cross-references MUID:92371423; PMID:1354611 !$#accession S23564 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 24-743,'A',745-842 ##label LOW !'##cross-references EMBL:X66729 GENETICS !$#gene fimC; fhaA CLASSIFICATION #superfamily outer membrane usher protein fimD KEYWORDS membrane protein SUMMARY #length 873 #molecular-weight 93369 #checksum 2877 SEQUENCE /// ENTRY A49891 #type complete TITLE outer membrane usher protein fasD precursor - Escherichia coli ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A49891 REFERENCE A49891 !$#authors Schifferli, D.M.; Alrutz, M.A. !$#journal J. Bacteriol. (1994) 176:1099-1110 !$#title Permissive linker insertion sites in the outer membrane !1protein of 987P fimbriae of Escherichia coli. !$#cross-references MUID:94148769; PMID:7906265 !$#accession A49891 !'##status preliminary !'##molecule_type DNA !'##residues 1-835 ##label SCH !'##cross-references GB:L22659; NID:g437334; PIDN:AAA21827.1; !1PID:g437336 GENETICS !$#gene fasD CLASSIFICATION #superfamily outer membrane usher protein fimD KEYWORDS membrane protein SUMMARY #length 835 #molecular-weight 92353 #checksum 6404 SEQUENCE /// ENTRY S25218 #type complete TITLE outer membrane usher protein papC precursor - Escherichia coli ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S25218; S03751; B33491; S16397 REFERENCE S25205 !$#authors Marklund, B.I.; Tennent, J.M.; Garcia, E.; Hamers, A.; Baga, !1M.; Lindberg, F.; Gaastra, W.; Normark, S. !$#journal Mol. Microbiol. (1992) 6:2225-2242 !$#title Horizontal gene transfer of the Escherichia coli pap and prs !1pili operons as a mechanism for the development of !1tissue-specific adhesive properties. !$#cross-references MUID:93023852; PMID:1357526 !$#accession S25218 !'##molecule_type DNA !'##residues 1-836 ##label MAR !'##cross-references EMBL:X61239; NID:g42290; PIDN:CAA43564.1; !1PID:g42295 !'##experimental_source strain J96 !'##note in the authors' translation residues 432-470 do not match the !1nucleotide sequence REFERENCE S03750 !$#authors Norgren, M.; Baga, M.; Tennent, J.M.; Normark, S. !$#journal Mol. Microbiol. (1987) 1:169-178 !$#title Nucleotide sequence, regulation and functional analysis of !1the papC gene required for cell surface localization of Pap !1pili of uropathogenic Escherichia coli. !$#cross-references MUID:88216160; PMID:2897064 !$#accession S03751 !'##status preliminary !'##molecule_type DNA !'##residues 1-836 ##label NOR !'##cross-references EMBL:Y00529; NID:g42303; PIDN:CAA68588.1; !1PID:g42304 REFERENCE A33491 !$#authors Lindberg, F.; Tennent, J.M.; Hultgren, S.J.; Lund, B.; !1Normark, S. !$#journal J. Bacteriol. (1989) 171:6052-6058 !$#title PapD, a periplasmic transport protein in P-pilus biogenesis. !$#cross-references MUID:90036691; PMID:2572580 !$#accession B33491 !'##status preliminary !'##molecule_type DNA !'##residues 720-836 ##label LIN !'##cross-references GB:Y00529; GB:M30806 GENETICS !$#gene papC CLASSIFICATION #superfamily outer membrane usher protein fimD KEYWORDS membrane protein FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-836 #product papC protein #status predicted #label MAT SUMMARY #length 836 #molecular-weight 91076 #checksum 7850 SEQUENCE /// ENTRY E64807 #type complete TITLE outer membrane usher protein ybgQ precursor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS E64807 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64807 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-818 ##label BLAT !'##cross-references GB:AE000175; GB:U00096; NID:g1786934; !1PIDN:AAC73812.1; PID:g1786937; UWGP:b0718 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ybgQ FUNCTION !$#description biogenesis of fimbriae CLASSIFICATION #superfamily outer membrane usher protein fimD KEYWORDS membrane protein FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-818 #product outer membrane usher protein ybgQ #status !8predicted #label MAT SUMMARY #length 818 #molecular-weight 90442 #checksum 2204 SEQUENCE /// ENTRY D65092 #type complete TITLE outer membrane usher protein pmfC precursor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS D65092 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65092 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-821 ##label BLAT !'##cross-references GB:AE000386; GB:U00096; NID:g2367187; !1PIDN:AAC76082.1; PID:g2367188; UWGP:b3046 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily outer membrane usher protein fimD KEYWORDS membrane protein SUMMARY #length 821 #molecular-weight 91886 #checksum 4575 SEQUENCE /// ENTRY I83350 #type complete TITLE outer membrane usher protein cssD precursor - Escherichia coli ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS I83350 REFERENCE I60266 !$#authors Willshaw, G.A.; Smith, H.R.; McConnell, M.M.; Rowe, B. !$#journal FEMS Microbiol. Lett. (1988) 49:473-478 !$#title Cloning of genes encoding coli-surface (CS) antigens in !1enterotoxigenic Escherichia coli. !$#accession I83350 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-819 ##label RES !'##cross-references EMBL:U04844; NID:g442375; PIDN:AAC45096.1; !1PID:g442379 CLASSIFICATION #superfamily outer membrane usher protein fimD KEYWORDS membrane protein SUMMARY #length 819 #molecular-weight 92378 #checksum 2723 SEQUENCE /// ENTRY MMECOF #type complete TITLE outer membrane usher protein faeD precursor - Escherichia coli ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 21-Nov-1998 #text_change 16-Jul-1999 ACCESSIONS S24931; A24934; S15226; S69760 REFERENCE S24931 !$#authors Oudega, B. !$#submission submitted to the EMBL Data Library, October 1990 !$#accession S24931 !'##molecule_type DNA !'##residues 1-812 ##label OUD !'##cross-references EMBL:X56002; NID:g41388; PIDN:CAA39476.1; !1PID:g41389 REFERENCE A24934 !$#authors Mooi, F.R.; Claassen, I.; Bakker, D.; Kuipers, H.; de Graaf, !1F.K. !$#journal Nucleic Acids Res. (1986) 14:2443-2457 !$#title Regulation and structure of an Escherichia coli gene coding !1for an outer membrane protein involved in export of K88ab !1fimbrial subunits. !$#cross-references MUID:86176742; PMID:2870470 !$#accession A24934 !'##molecule_type DNA !'##residues 1-634,'SQWFCLGQRFGTGSSGGERHHVQPHDRRHGGGGECE',637,'HAGSE', !1643,'D',679-812 ##label MOO !'##cross-references GB:X03675 !'##note sequence has been revised (see reference S24931) REFERENCE S15226 !$#authors Bakker, D.; Vader, C.E.M.; Roosendaal, B.; Mooi, F.R.; !1Oudega, B.; de Graaf, F.K. !$#journal Mol. Microbiol. (1991) 5:875-886 !$#title Structure and function of periplasmic chaperone-like !1proteins involved in the biosynthesis of K88 and K99 !1fimbriae in enterotoxigenic Escherichia coli. !$#cross-references MUID:91312125; PMID:1713284 !$#accession S15226 !'##status preliminary !'##molecule_type DNA !'##residues 794-812 ##label BAK !'##cross-references EMBL:X56003; NID:g41384; PIDN:CAA39477.1; !1PID:g41385 REFERENCE S69760 !$#authors Valent, Q.A.; Zaal, J.; de Graaf, F.K.; Oudega, B. !$#journal Mol. Microbiol. (1995) 16:1243-1257 !$#title Subcellular localization and topology of the K88 usher FaeD !1in Escherichia coli. !$#cross-references MUID:96020654; PMID:8577257 !$#accession S69760 !'##molecule_type protein !'##residues 36-40 ##label VAL GENETICS !$#gene faeD FUNCTION !$#description required for transport of K88ab fimbrial adhesin chains !1across the outer membrane; essential for production of !1fimbriae CLASSIFICATION #superfamily outer membrane usher protein fimD KEYWORDS membrane protein; protein export FEATURE !$1-35 #domain signal sequence #status predicted #label SIG\ !$36-812 #product outer membrane usher protein faeD #status !8experimental #label MAT SUMMARY #length 812 #molecular-weight 85496 #checksum 5978 SEQUENCE /// ENTRY S02755 #type complete TITLE outer membrane usher protein fanD precursor - Escherichia coli plasmid pFK99 ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S02755; I41322 REFERENCE S02755 !$#authors Roosendaal, B.; de Graaf, F.K. !$#journal Nucleic Acids Res. (1989) 17:1263 !$#title The nucleotide sequence of the fanD gene encoding the large !1outer membrane protein involved in the biosynthesis of K99 !1fimbriae. !$#cross-references MUID:89160266; PMID:2564179 !$#accession S02755 !'##status translation not shown !'##molecule_type DNA !'##residues 1-783 ##label ROO !'##cross-references EMBL:X13560; NID:g41407; PIDN:CAA31911.1; !1PID:g41408 REFERENCE I41321 !$#authors Roosendaal, B.; Gaastra, W.; de Graaf, F.K. !$#journal FEMS Microbiol. Lett. (1984) 22:253-258 !$#title The nucleotide sequence of the gene encoding the K99 subunit !1of enterotoxigenic Escherichia coli. !$#accession I41322 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 'MIARNITDGYY',1-20 ##label RES !'##cross-references GB:M35282; NID:g146528; PIDN:AAA24038.1; !1PID:g146530 GENETICS !$#gene fanD !$#genome plasmid CLASSIFICATION #superfamily outer membrane usher protein fimD KEYWORDS membrane protein SUMMARY #length 783 #molecular-weight 87156 #checksum 617 SEQUENCE /// ENTRY A37142 #type complete TITLE outer membrane usher protein pefC precursor - Salmonella typhimurium plasmid pCRR10 ORGANISM #formal_name Salmonella typhimurium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A37142; S32889 REFERENCE A37142 !$#authors Rioux, C.R.; Friedrich, M.J.; Kadner, R.J. !$#journal J. Bacteriol. (1990) 172:6217-6222 !$#title Genes on the 90-kilobase plasmid of Salmonella typhimurium !1confer low-affinity cobalamin transport: relationship to !1fimbria biosynthesis genes. !$#cross-references MUID:91035228; PMID:1977735 !$#accession A37142 !'##status preliminary !'##molecule_type DNA !'##residues 1-802 ##label RIO !'##cross-references GB:M37853; NID:g153964; PIDN:AAA63534.1; !1PID:g153965 REFERENCE S32886 !$#authors Friedrich, M.J.; Kinsey, N.E.; Vila, J.; Kadner, R.J. !$#journal Mol. Microbiol. (1993) 8:543-558 !$#title Nucleotide sequence of a 13.9kb segment of the 90kb !1virulence plasmid of Salmonella typhimurium: the presence of !1fimbrial biosynthetic genes. !$#cross-references MUID:93316852; PMID:8100983 !$#accession S32889 !'##status preliminary !'##molecule_type DNA !'##residues 1-802 ##label FRI !'##cross-references EMBL:L08613; NID:g154239; PIDN:AAC36960.1; !1PID:g154243 GENETICS !$#gene pefC !$#genome plasmid !$#start_codon GTG CLASSIFICATION #superfamily outer membrane usher protein fimD KEYWORDS membrane protein SUMMARY #length 802 #molecular-weight 86410 #checksum 2347 SEQUENCE /// ENTRY MMECTC #type complete TITLE export system outer membrane protein tolC precursor [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 17-May-1985 #sequence_revision 30-Sep-1997 #text_change 01-Mar-2002 ACCESSIONS A65091; A03430; S11457; I53455 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65091 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-495 ##label BLAT !'##cross-references GB:AE000385; GB:U00096; NID:g1789405; !1PIDN:AAC76071.1; PID:g1789413; UWGP:b3035 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A03430 !$#authors Hackett, J.; Reeves, P. !$#journal Nucleic Acids Res. (1983) 11:6487-6495 !$#title Primary structure of the tolC gene that codes for an outer !1membrane protein of Escherichia coli K12. !$#cross-references MUID:84015386; PMID:6312426 !$#accession A03430 !'##molecule_type DNA !'##residues 3-179,'K',181-204,'HV',207-215,'GT',218-259, !1'KFARRRMVTYRLW',273-279,'FLTPLIAVR',289,'P','C',294,'AVP', !1298-326,'T',328-336,'ASTWKVPIVASC',349,'RA','FC',355,'S', !1357-366,'R',368,'T',370-371,'A',373-401,'SC','T',406, !1'QARAG',412,'P',414-446,'I',448-495 ##label HAC !'##cross-references GB:X00016; GB:J01711; NID:g43103; PIDN:CAA24914.1; !1PID:g43104 REFERENCE S11457 !$#authors Niki, H.; Imamura, R.; Ogura, T.; Hiraga, S. !$#journal Nucleic Acids Res. (1990) 18:5547 !$#title Nucleotide sequence of the tolC gene of Escherichia coli. !$#cross-references MUID:91016844; PMID:2216730 !$#accession S11457 !'##molecule_type DNA !'##residues 1-192,'L',194-495 ##label NIK !'##cross-references EMBL:X54049; NID:g43106; PIDN:CAA37982.1; !1PID:g43107 REFERENCE I53455 !$#authors Hackett, J.; Misra, R.; Reeves, P. !$#journal FEBS Lett. (1983) 156:307-310 !$#title The TolC protein of Escherichia coli K12 is synthesised in a !1precursor form. !$#cross-references MUID:83210228; PMID:6303857 !$#accession I53455 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-47 ##label RES !'##cross-references EMBL:V01505; NID:g43100; PIDN:CAA24751.1; !1PID:g43101 COMMENT This protein is required for proper expression of outer !1membrane protein genes such as ompF, nmpC, and protein 2. !1Strains that are mutant in tolC show tolerance to colicin !1E1. GENETICS !$#gene tolC !$#map_position 66 min COMPLEX the hemolysin export system consists of the ATP-binding !1protein hlyB (see PIR:S10057), the membrane fusion protein !1hlyD (see PIR:LEECD) and the outer membrane protein tolC !1(see PIR:MMECTC) [validated, MUID:97368101] FUNCTION HEM !$#description tolC is involved in the export of hemolysin [validated, !1MUID:90280458] FUNCTION COL !$#description tolC is involved in the export of colicin V [validated, !1MUID:91065315] FUNCTION CHR !$#description tolC is involved in chromosome partitioning after !1replication [validated, MUID:92021778] CLASSIFICATION #superfamily outer membrane protein tolC KEYWORDS membrane protein; membrane-associated protein; protein !1export; pyroglutamic acid FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-495 #product outer membrane protein tolC #status !8predicted #label MAT\ !$23 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status predicted SUMMARY #length 495 #molecular-weight 54000 #checksum 4517 SEQUENCE /// ENTRY MMECF #type complete TITLE outer membrane porin ompF precursor - Escherichia coli (strain K-12) ALTERNATE_NAMES outer membrane protein 1a; outer membrane protein b ORGANISM #formal_name Escherichia coli DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 01-Mar-2002 ACCESSIONS A93449; A91301; A90314; A25029; H64832; A03431 REFERENCE A93449 !$#authors Inokuchi, K.; Mutoh, N.; Matsuyama, S.; Mizushima, S. !$#journal Nucleic Acids Res. (1982) 10:6957-6968 !$#title Primary structure of the ompF gene that codes for a major !1outer membrane protein of Escherichia coli K-12. !$#cross-references MUID:83090452; PMID:6294623 !$#accession A93449 !'##molecule_type DNA !'##residues 1-362 ##label INO !'##cross-references GB:J01655; GB:M10311; GB:M10312; NID:g147009; !1PIDN:AAA24244.1; PID:g147010 !'##experimental_source strain K12 REFERENCE A91301 !$#authors Mutoh, N.; Inokuchi, K.; Mizushima, S. !$#journal FEBS Lett. (1982) 137:171-174 !$#title Amino acid sequence of the signal peptide of OmpF, a major !1outer membrane protein of Escherichia coli. !$#cross-references MUID:82139379; PMID:7037455 !$#accession A91301 !'##molecule_type DNA !'##residues 1-37 ##label MUT REFERENCE A90314 !$#authors Chen, R.; Kramer, C.; Schmidmayr, W.; Chen-Schmeisser, U.; !1Henning, U. !$#journal Biochem. J. (1982) 203:33-43 !$#title Primary structure of major outer-membrane protein I (ompF !1protein, porin) of Escherichia coli B/r. !$#cross-references MUID:82256494; PMID:7049161 !$#accession A90314 !'##molecule_type protein !'##residues 23-87,'E',89-138,'G',140-283,'L',285-362 ##label CHE REFERENCE A91809 !$#authors Nogami, T.; Mizuno, T.; Mizushima, S. !$#journal J. Bacteriol. (1985) 164:797-801 !$#title Construction of a series of ompF-ompC chimeric genes by in !1vivo homologous recombination in Escherichia coli and !1characterization of the translational products. !$#cross-references MUID:86033642; PMID:2997131 !$#accession A25029 !'##molecule_type DNA !'##residues 33-63 ##label NOG REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64832 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-362 ##label BLAT !'##cross-references GB:AE000195; GB:U00096; NID:g1787156; !1PIDN:AAC74015.1; PID:g1787160; UWGP:b0929 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ompF; tolF; cmlB; coa; cry !$#map_position 21 min COMPLEX homotrimer FUNCTION POR !$#description forms aqueous channels that faciliate diffusion of small !1hydrophilic molecules across the outer membrane FUNCTION REC !$#description receptor for bacteriophage T2 CLASSIFICATION #superfamily outer membrane protein phoE KEYWORDS membrane protein; porin; trimer FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-362 #product outer membrane porin ompF #status !8experimental #label MAT SUMMARY #length 362 #molecular-weight 39333 #checksum 2147 SEQUENCE /// ENTRY MMECPE #type complete TITLE outer membrane porin phoE precursor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 01-Mar-2002 ACCESSIONS A03432; B64749 REFERENCE A92893 !$#authors Overbeeke, N.; Bergmans, H.; van Mansfeld, F.; Lugtenberg, !1B. !$#journal J. Mol. Biol. (1983) 163:513-532 !$#title Complete nucleotide sequence of phoE, the structural gene !1for the phosphate limitation inducible outer membrane pore !1protein of Escherichia coli K12. !$#cross-references MUID:83189086; PMID:6341601 !$#accession A03432 !'##molecule_type DNA !'##residues 1-351 ##label OVE !'##cross-references GB:D83536; NID:g4902908; PIDN:BAA77910.1; !1PID:g4902976 !'##experimental_source strain K12 !'##note this is one of the proteins induced when the E. coli cells are !1grown under phosphate limitation; its protein pore is !1particularly efficient in the uptake of inorganic phosphate, !1phosphorylated compounds, and some other negatively charged !1solutes REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64749 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-351 ##label BLAT !'##cross-references GB:AE000132; GB:U00096; NID:g2367098; !1PIDN:AAC73345.1; PID:g1786436; UWGP:b0241 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene phoE !$#map_position 6 min COMPLEX homotrimer FUNCTION !$#description allows passive diffusion of small hydrophilic molecules with !1molecular weights of up to 600 Da; phoE pores are !1anion-selective !$#note induced under phosphate limitation CLASSIFICATION #superfamily outer membrane protein phoE KEYWORDS homotrimer; membrane protein; porin FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-351 #product outer membrane porin phoE #status predicted !8#label OPP SUMMARY #length 351 #molecular-weight 38922 #checksum 6351 SEQUENCE /// ENTRY MMECPC #type complete TITLE outer membrane porin ompC precursor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 01-Mar-2002 ACCESSIONS A20867; A18885; B25029; E64991 REFERENCE A20867 !$#authors Mizuno, T.; Chou, M.Y.; Inouye, M. !$#journal J. Biol. Chem. (1983) 258:6932-6940 !$#title A comparative study on the genes for three porins of the !1Escherichia coli outer membrane. DNA sequence of the !1osmoregulated ompC gene. !$#cross-references MUID:83213433; PMID:6304064 !$#accession A20867 !'##molecule_type DNA !'##residues 1-367 ##label MIZ !'##cross-references GB:K00541; GB:M10314; GB:M14188; NID:g147007; !1PIDN:AAA24243.1; PID:g147008 REFERENCE A18885 !$#authors Mizuno, T.; Chou, M.Y.; Inouye, M. !$#journal FEBS Lett. (1983) 151:159-164 !$#title DNA sequence of the promoter region of the ompC gene and the !1amino acid sequence of the signal peptide of pro-OmpC !1protein of Escherichia coli. !$#cross-references MUID:83132326; PMID:6297988 !$#accession A18885 !'##molecule_type DNA !'##residues 1-40 ##label MI2 REFERENCE A91809 !$#authors Nogami, T.; Mizuno, T.; Mizushima, S. !$#journal J. Bacteriol. (1985) 164:797-801 !$#title Construction of a series of ompF-ompC chimeric genes by in !1vivo homologous recombination in Escherichia coli and !1characterization of the translational products. !$#cross-references MUID:86033642; PMID:2997131 !$#accession B25029 !'##molecule_type DNA !'##residues 32-57 ##label NOG REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64991 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-367 ##label BLAT !'##cross-references GB:AE000310; GB:U00096; NID:g2367131; !1PIDN:AAC75275.1; PID:g1788544; UWGP:b2215 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ompC !$#map_position 47 min FUNCTION !$#description one of the E. coli major outer membrane proteins that form !1passive diffusion pores and allow small hydrophilic !1molecules across the outer membrane CLASSIFICATION #superfamily outer membrane protein phoE KEYWORDS membrane protein; porin; trimer FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-367 #product outer membrane porin ompC #status predicted !8#label MAT SUMMARY #length 367 #molecular-weight 40368 #checksum 3653 SEQUENCE /// ENTRY MMEBPC #type complete TITLE outer membrane porin ompC precursor - Salmonella typhi ORGANISM #formal_name Salmonella typhi DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS JQ0119; S01248; S10122 REFERENCE JQ0119 !$#authors Puente, J.L.; Alvarez-Scherer, V.; Gosset, G.; Calva, E. !$#journal Gene (1989) 83:197-206 !$#title Comparative analysis of the Salmonella typhi and Escherichia !1coli ompC genes. !$#cross-references MUID:90060831; PMID:2684785 !$#accession JQ0119 !'##molecule_type DNA !'##residues 1-378 ##label PUE !'##cross-references GB:M31424; NID:g154207; PIDN:AAA27169.1; !1PID:g154208 REFERENCE S01248 !$#authors Venegas, A.; Gomez, I.; Zaror, I.; Yudelevich, A. !$#journal Nucleic Acids Res. (1988) 16:7721 !$#title The nucleotide sequence of the Salmonella typhi ompC porin !1gene. !$#cross-references MUID:88319959; PMID:3412902 !$#accession S01248 !'##molecule_type DNA !'##residues 1-5,'Q',7-361,363-378 ##label VEN1 !'##cross-references EMBL:X07835; NID:g47796; PIDN:CAA30688.1; !1PID:g47797 !'##experimental_source strain Ty2 REFERENCE S10122 !$#authors Venegas, A. !$#submission submitted to the EMBL Data Library, May 1988 !$#accession S10122 !'##molecule_type DNA !'##residues 1-361,363-378 ##label VEN2 !'##cross-references EMBL:X07835; NID:g47796; PIDN:CAA30688.1; !1PID:g47797 GENETICS !$#gene ompC !$#map_position 45 min CLASSIFICATION #superfamily outer membrane protein phoE KEYWORDS membrane protein; porin; trimer FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-378 #product outer membrane porin ompC #status predicted !8#label MAT SUMMARY #length 378 #molecular-weight 41239 #checksum 7061 SEQUENCE /// ENTRY A59139 #type complete TITLE outer membrane porin C precursor - Salmonella typhimurium ALTERNATE_NAMES ompC protein ORGANISM #formal_name Salmonella typhimurium DATE 12-Nov-1999 #sequence_revision 12-Nov-1999 #text_change 12-Nov-1999 ACCESSIONS A59139 REFERENCE A59139 !$#authors Negm, R.S.; Pistole, T.G. !$#journal Can. J. Microbiol. (1999) 45:658-669 !$#title The porin OmpC of Salmonella typhimurium mediates adherence !1to macrophages. !$#cross-references MUID:99457705; PMID:10528398 !$#accession A59139 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-378 ##label NEG !'##cross-references GB:AF039309; NID:g2773086; PIDN:AAB96675.1; !1PID:g2773087 !'##experimental_source strain 14028 !'##note submitted to GenBank, December 1997 GENETICS !$#gene ompC !$#map_position 49.3 minutes COMPLEX homotrimer CLASSIFICATION #superfamily outer membrane protein phoE KEYWORDS homotrimer; membrane protein; porin FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-378 #product outer membrane porin ompC #status predicted !8#label MAT SUMMARY #length 378 #molecular-weight 41299 #checksum 7317 SEQUENCE /// ENTRY MMBPP2 #type complete TITLE outer membrane porin lc precursor - phage PA2 ORGANISM #formal_name phage PA2 #note host Escherichia coli DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 02-Jul-1998 ACCESSIONS D25647 REFERENCE A25647 !$#authors Blasband, A.J.; Marcotte Jr., W.R.; Schnaitman, C.A. !$#journal J. Biol. Chem. (1986) 261:12723-12732 !$#title Structure of the lc and nmpC outer membrane porin protein !1genes of lambdoid bacteriophage. !$#cross-references MUID:86304457; PMID:3017988 !$#accession D25647 !'##molecule_type DNA !'##residues 1-365 ##label BLA GENETICS !$#gene lc CLASSIFICATION #superfamily outer membrane protein phoE KEYWORDS membrane protein; porin; trimer FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-365 #product outer membrane porin lc #status predicted !8#label MAT SUMMARY #length 365 #molecular-weight 40309 #checksum 4004 SEQUENCE /// ENTRY MMECNC #type complete TITLE outer membrane porin nmpC precursor - Escherichia coli (strain K-12) cryptic lambdoid prophage DLP12 ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 01-Mar-2002 ACCESSIONS A25647; S66594; G64787 REFERENCE A25647 !$#authors Blasband, A.J.; Marcotte Jr., W.R.; Schnaitman, C.A. !$#journal J. Biol. Chem. (1986) 261:12723-12732 !$#title Structure of the lc and nmpC outer membrane porin protein !1genes of lambdoid bacteriophage. !$#cross-references MUID:86304457; PMID:3017988 !$#contents mutant strain CS384 !$#accession A25647 !'##molecule_type DNA !'##residues 1-365 ##label BLA REFERENCE S66579 !$#authors Mahdi, A.A.; Sharples, G.J.; Mandal, T.N.; Lloyd, R.G. !$#journal J. Mol. Biol. (1996) 257:561-573 !$#title Holliday junction resolvases encoded by homologous rusA !1genes in Escherichia coli K-12 and phage 82. !$#cross-references MUID:96196428; PMID:8648624 !$#accession S66594 !'##molecule_type DNA !'##residues 347-365 ##label MAH !'##cross-references EMBL:X92587; NID:g1051136; PIDN:CAA63325.1; !1PID:g1051145 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64787 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 'MNIYRAVTSFFNNSSKKGLT',1-325,'N',327-347,'EGANKSLI' ##label !1BLAT !'##cross-references GB:AE000160; GB:U00096; NID:g1786751; !1PIDN:AAC73654.1; PID:g1786765; UWGP:b0553 !'##experimental_source strain K-12, substrain MG1655 COMMENT In wild-type strains of E. coli K-12, the nmpC open reading !1frame is interrupted by an IS5 insertion and generates a !1hybrid open reading frame that is not expressed. However, in !1mutant strain CS348, the IS5 element has been deleted and !1nmpC is expressed. GENETICS !$#gene nmpC !$#map_position 12 min !$#genome cryptic lambdoid prophage DLP12 CLASSIFICATION #superfamily outer membrane protein phoE KEYWORDS membrane protein; porin; trimer FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-365 #product outer membrane porin nmpC #status predicted !8#label MAT SUMMARY #length 365 #molecular-weight 40316 #checksum 4168 SEQUENCE /// ENTRY MMNHPB #type complete TITLE outer membrane protein PIB precursor - Neisseria gonorrhoeae (strain P9 serovar IB26 and strain S4 serovar IB4 ) ORGANISM #formal_name Neisseria gonorrhoeae #variety strain P9 serovar IB26; strain S4 serovar IB4 DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS S10509; S45382 REFERENCE S10509 !$#authors Butt, N.J.; Lambden, P.R.; Heckels, J.E. !$#journal Nucleic Acids Res. (1990) 18:4258 !$#title The nucleotide sequence of the por gene from Neisseria !1gonorrhoeae strain P9 encoding outer membrane protein PIB. !$#cross-references MUID:90332432; PMID:1696003 !$#accession S10509 !'##molecule_type DNA !'##residues 1-348 ##label BUT !'##cross-references EMBL:X52823; NID:g44918; PIDN:CAA37005.1; !1PID:g44919 !'##experimental_source strain P9 serovar IB26 REFERENCE S45381 !$#authors Lau, Q.C.; Chow, V.T.K.; Poh, C.L. !$#journal Med. Microbiol. Immunol. (1993) 182:137-145 !$#title Polymerase chain reaction and direct sequencing of Neisseria !1gonorrhoeae protein IB gene: partial nucleotide and amino !1acid sequence analysis of strains S4, S11, S48 (serovar IB4) !1and S34 (serovar IB5). !$#cross-references MUID:94049424; PMID:8232067 !$#accession S45382 !'##status preliminary !'##molecule_type DNA !'##residues 175-268 ##label LAU !'##cross-references EMBL:U07827; NID:g468891; PIDN:AAA53549.1; !1PID:g468892 !'##experimental_source strain S4 serovar IB4 CLASSIFICATION #superfamily outer membrane protein class 1 KEYWORDS membrane protein; porin FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-348 #product outer membrane protein PIB #status predicted !8#label MAT SUMMARY #length 348 #molecular-weight 37416 #checksum 2003 SEQUENCE /// ENTRY MMNH1 #type complete TITLE outer membrane protein class 1 precursor - Neisseria meningitidis ORGANISM #formal_name Neisseria meningitidis DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 21-Jan-2000 ACCESSIONS S11717; JL0141; S26099; S26113; S26125; S26105; S26106; !1S26111 REFERENCE S11717 !$#authors McGuinnes, B.; Barlow, A.K.; Clarke, I.N.; Farley, J.E.; !1Anilionis, A.; Poolman, J.T.; Heckels, J.E. !$#submission submitted to the EMBL Data Library, May 1990 !$#description Deduced amino acid sequence of class 1 protein (porA) from !1three strains of Neisseria meningitidis. !$#accession S11717 !'##molecule_type DNA !'##residues 1-387 ##label MCG !'##cross-references EMBL:X52996; NID:g45182; PIDN:CAA37185.1; !1PID:g45183 !'##experimental_source strain MC51 REFERENCE JL0140 !$#authors McGuinness, B.T.; Barlow, A.K.; Clarke, I.N.; Farley, J.E.; !1Anilionis, A.; Poolman, J.T.; Heckels, J.E. !$#journal J. Exp. Med. (1990) 171:1871-1882 !$#title Deduced amino acid sequences of class 1 protein (porA) from !1three strains of Neisseria meningitidis: synthetic peptides !1define the epitopes responsible for serosubtype specificity. !$#cross-references MUID:90278344; PMID:1693651 !$#accession JL0141 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 20-387 ##label MC2 !'##experimental_source strain MC51 REFERENCE S26099 !$#authors McGuinness, B.T. !$#submission submitted to the EMBL Data Library, August 1992 !$#accession S26099 !'##molecule_type DNA !'##residues 29-86 ##label MC3 !'##cross-references EMBL:Z14257; NID:g45068; PIDN:CAA78624.1; !1PID:g45069; EMBL:Z14269; NID:g45092; PID:g45093 !'##experimental_source strain L2130 !$#accession S26113 !'##molecule_type DNA !'##residues 29-75 ##label MC4 !'##cross-references EMBL:Z14271; NID:g45105; PIDN:CAA78638.1; !1PID:g45106 !$#accession S26125 !'##molecule_type DNA !'##residues 29-88 ##label MC5 !'##cross-references EMBL:Z14283; NID:g45129; PIDN:CAA78650.1; !1PID:g45130 !$#accession S26105 !'##molecule_type DNA !'##residues 176-224 ##label MC6 !'##cross-references EMBL:Z14264; NID:g45082; PIDN:CAA78631.1; !1PID:g45083 GENETICS !$#gene porA CLASSIFICATION #superfamily outer membrane protein class 1 KEYWORDS membrane protein; porin FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-387 #product outer membrane protein class 1 #status !8predicted #label MAT SUMMARY #length 387 #molecular-weight 41776 #checksum 3217 SEQUENCE /// ENTRY MMBYO #type complete TITLE mitochondrial outer membrane protein, 70K - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein N1905; protein YNL121c ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1991 #sequence_revision 17-May-1996 #text_change 16-Jun-2000 ACCESSIONS S63062; S05884; S67337 REFERENCE S63047 !$#authors De Antoni, A.; D Angelo, M.; Dal Pero, F.; Sartorello, F.; !1Pandolfo, D.; Lanfranchi, G.; Valle, G. !$#submission submitted to the Protein Sequence Database, April 1996 !$#accession S63062 !'##molecule_type DNA !'##residues 1-617 ##label DEA !'##cross-references EMBL:Z71397; NID:g1302049; PIDN:CAA96002.1; !1PID:g1302050; GSPDB:GN00014; MIPS:YNL121c !'##experimental_source strain S288C REFERENCE S05884 !$#authors Hase, T.; Riezman, H.; Suda, K.; Schatz, G. !$#journal EMBO J. (1983) 2:2169-2172 !$#title Import of proteins into mitochondria: nucleotide sequence of !1the gene for a 70-kd protein of the yeast mitochondrial !1outer membrane. !$#cross-references MUID:84131928; PMID:6365533 !$#accession S05884 !'##molecule_type DNA !'##residues 1-184,'R',186-617 ##label HAS !'##cross-references EMBL:X05585; NID:g4081; PIDN:CAA29085.1; PID:g4082 REFERENCE S67327 !$#authors d'Antoni, A.; d'Angelo, M.; dal Pero, F.; Sartorello, F.; !1Pandolfo, D.; Lanfranchi, G.; Valle, G. !$#submission submitted to the EMBL Data Library, February 1996 !$#description The DNA sequence of cosmid 14-13b from chromosome XIV of !1Saccharomyces cerevisiae reveals an unusually high number of !1overlapping ORFs. !$#accession S67337 !'##molecule_type DNA !'##residues 1-617 ##label DAN !'##cross-references EMBL:Z69382; NID:g1183941; PIDN:CAA93386.1; !1PID:g1183952 GENETICS !$#gene SGD:TOM70; OMP1; MOM72; MAS70; MIPS:YNL121c !'##cross-references SGD:S0005065; MIPS:YNL121c !$#map_position 14L !$#genome nuclear CLASSIFICATION #superfamily mitochondrial outer membrane protein, 70K; !1tetratricopeptide repeat homology KEYWORDS mitochondrion; transmembrane protein FEATURE !$10-29 #domain transmembrane #status predicted #label TMM\ !$99-131 #domain tetratricopeptide repeat homology #label TT1\ !$132-165 #domain tetratricopeptide repeat homology #label TT2\ !$363-396 #domain tetratricopeptide repeat homology #label TT3\ !$397-430 #domain tetratricopeptide repeat homology #label TT4\ !$465-498 #domain tetratricopeptide repeat homology #label TT5\ !$508-541 #domain tetratricopeptide repeat homology #label TT6\ !$542-575 #domain tetratricopeptide repeat homology #label TT7 SUMMARY #length 617 #molecular-weight 70122 #checksum 7043 SEQUENCE /// ENTRY MMHUP3 #type complete TITLE voltage-dependent anion channel 1 [validated] - human ALTERNATE_NAMES 31K porin, lymphocyte; mitochondrial porin 1; porin 31HL; porin 31HM ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Dec-1991 #sequence_revision 08-Feb-1996 #text_change 08-Dec-2000 ACCESSIONS A44422; S07478; S16195; S04018 REFERENCE A44422 !$#authors Blachly-Dyson, E.; Zambronicz, E.B.; Yu, W.H.; Adams, V.; !1McCabe, E.R.; Adelman, J.; Colombini, M.; Forte, M. !$#journal J. Biol. Chem. (1993) 268:1835-1841 !$#title Cloning and functional expression in yeast of two human !1isoforms of the outer mitochondrial membrane channel, the !1voltage-dependent anion channel. !$#cross-references MUID:93131931; PMID:8420959 !$#accession A44422 !'##molecule_type mRNA !'##residues 1-283 ##label BLA !'##cross-references GB:L06132; NID:g340198; PIDN:AAA61272.1; !1PID:g340199 !'##experimental_source B cell line WIL-2NS !'##note sequence extracted from NCBI backbone (NCBIP:122926) REFERENCE S07478 !$#authors Kayser, H.; Kratzin, H.D.; Thinnes, F.P.; Goetz, H.; !1Schmidt, W.E.; Eckart, K.; Hilschmann, N. !$#journal Biol. Chem. Hoppe-Seyler (1989) 370:1265-1278 !$#title To the knowledge of human porins. II. Characterization and !1primary structure of a 31-kDa porin from human B lymphocytes !1(Porin 31HL). !$#cross-references MUID:90148194; PMID:2559745 !$#accession S07478 !'##molecule_type protein !'##residues 2-283 ##label KAY !'##note article in German with English abstract REFERENCE S16195 !$#authors Juergens, L.; Ilsemann, P.; Kratzin, H.D.; Hesse, D.; !1Eckart, K.; Thinnes, F.P.; Hilschmann, N. !$#journal Biol. Chem. Hoppe-Seyler (1991) 372:455-463 !$#title Studies on human porin. IV. The primary structures of "Porin !131HM" purified from human skeletal muscle membranes and of !1"Porin 31HL" derived from human B lymphocyte membranes are !1identical. !$#cross-references MUID:92029673; PMID:1657034 !$#accession S16195 !'##status preliminary !'##molecule_type protein !'##residues 2-283 ##label FPH REFERENCE S04018 !$#authors Kayser, H.; Kratzin, H.D.; Thinnes, F.P.; Goetz, H.; !1Hilschmann, N. !$#submission submitted to the Protein Sequence Database, April 1989 !$#accession S04018 !'##molecule_type protein !'##residues 2-283 ##label KAT GENETICS !$#gene GDB:VDAC1 !'##cross-references GDB:138280; OMIM:314555 !$#map_position Xq13-Xq21 CLASSIFICATION #superfamily porin KEYWORDS acetylated amino end; mitochondrial outer membrane FEATURE !$2-283 #product voltage-dependent anion channel 1 #status !8experimental #label MAT\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental SUMMARY #length 283 #molecular-weight 30772 #checksum 100 SEQUENCE /// ENTRY A38102 #type complete TITLE voltage-dependent anion channel-like protein - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A38102 REFERENCE A38102 !$#authors Bureau, M.H.; Khrestchatisky, M.; Heeren, M.A.; Zambrowicz, !1E.B.; Kim, H.; Grisar, T.M.; Colombini, M.; Tobin, A.J.; !1Olsen, R.W. !$#journal J. Biol. Chem. (1992) 267:8679-8684 !$#title Isolation and cloning of a voltage-dependent anion !1channel-like M-r 36,000 polypeptide from mammalian brain. !$#cross-references MUID:92235102; PMID:1373732 !$#accession A38102 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-295 ##label BUR CLASSIFICATION #superfamily porin SUMMARY #length 295 #molecular-weight 31720 #checksum 1550 SEQUENCE /// ENTRY MMBYP #type complete TITLE porin - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein N2441; protein YNL055c; protein YNL1624 ORGANISM #formal_name Saccharomyces cerevisiae DATE 28-Dec-1987 #sequence_revision 23-Feb-1996 #text_change 16-Jun-2000 ACCESSIONS S58721; A22718; S62983; A05014 REFERENCE S58711 !$#authors Bergez, P.; Doignon, F.; Crouzet, M. !$#journal Yeast (1995) 11:967-974 !$#title The sequence of a 44 420 bp fragment located on the left arm !1of chromosome XIV from Saccharomyces cerevisiae. !$#cross-references MUID:96021608; PMID:8533472 !$#accession S58721 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-283 ##label BER !'##cross-references EMBL:U12141; NID:g1314216; PIDN:AAA99656.1; !1PID:g994830 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1994 REFERENCE A91035 !$#authors Mihara, K.; Sato, R. !$#journal EMBO J. (1985) 4:769-774 !$#title Molecular cloning and sequencing of cDNA for yeast porin, an !1outer mitochondrial membrane protein: a search for targeting !1signal in the primary structure. !$#cross-references MUID:85230548; PMID:2408884 !$#accession A22718 !'##molecule_type mRNA !'##residues 1-117,'E',119-283 ##label MIH !'##cross-references EMBL:X02324; NID:g4194; PIDN:CAA26184.1; PID:g4195 !'##note the authors translated the codon GAA for residue 118 as Gln REFERENCE S62975 !$#authors Bergez, P.; Doignon, F.; Crouzet, M. !$#submission submitted to the Protein Sequence Database, April 1996 !$#accession S62983 !'##molecule_type DNA !'##residues 1-283 ##label BEW !'##cross-references EMBL:Z71331; NID:g1301922; PIDN:CAA95926.1; !1PID:g1301923; GSPDB:GN00014; MIPS:YNL1624 !'##experimental_source strain S288C COMMENT This is the pore-forming protein of the mitochondrial outer !1membrane; it is synthesized in the cytosol and transported !1into the mitochondrion without transit peptide and without !1depending on electrochemical potential across the inner !1membrane. GENETICS !$#gene SGD:POR1; OMP2; VDAC; MIPS:YNL1624 !'##cross-references SGD:S0005000; MIPS:YNL055c !$#map_position 14L !$#genome nuclear CLASSIFICATION #superfamily porin KEYWORDS membrane protein; mitochondrion SUMMARY #length 283 #molecular-weight 30428 #checksum 2244 SEQUENCE /// ENTRY MMNCP #type complete TITLE porin - Neurospora crassa ORGANISM #formal_name Neurospora crassa DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS S07195 REFERENCE S07195 !$#authors Kleene, R.; Pfanner, N.; Pfaller, R.; Link, T.A.; Sebald, !1W.; Neupert, W.; Tropschug, M. !$#journal EMBO J. (1987) 6:2627-2633 !$#title Mitochondrial porin of Neurospora crassa: cDNA cloning, in !1vitro expression and import into mitochondria. !$#cross-references MUID:88054957; PMID:2960519 !$#accession S07195 !'##molecule_type mRNA !'##residues 1-283 ##label KLE !'##cross-references EMBL:X05824; NID:g3056; PIDN:CAA29264.1; PID:g3057 CLASSIFICATION #superfamily porin KEYWORDS membrane protein; mitochondrion SUMMARY #length 283 #molecular-weight 29999 #checksum 7947 SEQUENCE /// ENTRY RGUS1M #type complete TITLE exonuclease REC1 (EC 3.1.-.-) - smut fungus (Ustilago maydis) ORGANISM #formal_name Ustilago maydis #common_name corn smut DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jul-1999 ACCESSIONS S06912; S12481 REFERENCE S06912 !$#authors Holden, D.W.; Spanos, A.; Banks, G.R. !$#journal Nucleic Acids Res. (1989) 17:10489 !$#title Nucleotide sequence of the REC1 gene of Ustilago maydis. !$#cross-references MUID:90098882; PMID:2602156 !$#accession S06912 !'##molecule_type DNA !'##residues 1-522 ##label HOL !'##cross-references EMBL:X17663 REFERENCE S12481 !$#authors Holden, D.W. !$#submission submitted to the EMBL Data Library, November 1989 !$#accession S12481 !'##molecule_type DNA !'##residues 1-353,'Q',355-522 ##label HO2 !'##cross-references EMBL:X17663; NID:g5228; PIDN:CAA35660.1; PID:g5229 GENETICS !$#gene REC1 CLASSIFICATION #superfamily REC1 protein KEYWORDS DNA repair; exonuclease; hydrolase; nucleus SUMMARY #length 522 #molecular-weight 56859 #checksum 3107 SEQUENCE /// ENTRY MMECZB #type complete TITLE protein-histidine kinase osmosensor envZ (EC 2.7.3.-) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 05-Apr-1983 #sequence_revision 23-Mar-1995 #text_change 01-Mar-2002 ACCESSIONS B25024; A03433; A53514; G65135 REFERENCE A94671 !$#authors Comeau, D.E.; Ikenaka, K.; Tsung, K.; Inouye, M. !$#journal J. Bacteriol. (1985) 164:578-584 !$#title Primary characterization of the protein products of the !1Escherichia coli ompB locus: structure and regulation of !1synthesis of the OmpR and EnvZ proteins. !$#cross-references MUID:86033612; PMID:2997120 !$#accession B25024 !'##molecule_type DNA !'##residues 1-450 ##label COM !'##cross-references GB:J01656; GB:J01606; GB:M11202; NID:g453286; !1PIDN:AAA16242.1; PID:g147006 !'##experimental_source K12 REFERENCE A03433 !$#authors Mizuno, T.; Wurtzel, E.T.; Inouye, M. !$#journal J. Biol. Chem. (1982) 257:13692-13698 !$#title Osmoregulation of gene expression. II. DNA sequence of the !1envZ gene of the ompB operon of Escherichia coli and !1characterization of its gene product. !$#cross-references MUID:83056872; PMID:6292200 !$#accession A03433 !'##molecule_type DNA !'##residues 56-450 ##label MIZ !'##cross-references GB:J01656; GB:J01606; GB:M11202; NID:g453286 REFERENCE A53514 !$#authors Roberts, D.L.; Bennett, D.W.; Forst, S.A. !$#journal J. Biol. Chem. (1994) 269:8728-8733 !$#title Identification of the site of phosphorylation on the !1osmosensor, EnvZ, of Escherichia coli. !$#cross-references MUID:94179275; PMID:8132603 !$#accession A53514 !'##molecule_type protein !'##residues 238-248 ##label ROB REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65135 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-450 ##label BLAT !'##cross-references GB:AE000416; GB:U00096; NID:g2367219; !1PIDN:AAC76429.1; PID:g1789808; UWGP:b3404 !'##experimental_source strain K-12, substrain MG1655 COMMENT This essential membrane protein, together with ompR protein, !1is involved in the regulation of the expression of the genes !1of ompF and ompC proteins. GENETICS !$#gene envZ !$#map_position 75 min !$#note initiator codon overlaps terminator of 5'-region gene for !1OmpR protein for probable tranlational coupling CLASSIFICATION #superfamily envZ protein; sensor histidine kinase homology KEYWORDS autophosphorylation; membrane protein; phosphohistidine; !1phosphoprotein; phosphotransferase; sensory transduction; !1two-component regulatory system FEATURE !$212-437 #domain sensor histidine kinase homology #label SHK\ !$243 #binding_site phosphate (His) (covalent) (by !8autophosphorylation) #status experimental SUMMARY #length 450 #molecular-weight 50334 #checksum 2919 SEQUENCE /// ENTRY RGECFM #type complete TITLE sensor protein creC (EC 2.7.3.-) - Escherichia coli (strain K-12) ALTERNATE_NAMES pho regulon positive regulatory protein creC ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS S56623; F65255; C25038; S03764 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56623 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-474 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97295.1; !1PID:g537239 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65255 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-474 ##label BLAT !'##cross-references GB:AE000510; GB:U00096; NID:g1790858; !1PIDN:AAC77352.1; PID:g1790861; UWGP:b4399 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A25038 !$#authors Amemura, M.; Makino, K.; Shinagawa, H.; Nakata, A. !$#journal J. Bacteriol. (1986) 168:294-302 !$#title Nucleotide sequence of the phoM region of Escherichia coli: !1four open reading frames may constitute an operon. !$#cross-references MUID:87008393; PMID:3531171 !$#accession C25038 !'##molecule_type DNA !'##residues 1-76,'P',78-474 ##label AME !'##cross-references EMBL:M13608; NID:g147248; PIDN:AAA24375.1; !1PID:g147251 REFERENCE S03764 !$#authors Drury, L.S.; Buxton, R.S. !$#journal Mol. Microbiol. (1988) 2:109-119 !$#title Identification and sequencing of the Escherichia coli cet !1gene which codes for an inner membrane protein, mutation of !1which causes tolerance to colicin E2. !$#cross-references MUID:88216172; PMID:2835585 !$#accession S03764 !'##molecule_type DNA !'##residues 381-474 ##label DRU !'##cross-references EMBL:Y00538; NID:g41102; PIDN:CAA68601.1; !1PID:g809670 GENETICS !$#gene creC; phoM !$#map_position 100 min CLASSIFICATION #superfamily envZ protein; sensor histidine kinase homology KEYWORDS autophosphorylation; phosphohistidine; phosphoprotein; !1phosphotransferase; transmembrane protein FEATURE !$235-470 #domain sensor histidine kinase homology #label SHK\ !$265 #binding_site phosphate (His) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 474 #molecular-weight 52176 #checksum 9169 SEQUENCE /// ENTRY VZEBPT #type complete TITLE sensor kinase phoQ (EC 2.7.3.-) - Salmonella typhimurium ALTERNATE_NAMES virulence membrane protein phoQ ORGANISM #formal_name Salmonella typhimurium DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 11-Sep-1998 ACCESSIONS B32932 REFERENCE A32932 !$#authors Miller, S.I.; Kukral, A.M.; Mekalanos, J.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:5054-5058 !$#title A two-component regulatory system (phoP phoQ) controls !1Salmonella typhimurium virulence. !$#cross-references MUID:89296942; PMID:2544889 !$#accession B32932 !'##molecule_type DNA !'##residues 1-487 ##label MIL GENETICS !$#gene phoQ !$#map_position 25 min FUNCTION !$#description phosphorylates phoP in response to enviromental signals !$#note two-component regulatory system, phoP/phoQ, controls the !1expression of several genes, some of which are necessary for !1virulence; involved in regulation of acid phosphatase CLASSIFICATION #superfamily envZ protein; sensor histidine kinase homology KEYWORDS autophosphorylation; phosphohistidine; phosphoprotein; !1phosphotransferase; sensory transduction; transmembrane !1protein; two-component regulatory system FEATURE !$17-40 #domain transmembrane #status predicted #label TM1\ !$189-216 #domain transmembrane #status predicted #label TM2\ !$246-478 #domain sensor histidine kinase homology #label SHK\ !$277 #binding_site phosphate (His) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 487 #molecular-weight 55494 #checksum 5139 SEQUENCE /// ENTRY B41966 #type complete TITLE sensor kinase phoQ (EC 2.7.3.-) - Escherichia coli (strain K-12) ALTERNATE_NAMES sensor protein phoQ ORGANISM #formal_name Escherichia coli DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 01-Mar-2002 ACCESSIONS B41966; B41965; F64857; JU0380 REFERENCE A41966 !$#authors Kasahara, M.; Nakata, A.; Shinagawa, H. !$#journal J. Bacteriol. (1992) 174:492-498 !$#title Molecular analysis of the Escherichia coli phoP-phoQ operon. !$#cross-references MUID:92105017; PMID:1729240 !$#accession B41966 !'##molecule_type DNA !'##residues 1-486 ##label KAS !'##cross-references GB:D90393; NID:g216607; PIDN:BAA14391.1; !1PID:g216609 !'##experimental_source strain K-12 !'##note sequence extracted from NCBI backbone (NCBIN:75617, !1NCBIP:75621) REFERENCE A41965 !$#authors Groisman, E.A.; Heffron, F.; Solomon, F. !$#journal J. Bacteriol. (1992) 174:486-491 !$#title Molecular genetic analysis of the Escherichia coli phoP !1locus. !$#cross-references MUID:92105016; PMID:1530848 !$#accession B41965 !'##molecule_type DNA !'##residues 1-22 ##label GRO !'##note sequence extracted from NCBI backbone (NCBIN:75507, !1NCBIP:85375) REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64857 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-486 ##label BLAT !'##cross-references GB:AE000213; GB:U00096; NID:g1787371; !1PIDN:AAC74213.1; PID:g1787374; UWGP:b1129 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene phoQ !$#map_position 25 min FUNCTION !$#description phosphorylates phoP in response to enviromental signals !$#note two-component regulatory system, phoP/phoQ, controls the !1expression of several genes; involved in regulation of acid !1phosphatase CLASSIFICATION #superfamily envZ protein; sensor histidine kinase homology KEYWORDS autophosphorylation; phosphohistidine; phosphoprotein; !1phosphotransferase; sensory transduction; transmembrane !1protein; two-component regulatory system FEATURE !$17-44 #domain transmembrane #status predicted #label TM1\ !$191-218 #domain transmembrane #status predicted #label TM2\ !$246-477 #domain sensor histidine kinase homology #label SHK\ !$277 #binding_site phosphate (His) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 486 #molecular-weight 55299 #checksum 4675 SEQUENCE /// ENTRY D65222 #type complete TITLE hypothetical 60.6 kD protein in dcub-lysu intergenic region - Escherichia coli (strain K-12) ALTERNATE_NAMES hypothetical protein f543 ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS D65222; S56354 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65222 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-543 ##label BLAT !'##cross-references GB:AE000485; GB:U00096; NID:g1790563; !1PIDN:AAC77086.1; PID:g1790567; UWGP:b4125 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56354 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-340,'X',342-543 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97025.1; !1PID:g536970 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 GENETICS !$#gene yjdH CLASSIFICATION #superfamily two-component sensor histidine kinase; sensor !1histidine kinase homology KEYWORDS autophosphorylation; phosphohistidine; phosphoprotein FEATURE !$240-535 #domain sensor histidine kinase homology #status !8atypical #label SHK\ !$271 #binding_site phosphate (His) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 543 #molecular-weight 60550 #checksum 1198 SEQUENCE /// ENTRY A70009 #type complete TITLE two-component sensor histidine kinase homolog yufL - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A70009; E41835 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A70009 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-533 ##label KUN !'##cross-references GB:Z99120; GB:AL009126; NID:g2635613; !1PIDN:CAB15141.1; PID:g2635648 !'##experimental_source strain 168 REFERENCE A41835 !$#authors Mitchell, C.; Morris, P.W.; Vary, J.C. !$#journal J. Bacteriol. (1992) 174:2474-2477 !$#title Identification of proteins phosphorylated by ATP during !1sporulation of Bacillus subtilis. !$#cross-references MUID:92210489; PMID:1556067 !$#accession E41835 !'##molecule_type protein !'##residues 1,'P',3-5,'LK' ##label MIT !'##note this protein is phosphorylated during stationary phase but not !1during exponential growth GENETICS !$#gene yufL CLASSIFICATION #superfamily two-component sensor histidine kinase; sensor !1histidine kinase homology SUMMARY #length 533 #molecular-weight 58930 #checksum 5807 SEQUENCE /// ENTRY A69771 #type complete TITLE two-component sensor histidine kinase homolog ydbF - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A69771 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69771 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-535 ##label KUN !'##cross-references GB:Z99106; GB:AL009126; NID:g2632653; !1PIDN:CAB12252.1; PID:g2632745 !'##experimental_source strain 168 GENETICS !$#gene ydbF CLASSIFICATION #superfamily two-component sensor histidine kinase; sensor !1histidine kinase homology SUMMARY #length 535 #molecular-weight 59942 #checksum 7717 SEQUENCE /// ENTRY E69600 #type complete TITLE two-component sensor histidine kinase citS - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS E69600 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69600 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-542 ##label KUN !'##cross-references GB:Z99108; GB:AL009126; NID:g2633055; !1PIDN:CAB12587.1; PID:g2633082 !'##experimental_source strain 168 GENETICS !$#gene citS CLASSIFICATION #superfamily two-component sensor histidine kinase; sensor !1histidine kinase homology SUMMARY #length 542 #molecular-weight 59891 #checksum 9922 SEQUENCE /// ENTRY A64796 #type complete TITLE signal-transducing histidine kinase homolog b0619 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS A64796 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64796 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-552 ##label BLAT !'##cross-references GB:AE000167; GB:U00096; NID:g1786836; !1PIDN:AAC73720.1; PID:g1786837; UWGP:b0619 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily two-component sensor histidine kinase; sensor !1histidine kinase homology KEYWORDS transmembrane protein FEATURE !$22-38 #domain transmembrane #status predicted #label TM1\ !$186-202 #domain transmembrane #status predicted #label TM2 SUMMARY #length 552 #molecular-weight 61683 #checksum 8907 SEQUENCE /// ENTRY G65010 #type complete TITLE sensor protein evgS (EC 2.7.3.-) precursor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS G65010; JU0221; I41200 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65010 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1197 ##label BLAT !'##cross-references GB:AE000325; GB:U00096; NID:g1788709; !1PIDN:AAC75429.1; PID:g1788713; UWGP:b2370 !'##experimental_source strain K-12, substrain MG1655 REFERENCE JU0220 !$#authors Utsumi, R. !$#submission submitted to JIPID, January 1993 !$#description Newly identified genes involved in signal transduction of !1Escherichia coli K-12. !$#accession JU0221 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-151,'F',153-241,'PL',244-274,'R',276-419,'FE',422-738, !1'D',740-757,'K',759-760,'V',762-876,'L',878-1044,'H', !11046-1073,'Y',1075-1197 ##label UTS REFERENCE I41198 !$#authors Utsumi, R.; Katayama, S.; Taniguchi, M.; Horie, T.; Ikeda, !1M.; Igaki, S.; Nakagawa, H.; Miwa, A.; Tanabe, H.; Noda, M. !$#journal Gene (1994) 140:73-77 !$#title Newly identified genes involved in the signal transduction !1of Escherichia coli K-12. !$#cross-references MUID:94171083; PMID:8125343 !$#accession I41200 !'##status preliminary !'##molecule_type DNA !'##residues 1-151,'F',153-241,'PL',244-274,'R',276-419,'FE',422-738, !1'D',740-757,'K',759-760,'V',762-876,'L',878-1044,'H', !11046-1073,'Y',1075-1197 ##label RES !'##cross-references GB:D14008; NID:g456162; PIDN:BAA03108.1; !1PID:g216554 GENETICS !$#gene evgS CLASSIFICATION #superfamily evgS protein; response regulator homology KEYWORDS autophosphorylation; phosphohistidine; phosphoprotein; !1phosphotransferase; transmembrane protein FEATURE !$687-935 #domain sensor histidine kinase homology #label SHK\ !$961-1070 #domain response regulator homology #label RRH\ !$721 #binding_site phosphate (His) (covalent) #status !8predicted\ !$1009 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 1197 #molecular-weight 134741 #checksum 833 SEQUENCE /// ENTRY S17944 #type complete TITLE virulence sensor protein bvgS precursor - Bordetella bronchiseptica ORGANISM #formal_name Bordetella bronchiseptica DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S17944 REFERENCE S17943 !$#authors Arico, B.; Scarlato, V.; Monack, D.M.; Falkow, S.; Rappuoli, !1R. !$#journal Mol. Microbiol. (1991) 5:2481-2491 !$#title Structural and genetic analysis of the bvg locus in !1Bordetella species. !$#cross-references MUID:92167813; PMID:1791760 !$#accession S17944 !'##molecule_type DNA !'##residues 1-1238 ##label ARI !'##cross-references EMBL:X58355; NID:g39352; PIDN:CAA41252.1; !1PID:g39354 !'##experimental_source strain 7865 !'##note the authors translated the codon GAG for residue 134 as Gly and !1TCC for residue 1008 as Ser FUNCTION !$#description involved in signal transduction CLASSIFICATION #superfamily evgS protein; response regulator homology KEYWORDS autophosphorylation; phosphohistidine; phosphoprotein; !1phosphotransferase; transmembrane protein; two-component !1regulatory system; virulence regulation FEATURE !$1-30 #domain signal sequence #status predicted #label SIG\ !$31-1238 #product virulence sensor protein bvgS #status !8predicted #label MAT\ !$698-945 #domain sensor histidine kinase homology #label SHK\ !$975-1091 #domain response regulator homology #label RRH\ !$729 #active_site His (phosphohistidine intermediate) !8#status predicted\ !$1023 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 1238 #molecular-weight 134732 #checksum 3543 SEQUENCE /// ENTRY S17946 #type complete TITLE virulence sensor protein bvgS precursor - Bordetella parapertussis ORGANISM #formal_name Bordetella parapertussis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S17946 REFERENCE S17943 !$#authors Arico, B.; Scarlato, V.; Monack, D.M.; Falkow, S.; Rappuoli, !1R. !$#journal Mol. Microbiol. (1991) 5:2481-2491 !$#title Structural and genetic analysis of the bvg locus in !1Bordetella species. !$#cross-references MUID:92167813; PMID:1791760 !$#accession S17946 !'##molecule_type DNA !'##residues 1-1238 ##label ARI !'##cross-references EMBL:X52948; NID:g39727; PIDN:CAA37124.1; !1PID:g39729 !'##experimental_source strain 9305 !'##note the authors translated the codon GAG for residue 134 as Gly FUNCTION !$#description involved in signal transduction CLASSIFICATION #superfamily evgS protein; response regulator homology KEYWORDS autophosphorylation; phosphohistidine; phosphoprotein; !1phosphotransferase; transmembrane protein; two-component !1regulatory system; virulence regulation FEATURE !$1-30 #domain signal sequence #status predicted #label SIG\ !$31-1238 #product virulence sensor protein bvgS #status !8predicted #label MAT\ !$698-945 #domain sensor histidine kinase homology #label SHK\ !$975-1091 #domain response regulator homology #label RRH\ !$729 #active_site His (phosphohistidine intermediate) !8#status predicted\ !$1023 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 1238 #molecular-weight 134742 #checksum 1811 SEQUENCE /// ENTRY A40185 #type complete TITLE virulence protein bvgC - Bordetella pertussis CONTAINS protein-histidine kinase (EC 2.7.3.-) ORGANISM #formal_name Bordetella pertussis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A40185; A33729; S03541 REFERENCE A40185 !$#authors Arico, B. !$#submission submitted to GenBank, June 1989 !$#accession A40185 !'##molecule_type DNA !'##residues 1-1238 ##label AR1 !'##cross-references GB:M25401; NID:g144038; PIDN:AAA22970.1; !1PID:g144040 REFERENCE A33729 !$#authors Arico, B.; Miller, J.F.; Roy, C.; Stibitz, S.; Monack, D.; !1Falkow, S.; Gross, R.; Rappuoli, R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:6671-6675 !$#title Sequences required for expression of Bordetella pertussis !1virulence factors share homology with prokaryotic signal !1transduction proteins. !$#cross-references MUID:89367311; PMID:2549542 !$#accession A33729 !'##molecule_type DNA !'##residues 307-957;974-1092 ##label AR2 !'##cross-references GB:M25401 REFERENCE S03541 !$#authors Stibitz, S.; Aaronson, W.; Monack, D.; Falkow, S. !$#journal Nature (1989) 338:266-269 !$#title Phase variation in Bordetella pertussis by frameshift !1mutation in a gene for a novel two-component system. !$#cross-references MUID:89159416; PMID:2537932 !$#accession S03541 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 827-1067,'R',1069-1153 ##label STI CLASSIFICATION #superfamily evgS protein; response regulator homology KEYWORDS autophosphorylation; phosphohistidine; phosphoprotein; !1phosphotransferase; transmembrane protein FEATURE !$698-945 #domain sensor histidine kinase homology #label SHK\ !$975-1091 #domain response regulator homology #label RRH\ !$729 #active_site His (phosphohistidine intermediate) !8#status predicted\ !$1023 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 1238 #molecular-weight 134916 #checksum 7796 SEQUENCE /// ENTRY S75003 #type complete TITLE beta-lactamase regulatory protein - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein sll1005 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S75003 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75003 !'##status preliminary !'##molecule_type DNA !'##residues 1-269 ##label KAN !'##cross-references EMBL:D90902; GB:AB001339; NID:g1652027; !1PIDN:BAA17043.1; PID:g1652118 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily beta-lactamase regulatory protein; !1beta-lactamase regulatory protein homology FEATURE !$20-264 #domain beta-lactamase regulatory protein homology !8#label BLR SUMMARY #length 269 #molecular-weight 30244 #checksum 8736 SEQUENCE /// ENTRY H64069 #type complete TITLE beta-lactamase regulatory protein homolog - Haemophilus influenzae ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS H64069 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession H64069 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-263 ##label TIGR !'##cross-references GB:U32728; GB:L42023; NID:g1573425; !1PIDN:AAC22118.1; PID:g1573434; TIGR:HI0460 !'##experimental_source strain Rd KW20 CLASSIFICATION #superfamily beta-lactamase regulatory protein; !1beta-lactamase regulatory protein homology FEATURE !$14-259 #domain beta-lactamase regulatory protein homology !8#label BLR SUMMARY #length 263 #molecular-weight 30519 #checksum 4627 SEQUENCE /// ENTRY S66088 #type complete TITLE conserved hypothetical protein yabN - Bacillus subtilis ALTERNATE_NAMES beta-lactamase regulatory protein homolog yabN ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S66088; E69739 REFERENCE S65967 !$#authors Ogasawara, N.; Nakai, S.; Yoshikawa, H. !$#journal DNA Res. (1994) 1:1-14 !$#title Systematic sequencing of the 180 kilobase region of the !1Bacillus subtilis chromosome containing the replication !1origin. !$#cross-references MUID:96051385; PMID:7584024 !$#accession S66088 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-489 ##label OGA !'##cross-references EMBL:D26185; NID:g467326; PIDN:BAA05293.1; !1PID:g467447 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1993 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69739 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-489 ##label KUN !'##cross-references GB:Z99104; GB:AL009126; NID:g2632267; !1PIDN:CAB11834.1; PID:g2632325 !'##experimental_source strain 168 GENETICS !$#gene yabN CLASSIFICATION #superfamily beta-lactamase regulatory protein homolog; !1beta-lactamase regulatory protein homology FEATURE !$242-483 #domain beta-lactamase regulatory protein homology !8#label BLR SUMMARY #length 489 #molecular-weight 56106 #checksum 2207 SEQUENCE /// ENTRY BVECCC #type complete TITLE sensor protein rcsC (EC 2.7.3.-) - Escherichia coli (strain K-12) ALTERNATE_NAMES regulatory protein rcsC ORGANISM #formal_name Escherichia coli DATE 30-Jun-1991 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS H64991; JV0069; A48659 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64991 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-933 ##label BLAT !'##cross-references GB:AE000311; GB:U00096; NID:g1788547; !1PIDN:AAC75278.1; PID:g1788548; UWGP:b2218 !'##experimental_source strain K-12, substrain MG1655 REFERENCE JV0068 !$#authors Stout, V.; Gottesman, S. !$#journal J. Bacteriol. (1990) 172:659-669 !$#title RcsB and RcsC: a two-component regulator of capsule !1synthesis in Escherichia coli. !$#cross-references MUID:90130299; PMID:2404948 !$#accession JV0069 !'##molecule_type DNA !'##residues 1-112,'IG',115-918,'S',920-933 ##label STO !'##cross-references GB:M28242; NID:g147524; PIDN:AAA24503.1; !1PID:g147525 !'##experimental_source strain K12 REFERENCE A48659 !$#authors Jayaratne, P.; Keenleyside, W.J.; MacLachlan, P.R.; Dodgson, !1C.; Whitfield, C. !$#journal J. Bacteriol. (1993) 175:5384-5394 !$#title Characterization of rcsB and rcsC from Escherichia coli O9: !1K30:H12 and examination of the role of the rcs regulatory !1system in expression of group I capsular polysaccharides. !$#cross-references MUID:93374832; PMID:8366025 !$#accession A48659 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-112,'IG',115-298,'V',300-759,'E',761-873,'T',875-921,'V', !1923-931,'E',933 ##label JAY !'##cross-references GB:L11272; NID:g147527; PIDN:AAA24505.1; !1PID:g147528 !'##experimental_source strain K30 (09:K30:H12) COMMENT This protein acts as the sensor of the two-component !1regulatory system to stimulate capsule synthesis from cps !1genes; rcsB protein, the other component, acts as the !1receiver or effector. GENETICS !$#gene rcsC !$#map_position 48 min CLASSIFICATION #superfamily rcsC protein; response regulator homology KEYWORDS autophosphorylation; capsule synthesis; phosphohistidine; !1phosphoprotein; phosphotransferase; transmembrane protein; !1two-component regulatory system FEATURE !$4-26 #domain transmembrane #status predicted #label TM1\ !$298-318 #domain transmembrane #status predicted #label TM2\ !$811-920 #domain response regulator homology #label RRH\ !$463 #binding_site phosphate (His) (covalent) #status !8predicted\ !$859 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 933 #molecular-weight 104587 #checksum 7969 SEQUENCE /// ENTRY RGECGL #type complete TITLE nitrogen regulation protein II (EC 2.7.3.-) ntrB - Escherichia coli (strain K-12) ALTERNATE_NAMES regulatory protein glnL ORGANISM #formal_name Escherichia coli DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 01-Mar-2002 ACCESSIONS A30377; S40814; B23970; H65191; A39765; Q00553 REFERENCE A30377 !$#authors Miranda-Rios, J.; Sanchez-Pescador, R.; Urdea, M.; !1Covarrubias, A.A. !$#journal Nucleic Acids Res. (1987) 15:2757-2770 !$#title The complete nucleotide sequence of the glnALG operon of !1Escherichia coli K12. !$#cross-references MUID:87174797; PMID:2882477 !$#accession A30377 !'##molecule_type DNA !'##residues 1-349 ##label MIR !'##cross-references EMBL:X05173; NID:g41562; PIDN:CAA28807.1; !1PID:g41564 !'##experimental_source K-12 REFERENCE S40802 !$#authors Plunkett III, G.; Burland, V.; Daniels, D.L.; Blattner, F.R. !$#journal Nucleic Acids Res. (1993) 21:3391-3398 !$#title Analysis of the Escherichia coli genome. III. DNA sequence !1of the region from 87.2 to 89.2 minutes. !$#cross-references MUID:93347969; PMID:8346018 !$#accession S40814 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-349 ##label PLU !'##cross-references EMBL:L19201; NID:g304961; PIDN:AAB03003.1; !1PID:g304974 !'##experimental_source strain K-12, substrain MG1655 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1993 REFERENCE A91533 !$#authors Rocha, M.; Vazquez, M.; Garciarrubio, A.; Covarrubias, A.A. !$#journal Gene (1985) 37:91-99 !$#title Nucleotide sequence of the glnA-glnL intercistronic region !1of Escherichia coli. !$#cross-references MUID:86031370; PMID:2865194 !$#accession B23970 !'##molecule_type DNA !'##residues 1-24 ##label ROC !'##cross-references GB:K02176; GB:M11581; NID:g146160; PIDN:AAA23881.1; !1PID:g146162 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65191 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-349 ##label BLAT !'##cross-references GB:AE000462; GB:U00096; NID:g1790295; !1PIDN:AAC76866.1; PID:g1790300; UWGP:b3869 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A39765 !$#authors Ninfa, A.J.; Bennett, R.L. !$#journal J. Biol. Chem. (1991) 266:6888-6893 !$#title Identification of the site of autophosphorylation of the !1bacterial protein kinase/phosphatase NR-II. !$#cross-references MUID:91201336; PMID:2016302 !$#accession A39765 !'##status preliminary !'##molecule_type protein !'##residues 2-11;136-142;158-162,'X',164-169 ##label NIN GENETICS !$#gene glnL; ntrB !$#map_position 87 min FUNCTION !$#description de-uridylylated P-II forms a complex with nitrogen !1regulation protein II (ntrB); ntrB, when complexed with !1de-uridylylated P-II, dephosphorylates nitrogen regulation !1protein I (ntrC); the uridylylated form of P-II does not !1complex with ntrB; free ntrB phosphorylates nitrogen !1regulation protein I (ntrC) !$#note phosphorylated nitrogen regulation protein I (ntrC) !1activates transcription of the glutamine synthase (glnA) !1gene CLASSIFICATION #superfamily glnL regulatory protein II; sensor histidine !1kinase homology KEYWORDS ATP; autophosphorylation; phosphohistidine; phosphoprotein; !1phosphotransferase; signal transduction FEATURE !$104-346 #domain sensor histidine kinase homology #label SHK\ !$139 #binding_site phosphate (His) (covalent) (by !8autophosphorylation) #status predicted\ !$329 #binding_site ATP (Lys) #status predicted SUMMARY #length 349 #molecular-weight 38556 #checksum 8402 SEQUENCE /// ENTRY RGECFR #type complete TITLE sensor kinase (EC 2.7.3.-) phoR - Escherichia coli (strain K-12) ALTERNATE_NAMES phosphate regulon sensor protein phoR ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 01-Mar-2002 ACCESSIONS A25557; H64768; S11888 REFERENCE A25557 !$#authors Makino, K.; Shinagawa, H.; Amemura, M.; Nakata, A. !$#journal J. Mol. Biol. (1986) 192:549-556 !$#title Nucleotide sequence of the phoR gene, a regulatory gene for !1the phosphate regulon of Escherichia coli. !$#cross-references MUID:87169739; PMID:3550103 !$#accession A25557 !'##molecule_type DNA !'##residues 1-431 ##label MAK !'##cross-references GB:X04704; NID:g42393; PIDN:CAA28409.1; PID:g581188 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64768 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-431 ##label BLAT !'##cross-references GB:AE000146; GB:U00096; NID:g1786596; !1PIDN:AAC73503.1; PID:g1786600; UWGP:b0400 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S11888 !$#authors Yamada, M.; Makino, K.; Shinagawa, H.; Nakata, A. !$#journal Mol. Gen. Genet. (1990) 220:366-372 !$#title Regulation of the phosphate regulon of Escherichia coli: !1properties of phoR deletion mutants and subcellular !1localization of PhoR protein. !$#cross-references MUID:90251245; PMID:2187152 !$#accession S11888 !'##molecule_type DNA !'##residues 1-13 ##label YAM GENETICS !$#gene phoR !$#map_position 9 min !$#start_codon GTG FUNCTION !$#description transcription regulation; involved in transcription !1activation of the phosphate regulon !$#note phosphorylated phoR protein phosphorylates phoB protein; !1phosphorylated phoB protein activates transcription of the !1phosphate regulon; phoR protein is phosphorylated upon !1phosphate limitation CLASSIFICATION #superfamily phosphate regulon regulatory protein; sensor !1histidine kinase homology KEYWORDS autophosphorylation; membrane protein; phosphate transport; !1phosphohistidine; phosphoprotein; phosphotransferase; !1two-component regulatory system FEATURE !$10-26 #domain transmembrane #status predicted #label TM1\ !$28-44 #domain transmembrane #status predicted #label TM2\ !$160-422 #domain sensor histidine kinase homology #label SHK\ !$213 #binding_site phosphate (His) (covalent) #status !8predicted\ !$213 #binding_site phosphate (His) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 431 #molecular-weight 49629 #checksum 2106 SEQUENCE /// ENTRY S75782 #type complete TITLE methanol dehydrogenase regulatory protein - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein slr0835 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S75782 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75782 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-303 ##label KAN !'##cross-references EMBL:D64003; GB:AB001339; NID:g1001200; !1PIDN:BAA10517.1; PID:g1001272 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene moxR CLASSIFICATION #superfamily methanol dehydrogenase regulatory protein SUMMARY #length 303 #molecular-weight 33452 #checksum 9945 SEQUENCE /// ENTRY B69553 #type complete TITLE methanol dehydrogenase regulatory protein (moxR) homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B69553 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession B69553 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-324 ##label KLE !'##cross-references GB:AE001108; GB:AE000782; NID:g2689431; !1PIDN:AAB91247.1; PID:g2650675; TIGR:AF2425 CLASSIFICATION #superfamily methanol dehydrogenase regulatory protein SUMMARY #length 324 #molecular-weight 36609 #checksum 7184 SEQUENCE /// ENTRY S74593 #type complete TITLE MorR protein - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES hypothetical protein slr1416 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S74593 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74593 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-314 ##label KAN !'##cross-references EMBL:D90900; GB:AB001339; NID:g1651768; !1PIDN:BAA16745.1; PID:g1651818 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene morR CLASSIFICATION #superfamily methanol dehydrogenase regulatory protein SUMMARY #length 314 #molecular-weight 35091 #checksum 2701 SEQUENCE /// ENTRY H70121 #type complete TITLE methanol dehydrogenase regulator (moxR) homolog - Lyme disease spirochete ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS H70121 REFERENCE A70100 !$#authors Fraser, C.M.; Casjens, S.; Huang, W.M.; Sutton, G.G.; !1Clayton, R.; Lathigra, R.; White, O.; Ketchum, K.A.; Dodson, !1R.; Hickey, E.K.; Gwinn, M.; Dougherty, B.; Tomb, J.F.; !1Fleischmann, R.D.; Richardson, D.; Peterson, J.; Kerlavage, !1A.R.; Quackenbush, J.; Salzberg, S.; Hanson, M.; Vugt, R.V.; !1Palmer, N.; Adams, M.D.; Gocayne, J.; Weidman, J.; !1Utterback, T.; Watthey, L.; McDonald, L.; Artiach, P.; !1Bowman, C.; Garland, S.; Fujii, C.; Cotton, M.D.; Horst, K.; !1Roberts, K.; Hatch, B.; Smith, H.O.; Venter, J.C. !$#journal Nature (1997) 390:580-586 !$#title Genomic sequence of a Lyme disease spirochaete, Borrelia !1burgdorferi. !$#cross-references MUID:98065943; PMID:9403685 !$#accession H70121 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-337 ##label KLE !'##cross-references GB:AE001128; GB:AE000783; NID:g2688057; !1PIDN:AAC66559.1; PID:g2688061; TIGR:BB0176 !'##experimental_source strain B31 CLASSIFICATION #superfamily methanol dehydrogenase regulatory protein SUMMARY #length 337 #molecular-weight 37779 #checksum 3216 SEQUENCE /// ENTRY C69791 #type complete TITLE methanol dehydrogenase regulation homolog yeaC - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS C69791 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69791 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-320 ##label KUN !'##cross-references GB:Z99107; GB:AL009126; NID:g2632866; !1PIDN:CAB12452.1; PID:g2632946 !'##experimental_source strain 168 GENETICS !$#gene yeaC CLASSIFICATION #superfamily methanol dehydrogenase regulatory protein SUMMARY #length 320 #molecular-weight 35803 #checksum 7602 SEQUENCE /// ENTRY H70321 #type complete TITLE conserved hypothetical protein aq_240 - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS H70321 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession H70321 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-300 ##label AQF !'##cross-references GB:AE000680; NID:g2982948; PIDN:AAC06575.1; !1PID:g2982960; GB:AE000657 !'##experimental_source strain VF5 GENETICS !$#gene aq_240 CLASSIFICATION #superfamily methanol dehydrogenase regulatory protein SUMMARY #length 300 #molecular-weight 33273 #checksum 5165 SEQUENCE /// ENTRY S43189 #type complete TITLE hypothetical protein - Pseudomonas aeruginosa ORGANISM #formal_name Pseudomonas aeruginosa DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S43189 REFERENCE S43188 !$#authors Strych, U.; Wohlfarth, S.; Winkler, U.K. !$#submission submitted to the EMBL Data Library, April 1992 !$#accession S43189 !'##status preliminary !'##molecule_type DNA !'##residues 1-263 ##label STR !'##cross-references EMBL:X65613; NID:g469099; PIDN:CAA46565.1; !1PID:g469101 CLASSIFICATION #superfamily methanol dehydrogenase regulatory protein SUMMARY #length 263 #molecular-weight 29001 #checksum 476 SEQUENCE /// ENTRY S03320 #type complete TITLE regulatory protein ntrB - Rhodobacter capsulatus ALTERNATE_NAMES regulatory protein nifR2 ORGANISM #formal_name Rhodobacter capsulatus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S03320; S37481; S34982 REFERENCE S03318 !$#authors Jones, R.; Haselkorn, R. !$#journal Mol. Gen. Genet. (1989) 215:507-516 !$#title The DNA sequence of the Rhodobacter capsulatus ntrA, ntrB !1and ntrC gene analogues required for nitrogen fixation. !$#cross-references MUID:89218961; PMID:2710108 !$#accession S03320 !'##molecule_type DNA !'##residues 1-356 ##label JON !'##cross-references EMBL:X12359; NID:g46077; PIDN:CAA30921.1; !1PID:g46078 REFERENCE S37299 !$#authors Kranz, R. !$#submission submitted to the EMBL Data Library, March 1993 !$#accession S37481 !'##molecule_type DNA !'##residues 1-356 ##label KRA !'##cross-references EMBL:X72382; NID:g313162; PIDN:CAA51074.1; !1PID:g313165 REFERENCE S34980 !$#authors Foster-Hartnett, D.; Cullen, P.J.; Gabbert, K.K.; Kranz, !1R.G. !$#journal Mol. Microbiol. (1993) 8:903-914 !$#title Sequence, genetic, and lacZ fusion analyses of a !1nifR3-ntrB-ntrC operon in Rhodobacter capsulatus. !$#cross-references MUID:93360820; PMID:8355615 !$#accession S34982 !'##molecule_type DNA !'##residues 1-19 ##label FOS !'##cross-references EMBL:X72382 GENETICS !$#gene ntrB; nifR2 CLASSIFICATION #superfamily regulatory protein ntrB; sensor histidine !1kinase homology KEYWORDS autophosphorylation; phosphohistidine; phosphoprotein FEATURE !$106-350 #domain sensor histidine kinase homology #label SHK\ !$140 #binding_site phosphate (His) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 356 #molecular-weight 38212 #checksum 2948 SEQUENCE /// ENTRY A26499 #type complete TITLE regulatory protein ntrB - Bradyrhizobium sp. ALTERNATE_NAMES nitrogen assimilation regulatory protein C ORGANISM #formal_name Bradyrhizobium sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A26499 REFERENCE A94133 !$#authors Nixon, B.T.; Ronson, C.W.; Ausubel, F.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:7850-7854 !$#title Two-component regulatory systems responsive to environmental !1stimuli share strongly conserved domains with the nitrogen !1assimilation regulatory genes ntrB and ntrC. !$#cross-references MUID:87017043; PMID:3020561 !$#accession A26499 !'##molecule_type DNA !'##residues 1-377 ##label NIX !'##cross-references GB:M14227; NID:g152129; PIDN:AAA26238.1; !1PID:g152130 !'##experimental_source strain RP501 from Parasponia CLASSIFICATION #superfamily regulatory protein ntrB; sensor histidine !1kinase homology KEYWORDS autophosphorylation; phosphohistidine; phosphoprotein FEATURE !$114-363 #domain sensor histidine kinase homology #label SHK\ !$149 #binding_site phosphate (His) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 377 #molecular-weight 41292 #checksum 950 SEQUENCE /// ENTRY S36202 #type complete TITLE regulatory protein ntrB - Rhizobium leguminosarum bv. phaseoli ORGANISM #formal_name Rhizobium leguminosarum bv. phaseoli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S36202 REFERENCE S36201 !$#authors Patriarca, E.J.; Riccio, A.; Tate, R.; Colonna-Romano, S.; !1Iaccarino, M.; Defez, R. !$#journal Mol. Microbiol. (1993) 9:569-577 !$#title The ntrBC genes of Rhizobium leguminosarum are part of a !1complex operon subject to negative regulation. !$#cross-references MUID:94018651; PMID:8412703 !$#accession S36202 !'##molecule_type DNA !'##residues 1-383 ##label PAT !'##cross-references EMBL:X71436; NID:g402781; PIDN:CAA50568.1; !1PID:g402783 !'##note the authors translated the codon GTC for residue 141 as Val and !1AAT for residue 305 as Asn GENETICS !$#gene ntrB CLASSIFICATION #superfamily regulatory protein ntrB; sensor histidine !1kinase homology KEYWORDS autophosphorylation; phosphohistidine; phosphoprotein FEATURE !$115-363 #domain sensor histidine kinase homology #label SHK\ !$150 #binding_site phosphate (His) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 383 #molecular-weight 41193 #checksum 6650 SEQUENCE /// ENTRY MMCWTH #type complete TITLE major outer membrane protein precursor - Chlamydia trachomatis (serotype H) ORGANISM #formal_name Chlamydia trachomatis DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 21-Jul-2000 ACCESSIONS S06589 REFERENCE S06589 !$#authors Hamilton, P.T.; Malinowski, D.P. !$#journal Nucleic Acids Res. (1989) 17:8366 !$#title Nucleotide sequence of the major outer membrane protein gene !1from Chlamydia trachomatis serovar H. !$#cross-references MUID:90045958; PMID:2813066 !$#accession S06589 !'##molecule_type DNA !'##residues 1-397 ##label HAM !'##cross-references EMBL:X16007; NID:g40720; PIDN:CAA34145.1; !1PID:g4377420 CLASSIFICATION #superfamily Chlamydia major outer membrane protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-397 #product major outer membrane protein #status !8predicted #label MAT SUMMARY #length 397 #molecular-weight 42946 #checksum 4595 SEQUENCE /// ENTRY MMCWTC #type complete TITLE major outer membrane protein precursor - Chlamydia trachomatis (serotype C) ORGANISM #formal_name Chlamydia trachomatis DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jul-1999 ACCESSIONS S11011 REFERENCE S11010 !$#authors Stephens, R.S.; Sanchez-Pescador, R.; Wagar, E.A.; Inouye, !1C.; Urdea, M.S. !$#journal J. Bacteriol. (1987) 169:3879-3885 !$#title Diversity of Chlamydia trachomatis major outer membrane !1protein genes. !$#cross-references MUID:87307955; PMID:3040664 !$#accession S11011 !'##molecule_type DNA !'##residues 1-397 ##label STE !'##cross-references EMBL:M17343; NID:g144600; PIDN:AAA23156.1; !1PID:g144601 !'##note the authors translated the codon ATA for residue 102 as Thr, !1CGA for residue 324 as Pro, and ACT for residue 326 as Ile GENETICS !$#gene omp1 CLASSIFICATION #superfamily Chlamydia major outer membrane protein KEYWORDS disulfide bond; membrane protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-397 #product major outer membrane protein #status !8predicted #label MAT SUMMARY #length 397 #molecular-weight 42892 #checksum 7600 SEQUENCE /// ENTRY MMCWTE #type complete TITLE major outer membrane protein precursor - Chlamydia trachomatis (serotype E) ORGANISM #formal_name Chlamydia trachomatis DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS S10201 REFERENCE S10201 !$#authors Peterson, E.M.; Markoff, B.A.; de la Maza, L.M. !$#journal Nucleic Acids Res. (1990) 18:3414 !$#title The major outer membrane protein nucleotide sequence of !1Chlamydia trachomatis, serovar E. !$#cross-references MUID:90287737; PMID:2356137 !$#accession S10201 !'##status translation not shown !'##molecule_type DNA !'##residues 1-393 ##label PET !'##cross-references EMBL:X52557; NID:g40713; PIDN:CAA36791.1; !1PID:g40714 CLASSIFICATION #superfamily Chlamydia major outer membrane protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-393 #product major outer membrane protein #status !8predicted #label MAT SUMMARY #length 393 #molecular-weight 42424 #checksum 1801 SEQUENCE /// ENTRY MMCWTB #type complete TITLE major outer membrane protein precursor - Chlamydia trachomatis (serotype B) ORGANISM #formal_name Chlamydia trachomatis DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jul-1999 ACCESSIONS S11010; S12473 REFERENCE S11010 !$#authors Stephens, R.S.; Sanchez-Pescador, R.; Wagar, E.A.; Inouye, !1C.; Urdea, M.S. !$#journal J. Bacteriol. (1987) 169:3879-3885 !$#title Diversity of Chlamydia trachomatis major outer membrane !1protein genes. !$#cross-references MUID:87307955; PMID:3040664 !$#accession S11010 !'##molecule_type DNA !'##residues 1-394 ##label ST1 !'##cross-references EMBL:M17342 REFERENCE S12473 !$#authors Stephens, R.S. !$#submission submitted to the EMBL Data Library, January 1988 !$#accession S12473 !'##molecule_type DNA !'##residues 1-170,'S',172-394 ##label ST2 !'##cross-references EMBL:M17342; NID:g144598; PIDN:AAA23155.1; !1PID:g144599 GENETICS !$#gene omp1 CLASSIFICATION #superfamily Chlamydia major outer membrane protein KEYWORDS disulfide bond; membrane protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-394 #product major outer membrane protein #status !8predicted #label MAT SUMMARY #length 394 #molecular-weight 42528 #checksum 6767 SEQUENCE /// ENTRY MMCWTF #type complete TITLE major outer membrane protein precursor - Chlamydia trachomatis (serotype F) ORGANISM #formal_name Chlamydia trachomatis DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS S08463 REFERENCE S08463 !$#authors Zhang, Y.X.; Morrison, S.G.; Caldwell, H.D. !$#journal Nucleic Acids Res. (1990) 18:1061 !$#title The nucleotide sequence of major outer membrane protein gene !1of Chlamydia trachomatis serovar F. !$#cross-references MUID:90192102; PMID:2315025 !$#accession S08463 !'##molecule_type DNA !'##residues 1-395 ##label ZHA !'##cross-references EMBL:X52080; NID:g40705; PIDN:CAA36299.1; !1PID:g40706 CLASSIFICATION #superfamily Chlamydia major outer membrane protein KEYWORDS disulfide bond; membrane protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-395 #product major outer membrane protein #status !8predicted #label MAT SUMMARY #length 395 #molecular-weight 42586 #checksum 8968 SEQUENCE /// ENTRY MMCWP3 #type complete TITLE major outer membrane protein precursor - Chlamydophila psittaci (strain S26/3) ORGANISM #formal_name Chlamydophila psittaci, Chlamydia psittaci DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 31-Mar-2000 ACCESSIONS S08770 REFERENCE S08770 !$#authors Herring, A.J.; Tan, T.W.; Baxter, S.; Inglis, N.F.; Dunbar, !1S. !$#journal FEMS Microbiol. Lett. (1989) 65:153-158 !$#title Sequence analysis of the major outer membrane protein gene !1of an ovine abortion strain of Chlamydia psittaci. !$#accession S08770 !'##molecule_type DNA !'##residues 1-389 ##label HER !'##cross-references EMBL:X51859; NID:g40600; PIDN:CAA36152.1; !1PID:g40601 CLASSIFICATION #superfamily Chlamydia major outer membrane protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-389 #product major outer membrane protein #status !8predicted #label MAT SUMMARY #length 389 #molecular-weight 41883 #checksum 5897 SEQUENCE /// ENTRY MMCWPM #type complete TITLE major outer membrane protein precursor - Chlamydophila psittaci (strain A22/M) ORGANISM #formal_name Chlamydophila psittaci, Chlamydia psittaci DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 31-Mar-2000 ACCESSIONS S05954 REFERENCE S05954 !$#authors Pickett, M.A.; Everson, J.S.; Clarke, I.N. !$#journal FEMS Microbiol. Lett. (1988) 55:229-234 !$#title Chlamydia psittaci ewe abortion agent: complete nucleotide !1sequence of the major outer membrane protein gene. !$#accession S05954 !'##molecule_type DNA !'##residues 1-402 ##label PIC !'##cross-references EMBL:X12647; NID:g40604; PIDN:CAA31177.1; !1PID:g40605 CLASSIFICATION #superfamily Chlamydia major outer membrane protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-402 #product major outer membrane protein #status !8predicted #label MAT SUMMARY #length 402 #molecular-weight 43277 #checksum 8083 SEQUENCE /// ENTRY B39439 #type complete TITLE 60K cysteine-rich outer membrane protein 1 precursor - Chlamydophila psittaci ORGANISM #formal_name Chlamydophila psittaci, Chlamydia psittaci DATE 21-Feb-1992 #sequence_revision 27-Jun-1994 #text_change 31-Mar-2000 ACCESSIONS B39439; S12603 REFERENCE A39439 !$#authors Everett, K.D.E.; Hatch, T.P. !$#journal J. Bacteriol. (1991) 173:3821-3830 !$#title Sequence analysis and lipid modification of the !1cysteine-rich envelope proteins of Chlamydia psittaci 6BC. !$#cross-references MUID:91267949; PMID:2050637 !$#accession B39439 !'##molecule_type DNA !'##residues 1-557 ##label EVE !'##cross-references GB:M61116; NID:g144489; PIDN:AAB61619.1; !1PID:g144491 !'##experimental_source strain 6BC REFERENCE S12603 !$#authors Watson, M.W.; Lambden, P.R.; Clarke, I.N. !$#journal Nucleic Acids Res. (1990) 18:5300 !$#title The nucleotide sequence of the 60kDa cysteine rich outer !1membrane protein of Chlamydia psittaci strain EAE/A22/M. !$#cross-references MUID:90384851; PMID:2402464 !$#accession S12603 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-44,'A',46-72,'E',74-557 ##label WAT !'##cross-references GB:X53512; NID:g40625; PIDN:CAA37592.1; PID:g40627 !'##experimental_source strain EAE/A22/M FUNCTION !$#description associated with the differentiation of reticulate bodies !1into elementary bodies; it is essential for the structural !1integrity of the outer envelope of the elementary bodies. It !1may also be an important virulence factor. CLASSIFICATION #superfamily 60K cysteine-rich outer membrane protein KEYWORDS membrane protein; virulence FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-40 #domain propeptide #status predicted #label PRO\ !$41-557 #product 60K cysteine-rich outer membrane protein 1 !8#status predicted #label MAT SUMMARY #length 557 #molecular-weight 59787 #checksum 9655 SEQUENCE /// ENTRY S12602 #type complete TITLE 60K cysteine-rich outer membrane protein precursor [similarity] - Chlamydophila pneumoniae (strains CWL029 and AR39) ORGANISM #formal_name Chlamydophila pneumoniae, Chlamydia pneumoniae DATE 30-Sep-1993 #sequence_revision 27-Jun-1994 #text_change 11-May-2000 ACCESSIONS S12602; H72063; A81604 REFERENCE S12602 !$#authors Watson, M.W.; Al-Mahdawi, S.; Lamden, P.R.; Clarke, I.N. !$#journal Nucleic Acids Res. (1990) 18:5299 !$#title The nucleotide sequence of the 60kDa cysteine rich outer !1membrane protein of Chlamydia pneumoniae strain IOL-207. !$#cross-references MUID:90384850; PMID:2402463 !$#accession S12602 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-556 ##label WAT !'##cross-references GB:X53511; NID:g550564; PIDN:CAA37590.1; !1PID:g550566 !'##experimental_source isolate IOL-207 REFERENCE A72000 !$#authors Kalman, S.; Mitchell, W.; Marathe, R.; Lammel, C.; Fan, J.; !1Olinger, L.; Grimwood, J.; Davis, R.W.; Stephens, R.S. !$#journal Nature Genet. (1999) 21:385-389 !$#title Comparative genomes of Clamydia pneumoniae and C. !1trachomatis. !$#cross-references MUID:99206606; PMID:10192388 !$#accession H72063 !'##molecule_type DNA !'##residues 1-556 ##label ARN !'##cross-references GB:AE001640; GB:AE001363; NID:g4376845; !1PIDN:AAD18697.1; PID:g4376849 !'##experimental_source strain CWL029 REFERENCE A81500 !$#authors Read, T.D.; Brunham, R.C.; Shen, C.; Gill, S.R.; Heidelberg, !1J.F.; White, O.; Hickey, E.K.; Peterson, J.; Utterback, T.; !1Berry, K.; Bass, S.; Linher, K.; Weidman, J.; Khouri, H.; !1Craven, B.; Bowman, C.; Dodson, R.; Gwinn, M.; Nelson, W.; !1DeBoy, R.; Kolonay, J.; McClarty, G.; Salzberg, S.L.; Eisen, !1J.; Fraser, C.M. !$#journal Nucleic Acids Res. (2000) 28:1397-1406 !$#title Genome sequences of Chlamydia trachomatis MoPn and Chlamydia !1pneumoniae AR39. !$#cross-references MUID:20150255; PMID:10684935 !$#accession A81604 !'##molecule_type DNA !'##residues 1-556 ##label REA !'##cross-references GB:AE002180; GB:AE002161; NID:g7189117; !1PIDN:AAF38068.1; PID:g7189126; GSPDB:GN00122; TIGR:CP0195 !'##experimental_source strain AR39, HL cells COMMENT This protein is associated with the differentiation of !1reticulate bodies into elementary bodies; it is essential !1for the structural integrity of the outer envelope of the !1elementary bodies. It may also be an important virulence !1factor. GENETICS !$#gene omcB; CP0195 CLASSIFICATION #superfamily 60K cysteine-rich outer membrane protein KEYWORDS membrane protein; virulence FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-40 #domain propeptide #status predicted #label PRO\ !$41-556 #product 60K cysteine-rich outer membrane protein !8#status predicted #label MAT SUMMARY #length 556 #molecular-weight 59719 #checksum 8952 SEQUENCE /// ENTRY A32244 #type complete TITLE 60K cysteine-rich outer membrane protein 2 precursor, serotype L1 and L2 - Chlamydia trachomatis ORGANISM #formal_name Chlamydia trachomatis DATE 12-Oct-1989 #sequence_revision 27-Jun-1994 #text_change 16-Jul-1999 ACCESSIONS A32244; A43584; A36043; A30472; JT0419; S18981; S24277 REFERENCE A32244 !$#authors Allen, J.E.; Stephens, R.S. !$#journal J. Bacteriol. (1989) 171:285-291 !$#title Identification by sequence analysis of two-site !1posttranslational processing of the cysteine-rich outer !1membrane protein 2 of Chlamydia trachomatis serovar L2. !$#cross-references MUID:89123030; PMID:2914847 !$#accession A32244 !'##molecule_type DNA !'##residues 1-547 ##label ALL !'##cross-references GB:M23001; NID:g144552; PIDN:AAA23152.1; !1PID:g144553 !'##experimental_source strain L2/434/Bu !'##note parts of this sequence, including the amino ends of the !1precursor and mature proteins, were determined by protein !1sequencing REFERENCE A43584 !$#authors de la Maza, L.M.; Fielder, T.J.; Carlson, E.J.; Markoff, !1B.A.; Peterson, E.M. !$#journal Infect. Immun. (1991) 59:1196-1201 !$#title Sequence diversity of the 60-kilodalton protein and of a !1putative 15-kilodalton protein between the trachoma and !1lymphogranuloma venereum biovars of Chlamydia trachomatis. !$#cross-references MUID:91147205; PMID:1997423 !$#accession A43584 !'##molecule_type DNA !'##residues 1-547 ##label DEL !'##cross-references GB:M23001; NID:g144552; PIDN:AAA23152.1; !1PID:g144553 !'##experimental_source serovar 2, strain L2/434/Bu REFERENCE A36043 !$#authors Wahlberg, J.; Lundeberg, J.; Hultman, T.; Uhlen, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:6569-6573 !$#title General colorimetric method for DNA diagnostics allowing !1direct solid-phase genomic sequencing of the positive !1samples. !$#cross-references MUID:90370827; PMID:2118652 !$#accession A36043 !'##molecule_type DNA !'##residues 294-402 ##label WAH !'##experimental_source serotype L2 REFERENCE JQ0514 !$#authors Lambden, P.R.; Everson, J.S.; Ward, M.E.; Clarke, I.N. !$#journal Gene (1990) 87:105-112 !$#title Sulfur-rich proteins of Chlamydia trachomatis: !1developmentally regulated transcription of polycistronic !1mRNA from tandem promoters. !$#cross-references MUID:90236284; PMID:2332164 !$#accession A30472 !'##molecule_type DNA !'##residues 1-46;528-547 ##label LAM !'##cross-references GB:M35148; GB:M23180; GB:M35161; NID:g144485 !'##experimental_source serotype L1 REFERENCE JT0419 !$#authors Clarke, I.N.; Ward, M.E.; Lambden, P.R. !$#journal Gene (1988) 71:307-314 !$#title Molecular cloning and sequence analysis of a developmentally !1regulated cysteine-rich outer membrane protein from !1Chlamydia trachomatis. !$#cross-references MUID:89138006; PMID:3066701 !$#accession JT0419 !'##molecule_type DNA !'##residues 30-547 ##label CLA !'##cross-references GB:M35148; NID:g144485; PIDN:AAA23119.1; !1PID:g144487 !'##experimental_source serotype L1 GENETICS !$#gene omp2; omcB FUNCTION !$#description associated with differentiation of reticulate bodies into !1elementary bodies !$#note essential for the structural integrity of the outer envelope !1of the elementary bodies; may also be an important virulence !1factor CLASSIFICATION #superfamily 60K cysteine-rich outer membrane protein KEYWORDS membrane protein; virulence FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-40 #domain propeptide #status experimental #label PRO\ !$41-547 #product 60K cysteine-rich outer membrane protein 2 !8#status experimental #label MAT SUMMARY #length 547 #molecular-weight 58782 #checksum 3124 SEQUENCE /// ENTRY MMECA #type complete TITLE outer membrane protein A precursor - Escherichia coli (strain K-12) ALTERNATE_NAMES outer membrane protein II* ORGANISM #formal_name Escherichia coli DATE 30-Sep-1980 #sequence_revision 30-Sep-1980 #text_change 01-Mar-2002 ACCESSIONS A93707; A92862; A93855; S50909; D64836; A03434 REFERENCE A93707 !$#authors Beck, E.; Bremer, E. !$#journal Nucleic Acids Res. (1980) 8:3011-3024 !$#title Nucleotide sequence of the gene ompA coding the outer !1membrane protein II of Escherichia coli K-12. !$#cross-references MUID:81053729; PMID:6253901 !$#accession A93707 !'##molecule_type DNA !'##residues 1-346 ##label BEC !'##cross-references GB:V00307; GB:J01654; NID:g42159; PIDN:CAA23588.1; !1PID:g42161 !'##experimental_source strain K12 REFERENCE A92862 !$#authors Movva, N.R.; Nakamura, K.; Inouye, M. !$#journal J. Mol. Biol. (1980) 143:317-328 !$#title Gene structure of the OmpA protein, a major surface protein !1of Escherichia coli required for cell-cell interaction. !$#cross-references MUID:81170587; PMID:6260961 !$#accession A92862 !'##molecule_type DNA !'##residues 1-346 ##label MOV !'##cross-references GB:J01654; GB:V00307; GB:V00358; NID:g146979; !1PIDN:AAA24231.1; PID:g146981 !'##experimental_source K12, strain K802 REFERENCE A93855 !$#authors Chen, R.; Schmidmayr, W.; Kramer, C.; Chen-Schmeisser, U.; !1Henning, U. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1980) 77:4592-4596 !$#title Primary structure of major outer membrane protein II* (ompA !1protein) of Escherichia coli K-12. !$#cross-references MUID:81054820; PMID:7001461 !$#accession A93855 !'##molecule_type protein !'##residues 22-346 ##label CHE !'##experimental_source K12, strain P400 REFERENCE S50909 !$#authors Kuhn, A.; Kiefer, D.; Koehne, C.; Zhu, H.Y.; Tschantz, W.R.; !1Dalbey, R.E. !$#journal Eur. J. Biochem. (1994) 226:891-897 !$#title Evidence for a loop-like insertion mechanism of pro-Omp A !1into the inner membrane of Escherichia coli. !$#cross-references MUID:95112855; PMID:7813480 !$#accession S50909 !'##status preliminary !'##molecule_type protein !'##residues 1-46 ##label KUH REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64836 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-346 ##label BLAT !'##cross-references GB:AE000198; GB:U00096; NID:g1787189; !1PIDN:AAC74043.1; PID:g1787191; UWGP:b0957 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ompA; tolG; tut; con !$#map_position 22 min FUNCTION !$#description required for the action of colicins K and L and for the !1stabilization of mating aggregates in conjugation; serves as !1a receptor for a number of T-even-like phages; produces !1nonspecific diffusion channels that allow penetration of !1various solutes CLASSIFICATION #superfamily outer membrane protein A KEYWORDS membrane protein; monomer FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-346 #product outer membrane protein A #status predicted !8#label MAT\ !$22-196 #domain intramembrane #status predicted #label INT\ !$196-208 #region alanine/proline-rich\ !$209-346 #domain periplasmic #status predicted #label PER\ !$257-301 #domain ompA-like domain #status predicted #label OMP SUMMARY #length 346 #molecular-weight 37201 #checksum 8041 SEQUENCE /// ENTRY MMEBAD #type complete TITLE outer membrane protein A precursor - Shigella dysenteriae ORGANISM #formal_name Shigella dysenteriae DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 16-Jul-1999 ACCESSIONS A03435 REFERENCE A03435 !$#authors Braun, G.; Cole, S.T. !$#journal Nucleic Acids Res. (1982) 10:2367-2378 !$#title The nucleotide sequence coding for major outer membrane !1protein OmpA of Shigella dysenteriae. !$#cross-references MUID:82221414; PMID:6283478 !$#accession A03435 !'##molecule_type DNA !'##residues 1-351 ##label BRA !'##cross-references GB:V01344; NID:g46943; PIDN:CAA24638.1; PID:g46945 GENETICS !$#gene ompA CLASSIFICATION #superfamily outer membrane protein A KEYWORDS transmembrane protein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-351 #product outer membrane protein A #status predicted !8#label MAT\ !$22-201 #domain intramembrane #status predicted #label INT\ !$201-213 #region alanine/proline-rich\ !$214-351 #domain periplasmic #status predicted #label PER SUMMARY #length 351 #molecular-weight 37741 #checksum 559 SEQUENCE /// ENTRY MMEBAT #type complete TITLE outer membrane protein A precursor - Salmonella typhimurium ALTERNATE_NAMES outer membrane major heat-modifiable protein; outer membrane protein 33K ORGANISM #formal_name Salmonella typhimurium DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 16-Jul-1999 ACCESSIONS A03436 REFERENCE A03436 !$#authors Freudl, R.; Cole, S.T. !$#journal Eur. J. Biochem. (1983) 134:497-502 !$#title Cloning and molecular characterization of the ompA gene from !1Salmonella typhimurium. !$#cross-references MUID:83287368; PMID:6349993 !$#accession A03436 !'##molecule_type DNA !'##residues 1-350 ##label FRE !'##cross-references GB:X02006; NID:g47798; PIDN:CAA26037.1; PID:g758341 GENETICS !$#gene ompA !$#map_position 20 min FUNCTION !$#description required for the action of colicins and for the !1stabilization of mating aggregates in conjugation; produces !1nonspecific diffusion channels that allow penetration of !1various solutes !$#note cannot serve as the receptor for the ompA-specific phages K3 !1and TuII CLASSIFICATION #superfamily outer membrane protein A KEYWORDS transmembrane protein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-350 #product outer membrane protein A #status predicted !8#label MAT\ !$22-200 #domain intramembrane #status predicted #label INT\ !$200-212 #region alanine/proline-rich\ !$213-350 #domain periplasmic #status predicted #label PER SUMMARY #length 350 #molecular-weight 37589 #checksum 8452 SEQUENCE /// ENTRY LPECPG #type complete TITLE peptidoglycan-associated lipoprotein precursor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 01-Mar-2002 ACCESSIONS A27534; S20547; D64810 REFERENCE A27534 !$#authors Chen, R.; Henning, U. !$#journal Eur. J. Biochem. (1987) 163:73-77 !$#title Nucleotide sequence of the gene for the !1peptidoglycan-associated lipoprotein of Escherichia coli !1K12. !$#cross-references MUID:87133578; PMID:3545827 !$#accession A27534 !'##molecule_type DNA !'##residues 1-173 ##label CHE !'##cross-references GB:X05123; NID:g42256; PIDN:CAA28771.1; PID:g42257 REFERENCE S20546 !$#authors Lazzaroni, J.C.; Portalier, R. !$#journal Mol. Microbiol. (1992) 6:735-742 !$#title The excC gene of Escherichia coli K-12 required for cell !1envelope integrity encodes the peptidoglycan-associated !1lipoprotein (PAL). !$#cross-references MUID:92244043; PMID:1574003 !$#accession S20547 !'##molecule_type DNA !'##residues 1-173 ##label LAZ !'##cross-references EMBL:X65796; NID:g41358; PIDN:CAA46673.1; !1PID:g41360 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64810 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-173 ##label BLAT !'##cross-references GB:AE000177; GB:U00096; NID:g1786955; !1PIDN:AAC73835.1; PID:g1786962; UWGP:b0741 !'##experimental_source strain K-12, substrain MG1655 COMMENT This lipoprotein of unknown function is very strongly !1associated with the peptidoglycan; however, it is not !1covalently bound to the membrane. GENETICS !$#gene pal; excC !$#map_position 17 min CLASSIFICATION #superfamily outer membrane protein A KEYWORDS lipid binding; lipoprotein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-173 #product peptidoglycan-associated lipoprotein #status !8predicted #label MAT SUMMARY #length 173 #molecular-weight 18824 #checksum 4717 SEQUENCE /// ENTRY S69783 #type complete TITLE outer membrane protein 1A precursor - Dichelobacter nodosus ORGANISM #formal_name Dichelobacter nodosus DATE 19-May-2000 #sequence_revision 19-May-2000 #text_change 19-May-2000 ACCESSIONS S69783; PS0047 REFERENCE S69780 !$#authors Moses, E.K.; Good, R.T.; Sinistaj, M.; Billington, S.J.; !1Langford, C.J.; Rood, J.I. !$#journal Mol. Microbiol. (1995) 17:183-196 !$#title A multiple site-specific DNA-inversion model for the control !1of Omp1 phase and antigenic variation in Dichelobacter !1nodosus. !$#cross-references MUID:96020672; PMID:7476204 !$#accession S69783 !'##molecule_type DNA !'##residues 1-676 ##label MOS !'##cross-references EMBL:U02462 REFERENCE PS0047 !$#authors Moses, E.K.; Rood, J.I.; Yong, W.K.; Riffkin, G.G. !$#journal Gene (1989) 77:219-228 !$#title Molecular analysis of one of multiple protease-encoding !1genes from the prototype virulent strain of Bacteroides !1nodosus. !$#cross-references MUID:89326139; PMID:2666262 !$#accession PS0047 !'##molecule_type DNA !'##residues 1-286,'S',288-314,'IP',317-378,'R',380-448 ##label MO2 !'##cross-references GB:M26969; NID:g341559; PIDN:AAA72773.1; !1PID:g529018 !'##experimental_source VCS 1001 COMMENT Bacteroides nodosus VCS1001 is a prototype virulent strain !1that causes footrot in sheep. GENETICS !$#gene omp1A CLASSIFICATION #superfamily Dichelobacter nodosus outer membrane protein 1A KEYWORDS membrane protein FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-676 #product outer membrane protein 1A #status predicted !8#label MAT SUMMARY #length 676 #molecular-weight 72309 #checksum 4537 SEQUENCE /// ENTRY S69780 #type complete TITLE outer membrane protein 1B precursor - Dichelobacter nodosus ORGANISM #formal_name Dichelobacter nodosus DATE 19-May-2000 #sequence_revision 19-May-2000 #text_change 19-May-2000 ACCESSIONS S69780 REFERENCE S69780 !$#authors Moses, E.K.; Good, R.T.; Sinistaj, M.; Billington, S.J.; !1Langford, C.J.; Rood, J.I. !$#journal Mol. Microbiol. (1995) 17:183-196 !$#title A multiple site-specific DNA-inversion model for the control !1of Omp1 phase and antigenic variation in Dichelobacter !1nodosus. !$#cross-references MUID:96020672; PMID:7476204 !$#accession S69780 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-683 ##label MOS !'##cross-references EMBL:U02462 GENETICS !$#gene omp1B CLASSIFICATION #superfamily Dichelobacter nodosus outer membrane protein 1A KEYWORDS membrane protein FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-683 #product outer membrane protein 1B #status predicted !8#label MAT SUMMARY #length 683 #molecular-weight 74050 #checksum 3300 SEQUENCE /// ENTRY S69781 #type complete TITLE outer membrane protein 1E precursor - Dichelobacter nodosus ORGANISM #formal_name Dichelobacter nodosus DATE 19-May-2000 #sequence_revision 19-May-2000 #text_change 19-May-2000 ACCESSIONS S69781 REFERENCE S69780 !$#authors Moses, E.K.; Good, R.T.; Sinistaj, M.; Billington, S.J.; !1Langford, C.J.; Rood, J.I. !$#journal Mol. Microbiol. (1995) 17:183-196 !$#title A multiple site-specific DNA-inversion model for the control !1of Omp1 phase and antigenic variation in Dichelobacter !1nodosus. !$#cross-references MUID:96020672; PMID:7476204 !$#accession S69781 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-707 ##label MOS !'##cross-references EMBL:U02462 GENETICS !$#gene omp1E CLASSIFICATION #superfamily Dichelobacter nodosus outer membrane protein 1A KEYWORDS membrane protein FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-707 #product outer membrane protein 1E #status predicted !8#label MAT SUMMARY #length 707 #molecular-weight 76267 #checksum 1694 SEQUENCE /// ENTRY S69782 #type complete TITLE outer membrane protein 1D precursor - Dichelobacter nodosus ORGANISM #formal_name Dichelobacter nodosus DATE 19-May-2000 #sequence_revision 19-May-2000 #text_change 19-May-2000 ACCESSIONS S69782 REFERENCE S69780 !$#authors Moses, E.K.; Good, R.T.; Sinistaj, M.; Billington, S.J.; !1Langford, C.J.; Rood, J.I. !$#journal Mol. Microbiol. (1995) 17:183-196 !$#title A multiple site-specific DNA-inversion model for the control !1of Omp1 phase and antigenic variation in Dichelobacter !1nodosus. !$#cross-references MUID:96020672; PMID:7476204 !$#accession S69782 !'##status preliminary; nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-712 ##label MOS !'##cross-references EMBL:U02462; NID:g1488247; PIDN:AAB12362.1; !1PID:g407294 GENETICS !$#gene omp1D CLASSIFICATION #superfamily Dichelobacter nodosus outer membrane protein 1A KEYWORDS membrane protein FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-712 #product outer membrane protein 1D #status predicted !8#label MAT SUMMARY #length 712 #molecular-weight 76658 #checksum 2151 SEQUENCE /// ENTRY LPEC28 #type complete TITLE lipoprotein-28 precursor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 01-Mar-2002 ACCESSIONS A26286; F65167 REFERENCE A26286 !$#authors Yu, F.; Inouye, S.; Inouye, M. !$#journal J. Biol. Chem. (1986) 261:2284-2288 !$#title Lipoprotein-28, a cytoplasmic membrane lipoprotein from !1Escherichia coli: cloning, DNA sequence, and expression of !1its gene. !$#cross-references MUID:86111928; PMID:3003106 !$#accession A26286 !'##molecule_type DNA !'##residues 1-272 ##label YUF !'##cross-references GB:M12163; NID:g146648; PIDN:AAA24080.1; !1PID:g146649 !'##experimental_source strain K12 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65167 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-272 ##label BLAT !'##cross-references GB:AE000443; GB:U00096; NID:g2367255; !1PIDN:AAC76684.1; PID:g1790093; UWGP:b3661 !'##experimental_source strain K-12, substrain MG1655 COMMENT This is a minor lipoprotein localized in the cytoplasmic !1membrane in E. coli. GENETICS !$#gene nlpA CLASSIFICATION #superfamily lipoprotein-28 KEYWORDS blocked amino end; lipoprotein; membrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-272 #product lipoprotein-28 #status predicted #label MAT\ !$24 #binding_site sn-2,3-diacylglycerol (Cys) (covalent) !8#status predicted\ !$24 #modified_site fatty acylated amino end (Cys) (in !8mature form) #status predicted SUMMARY #length 272 #molecular-weight 29423 #checksum 4806 SEQUENCE /// ENTRY LPECW #type complete TITLE murein-lipoprotein lpp precursor - Escherichia coli (strain K-12) ALTERNATE_NAMES major outer membrane lipoprotein ORGANISM #formal_name Escherichia coli DATE 29-Jul-1981 #sequence_revision 29-Jul-1981 #text_change 01-Mar-2002 ACCESSIONS A90783; A92270; A93807; A91199; A91204; S29235; E64925; !1A03437 REFERENCE A90783 !$#authors Nakamura, K.; Inouye, M. !$#journal Cell (1979) 18:1109-1117 !$#title DNA sequence of the gene for the outer membrane lipoprotein !1of E. coli: an extremely AT-rich promoter. !$#cross-references MUID:80090054; PMID:391404 !$#accession A90783 !'##molecule_type DNA !'##residues 1-78 ##label NA1 !'##cross-references GB:V00302; GB:J01645; NID:g41929; PIDN:CAA23580.1; !1PID:g41930 REFERENCE A92270 !$#authors Nakamura, K.; Pirtle, R.M.; Pirtle, I.L.; Takeishi, K.; !1Inouye, M. !$#journal J. Biol. Chem. (1980) 255:210-216 !$#title Messenger ribonucleic acid of the lipoprotein of the !1Escherichia coli outer membrane. II. The complete nucleotide !1sequence. !$#cross-references MUID:80072081; PMID:6765942 !$#accession A92270 !'##molecule_type mRNA !'##residues 1-78 ##label NA2 !'##cross-references GB:J01645; NID:g146658; PID:g146659 REFERENCE A93807 !$#authors Inouye, S.; Wang, S.; Sekizawa, J.; Halegoua, S.; Inouye, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1977) 74:1004-1008 !$#title Amino acid sequence for the peptide extension on the !1prolipoprotein of the Escherichia coli outer membrane. !$#cross-references MUID:77148935; PMID:322142 !$#accession A93807 !'##molecule_type protein !'##residues 1-20 ##label INO REFERENCE A91199 !$#authors Braun, V.; Bosch, V. !$#journal Eur. J. Biochem. (1972) 28:51-69 !$#title Sequence of the murein-lipoprotein and the attachment site !1of the lipid. !$#cross-references MUID:72253465; PMID:4261992 !$#accession A91199 !'##molecule_type protein !'##residues 22-28,'E',30-42,'E',44-78 ##label BRA !'##note the epsilon-amino group of Lys-78 covalently binds to a !1diaminopimelic acid group of murein in the rigid layer of !1the cell wall REFERENCE A91204 !$#authors Hantke, K.; Braun, V. !$#journal Eur. J. Biochem. (1973) 34:284-296 !$#title Covalent binding of lipid to protein. !$#cross-references MUID:73196685; PMID:4575979 !$#accession A91204 !'##molecule_type protein !'##residues 21-24 ##label HAN REFERENCE A43726 !$#authors Yu, F.; Furukawa, H.; Nakamura, K.; Mizushima, S. !$#journal J. Biol. Chem. (1984) 259:6013-6018 !$#title Mechanism of localization of major outer membrane !1lipoprotein in Escherichia coli. !$#cross-references MUID:84185760; PMID:6325457 !$#contents annotation; trimeric association REFERENCE S29235 !$#authors Zhang, W.Y.; Dai, R.M.; Wu, H.C. !$#journal FEBS Lett. (1992) 311:311-314 !$#title Deletion of internal twenty-one amino acid residues of !1Escherichia coli prolipoprotein does not affect the !1formation of the murein-bound lipoprotein. !$#cross-references MUID:93012006; PMID:1397334 !$#accession S29235 !'##molecule_type protein !'##residues 1-78 ##label ZHA REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64925 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-78 ##label BLAT !'##cross-references GB:AE000263; GB:U00096; NID:g1787966; !1PIDN:AAC74747.1; PID:g1787967; UWGP:b1677 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene lpp !$#map_position 36 min CLASSIFICATION #superfamily murein-lipoprotein KEYWORDS blocked amino end; cell wall; homotrimer; lipoprotein; !1membrane protein; tandem repeat FEATURE !$1-20 #domain signal sequence #status experimental #label !8SIG\ !$21-78 #product murein-lipoprotein lpp #status experimental !8#label MAT\ !$24-34,38-48 #region 11-residue repeats (N-A-K-I/V-D-Q-L-S-S/ !8N-D-V)\ !$1 #modified_site N-formylmethionine (partial) #status !8experimental\ !$21 #binding_site sn-2,3-diacylglycerol (Cys) (covalent) !8#status experimental\ !$21 #modified_site fatty acylated amino end (Cys) (in !8mature form) #status experimental\ !$78 #binding_site murein (Lys) (covalent) (partial) !8#status experimental SUMMARY #length 78 #molecular-weight 8323 #checksum 4298 SEQUENCE /// ENTRY LPSEW #type complete TITLE murein-lipoprotein precursor - Serratia marcescens ORGANISM #formal_name Serratia marcescens DATE 31-Jul-1980 #sequence_revision 31-Jul-1980 #text_change 16-Jul-1999 ACCESSIONS A03438 REFERENCE A03438 !$#authors Nakamura, K.; Inouye, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1980) 77:1369-1373 !$#title DNA sequence of the Serratia marcescens lipoprotein gene. !$#cross-references MUID:80190055; PMID:6990409 !$#accession A03438 !'##molecule_type DNA !'##residues 1-77 ##label NAK !'##cross-references GB:J01789; NID:g152844; PIDN:AAA26566.1; !1PID:g152847; GB:V01348; NID:g47235; PID:g47237 CLASSIFICATION #superfamily murein-lipoprotein KEYWORDS blocked amino end; cell wall; lipoprotein; membrane protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-77 #product murein-lipoprotein #status predicted #label !8MAT\ !$20 #binding_site sn-2,3-diacylglycerol (Cys) (covalent) !8#status predicted\ !$20 #modified_site fatty acylated amino end (Cys) (in !8mature form) #status predicted\ !$77 #binding_site murein (Lys) (covalent) #status !8predicted SUMMARY #length 77 #molecular-weight 8239 #checksum 1642 SEQUENCE /// ENTRY NPWCWY #type complete TITLE murein-lipoprotein precursor - Erwinia amylovora ORGANISM #formal_name Erwinia amylovora DATE 29-Jun-1981 #sequence_revision 29-Jun-1981 #text_change 16-Jul-1999 ACCESSIONS A03439 REFERENCE A03439 !$#authors Yamagata, H.; Nakamura, K.; Inouye, M. !$#journal J. Biol. Chem. (1981) 256:2194-2198 !$#title Comparison of the lipoprotein gene among the !1Enterobacteriaceae. DNA sequence of Erwinia amylovora !1lipoprotein gene. !$#cross-references MUID:81117327; PMID:6257705 !$#accession A03439 !'##molecule_type DNA !'##residues 1-78 ##label YAM !'##cross-references GB:J01577; NID:g148423; PIDN:AAA24824.1; !1PID:g148424 CLASSIFICATION #superfamily murein-lipoprotein KEYWORDS blocked amino end; cell wall; lipoprotein; membrane protein FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-78 #product murein-lipoprotein #status predicted #label !8MAT\ !$21 #binding_site sn-2,3-diacylglycerol (Cys) (covalent) !8#status predicted\ !$21 #modified_site fatty acylated amino end (Cys) (in !8mature form) #status predicted\ !$78 #binding_site murein (Lys) (covalent) #status !8predicted SUMMARY #length 78 #molecular-weight 8369 #checksum 4477 SEQUENCE /// ENTRY LPEBWM #type complete TITLE murein-lipoprotein precursor - Morganella morganii ORGANISM #formal_name Morganella morganii DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 16-Jul-1999 ACCESSIONS A03440 REFERENCE A03440 !$#authors Huang, Y.X.; Ching, G.; Inouye, M. !$#journal J. Biol. Chem. (1983) 258:8139-8145 !$#title Comparison of the lipoprotein gene among the !1Enterobacteriaceae. DNA sequence of Morganella morganii !1lipoprotein gene and its expression in Escherichia coli. !$#cross-references MUID:83238418; PMID:6305973 !$#accession A03440 !'##molecule_type DNA !'##residues 1-78 ##label HUA !'##cross-references GB:K00084; NID:g149860; PIDN:AAA25322.1; !1PID:g149861 GENETICS !$#gene lpp CLASSIFICATION #superfamily murein-lipoprotein KEYWORDS blocked amino end; cell wall; lipoprotein; membrane protein FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-78 #product murein-lipoprotein #status predicted #label !8MAT\ !$21 #binding_site sn-2,3-diacylglycerol (Cys) (covalent) !8#status predicted\ !$21 #modified_site fatty acylated amino end (Cys) (in !8mature form) #status predicted\ !$78 #binding_site murein (Lys) (covalent) #status !8predicted SUMMARY #length 78 #molecular-weight 8430 #checksum 3295 SEQUENCE /// ENTRY D65088 #type complete TITLE murein-lipoprotein b3014 precursor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS D65088 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65088 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-85 ##label BLAT !'##cross-references GB:AE000383; GB:U00096; NID:g2367184; !1PIDN:AAC76050.1; PID:g1789390; UWGP:b3014 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily murein-lipoprotein KEYWORDS blocked amino end; cell wall; homotrimer; lipoprotein; !1membrane protein; tandem repeat FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-85 #product murein-lipoprotein #status predicted #label !8MAT\ !$20 #binding_site sn-2,3-diacylglycerol (Cys) (covalent) !8#status predicted\ !$20 #modified_site fatty acylated amino end (Cys) (in !8mature form) #status predicted SUMMARY #length 85 #molecular-weight 9513 #checksum 5617 SEQUENCE /// ENTRY JN0750 #type complete TITLE lipoprotein Rz1 precursor - phage lambda ORGANISM #formal_name phage lambda DATE 23-Oct-1998 #sequence_revision 23-Oct-1998 #text_change 16-Jul-1999 ACCESSIONS JN0750 REFERENCE JN0749 !$#authors Hanych, B.; Kedzierska, S.; Walderich, B.; Uznanski, B.; !1Taylor, A. !$#journal Gene (1993) 129:1-8 !$#title Expression of the Rz gene and the overlapping Rz1 reading !1frame present at the right end of the bacteriophage lambda !1genome. !$#cross-references MUID:93328108; PMID:8335247 !$#accession JN0750 !'##molecule_type DNA !'##residues 1-60 ##label HAN !'##cross-references GB:U37314; NID:g1017780; PIDN:AAC48862.1; !1PID:g1017781 REFERENCE A58886 !$#authors Kedzierska, S.; Wawrzynow, A.; Taylor, A. !$#journal Gene (1996) 168:1-8 !$#title The Rz1 gene product of bacteriophage lambda is a !1lipoprotein localized in the outer membrane of Escherichia !1coli. !$#cross-references MUID:96186947; PMID:8626053 !$#contents annotation REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#contents annotation COMMENT This protein is encoded by an alternative reading frame !1within the Rz gene (see PIR:APBPML) and is expressed at low !1levels. GENETICS !$#gene Rz1 CLASSIFICATION #superfamily phage lambda lipoprotein Rz1 precursor KEYWORDS blocked amino end; host cell lysis; lipoprotein; membrane !1protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-60 #product lipoprotein Rz1 #status predicted #label !8MAT\ !$20 #modified_site fatty acylated amino end (Cys) (in !8mature form) #status predicted\ !$20 #binding_site sn-2,3-diacylglycerol (Cys) (covalent) !8#status predicted SUMMARY #length 60 #molecular-weight 6588 #checksum 429 SEQUENCE /// ENTRY LPECRA #type complete TITLE rare lipoprotein A precursor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 01-Mar-2002 ACCESSIONS A28387; C32257; G64797 REFERENCE A91853 !$#authors Takase, I.; Ishino, F.; Wachi, M.; Kamata, H.; Doi, M.; !1Asoh, S.; Matsuzawa, H.; Ohta, T.; Matsuhashi, M. !$#journal J. Bacteriol. (1987) 169:5692-5699 !$#title Genes encoding two lipoproteins in the leuS-dacA region of !1the Escherichia coli chromosome. !$#cross-references MUID:88058785; PMID:3316191 !$#accession A28387 !'##molecule_type DNA !'##residues 1-362 ##label TAK !'##cross-references GB:M18276; NID:g147658; PIDN:AAA24552.1; !1PID:g147660 REFERENCE A32257 !$#authors Matsuzawa, H.; Asoh, S.; Kunai, K.; Muraiso, K.; Takasuga, !1A.; Ohta, T. !$#journal J. Bacteriol. (1989) 171:558-560 !$#title Nucleotide sequence of the rodA gene, responsible for the !1rod shape of Escherichia coli: rodA and the pbpA gene, !1encoding penicillin-binding protein 2, constitute the rodA !1operon. !$#cross-references MUID:89123070; PMID:2644207 !$#accession C32257 !'##status preliminary !'##molecule_type DNA !'##residues 1-16 ##label MATS !'##cross-references GB:M22857; NID:g147693; PIDN:AAA24572.1; !1PID:g147696 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64797 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-362 ##label BLAT !'##cross-references GB:AE000168; GB:U00096; NID:g1786849; !1PIDN:AAC73734.1; PID:g1786852; UWGP:b0633 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene rlpA !$#map_position 15 min FUNCTION !$#description one of the minor lipoproteins CLASSIFICATION #superfamily rplA lipoprotein KEYWORDS blocked amino end; lipid binding; lipoprotein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-362 #product rare lipoprotein A #status predicted #label !8MAT\ !$18 #binding_site sn-2,3-diacylglycerol (Cys) (covalent) !8#status predicted\ !$18 #modified_site fatty acylated amino end (Cys) (in !8mature form) #status predicted SUMMARY #length 362 #molecular-weight 37528 #checksum 6264 SEQUENCE /// ENTRY LPECRB #type complete TITLE lipoprotein rlpB precursor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1988 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS G64798; B28387 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64798 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-193 ##label BLAT !'##cross-references GB:AE000168; GB:U00096; NID:g1786849; !1PIDN:AAC73742.1; PID:g1786860; UWGP:b0641 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A91853 !$#authors Takase, I.; Ishino, F.; Wachi, M.; Kamata, H.; Doi, M.; !1Asoh, S.; Matsuzawa, H.; Ohta, T.; Matsuhashi, M. !$#journal J. Bacteriol. (1987) 169:5692-5699 !$#title Genes encoding two lipoproteins in the leuS-dacA region of !1the Escherichia coli chromosome. !$#cross-references MUID:88058785; PMID:3316191 !$#accession B28387 !'##molecule_type DNA !'##residues 1-116,'S',118-193 ##label TAK !'##cross-references GB:M18277; NID:g147662; PIDN:AAA24554.1; !1PID:g147663 COMMENT This is one of the minor lipoproteins encoded by genes !1located in the leuS-dacC intergenic region. GENETICS !$#gene rlpB !$#map_position 15 min CLASSIFICATION #superfamily rplB lipoprotein KEYWORDS blocked amino end; lipoprotein FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-193 #product lipoprotein rlpB #status predicted #label !8MAT\ !$19 #binding_site sn-2,3-diacylglycerol (Cys) (covalent) !8#status predicted\ !$19 #modified_site fatty acylated amino end (Cys) (in !8mature form) #status predicted SUMMARY #length 193 #molecular-weight 21356 #checksum 9071 SEQUENCE /// ENTRY LPECOB #type complete TITLE lipoprotein B precursor, osmotically inducible - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 01-Mar-2002 ACCESSIONS A32255; F64876 REFERENCE A32255 !$#authors Jung, J.U.; Gutierrez, C.; Villarejo, M.R. !$#journal J. Bacteriol. (1989) 171:511-520 !$#title Sequence of an osmotically inducible lipoprotein gene. !$#cross-references MUID:89123064; PMID:2644204 !$#accession A32255 !'##molecule_type DNA !'##residues 1-72 ##label JUN !'##cross-references GB:M22859; NID:g147039; PIDN:AAA24256.1; !1PID:g147040 !'##note induced by osmotic and growth phase signals REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64876 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-72 ##label BLAT !'##cross-references GB:AE000226; GB:U00096; NID:g2367115; !1PIDN:AAC74365.1; PID:g1787539; UWGP:b1283 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene osmB !$#map_position 28 min CLASSIFICATION #superfamily osmotically inducible lipoprotein omsB KEYWORDS blocked amino end; lipoprotein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-72 #product lipoprotein B, osmotically inducible #status !8predicted #label MAT\ !$24 #binding_site sn-2,3-diacylglycerol (Cys) (covalent) !8#status predicted\ !$24 #modified_site fatty acylated amino end (Cys) (in !8mature form) #status predicted SUMMARY #length 72 #molecular-weight 6948 #checksum 3294 SEQUENCE /// ENTRY B54546 #type complete TITLE small peptidoglycan-associated lipoprotein slp precursor - Bacillus subtilis ALTERNATE_NAMES PAL-related lipoprotein; peptidoglycan-associated lipoprotein homolog ORGANISM #formal_name Bacillus subtilis DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 16-Jun-2000 ACCESSIONS B54546; D69708 REFERENCE A54546 !$#authors Hemilae, H. !$#journal FEMS Microbiol. Lett. (1991) 66:37-41 !$#title Sequence of a PAL-related lipoprotein from Bacillus !1subtilis. !$#cross-references MUID:92038903; PMID:1936936 !$#accession B54546 !'##molecule_type DNA !'##residues 1-124 ##label HEM !'##experimental_source 168 strain BRB1 !'##note sequence extracted from NCBI backbone (NCBIN:63826, !1NCBIP:63828) REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D69708 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-124 ##label KUN !'##cross-references GB:Z99111; GB:AL009126; NID:g2633699; !1PIDN:CAB13335.1; PID:g2633833 !'##experimental_source strain 168 GENETICS !$#gene slp CLASSIFICATION #superfamily Bacillus subtilis small !1peptidoglycan-associated lipoprotein slp KEYWORDS blocked amino end; lipoprotein FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19 #binding_site sn-2,3-diacylglycerol (Cys) (covalent) !8#status predicted\ !$19 #modified_site fatty acylated amino end (Cys) (in !8mature form) #status predicted SUMMARY #length 124 #molecular-weight 14538 #checksum 5684 SEQUENCE /// ENTRY QRECM2 #type complete TITLE methyl-accepting chemotaxis protein II - Escherichia coli (strain K-12) ALTERNATE_NAMES MCP-II ORGANISM #formal_name Escherichia coli DATE 31-Mar-1989 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS E64951; A30295 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64951 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-533 ##label BLAT !'##cross-references GB:AE000282; GB:U00096; NID:g1788189; !1PIDN:AAC74955.1; PID:g1788194; UWGP:b1885 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A90835 !$#authors Krikos, A.; Mutoh, N.; Boyd, A.; Simon, M.I. !$#journal Cell (1983) 33:615-622 !$#title Sensory transducers of E. coli are composed of discrete !1structural and functional domains. !$#cross-references MUID:83232896; PMID:6305515 !$#accession A30295 !'##molecule_type DNA !'##residues 1-334,'G',336-502,'R',504-526,'TNCASGILK' ##label KRI !'##cross-references GB:J01705; EMBL:V01504; NID:g145516; !1PIDN:AAA23567.1; PID:g145522 COMMENT The specific function of this sensory transducing protein is !1not known, but the general function of bacterial sensory !1transducing proteins is to act as chemoreceptors, monitoring !1the environment either by binding specific ligands directly !1or by interacting with ligand-binding proteins in the !1periplasmic space. GENETICS !$#gene tap !$#map_position 42 min CLASSIFICATION #superfamily methyl-accepting chemotaxis protein KEYWORDS chemotaxis; methylated amino acid; sensory transduction; !1transmembrane protein FEATURE !$293,307,496 #modified_site glutamate methyl ester (Gln) (by !8cheB-dependent deamidation and methylation) #status !8predicted\ !$489 #modified_site glutamate methyl ester (Glu) #status !8predicted SUMMARY #length 533 #molecular-weight 57511 #checksum 4720 SEQUENCE /// ENTRY QRECM4 #type complete TITLE aspartate chemoreceptor protein - Escherichia coli (strain K-12) ALTERNATE_NAMES methyl-accepting chemotaxis protein IV (MCP-IV) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1989 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS F64951; A30287 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64951 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-553 ##label BLAT !'##cross-references GB:AE000282; GB:U00096; NID:g1788189; !1PIDN:AAC74956.1; PID:g1788195; UWGP:b1886 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A90835 !$#authors Krikos, A.; Mutoh, N.; Boyd, A.; Simon, M.I. !$#journal Cell (1983) 33:615-622 !$#title Sensory transducers of E. coli are composed of discrete !1structural and functional domains. !$#cross-references MUID:83232896; PMID:6305515 !$#accession A30287 !'##molecule_type DNA !'##residues 1-163,'R',165-553 ##label KRI !'##cross-references GB:J01705; EMBL:V01504; NID:g145516; !1PIDN:AAA23566.1; PID:g145521 COMMENT This protein is one of the bacterial sensory transducing !1proteins, which act as chemoreceptors, monitoring the !1environment either by binding specific ligands directly or !1by interacting with ligand-binding proteins in the !1periplasmic space. The specific function of this protein is !1to respond to changes in aspartate concentration in the !1environment, transduce a signal from the outside to the !1inside of the cell, and facilitate sensory adaptation !1through various levels of methylation. GENETICS !$#gene tar !$#map_position 42 min CLASSIFICATION #superfamily methyl-accepting chemotaxis protein KEYWORDS chemotaxis; methylated amino acid; sensory transduction; !1transmembrane protein FEATURE !$295,309 #modified_site glutamate methyl ester (Gln) (by !8cheB-dependent deamidation and methylation) #status !8predicted\ !$302,491,501 #modified_site glutamate methyl ester (Glu) #status !8predicted SUMMARY #length 553 #molecular-weight 59943 #checksum 2398 SEQUENCE /// ENTRY QREBDT #type complete TITLE aspartate chemoreceptor protein - Salmonella typhimurium ALTERNATE_NAMES methyl-accepting chemotaxis protein II (MCP-II) ORGANISM #formal_name Salmonella typhimurium DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 15-Aug-1997 ACCESSIONS A03441; A29053 REFERENCE A03441 !$#authors Russo, A.F.; Koshland Jr., D.E. !$#journal Science (1983) 220:1016-1020 !$#title Separation of signal transduction and adaptation functions !1of the aspartate receptor in bacterial sensing. !$#cross-references MUID:83197387; PMID:6302843 !$#accession A03441 !'##molecule_type DNA !'##residues 1-552 ##label RUS !'##note residues 294-296, 301-302, 308-309, 483-484, 490-491, and !1499-501 are potential methylation sites REFERENCE A29053 !$#authors Mowbray, S.L.; Foster, D.L.; Koshland Jr., D.E. !$#journal J. Biol. Chem. (1985) 260:11711-11718 !$#title Proteolytic fragments identified with domains of the !1aspartate chemoreceptor. !$#cross-references MUID:86008217; PMID:2995347 !$#accession A29053 !'##molecule_type protein !'##residues 1-245,'E',247-552 ##label MOW COMMENT This protein responds to changes in aspartate concentration !1in the environment, transduces a signal from the outside to !1the inside of the cell, and facilitates sensory adaptation !1through various levels of methylation. GENETICS !$#gene tar CLASSIFICATION #superfamily methyl-accepting chemotaxis protein KEYWORDS chemotaxis; methylated amino acid; sensory transduction; !1transmembrane protein FEATURE !$295,309 #modified_site glutamate methyl ester (Gln) (by !8cheB-dependent deamidation and methylation) #status !8predicted\ !$302,491,500 #modified_site glutamate methyl ester (Glu) #status !8predicted SUMMARY #length 552 #molecular-weight 59410 #checksum 8753 SEQUENCE /// ENTRY QRECS #type complete TITLE serine chemoreceptor protein - Escherichia coli (strain K-12) ALTERNATE_NAMES methyl-accepting chemotaxis protein I (MCP-I) ORGANISM #formal_name Escherichia coli DATE 14-Nov-1983 #sequence_revision 13-Feb-1998 #text_change 01-Mar-2002 ACCESSIONS E65250; S56581; A03442; S30281 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65250 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-551 ##label BLAT !'##cross-references GB:AE000506; GB:U00096; NID:g2367377; !1PIDN:AAC77311.1; PID:g2367378; UWGP:b4355 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56581 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-503,'X',505-551 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97252.1; !1PID:g537197 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A03442 !$#authors Boyd, A.; Kendall, K.; Simon, M.I. !$#journal Nature (1983) 301:623-626 !$#title Structure of the serine chemoreceptor in Escherichia coli. !$#cross-references MUID:83141753; PMID:6402709 !$#accession A03442 !'##molecule_type DNA !'##residues 1-147,'STSSLISRPRDIRN',162-536 ##label BOY !'##cross-references GB:V00373; GB:J01718; NID:g43217; PIDN:CAA23676.1; !1PID:g43218 REFERENCE S30279 !$#authors Roper, D.I.; Fawcett, T.; Cooper, R.A. !$#journal Mol. Gen. Genet. (1993) 237:241-250 !$#title The Escherichia coli C homoprotocatechuate degradative !1operon: hpc gene order, direction of transcription and !1control of expression. !$#cross-references MUID:93204900; PMID:8384293 !$#accession S30281 !'##molecule_type DNA !'##residues 1-77 ##label ROP !'##cross-references GB:S56952; NID:g298654; PIDN:AAB25802.1; !1PID:g298656 COMMENT This protein responds to changes in serine concentration in !1the environment, transduces a signal from the outside to the !1inside of the cell, and facilitates sensory adaptation !1through various levels of methylation. GENETICS !$#gene tsr !$#map_position 99 min CLASSIFICATION #superfamily methyl-accepting chemotaxis protein KEYWORDS chemotaxis; methylated amino acid; sensory transduction; !1transmembrane protein FEATURE !$297,311 #modified_site glutamate methyl ester (Gln) (by !8cheB-dependent deamidation and methylation) #status !8experimental\ !$304,493 #modified_site glutamate methyl ester (Glu) #status !8experimental\ !$503 #modified_site glutamate methyl ester (Glu) #status !8predicted SUMMARY #length 551 #molecular-weight 59442 #checksum 1281 SEQUENCE /// ENTRY QREC3M #type complete TITLE methyl-accepting chemotaxis protein III - Escherichia coli (strain K-12) ALTERNATE_NAMES MCP-III protein; ribose and galactose chemoreceptor protein ORGANISM #formal_name Escherichia coli DATE 31-Mar-1990 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS H64893; A30398; Q00228 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64893 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-546 ##label BLAT !'##cross-references GB:AE000239; GB:U00096; NID:g1787682; !1PIDN:AAC74503.1; PID:g1787690; UWGP:b1421 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A30398 !$#authors Bollinger, J.; Park, C.; Harayama, S.; Hazelbauer, G.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:3287-3291 !$#title Structure of the trg protein: homologies with and !1differences from other sensory transducers of Escherichia !1coli. !$#cross-references MUID:84221944; PMID:6374654 !$#accession A30398 !'##molecule_type DNA !'##residues 1-54,'R',56-190,'N',192-197,'AWV',202-396,398-444,'NG', !1447-534,'AER' ##label BOL REFERENCE A37452 !$#authors Kehry, M.A.; Engstroem, P.; Dahlquist, F.W.; Hazelbauer, !1G.L. !$#journal J. Biol. Chem. (1983) 258:5050-5055 !$#title Multiple covalent modifications of Trg, a sensory transducer !1of Escherichia coli. !$#cross-references MUID:83161122; PMID:6300110 !$#contents annotation !$#note the methylated tryptic peptides were isolated GENETICS !$#gene trg !$#map_position 31 min FUNCTION !$#description acts as receptor for the attractants ribose and galactose; !1mediates response to sugars recognized by the galactose- and !1ribose-binding proteins, presumably by interaction with the !1ligand-occupied proteins; transduces a signal from the !1outside to the inside of the cell and facilitates sensory !1adaptation through various levels of methylation !$#note one of four methyl-accepting chemotaxis proteins (MCPs) in !1E.coli CLASSIFICATION #superfamily methyl-accepting chemotaxis protein KEYWORDS chemotaxis; inner membrane; methylated amino acid; !1transmembrane protein FEATURE !$17-33 #domain transmembrane #status predicted #label TM1\ !$205-221 #domain transmembrane #status predicted #label TM2\ !$305,501,511 #modified_site glutamate methyl ester (Glu) #status !8experimental\ !$312,319 #modified_site glutamate methyl ester (Gln) (by !8cheB-dependent deamidation and methylation) #status !8experimental SUMMARY #length 546 #molecular-weight 58898 #checksum 3692 SEQUENCE /// ENTRY D71155 #type complete TITLE probable methyl-accepting chemotaxis protein - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS D71155 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession D71155 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-428 ##label KAW !'##cross-references GB:AP000002; NID:g3236129; PIDN:BAA29529.1; !1PID:g3256846 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0443 CLASSIFICATION #superfamily Pyrococcus horikoshii probable methyl-accepting !1chemotaxis protein; transcription initiation factor sigma !1region 1 homology FEATURE !$177-369 #domain transcription initiation factor sigma region !81 homology #label SR1 SUMMARY #length 428 #molecular-weight 46919 #checksum 7996 SEQUENCE /// ENTRY QRBSCN #type complete TITLE two-component sensor histidine kinase chemotactic signal modululator cheA - Bacillus subtilis ALTERNATE_NAMES chemotaxis protein cheN ORGANISM #formal_name Bacillus subtilis DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jun-2000 ACCESSIONS A41653; E69598 REFERENCE A41653 !$#authors Fuhrer, D.K.; Ordal, G.W. !$#journal J. Bacteriol. (1991) 173:7443-7448 !$#title Bacillus subtilis CheN, a homolog of CheA, the central !1regulator of chemotaxis in Escherichia coli. !$#cross-references MUID:92041654; PMID:1938941 !$#accession A41653 !'##molecule_type DNA !'##residues 1-671 ##label FUH !'##cross-references GB:M57894; GB:M51894; NID:g142683; PIDN:AAA22313.1; !1PID:g142685 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69598 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-671 ##label KUN !'##cross-references GB:Z99112; GB:AL009126; NID:g2633902; !1PIDN:CAB13516.1; PID:g2634015 !'##experimental_source strain 168 GENETICS !$#gene cheA; cheN CLASSIFICATION #superfamily chemotaxis protein cheA KEYWORDS autophosphorylation; chemotaxis; phosphohistidine; !1phosphoprotein; sensory transduction FEATURE !$46 #binding_site phosphate (His) (covalent) (by !8autophosphorylation) #status predicted SUMMARY #length 671 #molecular-weight 74767 #checksum 1143 SEQUENCE /// ENTRY QRECCS #type complete TITLE chemotaxis protein cheA [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES histidine autokinase CONTAINS chemotaxis protein cheA-L; chemotaxis protein cheA-S; protein-aspartate kinase (EC 2.7.2.-) ORGANISM #formal_name Escherichia coli DATE 30-Sep-1992 #sequence_revision 21-Nov-1997 #text_change 01-Mar-2002 ACCESSIONS H64951; A38541; B38541; A25195; A61351 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64951 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-654 ##label BLAT !'##cross-references GB:AE000282; GB:U00096; NID:g1788189; !1PIDN:AAC74958.1; PID:g1788197; UWGP:b1888 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A38541 !$#authors Kofoid, E.C.; Parkinson, J.S. !$#journal J. Bacteriol. (1991) 173:2116-2119 !$#title Tandem translation starts in the cheA locus of Escherichia !1coli. !$#cross-references MUID:91161531; PMID:2002011 !$#accession A38541 !'##molecule_type DNA !'##residues 1-165,'P',167-654 ##label KOF1 !'##cross-references GB:M34669; NID:g145527; PIDN:AAA23573.1; !1PID:g145529 !'##genetics CHAL !$#accession B38541 !'##molecule_type DNA !'##residues 98-165,'P',167-654 ##label KOF2 !'##cross-references GB:M34669; NID:g145527; PIDN:AAA23574.1; !1PID:g145530 !'##genetics CHAS !'##note the authors translated the codon GTC for residue 450 as Gly, !1GCG for residue 451 as Arg, ATG for residue 452 as Cys, CAG !1for residue 495 as Lys, GCG for residue 520 as Gly, and GAA !1for residue 646 as Gln !'##note parts of these sequences, including the amino ends of the !1mature proteins, were determined by protein sequencing; !1proteins beginning with 2-Ser, 3-Met and 98-Met were !1sequenced REFERENCE A91811 !$#authors Mutoh, N.; Simon, M.I. !$#journal J. Bacteriol. (1986) 165:161-166 !$#title Nucleotide sequence corresponding to five chemotaxis genes !1in Escherichia coli. !$#cross-references MUID:86085665; PMID:3510184 !$#accession A25195 !'##molecule_type DNA !'##residues 430-547,'ASGCWKCGVNICPSSNCG',566-605,'A',607-654 ##label !1MUT !'##cross-references GB:M13462; NID:g145515; PIDN:AAA23564.1; !1PID:g145519 REFERENCE A61351 !$#authors Hess, J.F.; Bourret, R.B.; Simon, M.I. !$#journal Nature (1988) 336:139-143 !$#title Histidine phosphorylation and phosphoryl group transfer in !1bacterial chemotaxis. !$#cross-references MUID:89040216; PMID:3185734 !$#accession A61351 !'##molecule_type protein !'##residues 45-51 ##label HES REFERENCE A65652 !$#authors Mcevoy, M.M.; Dahlquist, F.W. !$#submission submitted to the Brookhaven Protein Data Bank, February 1996 !$#cross-references PDB:1FWP !$#contents annotation; conformation by (1)H-NMR, residues 159-227 REFERENCE A58670 !$#authors McEvoy, M.M.; Muhandiram, D.R.; Kay, L.E.; Dahlquist, F.W. !$#journal Biochemistry (1996) 35:5633-5640 !$#title Structure and dynamics of a CheY-binding domain of the !1chemotaxis kinase CheA determined by nuclear magnetic !1resonance spectroscopy. !$#cross-references MUID:96216833; PMID:8639521 !$#contents annotation; conformation by (1)H-NMR, residues 159-227 GENETICS CHAL !$#gene cheA !$#map_position 42 min !$#start_codon GUG GENETICS CHAS !$#gene cheA !$#map_position 42 min !$#start_codon AUG FUNCTION !$#description catalyzes the hydrolysis of ATP to ADP and the !1phosphorylation of the 4-carboxyl group of an aspartic acid !1in chemotaxis proteins cheY and cheB CLASSIFICATION #superfamily chemotaxis protein cheA KEYWORDS alternative initiators; autophosphorylation; chemotaxis; !1phosphohistidine; phosphoprotein; phosphotransferase; !1sensory transduction FEATURE !$2-654 #product chemotaxis protein cheA-L #status predicted !8#label MATL\ !$2-134 #domain P1, phosphocarrier #status predicted #label !8PHC\ !$98-654 #product chemotaxis protein cheA-S #status predicted !8#label MATS\ !$160-233 #domain P2, cheY binding #status predicted #label !8CYB\ !$260-500 #domain T, catalytic #status predicted #label CAT\ !$510-580 #domain M, receptor coupling #status predicted #label !8MRC\ !$590-654 #domain C, cheW binding #status predicted #label CWB\ !$48 #binding_site phosphate (His) (covalent) (by !8autophosphorylation) #status experimental SUMMARY #length 654 #molecular-weight 71382 #checksum 92 SEQUENCE /// ENTRY S54304 #type complete TITLE taxis sensor histidine kinase (EC 2.7.3.-) cheA [validated] - Halobacterium salinarum ORGANISM #formal_name Halobacterium salinarum DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 03-Jun-2002 ACCESSIONS S54304 REFERENCE S54304 !$#authors Rudolph, J.; Oesterhelt, D. !$#journal EMBO J. (1995) 14:667-673 !$#title Chemotaxis and phototaxis require a CheA histidine kinase in !1the archaeon Halobacterium salinarium. !$#cross-references MUID:95188871; PMID:7882970 !$#accession S54304 !'##status preliminary !'##molecule_type DNA !'##residues 1-668 ##label RUD !'##cross-references EMBL:X82645; NID:g671099; PIDN:CAA57970.1; !1PID:g671100 !'##note the authors translated the codon CAC for residue 128 as Asp and !1GTC for residue 163 as Ala !'##note the source is designated as Halobacterium salinarium GENETICS !$#gene cheA COMPLEX homodimer FUNCTION TACT !$#description cheA is involved in integration and transmission of tactic !1signals to the flagellar motor [validated, PMID:8636990]; !1cheA recieves tactic signals from several transducer !1proteins; cheA transmits the integrated tactic signal by !1regulating the activity of response regulator cheY !1(PIR:S58645) !$#pathway tactic signalling pathway !$#note an Asp residue in cheY is phosphorylated FUNCTION ADAP !$#description cheA is involved in adaptation to tactic signals [validated, !1MUID:96219170]; cheA regulates the activity of cheB !1(PIR:S58646), which is involved in adaptation to tactic !1signals !$#note an Asp residue in the response regulator domain of cheB is !1phosphorylated FUNCTION AUTO !$#description EC 2.7.3.-; protein-histidine kinase [validated, !1PMID:9601619]; upon activation, cheA autophosphorylates on a !1His residue !$#note in the homodimer, the catalytic site of one chain !1phosphorylates the His residue of the other chain FUNCTION CHED !$#description EC 2.7.-.-; protein-aspartate kinase [validated, !1PMID:9601619]; cheA phosphorylates response regulator cheY !1and other proteins containing the response regulator !1homology domain on a conserved aspartate residue; upon !1activation, cheA autophosphorylates on a His residue !$#note the phosphate covalently attached to the His residue upon !1autophosphorylation is transferred to the Asp in the target !1protein CLASSIFICATION #superfamily chemotaxis protein cheA KEYWORDS phosphohistidine; phosphoprotein; phosphotransferase; !1two-component regulatory system FEATURE !$1-160 #domain phosphotransfer domain #status predicted !8#label TRA\ !$260-507 #domain autophosphorylation domain #status predicted !8#label AUT\ !$44 #binding_site phosphate (His) (covalent) #status !8experimental SUMMARY #length 668 #molecular-weight 71931 #checksum 1362 SEQUENCE /// ENTRY QRECCW #type complete TITLE purine binding chemotaxis protein cheW - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 01-Mar-2002 ACCESSIONS B25195; G64951 REFERENCE A91811 !$#authors Mutoh, N.; Simon, M.I. !$#journal J. Bacteriol. (1986) 165:161-166 !$#title Nucleotide sequence corresponding to five chemotaxis genes !1in Escherichia coli. !$#cross-references MUID:86085665; PMID:3510184 !$#accession B25195 !'##molecule_type DNA !'##residues 1-167 ##label MUT !'##cross-references GB:M13462; NID:g145515; PIDN:AAA23565.1; !1PID:g145520 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64951 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-167 ##label BLAT !'##cross-references GB:AE000282; GB:U00096; NID:g1788189; !1PIDN:AAC74957.1; PID:g1788196; UWGP:b1887 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene cheW !$#map_position 42 min CLASSIFICATION #superfamily chemotaxis cheW protein KEYWORDS chemotaxis SUMMARY #length 167 #molecular-weight 18084 #checksum 1077 SEQUENCE /// ENTRY QRECCY #type complete TITLE chemotaxis protein cheY [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 01-Mar-2002 ACCESSIONS E25195; A28872; B64951 REFERENCE A91811 !$#authors Mutoh, N.; Simon, M.I. !$#journal J. Bacteriol. (1986) 165:161-166 !$#title Nucleotide sequence corresponding to five chemotaxis genes !1in Escherichia coli. !$#cross-references MUID:86085665; PMID:3510184 !$#accession E25195 !'##molecule_type DNA !'##residues 1-129 ##label MUT !'##cross-references GB:M13463; NID:g145517 !'##note the codon given for 113-Pro (CCC) is inconsistent with the !1authors' translation REFERENCE A28872 !$#authors Matsumura, P.; Rydel, J.J.; Linzmeier, R.; Vacante, D. !$#journal J. Bacteriol. (1984) 160:36-41 !$#title Overexpression and sequence of the Escherichia coli cheY !1gene and biochemical activities of the cheY protein. !$#cross-references MUID:85006810; PMID:6090423 !$#accession A28872 !'##molecule_type DNA !'##residues 1-129 ##label MAS !'##cross-references GB:K02175; NID:g145532; PIDN:AAA23577.1; !1PID:g145534 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64951 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-129 ##label BLAT !'##cross-references GB:AE000282; GB:U00096; NID:g1788189; !1PIDN:AAC74952.1; PID:g1788191; UWGP:b1882 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A50903 !$#authors Volz, K.; Matsumura, P. !$#submission submitted to the Brookhaven Protein Data Bank, April 1991 !$#cross-references PDB:3CHY !$#contents annotation; X-ray crystallography, 1.66 angstroms, residues !12-129 REFERENCE A39428 !$#authors Volz, K.; Matsumura, P. !$#journal J. Biol. Chem. (1991) 266:15511-15519 !$#title Crystal structure of Escherichia coli CheY refined at !11.7-angstrom resolution. !$#cross-references MUID:91332083; PMID:1869568 !$#contents annotation; X-ray crystallography, 1.7 angstroms REFERENCE A52302 !$#authors Bellsolell, L.; Coll, M. !$#submission submitted to the Brookhaven Protein Data Bank, April 1994 !$#cross-references PDB:1CHN !$#contents annotation; X-ray crystallography, 1.76 angstroms, with !1magnesium, residues 4-129 REFERENCE A58669 !$#authors Bellsolell, L.; Prieto, J.; Serrano, L.; Coll, M. !$#journal J. Mol. Biol. (1994) 238:489-495 !$#title Magnesium binding to the bacterial chemotaxis protein CheY !1results in large conformational changes involving its !1functional surface. !$#cross-references MUID:94231569; PMID:8176739 !$#contents annotation; X-ray crystallography, 1.76 angstroms REFERENCE A65256 !$#authors Moy, F.J.; Lowry, D.F.; Matsumura, P.; Dahlquist, F.W.; !1Krywko, J.E.; Domaille, P.J. !$#submission submitted to the Brookhaven Protein Data Bank, November 1994 !$#cross-references PDB:1CEY !$#contents annotation; conformation by (1)H-NMR, residues 2-129 REFERENCE A55781 !$#authors Moy, F.J.; Lowry, D.F.; Matsumura, P.; Dahlquist, F.W.; !1Krywko, J.E.; Domaille, P.J. !$#journal Biochemistry (1994) 33:10731-10742 !$#title Assignments, secondary structure, global fold, and dynamics !1of chemotaxis Y protein using three- and four-dimensional !1heteronuclear ((13)C,(15)N) NMR spectroscopy. !$#cross-references MUID:94355297; PMID:8075074 !$#contents annotation; conformation by (1)H-, (13)C- and (15)N-NMR COMMENT This protein plays a central role in generating a regulating !1signal for flagellar rotation. GENETICS !$#gene cheY !$#map_position 42 min CLASSIFICATION #superfamily chemotaxis cheY protein; response regulator !1homology KEYWORDS chemotaxis; flagellar rotation; magnesium; metalloprotein; !1phosphoprotein FEATURE !$8-120 #domain response regulator homology #label RRH\ !$13,57,59 #binding_site magnesium (Asp, Asp, Asn) #status !8experimental\ !$57 #binding_site phosphate (Asp) (covalent) #status !8experimental SUMMARY #length 129 #molecular-weight 14097 #checksum 5470 SEQUENCE /// ENTRY QREBCY #type complete TITLE chemotaxis protein cheY [validated] - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 15-Sep-2000 ACCESSIONS A23567 REFERENCE A23567 !$#authors Stock, A.; Koshland Jr., D.E.; Stock, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:7989-7993 !$#title Homologies between the Salmonella typhimurium cheY protein !1and proteins involved in the regulation of chemotaxis, !1membrane protein synthesis, and sporulation. !$#cross-references MUID:86068029; PMID:2999789 !$#accession A23567 !'##molecule_type DNA !'##residues 1-129 ##label STO !'##cross-references GB:M12131; NID:g153907; PIDN:AAA27037.1; !1PID:g153909 REFERENCE A52252 !$#authors Stock, A.; Martinez-hackert, E.; Rasmussen, B.; West, A.; !1Stock, J.; Ringe, D.; Petsko, G. !$#submission submitted to the Brookhaven Protein Data Bank, January 1994 !$#cross-references PDB:2CHE !$#contents annotation; X-ray crystallography, 1.8 angstroms, with !1magnesium, residues 2-129 REFERENCE A52253 !$#authors Stock, A.; Martinez-hackert, E.; Rasmussen, B.; West, A.; !1Stock, J.; Ringe, D.; Petsko, G. !$#submission submitted to the Brookhaven Protein Data Bank, January 1994 !$#cross-references PDB:2CHF !$#contents annotation; X-ray crystallography, 1.8 angstroms, residues !12-129 REFERENCE A54173 !$#authors Stock, A.M.; Martinez-Hackert, E.; Rasmussen, B.F.; West, !1A.H.; Stock, J.B.; Ringe, D.; Petsko, G.A. !$#journal Biochemistry (1993) 32:13375-13380 !$#title Structure of the Mg(2+)-bound form of CheY and mechanism of !1phosphoryl transfer in bacterial chemotaxis. !$#cross-references MUID:94079867; PMID:8257674 !$#contents annotation; X-ray crystallography, 1.8 angstroms REFERENCE A58225 !$#authors Lukat, G.S.; Lee, B.H.; Mottonen, J.M.; Stock, A.M.; Stock, !1J.B. !$#journal J. Biol. Chem. (1991) 266:8348-8354 !$#title Roles of the highly conserved aspartate and lysine residues !1in the response regulator of bacterial chemotaxis. !$#cross-references MUID:91217072; PMID:1902474 !$#contents annotation; mutagenic replacement REFERENCE A58226 !$#authors Lukat, G.S.; Stock, A.M.; Stock, J.B. !$#journal Biochemistry (1990) 29:5436-5442 !$#title Divalent metal ion binding to the CheY protein and its !1significance to phosphotransfer in bacterial chemotaxis. !$#cross-references MUID:90352291; PMID:2201404 !$#contents annotation; metal binding GENETICS !$#gene cheY !$#map_position 40 CLASSIFICATION #superfamily chemotaxis cheY protein; response regulator !1homology KEYWORDS chemotaxis; flagellar rotation; magnesium; metalloprotein; !1phosphoprotein FEATURE !$8-120 #domain response regulator homology #label RRH\ !$13,57,59 #binding_site magnesium (Asp, Asp, Asn) #status !8experimental\ !$57 #binding_site phosphate (Asp) (covalent) #status !8experimental SUMMARY #length 129 #molecular-weight 14125 #checksum 4027 SEQUENCE /// ENTRY SZBS0F #type complete TITLE stage 0 sporulation protein spo0F - Bacillus subtilis ALTERNATE_NAMES sporulation initiation two-component response regulator spo0F ORGANISM #formal_name Bacillus subtilis DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 16-Jun-2000 ACCESSIONS A24737; B32354; A23526; S55425; D69710 REFERENCE A24737 !$#authors Trach, K.A.; Chapman, J.W.; Piggot, P.J.; Hoch, J.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:7260-7264 !$#title Deduced product of the stage 0 sporulation gene spo0F shares !1homology with the spo0A, ompR, and sfrA proteins. !$#cross-references MUID:86042645; PMID:2997779 !$#accession A24737 !'##molecule_type DNA !'##residues 1-124 ##label TRA !'##cross-references GB:M11081; NID:g143600; PIDN:AAA22787.1; !1PID:g143601 REFERENCE A91883 !$#authors Trach, K.; Chapman, J.W.; Piggot, P.; LeCoq, D.; Hoch, J.A. !$#journal J. Bacteriol. (1988) 170:4194-4208 !$#title Complete sequence and transcriptional analysis of the spo0F !1region of the Bacillus subtilis chromosome. !$#cross-references MUID:88314920; PMID:2457578 !$#accession B32354 !'##molecule_type DNA !'##residues 1-123 ##label TR2 REFERENCE A23526 !$#authors Yoshikawa, H.; Kazami, J.; Yamashita, S.; Chibazakura, T.; !1Sone, H.; Kawamura, F.; Oda, M.; Isaka, M.; Kobayashi, Y.; !1Saito, H. !$#journal Nucleic Acids Res. (1986) 14:1063-1072 !$#title Revised assignment for the Bacillus subtilis spo0F gene and !1its homology with spo0A and with two Escherichia coli genes. !$#cross-references MUID:86120355; PMID:3003689 !$#accession A23526 !'##molecule_type DNA !'##residues 1-124 ##label YOS !'##cross-references GB:X03497; NID:g40155; PIDN:CAA27217.1; PID:g40157 !'##note both Met-1 and Met-2 are used as initiators when expressed in !1E. coli REFERENCE S55414 !$#authors Glaser, P.; Danchin, A. !$#submission submitted to the EMBL Data Library, May 1995 !$#description Cloning and sequencing of the Bacillus subtilis chromosomal !1region from 320 degrees to 321 degrees. !$#accession S55425 !'##molecule_type DNA !'##residues 1-124 ##label GLA !'##cross-references EMBL:Z49782; NID:g853752; PIDN:CAA89872.1; !1PID:g853764 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D69710 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-124 ##label KUN !'##cross-references GB:Z99122; GB:Z99123; GB:AL009126; NID:g2636240; !1PIDN:CAB15741.1; PID:g2636250; NID:g2636029; PID:g2636238 !'##experimental_source strain 168 COMMENT This protein is involved in the initiation of sporulation. GENETICS !$#gene spo0F !$#map_position 323 (degrees) CLASSIFICATION #superfamily chemotaxis cheY protein; response regulator !1homology KEYWORDS phosphoprotein; sporulation FEATURE !$6-115 #domain response regulator homology #label RRH\ !$54 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 124 #molecular-weight 14228 #checksum 650 SEQUENCE /// ENTRY S58645 #type complete TITLE response regulator cheY [validated] - Halobacterium salinarum ORGANISM #formal_name Halobacterium salinarum DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 21-Jul-2000 ACCESSIONS S58645 REFERENCE S58645 !$#authors Rudolph, J.; Tolliday, N.; Schmitt, C.; Schuster, S.C.; !1Oesterhelt, D. !$#journal EMBO J. (1995) 14:4249-4257 !$#title Phosphorylation in halobacterial signal transduction. !$#cross-references MUID:96016197; PMID:7556066 !$#accession S58645 !'##status preliminary !'##molecule_type DNA !'##residues 1-120 ##label RUD !'##cross-references EMBL:X86407; NID:g994801; PIDN:CAA60161.1; !1PID:g994802 !'##note the source is designated as Halobacterium salinarium GENETICS !$#gene cheY FUNCTION !$#description cheY regulates the switch of the flagellar motor; thus it !1mediates the response to tactic stimuli [validated, !1MUID:96016197] !$#pathway tactic signalling pathway !$#note phosphorylated cheY triggers the flagellar motor to switch CLASSIFICATION #superfamily chemotaxis cheY protein; response regulator !1homology KEYWORDS phosphoprotein; two-component regulatory system FEATURE !$5-114 #domain response regulator homology #label RRH\ !$53 #binding_site phosphate (Asp) (covalent) #status !8experimental SUMMARY #length 120 #molecular-weight 13436 #checksum 8913 SEQUENCE /// ENTRY A55592 #type complete TITLE cheA activity-modulating chemotaxis protein cheV - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A55592; B69599; S41419 REFERENCE A55592 !$#authors Fredrick, K.L.; Helmann, J.D. !$#journal J. Bacteriol. (1994) 176:2727-2735 !$#title Dual chemotaxis signaling pathway in Bacillus subtilis: a !1sigma(D)-dependent gene encodes a novel protein with both !1CheW and CheY homologous domains. !$#cross-references MUID:94222854; PMID:8169223 !$#accession A55592 !'##status preliminary !'##molecule_type DNA !'##residues 1-303 ##label FRE !'##cross-references EMBL:Z29584; NID:g456243; PIDN:CAA82701.1; !1PID:g580837 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69599 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-303 ##label KUN !'##cross-references GB:Z99111; GB:AL009126; NID:g2633699; !1PIDN:CAB13274.1; PID:g2633772 !'##experimental_source strain 168 GENETICS !$#gene cheV !$#start_codon TTG CLASSIFICATION #superfamily chemotaxis cheV protein; response regulator !1homology KEYWORDS phosphoprotein FEATURE !$177-298 #domain response regulator homology #status atypical !8#label RRH\ !$235 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 303 #molecular-weight 34633 #checksum 2318 SEQUENCE /// ENTRY C64522 #type complete TITLE chemotaxis protein cheV homolog 1 - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C64522 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession C64522 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-321 ##label TOM !'##cross-references GB:AE000524; GB:AE000511; NID:g2313090; !1PIDN:AAD07087.1; PID:g2313092; TIGR:HP0019 CLASSIFICATION #superfamily chemotaxis cheV protein; response regulator !1homology KEYWORDS phosphoprotein FEATURE !$199-315 #domain response regulator homology #status atypical !8#label RRH\ !$252 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 321 #molecular-weight 36587 #checksum 2357 SEQUENCE /// ENTRY H64596 #type complete TITLE chemotaxis protein cheV homolog 2 - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS H64596 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession H64596 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-313 ##label TOM !'##cross-references GB:AE000576; GB:AE000511; NID:g2313736; !1PIDN:AAD07681.1; PID:g2313738; TIGR:HP0616 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily chemotaxis cheV protein; response regulator !1homology KEYWORDS phosphoprotein FEATURE !$194-309 #domain response regulator homology #status atypical !8#label RRH\ !$246 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 313 #molecular-weight 35661 #checksum 8133 SEQUENCE /// ENTRY BVECAU #type complete TITLE transcription regulator uhpA [similarity] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 01-Mar-2002 ACCESSIONS A26925; E41853; F65168; S30076 REFERENCE A30395 !$#authors Friedrich, M.J.; Kadner, R.J. !$#journal J. Bacteriol. (1987) 169:3556-3563 !$#title Nucleotide sequence of the uhp region of Escherichia coli. !$#cross-references MUID:87279903; PMID:3301805 !$#accession A26925 !'##molecule_type DNA !'##residues 1-196 ##label FRI !'##cross-references GB:M17102; NID:g148110; PIDN:AAA24720.1; !1PID:g148112 REFERENCE A41853 !$#authors Island, M.D.; Wei, B.Y.; Kadner, R.J. !$#journal J. Bacteriol. (1992) 174:2754-2762 !$#title Structure and function of the uhp genes for the sugar !1phosphate transport system in Escherichia coli and !1Salmonella typhimurium. !$#cross-references MUID:92234930; PMID:1569007 !$#accession E41853 !'##molecule_type DNA !'##residues 1-196 ##label ISL !'##cross-references EMBL:M89479; NID:g148116; PIDN:AAA24724.1; !1PID:g148117 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65168 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-196 ##label BLAT !'##cross-references GB:AE000444; GB:U00096; NID:g2367258; !1PIDN:AAC76692.1; PID:g1790102; UWGP:b3669 !'##experimental_source strain K-12, substrain MG1655 COMMENT This protein appears to be the positive activator for the !1transcription of the uhpT gene. GENETICS !$#gene uhpA !$#map_position 82 CLASSIFICATION #superfamily regulatory protein comA; response regulator !1homology KEYWORDS DNA binding; phosphoprotein; transcription regulation; !1two-component regulatory system FEATURE !$4-112 #domain response regulator homology #label RRH\ !$54 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 196 #molecular-weight 20889 #checksum 7071 SEQUENCE /// ENTRY QQEC24 #type complete TITLE probable transcription regulator uvrY - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 01-Mar-2002 ACCESSIONS A26750; G64954; I58267 REFERENCE A26750 !$#authors Moolenaar, G.F.; van Sluis, C.A.; Backendorf, C.; van de !1Putte, P. !$#journal Nucleic Acids Res. (1987) 15:4273-4289 !$#title Regulation of the Escherichia coli excision repair gene !1uvrC. Overlap between the uvrC structural gene and the !1region coding for a 24kD protein. !$#cross-references MUID:87231005; PMID:3295776 !$#accession A26750 !'##molecule_type DNA !'##residues 1-218 ##label MOO !'##cross-references EMBL:X05398; NID:g43291; PIDN:CAA28982.1; !1PID:g581252 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64954 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-218 ##label BLAT !'##cross-references GB:AE000284; GB:U00096; NID:g1788214; !1PIDN:AAC74981.1; PID:g1788222; UWGP:b1914 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene uvrY !$#map_position 42 min !$#start_codon TTG CLASSIFICATION #superfamily regulatory protein comA; response regulator !1homology KEYWORDS phosphoprotein; transcription regulation FEATURE !$4-115 #domain response regulator homology #label RRH\ !$54 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 218 #molecular-weight 23892 #checksum 2602 SEQUENCE /// ENTRY QQECY5 #type complete TITLE fimbriae Z protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1991 #sequence_revision 23-Jan-1998 #text_change 01-Mar-2002 ACCESSIONS F64785; JV0070 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64785 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-210 ##label BLAT !'##cross-references GB:AE000159; GB:U00096; NID:g1786739; !1PIDN:AAC73637.1; PID:g1786747; UWGP:b0535 !'##experimental_source strain K-12, substrain MG1655 REFERENCE JV0070 !$#authors Muramatsu, S.; Mizuno, T. !$#journal Mol. Gen. Genet. (1990) 220:325-328 !$#title Nucleotide sequence of the region encompassing the int gene !1of a cryptic prophage and the dna Y gene flanked by a curved !1DNA sequence of Escherichia coli K12. !$#cross-references MUID:90220507; PMID:2183007 !$#accession JV0070 !'##molecule_type DNA !'##residues 'MYQSTISRPNGKLSAPMRLVT',1-210 ##label MUR !'##cross-references GB:X51662; NID:g41809; PIDN:CAA35973.1; PID:g41810 !'##experimental_source strain K12 !'##note the authors translated the codon ACC for residue 41 as Ser GENETICS !$#gene fimZ !$#map_position 13 min CLASSIFICATION #superfamily regulatory protein comA; response regulator !1homology KEYWORDS phosphoprotein; two-component regulatory system FEATURE !$6-117 #domain response regulator homology #label RRH\ !$56 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 210 #molecular-weight 23663 #checksum 252 SEQUENCE /// ENTRY BVECCB #type complete TITLE colanic acid biosynthesis positive regulator rcsB - Escherichia coli (strain K-12) ALTERNATE_NAMES regulator of capsule synthesis B component ORGANISM #formal_name Escherichia coli DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 01-Mar-2002 ACCESSIONS JV0068; A44909; G64991 REFERENCE JV0068 !$#authors Stout, V.; Gottesman, S. !$#journal J. Bacteriol. (1990) 172:659-669 !$#title RcsB and RcsC: a two-component regulator of capsule !1synthesis in Escherichia coli. !$#cross-references MUID:90130299; PMID:2404948 !$#accession JV0068 !'##molecule_type DNA !'##residues 1-216 ##label STO !'##cross-references GB:M28242; NID:g147524; PIDN:AAA24504.1; !1PID:g457113 !'##experimental_source strain K12 REFERENCE A44909 !$#authors Gervais, F.G.; Phoenix, P.; Drapeau, G.R. !$#journal J. Bacteriol. (1992) 174:3964-3971 !$#title The rcsB gene, a positive regulator of colanic acid !1biosynthesis in Escherichia coli, is also an activator of !1ftsZ expression. !$#cross-references MUID:92283751; PMID:1597415 !$#accession A44909 !'##status preliminary !'##molecule_type DNA !'##residues 4-9 ##label GER !'##cross-references GB:S37760; NID:g250030; PIDN:AAB22290.1; !1PID:g250031 !'##note sequence extracted from NCBI backbone (NCBIN:106452, !1NCBIP:106454) REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64991 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-216 ##label BLAT !'##cross-references GB:AE000310; GB:U00096; NID:g2367131; !1PIDN:AAC75277.1; PID:g1788546; UWGP:b2217 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene rcsB !$#map_position 48 min FUNCTION !$#description acts as the receiver or effector of the two-component !1regulatory system to stimulate capsule synthesis from cps !1genes; rcsC protein, the other component, acts as the sensor !$#pathway capsule synthesis CLASSIFICATION #superfamily regulatory protein comA; response regulator !1homology KEYWORDS capsule synthesis; DNA binding; phosphoprotein; !1transcription regulation; two-component regulatory system FEATURE !$6-120 #domain response regulator homology #label RRH\ !$56 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 216 #molecular-weight 23670 #checksum 4342 SEQUENCE /// ENTRY RGECNL #type complete TITLE nitrate/nitrite response regulator protein narL - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli #variety strain K12 DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 01-Mar-2002 ACCESSIONS S09285; S04197; JS0118; B64869 REFERENCE S09285 !$#authors Gunsalus, R.P.; Kalman, L.V.; Stewart, R.R. !$#journal Nucleic Acids Res. (1989) 17:1965-1975 !$#title Nucleotide sequence of the narL gene that is involved in !1global regulation of nitrate controlled respiratory genes of !1Escherichia coli. !$#cross-references MUID:89183605; PMID:2648330 !$#accession S09285 !'##molecule_type DNA !'##residues 1-216 ##label GUN !'##cross-references GB:X69189; NID:g42103; PIDN:CAA48935.1; PID:g42106 !'##experimental_source strain K-12, substrain JM103 REFERENCE S04195 !$#authors Nohno, T.; Noji, S.; Taniguchi, S.; Saito, T. !$#journal Nucleic Acids Res. (1989) 17:2947-2957 !$#title The narX and narL genes encoding the nitrate-sensing !1regulators of Escherichia coli are homologous to a family of !1prokaryotic two-component regulatory genes. !$#cross-references MUID:89263708; PMID:2657652 !$#accession S04197 !'##molecule_type DNA !'##residues 1-216 ##label NOH !'##cross-references EMBL:X13360; NID:g42099; PIDN:CAA31742.1; !1PID:g42102 !'##experimental_source strain K-12 REFERENCE JS0117 !$#authors Stewart, V.; Parales Jr., J.; Merkel, S.M. !$#journal J. Bacteriol. (1989) 171:2229-2234 !$#title Structure of genes narL and narX of the nar (nitrate !1reductase) locus in Escherichia coli K-12. !$#cross-references MUID:89197802; PMID:2649492 !$#accession JS0118 !'##molecule_type DNA !'##residues 1-216 ##label STE !'##cross-references GB:X69189; NID:g42103; PIDN:CAA48935.1; PID:g42106 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64869 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-216 ##label BLAT !'##cross-references GB:AE000220; GB:U00096; NID:g1787467; !1PIDN:AAC74305.1; PID:g1787473; UWGP:b1221 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene narL; frdR !$#map_position 27 min FUNCTION !$#description activates expression of the nitrate reductase operon and !1represses transcription of the fumarate reductase operon in !1response to a nitrate induction signal transmitted by the !1narX or narQ proteins !$#note is part of the narX-narL regulatory system CLASSIFICATION #superfamily regulatory protein comA; response regulator !1homology KEYWORDS DNA binding; phosphoprotein; sensory transduction; !1transcription regulation FEATURE !$9-120 #domain response regulator homology #label RRH\ !$173-192 #region helix-turn-helix motif\ !$59 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 216 #molecular-weight 23927 #checksum 3511 SEQUENCE /// ENTRY RGBSXD #type complete TITLE extracellular proteinase response regulator degU - Bacillus subtilis ALTERNATE_NAMES extracellular proteinase regulatory protein iep ORGANISM #formal_name Bacillus subtilis DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jun-2000 ACCESSIONS C30191; B30190; A31097; C69614 REFERENCE A30191 !$#authors Henner, D.J.; Yang, M.; Ferrari, E. !$#journal J. Bacteriol. (1988) 170:5102-5109 !$#title Localization of Bacillus subtilis sacU(Hy) mutations to two !1linked genes with similarities to the conserved procaryotic !1family of two-component signalling systems. !$#cross-references MUID:89033891; PMID:3141378 !$#accession C30191 !'##molecule_type DNA !'##residues 1-229 ##label HEN !'##cross-references GB:M23558; NID:g143497; PIDN:AAA22733.1; !1PID:g143499 REFERENCE A30190 !$#authors Kunst, F.; Debarbouille, M.; Msadek, T.; Young, M.; Mauel, !1C.; Karamata, D.; Klier, A.; Rapoport, G.; Dedonder, R. !$#journal J. Bacteriol. (1988) 170:5093-5101 !$#title Deduced polypeptides encoded by the Bacillus subtilis sacU !1locus share homology with two-component sensor-regulator !1systems. !$#cross-references MUID:89033890; PMID:3141377 !$#accession B30190 !'##molecule_type DNA !'##residues 1-229 ##label KUN !'##cross-references GB:M23649; NID:g143500; PIDN:AAA22735.1; !1PID:g143502 REFERENCE A31097 !$#authors Tanaka, T.; Kawata, M. !$#journal J. Bacteriol. (1988) 170:3593-3600 !$#title Cloning and characterization of Bacillus subtilis iep, which !1has positive and negative effects on production of !1extracellular proteases. !$#cross-references MUID:88298669; PMID:3136143 !$#accession A31097 !'##molecule_type DNA !'##residues 1-229 ##label TAN !'##cross-references GB:M21658; NID:g143087; PIDN:AAA22545.1; !1PID:g143089 !'##experimental_source strain 168 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69614 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-229 ##label KU2 !'##cross-references GB:Z99122; GB:AL009126; NID:g2636029; !1PIDN:CAB15566.1; PID:g2636075 !'##experimental_source strain 168 COMMENT This protein has two functional regions: the amino-terminal !1region, which contains inhibitory activity for the !1production of exoprotease and levansucrase, and the !1carboxyl-terminal region, which carries the enhancing !1activity for these enzymes. GENETICS !$#gene degU; iep !$#start_codon GTG CLASSIFICATION #superfamily regulatory protein comA; response regulator !1homology KEYWORDS DNA binding; phosphoprotein; transcription regulation; !1two-component regulatory system FEATURE !$6-117 #domain response regulator homology #label RRH\ !$56 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 229 #molecular-weight 25866 #checksum 3573 SEQUENCE /// ENTRY RGBSCA #type complete TITLE regulatory protein comA - Bacillus subtilis ALTERNATE_NAMES late competence genes response regulator comA ORGANISM #formal_name Bacillus subtilis DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jun-2000 ACCESSIONS A33591; A69602 REFERENCE A33591 !$#authors Weinrauch, Y.; Guillen, N.; Dubnau, D.A. !$#journal J. Bacteriol. (1989) 171:5362-5375 !$#title Sequence and transcription mapping of Bacillus subtilis !1competence genes comB and comA, one of which is related to a !1family of bacterial regulatory determinants. !$#cross-references MUID:90008771; PMID:2507523 !$#accession A33591 !'##molecule_type DNA !'##residues 1-214 ##label WEI !'##cross-references GB:M22856; GB:M29689; GB:M29851; NID:g142697; !1PIDN:AAA22320.1; PID:g142701 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69602 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-214 ##label KUN !'##cross-references GB:Z99120; GB:AL009126; NID:g2635613; !1PIDN:CAB15156.1; PID:g2635663 !'##experimental_source strain 168 COMMENT This protein may be a transcriptional effector that responds !1to signals that are essential for the initiation of !1competence development in B. subtilis. GENETICS !$#gene comA CLASSIFICATION #superfamily regulatory protein comA; response regulator !1homology KEYWORDS DNA binding; phosphoprotein; transcription regulation; !1two-component regulatory system FEATURE !$4-117 #domain response regulator homology #label RRH\ !$55 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 214 #molecular-weight 24128 #checksum 8592 SEQUENCE /// ENTRY VZBRGP #type complete TITLE transcription regulator bvgA - Bordetella pertussis ALTERNATE_NAMES virulence protein bvgA ORGANISM #formal_name Bordetella pertussis DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS B33729; A36050 REFERENCE A33729 !$#authors Arico, B.; Miller, J.F.; Roy, C.; Stibitz, S.; Monack, D.; !1Falkow, S.; Gross, R.; Rappuoli, R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:6671-6675 !$#title Sequences required for expression of Bordetella pertussis !1virulence factors share homology with prokaryotic signal !1transduction proteins. !$#cross-references MUID:89367311; PMID:2549542 !$#accession B33729 !'##molecule_type DNA !'##residues 1-209 ##label ARI !'##cross-references GB:M25401; NID:g144038; PIDN:AAA22969.1; !1PID:g144039 REFERENCE A36050 !$#authors Scarlato, V.; Prugnola, A.; Arico, B.; Rappuoli, R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:6753-6757 !$#title Positive transcriptional feedback at the bvg locus controls !1expression of virulence factors in Bordetella pertussis. !$#cross-references MUID:90370862; PMID:1697687 !$#accession A36050 !'##status preliminary !'##molecule_type DNA !'##residues 1-7 ##label SCA GENETICS !$#gene bvgA FUNCTION !$#description regulates the expression of Bordetella virulence factors CLASSIFICATION #superfamily regulatory protein comA; response regulator !1homology KEYWORDS DNA binding; phosphoprotein; transcription regulation; !1two-component regulatory system; virulence regulation FEATURE !$5-115 #domain response regulator homology #label RRH\ !$54 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 209 #molecular-weight 22952 #checksum 280 SEQUENCE /// ENTRY S17943 #type complete TITLE transcription regulator bvgA - Bordetella bronchiseptica ALTERNATE_NAMES virulence protein bvgA ORGANISM #formal_name Bordetella bronchiseptica DATE 20-Feb-1995 #sequence_revision 20-Feb-1995 #text_change 16-Jul-1999 ACCESSIONS S17943 REFERENCE S17943 !$#authors Arico, B.; Scarlato, V.; Monack, D.M.; Falkow, S.; Rappuoli, !1R. !$#journal Mol. Microbiol. (1991) 5:2481-2491 !$#title Structural and genetic analysis of the bvg locus in !1Bordetella species. !$#cross-references MUID:92167813; PMID:1791760 !$#accession S17943 !'##molecule_type DNA !'##residues 1-209 ##label ARI !'##cross-references EMBL:X58355; NID:g39352; PIDN:CAA41251.1; !1PID:g39353 !'##experimental_source strain 7865 GENETICS !$#gene bvgA FUNCTION !$#description regulates the expression of Bordetella virulence factors CLASSIFICATION #superfamily regulatory protein comA; response regulator !1homology KEYWORDS DNA binding; phosphoprotein; transcription regulation; !1two-component regulatory system; virulence regulation FEATURE !$5-115 #domain response regulator homology #label RRH\ !$54 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 209 #molecular-weight 22952 #checksum 280 SEQUENCE /// ENTRY S17945 #type complete TITLE transcription regulator bvgA - Bordetella parapertussis ALTERNATE_NAMES virulence protein bvgA ORGANISM #formal_name Bordetella parapertussis DATE 12-Feb-1998 #sequence_revision 20-Feb-1998 #text_change 16-Jul-1999 ACCESSIONS S17945; S18223 REFERENCE S17943 !$#authors Arico, B.; Scarlato, V.; Monack, D.M.; Falkow, S.; Rappuoli, !1R. !$#journal Mol. Microbiol. (1991) 5:2481-2491 !$#title Structural and genetic analysis of the bvg locus in !1Bordetella species. !$#cross-references MUID:92167813; PMID:1791760 !$#accession S17945 !'##molecule_type DNA !'##residues 1-209 ##label ARI !'##cross-references EMBL:X52948; NID:g39727; PIDN:CAA37123.1; !1PID:g39728 !'##experimental_source strain 9305 REFERENCE S18223 !$#authors Scarlato, V.; Prugnola, A.; Arico, B.; Rappuoli, R. !$#journal Mol. Microbiol. (1991) 5:2493-2498 !$#title The bvg-dependent promoters show similar behaviour in !1different Bordetella species and share sequence homologies. !$#cross-references MUID:92167814; PMID:1791761 !$#accession S18223 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-20 ##label SCA GENETICS !$#gene bvgA FUNCTION !$#description regulates the expression of Bordetella virulence factors CLASSIFICATION #superfamily regulatory protein comA; response regulator !1homology KEYWORDS DNA binding; phosphoprotein; transcription regulation; !1two-component regulatory system; virulence regulation FEATURE !$5-115 #domain response regulator homology #label RRH\ !$54 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 209 #molecular-weight 22952 #checksum 280 SEQUENCE /// ENTRY JC6019 #type complete TITLE response regulator frzZ [validated] - Myxococcus xanthus ORGANISM #formal_name Myxococcus xanthus DATE 15-Aug-1996 #sequence_revision 18-Oct-1996 #text_change 22-Oct-2001 ACCESSIONS JC6019 REFERENCE JC6019 !$#authors Trudeau, K.G.; Ward, M.J.; Zusman, D.R. !$#journal Mol. Microbiol. (1996) 20:645-655 !$#title Identification and characterization of FrzZ, a novel !1response regulator necessary for swarming and fruiting-body !1formation in Myxococcus xanthus. !$#cross-references MUID:96347136; PMID:8736543 !$#accession JC6019 !'##molecule_type DNA !'##residues 1-290 ##label TRU !'##cross-references GB:U47814; NID:g1236916; PIDN:AAC44537.1; !1PID:g1236917 COMMENT This protein is involved in a chemotactic !1signal-transduction pathway similar to that in enteric !1bacteria. It regulates individual cell movements and is !1necessary for swarming and fruiting-body formation. GENETICS !$#gene frzZ CLASSIFICATION #superfamily Myxococcus xanthus response regulator frzZ; !1response regulator homology KEYWORDS phosphoprotein; signal transduction FEATURE !$4-114 #domain response regulator homology #label RRH1\ !$124-162 #region alanine/proline-rich\ !$170-283 #domain response regulator homology #label RRH2\ !$52 #binding_site phosphate (Asp) (covalent) #status !8predicted\ !$220 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 290 #molecular-weight 30485 #checksum 2747 SEQUENCE /// ENTRY B64850 #type complete TITLE probable virulence factor mviN - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS B64850 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64850 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-511 ##label BLAT !'##cross-references GB:AE000208; GB:U00096; NID:g1787308; !1PIDN:AAC74153.1; PID:g1787309; UWGP:b1069 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene mviN CLASSIFICATION #superfamily mviN protein KEYWORDS transmembrane protein; virulence FEATURE !$90-106 #domain transmembrane #status predicted #label TM1\ !$135-151 #domain transmembrane #status predicted #label TM2\ !$161-177 #domain transmembrane #status predicted #label TM3\ !$186-202 #domain transmembrane #status predicted #label TM4\ !$237-253 #domain transmembrane #status predicted #label TM5\ !$276-292 #domain transmembrane #status predicted #label TM6\ !$313-329 #domain transmembrane #status predicted #label TM7\ !$354-370 #domain transmembrane #status predicted #label TM8\ !$386-402 #domain transmembrane #status predicted #label TM9\ !$409-425 #domain transmembrane #status predicted #label TM10\ !$444-460 #domain transmembrane #status predicted #label TM11\ !$483-499 #domain transmembrane #status predicted #label TM12 SUMMARY #length 511 #molecular-weight 55267 #checksum 7668 SEQUENCE /// ENTRY S40271 #type complete TITLE virulence factor mviN - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S40271 REFERENCE S40270 !$#authors van Slooten, J.C.; Okada, T.T.; Pechere, J.C.; Kutsukake, !1K.K. !$#submission submitted to the EMBL Data Library, September 1993 !$#description Locus mviS encodes two virulence factors of Salmonella !1typhimurium. !$#accession S40271 !'##molecule_type DNA !'##residues 1-524 ##label VAN !'##cross-references EMBL:Z26133; NID:g438250; PIDN:CAA81134.1; !1PID:g438252 !'##experimental_source strain LT2 / KK1004 GENETICS !$#gene mviN CLASSIFICATION #superfamily mviN protein KEYWORDS transmembrane protein; virulence FEATURE !$95-111 #domain transmembrane #status predicted #label TM1\ !$148-164 #domain transmembrane #status predicted #label TM2\ !$174-190 #domain transmembrane #status predicted #label TM3\ !$199-215 #domain transmembrane #status predicted #label TM4\ !$250-266 #domain transmembrane #status predicted #label TM5\ !$289-305 #domain transmembrane #status predicted #label TM6\ !$326-342 #domain transmembrane #status predicted #label TM7\ !$367-383 #domain transmembrane #status predicted #label TM8\ !$399-415 #domain transmembrane #status predicted #label TM9\ !$422-438 #domain transmembrane #status predicted #label TM10\ !$462-478 #domain transmembrane #status predicted #label TM11\ !$496-512 #domain transmembrane #status predicted #label TM12 SUMMARY #length 524 #molecular-weight 57314 #checksum 9796 SEQUENCE /// ENTRY I64162 #type complete TITLE mviN protein homolog HI0964 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS I64162 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession I64162 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-510 ##label TIGR !'##cross-references GB:U32777; GB:L42023; NID:g1573983; !1PIDN:AAC22623.1; PID:g1573989; TIGR:HI0964 CLASSIFICATION #superfamily mviN protein SUMMARY #length 510 #molecular-weight 56164 #checksum 7011 SEQUENCE /// ENTRY E64630 #type complete TITLE virulence factor mviN protein - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS E64630 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession E64630 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-461 ##label TOM !'##cross-references GB:AE000598; GB:AE000511; NID:g2314019; !1PIDN:AAD07933.1; PID:g2314021; TIGR:HP0885 CLASSIFICATION #superfamily mviN protein SUMMARY #length 461 #molecular-weight 51618 #checksum 7651 SEQUENCE /// ENTRY A70201 #type complete TITLE virulence factor mviN protein homolog precursor - Lyme disease spirochete ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Dec-1999 ACCESSIONS A70201 REFERENCE A70100 !$#authors Fraser, C.M.; Casjens, S.; Huang, W.M.; Sutton, G.G.; !1Clayton, R.; Lathigra, R.; White, O.; Ketchum, K.A.; Dodson, !1R.; Hickey, E.K.; Gwinn, M.; Dougherty, B.; Tomb, J.F.; !1Fleischmann, R.D.; Richardson, D.; Peterson, J.; Kerlavage, !1A.R.; Quackenbush, J.; Salzberg, S.; Hanson, M.; Vugt, R.V.; !1Palmer, N.; Adams, M.D.; Gocayne, J.; Weidman, J.; !1Utterback, T.; Watthey, L.; McDonald, L.; Artiach, P.; !1Bowman, C.; Garland, S.; Fujii, C.; Cotton, M.D.; Horst, K.; !1Roberts, K.; Hatch, B.; Smith, H.O.; Venter, J.C. !$#journal Nature (1997) 390:580-586 !$#title Genomic sequence of a Lyme disease spirochaete, Borrelia !1burgdorferi. !$#cross-references MUID:98065943; PMID:9403685 !$#accession A70201 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-512 ##label KLE !'##cross-references GB:AE001179; GB:AE000783; NID:g2688738; !1PIDN:AAC67146.1; PID:g2688740; TIGR:BB0810 !'##experimental_source strain B31 CLASSIFICATION #superfamily mviN protein FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-512 #product virulence factor mviN protein homolog !8#status predicted #label MAT SUMMARY #length 512 #molecular-weight 58902 #checksum 969 SEQUENCE /// ENTRY S74401 #type complete TITLE hypothetical protein slr0488 - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S74401 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74401 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-533 ##label KAN !'##cross-references EMBL:D64001; GB:AB001339; NID:g1001102; !1PIDN:BAA10319.1; PID:g1001176 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily mviN protein SUMMARY #length 533 #molecular-weight 57052 #checksum 2224 SEQUENCE /// ENTRY B49205 #type complete TITLE virulence-associated protein vapC - Dichelobacter nodosus ORGANISM #formal_name Dichelobacter nodosus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 24-Sep-1999 ACCESSIONS B49205 REFERENCE A49205 !$#authors Katz, M.E.; Strugnell, R.A.; Rood, J.I. !$#journal Infect. Immun. (1992) 60:4586-4592 !$#title Molecular characterization of a genomic region associated !1with virulence in Dichelobacter nodosus. !$#cross-references MUID:93014173; PMID:1398971 !$#accession B49205 !'##status preliminary !'##molecule_type DNA !'##residues 1-135 ##label KAT !'##cross-references GB:L22308; NID:g438532; PIDN:AAA20205.1; !1PID:g438534 !'##note sequence extracted from NCBI backbone (NCBIN:116426, !1NCBIP:116429) CLASSIFICATION #superfamily virulence-associated protein vapC SUMMARY #length 135 #molecular-weight 15128 #checksum 5461 SEQUENCE /// ENTRY S74412 #type complete TITLE virulence-associated protein C-1 - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein sll0690 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S74412 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74412 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-133 ##label KAN !'##cross-references EMBL:D64001; GB:AB001339; NID:g1001102; !1PIDN:BAA10330.1; PID:g1001187 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene vapC-1 !$#start_codon GTG CLASSIFICATION #superfamily virulence-associated protein vapC SUMMARY #length 133 #molecular-weight 14763 #checksum 2636 SEQUENCE /// ENTRY S74972 #type complete TITLE virulence-associated protein C-2 - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein ssl2923 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S74972 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74972 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-83 ##label KAN !'##cross-references EMBL:D90902; GB:AB001339; NID:g1652027; !1PIDN:BAA17012.1; PID:g1652087 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene vapC-2 CLASSIFICATION #superfamily virulence-associated protein vapC SUMMARY #length 83 #molecular-weight 9540 #checksum 4897 SEQUENCE /// ENTRY B64104 #type complete TITLE virulence-associated protein vapC homolog HI0947 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B64104 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession B64104 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-132 ##label TIGR !'##cross-references GB:U32776; GB:L42023; NID:g1573969; !1PIDN:AAC22608.1; PID:g1573972; TIGR:HI0947 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily virulence-associated protein vapC SUMMARY #length 132 #molecular-weight 15147 #checksum 3048 SEQUENCE /// ENTRY G64061 #type complete TITLE virulence-associated protein vapC homolog HI0322 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS G64061 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession G64061 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-134 ##label TIGR !'##cross-references GB:U32717; GB:L42023; NID:g1573283; !1PIDN:AAC21985.1; PID:g1573291; TIGR:HI0322 CLASSIFICATION #superfamily virulence-associated protein vapC SUMMARY #length 134 #molecular-weight 15726 #checksum 8218 SEQUENCE /// ENTRY F64061 #type complete TITLE virulence-associated protein vapB homolog HI0321 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS F64061 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession F64061 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-78 ##label TIGR !'##cross-references GB:U32717; GB:L42023; NID:g1573283; !1PIDN:AAC21984.1; PID:g1573290; TIGR:HI0321 CLASSIFICATION #superfamily virulence-associated protein vagC homolog SUMMARY #length 78 #molecular-weight 9037 #checksum 1195 SEQUENCE /// ENTRY S22685 #type complete TITLE virulence-associated protein vagC - Salmonella dublin plasmid ORGANISM #formal_name Salmonella dublin DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S22685 REFERENCE S22685 !$#authors Pullinger, G.D.; Lax, A.J. !$#journal Mol. Microbiol. (1992) 6:1631-1643 !$#title A Salmonella dublin virulence plasmid locus that affects !1bacterial growth under nutrient-limited conditions. !$#cross-references MUID:92356827; PMID:1495391 !$#accession S22685 !'##molecule_type DNA !'##residues 1-100 ##label PUL !'##cross-references EMBL:X66934; NID:g49101; PIDN:CAA47368.1; !1PID:g49102 GENETICS !$#gene vagC !$#genome plasmid CLASSIFICATION #superfamily virulence-associated protein vagC SUMMARY #length 100 #molecular-weight 11492 #checksum 6462 SEQUENCE /// ENTRY S09497 #type complete TITLE virulence-associated protein, 32K - Salmonella choleraesuis plasmid pKDSC50 ALTERNATE_NAMES protein M3 ORGANISM #formal_name Salmonella choleraesuis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S09497 REFERENCE S09497 !$#authors Matsui, H.; Kawahara, K.; Terakado, N.; Danbara, H. !$#journal Nucleic Acids Res. (1990) 18:2181-2182 !$#title Nucleotide sequences of genes encoding 32 kDa and 70 kDa !1polypeptides in mba region of the virulence plasmid, !1pKDSC50, of Salmonella choleraesuis. !$#cross-references MUID:90245675; PMID:2336400 !$#accession S09497 !'##molecule_type DNA !'##residues 1-255 ##label MAT !'##cross-references EMBL:X52035; NID:g46896; PIDN:CAA36277.1; !1PID:g46897 GENETICS !$#genome plasmid pKDSC50 CLASSIFICATION #superfamily virulence-associated protein spvA SUMMARY #length 255 #molecular-weight 28184 #checksum 9572 SEQUENCE /// ENTRY S23715 #type complete TITLE virulence-associated protein mkfD - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S23715 REFERENCE S23714 !$#authors Norel, F.; Pisano, M.R.; Nicoli, J.; Popoff, M.Y. !$#journal Res. Microbiol. (1989) 140:627-630 !$#title A plasmid-borne virulence region (2.8 kb) from Salmonella !1typhimurium contains two open reading frames. !$#cross-references MUID:90176091; PMID:2697048 !$#accession S23715 !'##status preliminary !'##molecule_type DNA !'##residues 1-255 ##label NOR !'##cross-references EMBL:X57092; NID:g47788; PIDN:CAA40372.1; !1PID:g47790 GENETICS !$#gene mkfD CLASSIFICATION #superfamily virulence-associated protein spvA SUMMARY #length 255 #molecular-weight 28223 #checksum 9151 SEQUENCE /// ENTRY S09498 #type complete TITLE virulence-associated protein, 70K - Salmonella choleraesuis plasmid pKDSC50 ALTERNATE_NAMES protein M2 ORGANISM #formal_name Salmonella choleraesuis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S09498 REFERENCE S09497 !$#authors Matsui, H.; Kawahara, K.; Terakado, N.; Danbara, H. !$#journal Nucleic Acids Res. (1990) 18:2181-2182 !$#title Nucleotide sequences of genes encoding 32 kDa and 70 kDa !1polypeptides in mba region of the virulence plasmid, !1pKDSC50, of Salmonella choleraesuis. !$#cross-references MUID:90245675; PMID:2336400 !$#accession S09498 !'##molecule_type DNA !'##residues 1-591 ##label MAT !'##cross-references EMBL:X52035; NID:g46896; PIDN:CAA36278.1; !1PID:g46898 GENETICS !$#genome plasmid pKDSC50 CLASSIFICATION #superfamily virulence-associated protein spvB KEYWORDS DNA binding; transcription regulation SUMMARY #length 591 #molecular-weight 65341 #checksum 8680 SEQUENCE /// ENTRY S22664 #type complete TITLE virulence-associated protein spvB - Salmonella typhimurium plasmid ORGANISM #formal_name Salmonella typhimurium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S22664; S19790 REFERENCE S22663 !$#authors Gulig, P.A.; Caldwell, A.L.; Chiodo, V.A. !$#journal Mol. Microbiol. (1992) 6:1395-1411 !$#title Identification, genetic analysis and DNA sequence of a !17.8-kb virulence region of the Salmonella typhimurium !1virulence plasmid. !$#cross-references MUID:92349967; PMID:1322485 !$#accession S22664 !'##molecule_type DNA !'##residues 1-591 ##label GUL !'##cross-references EMBL:Z11557; NID:g47853; PIDN:CAA77649.1; !1PID:g47855 GENETICS !$#gene spvB !$#genome plasmid CLASSIFICATION #superfamily virulence-associated protein spvB KEYWORDS DNA binding; transcription regulation SUMMARY #length 591 #molecular-weight 65419 #checksum 8369 SEQUENCE /// ENTRY S30896 #type complete TITLE virulence-associated protein mba1 - Salmonella choleraesuis plasmid pKDSC50 ORGANISM #formal_name Salmonella choleraesuis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S30896; S20733 REFERENCE S30896 !$#authors Matsui, H.; Abe, A.; Suzuki, S.; Kijima, M.; Tamura, Y.; !1Nakamura, M.; Kawahara, K.; Danbara, H. !$#journal Mol. Gen. Genet. (1993) 236:219-226 !$#title Molecular mechanism of the regulation of expression of !1plasmid-encoded mouse bacteremia (mba) genes in Salmonella !1serovar Choleraesuis. !$#cross-references MUID:93173095; PMID:8437568 !$#accession S30896 !'##molecule_type DNA !'##residues 1-297 ##label MAT !'##cross-references EMBL:X54148; NID:g48765; PIDN:CAA38087.1; !1PID:g48766 GENETICS !$#gene mba1 !$#genome plasmid CLASSIFICATION #superfamily virulence-associated protein spvR KEYWORDS DNA binding; transcription regulation SUMMARY #length 297 #molecular-weight 34006 #checksum 7059 SEQUENCE /// ENTRY S06670 #type complete TITLE virulence-associated protein, mkaC - Salmonella typhimurium plasmid ALTERNATE_NAMES 33K virulence protein spvR ORGANISM #formal_name Salmonella typhimurium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S06670; A41318; S06089; S23714; S15213; C54540 REFERENCE S06669 !$#authors Taira, S.; Rhen, M. !$#journal FEBS Lett. (1989) 257:274-278 !$#title Molecular organization of genes constituting the virulence !1determinant on the Salmonella typhimurium 96 kilobase pair !1plasmid. !$#cross-references MUID:90060335; PMID:2684688 !$#accession S06670 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-297 ##label TAI !'##experimental_source virulence plasmid REFERENCE A41318 !$#authors Caldwell, A.L.; Gulig, P.A. !$#journal J. Bacteriol. (1991) 173:7176-7185 !$#title The Salmonella typhimurium virulence plasmid encodes a !1positive regulator of a plasmid-encoded virulence gene. !$#cross-references MUID:92041614; PMID:1657882 !$#accession A41318 !'##status preliminary !'##molecule_type DNA !'##residues 1-295 ##label CAL !'##cross-references GB:M74110 !'##experimental_source strain SR-11, virulence plasmid REFERENCE S06089 !$#authors Pullinger, G.D.; Baird, G.D.; Williamson, C.M.; Lax, A.J. !$#journal Nucleic Acids Res. (1989) 17:7983 !$#title Nucleotide sequence of a plasmid gene involved in the !1virulence of salmonellas. !$#cross-references MUID:90016881; PMID:2798139 !$#accession S06089 !'##molecule_type DNA !'##residues 1-297 ##label PUL !'##cross-references EMBL:X16111; NID:g47859; PIDN:CAA34244.1; !1PID:g47860 !'##experimental_source isolate 1275 wild-type, virulence plasmid REFERENCE S23714 !$#authors Norel, F.; Pisano, M.R.; Nicoli, J.; Popoff, M.Y. !$#journal Res. Microbiol. (1989) 140:627-630 !$#title A plasmid-borne virulence region (2.8 kb) from Salmonella !1typhimurium contains two open reading frames. !$#cross-references MUID:90176091; PMID:2697048 !$#accession S23714 !'##status preliminary !'##molecule_type DNA !'##residues 1-297 ##label NOR !'##cross-references EMBL:X57092; NID:g47788; PIDN:CAA40371.1; !1PID:g47789 !'##experimental_source strain C5, virulence plasmid REFERENCE S15213 !$#authors Krause, M.; Roudier, C.; Fierer, J.; Harwood, J.; Guiney, D. !$#journal Mol. Microbiol. (1991) 5:307-316 !$#title Molecular analysis of the virulence locus of the Salmonella !1dublin plasmid pSDL2. !$#cross-references MUID:91251759; PMID:2041471 !$#accession S15213 !'##status preliminary !'##molecule_type DNA !'##residues 1-40,'G',42-103,'E',105-297 ##label KRA !'##cross-references EMBL:X56727; NID:g47836; PIDN:CAA40047.1; !1PID:g47837 REFERENCE A54540 !$#authors Taira, S.; Baumann, M.; Riikonen, P.; Sukupolvi, S.; Rhen, !1M. !$#journal FEMS Microbiol. Lett. (1991) 77:319-324 !$#title Amino-terminal sequence analysis of four plasmid-encoded !1virulence-associated proteins of Salmonella typhimurium. !$#accession C54540 !'##status preliminary !'##molecule_type protein !'##residues 1-10 ##label TA2 GENETICS !$#gene mkaC; mkfC; spvR !$#genome plasmid CLASSIFICATION #superfamily virulence-associated protein spvR KEYWORDS DNA binding; transcription regulation SUMMARY #length 297 #molecular-weight 33835 #checksum 7032 SEQUENCE /// ENTRY B64779 #type complete TITLE hypothetical protein b0483 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS B64779 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64779 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-131 ##label BLAT !'##cross-references GB:AE000154; GB:U00096; NID:g1786683; !1PIDN:AAC73585.1; PID:g1786690; UWGP:b0483 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily virulence-associated protein vapA SUMMARY #length 131 #molecular-weight 15322 #checksum 2947 SEQUENCE /// ENTRY D49205 #type complete TITLE virulence-associated protein vapA - Dichelobacter nodosus ORGANISM #formal_name Dichelobacter nodosus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 24-Sep-1999 ACCESSIONS D49205 REFERENCE A49205 !$#authors Katz, M.E.; Strugnell, R.A.; Rood, J.I. !$#journal Infect. Immun. (1992) 60:4586-4592 !$#title Molecular characterization of a genomic region associated !1with virulence in Dichelobacter nodosus. !$#cross-references MUID:93014173; PMID:1398971 !$#accession D49205 !'##status preliminary !'##molecule_type DNA !'##residues 1-102 ##label KAT !'##cross-references GB:L22308; NID:g438532; PIDN:AAA20207.1; !1PID:g438536 !'##note sequence extracted from NCBI backbone (NCBIN:116426, !1NCBIP:116432) CLASSIFICATION #superfamily virulence-associated protein vapA KEYWORDS DNA binding; transcription regulation SUMMARY #length 102 #molecular-weight 11266 #checksum 5194 SEQUENCE /// ENTRY H64112 #type complete TITLE virulence-associated protein vapA homolog HI1251 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS H64112 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession H64112 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-107 ##label TIGR !'##cross-references GB:U32805; GB:L42023; NID:g1574180; !1PIDN:AAC22901.1; PID:g1574183; TIGR:HI1251 CLASSIFICATION #superfamily virulence-associated protein vapA KEYWORDS DNA binding; transcription regulation SUMMARY #length 107 #molecular-weight 12347 #checksum 3954 SEQUENCE /// ENTRY C49205 #type complete TITLE virulence-associated protein vapB - Dichelobacter nodosus ORGANISM #formal_name Dichelobacter nodosus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 24-Sep-1999 ACCESSIONS C49205 REFERENCE A49205 !$#authors Katz, M.E.; Strugnell, R.A.; Rood, J.I. !$#journal Infect. Immun. (1992) 60:4586-4592 !$#title Molecular characterization of a genomic region associated !1with virulence in Dichelobacter nodosus. !$#cross-references MUID:93014173; PMID:1398971 !$#accession C49205 !'##status preliminary !'##molecule_type DNA !'##residues 1-76 ##label KAT !'##cross-references GB:L22308; NID:g438532; PIDN:AAA20206.1; !1PID:g438535 !'##note sequence extracted from NCBI backbone (NCBIN:116426, !1NCBIP:116431) CLASSIFICATION #superfamily virulence-associated protein vapB KEYWORDS DNA binding; transcription regulation SUMMARY #length 76 #molecular-weight 8899 #checksum 7846 SEQUENCE /// ENTRY S74973 #type complete TITLE virulence associated protein vapB - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein ssl2922 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S74973 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74973 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-75 ##label KAN !'##cross-references EMBL:D90902; GB:AB001339; NID:g1652027; !1PIDN:BAA17013.1; PID:g1652088 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene vapB CLASSIFICATION #superfamily virulence-associated protein vapB KEYWORDS DNA binding; transcription regulation SUMMARY #length 75 #molecular-weight 8539 #checksum 9185 SEQUENCE /// ENTRY C27893 #type complete TITLE transcription regulator gerE - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 19-Nov-1988 #sequence_revision 02-Jun-1994 #text_change 16-Jun-2000 ACCESSIONS C27893; S04469; G69630 REFERENCE A92785 !$#authors Cutting, S.; Mandelstam, J. !$#journal J. Gen. Microbiol. (1986) 132:3013-3024 !$#title The nucleotide sequence and the transcription during !1sporulation of the gerE gene of Bacillus subtilis. !$#cross-references MUID:87310370; PMID:3114423 !$#accession C27893 !'##molecule_type DNA !'##residues 1-74 ##label CUT !'##cross-references GB:M17642; NID:g142966; PIDN:AAA22473.1; !1PID:g142969 REFERENCE S04469 !$#authors Cutting, S.; Panzer, S.; Losick, R. !$#journal J. Mol. Biol. (1989) 207:393-404 !$#title Regulatory studies on the promoter for a gene governing !1synthesis and assembly of the spore coat in Bacillus !1subtilis. !$#cross-references MUID:89329031; PMID:2474075 !$#accession S04469 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-10,'L',12-35 ##label CU2 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69630 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-74 ##label KUN !'##cross-references GB:Z99118; GB:AL009126; NID:g2635200; !1PIDN:CAB14801.1; PID:g2635306 !'##experimental_source strain 168 COMMENT The gerE locus is a monocistronic operon switched on in the !1mother cell during stage V of sporulation. Its product is a !1small regulatory protein required for expression of the !1correct coat protein genes, synthesis of an intracellular !1protease (protease e), and perhaps for regulation of other !1late sporulation genes. The impaired germination of gerE !1mutants may be a secondary effect of defective sporulation. COMMENT This protein contains a pentapeptide sequence identical to !1the target site in the alpha/beta type small acid-soluble !1spore proteins (SASP) for the tetrameric spore protease GPR. GENETICS !$#gene gerE !$#start_codon TTG CLASSIFICATION #superfamily transcription regulator gerE KEYWORDS DNA binding; sporulation; transcription regulation SUMMARY #length 74 #molecular-weight 8562 #checksum 7849 SEQUENCE /// ENTRY B70018 #type complete TITLE transcription regulator GntR family homolog yurK - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS B70018 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B70018 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-242 ##label KUN !'##cross-references GB:Z99120; GB:AL009126; NID:g2635613; !1PIDN:CAB15246.1; PID:g2635753 !'##experimental_source strain 168 GENETICS !$#gene yurK CLASSIFICATION #superfamily transcription regulator GntR SUMMARY #length 242 #molecular-weight 27509 #checksum 1557 SEQUENCE /// ENTRY B65132 #type complete TITLE hypothetical transcription regulator, cysG-trpS intergenic region - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS B65132 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65132 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-265 ##label BLAT !'##cross-references GB:AE000413; GB:U00096; NID:g2367215; !1PIDN:AAC76400.1; PID:g1789776; UWGP:b3375 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yhfR CLASSIFICATION #superfamily transcription regulator GntR SUMMARY #length 265 #molecular-weight 30215 #checksum 9249 SEQUENCE /// ENTRY F69750 #type complete TITLE transcription regulator GntR family homolog ybgA - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS F69750 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69750 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-235 ##label KUN !'##cross-references GB:Z99105; GB:AL009126; NID:g2632457; !1PIDN:CAB12031.1; PID:g2632523 !'##experimental_source strain 168 GENETICS !$#gene ybgA CLASSIFICATION #superfamily transcription regulator GntR SUMMARY #length 235 #molecular-weight 26603 #checksum 7433 SEQUENCE /// ENTRY S04645 #type complete TITLE transcription regulator farR, fatty acyl-responsive - Escherichia coli (strain K-12) ALTERNATE_NAMES gp30 protein ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS S04645; S50896; A64809; PC4138 REFERENCE S04645 !$#authors Buck, D.; Guest, J.R. !$#journal Biochem. J. (1989) 260:737-747 !$#title Overexpression and site-directed mutagenesis of the !1succinyl-CoA synthetase of Escherichia coli and nucleotide !1sequence of a gene (g30) that is adjacent to the suc operon. !$#cross-references MUID:89350876; PMID:2548486 !$#accession S04645 !'##molecule_type DNA !'##residues 1-240 ##label BUC !'##cross-references EMBL:X15790; NID:g41518; PIDN:CAA33791.1; !1PID:g41519 REFERENCE S50896 !$#authors Quail, M.A.; Dempsey, C.E.; Guest, J.R. !$#journal FEBS Lett. (1994) 356:183-187 !$#title Identification of a fatty acyl responsive regulator (FarR) !1in Escherichia coli. !$#cross-references MUID:95104410; PMID:7805834 !$#accession S50896 !'##status preliminary !'##molecule_type DNA !'##residues 1-12 ##label QUA REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64809 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-240 ##label BLAT !'##cross-references GB:AE000176; GB:U00096; NID:g1786947; !1PIDN:AAC73824.1; PID:g1786950; UWGP:b0730 !'##experimental_source strain K-12, substrain MG1655 REFERENCE JC4598 !$#authors Utsumi, R.; Horie, T.; Katoh, A.; Kaino, Y.; Tanabe, H.; !1Noda, M. !$#journal Biosci. Biotechnol. Biochem. (1996) 60:309-315 !$#title Isolation and characterization of the heat-responsive genes !1in Escherichia coli. !$#cross-references MUID:97076625; PMID:9063979 !$#accession PC4138 !'##molecule_type DNA !'##residues 1-40 ##label UTS !'##cross-references DDBJ:D64014 !'##experimental_source RU1012 GENETICS !$#gene farR; gp30 !$#map_position 16.8 min FUNCTION !$#description probably a transcription regulator of the succinyl-CoA !1synthase operon; negatively autoregulates its own synthesis !1in response to long-chain fatty acid deficiency CLASSIFICATION #superfamily transcription regulator GntR KEYWORDS DNA binding; transcription regulation SUMMARY #length 240 #molecular-weight 28273 #checksum 4844 SEQUENCE /// ENTRY E65170 #type complete TITLE hypothetical transcription regulator, ilvO-ibpB intergenic region - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS E65170 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65170 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-238 ##label BLAT !'##cross-references GB:AE000445; GB:U00096; NID:g1790105; !1PIDN:AAC76707.1; PID:g1790118; UWGP:b3684 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yidP CLASSIFICATION #superfamily transcription regulator GntR SUMMARY #length 238 #molecular-weight 27328 #checksum 1413 SEQUENCE /// ENTRY G69999 #type complete TITLE transcription regulator GntR related protein ytrA - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS G69999 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69999 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-130 ##label KUN !'##cross-references GB:Z99119; GB:AL009126; NID:g2635411; !1PIDN:CAB15024.1; PID:g2635530 !'##experimental_source strain 168 GENETICS !$#gene ytrA CLASSIFICATION #superfamily transcription regulator gntR-related protein !1ytrA SUMMARY #length 130 #molecular-weight 14694 #checksum 403 SEQUENCE /// ENTRY B69822 #type complete TITLE transcription regulator GntR related protein yhcF - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS B69822 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69822 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-121 ##label KUN !'##cross-references GB:Z99108; GB:AL009126; NID:g2633055; !1PIDN:CAB12734.1; PID:g2633229 !'##experimental_source strain 168 GENETICS !$#gene yhcF CLASSIFICATION #superfamily transcription regulator gntR-related protein !1ytrA SUMMARY #length 121 #molecular-weight 13953 #checksum 4560 SEQUENCE /// ENTRY S08402 #type complete TITLE virulence associated protein, 29K - Salmonella choleraesuis plasmid pKDSC50 ORGANISM #formal_name Salmonella choleraesuis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S08402 REFERENCE S08402 !$#authors Matsui, H.; Kawahara, K.; Terakado, N.; Danbara, H. !$#journal Nucleic Acids Res. (1990) 18:1055 !$#title Nucleotide sequence of a gene encoding a 29 kDa polypeptide !1in mba region of the virulence plasmid, pKDSC50, of !1Salmonella choleraesuis. !$#cross-references MUID:90192096; PMID:2315022 !$#accession S08402 !'##molecule_type DNA !'##residues 1-241 ##label MAT !'##cross-references EMBL:X51453; NID:g46884; PIDN:CAA35819.1; !1PID:g46885 GENETICS !$#genome plasmid CLASSIFICATION #superfamily virulence-associated protein mkfA SUMMARY #length 241 #molecular-weight 27668 #checksum 3003 SEQUENCE /// ENTRY C64069 #type complete TITLE virulence-associated protein vapD homolog HI0450 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C64069 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession C64069 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-91 ##label TIGR !'##cross-references GB:U32728; GB:L42023; NID:g1573425; !1PIDN:AAC22108.1; PID:g1573426; TIGR:HI0450 CLASSIFICATION #superfamily virulence-associated protein vapD SUMMARY #length 91 #molecular-weight 10543 #checksum 332 SEQUENCE /// ENTRY A49205 #type complete TITLE virulence-associated protein vapD - Dichelobacter nodosus ORGANISM #formal_name Dichelobacter nodosus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 24-Sep-1999 ACCESSIONS A49205 REFERENCE A49205 !$#authors Katz, M.E.; Strugnell, R.A.; Rood, J.I. !$#journal Infect. Immun. (1992) 60:4586-4592 !$#title Molecular characterization of a genomic region associated !1with virulence in Dichelobacter nodosus. !$#cross-references MUID:93014173; PMID:1398971 !$#accession A49205 !'##status preliminary !'##molecule_type DNA !'##residues 1-93 ##label KAT !'##cross-references GB:L22308; NID:g438532; PIDN:AAA20204.1; !1PID:g438533 !'##note sequence extracted from NCBI backbone (NCBIN:116426, !1NCBIP:116427) CLASSIFICATION #superfamily virulence-associated protein vapD SUMMARY #length 93 #molecular-weight 10590 #checksum 7423 SEQUENCE /// ENTRY S56404 #type complete TITLE virulence-associated protein vacB homolog - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS S56404; C31965; F65228 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56404 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-827 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97075.1; !1PID:g537020 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A31965 !$#authors Wolfe, S.A.; Smith, J.M. !$#journal J. Biol. Chem. (1988) 263:19147-19153 !$#title Nucleotide sequence and analysis of the purA gene encoding !1adenylosuccinate synthetase of Escherichia coli K12. !$#cross-references MUID:89066719; PMID:3058695 !$#accession C31965 !'##molecule_type DNA !'##residues 15-100 ##label WOL !'##cross-references GB:J04199 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65228 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-827 ##label BLAT !'##cross-references GB:AE000490; GB:U00096; NID:g2367356; !1PIDN:AAC77136.1; PID:g1790622; UWGP:b4179 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene vacB !$#map_position 95 min !$#start_codon GTG CLASSIFICATION #superfamily virulence-associated protein vacB homolog SUMMARY #length 827 #molecular-weight 93687 #checksum 3851 SEQUENCE /// ENTRY G64098 #type complete TITLE virulence-associated protein vacB homolog HI0861 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS G64098 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession G64098 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-782 ##label TIGR !'##cross-references GB:U32767; GB:L42023; NID:g1573868; !1PIDN:AAC22520.1; PID:g1573876; TIGR:HI0861 CLASSIFICATION #superfamily virulence-associated protein vacB homolog SUMMARY #length 782 #molecular-weight 89845 #checksum 6878 SEQUENCE /// ENTRY S73915 #type complete TITLE virulence-associated protein vacB homolog - Mycoplasma pneumoniae (strain ATCC 29342) ALTERNATE_NAMES hypothetical protein K04_orf726 ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Dec-1999 ACCESSIONS S73915 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73915 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-726 ##label HIM !'##cross-references EMBL:AE000057; GB:U00089; NID:g1674279; !1PIDN:AAB96237.1; PID:g1674290 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#gene vacB !$#genetic_code SGC3 CLASSIFICATION #superfamily virulence-associated protein vacB homolog SUMMARY #length 726 #molecular-weight 83218 #checksum 1103 SEQUENCE /// ENTRY E64211 #type complete TITLE virulence-associated protein vacB homolog - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 07-Dec-1999 ACCESSIONS E64211 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession E64211 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-725 ##label TIGR !'##cross-references GB:U39690; GB:L43967; NID:g1045782; PID:g1045783; !1TIGR:MG104 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily virulence-associated protein vacB homolog SUMMARY #length 725 #molecular-weight 82898 #checksum 8144 SEQUENCE /// ENTRY QRECCZ #type complete TITLE chemotaxis protein cheZ - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 01-Mar-2002 ACCESSIONS F25195; A64951 REFERENCE A91811 !$#authors Mutoh, N.; Simon, M.I. !$#journal J. Bacteriol. (1986) 165:161-166 !$#title Nucleotide sequence corresponding to five chemotaxis genes !1in Escherichia coli. !$#cross-references MUID:86085665; PMID:3510184 !$#accession F25195 !'##molecule_type DNA !'##residues 1-214 ##label MUT !'##cross-references GB:M13463; NID:g145517 !'##note the sequence in GenBank entry ECOCHE3, release 111.0, !1(PID:g145526) has the codon CCA for 119-Ala rather than the !1published GCA, and the codon GGG for 130-Ala rather than the !1published GCG REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64951 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-214 ##label BLAT !'##cross-references GB:AE000282; GB:U00096; NID:g1788189; !1PIDN:AAC74951.1; PID:g1788190; UWGP:b1881 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A30660 !$#authors Stock, A.; Schaeffer, E.; Koshland Jr., D.E.; Stock, J. !$#journal J. Biol. Chem. (1987) 262:8011-8014 !$#title A second type of protein methylation reaction in bacterial !1chemotaxis. !$#cross-references MUID:87250383; PMID:3298225 !$#contents annotation; identification of modification !$#note it is demonstrated that 1-Met, and not 2-Met, is methylated COMMENT This protein is involved in generating a regulating signal !1for bacterial flagellar rotation. GENETICS !$#gene cheZ !$#map_position 42 min CLASSIFICATION #superfamily chemotaxis cheZ protein KEYWORDS chemotaxis; flagellar rotation; methylated amino end FEATURE !$1 #modified_site methylated amino end (Met) #status !8experimental SUMMARY #length 214 #molecular-weight 23976 #checksum 4289 SEQUENCE /// ENTRY QRECMA #type complete TITLE chemotaxis protein motA - Escherichia coli (strain K-12) ALTERNATE_NAMES motility protein A ORGANISM #formal_name Escherichia coli DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 01-Mar-2002 ACCESSIONS A30279; B64952 REFERENCE A94494 !$#authors Dean, G.; Stader, J.; Macnab, R.; Matsumura, P. !$#submission submitted to the EMBL Data Library, June 1983 !$#accession A30279 !'##molecule_type DNA !'##residues 1-295 ##label DEA !'##cross-references EMBL:J01652; NID:g146881; PIDN:AAA24177.1; !1PID:g146882 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64952 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-295 ##label BLAT !'##cross-references GB:AE000282; GB:U00096; NID:g1788189; !1PIDN:AAC74960.1; PID:g1788199; UWGP:b1890 !'##experimental_source strain K-12, substrain MG1655 COMMENT This protein is thought to be a membrane protein. GENETICS !$#gene motA !$#map_position 42 min !$#start_codon GTG CLASSIFICATION #superfamily motA protein KEYWORDS chemotaxis; flagellar rotation; membrane protein SUMMARY #length 295 #molecular-weight 32011 #checksum 7793 SEQUENCE /// ENTRY QRECMB #type complete TITLE chemotaxis protein motB - Escherichia coli (strain K-12) ALTERNATE_NAMES motility protein B ORGANISM #formal_name Escherichia coli DATE 31-Mar-1989 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS A64952; A58693; A30280 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64952 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-308 ##label BLAT !'##cross-references GB:AE000282; GB:U00096; NID:g1788189; !1PIDN:AAC74959.1; PID:g1788198; UWGP:b1889 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A58693 !$#authors Stader, J.; Matsumura, P.; Vacante, D.; Dean, G.E.; Macnab, !1R.M. !$#journal J. Bacteriol. (1986) 166:244-252 !$#title Nucleotide sequence of the Escherichia coli motB gene and !1site-limited incorporation of its product into the !1cytoplasmic membrane. !$#cross-references MUID:86168022; PMID:3007435 !$#accession A58693 !'##molecule_type DNA !'##residues 1-308 ##label STA !'##cross-references EMBL:J01652; NID:g146881; PIDN:AAA24178.1; !1PID:g146883 !'##note the sequence in this report is a revision of the sequence in !1A94494 REFERENCE A94494 !$#authors Dean, G.; Stader, J.; Macnab, R.; Matsumura, P. !$#submission submitted to the EMBL Data Library, June 1983 !$#accession A30280 !'##molecule_type DNA !'##residues 1-154,'KPEFARCLEPAVPCRTLYARHSAR',179-217,'V',219-249,'A', !1251-288,'KNLRLHHRSVF',300, !1'QCHQPNRGDSVSMDISDFYQTFFDEADELLADMEQHLLVLQPEAPDAEQLNAIFRAAH' !1##label DEA !'##cross-references EMBL:J01652 GENETICS !$#gene motB !$#map_position 42 min CLASSIFICATION #superfamily motB protein KEYWORDS chemotaxis; flagellar rotation; transmembrane protein SUMMARY #length 308 #molecular-weight 34186 #checksum 1602 SEQUENCE /// ENTRY XMECF1 #type complete TITLE flagellar protein fliL - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 01-Mar-2002 ACCESSIONS A29842; E64958; S78695 REFERENCE A91814 !$#authors Kuo, S.C.; Koshland Jr., D.E. !$#journal J. Bacteriol. (1986) 166:1007-1012 !$#title Sequence of the flaA (cheC) locus of Escherichia coli and !1discovery of a new gene. !$#cross-references MUID:86223759; PMID:3519573 !$#accession A29842 !'##molecule_type DNA !'##residues 1-154 ##label KUO !'##cross-references GB:M12784; NID:g145979; PIDN:AAA23785.1; !1PID:g145980 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64958 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-154 ##label BLAT !'##cross-references GB:AE000286; GB:U00096; NID:g1788241; !1PIDN:AAC75011.1; PID:g1788254; UWGP:b1944 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S78690 !$#authors Kawagishi, I.; Homma, M.; Williams, A.W.; Macnab, R.M. !$#journal J. Bacteriol. (1996) 178:2954-2959 !$#title Characterization of the flagellar hook length control !1protein fliK of Salmonella typhimurium and Escherichia coli. !$#cross-references MUID:96213039; PMID:8631687 !$#accession S78695 !'##molecule_type DNA !'##residues 1-16 ##label KAW !'##cross-references EMBL:L43491; NID:g894081; PIDN:AAB06633.1; !1PID:g894084 !'##experimental_source strain K-12, substrain KS650 GENETICS !$#gene fliL; flaAI; cheCI !$#map_position 43 min FUNCTION !$#description part of the flagellar switch mediating flagella rotation !1during chemotaxis CLASSIFICATION #superfamily flaAI protein KEYWORDS chemotaxis; flagellar rotation; flagellum; membrane protein SUMMARY #length 154 #molecular-weight 17221 #checksum 8034 SEQUENCE /// ENTRY XMECF2 #type complete TITLE flagellar motor switch protein fliM - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 01-Mar-2002 ACCESSIONS B29842; PS0027; F64958 REFERENCE A91814 !$#authors Kuo, S.C.; Koshland Jr., D.E. !$#journal J. Bacteriol. (1986) 166:1007-1012 !$#title Sequence of the flaA (cheC) locus of Escherichia coli and !1discovery of a new gene. !$#cross-references MUID:86223759; PMID:3519573 !$#accession B29842 !'##molecule_type DNA !'##residues 1-334 ##label KUO !'##cross-references EMBL:M12784; NID:g145979; PIDN:AAA23786.1; !1PID:g145981 REFERENCE PS0027 !$#authors Malakooti, J.; Komeda, Y.; Matsumura, P. !$#journal J. Bacteriol. (1989) 171:2728-2734 !$#title DNA sequence analysis, gene product identification, and !1localization of flagellar motor components of Escherichia !1coli. !$#cross-references MUID:89213963; PMID:2651416 !$#accession PS0027 !'##molecule_type DNA !'##residues 327-334 ##label MAL !'##cross-references GB:M26294 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64958 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-334 ##label BLAT !'##cross-references GB:AE000286; GB:U00096; NID:g1788241; !1PIDN:AAC75012.1; PID:g1788255; UWGP:b1945 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene fliM; flaAII; cheCII; flaA; cheC !$#map_position 43 min FUNCTION !$#description part of the flagellar switch mediating flagella rotation !1during chemotaxis !$#note there are three switch proteins (fliG, fliM, fliN) which !1together determine the direction of rotation; fliG-fliM !1interaction plays a central role in switching CLASSIFICATION #superfamily flagellar motor switch protein fliM KEYWORDS chemotaxis; flagellar rotation; flagellum SUMMARY #length 334 #molecular-weight 37849 #checksum 6623 SEQUENCE /// ENTRY C30929 #type complete TITLE flagellar motor switch protein fliM - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C44513; C30929 REFERENCE A44513 !$#authors Kihara, M.; Homma, M.; Kutsukake, K.; Macnab, R.M. !$#journal J. Bacteriol. (1989) 171:3247-3257 !$#title Flagellar switch of Salmonella typhimurium: gene sequences !1and deduced protein sequences. !$#cross-references MUID:89255090; PMID:2656645 !$#accession C44513 !'##status preliminary !'##molecule_type DNA !'##residues 1-334 ##label KIH !'##cross-references EMBL:M24463; NID:g154032; PIDN:AAA27104.1; !1PID:g154035 GENETICS !$#gene fliM; formerly flaQII !$#map_position 40 min FUNCTION !$#description part of the flagellar switch mediating flagella rotation !1during chemotaxis !$#note there are three switch proteins (fliG, fliM, fliN) which !1together determine the direction of rotation; fliG-fliM !1interaction plays a central role in switching CLASSIFICATION #superfamily flagellar motor switch protein fliM KEYWORDS chemotaxis; flagellar rotation; flagellum SUMMARY #length 334 #molecular-weight 37858 #checksum 6058 SEQUENCE /// ENTRY B39136 #type complete TITLE flagellar motor switch protein fliM - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS B39136; B38845; S25278; A69625; S14504 REFERENCE A39136 !$#authors Zuberi, A.R.; Bischoff, D.S.; Ordal, G.W. !$#journal J. Bacteriol. (1991) 173:710-719 !$#title Nucleotide sequence and characterization of a Bacillus !1subtilis gene encoding a flagellar switch protein. !$#cross-references MUID:91100360; PMID:1898932 !$#accession B39136 !'##molecule_type DNA !'##residues 1-332 ##label ZUB !'##cross-references GB:M37691; NID:g142920; PIDN:AAA22446.1; !1PID:g142922 REFERENCE A42365 !$#authors Albertini, A.M.; Caramori, T.; Crabb, W.D.; Scoffone, F.; !1Galizzi, A. !$#journal J. Bacteriol. (1991) 173:3573-3579 !$#title The flaA locus of Bacillus subtilis is part of a large !1operon coding for flagellar structures, motility functions, !1and an ATPase-like polypeptide. !$#cross-references MUID:91258343; PMID:1828465 !$#accession B38845 !'##status preliminary !'##molecule_type DNA !'##residues 1-59 ##label ALB !'##cross-references EMBL:X56049 REFERENCE S25278 !$#authors Bischoff, D.S.; Ordal, G.W. !$#journal Mol. Microbiol. (1992) 6:2715-2723 !$#title Identification and characterization of FliY, a novel !1component of the Bacillus subtilis flagellar switch complex. !$#cross-references MUID:93078625; PMID:1447979 !$#accession S25278 !'##molecule_type DNA !'##residues 309-332 ##label BIS !'##cross-references EMBL:M86738; NID:g142924; PIDN:AAA22448.1; !1PID:g142925 !'##note the authors translated the codon GGC for residue 2 as Gln and !1ATA for residue 17 as Leu REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69625 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-332 ##label KUN !'##cross-references GB:Z99112; GB:AL009126; NID:g2633902; !1PIDN:CAB13504.1; PID:g2634003 !'##experimental_source strain 168 GENETICS !$#gene fliM CLASSIFICATION #superfamily flagellar motor switch protein fliM KEYWORDS flagellar rotation SUMMARY #length 332 #molecular-weight 37529 #checksum 4644 SEQUENCE /// ENTRY G64648 #type complete TITLE flagellar motor switch protein - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS G64648 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession G64648 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-354 ##label TOM !'##cross-references GB:AE000611; GB:AE000511; NID:g2314173; !1PIDN:AAD08075.1; PID:g2314176; TIGR:HP1031 CLASSIFICATION #superfamily flagellar motor switch protein fliM SUMMARY #length 354 #molecular-weight 40170 #checksum 9765 SEQUENCE /// ENTRY A41875 #type complete TITLE flagellar switch protein fliM - Caulobacter crescentus ORGANISM #formal_name Caulobacter crescentus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A41875 REFERENCE A41875 !$#authors Yu, J.; Shapiro, L. !$#journal J. Bacteriol. (1992) 174:3327-3338 !$#title Early Caulobacter crescentus genes fliL and fliM are !1required for flagellar gene expression and normal cell !1division. !$#cross-references MUID:92250429; PMID:1315735 !$#accession A41875 !'##status preliminary !'##molecule_type DNA !'##residues 1-373 ##label YUA !'##cross-references GB:M85232; NID:g682648; PIDN:AAA62449.1; !1PID:g144253 GENETICS !$#gene fliM CLASSIFICATION #superfamily flagellar motor switch protein fliM KEYWORDS flagellar rotation SUMMARY #length 373 #molecular-weight 41331 #checksum 3631 SEQUENCE /// ENTRY XMEBFB #type complete TITLE flagellar basal body rod protein flgB - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS S08171; S15353; JS0346 REFERENCE S08171 !$#authors Homma, M.; Kutsukake, K.; Hasebe, M.; Iino, T.; Macnab, R.M. !$#journal J. Mol. Biol. (1990) 211:465-477 !$#title FlgB, FlgC, FlgF and FlgG. A family of structurally related !1proteins in the flagellar basal body of Salmonella !1typhimurium. !$#cross-references MUID:90172414; PMID:2129540 !$#accession S08171 !'##molecule_type DNA !'##residues 1-138 ##label HOM !'##cross-references EMBL:X52093; NID:g47668; PIDN:CAA36309.1; !1PID:g47669 REFERENCE S15353 !$#authors Jones, C.J.; Macnab, R.M.; Okino, H.; Aizawa, S.I. !$#journal J. Mol. Biol. (1990) 212:377-387 !$#title Stoichiometric analysis of the flagellar hook-(basal-body) !1complex of Salmonella typhimurium. !$#cross-references MUID:90204563; PMID:2181149 !$#accession S15353 !'##molecule_type protein !'##residues 2-5 ##label JON REFERENCE A94543 !$#authors Kutsukake, K.; Iino, T. !$#submission submitted to JIPID, November 1989 !$#accession JS0346 !'##molecule_type DNA !'##residues 1-138 ##label KUT !'##experimental_source strain LT2 GENETICS !$#gene flgB !$#map_position 23 min FUNCTION !$#description component of the proximal rod CLASSIFICATION #superfamily rod protein flgB KEYWORDS basal body; flagellum FEATURE !$2-138 #product rod protein flgB #status experimental #label !8MAT SUMMARY #length 138 #molecular-weight 15129 #checksum 4378 SEQUENCE /// ENTRY XMEBFC #type complete TITLE flagellar basal body rod protein flgC - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS S08172; S15354; JS0347 REFERENCE S08171 !$#authors Homma, M.; Kutsukake, K.; Hasebe, M.; Iino, T.; Macnab, R.M. !$#journal J. Mol. Biol. (1990) 211:465-477 !$#title FlgB, FlgC, FlgF and FlgG. A family of structurally related !1proteins in the flagellar basal body of Salmonella !1typhimurium. !$#cross-references MUID:90172414; PMID:2129540 !$#accession S08172 !'##molecule_type DNA !'##residues 1-134 ##label HOM !'##cross-references EMBL:X52093; NID:g47668; PIDN:CAA36310.1; !1PID:g581758 REFERENCE S15353 !$#authors Jones, C.J.; Macnab, R.M.; Okino, H.; Aizawa, S.I. !$#journal J. Mol. Biol. (1990) 212:377-387 !$#title Stoichiometric analysis of the flagellar hook-(basal-body) !1complex of Salmonella typhimurium. !$#cross-references MUID:90204563; PMID:2181149 !$#accession S15354 !'##molecule_type protein !'##residues 1-5 ##label JON REFERENCE A94543 !$#authors Kutsukake, K.; Iino, T. !$#submission submitted to JIPID, November 1989 !$#accession JS0347 !'##molecule_type DNA !'##residues 1-134 ##label KUT !'##experimental_source strain LT2 GENETICS !$#gene flgC !$#map_position 23 min !$#start_codon GTG FUNCTION !$#description component of the proximal rod CLASSIFICATION #superfamily rod protein flgC KEYWORDS basal body; flagellum SUMMARY #length 134 #molecular-weight 13996 #checksum 763 SEQUENCE /// ENTRY XMEBFF #type complete TITLE flagellar basal body rod protein flgF - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS S08173; S15355 REFERENCE S08171 !$#authors Homma, M.; Kutsukake, K.; Hasebe, M.; Iino, T.; Macnab, R.M. !$#journal J. Mol. Biol. (1990) 211:465-477 !$#title FlgB, FlgC, FlgF and FlgG. A family of structurally related !1proteins in the flagellar basal body of Salmonella !1typhimurium. !$#cross-references MUID:90172414; PMID:2129540 !$#accession S08173 !'##molecule_type DNA !'##residues 1-251 ##label HOM !'##cross-references EMBL:X52094; NID:g47674; PIDN:CAA36313.1; !1PID:g47676 REFERENCE S15353 !$#authors Jones, C.J.; Macnab, R.M.; Okino, H.; Aizawa, S.I. !$#journal J. Mol. Biol. (1990) 212:377-387 !$#title Stoichiometric analysis of the flagellar hook-(basal-body) !1complex of Salmonella typhimurium. !$#cross-references MUID:90204563; PMID:2181149 !$#accession S15355 !'##molecule_type protein !'##residues 1-5 ##label JON GENETICS !$#gene flgF FUNCTION !$#description component of the proximal rod CLASSIFICATION #superfamily rod protein flgF KEYWORDS basal body; flagellum SUMMARY #length 251 #molecular-weight 26102 #checksum 4905 SEQUENCE /// ENTRY XMEBFG #type complete TITLE flagellar basal body rod protein flgG - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS S08174; S15356 REFERENCE S08171 !$#authors Homma, M.; Kutsukake, K.; Hasebe, M.; Iino, T.; Macnab, R.M. !$#journal J. Mol. Biol. (1990) 211:465-477 !$#title FlgB, FlgC, FlgF and FlgG. A family of structurally related !1proteins in the flagellar basal body of Salmonella !1typhimurium. !$#cross-references MUID:90172414; PMID:2129540 !$#accession S08174 !'##molecule_type DNA !'##residues 1-260 ##label HOM !'##cross-references EMBL:X52094; NID:g47674; PIDN:CAA36314.1; !1PID:g47677 REFERENCE S15353 !$#authors Jones, C.J.; Macnab, R.M.; Okino, H.; Aizawa, S.I. !$#journal J. Mol. Biol. (1990) 212:377-387 !$#title Stoichiometric analysis of the flagellar hook-(basal-body) !1complex of Salmonella typhimurium. !$#cross-references MUID:90204563; PMID:2181149 !$#accession S15356 !'##molecule_type protein !'##residues 1-5 ##label JON GENETICS !$#gene flgG FUNCTION !$#description located in the distal rod CLASSIFICATION #superfamily rod protein flgF KEYWORDS basal body; flagellum SUMMARY #length 260 #molecular-weight 27770 #checksum 1514 SEQUENCE /// ENTRY A43824 #type complete TITLE periplasmic flagellar sheath protein precursor - Treponema hyodysenteriae ORGANISM #formal_name Treponema hyodysenteriae DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS A43824 REFERENCE A43824 !$#authors Koopman, M.B.; de Leeuw, O.S.; van der Zeijst, B.M.; !1Kusters, J.G. !$#journal Infect. Immun. (1992) 60:2920-2925 !$#title Cloning and DNA sequence analysis of a Serpulina (Treponema) !1hyodysenteriae gene encoding a periplasmic flagellar sheath !1protein. !$#cross-references MUID:92307926; PMID:1612759 !$#accession A43824 !'##molecule_type DNA !'##residues 1-320 ##label KOO !'##cross-references EMBL:X63006; NID:g433523; PIDN:CAA44735.1; !1PID:g433524 COMMENT The flagella of this spirochete are reported to be enclosed !1completely within the outer envelope. The organism causes !1swine dysentery. GENETICS !$#gene flaA CLASSIFICATION #superfamily spirochete flagellar sheath protein KEYWORDS flagellum; periplasmic space FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-320 #product periplasmic flagellar sheath protein #status !8experimental #label MAT SUMMARY #length 320 #molecular-weight 35986 #checksum 9966 SEQUENCE /// ENTRY QRECL #type complete TITLE lambda receptor protein precursor - Escherichia coli (strain K-12) ALTERNATE_NAMES lamB protein precursor; maltoporin precursor ORGANISM #formal_name Escherichia coli DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 01-Mar-2002 ACCESSIONS A03443; A29462; A27738; I51944; I41095; C65211 REFERENCE A03443 !$#authors Clement, J.M.; Hofnung, M. !$#journal Cell (1981) 27:507-514 !$#title Gene sequence of the lambda receptor, an outer membrane !1protein of E. coli K12. !$#cross-references MUID:93358323; PMID:6086106 !$#accession A03443 !'##molecule_type DNA !'##residues 1-446 ##label CLE !'##cross-references GB:V00298; NID:g41907; PIDN:CAA23575.1; PID:g41908 !'##experimental_source strain K12 REFERENCE A29462 !$#authors Heine, H.G.; Kyngdon, J.; Ferenci, T. !$#journal Gene (1987) 53:287-292 !$#title Sequence determinants in the lamB gene of Escherichia coli !1influencing the binding and pore selectivity of maltoporin. !$#cross-references MUID:87277420; PMID:3301537 !$#accession A29462 !'##molecule_type DNA !'##residues 1-156 ##label HE1 !'##cross-references GB:M16643; NID:g146589; PIDN:AAA24059.1; !1PID:g551815 REFERENCE A27738 !$#authors Heine, H.G.; Francis, G.; Lee, K.S.; Ferenci, T. !$#journal J. Bacteriol. (1988) 170:1730-1738 !$#title Genetic analysis of sequences in maltoporin that contribute !1to binding domains and pore structure. !$#cross-references MUID:88169498; PMID:2832377 !$#contents mutant plasmid pAM117 !$#accession A27738 !'##molecule_type DNA !'##residues 26-35,'SG',36-208,'DP',209-385,'DP',386-446 ##label HE2 REFERENCE I51944 !$#authors Clement, J. !$#journal Ann. Inst. Pasteur Microbiol. (1982) 133:9-20 !$#title A system for genetic analysis in gene lamB: First results !1with lambda-resistant tight mutants. !$#accession I51944 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-446 ##label RES !'##cross-references GB:M26131; NID:g146593; PIDN:AAA24060.1; !1PID:g146594 REFERENCE I41095 !$#authors Hedgpeth, J.; Clement, J.M.; Marchal, C.; Perrin, D.; !1Hofnung, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1980) 77:2621-2625 !$#title DNA sequence encoding the NH2-terminal peptide involved in !1transport of lambda receptor, an Escherichia coli secretory !1protein. !$#cross-references MUID:80234675; PMID:6446717 !$#accession I41095 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-35 ##label RE2 !'##cross-references EMBL:V00297; NID:g41905; PIDN:CAA23574.1; !1PID:g41906 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65211 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-446 ##label BLAT !'##cross-references GB:AE000477; GB:U00096; NID:g2367338; !1PIDN:AAC77006.1; PID:g1790469; UWGP:b4036 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene lamB !$#map_position 92 min FUNCTION !$#description acts as a receptor for several bacteriophages, including !1lambda and TP1, and is also involved in the transport of !1maltose and maltodextrins; it belongs to a family of major !1outer membrane proteins, porins, which play the role of !1hydrophilic pores CLASSIFICATION #superfamily lambda receptor protein KEYWORDS membrane protein; receptor FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-446 #product lambda receptor protein #status predicted !8#label MAT SUMMARY #length 446 #molecular-weight 49912 #checksum 9452 SEQUENCE /// ENTRY TKMYT #type complete TITLE tuberculin-active protein - Mycobacterium tuberculosis (strain Aoyama/B) ORGANISM #formal_name Mycobacterium tuberculosis DATE 22-Jun-1981 #sequence_revision 22-Jun-1981 #text_change 21-Nov-1998 ACCESSIONS A03444 REFERENCE A03444 !$#authors Kuwabara, S. !$#journal J. Biol. Chem. (1975) 250:2563-2568 !$#title Amino acid sequence of tuberculin-active protein from !1Mycobacterium tuberculosis. !$#cross-references MUID:75133468; PMID:804477 !$#accession A03444 !'##molecule_type protein !'##residues 1-89 ##label KUW !'##experimental_source human type Aoyama/B strain COMMENT Tuberculin is the soluble protein produced by the bacterium !1to which infected animals become hypersensitive and react !1characteristically after dermal injections. COMMENT This protein is the most potent component with tuberculin !1activity so far purified and characterized. CLASSIFICATION #superfamily tuberculin-active protein FEATURE !$27-59 #disulfide_bonds #status experimental SUMMARY #length 89 #molecular-weight 9493 #checksum 2606 SEQUENCE /// ENTRY YXDOTC #type complete TITLE thymidylate synthase-complementing protein - slime mold (Dictyostelium discoideum) ORGANISM #formal_name Dictyostelium discoideum DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS A33987 REFERENCE A33987 !$#authors Dynes, J.L.; Firtel, R.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:7966-7970 !$#title Molecular complementation of a genetic marker in !1Dictyostelium using a genomic DNA library. !$#cross-references MUID:90046718; PMID:2813371 !$#accession A33987 !'##molecule_type DNA !'##residues 1-260 ##label DYN !'##cross-references GB:M27713; NID:g167912; PIDN:AAA33257.1; !1PID:g167913 COMMENT This protein complements the thymidine growth requirement of !1Dictyostelium strain HPS400, which lacks thymidylate !1synthase activity and requires exogenous thymidylate for !1growth. GENETICS !$#gene thy1 CLASSIFICATION #superfamily thymidylate synthase-complementing protein SUMMARY #length 260 #molecular-weight 30422 #checksum 5503 SEQUENCE /// ENTRY IMBKBB #type complete TITLE immunogenic protein BCSP31 precursor - Brucella abortus ORGANISM #formal_name Brucella abortus DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jul-1999 ACCESSIONS JT0279 REFERENCE JT0279 !$#authors Mayfield, J.E.; Bricker, B.J.; Godfrey, H.; Crosby, R.M.; !1Knight, D.J.; Halling, S.M.; Balinsky, D.; Tabatabai, L.B. !$#journal Gene (1988) 63:1-9 !$#title The cloning, expression, and nucleotide sequence of a gene !1coding for an immunogenic Brucella abortus protein. !$#cross-references MUID:88255848; PMID:3133283 !$#accession JT0279 !'##molecule_type mRNA !'##residues 1-329 ##label MAY !'##cross-references GB:M20404; NID:g144104; PIDN:AAA22993.1; !1PID:g144105 COMMENT Brucella abortus is the causative agent for brucellosis in !1cattle and man. CLASSIFICATION #superfamily immunogenic protein BCSP31 FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-329 #product immunogenic protein BCSP31 #status predicted !8#label MAT SUMMARY #length 329 #molecular-weight 34273 #checksum 410 SEQUENCE /// ENTRY SVXC #type complete TITLE gas-vesicle protein - Calothrix sp. (strain PCC 7601) ORGANISM #formal_name Calothrix sp. #note Calothrix sp. is a filamentous cyanobacterium DATE 31-Mar-1988 #sequence_revision 12-Apr-1996 #text_change 16-Jun-2000 ACCESSIONS A27475; A24276; B23851 REFERENCE A91577 !$#authors Damerval, T.; Houmard, J.; Guglielmi, G.; Csiszar, K.; !1Tandeau de Marsac, N. !$#journal Gene (1987) 54:83-92 !$#title A developmentally regulated gvpABC operon is involved in the !1formation of gas vesicles in the cyanobacterium Calothrix !17601. !$#cross-references MUID:87277436; PMID:3111941 !$#accession A27475 !'##molecule_type DNA !'##residues 1-71 ##label DAM !'##cross-references GB:X06085; GB:M16733; GB:X03101; NID:g43391; !1PIDN:CAA29467.1; PID:g43392 !'##experimental_source PCC 7601 !'##note the proteins encoded by the structural genes gvpB and gvpA are !1identical REFERENCE A93594 !$#authors de Marsac, N.T.; Mazel, D.; Bryant, D.A.; Houmard, J. !$#journal Nucleic Acids Res. (1985) 13:7223-7236 !$#title Molecular cloning and nucleotide sequence of a !1developmentally regulated gene from the cyanobacterium !1Calothrix PCC 7601: a gas vesicle protein gene. !$#cross-references MUID:86041911; PMID:2997744 !$#accession A24276 !'##molecule_type DNA !'##residues 2-71 ##label DEM !'##cross-references GB:X06085; GB:M16733; GB:X03101; NID:g43391; !1PIDN:CAA29467.1; PID:g43392 !'##note initiator Met not shown REFERENCE A90331 !$#authors Hayes, P.K.; Walsby, A.E.; Walker, J.E. !$#journal Biochem. J. (1986) 236:31-36 !$#title Complete amino acid sequence of cyanobacterial gas-vesicle !1protein indicates a 70-residue molecule that corresponds in !1size to the crystallographic unit cell. !$#cross-references MUID:87075623; PMID:3098234 !$#accession B23851 !'##molecule_type protein !'##residues 2-58 ##label HAY !'##note 27-Asn was also found !'##note the cyanobacterium gets its buoyancy from hollow cylindrical !1structures called gas vesicles; the membrane of the vesicle !1is composed of a single kind of protein, the gas vesicle !1protein, which is present as a trimer GENETICS !$#gene gvpB; gvpA COMPLEX homotrimer CLASSIFICATION #superfamily gas-vesicle protein KEYWORDS structural protein SUMMARY #length 71 #molecular-weight 7515 #checksum 5213 SEQUENCE /// ENTRY SVIA #type complete TITLE gas-vesicle protein - Microcystis sp. ALTERNATE_NAMES GVP ORGANISM #formal_name Microcystis sp. DATE 31-Mar-1988 #sequence_revision 31-Dec-1988 #text_change 30-Jun-1993 ACCESSIONS C23851 REFERENCE A90331 !$#authors Hayes, P.K.; Walsby, A.E.; Walker, J.E. !$#journal Biochem. J. (1986) 236:31-36 !$#title Complete amino acid sequence of cyanobacterial gas-vesicle !1protein indicates a 70-residue molecule that corresponds in !1size to the crystallographic unit cell. !$#cross-references MUID:87075623; PMID:3098234 !$#contents BC 84/1 !$#accession C23851 !'##molecule_type protein !'##residues 1-70 ##label HAY COMMENT Microcystis sp. is a cyanobacterium. CLASSIFICATION #superfamily gas-vesicle protein KEYWORDS structural protein SUMMARY #length 70 #molecular-weight 7442 #checksum 3560 SEQUENCE /// ENTRY SVFZ #type complete TITLE gas-vesicle protein - Aphanizomenon flos-aquae ALTERNATE_NAMES GVP ORGANISM #formal_name Aphanizomenon flos-aquae DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 17-Feb-1995 ACCESSIONS A23851 REFERENCE A90331 !$#authors Hayes, P.K.; Walsby, A.E.; Walker, J.E. !$#journal Biochem. J. (1986) 236:31-36 !$#title Complete amino acid sequence of cyanobacterial gas-vesicle !1protein indicates a 70-residue molecule that corresponds in !1size to the crystallographic unit cell. !$#cross-references MUID:87075623; PMID:3098234 !$#note Anabaena flos-aquae !$#accession A23851 !'##molecule_type protein !'##residues 1-70 ##label HAY !'##experimental_source strain 1403/13f CLASSIFICATION #superfamily gas-vesicle protein KEYWORDS structural protein SUMMARY #length 70 #molecular-weight 7396 #checksum 3581 SEQUENCE /// ENTRY RAHSB #type complete TITLE bacteriorhodopsin precursor - Halobacterium salinarum ORGANISM #formal_name Halobacterium salinarum DATE 28-Feb-1980 #sequence_revision 18-Aug-1982 #text_change 21-Jul-2000 ACCESSIONS A93898; A90724; A93836; S35730; A03445 REFERENCE A93898 !$#authors Dunn, R.; McCoy, J.; Simsek, M.; Majumdar, A.; Chang, S.H.; !1RajBhandary, U.L.; Khorana, H.G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:6744-6748 !$#title The bacteriorhodopsin gene. !$#accession A93898 !'##molecule_type DNA !'##residues 1-262 ##label DUN !'##experimental_source strain S9 !'##note the source is designated as Halobacterium halobium REFERENCE A90724 !$#authors Ovchinnikov, Y.A.; Abdulaev, N.G.; Feigina, M.Y.; Kiselev, !1A.V.; Lobanov, N.A.; Nasimov, I.V. !$#journal Bioorg. Khim. (1978) 4:1573-1574 !$#accession A90724 !'##molecule_type protein !'##residues 14-117,'E',119-123,'I',125-129,'L',131-150,152-158,'S', !1160-218,'A',220-261 ##label OVC !'##note the source is designated as Halobacterium halobium REFERENCE A93836 !$#authors Khorana, H.G.; Gerber, G.E.; Herlihy, W.C.; Gray, C.P.; !1Anderegg, R.J.; Nihei, K.; Biemann, K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1979) 76:5046-5050 !$#title Amino acid sequence of bacteriorhodopsin. !$#cross-references MUID:80056631; PMID:291920 !$#accession A93836 !'##molecule_type protein !'##residues 14-261 ##label KHO !'##note the source is designated as Halobacterium halobium !'##note the amidation states of residues at positions 128 and 174 were !1not determined REFERENCE A93877 !$#authors Katre, N.V.; Wolber, P.K.; Stoeckenius, W.; Stroud, R.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:4068-4072 !$#title Attachment site(s) of retinal in bacteriorhodopsin. !$#cross-references MUID:82037784; PMID:6794028 !$#contents annotation; retinal-binding site REFERENCE S29987 !$#authors Soppa, J.A. !$#submission submitted to the EMBL Data Library, February 1993 !$#accession S35730 !'##molecule_type DNA !'##residues 1-262 ##label SOP !'##cross-references EMBL:X70293; NID:g43642; PIDN:CAA49774.1; !1PID:g43643 !'##note the source is designated as Halobacterium CLASSIFICATION #superfamily bacteriorhodopsin KEYWORDS chromoprotein; photoreceptor; pyroglutamic acid; retinal; !1transmembrane protein FEATURE !$1-13 #domain signal sequence #status predicted #label SIG\ !$14-262 #product bacteriorhodopsin #status experimental !8#label MAT\ !$14 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$229 #binding_site retinal (Lys) (covalent) #status !8experimental SUMMARY #length 262 #molecular-weight 28256 #checksum 1212 SEQUENCE /// ENTRY A26161 #type complete TITLE halorhodopsin precursor [validated] - Halobacterium salinarum ORGANISM #formal_name Halobacterium salinarum DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 21-Jul-2000 ACCESSIONS A26161 REFERENCE A26161 !$#authors Blanck, A.; Oesterhelt, D. !$#journal EMBO J. (1987) 6:265-273 !$#title The halo-opsin gene. II. Sequence, primary structure of !1halorhodopsin and comparison with bacteriorhodopsin. !$#accession A26161 !'##molecule_type DNA !'##residues 1-274 ##label BLA !'##experimental_source strain L-33 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing !'##note the source is designated as Halobacterium halobium GENETICS !$#gene hop FUNCTION !$#description light-driven chloride pump; chloride is pumped into the cell !1[validated, MUID:93239699] CLASSIFICATION #superfamily bacteriorhodopsin KEYWORDS chromoprotein; photoreceptor; retinal; transmembrane protein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-274 #product halorhodopsin #status experimental #label !8MAT\ !$28-51 #domain transmembrane #status predicted #label TM1\ !$63-86 #domain transmembrane #status predicted #label TM2\ !$104-127 #domain transmembrane #status predicted #label TM3\ !$133-156 #domain transmembrane #status predicted #label TM4\ !$160-184 #domain transmembrane #status predicted #label TM5\ !$193-216 #domain transmembrane #status predicted #label TM6\ !$229-252 #domain transmembrane #status predicted #label TM7\ !$253-274 #domain intracellular #status predicted #label INT\ !$242 #binding_site retinal (Lys) (covalent) #status !8predicted SUMMARY #length 274 #molecular-weight 28874 #checksum 8629 SEQUENCE /// ENTRY S09277 #type complete TITLE sensory rhodopsin I [validated] - Halobacterium salinarum ORGANISM #formal_name Halobacterium salinarum DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 21-Jul-2000 ACCESSIONS S09277; S27219; B47190 REFERENCE S09277 !$#authors Blanck, A.; Oesterhelt, D.; Ferrando, E.; Schegk, E.S.; !1Lottspeich, F. !$#journal EMBO J. (1989) 8:3963-3971 !$#title Primary structure of sensory rhodopsin I, a prokaryotic !1photoreceptor. !$#cross-references MUID:90076116; PMID:2591367 !$#accession S09277 !'##molecule_type DNA !'##residues 1-239 ##label BLA !'##cross-references EMBL:X51682 !'##experimental_source strain L33 !'##note the source is designated as Halobacterium halobium !$#accession S27219 !'##molecule_type protein !'##residues 1-35 ##label BL2 !'##experimental_source strain flx3 REFERENCE A47190 !$#authors Yao, V.J.; Spudich, J.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:11915-11919 !$#title Primary structure of an archaebacterial transducer, a !1methyl-accepting protein associated with sensory rhodopsin !1I. !$#cross-references MUID:93101637; PMID:1465418 !$#accession B47190 !'##molecule_type DNA !'##residues 1-239 ##label YAO !'##cross-references GB:L05603; NID:g305351; PID:g305353 !'##experimental_source strain Flx5R !'##note sequence extracted from NCBI backbone (NCBIN:120670, !1NCBIP:120672) !'##note the source is designated as Halobacterium halobium GENETICS !$#gene sopI FUNCTION !$#description phototaxis; photoreceptor SR-I mediates the photophilic !1response to orange light [validated, MUID:90076116] CLASSIFICATION #superfamily bacteriorhodopsin KEYWORDS chromoprotein; photoreceptor; phototaxis; retinal; !1transmembrane protein FEATURE !$1-238 #product sensory rhodopsin I #status experimental !8#label MAT\ !$3-26 #domain transmembrane #status predicted #label TM1\ !$38-59 #domain transmembrane #status predicted #label TM2\ !$69-91 #domain transmembrane #status predicted #label TM3\ !$101-119 #domain transmembrane #status predicted #label TM4\ !$124-147 #domain transmembrane #status predicted #label TM5\ !$157-181 #domain transmembrane #status predicted #label TM6\ !$193-214 #domain transmembrane #status predicted #label TM7\ !$205 #binding_site retinal (Lys) (covalent) #status !8predicted SUMMARY #length 239 #molecular-weight 25501 #checksum 1266 SEQUENCE /// ENTRY T44947 #type complete TITLE sensory rhodopsin II [validated] - Halobacterium salinarum ALTERNATE_NAMES phoborhodopsin ORGANISM #formal_name Halobacterium salinarum DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 21-Jul-2000 ACCESSIONS T44947 REFERENCE Z22877 !$#authors Zhang, W.; Brooun, A.; Mueller, M.M.; Alam, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1996) 93:8230-8235 !$#title The primary structures in the Archaeon Halobacterium !1salinarium blue light receptor sensory rhodopsin II and its !1transducer, a methyl-accepting protein. !$#cross-references MUID:96323203; PMID:8710852 !$#accession T44947 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-237 ##label ZHA !'##cross-references EMBL:U62676; PIDN:AAC44370.1 !'##experimental_source strain Flx15 !'##note the source is designated as Halobacterium salinarium GENETICS !$#gene sopII FUNCTION !$#description phototaxis; photoreceptor SR-II mediates the photophobic !1response to blue light [validated, MUID:96323203] CLASSIFICATION #superfamily bacteriorhodopsin KEYWORDS chromoprotein; photoreceptor; phototaxis; retinal; !1transmembrane protein FEATURE !$202 #binding_site retinal (Lys) (covalent) #status !8predicted SUMMARY #length 237 #molecular-weight 25279 #checksum 4389 SEQUENCE /// ENTRY A47190 #type complete TITLE transducer protein htrI [validated] - Halobacterium salinarum ALTERNATE_NAMES methyl-accepting transducer protein htrI; transducer protein htp1 ORGANISM #formal_name Halobacterium salinarum DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 19-Jan-2001 ACCESSIONS A47190; S28466 REFERENCE A47190 !$#authors Yao, V.J.; Spudich, J.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:11915-11919 !$#title Primary structure of an archaebacterial transducer, a !1methyl-accepting protein associated with sensory rhodopsin !1I. !$#cross-references MUID:93101637; PMID:1465418 !$#accession A47190 !'##status preliminary !'##molecule_type DNA; protein !'##residues 1-536 ##label YAO !'##cross-references GB:L05603; NID:g305351; PID:g305352 !'##experimental_source strain Flx5R !'##note sequence inconsistent with the nucleotide translation !'##note sequence extracted from NCBI backbone (NCBIN:120670, !1NCBIP:120671) !'##note the source is designated as Halobacterium halobium REFERENCE S28466 !$#authors Ferrando, E.; Krah, M.; Marwan, W.; Oesterhelt, D. !$#submission submitted to the EMBL Data Library, October 1992 !$#description Halobacterial phototaxis requires a gene with homology to !1eubacterial chemoreceptor genes. !$#accession S28466 !'##molecule_type DNA !'##residues 1-33,'E',35-54,'G',56-58,'GR',61-64,'G',66-113,'S',115-120, !1'T',122,'S',124-125,'T',127-129,'S',131-138,'S',140-153, !1'SSN',157,'D',159-163,'SS',166-169,'F',171-179,'P',181-185, !1'F',187-242,'P',244-308,'P',310-314,'H',316-400,'H',402-417, !1'LH',420-427,'S',429-474,'P',476-536 ##label FER !'##cross-references EMBL:X68591; NID:g2648027; PIDN:CAA48578.1; !1PID:g2648028 !'##experimental_source strain L33 !'##note the source is designated as Halobacterium salinarium GENETICS !$#gene htrI; htp1 FUNCTION !$#description involved in phototactic signal transduction from sensory !1rhodopsin I (PIR:S09277) [validated, MUID:93345444] !$#note the adaptation response is mediated by methylation of the !1transducer protein CLASSIFICATION #superfamily Halobacterium salinarum transducer protein htrI KEYWORDS methylated amino acid; signal transduction; transmembrane !1protein FEATURE !$232-486 #region MCP signalling domain similarity SUMMARY #length 536 #molecular-weight 56675 #checksum 4205 SEQUENCE /// ENTRY T44946 #type complete TITLE transducer protein htrII [validated] - Halobacterium salinarum ALTERNATE_NAMES methyl-accepting taxis protein htrII; transducer protein htp2 ORGANISM #formal_name Halobacterium salinarum DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 18-Aug-2000 ACCESSIONS T44946 REFERENCE Z22877 !$#authors Zhang, W.; Brooun, A.; Mueller, M.M.; Alam, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1996) 93:8230-8235 !$#title The primary structures in the Archaeon Halobacterium !1salinarium blue light receptor sensory rhodopsin II and its !1transducer, a methyl-accepting protein. !$#cross-references MUID:96323203; PMID:8710852 !$#accession T44946 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-765 ##label ZHA !'##cross-references EMBL:U62676; PIDN:AAC44369.1 !'##experimental_source strain Flx15 !'##note the source is designated as Halobacterium salinarium GENETICS !$#gene htrII; htp2 FUNCTION !$#description involved in phototactic signal transduction from sensory !1rhodopsin II (PIR:T44947) [validated, MUID:96323203] !$#note the adaptation response is mediated by methylation of the !1transducer protein CLASSIFICATION #superfamily Halobacterium salinarum transducer protein !1htrII KEYWORDS methylated amino acid; signal transduction; transmembrane !1protein FEATURE !$481-733 #region MCP signalling domain similarity SUMMARY #length 765 #molecular-weight 79318 #checksum 4493 SEQUENCE /// ENTRY T44253 #type complete TITLE transducer protein htrVIII [validated] - Halobacterium salinarum ALTERNATE_NAMES methyl-accepting aerotaxis transducer protein htrVIII; transducer protein htK; transducer protein htp8 ORGANISM #formal_name Halobacterium salinarum DATE 03-Nov-2000 #sequence_revision 03-Nov-2000 #text_change 03-Nov-2000 ACCESSIONS T44253 REFERENCE Z22736 !$#authors Brooun, A.; Bell, J.; Freitas, T.; Larsen, R.W.; Alam, M. !$#journal J. Bacteriol. (1998) 180:1642-1646 !$#title An archaeal aerotaxis transducer combines subunit I core !1structures of eukaryotic cytochrome c oxidase and !1eubacterial methyl-accepting chemotaxis proteins. !$#cross-references MUID:98196704; PMID:9537358 !$#accession T44253 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-642 ##label BRO !'##cross-references EMBL:AF031641; NID:g3015618; PIDN:AAC38313.1; !1PID:g3015619 !'##note the source is designated as Halobacterium salinarium GENETICS !$#gene htrVIII; htp8; htK FUNCTION !$#description involved in aerotactic signal transduction; involved in !1oxygen sensing; mediates the aerophilic response !$#note methyl-accepting protein which demethylates during the !1aerotaxis response CLASSIFICATION #superfamily Halobacterium salinarum transducer protein !1htrVIII KEYWORDS methylated amino acid; signal transduction; transmembrane !1protein SUMMARY #length 642 #molecular-weight 67101 #checksum 9916 SEQUENCE /// ENTRY LBRFAV #type complete TITLE light-harvesting complex protein alpha chain - Rhodopseudomonas viridis ORGANISM #formal_name Rhodopseudomonas viridis DATE 04-Dec-1986 #sequence_revision 12-Apr-1996 #text_change 16-Jul-1999 ACCESSIONS C35382; A03448 REFERENCE A35382 !$#authors Wiessner, C.; Dunger, I.; Michel, H. !$#journal J. Bacteriol. (1990) 172:2877-2887 !$#title Structure and transcription of the genes encoding the B1015 !1light-harvesting complex beta and alpha subunits and the !1photosynthetic reaction center L, M, and cytochrome c !1subunits from Rhodopseudomonas viridis. !$#cross-references MUID:90264272; PMID:1693143 !$#accession C35382 !'##status preliminary !'##molecule_type DNA !'##residues 1-69 ##label WIE !'##cross-references GB:M55261; NID:g151878; PIDN:AAA64256.1; !1PID:g151881 REFERENCE A90694 !$#authors Brunisholz, R.A.; Jay, F.; Suter, F.; Zuber, H. !$#journal Biol. Chem. Hoppe-Seyler (1985) 366:87-98 !$#title The light-harvesting polypeptides of Rhodopseudomonas !1viridis. The complete amino-acid sequences of B1015-alpha, !1B1015-beta and B1015-gamma. !$#cross-references MUID:85225948; PMID:3890891 !$#accession A03448 !'##molecule_type protein !'##residues 2-59 ##label BRU CLASSIFICATION #superfamily light-harvesting protein alpha chain KEYWORDS bacteriochlorophyll; light-harvesting polypeptide; !1magnesium; membrane protein FEATURE !$37 #binding_site bacteriochlorophyll magnesium (His) !8(axial ligand) #status predicted SUMMARY #length 69 #molecular-weight 7895 #checksum 3762 SEQUENCE /// ENTRY LBRF2S #type complete TITLE light-harvesting protein B-800/850 alpha chain - Rhodobacter sphaeroides ALTERNATE_NAMES antenna pigment protein, alpha chain; B-800/850 alpha; LH-2 ORGANISM #formal_name Rhodobacter sphaeroides DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 24-Feb-1995 ACCESSIONS A03446 REFERENCE A91736 !$#authors Theiler, R.; Suter, F.; Wiemken, V.; Zuber, H. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1984) 365:703-719 !$#title The light-harvesting polypeptides of Rhodopseudomonas !1sphaeroides R-26.1: I. Isolation, purification and sequence !1analyses. !$#cross-references MUID:85005243; PMID:6384009 !$#contents mutant R-26.1 !$#accession A03446 !'##molecule_type protein !'##residues 1-54 ##label THE COMMENT This polypeptide (LH-2) and LH-3b constitute the B-800/850 !1complex of R. sphaeroides 2.4.1 and the spectrally altered !1B-850 complex isolated from the blue-green mutant R-26.1, !1which absorbs at 860 nm. CLASSIFICATION #superfamily light-harvesting protein alpha chain KEYWORDS antenna complex; bacteriochlorophyll; light-harvesting !1polypeptide; magnesium; membrane protein FEATURE !$31 #binding_site bacteriochlorophyll magnesium (His) !8(axial ligand) #status predicted SUMMARY #length 54 #molecular-weight 5647 #checksum 3455 SEQUENCE /// ENTRY LBQFR #type complete TITLE light-harvesting protein B-880 alpha chain - Rhodospirillum rubrum ALTERNATE_NAMES antenna pigment protein, alpha chain; B-870 alpha; LH-1 ORGANISM #formal_name Rhodospirillum rubrum DATE 01-Sep-1981 #sequence_revision 12-Apr-1996 #text_change 24-Nov-1999 ACCESSIONS B24206; A03447 REFERENCE A92590 !$#authors Berard, J.; Belanger, G.; Corriveau, P.; Gingras, G. !$#journal J. Biol. Chem. (1986) 261:82-87 !$#title Molecular cloning and sequence of the B880 holochrome gene !1from Rhodospirillum rubrum. !$#cross-references MUID:86085865; PMID:3001063 !$#accession B24206 !'##molecule_type DNA !'##residues 1-62 ##label BER !'##cross-references GB:M11801; NID:g152606; PIDN:AAA26462.1; !1PID:g152608 REFERENCE A03447 !$#authors Brunisholz, R.A.; Cuendet, P.A.; Theiler, R.; Zuber, H. !$#journal FEBS Lett. (1981) 129:150-154 !$#title The complete amino acid sequence of the single light !1harvesting protein from chromatophores of Rhodospirillum !1rubrum G9(+). !$#accession A03447 !'##molecule_type protein !'##residues 1-52 ##label BRU !'##experimental_source strain G-9+ FUNCTION !$#description this protein is one of the components of the !1bacteriochlorophyll-protein complex in the chromatophore !1membrane CLASSIFICATION #superfamily light-harvesting protein alpha chain KEYWORDS antenna complex; bacteriochlorophyll; blocked amino end; !1light-harvesting polypeptide; magnesium; membrane protein FEATURE !$1 #modified_site blocked amino end (Met) (probably !8formylated) #status experimental\ !$29 #binding_site bacteriochlorophyll magnesium (His) !8(axial ligand) #status predicted SUMMARY #length 62 #molecular-weight 7107 #checksum 9432 SEQUENCE /// ENTRY LBRFAC #type complete TITLE light-harvesting protein B-870 alpha chain - Rhodobacter capsulatus ALTERNATE_NAMES antenna pigment protein, alpha chain; B-870 alpha; LH-1 ORGANISM #formal_name Rhodobacter capsulatus DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 04-Dec-1994 ACCESSIONS A03449; E28771; A24094 REFERENCE A93988 !$#authors Youvan, D.C.; Alberti, M.; Begusch, H.; Bylina, E.J.; !1Hearst, J.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:189-192 !$#title Reaction center and light-harvesting I genes from !1Rhodopseudomonas capsulata. !$#accession A03449 !'##molecule_type DNA !'##residues 1-58 ##label YOU REFERENCE A90850 !$#authors Youvan, D.C.; Bylina, E.J.; Alberti, M.; Begusch, H.; !1Hearst, J.E. !$#journal Cell (1984) 37:949-957 !$#title Nucleotide and deduced polypeptide sequences of the !1photosynthetic reaction-center, B870 antenna, and flanking !1polypeptides from R. capsulata. !$#cross-references MUID:84259352; PMID:6744416 !$#accession E28771 !'##molecule_type DNA !'##residues 1-58 ##label YO2 !'##cross-references GB:K01183 REFERENCE A24094 !$#authors Tadros, M.H.; Frank, G.; Zuber, H.; Drews, G. !$#journal FEBS Lett. (1985) 190:41-44 !$#title The complete amino acid sequence of the large !1bacteriochlorophyll-binding polypeptide B870-alpha from the !1light-harvesting complex B870 of Rhodopseudomonas capsulata. !$#accession A24094 !'##molecule_type protein !'##residues 1-58 ##label TAD CLASSIFICATION #superfamily light-harvesting protein alpha chain KEYWORDS antenna complex; bacteriochlorophyll; light-harvesting !1polypeptide; magnesium; membrane protein FEATURE !$32 #binding_site bacteriochlorophyll magnesium (His) !8(axial ligand) #status predicted SUMMARY #length 58 #molecular-weight 6594 #checksum 5207 SEQUENCE /// ENTRY LBRF1S #type complete TITLE light-harvesting protein B-870 alpha chain [validated] - Rhodobacter sphaeroides ALTERNATE_NAMES antenna pigment protein, alpha chain; B-870 alpha; B-875 alpha; LH-1 ORGANISM #formal_name Rhodobacter sphaeroides DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 18-Aug-2000 ACCESSIONS A27760; A03450; T50759 REFERENCE A91860 !$#authors Kiley, P.J.; Donohue, T.J.; Havelka, W.A.; Kaplan, S. !$#journal J. Bacteriol. (1987) 169:742-750 !$#title DNA sequence and in vitro expression of the B875 !1light-harvesting polypeptides of Rhodobacter sphaeroides. !$#cross-references MUID:87109067; PMID:3027044 !$#accession A27760 !'##molecule_type DNA !'##residues 1-58 ##label KIL !'##cross-references GB:M15105; NID:g152003; PIDN:AAA26167.1; !1PID:g152005 REFERENCE A91736 !$#authors Theiler, R.; Suter, F.; Wiemken, V.; Zuber, H. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1984) 365:703-719 !$#title The light-harvesting polypeptides of Rhodopseudomonas !1sphaeroides R-26.1: I. Isolation, purification and sequence !1analyses. !$#cross-references MUID:85005243; PMID:6384009 !$#accession A03450 !'##molecule_type protein !'##residues 1-58 ##label THE REFERENCE Z25222 !$#authors Choudhary, M.; Kaplan, S. !$#journal Nucleic Acids Res. (2000) 28:862-867 !$#title DNA sequence analysis of the photosynthesis region of !1Rhodobacter sphaeroides 2.4.1. !$#cross-references MUID:20115911; PMID:10648776 !$#accession T50759 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-58 ##label CHO !'##cross-references EMBL:AF195122; PIDN:AAF24303.1 !'##experimental_source strain 2.4.1 COMMENT This polypeptide is part of a heterodimer (LH-1/LH-3A) in !1the B-870 antenna-pigment-protein complex of R. sphaeroides. GENETICS !$#gene pufA CLASSIFICATION #superfamily light-harvesting protein alpha chain KEYWORDS antenna complex; bacteriochlorophyll; light-harvesting !1polypeptide; magnesium; membrane protein FEATURE !$1 #modified_site N-formylmethionine #status !8experimental\ !$32 #binding_site bacteriochlorophyll magnesium (His) !8(axial ligand) #status predicted SUMMARY #length 58 #molecular-weight 6809 #checksum 7300 SEQUENCE /// ENTRY LBBCA #type complete TITLE light-harvesting protein B-870 alpha chain - Erythrobacter sp. (strain OCH114) ALTERNATE_NAMES B870 antenna polypeptide alpha ORGANISM #formal_name Erythrobacter sp. DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS S16311 REFERENCE S16309 !$#authors Liebetanz, R.; Hornberger, U.; Drews, G. !$#journal Mol. Microbiol. (1991) 5:1459-1468 !$#title Organization of the genes coding for the reaction-centre L !1and M subunits and B870 antenna polypeptides alpha and beta !1from the aerobic photosynthetic bacterium Erythrobacter !1species OCH114. !$#cross-references MUID:92157872; PMID:1787796 !$#accession S16311 !'##molecule_type DNA !'##residues 1-52 ##label LIE !'##cross-references EMBL:X57597; NID:g43356; PIDN:CAA40817.1; !1PID:g43358 GENETICS !$#gene pufA CLASSIFICATION #superfamily light-harvesting protein alpha chain KEYWORDS bacteriochlorophyll; light-harvesting complex; magnesium; !1membrane protein FEATURE !$32 #binding_site bacteriochlorophyll magnesium (His) !8(axial ligand) #status predicted SUMMARY #length 52 #molecular-weight 5814 #checksum 3175 SEQUENCE /// ENTRY LBRFA8 #type complete TITLE light-harvesting protein B-800/850 alpha chain - Rhodobacter capsulatus ALTERNATE_NAMES antenna pigment protein, alpha chain; B-800/850 alpha; LH-2 ORGANISM #formal_name Rhodobacter capsulatus DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 16-Jul-1999 ACCESSIONS B21901; B33958; A18974 REFERENCE A94058 !$#authors Youvan, D.C.; Ismail, S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:58-62 !$#title Light-harvesting II (B800-B850 complex) structural genes !1from Rhodopseudomonas capsulata. !$#accession B21901 !'##molecule_type DNA !'##residues 1-60 ##label YOU REFERENCE A33958 !$#authors Tichy, H.V.; Oberle, B.; Stiehle, H.; Schiltz, E.; Drews, G. !$#journal J. Bacteriol. (1989) 171:4914-4922 !$#title Genes downstream from pucB and pucA are essential for !1formation of the B800-850 complex of Rhodobacter capsulatus. !$#cross-references MUID:89359127; PMID:2549005 !$#accession B33958 !'##molecule_type DNA !'##residues 1-60 ##label TIC !'##cross-references GB:M28510; NID:g151997; PIDN:AAA26162.1; !1PID:g151999 REFERENCE A18974 !$#authors Tadros, M.H.; Suter, F.; Drews, G.; Zuber, H. !$#journal Eur. J. Biochem. (1983) 129:533-536 !$#title The complete amino-acid sequence of the large !1bacteriochlorophyll-binding polypeptide from !1light-harvesting complex II (B800-850) of Rhodopseudomonas !1capsulata. !$#cross-references MUID:83131599; PMID:6825670 !$#accession A18974 !'##molecule_type protein !'##residues 1-60 ##label TAD GENETICS !$#gene pucA CLASSIFICATION #superfamily light-harvesting protein alpha chain KEYWORDS antenna complex; bacteriochlorophyll; light-harvesting !1polypeptide; magnesium; membrane protein FEATURE !$31 #binding_site bacteriochlorophyll magnesium (His) !8(axial ligand) #status predicted SUMMARY #length 60 #molecular-weight 6259 #checksum 7657 SEQUENCE /// ENTRY LBRFBC #type complete TITLE light-harvesting protein B-870 beta chain - Rhodobacter capsulatus ALTERNATE_NAMES antenna pigment protein, beta chain; B-870 beta; LH-2 ORGANISM #formal_name Rhodobacter capsulatus DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 12-Apr-1996 ACCESSIONS A03451; D28771; A37850; S13783 REFERENCE A93988 !$#authors Youvan, D.C.; Alberti, M.; Begusch, H.; Bylina, E.J.; !1Hearst, J.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:189-192 !$#title Reaction center and light-harvesting I genes from !1Rhodopseudomonas capsulata. !$#accession A03451 !'##molecule_type DNA !'##residues 1-49 ##label YOU1 REFERENCE A90850 !$#authors Youvan, D.C.; Bylina, E.J.; Alberti, M.; Begusch, H.; !1Hearst, J.E. !$#journal Cell (1984) 37:949-957 !$#title Nucleotide and deduced polypeptide sequences of the !1photosynthetic reaction-center, B870 antenna, and flanking !1polypeptides from R. capsulata. !$#cross-references MUID:84259352; PMID:6744416 !$#accession D28771 !'##molecule_type DNA !'##residues 1-49 ##label YOU2 !'##cross-references GB:K01183 REFERENCE A37850 !$#authors Stiehle, H.; Cortez, N.; Klug, G.; Drews, G. !$#journal J. Bacteriol. (1990) 172:7131-7137 !$#title A negatively charged N terminus in the alpha polypeptide !1inhibits formation of light-harvesting complex I in !1Rhodobacter capsulatus. !$#cross-references MUID:91072268; PMID:2254277 !$#accession A37850 !'##status preliminary !'##molecule_type protein !'##residues 2-21 ##label STI REFERENCE S13783 !$#authors Tadros, M.H.; Suter, F.; Seydewitz, H.H.; Witt, I.; Zuber, !1H.; Drews, G. !$#journal Eur. J. Biochem. (1984) 138:209-212 !$#title Isolation and complete amino-acid sequence of the small !1polypeptide from light-harvesting pigment-protein complex I !1(B870) of Rhodopseudomonas capsulata. !$#cross-references MUID:84108384; PMID:6363069 !$#accession S13783 !'##status preliminary !'##molecule_type protein !'##residues 2-49 ##label TAD !'##note the source is designated as Rhodopseudomonas capsulata CLASSIFICATION #superfamily light-harvesting protein beta chain KEYWORDS antenna complex; bacteriochlorophyll; light-harvesting !1polypeptide; magnesium; membrane protein FEATURE !$39 #binding_site bacteriochlorophyll magnesium (His) !8(axial ligand) #status predicted SUMMARY #length 49 #molecular-weight 5466 #checksum 3107 SEQUENCE /// ENTRY LBRFAS #type complete TITLE light-harvesting protein B-870 beta chain [validated] - Rhodobacter sphaeroides ALTERNATE_NAMES antenna pigment protein, beta chain; B-870 beta; B-875 beta; LH-3A ORGANISM #formal_name Rhodobacter sphaeroides DATE 27-Nov-1985 #sequence_revision 31-Dec-1993 #text_change 18-Aug-2000 ACCESSIONS B27760; A03452; T50758 REFERENCE A91860 !$#authors Kiley, P.J.; Donohue, T.J.; Havelka, W.A.; Kaplan, S. !$#journal J. Bacteriol. (1987) 169:742-750 !$#title DNA sequence and in vitro expression of the B875 !1light-harvesting polypeptides of Rhodobacter sphaeroides. !$#cross-references MUID:87109067; PMID:3027044 !$#accession B27760 !'##molecule_type DNA !'##residues 1-49 ##label KIL !'##cross-references GB:M15105; NID:g152003; PIDN:AAA26166.1; !1PID:g152004 REFERENCE A91736 !$#authors Theiler, R.; Suter, F.; Wiemken, V.; Zuber, H. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1984) 365:703-719 !$#title The light-harvesting polypeptides of Rhodopseudomonas !1sphaeroides R-26.1: I. Isolation, purification and sequence !1analyses. !$#cross-references MUID:85005243; PMID:6384009 !$#contents mutant R-26.1 !$#accession A03452 !'##molecule_type protein !'##residues 2-29,'P',31-49 ##label THE REFERENCE Z25222 !$#authors Choudhary, M.; Kaplan, S. !$#journal Nucleic Acids Res. (2000) 28:862-867 !$#title DNA sequence analysis of the photosynthesis region of !1Rhodobacter sphaeroides 2.4.1. !$#cross-references MUID:20115911; PMID:10648776 !$#accession T50758 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-49 ##label CHO !'##cross-references EMBL:AF195122; PIDN:AAF24302.1 !'##experimental_source strain 2.4.1 COMMENT This polypeptide is part of a heterodimer (LH-1/LH-3A) in !1the B-870 antenna-pigment-protein complex of R. sphaeroides. COMMENT His-21, which is conserved only in the beta chain, is !1located close to an "acid cluster" at the beginning of the !1hydrophobic segment; its function is not yet clear. GENETICS !$#gene pufB CLASSIFICATION #superfamily light-harvesting protein beta chain KEYWORDS antenna complex; bacteriochlorophyll; light-harvesting !1polypeptide; magnesium; membrane protein FEATURE !$2-49 #product light-harvesting protein B-870 beta chain !8#status experimental #label MAT\ !$39 #binding_site bacteriochlorophyll magnesium (His) !8(axial ligand) #status predicted SUMMARY #length 49 #molecular-weight 5588 #checksum 4787 SEQUENCE /// ENTRY LBBCB #type complete TITLE light-harvesting protein B-870 beta chain - Erythrobacter sp. (strain OCH114) ALTERNATE_NAMES B870 antenna polypeptide beta ORGANISM #formal_name Erythrobacter sp. DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS S16309 REFERENCE S16309 !$#authors Liebetanz, R.; Hornberger, U.; Drews, G. !$#journal Mol. Microbiol. (1991) 5:1459-1468 !$#title Organization of the genes coding for the reaction-centre L !1and M subunits and B870 antenna polypeptides alpha and beta !1from the aerobic photosynthetic bacterium Erythrobacter !1species OCH114. !$#cross-references MUID:92157872; PMID:1787796 !$#accession S16309 !'##molecule_type DNA !'##residues 1-50 ##label LIE !'##cross-references EMBL:X57597; NID:g43356; PIDN:CAA40815.1; !1PID:g43357 GENETICS !$#gene pufB CLASSIFICATION #superfamily light-harvesting protein beta chain KEYWORDS bacteriochlorophyll; light-harvesting complex; magnesium; !1membrane protein FEATURE !$39 #binding_site bacteriochlorophyll magnesium (His) !8(axial ligand) #status predicted SUMMARY #length 50 #molecular-weight 5592 #checksum 7594 SEQUENCE /// ENTRY LBRFBV #type complete TITLE light-harvesting complex protein beta chain - Rhodopseudomonas viridis ORGANISM #formal_name Rhodopseudomonas viridis DATE 04-Dec-1986 #sequence_revision 12-Apr-1996 #text_change 16-Jul-1999 ACCESSIONS B35382; A03453 REFERENCE A35382 !$#authors Wiessner, C.; Dunger, I.; Michel, H. !$#journal J. Bacteriol. (1990) 172:2877-2887 !$#title Structure and transcription of the genes encoding the B1015 !1light-harvesting complex beta and alpha subunits and the !1photosynthetic reaction center L, M, and cytochrome c !1subunits from Rhodopseudomonas viridis. !$#cross-references MUID:90264272; PMID:1693143 !$#accession B35382 !'##status preliminary !'##molecule_type DNA !'##residues 1-69 ##label WIE !'##cross-references GB:M55261; NID:g151878; PIDN:AAA64255.1; !1PID:g151880 REFERENCE A90694 !$#authors Brunisholz, R.A.; Jay, F.; Suter, F.; Zuber, H. !$#journal Biol. Chem. Hoppe-Seyler (1985) 366:87-98 !$#title The light-harvesting polypeptides of Rhodopseudomonas !1viridis. The complete amino-acid sequences of B1015-alpha, !1B1015-beta and B1015-gamma. !$#cross-references MUID:85225948; PMID:3890891 !$#accession A03453 !'##molecule_type protein !'##residues 2-56 ##label BRU CLASSIFICATION #superfamily light-harvesting protein beta chain KEYWORDS antenna complex; bacteriochlorophyll; light-harvesting !1complex; magnesium; membrane protein FEATURE !$38 #binding_site bacteriochlorophyll magnesium (His) !8(axial ligand) #status predicted SUMMARY #length 69 #molecular-weight 7643 #checksum 5139 SEQUENCE /// ENTRY LBRFBS #type complete TITLE light-harvesting protein B-800/850 beta chain [validated] - Rhodobacter sphaeroides ALTERNATE_NAMES antenna pigment protein, beta chain; B-800/850 beta; LH-3B ORGANISM #formal_name Rhodobacter sphaeroides DATE 27-Nov-1985 #sequence_revision 12-Apr-1996 #text_change 18-Aug-2000 ACCESSIONS B27087; S28023; A45795; A03454; T50703 REFERENCE A91838 !$#authors Kiley, P.J.; Kaplan, S. !$#journal J. Bacteriol. (1987) 169:3268-3275 !$#title Cloning, DNA sequence, and expression of the Rhodobacter !1sphaeroides light-harvesting B800-850-alpha and !1B800-850-beta genes. !$#cross-references MUID:87250299; PMID:3036782 !$#accession B27087 !'##molecule_type DNA !'##residues 1-51 ##label KIL !'##cross-references GB:M16777; NID:g151994; PIDN:AAA26159.1; !1PID:g294664 REFERENCE S28023 !$#authors Gibson, L.C.D.; McGlynn, P.; Chaudhri, M.; Hunter, C.N. !$#journal Mol. Microbiol. (1992) 6:3171-3186 !$#title A putative anaerobic coproporphyrinogen III oxidase in !1Rhodobacter sphaeroides. II. Analysis of a region of the !1genome encoding hemF and the puc operon. !$#cross-references MUID:93086425; PMID:1453956 !$#accession S28023 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-51 ##label GIB !'##cross-references EMBL:X68796; NID:g46438; PIDN:CAA48699.1; !1PID:g581538 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1992 REFERENCE A45795 !$#authors Burgess, J.G.; Ashby, M.K.; Hunter, C.N. !$#journal J. Gen. Microbiol. (1989) 135:1809-1816 !$#title Characterization and complementation of a mutant of !1Rhodobacter sphaeroides with a chromosomal deletion in the !1light-harvesting (LH2) genes. !$#cross-references MUID:90132586; PMID:2693605 !$#accession A45795 !'##status preliminary !'##molecule_type DNA !'##residues 1-51 ##label BUR !'##cross-references GB:M28360; NID:g151958; PIDN:AAA26130.1; !1PID:g151959 REFERENCE A91736 !$#authors Theiler, R.; Suter, F.; Wiemken, V.; Zuber, H. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1984) 365:703-719 !$#title The light-harvesting polypeptides of Rhodopseudomonas !1sphaeroides R-26.1: I. Isolation, purification and sequence !1analyses. !$#cross-references MUID:85005243; PMID:6384009 !$#contents mutant R-26.1 !$#accession A03454 !'##molecule_type protein !'##residues 2-51 ##label THE REFERENCE Z25222 !$#authors Choudhary, M.; Kaplan, S. !$#journal Nucleic Acids Res. (2000) 28:862-867 !$#title DNA sequence analysis of the photosynthesis region of !1Rhodobacter sphaeroides 2.4.1. !$#cross-references MUID:20115911; PMID:10648776 !$#accession T50703 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-51 ##label CHO !'##cross-references EMBL:AF195122; PIDN:AAF24247.1 !'##experimental_source strain 2.4.1 GENETICS !$#gene pucB !$#start_codon GTG FUNCTION !$#description this polypeptide (LH-3B) and LH-2 constitute the B-800/850 !1complex of R. sphaeroides 2.4.1 and the spectrally altered !1B-850 complex isolated from the blue-green mutant R-26.1, !1which absorbs at 860 nm !$#note His-22, which is conserved only in the beta chain, is !1located close to an "acid cluster" at the beginning of the !1hydrophobic segment; its function is not yet clear CLASSIFICATION #superfamily light-harvesting protein beta chain KEYWORDS antenna complex; bacteriochlorophyll; blocked amino end; !1light-harvesting polypeptide; magnesium; membrane protein FEATURE !$2-51 #product light-harvesting protein B-800/850 beta !8chain #status experimental #label MAT\ !$2 #modified_site blocked amino end (Thr) (in mature !8form) #status experimental\ !$40 #binding_site bacteriochlorophyll magnesium (His) !8(axial ligand) #status predicted SUMMARY #length 51 #molecular-weight 5448 #checksum 8254 SEQUENCE /// ENTRY LBRF8C #type complete TITLE light-harvesting protein B-800/850 beta chain - Rhodobacter capsulatus ALTERNATE_NAMES antenna pigment protein, beta chain; B-800/850 beta; cytochrome b561; LH-3B ORGANISM #formal_name Rhodobacter capsulatus DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 16-Jul-1999 ACCESSIONS A21901; A33958; A22258; S34741 REFERENCE A94058 !$#authors Youvan, D.C.; Ismail, S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:58-62 !$#title Light-harvesting II (B800-B850 complex) structural genes !1from Rhodopseudomonas capsulata. !$#accession A21901 !'##molecule_type DNA !'##residues 1-49 ##label YOU REFERENCE A33958 !$#authors Tichy, H.V.; Oberle, B.; Stiehle, H.; Schiltz, E.; Drews, G. !$#journal J. Bacteriol. (1989) 171:4914-4922 !$#title Genes downstream from pucB and pucA are essential for !1formation of the B800-850 complex of Rhodobacter capsulatus. !$#cross-references MUID:89359127; PMID:2549005 !$#accession A33958 !'##molecule_type DNA !'##residues 1-49 ##label TIC !'##cross-references GB:M28510; NID:g151997; PIDN:AAA26161.1; !1PID:g151998 REFERENCE A22258 !$#authors Tadros, M.H.; Frank, R.; Drews, G. !$#journal FEBS Lett. (1985) 183:91-94 !$#title The complete amino-acid sequence of the small !1bacteriochlorophyll-binding polypeptide B800-850-beta from !1light-harvesting complex B800-850 of Rhodopseudomonas !1capsulata. !$#accession A22258 !'##molecule_type protein !'##residues 1-49 ##label TAD REFERENCE S34741 !$#authors Bartsch, R.G.; Caffrey, M.S.; van Beeumen, J.J.; Salamon, !1Z.; Tollin, G.; Meyer, T.E.; Cusanovich, M.A. !$#journal Arch. Biochem. Biophys. (1993) 304:117-122 !$#title Purification and properties of an unusual membrane-derived !1cytochrome b-561 from the purple phototrophic bacterium !1Rhodobacter capsulatus, which is structurally related to the !1bacteriochlorophyll-binding protein, LHII-beta. !$#cross-references MUID:93311992; PMID:8323277 !$#accession S34741 !'##status preliminary !'##molecule_type protein !'##residues 2-19 ##label BAR GENETICS !$#gene pucB FUNCTION !$#description this polypeptide (LH-3B) and LH-2 constitute the B-800/850 !1complex of R. sphaeroides 2.4.1 and the spectrally altered !1B-850 complex isolated from the blue-green mutant R-26.1, !1which absorbs at 860 nm !$#note His-20, which is conserved only in the beta chain, is !1located close to an "acid cluster" at the beginning of the !1hydrophobic segment; its function is not yet clear CLASSIFICATION #superfamily light-harvesting protein beta chain KEYWORDS antenna complex; bacteriochlorophyll; light-harvesting !1polypeptide; magnesium; membrane protein FEATURE !$38 #binding_site bacteriochlorophyll magnesium (His) !8(axial ligand) #status predicted SUMMARY #length 49 #molecular-weight 5155 #checksum 1796 SEQUENCE /// ENTRY LBERBC #type complete TITLE light-harvesting protein beta chain - Ectothiorhodospira halochloris ORGANISM #formal_name Ectothiorhodospira halochloris DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 01-Sep-1995 ACCESSIONS S00800; S23287 REFERENCE S00800 !$#authors Wagner-Huber, R.; Brunisholz, R.A.; Bissig, I.; Frank, G.; !1Zuber, H. !$#journal FEBS Lett. (1988) 233:7-11 !$#title A new possible binding site for bacteriochlorophyll b in a !1light-harvesting polypeptide of the bacterium !1Ectothiorhodospira halochloris. !$#accession S00800 !'##molecule_type protein !'##residues 1-65 ##label WAG1 REFERENCE S23164 !$#authors Wagner-Huber, R.; Brunisholz, R.A.; Bissig, I.; Frank, G.; !1Suter, F.; Zuber, H. !$#journal Eur. J. Biochem. (1992) 205:917-925 !$#title The primary structure of the antenna polypeptides of !1Ectothiorhodospira halochloris and Ectothiorhodospira !1halophila. Four core-type antenna polypeptides in E. !1halochloris and E. halophila. !$#cross-references MUID:92249336; PMID:1577009 !$#accession S23287 !'##status preliminary !'##molecule_type protein !'##residues 1-65 ##label WAG2 CLASSIFICATION #superfamily light-harvesting protein beta chain KEYWORDS bacteriochlorophyll; light-harvesting complex; membrane !1protein FEATURE !$34 #binding_site bacteriochlorophyll b magnesium (Asn) !8(axial ligand) #status predicted SUMMARY #length 65 #molecular-weight 7415 #checksum 5975 SEQUENCE /// ENTRY LBRFGV #type complete TITLE light-harvesting protein B-1015 gamma chain - Rhodopseudomonas viridis ORGANISM #formal_name Rhodopseudomonas viridis DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 31-Dec-1993 ACCESSIONS A03455 REFERENCE A90694 !$#authors Brunisholz, R.A.; Jay, F.; Suter, F.; Zuber, H. !$#journal Biol. Chem. Hoppe-Seyler (1985) 366:87-98 !$#title The light-harvesting polypeptides of Rhodopseudomonas !1viridis. The complete amino-acid sequences of B1015-alpha, !1B1015-beta and B1015-gamma. !$#cross-references MUID:85225948; PMID:3890891 !$#accession A03455 !'##molecule_type protein !'##residues 1-36 ##label BRU !'##note residue 34 is Val in approximately one-third of the molecules CLASSIFICATION #superfamily light-harvesting protein gamma chain KEYWORDS antenna complex; bacteriochlorophyll; light-harvesting !1complex; membrane protein SUMMARY #length 36 #molecular-weight 4006 #checksum 2105 SEQUENCE /// ENTRY WNRFMS #type complete TITLE reaction center protein chain M - Rhodobacter sphaeroides ORGANISM #formal_name Rhodobacter sphaeroides DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 16-Feb-1997 ACCESSIONS A03456 REFERENCE A03456 !$#authors Williams, J.C.; Steiner, L.A.; Ogden, R.C.; Simon, M.I.; !1Feher, G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:6505-6509 !$#title Primary structure of the M subunit of the reaction center !1from Rhodopseudomonas sphaeroides. !$#accession A03456 !'##molecule_type DNA !'##residues 1-308 ##label WIL COMMENT The reaction center is a membrane-bound complex that !1mediates the initial photochemical event in the electron !1transfer process of photosynthesis; it is composed of four !1bacteriochlorophylls, two bacteriopheophytins, two !1ubiquinones, one iron, and three highly hydrophobic !1polypeptide chains (designated L, M, and H). CLASSIFICATION #superfamily reaction center protein KEYWORDS transmembrane protein SUMMARY #length 308 #molecular-weight 34509 #checksum 7441 SEQUENCE /// ENTRY WNBCM #type complete TITLE photosynthetic reaction center chain M - Erythrobacter sp. (strain OCH114) ORGANISM #formal_name Erythrobacter sp. DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 03-Mar-2000 ACCESSIONS S16313 REFERENCE S16309 !$#authors Liebetanz, R.; Hornberger, U.; Drews, G. !$#journal Mol. Microbiol. (1991) 5:1459-1468 !$#title Organization of the genes coding for the reaction-centre L !1and M subunits and B870 antenna polypeptides alpha and beta !1from the aerobic photosynthetic bacterium Erythrobacter !1species OCH114. !$#cross-references MUID:92157872; PMID:1787796 !$#accession S16313 !'##molecule_type DNA !'##residues 1-330 ##label LIE !'##cross-references EMBL:X57597; NID:g43356; PIDN:CAA40819.1; !1PID:g43360 GENETICS !$#gene pufM CLASSIFICATION #superfamily reaction center protein KEYWORDS heterodimer; iron; metalloprotein; photosynthesis; !1transmembrane protein FEATURE !$58-82 #domain transmembrane #status predicted #label TM1\ !$112-140 #domain transmembrane #status predicted #label TM2\ !$150-171 #domain transmembrane #status predicted #label TM3\ !$203-229 #domain transmembrane #status predicted #label TM4\ !$265-289 #domain transmembrane #status predicted #label TM5\ !$132 #binding_site bacteriopheophytin (Trp) #status !8predicted\ !$205 #binding_site bacteriochlorophyll magnesium, special !8pair (His) (axial ligand) #status predicted\ !$222,237,269 #binding_site iron (His, Glu, His) (shared with chain !8L) #status predicted SUMMARY #length 330 #molecular-weight 37671 #checksum 7689 SEQUENCE /// ENTRY WNJXM #type complete TITLE photosynthetic reaction center chain M - Chloroflexus aurantiacus ORGANISM #formal_name Chloroflexus aurantiacus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Mar-2000 ACCESSIONS S03567; S03598; S00619; S18296 REFERENCE S03566 !$#authors Shiozawa, J.A.; Lottspeich, F.; Oesterhelt, D.; Feick, R. !$#journal Eur. J. Biochem. (1989) 180:75-84 !$#title The primary structure of the Chloroflexus aurantiacus !1reaction-center polypeptides. !$#cross-references MUID:89210866; PMID:2651125 !$#accession S03567 !'##molecule_type DNA !'##residues 1-307 ##label SHI !'##cross-references EMBL:X14979; NID:g40373; PIDN:CAA33103.1; !1PID:g40375 !$#accession S03598 !'##molecule_type protein !'##residues 2-5;7-14;66-73;122-129;159-166;194-199 ##label SHI2 REFERENCE S00619 !$#authors Ovchinnikov, Y.A.; Abdulaev, N.G.; Shmuckler, B.E.; !1Zargarov, A.A.; Kutuzov, M.A.; Telezhinskaya, I.N.; Levina, !1N.B.; Zolotarev, A.S. !$#journal FEBS Lett. (1988) 232:364-368 !$#title Photosynthetic reaction centre of Chloroflexus aurantiacus. !1Primary structure of M-subunit. !$#cross-references MUID:88242827; PMID:3288502 !$#accession S00619 !'##molecule_type DNA !'##residues 1-307 ##label OVC !'##cross-references EMBL:X07847; NID:g40371; PIDN:CAA30694.1; !1PID:g40372 !$#accession S18296 !'##molecule_type protein !'##residues 13;66-91;129-134;171-174,'X', !1176-180;194-199;218-224;228-236;238-243;247-249;292-304 !1##label OVC2 CLASSIFICATION #superfamily reaction center protein KEYWORDS blocked amino end; heterodimer; iron; metalloprotein; !1photosynthesis; transmembrane protein FEATURE !$2-307 #product photosynthetic reaction center chain M !8#status experimental #label MAT\ !$45-69 #domain transmembrane #status predicted #label TM1\ !$99-129 #domain transmembrane #status predicted #label TM2\ !$137-158 #domain transmembrane #status predicted #label TM3\ !$190-216 #domain transmembrane #status predicted #label TM4\ !$252-276 #domain transmembrane #status predicted #label TM5\ !$2 #modified_site blocked amino end (Ala) (in mature !8form) #status experimental\ !$119 #binding_site bacteriopheophytin (Trp) #status !8predicted\ !$192 #binding_site bacteriochlorophyll magnesium, special !8pair (His) (axial ligand) #status predicted\ !$209,224,256 #binding_site iron (His, Glu, His) (shared with chain !8L) #status predicted SUMMARY #length 307 #molecular-weight 34966 #checksum 6586 SEQUENCE /// ENTRY WNRFLS #type complete TITLE reaction center protein chain L - Rhodobacter sphaeroides ORGANISM #formal_name Rhodobacter sphaeroides DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 16-Jul-1999 ACCESSIONS S24212; A03457 REFERENCE S24212 !$#authors Arnoux, B.; Ducruix, A.; Astier, C.; Picaud, M.; Roth, M.; !1Reiss-Husson, F. !$#journal Biochimie (1990) 72:525-530 !$#title Towards the understanding of the function of Rb sphaeroides !1Y wild type reaction center: gene cloning, protein and !1detergent structures in the three-dimensional crystals. !$#cross-references MUID:91129295; PMID:2126457 !$#accession S24212 !'##molecule_type DNA !'##residues 1-282 ##label ARN !'##cross-references EMBL:X63404; NID:g46442; PIDN:CAA44999.1; !1PID:g46443 REFERENCE A03457 !$#authors Williams, J.C.; Steiner, L.A.; Feher, G.; Simon, M.I. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:7303-7307 !$#title Primary structure of the L subunit of the reaction center !1from Rhodopseudomonas sphaeroides. !$#cross-references MUID:85063779; PMID:6095283 !$#accession A03457 !'##molecule_type DNA !'##residues 1-282 ##label WIL !'##cross-references GB:M10206; NID:g152024; PIDN:AAA26177.1; !1PID:g152025 COMMENT The reaction center is a membrane-bound complex that !1mediates the initial photochemical event in the electron !1transport process of photosynthesis; it is composed of four !1bacteriochlorophylls, two bacteriopheophytins, two !1ubiquinones, one iron, and three highly hydrophobic !1polypeptide chains (designated L, M, and H). CLASSIFICATION #superfamily reaction center protein KEYWORDS electron transfer; membrane protein; photosynthesis SUMMARY #length 282 #molecular-weight 31457 #checksum 7519 SEQUENCE /// ENTRY WNBCL #type complete TITLE photosynthetic reaction center chain L - Erythrobacter sp. (strain OCH114) ORGANISM #formal_name Erythrobacter sp. DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 03-Mar-2000 ACCESSIONS S16312 REFERENCE S16309 !$#authors Liebetanz, R.; Hornberger, U.; Drews, G. !$#journal Mol. Microbiol. (1991) 5:1459-1468 !$#title Organization of the genes coding for the reaction-centre L !1and M subunits and B870 antenna polypeptides alpha and beta !1from the aerobic photosynthetic bacterium Erythrobacter !1species OCH114. !$#cross-references MUID:92157872; PMID:1787796 !$#accession S16312 !'##molecule_type DNA !'##residues 1-283 ##label LIE !'##cross-references EMBL:X57597; NID:g43356; PIDN:CAA40818.1; !1PID:g43359 GENETICS !$#gene pufL CLASSIFICATION #superfamily reaction center protein KEYWORDS heterodimer; iron; metalloprotein; photosynthesis; !1transmembrane protein FEATURE !$33-54 #domain transmembrane #status predicted #label TM1\ !$84-112 #domain transmembrane #status predicted #label TM2\ !$117-140 #domain transmembrane #status predicted #label TM3\ !$172-199 #domain transmembrane #status predicted #label TM4\ !$226-251 #domain transmembrane #status predicted #label TM5\ !$101 #binding_site bacteriopheophytin (Trp) #status !8predicted\ !$154 #binding_site bacteriochlorophyll magnesium, !8accessory (His) (axial ligand) #status predicted\ !$174 #binding_site bacteriochlorophyll magnesium, special !8pair (His) (axial ligand) #status predicted\ !$191,231 #binding_site iron (His) (shared with chain M) !8#status predicted SUMMARY #length 283 #molecular-weight 31364 #checksum 8020 SEQUENCE /// ENTRY WNJXL #type complete TITLE photosynthetic reaction center chain L - Chloroflexus aurantiacus ORGANISM #formal_name Chloroflexus aurantiacus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Mar-2000 ACCESSIONS S03566; S03597; S00499; S18295 REFERENCE S03566 !$#authors Shiozawa, J.A.; Lottspeich, F.; Oesterhelt, D.; Feick, R. !$#journal Eur. J. Biochem. (1989) 180:75-84 !$#title The primary structure of the Chloroflexus aurantiacus !1reaction-center polypeptides. !$#cross-references MUID:89210866; PMID:2651125 !$#accession S03566 !'##molecule_type DNA !'##residues 1-311 ##label SHI !'##cross-references EMBL:X14979; NID:g40373; PIDN:CAA33102.1; !1PID:g40374 !$#accession S03597 !'##molecule_type protein !'##residues !12-33;70-79;127-130;141-146;154-161;169-174;182-185;192-202; !1226-234 ##label SHI2 REFERENCE S00499 !$#authors Ovchinnikov, Y.A.; Abdulaev, N.G.; Zolotarev, A.S.; !1Shmukler, B.E.; Zargarov, A.A.; Kutuzov, M.A.; !1Telezhinskaya, I.N.; Levina, N.B. !$#journal FEBS Lett. (1988) 231:237-242 !$#title Photosynthetic reaction centre of Chloroflexus aurantiacus. !1I. Primary structure of L-subunit. !$#cross-references MUID:88196390; PMID:2834225 !$#accession S00499 !'##molecule_type DNA !'##residues 1-311 ##label OVC !$#accession S18295 !'##molecule_type protein !'##residues 2-41;49-53;101-104;107-125;150-157;162-165;'X', !1183-186;201-203,'X',205-208;236-240;242-263 ##label OVC2 CLASSIFICATION #superfamily reaction center protein KEYWORDS heterodimer; iron; metalloprotein; photosynthesis; !1transmembrane protein FEATURE !$2-311 #product photosynthetic reaction center chain L !8#status experimental #label MAT\ !$67-90 #domain transmembrane #status predicted #label TM1\ !$122-151 #domain transmembrane #status predicted #label TM2\ !$156-179 #domain transmembrane #status predicted #label TM3\ !$211-238 #domain transmembrane #status predicted #label TM4\ !$262-287 #domain transmembrane #status predicted #label TM5\ !$140 #binding_site bacteriopheophytin (Trp) #status !8predicted\ !$193 #binding_site bacteriochlorophyll magnesium, !8accessory (His) (axial ligand) #status predicted\ !$213 #binding_site bacteriochlorophyll magnesium, special !8pair (His) (axial ligand) #status predicted\ !$230,267 #binding_site iron (His) (shared with chain M) !8#status predicted SUMMARY #length 311 #molecular-weight 35147 #checksum 5142 SEQUENCE /// ENTRY FMSP32 #type complete TITLE photosystem II protein D1 precursor [validated] - spinach chloroplast ALTERNATE_NAMES 32K thylakoid membrane protein ORGANISM #formal_name chloroplast Spinacia oleracea #common_name spinach DATE 05-Apr-1983 #sequence_revision 05-Apr-1983 #text_change 15-Sep-2000 ACCESSIONS A38055; S09188; S12196; A60682; S48682; A03458 REFERENCE A38055 !$#authors Zurawski, G.; Bohnert, H.J.; Whitfeld, P.R.; Bottomley, W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:7699-7703 !$#title Nucleotide sequence of the gene for the M-r 32,000 thylakoid !1membrane protein from Spinacia oleracea and Nicotiana !1debneyi predicts a totally conserved primary translation !1product of M-r 38,950. !$#accession A38055 !'##molecule_type DNA !'##residues 1-353 ##label ZUR !'##cross-references EMBL:J01442; NID:g343370; PIDN:AAA84636.1; !1PID:g343371 REFERENCE S09188 !$#authors Marder, J.B.; Goloubinoff, P.; Edelman, M. !$#journal J. Biol. Chem. (1984) 259:3900-3908 !$#title Molecular architecture of the rapidly metabolized !132-kilodalton protein of photosystem II. !$#cross-references MUID:84162071; PMID:6368553 !$#accession S09188 !'##status preliminary !'##molecule_type DNA !'##residues 195-213,'N',215-243;315-353 ##label MAR REFERENCE S09185 !$#authors Michel, H.; Hunt, D.F.; Shabanowitz, J.; Bennett, J. !$#journal J. Biol. Chem. (1988) 263:1123-1130 !$#title Tandem mass spectrometry reveals that three photosystem II !1proteins of spinach chloroplasts contain !1N-acetyl-O-phosphothreonine at their NH(2) termini. !$#cross-references MUID:88087237; PMID:3121625 !$#accession S12196 !'##molecule_type protein !'##residues 2-8 ##label MIC REFERENCE A60682 !$#authors Takahashi, Y.; Nakane, H.; Kojima, H.; Satoh, K. !$#journal Plant Cell Physiol. (1990) 31:273-280 !$#title Chromatographic purification and determination of the !1carboxy-terminal sequences of photosystem II reaction center !1proteins, D1 and D2. !$#accession A60682 !'##molecule_type protein !'##residues 340-344 ##label TAK REFERENCE S48682 !$#authors Tomo, T.; Satoh, K. !$#journal FEBS Lett. (1994) 351:27-30 !$#title Nearest neighbor analysis of D1 and D2 subunits in the !1photosystem II reaction center using a bifunctional !1cross-linker, hexamethylene diisocyanate. !$#cross-references MUID:94357272; PMID:8076687 !$#accession S48682 !'##molecule_type protein !'##residues !12-37;38-57;119-127;128-139;140-172;173-183;184-194;195-199; !1200-214;215-232;283-293;294-328;329-331;332-344 ##label TOM REFERENCE A65447 !$#authors Svensson, B.; Etchebest, C.; Tuffery, P.; Van Kan, P.; !1Smith, J.; Styring, S. !$#submission submitted to the Brookhaven Protein Data Bank, October 1996 !$#cross-references PDB:1DOP !$#contents annotation; theoretical model, residues 106-224;266-297 REFERENCE A58807 !$#authors Svensson, B.; Etchebest, C.; Tuffery, P.; van Kan, P.; !1Smith, J.; Styring, S. !$#journal Biochemistry (1996) 35:14486-14502 !$#title A model for the photosystem II reaction center core !1including the structure of the primary donor P680. !$#cross-references MUID:97085405; PMID:8931545 !$#contents annotation; theoretical model GENETICS !$#gene psbA !$#genome chloroplast CLASSIFICATION #superfamily photosystem II D2 protein KEYWORDS acetylated amino end; chlorophyll; chloroplast; !1chromoprotein; electron transfer; iron; magnesium; !1membrane-associated complex; metalloprotein; phosphoprotein; !1photosynthesis; photosystem II; thylakoid; transmembrane !1protein FEATURE !$2-344 #product photosystem II protein D1 #status !8experimental #label MAT\ !$31-55 #domain transmembrane #status predicted #label TM1\ !$111-136 #domain transmembrane #status predicted #label TM2\ !$142-165 #domain transmembrane #status predicted #label TM3\ !$196-221 #domain transmembrane #status predicted #label TM4\ !$270-290 #domain transmembrane #status predicted #label TM5\ !$345-353 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$2 #modified_site acetylated amino end (Thr) (in mature !8form) #status experimental\ !$2 #binding_site phosphate (Thr) (covalent) #status !8experimental\ !$126,130,147 #binding_site pheophytin (Tyr, Glu, Tyr) #status !8predicted\ !$161 #active_site Tyr (tyrosyl radical intermediate) !8#status predicted\ !$190 #active_site His #status predicted\ !$198 #binding_site chlorophyll magnesium (His) (axial !8ligand) #status predicted\ !$215,272 #binding_site iron (His) #status predicted\ !$286 #binding_site chlorophyll (Thr) #status predicted SUMMARY #length 353 #molecular-weight 38950 #checksum 9364 SEQUENCE /// ENTRY FMNT3D #type complete TITLE photosystem II protein D1 precursor - Debney's tobacco chloroplast ALTERNATE_NAMES 32K thylakoid membrane protein ORGANISM #formal_name chloroplast Nicotiana debneyi #common_name Debney's tobacco DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jul-1999 ACCESSIONS B38055; A03458 REFERENCE A38055 !$#authors Zurawski, G.; Bohnert, H.J.; Whitfeld, P.R.; Bottomley, W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:7699-7703 !$#title Nucleotide sequence of the gene for the M-r 32,000 thylakoid !1membrane protein from Spinacia oleracea and Nicotiana !1debneyi predicts a totally conserved primary translation !1product of M-r 38,950. !$#accession B38055 !'##molecule_type DNA !'##residues 1-353 ##label ZUR !'##cross-references GB:J01448; NID:g343496; PIDN:AAA84687.1; !1PID:g343497 GENETICS !$#gene psbA !$#genome chloroplast CLASSIFICATION #superfamily photosystem II D2 protein KEYWORDS acetylated amino end; chlorophyll; chloroplast; !1chromoprotein; electron transfer; iron; magnesium; !1membrane-associated complex; metalloprotein; phosphoprotein; !1photosynthesis; photosystem II; thylakoid; transmembrane !1protein FEATURE !$2-344 #product photosystem II protein D1 #status predicted !8#label MAT\ !$31-55 #domain transmembrane #status predicted #label TM1\ !$101-136 #domain transmembrane #status predicted #label TM2\ !$142-165 #domain transmembrane #status predicted #label TM3\ !$196-221 #domain transmembrane #status predicted #label TM4\ !$270-290 #domain transmembrane #status predicted #label TM5\ !$345-353 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$2 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$2 #modified_site acetylated amino end (Thr) (in mature !8form) #status predicted\ !$126,130,147 #binding_site pheophytin (Tyr, Glu, Tyr) #status !8predicted\ !$161 #active_site Tyr (tyrosyl radical intermediate) !8#status predicted\ !$190 #active_site His #status predicted\ !$198 #binding_site chlorophyll magnesium (His) (axial !8ligand) #status predicted\ !$215,272 #binding_site iron (His) #status predicted\ !$286 #binding_site chlorophyll (Thr) #status predicted SUMMARY #length 353 #molecular-weight 38950 #checksum 9364 SEQUENCE /// ENTRY FMMH32 #type complete TITLE photosystem II protein D1 precursor - green amaranth chloroplast ALTERNATE_NAMES 32K thylakoid membrane protein ORGANISM #formal_name chloroplast Amaranthus hybridus #common_name green amaranth DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 18-Sep-1998 ACCESSIONS A37572; A03458 REFERENCE A37572 !$#authors Hirschberg, J.; McIntosh, L. !$#journal Science (1983) 222:1346-1349 !$#title Molecular basis of herbicide resistance in Amaranthus !1hybridus. !$#accession A37572 !'##molecule_type DNA !'##residues 1-353 ##label HIR !'##cross-references GB:K01200 !'##note the sequence of the "herbicide-resistant" protein differs from !1the wild type ("herbicide-susceptible") sequence shown in !1having 264-Gly COMMENT This protein, which is tightly bound to the thylakoid !1membrane, may be involved in the electron flow of the !1chloroplast photosystem II; its synthesis is regulated by !1light. GENETICS !$#gene psbA !$#genome chloroplast CLASSIFICATION #superfamily photosystem II D2 protein KEYWORDS acetylated amino end; chlorophyll; chloroplast; !1chromoprotein; electron transfer; iron; magnesium; !1membrane-associated complex; metalloprotein; phosphoprotein; !1photosynthesis; photosystem II; thylakoid; transmembrane !1protein FEATURE !$2-344 #product photosystem II protein D1 #status predicted !8#label MAT\ !$31-55 #domain transmembrane #status predicted #label TM1\ !$101-136 #domain transmembrane #status predicted #label TM2\ !$142-165 #domain transmembrane #status predicted #label TM3\ !$196-221 #domain transmembrane #status predicted #label TM4\ !$270-290 #domain transmembrane #status predicted #label TM5\ !$345-353 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$2 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$2 #modified_site acetylated amino end (Thr) (in mature !8form) #status predicted\ !$126,130,147 #binding_site pheophytin (Tyr, Glu, Tyr) #status !8predicted\ !$161 #active_site Tyr (tyrosyl radical intermediate) !8#status predicted\ !$190 #active_site His #status predicted\ !$198 #binding_site chlorophyll magnesium (His) (axial !8ligand) #status predicted\ !$215,272 #binding_site iron (His) #status predicted\ !$286 #binding_site chlorophyll (Thr) #status predicted SUMMARY #length 353 #molecular-weight 38964 #checksum 8675 SEQUENCE /// ENTRY FMSX3N #type complete TITLE photosystem II protein D1 precursor - black nightshade chloroplast ALTERNATE_NAMES 32K thylakoid membrane protein ORGANISM #formal_name chloroplast Solanum nigrum #common_name black nightshade DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jul-1999 ACCESSIONS A37573; A03458 REFERENCE A37573 !$#authors Goloubinoff, P.; Edelman, M.; Hallick, R.B. !$#journal Nucleic Acids Res. (1984) 12:9489-9496 !$#title Chloroplast-coded atrazine resistance in Solanum nigrum: !1psbA loci from susceptible and resistant biotypes are !1isogenic except for a single codon change. !$#cross-references MUID:85087951; PMID:6514581 !$#accession A37573 !'##molecule_type DNA !'##residues 1-353 ##label GOL !'##cross-references GB:X01651; NID:g12243; PIDN:CAA25815.1; PID:g12244 !'##note the sequence of the wild type ("herbicide-susceptible") protein !1is shown; the sequence of the "herbicide-resistant" protein !1differs in having 264-Gly GENETICS !$#gene psbA !$#genome chloroplast CLASSIFICATION #superfamily photosystem II D2 protein KEYWORDS acetylated amino end; chlorophyll; chloroplast; !1chromoprotein; electron transfer; iron; magnesium; !1membrane-associated complex; metalloprotein; phosphoprotein; !1photosynthesis; photosystem II; thylakoid; transmembrane !1protein FEATURE !$2-344 #product photosystem II protein D1 #status predicted !8#label MAT\ !$31-55 #domain transmembrane #status predicted #label TM1\ !$101-136 #domain transmembrane #status predicted #label TM2\ !$142-165 #domain transmembrane #status predicted #label TM3\ !$196-221 #domain transmembrane #status predicted #label TM4\ !$270-290 #domain transmembrane #status predicted #label TM5\ !$345-353 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$2 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$2 #modified_site acetylated amino end (Thr) (in mature !8form) #status predicted\ !$126,130,147 #binding_site pheophytin (Tyr, Glu, Tyr) #status !8predicted\ !$161 #active_site Tyr (tyrosyl radical intermediate) !8#status predicted\ !$190 #active_site His #status predicted\ !$198 #binding_site chlorophyll magnesium (His) (axial !8ligand) #status predicted\ !$215,272 #binding_site iron (His) #status predicted\ !$286 #binding_site chlorophyll (Thr) #status predicted SUMMARY #length 353 #molecular-weight 38950 #checksum 9364 SEQUENCE /// ENTRY FMNT32 #type complete TITLE photosystem II protein D1 precursor - common tobacco chloroplast ALTERNATE_NAMES 32K thylakoid membrane protein ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 18-Sep-1998 ACCESSIONS A03459 REFERENCE A00149 !$#authors Sugiura, M. !$#submission submitted to the EMBL Data Library, August 1986 !$#accession A03459 !'##molecule_type DNA !'##residues 1-353 ##label SUG !'##cross-references EMBL:Z00044 REFERENCE A38013 !$#authors Shinozaki, K.; Ohme, M.; Tanaka, M.; Wakasugi, T.; !1Hayashida, N.; Matsubayashi, T.; Zaita, N.; Chunwongse, J.; !1Obokata, J.; Yamaguchi-Shinozaki, K.; Ohto, C.; Torazawa, !1K.; Meng, B.Y.; Sugita, M.; Deno, H.; Kamogashira, T.; !1Yamada, K.; Kusuda, J.; Takaiwa, F.; Kato, A.; Tohdoh, N.; !1Shimada, H.; Sugiura, M. !$#journal EMBO J. (1986) 5:2043-2049 !$#title The complete nucleotide sequence of the tobacco chloroplast !1genome: its gene organization and expression. !$#contents annotation; gene organization, sites, features GENETICS !$#gene psbA !$#genome chloroplast CLASSIFICATION #superfamily photosystem II D2 protein KEYWORDS acetylated amino end; chlorophyll; chloroplast; !1chromoprotein; electron transfer; iron; magnesium; !1membrane-associated complex; metalloprotein; phosphoprotein; !1photosynthesis; photosystem II; thylakoid; transmembrane !1protein FEATURE !$2-344 #product photosystem II protein D1 #status predicted !8#label MAT\ !$31-55 #domain transmembrane #status predicted #label TM1\ !$101-136 #domain transmembrane #status predicted #label TM2\ !$142-165 #domain transmembrane #status predicted #label TM3\ !$196-221 #domain transmembrane #status predicted #label TM4\ !$270-290 #domain transmembrane #status predicted #label TM5\ !$345-353 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$2 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$2 #modified_site acetylated amino end (Thr) (in mature !8form) #status predicted\ !$126,130,147 #binding_site pheophytin (Tyr, Glu, Tyr) #status !8predicted\ !$161 #active_site Tyr (tyrosyl radical intermediate) !8#status predicted\ !$190 #active_site His #status predicted\ !$198 #binding_site chlorophyll magnesium (His) (axial !8ligand) #status predicted\ !$215,272 #binding_site iron (His) #status predicted\ !$286 #binding_site chlorophyll (Thr) #status predicted SUMMARY #length 353 #molecular-weight 38972 #checksum 9548 SEQUENCE /// ENTRY FMSY32 #type complete TITLE photosystem II protein D1 precursor - soybean chloroplast ALTERNATE_NAMES 32K thylakoid membrane protein ORGANISM #formal_name chloroplast Glycine max #common_name soybean DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS A03460 REFERENCE A03460 !$#authors Spielmann, A.; Stutz, E. !$#journal Nucleic Acids Res. (1983) 11:7157-7167 !$#title Nucleotide sequence of soybean chloroplast DNA regions which !1contain the psb A and trn H genes and cover the ends of the !1large single copy region and one end of the inverted !1repeats. !$#cross-references MUID:84041511; PMID:6314279 !$#accession A03460 !'##molecule_type DNA !'##residues 1-353 ##label SPI !'##cross-references EMBL:X00152; NID:g11565; PIDN:CAA24986.1; !1PID:g11566 GENETICS !$#gene psbA !$#genome chloroplast CLASSIFICATION #superfamily photosystem II D2 protein KEYWORDS acetylated amino end; chlorophyll; chloroplast; !1chromoprotein; electron transfer; iron; magnesium; !1membrane-associated complex; metalloprotein; phosphoprotein; !1photosynthesis; photosystem II; thylakoid; transmembrane !1protein FEATURE !$2-344 #product photosystem II protein D1 #status predicted !8#label MAT\ !$31-55 #domain transmembrane #status predicted #label TM1\ !$101-136 #domain transmembrane #status predicted #label TM2\ !$142-165 #domain transmembrane #status predicted #label TM3\ !$196-221 #domain transmembrane #status predicted #label TM4\ !$270-290 #domain transmembrane #status predicted #label TM5\ !$345-353 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$2 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$2 #modified_site acetylated amino end (Thr) (in mature !8form) #status predicted\ !$126,130,147 #binding_site pheophytin (Tyr, Glu, Tyr) #status !8predicted\ !$161 #active_site Tyr (tyrosyl radical intermediate) !8#status predicted\ !$190 #active_site His #status predicted\ !$198 #binding_site chlorophyll magnesium (His) (axial !8ligand) #status predicted\ !$215,272 #binding_site iron (His) #status predicted\ !$286 #binding_site chlorophyll (Thr) #status predicted SUMMARY #length 353 #molecular-weight 38948 #checksum 9260 SEQUENCE /// ENTRY FMRZ32 #type complete TITLE photosystem II protein D1 precursor - rice chloroplast ALTERNATE_NAMES 32K thylakoid membrane protein; photosystem II D1 protein ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS JQ0200; S05080; A54732 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0200 !'##molecule_type DNA !'##residues 1-353 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05080 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-353 ##label HIR !'##cross-references EMBL:X15901; NID:g11957; PIDN:CAA34007.1; !1PID:g11958 !'##experimental_source cv. Nihonbare !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1989 REFERENCE A54732 !$#authors Wu, N.H.; Cote, J.C.; Wu, R. !$#journal Dev. Genet. (1987) 8:339-350 !$#title Structure of the chloroplast psbA gene encoding the Q-B !1protein from Oryza sativa L. !$#accession A54732 !'##molecule_type DNA !'##residues 1-353 ##label WUA !'##cross-references GB:M36191; NID:g343211; PIDN:AAA84591.1; !1PID:g343212 GENETICS !$#gene psbA !$#genome chloroplast CLASSIFICATION #superfamily photosystem II D2 protein KEYWORDS acetylated amino end; chlorophyll; chloroplast; !1chromoprotein; electron transfer; iron; magnesium; !1membrane-associated complex; metalloprotein; phosphoprotein; !1photosynthesis; photosystem II; thylakoid; transmembrane !1protein FEATURE !$2-344 #product photosystem II protein D1 #status predicted !8#label MAT\ !$31-55 #domain transmembrane #status predicted #label TM1\ !$101-136 #domain transmembrane #status predicted #label TM2\ !$142-165 #domain transmembrane #status predicted #label TM3\ !$196-221 #domain transmembrane #status predicted #label TM4\ !$270-290 #domain transmembrane #status predicted #label TM5\ !$345-353 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$2 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$2 #modified_site acetylated amino end (Thr) (in mature !8form) #status predicted\ !$126,130,147 #binding_site pheophytin (Tyr, Glu, Tyr) #status !8predicted\ !$161 #active_site Tyr (tyrosyl radical intermediate) !8#status predicted\ !$190 #active_site His #status predicted\ !$198 #binding_site chlorophyll magnesium (His) (axial !8ligand) #status predicted\ !$215,272 #binding_site iron (His) #status predicted\ !$286 #binding_site chlorophyll (Thr) #status predicted SUMMARY #length 353 #molecular-weight 38962 #checksum 9595 SEQUENCE /// ENTRY F2VFD1 #type complete TITLE photosystem II protein D1 precursor - fava bean chloroplast ORGANISM #formal_name chloroplast Vicia faba #common_name fava bean DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jul-1999 ACCESSIONS S14911; S08446; S06764 REFERENCE S14911 !$#authors Ko, K. !$#journal Nucleic Acids Res. (1990) 18:375 !$#title Nucleotide sequence of the psbA gene encoded by the Vicia !1faba chloroplast genome. !$#cross-references MUID:90221833; PMID:2326175 !$#accession S14911 !'##molecule_type DNA !'##residues 1-353 ##label KOK !'##cross-references EMBL:X17694; NID:g12380; PIDN:CAA35688.1; !1PID:g12381 REFERENCE S08443 !$#authors Herdenberger, F.; Pillay, D.T.N.; Steinmetz, A. !$#journal Nucleic Acids Res. (1990) 18:1297 !$#title Sequence of the trnH gene and the inverted repeat structure !1deletion site of the broad bean chloroplast genome. !$#cross-references MUID:90206803; PMID:2320425 !$#accession S08446 !'##status translation not shown !'##molecule_type DNA !'##residues 341-346,'E',348-351,'N',353 ##label HER !'##cross-references EMBL:X51471; NID:g12387; PIDN:CAA35835.1; !1PID:g12391 GENETICS !$#gene psbA !$#genome chloroplast CLASSIFICATION #superfamily photosystem II D2 protein KEYWORDS acetylated amino end; chlorophyll; chloroplast; !1chromoprotein; electron transfer; iron; magnesium; !1membrane-associated complex; metalloprotein; phosphoprotein; !1photosynthesis; photosystem II; thylakoid; transmembrane !1protein FEATURE !$2-344 #product photosystem II protein D1 #status predicted !8#label MAT\ !$31-55 #domain transmembrane #status predicted #label TM1\ !$101-136 #domain transmembrane #status predicted #label TM2\ !$142-165 #domain transmembrane #status predicted #label TM3\ !$196-221 #domain transmembrane #status predicted #label TM4\ !$270-290 #domain transmembrane #status predicted #label TM5\ !$345-353 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$2 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$2 #modified_site acetylated amino end (Thr) (in mature !8form) #status predicted\ !$126,130,147 #binding_site pheophytin (Tyr, Glu, Tyr) #status !8predicted\ !$161 #active_site Tyr (tyrosyl radical intermediate) !8#status predicted\ !$190 #active_site His #status predicted\ !$198 #binding_site chlorophyll magnesium (His) (axial !8ligand) #status predicted\ !$286 #binding_site chlorophyll (Thr) #status predicted SUMMARY #length 353 #molecular-weight 38974 #checksum 724 SEQUENCE /// ENTRY F2DWD1 #type complete TITLE photosystem II protein D1 precursor - Spirodela oligorhiza chloroplast ORGANISM #formal_name chloroplast Spirodela oligorhiza DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS S17738 REFERENCE S17738 !$#authors Avni, A.; Mehta, R.A.; Mattoo, A.K.; Greenberg, B.M.; !1Chattoo, B.B.; Heller, D.; Edelman, M. !$#journal Plant Mol. Biol. (1991) 17:919-921 !$#title Nucleotide sequence of the Spirodela oligorrhiza chloroplast !1psbA gene coding for the D1 (32 kDa) photosystem II protein. !$#cross-references MUID:92003702; PMID:1912505 !$#accession S17738 !'##molecule_type DNA !'##residues 1-353 ##label AVN !'##cross-references EMBL:X59557; NID:g12275; PIDN:CAA42156.1; !1PID:g12276 GENETICS !$#gene psbA !$#genome chloroplast CLASSIFICATION #superfamily photosystem II D2 protein KEYWORDS acetylated amino end; chlorophyll; chloroplast; !1chromoprotein; electron transfer; iron; magnesium; !1membrane-associated complex; metalloprotein; phosphoprotein; !1photosynthesis; photosystem II; thylakoid; transmembrane !1protein FEATURE !$2-344 #product photosystem II protein D1 #status predicted !8#label MAT\ !$31-55 #domain transmembrane #status predicted #label TM1\ !$101-136 #domain transmembrane #status predicted #label TM2\ !$142-165 #domain transmembrane #status predicted #label TM3\ !$196-221 #domain transmembrane #status predicted #label TM4\ !$270-290 #domain transmembrane #status predicted #label TM5\ !$345-353 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$2 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$2 #modified_site acetylated amino end (Thr) (in mature !8form) #status predicted\ !$126,130,147 #binding_site pheophytin (Tyr, Glu, Tyr) #status !8predicted\ !$161 #active_site Tyr (tyrosyl radical intermediate) !8#status predicted\ !$190 #active_site His #status predicted\ !$198 #binding_site chlorophyll magnesium (His) (axial !8ligand) #status predicted\ !$215,272 #binding_site iron (His) #status predicted\ !$286 #binding_site chlorophyll (Thr) #status predicted SUMMARY #length 353 #molecular-weight 39008 #checksum 9321 SEQUENCE /// ENTRY F2BHD1 #type complete TITLE photosystem II protein D1 precursor - barley chloroplast ALTERNATE_NAMES photosystem II 32K protein; photosystem II Q-B protein; thylakoid membrane 32K protein ORGANISM #formal_name chloroplast Hordeum vulgare #common_name barley DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS S00883; JN0422; S02335 REFERENCE S00883 !$#authors Efimov, V.A.; Andreeva, A.V.; Reverdatto, S.V.; Jung, R.; !1Chakhmakhcheva, O.G. !$#journal Nucleic Acids Res. (1988) 16:5685 !$#title Nucleotide sequence of the barley chloroplast psbA gene for !1the Q-beta protein of photosystem II. !$#cross-references MUID:88262570; PMID:3290855 !$#accession S00883 !'##molecule_type DNA !'##residues 1-353 ##label EFI !'##cross-references EMBL:X07521; NID:g12589; PIDN:CAA30400.1; !1PID:g12590 REFERENCE JN0422 !$#authors Efimov, V.A.; Andreeva, A.V.; Dmitrakova, E.V.; Pashkova, !1I.N.; Reverdatto, S.V.; Jung, R.; Chakhmakhcheva, O.G. !$#journal Bioorg. Khim. (1988) 14:1117-1121 !$#title Nucleotide sequence of the barley chloroplast psbA gene !1coding for a herbicide-binding protein. !$#cross-references MUID:89117611; PMID:3064751 !$#accession JN0422 !'##status preliminary !'##molecule_type DNA !'##residues 1-353 ##label EF2 !'##cross-references GB:M38374; NID:g336411; PIDN:AAA84046.1; !1PID:g336412 REFERENCE S01291 !$#authors Boyer, S.K.; Mullet, J.E. !$#journal Nucleic Acids Res. (1988) 16:8184 !$#title Sequence and transcript map of barley chloroplast psbA gene. !$#cross-references MUID:88335566; PMID:3419912 !$#accession S02335 !'##molecule_type DNA !'##residues 1-353 ##label BOY !'##cross-references EMBL:X07942; NID:g11588; PIDN:CAA30763.1; !1PID:g11590 GENETICS !$#gene psbA !$#genome chloroplast CLASSIFICATION #superfamily photosystem II D2 protein KEYWORDS acetylated amino end; chlorophyll; chloroplast; !1chromoprotein; electron transfer; iron; magnesium; !1membrane-associated complex; metalloprotein; phosphoprotein; !1photosynthesis; photosystem II; thylakoid; transmembrane !1protein FEATURE !$2-344 #product photosystem II protein D1 #status predicted !8#label MAT\ !$31-55 #domain transmembrane #status predicted #label TM1\ !$101-136 #domain transmembrane #status predicted #label TM2\ !$142-165 #domain transmembrane #status predicted #label TM3\ !$196-221 #domain transmembrane #status predicted #label TM4\ !$270-290 #domain transmembrane #status predicted #label TM5\ !$345-353 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$2 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$2 #modified_site acetylated amino end (Thr) (in mature !8form) #status predicted\ !$126,130,147 #binding_site pheophytin (Tyr, Glu, Tyr) #status !8predicted\ !$161 #active_site Tyr (tyrosyl radical intermediate) !8#status predicted\ !$190 #active_site His #status predicted\ !$198 #binding_site chlorophyll magnesium (His) (axial !8ligand) #status predicted\ !$215,272 #binding_site iron (His) #status predicted\ !$286 #binding_site chlorophyll (Thr) #status predicted SUMMARY #length 353 #molecular-weight 38904 #checksum 9394 SEQUENCE /// ENTRY F2NUD1 #type complete TITLE photosystem II protein D1 precursor - rye chloroplast ALTERNATE_NAMES photosystem II 32K protein; photosystem II Q-B protein; thylakoid membrane 32K protein ORGANISM #formal_name chloroplast Secale cereale #common_name rye DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 18-Sep-1998 ACCESSIONS S03195; S05071 REFERENCE S03195 !$#authors Kolosov, V.L.; Bukharov, A.A.; Zolotarev, A.S. !$#journal Nucleic Acids Res. (1989) 17:1759 !$#title Nucleotide sequence of the rye chloroplast psbA gene, !1encoding D1 protein of photosystem II. !$#cross-references MUID:89160330; PMID:2646598 !$#accession S03195 !'##molecule_type DNA !'##residues 1-353 ##label KOL !'##cross-references EMBL:X13327 !'##note the authors translated the codon GTT for residue 346 as Ile and !1GTT for residue 348 as Ala REFERENCE S05071 !$#authors Zolotarev, A.S. !$#submission submitted to the EMBL Data Library, October 1989 !$#accession S05071 !'##molecule_type DNA !'##residues 1-100,'S',102-353 ##label ZOL !'##cross-references EMBL:X13327 GENETICS !$#gene psbA !$#genome chloroplast CLASSIFICATION #superfamily photosystem II D2 protein KEYWORDS acetylated amino end; chlorophyll; chloroplast; !1chromoprotein; electron transfer; iron; magnesium; !1membrane-associated complex; metalloprotein; phosphoprotein; !1photosynthesis; photosystem II; thylakoid; transmembrane !1protein FEATURE !$2-344 #product photosystem II protein D1 #status predicted !8#label MAT\ !$31-55 #domain transmembrane #status predicted #label TM1\ !$101-136 #domain transmembrane #status predicted #label TM2\ !$142-165 #domain transmembrane #status predicted #label TM3\ !$196-221 #domain transmembrane #status predicted #label TM4\ !$270-290 #domain transmembrane #status predicted #label TM5\ !$345-353 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$2 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$2 #modified_site acetylated amino end (Thr) (in mature !8form) #status predicted\ !$126,130,147 #binding_site pheophytin (Tyr, Glu, Tyr) #status !8predicted\ !$161 #active_site Tyr (tyrosyl radical intermediate) !8#status predicted\ !$190 #active_site His #status predicted\ !$198 #binding_site chlorophyll magnesium (His) (axial !8ligand) #status predicted\ !$215,272 #binding_site iron (His) #status predicted\ !$286 #binding_site chlorophyll (Thr) #status predicted SUMMARY #length 353 #molecular-weight 38980 #checksum 8966 SEQUENCE /// ENTRY F2CN1U #type complete TITLE photosystem II protein D1 precursor - upland cotton chloroplast ALTERNATE_NAMES Q-B protein; thylakoid herbicide-binding protein, 32K ORGANISM #formal_name chloroplast Gossypium hirsutum #common_name upland cotton DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS S07583 REFERENCE S07583 !$#authors Ulmasov, T.N.; Gulov, M.K.; Aliev, K.A.; Andrianov, V.M.; !1Piruzian, E.S. !$#journal Nucleic Acids Res. (1990) 18:186 !$#title Nucleotide sequences of the chloroplast psbA and trnH genes !1from cotton Gossypium hirsutum. !$#cross-references MUID:90174919; PMID:2408006 !$#accession S07583 !'##status translation not shown !'##molecule_type DNA !'##residues 1-353 ##label ULM !'##cross-references EMBL:X15885; NID:g11306; PIDN:CAA33895.1; !1PID:g11307 GENETICS !$#gene psbA !$#genome chloroplast CLASSIFICATION #superfamily photosystem II D2 protein KEYWORDS acetylated amino end; chlorophyll; chloroplast; !1chromoprotein; electron transfer; iron; magnesium; !1membrane-associated complex; metalloprotein; phosphoprotein; !1photosynthesis; photosystem II; thylakoid; transmembrane !1protein FEATURE !$2-344 #product photosystem II protein D1 #status predicted !8#label MAT\ !$31-55 #domain transmembrane #status predicted #label TM1\ !$101-136 #domain transmembrane #status predicted #label TM2\ !$142-165 #domain transmembrane #status predicted #label TM3\ !$196-221 #domain transmembrane #status predicted #label TM4\ !$270-290 #domain transmembrane #status predicted #label TM5\ !$345-353 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$2 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$2 #modified_site acetylated amino end (Thr) (in mature !8form) #status predicted\ !$126,130,147 #binding_site pheophytin (Tyr, Glu, Tyr) #status !8predicted\ !$161 #active_site Tyr (tyrosyl radical intermediate) !8#status predicted\ !$190 #active_site His #status predicted\ !$198 #binding_site chlorophyll magnesium (His) (axial !8ligand) #status predicted\ !$215,272 #binding_site iron (His) #status predicted\ !$286 #binding_site chlorophyll (Thr) #status predicted SUMMARY #length 353 #molecular-weight 38950 #checksum 9364 SEQUENCE /// ENTRY F2PMD1 #type complete TITLE photosystem II protein D1 precursor - garden pea chloroplast ALTERNATE_NAMES thylakoid membrane 32K protein ORGANISM #formal_name chloroplast Pisum sativum #common_name garden pea DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS S11299; S07401; S24139 REFERENCE S11299 !$#authors Oishi, K.K.; Shapiro, D.R.; Tewari, K.K. !$#journal Mol. Cell. Biol. (1984) 4:2556-2563 !$#title Sequence organization of a pea chloroplast DNA gene coding !1for a 34,500-dalton protein. !$#cross-references MUID:85085966; PMID:6513932 !$#accession S11299 !'##molecule_type DNA !'##residues 1-353 ##label OIS !'##cross-references EMBL:M11005; NID:g343031; PIDN:AAA84547.1; !1PID:g343032 !'##note the authors translated the codon GTT for residue 346 as Ile REFERENCE S07401 !$#authors Boyer, S.K.; Mullet, J.E. !$#journal Plant Mol. Biol. (1986) 6:229-243 !$#title Characterization of P. sativum chloroplast psbA transcripts !1produced in vivo, in vitro and in E. coli. !$#accession S07401 !'##molecule_type DNA !'##residues 1-156 ##label BOY !'##cross-references EMBL:M16899; NID:g343033; PIDN:AAA84549.1; !1PID:g552818 REFERENCE S24139 !$#authors Whitelegge, J.P.; Jewess, P.; Pickering, M.G.; Gerrish, C.; !1Camilleri, P.; Bowyer, J.R. !$#journal Eur. J. Biochem. (1992) 207:1077-1084 !$#title Sequence analysis of photoaffinity-labelled peptides derived !1by proteolysis of photosystem-2 reaction centres from !1thylakoid membranes treated with [(14)C]azidoatrazine. !$#cross-references MUID:92362609; PMID:1499553 !$#accession S24139 !'##molecule_type protein !'##residues 137-141,'X',143-147 ##label WHI GENETICS !$#gene psbA !$#genome chloroplast CLASSIFICATION #superfamily photosystem II D2 protein KEYWORDS acetylated amino end; chlorophyll; chloroplast; !1chromoprotein; electron transfer; iron; magnesium; !1membrane-associated complex; metalloprotein; phosphoprotein; !1photosynthesis; photosystem II; thylakoid; transmembrane !1protein FEATURE !$2-344 #product photosystem II protein D1 #status predicted !8#label MAT\ !$31-55 #domain transmembrane #status predicted #label TM1\ !$101-136 #domain transmembrane #status predicted #label TM2\ !$142-165 #domain transmembrane #status predicted #label TM3\ !$196-221 #domain transmembrane #status predicted #label TM4\ !$270-290 #domain transmembrane #status predicted #label TM5\ !$345-353 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$2 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$2 #modified_site acetylated amino end (Thr) (in mature !8form) #status predicted\ !$126,130,147 #binding_site pheophytin (Tyr, Glu, Tyr) #status !8predicted\ !$161 #active_site Tyr (tyrosyl radical intermediate) !8#status predicted\ !$190 #active_site His #status predicted\ !$198 #binding_site chlorophyll magnesium (His) (axial !8ligand) #status predicted\ !$215,272 #binding_site iron (His) #status predicted\ !$286 #binding_site chlorophyll (Thr) #status predicted SUMMARY #length 353 #molecular-weight 38961 #checksum 9248 SEQUENCE /// ENTRY F2NT1C #type complete TITLE photosystem II protein D1 precursor - curled-leaved tobacco chloroplast ALTERNATE_NAMES thylakoid membrane 32K protein ORGANISM #formal_name chloroplast Nicotiana plumbaginifolia #common_name curled-leaved tobacco DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS S02169 REFERENCE S01616 !$#authors Pay, A.; Smith, M.A.; Nagy, F.; Marton, L. !$#journal Nucleic Acids Res. (1988) 16:8176 !$#title Sequence of the psbA gene from wild type and !1triazin-resistant Nicotiana plumbaginifolia. !$#cross-references MUID:88335558; PMID:3419908 !$#accession S02169 !'##molecule_type DNA !'##residues 1-353 ##label PAY !'##cross-references EMBL:X08016; NID:g11754; PIDN:CAA30817.1; !1PID:g11755 GENETICS !$#gene psbA !$#genome chloroplast CLASSIFICATION #superfamily photosystem II D2 protein KEYWORDS acetylated amino end; chlorophyll; chloroplast; !1chromoprotein; electron transfer; iron; magnesium; !1membrane-associated complex; metalloprotein; phosphoprotein; !1photosynthesis; photosystem II; thylakoid; transmembrane !1protein FEATURE !$2-344 #product photosystem II protein D1 #status predicted !8#label MAT\ !$31-55 #domain transmembrane #status predicted #label TM1\ !$101-136 #domain transmembrane #status predicted #label TM2\ !$142-165 #domain transmembrane #status predicted #label TM3\ !$196-221 #domain transmembrane #status predicted #label TM4\ !$270-290 #domain transmembrane #status predicted #label TM5\ !$345-353 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$2 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$2 #modified_site acetylated amino end (Thr) (in mature !8form) #status predicted\ !$126,130,147 #binding_site pheophytin (Tyr, Glu, Tyr) #status !8predicted\ !$161 #active_site Tyr (tyrosyl radical intermediate) !8#status predicted\ !$190 #active_site His #status predicted\ !$198 #binding_site chlorophyll magnesium (His) (axial !8ligand) #status predicted\ !$215,272 #binding_site iron (His) #status predicted\ !$286 #binding_site chlorophyll (Thr) #status predicted SUMMARY #length 353 #molecular-weight 38950 #checksum 9364 SEQUENCE /// ENTRY S34503 #type complete TITLE photosystem II protein D1 - Euglena gracilis chloroplast ALTERNATE_NAMES photosystem II Q-B protein; thylakoid membrane 32K protein ORGANISM #formal_name chloroplast Euglena gracilis DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS A22883; S34503; S34870 REFERENCE A22883 !$#authors Karabin, G.D.; Farley, M.; Hallick, R.B. !$#journal Nucleic Acids Res. (1984) 12:5801-5812 !$#title Chloroplast gene for Mr 32000 polypeptide of photosystem II !1in Euglena gracilis is interrupted by four introns with !1conserved boundary sequences. !$#cross-references MUID:84272254; PMID:6431398 !$#accession A22883 !'##molecule_type DNA !'##residues 1-345 ##label KAR !'##cross-references EMBL:X00735; NID:g11490; PIDN:CAA25319.1; !1PID:g11491 REFERENCE S34494 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.; Monfort, !1A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#submission submitted to the EMBL Data Library, January 1993 !$#description The complete sequence of the Euglena gracilis chloroplast !1genome (tentative). !$#accession S34503 !'##molecule_type DNA !'##residues 1-345 ##label HAL1 !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50082.1; !1PID:g415738 REFERENCE S34862 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.R.; !1Monfort, A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#journal Nucleic Acids Res. (1993) 21:3537-3544 !$#title Complete sequence of Euglena gracilis chloroplast DNA. !$#cross-references MUID:93347989; PMID:8346031 !$#contents annotation !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene psbA !$#genome chloroplast !$#introns 79/1; 106/3; 299/3; 332/3 CLASSIFICATION #superfamily photosystem II D2 protein KEYWORDS acetylated amino end; chlorophyll; chloroplast; !1chromoprotein; electron transfer; iron; magnesium; !1membrane-associated complex; metalloprotein; phosphoprotein; !1photosynthesis; photosystem II; thylakoid; transmembrane !1protein FEATURE !$2-345 #product photosystem II protein D1 #status predicted !8#label MAT\ !$32-56 #domain transmembrane #status predicted #label TM1\ !$102-137 #domain transmembrane #status predicted #label TM2\ !$143-166 #domain transmembrane #status predicted #label TM3\ !$197-222 #domain transmembrane #status predicted #label TM4\ !$271-291 #domain transmembrane #status predicted #label TM5\ !$127,131,148 #binding_site pheophytin (Tyr, Glu, Tyr) #status !8predicted\ !$162 #active_site Tyr (tyrosyl radical intermediate) !8#status predicted\ !$191 #active_site His #status predicted\ !$199 #binding_site chlorophyll magnesium (His) (axial !8ligand) #status predicted\ !$216,273 #binding_site iron (His) #status predicted\ !$287 #binding_site chlorophyll (Thr) #status predicted SUMMARY #length 345 #molecular-weight 38365 #checksum 8148 SEQUENCE /// ENTRY F2KM1M #type complete TITLE photosystem II protein D1 precursor - Chlamydomonas moewusii chloroplast ALTERNATE_NAMES photosystem II Q-B protein; thylakoid membrane 32K protein ORGANISM #formal_name chloroplast Chlamydomonas moewusii DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS S04279 REFERENCE S04279 !$#authors Turmel, M.; Boulanger, J.; Lemieux, C. !$#journal Nucleic Acids Res. (1989) 17:3875-3887 !$#title Two group I introns with long internal open reading frames !1in the chloroplast psbA gene of Chlamydomonas moewusii. !$#cross-references MUID:89282392; PMID:2660104 !$#accession S04279 !'##molecule_type DNA !'##residues 1-353 ##label TUR !'##cross-references EMBL:X13486; NID:g11369; PIDN:CAA31841.1; !1PID:g11372 GENETICS !$#gene psbA !$#genome chloroplast !$#introns 252/3; 264/1 CLASSIFICATION #superfamily photosystem II D2 protein KEYWORDS acetylated amino end; chlorophyll; chloroplast; !1chromoprotein; electron transfer; iron; magnesium; !1membrane-associated complex; metalloprotein; phosphoprotein; !1photosynthesis; photosystem II; thylakoid; transmembrane !1protein FEATURE !$2-344 #product photosystem II protein D1 #status predicted !8#label MAT\ !$31-55 #domain transmembrane #status predicted #label TM1\ !$101-136 #domain transmembrane #status predicted #label TM2\ !$142-165 #domain transmembrane #status predicted #label TM3\ !$196-221 #domain transmembrane #status predicted #label TM4\ !$270-290 #domain transmembrane #status predicted #label TM5\ !$345-353 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$2 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$2 #modified_site acetylated amino end (Thr) (in mature !8form) #status predicted\ !$126,130,147 #binding_site pheophytin (Tyr, Glu, Tyr) #status !8predicted\ !$161 #active_site Tyr (tyrosyl radical intermediate) !8#status predicted\ !$190 #active_site His #status predicted\ !$198 #binding_site chlorophyll magnesium (His) (axial !8ligand) #status predicted\ !$215,272 #binding_site iron (His) #status predicted\ !$286 #binding_site chlorophyll (Thr) #status predicted SUMMARY #length 353 #molecular-weight 39031 #checksum 8920 SEQUENCE /// ENTRY F2LVD1 #type complete TITLE photosystem II protein D1 precursor - liverwort (Marchantia polymorpha) chloroplast ALTERNATE_NAMES thylakoid membrane 32K protein ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS S01590; A03461 REFERENCE S01567 !$#authors Umesono, K.; Inokuchi, H.; Shiki, Y.; Takeuchi, M.; Chang, !1Z.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Ohyama, K.; Ozeki, !1H. !$#journal J. Mol. Biol. (1988) 203:299-331 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. II. Gene organization of the large !1single copy region from rps'12 to atpB. !$#cross-references MUID:89068686; PMID:2974085 !$#accession S01590 !'##molecule_type DNA !'##residues 1-353 ##label UME !'##cross-references EMBL:X04465; NID:g11640; PIDN:CAA28077.1; !1PID:g11664 REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features GENETICS !$#gene psbA !$#genome chloroplast CLASSIFICATION #superfamily photosystem II D2 protein KEYWORDS acetylated amino end; chlorophyll; chloroplast; !1chromoprotein; electron transfer; iron; magnesium; !1membrane-associated complex; metalloprotein; phosphoprotein; !1photosynthesis; photosystem II; thylakoid; transmembrane !1protein FEATURE !$2-344 #product photosystem II protein D1 #status predicted !8#label MAT\ !$31-55 #domain transmembrane #status predicted #label TM1\ !$101-136 #domain transmembrane #status predicted #label TM2\ !$142-165 #domain transmembrane #status predicted #label TM3\ !$196-221 #domain transmembrane #status predicted #label TM4\ !$270-290 #domain transmembrane #status predicted #label TM5\ !$345-353 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$2 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$2 #modified_site acetylated amino end (Thr) (in mature !8form) #status predicted\ !$126,130,147 #binding_site pheophytin (Tyr, Glu, Tyr) #status !8predicted\ !$161 #active_site Tyr (tyrosyl radical intermediate) !8#status predicted\ !$190 #active_site His #status predicted\ !$198 #binding_site chlorophyll magnesium (His) (axial !8ligand) #status predicted\ !$215,272 #binding_site iron (His) #status predicted\ !$286 #binding_site chlorophyll (Thr) #status predicted SUMMARY #length 353 #molecular-weight 38765 #checksum 9635 SEQUENCE /// ENTRY F2KTD1 #type complete TITLE photosystem II protein D1 precursor - Cyanophora paradoxa cyanelle ALTERNATE_NAMES thylakoid membrane 32K protein ORGANISM #formal_name cyanelle Cyanophora paradoxa DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS S05961; T06926 REFERENCE S05961 !$#authors Janssen, I.; Jakowitsch, J.; Michalowski, C.B.; Bohnert, !1H.J.; Loeffelhardt, W. !$#journal Curr. Genet. (1989) 15:335-340 !$#title Evolutionary relationship of psbA genes from cyanobacteria, !1cyanelles and plastids. !$#cross-references MUID:90003351; PMID:2507175 !$#accession S05961 !'##molecule_type DNA !'##residues 1-360 ##label JAN !'##cross-references EMBL:X14667; NID:g11392; PIDN:CAA32795.1; !1PID:g11393 REFERENCE Z15840 !$#authors Stirewalt, V.L.; Michalowski, C.B.; Luffelhardt, W.; !1Bohnert, H.J.; Bryant, D.A. !$#submission submitted to the EMBL Data Library, July 1995 !$#description Nucleotide sequence of the cyanelle genome from Cyanophora !1paradoxa. !$#accession T06926 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-232,'A',234-360 ##label STI !'##cross-references EMBL:U30821; NID:g1016083; PIDN:AAA81269.1; !1PID:g1016182 !'##experimental_source strain Pringsheim LB555 GENETICS !$#gene psbA !$#genome cyanelle CLASSIFICATION #superfamily photosystem II D2 protein KEYWORDS acetylated amino end; chlorophyll; chromoprotein; cyanelle; !1electron transfer; iron; magnesium; membrane-associated !1complex; metalloprotein; phosphoprotein; photosynthesis; !1photosystem II; thylakoid; transmembrane protein FEATURE !$2-351 #product photosystem II protein D1 #status predicted !8#label MAT\ !$31-55 #domain transmembrane #status predicted #label TM1\ !$101-136 #domain transmembrane #status predicted #label TM2\ !$142-165 #domain transmembrane #status predicted #label TM3\ !$196-221 #domain transmembrane #status predicted #label TM4\ !$270-290 #domain transmembrane #status predicted #label TM5\ !$352-360 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$2 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$2 #modified_site acetylated amino end (Thr) (in mature !8form) #status predicted\ !$126,130,147 #binding_site pheophytin (Tyr, Glu, Tyr) #status !8predicted\ !$161 #active_site Tyr (tyrosyl radical intermediate) !8#status predicted\ !$190 #active_site His #status predicted\ !$198 #binding_site chlorophyll magnesium (His) (axial !8ligand) #status predicted\ !$215,272 #binding_site iron (His) #status predicted\ !$286 #binding_site chlorophyll (Thr) #status predicted SUMMARY #length 360 #molecular-weight 39528 #checksum 7549 SEQUENCE /// ENTRY F2AI17 #type complete TITLE photosystem II protein D1 precursor - Anabaena sp. (strain PCC 7120) ORGANISM #formal_name Anabaena sp. #variety PCC 7120 DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS S11849 REFERENCE S11849 !$#authors Vrba, J.M.; Curtis, S.E. !$#journal Plant Mol. Biol. (1990) 14:81-92 !$#title Characterization of a four-member psbA gene family from the !1cyanobacterium Anabaena PCC 7120. !$#cross-references MUID:91322491; PMID:2129283 !$#accession S11849 !'##molecule_type DNA !'##residues 1-360 ##label VRB !'##cross-references GB:U21332; GB:S47092; NID:g709795; PIDN:AAA63703.1; !1PID:g709796 GENETICS !$#gene psbA CLASSIFICATION #superfamily photosystem II D2 protein KEYWORDS acetylated amino end; chlorophyll; chromoprotein; electron !1transfer; iron; magnesium; membrane-associated complex; !1metalloprotein; phosphoprotein; photosynthesis; photosystem !1II; thylakoid; transmembrane protein FEATURE !$2-351 #product photosystem II protein D1 #status predicted !8#label MAT\ !$31-55 #domain transmembrane #status predicted #label TM1\ !$101-136 #domain transmembrane #status predicted #label TM2\ !$142-165 #domain transmembrane #status predicted #label TM3\ !$196-221 #domain transmembrane #status predicted #label TM4\ !$270-290 #domain transmembrane #status predicted #label TM5\ !$352-360 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$2 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$2 #modified_site acetylated amino end (Thr) (in mature !8form) #status predicted\ !$161 #active_site Tyr (tyrosyl radical intermediate) !8#status predicted\ !$190 #active_site His #status predicted\ !$198 #binding_site chlorophyll magnesium (His) (axial !8ligand) #status predicted\ !$215,272 #binding_site iron (His) #status predicted\ !$286 #binding_site chlorophyll (Thr) #status predicted SUMMARY #length 360 #molecular-weight 39715 #checksum 5664 SEQUENCE /// ENTRY F2AI1Z #type complete TITLE photosystem II protein D1 precursor - Anabaena azollae ORGANISM #formal_name Anabaena azollae DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS S18959 REFERENCE S18959 !$#authors Gebhardt, J.S.; Nierzwicki-Bauer, S.A. !$#submission submitted to the EMBL Data Library, January 1992 !$#description Characterization of psbA gene family expression in symbiotic !1Anabaena azollae. !$#accession S18959 !'##molecule_type DNA !'##residues 1-360 ##label GEB !'##cross-references EMBL:X64174; NID:g38650; PIDN:CAA45515.1; !1PID:g38651 GENETICS !$#gene psbA CLASSIFICATION #superfamily photosystem II D2 protein KEYWORDS acetylated amino end; chlorophyll; chromoprotein; electron !1transfer; iron; magnesium; membrane-associated complex; !1metalloprotein; phosphoprotein; photosynthesis; photosystem !1II; thylakoid; transmembrane protein FEATURE !$31-55 #domain transmembrane #status predicted #label TM1\ !$101-136 #domain transmembrane #status predicted #label TM2\ !$142-165 #domain transmembrane #status predicted #label TM3\ !$196-221 #domain transmembrane #status predicted #label TM4\ !$270-290 #domain transmembrane #status predicted #label TM5\ !$352-360 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$2 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$2 #modified_site acetylated amino end (Thr) (in mature !8form) #status predicted\ !$161 #active_site Tyr (tyrosyl radical intermediate) !8#status predicted\ !$190 #active_site His #status predicted\ !$198 #binding_site chlorophyll magnesium (His) (axial !8ligand) #status predicted\ !$215,272 #binding_site iron (His) #status predicted\ !$286 #binding_site chlorophyll (Thr) #status predicted SUMMARY #length 360 #molecular-weight 39540 #checksum 6791 SEQUENCE /// ENTRY F2YB16 #type complete TITLE photosystem II protein D1.II precursor - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES hypothetical protein slr1311; QB-binding protein ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jun-2000 ACCESSIONS S13112; S04364; S74434; S75669 REFERENCE S13112 !$#authors Metz, J.; Nixon, P.; Diner, B. !$#journal Nucleic Acids Res. (1990) 18:6715 !$#title Nucleotide sequence of the psbA3 gene from the !1cyanobacterium Synechocystis PCC 6803. !$#cross-references MUID:91067488; PMID:2123543 !$#accession S13112 !'##molecule_type DNA !'##residues 1-360 ##label MET !'##cross-references EMBL:X56000; NID:g48060; PIDN:CAA39472.1; !1PID:g48061 !'##experimental_source PCC 6803 REFERENCE S04364 !$#authors Ravnikar, P.D.; Debus, R.; Sevrinck, J.; Saetaert, P.; !1McIntosh, L. !$#journal Nucleic Acids Res. (1989) 17:3991 !$#title Nucleotide sequence of a second psbA gene from the !1unicellular cyanobacterium Synechocystis 6803. !$#cross-references MUID:89282415; PMID:2499875 !$#accession S04364 !'##molecule_type DNA !'##residues 1-360 ##label RAV !'##cross-references EMBL:X13547; NID:g48049; PIDN:CAA31899.1; !1PID:g48050 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74434 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-360 ##label KAN !'##cross-references EMBL:D90899; GB:AB001339; NID:g1651650; !1PIDN:BAA16586.1; PID:g1651658 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 !$#accession S75669 !'##molecule_type DNA !'##residues 1-360 ##label KA2 !'##cross-references EMBL:D90912; GB:AB001339; NID:g1653228; !1PIDN:BAA18230.1; PID:g1653315 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene psbA3; psbA2 CLASSIFICATION #superfamily photosystem II D2 protein KEYWORDS acetylated amino end; chlorophyll; chromoprotein; electron !1transfer; iron; magnesium; membrane-associated complex; !1metalloprotein; phosphoprotein; photosynthesis; photosystem !1II; thylakoid; transmembrane protein FEATURE !$31-55 #domain transmembrane #status predicted #label TM1\ !$101-136 #domain transmembrane #status predicted #label TM2\ !$142-165 #domain transmembrane #status predicted #label TM3\ !$196-221 #domain transmembrane #status predicted #label TM4\ !$270-290 #domain transmembrane #status predicted #label TM5\ !$352-360 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$2 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$2 #modified_site acetylated amino end (Thr) (in mature !8form) #status predicted\ !$161 #active_site Tyr (tyrosyl radical intermediate) !8#status predicted\ !$190 #active_site His #status predicted\ !$198 #binding_site chlorophyll magnesium (His) (axial !8ligand) #status predicted\ !$215,272 #binding_site iron (His) #status predicted\ !$286 #binding_site chlorophyll (Thr) #status predicted SUMMARY #length 360 #molecular-weight 39721 #checksum 9517 SEQUENCE /// ENTRY F2YB17 #type complete TITLE photosystem II protein D1 precursor - Synechocystis sp. (strain PCC 6714) ORGANISM #formal_name Synechocystis sp. DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS S07461 REFERENCE S07461 !$#authors Ajlani, G.; Kirilovsky, D.; Picaud, M.; Astier, C. !$#journal Plant Mol. Biol. (1989) 13:469-479 !$#title Molecular analysis of psbA mutations responsible for various !1herbicide resistance phenotypes in Synechocystis 6714. !$#cross-references MUID:91370829; PMID:2518834 !$#accession S07461 !'##molecule_type DNA !'##residues 1-360 ##label AJL !'##cross-references EMBL:X15514; NID:g48062; PIDN:CAA33538.1; !1PID:g48063 !'##note the authors translated the codon CAA for residue 118 as His and !1CAA for residue 348 as Glu GENETICS !$#gene psbA1 CLASSIFICATION #superfamily photosystem II D2 protein KEYWORDS acetylated amino end; chlorophyll; chromoprotein; electron !1transfer; iron; magnesium; membrane-associated complex; !1metalloprotein; phosphoprotein; photosynthesis; photosystem !1II; thylakoid; transmembrane protein FEATURE !$31-55 #domain transmembrane #status predicted #label TM1\ !$101-136 #domain transmembrane #status predicted #label TM2\ !$142-165 #domain transmembrane #status predicted #label TM3\ !$196-221 #domain transmembrane #status predicted #label TM4\ !$270-290 #domain transmembrane #status predicted #label TM5\ !$352-360 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$2 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$2 #modified_site acetylated amino end (Thr) (in mature !8form) #status predicted\ !$161 #active_site Tyr (tyrosyl radical intermediate) !8#status predicted\ !$190 #active_site His #status predicted\ !$198 #binding_site chlorophyll magnesium (His) (axial !8ligand) #status predicted\ !$215,272 #binding_site iron (His) #status predicted\ !$286 #binding_site chlorophyll (Thr) #status predicted SUMMARY #length 360 #molecular-weight 39811 #checksum 25 SEQUENCE /// ENTRY F2YB13 #type complete TITLE photosystem II protein D1 precursor - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES QB binding protein ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 31-Mar-1993 #sequence_revision 01-May-1998 #text_change 16-Jun-2000 ACCESSIONS S76917; S06319 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76917 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-360 ##label KAN !'##cross-references EMBL:D90917; GB:AB001339; NID:g1653836; !1PIDN:BAA18829.1; PID:g1653919 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 REFERENCE S06319 !$#authors Osiewacz, H.D.; McIntosh, L. !$#journal Nucleic Acids Res. (1987) 15:10585 !$#title Nucleotide sequence of a member of the psbA multigene family !1from the unicellular cyanobacterium Synechocystis 6803. !$#cross-references MUID:88096589; PMID:3122184 !$#accession S06319 !'##molecule_type DNA !'##residues 1-89,'A',91-114,'N',116-272,'S',274-360 ##label OSI !'##cross-references GB:Y00885; NID:g47428; PIDN:CAA68778.1; PID:g47429 !'##note the authors translated the codon GCC for residue 90 as Gly, AAT !1for residue 115 as Ile, TTG for residue 193 as Ile, and TCC !1for residue 273 as Phe GENETICS !$#gene psbA-1 CLASSIFICATION #superfamily photosystem II D2 protein KEYWORDS acetylated amino end; chlorophyll; chromoprotein; electron !1transfer; iron; magnesium; membrane-associated complex; !1metalloprotein; phosphoprotein; photosynthesis; photosystem !1II; thylakoid; transmembrane protein FEATURE !$2-351 #product photosystem II protein D1 #status predicted !8#label MAT\ !$31-55 #domain transmembrane #status predicted #label TM1\ !$101-136 #domain transmembrane #status predicted #label TM2\ !$142-165 #domain transmembrane #status predicted #label TM3\ !$196-221 #domain transmembrane #status predicted #label TM4\ !$270-290 #domain transmembrane #status predicted #label TM5\ !$352-360 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$2 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$2 #modified_site acetylated amino end (Thr) (in mature !8form) #status predicted\ !$161 #active_site Tyr (tyrosyl radical intermediate) !8#status predicted\ !$190 #active_site His #status predicted\ !$198 #binding_site chlorophyll magnesium (His) (axial !8ligand) #status predicted\ !$215,272 #binding_site iron (His) #status predicted SUMMARY #length 360 #molecular-weight 39650 #checksum 7285 SEQUENCE /// ENTRY F2MWD1 #type complete TITLE photosystem II protein D1 precursor - Prochlorothrix hollandica ALTERNATE_NAMES 32K thylakoid protein ORGANISM #formal_name Prochlorothrix hollandica DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS S02171; S07994 REFERENCE S02171 !$#authors Morden, C.W.; Golden, S.S. !$#journal Nature (1989) 337:382-385 !$#title psbA genes indicate common ancestry of prochlorophytes and !1chloroplasts. !$#cross-references MUID:89097313; PMID:2643058 !$#accession S02171 !'##molecule_type DNA !'##residues 1-353 ##label MOR !'##cross-references EMBL:X14523; NID:g45535; PIDN:CAA32665.1; !1PID:g45536 GENETICS !$#gene psbAI; psbAII CLASSIFICATION #superfamily photosystem II D2 protein KEYWORDS acetylated amino end; chlorophyll; chromoprotein; electron !1transfer; iron; magnesium; membrane-associated complex; !1metalloprotein; phosphoprotein; photosynthesis; photosystem !1II; thylakoid; transmembrane protein FEATURE !$2-344 #product photosystem II protein D1 #status predicted !8#label MAT\ !$31-55 #domain transmembrane #status predicted #label TM1\ !$101-136 #domain transmembrane #status predicted #label TM2\ !$142-165 #domain transmembrane #status predicted #label TM3\ !$196-221 #domain transmembrane #status predicted #label TM4\ !$270-290 #domain transmembrane #status predicted #label TM5\ !$345-353 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$2 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$2 #modified_site acetylated amino end (Thr) (in mature !8form) #status predicted\ !$126,130,147 #binding_site pheophytin (Tyr, Glu, Tyr) #status !8predicted\ !$161 #active_site Tyr (tyrosyl radical intermediate) !8#status predicted\ !$190 #active_site His #status predicted\ !$198 #binding_site chlorophyll magnesium (His) (axial !8ligand) #status predicted\ !$215,272 #binding_site iron (His) #status predicted\ !$286 #binding_site chlorophyll (Thr) #status predicted SUMMARY #length 353 #molecular-weight 39153 #checksum 9150 SEQUENCE /// ENTRY F2NTD2 #type complete TITLE photosystem II protein D2 - common tobacco chloroplast ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 03-Mar-2000 ACCESSIONS A03462 REFERENCE A00149 !$#authors Sugiura, M. !$#submission submitted to the EMBL Data Library, August 1986 !$#accession A03462 !'##molecule_type DNA !'##residues 1-353 ##label SUG !'##experimental_source cv. Bright Yellow 4 REFERENCE A38013 !$#authors Shinozaki, K.; Ohme, M.; Tanaka, M.; Wakasugi, T.; !1Hayashida, N.; Matsubayashi, T.; Zaita, N.; Chunwongse, J.; !1Obokata, J.; Yamaguchi-Shinozaki, K.; Ohto, C.; Torazawa, !1K.; Meng, B.Y.; Sugita, M.; Deno, H.; Kamogashira, T.; !1Yamada, K.; Kusuda, J.; Takaiwa, F.; Kato, A.; Tohdoh, N.; !1Shimada, H.; Sugiura, M. !$#journal EMBO J. (1986) 5:2043-2049 !$#title The complete nucleotide sequence of the tobacco chloroplast !1genome: its gene organization and expression. !$#contents annotation; gene organization, sites, features GENETICS !$#gene psbD !$#genome chloroplast CLASSIFICATION #superfamily photosystem II D2 protein KEYWORDS acetylated amino end; chlorophyll; chloroplast; !1chromoprotein; electron transfer; iron; magnesium; !1membrane-associated complex; metalloprotein; phosphoprotein; !1photosynthesis; photosystem II; thylakoid; transmembrane !1protein FEATURE !$2-353 #product photosystem II protein D2 #status predicted !8#label MAT\ !$31-55 #domain transmembrane #status predicted #label TM1\ !$110-135 #domain transmembrane #status predicted #label TM2\ !$142-165 #domain transmembrane #status predicted #label TM3\ !$196-221 #domain transmembrane #status predicted #label TM4\ !$265-318 #domain transmembrane #status predicted #label TM5\ !$2 #modified_site acetylated amino end (Thr) (in mature !8form) #status predicted\ !$2 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$161 #active_site Tyr (tyrosyl radical intermediate) !8#status predicted\ !$190 #active_site His #status predicted\ !$198 #binding_site chlorophyll magnesium (His) (axial !8ligand) #status predicted\ !$215,269 #binding_site iron (His) #status predicted\ !$283 #binding_site chlorophyll (Ser) #status predicted SUMMARY #length 353 #molecular-weight 39535 #checksum 6059 SEQUENCE /// ENTRY F2RZD2 #type complete TITLE photosystem II protein D2 - rice chloroplast ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 03-Mar-2000 ACCESSIONS JQ0206; S05086 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0206 !'##molecule_type DNA !'##residues 1-353 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05086 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-353 ##label HIR !'##cross-references EMBL:X15901; NID:g11957; PIDN:CAA34013.1; !1PID:g11964 !'##experimental_source cv. Nihonbare !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1989 GENETICS !$#gene psbD !$#genome chloroplast CLASSIFICATION #superfamily photosystem II D2 protein KEYWORDS acetylated amino end; chlorophyll; chloroplast; !1chromoprotein; electron transfer; iron; magnesium; !1membrane-associated complex; metalloprotein; phosphoprotein; !1photosynthesis; photosystem II; thylakoid; transmembrane !1protein FEATURE !$2-353 #product photosystem II protein D2 #status predicted !8#label MAT\ !$31-55 #domain transmembrane #status predicted #label TM1\ !$110-135 #domain transmembrane #status predicted #label TM2\ !$142-165 #domain transmembrane #status predicted #label TM3\ !$196-221 #domain transmembrane #status predicted #label TM4\ !$265-318 #domain transmembrane #status predicted #label TM5\ !$2 #modified_site acetylated amino end (Thr) (in mature !8form) #status predicted\ !$2 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$161 #active_site Tyr (tyrosyl radical intermediate) !8#status predicted\ !$190 #active_site His #status predicted\ !$198 #binding_site chlorophyll magnesium (His) (axial !8ligand) #status predicted\ !$215,269 #binding_site iron (His) #status predicted\ !$283 #binding_site chlorophyll (Ser) #status predicted SUMMARY #length 353 #molecular-weight 39573 #checksum 6144 SEQUENCE /// ENTRY F2LVD2 #type complete TITLE photosystem II protein D2 - liverwort (Marchantia polymorpha) chloroplast ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 03-Mar-2000 ACCESSIONS A03463; S01593 REFERENCE A00150 !$#authors Ohyama, K. !$#submission submitted to the EMBL Data Library, October 1986 !$#accession A03463 !'##molecule_type DNA !'##residues 1-353 ##label OHY REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features REFERENCE S01567 !$#authors Umesono, K.; Inokuchi, H.; Shiki, Y.; Takeuchi, M.; Chang, !1Z.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Ohyama, K.; Ozeki, !1H. !$#journal J. Mol. Biol. (1988) 203:299-331 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. II. Gene organization of the large !1single copy region from rps'12 to atpB. !$#cross-references MUID:89068686; PMID:2974085 !$#accession S01593 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-353 ##label UME !'##cross-references GB:X04465; GB:Y00686; NID:g11640; PIDN:CAA28080.1; !1PID:g11667 GENETICS !$#gene psbD !$#genome chloroplast CLASSIFICATION #superfamily photosystem II D2 protein KEYWORDS acetylated amino end; chlorophyll; chloroplast; !1chromoprotein; electron transfer; iron; magnesium; !1membrane-associated complex; metalloprotein; phosphoprotein; !1photosynthesis; photosystem II; thylakoid; transmembrane !1protein FEATURE !$2-353 #product photosystem II protein D2 #status predicted !8#label MAT\ !$31-55 #domain transmembrane #status predicted #label TM1\ !$110-135 #domain transmembrane #status predicted #label TM2\ !$142-165 #domain transmembrane #status predicted #label TM3\ !$196-221 #domain transmembrane #status predicted #label TM4\ !$265-318 #domain transmembrane #status predicted #label TM5\ !$2 #modified_site acetylated amino end (Thr) (in mature !8form) #status predicted\ !$2 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$161 #active_site Tyr (tyrosyl radical intermediate) !8#status predicted\ !$190 #active_site His #status predicted\ !$198 #binding_site chlorophyll magnesium (His) (axial !8ligand) #status predicted\ !$215,269 #binding_site iron (His) #status predicted\ !$283 #binding_site chlorophyll (Ser) #status predicted SUMMARY #length 353 #molecular-weight 39389 #checksum 6796 SEQUENCE /// ENTRY F2SPD2 #type complete TITLE photosystem II protein D2 [validated] - spinach chloroplast ORGANISM #formal_name chloroplast Spinacia oleracea #common_name spinach DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 15-Sep-2000 ACCESSIONS A23038; T08997; S00432; S09185; S48683 REFERENCE A93547 !$#authors Holschuh, K.; Bottomley, W.; Whitfeld, P.R. !$#journal Nucleic Acids Res. (1984) 12:8819-8834 !$#title Structure of the spinach chloroplast genes for the D2 and 44 !1kd reaction-centre proteins of photosystem II and for !1tRNA-Ser (UGA). !$#cross-references MUID:85087902; PMID:6096808 !$#accession A23038 !'##molecule_type DNA !'##residues 1-353 ##label HOL !'##cross-references GB:X01724; GB:M12028; GB:M16873; GB:M27308; !1NID:g12279; PIDN:CAA25863.1; PID:g12280 !$#accession T08997 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-353 ##label HO2 !'##cross-references EMBL:M27308; NID:g12279; PIDN:CAA25863.1; !1PID:g12280 REFERENCE S00416 !$#authors Alt, J.; Morris, J.; Westhoff, P.; Herrmann, R.G. !$#journal Curr. Genet. (1984) 8:597-606 !$#title Nucleotide sequence of the clustered genes for the 44kd !1chlorophyll a apoprotein and the "32kd"-like protein of the !1photosystem II reaction center in the spinach plastid !1chromosome. !$#accession S00432 !'##molecule_type DNA !'##residues 1-353 ##label ALT !'##cross-references EMBL:M36833; NID:g343360; PIDN:AAA84630.1; !1PID:g552887 !'##note the sequence from Fig. 3 is inconsistent with that from Fig. 2 !1in having 329-Gly and 330-Trp REFERENCE A60682 !$#authors Takahashi, Y.; Nakane, H.; Kojima, H.; Satoh, K. !$#journal Plant Cell Physiol. (1990) 31:273-280 !$#title Chromatographic purification and determination of the !1carboxy-terminal sequences of photosystem II reaction center !1proteins, D1 and D2. !$#contents annotation !$#note the carboxyl-terminal residue was determined; this protein !1is not processed at the carboxyl end REFERENCE S09185 !$#authors Michel, H.; Hunt, D.F.; Shabanowitz, J.; Bennett, J. !$#journal J. Biol. Chem. (1988) 263:1123-1130 !$#title Tandem mass spectrometry reveals that three photosystem II !1proteins of spinach chloroplasts contain !1N-acetyl-O-phosphothreonine at their NH(2) termini. !$#cross-references MUID:88087237; PMID:3121625 !$#accession S09185 !'##molecule_type protein !'##residues 2-7 ##label MIC REFERENCE A65447 !$#authors Svensson, B.; Etchebest, C.; Tuffery, P.; Van Kan, P.; !1Smith, J.; Styring, S. !$#submission submitted to the Brookhaven Protein Data Bank, October 1996 !$#cross-references PDB:1DOP !$#contents annotation; theoretical model, residues 106-224;263-294 REFERENCE A58807 !$#authors Svensson, B.; Etchebest, C.; Tuffery, P.; van Kan, P.; !1Smith, J.; Styring, S. !$#journal Biochemistry (1996) 35:14486-14502 !$#title A model for the photosystem II reaction center core !1including the structure of the primary donor P680. !$#cross-references MUID:97085405; PMID:8931545 !$#contents annotation; theoretical model REFERENCE S48682 !$#authors Tomo, T.; Satoh, K. !$#journal FEBS Lett. (1994) 351:27-30 !$#title Nearest neighbor analysis of D1 and D2 subunits in the !1photosystem II reaction center using a bifunctional !1cross-linker, hexamethylene diisocyanate. !$#cross-references MUID:94357272; PMID:8076687 !$#accession S48683 !'##molecule_type protein !'##residues 2-19;20-38;122-127;106-121, !1128-131;192-199;1;201-224;241-247;248-272;273-282;283-304; !1322-330;331-353 ##label TOM GENETICS !$#gene psbD !$#genome chloroplast CLASSIFICATION #superfamily photosystem II D2 protein KEYWORDS acetylated amino end; chlorophyll; chloroplast; !1chromoprotein; electron transfer; iron; magnesium; !1membrane-associated complex; metalloprotein; phosphoprotein; !1photosynthesis; photosystem II; thylakoid; transmembrane !1protein FEATURE !$2-353 #product photosystem II protein D2 #status !8experimental #label MAT\ !$31-55 #domain transmembrane #status predicted #label TM1\ !$110-135 #domain transmembrane #status predicted #label TM2\ !$142-165 #domain transmembrane #status predicted #label TM3\ !$196-221 #domain transmembrane #status predicted #label TM4\ !$265-288 #domain transmembrane #status predicted #label TM5\ !$2 #modified_site acetylated amino end (Thr) (in mature !8form) #status experimental\ !$2 #binding_site phosphate (Thr) (covalent) #status !8experimental\ !$161 #active_site Tyr (tyrosyl radical intermediate) !8#status predicted\ !$190 #active_site His #status predicted\ !$198 #binding_site chlorophyll magnesium (His) (axial !8ligand) #status predicted\ !$215,269 #binding_site iron (His) #status predicted\ !$283 #binding_site chlorophyll (Ser) #status predicted SUMMARY #length 353 #molecular-weight 39507 #checksum 4678 SEQUENCE /// ENTRY F2PMD2 #type complete TITLE photosystem II protein D2 - garden pea chloroplast ORGANISM #formal_name chloroplast Pisum sativum #common_name garden pea DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 03-Mar-2000 ACCESSIONS A26059 REFERENCE A26059 !$#authors Rasmussen, O.F.; Bookjans, G.; Stummann, B.M.; Henningsen, !1K.W. !$#journal Plant Mol. Biol. (1984) 3:191-199 !$#title Localization and nucleotide sequence of the gene for the !1membrane polypeptide D2 from pea chloroplast DNA. !$#accession A26059 !'##molecule_type DNA !'##residues 1-353 ##label RAS GENETICS !$#gene psbD !$#genome chloroplast CLASSIFICATION #superfamily photosystem II D2 protein KEYWORDS acetylated amino end; chlorophyll; chloroplast; !1chromoprotein; electron transfer; iron; magnesium; !1membrane-associated complex; metalloprotein; phosphoprotein; !1photosynthesis; photosystem II; thylakoid; transmembrane !1protein FEATURE !$2-353 #product photosystem II protein D2 #status predicted !8#label MAT\ !$31-55 #domain transmembrane #status predicted #label TM1\ !$110-135 #domain transmembrane #status predicted #label TM2\ !$142-165 #domain transmembrane #status predicted #label TM3\ !$196-221 #domain transmembrane #status predicted #label TM4\ !$265-318 #domain transmembrane #status predicted #label TM5\ !$2 #modified_site acetylated amino end (Thr) (in mature !8form) #status predicted\ !$2 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$161 #active_site Tyr (tyrosyl radical intermediate) !8#status predicted\ !$190 #active_site His #status predicted\ !$198 #binding_site chlorophyll magnesium (His) (axial !8ligand) #status predicted\ !$215,269 #binding_site iron (His) #status predicted\ !$283 #binding_site chlorophyll (Ser) #status predicted SUMMARY #length 353 #molecular-weight 39530 #checksum 7366 SEQUENCE /// ENTRY F2KKD2 #type complete TITLE photosystem II protein D2 - red alga (Cyanidium caldarium) chloroplast ORGANISM #formal_name chloroplast Cyanidium caldarium DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 03-Mar-2000 ACCESSIONS S20855; S25085 REFERENCE S20854 !$#authors Kessler, U.; Maid, U.; Zetsche, K. !$#journal Plant Mol. Biol. (1992) 18:777-780 !$#title An equivalent to bacterial ompR genes is encoded on the !1plastid genome of red algae. !$#cross-references MUID:92216053; PMID:1558950 !$#accession S20855 !'##status translation not shown !'##molecule_type DNA !'##residues 1-351 ##label KES !'##cross-references EMBL:X62578; NID:g11278; PIDN:CAA44459.1; !1PID:g11280 REFERENCE S25084 !$#authors Maid, U.; Zetsche, K. !$#journal Plant Mol. Biol. (1992) 19:1001-1010 !$#title A 16 kb small single-copy region separates the plastid DNA !1inverted repeat of the unicellular red alga Cyanidium !1caldarium: physical mapping of the IR-flanking regions and !1nucleotide sequences of the psbD-psbC, rps16, 5S rRNA and !1rpl21 genes. !$#cross-references MUID:92379254; PMID:1511125 !$#accession S25085 !'##molecule_type DNA !'##residues 1-351 ##label MAI !'##cross-references EMBL:X62578; NID:g11278; PIDN:CAA44459.1; !1PID:g11280 GENETICS !$#gene psbD !$#genome chloroplast CLASSIFICATION #superfamily photosystem II D2 protein KEYWORDS acetylated amino end; chlorophyll; chloroplast; !1chromoprotein; electron transfer; iron; magnesium; !1membrane-associated complex; metalloprotein; phosphoprotein; !1photosynthesis; photosystem II; thylakoid; transmembrane !1protein FEATURE !$2-351 #product photosystem II protein D2 #status predicted !8#label MAT\ !$29-53 #domain transmembrane #status predicted #label TM1\ !$108-133 #domain transmembrane #status predicted #label TM2\ !$140-163 #domain transmembrane #status predicted #label TM3\ !$194-219 #domain transmembrane #status predicted #label TM4\ !$263-316 #domain transmembrane #status predicted #label TM5\ !$2 #modified_site acetylated amino end (Thr) (in mature !8form) #status predicted\ !$2 #binding_site phosphate (Thr) (covalent) #status !8predicted\ !$159 #active_site Tyr (tyrosyl radical intermediate) !8#status predicted\ !$188 #active_site His #status predicted\ !$196 #binding_site chlorophyll magnesium (His) (axial !8ligand) #status predicted\ !$213,267 #binding_site iron (His) #status predicted\ !$281 #binding_site chlorophyll (Ser) #status predicted SUMMARY #length 351 #molecular-weight 39346 #checksum 6165 SEQUENCE /// ENTRY A1NTP7 #type complete TITLE photosystem I P700 apoprotein A1 - common tobacco chloroplast ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 17-Feb-1995 ACCESSIONS A03464 REFERENCE A00149 !$#authors Sugiura, M. !$#submission submitted to the EMBL Data Library, August 1986 !$#accession A03464 !'##molecule_type DNA !'##residues 1-750 ##label SUG !'##experimental_source cv. Bright Yellow 4 REFERENCE A38013 !$#authors Shinozaki, K.; Ohme, M.; Tanaka, M.; Wakasugi, T.; !1Hayashida, N.; Matsubayashi, T.; Zaita, N.; Chunwongse, J.; !1Obokata, J.; Yamaguchi-Shinozaki, K.; Ohto, C.; Torazawa, !1K.; Meng, B.Y.; Sugita, M.; Deno, H.; Kamogashira, T.; !1Yamada, K.; Kusuda, J.; Takaiwa, F.; Kato, A.; Tohdoh, N.; !1Shimada, H.; Sugiura, M. !$#journal EMBO J. (1986) 5:2043-2049 !$#title The complete nucleotide sequence of the tobacco chloroplast !1genome: its gene organization and expression. !$#contents annotation; gene organization, sites, features COMMENT This is one of the specific proteins associated with !1chlorophyll a of the P700 complex, which is considered the !1reaction center of photosystem I in the chloroplast. P700 !1transfers electrons supplied by photosystem II to !1Z-substance (an iron-sulfur protein), which in turn reduces !1NADP to NADPH via a complex electron transfer system that !1includes chloroplast ferredoxin and other iron-sulfur !1proteins. GENETICS !$#gene psaA !$#genome chloroplast CLASSIFICATION #superfamily photosystem I P700 apoprotein KEYWORDS chloroplast; electron transfer; membrane protein; !1photosynthesis; photosystem I; thylakoid SUMMARY #length 750 #molecular-weight 82991 #checksum 5816 SEQUENCE /// ENTRY A1RZP7 #type complete TITLE photosystem I P700 apoprotein A1 - rice chloroplast ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS JQ0223; S05103 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0223 !'##molecule_type DNA !'##residues 1-750 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05103 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-750 ##label HIR !'##cross-references EMBL:X15901; NID:g11957; PIDN:CAA33996.1; !1PID:g11982 !'##experimental_source cv. Nihonbare GENETICS !$#gene psaA !$#map_position CP41250-38998 !$#genome chloroplast CLASSIFICATION #superfamily photosystem I P700 apoprotein KEYWORDS chloroplast; electron transfer; membrane protein; !1photosynthesis; photosystem I; thylakoid SUMMARY #length 750 #molecular-weight 83384 #checksum 7876 SEQUENCE /// ENTRY A1LVP7 #type complete TITLE photosystem I P700 apoprotein A1 - liverwort (Marchantia polymorpha) chloroplast ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 16-Jul-1999 ACCESSIONS A03465; S01604 REFERENCE A00150 !$#authors Ohyama, K. !$#submission submitted to the EMBL Data Library, October 1986 !$#accession A03465 !'##molecule_type DNA !'##residues 1-750 ##label OHY REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features REFERENCE S01567 !$#authors Umesono, K.; Inokuchi, H.; Shiki, Y.; Takeuchi, M.; Chang, !1Z.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Ohyama, K.; Ozeki, !1H. !$#journal J. Mol. Biol. (1988) 203:299-331 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. II. Gene organization of the large !1single copy region from rps'12 to atpB. !$#cross-references MUID:89068686; PMID:2974085 !$#accession S01604 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-750 ##label UME !'##cross-references GB:X04465; GB:Y00686; NID:g11640; PIDN:CAA28085.1; !1PID:g11672 COMMENT This is one of the specific proteins associated with !1chlorophyll a of the P700 complex, which is considered the !1reaction center of photosystem I in the chloroplast. P700 !1transfers electrons supplied by photosystem II to !1Z-substance (an iron-sulfur protein), which in turn reduces !1NADP to NADPH via a complex electron transfer system that !1includes chloroplast ferredoxin and other iron-sulfur !1proteins. GENETICS !$#gene psaA !$#genome chloroplast CLASSIFICATION #superfamily photosystem I P700 apoprotein KEYWORDS chloroplast; electron transfer; membrane protein; !1photosynthesis; photosystem I; thylakoid SUMMARY #length 750 #molecular-weight 83213 #checksum 8399 SEQUENCE /// ENTRY S20922 #type complete TITLE photosystem I protein A1 - Synechococcus sp. ALTERNATE_NAMES photosystem I core protein A ORGANISM #formal_name Synechococcus sp. DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jun-2000 ACCESSIONS S20922; JQ1115; S19174 REFERENCE S20922 !$#authors Shimizu, T.; Hiyama, T.; Ikeuchi, M.; Inoue, Y. !$#journal Plant Mol. Biol. (1992) 18:785-791 !$#title Nucleotide sequences of the psaA and psaB genes encoding the !1photosystem I core proteins from the thermophilic !1cyanobacterium Synechococcus vulcanus. !$#cross-references MUID:92216055; PMID:1558952 !$#accession S20922 !'##molecule_type DNA !'##residues 1-755 ##label SHI1 !'##cross-references EMBL:D10986; NID:g217127; PIDN:BAA01759.1; !1PID:g217129 !'##note in Fig. 1, the authors used the yeast mitochondrial genetic !1code in their translation. Correspondingly, the sequence !1from Fig. 1 is inconsistent with that from Fig. 2 in having !1Thr rather than Leu at 55 positions !'##note the source is designated as Synechococcus vulcanus REFERENCE JQ1114 !$#authors Shimizu, T.; Ikeuchi, M.; Inoue, Y.; Hiyama, T. !$#submission submitted to JIPID, August 1991 !$#accession JQ1115 !'##molecule_type DNA !'##residues 1-755 ##label SHI2 !'##note the source is designated as Synechococcus vulcanus REFERENCE S18970 !$#authors Muehlenhoff, U.; Haehnel, W.; Witt, H.T.; Herrmann, R.G. !$#submission submitted to the EMBL Data Library, January 1992 !$#description Genes encoding ten subunits of photosystem I from the !1thermophilic cyanobacterium Synechococcus sp. !$#accession S19174 !'##molecule_type DNA !'##residues 1-210,'A',212-755 ##label MUE !'##cross-references EMBL:X63768; NID:g47570; PIDN:CAA45304.1; !1PID:g47571 GENETICS !$#gene psaA CLASSIFICATION #superfamily photosystem I P700 apoprotein KEYWORDS electron transfer; membrane protein; photosynthesis; !1photosystem I; thylakoid SUMMARY #length 755 #molecular-weight 83199 #checksum 6832 SEQUENCE /// ENTRY S26071 #type complete TITLE photosystem I protein A1 - Euglena gracilis chloroplast ORGANISM #formal_name chloroplast Euglena gracilis DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS S26071; S34514; S06273; S34881 REFERENCE S26071 !$#authors Cushman, J.C.; Hallick, R.B.; Price, C.A. !$#journal Curr. Genet. (1988) 13:159-171 !$#title The two genes for the P(700) chlorophyll a apoproteins on !1the Euglena gracilis chloroplast genome contain multiple !1introns. !$#cross-references MUID:88223484; PMID:2836086 !$#accession S26071 !'##molecule_type DNA !'##residues 1-751 ##label CUS !'##cross-references EMBL:Z11874; NID:g14353; PIDN:CAA77910.1; !1PID:g14360 !'##note the sequence of residues 66-105 and the corresponding !1nucleotide sequence are not shown in Fig. 3 REFERENCE S34494 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.; Monfort, !1A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#submission submitted to the EMBL Data Library, January 1993 !$#description The complete sequence of the Euglena gracilis chloroplast !1genome (tentative). !$#accession S34514 !'##molecule_type DNA !'##residues 1-751 ##label HAL1 !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50093.1; !1PID:g415749 REFERENCE S34862 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.R.; !1Monfort, A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#journal Nucleic Acids Res. (1993) 21:3537-3544 !$#title Complete sequence of Euglena gracilis chloroplast DNA. !$#cross-references MUID:93347989; PMID:8346031 !$#contents annotation !$#note neither amino acid nor nucleotide sequence is given REFERENCE S06273 !$#authors Manzara, T.; Hu, J.X.; Price, C.A.; Hallick, R.B. !$#journal Plant Mol. Biol. (1987) 8:327-336 !$#title Characterization of the TrnD, TrnK, PsaA locus of Euglena !1gracilis chloroplast DNA. !$#accession S06273 !'##molecule_type DNA !'##residues 1-398 ##label MAN !'##cross-references EMBL:M17309; NID:g336892; PIDN:AAA84232.1; !1PID:g336893 GENETICS !$#gene psaA !$#genome chloroplast !$#introns 399/1; 472/3; 685/2 CLASSIFICATION #superfamily photosystem I P700 apoprotein KEYWORDS chloroplast; electron transfer; membrane protein; !1photosynthesis; photosystem I; thylakoid SUMMARY #length 751 #molecular-weight 83988 #checksum 9379 SEQUENCE /// ENTRY A2NTP7 #type complete TITLE photosystem I P700 apoprotein A2 - common tobacco chloroplast ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 17-Feb-1995 ACCESSIONS A03466 REFERENCE A00149 !$#authors Sugiura, M. !$#submission submitted to the EMBL Data Library, August 1986 !$#accession A03466 !'##molecule_type DNA !'##residues 1-734 ##label SUG !'##experimental_source cv. Bright Yellow 4 REFERENCE A38013 !$#authors Shinozaki, K.; Ohme, M.; Tanaka, M.; Wakasugi, T.; !1Hayashida, N.; Matsubayashi, T.; Zaita, N.; Chunwongse, J.; !1Obokata, J.; Yamaguchi-Shinozaki, K.; Ohto, C.; Torazawa, !1K.; Meng, B.Y.; Sugita, M.; Deno, H.; Kamogashira, T.; !1Yamada, K.; Kusuda, J.; Takaiwa, F.; Kato, A.; Tohdoh, N.; !1Shimada, H.; Sugiura, M. !$#journal EMBO J. (1986) 5:2043-2049 !$#title The complete nucleotide sequence of the tobacco chloroplast !1genome: its gene organization and expression. !$#contents annotation; gene organization, sites, features COMMENT This is one of the specific proteins associated with !1chlorophyll a of the P700 complex, which is considered the !1reaction center of photosystem I in the chloroplast. P700 !1transfers electrons supplied by photosystem II to !1Z-substance (an iron-sulfur protein), which in turn reduces !1NADP to NADPH via a complex electron transfer system that !1includes chloroplast ferredoxin and other iron-sulfur !1proteins. GENETICS !$#gene psaB !$#genome chloroplast CLASSIFICATION #superfamily photosystem I P700 apoprotein KEYWORDS chloroplast; electron transfer; membrane protein; !1photosynthesis; photosystem I; thylakoid SUMMARY #length 734 #molecular-weight 82409 #checksum 9857 SEQUENCE /// ENTRY A2RZP7 #type complete TITLE photosystem I P700 apoprotein A2 - rice chloroplast ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS JQ0222; S05102 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0222 !'##molecule_type DNA !'##residues 1-734 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05102 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-734 ##label HIR !'##cross-references EMBL:X15901; NID:g11957; PIDN:CAA33995.1; !1PID:g11981 !'##experimental_source cv. Nihonbare GENETICS !$#gene psaB !$#map_position CP38972-36768 !$#genome chloroplast CLASSIFICATION #superfamily photosystem I P700 apoprotein KEYWORDS chloroplast; electron transfer; membrane protein; !1photosynthesis; photosystem I; thylakoid SUMMARY #length 734 #molecular-weight 82560 #checksum 1108 SEQUENCE /// ENTRY A2LVP7 #type complete TITLE photosystem I P700 apoprotein A2 - liverwort (Marchantia polymorpha) chloroplast ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 16-Jul-1999 ACCESSIONS A03467; S01605 REFERENCE A00150 !$#authors Ohyama, K. !$#submission submitted to the EMBL Data Library, October 1986 !$#accession A03467 !'##molecule_type DNA !'##residues 1-734 ##label OHY REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features REFERENCE S01567 !$#authors Umesono, K.; Inokuchi, H.; Shiki, Y.; Takeuchi, M.; Chang, !1Z.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Ohyama, K.; Ozeki, !1H. !$#journal J. Mol. Biol. (1988) 203:299-331 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. II. Gene organization of the large !1single copy region from rps'12 to atpB. !$#cross-references MUID:89068686; PMID:2974085 !$#accession S01605 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-734 ##label UME !'##cross-references GB:X04465; GB:Y00686; NID:g11640; PIDN:CAA28084.1; !1PID:g11671 COMMENT This is one of the specific proteins associated with !1chlorophyll a of the P700 complex, which is considered the !1reaction center of photosystem I in the chloroplast. P700 !1transfers electrons supplied by photosystem II to !1Z-substance (an iron-sulfur protein), which in turn reduces !1NADP to NADPH via a complex electron transfer system that !1includes chloroplast ferredoxin and other iron-sulfur !1proteins. GENETICS !$#gene psaB !$#genome chloroplast CLASSIFICATION #superfamily photosystem I P700 apoprotein KEYWORDS chloroplast; electron transfer; membrane protein; !1membrane-associated complex; photosynthesis; photosystem I; !1thylakoid SUMMARY #length 734 #molecular-weight 82415 #checksum 7714 SEQUENCE /// ENTRY S26072 #type complete TITLE photosystem I protein A2 - Euglena gracilis chloroplast ALTERNATE_NAMES photosystem I protein B1 ORGANISM #formal_name chloroplast Euglena gracilis DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS S26072; S34515; S34882 REFERENCE S26071 !$#authors Cushman, J.C.; Hallick, R.B.; Price, C.A. !$#journal Curr. Genet. (1988) 13:159-171 !$#title The two genes for the P(700) chlorophyll a apoproteins on !1the Euglena gracilis chloroplast genome contain multiple !1introns. !$#cross-references MUID:88223484; PMID:2836086 !$#accession S26072 !'##molecule_type DNA !'##residues 1-734 ##label CUS !'##cross-references EMBL:Z11874; NID:g14353; PIDN:CAA77911.1; !1PID:g14361 REFERENCE S34494 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.; Monfort, !1A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#submission submitted to the EMBL Data Library, January 1993 !$#description The complete sequence of the Euglena gracilis chloroplast !1genome (tentative). !$#accession S34515 !'##molecule_type DNA !'##residues 1-734 ##label HAL1 !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50094.1; !1PID:g415750 REFERENCE S34862 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.R.; !1Monfort, A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#journal Nucleic Acids Res. (1993) 21:3537-3544 !$#title Complete sequence of Euglena gracilis chloroplast DNA. !$#cross-references MUID:93347989; PMID:8346031 !$#accession S34882 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-734 ##label HAL2 !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50094.1; !1PID:g415750 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1993 GENETICS !$#gene psaB !$#genome chloroplast !$#introns 380/1; 394/1; 504/1; 533/1; 603/1; 640/1 CLASSIFICATION #superfamily photosystem I P700 apoprotein KEYWORDS chloroplast; electron transfer; membrane-associated complex; !1photosynthesis; photosystem I; thylakoid; transmembrane !1protein SUMMARY #length 734 #molecular-weight 82695 #checksum 7880 SEQUENCE /// ENTRY S20923 #type complete TITLE photosystem I protein A2 - Synechococcus sp. ORGANISM #formal_name Synechococcus sp. DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS S20923; JQ1116; S19175 REFERENCE S20922 !$#authors Shimizu, T.; Hiyama, T.; Ikeuchi, M.; Inoue, Y. !$#journal Plant Mol. Biol. (1992) 18:785-791 !$#title Nucleotide sequences of the psaA and psaB genes encoding the !1photosystem I core proteins from the thermophilic !1cyanobacterium Synechococcus vulcanus. !$#cross-references MUID:92216055; PMID:1558952 !$#accession S20923 !'##molecule_type DNA !'##residues 1-741 ##label SHI1 !'##note in Fig. 1, the authors used the yeast mitochondrial genetic !1code in their translation; correspondingly, the sequence !1from Fig. 1 is inconsistent with that from Fig. 2 in having !1Thr rather than Leu at 55 positions !'##note the source is designated as Synechococcus vulcanus REFERENCE JQ1114 !$#authors Shimizu, T.; Ikeuchi, M.; Inoue, Y.; Hiyama, T. !$#submission submitted to JIPID, August 1991 !$#accession JQ1116 !'##molecule_type DNA !'##residues 1-741 ##label SHI2 !'##note the source is designated as Synechococcus vulcanus REFERENCE S18970 !$#authors Muehlenhoff, U.; Haehnel, W.; Witt, H.T.; Herrmann, R.G. !$#submission submitted to the EMBL Data Library, January 1992 !$#description Genes encoding ten subunits of photosystem I from the !1thermophilic cyanobacterium Synechococcus sp. !$#accession S19175 !'##molecule_type DNA !'##residues 1-741 ##label MUE !'##cross-references EMBL:X63768; NID:g47570; PIDN:CAA45305.1; !1PID:g47572 GENETICS !$#gene psaB CLASSIFICATION #superfamily photosystem I P700 apoprotein KEYWORDS electron transfer; membrane-associated complex; !1photosynthesis; photosystem I; thylakoid; transmembrane !1protein SUMMARY #length 741 #molecular-weight 83044 #checksum 7494 SEQUENCE /// ENTRY A1RZJ #type complete TITLE photosystem I protein psaJ - rice chloroplast ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS JQ0246; S05126 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0246 !'##molecule_type DNA !'##residues 1-44 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05126 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-44 ##label HIR !'##cross-references EMBL:X15901; NID:g11957; PIDN:CAA33968.1; !1PID:g12007 !'##experimental_source cv. Nihonbare GENETICS !$#gene psaJ !$#map_position CP64622-64756 !$#genome chloroplast CLASSIFICATION #superfamily photosystem I protein psaJ KEYWORDS chloroplast; photosystem I; transmembrane protein SUMMARY #length 44 #molecular-weight 5050 #checksum 4590 SEQUENCE /// ENTRY A1RZI #type complete TITLE photosystem I protein psaI - rice chloroplast ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS JQ0235; S05115 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0235 !'##molecule_type DNA !'##residues 1-36 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05115 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-36 ##label HIR !'##cross-references EMBL:X15901; NID:g11957; PIDN:CAA33957.1; !1PID:g11996 !'##experimental_source cv. Nihonbare GENETICS !$#gene psaI !$#map_position CP57222-57332 !$#genome chloroplast CLASSIFICATION #superfamily photosystem I protein psaI KEYWORDS chloroplast; photosystem I; transmembrane protein SUMMARY #length 36 #molecular-weight 4028 #checksum 1273 SEQUENCE /// ENTRY F1FNIT #type complete TITLE photosystem I protein psaI - turnip fern chloroplast ORGANISM #formal_name chloroplast Angiopteris lygodiifolia #common_name turnip fern DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS S19231 REFERENCE S19228 !$#authors Yoshinaga, K.; Kubota, Y.; Ishii, T.; Wada, K. !$#journal Plant Mol. Biol. (1992) 18:79-82 !$#title Nucleotide sequence of atpB, rbcL, trnR, dedB and psaI !1chloroplast genes from a fern Angiopteris lygodiifolia: a !1possible emergence of Spermatophyta lineage before the !1separation of Bryophyta and Pteridophyta. !$#cross-references MUID:92119238; PMID:1731980 !$#accession S19231 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-36 ##label YOS !'##cross-references EMBL:X58429; NID:g11189; PIDN:CAA41334.1; !1PID:g11193 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1March 1991 GENETICS !$#gene psaI !$#genome chloroplast CLASSIFICATION #superfamily photosystem I protein psaI KEYWORDS chloroplast; photosynthesis; photosystem I; thylakoid; !1transmembrane protein SUMMARY #length 36 #molecular-weight 3930 #checksum 966 SEQUENCE /// ENTRY A1RZH #type complete TITLE photosystem I protein psaH precursor - rice ORGANISM #formal_name Oryza sativa #common_name rice DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jul-1999 ACCESSIONS S11953 REFERENCE S11953 !$#authors de Pater, S.; Hensgens, L.A.M.; Schilperoort, R.A. !$#journal Plant Mol. Biol. (1990) 15:399-406 !$#title Structure and expression of a light-inducible shoot-specific !1rice gene. !$#cross-references MUID:91355888; PMID:2103460 !$#accession S11953 !'##molecule_type DNA !'##residues 1-142 ##label DEP !'##cross-references EMBL:X51911; NID:g20239; PIDN:CAA36191.1; !1PID:g20240 GENETICS !$#introns 40/2; 83/3 CLASSIFICATION #superfamily photosystem I protein psaH KEYWORDS chloroplast; photosynthesis; photosystem I; thylakoid; !1transmembrane protein FEATURE !$1-47 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$48-142 #product photosystem I protein psaH #status predicted !8#label MAT SUMMARY #length 142 #molecular-weight 15052 #checksum 4744 SEQUENCE /// ENTRY A1SP2 #type complete TITLE photosystem I chain II precursor - spinach ALTERNATE_NAMES photosystem I 20K protein ORGANISM #formal_name Spinacia oleracea #common_name spinach DATE 30-Jun-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jul-1999 ACCESSIONS S03016; A38065; S00617; B30473; A38786 REFERENCE S00450 !$#authors Muench, S.; Ljungberg, U.; Steppuhn, J.; Schneiderbauer, A.; !1Nechushtai, R.; Beyreuther, K.; Herrmann, R.G. !$#journal Curr. Genet. (1988) 14:511-518 !$#title Nucleotide sequences of cDNAs encoding the entire precursor !1polypeptides for subunits II and III of the photosystem I !1reaction center from spinach. !$#cross-references MUID:89136070; PMID:3066511 !$#accession S03016 !'##molecule_type mRNA !'##residues 1-212 ##label MUE !'##cross-references EMBL:X14017; NID:g21288; PIDN:CAA32182.1; !1PID:g21289 !$#accession A38065 !'##molecule_type protein !'##residues 51-64 ##label MUE2 REFERENCE S00617 !$#authors Lagoutte, B. !$#journal FEBS Lett. (1988) 232:275-280 !$#title Cloning and sequencing of spinach cDNA clones encoding the !120 kDa PS I polypeptide. !$#cross-references MUID:88242812; PMID:3288500 !$#accession S00617 !'##molecule_type mRNA !'##residues 1-34,'VT',37-57,'R',59,'AA',62-212 ##label LAG !'##cross-references EMBL:Y00759; NID:g21292; PIDN:CAA68728.1; !1PID:g21293 REFERENCE JT0211 !$#authors Oh-oka, H.; Takahashi, Y.; Kuriyama, K.; Saeki, K.; !1Matsubara, H. !$#journal J. Biochem. (1988) 103:962-968 !$#title The protein responsible for center A/B in spinach !1photosystem I: isolation with iron-sulfur cluster(s) and !1complete sequence analysis. !$#cross-references MUID:89008208; PMID:3049567 !$#accession B30473 !'##molecule_type protein !'##residues 51-63 ##label OHA GENETICS !$#gene psaD CLASSIFICATION #superfamily photosystem I chain II KEYWORDS chloroplast; photosynthesis; photosystem I; thylakoid FEATURE !$1-50 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$51-212 #product photosystem I chain II #status experimental !8#label MAT SUMMARY #length 212 #molecular-weight 23158 #checksum 4895 SEQUENCE /// ENTRY F1SP3 #type complete TITLE photosystem I chain III precursor - spinach ALTERNATE_NAMES photosystem I plastocyanin-binding subunit ORGANISM #formal_name Spinacia oleracea #common_name spinach DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jul-1999 ACCESSIONS S00451; A38785; S05003 REFERENCE S00451 !$#authors Steppuhn, J.; Hermans, J.; Nechushtai, R.; Ljungberg, U.; !1Thuemmler, F.; Lottspeich, F.; Herrmann, R.G. !$#journal FEBS Lett. (1988) 237:218-224 !$#title Nucleotide sequence of cDNA clones encoding the entire !1precursor polypeptides for subunits IV and V of the !1photosystem I reaction center from spinach. !$#cross-references MUID:89005631; PMID:3049152 !$#accession S00451 !'##molecule_type mRNA !'##residues 1-231 ##label STE !'##cross-references EMBL:X13133; NID:g21302; PIDN:CAA31523.1; !1PID:g21303 !$#accession A38785 !'##molecule_type protein !'##residues 78-90 ##label STE2 !'##note the authors identified this protein as photosystem I chain IV !1and subsequently (pers. comm.) revised this identification REFERENCE S05003 !$#authors Hippler, M.; Ratajczak, R.; Haehnel, W. !$#journal FEBS Lett. (1989) 250:280-284 !$#title Identification of the plastocyanin binding subunit of !1photosystem I. !$#accession S05003 !'##molecule_type protein !'##residues 'X',79-82,'X',84,'X',86-87,'X',89-91 ##label HIP GENETICS !$#gene psaF CLASSIFICATION #superfamily photosystem I chain III KEYWORDS chloroplast; photosynthesis; photosystem I; thylakoid FEATURE !$1-77 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$78-231 #product photosystem I chain III #status experimental !8#label MAT SUMMARY #length 231 #molecular-weight 25412 #checksum 7285 SEQUENCE /// ENTRY F1SP4 #type complete TITLE photosystem I chain IV precursor - spinach ORGANISM #formal_name Spinacia oleracea #common_name spinach DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jul-1999 ACCESSIONS S00450; A38784; A30473 REFERENCE S00450 !$#authors Muench, S.; Ljungberg, U.; Steppuhn, J.; Schneiderbauer, A.; !1Nechushtai, R.; Beyreuther, K.; Herrmann, R.G. !$#journal Curr. Genet. (1988) 14:511-518 !$#title Nucleotide sequences of cDNAs encoding the entire precursor !1polypeptides for subunits II and III of the photosystem I !1reaction center from spinach. !$#cross-references MUID:89136070; PMID:3066511 !$#accession S00450 !'##molecule_type mRNA !'##residues 1-125 ##label MUE !'##cross-references EMBL:X14018; NID:g21294; PIDN:CAA32183.1; !1PID:g21295 !$#accession A38784 !'##molecule_type protein !'##residues 35-54 ##label MUE2 !'##note the authors identified this protein as photosystem I chain III !1and subsequently (pers. comm.) revised this identification REFERENCE JT0211 !$#authors Oh-oka, H.; Takahashi, Y.; Kuriyama, K.; Saeki, K.; !1Matsubara, H. !$#journal J. Biochem. (1988) 103:962-968 !$#title The protein responsible for center A/B in spinach !1photosystem I: isolation with iron-sulfur cluster(s) and !1complete sequence analysis. !$#cross-references MUID:89008208; PMID:3049567 !$#accession A30473 !'##molecule_type protein !'##residues 35-45 ##label OHA GENETICS !$#gene psaE CLASSIFICATION #superfamily photosystem I chain IV KEYWORDS chloroplast; photosynthesis; photosystem I; thylakoid FEATURE !$1-34 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$35-125 #product photosystem I chain IV #status experimental !8#label MAT SUMMARY #length 125 #molecular-weight 13367 #checksum 8045 SEQUENCE /// ENTRY F1BH4 #type complete TITLE photosystem I chain IV precursor - barley ALTERNATE_NAMES photosystem I 10.8K chain; photosystem I 16K chain ORGANISM #formal_name Hordeum vulgare #common_name barley DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jul-1999 ACCESSIONS S01326; S06151 REFERENCE S01326 !$#authors Okkels, J.S.; Jepsen, L.B.; Honberg, L.S.; Lehmbeck, J.; !1Scheller, H.V.; Brandt, P.; Hoyer-Hansen, G.; Stummann, B.; !1Henningsen, K.W.; von Wettstein, D.; Moller, B.L. !$#journal FEBS Lett. (1988) 237:108-112 !$#title A cDNA clone encoding a 10.8 kDa photosystem I polypeptide !1of barley. !$#cross-references MUID:89005607; PMID:3049147 !$#accession S01326 !'##molecule_type mRNA !'##residues 1-147 ##label OKK !'##cross-references EMBL:Y00966; NID:g19086; PIDN:CAA68782.1; !1PID:g19087 REFERENCE S06149 !$#authors Anandan, S.; Vainstein, A.; Thornber, J.P. !$#journal FEBS Lett. (1989) 256:150-154 !$#title Correlation of some published amino acid sequences for !1photosystem I polypeptides to a 17 kDa LHCI pigment-protein !1and to subunits III and IV of the core complex. !$#cross-references MUID:90033290; PMID:2680596 !$#accession S06151 !'##molecule_type protein !'##residues 47-63 ##label ANA !'##note the authors identified this protein as photosystem I chain III CLASSIFICATION #superfamily photosystem I chain IV KEYWORDS chloroplast; photosynthesis; photosystem I; thylakoid FEATURE !$1-46 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$47-147 #product photosystem I chain IV #status experimental !8#label MAT SUMMARY #length 147 #molecular-weight 15456 #checksum 5467 SEQUENCE /// ENTRY F1YB4 #type complete TITLE photosystem I chain IV - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES photosystem I 8K chain ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 30-Sep-1991 #sequence_revision 23-May-1997 #text_change 16-Jun-2000 ACCESSIONS S75924; B34301; S08776; A34129 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75924 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-74 ##label KAN !'##cross-references EMBL:D90913; GB:AB001339; NID:g1653348; !1PIDN:BAA18383.1; PID:g1653469 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 REFERENCE A34301 !$#authors Chitnis, P.R.; Reilly, P.A.; Miedel, M.C.; Nelson, N. !$#journal J. Biol. Chem. (1989) 264:18374-18380 !$#title Structure and targeted mutagenesis of the gene encoding !18-kDa subunit of photosystem I from the cyanobacterium !1Synechocystis sp. PCC 6803. !$#cross-references MUID:90036928; PMID:2509456 !$#accession B34301 !'##molecule_type DNA !'##residues 1-9,'S',11-74 ##label CHI !'##cross-references GB:J05079; NID:g154482; PIDN:AAA88629.1; !1PID:g154483 REFERENCE A34129 !$#authors Rousseau, F.; Lagoutte, B. !$#journal FEBS Lett. (1990) 260:241-244 !$#title Amino acid sequence of photosystem I subunit IV from the !1cyanobacterium Synechocystis PCC 6803. !$#cross-references MUID:90127438; PMID:2105239 !$#accession S08776 !'##molecule_type protein !'##residues 2-25,'G',27-74 ##label ROU !'##note the sequence in Fig. 4 is inconsistent with that from Fig. 2 in !1having 8-Arg GENETICS !$#gene psaE CLASSIFICATION #superfamily photosystem I chain IV KEYWORDS photosynthesis; photosystem I; thylakoid SUMMARY #length 74 #molecular-weight 8145 #checksum 294 SEQUENCE /// ENTRY F1PR4U #type complete TITLE photosystem I chain IV - red alga (Porphyra umbilicalis) chloroplast ORGANISM #formal_name chloroplast Porphyra umbilicalis #common_name laver DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS S20861 REFERENCE S20861 !$#authors Reith, M. !$#journal Plant Mol. Biol. (1992) 18:773-775 !$#title psaE and trnS(CGA) are encoded on the plastid genome of the !1red alga Porphyra umbilicalis. !$#cross-references MUID:92216052; PMID:1373082 !$#accession S20861 !'##molecule_type DNA !'##residues 1-62 ##label REI !'##cross-references EMBL:X60434; NID:g14207; PIDN:CAA42961.1; !1PID:g14208 GENETICS !$#gene psaE !$#genome chloroplast CLASSIFICATION #superfamily photosystem I chain IV KEYWORDS chloroplast; photosynthesis; photosystem I; thylakoid SUMMARY #length 62 #molecular-weight 7172 #checksum 8819 SEQUENCE /// ENTRY F1SP5 #type complete TITLE photosystem I chain V precursor - spinach ALTERNATE_NAMES photosystem I reaction center chain V ORGANISM #formal_name Spinacia oleracea #common_name spinach DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jul-1999 ACCESSIONS S00452 REFERENCE S00451 !$#authors Steppuhn, J.; Hermans, J.; Nechushtai, R.; Ljungberg, U.; !1Thuemmler, F.; Lottspeich, F.; Herrmann, R.G. !$#journal FEBS Lett. (1988) 237:218-224 !$#title Nucleotide sequence of cDNA clones encoding the entire !1precursor polypeptides for subunits IV and V of the !1photosystem I reaction center from spinach. !$#cross-references MUID:89005631; PMID:3049152 !$#accession S00452 !'##molecule_type mRNA !'##residues 1-167 ##label STE !'##cross-references EMBL:X13134; NID:g21298; PIDN:CAA31524.1; !1PID:g21299 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing GENETICS !$#gene psaG CLASSIFICATION #superfamily photosystem I chain V KEYWORDS chloroplast; photosynthesis; photosystem I; thylakoid; !1transmembrane protein FEATURE !$1-69 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$70-167 #product photosystem I chain V #status experimental !8#label MAT SUMMARY #length 167 #molecular-weight 18214 #checksum 4783 SEQUENCE /// ENTRY F2NTG #type complete TITLE psbG protein - common tobacco chloroplast ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 17-Feb-1995 ACCESSIONS A03468; A05195 REFERENCE A38013 !$#authors Shinozaki, K.; Ohme, M.; Tanaka, M.; Wakasugi, T.; !1Hayashida, N.; Matsubayashi, T.; Zaita, N.; Chunwongse, J.; !1Obokata, J.; Yamaguchi-Shinozaki, K.; Ohto, C.; Torazawa, !1K.; Meng, B.Y.; Sugita, M.; Deno, H.; Kamogashira, T.; !1Yamada, K.; Kusuda, J.; Takaiwa, F.; Kato, A.; Tohdoh, N.; !1Shimada, H.; Sugiura, M. !$#journal EMBO J. (1986) 5:2043-2049 !$#title The complete nucleotide sequence of the tobacco chloroplast !1genome: its gene organization and expression. !$#accession A03468 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-247 ##label SHI !'##cross-references EMBL:Z00044 !'##experimental_source cv. Bright Yellow 4 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1986 GENETICS !$#gene psbG !$#genome chloroplast CLASSIFICATION #superfamily psbG protein KEYWORDS chloroplast SUMMARY #length 247 #molecular-weight 27961 #checksum 9410 SEQUENCE /// ENTRY F2RZG #type complete TITLE psbG protein - rice chloroplast ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS JQ0227; S05107 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0227 !'##molecule_type DNA !'##residues 1-246 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05107 !'##molecule_type DNA !'##residues 1-246 ##label HIR !'##cross-references GB:X15901; NID:g11957; PIDN:CAA34000.1; PID:g11988 !'##experimental_source cv. Nihonbare GENETICS !$#gene psbG !$#genome chloroplast CLASSIFICATION #superfamily psbG protein KEYWORDS chloroplast SUMMARY #length 246 #molecular-weight 27681 #checksum 9568 SEQUENCE /// ENTRY F2ZMG #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain ndhK - maize chloroplast ALTERNATE_NAMES psbG protein ORGANISM #formal_name chloroplast Zea mays #common_name maize DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Jun-2002 ACCESSIONS A25710; S04436; S58556 REFERENCE A25710 !$#authors Steinmetz, A.A.; Castroviejo, M.; Sayre, R.T.; Bogorad, L. !$#journal J. Biol. Chem. (1986) 261:2485-2488 !$#title Protein PSII-G. An additional component of photosystem II !1identified through its plastid gene in maize. !$#cross-references MUID:86139982; PMID:3512536 !$#accession A25710 !'##molecule_type DNA !'##residues 1-248 ##label STE1 !'##cross-references EMBL:M12704; NID:g342592; PIDN:AAA84484.1; !1PID:g552735 REFERENCE S04434 !$#authors Steinmueller, K.; Ley, A.C.; Steinmetz, A.A.; Sayre, R.T.; !1Bogorad, L. !$#journal Mol. Gen. Genet. (1989) 216:60-69 !$#title Characterization of the ndhC-psbG-ORF157/159 operon of maize !1plastid DNA and of the cyanobacterium Synechocystis sp. !1PCC6803. !$#cross-references MUID:89281491; PMID:2499764 !$#accession S04436 !'##molecule_type DNA !'##residues 1-248 ##label STE2 !'##cross-references EMBL:X17438; NID:g12425; PIDN:CAA35482.1; !1PID:g12427 REFERENCE S58531 !$#authors Maier, R.M.; Neckermann, K.; Igloi, G.L.; Koessel, H. !$#journal J. Mol. Biol. (1995) 251:614-628 !$#title Complete sequence of the maize chloroplast genome: gene !1content, hotspots of divergence and fine tuning of genetic !1information by transcript editing. !$#cross-references MUID:95395841; PMID:7666415 !$#accession S58556 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-18,'G',20-248 ##label MAI !'##cross-references EMBL:X86563; NID:g902200; PIDN:CAA60290.1; !1PID:g902226 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1995 GENETICS !$#gene ndhK; psbG !$#genome chloroplast CLASSIFICATION #superfamily psbG protein KEYWORDS chloroplast; membrane-associated complex; NAD; !1oxidoreductase SUMMARY #length 248 #molecular-weight 27920 #checksum 2486 SEQUENCE /// ENTRY S04437 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) chain ndhK - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES psbG protein ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 16-Oct-1998 #sequence_revision 16-Oct-1998 #text_change 03-Jun-2002 ACCESSIONS S04437; S75825; S34478 REFERENCE S04434 !$#authors Steinmueller, K.; Ley, A.C.; Steinmetz, A.A.; Sayre, R.T.; !1Bogorad, L. !$#journal Mol. Gen. Genet. (1989) 216:60-69 !$#title Characterization of the ndhC-psbG-ORF157/159 operon of maize !1plastid DNA and of the cyanobacterium Synechocystis sp. !1PCC6803. !$#cross-references MUID:89281491; PMID:2499764 !$#accession S04437 !'##molecule_type DNA !'##residues 1-248 ##label STE !'##cross-references EMBL:X17439; NID:g48045; PIDN:CAA35485.1; !1PID:g48047 !'##note the authors translated the codon GCC for residue 23 as Ser and !1AGC for residue 24 as Ala REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75825 !'##molecule_type DNA !'##residues 1-248 ##label KAN !'##cross-references EMBL:D90913; GB:AB001339; NID:g1653348; !1PIDN:BAA18284.1; PID:g1653370 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 REFERENCE S34477 !$#authors Berger, S.; Ellersiek, U.; Kinzelt, D.; Steinmueller, K. !$#journal FEBS Lett. (1993) 326:246-250 !$#title Immunopurification of a subcomplex of the NAD !1(P)H-plastoquinone-oxidoreductase from the cyanobacterium !1Synechocystis sp. PCC6803. !$#cross-references MUID:93314795; PMID:8325373 !$#accession S34478 !'##molecule_type protein !'##residues 3-9 ##label BER !'##note this protein probably does not carry the iron-sulfur cluster in !1the complex GENETICS !$#gene ndhK; psbG; psbG1 CLASSIFICATION #superfamily psbG protein KEYWORDS NAD; oxidoreductase FEATURE !$3-248 #product NADH dehydrogenase (ubiquinone) chain ndhK !8#status experimental #label MAT SUMMARY #length 248 #molecular-weight 27345 #checksum 3022 SEQUENCE /// ENTRY F2YBG2 #type complete TITLE hypothetical ndhK homolog - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES psbG2 protein ORGANISM #formal_name Synechocystis sp. DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jul-1999 ACCESSIONS S09199; A34557 REFERENCE A34557 !$#authors Mayes, S.R.; Cook, K.M.; Barber, J. !$#journal FEBS Lett. (1990) 262:49-54 !$#title Nucleotide sequence of the second psbG gene in Synechocystis !16803. Possible implications for psbG function as a NAD(P)H !1dehydrogenase subunit gene. !$#cross-references MUID:90201372; PMID:2108054 !$#accession S09199 !'##molecule_type DNA !'##residues 1-219 ##label MAY !'##cross-references EMBL:X17359; NID:g48067; PIDN:CAA35236.1; !1PID:g48068 !'##note there is no evidence this sequence is transcribed or translated COMMENT This is the hypothetical translation of a sequence that was !1not reported as a coding sequence in the complete genome. GENETICS !$#gene psbG2 CLASSIFICATION #superfamily psbG protein SUMMARY #length 219 #molecular-weight 24540 #checksum 7128 SEQUENCE /// ENTRY F2LVG #type complete TITLE psbG protein - liverwort (Marchantia polymorpha) chloroplast ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 16-Jul-1999 ACCESSIONS A03469; S01600 REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#accession A03469 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-243 ##label OHY !'##cross-references EMBL:X04465; NID:g11640; PIDN:CAA28088.1; !1PID:g11676 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1986 REFERENCE S01567 !$#authors Umesono, K.; Inokuchi, H.; Shiki, Y.; Takeuchi, M.; Chang, !1Z.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Ohyama, K.; Ozeki, !1H. !$#journal J. Mol. Biol. (1988) 203:299-331 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. II. Gene organization of the large !1single copy region from rps'12 to atpB. !$#cross-references MUID:89068686; PMID:2974085 !$#accession S01600 !'##molecule_type DNA !'##residues 1-243 ##label UME !'##cross-references GB:X04465; GB:Y00686; NID:g11640; PIDN:CAA28088.1; !1PID:g11676 GENETICS !$#gene psbG !$#genome chloroplast CLASSIFICATION #superfamily psbG protein KEYWORDS chloroplast SUMMARY #length 243 #molecular-weight 27610 #checksum 7378 SEQUENCE /// ENTRY F2PPG #type complete TITLE psbG protein - Paramecium tetraurelia mitochondrion ORGANISM #formal_name mitochondrion Paramecium tetraurelia DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 19-Jan-2001 ACCESSIONS S07736; JS0235 REFERENCE S07725 !$#authors Pritchard, A.E.; Seilhamer, J.J.; Mahalingam, R.; Sable, !1C.L.; Venuti, S.E.; Cummings, D.J. !$#journal Nucleic Acids Res. (1990) 18:173-180 !$#title Nucleotide sequence of the mitochondrial genome of !1Paramecium. !$#cross-references MUID:90174913; PMID:2308823 !$#accession S07736 !'##status translation not shown !'##molecule_type DNA !'##residues 1-156 ##label PRI !'##cross-references EMBL:X15917; NID:g13256; PIDN:CAA34045.1; !1PID:g578753 REFERENCE JS0231 !$#authors Pritchard, A.E.; Venuti, S.E.; Ghalambor, M.A.; Sable, C.L.; !1Cummings, D.J. !$#journal Gene (1989) 78:121-134 !$#title An unusual region of Paramecium mitochondrial DNA containing !1chloroplast-like genes. !$#cross-references MUID:89357489; PMID:2670676 !$#accession JS0235 !'##molecule_type DNA !'##residues 1-122,'IFV',126,'G',128-156 ##label PRI2 !'##cross-references GB:M26930; NID:g341550; PIDN:AAA79257.1; !1PID:g1019632 !'##experimental_source strain sp. 4.51 !'##note the source is designated as Paramecium aurelia species 4 stock !151, now designated Paramecium tetraurelia, ATCC 30567 GENETICS !$#gene psbG !$#genome mitochondrion !$#genetic_code SGC6 !$#start_codon ATA CLASSIFICATION #superfamily psbG protein KEYWORDS mitochondrion SUMMARY #length 156 #molecular-weight 17453 #checksum 1158 SEQUENCE /// ENTRY E65000 #type complete TITLE NADH2 dehydrogenase (ubiquinone) (EC 1.6.5.3) I chain B - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 12-Sep-1997 #sequence_revision 17-Sep-1997 #text_change 03-Jun-2002 ACCESSIONS E65000; S38311; S65633; S37059 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65000 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-220 ##label BLAT !'##cross-references GB:AE000318; GB:U00096; NID:g1788623; !1PIDN:AAC75347.1; PID:g1788624; UWGP:b2287 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S38310 !$#authors Weidner, U.; Geier, S.; Ptock, A.; Friedrich, T.; Leif, H.; !1Weiss, H. !$#journal J. Mol. Biol. (1993) 233:109-122 !$#title The gene locus of the proton-translocating NADH:ubiquinone !1oxidoreductase in Escherichia coli. Organization of the 14 !1genes and relationship between the derived proteins and !1subunits of mitochondrial complex I. !$#cross-references MUID:93389724; PMID:7690854 !$#accession S38311 !'##status preliminary !'##molecule_type DNA !'##residues 1-70,'L',72-220 ##label WE2 !'##cross-references EMBL:X68301; NID:g444012; PIDN:CAA48361.1; !1PID:g397899 !'##experimental_source strain AN387 REFERENCE S65633 !$#authors Leif, H.; Sled, V.D.; Ohnishi, T.; Weiss, H.; Friedrich, T. !$#journal Eur. J. Biochem. (1995) 230:538-548 !$#title Isolation and characterization of the proton-translocating !1NADH:ubiquinone oxidoreductase from Escherichia coli. !$#cross-references MUID:95331291; PMID:7607227 !$#accession S65633 !'##status preliminary !'##molecule_type protein !'##residues 1-6 ##label LEI GENETICS !$#gene nuoB !$#map_position 49.5 min CLASSIFICATION #superfamily psbG protein KEYWORDS NAD; oxidoreductase SUMMARY #length 220 #molecular-weight 25056 #checksum 7357 SEQUENCE /// ENTRY F2RZI #type complete TITLE photosystem II protein psbI - rice chloroplast ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS JQ0204; S05084 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0204 !'##molecule_type DNA !'##residues 1-36 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05084 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-36 ##label HIR !'##cross-references EMBL:X15901; NID:g11957; PIDN:CAA34011.1; !1PID:g11962 !'##experimental_source cv. Nihonbare !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1989 GENETICS !$#gene psbI !$#genome chloroplast CLASSIFICATION #superfamily photosystem II protein psbI KEYWORDS chloroplast; photosystem II; transmembrane protein SUMMARY #length 36 #molecular-weight 4154 #checksum 474 SEQUENCE /// ENTRY F2NTI #type complete TITLE photosystem II protein psbI - common tobacco chloroplast ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Feb-1997 ACCESSIONS S05608; S18008 REFERENCE A38013 !$#authors Shinozaki, K.; Ohme, M.; Tanaka, M.; Wakasugi, T.; !1Hayashida, N.; Matsubayashi, T.; Zaita, N.; Chunwongse, J.; !1Obokata, J.; Yamaguchi-Shinozaki, K.; Ohto, C.; Torazawa, !1K.; Meng, B.Y.; Sugita, M.; Deno, H.; Kamogashira, T.; !1Yamada, K.; Kusuda, J.; Takaiwa, F.; Kato, A.; Tohdoh, N.; !1Shimada, H.; Sugiura, M. !$#journal EMBO J. (1986) 5:2043-2049 !$#title The complete nucleotide sequence of the tobacco chloroplast !1genome: its gene organization and expression. !$#accession S05608 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-36 ##label SHI !'##cross-references EMBL:Z00044 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1986 GENETICS !$#gene psbI !$#genome chloroplast CLASSIFICATION #superfamily photosystem II protein psbI KEYWORDS chloroplast; photosynthesis; photosystem II; thylakoid; !1transmembrane protein SUMMARY #length 36 #molecular-weight 4168 #checksum 509 SEQUENCE /// ENTRY F2KHID #type complete TITLE photosystem II protein psbI - Douglas fir chloroplast ORGANISM #formal_name chloroplast Pseudotsuga menziesii #common_name Douglas fir DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS S21421; S55880 REFERENCE S21421 !$#authors Tsai, C.H.; Strauss, S.H. !$#submission submitted to the EMBL Data Library, September 1989 !$#description Nucleotide sequences of the Douglas-fir chloroplast DNA !1region containing the dispersed repeat and a tRNA-Serine !1genes. !$#accession S21421 !'##molecule_type DNA !'##residues 1-36 ##label TSA !'##cross-references EMBL:X16571; NID:g12124; PIDN:CAA34592.1; !1PID:g12125 REFERENCE S55880 !$#authors Hipkins, V.D.; Marshall, K.A.; Neale, D.B.; Rottmann, W.H.; !1Strauss, S.H. !$#journal Curr. Genet. (1995) 27:572-579 !$#title A mutation hotspot in the chloroplast genome of a conifer !1(Douglas-fir: Pseudotsuga) is caused by variability in the !1number of direct repeats derived from a partially duplicated !1tRNA gene. !$#cross-references MUID:96031715; PMID:7553944 !$#accession S55880 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-36 ##label HIP !'##cross-references EMBL:L20416; NID:g309889; PIDN:AAB01440.1; !1PID:g309890; EMBL:L20417; NID:g309891; PID:g309892 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1993 GENETICS !$#genome chloroplast CLASSIFICATION #superfamily photosystem II protein psbI KEYWORDS chloroplast; membrane-associated complex; photosynthesis; !1photosystem II; thylakoid SUMMARY #length 36 #molecular-weight 4151 #checksum 321 SEQUENCE /// ENTRY F2EGI #type complete TITLE photosystem II protein psbI - Euglena gracilis chloroplast ORGANISM #formal_name chloroplast Euglena gracilis DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS S26086; S34512; S34879 REFERENCE S26086 !$#authors Hallick, R.B. !$#submission submitted to the EMBL Data Library, March 1992 !$#accession S26086 !'##molecule_type DNA !'##residues 1-53 ##label HAL !'##cross-references EMBL:Z11874; NID:g14353; PIDN:CAA77908.1; !1PID:g14358 REFERENCE S34494 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.; Monfort, !1A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#submission submitted to the EMBL Data Library, January 1993 !$#description The complete sequence of the Euglena gracilis chloroplast !1genome (tentative). !$#accession S34512 !'##molecule_type DNA !'##residues 1-53 ##label HAL1 !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50091.1; !1PID:g415747 REFERENCE S34862 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.R.; !1Monfort, A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#journal Nucleic Acids Res. (1993) 21:3537-3544 !$#title Complete sequence of Euglena gracilis chloroplast DNA. !$#cross-references MUID:93347989; PMID:8346031 !$#accession S34879 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-53 ##label HAL2 !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50091.1; !1PID:g415747 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1993 GENETICS !$#gene psbI !$#genome chloroplast CLASSIFICATION #superfamily photosystem II protein psbI KEYWORDS chloroplast; photosynthesis; photosystem II; thylakoid; !1transmembrane protein SUMMARY #length 53 #molecular-weight 6129 #checksum 9924 SEQUENCE /// ENTRY F2RZL #type complete TITLE photosystem II protein psbL - rice chloroplast ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 18-Feb-2000 ACCESSIONS JQ0241; S05121 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0241 !'##molecule_type DNA !'##residues 1-38 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05121 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-38 ##label HIR !'##cross-references EMBL:X15901; NID:g11957; PIDN:CAA33963.1; !1PID:g12002 !'##experimental_source cv. Nihonbare !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1989 GENETICS !$#gene psbL !$#genome chloroplast CLASSIFICATION #superfamily photosystem II protein psbL KEYWORDS chloroplast; photosynthesis; photosystem II FEATURE !$18-37 #domain transmembrane #status predicted #label TMM SUMMARY #length 38 #molecular-weight 4497 #checksum 7406 SEQUENCE /// ENTRY F2WTL #type complete TITLE photosystem II protein psbL - wheat chloroplast ALTERNATE_NAMES hypothetical protein 38 ORGANISM #formal_name chloroplast Triticum aestivum #common_name common wheat DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS JG0010; S20843; S03623 REFERENCE JG0010 !$#authors Webber, A.N.; Hird, S.M.; Packman, L.C.; Dyer, T.A.; Gray, !1J.C. !$#journal Plant Mol. Biol. (1989) 12:141-151 !$#title A photosystem II polypeptide is encoded by an open reading !1frame cotranscribed with genes for cytochrome b-559 in wheat !1chloroplast DNA. !$#accession JG0010 !'##molecule_type DNA !'##residues 1-38 ##label WEB !'##cross-references EMBL:X15225; NID:g14259; PIDN:CAA33296.1; !1PID:g14262 !$#accession S20843 !'##molecule_type protein !'##residues 'XXXX',6-17 ##label WEB2 GENETICS !$#gene psbL !$#genome chloroplast CLASSIFICATION #superfamily photosystem II protein psbL KEYWORDS chloroplast; photosynthesis; photosystem II; thylakoid; !1transmembrane protein FEATURE !$2-38 #product photosystem II protein psbL #status !8experimental #label MAT\ !$18-37 #domain transmembrane #status predicted #label TMM SUMMARY #length 38 #molecular-weight 4497 #checksum 7406 SEQUENCE /// ENTRY F2SKL #type complete TITLE photosystem II protein psbL - garden snapdragon chloroplast ORGANISM #formal_name chloroplast Antirrhinum majus #common_name garden snapdragon DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 18-Feb-2000 ACCESSIONS S19786 REFERENCE S19786 !$#authors Kudla, J. !$#submission submitted to the EMBL Data Library, November 1991 !$#accession S19786 !'##molecule_type DNA !'##residues 1-38 ##label KUD !'##cross-references EMBL:X63206; NID:g11318; PIDN:CAA44889.1; !1PID:g11319 GENETICS !$#gene psbL !$#genome chloroplast CLASSIFICATION #superfamily photosystem II protein psbL KEYWORDS chloroplast; photosynthesis; photosystem II; thylakoid FEATURE !$18-37 #domain transmembrane #status predicted #label TMM SUMMARY #length 38 #molecular-weight 4470 #checksum 7456 SEQUENCE /// ENTRY F2KTL #type complete TITLE photosystem II protein psbL - Cyanophora paradoxa cyanelle ALTERNATE_NAMES photosystem II protein psbH ORGANISM #formal_name cyanelle Cyanophora paradoxa DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS S09483; T06868 REFERENCE S09182 !$#authors Cantrell, A.; Bryant, D.A. !$#journal Prog. Photosyn. Res. (1987) 4:659-662 !$#title Molecular cloning and nucleotide sequences of the genes !1encoding cytochrome B-559 from the cyanelle genome of !1Cyanophora paradoxa. !$#accession S09483 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type DNA !'##residues 1-38 ##label CAN REFERENCE Z15840 !$#authors Stirewalt, V.L.; Michalowski, C.B.; Luffelhardt, W.; !1Bohnert, H.J.; Bryant, D.A. !$#submission submitted to the EMBL Data Library, July 1995 !$#description Nucleotide sequence of the cyanelle genome from Cyanophora !1paradoxa. !$#accession T06868 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-38 ##label STI !'##cross-references EMBL:U30821; NID:g1016083; PIDN:AAA81211.1; !1PID:g1016124 !'##experimental_source strain Pringsheim LB555 GENETICS !$#gene psbL; psbH !$#genome cyanelle CLASSIFICATION #superfamily photosystem II protein psbL KEYWORDS cyanelle; photosynthesis; photosystem II; thylakoid; !1transmembrane protein FEATURE !$18-37 #domain transmembrane #status predicted #label TMM SUMMARY #length 38 #molecular-weight 4473 #checksum 7009 SEQUENCE /// ENTRY F2RZKS #type complete TITLE photosystem II protein psbK - rice chloroplast ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS JQ0203; S05083 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0203 !'##molecule_type DNA !'##residues 1-61 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05083 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-61 ##label HIR !'##cross-references EMBL:X15901; NID:g11957; PIDN:CAA34010.1; !1PID:g11961 !'##experimental_source cv. Nihonbare !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1989 GENETICS !$#gene psbK !$#genome chloroplast CLASSIFICATION #superfamily photosystem II protein psbK KEYWORDS chloroplast; photosystem II SUMMARY #length 61 #molecular-weight 6982 #checksum 5485 SEQUENCE /// ENTRY F2NTK #type complete TITLE photosystem II protein psbK precursor - common tobacco chloroplast ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 01-Nov-1996 ACCESSIONS A05064; S32616; S18007 REFERENCE A00149 !$#authors Sugiura, M. !$#submission submitted to the EMBL Data Library, August 1986 !$#accession A05064 !'##molecule_type DNA !'##residues 1-98 ##label SUG !'##cross-references EMBL:Z00044 !'##experimental_source cv. Bright Yellow 4 !'##note it is uncertain whether Met-1 or Met-38 is the initiator REFERENCE A38013 !$#authors Shinozaki, K.; Ohme, M.; Tanaka, M.; Wakasugi, T.; !1Hayashida, N.; Matsubayashi, T.; Zaita, N.; Chunwongse, J.; !1Obokata, J.; Yamaguchi-Shinozaki, K.; Ohto, C.; Torazawa, !1K.; Meng, B.Y.; Sugita, M.; Deno, H.; Kamogashira, T.; !1Yamada, K.; Kusuda, J.; Takaiwa, F.; Kato, A.; Tohdoh, N.; !1Shimada, H.; Sugiura, M. !$#journal EMBO J. (1986) 5:2043-2049 !$#title The complete nucleotide sequence of the tobacco chloroplast !1genome: its gene organization and expression. !$#contents annotation; gene organization, sites, features REFERENCE S32616 !$#authors Murata, N. !$#submission submitted to the EMBL Data Library, September 1988 !$#accession S32616 !'##molecule_type DNA !'##residues 1-98 ##label MUR !'##cross-references EMBL:X12786 GENETICS !$#gene psbK !$#genome chloroplast !$#start_codon GTG CLASSIFICATION #superfamily photosystem II protein psbK KEYWORDS chloroplast; membrane-associated complex; photosynthesis; !1photosystem II; thylakoid FEATURE !$62-98 #product photosystem II protein psbK #status !8predicted #label MAT SUMMARY #length 98 #molecular-weight 11229 #checksum 3693 SEQUENCE /// ENTRY F2YB2K #type complete TITLE photosystem II protein psbK precursor - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein sml0005 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jun-2000 ACCESSIONS S14917; A40531; S75161; S08051 REFERENCE S14917 !$#authors Zhang, Z.H.; Mayes, S.R.; Barber, J. !$#journal Nucleic Acids Res. (1990) 18:1284 !$#title Nucleotide sequence of the psbK gene of the cyanobacterium !1Synechocystis 6803. !$#cross-references MUID:90206790; PMID:2108431 !$#accession S14917 !'##molecule_type DNA !'##residues 1-45 ##label ZHA !'##cross-references EMBL:X51588; NID:g40777; PIDN:CAA35938.1; !1PID:g40778 REFERENCE A40531 !$#authors Ikeuchi, M.; Eggers, B.; Shen, G.; Webber, A.; Yu, J.; !1Hirano, A.; Inoue, Y.; Vermaas, W. !$#journal J. Biol. Chem. (1991) 266:11111-11115 !$#title Cloning of the psbK gene from Synechocystis sp. PCC 6803 and !1characterization of photosystem II in mutants lacking !1PSII-K. !$#cross-references MUID:91250419; PMID:1904061 !$#accession A40531 !'##molecule_type DNA !'##residues 1-45 ##label IKE !'##cross-references GB:M74841; NID:g154486; PIDN:AAA27298.1; !1PID:g154487 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75161 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-45 ##label KAN !'##cross-references EMBL:D90903; GB:AB001339; NID:g1652127; !1PIDN:BAA17075.1; PID:g1652151 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene psbK CLASSIFICATION #superfamily photosystem II protein psbK KEYWORDS membrane protein; photosynthesis; photosystem II; thylakoid FEATURE !$9-45 #product photosystem II protein psbK #status !8experimental #label MAT SUMMARY #length 45 #molecular-weight 5112 #checksum 7796 SEQUENCE /// ENTRY QJSP6A #type complete TITLE photosystem II chlorophyll a-binding protein psbB - spinach chloroplast ORGANISM #formal_name chloroplast Spinacia oleracea #common_name spinach DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 31-Dec-1993 ACCESSIONS A03470 REFERENCE A03470 !$#authors Morris, J.; Herrmann, R.G. !$#journal Nucleic Acids Res. (1984) 12:2837-2850 !$#title Nucleotide sequence of the gene for the P-680 chlorophyll !1alpha apoprotein of the photosystem II reaction center from !1spinach. !$#cross-references MUID:84169576; PMID:6324128 !$#accession A03470 !'##molecule_type DNA !'##residues 1-508 ##label MOR !'##note the authors translated the codons ACT for residues 436, 452, !1and 502, ACC for residue 473, and ACA for residue 503 as Ser COMMENT This thylakoid membrane protein conjugates with chlorophyll !1and catalyzes the primary light-induced photochemical !1processes of photosystem II. GENETICS !$#genome chloroplast CLASSIFICATION #superfamily photosystem II chlorophyll a-binding protein !1psbB KEYWORDS chlorophyll; chloroplast; membrane protein; photosynthesis; !1photosystem II; thylakoid SUMMARY #length 508 #molecular-weight 56350 #checksum 2072 SEQUENCE /// ENTRY QJNT6A #type complete TITLE photosystem II chlorophyll a-binding protein psbB - common tobacco chloroplast ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 17-Feb-1995 ACCESSIONS A03471 REFERENCE A00149 !$#authors Sugiura, M. !$#submission submitted to the EMBL Data Library, August 1986 !$#accession A03471 !'##molecule_type DNA !'##residues 1-508 ##label SUG !'##experimental_source cv. Bright Yellow 4 REFERENCE A38013 !$#authors Shinozaki, K.; Ohme, M.; Tanaka, M.; Wakasugi, T.; !1Hayashida, N.; Matsubayashi, T.; Zaita, N.; Chunwongse, J.; !1Obokata, J.; Yamaguchi-Shinozaki, K.; Ohto, C.; Torazawa, !1K.; Meng, B.Y.; Sugita, M.; Deno, H.; Kamogashira, T.; !1Yamada, K.; Kusuda, J.; Takaiwa, F.; Kato, A.; Tohdoh, N.; !1Shimada, H.; Sugiura, M. !$#journal EMBO J. (1986) 5:2043-2049 !$#title The complete nucleotide sequence of the tobacco chloroplast !1genome: its gene organization and expression. !$#contents annotation; gene organization, sites, features COMMENT This thylakoid membrane protein conjugates with chlorophyll !1and catalyzes the primary light-induced photochemical !1processes of photosystem II. GENETICS !$#gene psbB !$#genome chloroplast CLASSIFICATION #superfamily photosystem II chlorophyll a-binding protein !1psbB KEYWORDS chlorophyll; chloroplast; membrane protein; photosynthesis; !1photosystem II; thylakoid SUMMARY #length 508 #molecular-weight 56015 #checksum 240 SEQUENCE /// ENTRY QJRZ6A #type complete TITLE photosystem II chlorophyll a-binding protein psbB - rice chloroplast ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS JQ0252; S05132 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0252 !'##molecule_type DNA !'##residues 1-508 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05132 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-508 ##label HIR !'##cross-references EMBL:X15901; NID:g11957; PIDN:CAA33973.1; !1PID:g12013 !'##experimental_source cv. Nihonbare !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1989 GENETICS !$#gene psbB !$#genome chloroplast CLASSIFICATION #superfamily photosystem II chlorophyll a-binding protein !1psbB KEYWORDS chlorophyll; chloroplast; membrane protein; photosynthesis; !1photosystem II; thylakoid SUMMARY #length 508 #molecular-weight 55999 #checksum 1802 SEQUENCE /// ENTRY QJZMBB #type complete TITLE photosystem II chlorophyll a-binding protein psbB - maize chloroplast ALTERNATE_NAMES photosystem II 47K protein ORGANISM #formal_name chloroplast Zea mays #common_name maize DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jul-1999 ACCESSIONS S07171; S58577 REFERENCE S07171 !$#authors Rock, C.D.; Barkan, A.; Taylor, W.C. !$#journal Curr. Genet. (1987) 12:69-77 !$#title The maize plastid psbB-psbF-petB-petD gene cluster: spliced !1and unspliced petB and petD RNAs encode alternative !1products. !$#cross-references MUID:88210525; PMID:2835175 !$#accession S07171 !'##molecule_type DNA !'##residues 1-508 ##label ROC !'##cross-references EMBL:X05422; NID:g12434; PIDN:CAA28997.1; !1PID:g12435 REFERENCE S58531 !$#authors Maier, R.M.; Neckermann, K.; Igloi, G.L.; Koessel, H. !$#journal J. Mol. Biol. (1995) 251:614-628 !$#title Complete sequence of the maize chloroplast genome: gene !1content, hotspots of divergence and fine tuning of genetic !1information by transcript editing. !$#cross-references MUID:95395841; PMID:7666415 !$#accession S58577 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-508 ##label MAI !'##cross-references EMBL:X86563; NID:g902200; PIDN:CAA60311.1; !1PID:g902247 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1995 GENETICS !$#gene psbB !$#genome chloroplast CLASSIFICATION #superfamily photosystem II chlorophyll a-binding protein !1psbB KEYWORDS chlorophyll; chloroplast; membrane-associated complex; !1photosynthesis; photosystem II; thylakoid SUMMARY #length 508 #molecular-weight 56106 #checksum 1175 SEQUENCE /// ENTRY QJMWPB #type complete TITLE photosystem II chlorophyll a-binding protein psbB precursor - Prochlorothrix hollandica ALTERNATE_NAMES photosystem II CP-47 protein ORGANISM #formal_name Prochlorothrix hollandica DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS S17739 REFERENCE S17739 !$#authors Greer, K.L.; Golden, S.S. !$#journal Plant Mol. Biol. (1991) 17:915-917 !$#title Nucleotide sequence of psbB from Prochlorothrix hollandica. !$#cross-references MUID:92003701; PMID:1840692 !$#accession S17739 !'##molecule_type DNA !'##residues 1-514 ##label GRE !'##cross-references EMBL:X59614; NID:g45537; PIDN:CAA42177.1; !1PID:g45538 !'##note the authors translated the codon CCC for residue 134 as O GENETICS !$#gene psbB CLASSIFICATION #superfamily photosystem II chlorophyll a-binding protein !1psbB KEYWORDS chlorophyll; photosynthesis; photosystem II; transmembrane !1protein FEATURE !$19-40 #domain transmembrane #status predicted #label TM1\ !$104-120 #domain transmembrane #status predicted #label TM2\ !$146-162 #domain transmembrane #status predicted #label TM3\ !$211-227 #domain transmembrane #status predicted #label TM4\ !$245-261 #domain transmembrane #status predicted #label TM5\ !$459-475 #domain transmembrane #status predicted #label TM6 SUMMARY #length 514 #molecular-weight 56856 #checksum 5321 SEQUENCE /// ENTRY QJLV6A #type complete TITLE photosystem II chlorophyll a-binding protein psbB - liverwort (Marchantia polymorpha) chloroplast ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 16-Jul-1999 ACCESSIONS A03472; S01548 REFERENCE A00150 !$#authors Ohyama, K. !$#submission submitted to the EMBL Data Library, October 1986 !$#accession A03472 !'##molecule_type DNA !'##residues 1-508 ##label OHY REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features REFERENCE S01529 !$#authors Fukuzawa, H.; Kohchi, T.; Sano, T.; Shirai, H.; Umesono, K.; !1Inokuchi, H.; Ozeki, H.; Ohyama, K. !$#journal J. Mol. Biol. (1988) 203:333-351 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. III. Gene organization of the large !1single copy region from rbcL to trnI(CAU). !$#cross-references MUID:89068687; PMID:3199436 !$#accession S01548 !'##molecule_type DNA !'##residues 1-508 ##label FUK !'##cross-references EMBL:X04465; NID:g11640; PIDN:CAA28110.1; !1PID:g11700 COMMENT This thylakoid membrane protein conjugates with chlorophyll !1and catalyzes the primary light-induced photochemical !1processes of photosystem II. GENETICS !$#gene psbB !$#genome chloroplast CLASSIFICATION #superfamily photosystem II chlorophyll a-binding protein !1psbB KEYWORDS chlorophyll; chloroplast; membrane protein; photosynthesis; !1photosystem II; thylakoid SUMMARY #length 508 #molecular-weight 56224 #checksum 6872 SEQUENCE /// ENTRY F2NT44 #type complete TITLE photosystem II chlorophyll a-binding protein psbC precursor - common tobacco chloroplast ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 16-Jul-1999 ACCESSIONS A03473 REFERENCE A00149 !$#authors Sugiura, M. !$#submission submitted to the EMBL Data Library, August 1986 !$#accession A03473 !'##molecule_type DNA !'##residues 1-473 ##label SUG !'##experimental_source cv. Bright Yellow 4 REFERENCE A38013 !$#authors Shinozaki, K.; Ohme, M.; Tanaka, M.; Wakasugi, T.; !1Hayashida, N.; Matsubayashi, T.; Zaita, N.; Chunwongse, J.; !1Obokata, J.; Yamaguchi-Shinozaki, K.; Ohto, C.; Torazawa, !1K.; Meng, B.Y.; Sugita, M.; Deno, H.; Kamogashira, T.; !1Yamada, K.; Kusuda, J.; Takaiwa, F.; Kato, A.; Tohdoh, N.; !1Shimada, H.; Sugiura, M. !$#journal EMBO J. (1986) 5:2043-2049 !$#title The complete nucleotide sequence of the tobacco chloroplast !1genome: its gene organization and expression. !$#contents annotation; gene organization, sites, features GENETICS !$#gene psbC !$#genome chloroplast CLASSIFICATION #superfamily photosystem II chlorophyll a-binding protein !1psbC KEYWORDS acetylated amino end; chlorophyll; chloroplast; !1phosphoprotein; photosynthesis; photosystem II; thylakoid FEATURE !$1-14 #domain transit peptide (thylakoid) #status predicted !8#label TRP\ !$15-473 #product photosystem II chlorophyll a-binding protein !8psbC #status predicted #label MAT\ !$15 #modified_site acetylated amino end (Thr) (in mature !8form) #status predicted\ !$15 #binding_site phosphate (Thr) (covalent) #status !8predicted SUMMARY #length 473 #molecular-weight 51909 #checksum 4999 SEQUENCE /// ENTRY F2RZ44 #type complete TITLE photosystem II chlorophyll a-binding protein psbC precursor - rice chloroplast ALTERNATE_NAMES photosystem II 44K protein ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS JQ0207; S05087 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0207 !'##molecule_type DNA !'##residues 1-473 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05087 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-473 ##label HIR !'##cross-references EMBL:X15901; NID:g11957; PIDN:CAA34014.1; !1PID:g11965 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1989 GENETICS !$#gene psbC !$#genome chloroplast CLASSIFICATION #superfamily photosystem II chlorophyll a-binding protein !1psbC KEYWORDS acetylated amino end; chlorophyll; chloroplast; !1phosphoprotein; photosynthesis; photosystem II; thylakoid FEATURE !$1-14 #domain transit peptide (thylakoid) #status predicted !8#label TRP\ !$15-473 #product photosystem II chlorophyll a-binding protein !8psbC #status predicted #label MAT\ !$15 #modified_site acetylated amino end (Thr) (in mature !8form) #status predicted\ !$15 #binding_site phosphate (Thr) (covalent) #status !8predicted SUMMARY #length 473 #molecular-weight 52076 #checksum 5013 SEQUENCE /// ENTRY F2LV44 #type complete TITLE photosystem II chlorophyll a-binding protein psbC precursor - liverwort (Marchantia polymorpha) chloroplast ALTERNATE_NAMES photosystem II 44K protein ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 03-Dec-1999 ACCESSIONS A03474; S01594 REFERENCE A00150 !$#authors Ohyama, K. !$#submission submitted to the EMBL Data Library, October 1986 !$#accession A03474 !'##molecule_type DNA !'##residues 1-473 ##label OHY REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features REFERENCE S01567 !$#authors Umesono, K.; Inokuchi, H.; Shiki, Y.; Takeuchi, M.; Chang, !1Z.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Ohyama, K.; Ozeki, !1H. !$#journal J. Mol. Biol. (1988) 203:299-331 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. II. Gene organization of the large !1single copy region from rps'12 to atpB. !$#cross-references MUID:89068686; PMID:2974085 !$#accession S01594 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-473 ##label UME !'##cross-references GB:X04465; GB:Y00686; NID:g11640; PIDN:CAA28081.1; !1PID:g11668 GENETICS !$#gene psbC !$#genome chloroplast CLASSIFICATION #superfamily photosystem II chlorophyll a-binding protein !1psbC KEYWORDS acetylated amino end; chlorophyll; chloroplast; !1membrane-associated complex; phosphoprotein; photosynthesis; !1photosystem II; thylakoid FEATURE !$1-14 #domain transit peptide (thylakoid) #status predicted !8#label TRP\ !$15-473 #product photosystem II chlorophyll a-binding protein !8psbC #status predicted #label MAT\ !$15 #modified_site acetylated amino end (Thr) (in mature !8form) #status predicted\ !$15 #binding_site phosphate (Thr) (covalent) #status !8predicted SUMMARY #length 473 #molecular-weight 51785 #checksum 2457 SEQUENCE /// ENTRY F2SP44 #type complete TITLE photosystem II chlorophyll a-binding protein psbC precursor - spinach chloroplast ALTERNATE_NAMES photosystem II chain CPa-2 ORGANISM #formal_name chloroplast Spinacia oleracea #common_name spinach DATE 28-Dec-1987 #sequence_revision 03-Oct-1995 #text_change 16-Jul-1999 ACCESSIONS B23038; S00416; S12197 REFERENCE A93547 !$#authors Holschuh, K.; Bottomley, W.; Whitfeld, P.R. !$#journal Nucleic Acids Res. (1984) 12:8819-8834 !$#title Structure of the spinach chloroplast genes for the D2 and 44 !1kd reaction-centre proteins of photosystem II and for !1tRNA-Ser (UGA). !$#cross-references MUID:85087902; PMID:6096808 !$#accession B23038 !'##molecule_type DNA !'##residues 1-473 ##label HOL !'##cross-references GB:X01724; NID:g12279; PIDN:CAA25864.1; PID:g12281 !'##note the codon given for 425-Trp (UGU) is inconsistent with the !1authors' translation REFERENCE S00416 !$#authors Alt, J.; Morris, J.; Westhoff, P.; Herrmann, R.G. !$#journal Curr. Genet. (1984) 8:597-606 !$#title Nucleotide sequence of the clustered genes for the 44kd !1chlorophyll a apoprotein and the "32kd"-like protein of the !1photosystem II reaction center in the spinach plastid !1chromosome. !$#accession S00416 !'##molecule_type DNA !'##residues 1-473 ##label ALT !'##cross-references EMBL:M36833; NID:g343360; PIDN:AAA84631.1; !1PID:g343362 !'##note it is uncertain whether Met-1 is the initiator or whether !1translation is initiated at 13-Val (GTG) REFERENCE S09185 !$#authors Michel, H.; Hunt, D.F.; Shabanowitz, J.; Bennett, J. !$#journal J. Biol. Chem. (1988) 263:1123-1130 !$#title Tandem mass spectrometry reveals that three photosystem II !1proteins of spinach chloroplasts contain !1N-acetyl-O-phosphothreonine at their NH(2) termini. !$#cross-references MUID:88087237; PMID:3121625 !$#accession S12197 !'##molecule_type protein !'##residues 15-26 ##label MIC GENETICS !$#gene psbC !$#genome chloroplast CLASSIFICATION #superfamily photosystem II chlorophyll a-binding protein !1psbC KEYWORDS acetylated amino end; chlorophyll; chloroplast; !1phosphoprotein; photosynthesis; photosystem II; thylakoid FEATURE !$1-14 #domain transit peptide (thylakoid) #status predicted !8#label TRP\ !$15-473 #product photosystem II chlorophyll a-binding protein !8psbC #status experimental #label MAT\ !$15 #binding_site phosphate (Thr) (covalent) #status !8experimental\ !$15 #modified_site acetylated amino end (Thr) (in mature !8form) #status experimental SUMMARY #length 473 #molecular-weight 51833 #checksum 5197 SEQUENCE /// ENTRY F2KK4C #type complete TITLE photosystem II chlorophyll a-binding protein psbC precursor - red alga (Cyanidium caldarium) chloroplast ORGANISM #formal_name chloroplast Cyanidium caldarium DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS S20856; S25086 REFERENCE S20854 !$#authors Kessler, U.; Maid, U.; Zetsche, K. !$#journal Plant Mol. Biol. (1992) 18:777-780 !$#title An equivalent to bacterial ompR genes is encoded on the !1plastid genome of red algae. !$#cross-references MUID:92216053; PMID:1558950 !$#accession S20856 !'##status translation not shown !'##molecule_type DNA !'##residues 1-473 ##label KES !'##cross-references EMBL:X62578; NID:g11278; PIDN:CAA44460.1; !1PID:g11281 REFERENCE S25084 !$#authors Maid, U.; Zetsche, K. !$#journal Plant Mol. Biol. (1992) 19:1001-1010 !$#title A 16 kb small single-copy region separates the plastid DNA !1inverted repeat of the unicellular red alga Cyanidium !1caldarium: physical mapping of the IR-flanking regions and !1nucleotide sequences of the psbD-psbC, rps16, 5S rRNA and !1rpl21 genes. !$#cross-references MUID:92379254; PMID:1511125 !$#accession S25086 !'##molecule_type DNA !'##residues 1-473 ##label MAI !'##cross-references EMBL:X62578; NID:g11278; PIDN:CAA44460.1; !1PID:g11281 GENETICS !$#gene psbC !$#genome chloroplast CLASSIFICATION #superfamily photosystem II chlorophyll a-binding protein !1psbC KEYWORDS chlorophyll; chloroplast; photosynthesis; photosystem II; !1thylakoid FEATURE !$1-14 #domain transit peptide (thylakoid) #status predicted !8#label TRP\ !$15-473 #product photosystem II chlorophyll a-binding protein !8psbC #status predicted #label MAT SUMMARY #length 473 #molecular-weight 52487 #checksum 4379 SEQUENCE /// ENTRY F2MU10 #type complete TITLE photosystem II 10K protein precursor - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS S17430; T01051 REFERENCE S17430 !$#authors Gil-Gomez, G.; Marrero, P.F.; Haro, D.; Ayte, J.; Hegardt, !1F.G. !$#journal Plant Mol. Biol. (1991) 17:517-522 !$#title Characterization of the gene encoding the 10 kDa polypeptide !1of photosystem II from Arabidopsis thaliana. !$#cross-references MUID:91355945; PMID:1884004 !$#accession S17430 !'##molecule_type DNA !'##residues 1-140 ##label GIL !'##cross-references EMBL:X55970; NID:g16446; PIDN:CAA39441.1; !1PID:g16447 !'##note the authors translated the codon AAC for residue 56 as Lys REFERENCE Z14227 !$#authors Theologis, A.; Vysotskaia, V.S.; Osborne, B.I.; Schwartz, !1J.R.; Federspiel, N.A.; Kwan, A.; Toriumi, M.; Yu, G.; Oji, !1O.; Araujo, R.; Chung, E.; Dewer, K.; Dietrich, F.; Ecker, !1J.R.; Marziali, A.; Oefner, P.; Davis, R.W. !$#submission submitted to the EMBL Data Library, May 1998 !$#description Arabidopsis thaliana chromosome 1 YAC YUP8H12R sequence. !$#accession T01051 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-140 ##label THE !'##cross-references EMBL:AC002986; NID:g2494106; PIDN:AAC17052.1; !1PID:g3152571 GENETICS !$#gene art1 !$#map_position I !$#introns 54/1; 74/1; 92/2 !$#note YUP8H12R.34 CLASSIFICATION #superfamily photosystem II 10K protein KEYWORDS chloroplast; glycoprotein; photosynthesis; photosystem II; !1thylakoid FEATURE !$1-41 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$42-140 #product photosystem II 10K protein #status predicted !8#label MAT\ !$134 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 140 #molecular-weight 14586 #checksum 237 SEQUENCE /// ENTRY F2NT0P #type complete TITLE photosystem II phosphoprotein psbH - common tobacco chloroplast ORGANISM #formal_name chloroplast Nicotiana tabacum #common_name common tobacco DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 16-Feb-1997 ACCESSIONS A03475 REFERENCE A00149 !$#authors Sugiura, M. !$#submission submitted to the EMBL Data Library, August 1986 !$#accession A03475 !'##molecule_type DNA !'##residues 1-73 ##label SUG !'##experimental_source cv. Bright Yellow 4 REFERENCE A38013 !$#authors Shinozaki, K.; Ohme, M.; Tanaka, M.; Wakasugi, T.; !1Hayashida, N.; Matsubayashi, T.; Zaita, N.; Chunwongse, J.; !1Obokata, J.; Yamaguchi-Shinozaki, K.; Ohto, C.; Torazawa, !1K.; Meng, B.Y.; Sugita, M.; Deno, H.; Kamogashira, T.; !1Yamada, K.; Kusuda, J.; Takaiwa, F.; Kato, A.; Tohdoh, N.; !1Shimada, H.; Sugiura, M. !$#journal EMBO J. (1986) 5:2043-2049 !$#title The complete nucleotide sequence of the tobacco chloroplast !1genome: its gene organization and expression. !$#contents annotation; gene organization, sites, features GENETICS !$#gene psbH !$#genome chloroplast CLASSIFICATION #superfamily photosystem II phosphoprotein psbH KEYWORDS chloroplast; phosphoprotein; photosystem II; transmembrane !1protein SUMMARY #length 73 #molecular-weight 7759 #checksum 6470 SEQUENCE /// ENTRY F2RZ0P #type complete TITLE photosystem II phosphoprotein psbH - rice chloroplast ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS JQ0253; S05133; S01905 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0253 !'##molecule_type DNA !'##residues 1-73 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05133 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-73 ##label HIR !'##cross-references EMBL:X15901; NID:g11957; PIDN:CAA33976.1; !1PID:g12016 !'##experimental_source cv. Nihonbare REFERENCE S01905 !$#authors Cote, J.C.; Wu, R. !$#journal Nucleic Acids Res. (1988) 16:10384 !$#title Sequence of the chloroplast psbF gene encoding the !1photosystem II 10kDa phosphoprotein from Oryza sativa L. !$#cross-references MUID:89057496; PMID:3057446 !$#accession S01905 !'##molecule_type DNA !'##residues 1-73 ##label COT !'##cross-references EMBL:X12695; NID:g11952; PIDN:CAA31204.1; !1PID:g11953 !'##note the authors designated the gene coding for this protein as psbF GENETICS !$#gene psbH !$#map_position CP70881-71102 !$#genome chloroplast CLASSIFICATION #superfamily photosystem II phosphoprotein psbH KEYWORDS chloroplast; phosphoprotein; photosystem II; transmembrane !1protein SUMMARY #length 73 #molecular-weight 7886 #checksum 6504 SEQUENCE /// ENTRY F2ZMBH #type complete TITLE photosystem II phosphoprotein psbH - maize chloroplast ALTERNATE_NAMES photosystem II 10K phosphoprotein; photosystem II phosphoprotein psbF ORGANISM #formal_name chloroplast Zea mays #common_name maize DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jul-1999 ACCESSIONS S08591; S58580 REFERENCE S07171 !$#authors Rock, C.D.; Barkan, A.; Taylor, W.C. !$#journal Curr. Genet. (1987) 12:69-77 !$#title The maize plastid psbB-psbF-petB-petD gene cluster: spliced !1and unspliced petB and petD RNAs encode alternative !1products. !$#cross-references MUID:88210525; PMID:2835175 !$#accession S08591 !'##molecule_type DNA !'##residues 1-73 ##label ROC !'##cross-references EMBL:X05422; NID:g12434; PIDN:CAA28998.1; !1PID:g12436 REFERENCE S58531 !$#authors Maier, R.M.; Neckermann, K.; Igloi, G.L.; Koessel, H. !$#journal J. Mol. Biol. (1995) 251:614-628 !$#title Complete sequence of the maize chloroplast genome: gene !1content, hotspots of divergence and fine tuning of genetic !1information by transcript editing. !$#cross-references MUID:95395841; PMID:7666415 !$#accession S58580 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-73 ##label MAI !'##cross-references EMBL:X86563; NID:g902200; PIDN:CAA60314.1; !1PID:g902250 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1995 GENETICS !$#gene psbH; psbF !$#genome chloroplast CLASSIFICATION #superfamily photosystem II phosphoprotein psbH KEYWORDS chloroplast; membrane-associated complex; phosphoprotein; !1photosynthesis; photosystem II; thylakoid SUMMARY #length 73 #molecular-weight 7787 #checksum 5404 SEQUENCE /// ENTRY F2WTH #type complete TITLE photosystem II phosphoprotein psbH - wheat chloroplast ALTERNATE_NAMES photosystem II 10K phosphoprotein ORGANISM #formal_name chloroplast Triticum aestivum #common_name common wheat DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 21-Jan-2000 ACCESSIONS S14143; A33240; PW0016; A25648; S14960; S14565 REFERENCE S14140 !$#authors Hird, S.M.; Webber, A.N.; Wilson, R.J.; Dyer, T.A.; Gray, !1J.C. !$#journal Curr. Genet. (1991) 19:199-206 !$#title Differential expression of the psbB and psbH genes encoding !1the 47 kDa chlorophyll a-protein and the 10 kDa !1phosphoprotein of photosystem II during chloroplast !1development in wheat. !$#cross-references MUID:91330334; PMID:1714358 !$#accession S14143 !'##molecule_type DNA !'##residues 1-73 ##label HIR1 !'##cross-references EMBL:X54749; NID:g12356; PIDN:CAA38544.1; !1PID:g12360 !'##experimental_source cv. Sentry !$#accession A33240 !'##molecule_type protein !'##residues 'X',3-15 ##label HIR2 REFERENCE JG0010 !$#authors Webber, A.N.; Hird, S.M.; Packman, L.C.; Dyer, T.A.; Gray, !1J.C. !$#journal Plant Mol. Biol. (1989) 12:141-151 !$#title A photosystem II polypeptide is encoded by an open reading !1frame cotranscribed with genes for cytochrome b-559 in wheat !1chloroplast DNA. !$#accession PW0016 !'##molecule_type protein !'##residues 2-20,'X',22 ##label WEB REFERENCE A25648 !$#authors Hird, S.M.; Dyer, T.A.; Gray, J.C. !$#journal FEBS Lett. (1986) 209:181-186 !$#title The gene for the 10 kDa phosphoprotein of photosystem II is !1located in chloroplast DNA. !$#accession A25648 !'##molecule_type DNA !'##residues 1-73 ##label HIR3 !'##cross-references EMBL:X04710; NID:g12354; PIDN:CAA28415.1; !1PID:g12355 REFERENCE S14960 !$#authors Hird, S.M.; Wilson, R.J.; Dyer, T.A.; Gray, J.C. !$#journal Plant Mol. Biol. (1991) 16:745-747 !$#title Nucleotide sequence of the wheat chloroplast petB and petD !1genes encoding apocytochrome b-563 and subunit IV of the !1cytochrome bf complex. !$#cross-references MUID:91329710; PMID:1868207 !$#accession S14960 !'##molecule_type DNA !'##residues 59-73 ##label HIR !'##cross-references EMBL:X54751; NID:g12361; PIDN:CAA38550.1; !1PID:g12362 GENETICS !$#gene psbH !$#genome chloroplast CLASSIFICATION #superfamily photosystem II phosphoprotein psbH KEYWORDS chloroplast; phosphoprotein; photosynthesis; photosystem II; !1thylakoid; transmembrane protein FEATURE !$2-73 #product photosystem II phosphoprotein psbH #status !8experimental #label MAT SUMMARY #length 73 #molecular-weight 7787 #checksum 5418 SEQUENCE /// ENTRY F2RZM #type complete TITLE photosystem II protein psbM - rice chloroplast ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS JQ0211; S05091 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0211 !'##molecule_type DNA !'##residues 1-34 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05091 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-34 ##label HIR !'##cross-references EMBL:X15901; NID:g11957; PIDN:CAA33984.1; !1PID:g11969 !'##experimental_source cv. Nihonbare !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1989 GENETICS !$#gene psbM !$#genome chloroplast CLASSIFICATION #superfamily photosystem II protein psbM KEYWORDS chloroplast; photosynthesis; photosystem II; transmembrane !1protein SUMMARY #length 34 #molecular-weight 3783 #checksum 5979 SEQUENCE /// ENTRY F2RZN #type complete TITLE photosystem II protein psbN - rice chloroplast ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS JQ0255; S05135 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0255 !'##molecule_type DNA !'##residues 1-43 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05135 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-43 ##label HIR !'##cross-references EMBL:X15901; NID:g11957; PIDN:CAA33975.1; !1PID:g12015 !'##experimental_source cv. Nihonbare !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1989 GENETICS !$#gene psbN !$#genome chloroplast CLASSIFICATION #superfamily photosystem II protein psbN KEYWORDS chloroplast; photosystem II; transmembrane protein SUMMARY #length 43 #molecular-weight 4662 #checksum 1470 SEQUENCE /// ENTRY F2RZJ #type complete TITLE photosystem II protein psbJ - rice chloroplast ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS JQ0240; S05120 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0240 !'##molecule_type DNA !'##residues 1-40 ##label SHI !'##experimental_source cv. Nihonbare !'##note this protein is a possible PSII component REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05120 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-40 ##label HIR !'##cross-references EMBL:X15901; NID:g11957; PIDN:CAA33962.1; !1PID:g12001 !'##experimental_source cv. Nihonbare !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1989 GENETICS !$#gene psbJ !$#genome chloroplast CLASSIFICATION #superfamily photosystem II protein psbJ KEYWORDS chloroplast; photosystem II SUMMARY #length 40 #molecular-weight 4105 #checksum 3489 SEQUENCE /// ENTRY F2WT4J #type complete TITLE photosystem II 4K protein - wheat chloroplast ORGANISM #formal_name chloroplast Triticum aestivum #common_name common wheat DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS JG0011; S03624 REFERENCE JG0010 !$#authors Webber, A.N.; Hird, S.M.; Packman, L.C.; Dyer, T.A.; Gray, !1J.C. !$#journal Plant Mol. Biol. (1989) 12:141-151 !$#title A photosystem II polypeptide is encoded by an open reading !1frame cotranscribed with genes for cytochrome b-559 in wheat !1chloroplast DNA. !$#accession JG0011 !'##molecule_type DNA !'##residues 1-40 ##label WEB !'##cross-references EMBL:X15225; NID:g14259; PIDN:CAA33297.1; !1PID:g14263 GENETICS !$#genome chloroplast CLASSIFICATION #superfamily photosystem II protein psbJ KEYWORDS chloroplast; photosystem II; thylakoid; transmembrane !1protein FEATURE !$8-40 #domain transmembrane #status predicted #label TMM SUMMARY #length 40 #molecular-weight 4061 #checksum 3491 SEQUENCE /// ENTRY F2TOX2 #type complete TITLE photosystem II oxygen-evolving complex protein 2 precursor - tomato ALTERNATE_NAMES photosystem II oxygen-evolving complex 23K protein ORGANISM #formal_name Lycopersicon esculentum #common_name tomato DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS S20872 REFERENCE S20872 !$#authors Betts, S.; Pichersky, E. !$#journal Plant Mol. Biol. (1992) 18:995-996 !$#title Nucleotide sequence of cDNA encoding the precursor of the 23 !1kDa photosystem II protein of tomato. !$#cross-references MUID:92256823; PMID:1581578 !$#accession S20872 !'##molecule_type mRNA !'##residues 1-258 ##label BET !'##cross-references EMBL:X63007; NID:g19316; PIDN:CAA44736.1; !1PID:g19317 CLASSIFICATION #superfamily photosystem II oxygen-evolving complex protein !12 KEYWORDS chloroplast; photosynthesis; photosystem II; thylakoid FEATURE !$1-73 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$74-258 #product photosystem II oxygen-evolving complex !8protein 2 #status predicted #label MAT SUMMARY #length 258 #molecular-weight 27792 #checksum 9784 SEQUENCE /// ENTRY CDPJ25 #type complete TITLE chlorophyll a/b-binding protein 25 precursor - petunia ALTERNATE_NAMES light-harvesting complex Cab protein 25 ORGANISM #formal_name Petunia sp. #common_name petunia DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 16-Jul-1999 ACCESSIONS C22936 REFERENCE A93563 !$#authors Dunsmuir, P. !$#journal Nucleic Acids Res. (1985) 13:2503-2518 !$#title The petunia chlorophyll a/b binding protein genes: a !1comparison of Cab genes from different gene families. !$#cross-references MUID:85215630; PMID:2987856 !$#accession C22936 !'##molecule_type DNA !'##residues 1-266 ##label DUN !'##cross-references GB:X02358; NID:g20482; PIDN:CAA26211.1; PID:g20483 COMMENT The light-harvesting complex (LHC) of the higher plant !1chloroplast is a thylakoid membrane-bound complex consisting !1of the chlorophylls (a and b) and chlorophyll a-b binding !1proteins. Functioning in photosynthesis as a light receptor, !1the LHC captures and delivers excitation energy to the !1photosystems with which it is closely associated. COMMENT The Cab proteins, encoded by nuclear genes whose expression !1is regulated by light, are synthesized as soluble precursors !1in the stroma. They are transported into the thylakoid !1membrane (an ATP-dependent process) where the mature !1polypeptides are assembled in the LHC. The transition from !1cytoplasmic precursor to LHC component is accompanied by !1loss of a "transit peptide" from the precursor. COMMENT The amino peptide of the mature protein extends into the !1stroma where it is involved with adhesion of granal !1membranes (granal stacking) and photoregulated reversible !1phosphorylation of its threonine residues. Both are believed !1to mediate the distribution of excitation energy between !1photosystems I and II. GENETICS !$#gene Cab-25 CLASSIFICATION #superfamily chlorophyll a/b-binding protein KEYWORDS chloroplast; grana; light-harvesting complex; membrane !1adhesion; membrane protein; phosphoprotein; photosynthesis; !1photosystem I; photosystem II; thylakoid FEATURE !$1-33 #domain (or 1-34) transit peptide (chloroplast) !8#status predicted #label TNP\ !$34-266 #product (or 35-266) chlorophyll a/b-binding protein !825 #status predicted #label MAT SUMMARY #length 266 #molecular-weight 28167 #checksum 5399 SEQUENCE /// ENTRY CDPJ13 #type complete TITLE chlorophyll a/b-binding protein 13 precursor - petunia ALTERNATE_NAMES light-harvesting complex Cab protein 13 ORGANISM #formal_name Petunia sp. #common_name petunia DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 16-Jul-1999 ACCESSIONS B22936 REFERENCE A93563 !$#authors Dunsmuir, P. !$#journal Nucleic Acids Res. (1985) 13:2503-2518 !$#title The petunia chlorophyll a/b binding protein genes: a !1comparison of Cab genes from different gene families. !$#cross-references MUID:85215630; PMID:2987856 !$#accession B22936 !'##molecule_type DNA !'##residues 1-266 ##label DUN !'##cross-references GB:X02357; NID:g20470; PIDN:CAA26210.1; PID:g20471 COMMENT The light-harvesting complex (LHC) of the higher plant !1chloroplast is a thylakoid membrane-bound complex consisting !1of the chlorophylls (a and b) and chlorophyll a-b binding !1proteins. Functioning in photosynthesis as a light receptor, !1the LHC captures and delivers excitation energy to the !1photosystems with which it is closely associated. COMMENT The Cab proteins, encoded by nuclear genes whose expression !1is regulated by light, are synthesized as soluble precursors !1in the stroma. They are transported into the thylakoid !1membrane (an ATP-dependent process) where the mature !1polypeptides are assembled in the LHC. The transition from !1cytoplasmic precursor to LHC component is accompanied by !1loss of a "transit peptide" from the precursor. COMMENT The amino peptide of the mature protein extends into the !1stroma where it is involved with adhesion of granal !1membranes (granal stacking) and photoregulated reversible !1phosphorylation of its threonine residues. Both are believed !1to mediate the distribution of excitation energy between !1photosystems I and II. GENETICS !$#gene Cab-13 CLASSIFICATION #superfamily chlorophyll a/b-binding protein KEYWORDS chloroplast; grana; light-harvesting complex; membrane !1adhesion; membrane protein; phosphoprotein; photosynthesis; !1photosystem I; photosystem II; thylakoid FEATURE !$1-33 #domain (or 1-34) transit peptide (chloroplast) !8#status predicted #label TNP\ !$34-266 #product (or 35-266) chlorophyll a/b-binding protein !813 #status predicted #label MAT SUMMARY #length 266 #molecular-weight 28308 #checksum 6694 SEQUENCE /// ENTRY CDPJ91 #type complete TITLE chlorophyll a/b-binding protein 91R precursor - petunia ALTERNATE_NAMES light-harvesting complex Cab protein 91R ORGANISM #formal_name Petunia sp. #common_name petunia DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 16-Jul-1999 ACCESSIONS A22936 REFERENCE A93563 !$#authors Dunsmuir, P. !$#journal Nucleic Acids Res. (1985) 13:2503-2518 !$#title The petunia chlorophyll a/b binding protein genes: a !1comparison of Cab genes from different gene families. !$#cross-references MUID:85215630; PMID:2987856 !$#accession A22936 !'##molecule_type DNA !'##residues 1-267 ##label DUN !'##cross-references GB:X02356; NID:g20486; PIDN:CAA26209.1; PID:g20487 COMMENT The light-harvesting complex (LHC) of the higher plant !1chloroplast is a thylakoid membrane-bound complex consisting !1of the chlorophylls (a and b) and chlorophyll a-b binding !1proteins. Functioning in photosynthesis as a light receptor, !1the LHC captures and delivers excitation energy to the !1photosystems with which it is closely associated. COMMENT The Cab proteins, encoded by nuclear genes whose expression !1is regulated by light, are synthesized as soluble precursors !1in the stroma. They are transported into the thylakoid !1membrane (an ATP-dependent process) where the mature !1polypeptides are assembled in the LHC. The transition from !1cytoplasmic precursor to LHC component is accompanied by !1loss of a "transit peptide" from the precursor. COMMENT The amino peptide of the mature protein extends into the !1stroma where it is involved with adhesion of granal !1membranes (granal stacking) and photoregulated reversible !1phosphorylation of its threonine residues. Both are believed !1to mediate the distribution of excitation energy between !1photosystems I and II. GENETICS !$#gene Cab-91R CLASSIFICATION #superfamily chlorophyll a/b-binding protein KEYWORDS chloroplast; grana; light-harvesting complex; membrane !1adhesion; membrane protein; phosphoprotein; photosynthesis; !1photosystem I; photosystem II; thylakoid FEATURE !$1-34 #domain (or 1-35) transit peptide (chloroplast) !8#status predicted #label TNP\ !$35-267 #product (or 36-267) chlorophyll a/b-binding protein !891R #status predicted #label MAT SUMMARY #length 267 #molecular-weight 28383 #checksum 9464 SEQUENCE /// ENTRY CDPJ2R #type complete TITLE chlorophyll a/b-binding protein 22R precursor - petunia ALTERNATE_NAMES light-harvesting complex Cab protein 22R ORGANISM #formal_name Petunia sp. #common_name petunia DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 16-Jul-1999 ACCESSIONS E22936 REFERENCE A93563 !$#authors Dunsmuir, P. !$#journal Nucleic Acids Res. (1985) 13:2503-2518 !$#title The petunia chlorophyll a/b binding protein genes: a !1comparison of Cab genes from different gene families. !$#cross-references MUID:85215630; PMID:2987856 !$#accession E22936 !'##molecule_type DNA !'##residues 1-267 ##label DUN !'##cross-references GB:X02360; NID:g20478; PIDN:CAA26213.1; PID:g20479 COMMENT The light-harvesting complex (LHC) of the higher plant !1chloroplast is a thylakoid membrane-bound complex consisting !1of the chlorophylls (a and b) and chlorophyll a-b binding !1proteins. Functioning in photosynthesis as a light receptor, !1the LHC captures and delivers excitation energy to the !1photosystems with which it is closely associated. COMMENT The Cab proteins, encoded by nuclear genes whose expression !1is regulated by light, are synthesized as soluble precursors !1in the stroma. They are transported into the thylakoid !1membrane (an ATP-dependent process) where the mature !1polypeptides are assembled in the LHC. The transition from !1cytoplasmic precursor to LHC component is accompanied by !1loss of a "transit peptide" from the precursor. COMMENT The amino peptide of the mature protein extends into the !1stroma where it is involved with adhesion of granal !1membranes (granal stacking) and photoregulated reversible !1phosphorylation of its threonine residues. Both are believed !1to mediate the distribution of excitation energy between !1photosystems I and II. GENETICS !$#gene Cab-22R CLASSIFICATION #superfamily chlorophyll a/b-binding protein KEYWORDS chloroplast; grana; light-harvesting complex; membrane !1adhesion; membrane protein; phosphoprotein; photosynthesis; !1photosystem I; photosystem II; thylakoid FEATURE !$1-34 #domain (or 1-35) transit peptide (chloroplast) !8#status predicted #label TNP\ !$35-267 #product (or 36-267) chlorophyll a/b-binding protein !822R #status predicted #label MAT SUMMARY #length 267 #molecular-weight 28407 #checksum 9610 SEQUENCE /// ENTRY CDTO3C #type complete TITLE chlorophyll a/b-binding protein 3C precursor - tomato ALTERNATE_NAMES light-harvesting complex Cab protein 3C ORGANISM #formal_name Lycopersicon esculentum #common_name tomato DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 25-Oct-1996 ACCESSIONS G24039 REFERENCE A24039 !$#authors Pichersky, E.; Bernatzky, R.; Tanksley, S.D.; Breidenbach, !1R.B.; Kausch, A.P.; Cashmore, A.R. !$#journal Gene (1985) 40:247-258 !$#title Molecular characterization and genetic mapping of two !1clusters of genes encoding chlorophyll a/b-binding proteins !1in Lycopersicon esculentum (tomato). !$#cross-references MUID:86165866; PMID:3007291 !$#accession G24039 !'##molecule_type DNA !'##residues 1-267 ##label PIC !'##experimental_source cv. T6 COMMENT The light-harvesting complex (LHC) of the higher plant !1chloroplast is a thylakoid membrane-bound complex consisting !1of the chlorophylls (a and b) and chlorophyll a/b-binding !1proteins. Functioning in photosynthesis as a light receptor, !1the LHC captures and delivers excitation energy to the !1photosystems with which it is closely associated. COMMENT The amino peptide of the mature protein extends into the !1stroma where it is involved with adhesion of granal !1membranes (granal stacking) and photoregulated reversible !1phosphorylation of its threonine residues. Both are believed !1to mediate the distribution of excitation energy between !1photosystems I and II. GENETICS !$#gene Cab-3C !$#map_position 3 CLASSIFICATION #superfamily chlorophyll a/b-binding protein KEYWORDS chloroplast; grana; light-harvesting complex; membrane !1adhesion; membrane protein; phosphoprotein; photosynthesis; !1photosystem I; photosystem II; thylakoid FEATURE !$1-34 #domain (or 1-35) transit peptide (chloroplast) !8#status predicted #label TNP\ !$35-267 #product (or 36-267) chlorophyll a/b-binding protein !83C #status predicted #label MAT SUMMARY #length 267 #molecular-weight 28325 #checksum 7927 SEQUENCE /// ENTRY CDNTCC #type complete TITLE chlorophyll a/b-binding protein type I precursor (cab-C) - curled-leaved tobacco ALTERNATE_NAMES light-harvesting complex apoprotein cab ORGANISM #formal_name Nicotiana plumbaginifolia #common_name curled-leaved tobacco DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS S07940 REFERENCE S07404 !$#authors Castresana, C.; Staneloni, R.; Malik, V.S.; Cashmore, A.R. !$#journal Plant Mol. Biol. (1987) 10:117-126 !$#title Molecular characterization of two clusters of genes encoding !1the type I CAB polypeptides of PSII in Nicotiana !1plumbaginifolia. !$#accession S07940 !'##molecule_type DNA !'##residues 1-267 ##label CAS !'##cross-references EMBL:M21397; NID:g170209; PIDN:AAA34055.1; !1PID:g170210 GENETICS !$#gene cab-C CLASSIFICATION #superfamily chlorophyll a/b-binding protein KEYWORDS chlorophyll; chloroplast; light-harvesting complex; !1photosystem II; thylakoid; transmembrane protein FEATURE !$1-34 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$35-267 #product chlorophyll a/b-binding protein type I !8(cab-C) #status predicted #label MAT SUMMARY #length 267 #molecular-weight 28369 #checksum 819 SEQUENCE /// ENTRY CDNTEC #type complete TITLE chlorophyll a/b-binding protein type I precursor (cab-E) - curled-leaved tobacco ALTERNATE_NAMES light-harvesting complex apoprotein cab ORGANISM #formal_name Nicotiana plumbaginifolia #common_name curled-leaved tobacco DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS S07404 REFERENCE S07404 !$#authors Castresana, C.; Staneloni, R.; Malik, V.S.; Cashmore, A.R. !$#journal Plant Mol. Biol. (1987) 10:117-126 !$#title Molecular characterization of two clusters of genes encoding !1the type I CAB polypeptides of PSII in Nicotiana !1plumbaginifolia. !$#accession S07404 !'##molecule_type DNA !'##residues 1-266 ##label CAS !'##cross-references EMBL:M21398; NID:g170211; PIDN:AAA34056.1; !1PID:g170212 GENETICS !$#gene cab-E CLASSIFICATION #superfamily chlorophyll a/b-binding protein KEYWORDS chlorophyll; chloroplast; light-harvesting complex; !1photosystem II; thylakoid; transmembrane protein FEATURE !$1-33 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$34-266 #product chlorophyll a/b-binding protein type I !8(cab-E) #status predicted #label MAT SUMMARY #length 266 #molecular-weight 28277 #checksum 6513 SEQUENCE /// ENTRY CDNT50 #type complete TITLE chlorophyll a/b-binding protein precursor (cab-50) - common tobacco ORGANISM #formal_name Nicotiana tabacum #common_name common tobacco DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS S11720 REFERENCE S11719 !$#authors Jin, D.S.; Bogorad, L. !$#submission submitted to the EMBL Data Library, April 1990 !$#description Cab Genes from Nicotiana tabacum. !$#accession S11720 !'##molecule_type mRNA !'##residues 1-267 ##label EMB !'##cross-references EMBL:X52742; NID:g19832; PIDN:CAA36956.1; !1PID:g19833 GENETICS !$#gene Cab50 CLASSIFICATION #superfamily chlorophyll a/b-binding protein KEYWORDS chlorophyll; chloroplast; light-harvesting complex; !1thylakoid; transmembrane protein FEATURE !$1-33 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$34-267 #product chlorophyll a/b-binding protein #status !8predicted #label MAT\ !$101-120 #domain transmembrane #status predicted #label TM1\ !$153-173 #domain transmembrane #status predicted #label TM2\ !$221-237 #domain transmembrane #status predicted #label TM3 SUMMARY #length 267 #molecular-weight 28347 #checksum 260 SEQUENCE /// ENTRY CDNT16 #type complete TITLE chlorophyll a/b-binding protein precursor (cab-16) - common tobacco ORGANISM #formal_name Nicotiana tabacum #common_name common tobacco DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 23-Mar-2001 ACCESSIONS S11721 REFERENCE S11719 !$#authors Jin, D.S.; Bogorad, L. !$#submission submitted to the EMBL Data Library, April 1990 !$#description Cab Genes from Nicotiana tabacum. !$#accession S11721 !'##molecule_type mRNA !'##residues 1-266 ##label EMB !'##cross-references EMBL:X52741; NID:g19818; PIDN:CAA36955.1; !1PID:g19819 GENETICS !$#gene Cab16 CLASSIFICATION #superfamily chlorophyll a/b-binding protein KEYWORDS chlorophyll; chloroplast; light-harvesting complex; !1thylakoid; transmembrane protein FEATURE !$1-32 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$33-266 #product chlorophyll a/b-binding protein #status !8predicted #label MAT\ !$100-119 #domain transmembrane #status predicted #label TM1\ !$152-172 #domain transmembrane #status predicted #label TM2\ !$220-236 #domain transmembrane #status predicted #label TM3 SUMMARY #length 266 #molecular-weight 28178 #checksum 6711 SEQUENCE /// ENTRY CDNT40 #type complete TITLE chlorophyll a/b-binding protein precursor (cab-40) - common tobacco ORGANISM #formal_name Nicotiana tabacum #common_name common tobacco DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 23-Mar-2001 ACCESSIONS S11722 REFERENCE S11719 !$#authors Jin, D.S.; Bogorad, L. !$#submission submitted to the EMBL Data Library, April 1990 !$#description Cab Genes from Nicotiana tabacum. !$#accession S11722 !'##molecule_type mRNA !'##residues 1-267 ##label EMB !'##cross-references EMBL:X52744; NID:g19828; PIDN:CAA36958.1; !1PID:g19829 GENETICS !$#gene Cab40 CLASSIFICATION #superfamily chlorophyll a/b-binding protein KEYWORDS chlorophyll; chloroplast; light-harvesting complex; !1thylakoid; transmembrane protein FEATURE !$1-34 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$35-267 #product chlorophyll a/b-binding protein #status !8predicted #label MAT\ !$101-120 #domain transmembrane #status predicted #label TM1\ !$153-173 #domain transmembrane #status predicted #label TM2\ !$221-237 #domain transmembrane #status predicted #label TM3 SUMMARY #length 267 #molecular-weight 28297 #checksum 9394 SEQUENCE /// ENTRY CDPJ2L #type complete TITLE chlorophyll a/b-binding protein 22L precursor - petunia ALTERNATE_NAMES light-harvesting complex Cab protein 22L ORGANISM #formal_name Petunia sp. #common_name petunia DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 25-Oct-1996 ACCESSIONS D22936 REFERENCE A93563 !$#authors Dunsmuir, P. !$#journal Nucleic Acids Res. (1985) 13:2503-2518 !$#title The petunia chlorophyll a/b binding protein genes: a !1comparison of Cab genes from different gene families. !$#cross-references MUID:85215630; PMID:2987856 !$#accession D22936 !'##molecule_type DNA !'##residues 1-267 ##label DUN COMMENT The light-harvesting complex (LHC) of the higher plant !1chloroplast is a thylakoid membrane-bound complex consisting !1of the chlorophylls (a and b) and chlorophyll a-b binding !1proteins. Functioning in photosynthesis as a light receptor, !1the LHC captures and delivers excitation energy to the !1photosystems with which it is closely associated. COMMENT The Cab proteins, encoded by nuclear genes whose expression !1is regulated by light, are synthesized as soluble precursors !1in the stroma. They are transported into the thylakoid !1membrane (an ATP-dependent process) where the mature !1polypeptides are assembled in the LHC. The transition from !1cytoplasmic precursor to LHC component is accompanied by !1loss of a "transit peptide" from the precursor. COMMENT The amino peptide of the mature protein extends into the !1stroma where it is involved with adhesion of granal !1membranes (granal stacking) and photoregulated reversible !1phosphorylation of its threonine residues. Both are believed !1to mediate the distribution of excitation energy between !1photosystems I and II. GENETICS !$#gene Cab-22L CLASSIFICATION #superfamily chlorophyll a/b-binding protein KEYWORDS chloroplast; grana; light-harvesting complex; membrane !1adhesion; membrane protein; phosphoprotein; photosynthesis; !1photosystem I; photosystem II; thylakoid FEATURE !$1-34 #domain (or 1-35) transit peptide (chloroplast) !8#status predicted #label TNP\ !$35-267 #product (or 36-267) chlorophyll a/b-binding protein !822L #status predicted #label MAT SUMMARY #length 267 #molecular-weight 28442 #checksum 232 SEQUENCE /// ENTRY CDTO1B #type complete TITLE chlorophyll a/b-binding protein 1B precursor - tomato ALTERNATE_NAMES light-harvesting complex Cab protein 1B ORGANISM #formal_name Lycopersicon esculentum #common_name tomato DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 28-May-1999 ACCESSIONS B24039 REFERENCE A24039 !$#authors Pichersky, E.; Bernatzky, R.; Tanksley, S.D.; Breidenbach, !1R.B.; Kausch, A.P.; Cashmore, A.R. !$#journal Gene (1985) 40:247-258 !$#title Molecular characterization and genetic mapping of two !1clusters of genes encoding chlorophyll a/b-binding proteins !1in Lycopersicon esculentum (tomato). !$#cross-references MUID:86165866; PMID:3007291 !$#accession B24039 !'##molecule_type DNA !'##residues 1-265 ##label PIC !'##cross-references GB:M14443; NID:g170401; PIDN:AAA34147.1; !1PID:g170402 !'##experimental_source cv. T6 COMMENT The light-harvesting complex (LHC) of the higher plant !1chloroplast is a thylakoid membrane-bound complex consisting !1of the chlorophylls (a and b) and chlorophyll a/b-binding !1proteins. Functioning in photosynthesis as a light receptor, !1the LHC captures and delivers excitation energy to the !1photosystems with which it is closely associated. COMMENT The amino peptide of the mature protein extends into the !1stroma where it is involved with adhesion of granal !1membranes (granal stacking). GENETICS !$#gene CAB-1B !$#map_position 2 CLASSIFICATION #superfamily chlorophyll a/b-binding protein KEYWORDS chloroplast; grana; light-harvesting complex; membrane !1adhesion; membrane protein; photosynthesis; photosystem I; !1photosystem II; thylakoid FEATURE !$1-34 #domain (or 1-35) transit peptide (chloroplast) !8#status predicted #label TNP\ !$35-265 #product (or 36-265) chlorophyll a/b-binding protein !81B #status predicted #label MAT SUMMARY #length 265 #molecular-weight 28072 #checksum 2017 SEQUENCE /// ENTRY CDNT21 #type complete TITLE chlorophyll a/b-binding protein precursor (cab-21) - common tobacco ORGANISM #formal_name Nicotiana tabacum #common_name common tobacco DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS S11719 REFERENCE S11719 !$#authors Jin, D.S.; Bogorad, L. !$#submission submitted to the EMBL Data Library, April 1990 !$#description Cab Genes from Nicotiana tabacum. !$#accession S11719 !'##molecule_type mRNA !'##residues 1-265 ##label EMB !'##cross-references EMBL:X52743; NID:g19822; PIDN:CAA36957.1; !1PID:g19823 GENETICS !$#gene Cab21 CLASSIFICATION #superfamily chlorophyll a/b-binding protein KEYWORDS chlorophyll; chloroplast; light-harvesting complex; !1thylakoid; transmembrane protein FEATURE !$1-33 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$34-265 #product chlorophyll a/b-binding protein #status !8predicted #label MAT\ !$99-118 #domain transmembrane #status predicted #label TM1\ !$151-171 #domain transmembrane #status predicted #label TM2\ !$219-235 #domain transmembrane #status predicted #label TM3 SUMMARY #length 265 #molecular-weight 28126 #checksum 3144 SEQUENCE /// ENTRY CDKV #type fragment TITLE chlorophyll a/b-binding protein precursor - cucumber (fragment) ALTERNATE_NAMES light-harvesting complex cab protein ORGANISM #formal_name Cucumis sativus #common_name cucumber DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS S07942 REFERENCE S07410 !$#authors Greenland, A.J.; Thomas, M.V.; Walden, R.M. !$#journal Planta (1987) 170:99-110 !$#title Expression of two nuclear genes encoding chloroplast !1proteins during early development of cucumber seedlings. !$#accession S07942 !'##molecule_type mRNA !'##residues 1-255 ##label GRE !'##cross-references EMBL:M16057; NID:g167522; PIDN:AAA33124.1; !1PID:g167523 CLASSIFICATION #superfamily chlorophyll a/b-binding protein KEYWORDS chlorophyll; chloroplast; light-harvesting complex; !1thylakoid; transmembrane protein FEATURE !$1-24 #domain transit peptide (chloroplast) (fragment) !8#status predicted #label TNP\ !$25-255 #product chlorophyll a/b-binding protein #status !8predicted #label MAT SUMMARY #length 255 #checksum 1057 SEQUENCE /// ENTRY CDPM96 #type fragment TITLE chlorophyll a/b-binding protein AB96 - garden pea (fragment) ALTERNATE_NAMES AB polypeptide; Cab protein 15; light-harvesting complex Cab protein; major Cab protein ORGANISM #formal_name Pisum sativum #common_name garden pea DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 16-Jul-1999 ACCESSIONS A26194; A05138 REFERENCE A92406 !$#authors Coruzzi, G.; Broglie, R.; Cashmore, A.; Chua, N.H. !$#journal J. Biol. Chem. (1983) 258:1399-1402 !$#title Nucleotide sequences of two pea cDNA clones encoding the !1small subunit of ribulose 1,5-bisphosphate carboxylase and !1the major chlorophyll a/b-binding thylakoid polypeptide. !$#cross-references MUID:83108917; PMID:6296093 !$#accession A26194 !'##molecule_type mRNA !'##residues 1-228 ##label COR !'##cross-references GB:J01253; NID:g169050; PIDN:AAA33650.1; !1PID:g169051 !'##experimental_source cv. Progress No. 9, clone pAB96 !'##note the authors translated the codon GGU for residue 17 as Arg, AAG !1for residue 56 as Tyr, AAA for residue 87 as Leu, AAG for !1residue 95 as Leu, and CCA for residue 193 as Gln COMMENT The light-harvesting complex (LHC) of the higher plant !1chloroplast is a thylakoid membrane-bound complex consisting !1of the chlorophylls (a and b) and chlorophyll a-b binding !1proteins. Functioning in photosynthesis as a light receptor, !1the LHC captures and delivers excitation energy to the !1photosystems with which it is closely associated. COMMENT The amino peptide of the mature protein extends into the !1stroma where it is involved with adhesion of granal !1membranes (granal stacking) and photoregulated reversible !1phosphorylation of its threonine residues. Both are believed !1to mediate the distribution of excitation energy between !1photosystems I and II. COMMENT This apoprotein binds at least three molecules of both !1chlorophylls a and b. GENETICS !$#gene AB96 CLASSIFICATION #superfamily chlorophyll a/b-binding protein KEYWORDS chloroplast; grana; light-harvesting complex; membrane !1adhesion; membrane protein; phosphoprotein; photosynthesis; !1photosystem I; photosystem II; thylakoid SUMMARY #length 228 #checksum 8356 SEQUENCE /// ENTRY CDPM80 #type complete TITLE chlorophyll a/b-binding protein AB80 precursor - garden pea ALTERNATE_NAMES AB polypeptide; Cab protein 15; grana-stacking polypeptide; light-harvesting complex Cab protein; major Cab protein ORGANISM #formal_name Pisum sativum #common_name garden pea DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 10-Oct-1997 ACCESSIONS A26780; A21004; S13976 REFERENCE A26780 !$#authors Cashmore, A.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:2960-2964 !$#title Structure and expression of a pea nuclear gene encoding a !1chlorophyll a/b-binding polypeptide. !$#accession A26780 !'##molecule_type DNA !'##residues 1-269 ##label CAS !'##experimental_source cv. Progress No. 9, clone AB80 REFERENCE A21004 !$#authors Mullet, J.E. !$#journal J. Biol. Chem. (1983) 258:9941-9948 !$#title The amino acid sequence of the polypeptide segment which !1regulates membrane adhesion (grana stacking) in !1chloroplasts. !$#cross-references MUID:83290920; PMID:6350285 !$#accession A21004 !'##molecule_type protein !'##residues 38-45 ##label MUL !'##note the order of the first two residues was not determined REFERENCE S13973 !$#authors Jahns, P.; Junge, W. !$#journal Eur. J. Biochem. (1990) 193:731-736 !$#title Dicyclohexylcarbodiimide-binding proteins related to the !1short circuit of the proton-pumping activity of photosystem !1II. Identified as light-harvesting chlorophyll-a/b-binding !1proteins. !$#cross-references MUID:91065379; PMID:2174365 !$#accession S13976 !'##status preliminary !'##molecule_type protein !'##residues 111-115,'XXX',119-122,'XX',125-126 ##label JAH COMMENT The light-harvesting complex (LHC) of the higher plant !1chloroplast is a thylakoid membrane-bound complex consisting !1of the chlorophylls (a and b) and chlorophyll a-b binding !1proteins. Functioning in photosynthesis as a light receptor, !1the LHC captures and delivers excitation energy to the !1photosystems with which it is closely associated. COMMENT The Cab proteins, encoded by nuclear genes whose expression !1is regulated by light, are synthesized as soluble precursors !1in the stroma. They are transported into the thylakoid !1membrane (an ATP-dependent process) where the mature !1polypeptides are assembled in the LHC. The transition from !1cytoplasmic precursor to LHC component is accompanied by !1loss of a "transit peptide" from the precursor. COMMENT The amino peptide of the mature protein extends into the !1stroma where it is involved with adhesion of granal !1membranes (granal stacking) and photoregulated reversible !1phosphorylation of its threonine residues. Both are believed !1to mediate the distribution of excitation energy between !1photosystems I and II. GENETICS !$#gene AB80 CLASSIFICATION #superfamily chlorophyll a/b-binding protein KEYWORDS chloroplast; grana; light-harvesting complex; membrane !1adhesion; membrane protein; phosphoprotein; photosynthesis; !1photosystem I; photosystem II; thylakoid FEATURE !$1-37 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$38-269 #product chlorophyll a/b-binding protein AB80 #status !8experimental #label MAT SUMMARY #length 269 #molecular-weight 28653 #checksum 7573 SEQUENCE /// ENTRY CDPMI8 #type complete TITLE chlorophyll a/b-binding protein type I precursor (cab-8) - garden pea ORGANISM #formal_name Pisum sativum #common_name garden pea DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS S17429 REFERENCE S17429 !$#authors Alexander, L.; Falconet, D.; Fristensky, B.W.; White, M.J.; !1Watson, J.C.; Roe, B.A.; Thompson, W.F. !$#journal Plant Mol. Biol. (1991) 17:523-526 !$#title Nucleotide sequence of Cab-8, a new type I gene encoding a !1chlorophyll a/b-binding protein of LHC II in Pisum. !$#cross-references MUID:91355946; PMID:1884005 !$#accession S17429 !'##molecule_type DNA !'##residues 1-268 ##label ALE !'##cross-references EMBL:X56538; NID:g20668; PIDN:CAA39883.1; !1PID:g20669 GENETICS !$#gene Cab-8 CLASSIFICATION #superfamily chlorophyll a/b-binding protein KEYWORDS chlorophyll; chloroplast; light-harvesting complex; !1thylakoid; transmembrane protein FEATURE !$1-35 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$36-268 #product chlorophyll a/b-binding protein #status !8predicted #label MAT\ !$102-121 #domain transmembrane #status predicted #label TM1\ !$154-174 #domain transmembrane #status predicted #label TM2\ !$222-238 #domain transmembrane #status predicted #label TM3 SUMMARY #length 268 #molecular-weight 28526 #checksum 5078 SEQUENCE /// ENTRY CDWT #type complete TITLE chlorophyll a/b-binding protein precursor - wheat ALTERNATE_NAMES light-harvesting complex Cab protein ORGANISM #formal_name Triticum aestivum #common_name common wheat DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 16-Jul-1999 ACCESSIONS A23755 REFERENCE A23755 !$#authors Lamppa, G.K.; Morelli, G.; Chua, N.H. !$#journal Mol. Cell. Biol. (1985) 5:1370-1378 !$#title Structure and developmental regulation of a wheat gene !1encoding the major chlorophyll a/b-binding polypeptide. !$#cross-references MUID:85295969; PMID:3897835 !$#accession A23755 !'##molecule_type DNA !'##residues 1-266 ##label LAM !'##cross-references GB:M10144; NID:g170673; PIDN:AAA34260.1; !1PID:g170674 COMMENT The light-harvesting complex (LHC) of the higher plant !1chloroplast is a thylakoid membrane-bound complex consisting !1of the chlorophylls (a and b) and chlorophyll a-b binding !1proteins. Functioning in photosynthesis as a light receptor, !1the LHC captures and delivers excitation energy to the !1photosystems with which it is closely associated. COMMENT The Cab proteins, encoded by nuclear genes whose expression !1is regulated by light, are synthesized as soluble precursors !1in the stroma. They are transported into the thylakoid !1membrane (an ATP-dependent process) where the mature !1polypeptides are assembled in the LHC. The transition from !1cytoplasmic precursor to LHC component is accompanied by !1loss of a "transit peptide" from the precursor. COMMENT The amino peptide of the mature protein extends into the !1stroma where it is involved with adhesion of granal !1membranes (granal stacking) and photoregulated reversible !1phosphorylation of its threonine residues. Both are believed !1to mediate the distribution of excitation energy between !1photosystems I and II. GENETICS !$#gene whAB1.6 CLASSIFICATION #superfamily chlorophyll a/b-binding protein KEYWORDS chloroplast; grana; light-harvesting complex; membrane !1adhesion; membrane protein; phosphoprotein; photosynthesis; !1photosystem I; photosystem II; thylakoid FEATURE !$1-33 #domain (or 1-34) transit peptide (chloroplast) !8#status predicted #label TNP\ !$34-266 #product (or 35-266) chlorophyll a/b-binding protein !8#status predicted #label MAT SUMMARY #length 266 #molecular-weight 28264 #checksum 5238 SEQUENCE /// ENTRY CDTO33 #type complete TITLE chlorophyll a/b-binding protein type III precursor (cab-13) - tomato ORGANISM #formal_name Lycopersicon esculentum #common_name tomato DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS S17737; S20210 REFERENCE S17737 !$#authors Schwartz, E.; Stasys, R.; Aebersold, R.; McGrath, J.M.; !1Green, B.R.; Pichersky, E. !$#journal Plant Mol. Biol. (1991) 17:923-925 !$#title Sequence of a tomato gene encoding a third type of LHCII !1chlorophyll a/b-binding polypeptide. !$#cross-references MUID:92003703; PMID:1912506 !$#accession S17737 !'##molecule_type DNA !'##residues 1-265 ##label SCH !'##cross-references EMBL:X60275; NID:g19276; PIDN:CAA42818.1; !1PID:g19277 !$#accession S20210 !'##molecule_type protein !'##residues 'X',44-51,'X',53,'X',55-56 ##label SC2 GENETICS !$#gene cab13; lhbC1 !$#map_position 12 !$#introns 42/3; 96/3 CLASSIFICATION #superfamily chlorophyll a/b-binding protein KEYWORDS chlorophyll; chloroplast; light-harvesting complex; !1thylakoid; transmembrane protein FEATURE !$1-42 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$43-265 #product chlorophyll a/b-binding protein #status !8predicted #label MAT\ !$97-116 #domain transmembrane #status predicted #label TM1\ !$150-170 #domain transmembrane #status predicted #label TM2\ !$219-235 #domain transmembrane #status predicted #label TM3 SUMMARY #length 265 #molecular-weight 28623 #checksum 2661 SEQUENCE /// ENTRY CDBH3 #type complete TITLE chlorophyll a/b-binding protein type III precursor - barley ORGANISM #formal_name Hordeum vulgare #common_name barley DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS S22482; S18861 REFERENCE S22482 !$#authors Brandt, J.; Nielsen, V.S.; Thordal-Christensen, H.; Simpson, !1D.J.; Okkels, J.S. !$#journal Plant Mol. Biol. (1992) 19:699-703 !$#title A barley cDNA clone encoding a Type III chlorophyll a/ !1b-binding polypeptide of the light-harvesting complex II. !$#cross-references MUID:92329730; PMID:1627782 !$#accession S22482 !'##molecule_type mRNA !'##residues 1-268 ##label BRA !'##cross-references EMBL:X63197; NID:g19022; PIDN:CAA44881.1; !1PID:g19023 GENETICS !$#gene cab CLASSIFICATION #superfamily chlorophyll a/b-binding protein KEYWORDS chlorophyll; chloroplast; light-harvesting complex; !1thylakoid; transmembrane protein FEATURE !$1-45 #domain transit peptide (chloroplast) #status !8predicted #label TNP\ !$46-268 #product chlorophyll a/b-binding protein type III !8#status predicted #label MAT\ !$100-119 #domain transmembrane #status predicted #label TM1\ !$153-173 #domain transmembrane #status predicted #label TM2\ !$222-238 #domain transmembrane #status predicted #label TM3 SUMMARY #length 268 #molecular-weight 28759 #checksum 9429 SEQUENCE /// ENTRY USBS1 #type complete TITLE small acid-soluble spore protein C - Bacillus subtilis phage SPBc2 ALTERNATE_NAMES SASP-1; SASP-C; small acid-soluble spore protein beta ORGANISM #formal_name Bacillus subtilis phage SPBc2 DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 16-Jun-2000 ACCESSIONS A03476; B24546; B60927; A69719; T12936 REFERENCE A03476 !$#authors Connors, M.J.; Setlow, P. !$#journal J. Bacteriol. (1985) 161:333-339 !$#title Cloning of a small, acid-soluble spore protein gene from !1Bacillus subtilis and determination of its complete !1nucleotide sequence. !$#cross-references MUID:85104728; PMID:2981806 !$#accession A03476 !'##molecule_type DNA !'##residues 1-72 ##label CON !'##cross-references GB:K02968; NID:g143509; PIDN:AAA22737.1; !1PID:g143510 REFERENCE A91816 !$#authors Connors, M.J.; Mason, J.M.; Setlow, P. !$#journal J. Bacteriol. (1986) 166:417-425 !$#title Cloning and nucleotide sequencing of genes for three small, !1acid-soluble proteins from Bacillus subtilis spores. !$#cross-references MUID:86195826; PMID:3009398 !$#accession B24546 !'##molecule_type DNA !'##residues 'MANQ',10,'SS',13-16,'V',18,'G',20-21,'Q',23-24,'D',26-37, !1'N',39-41,'D',43-60,'SF',63-65,'Q',67-69,'RVQ' ##label CO2 !'##cross-references GB:M12621; NID:g143707; PIDN:AAA22834.1; !1PID:g143708 REFERENCE A60927 !$#authors Blom, H.; Morse, R.; Mandelkorn, J.; Arnaud, M.; Warburg, !1R.; Tipper, D.J. !$#journal J. Gen. Microbiol. (1987) 133:2237-2246 !$#title The major acid-soluble proteins of Bacillus subtilis spores: !1partial amino acid sequence and forespore location of their !1mRNAs. !$#cross-references MUID:88171434; PMID:2450963 !$#accession B60927 !'##molecule_type protein !'##residues 'ANQ',10,'SS',13-16,'V',18,'G',20-21,'Q',23-24,'D',26-37, !1'N',39-41,'X',43-44 ##label BLO REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69719 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-72 ##label KUN !'##cross-references GB:Z99114; GB:AL009126; NID:g2634230; !1PIDN:CAB13886.1; PID:g2634387 !'##experimental_source strain 168 REFERENCE Z17583 !$#authors Lazarevic, V.; Duesterhoeft, A.; Soldo, B.; Hilbert, H.; !1Mauel, C.; Karamata, D. !$#submission submitted to the EMBL Data Library, August 1997 !$#description The complete nucleotide sequence of the Bacillus subtilis !1SPbetac2 prophage. !$#accession T12936 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-72 ##label LAZ !'##cross-references EMBL:AF020713; NID:g3025478; PID:g3025650; !1PIDN:AAC13145.1 COMMENT This protein belongs to a group of small, acid-soluble !1proteins of dormant bacterial spores. They are synthesized !1only during sporulation under transcriptional control and !1are degraded during early germination. COMMENT Saturation of DNA with this alpha/beta-type small !1acid-soluble spore protein (SASP) protects the DNA from !1damage by preventing the formation of thymine dimers. The !1protein is degraded rapidly during the first minutes of !1germination, after an initial cleavage by the spore protease !1GPR, to provide nutrients for protein synthesis. GENETICS LA !$#gene sspC GENETICS KU !$#gene SASP-1 CLASSIFICATION #superfamily alpha/beta-type small acid-soluble spore !1protein KEYWORDS DNA binding; germination; sporulation; storage protein FEATURE !$2-72 #product small acid-soluble spore protein C #status !8predicted #label MAT\ !$30-31 #cleavage_site Glu-Ile (spore-specific proteinase) !8#status predicted SUMMARY #length 72 #molecular-weight 7758 #checksum 3691 SEQUENCE /// ENTRY A24033 #type complete TITLE small acid-soluble spore protein C-1 - Bacillus megaterium ALTERNATE_NAMES SASP-C-1 ORGANISM #formal_name Bacillus megaterium DATE 23-Aug-1987 #sequence_revision 19-May-1994 #text_change 19-May-1994 ACCESSIONS A24033 REFERENCE A91523 !$#authors Fliss, E.R.; Setlow, P. !$#journal Gene (1985) 35:151-157 !$#title Genes for Bacillus megaterium small, acid-soluble spore !1proteins: nucleotide sequence of two genes and their !1expression during sporulation. !$#cross-references MUID:85286345; PMID:3928443 !$#accession A24033 !'##molecule_type DNA !'##residues 1-68 ##label FLI COMMENT Saturation of DNA with this alpha/beta-type small !1acid-soluble spore protein (SASP) protects the DNA from !1damage by preventing the formation of thymine dimers. The !1protein is degraded rapidly during the first minutes of !1germination, after an initial cleavage by the spore protease !1GPR, to provide nutrients for protein synthesis. CLASSIFICATION #superfamily alpha/beta-type small acid-soluble spore !1protein KEYWORDS DNA binding; germination; sporulation; storage protein FEATURE !$2-68 #product small acid-soluble spore protein C-1 #status !8predicted #label MAT\ !$27-28 #cleavage_site Glu-Ile (spore-specific proteinase) !8#status predicted SUMMARY #length 68 #molecular-weight 7205 #checksum 18 SEQUENCE /// ENTRY B24543 #type complete TITLE small acid-soluble spore protein C-4 - Bacillus megaterium ALTERNATE_NAMES SASP-C-4 ORGANISM #formal_name Bacillus megaterium DATE 20-Aug-1987 #sequence_revision 19-May-1994 #text_change 16-Jul-1999 ACCESSIONS B24543 REFERENCE A91813 !$#authors Fliss, E.R.; Loshon, C.A.; Setlow, P. !$#journal J. Bacteriol. (1986) 165:467-473 !$#title Genes for Bacillus megaterium small, acid-soluble spore !1proteins: cloning and nucleotide sequence of three !1additional genes from this multigene family. !$#cross-references MUID:86111611; PMID:3080406 !$#accession B24543 !'##molecule_type DNA !'##residues 1-69 ##label FLI !'##cross-references GB:M14110; NID:g142624; PIDN:AAA22283.1; !1PID:g142625 COMMENT Saturation of DNA with this alpha/beta-type small !1acid-soluble spore protein (SASP) protects the DNA from !1damage by preventing the formation of thymine dimers. The !1protein is degraded rapidly during the first minutes of !1germination, after an initial cleavage by the spore protease !1GPR, to provide nutrients for protein synthesis. CLASSIFICATION #superfamily alpha/beta-type small acid-soluble spore !1protein KEYWORDS DNA binding; germination; sporulation; storage protein FEATURE !$2-69 #product small acid-soluble spore protein C-4 #status !8predicted #label MAT\ !$27-28 #cleavage_site Glu-Ile (spore-specific proteinase) !8#status predicted SUMMARY #length 69 #molecular-weight 7347 #checksum 930 SEQUENCE /// ENTRY B24033 #type complete TITLE small acid-soluble spore protein C-2 - Bacillus megaterium ALTERNATE_NAMES SASP-C-2 ORGANISM #formal_name Bacillus megaterium DATE 23-Aug-1987 #sequence_revision 19-May-1994 #text_change 19-May-1994 ACCESSIONS B24033 REFERENCE A91523 !$#authors Fliss, E.R.; Setlow, P. !$#journal Gene (1985) 35:151-157 !$#title Genes for Bacillus megaterium small, acid-soluble spore !1proteins: nucleotide sequence of two genes and their !1expression during sporulation. !$#cross-references MUID:85286345; PMID:3928443 !$#accession B24033 !'##molecule_type DNA !'##residues 1-72 ##label FLI COMMENT Saturation of DNA with this alpha/beta-type small !1acid-soluble spore protein (SASP) protects the DNA from !1damage by preventing the formation of thymine dimers. The !1protein is degraded rapidly during the first minutes of !1germination, after an initial cleavage by the spore protease !1GPR, to provide nutrients for protein synthesis. CLASSIFICATION #superfamily alpha/beta-type small acid-soluble spore !1protein KEYWORDS DNA binding; germination; sporulation; storage protein FEATURE !$2-72 #product small acid-soluble spore protein C-2 #status !8predicted #label MAT\ !$27-28 #cleavage_site Glu-Ile (spore-specific proteinase) !8#status predicted SUMMARY #length 72 #molecular-weight 7602 #checksum 4454 SEQUENCE /// ENTRY C25234 #type complete TITLE small acid-soluble spore protein 1 - Bacillus stearothermophilus ORGANISM #formal_name Bacillus stearothermophilus DATE 16-Aug-1988 #sequence_revision 19-May-1994 #text_change 16-Jul-1999 ACCESSIONS C25234 REFERENCE A91820 !$#authors Loshon, C.A.; Fliss, E.R.; Setlow, B.; Foerster, H.F.; !1Setlow, P. !$#journal J. Bacteriol. (1986) 167:168-173 !$#title Cloning and nucleotide sequencing of genes for small, !1acid-soluble spore proteins of Bacillus cereus, Bacillus !1stearothermophilus, and "Thermoactinomyces thalpophilus". !$#cross-references MUID:86250587; PMID:3087949 !$#accession C25234 !'##molecule_type DNA !'##residues 1-70 ##label LOS !'##cross-references GB:M13061; NID:g143515; PIDN:AAA22740.1; !1PID:g143516 COMMENT Saturation of DNA with this alpha/beta-type small !1acid-soluble spore protein (SASP) protects the DNA from !1damage by preventing the formation of thymine dimers. The !1protein is degraded rapidly during the first minutes of !1germination, after an initial cleavage by the spore protease !1GPR, to provide nutrients for protein synthesis. CLASSIFICATION #superfamily alpha/beta-type small acid-soluble spore !1protein KEYWORDS DNA binding; germination; sporulation; storage protein FEATURE !$2-70 #product small acid-soluble spore protein 1 #status !8predicted #label MAT\ !$28-29 #cleavage_site Glu-Ile (spore-specific proteinase) !8#status predicted SUMMARY #length 70 #molecular-weight 7227 #checksum 2335 SEQUENCE /// ENTRY A24546 #type complete TITLE small acid-soluble spore protein (major alpha-type SASP) sspA - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 30-Jun-1988 #sequence_revision 19-May-1994 #text_change 16-Jun-2000 ACCESSIONS A24546; A60927; G69718 REFERENCE A91816 !$#authors Connors, M.J.; Mason, J.M.; Setlow, P. !$#journal J. Bacteriol. (1986) 166:417-425 !$#title Cloning and nucleotide sequencing of genes for three small, !1acid-soluble proteins from Bacillus subtilis spores. !$#cross-references MUID:86195826; PMID:3009398 !$#accession A24546 !'##molecule_type DNA !'##residues 1-69 ##label CON !'##cross-references GB:M12620; NID:g143703; PIDN:AAA22833.1; !1PID:g143704 REFERENCE A60927 !$#authors Blom, H.; Morse, R.; Mandelkorn, J.; Arnaud, M.; Warburg, !1R.; Tipper, D.J. !$#journal J. Gen. Microbiol. (1987) 133:2237-2246 !$#title The major acid-soluble proteins of Bacillus subtilis spores: !1partial amino acid sequence and forespore location of their !1mRNAs. !$#cross-references MUID:88171434; PMID:2450963 !$#accession A60927 !'##molecule_type protein !'##residues 2-37 ##label BLO REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69718 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-69 ##label KUN !'##cross-references GB:Z99119; GB:AL009126; NID:g2635411; !1PIDN:CAB14935.1; PID:g2635441 !'##experimental_source strain 168 COMMENT Saturation of DNA with this alpha/beta-type small !1acid-soluble spore protein (SASP) protects the DNA from !1damage by preventing the formation of thymine dimers. The !1protein is degraded rapidly during the first minutes of !1germination, after an initial cleavage by the spore protease !1GPR, to provide nutrients for protein synthesis. GENETICS !$#gene sspA CLASSIFICATION #superfamily alpha/beta-type small acid-soluble spore !1protein KEYWORDS DNA binding; germination; sporulation; storage protein FEATURE !$2-69 #product small acid-soluble spore protein alpha !8#status experimental #label MAT\ !$27-28 #cleavage_site Glu-Ile (spore-specific proteinase) !8#status predicted SUMMARY #length 69 #molecular-weight 7071 #checksum 1232 SEQUENCE /// ENTRY B25234 #type complete TITLE small acid-soluble spore protein A - Bacillus cereus ALTERNATE_NAMES SASP-2; SASP-A ORGANISM #formal_name Bacillus cereus DATE 16-Aug-1988 #sequence_revision 19-May-1994 #text_change 16-Jul-1999 ACCESSIONS B25234; A61111 REFERENCE A91820 !$#authors Loshon, C.A.; Fliss, E.R.; Setlow, B.; Foerster, H.F.; !1Setlow, P. !$#journal J. Bacteriol. (1986) 167:168-173 !$#title Cloning and nucleotide sequencing of genes for small, !1acid-soluble spore proteins of Bacillus cereus, Bacillus !1stearothermophilus, and "Thermoactinomyces thalpophilus". !$#cross-references MUID:86250587; PMID:3087949 !$#accession B25234 !'##molecule_type DNA !'##residues 1-65 ##label LOS !'##cross-references GB:M13060; NID:g143513; PIDN:AAA22739.1; !1PID:g143514 REFERENCE A61111 !$#authors Yuan, K.; Johnson, W.C.; Tipper, D.J.; Setlow, P. !$#journal J. Bacteriol. (1981) 146:965-971 !$#title Comparison of various properties of low-molecular-weight !1proteins from dormant spores of several Bacillus species. !$#cross-references MUID:81215316; PMID:6787019 !$#accession A61111 !'##molecule_type protein !'##residues 2-16;24-29 ##label YUA COMMENT Saturation of DNA with this alpha/beta-type small !1acid-soluble spore protein (SASP) protects the DNA from !1damage by preventing the formation of thymine dimers. The !1protein is degraded rapidly during the first minutes of !1germination, after an initial cleavage by the spore protease !1GPR, to provide nutrients for protein synthesis. CLASSIFICATION #superfamily alpha/beta-type small acid-soluble spore !1protein KEYWORDS DNA binding; germination; sporulation; storage protein FEATURE !$2-65 #product small acid-soluble spore protein A #status !8experimental #label MAT\ !$23-24 #cleavage_site Glu-Ile (spore-specific proteinase) !8#status experimental SUMMARY #length 65 #molecular-weight 6842 #checksum 6712 SEQUENCE /// ENTRY A25234 #type complete TITLE small acid-soluble spore protein 1 - Bacillus cereus ORGANISM #formal_name Bacillus cereus DATE 16-Aug-1988 #sequence_revision 19-May-1994 #text_change 16-Jul-1999 ACCESSIONS A25234 REFERENCE A91820 !$#authors Loshon, C.A.; Fliss, E.R.; Setlow, B.; Foerster, H.F.; !1Setlow, P. !$#journal J. Bacteriol. (1986) 167:168-173 !$#title Cloning and nucleotide sequencing of genes for small, !1acid-soluble spore proteins of Bacillus cereus, Bacillus !1stearothermophilus, and "Thermoactinomyces thalpophilus". !$#cross-references MUID:86250587; PMID:3087949 !$#accession A25234 !'##molecule_type DNA !'##residues 1-70 ##label LOS !'##cross-references GB:M13059; NID:g143511; PIDN:AAA22738.1; !1PID:g143512 COMMENT Saturation of DNA with this alpha/beta-type small !1acid-soluble spore protein (SASP) protects the DNA from !1damage by preventing the formation of thymine dimers. The !1protein is degraded rapidly during the first minutes of !1germination, after an initial cleavage by the spore protease !1GPR, to provide nutrients for protein synthesis. CLASSIFICATION #superfamily alpha/beta-type small acid-soluble spore !1protein KEYWORDS DNA binding; germination; sporulation; storage protein FEATURE !$2-70 #product small acid-soluble spore protein 1 #status !8predicted #label MAT\ !$27-28 #cleavage_site Glu-Ile (spore-specific proteinase) !8#status predicted SUMMARY #length 70 #molecular-weight 7466 #checksum 2926 SEQUENCE /// ENTRY D25234 #type complete TITLE small acid-soluble spore protein 1 - Thermoactinomyces sp. ORGANISM #formal_name Thermoactinomyces sp. DATE 16-Aug-1988 #sequence_revision 19-May-1994 #text_change 28-May-1999 ACCESSIONS D25234 REFERENCE A91820 !$#authors Loshon, C.A.; Fliss, E.R.; Setlow, B.; Foerster, H.F.; !1Setlow, P. !$#journal J. Bacteriol. (1986) 167:168-173 !$#title Cloning and nucleotide sequencing of genes for small, !1acid-soluble spore proteins of Bacillus cereus, Bacillus !1stearothermophilus, and "Thermoactinomyces thalpophilus". !$#cross-references MUID:86250587; PMID:3087949 !$#accession D25234 !'##molecule_type DNA !'##residues 1-71 ##label LOS !'##cross-references GB:M13062; NID:g144131; PIDN:AAA23003.1; !1PID:g144132 !'##note source was designated as "T. thalpophilus," strain HA-01 COMMENT Saturation of DNA with this alpha/beta-type small !1acid-soluble spore protein (SASP) protects the DNA from !1damage by preventing the formation of thymine dimers. The !1protein is degraded rapidly during the first minutes of !1germination, after an initial cleavage by the spore protease !1GPR, to provide nutrients for protein synthesis. CLASSIFICATION #superfamily alpha/beta-type small acid-soluble spore !1protein KEYWORDS DNA binding; germination; sporulation; storage protein FEATURE !$2-71 #product small acid-soluble spore protein 1 #status !8predicted #label MAT\ !$28-29 #cleavage_site Glu-Ile (spore-specific proteinase) !8#status predicted SUMMARY #length 71 #molecular-weight 7369 #checksum 2742 SEQUENCE /// ENTRY C24543 #type complete TITLE small acid-soluble spore protein C-5 - Bacillus megaterium ALTERNATE_NAMES SASP-C-5 ORGANISM #formal_name Bacillus megaterium DATE 20-Aug-1987 #sequence_revision 19-May-1994 #text_change 16-Jul-1999 ACCESSIONS C24543 REFERENCE A91813 !$#authors Fliss, E.R.; Loshon, C.A.; Setlow, P. !$#journal J. Bacteriol. (1986) 165:467-473 !$#title Genes for Bacillus megaterium small, acid-soluble spore !1proteins: cloning and nucleotide sequence of three !1additional genes from this multigene family. !$#cross-references MUID:86111611; PMID:3080406 !$#accession C24543 !'##molecule_type DNA !'##residues 1-73 ##label FLI !'##cross-references GB:M14111; NID:g142626; PIDN:AAA22284.1; !1PID:g142627 COMMENT Saturation of DNA with this alpha/beta-type small !1acid-soluble spore protein (SASP) protects the DNA from !1damage by preventing the formation of thymine dimers. The !1protein is degraded rapidly during the first minutes of !1germination, after an initial cleavage by the spore protease !1GPR, to provide nutrients for protein synthesis. CLASSIFICATION #superfamily alpha/beta-type small acid-soluble spore !1protein KEYWORDS DNA binding; germination; sporulation; storage protein FEATURE !$2-73 #product small acid-soluble spore protein C-5 #status !8predicted #label MAT\ !$27-28 #cleavage_site Glu-Ile (spore-specific proteinase) !8#status predicted SUMMARY #length 73 #molecular-weight 7680 #checksum 6345 SEQUENCE /// ENTRY D24546 #type complete TITLE small acid-soluble spore protein (minor alpha/beta-type SASP) sspD - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 30-Jun-1988 #sequence_revision 19-May-1994 #text_change 16-Jun-2000 ACCESSIONS D24546; B69719 REFERENCE A91816 !$#authors Connors, M.J.; Mason, J.M.; Setlow, P. !$#journal J. Bacteriol. (1986) 166:417-425 !$#title Cloning and nucleotide sequencing of genes for three small, !1acid-soluble proteins from Bacillus subtilis spores. !$#cross-references MUID:86195826; PMID:3009398 !$#accession D24546 !'##molecule_type DNA !'##residues 1-64 ##label CON !'##cross-references GB:M12622; NID:g143709; PIDN:AAA22835.1; !1PID:g143710 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69719 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-64 ##label KUN !'##cross-references GB:Z99111; GB:AL009126; NID:g2633699; !1PIDN:CAB13220.1; PID:g2633718 !'##experimental_source strain 168 COMMENT Saturation of DNA with this alpha/beta-type small !1acid-soluble spore protein (SASP) protects the DNA from !1damage by preventing the formation of thymine dimers. The !1protein is degraded rapidly during the first minutes of !1germination, after an initial cleavage by the spore protease !1GPR, to provide nutrients for protein synthesis. GENETICS !$#gene sspD CLASSIFICATION #superfamily alpha/beta-type small acid-soluble spore !1protein KEYWORDS DNA binding; germination; sporulation; storage protein FEATURE !$2-64 #product small acid-soluble spore protein D #status !8predicted #label MAT\ !$22-23 #cleavage_site Glu-Val (spore-specific proteinase) !8#status predicted SUMMARY #length 64 #molecular-weight 6804 #checksum 9042 SEQUENCE /// ENTRY A22810 #type complete TITLE small acid-soluble spore protein C-3 - Bacillus megaterium ALTERNATE_NAMES SASP C-3 ORGANISM #formal_name Bacillus megaterium DATE 23-Aug-1987 #sequence_revision 19-May-1994 #text_change 16-Jul-1999 ACCESSIONS A22810 REFERENCE A22810 !$#authors Fliss, E.R.; Setlow, P. !$#journal Gene (1984) 30:167-172 !$#title Bacillus megaterium spore protein C-3: nucleotide sequence !1of its gene and the amino acid sequence at its spore !1protease cleavage site. !$#cross-references MUID:85077608; PMID:6439604 !$#accession A22810 !'##molecule_type DNA !'##residues 1-65 ##label FLI !'##cross-references GB:M12336; NID:g143572; PIDN:AAA22782.1; !1PID:g143573 COMMENT Saturation of DNA with this alpha/beta-type small !1acid-soluble spore protein (SASP) protects the DNA from !1damage by preventing the formation of thymine dimers. The !1protein is degraded rapidly during the first minutes of !1germination, after an initial cleavage by the spore protease !1GPR, to provide nutrients for protein synthesis. CLASSIFICATION #superfamily alpha/beta-type small acid-soluble spore !1protein KEYWORDS DNA binding; germination; sporulation; storage protein FEATURE !$2-65 #product small acid-soluble spore protein C-3 #status !8experimental #label MAT\ !$22-23 #cleavage_site Glu-Ile (spore-specific proteinase) !8#status experimental SUMMARY #length 65 #molecular-weight 7027 #checksum 8914 SEQUENCE /// ENTRY USBSAM #type complete TITLE small acid-soluble spore protein A - Bacillus megaterium ALTERNATE_NAMES SASP-A ORGANISM #formal_name Bacillus megaterium DATE 28-Feb-1980 #sequence_revision 19-May-1994 #text_change 16-Jul-1999 ACCESSIONS A24543; A03477 REFERENCE A91813 !$#authors Fliss, E.R.; Loshon, C.A.; Setlow, P. !$#journal J. Bacteriol. (1986) 165:467-473 !$#title Genes for Bacillus megaterium small, acid-soluble spore !1proteins: cloning and nucleotide sequence of three !1additional genes from this multigene family. !$#cross-references MUID:86111611; PMID:3080406 !$#accession A24543 !'##molecule_type DNA !'##residues 1-62 ##label FLI !'##cross-references GB:M14109; NID:g142628; PIDN:AAA22285.1; !1PID:g142629 REFERENCE A03477 !$#authors Setlow, P.; Ozols, J. !$#journal J. Biol. Chem. (1979) 254:11938-11942 !$#title Covalent structure of protein A. A low molecular weight !1protein degraded during germination of Bacillus megaterium !1spores. !$#cross-references MUID:80049843; PMID:115874 !$#accession A03477 !'##molecule_type protein !'##residues 2-62 ##label SET COMMENT Saturation of DNA with this alpha/beta-type small !1acid-soluble spore protein (SASP) protects the DNA from !1damage by preventing the formation of thymine dimers. The !1protein is degraded rapidly during the first minutes of !1germination, after an initial cleavage by the spore protease !1GPR, to provide nutrients for protein synthesis. CLASSIFICATION #superfamily alpha/beta-type small acid-soluble spore !1protein KEYWORDS DNA binding; germination; sporulation; storage protein FEATURE !$2-62 #product small acid-soluble spore protein A #status !8experimental #label MAT\ !$22-23 #cleavage_site Glu-Ile (spore-specific proteinase) !8#status experimental SUMMARY #length 62 #molecular-weight 6391 #checksum 5556 SEQUENCE /// ENTRY USBSCM #type complete TITLE small acid-soluble spore protein C - Bacillus megaterium ORGANISM #formal_name Bacillus megaterium DATE 31-Dec-1980 #sequence_revision 01-Nov-1996 #text_change 16-Jul-1999 ACCESSIONS I39794; B92274; A92287; A03478 REFERENCE I39794 !$#authors Fliss, E.R.; Setlow, P.L. !$#journal J. Bacteriol. (1984) 158:809-813 !$#title Complete nucleotide sequence and start sites for !1transcription and translation of the Bacillus megaterium !1protein C gene. !$#cross-references MUID:84212301; PMID:6327639 !$#accession I39794 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-72 ##label RES !'##cross-references GB:K01833; NID:g142620; PIDN:AAA22282.1; !1PID:g142621 REFERENCE A92274 !$#authors Setlow, P.; Gerard, C.; Ozols, J. !$#journal J. Biol. Chem. (1980) 255:3624-3628 !$#title The amino acid sequence specificity of a protease from !1spores of Bacillus megaterium. !$#cross-references MUID:80159989; PMID:6767722 !$#accession B92274 !'##molecule_type protein !'##residues 2-39 ##label SE1 REFERENCE A92287 !$#authors Setlow, P.; Ozols, J. !$#journal J. Biol. Chem. (1980) 255:8413-8416 !$#title Covalent structure of protein C. A second major low !1molecular weight protein degraded during germination of !1Bacillus megaterium spores. !$#cross-references MUID:81006871; PMID:6773941 !$#accession A92287 !'##molecule_type protein !'##residues 2-15;32-72 ##label SE2 COMMENT Saturation of DNA with this alpha/beta-type small !1acid-soluble spore protein (SASP) protects the DNA from !1damage by preventing the formation of thymine dimers. The !1protein is degraded rapidly during the first minutes of !1germination, after an initial cleavage by the spore protease !1GPR, to provide nutrients for protein synthesis. CLASSIFICATION #superfamily alpha/beta-type small acid-soluble spore !1protein KEYWORDS DNA binding; germination; sporulation; storage protein FEATURE !$31-32 #cleavage_site Glu-Ile (spore-specific proteinase) !8#status experimental SUMMARY #length 72 #molecular-weight 7554 #checksum 2344 SEQUENCE /// ENTRY A39059 #type fragment TITLE small acid-soluble spore protein C homolog - Mycobacterium phlei (fragment) ALTERNATE_NAMES SASP-C homolog ORGANISM #formal_name Mycobacterium phlei DATE 28-Feb-1992 #sequence_revision 19-May-1994 #text_change 19-May-1994 ACCESSIONS A39059 REFERENCE A39059 !$#authors Vocero-Villeta, A.M.; Schilling, D.M.; Fliss, E.R. !$#journal Genomics (1991) 9:290-297 !$#title Nonsporulating bacterial species contain DNA sequences !1homologous to the Bacillus spore-specific C-protein gene. !$#cross-references MUID:91169532; PMID:1848527 !$#accession A39059 !'##molecule_type DNA !'##residues 1-51 ##label VOC !'##cross-references GB:M57779 COMMENT The function of this protein is unknown. Homologous proteins !1in spore-forming species protect spore DNA and store amino !1acids for germination. CLASSIFICATION #superfamily alpha/beta-type small acid-soluble spore !1protein KEYWORDS DNA binding; germination; sporulation; storage protein FEATURE !$2-51 #product small acid-soluble spore protein C homolog !8#status predicted #label MAT SUMMARY #length 51 #checksum 472 SEQUENCE /// ENTRY B39059 #type fragment TITLE small acid-soluble spore protein C homolog - Streptococcus pyogenes (fragment) ALTERNATE_NAMES SASP-C homolog ORGANISM #formal_name Streptococcus pyogenes DATE 28-Feb-1992 #sequence_revision 19-May-1994 #text_change 19-May-1994 ACCESSIONS B39059 REFERENCE A39059 !$#authors Vocero-Villeta, A.M.; Schilling, D.M.; Fliss, E.R. !$#journal Genomics (1991) 9:290-297 !$#title Nonsporulating bacterial species contain DNA sequences !1homologous to the Bacillus spore-specific C-protein gene. !$#cross-references MUID:91169532; PMID:1848527 !$#accession B39059 !'##molecule_type DNA !'##residues 1-51 ##label VOC !'##cross-references GB:M57780 COMMENT The function of this protein is unknown. Homologous proteins !1in spore-forming species protect spore DNA and store amino !1acids for germination. CLASSIFICATION #superfamily alpha/beta-type small acid-soluble spore !1protein KEYWORDS DNA binding; germination; sporulation; storage protein FEATURE !$2-51 #product small acid-soluble spore protein C homolog !8#status predicted #label MAT SUMMARY #length 51 #checksum 678 SEQUENCE /// ENTRY A48180 #type complete TITLE small acid-soluble spore protein 1 - Sporosarcina ureae ORGANISM #formal_name Sporosarcina ureae DATE 10-Mar-1994 #sequence_revision 19-May-1994 #text_change 16-Jul-1999 ACCESSIONS A48180 REFERENCE A48180 !$#authors Magill, N.G.; Loshon, C.A.; Setlow, P. !$#journal FEMS Microbiol. Lett. (1990) 72:293-298 !$#title Small, acid-soluble, spore proteins and their genes from two !1species of Sporosarcina. !$#accession A48180 !'##molecule_type DNA !'##residues 1-69 ##label MAG !'##cross-references GB:X55158; NID:g47971; PIDN:CAA38957.1; PID:g47972 COMMENT Saturation of DNA with this alpha/beta-type small !1acid-soluble spore protein (SASP) protects the DNA from !1damage by preventing the formation of thymine dimers. The !1protein is degraded rapidly during the first minutes of !1germination, after an initial cleavage by the spore protease !1GPR, to provide nutrients for protein synthesis. CLASSIFICATION #superfamily alpha/beta-type small acid-soluble spore !1protein KEYWORDS DNA binding; germination; sporulation; storage protein FEATURE !$2-69 #product small acid-soluble spore protein 1 #status !8predicted #label MAT\ !$27-28 #cleavage_site Glu-Ile (spore-specific proteinase) !8#status predicted SUMMARY #length 69 #molecular-weight 7451 #checksum 2798 SEQUENCE /// ENTRY B48180 #type complete TITLE small acid-soluble spore protein 2 - Sporosarcina ureae ORGANISM #formal_name Sporosarcina ureae DATE 10-Mar-1994 #sequence_revision 19-May-1994 #text_change 16-Jul-1999 ACCESSIONS B48180 REFERENCE A48180 !$#authors Magill, N.G.; Loshon, C.A.; Setlow, P. !$#journal FEMS Microbiol. Lett. (1990) 72:293-298 !$#title Small, acid-soluble, spore proteins and their genes from two !1species of Sporosarcina. !$#accession B48180 !'##molecule_type DNA !'##residues 1-67 ##label MAG !'##cross-references GB:X55159; NID:g47973; PIDN:CAA38958.1; PID:g47974 COMMENT Saturation of DNA with this alpha/beta-type small !1acid-soluble spore protein (SASP) protects the DNA from !1damage by preventing the formation of thymine dimers. The !1protein is degraded rapidly during the first minutes of !1germination, after an initial cleavage by the spore protease !1GPR, to provide nutrients for protein synthesis. CLASSIFICATION #superfamily alpha/beta-type small acid-soluble spore !1protein KEYWORDS DNA binding; germination; sporulation; storage protein FEATURE !$2-67 #product small acid-soluble spore protein 2 #status !8predicted #label MAT\ !$25-26 #cleavage_site Glu-Ile (spore-specific proteinase) !8#status predicted SUMMARY #length 67 #molecular-weight 7176 #checksum 1079 SEQUENCE /// ENTRY C48180 #type complete TITLE small acid-soluble spore protein 1 - Sporosarcina halophila ORGANISM #formal_name Sporosarcina halophila DATE 10-Mar-1994 #sequence_revision 19-May-1994 #text_change 16-Jul-1999 ACCESSIONS C48180 REFERENCE A48180 !$#authors Magill, N.G.; Loshon, C.A.; Setlow, P. !$#journal FEMS Microbiol. Lett. (1990) 72:293-298 !$#title Small, acid-soluble, spore proteins and their genes from two !1species of Sporosarcina. !$#accession C48180 !'##molecule_type DNA !'##residues 1-72 ##label MAG !'##cross-references GB:X55160; NID:g47141; PIDN:CAA38959.1; PID:g47142 COMMENT Saturation of DNA with this alpha/beta-type small !1acid-soluble spore protein (SASP) protects the DNA from !1damage by preventing the formation of thymine dimers. The !1protein is degraded rapidly during the first minutes of !1germination, after an initial cleavage by the spore protease !1GPR, to provide nutrients for protein synthesis. CLASSIFICATION #superfamily alpha/beta-type small acid-soluble spore !1protein KEYWORDS DNA binding; germination; sporulation; storage protein FEATURE !$2-72 #product small acid-soluble spore protein 1 #status !8predicted #label MAT\ !$25-26 #cleavage_site Glu-Ile (spore-specific proteinase) !8#status predicted SUMMARY #length 72 #molecular-weight 7790 #checksum 6181 SEQUENCE /// ENTRY A61028 #type complete TITLE small acid-soluble spore protein alpha - Clostridium bifermentans ALTERNATE_NAMES SASP-alpha ORGANISM #formal_name Clostridium bifermentans DATE 31-Dec-1993 #sequence_revision 19-May-1994 #text_change 16-Feb-1997 ACCESSIONS A61028 REFERENCE A61028 !$#authors Cabrera-Martinez, R.M.; Mason, J.M.; Setlow, B.; Waites, !1W.M.; Setlow, P. !$#journal FEMS Microbiol. Lett. (1989) 61:139-144 !$#title Purification and amino acid sequence of two small, !1acid-soluble proteins from Clostridium bifermentans spores. !$#accession A61028 !'##molecule_type protein !'##residues 1-70 ##label CAB COMMENT Saturation of DNA with this alpha/beta-type small !1acid-soluble spore protein (SASP) protects the DNA from !1damage by preventing the formation of thymine dimers. The !1protein is degraded rapidly during the first minutes of !1germination, after an initial cleavage by the spore protease !1GPR, to provide nutrients for protein synthesis. COMMENT This species seems to lack any gamma-type SASP. CLASSIFICATION #superfamily alpha/beta-type small acid-soluble spore !1protein KEYWORDS DNA binding; sporulation; storage protein FEATURE !$23-24 #cleavage_site Glu-Ile (spore-specific proteinase) !8#status predicted SUMMARY #length 70 #molecular-weight 7696 #checksum 3292 SEQUENCE /// ENTRY B61028 #type complete TITLE small acid-soluble spore protein beta - Clostridium bifermentans ALTERNATE_NAMES SASP-beta ORGANISM #formal_name Clostridium bifermentans DATE 31-Dec-1993 #sequence_revision 19-May-1994 #text_change 16-Feb-1997 ACCESSIONS B61028 REFERENCE A61028 !$#authors Cabrera-Martinez, R.M.; Mason, J.M.; Setlow, B.; Waites, !1W.M.; Setlow, P. !$#journal FEMS Microbiol. Lett. (1989) 61:139-144 !$#title Purification and amino acid sequence of two small, !1acid-soluble proteins from Clostridium bifermentans spores. !$#accession B61028 !'##molecule_type protein !'##residues 1-64 ##label CAB COMMENT Saturation of DNA with this alpha/beta-type small !1acid-soluble spore protein (SASP) protects the DNA from !1damage by preventing the formation of thymine dimers. The !1protein is degraded rapidly during the first minutes of !1germination, after an initial cleavage by the spore protease !1GPR, to provide nutrients for protein synthesis. COMMENT This species seems to lack any gamma-type SASP. CLASSIFICATION #superfamily alpha/beta-type small acid-soluble spore !1protein KEYWORDS DNA binding; sporulation; storage protein FEATURE !$19-20 #cleavage_site Glu-Ile (spore-specific proteinase) !8#status predicted SUMMARY #length 64 #molecular-weight 6992 #checksum 8693 SEQUENCE /// ENTRY JN0082 #type complete TITLE small acid-soluble spore protein C1 - Clostridium perfringens ALTERNATE_NAMES ASSP C1; SASP 2; SASP C1; ssp2 ORGANISM #formal_name Clostridium perfringens DATE 31-Dec-1991 #sequence_revision 19-May-1994 #text_change 16-Jul-1999 ACCESSIONS JN0082; B54537 REFERENCE JN0082 !$#authors Holck, A.; Blom, H.; Granum, P.E. !$#journal Gene (1990) 91:107-111 !$#title Cloning and sequencing of the genes encoding acid-soluble !1spore proteins from Clostridium perfringens. !$#cross-references MUID:90382684; PMID:2401406 !$#accession JN0082 !'##molecule_type DNA !'##residues 1-59 ##label HOL !'##cross-references GB:M57433; GB:M31618; NID:g144916; PIDN:AAA62757.1; !1PID:g144917 REFERENCE A54537 !$#authors Cabrera-Martinez, R.; Setlow, P. !$#journal FEMS Microbiol. Lett. (1991) 77:127-132 !$#title Cloning and nucleotide sequence of three genes coding for !1small, acid-soluble proteins of Clostridium perfringens !1spores. !$#accession B54537 !'##molecule_type DNA !'##residues 1-59 ##label CAB !'##cross-references GB:X59481; NID:g40630; PIDN:CAA42082.1; PID:g40631 REFERENCE S06260 !$#authors Granum, P.E.; Richardson, M.; Blom, H. !$#journal FEMS Microbiol. Lett. (1987) 42:225-230 !$#title Isolation and amino acid sequence of an acid soluble protein !1from Clostridium perfringens spores. !$#contents annotation COMMENT Saturation of DNA with this alpha/beta-type small !1acid-soluble spore protein (SASP) protects the DNA from !1damage by preventing the formation of thymine dimers. GENETICS !$#gene sspC1; ssp2 CLASSIFICATION #superfamily alpha/beta-type small acid-soluble spore !1protein KEYWORDS DNA binding; germination; sporulation; storage protein FEATURE !$2-59 #product small acid-soluble spore protein C1 #status !8experimental #label MAT\ !$19-20 #cleavage_site Glu-Val (spore-specific proteinase) !8#status predicted SUMMARY #length 59 #molecular-weight 6437 #checksum 6849 SEQUENCE /// ENTRY JN0083 #type complete TITLE small acid-soluble spore protein C2 - Clostridium perfringens ALTERNATE_NAMES ASSP C2; SASP 3; SASP C2; small acid-soluble spore protein ssp3 ORGANISM #formal_name Clostridium perfringens DATE 31-Dec-1991 #sequence_revision 19-May-1994 #text_change 16-Jul-1999 ACCESSIONS C54537; JN0083; S06260 REFERENCE A54537 !$#authors Cabrera-Martinez, R.; Setlow, P. !$#journal FEMS Microbiol. Lett. (1991) 77:127-132 !$#title Cloning and nucleotide sequence of three genes coding for !1small, acid-soluble proteins of Clostridium perfringens !1spores. !$#accession C54537 !'##molecule_type DNA !'##residues 1-60 ##label CAB !'##cross-references GB:X59482; NID:g40632; PIDN:CAA42083.1; PID:g40633 REFERENCE JN0082 !$#authors Holck, A.; Blom, H.; Granum, P.E. !$#journal Gene (1990) 91:107-111 !$#title Cloning and sequencing of the genes encoding acid-soluble !1spore proteins from Clostridium perfringens. !$#cross-references MUID:90382684; PMID:2401406 !$#accession JN0083 !'##molecule_type DNA !'##residues 1-60 ##label HOL !'##cross-references GB:M57434; GB:M31619; NID:g144918; PIDN:AAA62758.1; !1PID:g144919 REFERENCE S06260 !$#authors Granum, P.E.; Richardson, M.; Blom, H. !$#journal FEMS Microbiol. Lett. (1987) 42:225-230 !$#title Isolation and amino acid sequence of an acid soluble protein !1from Clostridium perfringens spores. !$#accession S06260 !'##molecule_type protein !'##residues 2-21,'A',23,'L',25-35,'QSS',42-50,'I',52-53,'Q',55-60 !1##label GRA !'##note 22-Arg, 22-Asn, 24-Met, 35-Arg, 51-Met, and 54-Lys were also !1found !'##note this sequence appears to represent a mixture of several alpha/ !1beta-type small acid-soluble spore proteins; the results !1agree best with this protein of the three described in !1reference A54537 COMMENT Saturation of DNA with this alpha/beta-type small !1acid-soluble spore protein (SASP) protects the DNA from !1damage by preventing the formation of thymine dimers. The !1protein is degraded rapidly during the first minutes of !1germination, after an initial cleavage by the spore protease !1GPR, to provide nutrients for protein synthesis. GENETICS !$#gene sspC2; ssp3 CLASSIFICATION #superfamily alpha/beta-type small acid-soluble spore !1protein KEYWORDS DNA binding; germination; sporulation; storage protein FEATURE !$2-60 #product small acid-soluble spore protein C2 #status !8predicted #label MAT\ !$19-20 #cleavage_site Glu-Val (spore-specific proteinase) !8#status predicted SUMMARY #length 60 #molecular-weight 6685 #checksum 7664 SEQUENCE /// ENTRY A54537 #type complete TITLE small acid-soluble spore ssp1 - Clostridium perfringens ALTERNATE_NAMES SASP 1 ORGANISM #formal_name Clostridium perfringens DATE 28-Oct-1994 #sequence_revision 02-Dec-1994 #text_change 16-Jul-1999 ACCESSIONS A54537 REFERENCE A54537 !$#authors Cabrera-Martinez, R.; Setlow, P. !$#journal FEMS Microbiol. Lett. (1991) 77:127-132 !$#title Cloning and nucleotide sequence of three genes coding for !1small, acid-soluble proteins of Clostridium perfringens !1spores. !$#accession A54537 !'##molecule_type DNA !'##residues 1-60 ##label CAB !'##cross-references GB:X59480; NID:g40628; PIDN:CAA42081.1; PID:g40629 REFERENCE S06260 !$#authors Granum, P.E.; Richardson, M.; Blom, H. !$#journal FEMS Microbiol. Lett. (1987) 42:225-230 !$#title Isolation and amino acid sequence of an acid soluble protein !1from Clostridium perfringens spores. !$#contents annotation COMMENT Saturation of DNA with this alpha/beta-type small !1acid-soluble spore protein (SASP) protects the DNA from !1damage by preventing the formation of thymine dimers. GENETICS !$#gene ssp1 CLASSIFICATION #superfamily alpha/beta-type small acid-soluble spore !1protein KEYWORDS DNA binding; germination; sporulation; storage protein FEATURE !$2-60 #product small acid-soluble spore ssp1 #status !8experimental #label MAT SUMMARY #length 60 #molecular-weight 6583 #checksum 7318 SEQUENCE /// ENTRY USBSBM #type complete TITLE small acid-soluble spore protein B - Bacillus megaterium ALTERNATE_NAMES SASP-B ORGANISM #formal_name Bacillus megaterium DATE 31-Dec-1980 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS A25162; A92274; A92265; A03479 REFERENCE A25162 !$#authors Hackett, R.H.; Setlow, B.; Setlow, P. !$#journal J. Bacteriol. (1986) 168:1023-1025 !$#title Cloning and nucleotide sequence of the Bacillus megaterium !1gene coding for small, acid-soluble spore protein B. !$#cross-references MUID:87056915; PMID:2430935 !$#accession A25162 !'##molecule_type DNA !'##residues 1-97 ##label HAC !'##cross-references GB:M14161; NID:g142649; PIDN:AAA22293.1; !1PID:g142650 REFERENCE A92274 !$#authors Setlow, P.; Gerard, C.; Ozols, J. !$#journal J. Biol. Chem. (1980) 255:3624-3628 !$#title The amino acid sequence specificity of a protease from !1spores of Bacillus megaterium. !$#cross-references MUID:80159989; PMID:6767722 !$#accession A92274 !'##molecule_type protein !'##residues 2-20,'D',22-44;68-79 ##label SE1 REFERENCE A92265 !$#authors Setlow, P.; Ozols, J. !$#journal J. Biol. Chem. (1980) 255:10445-10450 !$#title The complete covalent structure of protein B. The third !1major protein degraded during germination of Bacillus !1megaterium spores. !$#cross-references MUID:81046882; PMID:6776116 !$#accession A92265 !'##molecule_type protein !'##residues 33-97 ##label SE2 COMMENT This storage protein has not been shown to associate with !1DNA or protect it from photochemical damage. CLASSIFICATION #superfamily gamma-type small acid-soluble spore protein KEYWORDS germination; sporulation; storage protein; tandem repeat FEATURE !$2-97 #product small acid-soluble spore protein B #status !8experimental #label MAT\ !$7-31 #domain spore protein repeat #label SB1\ !$32-66 #domain spore protein repeat #label SB2\ !$67-97 #domain spore protein repeat #label SB3\ !$32-33 #cleavage_site Glu-Phe (spore-specific proteinase) !8#status experimental\ !$67-68 #cleavage_site Glu-Phe (spore-specific proteinase) !8#status experimental SUMMARY #length 97 #molecular-weight 10438 #checksum 8182 SEQUENCE /// ENTRY C27086 #type complete TITLE small acid-soluble spore protein B - Thermoactinomyces sp. ORGANISM #formal_name Thermoactinomyces sp. DATE 15-Dec-1988 #sequence_revision 19-May-1994 #text_change 28-May-1999 ACCESSIONS C27086 REFERENCE A91837 !$#authors Sun, D.; Setlow, P. !$#journal J. Bacteriol. (1987) 169:3088-3093 !$#title Cloning and nucleotide sequencing of genes for a second type !1of small, acid-soluble spore proteins of Bacillus cereus, !1Bacillus stearothermophilus, and "Thermoactinomyces !1thalpophilus". !$#cross-references MUID:87250274; PMID:3036769 !$#accession C27086 !'##molecule_type DNA !'##residues 1-96 ##label SUN !'##cross-references GB:M16815; NID:g144133; PIDN:AAA23004.1; !1PID:g144134 !'##note source was designated as "T. thalpophilus" COMMENT This storage protein has not been shown to associate with !1DNA or protect it from photochemical damage. CLASSIFICATION #superfamily gamma-type small acid-soluble spore protein KEYWORDS germination; sporulation; storage protein; tandem repeat FEATURE !$2-96 #product small acid-soluble spore protein B #status !8predicted #label MAT\ !$8-35 #domain spore protein repeat #label SB1\ !$36-69 #domain spore protein repeat #label SB2\ !$70-96 #domain spore protein repeat #label SB3\ !$36-37 #cleavage_site Glu-Phe (spore-specific proteinase) !8#status predicted\ !$70-71 #cleavage_site Glu-Phe (spore-specific proteinase) !8#status predicted SUMMARY #length 96 #molecular-weight 10683 #checksum 8428 SEQUENCE /// ENTRY A26873 #type complete TITLE small acid-soluble spore protein (major gamma-type SASP) sspE - Bacillus subtilis ALTERNATE_NAMES SASP-delta CONTAINS small acid-soluble spore protein gamma ORGANISM #formal_name Bacillus subtilis DATE 19-Nov-1988 #sequence_revision 19-May-1994 #text_change 16-Jun-2000 ACCESSIONS A26873; C60927; C61111; C69719 REFERENCE A26873 !$#authors Hackett, R.H.; Setlow, P. !$#journal J. Bacteriol. (1987) 169:1985-1992 !$#title Cloning, nucleotide sequencing, and genetic mapping of the !1gene for small, acid-soluble spore protein gamma of Bacillus !1subtilis. !$#cross-references MUID:87194576; PMID:3106326 !$#accession A26873 !'##molecule_type DNA !'##residues 1-84 ##label HAC !'##cross-references GB:M16184; NID:g143711; PIDN:AAA22836.1; !1PID:g143712 REFERENCE A60927 !$#authors Blom, H.; Morse, R.; Mandelkorn, J.; Arnaud, M.; Warburg, !1R.; Tipper, D.J. !$#journal J. Gen. Microbiol. (1987) 133:2237-2246 !$#title The major acid-soluble proteins of Bacillus subtilis spores: !1partial amino acid sequence and forespore location of their !1mRNAs. !$#cross-references MUID:88171434; PMID:2450963 !$#accession C60927 !'##molecule_type protein !'##residues 2-13,'E',15-38 ##label BLO REFERENCE A61111 !$#authors Yuan, K.; Johnson, W.C.; Tipper, D.J.; Setlow, P. !$#journal J. Bacteriol. (1981) 146:965-971 !$#title Comparison of various properties of low-molecular-weight !1proteins from dormant spores of several Bacillus species. !$#cross-references MUID:81215316; PMID:6787019 !$#accession C61111 !'##molecule_type protein !'##residues 33-38;60-65 ##label YUA REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69719 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-84 ##label KUN !'##cross-references GB:Z99108; GB:AL009126; NID:g2633055; !1PIDN:CAB12694.1; PID:g2633189 !'##experimental_source strain 168 COMMENT This storage protein has not been shown to associate with !1DNA or protect it from photochemical damage. COMMENT It appears that SASP-gamma is derived from SASP-delta. GENETICS !$#gene sspE CLASSIFICATION #superfamily gamma-type small acid-soluble spore protein KEYWORDS germination; sporulation; storage protein; tandem repeat FEATURE !$2-84 #product small acid-soluble spore protein gamma/delta !8#status experimental #label MAT\ !$6-31 #domain spore protein repeat #label SB1\ !$32-58 #domain spore protein repeat #label SB2\ !$59-84 #domain spore protein repeat #label SB3\ !$32-33 #cleavage_site Glu-Phe (spore-specific proteinase) !8#status experimental\ !$59-60 #cleavage_site Glu-Phe (spore-specific proteinase) !8#status experimental SUMMARY #length 84 #molecular-weight 9268 #checksum 5824 SEQUENCE /// ENTRY B27086 #type complete TITLE small acid-soluble spore protein B - Bacillus stearothermophilus ORGANISM #formal_name Bacillus stearothermophilus DATE 15-Dec-1988 #sequence_revision 19-May-1994 #text_change 16-Jul-1999 ACCESSIONS B27086 REFERENCE A91837 !$#authors Sun, D.; Setlow, P. !$#journal J. Bacteriol. (1987) 169:3088-3093 !$#title Cloning and nucleotide sequencing of genes for a second type !1of small, acid-soluble spore proteins of Bacillus cereus, !1Bacillus stearothermophilus, and "Thermoactinomyces !1thalpophilus". !$#cross-references MUID:87250274; PMID:3036769 !$#accession B27086 !'##molecule_type DNA !'##residues 1-82 ##label SUN !'##cross-references GB:M16814; NID:g143517; PIDN:AAA22741.1; !1PID:g143518 COMMENT This storage protein has not been shown to associate with !1DNA or protect it from photochemical damage. CLASSIFICATION #superfamily gamma-type small acid-soluble spore protein KEYWORDS germination; sporulation; storage protein; tandem repeat FEATURE !$2-82 #product small acid-soluble spore protein B #status !8predicted #label MAT\ !$7-29 #domain spore protein repeat #label SB1\ !$30-56 #domain spore protein repeat #label SB2\ !$57-82 #domain spore protein repeat #label SB3\ !$30-31 #cleavage_site Glu-Phe (spore-specific proteinase) !8#status predicted\ !$57-58 #cleavage_site Glu-Phe (spore-specific proteinase) !8#status predicted SUMMARY #length 82 #molecular-weight 9021 #checksum 2100 SEQUENCE /// ENTRY A27086 #type complete TITLE small acid-soluble spore protein B - Bacillus cereus ALTERNATE_NAMES SASP-B ORGANISM #formal_name Bacillus cereus DATE 15-Dec-1988 #sequence_revision 19-May-1994 #text_change 16-Jul-1999 ACCESSIONS A27086; B61111 REFERENCE A91837 !$#authors Sun, D.; Setlow, P. !$#journal J. Bacteriol. (1987) 169:3088-3093 !$#title Cloning and nucleotide sequencing of genes for a second type !1of small, acid-soluble spore proteins of Bacillus cereus, !1Bacillus stearothermophilus, and "Thermoactinomyces !1thalpophilus". !$#cross-references MUID:87250274; PMID:3036769 !$#accession A27086 !'##molecule_type DNA !'##residues 1-93 ##label SUN !'##cross-references GB:M16813; NID:g143507; PIDN:AAA22736.1; !1PID:g143508 REFERENCE A61111 !$#authors Yuan, K.; Johnson, W.C.; Tipper, D.J.; Setlow, P. !$#journal J. Bacteriol. (1981) 146:965-971 !$#title Comparison of various properties of low-molecular-weight !1proteins from dormant spores of several Bacillus species. !$#cross-references MUID:81215316; PMID:6787019 !$#accession B61111 !'##molecule_type protein !'##residues 2-15;65-70 ##label YUA !'##note the peptide sequencing results shown here were revised in !1reference A27086 to reflect sequence from an additional !1cleavage site COMMENT This storage protein has not been shown to associate with !1DNA or protect it from photochemical damage. CLASSIFICATION #superfamily gamma-type small acid-soluble spore protein KEYWORDS germination; sporulation; storage protein; tandem repeat FEATURE !$2-93 #product small acid-soluble spore protein B #status !8experimental #label MAT\ !$7-26 #domain spore protein repeat #label SB1\ !$27-63 #domain spore protein repeat #label SB2\ !$64-93 #domain spore protein repeat #label SB3\ !$27-28 #cleavage_site Glu-Phe (spore-specific proteinase) !8#status experimental\ !$64-65 #cleavage_site Glu-Phe (spore-specific proteinase) !8#status experimental SUMMARY #length 93 #molecular-weight 9671 #checksum 6314 SEQUENCE /// ENTRY A36939 #type complete TITLE small acid-soluble spore protein SASP-G - Bacillus megaterium (strain QMB1551) 111-kb plasmid ORGANISM #formal_name Bacillus megaterium DATE 11-Nov-1994 #sequence_revision 02-Dec-1994 #text_change 16-Jul-1999 ACCESSIONS A36939; B36939 REFERENCE A36939 !$#authors Carrillo-Martinez, Y.; Setlow, P. !$#journal J. Bacteriol. (1993) 175:6337-6340 !$#title Cloning and nucleotide sequence of a plasmid-carried gene !1coding for a minor small, acid-soluble protein from Bacillus !1megaterium spores. !$#cross-references MUID:94012497; PMID:8407806 !$#accession A36939 !'##molecule_type DNA !'##residues 1-43 ##label CAR !'##cross-references GB:L20464; NID:g304174; PIDN:AAC36830.1; !1PID:g304175 !'##note authors translated the codon ACG for residue 33 as Ser !$#accession B36939 !'##molecule_type protein !'##residues 2-41 ##label CA2 COMMENT This minor small, acid-soluble spore protein (SASP) is !1unusual in containing tryptophan residues and a high !1percentage of lysine residues. COMMENT No homolog to this protein could be detected in Bacillus !1subtilis or Bacillus cereus. GENETICS !$#gene sspG !$#genome plasmid CLASSIFICATION #superfamily small acid-soluble spore protein SASP-G KEYWORDS germination; sporulation; storage protein FEATURE !$2-43 #product small acid-soluble spore protein SASP-G !8#status experimental #label MAT SUMMARY #length 43 #molecular-weight 5071 #checksum 2224 SEQUENCE /// ENTRY F69629 #type complete TITLE spore germination protein II - Bacillus subtilis ALTERNATE_NAMES germination response to L-alanine gerAB ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS F69629; A26470 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69629 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-365 ##label KUN !'##cross-references GB:Z99120; GB:AL009126; NID:g2635613; !1PIDN:CAB15296.1; PID:g2635803 !'##experimental_source strain 168 REFERENCE A91571 !$#authors Zuberi, A.R.; Moir, A.; Feavers, I.M. !$#journal Gene (1987) 51:1-11 !$#title The nucleotide sequence and gene organization of the gerA !1spore germination operon of Bacillus subtilis 168. !$#cross-references MUID:87248055; PMID:3110007 !$#accession A26470 !'##molecule_type DNA !'##residues 1-41,43-231,'LF',234-348,'AVHSL',354,'H',356-365 ##label !1ZUB !'##cross-references GB:M16189; NID:g1236177 !'##experimental_source strain 168 GENETICS !$#gene gerAB CLASSIFICATION #superfamily spore germination protein KEYWORDS transmembrane protein SUMMARY #length 365 #molecular-weight 41458 #checksum 7070 SEQUENCE /// ENTRY E69889 #type complete TITLE spore germination protein homolog yndE - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS E69889 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69889 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-363 ##label KUN !'##cross-references GB:Z99113; GB:AL009126; NID:g2634090; !1PIDN:CAB13660.1; PID:g2634160 !'##experimental_source strain 168 GENETICS !$#gene yndE CLASSIFICATION #superfamily spore germination protein SUMMARY #length 363 #molecular-weight 40470 #checksum 5211 SEQUENCE /// ENTRY I39856 #type complete TITLE spore germination apparatus protein gerBB - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS I39856; A69630 REFERENCE I39854 !$#authors Corfe, B.M.; Sammons, R.L.; Smith, D.A.; Mauel, C. !$#journal Microbiology (1994) 140:471-478 !$#title The gerB region of the Bacillus subtilis 168 chromosome !1encodes a homologue of the gerA spore germination operon. !$#cross-references MUID:94282292; PMID:8012571 !$#accession I39856 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-368 ##label RES !'##cross-references GB:L16960; NID:g289274; PIDN:AAA22467.1; !1PID:g289276 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69630 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-368 ##label KUN !'##cross-references GB:Z99122; GB:AL009126; NID:g2636029; !1PIDN:CAB15598.1; PID:g2636107 !'##experimental_source strain 168 !'##note germination response to the combination of glucose, fructose, !1L-asparagine, and KCL GENETICS !$#gene gerBB; gerB-2 !$#map_position 314 deg. CLASSIFICATION #superfamily spore germination protein SUMMARY #length 368 #molecular-weight 41709 #checksum 309 SEQUENCE /// ENTRY I39860 #type complete TITLE germination response protein gerKB - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS I39860; A69631 REFERENCE I39858 !$#authors Irie, R.; Fujita, Y.Y.F.; Okamoto, T. !$#journal J. Gen. Microbiol. (1993) 39:453-465 !$#title Cloning and sequencing of the gerK spore germination gene of !1Bacillus subtilis 168. !$#accession I39860 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-373 ##label RES !'##cross-references GB:D78187; NID:g1063253; PIDN:BAA11256.1; !1PID:g1063256 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69631 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-373 ##label KUN !'##cross-references GB:Z99106; GB:AL009126; NID:g2632653; !1PIDN:CAB12180.1; PID:g2632673 !'##experimental_source strain 168 !'##note germination response to the combination of glucose, fructose, !1L-asparagine, and KCl GENETICS !$#gene gerKB CLASSIFICATION #superfamily spore germination protein SUMMARY #length 373 #molecular-weight 41770 #checksum 9353 SEQUENCE /// ENTRY A36131 #type complete TITLE positive regulator of sigma-B activity (anti-anti-sigma factor) rsbV - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A36131; A69702 REFERENCE A36131 !$#authors Kalman, S.; Duncan, M.L.; Thomas, S.M.; Price, C.W. !$#journal J. Bacteriol. (1990) 172:5575-5585 !$#title Similar organization of the sigB and spoIIA operons encoding !1alternate sigma factors of Bacillus subtilis RNA polymerase. !$#cross-references MUID:91008924; PMID:2170324 !$#accession A36131 !'##status preliminary !'##molecule_type DNA !'##residues 1-109 ##label KAL !'##cross-references GB:M34995; NID:g143457; PIDN:AAA22711.1; !1PID:g143458 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69702 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-109 ##label KUN !'##cross-references GB:Z99106; GB:AL009126; NID:g2632653; !1PIDN:CAB12278.1; PID:g2632771 !'##experimental_source strain 168 GENETICS !$#gene rsbV CLASSIFICATION #superfamily sporulation protein stage II KEYWORDS phosphoprotein SUMMARY #length 109 #molecular-weight 11939 #checksum 9651 SEQUENCE /// ENTRY A55646 #type complete TITLE stage II sporulation protein AA protein - Bacillus subtilis ALTERNATE_NAMES sigma-F 5'-region regulatory protein spoIIAA ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A55646; C42708; A47540; F69710 REFERENCE A55646 !$#authors Fort, P.; Piggot, P.J. !$#journal J. Gen. Microbiol. (1984) 130:2147-2153 !$#title Nucleotide sequence of sporulation locus spoIIA in Bacillus !1subtilis. !$#cross-references MUID:84291358; PMID:6088674 !$#accession A55646 !'##molecule_type DNA !'##residues 1-119 ##label FOR !'##cross-references GB:M85047 REFERENCE A42708 !$#authors Wu, J.J.; Schuch, R.; Piggot, P.J. !$#journal J. Bacteriol. (1992) 174:4885-4892 !$#title Characterization of a Bacillus subtilis sporulation operon !1that includes genes for an RNA polymerase sigma factor and !1for a putative DD-carboxypeptidase. !$#cross-references MUID:92332420; PMID:1629150 !$#accession C42708 !'##molecule_type DNA !'##residues 3-6 ##label WU1 !'##note sequence extracted from NCBI backbone (NCBIN:108894, !1NCBIP:111054) REFERENCE A47540 !$#authors Min, K.T.; Hilditch, C.M.; Diederich, B.; Errington, J.; !1Yudkin, M.D. !$#journal Cell (1993) 74:735-742 !$#title sigma(F), the first compartment-specific transcription !1factor of Bacillus subtilis, is regulated by an anti-sigma !1factor that is also a protein kinase. !$#cross-references MUID:93364989; PMID:8358793 !$#accession A47540 !'##molecule_type protein !'##residues 4-16 ##label MIN !'##note overexpression of recombinant protein in E. coli !'##note translation is shown from Met-1 to illustrate the longest open !1reading frame; Met-3 may be the preferred initiator REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69710 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 3-119 ##label KUN !'##cross-references GB:Z99116; GB:AL009126; NID:g2634723; !1PIDN:CAB14279.1; PID:g2634782 !'##experimental_source strain 168 GENETICS !$#gene spoIIAA CLASSIFICATION #superfamily sporulation protein stage II KEYWORDS phosphoprotein; sporulation SUMMARY #length 119 #molecular-weight 13208 #checksum 1375 SEQUENCE /// ENTRY I39857 #type complete TITLE spore germination apparatus protein gerBC - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS I39857; B69630 REFERENCE I39854 !$#authors Corfe, B.M.; Sammons, R.L.; Smith, D.A.; Mauel, C. !$#journal Microbiology (1994) 140:471-478 !$#title The gerB region of the Bacillus subtilis 168 chromosome !1encodes a homologue of the gerA spore germination operon. !$#cross-references MUID:94282292; PMID:8012571 !$#accession I39857 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-374 ##label RES !'##cross-references GB:L16960; NID:g289274; PIDN:AAA22468.1; !1PID:g289277 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69630 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-374 ##label KUN !'##cross-references GB:Z99122; GB:AL009126; NID:g2636029; !1PIDN:CAB15599.1; PID:g2636108 !'##experimental_source strain 168 !'##note germination response to the combination of glucose, fructose, !1L-asparagine, and KCL GENETICS !$#gene gerBC; gerB-3 !$#map_position 314 deg. CLASSIFICATION #superfamily spore germination protein III SUMMARY #length 374 #molecular-weight 42468 #checksum 9522 SEQUENCE /// ENTRY F69889 #type complete TITLE spore germination protein homolog yndF - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS F69889 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69889 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-404 ##label KUN !'##cross-references GB:Z99113; GB:AL009126; NID:g2634090; !1PIDN:CAB13661.1; PID:g2634161 !'##experimental_source strain 168 GENETICS !$#gene yndF CLASSIFICATION #superfamily spore germination protein III SUMMARY #length 404 #molecular-weight 44824 #checksum 6588 SEQUENCE /// ENTRY A26936 #type complete TITLE NAD synthase (EC 6.3.1.5) [validated] - Bacillus subtilis ALTERNATE_NAMES 32K phosphoprotein outB; NH3-dependent NAD+ synthetase nadE; spore outgrowth factor B ORGANISM #formal_name Bacillus subtilis DATE 03-Mar-1994 #sequence_revision 03-Mar-1994 #text_change 03-Jun-2002 ACCESSIONS A26936; C41835; H69663 REFERENCE A26936 !$#authors Albertini, A.M.; Caramori, T.; Henner, D.; Ferrari, E.; !1Galizzi, A. !$#journal J. Bacteriol. (1987) 169:1480-1484 !$#title Nucleotide sequence of the outB locus of Bacillus subtilis !1and regulation of its expression. !$#cross-references MUID:87165753; PMID:2435704 !$#accession A26936 !'##molecule_type DNA !'##residues 1-272 ##label ALB !'##cross-references GB:M15811; NID:g143278; PIDN:AAA22635.1; !1PID:g143279 REFERENCE A41835 !$#authors Mitchell, C.; Morris, P.W.; Vary, J.C. !$#journal J. Bacteriol. (1992) 174:2474-2477 !$#title Identification of proteins phosphorylated by ATP during !1sporulation of Bacillus subtilis. !$#cross-references MUID:92210489; PMID:1556067 !$#accession C41835 !'##molecule_type protein !'##residues 2-11 ##label MIT REFERENCE A67658 !$#authors Rizzi, M.; Nessi, C.; Bolognesi, M.; Galizzi, A.; Coda, A. !$#submission submitted to the Brookhaven Protein Data Bank, July 1996 !$#cross-references PDB:1NSY !$#contents annotation; X-ray crystallography, 2.0 angstroms, residues !12-272 REFERENCE A58683 !$#authors Rizzi, M.; Nessi, C.; Mattevi, A.; Coda, A.; Bolognesi, M.; !1Galizzi, A. !$#journal EMBO J. (1996) 15:5125-5134 !$#title Crystal structure of NH-3-dependent NAD+ synthetase from !1Bacillus subtilis. !$#cross-references MUID:97050817; PMID:8895556 !$#contents annotation; X-ray crystallography, 2.0 angstroms REFERENCE A58684 !$#authors Nessi, C.; Albertini, A.M.; Speranza, M.L.; Galizzi, A. !$#journal J. Biol. Chem. (1995) 270:6181-6185 !$#title The outB gene of Bacillus subtilis codes for NAD synthetase. !$#cross-references MUID:95197650; PMID:7890752 !$#contents annotation; enzymatic activity REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69663 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-272 ##label KUN !'##cross-references GB:Z99105; GB:AL009126; NID:g2632457; !1PIDN:CAB12107.1; PID:g2632599 !'##experimental_source strain 168 COMMENT One mRNA transcript for this protein is expressed !1constitutively at low levels. A second, longer transcript !1from an upstream promoter is produced during spore !1outgrowth. GENETICS !$#gene nadE; outB COMPLEX homodimer [validated, MUID:95197650] FUNCTION !$#description EC 6.3.1.5 [validated, MUID:95197650]; catalyzes the !1amidation of nicotinic acid dinucleotide to NAD by ammonia !1with the hydrolysis of ATP to AMP and pyrophosphate !$#pathway NAD biosynthesis CLASSIFICATION #superfamily Bacillus subtilis NH3-dependent NAD+ synthase KEYWORDS ATP; homodimer; ligase; magnesium; metalloprotein; NAD !1biosynthesis FEATURE !$2-272 #product NAD+ synthase #status experimental #label !8MAT\ !$47 #active_site Ser #status predicted\ !$51,163 #binding_site magnesium (Asp, Glu) #status !8experimental SUMMARY #length 272 #molecular-weight 30395 #checksum 4283 SEQUENCE /// ENTRY ZZZRAM #type complete TITLE nodulation protein nodA - Rhizobium meliloti ORGANISM #formal_name Rhizobium meliloti DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 16-Jul-1999 ACCESSIONS A03480 REFERENCE A90951 !$#authors Egelhoff, T.T.; Fisher, R.F.; Jacobs, T.W.; Mulligan, J.T.; !1Long, S.R. !$#journal DNA (1985) 4:241-248 !$#title Nucleotide sequence of Rhizobium meliloti 1021 nodulation !1genes: nodD is read divergently from modABC. !$#cross-references MUID:85229955; PMID:4006668 !$#accession A03480 !'##molecule_type DNA !'##residues 1-196 ##label EGE !'##cross-references GB:M11268; NID:g152340; PIDN:AAA98360.1; !1PID:g152342 !'##experimental_source strain 1021 symbiotic plasmid COMMENT This is one of the proteins, coded by nodulation genes, that !1are required for R. meliloti to invade and stimulate nodule !1formation in its leguminous hosts. GENETICS !$#gene nodA CLASSIFICATION #superfamily nodulation protein nodA KEYWORDS nodulation SUMMARY #length 196 #molecular-weight 21779 #checksum 2595 SEQUENCE /// ENTRY ZZZRA4 #type complete TITLE nodulation protein nodA - Rhizobium meliloti (strain 41) ORGANISM #formal_name Rhizobium meliloti DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 16-Jul-1999 ACCESSIONS A03481 REFERENCE A93553 !$#authors Torok, I.; Kondorosi, E.; Stepkowski, T.; Posfai, J.; !1Kondorosi, A. !$#journal Nucleic Acids Res. (1984) 12:9509-9524 !$#title Nucleotide sequence of Rhizobium meliloti nodulation genes. !$#cross-references MUID:85087953; PMID:6336331 !$#accession A03481 !'##molecule_type DNA !'##residues 1-196 ##label TOR !'##cross-references GB:X01649; GB:M13287; NID:g46287; PIDN:CAA25808.1; !1PID:g46289 COMMENT This is one of the proteins, coded by nodulation genes, that !1are required for R. meliloti to invade and stimulate nodule !1formation in its leguminous hosts. GENETICS !$#gene nodA CLASSIFICATION #superfamily nodulation protein nodA KEYWORDS nodulation SUMMARY #length 196 #molecular-weight 21837 #checksum 2605 SEQUENCE /// ENTRY ZZZRAL #type complete TITLE nodulation protein nodA - Rhizobium leguminosarum plasmid pRL1JI ORGANISM #formal_name Rhizobium leguminosarum DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 16-Jul-1999 ACCESSIONS A03482 REFERENCE A03482 !$#authors Rossen, L.; Johnston, A.W.B.; Downie, J.A. !$#journal Nucleic Acids Res. (1984) 12:9497-9508 !$#title DNA sequence of the Rhizobium leguminosarum nodulation genes !1nodAB and C required for root hair curling. !$#cross-references MUID:85087952; PMID:6514582 !$#accession A03482 !'##molecule_type DNA !'##residues 1-157 ##label ROS !'##cross-references GB:X01650; NID:g46223; PIDN:CAA25812.1; PID:g46224 COMMENT This is one of the proteins, coded by nodulation genes, that !1are required for R. leguminosarum to invade and stimulate !1nodule formation in its leguminous hosts. GENETICS !$#gene nodA !$#genome plasmid CLASSIFICATION #superfamily nodulation protein nodA KEYWORDS nodulation SUMMARY #length 157 #molecular-weight 17579 #checksum 3759 SEQUENCE /// ENTRY A23766 #type complete TITLE nodulation protein nodA - Rhizobium leguminosarum bv. trifolii ORGANISM #formal_name Rhizobium leguminosarum bv. trifolii DATE 21-May-1988 #sequence_revision 27-Jan-1995 #text_change 10-Feb-1995 ACCESSIONS A23766 REFERENCE A93614 !$#authors Schofield, P.R.; Watson, J.M. !$#journal Nucleic Acids Res. (1986) 14:2891-2903 !$#title DNA sequence of Rhizobium trifolii nodulation genes reveals !1a reiterated and potentially regulatory sequence preceding !1nodABC and nodFE. !$#cross-references MUID:86176774; PMID:3008100 !$#accession A23766 !'##molecule_type DNA !'##residues 1-196 ##label SCH !'##cross-references GB:X03721 !'##experimental_source strain ANU843 COMMENT This is one of the proteins, coded by nodulation genes, that !1are required for this bacterium to invade and stimulate !1nodule formation in its hosts. GENETICS !$#gene nodA CLASSIFICATION #superfamily nodulation protein nodA KEYWORDS nodulation SUMMARY #length 196 #molecular-weight 21642 #checksum 1347 SEQUENCE /// ENTRY S34303 #type complete TITLE nodulation protein nodA - Rhizobium sp. ORGANISM #formal_name Rhizobium sp. DATE 13-Jan-1995 #sequence_revision 27-Jan-1995 #text_change 16-Jul-1999 ACCESSIONS S34303 REFERENCE S34303 !$#authors Relix, B.; Perret, X.; Golinowsky, W.; Pueppke, S.G.; !1Krishnan, H.B.; Broughton, W.J. !$#submission submitted to the EMBL Data Library, June 1993 !$#description Lipo-oligosaccharide Nod-factor signals permit rhizobial !1penetration into legume roots. !$#accession S34303 !'##molecule_type DNA !'##residues 1-196 ##label REL !'##cross-references EMBL:X73362; NID:g312347; PIDN:CAA51772.1; !1PID:g312348 COMMENT This is one of the proteins, coded by nodulation genes, that !1are required for this bacterium to invade and stimulate !1nodule formation in its hosts. GENETICS !$#gene nodA CLASSIFICATION #superfamily nodulation protein nodA KEYWORDS nodulation SUMMARY #length 196 #molecular-weight 21899 #checksum 6981 SEQUENCE /// ENTRY A38180 #type complete TITLE nodulation protein nodA - Rhizobium leguminosarum bv. phaseoli ORGANISM #formal_name Rhizobium leguminosarum bv. phaseoli DATE 28-Aug-1992 #sequence_revision 27-Jan-1995 #text_change 16-Jul-1999 ACCESSIONS A38180 REFERENCE A38180 !$#authors Vazquez, M.; Davalos, A.; de las Penas, A.; Sanchez, F.; !1Quinto, C. !$#journal J. Bacteriol. (1991) 173:1250-1258 !$#title Novel organization of the common nodulation genes in !1Rhizobium leguminosarum bv. phaseoli strains. !$#cross-references MUID:91123201; PMID:1991718 !$#accession A38180 !'##molecule_type DNA !'##residues 1-195 ##label VAZ !'##cross-references GB:M58625; NID:g150471; PIDN:AAA98207.1; !1PID:g150472 COMMENT This is one of the proteins, coded by nodulation genes, that !1are required for this bacterium to invade and stimulate !1nodule formation in its hosts. GENETICS !$#gene nodA CLASSIFICATION #superfamily nodulation protein nodA KEYWORDS nodulation SUMMARY #length 195 #molecular-weight 21870 #checksum 7110 SEQUENCE /// ENTRY A26813 #type complete TITLE nodulation protein nodA - Bradyrhizobium sp. ORGANISM #formal_name Bradyrhizobium sp. DATE 19-Nov-1988 #sequence_revision 27-Jan-1995 #text_change 16-Jul-1999 ACCESSIONS A26813 REFERENCE A93615 !$#authors Scott, K.F. !$#journal Nucleic Acids Res. (1986) 14:2905-2919 !$#title Conserved nodulation genes from the non-legume symbiont !1Bradyrhizobium sp. (Parasponia). !$#cross-references MUID:86176775; PMID:3960737 !$#accession A26813 !'##molecule_type DNA !'##residues 1-210 ##label SCO !'##cross-references GB:X03720; NID:g39996; PIDN:CAA27348.1; PID:g39999 COMMENT This is one of the proteins, coded by nodulation genes, that !1are required for this bacterium to invade and stimulate !1nodule formation in its hosts. GENETICS !$#gene nodA CLASSIFICATION #superfamily nodulation protein nodA KEYWORDS nodulation SUMMARY #length 210 #molecular-weight 23320 #checksum 6267 SEQUENCE /// ENTRY JQ0393 #type complete TITLE nodulation protein nodA - Azorhizobium caulinodans ALTERNATE_NAMES hypothetical 24.9K protein ORGANISM #formal_name Azorhizobium caulinodans #note host Sesbania rostrata DATE 07-Sep-1990 #sequence_revision 27-Jan-1995 #text_change 16-Jul-1999 ACCESSIONS JQ0393 REFERENCE JQ0393 !$#authors Goethals, K.; Gao, M.; Tomekpe, K.; Van Montagu, M.; !1Holsters, M. !$#journal Mol. Gen. Genet. (1989) 219:289-298 !$#title Common nodABC genes in Nod locus 1 of Azorhizobium !1caulinodans: nucleotide sequence and plant-inducible !1expression. !$#cross-references MUID:90136519; PMID:2615763 !$#accession JQ0393 !'##molecule_type DNA !'##residues 1-226 ##label GOE !'##cross-references GB:L18897; NID:g1293899; PIDN:AAB51162.1; !1PID:g310292 !'##experimental_source strain ORS571 COMMENT This is one of the proteins, coded by nodulation genes, that !1are required for this bacterium to invade and stimulate !1nodule formation in its hosts. GENETICS !$#gene nodA CLASSIFICATION #superfamily nodulation protein nodA KEYWORDS nodulation SUMMARY #length 226 #molecular-weight 24915 #checksum 309 SEQUENCE /// ENTRY ZZZRBM #type complete TITLE nodulation protein nodB - Rhizobium meliloti ORGANISM #formal_name Rhizobium meliloti DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 11-Apr-1997 ACCESSIONS A03483 REFERENCE A90951 !$#authors Egelhoff, T.T.; Fisher, R.F.; Jacobs, T.W.; Mulligan, J.T.; !1Long, S.R. !$#journal DNA (1985) 4:241-248 !$#title Nucleotide sequence of Rhizobium meliloti 1021 nodulation !1genes: nodD is read divergently from modABC. !$#cross-references MUID:85229955; PMID:4006668 !$#accession A03483 !'##molecule_type DNA !'##residues 1-217 ##label EGE !'##cross-references GB:X01649 !'##experimental_source strain 1021 symbiotic plasmid COMMENT This is one of the proteins, coded by nodulation genes, that !1are required for R. meliloti to invade and stimulate nodule !1formation in its leguminous hosts. GENETICS !$#gene nodB CLASSIFICATION #superfamily nodulation protein nodB; nodB homology KEYWORDS nodulation FEATURE !$26-175 #domain nodB homology #label NODB SUMMARY #length 217 #molecular-weight 23798 #checksum 7861 SEQUENCE /// ENTRY ZZZRB4 #type complete TITLE nodulation protein nodB - Rhizobium meliloti (strain 41) ORGANISM #formal_name Rhizobium meliloti DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 16-Jul-1999 ACCESSIONS A03484 REFERENCE A93553 !$#authors Torok, I.; Kondorosi, E.; Stepkowski, T.; Posfai, J.; !1Kondorosi, A. !$#journal Nucleic Acids Res. (1984) 12:9509-9524 !$#title Nucleotide sequence of Rhizobium meliloti nodulation genes. !$#cross-references MUID:85087953; PMID:6336331 !$#accession A03484 !'##molecule_type DNA !'##residues 1-217 ##label TOR !'##cross-references GB:X01649; GB:M13287; NID:g46287; PIDN:CAA25809.1; !1PID:g46290 !'##experimental_source strain 41 COMMENT This is one of the proteins, coded by nodulation genes, that !1are required for R. meliloti to invade and stimulate nodule !1formation in its leguminous hosts. GENETICS !$#gene nodB CLASSIFICATION #superfamily nodulation protein nodB; nodB homology KEYWORDS nodulation FEATURE !$26-175 #domain nodB homology #label NODB SUMMARY #length 217 #molecular-weight 23753 #checksum 4826 SEQUENCE /// ENTRY ZZZRBL #type complete TITLE nodulation protein nodB - Rhizobium leguminosarum plasmid pRL1JI ORGANISM #formal_name Rhizobium leguminosarum DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 16-Jul-1999 ACCESSIONS A03485; S10232 REFERENCE A03482 !$#authors Rossen, L.; Johnston, A.W.B.; Downie, J.A. !$#journal Nucleic Acids Res. (1984) 12:9497-9508 !$#title DNA sequence of the Rhizobium leguminosarum nodulation genes !1nodAB and C required for root hair curling. !$#cross-references MUID:85087952; PMID:6514582 !$#accession A03485 !'##molecule_type DNA !'##residues 1-216 ##label ROS !'##cross-references GB:X01650; NID:g46223; PIDN:CAA25813.1; PID:g46225 REFERENCE S02059 !$#authors Downie, J.A. !$#submission submitted to the EMBL Data Library, April 1988 !$#accession S10232 !'##molecule_type DNA !'##residues 1-6,'IG',9-216 ##label DOW !'##cross-references EMBL:Y00548; NID:g46212; PIDN:CAA68620.1; !1PID:g46216 COMMENT This is one of the proteins, coded by nodulation genes, that !1are required for R. leguminosarum to invade and stimulate !1nodule formation in its leguminous hosts. GENETICS !$#gene nodB !$#genome plasmid CLASSIFICATION #superfamily nodulation protein nodB; nodB homology KEYWORDS nodulation FEATURE !$26-175 #domain nodB homology #label NODB SUMMARY #length 216 #molecular-weight 23632 #checksum 1168 SEQUENCE /// ENTRY B23766 #type complete TITLE nodulation protein nodB - Rhizobium leguminosarum bv. trifolii ORGANISM #formal_name Rhizobium leguminosarum bv. trifolii DATE 21-May-1988 #sequence_revision 27-Jan-1995 #text_change 16-Jul-1999 ACCESSIONS B23766 REFERENCE A93614 !$#authors Schofield, P.R.; Watson, J.M. !$#journal Nucleic Acids Res. (1986) 14:2891-2903 !$#title DNA sequence of Rhizobium trifolii nodulation genes reveals !1a reiterated and potentially regulatory sequence preceding !1nodABC and nodFE. !$#cross-references MUID:86176774; PMID:3008100 !$#accession B23766 !'##molecule_type DNA !'##residues 1-215 ##label SCH !'##cross-references GB:X03721; NID:g46461; PIDN:CAA27352.1; PID:g46463 !'##experimental_source strain ANU843 COMMENT This is one of the proteins, coded by nodulation genes, that !1are required for this bacterium to invade and stimulate !1nodule formation in its hosts. GENETICS !$#gene nodB CLASSIFICATION #superfamily nodulation protein nodB; nodB homology KEYWORDS nodulation FEATURE !$25-173 #domain nodB homology #label NODB SUMMARY #length 215 #molecular-weight 23541 #checksum 9438 SEQUENCE /// ENTRY D38180 #type complete TITLE nodulation protein nodB homolog - Rhizobium leguminosarum bv. phaseoli ORGANISM #formal_name Rhizobium leguminosarum bv. phaseoli DATE 28-Aug-1992 #sequence_revision 27-Jan-1995 #text_change 16-Jul-1999 ACCESSIONS D38180 REFERENCE A38180 !$#authors Vazquez, M.; Davalos, A.; de las Penas, A.; Sanchez, F.; !1Quinto, C. !$#journal J. Bacteriol. (1991) 173:1250-1258 !$#title Novel organization of the common nodulation genes in !1Rhizobium leguminosarum bv. phaseoli strains. !$#cross-references MUID:91123201; PMID:1991718 !$#accession D38180 !'##molecule_type DNA !'##residues 1-229 ##label VAZ !'##cross-references GB:M58626; NID:g150473; PIDN:AAA98210.1; !1PID:g150476 COMMENT This is one of the proteins, coded by nodulation genes, that !1are required for this bacterium to invade and stimulate !1nodule formation in its hosts. GENETICS !$#gene nodA CLASSIFICATION #superfamily nodulation protein nodB; nodB homology KEYWORDS nodulation FEATURE !$26-176 #domain nodB homology #label NODB SUMMARY #length 229 #molecular-weight 25061 #checksum 9975 SEQUENCE /// ENTRY B26813 #type complete TITLE nodulation protein nodB - Bradyrhizobium sp. ORGANISM #formal_name Bradyrhizobium sp. DATE 19-Nov-1988 #sequence_revision 27-Jan-1995 #text_change 11-Apr-1997 ACCESSIONS B26813 REFERENCE A93615 !$#authors Scott, K.F. !$#journal Nucleic Acids Res. (1986) 14:2905-2919 !$#title Conserved nodulation genes from the non-legume symbiont !1Bradyrhizobium sp. (Parasponia). !$#cross-references MUID:86176775; PMID:3960737 !$#accession B26813 !'##molecule_type DNA !'##residues 1-219 ##label SCO !'##cross-references GB:X03720 COMMENT This is one of the proteins, coded by nodulation genes, that !1are required for this bacterium to invade and stimulate !1nodule formation in its hosts. GENETICS !$#gene nodB !$#start_codon GTG CLASSIFICATION #superfamily nodulation protein nodB; nodB homology KEYWORDS nodulation FEATURE !$26-175 #domain nodB homology #label NODB SUMMARY #length 219 #molecular-weight 24247 #checksum 8640 SEQUENCE /// ENTRY S34304 #type complete TITLE nodulation protein nodB - Rhizobium sp. ORGANISM #formal_name Rhizobium sp. DATE 13-Jan-1995 #sequence_revision 27-Jan-1995 #text_change 16-Jul-1999 ACCESSIONS S34304 REFERENCE S34303 !$#authors Relix, B.; Perret, X.; Golinowsky, W.; Pueppke, S.G.; !1Krishnan, H.B.; Broughton, W.J. !$#submission submitted to the EMBL Data Library, June 1993 !$#description Lipo-oligosaccharide Nod-factor signals permit rhizobial !1penetration into legume roots. !$#accession S34304 !'##molecule_type DNA !'##residues 1-214 ##label REL !'##cross-references EMBL:X73362; NID:g312347; PIDN:CAA51773.1; !1PID:g312349 COMMENT This is one of the proteins, coded by nodulation genes, that !1are required for this bacterium to invade and stimulate !1nodule formation in its hosts. GENETICS !$#gene nodB CLASSIFICATION #superfamily nodulation protein nodB; nodB homology KEYWORDS nodulation FEATURE !$23-171 #domain nodB homology #label NODB SUMMARY #length 214 #molecular-weight 23458 #checksum 7482 SEQUENCE /// ENTRY JQ0394 #type complete TITLE nodB protein - Azorhizobium caulinodans ORGANISM #formal_name Azorhizobium caulinodans #note host Sesbania rostrata DATE 07-Sep-1990 #sequence_revision 27-Jan-1995 #text_change 16-Jul-1999 ACCESSIONS JQ0394 REFERENCE JQ0393 !$#authors Goethals, K.; Gao, M.; Tomekpe, K.; Van Montagu, M.; !1Holsters, M. !$#journal Mol. Gen. Genet. (1989) 219:289-298 !$#title Common nodABC genes in Nod locus 1 of Azorhizobium !1caulinodans: nucleotide sequence and plant-inducible !1expression. !$#cross-references MUID:90136519; PMID:2615763 !$#accession JQ0394 !'##molecule_type DNA !'##residues 1-210 ##label GOE !'##cross-references GB:L18897; NID:g1293899; PIDN:AAB51163.1; !1PID:g310293 !'##experimental_source strain ORS571 COMMENT This is one of the proteins, coded by nodulation genes, that !1are required for this bacterium to invade and stimulate !1nodule formation in its hosts. GENETICS !$#gene nodB CLASSIFICATION #superfamily nodulation protein nodB; nodB homology KEYWORDS nodulation FEATURE !$20-169 #domain nodB homology #label NODB SUMMARY #length 210 #molecular-weight 23418 #checksum 3416 SEQUENCE /// ENTRY B47692 #type complete TITLE nodulation protein nodB homolog - Bacillus stearothermophilus ORGANISM #formal_name Bacillus stearothermophilus DATE 19-Dec-1993 #sequence_revision 27-Jan-1995 #text_change 11-Apr-1997 ACCESSIONS B47692 REFERENCE A47692 !$#authors Reaney, S.K.; Bungard, S.J.; Guest, J.R. !$#journal J. Gen. Microbiol. (1993) 139:403-416 !$#title Molecular and enzymological evidence for two classes of !1fumarase in Bacillus stearothermophilus (var. !1non-diastaticus). !$#cross-references MUID:93232761; PMID:8473853 !$#accession B47692 !'##molecule_type DNA !'##residues 1-265 ##label REA !'##experimental_source var. non-diastaticus, DSM 2334 !'##note sequence extracted from NCBI backbone (NCBIN:129946, !1NCBIP:129948) CLASSIFICATION #superfamily nodulation protein nodB; nodB homology FEATURE !$72-224 #domain nodB homology #label NODB SUMMARY #length 265 #molecular-weight 30565 #checksum 9949 SEQUENCE /// ENTRY ZZZRCL #type complete TITLE nodulation protein nodC - Rhizobium leguminosarum plasmid pRL1JI ORGANISM #formal_name Rhizobium leguminosarum DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 21-Jul-2000 ACCESSIONS A03486 REFERENCE A03482 !$#authors Rossen, L.; Johnston, A.W.B.; Downie, J.A. !$#journal Nucleic Acids Res. (1984) 12:9497-9508 !$#title DNA sequence of the Rhizobium leguminosarum nodulation genes !1nodAB and C required for root hair curling. !$#cross-references MUID:85087952; PMID:6514582 !$#accession A03486 !'##molecule_type DNA !'##residues 1-424 ##label ROS !'##cross-references GB:X01650; NID:g46212; PIDN:CAA68619.1; PID:g46215 COMMENT This is one of the proteins, coded by nodulation genes, that !1are required for R. leguminosarum to invade and stimulate !1nodule formation in its leguminous hosts. GENETICS !$#gene nodC !$#genome plasmid CLASSIFICATION #superfamily nodulation protein nodC KEYWORDS nodulation SUMMARY #length 424 #molecular-weight 46255 #checksum 9365 SEQUENCE /// ENTRY ZZZRC4 #type complete TITLE nodulation protein nodC - Rhizobium meliloti (strain 41) ORGANISM #formal_name Rhizobium meliloti DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 16-Jul-1999 ACCESSIONS A03487; A25097 REFERENCE A93553 !$#authors Torok, I.; Kondorosi, E.; Stepkowski, T.; Posfai, J.; !1Kondorosi, A. !$#journal Nucleic Acids Res. (1984) 12:9509-9524 !$#title Nucleotide sequence of Rhizobium meliloti nodulation genes. !$#cross-references MUID:85087953; PMID:6336331 !$#accession A03487 !'##molecule_type DNA !'##residues 1-426 ##label TOR !'##cross-references GB:X01649; NID:g46287; PIDN:CAA25810.1; PID:g46291 !'##experimental_source strain 41 REFERENCE A25097 !$#authors Jacobs, T.W.; Egelhoff, T.T.; Long, S.R. !$#journal J. Bacteriol. (1985) 162:469-476 !$#title Physical and genetic map of a Rhizobium meliloti nodulation !1gene region and nucleotide sequence of nodC. !$#cross-references MUID:85182456; PMID:2985535 !$#accession A25097 !'##molecule_type DNA !'##residues 1-38,'A',40-165,'M',167-426 ##label JAC !'##cross-references GB:M11268; NID:g152340; PIDN:AAA98362.1; !1PID:g152344 !'##experimental_source strain 1021 symbiotic plasmid COMMENT This is one of the proteins, coded by nodulation genes, that !1are required for R. meliloti to invade and stimulate nodule !1formation in its leguminous hosts. GENETICS !$#gene nodC CLASSIFICATION #superfamily nodulation protein nodC KEYWORDS nodulation SUMMARY #length 426 #molecular-weight 46753 #checksum 9385 SEQUENCE /// ENTRY S12793 #type complete TITLE nodulation protein nodC - Rhizobium loti ORGANISM #formal_name Rhizobium loti DATE 30-Sep-1993 #sequence_revision 27-Jan-1995 #text_change 16-Jul-1999 ACCESSIONS S12793 REFERENCE S12793 !$#authors Collins-Emerson, J.M.; Terzaghi, E.A.; Scott, D.B. !$#journal Nucleic Acids Res. (1990) 18:6690 !$#title Nucleotide sequence of Rhizobium loti nodC. !$#cross-references MUID:91067465; PMID:2251130 !$#accession S12793 !'##molecule_type DNA !'##residues 1-424 ##label COL !'##cross-references EMBL:X52958; NID:g46227; PIDN:CAA37131.1; !1PID:g46228 COMMENT This is one of the proteins, coded by nodulation genes, that !1are required for this bacterium to invade and stimulate !1nodule formation in its hosts. GENETICS !$#gene nodC CLASSIFICATION #superfamily nodulation protein nodC KEYWORDS nodulation SUMMARY #length 424 #molecular-weight 46503 #checksum 1503 SEQUENCE /// ENTRY S34305 #type complete TITLE nodulation protein nodC - Rhizobium sp. ORGANISM #formal_name Rhizobium sp. DATE 13-Jan-1995 #sequence_revision 27-Jan-1995 #text_change 16-Jul-1999 ACCESSIONS S34305 REFERENCE S34303 !$#authors Relix, B.; Perret, X.; Golinowsky, W.; Pueppke, S.G.; !1Krishnan, H.B.; Broughton, W.J. !$#submission submitted to the EMBL Data Library, June 1993 !$#description Lipo-oligosaccharide Nod-factor signals permit rhizobial !1penetration into legume roots. !$#accession S34305 !'##molecule_type DNA !'##residues 1-413 ##label REL !'##cross-references EMBL:X73362; NID:g312347; PIDN:CAA51774.1; !1PID:g312350 COMMENT This is one of the proteins, coded by nodulation genes, that !1are required for this bacterium to invade and stimulate !1nodule formation in its hosts. GENETICS !$#gene nodC CLASSIFICATION #superfamily nodulation protein nodC KEYWORDS nodulation SUMMARY #length 413 #molecular-weight 44726 #checksum 2298 SEQUENCE /// ENTRY E38180 #type complete TITLE nodulation protein nodC - Rhizobium leguminosarum bv. phaseoli ORGANISM #formal_name Rhizobium leguminosarum bv. phaseoli DATE 28-Aug-1992 #sequence_revision 27-Jan-1995 #text_change 16-Jul-1999 ACCESSIONS E38180 REFERENCE A38180 !$#authors Vazquez, M.; Davalos, A.; de las Penas, A.; Sanchez, F.; !1Quinto, C. !$#journal J. Bacteriol. (1991) 173:1250-1258 !$#title Novel organization of the common nodulation genes in !1Rhizobium leguminosarum bv. phaseoli strains. !$#cross-references MUID:91123201; PMID:1991718 !$#accession E38180 !'##molecule_type DNA !'##residues 1-428 ##label VAZ !'##cross-references GB:M58626; NID:g150473; PIDN:AAA98211.1; !1PID:g150477 COMMENT This is one of the proteins, coded by nodulation genes, that !1are required for this bacterium to invade and stimulate !1nodule formation in its hosts. GENETICS !$#gene nodC CLASSIFICATION #superfamily nodulation protein nodC KEYWORDS nodulation SUMMARY #length 428 #molecular-weight 47236 #checksum 926 SEQUENCE /// ENTRY JQ0396 #type complete TITLE nodulation protein nodC - Azorhizobium caulinodans ORGANISM #formal_name Azorhizobium caulinodans #note host Sesbania rostrata DATE 07-Sep-1990 #sequence_revision 27-Jan-1995 #text_change 16-Jul-1999 ACCESSIONS JQ0396 REFERENCE JQ0393 !$#authors Goethals, K.; Gao, M.; Tomekpe, K.; Van Montagu, M.; !1Holsters, M. !$#journal Mol. Gen. Genet. (1989) 219:289-298 !$#title Common nodABC genes in Nod locus 1 of Azorhizobium !1caulinodans: nucleotide sequence and plant-inducible !1expression. !$#cross-references MUID:90136519; PMID:2615763 !$#accession JQ0396 !'##molecule_type DNA !'##residues 1-395 ##label GOE !'##cross-references GB:L18897; NID:g1293899; PIDN:AAB51164.1; !1PID:g310294 !'##experimental_source strain ORS571 COMMENT This is one of the proteins, coded by nodulation genes, that !1are required for this bacterium to invade and stimulate !1nodule formation in its hosts. GENETICS !$#gene nodC CLASSIFICATION #superfamily nodulation protein nodC KEYWORDS nodulation SUMMARY #length 395 #molecular-weight 43583 #checksum 6153 SEQUENCE /// ENTRY ZZZRNP #type complete TITLE 3'-phosphoadenosine-5'-phosphosulfate synthetase small chain - Rhizobium meliloti plasmid pSym ALTERNATE_NAMES ATP sulfurylase small chain; nodulation protein nodP CONTAINS sulfate adenylyltransferase (EC 2.7.7.4) ORGANISM #formal_name Rhizobium meliloti DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jul-1999 ACCESSIONS S14898; S06190 REFERENCE S14898 !$#authors Cervantes, E.; Sharma, S.B.; Maillet, F.; Vasse, J.; !1Truchet, G.; Rosenberg, C. !$#journal Mol. Microbiol. (1989) 3:745-755 !$#title The Rhizobium meliloti host range nodQ gene encodes a !1protein which shares homology with translation elongation !1and initiation factors. !$#cross-references MUID:89313304; PMID:2546009 !$#accession S14898 !'##molecule_type DNA !'##residues 1-299 ##label CER !'##cross-references EMBL:X14809; NID:g46311; PIDN:CAA32913.1; !1PID:g46312 COMMENT 3'-phosphoadenosine-5'-phosphosulfate is required for !1production of the nod factors, which are sulfated !1oligosaccharides that stimulate host plant-specific !1responses to the nitrogen-fixing bacterial symbiont. GENETICS !$#gene nodP !$#genome plasmid COMPLEX associates with the nodQ protein to form a sulfate !1activation complex with adenylylsulfate kinase and sulfate !1adenylyltransferase activities FUNCTION !$#description sulfate adenylyltransferase catalyzes the reaction of !1sulfate and ATP to form adenylylsulfate and pyrophosphate CLASSIFICATION #superfamily nodulation protein nodP KEYWORDS nucleotidyltransferase SUMMARY #length 299 #molecular-weight 34763 #checksum 3384 SEQUENCE /// ENTRY SZBS0A #type complete TITLE stage 0 sporulation protein spo0A - Bacillus subtilis ALTERNATE_NAMES sporulation initiation two-component response regulator spo0A ORGANISM #formal_name Bacillus subtilis DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 16-Jun-2000 ACCESSIONS A94036; A22665; I40013; A69710; A26068; A29099; B22665 REFERENCE A94036 !$#authors Ferrari, F.A.; Trach, K.; LeCoq, D.; Spence, J.; Ferrari, !1E.; Hoch, J.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:2647-2651 !$#title Characterization of the spo0A locus and its deduced product. !$#cross-references MUID:85190553; PMID:3157992 !$#accession A94036 !'##molecule_type DNA !'##residues 1-267 ##label FER !'##cross-references GB:M10082; NID:g143584; PIDN:AAA22786.1; !1PID:g143585 REFERENCE A22665 !$#authors Kudoh, J.; Ikeuchi, T.; Kurahashi, K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:2665-2668 !$#title Nucleotide sequences of the sporulation gene spo0A and its !1mutant genes of Bacillus subtilis. !$#cross-references MUID:85190557; PMID:3921963 !$#accession A22665 !'##molecule_type DNA !'##residues 1-267 ##label KUD !'##cross-references GB:M10082; NID:g143584; PIDN:AAA22786.1; !1PID:g143585 !'##note these authors assume that the codon ATG for Met-29 is the !1initiator for translation REFERENCE A26068 !$#authors Ikeuchi, T.; Kudoh, J.; Tsunasawa, S. !$#journal Mol. Gen. Genet. (1986) 203:371-376 !$#title Amino-terminal structure of spo0A protein and sequence !1homology with spo0F and spo0B proteins. !$#cross-references MUID:86310272; PMID:3018427 !$#contents annotation !$#note initation at the codon GTG for Met-1 was demonstrated REFERENCE I40013 !$#authors Shoji, K.; Hiratsuka, S.; Kawamura, F.; Kobayashi, Y. !$#journal J. Gen. Microbiol. (1988) 134:3249-3257 !$#title New Suppressor Mutation sur0B of spo0B and spo0F Mutations !1in Bacillus subtilis. !$#cross-references MUID:90063528; PMID:3151993 !$#accession I40013 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-16 ##label RES !'##cross-references GB:M23656; NID:g143720; PIDN:AAA22842.1; !1PID:g143721 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69710 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-267 ##label KUN !'##cross-references GB:Z99116; GB:AL009126; NID:g2634723; !1PIDN:CAB14353.1; PID:g2634856 !'##experimental_source strain 168 COMMENT This protein is involved in the initiation of sporulation. GENETICS !$#gene spo0A !$#map_position 215 (degrees) !$#start_codon GTG CLASSIFICATION #superfamily stage 0 sporulation protein A; response !1regulator homology KEYWORDS phosphoprotein; sporulation FEATURE !$6-119 #domain response regulator homology #label RRH\ !$56 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 267 #molecular-weight 29691 #checksum 9619 SEQUENCE /// ENTRY SZBS0B #type complete TITLE stage 0 sporulation protein B - Bacillus subtilis ALTERNATE_NAMES Spo0B protein B; sporulation initiation phosphoprotein spo0B ORGANISM #formal_name Bacillus subtilis DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 16-Jun-2000 ACCESSIONS A22974; A32804; A21895; B69710 REFERENCE A22974 !$#authors Bouvier, J.; Stragier, P.; Bonamy, C.; Szulmajster, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:7012-7016 !$#title Nucleotide sequence of the spo0B gene of Bacillus subtilis !1and regulation of its expression. !$#cross-references MUID:85063722; PMID:6438629 !$#accession A22974 !'##molecule_type DNA !'##residues 1-192 ##label BOU !'##cross-references GB:K02664; NID:g143586; PIDN:AAB05348.1; !1PID:g143587 REFERENCE A32804 !$#authors Trach, K.; Hoch, J.A. !$#journal J. Bacteriol. (1989) 171:1362-1371 !$#title The Bacillus subtilis spo0B stage 0 sporulation operon !1encodes an essential GTP-binding protein. !$#cross-references MUID:89155435; PMID:2537815 !$#accession A32804 !'##molecule_type DNA !'##residues 1-192 ##label TRA !'##cross-references GB:M24537; NID:g341195; PIDN:AAA22504.1; !1PID:g508978 REFERENCE A94670 !$#authors Ferrari, F.A.; Trach, K.; Hoch, J.A. !$#journal J. Bacteriol. (1985) 161:556-562 !$#title Sequence analysis of the spo0B locus reveals a polycistronic !1transcription unit. !$#cross-references MUID:85104776; PMID:3918016 !$#accession A21895 !'##molecule_type DNA !'##residues 1-192 ##label FER !'##cross-references GB:X02655; GB:K02666; NID:g40178; PIDN:CAA26489.1; !1PID:g40179 !'##note the authors translated the codon GGA for residue 169 as Glu REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69710 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-192 ##label KUN !'##cross-references GB:Z99118; GB:AL009126; NID:g2635200; !1PIDN:CAB14753.1; PID:g2635258 !'##experimental_source strain 168 COMMENT This protein is involved in the initiation of sporulation. GENETICS !$#gene spo0B !$#map_position 245 (degrees) CLASSIFICATION #superfamily stage 0 sporulation protein B KEYWORDS phosphoprotein; sporulation SUMMARY #length 192 #molecular-weight 22542 #checksum 1266 SEQUENCE /// ENTRY SZBSSL #type complete TITLE transcription initiation factor sigma H - Bacillus licheniformis ALTERNATE_NAMES RNA polymerase sigma H factor; stage 0 sporulation protein spo0H ORGANISM #formal_name Bacillus licheniformis DATE 28-Feb-1986 #sequence_revision 10-Feb-1995 #text_change 16-Jul-1999 ACCESSIONS B28625; A03488 REFERENCE A28625 !$#authors Dubnau, E.; Weir, J.; Nair, G.; Carter III, L.; Moran Jr., !1C.; Smith, I. !$#journal J. Bacteriol. (1988) 170:1054-1062 !$#title Bacillus sporulation gene spo0H codes for sigma-30 !1(sigma-H). !$#cross-references MUID:88139159; PMID:3277943 !$#accession B28625 !'##molecule_type DNA !'##residues 1-223 ##label DUB !'##cross-references GB:M29694; NID:g143541; PIDN:AAA22755.1; !1PID:g143542; GB:M20395 REFERENCE A03488 !$#authors Ramakrishna, N.; Dubnau, E.; Smith, I. !$#journal Nucleic Acids Res. (1984) 12:1779-1790 !$#title The complete DNA sequence and regulatory regions of the !1Bacillus licheniformis spo0H gene. !$#cross-references MUID:84144068; PMID:6322121 !$#accession A03488 !'##molecule_type DNA !'##residues 'MDSTNLSVILERTSW',89-156,'RIRD',162-177,'P',179-180,'H', !1182-198,'NRSIMRSSVSKKLESTWSSAKSACSQCLWHIDSHFMTVICYLGK' !1##label RAM !'##cross-references GB:X00413; NID:g39578; PIDN:CAA25119.1; PID:g580783 !'##note this sequence appears to contain several frameshift errors COMMENT The gene that codes for this protein is one of those !1required for initiation of sporulation in this species; !1however, the actual process is unknown. GENETICS !$#gene spo0H CLASSIFICATION #superfamily transcription initiation factor sigma H KEYWORDS DNA binding; sigma factor; sporulation; transcription !1initiation SUMMARY #length 223 #molecular-weight 26109 #checksum 9571 SEQUENCE /// ENTRY SZBS2D #type complete TITLE stage II sporulation protein spoIID - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 16-Jun-2000 ACCESSIONS A26083; A69711 REFERENCE A26083 !$#authors Lopez-Diaz, I.; Clarke, S.; Mandelstam, J. !$#journal J. Gen. Microbiol. (1986) 132:341-354 !$#title spoIID operon of Bacillus subtilis: cloning and sequence. !$#cross-references MUID:86226160; PMID:3011962 !$#accession A26083 !'##molecule_type DNA !'##residues 1-343 ##label LOP !'##cross-references GB:M15736; NID:g143618; PIDN:AAA22793.1; !1PID:g143619 !'##note the authors translated the codon GAA for residue 53 as Gly REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69711 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-343 ##label KUN !'##cross-references GB:Z99122; GB:AL009126; NID:g2636029; !1PIDN:CAB15692.1; PID:g2636200 !'##experimental_source strain 168 COMMENT This stage II sporulation protein is required for complete !1dissolution of the asymmetric septum. GENETICS !$#gene spoIID !$#map_position 316 (degrees) CLASSIFICATION #superfamily stage II sporulation protein D KEYWORDS sporulation SUMMARY #length 343 #molecular-weight 37402 #checksum 5563 SEQUENCE /// ENTRY SZBS2N #type complete TITLE stage II sporulation protein D - Bacillus amyloliquefaciens ORGANISM #formal_name Bacillus amyloliquefaciens DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jul-1999 ACCESSIONS A27875 REFERENCE A27875 !$#authors Turner, S.M.; Mandelstam, J. !$#journal J. Gen. Microbiol. (1986) 132:3025-3035 !$#title Cloning and sequencing of a gene from Bacillus !1amyloliquefaciens that complements mutations of the !1sporulation gene spoIID in Bacillus subtilis. !$#cross-references MUID:87310371; PMID:3114424 !$#accession A27875 !'##molecule_type DNA !'##residues 1-344 ##label TUR !'##cross-references GB:M20331; NID:g143616; PIDN:AAA22792.1; !1PID:g143617 !'##note the authors translated the codon GAA for residue 79 as Leu, TTT !1for residue 94 as Pro, AGC for residue 141 as Ala, CAG for !1residue 142 as Glu, GAA for residue 146 as Gln, AAC for !1residue 154 as Ser, and TGG for residue 282 as Thr COMMENT This protein is involved in regulation of sporulation and !1the morphological development of the spore at stage II. GENETICS !$#gene spoIID CLASSIFICATION #superfamily stage II sporulation protein D KEYWORDS sporulation SUMMARY #length 344 #molecular-weight 37899 #checksum 8177 SEQUENCE /// ENTRY S66094 #type complete TITLE stage II sporulation protein SpoIIE - Bacillus subtilis ALTERNATE_NAMES asymmetric septum formation protein spoIIE; sigma-F activation serine phosphatase spoIIE ORGANISM #formal_name Bacillus subtilis DATE 28-Oct-1996 #sequence_revision 13-Mar-1997 #text_change 16-Jun-2000 ACCESSIONS S66094; I39988; B69711; D53380 REFERENCE S65967 !$#authors Ogasawara, N.; Nakai, S.; Yoshikawa, H. !$#journal DNA Res. (1994) 1:1-14 !$#title Systematic sequencing of the 180 kilobase region of the !1Bacillus subtilis chromosome containing the replication !1origin. !$#cross-references MUID:96051385; PMID:7584024 !$#accession S66094 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-827 ##label OGA !'##cross-references EMBL:D26185; NID:g467326; PIDN:BAA05299.1; !1PID:g467453 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1993 REFERENCE I39988 !$#authors Guzman, P.; Westpheling, J.; Youngman, P. !$#journal J. Bacteriol. (1988) 170:1598-1609 !$#title Characterization of the promoter region of the Bacillus !1subtilis spoIIE operon. !$#cross-references MUID:88169481; PMID:2832371 !$#accession I39988 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-16 ##label RES !'##cross-references GB:M29403; NID:g143627; PIDN:AAA22798.1; !1PID:g551729 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69711 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-827 ##label KUN !'##cross-references GB:Z99104; GB:AL009126; NID:g2632267; !1PIDN:CAB11840.1; PID:g2632331 !'##experimental_source strain 168 REFERENCE A53380 !$#authors Levin, P.A.; Losick, R. !$#journal J. Bacteriol. (1994) 176:1451-1459 !$#title Characterization of a cell division gene from Bacillus !1subtilis that is required for vegetative and sporulation !1septum formation. !$#cross-references MUID:94156852; PMID:8113187 !$#accession D53380 !'##molecule_type DNA !'##residues 1-7 ##label LEV !'##cross-references GB:L23497; NID:g469178; PIDN:AAB38381.1; !1PID:g385179 GENETICS !$#gene spoIIE CLASSIFICATION #superfamily stage II sporulation protein E KEYWORDS sporulation SUMMARY #length 827 #molecular-weight 91968 #checksum 3542 SEQUENCE /// ENTRY G69963 #type complete TITLE lipoprotein SpoIIIJ-like homolog yqjG - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS G69963 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69963 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-275 ##label KUN !'##cross-references GB:Z99116; GB:AL009126; NID:g2634723; !1PIDN:CAB14320.1; PID:g2634823 !'##experimental_source strain 168 GENETICS !$#gene yqjG CLASSIFICATION #superfamily stage III sporulation protein; stage III !1sporulation protein homology FEATURE !$43-257 #domain stage III sporulation protein homology #label !8SPOR SUMMARY #length 275 #molecular-weight 30748 #checksum 1468 SEQUENCE /// ENTRY I40437 #type complete TITLE stage III sporulation protein spoIIIJ - Bacillus subtilis ALTERNATE_NAMES hypothetical protein 1 (replication origin region) ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS I40437; S24670; S66028; G69712; S18073 REFERENCE I40435 !$#authors Ogasawara, N.; Yoshikawa, H. !$#journal Mol. Microbiol. (1992) 6:629-634 !$#title Genes and their organization in the replication origin !1region of the bacterial chromosome. !$#cross-references MUID:92204018; PMID:1552862 !$#accession I40437 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-261 ##label RES !'##cross-references EMBL:X62539; NID:g40020; PIDN:CAA44401.1; !1PID:g40023 REFERENCE S24669 !$#authors Errington, J. !$#submission submitted to the EMBL Data Library, August 1992 !$#accession S24670 !'##status preliminary !'##molecule_type DNA !'##residues 1-261 ##label ERR !'##cross-references EMBL:Z14225 REFERENCE S65967 !$#authors Ogasawara, N.; Nakai, S.; Yoshikawa, H. !$#journal DNA Res. (1994) 1:1-14 !$#title Systematic sequencing of the 180 kilobase region of the !1Bacillus subtilis chromosome containing the replication !1origin. !$#cross-references MUID:96051385; PMID:7584024 !$#accession S66028 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-261 ##label OGA !'##cross-references EMBL:D26185; NID:g467326; PIDN:BAA05234.1; !1PID:g467388 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1993 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69712 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-261 ##label KUN !'##cross-references GB:Z99124; GB:AL009126; NID:g2636442; !1PIDN:CAB16141.1; PID:g2636651 !'##experimental_source strain 168 GENETICS !$#gene spoIIIJ CLASSIFICATION #superfamily stage III sporulation protein; stage III !1sporulation protein homology FEATURE !$41-242 #domain stage III sporulation protein homology #label !8SPOR SUMMARY #length 261 #molecular-weight 29521 #checksum 7617 SEQUENCE /// ENTRY JQ1221 #type complete TITLE probable 60K inner membrane protein - Pseudomonas putida ORGANISM #formal_name Pseudomonas putida DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JQ1221; S18093 REFERENCE JQ1213 !$#authors Ogasawara, N.; Yoshikawa, H. !$#submission submitted to JIPID, October 1991 !$#description Genes and their organization in replication origin region of !1bacterial chromosome. !$#accession JQ1221 !'##molecule_type DNA !'##residues 1-560 ##label OGA !'##cross-references EMBL:X62540; NID:g45705; PIDN:CAA44417.1; !1PID:g45709 !'##experimental_source strain TN2100 CLASSIFICATION #superfamily probable 60K inner membrane protein; stage III !1sporulation protein homology KEYWORDS inner membrane; transmembrane protein FEATURE !$352-547 #domain stage III sporulation protein homology #label !8SPOR SUMMARY #length 560 #molecular-weight 61919 #checksum 4717 SEQUENCE /// ENTRY H64163 #type complete TITLE probable 60K inner membrane protein - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS H64163 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession H64163 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-541 ##label TIGR !'##cross-references GB:U32781; GB:L42023; NID:g1574028; !1PIDN:AAC22663.1; PID:g1574032; TIGR:HI1001 CLASSIFICATION #superfamily probable 60K inner membrane protein; stage III !1sporulation protein homology KEYWORDS inner membrane; transmembrane protein FEATURE !$331-527 #domain stage III sporulation protein homology #label !8SPOR SUMMARY #length 541 #molecular-weight 61239 #checksum 7331 SEQUENCE /// ENTRY B65173 #type complete TITLE probable 60K inner membrane protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS B65173 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65173 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-548 ##label BLAT !'##cross-references GB:AE000447; GB:U00096; NID:g2367266; !1PIDN:AAC76728.1; PID:g1790140; UWGP:b3705 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yidC CLASSIFICATION #superfamily probable 60K inner membrane protein; stage III !1sporulation protein homology KEYWORDS inner membrane; transmembrane protein FEATURE !$335-531 #domain stage III sporulation protein homology #label !8SPOR SUMMARY #length 548 #molecular-weight 61526 #checksum 7261 SEQUENCE /// ENTRY I40654 #type complete TITLE 60K inner membrane protein - Coxiella burnetii ORGANISM #formal_name Coxiella burnetii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS I40654 REFERENCE I40647 !$#authors Suhan, M.; Chen, S.Y.; Thompson, H.A.; Hoover, T.A.; Hill, !1A.; Williams, J.C. !$#journal J. Bacteriol. (1994) 176:5233-5243 !$#title Cloning and characterization of an autonomous replication !1sequence from Coxiella burnetii. !$#cross-references MUID:94350801; PMID:8071197 !$#accession I40654 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-487 ##label RES !'##cross-references EMBL:U10529; NID:g511451; PIDN:AAA56919.1; !1PID:g511459 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily probable 60K inner membrane protein; stage III !1sporulation protein homology KEYWORDS inner membrane; transmembrane protein SUMMARY #length 487 #molecular-weight 55165 #checksum 2495 SEQUENCE /// ENTRY B64701 #type complete TITLE probable 60K inner membrane protein - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B64701 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession B64701 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-547 ##label TOM !'##cross-references GB:AE000645; GB:AE000511; NID:g2314623; !1PIDN:AAD08491.1; PID:g2314626; TIGR:HP1450 CLASSIFICATION #superfamily probable 60K inner membrane protein; stage III !1sporulation protein homology KEYWORDS inner membrane; transmembrane protein FEATURE !$333-529 #domain stage III sporulation protein homology #label !8SPOR SUMMARY #length 547 #molecular-weight 62583 #checksum 4008 SEQUENCE /// ENTRY SNPSO #type complete TITLE ice nucleation protein [validated] - Pseudomonas syringae ALTERNATE_NAMES Snomax (TM) ORGANISM #formal_name Pseudomonas syringae DATE 31-Mar-1988 #sequence_revision 21-Jan-1997 #text_change 15-Sep-2000 ACCESSIONS A24405 REFERENCE A24405 !$#authors Green, R.L.; Warren, G.J. !$#journal Nature (1985) 317:645-648 !$#title Physical and functional repetition in a bacterial ice !1nucleation gene. !$#accession A24405 !'##molecule_type DNA !'##residues 1-1200 ##label GRE !'##cross-references EMBL:X03035; NID:g45828; PIDN:CAA26837.1; !1PID:g45829 REFERENCE A51242 !$#authors Kajava, A.V.; Lindow, S.E. !$#submission submitted to the Brookhaven Protein Data Bank, June 1993 !$#cross-references PDB:1INA !$#contents annotation; theoretical model, residues 490-535 REFERENCE A58442 !$#authors Kajava, A.V.; Lindow, S.E. !$#journal J. Mol. Biol. (1993) 232:709-717 !$#title A model of the three-dimensional structure of ice nucleation !1proteins. !$#cross-references MUID:93360260; PMID:8355267 !$#contents annotation; theoretical model COMMENT Found on the outer membrane of the bacteria, this protein !1stimulates ice formation and frost damage of fruit. It is !1manufactured from clones of Escherichia coli and used in !1snow making. COMMENT Snomax is a trademark of Snomax Technologies, Rochester, NY. CLASSIFICATION #superfamily ice nucleation protein KEYWORDS tandem repeat FEATURE !$208-1151 #region 8-residue repeats (A-G-Y-G-S-T-L-T) SUMMARY #length 1200 #molecular-weight 118587 #checksum 8220 SEQUENCE /// ENTRY USBS8I #type complete TITLE parasporal crystal protein cry4Ba1 [validated] - Bacillus thuringiensis subsp. israelensis ALTERNATE_NAMES delta-endotoxin Bt8; insecticidal protein ISRH3; mosquitocidal 130K protein ORGANISM #formal_name Bacillus thuringiensis subsp. israelensis DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 01-Dec-2000 ACCESSIONS S00398; A37587; JT0315; A28541; I39869; I40584 REFERENCE S00398 !$#authors Chungjatupornchai, W.; Hoefte, H.; Seurinck, J.; !1Angsuthanasombat, C.; Vaeck, M. !$#journal Eur. J. Biochem. (1988) 173:9-16 !$#title Common features of Bacillus thuringiensis toxins specific !1for Diptera and Lepidoptera. !$#cross-references MUID:88185334; PMID:2833395 !$#accession S00398 !'##molecule_type DNA !'##residues 1-1136 ##label CHU !'##cross-references EMBL:X07423; NID:g40353; PIDN:CAA30312.1; !1PID:g40354 REFERENCE JT0315 !$#authors Yamamoto, T.; Watkinson, I.A.; Kim, L.; Sage, M.V.; !1Stratton, R.; Akande, N.; Li, Y.; Ma, D.P.; Roe, B.A. !$#journal Gene (1988) 66:107-120 !$#title Nucleotide sequence of the gene coding for a 130-kDa !1mosquitocidal protein of Bacillus thuringiensis israelensis. !$#cross-references MUID:88329719; PMID:2901387 !$#accession A37587 !'##molecule_type DNA !'##residues 1-50,'D',52-64,'S',66-192,'PHKCTRMVY',202-204,'C',207-363, !1'LVQIYLIKFN',374,'ILI',378,'I',380,'LLSQILAP',389,'LIELQ', !1395,'WIST',400,'F',402-466,'N',468-495,'R',497-519,'G', !1520-550,'IECDHMYYKEFLEEQRLVQNYV',573-593,'N',595-686,'GIIS', !1691-720,'R',722-822,'LIVVSVRCA',833-835,'WD',838-901,'R', !1903-1014,'V',1016-1136 ##label YAM !'##cross-references GB:M20242; NID:g142737; PIDN:AAA22337.1; !1PID:g142738 !$#accession JT0315 !'##molecule_type protein !'##residues 1-13 ##label YA2 !'##note the majority of sequence differences are consistent with !1frameshift errors REFERENCE A28541 !$#authors Tungpradubkul, S.; Settasatien, C.; Panyim, S. !$#journal Nucleic Acids Res. (1988) 16:1637-1638 !$#title The complete nucleotide sequence of a 130 kDa !1mosquito-larvicidal delta-endotoxin gene of Bacillus !1thuringiensis var. israelensis. !$#cross-references MUID:88157738; PMID:2831510 !$#accession A28541 !'##molecule_type DNA !'##residues 1-204,'R',206-1136 ##label TUN !'##cross-references EMBL:X07082; NID:g40309; PIDN:CAA30114.1; !1PID:g40310 REFERENCE I39869 !$#authors Sen, K.; Honda, G.; Koyama, N.; Nishida, M.; Neki, A.; !1Sakai, H.; Himeno, M.; Komano, T. !$#journal Agric. Biol. Chem. (1988) 52:873-878 !$#title Cloning and nucleotide sequences of the two 130 kDa !1insecticidal protein genes of Bacillus thuringiensis var. !1israelensis. !$#accession I39869 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-202,'C',205-271,'L',273-324,'Y',326-1136 ##label RES !'##cross-references GB:D00247; NID:g216287; PIDN:BAA00178.1; !1PID:g216288 REFERENCE I40584 !$#authors Angsuthanasombat, C.; Chungjatupornchai, W.; Kertbundit, S.; !1Luxananil, P.; Settasatian, C.; Wilairat, P.; Panyim, S. !$#journal Mol. Gen. Genet. (1987) 208:384-389 !$#title Cloning and expression of 130-kd mosquito-larvicidal !1delta-endotoxin gene of Bacillus thuringiensis var. !1Israelensis in Escherichia coli. !$#cross-references MUID:88038331; PMID:2890080 !$#accession I40584 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-142 ##label RE2 !'##cross-references EMBL:X05692; NID:g40350; PIDN:CAA29174.1; !1PID:g408121 COMMENT This protein is toxic to many lepidopteran larvae. CLASSIFICATION #superfamily parasporal crystal protein KEYWORDS delta-endotoxin SUMMARY #length 1136 #molecular-weight 127763 #checksum 955 SEQUENCE /// ENTRY USBSXH #type complete TITLE parasporal crystal protein cry1Ac1 [validated] - Bacillus thuringiensis subsp. kurstaki (strain HD-73) ORGANISM #formal_name Bacillus thuringiensis subsp. kurstaki DATE 18-Apr-1984 #sequence_revision 31-Dec-1992 #text_change 01-Dec-2000 ACCESSIONS A23962; A03489 REFERENCE A91526 !$#authors Adang, M.J.; Staver, M.J.; Rocheleau, T.A.; Leighton, J.; !1Barker, R.F.; Thompson, D.V. !$#journal Gene (1985) 36:289-300 !$#title Characterized full-length and truncated plasmid clones of !1the crystal protein of Bacillus thuringiensis subsp. !1kurstaki HD-73 and their toxicity to Manduca sexta. !$#cross-references MUID:86083171; PMID:3000881 !$#accession A23962 !'##molecule_type DNA !'##residues 1-1178 ##label ADA !'##cross-references GB:M11068; NID:g142721; PIDN:AAA22331.1; !1PID:g142722 !'##experimental_source strain HD-73 !'##note the authors translated the codon ATT for residue 11 as Leu REFERENCE A92410 !$#authors Wong, H.C.; Schnepf, H.E.; Whiteley, H.R. !$#journal J. Biol. Chem. (1983) 258:1960-1967 !$#title Transcriptional and translational start sites for the !1Bacillus thuringiensis crystal protein gene. !$#cross-references MUID:83109004; PMID:6296116 !$#accession A03489 !'##molecule_type DNA !'##residues 1-76,'P',78-147,'L',149-247,'S',249-282,'M',284-285,'R', !1287-288,'QN',291-292,'Q',294-308,'V',310-312,'FN',315-321, !1'T',323-333 ##label WON !'##experimental_source strain HD-1 COMMENT This protein is present in crystalline form as a component !1of the spore coat. This protein is toxic to many !1lepidopteran larvae. CLASSIFICATION #superfamily parasporal crystal protein KEYWORDS delta-endotoxin SUMMARY #length 1178 #molecular-weight 133330 #checksum 8249 SEQUENCE /// ENTRY JH0261 #type complete TITLE parasporal crystal protein cry3Ca1 - Bacillus thuringiensis subsp. kurstaki (strain BTI109P) ALTERNATE_NAMES parasporal crystal protein cryIIID ORGANISM #formal_name Bacillus thuringiensis subsp. kurstaki DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Dec-2000 ACCESSIONS JH0261; S18944 REFERENCE JH0261 !$#authors Lambert, B.; Theunis, W.; Aguda, R.; Van Audenhove, K.; !1Decock, C.; Jansens, S.; Seurinck, J.; Peferoen, M. !$#journal Gene (1992) 110:131-132 !$#title Nucleotide sequence of gene cryIIID encoding a novel !1coleopteran-active crystal protein from strain BTI109P of !1Bacillus thuringiensis subsp. kurstaki. !$#cross-references MUID:92184108; PMID:1544571 !$#accession JH0261 !'##molecule_type DNA !'##residues 1-649 ##label LAM !'##cross-references EMBL:X59797; NID:g40287; PIDN:CAA42469.1; !1PID:g40288 GENETICS !$#gene cryIIID CLASSIFICATION #superfamily parasporal crystal protein SUMMARY #length 649 #molecular-weight 73026 #checksum 9764 SEQUENCE /// ENTRY S49247 #type complete TITLE parasporal crystal protein cry9Ca1 [validated] - Bacillus thuringiensis ALTERNATE_NAMES parasporal crystal protein cryIH ORGANISM #formal_name Bacillus thuringiensis DATE 01-Dec-2000 #sequence_revision 01-Dec-2000 #text_change 01-Dec-2000 ACCESSIONS A59350; S49247 REFERENCE A59350 !$#authors Lambert, B.; Buysse, L.; Decock, C.; Jansens, S.; Piens, C.; !1Saey, B.; Seurinck, J.; Van Audenhove, K.; Van Rie, J.; Van !1Vliet, A.; Peferoen, M. !$#journal Appl. Environ. Microbiol. (1996) 62:80-86 !$#title A Bacillus thuringiensis insecticidal crystal protein with a !1high activity against members of the family Noctuidae. !$#cross-references MUID:96141404; PMID:8572715 !$#accession A59350 !'##molecule_type DNA !'##residues 1-1157 ##label LAM !'##cross-references EMBL:Z37527; NID:g547554; PIDN:CAA85764.1; !1PID:g547556 !'##experimental_source serovar tolworthi COMMENT This parasporal crystal protein, active against corn borer !1and other insects, may be allergenic. CLASSIFICATION #superfamily parasporal crystal protein KEYWORDS delta-endotoxin SUMMARY #length 1157 #molecular-weight 129775 #checksum 6758 SEQUENCE /// ENTRY F32354 #type complete TITLE transaldolase (pentose phosphate) homolog ywjH - Bacillus subtilis ALTERNATE_NAMES 23K phosphoprotein orfU (tsr 3' region); hypothetical protein U ORGANISM #formal_name Bacillus subtilis DATE 03-Mar-1994 #sequence_revision 03-Mar-1994 #text_change 16-Jun-2000 ACCESSIONS F32354; S55427; F41835; F70060 REFERENCE A91883 !$#authors Trach, K.; Chapman, J.W.; Piggot, P.; LeCoq, D.; Hoch, J.A. !$#journal J. Bacteriol. (1988) 170:4194-4208 !$#title Complete sequence and transcriptional analysis of the spo0F !1region of the Bacillus subtilis chromosome. !$#cross-references MUID:88314920; PMID:2457578 !$#accession F32354 !'##molecule_type DNA !'##residues 1-186 ##label TRA !'##cross-references GB:M22039 REFERENCE S55414 !$#authors Glaser, P.; Danchin, A. !$#submission submitted to the EMBL Data Library, May 1995 !$#description Cloning and sequencing of the Bacillus subtilis chromosomal !1region from 320 degrees to 321 degrees. !$#accession S55427 !'##molecule_type DNA !'##residues 1-186 ##label GLA !'##cross-references EMBL:Z49782; NID:g853752; PIDN:CAA89874.1; !1PID:g853766 REFERENCE A41835 !$#authors Mitchell, C.; Morris, P.W.; Vary, J.C. !$#journal J. Bacteriol. (1992) 174:2474-2477 !$#title Identification of proteins phosphorylated by ATP during !1sporulation of Bacillus subtilis. !$#cross-references MUID:92210489; PMID:1556067 !$#accession F41835 !'##molecule_type protein !'##residues 1-17,'X',19-24 ##label MIT REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F70060 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-186 ##label KUN !'##cross-references GB:Z99122; GB:Z99123; GB:AL009126; NID:g2636240; !1PIDN:CAB15739.1; PID:g2636248; NID:g2636029; PID:g2636236 !'##experimental_source strain 168 COMMENT This protein is encoded by the fourth open reading frame 3' !1to the stage 0 sporulation gene spo0F, although spo0F !1appears to be monocistronic. The orfU gene product is not !1required for sporulation or growth, and its function is not !1known. COMMENT This protein is not phosphorylated during exponential growth !1but is phosphorylated during early stationary phase. GENETICS !$#gene ywjH CLASSIFICATION #superfamily Bacillus subtilis 23K phosphoprotein orfU KEYWORDS phosphoprotein SUMMARY #length 186 #molecular-weight 19975 #checksum 3738 SEQUENCE /// ENTRY DZYZSX #type complete TITLE development-specific protein S - Myxococcus xanthus ALTERNATE_NAMES spore coat protein S ORGANISM #formal_name Myxococcus xanthus DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 16-Jul-1999 ACCESSIONS A03490; A22273 REFERENCE A93976 !$#authors Inouye, S.; Franceschini, T.; Inouye, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:6829-6833 !$#title Structural similarities between the development-specific !1protein S from a gram-negative bacterium, Myxococcus !1xanthus, and calmodulin. !$#cross-references MUID:84070723; PMID:6316328 !$#accession A03490 !'##molecule_type DNA !'##residues 1-173 ##label INO !'##cross-references GB:J01745; GB:J01746; NID:g150125; PIDN:AAA25407.1; !1PID:g150127 REFERENCE A22273 !$#authors Wistow, G.; Summers, L.; Blundell, T. !$#journal Nature (1985) 315:771-773 !$#cross-references MUID:85240568; PMID:3925350 !$#accession A22273 !'##status preliminary !'##molecule_type protein !'##residues 1-173 ##label WIS COMMENT This protein is induced in large amounts during fruiting !1body formation, assembles on the surface of myxospores in !1the presence of calcium ion. CLASSIFICATION #superfamily development-specific protein S SUMMARY #length 173 #molecular-weight 18793 #checksum 2570 SEQUENCE /// ENTRY DZYZ1X #type complete TITLE gene 1 protein - Myxococcus xanthus ORGANISM #formal_name Myxococcus xanthus DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 16-Jul-1999 ACCESSIONS A03491 REFERENCE A93976 !$#authors Inouye, S.; Franceschini, T.; Inouye, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:6829-6833 !$#title Structural similarities between the development-specific !1protein S from a gram-negative bacterium, Myxococcus !1xanthus, and calmodulin. !$#cross-references MUID:84070723; PMID:6316328 !$#accession A03491 !'##molecule_type DNA !'##residues 1-175 ##label INO !'##cross-references GB:J01745; GB:J01746; NID:g150125; PIDN:AAA25406.1; !1PID:g150126 COMMENT This sequence is homologous with that of protein S; it is !1not certain whether the gene is expressed. CLASSIFICATION #superfamily development-specific protein S SUMMARY #length 175 #molecular-weight 19235 #checksum 1951 SEQUENCE /// ENTRY HMYZMX #type complete TITLE myxobacterial hemagglutinin - Myxococcus xanthus ALTERNATE_NAMES lectin ORGANISM #formal_name Myxococcus xanthus DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 16-Jul-1999 ACCESSIONS A23542 REFERENCE A23542 !$#authors Romeo, J.M.; Esmon, B.; Zusman, D.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:6332-6336 !$#title Nucleotide sequence of the myxobacterial hemagglutinin gene !1contains four homologous domains. !$#cross-references MUID:86313575; PMID:3092212 !$#accession A23542 !'##molecule_type DNA !'##residues 1-267 ##label ROM !'##cross-references GB:M13831; NID:g150095; PIDN:AAA25399.1; !1PID:g150096 COMMENT M. xanthus is a rod-shaped bacterium with a complex life !1cycle that includes formation of fruiting bodies. This !1protein is a lectin that is induced during the aggregation !1phase of fruiting body formation. GENETICS !$#gene mbhA CLASSIFICATION #superfamily myxobacterial hemagglutinin KEYWORDS duplication; hemagglutinin; lectin FEATURE !$1-66,67-133, !$134-200,201-267 #region duplication SUMMARY #length 267 #molecular-weight 27916 #checksum 7587 SEQUENCE /// ENTRY HMECA1 #type complete TITLE hemagglutinin AFA-I precursor - Escherichia coli ALTERNATE_NAMES afimbrial adhesin AFA-I precursor ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 17-Oct-1997 #text_change 16-Jul-1999 ACCESSIONS S42624; A24586 REFERENCE S42623 !$#authors le Bouguenec, C.; Garcia, M.I.; Ouin, V.; Desperrier, J.M.; !1Gounon, P.; Labigne, A. !$#journal Infect. Immun. (1993) 61:5106-5114 !$#title Characterization of plasmid-borne afa-3 gene clusters !1encoding afimbrial adhesins expressed by Escherichia coli !1strains associated with intestinal or urinary tract !1infections. !$#cross-references MUID:94041631; PMID:7901162 !$#accession S42624 !'##status preliminary !'##molecule_type DNA !'##residues 1-161 ##label LEB !'##cross-references EMBL:X69197; NID:g433882; PIDN:CAA48941.1; !1PID:g433883 REFERENCE A24586 !$#authors Labigne-Roussel, A.; Schmidt, M.A.; Walz, W.; Falkow, S. !$#journal J. Bacteriol. (1985) 162:1285-1292 !$#title Genetic organization of the afimbrial adhesin operon and !1nucleotide sequence from a uropathogenic Escherichia coli !1gene encoding an afimbrial adhesin. !$#cross-references MUID:85207453; PMID:2860096 !$#accession A24586 !'##molecule_type DNA !'##residues 1-128,'TGT',132,'R',159,'CSSYEMTNSTYQPASTP' ##label LAB !'##cross-references GB:M12868; NID:g146387; PIDN:AAA23981.1; !1PID:g146388 !'##experimental_source strain KS52 COMMENT The capacity of uropathogenic E. coli to adhere to !1uroepithelial cells correlates with the ability of bacteria !1to agglutinate human erythrocytes in the presence of !1D-mannose and is referred to as mannose-resistant !1hemagglutination (MRHA). KS52 is one of the MRHA strains !1that are responsible for acute urinary tract infection and !1that have hemagglutinin that recognizes specific receptors !1on the uroepithelial cells. GENETICS !$#gene afaE CLASSIFICATION #superfamily hemagglutinin AFA-I KEYWORDS hemagglutinin; mannose-resistant hemagglutination FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-161 #product hemagglutinin AFA-I #status predicted #label !8MAT SUMMARY #length 161 #molecular-weight 17184 #checksum 146 SEQUENCE /// ENTRY S21010 #type complete TITLE filamentous hemagglutinin B precursor - Bordetella pertussis ORGANISM #formal_name Bordetella pertussis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S21010; S18225; S10236; S62090; A41475; S12465 REFERENCE S12465 !$#authors Relman, D.A. !$#submission submitted to the EMBL Data Library, March 1990 !$#accession S21010 !'##molecule_type DNA !'##residues 1-3591 ##label REL !'##cross-references EMBL:X52156; NID:g39739; PID:g39740 REFERENCE S18223 !$#authors Scarlato, V.; Prugnola, A.; Arico, B.; Rappuoli, R. !$#journal Mol. Microbiol. (1991) 5:2493-2498 !$#title The bvg-dependent promoters show similar behaviour in !1different Bordetella species and share sequence homologies. !$#cross-references MUID:92167814; PMID:1791761 !$#accession S18225 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-35 ##label SCA REFERENCE S10236 !$#authors Domenighini, M.; Relman, D.; Capiau, C.; Falkow, S.; !1Prugnola, A.; Scarlato, V.; Rappuoli, R. !$#journal Mol. Microbiol. (1990) 4:787-800 !$#title Genetic characterization of Bordetella pertussis filamentous !1haemagglutinin: a protein processed from an unusually large !1precursor. !$#cross-references MUID:90355839; PMID:2388559 !$#accession S10236 !'##molecule_type DNA !'##residues 1-3329,'AQPLPPRPVA',3340-3591 ##label DOM !'##cross-references GB:M60351; EMBL:J04531; NID:g144047; !1PIDN:AAA22974.1; PID:g144048 !$#accession S62090 !'##molecule_type protein !'##residues 1074-1092 ##label DOE REFERENCE A41475 !$#authors Delisse-Gathoye, A.M.; Locht, C.; Jacob, F.; !1Raaschou-Nielsen, M.; Heron, I.; Ruelle, J.L.; De Wilde, M.; !1Cabezon, T. !$#journal Infect. Immun. (1990) 58:2895-2905 !$#title Cloning, partial sequence, expression, and antigenic !1analysis of the filamentous hemagglutinin gene of Bordetella !1pertussis. !$#cross-references MUID:90354052; PMID:1696934 !$#accession A41475 !'##molecule_type DNA !'##residues 1-279,'R',281-283,'A',285-515,'V',517-613,'G',615-1087 !1##label DEL !'##cross-references GB:X53405; NID:g39737; PIDN:CAA37481.1; PID:g39738 GENETICS !$#gene fhaB; fha CLASSIFICATION #superfamily Bordetella filamentous hemagglutinin B KEYWORDS hemagglutinin SUMMARY #length 3591 #molecular-weight 367110 #checksum 9711 SEQUENCE /// ENTRY PRSAK #type complete TITLE staphylokinase - phage S phi-C ORGANISM #formal_name phage S phi-C #note host Staphylococcus aureus DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 28-May-1999 ACCESSIONS A00995 REFERENCE A00995 !$#authors Sako, T.; Tsuchida, N. !$#journal Nucleic Acids Res. (1983) 11:7679-7693 !$#title Nucleotide sequence of the staphylokinase gene from !1Staphylococcus aureus. !$#cross-references MUID:84069795; PMID:6359061 !$#accession A00995 !'##molecule_type DNA !'##residues 1-163 ##label SAK !'##cross-references GB:X00127; NID:g47425; PIDN:CAA24957.1; PID:g758303 COMMENT Although it has no intrinsic proteolytic activity, this !1secreted protein is a plasminogen activator. It forms a 1:1 !1molar complex with plasminogen; consequent alteration of the !1tertiary structure of plasminogen is thought to expose the !1plasmin active site. COMMENT The designation of staphylokinase as synonomous with !1Staphylococcal aureus neutral proteinase (EC 3.4.24.4) is !1apparently erroneous. GENETICS !$#gene sak CLASSIFICATION #superfamily phage S phi-C staphylokinase KEYWORDS plasminogen activator SUMMARY #length 163 #molecular-weight 18490 #checksum 7631 SEQUENCE /// ENTRY HMECBM #type complete TITLE M-agglutinin precursor - Escherichia coli ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 16-Jul-1999 ACCESSIONS A27165 REFERENCE A27165 !$#authors Rhen, M.; Vaisanen-Rhen, V.; Saraste, M.; Korhonen, T.K. !$#journal Gene (1986) 49:351-360 !$#title Organization of genes expressing the blood-group-M-specific !1hemagglutinin of Escherichia coli: identification and !1nucleotide sequence of the M-agglutinin subunit gene. !$#cross-references MUID:87192025; PMID:2883087 !$#accession A27165 !'##molecule_type DNA !'##residues 1-170 ##label RHE !'##cross-references GB:M15677; NID:g145437; PIDN:AAA23523.1; !1PID:g145438 COMMENT This protein is a nonfimbrial hemagglutinin that is specific !1for blood group M. GENETICS !$#gene bmaE CLASSIFICATION #superfamily M-agglutinin KEYWORDS hemagglutinin FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-170 #product M-agglutinin #status predicted #label MAT SUMMARY #length 170 #molecular-weight 17952 #checksum 4418 SEQUENCE /// ENTRY HMSO1F #type complete TITLE aggregation protein asa1 precursor - Enterococcus faecalis plasmid pAD1 ALTERNATE_NAMES aggregation substance ORGANISM #formal_name Enterococcus faecalis DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Jul-1999 ACCESSIONS S10223; A37537 REFERENCE S10222 !$#authors Galli, D.; Lottspeich, F.; Wirth, R. !$#journal Mol. Microbiol. (1990) 4:895-904 !$#title Sequence analysis of Enterococcus faecalis aggregation !1substance encoded by the sex pheromone plasmid pAD1. !$#cross-references MUID:91014689; PMID:2120541 !$#accession S10223 !'##molecule_type DNA !'##residues 1-1296 ##label GAL1 !'##cross-references EMBL:X17214; NID:g47047; PIDN:CAA35083.1; !1PID:g47049 !$#accession A37537 !'##molecule_type protein !'##residues 44-51 ##label GAL2 GENETICS !$#gene asa1 !$#genome plasmid CLASSIFICATION #superfamily aggregation protein asa1 KEYWORDS transmembrane protein FEATURE !$1-43 #domain signal sequence #status predicted #label SIG\ !$44-1296 #product aggregation protein asa1 #status !8experimental #label MAT\ !$1270-1289 #domain transmembrane #status predicted #label TMM SUMMARY #length 1296 #molecular-weight 142284 #checksum 7546 SEQUENCE /// ENTRY XMECAD #type complete TITLE dedA protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 01-Mar-2002 ACCESSIONS B29803; D40637; I69367; C65004 REFERENCE A29803 !$#authors Nonet, M.L.; Marvel, C.C.; Tolan, D.R. !$#journal J. Biol. Chem. (1987) 262:12209-12217 !$#title The hisT-purF region of the Escherichia coli K-12 !1chromosome. Identification of additional genes of the hisT !1and purF operons. !$#cross-references MUID:87308226; PMID:3040734 !$#accession B29803 !'##molecule_type DNA !'##residues 1-219 ##label NON !'##cross-references GB:M68934; GB:J02800; NID:g146359; PIDN:AAA23964.1; !1PID:g146363 REFERENCE A40637 !$#authors Li, S.J.; Cronan Jr., J.E. !$#journal J. Bacteriol. (1993) 175:332-340 !$#title Growth rate regulation of Escherichia coli acetyl coenzyme A !1carboxylase, which catalyzes the first committed step of !1lipid biosynthesis. !$#cross-references MUID:93123150; PMID:7678242 !$#accession D40637 !'##status preliminary !'##molecule_type DNA !'##residues 204-219 ##label LI1 !'##cross-references GB:S53037; NID:g263402; PIDN:AAB24893.1; !1PID:g263403 !'##note sequence extracted from NCBI backbone (NCBIN:122320, !1NCBIP:122321) REFERENCE I54872 !$#authors Arps, P.J.; Winkler, M.E. !$#journal J. Bacteriol. (1987) 169:1061-1070 !$#title Structural analysis of the Escherichia coli K-12 hisT operon !1by using a kanamycin resistance cassette. !$#cross-references MUID:87137258; PMID:3029016 !$#accession I69367 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-9 ##label RES !'##cross-references GB:M15543; NID:g147128; PIDN:AAA24314.1; !1PID:g147135 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65004 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-219 ##label BLAT !'##cross-references GB:AE000320; GB:U00096; NID:g1788647; !1PIDN:AAC75377.1; PID:g1788656; UWGP:b2317 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene dedA !$#map_position 50 min !$#note this protein is encoded by a hisT operon gene downstream of !1the hisT gene CLASSIFICATION #superfamily dedA protein SUMMARY #length 219 #molecular-weight 24510 #checksum 6775 SEQUENCE /// ENTRY BVECZE #type complete TITLE cell growth regulatory protein mazE - Escherichia coli (strain K-12) ALTERNATE_NAMES pemI-like protein 1 ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 01-Mar-2002 ACCESSIONS B31996; A49339; C65060 REFERENCE A31996 !$#authors Metzger, S.; Dror, I.B.; Aizenman, E.; Schreiber, G.; Toone, !1M.; Friesen, J.D.; Cashel, M.; Glaser, G. !$#journal J. Biol. Chem. (1988) 263:15699-15704 !$#title The nucleotide sequence and characterization of the relA !1gene of Escherichia coli. !$#cross-references MUID:89008481; PMID:2844820 !$#accession B31996 !'##molecule_type DNA !'##residues 1-82 ##label MET !'##cross-references GB:J04039; NID:g416195; PIDN:AAA03238.1; !1PID:g416196 REFERENCE A49339 !$#authors Masuda, Y.; Miyakawa, K.; Nishimura, Y.; Ohtsubo, E. !$#journal J. Bacteriol. (1993) 175:6850-6856 !$#title chpA and chpB, Escherichia coli chromosomal homologs of the !1pem locus responsible for stable maintenance of plasmid !1R100. !$#cross-references MUID:94042847; PMID:8226627 !$#accession A49339 !'##molecule_type DNA !'##residues 1-82 ##label MAS !'##cross-references GB:D16450; NID:g452512; PIDN:BAA41177.1; !1PID:g506193 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65060 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-82 ##label BLAT !'##cross-references GB:AE000362; GB:U00096; NID:g1789143; !1PIDN:AAC75825.1; PID:g1789146; UWGP:b2783 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene chpR; chpA1; mazE !$#map_position 60 min CLASSIFICATION #superfamily mazE protein KEYWORDS DNA binding SUMMARY #length 82 #molecular-weight 9356 #checksum 9386 SEQUENCE /// ENTRY QQECR8 #type complete TITLE cell growth regulatory protein ChpBI - Escherichia coli (strain K-12) ALTERNATE_NAMES PemI-like protein 2 ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 01-Mar-1996 #text_change 01-Mar-2002 ACCESSIONS S56450; A24412; C49339; C65234 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56450 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-85 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97121.1; !1PID:g537066 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A92595 !$#authors Weiss, D.L.; Johnson, D.I.; Weith, H.L.; Somerville, R.L. !$#journal J. Biol. Chem. (1986) 261:9966-9971 !$#title Structural analysis of the ileR locus of Escherichia coli !1K12. !$#cross-references MUID:86278038; PMID:3525538 !$#accession A24412 !'##molecule_type DNA !'##residues 3-85 ##label WEI !'##cross-references GB:M14018 REFERENCE A49339 !$#authors Masuda, Y.; Miyakawa, K.; Nishimura, Y.; Ohtsubo, E. !$#journal J. Bacteriol. (1993) 175:6850-6856 !$#title chpA and chpB, Escherichia coli chromosomal homologs of the !1pem locus responsible for stable maintenance of plasmid !1R100. !$#cross-references MUID:94042847; PMID:8226627 !$#accession C49339 !'##molecule_type DNA !'##residues 3-85 ##label MAS !'##cross-references GB:D16451; NID:g452513; PIDN:BAA41179.1; !1PID:g506195 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65234 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-85 ##label BLAT !'##cross-references GB:AE000494; GB:U00096; NID:g1790670; !1PIDN:AAC77181.1; PID:g1790671; UWGP:b4224 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene chpS !$#map_position 99.5 min !$#start_codon GTG CLASSIFICATION #superfamily mazE protein KEYWORDS DNA binding SUMMARY #length 85 #molecular-weight 9531 #checksum 9387 SEQUENCE /// ENTRY XMECDD #type complete TITLE dedD protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1988 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS H65003; E29803 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65003 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-211 ##label BLAT !'##cross-references GB:AE000320; GB:U00096; NID:g1788647; !1PIDN:AAC75374.1; PID:g1788653; UWGP:b2314 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A29803 !$#authors Nonet, M.L.; Marvel, C.C.; Tolan, D.R. !$#journal J. Biol. Chem. (1987) 262:12209-12217 !$#title The hisT-purF region of the Escherichia coli K-12 !1chromosome. Identification of additional genes of the hisT !1and purF operons. !$#cross-references MUID:87308226; PMID:3040734 !$#accession E29803 !'##molecule_type DNA !'##residues 'V',2-211 ##label NON COMMENT This protein is encoded by a gene located between the hisT !1and purF operons; its function is not yet known. GENETICS !$#gene dedD !$#map_position 50 min CLASSIFICATION #superfamily dedD protein SUMMARY #length 211 #molecular-weight 21894 #checksum 1811 SEQUENCE /// ENTRY XMECED #type complete TITLE colicin V production protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 01-Mar-2002 ACCESSIONS A29803; A92491; A44760; G65003; A23892; F29803 REFERENCE A29803 !$#authors Nonet, M.L.; Marvel, C.C.; Tolan, D.R. !$#journal J. Biol. Chem. (1987) 262:12209-12217 !$#title The hisT-purF region of the Escherichia coli K-12 !1chromosome. Identification of additional genes of the hisT !1and purF operons. !$#cross-references MUID:87308226; PMID:3040734 !$#accession A29803 !'##molecule_type DNA !'##residues 1-162 ##label NON !'##cross-references GB:M68934; GB:J02800; NID:g146359; PIDN:AAA23968.1; !1PID:g146367 REFERENCE A92491 !$#authors Makaroff, C.A.; Zalkin, H. !$#journal J. Biol. Chem. (1985) 260:10378-10387 !$#title Regulation of Escherichia coli purF: analysis of the control !1region of a pur regulon gene. !$#cross-references MUID:85261467; PMID:2991286 !$#accession A92491 !'##molecule_type mRNA !'##residues 1-162 ##label MAK !'##cross-references GB:J01666; GB:M10318; NID:g147414; PIDN:AAA24451.1; !1PID:g147415 REFERENCE A44760 !$#authors Fath, M.J.; Mahanty, H.K.; Kolter, R. !$#journal J. Bacteriol. (1989) 171:3158-3161 !$#title Characterization of a purF operon mutation which affects !1colicin V production. !$#cross-references MUID:89255077; PMID:2542219 !$#accession A44760 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 94-110 ##label FAT REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65003 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-162 ##label BLAT !'##cross-references GB:AE000320; GB:U00096; NID:g1788647; !1PIDN:AAC75373.1; PID:g1788652; UWGP:b2313 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene cvpA; dedE !$#map_position 50 min !$#note this protein is encoded by a purF operon gene immediately !1upstream of the purF gene CLASSIFICATION #superfamily dedE protein KEYWORDS transmembrane protein SUMMARY #length 162 #molecular-weight 17907 #checksum 3468 SEQUENCE /// ENTRY XMECFD #type complete TITLE 3-octaprenyl-4-hydroxybenzoate carboxy-lyase (EC 4.1.1.-) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1988 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS E65003; H29803 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65003 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-189 ##label BLAT !'##cross-references GB:AE000320; GB:U00096; NID:g1788647; !1PIDN:AAC75371.1; PID:g1788650; UWGP:b2311 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A29803 !$#authors Nonet, M.L.; Marvel, C.C.; Tolan, D.R. !$#journal J. Biol. Chem. (1987) 262:12209-12217 !$#title The hisT-purF region of the Escherichia coli K-12 !1chromosome. Identification of additional genes of the hisT !1and purF operons. !$#cross-references MUID:87308226; PMID:3040734 !$#accession H29803 !'##molecule_type DNA !'##residues 1-61,'S',63-138,'GRNRCGDYAS',149-189 ##label NON !'##cross-references GB:M68935; GB:J02800; NID:g146360; PIDN:AAA23970.1; !1PID:g146369 COMMENT This protein is encoded by a purF operon gene immediately !1downstream of the purF gene; its function is not yet known. GENETICS !$#gene dedF; ubiX !$#map_position 50 min CLASSIFICATION #superfamily dedF protein KEYWORDS carbon-carbon lyase; carboxy-lyase SUMMARY #length 189 #molecular-weight 20695 #checksum 4585 SEQUENCE /// ENTRY C28944 #type complete TITLE flagellin B1 precursor [validated] - Halobacterium salinarum ORGANISM #formal_name Halobacterium salinarum DATE 30-Jun-1989 #sequence_revision 04-Oct-1996 #text_change 21-Jul-2000 ACCESSIONS C28944 REFERENCE A28944 !$#authors Gerl, L.; Sumper, M. !$#journal J. Biol. Chem. (1988) 263:13246-13251 !$#title Halobacterial flagellins are encoded by a multigene family. !1Characterization of five flagellin genes. !$#cross-references MUID:88330827; PMID:3417656 !$#accession C28944 !'##molecule_type DNA !'##residues 1-193 ##label GER !'##cross-references GB:M19884; NID:g148765; PIDN:AAA72643.1; !1PID:g148766; GB:J03942 !'##note parts of this sequence were confirmed by protein sequencing !'##note the source is designated as Halobacterium halobium GENETICS !$#gene flgB1 FUNCTION !$#description structural component of the flagellar filament [validated, !1MUID:88330827] CLASSIFICATION #superfamily archaeal flagellin KEYWORDS flagellum; glycoprotein FEATURE !$1-12 #domain signal sequence #status predicted #label SIG\ !$13-193 #product flagellin B1 #status predicted #label MAT\ !$80,123 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$93 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 193 #molecular-weight 20455 #checksum 1632 SEQUENCE /// ENTRY E28944 #type complete TITLE flagellin B3 precursor [validated] - Halobacterium salinarum ORGANISM #formal_name Halobacterium salinarum DATE 30-Jun-1989 #sequence_revision 04-Oct-1996 #text_change 21-Jul-2000 ACCESSIONS E28944 REFERENCE A28944 !$#authors Gerl, L.; Sumper, M. !$#journal J. Biol. Chem. (1988) 263:13246-13251 !$#title Halobacterial flagellins are encoded by a multigene family. !1Characterization of five flagellin genes. !$#cross-references MUID:88330827; PMID:3417656 !$#accession E28944 !'##molecule_type DNA !'##residues 1-193 ##label GER !'##cross-references GB:M19884; NID:g148765; PIDN:AAA72645.1; !1PID:g148768; GB:J03942 !'##note parts of this sequence were confirmed by protein sequencing !'##note the source is designated as Halobacterium halobium GENETICS !$#gene flgB3 FUNCTION !$#description structural component of the flagellar filament [validated, !1MUID:88330827] CLASSIFICATION #superfamily archaeal flagellin KEYWORDS flagellum; glycoprotein FEATURE !$1-12 #domain signal sequence #status predicted #label SIG\ !$13-193 #product flagellin B3 #status predicted #label MAT\ !$80,123 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$93 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 193 #molecular-weight 20521 #checksum 2048 SEQUENCE /// ENTRY B28944 #type complete TITLE flagellin A2 precursor [validated] - Halobacterium salinarum ALTERNATE_NAMES flagellin I ORGANISM #formal_name Halobacterium salinarum DATE 30-Jun-1989 #sequence_revision 04-Oct-1996 #text_change 21-Jul-2000 ACCESSIONS B28944 REFERENCE A28944 !$#authors Gerl, L.; Sumper, M. !$#journal J. Biol. Chem. (1988) 263:13246-13251 !$#title Halobacterial flagellins are encoded by a multigene family. !1Characterization of five flagellin genes. !$#cross-references MUID:88330827; PMID:3417656 !$#accession B28944 !'##molecule_type DNA !'##residues 1-194 ##label GER !'##cross-references GB:M22568; GB:M19883; GB:J03942; NID:g148762; !1PIDN:AAA72642.1; PID:g148764 !'##note parts of this sequence were confirmed by protein sequencing !'##note the source is designated as Halobacterium halobium GENETICS !$#gene flgA2 FUNCTION !$#description structural component of the flagellar filament [validated, !1MUID:88330827] CLASSIFICATION #superfamily archaeal flagellin KEYWORDS blocked amino end; flagellum; glycoprotein FEATURE !$1-12 #domain signal sequence #status predicted #label SIG\ !$13-194 #product flagellin A2 #status predicted #label MAT\ !$80,93,126 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 194 #molecular-weight 20605 #checksum 8842 SEQUENCE /// ENTRY A28944 #type complete TITLE flagellin A1 precursor [validated] - Halobacterium salinarum ALTERNATE_NAMES flagellin II ORGANISM #formal_name Halobacterium salinarum DATE 30-Jun-1989 #sequence_revision 04-Oct-1996 #text_change 21-Jul-2000 ACCESSIONS A28944 REFERENCE A28944 !$#authors Gerl, L.; Sumper, M. !$#journal J. Biol. Chem. (1988) 263:13246-13251 !$#title Halobacterial flagellins are encoded by a multigene family. !1Characterization of five flagellin genes. !$#cross-references MUID:88330827; PMID:3417656 !$#accession A28944 !'##molecule_type DNA !'##residues 1-196 ##label GER !'##cross-references GB:M21571; GB:J03638 !'##note parts of this sequence were confirmed by protein sequencing !'##note the source is designated as Halobacterium halobium GENETICS !$#gene flgA1 FUNCTION !$#description structural component of the flagellar filament [validated, !1MUID:88330827] CLASSIFICATION #superfamily archaeal flagellin KEYWORDS flagellum; glycoprotein FEATURE !$1-12 #domain signal sequence #status predicted #label SIG\ !$13-196 #product flagellin A1 #status predicted #label MAT\ !$84,97,125 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 196 #molecular-weight 20623 #checksum 1257 SEQUENCE /// ENTRY D28944 #type complete TITLE flagellin B2 precursor [validated] - Halobacterium salinarum ORGANISM #formal_name Halobacterium salinarum DATE 30-Jun-1989 #sequence_revision 04-Oct-1996 #text_change 21-Jul-2000 ACCESSIONS D28944 REFERENCE A28944 !$#authors Gerl, L.; Sumper, M. !$#journal J. Biol. Chem. (1988) 263:13246-13251 !$#title Halobacterial flagellins are encoded by a multigene family. !1Characterization of five flagellin genes. !$#cross-references MUID:88330827; PMID:3417656 !$#accession D28944 !'##molecule_type DNA !'##residues 1-196 ##label GER !'##cross-references GB:M19884; NID:g148765; PIDN:AAA72644.1; !1PID:g148767; GB:J03942 !'##note parts of this sequence were confirmed by protein sequencing !'##note the source is designated as Halobacterium halobium GENETICS !$#gene flgB2 FUNCTION !$#description structural component of the flagellar filament [validated, !1MUID:88330827] CLASSIFICATION #superfamily archaeal flagellin KEYWORDS flagellum; glycoprotein FEATURE !$1-12 #domain signal sequence #status predicted #label SIG\ !$13-196 #product flagellin B2 #status predicted #label MAT\ !$84,97,125 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 196 #molecular-weight 20682 #checksum 1728 SEQUENCE /// ENTRY C64411 #type complete TITLE flagellin B1 precursor - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 13-Sep-1996 #sequence_revision 04-Oct-1996 #text_change 21-Jul-2000 ACCESSIONS C64411 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession C64411 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-217 ##label BUL !'##cross-references GB:U67533; GB:L77117; NID:g2826346; !1PIDN:AAB98894.1; PID:g1591569; TIGR:MJ0891 GENETICS !$#gene flaB1 !$#map_position FOR821708-822361 CLASSIFICATION #superfamily archaeal flagellin KEYWORDS flagellum FEATURE !$1-12 #domain signal sequence #status predicted #label SIG\ !$13-217 #product flagellin B1 #status predicted #label MAT SUMMARY #length 217 #molecular-weight 22700 #checksum 8701 SEQUENCE /// ENTRY D64411 #type complete TITLE flagellin B2 precursor - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 13-Sep-1996 #sequence_revision 04-Oct-1996 #text_change 21-Jul-2000 ACCESSIONS D64411 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession D64411 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-217 ##label BUL !'##cross-references GB:U67533; GB:L77117; NID:g2826346; !1PIDN:AAB98895.1; PID:g1591570; TIGR:MJ0892 GENETICS !$#gene flaB2 !$#map_position FOR822444-823097 CLASSIFICATION #superfamily archaeal flagellin KEYWORDS flagellum FEATURE !$1-12 #domain signal sequence #status predicted #label SIG\ !$13-217 #product flagellin B2 #status predicted #label MAT SUMMARY #length 217 #molecular-weight 22577 #checksum 8740 SEQUENCE /// ENTRY B41316 #type complete TITLE flagellin B1 precursor - Methanococcus voltae ALTERNATE_NAMES 31K flagellin ORGANISM #formal_name Methanococcus voltae DATE 21-Apr-1992 #sequence_revision 04-Oct-1996 #text_change 16-Jul-1999 ACCESSIONS B41316; A34624 REFERENCE A41316 !$#authors Kalmokoff, M.L.; Jarrell, K.F. !$#journal J. Bacteriol. (1991) 173:7113-7125 !$#title Cloning and sequencing of a multigene family encoding the !1flagellins of Methanococcus voltae. !$#cross-references MUID:92041608; PMID:1718944 !$#accession B41316 !'##molecule_type DNA !'##residues 1-218 ##label KAL !'##cross-references GB:M72148; NID:g150060; PIDN:AAA73074.1; !1PID:g150062 REFERENCE A34624 !$#authors Kalmokoff, M.L.; Karnauchow, T.M.; Jarrell, K.F. !$#journal Biochem. Biophys. Res. Commun. (1990) 167:154-160 !$#title Conserved N-terminal sequences in the flagellins of !1archaebacteria. !$#cross-references MUID:90179742; PMID:2106880 !$#accession A34624 !'##molecule_type protein !'##residues 13-29,'VA' ##label KA2 COMMENT Archaeal flagellins are 10-13 nm in thickness, which is !1thinner than the 20 nm of eubacterial flagellins, and show !1no homology to eubacterial flagellins. GENETICS !$#gene flaB1 CLASSIFICATION #superfamily archaeal flagellin KEYWORDS flagellum FEATURE !$1-12 #domain signal sequence #status predicted #label SIG\ !$13-218 #product flagellin B1 #status experimental #label MAT SUMMARY #length 218 #molecular-weight 22513 #checksum 7076 SEQUENCE /// ENTRY C41316 #type complete TITLE flagellin B2 precursor - Methanococcus voltae ORGANISM #formal_name Methanococcus voltae DATE 21-Apr-1992 #sequence_revision 04-Oct-1996 #text_change 16-Jul-1999 ACCESSIONS C41316 REFERENCE A41316 !$#authors Kalmokoff, M.L.; Jarrell, K.F. !$#journal J. Bacteriol. (1991) 173:7113-7125 !$#title Cloning and sequencing of a multigene family encoding the !1flagellins of Methanococcus voltae. !$#cross-references MUID:92041608; PMID:1718944 !$#accession C41316 !'##molecule_type DNA !'##residues 1-216 ##label KAL !'##cross-references GB:M72148; NID:g150060; PIDN:AAA73075.1; !1PID:g150063 GENETICS !$#gene flaB2 CLASSIFICATION #superfamily archaeal flagellin KEYWORDS flagellum FEATURE !$1-12 #domain signal sequence #status predicted #label SIG\ !$13-216 #product flagellin B2 #status predicted #label MAT SUMMARY #length 216 #molecular-weight 22799 #checksum 9101 SEQUENCE /// ENTRY E64411 #type complete TITLE flagellin B3 precursor - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 13-Sep-1996 #sequence_revision 04-Oct-1996 #text_change 21-Jul-2000 ACCESSIONS E64411 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession E64411 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-223 ##label BUL !'##cross-references GB:U67533; GB:L77117; NID:g2826346; !1PIDN:AAB98896.1; PID:g1591571; TIGR:MJ0893 COMMENT Homology to other archaeal flagellins suggests that !1translation should begin at Met-8 rather than Met-1. GENETICS !$#gene flaB3 !$#map_position FOR823179-823850 !$#start_codon TTG CLASSIFICATION #superfamily archaeal flagellin KEYWORDS flagellum FEATURE !$1-18 #domain (or 8-18) signal sequence #status predicted !8#label SIG\ !$19-223 #product flagellin B3 #status predicted #label MAT SUMMARY #length 223 #molecular-weight 24007 #checksum 1463 SEQUENCE /// ENTRY D41316 #type complete TITLE flagellin B3 precursor - Methanococcus voltae ORGANISM #formal_name Methanococcus voltae DATE 21-Apr-1992 #sequence_revision 04-Oct-1996 #text_change 16-Jul-1999 ACCESSIONS D41316 REFERENCE A41316 !$#authors Kalmokoff, M.L.; Jarrell, K.F. !$#journal J. Bacteriol. (1991) 173:7113-7125 !$#title Cloning and sequencing of a multigene family encoding the !1flagellins of Methanococcus voltae. !$#cross-references MUID:92041608; PMID:1718944 !$#accession D41316 !'##molecule_type DNA !'##residues 1-239 ##label KAL !'##cross-references GB:M72148; NID:g150060; PIDN:AAA73076.1; !1PID:g150064 GENETICS !$#gene flaB3 CLASSIFICATION #superfamily archaeal flagellin KEYWORDS flagellum FEATURE !$1-11 #domain signal sequence #status predicted #label SIG\ !$12-239 #product flagellin B3 #status predicted #label MAT SUMMARY #length 239 #molecular-weight 25523 #checksum 9766 SEQUENCE /// ENTRY A41316 #type complete TITLE flagellin A precursor - Methanococcus voltae ORGANISM #formal_name Methanococcus voltae DATE 21-Apr-1992 #sequence_revision 04-Oct-1996 #text_change 16-Jul-1999 ACCESSIONS A41316 REFERENCE A41316 !$#authors Kalmokoff, M.L.; Jarrell, K.F. !$#journal J. Bacteriol. (1991) 173:7113-7125 !$#title Cloning and sequencing of a multigene family encoding the !1flagellins of Methanococcus voltae. !$#cross-references MUID:92041608; PMID:1718944 !$#accession A41316 !'##molecule_type DNA !'##residues 1-219 ##label KAL !'##cross-references GB:M72148; NID:g150060; PIDN:AAA73073.1; !1PID:g150061 GENETICS !$#gene flaA CLASSIFICATION #superfamily archaeal flagellin KEYWORDS flagellum FEATURE !$1-12 #domain signal sequence #status predicted #label SIG\ !$13-219 #product flagellin A #status predicted #label MAT SUMMARY #length 219 #molecular-weight 23905 #checksum 3510 SEQUENCE /// ENTRY FLEC #type complete TITLE flagellin - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli #variety strain K-12 DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 01-Mar-2002 ACCESSIONS A37249; JV0018; I41270; H64955; A28187 REFERENCE A37249 !$#authors Kuwajima, G.; Asaka, J.I.; Fujiwara, T.; Fujiwara, T.; Node, !1K.; Kondo, E. !$#journal J. Bacteriol. (1986) 168:1479-1483 !$#title Nucleotide sequence of the hag gene encoding flagellin of !1Escherichia coli. !$#cross-references MUID:87057066; PMID:3536885 !$#accession A37249 !'##molecule_type DNA !'##residues 1-498 ##label KUW !'##cross-references GB:M14358; NID:g146311; PIDN:AAA23950.1; !1PID:g146312 !'##experimental_source strain K-12 REFERENCE JV0018 !$#authors Hanafusa, T.; Sakai, A.; Tominaga, A.; Enomoto, M. !$#journal Mol. Gen. Genet. (1989) 216:44-50 !$#title Isolation and characterization of Escherichia coli hag !1operator mutants whose hag48 expression has become !1repressible by a Salmonella H1 repressor. !$#cross-references MUID:89281489; PMID:2659972 !$#accession JV0018 !'##molecule_type DNA !'##residues 1-284,'L',286-498 ##label HAN !'##cross-references GB:X17440; NID:g41649; PIDN:CAA35488.1; PID:g41651 !'##experimental_source strain K-12 REFERENCE I41269 !$#authors Szekely, E.; Simon, M. !$#journal J. Bacteriol. (1983) 155:74-81 !$#title DNA sequence adjacent to flagellar genes and evolution of !1flagellar- phase variation. !$#cross-references MUID:83238225; PMID:6305924 !$#accession I41270 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-20 ##label RES !'##cross-references GB:J01607; NID:g146315; PIDN:AAA92491.1; !1PID:g146317 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64955 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-498 ##label BLAT !'##cross-references GB:AE000285; GB:U00096; NID:g1788229; !1PIDN:AAC74990.1; PID:g1788232; UWGP:b1923 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A28187 !$#authors Kuwajima, G. !$#journal J. Bacteriol. (1988) 170:3305-3309 !$#title Construction of a minimum-size functional flagellin of !1Escherichia coli. !$#cross-references MUID:88257060; PMID:3290204 !$#accession A28187 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-15,140-402,489-498 ##label KU2 !'##cross-references GB:M21445; NID:g146313; PIDN:AAA23951.1; !1PID:g146314 COMMENT This is the principal protein component of the flagellar !1filament, which is a helical, cylindrical structure. The !1flagellin units associate with each other by noncovalent !1interactions. GENETICS !$#gene fliC; hag !$#map_position 42 min CLASSIFICATION #superfamily flagellin KEYWORDS flagellum SUMMARY #length 498 #molecular-weight 51295 #checksum 8876 SEQUENCE /// ENTRY FLBS68 #type complete TITLE flagellin (hag) - Bacillus subtilis (strain I168) ORGANISM #formal_name Bacillus subtilis DATE 30-Nov-1980 #sequence_revision 30-Jun-1993 #text_change 16-Jun-2000 ACCESSIONS A44759; A44758; A03492; C44519; A69639; B44519 REFERENCE A44759 !$#authors Mirel, D.B.; Chamberlin, M.J. !$#journal J. Bacteriol. (1989) 171:3095-3101 !$#title The Bacillus subtilis flagellin gene (hag) is transcribed by !1the sigma(28) form of RNA polymerase. !$#cross-references MUID:89255067; PMID:2498284 !$#accession A44759 !'##molecule_type DNA !'##residues 1-304 ##label MIR !'##cross-references GB:M26948; NID:g143032; PIDN:AAA22509.1; !1PID:g143033 REFERENCE A44758 !$#authors LaVallie, E.R.; Stahl, M.L. !$#journal J. Bacteriol. (1989) 171:3085-3094 !$#title Cloning of the flagellin gene from Bacillus subtilis and !1complementation studies of an in vitro-derived deletion !1mutation. !$#cross-references MUID:89255066; PMID:2498283 !$#accession A44758 !'##molecule_type DNA !'##residues 1-304 ##label LAV !'##cross-references GB:M26947; NID:g142908; PIDN:AAA22437.1; !1PID:g142909 REFERENCE A03492 !$#authors DeLange, R.J.; Chang, J.Y.; Shaper, J.H.; Glazer, A.N. !$#journal J. Biol. Chem. (1976) 251:705-711 !$#title Amino acid sequence of flagellin of Bacillus subtilis 168. !1III. Tryptic peptides, N-bromosuccinimide peptides, and the !1complete amino acid sequence. !$#cross-references MUID:76120526; PMID:814121 !$#accession A03492 !'##molecule_type protein !'##residues 1-100,'TG',103-304 ##label DEL !'##note this is the final paper in a series REFERENCE A44519 !$#authors Dowds, B.C.A. !$#submission submitted to the Protein Sequence Database, February 1993 !$#accession C44519 !'##molecule_type protein !'##residues 1-20,'X',22,'X',24-29 ##label DOW REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69639 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-304 ##label KUN !'##cross-references GB:Z99122; GB:AL009126; NID:g2636029; !1PIDN:CAB15553.1; PID:g2636062 !'##experimental_source strain 168 GENETICS !$#gene hag CLASSIFICATION #superfamily flagellin KEYWORDS flagellum SUMMARY #length 304 #molecular-weight 32626 #checksum 8256 SEQUENCE /// ENTRY FLLYB3 #type complete TITLE flagellin - Lyme disease spirochete ALTERNATE_NAMES flagellum-associated 41K antigen ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS A41470; S04696; B60118; A60705; I40080; S08541 REFERENCE A41470 !$#authors Wallich, R.; Motor, S.E.; Simon, M.M.; Ebnet, K.; Heiberger, !1A.; Kramer, M.D. !$#journal Infect. Immun. (1990) 58:1711-1719 !$#title The Borrelia burgdorferi flagellum-associated 41-kilodalton !1antigen (flagellin): molecular cloning, expression, and !1amplification of the gene. !$#cross-references MUID:90256248; PMID:2341173 !$#accession A41470 !'##molecule_type DNA !'##residues 1-336 ##label WA2 !'##cross-references GB:X16833; NID:g39356; PIDN:CAA34735.1; PID:g39357 !'##experimental_source strain B31 REFERENCE S04091 !$#authors Gassmann, G.S.; Kramer, M.; Goebel, U.B.; Wallich, R. !$#journal Nucleic Acids Res. (1989) 17:3590 !$#title Nucleotide sequence of a gene encoding the Borrelia !1burgdorferi flagellin. !$#cross-references MUID:89263802; PMID:2726494 !$#accession S04696 !'##status translation not shown !'##molecule_type DNA !'##residues 1-336 ##label GAS !'##cross-references EMBL:X15661; NID:g39360; PIDN:CAA33696.1; !1PID:g39361 REFERENCE A60118 !$#authors Luft, B.J.; Jiang, W.; Munoz, P.; Dattwyler, R.J.; Gorevic, !1P.D. !$#journal Infect. Immun. (1989) 57:3637-3645 !$#title Biochemical and immunological characterization of the !1surface proteins of Borrelia burgdorferi. !$#cross-references MUID:90035442; PMID:2807540 !$#accession B60118 !'##molecule_type protein !'##residues 1-9,'A',11-13,'X',15-18 ##label LUF REFERENCE A60705 !$#authors Coleman, J.L.; Benach, J.L. !$#journal J. Clin. Invest. (1989) 84:322-330 !$#title Identification and characterization of an endoflagellar !1antigen of Borrelia burgdorferi. !$#cross-references MUID:89292177; PMID:2738156 !$#accession A60705 !'##molecule_type protein !'##residues 1-10 ##label COL CLASSIFICATION #superfamily flagellin KEYWORDS flagellum; periplasmic space SUMMARY #length 336 #molecular-weight 35751 #checksum 54 SEQUENCE /// ENTRY FLQL2C #type complete TITLE flagellin, 28.5K - Caulobacter crescentus ORGANISM #formal_name Caulobacter crescentus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 15-Nov-1996 ACCESSIONS A03493 REFERENCE A03493 !$#authors Gill, P.R.; Agabian, N. !$#journal J. Biol. Chem. (1983) 258:7395-7401 !$#title The nucleotide sequence of the M-r=28,500 flagellin gene of !1Caulobacter crescentus. !$#cross-references MUID:83238304; PMID:6305939 !$#accession A03493 !'##molecule_type DNA !'##residues 1-276 ##label GIL COMMENT This is one of the three flagellin proteins in C. !1crescentus; the other two are designated 25K and 27K. CLASSIFICATION #superfamily flagellin KEYWORDS flagellum SUMMARY #length 276 #molecular-weight 28666 #checksum 6970 SEQUENCE /// ENTRY A34965 #type complete TITLE 62K membrane antigen ipaB - Shigella flexneri plasmid ORGANISM #formal_name Shigella flexneri DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS A34965; B31265; S06203 REFERENCE A34965 !$#authors Baudry, B.; Kaczorek, M.; Sansonetti, P.J. !$#journal Microb. Pathog. (1988) 4:345-357 !$#title Nucleotide sequence of the invasion plasmid antigen B and C !1genes (ipaB and ipaC) of Shigella flexneri. !$#cross-references MUID:89200844; PMID:3071655 !$#accession A34965 !'##molecule_type DNA !'##residues 1-580 ##label BAU !'##cross-references EMBL:M34849; NID:g155327; PIDN:AAA98424.1; !1PID:g155330 REFERENCE A94219 !$#authors Venkatesan, M.M.; Buysse, J.M.; Kopecko, D.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:9317-9321 !$#title Characterization of invasion plasmid antigen genes (ipaBCD) !1from Shigella flexneri. !$#cross-references MUID:89057927; PMID:3057506 !$#accession B31265 !'##molecule_type DNA !'##residues 1-166,'N',168-580 ##label VEN !'##cross-references GB:J04117; NID:g152740; PIDN:AAA26522.1; !1PID:g152742 REFERENCE S06201 !$#authors Sasakawa, C.; Adler, B.; Tobe, T.; Okada, N.; Nagai, S.; !1Komatsu, K.; Yoshikawa, M. !$#journal Mol. Microbiol. (1989) 3:1191-1201 !$#title Functional organization and nucleotide sequence of virulence !1region-2 on the large virulence plasmid in Shigella flexneri !12a. !$#cross-references MUID:90014179; PMID:2552264 !$#accession S06203 !'##molecule_type DNA !'##residues 1-17,'A',19-580 ##label SAS !'##cross-references EMBL:X15319; NID:g47052; PIDN:CAA33381.1; !1PID:g47055 COMMENT This protein was found in virulent strains but not in !1avirulent, invasion-negative strains; it is induced by Congo !1red, a stain whose uptake correlates with virulence in !1Shigella. Its function is associated with the invasion of !1the bacteria into colonic epithelial cells. GENETICS !$#gene ipaB !$#genome plasmid CLASSIFICATION #superfamily 62K membrane antigen ipaB KEYWORDS bacterial virulence; membrane protein SUMMARY #length 580 #molecular-weight 62201 #checksum 4585 SEQUENCE /// ENTRY S15577 #type complete TITLE 62K membrane antigen ipaB - Shigella dysenteriae plasmid ORGANISM #formal_name Shigella dysenteriae DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS S15577 REFERENCE S15575 !$#authors Yao, R.; Palchaudhuri, S. !$#submission submitted to the EMBL Data Library, June 1991 !$#description Nucleotide sequence of the ipaBCD structure genes of !1Shigella dysenteriae. !$#accession S15577 !'##molecule_type DNA !'##residues 1-580 ##label YAO !'##cross-references EMBL:X60777; NID:g46932; PIDN:CAA43190.1; !1PID:g46935 GENETICS !$#gene ipaB !$#genome plasmid CLASSIFICATION #superfamily 62K membrane antigen ipaB KEYWORDS bacterial virulence; membrane protein SUMMARY #length 580 #molecular-weight 62170 #checksum 4308 SEQUENCE /// ENTRY S22687 #type complete TITLE intercellular spread protein icsB - Shigella flexneri virulence plasmid pWR100 ORGANISM #formal_name Shigella flexneri DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Dec-1999 ACCESSIONS S22687 REFERENCE S22687 !$#authors Allaoui, A.; Mounier, J.; Prevost, M.C.; Sansonetti, P.J.; !1Parsot, C. !$#journal Mol. Microbiol. (1992) 6:1605-1616 !$#title icsB: a Shigella flexneri virulence gene necessary for the !1lysis of protrusions during intercellular spread. !$#cross-references MUID:92356824; PMID:1495389 !$#accession S22687 !'##molecule_type DNA !'##residues 1-494 ##label ALL !'##cross-references EMBL:M86530; NID:g155321; PIDN:AAD15221.1; !1PID:g155322 GENETICS !$#gene icsB !$#genome plasmid CLASSIFICATION #superfamily Shigella flexneri virulence plasmid pWR100 !1intercellular spread protein icsB KEYWORDS bacterial virulence SUMMARY #length 494 #molecular-weight 56323 #checksum 6077 SEQUENCE /// ENTRY A60112 #type complete TITLE 42K membrane antigen ipaC precursor - Shigella flexneri plasmid ORGANISM #formal_name Shigella flexneri DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS C31265; B34965; S06204; A60112 REFERENCE A94219 !$#authors Venkatesan, M.M.; Buysse, J.M.; Kopecko, D.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:9317-9321 !$#title Characterization of invasion plasmid antigen genes (ipaBCD) !1from Shigella flexneri. !$#cross-references MUID:89057927; PMID:3057506 !$#accession C31265 !'##molecule_type DNA !'##residues 1-382 ##label VEN !'##cross-references EMBL:J04117; NID:g152740; PIDN:AAA26523.1; !1PID:g152743 REFERENCE A34965 !$#authors Baudry, B.; Kaczorek, M.; Sansonetti, P.J. !$#journal Microb. Pathog. (1988) 4:345-357 !$#title Nucleotide sequence of the invasion plasmid antigen B and C !1genes (ipaB and ipaC) of Shigella flexneri. !$#cross-references MUID:89200844; PMID:3071655 !$#accession B34965 !'##molecule_type DNA !'##residues 20-382 ##label BAU !'##cross-references EMBL:M34849; NID:g155327; PIDN:AAA98425.1; !1PID:g155331 REFERENCE S06201 !$#authors Sasakawa, C.; Adler, B.; Tobe, T.; Okada, N.; Nagai, S.; !1Komatsu, K.; Yoshikawa, M. !$#journal Mol. Microbiol. (1989) 3:1191-1201 !$#title Functional organization and nucleotide sequence of virulence !1region-2 on the large virulence plasmid in Shigella flexneri !12a. !$#cross-references MUID:90014179; PMID:2552264 !$#accession S06204 !'##molecule_type DNA !'##residues 1-29,'I',31-371,'T',373-382 ##label SAS !'##cross-references EMBL:X15319; NID:g47052; PIDN:CAA33382.1; !1PID:g47056 REFERENCE A60112 !$#authors Sankaran, K.; Ramachandran, V.; Subrahmanyam, Y.V.B.K.; !1Rajarathnam, S.; Elango, S.; Roy, R.K. !$#journal Infect. Immun. (1989) 57:2364-2371 !$#title Congo red-mediated regulation of levels of Shigella flexneri !12a membrane proteins. !$#cross-references MUID:89307550; PMID:2663721 !$#accession A60112 !'##molecule_type protein !'##residues 20-29,'X',31-35,'X',37-38,'X';49-57,'X',59-64;318-335 !1##label SAN COMMENT This protein was found in virulent strains but not in !1avirulent, invasion-negative strains; it is induced by Congo !1red, a stain whose uptake correlates with virulence in !1Shigella. Its function is associated with the invasion of !1the bacteria into colonic epithelial cells. GENETICS !$#gene ipaC !$#genome plasmid CLASSIFICATION #superfamily 42K membrane antigen ipaC KEYWORDS bacterial virulence; membrane protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-382 #product 42K membrane antigen ipaC #status !8experimental #label MAT SUMMARY #length 382 #molecular-weight 41038 #checksum 8821 SEQUENCE /// ENTRY D31265 #type complete TITLE 37K membrane antigen ipaD - Shigella flexneri plasmid ORGANISM #formal_name Shigella flexneri DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS D31265; S06205 REFERENCE A94219 !$#authors Venkatesan, M.M.; Buysse, J.M.; Kopecko, D.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:9317-9321 !$#title Characterization of invasion plasmid antigen genes (ipaBCD) !1from Shigella flexneri. !$#cross-references MUID:89057927; PMID:3057506 !$#accession D31265 !'##molecule_type DNA !'##residues 1-332 ##label VEN !'##cross-references GB:J04117; NID:g152740; PIDN:AAA26524.1; !1PID:g152744 REFERENCE S06201 !$#authors Sasakawa, C.; Adler, B.; Tobe, T.; Okada, N.; Nagai, S.; !1Komatsu, K.; Yoshikawa, M. !$#journal Mol. Microbiol. (1989) 3:1191-1201 !$#title Functional organization and nucleotide sequence of virulence !1region-2 on the large virulence plasmid in Shigella flexneri !12a. !$#cross-references MUID:90014179; PMID:2552264 !$#accession S06205 !'##molecule_type DNA !'##residues 1-101,'H',103-332 ##label SAS !'##cross-references EMBL:X15319; NID:g47052; PIDN:CAA33383.1; !1PID:g47057 COMMENT This protein was found in virulent strains but not in !1avirulent, invasion-negative strains; it is induced by Congo !1red, a stain whose uptake correlates with virulence in !1Shigella. Its function is associated with the invasion of !1the bacteria into colonic epithelial cells. GENETICS !$#gene ipaD !$#genome plasmid CLASSIFICATION #superfamily 37K membrane antigen ipaD KEYWORDS bacterial virulence; membrane protein SUMMARY #length 332 #molecular-weight 36639 #checksum 4252 SEQUENCE /// ENTRY YQEC88 #type complete TITLE fimbrial adhesin K88ab precursor - Escherichia coli plasmid ALTERNATE_NAMES K88 adhesion antigen; K88 pilin ORGANISM #formal_name Escherichia coli DATE 14-Nov-1983 #sequence_revision 01-Mar-1996 #text_change 16-Jul-1999 ACCESSIONS S07208; A03494; C45725; D45725; I41316; I41317; S20036; !1A43634; S24808; S24809; S24818 REFERENCE S07208 !$#authors Gaastra, W.; Mooi, F.R.; Stuitje, A.R.; de Graaf, F.K. !$#journal FEMS Microbiol. Lett. (1981) 12:41-46 !$#title The nucleotide sequence of the gene encoding the K88ab !1protein subunit of porcine enterotoxigenic Escherichia coli. !$#accession S07208 !'##molecule_type DNA !'##residues 1-285 ##label GAA !'##cross-references EMBL:V00292; NID:g41846; PIDN:CAA23567.1; !1PID:g41847 !'##experimental_source variant ab REFERENCE A03494 !$#authors Klemm, P. !$#journal Eur. J. Biochem. (1981) 117:617-627 !$#title The complete amino-acid sequence of the K88 antigen, a !1fimbrial protein from Escherichia coli. !$#cross-references MUID:82027186; PMID:7026236 !$#accession A03494 !'##molecule_type protein !'##residues 22-285 ##label KLE !'##experimental_source strain D1721 !'##note the K88 fimbria, 0.1-1 micrometer in length and 7 nanometers in !1diameter, is composed of about 100 identical subunits; the !1protein exists in several antigenic variants; the sequence !1of the K88ab variant is shown REFERENCE A45725 !$#authors Bakker, D.; Willemsen, P.T.; Willems, R.H.; Huisman, T.T.; !1Mooi, F.R.; Oudega, B.; Stegehuis, F.; de Graaf, F.K. !$#journal J. Bacteriol. (1992) 174:6350-6358 !$#title Identification of minor fimbrial subunits involved in !1biosynthesis of K88 fimbriae. !$#cross-references MUID:93015683; PMID:1400188 !$#contents K12 !$#accession C45725 !'##status preliminary !'##molecule_type DNA !'##residues 1-51 ##label BAK !'##note this sequence (subunit feaG) may be one segment of several !'##note sequence inconsistent with the nucleotide translation !'##note sequence extracted from NCBI backbone (NCBIN:115475, !1NCBIP:115486) !$#accession D45725 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 272-285 ##label BA2 !'##cross-references EMBL:Z11710; NID:g41399; PIDN:CAA77770.1; !1PID:g41400 !'##note sequence extracted from NCBI backbone (NCBIP:115490) REFERENCE I41316 !$#authors Dykes, C.W.; Halliday, I.J.; Read, M.J.; Hobden, A.N.; !1Harford, S. !$#journal Infect. Immun. (1985) 50:279-283 !$#title Nucleotide sequences of four variants of the K88 gene of !1porcine enterotoxigenic Escherichia coli. !$#cross-references MUID:86007039; PMID:2412961 !$#accession I41316 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-285 ##label RES !'##cross-references GB:M29374; NID:g146518; PIDN:AAA24032.1; !1PID:g146519 !$#accession I41317 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-94,'T',96-102,'H',104-114,'V',116-118,'P',120-125,'K', !1126-154,'L',156,'R',158-167,'L',169-175,'SS',178-183,'PR', !1189,'SE',192,'SA',195-202,'K',204-236,'N',238-285 ##label !1RE2 !'##cross-references GB:M29375; NID:g146520; PIDN:AAA24033.1; !1PID:g146521 REFERENCE S20036 !$#authors Bakker, D.; Willemsen, P.T.J.; Simons, L.H.; van Zijderveld, !1F.G.; de Graaf, F.K. !$#journal Mol. Microbiol. (1992) 6:247-255 !$#title Characterization of the antigenic and adhesive properties of !1FaeG, the major subunit of K88 fimbriae. !$#cross-references MUID:92186715; PMID:1372075 !$#accession S20036 !'##molecule_type DNA !'##residues 1-285 ##label GAW !'##cross-references EMBL:V00292; NID:g41846; PIDN:CAA23567.1; !1PID:g41847 !'##experimental_source variant ab !'##note the sequence of residues 1-21 and the corresponding nucleic !1acid sequence are not shown REFERENCE A43634 !$#authors Thiry, G.; Clippe, A.; Scarcez, T.; Petre, J. !$#journal Appl. Environ. Microbiol. (1989) 55:984-993 !$#title Cloning of DNA sequences encoding foreign peptides and their !1expression in the K88 pili. !$#cross-references MUID:89271902; PMID:2471451 !$#accession A43634 !'##status preliminary !'##molecule_type DNA !'##residues 1-94,'T',96-102,'H',104-114,'V',116-118,'P',120-125,'K', !1126-154,'L',156,'R',158-167,'L',169-175,'SS',178-183,'PR', !1189,'SE',192,'SA',195-202,'K',204-236,'N',238-285 ##label !1THI !'##cross-references GB:M25302; NID:g147271; PIDN:AAA24390.1; !1PID:g147272 GENETICS !$#genome plasmid FUNCTION !$#description fimbriae (also called pili), polar filaments radiating from !1the surface of the bacterium to a length of 0.5-1.5 !1micrometers and numbering 100-300 per cell, enable bacteria !1to colonize the epithelium of specific host organs CLASSIFICATION #superfamily fimbrial adhesin K88 KEYWORDS fimbria; surface antigen FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-285 #product fimbrial protein K88 #status predicted !8#label MAT SUMMARY #length 285 #molecular-weight 29546 #checksum 1297 SEQUENCE /// ENTRY I41319 #type complete TITLE fimbrial adhesin K88ad precursor - Escherichia coli plasmid ORGANISM #formal_name Escherichia coli DATE 21-Nov-1998 #sequence_revision 21-Nov-1998 #text_change 16-Jul-1999 ACCESSIONS I41319; I41320 REFERENCE I41316 !$#authors Dykes, C.W.; Halliday, I.J.; Read, M.J.; Hobden, A.N.; !1Harford, S. !$#journal Infect. Immun. (1985) 50:279-283 !$#title Nucleotide sequences of four variants of the K88 gene of !1porcine enterotoxigenic Escherichia coli. !$#cross-references MUID:86007039; PMID:2412961 !$#accession I41319 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-285 ##label DYK !'##cross-references GB:M29376; NID:g146524; PIDN:AAA24035.1; !1PID:g146525 REFERENCE I41320 !$#authors Gaastra, W.; Klemm, P.; de Graaf, F.K. !$#journal FEMS Microbiol. Lett. (1983) 18:177-183 !$#title The nucleotide sequence of the K88ad protein subunit of !1porcine enterotoxigenic Escherichia coli. !$#accession I41320 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 28-58,'S',60-69,'E',71-80,'S',82-86,'R',88-94,'VG',97-122, !1'I',124-187,'Q',189-190,'A',192,'P',194-256,'R',258-275 !1##label GAA !'##cross-references GB:M35637; NID:g146526; PIDN:AAA24036.1; !1PID:g146527 GENETICS !$#genome plasmid CLASSIFICATION #superfamily fimbrial adhesin K88 KEYWORDS fimbria; surface antigen FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-285 #product fimbrial adhesin K88ad #status predicted !8#label MAT SUMMARY #length 285 #molecular-weight 29602 #checksum 1224 SEQUENCE /// ENTRY I41318 #type complete TITLE fimbrial adhesin K88ac precursor - Escherichia coli plasmid ORGANISM #formal_name Escherichia coli DATE 21-Nov-1998 #sequence_revision 21-Nov-1998 #text_change 16-Jul-1999 ACCESSIONS I41318 REFERENCE I41318 !$#authors Josephsen, J.; Hansen, F.; de Graaf, F.K.; Gaastra, W. !$#journal FEMS Microbiol. Lett. (1984) 25:301-306 !$#title The nucleotide sequence of the protein subunit of the K88ac !1fimbriae of porcine enterotoxigenic Escherichia coli. !$#accession I41318 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-283 ##label JOS !'##cross-references GB:M35954; NID:g146522; PIDN:AAA24034.1; !1PID:g146523 GENETICS !$#genome plasmid CLASSIFICATION #superfamily fimbrial adhesin K88 KEYWORDS fimbria; surface antigen FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-283 #product fimbrial adhesin K88ac #status predicted !8#label MAT SUMMARY #length 283 #molecular-weight 29335 #checksum 3403 SEQUENCE /// ENTRY A41663 #type complete TITLE fimbrial adhesin CS31A precursor - Escherichia coli plasmid ALTERNATE_NAMES pilin CS31A ORGANISM #formal_name Escherichia coli DATE 21-Nov-1998 #sequence_revision 21-Nov-1998 #text_change 16-Jul-1999 ACCESSIONS A41663; A43588; A60120 REFERENCE A41663 !$#authors Girardeau, J.P.; Bertin, Y.; Martin, C.; Der Vartanian, M.; !1Boeuf, C. !$#journal J. Bacteriol. (1991) 173:7673-7683 !$#title Sequence analysis of the clpG gene, which codes for surface !1antigen CS31A subunit: evidence of an evolutionary !1relationship between CS31A, K88, and F41 subunit genes. !$#cross-references MUID:92041681; PMID:1938963 !$#accession A41663 !'##molecule_type DNA !'##residues 1-278 ##label GIR !'##cross-references GB:M55389; NID:g145552; PIDN:AAA23585.1; !1PID:g145553 !'##experimental_source plasmid pAG315 REFERENCE A43588 !$#authors Korth, M.J.; Schneider, R.A.; Moseley, S.L. !$#journal Infect. Immun. (1991) 59:2333-2340 !$#title An F41-K88-related genetic determinant of bovine septicemic !1Escherichia coli mediates expression of CS31A fimbriae and !1adherence to epithelial cells. !$#cross-references MUID:91267610; PMID:1675627 !$#accession A43588 !'##molecule_type DNA !'##residues 1-109,'K',111-278 ##label KOR !'##cross-references GB:M59905; NID:g145628; PIDN:AAA23615.1; !1PID:g145629 !'##experimental_source strain 424 genomic DNA REFERENCE A60120 !$#authors Girardeau, J.P.; der Vartanian, M.; Ollier, J.L.; !1Contrepois, M. !$#journal Infect. Immun. (1988) 56:2180-2188 !$#title CS31A, a new K88-related fimbrial antigen on bovine !1enterotoxigenic and septicemic Escherichia coli strains. !$#cross-references MUID:88284951; PMID:2899553 !$#accession A60120 !'##molecule_type protein !'##residues 'G',23-45,'T' ##label GI2 GENETICS !$#gene clpG !$#genome plasmid CLASSIFICATION #superfamily fimbrial adhesin K88 KEYWORDS fimbria; surface antigen FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-278 #product fimbrial adhesin CS31A #status experimental !8#label MAT SUMMARY #length 278 #molecular-weight 28785 #checksum 3750 SEQUENCE /// ENTRY S04072 #type complete TITLE fimbrial adhesin F41 precursor - Escherichia coli (strain B41) ALTERNATE_NAMES minor fimbrial subunit faeI ORGANISM #formal_name Escherichia coli DATE 21-Nov-1998 #sequence_revision 21-Nov-1998 #text_change 16-Jul-1999 ACCESSIONS S04072; I41116 REFERENCE S04072 !$#authors Fidock, D.A.; McNicholas, P.A.; Lehrbach, P.R. !$#journal Nucleic Acids Res. (1989) 17:2849 !$#title Nucleotide sequence of the F41 fimbriae subunit gene in !1Escherichia coli B41. !$#cross-references MUID:89240037; PMID:2566150 !$#accession S04072 !'##molecule_type DNA !'##residues 1-277 ##label FID !'##cross-references EMBL:X14354; NID:g41452; PIDN:CAA32535.1; !1PID:g41453 REFERENCE I41116 !$#authors Anderson, D.G.; Moseley, S.L. !$#journal J. Bacteriol. (1988) 170:4890-4896 !$#title Escherichia coli F41 adhesin: Genetic organization, !1nucleotide sequence, and homology with the K88 determinant. !$#cross-references MUID:89008112; PMID:2902070 !$#accession I41116 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-155,'N',157-165,'TS',168-210,'K',212-228,'P',230-234,'D', !1236-277 ##label AND !'##cross-references GB:M21788; NID:g145207; PIDN:AAA23421.1; !1PID:g145208 CLASSIFICATION #superfamily fimbrial adhesin K88 KEYWORDS fimbria; surface antigen FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-277 #product fimbrial adhesin F41 #status predicted !8#label MAT SUMMARY #length 277 #molecular-weight 29000 #checksum 9132 SEQUENCE /// ENTRY I41314 #type complete TITLE K88 fimbrial protein A precursor - Escherichia coli plasmid ORGANISM #formal_name Escherichia coli DATE 21-Nov-1998 #sequence_revision 21-Nov-1998 #text_change 21-Jul-2000 ACCESSIONS I41314; S24817; I41092 REFERENCE I41092 !$#authors Mooi, F.R.; van Buuren, M.; Koopman, G.; Roosendaal, B.; de !1Graaf, F.K. !$#journal J. Bacteriol. (1984) 159:482-487 !$#title K88ab gene of Escherichia coli encodes a fimbria-like !1protein distinct from the K88ab fimbrial adhesin. !$#cross-references MUID:84264326; PMID:6086572 !$#accession I41314 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-181 ##label RES !'##cross-references GB:K02669; NID:g41848; PIDN:CAA25454.1; !1PID:g1359629 !'##experimental_source plasmid pFM205 derived from the wild-type !1plasmid pRI8801, which contains the K88ab adhesin operon, !1and plasmid pBR322 REFERENCE S24806 !$#authors Bakker, D. !$#submission submitted to the EMBL Data Library, February 1992 !$#accession S24817 !'##molecule_type DNA !'##residues 1-32 ##label BAK !'##cross-references EMBL:Z11709; NID:g41375; PIDN:CAA77769.1; !1PID:g41377 COMMENT This protein is necessary for fimbrial adhesin export; it !1may be a protein component of the fimbria, along with the !1K88ab adhesin (see PIR:YQEC88). GENETICS !$#gene faeC !$#genome plasmid CLASSIFICATION #superfamily K88 fimbrial protein A KEYWORDS fimbria SUMMARY #length 181 #molecular-weight 19066 #checksum 1321 SEQUENCE /// ENTRY YQECC1 #type complete TITLE CFA1 fimbrial protein precursor - Escherichia coli ALTERNATE_NAMES CFA1 pilin; colonization factor antigen I (CFA1) ORGANISM #formal_name Escherichia coli DATE 14-Nov-1983 #sequence_revision 30-Jun-1991 #text_change 15-Nov-1996 ACCESSIONS A30589; A03495; A43831 REFERENCE A30589 !$#authors Karjalainen, T.K.; Evans, D.G.; So, M.; Lee, C.H. !$#journal Infect. Immun. (1989) 57:1126-1130 !$#title Molecular cloning and nucleotide sequence of the !1colonization factor antigen I gene of Escherichia coli. !$#cross-references MUID:89173309; PMID:2564374 !$#accession A30589 !'##molecule_type DNA !'##residues 1-170 ##label KAR REFERENCE A03495 !$#authors Klemm, P. !$#journal Eur. J. Biochem. (1982) 124:339-348 !$#title Primary structure of the CFA1 fimbrial protein from human !1enterotoxigenic Escherichia coli strains. !$#cross-references MUID:82235736; PMID:6124420 !$#accession A03495 !'##molecule_type DNA !'##residues 24-75,'N',77-96,'A',98-170 ##label KLE !'##experimental_source strain H10407 REFERENCE A43831 !$#authors Cassels, F.J.; Deal, C.D.; Reid, R.H.; Jarboe, D.L.; Nauss, !1J.L.; Carter, J.M.; Boedeker, E.C. !$#journal Infect. Immun. (1992) 60:2174-2181 !$#title Analysis of Escherichia coli colonization factor antigen I !1linear B-cell epitopes, as determined by primate responses, !1following protein sequence verification. !$#cross-references MUID:92267624; PMID:1375193 !$#accession A43831 !'##molecule_type protein !'##residues 24-170 ##label CAS !'##experimental_source strain H10407 !'##note sequence extracted from NCBI backbone (NCBIP:104220) COMMENT The CFA1 fimbriae are rather rigid, thread-like filaments of !10.5-1 micrometer, with an apparent axial hole, and a !1diameter of 7 nanometers. A single CFA1 fimbria consists of !1about 100 identical protein subunits. CLASSIFICATION #superfamily CFA1 fimbrial protein KEYWORDS fimbria FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-170 #product CFA1 fimbrial protein #status experimental !8#label MAT SUMMARY #length 170 #molecular-weight 17461 #checksum 1166 SEQUENCE /// ENTRY YQECKS #type complete TITLE KS71A fimbrial protein precursor - Escherichia coli ALTERNATE_NAMES KS71A pilin ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jul-1999 ACCESSIONS A23117 REFERENCE A23117 !$#authors Rhen, M.; van Die, I.; Rhen, V.; Bergmans, H. !$#journal Eur. J. Biochem. (1985) 151:573-577 !$#title Comparison of the nucleotide sequences of the genes encoding !1the KS71A and F7-1 fimbrial antigens of uropathogenic !1Escherichia coli. !$#cross-references MUID:85285072; PMID:2992970 !$#accession A23117 !'##molecule_type DNA !'##residues 1-187 ##label RHE !'##cross-references GB:X02921; NID:g41880; PIDN:CAA26678.1; PID:g41881 CLASSIFICATION #superfamily F7-2 fimbrial protein KEYWORDS fimbria FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-187 #product KS71A fimbrial protein #status predicted !8#label MAT SUMMARY #length 187 #molecular-weight 19310 #checksum 2976 SEQUENCE /// ENTRY YQECF2 #type complete TITLE F7-2 fimbrial protein precursor - Escherichia coli ALTERNATE_NAMES F7-2 pilin ORGANISM #formal_name Escherichia coli DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 16-Jul-1999 ACCESSIONS A03496; B43597 REFERENCE A03496 !$#authors Van Die, I.; Bergmans, H. !$#journal Gene (1984) 32:83-90 !$#title Nucleotide sequence of the gene encoding the F7-2 fimbrial !1subunit of a uropathogenic Escherichia coli strain. !$#cross-references MUID:85155489; PMID:6152241 !$#accession A03496 !'##molecule_type DNA !'##residues 1-188 ##label VAN !'##cross-references GB:M12861; NID:g145963; PIDN:AAA23778.1; !1PID:g145964 REFERENCE A43597 !$#authors Denich, K.; Blyn, L.B.; Craiu, A.; Braaten, B.A.; Hardy, J.; !1Low, D.A.; O'Hanley, P.D. !$#journal Infect. Immun. (1991) 59:3849-3858 !$#title DNA sequences of three papA genes from uropathogenic !1Escherichia coli strains: evidence of structural and !1serological conservation. !$#cross-references MUID:92040048; PMID:1682251 !$#accession B43597 !'##molecule_type DNA !'##residues 1-188 ##label DEN !'##cross-references GB:M68060; NID:g147070; PIDN:AAA24278.1; !1PID:g147071 GENETICS !$#gene papA FUNCTION !$#description one of the fimbrial proteins involved in mannose-resistant !1hemagglutination of human erythrocytes; they may also be !1involved in the translocation of the fimbrial subunit, !1assembly of subunits into fimbriae, or regulation of phase !1variation CLASSIFICATION #superfamily F7-2 fimbrial protein KEYWORDS fimbria; mannose-resistant hemagglutination FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-188 #product F7-2 fimbrial protein #status predicted !8#label MAT SUMMARY #length 188 #molecular-weight 19184 #checksum 6960 SEQUENCE /// ENTRY YQECPP #type complete TITLE fimbrial protein papA precursor - Escherichia coli ALTERNATE_NAMES pap pili ORGANISM #formal_name Escherichia coli DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 16-Jul-1999 ACCESSIONS A23221; S25216; A05229; S16395 REFERENCE A91794 !$#authors Baga, M.; Normark, S.; Hardy, J.; O'Hanley, P.; Lark, D.; !1Olsson, O.; Schoolnik, G.; Falkow, S. !$#journal J. Bacteriol. (1984) 157:330-333 !$#title Nucleotide sequence of the papA gene encoding the pap pilus !1subunit of human uropathogenic Escherichia coli. !$#cross-references MUID:84087728; PMID:6140260 !$#accession A23221 !'##molecule_type DNA !'##residues 1-185 ##label BAG !'##cross-references GB:X03391; GB:K01176; GB:X03392; NID:g42309; !1PIDN:CAA27126.1; PID:g42312 REFERENCE S25205 !$#authors Marklund, B.I.; Tennent, J.M.; Garcia, E.; Hamers, A.; Baga, !1M.; Lindberg, F.; Gaastra, W.; Normark, S. !$#journal Mol. Microbiol. (1992) 6:2225-2242 !$#title Horizontal gene transfer of the Escherichia coli pap and prs !1pili operons as a mechanism for the development of !1tissue-specific adhesive properties. !$#cross-references MUID:93023852; PMID:1357526 !$#accession S25216 !'##molecule_type DNA !'##residues 1-185 ##label MA2 !'##cross-references EMBL:X61239; NID:g42290; PIDN:CAA43562.1; !1PID:g42293 !'##experimental_source strain J96 GENETICS !$#gene papA CLASSIFICATION #superfamily F7-2 fimbrial protein KEYWORDS fimbria FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-185 #product fimbrial protein papA #status predicted !8#label MAT SUMMARY #length 185 #molecular-weight 18686 #checksum 2838 SEQUENCE /// ENTRY A40643 #type complete TITLE MR/P fimbriae, major fimbrial subunit - Proteus mirabilis ORGANISM #formal_name Proteus mirabilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A40643 REFERENCE A40643 !$#authors Bahrani, F.K.; Mobley, H.L. !$#journal J. Bacteriol. (1993) 175:457-464 !$#title Proteus mirabilis MR/P fimbriae: molecular cloning, !1expression, and nucleotide sequence of the major fimbrial !1subunit gene. !$#cross-references MUID:93123164; PMID:8093447 !$#accession A40643 !'##status preliminary !'##molecule_type DNA; protein !'##residues 1-175 ##label BAH !'##cross-references GB:Z18753; GB:S52945; NID:g45624; PIDN:CAA79244.1; !1PID:g45625 !'##experimental_source HI4320 !'##note sequence extracted from NCBI backbone (NCBIN:122462, !1NCBIP:122463) CLASSIFICATION #superfamily F7-2 fimbrial protein SUMMARY #length 175 #molecular-weight 17910 #checksum 3960 SEQUENCE /// ENTRY A31096 #type complete TITLE fimbrial protein precursor, mannose-resistant - Serratia marcescens (strain US46) ORGANISM #formal_name Serratia marcescens DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A31096 REFERENCE A31096 !$#authors Mizunoe, Y.; Nakabeppu, Y.; Sekiguchi, M.; Kawabata, S.I.; !1Moriya, T.; Amako, K. !$#journal J. Bacteriol. (1988) 170:3567-3574 !$#title Cloning and sequence of the gene encoding the major !1structural component of mannose-resistant fimbriae of !1Serratia marcescens. !$#cross-references MUID:88298666; PMID:2900238 !$#accession A31096 !'##molecule_type DNA !'##residues 1-174 ##label MIZ !'##cross-references GB:M21161; NID:g152863; PIDN:AAA26576.1; !1PID:g152864 GENETICS !$#gene smfA CLASSIFICATION #superfamily F7-2 fimbrial protein FEATURE !$1-21 #domain (or 1-22) signal sequence #status predicted !8#label SIG\ !$22-174 #product (or 23-174) fimbrial protein, !8mannose-resistant #status predicted #label MAT SUMMARY #length 174 #molecular-weight 17771 #checksum 2103 SEQUENCE /// ENTRY YQECPH #type complete TITLE fimbrial protein papH precursor - Escherichia coli ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 16-Jul-1999 ACCESSIONS A27021; S25217; S03750; S16396 REFERENCE A27021 !$#authors Baga, M.; Norgren, M.; Normark, S. !$#journal Cell (1987) 49:241-251 !$#title Biogenesis of E. coli pap pili: papH, a minor pilin subunit !1involved in cell anchoring and length modulation. !$#cross-references MUID:87187619; PMID:2882856 !$#accession A27021 !'##molecule_type DNA !'##residues 1-195 ##label BAG !'##cross-references GB:M16202; NID:g147083; PIDN:AAA24286.1; !1PID:g147085 REFERENCE S25205 !$#authors Marklund, B.I.; Tennent, J.M.; Garcia, E.; Hamers, A.; Baga, !1M.; Lindberg, F.; Gaastra, W.; Normark, S. !$#journal Mol. Microbiol. (1992) 6:2225-2242 !$#title Horizontal gene transfer of the Escherichia coli pap and prs !1pili operons as a mechanism for the development of !1tissue-specific adhesive properties. !$#cross-references MUID:93023852; PMID:1357526 !$#accession S25217 !'##molecule_type DNA !'##residues 1-195 ##label MA2 !'##cross-references EMBL:X61239; NID:g42290; PIDN:CAA43563.1; !1PID:g42294 !'##experimental_source strain J96 REFERENCE S03750 !$#authors Norgren, M.; Baga, M.; Tennent, J.M.; Normark, S. !$#journal Mol. Microbiol. (1987) 1:169-178 !$#title Nucleotide sequence, regulation and functional analysis of !1the papC gene required for cell surface localization of Pap !1pili of uropathogenic Escherichia coli. !$#cross-references MUID:88216160; PMID:2897064 !$#accession S03750 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 149-195 ##label NOR !'##cross-references EMBL:Y00529; NID:g42303; PIDN:CAA68587.1; !1PID:g747709 GENETICS !$#gene papH FUNCTION !$#description involved in anchoring the pilus to the bacterial cell and in !1modulation of the pilus length CLASSIFICATION #superfamily papH fimbrial protein KEYWORDS fimbria FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-195 #product fimbrial protein papH #status predicted !8#label MAT SUMMARY #length 195 #molecular-weight 21835 #checksum 9123 SEQUENCE /// ENTRY YQEC7P #type complete TITLE fimbrial protein 987P precursor - Escherichia coli ALTERNATE_NAMES fimbrial adhesin 987P ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS S06261; A41501; S12505 REFERENCE S06261 !$#authors de Graaf, F.K.; Klaasen, P. !$#journal FEMS Microbiol. Lett. (1987) 42:253-258 !$#title Nucleotide sequence of the gene encoding the 987P fimbrial !1subunit of Escherichia coli. !$#accession S06261 !'##molecule_type DNA !'##residues 1-194 ##label DEG !'##cross-references EMBL:M35257; NID:g145159; PIDN:AAA23405.1; !1PID:g145160 !'##note it is uncertain whether Met-1 or Met-3 is the initiator REFERENCE A41501 !$#authors Klaasen, P.; Woodward, M.J.; van Zijderveld, F.G.; de Graaf, !1F.K. !$#journal Infect. Immun. (1990) 58:801-807 !$#title The 987P gene cluster in enterotoxigenic Escherichia coli !1contains an ST-pa transposon that activates 987P expression. !$#cross-references MUID:90170142; PMID:1968436 !$#accession A41501 !'##molecule_type DNA !'##residues 1-10 ##label KLA REFERENCE S12505 !$#authors Pedersen, J.K.; Klemm, P.; Gaastra, W. !$#journal FEMS Microbiol. Lett. (1986) 33:229-234 !$#title 987P fimbriae from porcine enterotoxigenic Escherichia coli: !1characterization, N-terminal amino acid sequence and !1immunization with purified antigen. !$#accession S12505 !'##molecule_type protein !'##residues 24-31,'Z',33,'B',35 ##label PED CLASSIFICATION #superfamily type 1 fimbrial protein KEYWORDS fimbria FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-194 #product fimbrial protein 987P #status experimental !8#label MAT\ !$46-85 #disulfide_bonds #status predicted SUMMARY #length 194 #molecular-weight 19660 #checksum 4357 SEQUENCE /// ENTRY YQECT1 #type complete TITLE type 1 fimbrial protein fimA precursor - Escherichia coli (strain K-12) ALTERNATE_NAMES type 1 pilin ORGANISM #formal_name Escherichia coli DATE 28-Dec-1987 #sequence_revision 30-Jan-1998 #text_change 01-Mar-2002 ACCESSIONS S56539; D65245; A23102; A23180; A05230 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56539 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-182 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97210.1; !1PID:g537155 !'##experimental_source strain K-12, substrain MG1655 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65245 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-182 ##label BLAT !'##cross-references GB:AE000502; GB:U00096; NID:g2367374; !1PIDN:AAC77270.1; PID:g1790769; UWGP:b4314 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A23102 !$#authors Orndorff, P.E.; Falkow, S. !$#journal J. Bacteriol. (1985) 162:454-457 !$#title Nucleotide sequence of pilA, the gene encoding the !1structural component of type 1 pili in Escherichia coli. !$#cross-references MUID:85157451; PMID:2858471 !$#accession A23102 !'##molecule_type DNA !'##residues 1-19,'T',21-182 ##label ORN !'##cross-references GB:M27603; NID:g147269; PIDN:AAA24389.1; !1PID:g147270 REFERENCE A91138 !$#authors Klemm, P. !$#journal Eur. J. Biochem. (1984) 143:395-399 !$#title The fimA gene encoding the type-1 fimbrial subunit of !1Escherichia coli. !$#cross-references MUID:84285425; PMID:6147250 !$#accession A23180 !'##molecule_type DNA !'##residues 1-162,164-182 ##label KLE !'##cross-references GB:X00981; NID:g41456; PIDN:CAA25489.1; PID:g41457 GENETICS !$#gene fimA CLASSIFICATION #superfamily type 1 fimbrial protein KEYWORDS fimbria; mannose-resistant hemagglutination FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-182 #product type 1 fimbrial protein #status predicted !8#label MAT SUMMARY #length 182 #molecular-weight 18111 #checksum 8837 SEQUENCE /// ENTRY YQKBT1 #type complete TITLE type 1 fimbrial protein precursor - Klebsiella pneumoniae (strain IA565) ORGANISM #formal_name Klebsiella pneumoniae DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jul-1999 ACCESSIONS JT0284 REFERENCE JT0284 !$#authors Gerlach, G.F.; Clegg, S. !$#journal Gene (1988) 64:231-240 !$#title Characterization of two genes encoding antigenically !1distinct type-1 fimbriae of Klebsiella pneumoniae. !$#cross-references MUID:88297154; PMID:2456966 !$#accession JT0284 !'##molecule_type DNA !'##residues 1-182 ##label GER !'##cross-references GB:M20917; NID:g149229; PIDN:AAA25091.1; !1PID:g149230 CLASSIFICATION #superfamily type 1 fimbrial protein KEYWORDS fimbria FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-182 #product type 1 fimbrial protein #status predicted !8#label MAT SUMMARY #length 182 #molecular-weight 18181 #checksum 9626 SEQUENCE /// ENTRY YQEC1C #type complete TITLE type 1 fimbrial protein pilC precursor - Escherichia coli ALTERNATE_NAMES type 1C pilin ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Oct-1997 #text_change 16-Jul-1999 ACCESSIONS I76901; A22795; I41207 REFERENCE I57111 !$#authors Harel, J.; Jacques, M.; Fairbrother, J.M.; Bosse, M.; !1Forget, C. !$#journal Microbiology (1995) 141:221-228 !$#title Cloning of determinants encoding F165(2) fimbriae from !1porcine septicaemic Escherichia coli confirms their identity !1as F1C fimbriae. !$#cross-references MUID:95202083; PMID:7894716 !$#accession I76901 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-180 ##label RES !'##cross-references EMBL:U09857; NID:g1230560; PIDN:AAA97532.1; !1PID:g967131 !'##experimental_source strain 4787 o115:v165:f165 REFERENCE A22795 !$#authors van Die, I.; van Geffen, B.; Hoekstra, W.; Bergmans, H. !$#journal Gene (1985) 34:187-196 !$#title Type 1C fimbriae of a uropathogenic Escherichia coli strain: !1cloning and characterization of the genes involved in the !1expression of the 1C antigen and nucleotide sequence of the !1subunit gene. !$#cross-references MUID:85232064; PMID:2861144 !$#accession A22795 !'##molecule_type DNA !'##residues 1-24,'V',26-180 ##label VAN !'##cross-references GB:M13053; NID:g145957; PIDN:AAA23775.1; !1PID:g145958 !'##experimental_source strain AD110 GENETICS !$#gene pilC !$#map_position 98 min CLASSIFICATION #superfamily type 1 fimbrial protein KEYWORDS fimbria; mannose-resistant hemagglutination FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-180 #product type 1 fimbrial protein pilC #status !8predicted #label MAT SUMMARY #length 180 #molecular-weight 18299 #checksum 807 SEQUENCE /// ENTRY YQECFA #type complete TITLE fimbrial protein sfaA precursor - Escherichia coli (strain O6-536) ALTERNATE_NAMES S-fimbrial adhesin; S-fimbrillin ORGANISM #formal_name Escherichia coli DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jul-1999 ACCESSIONS S00352 REFERENCE S00352 !$#authors Schmoll, T.; Hacker, J.; Goebel, W. !$#journal FEMS Microbiol. Lett. (1987) 41:229-235 !$#title Nucleotide sequence of the sfaA gene coding for the !1S-fimbrial protein subunit of Escherichia coli. !$#accession S00352 !'##molecule_type DNA !'##residues 1-180 ##label SCH !'##cross-references EMBL:X17420; NID:g42951; PIDN:CAA35468.1; !1PID:g42952 GENETICS !$#gene sfaA CLASSIFICATION #superfamily type 1 fimbrial protein KEYWORDS fimbria; mannose-resistant hemagglutination FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-180 #product S-fimbrial protein #status predicted #label !8MAT\ !$44-83 #disulfide_bonds #status predicted SUMMARY #length 180 #molecular-weight 18399 #checksum 9599 SEQUENCE /// ENTRY YQSE1 #type complete TITLE type 1 fimbrial protein precursor - Serratia marcescens ORGANISM #formal_name Serratia marcescens DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS S12398; S14465 REFERENCE S12398 !$#authors Nichols, W.A.; Clegg, S.; Brown, M.R. !$#journal Mol. Microbiol. (1990) 4:2119-2126 !$#title Characterization of the type 1 fimbrial subunit gene (fimA) !1of Serratia marcescens. !$#cross-references MUID:91211622; PMID:1982455 !$#accession S12398 !'##molecule_type DNA !'##residues 1-180 ##label NIC1 !'##cross-references EMBL:X55025; NID:g47281; PIDN:CAA38764.1; !1PID:g47282 !'##note the sequence from Fig. 3 is inconsistent with that shown in !1Fig. 2 in having 86-Ala !'##note the authors translated the codon GAC for residue 97 as Asn, GGC !1for residue 129 as Pro, and CGT for residue 158 as Ala GENETICS !$#gene fimA CLASSIFICATION #superfamily type 1 fimbrial protein KEYWORDS fimbria; mannose-resistant hemagglutination FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-180 #product type 1 fimbrial protein #status predicted !8#label MAT SUMMARY #length 180 #molecular-weight 18546 #checksum 1617 SEQUENCE /// ENTRY YQECF7 #type complete TITLE F17 fimbrial protein precursor - Escherichia coli ALTERNATE_NAMES F17 fimbrial adhesive antigen; F17 pilin ORGANISM #formal_name Escherichia coli DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 05-Jan-1996 ACCESSIONS A27625 REFERENCE A27625 !$#authors Lintermans, P.; Pohl, P.; Deboeck, F.; Bertels, A.; !1Schlicker, C.; Vandekerckhove, J.; Van Damme, J.; Van !1Montagu, M.; De Greve, H. !$#journal Infect. Immun. (1988) 56:1475-1484 !$#title Isolation and nucleotide sequence of the F17-A gene encoding !1the structural protein of the F17 fimbriae in bovine !1enterotoxigenic Escherichia coli. !$#cross-references MUID:88226920; PMID:2897333 !$#accession A27625 !'##molecule_type DNA !'##residues 1-180 ##label LIN !'##note the authors translated the codon ATT for residue 104 as Asn GENETICS !$#gene F17A CLASSIFICATION #superfamily type 1 fimbrial protein KEYWORDS fimbria FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-180 #product F17 fimbrial protein #status predicted !8#label MAT SUMMARY #length 180 #molecular-weight 18557 #checksum 6888 SEQUENCE /// ENTRY A39202 #type complete TITLE site-specific integrase/recombinase, with XerC - Escherichia coli (strain K-12) ALTERNATE_NAMES recombinase XerD; XprB protein ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS A39202; A49071; F65073 REFERENCE A39202 !$#authors Lovett, S.T.; Kolodner, R.D. !$#journal J. Bacteriol. (1991) 173:353-364 !$#title Nucleotide sequence of the Escherichia coli recJ chromosomal !1region and construction of recJ-overexpression plasmids. !$#cross-references MUID:91100304; PMID:1987126 !$#accession A39202 !'##molecule_type DNA !'##residues 1-298 ##label LOV !'##cross-references GB:M54884; NID:g147547; PIDN:AAA62787.1; !1PID:g147548 REFERENCE A49071 !$#authors Blakely, G.; May, G.; McCulloch, R.; Arciszewska, L.K.; !1Burke, M.; Lovett, S.T.; Sherratt, D.J. !$#journal Cell (1993) 75:351-361 !$#title Two related recombinases are required for site-specific !1recombination at dif and cer in Escherichia coli K12. !$#cross-references MUID:94006566; PMID:8402918 !$#accession A49071 !'##molecule_type protein !'##residues 1-29 ##label BLA REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65073 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-298 ##label BLAT !'##cross-references GB:AE000373; GB:U00096; NID:g2367173; !1PIDN:AAC75932.1; PID:g1789261; UWGP:b2894 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene xerD; XprB !$#start_codon GTG CLASSIFICATION #superfamily probable site-specific integrase/recombinase !1XerC SUMMARY #length 298 #molecular-weight 34246 #checksum 3105 SEQUENCE /// ENTRY A64061 #type complete TITLE probable integrase/recombinase - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A64061 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession A64061 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-297 ##label TIGR !'##cross-references GB:U32716; GB:L42023; NID:g1573268; !1PIDN:AAC21974.1; PID:g1573278; TIGR:HI0309 CLASSIFICATION #superfamily probable site-specific integrase/recombinase !1XerC SUMMARY #length 297 #molecular-weight 34120 #checksum 6740 SEQUENCE /// ENTRY F64085 #type complete TITLE probable site-specific recombinase xerC - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS F64085 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession F64085 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-295 ##label TIGR !'##cross-references GB:U32750; GB:L42023; NID:g1573668; !1PIDN:AAC22336.1; PID:g1573676; TIGR:HI0676 !'##note named as homolog to a protein from Escherichia coli CLASSIFICATION #superfamily probable site-specific integrase/recombinase !1XerC SUMMARY #length 295 #molecular-weight 33935 #checksum 9825 SEQUENCE /// ENTRY C37841 #type complete TITLE probable site-specific recombinase xerC - Escherichia coli (strain K-12) ALTERNATE_NAMES integrase/recombinase XerC ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS C37841; D65185; S30701 REFERENCE A37841 !$#authors Colloms, S.D.; Sykora, P.; Szatmari, G.; Sherratt, D.J. !$#journal J. Bacteriol. (1990) 172:6973-6980 !$#title Recombination at ColE1 cer requires the Escherichia coli !1xerC gene product, a member of the lambda integrase family !1of site-specific recombinases. !$#cross-references MUID:91072248; PMID:2254268 !$#accession C37841 !'##status preliminary !'##molecule_type DNA !'##residues 1-298 ##label COL !'##cross-references GB:M38257; NID:g148267; PIDN:AAA24763.1; !1PID:g148270 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65185 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-298 ##label BLAT !'##cross-references GB:AE000457; GB:U00096; NID:g2367294; !1PIDN:AAC76814.1; PID:g1790244; UWGP:b3811 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S30660 !$#authors Daniels, D.L.; Plunkett III, G.; Burland, V.; Blattner, F.R. !$#journal Science (1992) 257:771-778 !$#title Analysis of the Escherichia coli genome: DNA sequence of the !1region from 84.5 to 86.5 minutes. !$#cross-references MUID:92358234; PMID:1379743 !$#accession S30701 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-183,'KP',186-214,'X',216-242,'X',244-298 ##label DAN !'##cross-references EMBL:M87049; NID:g836656; PIDN:AAA67607.1; !1PID:g148210 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1992 GENETICS !$#gene xerC CLASSIFICATION #superfamily probable site-specific integrase/recombinase !1XerC SUMMARY #length 298 #molecular-weight 33867 #checksum 6346 SEQUENCE /// ENTRY S61402 #type complete TITLE site-specific recombinase sss - Pseudomonas aeruginosa ORGANISM #formal_name Pseudomonas aeruginosa DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S61402; S43156 REFERENCE S61400 !$#authors Hoefte, M.; Dong, Q.; Kourambas, S.; Krishnapillai, V.; !1Sherratt, D.; Mergeay, M. !$#journal Mol. Microbiol. (1994) 14:1011-1020 !$#title The sss gene product, which affects pyoverdin production in !1Pseudomonas aeruginosa 7NSK2, is a site-specific !1recombinase. !$#cross-references MUID:95231283; PMID:7715441 !$#accession S61402 !'##status preliminary; nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-302 ##label HOE !'##cross-references EMBL:X78478 REFERENCE S43154 !$#authors Hofte, M.; Dong, Q.; Kourambas, S.; Krishnapillai, V.; !1Mergeay, M. !$#submission submitted to the EMBL Data Library, March 1994 !$#description The sss gene product which affects pyoverdin production in !1Pseudomonas aeruginosa 7NSK2 is a site-specific recombinase. !$#accession S43156 !'##status preliminary !'##molecule_type DNA !'##residues 1-292,'Q',294-302 ##label HOF !'##cross-references EMBL:X78478; NID:g468712; PIDN:CAA55226.1; !1PID:g468715 GENETICS !$#gene sss CLASSIFICATION #superfamily probable site-specific integrase/recombinase !1XerC SUMMARY #length 302 #molecular-weight 33886 #checksum 411 SEQUENCE /// ENTRY G69601 #type complete TITLE integrase/recombinase codV - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS G69601; S61493; S72309 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69601 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-304 ##label KUN !'##cross-references GB:Z99112; GB:AL009126; NID:g2633902; !1PIDN:CAB13487.1; PID:g2633986 !'##experimental_source strain 168 REFERENCE S61493 !$#authors Slack, F.J.; Serror, P.; Joyce, E.; Sonenshein, A.L. !$#journal Mol. Microbiol. (1995) 15:689-702 !$#title A gene required for nutritional repression of the Bacillus !1subtilis dipeptide permease operon. !$#cross-references MUID:95302982; PMID:7783641 !$#accession S61493 !'##molecule_type DNA !'##residues 1-264,'GL',267-304 ##label SLA !'##cross-references EMBL:U13634; NID:g535347 REFERENCE S72309 !$#authors Sonenshein, A.L. !$#submission submitted to the EMBL Data Library, August 1994 !$#accession S72309 !'##molecule_type DNA !'##residues 1-304 ##label SON !'##cross-references EMBL:U13634; NID:g535347; PIDN:AAB03369.1; !1PID:g535348 !'##experimental_source strain JH642 GENETICS !$#gene codV CLASSIFICATION #superfamily probable site-specific integrase/recombinase !1XerC SUMMARY #length 304 #molecular-weight 35342 #checksum 6515 SEQUENCE /// ENTRY S72959 #type complete TITLE probable integrase - Mycobacterium leprae ALTERNATE_NAMES u0247d protein ORGANISM #formal_name Mycobacterium leprae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 23-Mar-2001 ACCESSIONS S72959 REFERENCE S72589 !$#authors Smith, D.R.; Robison, K. !$#submission submitted to the EMBL Data Library, November 1993 !$#description Mycobacterium leprae cosmid L247. !$#accession S72959 !'##status preliminary !'##molecule_type DNA !'##residues 1-316 ##label SMI !'##cross-references EMBL:U00021; NID:g467141; PIDN:AAA50925.1; !1PID:g467161 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily probable site-specific integrase/recombinase !1XerC SUMMARY #length 316 #molecular-weight 33875 #checksum 4685 SEQUENCE /// ENTRY D70503 #type complete TITLE probable integrase/recombinase - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS D70503 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession D70503 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-311 ##label COL !'##cross-references GB:Z98268; GB:AL123456; NID:g3261839; !1PIDN:CAB10958.1; PID:g2326744 !'##experimental_source strain H37Rv GENETICS !$#gene Rv1701 CLASSIFICATION #superfamily probable site-specific integrase/recombinase !1XerC SUMMARY #length 311 #molecular-weight 33517 #checksum 896 SEQUENCE /// ENTRY A69693 #type complete TITLE integrase/recombinase ripX - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A69693 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69693 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-296 ##label KUN !'##cross-references GB:Z99116; GB:AL009126; NID:g2634723; !1PIDN:CAB14283.1; PID:g2634786 !'##experimental_source strain 168 GENETICS !$#gene ripX CLASSIFICATION #superfamily probable site-specific integrase/recombinase !1XerC SUMMARY #length 296 #molecular-weight 33995 #checksum 7846 SEQUENCE /// ENTRY D69219 #type complete TITLE integrase-recombinase protein - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS D69219 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession D69219 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-311 ##label MTH !'##cross-references GB:AE000865; GB:AE000666; NID:g2621984; !1PIDN:AAB85391.1; PID:g2621988 !'##experimental_source strain Delta H GENETICS !$#gene MTH893 CLASSIFICATION #superfamily probable site-specific integrase/recombinase !1XerC SUMMARY #length 311 #molecular-weight 36911 #checksum 2881 SEQUENCE /// ENTRY A29646 #type complete TITLE invasin - Yersinia pseudotuberculosis ORGANISM #formal_name Yersinia pseudotuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A29646; S12543 REFERENCE A29646 !$#authors Isberg, R.R.; Voorhis, D.L.; Falkow, S. !$#journal Cell (1987) 50:769-778 !$#title Identification of invasin: a protein that allows enteric !1bacteria to penetrate cultured mammalian cells. !$#cross-references MUID:87301720; PMID:3304658 !$#accession A29646 !'##molecule_type DNA !'##residues 1-986 ##label ISB !'##cross-references GB:M17448; NID:g155439; PIDN:AAA27632.1; !1PID:g155440 REFERENCE S12543 !$#authors Leong, J.M.; Fournier, R.S.; Isberg, R.R. !$#journal EMBO J. (1990) 9:1979-1989 !$#title Identification of the integrin binding domain of the !1Yersinia pseudotuberculosis invasin protein. !$#cross-references MUID:90269235; PMID:1693333 !$#accession S12543 !'##status preliminary !'##molecule_type DNA !'##residues 795-986 ##label LEO CLASSIFICATION #superfamily invasin SUMMARY #length 986 #molecular-weight 106758 #checksum 200 SEQUENCE /// ENTRY S54216 #type complete TITLE invasin - Yersinia enterocolitica (strain W1024) ORGANISM #formal_name Yersinia enterocolitica #variety strain W1024 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S54216 REFERENCE S54213 !$#authors Fauconnier, A.; Allaoui, A.; van Elsen, A.; Cornelis, G.; !1Bollen, A. !$#submission submitted to the EMBL Data Library, February 1995 !$#description Clustering of flagellar genes around invA, the Yersinia !1enterocolitica invasin locus. !$#accession S54216 !'##molecule_type DNA !'##residues 1-835 ##label FAU !'##cross-references EMBL:Z48169; NID:g793891; PIDN:CAA88188.1; !1PID:g793895 !'##experimental_source strain W1024; serotype O:9 GENETICS !$#gene invA CLASSIFICATION #superfamily invasin SUMMARY #length 835 #molecular-weight 91367 #checksum 1356 SEQUENCE /// ENTRY I41193 #type complete TITLE outer membrane protein eae - Escherichia coli ALTERNATE_NAMES outer membrane protein 1 ORGANISM #formal_name Escherichia coli DATE 31-May-1996 #sequence_revision 31-May-1996 #text_change 16-Jul-1999 ACCESSIONS I41193; S20027; I41191; S17357; S19838 REFERENCE I41193 !$#authors Beebakhee, G.; Louie, M.; De Azavedo, J.; Brunton, J. !$#journal FEMS Microbiol. Lett. (1992) 91:63-68 !$#title Cloning and nucleotide sequence of the eae gene homologue !1from enterohemorrhagic Escherichia coli serotype 0157:H7. !$#accession I41193 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-935 ##label RES !'##cross-references EMBL:X60439; NID:g42155; PIDN:CAA42967.1; !1PID:g42156 REFERENCE S20027 !$#authors Yu, J.; Kaper, J.B. !$#journal Mol. Microbiol. (1992) 6:411-417 !$#title Cloning and characterization of the eae gene of !1enterohaemorrhagic Escherichia coli O157:H7. !$#cross-references MUID:92204008; PMID:1552854 !$#accession S20027 !'##molecule_type DNA !'##residues 1-220,'D',222-310,'RR',313-317,'H',319-641,'S',643-769,771, !1'GE',774-935 ##label YUJ !'##cross-references EMBL:Z11541; NID:g41333; PIDN:CAA77642.1; !1PID:g41334 REFERENCE I41191 !$#authors Louie, M.; de Azavedo, J.; Clarke, R.; Borczyk, A.; Lior, !1H.; Richter, M.; Brunton, J. !$#journal Epidemiol. Infect. (1994) 112:449-461 !$#title Sequence heterogeneity of the eae gene and detection of !1verotoxin-producing Escherichia coli using serotype-specific !1primers. !$#cross-references MUID:94273785; PMID:8005211 !$#accession I41191 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 684-769,771,'GE',774-903,'S',905-929 ##label RE2 !'##cross-references GB:L08095; NID:g499364; PIDN:AAA21468.1; !1PID:g538254 GENETICS !$#gene eae CLASSIFICATION #superfamily invasin KEYWORDS membrane protein SUMMARY #length 935 #molecular-weight 101995 #checksum 6149 SEQUENCE /// ENTRY I40705 #type complete TITLE bacterial adhesin - Citrobacter freundii ORGANISM #formal_name Citrobacter freundii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS I40705 REFERENCE I40704 !$#authors Schauer, D.B.; Falkow, S. !$#journal Infect. Immun. (1993) 61:2486-2492 !$#title Attaching and effacing locus of a Citrobacter freundii that !1causes transmissible murine colonic hyperplasia. !$#cross-references MUID:93273499; PMID:8500884 !$#accession I40705 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-936 ##label RES !'##cross-references GB:L11691; NID:g304360; PIDN:AAA23097.1; !1PID:g304362 CLASSIFICATION #superfamily invasin SUMMARY #length 936 #molecular-weight 102104 #checksum 7013 SEQUENCE /// ENTRY YQECF #type complete TITLE fimbrial protein precursor - Escherichia coli ALTERNATE_NAMES F pilin ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jul-1999 ACCESSIONS A29332 REFERENCE A91799 !$#authors Frost, L.S.; Paranchych, W.; Willetts, N.S. !$#journal J. Bacteriol. (1984) 160:395-401 !$#title DNA sequence of the F traALE region that includes the gene !1for F pilin. !$#cross-references MUID:85006817; PMID:6090426 !$#accession A29332 !'##molecule_type DNA !'##residues 1-121 ##label FRO !'##cross-references GB:K01147; NID:g148640; PIDN:AAA24910.1; !1PID:g148644 COMMENT F pili are filamentous surface appendages required for !1cell-to-cell contact during bacterial conjugation. GENETICS !$#gene traA CLASSIFICATION #superfamily fimbrial protein KEYWORDS fimbria; structural protein FEATURE !$1-51 #domain signal sequence #status predicted #label SIG\ !$52-121 #product fimbrial protein #status predicted #label !8MAT SUMMARY #length 121 #molecular-weight 12810 #checksum 2973 SEQUENCE /// ENTRY YQECFX #type complete TITLE fimbrial protein precursor - Escherichia coli plasmid F ALTERNATE_NAMES F pilin ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 24-Sep-1999 ACCESSIONS A23106 REFERENCE A91805 !$#authors Frost, L.S.; Finlay, B.B.; Opgenorth, A.; Paranchych, W.; !1Lee, J.S. !$#journal J. Bacteriol. (1985) 164:1238-1247 !$#title Characterization and sequence analysis of pilin from F-like !1plasmids. !$#cross-references MUID:86059219; PMID:2999074 !$#accession A23106 !'##molecule_type DNA !'##residues 1-121 ##label FRO !'##cross-references GB:K03086; NID:g144694; PIDN:AAA92543.1; !1PID:g144695 COMMENT F pili are filamentous surface appendages required for !1cell-to-cell contact during bacterial conjugation. GENETICS !$#genome plasmid CLASSIFICATION #superfamily fimbrial protein KEYWORDS fimbria; structural protein FEATURE !$1-51 #domain signal sequence #status predicted #label SIG\ !$52-121 #product fimbrial protein #status predicted #label !8MAT SUMMARY #length 121 #molecular-weight 12768 #checksum 2958 SEQUENCE /// ENTRY YQECB2 #type complete TITLE fimbrial protein precursor - Escherichia coli plasmid (ColB2-like) ALTERNATE_NAMES F pilin ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 05-Jan-1996 ACCESSIONS B23106 REFERENCE A91805 !$#authors Frost, L.S.; Finlay, B.B.; Opgenorth, A.; Paranchych, W.; !1Lee, J.S. !$#journal J. Bacteriol. (1985) 164:1238-1247 !$#title Characterization and sequence analysis of pilin from F-like !1plasmids. !$#cross-references MUID:86059219; PMID:2999074 !$#accession B23106 !'##molecule_type DNA !'##residues 1-119 ##label FRO GENETICS !$#genome plasmid CLASSIFICATION #superfamily fimbrial protein KEYWORDS fimbria; structural protein FEATURE !$1-51 #domain signal sequence #status predicted #label SIG\ !$52-119 #product fimbrial protein #status predicted #label !8MAT SUMMARY #length 119 #molecular-weight 12665 #checksum 965 SEQUENCE /// ENTRY YQECR9 #type complete TITLE fimbrial protein precursor - Escherichia coli plasmid R1-19 ALTERNATE_NAMES F pilin; pilin protein traA precursor ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 24-Sep-1999 ACCESSIONS C23106; S03310; D24544; D32014 REFERENCE A91805 !$#authors Frost, L.S.; Finlay, B.B.; Opgenorth, A.; Paranchych, W.; !1Lee, J.S. !$#journal J. Bacteriol. (1985) 164:1238-1247 !$#title Characterization and sequence analysis of pilin from F-like !1plasmids. !$#cross-references MUID:86059219; PMID:2999074 !$#accession C23106 !'##molecule_type DNA !'##residues 1-120 ##label FRO !'##cross-references GB:M19710; GB:M13168; NID:g150857; PIDN:AAA92659.1; !1PID:g150862 REFERENCE S03309 !$#authors Koraimann, G.; Hoegenauer, G. !$#journal Nucleic Acids Res. (1989) 17:1283-1298 !$#title A stable core region of the tra operon mRNA of plasmid !1R1-19. !$#cross-references MUID:89160296; PMID:2564189 !$#accession S03310 !'##molecule_type DNA !'##residues 1-120 ##label KOR !'##cross-references EMBL:X13681; NID:g43119; PIDN:CAA31973.1; !1PID:g43122 !'##experimental_source plasmid R1-19 REFERENCE A24544 !$#authors Finlay, B.B.; Frost, L.S.; Paranchych, W. !$#journal J. Bacteriol. (1986) 166:368-374 !$#title Nucleotide sequences of the R1-19 plasmid transfer genes !1traM, finP, traJ, and traY and the traYZ promoter. !$#cross-references MUID:86195818; PMID:3009392 !$#accession D24544 !'##molecule_type DNA !'##residues 1-36 ##label FIN !'##experimental_source plasmid R1-19 REFERENCE A32014 !$#authors Inamoto, S.; Yoshioka, Y.; Ohtsubo, E. !$#journal J. Bacteriol. (1988) 170:2749-2757 !$#title Identification and characterization of the products from the !1traJ and traY genes of plasmid R100. !$#cross-references MUID:88227859; PMID:2836369 !$#accession D32014 !'##status preliminary !'##molecule_type DNA !'##residues 1-7 ##label INA !'##cross-references GB:M20941; NID:g151778; PIDN:AAA26074.1; !1PID:g151782 !'##experimental_source plasmid R100 GENETICS !$#gene traA !$#genome plasmid CLASSIFICATION #superfamily fimbrial protein KEYWORDS fimbria; structural protein FEATURE !$1-51 #domain signal sequence #status predicted #label SIG\ !$52-120 #product fimbrial protein #status predicted #label !8MAT SUMMARY #length 120 #molecular-weight 12824 #checksum 1472 SEQUENCE /// ENTRY YQECR1 #type complete TITLE fimbrial protein precursor - Escherichia coli plasmid R100-1 ALTERNATE_NAMES F pilin ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 28-May-1999 ACCESSIONS D23106 REFERENCE A91805 !$#authors Frost, L.S.; Finlay, B.B.; Opgenorth, A.; Paranchych, W.; !1Lee, J.S. !$#journal J. Bacteriol. (1985) 164:1238-1247 !$#title Characterization and sequence analysis of pilin from F-like !1plasmids. !$#cross-references MUID:86059219; PMID:2999074 !$#accession D23106 !'##molecule_type DNA !'##residues 1-119 ##label FRO !'##cross-references GB:K03090; NID:g151765; PIDN:AAA92754.1; !1PID:g151766 GENETICS !$#genome plasmid CLASSIFICATION #superfamily fimbrial protein KEYWORDS fimbria; structural protein FEATURE !$1-51 #domain signal sequence #status predicted #label SIG\ !$52-119 #product fimbrial protein #status predicted #label !8MAT SUMMARY #length 119 #molecular-weight 12761 #checksum 1826 SEQUENCE /// ENTRY YQPSPA #type complete TITLE fimbrial protein precursor - Pseudomonas aeruginosa (strain PAK) ALTERNATE_NAMES pilin ORGANISM #formal_name Pseudomonas aeruginosa DATE 14-Nov-1983 #sequence_revision 16-Oct-1998 #text_change 16-Jul-1999 ACCESSIONS A24603; A28780; A03497 REFERENCE A24603 !$#authors Johnson, K.; Parker, M.L.; Lory, S. !$#journal J. Biol. Chem. (1986) 261:15703-15708 !$#title Nucleotide sequence and transcriptional initiation site of !1two Pseudomonas aeruginosa pilin genes. !$#cross-references MUID:87057209; PMID:2430961 !$#accession A24603 !'##molecule_type DNA !'##residues 1-150 ##label JOH !'##cross-references GB:M14849; GB:J02609; NID:g151479; PIDN:AAA25955.1; !1PID:g151480 REFERENCE A28780 !$#authors Pasloske, B.L.; Finlay, B.B.; Paranchych, W. !$#journal FEBS Lett. (1985) 183:408-412 !$#title Cloning and sequencing of the Pseudomonas aeruginosa PAK !1pilin gene. !$#cross-references MUID:85180008; PMID:2985436 !$#accession A28780 !'##molecule_type DNA !'##residues 1-149,'R' ##label PSK !'##cross-references GB:X02402; GB:M11462; NID:g45331; PIDN:CAA26248.1; !1PID:g45332 REFERENCE A03497 !$#authors Sastry, P.A.; Pearlstone, J.R.; Smillie, L.B.; Paranchych, !1W. !$#journal FEBS Lett. (1983) 151:253-256 !$#title Amino acid sequence of pilin isolated from Pseudomonas !1aeruginosa PAK. !$#cross-references MUID:83158129; PMID:6131838 !$#accession A03497 !'##molecule_type protein !'##residues 7-90,'S',91-100,'DTA',104-150 ##label SAS !'##note the pili from which this protein was isolated are polar !1flexible filaments of about 5.4 nanometers diameter and 2.5 !1micrometers average length; they consist of only a single !1polypeptide chain CLASSIFICATION #superfamily gonococcal fimbrial protein KEYWORDS fimbria; methylated amino end; pilin formation FEATURE !$1-6 #domain propeptide #status predicted #label PRO\ !$7-150 #product fimbrial protein #status predicted #label !8MAT\ !$7 #modified_site methylated amino end (Phe) (in mature !8form) #status predicted SUMMARY #length 150 #molecular-weight 15622 #checksum 7700 SEQUENCE /// ENTRY YQNHG #type complete TITLE fimbrial protein class I precursor - Neisseria gonorrhoeae ALTERNATE_NAMES MS11 antigen; pilin ORGANISM #formal_name Neisseria gonorrhoeae DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 16-Jul-1999 ACCESSIONS A94007; A92776; A44149; S13372; C24886; A24886; E24886; !1A03498 REFERENCE A94007 !$#authors Meyer, T.F.; Billyard, E.; Haas, R.; Storzbach, S.; So, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:6110-6114 !$#title Pilus genes of Neisseria gonorrheae: chromosomal !1organization and DNA sequence. !$#cross-references MUID:85014915; PMID:6148752 !$#accession A94007 !'##molecule_type DNA !'##residues 1-166 ##label MEY !'##cross-references GB:K02078; NID:g150284; PIDN:AAA25466.1; !1PID:g150288 !'##experimental_source strain MS11 REFERENCE A92776 !$#authors Schoolnik, G.K.; Fernandez, R.; Tai, J.Y.; Rothbard, J.; !1Gotschlich, E.C. !$#journal J. Exp. Med. (1984) 159:1351-1370 !$#title Gonococcal pili. Primary structure and receptor binding !1domain. !$#cross-references MUID:84187404; PMID:6143785 !$#accession A92776 !'##molecule_type protein !'##residues 8-166 ##label SCH !'##experimental_source strain MS11 !'##note phosphoserine was detected but not located REFERENCE A44149 !$#authors Jonsson, A.B.; Pfeifer, J.; Normark, S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:3204-3208 !$#title Neisseria gonorrhoeae PilC expression provides a selective !1mechanism for structural diversity of pili. !$#cross-references MUID:92228752; PMID:1348857 !$#accession A44149 !'##status preliminary; nucleic acid sequence not shown; not compared !1with conceptual translation !'##molecule_type DNA !'##residues 1-166 ##label JON1 !'##experimental_source strain MS11mk[P+]-u REFERENCE S13372 !$#authors Jonsson, A.B.; Nyberg, G.; Normark, S. !$#journal EMBO J. (1991) 10:477-488 !$#title Phase variation of gonococcal pili by frameshift mutation in !1pilC, a novel gene for pilus assembly. !$#cross-references MUID:91122056; PMID:1671354 !$#accession S13372 !'##status preliminary !'##molecule_type DNA !'##residues 1-166 ##label JON2 REFERENCE A24886 !$#authors Bergstrom, S.; Robbins, K.; Koomey, J.M.; Swanson, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:3890-3894 !$#title Piliation control mechanisms in Neisseria gonorrhoeae. !$#cross-references MUID:86233338; PMID:2872674 !$#accession C24886 !'##molecule_type DNA !'##residues 1-24,'L',26-166 ##label BER1 !'##cross-references GB:M13222; NID:g150290 !'##experimental_source P(-)rp(-) revertant P(+) rev !$#accession A24886 !'##molecule_type DNA !'##residues 1-24,'L',26-60,'N',62,'T',64-68,'A',70-73,'G',75,'S',77, !1'T',79-158,'L',160-166 ##label BER2 !'##cross-references GB:M13222; NID:g150290 !'##experimental_source P(++) !$#accession E24886 !'##molecule_type DNA !'##residues 1-24,'L',26-60,'N',62,'T',64-68,'A',70-85,'QK',88-90,'AK', !193-99,'A',101-102,'N',104-117,'K',119-134,'A',136-166 !1##label BER3 !'##cross-references GB:M13222; NID:g150290 !'##experimental_source P(-)rp(+) revertant P(+) FUNCTION !$#description surface protein that binds various host cell molecules CLASSIFICATION #superfamily gonococcal fimbrial protein KEYWORDS fimbria; glycoprotein; methylated amino end; phosphoprotein; !1surface antigen FEATURE !$1-7 #domain propeptide #status predicted #label PRO\ !$8-166 #product fimbrial protein #status predicted #label !8MAT\ !$31-111 #domain receptor binding #status predicted #label !8RBC\ !$8 #modified_site methylated amino end (Phe) (in mature !8form) #status experimental\ !$101 #binding_site sn-1-glycerolphosphate (Ser) (covalent) !8#status predicted\ !$128-158 #disulfide_bonds #status experimental SUMMARY #length 166 #molecular-weight 17969 #checksum 5651 SEQUENCE /// ENTRY S03091 #type complete TITLE fimbrial protein class I precursor - Neisseria meningitidis ORGANISM #formal_name Neisseria meningitidis DATE 05-Dec-1998 #sequence_revision 05-Dec-1998 #text_change 16-Jul-1999 ACCESSIONS S03091 REFERENCE S03091 !$#authors Potts, W.J.; Saunders, J.R. !$#journal Mol. Microbiol. (1988) 2:647-653 !$#title Nucleotide sequence of the structural gene for class I pilin !1from Neisseria meningitidis: homologies with the pilE locus !1of Neisseria gonorrhoeae. !$#cross-references MUID:89039253; PMID:3141743 !$#accession S03091 !'##molecule_type DNA !'##residues 1-167 ##label POT !'##cross-references EMBL:X07731; NID:g45179; PIDN:CAA30557.1; !1PID:g45180 REFERENCE S68270 !$#authors Stimson, E.; Virji, M.; Barker, S.; Panico, M.; Blench, I.; !1Saunders, J.; Payne, G.; Moxon, E.R.; Dell, A.; Morris, H.R. !$#journal Biochem. J. (1996) 316:29-33 !$#title Discovery of a novel protein modification: !1alpha-glycerophosphate is a substituent of meningococcal !1pilin. !$#cross-references MUID:96235168; PMID:8645220 !$#contents annotation; alpha-glycerophosphate modification GENETICS !$#gene pilE CLASSIFICATION #superfamily gonococcal fimbrial protein KEYWORDS fimbria; glycoprotein; methylated amino end; phosphoprotein; !1surface antigen FEATURE !$1-7 #domain propeptide #status predicted #label PRO\ !$8-167 #product pilin #status predicted #label MAT\ !$8 #modified_site methylated amino end (Phe) (in mature !8form) #status predicted\ !$100 #binding_site sn-1-glycerolphosphate (Ser) (covalent) !8#status experimental\ !$127-160 #disulfide_bonds #status predicted SUMMARY #length 167 #molecular-weight 17776 #checksum 1310 SEQUENCE /// ENTRY YQBZN #type complete TITLE fimbrial protein precursor - Dichelobacter nodosus ALTERNATE_NAMES 198 antigen; pilin ORGANISM #formal_name Dichelobacter nodosus DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 16-Jul-1999 ACCESSIONS A03499; S15258 REFERENCE A03499 !$#authors Elleman, T.C.; Hoyne, P.A. !$#journal J. Bacteriol. (1984) 160:1184-1187 !$#title Nucleotide sequence of the gene encoding pilin of !1Bacteroides nodosus, the causal organism of ovine footrot. !$#cross-references MUID:85054641; PMID:6094507 !$#accession A03499 !'##molecule_type mRNA !'##residues 1-158 ##label ELL !'##cross-references GB:K02662; NID:g145060; PIDN:AAA23345.1; !1PID:g145061 !'##experimental_source strain 198 REFERENCE S15258 !$#authors Mattick, J.S.; Anderson, B.J.; Cox, P.T.; Dalrymple, B.P.; !1Bills, M.M.; Hobbs, M.; Egerton, J.R. !$#journal Mol. Microbiol. (1991) 5:561-573 !$#title Gene sequences and comparison of the fimbrial subunits !1representative of Bacteroides nodosus serotypes A to I: !1class I and class II strains. !$#cross-references MUID:91260440; PMID:1675419 !$#accession S15258 !'##status preliminary !'##molecule_type DNA !'##residues 1-158 ##label MATT !'##cross-references EMBL:X52403; NID:g39663; PIDN:CAA36648.1; !1PID:g39664 CLASSIFICATION #superfamily gonococcal fimbrial protein KEYWORDS fimbria; methylated amino end; surface antigen FEATURE !$1-7 #domain propeptide #status predicted #label PRO\ !$8-158 #product fimbrial protein #status predicted #label !8MAT\ !$8 #modified_site methylated amino end (Phe) (in mature !8form) #status predicted SUMMARY #length 158 #molecular-weight 16863 #checksum 2729 SEQUENCE /// ENTRY YQBZDZ #type complete TITLE fimbrial protein fimZ precursor - Dichelobacter nodosus (serotype D) ORGANISM #formal_name Dichelobacter nodosus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 22-Jan-1999 ACCESSIONS S15249 REFERENCE S15240 !$#authors Hobbs, M.; Dalrymple, B.P.; Cox, P.T.; Livingstone, S.P.; !1Delaney, S.F.; Mattick, J.S. !$#journal Mol. Microbiol. (1991) 5:543-560 !$#title Organization of the fimbrial gene region of Bacteroides !1nodosus: class I and class II strains. !$#cross-references MUID:91260439; PMID:1675418 !$#accession S15249 !'##molecule_type DNA !'##residues 1-159 ##label HOB !'##cross-references EMBL:X52389 !'##note the source is designated as Bacteroides nodosus GENETICS !$#gene fimZ CLASSIFICATION #superfamily gonococcal fimbrial protein KEYWORDS fimbria; methylated amino end FEATURE !$1-6 #domain propeptide #status predicted #label PRO\ !$7-159 #product fimbrial protein fimZ #status predicted !8#label MAT\ !$7 #modified_site methylated amino end (Phe) (in mature !8form) #status predicted SUMMARY #length 159 #molecular-weight 17101 #checksum 970 SEQUENCE /// ENTRY YQBZHZ #type complete TITLE fimbrial protein fimZ precursor - Dichelobacter nodosus (serotype H1) ORGANISM #formal_name Dichelobacter nodosus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS S15251 REFERENCE S15240 !$#authors Hobbs, M.; Dalrymple, B.P.; Cox, P.T.; Livingstone, S.P.; !1Delaney, S.F.; Mattick, J.S. !$#journal Mol. Microbiol. (1991) 5:543-560 !$#title Organization of the fimbrial gene region of Bacteroides !1nodosus: class I and class II strains. !$#cross-references MUID:91260439; PMID:1675418 !$#accession S15251 !'##molecule_type DNA !'##residues 1-159 ##label HOB !'##cross-references EMBL:X52390; NID:g39703; PIDN:CAA36622.1; !1PID:g39707 !'##note the source is designated as Bacteroides nodosus GENETICS !$#gene fimZ CLASSIFICATION #superfamily gonococcal fimbrial protein KEYWORDS fimbria; methylated amino end FEATURE !$1-6 #domain propeptide #status predicted #label PRO\ !$7-159 #product fimbrial protein fimZ #status predicted !8#label MAT\ !$7 #modified_site methylated amino end (Phe) (in mature !8form) #status predicted SUMMARY #length 159 #molecular-weight 17188 #checksum 1276 SEQUENCE /// ENTRY YQBZBI #type complete TITLE fimB protein - Dichelobacter nodosus ORGANISM #formal_name Dichelobacter nodosus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS S15247; S15241; S15244 REFERENCE S15240 !$#authors Hobbs, M.; Dalrymple, B.P.; Cox, P.T.; Livingstone, S.P.; !1Delaney, S.F.; Mattick, J.S. !$#journal Mol. Microbiol. (1991) 5:543-560 !$#title Organization of the fimbrial gene region of Bacteroides !1nodosus: class I and class II strains. !$#cross-references MUID:91260439; PMID:1675418 !$#accession S15247 !'##molecule_type DNA !'##residues 1-257 ##label HOB !'##cross-references EMBL:X52410; NID:g39691; PIDN:CAA36663.1; !1PID:g39694 !'##experimental_source serotype C1 !'##note the source is designated as Bacteroides nodosus !$#accession S15241 !'##molecule_type DNA !'##residues 1-30 ##label HO2 !'##cross-references EMBL:X52404; NID:g39667; PIDN:CAA36651.1; !1PID:g39670 !'##experimental_source serotype B1 !'##note the source is designated as Bacteroides nodosus !$#accession S15244 !'##molecule_type DNA !'##residues 1-48 ##label HO3 !'##cross-references EMBL:X52407; NID:g39679; PIDN:CAA36657.1; !1PID:g39682 !'##note the source is designated as Bacteroides nodosus GENETICS !$#gene fimB CLASSIFICATION #superfamily fimB protein KEYWORDS fimbria SUMMARY #length 257 #molecular-weight 29623 #checksum 7446 SEQUENCE /// ENTRY YQBZE1 #type complete TITLE fimB protein - Dichelobacter nodosus (serotype E1) ORGANISM #formal_name Dichelobacter nodosus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS S15252 REFERENCE S15240 !$#authors Hobbs, M.; Dalrymple, B.P.; Cox, P.T.; Livingstone, S.P.; !1Delaney, S.F.; Mattick, J.S. !$#journal Mol. Microbiol. (1991) 5:543-560 !$#title Organization of the fimbrial gene region of Bacteroides !1nodosus: class I and class II strains. !$#cross-references MUID:91260439; PMID:1675418 !$#accession S15252 !'##molecule_type DNA !'##residues 1-257 ##label HOB !'##cross-references EMBL:M32230; NID:g145054; PIDN:AAA23343.1; !1PID:g145056 !'##note the source is designated as Bacteroides nodosus GENETICS !$#gene fimB CLASSIFICATION #superfamily fimB protein KEYWORDS fimbria SUMMARY #length 257 #molecular-weight 29521 #checksum 8888 SEQUENCE /// ENTRY C64532 #type complete TITLE methyl-accepting chemotaxis protein (tlpA) - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C64532 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession C64532 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-675 ##label TOM !'##cross-references GB:AE000531; GB:AE000511; NID:g2313173; !1PIDN:AAD07167.1; PID:g2313179; TIGR:HP0099 GENETICS !$#start_codon TTG CLASSIFICATION #superfamily probable methyl-accepting chemotaxis transducer SUMMARY #length 675 #molecular-weight 74465 #checksum 614 SEQUENCE /// ENTRY B64530 #type complete TITLE methyl-accepting chemotaxis transducer (tlpC) - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B64530 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession B64530 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-673 ##label TOM !'##cross-references GB:AE000530; GB:AE000511; NID:g2313162; !1PIDN:AAD07152.1; PID:g2313163; TIGR:HP0082 CLASSIFICATION #superfamily probable methyl-accepting chemotaxis transducer SUMMARY #length 673 #molecular-weight 75213 #checksum 6625 SEQUENCE /// ENTRY YQBZCD #type complete TITLE fimC protein - Dichelobacter nodosus (serotype D) ORGANISM #formal_name Dichelobacter nodosus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 31-Mar-1993 ACCESSIONS S15248 REFERENCE S15240 !$#authors Hobbs, M.; Dalrymple, B.P.; Cox, P.T.; Livingstone, S.P.; !1Delaney, S.F.; Mattick, J.S. !$#journal Mol. Microbiol. (1991) 5:543-560 !$#title Organization of the fimbrial gene region of Bacteroides !1nodosus: class I and class II strains. !$#cross-references MUID:91260439; PMID:1675418 !$#accession S15248 !'##molecule_type DNA !'##residues 1-244 ##label HOB !'##cross-references EMBL:X52389 !'##note the source is designated as Bacteroides nodosus GENETICS !$#gene fimC CLASSIFICATION #superfamily fimC protein KEYWORDS fimbria SUMMARY #length 244 #molecular-weight 28026 #checksum 8618 SEQUENCE /// ENTRY YQBZCH #type complete TITLE fimC protein - Dichelobacter nodosus (serotype H1) ORGANISM #formal_name Dichelobacter nodosus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS S15250 REFERENCE S15240 !$#authors Hobbs, M.; Dalrymple, B.P.; Cox, P.T.; Livingstone, S.P.; !1Delaney, S.F.; Mattick, J.S. !$#journal Mol. Microbiol. (1991) 5:543-560 !$#title Organization of the fimbrial gene region of Bacteroides !1nodosus: class I and class II strains. !$#cross-references MUID:91260439; PMID:1675418 !$#accession S15250 !'##molecule_type DNA !'##residues 1-244 ##label HOB !'##cross-references EMBL:X52390; NID:g39703; PIDN:CAA36620.1; !1PID:g39705 !'##note the source is designated as Bacteroides nodosus GENETICS !$#gene fimC CLASSIFICATION #superfamily fimC protein KEYWORDS fimbria SUMMARY #length 244 #molecular-weight 27960 #checksum 1446 SEQUENCE /// ENTRY YQBZDH #type complete TITLE fimD protein - Dichelobacter nodosus (serotype H1) ORGANISM #formal_name Dichelobacter nodosus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS S15255 REFERENCE S15240 !$#authors Hobbs, M.; Dalrymple, B.P.; Cox, P.T.; Livingstone, S.P.; !1Delaney, S.F.; Mattick, J.S. !$#journal Mol. Microbiol. (1991) 5:543-560 !$#title Organization of the fimbrial gene region of Bacteroides !1nodosus: class I and class II strains. !$#cross-references MUID:91260439; PMID:1675418 !$#accession S15255 !'##molecule_type DNA !'##residues 1-394 ##label HOB !'##cross-references EMBL:X52390; NID:g39703; PIDN:CAA36621.1; !1PID:g580812 !'##note the source is designated as Bacteroides nodosus GENETICS !$#gene fimD !$#start_codon GTG CLASSIFICATION #superfamily fimD protein KEYWORDS fimbria SUMMARY #length 394 #molecular-weight 45105 #checksum 2838 SEQUENCE /// ENTRY A33491 #type complete TITLE chaperone protein papD precursor - Escherichia coli ORGANISM #formal_name Escherichia coli DATE 27-Feb-1990 #sequence_revision 02-Dec-1994 #text_change 16-Jul-1999 ACCESSIONS A33491; A28987; S25219; S16398 REFERENCE A33491 !$#authors Lindberg, F.; Tennent, J.M.; Hultgren, S.J.; Lund, B.; !1Normark, S. !$#journal J. Bacteriol. (1989) 171:6052-6058 !$#title PapD, a periplasmic transport protein in P-pilus biogenesis. !$#cross-references MUID:90036691; PMID:2572580 !$#accession A33491 !'##molecule_type DNA !'##residues 1-239 ##label LIN !'##cross-references GB:Y00529; GB:M30806 REFERENCE A28987 !$#authors Lindberg, F.P. !$#citation Ph.D. thesis, Umea University, 1987, cited by Holmgren, A., !1and Braenden, C.I., Nature 342, 248-251, 1989 !$#description Crystal structure of chaperone protein PapD reveals an !1immunoglobulin fold. !$#accession A28987 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-80,'D',82-239 ##label HOL REFERENCE A44668 !$#authors Holmgren, A.; Branden, C.I. !$#journal Nature (1989) 342:248 !$#title Crystal structure of chaperone protein papD reveals an !1immunoglobulin fold. !$#cross-references MUID:90044096; PMID:2478891 !$#contents annotation; X-ray crystallography, 2.5 angstroms REFERENCE S25205 !$#authors Marklund, B.I.; Tennent, J.M.; Garcia, E.; Hamers, A.; Baga, !1M.; Lindberg, F.; Gaastra, W.; Normark, S. !$#journal Mol. Microbiol. (1992) 6:2225-2242 !$#title Horizontal gene transfer of the Escherichia coli pap and prs !1pili operons as a mechanism for the development of !1tissue-specific adhesive properties. !$#cross-references MUID:93023852; PMID:1357526 !$#accession S25219 !'##molecule_type DNA !'##residues 1-239 ##label MAR !'##cross-references EMBL:X61239; NID:g42290; PIDN:CAA43565.1; !1PID:g42296 !'##experimental_source strain J96 GENETICS !$#gene papD FUNCTION !$#description mediates the assembly of pili on the surface of E. coli by !1forming soluble multimeric complexes with pili subunits as !1an intermediate step in the assembly process CLASSIFICATION #superfamily chaperone protein papD KEYWORDS molecular chaperone FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-239 #product chaperone protein papD #status experimental !8#label MAT\ !$228-233 #disulfide_bonds #status predicted SUMMARY #length 239 #molecular-weight 26803 #checksum 6549 SEQUENCE /// ENTRY S36632 #type complete TITLE molecular chaperone fimC - Salmonella typhi ALTERNATE_NAMES fimbrial protein fimC ORGANISM #formal_name Salmonella typhi DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S36632 REFERENCE S36632 !$#authors Rossolini, G.M.; Muscas, P.; Chiesurin, A.; Satta, G. !$#submission submitted to the EMBL Data Library, August 1993 !$#accession S36632 !'##molecule_type DNA !'##residues 1-237 ##label ROS !'##cross-references EMBL:X74602; NID:g397532; PIDN:CAA52682.1; !1PID:g397533 !'##experimental_source strain Sty4 GENETICS !$#gene fimC CLASSIFICATION #superfamily chaperone protein papD KEYWORDS molecular chaperone SUMMARY #length 237 #molecular-weight 25823 #checksum 328 SEQUENCE /// ENTRY S56541 #type complete TITLE chaperone protein (involved in biogenesis of type 1 fimbriae) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS S56541; F65245; S53067; A47510 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56541 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-241 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97212.1; !1PID:g537157 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65245 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-241 ##label BLAT !'##cross-references GB:AE000502; GB:U00096; NID:g2367374; !1PIDN:AAC77272.1; PID:g1790771; UWGP:b4316 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S53063 !$#authors Marc, D.; Dho-Moulin, M. !$#submission submitted to the EMBL Data Library, September 1994 !$#description Hypervariable sites within the major subunit of type 1 !1fimbriae, identified through analysis of the fim gene !1cluster of an avian pathogenic strain of Escherichia coli. !$#accession S53067 !'##status preliminary !'##molecule_type DNA !'##residues 1-28,'V',30-53,'V',55-209,'A',211-241 ##label MAR !'##cross-references EMBL:Z37500; NID:g732680; PIDN:CAA85729.1; !1PID:g732685 REFERENCE A47510 !$#authors Jones, C.H.; Pinkner, J.S.; Nicholes, A.V.; Slonim, L.N.; !1Abraham, S.N.; Hultgren, S.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:8397-8401 !$#title FimC is a periplasmic PapD-like chaperone that directs !1assembly of type 1 pili in bacteria. !$#cross-references MUID:93391362; PMID:8104335 !$#contents ORN103 !$#accession A47510 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 37-53,'V',55-209,'A',211-241 ##label JON !'##note sequence extracted from NCBI backbone (NCBIP:137585) GENETICS !$#gene fimC !$#start_codon GTG CLASSIFICATION #superfamily chaperone protein papD KEYWORDS molecular chaperone SUMMARY #length 241 #molecular-weight 26689 #checksum 642 SEQUENCE /// ENTRY C65104 #type complete TITLE hypothetical 25.7 kD fimbrial chaperone in agai- mtr intergeni - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS C65104 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65104 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-231 ##label BLAT !'##cross-references GB:AE000395; GB:U00096; NID:g1789524; !1PIDN:AAC76177.1; PID:g1789532; UWGP:b3143 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yraI CLASSIFICATION #superfamily chaperone protein papD SUMMARY #length 231 #molecular-weight 25676 #checksum 3896 SEQUENCE /// ENTRY B56271 #type complete TITLE long polar fimbrial chaperone - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B56271 REFERENCE A56271 !$#authors Baeumler, A.J.; Heffron, F. !$#journal J. Bacteriol. (1995) 177:2087-2097 !$#title Identification and sequence analysis of lpfABCDE, a putative !1fimbrial operon of Salmonella typhimurium. !$#cross-references MUID:95238281; PMID:7721701 !$#accession B56271 !'##status preliminary !'##molecule_type DNA !'##residues 1-232 ##label BAE !'##cross-references GB:U18559; NID:g829370; PIDN:AAA73967.1; !1PID:g829372 GENETICS !$#gene lpfB CLASSIFICATION #superfamily chaperone protein papD KEYWORDS molecular chaperone SUMMARY #length 232 #molecular-weight 25489 #checksum 7724 SEQUENCE /// ENTRY S24978 #type complete TITLE fimbrial protein hifB - Haemophilus influenzae (strain b) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S24978 REFERENCE S24978 !$#authors Smith, A.L.; Forney, L.; Chanyangam, M. !$#submission submitted to the EMBL Data Library, June 1992 !$#description hif B of H. influenzae is a member of the chaperone family. !$#accession S24978 !'##molecule_type DNA !'##residues 1-241 ##label SMI !'##cross-references EMBL:X66606; NID:g43571; PIDN:CAA47175.1; !1PID:g43572 !'##experimental_source strain b, isolate R1369 GENETICS !$#gene hifB CLASSIFICATION #superfamily chaperone protein papD SUMMARY #length 241 #molecular-weight 26602 #checksum 1363 SEQUENCE /// ENTRY C39142 #type complete TITLE mrkB protein precursor - Klebsiella pneumoniae ORGANISM #formal_name Klebsiella pneumoniae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C39142 REFERENCE A39142 !$#authors Allen, B.L.; Gerlach, G.F.; Clegg, S. !$#journal J. Bacteriol. (1991) 173:916-920 !$#title Nucleotide sequence and functions of mrk determinants !1necessary for expression of type 3 fimbriae in Klebsiella !1pneumoniae. !$#cross-references MUID:91100388; PMID:1670938 !$#accession C39142 !'##status preliminary !'##molecule_type DNA !'##residues 1-233 ##label ALL !'##cross-references GB:M55912; NID:g149234; PIDN:AAA25094.1; !1PID:g149237 CLASSIFICATION #superfamily chaperone protein papD SUMMARY #length 233 #molecular-weight 25143 #checksum 5271 SEQUENCE /// ENTRY S45209 #type complete TITLE pili assembly chaperone ecpD precursor, periplasmic - Escherichia coli (strain K-12) ALTERNATE_NAMES fimbriae biogenesis protein homolog ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS S45209; D64737; A53303 REFERENCE S45181 !$#authors Fujita, N. !$#submission submitted to the EMBL Data Library, January 1994 !$#accession S45209 !'##molecule_type DNA !'##residues 1-246 ##label FUJ !'##cross-references EMBL:D26562; NID:g473770; PIDN:BAA05588.1; !1PID:g473799 !'##experimental_source strain K-12, substrain W3110 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64737 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-246 ##label BLAT !'##cross-references GB:AE000123; GB:U00096; NID:g1786327; !1PIDN:AAC73251.1; PID:g1786333; UWGP:b0140 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A53303 !$#authors Raina, S.; Missiakas, D.; Baird, L.; Kumar, S.; !1Georgopoulos, C. !$#journal J. Bacteriol. (1993) 175:5009-5021 !$#title Identification and transcriptional analysis of the !1Escherichia coli htrE operon which is homologous to pap and !1related pilin operons. !$#cross-references MUID:93352405; PMID:8102362 !$#accession A53303 !'##status preliminary !'##molecule_type DNA !'##residues 1-78,'R',80-109,'RA',112-246 ##label RAI !'##cross-references GB:L00680; NID:g385210; PIDN:AAA23720.1; !1PID:g385211 GENETICS !$#gene ecpD FUNCTION !$#description molecular chaperone involved in pili assembly CLASSIFICATION #superfamily chaperone protein papD SUMMARY #length 246 #molecular-weight 27054 #checksum 1023 SEQUENCE /// ENTRY E64978 #type complete TITLE hypothetical 26.6 kD fimbrial chaperone in mrp 5'region - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS E64978 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64978 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-239 ##label BLAT !'##cross-references GB:AE000300; GB:U00096; NID:g1788425; !1PIDN:AAC75171.1; PID:g1788428; UWGP:b2110 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yehC CLASSIFICATION #superfamily chaperone protein papD SUMMARY #length 239 #molecular-weight 26589 #checksum 3579 SEQUENCE /// ENTRY A55853 #type complete TITLE chaperone protein aggD precursor - Escherichia coli ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A55853 REFERENCE A55853 !$#authors Savarino, S.J.; Fox, P.; Yikang, D.; Nataro, J.P. !$#journal J. Bacteriol. (1994) 176:4949-4957 !$#title Identification and characterization of a gene cluster !1mediating enteroaggregative Escherichia coli aggregative !1adherence fimbria I biogenesis. !$#cross-references MUID:94327462; PMID:7914189 !$#accession A55853 !'##status preliminary !'##molecule_type DNA !'##residues 1-252 ##label SAV !'##cross-references GB:U12894; NID:g531396; PIDN:AAA57451.1; !1PID:g531397 GENETICS !$#gene aggD CLASSIFICATION #superfamily chaperone protein papD KEYWORDS molecular chaperone SUMMARY #length 252 #molecular-weight 28161 #checksum 8350 SEQUENCE /// ENTRY S16965 #type complete TITLE probable chaperone precursor - Yersinia pestis ORGANISM #formal_name Yersinia pestis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S16965 REFERENCE S16965 !$#authors Galyov, E.E.; Karlishev, A.V.; Chernovskaya, T.V.; Dolgikh, !1D.A.; Smirnov, O.Y.; Volkovoy, K.I.; Abramov, V.M.; !1Zavyalov, V.P. !$#journal FEBS Lett. (1991) 286:79-82 !$#title Expression of the envelope antigen F1 of Yersinia pestis is !1mediated by the product of caf1M gene having homology with !1the chaperone protein PapD of Escherichia coli. !$#cross-references MUID:91323540; PMID:1677900 !$#accession S16965 !'##molecule_type DNA !'##residues 1-258 ##label GAL !'##cross-references EMBL:X61996; NID:g48620; PIDN:CAA43967.1; !1PID:g1072424 GENETICS !$#gene caf1M CLASSIFICATION #superfamily chaperone protein papD KEYWORDS molecular chaperone FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-258 #product probable chaperone #status predicted #label !8MAT\ !$121-160 #disulfide_bonds #status predicted SUMMARY #length 258 #molecular-weight 28765 #checksum 9616 SEQUENCE /// ENTRY B40618 #type complete TITLE fimbrial periplasmic chaperone protein homolog SefB - Salmonella enteritidis ORGANISM #formal_name Salmonella enteritidis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B40618 REFERENCE A40618 !$#authors Clouthier, S.C.; Muller, K.H.; Doran, J.L.; Collinson, S.K.; !1Kay, W.W. !$#journal J. Bacteriol. (1993) 175:2523-2533 !$#title Characterization of three fimbrial genes, sefABC, of !1Salmonella enteritidis. !$#cross-references MUID:93239677; PMID:8097515 !$#contents 27655-3b !$#accession B40618 !'##status preliminary !'##molecule_type DNA !'##residues 1-246 ##label CLO !'##cross-references GB:L11009; NID:g310647; PIDN:AAA27220.1; !1PID:g310648 !'##note sequence extracted from NCBI backbone (NCBIN:130387, !1NCBIP:130396) CLASSIFICATION #superfamily chaperone protein papD SUMMARY #length 246 #molecular-weight 28030 #checksum 5954 SEQUENCE /// ENTRY F65006 #type complete TITLE hypothetical protein b2336 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS F65006 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65006 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-250 ##label BLAT !'##cross-references GB:AE000322; GB:U00096; NID:g1788672; !1PIDN:AAC75396.1; PID:g1788677; UWGP:b2336 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily chaperone protein papD SUMMARY #length 250 #molecular-weight 27728 #checksum 1861 SEQUENCE /// ENTRY D64807 #type complete TITLE probable molecular chaperone ybgP - Escherichia coli (strain K-12) ALTERNATE_NAMES probable fimbrial chaperone ybgP ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS D64807 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64807 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-242 ##label BLAT !'##cross-references GB:AE000175; GB:U00096; NID:g1786934; !1PIDN:AAC73811.1; PID:g1786936; UWGP:b0717 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ybgP CLASSIFICATION #superfamily chaperone protein papD KEYWORDS molecular chaperone SUMMARY #length 242 #molecular-weight 26954 #checksum 394 SEQUENCE /// ENTRY G64834 #type complete TITLE probable fimbrial chaperone precursor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS G64834 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64834 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-245 ##label BLAT !'##cross-references GB:AE000196; GB:U00096; NID:g1787169; !1PIDN:AAC74030.1; PID:g1787176; UWGP:b0944 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ycbF CLASSIFICATION #superfamily chaperone protein papD KEYWORDS fimbria; membrane protein; molecular chaperone; periplasmic !1space FEATURE !$1-35 #domain signal sequence #status predicted #label SIG\ !$36-245 #product probable fimbrial chaperone #status !8predicted #label MAT\ !$82-98 #domain transmembrane #status predicted #label TMM SUMMARY #length 245 #molecular-weight 26982 #checksum 1251 SEQUENCE /// ENTRY I83349 #type complete TITLE CS6 subunits chaperone - Escherichia coli ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS I83349 REFERENCE I60266 !$#authors Willshaw, G.A.; Smith, H.R.; McConnell, M.M.; Rowe, B. !$#journal FEMS Microbiol. Lett. (1988) 49:473-478 !$#title Cloning of genes encoding coli-surface (CS) antigens in !1enterotoxigenic Escherichia coli. !$#accession I83349 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-232 ##label RES !'##cross-references EMBL:U04844; NID:g442375; PIDN:AAC45095.1; !1PID:g442378 CLASSIFICATION #superfamily chaperone protein papD KEYWORDS molecular chaperone SUMMARY #length 232 #molecular-weight 26832 #checksum 1296 SEQUENCE /// ENTRY YQECPE #type complete TITLE fimbrial protein papE precursor - Escherichia coli ALTERNATE_NAMES prsE protein ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jul-1999 ACCESSIONS A25134; A27743; S25222; S25227; S16401; S16406 REFERENCE A25134 !$#authors Lindberg, F.; Lund, B.; Normark, S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:1891-1895 !$#title Gene products specifying adhesion of uropathogenic !1Escherichia coli are minor components of pili. !$#cross-references MUID:86149403; PMID:2869489 !$#accession A25134 !'##molecule_type DNA !'##residues 1-173 ##label LIN !'##cross-references EMBL:M13239; NID:g147074; PIDN:AAA24280.1; !1PID:g147075 REFERENCE A27743 !$#authors Lund, B.; Lindberg, F.; Normark, S. !$#journal J. Bacteriol. (1988) 170:1887-1894 !$#title Structure and antigenic properties of the tip-located P !1pilus proteins of uropathogenic Escherichia coli. !$#cross-references MUID:88169520; PMID:2895103 !$#accession A27743 !'##molecule_type DNA !'##residues 1-173 ##label LUN !'##cross-references EMBL:M13239; NID:g147074; PIDN:AAA24280.1; !1PID:g147075 REFERENCE S25205 !$#authors Marklund, B.I.; Tennent, J.M.; Garcia, E.; Hamers, A.; Baga, !1M.; Lindberg, F.; Gaastra, W.; Normark, S. !$#journal Mol. Microbiol. (1992) 6:2225-2242 !$#title Horizontal gene transfer of the Escherichia coli pap and prs !1pili operons as a mechanism for the development of !1tissue-specific adhesive properties. !$#cross-references MUID:93023852; PMID:1357526 !$#accession S25222 !'##molecule_type DNA !'##residues 1-173 ##label MAR !'##cross-references EMBL:X61239; NID:g42290; PIDN:CAA43568.1; !1PID:g42299 !'##experimental_source strain J96 !$#accession S25227 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-173 ##label MA2 !'##cross-references EMBL:X61238; NID:g42526; PIDN:CAA43556.1; !1PID:g42527 !'##experimental_source strain J96 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1991 COMMENT This protein is one of the minor components of pili. Pili !1with a defective papE gene will have low adhesive capacity !1or none; however, the binding property of the whole cell !1will not be affected. GENETICS !$#gene papE; prsE CLASSIFICATION #superfamily papE fimbrial protein KEYWORDS fimbria; pili adhesion FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-173 #product fimbrial protein papE #status predicted !8#label MAT SUMMARY #length 173 #molecular-weight 18569 #checksum 4728 SEQUENCE /// ENTRY YQECPF #type complete TITLE fimbrial protein papF - Escherichia coli ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jul-1999 ACCESSIONS B25134; S16402; S25223 REFERENCE A25134 !$#authors Lindberg, F.; Lund, B.; Normark, S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:1891-1895 !$#title Gene products specifying adhesion of uropathogenic !1Escherichia coli are minor components of pili. !$#cross-references MUID:86149403; PMID:2869489 !$#accession B25134 !'##molecule_type DNA !'##residues 1-167 ##label LIN !'##cross-references GB:M13239; NID:g147074; PIDN:AAA24281.1; !1PID:g147076 REFERENCE S16393 !$#authors Marklund, B.I.H. !$#submission submitted to the EMBL Data Library, August 1991 !$#accession S16402 !'##molecule_type DNA !'##residues 1-167 ##label MAR !'##cross-references EMBL:X61239; NID:g42290; PIDN:CAA43569.1; !1PID:g42300 REFERENCE S25205 !$#authors Marklund, B.I.; Tennent, J.M.; Garcia, E.; Hamers, A.; Baga, !1M.; Lindberg, F.; Gaastra, W.; Normark, S. !$#journal Mol. Microbiol. (1992) 6:2225-2242 !$#title Horizontal gene transfer of the Escherichia coli pap and prs !1pili operons as a mechanism for the development of !1tissue-specific adhesive properties. !$#cross-references MUID:93023852; PMID:1357526 !$#accession S25223 !'##molecule_type DNA !'##residues 1-167 ##label MA2 !'##cross-references EMBL:X61239; NID:g42290; PIDN:CAA43569.1; !1PID:g42300 !'##experimental_source strain J96 COMMENT The papF and papG genes are required for !1digalactoside-specific adhesion but surface-localized pili !1can be made without them. GENETICS !$#gene papF CLASSIFICATION #superfamily papF fimbrial protein KEYWORDS fimbria; pili adhesion SUMMARY #length 167 #molecular-weight 17625 #checksum 4855 SEQUENCE /// ENTRY KONH0 #type fragments TITLE opacity protein opaC precursor - Neisseria gonorrhoeae (strain MS11) (fragments) ALTERNATE_NAMES opacity protein V0; triosephosphate dehydrogenase ORGANISM #formal_name Neisseria gonorrhoeae #variety strain MS11 DATE 31-Mar-1989 #sequence_revision 17-Oct-1997 #text_change 16-Jul-1999 ACCESSIONS S16618; A24429; S36328; S28621 REFERENCE S16610 !$#authors Bhat, K.S.; Gibbs, C.P.; Barrera, O.; Morrison, S.G.; !1Jaehnig, F.; Stern, A.; Kupsch, E.M.; Meyer, T.F.; Swanson, !1J. !$#journal Mol. Microbiol. (1991) 5:1889-1901 !$#title The opacity proteins of Neisseria gonorrhoeae strain MS11 !1are encoded by a family of 11 complete genes. !$#cross-references MUID:92114767; PMID:1815562 !$#accession S16618 !'##molecule_type DNA !'##residues 1-260 ##label BHA !'##cross-references EMBL:X52370 !'##experimental_source strain MS11, variant 4.8 !'##note the authors translated the codon CCA for residue 32 as Thr !'##note the authors did not translate the sequence for the signal !1peptide !'##note expression of opacity proteins is regulated by the number of !1translated repeat elements CTCTT, which code for part of the !1signal sequence; the protein can only be synthesized when !1the number of repeats place the start codon in frame with !1the rest of the protein REFERENCE A90887 !$#authors Stern, A.; Brown, M.; Nickel, P.; Meyer, T.F. !$#journal Cell (1986) 47:61-71 !$#title Opacity genes in Neisseria gonorrhoeae: control of phase and !1antigenic variation. !$#cross-references MUID:87002493; PMID:3093085 !$#accession A24429 !'##molecule_type DNA !'##residues 25-260 ##label STE !'##note this protein is synthesized as a precursor; however, the !1authors are uncertain as to which start codon is used in !1translation; the amino end of the mature protein was !1confirmed by protein sequencing REFERENCE S36328 !$#authors Kupsch, E.M.; Knepper, B.; Kuroki, T.; Heuer, I.; Meyer, !1T.F. !$#journal EMBO J. (1993) 12:641-650 !$#title Variable opacity (Opa) outer membrane proteins account for !1the cell tropisms displayed by Neisseria gonorrhoeae for !1human leukocytes and epithelial cells. !$#cross-references MUID:93178439; PMID:8440254 !$#accession S36328 !'##status preliminary !'##molecule_type DNA !'##residues 25-260 ##label KUP !'##cross-references EMBL:Z18927; NID:g49323; PIDN:CAA79360.1; !1PID:g940789 REFERENCE S28617 !$#authors Meyer, T.F. !$#submission submitted to the EMBL Data Library, November 1992 !$#accession S28621 !'##molecule_type DNA !'##residues 25-260 ##label MEY !'##cross-references EMBL:Z18927; NID:g49323; PIDN:CAA79360.1; !1PID:g940789 GENETICS !$#gene opaC CLASSIFICATION #superfamily opacity protein KEYWORDS cell surface component; transmembrane protein FEATURE !$1-11,12-24 #domain signal sequence (fragments) #status predicted !8#label SIG\ !$25-260 #product opacity protein opaC #status predicted !8#label MAT\ !$35-43 #domain transmembrane #status predicted #label TM1\ !$44-75 #domain extracellular #status predicted #label EXT1\ !$52-61 #region semivariable region\ !$76-84 #domain transmembrane #status predicted #label TM2\ !$89-95 #domain transmembrane #status predicted #label TM3\ !$96-134 #domain extracellular #status predicted #label EXT2\ !$102-129 #region hypervariable region HV1\ !$135-149 #domain transmembrane #status predicted #label TM4\ !$155-165 #domain transmembrane #status predicted #label TM5\ !$166-211 #domain extracellular #status predicted #label EXT3\ !$171-217 #region hypervariable region HV2\ !$212-224 #domain transmembrane #status predicted #label TM6\ !$228-236 #domain transmembrane #status predicted #label TM7\ !$237-251 #domain extracellular #status predicted #label EXT4\ !$252-260 #domain transmembrane #status predicted #label TM8 SUMMARY #length 260 #checksum 9419 SEQUENCE /// ENTRY KONH8 #type fragment TITLE opacity protein V28 - Neisseria gonorrhoeae (fragment) ORGANISM #formal_name Neisseria gonorrhoeae DATE 31-Mar-1989 #sequence_revision 17-Oct-1997 #text_change 17-Oct-1997 ACCESSIONS B24429 REFERENCE A90887 !$#authors Stern, A.; Brown, M.; Nickel, P.; Meyer, T.F. !$#journal Cell (1986) 47:61-71 !$#title Opacity genes in Neisseria gonorrhoeae: control of phase and !1antigenic variation. !$#cross-references MUID:87002493; PMID:3093085 !$#accession B24429 !'##molecule_type DNA !'##residues 1-234 ##label STE !'##note this protein is synthesized as a precursor; however, the !1authors are uncertain as to which start codon is used in !1translation; the amino end of the mature protein was !1confirmed by protein sequencing !'##note expression of opacity proteins is regulated by the number of !1translated repeat elements CTCTT, which code for part of the !1signal sequence; the protein can only be synthesized when !1the number of repeats place the start codon in frame with !1the rest of the protein GENETICS !$#gene opaV28 CLASSIFICATION #superfamily opacity protein KEYWORDS cell surface component; transmembrane protein FEATURE !$1-234 #product opacity protein opaV28 #status predicted !8#label MAT\ !$11-19 #domain transmembrane #status predicted #label TM1\ !$20-51 #domain extracellular #status predicted #label EXT1\ !$28-37 #region semivariable region\ !$52-60 #domain transmembrane #status predicted #label TM2\ !$65-71 #domain transmembrane #status predicted #label TM3\ !$72-108 #domain extracellular #status predicted #label EXT2\ !$78-103 #region hypervariable region HV1\ !$109-123 #domain transmembrane #status predicted #label TM4\ !$129-139 #domain transmembrane #status predicted #label TM5\ !$140-185 #domain extracellular #status predicted #label EXT3\ !$145-191 #region hypervariable region HV2\ !$186-198 #domain transmembrane #status predicted #label TM6\ !$202-210 #domain transmembrane #status predicted #label TM7\ !$211-225 #domain extracellular #status predicted #label EXT4\ !$226-234 #domain transmembrane #status predicted #label TM8 SUMMARY #length 234 #checksum 2691 SEQUENCE /// ENTRY KONH2C #type fragments TITLE opacity protein P.IIc precursor - Neisseria gonorrhoeae (strain JS3) (fragments) ALTERNATE_NAMES outer membrane protein P.IIc ORGANISM #formal_name Neisseria gonorrhoeae #variety strain JS3 DATE 31-Mar-1992 #sequence_revision 17-Oct-1997 #text_change 08-May-1998 ACCESSIONS S03095; S16360 REFERENCE S03095 !$#authors van der Ley, P. !$#journal Mol. Microbiol. (1988) 2:797-806 !$#title Three copies of a single protein II-encoding sequence in the !1genome of Neisseria gonorrhoeae JS3: evidence for gene !1conversion and gene duplication. !$#cross-references MUID:89096501; PMID:3145386 !$#accession S03095 !'##molecule_type DNA !'##residues 1-268 ##label VAN !'##cross-references EMBL:X12625 !'##experimental_source strain JS3 !'##note 241-Val was also found !'##note expression of opacity proteins is regulated by the number of !1translated repeat elements CTCTT, which code for part of the !1signal sequence; the protein can only be synthesized when !1the number of repeats place the start codon in frame with !1the rest of the protein REFERENCE S16360 !$#authors Barritt, D.S.; Schwalbe, R.S.; Klapper, D.G.; Cannon, J.G. !$#journal Infect. Immun. (1987) 55:2026-2031 !$#title Antigenic and structural differences among six proteins II !1expressed by a single strain of Neisseria gonorrhoeae. !$#cross-references MUID:87306843; PMID:3114142 !$#accession S16360 !'##status preliminary !'##molecule_type protein !'##residues 24-34 ##label BAR GENETICS !$#gene PIIc CLASSIFICATION #superfamily opacity protein KEYWORDS cell surface component; transmembrane protein FEATURE !$1-10,11-23 #domain signal sequence (fragments) #status predicted !8#label SIG\ !$24-268 #product opacity protein P.IIc #status experimental !8#label MAT\ !$34-42 #domain transmembrane #status predicted #label TM1\ !$43-74 #domain extracellular #status predicted #label EXT1\ !$51-60 #region semivariable region\ !$75-83 #domain transmembrane #status predicted #label TM2\ !$88-94 #domain transmembrane #status predicted #label TM3\ !$95-140 #domain extracellular #status predicted #label EXT2\ !$101-135 #region hypervariable region HV1\ !$141-155 #domain transmembrane #status predicted #label TM4\ !$161-171 #domain transmembrane #status predicted #label TM5\ !$172-219 #domain extracellular #status predicted #label EXT3\ !$177-225 #region hypervariable region HV2\ !$220-232 #domain transmembrane #status predicted #label TM6\ !$236-244 #domain transmembrane #status predicted #label TM7\ !$245-259 #domain extracellular #status predicted #label EXT4\ !$260-268 #domain transmembrane #status predicted #label TM8 SUMMARY #length 268 #checksum 4200 SEQUENCE /// ENTRY QVSAA #type complete TITLE protein A precursor - Staphylococcus aureus ORGANISM #formal_name Staphylococcus aureus DATE 28-Feb-1986 #sequence_revision 18-Mar-1997 #text_change 16-Jul-1999 ACCESSIONS A58531; A03500; A19498 REFERENCE A58531 !$#authors Uhlen, M.; Guss, B.; Nilsson, B.; Gatenbeck, S.; Philipson, !1L.; Lindberg, M. !$#journal J. Biol. Chem. (1984) 259:13628 !$#contents correction to A03500 !$#accession A58531 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-524 ##label UHL1 !'##cross-references GB:J01786; NID:g153103; PIDN:AAA26676.1; !1PID:g153104 !'##note a single base omission is noted; the complete translation is !1not shown REFERENCE A03500 !$#authors Uhlen, M.; Guss, B.; Nilsson, B.; Gatenbeck, S.; Philipson, !1L.; Lindberg, M. !$#journal J. Biol. Chem. (1984) 259:1695-1702 !$#title Complete sequence of the staphylococcal gene encoding !1protein A. A gene evolved through multiple duplications. !$#cross-references MUID:84111639; PMID:6319407 !$#accession A03500 !'##molecule_type DNA !'##residues 1-478,'QTMQMLTKLKHYQKLAKKIHSSVQLYLVDYH' ##label UHL2 !'##cross-references GB:J01786; NID:g153103 !'##experimental_source strain 8325-4 !'##note this sequence has been corrected in A58531 REFERENCE A19498 !$#authors Loefdahl, S.; Guss, B.; Uhlen, M.; Philipson, L.; Lindberg, !1M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:697-701 !$#title Gene for staphylococcal protein A. !$#cross-references MUID:83143997; PMID:6338496 !$#accession A19498 !'##molecule_type DNA !'##residues 'L',2-100,'D',102-186 ##label LOE !'##cross-references GB:J01786; NID:g153103 !'##experimental_source strain 8325-4 !'##note the authors translated the initiation codon TTG for residue 1 !1as Leu COMMENT This protein is part of the cell wall structure and is !1covalently linked to the peptidoglycan moiety. GENETICS !$#gene spa !$#start_codon TTG CLASSIFICATION #superfamily staphylococcal protein A KEYWORDS cell wall; duplication; IgG constant region-binding; tandem !1repeat; transmembrane protein FEATURE !$1-36 #domain signal sequence #status predicted #label SIG\ !$37-524 #product protein A #status predicted #label MAT\ !$37-100 #domain IgG constant region-binding repeat #label !8IGB1\ !$101-158 #domain IgG constant region-binding repeat #label !8IGB2\ !$159-216 #domain IgG constant region-binding repeat #label !8IGB3\ !$217-274 #domain IgG constant region-binding repeat #label !8IGB4\ !$275-332 #domain IgG constant region-binding repeat #label !8IGB5\ !$329-424 #region 8-residue repeats (E-D-G/N-N-K-P-G-K)\ !$333-428 #region cell wall binding #status predicted\ !$499-519 #domain transmembrane #status predicted #label TRM SUMMARY #length 524 #molecular-weight 57320 #checksum 5699 SEQUENCE /// ENTRY A47605 #type complete TITLE virF virulence protein - Shigella flexneri ORGANISM #formal_name Shigella flexneri DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A47605 REFERENCE A47605 !$#authors Sakai, T.; Sasakawa, C.; Makino, S.; Yoshikawa, M. !$#journal Infect. Immun. (1986) 54:395-402 !$#title DNA sequence and product analysis of the virF locus !1responsible for Congo red binding and cell invasion in !1Shigella flexneri 2a. !$#cross-references MUID:87032409; PMID:3021627 !$#accession A47605 !'##status preliminary !'##molecule_type DNA !'##residues 1-262 ##label SAK !'##cross-references GB:X16661; NID:g47066; PIDN:CAA34648.1; PID:g47067 CLASSIFICATION #superfamily fapR protein KEYWORDS DNA binding; transcription regulation SUMMARY #length 262 #molecular-weight 30549 #checksum 1144 SEQUENCE /// ENTRY S11984 #type complete TITLE fapR protein - Escherichia coli ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S11984 REFERENCE S11984 !$#authors Klaasen, P.; de Graaf, F.K. !$#journal Mol. Microbiol. (1990) 4:1779-1783 !$#title Characterization of FapR, a positive regulator of expression !1of the 987P operon in enterotoxigenic Escherichia coli. !$#cross-references MUID:91171879; PMID:2077360 !$#accession S11984 !'##status preliminary !'##molecule_type DNA !'##residues 1-260 ##label KLA !'##cross-references EMBL:X53494 !'##note the sequence from Fig. 3 is inconsistent with that from Fig. 2 !1in lacking 96-Lys and in having an additional Lys after !199-Phe GENETICS !$#gene fapR CLASSIFICATION #superfamily fapR protein KEYWORDS DNA binding; transcription regulation SUMMARY #length 260 #molecular-weight 30349 #checksum 6453 SEQUENCE /// ENTRY BVECM5 #type complete TITLE transcription regulator appY - Escherichia coli (strain K-12) ALTERNATE_NAMES M5 polypeptide ORGANISM #formal_name Escherichia coli DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 01-Mar-2002 ACCESSIONS A94498; A93664; JS0110; B64789; A29260 REFERENCE A94498 !$#authors Mann, N.H. !$#submission submitted to the EMBL Data Library, May 1987 !$#accession A94498 !'##molecule_type DNA !'##residues 1-249 ##label MAN REFERENCE A93664 !$#authors Kemp, E.H.; Minton, N.P.; Mann, N.H. !$#journal Nucleic Acids Res. (1987) 15:3924 !$#title Complete nucleotide sequence and deduced amino acid sequence !1of the M5 polypeptide gene of Escherichia coli. !$#cross-references MUID:87231084; PMID:3295784 !$#accession A93664 !'##molecule_type DNA !'##residues 1-249 ##label KEM !'##cross-references GB:Y00138; NID:g41947; PIDN:CAA68331.1; PID:g41948 REFERENCE JS0110 !$#authors Atlung, T.; Nielsen, A.; Hansen, F.G. !$#journal J. Bacteriol. (1989) 171:1683-1691 !$#title Isolation, characterization, and nucleotide sequence of !1appY, a regulatory gene for growth-phase-dependent gene !1expression in Escherichia coli. !$#cross-references MUID:89155479; PMID:2537825 !$#accession JS0110 !'##molecule_type DNA !'##residues 1-25,32-249 ##label ATL !'##cross-references GB:M24530; NID:g145291; PIDN:AAA23454.1; !1PID:g145292 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64789 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-249 ##label BLAT !'##cross-references GB:AE000161; GB:U00096; NID:g1786766; !1PIDN:AAC73665.1; PID:g1786776; UWGP:b0564 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene appY !$#map_position 13 min CLASSIFICATION #superfamily M5 polypeptide KEYWORDS DNA binding; transcription regulation FEATURE !$155-174 #domain DNA binding #status predicted #label DBR SUMMARY #length 249 #molecular-weight 28763 #checksum 2528 SEQUENCE /// ENTRY MMSOMP #type fragment TITLE M5 protein - Streptococcus pyogenes (fragment) ORGANISM #formal_name Streptococcus pyogenes DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 16-Feb-1997 ACCESSIONS A03501 REFERENCE A03501 !$#authors Manjula, B.N.; Acharya, A.S.; Mische, S.M.; Fairwell, T.; !1Fischetti, V.A. !$#journal J. Biol. Chem. (1984) 259:3686-3693 !$#title The complete amino acid sequence of a biologically active !1197-residue fragment of M protein isolated from type 5 group !1A streptococci. !$#cross-references MUID:84162039; PMID:6368549 !$#accession A03501 !'##molecule_type protein !'##residues 1-197 ##label MAN COMMENT Residues 27-58 contain several tandem 7-residue repeats, and !1residues 150-172 and 175-197 are homologous. COMMENT This protein is closely associated with the virulence of the !1bacterium and it impedes phagocytosis. It is a constituent !1of the cell wall and is present on the cell surface. CLASSIFICATION #superfamily M5 protein KEYWORDS cell wall; transmembrane protein; virulence SUMMARY #length 197 #checksum 1254 SEQUENCE /// ENTRY FCSOAG #type complete TITLE IgA Fc receptor precursor - Streptococcus agalactiae ALTERNATE_NAMES beta antigen ORGANISM #formal_name Streptococcus agalactiae DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS S15330; S20240; S17038 REFERENCE S15330 !$#authors Jerlstroem, P.G.; Chhatwal, G.S.; Timmis, K.N. !$#journal Mol. Microbiol. (1991) 5:843-849 !$#title The IgA-binding beta antigen of the c protein complex of !1Group B streptococci: sequence determination of its gene and !1detection of two binding regions. !$#cross-references MUID:91312121; PMID:1857207 !$#accession S15330 !'##molecule_type DNA !'##residues 1-1164 ##label JER1 !'##cross-references EMBL:X59771 !$#accession S20240 !'##molecule_type protein !'##residues 38-48 ##label JE2 REFERENCE S17038 !$#authors Jerlstroem, P.G. !$#submission submitted to the EMBL Data Library, August 1991 !$#accession S17038 !'##molecule_type DNA !'##residues 1-914,'E',916-1164 ##label JE3 !'##cross-references EMBL:X59771; NID:g46522; PIDN:CAA42442.1; !1PID:g46523 CLASSIFICATION #superfamily IgA Fc receptor KEYWORDS cell wall; immunoglobulin receptor; tandem repeat; !1transmembrane protein FEATURE !$1-37 #domain signal sequence #status predicted #label SIG\ !$38-1164 #product IgA Fc receptor #status experimental #label !8MAT\ !$199-438 #domain IgA binding #status predicted #label IGA1\ !$439-826 #domain IgA binding #status predicted #label IGA2\ !$827-945 #region proline-rich repeats\ !$946-1131 #domain cell wall-spanning #status predicted #label !8CWS\ !$1132-1159 #domain transmembrane #status predicted #label TMM SUMMARY #length 1164 #molecular-weight 131050 #checksum 4140 SEQUENCE /// ENTRY IKEC1 #type complete TITLE colicin E1 - Escherichia coli plasmid colicin E1 ORGANISM #formal_name Escherichia coli DATE 31-Oct-1980 #sequence_revision 18-Aug-1982 #text_change 28-May-1999 ACCESSIONS A93913; A91485; A93118; A03502 REFERENCE A93913 !$#authors Yamada, M.; Ebina, Y.; Miyata, T.; Nakazawa, T.; Nakazawa, !1A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:2827-2831 !$#title Nucleotide sequence of the structural gene for colicin E1 !1and predicted structure of the protein. !$#cross-references MUID:82222230; PMID:6953432 !$#contents plasmid colicin E1 !$#accession A93913 !'##molecule_type DNA !'##residues 1-522 ##label YAM !'##cross-references GB:J01563; NID:g144332; PIDN:AAA87379.1; !1PID:g144333 REFERENCE A91485 !$#authors Ebina, Y.; Kishi, F.; Miki, T.; Kagamiyama, H.; Nakazawa, !1T.; Nakazawa, A. !$#journal Gene (1981) 15:119-126 !$#title The nucleotide sequence surrounding the promoter region of !1colicin E1 gene. !$#cross-references MUID:82051304; PMID:6271636 !$#contents plasmid colicin E1 !$#accession A91485 !'##molecule_type DNA !'##residues 1-71 ##label EBI REFERENCE A93118 !$#authors Oka, A.; Nomura, N.; Morita, M.; Sugisaki, H.; Sugimoto, K.; !1Takanami, M. !$#journal Mol. Gen. Genet. (1979) 172:151-159 !$#title Nucleotide sequence of small CoIE1 derivitives: structure of !1the regions essential for autonomous replication and colicin !1E1 immunity. !$#cross-references MUID:80010893; PMID:384144 !$#contents plasmid pAO3 !$#accession A93118 !'##molecule_type DNA !'##residues 480-522 ##label OKA !'##note plasmid pAO3 is a small colicin E1 derivative GENETICS !$#gene cea !$#map_position 75-100/0-1 !$#genome plasmid CLASSIFICATION #superfamily colicin IB KEYWORDS antibiotic; bacteriocin; toxin; transmembrane protein SUMMARY #length 522 #molecular-weight 57279 #checksum 9880 SEQUENCE /// ENTRY IKECB #type complete TITLE colicin Ib - Escherichia coli plasmid ColIb ORGANISM #formal_name Escherichia coli DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 16-Jun-2000 ACCESSIONS A93533; D25035; A22503; B22503; A03503 REFERENCE A93533 !$#authors Varley, J.M.; Boulnois, G.J. !$#journal Nucleic Acids Res. (1984) 12:6727-6739 !$#title Analysis of a cloned colicin IB gene: complete nucleotide !1sequence and implications for regulation of expression. !$#cross-references MUID:85014128; PMID:6091036 !$#accession A93533 !'##molecule_type DNA !'##residues 1-626 ##label VAR !'##cross-references GB:X01009; NID:g41141; PIDN:CAA25505.1; PID:g41142 !'##note the authors translated the codon GAA for residue 294 as Gln REFERENCE A91822 !$#authors Mankovich, J.A.; Hsu, C.H.; Konisky, J. !$#journal J. Bacteriol. (1986) 168:228-236 !$#title DNA and amino acid sequence analysis of structural and !1immunity genes of colicins Ia and Ib. !$#cross-references MUID:87008385; PMID:3531169 !$#accession D25035 !'##molecule_type DNA !'##residues 1-626 ##label MAN !'##cross-references GB:AB021078; NID:g4512437; PIDN:BAA75098.1; !1PID:g4512449 REFERENCE A22503 !$#authors Mankovich, J.A.; Lai, P.H.; Gokul, N.; Konisky, J. !$#journal J. Biol. Chem. (1984) 259:8764-8768 !$#title Organization of the colicin Ib gene. !$#cross-references MUID:84264487; PMID:6204975 !$#accession A22503 !'##molecule_type DNA !'##residues 1-40 ##label MA2 !'##cross-references GB:K02071; NID:g144639; PIDN:AAA92225.1; !1PID:g144640 !$#accession B22503 !'##molecule_type protein !'##residues 2-21 ##label MA3 REFERENCE A93546 !$#authors Varley, J.M.; Boulnois, G.J. !$#journal Nucleic Acids Res. (1984) 12:8748 !$#contents annotation; corrigendum COMMENT This bactericidal protein functions by depolarizing the !1cytoplasmic membrane of sensitive cells. GENETICS !$#gene cib !$#genome plasmid CLASSIFICATION #superfamily colicin IB KEYWORDS antibiotic; bacteriocin; toxin; transmembrane protein FEATURE !$2-626 #product colicin Ib #status experimental #label MAT SUMMARY #length 626 #molecular-weight 69923 #checksum 8113 SEQUENCE /// ENTRY IKEBCA #type complete TITLE colicin A - Citrobacter freundii (strain CA31) plasmid ColA ORGANISM #formal_name Citrobacter freundii DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 16-Jul-1999 ACCESSIONS I40784; A03504; I40777 REFERENCE I40778 !$#authors Morlon, J.; Chartier, M.; Bidaud, M.; Lazdunski, C. !$#journal Mol. Gen. Genet. (1988) 211:231-243 !$#title The complete nucleotide sequence of the colicinogenic !1plasmid ColA. High extent of homology with ColE1. !$#cross-references MUID:88174422; PMID:2832701 !$#accession I40784 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-592 ##label RES !'##cross-references GB:M37402; NID:g144661; PIDN:AAA72879.1; !1PID:g144667 !'##experimental_source plasmid ColA REFERENCE A03504 !$#authors Morlon, J.; Lloubes, R.; Varenne, S.; Chartier, M.; !1Lazdunski, C. !$#journal J. Mol. Biol. (1983) 170:271-285 !$#title Complete nucleotide sequence of the structural gene for !1colicin A, a gene translated at non-uniform rate. !$#cross-references MUID:84036205; PMID:6313941 !$#accession A03504 !'##molecule_type DNA !'##residues 1-592 ##label MOR !'##cross-references GB:X01008; GB:X00034; NID:g40459; PIDN:CAA25503.1; !1PID:g40460 REFERENCE I40777 !$#authors Morlon, J.; Lloubes, R.; Chartier, M.; Bonicel, J.; !1Lazdunski, C. !$#journal EMBO J. (1983) 2:787-789 !$#title Nucleotide sequence of promoter, operator and amino-terminal !1region of caa, the structural gene of colicin A. !$#cross-references MUID:84057757; PMID:6641715 !$#accession I40777 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-53,'X',55-70 ##label RE2 !'##cross-references GB:M26369; NID:g144659; PIDN:AAA98057.1; !1PID:g144660 !'##experimental_source plasmid ColA COMMENT This protein acts to depolarize the bacterial inner !1membrane, most likely by forming voltage-dependent ion !1channels. GENETICS !$#gene caa !$#genome plasmid CLASSIFICATION #superfamily colicin IB KEYWORDS antibiotic; bacteriocin; toxin; transmembrane protein SUMMARY #length 592 #molecular-weight 62992 #checksum 5200 SEQUENCE /// ENTRY IKECBB #type complete TITLE colicin B - Escherichia coli plasmid ColBM-pF166 ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 28-May-1999 ACCESSIONS A27089 REFERENCE A27089 !$#authors Schramm, E.; Mende, J.; Braun, V.; Kamp, R.M. !$#journal J. Bacteriol. (1987) 169:3350-3357 !$#title Nucleotide sequence of the colicin B activity gene cba: !1consensus pentapeptide among tonB-dependent colicins and !1receptors. !$#cross-references MUID:87250309; PMID:2439491 !$#accession A27089 !'##molecule_type DNA !'##residues 1-511 ##label SCH !'##cross-references GB:M16816; NID:g145566; PIDN:AAA98063.1; !1PID:g145567 COMMENT Colicins are plasmid-encoded proteins that kill sensitive !1strains of E. coli and closely related species. Colicin B is !1a channel-forming colicin. These transmembrane toxins !1depolarize the cytoplasmic membrane, leading to dissipation !1of cellular energy. GENETICS !$#gene cba !$#genome plasmid CLASSIFICATION #superfamily colicin IB KEYWORDS antibiotic; bacteriocin; toxin; transmembrane protein SUMMARY #length 511 #molecular-weight 54863 #checksum 226 SEQUENCE /// ENTRY IKECM #type complete TITLE colicin M - Escherichia coli ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 28-May-1999 ACCESSIONS A27090 REFERENCE A27090 !$#authors Kock, J.; Oelschlaeger, T.; Kamp, R.M.; Braun, V. !$#journal J. Bacteriol. (1987) 169:3358-3361 !$#title Primary structure of colicin M, an inhibitor of murein !1biosynthesis. !$#cross-references MUID:87250310; PMID:3036784 !$#accession A27090 !'##molecule_type DNA !'##residues 1-271 ##label KOC !'##cross-references GB:M16754; NID:g145557; PIDN:AAA23589.1; !1PID:g145558 COMMENT This is a calcium-requiring inhibitor for murein !1biosynthesis; it causes lysis of sensitive cells accompanied !1by murein degradation. The target site is possibly the !1cytoplasmic membrane. GENETICS !$#gene cma CLASSIFICATION #superfamily colicin M KEYWORDS antibacterial; antibiotic; bacteriocin SUMMARY #length 271 #molecular-weight 29482 #checksum 2221 SEQUENCE /// ENTRY IKECV #type complete TITLE colicin V - Escherichia coli plasmid ColV ORGANISM #formal_name Escherichia coli DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 21-Jan-2000 ACCESSIONS S12274; A54469 REFERENCE S12271 !$#authors Gilson, L.; Mahanty, H.K.; Kolter, R. !$#journal EMBO J. (1990) 9:3875-3884 !$#title Genetic analysis of an MDR-like export system: the secretion !1of colicin V. !$#cross-references MUID:91065315; PMID:2249654 !$#accession S12274 !'##molecule_type DNA !'##residues 1-103 ##label GIL !'##cross-references EMBL:X57525; NID:g41177; PIDN:CAA40746.1; !1PID:g41179 REFERENCE A54469 !$#authors Fath, M.J.; Zhang, L.H.; Rush, J.; Kolter, R. !$#journal Biochemistry (1994) 33:6911-6917 !$#title Purification and characterization of colicin V from !1Escherichia coli culture supernatants. !$#cross-references MUID:94264007; PMID:8204625 !$#accession A54469 !'##status preliminary !'##molecule_type protein !'##residues 16-28 ##label FAT GENETICS !$#gene cvaC !$#genome plasmid ColV CLASSIFICATION #superfamily colicin V KEYWORDS bacteriocin; extracellular protein SUMMARY #length 103 #molecular-weight 10310 #checksum 4847 SEQUENCE /// ENTRY YTBSMA #type complete TITLE methylenomycin A resistance protein mmr - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jun-2000 ACCESSIONS I40493; G69658; S22742 REFERENCE I40493 !$#authors Putzer, H.; Gendron, N.; Grunberg-Manago, M. !$#journal EMBO J. (1992) 11:3117-3127 !$#title Co-ordinate expression of the two threonyl-tRNA synthetase !1genes in Bacillus subtilis: control by transcriptional !1antitermination involving a conserved regulatory sequence. !$#cross-references MUID:92347349; PMID:1379177 !$#accession I40493 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-466 ##label RES !'##cross-references EMBL:X66121; NID:g40214; PIDN:CAA46908.1; !1PID:g40215 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69658 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-466 ##label KUN !'##cross-references GB:Z99123; GB:AL009126; NID:g2636240; !1PIDN:CAB15784.1; PID:g2636293 !'##experimental_source strain 168 GENETICS !$#gene mmr CLASSIFICATION #superfamily tetracycline resistance protein KEYWORDS antibiotic resistance; membrane protein SUMMARY #length 466 #molecular-weight 48845 #checksum 3285 SEQUENCE /// ENTRY YTECT0 #type complete TITLE tetracycline resistance protein - Escherichia coli transposon Tn10 ORGANISM #formal_name Escherichia coli DATE 13-Jun-1983 #sequence_revision 20-Sep-1984 #text_change 24-Sep-1999 ACCESSIONS A91505; A93481; A03507 REFERENCE A91505 !$#authors Nguyen, T.T.; Postle, K.; Bertrand, K.P. !$#journal Gene (1983) 25:83-92 !$#title Sequence homology between the tetracycline-resistance !1determinants of Tn10 and pBR322. !$#cross-references MUID:84109550; PMID:6319234 !$#accession A91505 !'##molecule_type DNA !'##residues 1-401 ##label NGU REFERENCE A93481 !$#authors Hillen, W.; Schollmeier, K. !$#journal Nucleic Acids Res. (1983) 11:525-539 !$#title Nucleotide sequence of the Tn10 encoded tetracycline !1resistance gene. !$#cross-references MUID:83143319; PMID:6298728 !$#accession A93481 !'##molecule_type DNA !'##residues 1-280,'E',282-300,'D',302-329,'E',331-353,'T',355-401 !1##label HIL !'##cross-references GB:V00611; NID:g43700; PIDN:CAA23880.1; PID:g43701 GENETICS !$#gene tet CLASSIFICATION #superfamily tetracycline resistance protein KEYWORDS antibiotic resistance; transmembrane protein SUMMARY #length 401 #molecular-weight 43267 #checksum 6992 SEQUENCE /// ENTRY S30286 #type complete TITLE tetracycline resistance protein - Salmonella ordonez plasmid pIP173 ORGANISM #formal_name Salmonella ordonez DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S30286 REFERENCE S30286 !$#authors Allard, J.D.; Gibson, M.L.; Vu, L.H.; Nguyen, T.T.; !1Bertrand, K.P. !$#journal Mol. Gen. Genet. (1993) 237:301-305 !$#title Nucleotide sequence of class D tetracycline resistance genes !1from Salmonella ordonez. !$#cross-references MUID:93204906; PMID:8384294 !$#accession S30286 !'##molecule_type DNA !'##residues 1-394 ##label ALL !'##cross-references EMBL:X65876; NID:g49073; PIDN:CAA46706.1; !1PID:g49074 GENETICS !$#gene tetA !$#genome plasmid CLASSIFICATION #superfamily tetracycline resistance protein KEYWORDS antibiotic resistance; transmembrane protein SUMMARY #length 394 #molecular-weight 41035 #checksum 6286 SEQUENCE /// ENTRY YTBSRT #type complete TITLE tetracycline resistance protein - Bacillus sp. plasmid pTHT15 ORGANISM #formal_name Bacillus sp. DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 28-May-1999 ACCESSIONS A23973 REFERENCE A23973 !$#authors Hoshino, T.; Ikeda, T.; Tomizuka, N.; Furukawa, K. !$#journal Gene (1985) 37:131-138 !$#title Nucleotide sequence of the tetracycline resistance gene of !1pTHT15, a thermophilic Bacillus plasmid: comparison with !1staphylococcal Tc-R controls. !$#cross-references MUID:86031344; PMID:2996983 !$#accession A23973 !'##molecule_type DNA !'##residues 1-458 ##label HOS !'##cross-references GB:M11036; NID:g143737; PIDN:AAA22851.1; !1PID:g143739 GENETICS !$#gene tet !$#genome plasmid !$#start_codon GTG CLASSIFICATION #superfamily tetracycline resistance protein KEYWORDS antibiotic resistance; transmembrane protein FEATURE !$12-33 #domain transmembrane #status predicted #label TM1\ !$81-100 #domain transmembrane #status predicted #label TM2\ !$111-129 #domain transmembrane #status predicted #label TM3\ !$140-162 #domain transmembrane #status predicted #label TM4\ !$165-185 #domain transmembrane #status predicted #label TM5\ !$201-221 #domain transmembrane #status predicted #label TM6\ !$223-240 #domain transmembrane #status predicted #label TM7\ !$256-276 #domain transmembrane #status predicted #label TM8\ !$297-317 #domain transmembrane #status predicted #label TM9\ !$324-344 #domain transmembrane #status predicted #label TM10\ !$346-365 #domain transmembrane #status predicted #label TM11\ !$432-451 #domain transmembrane #status predicted #label TM12 SUMMARY #length 458 #molecular-weight 50118 #checksum 5577 SEQUENCE /// ENTRY YTBSU6 #type complete TITLE tetracycline resistance protein - Bacillus cereus plasmid pBC16 ORGANISM #formal_name Bacillus cereus DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS S09234 REFERENCE S09233 !$#authors Palva, A.; Vidgren, G.; Simonen, M.; Rintala, H.; Laamanen, !1P. !$#journal Nucleic Acids Res. (1990) 18:1635 !$#title Nucleotide sequence of the tetracycline resistance gene of !1pBC16 from Bacillus cereus. !$#cross-references MUID:90221899; PMID:2109312 !$#accession S09234 !'##status translation not shown !'##molecule_type DNA !'##residues 1-458 ##label PAL !'##cross-references EMBL:X51366; NID:g39459; PIDN:CAA35751.1; !1PID:g580765 GENETICS !$#gene tet !$#genome plasmid !$#start_codon GTG CLASSIFICATION #superfamily tetracycline resistance protein KEYWORDS antibiotic resistance; transmembrane protein FEATURE !$12-33 #domain transmembrane #status predicted #label TM1\ !$81-100 #domain transmembrane #status predicted #label TM2\ !$111-129 #domain transmembrane #status predicted #label TM3\ !$140-162 #domain transmembrane #status predicted #label TM4\ !$165-185 #domain transmembrane #status predicted #label TM5\ !$201-221 #domain transmembrane #status predicted #label TM6\ !$223-240 #domain transmembrane #status predicted #label TM7\ !$256-276 #domain transmembrane #status predicted #label TM8\ !$297-317 #domain transmembrane #status predicted #label TM9\ !$324-344 #domain transmembrane #status predicted #label TM10\ !$346-365 #domain transmembrane #status predicted #label TM11\ !$432-451 #domain transmembrane #status predicted #label TM12 SUMMARY #length 458 #molecular-weight 50092 #checksum 5724 SEQUENCE /// ENTRY YTSOG #type complete TITLE tetracycline resistance protein - Streptococcus agalactiae plasmid pMV158 ORGANISM #formal_name Streptococcus agalactiae DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS C25599; S05982 REFERENCE A25599 !$#authors Lacks, S.A.; Lopez, P.; Greenberg, B.; Espinosa, M. !$#journal J. Mol. Biol. (1986) 192:753-765 !$#title Identification and analysis of genes for tetracycline !1resistance and replication functions in the broad-host-range !1plasmid pLS1. !$#cross-references MUID:87226167; PMID:2438417 !$#contents plasmid pLS1 !$#accession C25599 !'##molecule_type DNA !'##residues 1-458 ##label LAC !'##cross-references GB:M29725; NID:g149697; PIDN:AAA98167.1; !1PID:g551885 !'##note plasmid pSL1, derived from plasmid pMV158 in vitro, was !1amplified in Streptococcus pneumoniae REFERENCE S05980 !$#authors van der Lelie, D.; Bron, S.; Venema, G.; Oskam, L. !$#journal Nucleic Acids Res. (1989) 17:7283-7294 !$#title Similarity of minus origins of replication and flanking open !1reading frames of plasmids pUB110, pTB913 and pMV158. !$#cross-references MUID:90016790; PMID:2677995 !$#contents plasmid pMV158 !$#accession S05982 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-158,'V',160-256,'L',258-340,'F',342-369,'P',371-420,'G', !1422-443,'G',445-447,'V',449-458 ##label VAN !'##cross-references EMBL:X15669; NID:g46662; PIDN:CAA33712.1; !1PID:g581578 !'##note this sequence was submitted to the EMBL Data Library, June 1989 GENETICS !$#gene tet !$#genome plasmid !$#start_codon GTG CLASSIFICATION #superfamily tetracycline resistance protein KEYWORDS antibiotic resistance; transmembrane protein FEATURE !$12-33 #domain transmembrane #status predicted #label TM1\ !$81-100 #domain transmembrane #status predicted #label TM2\ !$111-129 #domain transmembrane #status predicted #label TM3\ !$140-162 #domain transmembrane #status predicted #label TM4\ !$165-185 #domain transmembrane #status predicted #label TM5\ !$201-221 #domain transmembrane #status predicted #label TM6\ !$223-240 #domain transmembrane #status predicted #label TM7\ !$256-276 #domain transmembrane #status predicted #label TM8\ !$297-317 #domain transmembrane #status predicted #label TM9\ !$324-344 #domain transmembrane #status predicted #label TM10\ !$346-365 #domain transmembrane #status predicted #label TM11\ !$432-451 #domain transmembrane #status predicted #label TM12 SUMMARY #length 458 #molecular-weight 50092 #checksum 5724 SEQUENCE /// ENTRY YTBSY8 #type complete TITLE tetracycline resistance protein tetB - Bacillus subtilis ALTERNATE_NAMES tetracycline-resistance determinant ORGANISM #formal_name Bacillus subtilis DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jun-2000 ACCESSIONS JT0427; S66002; G69721; S03327 REFERENCE JT0427 !$#authors Sakaguchi, R.; Amano, H.; Shishido, K. !$#journal Biochim. Biophys. Acta (1988) 950:441-444 !$#title Nucleotide sequence homology of the tetracycline-resistance !1determinant naturally maintained in Bacillus subtilis !1Marburg 168 chromosome and the tetracycline-resistance gene !1of B. subtilis plasmid pNS1981. !$#cross-references MUID:89000797; PMID:2844262 !$#accession JT0427 !'##molecule_type DNA !'##residues 1-458 ##label SAK !'##cross-references EMBL:X08034; NID:g40207; PIDN:CAA30827.1; !1PID:g580940 !'##experimental_source strain BSY908 REFERENCE S65967 !$#authors Ogasawara, N.; Nakai, S.; Yoshikawa, H. !$#journal DNA Res. (1994) 1:1-14 !$#title Systematic sequencing of the 180 kilobase region of the !1Bacillus subtilis chromosome containing the replication !1origin. !$#cross-references MUID:96051385; PMID:7584024 !$#accession S66002 !'##status preliminary !'##molecule_type DNA !'##residues 1-458 ##label OGA !'##cross-references EMBL:D26185; NID:g467326; PIDN:BAA05208.1; !1PID:g467362 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69721 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-458 ##label KUN !'##cross-references GB:Z99124; GB:AL009126; NID:g2636442; !1PIDN:CAB16114.1; PID:g2636624 !'##experimental_source strain 168 GENETICS !$#gene tetB !$#start_codon GTG CLASSIFICATION #superfamily tetracycline resistance protein KEYWORDS antibiotic resistance; transmembrane protein FEATURE !$12-33 #domain transmembrane #status predicted #label TM1\ !$81-100 #domain transmembrane #status predicted #label TM2\ !$111-129 #domain transmembrane #status predicted #label TM3\ !$140-162 #domain transmembrane #status predicted #label TM4\ !$165-185 #domain transmembrane #status predicted #label TM5\ !$201-221 #domain transmembrane #status predicted #label TM6\ !$223-240 #domain transmembrane #status predicted #label TM7\ !$256-276 #domain transmembrane #status predicted #label TM8\ !$297-317 #domain transmembrane #status predicted #label TM9\ !$324-344 #domain transmembrane #status predicted #label TM10\ !$346-365 #domain transmembrane #status predicted #label TM11\ !$432-451 #domain transmembrane #status predicted #label TM12 SUMMARY #length 458 #molecular-weight 49756 #checksum 7752 SEQUENCE /// ENTRY YTEC32 #type complete TITLE tetracycline resistance protein - Escherichia coli plasmid pBR322 ORGANISM #formal_name Escherichia coli DATE 08-Aug-1983 #sequence_revision 08-Aug-1983 #text_change 16-Feb-1997 ACCESSIONS B90923; A03508 REFERENCE A90923 !$#authors Sutcliffe, J.G. !$#journal Cold Spring Harb. Symp. Quant. Biol. (1979) 43:77-90 !$#title Complete nucleotide sequence of the Escherichia coli plasmid !1pBR322. !$#cross-references MUID:80002802; PMID:383387 !$#accession B90923 !'##molecule_type DNA !'##residues 1-396 ##label SUT REFERENCE A93946 !$#authors Livneh, Z. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:237-241 !$#title Directed mutagenesis mthod for analysis of mutagen !1specificity: application to ultraviolet-induced mutagenesis. !$#cross-references MUID:83117828; PMID:6337373 !$#contents annotation; revision to the DNA sequence and identification !1of the protein REFERENCE A91499 !$#authors Peden, K.W.C. !$#journal Gene (1983) 22:277-280 !$#title Revised sequence of the tetracycline-resistance gene of !1pBR322. !$#cross-references MUID:83263146; PMID:6307828 !$#contents annotation; revision to the DNA sequence and identification !1of the protein GENETICS !$#genome plasmid CLASSIFICATION #superfamily tetracycline resistance protein KEYWORDS antibiotic resistance; transmembrane protein SUMMARY #length 396 #molecular-weight 41510 #checksum 9995 SEQUENCE /// ENTRY S38656 #type complete TITLE tetA protein - Pseudomonas aeruginosa ORGANISM #formal_name Pseudomonas aeruginosa DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S38656 REFERENCE S38655 !$#authors Trueman, P.; Sharpe, G.S.; Barth, P.T. !$#submission submitted to the EMBL Data Library, November 1993 !$#accession S38656 !'##status preliminary !'##molecule_type DNA !'##residues 1-399 ##label TRU !'##cross-references EMBL:X75761; NID:g415984; PIDN:CAA53389.1; !1PID:g581438 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily tetracycline resistance protein KEYWORDS antibiotic resistance; transmembrane protein SUMMARY #length 399 #molecular-weight 42209 #checksum 9824 SEQUENCE /// ENTRY YTECR1 #type complete TITLE tetracycline resistance protein - Escherichia coli plasmid PR1 transposon Tn1721 ORGANISM #formal_name Escherichia coli DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jun-2000 ACCESSIONS A03509 REFERENCE A93486 !$#authors Waters, S.H.; Rogowsky, P.; Grinsted, J.; Altenbuchner, J.; !1Schmitt, R. !$#journal Nucleic Acids Res. (1983) 11:6089-6105 !$#title The tetracycline resistance determinants of RP1 and Tn1721: !1nucleotide sequence analysis. !$#cross-references MUID:83299270; PMID:6310527 !$#accession A03509 !'##molecule_type DNA !'##residues 1-399 ##label WAT !'##cross-references GB:X00006; NID:g42508; PIDN:CAA24909.1; !1PID:g1333751 COMMENT This membrane-bound protein is one of the four tetracycline !1resistance proteins encoded by genetically different !1determinants from E. coli plasmids. It is responsible for an !1active tetracycline efflux, an energy-dependent process that !1decreases the accumulation of the antibiotic in whole cells !1in which resistance has been induced. GENETICS !$#gene tetA !$#genome plasmid !$#start_codon GTG CLASSIFICATION #superfamily tetracycline resistance protein KEYWORDS antibiotic resistance; transmembrane protein SUMMARY #length 399 #molecular-weight 42237 #checksum 473 SEQUENCE /// ENTRY QQSABT #type complete TITLE hypothetical protein B-295 - Staphylococcus aureus plasmid pT181 ORGANISM #formal_name Staphylococcus aureus DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 28-May-1999 ACCESSIONS A03510 REFERENCE A03510 !$#authors Khan, S.A.; Novick, R.P. !$#journal Plasmid (1983) 10:251-259 !$#title Complete nucleotide sequence of pT181, a !1tetracycline-resistance plasmid from Staphylococcus aureus. !$#cross-references MUID:84095990; PMID:6657777 !$#accession A03510 !'##molecule_type DNA !'##residues 1-295 ##label KHA !'##cross-references GB:J01764; GB:J01765; NID:g151679; PIDN:AAA26034.1; !1PID:g473641 GENETICS !$#genome plasmid CLASSIFICATION #superfamily tetracycline resistance protein KEYWORDS antibiotic resistance SUMMARY #length 295 #molecular-weight 33096 #checksum 5572 SEQUENCE /// ENTRY QQSACT #type complete TITLE hypothetical protein C-156 - Staphylococcus aureus plasmid pT181 ORGANISM #formal_name Staphylococcus aureus DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 28-May-1999 ACCESSIONS A04492 REFERENCE A03510 !$#authors Khan, S.A.; Novick, R.P. !$#journal Plasmid (1983) 10:251-259 !$#title Complete nucleotide sequence of pT181, a !1tetracycline-resistance plasmid from Staphylococcus aureus. !$#cross-references MUID:84095990; PMID:6657777 !$#accession A04492 !'##molecule_type DNA !'##residues 1-152 ##label KHA !'##cross-references GB:J01764; GB:J01765; NID:g151679; PIDN:AAA26035.1; !1PID:g151682 GENETICS !$#genome plasmid CLASSIFICATION #superfamily tetracycline resistance protein KEYWORDS antibiotic resistance SUMMARY #length 152 #molecular-weight 16640 #checksum 2121 SEQUENCE /// ENTRY E64143 #type complete TITLE chloramphenicol resistance protein homolog HI0135 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS E64143 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession E64143 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-396 ##label TIGR !'##cross-references GB:U32699; GB:L42023; NID:g3212180; !1PIDN:AAC21806.1; PID:g1573088; TIGR:HI0135 !'##note best homolog was a hypothetical protein from Escherichia coli CLASSIFICATION #superfamily Streptomyces lividans chloramphenicol !1resistance protein KEYWORDS antibiotic resistance; transmembrane protein SUMMARY #length 396 #molecular-weight 43360 #checksum 7423 SEQUENCE /// ENTRY A64668 #type complete TITLE chloramphenicol resistance protein homolog HP1185 - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A64668 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession A64668 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-391 ##label TOM !'##cross-references GB:AE000624; GB:AE000511; NID:g2314340; !1PIDN:AAD08231.1; PID:g2314345; TIGR:HP1185 CLASSIFICATION #superfamily Streptomyces lividans chloramphenicol !1resistance protein KEYWORDS antibiotic resistance; transmembrane protein SUMMARY #length 391 #molecular-weight 43110 #checksum 8254 SEQUENCE /// ENTRY C64907 #type complete TITLE chloramphenicol resistance protein homolog ydeA - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS C64907 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64907 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-396 ##label BLAT !'##cross-references GB:AE000250; GB:U00096; NID:g1787801; !1PIDN:AAC74601.1; PID:g1787808; UWGP:b1528 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ydeA CLASSIFICATION #superfamily Streptomyces lividans chloramphenicol !1resistance protein KEYWORDS antibiotic resistance; transmembrane protein FEATURE !$10-26 #domain transmembrane #status predicted #label TM1\ !$50-66 #domain transmembrane #status predicted #label TM2\ !$80-96 #domain transmembrane #status predicted #label TM3\ !$101-117 #domain transmembrane #status predicted #label TM4\ !$138-154 #domain transmembrane #status predicted #label TM5\ !$169-185 #domain transmembrane #status predicted #label TM6\ !$210-226 #domain transmembrane #status predicted #label TM7\ !$249-265 #domain transmembrane #status predicted #label TM8\ !$276-292 #domain transmembrane #status predicted #label TM9\ !$301-317 #domain transmembrane #status predicted #label TM10\ !$336-352 #domain transmembrane #status predicted #label TM11\ !$368-384 #domain transmembrane #status predicted #label TM12 SUMMARY #length 396 #molecular-weight 42538 #checksum 1185 SEQUENCE /// ENTRY C64923 #type complete TITLE chloramphenicol resistance protein homolog b1657 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS C64923 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64923 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-389 ##label BLAT !'##cross-references GB:AE000261; GB:U00096; NID:g1787945; !1PIDN:AAC74729.1; PID:g1787947; UWGP:b1657 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily Streptomyces lividans chloramphenicol !1resistance protein KEYWORDS antibiotic resistance; transmembrane protein FEATURE !$48-64 #domain transmembrane #status predicted #label TM01\ !$73-89 #domain transmembrane #status predicted #label TM02\ !$162-178 #domain transmembrane #status predicted #label TM03\ !$203-219 #domain transmembrane #status predicted #label TM04\ !$237-253 #domain transmembrane #status predicted #label TM05\ !$271-287 #domain transmembrane #status predicted #label TM06\ !$292-308 #domain transmembrane #status predicted #label TM07\ !$357-373 #domain transmembrane #status predicted #label TM08 SUMMARY #length 389 #molecular-weight 40064 #checksum 9224 SEQUENCE /// ENTRY C69988 #type complete TITLE chloramphenicol resistance protein homolog ytbD - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS C69988 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69988 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-396 ##label KUN !'##cross-references GB:Z99118; GB:AL009126; NID:g2635200; !1PIDN:CAB14864.1; PID:g2635369 !'##experimental_source strain 168 GENETICS !$#gene ytbD CLASSIFICATION #superfamily Streptomyces lividans chloramphenicol !1resistance protein KEYWORDS antibiotic resistance; transmembrane protein SUMMARY #length 396 #molecular-weight 41628 #checksum 7722 SEQUENCE /// ENTRY B69801 #type complete TITLE chloramphenicol resistance protein homolog yfhI - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS B69801 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69801 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-397 ##label KUN !'##cross-references GB:Z99108; GB:AL009126; NID:g2633055; !1PIDN:CAB12683.1; PID:g2633178 !'##experimental_source strain 168 GENETICS !$#gene yfhI CLASSIFICATION #superfamily Streptomyces lividans chloramphenicol !1resistance protein KEYWORDS antibiotic resistance; transmembrane protein SUMMARY #length 397 #molecular-weight 41528 #checksum 1480 SEQUENCE /// ENTRY B43750 #type complete TITLE chloramphenicol resistance protein homolog araJ precursor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS B43750; D64768; S27549 REFERENCE A43750 !$#authors Reeder, T.; Schleif, R. !$#journal J. Bacteriol. (1991) 173:7765-7771 !$#title Mapping, sequence, and apparent lack of function of araJ, a !1gene of the Escherichia coli arabinose regulon. !$#cross-references MUID:92078081; PMID:1744033 !$#accession B43750 !'##molecule_type DNA !'##residues 1-394 ##label REE !'##cross-references EMBL:M64787; NID:g145326; PIDN:AAA23474.1; !1PID:g145328 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64768 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-394 ##label BLAT !'##cross-references GB:AE000145; GB:U00096; NID:g1786580; !1PIDN:AAC73499.1; PID:g1786595; UWGP:b0396 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene araJ !$#map_position 9 min CLASSIFICATION #superfamily Streptomyces lividans chloramphenicol !1resistance protein KEYWORDS antibiotic resistance; transmembrane protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-394 #product araJ protein #status predicted #label MAT\ !$44-60 #domain transmembrane #status predicted #label TM1\ !$70-86 #domain transmembrane #status predicted #label TM2\ !$128-144 #domain transmembrane #status predicted #label TM3\ !$160-176 #domain transmembrane #status predicted #label TM4\ !$203-219 #domain transmembrane #status predicted #label TM5\ !$235-251 #domain transmembrane #status predicted #label TM6\ !$267-283 #domain transmembrane #status predicted #label TM7\ !$292-308 #domain transmembrane #status predicted #label TM8\ !$357-373 #domain transmembrane #status predicted #label TM9 SUMMARY #length 394 #molecular-weight 41926 #checksum 3960 SEQUENCE /// ENTRY S18593 #type complete TITLE chloramphenicol resistance protein - Streptomyces lividans ORGANISM #formal_name Streptomyces lividans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S18593 REFERENCE S18593 !$#authors Dittrich, W.; Betzler, M.; Schrempf, H. !$#journal Mol. Microbiol. (1991) 5:2789-2797 !$#title An amplifiable and deletable chloramphenicol-resistance !1determinant of Streptomyces lividans 1326 encodes a putative !1transmembrane protein. !$#cross-references MUID:92140043; PMID:1779766 !$#accession S18593 !'##status preliminary !'##molecule_type DNA !'##residues 1-392 ##label DIT !'##cross-references EMBL:X59968; NID:g47159; PIDN:CAA42594.1; !1PID:g47160 CLASSIFICATION #superfamily Streptomyces lividans chloramphenicol !1resistance protein KEYWORDS antibiotic resistance; transmembrane protein SUMMARY #length 392 #molecular-weight 38855 #checksum 1618 SEQUENCE /// ENTRY S25183 #type complete TITLE chloramphenicol resistance protein - Rhodococcus fascians ORGANISM #formal_name Rhodococcus fascians DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S25183; S21395 REFERENCE S25183 !$#authors Desomer, J.; Vereecke, D.; Crespi, M.; van Montagu, M. !$#journal Mol. Microbiol. (1992) 6:2377-2385 !$#title The plasmid-encoded chloramphenicol-resistance protein of !1Rhodococcus fascians is homologous to the transmembrane !1tetracycline efflux proteins. !$#cross-references MUID:93023865; PMID:1406276 !$#accession S25183 !'##molecule_type DNA !'##residues 1-391 ##label DES !'##cross-references EMBL:Z12001; NID:g46157; PIDN:CAA78046.1; !1PID:g581504 GENETICS !$#gene cmr !$#start_codon GTG CLASSIFICATION #superfamily Streptomyces lividans chloramphenicol !1resistance protein KEYWORDS antibiotic resistance; membrane protein SUMMARY #length 391 #molecular-weight 40323 #checksum 5187 SEQUENCE /// ENTRY A69746 #type complete TITLE chloramphenicol resistance protein homolog ybcL - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A69746 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69746 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-390 ##label KUN !'##cross-references GB:Z99104; GB:Z99105; GB:AL009126; NID:g2632457; !1PIDN:CAB11982.1; PID:g2632474; NID:g2632267; PID:g2632456 !'##experimental_source strain 168 GENETICS !$#gene ybcL CLASSIFICATION #superfamily Streptomyces lividans chloramphenicol !1resistance protein KEYWORDS antibiotic resistance; transmembrane protein SUMMARY #length 390 #molecular-weight 41408 #checksum 8147 SEQUENCE /// ENTRY H69784 #type complete TITLE chloramphenicol resistance protein homolog ydhL - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS H69784 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69784 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-425 ##label KUN !'##cross-references GB:Z99107; GB:AL009126; NID:g2632866; !1PIDN:CAB12399.1; PID:g2632893 !'##experimental_source strain 168 GENETICS !$#gene ydhL CLASSIFICATION #superfamily Streptomyces lividans chloramphenicol !1resistance protein KEYWORDS antibiotic resistance; transmembrane protein SUMMARY #length 425 #molecular-weight 45993 #checksum 8508 SEQUENCE /// ENTRY S23860 #type complete TITLE chloramphenicol resistance protein homolog opdE - Pseudomonas aeruginosa ORGANISM #formal_name Pseudomonas aeruginosa DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 31-Dec-2000 ACCESSIONS S23860; H83368 REFERENCE S23859 !$#authors Huang, H.; Siehnel, R.J.; Bellido, F.; Rawling, E.; Hancock, !1R.E.W. !$#submission submitted to the EMBL Data Library, July 1992 !$#description Analysis of two gene regions involved in the expression of !1the imipenem-specific, outer membrane porin protein OprD of !1Pseudomonas aeruginosa. !$#accession S23860 !'##status preliminary !'##molecule_type DNA !'##residues 1-402 ##label HUA !'##cross-references EMBL:Z14064; NID:g45366; PIDN:CAA78446.1; !1PID:g45368 REFERENCE A82950 !$#authors Stover, C.K.; Pham, X.Q.; Erwin, A.L.; Mizoguchi, S.D.; !1Warrener, P.; Hickey, M.J.; Brinkman, F.S.L.; Hufnagle, !1W.O.; Kowalik, D.J.; Lagrou, M.; Garber, R.L.; Goltry, L.; !1Tolentino, E.; Westbrook-Wadman, S.; Yuan, Y.; Brody, L.L.; !1Coulter, S.N.; Folger, K.R.; Kas, A.; Larbig, K.; Lim, R.M.; !1Smith, K.A.; Spencer, D.H.; Wong, G.K.S.; Wu, Z.; Paulsen, !1I.T.; Reizer, J.; Saier, M.H.; Hancock, R.E.W.; Lory, S.; !1Olson, M.V. !$#journal Nature (2000) 406:959-964 !$#title Complete genome sequence of Pseudomonas aeruginosa PA01, an !1opportunistic pathogen. !$#cross-references MUID:20437337; PMID:10984043 !$#accession H83368 !'##status preliminary !'##molecule_type DNA !'##residues 1-402 ##label STO !'##cross-references GB:AE004648; GB:AE004091; NID:g9948237; !1PIDN:AAG05607.1; GSPDB:GN00131; PASP:PA2219 !'##experimental_source strain PAO1 GENETICS !$#gene opdE; PA2219 CLASSIFICATION #superfamily Streptomyces lividans chloramphenicol !1resistance protein KEYWORDS antibiotic resistance; transmembrane protein SUMMARY #length 402 #molecular-weight 41592 #checksum 7003 SEQUENCE /// ENTRY G65167 #type complete TITLE chloramphenicol resistance protein homolog (nlpA 3' region) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS G65167 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65167 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-451 ##label BLAT !'##cross-references GB:AE000444; GB:U00096; NID:g2367258; !1PIDN:AAC76685.1; PID:g1790095; UWGP:b3662 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yicM CLASSIFICATION #superfamily Streptomyces lividans chloramphenicol !1resistance protein KEYWORDS antibiotic resistance; transmembrane protein SUMMARY #length 451 #molecular-weight 47930 #checksum 4875 SEQUENCE /// ENTRY B69656 #type complete TITLE multidrug-efflux transporter (puromycin, nerfloxacin, tosufloxa) mdr - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS B69656 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69656 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-426 ##label KUN !'##cross-references GB:Z99105; GB:AL009126; NID:g2632457; !1PIDN:CAB12101.1; PID:g2632593 !'##experimental_source strain 168 GENETICS !$#gene mdr CLASSIFICATION #superfamily multidrug-efflux transporter KEYWORDS antibiotic resistance; transmembrane protein SUMMARY #length 426 #molecular-weight 46816 #checksum 7337 SEQUENCE /// ENTRY A70022 #type complete TITLE multidrug-efflux transporter homolog yusP - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A70022 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A70022 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-541 ##label KUN !'##cross-references GB:Z99120; GB:AL009126; NID:g2635613; !1PIDN:CAB15277.1; PID:g2635784 !'##experimental_source strain 168 GENETICS !$#gene yusP CLASSIFICATION #superfamily multidrug-efflux transporter KEYWORDS antibiotic resistance; transmembrane protein SUMMARY #length 541 #molecular-weight 57946 #checksum 2570 SEQUENCE /// ENTRY G69804 #type complete TITLE multidrug-efflux transporter homolog yfiU - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS G69804 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69804 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-518 ##label KUN !'##cross-references GB:Z99108; GB:AL009126; NID:g2633055; !1PIDN:CAB12669.1; PID:g2633164 !'##experimental_source strain 168 GENETICS !$#gene yfiU CLASSIFICATION #superfamily multidrug-efflux transporter KEYWORDS antibiotic resistance; transmembrane protein SUMMARY #length 518 #molecular-weight 54936 #checksum 7085 SEQUENCE /// ENTRY G69005 #type complete TITLE multidrug transporter homolog - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS G69005 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession G69005 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-459 ##label MTH !'##cross-references GB:AE000800; GB:AE000666; NID:g2621130; !1PIDN:AAB84603.1; PID:g2621135 !'##experimental_source strain Delta H GENETICS !$#gene MTH104 CLASSIFICATION #superfamily multidrug-efflux transporter KEYWORDS antibiotic resistance; transmembrane protein SUMMARY #length 459 #molecular-weight 48533 #checksum 5648 SEQUENCE /// ENTRY C65179 #type complete TITLE hypothetical 51.5 kD protein in rbsR-rrsC intergenic region - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS C65179 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65179 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-475 ##label BLAT !'##cross-references GB:AE000452; GB:U00096; NID:g1790188; !1PIDN:AAC76777.1; PID:g1790195; UWGP:b3754 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yieO CLASSIFICATION #superfamily multidrug-efflux transporter KEYWORDS antibiotic resistance; transmembrane protein SUMMARY #length 475 #molecular-weight 51461 #checksum 5295 SEQUENCE /// ENTRY YESAEE #type complete TITLE erythromycin resistance protein - Staphylococcus epidermidis plasmid pUL5050 ORGANISM #formal_name Staphylococcus epidermidis DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 19-Jan-2001 ACCESSIONS S11158; S12475 REFERENCE S11157 !$#authors Ross, J.I.; Eady, E.A.; Cove, J.H.; Cunliffe, W.J.; !1Baumberg, S.; Wootton, J.C. !$#journal Mol. Microbiol. (1990) 4:1207-1214 !$#title Inducible erythromycin resistance in staphylococci is !1encoded by a member of the ATP-binding transport super-gene !1family. !$#cross-references MUID:91041730; PMID:2233255 !$#accession S11158 !'##molecule_type DNA !'##residues 1-488 ##label ROS !'##cross-references EMBL:X52085 REFERENCE S12475 !$#authors Eady, E.A. !$#submission submitted to the EMBL Data Library, March 1990 !$#accession S12475 !'##molecule_type DNA !'##residues 1-113,'R',115-488 ##label EAD !'##cross-references EMBL:X52085; NID:g47000; PIDN:CAA36304.1; !1PID:g47001 GENETICS !$#gene msrA !$#genome plasmid CLASSIFICATION #superfamily Staphylococcus erythromycin resistance protein; !1ATP-binding cassette homology KEYWORDS antibiotic resistance; ATP; nucleotide binding; P-loop FEATURE !$21-175 #domain ATP-binding cassette homology #label ABC1\ !$26-173 #domain ATP binding #status predicted #label ATP1\ !$38-45 #region nucleotide-binding motif A (P-loop)\ !$123-128 #region nucleotide-binding motif B\ !$314-482 #domain ATP-binding cassette homology #label ABC2\ !$320-480 #domain ATP binding #status predicted #label ATP2\ !$331-338 #region nucleotide-binding motif A (P-loop)\ !$430-435 #region nucleotide-binding motif B\ !$44,337 #binding_site ATP (Lys) #status predicted SUMMARY #length 488 #molecular-weight 55912 #checksum 6977 SEQUENCE /// ENTRY YTBST #type complete TITLE tunicamycin resistance protein - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 30-Jun-1989 #sequence_revision 02-Jul-1998 #text_change 19-Jan-2001 ACCESSIONS E69724; JT0240 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69724 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-197 ##label KUN !'##cross-references GB:Z99105; GB:AL009126; NID:g2632457; !1PIDN:CAB12108.1; PID:g2632600 !'##experimental_source strain 168 REFERENCE JT0240 !$#authors Harada, S.; Yoda, K.; Mori, M.; Tanimoto, A.; Furusato, T.; !1Yamane, K.; Takatsuki, A.; Yamasaki, M.; Tamura, G. !$#journal Agric. Biol. Chem. (1988) 52:1785-1789 !$#title The gene responsible for tunicamycin resistance, tmrB, in !1Bacillus subtilis. !$#accession JT0240 !'##molecule_type DNA !'##residues 'MINRKGEMA',1-32,'E',34-197 ##label HAR !'##cross-references DDBJ:D13793; DDBJ:D00343; NID:g216349; !1PIDN:BAA02944.1; PID:g216350; PID:g216351; PID:g216352 !'##note the authors are uncertain which methionine is the initiator REFERENCE A42886 !$#authors Noda, Y.; Yoda, K.; Takatsuki, A.; Yamasaki, M. !$#journal J. Bacteriol. (1992) 174:4302-4307 !$#title TmrB protein, responsible for tunicamycin resistance of !1Bacillus subtilis, is a novel ATP-binding membrane protein. !$#cross-references MUID:92325013; PMID:1624425 !$#contents annotation GENETICS !$#gene tmrB CLASSIFICATION #superfamily tunicamycin resistance protein KEYWORDS antibiotic resistance; ATP binding; nucleotide binding; !1P-loop FEATURE !$7-14 #region nucleotide-binding motif A (P-loop)\ !$180-197 #domain amphipathic helix #status predicted #label !8APH SUMMARY #length 197 #molecular-weight 22729 #checksum 3022 SEQUENCE /// ENTRY IMECE3 #type complete TITLE immunity protein (colicin E3, chain B) - Escherichia coli plasmid ColE3(-CA38) ORGANISM #formal_name Escherichia coli DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 16-Jun-2000 ACCESSIONS B91307; B93470; D00789; S09528; I40690; A03511 REFERENCE A91307 !$#authors Masaki, H.; Ohta, T. !$#journal FEBS Lett. (1982) 149:129-132 !$#title A plasmid region encoding the active fragment and the !1inhibitor protein of colicin E3-CA38. !$#cross-references MUID:83105715; PMID:6295812 !$#accession B91307 !'##molecule_type DNA !'##residues 1-85 ##label MAS1 !'##cross-references GB:J01574; GB:J01575; GB:M14038; GB:X02397; !1NID:g144389; PIDN:AAA88417.1; PID:g144391 REFERENCE A93470 !$#authors Mock, M.; Miyada, C.G.; Gunsalus, R.P. !$#journal Nucleic Acids Res. (1983) 11:3547-3557 !$#title Nucleotide sequence for the catalytic domain of colicin E3 !1and its immunity protein. Evidence for a third gene !1overlapping colicin. !$#cross-references MUID:83220760; PMID:6344012 !$#accession B93470 !'##molecule_type DNA !'##residues 1-85 ##label MOC !'##cross-references GB:J01574; GB:J01575; GB:M14038; GB:X02397; !1NID:g144389; PIDN:AAA88417.1; PID:g144391 REFERENCE A00789 !$#authors Lau, P.C.K.; Rowsome, R.W.; Zuker, M.; Visentin, L.P. !$#journal Nucleic Acids Res. (1984) 12:8733-8745 !$#title Comparative nucleotide sequences encoding the immunity !1proteins and the carboxyl-terminal peptides of colicins E2 !1and E3. !$#cross-references MUID:85062845; PMID:6095211 !$#accession D00789 !'##molecule_type DNA !'##residues 1-85 ##label LAU !'##cross-references GB:X01162; NID:g41802; PIDN:CAA25608.1; !1PID:g1333745 REFERENCE S07269 !$#authors Masaki, H.; Ohta, T. !$#journal J. Mol. Biol. (1985) 182:217-227 !$#title Colicin E3 and its immunity genes. !$#cross-references MUID:85210906; PMID:3889348 !$#accession S09528 !'##molecule_type DNA !'##residues 1-85 ##label MAS2 !'##cross-references EMBL:X02397; NID:g41132; PIDN:CAA26242.1; !1PID:g41134 REFERENCE I40690 !$#authors Lau, P.C.K.; Rowsome, R.W.; Watson, R.J.; Visentin, L.P. !$#journal Biosci. Rep. (1984) 4:565-572 !$#title The immunity genes of colicins E2 and E8 are closely !1related. !$#cross-references MUID:85000799; PMID:6383494 !$#accession I40690 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-85 ##label RES !'##cross-references GB:M26136; NID:g144399; PIDN:AAA98285.1; !1PID:g144400 !'##experimental_source plasmid ColE3-CA38 COMMENT Colicin E3 is a plasmid-specified antibiotic. GENETICS !$#gene ceiC !$#genome plasmid COMPLEX heterodimer of chain A and chain B FUNCTION !$#description inhibits this activity of chain A, which inactivates !1ribosomes by hydrolyzing 16S RNA in 30S ribosomes at a !1specific site; both chains are essential for bactericidal !1activity CLASSIFICATION #superfamily immunity protein (colicin E3, chain B) KEYWORDS bacteriocin immunity SUMMARY #length 85 #molecular-weight 9904 #checksum 5840 SEQUENCE /// ENTRY IMECP3 #type complete TITLE immunity protein - Escherichia coli plasmid CloDF13 ALTERNATE_NAMES protein E ORGANISM #formal_name Escherichia coli DATE 22-May-1981 #sequence_revision 01-Sep-1981 #text_change 16-Jul-1999 ACCESSIONS A93250; A93710; B28585; A03514 REFERENCE A93250 !$#authors Stuitje, A.R.; Spelt, C.E.; Veltkamp, E.; Nijkamp, H.J.J. !$#journal Nature (1981) 290:264-267 !$#title Identification of mutations affecting replication control of !1plasmid Clo DF13. !$#cross-references MUID:81148852; PMID:6163089 !$#accession A93250 !'##molecule_type DNA !'##residues 1-85 ##label STU !'##cross-references GB:X04466; GB:J01560; NID:g42320; PIDN:CAA28146.1; !1PID:g42322 REFERENCE A93710 !$#authors van den Elzen, P.J.M.; Gaastra, W.; Spelt, C.E.; de Graaf, !1F.K.; Veltkamp, E.; Nijkamp, H.J.J. !$#journal Nucleic Acids Res. (1980) 8:4349-4363 !$#title Molecular structure of the immunity gene and immunity !1protein of the bacteriocinogenic plasmid Clo DF13. !$#cross-references MUID:81053773; PMID:6253914 !$#accession A93710 !'##molecule_type DNA !'##residues 1-85 ##label VAN !'##cross-references GB:X04466; GB:J01559; NID:g42320; PIDN:CAA28146.1; !1PID:g42322 !'##note this sequence was partially confirmed by amino acid analysis REFERENCE A93765 !$#authors Nijkamp, H.J.J.; de Lang, R.; Stuitje, A.R.; van den Elzen, !1P.J.M.; Veltkamp, E.; van Putten, A.J. !$#journal Plasmid (1986) 16:135-160 !$#title The complete nucleotide sequence of the bacteriocinogenic !1plasmid CloDF13. !$#cross-references MUID:86314306; PMID:3749334 !$#accession B28585 !'##molecule_type DNA !'##residues 1-85 ##label NIJ !'##cross-references GB:X04466; GB:X00141; NID:g42320; PIDN:CAA28146.1; !1PID:g42322 !'##experimental_source strain K12 P678-54 COMMENT This protein complexes with cloacin in equimolar amounts and !1inhibits it. COMMENT Plasmid CloDF13 originates from Enterobacter cloacae but is !1stably maintained in and studied mostly from E. coli. GENETICS !$#gene cim !$#genome plasmid !$#start_codon GTG CLASSIFICATION #superfamily immunity protein (colicin E3, chain B) KEYWORDS bacteriocin immunity; methylated amino acid FEATURE !$12 #modified_site N6-methyllysine (Lys) #status !8predicted SUMMARY #length 85 #molecular-weight 10004 #checksum 7552 SEQUENCE /// ENTRY IMECE2 #type complete TITLE colicin E2 immunity protein - Escherichia coli plasmids ORGANISM #formal_name Escherichia coli DATE 17-Mar-1987 #sequence_revision 23-Aug-1996 #text_change 16-Jun-2000 ACCESSIONS A03512; A23019; PQ0033; I40688 REFERENCE A00789 !$#authors Lau, P.C.K.; Rowsome, R.W.; Zuker, M.; Visentin, L.P. !$#journal Nucleic Acids Res. (1984) 12:8733-8745 !$#title Comparative nucleotide sequences encoding the immunity !1proteins and the carboxyl-terminal peptides of colicins E2 !1and E3. !$#cross-references MUID:85062845; PMID:6095211 !$#accession A03512 !'##molecule_type DNA !'##residues 1-86 ##label LAU !'##cross-references GB:X01163; NID:g41800; PIDN:CAA25610.1; !1PID:g1333744 REFERENCE A23019 !$#authors Masaki, H.; Toba, M.; Ohta, T. !$#journal Nucleic Acids Res. (1985) 13:1623-1635 !$#title Structure and expression of the ColE2-P9 immunity gene. !$#cross-references MUID:85215569; PMID:2987833 !$#accession A23019 !'##molecule_type DNA !'##residues 1-86 ##label MAS1 !'##cross-references GB:X02227; NID:g41130; PIDN:CAA26146.1; PID:g41131 !'##experimental_source plasmid ColE2-P9 REFERENCE JQ0326 !$#authors Lau, P.C.K.; Condie, J.A. !$#journal Mol. Gen. Genet. (1989) 217:269-277 !$#title Nucleotide sequences from the colicin E5, E6 and E9 operons: !1presence of a degenerate transposon-like structure in the !1ColE9-J plasmid. !$#cross-references MUID:89364708; PMID:2549375 !$#accession PQ0033 !'##molecule_type DNA !'##residues 1-9 ##label LA2 !'##cross-references EMBL:X15858 !'##experimental_source strain W3110, plasmid ColE9-J !'##note this plasmid-coded protein is released as an equimolar complex !1with the bactericidal colicin E2 protein REFERENCE I40687 !$#authors Cole, S.T.; Saint-Joanis, B.; Pugsley, A.P. !$#journal Mol. Gen. Genet. (1985) 198:465-472 !$#title Molecular characterisation of the colicin E2 operon and !1identification of its products. !$#cross-references MUID:85239907; PMID:3892228 !$#accession I40688 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-86 ##label RES !'##cross-references GB:M29885; NID:g144366; PIDN:AAA23069.1; !1PID:g144368 !'##experimental_source plasmid ColE2 GENETICS !$#gene imm; ceiB !$#genome plasmid FUNCTION !$#description to protect the colicinogenic cells from the lethal action of !1their own toxin CLASSIFICATION #superfamily immunity protein E2 KEYWORDS bacteriocin immunity SUMMARY #length 86 #molecular-weight 9995 #checksum 7231 SEQUENCE /// ENTRY IMECE8 #type complete TITLE colicin E8 immunity protein - Escherichia coli plasmid ColE8-J ALTERNATE_NAMES colicin E8 complex, protein B ORGANISM #formal_name Escherichia coli DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jul-1999 ACCESSIONS B28184; S01081 REFERENCE A91874 !$#authors Toba, M.; Masaki, H.; Ohta, T. !$#journal J. Bacteriol. (1988) 170:3237-3242 !$#title Colicin E8, a DNase which indicates an evolutionary !1relationship between colicins E2 and E3. !$#cross-references MUID:88257046; PMID:3290201 !$#accession B28184 !'##molecule_type DNA !'##residues 1-85 ##label TOB !'##cross-references GB:M21404; NID:g144380; PIDN:AAA23074.1; !1PID:g144382 REFERENCE S01080 !$#authors Uchimura, T.; Lau, P.C.K. !$#journal Mol. Gen. Genet. (1987) 209:489-493 !$#title Nucleotide sequences from the colicin E8 operon: homology !1with plasmid ColE2-P9. !$#cross-references MUID:88121677; PMID:3323826 !$#accession S01081 !'##molecule_type DNA !'##residues 1-85 ##label UCH !'##cross-references EMBL:X06119; NID:g41136; PIDN:CAA29492.1; !1PID:g41137 GENETICS !$#gene imm !$#genome plasmid CLASSIFICATION #superfamily immunity protein E2 KEYWORDS bacteriocin immunity SUMMARY #length 85 #molecular-weight 9622 #checksum 4784 SEQUENCE /// ENTRY IMECE1 #type complete TITLE colicin E1 immunity protein - Escherichia coli plasmid colicin E1 ORGANISM #formal_name Escherichia coli DATE 02-Apr-1982 #sequence_revision 02-Apr-1982 #text_change 24-Sep-1999 ACCESSIONS A94079; B93118; I54985; A03513; A24685 REFERENCE A94079 !$#authors Waleh, N.S.; Johnson, P.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:8389-8393 !$#title Structural and functional organization of the colicin E1 !1operon. !$#cross-references MUID:86094231; PMID:3936034 !$#accession A94079 !'##molecule_type DNA !'##residues 1-113 ##label WAL REFERENCE A93118 !$#authors Oka, A.; Nomura, N.; Morita, M.; Sugisaki, H.; Sugimoto, K.; !1Takanami, M. !$#journal Mol. Gen. Genet. (1979) 172:151-159 !$#title Nucleotide sequence of small CoIE1 derivitives: structure of !1the regions essential for autonomous replication and colicin !1E1 immunity. !$#cross-references MUID:80010893; PMID:384144 !$#accession B93118 !'##molecule_type DNA !'##residues 1-113 ##label OKA !'##cross-references GB:V00268; NID:g41124; PIDN:CAA23529.1; PID:g41125 !'##note plasmid pAO3 is a small col E1 derivative REFERENCE I54985 !$#authors Jilk, R.A.; Makris, J.C.; Borchardt, L.; Reznikoff, W.S. !$#journal J. Bacteriol. (1993) 175:1264-1271 !$#title Implications of Tn5-associated adjacent deletions. !$#cross-references MUID:93186691; PMID:8383110 !$#accession I54985 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-113 ##label RES !'##cross-references GB:S56312; NID:g298343 GENETICS !$#gene imm !$#map_position 75-100/0-1 !$#genome plasmid CLASSIFICATION #superfamily colicin E1 immunity protein SUMMARY #length 113 #molecular-weight 13287 #checksum 8794 SEQUENCE /// ENTRY IKEC5I #type complete TITLE colicin V immunity protein - Escherichia coli plasmid ColV ORGANISM #formal_name Escherichia coli DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jul-1999 ACCESSIONS S12273 REFERENCE S12271 !$#authors Gilson, L.; Mahanty, H.K.; Kolter, R. !$#journal EMBO J. (1990) 9:3875-3884 !$#title Genetic analysis of an MDR-like export system: the secretion !1of colicin V. !$#cross-references MUID:91065315; PMID:2249654 !$#accession S12273 !'##molecule_type DNA !'##residues 1-78 ##label GIL !'##cross-references EMBL:X57525; NID:g41177; PIDN:CAA40745.1; !1PID:g41178 GENETICS !$#gene cvi !$#genome plasmid CLASSIFICATION #superfamily colicin V immunity protein SUMMARY #length 78 #molecular-weight 9102 #checksum 1268 SEQUENCE /// ENTRY IMECB #type complete TITLE colicin B immunity protein - Escherichia coli plasmid ColBM ORGANISM #formal_name Escherichia coli DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Jul-1999 ACCESSIONS S06459 REFERENCE S06459 !$#authors Schramm, E.; Oelschlaeger, T.; Troeger, W.; Braun, V. !$#journal Mol. Gen. Genet. (1988) 211:176-182 !$#title Sequence, expression and localization of the immunity !1protein for colicin B. !$#cross-references MUID:88142567; PMID:2830463 !$#accession S06459 !'##molecule_type DNA !'##residues 1-175 ##label SCH !'##cross-references GB:M36645; NID:g145465; PIDN:AAA23540.1; !1PID:g145466 GENETICS !$#gene cbi !$#genome plasmid CLASSIFICATION #superfamily colicin N immunity protein KEYWORDS transmembrane protein FEATURE !$14-32 #domain transmembrane #status predicted #label TM1\ !$104-121 #domain transmembrane #status predicted #label TM2\ !$149-168 #domain transmembrane #status predicted #label TM3 SUMMARY #length 175 #molecular-weight 20186 #checksum 6813 SEQUENCE /// ENTRY IMEBAC #type complete TITLE colicin A immunity protein - Citrobacter freundii (strain CA31) plasmid ColA ORGANISM #formal_name Citrobacter freundii DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Jul-1999 ACCESSIONS S07230; I40785 REFERENCE S07230 !$#authors Lloubes, R.P.; Chartier, M.J.; Journet, A.M.; Varenne, S.G.; !1Lazdunski, C.J. !$#journal Eur. J. Biochem. (1984) 144:73-78 !$#title Nucleotide sequence of the gene for the immunity protein to !1colicin A. Analysis of codon usage of immunity proteins as !1compared to colicins. !$#cross-references MUID:85003668; PMID:6383827 !$#accession S07230 !'##molecule_type DNA !'##residues 1-178 ##label LLO !'##cross-references EMBL:X00964; NID:g40461; PIDN:CAA25476.1; !1PID:g40462 REFERENCE I40778 !$#authors Morlon, J.; Chartier, M.; Bidaud, M.; Lazdunski, C. !$#journal Mol. Gen. Genet. (1988) 211:231-243 !$#title The complete nucleotide sequence of the colicinogenic !1plasmid ColA. High extent of homology with ColE1. !$#cross-references MUID:88174422; PMID:2832701 !$#accession I40785 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-178 ##label RES !'##cross-references GB:M37402; NID:g144661; PIDN:AAA72880.1; !1PID:g144668 !'##experimental_source plasmid ColA GENETICS !$#gene cai !$#genome plasmid CLASSIFICATION #superfamily colicin N immunity protein KEYWORDS bacteriocin immunity; transmembrane protein FEATURE !$1-13 #domain intracellular #status predicted #label INT1\ !$14-37 #domain transmembrane #status predicted #label TM1\ !$69-89 #domain transmembrane #status predicted #label TM2\ !$107-123 #domain transmembrane #status predicted #label TM3\ !$143-165 #domain transmembrane #status predicted #label TM4\ !$166-178 #domain intracellular #status predicted #label INT2 SUMMARY #length 178 #molecular-weight 20463 #checksum 5771 SEQUENCE /// ENTRY IMECN4 #type complete TITLE colicin N immunity protein - Escherichia coli plasmid pCHAP4 ORGANISM #formal_name Escherichia coli DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Jul-1999 ACCESSIONS S01761 REFERENCE S01760 !$#authors Pugsley, A.P. !$#journal Mol. Gen. Genet. (1988) 211:335-341 !$#title The immunity and lysis genes of ColN plasmid pCHAP4. !$#cross-references MUID:88174431; PMID:3280946 !$#accession S01761 !'##molecule_type DNA !'##residues 1-131 ##label PUG !'##cross-references EMBL:X06933; NID:g41117; PIDN:CAA30020.1; !1PID:g41119 !'##note the authors translated the codon ACC for residue 42 as Ile and !1GTT for residue 104 as Phe GENETICS !$#gene cni !$#genome plasmid CLASSIFICATION #superfamily colicin N immunity protein KEYWORDS transmembrane protein FEATURE !$66-84 #domain transmembrane #status predicted #label TM1 SUMMARY #length 131 #molecular-weight 15245 #checksum 6528 SEQUENCE /// ENTRY ZHECN4 #type complete TITLE colicin N lysis protein precursor - Escherichia coli plasmid pCHAP4 ORGANISM #formal_name Escherichia coli DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Jul-1999 ACCESSIONS S01760 REFERENCE S01760 !$#authors Pugsley, A.P. !$#journal Mol. Gen. Genet. (1988) 211:335-341 !$#title The immunity and lysis genes of ColN plasmid pCHAP4. !$#cross-references MUID:88174431; PMID:3280946 !$#accession S01760 !'##molecule_type DNA !'##residues 1-52 ##label PUG !'##cross-references EMBL:X06933; NID:g41117; PIDN:CAA30019.1; !1PID:g41118 !'##note the authors translated the codon ATC for residue 23 as Ala GENETICS !$#gene cnl !$#genome plasmid CLASSIFICATION #superfamily colicin E1 lysis protein KEYWORDS blocked amino end; host cell lysis; lipoprotein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-52 #product colicin N lysis protein #status experimental !8#label MAT\ !$18 #modified_site fatty acylated amino end (Cys) (in !8mature form) #status experimental\ !$18 #binding_site sn-2,3-diacylglycerol (Cys) (covalent) !8#status predicted SUMMARY #length 52 #molecular-weight 5633 #checksum 6717 SEQUENCE /// ENTRY ZHECP1 #type complete TITLE colicin E1 lysis protein precursor - Escherichia coli plasmid ColE1 ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 22-Jun-1999 ACCESSIONS B24685 REFERENCE A94079 !$#authors Waleh, N.S.; Johnson, P.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:8389-8393 !$#title Structural and functional organization of the colicin E1 !1operon. !$#cross-references MUID:86094231; PMID:3936034 !$#accession B24685 !'##molecule_type DNA !'##residues 1-45 ##label WAL !'##cross-references GB:M12543; NID:g144303; PIDN:AAA23067.1; !1PID:g144306 COMMENT This protein is responsible for the death of colicinogenic !1bacteria when induced with UV light or mitomycin C. This !1mitomycin C-induced lethality function also causes !1nonspecific membrane damage and delayed cellular enzyme !1linkage. GENETICS !$#gene lys !$#genome plasmid CLASSIFICATION #superfamily colicin E1 lysis protein KEYWORDS blocked amino end; host cell lysis; lipoprotein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-45 #product colicin E1 lysis protein #status predicted !8#label MAT\ !$18 #binding_site sn-2,3-diacylglycerol (Cys) (covalent) !8#status predicted\ !$18 #modified_site fatty acylated amino end (Cys) (in !8mature form) #status predicted SUMMARY #length 45 #molecular-weight 4829 #checksum 9605 SEQUENCE /// ENTRY ZHECP3 #type complete TITLE colicin lysis protein precursor - Escherichia coli plasmid CloDF13 ALTERNATE_NAMES protein H ORGANISM #formal_name Escherichia coli DATE 29-Jul-1981 #sequence_revision 01-Sep-1981 #text_change 16-Jul-1999 ACCESSIONS A03515; A28585 REFERENCE A93250 !$#authors Stuitje, A.R.; Spelt, C.E.; Veltkamp, E.; Nijkamp, H.J.J. !$#journal Nature (1981) 290:264-267 !$#title Identification of mutations affecting replication control of !1plasmid Clo DF13. !$#cross-references MUID:81148852; PMID:6163089 !$#accession A03515 !'##molecule_type DNA !'##residues 1-49 ##label STU !'##cross-references GB:X04466; GB:J01560; NID:g42320; PIDN:CAA28145.1; !1PID:g42321 REFERENCE A93765 !$#authors Nijkamp, H.J.J.; de Lang, R.; Stuitje, A.R.; van den Elzen, !1P.J.M.; Veltkamp, E.; van Putten, A.J. !$#journal Plasmid (1986) 16:135-160 !$#title The complete nucleotide sequence of the bacteriocinogenic !1plasmid CloDF13. !$#cross-references MUID:86314306; PMID:3749334 !$#accession A28585 !'##molecule_type DNA !'##residues 1-49 ##label NIJ !'##cross-references GB:X04466; GB:X00141; NID:g42320; PIDN:CAA28145.1; !1PID:g42321 !'##experimental_source strain K12 P678-54 COMMENT Plasmid CloDF13 originates from Enterobacter cloacae but is !1stably maintained in and studied mostly from E. coli. GENETICS !$#gene cex !$#genome plasmid CLASSIFICATION #superfamily colicin E1 lysis protein KEYWORDS blocked amino end; host cell lysis; lipoprotein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-49 #product colicin E1 lysis protein #status predicted !8#label MAT\ !$22 #binding_site sn-2,3-diacylglycerol (Cys) (covalent) !8#status predicted\ !$22 #modified_site fatty acylated amino end (Cys) (in !8mature form) #status predicted SUMMARY #length 49 #molecular-weight 5157 #checksum 4221 SEQUENCE /// ENTRY BVECH8 #type complete TITLE hic lysis protein precursor - Escherichia coli plasmids ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 24-Sep-1999 ACCESSIONS A91514; JS0004; S09529; I40689; A22383; A25639 REFERENCE A91514 !$#authors Watson, R.J.; Lau, P.C.K.; Vernet, T.; Visentin, L.P. !$#journal Gene (1984) 29:175-184 !$#title Characterization and nucleotide sequence of a !1colicin-release gene in the hic region of plasmid !1ColE3-CA38. !$#cross-references MUID:85028427; PMID:6092219 !$#accession A91514 !'##molecule_type DNA !'##residues 1-47 ##label WAT !'##cross-references GB:J01574; GB:J01575; GB:M14038; GB:X02397; !1NID:g144389; PIDN:AAA88419.1; PID:g144393 !'##experimental_source ColE3-CA38 REFERENCE A91547 !$#authors Watson, R.J.; Lau, P.C.K.; Vernet, T.; Visentin, L.P. !$#journal Gene (1986) 42:351-353 !$#contents annotation; erratum REFERENCE JS0004 !$#authors Toba, M.; Masaki, H.; Ohta, T. !$#journal J. Biochem. (1986) 99:591-596 !$#title Primary structure of the ColE2-P9 and ColE3-CA38 lysis !1genes. !$#cross-references MUID:86195936; PMID:3516985 !$#accession JS0004 !'##molecule_type DNA !'##residues 1-47 ##label TOB !'##cross-references GB:X03632; GB:D00020; GB:N00020; NID:g41939; !1PIDN:CAA27282.1; PID:g41940 !'##experimental_source ColE2-P9 !'##note this sequence is highly homologous to the lysis protein of DF13 !1and ColE1 REFERENCE S07269 !$#authors Masaki, H.; Ohta, T. !$#journal J. Mol. Biol. (1985) 182:217-227 !$#title Colicin E3 and its immunity genes. !$#cross-references MUID:85210906; PMID:3889348 !$#accession S09529 !'##status preliminary !'##molecule_type DNA !'##residues 1-38 ##label MAS !'##cross-references EMBL:X02397; NID:g41132; PIDN:CAA26243.1; !1PID:g41135 !'##experimental_source ColE3 REFERENCE I40687 !$#authors Cole, S.T.; Saint-Joanis, B.; Pugsley, A.P. !$#journal Mol. Gen. Genet. (1985) 198:465-472 !$#title Molecular characterisation of the colicin E2 operon and !1identification of its products. !$#cross-references MUID:85239907; PMID:3892228 !$#accession I40689 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-47 ##label RES !'##cross-references GB:M29885; NID:g144366; PIDN:AAA23070.1; !1PID:g144369 !'##experimental_source plasmid ColE2 GENETICS !$#gene hic; celB !$#genome plasmid FUNCTION !$#description required for high colicin production, which occurs only !1after activation of the host SOS system; this colicin !1induction is accompanied by increased synthesis of immunity !1protein (which protects the host cell from the lethal !1activity of its own colicin), reduction of host-cell protein !1synthesis (which leads to cell death), and release of large !1amounts of colicin-immunity protein complex; its function is !1related to phospholipase A of the host cell CLASSIFICATION #superfamily colicin E1 lysis protein KEYWORDS blocked amino end; host cell lysis; lipoprotein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-47 #product hic lysis protein #status predicted #label !8MAT\ !$20 #binding_site sn-2,3-diacylglycerol (Cys) (covalent) !8#status predicted\ !$20 #modified_site fatty acylated amino end (Cys) (in !8mature form) #status predicted SUMMARY #length 47 #molecular-weight 4860 #checksum 7233 SEQUENCE /// ENTRY ZHECE8 #type complete TITLE colicin E8 lysis protein precursor - Escherichia coli plasmid ColE8-J ORGANISM #formal_name Escherichia coli DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jul-1999 ACCESSIONS C28184; S01082 REFERENCE A91874 !$#authors Toba, M.; Masaki, H.; Ohta, T. !$#journal J. Bacteriol. (1988) 170:3237-3242 !$#title Colicin E8, a DNase which indicates an evolutionary !1relationship between colicins E2 and E3. !$#cross-references MUID:88257046; PMID:3290201 !$#accession C28184 !'##molecule_type DNA !'##residues 1-47 ##label TOB !'##cross-references GB:M21404; NID:g144380; PIDN:AAA23075.1; !1PID:g144383 REFERENCE S01080 !$#authors Uchimura, T.; Lau, P.C.K. !$#journal Mol. Gen. Genet. (1987) 209:489-493 !$#title Nucleotide sequences from the colicin E8 operon: homology !1with plasmid ColE2-P9. !$#cross-references MUID:88121677; PMID:3323826 !$#accession S01082 !'##molecule_type DNA !'##residues 1-47 ##label UCH !'##cross-references EMBL:X06119; NID:g41136; PIDN:CAA29493.1; !1PID:g41138 GENETICS !$#gene lys !$#genome plasmid CLASSIFICATION #superfamily colicin E1 lysis protein KEYWORDS blocked amino end; host cell lysis; lipoprotein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-47 #product colicin E8 lysis protein #status predicted !8#label MAT\ !$20 #modified_site fatty acylated amino end (Cys) (in !8mature form) #status predicted\ !$20 #binding_site sn-2,3-diacylglycerol (Cys) (covalent) !8#status predicted SUMMARY #length 47 #molecular-weight 4844 #checksum 6909 SEQUENCE /// ENTRY D32535 #type complete TITLE colicin E5 lysis protein precursor - Escherichia coli plasmid ColE9-J ORGANISM #formal_name Escherichia coli DATE 21-May-1990 #sequence_revision 25-Apr-1997 #text_change 22-Jun-1999 ACCESSIONS D32535 REFERENCE A92786 !$#authors James, R.; Jarvis, M.; Barker, D.F. !$#journal J. Gen. Microbiol. (1987) 133:1553-1562 !$#title Nucleotide sequence of the immunity and lysis region of the !1ColE9-J plasmid. !$#cross-references MUID:88034907; PMID:3312476 !$#accession D32535 !'##molecule_type DNA !'##residues 1-47 ##label JAM !'##cross-references GB:M16803; NID:g144384; PIDN:AAA23079.1; !1PID:g144388 COMMENT This protein activates the detergent-resistant phospholipase !1A of the colicinogenic bacterium to lyse the cell and !1release the colicin. GENETICS !$#gene lys; cal !$#genome plasmid CLASSIFICATION #superfamily colicin E1 lysis protein KEYWORDS blocked amino end; host cell lysis; lipoprotein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-47 #product colicin E5 lysis protein #status predicted !8#label MAT\ !$20 #binding_site sn-2,3-diacylglycerol (Cys) (covalent) !8#status predicted\ !$20 #modified_site fatty acylated amino end (Cys) (in !8mature form) #status predicted SUMMARY #length 47 #molecular-weight 4816 #checksum 6167 SEQUENCE /// ENTRY JQ0330 #type complete TITLE colicin E5 lysis protein precursor - Escherichia coli plasmid ColE5-099 ORGANISM #formal_name Escherichia coli DATE 07-Sep-1990 #sequence_revision 25-Apr-1997 #text_change 16-Jul-1999 ACCESSIONS JQ0330; C45799 REFERENCE JQ0326 !$#authors Lau, P.C.K.; Condie, J.A. !$#journal Mol. Gen. Genet. (1989) 217:269-277 !$#title Nucleotide sequences from the colicin E5, E6 and E9 operons: !1presence of a degenerate transposon-like structure in the !1ColE9-J plasmid. !$#cross-references MUID:89364708; PMID:2549375 !$#accession JQ0330 !'##molecule_type DNA !'##residues 1-47 ##label LAU !'##cross-references EMBL:X15857; NID:g40541; PIDN:CAA33861.1; !1PID:g40543 !'##experimental_source strain WA802 REFERENCE A45799 !$#authors Curtis, M.D.; James, R.; Coddington, A. !$#journal J. Gen. Microbiol. (1989) 135:2783-2788 !$#title An evolutionary relationship between the ColE5-099 and the !1ColE9-J plasmids revealed by nucleotide sequencing. !$#cross-references MUID:90218006; PMID:2561131 !$#accession C45799 !'##status preliminary !'##molecule_type DNA !'##residues 1-47 ##label CUR !'##cross-references GB:M30445; NID:g144370; PIDN:AAA98053.1; !1PID:g144373 COMMENT This protein activates the detergent-resistant phospholipase !1A of the colicinogenic bacterium to lyse the cell and !1release the colicin. GENETICS !$#gene lys; cal !$#genome plasmid CLASSIFICATION #superfamily colicin E1 lysis protein KEYWORDS blocked amino end; host cell lysis; lipoprotein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-47 #product colicin E5 lysis protein #status predicted !8#label MAT\ !$20 #binding_site sn-2,3-diacylglycerol (Cys) (covalent) !8#status predicted\ !$20 #modified_site fatty acylated amino end (Cys) (in !8mature form) #status predicted SUMMARY #length 47 #molecular-weight 4926 #checksum 6003 SEQUENCE /// ENTRY JQ0328 #type complete TITLE colicin E6 lysis protein precursor - Escherichia coli plasmid ColE6-CT14 ORGANISM #formal_name Escherichia coli DATE 07-Sep-1990 #sequence_revision 25-Apr-1997 #text_change 16-Jul-1999 ACCESSIONS JQ0328; D43716 REFERENCE JQ0326 !$#authors Lau, P.C.K.; Condie, J.A. !$#journal Mol. Gen. Genet. (1989) 217:269-277 !$#title Nucleotide sequences from the colicin E5, E6 and E9 operons: !1presence of a degenerate transposon-like structure in the !1ColE9-J plasmid. !$#cross-references MUID:89364708; PMID:2549375 !$#accession JQ0328 !'##molecule_type DNA !'##residues 1-47 ##label LAU !'##cross-references EMBL:X15856; NID:g40544; PIDN:CAA33858.1; !1PID:g40547 !'##experimental_source strain WA802 REFERENCE A43716 !$#authors Akutsu, A.; Masaki, H.; Ohta, T. !$#journal J. Bacteriol. (1989) 171:6430-6436 !$#title Molecular structure and immunity specificity of colicin E6, !1an evolutionary intermediate between E-group colicins and !1cloacin DF13. !$#cross-references MUID:90078082; PMID:2687234 !$#accession D43716 !'##status preliminary !'##molecule_type DNA !'##residues 1-47 ##label AKU !'##cross-references GB:J01574; GB:J01575; GB:M14038; GB:X02397 COMMENT This protein activates the detergent-resistant phospholipase !1A of the colicinogenic bacterium to lyse the cell and !1release the colicin. GENETICS !$#gene lys; cal !$#genome plasmid CLASSIFICATION #superfamily colicin E1 lysis protein KEYWORDS blocked amino end; host cell lysis; lipoprotein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-47 #product colicin E6 lysis protein #status predicted !8#label MAT\ !$20 #binding_site sn-2,3-diacylglycerol (Cys) (covalent) !8#status predicted\ !$20 #modified_site fatty acylated amino end (Cys) (in !8mature form) #status predicted SUMMARY #length 47 #molecular-weight 4902 #checksum 7119 SEQUENCE /// ENTRY S27395 #type complete TITLE colicin E7 lysis protein precursor - Escherichia coli plasmid ColE7 ORGANISM #formal_name Escherichia coli DATE 22-Nov-1993 #sequence_revision 25-Apr-1997 #text_change 16-Jul-1999 ACCESSIONS S27395; S49181 REFERENCE S27394 !$#authors Chak, K.F.; Kuo, W.S.; Lu, F.M.; James, R. !$#journal J. Gen. Microbiol. (1991) 137:91-100 !$#title Cloning and characterization of the ColE7 plasmid. !$#cross-references MUID:91259043; PMID:2045785 !$#accession S27395 !'##status preliminary !'##molecule_type DNA !'##residues 1-47 ##label CHA !'##cross-references EMBL:M57540; NID:g144377; PIDN:AAA23072.1; !1PID:g144379 REFERENCE S49176 !$#authors Lau, P.C.K.; Parsons, M. !$#submission submitted to the EMBL Data Library, December 1991 !$#description Nucleotide sequence encoding the immunity and lysis proteins !1and the carboxyl terminl peptides of colicins E4 and E7. !$#accession S49181 !'##status preliminary !'##molecule_type DNA !'##residues 1-47 ##label LAU !'##cross-references EMBL:X63620; NID:g510384; PIDN:CAA45166.1; !1PID:g510386 COMMENT This protein activates the detergent-resistant phospholipase !1A of the colicinogenic bacterium to lyse the cell and !1release the colicin. GENETICS !$#gene lys; cal !$#genome plasmid CLASSIFICATION #superfamily colicin E1 lysis protein KEYWORDS blocked amino end; host cell lysis; lipoprotein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-47 #product colicin E7 lysis protein #status predicted !8#label MAT\ !$20 #binding_site sn-2,3-diacylglycerol (Cys) (covalent) !8#status predicted\ !$20 #modified_site fatty acylated amino end (Cys) (in !8mature form) #status predicted SUMMARY #length 47 #molecular-weight 4874 #checksum 6825 SEQUENCE /// ENTRY S49178 #type complete TITLE colicin E4 lysis protein precursor - Escherichia coli plasmid colE4 ORGANISM #formal_name Escherichia coli DATE 16-Feb-1995 #sequence_revision 25-Apr-1997 #text_change 16-Jul-1999 ACCESSIONS S49178 REFERENCE S49176 !$#authors Lau, P.C.K.; Parsons, M. !$#submission submitted to the EMBL Data Library, December 1991 !$#description Nucleotide sequence encoding the immunity and lysis proteins !1and the carboxyl terminl peptides of colicins E4 and E7. !$#accession S49178 !'##molecule_type DNA !'##residues 1-47 ##label LAU !'##cross-references EMBL:X63621; NID:g510380; PIDN:CAA45169.1; !1PID:g510383 COMMENT This protein activates the detergent-resistant phospholipase !1A of the colicinogenic bacterium to lyse the cell and !1release the colicin. GENETICS !$#gene lys; cal !$#genome plasmid CLASSIFICATION #superfamily colicin E1 lysis protein KEYWORDS blocked amino end; host cell lysis; lipoprotein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-47 #product colicin E4 lysis protein #status predicted !8#label MAT\ !$20 #binding_site sn-2,3-diacylglycerol (Cys) (covalent) !8#status predicted\ !$20 #modified_site fatty acylated amino end (Cys) (in !8mature form) #status predicted SUMMARY #length 47 #molecular-weight 4908 #checksum 6753 SEQUENCE /// ENTRY S07307 #type complete TITLE colicin A lysis protein precursor - Citrobacter freundii (strain CA31) plasmid ColA ORGANISM #formal_name Citrobacter freundii DATE 12-Feb-1993 #sequence_revision 25-Apr-1997 #text_change 16-Jul-1999 ACCESSIONS S07307; I40786 REFERENCE S07307 !$#authors Cavard, D.; Lloubes, R.; Morlon, J.; Chartier, M.; !1Lazdunski, C. !$#journal Mol. Gen. Genet. (1985) 199:95-100 !$#title Lysis protein encoded by plasmid ColA-CA31. Gene sequence !1and export. !$#cross-references MUID:85213115; PMID:3889552 !$#accession S07307 !'##molecule_type DNA !'##residues 1-51 ##label CAV !'##cross-references EMBL:X02391; NID:g41076; PIDN:CAA26233.1; !1PID:g41077 REFERENCE I40778 !$#authors Morlon, J.; Chartier, M.; Bidaud, M.; Lazdunski, C. !$#journal Mol. Gen. Genet. (1988) 211:231-243 !$#title The complete nucleotide sequence of the colicinogenic !1plasmid ColA. High extent of homology with ColE1. !$#cross-references MUID:88174422; PMID:2832701 !$#accession I40786 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-51 ##label RES !'##cross-references GB:M37402; NID:g144661; PIDN:AAA72881.1; !1PID:g144669 !'##experimental_source plasmid ColA COMMENT This protein activates the detergent-resistant phospholipase !1A of the colicinogenic bacterium to lyse the cell and !1release the colicin. GENETICS !$#gene cal !$#genome plasmid CLASSIFICATION #superfamily colicin E1 lysis protein KEYWORDS blocked amino end; host cell lysis; lipoprotein FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-51 #product colicin A lysis protein #status predicted !8#label MAT\ !$19 #modified_site fatty acylated amino end (Cys) (in !8mature form) #status predicted\ !$19 #binding_site sn-2,3-diacylglycerol (Cys) (covalent) !8#status predicted SUMMARY #length 51 #molecular-weight 5088 #checksum 2927 SEQUENCE /// ENTRY QVECK #type complete TITLE protein K - Escherichia coli plasmid CloDF13 ORGANISM #formal_name Escherichia coli DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 16-Jul-1999 ACCESSIONS A03516; D28585 REFERENCE A93500 !$#authors van den Elzen, P.J.M.; Hakkaart, M.J.J.; van Putten, A.J.; !1Walters, H.H.B.; Veltkamp, E.; Nijkamp, H.J.J. !$#journal Nucleic Acids Res. (1983) 11:8791-8808 !$#title Structure and regulation of gene expression of a Clo DF13 !1plasmid DNA region involved in plasmid segregation and !1incompatibility. !$#cross-references MUID:84169516; PMID:6324101 !$#accession A03516 !'##molecule_type DNA !'##residues 1-188 ##label VAN !'##cross-references GB:X04466; GB:M23861; NID:g42320; PIDN:CAA28148.1; !1PID:g42324 !'##note the authors translated the codon TGG for residue 136 as Thr REFERENCE A93765 !$#authors Nijkamp, H.J.J.; de Lang, R.; Stuitje, A.R.; van den Elzen, !1P.J.M.; Veltkamp, E.; van Putten, A.J. !$#journal Plasmid (1986) 16:135-160 !$#title The complete nucleotide sequence of the bacteriocinogenic !1plasmid CloDF13. !$#cross-references MUID:86314306; PMID:3749334 !$#accession D28585 !'##molecule_type DNA !'##residues 1-188 ##label NIJ !'##cross-references GB:X04466; GB:X00141; NID:g42320; PIDN:CAA28148.1; !1PID:g42324 !'##experimental_source strain K12 P678-54 !'##note the authors translated the codon AAA for residue 145 as Asn GENETICS !$#gene cun !$#map_position 37.3-43% of the plasmid genome !$#genome plasmid CLASSIFICATION #superfamily CloDF13 protein K SUMMARY #length 188 #molecular-weight 21305 #checksum 592 SEQUENCE /// ENTRY QVECL #type complete TITLE protein L - Escherichia coli plasmid CloDF13 ORGANISM #formal_name Escherichia coli DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 16-Jul-1999 ACCESSIONS A03517; E28585 REFERENCE A93500 !$#authors van den Elzen, P.J.M.; Hakkaart, M.J.J.; van Putten, A.J.; !1Walters, H.H.B.; Veltkamp, E.; Nijkamp, H.J.J. !$#journal Nucleic Acids Res. (1983) 11:8791-8808 !$#title Structure and regulation of gene expression of a Clo DF13 !1plasmid DNA region involved in plasmid segregation and !1incompatibility. !$#cross-references MUID:84169516; PMID:6324101 !$#accession A03517 !'##molecule_type DNA !'##residues 1-87 ##label VAN !'##cross-references GB:X04466; GB:M23861; NID:g42320; PIDN:CAA28149.1; !1PID:g42325 REFERENCE A93765 !$#authors Nijkamp, H.J.J.; de Lang, R.; Stuitje, A.R.; van den Elzen, !1P.J.M.; Veltkamp, E.; van Putten, A.J. !$#journal Plasmid (1986) 16:135-160 !$#title The complete nucleotide sequence of the bacteriocinogenic !1plasmid CloDF13. !$#cross-references MUID:86314306; PMID:3749334 !$#accession E28585 !'##molecule_type DNA !'##residues 1-87 ##label NIJ !'##cross-references GB:X04466; GB:X00141; NID:g42320; PIDN:CAA28149.1; !1PID:g42325 !'##experimental_source strain K12 P678-54 COMMENT This protein inhibits the multiplication of double-stranded !1DNA phages, such as P1 and lambda. GENETICS !$#gene L; dpi !$#map_position 43.9-46.6% of the plasmid genome !$#genome plasmid CLASSIFICATION #superfamily CloDF13 protein L SUMMARY #length 87 #molecular-weight 9895 #checksum 3538 SEQUENCE /// ENTRY EFYMTG #type complete TITLE translation elongation factor EF-Tu - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 19-Jan-2001 ACCESSIONS S14909; H64249; S06703 REFERENCE S14909 !$#authors Loechel, S.; Inamine, J.M.; Hu, P.C. !$#journal Nucleic Acids Res. (1989) 17:10127 !$#title Nucleotide sequence of the tuf gene from Mycoplasma !1genitalium. !$#cross-references MUID:90098801; PMID:2602130 !$#accession S14909 !'##molecule_type DNA !'##residues 1-394 ##label LOE !'##cross-references EMBL:X16463; NID:g44305; PIDN:CAA34483.1; !1PID:g44306 !'##experimental_source strain G-37 (ATCC 33530) REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession H64249 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-394 ##label TIGR !'##cross-references GB:U39732; GB:L43967; NID:g3845044; !1PIDN:AAC72471.1; PID:g3845045; TIGR:MG451 !'##experimental_source strain G-37 GENETICS !$#gene tuf !$#genetic_code SGC3 CLASSIFICATION #superfamily translation elongation factor Tu; translation !1elongation factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop; protein !1biosynthesis FEATURE !$13-139 #domain translation elongation factor Tu homology !8#label ETU\ !$19-26 #region nucleotide-binding motif A (P-loop)\ !$136-139 #region GTP-binding NKXD motif\ !$174-176 #region GTP-binding SAK/L motif\ !$25,26,62,136,137, !$139,174 #binding_site Mg-GTP (Lys, Thr, Thr, Asn, Lys, Asp, !8Ser) #status predicted SUMMARY #length 394 #molecular-weight 42990 #checksum 5072 SEQUENCE /// ENTRY EFYMTS #type complete TITLE translation elongation factor EF-Tu - Mycoplasma gallisepticum ORGANISM #formal_name Mycoplasma gallisepticum DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 19-Jan-2001 ACCESSIONS S14910; S06704 REFERENCE S14910 !$#authors Inamine, J.M.; Loechel, S.; Hu, P.C. !$#journal Nucleic Acids Res. (1989) 17:10126 !$#title Nucleotide sequence of the tuf gene from Mycoplasma !1gallisepticum. !$#cross-references MUID:90098800; PMID:2602129 !$#accession S14910 !'##molecule_type DNA !'##residues 1-394 ##label INA !'##cross-references EMBL:X16462; NID:g44292; PIDN:CAA34482.1; !1PID:g44293 GENETICS !$#gene tuf !$#genetic_code SGC3 CLASSIFICATION #superfamily translation elongation factor Tu; translation !1elongation factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop; protein !1biosynthesis FEATURE !$13-139 #domain translation elongation factor Tu homology !8#label ETU\ !$19-26 #region nucleotide-binding motif A (P-loop)\ !$136-139 #region GTP-binding NKXD motif\ !$174-176 #region GTP-binding SAK/L motif\ !$25,26,62,136,137, !$139,174 #binding_site Mg-GTP (Lys, Thr, Thr, Asn, Lys, Asp, !8Ser) #status predicted SUMMARY #length 394 #molecular-weight 43099 #checksum 5048 SEQUENCE /// ENTRY EFECT #type complete TITLE translation elongation factor EF-Tu.B [validated] - Escherichia coli (strain K-12) CONTAINS GTPase (EC 3.6.1.-) ORGANISM #formal_name Escherichia coli DATE 30-Nov-1980 #sequence_revision 15-Oct-1982 #text_change 01-Mar-2002 ACCESSIONS A91478; A91095; A92332; I58035; G65204; A03518; A91475 REFERENCE A91478 !$#authors An, G.; Friesen, J.D. !$#journal Gene (1980) 12:33-39 !$#title The nucleotide sequence of tufB and four nearby tRNA !1structural genes of Escherichia coli. !$#cross-references MUID:81165558; PMID:7011904 !$#accession A91478 !'##molecule_type DNA !'##residues 1-394 ##label ANG !'##cross-references GB:J01717; NID:g147968; PIDN:AAA24669.1; !1PID:g147969 REFERENCE A91095 !$#authors Jones, M.D.; Petersen, T.E.; Nielsen, K.M.; Magnusson, S.; !1Sottrup-Jensen, L.; Gausing, K.; Clark, B.F.C. !$#journal Eur. J. Biochem. (1980) 108:507-526 !$#title The complete amino-acid sequence of elongation factor Tu !1from Escherichia coli. !$#cross-references MUID:81003875; PMID:6997043 !$#accession A91095 !'##molecule_type protein !'##residues 2-394 ##label JON REFERENCE A92332 !$#authors Laursen, R.A.; L'Italien, J.J.; Nagarkatti, S.; Miller, D.L. !$#journal J. Biol. Chem. (1981) 256:8102-8109 !$#title The amino acid sequence of elongation factor Tu of !1Escherichia coli. The complete sequence. !$#cross-references MUID:81264196; PMID:7021545 !$#accession A92332 !'##molecule_type protein !'##residues 2-394 ##label LAU REFERENCE I58035 !$#authors Hudson, L.; Rossi, J.; Landy, A. !$#journal Nature (1981) 294:422-427 !$#title Dual function transcripts specifying tRNA and mRNA. !$#cross-references MUID:82080657; PMID:7312036 !$#accession I58035 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-13 ##label RES !'##cross-references EMBL:X04181; NID:g43228; PIDN:CAA27777.1; !1PID:g43229 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65204 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-394 ##label BLAT !'##cross-references GB:AE000472; GB:U00096; NID:g2367333; !1PIDN:AAC76954.1; PID:g1790412; UWGP:b3980 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A65506 !$#authors Kawashima, T.; Berthet-colominas, C.; Wulff, M.; Cusack, S.; !1Leberman, R. !$#submission submitted to the Brookhaven Protein Data Bank, July 1996 !$#cross-references PDB:1EFU !$#contents annotation; X-ray crystallography, 2.5 angstroms REFERENCE A58848 !$#authors Kawashima, T.; Colominas, C.B.; Wulff, M.; Cusack, S.; !1Leberman, R. !$#journal Nature (1996) 379:511-518 !$#title The structure of the Escherichia coli EF-Tu.EF-Ts complex at !12.5angstroms resolution. !$#cross-references MUID:96170031; PMID:8596629 !$#contents annotation; X-ray crystallography, 2.5 angstroms GENETICS !$#gene tufB !$#map_position 90 min !$#start_codon GTG FUNCTION !$#description elongation factor Tu promotes the binding of aminoacyl-tRNA !1to ribosomes during protein biosynthesis; this chain is also !1used in bacteriophage Q-beta RNA polymerase CLASSIFICATION #superfamily translation elongation factor Tu; translation !1elongation factor Tu homology KEYWORDS acetylated amino end; GTP binding; hydrolase; methylated !1amino acid; nucleotide binding; P-loop; protein biosynthesis FEATURE !$2-394 #product translation elongation factor Tu #status !8experimental #label MAT\ !$13-139 #domain translation elongation factor Tu homology !8#label ETU\ !$19-26 #region nucleotide-binding motif A (P-loop)\ !$136-139 #region GTP-binding NKXD motif\ !$174-176 #region GTP-binding SAK/L motif\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental\ !$25,26,62,136,137, !$139,174 #binding_site Mg-GTP (Lys, Thr, Thr, Asn, Lys, Asp, !8Ser) #status predicted\ !$57 #modified_site N6-methyllysine or N6, !8N6-dimethyllysine (Lys) (partial) #status !8experimental SUMMARY #length 394 #molecular-weight 43313 #checksum 5591 SEQUENCE /// ENTRY EFECTA #type complete TITLE translation elongation factor EF-Tu.A [validated] - Escherichia coli (strain K-12) CONTAINS GTPase (EC 3.6.1.-) ORGANISM #formal_name Escherichia coli DATE 30-Nov-1980 #sequence_revision 09-Jun-1994 #text_change 01-Mar-2002 ACCESSIONS A91475; B91095; B92332; A61304; F65127; A03518; A91478 REFERENCE A91475 !$#authors Yokota, T.; Sugisaki, H.; Takanami, M.; Kaziro, Y. !$#journal Gene (1980) 12:25-31 !$#title The nucleotide sequence of the cloned tufA gene of !1Escherichia coli. !$#cross-references MUID:81165557; PMID:7011903 !$#accession A91475 !'##molecule_type DNA !'##residues 1-394 ##label YOK !'##cross-references GB:J01690; NID:g147889; PID:g147897 REFERENCE A91095 !$#authors Jones, M.D.; Petersen, T.E.; Nielsen, K.M.; Magnusson, S.; !1Sottrup-Jensen, L.; Gausing, K.; Clark, B.F.C. !$#journal Eur. J. Biochem. (1980) 108:507-526 !$#title The complete amino-acid sequence of elongation factor Tu !1from Escherichia coli. !$#cross-references MUID:81003875; PMID:6997043 !$#accession B91095 !'##molecule_type protein !'##residues 2-394 ##label JON REFERENCE A92332 !$#authors Laursen, R.A.; L'Italien, J.J.; Nagarkatti, S.; Miller, D.L. !$#journal J. Biol. Chem. (1981) 256:8102-8109 !$#title The amino acid sequence of elongation factor Tu of !1Escherichia coli. The complete sequence. !$#cross-references MUID:81264196; PMID:7021545 !$#accession B92332 !'##molecule_type protein !'##residues 2-394 ##label LAU REFERENCE A61304 !$#authors Nakamura, S.; Nakayama, N.; Takahashi, K.; Kaziro, Y. !$#journal J. Biochem. (1982) 91:1047-1063 !$#title Primary structure of the polypeptide chain elongation factor !1Tu from Escherichia coli. I. Amino acid sequence of fragment !1B. !$#cross-references MUID:82189911; PMID:7042700 !$#accession A61304 !'##molecule_type protein !'##residues 60-264 ##label NAK !'##note this portion of the molecule was designated fragment B REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65127 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-394 ##label BLAT !'##cross-references GB:AE000410; GB:U00096; NID:g1789734; !1PIDN:AAC76364.1; PID:g1789737; UWGP:b3339 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A65506 !$#authors Kawashima, T.; Berthet-colominas, C.; Wulff, M.; Cusack, S.; !1Leberman, R. !$#submission submitted to the Brookhaven Protein Data Bank, July 1996 !$#cross-references PDB:1EFU !$#contents annotation; X-ray crystallography, 2.5 angstroms REFERENCE A58848 !$#authors Kawashima, T.; Colominas, C.B.; Wulff, M.; Cusack, S.; !1Leberman, R. !$#journal Nature (1996) 379:511-518 !$#title The structure of the Escherichia coli EF-Tu.EF-Ts complex at !12.5angstroms resolution. !$#cross-references MUID:96170031; PMID:8596629 !$#contents annotation; X-ray crystallography, 2.5 angstroms GENETICS !$#gene tufA; strD !$#map_position 74 min !$#start_codon GTG FUNCTION !$#description elongation factor Tu promotes the binding of aminoacyl-tRNA !1to ribosomes during protein biosynthesis; this chain is also !1used in bacteriophage Q-beta RNA polymerase CLASSIFICATION #superfamily translation elongation factor Tu; translation !1elongation factor Tu homology KEYWORDS acetylated amino end; GTP binding; hydrolase; methylated !1amino acid; nucleotide binding; P-loop; protein biosynthesis FEATURE !$2-394 #product translation elongation factor Tu #status !8experimental #label MAT\ !$13-139 #domain translation elongation factor Tu homology !8#label ETU\ !$19-26 #region nucleotide-binding motif A (P-loop)\ !$136-139 #region GTP-binding NKXD motif\ !$174-176 #region GTP-binding SAK/L motif\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental\ !$25,26,62,136,137, !$139,174 #binding_site Mg-GTP (Lys, Thr, Thr, Asn, Lys, Asp, !8Ser) #status experimental\ !$57 #modified_site N6-methyllysine or N6, !8N6-dimethyllysine (Lys) (partial) #status !8experimental SUMMARY #length 394 #molecular-weight 43283 #checksum 4967 SEQUENCE /// ENTRY EFEGT #type complete TITLE translation elongation factor EF-Tu - Euglena gracilis chloroplast ORGANISM #formal_name chloroplast Euglena gracilis DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 19-Jan-2001 ACCESSIONS S34508; S34875; A03519; S02254 REFERENCE S34494 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.; Monfort, !1A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#submission submitted to the EMBL Data Library, January 1993 !$#description The complete sequence of the Euglena gracilis chloroplast !1genome (tentative). !$#accession S34508 !'##molecule_type DNA !'##residues 1-409 ##label HAL !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50087.1; !1PID:g415743 REFERENCE S34862 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.R.; !1Monfort, A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#journal Nucleic Acids Res. (1993) 21:3537-3544 !$#title Complete sequence of Euglena gracilis chloroplast DNA. !$#cross-references MUID:93347989; PMID:8346031 !$#accession S34875 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-409 ##label HAL2 !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50087.1; !1PID:g415743 REFERENCE A03519 !$#authors Montandon, P.E.; Stutz, E. !$#journal Nucleic Acids Res. (1983) 11:5877-5892 !$#title Nucleotide sequence of a Euglena gracilis chloroplast genome !1region coding for the elongation factor Tu; evidence for a !1spliced mRNA. !$#cross-references MUID:83299257; PMID:6310519 !$#accession A03519 !'##molecule_type DNA !'##residues 1-409 ##label MON !'##cross-references EMBL:X00044; NID:g11531; PIDN:CAA24925.1; !1PID:g311712 REFERENCE S01049 !$#authors Montandon, P.E.; Knuchel-Aegerter, C.; Stutz, E. !$#journal Nucleic Acids Res. (1987) 15:7809-7822 !$#title Euglena gracilis chloroplast DNA: the untranslated leader of !1tufA-ORF206 gene contains an intron. !$#cross-references MUID:88040410; PMID:3118328 !$#contents intron locations !$#accession S02254 !'##molecule_type DNA !'##residues 1-409 ##label MO2 !'##cross-references EMBL:X06254; NID:g11533; PIDN:CAA29599.1; !1PID:g312223 !'##note neither the complete nucleic acid sequence nor the complete !1translation are shown REFERENCE A48159 !$#authors Toledo, H.; Jerez, C.A. !$#journal FEMS Microbiol. Lett. (1990) 71:241-246 !$#title In vivo and in vitro methylation of the elongation factor !1EF-Tu from Euglena gracilis chloroplast. !$#contents annotation COMMENT This protein promotes the binding of aminoacyl-tRNA to !1ribosomes during protein biosynthesis. GENETICS !$#gene tufA !$#genome chloroplast !$#introns 142/2; 385/3 CLASSIFICATION #superfamily translation elongation factor Tu; translation !1elongation factor Tu homology KEYWORDS chloroplast; GTP binding; methylated amino acid; nucleotide !1binding; P-loop; protein biosynthesis FEATURE !$13-139 #domain translation elongation factor Tu homology !8#label ETU\ !$19-26 #region nucleotide-binding motif A (P-loop)\ !$136-139 #region GTP-binding NKXD motif\ !$174-176 #region GTP-binding SAK/L motif\ !$25,26,62,136,137, !$139,174 #binding_site Mg-GTP (Lys, Thr, Thr, Asn, Lys, Asp, !8Ser) #status predicted\ !$57 #modified_site N6-methyllysine (Lys) #status !8predicted SUMMARY #length 409 #molecular-weight 45062 #checksum 9589 SEQUENCE /// ENTRY EFITT #type complete TITLE translation elongation factor EF-Tu - euglenid (Astasia longa) plastid ORGANISM #formal_name plastid Astasia longa DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 19-Jan-2001 ACCESSIONS S14923; S38612; S08115 REFERENCE S14920 !$#authors Siemeister, G.; Buchholz, C.; Hachtel, W. !$#journal Mol. Gen. Genet. (1990) 220:425-432 !$#title Genes for the plastid elongation factor Tu and ribosomal !1protein S7 and six tRNA genes on the 73 kb DNA from Astasia !1longa that resembles the chloroplast DNA of Euglena. !$#cross-references MUID:90251252; PMID:2338940 !$#accession S14923 !'##molecule_type DNA !'##residues 1-409 ##label SIE !'##cross-references EMBL:X14385; NID:g11197; PIDN:CAB37997.1; !1PID:g4468077 !'##experimental_source strain CCAP 1204-17a REFERENCE S38590 !$#authors Gockel, G.; Baier, S.; Hachtel, W. !$#submission submitted to the EMBL Data Library, November 1993 !$#accession S38612 !'##molecule_type DNA !'##residues 1-409 ##label GOC !'##cross-references EMBL:X75652; NID:g414919; PIDN:CAA53319.1; !1PID:g414923 GENETICS !$#gene tufA !$#genome plastid !$#introns 142/2; 385/1 CLASSIFICATION #superfamily translation elongation factor Tu; translation !1elongation factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop; plastid; protein !1biosynthesis FEATURE !$13-139 #domain translation elongation factor Tu homology !8#label ETU\ !$19-26 #region nucleotide-binding motif A (P-loop)\ !$136-139 #region GTP-binding NKXD motif\ !$174-176 #region GTP-binding SAK/L motif\ !$25,26,62,136,137, !$139,174 #binding_site Mg-GTP (Lys, Thr, Thr, Asn, Lys, Asp, !8Ser) #status predicted SUMMARY #length 409 #molecular-weight 45184 #checksum 6871 SEQUENCE /// ENTRY EFKTT #type complete TITLE translation elongation factor EF-Tu - Cyanophora paradoxa cyanelle ORGANISM #formal_name cyanelle Cyanophora paradoxa DATE 31-Dec-1991 #sequence_revision 21-May-1999 #text_change 19-Jan-2001 ACCESSIONS T06895; S14715; PS0414; S10463 REFERENCE Z15840 !$#authors Stirewalt, V.L.; Michalowski, C.B.; Luffelhardt, W.; !1Bohnert, H.J.; Bryant, D.A. !$#submission submitted to the EMBL Data Library, July 1995 !$#description Nucleotide sequence of the cyanelle genome from Cyanophora !1paradoxa. !$#accession T06895 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-409 ##label STI !'##cross-references EMBL:U30821; NID:g1016083; PIDN:AAA81238.1; !1PID:g1016151 !'##experimental_source strain Pringsheim LB555 REFERENCE S14713 !$#authors Kraus, M.; Goetz, M.; Loeffelhardt, W. !$#journal Plant Mol. Biol. (1990) 15:561-573 !$#title The cyanelle str operon from Cyanophora paradoxa: sequence !1analysis and phylogenetic implications. !$#cross-references MUID:91338695; PMID:2129337 !$#accession S14715 !'##molecule_type DNA !'##residues 1-390,'R',392-409 ##label KRA !'##cross-references EMBL:X52497; NID:g11413; PIDN:CAA36740.1; !1PID:g11416 REFERENCE JU0459 !$#authors Bryant, D.A.; Schluchter, W.M.; Stirewalt, V.L. !$#journal Gene (1991) 98:169-175 !$#title Ferredoxin and ribosomal protein S10 are encoded on the !1cyanelle genome of Cyanophora paradoxa. !$#cross-references MUID:91200662; PMID:1901820 !$#accession PS0414 !'##molecule_type DNA !'##residues 357-409 ##label BRY !'##cross-references GB:M35206; NID:g336630; PIDN:AAA31701.1; !1PID:g336633 GENETICS !$#gene tufA !$#genome cyanelle CLASSIFICATION #superfamily translation elongation factor Tu; translation !1elongation factor Tu homology KEYWORDS cyanelle; GTP binding; nucleotide binding; P-loop; protein !1biosynthesis FEATURE !$13-139 #domain translation elongation factor Tu homology !8#label ETU\ !$19-26 #region nucleotide-binding motif A (P-loop)\ !$136-139 #region GTP-binding NKXD motif\ !$174-176 #region GTP-binding SAK/L motif\ !$25,26,62,136,137, !$139,174 #binding_site Mg-GTP (Lys, Thr, Thr, Asn, Lys, Asp, !8Ser) #status predicted SUMMARY #length 409 #molecular-weight 44538 #checksum 6831 SEQUENCE /// ENTRY EFBYT #type complete TITLE translation elongation factor EF-Tu precursor, mitochondrial - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein O4741; protein YOR187w ORGANISM #formal_name Saccharomyces cerevisiae DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 19-Apr-2002 ACCESSIONS A03520; S67079 REFERENCE A03520 !$#authors Nagata, S.; Tsunetsugu-Yokota, Y.; Naito, A.; Kaziro, Y. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:6192-6196 !$#title Molecular cloning and sequence determination of the nuclear !1gene coding for mitochondrial elongation factor Tu of !1Saccharomyces cerevisiae. !$#cross-references MUID:84016020; PMID:6353412 !$#accession A03520 !'##molecule_type DNA !'##residues 1-437 ##label NAG !'##cross-references EMBL:K00428 REFERENCE S66685 !$#authors Hughes, B.; Pohl, T.M. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67079 !'##molecule_type DNA !'##residues 1-437 ##label HUG !'##cross-references EMBL:Z75095; NID:g1420448; PIDN:CAA99396.1; !1PID:g1420449; GSPDB:GN00015; MIPS:YOR187w !'##experimental_source strain S288C COMMENT This protein functions in the mitochondrion to promote the !1GTP-dependent binding of aminoacyl-tRNA to the 70S ribosomes !1during protein biosynthesis. GENETICS !$#gene SGD:TUF1; TUF1; MIPS:YOR187w !'##cross-references SGD:S0005713 !$#map_position 15R !$#genome nuclear CLASSIFICATION #superfamily translation elongation factor Tu; translation !1elongation factor Tu homology KEYWORDS GTP binding; mitochondrion; nucleotide binding; P-loop; !1protein biosynthesis FEATURE !$49-175 #domain translation elongation factor Tu homology !8#label ETU\ !$55-62 #region nucleotide-binding motif A (P-loop)\ !$172-175 #region GTP-binding NKXD motif\ !$210-212 #region GTP-binding SAK/L motif\ !$61,62,98,172,173, !$175,210 #binding_site Mg-GTP (Lys, Thr, Thr, Asn, Lys, Asp, !8Ser) #status predicted SUMMARY #length 437 #molecular-weight 47972 #checksum 5585 SEQUENCE /// ENTRY A54536 #type complete TITLE translation elongation factor EF-Tu - Flexistipes sinusarabici ORGANISM #formal_name Flexistipes sinusarabici DATE 18-Oct-1994 #sequence_revision 02-Dec-1994 #text_change 19-Jan-2001 ACCESSIONS A54536 REFERENCE A54536 !$#authors Ludwig, W.; Wallner, G.; Tesch, A.; Klink, F. !$#journal FEMS Microbiol. Lett. (1991) 78:139-144 !$#title A novel eubacterial phylum: comparative nucleotide sequence !1analysis of a tuf-gene of Flexistipes sinusarabici. !$#accession A54536 !'##molecule_type DNA !'##residues 1-396 ##label LUD !'##cross-references GB:X59461 CLASSIFICATION #superfamily translation elongation factor Tu; translation !1elongation factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop; protein !1biosynthesis FEATURE !$13-139 #domain translation elongation factor Tu homology !8#label ETU\ !$19-26 #region nucleotide-binding motif A (P-loop)\ !$136-139 #region GTP-binding NKXD motif\ !$174-176 #region GTP-binding SAK/L motif\ !$25,26,62,136,137, !$139,174 #binding_site Mg-GTP (Lys, Thr, Thr, Asn, Lys, Asp, !8Ser) #status predicted SUMMARY #length 396 #molecular-weight 43900 #checksum 423 SEQUENCE /// ENTRY EFHU1 #type complete TITLE translation elongation factor eEF-1 alpha-1 chain - human ALTERNATE_NAMES translation elongation factor Tu ORGANISM #formal_name Homo sapiens #common_name man DATE 30-Jun-1988 #sequence_revision 05-Apr-1995 #text_change 19-Jan-2001 ACCESSIONS B24977; A25409; A29946; A32863; I37339 REFERENCE A93610 !$#authors Rao, T.R.; Slobin, L.I. !$#journal Nucleic Acids Res. (1986) 14:2409 !$#title Structure of the amino-terminal end of mammalian elongation !1factor Tu. !$#cross-references MUID:86176739; PMID:3960725 !$#accession B24977 !'##molecule_type mRNA !'##residues 1-82,'A',84-94 ##label RAO !'##cross-references EMBL:X03689; NID:g31109; PIDN:CAA27325.1; !1PID:g31110 REFERENCE A25409 !$#authors Brands, J.H.G.M.; Maassen, J.A.; Van Hemert, F.J.; Amons, !1R.; Moeller, W. !$#journal Eur. J. Biochem. (1986) 155:167-171 !$#title The primary structure of the alpha-subunit of human !1elongation factor 1. Structural aspects of !1guanine-nucleotide-binding sites. !$#cross-references MUID:86136120; PMID:3512269 !$#accession A25409 !'##molecule_type mRNA !'##residues 1-462 ##label BRA !'##cross-references EMBL:X03558; NID:g31097; PIDN:CAA27245.1; !1PID:g31098 REFERENCE A29946 !$#authors Ann, D.K.; Wu, M.M.J.; Huang, T.; Carlson, D.M.; Wu, R. !$#journal J. Biol. Chem. (1988) 263:3546-3549 !$#title Retinol-regulated gene expression in human tracheobronchial !1epithelial cells. Enhanced expression of elongation factor !1EF-1-alpha. !$#cross-references MUID:88153640; PMID:3346208 !$#accession A29946 !'##molecule_type mRNA !'##residues 'AC',138-462 ##label ANN !'##cross-references GB:M29548; NID:g181966; PIDN:AAA52367.1; !1PID:g181967 REFERENCE A32863 !$#authors Uetsuki, T.; Naito, A.; Nagata, S.; Kaziro, Y. !$#journal J. Biol. Chem. (1989) 264:5791-5798 !$#title Isolation and characterization of the human chromosomal gene !1for polypeptide chain elongation factor-1alpha. !$#cross-references MUID:89174636; PMID:2564392 !$#accession A32863 !'##molecule_type DNA; mRNA !'##residues 1-462 ##label UET !'##cross-references GB:J04617; NID:g181962; PIDN:AAA52343.1; !1PID:g181963 REFERENCE I37339 !$#authors Madsen, H.O.; Poulsen, K.; Dahl, O.; Clark, B.F.; Hjorth, !1J.P. !$#journal Nucleic Acids Res. (1990) 18:1513-1516 !$#title Retropseudogenes constitute the major part of the human !1elongation factor 1 alpha gene family. !$#cross-references MUID:90221877; PMID:2183196 !$#accession I37339 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-231,'V',233-462 ##label RES !'##cross-references EMBL:X16869; NID:g31091; PIDN:CAA34756.1; !1PID:g31092 !'##note submitted to the EMBL/GenBank/DDBJ databases by J.P. Hjorth !1October 1989 GENETICS !$#gene GDB:EEF1A1; EEF1A; EF1A !'##cross-references GDB:118791; OMIM:130590 !$#map_position 6q14-6q14 !$#introns 48/3; 108/3; 207/3; 258/1; 343/3; 422/1 CLASSIFICATION #superfamily translation elongation factor Tu; translation !1elongation factor Tu homology KEYWORDS GTP binding; methylated amino acid; nucleotide binding; !1P-loop; phosphoprotein; protein biosynthesis; RNA binding FEATURE !$1-223 #domain eEF-1 alpha domain I, GTP-binding #status !8predicted #label EF1\ !$8-156 #domain translation elongation factor Tu homology !8#label ETU\ !$14-21 #region nucleotide-binding motif A (P-loop)\ !$153-156 #region GTP-binding NKXD motif\ !$245-330 #domain eEF-1 alpha domain II, tRNA-binding #status !8predicted #label EF2\ !$332-462 #domain eEF-1 alpha domain III, tRNA-binding #status !8predicted #label EF3\ !$36,55,79,165,318 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8predicted\ !$301,374 #binding_site glycerylphosphorylethanolamine (Glu) !8(covalent) #status predicted SUMMARY #length 462 #molecular-weight 50141 #checksum 5308 SEQUENCE /// ENTRY EFRB1 #type complete TITLE translation elongation factor eEF-1 alpha chain - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 19-Jan-2001 ACCESSIONS S22583; A32684; A42039; S18054 REFERENCE S22583 !$#authors Cavallius, J.; Merrick, W.C. !$#journal Nucleic Acids Res. (1992) 20:1422 !$#title Nucleotide sequence of rabbit elongation factor 1 alpha !1cDNA. !$#cross-references MUID:92220623; PMID:1561101 !$#accession S22583 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type mRNA !'##residues 1-462 ##label CAV !'##cross-references EMBL:X62245; NID:g1550; PIDN:CAA44162.1; PID:g1551 REFERENCE A32684 !$#authors Dever, T.E.; Costello, C.E.; Owens, C.L.; Rosenberry, T.L.; !1Merrick, W.C. !$#journal J. Biol. Chem. (1989) 264:20518-20525 !$#title Location of seven post-translational modifications in rabbit !1elongation factor 1alpha including dimethyllysine, !1trimethyllysine, and glycerylphosphorylethanolamine. !$#cross-references MUID:90062188; PMID:2511205 !$#accession A32684 !'##molecule_type protein !'##residues 6-30,'Q',32-129;135-300,'Q',302-373,'Q',375-382;386-462 !1##label DEV !'##note methyllysine; glycerylphosphorylethanolamine REFERENCE A42039 !$#authors Kinzy, T.G.; Freeman, J.P.; Johnson, A.E.; Merrick, W.C. !$#journal J. Biol. Chem. (1992) 267:1623-1632 !$#title A model for the aminoacyl-tRNA binding site of eukaryotic !1elongation factor 1alpha. !$#cross-references MUID:92112879; PMID:1730707 !$#accession A42039 !'##molecule_type protein !'##residues 291-404 ##label KIN CLASSIFICATION #superfamily translation elongation factor Tu; translation !1elongation factor Tu homology KEYWORDS GTP binding; methylated amino acid; nucleotide binding; !1P-loop; phosphoprotein; protein biosynthesis FEATURE !$1-223 #domain eEF-1 alpha domain I, GTP-binding #status !8predicted #label EF1\ !$8-156 #domain translation elongation factor Tu homology !8#label ETU\ !$14-21 #region nucleotide-binding motif A (P-loop)\ !$153-156 #region GTP-binding NKXD motif\ !$245-330 #domain eEF-1 alpha domain II, tRNA-binding #status !8predicted #label EF2\ !$332-462 #domain eEF-1 alpha domain III, tRNA-binding #status !8predicted #label EF3\ !$36,79,318 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental\ !$55,165 #modified_site N6,N6-dimethyllysine (Lys) #status !8experimental\ !$301,374 #binding_site glycerylphosphorylethanolamine (Glu) !8(covalent) #status predicted SUMMARY #length 462 #molecular-weight 50141 #checksum 5308 SEQUENCE /// ENTRY EFMS1 #type complete TITLE translation elongation factor eEF-1 alpha chain - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 19-Jan-2001 ACCESSIONS S02114; A44784; A24977; A27123 REFERENCE S02114 !$#authors Lu, X.; Werner, D. !$#journal Nucleic Acids Res. (1989) 17:442 !$#title The complete cDNA sequence of mouse elongation factor 1 !1alpha (EF 1 alpha) mRNA. !$#cross-references MUID:89098401; PMID:2911475 !$#accession S02114 !'##molecule_type mRNA !'##residues 1-461 ##label LU1 !'##cross-references EMBL:X13661; NID:g50796; PIDN:CAA31957.1; !1PID:g50797 REFERENCE A44784 !$#authors Whiteheart, S.W.; Shenbagamurthi, P.; Chen, L.; Cotter, !1R.J.; Hart, G.W. !$#journal J. Biol. Chem. (1989) 264:14334-14341 !$#title Murine elongation factor 1alpha (EF-1alpha) is !1posttranslationally modified by novel amide-linked !1ethanolamine-phosphoglycerol moieties. Addition of !1ethanolamine-phosphoglycerol to specific glutamic acid !1residues on EF-1alpha. !$#cross-references MUID:89340549; PMID:2569467 !$#accession A44784 !'##molecule_type protein !'##residues 290-299,'Z',301-312;371-372,'Z',374-375 ##label WHI REFERENCE A93610 !$#authors Rao, T.R.; Slobin, L.I. !$#journal Nucleic Acids Res. (1986) 14:2409 !$#title Structure of the amino-terminal end of mammalian elongation !1factor Tu. !$#cross-references MUID:86176739; PMID:3960725 !$#accession A24977 !'##molecule_type mRNA !'##residues 1-76,'LW',79-82,'A',84-90,'DA',93-94 ##label RAO !'##cross-references GB:X03688; NID:g50798; PIDN:CAA27324.1; PID:g50799 REFERENCE A27123 !$#authors Roth, W.W.; Bragg, P.W.; Corrias, M.V.; Reddy, N.S.; !1Dholakia, J.N.; Wahba, A.J. !$#journal Mol. Cell. Biol. (1987) 7:3929-3936 !$#title Expression of a gene for mouse eucaryotic elongation factor !1Tu during murine erythroleukemic cell differentiation. !$#cross-references MUID:88122115; PMID:3481036 !$#accession A27123 !'##molecule_type mRNA !'##residues 1-6,'R',8-14,'L',16-22,'S',24-76,'LW',79-90,'DA',93-107,'R' !1##label ROT !'##cross-references GB:M17878; NID:g192991; PIDN:AAA37538.1; !1PID:g553907 CLASSIFICATION #superfamily translation elongation factor Tu; translation !1elongation factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop; phosphoprotein; !1protein biosynthesis FEATURE !$8-156 #domain translation elongation factor Tu homology !8#label ETU\ !$14-21 #region nucleotide-binding motif A (P-loop)\ !$153-156 #region GTP-binding NKXD motif\ !$300,373 #binding_site glycerylphosphorylethanolamine (Glu) !8(covalent) #status experimental SUMMARY #length 461 #molecular-weight 50050 #checksum 5386 SEQUENCE /// ENTRY EFHUA2 #type complete TITLE translation elongation factor eEF-1 alpha-2 chain - human ALTERNATE_NAMES second translation elongation factor eEF-1 alpha; translation elongation factor eEF-1 alpha like protein S1 ORGANISM #formal_name Homo sapiens #common_name man DATE 22-Jan-1994 #sequence_revision 03-May-1996 #text_change 19-Jan-2001 ACCESSIONS S35033; JC2446; S32043 REFERENCE S35033 !$#authors Knudsen, S.M.; Frydenberg, J.; Clark, B.F.C.; Leffers, H. !$#journal Eur. J. Biochem. (1993) 215:549-554 !$#title Tissue-dependent variation in the expression of elongation !1factor-1-alpha isoforms: isolation and characterisation of a !1cDNA encoding a novel variant of human elongation-factor !11-alpha. !$#cross-references MUID:93358875; PMID:8354261 !$#accession S35033 !'##molecule_type mRNA !'##residues 1-463 ##label KNU !'##cross-references EMBL:X70940; NID:g38455; PIDN:CAA50280.1; !1PID:g38456 REFERENCE JC2445 !$#authors Lee, S.; Ann, D.K.; Wang, E. !$#journal Biochem. Biophys. Res. Commun. (1994) 203:1371-1377 !$#title Cloning of human and mouse brain cDNAs coding for S1, the !1second member of the mammalian elongation factor-1 alpha !1gene family: Analysis of a possible evolutionary pathway. !$#cross-references MUID:95032003; PMID:7945283 !$#accession JC2446 !'##molecule_type mRNA !'##residues 29-463 ##label LEE !'##cross-references GB:L10340 !'##experimental_source hippocampus GENETICS !$#gene GDB:EEF1A2 !'##cross-references GDB:574205 !$#map_position 20q13.3-20q13.3 CLASSIFICATION #superfamily translation elongation factor Tu; translation !1elongation factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop; protein !1biosynthesis FEATURE !$8-156 #domain translation elongation factor Tu homology !8#label ETU\ !$14-21 #region nucleotide-binding motif A (P-loop)\ !$91-94 #region GTP binding #status predicted\ !$153-156 #region GTP binding #status predicted SUMMARY #length 463 #molecular-weight 50470 #checksum 7892 SEQUENCE /// ENTRY EFHB1 #type complete TITLE translation elongation factor eEF-1 alpha chain - honeybee ORGANISM #formal_name Apis mellifera #common_name honeybee DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 19-Jan-2001 ACCESSIONS S10738 REFERENCE S10738 !$#authors Walldorf, U.; Hovemann, B.T. !$#journal FEBS Lett. (1990) 267:245-249 !$#title Apis mellifera cytoplasmic elongation factor 1-alpha !1(EF-1-alpha) is closely related to Drosophila melanogaster !1EF-1-alpha. !$#cross-references MUID:90336785; PMID:2116322 !$#accession S10738 !'##molecule_type DNA !'##residues 1-461 ##label WAL !'##cross-references EMBL:X52884; NID:g5618; PIDN:CAA37066.1; !1PID:g671738 !'##note the authors translated the codon GTC for residue 292 as Ile GENETICS !$#gene EF-1-alpha !$#introns 275/1; 439/3 CLASSIFICATION #superfamily translation elongation factor Tu; translation !1elongation factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop; protein !1biosynthesis FEATURE !$8-156 #domain translation elongation factor Tu homology !8#label ETU\ !$14-21 #region nucleotide-binding motif A (P-loop)\ !$153-156 #region GTP-binding NKXD motif SUMMARY #length 461 #molecular-weight 50521 #checksum 88 SEQUENCE /// ENTRY A45618 #type complete TITLE translation elongation factor eEF-1 alpha chain - nematode (Onchocerca volvulus) ORGANISM #formal_name Onchocerca volvulus DATE 22-Apr-1993 #sequence_revision 02-Jun-1994 #text_change 19-Jan-2001 ACCESSIONS A45618 REFERENCE A45618 !$#authors Alarcon, C.M.; Donelson, J.E. !$#journal Mol. Biochem. Parasitol. (1991) 48:105-107 !$#title Translational elongation factor 1 alpha (EF-1 alpha) of !1Onchocerca volvulus. !$#cross-references MUID:92140447; PMID:1779985 !$#accession A45618 !'##molecule_type mRNA !'##residues 1-464 ##label ALA !'##cross-references GB:M64333; NID:g159884; PIDN:AAA29416.1; !1PID:g159885 !'##note sequence extracted from NCBI backbone (NCBIN:79634, !1NCBIP:79635) CLASSIFICATION #superfamily translation elongation factor Tu; translation !1elongation factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop; protein !1biosynthesis FEATURE !$8-156 #domain translation elongation factor Tu homology !8#label ETU\ !$14-21 #region nucleotide-binding motif A (P-loop)\ !$153-156 #region GTP-binding NKXD motif SUMMARY #length 464 #molecular-weight 50723 #checksum 5078 SEQUENCE /// ENTRY EFSS1A #type complete TITLE translation elongation factor eEF-1 alpha chain - brine shrimp ORGANISM #formal_name Artemia salina #common_name brine shrimp DATE 13-Jun-1983 #sequence_revision 03-Mar-1994 #text_change 19-Jan-2001 ACCESSIONS A25056; A03521; B03521 REFERENCE A25056 !$#authors Lenstra, J.A.; Van Vliet, A.; Arnberg, A.C.; Van Hemert, !1F.J.; Moeller, W. !$#journal Eur. J. Biochem. (1986) 155:475-483 !$#title Genes coding for the elongation factor EF-1 alpha in !1Artemia. !$#cross-references MUID:86164304; PMID:3514211 !$#accession A25056 !'##molecule_type DNA !'##residues 1-462 ##label LEN !'##cross-references GB:X03704; NID:g5674; PIDN:CAA27334.1; PID:g1197188 REFERENCE A03521 !$#authors van Hemert, F.J.; Amons, R.; Pluijms, W.J.M.; van Ormondt, !1H.; Moller, W. !$#journal EMBO J. (1984) 3:1109-1113 !$#title The primary structure of elongation factor EF-1-alpha from !1the brine shrimp Artemia. !$#cross-references MUID:84236107; PMID:6203745 !$#accession A03521 !'##molecule_type mRNA !'##residues 1-32,'S',34-181,'D',183-462 ##label VAN !'##cross-references EMBL:X03349 !$#accession B03521 !'##molecule_type protein !'##residues 6-12,'X',14-66,'X',68,'X',70-107,'Z',109-110,'X',112-120, !1'XXXX',125-195,'X',197-462 ##label VAN2 COMMENT This cytosolic protein promotes the GTP-dependent binding of !1aminoacyl-tRNA to 80S ribosomes during protein biosynthesis. GENETICS !$#introns 48/3; 108/3; 343/3; 422/1 !$#note there appear to be several genes per haploid genome encoding !1this protein CLASSIFICATION #superfamily translation elongation factor Tu; translation !1elongation factor Tu homology KEYWORDS blocked amino end; GTP binding; methylated amino acid; !1nucleotide binding; P-loop; protein biosynthesis FEATURE !$2-462 #product translation elongation factor eEF-1 alpha !8chain #status experimental #label MAT\ !$8-156 #domain translation elongation factor Tu homology !8#label ETU\ !$14-21 #region nucleotide-binding motif A (P-loop)\ !$153-156 #region GTP-binding NKXD motif\ !$2 #modified_site blocked amino end (Gly) (in mature !8form) #status experimental\ !$36,79,219,318 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental\ !$55 #modified_site N6-methyllysine (Lys) #status !8predicted SUMMARY #length 462 #molecular-weight 50567 #checksum 8369 SEQUENCE /// ENTRY EFBY1A #type complete TITLE translation elongation factor eEF-1 alpha-A chain, cytosolic - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein P9513.7; protein YBR0913; protein YBR118w; protein YPR080w ORGANISM #formal_name Saccharomyces cerevisiae DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 19-Jan-2001 ACCESSIONS A03522; A22819; A22298; S45171; S45172; S48282; S45986; !1S32517; S37808; A41453; S69066; S34169; S44697 REFERENCE A03522 !$#authors Nagata, S.; Nagashima, K.; Tsunetsugu-Yokota, Y.; Fujimura, !1K.; Miyazaki, M.; Kaziro, Y. !$#journal EMBO J. (1984) 3:1825-1830 !$#title Polypeptide chain elongation factor 1alpha (EF-1alpha) from !1yeast: nucleotide sequence of one of the two genes for !1EF-1alpha from Saccharomyces cerevisiae. !$#cross-references MUID:85003595; PMID:6383821 !$#accession A03522 !'##molecule_type DNA !'##residues 1-458 ##label NAG !'##cross-references GB:X00779; NID:g3668; PIDN:CAA25356.1; PID:g3669 !'##genetics TEF1 REFERENCE A22819 !$#authors Schirmaier, F.; Philippsen, P. !$#journal EMBO J. (1984) 3:3311-3315 !$#title Identification of two genes coding for the translation !1elongation factor EF-1alpha of Saccharomyces cerevisiae. !$#cross-references MUID:85126940; PMID:6396088 !$#accession A22819 !'##molecule_type DNA !'##residues 1-458 ##label SCH !'##cross-references EMBL:X01638; NID:g4606; PIDN:CAA25798.1; PID:g4607 !'##genetics TEF2 REFERENCE A22298 !$#authors Cottrelle, P.; Thiele, D.; Price, V.L.; Memet, S.; Micouin, !1J.Y.; Marck, C.; Buhler, J.M.; Sentenac, A.; Fromageot, P. !$#journal J. Biol. Chem. (1985) 260:3090-3096 !$#title Cloning, nucleotide sequence, and expression of one of two !1genes coding for yeast elongation factor 1 alpha. !$#cross-references MUID:85131088; PMID:2982849 !$#accession A22298 !'##molecule_type DNA !'##residues 1-458 ##label COT !'##cross-references EMBL:M10992; NID:g171433; PIDN:AAA34585.1; !1PID:g171434 !'##genetics TEF1 REFERENCE S45171 !$#authors Nagashima, K.; Kasai, M.; Nagata, S.; Kaziro, Y. !$#journal Gene (1986) 45:265-273 !$#title Structure of the two genes coding for polypeptide chain !1elongation factor 1-alpha (EF-1-alpha) from Saccharomyces !1cerevisiae. !$#cross-references MUID:87106823; PMID:3026912 !$#accession S45171 !'##molecule_type DNA !'##residues 1-458 ##label NA2 !'##cross-references EMBL:M15666; NID:g171431; PIDN:AAA34584.1; !1PID:g171432 !'##genetics TEF1 !$#accession S45172 !'##molecule_type DNA !'##residues 1-458 ##label NA3 !'##cross-references EMBL:M15667; NID:g171435; PIDN:AAA34586.1; !1PID:g171436 !'##genetics TEF2 REFERENCE S48255 !$#authors Mannhaupt, G.; Stucka, R.; Ehnle, S.; Vetter, I.; Feldmann, !1H. !$#journal Yeast (1994) 10:1363-1381 !$#title Analysis of a 70 kb region on the right arm of yeast !1chromosome II. !$#cross-references MUID:95208357; PMID:7900426 !$#accession S48282 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-458 ##label MAN !'##cross-references EMBL:X78993; NID:g476045; PIDN:CAA55620.1; !1PID:g476072 !'##genetics TEF2 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1994 REFERENCE S45927 !$#authors Feldmann, H.; Mannhaupt, G.; Schwarzlose, C.; Vetter, I. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S45986 !'##molecule_type DNA !'##residues 1-458 ##label FE2 !'##cross-references EMBL:Z35987; GSPDB:GN00002; MIPS:YBR118w; !1NID:g536395; PIDN:CAA85075.1; PID:g536396 !'##genetics TEF2 REFERENCE S32517 !$#authors Cavallius, J.; Zoll, W.; Chakraburtty, K.; Merrick, W.C. !$#journal Biochim. Biophys. Acta (1993) 1163:75-80 !$#title Characterization of yeast EF-1-alpha: non-conservation of !1post-translational modifications. !$#cross-references MUID:93237325; PMID:8476932 !$#accession S32517 !'##molecule_type protein !'##residues 5-53,'K',55-458 ##label CAV !'##note 45-Asp was also found REFERENCE S37808 !$#authors Schaaff-Gerstenschlaeger, I.; Mannhaupt, G.; Vetter, I.; !1Zimmermann, F.K.; Feldmann, H. !$#journal Eur. J. Biochem. (1993) 217:487-492 !$#title TKL2, a second transketolase gene of Saccharomyces !1cerevisiae. Cloning, sequence and deletion analysis of the !1gene. !$#cross-references MUID:94039074; PMID:7916691 !$#accession S37808 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-237 ##label SC2 !'##cross-references EMBL:X73532; NID:g313260; PIDN:CAA51936.1; !1PID:g313261 !'##genetics TEF2 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1993 REFERENCE A41453 !$#authors Miyazaki, M.; Uritani, M.; Fujimura, K.; Yamakatsu, H.; !1Kageyama, T.; Takahashi, K. !$#journal J. Biochem. (1988) 103:508-521 !$#title Peptide elongation factor 1 from yeasts: purification and !1biochemical characterization of peptide elongation factors !11alpha and 1beta(gamma) from Saccharomyces carlsbergensis !1and Schizosaccharomyces pombe. !$#cross-references MUID:88273078; PMID:3214489 !$#accession A41453 !'##molecule_type protein !'##residues 1-78,'X',80-94;457-458 ##label MIY !'##note failure to detect a residue at position 79 may be due to !1modification of a lysine !'##note the source is designated as Saccharomyces carlsbergensis REFERENCE S69057 !$#authors Couch, J. !$#submission submitted to the EMBL Data Library, March 1996 !$#description The sequence of S. cerevisiae cosmid 9513. !$#accession S69066 !'##molecule_type DNA !'##residues 1-458 ##label COU !'##cross-references EMBL:U51033; NID:g1230676; PIDN:AAB68129.1; !1PID:g1230686; GSPDB:GN00016; MIPS:YPR080w !'##genetics TEF1 COMMENT This protein promotes the GTP-dependent binding of !1aminoacyl-tRNA ribosomes. GENETICS TEF2 !$#gene SGD:TEF2; MIPS:YBR118w !'##cross-references MIPS:YBR118w; SGD:S0000322 !$#map_position 2R GENETICS TEF1 !$#gene SGD:TEF1; MIPS:YPR080w !'##cross-references MIPS:YPR080w; SGD:S0006284 !$#map_position 16R CLASSIFICATION #superfamily translation elongation factor Tu; translation !1elongation factor Tu homology KEYWORDS GTP binding; methylated amino acid; nucleotide binding; !1P-loop; protein biosynthesis FEATURE !$8-156 #domain translation elongation factor Tu homology !8#label ETU\ !$14-21 #region nucleotide-binding motif A (P-loop)\ !$153-156 #region GTP-binding NKXD motif\ !$30 #modified_site N6-methyllysine (Lys) #status !8experimental\ !$79 #modified_site N6,N6,N6-trimethyllysine (Lys) #status !8experimental\ !$316 #modified_site N6,N6-dimethyllysine (Lys) #status !8experimental\ !$390 #modified_site N6-methyllysine (Lys) (partial) !8#status experimental SUMMARY #length 458 #molecular-weight 50032 #checksum 9434 SEQUENCE /// ENTRY EFHST #type complete TITLE translation elongation factor aEF-1 alpha chain - Haloarcula marismortui ALTERNATE_NAMES translation elongation factor Tu ORGANISM #formal_name Haloarcula marismortui DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 19-Jan-2001 ACCESSIONS S15761; S00367; S08060 REFERENCE S15761 !$#authors Baldacci, G.; Guinet, F.; Tillit, J.; Zaccai, G.; de !1Recondo, A.M. !$#journal Nucleic Acids Res. (1990) 18:507-511 !$#title Functional implications related to the gene structure of the !1elongation factor EF-Tu from Halobacterium marismortui. !$#cross-references MUID:90174971; PMID:2155402 !$#accession S15761 !'##molecule_type DNA !'##residues 1-421 ##label BA2 !'##cross-references EMBL:X16677; NID:g43597; PIDN:CAA34665.1; !1PID:g43598 !'##note the source is designated as Halobacterium marismortui REFERENCE S00367 !$#authors Guinet, F.; Frank, R.; Leberman, R. !$#journal Eur. J. Biochem. (1988) 172:687-694 !$#title Polypeptide elongation factor Tu from Halobacterium !1marismortui. !$#cross-references MUID:88166752; PMID:3127212 !$#accession S00367 !'##molecule_type protein !'##residues 2-24 ##label GUI !'##note the source is designated as Halobacterium marismortui GENETICS !$#gene EF-Tu CLASSIFICATION #superfamily translation elongation factor Tu; translation !1elongation factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop; protein !1biosynthesis FEATURE !$7-148 #domain translation elongation factor Tu homology !8#label ETU\ !$13-20 #region nucleotide-binding motif A (P-loop)\ !$145-148 #region GTP-binding NKXD motif SUMMARY #length 421 #molecular-weight 45731 #checksum 6801 SEQUENCE /// ENTRY EFUC1A #type complete TITLE translation elongation factor aEF-1 alpha chain - Sulfolobus acidocaldarius ORGANISM #formal_name Sulfolobus acidocaldarius DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 19-Jan-2001 ACCESSIONS S12818 REFERENCE S12817 !$#authors Auer, J. !$#submission submitted to the EMBL Data Library, March 1990 !$#accession S12818 !'##molecule_type DNA !'##residues 1-435 ##label AUE !'##cross-references EMBL:X52382; NID:g46562; PIDN:CAA36608.1; !1PID:g46564 GENETICS !$#gene EF-1a CLASSIFICATION #superfamily translation elongation factor Tu; translation !1elongation factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop; protein !1biosynthesis FEATURE !$7-155 #domain translation elongation factor Tu homology !8#label ETU\ !$13-20 #region nucleotide-binding motif A (P-loop)\ !$152-155 #region GTP-binding NKXD motif SUMMARY #length 435 #molecular-weight 48200 #checksum 6650 SEQUENCE /// ENTRY S00229 #type complete TITLE translation elongation factor EF-Tu.A version 1 [validated] - Thermus aquaticus CONTAINS GTPase (EC 3.6.1.-) ORGANISM #formal_name Thermus aquaticus DATE 14-Aug-1998 #sequence_revision 14-Aug-1998 #text_change 03-Jun-2002 ACCESSIONS S00229; A27277 REFERENCE S00229 !$#authors Kushiro, A.; Shimizu, M.; Tomita, K.I. !$#journal Eur. J. Biochem. (1987) 170:93-98 !$#title Molecular cloning and sequence determination of the tuf gene !1coding for the elongation factor Tu of Thermus thermophilus !1HB8. !$#cross-references MUID:88082865; PMID:2826164 !$#accession S00229 !'##molecule_type DNA !'##residues 1-406 ##label KUS !'##cross-references EMBL:X06657; NID:g48285; PIDN:CAA29856.1; !1PID:g48286 !'##experimental_source strain HB8 !'##note the source is designated as Thermus thermophilus HB8 REFERENCE A27277 !$#authors Seidler, L.; Peter, M.; Meissner, F.; Sprinzl, M. !$#journal Nucleic Acids Res. (1987) 15:9263-9277 !$#title Sequence and identification of the nucleotide binding site !1for the elongation factor Tu from Thermus thermophilus HB8. !$#cross-references MUID:88067755; PMID:3317278 !$#accession A27277 !'##molecule_type DNA !'##residues 1-379,'G',381-406 ##label SEI !'##cross-references GB:X05977; NID:g48287; PIDN:CAA29397.1; PID:g48288 !'##note the source is designated as Thermus thermophilus HB8 !'##note this sequence was confirmed by amino acid analysis REFERENCE A67698 !$#authors Polekhina, G.; Thirup, S.; Kjeldgaard, M.; Nissen, P.; !1Lippmann, C.; Nyborg, J. !$#submission submitted to the Brookhaven Protein Data Bank, May 1996 !$#cross-references PDB:1TUI !$#contents annotation; X-ray crystallography, 2.7 angstroms !$#note strain yt-1 REFERENCE A57609 !$#authors Nissen, P.; Kjeldgaard, M.; Thirup, S.; Polekhina, G.; !1Reshetnikova, L.; Clark, B.F.C.; Nyborg, J. !$#journal Science (1995) 270:1464-1472 !$#title Crystal structure of the ternary complex of Phe-tRNA(Phe), !1EF-Tu, and a GTP analog. !$#cross-references MUID:96095207; PMID:7491491 !$#contents annotation; X-ray crystallography, 2.7 angstroms REFERENCE A58849 !$#authors Berchtold, H.; Reshetnikova, L.; Reiser, C.O.; Schirmer, !1N.K.; Sprinzl, M.; Hilgenfeld, R. !$#journal Nature (1993) 365:126 !$#title Crystal structure of active elongation factor Tu reveals !1major domain rearrangements. !$#cross-references MUID:93382498; PMID:8371755 !$#contents annotation; X-ray crystallography, 1.7 angstroms GENETICS !$#gene tufA; tuf1 FUNCTION EFTU !$#description transports aminoacylated transfer RNAs to the messenger !1RNA:ribosome complex [validated, PMID:3317278] FUNCTION GTP !$#description binds GTP/GDP; catalyses the hydrolysis of GTP !$#note the complex with GTP is active; the complex with GDP is !1inactive; recycling of the inacvtive complex is catalysed by !1translation elongation factor TS CLASSIFICATION #superfamily translation elongation factor Tu; translation !1elongation factor Tu homology KEYWORDS GTP binding; hydrolase; nucleotide binding; P-loop; protein !1biosynthesis FEATURE !$13-140 #domain translation elongation factor Tu homology !8#label ETU\ !$19-26 #region nucleotide-binding motif A (P-loop)\ !$137-140 #region GTP-binding NKXD motif\ !$175-177 #region GTP-binding SAK/L motif\ !$25,26,63,137,138, !$140,175 #binding_site Mg-GTP (Lys, Thr, Thr, Asn, Lys, Asp, !8Ser) #status predicted SUMMARY #length 406 #molecular-weight 44782 #checksum 9987 SEQUENCE /// ENTRY S17146 #type complete TITLE translation elongation factor EF-Tu.B [validated] - Thermus aquaticus CONTAINS GTPase (EC 3.6.1.-) ORGANISM #formal_name Thermus aquaticus DATE 14-Aug-1998 #sequence_revision 14-Aug-1998 #text_change 19-Jan-2001 ACCESSIONS S17146 REFERENCE S17146 !$#authors Satoh, M.; Tanaka, T.; Kushiro, A.; Hakoshima, T.; Tomita, !1K. !$#journal FEBS Lett. (1991) 288:98-100 !$#title Molecular cloning, nucleotide sequence and expression of the !1tufB gene encoding elongation factor Tu from Thermus !1thermophilus HB8. !$#cross-references MUID:91348298; PMID:1908798 !$#accession S17146 !'##molecule_type DNA !'##residues 1-406 ##label SAT !'##cross-references EMBL:X61957; NID:g312959; PIDN:CAA43956.1; !1PID:g312960 !'##experimental_source strain HB8 !'##note the source is designated as Thermus thermophilus REFERENCE A67698 !$#authors Polekhina, G.; Thirup, S.; Kjeldgaard, M.; Nissen, P.; !1Lippmann, C.; Nyborg, J. !$#submission submitted to the Brookhaven Protein Data Bank, May 1996 !$#cross-references PDB:1TUI !$#contents annotation; X-ray crystallography, 2.7 angstroms !$#note strain yt-1 REFERENCE A57609 !$#authors Nissen, P.; Kjeldgaard, M.; Thirup, S.; Polekhina, G.; !1Reshetnikova, L.; Clark, B.F.C.; Nyborg, J. !$#journal Science (1995) 270:1464-1472 !$#title Crystal structure of the ternary complex of Phe-tRNA(Phe), !1EF-Tu, and a GTP analog. !$#cross-references MUID:96095207; PMID:7491491 !$#contents annotation; X-ray crystallography, 2.7 angstroms REFERENCE A58849 !$#authors Berchtold, H.; Reshetnikova, L.; Reiser, C.O.; Schirmer, !1N.K.; Sprinzl, M.; Hilgenfeld, R. !$#journal Nature (1993) 365:126 !$#title Crystal structure of active elongation factor Tu reveals !1major domain rearrangements. !$#cross-references MUID:93382498; PMID:8371755 !$#contents annotation; X-ray crystallography, 1.7 angstroms COMMENT Translation elongation factor Tu is the archetypal guanine !1nucleotide binding protein (G-protein). During protein !1biosynthesis it transports aminoacylated transfer RNAs to !1the messenger RNA:ribosome complex. Recycling of the !1inacvtive GDP complex is catalysed by translation elongation !1factor TS. GENETICS !$#gene tufB CLASSIFICATION #superfamily translation elongation factor Tu; translation !1elongation factor Tu homology KEYWORDS GTP binding; hydrolase; nucleotide binding; P-loop; protein !1biosynthesis FEATURE !$13-140 #domain translation elongation factor Tu homology !8#label ETU\ !$19-26 #region nucleotide-binding motif A (P-loop)\ !$137-140 #region GTP-binding NKXD motif\ !$175-177 #region GTP-binding SAK/L motif\ !$25,26,63,137,138, !$140,175 #binding_site Mg-GTP (Lys, Thr, Thr, Asn, Lys, Asp, !8Ser) #status predicted SUMMARY #length 406 #molecular-weight 44782 #checksum 9675 SEQUENCE /// ENTRY S29293 #type complete TITLE translation elongation factor EF-Tu.A version 2 [validated] - Thermus aquaticus CONTAINS GTPase (EC 3.6.1.-) ORGANISM #formal_name Thermus aquaticus DATE 14-Aug-1998 #sequence_revision 14-Aug-1998 #text_change 19-Jan-2001 ACCESSIONS S29293 REFERENCE S29293 !$#authors Voss, R.H.; Hartmann, R.K.; Lippmann, C.; Alexander, C.; !1Jahn, O.; Erdmann, V.A. !$#journal Eur. J. Biochem. (1992) 207:839-846 !$#title Sequence of the tufA gene encoding elongation factor EF-Tu !1from Thermus aquaticus and overproduction of the protein in !1Escherichia coli. !$#cross-references MUID:92362620; PMID:1499561 !$#accession S29293 !'##molecule_type DNA !'##residues 1-406 ##label VOS !'##cross-references EMBL:X66322; NID:g49096; PIDN:CAA46998.1; !1PID:g49098 !'##experimental_source strain EP00276 REFERENCE A67698 !$#authors Polekhina, G.; Thirup, S.; Kjeldgaard, M.; Nissen, P.; !1Lippmann, C.; Nyborg, J. !$#submission submitted to the Brookhaven Protein Data Bank, May 1996 !$#cross-references PDB:1TUI !$#contents annotation; X-ray crystallography, 2.7 angstroms !$#note strain yt-1 REFERENCE A57609 !$#authors Nissen, P.; Kjeldgaard, M.; Thirup, S.; Polekhina, G.; !1Reshetnikova, L.; Clark, B.F.C.; Nyborg, J. !$#journal Science (1995) 270:1464-1472 !$#title Crystal structure of the ternary complex of Phe-tRNA(Phe), !1EF-Tu, and a GTP analog. !$#cross-references MUID:96095207; PMID:7491491 !$#contents annotation; X-ray crystallography, 2.7 angstroms REFERENCE A58849 !$#authors Berchtold, H.; Reshetnikova, L.; Reiser, C.O.; Schirmer, !1N.K.; Sprinzl, M.; Hilgenfeld, R. !$#journal Nature (1993) 365:126 !$#title Crystal structure of active elongation factor Tu reveals !1major domain rearrangements. !$#cross-references MUID:93382498; PMID:8371755 !$#contents annotation; X-ray crystallography, 1.7 angstroms COMMENT Translation elongation factor Tu is the archetypal guanine !1nucleotide binding protein (G-protein). During protein !1biosynthesis it transports aminoacylated transfer RNAs to !1the messenger RNA:ribosome complex. Recycling of the !1inacvtive GDP complex is catalysed by translation elongation !1factor TS. GENETICS !$#gene tufA CLASSIFICATION #superfamily translation elongation factor Tu; translation !1elongation factor Tu homology KEYWORDS GTP binding; hydrolase; nucleotide binding; P-loop; protein !1biosynthesis FEATURE !$13-140 #domain translation elongation factor Tu homology !8#label ETU\ !$19-26 #region nucleotide-binding motif A (P-loop)\ !$137-140 #region GTP-binding NKXD motif\ !$175-177 #region GTP-binding SAK/L motif\ !$25,26,63,137,138, !$140,175 #binding_site Mg-GTP (Lys, Thr, Thr, Asn, Lys, Asp, !8Ser) #status experimental SUMMARY #length 406 #molecular-weight 44814 #checksum 8821 SEQUENCE /// ENTRY EFECSB #type complete TITLE translation elongation factor EF-selB - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 01-Mar-2002 ACCESSIONS JV0050; S47811; A35302; H65158 REFERENCE JV0050 !$#authors Forchhammer, K.; Leinfelder, W.; Boeck, A. !$#journal Nature (1989) 342:453-456 !$#title Identification of a novel translation factor necessary for !1the incorporation of selenocysteine into protein. !$#cross-references MUID:90066680; PMID:2531290 !$#accession JV0050 !'##molecule_type DNA !'##residues 1-614 ##label FOR !'##cross-references GB:X16644; NID:g42936; PIDN:CAA34637.1; PID:g42937 REFERENCE S47666 !$#authors Plunkett, G. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S47811 !'##status preliminary !'##molecule_type DNA !'##residues 1-195,'X',197-345,'X',347-606,'ATHYYFR',614,'NKEMIN' !1##label PLU !'##cross-references EMBL:U00039; NID:g466582; PIDN:AAB18567.1; !1PID:g466728 REFERENCE A35302 !$#authors Forchhammer, K.; Ruecknagel, K.P.; Boeck, A. !$#journal J. Biol. Chem. (1990) 265:9346-9350 !$#title Purification and biochemical characterization of SELB, a !1translation factor involved in selenoprotein synthesis. !$#cross-references MUID:90264431; PMID:2140572 !$#accession A35302 !'##status preliminary !'##molecule_type protein !'##residues 26-41 ##label FO2 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65158 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-614 ##label BLAT !'##cross-references GB:AE000436; GB:U00096; NID:g2367246; !1PIDN:AAC76614.1; PID:g2367247; UWGP:b3590 !'##experimental_source strain K-12, substrain MG1655 COMMENT The selB protein may be an amino acid-specific elongation !1factor, replacing EF-Tu in a special translation step; it !1involves the cotranslational incorporation of selenocysteine !1into the nascent polypeptide chain through a process !1directed by a UGA codon that otherwise functions as a stop !1codon. GENETICS !$#gene selB CLASSIFICATION #superfamily translation elongation factor selB; translation !1elongation factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop; protein !1biosynthesis; selenocysteine incorporation FEATURE !$1-115 #domain translation elongation factor Tu homology !8#label ETU\ !$7-14 #region nucleotide-binding motif A (P-loop) SUMMARY #length 614 #molecular-weight 68867 #checksum 5112 SEQUENCE /// ENTRY ZZZRNQ #type complete TITLE adenylyl-sulfate kinase (EC 2.7.1.25) - Rhizobium meliloti plasmid pSym ALTERNATE_NAMES ATP sulfurylase large chain; nodulation protein nodQ CONTAINS adenylylsulfate kinase (EC 2.7.1.25); sulfate adenylyltransferase (EC 2.7.7.4) ORGANISM #formal_name Rhizobium meliloti DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 03-Jun-2002 ACCESSIONS S14899; S06191 REFERENCE S14898 !$#authors Cervantes, E.; Sharma, S.B.; Maillet, F.; Vasse, J.; !1Truchet, G.; Rosenberg, C. !$#journal Mol. Microbiol. (1989) 3:745-755 !$#title The Rhizobium meliloti host range nodQ gene encodes a !1protein which shares homology with translation elongation !1and initiation factors. !$#cross-references MUID:89313304; PMID:2546009 !$#accession S14899 !'##molecule_type DNA !'##residues 1-641 ##label CER !'##cross-references EMBL:X14809; NID:g46311; PIDN:CAA32914.1; !1PID:g46313 COMMENT 3'-phosphoadenosine-5'-phosphosulfate is required for !1production of the nod factors, which are sulfated !1oligosaccharides that stimulate host plant-specific !1responses to the nitrogen-fixing bacterial symbiont. GENETICS !$#gene nodQ !$#genome plasmid COMPLEX associates with the nodP protein to form a sulfate !1activation complex with adenylylsulfate kinase and sulfate !1adenylyltransferase activities FUNCTION ASKF !$#description as adenylylsulfate kinase catalyzes the phosphorylation of !1adenylylsulfate by ATP to form 3'-phosphoadenylylsulfate and !1ADP FUNCTION SATF !$#description as sulfate adenylyltransferase catalyzes the reaction of !1sulfate and ATP to form adenylylsulfate and pyrophosphate CLASSIFICATION #superfamily nodulation protein nodQ; adenylylsulfate kinase !1homology; translation elongation factor Tu homology KEYWORDS GTP binding; multifunctional enzyme; nucleotide binding; !1nucleotidyltransferase; P-loop; phosphotransferase FEATURE !$25-168 #domain translation elongation factor Tu homology !8#label ETU\ !$31-38 #region nucleotide-binding motif A (P-loop)\ !$165-168 #region GTP-binding NKXD motif\ !$460-621 #domain adenylylsulfate kinase homology #label ASK\ !$467-474 #region nucleotide-binding motif A (P-loop) SUMMARY #length 641 #molecular-weight 70613 #checksum 2092 SEQUENCE /// ENTRY I39755 #type complete TITLE adenylyl-sulfate kinase (EC 2.7.1.25) - Azospirillum brasilense ALTERNATE_NAMES ATP sulfurylase large chain; nodulation protein nodQ CONTAINS adenylylsulfate kinase (EC 2.7.1.25); sulfate adenylyltransferase (EC 2.7.7.4) ORGANISM #formal_name Azospirillum brasilense DATE 21-May-1999 #sequence_revision 21-May-1999 #text_change 03-Jun-2002 ACCESSIONS I39755 REFERENCE I39754 !$#authors Vieille, C.; Elmerich, C. !$#journal Mol. Plant Microbe Interact. (1990) 3:389-400 !$#title Characterization of two Azospirillum brasilense Sp7 plasmid !1genes homologous to Rhizobium meliloti nodPQ. !$#cross-references MUID:92033082; PMID:2131098 !$#accession I39755 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-620 ##label RES !'##cross-references GB:M94886; NID:g142423; PIDN:AAA22186.1; !1PID:g142425 COMMENT 3'-phosphoadenosine-5'-phosphosulfate is required for !1production of the nod factors, which are sulfated !1oligosaccharides that stimulate host plant-specific !1responses to the nitrogen-fixing bacterial symbiont. GENETICS !$#gene nodQ COMPLEX associates with the nodP protein to form a sulfate !1activation complex with adenylylsulfate kinase and sulfate !1adenylyltransferase activities FUNCTION ASKF !$#description as adenylylsulfate kinase catalyzes the phosphorylation of !1adenylylsulfate by ATP to form 3'-phosphoadenylylsulfate and !1ADP FUNCTION SATF !$#description as sulfate adenylyltransferase catalyzes the reaction of !1sulfate and ATP to form adenylylsulfate and pyrophosphate CLASSIFICATION #superfamily nodulation protein nodQ; adenylylsulfate kinase !1homology; translation elongation factor Tu homology KEYWORDS GTP binding; multifunctional enzyme; nucleotide binding; !1nucleotidyltransferase; P-loop; phosphotransferase FEATURE !$10-153 #domain translation elongation factor Tu homology !8#label ETU\ !$16-23 #region nucleotide-binding motif A (P-loop)\ !$150-153 #region GTP-binding NKXD motif\ !$446-607 #domain adenylylsulfate kinase homology #label ASK\ !$453-460 #region nucleotide-binding motif A (P-loop) SUMMARY #length 620 #molecular-weight 67040 #checksum 555 SEQUENCE /// ENTRY B70772 #type complete TITLE probable adenylyl-sulfate kinase (EC 2.7.1.25) - Mycobacterium tuberculosis (strain H37RV) ALTERNATE_NAMES ATP sulfurylase large chain CONTAINS adenylylsulfate kinase (EC 2.7.1.25); sulfate adenylyltransferase (EC 2.7.7.4) ORGANISM #formal_name Mycobacterium tuberculosis DATE 21-May-1999 #sequence_revision 21-May-1999 #text_change 03-Jun-2002 ACCESSIONS B70772 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession B70772 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-614 ##label COL !'##cross-references GB:Z73419; GB:AL123456; NID:g3261573; !1PIDN:CAA97752.1; PID:g1322410 !'##experimental_source strain H37Rv GENETICS !$#gene cysN !$#note contains domains equivalent to cysN and cysC COMPLEX may associate with small chain to form a sulfate activation !1complex with adenylylsulfate kinase and sulfate !1adenylyltransferase activities FUNCTION ASKF !$#description as adenylylsulfate kinase catalyzes the phosphorylation of !1adenylylsulfate by ATP to form 3'-phosphoadenylylsulfate and !1ADP FUNCTION SATF !$#description as sulfate adenylyltransferase catalyzes the reaction of !1sulfate and ATP to form adenylylsulfate and pyrophosphate CLASSIFICATION #superfamily nodulation protein nodQ; adenylylsulfate kinase !1homology; translation elongation factor Tu homology KEYWORDS GTP binding; multifunctional enzyme; nucleotide binding; !1nucleotidyltransferase; P-loop; phosphotransferase FEATURE !$5-146 #domain translation elongation factor Tu homology !8#label ETU\ !$11-18 #region nucleotide-binding motif A (P-loop)\ !$143-146 #region GTP-binding NKXD motif\ !$443-605 #domain adenylylsulfate kinase homology #label ASK\ !$450-457 #region nucleotide-binding motif A (P-loop) SUMMARY #length 614 #molecular-weight 67838 #checksum 6804 SEQUENCE /// ENTRY JN0327 #type complete TITLE sulfate adenylyltransferase (EC 2.7.7.4) large chain - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS JN0327; PS0400; C65056 REFERENCE JN0326 !$#authors Leyh, T.S.; Vogt, T.F.; Suo, Y. !$#journal J. Biol. Chem. (1992) 267:10405-10410 !$#title The DNA sequence of the sulfate activation locus from !1Escherichia coli K-12. !$#cross-references MUID:92268080; PMID:1316900 !$#accession JN0327 !'##molecule_type DNA !'##residues 1-475 ##label LEY !'##cross-references GB:M74586; NID:g145670; PIDN:AAA23646.1; !1PID:g145673 !'##experimental_source strain K12 !$#accession PS0400 !'##molecule_type protein !'##residues 1-5 ##label LEY1 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65056 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-475 ##label BLAT !'##cross-references GB:AE000358; GB:U00096; NID:g2367156; !1PIDN:AAC75793.1; PID:g1789108; UWGP:b2751 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene cysN !$#map_position 59 min CLASSIFICATION #superfamily Escherichia coli sulfate adenylyltransferase !1large chain; translation elongation factor Tu homology KEYWORDS cysteine biosynthesis; GTP binding; nucleotide binding; !1nucleotidyltransferase; P-loop FEATURE !$28-171 #domain translation elongation factor Tu homology !8#label ETU\ !$34-41 #region nucleotide-binding motif A (P-loop)\ !$109-114 #region nucleotide-binding motif B\ !$168-171 #region GTP-binding NKXD motif\ !$206-208 #region GTP-binding SAK/L motif\ !$40,41,94,168,169, !$171,206 #binding_site Mg-GTP (Lys, Ser, Thr, Asn, Lys, Asp, !8Ser) #status predicted SUMMARY #length 475 #molecular-weight 52558 #checksum 3072 SEQUENCE /// ENTRY EFBYS2 #type complete TITLE suppressor 2 protein - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES G1-to-S transition protein; protein YD9395.05; protein YDR172w ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 19-Jan-2001 ACCESSIONS S00733; JT0323; S49768; S00488; A26742; S00533; S05723 REFERENCE S00733 !$#authors Wilson, P.G.; Culbertson, M.R. !$#journal J. Mol. Biol. (1988) 199:559-573 !$#title SUF12 suppressor protein of yeast. A fusion protein related !1to the EF-1 family of elongation factors. !$#cross-references MUID:88172503; PMID:3280807 !$#accession S00733 !'##molecule_type DNA !'##residues 1-685 ##label WIL !'##cross-references EMBL:X07163; NID:g4581; PIDN:CAA30155.1; PID:g4582 REFERENCE JT0323 !$#authors Kushnirov, V.V.; Ter-Avanesyan, M.D.; Telckov, M.V.; !1Surguchov, A.P.; Smirnov, V.N.; Inge-Vechtomov, S.G. !$#journal Gene (1988) 66:45-54 !$#title Nucleotide sequence of the SUP2(SUP35) gene of Saccharomyces !1cerevisiae. !$#cross-references MUID:88329727; PMID:3047009 !$#accession JT0323 !'##molecule_type DNA !'##residues 1-685 ##label KUS !'##cross-references EMBL:M21129; NID:g172789; PIDN:AAA35133.1; !1PID:g172791 REFERENCE S49764 !$#authors Murphy, L.; Harris, D.E. !$#submission submitted to the EMBL Data Library, November 1994 !$#accession S49768 !'##molecule_type DNA !'##residues 1-685 ##label MUR !'##cross-references EMBL:Z46727; NID:g1289283; PIDN:CAA86677.1; !1PID:g1289287; GSPDB:GN00004; MIPS:YDR172w REFERENCE S00488 !$#authors Kikuchi, Y.; Shimatake, H.; Kikuchi, A. !$#journal EMBO J. (1988) 7:1175-1182 !$#title A yeast gene required for the G1-to-S transition encodes a !1protein containing an A-kinase target site and GTPase !1domain. !$#cross-references MUID:88296422; PMID:2841115 !$#accession S00488 !'##molecule_type DNA !'##residues 1-52,'C',54-685 ##label KIK !'##cross-references GB:Y00829; EMBL:Y00859; NID:g3711; PIDN:CAA68760.1; !1PID:g3712 GENETICS !$#gene SGD:SUP35; SUF12; GST1; SUP2; MIPS:YDR172w !'##cross-references SGD:S0002579; MIPS:YDR172w !$#map_position 4R CLASSIFICATION #superfamily suppressor 2 protein; translation elongation !1factor Tu homology KEYWORDS duplication; GTP binding; nucleotide binding; P-loop; !1phosphoprotein; tandem repeat FEATURE !$1-123 #domain A #label DOM1\ !$42-119 #region 10-residue repeats\ !$124-253 #domain charged #label DOM2\ !$159-222 #region glutamic acid/lysine-rich\ !$254-685 #domain C #label DOM4\ !$261-409 #domain translation elongation factor Tu homology !8#label ETU\ !$267-274 #region nucleotide-binding motif A (P-loop)\ !$406-409 #region GTP-binding NKXD motif\ !$273 #binding_site GTP (Lys) #status predicted SUMMARY #length 685 #molecular-weight 76551 #checksum 8398 SEQUENCE /// ENTRY FIEC2 #type complete TITLE translation initiation factor IF-2 [validated] - Escherichia coli (strain K-12) CONTAINS GTPase (EC 3.6.1.-), ribosome-dependent ORGANISM #formal_name Escherichia coli DATE 28-May-1986 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS D65107; A03523; A21496; S02368 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65107 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-890 ##label BLAT !'##cross-references GB:AE000397; GB:U00096; NID:g2367199; !1PIDN:AAC76202.1; PID:g1789559; UWGP:b3168 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A94022 !$#authors Sacerdot, C.; Dessen, P.; Hershey, J.W.B.; Plumbridge, J.A.; !1Grunberg-Manago, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:7787-7791 !$#title Sequence of the initiation factor IF2 gene: unusual protein !1features and homologies with elongation factors. !$#cross-references MUID:85088492; PMID:6096856 !$#accession A03523 !'##molecule_type DNA !'##residues 1-242,'DE',243-418,'K',420-465,'LV',468-480,'Q',482-642, !1'T',643-753,'S',754-890 ##label SAC REFERENCE A93514 !$#authors Ishii, S.; Ihara, M.; Maekawa, T.; Nakamura, Y.; Uchida, H.; !1Imamoto, F. !$#journal Nucleic Acids Res. (1984) 12:3333-3342 !$#title The nucleotide sequence of the cloned nusA gene and its !1flanking region of Escherichia coli. !$#cross-references MUID:84193200; PMID:6326058 !$#accession A21496 !'##molecule_type DNA !'##residues 1-22 ##label ISH REFERENCE S01915 !$#authors Sands, J.F.; Regnier, P.; Cummings, H.S.; Grunberg-Manago, !1M.; Hershey, J.W.B. !$#journal Nucleic Acids Res. (1988) 16:10803-10816 !$#title The existence of two genes between infB and rpsO in the !1Escherichia coli genome: DNA sequencing and S1 nuclease !1mapping. !$#cross-references MUID:89083498; PMID:2849753 !$#accession S02368 !'##molecule_type DNA !'##residues 864-890 ##label SAN !'##cross-references EMBL:X13270 COMMENT IF-2, one of the essential components for the initiation of !1protein synthesis in vitro, protects formylmethionyl-tRNA !1from spontaneous hydrolysis and promotes its binding to the !130S ribosomal subunits. It is also involved in the !1hydrolysis of GTP during the formation of the 70S ribosomal !1complex. COMMENT Using alternative initiation codons in the same reading !1frame, the gene translates into two isozymes, alpha and !1beta, having different amino ends. GENETICS !$#gene infB !$#map_position 69 min FUNCTION TIC !$#description the translation initiation complex is responsible for the !1seletcion of the proper start codon for the synthesis of a !1polypeptide [validated, MUID:97114079] FUNCTION RIB !$#description IF2 promotes binding of the fMet-tRNA to the 30S ribosomal !1subunit [validated, MUID:97114079] FUNCTION GTP !$#description catalyzes the hydrolysis of GTP in a ribosome-dependent !1manner [validated, MUID:97114079] CLASSIFICATION #superfamily translation initiation factor IF-2; translation !1elongation factor Tu homology KEYWORDS alternative initiators; GTP binding; hydrolase; nucleotide !1binding; P-loop; protein biosynthesis FEATURE !$1-890 #product translation initiation factor IF2-alpha !8#status experimental #label ALP\ !$158-890 #product translation initiation factor IF2-beta !8#status experimental #label BET\ !$165-890 #product translation initiation factor IF2-beta' !8#status experimental #label BES\ !$392-501 #domain translation elongation factor Tu homology !8#label ETU\ !$398-405 #region nucleotide-binding motif A (P-loop)\ !$498-501 #region GTP-binding NKXD motif\ !$534-536 #region GTP-binding SAK/L motif\ !$404,405,425,498, !$499,501,534 #binding_site Mg-GTP (Lys, Thr, Thr, Asn, Lys, Asp, !8Ser) #status predicted SUMMARY #length 890 #molecular-weight 97349 #checksum 9852 SEQUENCE /// ENTRY A35269 #type complete TITLE translation initiation factor IF-2 - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 17-Aug-1990 #sequence_revision 06-Jan-1995 #text_change 19-Jan-2001 ACCESSIONS A35269; B35269; S31994; G69644 REFERENCE A35269 !$#authors Shazand, K.; Tucker, J.; Chiang, R.; Stansmore, K.; !1Sperling-Petersen, H.U.; Grunberg-Manago, M.; Rabinowitz, !1J.C.; Leighton, T. !$#journal J. Bacteriol. (1990) 172:2675-2687 !$#title Isolation and molecular genetic characterization of the !1Bacillus subtilis gene (infB) encoding protein synthesis !1initiation factor 2. !$#cross-references MUID:90236932; PMID:2110148 !$#accession A35269 !'##molecule_type DNA !'##residues 1-716 ##label SHA1 !'##cross-references GB:M34836; NID:g143358; PIDN:AAA22673.1; !1PID:g143359 !$#accession B35269 !'##molecule_type DNA !'##residues 94-716 ##label SHA2 REFERENCE S31990 !$#authors Shazand, K. !$#submission submitted to the EMBL Data Library, November 1992 !$#accession S31994 !'##molecule_type DNA !'##residues 1-716 ##label SHA3 !'##cross-references EMBL:Z18631; NID:g49314; PIDN:CAA79234.1; !1PID:g49319 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69644 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-55,'A',57-716 ##label KUN !'##cross-references GB:Z99112; GB:AL009126; NID:g2633902; !1PIDN:CAB13536.1; PID:g2634035 !'##experimental_source strain 168 COMMENT IF-2, one of the essential components for the initiation of !1protein synthesis in vitro, protects formylmethionyl-tRNA !1from spontaneous hydrolysis and promotes its binding to the !130S ribosomal subunits. It is also involved in the !1hydrolysis of GTP during the formation of the 70S ribosomal !1complex. COMMENT Alternative initiation codons in the same reading frame do !1appear to be utilized to produce two isozymes designated !1alpha and beta. GENETICS !$#gene infB CLASSIFICATION #superfamily translation initiation factor IF-2; translation !1elongation factor Tu homology KEYWORDS alternative initiators; GTP binding; nucleotide binding; !1P-loop; protein biosynthesis FEATURE !$1-716 #product translation initiation factor IF-2-alpha !8#status predicted #label ALP\ !$94-716 #product translation initiation factor IF-2-beta !8#status predicted #label BET\ !$220-329 #domain translation elongation factor Tu homology !8#label ETU\ !$226-233 #region nucleotide-binding motif A (P-loop)\ !$326-329 #region GTP-binding NKXD motif\ !$362-364 #region GTP-binding SAK/L motif\ !$232,233,253,326, !$327,329,362 #binding_site Mg-GTP (Lys, Thr, Thr, Asn, Lys, Asp, !8Ser) #status predicted SUMMARY #length 716 #molecular-weight 78621 #checksum 7115 SEQUENCE /// ENTRY EFECG #type complete TITLE translation elongation factor EF-G - Escherichia coli (strain K-12) ALTERNATE_NAMES fusA protein ORGANISM #formal_name Escherichia coli DATE 28-Feb-1981 #sequence_revision 12-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS G65127; A28513; S13740; A03524; S24928; I41064 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65127 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-704 ##label BLAT !'##cross-references GB:AE000410; GB:U00096; NID:g1789734; !1PIDN:AAC76365.1; PID:g1789738; UWGP:b3340 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A28513 !$#authors Ovchinnikov, Y.A.; Alakhov, Y.B.; Bundulis, Y.P.; Bundule, !1M.A.; Dovgas, N.V.; Kozlov, V.P.; Motuz, L.P.; Vinokurov, !1L.M. !$#journal FEBS Lett. (1982) 139:130-135 !$#title The primary structure of elongation factor G from !1Escherichia coli. A complete amino acid sequence. !$#cross-references MUID:82187171; PMID:7042386 !$#accession A28513 !'##molecule_type protein !'##residues 2-295,'DC',298-299,303-395,'C',397-575,'V',577-583,'K', !1585-593,'H',595-625,'Q',627-645,'Q',647-656,'Q',658-662,'Q', !1663-704 ##label OVC REFERENCE S13738 !$#authors Post, L.E.; Nomura, M. !$#journal J. Biol. Chem. (1980) 255:4660-4666 !$#title DNA sequences from the str operon of Escherichia coli. !$#cross-references MUID:80182129; PMID:6989816 !$#accession S13740 !'##molecule_type DNA !'##residues 1-93 ##label POS !'##cross-references EMBL:V00355 REFERENCE A03524 !$#authors Alakhov, Y.B.; Dovgas, N.V.; Motuz, L.P.; Vinokurov, L.M.; !1Ovchinnikov, Y.A. !$#journal FEBS Lett. (1981) 126:183-186 !$#title The primary structure of the elongation factor G from !1Escherichia coli. Amino acid sequence of the C-terminal !1domain. !$#cross-references MUID:81212798; PMID:7016587 !$#accession A03524 !'##molecule_type protein !'##residues 476-575,'V',577-583,'K',585-593,'H',595-625,'Q',627-645, !1'Q',647-656,'Q',658-662,'Q',663-704 ##label ALA REFERENCE S24928 !$#authors Weigel, C.T.O. !$#submission submitted to the EMBL Data Library, May 1992 !$#accession S24928 !'##status preliminary !'##molecule_type DNA !'##residues 1-21 ##label WEI !'##cross-references EMBL:X65735 REFERENCE I41064 !$#authors Zengel, J.M.; Archer, R.H.; Lindahl, L. !$#journal Nucleic Acids Res. (1984) 12:2181-2192 !$#title The nucleotide sequence of the Escherichia coli fus gene, !1coding for elongation factor G. !$#cross-references MUID:84144098; PMID:6322136 !$#accession I41064 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-704 ##label RES !'##cross-references EMBL:X00415; NID:g41516; PIDN:CAA25120.1; !1PID:g41517 GENETICS !$#gene fusA; strC !$#map_position 73 min CLASSIFICATION #superfamily translation elongation factor G; translation !1elongation factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop; protein !1biosynthesis FEATURE !$2-704 #product translation elongation factor G #status !8experimental #label MAT\ !$11-145 #domain translation elongation factor Tu homology !8#label ETU\ !$17-24 #region nucleotide-binding motif A (P-loop)\ !$142-145 #region GTP-binding NKXD motif\ !$318-320 #region GTP-binding SAK/L motif\ !$23,24,62,142,143, !$145,318 #binding_site Mg-GTP (Lys, Thr, Thr, Asn, Lys, Asp, !8Ser) #status predicted SUMMARY #length 704 #molecular-weight 77581 #checksum 6550 SEQUENCE /// ENTRY EFTWG #type complete TITLE translation elongation factor EF-G - Thermus aquaticus ORGANISM #formal_name Thermus aquaticus DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 19-Jan-2001 ACCESSIONS S15928; S29294; S05978 REFERENCE S15928 !$#authors Yakhnin, A.V.; Vorozheykina, D.P.; Matvienko, N.I. !$#journal Nucleic Acids Res. (1989) 17:8863 !$#title Nucleotide sequence of the Thermus thermophilus HB8 gene !1coding for elongation factor G. !$#cross-references MUID:90067858; PMID:2587224 !$#accession S15928 !'##molecule_type DNA !'##residues 1-691 ##label YAK !'##cross-references EMBL:X16278; NID:g48239; PIDN:CAA34354.1; !1PID:g48240 !'##experimental_source HB8 !'##note the authors did not translate the codon for residue 1 !'##note the source is designated as Thermus thermophilus REFERENCE S29293 !$#authors Voss, R.H.; Hartmann, R.K.; Lippmann, C.; Alexander, C.; !1Jahn, O.; Erdmann, V.A. !$#journal Eur. J. Biochem. (1992) 207:839-846 !$#title Sequence of the tufA gene encoding elongation factor EF-Tu !1from Thermus aquaticus and overproduction of the protein in !1Escherichia coli. !$#cross-references MUID:92362620; PMID:1499561 !$#accession S29294 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 675-680,'R',682,'I',684-691 ##label VOS !'##cross-references EMBL:X66322; NID:g49096; PIDN:CAA46997.1; !1PID:g49097 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1May 1992 GENETICS !$#gene fus CLASSIFICATION #superfamily translation elongation factor G; translation !1elongation factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop; protein !1biosynthesis FEATURE !$13-140 #domain translation elongation factor Tu homology !8#label ETU\ !$19-26 #region nucleotide-binding motif A (P-loop)\ !$262-264 #region GTP-binding SAK/L motif\ !$25,26,64,137,138, !$140,262 #binding_site Mg-GTP (Lys, Thr, Thr, Asn, Lys, Asp, !8Ser) #status predicted SUMMARY #length 691 #molecular-weight 76879 #checksum 3657 SEQUENCE /// ENTRY S04429 #type complete TITLE translation elongation factor EF-G - Synechococcus sp. (strain PCC 6301) ORGANISM #formal_name Synechococcus sp. DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 19-Jan-2001 ACCESSIONS S04429 REFERENCE S04426 !$#authors Meng, B.Y.; Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 216:25-30 !$#title Genes for the ribosomal proteins S12 and S7 and elongation !1factors EF-G and EF-Tu of the cyanobacterium, Anacystis !1nidulans: structural homology between 16S rRNA and S7 mRNA. !$#cross-references MUID:89281486; PMID:2499762 !$#accession S04429 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-694 ##label MEN !'##cross-references GB:X17442; NID:g11204; PIDN:CAA35495.1; !1PID:g1405432 !'##note the source is designated as Anacystis nidulans GENETICS !$#gene fus CLASSIFICATION #superfamily translation elongation factor G; translation !1elongation factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop; protein !1biosynthesis FEATURE !$11-138 #domain translation elongation factor Tu homology !8#label ETU\ !$17-24 #region nucleotide-binding motif A (P-loop)\ !$135-138 #region GTP-binding NKXD motif\ !$311-313 #region GTP-binding SAK/L motif\ !$23,24,62,135,136, !$138,311 #binding_site Mg-GTP (Lys, Thr, Thr, Asn, Lys, Asp, !8Ser) #status predicted SUMMARY #length 694 #molecular-weight 75909 #checksum 4617 SEQUENCE /// ENTRY S40780 #type complete TITLE translation elongation factor EF-G, mitochondrial - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S40780 REFERENCE S40780 !$#authors Barker, C.; Makris, A.; Patriotis, C.; Bear, S.E.; Tsichlis, !1P.N. !$#journal Nucleic Acids Res. (1993) 21:2641-2647 !$#title Identification of the gene encoding the mitochondrial !1elongation factor G in mammals. !$#cross-references MUID:93324327; PMID:8332461 !$#accession S40780 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-752 ##label BAR !'##cross-references EMBL:L14684; NID:g310101; PIDN:AAA41107.1; !1PID:g310102 GENETICS !$#map_position 2 CLASSIFICATION #superfamily translation elongation factor G; translation !1elongation factor Tu homology KEYWORDS GTP binding; mitochondrion; nucleotide binding; P-loop; !1protein biosynthesis FEATURE !$48-178 #domain translation elongation factor Tu homology !8#label ETU\ !$54-61 #region nucleotide-binding motif A (P-loop)\ !$175-178 #region GTP-binding NKXD motif\ !$300-302 #region GTP-binding SAK/L motif\ !$60,61,102,175,176, !$178,300 #binding_site Mg-GTP (Lys, Thr, Thr, Asn, Lys, Asp, !8Ser) #status predicted SUMMARY #length 752 #molecular-weight 83769 #checksum 7583 SEQUENCE /// ENTRY S61642 #type complete TITLE translation elongation factor EF-G, mitochondrial - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein L2195; protein YLR069c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S61642; S20179; S64897; S64901; S17025 REFERENCE S61618 !$#authors Urrestarazu, L.A. !$#submission submitted to the EMBL Data Library, December 1995 !$#accession S61642 !'##molecule_type DNA !'##residues 1-761 ##label URR !'##cross-references EMBL:X94607; NID:g1181264; PIDN:CAA64315.1; !1PID:g1181289 REFERENCE S20177 !$#authors Vambutas, A.; Ackerman, S.H.; Tzagoloff, A. !$#journal Eur. J. Biochem. (1991) 201:643-652 !$#title Mitochondrial translational-initiation and elongation !1factors in Saccharomyces cerevisiae. !$#cross-references MUID:92037620; PMID:1935960 !$#accession S20179 !'##molecule_type DNA !'##residues 1-65,'I',67-232,'V',234-477,'S',479-628,'P',630-761 ##label !1VAM !'##cross-references EMBL:X58378; NID:g3917; PIDN:CAA41267.1; PID:g3918 REFERENCE S64872 !$#authors Andre, B.; Urrestarazu, L.A. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64897 !'##molecule_type DNA !'##residues 1-761 ##label AND !'##cross-references EMBL:Z73241; NID:g1360421; PIDN:CAA97626.1; !1PID:g1360422; GSPDB:GN00012; MIPS:YLR069c !'##experimental_source strain S288C REFERENCE S64899 !$#authors Pohl, T.M. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64901 !'##molecule_type DNA !'##residues 1-761 ##label POH !'##cross-references EMBL:Z73241; NID:g1360421; PIDN:CAA97626.1; !1PID:g1360422; GSPDB:GN00012; MIPS:YLR069c !'##experimental_source strain S288C GENETICS !$#gene SGD:MEF1; MIPS:YLR069c !'##cross-references SGD:S0004059; MIPS:YLR069c !$#map_position 12R CLASSIFICATION #superfamily translation elongation factor G; translation !1elongation factor Tu homology KEYWORDS GTP binding; mitochondrion; nucleotide binding; P-loop; !1protein biosynthesis FEATURE !$71-205 #domain translation elongation factor Tu homology !8#label ETU\ !$77-84 #region nucleotide-binding motif A (P-loop)\ !$202-205 #region GTP-binding NKXD motif\ !$327-329 #region GTP-binding SAK/L motif SUMMARY #length 761 #molecular-weight 84573 #checksum 8835 SEQUENCE /// ENTRY I40188 #type complete TITLE tetracycline resistance protein tetQ - Bacteroides fragilis ALTERNATE_NAMES tetA(Q)2 ORGANISM #formal_name Bacteroides fragilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS I40188; I40189; S34643 REFERENCE I40188 !$#authors Lepine, G.; Lacroix, J.M.; Walker, C.B.; Progulske-Fox, A. !$#journal Antimicrob. Agents Chemother. (1993) 37:2037-2041 !$#title Sequencing of a tet(Q) gene isolated from Bacteroides !1fragilis 1126. !$#cross-references MUID:94058212; PMID:7916585 !$#accession I40188 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-657 ##label RES !'##cross-references EMBL:Z21523; NID:g394758; PIDN:CAA79727.1; !1PID:g580768 !$#accession I40189 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 17-657 ##label RE2 !'##cross-references EMBL:Z21523; NID:g394758; PIDN:CAA79728.1; !1PID:g394760 GENETICS !$#gene tetA(Q)2 !$#start_codon GTG CLASSIFICATION #superfamily translation elongation factor G; translation !1elongation factor Tu homology KEYWORDS antibiotic resistance; GTP binding; nucleotide binding; !1P-loop FEATURE !$20-147 #domain translation elongation factor Tu homology !8#label ETU\ !$26-33 #region nucleotide-binding motif A (P-loop)\ !$144-147 #region GTP-binding NKXD motif\ !$380-382 #region GTP-binding SAK/L motif SUMMARY #length 657 #molecular-weight 74440 #checksum 1896 SEQUENCE /// ENTRY S41522 #type complete TITLE tetracycline resistance protein tetB - Clostridium perfringens ORGANISM #formal_name Clostridium perfringens DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S41522 REFERENCE S41522 !$#authors Sloan, J.; McMurry, L.M.; Lyras, D.; Levy, S.B.; Rood, J.I. !$#journal Mol. Microbiol. (1994) 11:403-415 !$#title The Clostridium perfringens Tet P determinant comprises two !1overlapping genes: tetA(P), which mediates active !1tetracycline efflux, and tetB(P), which is related to the !1ribosomal protection family of tetracycline-resistance !1determinants. !$#cross-references MUID:94224158; PMID:8170402 !$#accession S41522 !'##status preliminary !'##molecule_type DNA !'##residues 1-652 ##label SLO !'##cross-references GB:L20800; NID:g456030; PIDN:AAA20117.1; !1PID:g456035 CLASSIFICATION #superfamily translation elongation factor G; translation !1elongation factor Tu homology KEYWORDS antibiotic resistance; GTP binding; nucleotide binding; !1P-loop FEATURE !$5-132 #domain translation elongation factor Tu homology !8#label ETU\ !$11-18 #region nucleotide-binding motif A (P-loop)\ !$129-132 #region GTP-binding NKXD motif SUMMARY #length 652 #molecular-weight 72722 #checksum 6526 SEQUENCE /// ENTRY A48900 #type complete TITLE tetracycline resistance protein - Streptomyces lividans ALTERNATE_NAMES translation elongation factor homolog ORGANISM #formal_name Streptomyces lividans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS A48900 REFERENCE A48900 !$#authors Dittrich, W.; Schrempf, H. !$#journal Antimicrob. Agents Chemother. (1992) 36:1119-1124 !$#title The unstable tetracycline resistance gene of Streptomyces !1lividans 1326 encodes a putative protein with similarities !1to translational elongation factors and Tet(M) and Tet(O) !1proteins. !$#cross-references MUID:92378191; PMID:1510403 !$#contents 1326 !$#accession A48900 !'##molecule_type DNA !'##residues 1-639 ##label DIT !'##cross-references GB:M74049; NID:g153501; PIDN:AAA26830.1; !1PID:g153502 !'##note sequence extracted from NCBI backbone (NCBIN:111405, !1NCBIP:111406) CLASSIFICATION #superfamily translation elongation factor G; translation !1elongation factor Tu homology KEYWORDS antibiotic resistance; GTP binding; nucleotide binding; !1P-loop FEATURE !$4-131 #domain translation elongation factor Tu homology !8#label ETU\ !$10-17 #region nucleotide-binding motif A (P-loop)\ !$128-131 #region GTP-binding NKXD motif\ !$223-225 #region GTP-binding SAK/L motif\ !$16,17,55,128,129, !$131,223 #binding_site Mg-GTP (Lys, Thr, Thr, Asn, Lys, Asp, !8Ser) #status predicted SUMMARY #length 639 #molecular-weight 67171 #checksum 3947 SEQUENCE /// ENTRY S18572 #type complete TITLE tetracycline resistance protein otrA - Streptomyces rimosus ORGANISM #formal_name Streptomyces rimosus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S18572 REFERENCE S18571 !$#authors Doyle, D.; McDowall, K.J.; Butler, M.J.; Hunter, I.S. !$#journal Mol. Microbiol. (1991) 5:2923-2933 !$#title Characterization of an oxytetracycline-resistance gene, !1otrA, of Streptomyces rimosus. !$#cross-references MUID:92236410; PMID:1809836 !$#accession S18572 !'##status preliminary !'##molecule_type DNA !'##residues 1-663 ##label DOY !'##cross-references EMBL:X53401; NID:g47472; PIDN:CAA37477.1; !1PID:g47473 GENETICS !$#gene otrA CLASSIFICATION #superfamily translation elongation factor G; translation !1elongation factor Tu homology KEYWORDS antibiotic resistance; GTP binding; nucleotide binding; !1P-loop FEATURE !$4-131 #domain translation elongation factor Tu homology !8#label ETU\ !$10-17 #region nucleotide-binding motif A (P-loop)\ !$128-131 #region GTP-binding NKXD motif\ !$230-232 #region GTP-binding SAK/L motif\ !$16,17,55,128,129, !$131,230 #binding_site Mg-GTP (Lys, Thr, Thr, Asn, Lys, Asp, !8Ser) #status predicted SUMMARY #length 663 #molecular-weight 71786 #checksum 722 SEQUENCE /// ENTRY EFECS #type complete TITLE translation elongation factor EF-Ts - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 02-Apr-1982 #sequence_revision 02-Apr-1982 #text_change 01-Mar-2002 ACCESSIONS A03525; A45269; A32881; S45235; B64741; S66207 REFERENCE A02696 !$#authors An, G.; Bendiak, D.S.; Mamelak, L.A.; Friesen, J.D. !$#journal Nucleic Acids Res. (1981) 9:4163-4172 !$#title Organization and nucleotide sequence of a new ribosomal !1operon in Escherichia coli containing the genes for !1ribosomal protein S2 and elongation factor Ts. !$#cross-references MUID:82059454; PMID:6272196 !$#accession A03525 !'##molecule_type DNA !'##residues 1-283 ##label ANG !'##cross-references GB:V00343; NID:g42841; PIDN:CAA23632.1; PID:g42843 REFERENCE A45269 !$#authors Yamanaka, K.; Ogura, T.; Niki, H.; Hiraga, S. !$#journal J. Bacteriol. (1992) 174:7517-7526 !$#title Identification and characterization of the smbA gene, a !1suppressor of the mukB null mutant of Escherichia coli. !$#cross-references MUID:93077430; PMID:1447125 !$#contents W3110 !$#accession A45269 !'##molecule_type DNA !'##residues 179-283 ##label YAM !'##cross-references GB:D13334; NID:g216660; PIDN:BAA02597.1; !1PID:g216661 !'##note sequence extracted from NCBI backbone (NCBIP:119077) REFERENCE A32881 !$#authors Ichikawa, S.; Ryoji, M.; Siegfried, Z.; Kaji, A. !$#journal J. Bacteriol. (1989) 171:3689-3695 !$#title Localization of the ribosome-releasing factor gene in the !1Escherichia coli chromosome. !$#cross-references MUID:89291711; PMID:2661533 !$#accession A32881 !'##molecule_type DNA !'##residues 199-275 ##label ICH !'##cross-references GB:M27211 REFERENCE S45181 !$#authors Fujita, N. !$#submission submitted to the EMBL Data Library, January 1994 !$#accession S45235 !'##molecule_type DNA !'##residues 1-283 ##label FUJ !'##cross-references EMBL:D26562; NID:g473770; PIDN:BAA05614.1; !1PID:g473825 !'##experimental_source strain K-12, substrain W3110 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64741 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-283 ##label BLAT !'##cross-references GB:AE000126; GB:U00096; NID:g1786358; !1PIDN:AAC73281.1; PID:g1786366; UWGP:b0170 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S66207 !$#authors Bogestrand, S.; Wiborg, O.; Thirup, S.; Nyborg, J. !$#journal FEBS Lett. (1995) 368:49-54 !$#title Analysis and crystallization of a 25 kDa C-terminal fragment !1of cloned elongation factor Ts from Escherichia coli. !$#cross-references MUID:95339981; PMID:7615087 !$#accession S66207 !'##molecule_type protein !'##residues 52-56 ##label BOG GENETICS !$#gene tsf !$#map_position 4 min CLASSIFICATION #superfamily translation elongation factor EF-Ts KEYWORDS protein biosynthesis SUMMARY #length 283 #molecular-weight 30423 #checksum 5340 SEQUENCE /// ENTRY B35270 #type complete TITLE translation elongation factor EF-Ts - Spiroplasma citri ORGANISM #formal_name Spiroplasma citri DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 07-Dec-1999 ACCESSIONS B35270 REFERENCE A35270 !$#authors Chevalier, C.; Saillard, C.; Bove, J.M. !$#journal J. Bacteriol. (1990) 172:2693-2703 !$#title Organization and nucleotide sequences of the Spiroplasma !1citri genes for ribosomal protein S2, elongation factor Ts, !1spiralin, phosphofructokinase, pyruvate kinase, and an !1unidentified protein. !$#cross-references MUID:90236934; PMID:2139649 !$#accession B35270 !'##status preliminary !'##molecule_type DNA !'##residues 1-297 ##label CHE !'##cross-references GB:M31161; NID:g152884; PID:g152886 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily translation elongation factor EF-Ts SUMMARY #length 297 #molecular-weight 32828 #checksum 1945 SEQUENCE /// ENTRY S25432 #type complete TITLE translation elongation factor eEF-1 beta chain - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 29-Sep-1999 ACCESSIONS S25432; JQ1038; B61013; S15689 REFERENCE S25432 !$#authors Sanders, J.; Maassen, J.A.; Amons, R.; Moeller, W. !$#journal Nucleic Acids Res. (1991) 19:4551 !$#title Nucleotide sequence of human elongation factor-1-beta cDNA. !$#cross-references MUID:91360360; PMID:1886777 !$#accession S25432 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-225 ##label SAN !'##cross-references EMBL:X60489; NID:g31099; PIDN:CAA43019.1; !1PID:g31100 REFERENCE JQ1038 !$#authors Von der Kammer, H.; Klaudiny, J.; Zimmer, M.; Scheit, K.H. !$#journal Biochem. Biophys. Res. Commun. (1991) 177:312-317 !$#title Human elongation factor 1beta: cDNA and derived amino acid !1sequence. !$#cross-references MUID:91254293; PMID:1710449 !$#accession JQ1038 !'##molecule_type mRNA !'##residues 1-225 ##label VON !'##cross-references GB:X60656; NID:g31134; PIDN:CAA43063.1; PID:g31135 !'##experimental_source ovarian granulosa cells REFERENCE A61002 !$#authors Bauw, G.; Rasmussen, H.H.; Van Den Bulcke, M.; Van Damme, !1J.; Puype, M.; Gesser, B.; Celis, J.E.; Vandekerckhove, J. !$#journal Electrophoresis (1990) 11:528-536 !$#title Two-dimensional gel electrophoresis, protein electroblotting !1and microsequencing: a direct link between proteins and !1genes. !$#cross-references MUID:91031404; PMID:1699755 !$#accession B61013 !'##status preliminary !'##molecule_type protein !'##residues 2-6,'X';'X',56-60 ##label BAU GENETICS !$#gene GDB:EEF1B2 !'##cross-references GDB:682589 !$#map_position 2pter-2qter CLASSIFICATION #superfamily translation elongation factor eEF-1 beta chain; !1translation elongation factor eEF-1 beta chain GTP exchange !1domain homology KEYWORDS phosphoprotein; protein biosynthesis FEATURE !$2-225 #product translation elongation factor eEF-1 beta !8chain #status predicted #label MAT SUMMARY #length 225 #molecular-weight 24763 #checksum 3459 SEQUENCE /// ENTRY A24806 #type complete TITLE translation elongation factor eEF-1 beta chain - brine shrimp ORGANISM #formal_name Artemia franciscana #common_name brine shrimp DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A24806; S13148 REFERENCE A24806 !$#authors Maessen, G.D.F.; Amons, R.; Maassen, J.A.; Moeller, W. !$#journal FEBS Lett. (1986) 208:77-83 !$#title Primary structure of elongation factor 1-beta- from Artemia. !$#accession A24806 !'##molecule_type mRNA !'##residues 1-207 ##label MAE !'##cross-references GB:M35636; NID:g161169; PIDN:AAC83402.1; !1PID:g161170 REFERENCE S13148 !$#authors van Damme, H.T.F.; Amons, R.; Karssies, R.; Timmers, C.J.; !1Janssen, G.M.C.; Moeller, W. !$#journal Biochim. Biophys. Acta (1990) 1050:241-247 !$#title Elongation factor 1-beta of artemia: localization of !1functional sites and homology to elongation factor 1-delta. !$#cross-references MUID:91002651; PMID:2207149 !$#accession S13148 !'##molecule_type protein !'##residues 2-207 ##label DAM CLASSIFICATION #superfamily translation elongation factor eEF-1 beta chain; !1translation elongation factor eEF-1 beta chain GTP exchange !1domain homology KEYWORDS phosphoprotein; protein biosynthesis SUMMARY #length 207 #molecular-weight 23324 #checksum 3629 SEQUENCE /// ENTRY S35514 #type complete TITLE translation elongation factor eEF-1 beta chain - silkworm ORGANISM #formal_name Bombyx mori #common_name silkworm DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S35514 REFERENCE S35514 !$#authors Taira, H.; Kamiie, K.; Kakuta, A.; Ooura, H.; Matsumoto, S.; !1Ejiri, S.; Katsumata, T. !$#journal Nucleic Acids Res. (1992) 20:6734 !$#title Nucleotide sequence of the cDNA encoding silk gland !1elongation factor 1-beta'. !$#cross-references MUID:93126120; PMID:1480492 !$#accession S35514 !'##status preliminary; nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-222 ##label TAI !'##cross-references EMBL:D13339; NID:g217275; PIDN:BAA02602.1; !1PID:g217276 CLASSIFICATION #superfamily translation elongation factor eEF-1 beta chain; !1translation elongation factor eEF-1 beta chain GTP exchange !1domain homology SUMMARY #length 222 #molecular-weight 24548 #checksum 1593 SEQUENCE /// ENTRY S44832 #type complete TITLE translation elongation factor eEF-1 beta chain - Caenorhabditis elegans ALTERNATE_NAMES protein F54H12.6 ORGANISM #formal_name Caenorhabditis elegans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S44832 REFERENCE S44831 !$#authors Latreille, P. !$#submission submitted to the EMBL Data Library, November 1993 !$#description Sequence of the C. elegans cosmid F54H12. !$#accession S44832 !'##status preliminary !'##molecule_type DNA !'##residues 1-213 ##label LAT !'##cross-references EMBL:L25599; NID:g409296; PIDN:AAA28051.1; !1PID:g409298 GENETICS !$#map_position 3 !$#introns 26/2; 170/1 CLASSIFICATION #superfamily translation elongation factor eEF-1 beta chain; !1translation elongation factor eEF-1 beta chain GTP exchange !1domain homology KEYWORDS protein biosynthesis SUMMARY #length 213 #molecular-weight 22704 #checksum 5859 SEQUENCE /// ENTRY JC4777 #type complete TITLE translation elongation factor eEF-1 beta chain - Arabidopsis thaliana (cv. WS) ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress #variety cv. WS DATE 10-May-1996 #sequence_revision 11-Apr-1997 #text_change 16-Jul-1999 ACCESSIONS JC4777; S37102 REFERENCE JC4777 !$#authors Gidekel, M.; Jimenez, B.; Herrera-Estrella, L. !$#journal Gene (1996) 170:201-206 !$#title The first intron of the Arabidopsis thaliana gene coding for !1elongation factor 1beta contains an enhancer-like element. !$#cross-references MUID:96235135; PMID:8666245 !$#accession JC4777 !'##molecule_type DNA !'##residues 1-229 ##label GID !'##cross-references EMBL:X74734; NID:g398605; PIDN:CAA52752.1; !1PID:g398606 !'##experimental_source cv. WS GENETICS !$#introns 28/3; 67/3; 139/3 COMPLEX Alpha chain associates with a complex of beta (p30), delta !1(p36 or p34, corresponding to delta-2 or delta-1), and gamma !1(p47) chains. The gamma and delta chains are phosphorylated !1by the cdc2 kinase; the beta chain is phosphorylated in vivo !1by an endogenous kinase and in vitro by casein kinase II. FUNCTION !$#description beta chain catalyzes the replacement of GDP by GTP on !1elongation factor eEF-1 alpha chain; gamma chain enhances !1the exchange; delta chain may help anchor the beta chain to !1microtubules and membranes and also has GDP/GTP exchange !1activity !$#pathway protein biosynthesis CLASSIFICATION #superfamily translation elongation factor eEF-1 beta chain; !1translation elongation factor eEF-1 beta chain GTP exchange !1domain homology KEYWORDS GTP exchange; phosphoprotein; protein biosynthesis SUMMARY #length 229 #molecular-weight 25094 #checksum 2369 SEQUENCE /// ENTRY S29224 #type complete TITLE translation elongation factor eEF-1 beta' chain - rice ORGANISM #formal_name Oryza sativa #common_name rice DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S29224; S39846; JS0729 REFERENCE S29224 !$#authors Matsumoto, S.; Oizumi, N.; Taira, H.; Ejiri, S. !$#journal FEBS Lett. (1992) 311:46-48 !$#title Cloning and sequencing of the cDNA encoding rice elongation !1factor 1beta'. !$#cross-references MUID:93011944; PMID:1397289 !$#accession S29224 !'##molecule_type mRNA !'##residues 1-223 ##label MAT1 !'##cross-references DDBJ:D12821; NID:g218160; PIDN:BAA02253.1; !1PID:g218161 !'##note submitted to JIPID, August 1992 !$#accession S39846 !'##molecule_type protein !'##residues 2-32 ##label MAT2 !'##experimental_source strain Hayayuki CLASSIFICATION #superfamily translation elongation factor eEF-1 beta chain; !1translation elongation factor eEF-1 beta chain GTP exchange !1domain homology KEYWORDS protein biosynthesis FEATURE !$2-223 #product translation elongation factor eEF-1 beta' !8chain #status predicted #label MAT SUMMARY #length 223 #molecular-weight 23773 #checksum 2094 SEQUENCE /// ENTRY S35501 #type complete TITLE translation elongation factor eEF-1 beta' chain - wheat ORGANISM #formal_name Triticum aestivum #common_name common wheat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S35501; JS0760 REFERENCE S35501 !$#authors Oizumi, N.; Matsumoto, S.; Taira, H.; Ejiri, S. !$#journal Nucleic Acids Res. (1992) 20:5225 !$#title Nucleotide sequences of the cDNA encoding wheat elongation !1factor 1-beta'. !$#cross-references MUID:93027267; PMID:1383944 !$#accession S35501 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-216 ##label OIZ1 !'##cross-references EMBL:D13147; NID:g218340; PIDN:BAA02436.1; !1PID:g218341 REFERENCE JS0760 !$#authors Oizumi, N.; Matsumoto, S.; Taira, H.; Ejiri, S. !$#submission submitted to JIPID, September 1992 !$#accession JS0760 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-216 ##label OIZ2 !'##cross-references DDBJ:D13147; NID:g218340; PIDN:BAA02436.1; !1PID:g218341 !'##experimental_source strain Nanbukomugi CLASSIFICATION #superfamily translation elongation factor eEF-1 beta chain; !1translation elongation factor eEF-1 beta chain GTP exchange !1domain homology KEYWORDS protein biosynthesis SUMMARY #length 216 #molecular-weight 23088 #checksum 5558 SEQUENCE /// ENTRY S34626 #type complete TITLE translation elongation factor eEF-1 delta chain - human ORGANISM #formal_name Homo sapiens #common_name man DATE 01-Feb-1995 #sequence_revision 11-Apr-1997 #text_change 16-Jul-1999 ACCESSIONS S34626; S31789 REFERENCE S34626 !$#authors Sanders, J.; Raggiaschi, R.; Morales, J.; Moeller, W. !$#journal Biochim. Biophys. Acta (1993) 1174:87-90 !$#title The human leucine zipper-containing guanine-nucleotide !1exchange protein elongation factor-1-delta. !$#cross-references MUID:93326642; PMID:8334168 !$#accession S34626 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-281 ##label SAN1 !'##cross-references EMBL:Z21507; NID:g38521; PIDN:CAA79716.1; !1PID:g38522 REFERENCE S31789 !$#authors Sanders, J.J.; Raggiaschi, R.R.; Moeller, W.W. !$#submission submitted to the EMBL Data Library, January 1993 !$#description Sequencing of the human guanine-nucleotide exchange protein !1elongation factor-1-delta. !$#accession S31789 !'##molecule_type mRNA !'##residues 1-33,'A',35-67,'RG',70-124,'RPTDPARI',133;135-281 ##label !1SAN2 !'##cross-references EMBL:Z21507 GENETICS !$#gene GDB:EEF1D; EF-1D !'##cross-references GDB:216099; OMIM:130592 !$#map_position Xpter-Xqter COMPLEX Alpha chain associates with a complex of beta, delta, and !1gamma chains. The gamma and delta chains are phosphorylated !1by the cdc2 kinase; the beta chain is phosphorylated in vivo !1by an endogenous kinase and in vitro by casein kinase II. FUNCTION !$#description beta chain catalyzes the replacement of GDP by GTP on !1elongation factor eEF-1 alpha chain; gamma chain enhances !1the exchange; delta chain may help anchor the beta chain to !1microtubules and membranes and also has GDP/GTP exchange !1activity !$#pathway protein biosynthesis CLASSIFICATION #superfamily translation elongation factor eEF-1 beta chain; !1translation elongation factor eEF-1 beta chain GTP exchange !1domain homology KEYWORDS GTP exchange; leucine zipper; phosphoprotein; protein !1biosynthesis FEATURE !$80-115 #region leucine zipper motif SUMMARY #length 281 #molecular-weight 31221 #checksum 4196 SEQUENCE /// ENTRY S30223 #type complete TITLE translation elongation factor eEF-1 beta chain - African clawed frog ALTERNATE_NAMES translation elongation factor eEF-1 p30 protein ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 13-Jan-1995 #sequence_revision 05-Jan-1996 #text_change 16-Jul-1999 ACCESSIONS S30223; S49566; B39331; S08838 REFERENCE S30223 !$#authors Cormier, P.; Osborne, H.B.; Morales, J.; Bassez, T.; !1Minella, O.; Poulhe, R.; Belle, R.; Mulner-Lorillon, O. !$#journal Nucleic Acids Res. (1993) 21:743 !$#title Elongation factor 1 contains two homologous !1guanine-nucleotide exchange proteins as shown from the !1molecular cloning of beta and delta subunits. !$#cross-references MUID:93181274; PMID:8441685 !$#accession S30223 !'##molecule_type mRNA !'##residues 1-227 ##label COR !'##cross-references EMBL:X69764; NID:g64661; PIDN:CAA49418.1; !1PID:g64662 !$#accession S49566 !'##molecule_type protein !'##residues 18-26;148-154;208-213;214-220 ##label CO2 REFERENCE A39331 !$#authors Janssen, G.M.C.; Morales, J.; Schipper, A.; Labbes, J.C.; !1Mulner-Lorillon, O.; Belle, R.; Moeller, W. !$#journal J. Biol. Chem. (1991) 266:14885-14888 !$#title A major substrate of maturation promoting factor identified !1as elongation factor 1 betagammadelta in Xenopus laevis. !$#cross-references MUID:91331996; PMID:1869528 !$#accession B39331 !'##molecule_type protein !'##residues 148-154;208-209,'G',211-213;214-220 ##label JAN REFERENCE S08838 !$#authors Belle, R.; Derancourt, J.; Poulhe, R.; Capony, J.P.; Ozon, !1R.; Mulner-Lorillon, O. !$#journal FEBS Lett. (1989) 255:101-104 !$#title A purified complex from Xenopus oocytes contains a p47 !1protein, an in vivo substrate of MPF, and a p30 protein !1respectively homologous to elongation factors EF-1gamma and !1EF-1beta. !$#cross-references MUID:90005944; PMID:2676593 !$#accession S08838 !'##molecule_type protein !'##residues 18-26;148-154;208-209,'G',211-213;214-220 ##label BEL COMPLEX The complex consists of beta (p30), delta (p36), and gamma !1(p47) chains. The gamma chain is phosphorylated by the cdc2 !1kinase; the beta and delta chains are phosphorylated in vivo !1by an endogenous kinase and in vitro by casein kinase II. FUNCTION !$#description beta chain catalyzes the replacement of GDP by GTP on !1elongation factor eEF-1 alpha chain; gamma chain enhances !1the exchange; delta chain may help anchor the beta chain to !1microtubules and membranes and also has GDP/GTP exchange !1activity !$#pathway protein biosynthesis CLASSIFICATION #superfamily translation elongation factor eEF-1 beta chain; !1translation elongation factor eEF-1 beta chain GTP exchange !1domain homology KEYWORDS GTP exchange; phosphoprotein; protein biosynthesis FEATURE !$108 #binding_site phosphate (Ser) (covalent) (by !8unidentified kinase) #status predicted SUMMARY #length 227 #molecular-weight 25175 #checksum 9307 SEQUENCE /// ENTRY S22655 #type complete TITLE translation elongation factor eEF-1 gamma chain - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 29-Sep-1999 ACCESSIONS S22655; S26676; S22130 REFERENCE S22655 !$#authors Kumabe, T.; Sohma, Y.; Yamamoto, T. !$#journal Nucleic Acids Res. (1992) 20:2598 !$#title Human cDNAs encoding elongation factor 1gamma and the !1ribosomal protein L19. !$#cross-references MUID:92285147; PMID:1598220 !$#accession S22655 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type mRNA !'##residues 1-437 ##label KUM !'##cross-references EMBL:X63526; NID:g31101; PIDN:CAA45089.1; !1PID:g31102 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1991 REFERENCE S26676 !$#authors Sanders, J.; Maassen, J.A.; Moeller, W. !$#journal Nucleic Acids Res. (1992) 20:5907-5910 !$#title Elongation factor-1 messenger-RNA levels in cultured cells !1are high compared to tissue and are not drastically affected !1further by oncogenic transformation. !$#cross-references MUID:93096576; PMID:1461723 !$#accession S26676 !'##molecule_type mRNA !'##residues 1-437 ##label SAN !'##cross-references EMBL:Z11531; NID:g31103; PIDN:CAA77630.1; !1PID:g31104 COMMENT S22655(49-98) is homologous to dichloromethane dehalogenase !1A47654(56-113) and translation elongation factor gamma !1S22655(49-98). GENETICS !$#gene GDB:EEF1G !'##cross-references GDB:133781; OMIM:130593 CLASSIFICATION #superfamily translation elongation factor eEF-1 gamma chain KEYWORDS protein biosynthesis SUMMARY #length 437 #molecular-weight 50118 #checksum 6643 SEQUENCE /// ENTRY S26649 #type complete TITLE translation elongation factor eEF-1 gamma chain - rabbit ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S26649; S25524 REFERENCE S26649 !$#authors Sheu, G.T.; Traugh, J.A. !$#journal Nucleic Acids Res. (1992) 20:5849 !$#title Nucleotide sequence of a rabbit cDNA encoding elongation !1factor 1 gamma. !$#cross-references MUID:93087211; PMID:1454551 !$#accession S26649 !'##molecule_type mRNA !'##residues 1-437 ##label SHE !'##cross-references EMBL:X68142; NID:g1552; PIDN:CAA48242.1; PID:g1553 CLASSIFICATION #superfamily translation elongation factor eEF-1 gamma chain KEYWORDS protein biosynthesis SUMMARY #length 437 #molecular-weight 50048 #checksum 4989 SEQUENCE /// ENTRY S00162 #type complete TITLE translation elongation factor eEF-1 gamma chain - brine shrimp ORGANISM #formal_name Artemia sp. #common_name brine shrimp DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S00162 REFERENCE S00162 !$#authors Maessen, G.D.F.; Amons, R.; Zeelen, J.P.; Moeller, W. !$#journal FEBS Lett. (1987) 223:181-186 !$#title Primary structure of elongation factor 1-gamma from Artemia. !$#cross-references MUID:88030035; PMID:3666137 !$#accession S00162 !'##molecule_type mRNA !'##residues 1-430 ##label MAE !'##cross-references EMBL:M28020; NID:g161171; PIDN:AAC83401.1; !1PID:g161172 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing !'##note 137-Glu, 189-Met, and 412-Ser were also found COMMENT Elongation factor 1 mediates the transport of aminoacyl-tRNA !1to 80S ribosomes. It is composed of three subunits, named !1alpha, beta and gamma. The beta-gamma complex mediates GDP/ !1GTP exchange in the alpha subunit. CLASSIFICATION #superfamily translation elongation factor eEF-1 gamma chain KEYWORDS GTP binding; protein biosynthesis FEATURE !$2-430 #product translation elongation factor eEF-1 gamma !8chain #status experimental #label MAT SUMMARY #length 430 #molecular-weight 49309 #checksum 1906 SEQUENCE /// ENTRY S57631 #type complete TITLE translation elongation factor eEF-1 delta-2 chain - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 19-Oct-1995 #sequence_revision 11-Apr-1997 #text_change 02-Aug-2002 ACCESSIONS S65483; S65446; A39331; S57631 REFERENCE S65446 !$#authors Minella, O.; Mulner-Lorillon, O.; Poulhe, R.; Belle, R.; !1Cormier, P. !$#journal Eur. J. Biochem. (1996) 237:685-690 !$#title The guanine-nucleotide-exchange complex !1(EF-1-beta-gamma-delta) of elongation factor-1 contains two !1similar leucine-zipper proteins EF-1-delta, p34 encoded by !1EF-1-delta(1) and p36 encoded by EF-1-delta(2). !$#cross-references MUID:96235233; PMID:8647113 !$#accession S65483 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-260 ##label MIN !'##cross-references EMBL:X85096; NID:g886723; PIDN:CAA59420.1; !1PID:g886724 !'##experimental_source oocyte !$#accession S65446 !'##molecule_type protein !'##residues 15-38;69-73;81-85;110-116;181-187;221-240;242-258 ##label !1MIW REFERENCE A39331 !$#authors Janssen, G.M.C.; Morales, J.; Schipper, A.; Labbes, J.C.; !1Mulner-Lorillon, O.; Belle, R.; Moeller, W. !$#journal J. Biol. Chem. (1991) 266:14885-14888 !$#title A major substrate of maturation promoting factor identified !1as elongation factor 1 betagammadelta in Xenopus laevis. !$#cross-references MUID:91331996; PMID:1869528 !$#accession A39331 !'##molecule_type protein !'##residues 15-27;110-115,'I';181-187;221-225,'X',227-240;242-258 !1##label JAN COMPLEX the alpha chain associates with a complex of beta (p30), !1delta (p36 or p34, corresponding to delta-2 or delta-1), and !1gamma (p47) chains; the gamma and delta chains are !1phosphorylated by the cdc2 kinase; the beta chain is !1phosphorylated in vivo by an endogenous kinase and in vitro !1by casein kinase II FUNCTION !$#description beta chain catalyzes the replacement of GDP by GTP on !1elongation factor eEF-1 alpha chain; gamma chain enhances !1the exchange; delta chain may help anchor the beta chain to !1microtubules and membranes and also has GDP/GTP exchange !1activity !$#pathway protein biosynthesis CLASSIFICATION #superfamily translation elongation factor eEF-1 beta chain; !1translation elongation factor eEF-1 beta chain GTP exchange !1domain homology KEYWORDS GTP exchange; leucine zipper; phosphoprotein; protein !1biosynthesis FEATURE !$56-91 #region leucine zipper motif\ !$120 #binding_site phosphate (Thr) (covalent) (by cdc2 !8kinase) #status experimental\ !$141 #binding_site phosphate (Ser) (covalent) (by !8unidentified kinase) #status predicted SUMMARY #length 260 #molecular-weight 28645 #checksum 3845 SEQUENCE /// ENTRY S47630 #type complete TITLE translation elongation factor eEF-1 delta chain - brine shrimp ORGANISM #formal_name Artemia sp. #common_name brine shrimp DATE 19-Mar-1997 #sequence_revision 11-Apr-1997 #text_change 02-Aug-2002 ACCESSIONS S47630; S13149 REFERENCE S47630 !$#authors Amons, R.; Guerrucci, M.A.; Karssies, R.H.; Morales, J.; !1Cormier, P.; Moeller, W.; Belle, R. !$#journal Biochim. Biophys. Acta (1994) 1218:346-350 !$#title The leucine-zipper in elongation factor EF-1-delta, a !1guanine-nucleotide exchange protein, is conserved in Artemia !1and Xenopus. !$#cross-references MUID:94325342; PMID:8049261 !$#accession S47630 !'##molecule_type protein; mRNA !'##residues 1-237 ##label AMO REFERENCE S13148 !$#authors van Damme, H.T.F.; Amons, R.; Karssies, R.; Timmers, C.J.; !1Janssen, G.M.C.; Moeller, W. !$#journal Biochim. Biophys. Acta (1990) 1050:241-247 !$#title Elongation factor 1-beta of artemia: localization of !1functional sites and homology to elongation factor 1-delta. !$#cross-references MUID:91002651; PMID:2207149 !$#accession S13149 !'##molecule_type protein !'##residues 1-31;102-120;'TXI',156-159,'XX',162;176-177,'XX',180-193, !1'T',195-196,'S';219-228 ##label DAM COMPLEX Alpha chain associates with a complex of beta, delta, and !1gamma chains. The gamma and delta chains are phosphorylated !1by the cdc2 kinase; the beta chain is phosphorylated in vivo !1by an endogenous kinase and in vitro by casein kinase II. FUNCTION !$#description beta chain catalyzes the replacement of GDP by GTP on !1elongation factor eEF-1 alpha chain; gamma chain enhances !1the exchange; delta chain may help anchor the beta chain to !1microtubules and membranes and also has GDP/GTP exchange !1activity !$#pathway protein biosynthesis CLASSIFICATION #superfamily translation elongation factor eEF-1 beta chain; !1translation elongation factor eEF-1 beta chain GTP exchange !1domain homology KEYWORDS GTP exchange; leucine zipper; phosphoprotein; protein !1biosynthesis FEATURE !$58-93 #region leucine zipper motif SUMMARY #length 237 #molecular-weight 26318 #checksum 1365 SEQUENCE /// ENTRY S26280 #type complete TITLE translation elongation factor eEF-1 delta-1 chain - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 28-May-1993 #sequence_revision 11-Apr-1997 #text_change 16-Jul-1999 ACCESSIONS S26280; S49567; S24635 REFERENCE S26280 !$#authors Morales, J.; Cormier, P.; Mulner-Lorillon, O.; Poulhe, R.; !1Belle, R. !$#journal Nucleic Acids Res. (1992) 20:4091 !$#title Molecular cloning of a new guanine nucleotide-exchange !1protein, EF1delta. !$#cross-references MUID:92375699; PMID:1508694 !$#accession S26280 !'##molecule_type mRNA !'##residues 1-265 ##label MOR !'##cross-references EMBL:X66837; NID:g64667; PIDN:CAA47313.1; !1PID:g64668 !$#accession S49567 !'##molecule_type protein !'##residues !115-27;28-38;83-87;112-118;122-126;146-150;162-166;186-192; !1226-245;247-251;252-263 ##label MO2 !'##note reference S65483 suggests that Met-30 is the initiator for !1delta-1 and that the sequenced peptides actually come from !1the very similar delta-2 chain COMPLEX Alpha chain associates with a complex of beta (p30), delta !1(p36 or p34, corresponding to delta-2 or delta-1), and gamma !1(p47) chains. The gamma and delta chains are phosphorylated !1by the cdc2 kinase; the beta chain is phosphorylated in vivo !1by an endogenous kinase and in vitro by casein kinase II. FUNCTION !$#description beta chain catalyzes the replacement of GDP by GTP on !1elongation factor eEF-1 alpha chain; gamma chain enhances !1the exchange; delta chain may help anchor the beta chain to !1microtubules and membranes and also has GDP/GTP exchange !1activity !$#pathway protein biosynthesis CLASSIFICATION #superfamily translation elongation factor eEF-1 beta chain; !1translation elongation factor eEF-1 beta chain GTP exchange !1domain homology KEYWORDS GTP exchange; leucine zipper; phosphoprotein; protein !1biosynthesis FEATURE !$58-93 #region leucine zipper motif\ !$122 #binding_site phosphate (Thr) (covalent) (by cdc2 !8kinase) #status predicted\ !$146 #binding_site phosphate (Ser) (covalent) (by !8unidentified kinase) #status predicted SUMMARY #length 265 #molecular-weight 29237 #checksum 2350 SEQUENCE /// ENTRY EFHU2 #type complete TITLE translation elongation factor eEF-2 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1992 #sequence_revision 03-Oct-1995 #text_change 19-Jan-2001 ACCESSIONS S18294; S00467; H33178; S06137 REFERENCE S06137 !$#authors Rapp, G.; Klaudiny, J.; Hagendorff, G.; Luck, M.R.; Scheit, !1K.H. !$#journal Biol. Chem. Hoppe-Seyler (1989) 370:1071-1075 !$#title Complete sequence of the coding region of human elongation !1factor 2 (EF-2) by enzymatic amplification of cDNA from !1human ovarian granulosa cells. !$#cross-references MUID:90121741; PMID:2610926 !$#accession S18294 !'##molecule_type mRNA !'##residues 1-858 ##label RAP !'##cross-references EMBL:X51466; NID:g31105; PIDN:CAA35829.1; !1PID:g31106 REFERENCE S00467 !$#authors Rapp, G.; Mucha, J.; Einspanier, R.; Luck, M.; Scheit, K.H. !$#journal Biol. Chem. Hoppe-Seyler (1988) 369:247-250 !$#title Cloning and sequence analysis of a cDNA from human ovarian !1granulosa cells encoding the C-terminal part of human !1elongation factor 2. !$#cross-references MUID:88293714; PMID:2840927 !$#accession S00467 !'##molecule_type mRNA !'##residues 501-858 ##label RA2 !'##cross-references EMBL:M19997; NID:g181968; PIDN:AAA50388.1; !1PID:g181969 !'##note the amino end of the mature protein was determined by protein !1sequencing REFERENCE A33178 !$#authors Ward, L.D.; Hong, J.; Whitehead, R.H.; Simpson, R.J. !$#journal Electrophoresis (1990) 11:883-891 !$#title Development of a database of amino acid sequences for human !1colon carcinoma proteins separated by two-dimensional !1polyacrylamide gel electrophoresis. !$#cross-references MUID:91176935; PMID:2079031 !$#accession H33178 !'##molecule_type protein !'##residues 2-14,'X',16,'X',18-19 ##label WAR !'##note the amino end of the mature protein was determined COMMENT Phosphorylation is regulatory and inactivates eEF-2. GENETICS !$#gene GDB:EEF2; EF2 !'##cross-references GDB:119104; OMIM:130610 !$#map_position 19pter-19q12 CLASSIFICATION #superfamily translation elongation factor 2; translation !1elongation factor Tu homology KEYWORDS diphthamide; GTP binding; nucleotide binding; P-loop; !1phosphoprotein; protein biosynthesis FEATURE !$2-858 #product translation elongation factor eEF-2 #status !8predicted #label MAT\ !$20-161 #domain translation elongation factor Tu homology !8#label ETU\ !$26-33 #region nucleotide-binding motif A (P-loop)\ !$158-161 #region GTP-binding NKXD motif\ !$57,59 #binding_site phosphate (Thr) (covalent) (by !8elongation factor 2 kinase) #status predicted\ !$715 #modified_site 2'-[3-carboxamido-3- !8(trimethylammonio)propyl]histidine (His) #status !8predicted SUMMARY #length 858 #molecular-weight 95337 #checksum 5839 SEQUENCE /// ENTRY EFRT2 #type complete TITLE translation elongation factor eEF-2 - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 28-Feb-1990 #sequence_revision 02-Dec-1994 #text_change 19-Jan-2001 ACCESSIONS S04007; B25440; A11180; S02526; S62217 REFERENCE S04007 !$#authors Oleinikov, A.V.; Jokhadze, G.G.; Alakhov, Y.B. !$#journal FEBS Lett. (1989) 248:131-136 !$#title Primary structure of rat liver elongation factor 2 deduced !1from the cDNA sequence. !$#cross-references MUID:89252028; PMID:2721670 !$#accession S04007 !'##molecule_type mRNA !'##residues 1-693 ##label OLE !'##cross-references EMBL:Y07504; NID:g56081 !'##note the sequence in GenBank entry RNEF2R (PID:g56082) includes the !1sequence of B25440 not determined by these authors REFERENCE A25440 !$#authors Kohno, K.; Uchida, T.; Ohkubo, H.; Nakanishi, S.; Nakanishi, !1T.; Fukui, T.; Ohtsuka, E.; Ikehara, M.; Okada, Y. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:4978-4982 !$#title Amino acid sequence of mammalian elongation factor 2 deduced !1from the cDNA sequence: homology with GTP-binding proteins. !$#cross-references MUID:86259716; PMID:3014523 !$#accession B25440 !'##molecule_type mRNA !'##residues 516-858 ##label KOH !'##cross-references GB:K03502; NID:g203996; PIDN:AAA41106.1; !1PID:g203997 !'##note nucleotide differences with hamster shown REFERENCE A11180 !$#authors Robinson, E.A.; Henriksen, O.; Maxwell, E.S. !$#journal J. Biol. Chem. (1974) 249:5088-5093 !$#title Elongation factor 2. Amino acid sequence at the site of !1adenosine diphosphate ribosylation. !$#cross-references MUID:74301260; PMID:4368673 !$#accession A11180 !'##molecule_type protein !'##residues 702-714,'X',716 ##label ROB !'##experimental_source liver REFERENCE S02526 !$#authors Nilsson, L.; Nygard, O. !$#journal Eur. J. Biochem. (1988) 171:293-299 !$#title Structural and functional studies of the interaction of the !1eukaryotic elongation factor EF-2 with GTP and ribosomes. !$#cross-references MUID:88111683; PMID:3338467 !$#accession S02526 !'##molecule_type protein !'##residues 2-14;68-79;572-585 ##label NIL REFERENCE S62217 !$#authors Guillot, D.; Vard, C.; Reboud, J.P. !$#journal Eur. J. Biochem. (1996) 236:149-154 !$#title Photoaffinity labeling of elongation factor-2 with 8-azido !1derivatives of GTP and ATP. !$#cross-references MUID:96184892; PMID:8617259 !$#accession S62217 !'##status preliminary !'##molecule_type protein !'##residues 2-7;240-244;265-272 ##label GUI COMMENT Phosphorylation is regulatory and inactivates eEF-2. CLASSIFICATION #superfamily translation elongation factor 2; translation !1elongation factor Tu homology KEYWORDS diphthamide; GTP binding; nucleotide binding; P-loop; !1phosphoprotein; protein biosynthesis FEATURE !$2-858 #product translation elongation factor eEF-2 #status !8predicted #label MAT\ !$20-161 #domain translation elongation factor Tu homology !8#label ETU\ !$26-33 #region nucleotide-binding motif A (P-loop)\ !$158-161 #region GTP-binding NKXD motif\ !$57,59 #binding_site phosphate (Thr) (covalent) (by !8elongation factor 2 kinase) #status predicted\ !$715 #modified_site 2'-[3-carboxamido-3- !8(trimethylammonio)propyl]histidine (His) #status !8experimental SUMMARY #length 858 #molecular-weight 95283 #checksum 6241 SEQUENCE /// ENTRY S01289 #type complete TITLE translation elongation factor aEF-2 - Methanococcus vannielii ORGANISM #formal_name Methanococcus vannielii DATE 30-Sep-1989 #sequence_revision 15-Nov-1996 #text_change 19-Jan-2001 ACCESSIONS S01289 REFERENCE S01289 !$#authors Lechner, K.; Heller, G.; Boeck, A. !$#journal Nucleic Acids Res. (1988) 16:7817-7826 !$#title Gene for the diphtheria toxin-susceptible elongation factor !12 from Methanococcus vannielii. !$#cross-references MUID:88335529; PMID:3419900 !$#accession S01289 !'##molecule_type DNA !'##residues 1-727 ##label LEC !'##cross-references EMBL:X12384; NID:g44709; PIDN:CAA30941.1; !1PID:g44710 GENETICS !$#gene fus CLASSIFICATION #superfamily translation elongation factor 2; translation !1elongation factor Tu homology KEYWORDS diphthamide; GTP binding; nucleotide binding; P-loop; !1protein biosynthesis FEATURE !$22-151 #domain translation elongation factor Tu homology !8#label ETU\ !$28-35 #region nucleotide-binding motif A (P-loop)\ !$148-151 #region GTP-binding NKXD motif\ !$204-206 #region GTP-binding SAK/L motif #status atypical\ !$34,35,71,148,149, !$151,204 #binding_site Mg-GTP (Lys, Thr, Thr, Asn, Lys, Asp, !8Ser) #status predicted\ !$603 #modified_site 2'-[3-carboxamido-3- !8(trimethylammonio)propyl]histidine (His) #status !8predicted SUMMARY #length 727 #molecular-weight 80117 #checksum 5561 SEQUENCE /// ENTRY G64430 #type complete TITLE translation elongation factor aEF-2 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 13-Sep-1996 #sequence_revision 15-Nov-1996 #text_change 19-Jan-2001 ACCESSIONS G64430 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession G64430 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-726 ##label BUL !'##cross-references GB:U67547; GB:L77117; NID:g1591695; !1PIDN:AAB99052.1; PID:g1591702; TIGR:MJ1048 GENETICS !$#gene fus !$#map_position FOR983850-986030 CLASSIFICATION #superfamily translation elongation factor 2; translation !1elongation factor Tu homology KEYWORDS diphthamide; GTP binding; nucleotide binding; P-loop; !1protein biosynthesis FEATURE !$22-151 #domain translation elongation factor Tu homology !8#label ETU\ !$28-35 #region nucleotide-binding motif A (P-loop)\ !$148-151 #region GTP-binding NKXD motif\ !$602 #modified_site 2'-[3-carboxamido-3- !8(trimethylammonio)propyl]histidine (His) #status !8predicted SUMMARY #length 726 #molecular-weight 80988 #checksum 337 SEQUENCE /// ENTRY S23864 #type complete TITLE translation elongation factor aEF-2 - Pyrococcus woesei ORGANISM #formal_name Pyrococcus woesei DATE 28-May-1993 #sequence_revision 15-Nov-1996 #text_change 19-Jan-2001 ACCESSIONS S54741; S23864 REFERENCE S54740 !$#authors Creti, R.; Ceccarelli, E.; Bocchetta, M.; Sanangelantoni, !1A.M.; Tiboni, O.; Palm, P.; Cammarano, P. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1994) 91:3255-3259 !$#title Evolution of translational elongation factor (EF) sequences: !1reliability of global phylogenies inferred from EF-1-alpha !1(Tu) and EF-2(G) proteins. !$#cross-references MUID:94211842; PMID:8159735 !$#accession S54741 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-732 ##label CR2 !'##cross-references EMBL:X67205; NID:g45949; PIDN:CAA47641.1; !1PID:g45950 GENETICS !$#gene fus CLASSIFICATION #superfamily translation elongation factor 2; translation !1elongation factor Tu homology KEYWORDS diphthamide; GTP binding; nucleotide binding; P-loop; !1protein biosynthesis FEATURE !$22-151 #domain translation elongation factor Tu homology !8#label ETU\ !$28-35 #region nucleotide-binding motif A (P-loop)\ !$148-151 #region GTP-binding NKXD motif\ !$597 #modified_site 2'-[3-carboxamido-3- !8(trimethylammonio)propyl]histidine (His) #status !8predicted SUMMARY #length 732 #molecular-weight 82255 #checksum 6517 SEQUENCE /// ENTRY S07558 #type complete TITLE translation elongation factor aEF-2 - Halobacterium salinarum ORGANISM #formal_name Halobacterium salinarum DATE 22-Jan-1993 #sequence_revision 15-Nov-1996 #text_change 19-Jan-2001 ACCESSIONS S07558 REFERENCE S07086 !$#authors Itoh, T. !$#journal Eur. J. Biochem. (1989) 186:213-219 !$#title Sequence analysis of the peptide-elongation factor EF-2 !1gene, downstream from those of ribosomal proteins H-S12 and !1H-S7, from the archaebacterial extreme halophile, !1Halobacterium halobium. !$#cross-references MUID:90092102; PMID:2513185 !$#accession S07558 !'##molecule_type DNA !'##residues 1-728 ##label ITO !'##cross-references EMBL:X17148; NID:g43494; PIDN:CAA35029.1; !1PID:g43496 !'##note the source is designated as Halobacterium halobium GENETICS !$#gene fus CLASSIFICATION #superfamily translation elongation factor 2; translation !1elongation factor Tu homology KEYWORDS diphthamide; GTP binding; nucleotide binding; P-loop; !1protein biosynthesis FEATURE !$22-151 #domain translation elongation factor Tu homology !8#label ETU\ !$28-35 #region nucleotide-binding motif A (P-loop)\ !$148-151 #region GTP-binding NKXD motif\ !$205-207 #region GTP-binding SAK/L motif\ !$34,35,71,148,149, !$151,205 #binding_site Mg-GTP (Lys, Thr, Thr, Asn, Lys, Asp, !8Ser) #status predicted\ !$596 #modified_site 2'-[3-carboxamido-3- !8(trimethylammonio)propyl]histidine (His) #status !8predicted SUMMARY #length 728 #molecular-weight 80338 #checksum 5350 SEQUENCE /// ENTRY S36089 #type complete TITLE translation elongation factor aEF-2 - Thermoplasma acidophilum ORGANISM #formal_name Thermoplasma acidophilum DATE 31-Dec-1993 #sequence_revision 15-Nov-1996 #text_change 19-Jan-2001 ACCESSIONS S36089 REFERENCE S36089 !$#authors Pechmann, H.; Tesch, A.; Klink, F. !$#journal FEMS Microbiol. Lett. (1991) 79:51-56 !$#title Cloning and sequencing of the fus-gene encoding elongation !1factor 2 in the archaebacterium Thermoplasma acidophilum. !$#accession S36089 !'##molecule_type DNA !'##residues 1-732 ##label PEC !'##cross-references EMBL:X56840; NID:g48075; PIDN:CAA40171.1; !1PID:g48076 GENETICS !$#gene fus CLASSIFICATION #superfamily translation elongation factor 2; translation !1elongation factor Tu homology KEYWORDS diphthamide; GTP binding; nucleotide binding; P-loop; !1protein biosynthesis FEATURE !$22-151 #domain translation elongation factor Tu homology !8#label ETU\ !$28-35 #region nucleotide-binding motif A (P-loop)\ !$148-151 #region GTP-binding NKXD motif\ !$598 #modified_site 2'-[3-carboxamido-3- !8(trimethylammonio)propyl]histidine (His) #status !8predicted SUMMARY #length 732 #molecular-weight 81260 #checksum 8051 SEQUENCE /// ENTRY S14408 #type complete TITLE translation elongation factor aEF-2 - Sulfolobus acidocaldarius ORGANISM #formal_name Sulfolobus acidocaldarius DATE 28-May-1993 #sequence_revision 15-Nov-1996 #text_change 19-Jan-2001 ACCESSIONS S14408; S31657 REFERENCE S14408 !$#authors Schroeder, J.; Klink, F. !$#journal Eur. J. Biochem. (1991) 195:321-327 !$#title Gene for the ADP-ribosylatable elongation factor 2 from the !1extreme thermoacidophilic archaebacterium Sulfolobus !1acidocaldarius. Cloning, sequencing, comparative analysis. !$#cross-references MUID:91146567; PMID:1900048 !$#accession S14408 !'##molecule_type DNA !'##residues 1-737 ##label SCH1 !'##cross-references EMBL:X54972; NID:g46583; PIDN:CAA38716.1; !1PID:g581563 !$#accession S31657 !'##molecule_type protein !'##residues 2-14 ##label SCH2 GENETICS !$#gene fus !$#start_codon TTG CLASSIFICATION #superfamily translation elongation factor 2; translation !1elongation factor Tu homology KEYWORDS diphthamide; GTP binding; nucleotide binding; P-loop; !1protein biosynthesis FEATURE !$2-737 #product translation elongation factor 2 #status !8experimental #label MAT\ !$21-150 #domain translation elongation factor Tu homology !8#label ETU\ !$27-34 #region nucleotide-binding motif A (P-loop)\ !$147-150 #region GTP-binding NKXD motif\ !$203-205 #region GTP-binding SAK/L motif\ !$604 #modified_site 2'-[3-carboxamido-3- !8(trimethylammonio)propyl]histidine (His) #status !8predicted SUMMARY #length 737 #molecular-weight 81905 #checksum 1280 SEQUENCE /// ENTRY S31809 #type complete TITLE translation elongation factor aEF-2 - Sulfolobus solfataricus ORGANISM #formal_name Sulfolobus solfataricus DATE 13-Jan-1995 #sequence_revision 15-Nov-1996 #text_change 19-Jan-2001 ACCESSIONS S31809; S28936 REFERENCE S31809 !$#authors de Vendittis, E. !$#submission submitted to the EMBL Data Library, November 1992 !$#accession S31809 !'##molecule_type DNA !'##residues 1-736 ##label DEV !'##cross-references EMBL:X69297; NID:g47522; PIDN:CAA49157.1; !1PID:g809767 !'##experimental_source strain MT4; ATCC 49255 REFERENCE S28936 !$#authors Raimo, G.; Masullo, M.; Parente, A.; dello Russo, A.; !1Bocchini, V. !$#journal Biochim. Biophys. Acta (1992) 1132:127-132 !$#title Molecular, functional and structural properties of an !1archaebacterial elongation factor 2. !$#cross-references MUID:93003314; PMID:1390884 !$#accession S28936 !'##molecule_type protein !'##residues 2-23;590-602,'X',604 ##label RAI !'##experimental_source strain MT4; ATCC 49255 !'##note the residue designated 'X' was determined to be diphthamide GENETICS !$#gene EF-2 !$#start_codon TTG CLASSIFICATION #superfamily translation elongation factor 2; translation !1elongation factor Tu homology KEYWORDS diphthamide; GTP binding; nucleotide binding; P-loop; !1protein biosynthesis FEATURE !$21-150 #domain translation elongation factor Tu homology !8#label ETU\ !$27-34 #region nucleotide-binding motif A (P-loop)\ !$147-150 #region GTP-binding NKXD motif\ !$203-205 #region GTP-binding SAK/L motif\ !$603 #modified_site 2'-[3-carboxamido-3- !8(trimethylammonio)propyl]histidine (His) #status !8experimental SUMMARY #length 736 #molecular-weight 81820 #checksum 8031 SEQUENCE /// ENTRY S25166 #type complete TITLE translation elongation factor aEF-2 - Desulfurococcus mobilis ORGANISM #formal_name Desulfurococcus mobilis DATE 28-May-1993 #sequence_revision 15-Nov-1996 #text_change 19-Jan-2001 ACCESSIONS S54740; S25166 REFERENCE S54740 !$#authors Creti, R.; Ceccarelli, E.; Bocchetta, M.; Sanangelantoni, !1A.M.; Tiboni, O.; Palm, P.; Cammarano, P. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1994) 91:3255-3259 !$#title Evolution of translational elongation factor (EF) sequences: !1reliability of global phylogenies inferred from EF-1-alpha !1(Tu) and EF-2(G) proteins. !$#cross-references MUID:94211842; PMID:8159735 !$#accession S54740 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-734 ##label CRE !'##cross-references EMBL:X68014; NID:g40806; PIDN:CAA48150.1; !1PID:g40807 GENETICS !$#gene fus CLASSIFICATION #superfamily translation elongation factor 2; translation !1elongation factor Tu homology KEYWORDS diphthamide; GTP binding; nucleotide binding; P-loop; !1protein biosynthesis FEATURE !$21-150 #domain translation elongation factor Tu homology !8#label ETU\ !$27-34 #region nucleotide-binding motif A (P-loop)\ !$147-150 #region GTP-binding NKXD motif\ !$600 #modified_site 2'-[3-carboxamido-3- !8(trimethylammonio)propyl]histidine (His) #status !8predicted SUMMARY #length 734 #molecular-weight 82331 #checksum 9861 SEQUENCE /// ENTRY FIEC1 #type complete TITLE translation initiation factor IF-1 - Escherichia coli (strain K-12) ALTERNATE_NAMES translation initiation factor eIF-1 ORGANISM #formal_name Escherichia coli DATE 31-Jul-1979 #sequence_revision 30-Sep-1992 #text_change 01-Mar-2002 ACCESSIONS A27855; A41167; A03526; C36888; C64827 REFERENCE A27855 !$#authors Sands, J.F.; Cummings, H.S.; Sacerdot, C.; Dondon, L.; !1Grunberg-Manago, M.; Hershey, J.W.B. !$#journal Nucleic Acids Res. (1987) 15:5157-5168 !$#title Cloning and mapping of infA, the gene for protein synthesis !1initiation factor IF1. !$#cross-references MUID:87259992; PMID:3037488 !$#accession A27855 !'##molecule_type DNA !'##residues 1-72 ##label SAN !'##cross-references GB:Y00373; NID:g41807; PIDN:CAA68446.1; PID:g41808 REFERENCE PS0228 !$#authors Cummings, H.S.; Sands, J.F.; Foreman, P.C.; Fraser, J.; !1Hershey, J.W.B. !$#journal J. Biol. Chem. (1991) 266:16491-16498 !$#title Structure and expression of the infA operon encoding !1translational initiation factor IF1. Transcriptional control !1by growth rate. !$#cross-references MUID:91358434; PMID:1909328 !$#accession A41167 !'##molecule_type DNA !'##residues 1-72 ##label CUM !'##cross-references GB:M63145 REFERENCE A03526 !$#authors Pon, C.L.; Wittmann-Liebold, B.; Gualerzi, C. !$#journal FEBS Lett. (1979) 101:157-160 !$#title Structure-function relationships in Escherichia coli !1initiation factors. II. Elucidation of the primary structure !1of initiation factor IF-1. !$#cross-references MUID:79191815; PMID:376343 !$#accession A03526 !'##molecule_type protein !'##residues 2-72 ##label PON !'##note no specific function has so far been attributed to this !1initiation factor; however, it seems to stimulate more or !1less all the activities of the other two initiation factors, !1IF-2 and IF-3 REFERENCE A36888 !$#authors Shrader, T.E.; Tobias, J.W.; Varshavsky, A. !$#journal J. Bacteriol. (1993) 175:4364-4374 !$#title The N-end rule in Escherichia coli: cloning and analysis of !1the leucyl, phenylalanyl-tRNA-protein transferase gene aat. !$#cross-references MUID:93322314; PMID:8331068 !$#accession C36888 !'##molecule_type DNA !'##residues 1-72 ##label SHR !'##cross-references GB:L10383; NID:g145164; PIDN:AAA03232.1; !1PID:g145167 !'##experimental_source strain MC1061 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64827 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-72 ##label BLAT !'##cross-references GB:AE000190; GB:U00096; NID:g1787106; !1PIDN:AAC73970.1; PID:g1787110; UWGP:b0884 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene infA !$#map_position 20 min FUNCTION !$#pathway protein biosynthesis CLASSIFICATION #superfamily translation initiation factor IF-1 KEYWORDS protein biosynthesis FEATURE !$2-72 #product translation initiation factor IF-1 #status !8experimental #label MAT SUMMARY #length 72 #molecular-weight 8250 #checksum 7160 SEQUENCE /// ENTRY A05008 #type complete TITLE translation initiation factor IF-1 - liverwort (Marchantia polymorpha) chloroplast ORGANISM #formal_name chloroplast Marchantia polymorpha DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS A05008; S01562 REFERENCE A00150 !$#authors Ohyama, K. !$#submission submitted to the EMBL Data Library, October 1986 !$#accession A05008 !'##molecule_type DNA !'##residues 1-78 ##label OHY !'##cross-references EMBL:X04465; NID:g11640; PIDN:CAA28120.1; !1PID:g11709 REFERENCE A38014 !$#authors Ohyama, K.; Fukuzawa, H.; Kohchi, T.; Shirai, H.; Sano, T.; !1Sano, S.; Umesono, K.; Shiki, Y.; Takeuchi, M.; Chang, Z.; !1Aota, S.; Inokuchi, H.; Ozeki, H. !$#journal Nature (1986) 322:572-574 !$#title Chloroplast gene organization deduced from complete sequence !1of liverwort Marchantia polymorpha chloroplast DNA. !$#contents annotation; gene organization, sites, features REFERENCE S01529 !$#authors Fukuzawa, H.; Kohchi, T.; Sano, T.; Shirai, H.; Umesono, K.; !1Inokuchi, H.; Ozeki, H.; Ohyama, K. !$#journal J. Mol. Biol. (1988) 203:333-351 !$#title Structure and organization of Marchantia polymorpha !1chloroplast genome. III. Gene organization of the large !1single copy region from rbcL to trnI(CAU). !$#cross-references MUID:89068687; PMID:3199436 !$#accession S01562 !'##molecule_type DNA !'##residues 1-78 ##label FUK !'##cross-references EMBL:X04465; NID:g11640; PIDN:CAA28120.1; !1PID:g11709 GENETICS !$#gene infA !$#genome chloroplast CLASSIFICATION #superfamily translation initiation factor IF-1 KEYWORDS chloroplast; protein biosynthesis SUMMARY #length 78 #molecular-weight 8978 #checksum 5659 SEQUENCE /// ENTRY FIRZ1 #type complete TITLE translation initiation factor IF-1 - rice chloroplast ORGANISM #formal_name chloroplast Oryza sativa #common_name rice DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS JQ0261; S05141 REFERENCE JQ0200 !$#authors Shimada, H.; Whittier, R.F.; Hiratsuka, J.; Maeda, Y.; !1Hirai, A.; Sugiura, M. !$#submission submitted to JIPID, December 1989 !$#accession JQ0261 !'##molecule_type DNA !'##residues 1-107 ##label SHI !'##experimental_source cv. Nihonbare REFERENCE S05080 !$#authors Hiratsuka, J.; Shimada, H.; Whittier, R.; Ishibashi, T.; !1Sakamoto, M.; Mori, M.; Kondo, C.; Honji, Y.; Sun, C.R.; !1Meng, B.Y.; Li, Y.Q.; Kanno, A.; Nishizawa, Y.; Hirai, A.; !1Shinozaki, K.; Sugiura, M. !$#journal Mol. Gen. Genet. (1989) 217:185-194 !$#title The complete sequence of the rice (Oryza sativa) chloroplast !1genome: intermolecular recombination between distinct tRNA !1genes accounts for a major plastid DNA inversion during the !1evolution of the cereals. !$#cross-references MUID:89364698; PMID:2770692 !$#accession S05141 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-107 ##label HIR !'##cross-references EMBL:X15901; NID:g11957; PIDN:CAA33930.1; !1PID:g12021 !'##experimental_source cv. Nihonbare GENETICS !$#gene infA !$#map_position CP76561-76238 !$#genome chloroplast CLASSIFICATION #superfamily translation initiation factor IF-1 KEYWORDS chloroplast; protein biosynthesis SUMMARY #length 107 #molecular-weight 12417 #checksum 3707 SEQUENCE /// ENTRY A53048 #type complete TITLE translation initiation factor eIF-2 gamma chain [validated] - human ORGANISM #formal_name Homo sapiens #common_name man DATE 26-Aug-1999 #sequence_revision 26-Aug-1999 #text_change 19-Jan-2001 ACCESSIONS A53048 REFERENCE A53048 !$#authors Gaspar, N.J.; Kinzy, T.G.; Scherer, B.J.; Huembelin, M.; !1Hershey, J.W.B.; Merrick, W.C. !$#journal J. Biol. Chem. (1994) 269:3415-3422 !$#title Translation initiation factor eIF-2. Cloning and expression !1of the human cDNA encoding the gamma-subunit. !$#cross-references MUID:94148837; PMID:8106381 !$#accession A53048 !'##molecule_type mRNA !'##residues 1-472 ##label GAS !'##cross-references GB:L19161; NID:g306899; PIDN:AAA19696.1; !1PID:g306900 GENETICS !$#gene GDB:EIF2G !'##cross-references GDB:306330 !$#map_position 3q27-3q27 COMPLEX heterotrimer [validated, MUID:94148837] FUNCTION !$#description involved in the recruitment of methionyl-tRNAs to the 40S !1ribosomal subunit [validated, MUID:94148837] CLASSIFICATION #superfamily translation initiation factor eIF-2 gamma !1chain; translation elongation factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop; protein !1biosynthesis FEATURE !$42-193 #domain translation elongation factor Tu homology !8#label ETU\ !$48-55 #region nucleotide-binding motif A (P-loop)\ !$190-193 #region GTP-binding NKXD motif SUMMARY #length 472 #molecular-weight 51109 #checksum 4430 SEQUENCE /// ENTRY S46941 #type complete TITLE translation initiation factor eIF-2 gamma chain - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 26-Aug-1999 #sequence_revision 26-Aug-1999 #text_change 19-Jan-2001 ACCESSIONS S47005; S46941 REFERENCE S47004 !$#authors Tschiersch, B.; Hofmann, A.; Krauss, V.; Dorn, R.; Korge, !1G.; Reuter, G. !$#journal EMBO J. (1994) 13:3822-3831 !$#title The protein encoded by the Drosophila position-effect !1variegation suppressor gene Su(var)3-9 combines domains of !1antagonistic regulators of homeotic gene complexes. !$#cross-references MUID:94349930; PMID:7915232 !$#accession S47005 !'##molecule_type mRNA !'##residues 1-475 ##label TS2 !'##cross-references EMBL:X80069; NID:g516305; PIDN:CAA56375.1; !1PID:g516306 !'##note submitted to the EMBL Data Library, July 1994 GENETICS !$#gene FlyBase:Su(var)3-9 !'##cross-references FlyBase:FBgn0003600 CLASSIFICATION #superfamily translation initiation factor eIF-2 gamma !1chain; translation elongation factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop; protein !1biosynthesis FEATURE !$41-192 #domain translation elongation factor Tu homology !8#label ETU\ !$47-54 #region nucleotide-binding motif A (P-loop)\ !$189-192 #region GTP-binding NKXD motif SUMMARY #length 475 #molecular-weight 51484 #checksum 9985 SEQUENCE /// ENTRY A48117 #type complete TITLE translation initiation factor eIF-2 gamma chain - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YER025w ORGANISM #formal_name Saccharomyces cerevisiae DATE 26-Aug-1999 #sequence_revision 26-Aug-1999 #text_change 19-Jan-2001 ACCESSIONS A48117; S50483 REFERENCE A48117 !$#authors Hannig, E.M.; Cigan, A.M.; Freeman, B.A.; Kinzy, T.G. !$#journal Mol. Cell. Biol. (1993) 13:506-520 !$#title GCD11, a negative regulator of GCN4 expression, encodes the !1gamma subunit of eIF-2 in Saccharomyces cerevisiae. !$#cross-references MUID:93109337; PMID:8417348 !$#accession A48117 !'##molecule_type DNA !'##residues 1-527 ##label HAN !'##cross-references EMBL:L04268; NID:g171570; PIDN:AAA34633.1; !1PID:g171571 !'##note sequence extracted from NCBI backbone (NCBIN:121264, !1NCBIP:121266) REFERENCE S50459 !$#authors Dietrich, F.S. !$#submission submitted to the EMBL Data Library, December 1994 !$#description The sequence of S. cerevisiae cosmids 9537, 9581, 9495, !19867, and lambda clone 5898. !$#accession S50483 !'##molecule_type DNA !'##residues 1-527 ##label DIE !'##cross-references EMBL:U18778; NID:g603592; PID:g603617; !1GSPDB:GN00005; MIPS:YER025w GENETICS !$#gene SGD:GCD11; MIPS:YER025w !'##cross-references SGD:S0000827; MIPS:YER025w !$#map_position 5R CLASSIFICATION #superfamily translation initiation factor eIF-2 gamma !1chain; translation elongation factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop; protein !1biosynthesis FEATURE !$101-252 #domain translation elongation factor Tu homology !8#label ETU\ !$107-114 #region nucleotide-binding motif A (P-loop)\ !$249-252 #region GTP-binding NKXD motif\ !$258-260 #region GTP-binding SAK/L motif SUMMARY #length 527 #molecular-weight 57865 #checksum 8554 SEQUENCE /// ENTRY T00956 #type complete TITLE translation initiation factor eIF-2 gamma chain F20D22.6 - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 26-Aug-1999 #sequence_revision 26-Aug-1999 #text_change 19-Jan-2001 ACCESSIONS T00956 REFERENCE Z14214 !$#authors Vysotskaia, V.S.; Osborne, B.I.; Schwartz, J.R.; Toriumi, !1M.; Kwan, A.; Yu, G.; Oji, O.; Liu, S.; Li, J.; Hoang, L.; !1Araujo, R.; Au, M.; Brendel, V.; Buehler, E.; Conway, A.B.; !1Conway, A.R.; Dewar, K.; Feng, J.; Kim, C.; Kurtz, D.; Li, !1Y.; Palm, C.J.; Shinn, P.; Sun, H.; Davis, R.W.; Ecker, !1J.R.; Federspiel, N.A.; Theologis, A. !$#submission submitted to the EMBL Data Library, May 1998 !$#description Arabidopsis thaliana chromosome 1 BAC F20D22 complete !1sequence. !$#accession T00956 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-465 ##label VYS !'##cross-references EMBL:AC002411; NID:g2570223; PID:g3142294 GENETICS !$#map_position 1 !$#introns 37/1; 57/3; 95/2; 129/3; 205/3; 278/3; 365/3 !$#note F20D22.6 CLASSIFICATION #superfamily translation initiation factor eIF-2 gamma !1chain; translation elongation factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop; protein !1biosynthesis FEATURE !$34-186 #domain translation elongation factor Tu homology !8#label ETU\ !$40-47 #region nucleotide-binding motif A (P-loop)\ !$183-186 #region GTP-binding NKXD motif SUMMARY #length 465 #molecular-weight 50853 #checksum 2014 SEQUENCE /// ENTRY T04935 #type complete TITLE translation initiation factor eIF-2 gamma chain T9A21.180 - Arabidopsis thaliana ALTERNATE_NAMES protein T9A21.180 ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 26-Aug-1999 #sequence_revision 26-Aug-1999 #text_change 19-Jan-2001 ACCESSIONS T04935 REFERENCE Z15390 !$#authors Bevan, M.; Murphy, G.; Ridley, P.; Hudson, S.; Bancroft, I.; !1Mewes, H.W.; Mayer, K.F.X.; Schueller, C. !$#submission submitted to the Protein Sequence Database, February 1999 !$#accession T04935 !'##molecule_type DNA !'##residues 1-471 ##label BEV !'##cross-references EMBL:AL021713 !'##experimental_source cultivar Columbia; BAC clone T9A21 GENETICS !$#map_position 4 !$#introns 43/1; 101/2; 135/3; 211/3; 276/1 !$#note T9A21.180 CLASSIFICATION #superfamily translation initiation factor eIF-2 gamma !1chain; translation elongation factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop; protein !1biosynthesis FEATURE !$40-192 #domain translation elongation factor Tu homology !8#label ETU\ !$46-53 #region nucleotide-binding motif A (P-loop)\ !$189-192 #region GTP-binding NKXD motif SUMMARY #length 471 #molecular-weight 51679 #checksum 5799 SEQUENCE /// ENTRY E71178 #type complete TITLE translation initiation factor aIF-2 gamma chain - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 26-Aug-1999 #sequence_revision 26-Aug-1999 #text_change 19-Jan-2001 ACCESSIONS E71178 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession E71178 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-411 ##label KAW !'##cross-references GB:AP000007; NID:g3236134; PIDN:BAA30820.1; !1PID:g3258137 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1706 CLASSIFICATION #superfamily translation initiation factor eIF-2 gamma !1chain; translation elongation factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop; protein !1biosynthesis FEATURE !$12-149 #domain translation elongation factor Tu homology !8#label ETU\ !$18-25 #region nucleotide-binding motif A (P-loop) SUMMARY #length 411 #molecular-weight 45099 #checksum 4014 SEQUENCE /// ENTRY H69132 #type complete TITLE translation initiation factor aIF-2 gamma chain - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 26-Aug-1999 #sequence_revision 26-Aug-1999 #text_change 19-Jan-2001 ACCESSIONS H69132 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession H69132 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-408 ##label MTH !'##cross-references GB:AE000812; GB:AE000666; NID:g2621298; !1PIDN:AAB84767.1; PID:g2621311 !'##experimental_source strain Delta H GENETICS !$#gene MTH261 !$#start_codon GTG CLASSIFICATION #superfamily translation initiation factor eIF-2 gamma !1chain; translation elongation factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop; protein !1biosynthesis FEATURE !$7-147 #domain translation elongation factor Tu homology !8#label ETU\ !$13-20 #region nucleotide-binding motif A (P-loop)\ !$144-147 #region GTP-binding NKXD motif SUMMARY #length 408 #molecular-weight 43897 #checksum 8862 SEQUENCE /// ENTRY D64457 #type complete TITLE translation initiation factor aIF-2 gamma chain - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 26-Aug-1999 #sequence_revision 26-Aug-1999 #text_change 19-Jan-2001 ACCESSIONS D64457 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession D64457 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-437 ##label BUL !'##cross-references GB:U67566; GB:L77117; NID:g1591887; !1PIDN:AAB99264.1; PID:g1591895; TIGR:MJ1261 GENETICS !$#map_position FOR1202889-1204202 CLASSIFICATION #superfamily translation initiation factor eIF-2 gamma !1chain; translation elongation factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop; protein !1biosynthesis FEATURE !$38-175 #domain translation elongation factor Tu homology !8#label ETU\ !$44-51 #region nucleotide-binding motif A (P-loop)\ !$172-175 #region GTP-binding NKXD motif SUMMARY #length 437 #molecular-weight 47745 #checksum 1295 SEQUENCE /// ENTRY H69323 #type complete TITLE translation initiation factor aIF-2 gamma chain - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 26-Aug-1999 #sequence_revision 26-Aug-1999 #text_change 19-Jan-2001 ACCESSIONS H69323 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession H69323 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-424 ##label KLE !'##cross-references GB:AE001064; GB:AE000782; NID:g2689387; !1PIDN:AAB90649.1; PID:g2650032; TIGR:AF0592 CLASSIFICATION #superfamily translation initiation factor eIF-2 gamma !1chain; translation elongation factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop; protein !1biosynthesis FEATURE !$26-166 #domain translation elongation factor Tu homology !8#label ETU\ !$32-39 #region nucleotide-binding motif A (P-loop)\ !$163-166 #region GTP-binding NKXD motif SUMMARY #length 424 #molecular-weight 46270 #checksum 5271 SEQUENCE /// ENTRY FIEC3 #type complete TITLE translation initiation factor IF-3 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-May-1979 #sequence_revision 25-Feb-1985 #text_change 01-Mar-2002 ACCESSIONS S13748; A03527; I41281; F64930 REFERENCE S13748 !$#authors Sacerdot, C.; Fayat, G.; Dessen, P.; Springer, M.; !1Plumbridge, J.A.; Grunberg-Manago, M.; Blanquet, S. !$#journal EMBO J. (1982) 1:311-315 !$#title Sequence of a 1.26-kb DNA fragment containing the structural !1gene for E.coli initiation factor IF3: presence of an AUU !1initiator codon. !$#cross-references MUID:84182476; PMID:6325158 !$#accession S13748 !'##molecule_type DNA !'##residues 1-180 ##label SAC !'##cross-references EMBL:V00291; NID:g43065; PIDN:CAA23561.1; !1PID:g43067 REFERENCE A03527 !$#authors Brauer, D.; Wittmann-Liebold, B. !$#journal FEBS Lett. (1977) 79:269-275 !$#title The primary structure of the initiation factor IF-3 from !1Escherichia coli. !$#cross-references MUID:77246715; PMID:330233 !$#accession A03527 !'##molecule_type protein !'##residues 1-21,'E',23-33,'I',35,'MV',37-46,'Q',48-51,'N',53-60,'Q', !162-86,'E',88-89,'K',90-102,'N',104,'N',106-177,'Q',179 !1##label BRA REFERENCE I41281 !$#authors Miller, H.I. !$#journal Cold Spring Harb. Symp. Quant. Biol. (1984) 49:691-698 !$#title Primary structure of the himA gene of Escherichia coli: !1homology with DNA-binding protein HU and association with !1the phenylalanyl-tRNA synthetase operon. !$#cross-references MUID:85153048; PMID:6397321 !$#accession I41281 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-160,'S',162-180 ##label RES !'##cross-references GB:K02844; NID:g146342; PIDN:AAA51467.1; !1PID:g290449 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64930 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-180 ##label BLAT !'##cross-references GB:AE000267; GB:U00096; NID:g1788011; !1PIDN:AAC74788.1; PID:g1788012; UWGP:b1718 !'##experimental_source strain K-12, substrain MG1655 COMMENT IF-3 exists in two main forms: IF-3L, consisting of 180 !1residues, and IF-3S, which differs in lacking residues 1-6. !1There is at least one minor form that differs from IF-3L !1only in the absence of the first residue. GENETICS !$#gene infC !$#map_position 38 min !$#start_codon ATT FUNCTION !$#description one of the essential components for the initiation of !1protein synthesis in vitro; it may be involved in the !1specific recognition of the initiation regions of mRNAs CLASSIFICATION #superfamily translation initiation factor IF-3 KEYWORDS methylated amino end; protein biosynthesis FEATURE !$1-180 #product translation initiation factor IF-3 #status !8experimental #label MAT\ !$1 #modified_site methylated amino end (Met) #status !8experimental SUMMARY #length 180 #molecular-weight 20564 #checksum 9871 SEQUENCE /// ENTRY I40072 #type complete TITLE translation initiation factor IF-3 - Buchnera aphidicola ALTERNATE_NAMES integration host factor 3 [misidentification] ORGANISM #formal_name Buchnera aphidicola DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 04-Feb-2000 ACCESSIONS I40072 REFERENCE I40070 !$#authors Munson, M.A.; Baumann, L.; Baumann, P. !$#journal Curr. Microbiol. (1992) 24:23-29 !$#title Buchnera aphidicola, the endosymbiont of aphids, contains !1genes for four ribosomal RNA proteins, initiation factor-3, !1and the alpha subunit of RNA polymerase. !$#accession I40072 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-178 ##label RES !'##cross-references EMBL:U11066; NID:g868025; PIDN:AAC43606.1; !1PID:g868028 GENETICS !$#gene infC !$#start_codon ATT CLASSIFICATION #superfamily translation initiation factor IF-3 SUMMARY #length 178 #molecular-weight 20601 #checksum 9047 SEQUENCE /// ENTRY B64116 #type complete TITLE translation initiation factor IF-3 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B64116 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession B64116 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-135 ##label TIGR !'##cross-references GB:U32811; GB:L42023; NID:g1574774; !1PIDN:AAC22963.1; PID:g1574778; TIGR:HI1318 CLASSIFICATION #superfamily translation initiation factor IF-3 KEYWORDS protein biosynthesis SUMMARY #length 135 #molecular-weight 15356 #checksum 9301 SEQUENCE /// ENTRY FIBS3F #type complete TITLE translation initiation factor IF-3 - Bacillus stearothermophilus ORGANISM #formal_name Bacillus stearothermophilus DATE 03-Aug-1984 #sequence_revision 12-Apr-1996 #text_change 16-Jun-2000 ACCESSIONS S05346; A03528 REFERENCE S05346 !$#authors Pon, C.L.; Brombach, M.; Thamm, S.; Gualerzi, C.O. !$#journal Mol. Gen. Genet. (1989) 218:355-357 !$#title Cloning and characterization of a gene cluster from Bacillus !1stearothermophilus comprising infC, rpmI and rplT. !$#cross-references MUID:89384464; PMID:2779520 !$#accession S05346 !'##molecule_type DNA !'##residues 1-172 ##label PON !'##cross-references EMBL:X16188; NID:g39960; PIDN:CAA34312.1; !1PID:g580890 REFERENCE A03528 !$#authors Kimura, M.; Ernst, H.; Appelt, K. !$#journal FEBS Lett. (1983) 160:78-81 !$#title The primary structure of initiation factor IF3 from Bacillus !1stearothermophilus. !$#cross-references MUID:83287778; PMID:6884517 !$#contents NCA 1503 !$#accession A03528 !'##molecule_type protein !'##residues 2-172 ##label KIM GENETICS !$#gene infC !$#start_codon ATT CLASSIFICATION #superfamily translation initiation factor IF-3 KEYWORDS protein biosynthesis FEATURE !$2-172 #product translation initiation factor IF-3 #status !8experimental #label MAT SUMMARY #length 172 #molecular-weight 19809 #checksum 2764 SEQUENCE /// ENTRY A53379 #type complete TITLE translation initiation factor IF-3 homolog - Myxococcus xanthus ORGANISM #formal_name Myxococcus xanthus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A53379 REFERENCE A53379 !$#authors Cheng, Y.L.; Kalman, L.V.; Kaiser, D. !$#journal J. Bacteriol. (1994) 176:1427-1433 !$#title The dsg gene of Myxococcus xanthus encodes a protein similar !1to translation initiation factor IF3. !$#cross-references MUID:94156849; PMID:8113184 !$#accession A53379 !'##status preliminary !'##molecule_type DNA !'##residues 1-247 ##label CHE !'##cross-references GB:U04438; NID:g436164; PIDN:AAC13748.1; !1PID:g436165 GENETICS !$#start_codon ATC CLASSIFICATION #superfamily translation initiation factor IF-3 SUMMARY #length 247 #molecular-weight 27145 #checksum 905 SEQUENCE /// ENTRY S74739 #type complete TITLE translation initiation factor IF-3 - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein slr0974 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S74739 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74739 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-177 ##label KAN !'##cross-references EMBL:D90901; GB:AB001339; NID:g1651897; !1PIDN:BAA16890.1; PID:g1651964 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene infC !$#start_codon GTG CLASSIFICATION #superfamily translation initiation factor IF-3 KEYWORDS protein biosynthesis SUMMARY #length 177 #molecular-weight 20560 #checksum 4059 SEQUENCE /// ENTRY S73152 #type complete TITLE translation initiation factor IF-3 - red alga (Porphyra purpurea) chloroplast ORGANISM #formal_name chloroplast Porphyra purpurea DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S73152 REFERENCE S73108 !$#authors Reith, M.; Munholland, J. !$#journal Plant Mol. Biol. Rep. (1995) 13:333-335 !$#title Complete nucleotide sequence of the Porphyra purpurea !1chloroplast genome. !$#accession S73152 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-182 ##label REI !'##cross-references EMBL:U38804; NID:g1276652; PIDN:AAC08117.1; !1PID:g1276697 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1995 GENETICS !$#gene infC !$#genome chloroplast !$#start_codon GTG CLASSIFICATION #superfamily translation initiation factor IF-3 KEYWORDS chloroplast; protein biosynthesis SUMMARY #length 182 #molecular-weight 20862 #checksum 9680 SEQUENCE /// ENTRY FIMS4A #type complete TITLE translation initiation factor eIF-4A I - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Mar-1988 #sequence_revision 09-Apr-1998 #text_change 19-Jan-2001 ACCESSIONS JS0039; A24267; B24267; S00986; A58767 REFERENCE JS0039 !$#authors Reddy, N.S.; Roth, W.W.; Bragg, P.W.; Wahba, A.J. !$#journal Gene (1988) 70:231-243 !$#title Isolation and mapping of a gene for protein synthesis !1initiation factor 4A and its expression during !1differentiation of murine erythroleukemia cells. !$#cross-references MUID:89108007; PMID:3215517 !$#accession JS0039 !'##molecule_type DNA !'##residues 1-299,'C',301-406 ##label RED !'##cross-references GB:L36611; NID:g556306; PIDN:AAA50407.1; !1PID:g556308 !'##note the authors translated the codon GAG for residue 143 as Gly !'##note the codon given for 300-Ser (TGT) is inconsistent with the !1authors' translation REFERENCE A24267 !$#authors Nielsen, P.J.; McMaster, G.K.; Trachsel, H. !$#journal Nucleic Acids Res. (1985) 13:6867-6880 !$#title Cloning of eukaryotic protein synthesis initiation factor !1genes: isolation and characterization of cDNA clones !1encoding factor eIF-4A. !$#cross-references MUID:86041884; PMID:3840589 !$#accession A24267 !'##molecule_type mRNA !'##residues 17-406 ##label NIE !'##cross-references GB:X03039; NID:g50812; PIDN:CAA26842.1; PID:g50814; !1GB:X03040; NID:g50817; PID:g50819 !$#accession B24267 !'##molecule_type mRNA !'##residues 37-406 ##label NIE2 !'##cross-references GB:X03039; NID:g50812; PIDN:CAA26843.1; PID:g50815; !1GB:X03040; NID:g50817; PID:g50820 REFERENCE S00985 !$#authors Nielsen, P.J.; Trachsel, H. !$#journal EMBO J. (1988) 7:2097-2105 !$#title The mouse protein synthesis initiation factor 4A gene family !1includes two related functional genes which are !1differentially expressed. !$#cross-references MUID:88328998; PMID:3046931 !$#accession S00986 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 'M',1-154,'VI',157-406 ##label NIE3 !'##cross-references EMBL:X14421; NID:g50810 !$#accession A58767 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-8 ##label NIE4 !'##cross-references EMBL:X14421; NID:g50810; PIDN:CAA32584.1; !1PID:g581984 COMMENT This is one of the many factors involved in the complex !1assembly process of eukaryotic protein synthesis initiation. !1It is required for mRNA binding to ribosomes and is also a !1component of a protein complex involved in "cap" !1recognition. GENETICS !$#gene MGI:Eif4a1 !'##cross-references MGI:95303 !$#map_position 11:39.0 !$#introns 8/2; 24/3; 68/3; 115/3; 172/1; 208/3; 256/3; 302/3; 332/3; !1359/2 CLASSIFICATION #superfamily translation initiation factor eIF-4A KEYWORDS ATP; nucleotide binding; P-loop; protein biosynthesis; RNA !1binding FEATURE !$76-83 #region nucleotide-binding motif A (P-loop)\ !$178-183 #region nucleotide-binding motif B\ !$182-185 #region DEAD motif\ !$82 #binding_site ATP (Lys) #status predicted SUMMARY #length 406 #molecular-weight 46154 #checksum 7570 SEQUENCE /// ENTRY FIBY1 #type complete TITLE translation initiation factor eIF-4A - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES DNA polymerase epsilon stimulatory factor I chain p37; protein J0660; protein YJL138c; protein YKR059w ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 17-Nov-2000 ACCESSIONS S05835; S07609; S38135; S55175; S36855; S17006; S56920; !1S41073; S71659; A32752 REFERENCE S05835 !$#authors Linder, P.; Slonimski, P.P. !$#journal Nucleic Acids Res. (1988) 16:10359 !$#title Sequence of the genes TIF1 and TIF2 from Saccharomyces !1cerevisiae coding for a translation initiation factor. !$#cross-references MUID:89057473; PMID:3057442 !$#accession S05835 !'##molecule_type DNA !'##residues 1-395 ##label LIN !'##cross-references EMBL:X12813; NID:g4620; PIDN:CAA31301.1; PID:g4621 !'##genetics TIF1 !$#accession S07609 !'##molecule_type DNA !'##residues 1-395 ##label LIW !'##cross-references EMBL:X12814; NID:g4622; PIDN:CAA31302.1; PID:g4623 !'##genetics TIF2 REFERENCE S38130 !$#authors van Vliet-Reedijk, J.C.; Planta, R.J. !$#submission submitted to the Protein Sequence Database, March 1994 !$#accession S38135 !'##molecule_type DNA !'##residues 1-395 ##label VAN !'##cross-references EMBL:Z28284; GSPDB:GN00011; MIPS:YKR059w; !1NID:g486520; PIDN:CAA82138.1; PID:g486521 !'##genetics TIF1 REFERENCE S55159 !$#authors Katsoulou, C.; Tzermia, M.; Alexandraki, D. !$#submission submitted to the EMBL Data Library, May 1995 !$#description The complete sequence of a 40.7 kb segment located on the !1left arm of yeast chromosome X identified 13 known genes and !1revealed 13 new open reading frames including homologues to !1other yeast hypothetical proteins. !$#accession S55175 !'##molecule_type DNA !'##residues 1-395 ##label KAT !'##cross-references EMBL:X87371; NID:g854542; PIDN:CAA60817.1; !1PID:g854559 !'##genetics TIF2 REFERENCE S36855 !$#authors Foreman, P.K.; Davis, R.W.; Sachs, A.B. !$#journal Nucleic Acids Res. (1991) 19:2781 !$#title The Saccharomyces cerevisiae RPB4 gene is tightly linked to !1the TIF2 gene. !$#cross-references MUID:91252230; PMID:2041753 !$#accession S36855 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 307-395 ##label FOR !'##cross-references EMBL:X58099; NID:g4831; PIDN:CAA41110.1; PID:g4832 !'##genetics TIF2 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1March 1991 REFERENCE S17006 !$#authors Foreman, P.K.; Davis, R.W.; Sachs, A.B. !$#submission submitted to the EMBL Data Library, March 1991 !$#description The Saccharomyces cerevisiae RPB4 gene is tightly linked to !1the TIF2 gene. !$#accession S17006 !'##molecule_type DNA !'##residues 307-395 ##label FO2 !'##cross-references EMBL:X58099; NID:g4831; PIDN:CAA41110.1; PID:g4832 !'##genetics TIF2 REFERENCE S56912 !$#authors Katsoulou, C.; Tzermia, M.; Alexandraki, D. !$#submission submitted to the Protein Sequence Database, September 1995 !$#accession S56920 !'##molecule_type DNA !'##residues 1-395 ##label KAW !'##cross-references EMBL:Z49413; GSPDB:GN00010; MIPS:YJL138c; !1NID:g1015543; PIDN:CAA89433.1; PID:g1015544 !'##genetics TIF2 REFERENCE S41073 !$#authors Smiley, J.K.; Brown, W.C.; Campbell, J.L. !$#journal Nucleic Acids Res. (1992) 20:4913-4918 !$#title The 66 kDa component of yeast SFI, stimulatory factor I, is !1hsp60. !$#cross-references MUID:93027213; PMID:1408806 !$#accession S41073 !'##molecule_type protein !'##residues 378-384,'A',386-391;342-347,'N';332-340 ##label SMI !'##note 386-Gly, 387-His, 390-Cys, and 348-Ala were also found REFERENCE S71643 !$#authors Katsoulou, C.; Tzermia, M.; Tavernarakis, N.; Alexandraki, !1D. !$#journal Yeast (1996) 12:787-797 !$#title Sequence analysis of a 40.7 kb segment from the left arm of !1yeast chromosome X reveals 14 known genes and 13 new open !1reading frames including homologues of genes clustered on !1the right arm of chromosome XI. !$#cross-references MUID:96408771; PMID:8813765 !$#accession S71659 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-395 ##label KAF !'##cross-references EMBL:X87371; NID:g854542; PIDN:CAA60817.1; !1PID:g854559 !'##genetics TIF2 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1May 1995 GENETICS TIF1 !$#gene SGD:TIF1; MIPS:YKR059w !'##cross-references MIPS:YKR059w; SGD:S0001767 !$#map_position 11R GENETICS TIF2 !$#gene SGD:TIF2; MIPS:YJL138c !'##cross-references MIPS:YJL138c; SGD:S0003674 !$#map_position 10L FUNCTION !$#description protein biosynthesis CLASSIFICATION #superfamily translation initiation factor eIF-4A KEYWORDS ATP; DEAD box; P-loop; protein biosynthesis; purine !1nucleotide binding; RNA binding FEATURE !$66-73 #region nucleotide-binding motif A (P-loop)\ !$166-171 #region nucleotide-binding motif B\ !$170-173 #region DEAD motif\ !$72 #binding_site ATP (Lys) #status predicted SUMMARY #length 395 #molecular-weight 44697 #checksum 5551 SEQUENCE /// ENTRY S71745 #type complete TITLE translation initiation factor eIF-4A [similarity] - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES cell cycle control protein eIF-4A ORGANISM #formal_name Schizosaccharomyces pombe DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S71745; T46563; T50455 REFERENCE S71745 !$#authors Fischli, A.; Schmid, S.R.; Coppolecchia, R.; Linder, P. !$#journal Yeast (1996) 12:977-981 !$#title The translation initiation factor eIF4A from !1Schizosaccharomyces pombe is closely related to its !1mammalian counterpart. !$#cross-references MUID:97027307; PMID:8873451 !$#accession S71745 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-392 ##label FIS !'##cross-references EMBL:X80796; NID:g1321960; PIDN:CAA56772.1; !1PID:g1321961 REFERENCE Z23069 !$#authors Daga, R.; Jimenez, J. !$#submission submitted to the EMBL Data Library, March 1995 !$#description Co-ordination of the cell cycle and the translation !1machinery in fission yeast: A molecular mechanism for the !1control of the cell cycle. !$#accession T46563 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-392 ##label DAG !'##cross-references EMBL:L40627; PIDN:AAB61679.1 !'##experimental_source strain 972h(-) REFERENCE Z25030 !$#authors McDougall, R.C.; Rajandream, M.A.; Barrell, B.G.; Simmonds, !1M.; Churcher, C.M. !$#submission submitted to the EMBL Data Library, November 1999 !$#accession T50455 !'##molecule_type DNA !'##residues 1-392 ##label MCD !'##cross-references EMBL:AL132828; PIDN:CAB60237.1; GSPDB:GN00066; !1SPDB:SPAC1006.07 !'##experimental_source strain 972h(-); cosmid c1006 GENETICS !$#gene tif1; SPDB:SPAC1006.07 !$#map_position 1 CLASSIFICATION #superfamily translation initiation factor eIF-4A KEYWORDS ATP; DEAD box; nucleotide binding; P-loop; protein !1biosynthesis; RNA binding FEATURE !$63-70 #region nucleotide-binding motif A (P-loop)\ !$164-169 #region nucleotide-binding motif B\ !$168-171 #region DEAD motif\ !$69 #binding_site ATP (Lys) #status predicted SUMMARY #length 392 #molecular-weight 44436 #checksum 5652 SEQUENCE /// ENTRY I37201 #type complete TITLE nuclear RNA helicase (DEAD family) BAT1 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS I37201 REFERENCE I37200 !$#authors Peelman, L.; Chardon, P.; Nunes, M.; Renard, C.; Geffrotin, !1C.; Vaiman, M.; Van Zeveren, A.; Coppieters, W.; Van de !1Weghe, A.; Bouquet, Y.; Choy, W.; Strominger, J.; Spies, T. !$#journal Genomics (1995) 26:210-218 !$#title The BAT1 gene in the MHC encodes an evolutionarily conserved !1putative nuclear RNA helicase of the DEAD family. !$#cross-references MUID:95324911; PMID:7601445 !$#accession I37201 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-428 ##label RES !'##cross-references EMBL:Z37166; NID:g587145; PIDN:CAA85523.1; !1PID:g587146 GENETICS !$#gene GDB:D6S81E; BAT1 !'##cross-references GDB:124608; OMIM:142560 !$#map_position 6pter-6qter CLASSIFICATION #superfamily translation initiation factor eIF-4A KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$89-96 #region nucleotide-binding motif A (P-loop)\ !$192-197 #region nucleotide-binding motif B\ !$196-199 #region DEAD motif SUMMARY #length 428 #molecular-weight 48991 #checksum 1258 SEQUENCE /// ENTRY S51601 #type complete TITLE DEAD-box RNA helicase WM6 - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S51601; S47176 REFERENCE S51601 !$#authors Warbrick, E.; Glover, D. !$#journal Mol. Gen. Genet. (1994) 245:654-657 !$#title A Drosophila gene encoding a DEAD box RNA helicase can !1suppress loss of wee1/mik1 function in Schizosaccharomyces !1pombe. !$#cross-references MUID:95107265; PMID:7808417 !$#accession S51601 !'##molecule_type mRNA !'##residues 1-424 ##label WAR !'##cross-references EMBL:X79802; NID:g505582; PIDN:CAA56197.1; !1PID:g505583 GENETICS !$#gene FlyBase:Dbp25F !'##cross-references FlyBase:FBgn0014189 CLASSIFICATION #superfamily translation initiation factor eIF-4A KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$85-92 #region nucleotide-binding motif A (P-loop)\ !$189-194 #region nucleotide-binding motif B\ !$193-196 #region DEAD motif SUMMARY #length 424 #molecular-weight 48651 #checksum 3843 SEQUENCE /// ENTRY E64383 #type complete TITLE translation initiation factor eIF-4A homolog - Methanococcus jannaschii ALTERNATE_NAMES eIF-4A family probable ATP-dependent RNA helicase homolog ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 17-Nov-2000 ACCESSIONS E64383 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession E64383 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-367 ##label BUL !'##cross-references GB:U67514; GB:L77117; NID:g2826304; !1PIDN:AAB98663.1; PID:g1591383; TIGR:MJ0669 GENETICS !$#map_position REV595826-594723 !$#start_codon TTG CLASSIFICATION #superfamily translation initiation factor eIF-4A KEYWORDS ATP; DEAD box; P-loop; protein biosynthesis; purine !1nucleotide binding; RNA binding FEATURE !$51-58 #region nucleotide-binding motif A (P-loop)\ !$150-155 #region nucleotide-binding motif B\ !$154-157 #region DEAD motif SUMMARY #length 367 #molecular-weight 41920 #checksum 902 SEQUENCE /// ENTRY H69124 #type complete TITLE translation initiation factor eIF-4A homolog - Methanobacterium thermoautotrophicum (strain Delta H) ALTERNATE_NAMES ATP-dependent RNA helicase, eIF-4A family ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 17-Nov-2000 ACCESSIONS H69124 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession H69124 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-425 ##label MTH !'##cross-references GB:AE000807; GB:AE000666; NID:g2621239; !1PIDN:AAB84709.1; PID:g2621248 !'##experimental_source strain Delta H GENETICS !$#gene MTH203 CLASSIFICATION #superfamily translation initiation factor eIF-4A KEYWORDS ATP; DEAD box; P-loop; protein biosynthesis; purine !1nucleotide binding; RNA binding FEATURE !$48-55 #region nucleotide-binding motif A (P-loop)\ !$148-153 #region nucleotide-binding motif B\ !$152-155 #region DEAD motif SUMMARY #length 425 #molecular-weight 48232 #checksum 611 SEQUENCE /// ENTRY FIHUA #type complete TITLE translation initiation factor eIF-5A [validated] - human ALTERNATE_NAMES eIF-4D; REV binding factor ORGANISM #formal_name Homo sapiens #common_name man DATE 20-Jul-1989 #sequence_revision 01-Dec-1995 #text_change 18-Aug-2000 ACCESSIONS B31486; I53801; A49460; A25996 REFERENCE A31486 !$#authors Smit-McBride, Z.; Dever, T.E.; Hershey, J.W.B.; Merrick, !1W.C. !$#journal J. Biol. Chem. (1989) 264:1578-1583 !$#title Sequence determination and cDNA cloning of eukaryotic !1initiation factor 4D, the hypusine-containing protein. !$#cross-references MUID:89109169; PMID:2492279 !$#accession B31486 !'##molecule_type mRNA !'##residues 1-154 ##label SMI !'##cross-references GB:M23419; NID:g181996; PIDN:AAA58453.1; !1PID:g181997 REFERENCE I53801 !$#authors Koettnitz, K.; Kappel, B.; Baumruker, T.; Hauber, J.; Bevec, !1D. !$#journal Gene (1994) 144:249-252 !$#title The genomic structure encoding human initiation factor !1eIF-5A. !$#cross-references MUID:94314224; PMID:7545941 !$#accession I53801 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-35,'W',37-44,'A',46-84,'R',86-108,'P',110-154 ##label KOE !'##cross-references GB:S72024; NID:g565186; PIDN:AAD14095.1; !1PID:g4261795 REFERENCE A49460 !$#authors Ruhl, M.; Himmelspach, M.; Bahr, G.M.; Hammerschmid, F.; !1Jaksche, H.; Wolff, B.; Aschauer, H.; Farrington, G.K.; !1Probst, H.; Bevec, D.; Hauber, J. !$#journal J. Cell Biol. (1993) 123:1309-1320 !$#title Eukaryotic initiation factor 5A is a cellular target of the !1human immunodeficiency virus type 1 Rev activation domain !1mediating trans-activation. !$#cross-references MUID:94075396; PMID:8253832 !$#accession A49460 !'##molecule_type protein !'##residues 21-154 ##label RUH !'##experimental_source HeLa cells !'##note sequence extracted from NCBI backbone (NCBIP:140595) and !1corrected to correspond with the published sequence !'##note the amino terminal of the mature form is blocked REFERENCE A25996 !$#authors Park, M.H.; Liu, T.Y.; Neece, S.H.; Swiggard, W.J. !$#journal J. Biol. Chem. (1986) 261:14515-14519 !$#title Eukaryotic initiation factor 4D. Purification from human red !1blood cells and the sequence of amino acids around its !1single hypusine residue. !$#cross-references MUID:87033655; PMID:3095320 !$#accession A25996 !'##molecule_type protein !'##residues 48-49,'X',51-55 ##label PAR !'##note the residue designated 'X' was determined to be hypusine GENETICS !$#gene GDB:EIF5A !'##cross-references GDB:126412; OMIM:600187 !$#map_position 3q27-3qter CLASSIFICATION #superfamily translation initiation factor eIF-5A KEYWORDS acetylated amino end; hypusine; protein biosynthesis FEATURE !$2-154 #product translation initiation factor eIF-5A #status !8predicted #label MAT\ !$2 #modified_site blocked amino end (Ala) (in mature !8form) (probably acetylated) #status experimental\ !$50 #modified_site N6-(4-amino-2-hydroxybutyl)lysine !8(Lys) #status experimental SUMMARY #length 154 #molecular-weight 16832 #checksum 934 SEQUENCE /// ENTRY A31486 #type complete TITLE translation initiation factor eIF-5A [validated] - rabbit ALTERNATE_NAMES eIF-4D ORGANISM #formal_name Oryctolagus cuniculus #common_name domestic rabbit DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 18-Aug-2000 ACCESSIONS A31486 REFERENCE A31486 !$#authors Smit-McBride, Z.; Dever, T.E.; Hershey, J.W.B.; Merrick, !1W.C. !$#journal J. Biol. Chem. (1989) 264:1578-1583 !$#title Sequence determination and cDNA cloning of eukaryotic !1initiation factor 4D, the hypusine-containing protein. !$#cross-references MUID:89109169; PMID:2492279 !$#accession A31486 !'##molecule_type protein !'##residues 1-154 ##label SMI !'##note the authors placed residues 1-8 by homology with human !1initiation factor eIF-5A CLASSIFICATION #superfamily translation initiation factor eIF-5A KEYWORDS blocked amino end; hypusine; protein biosynthesis FEATURE !$2-154 #product translation initiation factor eIF-5A #status !8experimental #label MAT\ !$2 #modified_site blocked amino end (Ala) (in mature !8form) (probably acetylated) #status experimental\ !$50 #modified_site N6-(4-amino-2-hydroxybutyl)lysine !8(Lys) #status predicted SUMMARY #length 154 #molecular-weight 16816 #checksum 1174 SEQUENCE /// ENTRY A42156 #type complete TITLE translation initiation factor eIF-5A I [validated] - chicken ALTERNATE_NAMES eIF-4D; hypusine-containing protein ORGANISM #formal_name Gallus gallus #common_name chicken DATE 07-Apr-1994 #sequence_revision 04-Oct-1996 #text_change 18-Aug-2000 ACCESSIONS I50227; A42156 REFERENCE I50227 !$#authors Rinaudo, M.S.; Joe, Y.A.; Park, M.H. !$#journal Gene (1993) 137:303-307 !$#title Cloning and sequencing of a chick embryo cDNA encoding the !120-kDa hypusine-containing protein, eIF-5A. !$#cross-references MUID:94131302; PMID:7916728 !$#accession I50227 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-153 ##label RIN !'##cross-references GB:M99499; NID:g289799; PIDN:AAA17444.1; !1PID:g289800 REFERENCE A42156 !$#authors Wolff, E.C.; Kinzy, T.G.; Merrick, W.C.; Park, M.H. !$#journal J. Biol. Chem. (1992) 267:6107-6113 !$#title Two isoforms of eIF-5A in chick embryo. Isolation, activity, !1and comparison of sequences of the hypusine-containing !1proteins. !$#cross-references MUID:92210582; PMID:1556119 !$#accession A42156 !'##molecule_type protein !'##residues 7-21,'X',23-37,'X',39-72,'X',74-85;87-121 ##label WOL CLASSIFICATION #superfamily translation initiation factor eIF-5A KEYWORDS hypusine; protein biosynthesis FEATURE !$2-153 #product translation initiation factor eIF-5A #status !8predicted #label MAT\ !$50 #modified_site N6-(4-amino-2-hydroxybutyl)lysine !8(Lys) #status experimental SUMMARY #length 153 #molecular-weight 16720 #checksum 9600 SEQUENCE /// ENTRY S41010 #type complete TITLE translation initiation factor eIF-5A T05G5.10 [similarity] - Caenorhabditis elegans ALTERNATE_NAMES protein T05G5.10 ORGANISM #formal_name Caenorhabditis elegans DATE 10-Sep-1999 #sequence_revision 18-Aug-2000 #text_change 18-Aug-2000 ACCESSIONS S41010 REFERENCE S41001 !$#authors Thomas, K. !$#submission submitted to the EMBL Data Library, October 1993 !$#accession S41010 !'##molecule_type DNA !'##residues 1-161 ##label THO !'##cross-references EMBL:Z27079; NID:g414641; PIDN:CAA81597.1; !1PID:g3879493 !'##note the initiation codon for the translation of this sequence is !1revised in GenBank entry CET05G5 GENETICS !$#introns 12/2; 55/3; 106/3; 152/3 CLASSIFICATION #superfamily translation initiation factor eIF-5A KEYWORDS hypusine; protein biosynthesis FEATURE !$54 #modified_site N6-(4-amino-2-hydroxybutyl)lysine !8(Lys) #status predicted SUMMARY #length 161 #molecular-weight 17867 #checksum 4123 SEQUENCE /// ENTRY FIBYA1 #type complete TITLE translation initiation factor eIF-5A.1 [validated] - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypusine-containing protein HP2; protein YEL034w; translation initiation factor eIF-4D ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 23-Mar-2001 ACCESSIONS A40259; S13772; S43753; S30849; S50510; S39918; S38975; !1S16794 REFERENCE A40259 !$#authors Schnier, J.; Schwelberger, H.G.; Smit-McBride, Z.; Kang, !1H.A.; Hershey, J.W.B. !$#journal Mol. Cell. Biol. (1991) 11:3105-3114 !$#title Translation initiation factor 5A and its hypusine !1modification are essential for cell viability in the yeast !1Saccharomyces cerevisiae. !$#cross-references MUID:91246178; PMID:1903841 !$#accession A40259 !'##molecule_type DNA !'##residues 1-157 ##label SCH !'##cross-references EMBL:M63541; NID:g172979; PIDN:AAA35155.1; !1PID:g172980 REFERENCE S13771 !$#authors Sandholzer, U.R. !$#submission submitted to the Protein Sequence Database, December 1990 !$#accession S13772 !'##molecule_type DNA !'##residues 1-157 ##label SAN REFERENCE S43753 !$#authors Sandholzer, U.R. !$#submission submitted to the EMBL Data Library, December 1990 !$#accession S43753 !'##molecule_type DNA !'##residues 1-157 ##label SA2 !'##cross-references EMBL:X56236; NID:g3805; PIDN:CAA39693.1; PID:g3806 REFERENCE S30812 !$#authors Mulligan, J.T.; Dietrich, F.S.; Hennessey, K.M.; Sehl, P.; !1Komp, C.; Wei, Y.; Taylor, P.; Nakahara, K.; Roberts, D.; !1Davis, R.W. !$#submission submitted to the EMBL Data Library, February 1993 !$#accession S30849 !'##molecule_type DNA !'##residues 1-157 ##label MUL !'##cross-references GB:U18779; EMBL:L10830; NID:g603625; !1PIDN:AAB65008.1; PID:g603645 REFERENCE S50429 !$#authors Dietrich, F.S. !$#submission submitted to the EMBL Data Library, December 1994 !$#description The sequence of S. cerevisiae cosmids 8199, 8334, and 9871. !$#accession S50510 !'##molecule_type DNA !'##residues 1-157 ##label DIE !'##cross-references EMBL:U18779; NID:g603625; PIDN:AAB65008.1; !1PID:g603645; GSPDB:GN00005; MIPS:YEL034w REFERENCE S39918 !$#authors Woehl, T.; Klier, H.; Ammer, H.; Lottspeich, F.; Magdolen, !1V. !$#journal Mol. Gen. Genet. (1993) 241:305-311 !$#title The HYP2 gene of Saccharomyces cerevisiae is essential for !1aerobic growth: characterization of different isoforms of !1the hypusine-containing protein Hyp2p and analysis of gene !1disruption mutants. !$#cross-references MUID:94067011; PMID:8246884 !$#accession S39918 !'##molecule_type protein !'##residues 2-16 ##label WOE REFERENCE S38975 !$#authors Klier, H.; Woehl, T.; Eckerskorn, C.; Magdolen, V.; !1Lottspeich, F. !$#journal FEBS Lett. (1993) 334:360-364 !$#title Determination and mutational analysis of the phosphorylation !1site in the hypusine-containing protein Hyp2p. !$#cross-references MUID:94063058; PMID:8243648 !$#accession S38975 !'##molecule_type protein !'##residues 2-27 ##label KLI GENETICS !$#gene SGD:HYP2; TIF51A; MIPS:YEL034w !'##cross-references SGD:S0000760; MIPS:YEL034w !$#map_position 5L CLASSIFICATION #superfamily translation initiation factor eIF-5A KEYWORDS acetylated amino end; hypusine; phosphoprotein; protein !1biosynthesis FEATURE !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental\ !$2 #binding_site phosphate (Ser) (covalent) #status !8experimental\ !$51 #modified_site N6-(4-amino-2-hydroxybutyl)lysine !8(Lys) #status predicted SUMMARY #length 157 #molecular-weight 17114 #checksum 427 SEQUENCE /// ENTRY FIBYA2 #type complete TITLE translation initiation factor eIF-5A.2 [similarity] - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypusine-containing protein HP1; protein GTD157; protein J1651; protein YJR047c; translation initiation factor eIF-4D ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 18-Aug-2000 ACCESSIONS B40259; A36281; S13771; S57066; S63772; S16795 REFERENCE A40259 !$#authors Schnier, J.; Schwelberger, H.G.; Smit-McBride, Z.; Kang, !1H.A.; Hershey, J.W.B. !$#journal Mol. Cell. Biol. (1991) 11:3105-3114 !$#title Translation initiation factor 5A and its hypusine !1modification are essential for cell viability in the yeast !1Saccharomyces cerevisiae. !$#cross-references MUID:91246178; PMID:1903841 !$#accession B40259 !'##molecule_type DNA !'##residues 1-157 ##label SCH !'##cross-references EMBL:M63542; NID:g172981; PIDN:AAA35156.1; !1PID:g172982 REFERENCE A36281 !$#authors Mehta, K.D.; Leung, D.; Lefebvre, L.; Smith, M. !$#journal J. Biol. Chem. (1990) 265:8802-8807 !$#title The ANB1 locus of Saccharomyces cerevisiae encodes the !1protein synthesis initiation factor eIF-4D. !$#cross-references MUID:90256809; PMID:2187871 !$#accession A36281 !'##molecule_type DNA !'##residues 1-157 ##label MEH !'##cross-references GB:J05455; NID:g171061; PIDN:AAA34425.1; !1PID:g171062 REFERENCE S13771 !$#authors Sandholzer, U.R. !$#submission submitted to the Protein Sequence Database, December 1990 !$#accession S13771 !'##molecule_type DNA !'##residues 1-157 ##label SAN !'##cross-references EMBL:X56235; NID:g3803; PIDN:CAA39692.1; PID:g3804; !1GSPDB:GN00010; MIPS:YJR047c REFERENCE S57052 !$#authors Huang, M.E.; Chuat, J.C.; Galibert, F. !$#submission submitted to the Protein Sequence Database, September 1995 !$#accession S57066 !'##molecule_type DNA !'##residues 1-157 ##label MAN !'##cross-references EMBL:Z49547; NID:g1015704; PIDN:CAA89575.1; !1PID:g1015705; GSPDB:GN00010; MIPS:YJR047c REFERENCE S63757 !$#authors Huang, M.E.; Chuat, J.C.; Galibert, F. !$#journal Yeast (1995) 11:775-781 !$#title Analysis of a 42.5 kb DNA sequence of chromosome X reveals !1three tRNA genes and 14 new open reading frames including a !1gene most probably belonging to the family of !1ubiquitin-protein ligases. !$#cross-references MUID:95397595; PMID:7668047 !$#accession S63772 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-157 ##label HUA !'##cross-references EMBL:L36344; NID:g1197060; PIDN:AAA88750.1; !1PID:g1197076 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1February 1996 GENETICS !$#gene SGD:ANB1; HYP1; TIF51B; MIPS:YJR047c !'##cross-references SGD:S0003808; MIPS:YJR047c !$#map_position 10R CLASSIFICATION #superfamily translation initiation factor eIF-5A KEYWORDS hypusine; phosphoprotein; protein biosynthesis FEATURE !$51 #modified_site N6-(4-amino-2-hydroxybutyl)lysine !8(Lys) #status predicted SUMMARY #length 157 #molecular-weight 17131 #checksum 927 SEQUENCE /// ENTRY FIAAA #type complete TITLE translation initiation factor eIF-5A [similarity] - alfalfa ALTERNATE_NAMES translation initiation factor eIF-4D ORGANISM #formal_name Medicago sativa #common_name alfalfa DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 18-Aug-2000 ACCESSIONS S17736 REFERENCE S17736 !$#authors Pay, A.; Heberle-Bors, E.; Hirt, H. !$#journal Plant Mol. Biol. (1991) 17:927-929 !$#title Isolation and sequence determination of the plant homologue !1of the eukaryotic initiation factor 4D cDNA from alfalfa, !1Medicago sativa. !$#cross-references MUID:92003704; PMID:1912507 !$#accession S17736 !'##molecule_type mRNA !'##residues 1-161 ##label PAY !'##cross-references EMBL:X59441; NID:g19600; PIDN:CAA42065.1; !1PID:g19601 CLASSIFICATION #superfamily translation initiation factor eIF-5A KEYWORDS hypusine; protein biosynthesis FEATURE !$52 #modified_site N6-(4-amino-2-hydroxybutyl)lysine !8(Lys) #status predicted SUMMARY #length 161 #molecular-weight 17659 #checksum 6859 SEQUENCE /// ENTRY FIDOA #type complete TITLE translation initiation factor eIF-5A [validated] - slime mold (Dictyostelium discoideum) ALTERNATE_NAMES hypusine-containing protein; translation initiation factor eIF-4D ORGANISM #formal_name Dictyostelium discoideum DATE 31-Mar-1992 #sequence_revision 30-Sep-1992 #text_change 18-Aug-2000 ACCESSIONS S03886; S18514 REFERENCE S03886 !$#authors Sandholzer, U.; Centea-Intemann, M.; Noegel, A.A.; !1Lottspeich, F. !$#journal FEBS Lett. (1989) 246:94-100 !$#title cDNA and derived amino acid sequence of the hypusine !1containing protein from Dictyostelium discoideum. !$#cross-references MUID:89211421; PMID:2540042 !$#accession S03886 !'##molecule_type mRNA !'##residues 1-169 ##label SAN !'##cross-references EMBL:X14970; NID:g7278; PIDN:CAA33095.1; PID:g7279 !$#accession S18514 !'##molecule_type protein !'##residues 43-49;63-82;103-150 ##label SAN2 !'##note the authors translated the codon GCC for residue 22 as Tyr, GGT !1for residue 23 as Ala, TCA for residue 24 as Gln, GGT for !1residue 25 as Ala, and GCT for residue 26 as Gly; the !1sequence shown follows the authors' translation CLASSIFICATION #superfamily translation initiation factor eIF-5A KEYWORDS hypusine; protein biosynthesis FEATURE !$65 #modified_site N6-(4-amino-2-hydroxybutyl)lysine !8(Lys) #status experimental SUMMARY #length 169 #molecular-weight 18339 #checksum 637 SEQUENCE /// ENTRY A34888 #type complete TITLE transcription factor GATA-1 - human ALTERNATE_NAMES finger protein GF-1; transcription factor Eryf1; transcription factor NF-E1 ORGANISM #formal_name Homo sapiens #common_name man DATE 20-Jul-1990 #sequence_revision 12-Jul-1996 #text_change 16-Jul-1999 ACCESSIONS A34888; S07121 REFERENCE A34888 !$#authors Zon, L.I.; Tsai, S.F.; Burgess, S.; Matsudaira, P.; Bruns, !1G.A.P.; Orkin, S.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:668-672 !$#title The major human erythroid DNA-binding protein (GF-1): !1primary sequence and localization of the gene to the X !1chromosome. !$#cross-references MUID:90138889; PMID:2300555 !$#accession A34888 !'##molecule_type mRNA !'##residues 1-413 ##label ZON !'##cross-references GB:M30601; NID:g183071; PIDN:AAA35885.1; !1PID:g183072 REFERENCE S07121 !$#authors Trainor, C.D.; Evans, T.; Felsenfeld, G.; Boguski, M.S. !$#journal Nature (1990) 343:92-96 !$#title Structure and evolution of a human erythroid transcription !1factor. !$#cross-references MUID:90114418; PMID:2104960 !$#accession S07121 !'##molecule_type mRNA !'##residues 1-413 ##label TRA !'##cross-references EMBL:X17254; NID:g31242; PIDN:CAA35120.1; !1PID:g31243 COMMENT This transcriptional activator is named for the core, GATA, !1of the nucleotide motif (A/T)GATA(A/G) to which it binds. COMMENT GATA-1 appears to be a major regulator of both globin and !1non-globin erythroid-specific gene transcription, including !1its own. COMMENT GATA-1 is expressed in erythroid cells, megakaryocytes, and !1mast cells of myeloid origin. GENETICS !$#gene GDB:GATA1; GF1 !'##cross-references GDB:125373; OMIM:305371 !$#map_position Xp11.23-Xp11.23 CLASSIFICATION #superfamily transcription factor GATA-1; GATA-type zinc !1finger homology KEYWORDS DNA binding; nucleus; transcription factor; transcription !1regulation; zinc finger FEATURE !$201-254 #domain GATA-type zinc finger homology #label GZF1\ !$204-228 #region zinc finger GATA motif\ !$255-308 #domain GATA-type zinc finger homology #label GZF2\ !$258-282 #region zinc finger GATA motif SUMMARY #length 413 #molecular-weight 42751 #checksum 2904 SEQUENCE /// ENTRY A41267 #type complete TITLE transcription factor elt-1 - Caenorhabditis elegans ALTERNATE_NAMES erythrocytelike transcription factor ORGANISM #formal_name Caenorhabditis elegans DATE 28-May-1992 #sequence_revision 12-Jul-1996 #text_change 16-Jul-1999 ACCESSIONS A41267; S23646 REFERENCE A41267 !$#authors Spieth, J.; Shim, Y.H.; Lea, K.; Conrad, R.; Blumenthal, T. !$#journal Mol. Cell. Biol. (1991) 11:4651-4659 !$#title elt-1, an embryonically expressed Caenorhabditis elegans !1gene homologous to the GATA transcription factor family. !$#cross-references MUID:91342668; PMID:1875944 !$#accession A41267 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-416 ##label SPI !'##cross-references GB:X57834; NID:g6701; PIDN:CAA40967.1; PID:g6702 COMMENT The 300 base pair region immediately upstream of the TATA !1box for this gene contains eight copies of the (A/T)GATA(A/ !1G) motif, to which the elt-1 gene product binds. This !1suggests that elt-1 regulates its own expression. COMMENT This protein appears to be expressed mostly or entirely in !1embryos. GENETICS !$#gene elt-1 !$#introns 51/1; 87/1; 210/1; 261/3; 304/3 !$#note elt-1 mRNA is trans-spliced, upstream of the coding region, !1to the 22-base leader SL1 CLASSIFICATION #superfamily transcription factor GATA-1; GATA-type zinc !1finger homology KEYWORDS DNA binding; nucleus; transcription factor; transcription !1regulation; zinc finger FEATURE !$214-267 #domain GATA-type zinc finger homology #label GZF1\ !$217-241 #region zinc finger GATA motif\ !$269-322 #domain GATA-type zinc finger homology #label GZF2\ !$272-296 #region zinc finger GATA motif SUMMARY #length 416 #molecular-weight 44823 #checksum 1064 SEQUENCE /// ENTRY A39794 #type complete TITLE transcription factor GATA-3 - human ALTERNATE_NAMES enhancer-binding protein Gata3; GATA-binding protein 3 ORGANISM #formal_name Homo sapiens #common_name man DATE 07-Feb-1992 #sequence_revision 12-Jul-1996 #text_change 16-Jul-1999 ACCESSIONS A39794; S16326; S15027; A41148; S16155 REFERENCE A39794 !$#authors Ko, L.J.; Yamamoto, M.; Leonard, M.W.; George, K.M.; Ting, !1P.; Engel, J.D. !$#journal Mol. Cell. Biol. (1991) 11:2778-2784 !$#title Murine and human T-lymphocyte GATA-3 factors mediate !1transcription through a cis-regulatory element within the !1human T-cell receptor delta gene enhancer. !$#cross-references MUID:91203899; PMID:2017177 !$#accession A39794 !'##molecule_type mRNA !'##residues 1-444 ##label KOA !'##cross-references GB:X55122; NID:g31663; PIDN:CAA38916.1; PID:g31664 REFERENCE S16326 !$#authors Joulin, V.; Bories, D.; Eleouet, J.F.; Labastie, M.C.; !1Chretien, S.; Mattei, M.G.; Romeo, P.H. !$#journal EMBO J. (1991) 10:1809-1816 !$#title A T-cell specific TCR delta DNA binding protein is a member !1of the human GATA family. !$#cross-references MUID:91266910; PMID:2050118 !$#accession S16326 !'##molecule_type mRNA !'##residues 1-259,261-444 ##label JOU !'##cross-references EMBL:X58072; NID:g31665; PIDN:CAA41102.1; !1PID:g31666 REFERENCE S15027 !$#authors Ho, I.C.; Vorhees, P.; Marin, N.; Oakley, B.K.; Tsai, S.F.; !1Orkin, S.H.; Leiden, J.M. !$#journal EMBO J. (1991) 10:1187-1192 !$#title Human GATA-3: a lineage-restricted transcription factor that !1regulates the expression of the T cell receptor alpha gene. !$#cross-references MUID:91216113; PMID:1827068 !$#accession S15027 !'##status preliminary !'##molecule_type mRNA !'##residues 1-101,'V',103-172,'G',174-259,261-444 ##label HOI !'##cross-references EMBL:X55037; NID:g31661; PIDN:CAA38877.1; !1PID:g31662 REFERENCE A41148 !$#authors Marine, J.; Winoto, A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:7284-7288 !$#title The human enhancer-binding protein Gata3 binds to several !1T-cell receptor regulatory elements. !$#cross-references MUID:91334450; PMID:1871134 !$#accession A41148 !'##molecule_type mRNA !'##residues 1-10,'L',12-218,'Y',220-224,'TC',227-285,'RR',288-425,'A', !1427-441,'G',443-444 ##label MAR !'##cross-references GB:M69106; NID:g182999; PIDN:AAA35870.1; !1PID:g183000 COMMENT This transcriptional activator is named for the core, GATA, !1of the nucleotide motif (A/T)GATA(A/G) to which it binds. COMMENT GATA-3 is expressed in T cells, mast cells, embryonic brain, !1and kidney. GENETICS !$#gene GDB:GATA3 !'##cross-references GDB:132140; OMIM:131320 !$#map_position 10p15-10p15 CLASSIFICATION #superfamily transcription factor GATA-2; GATA-type zinc !1finger homology KEYWORDS DNA binding; nucleus; transcription factor; transcription !1regulation; zinc finger FEATURE !$261-314 #domain GATA-type zinc finger homology #label GZF1\ !$264-288 #region zinc finger GATA motif\ !$315-368 #domain GATA-type zinc finger homology #label GZF2\ !$318-342 #region zinc finger GATA motif SUMMARY #length 444 #molecular-weight 48045 #checksum 796 SEQUENCE /// ENTRY A48099 #type complete TITLE transcription factor GATA-4, retinoic acid-inducible - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 21-Jan-1994 #sequence_revision 12-Jul-1996 #text_change 16-Jul-1999 ACCESSIONS A48099 REFERENCE A48099 !$#authors Arceci, R.J.; King, A.A.; Simon, M.C.; Orkin, S.H.; Wilson, !1D.B. !$#journal Mol. Cell. Biol. (1993) 13:2235-2246 !$#title Mouse GATA-4: a retinoic acid-inducible GATA-binding !1transcription factor expressed in endodermally derived !1tissues and heart. !$#cross-references MUID:93204969; PMID:8455608 !$#accession A48099 !'##molecule_type mRNA !'##residues 1-439 ##label ARC !'##cross-references GB:M98339; NID:g293344; PIDN:AAA37662.1; !1PID:g293345 !'##experimental_source embryo !'##note sequence extracted from NCBI backbone (NCBIN:127640, !1NCBIP:127641) COMMENT This transcriptional activator is named for the core, GATA, !1of the nucleotide motif (A/T)GATA(A/G) to which it binds. COMMENT GATA-4 is expressed in heart, intestinal epithelium, gonads, !1and primitive endoderm. CLASSIFICATION #superfamily transcription factor GATA-4; GATA-type zinc !1finger homology KEYWORDS DNA binding; nucleus; transcription factor; transcription !1regulation; zinc finger FEATURE !$212-265 #domain GATA-type zinc finger homology #label GZF1\ !$266-319 #domain GATA-type zinc finger homology #label GZF2 SUMMARY #length 439 #molecular-weight 45245 #checksum 9971 SEQUENCE /// ENTRY A57601 #type complete TITLE transcription factor dGATAc - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 08-Feb-1996 #sequence_revision 26-Jul-1996 #text_change 17-Nov-2000 ACCESSIONS A57601 REFERENCE A57601 !$#authors Lin, W.H.; Huang, L.H.; Yeh, J.Y.; Hoheisel, J.; Lehrach, !1H.; Sun, Y.H.; Tsai, S.F. !$#journal J. Biol. Chem. (1995) 270:25150-25158 !$#title Expression of a Drosophila GATA transcription factor in !1multiple tissues in the developing embryos. Identification !1of homozygous lethal mutants with P-element insertion at the !1promoter region. !$#cross-references MUID:96027621; PMID:7559649 !$#accession A57601 !'##molecule_type mRNA !'##residues 1-486 ##label LIN !'##cross-references GB:D50542; NID:g1060873; PIDN:BAA09102.1; !1PID:g1815600 GENETICS !$#gene FlyBase:Gata-c !'##cross-references FlyBase:FBgn0001138 CLASSIFICATION #superfamily transcription factor dGATAc; GATA-type zinc !1finger homology KEYWORDS DNA binding; transcription factor; zinc finger FEATURE !$258-311 #domain GATA-type zinc finger homology #label GZF1\ !$318-371 #domain GATA-type zinc finger homology #label GZF2 SUMMARY #length 486 #molecular-weight 50634 #checksum 6839 SEQUENCE /// ENTRY S40382 #type complete TITLE box A-binding factor - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES ABF; transcription factor dGATAb ORGANISM #formal_name Drosophila melanogaster DATE 13-Jan-1995 #sequence_revision 06-Sep-1996 #text_change 16-Jul-1999 ACCESSIONS S40382 REFERENCE S40382 !$#authors Abel, T.; Michelson, A.M.; Maniatis, T. !$#journal Development (1993) 119:623-633 !$#title A Drosophila GATA family member that binds to Adh regulatory !1sequences is expressed in the developing fat body. !$#cross-references MUID:94244465; PMID:8187633 !$#accession S40382 !'##molecule_type mRNA !'##residues 1-779 ##label ABE !'##cross-references EMBL:X76217; NID:g441491; PIDN:CAA53807.1; !1PID:g441492 COMMENT This transcriptional activator is the earliest known marker !1of the developing fat body and may play a role in its !1organogenesis. GENETICS !$#gene FlyBase:srp !'##cross-references FlyBase:FBgn0003507 CLASSIFICATION #superfamily box A-binding factor; GATA-type zinc finger !1homology KEYWORDS DNA binding; nucleus; transcription factor; transcription !1regulation; zinc finger FEATURE !$316-369 #domain GATA-type zinc finger homology #label GZF\ !$319-343 #region zinc finger GATA motif SUMMARY #length 779 #molecular-weight 82109 #checksum 2173 SEQUENCE /// ENTRY A34755 #type complete TITLE nitrogen regulatory protein nit-2 - Neurospora crassa ORGANISM #formal_name Neurospora crassa DATE 13-Jul-1990 #sequence_revision 26-Jul-1996 #text_change 16-Feb-1997 ACCESSIONS A34755 REFERENCE A34755 !$#authors Fu, Y.H.; Marzluf, G.A. !$#journal Mol. Cell. Biol. (1990) 10:1056-1065 !$#title nit-2, the major nitrogen regulatory gene of Neurospora !1crassa, encodes a protein with a putative zinc finger !1DNA-binding domain. !$#cross-references MUID:90158568; PMID:2137552 !$#accession A34755 !'##molecule_type DNA; mRNA !'##residues 1-1036 ##label FUY !'##cross-references GB:M33956 GENETICS !$#introns 209/2; 335/3 CLASSIFICATION #superfamily nitrogen regulatory protein nit-2; GATA-type !1zinc finger homology KEYWORDS DNA binding; transcription regulation; zinc finger FEATURE !$740-793 #domain GATA-type zinc finger homology #label GZF\ !$743-767 #region zinc finger GATA motif SUMMARY #length 1036 #molecular-weight 109295 #checksum 235 SEQUENCE /// ENTRY A57988 #type complete TITLE regulatory protein areA - Emericella nidulans ORGANISM #formal_name Emericella nidulans, Aspergillus nidulans DATE 26-Jul-1996 #sequence_revision 26-Jul-1996 #text_change 16-Jun-2000 ACCESSIONS A57988; S10017; S70168; S72883 REFERENCE S10017 !$#authors Kudla, B.; Caddick, M.X.; Langdon, T.; Martinez-Rossi, N.M.; !1Bennett, C.F.; Sibley, S.; Davies, R.W.; Arst Jr., H.N. !$#journal EMBO J. (1990) 9:1355-1364 !$#title The regulatory gene areA mediating nitrogen metabolite !1repression in Aspergillus nidulans. Mutations affecting !1specificity of gene activation alter a loop residue of a !1putative zinc finger. !$#cross-references MUID:90228331; PMID:1970293 !$#accession A57988 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-876 ##label KUD !'##cross-references EMBL:X52491; NID:g1019911; PIDN:CAA36731.1; !1PID:g1154625 !'##note this sequence represents reinterpretation to include two exons !$#accession S10017 !'##molecule_type DNA !'##residues 158-876 ##label KU2 !'##cross-references EMBL:X52491 !'##note this sequence represents the authors' original translation REFERENCE S70167 !$#authors Langdon, T.; Sheerins, A.; Ravagnani, A.; Gielkens, M.; !1Caddick, M.X.; Arst Jr., H.N. !$#journal Mol. Microbiol. (1995) 17:877-888 !$#title Mutational analysis reveals dispensability of the N-terminal !1region of the Aspergillus transcription factor mediating !1nitrogen metabolite repression. !$#cross-references MUID:96123430; PMID:8596437 !$#accession S70168 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-791,'A',793,'T',795,'SPGTNS',802-876 ##label LAN !'##cross-references EMBL:X52491 REFERENCE S72883 !$#authors Caddick, M.X. !$#submission submitted to the EMBL Data Library, October 1995 !$#accession S72883 !'##molecule_type DNA !'##residues 1-876 ##label CAD !'##cross-references EMBL:X52491; NID:g1019911; PIDN:CAA36731.1; !1PID:g1154625 GENETICS !$#gene areA !$#introns 147/2 FUNCTION !$#description mediates nitrogen metabolite repression CLASSIFICATION #superfamily nitrogen regulatory protein nit-2; GATA-type !1zinc finger homology KEYWORDS DNA binding; transcription regulation; zinc finger FEATURE !$670-723 #domain GATA-type zinc finger homology #label GZF\ !$673-697 #region zinc finger GATA motif SUMMARY #length 876 #molecular-weight 94195 #checksum 5589 SEQUENCE /// ENTRY TVHUGL #type complete TITLE transforming protein gli - human ALTERNATE_NAMES glioma-associated transforming protein ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 10-Sep-1999 ACCESSIONS S00672 REFERENCE S00672 !$#authors Kinzler, K.W.; Ruppert, J.M.; Bigner, S.H.; Vogelstein, B. !$#journal Nature (1988) 332:371-374 !$#title The GLI gene is a member of the Kruppel family of zinc !1finger proteins. !$#cross-references MUID:88175051; PMID:2832761 !$#accession S00672 !'##molecule_type mRNA !'##residues 1-1106 ##label KIN !'##cross-references EMBL:X07384; NID:g31767; PIDN:CAA30297.1; !1PID:g31768 GENETICS !$#gene GDB:GLI !'##cross-references GDB:119988; OMIM:165220 !$#map_position 12q13.2-12q13.3 CLASSIFICATION #superfamily gli transforming protein KEYWORDS DNA binding; duplication; oncogene; transcription !1regulation; transforming protein; zinc finger FEATURE !$235-260 #region zinc finger CCHH motif\ !$268-295 #region zinc finger CCHH motif\ !$301-325 #region zinc finger CCHH motif\ !$331-356 #region zinc finger CCHH motif\ !$362-387 #region zinc finger CCHH motif SUMMARY #length 1106 #molecular-weight 117904 #checksum 1196 SEQUENCE /// ENTRY TWXL3 #type complete TITLE transcription factor IIIA - African clawed frog ALTERNATE_NAMES factor A; TFIIIA ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 21-Jul-2000 ACCESSIONS A90857; A24961; S21776; A03529; A91007; S40784; S40785 REFERENCE A90857 !$#authors Ginsberg, A.M.; King, B.O.; Roeder, R.G. !$#journal Cell (1984) 39:479-489 !$#title Xenopus 5S gene transcription factor, TFIIIA: !1characterization of a cDNA clone and measurement of RNA !1levels throughout development. !$#cross-references MUID:85074456; PMID:6210149 !$#accession A90857 !'##molecule_type mRNA !'##residues 1-344 ##label GIN !'##cross-references GB:K02938; NID:g214818; PIDN:AAA49967.1; !1PID:g214819 REFERENCE A91007 !$#authors Miller, J.; McLachlan, A.D.; Klug, A. !$#journal EMBO J. (1985) 4:1609-1614 !$#title Repetitive zinc-binding domains in the protein transcription !1factor IIIA from Xenopus oocytes. !$#cross-references MUID:85284956; PMID:4040853 !$#contents annotation REFERENCE S40785 !$#authors Smith, J.F.; Hawkins, J.; Leonard, R.E.; Hanas, J.S. !$#journal Nucleic Acids Res. (1991) 19:6871-6876 !$#title Structural elements in the N-terminal half of transcription !1factor IIIA required for factor binding to the 5S RNA gene !1internal control region. !$#cross-references MUID:92107675; PMID:1762917 !$#contents annotation; site-directed mutagenesis REFERENCE A24961 !$#authors Tso, J.Y.; Van Den Berg, D.J.; Korn, L.J. !$#journal Nucleic Acids Res. (1986) 14:2187-2200 !$#title Structure of the gene for Xenopus transcription factor !1TFIIIA. !$#cross-references MUID:86176722; PMID:3754326 !$#accession A24961 !'##molecule_type DNA !'##residues 1-296,'C',298-312,'I',314-333,'D',335-342,'L',344 ##label !1TSO !'##cross-references EMBL:X03681; NID:g65111; PIDN:CAB51745.1; !1PID:g5679716 REFERENCE S21776 !$#authors Liao, X.; Clemens, K.R.; Tennant, L.; Wright, P.E.; !1Gottesfeld, J.M. !$#journal J. Mol. Biol. (1992) 223:857-871 !$#title Specific interaction of the first three zinc fingers of !1TFIIIA with the internal control region of the Xenopus 5 S !1RNA gene. !$#cross-references MUID:92167265; PMID:1538401 !$#accession S21776 !'##molecule_type mRNA !'##residues 1-101 ##label LIA REFERENCE S40784 !$#authors del Rio, S.; Setzer, D.R. !$#journal Nucleic Acids Res. (1991) 19:6197-6203 !$#title High yield purification of active transcription factor IIIA !1expressed in E.coli. !$#cross-references MUID:92066468; PMID:1956778 !$#contents annotation !$#note an engineered sequence was used to obtain high-yield !1expression in an E. coli system COMMENT This zinc-containing protein (7-11 Zn/molecule), which !1interacts with the internal control region of approximately !150 bases within the 5S RNA genes, is required for correct !1transcription of these genes by RNA polymerase III. It also !1binds the transcribed 5S RNAs. COMMENT Most of the Cys and His residues are ligands for zinc !1binding. GENETICS !$#introns 40/3; 74/2; 106/3; 136/2; 161/1; 190/1; 266/3; 284/3 CLASSIFICATION #superfamily transcription factor IIIA KEYWORDS DNA binding; duplication; nucleus; tandem repeat; !1transcription factor; zinc finger FEATURE !$15-37 #region zinc finger CCHH motif\ !$45-67 #region zinc finger CCHH motif\ !$75-98 #region zinc finger CCHH motif\ !$107-129 #region zinc finger CCHH motif\ !$137-159 #region zinc finger CCHH motif\ !$164-188 #region zinc finger CCHH motif\ !$194-214 #region zinc finger CCHH motif\ !$223-246 #region zinc finger CCHH motif\ !$254-276 #region zinc finger CCHH motif SUMMARY #length 344 #molecular-weight 39745 #checksum 8531 SEQUENCE /// ENTRY S27802 #type complete TITLE zinc finger protein - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 08-Dec-2000 ACCESSIONS A45172; S27802 REFERENCE A45172 !$#authors Klein, R.D.; Meyer, B.J. !$#journal Cell (1993) 72:349-364 !$#title Independent domains of the Sdc-3 protein control sex !1determination and dosage compensation in C. elegans. !$#cross-references MUID:93161411; PMID:8431944 !$#accession A45172 !'##status preliminary !'##molecule_type DNA !'##residues 1-2150 ##label KLE !'##cross-references EMBL:M85149; NID:g156440; PIDN:AAA28144.1; !1PID:g156441 !'##experimental_source strain N2 !'##note sequence extracted from NCBI backbone (NCBIP:124842) GENETICS !$#gene sdc-3 !$#introns 70/1; 102/1; 153/3; 258/1; 305/1; 1283/1; 1398/1; 1703/2; !11853/1; 1887/1; 1908/3; 1982/3; 2075/2 CLASSIFICATION #superfamily zinc finger protein sdc-3 KEYWORDS DNA binding; nucleus; zinc finger SUMMARY #length 2150 #molecular-weight 249954 #checksum 8173 SEQUENCE /// ENTRY TWBYA2 #type complete TITLE transcription factor ACE2 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES metallothionein expression activator; protein L3123; protein YLR131c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 08-Dec-2000 ACCESSIONS S12943; S59320; S64973 REFERENCE S12943 !$#authors Butler, G.; Thiele, D.J. !$#journal Mol. Cell. Biol. (1991) 11:476-485 !$#title ACE2, an activator of yeast metallothionein expression which !1is homologous to SWI5. !$#cross-references MUID:91094864; PMID:1986241 !$#accession S12943 !'##molecule_type DNA !'##residues 1-770 ##label BUT !'##cross-references GB:M55619; NID:g170975; PIDN:AAA34387.1; !1PID:g170976 !'##experimental_source strain DBY939 REFERENCE S59313 !$#authors Delius, H. !$#submission submitted to the EMBL Data Library, June 1995 !$#description 36.8 kb of S.cerevisiae chromosome XII including ACE2, CKI1, !1PDC5, SLS1, PUT1 and tRNA-Asp. !$#accession S59320 !'##molecule_type DNA !'##residues 1-770 ##label DEL !'##cross-references EMBL:X91258; NID:g995686; PIDN:CAA62643.1; !1PID:g995694 !'##experimental_source strain S288C REFERENCE S64967 !$#authors Delius, H.; Hebling, U. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64973 !'##molecule_type DNA !'##residues 1-770 ##label DEW !'##cross-references EMBL:Z73303; NID:g1360542; PIDN:CAA97702.1; !1PID:g1360543; GSPDB:GN00012; MIPS:YLR131c !'##note experimental_source strain S288C GENETICS !$#gene SGD:ACE2; MIPS:YLR131c !'##cross-references SGD:S0004121; MIPS:YLR131c !$#map_position 12R CLASSIFICATION #superfamily transcription factor SWI5 KEYWORDS DNA binding; metalloprotein; transcription factor; zinc !1finger FEATURE !$603-627 #region zinc finger CCHH motif\ !$633-657 #region zinc finger CCHH motif\ !$662-685 #region zinc finger CCHC motif\ !$605,610,623,627 #binding_site zinc (Cys, Cys, His, His) #status !8predicted\ !$635,640,653,657 #binding_site zinc (Cys, Cys, His, His) #status !8predicted\ !$664,666,679,685 #binding_site zinc (Cys, Cys, His, Cys) #status !8predicted SUMMARY #length 770 #molecular-weight 86633 #checksum 6196 SEQUENCE /// ENTRY TWBYS5 #type complete TITLE transcription factor SWI5 [validated] - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YD8358.03c; protein YDR146c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 08-Dec-2000 ACCESSIONS S00342; S57973 REFERENCE S00342 !$#authors Stillman, D.J.; Bankier, A.T.; Seddon, A.; Groenhout, E.G.; !1Nasmyth, K.A. !$#journal EMBO J. (1988) 7:485-494 !$#title Characterization of a transcription factor involved in !1mother cell specific transcription of the yeast HO gene. !$#cross-references MUID:88211561; PMID:3284746 !$#accession S00342 !'##molecule_type DNA !'##residues 1-709 ##label STI !'##cross-references EMBL:X06978; NID:g4595; PIDN:CAA30040.1; PID:g4596 REFERENCE S57971 !$#authors Murphy, L.; Richards, C.; Harris, D. !$#submission submitted to the EMBL Data Library, July 1995 !$#accession S57973 !'##molecule_type DNA !'##residues 1-709 ##label MUR !'##cross-references EMBL:Z50046; NID:g899393; PIDN:CAA90369.1; !1PID:g899396; GSPDB:GN00004; MIPS:YDR146c !'##experimental_source strain AB972 REFERENCE A66200 !$#authors Dutnall, R.N.; Neuhaus, D.; Rhodes, D. !$#submission submitted to the Brookhaven Protein Data Bank, February 1996 !$#cross-references PDB:1NCS !$#contents annotation; conformation by (1)H-NMR, residues 532-578 REFERENCE A67819 !$#authors Neuhaus, D.; Nakaseko, Y.; Schwabe, J.W.R.; Rhodes, D.; !1Klug, A. !$#submission submitted to the Brookhaven Protein Data Bank, April 1996 !$#cross-references PDB:1ZFD !$#contents annotation; conformation by (1)H-NMR, residues 577-608 REFERENCE A58624 !$#authors Nakaseko, Y.; Neuhaus, D.; Klug, A.; Rhodes, D. !$#journal J. Mol. Biol. (1992) 228:619-636 !$#title Adjacent zinc-finger motifs in multiple zinc-finger peptides !1from SWI5 form structurally independent, flexibly linked !1domains. !$#cross-references MUID:93085740; PMID:1453467 !$#contents annotation; conformation by (1)H-NMR REFERENCE A58623 !$#authors Neuhaus, D.; Nakaseko, Y.; Schwabe, J.W.R.; Klug, A. !$#journal J. Mol. Biol. (1992) 228:637-651 !$#title Solution structures of two zinc-finger domains from SWI5 !1obtained using two-dimensional (1)H nuclear magnetic !1resonance spectroscopy. A zinc-finger structure with a third !1strand of beta-sheet. !$#cross-references MUID:93085741; PMID:1453468 !$#contents annotation; conformation by (1)H-NMR COMMENT This protein activates the HO gene, which codes for an !1endonuclease responsible for the switch of mating type. GENETICS !$#gene SGD:SWI5; MIPS:YDR146c !'##cross-references SGD:S0002553; MIPS:YDR146c !$#map_position 4R CLASSIFICATION #superfamily transcription factor SWI5 KEYWORDS DNA binding; metalloprotein; transcription factor; zinc !1finger FEATURE !$550-574 #region zinc finger CCHH motif\ !$580-604 #region zinc finger CCHH motif\ !$609-632 #region zinc finger CCHC motif\ !$552,557,570,574 #binding_site zinc (Cys, Cys, His, His) #status !8experimental\ !$582,587,600,604 #binding_site zinc (Cys, Cys, His, His) #status !8experimental\ !$611,613,626,632 #binding_site zinc (Cys, Cys, His, Cys) #status !8experimental SUMMARY #length 709 #molecular-weight 79774 #checksum 1827 SEQUENCE /// ENTRY S39004 #type complete TITLE finger protein MSN2 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YM9532.O2c; protein YMR037c ORGANISM #formal_name Saccharomyces cerevisiae DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 21-Jul-2000 ACCESSIONS S39004; S52886; A48131 REFERENCE A48131 !$#authors Estruch, F.; Carlson, M. !$#journal Mol. Cell. Biol. (1993) 13:3872-3881 !$#title Two homologous zinc finger genes identified by multicopy !1suppression in a SNF1 protein kinase mutant of Saccharomyces !1cerevisiae. !$#cross-references MUID:93309420; PMID:8321194 !$#accession S39004 !'##molecule_type DNA !'##residues 1-704 ##label EST !'##cross-references EMBL:L08838; NID:g349594; PIDN:AAA34806.1; !1PID:g349595 REFERENCE S52885 !$#authors Odell, C.; Bowman, S. !$#submission submitted to the EMBL Data Library, February 1995 !$#accession S52886 !'##molecule_type DNA !'##residues 1-704 ##label ODE !'##cross-references EMBL:Z48502; NID:g695715; PIDN:CAA88403.1; !1PID:g695717; GSPDB:GN00013; MIPS:YMR037c GENETICS !$#gene SGD:MSN2; MIPS:YMR037c !'##cross-references SGD:S0004640; MIPS:YMR037c !$#map_position 13R CLASSIFICATION #superfamily finger protein MSN2 KEYWORDS DNA binding; nucleus; transcription regulation; zinc finger FEATURE !$649-665 #region zinc finger CCHH motif\ !$678-698 #region zinc finger CCHH motif SUMMARY #length 704 #molecular-weight 77860 #checksum 9259 SEQUENCE /// ENTRY S37884 #type complete TITLE finger protein MSN4 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YKL062w; protein YKL323; transcription factor homolog MSN4 ORGANISM #formal_name Saccharomyces cerevisiae DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 12-Nov-1999 ACCESSIONS S37884; S39005; S39187; S44532; B48131 REFERENCE S37872 !$#authors Rasmussen, S.; von Wettstein, D. !$#submission submitted to the Protein Sequence Database, March 1994 !$#accession S37884 !'##molecule_type DNA !'##residues 1-630 ##label RAS !'##cross-references EMBL:Z28062; NID:g486082; PIDN:CAA81899.1; !1PID:g486083; GSPDB:GN00011; MIPS:YKL062w !'##experimental_source strain S288C REFERENCE A48131 !$#authors Estruch, F.; Carlson, M. !$#journal Mol. Cell. Biol. (1993) 13:3872-3881 !$#title Two homologous zinc finger genes identified by multicopy !1suppression in a SNF1 protein kinase mutant of Saccharomyces !1cerevisiae. !$#cross-references MUID:93309420; PMID:8321194 !$#accession S39005 !'##molecule_type DNA !'##residues 1-630 ##label EST !'##cross-references EMBL:L08839; NID:g349592; PIDN:AAA34807.1; !1PID:g349593 !'##note sequence extracted from NCBI backbone (NCBIN:134621, !1NCBIP:134622) REFERENCE S39168 !$#authors Rasmussen, S.W. !$#submission submitted to the EMBL Data Library, November 1993 !$#accession S39187 !'##molecule_type DNA !'##residues 1-630 ##label RA2 !'##cross-references EMBL:X75781; NID:g433634; PIDN:CAA53421.1; !1PID:g433646 !'##experimental_source strain S288C REFERENCE S44521 !$#authors Rasmussen, S.W. !$#journal Yeast (1994) 10:63-68 !$#title Sequence of a 28.6 kb region of yeast chromosome XI includes !1the FBA1 and TOA2 genes, an open reading frame (ORF) similar !1to a translationally controlled tumour protein, one ORF !1containing motifs also found in plant storage proteins and !113 ORFs with weak or no homology to known proteins. !$#accession S44532 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-630 ##label RAW !'##cross-references EMBL:X75781; NID:g433634; PIDN:CAA53421.1; !1PID:g433646 !'##experimental_source strain S288C GENETICS !$#gene SGD:MSN4; MIPS:YKL062w !'##cross-references SGD:S0001545; MIPS:YKL062w !$#map_position 11L CLASSIFICATION #superfamily finger protein MSN2 KEYWORDS DNA binding; nucleus; transcription regulation; zinc finger FEATURE !$575-596 #region zinc finger CCHH motif\ !$604-624 #region zinc finger CCHH motif SUMMARY #length 630 #molecular-weight 69722 #checksum 7681 SEQUENCE /// ENTRY TWBYM1 #type complete TITLE transcription factor MTF2 precursor, mitochondrial - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES COXI-specific mRNA splicing-enhancing protein; mitochondrial protein translation regulator; protein D2705; protein YDL044c; transcription factor NAM1 ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 21-Jul-2000 ACCESSIONS JV0015; S25414; S17240; S67577 REFERENCE JV0015 !$#authors Asher, E.B.; Groudinsky, O.; Dujardin, G.; Altamura, N.; !1Kermorgant, M.; Slonimski, P.P. !$#journal Mol. Gen. Genet. (1989) 215:517-528 !$#title Novel class of nuclear genes involved in both mRNA splicing !1and protein synthesis in Saccharomyces cerevisiae !1mitochondria. !$#cross-references MUID:89218962; PMID:2651895 !$#accession JV0015 !'##molecule_type DNA !'##residues 1-440 ##label ASH !'##cross-references EMBL:X14719; NID:g2950; PIDN:CAA32845.1; PID:g2951 REFERENCE S25414 !$#authors Lisowsky, T. !$#journal Mol. Gen. Genet. (1990) 220:186-190 !$#title Molecular analysis of the mitochondrial transcription factor !1mtf2 of Saccharomyces cerevisiae. !$#cross-references MUID:90220489; PMID:2183001 !$#accession S25414 !'##molecule_type DNA !'##residues 1-186,'P',188-440 ##label LIS REFERENCE S05891 !$#authors Shore, D.; Squire, M.; Nasmyth, K.A. !$#journal EMBO J. (1984) 3:2817-2823 !$#title Characterization of two genes required for the !1position-effect control of yeast mating-type genes. !$#cross-references MUID:85126876; PMID:6098447 !$#accession S17240 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-111 ##label SHO !'##cross-references EMBL:X01419 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1984 REFERENCE S67560 !$#authors Paulin, L.; Saren, A.M.; Laamanen, P. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67577 !'##molecule_type DNA !'##residues 1-440 ##label PAU !'##cross-references EMBL:Z74092; NID:g1431031; PIDN:CAA98603.1; !1PID:g1431032; GSPDB:GN00004; MIPS:YDL044c !'##experimental_source strain S288C GENETICS !$#gene SGD:MTF2; NAM1; MIPS:YDL044c !'##cross-references SGD:S0002202; MIPS:YDL044c !$#map_position 4L !$#genome nuclear CLASSIFICATION #superfamily transcription factor NAM1 KEYWORDS mitochondrion; transcription factor FEATURE !$1-15 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$16-440 #product transcription factor NAM1, mitochondrial !8#status predicted #label MAT SUMMARY #length 440 #molecular-weight 51192 #checksum 7954 SEQUENCE /// ENTRY TWFF #type complete TITLE transcription factor Krueppel - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES Kruppel segmentation protein ORGANISM #formal_name Drosophila melanogaster DATE 30-Jun-1989 #sequence_revision 21-Nov-1997 #text_change 10-Sep-1999 ACCESSIONS A24566; B46363 REFERENCE A24566 !$#authors Rosenberg, U.B.; Schroeder, C.; Preiss, A.; Kienlin, A.; !1Cote, S.; Riede, I.; Jaeckle, H. !$#journal Nature (1986) 319:336-339 !$#title Structural homology of the product of the Drosophila !1Krueppel gene with Xenopus transcription factor IIIA. !$#accession A24566 !'##molecule_type DNA; mRNA !'##residues 1-255,'D',257-466 ##label ROS !'##cross-references GB:X03414; NID:g8158; PIDN:CAA27148.1; PID:g8159 !'##note it is uncertain whether Met-1 or Met-32 is the initiator; !1181-His, 182-Thr, 210-Ile, 256-His, 397-Gly, 429-Ala, and !1451-Phe were also found REFERENCE A46363 !$#authors Sommer, R.J.; Retzlaff, M.; Goerlich, K.; Sander, K.; Tautz, !1D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:10782-10786 !$#title Evolutionary conservation pattern of zinc-finger domains of !1Drosophila segmentation genes. !$#cross-references MUID:93066327; PMID:1438276 !$#accession B46363 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type DNA !'##residues 240-314 ##label SOM !'##note sequence extracted from NCBI backbone (NCBIP:118692) COMMENT This protein belongs to the gap class of segmentation !1proteins. COMMENT This protein is expressed primarily in the !1blastoderm-gastrulation stage and is involved in the !1segmentation of the embryo and in the differentiation of the !1Malpighian tubules. COMMENT Mutations in this protein result in varying degrees of !1segment deletions in the thoracic and abdominal regions. !1Strong Krueppel mutants lack all thoracic and five anterior !1abdominal segments with portions of the remaining posterior !1abdominal segments being present as a mirror-image !1duplication. GENETICS !$#gene FlyBase:Kr !'##cross-references FlyBase:FBgn0001325 !$#map_position 2R (60F3) !$#introns 13/1 CLASSIFICATION #superfamily transcription factor Krueppel KEYWORDS DNA binding; duplication; nucleus; segmentation; !1transcription factor; zinc finger FEATURE !$222-244 #region zinc finger CCHH motif\ !$250-272 #region zinc finger CCHH motif\ !$278-300 #region zinc finger CCHH motif\ !$306-328 #region zinc finger CCHH motif\ !$334-352 #region incomplete zinc finger SUMMARY #length 466 #molecular-weight 50820 #checksum 5796 SEQUENCE /// ENTRY A28123 #type complete TITLE transcription factor HAP3 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YBL021c; protein YBL0441 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A28123; S43937; S45755 REFERENCE A93110 !$#authors Hahn, S.; Pinkham, J.; Wei, R.; Miller, R.; Guarente, L. !$#journal Mol. Cell. Biol. (1988) 8:655-663 !$#title The HAP3 regulatory locus of Saccharomyces cerevisiae !1encodes divergent overlapping transcripts. !$#cross-references MUID:88174707; PMID:2832732 !$#accession A28123 !'##molecule_type DNA !'##residues 1-144 ##label HAH !'##cross-references EMBL:M20318; NID:g577522; PIDN:AAA53538.1; !1PID:g171643 REFERENCE S43937 !$#authors van Dyck, L.; Pearce, D.A.; Sherman, F. !$#journal J. Biol. Chem. (1994) 269:238-242 !$#title PIM1 encodes a mitochondrial ATP-dependent protease that is !1required for mitochondrial function in the yeast !1Saccharomyces cerevisiae. !$#cross-references MUID:94103216; PMID:8276800 !$#accession S43937 !'##molecule_type DNA !'##residues 1-144 ##label VAN !'##cross-references EMBL:X74544; NID:g453234; PIDN:CAA52633.1; !1PID:g453235 REFERENCE S45745 !$#authors Goffeau, A.; Jonniaux, J.L.; Purnelle, B.; Skala, J.; de !1Wergifosse, P.; van Dyck, L. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S45755 !'##molecule_type DNA !'##residues 1-144 ##label GOF !'##cross-references EMBL:Z35782; NID:g536016; PIDN:CAA84840.1; !1PID:g536017; GSPDB:GN00002; MIPS:YBL021c GENETICS !$#gene SGD:HAP3; MIPS:YBL021c !'##cross-references SGD:S0000117; MIPS:YBL021c !$#map_position 2L CLASSIFICATION #superfamily transcription factor HAP3 KEYWORDS DNA binding; nucleus; transcription regulation FEATURE !$36-125 #domain DNA binding #status predicted #label DNA SUMMARY #length 144 #molecular-weight 16154 #checksum 6718 SEQUENCE /// ENTRY S06206 #type complete TITLE grainy-head protein - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES DNA-binding protein elf-1; element I-binding activity; transcription factor NTF1 ORGANISM #formal_name Drosophila melanogaster DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 21-Jul-2000 ACCESSIONS S06206; A33471 REFERENCE S06206 !$#authors Bray, S.J.; Burke, B.; Brown, N.H.; Hirsh, J. !$#journal Genes Dev. (1989) 3:1130-1145 !$#title Embryonic expression pattern of a family of Drosophila !1proteins that interact with a central nervous system !1regulatory element. !$#cross-references MUID:90006735; PMID:2792757 !$#accession S06206 !'##molecule_type mRNA !'##residues 1-1063 ##label BRA !'##cross-references EMBL:X15657; NID:g7938; PIDN:CAA33692.1; PID:g7939 REFERENCE A33471 !$#authors Dynlacht, B.D.; Attardi, L.D.; Admon, A.; Freeman, M.; !1Tjian, R. !$#journal Genes Dev. (1989) 3:1677-1688 !$#title Functional analysis of NTF-1, a developmentally regulated !1Drosophila transcription factor that binds neuronal cis !1elements. !$#cross-references MUID:90108664; PMID:2606344 !$#accession A33471 !'##status preliminary; nucleic acid sequence not shown; not compared !1with conceptual translation !'##molecule_type mRNA !'##residues 198-261,'P',263-728,'C',730-735,'NA',738-862,894-1063 !1##label DYN GENETICS !$#gene FlyBase:grh !'##cross-references FlyBase:FBgn0004586 CLASSIFICATION #superfamily Drosophila grainy-head protein KEYWORDS DNA binding; transcription regulation SUMMARY #length 1063 #molecular-weight 116153 #checksum 9975 SEQUENCE /// ENTRY TWECNG #type complete TITLE transcription antitermination factor nusG - Escherichia coli (strain K-12) ALTERNATE_NAMES transcription elongation factor nusG ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 01-Mar-2002 ACCESSIONS B35139; A42154; A65205 REFERENCE A35139 !$#authors Downing, W.L.; Sullivan, S.L.; Gottesman, M.E.; Dennis, P.P. !$#journal J. Bacteriol. (1990) 172:1621-1627 !$#title Sequence and transcriptional pattern of the essential !1Escherichia coli secE-nusG operon. !$#cross-references MUID:90170882; PMID:2137819 !$#accession B35139 !'##molecule_type DNA !'##residues 1-181 ##label DOW !'##cross-references GB:M30610; NID:g147798; PIDN:AAA24622.1; !1PID:g147801 REFERENCE A42154 !$#authors Li, J.; Horwitz, R.; McCracken, S.; Greenblatt, J. !$#journal J. Biol. Chem. (1992) 267:6012-6019 !$#title NusG, a new Escherichia coli elongation factor involved in !1transcriptional antitermination by the N protein of phage !1lambda. !$#cross-references MUID:92210569; PMID:1532577 !$#accession A42154 !'##molecule_type protein !'##residues 'X',3-12 ##label LIA REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65205 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-181 ##label BLAT !'##cross-references GB:AE000472; GB:U00096; NID:g2367333; !1PIDN:AAC76956.1; PID:g1790414; UWGP:b3982 !'##experimental_source strain K-12, substrain MG1655 COMMENT This protein is involved in the transcriptional !1antitermination process. GENETICS !$#gene nusG !$#map_position 90 min CLASSIFICATION #superfamily transcription antitermination factor nusG KEYWORDS transcription antitermination; transcription factor SUMMARY #length 181 #molecular-weight 20531 #checksum 4464 SEQUENCE /// ENTRY TWHU2D #type complete TITLE transcription initiation factor IID - human ALTERNATE_NAMES TATA-binding protein ORGANISM #formal_name Homo sapiens #common_name man DATE 20-Jul-1990 #sequence_revision 19-May-1995 #text_change 18-Feb-2000 ACCESSIONS A34830; A34831; S10944; I60128 REFERENCE A34830 !$#authors Peterson, M.G.; Tanese, N.; Pugh, B.F.; Tjian, R. !$#journal Science (1990) 248:1625-1630 !$#title Functional domains and upstream activation properties of !1cloned human TATA binding protein. !$#cross-references MUID:90302006; PMID:2363050 !$#accession A34830 !'##molecule_type mRNA !'##residues 1-339 ##label PET !'##cross-references GB:M55654; NID:g339491; PIDN:AAA36731.1; !1PID:g339492 REFERENCE A34831 !$#authors Kao, C.C.; Lieberman, P.M.; Schmidt, M.C.; Zhou, Q.; Pei, !1R.; Berk, A.J. !$#journal Science (1990) 248:1646-1649 !$#title Cloning of a transcriptionally active human TATA binding !1factor. !$#cross-references MUID:90302010; PMID:2194289 !$#accession A34831 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-17,'N',19-186,'R',188-339 ##label KAO REFERENCE S10944 !$#authors Hoffmann, A.; Sinn, E.; Yamamoto, T.; Wang, J.; Roy, A.; !1Horikoshi, M.; Roeder, R.G. !$#journal Nature (1990) 346:387-390 !$#title Highly conserved core domain and unique N terminus with !1presumptive regulatory motifs in a human TATA factor !1(TFIID). !$#cross-references MUID:90326195; PMID:2374612 !$#accession S10944 !'##molecule_type mRNA !'##residues 1-91,96-339 ##label HOF !'##cross-references EMBL:X54993; NID:g37065; PIDN:CAA38736.1; !1PID:g37066 REFERENCE I60128 !$#authors Kao, C.; Lieberman, P.; Schmidt, M.; Zhou, Q.; Pei, R.; !1Berk, A.J. !$#journal Science (1990) 248:1626 !$#title Cloning of the human TATA binding factor: Expression of a !1transcriptionally active TFIID protein. !$#accession I60128 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-186,'R',188-299,'MIKPR',300-339 ##label RES !'##cross-references GB:M34960; NID:g339493; PID:g339494 GENETICS !$#gene GDB:TBP; GTF2D1 !'##cross-references GDB:138768; OMIM:600075 !$#map_position 6q27-6q27 CLASSIFICATION #superfamily human transcription initiation factor IID KEYWORDS alternative splicing; DNA binding; nucleus; transcription !1initiation FEATURE !$55-95 #region glutamine-rich SUMMARY #length 339 #molecular-weight 37698 #checksum 4870 SEQUENCE /// ENTRY S34437 #type complete TITLE transcription initiation factor IID - mouse ALTERNATE_NAMES TATA-binding protein ORGANISM #formal_name Mus musculus #common_name house mouse DATE 18-Feb-2000 #sequence_revision 18-Feb-2000 #text_change 16-Jun-2000 ACCESSIONS S34437; PC4189 REFERENCE S34437 !$#authors Tamura, T.A.; Sumita, K.; Fujino, I.; Aoyama, A.; Horikoshi, !1M.; Hoffmann, A.; Roeder, R.G.; Muramatsu, M.; Mikoshiba, K. !$#journal Nucleic Acids Res. (1991) 19:3861-3865 !$#title Striking homology of the 'variable' N-terminal as well as !1the 'conserved core' domains of the mouse and human !1TATA-factors (TFIID). !$#cross-references MUID:91319543; PMID:1861978 !$#accession S34437 !'##molecule_type mRNA !'##residues 1-316 ##label TAM !'##cross-references EMBL:D01034; NID:g220611; PIDN:BAA00840.1; !1PID:g220612 REFERENCE PC4189 !$#authors Ohbayashi, T.; Schmidt, E.E.; Makino, Y.; Kishimoto, T.; !1Nabeshima, Y.; Muramatsu, M.; Tamura, T. !$#journal Biochem. Biophys. Res. Commun. (1996) 225:275-280 !$#title Promoter structure of the mouse TATA-binding protein (TBP) !1gene. !$#cross-references MUID:96332441; PMID:8769130 !$#accession PC4189 !'##molecule_type DNA !'##residues 1-36 ##label OHB COMMENT This protein is required by all classes of nuclear RNA !1polymerases. GENETICS !$#gene tbp !$#introns 18/3 CLASSIFICATION #superfamily human transcription initiation factor IID KEYWORDS alternative splicing; DNA binding; nucleus; transcription !1initiation FEATURE !$55-70 #region glutamine-rich SUMMARY #length 316 #molecular-weight 34709 #checksum 6006 SEQUENCE /// ENTRY JC5513 #type complete TITLE transcription initiation factor IID - chicken ALTERNATE_NAMES TATA-binding protein ORGANISM #formal_name Gallus gallus #common_name chicken DATE 18-Feb-2000 #sequence_revision 18-Feb-2000 #text_change 16-Jun-2000 ACCESSIONS JC5513 REFERENCE JC5513 !$#authors Yamauchi, J.; Sugita, A.; Fujiwara, M.; Suzuki, K.; !1Matsumoto, H.; Yamazaki, T.; Ninomiya, Y.; Ono, T.; !1Hasegawa, T.; Masushige, S.; Muramatsu, M.; Tamura, T.; !1Kato, S. !$#journal Biochem. Biophys. Res. Commun. (1997) 234:406-411 !$#title Two forms of avian (chicken) TATA-binding protein mRNA !1generated by alternative polyadenylation. !$#cross-references MUID:97320433; PMID:9177284 !$#accession JC5513 !'##molecule_type mRNA !'##residues 1-302 ##label YAM !'##cross-references DDBJ:D83127; NID:g1183016; PIDN:BAA20297.1; !1PID:g2145310 !'##note the authors translated the codon CCT for residue 17 as Thr COMMENT This protein recognizes to promoter sequences, commits the !1formation of pre-initiation complexes, and allows !1transcription initiation along with various basal !1transcription factors and RNA polymerase I, II and III. CLASSIFICATION #superfamily human transcription initiation factor IID KEYWORDS DNA binding; nucleus; transcription initiation SUMMARY #length 302 #molecular-weight 33134 #checksum 1331 SEQUENCE /// ENTRY JC4059 #type complete TITLE transcription initiation factor IID - Indian green tree viper ALTERNATE_NAMES TATA-binding protein ORGANISM #formal_name Trimeresurus gramineus #common_name Indian green tree viper DATE 18-Feb-2000 #sequence_revision 18-Feb-2000 #text_change 16-Jun-2000 ACCESSIONS JC4059 REFERENCE JC4059 !$#authors Nakashima, K.; Nobuhisa, I.; Deshimaru, M.; Ogawa, T.; !1Shimohigashi, Y.; Fukumaki, Y.; Hattori, M.; Sakaki, Y.; !1Hattori, S.; Ohno, M. !$#journal Gene (1995) 152:209-213 !$#title Structures of genes encoding TATA box-binding proteins from !1Trimeresurus gramineus and T. flavoviridis snakes. !$#cross-references MUID:95137390; PMID:7835702 !$#accession JC4059 !'##molecule_type mRNA !'##residues 1-302 ##label NAK !'##cross-references DDBJ:D31776; NID:g1483196; PIDN:BAA06554.1; !1PID:g808897 COMMENT This protein recognizes and binds the TATA box and is !1required by RNA polymerase for transcription. GENETICS !$#gene tbp CLASSIFICATION #superfamily human transcription initiation factor IID KEYWORDS DNA binding; nucleus; transcription initiation SUMMARY #length 302 #molecular-weight 33142 #checksum 869 SEQUENCE /// ENTRY I51648 #type complete TITLE transcription initiation factor IID - African clawed frog ALTERNATE_NAMES TATA-binding protein ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 18-Feb-2000 #sequence_revision 18-Feb-2000 #text_change 03-Mar-2000 ACCESSIONS I51648; S68859; S26292 REFERENCE I51648 !$#authors Hashimoto, S.; Fujita, H.; Hasegawa, S.; Roeder, R.G.; !1Horikoshi, M. !$#journal Nucleic Acids Res. (1992) 20:3788 !$#title Conserved structural motifs within the N-terminal domain of !1TFIID tau from Xenopus, mouse and human. !$#cross-references MUID:92350691; PMID:1641350 !$#accession I51648 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-297 ##label HAS !'##cross-references EMBL:X66033; NID:g65148; PIDN:CAA46832.1; !1PID:g65149 !'##note only a part of the translation is shown REFERENCE S68859 !$#authors Labhart, P. !$#journal FEBS Lett. (1996) 386:110-114 !$#title Phosphorylation of the N-terminal domain of Xenopus TATA-box !1binding protein by DNA-dependent protein kinase depends on !1the C-terminal core domain. !$#cross-references MUID:96228045; PMID:8647263 !$#accession S68859 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type mRNA !'##residues 1-54,'R',56-176,'I',178-297 ##label LAB !'##note only a list of differences from sequence S26292 is shown in !1this paper GENETICS !$#gene TFIIDtau CLASSIFICATION #superfamily human transcription initiation factor IID KEYWORDS DNA binding; nucleus; transcription initiation SUMMARY #length 297 #molecular-weight 32703 #checksum 2564 SEQUENCE /// ENTRY A35615 #type complete TITLE transcription initiation factor IID - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES TATA box-binding protein ORGANISM #formal_name Drosophila melanogaster DATE 18-Feb-2000 #sequence_revision 18-Feb-2000 #text_change 18-Feb-2000 ACCESSIONS A35615; A38416; JC4056 REFERENCE A35615 !$#authors Hoey, T.; Dynlacht, B.D.; Peterson, M.G.; Pugh, B.F.; Tjian, !1R. !$#journal Cell (1990) 61:1179-1186 !$#title Isolation and characterization of the Drosophila gene !1encoding the TATA box binding protein, TFIID. !$#cross-references MUID:90304877; PMID:2194666 !$#accession A35615 !'##molecule_type mRNA !'##residues 1-353 ##label HOE !'##cross-references GB:M38082; NID:g158541; PIDN:AAA28931.1; !1PID:g158542 REFERENCE A38416 !$#authors Muhich, M.L.; Iida, C.T.; Horikoshi, M.; Roeder, R.G.; !1Parker, C.S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:9148-9152 !$#title cDNA clone encoding Drosophila transcription factor TFIID. !$#cross-references MUID:91067664; PMID:2123550 !$#accession A38416 !'##molecule_type mRNA !'##residues 1-353 ##label MUH !'##cross-references GB:M38388; NID:g158531; PIDN:AAA28926.1; !1PID:g158532 REFERENCE JC4055 !$#authors Lira-DeVito, L.M.; Burke, T.W.; Kadonaga, J.T. !$#journal Gene (1995) 153:203-207 !$#title Structure of the genes encoding transcription factor IIB and !1TATA box-binding protein from Drosophila melanogaster. !$#cross-references MUID:95180719; PMID:7875589 !$#accession JC4056 !'##molecule_type DNA !'##residues 1-353 ##label LIR !'##cross-references GB:U11718; NID:g515664; PIDN:AAA68629.1; !1PID:g515665 GENETICS !$#gene FlyBase:Tbp !'##cross-references FlyBase:FBgn0003687 CLASSIFICATION #superfamily Drosophila transcription initiation factor IID KEYWORDS DNA binding; nucleus; transcription initiation SUMMARY #length 353 #molecular-weight 38451 #checksum 4732 SEQUENCE /// ENTRY TWPO2D #type complete TITLE transcription initiation factor IID - potato ALTERNATE_NAMES TATA-binding protein ORGANISM #formal_name Solanum tuberosum #common_name potato DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jul-1999 ACCESSIONS S22476; S18050 REFERENCE S22476 !$#authors Holdsworth, M.J.; Grierson, C.; Schuch, W.; Bevan, M. !$#journal Plant Mol. Biol. (1992) 19:455-464 !$#title DNA-binding properties of cloned TATA-binding protein from !1potato tubers. !$#cross-references MUID:92322977; PMID:1377967 !$#accession S22476 !'##molecule_type mRNA !'##residues 1-200 ##label HOL !'##cross-references EMBL:X62494; NID:g21580; PIDN:CAA44360.1; !1PID:g21581 CLASSIFICATION #superfamily transcription initiation factor IID KEYWORDS DNA binding; transcription initiation SUMMARY #length 200 #molecular-weight 22311 #checksum 9110 SEQUENCE /// ENTRY A40262 #type complete TITLE transcription initiation factor IID 250K chain splice form 1 - human ALTERNATE_NAMES 210K nuclear DNA-binding cell cycle gene 1 protein (CCG1); TATA-binding protein (TBP) associated factor II-250 CONTAINS transcription initiation factor IID 250K chain splice form 2 ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A40262; S03005; S00830; S32352; S32353 REFERENCE A40262 !$#authors Sekiguchi, T.; Nohiro, Y.; Nakamura, Y.; Hisamoto, N.; !1Nishimoto, T. !$#journal Mol. Cell. Biol. (1991) 11:3317-3325 !$#title The human CCG1 gene, essential for progression of the G-1 !1phase, encodes a 210-kilodalton nuclear DNA-binding protein. !$#cross-references MUID:91246200; PMID:2038334 !$#accession A40262 !'##molecule_type mRNA !'##residues 1-177,199-1893 ##label SEK !'##cross-references GB:D90359; NID:g559319; PIDN:BAA14374.1; !1PID:g219528 !'##note nucleotide sequence not complete REFERENCE S03005 !$#authors Sekiguchi, T.; Miyata, T.; Nishimoto, T. !$#submission submitted to the EMBL Data Library, February 1988 !$#accession S03005 !'##molecule_type mRNA !'##residues 'MYR',60-177,199-1604,'DNECSSKANDIVCLIQYCSSQIEELRF' ##label !1SE5 !'##cross-references EMBL:X07024; NID:g29732; PIDN:CAA30073.1; !1PID:g29733 !'##note this sequence has been revised in reference A40262 REFERENCE S00830 !$#authors Sekiguchi, T.; Miyata, T.; Nishimoto, T. !$#journal EMBO J. (1988) 7:1683-1687 !$#title Molecular cloning of the cDNA of human X chromosomal gene !1(CCG1) which complements the temperature-sensitive G1 !1mutants, tsBN462 and ts13, of the BHK cell line. !$#cross-references MUID:89005056; PMID:3169001 !$#accession S00830 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1372-1379;1386-1604,'DNE','CSSKANDIVCLIQYCSSQIEELRF' !1##label SE6 !'##cross-references EMBL:X07024 REFERENCE S32352 !$#authors Ruppert, S.; Wang, E.H.; Tjian, R. !$#journal Nature (1993) 362:175-179 !$#title Cloning and expression of human TAF(II)250: a TBP-associated !1factor implicated in cell-cycle regulation. !$#cross-references MUID:93196704; PMID:7680771 !$#accession S32352 !'##status preliminary !'##molecule_type mRNA !'##residues 178-198 ##label RUP REFERENCE S32353 !$#authors Hisatake, K.; Hasegawa, S.; Takada, R.; Nakatani, Y.; !1Horikoshi, M.; Roeder, R.G. !$#journal Nature (1993) 362:179-181 !$#title The p250 subunit of native TATA box-binding factor TFIID is !1the cell-cycle regulatory protein CCG1. !$#cross-references MUID:93196705; PMID:8450888 !$#accession S32353 !'##status preliminary !'##molecule_type protein !'##residues 'P';587-595;1009-1022;1351-1355;1357-1360 ##label HIS !'##note 1351-Val, 1353-Lys, and 1354-Glu were also found GENETICS !$#gene GDB:TAF2A; CCG1; CCGS; NSCL2; TAFII250 !'##cross-references GDB:120573; OMIM:313650 !$#map_position Xq13.1-Xq13.1 CLASSIFICATION #superfamily transcription initiation factor IID 250K chain; !1bromodomain homology; HMG box homology KEYWORDS alternative splicing; cell cycle control; DNA binding; !1duplication; phosphoprotein; transcription initiation FEATURE !$1-1893 #product transcription initiation factor IID 250K !8chain splice form 1 #status predicted #label MAT\ !$1-177,199-1893 #product transcription initiation factor IID 250K !8chain splice form 2 #status predicted #label MA2\ !$1216-1295 #domain HMG box homology #label HMG1\ !$1372-1379 #region nuclear location signal\ !$1426-1481 #domain bromodomain homology #label BRO1\ !$1549-1604 #domain bromodomain homology #label BRO2\ !$137,1740,1751,1847, !$1871 #binding_site phosphate (Ser) (covalent) (by casein !8kinase II) #status predicted\ !$678,1054,1684 #binding_site phosphate (Ser) (covalent) (by !8calmodulin-dependent kinase) #status predicted\ !$1020,1361 #binding_site phosphate (Ser) (covalent) (by !8cAMP-dependent kinase) #status predicted\ !$1381,1400 #binding_site phosphate (Thr) (covalent) (by !8calmodulin-dependent kinase) #status predicted SUMMARY #length 1893 #molecular-weight 214712 #checksum 9673 SEQUENCE /// ENTRY I48155 #type complete TITLE transcription initiation factor IID 250K chain splice form 2 - golden hamster ALTERNATE_NAMES 210K nuclear DNA-binding cell cycle gene 1 protein (CCG1); CCG1; TATA-binding protein (TBP) associated factor II-250 ORGANISM #formal_name Mesocricetus auratus #common_name golden hamster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 15-Oct-1999 ACCESSIONS I48155 REFERENCE I48155 !$#authors Hayashida, T.; Sekiguchi, T.; Noguchi, E.; Sunamoto, H.; !1Ohba, T.; Nishimoto, T. !$#journal Gene (1994) 141:267-270 !$#title The CCG1/TAFII250 gene is mutated in thermosensitive G1 !1mutants of the BHK21 cell line derived from goldenhamster. !$#cross-references MUID:94215915; PMID:8163200 !$#accession I48155 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-1865 ##label RES !'##cross-references GB:D26114; NID:g439485; PIDN:BAA05110.1; !1PID:g474971 CLASSIFICATION #superfamily transcription initiation factor IID 250K chain; !1bromodomain homology; HMG box homology KEYWORDS alternative splicing; cell cycle control; DNA binding; !1duplication; phosphoprotein; transcription initiation FEATURE !$1190-1269 #domain HMG box homology #label HMG1\ !$1346-1353 #region nuclear location signal\ !$1400-1455 #domain bromodomain homology #label BRO1\ !$1523-1578 #domain bromodomain homology #label BRO2\ !$131,1714,1725,1821, !$1843 #binding_site phosphate (Ser) (covalent) (by casein !8kinase II) #status predicted\ !$652,1028,1658 #binding_site phosphate (Ser) (covalent) (by !8calmodulin-dependent kinase) #status predicted\ !$994,1335 #binding_site phosphate (Ser) (covalent) (by !8cAMP-dependent kinase) #status predicted\ !$1355,1374 #binding_site phosphate (Thr) (covalent) (by !8calmodulin-dependent kinase) #status predicted SUMMARY #length 1865 #molecular-weight 211866 #checksum 9243 SEQUENCE /// ENTRY S71788 #type complete TITLE P/CAF protein - human ALTERNATE_NAMES CREBBP-associated factor ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 29-Sep-1999 ACCESSIONS S71788 REFERENCE S71788 !$#authors Yang, X.J.; Ogryzko, V.V.; Nishikawa, J.; Howard, B.H.; !1Nakatani, Y. !$#journal Nature (1996) 382:319-324 !$#title A p300/CBP-associated factor that competes with the !1adenoviral oncoprotein E1A. !$#cross-references MUID:96300317; PMID:8684459 !$#accession S71788 !'##status preliminary; nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-832 ##label YAN !'##cross-references EMBL:U57317; NID:g1491936; PIDN:AAC50890.1; !1PID:g1491937 GENETICS !$#gene GDB:CAF !'##cross-references GDB:9864231; OMIM:602303 !$#map_position 3p24-3p24 CLASSIFICATION #superfamily human P/CAF protein; bromodomain homology FEATURE !$748-803 #domain bromodomain homology #label BRO1 SUMMARY #length 832 #molecular-weight 92926 #checksum 8709 SEQUENCE /// ENTRY S71789 #type complete TITLE GCN5 protein - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 29-Sep-1999 ACCESSIONS S71789 REFERENCE S71788 !$#authors Yang, X.J.; Ogryzko, V.V.; Nishikawa, J.; Howard, B.H.; !1Nakatani, Y. !$#journal Nature (1996) 382:319-324 !$#title A p300/CBP-associated factor that competes with the !1adenoviral oncoprotein E1A. !$#cross-references MUID:96300317; PMID:8684459 !$#accession S71789 !'##status preliminary; nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-476 ##label YAN !'##cross-references EMBL:U57316; NID:g1491934; PIDN:AAC50641.1; !1PID:g1491935 GENETICS !$#gene GDB:GCN5L2; hGCN5 !'##cross-references GDB:5195863; OMIM:602301 !$#map_position 17q12-17q21 CLASSIFICATION #superfamily transcription factor GCN5; bromodomain homology FEATURE !$392-447 #domain bromodomain homology #label BRO SUMMARY #length 476 #molecular-weight 54065 #checksum 431 SEQUENCE /// ENTRY S28051 #type complete TITLE transcription factor GCN5 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein G9145; protein YGR252w; transcription activator GCN5 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S28051; S64584 REFERENCE S28051 !$#authors Georgakopoulos, T.; Thireos, G. !$#journal EMBO J. (1992) 11:4145-4152 !$#title Two distinct yeast transcriptional activators require the !1function of the GCN5 protein to promote normal levels of !1transcription. !$#cross-references MUID:93011009; PMID:1396595 !$#accession S28051 !'##molecule_type DNA !'##residues 1-439 ##label GEO !'##cross-references EMBL:X68628; NID:g3735; PIDN:CAA48602.1; PID:g3736 REFERENCE S64577 !$#authors Agostoni Carbone, M.L.; Panzeri, L.; Melchioretto, P.; !1Carignani, G.; Feroli, F.; Frontali, L.; Mazzoni, C.; !1Rinaldi, T.; Ruzzi, M. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64584 !'##molecule_type DNA !'##residues 1-439 ##label AGO !'##cross-references EMBL:Z73037; NID:g1323457; PID:g1323458; !1GSPDB:GN00007; MIPS:YGR252w !'##experimental_source strain S288C GENETICS !$#gene SGD:GCN5; ADA4; MIPS:YGR252w !'##cross-references SGD:S0003484; MIPS:YGR252w !$#map_position 7R CLASSIFICATION #superfamily transcription factor GCN5; bromodomain homology KEYWORDS DNA binding; nucleus; transcription regulation FEATURE !$352-407 #domain bromodomain homology #label BRO SUMMARY #length 439 #molecular-weight 51069 #checksum 2113 SEQUENCE /// ENTRY TWHU2B #type complete TITLE transcription initiation factor IIB [validated] - human ALTERNATE_NAMES S300-II factor; TFIIB ORGANISM #formal_name Homo sapiens #common_name man DATE 04-Dec-1992 #sequence_revision 24-May-1996 #text_change 26-May-2000 ACCESSIONS S17654; S24672; A43393; A56407 REFERENCE S17654 !$#authors Ha, I.; Lane, W.S.; Reinberg, D. !$#journal Nature (1991) 352:689-695 !$#title Cloning of a human gene encoding the general transcription !1initiation factor IIB. !$#cross-references MUID:91342994; PMID:1876184 !$#accession S17654 !'##molecule_type mRNA !'##residues 1-316 ##label HAI !'##cross-references EMBL:X59268; NID:g37057; PIDN:CAA41958.1; !1PID:g37058 !$#accession S24672 !'##molecule_type protein !'##residues 101-119;150-178;239-293 ##label HA2 REFERENCE A43393 !$#authors Ing, N.H.; Beekman, J.M.; Tsai, S.Y.; Tsai, M.J.; O'Malley, !1B.W. !$#journal J. Biol. Chem. (1992) 267:17617-17623 !$#title Members of the steroid hormone receptor superfamily interact !1with TFIIB (S300-II). !$#cross-references MUID:92388108; PMID:1517211 !$#accession A43393 !'##molecule_type mRNA !'##residues 6-316 ##label ING !'##cross-references GB:S44184; NID:g254933; PIDN:AAB23144.1; !1PID:g254934 !'##note sequence extracted from NCBI backbone (NCBIN:112737, !1NCBIP:112738) !'##note parts of this sequence were confirmed by protein sequencing REFERENCE A56407 !$#authors Malik, S.; Hisatake, K.; Sumimoto, H.; Horikoshi, M.; !1Roeder, R.G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:9553-9557 !$#title Sequence of general transcription factor TFIIB and !1relationships to other initiation factors. !$#cross-references MUID:92052130; PMID:1946368 !$#accession A56407 !'##molecule_type mRNA !'##residues 1-75,'N',77-316 ##label MAL !'##cross-references GB:M76766 !'##note parts of this sequence were confirmed by peptide sequencing; !176-Ser was also found REFERENCE A57980 !$#authors Nikolov, D.B.; Chen, H.; Halay, E.D.; Usheva, A.A.; !1Hisatake, K.; Lee, D.K.; Roeder, R.G.; Burley, S.K. !$#journal Nature (1995) 377:119-128 !$#title Crystal structure of a TFIIB-TBP-TATA-element ternary !1complex. !$#cross-references MUID:95405464; PMID:7675079 !$#contents annotation; X-ray crystallography, 2.7 angstroms, residues !1112-316 GENETICS !$#gene GDB:GTF2B !'##cross-references GDB:128734; OMIM:189963 !$#map_position 1p22-1p22 COMPLEX sequential heterotrimer with factor IIA and factor IID on !1DNA [validated, MUID:95405464]; consequent binding of !1activated RNA polymerase II complex FUNCTION !$#description binds to a preinitiation complex of DNA (TATA box or other !1class II promoter motif), factor IID and factor IIA; permits !1the binding of activated RNA polymerase II complex !1[validated, MUID:93296192] !$#pathway transcription initiation CLASSIFICATION #superfamily transcription initiation factor IIB; !1transcription initiation factor IIB homology KEYWORDS DNA binding; duplication; phosphoprotein; transcription !1initiation; zinc finger FEATURE !$2-315 #product transcription initiation factor IIB #status !8predicted #label MAT\ !$14-294 #domain transcription initiation factor IIB homology !8#label TF2B\ !$15-36 #region zinc finger CHCC motif\ !$117-199 #domain five helix repeat #status experimental #label !8FH1\ !$121-198 #region duplication\ !$211-293 #domain five helix repeat #status experimental #label !8FH2\ !$215-292 #region duplication\ !$108 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 316 #molecular-weight 34832 #checksum 4175 SEQUENCE /// ENTRY S26299 #type complete TITLE transcription initiation factor IIB - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S26299 REFERENCE S26299 !$#authors Tsuboi, A.; Conger, K.; Garrett, K.P.; Conaway, R.C.; !1Conaway, J.W.; Arai, N. !$#journal Nucleic Acids Res. (1992) 20:3250 !$#title RNA polymerase II initiation factor alpha from rat liver is !1almost identical to human TFIIB. !$#cross-references MUID:92319661; PMID:1620622 !$#accession S26299 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type mRNA !'##residues 1-316 ##label TSU !'##cross-references EMBL:X65948; NID:g55623; PIDN:CAA46766.1; !1PID:g55624 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1992 CLASSIFICATION #superfamily transcription initiation factor IIB; !1transcription initiation factor IIB homology KEYWORDS DNA binding; duplication; nucleus; transcription initiation; !1zinc finger FEATURE !$14-294 #domain transcription initiation factor IIB homology !8#label TF2B\ !$15-37 #region zinc finger CHCC motif SUMMARY #length 316 #molecular-weight 34818 #checksum 4158 SEQUENCE /// ENTRY S20071 #type complete TITLE transcription initiation factor IIB - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S20071 REFERENCE S20071 !$#authors Hisatake, K.; Malik, S.; Roeder, R.G.; Horikoshi, M. !$#journal Nucleic Acids Res. (1991) 19:6639 !$#title Conserved structural motifs between Xenopus and human TFIIB. !$#cross-references MUID:92093629; PMID:1840674 !$#accession S20071 !'##status preliminary; nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-316 ##label HIS !'##cross-references EMBL:X62868; NID:g65128; PIDN:CAA44668.1; !1PID:g65129 CLASSIFICATION #superfamily transcription initiation factor IIB; !1transcription initiation factor IIB homology KEYWORDS DNA binding; duplication; nucleus; transcription initiation; !1zinc finger FEATURE !$14-294 #domain transcription initiation factor IIB homology !8#label TF2B\ !$15-37 #region zinc finger CHCC motif SUMMARY #length 316 #molecular-weight 34677 #checksum 5099 SEQUENCE /// ENTRY A42695 #type complete TITLE transcription initiation factor IIB - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A42695; A44075 REFERENCE A42695 !$#authors Yamashita, S.; Wada, K.; Horikoshi, M.; Gong, D.W.; Kokubo, !1T.; Hisatake, K.; Yokotani, N.; Malik, S.; Roeder, R.G.; !1Nakatani, Y. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:2839-2843 !$#title Isolation and characterization of a cDNA encoding Drosophila !1transcription factor TFIIB. !$#cross-references MUID:92212925; PMID:1557390 !$#accession A42695 !'##status preliminary !'##molecule_type mRNA !'##residues 1-315 ##label YAM !'##cross-references GB:M88164; NID:g158539; PIDN:AAA28930.1; !1PID:g158540 REFERENCE A44075 !$#authors Wampler, S.L.; Kadonaga, J.T. !$#journal Genes Dev. (1992) 6:1542-1552 !$#title Functional analysis of Drosophila transcription factor IIB. !$#cross-references MUID:92354915; PMID:1644295 !$#accession A44075 !'##status preliminary !'##molecule_type mRNA !'##residues 1-315 ##label WAM !'##cross-references GB:M91081; NID:g158537; PIDN:AAA28929.1; !1PID:g158538 !'##note sequence extracted from NCBI backbone (NCBIN:110724, !1NCBIP:110725) GENETICS !$#gene FlyBase:TfIIB !'##cross-references FlyBase:FBgn0004915 CLASSIFICATION #superfamily transcription initiation factor IIB; !1transcription initiation factor IIB homology KEYWORDS DNA binding; duplication; nucleus; transcription initiation; !1zinc finger FEATURE !$13-293 #domain transcription initiation factor IIB homology !8#label TF2B\ !$14-36 #region zinc finger CHCC motif SUMMARY #length 315 #molecular-weight 34369 #checksum 9986 SEQUENCE /// ENTRY S26707 #type complete TITLE transcription initiation factor IIB - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein P9513.4; protein YPR086w ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S26707; S69072 REFERENCE S26707 !$#authors Pinto, I.; Ware, D.E.; Hampsey, M. !$#journal Cell (1992) 68:977-988 !$#title The yeast SUA7 gene encodes a homolog of human transcription !1factor TFIIB and is required for normal start site selection !1in vivo. !$#cross-references MUID:92191276; PMID:1547497 !$#accession S26707 !'##molecule_type DNA !'##residues 1-345 ##label PIN !'##cross-references EMBL:M81380; NID:g172776; PIDN:AAA35126.1; !1PID:g172777 !'##experimental_source strain T15 REFERENCE S69057 !$#authors Couch, J. !$#submission submitted to the EMBL Data Library, March 1996 !$#description The sequence of S. cerevisiae cosmid 9513. !$#accession S69072 !'##molecule_type DNA !'##residues 1-345 ##label COU !'##cross-references EMBL:U51033; NID:g1230676; PIDN:AAB68135.1; !1PID:g1230692; GSPDB:GN00016; MIPS:YPR086w GENETICS !$#gene SGD:SUA7; MIPS:YPR086w !'##cross-references SGD:S0006290; MIPS:YPR086w !$#map_position 16R CLASSIFICATION #superfamily transcription initiation factor IIB; !1transcription initiation factor IIB homology KEYWORDS DNA binding; duplication; nucleus; transcription initiation; !1zinc finger FEATURE !$23-318 #domain transcription initiation factor IIB homology !8#label TF2B\ !$24-48 #region zinc finger CCCC motif\ !$133-210,239-313 #region duplication SUMMARY #length 345 #molecular-weight 38200 #checksum 1654 SEQUENCE /// ENTRY S34953 #type complete TITLE transcription initiation factor IIB - yeast (Kluyveromyces marxianus var. lactis) ORGANISM #formal_name Kluyveromyces marxianus var. lactis, Candida sphaerica DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S34953 REFERENCE S34953 !$#authors Na, J.G.; Hampsey, M. !$#journal Nucleic Acids Res. (1993) 21:3413-3417 !$#title The Kluyveromyces gene encoding the general transcription !1factor IIB: structural analysis and expression in !1Saccharomyces cerevisiae. !$#cross-references MUID:93347972; PMID:8346020 !$#accession S34953 !'##status preliminary !'##molecule_type DNA !'##residues 1-357 ##label NAJ !'##cross-references EMBL:L11606; NID:g173288; PIDN:AAA35258.1; !1PID:g173289 CLASSIFICATION #superfamily transcription initiation factor IIB; !1transcription initiation factor IIB homology KEYWORDS DNA binding; duplication; nucleus; transcription initiation; !1zinc finger FEATURE !$27-324 #domain transcription initiation factor IIB homology !8#label TF2B\ !$28-52 #region zinc finger CCCC motif\ !$137-214,245-319 #region duplication SUMMARY #length 357 #molecular-weight 39147 #checksum 1821 SEQUENCE /// ENTRY F64397 #type complete TITLE transcription initiation factor IIB homolog (intein-containing) - Methanococcus jannaschii CONTAINS intein ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F64397 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession F64397 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-673 ##label BUL !'##cross-references GB:U67522; GB:L77117; NID:g2826315; !1PIDN:AAB98771.1; PID:g1591481; TIGR:MJ0782 GENETICS !$#map_position REV705789-703768 CLASSIFICATION #superfamily Methanococcus transcription initiation factor !1IIB homolog; transcription initiation factor IIB homology KEYWORDS duplication; protein splicing; transcription initiation FEATURE !$492-569,586-660 #region duplication SUMMARY #length 673 #molecular-weight 76968 #checksum 1450 SEQUENCE /// ENTRY A55483 #type complete TITLE transcription initiation factor IIIB chain BRF - yeast (Kluyveromyces marxianus var. lactis) ALTERNATE_NAMES B-related factor ORGANISM #formal_name Kluyveromyces marxianus var. lactis, Candida sphaerica DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 15-Oct-1999 ACCESSIONS A55483 REFERENCE A55483 !$#authors Khoo, B.; Brophy, B.; Jackson, S.P. !$#journal Genes Dev. (1994) 8:2879-2890 !$#title Conserved functional domains of the RNA polymerase III !1general transcription factor BRF. !$#cross-references MUID:95087888; PMID:7995525 !$#accession A55483 !'##status preliminary !'##molecule_type DNA !'##residues 1-556 ##label KHO !'##cross-references GB:Z47203 CLASSIFICATION #superfamily transcription initiation factor IIIB chain BRF; !1transcription initiation factor IIB homology KEYWORDS transcription initiation FEATURE !$11-275 #domain transcription initiation factor IIB homology !8#label TF2B SUMMARY #length 556 #molecular-weight 62248 #checksum 2947 SEQUENCE /// ENTRY A44072 #type complete TITLE transcription factor IIIB chain BRF1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein G9110; protein YGR246c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A44072; A44295; A44296; S64572; S64578; S27464 REFERENCE A44072 !$#authors Colbert, T.; Hahn, S. !$#journal Genes Dev. (1992) 6:1940-1949 !$#title A yeast TFIIB-related factor involved in RNA polymerase III !1transcription. !$#cross-references MUID:93012949; PMID:1398071 !$#accession A44072 !'##molecule_type DNA !'##residues 1-596 ##label COL !'##cross-references EMBL:M91073; NID:g172896; PIDN:AAB04945.1; !1PID:g172897 !'##note sequence extracted from NCBI backbone (NCBIP:116238) REFERENCE A44295 !$#authors Buratowski, S.; Zhou, H. !$#journal Cell (1992) 71:221-230 !$#title A suppressor of TBP mutations encodes an RNA polymerase III !1transcription factor with homology to TFIIB. !$#cross-references MUID:93046623; PMID:1423590 !$#accession A44295 !'##molecule_type DNA !'##residues 1-596 ##label BUR !'##cross-references EMBL:L00630; NID:g172904; PIDN:AAA35148.1; !1PID:g172905 !'##note sequence extracted from NCBI backbone (NCBIP:116658) REFERENCE A44296 !$#authors Lopez-De-Leon, A.; Librizzi, M.; Puglia, K.; Willis, I.M. !$#journal Cell (1992) 71:211-220 !$#title PCF4 encodes an RNA polymerase III transcription factor with !1homology to TFIIB. !$#cross-references MUID:93046622; PMID:1423589 !$#accession A44296 !'##molecule_type DNA !'##residues 1-596 ##label LOP !'##note sequence extracted from NCBI backbone (NCBIP:116653) REFERENCE S64565 !$#authors Guerreiro, P.; Barreiros, T.; Azevedo, D.; !1Rodrigues-Pousada, C. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64572 !'##molecule_type DNA !'##residues 1-596 ##label GUE !'##cross-references EMBL:Z73031; NID:g1323445; PIDN:CAA97275.1; !1PID:g1323446; GSPDB:GN00007; MIPS:YGR246c !'##experimental_source strain S288C REFERENCE S64577 !$#authors Agostoni Carbone, M.L.; Panzeri, L.; Melchioretto, P.; !1Carignani, G.; Feroli, F.; Frontali, L.; Mazzoni, C.; !1Rinaldi, T.; Ruzzi, M. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64578 !'##molecule_type DNA !'##residues 1-596 ##label AGO !'##cross-references EMBL:Z73031; NID:g1323445; PIDN:CAA97275.1; !1PID:g1323446; GSPDB:GN00007; MIPS:YGR246c !'##experimental_source strain S288C GENETICS !$#gene SGD:BRF1; TDS4; PCF4; MIPS:YGR246c !'##cross-references SGD:S0003478; MIPS:YGR246c !$#map_position 7R CLASSIFICATION #superfamily transcription initiation factor IIIB chain BRF; !1transcription initiation factor IIB homology KEYWORDS duplication; nucleus; transcription regulation FEATURE !$3-264 #domain transcription initiation factor IIB homology !8#label TF2B\ !$87-164,182-259 #region duplication SUMMARY #length 596 #molecular-weight 66906 #checksum 2770 SEQUENCE /// ENTRY B55483 #type complete TITLE transcription initiation factor IIIB chain BRF - yeast (Candida albicans) ALTERNATE_NAMES B-related factor ORGANISM #formal_name Candida albicans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 15-Oct-1999 ACCESSIONS B55483 REFERENCE A55483 !$#authors Khoo, B.; Brophy, B.; Jackson, S.P. !$#journal Genes Dev. (1994) 8:2879-2890 !$#title Conserved functional domains of the RNA polymerase III !1general transcription factor BRF. !$#cross-references MUID:95087888; PMID:7995525 !$#accession B55483 !'##status preliminary !'##molecule_type DNA !'##residues 1-553 ##label KHO !'##cross-references GB:Z47202; NID:g619451; PIDN:CAA87398.1; !1PID:g619452 CLASSIFICATION #superfamily transcription initiation factor IIIB chain BRF; !1transcription initiation factor IIB homology KEYWORDS transcription initiation FEATURE !$9-272 #domain transcription initiation factor IIB homology !8#label TF2B SUMMARY #length 553 #molecular-weight 61840 #checksum 6562 SEQUENCE /// ENTRY TWECR #type complete TITLE transcription termination factor rho - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 01-Mar-2002 ACCESSIONS A03530; S30677; I69359; S16607; I53913; B65182 REFERENCE A93469 !$#authors Pinkham, J.L.; Platt, T. !$#journal Nucleic Acids Res. (1983) 11:3531-3545 !$#title The nucleotide sequence of the rho gene of Escherichia coli !1K-12. !$#cross-references MUID:83220759; PMID:6304634 !$#accession A03530 !'##molecule_type DNA !'##residues 1-419 ##label PIN !'##cross-references GB:J01673; GB:J01674; NID:g147605; PIDN:AAA24532.1; !1PID:g147607 !'##experimental_source strain K12 REFERENCE S30660 !$#authors Daniels, D.L.; Plunkett III, G.; Burland, V.; Blattner, F.R. !$#journal Science (1992) 257:771-778 !$#title Analysis of the Escherichia coli genome: DNA sequence of the !1region from 84.5 to 86.5 minutes. !$#cross-references MUID:92358234; PMID:1379743 !$#accession S30677 !'##status preliminary !'##molecule_type DNA !'##residues 1-419 ##label DAN !'##cross-references EMBL:M87049; NID:g836656; PIDN:AAA67583.1; !1PID:g148186 REFERENCE I54863 !$#authors Matsumoto, Y.; Shigesada, K.; Hirano, M.; Imai, M. !$#journal J. Bacteriol. (1986) 166:945-958 !$#title Autogenous regulation of the gene for transcription !1termination factor rho in Escherichia coli: Localization and !1function of its attenuators. !$#cross-references MUID:86223816; PMID:2423505 !$#accession I69359 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-196 ##label MAS !'##cross-references GB:M12779; NID:g148067; PIDN:AAA24695.1; !1PID:g551843 REFERENCE S16607 !$#authors Ohta, M.; Ina, K.; Kusuzaki, K.; Kido, N.; Arakawa, Y.; !1Kato, N. !$#journal Mol. Microbiol. (1991) 5:1853-1862 !$#title Cloning and expression of the rfe-rff gene cluster of !1Escherichia coli. !$#cross-references MUID:92114763; PMID:1722555 !$#accession S16607 !'##molecule_type DNA !'##residues 397-419 ##label OHT !'##cross-references GB:S75640; NID:g242028; PIDN:AAB20841.1; !1PID:g242029 REFERENCE I53913 !$#authors Opperman, T.; Martinez, A.; Richardson, J.P. !$#journal Gene (1995) 152:133-134 !$#title The ts15 mutation of Escherichia coli alters the sequence of !1the C-terminal nine residues of Rho protein. !$#cross-references MUID:95129907; PMID:7828920 !$#accession I53913 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 405-410,'EVMTPTY' ##label OPP !'##cross-references GB:L34404; NID:g508850; PIDN:AAA68985.1; !1PID:g508851 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65182 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-419 ##label BLAT !'##cross-references GB:AE000454; GB:U00096; NID:g2367278; !1PIDN:AAC76788.1; PID:g1790217; UWGP:b3783 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene rho !$#map_position 85 min FUNCTION !$#description causes termination of transcription at specific sites and !1catalyzes the release of the nascent RNA from the !1transcription complex !$#note may have an RNA-dependent ATPase activity CLASSIFICATION #superfamily transcription termination factor rho KEYWORDS ATP; transcription termination FEATURE !$169-380 #domain ATP-binding #status predicted #label ATP SUMMARY #length 419 #molecular-weight 47004 #checksum 1081 SEQUENCE /// ENTRY S50853 #type complete TITLE translation releasing factor eRF-1 [validated] - human ALTERNATE_NAMES omnipotent suppressor protein SUP1 homolog; peptide chain release factor 1; TB3-1 protein; translation termination factor 1 ORGANISM #formal_name Homo sapiens #common_name man DATE 14-Jul-1995 #sequence_revision 19-Oct-1995 #text_change 15-Sep-2000 ACCESSIONS S50853; JQ1460 REFERENCE S50853 !$#authors Frolova, L.; le Goff, X.; Rasmussen, H.H.; Cheperegin, S.; !1Drugeon, G.; Kress, M.; Arman, I.; Haenni, A.L.; Celis, !1J.E.; Philippe, M.; Justesen, J.; Kisselev, L. !$#journal Nature (1994) 372:701-703 !$#title A highly conserved eukaryotic protein family possessing !1properties of polypeptide chain release factor. !$#cross-references MUID:95082951; PMID:7990965 !$#accession S50853 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type mRNA !'##residues 1-437 ##label FRO !'##cross-references EMBL:X81625; NID:g1491703; PIDN:CAA57281.1; !1PID:g1491704 !'##note sequenced the same clone as used in reference JQ1460, as well !1as an independently isolated clone REFERENCE JQ1460 !$#authors Grenett, H.E.; Bounelis, P.; Fuller, G.M. !$#journal Gene (1992) 110:239-243 !$#title Identification of a human cDNA with high homology to yeast !1omnipotent suppressor 45. !$#cross-references MUID:92165066; PMID:1537561 !$#accession JQ1460 !'##molecule_type mRNA !'##residues 1-93,'E',95-297,'SLASTVLALKIHIGFG',314-318, !1'NSNSHMKSGYNEICSSLPRHRRRN',344-383,'NLELRWKLSQINHKKGLSLM', !1404-415,'QSRFPGNGIPRRRR' ##label GRE !'##cross-references GB:M75715; NID:g338686; PIDN:AAA36665.1; !1PID:g338687 GENETICS !$#gene GDB:ETF1; ERF !'##cross-references GDB:127559 FUNCTION !$#description eRF-1 recognizes stop codons and catalyzes peptidyl-tRNA !1hydrolysis [validated, MUID:95082951] CLASSIFICATION #superfamily translation releasing factor eRF-1 KEYWORDS protein biosynthesis SUMMARY #length 437 #molecular-weight 49031 #checksum 1490 SEQUENCE /// ENTRY S46014 #type complete TITLE omnipotent suppressor protein SUP45 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YBR1120; protein YBR143c; supressor protein SUP1 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 18-Feb-2000 ACCESSIONS S46014; S46012; S39109; A23642; S45532; S68105 REFERENCE S46013 !$#authors Entian, K.D.; Koetter, P.; Rose, M.; Becker, J.; Grey, M.; !1Li, Z.; Niegemann, E.; Schenk-Groeninger, R.; Servos, J.; !1Wehner, E.; Wolter, R.; Brendel, M.; Bauer, J.; Braun, H.; !1Dern, K.; Duesterhus, S.; Gruenbein, R.; Hedges, D.; Kiesau, !1P.; Korol, S.; Krems, B.; Proft, M.; Siegers, K.; Baur, A.; !1Boles, E.; Miosga, T.; Schaaff-Gerstenschlaeger, I.; !1Zimmermann, F.K. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S46014 !'##molecule_type DNA !'##residues 1-437 ##label ENT !'##cross-references EMBL:Z36012; GB:Y13134; NID:g536443; !1PIDN:CAA85101.1; PID:g536444; GSPDB:GN00002; MIPS:YBR143c !'##experimental_source strain S288C REFERENCE S45995 !$#authors Becam, A.M.; Herbert, C.J.; Nasr, F.; Slonimski, P.P.; !1Zagulski, M. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S46012 !'##molecule_type DNA !'##residues 431-437 ##label BEC !'##cross-references EMBL:Z36012; NID:g536443 !'##experimental_source strain S288C REFERENCE S39108 !$#authors Miosga, T.; Zimmermann, F.K. !$#journal Yeast (1993) 9:1273-1277 !$#title Sequence and function analysis of a 2.73 kb fragment of !1Saccharomyces cerevisiae chromosome II. !$#cross-references MUID:94152175; PMID:8109177 !$#accession S39109 !'##status translation not shown !'##molecule_type DNA !'##residues 1-432 ##label MIO !'##cross-references EMBL:X73531; NID:g313258; PIDN:CAA51935.1; !1PID:g468605 !'##experimental_source strain S288C REFERENCE A23642 !$#authors Breining, P.; Piepersberg, W. !$#journal Nucleic Acids Res. (1986) 14:5187-5197 !$#title Yeast omnipotent supressor SUP1 (SUP45): nucleotide sequence !1of the wildtype and a mutant gene. !$#cross-references MUID:86286537; PMID:3526282 !$#accession A23642 !'##molecule_type DNA !'##residues 1-40,'L',42-437 ##label BRE !'##cross-references EMBL:X04082; NID:g4592; PIDN:CAA27719.1; PID:g4593 REFERENCE S45532 !$#authors Surguchev, A.P.; Telkov, M.V.; Smirnov, V.N.; Breining, P.; !1Piepersberg, W. !$#journal Mol. Biol. (Mosk.) (1987) 21:290-301 !$#title Nucleotide sequence of mutant and wild-type alleles of the !1SUP1 gene and comparison of transcripts of SUP1 and SUP2 !1genes. !$#accession S45532 !'##molecule_type DNA !'##residues 1-40,'L',42-437 ##label SUR !'##cross-references EMBL:M28042; NID:g172788 !'##note the authors translated the codon GTT for residue 26 as Glu !'##note this translation is not annotated in GenBank entry YSCSUP1AA, !1release 116.0 REFERENCE S68105 !$#authors Mironova, L.N.; Samsonova, M.G.; Zhouravleva, G.A.; Kulikov, !1V.N.; Soom, M.J. !$#journal Curr. Genet. (1995) 27:195-200 !$#title Reversions to respiratory competence of omnipotent sup45 !1suppressor mutants may be caused by secondary sup45 !1mutations. !$#cross-references MUID:95254659; PMID:7736601 !$#accession S68105 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-437 ##label MIR GENETICS !$#gene SGD:SUP45; SUP1; MIPS:YBR143c !'##cross-references MIPS:YBR143c; SGD:S0000347 !$#map_position 2R CLASSIFICATION #superfamily translation releasing factor eRF-1 KEYWORDS cytosol; mitochondrion; protein biosynthesis SUMMARY #length 437 #molecular-weight 49005 #checksum 3067 SEQUENCE /// ENTRY S31328 #type complete TITLE omnipotent suppressor protein SUP1 homolog (clone G18) - Arabidopsis thaliana ALTERNATE_NAMES omnipotent suppressor protein SUP45 homolog ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S31328 REFERENCE S31328 !$#authors Quigley, F.R. !$#submission submitted to the EMBL Data Library, November 1992 !$#accession S31328 !'##status preliminary !'##molecule_type DNA !'##residues 1-435 ##label QUI !'##cross-references EMBL:X69375; NID:g16513; PIDN:CAA49172.1; !1PID:g16514 CLASSIFICATION #superfamily translation releasing factor eRF-1 SUMMARY #length 435 #molecular-weight 49007 #checksum 1568 SEQUENCE /// ENTRY A48061 #type complete TITLE translation releasing factor eRF-1 - African clawed frog ALTERNATE_NAMES omnipotent suppressor protein SUP1 homolog; peptide chain release factor 1 ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 21-Jan-1994 #sequence_revision 19-Oct-1995 #text_change 16-Jul-1999 ACCESSIONS A48061; S31633 REFERENCE A48061 !$#authors Tassan, J.P.; Le Guellec, K.; Kress, M.; Faure, M.; Camonis, !1J.; Jacquet, M.; Philippe, M. !$#journal Mol. Cell. Biol. (1993) 13:2815-2821 !$#title In Xenopus laevis, the product of a developmentally !1regulated mRNA is structurally and functionally homologous !1to a Saccharomyces cerevisiae protein involved in !1translation fidelity. !$#cross-references MUID:93233643; PMID:8474443 !$#accession A48061 !'##molecule_type mRNA !'##residues 1-437 ##label TAS !'##cross-references EMBL:Z14253; NID:g64631; PIDN:CAA78620.1; !1PID:g64632 !'##experimental_source oocytes !'##note sequence extracted from NCBI backbone (NCBIN:129824, !1NCBIP:129825) COMMENT This protein is expressed in oocytes and embryos; its !1expression in adults differs in different tissues. FUNCTION !$#description eRF-1 recognizes stop codons and catalyzes peptidyl-tRNA !1hydrolysis; in yeast, mutants are omnipotent suppressors of !1nonsense codons CLASSIFICATION #superfamily translation releasing factor eRF-1 KEYWORDS protein biosynthesis SUMMARY #length 437 #molecular-weight 49010 #checksum 2673 SEQUENCE /// ENTRY FCECR1 #type complete TITLE translation releasing factor RF-1 - Escherichia coli (strain K-12) ALTERNATE_NAMES peptide chain release factor 1 ORGANISM #formal_name Escherichia coli DATE 31-Mar-1990 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS H64867; I83569; A30387; PQ0013; A31838; I52973; Q00212 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64867 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-360 ##label BLAT !'##cross-references GB:AE000219; GB:U00096; NID:g1787453; !1PIDN:AAC74295.1; PID:g1787462; UWGP:b1211 !'##experimental_source strain K-12, substrain MG1655 REFERENCE I60364 !$#authors Strohmaier, H.; Remler, P.; Renner, W.; Hogenauer, G. !$#journal J. Bacteriol. (1995) 177:4488-4500 !$#title Expression of genes kdsA and kdsB involved in !13-deoxy-D-manno-octulosonic acid metabolism and biosynthesis !1of enterobacterial lipopolysaccharide is growth phase !1regulated primarily at the transcriptional level in !1Escherichia coli K-12. !$#cross-references MUID:95362678; PMID:7543480 !$#accession I83569 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-210,'E',212-360 ##label RES !'##cross-references EMBL:U18555; NID:g968925; PIDN:AAC43437.1; !1PID:g968930 !'##experimental_source strain K-12 REFERENCE A30387 !$#authors Craigen, W.J.; Cook, R.G.; Tate, W.P.; Caskey, C.T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:3616-3620 !$#title Bacterial peptide chain release factors: conserved primary !1structure and possible frameshift regulation of release !1factor 2. !$#cross-references MUID:85216549; PMID:3889910 !$#accession A30387 !'##molecule_type DNA !'##residues 1-240,'G',242-315,'ALPITAST' ##label CRA !'##cross-references GB:M11519 !'##experimental_source strain RR1 !'##note this sequence has been revised in reference A31838 REFERENCE JQ0089 !$#authors Li, J.M.; Russell, C.S.; Cosloy, S.D. !$#journal Gene (1989) 82:209-217 !$#title Cloning and structure of the hemA gene of Escherichia coli !1K-12. !$#cross-references MUID:90060810; PMID:2684779 !$#accession PQ0013 !'##status translation not shown !'##molecule_type DNA !'##residues 1-71,'LRYLLYLRLFVVLF',75,'HVVG',80 ##label LIJ !'##experimental_source strain K-12 REFERENCE A31838 !$#authors Lee, C.C.; Kohara, Y.; Akiyama, K.; Smith, C.L.; Craigen, !1W.J.; Caskey, C.T. !$#journal J. Bacteriol. (1988) 170:4537-4541 !$#title Rapid and precise mapping of the Escherichia coli release !1factor genes by two physical approaches. !$#cross-references MUID:89008065; PMID:3049538 !$#accession A31838 !'##molecule_type DNA !'##residues 279-360 ##label LEE REFERENCE I52973 !$#authors Nakayashiki, T.; Nishimura, K.; Inokuchi, H. !$#journal DNA (1995) 153:67-70 !$#title Cloning and sequencing of a previously unidentified gene !1that is involved in the biosynthesis of heme in Escherichia !1coli. !$#accession I52973 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 339-360 ##label RE2 !'##cross-references GB:D28567; NID:g466531; PIDN:BAA05914.1; !1PID:g466532 !'##experimental_source strain K-12 GENETICS !$#gene prfA; RF-1; sueB; uar !$#map_position 27 min FUNCTION !$#description codon-specific peptide-chain-release factor reponsible for !1release of the polypeptide chain by peptidyl-tRNA !1hydrolysis; recognizes termination codons UAG and UAA !$#pathway protein biosynthesis CLASSIFICATION #superfamily translation releasing factor KEYWORDS protein biosynthesis SUMMARY #length 360 #molecular-weight 40517 #checksum 8996 SEQUENCE /// ENTRY B32890 #type complete TITLE translation releasing factor RF-1 - Salmonella typhimurium ALTERNATE_NAMES peptide chain release factor 1 ORGANISM #formal_name Salmonella typhimurium DATE 08-Dec-1989 #sequence_revision 06-Jun-1997 #text_change 16-Jul-1999 ACCESSIONS B32890 REFERENCE A32661 !$#authors Elliott, T. !$#journal J. Bacteriol. (1989) 171:3948-3960 !$#title Cloning, genetic characterization, and nucleotide sequence !1of the hemA-prfA operon of Salmonella typhimurium. !$#cross-references MUID:89291746; PMID:2544564 !$#accession B32890 !'##molecule_type DNA !'##residues 1-360 ##label EL2 !'##cross-references GB:J04243; NID:g154102; PIDN:AAA88611.1; !1PID:g154104 !'##note the authors translated the codon CTC for residue 271 as Val GENETICS !$#gene prfA; RF-1 FUNCTION !$#description codon-specific peptide-chain-release factor reponsible for !1release of the polypeptide chain by peptidyl-tRNA !1hydrolysis; recognizes termination codons UAG and UAA !$#pathway protein biosynthesis CLASSIFICATION #superfamily translation releasing factor KEYWORDS protein biosynthesis SUMMARY #length 360 #molecular-weight 40461 #checksum 9169 SEQUENCE /// ENTRY I64129 #type complete TITLE translation releasing factor RF-1 - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES peptide chain release factor 1 ORGANISM #formal_name Haemophilus influenzae DATE 18-Aug-1995 #sequence_revision 06-Jun-1997 #text_change 16-Jul-1999 ACCESSIONS I64129 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession I64129 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-361 ##label TIGR !'##cross-references GB:U32830; GB:L42023; NID:g1574389; !1PIDN:AAC23209.1; PID:g1574404; TIGR:HI1561 GENETICS !$#gene prfA; RF-1 FUNCTION !$#description codon-specific peptide-chain-release factors reponsible for !1the release of the polypeptide chain by peptidyl-tRNA !1hydrolysis; recognizes termination codons UAG and UAA !$#pathway protein biosynthesis CLASSIFICATION #superfamily translation releasing factor KEYWORDS protein biosynthesis SUMMARY #length 361 #molecular-weight 41048 #checksum 1174 SEQUENCE /// ENTRY S55437 #type complete TITLE translation releasing factor RF-1 - Bacillus subtilis ALTERNATE_NAMES peptide chain release factor 1 ORGANISM #formal_name Bacillus subtilis DATE 15-Jul-1995 #sequence_revision 06-Jun-1997 #text_change 16-Jun-2000 ACCESSIONS S55437; G69681 REFERENCE S55414 !$#authors Glaser, P.; Danchin, A. !$#submission submitted to the EMBL Data Library, May 1995 !$#description Cloning and sequencing of the Bacillus subtilis chromosomal !1region from 320 degrees to 321 degrees. !$#accession S55437 !'##molecule_type DNA !'##residues 1-356 ##label GLA !'##cross-references EMBL:Z49782; NID:g853752; PIDN:CAA89884.1; !1PID:g853776 !'##experimental_source strain 168 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69681 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-356 ##label KUN !'##cross-references GB:Z99122; GB:AL009126; NID:g2636029; !1PIDN:CAB15718.1; PID:g2636226 !'##experimental_source strain 168 GENETICS !$#gene prfA; RF-1 !$#start_codon GTG FUNCTION !$#description codon-specific peptide-chain-release factors reponsible for !1the release of the polypeptide chain by peptidyl-tRNA !1hydrolysis; recognizes termination codons UAG and UAA !$#pathway protein biosynthesis CLASSIFICATION #superfamily translation releasing factor KEYWORDS protein biosynthesis SUMMARY #length 356 #molecular-weight 40233 #checksum 3380 SEQUENCE /// ENTRY A61648 #type complete TITLE translation releasing factor RF-1 - Coxiella burnetii ALTERNATE_NAMES peptide chain release factor 1 ORGANISM #formal_name Coxiella burnetii DATE 06-Jun-1997 #sequence_revision 06-Jun-1997 #text_change 16-Jul-1999 ACCESSIONS A61648 REFERENCE S44206 !$#authors Willems, H.; Thiele, D.; Oswald, W.; Krauss, H. !$#submission submitted to the EMBL Data Library, April 1994 !$#accession A61648 !'##molecule_type DNA !'##residues 1-361 ##label WIL !'##cross-references EMBL:X78969; NID:g623026; PIDN:CAA55563.1; !1PID:g623028 !'##experimental_source isolate Nine Mile RSA493, phase I GENETICS !$#gene prfA; RF-1 FUNCTION !$#description codon-specific peptide-chain-release factor reponsible for !1release of the polypeptide chain by peptidyl-tRNA !1hydrolysis; recognizes termination codons UAG and UAA !$#pathway protein biosynthesis CLASSIFICATION #superfamily translation releasing factor KEYWORDS protein biosynthesis SUMMARY #length 361 #molecular-weight 40749 #checksum 5705 SEQUENCE /// ENTRY S76914 #type complete TITLE translation releasing factor RF-1 - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES peptide chain release factor 1 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 25-Apr-1997 #sequence_revision 06-Jun-1997 #text_change 16-Jun-2000 ACCESSIONS S76914 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76914 !'##molecule_type DNA !'##residues 1-365 ##label KAN !'##cross-references EMBL:D90917; GB:AB001339; NID:g1653836; !1PIDN:BAA18826.1; PID:g1653916 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene prfA; RF-1 FUNCTION !$#description this is one of two codon-specific peptide-chain-release !1factors that is reponsible for the release of the !1polypeptide chain from the ribosome by peptidyl tRNA !1hydrolysis in the chain termination process, the final step !1of protein synthesis. It recognizes termination codons UAG !1and UAA. CLASSIFICATION #superfamily translation releasing factor KEYWORDS protein biosynthesis SUMMARY #length 365 #molecular-weight 41126 #checksum 3642 SEQUENCE /// ENTRY E64228 #type complete TITLE translation releasing factor RF-1 - Mycoplasma genitalium ALTERNATE_NAMES peptide chain release factor 1 ORGANISM #formal_name Mycoplasma genitalium DATE 17-Nov-1995 #sequence_revision 06-Jun-1997 #text_change 21-Jul-2000 ACCESSIONS E64228 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession E64228 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-359 ##label TIGR !'##cross-references GB:U39704; GB:L43967; NID:g3844847; !1PIDN:AAC71478.1; PID:g1045950; TIGR:MG258 !'##experimental_source strain G-37 COMMENT This is the only codon-specific peptide-chain-release factor !1of the Mycoplasmas, where UGA encodes Trp rather than stop. !1Peptide chain release factor 2, which in other species !1recognizes termination codons UGA and UAA, is not present. GENETICS !$#gene prfA; RF-1 !$#genetic_code SGC3 !$#start_codon GTG FUNCTION !$#description reponsible for the release of the polypeptide chain from the !1ribosome by peptidyl tRNA hydrolysis in the chain !1termination process, final step of protein synthesis; !1recognizes termination codons UAG and UAA CLASSIFICATION #superfamily translation releasing factor KEYWORDS protein biosynthesis SUMMARY #length 359 #molecular-weight 40807 #checksum 8202 SEQUENCE /// ENTRY S28602 #type complete TITLE translation releasing factor RF-1, mitochondrial - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein G2530; protein YGL143c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S28602; S64157 REFERENCE S28601 !$#authors Pel, H.J.; Maat, C.; Rep, M.; Grivell, L.A. !$#journal Nucleic Acids Res. (1992) 20:6339-6346 !$#title The yeast nuclear gene MRF1 encodes a mitochondrial peptide !1chain release factor and cures several mitochondrial RNA !1splicing defects. !$#cross-references MUID:93117110; PMID:1475194 !$#accession S28602 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-413 ##label PEL !'##cross-references EMBL:X60381; NID:g3971; PIDN:CAA42932.1; PID:g3972 REFERENCE S64153 !$#authors Volckaert, G.; Voet, M.; Verhasselt, P.; Defoor, E. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64157 !'##molecule_type DNA !'##residues 1-413 ##label VOL !'##cross-references EMBL:Z72665; NID:g1322721; PIDN:CAA96855.1; !1PID:g1322722; GSPDB:GN00007; MIPS:YGL143c !'##experimental_source strain S288C GENETICS !$#gene SGD:MRF1; MIPS:YGL143c !'##cross-references SGD:S0003111; MIPS:YGL143c !$#map_position 7L !$#genome nuclear CLASSIFICATION #superfamily translation releasing factor KEYWORDS mitochondrion SUMMARY #length 413 #molecular-weight 46770 #checksum 6605 SEQUENCE /// ENTRY S70354 #type complete TITLE translation releasing factor RF-1 precursor, mitochondrial - yeast (Kluyveromyces marxianus var. lactis) ORGANISM #formal_name Kluyveromyces marxianus var. lactis, Candida sphaerica DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S70354 REFERENCE S70353 !$#authors Pel, H.J.; Rozenfeld, S.; Bolotin-Fukuhara, M. !$#journal Curr. Genet. (1996) 30:19-28 !$#title The nuclear Kluyveromyces lactis MRF1 gene encodes a !1mitochondrial class I peptide chain release factor that is !1important for cell viability. !$#cross-references MUID:96269925; PMID:8662205 !$#accession S70354 !'##status preliminary; nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-396 ##label PEL !'##cross-references EMBL:U19586; NID:g641908; PIDN:AAB18362.1; !1PID:g641909 !'##note the source is designated as Kluyveromyces lactis GENETICS !$#gene MRF1 !$#genome nuclear CLASSIFICATION #superfamily translation releasing factor KEYWORDS mitochondrion SUMMARY #length 396 #molecular-weight 44994 #checksum 7310 SEQUENCE /// ENTRY FCECR2 #type complete TITLE translation releasing factor RF-2 - Escherichia coli (strain K-12) ALTERNATE_NAMES peptide chain release factor 2 ORGANISM #formal_name Escherichia coli DATE 31-Mar-1990 #sequence_revision 10-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS C65073; B30387; A32651; B31838; A31325; Q00389 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65073 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-365 ##label BLAT !'##cross-references GB:AE000372; GB:U00096; NID:g2367171; !1PIDN:AAC75929.1; PID:g2367172; UWGP:b2891 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A30387 !$#authors Craigen, W.J.; Cook, R.G.; Tate, W.P.; Caskey, C.T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:3616-3620 !$#title Bacterial peptide chain release factors: conserved primary !1structure and possible frameshift regulation of release !1factor 2. !$#cross-references MUID:85216549; PMID:3889910 !$#accession B30387 !'##molecule_type DNA !'##residues 1-200,'V',202-296, !1'NWRCRRKMPRNRRWKITNPTSAGAARFVLMSLMTPALKICAPG' ##label CRA !'##experimental_source strain RR1 !'##note residues 1-44 were confirmed by protein sequencing !'##note this sequence differs from that shown because of a frameshift !1in translation caused by an additional guanine residue in !1the DNA sequence REFERENCE A32651 !$#authors Kawakami, K.; Joensson, Y.H.; Bjoerk, G.R.; Ikeda, H.; !1Nakamura, Y. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:5620-5624 !$#title Chromosomal location and structure of the operon encoding !1peptide-chain-release factor 2 of Escherichia coli. !$#cross-references MUID:88289768; PMID:2456575 !$#accession A32651 !'##molecule_type DNA !'##residues 294-365 ##label KAW !'##cross-references GB:J03795; NID:g146339; PIDN:AAA23958.1; !1PID:g146340 REFERENCE A31838 !$#authors Lee, C.C.; Kohara, Y.; Akiyama, K.; Smith, C.L.; Craigen, !1W.J.; Caskey, C.T. !$#journal J. Bacteriol. (1988) 170:4537-4541 !$#title Rapid and precise mapping of the Escherichia coli release !1factor genes by two physical approaches. !$#cross-references MUID:89008065; PMID:3049538 !$#accession B31838 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 296-365 ##label LEE COMMENT This is one of two codon-specific peptide-chain-release !1factors that are responsible for release of polypeptide !1chains from the ribosome by peptidyl tRNA hydrolysis. It !1recognizes termination codons UGA and UAA. COMMENT The gene coding for this protein (RF-2) contains a UGA !1in-frame termination codon after 25-Leu; the protein !1sequence indicates that a naturally occurring frameshift !1enables complete translation of RF-2. This provides a !1mechanism for the protein to regulate its own production. GENETICS !$#gene prfB !$#map_position 62 min CLASSIFICATION #superfamily translation releasing factor KEYWORDS protein biosynthesis; translational frameshift FEATURE !$25-26 #region plus-one translational frameshift SUMMARY #length 365 #molecular-weight 41250 #checksum 1259 SEQUENCE /// ENTRY A36480 #type complete TITLE translation releasing factor RF-2 - Salmonella typhimurium ALTERNATE_NAMES peptide chain release factor 2 ORGANISM #formal_name Salmonella typhimurium DATE 28-Mar-1991 #sequence_revision 06-Jun-1997 #text_change 16-Jul-1999 ACCESSIONS A36480 REFERENCE A36480 !$#authors Kawakami, K.; Nakamura, Y. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:8432-8436 !$#title Autogenous suppression of an opal mutation in the gene !1encoding peptide chain release factor 2. !$#cross-references MUID:91046011; PMID:2236050 !$#accession A36480 !'##molecule_type DNA !'##residues 1-365 ##label KAW !'##cross-references GB:M38590; NID:g154274; PIDN:AAA72914.1; !1PID:g154276 COMMENT This is one of two codon-specific peptide-chain-release !1factors that are responsible for release of polypeptide !1chains from the ribosome by peptidyl tRNA hydrolysis. It !1recognizes termination codons UGA and UAA. COMMENT The gene coding for this protein (RF-2) contains a UGA !1in-frame termination codon after 25-Leu; the protein !1sequence indicates that a naturally occurring frameshift !1enables complete translation of RF-2. This provides a !1mechanism for the protein to regulate its own production. GENETICS !$#gene prfB CLASSIFICATION #superfamily translation releasing factor KEYWORDS protein biosynthesis; translational frameshift FEATURE !$25-26 #region plus-one translational frameshift SUMMARY #length 365 #molecular-weight 41148 #checksum 2648 SEQUENCE /// ENTRY A64190 #type complete TITLE translation releasing factor RF-2 - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES peptide chain release factor 2 ORGANISM #formal_name Haemophilus influenzae DATE 06-Jun-1997 #sequence_revision 06-Jun-1997 #text_change 23-Aug-1997 ACCESSIONS A64190 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession A64190 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-365 ##label COT !'##cross-references GB:U32800; TIGR:HI1212 COMMENT This is one of two codon-specific peptide-chain-release !1factors that are responsible for release of polypeptide !1chains from the ribosome by peptidyl tRNA hydrolysis. It !1recognizes termination codons UGA and UAA. COMMENT The gene coding for this protein (RF-2) contains a UGA !1in-frame termination codon after 25-Leu; the protein !1sequence indicates that a naturally occurring frameshift !1enables complete translation of RF-2. This provides a !1mechanism for the protein to regulate its own production. GENETICS !$#gene prfB CLASSIFICATION #superfamily translation releasing factor KEYWORDS protein biosynthesis; translational frameshift FEATURE !$25-26 #region plus-one translational frameshift SUMMARY #length 365 #molecular-weight 41281 #checksum 9941 SEQUENCE /// ENTRY JN0146 #type complete TITLE translation releasing factor RF-2 - Bacillus subtilis ALTERNATE_NAMES peptide chain release factor 2; prfB ORGANISM #formal_name Bacillus subtilis DATE 30-Sep-1991 #sequence_revision 13-Feb-1998 #text_change 16-Jun-2000 ACCESSIONS H69681; JN0146 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69681 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-366 ##label KUN !'##cross-references GB:Z99122; GB:AL009126; NID:g2636029; !1PIDN:CAB15546.1; PID:g2636055 !'##experimental_source strain 168 REFERENCE JN0145 !$#authors Sadaie, Y.; Takamatsu, H.; Nakamura, K.; Yamane, K. !$#journal Gene (1991) 98:101-105 !$#title Sequencing reveals similarity of the wild-type div+ gene of !1Bacillus subtilis to the Escherichia coli secA gene. !$#cross-references MUID:91192600; PMID:1901557 !$#accession JN0146 !'##molecule_type DNA !'##residues 13-337,'D' ##label SAD COMMENT This is one of two codon-specific peptide-chain-release !1factors that are responsible for release of polypeptide !1chains from the ribosome by peptidyl tRNA hydrolysis. It !1recognizes termination codons UGA and UAA. COMMENT The gene coding for this protein (RF-2) contains a UGA !1in-frame termination codon after 24-Leu; the protein !1sequence indicates that a naturally occurring frameshift !1enables complete translation of RF-2. This provides a !1mechanism for the protein to regulate its own production. GENETICS !$#gene prfB CLASSIFICATION #superfamily translation releasing factor KEYWORDS protein biosynthesis; translational frameshift FEATURE !$24-25 #region plus-one translational frameshift SUMMARY #length 366 #molecular-weight 42073 #checksum 88 SEQUENCE /// ENTRY S76448 #type complete TITLE translation releasing factor RF-2 - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES peptide chain release factor 2 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 25-Apr-1997 #sequence_revision 06-Jun-1997 #text_change 10-Jul-1998 ACCESSIONS S76448 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76448 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-372 ##label KAN !'##cross-references EMBL:D90915; GB:AB001339; NID:g1653604 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 COMMENT This is one of two codon-specific peptide-chain-release !1factors that are responsible for release of polypeptide !1chains from the ribosome by peptidyl tRNA hydrolysis. It !1recognizes termination codons UGA and UAA. COMMENT The gene coding for this protein (RF-2) contains a UGA !1in-frame termination codon after 26-Leu; the protein !1sequence indicates that a naturally occurring frameshift !1enables complete translation of RF-2. This provides a !1mechanism for the protein to regulate its own production. GENETICS !$#gene prfB CLASSIFICATION #superfamily translation releasing factor KEYWORDS protein biosynthesis; translational frameshift FEATURE !$26-27 #region plus-one translational frameshift SUMMARY #length 372 #molecular-weight 41760 #checksum 1889 SEQUENCE /// ENTRY A34495 #type complete TITLE ribosome releasing factor - Escherichia coli (strain K-12) ALTERNATE_NAMES ribosome recycling factor; translation releasing factor ORGANISM #formal_name Escherichia coli DATE 07-Sep-1990 #sequence_revision 07-Sep-1990 #text_change 01-Mar-2002 ACCESSIONS A34495; C45269; S45237; D64741; I41217 REFERENCE A34495 !$#authors Ichikawa, S.; Kaji, A. !$#journal J. Biol. Chem. (1989) 264:20054-20059 !$#title Molecular cloning and expression of ribosome releasing !1factor. !$#cross-references MUID:90062117; PMID:2684966 !$#accession A34495 !'##molecule_type DNA !'##residues 1-185 ##label ICH !'##cross-references GB:J05113; NID:g147770; PIDN:AAA24607.1; !1PID:g147771 REFERENCE A45269 !$#authors Yamanaka, K.; Ogura, T.; Niki, H.; Hiraga, S. !$#journal J. Bacteriol. (1992) 174:7517-7526 !$#title Identification and characterization of the smbA gene, a !1suppressor of the mukB null mutant of Escherichia coli. !$#cross-references MUID:93077430; PMID:1447125 !$#accession C45269 !'##status preliminary !'##molecule_type DNA !'##residues 1-185 ##label YAM !'##cross-references GB:D26562; NID:g473770; PIDN:BAA05616.1; !1PID:g473827 !'##experimental_source W3110 !'##note sequence extracted from NCBI backbone (NCBIP:119079) REFERENCE S45181 !$#authors Fujita, N. !$#submission submitted to the EMBL Data Library, January 1994 !$#accession S45237 !'##molecule_type DNA !'##residues 1-185 ##label FUJ !'##cross-references EMBL:D26562; NID:g473770; PIDN:BAA05616.1; !1PID:g473827 !'##experimental_source strain K-12, substrain W3110 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64741 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-185 ##label BLAT !'##cross-references GB:AE000126; GB:U00096; NID:g1786358; !1PIDN:AAC73283.1; PID:g1786368; UWGP:b0172 !'##experimental_source strain K-12, substrain MG1655 REFERENCE I41217 !$#authors Shimizu, I.; Kaji, A. !$#journal J. Bacteriol. (1991) 173:5181-5187 !$#title Identification of the promoter region of the !1ribosome-releasing factor cistron (frr). !$#cross-references MUID:91317739; PMID:1860827 !$#accession I41217 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-5 ##label RES !'##cross-references GB:M69029; NID:g146016 GENETICS !$#gene frr; rrf !$#map_position 4 min !$#start_codon GTG FUNCTION !$#description responsible for releasing ribosomes from mRNA and recycling !1the ribosomes for another round of translation CLASSIFICATION #superfamily ribosome releasing factor KEYWORDS protein biosynthesis SUMMARY #length 185 #molecular-weight 20638 #checksum 6081 SEQUENCE /// ENTRY D64095 #type complete TITLE ribosome releasing factor - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES ribosome recycling factor; translation releasing factor ORGANISM #formal_name Haemophilus influenzae DATE 18-Aug-1995 #sequence_revision 18-Aug-1995 #text_change 16-Jul-1999 ACCESSIONS D64095 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession D64095 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-185 ##label TIGR !'##cross-references GB:U32763; GB:L42023; NID:g1573817; !1PIDN:AAC22467.1; PID:g1573820; TIGR:HI0808 COMMENT This protein is responsible for the release of ribosomes !1from mRNA and recycling the ribosomes from one round of !1translation to another during protein biosynthesis. GENETICS !$#gene frr; rrf CLASSIFICATION #superfamily ribosome releasing factor KEYWORDS protein biosynthesis SUMMARY #length 185 #molecular-weight 20729 #checksum 4653 SEQUENCE /// ENTRY S76428 #type complete TITLE ribosome releasing factor - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein sll0145; ribosome recycling factor; translation releasing factor ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 25-Apr-1997 #sequence_revision 25-Apr-1997 #text_change 16-Jun-2000 ACCESSIONS S76428 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76428 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-182 ##label KAN !'##cross-references EMBL:D90915; GB:AB001339; NID:g1653604; !1PIDN:BAA18557.1; PID:g1653645 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 COMMENT This protein is responsible for the release of ribosomes !1from mRNA and recycling the ribosomes from one round of !1translation to another during protein biosynthesis. GENETICS !$#gene frr; rrf !$#start_codon GTG CLASSIFICATION #superfamily ribosome releasing factor KEYWORDS protein biosynthesis SUMMARY #length 182 #molecular-weight 20186 #checksum 2680 SEQUENCE /// ENTRY S32716 #type complete TITLE ribosome releasing factor - carrot ALTERNATE_NAMES nuclear protein; protein sll0145; ribosome recycling factor; translation releasing factor ORGANISM #formal_name Daucus carota #common_name carrot DATE 06-Feb-1995 #sequence_revision 06-Feb-1995 #text_change 16-Jul-1999 ACCESSIONS S32716; S32125 REFERENCE S32123 !$#authors Schrader, S.; Kaldenhoff, R.; Richter, G. !$#submission submitted to the EMBL Data Library, March 1993 !$#accession S32716 !'##status preliminary !'##molecule_type mRNA !'##residues 1-167 ##label SCH !'##cross-references EMBL:X72384; NID:g297890; PIDN:CAA51077.1; !1PID:g297891 COMMENT This protein is responsible for the release of ribosomes !1from mRNA and recycling the ribosomes from one round of !1translation to another during protein biosynthesis. CLASSIFICATION #superfamily ribosome releasing factor KEYWORDS nucleus; protein biosynthesis SUMMARY #length 167 #molecular-weight 18840 #checksum 4075 SEQUENCE /// ENTRY H64676 #type complete TITLE ribosome releasing factor - Helicobacter pylori (strain 26695) ALTERNATE_NAMES ribosome recycling factor; translation releasing factor ORGANISM #formal_name Helicobacter pylori DATE 09-Aug-1997 #sequence_revision 09-Aug-1997 #text_change 16-Jul-1999 ACCESSIONS H64676 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession H64676 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-185 ##label TOM !'##cross-references GB:AE000631; GB:AE000511; NID:g2314421; !1PIDN:AAD08302.1; PID:g2314423; TIGR:HP1256 COMMENT This protein is responsible for the release of ribosomes !1from mRNA and recycling the ribosomes from one round of !1translation to another during protein biosynthesis. GENETICS !$#gene frr; rrf CLASSIFICATION #superfamily ribosome releasing factor KEYWORDS protein biosynthesis SUMMARY #length 185 #molecular-weight 20915 #checksum 4844 SEQUENCE /// ENTRY BWQXQX #type complete TITLE RUBISCO-expression protein cfxQ - Xanthobacter flavus ORGANISM #formal_name Xanthobacter flavus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 05-May-2000 ACCESSIONS S13575 REFERENCE S13573 !$#authors Meijer, W.G.; Arnberg, A.C.; Enequist, H.G.; Terpstra, P.; !1Lidstrom, M.E.; Dijkhuizen, L. !$#journal Mol. Gen. Genet. (1991) 225:320-330 !$#title Identification and organization of carbon dioxide fixation !1genes in Xanthobacter flavus H4-14. !$#cross-references MUID:91172133; PMID:1900916 !$#accession S13575 !'##molecule_type DNA !'##residues 1-317 ##label MEI !'##cross-references EMBL:X17252; NID:g48543; PIDN:CAA35117.1; !1PID:g48546 GENETICS !$#gene cfxQ CLASSIFICATION #superfamily cfxQ protein FEATURE !$91 #binding_site ATP (Lys) #status predicted SUMMARY #length 317 #molecular-weight 35147 #checksum 1497 SEQUENCE /// ENTRY BWSOGM #type complete TITLE gtfA protein - Streptococcus mutans ORGANISM #formal_name Streptococcus mutans DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jul-1999 ACCESSIONS S01972; S05068 REFERENCE S01972 !$#authors James, L.C.; Hughes, T.A.; Curtiss III, R. !$#journal Nucleic Acids Res. (1988) 16:10398 !$#title Nucleotide sequence of the gtfA gene from S. mutans GS-5. !$#cross-references MUID:89057509; PMID:3194228 !$#accession S01972 !'##molecule_type DNA !'##residues 1-487 ##label JAM !'##cross-references EMBL:X08057 REFERENCE S05068 !$#authors Hughes, T.A. !$#submission submitted to the EMBL Data Library, August 1988 !$#accession S05068 !'##molecule_type DNA !'##residues 1-4,'I',6-31,'A',33-392,'I',394-423,'I',425-442,'EN', !1445-487 ##label HUG !'##cross-references EMBL:X08057; NID:g47231; PIDN:CAA30846.1; !1PID:g47232 GENETICS !$#gene gtfA CLASSIFICATION #superfamily gtfA protein SUMMARY #length 487 #molecular-weight 56244 #checksum 8352 SEQUENCE /// ENTRY BVECLT #type complete TITLE bacteriophage T4 late gene expression-blocking protein - Escherichia coli (strain K-12) cryptic prophage e14 ORGANISM #formal_name Escherichia coli DATE 31-Mar-1990 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS H64858; A30386; Q00194 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64858 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-297 ##label BLAT !'##cross-references GB:AE000214; GB:U00096; NID:g1787382; !1PIDN:AAC74223.1; PID:g1787385; UWGP:b1139 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A30386 !$#authors Kao, C.; Snyder, L. !$#journal J. Bacteriol. (1988) 170:2056-2062 !$#title The lit gene product which blocks bacteriophage T4 late gene !1expression is a membrane protein encoded by a cryptic DNA !1element, e14. !$#cross-references MUID:88197991; PMID:2452152 !$#accession A30386 !'##molecule_type DNA !'##residues 1-120,'QVANHGL',128,'NV',131,'SQKH',136-297 ##label KAO !'##cross-references GB:M19634; NID:g146626; PIDN:AAA24074.1; !1PID:g146627 !'##experimental_source strain JM101 GENETICS !$#gene lit !$#map_position 25 min !$#genome cryptic prophage e14 FUNCTION !$#description interacts with a short DNA sequence of the major capsid !1protein gene of bacteriophage T4 and inhibits the expression !1of this late gene !$#note may interfere with coordination of protein synthesis and !1assembly of T4 heads CLASSIFICATION #superfamily bacteriophage T4 late gene expression blocking !1protein KEYWORDS transmembrane protein; zinc FEATURE !$61-82 #domain transmembrane #status predicted #label TM1\ !$149-178 #domain transmembrane #status predicted #label TM2\ !$160,164 #binding_site zinc (His) #status predicted\ !$161 #active_site Glu #status predicted SUMMARY #length 297 #molecular-weight 33762 #checksum 3482 SEQUENCE /// ENTRY BVECKB #type complete TITLE alkB protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 01-Mar-2002 ACCESSIONS A24605; B64991 REFERENCE A24605 !$#authors Kondo, H.; Nakabeppu, Y.; Kataoka, H.; Kuhara, S.; Kawabata, !1S.; Sekiguchi, M. !$#journal J. Biol. Chem. (1986) 261:15772-15777 !$#title Structure and expression of the alkB gene of Escherichia !1coli related to the repair of alkylated DNA. !$#cross-references MUID:87057220; PMID:3536913 !$#accession A24605 !'##molecule_type DNA !'##residues 1-216 ##label KON !'##cross-references GB:J02607; NID:g145193; PIDN:AAA23416.1; !1PID:g145195 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64991 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-216 ##label BLAT !'##cross-references GB:AE000310; GB:U00096; NID:g2367131; !1PIDN:AAC75272.1; PID:g1788541; UWGP:b2212 !'##experimental_source strain K-12, substrain MG1655 COMMENT The precise function of this protein is not known; however, !1it must be involved in some steps in the repair process of !1alkylated DNA. GENETICS !$#gene alkB !$#map_position 48 min CLASSIFICATION #superfamily alkB protein KEYWORDS DNA repair SUMMARY #length 216 #molecular-weight 24075 #checksum 5469 SEQUENCE /// ENTRY BVECAM #type complete TITLE membrane protein aroM - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS F64767; C25197; S41305 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64767 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-225 ##label BLAT !'##cross-references GB:AE000145; GB:U00096; NID:g1786580; !1PIDN:AAC73493.1; PID:g1786589; UWGP:b0390 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A91812 !$#authors DeFeyter, R.C.; Davidson, B.E.; Pittard, J. !$#journal J. Bacteriol. (1986) 165:233-239 !$#title Nucleotide sequence of the transcription unit containing the !1aroL and aroM genes from Escherichia coli K-12. !$#cross-references MUID:86085676; PMID:3001025 !$#accession C25197 !'##molecule_type DNA !'##residues 1-151,'W',153-154,'R',156-225 ##label DEF !'##cross-references GB:M13045; NID:g145381; PIDN:AAA83835.1; !1PID:g145383 !'##experimental_source strain K12 REFERENCE S41303 !$#authors Ryder, L.; Sharples, G.J.; Lloyd, R.G. !$#submission submitted to the EMBL Data Library, December 1993 !$#description Molecular and functional analysis of Tn1000 insertions in !1the aroLM-scbDC of the Escherichia coli K-12 chromosome. !$#accession S41305 !'##molecule_type DNA !'##residues 198-225 ##label RYD !'##cross-references EMBL:X76979; NID:g440401; PIDN:CAA54283.1; !1PID:g809685 GENETICS !$#gene aroM !$#map_position 9 min !$#note this protein of unknown function is encoded by a gene that !1is regulated by aroR and cotranscribes with the aroL gene, !1which codes for shikimate kinase II CLASSIFICATION #superfamily aroM protein KEYWORDS aromatic amino acid biosynthesis; transmembrane protein FEATURE !$5-21 #domain transmembrane #status predicted #label TM1\ !$209-225 #domain transmembrane #status predicted #label TM2 SUMMARY #length 225 #molecular-weight 24917 #checksum 945 SEQUENCE /// ENTRY BVECLA #type complete TITLE GTP-binding membrane protein lepA - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS H65034; A22627 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65034 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-599 ##label BLAT !'##cross-references GB:AE000343; GB:U00096; NID:g2367139; !1PIDN:AAC75622.1; PID:g1788922; UWGP:b2569 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A22627 !$#authors March, P.E.; Inouye, M. !$#journal J. Biol. Chem. (1985) 260:7206-7213 !$#title Characterization of the lep operon of Escherichia coli. !1Identification of the promoter and the gene upstream of the !1signal peptidase I gene. !$#cross-references MUID:85207751; PMID:2987248 !$#accession A22627 !'##molecule_type DNA !'##residues 1-52,'N',54-155,'HRRGALFSENRRWCAGRSR',156,'SGA',160,'H', !1162-163,'AGS',186-265,267-599 ##label MAR !'##note the authors translated the codon AAC for residue 53 as Thr COMMENT The overproduction of this protein is lethal to E. coli. It !1is present in the cytoplasmic membrane and is also found in !1the periplasm. Its gene is cotranscribed with the lep gene, !1which encodes for signal peptidase. GENETICS !$#gene lepA !$#map_position 55 min CLASSIFICATION #superfamily GTP-binding membrane protein lepA; translation !1elongation factor Tu homology KEYWORDS GTP binding; membrane protein; nucleotide binding; P-loop FEATURE !$5-134 #domain translation elongation factor Tu homology !8#label ETU\ !$11-18 #region nucleotide-binding motif A (P-loop)\ !$131-134 #region GTP-binding NKXD motif\ !$162-164 #region GTP-binding SAK/L motif\ !$17,18,53,131,132, !$134,162 #binding_site Mg-GTP (Lys, Ser, Thr, Asn, Lys, Asp, !8Ser) #status predicted SUMMARY #length 599 #molecular-weight 66570 #checksum 5922 SEQUENCE /// ENTRY FJEC #type complete TITLE transcription termination-antitermination factor nusA - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 17-May-1985 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS E65107; A03532; A38451 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65107 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-495 ##label BLAT !'##cross-references GB:AE000397; GB:U00096; NID:g2367199; !1PIDN:AAC76203.1; PID:g1789560; UWGP:b3169 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A93514 !$#authors Ishii, S.; Ihara, M.; Maekawa, T.; Nakamura, Y.; Uchida, H.; !1Imamoto, F. !$#journal Nucleic Acids Res. (1984) 12:3333-3342 !$#title The nucleotide sequence of the cloned nusA gene and its !1flanking region of Escherichia coli. !$#cross-references MUID:84193200; PMID:6326058 !$#accession A03532 !'##molecule_type DNA !'##residues 1-67,'I',69-166,'SCRVKT',173,'ALATAFVACSIPFA','RR',191-223, !1'F',225,'SGSRS',231,'FS',234-261,'GLLNWVASV',271-495 ##label !1ISH !'##cross-references GB:X00513; GB:K01175; NID:g42142 !'##note the authors translated the codon ATC for residue 68 as Val, TTC !1for residue 173 as Ser, TTT for residue 224 as Lys, CAG for !1residue 345 as His, and GCT for residue 346 as Gly REFERENCE A38451 !$#authors Ito, K.; Egawa, K.; Nakamura, Y. !$#journal J. Bacteriol. (1991) 173:1492-1501 !$#title Genetic interaction between the beta' subunit of RNA !1polymerase and the arginine-rich domain of Escherichia coli !1nusA protein. !$#cross-references MUID:91139592; PMID:1847365 !$#accession A38451 !'##molecule_type DNA !'##residues 1-495 ##label ITO GENETICS !$#gene nusA !$#map_position 69 min FUNCTION !$#description binds directly to the core enzyme of the DNA-dependent RNA !1polymerase, but not to the holoenzyme, and is required for !1in vitro transcription, along with the beta and beta' chains !1of the RNA polymerase; participates in the antitermination !1reaction mediated by the bacteriophage lambda N gene protein !1to prevent premature termination of transcription initiated !1at the early lambda promoters CLASSIFICATION #superfamily Escherichia coli transcription factor nusA; !1transcription termination factor nusA homology KEYWORDS transcription antitermination FEATURE !$64-339 #domain transcription termination factor nusA !8homology #label TTN SUMMARY #length 495 #molecular-weight 54870 #checksum 1151 SEQUENCE /// ENTRY A53377 #type complete TITLE transcription termination-antitermination factor nusA - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 25-Aug-1995 #sequence_revision 02-Jul-1998 #text_change 16-Jul-1999 ACCESSIONS A53377 REFERENCE A53377 !$#authors Craven, M.G.; Granston, A.E.; Schauer, A.T.; Zheng, C.; !1Gray, T.A.; Friedman, D.I. !$#journal J. Bacteriol. (1994) 176:1394-1404 !$#title Escherichia coli-Salmonella typhimurium hybrid nusA genes: !1identification of a short motif required for action of the !1lambda N transcription antitermination protein. !$#cross-references MUID:94156845; PMID:8113180 !$#accession A53377 !'##molecule_type DNA !'##residues 1-500 ##label CRA !'##cross-references GB:M61008; NID:g515636; PIDN:AAA20049.1; !1PID:g515637 FUNCTION !$#description binds directly to the core enzyme of the DNA-dependent RNA !1polymerase, but not to the holoenzyme, and is required for !1transcription in vitro, along with the beta and beta' chains !1of the RNA polymerase !$#note unlike the closely related E.coli protein, does not !1participate in the antitermination reaction mediated by the !1bacteriophage lambda N gene protein CLASSIFICATION #superfamily Escherichia coli transcription factor nusA; !1transcription termination factor nusA homology KEYWORDS transcription antitermination FEATURE !$64-344 #domain transcription termination factor nusA !8homology #label TTN SUMMARY #length 500 #molecular-weight 55469 #checksum 4594 SEQUENCE /// ENTRY D64114 #type complete TITLE transcription termination-antitermination factor nusA - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS D64114 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession D64114 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-507 ##label TIGR !'##cross-references GB:L42023; TIGR:HI1283 GENETICS !$#gene nusA FUNCTION !$#description essential for the in vitro synthesis of beta-galactosidase !1as well as the beta and beta' subunits of the RNA !1polymerase; participates in the antitermination reaction !1mediated by the bacteriophage lambda N gene protein to !1prevent premature termination of transcription initiated at !1the early lambda promoters CLASSIFICATION #superfamily Escherichia coli transcription factor nusA; !1transcription termination factor nusA homology KEYWORDS transcription antitermination FEATURE !$76-351 #domain transcription termination factor nusA !8homology #label TTN SUMMARY #length 507 #molecular-weight 56863 #checksum 9306 SEQUENCE /// ENTRY S74543 #type complete TITLE transcription termination factor nusA - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES hypothetical protein slr0743; N utilization substance protein A (nusA) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S74543 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74543 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-458 ##label KAN !'##cross-references EMBL:D90899; GB:AB001339; NID:g1651650; !1PIDN:BAA16695.1; PID:g1651767 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene nusA CLASSIFICATION #superfamily Escherichia coli transcription factor nusA; !1transcription termination factor nusA homology KEYWORDS transcription termination FEATURE !$79-370 #domain transcription termination factor nusA !8homology #label TTN SUMMARY #length 458 #molecular-weight 51330 #checksum 6955 SEQUENCE /// ENTRY QQMX2 #type complete TITLE probable transcription termination factor nusA - Methanococcus vannielii ORGANISM #formal_name Methanococcus vannielii DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS S06622 REFERENCE S06620 !$#authors Lechner, K.; Heller, G.; Boeck, A. !$#journal J. Mol. Evol. (1989) 29:20-27 !$#title Organization and nucleotide sequence of a transcriptional !1unit of Methanococcus vannielii comprising genes for protein !1synthesis elongation factors and ribosomal proteins. !$#cross-references MUID:89362493; PMID:2475640 !$#accession S06622 !'##molecule_type DNA !'##residues 1-173 ##label LEC !'##cross-references EMBL:X15970; NID:g44780; PIDN:CAA34088.1; !1PID:g44783 CLASSIFICATION #superfamily archaebacterial probable transcription !1termination factor nusA KEYWORDS transcription termination SUMMARY #length 173 #molecular-weight 19309 #checksum 2259 SEQUENCE /// ENTRY D64430 #type complete TITLE probable transcription termination factor nusA - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 13-Sep-1996 #sequence_revision 10-Jul-1998 #text_change 21-Jul-2000 ACCESSIONS D64430 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession D64430 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-183 ##label BUL !'##cross-references GB:U67547; GB:L77117; NID:g1591695; !1PIDN:AAB99049.1; PID:g1591699; TIGR:MJ1045 GENETICS !$#map_position FOR981967-982518 CLASSIFICATION #superfamily archaebacterial probable transcription !1termination factor nusA KEYWORDS transcription termination SUMMARY #length 183 #molecular-weight 21135 #checksum 3755 SEQUENCE /// ENTRY B69486 #type complete TITLE probable transcription termination factor nusA - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 05-Dec-1997 #sequence_revision 10-Jul-1998 #text_change 16-Jul-1999 ACCESSIONS B69486 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession B69486 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-139 ##label KLE !'##cross-references GB:AE000972; GB:AE000782; NID:g2689295; !1PIDN:AAB89363.1; PID:g2648654; TIGR:AF1891 CLASSIFICATION #superfamily archaebacterial probable transcription !1termination factor nusA KEYWORDS transcription termination SUMMARY #length 139 #molecular-weight 15273 #checksum 5102 SEQUENCE /// ENTRY B69007 #type complete TITLE probable transcription termination factor nusA - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 05-Dec-1997 #sequence_revision 10-Jul-1998 #text_change 16-Jul-1999 ACCESSIONS B69007 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession B69007 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-143 ##label MTH !'##cross-references GB:AE000876; GB:AE000666; NID:g2622140; !1PIDN:AAB85545.1; PID:g2622153 !'##experimental_source strain Delta H GENETICS !$#gene MTH1054 !$#start_codon GTG CLASSIFICATION #superfamily archaebacterial probable transcription !1termination factor nusA KEYWORDS transcription termination SUMMARY #length 143 #molecular-weight 15917 #checksum 2571 SEQUENCE /// ENTRY S18712 #type complete TITLE probable transcription termination factor nusA - Thermococcus celer ALTERNATE_NAMES hypothetical protein X (rpl30-rps12 intergenic region) ORGANISM #formal_name Thermococcus celer DATE 29-Jan-1993 #sequence_revision 10-Jul-1998 #text_change 16-Jul-1999 ACCESSIONS S18712; S25567 REFERENCE S18710 !$#authors Klenk, H.P.; Schwass, V.; Zillig, W. !$#journal Nucleic Acids Res. (1991) 19:6047 !$#title Nucleotide sequence of the genes encoding the L30, S12 and !1S7 equivalent ribosomal proteins from the archaeum !1Thermococcus celer. !$#cross-references MUID:92051399; PMID:1840672 !$#accession S18712 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-145 ##label KLE !'##cross-references EMBL:X60305; NID:g58408; PIDN:CAA42848.1; !1PID:g58411 !'##experimental_source DSM 2476 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1September 1991 CLASSIFICATION #superfamily archaebacterial probable transcription !1termination factor nusA KEYWORDS transcription termination SUMMARY #length 145 #molecular-weight 16461 #checksum 6412 SEQUENCE /// ENTRY S03579 #type complete TITLE probable transcription termination factor nusA - Halobacterium salinarum ORGANISM #formal_name Halobacterium salinarum DATE 01-Dec-1989 #sequence_revision 10-Jul-1998 #text_change 21-Jul-2000 ACCESSIONS S03579 REFERENCE S03572 !$#authors Leffers, H.; Gropp, F.; Lottspeich, F.; Zillig, W.; Garrett, !1R.A. !$#journal J. Mol. Biol. (1989) 206:1-17 !$#title Sequence, organization, transcription and evolution of RNA !1polymerase subunit genes from the archaebacterial extreme !1halophiles Halobacterium halobium and Halococcus morrhuae. !$#cross-references MUID:89199633; PMID:2495365 !$#accession S03579 !'##molecule_type DNA !'##residues 1-139 ##label LEF !'##cross-references EMBL:X57144; NID:g43538; PIDN:CAA40428.1; !1PID:g43544 !'##note the source is designated as Halobacterium halobium CLASSIFICATION #superfamily archaebacterial probable transcription !1termination factor nusA KEYWORDS transcription termination SUMMARY #length 139 #molecular-weight 14513 #checksum 1920 SEQUENCE /// ENTRY S03580 #type complete TITLE probable transcription termination factor nusA - Halococcus morrhuae ORGANISM #formal_name Halococcus morrhuae DATE 01-Dec-1989 #sequence_revision 10-Jul-1998 #text_change 16-Jul-1999 ACCESSIONS S03580 REFERENCE S03572 !$#authors Leffers, H.; Gropp, F.; Lottspeich, F.; Zillig, W.; Garrett, !1R.A. !$#journal J. Mol. Biol. (1989) 206:1-17 !$#title Sequence, organization, transcription and evolution of RNA !1polymerase subunit genes from the archaebacterial extreme !1halophiles Halobacterium halobium and Halococcus morrhuae. !$#cross-references MUID:89199633; PMID:2495365 !$#accession S03580 !'##molecule_type DNA !'##residues 1-139 ##label LEF !'##cross-references EMBL:X57145; NID:g43620; PIDN:CAA40433.1; !1PID:g43623 CLASSIFICATION #superfamily archaebacterial probable transcription !1termination factor nusA KEYWORDS transcription termination SUMMARY #length 139 #molecular-weight 14908 #checksum 2674 SEQUENCE /// ENTRY S04720 #type complete TITLE probable transcription termination factor nusA - Sulfolobus acidocaldarius ORGANISM #formal_name Sulfolobus acidocaldarius DATE 28-Feb-1990 #sequence_revision 10-Jul-1998 #text_change 16-Jul-1999 ACCESSIONS S04720 REFERENCE S04714 !$#authors Puehler, G.; Lottspeich, F.; Zillig, W. !$#journal Nucleic Acids Res. (1989) 17:4517-4534 !$#title Organization and nucleotide sequence of the genes encoding !1the large subunits A, B and C of the DNA-dependent RNA !1polymerase of the archaebacterium Sulfolobus acidocaldarius. !$#cross-references MUID:89315197; PMID:2501756 !$#accession S04720 !'##molecule_type DNA !'##residues 1-130 ##label PUE !'##cross-references EMBL:X14818; NID:g46667; PIDN:CAA32928.1; !1PID:g46673 CLASSIFICATION #superfamily archaebacterial probable transcription !1termination factor nusA KEYWORDS transcription termination SUMMARY #length 130 #molecular-weight 14533 #checksum 3475 SEQUENCE /// ENTRY S26725 #type complete TITLE probable transcription termination factor nusA - Thermoplasma acidophilum ALTERNATE_NAMES hypothetical protein X (rpoA2 3' region) ORGANISM #formal_name Thermoplasma acidophilum DATE 12-Feb-1993 #sequence_revision 10-Jul-1998 #text_change 16-Jul-1999 ACCESSIONS S26725 REFERENCE S26721 !$#authors Klenk, H.P.; Renner, O.; Schwass, V.; Zillig, W. !$#journal Nucleic Acids Res. (1992) 20:5226 !$#title Nucleotide sequence of the genes encoding the subunits H, B, !1A' and A'' of the DNA-dependent RNA polymerase and the !1initiator tRNA from Thermoplasma acidophilum. !$#cross-references MUID:93027268; PMID:1408839 !$#accession S26725 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-144 ##label KLE !'##cross-references EMBL:X68198; NID:g48089; PIDN:CAA48283.1; !1PID:g48094 !'##experimental_source DSM 1728 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1September 1992 CLASSIFICATION #superfamily archaebacterial probable transcription !1termination factor nusA KEYWORDS transcription termination SUMMARY #length 144 #molecular-weight 16776 #checksum 6417 SEQUENCE /// ENTRY FJECB #type complete TITLE transcription termination factor nusB [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES N utilization substance protein B ORGANISM #formal_name Escherichia coli DATE 17-Mar-1987 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS I51822; H64770; A93522; A93523; S26226; A03533; S19180 REFERENCE I51822 !$#authors Imamoto, F.; Nakamura, Y. !$#journal Adv. Biophys. (1986) 21:175-192 !$#title Escherichia coli proteins involved in regulation of !1transcription termination: Function, structure, and !1expression of the nusA and nusB genes. !$#cross-references MUID:86319526; PMID:3019094 !$#accession I51822 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-139 ##label IMA !'##cross-references GB:M26839; NID:g146975; PIDN:AAA24228.1; !1PID:g146976 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64770 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-139 ##label BLAT !'##cross-references GB:AE000148; GB:U00096; NID:g1786614; !1PIDN:AAC73519.1; PID:g1786618; UWGP:b0416 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A93522 !$#authors Swindle, J.; Ajioka, J.; Dawson, D.; Myers, R.; Carroll, D.; !1Georgopoulos, C. !$#journal Nucleic Acids Res. (1984) 12:4977-4985 !$#title The nucleotide sequence of the Escherichia coli K12 nusB !1(groNB) gene. !$#cross-references MUID:84247350; PMID:6330693 !$#accession A93522 !'##molecule_type DNA !'##residues 1-58,'S',60-139 ##label SWI REFERENCE A93523 !$#authors Ishii, S.; Hatada, E.; Maekawa, T.; Imamoto, F. !$#journal Nucleic Acids Res. (1984) 12:4987-4995 !$#title Molecular cloning and nucleotide sequencing of the nusB gene !1of Escherichia coli. !$#cross-references MUID:84247351; PMID:6330694 !$#accession A93523 !'##molecule_type DNA !'##residues 1-139 ##label ISH !'##cross-references GB:X00681; GB:X00684; NID:g42152; PIDN:CAA25289.1; !1PID:g581149 REFERENCE S26200 !$#authors Taura, T.; Ueguchi, C.; Shiba, K.; Ito, K. !$#journal Mol. Gen. Genet. (1992) 234:429-432 !$#title Insertional disruption of the nusB (ssyB) gene leads to !1cold-sensitive growth of Escherichia coli and suppression of !1the secY24 mutation. !$#cross-references MUID:93024316; PMID:1406588 !$#accession S26226 !'##molecule_type DNA !'##residues 1-139 ##label TAU !'##cross-references EMBL:X64395; NID:g42147; PIDN:CAA45737.1; !1PID:g581148 !'##experimental_source strain K-12 REFERENCE A76704 !$#authors Huenges, M.; Roelz, C.; Gschwind, R.M.; Peteranderl, R.; !1Berglechner, F.; Richter, G.; Bacher, A.; Kessler, H.; !1Gemmecker, G. !$#submission submitted to the Protein Data Bank, April 1998 !$#cross-references PDB:1BAQ !$#contents annotation; conformation by (1)H-, (13)C-, and (15)N-NMR, !1residues 1-139 REFERENCE A59244 !$#authors Huenges, M.; Rolz, C.; Gschwind, R.; Peteranderl, R.; !1Berglechner, F.; Richter, G.; Bacher, A.; Kessler, H.; !1Gemmecker, G. !$#journal EMBO J. (1998) 17:4092-4100 !$#title Solution structure of the antitermination protein nusb of !1escherichia coli: a novel all-helical fold for an !1RNA-binding protein. !$#cross-references MUID:98336198; PMID:9670024 !$#contents annotation; conformation by (1)H-, (13)C-, and (15)N-NMR GENETICS !$#gene nusB; ssyB; groNB !$#map_position 10 min !$#start_codon GTG FUNCTION !$#description essential for the formation of the RNA polymerase !1antitermination complex in the presence of lambda phage N !1protein; involved in the transcription termination process !1at certain sites during normal bacterial growth CLASSIFICATION #superfamily nusB protein KEYWORDS RNA binding; transcription antitermination SUMMARY #length 139 #molecular-weight 15689 #checksum 5293 SEQUENCE /// ENTRY BVECGX #type complete TITLE glycogen operon protein glgX (EC 3.2.1.-) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS B65139; JT0400 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65139 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-657 ##label BLAT !'##cross-references GB:AE000419; GB:U00096; NID:g2367227; !1PIDN:AAC76456.1; PID:g2367229; UWGP:b3431 !'##experimental_source strain K-12, substrain MG1655 REFERENCE JT0418 !$#authors Romeo, T.; Kumar, A.; Preiss, J. !$#journal Gene (1988) 70:363-376 !$#title Analysis of the Escherichia coli glycogen gene cluster !1suggests that catabolic enzymes are encoded among the !1biosynthetic genes. !$#cross-references MUID:89108020; PMID:2975249 !$#accession JT0400 !'##molecule_type DNA !'##residues 1-288,'Y',289-506 ##label ROM !'##cross-references GB:J01616; NID:g146134; PIDN:AAA98735.1; !1PID:g146135 !'##experimental_source strain K12 COMMENT This protein is similar to several glucan hydrolases and !1transferases. It is part of the glycogen biosynthetic/ !1catabolic operon but is not required for glycogen synthesis. GENETICS !$#gene glgX !$#map_position 75 min CLASSIFICATION #superfamily glyX protein KEYWORDS glycosidase; hydrolase FEATURE !$336,443 #active_site Asp #status predicted SUMMARY #length 657 #molecular-weight 73576 #checksum 344 SEQUENCE /// ENTRY BVECVB #type complete TITLE DNA-binding protein ruvB - Escherichia coli (strain K-12) ALTERNATE_NAMES Holliday junction DNA helicase ruvB ORGANISM #formal_name Escherichia coli DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 01-Mar-2002 ACCESSIONS B28533; B32358; D64948 REFERENCE A93681 !$#authors Benson, F.E.; Illing, G.T.; Sharples, G.J.; Lloyd, R.G. !$#journal Nucleic Acids Res. (1988) 16:1541-1549 !$#title Nucleotide sequencing of the ruv region of Escherichia coli !1K-12 reveals a lexA regulated operon encoding two genes. !$#cross-references MUID:88157713; PMID:3279394 !$#accession B28533 !'##molecule_type DNA !'##residues 1-336 ##label BEN !'##cross-references GB:X07091; NID:g42901; PIDN:CAA30120.1; PID:g42903 REFERENCE A32358 !$#authors Shinagawa, H.; Makino, K.; Amemura, M.; Kimura, S.; Iwasaki, !1H.; Nakata, A. !$#journal J. Bacteriol. (1988) 170:4322-4329 !$#title Structure and regulation of the Escherichia coli ruv operon !1involved in DNA repair and recombination. !$#cross-references MUID:88314937; PMID:2842314 !$#accession B32358 !'##molecule_type DNA !'##residues 1-336 ##label SHI !'##cross-references GB:M21298; NID:g147781; PIDN:AAA24613.1; !1PID:g147783 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64948 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-336 ##label BLAT !'##cross-references GB:AE000280; GB:U00096; NID:g1788163; !1PIDN:AAC74930.1; PID:g1788167; UWGP:b1860 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ruvB !$#map_position 41 min COMPLEX two hexameric rings of RuvB protein and two tetramers of !1RuvA protein FUNCTION !$#description ATPase activity; promotes movement of RuvA/RuvB-complex !1along DNA; RuvA and RuvB form a complex that interacts with !1Holliday junctions and promotes branch migration; involved !1together with RuvA and RuvC in late stages of homologous !1genetic recombination and DNA repair !$#note SOS inducible; regulated by LexA CLASSIFICATION #superfamily ruvB protein KEYWORDS ATP; DNA binding; DNA recombination; DNA repair; !1homohexamer; magnesium; nucleotide binding; P-loop; SOS !1response FEATURE !$62-69 #region nucleotide-binding motif A (P-loop)\ !$109-114 #region nucleotide-binding motif B SUMMARY #length 336 #molecular-weight 37173 #checksum 2879 SEQUENCE /// ENTRY IQECDA #type complete TITLE replication initiation protein dnaA - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 13-Jun-1983 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS G65172; A03534; A24944 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65172 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-467 ##label BLAT !'##cross-references GB:AE000447; GB:U00096; NID:g2367266; !1PIDN:AAC76725.1; PID:g2367267; UWGP:b3702 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A93450 !$#authors Hansen, E.B.; Hansen, F.G.; von Meyenburg, K. !$#journal Nucleic Acids Res. (1982) 10:7373-7385 !$#title The nucleotide sequence of the dnaA gene and the first part !1of the dnaN gene of Escherichia coli K-12. !$#cross-references MUID:83116961; PMID:6296774 !$#accession A03534 !'##molecule_type DNA !'##residues 1-68,'RI',71-467 ##label HAN !'##cross-references GB:J01602 !'##experimental_source strain K12 REFERENCE A91510 !$#authors Ohmori, H.; Kimura, M.; Nagata, T.; Sakakibara, Y. !$#journal Gene (1984) 28:159-170 !$#title Structural analysis of the dnaA and dnaN genes of !1Escherichia coli. !$#cross-references MUID:84237568; PMID:6234204 !$#accession A24944 !'##molecule_type DNA !'##residues 1-467 ##label OHM !'##cross-references GB:J01602; NID:g145758; PIDN:AAB59149.1; !1PID:g145760 GENETICS !$#gene dnaA !$#map_position 83 min !$#start_codon GTG CLASSIFICATION #superfamily replication initiation protein dnaA KEYWORDS ATP; DNA binding; DNA biosynthesis; nucleotide binding; !1P-loop; replication initiation FEATURE !$172-179 #region nucleotide-binding motif A (P-loop)\ !$231-235 #region nucleotide-binding motif B SUMMARY #length 467 #molecular-weight 52550 #checksum 2635 SEQUENCE /// ENTRY IQEBV #type complete TITLE replication initiation protein dnaA - Proteus mirabilis ORGANISM #formal_name Proteus mirabilis DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 19-Jan-2001 ACCESSIONS JQ0733 REFERENCE JQ0729 !$#authors Skovgaard, O. !$#journal Gene (1990) 93:27-34 !$#title Nucleotide sequence of a Proteus mirabilis DNA fragment !1homologous to the 60K-rnpA-rpmH-dnaA-dnaN-recF-gyrB region !1of Escherichia coli. !$#cross-references MUID:91033012; PMID:2172087 !$#accession JQ0733 !'##molecule_type DNA !'##residues 1-466 ##label SKO !'##cross-references GB:M58352; GB:M31295; NID:g150873; PIDN:AAA83958.1; !1PID:g150878 !'##experimental_source strain LM1509 !'##note the authors translated the codon CAA for residue 237 as Glu GENETICS !$#gene dnaA !$#start_codon GTG CLASSIFICATION #superfamily replication initiation protein dnaA KEYWORDS ATP; DNA binding; DNA biosynthesis; nucleotide binding; !1P-loop; replication initiation FEATURE !$171-178 #region nucleotide-binding motif A (P-loop)\ !$230-234 #region nucleotide-binding motif B SUMMARY #length 466 #molecular-weight 52974 #checksum 6379 SEQUENCE /// ENTRY IQJVBA #type complete TITLE replication initiation protein dnaA - Buchnera aphidicola ORGANISM #formal_name Buchnera aphidicola DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 19-Jan-2001 ACCESSIONS JC1158 REFERENCE JC1154 !$#authors Lai, C.Y.; Baumann, P. !$#journal Gene (1992) 113:175-181 !$#title Genetic analysis of an aphid endosymbiont DNA fragment !1homologous to the rnpA-rpmH-dnaA-dnaN-gyrB region of !1eubacteria. !$#cross-references MUID:92241666; PMID:1572539 !$#accession JC1158 !'##molecule_type DNA !'##residues 1-454 ##label LAI !'##cross-references GB:M80817 GENETICS !$#gene dnaA CLASSIFICATION #superfamily replication initiation protein dnaA KEYWORDS ATP; DNA binding; DNA biosynthesis; nucleotide binding; !1P-loop; replication initiation FEATURE !$159-166 #region nucleotide-binding motif A (P-loop)\ !$218-222 #region nucleotide-binding motif B SUMMARY #length 454 #molecular-weight 52526 #checksum 7786 SEQUENCE /// ENTRY IQPSP #type complete TITLE replication initiation protein dnaA - Pseudomonas putida ORGANISM #formal_name Pseudomonas putida DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 19-Jan-2001 ACCESSIONS JV0001; S20984; D34835 REFERENCE JV0002 !$#authors Fujita, M.Q.; Yoshikawa, H.; Ogasawara, N. !$#journal Mol. Gen. Genet. (1989) 215:381-387 !$#title Structure of the dnaA region of Pseudomonas putida: !1conservation among three bacteria, Bacillus subtilis, !1Escherichia coli and P. putida. !$#cross-references MUID:89218947; PMID:2540413 !$#accession JV0001 !'##molecule_type DNA !'##residues 1-506 ##label FUJ !'##cross-references GB:X14791; NID:g45689; PIDN:CAA32893.1; PID:g581460 REFERENCE S20984 !$#authors Ingmer, H.; Atlung, T. !$#journal Mol. Gen. Genet. (1992) 232:431-439 !$#title Expression and regulation of a dnaA homologue isolated from !1Pseudomonas putida. !$#cross-references MUID:92269764; PMID:1588913 !$#accession S20984 !'##molecule_type DNA !'##residues 1-26 ##label ING REFERENCE A34835 !$#authors Yee, T.W.; Smith, D.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:1278-1282 !$#title Pseudomonas chromosomal replication origins: a bacterial !1class distinct from Escherichia coli-type origins. !$#cross-references MUID:90160310; PMID:2106132 !$#accession D34835 !'##molecule_type DNA !'##residues 1-7 ##label YEE !'##cross-references GB:M30126; NID:g151422; PIDN:AAA25918.1; !1PID:g551935 GENETICS !$#gene dnaA CLASSIFICATION #superfamily replication initiation protein dnaA KEYWORDS ATP; DNA binding; DNA biosynthesis; nucleotide binding; !1P-loop; replication initiation FEATURE !$211-218 #region nucleotide-binding motif A (P-loop)\ !$270-274 #region nucleotide-binding motif B SUMMARY #length 506 #molecular-weight 56473 #checksum 937 SEQUENCE /// ENTRY IQBSOC #type complete TITLE replication initiation protein dnaA - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 19-Jan-2001 ACCESSIONS A22930; S66031; I40391; I40392; H69616; S12806 REFERENCE A94702 !$#authors Moriya, S.; Ogasawara, N.; Yoshikawa, H. !$#journal Nucleic Acids Res. (1985) 13:2251-2265 !$#title Structure and function of the region of the replication !1origin of the Bacillus subtilis chromosome. III. Nucleotide !1sequence of some 10,000 base pairs in the origin region. !$#cross-references MUID:85215612; PMID:2987847 !$#accession A22930 !'##molecule_type DNA !'##residues 1-446 ##label MOR !'##cross-references EMBL:X02369; NID:g40012; PIDN:CAA26217.1; !1PID:g40014 REFERENCE S65967 !$#authors Ogasawara, N.; Nakai, S.; Yoshikawa, H. !$#journal DNA Res. (1994) 1:1-14 !$#title Systematic sequencing of the 180 kilobase region of the !1Bacillus subtilis chromosome containing the replication !1origin. !$#cross-references MUID:96051385; PMID:7584024 !$#accession S66031 !'##status preliminary !'##molecule_type DNA !'##residues 1-446 ##label OGA !'##cross-references EMBL:D26185; NID:g467326; PIDN:BAA05237.1; !1PID:g467391 REFERENCE I40391 !$#authors Moriya, S.; Fukuoka, T.; Ogasawara, N.; Yoshikawa, H. !$#journal EMBO J. (1988) 7:2911-2917 !$#title Regulation of initiation of the chromosomal replication by !1DnaA-boxes in the origin region of the Bacillus subtilis !1chromosome. !$#cross-references MUID:89030659; PMID:2846289 !$#accession I40391 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-6 ##label RES !'##cross-references EMBL:X12778; NID:g39877; PIDN:CAA31269.1; !1PID:g580852 !$#accession I40392 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 441-446 ##label RE2 !'##cross-references EMBL:X12779; NID:g39878; PIDN:CAA31270.1; !1PID:g809659 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69616 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-446 ##label KUN !'##cross-references GB:Z99104; GB:AL009126; NID:g2632267; !1PIDN:CAB11777.1; PID:g2632268 !'##experimental_source strain 168 GENETICS !$#gene dnaA !$#map_position 0 CLASSIFICATION #superfamily replication initiation protein dnaA KEYWORDS ATP; DNA binding; nucleotide binding; P-loop FEATURE !$151-158 #region nucleotide-binding motif A (P-loop)\ !$210-214 #region nucleotide-binding motif B SUMMARY #length 446 #molecular-weight 50859 #checksum 9945 SEQUENCE /// ENTRY IQMCL #type complete TITLE replication initiation protein dnaA - Micrococcus luteus ORGANISM #formal_name Micrococcus luteus, Micrococcus lysodeikticus DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 19-Jan-2001 ACCESSIONS JQ0739 REFERENCE JQ0737 !$#authors Fujita, M.Q.; Yoshikawa, H.; Ogasawara, N. !$#journal Gene (1990) 93:73-78 !$#title Structure of the dnaA region of Micrococcus luteus: !1conservation and variations among eubacteria. !$#cross-references MUID:91033019; PMID:2172090 !$#accession JQ0739 !'##molecule_type DNA !'##residues 1-515 ##label FUJ !'##cross-references GB:M34006; NID:g149845; PIDN:AAA25315.1; !1PID:g149848 GENETICS !$#gene dnaA CLASSIFICATION #superfamily replication initiation protein dnaA KEYWORDS ATP; DNA binding; DNA biosynthesis; nucleotide binding; !1P-loop; replication initiation FEATURE !$214-221 #region nucleotide-binding motif A (P-loop)\ !$273-277 #region nucleotide-binding motif B SUMMARY #length 515 #molecular-weight 56876 #checksum 242 SEQUENCE /// ENTRY IQYMC #type complete TITLE replication initiation protein dnaA - Mycoplasma capricolum ALTERNATE_NAMES protein MC070 ORGANISM #formal_name Mycoplasma capricolum DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 19-Jan-2001 ACCESSIONS JN0272; S77809; JU0398 REFERENCE JN0272 !$#authors Fujita, M.Q.; Yoshikawa, H.; Ogasawara, N. !$#journal Gene (1992) 110:17-23 !$#title Structure of the dnaA and DnaA-box region in the Mycoplasma !1capricolum chromosome: conservation and variations in the !1course of evolution. !$#cross-references MUID:92184110; PMID:1544573 !$#accession JN0272 !'##molecule_type DNA !'##residues 1-450 ##label FUJ !'##cross-references DDBJ:D90426; NID:g216793; PIDN:BAA14415.1; !1PID:g216795 REFERENCE S77739 !$#authors Bork, P.; Ouzounis, C.; Casari, G.; Schneider, R.; Sander, !1C.; Dolan, M.; Gilbert, W.; Gillevet, P.M. !$#journal Mol. Microbiol. (1995) 16:955-967 !$#title Exploring the Mycoplasma capricolum genome: a minimal cell !1reveals its physiology. !$#cross-references MUID:96059641; PMID:7476192 !$#accession S77809 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 181-185,'X',187-195,'X',197-221,'X',223-239,'X',241,'X', !1243-417,'NSY' ##label BOR !'##cross-references EMBL:Z33057 !'##experimental_source ATCC 27343 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1994 GENETICS !$#gene dnaA !$#genetic_code SGC3 CLASSIFICATION #superfamily replication initiation protein dnaA KEYWORDS ATP; DNA binding; DNA biosynthesis; nucleotide binding; !1P-loop; replication initiation FEATURE !$148-155 #region nucleotide-binding motif A (P-loop)\ !$209-213 #region nucleotide-binding motif B SUMMARY #length 450 #molecular-weight 51764 #checksum 3548 SEQUENCE /// ENTRY IQBS44 #type complete TITLE primosome component (helicase loader) dnaI - Bacillus subtilis ALTERNATE_NAMES dnaA protein homolog, 44K; hypothetical protein Y (dnaB 3' region) ORGANISM #formal_name Bacillus subtilis DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 19-Jan-2001 ACCESSIONS B24720; C26580; F69617 REFERENCE A93650 !$#authors Ogasawara, N.; Moriya, S.; Mazza, P.G.; Yoshikawa, H. !$#journal Nucleic Acids Res. (1986) 14:9989-9999 !$#title Nucleotide sequence and organization of dnaB gene and !1neighbouring genes on the Bacillus subtilis chromosome. !$#cross-references MUID:87117549; PMID:3027671 !$#accession B24720 !'##molecule_type DNA !'##residues 1-311 ##label OGA !'##cross-references GB:X04963; NID:g39880; PIDN:CAA28633.1; PID:g39881 REFERENCE A94709 !$#authors Hoshino, T.; McKenzie, T.; Schmidt, S.; Tanaka, T.; Sueoka, !1N. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:653-657 !$#title Nucleotide sequence of Bacillus subtilis dnaB: a gene !1essential for DNA replication initiation and membrane !1attachment. !$#cross-references MUID:87118226; PMID:3027697 !$#accession C26580 !'##molecule_type DNA !'##residues 1-18,'N',20-23,'T',25-206 ##label HOS REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69617 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-311 ##label KUN !'##cross-references GB:Z99118; GB:AL009126; NID:g2635200; !1PIDN:CAB14858.1; PID:g2635363 !'##experimental_source strain 168 GENETICS !$#gene dnaI CLASSIFICATION #superfamily 44K dnaA protein homolog KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$168-175 #region nucleotide-binding motif A (P-loop) SUMMARY #length 311 #molecular-weight 36114 #checksum 530 SEQUENCE /// ENTRY IQECDB #type complete TITLE replicative DNA helicase (EC 3.6.1.-) DnaB - Escherichia coli (strain K-12) ALTERNATE_NAMES helicase ORGANISM #formal_name Escherichia coli DATE 25-Feb-1985 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS C65213; S45528; A03535 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65213 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-471 ##label BLAT !'##cross-references GB:AE000478; GB:U00096; NID:g2367339; !1PIDN:AAC77022.1; PID:g1790486; UWGP:b4052 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S45528 !$#authors Dixon, N.E.; Lilley, P.E. !$#submission submitted to the EMBL Data Library, September 1992 !$#description E. coli homolog of zeta crystallin. !$#accession S45528 !'##molecule_type DNA !'##residues 1-156 ##label DIX !'##cross-references EMBL:L02312 REFERENCE A03535 !$#authors Nakayama, N.; Arai, N.; Bond, M.W.; Kaziro, Y.; Arai, K. !$#journal J. Biol. Chem. (1984) 259:97-101 !$#title Nucleotide sequence of dnaB and the primary structure of the !1dnaB protein from Escherichia coli. !$#cross-references MUID:84161990; PMID:6323420 !$#accession A03535 !'##molecule_type DNA !'##residues 2-471 ##label NAK !'##cross-references GB:K01174; NID:g145762; PIDN:AAA23689.1; !1PID:g145763 !'##note initiator Met not shown COMMENT The active dnaB molecule, a hexamer of identical chains, !1participates in initiation and elongation during chromosome !1replication; it exhibits DNA-dependent ATPase activity and !1contains distinct active sites for ATP binding, DNA binding, !1and interaction with dnaC protein, primase, and other !1prepriming proteins. GENETICS !$#gene dnaB !$#map_position 92 min CLASSIFICATION #superfamily phage P22 gene 12 protein KEYWORDS ATP; DNA binding; homohexamer; hydrolase SUMMARY #length 471 #molecular-weight 52390 #checksum 3923 SEQUENCE /// ENTRY A32011 #type complete TITLE dnaB protein - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A32011 REFERENCE A32011 !$#authors Wong, A.; Kean, L.; Maurer, R. !$#journal J. Bacteriol. (1988) 170:2668-2675 !$#title Sequence of the dnaB gene of Salmonella typhimurium. !$#cross-references MUID:88227847; PMID:2836367 !$#accession A32011 !'##molecule_type DNA !'##residues 1-470 ##label WON !'##note initiator Met not shown GENETICS !$#gene dnaB CLASSIFICATION #superfamily phage P22 gene 12 protein KEYWORDS DNA binding SUMMARY #length 470 #molecular-weight 52556 #checksum 5693 SEQUENCE /// ENTRY D64130 #type complete TITLE dnaB protein - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES replicative DNA helicase ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS D64130 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession D64130 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-504 ##label TIGR !'##cross-references GB:U32831; GB:L42023; NID:g1574407; !1PIDN:AAC23217.1; PID:g1574411; TIGR:HI1574 GENETICS !$#gene dnaB !$#start_codon GTG CLASSIFICATION #superfamily phage P22 gene 12 protein KEYWORDS DNA binding SUMMARY #length 504 #molecular-weight 56811 #checksum 6387 SEQUENCE /// ENTRY Z2BPC2 #type complete TITLE gene 12 protein - phage P22 ALTERNATE_NAMES replication protein ORGANISM #formal_name phage P22 #note host Salmonella typhimurium DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 24-Sep-1999 ACCESSIONS A03536 REFERENCE A91518 !$#authors Backhaus, H.; Petri, J.B. !$#journal Gene (1984) 32:289-303 !$#title Sequence analysis of a region from the early right operon in !1phage P22 including the replication genes 18 and 12. !$#cross-references MUID:85155495; PMID:6241581 !$#accession A03536 !'##molecule_type DNA !'##residues 1-458 ##label BAC !'##cross-references GB:M10074; NID:g215307; PIDN:AAA32276.1; !1PID:g215311 COMMENT This protein is related to the dnaB protein of E. coli. GENETICS !$#gene 12 CLASSIFICATION #superfamily phage P22 gene 12 protein KEYWORDS DNA binding; replication SUMMARY #length 458 #molecular-weight 50127 #checksum 1836 SEQUENCE /// ENTRY XMECNC #type complete TITLE DNA replication protein dnaC - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 01-Mar-2002 ACCESSIONS A28484; S56588; B25124; C65251 REFERENCE A92600 !$#authors Nakayama, N.; Bond, M.W.; Miyajima, A.; Kobori, J.; Arai, K. !$#journal J. Biol. Chem. (1987) 262:10475-10480 !$#title Structure of Escherichia coli dnaC. Identification of a !1cysteine residue possibly involved in association with dnaB !1protein. !$#cross-references MUID:87280100; PMID:3301836 !$#accession A28484 !'##molecule_type DNA !'##residues 1-245 ##label NAK REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56588 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-5,'D',7-245 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97260.1; !1PID:g537204 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A94085 !$#authors Masai, H.; Bond, M.W.; Arai, K.I. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:1256-1260 !$#title Cloning of the Escherichia coli gene for primosomal protein !1i: the relationship to dnaT, essential for chromosomal DNA !1replication. !$#cross-references MUID:86149284; PMID:3006041 !$#accession B25124 !'##molecule_type DNA !'##residues 1-14 ##label MAS !'##cross-references GB:J04030; GB:J02785; GB:M13005; NID:g145788 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65251 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-5,'D',7-245 ##label BLAT !'##cross-references GB:AE000507; GB:U00096; NID:g2367380; !1PIDN:AAC77317.1; PID:g1790823; UWGP:b4361 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene dnaC !$#map_position 99 min FUNCTION !$#description this protein is one of the components of the prepriming !1protein complex, which combines with primase on the specific !1site of the template DNA to form the primosome that primes !1the single-stranded DNA for DNA polymerase reaction !$#pathway DNA biosynthesis CLASSIFICATION #superfamily DNA replication protein dnaC KEYWORDS DNA biosynthesis; P-loop FEATURE !$106-113 #region nucleotide-binding motif A (P-loop) #status !8atypical\ !$165-169 #region nucleotide-binding motif B SUMMARY #length 245 #molecular-weight 27891 #checksum 4440 SEQUENCE /// ENTRY C64886 #type complete TITLE DNA replication protein dnaC homolog - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 12-Sep-1997 #sequence_revision 17-Sep-1997 #text_change 01-Mar-2002 ACCESSIONS C64886; T09181 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64886 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-248 ##label BLAT !'##cross-references GB:AE000233; GB:U00096; NID:g1787613; !1PIDN:AAC74442.1; PID:g1787623; UWGP:b1360 !'##experimental_source strain K-12, substrain MG1655 REFERENCE Z16603 !$#authors Aiba, H.; Baba, T.; Fujita, K.; Hayashi, K.; Inada, T.; !1Isono, K.; Itoh, T.; Kasai, H.; Kashimoto, K.; Kimura, S.; !1Kitakawa, M.; Kitagawa, M.; Makino, K.; Miki, T.; Mizobuchi, !1K.; Mori, H.; Mori, T.; Motomura, K.; Nakade, S.; Nakamura, !1Y.; Nashimoto, H.; Nishio, Y.; Oshima, T.; Saito, N.; !1Sampei, G.; Seki, Y.; Sivasundaram, S.; Tagami, H.; Takeda, !1J.; Takemoto, K.; Takeuchi, Y.; Wada, C.; Yamamoto, Y.; !1Horiuchi, T. !$#journal DNA Res. (1996) 3:363-377 !$#title A 570-kb DNA sequence of the Escherichia coli K-12 genome !1corresponding to the 28.0-40.1 min region on the linkage !1map. !$#cross-references MUID:97251357; PMID:9097039 !$#accession T09181 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-248 ##label AIB !'##cross-references EMBL:D90774; NID:g1742217; PIDN:BAA14958.1; !1PID:g1742225 CLASSIFICATION #superfamily DNA replication protein dnaC KEYWORDS nucleotide binding; P-loop FEATURE !$108-115 #region nucleotide-binding motif A (P-loop) #status !8atypical\ !$166-170 #region nucleotide-binding motif B SUMMARY #length 248 #molecular-weight 28128 #checksum 9979 SEQUENCE /// ENTRY BVECIT #type complete TITLE istB protein - Escherichia coli plasmid R68.45 insertion sequence IS21 ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jul-1999 ACCESSIONS JV0013 REFERENCE A93128 !$#authors Reimmann, C.; Moore, R.; Little, S.; Savioz, A.; Willetts, !1N.S.; Haas, D. !$#journal Mol. Gen. Genet. (1989) 215:416-424 !$#title Genetic structure, function and regulation of the !1transposable element IS21. !$#cross-references MUID:89218951; PMID:2540414 !$#accession JV0013 !'##molecule_type DNA !'##residues 1-265 ##label REI !'##cross-references GB:X14793; NID:g41826; PIDN:CAA32899.1; PID:g41828 COMMENT The istB protein, one of two proteins expressed only when !1there is a tandem repeat of the IS21 insertion sequence, is !1necessary for the transposition of plasmids with that tandem !1repeat (such as plasmid R68.45, which is derived from tandem !1duplication of IS21 on plasmid R68). GENETICS !$#gene istB !$#genome plasmid R68.45 !$#mobile_element insertion sequence IS21 CLASSIFICATION #superfamily DNA replication protein dnaC KEYWORDS nucleotide binding; P-loop FEATURE !$104-111 #region nucleotide-binding motif A (P-loop)\ !$161-165 #region nucleotide-binding motif B SUMMARY #length 265 #molecular-weight 30529 #checksum 6112 SEQUENCE /// ENTRY IQECQ #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) III epsilon chain - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 18-Apr-1984 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS A64746; A03537; A24257 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64746 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-243 ##label BLAT !'##cross-references GB:AE000130; GB:U00096; NID:g1786402; !1PIDN:AAC73320.1; PID:g1786409; UWGP:b0215 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A93979 !$#authors Maki, H.; Horiuchi, T.; Sekiguchi, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:7137-7141 !$#title Structure and expression of the dnaQ mutator and the RNas H !1genes of Escherichia coli: overlap of the promoter regions. !$#cross-references MUID:84070781; PMID:6316347 !$#accession A03537 !'##molecule_type DNA !'##residues 1-24,'S',26-69,'VD',72-83,'V',85-118,'A',120-243 ##label !1MAK REFERENCE A24257 !$#authors Cox, E.C.; Horner, D.L. !$#journal J. Mol. Biol. (1986) 190:113-117 !$#title DNA sequence and coding properties of mutD(dnaQ) a dominant !1Escherichia coli mutator gene. !$#cross-references MUID:87060973; PMID:3023634 !$#accession A24257 !'##molecule_type DNA !'##residues 1-243 ##label COX !'##cross-references GB:X04027; NID:g42061; PIDN:CAA27661.1; PID:g42063 GENETICS !$#gene dnaQ !$#map_position 5 min COMPLEX DNA polymerase III is a multichain complex; alpha, epsilon, !1theta, tau, gamma, delta, delta', psi, chi and beta chains FUNCTION GEN !$#description DNA synthesis; synthesizes both, the lagging and the leading !1strands in E.coli !$#pathway DNA biosynthesis !$#note core enzyme (catalytic core) contains chains alpha, epsilon !1and theta; alpha chain has basic ability to synthesize DNA !1and theta chain is may be required for assembly; tau allows !1dimerization of the core complex and processivity is !1increased; the addition of the gamma/delta complex generates !1Pol III'-complex; gamma/delta complex binds template; the !1holoenzyme is completed by addition of beta chain which !1clamps the enzyme to DNA FUNCTION EPS !$#description has 3'-5' proofreading exonuclease activity CLASSIFICATION #superfamily dnaQ protein KEYWORDS DNA biosynthesis; DNA replication initiation; !1nucleotidyltransferase SUMMARY #length 243 #molecular-weight 27099 #checksum 4448 SEQUENCE /// ENTRY BVECCX #type complete TITLE membrane protein cynX - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1990 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS E64761; C31977; JS0144 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64761 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-384 ##label BLAT !'##cross-references GB:AE000141; GB:U00096; NID:g1786532; !1PIDN:AAC73444.1; PID:g1786536; UWGP:b0341 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A92672 !$#authors Sung, Y.; Fuchs, J.A. !$#journal J. Biol. Chem. (1988) 263:14769-14775 !$#title Characterization of the cyn operon in Escherichia coli K12. !$#cross-references MUID:89008347; PMID:3049588 !$#accession C31977 !'##molecule_type DNA !'##residues 1-26,'A',28-335,'PR','G',356,'L',358,'C',360-362,'SAA',366, !1'T' ##label SUN !'##cross-references GB:M23219; NID:g145641; PIDN:AAA23627.1; !1PID:g145644 !'##experimental_source strain K12 GENETICS !$#gene cynX !$#map_position 8 min !$#note part of the cyn operon FUNCTION !$#description belongs to a cyanate transport system CLASSIFICATION #superfamily cynX protein KEYWORDS transmembrane protein FEATURE !$1-17 #domain transmembrane #status predicted #label TM1\ !$36-52 #domain transmembrane #status predicted #label TM2\ !$68-84 #domain transmembrane #status predicted #label TM3\ !$89-105 #domain transmembrane #status predicted #label TM4\ !$235-251 #domain transmembrane #status predicted #label TM5\ !$263-279 #domain transmembrane #status predicted #label TM6\ !$291-307 #domain transmembrane #status predicted #label TM7\ !$321-337 #domain transmembrane #status predicted #label TM8\ !$358-374 #domain transmembrane #status predicted #label TM9 SUMMARY #length 384 #molecular-weight 41360 #checksum 3322 SEQUENCE /// ENTRY E64822 #type complete TITLE probable membrane protein b0845 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS E64822 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64822 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-402 ##label BLAT !'##cross-references GB:AE000186; GB:U00096; NID:g1787058; !1PIDN:AAC73932.1; PID:g1787068; UWGP:b0845 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily cynX protein KEYWORDS transmembrane protein FEATURE !$16-32 #domain transmembrane #status predicted #label TM1\ !$52-68 #domain transmembrane #status predicted #label TM2\ !$79-95 #domain transmembrane #status predicted #label TM3\ !$96-112 #domain transmembrane #status predicted #label TM4\ !$171-187 #domain transmembrane #status predicted #label TM5\ !$215-231 #domain transmembrane #status predicted #label TM6\ !$297-313 #domain transmembrane #status predicted #label TM7\ !$342-358 #domain transmembrane #status predicted #label TM8\ !$369-385 #domain transmembrane #status predicted #label TM9 SUMMARY #length 402 #molecular-weight 41852 #checksum 2520 SEQUENCE /// ENTRY G64939 #type complete TITLE hypothetical protein b1791 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS G64939 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64939 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-393 ##label BLAT !'##cross-references GB:AE000274; GB:U00096; NID:g1788089; !1PIDN:AAC74861.1; PID:g1788092; UWGP:b1791 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily cynX protein SUMMARY #length 393 #molecular-weight 41208 #checksum 63 SEQUENCE /// ENTRY S65973 #type complete TITLE transport protein homolog yycB - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S65973; A70089 REFERENCE S65967 !$#authors Ogasawara, N.; Nakai, S.; Yoshikawa, H. !$#journal DNA Res. (1994) 1:1-14 !$#title Systematic sequencing of the 180 kilobase region of the !1Bacillus subtilis chromosome containing the replication !1origin. !$#cross-references MUID:96051385; PMID:7584024 !$#accession S65973 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-402 ##label OGA !'##cross-references EMBL:D26185; NID:g467326; PIDN:BAA05179.1; !1PID:g467333 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1993 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A70089 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-402 ##label KUN !'##cross-references GB:Z99124; GB:AL009126; NID:g2636442; !1PIDN:CAB16085.1; PID:g2636595 !'##experimental_source strain 168 GENETICS !$#gene yycB !$#start_codon TTG CLASSIFICATION #superfamily cynX protein SUMMARY #length 402 #molecular-weight 43184 #checksum 3974 SEQUENCE /// ENTRY BVECRV #type complete TITLE ruvA protein - Escherichia coli (strain K-12) ALTERNATE_NAMES Holliday junction DNA helicase ruvA ORGANISM #formal_name Escherichia coli DATE 31-Dec-1988 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS E64948; A28533; A32358; F38113 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64948 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-203 ##label BLAT !'##cross-references GB:AE000280; GB:U00096; NID:g1788163; !1PIDN:AAC74931.1; PID:g1788168; UWGP:b1861 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A93681 !$#authors Benson, F.E.; Illing, G.T.; Sharples, G.J.; Lloyd, R.G. !$#journal Nucleic Acids Res. (1988) 16:1541-1549 !$#title Nucleotide sequencing of the ruv region of Escherichia coli !1K-12 reveals a lexA regulated operon encoding two genes. !$#cross-references MUID:88157713; PMID:3279394 !$#accession A28533 !'##molecule_type DNA !'##residues 1-165,'R',167-203 ##label BEN !'##cross-references GB:X07091; NID:g42901; PIDN:CAA30119.1; PID:g581226 REFERENCE A32358 !$#authors Shinagawa, H.; Makino, K.; Amemura, M.; Kimura, S.; Iwasaki, !1H.; Nakata, A. !$#journal J. Bacteriol. (1988) 170:4322-4329 !$#title Structure and regulation of the Escherichia coli ruv operon !1involved in DNA repair and recombination. !$#cross-references MUID:88314937; PMID:2842314 !$#accession A32358 !'##molecule_type DNA !'##residues 1-203 ##label SHI !'##cross-references EMBL:M21298; NID:g147781; PIDN:AAA24612.1; !1PID:g147782 REFERENCE A38113 !$#authors Takahagi, M.; Iwasaki, H.; Nakata, A.; Shinagawa, H. !$#journal J. Bacteriol. (1991) 173:5747-5753 !$#title Molecular analysis of the Escherichia coli ruvC gene, which !1encodes a Holliday junction-specific endonuclease. !$#cross-references MUID:91358366; PMID:1885548 !$#accession F38113 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-29 ##label TAK !'##cross-references GB:D10165; GB:D90392; NID:g216649; PIDN:BAA01034.1; !1PID:g2160258 GENETICS !$#gene ruvA !$#map_position 41 min !$#start_codon GTG COMPLEX two hexameric rings of RuvB protein and two tetramers of !1RuvA protein FUNCTION !$#description acting as specificity factor that targets RuvB; RuvA and !1RuvB form a complex that interacts with Holliday junctions !1and promotes branch migration; involved together with RuvB !1and RuvC in late stages of homologous genetic recombination !1and DNA repair !$#note SOS inducible; regulated by LexA CLASSIFICATION #superfamily holliday junction DNA helicase ruvA KEYWORDS DNA binding; DNA recombination; DNA repair; homotetramer; !1SOS response FEATURE !$106-126 #domain helix-hairpin-helix #status predicted #label !8HHH SUMMARY #length 203 #molecular-weight 22085 #checksum 1227 SEQUENCE /// ENTRY BVECQA #type complete TITLE glucose inhibited division protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1990 #sequence_revision 30-Jan-1998 #text_change 01-Mar-2002 ACCESSIONS F65177; B30389; A04441; Q90513 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65177 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-629 ##label BLAT !'##cross-references GB:AE000451; GB:U00096; NID:g2367272; !1PIDN:AAC76764.1; PID:g2367273; UWGP:b3741 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A30389 !$#authors Walker, J.E.; Gay, N.J.; Saraste, M.; Eberle, A.N. !$#journal Biochem. J. (1984) 224:799-815 !$#title DNA sequence around the Escherichia coli unc operon. !1Completion of the sequence of a 17 kilobase segment !1containing asnA, oriC, unc, glmS and phoS. !$#cross-references MUID:85121806; PMID:6395859 !$#accession B30389 !'##molecule_type DNA !'##residues 1-514,516-629 ##label WAL !'##cross-references GB:X01631; NID:g43256; PIDN:CAA25773.1; PID:g43257 REFERENCE A91504 !$#authors Buhk, H.J.; Messer, W. !$#journal Gene (1983) 24:265-279 !$#title The replication origin region of Escherichia coli: !1nucleotide sequence and functional units. !$#cross-references MUID:84059088; PMID:6357950 !$#accession A04441 !'##molecule_type DNA !'##residues 1-196 ##label BUH !'##cross-references GB:K00826; NID:g147029; PIDN:AAA24250.1; !1PID:g551821 GENETICS !$#gene gidA !$#map_position 84 min CLASSIFICATION #superfamily gidA protein SUMMARY #length 629 #molecular-weight 69521 #checksum 9778 SEQUENCE /// ENTRY BWPSAP #type complete TITLE gidA protein - Pseudomonas putida ORGANISM #formal_name Pseudomonas putida DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS JQ1223; S18095 REFERENCE JQ1213 !$#authors Ogasawara, N.; Yoshikawa, H. !$#submission submitted to JIPID, October 1991 !$#description Genes and their organization in replication origin region of !1bacterial chromosome. !$#accession JQ1223 !'##molecule_type DNA !'##residues 1-630 ##label OGA !'##cross-references EMBL:X62540; NID:g45705; PIDN:CAA44419.1; !1PID:g581463 !'##experimental_source strain TN2100 GENETICS !$#gene gidA !$#start_codon GTG CLASSIFICATION #superfamily gidA protein SUMMARY #length 630 #molecular-weight 69495 #checksum 2868 SEQUENCE /// ENTRY BWBSGA #type complete TITLE glucose-inhibited division protein gidA - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 21-Jul-2000 ACCESSIONS I40440; S66025; G69631; JQ1216; S18076 REFERENCE I40435 !$#authors Ogasawara, N.; Yoshikawa, H. !$#journal Mol. Microbiol. (1992) 6:629-634 !$#title Genes and their organization in the replication origin !1region of the bacterial chromosome. !$#cross-references MUID:92204018; PMID:1552862 !$#accession I40440 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-628 ##label RES !'##cross-references EMBL:X62539; NID:g40020; PIDN:CAA44404.1; !1PID:g40026 !'##experimental_source strain CRK2000 REFERENCE S65967 !$#authors Ogasawara, N.; Nakai, S.; Yoshikawa, H. !$#journal DNA Res. (1994) 1:1-14 !$#title Systematic sequencing of the 180 kilobase region of the !1Bacillus subtilis chromosome containing the replication !1origin. !$#cross-references MUID:96051385; PMID:7584024 !$#accession S66025 !'##status preliminary !'##molecule_type DNA !'##residues 1-628 ##label OGA !'##cross-references EMBL:D26185; NID:g467326; PIDN:BAA05231.1; !1PID:g467385 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69631 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-628 ##label KUN !'##cross-references GB:Z99124; GB:AL009126; NID:g2636442; !1PIDN:CAB16138.1; PID:g2636648 !'##experimental_source strain 168 GENETICS !$#gene gidA CLASSIFICATION #superfamily gidA protein SUMMARY #length 628 #molecular-weight 69752 #checksum 5500 SEQUENCE /// ENTRY BVECQB #type complete TITLE glucose-inhibited division protein GidB [imported] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 01-Mar-2002 ACCESSIONS C30389; I40999; E65177; Q00513 REFERENCE A30389 !$#authors Walker, J.E.; Gay, N.J.; Saraste, M.; Eberle, A.N. !$#journal Biochem. J. (1984) 224:799-815 !$#title DNA sequence around the Escherichia coli unc operon. !1Completion of the sequence of a 17 kilobase segment !1containing asnA, oriC, unc, glmS and phoS. !$#cross-references MUID:85121806; PMID:6395859 !$#accession C30389 !'##molecule_type DNA !'##residues 1-207 ##label WAL !'##cross-references GB:X01631; NID:g43256; PIDN:CAA25774.1; PID:g581247 REFERENCE I40999 !$#authors Nielsen, J.; Jorgensen, B.B.; van Meyenburg, K.V.; Hansen, !1F.G. !$#journal Mol. Gen. Genet. (1984) 193:64-71 !$#title The promoters of the atp operon of Escherichia coli K12. !$#cross-references MUID:84092835; PMID:6318052 !$#accession I40999 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 192-207 ##label RES !'##cross-references EMBL:X01383; NID:g41017; PIDN:CAA25639.1; !1PID:g41018 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65177 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-207 ##label BLAT !'##cross-references GB:AE000451; GB:U00096; NID:g2367272; !1PIDN:AAC76763.1; PID:g1790179; UWGP:b3740 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene gidB; giaB !$#map_position 84 min !$#start_codon GTG CLASSIFICATION #superfamily gidB protein SUMMARY #length 207 #molecular-weight 23431 #checksum 9904 SEQUENCE /// ENTRY BWPSBP #type complete TITLE gidB protein - Pseudomonas putida ORGANISM #formal_name Pseudomonas putida DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS JQ1224; S18096 REFERENCE JQ1213 !$#authors Ogasawara, N.; Yoshikawa, H. !$#submission submitted to JIPID, October 1991 !$#description Genes and their organization in replication origin region of !1bacterial chromosome. !$#accession JQ1224 !'##molecule_type DNA !'##residues 1-216 ##label OGA !'##cross-references EMBL:X62540; NID:g45705; PIDN:CAA44420.1; !1PID:g581464 !'##experimental_source strain TN2100 GENETICS !$#gene gidB !$#start_codon TTG CLASSIFICATION #superfamily gidB protein SUMMARY #length 216 #molecular-weight 24063 #checksum 6406 SEQUENCE /// ENTRY BWBSGB #type complete TITLE glucose-inhibited division protein gidB - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 21-Jul-2000 ACCESSIONS I40441; S66024; H69631; JQ1217; S18077 REFERENCE I40435 !$#authors Ogasawara, N.; Yoshikawa, H. !$#journal Mol. Microbiol. (1992) 6:629-634 !$#title Genes and their organization in the replication origin !1region of the bacterial chromosome. !$#cross-references MUID:92204018; PMID:1552862 !$#accession I40441 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-239 ##label RES !'##cross-references EMBL:X62539; NID:g40020; PIDN:CAA44405.1; !1PID:g40027 !'##experimental_source strain CRK200 REFERENCE S65967 !$#authors Ogasawara, N.; Nakai, S.; Yoshikawa, H. !$#journal DNA Res. (1994) 1:1-14 !$#title Systematic sequencing of the 180 kilobase region of the !1Bacillus subtilis chromosome containing the replication !1origin. !$#cross-references MUID:96051385; PMID:7584024 !$#accession S66024 !'##status preliminary !'##molecule_type DNA !'##residues 1-239 ##label OGA !'##cross-references EMBL:D26185; NID:g467326; PIDN:BAA05230.1; !1PID:g467384 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69631 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-239 ##label KUN !'##cross-references GB:Z99124; GB:AL009126; NID:g2636442; !1PIDN:CAB16137.1; PID:g2636647 !'##experimental_source strain 168 GENETICS !$#gene gidB CLASSIFICATION #superfamily gidB protein SUMMARY #length 239 #molecular-weight 26954 #checksum 9730 SEQUENCE /// ENTRY BVECGG #type complete TITLE glpG protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1989 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS C65138; A30276 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65138 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-276 ##label BLAT !'##cross-references GB:AE000418; GB:U00096; NID:g2367222; !1PIDN:AAC76449.1; PID:g2367225; UWGP:b3424 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A93685 !$#authors Choi, Y.L.; Kawase, S.; Nishida, T.; Sakai, H.; Komano, T.; !1Kawamukai, M.; Utsumi, R.; Kohara, Y.; Akiyama, K. !$#journal Nucleic Acids Res. (1988) 16:7732 !$#title Nucleotide sequence of the glpR gene encoding the repressor !1for the glycerol-3-phosphate regulon of Escherichia coli !1K12. !$#cross-references MUID:88319970; PMID:3045764 !$#accession A30276 !'##molecule_type DNA !'##residues 1-177,'RS',180-192,'T',194-276 ##label CHO !'##cross-references EMBL:X07520; NID:g41582; PIDN:CAA30398.1; !1PID:g41584 !'##experimental_source strain K12 COMMENT This protein is encoded by a gene located at the 5' end of !1the glpR gene, the repressor gene of the !1glycerol-3-phosphate regulon. GENETICS !$#gene glpG !$#map_position 75 min CLASSIFICATION #superfamily glpG protein KEYWORDS DNA binding SUMMARY #length 276 #molecular-weight 31278 #checksum 4952 SEQUENCE /// ENTRY BVECGE #type complete TITLE glpE protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1989 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS D65138; A30253 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65138 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-108 ##label BLAT !'##cross-references GB:AE000418; GB:U00096; NID:g2367222; !1PIDN:AAC76450.1; PID:g1789831; UWGP:b3425 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A93685 !$#authors Choi, Y.L.; Kawase, S.; Nishida, T.; Sakai, H.; Komano, T.; !1Kawamukai, M.; Utsumi, R.; Kohara, Y.; Akiyama, K. !$#journal Nucleic Acids Res. (1988) 16:7732 !$#title Nucleotide sequence of the glpR gene encoding the repressor !1for the glycerol-3-phosphate regulon of Escherichia coli !1K12. !$#cross-references MUID:88319970; PMID:3045764 !$#accession A30253 !'##molecule_type DNA !'##residues 1-107,'RNALYCPLLCGISDSNDVDDYLFC' ##label CHO !'##cross-references EMBL:X07520; NID:g41582; PIDN:CAA30397.1; !1PID:g41583 !'##experimental_source strain K12 GENETICS !$#gene glpE !$#map_position 75 min CLASSIFICATION #superfamily glpE protein SUMMARY #length 108 #molecular-weight 12082 #checksum 3237 SEQUENCE /// ENTRY H64085 #type complete TITLE glpE protein homolog - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS H64085 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession H64085 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-105 ##label TIGR !'##cross-references GB:U32750; GB:L42023; NID:g1573668; !1PIDN:AAC22338.1; PID:g1573679; TIGR:HI0679 CLASSIFICATION #superfamily glpE protein SUMMARY #length 105 #molecular-weight 12033 #checksum 3314 SEQUENCE /// ENTRY A64158 #type complete TITLE glpE protein homolog HI0744 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A64158 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession A64158 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-148 ##label TIGR !'##cross-references GB:U32758; GB:L42023; NID:g1573747; !1PIDN:AAC22402.1; PID:g1573751; TIGR:HI0744 !'##note best homolog was a hypothetical protein from Escherichia coli CLASSIFICATION #superfamily glpE protein SUMMARY #length 148 #molecular-weight 16537 #checksum 7373 SEQUENCE /// ENTRY C69959 #type complete TITLE glpE protein homolog yqhL - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS C69959 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69959 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-126 ##label KUN !'##cross-references GB:Z99116; GB:AL009126; NID:g2634723; !1PIDN:CAB14385.1; PID:g2634888 !'##experimental_source strain 168 GENETICS !$#gene yqhL CLASSIFICATION #superfamily glpE protein SUMMARY #length 126 #molecular-weight 14591 #checksum 7798 SEQUENCE /// ENTRY BVECAG #type complete TITLE apaG protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 01-Mar-2002 ACCESSIONS A30273; S40571; B64726 REFERENCE A26221 !$#authors Blanchin-Roland, S.; Blanquet, S.; Schmitter, J.M.; Fayat, !1G. !$#journal Mol. Gen. Genet. (1986) 205:515-522 !$#title The gene for Escherichia coli diadenosine tetraphosphatase !1is located immediately clockwise to folA and forms an operon !1with ksgA. !$#cross-references MUID:87172305; PMID:3031429 !$#accession A30273 !'##molecule_type DNA !'##residues 1-125 ##label BLA !'##cross-references GB:X04711; NID:g40916; PIDN:CAA28418.1; PID:g40918 REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40571 !'##molecule_type DNA !'##residues 1-125 ##label YUR !'##cross-references EMBL:D10483; NID:g216434; PIDN:BAA01326.1; !1PID:g216475 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64726 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-125 ##label BLAT !'##cross-references GB:AE000115; GB:U00096; NID:g1786230; !1PIDN:AAC73161.1; PID:g1786235; UWGP:b0050 !'##experimental_source strain K-12, substrain MG1655 COMMENT This protein is encoded by the apaG gene, which is located !1between ksgA (a 16S rRNA methyltransferase gene) and apaH !1(diadenosine tetraphosphatase gene). GENETICS !$#gene apaG !$#map_position 1 min CLASSIFICATION #superfamily apaG protein SUMMARY #length 125 #molecular-weight 13867 #checksum 73 SEQUENCE /// ENTRY BVECBH #type complete TITLE biotin biosynthesis protein bioH - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 01-Mar-2002 ACCESSIONS JQ0081; G65136; S06071 REFERENCE JQ0081 !$#authors O'Regan, M.; Gloeckler, R.; Bernard, S.; Ledoux, C.; Ohsawa, !1I.; Lemoine, Y. !$#journal Nucleic Acids Res. (1989) 17:8004 !$#title Nucleotide sequence of the bioH gene of Escherichia coli. !$#cross-references MUID:90016899; PMID:2678009 !$#accession JQ0081 !'##molecule_type DNA !'##residues 1-256 ##label ORE !'##cross-references GB:X15587; NID:g41067; PIDN:CAA33612.1; PID:g41068 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65136 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-256 ##label BLAT !'##cross-references GB:AE000417; GB:U00096; NID:g2367220; !1PIDN:AAC76437.1; PID:g1789817; UWGP:b3412 !'##experimental_source strain K-12, substrain MG1655 COMMENT This protein is involved in an early unknown step of the !1biotin biosynthesis pathway. GENETICS !$#gene bioH !$#map_position 75 min CLASSIFICATION #superfamily bioH protein KEYWORDS biotin biosynthesis SUMMARY #length 256 #molecular-weight 28505 #checksum 7892 SEQUENCE /// ENTRY BVECBC #type complete TITLE biotin biosynthesis protein bioC - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS A64814; E32025 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64814 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-251 ##label BLAT !'##cross-references GB:AE000180; GB:U00096; NID:g1786988; !1PIDN:AAC73864.1; PID:g1786994; UWGP:b0777 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A32025 !$#authors Otsuka, A.J.; Buoncristiani, M.R.; Howard, P.K.; Flamm, J.; !1Johnson, C.; Yamamoto, R.; Uchida, K.; Cook, C.; Ruppert, !1J.; Matsuzaki, J. !$#journal J. Biol. Chem. (1988) 263:19577-19585 !$#title The Escherichia coli biotin biosynthetic enzyme sequences !1predicted from the nucleotide sequence of the bio operon. !$#cross-references MUID:89066784; PMID:3058702 !$#accession E32025 !'##molecule_type DNA !'##residues 1-148,'R',150-251 ##label OTS !'##cross-references GB:J04423; NID:g145422; PIDN:AAA23517.1; !1PID:g145427 GENETICS !$#gene bioC !$#map_position 17 min FUNCTION !$#description involved in the synthesis of pimelic acid !$#pathway biotin biosynthesis CLASSIFICATION #superfamily bioC protein; bioC homology KEYWORDS biotin biosynthesis FEATURE !$43-140 #domain bioC homology #label BIOC SUMMARY #length 251 #molecular-weight 28276 #checksum 2519 SEQUENCE /// ENTRY S42003 #type complete TITLE sterol 24-C-methyltransferase (EC 2.1.1.41) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES PDR4-region bioC homolog; protein YM9571.10c; protein YML008c ORGANISM #formal_name Saccharomyces cerevisiae DATE 03-Feb-1994 #sequence_revision 27-Jan-1995 #text_change 03-Jun-2002 ACCESSIONS S42003; PE0402; S55111; S17001; S35982 REFERENCE S42003 !$#authors Hardwick, K.G.; Pelham, H.R.B. !$#journal Yeast (1994) 10:265-269 !$#title SED6 is identical to ERG6, and encodes a putative !1methyltransferase required for ergosterol synthesis. !$#cross-references MUID:94262330; PMID:8203167 !$#accession S42003 !'##molecule_type DNA !'##residues 1-383 ##label HAR !'##cross-references EMBL:X74249; NID:g396514; PIDN:CAA52308.1; !1PID:g396515 !'##note the authors translated the codon ACT for residue 322 as Ala REFERENCE JE0416 !$#authors Hussain, M.; Lenard, J. !$#journal Gene (1991) 101:149-152 !$#title Characterization of PDR4, a Saccharomyces cerevisiae gene !1that confers pleiotropic drug resistance in high-copy !1number. !$#cross-references MUID:91285426; PMID:2060792 !$#accession PE0402 !'##molecule_type DNA !'##residues 1-258 ##label HUS !'##cross-references GB:X53830; NID:g4121; PIDN:CAA37826.1; PID:g4122 !'##note the authors suggested that this protein is unrelated to the !1pleiotropic drug resistance (pdr) phenotype; a larger ORF in !1transcribed in the opposite direction was designated PDR4 !1and is now known to be a transcriptional activator (see !1PIR:S16706) REFERENCE S55102 !$#authors Gentles, S.; Bowman, S. !$#submission submitted to the EMBL Data Library, June 1995 !$#accession S55111 !'##molecule_type DNA !'##residues 1-383 ##label GEN !'##cross-references EMBL:Z49810; NID:g854472; PIDN:CAA89944.1; !1PID:g854482; GSPDB:GN00013; MIPS:YML008c !'##experimental_source strain AB972 GENETICS !$#gene SGD:ERG6; SED6; MIPS:YML008c !'##cross-references SGD:S0004467; MIPS:YML008c !$#map_position 13L CLASSIFICATION #superfamily 24-sterol C-methyltransferase; bioC homology KEYWORDS methyltransferase; S-adenosylmethionine FEATURE !$120-224 #domain bioC homology #label BIOC SUMMARY #length 383 #molecular-weight 43431 #checksum 8649 SEQUENCE /// ENTRY S36653 #type complete TITLE kpsD protein - Escherichia coli ORGANISM #formal_name Escherichia coli DATE 06-Jan-1995 #sequence_revision 06-Jan-1995 #text_change 16-Jul-1999 ACCESSIONS S36653; E48492; C42644 REFERENCE S36649 !$#authors Roberts, I.S. !$#submission submitted to the EMBL Data Library, August 1993 !$#accession S36653 !'##status preliminary !'##molecule_type DNA !'##residues 1-389 ##label ROB !'##cross-references EMBL:X74567; NID:g397404; PIDN:CAA52659.1; !1PID:g397409 REFERENCE A48492 !$#authors Pazzani, C.; Rosenow, C.; Boulnois, G.J.; Bronner, D.; Jann, !1K.; Roberts, I.S. !$#journal J. Bacteriol. (1993) 175:5978-5983 !$#title Molecular analysis of region 1 of the Escherichia coli K5 !1antigen gene cluster: a region encoding proteins involved in !1cell surface expression of capsular polysaccharide. !$#cross-references MUID:93388530; PMID:8397187 !$#accession E48492 !'##status preliminary !'##molecule_type DNA !'##residues 22-389 ##label PAZ !'##cross-references GB:X74567 REFERENCE A42644 !$#authors Steenbergen, S.M.; Wrona, T.J.; Vimr, E.R. !$#journal J. Bacteriol. (1992) 174:1099-1108 !$#title Functional analysis of the sialyltransferase complexes in !1Escherichia coli K1 and K92. !$#cross-references MUID:92138601; PMID:1735705 !$#accession C42644 !'##status preliminary !'##molecule_type DNA !'##residues 106-125,'D',127-244,'N',246-297,'S',299-300,'VI',303-379, !1'M',381-385,'W',387-389,'GGNTTNCQHNIY' ##label STE !'##cross-references GB:M76370; NID:g146947; PIDN:AAA24214.1; !1PID:g146950 !'##experimental_source K1, strain EV1 !'##note sequence extracted from NCBI backbone (NCBIN:79370, !1NCBIP:79381) GENETICS !$#gene kpsD CLASSIFICATION #superfamily kpsD protein SUMMARY #length 389 #molecular-weight 46381 #checksum 1013 SEQUENCE /// ENTRY S32880 #type complete TITLE lipB protein - Neisseria meningitidis ORGANISM #formal_name Neisseria meningitidis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S32880; S28078 REFERENCE S32879 !$#authors Frosch, M.; Mueller, A. !$#journal Mol. Microbiol. (1993) 8:483-493 !$#title Phospholipid substitution of capsular polysaccharides and !1mechanisms of capsule formation in Neisseria meningitidis. !$#cross-references MUID:93316845; PMID:8326861 !$#accession S32880 !'##status preliminary !'##molecule_type DNA !'##residues 1-419 ##label FRO !'##cross-references EMBL:Z13995 GENETICS !$#gene lipB CLASSIFICATION #superfamily kpsD protein SUMMARY #length 419 #molecular-weight 48678 #checksum 7803 SEQUENCE /// ENTRY BVECXA #type complete TITLE pyridoxal phosphate biosynthetic protein pdxA - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 01-Mar-2002 ACCESSIONS JV0026; S40573; D64726 REFERENCE JV0026 !$#authors Roa, B.B.; Connolly, D.M.; Winkler, M.E. !$#journal J. Bacteriol. (1989) 171:4767-4777 !$#title Overlap between pdxA and ksgA in the complex !1pdxA-ksgA-apaG-apaH operon of Escherichia coli K-12. !$#cross-references MUID:89359108; PMID:2670894 !$#accession JV0026 !'##molecule_type DNA !'##residues 1-329 ##label ROA !'##cross-references GB:M68521; GB:M28485; NID:g147118; PIDN:AAA24305.1; !1PID:g147120 !'##note the translational start codon was tentatively assigned based on !1polypeptide size and homology with the translational start !1site of pdxB REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40573 !'##molecule_type DNA !'##residues 1-20,'S',22-56,'C',58-101,'T',103-329 ##label YUR !'##cross-references EMBL:D10483; NID:g216434; PIDN:BAA01328.1; !1PID:g216477 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64726 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-329 ##label BLAT !'##cross-references GB:AE000115; GB:U00096; NID:g1786230; !1PIDN:AAC73163.1; PID:g1786237; UWGP:b0052 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene pdxA !$#map_position 1 min FUNCTION !$#description required for de novo biosynthesis of pyridoxine (vitamin B6) !1and pyridoxal phosphate !$#pathway pyridoxine biosynthesis CLASSIFICATION #superfamily pdxA protein KEYWORDS pyridoxine biosynthesis SUMMARY #length 329 #molecular-weight 35113 #checksum 7955 SEQUENCE /// ENTRY G64717 #type complete TITLE pyridoxal phosphate biosynthetic protein A - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS G64717 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession G64717 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-307 ##label TOM !'##cross-references GB:AE000655; GB:AE000511; NID:g2314757; !1PIDN:AAD08621.1; PID:g2314766; TIGR:HP1583 CLASSIFICATION #superfamily pdxA protein SUMMARY #length 307 #molecular-weight 33578 #checksum 1531 SEQUENCE /// ENTRY S77070 #type complete TITLE pyridoxal phosphate biosynthetic protein pdxA - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein sll0660 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S77070 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S77070 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-349 ##label KAN !'##cross-references EMBL:D64005; GB:AB001339; NID:g1001779; !1PIDN:BAA10762.1; PID:g1006608 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene pdxA CLASSIFICATION #superfamily pdxA protein KEYWORDS pyridoxine biosynthesis SUMMARY #length 349 #molecular-weight 37224 #checksum 9456 SEQUENCE /// ENTRY BVECYC #type complete TITLE hydrogenase (EC 1.18.99.1) (NiFe) b-type cytochrome chain - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 01-Mar-2002 ACCESSIONS JV0074; D64838 REFERENCE JV0072 !$#authors Menon, N.K.; Robbins, J.; Peck Jr., H.D.; Chatelus, C.Y.; !1Choi, E.S.; Przybyla, A.E. !$#journal J. Bacteriol. (1990) 172:1969-1977 !$#title Cloning and sequencing of a putative Escherichia coli [NiFe] !1hydrogenase-1 operon containing six open reading frames. !$#cross-references MUID:90202716; PMID:2180913 !$#accession JV0074 !'##molecule_type DNA !'##residues 1-235 ##label MEN !'##cross-references GB:M34825; NID:g146419; PIDN:AAA23999.1; !1PID:g146422 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64838 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-235 ##label BLAT !'##cross-references GB:AE000199; GB:U00096; NID:g1787202; !1PIDN:AAC74059.1; PID:g1787208; UWGP:b0974 !'##experimental_source strain K-12, substrain MG1655 COMMENT This protein may be involved in uptake and/or processing of !1nickel. GENETICS !$#gene hyaC !$#map_position 21 min CLASSIFICATION #superfamily hyaC protein KEYWORDS hydrolase; metalloprotein; nickel; oxidoreductase; !1transmembrane protein FEATURE !$24-40 #domain transmembrane #status predicted #label TM1\ !$59-75 #domain transmembrane #status predicted #label TM2\ !$134-150 #domain transmembrane #status predicted #label TM3\ !$186-202 #domain transmembrane #status predicted #label TM4 SUMMARY #length 235 #molecular-weight 27597 #checksum 5927 SEQUENCE /// ENTRY JQ0807 #type complete TITLE hydrogenase (EC 1.18.99.1) (NiFe) b-type cytochrome chain - Azotobacter vinelandii ORGANISM #formal_name Azotobacter vinelandii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JQ0807 REFERENCE JQ0805 !$#authors Menon, A.L.; Stults, L.W.; Robson, R.L.; Mortenson, L.E. !$#journal Gene (1990) 96:67-74 !$#title Cloning, sequencing and characterization of the [NiFe] !1hydrogenase-encoding structural genes (hoxK and hoxG) from !1Azotobacter vinelandii. !$#cross-references MUID:91092503; PMID:2265761 !$#accession JQ0807 !'##molecule_type DNA !'##residues 1-240 ##label MEN !'##cross-references GB:M33152; NID:g142310; PIDN:AAA82507.1; !1PID:g1088265 !'##experimental_source strain OP CLASSIFICATION #superfamily hyaC protein KEYWORDS hydrolase; metalloprotein; nickel; oxidoreductase; !1transmembrane protein FEATURE !$35-51 #domain transmembrane #status predicted #label TM1\ !$142-158 #domain transmembrane #status predicted #label TM2\ !$197-213 #domain transmembrane #status predicted #label TM3 SUMMARY #length 240 #molecular-weight 27737 #checksum 6645 SEQUENCE /// ENTRY S53656 #type complete TITLE hydrogenase (EC 1.18.99.1) (NiFe) b-type cytochrome chain - Azotobacter chroococcum ORGANISM #formal_name Azotobacter chroococcum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S53656 REFERENCE S53655 !$#authors Du, L.; Tibelius, K.H.; Souza, E.M.; Garg, R.P.; Yates, M.G. !$#journal J. Mol. Biol. (1994) 243:549-557 !$#title Sequences, organization and analysis of the hupZMNOQRTV !1genes from the Azotobacter chroococcum hydrogenase gene !1cluster. !$#cross-references MUID:95055698; PMID:7966281 !$#accession S53656 !'##molecule_type DNA !'##residues 1-240 ##label DUL !'##cross-references EMBL:L25315; NID:g408900; PIDN:AAA64447.1; !1PID:g408902 !'##experimental_source strain MCD1 GENETICS !$#gene hupZ CLASSIFICATION #superfamily hyaC protein KEYWORDS hydrolase; metalloprotein; nickel; oxidoreductase; !1transmembrane protein FEATURE !$35-51 #domain transmembrane #status predicted #label TM1\ !$142-158 #domain transmembrane #status predicted #label TM2\ !$196-212 #domain transmembrane #status predicted #label TM3 SUMMARY #length 240 #molecular-weight 27649 #checksum 4970 SEQUENCE /// ENTRY C43255 #type complete TITLE hydrogenase (EC 1.18.99.1) (NiFe) b-type cytochrome chain - Alcaligenes eutrophus ALTERNATE_NAMES hoxZ protein ORGANISM #formal_name Alcaligenes eutrophus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C43255 REFERENCE A43255 !$#authors Kortluke, C.; Horstmann, K.; Schwartz, E.; Rohde, M.; !1Binsack, R.; Friedrich, B. !$#journal J. Bacteriol. (1992) 174:6277-6289 !$#title A gene complex coding for the membrane-bound hydrogenase of !1Alcaligenes eutrophus H16. !$#cross-references MUID:93015670; PMID:1383192 !$#accession C43255 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-244 ##label KOR !'##cross-references GB:M96433; NID:g141932; PIDN:AAA16463.1; !1PID:g141935 !'##experimental_source strain H16, megaplasmid pHG1 !'##note sequence extracted from NCBI backbone (NCBIP:115452) GENETICS !$#gene hoxZ CLASSIFICATION #superfamily hyaC protein KEYWORDS hydrolase; metalloprotein; nickel; oxidoreductase; !1transmembrane protein FEATURE !$43-59 #domain transmembrane #status predicted #label TM1\ !$78-94 #domain transmembrane #status predicted #label TM2\ !$150-166 #domain transmembrane #status predicted #label TM3\ !$205-221 #domain transmembrane #status predicted #label TM4 SUMMARY #length 244 #molecular-weight 27581 #checksum 5171 SEQUENCE /// ENTRY A41892 #type complete TITLE hydrogenase (EC 1.18.99.1) (NiFe) b-type cytochrome chain - Rhizobium leguminosarum ORGANISM #formal_name Rhizobium leguminosarum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A41892 REFERENCE A41892 !$#authors Hidalgo, E.; Palacios, J.M.; Murillo, J.; Ruiz-Argueso, T. !$#journal J. Bacteriol. (1992) 174:4130-4139 !$#title Nucleotide sequence and characterization of four additional !1genes of the hydrogenase structural operon from Rhizobium !1leguminosarum bv. viciae. !$#cross-references MUID:92283771; PMID:1597428 !$#accession A41892 !'##status preliminary !'##molecule_type DNA !'##residues 1-239 ##label HID !'##cross-references GB:X52974; NID:g1167855; PIDN:CAA37150.1; !1PID:g48723 !'##experimental_source bv. viciae, UPM791 !'##note sequence extracted from NCBI backbone (NCBIN:106282, !1NCBIP:106285) GENETICS !$#gene hupC CLASSIFICATION #superfamily hyaC protein KEYWORDS hydrolase; metalloprotein; nickel; oxidoreductase; !1transmembrane protein FEATURE !$73-89 #domain transmembrane #status predicted #label TM1\ !$146-162 #domain transmembrane #status predicted #label TM2\ !$197-213 #domain transmembrane #status predicted #label TM3 SUMMARY #length 239 #molecular-weight 27869 #checksum 4758 SEQUENCE /// ENTRY S39400 #type complete TITLE hydrogenase (EC 1.18.99.1) (NiFe) b-type cytochrome chain - Bradyrhizobium japonicum ALTERNATE_NAMES hupC protein ORGANISM #formal_name Bradyrhizobium japonicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S39400 REFERENCE S39400 !$#authors van Soom, C.; Browaeys, J.; Verreth, C.; Vanderleyden, J. !$#journal J. Mol. Biol. (1993) 234:508-512 !$#title Nucleotide sequence analysis of four genes, hupC, hupD, hupF !1and hupG, downstream of the hydrogenase structural genes in !1Bradyrhizobium japonicum. !$#cross-references MUID:94047099; PMID:8230232 !$#accession S39400 !'##molecule_type DNA !'##residues 1-244 ##label VAN !'##cross-references EMBL:Z21948; NID:g311536; PIDN:CAA79943.1; !1PID:g311537 GENETICS !$#gene hupC CLASSIFICATION #superfamily hyaC protein KEYWORDS hydrolase; metalloprotein; nickel; oxidoreductase; !1transmembrane protein FEATURE !$44-60 #domain transmembrane #status predicted #label TM1\ !$87-103 #domain transmembrane #status predicted #label TM2\ !$155-171 #domain transmembrane #status predicted #label TM3\ !$205-221 #domain transmembrane #status predicted #label TM4 SUMMARY #length 244 #molecular-weight 27846 #checksum 6707 SEQUENCE /// ENTRY A64599 #type complete TITLE hydrogenase (EC 1.18.99.1) (NiFe) b-type cytochrome chain, quinone-reactive - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A64599 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession A64599 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-224 ##label TOM !'##cross-references GB:AE000577; GB:AE000511; NID:g2313747; !1PIDN:AAD07693.1; PID:g2313751; TIGR:HP0633 CLASSIFICATION #superfamily hyaC protein KEYWORDS hydrolase; metalloprotein; nickel; oxidoreductase; !1transmembrane protein SUMMARY #length 224 #molecular-weight 25824 #checksum 1772 SEQUENCE /// ENTRY S22406 #type complete TITLE hydrogenase (EC 1.18.99.1) (NiFe) b-type cytochrome chain, quinone-reactive - Wolinella succinogenes ALTERNATE_NAMES hydC protein ORGANISM #formal_name Wolinella succinogenes DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S22406 REFERENCE S22404 !$#authors Dross, F.; Geisler, V.; Lenger, R.; Theis, F.; Krafft, T.; !1Fahrenholz, F.; Kojro, E.; Duchene, A.; Tripier, D.; !1Juvenal, K.; Kroeger, A. !$#journal Eur. J. Biochem. (1992) 206:93-102 !$#title The quinone-reactive Ni/Fe-hydrogenase of Wolinella !1succinogenes. !$#cross-references MUID:92267032; PMID:1587288 !$#accession S22406 !'##status preliminary !'##molecule_type DNA !'##residues 1-230 ##label DRO !'##cross-references EMBL:X65189; NID:g296081; PIDN:CAA46304.1; !1PID:g48518 CLASSIFICATION #superfamily hyaC protein KEYWORDS hydrolase; metalloprotein; nickel; oxidoreductase; !1transmembrane protein SUMMARY #length 230 #molecular-weight 26829 #checksum 7035 SEQUENCE /// ENTRY CEECDC #type complete TITLE cell division control protein dicC, phage protein-related - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 01-Mar-2002 ACCESSIONS A24328; S02245; D64912 REFERENCE A93636 !$#authors Bejar, S.; Cam, K.; Bouche, J.P. !$#journal Nucleic Acids Res. (1986) 14:6821-6833 !$#title Control of cell division in Escherichia coli. DNA sequence !1of dicA and of a second gene complementing mutation dicA1, !1dicC. !$#cross-references MUID:87016327; PMID:3532030 !$#accession A24328 !'##molecule_type DNA !'##residues 1-76 ##label BEJ1 !'##cross-references GB:X07465; GB:X04395; NID:g312764; PIDN:CAA30348.1; !1PID:g41277 REFERENCE S02245 !$#authors Bejar, S.; Bouche, F.; Bouche, J.P. !$#journal Mol. Gen. Genet. (1988) 212:11-19 !$#title Cell division inhibition gene dicB is regulated by a locus !1similar to lambdoid bacteriophage immunity loci. !$#cross-references MUID:88232418; PMID:2836697 !$#accession S02245 !'##molecule_type DNA !'##residues 1-76 ##label BEJ2 !'##cross-references EMBL:X07465; NID:g312764; PIDN:CAA30348.1; !1PID:g41277 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64912 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-76 ##label BLAT !'##cross-references GB:AE000253; GB:U00096; NID:g1787841; !1PIDN:AAC74642.1; PID:g1787852; UWGP:b1569 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene dicC !$#map_position 35 min FUNCTION !$#description repressor of cell division inhibition gene dicB !$#note transcribed divergently from dicA; it can also complement !1mutation of the dicA gene, which leads to !1temperature-sensitive cell division CLASSIFICATION #superfamily cell division control protein dicC KEYWORDS cell division; DNA binding; repressor; transcription !1regulation SUMMARY #length 76 #molecular-weight 8578 #checksum 330 SEQUENCE /// ENTRY CEECDB #type complete TITLE cell division inhibitor dicB, phage protein-related - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1990 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS A64913; A32652; A30383; Q00232 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64913 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-62 ##label BLAT !'##cross-references GB:AE000253; GB:U00096; NID:g1787841; !1PIDN:AAC74647.1; PID:g1787857; UWGP:b1575 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A32652 !$#authors Bouche, J.P. !$#submission submitted to the EMBL Data Library, April 1988 !$#accession A32652 !'##molecule_type DNA !'##residues 'MRLSAREQLKPKTVLWVDSLYPALIVNWLTSPGGTRHCITKFIVEDAI',1-38, !1'Q',40-62 ##label BOU REFERENCE A30383 !$#authors Cam, K.; Bejar, S.; Gil, D.; Bouche, J.P. !$#journal Nucleic Acids Res. (1988) 16:6327-6338 !$#title Identification and sequence of gene dicB: translation of the !1division inhibitor from an in-phase internal start. !$#cross-references MUID:88289404; PMID:3041373 !$#accession A30383 !'##molecule_type DNA !'##residues 'MRLSAREQLKPKTVLWVDSLYPALIVNWLTSPGGTRHCITKFIVEDAI',1-38, !1'Q',40-62 ##label CAM GENETICS !$#gene dicB !$#map_position 35 min FUNCTION !$#description involved in cell division inhibition !$#note can be repressed by dicA and dicC proteins CLASSIFICATION #superfamily cell division inhibitor dicB KEYWORDS cell division; cell division control SUMMARY #length 62 #molecular-weight 6964 #checksum 7107 SEQUENCE /// ENTRY CEECIC #type complete TITLE cell division inhibitor minC - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 01-Mar-2002 ACCESSIONS A31877; E64863 REFERENCE A31877 !$#authors de Boer, P.A.J.; Crossley, R.E.; Rothfield, L.I. !$#journal Cell (1989) 56:641-649 !$#title A division inhibitor and a topological specificity factor !1coded for by the minicell locus determine proper placement !1of the division septum in Escherichia coli. !$#cross-references MUID:89136010; PMID:2645057 !$#accession A31877 !'##molecule_type DNA !'##residues 1-231 ##label DEB !'##cross-references GB:J03153; NID:g146865; PIDN:AAB59061.1; !1PID:g146866 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64863 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-231 ##label BLAT !'##cross-references GB:AE000216; GB:U00096; NID:g1787417; !1PIDN:AAC74260.1; PID:g1787424; UWGP:b1176 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene minC !$#map_position 26 min FUNCTION !$#description minC and minD act in concert to form an inhibitor capable of !1blocking formation of the cell division septum at all !1potential sites !$#note dicB cooperates with minC to promote division inhibition; !1minE reduces interaction between minC and minD; no !1interactin found between ftsZ and minCD; overproduction of !1minC alone leads to division inhibition CLASSIFICATION #superfamily cell division inhibitor minC KEYWORDS cell division; cell division control SUMMARY #length 231 #molecular-weight 24775 #checksum 9252 SEQUENCE /// ENTRY CCECID #type complete TITLE cell division inhibitor minD - Escherichia coli (strain K-12) ALTERNATE_NAMES septum site-determining protein minD ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 01-Mar-2002 ACCESSIONS B31877; D64863 REFERENCE A31877 !$#authors de Boer, P.A.J.; Crossley, R.E.; Rothfield, L.I. !$#journal Cell (1989) 56:641-649 !$#title A division inhibitor and a topological specificity factor !1coded for by the minicell locus determine proper placement !1of the division septum in Escherichia coli. !$#cross-references MUID:89136010; PMID:2645057 !$#accession B31877 !'##molecule_type DNA !'##residues 1-270 ##label DEB !'##cross-references GB:J03153; NID:g146865; PIDN:AAB59062.1; !1PID:g146867 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64863 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-270 ##label BLAT !'##cross-references GB:AE000216; GB:U00096; NID:g1787417; !1PIDN:AAC74259.1; PID:g1787423; UWGP:b1175 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene minD !$#map_position 26 min FUNCTION !$#description a membrane ATPase required for correct placement of cell !1division site !$#note minC and minD act in concert to form an inhibitor capable of !1blocking formation of the cell division septum at all !1potential sites; minE reduces interaction between minC and !1minD; no interaction found between ftsZ and minCD CLASSIFICATION #superfamily cell division inhibitor minD KEYWORDS ATP; cell division control; nucleotide binding; P-loop FEATURE !$10-17 #region nucleotide-binding motif A (P-loop)\ !$16 #binding_site ATP (Lys) #status predicted SUMMARY #length 270 #molecular-weight 29614 #checksum 7366 SEQUENCE /// ENTRY G45239 #type complete TITLE cell division inhibitor minD [validated] - Bacillus subtilis ALTERNATE_NAMES septum placement determinant minD ORGANISM #formal_name Bacillus subtilis DATE 10-Jun-1993 #sequence_revision 04-Oct-1996 #text_change 19-Jan-2001 ACCESSIONS S31205; G45239; F45240; A69658; S27521; S29866 REFERENCE S31204 !$#authors Lee, S.; Price, C.W. !$#journal Mol. Microbiol. (1993) 7:601-610 !$#title The minCD locus of Bacillus subtilis lacks the minE !1determinant that provides topological specificity to cell !1division. !$#cross-references MUID:93211302; PMID:8459776 !$#accession S31205 !'##molecule_type DNA !'##residues 1-268 ##label LEE !'##cross-references EMBL:Z15113; NID:g49307; PIDN:CAA78818.1; !1PID:g580893 REFERENCE A45239 !$#authors Levin, P.A.; Margolis, P.S.; Setlow, P.; Losick, R.; Sun, D. !$#journal J. Bacteriol. (1992) 174:6717-6728 !$#title Identification of Bacillus subtilis genes for septum !1placement and shape determination. !$#cross-references MUID:93015731; PMID:1400224 !$#accession G45239 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-268 ##label LEV !'##cross-references GB:M96343; NID:g142852; PIDN:AAA22401.1; !1PID:g142859 !'##note sequence extracted from NCBI backbone (NCBIP:116563) REFERENCE A45240 !$#authors Varley, A.W.; Stewart, G.C. !$#journal J. Bacteriol. (1992) 174:6729-6742 !$#title The divIVB region of the Bacillus subtilis chromosome !1encodes homologs of Escherichia coli septum placement !1(minCD) and cell shape (mreBCD) determinants. !$#cross-references MUID:93015732; PMID:1400225 !$#accession F45240 !'##molecule_type DNA !'##residues 1-268 ##label VA2 !'##cross-references EMBL:M95582; NID:g143211; PIDN:AAA22609.1; !1PID:g143216 !'##note sequence extracted from NCBI backbone (NCBIP:116574) REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69658 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-268 ##label KUN !'##cross-references GB:Z99118; GB:AL009126; NID:g2635200; !1PIDN:CAB14759.1; PID:g2635264 !'##experimental_source strain 168 GENETICS !$#gene minD !$#start_codon TTG FUNCTION !$#description mediates, together with minC, cell division site selection !1by specifically inhibiting division close to the cell poles !1[validated, MUID:99026115] CLASSIFICATION #superfamily cell division inhibitor minD KEYWORDS cell division control; nucleotide binding; P-loop FEATURE !$10-17 #region nucleotide-binding motif A (P-loop)\ !$16 #binding_site ATP (Lys) #status predicted SUMMARY #length 268 #molecular-weight 29407 #checksum 9764 SEQUENCE /// ENTRY B64321 #type complete TITLE cell division inhibitor MinD homolog MJ0169 - Methanococcus jannaschii ALTERNATE_NAMES septum placement determinant minD homolog MJ0169 ORGANISM #formal_name Methanococcus jannaschii DATE 13-Sep-1996 #sequence_revision 04-Oct-1996 #text_change 19-Jan-2001 ACCESSIONS B64321 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession B64321 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-263 ##label BUL !'##cross-references GB:U67474; GB:L77117; NID:g1590921; !1PIDN:AAB98154.1; PID:g1590922; TIGR:MJ0169 COMMENT Cell division inhibitors minC and minD act in concert to !1form an inhibitor capable of blocking formation of the cell !1division septum at all potential sites. GENETICS !$#map_position FOR171244-172035 !$#start_codon GTG CLASSIFICATION #superfamily cell division inhibitor minD KEYWORDS cell division control; nucleotide binding; P-loop FEATURE !$11-18 #region nucleotide-binding motif A (P-loop)\ !$17 #binding_site ATP (Lys) #status predicted SUMMARY #length 263 #molecular-weight 28950 #checksum 8607 SEQUENCE /// ENTRY C64368 #type complete TITLE cell division inhibitor MinD homolog MJ0547 - Methanococcus jannaschii ALTERNATE_NAMES septum placement determinant minD homolog MJ0547 ORGANISM #formal_name Methanococcus jannaschii DATE 13-Sep-1996 #sequence_revision 04-Oct-1996 #text_change 19-Jan-2001 ACCESSIONS C64368 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession C64368 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-264 ##label BUL !'##cross-references GB:U67504; GB:L77117; NID:g1591248; !1PIDN:AAB98539.1; PID:g1591252; TIGR:MJ0547 GENETICS !$#map_position REV484422-483628 CLASSIFICATION #superfamily cell division inhibitor minD KEYWORDS cell division control; nucleotide binding; P-loop FEATURE !$14-21 #region nucleotide-binding motif A (P-loop)\ !$20 #binding_site ATP (Lys) #status predicted SUMMARY #length 264 #molecular-weight 27737 #checksum 2254 SEQUENCE /// ENTRY QQECA1 #type complete TITLE cell division inhibitor sulA - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 24-Sep-1981 #sequence_revision 15-Oct-1996 #text_change 01-Mar-2002 ACCESSIONS A29016; A04468; I57720; E64836 REFERENCE A29016 !$#authors Freudl, R.; Braun, G.; Honore, N.; Cole, S.T. !$#journal Gene (1987) 52:31-40 !$#title Evolution of the enterobacterial sulA gene: a component of !1the SOS system encoding an inhibitor of cell division. !$#cross-references MUID:87248093; PMID:3297925 !$#accession A29016 !'##molecule_type DNA !'##residues 1-169 ##label FRE REFERENCE A93707 !$#authors Beck, E.; Bremer, E. !$#journal Nucleic Acids Res. (1980) 8:3011-3024 !$#title Nucleotide sequence of the gene ompA coding the outer !1membrane protein II of Escherichia coli K-12. !$#cross-references MUID:81053729; PMID:6253901 !$#accession A04468 !'##molecule_type DNA !'##residues 1-144,'IHSGKRILSRHETTFRAKNSL' ##label BEC !'##experimental_source strain K-12 !'##note this sequence has been revised by personal communication to the !1authors of reference A29016 REFERENCE I57720 !$#authors Cole, S.T. !$#journal Mol. Gen. Genet. (1983) 189:400-404 !$#title Characterisation of the promoter for the LexA regulated sulA !1gene of Escherichia coli. !$#cross-references MUID:83244178; PMID:6306396 !$#accession I57720 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-10 ##label RES !'##cross-references EMBL:V00358; NID:g43023; PIDN:CAA23654.1; !1PID:g43024 !'##note the sequence represented here from this article is quoted from !1references A29016 and A93707 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64836 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-169 ##label BLAT !'##cross-references GB:AE000198; GB:U00096; NID:g1787189; !1PIDN:AAC74044.1; PID:g1787192; UWGP:b0958 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene sulA; sfiA !$#map_position 22 min FUNCTION !$#description inducible cell division inhibitor; component of the SOS !1response; blocks formation of the ftsZ ring and leads to !1filamentation; sulA interacts with ftsZ protein to form a !1stable complex which may be the mechanism by which sulA !1inhibits cell division !$#note expression of sulA is repressed by lexA protein CLASSIFICATION #superfamily cell division inhibitor sulA KEYWORDS cell division control; SOS response SUMMARY #length 169 #molecular-weight 18801 #checksum 6582 SEQUENCE /// ENTRY CEECTF #type complete TITLE cell division topological specificity factor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 01-Mar-2002 ACCESSIONS C31877; C64863 REFERENCE A31877 !$#authors de Boer, P.A.J.; Crossley, R.E.; Rothfield, L.I. !$#journal Cell (1989) 56:641-649 !$#title A division inhibitor and a topological specificity factor !1coded for by the minicell locus determine proper placement !1of the division septum in Escherichia coli. !$#cross-references MUID:89136010; PMID:2645057 !$#accession C31877 !'##molecule_type DNA !'##residues 1-88 ##label DEB !'##cross-references GB:J03153; NID:g146865; PIDN:AAB59063.1; !1PID:g146868 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64863 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-88 ##label BLAT !'##cross-references GB:AE000216; GB:U00096; NID:g1787417; !1PIDN:AAC74258.1; PID:g1787422; UWGP:b1174 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene minE !$#map_position 26 min FUNCTION !$#description prevents cell division inhibition by proteins minC and minD !1at internal division sites while permitting inhibition at !1polar sites; this ensures cell division at the proper site !1by restricting the formation of a division septum at the !1midpoint of the long axis of the cell !$#note formation of the minE ring requires minD but is independent !1of minC and continues in nondividing cells in which ftsZ !1function is inhibited; minE ring represents a novel cell !1structure, which allows ftsZ ring formation at midcell by !1suppressing minCD activity at this site CLASSIFICATION #superfamily cell division topological specificity factor KEYWORDS cell division SUMMARY #length 88 #molecular-weight 10235 #checksum 2959 SEQUENCE /// ENTRY D64773 #type complete TITLE trigger factor [validated] - Escherichia coli (strain K-12) CONTAINS peptidylprolyl isomerase (EC 5.2.1.8), ribosome-bound ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS D64773; JS0357; A36129; A36575; S68370; S65516; S68845 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64773 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-432 ##label BLAT !'##cross-references GB:AE000150; GB:U00096; NID:g1786639; !1PIDN:AAC73539.1; PID:g1786640; UWGP:b0436 !'##experimental_source strain K-12, substrain MG1655 REFERENCE JS0356 !$#authors Aldea, M.; Garrido, T.; Hernandez-Chico, C.; Vicente, M.; !1Kushner, S.R. !$#journal EMBO J. (1989) 8:3923-3931 !$#title Induction of a growth-phase-dependent promoter triggers !1transcription of bolA, an Escherichia coli morphogene. !$#cross-references MUID:90059998; PMID:2684651 !$#accession JS0357 !'##molecule_type DNA !'##residues 1-145 ##label ALD !'##cross-references GB:X17642; NID:g41069; PIDN:CAA35634.1; PID:g41071 REFERENCE A36129 !$#authors Guthrie, B.; Wickner, W. !$#journal J. Bacteriol. (1990) 172:5555-5562 !$#title Trigger factor depletion or overproduction causes defective !1cell division but does not block protein export. !$#cross-references MUID:91008922; PMID:2211496 !$#accession A36129 !'##status preliminary !'##molecule_type DNA !'##residues 1-117,'E',119-278,'RAPSVTALS',288-432 ##label GUT !'##cross-references GB:M34066; NID:g147988; PIDN:AAA62791.1; !1PID:g147989 REFERENCE A36575 !$#authors Maurizi, M.R.; Clark, W.P.; Katayama, Y.; Rudikoff, S.; !1Pumphrey, J.; Bowers, B.; Gottesman, S. !$#journal J. Biol. Chem. (1990) 265:12536-12545 !$#title Sequence and structure of Clp P, the proteolytic component !1of the ATP-dependent Clp protease of Escherichia coli. !$#cross-references MUID:90324245; PMID:2197275 !$#accession A36575 !'##status preliminary !'##molecule_type DNA !'##residues 390-432 ##label MAU !'##cross-references GB:J05534; NID:g145554; PIDN:AAA23587.1; !1PID:g145555 REFERENCE S68370 !$#authors Ruecknagel, K.P.; Kipping, M.; Stoller, G.; Tradler, T.; !1Fischer, G. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S68370 !'##molecule_type protein !'##residues 99-128 ##label RUE !'##experimental_source strain K12, BL21(DE3) REFERENCE S65516 !$#authors Stoller, G.; Tradler, T.; Ruecknagel, K.P.; Rahfeld, J.U.; !1Fischer, G. !$#journal FEBS Lett. (1996) 384:117-122 !$#title An 11.8 kDa proteolytic fragment of the E. coli trigger !1factor represents the domain carrying the peptidyl-prolyl !1cis/trans isomerase activity. !$#cross-references MUID:96201948; PMID:8612805 !$#accession S65516 !'##molecule_type protein !'##residues 1-6;145-174 ##label STO REFERENCE S68845 !$#authors Hesterkamp, T.; Bukau, B. !$#journal FEBS Lett. (1996) 385:67-71 !$#title Identification of the prolyl isomerase domain of Escherichia !1coli trigger factor. !$#cross-references MUID:96200171; PMID:8641469 !$#accession S68845 !'##molecule_type protein !'##residues 117,'E',119-123;132-136;145-149 ##label HES GENETICS !$#gene tig !$#map_position 10 min FUNCTION !$#description may be involved in de novo protein folding; may act with !1signal recognition particle as secretion-specific and !1general molecular chaperone early in protein synthesis; !1involved in protein export CLASSIFICATION #superfamily trigger factor; BKBP-type peptidylprolyl !1isomerase homology KEYWORDS cis-trans-isomerase; molecular chaperone FEATURE !$161-205 #domain BKBP-type peptidylprolyl isomerase homology !8#label PPI SUMMARY #length 432 #molecular-weight 48192 #checksum 2839 SEQUENCE /// ENTRY C64619 #type complete TITLE trigger factor HP0795 [similarity] - Helicobacter pylori (strain 26695) CONTAINS peptidylprolyl isomerase (EC 5.2.1.8), ribosome-bound ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Sep-2000 ACCESSIONS C64619 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession C64619 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-451 ##label TOM !'##cross-references GB:AE000591; GB:AE000511; NID:g2313918; !1PIDN:AAD07843.1; PID:g2313924; TIGR:HP0795 CLASSIFICATION #superfamily trigger factor; BKBP-type peptidylprolyl !1isomerase homology KEYWORDS cis-trans-isomerase FEATURE !$165-209 #domain BKBP-type peptidylprolyl isomerase homology !8#label PPI SUMMARY #length 451 #molecular-weight 51988 #checksum 2066 SEQUENCE /// ENTRY I40755 #type complete TITLE trigger factor 2 [validated] - Campylobacter jejuni CONTAINS peptidylprolyl isomerase (EC 5.2.1.8), ribosome-bound ORGANISM #formal_name Campylobacter jejuni DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Sep-2000 ACCESSIONS I40755; I40756 REFERENCE I40754 !$#authors Griffiths, P.L.; Park, R.W.; Connerton, I.F. !$#journal Microbiology (1995) 141:1359-1367 !$#title The gene for Campylobacter trigger factor: evidence for !1multiple transcription start sites and protein products. !$#cross-references MUID:95400490; PMID:7670637 !$#accession I40755 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-410 ##label RES !'##cross-references EMBL:X85954; NID:g757795; PIDN:CAA59930.1; !1PID:g757797 !'##genetics TG2 !$#accession I40756 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 23-410 ##label RE2 !'##cross-references EMBL:X85954; NID:g757795; PIDN:CAA59931.1; !1PID:g757798 !'##genetics TG3 GENETICS TG2 !$#gene tigP2 GENETICS TG3 !$#gene tigP3 CLASSIFICATION #superfamily trigger factor; BKBP-type peptidylprolyl !1isomerase homology KEYWORDS cis-trans-isomerase FEATURE !$1-410 #product trigger factor 2 #status predicted #label !8TF2\ !$23-410 #product trigger factor 3 #status predicted #label !8TF3\ !$165-209 #domain BKBP-type peptidylprolyl isomerase homology !8#label PPI SUMMARY #length 410 #molecular-weight 47221 #checksum 8142 SEQUENCE /// ENTRY C64226 #type complete TITLE trigger factor MG238 [similarity] - Mycoplasma genitalium CONTAINS peptidylprolyl isomerase (EC 5.2.1.8), ribosome-bound ORGANISM #formal_name Mycoplasma genitalium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Sep-2000 ACCESSIONS C64226 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession C64226 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-444 ##label TIGR !'##cross-references GB:U39701; GB:L43967; NID:g1045915; PID:g1045927; !1TIGR:MG238 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily trigger factor; BKBP-type peptidylprolyl !1isomerase homology KEYWORDS cis-trans-isomerase FEATURE !$170-214 #domain BKBP-type peptidylprolyl isomerase homology !8#label PPI SUMMARY #length 444 #molecular-weight 50931 #checksum 8074 SEQUENCE /// ENTRY CEECQ #type complete TITLE cell division protein ftsQ - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 01-Mar-2002 ACCESSIONS S10852; A23318; A37155; S40603; E64731 REFERENCE S10852 !$#authors Robinson, A.C.; Kenan, D.J.; Hatfull, G.F.; Sullivan, N.F.; !1Spiegelberg, R.; Donachie, W.D. !$#journal J. Bacteriol. (1984) 160:546-555 !$#title DNA sequence and transcriptional organization of essential !1cell division genes ftsQ and ftsA of Escherichia coli: !1evidence for overlapping transcriptional units. !$#cross-references MUID:85054557; PMID:6094474 !$#accession S10852 !'##molecule_type DNA !'##residues 1-276 ##label ROB !'##cross-references EMBL:X02821; NID:g41492; PIDN:CAA26589.1; !1PID:g41493 REFERENCE A92913 !$#authors Yi, Q.M.; Rockenbach, S.; Ward Jr., J.E.; Lutkenhaus, J. !$#journal J. Mol. Biol. (1985) 184:399-412 !$#title Structure and expression of the cell division genes ftsQ, !1ftsA and ftsZ. !$#cross-references MUID:86011551; PMID:2995680 !$#accession A23318 !'##molecule_type DNA !'##residues 1-276 ##label YIQ !'##cross-references GB:X02821; GB:K02668; NID:g41492; PIDN:CAA26589.1; !1PID:g41493 REFERENCE A37155 !$#authors Dewar, S.J.; Donachie, W.D. !$#journal J. Bacteriol. (1990) 172:6611-6614 !$#title Regulation of expression of the ftsA cell division gene by !1sequences in upstream genes. !$#cross-references MUID:91035283; PMID:2228979 !$#accession A37155 !'##molecule_type DNA !'##residues 1-276 ##label DEW REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40603 !'##molecule_type DNA !'##residues 1-276 ##label YUR !'##cross-references EMBL:D10483; NID:g216434; PIDN:BAA01358.1; !1PID:g216507 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64731 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-276 ##label BLAT !'##cross-references GB:AE000118; GB:U00096; NID:g1786262; !1PIDN:AAC73204.1; PID:g1786281; UWGP:b0093 !'##experimental_source strain K-12, substrain MG1655 COMMENT This protein may be involved in anomalous filament growth; !1its gene is located at the 5' end of the ftsA gene, which !1encodes another cell-division protein also involved in !1anomalous filament growth. GENETICS !$#gene ftsQ !$#map_position 2 min CLASSIFICATION #superfamily cell division protein ftsQ KEYWORDS cell division; transmembrane protein FEATURE !$25-41 #domain transmembrane #status predicted #label TMM SUMMARY #length 276 #molecular-weight 31434 #checksum 2765 SEQUENCE /// ENTRY CEECFX #type complete TITLE cell division protein ftsX - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 01-Mar-2002 ACCESSIONS S03132; S47681; A65143 REFERENCE S03129 !$#authors Gill, D.R.; Hatfull, G.F.; Salmond, G.P.C. !$#journal Mol. Gen. Genet. (1986) 205:134-145 !$#title A new cell division operon in Escherichia coli. !$#cross-references MUID:87089083; PMID:3025556 !$#accession S03132 !'##molecule_type DNA !'##residues 1-352 ##label GIL !'##cross-references EMBL:X04398; NID:g41496; PIDN:CAA27986.1; !1PID:g41500 REFERENCE S47666 !$#authors Plunkett, G. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S47681 !'##molecule_type DNA !'##residues 1-352 ##label PLU !'##cross-references EMBL:U00039; NID:g466582; PIDN:AAB18437.1; !1PID:g466598 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65143 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-352 ##label BLAT !'##cross-references GB:AE000422; GB:U00096; NID:g1789868; !1PIDN:AAC76487.1; PID:g1789872; UWGP:b3462 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ftsX !$#map_position 76 min CLASSIFICATION #superfamily cell division protein ftsX KEYWORDS cell division SUMMARY #length 352 #molecular-weight 38543 #checksum 2046 SEQUENCE /// ENTRY CEECFY #type complete TITLE cell division protein ftsY - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 01-Mar-2002 ACCESSIONS S03130; S47683; C65143 REFERENCE S03129 !$#authors Gill, D.R.; Hatfull, G.F.; Salmond, G.P.C. !$#journal Mol. Gen. Genet. (1986) 205:134-145 !$#title A new cell division operon in Escherichia coli. !$#cross-references MUID:87089083; PMID:3025556 !$#accession S03130 !'##molecule_type DNA !'##residues 1-497 ##label GIL !'##cross-references EMBL:X04398; NID:g41496; PIDN:CAA27984.1; !1PID:g41498 REFERENCE S47666 !$#authors Plunkett, G. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S47683 !'##molecule_type DNA !'##residues 1-497 ##label PLU !'##cross-references EMBL:U00039; NID:g466582; PIDN:AAB18439.1; !1PID:g466600 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65143 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-497 ##label BLAT !'##cross-references GB:AE000422; GB:U00096; NID:g1789868; !1PIDN:AAC76489.1; PID:g1789874; UWGP:b3464 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ftsY !$#map_position 76 min CLASSIFICATION #superfamily cell division protein ftsY KEYWORDS cell division; nucleotide binding; P-loop FEATURE !$300-307 #region nucleotide-binding motif A (P-loop)\ !$378-382 #region nucleotide-binding motif B SUMMARY #length 497 #molecular-weight 54513 #checksum 1806 SEQUENCE /// ENTRY CEECZ #type complete TITLE cell division protein ftsZ - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS G64731; B23961; S40605; S10854; C23318 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64731 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-383 ##label BLAT !'##cross-references GB:AE000119; GB:U00096; NID:g1786283; !1PIDN:AAC73206.1; PID:g1786284; UWGP:b0095 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A94665 !$#authors Yi, Q.M.; Lutkenhaus, J. !$#journal Gene (1985) 36:241-247 !$#title The nucleotide sequence of the essential cell-division gene !1ftsZ of Escherichia coli. !$#cross-references MUID:86083166; PMID:3000876 !$#accession B23961 !'##molecule_type DNA !'##residues 1-157,'N',159-221,'H',223-383 ##label YIQ !'##cross-references GB:X55034; GB:M10429; NID:g40841; PIDN:CAA38872.1; !1PID:g40863 REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40605 !'##molecule_type DNA !'##residues 1-157,'N',159-221,'H',223-383 ##label YUR !'##cross-references EMBL:D10483; NID:g216434; PIDN:BAA01360.1; !1PID:g216509 REFERENCE S10852 !$#authors Robinson, A.C.; Kenan, D.J.; Hatfull, G.F.; Sullivan, N.F.; !1Spiegelberg, R.; Donachie, W.D. !$#journal J. Bacteriol. (1984) 160:546-555 !$#title DNA sequence and transcriptional organization of essential !1cell division genes ftsQ and ftsA of Escherichia coli: !1evidence for overlapping transcriptional units. !$#cross-references MUID:85054557; PMID:6094474 !$#accession S10854 !'##molecule_type DNA !'##residues 1-31,'DALKVLN' ##label ROB !'##cross-references EMBL:X02821; NID:g41492; PIDN:CAA26591.1; !1PID:g41495 REFERENCE A58109 !$#authors Mukherjee, A.; Dai, K.; Lutkenhaus, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:1053-1057 !$#title Escherichia coli cell division protein FtsZ is a guanine !1nucleotide binding protein. !$#cross-references MUID:93157341; PMID:8430073 !$#contents annotation !$#note a mutant form in which the motif GGGTGTG became GGGAGTG, !1isolated as resistant to the division inhibitor SulA, !1resembles wild type in structural properties including the !1formation of multimers but is defective in GTP binding COMMENT This cytoplasmic protein associates with the cell membrane !1in the form of a ring just prior to cell division. It is a !1GTP-binding protein capable of self-assembly and is !1essential for cell division. GENETICS !$#gene ftsZ !$#map_position 2 min CLASSIFICATION #superfamily cell division protein ftsZ KEYWORDS cell division; GTP binding FEATURE !$105-111 #region tubulin/FtsZ GTP/GDP-binding (G-G-G-T-G-[ST] !8-G) motif\ !$206-213 #region GTP hydrolizing region SUMMARY #length 383 #molecular-weight 40324 #checksum 2666 SEQUENCE /// ENTRY S58854 #type complete TITLE cell division protein ftsZ2 - Rhizobium meliloti ORGANISM #formal_name Rhizobium meliloti DATE 15-Feb-1996 #sequence_revision 04-Oct-1996 #text_change 16-Jul-1999 ACCESSIONS S58854 REFERENCE S58854 !$#authors Margolin, W.; Long, S.R. !$#journal J. Bacteriol. (1994) 176:2033-2043 !$#title Rhizobium meliloti contains a novel second homolog of the !1cell division gene ftsZ. !$#cross-references MUID:94193551; PMID:8144471 !$#accession S58854 !'##molecule_type DNA !'##residues 1-345 ##label MAR !'##cross-references EMBL:L25440; NID:g452125; PIDN:AAA26281.1; !1PID:g452126 COMMENT This cytoplasmic protein associates with the cell membrane !1at the site of cell division just prior to cell division. It !1is a GTP-binding protein capable of self-assembly and is !1essential for cell division. GENETICS !$#gene ftsZ2 !$#note ftsz2 appears not to be essential for viability CLASSIFICATION #superfamily cell division protein ftsZ KEYWORDS cell division; GTP binding FEATURE !$108-114 #region tubulin/FtsZ GTP/GDP-binding (G-G-G-T-G-[ST] !8-G) motif\ !$209-216 #region GTP hydrolizing SUMMARY #length 345 #molecular-weight 36021 #checksum 5760 SEQUENCE /// ENTRY I64185 #type complete TITLE cell division protein ftsZ - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 18-Aug-1995 #sequence_revision 04-Oct-1996 #text_change 16-Jul-1999 ACCESSIONS I64185 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession I64185 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-421 ##label TIGR !'##cross-references GB:U32794; GB:L42023; NID:g1574694; !1PIDN:AAC22798.1; PID:g1574699; TIGR:HI1143 COMMENT This cytoplasmic protein associates with the cell membrane !1in the form of a ring just prior to cell division. It is a !1GTP-binding protein capable of self-assembly and is !1essential for cell division. GENETICS !$#gene ftsZ CLASSIFICATION #superfamily cell division protein ftsZ KEYWORDS cell division; GTP binding FEATURE !$130-136 #region tubulin/FtsZ GTP/GDP-binding (G-G-G-T-G-[ST] !8-G) motif\ !$231-238 #region GTP-hydrolizing region SUMMARY #length 421 #molecular-weight 45022 #checksum 5641 SEQUENCE /// ENTRY I39848 #type complete TITLE cell division initiation protein (septum formation) FtsZ - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 19-Jul-1996 #sequence_revision 04-Oct-1996 #text_change 16-Jun-2000 ACCESSIONS I39848; A69628 REFERENCE I39846 !$#authors Beall, B.; Lowe, M.; Lutkenhaus, J. !$#journal J. Bacteriol. (1988) 170:4855-4864 !$#title Cloning and characterization of Bacillus subtilis homologs !1of Escherichia coli cell division genes ftsZ and ftsA. !$#cross-references MUID:89008108; PMID:3139638 !$#accession I39848 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-382 ##label RES !'##cross-references GB:M22630; NID:g142938; PIDN:AAA22457.1; !1PID:g142941 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69628 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-382 ##label KUN !'##cross-references GB:Z99111; GB:AL009126; NID:g2633699; !1PIDN:CAB13402.1; PID:g2633900 !'##experimental_source strain 168 COMMENT This cytoplasmic protein associates with the cell membrane !1just prior to cell division. It is a GTP-binding protein !1capable of self-assembly and is essential for septum !1formation during both vegetative and sporulating cell !1divisions. GENETICS !$#gene ftsZ CLASSIFICATION #superfamily cell division protein ftsZ KEYWORDS cell division; GTP binding FEATURE !$106-112 #region tubulin/FtsZ GTP/GDP-binding (G-G-G-T-G-[ST] !8-G) motif SUMMARY #length 382 #molecular-weight 40355 #checksum 296 SEQUENCE /// ENTRY S58814 #type complete TITLE cell division protein ftsZ - Staphylococcus aureus ORGANISM #formal_name Staphylococcus aureus DATE 28-Nov-1995 #sequence_revision 04-Oct-1996 #text_change 16-Jul-1999 ACCESSIONS S58814 REFERENCE S58814 !$#authors Alessi, D.M.; Olson, E.R. !$#submission submitted to the EMBL Data Library, February 1994 !$#description Cloning and sequencing of an ftsZ homologue from !1Staphylococcus aureus. !$#accession S58814 !'##molecule_type DNA !'##residues 1-390 ##label ALE !'##cross-references EMBL:U06462; NID:g458427; PIDN:AAA16512.1; !1PID:g458428 !'##experimental_source strain SA4 COMMENT This cytoplasmic protein associates with the cell membrane !1just prior to cell division. It is a GTP-binding protein !1capable of self-assembly and is essential for cell division. CLASSIFICATION #superfamily cell division protein ftsZ KEYWORDS cell division; GTP binding FEATURE !$106-112 #region tubulin/FtsZ GTP/GDP-binding (G-G-G-T-G-[ST] !8-G) motif\ !$207-214 #region GTP hydrolizing SUMMARY #length 390 #molecular-weight 41037 #checksum 7537 SEQUENCE /// ENTRY JC4289 #type complete TITLE cell division protein ftsZ - Anabaena sp. (PCC 7120) ORGANISM #formal_name Anabaena sp. #variety PCC 7120 DATE 14-Nov-1995 #sequence_revision 04-Oct-1996 #text_change 16-Jul-1999 ACCESSIONS JC4289 REFERENCE JC4289 !$#authors Doherty, H.M.; Adams, D.G. !$#journal Gene (1995) 163:93-96 !$#title Cloning and sequence of ftsZ and flanking regions from the !1cyanobacterium Anabaena PCC7120. !$#cross-references MUID:96001250; PMID:7557485 !$#accession JC4289 !'##molecule_type DNA !'##residues 1-379 ##label DOH !'##cross-references GB:U14408; NID:g555913; PIDN:AAA85526.1; !1PID:g555915 !'##experimental_source PCC 7120 COMMENT This cytoplasmic protein associates with the cell membrane !1just prior to cell division. It is a GTP-binding protein !1capable of self-assembly and is essential for cell division. GENETICS !$#gene ftsZ CLASSIFICATION #superfamily cell division protein ftsZ KEYWORDS cell division; GTP binding FEATURE !$109-115 #region tubulin/FtsZ GTP/GDP-binding (G-G-G-T-G-[ST] !8-G) motif\ !$210-217 #region GTP hydrolizing region SUMMARY #length 379 #molecular-weight 39407 #checksum 9789 SEQUENCE /// ENTRY S60765 #type complete TITLE cell division protein ftsZ - Streptomyces coelicolor ORGANISM #formal_name Streptomyces coelicolor DATE 27-Apr-1996 #sequence_revision 04-Oct-1996 #text_change 21-Jul-2000 ACCESSIONS S60765; T34952 REFERENCE S60763 !$#authors McCormick, J.R.; Su, E.P.; Driks, A.; Losick, R. !$#journal Mol. Microbiol. (1994) 14:243-254 !$#title Growth and viability of Streptomyces coelicolor mutant for !1the cell division gene ftsZ. !$#cross-references MUID:95131746; PMID:7830569 !$#accession S60765 !'##molecule_type DNA !'##residues 1-399 ##label MCC !'##cross-references EMBL:U10879; NID:g4204101; PIDN:AAD10533.1; !1PID:g527649 !'##experimental_source strain A3(2) REFERENCE Z21563 !$#authors Saunders, D.C.; Harris, D.; James, K.D.; Parkhill, J.; !1Barrell, B.G.; Rajandream, M.A. !$#submission submitted to the EMBL Data Library, August 1999 !$#accession T34952 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-399 ##label SAU !'##cross-references EMBL:AL109663; PIDN:CAB51991.1; GSPDB:GN00070; !1SCOEDB:ftsZ !'##experimental_source strain A3(2) COMMENT This cytoplasmic protein associates with the cell membrane !1just prior to cell division. It is a GTP-binding protein !1capable of self-assembly and is essential for cell division. GENETICS !$#gene ftsZ !$#start_codon GTG CLASSIFICATION #superfamily cell division protein ftsZ KEYWORDS cell division; GTP binding FEATURE !$103-109 #region tubulin/FtsZ GTP/GDP-binding (G-G-G-T-G-[ST] !8-G) motif\ !$204-211 #region GTP hydrolizing\ !$383-391 #region hydrophobic SUMMARY #length 399 #molecular-weight 41095 #checksum 9671 SEQUENCE /// ENTRY T44848 #type complete TITLE cell division protein ftsZ [validated] - Halobacterium salinarum ALTERNATE_NAMES GTP-binding protein ftsZ ORGANISM #formal_name Halobacterium salinarum DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 21-Jul-2000 ACCESSIONS T44848 REFERENCE Z22858 !$#authors Margolin, W.; Wang, R.; Kumar, M. !$#journal J. Bacteriol. (1996) 178:1320-1327 !$#title Isolation of an ftsZ homolog from the archaebacterium !1Halobacterium salinarium: implications for the evolution of !1FtsZ and tubulin. !$#cross-references MUID:96200101; PMID:8631708 !$#accession T44848 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-375 ##label MAR !'##cross-references EMBL:U32860; PIDN:AAB06191.1 GENETICS !$#gene ftsZ FUNCTION !$#description involved in cell division; overexpression of ftsZ induces !1significant morphological changes leading to the loss of rod !1shape [validated, MUID:96200101] CLASSIFICATION #superfamily cell division protein ftsZ KEYWORDS cell division; GTP binding SUMMARY #length 375 #molecular-weight 39261 #checksum 319 SEQUENCE /// ENTRY B64346 #type complete TITLE cell division protein FtsZ homolog MJ0370 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 13-Sep-1996 #sequence_revision 04-Oct-1996 #text_change 21-Jul-2000 ACCESSIONS B64346 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession B64346 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-364 ##label BUL !'##cross-references GB:U67490; GB:L77117; NID:g2826276; !1PIDN:AAB98359.1; PID:g1591077; TIGR:MJ0370 COMMENT This protein is the nearer of two homologs in the archeaon !1Methanococcus jannaschii to FtsZ, a GTP-binding protein of !1bacteria (gram-positive, gram-negative, and the Mycoplasmas) !1capable of self-assembly and required for initiating the !1partition between compartments during cell division. GENETICS !$#map_position FOR336314-337408 !$#start_codon GTG CLASSIFICATION #superfamily cell division protein ftsZ KEYWORDS cell division; GTP binding FEATURE !$132-138 #region tubulin/FtsZ GTP/GDP-binding (G-G-G-T-G-[ST] !8-G) motif SUMMARY #length 364 #molecular-weight 38924 #checksum 7796 SEQUENCE /// ENTRY A38119 #type complete TITLE cell division protein FtsZ1 - Rhizobium meliloti ORGANISM #formal_name Rhizobium meliloti DATE 24-Jul-1992 #sequence_revision 04-Oct-1996 #text_change 05-Sep-1997 ACCESSIONS A38119 REFERENCE A38119 !$#authors Margolin, W.; Corbo, J.C.; Long, S.R. !$#journal J. Bacteriol. (1991) 173:5822-5830 !$#title Cloning and characterization of a Rhizobium meliloti homolog !1of the Escherichia coli cell division gene ftsZ. !$#cross-references MUID:91358375; PMID:1653222 !$#accession A38119 !'##molecule_type DNA !'##residues 1-590 ##label MAR !'##cross-references GB:M94386; NID:g152226; PID:g152227 COMMENT This species is unusual among bacteria in having two !1homologs of FtsZ, a GTP-binding protein of bacteria !1(gram-positive, gram-negative, and the Mycoplasmas) capable !1of self-assembly and required for initiating the partition !1between compartments during cell division. GENETICS !$#gene ftsZ1 CLASSIFICATION #superfamily cell division protein ftsZ1 KEYWORDS cell division; GTP binding SUMMARY #length 590 #molecular-weight 62974 #checksum 5437 SEQUENCE /// ENTRY CEECA #type complete TITLE ATP-binding cell division protein FtsA [imported] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 01-Mar-2002 ACCESSIONS B23318; S40604; S10853; B37155; A23961; F64731; S03776 REFERENCE A92913 !$#authors Yi, Q.M.; Rockenbach, S.; Ward Jr., J.E.; Lutkenhaus, J. !$#journal J. Mol. Biol. (1985) 184:399-412 !$#title Structure and expression of the cell division genes ftsQ, !1ftsA and ftsZ. !$#cross-references MUID:86011551; PMID:2995680 !$#accession B23318 !'##molecule_type DNA !'##residues 1-420 ##label YIQ !'##cross-references EMBL:X02821; NID:g41492; PIDN:CAA26590.1; !1PID:g41494 REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40604 !'##molecule_type DNA !'##residues 1-420 ##label YUR !'##cross-references EMBL:D10483; NID:g216434; PIDN:BAA01359.1; !1PID:g216508 REFERENCE S10852 !$#authors Robinson, A.C.; Kenan, D.J.; Hatfull, G.F.; Sullivan, N.F.; !1Spiegelberg, R.; Donachie, W.D. !$#journal J. Bacteriol. (1984) 160:546-555 !$#title DNA sequence and transcriptional organization of essential !1cell division genes ftsQ and ftsA of Escherichia coli: !1evidence for overlapping transcriptional units. !$#cross-references MUID:85054557; PMID:6094474 !$#accession S10853 !'##molecule_type DNA !'##residues 1-338,'R',340-420 ##label ROB !'##cross-references EMBL:X02821; NID:g41492; PIDN:CAA26590.1; !1PID:g41494 REFERENCE A37155 !$#authors Dewar, S.J.; Donachie, W.D. !$#journal J. Bacteriol. (1990) 172:6611-6614 !$#title Regulation of expression of the ftsA cell division gene by !1sequences in upstream genes. !$#cross-references MUID:91035283; PMID:2228979 !$#accession B37155 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-116 ##label DEW REFERENCE A94665 !$#authors Yi, Q.M.; Lutkenhaus, J. !$#journal Gene (1985) 36:241-247 !$#title The nucleotide sequence of the essential cell-division gene !1ftsZ of Escherichia coli. !$#cross-references MUID:86083166; PMID:3000876 !$#accession A23961 !'##molecule_type DNA !'##residues 318-420 ##label YI2 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64731 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-420 ##label BLAT !'##cross-references GB:AE000118; GB:U00096; NID:g1786262; !1PIDN:AAC73205.1; PID:g1786282; UWGP:b0094 !'##experimental_source strain K-12, substrain MG1655 COMMENT This protein may be involved in anomalous filament growth. GENETICS !$#gene ftsA !$#map_position 2 min FUNCTION !$#description ftsA is localized to the septum in a ring pattern; !1interaction with ftsZ CLASSIFICATION #superfamily cell division protein ftsA KEYWORDS cell division SUMMARY #length 420 #molecular-weight 45330 #checksum 5676 SEQUENCE /// ENTRY BVECEA #type complete TITLE UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase (EC 3.5.1.-) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Dec-1988 #text_change 01-Mar-2002 ACCESSIONS A28381; S40606; H64731; C23961 REFERENCE A91852 !$#authors Beall, B.; Lutkenhaus, J. !$#journal J. Bacteriol. (1987) 169:5408-5415 !$#title Sequence analysis, transcriptional organization, and !1insertional mutagenesis of the envA gene of Escherichia !1coli. !$#cross-references MUID:88058745; PMID:2824434 !$#accession A28381 !'##molecule_type DNA !'##residues 1-305 ##label BEA !'##cross-references GB:X55034; GB:M10429; NID:g40841; PIDN:CAA38873.1; !1PID:g40864 REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40606 !'##status preliminary !'##molecule_type DNA !'##residues 1-305 ##label YUR !'##cross-references EMBL:D10483; NID:g216434; PIDN:BAA01361.1; !1PID:g216510 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64731 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-305 ##label BLAT !'##cross-references GB:AE000119; GB:U00096; NID:g1786283; !1PIDN:AAC73207.1; PID:g1786285; UWGP:b0096 !'##experimental_source strain K-12, substrain MG1655 COMMENT This protein is involved in cell envelope formation and !1anomalous cell division; its gene is located at the 3' end !1of ftsZ, which carries out an essential step in the cell !1division process. GENETICS !$#gene lpxC; envA !$#map_position 2 min FUNCTION !$#pathway lipid A biosynthesis CLASSIFICATION #superfamily envA protein KEYWORDS cell division; hydrolase; lipid A biosynthesis SUMMARY #length 305 #molecular-weight 33956 #checksum 9505 SEQUENCE /// ENTRY BVECMG #type complete TITLE UDP-N-acetylglucosamine-N-acetylmuramyl- (pentapeptide)pyrophosphoryl-undecaprenol N-acetylglucosamine transferase (EC 2.4.1.-) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 01-Mar-2002 ACCESSIONS JQ0544; JH0093; S40600; B64731 REFERENCE JQ0544 !$#authors Ikeda, M.; Wachi, M.; Jung, H.K.; Ishino, F.; Matsuhashi, M. !$#journal Nucleic Acids Res. (1990) 18:4014 !$#title Nucleotide sequence involving murG and murC in the mra gene !1cluster region of Escherichia coli. !$#cross-references MUID:90326550; PMID:2197603 !$#accession JQ0544 !'##molecule_type DNA !'##residues 1-355 ##label IKE !'##cross-references EMBL:X52644; NID:g42053; PIDN:CAA36867.1; !1PID:g42055 REFERENCE JH0093 !$#authors Mengin-Lecreulx, D.; Texier, L.; van Heijenoort, J. !$#journal Nucleic Acids Res. (1990) 18:2810 !$#title Nucleotide sequence of the cell-envelope murG gene of !1Escherichia coli. !$#cross-references MUID:90251461; PMID:2187180 !$#accession JH0093 !'##molecule_type DNA !'##residues 1-355 ##label MEN !'##cross-references EMBL:X52540; NID:g42051; PIDN:CAA36776.1; !1PID:g42052 !'##experimental_source strain K12 !'##note it is uncertain whether Met-1 or Met-9 is the initiator !'##note the codon GTA given for residue 274 is inconsistent with the !1authors' translation and with the nucleotide sequence !1submitted to EMBL REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40600 !'##molecule_type DNA !'##residues 1-355 ##label YUR !'##cross-references EMBL:D10483; NID:g216434; PIDN:BAA01355.1; !1PID:g216504 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64731 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-355 ##label BLAT !'##cross-references GB:AE000118; GB:U00096; NID:g1786262; !1PIDN:AAC73201.1; PID:g1786278; UWGP:b0090 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene murG !$#map_position 2 min FUNCTION !$#description involved in murein or cell envelope biosynthesis !$#pathway peptidoglycan biosynthesis CLASSIFICATION #superfamily murG protein KEYWORDS cell division; cell wall; glycosyltransferase; !1hexosyltransferase; peptidoglycan biosynthesis SUMMARY #length 355 #molecular-weight 37814 #checksum 7018 SEQUENCE /// ENTRY H64438 #type complete TITLE UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase (EC 2.7.8.15) - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS H64438 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession H64438 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-301 ##label BUL !'##cross-references GB:U67554; GB:L77117; NID:g2826365; !1PIDN:AAB99115.1; PID:g1591753; TIGR:MJ1113 GENETICS !$#map_position REV1054913-1054008 CLASSIFICATION #superfamily N-acetylglucosamine-1-phosphate transferase KEYWORDS transferase SUMMARY #length 301 #molecular-weight 33363 #checksum 700 SEQUENCE /// ENTRY BVECPW #type complete TITLE phosphate transport system permease protein pstC - Escherichia coli (strain K-12) ALTERNATE_NAMES phoW protein ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS H65175; A23311 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65175 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-319 ##label BLAT !'##cross-references GB:AE000449; GB:U00096; NID:g2367269; !1PIDN:AAC76750.1; PID:g1790164; UWGP:b3727 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A30382 !$#authors Amemura, M.; Makino, K.; Shinagawa, H.; Kobayashi, A.; !1Nakata, A. !$#journal J. Mol. Biol. (1985) 184:241-250 !$#title Nucleotide sequence of the genes involved in phosphate !1transport and regulation of the phosphate regulon in !1Escherichia coli. !$#cross-references MUID:85293094; PMID:2993631 !$#accession A23311 !'##molecule_type DNA !'##residues 1-119,'G',121-319 ##label AME COMMENT This protein is involved in the negative regulation of gene !1phoA, which codes for alkaline phosphatase. GENETICS !$#gene pstC; phoW !$#map_position 84 min CLASSIFICATION #superfamily phoW protein KEYWORDS phosphate transport; transmembrane protein SUMMARY #length 319 #molecular-weight 34121 #checksum 440 SEQUENCE /// ENTRY BVECPT #type complete TITLE phosphate transport system permease protein pstA - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 01-Mar-2002 ACCESSIONS B23311; G65175 REFERENCE A30382 !$#authors Amemura, M.; Makino, K.; Shinagawa, H.; Kobayashi, A.; !1Nakata, A. !$#journal J. Mol. Biol. (1985) 184:241-250 !$#title Nucleotide sequence of the genes involved in phosphate !1transport and regulation of the phosphate regulon in !1Escherichia coli. !$#cross-references MUID:85293094; PMID:2993631 !$#accession B23311 !'##molecule_type DNA !'##residues 1-296 ##label AME !'##cross-references GB:X02723; NID:g42395; PIDN:CAA26508.1; PID:g42397 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65175 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-296 ##label BLAT !'##cross-references GB:AE000449; GB:U00096; NID:g2367269; !1PIDN:AAC76749.1; PID:g1790163; UWGP:b3726 !'##experimental_source strain K-12, substrain MG1655 COMMENT This is one of the proteins required for !1binding-protein-mediated phosphate transport; it is involved !1in the negative regulation of the phosphate regulon. GENETICS !$#gene pstA; phoT !$#map_position 84 min CLASSIFICATION #superfamily phoW protein KEYWORDS phosphate transport; transmembrane protein SUMMARY #length 296 #molecular-weight 32321 #checksum 3246 SEQUENCE /// ENTRY G64120 #type complete TITLE phoT protein - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS G64120 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession G64120 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-282 ##label TIGR !'##cross-references GB:U32818; GB:L42023; NID:g1574209; !1PIDN:AAC23026.1; PID:g1574214; TIGR:HI1381 GENETICS !$#gene phoT FUNCTION !$#description required for binding-protein-mediated phosphate transport; !1involved in the negative regulation of the phosphate regulon CLASSIFICATION #superfamily phoW protein KEYWORDS phosphate transport; transmembrane protein SUMMARY #length 282 #molecular-weight 31194 #checksum 7963 SEQUENCE /// ENTRY F64637 #type complete TITLE D-alanine/glycine transport protein, sodium-dependent - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS F64637 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession F64637 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-450 ##label TOM !'##cross-references GB:AE000603; GB:AE000511; NID:g2314075; !1PIDN:AAD07987.1; PID:g2314080; TIGR:HP0942 CLASSIFICATION #superfamily sodium-dependent D-alanine/glycine transport !1protein SUMMARY #length 450 #molecular-weight 48725 #checksum 5934 SEQUENCE /// ENTRY H64099 #type complete TITLE probable amino acid transport protein HI0883, sodium-dependent - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS H64099 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession H64099 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-456 ##label TIGR !'##cross-references GB:U32770; GB:L42023; NID:g1573898; !1PIDN:AAC22541.1; PID:g1573900; TIGR:HI0883 CLASSIFICATION #superfamily sodium-dependent D-alanine/glycine transport !1protein KEYWORDS amino acid transport; transmembrane protein SUMMARY #length 456 #molecular-weight 48827 #checksum 4031 SEQUENCE /// ENTRY I64144 #type complete TITLE probable amino acid transport protein HI0183, sodium-dependent - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS I64144 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession I64144 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-481 ##label TIGR !'##cross-references GB:U32703; GB:L42023; NID:g1573133; !1PIDN:AAC21852.1; PID:g1573139; TIGR:HI0183 CLASSIFICATION #superfamily sodium-dependent D-alanine/glycine transport !1protein KEYWORDS amino acid transport; transmembrane protein SUMMARY #length 481 #molecular-weight 52953 #checksum 7535 SEQUENCE /// ENTRY S25276 #type complete TITLE D-alanine/glycine transport protein, sodium-dependent - Alteromonas haloplanktis ALTERNATE_NAMES D-alanine permease; dAgA permease ORGANISM #formal_name Alteromonas haloplanktis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S25276 REFERENCE S25276 !$#authors MacLeod, P.R.; MacLeod, R.A. !$#journal Mol. Microbiol. (1992) 6:2673-2681 !$#title Identification and sequence of a Na(+)-linked gene from the !1marine bacterium Alteromonas haloplanktis which functionally !1complements the dagA gene of Escherichia coli. !$#cross-references MUID:93078621; PMID:1447975 !$#accession S25276 !'##molecule_type DNA !'##residues 1-542 ##label MAC !'##cross-references EMBL:M59081; NID:g141991; PIDN:AAA21984.1; !1PID:g141992 GENETICS !$#gene dagA CLASSIFICATION #superfamily sodium-dependent D-alanine/glycine transport !1protein KEYWORDS amino acid transport; transmembrane protein FEATURE !$4-23 #domain transmembrane #status predicted #label TM1\ !$68-103 #domain transmembrane #status predicted #label TM2\ !$136-154 #domain transmembrane #status predicted #label TM3\ !$165-190 #domain transmembrane #status predicted #label TM4\ !$193-216 #domain transmembrane #status predicted #label TM5\ !$289-309 #domain transmembrane #status predicted #label TM6\ !$310-444 #domain extracellular #status predicted #label EXT\ !$445-462 #domain transmembrane #status predicted #label TM7\ !$484-521 #domain transmembrane #status predicted #label TM8 SUMMARY #length 542 #molecular-weight 59023 #checksum 2484 SEQUENCE /// ENTRY A45111 #type complete TITLE D-alanine/glycine transport protein, sodium-dependent - thermophilic bacterium PS-3 ALTERNATE_NAMES alanine carrier protein ORGANISM #formal_name thermophilic bacterium PS-3 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A45111; S27733 REFERENCE A45111 !$#authors Kamata, H.; Akiyama, S.; Morosawa, H.; Ohta, T.; Hamamoto, !1T.; Kambe, T.; Kagawa, Y.; Hirata, H. !$#journal J. Biol. Chem. (1992) 267:21650-21655 !$#title Primary structure of the alanine carrier protein of !1thermophilic bacterium PS3. !$#cross-references MUID:93016116; PMID:1400476 !$#accession A45111 !'##status preliminary !'##molecule_type DNA; protein !'##residues 1-445 ##label KAM !'##cross-references EMBL:D12512; NID:g217143; PIDN:BAA02075.1; !1PID:g217144 !'##note sequence extracted from NCBI backbone (NCBIP:116796) CLASSIFICATION #superfamily sodium-dependent D-alanine/glycine transport !1protein KEYWORDS transmembrane protein SUMMARY #length 445 #molecular-weight 47804 #checksum 979 SEQUENCE /// ENTRY BVECPU #type complete TITLE peripheral membrane protein U - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 01-Mar-2002 ACCESSIONS D23311; E65175 REFERENCE A30382 !$#authors Amemura, M.; Makino, K.; Shinagawa, H.; Kobayashi, A.; !1Nakata, A. !$#journal J. Mol. Biol. (1985) 184:241-250 !$#title Nucleotide sequence of the genes involved in phosphate !1transport and regulation of the phosphate regulon in !1Escherichia coli. !$#cross-references MUID:85293094; PMID:2993631 !$#accession D23311 !'##molecule_type DNA !'##residues 1-241 ##label AME !'##cross-references GB:X02723; NID:g42395; PIDN:CAA26510.1; PID:g42399 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65175 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-241 ##label BLAT !'##cross-references GB:AE000449; GB:U00096; NID:g2367269; !1PIDN:AAC76747.1; PID:g1790161; UWGP:b3724 !'##experimental_source strain K-12, substrain MG1655 COMMENT This is one of the proteins involved in the negative !1regulation of the phosphate regulon of the !1binding-protein-mediated inorganic phosphate transport !1system. GENETICS !$#gene phoU !$#map_position 84 min CLASSIFICATION #superfamily phoU protein KEYWORDS phosphate transport; transcription regulation SUMMARY #length 241 #molecular-weight 27417 #checksum 4120 SEQUENCE /// ENTRY B70105 #type complete TITLE phosphate transport system regulatory protein (phoU) homolog - Lyme disease spirochete ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B70105 REFERENCE A70100 !$#authors Fraser, C.M.; Casjens, S.; Huang, W.M.; Sutton, G.G.; !1Clayton, R.; Lathigra, R.; White, O.; Ketchum, K.A.; Dodson, !1R.; Hickey, E.K.; Gwinn, M.; Dougherty, B.; Tomb, J.F.; !1Fleischmann, R.D.; Richardson, D.; Peterson, J.; Kerlavage, !1A.R.; Quackenbush, J.; Salzberg, S.; Hanson, M.; Vugt, R.V.; !1Palmer, N.; Adams, M.D.; Gocayne, J.; Weidman, J.; !1Utterback, T.; Watthey, L.; McDonald, L.; Artiach, P.; !1Bowman, C.; Garland, S.; Fujii, C.; Cotton, M.D.; Horst, K.; !1Roberts, K.; Hatch, B.; Smith, H.O.; Venter, J.C. !$#journal Nature (1997) 390:580-586 !$#title Genomic sequence of a Lyme disease spirochaete, Borrelia !1burgdorferi. !$#cross-references MUID:98065943; PMID:9403685 !$#accession B70105 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-223 ##label KLE !'##cross-references GB:AE001118; GB:AE000783; NID:g2687921; !1PIDN:AAC66437.1; PID:g2687929; TIGR:BB0042 !'##experimental_source strain B31 CLASSIFICATION #superfamily phoU protein SUMMARY #length 223 #molecular-weight 25980 #checksum 5008 SEQUENCE /// ENTRY S65576 #type complete TITLE phosphate uptake regulatory protein PhoU PA5365 [imported] - Pseudomonas aeruginosa ORGANISM #formal_name Pseudomonas aeruginosa DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 31-Dec-2000 ACCESSIONS S68596; H82975; S65576 REFERENCE S68594 !$#authors Kato, J.; Sakai, Y.; Nikata, T.; Ohtake, H. !$#journal J. Bacteriol. (1994) 176:5874-5877 !$#title Cloning and characterization of a Pseudomonas aeruginosa !1gene involved in the negative regulation of phosphate taxis. !$#cross-references MUID:94364974; PMID:8083184 !$#accession S68596 !'##status preliminary; nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-242 ##label KAT !'##cross-references EMBL:D28587 REFERENCE A82950 !$#authors Stover, C.K.; Pham, X.Q.; Erwin, A.L.; Mizoguchi, S.D.; !1Warrener, P.; Hickey, M.J.; Brinkman, F.S.L.; Hufnagle, !1W.O.; Kowalik, D.J.; Lagrou, M.; Garber, R.L.; Goltry, L.; !1Tolentino, E.; Westbrook-Wadman, S.; Yuan, Y.; Brody, L.L.; !1Coulter, S.N.; Folger, K.R.; Kas, A.; Larbig, K.; Lim, R.M.; !1Smith, K.A.; Spencer, D.H.; Wong, G.K.S.; Wu, Z.; Paulsen, !1I.T.; Reizer, J.; Saier, M.H.; Hancock, R.E.W.; Lory, S.; !1Olson, M.V. !$#journal Nature (2000) 406:959-964 !$#title Complete genome sequence of Pseudomonas aeruginosa PA01, an !1opportunistic pathogen. !$#cross-references MUID:20437337; PMID:10984043 !$#accession H82975 !'##status preliminary !'##molecule_type DNA !'##residues 1-242 ##label STO !'##cross-references GB:AE004948; GB:AE004091; NID:g9951680; !1PIDN:AAG08750.1; GSPDB:GN00131; PASP:PA5365 !'##experimental_source strain PAO1 GENETICS !$#gene phoU; PA5365 CLASSIFICATION #superfamily phoU protein SUMMARY #length 242 #molecular-weight 27487 #checksum 7673 SEQUENCE /// ENTRY S74541 #type complete TITLE negative regulator phoU - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES hypothetical protein slr0741 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S74541 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74541 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-224 ##label KAN !'##cross-references EMBL:D90899; GB:AB001339; NID:g1651650; !1PIDN:BAA16693.1; PID:g1651765 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene phoU CLASSIFICATION #superfamily phoU protein SUMMARY #length 224 #molecular-weight 25767 #checksum 3632 SEQUENCE /// ENTRY C64245 #type complete TITLE peripheral membrane protein U homolog - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 07-Dec-1999 ACCESSIONS C64245 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession C64245 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-225 ##label TIGR !'##cross-references GB:U39726; GB:L43967; NID:g1046113; PID:g1046123; !1TIGR:MG409 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily phoU protein SUMMARY #length 225 #molecular-weight 27042 #checksum 7410 SEQUENCE /// ENTRY S73560 #type complete TITLE phosphate transport system regulatory protein phoU - Mycoplasma pneumoniae (strain ATCC 29342) ALTERNATE_NAMES hypothetical protein C12_orf225 ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Dec-1999 ACCESSIONS S73560 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73560 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-225 ##label HIM !'##cross-references EMBL:AE000023; GB:U00089; NID:g1673893; !1PIDN:AAB95882.1; PID:g1673901 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#gene phoU !$#genetic_code SGC3 CLASSIFICATION #superfamily phoU protein SUMMARY #length 225 #molecular-weight 26856 #checksum 447 SEQUENCE /// ENTRY F69098 #type complete TITLE phosphate transport system regulator - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS F69098 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession F69098 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-217 ##label MTH !'##cross-references GB:AE000929; GB:AE000666; NID:g2622853; !1PIDN:AAB86202.1; PID:g2622863 !'##experimental_source strain Delta H GENETICS !$#gene MTH1732 !$#start_codon GTG CLASSIFICATION #superfamily phoU protein SUMMARY #length 217 #molecular-weight 24913 #checksum 1863 SEQUENCE /// ENTRY H69098 #type complete TITLE phosphate transport system regulator - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS H69098 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession H69098 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-219 ##label MTH !'##cross-references GB:AE000929; GB:AE000666; NID:g2622853; !1PIDN:AAB86204.1; PID:g2622865 !'##experimental_source strain Delta H GENETICS !$#gene MTH1734 CLASSIFICATION #superfamily phoU protein SUMMARY #length 219 #molecular-weight 25642 #checksum 6965 SEQUENCE /// ENTRY H64425 #type complete TITLE phosphate transport system regulatory protein homolog - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H64425 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession H64425 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-236 ##label BUL !'##cross-references GB:U67543; GB:L77117; NID:g1591663; !1PIDN:AAB99011.1; PID:g1591668; TIGR:MJ1009 GENETICS !$#map_position REV939905-939195 CLASSIFICATION #superfamily phoU protein SUMMARY #length 236 #molecular-weight 27426 #checksum 9416 SEQUENCE /// ENTRY BVECRB #type complete TITLE relB protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 01-Mar-2002 ACCESSIONS A22830; G64911 REFERENCE A22830 !$#authors Bech, F.W.; Jorgensen, S.T.; Diderichsen, B.; Karlstrom, !1O.H. !$#journal EMBO J. (1985) 4:1059-1066 !$#title Sequence of the relB transcription unit from Escherichia !1coli and identification of the relB gene. !$#cross-references MUID:85257499; PMID:2990907 !$#accession A22830 !'##molecule_type DNA !'##residues 1-79 ##label BEC !'##cross-references GB:X02405; NID:g42699; PIDN:CAA26250.1; PID:g42700 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64911 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-79 ##label BLAT !'##cross-references GB:AE000253; GB:U00096; NID:g1787841; !1PIDN:AAC74637.1; PID:g1787847; UWGP:b1564 !'##experimental_source strain K-12, substrain MG1655 COMMENT In E. coli, shortage of amino acids causes RNA synthesis to !1be greatly reduced. Mutants lacking this type of regulation !1are said to be relaxed. The response of the relaxed relB to !1amino acid starvation is the accumulation of a translational !1inhibitor. GENETICS !$#gene relB !$#map_position 34 min CLASSIFICATION #superfamily relB protein SUMMARY #length 79 #molecular-weight 9071 #checksum 3157 SEQUENCE /// ENTRY BVECMB #type complete TITLE mcrC protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 01-Mar-2002 ACCESSIONS JS0121; S56571; B36708; C65249 REFERENCE A91894 !$#authors Ross, T.K.; Achberger, E.C.; Braymer, H.D. !$#journal J. Bacteriol. (1989) 171:1974-1981 !$#title Nucleotide sequence of the McrB region of Escherichia coli !1K-12 and evidence for two independent translational !1initiation sites at the mcrB locus. !$#cross-references MUID:89197765; PMID:2649480 !$#accession JS0121 !'##molecule_type DNA !'##residues 1-348 ##label ROS !'##cross-references GB:M24927; NID:g146789; PIDN:AAA24144.1; !1PID:g146792 !'##experimental_source strain K12 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56571 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-348 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97242.1; !1PID:g537187 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A36708 !$#authors Dila, D.; Sutherland, E.; Moran, L.; Slatko, B.; Raleigh, !1E.A. !$#journal J. Bacteriol. (1990) 172:4888-4900 !$#title Genetic and sequence organization of the mcrBC locus of !1Escherichia coli K-12. !$#cross-references MUID:90368539; PMID:2203735 !$#accession B36708 !'##status preliminary !'##molecule_type DNA !'##residues 'MDQQIIRGLIV',2-348 ##label DIL !'##cross-references GB:M58752; GB:M34235; NID:g146795; PIDN:AAA24146.1; !1PID:g146797 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65249 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-348 ##label BLAT !'##cross-references GB:AE000505; GB:U00096; NID:g2367375; !1PIDN:AAC77301.1; PID:g1790804; UWGP:b4345 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene mcrC !$#map_position 99 min !$#start_codon GTG FUNCTION !$#description essential to the mcrB restriction system, which is specific !1for DNA containing 5-methylcytosine CLASSIFICATION #superfamily mcrC protein KEYWORDS restriction modification system SUMMARY #length 348 #molecular-weight 40589 #checksum 3981 SEQUENCE /// ENTRY S47532 #type complete TITLE chaperonin groES - human ALTERNATE_NAMES chaperonin 10; co-chaperonin; heat shock protein 10 (hsp10) ORGANISM #formal_name Homo sapiens #common_name man DATE 27-Jan-1995 #sequence_revision 27-Jan-1995 #text_change 16-Jul-1999 ACCESSIONS S47532; S47634; S45625 REFERENCE S47532 !$#authors Chen, J.J.; McNealy, D.J.; Dalal, S.; Androphy, E.J. !$#journal Biochim. Biophys. Acta (1994) 1219:189-190 !$#title Isolation, sequence analysis and characterization of a cDNA !1encoding human chaperonin 10. !$#cross-references MUID:94368854; PMID:7916212 !$#accession S47532 !'##status preliminary !'##molecule_type mRNA !'##residues 1-102 ##label CHE !'##cross-references EMBL:U07550; NID:g469170; PIDN:AAA50953.1; !1PID:g469171 REFERENCE S47634 !$#authors Monzini, N.; Legname, G.; Marcucci, F.; Gromo, G.; Modena, !1D. !$#journal Biochim. Biophys. Acta (1994) 1218:478-480 !$#title Identification and cloning of human chaperonin 10 homologue. !$#cross-references MUID:94325366; PMID:7914093 !$#accession S47634 !'##status preliminary !'##molecule_type mRNA !'##residues 1-102 ##label MON !'##cross-references EMBL:X75821; NID:g509780; PIDN:CAA53455.1; !1PID:g509781 REFERENCE S45625 !$#authors Cavanagh, A.C.; Morton, H. !$#journal Eur. J. Biochem. (1994) 222:551-560 !$#title The purification of early-pregnancy factor to homogeneity !1from human platelets and identification as chaperonin 10. !$#cross-references MUID:94291652; PMID:7912672 !$#accession S45625 !'##molecule_type protein !'##residues 8-19;28-50,'X',52-54;70-102 ##label CAV GENETICS !$#gene GDB:HSPE1 !'##cross-references GDB:385426; OMIM:600141 !$#map_position 15pter-15q21 COMPLEX functional chaperonin includes 14 chains of groEL and 7 of !1groES FUNCTION !$#description mediates protein folding and renaturation CLASSIFICATION #superfamily chaperonin groES KEYWORDS acetylated amino end; ATP; heat shock; molecular chaperone; !1stress-induced protein FEATURE !$2-102 #product chaperonin groES #status predicted #label !8MAT\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status predicted SUMMARY #length 102 #molecular-weight 10932 #checksum 5119 SEQUENCE /// ENTRY BVECGS #type complete TITLE chaperonin groES - Escherichia coli (strain K-12) ALTERNATE_NAMES heat shock protein groES ORGANISM #formal_name Escherichia coli DATE 31-Dec-1988 #sequence_revision 31-Mar-1992 #text_change 01-Mar-2002 ACCESSIONS S03931; S19084; A29989; S38971; S56370; D65224 REFERENCE S01432 !$#authors Hemmingsen, S.M.; Woolford, C.; van der Vies, S.M.; Tilly, !1K.; Dennis, D.T.; Georgopoulos, C.P.; Hendrix, R.W.; Ellis, !1R.J. !$#journal Nature (1988) 333:330-334 !$#title Homologous plant and bacterial proteins chaperone oligomeric !1protein assembly. !$#cross-references MUID:88232881; PMID:2897629 !$#accession S03931 !'##molecule_type DNA !'##residues 1-97 ##label HEM1 !'##cross-references EMBL:X07850; NID:g41615; PIDN:CAA30697.1; !1PID:g41616 !$#accession S19084 !'##molecule_type protein !'##residues 1-8 ##label HEM2 REFERENCE A92944 !$#authors Miki, T.; Orita, T.; Furuno, M.; Horiuchi, T. !$#journal J. Mol. Biol. (1988) 201:327-338 !$#title Control of cell division by sex factor F in Escherichia !1coli. III. Participation of the groES (mopB) gene of the !1host bacteria. !$#cross-references MUID:88332969; PMID:2901493 !$#accession A29989 !'##molecule_type DNA !'##residues 1-88,'N',90-97 ##label MIK !'##cross-references GB:X07899; NID:g41612; PIDN:CAA30738.1; PID:g41613 !'##note the authors translated the codon AAC for residue 89 as Ser REFERENCE S38970 !$#authors Martin, J.; Geromanos, S.; Tempst, P.; Hartl, F.U. !$#journal Nature (1993) 366:279-282 !$#title Identification of nucleotide-binding regions in the !1chaperonin proteins GroEL and GroES. !$#cross-references MUID:94050183; PMID:7901771 !$#accession S38971 !'##molecule_type DNA !'##residues 61-74 ##label MAR REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56370 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-97 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97041.1; !1PID:g536986 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65224 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-97 ##label BLAT !'##cross-references GB:AE000487; GB:U00096; NID:g1790582; !1PIDN:AAC77102.1; PID:g1790585; UWGP:b4142 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene mopB; groES !$#map_position 94 min COMPLEX functional chaperonin includes 14 chains of groEL and 7 of !1groES FUNCTION !$#description mediates protein folding and renaturation CLASSIFICATION #superfamily chaperonin groES KEYWORDS ATP; heat shock; molecular chaperone; stress-induced protein FEATURE !$1-97 #product chaperonin groES #status predicted #label !8MAT SUMMARY #length 97 #molecular-weight 10387 #checksum 6291 SEQUENCE /// ENTRY A42281 #type complete TITLE symbionin symS - pea aphid ALTERNATE_NAMES 10K chaperonin ORGANISM #formal_name Acyrthosiphon pisum #common_name pea aphid DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A42281; S70752; S24480 REFERENCE A42281 !$#authors Ohtaka, C.; Nakamura, H.; Ishikawa, H. !$#journal J. Bacteriol. (1992) 174:1869-1874 !$#title Structures of chaperonins from an intracellular symbiont and !1their functional expression in Escherichia coli groE !1mutants. !$#cross-references MUID:92193273; PMID:1347769 !$#accession A42281 !'##molecule_type DNA !'##residues 1-96 ##label OHT !'##cross-references EMBL:X61150; NID:g5658; PIDN:CAA43459.1; PID:g5659 !'##note sequence extracted from NCBI backbone (NCBIN:88668, !1NCBIP:88673) REFERENCE S70752 !$#authors Ohtaka, C.; Ishikawa, H. !$#journal J. Mol. Evol. (1993) 36:121-126 !$#title Accumulation of adenine and thymine in a groE-homologous !1operon of an intracellular symbiont. !$#cross-references MUID:93164272; PMID:8433382 !$#accession S70752 !'##status preliminary; translation not shown !'##molecule_type DNA !'##residues 1-96 ##label OH2 !'##cross-references EMBL:X61150; NID:g5658; PIDN:CAA43459.1; PID:g5659 COMMENT This protein functions as a molecular chaperone in the !1endosymbiont. GENETICS !$#gene symS CLASSIFICATION #superfamily chaperonin groES KEYWORDS molecular chaperone SUMMARY #length 96 #molecular-weight 10244 #checksum 4110 SEQUENCE /// ENTRY BVMYBA #type complete TITLE chaperonin groES - Mycobacterium tuberculosis ALTERNATE_NAMES 10K antigen; BCG-a homolog; Cpn10; heat shock protein 10K (hsp10); immunogenic protein BCG-a ORGANISM #formal_name Mycobacterium tuberculosis DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jun-2000 ACCESSIONS S01381; A37166; S02727; A47292; G70737; A46481; S18040 REFERENCE S01381 !$#authors Baird, P.N.; Hall, L.M.C.; Coates, A.R.M. !$#journal Nucleic Acids Res. (1988) 16:9047 !$#title A major antigen from Mycobacterium tuberculosis which is !1homologous to the heat shock proteins groES from E. coli and !1the htpA gene product of Coxiella burneti. !$#cross-references MUID:89016584; PMID:2902558 !$#accession S01381 !'##molecule_type DNA !'##residues 1-100 ##label BAI !'##cross-references EMBL:X12598; NID:g44551; PID:g581358 REFERENCE A37166 !$#authors Baird, P.N.; Hall, L.M.C.; Coates, A.R.M. !$#journal J. Gen. Microbiol. (1989) 135:931-939 !$#title Cloning and sequence analysis of the 10 kDa antigen gene of !1Mycobacterium tuberculosis. !$#cross-references MUID:90095443; PMID:2480990 !$#accession A37166 !'##status preliminary !'##molecule_type DNA !'##residues 'V',2-100 ##label BA2 !'##cross-references GB:M25258; GB:X12598 REFERENCE S02727 !$#authors Shinnick, T.M.; Plikaytis, B.B.; Hyche, A.D.; van !1Landingham, R.M.; Walker, L.L. !$#journal Nucleic Acids Res. (1989) 17:1254 !$#title The Mycobacterium tuberculosis BCG-a protein has homology !1with the Escherichia coli GroES protein. !$#cross-references MUID:89160258; PMID:2564178 !$#accession S02727 !'##molecule_type DNA !'##residues 1-100 ##label SHI !'##cross-references EMBL:X13739; NID:g44571; PIDN:CAA32003.1; !1PID:g581360 REFERENCE A47292 !$#authors Kong, T.H.; Coates, A.R.; Butcher, P.D.; Hickman, C.J.; !1Shinnick, T.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:2608-2612 !$#title Mycobacterium tuberculosis expresses two chaperonin-60 !1homologs. !$#cross-references MUID:93219332; PMID:7681982 !$#accession A47292 !'##status preliminary !'##molecule_type DNA !'##residues 1-100 ##label KON !'##cross-references EMBL:X60350; NID:g44599; PIDN:CAA42908.1; !1PID:g581363 !'##note sequence extracted from NCBI backbone (NCBIN:128605, !1NCBIP:128607) REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession G70737 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-100 ##label COL !'##cross-references GB:Z77165; GB:AL123456; NID:g3261609; !1PIDN:CAB01005.1; PID:g1449369 !'##experimental_source strain H37Rv REFERENCE A46481 !$#authors Barnes, P.F.; Mehra, V.; Rivoire, B.; Fong, S.J.; Brennan, !1P.J.; Voegtline, M.S.; Minden, P.; Houghten, R.A.; Bloom, !1B.R.; Modlin, R.L. !$#journal J. Immunol. (1992) 148:1835-1840 !$#title Immunoreactivity of a 10-kDa antigen of Mycobacterium !1tuberculosis. !$#cross-references MUID:92176646; PMID:1371791 !$#accession A46481 !'##status preliminary !'##molecule_type protein !'##residues 2-16 ##label BAR !'##note sequence extracted from NCBI backbone (NCBIP:87128) GENETICS !$#gene groES; cpn10 !$#start_codon GTG COMPLEX functional chaperonin includes 14 chains of groEL and 7 of !1groES FUNCTION !$#description mediates protein folding and renaturation CLASSIFICATION #superfamily chaperonin groES KEYWORDS ATP; heat shock; molecular chaperone; stress-induced protein FEATURE !$2-100 #product chaperonin groES #status experimental #label !8MAT SUMMARY #length 100 #molecular-weight 10804 #checksum 7634 SEQUENCE /// ENTRY BVMY7B #type complete TITLE chaperonin groES - Mycobacterium bovis ALTERNATE_NAMES heat shock protein, 10K (hsp10); immunogenic protein MPB57 ORGANISM #formal_name Mycobacterium bovis DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Jul-1999 ACCESSIONS S01784; A37534; C60278 REFERENCE S01784 !$#authors Yamaguchi, R.; Matsuo, K.; Yamazaki, A.; Nagai, S.; !1Terasaka, K.; Yamada, T. !$#journal FEBS Lett. (1988) 240:115-117 !$#title Immunogenic protein MPB57 from Mycobacterium bovis BCG: !1molecular cloning, nucleotide sequence and expression. !$#cross-references MUID:89052868; PMID:3056744 !$#accession S01784 !'##molecule_type DNA !'##residues 1-100 ##label YAM !'##cross-references EMBL:X13970; NID:g44190; PIDN:CAA32149.1; !1PID:g581313 !$#accession A37534 !'##molecule_type protein !'##residues 2-21 ##label YAM2 REFERENCE A60278 !$#authors Fifis, T.; Costopoulos, C.; Radford, A.J.; Bacic, A.; Wood, !1P.R. !$#journal Infect. Immun. (1991) 59:800-807 !$#title Purification and characterization of major antigens from a !1Mycobacterium bovis culture filtrate. !$#cross-references MUID:91147217; PMID:1900061 !$#accession C60278 !'##molecule_type protein !'##residues 2-15,'E',17-20 ##label FIF GENETICS !$#gene groES !$#start_codon GTG CLASSIFICATION #superfamily chaperonin groES KEYWORDS heat shock; molecular chaperone; stress-induced protein FEATURE !$2-100 #product chaperonin groES #status predicted #label !8MAT SUMMARY #length 100 #molecular-weight 10950 #checksum 7378 SEQUENCE /// ENTRY A43827 #type complete TITLE chaperonin groES - Brucella abortus ALTERNATE_NAMES heat shock protein, 10K (hsp10) ORGANISM #formal_name Brucella abortus DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS A43827; S22346 REFERENCE A43827 !$#authors Lin, J.; Adams, L.G.; Ficht, T.A. !$#journal Infect. Immun. (1992) 60:2425-2431 !$#title Characterization of the heat shock response in Brucella !1abortus and isolation of the genes encoding the GroE heat !1shock proteins. !$#cross-references MUID:92267660; PMID:1350274 !$#accession A43827 !'##molecule_type DNA !'##residues 1-98 ##label LIN !'##cross-references GB:M83930; NID:g144106; PIDN:AAA22994.1; !1PID:g144107 !'##experimental_source strain S19 REFERENCE S22346 !$#authors Gor, D.; Mayfield, J.E. !$#journal Biochim. Biophys. Acta (1992) 1130:120-122 !$#title Cloning and nucleotide sequence of the Brucella abortus groE !1operon. !$#cross-references MUID:92182006; PMID:1347461 !$#accession S22346 !'##status preliminary !'##molecule_type DNA !'##residues 1-98 ##label GOR !'##cross-references EMBL:M82975; NID:g144109; PIDN:AAA22996.1; !1PID:g144110 GENETICS !$#gene groES COMPLEX functional chaperonin includes 14 chains of groEL and 7 of !1groES FUNCTION !$#description mediates protein folding and renaturation CLASSIFICATION #superfamily chaperonin groES KEYWORDS ATP; heat shock; molecular chaperone; stress-induced protein FEATURE !$2-98 #product chaperonin groES #status predicted #label !8MAT SUMMARY #length 98 #molecular-weight 10393 #checksum 5632 SEQUENCE /// ENTRY BVYCGS #type complete TITLE chaperonin groES - Synechococcus sp. (strain PCC 6301) ALTERNATE_NAMES heat shock protein, 10K (hsp10) ORGANISM #formal_name Synechococcus sp. DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jul-1999 ACCESSIONS S10836; S09619 REFERENCE S07286 !$#authors Cozens, A.L.; Walker, J.E. !$#journal J. Mol. Biol. (1987) 194:359-383 !$#title The organization and sequence of the genes for ATP synthase !1subunits in the cyanobacterium Synechococcus 6301. Support !1for an endosymbiotic origin of chloroplasts. !$#cross-references MUID:87311713; PMID:3041005 !$#accession S10836 !'##molecule_type DNA !'##residues 1-103 ##label COZ !'##cross-references EMBL:X05925; NID:g48021; PIDN:CAA29361.1; !1PID:g48023 COMPLEX functional chaperonin includes 14 chains of groEL and 7 of !1groES FUNCTION !$#description mediates protein folding and renaturation CLASSIFICATION #superfamily chaperonin groES KEYWORDS ATP; heat shock; molecular chaperone; stress-induced protein FEATURE !$2-97 #product chaperonin groES #status predicted #label !8MAT SUMMARY #length 103 #molecular-weight 10811 #checksum 6496 SEQUENCE /// ENTRY E64243 #type complete TITLE heat shock protein 60-like protein homolog - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 07-Dec-1999 ACCESSIONS E64243 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession E64243 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-110 ##label TIGR !'##cross-references GB:U39724; GB:L43967; NID:g1046098; PID:g1046105; !1TIGR:MG393 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily Mycoplasma heat shock protein groES homolog SUMMARY #length 110 #molecular-weight 12029 #checksum 1026 SEQUENCE /// ENTRY S73594 #type complete TITLE heat shock protein groES - Mycoplasma pneumoniae (strain ATCC 29342) ALTERNATE_NAMES hypothetical protein D02_orf116 ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 10-Dec-1999 ACCESSIONS S73594 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73594 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-116 ##label HIM !'##cross-references EMBL:AE000026; GB:U00089; NID:g1673929; !1PIDN:AAB95916.1; PID:g1673938 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#gene groES !$#genetic_code SGC3 CLASSIFICATION #superfamily Mycoplasma heat shock protein groES homolog SUMMARY #length 116 #molecular-weight 12618 #checksum 9841 SEQUENCE /// ENTRY BVECGL #type complete TITLE chaperonin groEL - Escherichia coli (strain K-12) ALTERNATE_NAMES heat shock protein groEL; hsp60; ribosomal protein A [misnomer] ORGANISM #formal_name Escherichia coli DATE 31-Dec-1988 #sequence_revision 23-Sep-1997 #text_change 01-Mar-2002 ACCESSIONS S56371; S01432; B29989; A27607; S38970; S39467; A26222; !1E65224; S65485; Q00189 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56371 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-548 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97042.1; !1PID:g536987 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE S01432 !$#authors Hemmingsen, S.M.; Woolford, C.; van der Vies, S.M.; Tilly, !1K.; Dennis, D.T.; Georgopoulos, C.P.; Hendrix, R.W.; Ellis, !1R.J. !$#journal Nature (1988) 333:330-334 !$#title Homologous plant and bacterial proteins chaperone oligomeric !1protein assembly. !$#cross-references MUID:88232881; PMID:2897629 !$#accession S01432 !'##molecule_type DNA !'##residues 1-261,'A',263-266,'I',268-548 ##label HEM !'##cross-references EMBL:X07850; NID:g41615; PIDN:CAA30698.1; !1PID:g41617 REFERENCE A92944 !$#authors Miki, T.; Orita, T.; Furuno, M.; Horiuchi, T. !$#journal J. Mol. Biol. (1988) 201:327-338 !$#title Control of cell division by sex factor F in Escherichia !1coli. III. Participation of the groES (mopB) gene of the !1host bacteria. !$#cross-references MUID:88332969; PMID:2901493 !$#accession B29989 !'##molecule_type DNA !'##residues 1-82,'G',84,'LQ' ##label MIK !'##cross-references GB:X07899; NID:g41612; PIDN:CAA30739.1; PID:g41614 REFERENCE A27607 !$#authors Subramanian, A.R.; Wittmann-Liebold, B.; Geissler, A.W.; !1Stoffler, G.; Giesen, M. !$#journal FEBS Lett. (1979) 99:357-360 !$#title Comparison of ribosomal protein S1 and the A-protein from !1Escherichia coli. !$#cross-references MUID:79148704; PMID:107049 !$#accession A27607 !'##molecule_type protein !'##residues 2-17,'E',19-21,'R',23-24,'Y' ##label SUB REFERENCE S38970 !$#authors Martin, J.; Geromanos, S.; Tempst, P.; Hartl, F.U. !$#journal Nature (1993) 366:279-282 !$#title Identification of nucleotide-binding regions in the !1chaperonin proteins GroEL and GroES. !$#cross-references MUID:94050183; PMID:7901771 !$#accession S38970 !'##molecule_type DNA !'##residues 471-498 ##label MAR REFERENCE S39467 !$#authors Thomson, G.J.; Coggins, J.R.; Price, N.C. !$#journal FEBS Lett. (1993) 336:19-22 !$#title The reaction of GroEL (cpn 60) with the ATP analogue 2', 3' !1dialdehyde ATP. !$#cross-references MUID:94085583; PMID:7903255 !$#accession S39467 !'##molecule_type protein !'##residues 454-457,'X',459-463;515-518,'X' ##label THO REFERENCE A26222 !$#authors Chanda, P.K.; Ono, M.; Kuwano, M.; Kung, H.F. !$#journal J. Bacteriol. (1985) 161:446-449 !$#title Cloning, sequence analysis, and expression of alteration of !1the mRNA stability gene (ams) of Escherichia coli. !$#cross-references MUID:85104747; PMID:2578448 !$#accession A26222 !'##molecule_type DNA !'##residues 307-342,'R',344-423,'LNWLTCVVRTKTRTWVSKLHCVQW',425-426, !1'RCV',430,'SY' ##label CHA !'##cross-references GB:M11294; NID:g146268; PIDN:AAA23934.1; !1PID:g146269 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65224 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-548 ##label BLAT !'##cross-references GB:AE000487; GB:U00096; NID:g1790582; !1PIDN:AAC77103.1; PID:g1790586; UWGP:b4143 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S65485 !$#authors Randak, C.; Roscher, A.A.; Hadorn, H.B.; Assfalg-Machleidt, !1I.; Auerswald, E.A.; Machleidt, W. !$#journal FEBS Lett. (1995) 363:189-194 !$#title Expression and functional properties of the second predicted !1nucleotide binding fold of the cystic fibrosis transmembrane !1conductance regulator fused to glutathione-S-transferase. !$#cross-references MUID:95246872; PMID:7537226 !$#accession S65485 !'##molecule_type protein !'##residues 365-371 ##label RAN GENETICS !$#gene mopA; groEL; ams !$#map_position 94 min COMPLEX homotetradecamer; functional chaperonin includes 7 chains of !1groES FUNCTION !$#description mediates protein folding and renaturation !$#note may be involved in the morphogenesis of certain !1bacteriophages and in the coupling between replication of !1the F plasmid and cell division CLASSIFICATION #superfamily chaperonin groEL KEYWORDS ATP; heat shock; molecular chaperone; stress-induced protein FEATURE !$2-548 #product chaperonin groEL #status predicted #label !8MAT SUMMARY #length 548 #molecular-weight 57328 #checksum 4111 SEQUENCE /// ENTRY B43827 #type complete TITLE chaperonin groEL - Brucella abortus (strain S19) ALTERNATE_NAMES 62K heat shock protein (Hsp62) ORGANISM #formal_name Brucella abortus DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS B43827 REFERENCE A43827 !$#authors Lin, J.; Adams, L.G.; Ficht, T.A. !$#journal Infect. Immun. (1992) 60:2425-2431 !$#title Characterization of the heat shock response in Brucella !1abortus and isolation of the genes encoding the GroE heat !1shock proteins. !$#cross-references MUID:92267660; PMID:1350274 !$#accession B43827 !'##molecule_type DNA !'##residues 1-544 ##label LIN !'##cross-references GB:M83930; NID:g144106; PIDN:AAA22995.1; !1PID:g144108 COMPLEX homotetradecamer; functional chaperonin includes 7 chains of !1groES FUNCTION !$#description mediates protein folding and renaturation CLASSIFICATION #superfamily chaperonin groEL KEYWORDS ATP; heat shock; molecular chaperone; stress-induced protein FEATURE !$2-544 #product chaperonin groEL #status predicted #label !8MAT SUMMARY #length 544 #molecular-weight 57569 #checksum 6249 SEQUENCE /// ENTRY A32800 #type complete TITLE chaperonin GroEL precursor - human ALTERNATE_NAMES chaperonin 60K (cpn60); GroEL homolog; heat shock protein 60 (HSP60); mitochondrial protein P1; ribosomal protein A [misnomer] ORGANISM #formal_name Homo sapiens #common_name man DATE 22-Nov-1989 #sequence_revision 07-Jul-1995 #text_change 04-Feb-2000 ACCESSIONS A32800; I53042; B33178; S01666; A35475 REFERENCE A32800 !$#authors Jindal, S.; Dudani, A.K.; Singh, B.; Harley, C.B.; Gupta, !1R.S. !$#journal Mol. Cell. Biol. (1989) 9:2279-2283 !$#title Primary structure of a human mitochondrial protein !1homologous to the bacterial and plant chaperonins and to the !165-kilodalton mycobacterial antigen. !$#cross-references MUID:89313783; PMID:2568584 !$#accession A32800 !'##molecule_type mRNA !'##residues 1-573 ##label JIN !'##cross-references GB:M22382; NID:g190126; PIDN:AAA60127.1; !1PID:g190127 !'##note the sequence shown follows the nucleotide sequence rather than !1the authors' translation for residues 266-270, 272-277, !1279-281, and 283-285 REFERENCE I53042 !$#authors Venner, T.J.; Singh, B.; Gupta, R.S. !$#journal DNA Cell Biol. (1990) 9:545-552 !$#title Nucleotide sequences and novel structural features of human !1and chinese hamster hsp60 (Chaperonin) gene families. !$#cross-references MUID:91103874; PMID:1980192 !$#accession I53042 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-66,'G',68-573 ##label VEN !'##cross-references GB:M34664; NID:g184411; PIDN:AAA36022.1; !1PID:g306890 REFERENCE A33178 !$#authors Ward, L.D.; Hong, J.; Whitehead, R.H.; Simpson, R.J. !$#journal Electrophoresis (1990) 11:883-891 !$#title Development of a database of amino acid sequences for human !1colon carcinoma proteins separated by two-dimensional !1polyacrylamide gel electrophoresis. !$#cross-references MUID:91176935; PMID:2079031 !$#accession B33178 !'##molecule_type protein !'##residues 27-55 ##label WAR REFERENCE S01666 !$#authors Waldinger, D.; Eckerskorn, C.; Lottspeich, F.; Cleve, H. !$#journal Biol. Chem. Hoppe-Seyler (1988) 369:1185-1189 !$#title Amino-acid sequence homology of a polymorphic cellular !1protein from human lymphocytes and the chaperonins from !1Escherichia coli (groEL) and chloroplasts (rubisco-binding !1protein). !$#cross-references MUID:89207104; PMID:2907406 !$#accession S01666 !'##molecule_type protein !'##residues 27-62 ##label WAL !'##note two forms were detected with different isoelectric points but !1identical amino-terminal sequences and amino acid !1composition REFERENCE A35475 !$#authors Singh, B.; Patel, H.V.; Ridley, R.G.; Freeman, K.B.; Gupta, !1R.S. !$#journal Biochem. Biophys. Res. Commun. (1990) 169:391-396 !$#title Mitochondrial import of the human chaperonin (HSP60) !1protein. !$#cross-references MUID:90290472; PMID:1972619 !$#contents annotation GENETICS !$#gene GDB:HSPD1 !'##cross-references GDB:126727; OMIM:118190 !$#map_position 15pter-15q21 COMPLEX homotetradecamer; functional chaperonin includes 7 chains of !1groES FUNCTION !$#description mediates protein folding and renaturation CLASSIFICATION #superfamily chaperonin groEL KEYWORDS ATP; heat shock; mitochondrion; molecular chaperone; !1stress-induced protein FEATURE !$1-26 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$27-573 #product chaperonin groEL #status predicted #label !8MAT SUMMARY #length 573 #molecular-weight 61054 #checksum 3175 SEQUENCE /// ENTRY HHRT60 #type complete TITLE chaperonin groEL precursor - rat ALTERNATE_NAMES heat shock protein, 60K (hsp60); mitochondrial protein P1 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 31-Mar-1991 #sequence_revision 23-Aug-1997 #text_change 16-Jun-2000 ACCESSIONS S13089; S11159 REFERENCE S13089 !$#authors Peralta, D.; Hartman, D.J.; McIntosh, A.M.; Hoogenraad, !1N.J.; Hoj, P.B. !$#journal Nucleic Acids Res. (1990) 18:7162 !$#title cDNA and deduced amino acid sequence of rat liver prehsp60 !1(chaperonin-60). !$#cross-references MUID:91088323; PMID:1979858 !$#accession S13089 !'##molecule_type mRNA !'##residues 1-573 ##label PER !'##cross-references EMBL:X54793; NID:g56382; PIDN:CAA38564.1; !1PID:g56383 REFERENCE S11159 !$#authors Venner, T.J.; Gupta, R.S. !$#journal Nucleic Acids Res. (1990) 18:5309 !$#title Nucleotide sequence of rat hsp60 (chaperonin, GroEL homolog) !1cDNA. !$#cross-references MUID:90384860; PMID:1976241 !$#accession S11159 !'##molecule_type mRNA !'##residues 27-536,'S',538-573 ##label VEN !'##cross-references EMBL:X53585; NID:g56380; PIDN:CAA37654.1; !1PID:g1334284 GENETICS !$#gene hsp60 COMPLEX homotetradecamer; functional chaperonin includes 7 chains of !1groES FUNCTION !$#description mediates protein folding and renaturation CLASSIFICATION #superfamily chaperonin groEL KEYWORDS ATP; heat shock; mitochondrion; molecular chaperone; !1stress-induced protein FEATURE !$1-26 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$27-573 #product chaperonin groEL #status predicted #label !8MAT SUMMARY #length 573 #molecular-weight 60965 #checksum 771 SEQUENCE /// ENTRY HHMS60 #type complete TITLE chaperonin groEL precursor - mouse ALTERNATE_NAMES groEL protein homolog; heat shock protein 60K (hsp60); mitochondrial protein P1 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Mar-1991 #sequence_revision 31-Dec-1992 #text_change 10-Sep-1999 ACCESSIONS S13084; S15929; A41931; S11627 REFERENCE S13084 !$#authors Lotscher, E.; Allison, J.P. !$#journal Nucleic Acids Res. (1990) 18:7153 !$#title Nucleotide and deduced amino acid sequence of a murine cDNA !1clone encoding one member of the hsp65 multigene family. !$#cross-references MUID:91088314; PMID:2263486 !$#accession S13084 !'##molecule_type mRNA !'##residues 1-573 ##label LOT !'##cross-references EMBL:X55023; NID:g51454; PIDN:CAA38762.1; !1PID:g51455 REFERENCE S15929 !$#authors Venner, T.J.; Gupta, R.S. !$#journal Biochim. Biophys. Acta (1990) 1087:336-338 !$#title Nucleotide sequence of mouse HSP60 (chaperonin, GroEL !1homolog) cDNA. !$#cross-references MUID:91064389; PMID:1979012 !$#accession S15929 !'##molecule_type mRNA !'##residues 19-250,'F',252-517,'I',519-573 ##label VEN !'##cross-references EMBL:X53584; NID:g51451; PIDN:CAA37653.1; !1PID:g51452 REFERENCE A41931 !$#authors Ikawa, S.; Weinberg, R.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:2012-2016 !$#title An interaction between p21ras and heat shock protein hsp60, !1a chaperonin. !$#cross-references MUID:92196047; PMID:1347942 !$#accession A41931 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA; protein !'##residues 1-3,'H',5-138,'K',140-517,'I',519-573 ##label IKA !'##cross-references PIDN:AAB21806.1; PID:g247242 !'##note sequence extracted from NCBI backbone (NCBIP:87915) COMPLEX homotetradecamer; functional chaperonin includes 7 chains of !1groES FUNCTION !$#description mediates protein folding and renaturation CLASSIFICATION #superfamily chaperonin groEL KEYWORDS ATP; heat shock; mitochondrion; molecular chaperone; !1stress-induced protein FEATURE !$1-26 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$27-573 #product chaperonin groEL #status predicted #label !8MAT SUMMARY #length 573 #molecular-weight 60941 #checksum 908 SEQUENCE /// ENTRY HHCSBA #type fragment TITLE chaperonin groEL - castor bean (fragment) ALTERNATE_NAMES RUBISCO subunit-binding protein alpha chain ORGANISM #formal_name Ricinus communis #common_name castor bean DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 23-Aug-1997 ACCESSIONS S02199 REFERENCE S01432 !$#authors Hemmingsen, S.M.; Woolford, C.; van der Vies, S.M.; Tilly, !1K.; Dennis, D.T.; Georgopoulos, C.P.; Hendrix, R.W.; Ellis, !1R.J. !$#journal Nature (1988) 333:330-334 !$#title Homologous plant and bacterial proteins chaperone oligomeric !1protein assembly. !$#cross-references MUID:88232881; PMID:2897629 !$#accession S02199 !'##molecule_type mRNA !'##residues 1-495 ##label HEM !'##cross-references EMBL:X07852 COMMENT This protein binds the newly synthesized large subunit and !1the newly imported small subunit of ribulose-bisphosphate !1carboxylase. COMPLEX homotetradecamer; functional chaperonin includes 7 chains of !1groES FUNCTION !$#description mediates protein folding and renaturation CLASSIFICATION #superfamily chaperonin groEL KEYWORDS ATP; chloroplast; heat shock; molecular chaperone; !1stress-induced protein FEATURE !$1-495 #product chaperonin groEL (fragment) #status !8predicted #label MAT SUMMARY #length 495 #checksum 8841 SEQUENCE /// ENTRY HHWTBA #type fragment TITLE chaperonin groEL alpha chain precursor - wheat (fragment) ALTERNATE_NAMES RUBISCO subunit-binding protein alpha chain ORGANISM #formal_name Triticum aestivum #common_name common wheat DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jun-2000 ACCESSIONS S02198; A34973 REFERENCE S01432 !$#authors Hemmingsen, S.M.; Woolford, C.; van der Vies, S.M.; Tilly, !1K.; Dennis, D.T.; Georgopoulos, C.P.; Hendrix, R.W.; Ellis, !1R.J. !$#journal Nature (1988) 333:330-334 !$#title Homologous plant and bacterial proteins chaperone oligomeric !1protein assembly. !$#cross-references MUID:88232881; PMID:2897629 !$#accession S02198 !'##molecule_type mRNA !'##residues 1-543 ##label HEM !'##cross-references EMBL:X07851; NID:g21863; PIDN:CAA30699.1; !1PID:g1345582 !$#accession A34973 !'##molecule_type protein !'##residues 'X',4,'P',6-11,'G',13-22 ##label HEM2 COMMENT This protein binds the newly synthesized large subunit and !1the newly imported small subunit of ribulose-bisphosphate !1carboxylase. COMPLEX homotetradecamer; functional chaperonin includes 7 chains of !1groES FUNCTION !$#description mediates protein folding and renaturation CLASSIFICATION #superfamily chaperonin groEL KEYWORDS ATP; chloroplast; heat shock; molecular chaperone; !1stress-induced protein FEATURE !$1-2 #domain transit peptide (chloroplast) (fragment) !8#status predicted #label TNP\ !$3-543 #product chaperonin groEL alpha chain #status !8predicted #label MAT SUMMARY #length 543 #checksum 5801 SEQUENCE /// ENTRY BVYCGL #type complete TITLE chaperonin groEL - Synechococcus sp. (strain PCC 7942) ORGANISM #formal_name Synechococcus sp. DATE 30-Sep-1991 #sequence_revision 12-Apr-1996 #text_change 16-Jul-1999 ACCESSIONS B36721; S10835; S09620 REFERENCE A36721 !$#authors Webb, R.; Reddy, K.J.; Sherman, L.A. !$#journal J. Bacteriol. (1990) 172:5079-5088 !$#title Regulation and sequence of the Synechococcus sp. strain PCC !17942 groESL operon, encoding a cyanobacterial chaperonin. !$#cross-references MUID:90368561; PMID:1975581 !$#accession B36721 !'##status preliminary !'##molecule_type DNA !'##residues 1-544 ##label WEB !'##cross-references GB:M58751; NID:g154519; PIDN:AAA27314.1; !1PID:g154521 REFERENCE S07286 !$#authors Cozens, A.L.; Walker, J.E. !$#journal J. Mol. Biol. (1987) 194:359-383 !$#title The organization and sequence of the genes for ATP synthase !1subunits in the cyanobacterium Synechococcus 6301. Support !1for an endosymbiotic origin of chloroplasts. !$#cross-references MUID:87311713; PMID:3041005 !$#accession S10835 !'##molecule_type DNA !'##residues 1-300 ##label COZ !'##cross-references EMBL:X05925; NID:g48021; PIDN:CAA29360.1; !1PID:g48022 COMPLEX homotetradecamer; functional chaperonin includes 7 chains of !1groES FUNCTION !$#description mediates protein folding and renaturation CLASSIFICATION #superfamily chaperonin groEL KEYWORDS ATP; heat shock; molecular chaperone; stress-induced protein SUMMARY #length 544 #molecular-weight 58096 #checksum 8399 SEQUENCE /// ENTRY BVECBA #type complete TITLE bolA protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 01-Mar-2002 ACCESSIONS JS0356; S37389; C64773 REFERENCE JS0356 !$#authors Aldea, M.; Garrido, T.; Hernandez-Chico, C.; Vicente, M.; !1Kushner, S.R. !$#journal EMBO J. (1989) 8:3923-3931 !$#title Induction of a growth-phase-dependent promoter triggers !1transcription of bolA, an Escherichia coli morphogene. !$#cross-references MUID:90059998; PMID:2684651 !$#accession JS0356 !'##molecule_type DNA !'##residues 1-116 ##label ALD !'##cross-references GB:X17642; NID:g41069; PIDN:CAA35633.1; PID:g41070 REFERENCE S37389 !$#authors Lindquist, S.; Weston-Hafer, K.; Schmidt, H.; Pul, C.; !1Korfmann, G.; Erickson, J.; Sanders, C.; Martin, H.H.; !1Normark, S. !$#journal Mol. Microbiol. (1993) 9:703-715 !$#title AmpG, a signal transducer in chromosomal beta-lactamase !1induction. !$#cross-references MUID:94049112; PMID:8231804 !$#accession S37389 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-10,'E',12-26 ##label LIN !'##cross-references GB:S67816; NID:g459274; PIDN:AAB28882.1; !1PID:g459275 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64773 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-116 ##label BLAT !'##cross-references GB:AE000149; GB:U00096; NID:g1786628; !1PIDN:AAC73538.1; PID:g1786638; UWGP:b0435 !'##experimental_source strain K-12, substrain MG1655 COMMENT This protein causes round morphology of the organism when !1overexpressed. GENETICS !$#gene bolA FUNCTION !$#description involved in the morphogenetic pathways; probably involved in !1the induction of the expression of penicillin-binding !1protein 6 in the transition of the stationary phase CLASSIFICATION #superfamily bolA protein KEYWORDS DNA binding; transcription regulation FEATURE !$37-56 #domain DNA binding #status predicted #label DBI SUMMARY #length 116 #molecular-weight 13479 #checksum 3393 SEQUENCE /// ENTRY QRSEUB #type complete TITLE sfuB protein - Serratia marcescens ORGANISM #formal_name Serratia marcescens DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 31-Dec-1996 ACCESSIONS B35108 REFERENCE A35108 !$#authors Angerer, A.; Gaisser, S.; Braun, V. !$#journal J. Bacteriol. (1990) 172:572-578 !$#title Nucleotide sequences of the sfuA, sfuB, and sfuC genes of !1Serratia marcescens suggest a !1periplasmic-binding-protein-dependent iron transport !1mechanism. !$#cross-references MUID:90130288; PMID:2404942 !$#accession B35108 !'##molecule_type DNA !'##residues 1-527 ##label ANG COMMENT This hydrophobic protein contains regions corresponding to !1the two integral cytoplasmic membrane proteins usually found !1in binding protein-dependent transport systems. GENETICS !$#gene sfuB CLASSIFICATION #superfamily sfuB protein KEYWORDS binding protein-dependent transport system; inner membrane; !1iron transport SUMMARY #length 527 #molecular-weight 56611 #checksum 5020 SEQUENCE /// ENTRY C64728 #type complete TITLE probable membrane protein yabK - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS C64728; S40583 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64728 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-536 ##label BLAT !'##cross-references GB:AE000117; GB:U00096; NID:g1786250; !1PIDN:AAC73178.1; PID:g1786254; UWGP:b0067 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40583 !'##status preliminary !'##molecule_type DNA !'##residues 1-510,'T',512-536 ##label YUR !'##cross-references EMBL:D10483; NID:g216434; PIDN:BAA01338.1; !1PID:g216487 GENETICS !$#gene yabK CLASSIFICATION #superfamily sfuB protein KEYWORDS transmembrane protein FEATURE !$17-33 #domain transmembrane #status predicted #label TM1\ !$62-78 #domain transmembrane #status predicted #label TM2\ !$95-111 #domain transmembrane #status predicted #label TM3\ !$199-215 #domain transmembrane #status predicted #label TM4\ !$244-260 #domain transmembrane #status predicted #label TM5\ !$295-311 #domain transmembrane #status predicted #label TM6\ !$337-353 #domain transmembrane #status predicted #label TM7\ !$377-393 #domain transmembrane #status predicted #label TM8\ !$407-423 #domain transmembrane #status predicted #label TM9\ !$466-482 #domain transmembrane #status predicted #label TM10\ !$509-525 #domain transmembrane #status predicted #label TM11 SUMMARY #length 536 #molecular-weight 59532 #checksum 9258 SEQUENCE /// ENTRY D64164 #type complete TITLE hypothetical protein HI1020 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS D64164 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession D64164 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-538 ##label TIGR !'##cross-references GB:U32782; GB:L42023; NID:g1574041; !1PIDN:AAC22679.1; PID:g1574049; TIGR:HI1020 !'##note best homolog was a hypothetical protein from Escherichia coli CLASSIFICATION #superfamily sfuB protein SUMMARY #length 538 #molecular-weight 60851 #checksum 4094 SEQUENCE /// ENTRY D64048 #type complete TITLE iron (III) ABC transporter, permease protein hitB [validated] - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES iron utilization protein ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 01-Sep-2000 #text_change 01-Sep-2000 ACCESSIONS T10887; D64048 REFERENCE Z17197 !$#authors Sanders, J.D.; Cope, L.D.; Hansen, E.J. !$#journal Infect. Immun. (1994) 62:4515-4525 !$#title Identification of a locus involved in the utilization of !1iron by Haemophilus influenzae. !$#cross-references MUID:95012644; PMID:7927717 !$#accession T10887 !'##status preliminary !'##molecule_type DNA !'##residues 1-506 ##label SAN !'##cross-references EMBL:S72674; NID:g619397; PIDN:AAB32111.1; !1PID:g619399 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession D64048 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 'M',35-71,'F',73-103,'G',105-115,'V',117-166,'S',168-251, !1'T',253-506 ##label TIGR !'##cross-references GB:U32695; GB:L42023; NID:g1573044; !1PIDN:AAC21774.1; PID:g1573049; TIGR:HI0098 GENETICS !$#gene hitB !$#start_codon GTG CLASSIFICATION #superfamily sfuB protein KEYWORDS binding protein-dependent transport system SUMMARY #length 506 #molecular-weight 56606 #checksum 1064 SEQUENCE /// ENTRY S76051 #type complete TITLE hypothetical protein - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S76051 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76051 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-557 ##label KAN !'##cross-references EMBL:D63999; GB:AB001339; NID:g1001396; !1PIDN:BAA10029.1; PID:g1001407 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily sfuB protein SUMMARY #length 557 #molecular-weight 61597 #checksum 8359 SEQUENCE /// ENTRY S75101 #type complete TITLE hypothetical protein sll0238 - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S75101 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75101 !'##status preliminary !'##molecule_type DNA !'##residues 1-534 ##label KAN !'##cross-references EMBL:D90910; GB:AB001339; NID:g1652956; !1PIDN:BAA17963.1; PID:g1653046 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily sfuB protein SUMMARY #length 534 #molecular-weight 57749 #checksum 8242 SEQUENCE /// ENTRY H64049 #type complete TITLE afuB protein homolog - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS H64049 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession H64049 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-550 ##label TIGR !'##cross-references GB:U32698; GB:L42023; NID:g1573072; PID:g1573082; !1TIGR:HI0129 CLASSIFICATION #superfamily Haemophilus influenzae probable afuB protein SUMMARY #length 550 #molecular-weight 61179 #checksum 4991 SEQUENCE /// ENTRY BVECIS #type complete TITLE istA protein - Escherichia coli plasmid R68.45 insertion sequence IS21 ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jul-1999 ACCESSIONS JV0012 REFERENCE A93128 !$#authors Reimmann, C.; Moore, R.; Little, S.; Savioz, A.; Willetts, !1N.S.; Haas, D. !$#journal Mol. Gen. Genet. (1989) 215:416-424 !$#title Genetic structure, function and regulation of the !1transposable element IS21. !$#cross-references MUID:89218951; PMID:2540414 !$#accession JV0012 !'##molecule_type DNA !'##residues 1-390 ##label REI !'##cross-references GB:X14793; NID:g41826; PIDN:CAA32898.1; PID:g41827 !'##note the authors translated the codon CGT for residue 283 as Leu !'##note it is uncertain whether Met-1 or Met-9 is the initiator COMMENT The istA protein, one of two proteins expressed only when !1there is a tandem repeat of the IS21 insertion sequence, is !1necessary for the transposition of plasmids with that tandem !1repeat (such as plasmid R68.45, which is derived from tandem !1duplication of IS21 on plasmid R68). GENETICS !$#gene istA !$#genome plasmid R68.45 !$#mobile_element insertion sequence IS21 CLASSIFICATION #superfamily istA protein SUMMARY #length 390 #molecular-weight 46025 #checksum 2869 SEQUENCE /// ENTRY TQEC34 #type complete TITLE transposase - Escherichia coli insertion sequence IS3411 ORGANISM #formal_name Escherichia coli DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 28-May-1999 ACCESSIONS A27744 REFERENCE A27744 !$#authors Ishiguro, N.; Sato, G. !$#journal J. Bacteriol. (1988) 170:1902-1906 !$#title Nucleotide sequence of insertion sequence IS3411, which !1flanks the citrate utilization determinant of transposon !1Tn3411. !$#cross-references MUID:88169522; PMID:2832386 !$#accession A27744 !'##molecule_type DNA !'##residues 1-240 ##label ISH !'##cross-references GB:M19532; NID:g154871; PIDN:AAA88669.1; !1PID:g1197003 !'##experimental_source strain K12 GENETICS !$#mobile_element insertion sequence IS CLASSIFICATION #superfamily transposase IS3 KEYWORDS DNA binding; DNA replication SUMMARY #length 240 #molecular-weight 28289 #checksum 2224 SEQUENCE /// ENTRY TQECI3 #type complete TITLE probable transposase - Escherichia coli (strain K-12) insertion sequence IS3 ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 30-Jan-1998 #text_change 01-Mar-2002 ACCESSIONS C64756; C64786; D64765; H64844; H64975; A23050 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64756 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-288 ##label BLAT !'##cross-references GB:AE000137; GB:U00096; NID:g2367108; !1PIDN:AAC73402.1; PID:g1786490; UWGP:b0299 !'##experimental_source strain K-12, substrain MG1655 !$#accession C64786 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-288 ##label BLA5 !'##cross-references GB:AE000160; GB:U00096; NID:g1786751; !1PIDN:AAC73642.1; PID:g1786753; UWGP:b0541 !'##experimental_source strain K-12, substrain MG1655 !'##genetics T52 !$#accession D64765 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-288 ##label BLA2 !'##cross-references GB:AE000144; GB:U00096; NID:g1786568; !1PIDN:AAC73475.1; PID:g1786570; UWGP:b0372 !'##experimental_source strain K-12, substrain MG1655 !'##genetics T51 !$#accession H64844 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-288 ##label BLA3 !'##cross-references GB:AE000204; GB:U00096; NID:g1787256; !1PIDN:AAC74111.1; PID:g1787263; UWGP:b1026 !'##experimental_source strain K-12, substrain MG1655 !'##genetics T53 !$#accession H64975 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-288 ##label BLA4 !'##cross-references GB:AE000298; GB:U00096; NID:g1788395; !1PIDN:AAC75150.1; PID:g1788405; UWGP:b2089 !'##experimental_source strain K-12, substrain MG1655 !'##genetics T54 REFERENCE A23050 !$#authors Timmerman, K.P.; Tu, C.P.D. !$#journal Nucleic Acids Res. (1985) 13:2127-2139 !$#title Complete sequence of IS3. !$#cross-references MUID:85215604; PMID:2987844 !$#accession A23050 !'##molecule_type DNA !'##residues 1-141,'P',143-288 ##label TIM GENETICS T52 !$#gene tra5_2 !$#mobile_element insertion sequence IS3 GENETICS T51 !$#gene tra5_1 !$#mobile_element insertion sequence IS3 GENETICS T53 !$#gene tra5_3 !$#mobile_element insertion sequence IS3 GENETICS T54 !$#gene tra5_4 !$#mobile_element insertion sequence IS3 CLASSIFICATION #superfamily transposase IS3 KEYWORDS DNA binding; DNA replication SUMMARY #length 288 #molecular-weight 33540 #checksum 6657 SEQUENCE /// ENTRY TQECT #type complete TITLE transposase - Escherichia coli transposon Tn3 ORGANISM #formal_name Escherichia coli DATE 30-Jun-1980 #sequence_revision 15-Oct-1982 #text_change 22-Nov-1996 ACCESSIONS A03538 REFERENCE A90784 !$#authors Heffron, F.; McCarthy, B.J.; Ohtsubo, H.; Ohtsubo, E. !$#journal Cell (1979) 18:1153-1163 !$#title DNA sequence analysis of the transposon Tn3: three genes and !1three sites involved in transposition of Tn3. !$#cross-references MUID:80090058; PMID:391406 !$#accession A03538 !'##molecule_type DNA !'##residues 1-1015 ##label HEF COMMENT This protein is required for transposition of transposon !1Tn3. GENETICS !$#start_codon GTG CLASSIFICATION #superfamily transposase Tn3 KEYWORDS DNA binding; DNA replication SUMMARY #length 1015 #molecular-weight 114529 #checksum 3750 SEQUENCE /// ENTRY TQEC93 #type complete TITLE transposase - Escherichia coli transposon Tn903 ORGANISM #formal_name Escherichia coli DATE 22-May-1981 #sequence_revision 15-Oct-1982 #text_change 16-Jul-1999 ACCESSIONS A92864; A93868; I77546; A03539 REFERENCE A92864 !$#authors Oka, A.; Sugisaki, H.; Takanami, M. !$#journal J. Mol. Biol. (1981) 147:217-226 !$#title Nucleotide sequence of the kanamycin resistance transposon !1Tn903. !$#cross-references MUID:82033200; PMID:6270337 !$#accession A92864 !'##molecule_type DNA !'##residues 1-307 ##label OKA !'##cross-references GB:V00359; GB:J01839; NID:g43025; PIDN:CAA23657.1; !1PID:g581236 REFERENCE A93868 !$#authors Grindley, N.D.F.; Joyce, C.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1980) 77:7176-7180 !$#title Genetic and DNA sequence analysis of the kanamycin !1resistance transposon Tn903. !$#cross-references MUID:81175113; PMID:6261245 !$#accession A93868 !'##molecule_type DNA !'##residues 1-307 ##label GRI !'##cross-references GB:V00621; GB:J01840; NID:g43762; PIDN:CAA23897.1; !1PID:g581283 REFERENCE I57738 !$#authors Mollet, B.; Iida, S.; Arber, W. !$#journal Mol. Gen. Genet. (1985) 199:534-536 !$#title An active variant of the prokaryotic transposable element !1IS903 carries an amber stop codon in the middle of an open !1reading frame. !$#cross-references MUID:85295477; PMID:2993802 !$#accession I77546 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-11,'P',13-23,'I',25-30,'E',32-81,'S',83-104,'V',106-109, !1'P',111-155,'N',157-190,'A',192-307 ##label RES !'##cross-references EMBL:X02527; NID:g43694; PIDN:CAA26362.1; !1PID:g581272 COMMENT This protein is required for transposition of transposon !1Tn903. GENETICS !$#start_codon GTG CLASSIFICATION #superfamily transposase Tn903 KEYWORDS DNA binding; DNA replication SUMMARY #length 307 #molecular-weight 34933 #checksum 2244 SEQUENCE /// ENTRY TQEC21 #type complete TITLE transposase - Escherichia coli transposon Tn21 ORGANISM #formal_name Escherichia coli DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS A26673 REFERENCE A26673 !$#authors Ward, E.; Grinsted, J. !$#journal Nucleic Acids Res. (1987) 15:1799-1806 !$#title The nucleotide sequence of the tnpA gene of Tn21. !$#cross-references MUID:87146495; PMID:3029727 !$#accession A26673 !'##molecule_type DNA !'##residues 1-988 ##label WAR !'##cross-references GB:X04891; NID:g48213; PIDN:CAA28579.1; PID:g48215 COMMENT This protein is responsible for transposition of transposon !1Tn21. GENETICS !$#gene tnpA CLASSIFICATION #superfamily transposase Tn21 KEYWORDS DNA binding; DNA replication SUMMARY #length 988 #molecular-weight 110823 #checksum 5152 SEQUENCE /// ENTRY TQEC26 #type complete TITLE transposase - Escherichia coli transposon Tn3926 ORGANISM #formal_name Escherichia coli DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jul-1999 ACCESSIONS S03285 REFERENCE S03285 !$#authors Turner, A.K.; Grinsted, J. !$#journal Nucleic Acids Res. (1989) 17:1757 !$#title DNA sequence of the transposase gene of the class II !1transposon, Tn3926. !$#cross-references MUID:89160328; PMID:2537961 !$#accession S03285 !'##molecule_type DNA !'##residues 1-990 ##label TUR !'##cross-references EMBL:X14236; NID:g48216; PIDN:CAA32453.1; !1PID:g48217 GENETICS !$#gene tnpA CLASSIFICATION #superfamily transposase Tn21 KEYWORDS DNA binding; DNA replication SUMMARY #length 990 #molecular-weight 111073 #checksum 9390 SEQUENCE /// ENTRY TQECT5 #type complete TITLE transposase - Escherichia coli transposon Tn2501 ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 31-Mar-1992 #text_change 16-Jul-1999 ACCESSIONS S06302; A27758 REFERENCE S06302 !$#authors Turner, A.K.; Grinsted, J. !$#journal Nucleic Acids Res. (1987) 15:10049 !$#title DNA sequence of the transposase gene of the new category of !1class II transposon, Tn2501. !$#cross-references MUID:88096496; PMID:2827105 !$#accession S06302 !'##molecule_type DNA !'##residues 1-994 ##label TUR !'##cross-references EMBL:Y00502; NID:g43098; PIDN:CAA68555.1; !1PID:g43099 REFERENCE A91859 !$#authors Michiels, T.; Cornelis, G.; Ellis, K.; Grinsted, J. !$#journal J. Bacteriol. (1987) 169:624-631 !$#title Tn2501, a component of the lactose transposon Tn951, is an !1example of a new category of class II transposable elements. !$#cross-references MUID:87109049; PMID:3027041 !$#accession A27758 !'##molecule_type DNA !'##residues 1-204 ##label MIC !'##cross-references GB:M15197; NID:g154866; PIDN:AAA27425.1; !1PID:g552039 !'##note the authors translated the codon TCA for residue 179 as Tyr GENETICS !$#gene tnpA CLASSIFICATION #superfamily transposase Tn21 KEYWORDS DNA binding; DNA replication SUMMARY #length 994 #molecular-weight 112749 #checksum 2362 SEQUENCE /// ENTRY TQBS30 #type complete TITLE transposase - Bacillus thuringiensis transposon Tn4430 ORGANISM #formal_name Bacillus thuringiensis DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 21-Jul-2000 ACCESSIONS S00570; S02241 REFERENCE S00554 !$#authors Mahillon, J.; Lereclus, D. !$#journal EMBO J. (1988) 7:1515-1526 !$#title Structural and functional analysis of Tn4430: identification !1of an integrase-like protein involved in the !1co-integrate-resolution process. !$#cross-references MUID:88312602; PMID:2842151 !$#accession S00570 !'##molecule_type DNA !'##residues 1-987 ##label MAH1 !'##cross-references EMBL:X07651; NID:g40347; PIDN:CAA30492.1; !1PID:g40349 REFERENCE S02047 !$#authors Mahillon, J.; Seurinck, J. !$#journal Nucleic Acids Res. (1988) 16:11827-11828 !$#title Complete nucleotide sequence of pG12, a Bacillus !1thuringiensis plasmid containing Tn4430. !$#cross-references MUID:89098342; PMID:3211758 !$#accession S02241 !'##status translation not shown !'##molecule_type DNA !'##residues 1-987 ##label MAH2 !'##cross-references EMBL:X13481; NID:g3171732; PIDN:CAA31833.1; !1PID:g40318 GENETICS !$#gene tnpA CLASSIFICATION #superfamily transposase Tn21 KEYWORDS DNA binding; DNA replication SUMMARY #length 987 #molecular-weight 113644 #checksum 8042 SEQUENCE /// ENTRY TQZMCA #type complete TITLE probable transposase - maize transposon Ac9 ORGANISM #formal_name Zea mays #common_name maize DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 20-Feb-1998 ACCESSIONS A03540; S18636 REFERENCE A90848 !$#authors Pohlman, R.F.; Fedoroff, N.V.; Messing, J. !$#journal Cell (1984) 37:635-643 !$#title The nucleotide sequence of the maize controlling element !1activator. !$#cross-references MUID:84205699; PMID:6327080 !$#accession A03540 !'##molecule_type DNA !'##residues 1-839 ##label POH !'##cross-references GB:K01964; NID:g168402 REFERENCE S18636 !$#authors Feldmar, S.; Kunze, R. !$#journal EMBO J. (1991) 10:4003-4010 !$#title The ORFa protein, the putative transposase of maize !1transposable element Ac, has a basic DNA binding domain. !$#cross-references MUID:92097517; PMID:1661668 !$#accession S18636 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type DNA !'##residues 103-184 ##label FEL COMMENT This protein is coded by the transposable maize controlling !1element "Activator," which is able to activate chromosome !1breakage at a specific location; it may be the structural !1gene for a trans-acting function required for transposition. CLASSIFICATION #superfamily hypothetical transposase Ac9 KEYWORDS DNA binding; DNA replication FEATURE !$136-145 #region DNA binding #status experimental SUMMARY #length 839 #molecular-weight 97068 #checksum 5547 SEQUENCE /// ENTRY RPECT #type complete TITLE transposase repressor - Escherichia coli ORGANISM #formal_name Escherichia coli DATE 30-Jun-1980 #sequence_revision 30-Jun-1980 #text_change 16-Jul-1999 ACCESSIONS A03541 REFERENCE A90784 !$#authors Heffron, F.; McCarthy, B.J.; Ohtsubo, H.; Ohtsubo, E. !$#journal Cell (1979) 18:1153-1163 !$#title DNA sequence analysis of the transposon Tn3: three genes and !1three sites involved in transposition of Tn3. !$#cross-references MUID:80090058; PMID:391406 !$#accession A03541 !'##molecule_type DNA !'##residues 1-185 ##label HEF !'##cross-references GB:V00613; GB:J01832; NID:g43710; PIDN:CAA23885.1; !1PID:g43712 !'##note this protein regulates the transcription of the transposase !1gene coded by transposon Tn3 CLASSIFICATION #superfamily transposase repressor KEYWORDS DNA binding SUMMARY #length 185 #molecular-weight 20617 #checksum 3181 SEQUENCE /// ENTRY RPECTG #type complete TITLE resolvase - Escherichia coli transposon gamma-delta ORGANISM #formal_name Escherichia coli DATE 17-Dec-1982 #sequence_revision 05-Apr-1983 #text_change 16-Jul-1999 ACCESSIONS A03542; I76576; I83239; S21900 REFERENCE A03542 !$#authors Reed, R.R.; Shibuya, G.I.; Steitz, J.A. !$#journal Nature (1982) 300:381-383 !$#title Nucleotide sequence of gammadelta resolvase gene and !1demonstration that its gene product acts as a repressor of !1transcription. !$#cross-references MUID:83062876; PMID:6292730 !$#accession A03542 !'##molecule_type DNA !'##residues 1-183 ##label REE !'##note the authors translated the codon CTC for residue 23 as Glu !'##note this protein catalyzes the site-specific recombination of the !1transposon and also regulates its frequency of !1transposition; its sequence is 79% identical with that of !1Tn3 transposase repressor REFERENCE I56963 !$#authors Maekawa, T.; Ohtsubo, E. !$#journal Jpn. J. Genet. (1994) 69:269-285 !$#title Identification of the region that determines the specificity !1of binding of the transposases encoded by Tn3 and gamma !1delta to the terminal inverted repeat sequences. !$#cross-references MUID:94361836; PMID:8080658 !$#accession I76576 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-183 ##label RES !'##cross-references GB:D16449; NID:g303565; PIDN:BAA03915.1; !1PID:g303567 REFERENCE I60218 !$#authors Broom, J.E.; Hill, D.F.; Hughes, G.; Jones, W.A.; !1McNaughton, J.C.; Stockwell, P.A.; Petersen, G.B. !$#journal DNA Seq. (1995) 5:185-189 !$#title Sequence of a transposon identified as Tn1000 (gamma delta). !$#cross-references MUID:95337425; PMID:7612932 !$#accession I83239 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-183 ##label RE2 !'##cross-references EMBL:X60200; NID:g295867; PIDN:CAA42759.1; !1PID:g43088 GENETICS !$#gene tnpR CLASSIFICATION #superfamily transposase repressor KEYWORDS DNA binding; DNA integration; DNA recombination; !1transcription regulation SUMMARY #length 183 #molecular-weight 20362 #checksum 1660 SEQUENCE /// ENTRY RPEC21 #type complete TITLE resolvase - Escherichia coli transposons ORGANISM #formal_name Escherichia coli DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 24-Sep-1999 ACCESSIONS A03543; S09631 REFERENCE A90871 !$#authors Hyde, D.R.; Tu, C.P.T. !$#journal Cell (1985) 42:629-638 !$#title tnpM: a novel regulatory gene that enhances Tn21 !1transposition and suppresses cointegrate resolution. !$#cross-references MUID:85282620; PMID:2992807 !$#accession A03543 !'##molecule_type DNA !'##residues 1-186 ##label HYD !'##cross-references GB:AF071413; NID:g3513654; PIDN:AAC33925.1; !1PID:g3513675 !'##experimental_source transposon Tn21 REFERENCE S07292 !$#authors Diver, W.P.; Grinsted, J.; Fritzinger, D.C.; Brown, N.L.; !1Altenbuchner, J.; Rogowsky, P.; Schmitt, R. !$#journal Mol. Gen. Genet. (1983) 191:189-193 !$#title DNA sequences of and complementation by the tnpR genes of !1Tn21, Tn501 and Tn1721. !$#cross-references MUID:84013495; PMID:6312271 !$#accession S09631 !'##status preliminary !'##molecule_type DNA !'##residues 1-186 ##label DIV !'##cross-references EMBL:X01298; NID:g43707; PIDN:CAA25626.1; !1PID:g43708 !'##experimental_source transposon Tn1721 GENETICS !$#gene tpnR !$#mobile_element transposons FUNCTION !$#description protein catalyzes the resolution (a site-specific !1recombination) of the cointegrated replicon to yield the !1final transposition products; the cointegrated replicon is !1an obligatory intermediate of the transposition process of !1Tn21, a transposon encoding resistance to sulfonamide, !1streptomycin, and mercuric ion CLASSIFICATION #superfamily transposase repressor KEYWORDS DNA binding; site-specific integration; transposition SUMMARY #length 186 #molecular-weight 21329 #checksum 4513 SEQUENCE /// ENTRY JWEBT #type complete TITLE DNA-invertase - Salmonella sp. ALTERNATE_NAMES gene hin protein ORGANISM #formal_name Salmonella sp. DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 11-Sep-1998 ACCESSIONS A03544 REFERENCE A03544 !$#authors Zieg, J.; Simon, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1980) 77:4196-4200 !$#title Analysis of the nucleotide sequence of an invertible !1controlling element. !$#cross-references MUID:81054741; PMID:6933466 !$#accession A03544 !'##molecule_type DNA !'##residues 1-190 ##label ZIE !'##note a DNA fragment of approximately 900 base pairs, adjacent to the !1H2 gene, which specifies the synthesis of one of the !1flagellar antigens, can exist in either orientation with !1respect to the H2 structural gene; the orientation of the !1inversion region controls expression of the H2 gene; the hin !1gene occupies about two-thirds of the inversion region; the !1hin protein is required for the inversion of the H2 !1controlling region GENETICS !$#gene hin CLASSIFICATION #superfamily transposase repressor KEYWORDS DNA binding; DNA integration; DNA recombination FEATURE !$162-181 #region helix-turn-helix motif\ !$10 #active_site Ser #status predicted SUMMARY #length 190 #molecular-weight 21356 #checksum 6927 SEQUENCE /// ENTRY JWEC #type complete TITLE DNA-invertase - Escherichia coli (strain K-12) ALTERNATE_NAMES gene pin protein ORGANISM #formal_name Escherichia coli DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 01-Mar-2002 ACCESSIONS A03545; S07958; C64861 REFERENCE A93968 !$#authors Plasterk, R.H.A.; Brinkman, A.; van de Putte, P. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:5355-5358 !$#title DNA inversions in the chromosome of Escherichia coli and in !1bacteriophage Mu: relationship to other site-specific !1recombination systems. !$#cross-references MUID:83299972; PMID:6310572 !$#accession A03545 !'##molecule_type DNA !'##residues 1-184 ##label PLA !'##cross-references GB:K00676; NID:g147273; PIDN:AAA24391.1; !1PID:g147274 !'##experimental_source K-12, strain HB101 REFERENCE S07185 !$#authors Plasterk, R.H.A.; van de Putte, P. !$#journal EMBO J. (1985) 4:237-242 !$#title The invertible P-DNA segment in the chromosome of !1Escherichia coli. !$#cross-references MUID:85257443; PMID:3894006 !$#accession S07958 !'##status translation not shown !'##molecule_type DNA !'##residues 1-77,'T',179-184 ##label PL2 !'##cross-references EMBL:X01805; NID:g42407; PIDN:CAA25948.1; !1PID:g42411 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64861 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-184 ##label BLAT !'##cross-references GB:AE000214; GB:U00096; NID:g1787382; !1PIDN:AAC74242.1; PID:g1787404; UWGP:b1158 !'##experimental_source strain K-12, substrain MG1655 COMMENT This protein catalyzes the inversion of an 1800-bp E. coli !1DNA fragment, the P region, which can exist in either !1orientation. The function of the inversion is not yet clear. GENETICS !$#gene pin CLASSIFICATION #superfamily transposase repressor KEYWORDS DNA binding; DNA integration; DNA recombination FEATURE !$161-180 #region helix-turn-helix motif\ !$9 #active_site Ser #status predicted SUMMARY #length 184 #molecular-weight 20573 #checksum 2059 SEQUENCE /// ENTRY JWBPP7 #type complete TITLE DNA-invertase - phage P7 ORGANISM #formal_name phage P7 DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jul-1999 ACCESSIONS S03663 REFERENCE S03663 !$#authors Ritthaler, W.; Kamp, D. !$#journal Nucleic Acids Res. (1988) 16:6246 !$#title DNA sequence of the site-specific recombination function cin !1of phage P7. !$#cross-references MUID:88289386; PMID:3399403 !$#accession S03663 !'##molecule_type DNA !'##residues 1-186 ##label RIT !'##cross-references EMBL:X07724; NID:g15482; PIDN:CAA30554.1; !1PID:g15483 GENETICS !$#gene cin CLASSIFICATION #superfamily transposase repressor KEYWORDS DNA binding; DNA integration; DNA recombination FEATURE !$161-180 #region helix-turn-helix motif\ !$9 #active_site Ser #status predicted SUMMARY #length 186 #molecular-weight 21246 #checksum 6474 SEQUENCE /// ENTRY JWBPU #type complete TITLE DNA-invertase - phage Mu ALTERNATE_NAMES gene gin protein ORGANISM #formal_name phage Mu DATE 19-Feb-1984 #sequence_revision 11-Sep-1998 #text_change 17-Nov-2000 ACCESSIONS S02705; A21135; A03546; S02455 REFERENCE S02705 !$#authors Klippel, A.; Cloppenborg, K.; Kahmann, R. !$#journal EMBO J. (1988) 7:3983-3989 !$#title Isolation and characterization of unusual gin mutants. !$#cross-references MUID:89091149; PMID:2974801 !$#accession S02705 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-193 ##label KLI REFERENCE A21135 !$#authors Plasterk, R.H.A.; Vollering, M.; Brinkman, A.; van de Putte, !1P. !$#journal Cell (1984) 36:189-196 !$#title Analysis of the methylation-regulated Mu mom transcript. !$#cross-references MUID:84106815; PMID:6229339 !$#accession A21135 !'##molecule_type DNA !'##residues 166-193 ##label PLA !'##cross-references GB:V01463; NID:g15804; PIDN:CAA24708.1; PID:g809115 REFERENCE A93968 !$#authors Plasterk, R.H.A.; Brinkman, A.; van de Putte, P. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:5355-5358 !$#title DNA inversions in the chromosome of Escherichia coli and in !1bacteriophage Mu: relationship to other site-specific !1recombination systems. !$#cross-references MUID:83299972; PMID:6310572 !$#accession A03546 !'##molecule_type DNA !'##residues 2-47,'D',49-98,'P',100-193 ##label PLW !'##note initiator Met not shown REFERENCE S02455 !$#authors Klippel, A.; Mertens, G.; Patschinsky, T.; Kahmann, R. !$#journal EMBO J. (1988) 7:1229-1237 !$#title The DNA invertase Gin of phage Mu: formation of a covalent !1complex with DNA via a phosphoserine at amino acid position !19. !$#cross-references MUID:88296429; PMID:3042382 !$#accession S02455 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-16 ##label KL2 GENETICS !$#gene gin CLASSIFICATION #superfamily transposase repressor KEYWORDS DNA binding; DNA integration; DNA recombination FEATURE !$161-180 #region helix-turn-helix motif\ !$9 #active_site Ser #status predicted SUMMARY #length 193 #molecular-weight 21740 #checksum 2789 SEQUENCE /// ENTRY RPECR5 #type complete TITLE resolvase - Escherichia coli transposon Tn2501 ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 28-May-1999 ACCESSIONS B27758 REFERENCE A91859 !$#authors Michiels, T.; Cornelis, G.; Ellis, K.; Grinsted, J. !$#journal J. Bacteriol. (1987) 169:624-631 !$#title Tn2501, a component of the lactose transposon Tn951, is an !1example of a new category of class II transposable elements. !$#cross-references MUID:87109049; PMID:3027041 !$#accession B27758 !'##molecule_type DNA !'##residues 1-194 ##label MIC !'##cross-references GB:M15197; NID:g154866; PIDN:AAA27426.1; !1PID:g154868 COMMENT Tn2501 is a cryptic class II transposon found as part of the !1lactose transposon Tn951. GENETICS !$#gene tnpR CLASSIFICATION #superfamily transposase repressor KEYWORDS DNA binding; site-specific integration; transposition SUMMARY #length 194 #molecular-weight 21420 #checksum 5930 SEQUENCE /// ENTRY PDBYA #type complete TITLE site-specific recombinase FLP - yeast (Saccharomyces cerevisiae) plasmid 2-mu ALTERNATE_NAMES hypothetical protein A CONTAINS DNA ligase (EC 6.5.1.-); DNA lyase (EC 4.2.99.-) ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Oct-1980 #sequence_revision 11-Apr-1997 #text_change 16-Jul-1999 ACCESSIONS A04502; A93695; A23905; A40544; A36099 REFERENCE A93232 !$#authors Hartley, J.L.; Donelson, J.E. !$#journal Nature (1980) 286:860-864 !$#title Nucleotide sequence of the yeast plasmid. !$#cross-references MUID:81012161; PMID:6251374 !$#accession A04502 !'##molecule_type DNA !'##residues 1-4,'G',6-423 ##label HAR !'##cross-references GB:J01347; NID:g172190; PIDN:AAB59340.1; !1PID:g172191 !'##experimental_source strain A364A D5 REFERENCE A93695 !$#authors Hindley, J.; Phear, G.A. !$#journal Nucleic Acids Res. (1979) 7:361-375 !$#title Sequence of 1019 nucleotides encompassing one of the !1inverted repeats from the yeast 2 mu plasmid. !$#cross-references MUID:80034481; PMID:386282 !$#accession A93695 !'##molecule_type DNA !'##residues 250-423 ##label HIN !'##note the nucleotide sequence determined by these authors has missing !1residues in the codons for residues 303 and 405 above. Each !1of these gaps shifts the reading frame so that residues !1303-423 are different from that shown; the codon !1corresponding to 347-Ile is AAG, which would translate into !1Val REFERENCE A23905 !$#authors Babineau, D.; Vetter, D.; Andrews, B.J.; Gronostajski, R.M.; !1Proteau, G.A.; Beatty, L.G.; Sadowski, P.D. !$#journal J. Biol. Chem. (1985) 260:12313-12319 !$#title The FLP protein of the 2-micron plasmid of yeast. !$#cross-references MUID:86008307; PMID:2995370 !$#accession A23905 !'##molecule_type protein !'##residues 'X',3,'X',5-7,'X',9,'X',11,'X' ##label BAB !'##note the identity of 5-Asp (not 5-Gly) was confirmed by both DNA and !1peptide sequencing; this corrects the residue from reference !1A93232 !'##note protein purified after expression in Escherichia coli REFERENCE A40544 !$#authors Pan, H.; Clary, D.; Sadowski, P.D. !$#journal J. Biol. Chem. (1991) 266:11347-11354 !$#title Identification of the DNA-binding domain of the FLP !1recombinase. !$#cross-references MUID:91250454; PMID:2040639 !$#accession A40544 !'##molecule_type protein !'##residues 2-7;124-129;148-153 ##label PAN REFERENCE A36099 !$#authors Evans, B.R.; Chen, J.W.; Parsons, R.L.; Bauer, T.K.; Teplow, !1D.B.; Jayaram, M. !$#journal J. Biol. Chem. (1990) 265:18504-18510 !$#title Identification of the active site tyrosine of Flp !1recombinase. Possible relevance of its location to the !1mechanism of recombination. !$#cross-references MUID:91009349; PMID:2211714 !$#accession A36099 !'##molecule_type protein !'##residues 1-4,'G',6-21;128-137;271-292;340-364;370-383 ##label EVA !'##note position 5 was assigned as Gly; lack of detection was blamed on !1high background from glycine in buffers, but see reference !1A23905 COMMENT This recombinase requires only monovalent or divalent !1cations for activity. It does not require ATP. GENETICS !$#genome plasmid 2-mu FUNCTION !$#description promotes recombination across two 599-base pair inverted !1repeats of the plasmid known as 2-micron circle DNA CLASSIFICATION #superfamily site-specific recombinase FLP KEYWORDS carbon-oxygen lyase; DNA binding; DNA recombination; ligase FEATURE !$343 #active_site Tyr (covalent DNA-binding) #status !8experimental SUMMARY #length 423 #molecular-weight 48677 #checksum 3455 SEQUENCE /// ENTRY RSBSTI #type complete TITLE site-specific recombinase tnpI - Bacillus thuringiensis transposon Tn4430 ALTERNATE_NAMES integrase homolog; resolvase ORGANISM #formal_name Bacillus thuringiensis DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 21-Jul-2000 ACCESSIONS S00554; S02240 REFERENCE S00554 !$#authors Mahillon, J.; Lereclus, D. !$#journal EMBO J. (1988) 7:1515-1526 !$#title Structural and functional analysis of Tn4430: identification !1of an integrase-like protein involved in the !1co-integrate-resolution process. !$#cross-references MUID:88312602; PMID:2842151 !$#accession S00554 !'##molecule_type DNA !'##residues 1-284 ##label MAH1 !'##cross-references EMBL:X07651; NID:g40347; PIDN:CAA30491.1; !1PID:g40348 REFERENCE S02047 !$#authors Mahillon, J.; Seurinck, J. !$#journal Nucleic Acids Res. (1988) 16:11827-11828 !$#title Complete nucleotide sequence of pG12, a Bacillus !1thuringiensis plasmid containing Tn4430. !$#cross-references MUID:89098342; PMID:3211758 !$#accession S02240 !'##status translation not shown !'##molecule_type DNA !'##residues 1-284 ##label MAH2 !'##cross-references EMBL:X13481; NID:g3171732; PIDN:CAA31832.1; !1PID:g40317 GENETICS !$#gene tnpI CLASSIFICATION #superfamily site-specific recombinase tnpI SUMMARY #length 284 #molecular-weight 32820 #checksum 4993 SEQUENCE /// ENTRY RSBSMT #type complete TITLE probable site-specific recombinase - Bacillus thuringiensis subsp. thuringiensis plasmid pGI2 ORGANISM #formal_name Bacillus thuringiensis subsp. thuringiensis DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 28-Jul-2000 ACCESSIONS S02050 REFERENCE S02047 !$#authors Mahillon, J.; Seurinck, J. !$#journal Nucleic Acids Res. (1988) 16:11827-11828 !$#title Complete nucleotide sequence of pG12, a Bacillus !1thuringiensis plasmid containing Tn4430. !$#cross-references MUID:89098342; PMID:3211758 !$#accession S02050 !'##status translation not shown !'##molecule_type DNA !'##residues 1-445 ##label MAH !'##cross-references EMBL:X13481; NID:g3171732; PIDN:CAA31835.1; !1PID:g40322 GENETICS !$#genome plasmid CLASSIFICATION #superfamily probable site-specific recombinase KEYWORDS DNA binding SUMMARY #length 445 #molecular-weight 52816 #checksum 4920 SEQUENCE /// ENTRY QQSA4E #type complete TITLE hypothetical protein C-403 - Staphylococcus aureus plasmid pE194 ORGANISM #formal_name Staphylococcus aureus DATE 18-Aug-1982 #sequence_revision 05-Apr-1983 #text_change 30-Sep-1993 ACCESSIONS A04486 REFERENCE A91790 !$#authors Horinouchi, S.; Weisblum, B. !$#journal J. Bacteriol. (1982) 150:804-814 !$#title Nucleotide sequence and functional map of pE194, a plasmid !1that specifies inducible resistance to macrolide, !1lincosamide, and streptogramin type B antibiotics. !$#cross-references MUID:82167187; PMID:6279574 !$#accession A04486 !'##molecule_type DNA !'##residues 1-403 ##label HOR GENETICS !$#genome plasmid CLASSIFICATION #superfamily probable site-specific recombinase SUMMARY #length 403 #molecular-weight 47883 #checksum 387 SEQUENCE /// ENTRY RQECA #type complete TITLE recombination protein recA [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES recombinase A ORGANISM #formal_name Escherichia coli DATE 31-Jul-1980 #sequence_revision 14-Nov-1997 #text_change 01-Mar-2002 ACCESSIONS G65049; A93847; A93846; S11931; S63525; S69129; S63979; !1A03548 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65049 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-353 ##label BLAT !'##cross-references GB:AE000354; GB:U00096; NID:g2367149; !1PIDN:AAC75741.1; PID:g1789051; UWGP:b2699 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A93847 !$#authors Horii, T.; Ogawa, T.; Ogawa, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1980) 77:313-317 !$#title Organization of the recA gene of Escherichia coli. !$#cross-references MUID:80145618; PMID:6244554 !$#accession A93847 !'##molecule_type DNA !'##residues 2-353 ##label HOR !'##cross-references GB:V00328; NID:g42672; PIDN:CAA23618.1; PID:g42673 REFERENCE A93846 !$#authors Sancar, A.; Stachelek, C.; Konigsberg, W.; Rupp, W.D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1980) 77:2611-2615 !$#title Sequences of the recA gene and protein. !$#cross-references MUID:80234673; PMID:6930655 !$#accession A93846 !'##molecule_type DNA !'##residues 2-353 ##label SAN !'##cross-references GB:V00328; GB:J01672; NID:g42672; PIDN:CAA23618.1; !1PID:g42673 REFERENCE S11931 !$#authors Zhao, X.J.; McEntee, K. !$#journal Mol. Gen. Genet. (1990) 222:369-376 !$#title DNA sequence analysis of the recA genes from Proteus !1vulgaris, Erwinia carotovora, Shigella flexneri and !1Escherichia coli B/r. !$#cross-references MUID:91109725; PMID:2274037 !$#accession S11931 !'##molecule_type DNA !'##residues 2-353 ##label ZHA !'##cross-references GB:X55552; NID:g42678 !'##note this ORF is not annotated in GenBank entry ECRECAGEN, release !1109.0 REFERENCE S63525 !$#authors Morimatsu, K.; Horii, T. !$#journal Eur. J. Biochem. (1995) 234:695-705 !$#title DNA-binding surface of RecA protein. Photochemical !1cross-linking of the first DNA binding site on RecA !1filament. !$#cross-references MUID:96096752; PMID:8529655 !$#accession S63525 !'##status preliminary !'##molecule_type protein !'##residues 65-69;90-97;179-184;200-207;258-265;304-311;323-331 ##label !1MOR1 REFERENCE S69129 !$#authors Morimatsu, K.; Horii, T. !$#journal Eur. J. Biochem. (1995) 228:772-778 !$#title The DNA-binding site of the RecA protein. Photochemical !1cross-linking of Tyr103 to single-stranded DNA. !$#cross-references MUID:95255284; PMID:7737176 !$#accession S69129 !'##status preliminary !'##molecule_type protein !'##residues 90-108,180-184 ##label MOR2 REFERENCE S63979 !$#authors Gardner, R.V.; Voloshin, O.N.; Camerini-Otero, R.D. !$#journal Eur. J. Biochem. (1995) 233:419-425 !$#title The identification of the single-stranded DNA-binding domain !1of the Escherichia coli RecA protein. !$#cross-references MUID:96067680; PMID:7588783 !$#accession S63979 !'##molecule_type protein !'##residues 'XX',187-190,192-194 ##label GAR REFERENCE A67277 !$#authors Yu, X.; Egelman, E.H. !$#submission submitted to the Brookhaven Protein Data Bank, December 1996 !$#cross-references PDB:2REC !$#contents annotation; X-ray crystallography, 2.3 angstroms, residues !14-157;166-195;211-329 REFERENCE A67455 !$#authors Aihara, H.; Ito, Y.; Kurumizaka, H.; Terada, T.; Yokoyama, !1S.; Shibata, T. !$#submission submitted to the Brookhaven Protein Data Bank, January 1997 !$#cross-references PDB:1AA3 !$#contents annotation; conformation by (1)H- and (15)N-NMR, residues !1269-331 GENETICS !$#gene recA !$#map_position 58 min FUNCTION !$#description plays an essential role in homologous recombination, in !1induction of the SOS response, and in initiation of stable !1DNA replication CLASSIFICATION #superfamily recombination protein recA KEYWORDS ATP; DNA binding; DNA recombination; DNA repair; nucleotide !1binding; P-loop; SOS response FEATURE !$67-74 #region nucleotide-binding motif A (P-loop)\ !$141-146 #region nucleotide-binding motif B\ !$73 #binding_site ATP (Lys) #status predicted SUMMARY #length 353 #molecular-weight 37973 #checksum 9068 SEQUENCE /// ENTRY RQBCAT #type complete TITLE recombination protein recA - Thiobacillus ferrooxidans ALTERNATE_NAMES recombinase A ORGANISM #formal_name Thiobacillus ferrooxidans DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 19-Jan-2001 ACCESSIONS JU0051 REFERENCE JU0051 !$#authors Ramesar, R.S.; Abratt, V.; Woods, D.R.; Rawlings, D.E. !$#journal Gene (1989) 78:1-8 !$#title Nucleotide sequence and expression of a cloned Thiobacillus !1ferrooxidans recA gene in Escherichia coli. !$#cross-references MUID:89357486; PMID:2504646 !$#accession JU0051 !'##molecule_type DNA !'##residues 1-346 ##label RAM !'##cross-references GB:M26933 GENETICS !$#gene recA FUNCTION !$#description plays an essential role in homologous recombination, in !1induction of the SOS response, and in initiation of stable !1DNA replication CLASSIFICATION #superfamily recombination protein recA KEYWORDS ATP; DNA binding; DNA recombination; DNA repair; nucleotide !1binding; P-loop; SOS response FEATURE !$66-73 #region nucleotide-binding motif A (P-loop)\ !$140-145 #region nucleotide-binding motif B\ !$72 #binding_site ATP (Lys) #status predicted SUMMARY #length 346 #molecular-weight 37096 #checksum 5119 SEQUENCE /// ENTRY RQPSAA #type complete TITLE RecA protein PA3617 [imported] - Pseudomonas aeruginosa (strain PAO1) ALTERNATE_NAMES recombinase A ORGANISM #formal_name Pseudomonas aeruginosa DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 19-Jan-2001 ACCESSIONS S06265; S10458; A49854; JN0304; G83192 REFERENCE S06265 !$#authors Sano, Y.; Kageyama, M. !$#journal Mol. Gen. Genet. (1987) 208:412-419 !$#title The sequence and function of the recA gene and its protein !1in Pseudomonas aeruginosa PAO. !$#cross-references MUID:88038334; PMID:2823059 !$#accession S06265 !'##molecule_type DNA !'##residues 1-346 ##label SAN1 !'##cross-references GB:X05691; NID:g45413; PIDN:CAA29173.1; PID:g45414 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE S10458 !$#authors Zaitsev, E.N.; Krjukov, V.M.; Kuzmin, N.P.; Alekseev, A.A.; !1Lanzov, V.A. !$#submission submitted to the EMBL Data Library, March 1990 !$#description Restriction polymorphism and nucleotide sequence !1substitutions in the recA gene of Pseudomonas aeruginosa !1strains. !$#accession S10458 !'##molecule_type DNA !'##residues 1-346 ##label ZAI !'##cross-references EMBL:X52261; NID:g45383; PIDN:CAA36504.1; !1PID:g45384 REFERENCE A49854 !$#authors Sano, Y. !$#journal J. Bacteriol. (1993) 175:2451-2454 !$#title Role of the recA-related gene adjacent to the recA gene in !1Pseudomonas aeruginosa. !$#cross-references MUID:93224470; PMID:8468303 !$#accession A49854 !'##status preliminary !'##molecule_type DNA !'##residues 313-346 ##label SAN2 !'##cross-references GB:D13090; NID:g286185 !'##note sequence extracted from NCBI backbone (NCBIN:129317, !1NCBIP:129318) REFERENCE JN0304 !$#authors Kryukov, V.M.; Zaitsev, E.N.; Kouzmin, N.P.; Bayev, A.A. !$#journal Bioorg. Khim. (1990) 16:1177-1182 !$#title Structure of the recA gene from Pseudomonas aeruginosa. !$#cross-references MUID:91182156; PMID:2127886 !$#accession JN0304 !'##molecule_type DNA !'##residues 1-332,'L',334-346 ##label KRY !'##cross-references GB:X52261; NID:g45383; PIDN:CAA36504.1; PID:g45384 !'##experimental_source strain PAM 7 !'##note the authors translated the codon CTG for residue 333 as Val REFERENCE A82950 !$#authors Stover, C.K.; Pham, X.Q.; Erwin, A.L.; Mizoguchi, S.D.; !1Warrener, P.; Hickey, M.J.; Brinkman, F.S.L.; Hufnagle, !1W.O.; Kowalik, D.J.; Lagrou, M.; Garber, R.L.; Goltry, L.; !1Tolentino, E.; Westbrook-Wadman, S.; Yuan, Y.; Brody, L.L.; !1Coulter, S.N.; Folger, K.R.; Kas, A.; Larbig, K.; Lim, R.M.; !1Smith, K.A.; Spencer, D.H.; Wong, G.K.S.; Wu, Z.; Paulsen, !1I.T.; Reizer, J.; Saier, M.H.; Hancock, R.E.W.; Lory, S.; !1Olson, M.V. !$#journal Nature (2000) 406:959-964 !$#title Complete genome sequence of Pseudomonas aeruginosa PA01, an !1opportunistic pathogen. !$#cross-references MUID:20437337; PMID:10984043 !$#accession G83192 !'##status preliminary !'##molecule_type DNA !'##residues 1-346 ##label STO !'##cross-references GB:AE004782; GB:AE004091; NID:g9949772; !1PIDN:AAG07005.1; GSPDB:GN00131; PASP:PA3617 !'##experimental_source strain PAO1 GENETICS !$#gene recA; PA3617 FUNCTION !$#description plays an essential role in homologous recombination, in !1induction of the SOS response, and in initiation of stable !1DNA replication CLASSIFICATION #superfamily recombination protein recA KEYWORDS ATP; DNA binding; DNA recombination; DNA repair; nucleotide !1binding; P-loop; SOS response FEATURE !$65-72 #region nucleotide-binding motif A (P-loop)\ !$139-144 #region nucleotide-binding motif B\ !$71 #binding_site ATP (Lys) #status predicted SUMMARY #length 346 #molecular-weight 36879 #checksum 5795 SEQUENCE /// ENTRY RQPSAC #type complete TITLE recombination protein recA - Pseudomonas cepacia ALTERNATE_NAMES recombinase A ORGANISM #formal_name Pseudomonas cepacia DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 19-Jan-2001 ACCESSIONS JQ0459 REFERENCE JQ0459 !$#authors Nakazawa, T.; Kimoto, M.; Abe, M. !$#submission submitted to JIPID, May 1990 !$#accession JQ0459 !'##molecule_type DNA !'##residues 1-347 ##label NAK GENETICS !$#gene recA FUNCTION !$#description plays an essential role in homologous recombination, in !1induction of the SOS response, and in initiation of stable !1DNA replication CLASSIFICATION #superfamily recombination protein recA KEYWORDS ATP; DNA binding; DNA recombination; DNA repair; nucleotide !1binding; P-loop; SOS response FEATURE !$66-73 #region nucleotide-binding motif A (P-loop)\ !$140-145 #region nucleotide-binding motif B\ !$72 #binding_site ATP (Lys) #status predicted SUMMARY #length 347 #molecular-weight 37257 #checksum 5673 SEQUENCE /// ENTRY RQEBPM #type complete TITLE recombination protein recA - Proteus mirabilis ALTERNATE_NAMES recombinase A ORGANISM #formal_name Proteus mirabilis DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 19-Jan-2001 ACCESSIONS S04606 REFERENCE S04606 !$#authors Akaboshi, E.; Yip, M.L.R.; Howard-Flanders, P. !$#journal Nucleic Acids Res. (1989) 17:4390 !$#title Nucleotide sequence of the recA gene of Proteus mirabilis. !$#cross-references MUID:89296502; PMID:2544862 !$#accession S04606 !'##molecule_type DNA !'##residues 1-355 ##label AKA !'##cross-references GB:X14870; NID:g45631; PIDN:CAA33015.1; PID:g45632 GENETICS !$#gene recA FUNCTION !$#description plays an essential role in homologous recombination, in !1induction of the SOS response, and in initiation of stable !1DNA replication CLASSIFICATION #superfamily recombination protein recA KEYWORDS ATP; DNA binding; DNA recombination; DNA repair; nucleotide !1binding; P-loop; SOS response FEATURE !$67-74 #region nucleotide-binding motif A (P-loop)\ !$141-146 #region nucleotide-binding motif B\ !$73 #binding_site ATP (Lys) #status predicted SUMMARY #length 355 #molecular-weight 38219 #checksum 901 SEQUENCE /// ENTRY RQAIA #type complete TITLE recombination protein recA - Anabaena variabilis ALTERNATE_NAMES recombinase A ORGANISM #formal_name Anabaena variabilis DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 19-Jan-2001 ACCESSIONS A33606 REFERENCE A33606 !$#authors Owttrim, G.W.; Coleman, J.R. !$#journal J. Bacteriol. (1989) 171:5713-5719 !$#title Regulation of expression and nucleotide sequence of the !1Anabaena variabilis recA gene. !$#cross-references MUID:90008816; PMID:2507530 !$#accession A33606 !'##molecule_type DNA !'##residues 1-358 ##label OWT !'##cross-references GB:M29680; NID:g142091; PIDN:AAA22031.1; !1PID:g142092 GENETICS !$#gene recA FUNCTION !$#description plays an essential role in homologous recombination, in !1induction of the SOS response, and in initiation of stable !1DNA replication CLASSIFICATION #superfamily recombination protein recA KEYWORDS ATP; DNA binding; DNA recombination; DNA repair; nucleotide !1binding; P-loop; SOS response FEATURE !$69-76 #region nucleotide-binding motif A (P-loop)\ !$143-148 #region nucleotide-binding motif B\ !$75 #binding_site ATP (Lys) #status predicted SUMMARY #length 358 #molecular-weight 38406 #checksum 5492 SEQUENCE /// ENTRY RQYCA #type complete TITLE recombination protein recA - Synechococcus sp. (strain PCC 7002) ALTERNATE_NAMES recombinase A ORGANISM #formal_name Synechococcus sp. DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 19-Jan-2001 ACCESSIONS A35120; A25930 REFERENCE A35120 !$#authors Murphy, R.C.; Gasparich, G.E.; Bryant, D.A.; Porter, R.D. !$#journal J. Bacteriol. (1990) 172:967-976 !$#title Nucleotide sequence and further characterization of the !1Synechococcus sp. strain PCC 7002 recA gene: complementation !1of a cyanobacterial recA mutation by the Escherichia coli !1recA gene. !$#cross-references MUID:90130334; PMID:2105307 !$#accession A35120 !'##molecule_type DNA !'##residues 1-348 ##label MU1 !'##cross-references GB:M29495; NID:g154601; PIDN:AAA88636.1; !1PID:g154602 REFERENCE A25930 !$#authors Murphy, R.C.; Bryant, D.A.; Porter, R.D.; Tandeau de Marsac, !1N. !$#journal J. Bacteriol. (1987) 169:2739-2747 !$#title Molecular cloning and characterization of the recA gene from !1the cyanobacterium Synechococcus sp. strain PCC 7002. !$#cross-references MUID:87222203; PMID:3108239 !$#accession A25930 !'##molecule_type DNA !'##residues 'I',199-237,'AK',240,'IC',244-280,'SRNKQCHYA',290-296 !1##label MU2 !'##cross-references GB:M16491; NID:g154599; PIDN:AAA27363.1; !1PID:g154600 GENETICS !$#gene recA FUNCTION !$#description plays an essential role in homologous recombination, in !1induction of the SOS response, and in initiation of stable !1DNA replication CLASSIFICATION #superfamily recombination protein recA KEYWORDS ATP; DNA binding; DNA recombination; DNA repair; nucleotide !1binding; P-loop; SOS response FEATURE !$69-76 #region nucleotide-binding motif A (P-loop)\ !$143-148 #region nucleotide-binding motif B\ !$75 #binding_site ATP (Lys) #status predicted SUMMARY #length 348 #molecular-weight 37243 #checksum 4880 SEQUENCE /// ENTRY RQBSEE #type complete TITLE recombination protein recA - Bacillus subtilis ALTERNATE_NAMES multifunctional protein involved in homologous recombination A; recombinase A ORGANISM #formal_name Bacillus subtilis DATE 30-Jun-1992 #sequence_revision 02-Jul-1998 #text_change 19-Jan-2001 ACCESSIONS S10370; S14684; F69690 REFERENCE S10370 !$#authors Stranathan, M.C.; Yasbin, R.E. !$#submission submitted to the EMBL Data Library, March 1990 !$#description The nucleotide sequence of the recE gene of Bacillus !1subtilis. !$#accession S10370 !'##molecule_type DNA !'##residues 1-347 ##label STR2 !'##cross-references EMBL:X52132; NID:g40069; PIDN:CAA36377.1; !1PID:g40070 REFERENCE S14684 !$#authors Stranathan, M.C.; Bayles, K.W.; Yasbin, R.E. !$#journal Nucleic Acids Res. (1990) 18:4249 !$#title The nucleotide sequence of the recE(+) gene of Bacillus !1subtilis. !$#cross-references MUID:90332424; PMID:2115993 !$#accession S14684 !'##molecule_type DNA !'##residues 1-84,'GGQA',88-347 ##label STR1 !'##cross-references EMBL:X52132 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69690 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-347 ##label KUN !'##cross-references GB:Z99112; GB:AL009126; NID:g2633902; !1PIDN:CAB13567.1; PID:g2634066 !'##experimental_source strain 168 GENETICS !$#gene recA CLASSIFICATION #superfamily recombination protein recA KEYWORDS ATP; DNA binding; DNA recombination; DNA repair; nucleotide !1binding; P-loop; SOS response FEATURE !$64-71 #region nucleotide-binding motif A (P-loop)\ !$137-142 #region nucleotide-binding motif B\ !$70 #binding_site ATP (Lys) #status predicted SUMMARY #length 347 #molecular-weight 38090 #checksum 2140 SEQUENCE /// ENTRY A60989 #type complete TITLE recombination protein recA - Legionella pneumophila ALTERNATE_NAMES recombinase A ORGANISM #formal_name Legionella pneumophila DATE 31-Dec-1993 #sequence_revision 27-Jun-1994 #text_change 19-Jan-2001 ACCESSIONS A60989 REFERENCE A60989 !$#authors Zhao, X.; Dreyfus, L.A. !$#journal FEMS Microbiol. Lett. (1990) 70:227-232 !$#title Expression and nucleotide sequence analysis of the !1Legionella pneumophila recA gene. !$#accession A60989 !'##molecule_type DNA !'##residues 1-348 ##label ZHA !'##cross-references GB:X55453; NID:g48779; PIDN:CAA39097.1; PID:g48780 GENETICS !$#gene recA FUNCTION !$#description plays an essential role in homologous recombination, in !1induction of the SOS response, and in initiation of stable !1DNA replication CLASSIFICATION #superfamily recombination protein recA KEYWORDS ATP; DNA binding; DNA recombination; DNA repair; nucleotide !1binding; P-loop; SOS response FEATURE !$66-73 #region nucleotide-binding motif A (P-loop)\ !$140-145 #region nucleotide-binding motif B\ !$72 #binding_site ATP (Lys) #status predicted SUMMARY #length 348 #molecular-weight 37934 #checksum 1920 SEQUENCE /// ENTRY RQECN #type complete TITLE recN protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS C65040; A27852 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65040 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-553 ##label BLAT !'##cross-references GB:AE000347; GB:U00096; NID:g2367142; !1PIDN:AAC75665.1; PID:g1788969; UWGP:b2616 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A27852 !$#authors Rostas, K.; Morton, S.J.; Picksley, S.M.; Lloyd, R.G. !$#journal Nucleic Acids Res. (1987) 15:5041-5049 !$#title Nucleotide sequence and LexA regulation of the Escherichia !1coli recN gene. !$#cross-references MUID:87259985; PMID:3037486 !$#accession A27852 !'##molecule_type DNA !'##residues 1-58,'C',61-75,'R',77-425,'P',427-534,'VAVKSHVIHWRMR',548, !1'NC',551,'QRKLFSCFTVRVNSKTP' ##label ROS !'##cross-references GB:Y00357; NID:g42692; PIDN:CAA68435.1; PID:g42693 COMMENT This protein is coded by a gene in the SOS network of genes, !1the expression of which is regulated by the lexA protein. It !1may bind adenine nucleotide and may be involved in !1recombinational repair of damaged DNA. GENETICS !$#gene recN !$#map_position 59 min CLASSIFICATION #superfamily recN protein KEYWORDS DNA recombination; DNA repair SUMMARY #length 553 #molecular-weight 61370 #checksum 6908 SEQUENCE /// ENTRY H64046 #type complete TITLE recN protein homolog - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS H64046 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession H64046 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-558 ##label TIGR !'##cross-references GB:U32692; GB:L42023; NID:g1573013; !1PIDN:AAC21748.1; PID:g1573019; TIGR:HI0070 CLASSIFICATION #superfamily recN protein SUMMARY #length 558 #molecular-weight 62633 #checksum 233 SEQUENCE /// ENTRY B35128 #type complete TITLE DNA repair and genetic recombination protein recN - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS B35128; PS0054; H69690 REFERENCE A35128 !$#authors Van Hoy, B.E.; Hoch, J.A. !$#journal J. Bacteriol. (1990) 172:1306-1311 !$#title Characterization of the spoIVB and recN loci of Bacillus !1subtilis. !$#cross-references MUID:90170841; PMID:2106508 !$#accession B35128 !'##molecule_type DNA !'##residues 1-576 ##label VAN !'##cross-references GB:M30297; NID:g143400; PIDN:AAA22691.1; !1PID:g143402 REFERENCE A91616 !$#authors North, A.K.; Smith, M.C.M.; Baumberg, S. !$#journal Gene (1989) 80:29-38 !$#title Nucleotide sequence of a Bacillus subtilis arginine !1regulatory gene and homology of its product to the !1Escherichia coli arginine repressor. !$#cross-references MUID:90006783; PMID:2507400 !$#accession PS0054 !'##molecule_type DNA !'##residues 1-73,'L',75-103,'AFAVSMAS' ##label NOR !'##cross-references GB:M27869; NID:g142448; PIDN:AAA22209.1; !1PID:g551689 !'##experimental_source strain EMG50 !'##note the last eight residues of this fragment differ because of a !1frameshift error from the sequence in reference A35128 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69690 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-576 ##label KUN !'##cross-references GB:Z99116; GB:AL009126; NID:g2634723; !1PIDN:CAB14355.1; PID:g2634858 !'##experimental_source strain 168 COMMENT This protein may be involved in recombinational repair of !1damaged DNA. GENETICS !$#gene recN !$#start_codon TTG CLASSIFICATION #superfamily recN protein KEYWORDS ATP SUMMARY #length 576 #molecular-weight 64483 #checksum 8183 SEQUENCE /// ENTRY BVECRR #type complete TITLE recombination protein recR - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 01-Mar-2002 ACCESSIONS JU0106; G64777 REFERENCE A30371 !$#authors Mahdi, A.A.; Lloyd, R.G. !$#journal Nucleic Acids Res. (1989) 17:6781-6794 !$#title The recR locus of Escherichia coli K-12: molecular cloning, !1DNA sequencing and identification of the gene product. !$#cross-references MUID:89386036; PMID:2674903 !$#accession JU0106 !'##molecule_type DNA !'##residues 1-201 ##label MAH !'##cross-references GB:X15761; NID:g42696; PIDN:CAA33768.1; PID:g42697 !'##experimental_source K-12 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64777 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-201 ##label BLAT !'##cross-references GB:AE000153; GB:U00096; NID:g1786671; !1PIDN:AAC73574.1; PID:g1786678; UWGP:b0472 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene recR FUNCTION !$#description involved in recBC-independent DNA recombination and DNA !1repair CLASSIFICATION #superfamily recR protein KEYWORDS DNA recombination; DNA repair; zinc finger FEATURE !$57-72 #region zinc finger CCCC motif SUMMARY #length 201 #molecular-weight 21963 #checksum 284 SEQUENCE /// ENTRY RQECF #type complete TITLE DNA replication and repair protein recF [similarity] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 01-Mar-2002 ACCESSIONS A03547; B22168; E65172 REFERENCE A93996 !$#authors Blanar, M.A.; Sandler, S.J.; Armengod, M.E.; Ream, L.W.; !1Clark, A.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:4622-4626 !$#title Molecular analysis of the recF gene of Escherichia coli. !$#cross-references MUID:84272685; PMID:6379647 !$#accession A03547 !'##molecule_type DNA !'##residues 1-357 ##label BLA !'##cross-references GB:K02179; NID:g147537; PIDN:AAA24511.1; !1PID:g147539 !'##note the authors translated the codon GAA for residue 172 as Gln REFERENCE A22168 !$#authors Adachi, T.; Mizuuchi, K.; Menzel, R.; Gellert, M. !$#journal Nucleic Acids Res. (1984) 12:6389-6395 !$#title DNA sequence and transcription of the region upstream of the !1E. coli gyrB gene. !$#cross-references MUID:84297235; PMID:6089112 !$#accession B22168 !'##molecule_type DNA !'##residues 1-357 ##label ADA !'##cross-references GB:X04341; GB:X00870; NID:g41643; PIDN:CAA27870.1; !1PID:g41645 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65172 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-357 ##label BLAT !'##cross-references GB:AE000447; GB:U00096; NID:g2367266; !1PIDN:AAC76723.1; PID:g1790135; UWGP:b3700 !'##experimental_source strain K-12, substrain MG1655 COMMENT The recF gene is involved in DNA metabolism; it is required !1for DNA replication and normal SOS inducibility. GENETICS !$#gene recF !$#map_position 83 min CLASSIFICATION #superfamily recF protein KEYWORDS DNA binding; DNA replication; SOS response SUMMARY #length 357 #molecular-weight 40514 #checksum 8616 SEQUENCE /// ENTRY JQ0735 #type complete TITLE recF protein - Proteus mirabilis ORGANISM #formal_name Proteus mirabilis DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 01-Feb-2002 ACCESSIONS JQ0735 REFERENCE JQ0729 !$#authors Skovgaard, O. !$#journal Gene (1990) 93:27-34 !$#title Nucleotide sequence of a Proteus mirabilis DNA fragment !1homologous to the 60K-rnpA-rpmH-dnaA-dnaN-recF-gyrB region !1of Escherichia coli. !$#cross-references MUID:91033012; PMID:2172087 !$#accession JQ0735 !'##molecule_type DNA !'##residues 1-362 ##label SKO !'##cross-references GB:M58352; GB:M31295; NID:g150873; PIDN:AAA83960.1; !1PID:g150880 !'##experimental_source strain LM1509 COMMENT The recF gene is involved in DNA metabolism; it is required !1for DNA replication and normal SOS inducibility. GENETICS !$#gene recF CLASSIFICATION #superfamily recF protein KEYWORDS DNA binding; DNA replication; SOS response SUMMARY #length 362 #molecular-weight 41293 #checksum 4767 SEQUENCE /// ENTRY I64106 #type complete TITLE recF protein - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES DNA/ATP-binding protein ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Feb-2002 ACCESSIONS I64106 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession I64106 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-375 ##label TIGR !'##cross-references GB:L42023; TIGR:HI0991 GENETICS !$#gene recF !$#start_codon GTG FUNCTION !$#description involved in DNA metabolism; required for DNA replication and !1normal SOS inducibility CLASSIFICATION #superfamily recF protein KEYWORDS ATP; DNA binding; DNA replication; nucleotide binding; !1P-loop; SOS response FEATURE !$46-53 #region nucleotide-binding motif A (P-loop) SUMMARY #length 375 #molecular-weight 42894 #checksum 6626 SEQUENCE /// ENTRY S22814 #type complete TITLE recF protein - Actinobacillus pleuropneumoniae ORGANISM #formal_name Actinobacillus pleuropneumoniae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Feb-2002 ACCESSIONS S22814; S22160 REFERENCE S22813 !$#authors Loynds, B.M.; Langford, P.R.; Kroll, J.S. !$#journal Nucleic Acids Res. (1992) 20:615 !$#title recF in Actinobacillus pleuropneumoniae. !$#cross-references MUID:92158680; PMID:1741300 !$#accession S22814 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-360 ##label LOY !'##cross-references EMBL:X63626; NID:g38951; PIDN:CAA45173.1; !1PID:g38953 GENETICS !$#gene recF FUNCTION !$#description involved in DNA metabolism; required for DNA replication and !1normal SOS inducibility CLASSIFICATION #superfamily recF protein KEYWORDS DNA binding; DNA replication; SOS response SUMMARY #length 360 #molecular-weight 41243 #checksum 6305 SEQUENCE /// ENTRY JC4077 #type complete TITLE recF protein - Streptococcus pyogenes ORGANISM #formal_name Streptococcus pyogenes DATE 30-Jun-1995 #sequence_revision 16-Aug-1996 #text_change 01-Feb-2002 ACCESSIONS JC4077; PC4023 REFERENCE JC4077 !$#authors DeAngelis, P.L.; Yang, N.; Weigel, P.H. !$#journal Gene (1995) 156:89-91 !$#title Molecular cloning of the gene encoding RecF, a DNA repair !1enzyme, from Streptococcus pyogenes. !$#cross-references MUID:95255674; PMID:7737521 !$#accession JC4077 !'##molecule_type DNA !'##residues 1-368 ##label DEA !'##cross-references GB:U07342; NID:g533079; PIDN:AAA85783.1; !1PID:g533080 !$#accession PC4023 !'##molecule_type protein !'##residues 118-138;309-323 ##label DE2 COMMENT The recF gene is involved in DNA metabolism; it is required !1for DNA replication and normal SOS inducibility. GENETICS !$#gene recF CLASSIFICATION #superfamily recF protein KEYWORDS DNA binding; DNA repair; nucleotide binding; P-loop; SOS !1response FEATURE !$30-37 #region nucleotide-binding motif A (P-loop) SUMMARY #length 368 #molecular-weight 41795 #checksum 8300 SEQUENCE /// ENTRY D22930 #type complete TITLE DNA repair and genetic recombination protein recF - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 21-May-1988 #sequence_revision 16-Aug-1996 #text_change 01-Feb-2002 ACCESSIONS D22930; S66034; G69690 REFERENCE A94702 !$#authors Moriya, S.; Ogasawara, N.; Yoshikawa, H. !$#journal Nucleic Acids Res. (1985) 13:2251-2265 !$#title Structure and function of the region of the replication !1origin of the Bacillus subtilis chromosome. III. Nucleotide !1sequence of some 10,000 base pairs in the origin region. !$#cross-references MUID:85215612; PMID:2987847 !$#accession D22930 !'##molecule_type DNA !'##residues 1-370 ##label MOR !'##cross-references EMBL:X02369; NID:g40012; PIDN:CAA26220.1; !1PID:g40017 !'##note the authors' tranlation begins at Met-48; translation from !1Met-1 is justified by homology to recF from other species REFERENCE S65967 !$#authors Ogasawara, N.; Nakai, S.; Yoshikawa, H. !$#journal DNA Res. (1994) 1:1-14 !$#title Systematic sequencing of the 180 kilobase region of the !1Bacillus subtilis chromosome containing the replication !1origin. !$#cross-references MUID:96051385; PMID:7584024 !$#accession S66034 !'##status preliminary !'##molecule_type DNA !'##residues 1-370 ##label OGA !'##cross-references EMBL:D26185; NID:g467326; PIDN:BAA05240.1; !1PID:g467394 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69690 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-370 ##label KUN !'##cross-references GB:Z99104; GB:AL009126; NID:g2632267; !1PIDN:CAB11780.1; PID:g2632271 !'##experimental_source strain 168 GENETICS !$#gene recF !$#map_position 0 min !$#start_codon TTG CLASSIFICATION #superfamily recF protein KEYWORDS DNA binding; DNA repair; SOS response SUMMARY #length 370 #molecular-weight 42304 #checksum 4747 SEQUENCE /// ENTRY BVECRO #type complete TITLE DNA repair protein recO - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 01-Mar-2002 ACCESSIONS JS0116; JV0035; S43360; C42294; D65034; I54908 REFERENCE A91897 !$#authors Takiff, H.E.; Chen, S.M.; Court, D.L. !$#journal J. Bacteriol. (1989) 171:2581-2590 !$#title Genetic analysis of the rnc operon of Escherichia coli. !$#cross-references MUID:89213943; PMID:2540151 !$#accession JS0116 !'##molecule_type DNA !'##residues 1-242 ##label TAK !'##cross-references GB:M26416; NID:g499367; PIDN:AAA21842.1; !1PID:g499369 !'##note it is uncertain whether Met-1 or Met-21 is the initiator REFERENCE A91898 !$#authors Morrison, P.T.; Lovett, S.T.; Gilson, L.E.; Kolodner, R. !$#journal J. Bacteriol. (1989) 171:3641-3649 !$#title Molecular analysis of the Escherichia coli recO gene. !$#cross-references MUID:89291705; PMID:2544549 !$#accession JV0035 !'##molecule_type DNA !'##residues 1-242 ##label MOR !'##cross-references GB:M27251; NID:g147551; PIDN:AAA24515.1; !1PID:g147552 REFERENCE S43360 !$#authors Luisi-DeLuca, C.; Kolodner, R. !$#journal J. Mol. Biol. (1994) 236:124-138 !$#title Purification and characterization of the Escherichia coli !1RecO protein. Renaturation of complementary single-stranded !1DNA molecules catalyzed by the RecO protein. !$#cross-references MUID:94149708; PMID:8107098 !$#accession S43360 !'##molecule_type protein !'##residues 1-14 ##label LUI REFERENCE A42294 !$#authors Lam, H.M.; Tancula, E.; Dempsey, W.B.; Winkler, M.E. !$#journal J. Bacteriol. (1992) 174:1554-1567 !$#title Suppression of insertions in the complex pdxJ operon of !1Escherichia coli K-12 by lon and other mutations. !$#cross-references MUID:92165730; PMID:1537800 !$#accession C42294 !'##status preliminary !'##molecule_type DNA !'##residues 225-242 ##label LAM !'##cross-references GB:M74526 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65034 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-242 ##label BLAT !'##cross-references GB:AE000343; GB:U00096; NID:g2367139; !1PIDN:AAC75618.1; PID:g2367140; UWGP:b2565 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene recO !$#map_position 55 min !$#note the recO gene is part of the operon including rnc and era !1that encodes RNase III and GTP-binding protein, respectively CLASSIFICATION #superfamily recO protein SUMMARY #length 242 #molecular-weight 27390 #checksum 3563 SEQUENCE /// ENTRY MVECMT #type complete TITLE 7,8-dihydro-8-oxoguanine-triphosphatase (EC 3.6.1.-) - Escherichia coli (strain K-12) ALTERNATE_NAMES mutator mutT (AT-GC transversion) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 01-Mar-2002 ACCESSIONS A27890; S40609; A28070; S45181; C64732 REFERENCE A27890 !$#authors Akiyama, M.; Horiuchi, T.; Sekiguchi, M. !$#journal Mol. Gen. Genet. (1987) 206:9-16 !$#title Molecular cloning and nucleotide sequence of the mutT !1mutator of Escherichia coli that causes A:T to C:G !1transversion. !$#cross-references MUID:87201091; PMID:3033442 !$#accession A27890 !'##molecule_type DNA !'##residues 1-129 ##label AKI !'##cross-references GB:X55034; GB:M10429; NID:g40841; PIDN:CAA38876.1; !1PID:g40867 REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40609 !'##molecule_type DNA !'##residues 1-129 ##label YUR !'##cross-references EMBL:D10483; NID:g216434; PIDN:BAA01364.1; !1PID:g216513 REFERENCE A28070 !$#authors Bhatnagar, S.K.; Bessman, M.J. !$#journal J. Biol. Chem. (1988) 263:8953-8957 !$#title Studies on the mutator gene, mutT of Escherichia coli. !1Molecular cloning of the gene, purification of the gene !1product, and identification of a novel nucleoside !1triphosphatase. !$#cross-references MUID:88243762; PMID:3288626 !$#accession A28070 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-20 ##label BHA REFERENCE S45181 !$#authors Fujita, N. !$#submission submitted to the EMBL Data Library, January 1994 !$#accession S45181 !'##status preliminary !'##molecule_type DNA !'##residues 74-129 ##label FUJ !'##cross-references EMBL:D26562; NID:g473770; PIDN:BAA05560.1; !1PID:g473771 !'##experimental_source strain K-12, substrain W3110 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64732 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-129 ##label BLAT !'##cross-references GB:AE000119; GB:U00096; NID:g1786283; !1PIDN:AAC73210.1; PID:g1786288; UWGP:b0099 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene mutT !$#map_position 3 min FUNCTION !$#description mutT specifically degrades 8-oxo-dGTP to 8-oxo-dGMP !$#note involved in GO system responsible for removing an !1oxidatively damaged form of guanine (7, !18-dihydro-8-oxoguanine) from DNA and the nucleotide pool; !18-oxo-dGTP is inserted opposite to dA and dC residues of !1template DNA with almost equal efficiency thus leading to !1A.T to G.C transversions CLASSIFICATION #superfamily mutator mutT; mutT domain homology KEYWORDS DNA repair; DNA replication; hydrolase; magnesium; monomer FEATURE !$33-67 #domain mutT domain homology #label MUTT SUMMARY #length 129 #molecular-weight 14927 #checksum 7404 SEQUENCE /// ENTRY MVECMH #type complete TITLE mutator mutH - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Sep-1988 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS H65065; A27506 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65065 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-229 ##label BLAT !'##cross-references GB:AE000367; GB:U00096; NID:g1789195; !1PIDN:AAC75870.1; PID:g1789196; UWGP:b2831 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A27506 !$#authors Grafstrom, R.H.; Hoess, R.H. !$#journal Nucleic Acids Res. (1987) 15:3073-3084 !$#title Nucleotide sequence of the Escherichia coli mutH gene. !$#cross-references MUID:87174827; PMID:3031619 !$#accession A27506 !'##molecule_type DNA !'##residues 1-82,'L',84-129,'RL',132-135,'A',137-229 ##label GRA !'##cross-references GB:Y00113; NID:g42064; PIDN:CAA68292.1; PID:g42065 !'##note the authors translated the codon CTG for residue 83 as Val COMMENT Two temperature-sensitive mutants have also been isolated !1and sequenced. GENETICS !$#gene mutH !$#map_position 61 min CLASSIFICATION #superfamily mutator mutH SUMMARY #length 229 #molecular-weight 25527 #checksum 4579 SEQUENCE /// ENTRY RMECI #type complete TITLE replication termination factor dnaT - Escherichia coli (strain K-12) ALTERNATE_NAMES primosomal protein i ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS S56589; B28484; D65251; A25124 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56589 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-179 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97261.1; !1PID:g537205 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A92600 !$#authors Nakayama, N.; Bond, M.W.; Miyajima, A.; Kobori, J.; Arai, K. !$#journal J. Biol. Chem. (1987) 262:10475-10480 !$#title Structure of Escherichia coli dnaC. Identification of a !1cysteine residue possibly involved in association with dnaB !1protein. !$#cross-references MUID:87280100; PMID:3301836 !$#accession B28484 !'##molecule_type DNA !'##residues 108-179 ##label NAK REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65251 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-179 ##label BLAT !'##cross-references GB:AE000507; GB:U00096; NID:g2367380; !1PIDN:AAC77318.1; PID:g1790824; UWGP:b4362 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A94085 !$#authors Masai, H.; Bond, M.W.; Arai, K.I. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:1256-1260 !$#title Cloning of the Escherichia coli gene for primosomal protein !1i: the relationship to dnaT, essential for chromosomal DNA !1replication. !$#cross-references MUID:86149284; PMID:3006041 !$#accession A25124 !'##molecule_type DNA !'##residues 1-133,'L',135-179 ##label MAS !'##cross-references GB:J04030; GB:J02785; GB:M13005; NID:g145788 !'##note the authors translated the codon CTC for residue 134 as Val COMMENT This protein is required for primosome-dependent normal DNA !1replication; it is also involved in inducing stable DNA !1replication during SOS response. GENETICS !$#gene dnaT !$#map_position 99 min CLASSIFICATION #superfamily primosomal protein i KEYWORDS DNA replication SUMMARY #length 179 #molecular-weight 19455 #checksum 7236 SEQUENCE /// ENTRY Q4ECFR #type complete TITLE primosomal replication protein n - Escherichia coli (strain K-12) ALTERNATE_NAMES priB protein ORGANISM #formal_name Escherichia coli DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 01-Mar-2002 ACCESSIONS A30281; PQ0204; S56426; D65231 REFERENCE A30281 !$#authors Schnier, J.; Kitakawa, M.; Isono, K. !$#journal Mol. Gen. Genet. (1986) 204:126-132 !$#title The nucleotide sequence of an Escherichia coli chromosomal !1region containing the genes for ribosomal proteins S6, S18, !1L9 and an open reading frame. !$#cross-references MUID:86310297; PMID:3528756 !$#accession A30281 !'##molecule_type DNA !'##residues 1-104 ##label SCH !'##cross-references GB:X04022; NID:g42844; PIDN:CAA27653.1; PID:g42846 REFERENCE PQ0204 !$#authors Zavitz, K.H.; DiGate, R.J.; Marians, K.J. !$#journal J. Biol. Chem. (1991) 266:13988-13995 !$#title The priB and priC replication proteins of Escherichia coli. !1Genes, DNA sequence, overexpression, and purification. !$#cross-references MUID:91310687; PMID:1856227 !$#accession PQ0204 !'##molecule_type protein !'##residues 2-26,'X',28 ##label ZAV !'##experimental_source strain HMS83 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56426 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-104 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97097.1; !1PID:g537042 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65231 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-104 ##label BLAT !'##cross-references GB:AE000491; GB:U00096; NID:g2367357; !1PIDN:AAC77158.1; PID:g1790645; UWGP:b4201 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene priB !$#map_position 95.5 min FUNCTION !$#description plays a role in the in vitro assembly of the primosome CLASSIFICATION #superfamily primosomal protein n FEATURE !$2-104 #product primosomal protein n #status experimental !8#label MAT SUMMARY #length 104 #molecular-weight 11442 #checksum 952 SEQUENCE /// ENTRY A54809 #type complete TITLE disease resistance protein RPS2 - Arabidopsis thaliana ALTERNATE_NAMES protein F20B18.200 ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 20-Apr-2000 ACCESSIONS A54809; A54811; T04264 REFERENCE A54809 !$#authors Mindrinos, M.; Katagiri, F.; Yu, G.L.; Ausubel, F.M. !$#journal Cell (1994) 78:1089-1099 !$#title The Arabidopsis thaliana disease resistance gene RPS2 !1encodes a protein containing a nucleotide-binding site and !1leucine-rich repeats. !$#cross-references MUID:95007758; PMID:7923358 !$#accession A54809 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-909 ##label MIN !'##cross-references GB:U12860; NID:g549978; PIDN:AAA50236.1; !1PID:g549979 REFERENCE A54811 !$#authors Bent, A.F.; Kunkel, B.N.; Dahlbeck, D.; Brown, K.L.; !1Schmidt, R.; Giraudat, J.; Leung, J.; Staskawicz, B.J. !$#journal Science (1994) 265:1856-1860 !$#title RPS2 of Arabidopsis thaliana: a leucine-rich repeat class of !1plant disease resistance genes. !$#cross-references MUID:94377978; PMID:8091210 !$#accession A54811 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA; mRNA !'##residues 1-909 ##label BEN !'##cross-references GB:U14158; NID:g548085; PIDN:AAA21874.1; !1PID:g548086 REFERENCE Z15263 !$#authors Bevan, M.; Rose, M.; Hempel, S.; Entian, K.D.; Hoheisel, J.; !1Mewes, H.W.; Mayer, K.F.X.; Schueller, C. !$#submission submitted to the Protein Sequence Database, March 1999 !$#accession T04264 !'##molecule_type DNA !'##residues 1-909 ##label BEV !'##cross-references EMBL:AL049483 !'##experimental_source cultivar Columbia; BAC clone F20B18 GENETICS !$#gene RPS2 !$#map_position 4 !$#note F20B18.200 CLASSIFICATION #superfamily disease resistance protein RPS2; leucine-rich !1alpha-2-glycoprotein repeat homology KEYWORDS leucine zipper; membrane protein; nucleotide binding SUMMARY #length 909 #molecular-weight 104640 #checksum 8865 SEQUENCE /// ENTRY RMEC14 #type complete TITLE primosomal operon 14K protein - Escherichia coli (strain K-12) ALTERNATE_NAMES P14 protein ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS S56590; E65251; A31983 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56590 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-108 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97262.1; !1PID:g537206 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65251 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-108 ##label BLAT !'##cross-references GB:AE000507; GB:U00096; NID:g2367380; !1PIDN:AAC77319.1; PID:g1790825; UWGP:b4363 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A31983 !$#authors Masai, H.; Arai, K. !$#journal J. Biol. Chem. (1988) 263:15083-15093 !$#title Operon structure of dnaT and dnaC genes essential for normal !1and stable DNA replication of Escherichia coli chromosome. !$#cross-references MUID:89008392; PMID:2844800 !$#accession A31983 !'##molecule_type DNA !'##residues 1-104,'PLAYKIASLKHTDERQPPLLRVLL' ##label MAS !'##cross-references GB:J04030; GB:J02785; GB:M13005; NID:g145788; !1PIDN:AAA23698.1; PID:g145789 COMMENT This may be a membrane-associated protein. GENETICS !$#gene yjjB !$#map_position 99 min CLASSIFICATION #superfamily primosomal operon 14K protein KEYWORDS transmembrane protein SUMMARY #length 108 #molecular-weight 11867 #checksum 1163 SEQUENCE /// ENTRY RMEC18 #type complete TITLE primosomal operon 17.5K protein (mdob-dnac intergenic region) - Escherichia coli (strain K-12) ALTERNATE_NAMES P18 protein ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS S56587; B65251; B31983 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56587 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-165 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97259.1; !1PID:g537203 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65251 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-165 ##label BLAT !'##cross-references GB:AE000507; GB:U00096; NID:g2367380; !1PIDN:AAC77316.1; PID:g1790822; UWGP:b4360 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A31983 !$#authors Masai, H.; Arai, K. !$#journal J. Biol. Chem. (1988) 263:15083-15093 !$#title Operon structure of dnaT and dnaC genes essential for normal !1and stable DNA replication of Escherichia coli chromosome. !$#cross-references MUID:89008392; PMID:2844800 !$#accession B31983 !'##molecule_type DNA !'##residues 1-74,'KS',77-165 ##label MAS !'##cross-references GB:J04030; GB:J02785; GB:M13005; NID:g145788; !1PIDN:AAA23701.1; PID:g145792 COMMENT This may be a membrane-associated protein. GENETICS !$#gene yjjA !$#map_position 99 min CLASSIFICATION #superfamily primosomal operon 18K protein SUMMARY #length 165 #molecular-weight 17484 #checksum 9893 SEQUENCE /// ENTRY ZWECC #type complete TITLE umuC protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 04-Dec-1986 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS E64864; A03550; B23157 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64864 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-422 ##label BLAT !'##cross-references GB:AE000216; GB:U00096; NID:g1787417; !1PIDN:AAC74268.1; PID:g1787432; UWGP:b1184 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A03550 !$#authors Kitagawa, Y.; Akaboshi, E.; Shinagawa, H.; Horii, T.; Ogawa, !1H.; Kato, T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:4336-4340 !$#title Structural analysis of the umu operon required for inducible !1mutagenesis in Escherichia coli. !$#cross-references MUID:85242679; PMID:2989817 !$#accession A03550 !'##molecule_type DNA !'##residues 1-151,'E',153-422 ##label KIT !'##cross-references GB:M10107; NID:g148124; PIDN:AAA24729.1; !1PID:g148126 !'##note the authors translated the codon GAG for residue 152 as Ala REFERENCE A23157 !$#authors Perry, K.L.; Elledge, S.J.; Mitchell, B.B.; Marsh, L.; !1Walker, G.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:4331-4335 !$#title umuDC and mucAB operons whose products are required for UV !1light- and chemical-induced mutagenesis: UmuD, MucA and LexA !1proteins share homology. !$#cross-references MUID:85242678; PMID:2989816 !$#accession B23157 !'##molecule_type DNA !'##residues 1-422 ##label PRY !'##cross-references GB:M13387; NID:g148127; PIDN:AAA98074.1; !1PID:g148129 GENETICS !$#gene umuC !$#map_position 26 min FUNCTION !$#description essential for induced and SOS mutagenesis in E. coli; !1controlled by recA and lexA gene products; acts in concert !1with umuD', recA and DNA polymerase III to facilitate the !1process of translesion synthesis, which results in the !1introduction of mutations !$#note is one of two proteins encoded by umu operon; intracellular !1levels of umuD and umuC proteins are kept to a minimum by !1lon serine protease CLASSIFICATION #superfamily umuC protein KEYWORDS DNA repair; induced mutagenesis; SOS mutagenesis SUMMARY #length 422 #molecular-weight 47679 #checksum 3145 SEQUENCE /// ENTRY ZWECBP #type complete TITLE mucB protein - Escherichia coli plasmid pKM101 ORGANISM #formal_name Escherichia coli DATE 28-Dec-1987 #sequence_revision 31-Dec-1996 #text_change 16-Jun-2000 ACCESSIONS C23157; JQ0452 REFERENCE A23157 !$#authors Perry, K.L.; Elledge, S.J.; Mitchell, B.B.; Marsh, L.; !1Walker, G.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:4331-4335 !$#title umuDC and mucAB operons whose products are required for UV !1light- and chemical-induced mutagenesis: UmuD, MucA and LexA !1proteins share homology. !$#cross-references MUID:85242678; PMID:2989816 !$#accession C23157 !'##molecule_type DNA !'##residues 1-420 ##label PER !'##cross-references GB:D90147; NID:g216826; PIDN:BAA14176.1; !1PID:g216828 REFERENCE JQ0451 !$#authors Tanooka, H. !$#submission submitted to JIPID, May 1990 !$#contents muc364 !$#accession JQ0452 !'##molecule_type DNA !'##residues 1-420 ##label TAN GENETICS !$#gene mucA !$#genome plasmid pKM101 FUNCTION !$#description essential for induced and SOS mutagenesis in E. coli; !1controlled by recA and lexA gene products; results in the !1introduction of mutations !$#note is one of two proteins encoded by mucAB operon, which is the !1plasmid-borne analog of the E. coli umuDC operon CLASSIFICATION #superfamily umuC protein KEYWORDS DNA repair; induced mutagenesis; SOS mutagenesis SUMMARY #length 420 #molecular-weight 46361 #checksum 711 SEQUENCE /// ENTRY G69965 #type complete TITLE ATP/GTP-binding protein homolog yqjW - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS G69965 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69965 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-412 ##label KUN !'##cross-references GB:Z99116; GB:AL009126; NID:g2634723; !1PIDN:CAB14303.1; PID:g2634806 !'##experimental_source strain 168 GENETICS !$#gene yqjW CLASSIFICATION #superfamily umuC protein SUMMARY #length 412 #molecular-weight 45944 #checksum 4821 SEQUENCE /// ENTRY H69963 #type complete TITLE DNA-damage repair protein homolog yqjH - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS H69963 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69963 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-414 ##label KUN !'##cross-references GB:Z99116; GB:AL009126; NID:g2634723; !1PIDN:CAB14319.1; PID:g2634822 !'##experimental_source strain 168 GENETICS !$#gene yqjH CLASSIFICATION #superfamily umuC protein SUMMARY #length 414 #molecular-weight 47020 #checksum 7750 SEQUENCE /// ENTRY H64747 #type complete TITLE DNA-damage-inducibile protein dinP - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS H64747 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64747 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-351 ##label BLAT !'##cross-references GB:AE000131; GB:U00096; NID:g1786415; !1PIDN:AAC73335.1; PID:g1786425; UWGP:b0231 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene dinP CLASSIFICATION #superfamily umuC protein SUMMARY #length 351 #molecular-weight 39516 #checksum 7271 SEQUENCE /// ENTRY ILEC #type complete TITLE lexA repressor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 29-Jul-1981 #sequence_revision 01-Sep-1981 #text_change 01-Mar-2002 ACCESSIONS A90808; A93734; S11945; B65212; A03569 REFERENCE A90808 !$#authors Horii, T.; Ogawa, T.; Ogawa, H. !$#journal Cell (1981) 23:689-697 !$#title Nucleotide sequence of the lexA gene of Escherichia coli. !$#cross-references MUID:81186269; PMID:7013987 !$#contents lexA !$#accession A90808 !'##molecule_type DNA !'##residues 1-202 ##label HOR !'##cross-references GB:J01643; GB:V00299; GB:V00300; NID:g146607; !1PIDN:AAA24067.1; PID:g146608 REFERENCE A93881 !$#authors Little, J.W.; Mount, D.W.; Yanisch-Perron, C.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:4199-4203 !$#title Purified lexA protein is a repressor of the recA and lexA !1genes. !$#cross-references MUID:82037806; PMID:7027255 !$#contents annotation; function REFERENCE A93882 !$#authors Brent, R.; Ptashne, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:4204-4208 !$#title Mechanism of action of the lexA gene product. !$#cross-references MUID:82037807; PMID:7027256 !$#contents annotation; function REFERENCE A93734 !$#authors Markham, B.E.; Little, J.W.; Mount, D.W. !$#journal Nucleic Acids Res. (1981) 9:4149-4161 !$#title Nucleotide sequence of the lexA gene of Escherichia coli !1K-12. !$#cross-references MUID:82059453; PMID:6272195 !$#contents lexA and mutant lexA3 !$#accession A93734 !'##molecule_type DNA !'##residues 1-202 ##label MAR !'##cross-references GB:J01643; GB:V00299; GB:V00300; NID:g146607; !1PIDN:AAA24067.1; PID:g146608 !'##note the lexA3 sequence differs from that shown in having 85-Asp; it !1is resistant to cleavage by the recA protein REFERENCE S11945 !$#authors Oertel-Buchheit, P.; Lamerichs, R.M.J.N.; Schnarr, M.; !1Granger-Schnarr, M. !$#journal Mol. Gen. Genet. (1990) 223:40-48 !$#title Genetic analysis of the LexA repressor: isolation and !1characterization of LexA(Def) mutant proteins. !$#cross-references MUID:91080864; PMID:2259342 !$#accession S11945 !'##status preliminary !'##molecule_type DNA !'##residues 1-93 ##label OER REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65212 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-202 ##label BLAT !'##cross-references GB:AE000477; GB:U00096; NID:g2367338; !1PIDN:AAC77013.1; PID:g1790476; UWGP:b4043 !'##experimental_source strain K-12, substrain MG1655 COMMENT This protein, encoded by the lexA gene, represses a number !1of genes involved in the response to DNA damage (SOS !1response), including recA and lexA. recA protein hydrolyzes !1the peptide bond between Ala-84 and Gly-85. GENETICS !$#gene lexA !$#map_position 92 min CLASSIFICATION #superfamily lexA repressor KEYWORDS DNA binding; repressor; transcription regulation SUMMARY #length 202 #molecular-weight 22358 #checksum 2354 SEQUENCE /// ENTRY ILEBT #type complete TITLE lexA protein - Salmonella typhimurium ALTERNATE_NAMES repressor lexA ORGANISM #formal_name Salmonella typhimurium DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS S35496; S30166; S19925 REFERENCE S35496 !$#authors Mustard, J.A.; Thliveris, A.T.; Mount, D.W. !$#journal Nucleic Acids Res. (1992) 20:1813 !$#title Sequence of the Salmonella typhimurium LT2 lexA gene and its !1regulatory region. !$#cross-references MUID:92253398; PMID:1579481 !$#accession S35496 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-202 ##label MUS !'##cross-references EMBL:M83220; NID:g154163; PIDN:AAA27157.1; !1PID:g552020; EMBL:X63562; NID:g47767; PID:g47768 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1March 1992 REFERENCE S30163 !$#authors Garriga, X.; Calero, S.; Barbe, J. !$#journal Mol. Gen. Genet. (1992) 236:125-134 !$#title Nucleotide sequence analysis and comparison of the lexA !1genes from Salmonella typhimurium, Erwinia carotovora, !1Pseudomonas aeruginosa and Pseudomonas putida. !$#cross-references MUID:93156677; PMID:1494343 !$#accession S30166 !'##molecule_type DNA !'##residues 1-135,'TQ',138-202 ##label GAR !'##cross-references EMBL:X63002; NID:g47765; PIDN:CAA44731.1; !1PID:g47766 GENETICS !$#gene lexA CLASSIFICATION #superfamily lexA repressor KEYWORDS DNA binding; repressor; transcription regulation SUMMARY #length 202 #molecular-weight 22291 #checksum 2383 SEQUENCE /// ENTRY ZWECD #type complete TITLE proteinase (EC 3.4.21.-) umuD - Escherichia coli (strain K-12) ALTERNATE_NAMES umuD' proprotein ORGANISM #formal_name Escherichia coli DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 01-Mar-2002 ACCESSIONS A03551; A23157; D64864 REFERENCE A03550 !$#authors Kitagawa, Y.; Akaboshi, E.; Shinagawa, H.; Horii, T.; Ogawa, !1H.; Kato, T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:4336-4340 !$#title Structural analysis of the umu operon required for inducible !1mutagenesis in Escherichia coli. !$#cross-references MUID:85242679; PMID:2989817 !$#accession A03551 !'##molecule_type DNA !'##residues 1-139 ##label KIT !'##cross-references GB:M10107; NID:g148124; PIDN:AAA24728.1; !1PID:g148125 REFERENCE A23157 !$#authors Perry, K.L.; Elledge, S.J.; Mitchell, B.B.; Marsh, L.; !1Walker, G.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:4331-4335 !$#title umuDC and mucAB operons whose products are required for UV !1light- and chemical-induced mutagenesis: UmuD, MucA and LexA !1proteins share homology. !$#cross-references MUID:85242678; PMID:2989816 !$#accession A23157 !'##molecule_type DNA !'##residues 1-139 ##label PRY !'##cross-references GB:M13387; NID:g148127; PIDN:AAA98073.1; !1PID:g148128 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64864 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-139 ##label BLAT !'##cross-references GB:AE000216; GB:U00096; NID:g1787417; !1PIDN:AAC74267.1; PID:g1787431; UWGP:b1183 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene umuD !$#map_position 26 min COMPLEX umuD/umuD homodimer; umuD'/umuD' homodimer; umuD/umuD' !1heterodimer FUNCTION !$#description essential for induced and SOS mutagenesis in E. coli; !1controlled by recA and lexA gene products; self cleavage of !1umuD to umuD' (mutagenetically active form); acts in concert !1with umuC, recA and DNA polymerase III to facilitate the !1process of translesion synthesis, which results in the !1introduction of mutations !$#note one of two proteins encoded by umu operon; intracellular !1levels of umuD and umuC proteins are kept to a minimum by !1lon serine proteinase; umuD' is removed from the cell by the !1clpXP serine protease, but only when it is in a heterodimer !1complex with umuD CLASSIFICATION #superfamily lexA repressor KEYWORDS DNA repair; heterodimer; homodimer; hydrolase; induced !1mutagenesis; serine proteinase; SOS mutagenesis FEATURE !$1-139 #product umuD protein #status predicted #label MAT1\ !$1-24 #domain propeptide #link MAT2 #status predicted !8#label PRO\ !$25-139 #product umuD' protein #status predicted #label MAT2 SUMMARY #length 139 #molecular-weight 15063 #checksum 8403 SEQUENCE /// ENTRY ZWECAP #type complete TITLE mucA protein - Escherichia coli plasmid pKM101 ORGANISM #formal_name Escherichia coli DATE 28-Dec-1987 #sequence_revision 31-Dec-1996 #text_change 28-May-1999 ACCESSIONS D23157; JQ0451 REFERENCE A23157 !$#authors Perry, K.L.; Elledge, S.J.; Mitchell, B.B.; Marsh, L.; !1Walker, G.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:4331-4335 !$#title umuDC and mucAB operons whose products are required for UV !1light- and chemical-induced mutagenesis: UmuD, MucA and LexA !1proteins share homology. !$#cross-references MUID:85242678; PMID:2989816 !$#accession D23157 !'##molecule_type DNA !'##residues 1-145 ##label PER !'##cross-references GB:M13388; NID:g150798; PIDN:AAA98277.1; !1PID:g150799 REFERENCE JQ0451 !$#authors Tanooka, H. !$#submission submitted to JIPID, May 1990 !$#contents muc364 !$#accession JQ0451 !'##molecule_type DNA !'##residues 1-12,'R',13-145 ##label TAN COMMENT This is one of the two proteins encoded by the mucAB operon, !1the plasmid-borne analog of the E. coli umuDC operon, which !1is required for induced (or SOS) mutagenesis. The expression !1of the operon is controlled by recA and lexA proteins. GENETICS !$#gene mucB !$#genome plasmid CLASSIFICATION #superfamily lexA repressor KEYWORDS induced mutagenesis; SOS mutagenesis SUMMARY #length 145 #molecular-weight 16371 #checksum 2700 SEQUENCE /// ENTRY BVECUB #type complete TITLE excinuclease ABC chain B - Escherichia coli (strain K-12) ALTERNATE_NAMES uvrB protein CONTAINS excision endonuclease ABC (EC 3.1.-.-) chain B ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 01-Mar-2002 ACCESSIONS A93613; A93612; C64814; A23765; A24939 REFERENCE A93613 !$#authors Backendorf, C.; Spaink, H.; Barbeiro, A.P.; van de Putte, P. !$#journal Nucleic Acids Res. (1986) 14:2877-2890 !$#title Structure of the uvrB gene of Escherichia coli. Homology !1with other DNA repair enzymes and characterization of the !1uvrB5 mutation. !$#cross-references MUID:86176773; PMID:3008099 !$#accession A93613 !'##molecule_type DNA !'##residues 1-673 ##label BAC !'##cross-references GB:X03722; NID:g43285; PIDN:CAA27357.1; PID:g43286 REFERENCE A93612 !$#authors Arikan, E.; Kulkarni, M.S.; Thomas, D.C.; Sancar, A. !$#journal Nucleic Acids Res. (1986) 14:2637-2650 !$#title Sequences of the E. coli uvrB gene and protein. !$#cross-references MUID:86176755; PMID:3515321 !$#accession A93612 !'##molecule_type DNA !'##residues 1-476,'R',478-673 ##label ARI !'##cross-references GB:X03678; GB:J01722; GB:J01723; GB:M24329; !1GB:V00374; GB:V00375; NID:g43283; PIDN:CAA27314.1; !1PID:g43284 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64814 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-673 ##label BLAT !'##cross-references GB:AE000180; GB:U00096; NID:g1786988; !1PIDN:AAC73866.1; PID:g1786996; UWGP:b0779 !'##experimental_source strain K-12, substrain MG1655 COMMENT uvrA, uvrB, and uvrC function together as excision nuclease. GENETICS !$#gene uvrB !$#map_position 18 min FUNCTION !$#description stimulates the ATPase activity of uvrA protein in the !1presence of UV-irradiated double-stranded DNA; enhances the !1ability of the uvrA protein to bind to UV-irradiated duplex !1DNA CLASSIFICATION #superfamily excinuclease ABC chain B KEYWORDS ATP; DNA repair; hydrolase; nucleotide binding; P-loop FEATURE !$39-46 #region nucleotide-binding motif A (P-loop)\ !$334-339 #region nucleotide-binding motif B\ !$338-341 #region DEXH motif SUMMARY #length 673 #molecular-weight 76225 #checksum 1944 SEQUENCE /// ENTRY BVECUC #type complete TITLE excinuclease ABC, chain C - Escherichia coli (strain K-12) ALTERNATE_NAMES excision nuclease ABC, chain C; uvrC protein ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 23-Jan-1998 #text_change 01-Mar-2002 ACCESSIONS F64954; A22863; C24964; I78634 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64954 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-588 ##label BLAT !'##cross-references GB:AE000284; GB:U00096; NID:g1788214; !1PIDN:AAC74980.1; PID:g1788221; UWGP:b1913 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A22863 !$#authors Sancar, G.B.; Sancar, A.; Rupp, W.D. !$#journal Nucleic Acids Res. (1984) 12:4593-4608 !$#title Sequences of the E. coli uvrC gene and protein. !$#cross-references MUID:84247323; PMID:6330676 !$#accession A22863 !'##molecule_type DNA !'##residues 1-268,'K',270-588 ##label SAN !'##cross-references GB:X03691; GB:X00189; GB:X00638; NID:g43287; !1PIDN:CAA27329.1; PID:g43290 REFERENCE A93609 !$#authors Sharma, S.; Stark, T.F.; Beattie, W.G.; Moses, R.E. !$#journal Nucleic Acids Res. (1986) 14:2301-2318 !$#title Multiple control elements for the uvrC gene unit of !1Escherichia coli. !$#cross-references MUID:86176730; PMID:3515318 !$#accession C24964 !'##molecule_type DNA !'##residues 1-96 ##label SHA !'##cross-references GB:X03691; GB:X00189; GB:X00638; NID:g43287 REFERENCE A26750 !$#authors Moolenaar, G.F.; van Sluis, C.A.; Backendorf, C.; van de !1Putte, P. !$#journal Nucleic Acids Res. (1987) 15:4273-4289 !$#title Regulation of the Escherichia coli excision repair gene !1uvrC. Overlap between the uvrC structural gene and the !1region coding for a 24kD protein. !$#cross-references MUID:87231005; PMID:3295776 !$#accession I78634 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 'MSDQFDAKAFLKTVTSQPGVYR',1-6 ##label RES !'##cross-references EMBL:X05398; NID:g43291; PIDN:CAA28983.1; !1PID:g581253 GENETICS !$#gene uvrC !$#map_position 42 min FUNCTION !$#description one of the proteins involved in DNA excision repair, a !1process to remove pyrimidine dimers from UV-damaged DNA; !1together with gene products of uvrA and uvrB, they function !1as excision nuclease CLASSIFICATION #superfamily excinuclease ABC chain C KEYWORDS DNA repair SUMMARY #length 588 #molecular-weight 65716 #checksum 1222 SEQUENCE /// ENTRY A37192 #type complete TITLE excinuclease ABC, chain C - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 07-Feb-1992 #sequence_revision 26-May-1994 #text_change 16-Jun-2000 ACCESSIONS A37192; H69729 REFERENCE A37192 !$#authors Chen, N.Y.; Zhang, J.J.; Paulus, H. !$#journal J. Gen. Microbiol. (1989) 135:2931-2940 !$#title Chromosomal location of the Bacillus subtilis aspartokinase !1II gene and nucleotide sequence of the adjacent genes !1homologous to uvrC and trx of Escherichia coli. !$#cross-references MUID:90132525; PMID:2559145 !$#accession A37192 !'##molecule_type DNA !'##residues 1-598 ##label CHE !'##cross-references GB:J03294; GB:M26384; NID:g142519; PIDN:AAA87316.1; !1PID:g142521 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69729 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-598 ##label KUN !'##cross-references GB:Z99118; GB:AL009126; NID:g2635200; !1PIDN:CAB14809.1; PID:g2635314 !'##experimental_source strain 168 COMMENT This is one of the proteins involved in DNA excision repair, !1a process to remove pyrimidine dimers from UV-damaged DNA. !1It functions together with the gene products of uvrA and !1uvrC as an excision nuclease. GENETICS !$#gene uvrC !$#map_position 70 min CLASSIFICATION #superfamily excinuclease ABC chain C KEYWORDS DNA repair SUMMARY #length 598 #molecular-weight 69458 #checksum 8485 SEQUENCE /// ENTRY E64622 #type complete TITLE excinuclease ABC chain C - Helicobacter pylori (strain 26695) ALTERNATE_NAMES uvrC protein CONTAINS excision endonuclease ABC (EC 3.1.-.-) chain C ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 12-Nov-1999 ACCESSIONS E64622 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession E64622 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-594 ##label TOM !'##cross-references GB:AE000593; GB:AE000511; NID:g2313944; !1PIDN:AAD07868.1; PID:g2313951; TIGR:HP0821 CLASSIFICATION #superfamily excinuclease ABC chain C KEYWORDS DNA repair; hydrolase SUMMARY #length 594 #molecular-weight 68679 #checksum 1694 SEQUENCE /// ENTRY S77286 #type complete TITLE excinuclease ABC chain C - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein sll0865; uvrC protein CONTAINS excision endonuclease ABC (EC 3.1.-.-) chain C ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S77286 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S77286 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-626 ##label KAN !'##cross-references EMBL:D90907; GB:AB001339; NID:g1652618; !1PIDN:BAA17620.1; PID:g1652700 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene uvrC CLASSIFICATION #superfamily excinuclease ABC chain C KEYWORDS DNA repair; hydrolase SUMMARY #length 626 #molecular-weight 71896 #checksum 9672 SEQUENCE /// ENTRY S73355 #type complete TITLE excinuclease ABC chain C - Mycoplasma pneumoniae (strain ATCC 29342) ALTERNATE_NAMES hypothetical protein C09_orf586; uvrC protein CONTAINS excision endonuclease ABC (EC 3.1.-.-) chain C ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Dec-1999 ACCESSIONS S73355 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73355 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-586 ##label HIM !'##cross-references EMBL:AE000004; GB:U00089; NID:g1673671; !1PIDN:AAB95677.1; PID:g1673677 !'##note the nucleotide sequence was submitted to the EMBL Data Libra !1November 1996 GENETICS !$#gene uvrC !$#genetic_code SGC3 !$#start_codon TTG CLASSIFICATION #superfamily excinuclease ABC chain C KEYWORDS DNA repair; hydrolase SUMMARY #length 586 #molecular-weight 67770 #checksum 6960 SEQUENCE /// ENTRY BVECSC #type complete TITLE exonuclease (EC 3.1.15.-) sbcC - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 01-Mar-2002 ACCESSIONS JS0350; A43750; S27548; E64768; S06604 REFERENCE JS0349 !$#authors Naom, I.S.; Morton, S.J.; Leach, D.R.F.; Lloyd, R.G. !$#journal Nucleic Acids Res. (1989) 17:8033-8045 !$#title Molecular organization of sbcC, a gene that affects genetic !1recombination and the viability of DNA palindromes in !1Escherichia coli K-12. !$#cross-references MUID:90045931; PMID:2530497 !$#accession JS0350 !'##molecule_type DNA !'##residues 1-1048 ##label NAO !'##cross-references GB:X15981; NID:g42912; PIDN:CAA34104.1; PID:g42914 !'##experimental_source strain K12 REFERENCE A43750 !$#authors Reeder, T.; Schleif, R. !$#journal J. Bacteriol. (1991) 173:7765-7771 !$#title Mapping, sequence, and apparent lack of function of araJ, a !1gene of the Escherichia coli arabinose regulon. !$#cross-references MUID:92078081; PMID:1744033 !$#accession A43750 !'##molecule_type DNA !'##residues 858-1048 ##label REE !'##cross-references EMBL:M64787 REFERENCE S27548 !$#authors Reeder, T.; Schleif, R. !$#submission submitted to the EMBL Data Library, May 1991 !$#description Mapping, sequence, and apparent lack of fuction of araJ, a !1gene of the Escherichia coli arabinose regulon. !$#accession S27548 !'##molecule_type DNA !'##residues 379-1048 ##label RE2 !'##cross-references EMBL:M64787 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64768 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1048 ##label BLAT !'##cross-references GB:AE000146; GB:U00096; NID:g1786596; !1PIDN:AAC73500.1; PID:g1786597; UWGP:b0397 !'##experimental_source strain K-12, substrain MG1655 COMMENT This protein interacts with long DNA palindromes and reduces !1the viability of the carrier DNA; it is also involved in !1genetic recombination and DNA repair. GENETICS !$#gene sbcC !$#map_position 9 min CLASSIFICATION #superfamily sbcC protein KEYWORDS coiled coil; DNA repair; exonuclease; hydrolase; nucleotide !1binding; P-loop FEATURE !$37-44 #region nucleotide-binding motif A (P-loop)\ !$1003-1010 #region nucleotide-binding motif A (P-loop) SUMMARY #length 1048 #molecular-weight 118720 #checksum 3454 SEQUENCE /// ENTRY BVECTD #type complete TITLE tdcABC operon transcription activator - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS D65101; JU0024; S05359 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65101 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-114 ##label BLAT !'##cross-references GB:AE000393; GB:U00096; NID:g1789499; !1PIDN:AAC76154.1; PID:g1789507; UWGP:b3119 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A93688 !$#authors Schweizer, H.P.; Datta, P. !$#journal Nucleic Acids Res. (1989) 17:3994 !$#title The complete nucleotide sequence of the tdc region of !1Escherichia coli. !$#cross-references MUID:89282418; PMID:2660107 !$#accession JU0024 !'##molecule_type DNA !'##residues 'M',17-114 ##label SCH !'##cross-references GB:X14430; NID:g43038; PIDN:CAA32591.1; PID:g581238 REFERENCE S05359 !$#authors Schweizer, H.P.; Datta, P. !$#journal Mol. Gen. Genet. (1989) 218:516-522 !$#title Identification and DNA sequence of tdcR, a positive !1regulatory gene of the tdc operon of Escherichia coli. !$#cross-references MUID:90066355; PMID:2573820 !$#accession S05359 !'##molecule_type DNA !'##residues 'M',17-114 ##label SCH2 !'##cross-references EMBL:X16445; NID:g43034; PIDN:CAA34464.1; !1PID:g581237 GENETICS !$#gene tdcR !$#map_position 67 min CLASSIFICATION #superfamily tdcABC operon transcription activator KEYWORDS DNA binding; transcription regulation SUMMARY #length 114 #molecular-weight 13574 #checksum 2575 SEQUENCE /// ENTRY BVECTC #type complete TITLE threonine-serine permease - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1992 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS A65101; A30197; JU0028 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65101 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-443 ##label BLAT !'##cross-references GB:AE000393; GB:U00096; NID:g1789499; !1PIDN:AAC76151.1; PID:g1789504; UWGP:b3116 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A30197 !$#authors Goss, T.J.; Schweizer, H.P.; Datta, P. !$#journal J. Bacteriol. (1988) 170:5352-5359 !$#title Molecular characterization of the tdc operon of Escherichia !1coli K-12. !$#cross-references MUID:89033926; PMID:3053659 !$#accession A30197 !'##molecule_type DNA !'##residues 1-69,71-430,'VC' ##label GOS !'##cross-references GB:M23638; NID:g147924; PIDN:AAA24662.1; !1PID:g147926 !'##experimental_source strain K12 REFERENCE A93688 !$#authors Schweizer, H.P.; Datta, P. !$#journal Nucleic Acids Res. (1989) 17:3994 !$#title The complete nucleotide sequence of the tdc region of !1Escherichia coli. !$#cross-references MUID:89282418; PMID:2660107 !$#accession JU0028 !'##molecule_type DNA !'##residues 1-69,71-430,'VC' ##label SCH !'##cross-references GB:X14430; NID:g43038; PIDN:CAA32594.1; PID:g43044 GENETICS !$#gene tdcC !$#map_position 67 min CLASSIFICATION #superfamily threonine-serine permease KEYWORDS transmembrane protein SUMMARY #length 443 #molecular-weight 48878 #checksum 5650 SEQUENCE /// ENTRY BVECAC #type complete TITLE racC protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 01-Mar-2002 ACCESSIONS JS0119; B64885; T09176 REFERENCE A91895 !$#authors Chu, C.C.; Templin, A.; Clark, A.J. !$#journal J. Bacteriol. (1989) 171:2101-2109 !$#title Suppression of a frameshift mutation in the recE gene of !1Escherichia coli K-12 occurs by gene fusion. !$#cross-references MUID:89197781; PMID:2649487 !$#accession JS0119 !'##molecule_type DNA !'##residues 1-91 ##label CHU !'##cross-references GB:M24905; NID:g147534; PIDN:AAA03211.1; !1PID:g147535 !'##experimental_source strain K12 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64885 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-91 ##label BLAT !'##cross-references GB:AE000233; GB:U00096; NID:g1787613; !1PIDN:AAC74433.1; PID:g1787614; UWGP:b1351 !'##experimental_source strain K-12, substrain MG1655 REFERENCE Z16603 !$#authors Aiba, H.; Baba, T.; Fujita, K.; Hayashi, K.; Inada, T.; !1Isono, K.; Itoh, T.; Kasai, H.; Kashimoto, K.; Kimura, S.; !1Kitakawa, M.; Kitagawa, M.; Makino, K.; Miki, T.; Mizobuchi, !1K.; Mori, H.; Mori, T.; Motomura, K.; Nakade, S.; Nakamura, !1Y.; Nashimoto, H.; Nishio, Y.; Oshima, T.; Saito, N.; !1Sampei, G.; Seki, Y.; Sivasundaram, S.; Tagami, H.; Takeda, !1J.; Takemoto, K.; Takeuchi, Y.; Wada, C.; Yamamoto, Y.; !1Horiuchi, T. !$#journal DNA Res. (1996) 3:363-377 !$#title A 570-kb DNA sequence of the Escherichia coli K-12 genome !1corresponding to the 28.0-40.1 min region on the linkage !1map. !$#cross-references MUID:97251357; PMID:9097039 !$#accession T09176 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-91 ##label AIB !'##cross-references EMBL:D90774; NID:g1742217; PIDN:BAA14953.1; !1PID:g1742220 GENETICS !$#gene racC !$#map_position 30 min CLASSIFICATION #superfamily racC protein SUMMARY #length 91 #molecular-weight 10016 #checksum 9865 SEQUENCE /// ENTRY BVECID #type complete TITLE lysine 6-monooxygenase (EC 1.13.12.10) iucD [validated] - Escherichia coli plasmid ColV-K30 ALTERNATE_NAMES aerobactin biosynthesis protein iucD ORGANISM #formal_name Escherichia coli DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 26-May-2000 ACCESSIONS A28665 REFERENCE A28665 !$#authors Herrero, M.; de Lorenzo, V.; Neilands, J.B. !$#journal J. Bacteriol. (1988) 170:56-64 !$#title Nucleotide sequence of the iucD gene of the pColV-K30 !1aerobactin operon and topology of its product studied with !1phoA and lacZ gene fusions. !$#cross-references MUID:88086924; PMID:3275632 !$#accession A28665 !'##molecule_type DNA !'##residues 1-426 ##label HER !'##cross-references GB:M18968; NID:g144692; PIDN:AAA23196.1; !1PID:g144693 !'##note residues 1-15 were confirmed by protein sequencing COMMENT This is one of the proteins involved in the biosynthesis of !1siderophores, which are chelators that mediate the !1high-affinity iron transport systems induced by the organism !1under iron-stressed conditions. It is a cytoplasmic !1membrane-bound protein catalyzing the formation of N !1(6)-hydroxylysine. GENETICS !$#gene iucD !$#genome plasmid ColV-K30 FUNCTION !$#description EC 1.13.12.10 [validated, MUID:86111626]; catalyzes !1oxygenation of lysine !$#pathway aerobactin biosynthesis CLASSIFICATION #superfamily iucD protein KEYWORDS iron transport; membrane protein; monooxygenase; !1oxidoreductase SUMMARY #length 426 #molecular-weight 48960 #checksum 387 SEQUENCE /// ENTRY BVECJ #type complete TITLE nitrate reductase 1 assembly protein narJ - Escherichia coli (strain K-12) ALTERNATE_NAMES nitrate reductase 1 delta chain [misnomer] ORGANISM #formal_name Escherichia coli DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 01-Mar-2002 ACCESSIONS B27737; PT0025; G64869 REFERENCE A91868 !$#authors Sodergren, E.J.; DeMoss, J.A. !$#journal J. Bacteriol. (1988) 170:1721-1729 !$#title narI region of the Escherichia coli nitrate reductase (nar) !1operon contains two genes. !$#cross-references MUID:88169497; PMID:2832376 !$#accession B27737 !'##molecule_type DNA !'##residues 1-236 ##label SOD !'##cross-references GB:M20147; NID:g146918; PIDN:AAA24196.1; !1PID:g146920 REFERENCE JV0037 !$#authors Blasco, F.; Iobbi, C.; Giordano, G.; Chippaux, M.; Bonnefoy, !1V. !$#journal Mol. Gen. Genet. (1989) 218:249-256 !$#title Nitrate reductase of Escherichia coli: completion of the !1nucleotide sequence of the nar operon and reassessment of !1the role of the alpha and beta subunits in iron binding and !1electron transfer. !$#cross-references MUID:89384449; PMID:2674654 !$#accession PT0025 !'##molecule_type DNA !'##residues 1-50 ##label BLA !'##experimental_source strain TG1 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64869 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-236 ##label BLAT !'##cross-references GB:AE000221; GB:U00096; NID:g1787476; !1PIDN:AAC74310.1; PID:g1787479; UWGP:b1226 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene narJ !$#map_position 27 min FUNCTION !$#description specific chaperone required for molybdenum cofactor assembly !1in nitrate reductase A !$#note formation of active, membrane-bound nitrate reductase A !1requires the presence of three subunits narG, narH and narI, !1as well as narJ that is not part of the active enzyme; narJ !1binds to narG and may thus keep it in an appropriate !1competent-open conformation for the molybdenum cofactor !1insertion to occur, resulting in a catalytically active !1enzyme; upon insertion of the molybdenum cofactor into the !1apo-nitrate reductase, narJ is then dissociated from the !1activated enzyme CLASSIFICATION #superfamily narJ protein KEYWORDS nitrate assimilation SUMMARY #length 236 #molecular-weight 26449 #checksum 7880 SEQUENCE /// ENTRY SYECLA #type complete TITLE lipid-A-disaccharide synthase (EC 2.4.1.182) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1988 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS F64742; B28389; D33171; A28390 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64742 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-382 ##label BLAT !'##cross-references GB:AE000127; GB:U00096; NID:g1786370; !1PIDN:AAC73293.1; PID:g1786379; UWGP:b0182 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A91854 !$#authors Crowell, D.N.; Reznikoff, W.S.; Raetz, C.R.H. !$#journal J. Bacteriol. (1987) 169:5727-5734 !$#title Nucleotide sequence of the Escherichia coli gene for lipid A !1disaccharide synthase. !$#cross-references MUID:88058790; PMID:2824445 !$#accession B28389 !'##molecule_type DNA !'##residues 1-148,'V',150-382 ##label CRO !'##cross-references GB:D83536; NID:g4902908; PIDN:BAA77857.1; !1PID:g4902923 REFERENCE A33171 !$#authors Coleman, J.; Raetz, C.R.H. !$#journal J. Bacteriol. (1988) 170:1268-1274 !$#title First committed step of lipid A biosynthesis in Escherichia !1coli: sequence of the lpxA gene. !$#cross-references MUID:88139188; PMID:3277952 !$#accession D33171 !'##status preliminary !'##molecule_type DNA !'##residues 1-19 ##label COL !'##cross-references GB:M19334; GB:M18265; GB:M18266 REFERENCE A91855 !$#authors Tomasiewicz, H.G.; McHenry, C.S. !$#journal J. Bacteriol. (1987) 169:5735-5744 !$#title Sequence analysis of the Escherichia coli dnaE gene. !$#cross-references MUID:88058791; PMID:3316192 !$#accession A28390 !'##molecule_type DNA !'##residues 329-382 ##label TOM GENETICS !$#gene lpxB !$#map_position 4 min FUNCTION !$#description catalyzes the condensation of UDP-2,3-diacylglucosamine and !12,3-diacylglucosamine-1-phosphate to form lipid A !1disaccharide, a precursor of lipid A, which is a !1phosphorylated glycolipid that anchors the !1lipopolysaccharide to the outer membrane of the E. coli cell CLASSIFICATION #superfamily lipid A disaccharide synthase KEYWORDS glycosyltransferase; hexosyltransferase; lipid A !1biosynthesis SUMMARY #length 382 #molecular-weight 42382 #checksum 1157 SEQUENCE /// ENTRY RGECF #type complete TITLE transcription regulator fnr - Escherichia coli (strain K-12) ALTERNATE_NAMES fumarate and nitrate reduction regulatory protein ORGANISM #formal_name Escherichia coli DATE 17-Dec-1982 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS A64883; A03552; S11810 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64883 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-250 ##label BLAT !'##cross-references GB:AE000231; GB:U00096; NID:g1787588; !1PIDN:AAC74416.1; PID:g1787595; UWGP:b1334 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A93444 !$#authors Shaw, D.J.; Guest, J.R. !$#journal Nucleic Acids Res. (1982) 10:6119-6130 !$#title Nucleotide sequence of the fnr gene and primary structure of !1the Fnr protein of Escherichia coli. !$#cross-references MUID:83064543; PMID:6292868 !$#accession A03552 !'##molecule_type DNA !'##residues 1-28,'S',30-250 ##label SHA !'##cross-references GB:J01608; NID:g146960; PIDN:AAA87981.1; !1PID:g146961 !'##experimental_source strain K-12 !'##note this protein is suggested to be a positive regulatory protein !1essential for the traoscription of the genes encoding !1proteins involved in a variety of anaerobic electron !1transport systems REFERENCE S11810 !$#authors Trageser, M.; Spiro, S.; Duchene, A.; Kojro, E.; Fahrenholz, !1F.; Guest, J.R.; Unden, G. !$#journal Mol. Microbiol. (1990) 4:21-27 !$#title Isolation of intact FNR protein (M(r)30000) of Escherichia !1coli. !$#cross-references MUID:90205623; PMID:2181237 !$#accession S11810 !'##molecule_type protein !'##residues 1,'V',3-20 ##label TRA GENETICS !$#gene fnr !$#map_position 29 min COMPLEX monomer FUNCTION !$#description transcription regulation; essential for expressing anaerobic !1respiratory processes; functions negatively as an anaerobic !1repressor as well as positively as an anaerobic activator !$#note senses anoxia and is thereby transformed in to its active !1form CLASSIFICATION #superfamily regulatory protein fnr; cAMP receptor protein !1cyclic nucleotide-binding domain homology KEYWORDS DNA binding; repressor; transcription regulation FEATURE !$31-152 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP\ !$197-216 #region helix-turn-helix crp-type motif SUMMARY #length 250 #molecular-weight 27967 #checksum 6980 SEQUENCE /// ENTRY A37769 #type complete TITLE hlyX protein - Actinobacillus pleuropneumoniae ORGANISM #formal_name Actinobacillus pleuropneumoniae DATE 31-May-1991 #sequence_revision 10-Feb-1995 #text_change 16-Jul-1999 ACCESSIONS A37769; I39517 REFERENCE A37769 !$#authors MacInnes, J.I.; Kim, J.E.; Lian, C.J.; Soltes, G.A. !$#journal J. Bacteriol. (1990) 172:4587-4592 !$#title Actinobacillus pleuropneumoniae hlyX gene homology with the !1fnr gene of Escherichia coli. !$#cross-references MUID:90330570; PMID:2198268 !$#accession A37769 !'##molecule_type DNA !'##residues 1-240 ##label MAC !'##cross-references GB:M34443; GB:M80712; NID:g141830; PIDN:AAA21920.1; !1PID:g141831 !'##experimental_source serotype 1 strain CM5 COMMENT The strong homology with regulatory protein fnr from E. coli !1suggests that this protein is regulatory rather than !1hemolytic. GENETICS !$#gene hlyX CLASSIFICATION #superfamily regulatory protein fnr; cAMP receptor protein !1cyclic nucleotide-binding domain homology KEYWORDS DNA binding; transcription regulation FEATURE !$30-151 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP\ !$196-215 #region helix-turn-helix crp-type motif SUMMARY #length 240 #molecular-weight 27107 #checksum 5700 SEQUENCE /// ENTRY S16307 #type complete TITLE transcription activator anr - Pseudomonas aeruginosa ORGANISM #formal_name Pseudomonas aeruginosa DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 31-Dec-2000 ACCESSIONS S16307; S16302; G83453 REFERENCE S16307 !$#authors Zimmermann, A.; Reimmann, C.; Galimand, M.; Haas, D. !$#journal Mol. Microbiol. (1991) 5:1483-1490 !$#title Anaerobic growth and cyanide synthesis of Pseudomonas !1aeruginosa depend on anr, a regulatory gene homologous with !1fnr of Escherichia coli. !$#cross-references MUID:92157874; PMID:1787798 !$#accession S16307 !'##status preliminary !'##molecule_type DNA !'##residues 1-244 ##label ZIM !'##cross-references EMBL:X57736; NID:g45359; PIDN:CAA40906.1; !1PID:g45363 REFERENCE S16302 !$#authors Sawers, R.G. !$#journal Mol. Microbiol. (1991) 5:1469-1481 !$#title Identification and molecular characterization of a !1transcriptional regulator from Pseudomonas aeruginosa PAO1 !1exhibiting structural and functional similarity to the FNR !1protein of Escherichia coli. !$#cross-references MUID:92157873; PMID:1787797 !$#accession S16302 !'##status preliminary !'##molecule_type DNA !'##residues 1-244 ##label SAW !'##cross-references EMBL:X58405; NID:g45277; PIDN:CAA41305.1; !1PID:g45278 REFERENCE A82950 !$#authors Stover, C.K.; Pham, X.Q.; Erwin, A.L.; Mizoguchi, S.D.; !1Warrener, P.; Hickey, M.J.; Brinkman, F.S.L.; Hufnagle, !1W.O.; Kowalik, D.J.; Lagrou, M.; Garber, R.L.; Goltry, L.; !1Tolentino, E.; Westbrook-Wadman, S.; Yuan, Y.; Brody, L.L.; !1Coulter, S.N.; Folger, K.R.; Kas, A.; Larbig, K.; Lim, R.M.; !1Smith, K.A.; Spencer, D.H.; Wong, G.K.S.; Wu, Z.; Paulsen, !1I.T.; Reizer, J.; Saier, M.H.; Hancock, R.E.W.; Lory, S.; !1Olson, M.V. !$#journal Nature (2000) 406:959-964 !$#title Complete genome sequence of Pseudomonas aeruginosa PA01, an !1opportunistic pathogen. !$#cross-references MUID:20437337; PMID:10984043 !$#accession G83453 !'##status preliminary !'##molecule_type DNA !'##residues 1-244 ##label STO !'##cross-references GB:AE004582; GB:AE004091; NID:g9947492; !1PIDN:AAG04933.1; GSPDB:GN00131; PASP:PA1544 !'##experimental_source strain PAO1 GENETICS !$#gene anr; PA1544 !$#map_position 61 min CLASSIFICATION #superfamily regulatory protein fnr; cAMP receptor protein !1cyclic nucleotide-binding domain homology KEYWORDS DNA binding; transcription regulation FEATURE !$26-147 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP\ !$192-211 #region helix-turn-helix crp-type motif SUMMARY #length 244 #molecular-weight 27129 #checksum 2731 SEQUENCE /// ENTRY B42371 #type complete TITLE regulatory protein fixK - Bradyrhizobium japonicum ORGANISM #formal_name Bradyrhizobium japonicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B42371 REFERENCE A42371 !$#authors Anthamatten, D.; Scherb, B.; Hennecke, H. !$#journal J. Bacteriol. (1992) 174:2111-2120 !$#title Characterization of a fixLJ-regulated Bradyrhizobium !1japonicum gene sharing similarity with the Escherichia coli !1fnr and Rhizobium meliloti fixK genes. !$#cross-references MUID:92202135; PMID:1551834 !$#accession B42371 !'##status preliminary !'##molecule_type DNA !'##residues 1-237 ##label ANT !'##cross-references GB:M86805; NID:g152085; PIDN:AAA26209.1; !1PID:g152087 CLASSIFICATION #superfamily regulatory protein fnr; cAMP receptor protein !1cyclic nucleotide-binding domain homology KEYWORDS DNA binding; transcription regulation SUMMARY #length 237 #molecular-weight 26168 #checksum 9541 SEQUENCE /// ENTRY S37397 #type complete TITLE regulatory protein fnrA - Pseudomonas stutzeri ORGANISM #formal_name Pseudomonas stutzeri DATE 06-Jan-1995 #sequence_revision 10-Feb-1995 #text_change 16-Jul-1999 ACCESSIONS A49927; S37397 REFERENCE A49927 !$#authors Cuypers, H.; Zumft, W.G. !$#journal J. Bacteriol. (1993) 175:7236-7246 !$#title Anaerobic control of denitrification in Pseudomonas stutzeri !1escapes mutagenesis of an fnr-like gene. !$#cross-references MUID:94042897; PMID:8226670 !$#accession A49927 !'##molecule_type DNA !'##residues 1-244 ##label CUY !'##cross-references EMBL:Z26044; NID:g398390; PIDN:CAA81129.1; !1PID:g398391 !'##experimental_source strain ZoBell (ATCC 14405) COMMENT This protein probably regulates the arginine catabolic !1pathway. GENETICS !$#gene fnrA CLASSIFICATION #superfamily regulatory protein fnr; cAMP receptor protein !1cyclic nucleotide-binding domain homology KEYWORDS DNA binding; transcription regulation FEATURE !$26-147 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP\ !$192-211 #region helix-turn-helix crp-type motif SUMMARY #length 244 #molecular-weight 27089 #checksum 2575 SEQUENCE /// ENTRY B43334 #type complete TITLE cAMP receptor protein transcription regulator AadR - Rhodopseudomonas palustris ORGANISM #formal_name Rhodopseudomonas palustris DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B43334 REFERENCE A43334 !$#authors Dispensa, M.; Thomas, C.T.; Kim, M.K.; Perrotta, J.A.; !1Gibson, J.; Harwood, C.S. !$#journal J. Bacteriol. (1992) 174:5803-5813 !$#title Anaerobic growth of Rhodopseudomonas palustris on !14-hydroxybenzoate is dependent on AadR, a member of the !1cyclic AMP receptor protein family of transcriptional !1regulators. !$#cross-references MUID:92394882; PMID:1522059 !$#accession B43334 !'##status preliminary !'##molecule_type DNA !'##residues 1-239 ##label DIS !'##cross-references GB:M92426; NID:g151870; PIDN:AAA26090.1; !1PID:g151872 !'##note sequence extracted from NCBI backbone (NCBIN:112964, !1NCBIP:112966) CLASSIFICATION #superfamily regulatory protein fnr; cAMP receptor protein !1cyclic nucleotide-binding domain homology KEYWORDS DNA binding; transcription regulation SUMMARY #length 239 #molecular-weight 26711 #checksum 4358 SEQUENCE /// ENTRY S16632 #type complete TITLE regulatory protein fixK - Azorhizobium caulinodans ORGANISM #formal_name Azorhizobium caulinodans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S16632 REFERENCE S16632 !$#authors Kaminski, P.A.; Mandon, K.; Arigoni, F.; Desnoues, N.; !1Elmerich, C. !$#journal Mol. Microbiol. (1991) 5:1983-1991 !$#title Regulation of nitrogen fixation in Azorhizobium caulinodans: !1identification of a fixK-like gene, a positive regulator of !1nifA. !$#cross-references MUID:92114774; PMID:1766374 !$#accession S16632 !'##status preliminary !'##molecule_type DNA !'##residues 1-248 ##label KAM !'##cross-references EMBL:X59071; NID:g38701; PIDN:CAA41794.1; !1PID:g38702 CLASSIFICATION #superfamily regulatory protein fnr; cAMP receptor protein !1cyclic nucleotide-binding domain homology KEYWORDS DNA binding; transcription regulation SUMMARY #length 248 #molecular-weight 27104 #checksum 7173 SEQUENCE /// ENTRY S04122 #type complete TITLE regulatory protein fixK - Rhizobium meliloti ORGANISM #formal_name Rhizobium meliloti DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S04122; S39986; S32839 REFERENCE S04122 !$#authors Batut, J.; Daveran-Mingot, M.L.; David, M.; Jacobs, J.; !1Garnerone, A.M.; Kahn, D. !$#journal EMBO J. (1989) 8:1279-1286 !$#title fixK, a gene homologous with fnr and crp from Escherichia !1coli, regulates nitrogen fixation genes both positively and !1negatively in Rhizobium meliloti. !$#cross-references MUID:89305532; PMID:2663474 !$#accession S04122 !'##molecule_type DNA !'##residues 1-211 ##label BAT !'##cross-references EMBL:Z21854; NID:g49403; PIDN:CAA79899.1; !1PID:g49406; EMBL:X15079; NID:g48690; PID:g48691 !$#accession S39986 !'##molecule_type DNA !'##residues 1-211 ##label KAH GENETICS !$#gene fixK CLASSIFICATION #superfamily regulatory protein fnr; cAMP receptor protein !1cyclic nucleotide-binding domain homology KEYWORDS DNA binding; transcription regulation FEATURE !$163-182 #region helix-turn-helix crp-type motif SUMMARY #length 211 #molecular-weight 23478 #checksum 8160 SEQUENCE /// ENTRY B48640 #type complete TITLE regulatory protein ntcA - Anabaena sp. (strain PCC 7120) ALTERNATE_NAMES regulatory protein bifA ORGANISM #formal_name Anabaena sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B48640; A40653; S32665 REFERENCE A48640 !$#authors Frias, J.E.; Merida, A.; Herrero, A.; Martin-Nieto, J.; !1Flores, E. !$#journal J. Bacteriol. (1993) 175:5710-5713 !$#title General distribution of the nitrogen control gene ntcA in !1cyanobacteria. !$#cross-references MUID:93374871; PMID:8366058 !$#accession B48640 !'##status preliminary !'##molecule_type DNA !'##residues 1-223 ##label FRI !'##cross-references EMBL:X71608; NID:g296875; PIDN:CAA50608.1; !1PID:g296876 REFERENCE A40653 !$#authors Wei, T.F.; Ramasubramanian, T.S.; Pu, F.; Golden, J.W. !$#journal J. Bacteriol. (1993) 175:4025-4035 !$#title Anabaena sp. strain PCC 7120 bifA gene encoding a !1sequence-specific DNA-binding protein cloned by in vivo !1transcriptional interference selection. !$#cross-references MUID:93308081; PMID:8391534 !$#accession A40653 !'##status preliminary !'##molecule_type DNA !'##residues 1-223 ##label WEI !'##cross-references GB:L10036; NID:g142008; PIDN:AAD04183.1; !1PID:g142009 GENETICS !$#gene ntcA; bifA CLASSIFICATION #superfamily regulatory protein fnr; cAMP receptor protein !1cyclic nucleotide-binding domain homology KEYWORDS DNA binding; transcription regulation FEATURE !$176-195 #region helix-turn-helix crp-type motif SUMMARY #length 223 #molecular-weight 24918 #checksum 2731 SEQUENCE /// ENTRY A48640 #type complete TITLE global nitrogen regulator protein - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A48640; S75450; S33206 REFERENCE A48640 !$#authors Frias, J.E.; Merida, A.; Herrero, A.; Martin-Nieto, J.; !1Flores, E. !$#journal J. Bacteriol. (1993) 175:5710-5713 !$#title General distribution of the nitrogen control gene ntcA in !1cyanobacteria. !$#cross-references MUID:93374871; PMID:8366058 !$#accession A48640 !'##status preliminary !'##molecule_type DNA !'##residues 1-225 ##label FRI !'##cross-references EMBL:X71607; NID:g296889; PIDN:CAA50607.1; !1PID:g296890 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75450 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-225 ##label KAN !'##cross-references EMBL:D90911; GB:AB001339; NID:g1653083; !1PIDN:BAA18011.1; PID:g1653095 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene ntcA CLASSIFICATION #superfamily regulatory protein fnr; cAMP receptor protein !1cyclic nucleotide-binding domain homology KEYWORDS DNA binding; transcription regulation FEATURE !$178-197 #region helix-turn-helix crp-type motif SUMMARY #length 225 #molecular-weight 25046 #checksum 2424 SEQUENCE /// ENTRY S25244 #type complete TITLE regulatory protein ntcA - Synechococcus sp. (strain PCC 7942) ORGANISM #formal_name Synechococcus sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S25244 REFERENCE S25244 !$#authors Vega-Palas, M.A.; Flores, E.; Herrero, A. !$#journal Mol. Microbiol. (1992) 6:1853-1859 !$#title NtcA, a global nitrogen regulator from the cyanobacterium !1Synechococcus that belongs to the Crp family of bacterial !1regulators. !$#cross-references MUID:92334161; PMID:1630321 !$#accession S25244 !'##molecule_type DNA !'##residues 1-222 ##label VEG !'##cross-references EMBL:X60197; NID:g47621; PIDN:CAA42755.1; !1PID:g47622 GENETICS !$#gene ntcA CLASSIFICATION #superfamily regulatory protein fnr; cAMP receptor protein !1cyclic nucleotide-binding domain homology KEYWORDS DNA binding; transcription regulation SUMMARY #length 222 #molecular-weight 24833 #checksum 640 SEQUENCE /// ENTRY QRECC #type complete TITLE cAMP receptor protein - Escherichia coli (strain K-12) ALTERNATE_NAMES catabolite gene activator protein (CAP) ORGANISM #formal_name Escherichia coli DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 01-Mar-2002 ACCESSIONS A93416; A93417; H65129; A03553 REFERENCE A93416 !$#authors Aiba, H.; Fujimoto, S.; Ozaki, N. !$#journal Nucleic Acids Res. (1982) 10:1345-1361 !$#title Molecular cloning and nucleotide sequencing of the gene for !1Escherichia coli cAMP receptor protein. !$#cross-references MUID:82174313; PMID:6280140 !$#accession A93416 !'##molecule_type DNA !'##residues 1-210 ##label AIB !'##cross-references GB:J01598; NID:g145593; PIDN:AAA23601.1; !1PID:g145594 REFERENCE A93417 !$#authors Cossart, P.; Gicquel-Sanzey, B. !$#journal Nucleic Acids Res. (1982) 10:1363-1378 !$#title Cloning and sequence of the crp gene of Escherichia coli !1K12. !$#cross-references MUID:82174314; PMID:6280141 !$#accession A93417 !'##molecule_type DNA !'##residues 1-210 ##label COS !'##cross-references GB:J01598; NID:g145593; PIDN:AAA23601.1; !1PID:g145594 !'##experimental_source strain K12 REFERENCE A92385 !$#authors McKay, D.B.; Weber, I.T.; Steitz, T.A. !$#journal J. Biol. Chem. (1982) 257:9518-9524 !$#title Structure of catabolite gene activator protein at !12.9-angstrom resolution. Incorporation of amino acid !1sequence and interactions with cyclic AMP. !$#cross-references MUID:82265592; PMID:6286624 !$#contents annotation; X-ray crystallography, 2.9 angstroms REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65129 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-210 ##label BLAT !'##cross-references GB:AE000411; GB:U00096; NID:g2367213; !1PIDN:AAC76382.1; PID:g1789756; UWGP:b3357 !'##experimental_source strain K-12, substrain MG1655 COMMENT This protein complexes with cyclic AMP and binds to specific !1DNA sites near the promoter to regulate the transcription of !1several catabolite-sensitive operons in E. coli. GENETICS !$#gene crp !$#map_position 74 min CLASSIFICATION #superfamily regulatory protein fnr; cAMP receptor protein !1cyclic nucleotide-binding domain homology KEYWORDS cAMP binding; DNA binding; transcription regulation FEATURE !$3-126 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP\ !$73,83 #binding_site cAMP (Glu, Arg) #status experimental SUMMARY #length 210 #molecular-weight 23640 #checksum 7447 SEQUENCE /// ENTRY A44903 #type complete TITLE cAMP receptor protein - Klebsiella pneumoniae ALTERNATE_NAMES CAP; catabolite gene activator protein ORGANISM #formal_name Klebsiella pneumoniae DATE 03-Feb-1994 #sequence_revision 10-Feb-1995 #text_change 20-Apr-2000 ACCESSIONS A44903 REFERENCE A44903 !$#authors Osuna, R.; Bender, R.A. !$#journal J. Bacteriol. (1991) 173:6626-6631 !$#title Klebsiella aerogenes catabolite gene activator protein and !1the gene encoding it (crp). !$#cross-references MUID:92011440; PMID:1655718 !$#accession A44903 !'##molecule_type DNA !'##residues 1-210 ##label OSU !'##cross-references GB:M68973; NID:g149176; PIDN:AAA25058.1; !1PID:g149177 !'##experimental_source strain KC1043 !'##note the source is designated as Klebsiella aerogenes !'##note sequence extracted from NCBI backbone (NCBIN:59917, !1NCBIP:59918) COMMENT In E. coli, the CAP-cAMP complex binds specifically at or !1near certain promoters, resulting in stimulation or !1repression of transcription. Transcription of the crp gene !1itself is negatively regulated. COMMENT The CAP-cAMP complex regulates several operons including lac !1and hut. GENETICS !$#gene crp CLASSIFICATION #superfamily regulatory protein fnr; cAMP receptor protein !1cyclic nucleotide-binding domain homology KEYWORDS cAMP binding; DNA binding; transcription regulation FEATURE !$3-126 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP\ !$170-189 #region helix-turn-helix crp-type motif\ !$73,83 #binding_site cAMP (Glu, Arg) #status predicted SUMMARY #length 210 #molecular-weight 23656 #checksum 7537 SEQUENCE /// ENTRY A26049 #type complete TITLE cAMP receptor protein - Salmonella typhimurium ALTERNATE_NAMES CAP; catabolite gene activator protein ORGANISM #formal_name Salmonella typhimurium DATE 05-Oct-1988 #sequence_revision 10-Feb-1995 #text_change 16-Jul-1999 ACCESSIONS A26049 REFERENCE A26049 !$#authors Schroeder, C.J.; Dobrogosz, W.J. !$#journal J. Bacteriol. (1986) 167:616-622 !$#title Cloning and DNA sequence analysis of the wild-type and !1mutant cyclic AMP receptor protein genes from Salmonella !1typhimurium. !$#cross-references MUID:86277921; PMID:3015882 !$#accession A26049 !'##molecule_type DNA !'##residues 1-210 ##label SCH !'##cross-references GB:M13770; NID:g145597; PIDN:AAA62414.1; !1PID:g145598 COMMENT In E. coli, the CAP-cAMP complex binds specifically at or !1near certain promoters, resulting in stimulation or !1repression of transcription. Transcription of the crp gene !1itself is negatively regulated. GENETICS !$#gene crp !$#map_position 72 min CLASSIFICATION #superfamily regulatory protein fnr; cAMP receptor protein !1cyclic nucleotide-binding domain homology KEYWORDS cAMP binding; DNA binding; transcription regulation FEATURE !$3-126 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP\ !$170-189 #region helix-turn-helix crp-type motif\ !$73,83 #binding_site cAMP (Glu, Arg) #status predicted SUMMARY #length 210 #molecular-weight 23614 #checksum 7727 SEQUENCE /// ENTRY B38225 #type complete TITLE cAMP receptor protein - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES CAP; catabolite gene activator protein ORGANISM #formal_name Haemophilus influenzae DATE 04-Mar-1993 #sequence_revision 10-Feb-1995 #text_change 16-Jul-1999 ACCESSIONS B38225; I64104 REFERENCE A38225 !$#authors Chandler, M.S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:1626-1630 !$#title The gene encoding cAMP receptor protein is required for !1competence development in Haemophilus influenzae Rd. !$#cross-references MUID:92179236; PMID:1542653 !$#accession B38225 !'##molecule_type DNA !'##residues 1-224 ##label CHA !'##cross-references GB:M77207; NID:g148878; PIDN:AAA24952.1; !1PID:g148880 !'##experimental_source Rd strain JG87 !'##note sequence extracted from NCBI backbone (NCBIN:86635, !1NCBIP:86639) REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession I64104 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-224 ##label TIGR !'##cross-references GB:U32776; GB:L42023; NID:g1573969; !1PIDN:AAC22618.1; PID:g1573982; TIGR:HI0957 !'##experimental_source Rd strain KW20 COMMENT In E. coli, the CAP-cAMP complex binds specifically at or !1near certain promoters, resulting in stimulation or !1repression of transcription. Transcription of the crp gene !1itself is negatively regulated. COMMENT The CAP-cAMP complex is required for this organism to be !1competent to bind, take up, and integrate exogenous DNA. GENETICS !$#gene crp CLASSIFICATION #superfamily regulatory protein fnr; cAMP receptor protein !1cyclic nucleotide-binding domain homology KEYWORDS cAMP binding; DNA binding; transcription regulation FEATURE !$17-140 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP\ !$184-203 #region helix-turn-helix crp-type motif\ !$87,97 #binding_site cAMP (Glu, Arg) #status predicted SUMMARY #length 224 #molecular-weight 25152 #checksum 5741 SEQUENCE /// ENTRY E43670 #type complete TITLE probable regulatory protein cysR - Synechococcus sp. ORGANISM #formal_name Synechococcus sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS E43670 REFERENCE A43670 !$#authors Laudenbach, D.E.; Grossman, A.R. !$#journal J. Bacteriol. (1991) 173:2739-2750 !$#title Characterization and mutagenesis of sulfur-regulated genes !1in a cyanobacterium: evidence for function in sulfate !1transport. !$#cross-references MUID:91210162; PMID:1708375 !$#accession E43670 !'##status preliminary !'##molecule_type DNA !'##residues 1-206 ##label LAU !'##cross-references GB:M65247; NID:g154505; PIDN:AAA73046.1; !1PID:g154510 CLASSIFICATION #superfamily regulatory protein fnr; cAMP receptor protein !1cyclic nucleotide-binding domain homology KEYWORDS DNA binding; transcription regulation SUMMARY #length 206 #molecular-weight 22760 #checksum 2349 SEQUENCE /// ENTRY A42949 #type complete TITLE cAMP receptor protein homolog - Xanthomonas campestris ALTERNATE_NAMES CAP-like protein; catabolite gene activator protein homolog; CLP ORGANISM #formal_name Xanthomonas campestris DATE 04-Mar-1993 #sequence_revision 10-Feb-1995 #text_change 01-Sep-2000 ACCESSIONS A42949; B36140 REFERENCE A42949 !$#authors Dong, Q.; Ebright, R.H. !$#journal J. Bacteriol. (1992) 174:5457-5461 !$#title DNA binding specificity and sequence of Xanthomonas !1campestris catabolite gene activator protein-like protein. !$#cross-references MUID:92355525; PMID:1322886 !$#accession A42949 !'##molecule_type DNA !'##residues 1-230 ##label DON !'##cross-references GB:M92289; NID:g155364; PIDN:AAA27598.1; !1PID:g155365 !'##note sequence extracted from NCBI backbone (NCBIN:110542, !1NCBIP:110543) REFERENCE A36140 !$#authors de Crecy-Lagard, V.; Glaser, P.; Lejeune, P.; Sismeiro, O.; !1Barber, C.E.; Daniels, M.J.; Danchin, A. !$#journal J. Bacteriol. (1990) 172:5877-5883 !$#title A Xanthomonas campestris pv. campestris protein similar to !1catabolite activation factor is involved in regulation of !1phytopathogenicity. !$#cross-references MUID:91008963; PMID:2170330 !$#accession B36140 !'##molecule_type DNA !'##residues 1-199,'CAQ',203-230 ##label DEC !'##cross-references GB:M58745; NID:g155361; PIDN:AAA27597.1; !1PID:g155363 !'##experimental_source Xanthomonas campestris pv. campestris COMMENT This protein regulates, directly or indirectly, genes !1implicated in phytopathogenicity. Regulation is independent !1of cAMP. COMMENT This organism is the causative agent of black rot of !1crucifers. GENETICS !$#gene clp CLASSIFICATION #superfamily regulatory protein fnr; cAMP receptor protein !1cyclic nucleotide-binding domain homology KEYWORDS DNA binding; transcription regulation; virulence regulation FEATURE !$18-146 #domain cAMP receptor protein cyclic !8nucleotide-binding domain homology #label CAP\ !$190-209 #region helix-turn-helix crp-type motif SUMMARY #length 230 #molecular-weight 25692 #checksum 6951 SEQUENCE /// ENTRY S51356 #type complete TITLE olfactory receptor - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S51356; S47014 REFERENCE S51356 !$#authors Gat, U.; Nekrasova, E.; Lancet, D.; Natochin, M. !$#journal Eur. J. Biochem. (1994) 225:1157-1168 !$#title Olfactory receptor proteins. Expression, characterization !1and partial purification. !$#cross-references MUID:95045546; PMID:7957207 !$#accession S51356 !'##status preliminary !'##molecule_type mRNA !'##residues 1-309 ##label GAT !'##cross-references EMBL:X80671; NID:g517365; PIDN:CAA56697.1; !1PID:g517366 REFERENCE S47014 !$#authors Gat, U.; Nekrasova, E.; Lancet, D.; Natochin, M. !$#submission submitted to the EMBL Data Library, July 1994 !$#description Olfactory receptor proteins: expression, characterization !1and partial purification. !$#accession S47014 !'##status preliminary !'##molecule_type mRNA !'##residues 1-309 ##label GA2 !'##cross-references EMBL:X80671; NID:g517365; PIDN:CAA56697.1; !1PID:g517366 CLASSIFICATION #superfamily olfactory receptor OR14 SUMMARY #length 309 #molecular-weight 34474 #checksum 9997 SEQUENCE /// ENTRY S05380 #type complete TITLE transcription factor ATF2 - human ALTERNATE_NAMES activating transcription factor 2 (ATF-2); cAMP response element-binding protein 1; TGACGTCA-binding transcription factor CONTAINS cAMP response element-binding protein HB16 ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 02-Jun-2000 ACCESSIONS S05380; A34776; B34223 REFERENCE S05380 !$#authors Maekawa, T.; Sakura, H.; Kanei-Ishii, C.; Sudo, T.; !1Yoshimura, T.; Fujisawa, J.I.; Yoshida, M.; Ishii, S. !$#journal EMBO J. (1989) 8:2023-2028 !$#title Leucine zipper structure of the protein CRE-BP1 binding to !1the cyclic AMP response element in brain. !$#cross-references MUID:90005408; PMID:2529117 !$#accession S05380 !'##molecule_type mRNA !'##residues 1-505 ##label MAE !'##cross-references EMBL:X15875; NID:g30214; PIDN:CAA33886.1; !1PID:g30215 REFERENCE A34776 !$#authors Kara, C.J.; Liou, H.C.; Ivashkiv, L.B.; Glimcher, L.H. !$#journal Mol. Cell. Biol. (1990) 10:1347-1357 !$#title A cDNA for a human cyclic AMP response element-binding !1protein which is distinct from CREB and expressed !1preferentially in brain. !$#cross-references MUID:90205810; PMID:2320002 !$#accession A34776 !'##status preliminary !'##molecule_type DNA !'##residues 211-222,'N',224-505 ##label KAR !'##cross-references GB:M31630; NID:g183787; PIDN:AAA35951.1; !1PID:g386762 REFERENCE A91622 !$#authors Hai, T.; Liu, F.; Coukos, W.J.; Green, M.R. !$#journal Genes Dev. (1989) 3:2083-2090 !$#title Transcription factor ATF cDNA clones: an extensive family of !1leucine zipper proteins able to selectively form DNA-binding !1heterodimers. !$#cross-references MUID:90185187; PMID:2516827 !$#accession B34223 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type mRNA !'##residues 107-357,'V',359-465 ##label HA2 GENETICS !$#gene GDB:ATF2; CREB2; TREB7; CRE-BP1 !'##cross-references GDB:128011; OMIM:123811 !$#map_position 2q32-2q32 CLASSIFICATION #superfamily cAMP response element-binding protein 1; fos/ !1jun DNA-binding domain homology KEYWORDS alternative splicing; DNA binding; nucleus; transcription !1regulation FEATURE !$347-387 #domain fos/jun DNA-binding domain homology #label !8FJD SUMMARY #length 505 #molecular-weight 54510 #checksum 5045 SEQUENCE /// ENTRY A39429 #type complete TITLE cAMP response element-binding protein ATF2 - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A39429 REFERENCE A39429 !$#authors Kageyama, R.; Sasai, Y.; Nakanishi, S. !$#journal J. Biol. Chem. (1991) 266:15525-15531 !$#title Molecular characterization of transcription factors that !1bind to the cAMP responsive region of the substance P !1precursor gene. cDNA cloning of a novel C/EBP-related !1factor. !$#cross-references MUID:91332085; PMID:1714459 !$#accession A39429 !'##status preliminary !'##molecule_type mRNA !'##residues 1-389 ##label KAG !'##cross-references GB:M65148; NID:g206569; PIDN:AAA42013.1; !1PID:g206570 CLASSIFICATION #superfamily cAMP response element-binding protein 1; fos/ !1jun DNA-binding domain homology KEYWORDS DNA binding; nucleus; transcription regulation FEATURE !$231-271 #domain fos/jun DNA-binding domain homology #label !8FJD SUMMARY #length 389 #molecular-weight 42320 #checksum 3280 SEQUENCE /// ENTRY QRECBT #type complete TITLE vitamin b12 receptor precursor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 28-Dec-1987 #sequence_revision 30-Sep-1997 #text_change 01-Mar-2002 ACCESSIONS A65204; A21892; I41186; C37321 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65204 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-614 ##label BLAT !'##cross-references GB:AE000471; GB:U00096; NID:g1790404; !1PIDN:AAC76948.1; PID:g1790405; UWGP:b3966 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A21892 !$#authors Heller, K.; Kadner, R.J. !$#journal J. Bacteriol. (1985) 161:904-908 !$#title Nucleotide sequence of the gene for the vitamin B12 receptor !1protein in the outer membrane of Escherichia coli. !$#cross-references MUID:85130824; PMID:3882670 !$#accession A21892 !'##molecule_type DNA !'##residues 1-161,'G',163-376,'R',378-614 ##label HEL !'##cross-references GB:M10112; NID:g145439; PIDN:AAA23524.1; !1PID:g145440 !'##note the authors translated the codon GAT for residue 592 as Arg REFERENCE I41186 !$#authors Doublet, P.; van Heijenoort, J.; Mengin-Lecreulx, D. !$#journal J. Bacteriol. (1992) 174:5772-5779 !$#title Identification of the Escherichia coli murI Gene, Which Is !1Required for the Biosynthesis of D-Glutamic Acid, a Specific !1Component of Bacterial Peptidoglycan. !$#cross-references MUID:92394878; PMID:1355768 !$#accession I41186 !'##status preliminary !'##molecule_type DNA !'##residues 456-614 ##label RES !'##cross-references GB:L14556; NID:g290426; PIDN:AAA23676.1; !1PID:g290427 REFERENCE A37321 !$#authors Gustafsson, C.; Lindstroem, P.H.R.; Hagervall, T.G.; Esberg, !1K.B.; Bjoerk, G.R. !$#journal J. Bacteriol. (1991) 173:1757-1764 !$#title The trmA promoter has regulatory features and sequence !1elements in common with the rRNA P1 promoter family of !1Escherichia coli. !$#cross-references MUID:91154132; PMID:1999392 !$#accession C37321 !'##molecule_type DNA !'##residues 1-5 ##label GUS !'##cross-references GB:M57568 GENETICS !$#gene btuB !$#map_position 90 min CLASSIFICATION #superfamily vitamin B12 receptor; tonB-dependent receptor !1amino-terminal homology; tonB-dependent receptor !1carboxyl-terminal homology KEYWORDS membrane protein; vitamin B12 transport FEATURE !$61-196 #domain tonB-dependent receptor amino-terminal !8homology #label TNN\ !$360-614 #domain tonB-dependent receptor carboxyl-terminal !8homology #label TNC SUMMARY #length 614 #molecular-weight 68407 #checksum 5894 SEQUENCE /// ENTRY QRECFA #type complete TITLE iron(III) dicitrate transport system outer membrane receptor precursor - Escherichia coli (strain K-12) ALTERNATE_NAMES iron(III) dicitrate transport protein FecA ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 10-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS E65242; S56516; JV0022; C37804; PS0029 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65242 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-774 ##label BLAT !'##cross-references GB:AE000499; GB:U00096; NID:g1790732; !1PIDN:AAC77247.1; PID:g1790743; UWGP:b4291 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56516 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-719,'X',721-774 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97187.1; !1PID:g537132 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE JV0022 !$#authors Pressler, U.; Staudenmaier, H.; Zimmermann, L.; Braun, V. !$#journal J. Bacteriol. (1988) 170:2716-2724 !$#title Genetics of the iron dicitrate transport system of !1Escherichia coli. !$#cross-references MUID:88227855; PMID:2836368 !$#accession JV0022 !'##molecule_type DNA !'##residues 1-15,'A',17-189,'T',191-299,'M',301-356,'R',358-443,'V', !1445-774 ##label PRE !'##cross-references EMBL:M20981 REFERENCE JV0111 !$#authors Van Hove, B.; Staudenmaier, H.; Braun, V. !$#journal J. Bacteriol. (1990) 172:6749-6758 !$#title Novel two-component transmembrane transcription control: !1regulation of iron dicitrate transport in Escherichia coli !1K-12. !$#cross-references MUID:91072220; PMID:2254251 !$#accession C37804 !'##status preliminary !'##molecule_type DNA !'##residues 1-428 ##label VAN !'##cross-references GB:M63115; NID:g145929; PIDN:AAA23768.1; !1PID:g145932 GENETICS !$#gene fecA !$#map_position 7 min FUNCTION !$#description this protein is the outer membrane receptor of one of the !1five identified iron(III) transport systems CLASSIFICATION #superfamily vitamin B12 receptor; tonB-dependent receptor !1amino-terminal homology; tonB-dependent receptor !1carboxyl-terminal homology KEYWORDS iron transport; membrane protein; receptor FEATURE !$1-33 #domain signal sequence #status predicted #label SIG\ !$34-774 #product iron(III) dicitrate transport system outer !8membrane receptor #status predicted #label MAT SUMMARY #length 774 #molecular-weight 85321 #checksum 9447 SEQUENCE /// ENTRY QRECFC #type complete TITLE ferrienterochelin receptor precursor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS F64791; A25953; S06980 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64791 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-746 ##label BLAT !'##cross-references GB:AE000163; GB:U00096; NID:g1786790; !1PIDN:AAC73685.1; PID:g1786798; UWGP:b0584 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A25953 !$#authors Lundrigan, M.D.; Kadner, R.J. !$#journal J. Biol. Chem. (1986) 261:10797-10801 !$#title Nucleotide sequence of the gene for the ferrienterochelin !1receptor FepA in Escherichia coli: homology among outer !1membrane receptors that interact with TonB. !$#cross-references MUID:86278160; PMID:3015941 !$#accession A25953 !'##molecule_type DNA !'##residues 1-151,'R',153-402,404-746 ##label LUN !'##cross-references GB:M13748; NID:g145941; PIDN:AAA65994.1; !1PID:g145942 REFERENCE S06980 !$#authors Armstrong, S.K.; Pettis, G.S.; Forrester, L.J.; McIntosh, !1M.A. !$#journal Mol. Microbiol. (1989) 3:757-766 !$#title The Escherichia coli enterobactin biosynthesis gene, entD: !1nucleotide sequence and membrane localization of its protein !1product. !$#cross-references MUID:89313305; PMID:2526281 !$#accession S06980 !'##molecule_type DNA !'##residues 735-746 ##label ARM !'##cross-references EMBL:X17426 GENETICS !$#gene fepA; fep !$#map_position 14 min FUNCTION !$#description receptor for ferrienterobactin (ferric enterochelin) CLASSIFICATION #superfamily ferrienterochelin receptor; tonB-dependent !1receptor amino-terminal homology; tonB-dependent receptor !1carboxyl-terminal homology KEYWORDS iron transport; membrane protein; receptor FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-746 #product ferrienterochelin receptor #status predicted !8#label MAT\ !$66-221 #domain tonB-dependent receptor amino-terminal !8homology #label TNN\ !$435-746 #domain tonB-dependent receptor carboxyl-terminal !8homology #label TNC SUMMARY #length 746 #molecular-weight 82106 #checksum 992 SEQUENCE /// ENTRY QRECIC #type complete TITLE colicin I receptor precursor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Sep-1990 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS B64984; A32056; A33868; A28377; C41871; A35408; S24561 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64984 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-663 ##label BLAT !'##cross-references GB:AE000304; GB:U00096; NID:g1788470; !1PIDN:AAC75216.1; PID:g1788478; UWGP:b2155 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A32056 !$#authors Nau, C.D.; Konisky, J. !$#journal J. Bacteriol. (1989) 171:1041-1047 !$#title Evolutionary relationship between the TonB-dependent outer !1membrane transport proteins: nucleotide and amino acid !1sequences of the Escherichia coli colicin I receptor gene. !$#cross-references MUID:89123100; PMID:2644220 !$#accession A32056 !'##molecule_type DNA !'##residues 1-146,'RCARRCSEYHHQ',159,'NRSEMV',166,'YRYRRYHHSGTSRSR', !1182-527,'N',529-613,'HLE',661-662,'RGLAGD' ##label NA1 !'##note the authors translated the codon AAT for residue 528 as Ile REFERENCE A33868 !$#authors Nau, C.D.; Konisky, J. !$#journal J. Bacteriol. (1989) 171:4530 !$#contents corrections !$#accession A33868 !'##molecule_type DNA !'##residues 144-184;610-663 ##label NA2 REFERENCE A28377 !$#authors Griggs, D.W.; Tharp, B.B.; Konisky, J. !$#journal J. Bacteriol. (1987) 169:5343-5352 !$#title Cloning and promoter identification of the iron-regulated !1cir gene of Escherichia coli. !$#cross-references MUID:88058737; PMID:3316180 !$#accession A28377 !'##molecule_type DNA !'##residues 1-59 ##label GRI !'##cross-references GB:M19295; NID:g145545; PIDN:AAA23581.1; !1PID:g551794 !'##note residues 26-45 were confirmed by protein sequencing REFERENCE A41871 !$#authors Steffes, C.; Ellis, J.; Wu, J.; Rosen, B.P. !$#journal J. Bacteriol. (1992) 174:3242-3249 !$#title The lysP gene encodes the lysine-specific permease. !$#cross-references MUID:92250419; PMID:1315732 !$#accession C41871 !'##status preliminary !'##molecule_type DNA !'##residues 1-96,'D',98-125 ##label STE !'##cross-references GB:M89774; NID:g466776; PIDN:AAA17054.1; !1PID:g466779; EMBL:X65029 REFERENCE A35408 !$#authors Griggs, D.W.; Kafka, K.; Nau, C.D.; Konisky, J. !$#journal J. Bacteriol. (1990) 172:3529-3533 !$#title Activation of expression of the Escherichia coli cir gene by !1an iron-independent regulatory mechanism involving cyclic !1AMP-cyclic AMP receptor protein complex. !$#cross-references MUID:90264362; PMID:2160948 !$#accession A35408 !'##status preliminary !'##molecule_type DNA !'##residues 1-21 ##label GR2 COMMENT This outer membrane receptor for colicins Ia and Ib is !1regulated by both cellular iron content and growth !1temperature; it shares many structural characteristics of !1the tonB-dependent outer membrane transport proteins. GENETICS !$#gene cir; cirA; feuA !$#map_position 43 min CLASSIFICATION #superfamily ferrienterochelin receptor; tonB-dependent !1receptor amino-terminal homology; tonB-dependent receptor !1carboxyl-terminal homology KEYWORDS iron transport; membrane protein FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-624 #product colicin I receptor #status experimental !8#label MAT\ !$66-211 #domain tonB-dependent receptor amino-terminal !8homology #label TNN\ !$365-663 #domain tonB-dependent receptor carboxyl-terminal !8homology #label TNC SUMMARY #length 663 #molecular-weight 73895 #checksum 3522 SEQUENCE /// ENTRY QRECFE #type complete TITLE ferrichrome-iron receptor precursor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS F64738; A25196; S45219; S06358 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64738 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-747 ##label BLAT !'##cross-references GB:AE000124; GB:U00096; NID:g1786339; !1PIDN:AAC73261.1; PID:g1786344; UWGP:b0150 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A25196 !$#authors Coulton, J.W.; Mason, P.; Cameron, D.R.; Carmel, G.; Jean, !1R.; Rode, H.N. !$#journal J. Bacteriol. (1986) 165:181-192 !$#title Protein fusions of beta-galactosidase to the !1ferrichrome-iron receptor of Escherichia coli K-12. !$#cross-references MUID:86085668; PMID:3079747 !$#accession A25196 !'##molecule_type DNA !'##residues 1-608,'RP',611-747 ##label COU !'##cross-references GB:D26562; NID:g473770; PIDN:BAA05598.1; !1PID:g473809 !'##experimental_source strain K-12 REFERENCE S45181 !$#authors Fujita, N. !$#submission submitted to the EMBL Data Library, January 1994 !$#accession S45219 !'##molecule_type DNA !'##residues 1-608,'RP',611-747 ##label FUJ !'##cross-references EMBL:D26562; NID:g473770; PIDN:BAA05598.1; !1PID:g473809 !'##experimental_source strain K-12, substrain W3110 REFERENCE A32650 !$#authors Burkhardt, R.; Braun, V. !$#journal Mol. Gen. Genet. (1987) 209:49-55 !$#title Nucleotide sequence of the fhuC and fhuD genes involved in !1iron (III) hydroxamate transport: domains in FhuC homologous !1to ATP-binding proteins. !$#cross-references MUID:88038363; PMID:2823072 !$#accession S06358 !'##molecule_type DNA !'##residues 723-747 ##label BUR !'##cross-references EMBL:X05810 GENETICS !$#gene fhuA; tonA !$#map_position 4 min FUNCTION !$#description located in the outer membrane, binds the ferrichrome-iron !1ligand; interacts with the tonB protein, which is !1responsible for energy coupling of the ferrichrome-promoted !1iron transport system CLASSIFICATION #superfamily ferrichrome-iron receptor; tonB-dependent !1receptor amino-terminal homology; tonB-dependent receptor !1carboxyl-terminal homology KEYWORDS iron transport; membrane protein FEATURE !$1-33 #domain signal sequence #status predicted #label SIG\ !$34-747 #product ferrichrome-iron receptor #status predicted !8#label MAT\ !$98-235 #domain tonB-dependent receptor amino-terminal !8homology #label TNN\ !$468-747 #domain tonB-dependent receptor carboxyl-terminal !8homology #label TNC SUMMARY #length 747 #molecular-weight 82182 #checksum 3376 SEQUENCE /// ENTRY XMECFB #type complete TITLE flagellar transcription activator flbB - Escherichia coli (strain K-12) ALTERNATE_NAMES flagellar transcriptional activator FlhD ORGANISM #formal_name Escherichia coli DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 01-Mar-2002 ACCESSIONS A27735; D64952 REFERENCE A91867 !$#authors Bartlett, D.H.; Frantz, B.B.; Matsumura, P. !$#journal J. Bacteriol. (1988) 170:1575-1581 !$#title Flagellar transcriptional activators flbB and flaI: gene !1sequences and 5' consensus sequences of operons under FlbB !1and FlaI control. !$#cross-references MUID:88169478; PMID:2832369 !$#accession A27735 !'##molecule_type DNA !'##residues 1-119 ##label BAR !'##cross-references GB:M19439; NID:g145982; PIDN:AAA23787.1; !1PID:g145983 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64952 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-119 ##label BLAT !'##cross-references GB:AE000283; GB:U00096; NID:g1788200; !1PIDN:AAC74962.1; PID:g1788202; UWGP:b1892 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene flhD; flbB !$#map_position 42 min !$#start_codon GTG CLASSIFICATION #superfamily activator flbB KEYWORDS chemotaxis; DNA binding; flagellum; transcription regulation SUMMARY #length 119 #molecular-weight 13618 #checksum 2685 SEQUENCE /// ENTRY XMECIF #type complete TITLE flagellar transcription activator flaI - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1989 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS C64952; B27735 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64952 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-192 ##label BLAT !'##cross-references GB:AE000283; GB:U00096; NID:g1788200; !1PIDN:AAC74961.1; PID:g1788201; UWGP:b1891 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A91867 !$#authors Bartlett, D.H.; Frantz, B.B.; Matsumura, P. !$#journal J. Bacteriol. (1988) 170:1575-1581 !$#title Flagellar transcriptional activators flbB and flaI: gene !1sequences and 5' consensus sequences of operons under FlbB !1and FlaI control. !$#cross-references MUID:88169478; PMID:2832369 !$#accession B27735 !'##molecule_type DNA !'##residues 1-148,'D',150-192 ##label BAR !'##cross-references GB:M19439; NID:g145982; PIDN:AAA23788.1; !1PID:g145984 GENETICS !$#gene flhC; flaI !$#map_position 42 min CLASSIFICATION #superfamily activator flaI KEYWORDS chemotaxis; DNA binding; flagellum; transcription regulation SUMMARY #length 192 #molecular-weight 21566 #checksum 5447 SEQUENCE /// ENTRY XMECII #type complete TITLE flagellar motor switch protein fliN - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 01-Mar-2002 ACCESSIONS JS0111; G64958 REFERENCE PS0027 !$#authors Malakooti, J.; Komeda, Y.; Matsumura, P. !$#journal J. Bacteriol. (1989) 171:2728-2734 !$#title DNA sequence analysis, gene product identification, and !1localization of flagellar motor components of Escherichia !1coli. !$#cross-references MUID:89213963; PMID:2651416 !$#accession JS0111 !'##molecule_type DNA !'##residues 1-137 ##label MAL !'##cross-references GB:M26294; NID:g341453; PIDN:AAA03207.1; !1PID:g414721 !'##experimental_source strain K12 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64958 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-137 ##label BLAT !'##cross-references GB:AE000286; GB:U00096; NID:g1788241; !1PIDN:AAC75013.1; PID:g1788256; UWGP:b1946 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene fliN; flaAII !$#map_position 43 min FUNCTION !$#description part of the flagellar switch mediating flagella rotation !1during chemotaxis; also involved in energy transduction and !1flagellar assembly !$#note there are three switch proteins (fliG, fliM, fliN) which !1together determine the direction of rotation CLASSIFICATION #superfamily flagellar motor switch protein KEYWORDS chemotaxis; flagellar rotation; flagellum; membrane protein SUMMARY #length 137 #molecular-weight 14855 #checksum 2706 SEQUENCE /// ENTRY A30929 #type complete TITLE flagellar motor switch protein fliG - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A44513; A42364; A30929 REFERENCE A44513 !$#authors Kihara, M.; Homma, M.; Kutsukake, K.; Macnab, R.M. !$#journal J. Bacteriol. (1989) 171:3247-3257 !$#title Flagellar switch of Salmonella typhimurium: gene sequences !1and deduced protein sequences. !$#cross-references MUID:89255090; PMID:2656645 !$#accession A44513 !'##status preliminary !'##molecule_type DNA !'##residues 1-331 ##label KIH !'##cross-references EMBL:M24462; NID:g154022; PIDN:AAA27097.1; !1PID:g154024 REFERENCE A42364 !$#authors Vogler, A.P.; Homma, M.; Irikura, V.M.; Macnab, R.M. !$#journal J. Bacteriol. (1991) 173:3564-3572 !$#title Salmonella typhimurium mutants defective in flagellar !1filament regrowth and sequence similarity of fliI to F-0F-1, !1vacuolar, and archaebacterial ATPase subunits. !$#cross-references MUID:91258342; PMID:1646201 !$#accession A42364 !'##status preliminary !'##molecule_type DNA !'##residues 297-331 ##label VOG !'##cross-references GB:M62408; NID:g154026; PIDN:AAA27099.1; !1PID:g154027 GENETICS !$#gene fliG; formerly flaAII.2 !$#map_position 40 min FUNCTION !$#description part of the flagellar switch mediating flagella rotation !1during chemotaxis !$#note there are three switch proteins (fliG, fliM, fliN) which !1together determine the direction of rotation; fliG-fliM !1interaction plays a central role in switching CLASSIFICATION #superfamily flagellar switch protein fliG KEYWORDS chemotaxis; flagellar rotation; flagellum SUMMARY #length 331 #molecular-weight 36851 #checksum 6301 SEQUENCE /// ENTRY B42365 #type complete TITLE flagellar motor switch protein fliG - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS B42365; C69624; S14495 REFERENCE A42365 !$#authors Albertini, A.M.; Caramori, T.; Crabb, W.D.; Scoffone, F.; !1Galizzi, A. !$#journal J. Bacteriol. (1991) 173:3573-3579 !$#title The flaA locus of Bacillus subtilis is part of a large !1operon coding for flagellar structures, motility functions, !1and an ATPase-like polypeptide. !$#cross-references MUID:91258343; PMID:1828465 !$#accession B42365 !'##molecule_type DNA !'##residues 1-338 ##label ALB !'##cross-references EMBL:X56049; NID:g39904; PIDN:CAA39521.1; !1PID:g39905 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69624 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-338 ##label KUN !'##cross-references GB:Z99112; GB:AL009126; NID:g2633902; !1PIDN:CAB13495.1; PID:g2633994 !'##experimental_source strain 168 GENETICS !$#gene fliG CLASSIFICATION #superfamily flagellar switch protein fliG KEYWORDS flagellar rotation SUMMARY #length 338 #molecular-weight 38191 #checksum 6265 SEQUENCE /// ENTRY H64563 #type complete TITLE flagellar motor switch protein - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS H64563 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession H64563 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-343 ##label TOM !'##cross-references GB:AE000552; GB:AE000511; NID:g2313451; !1PIDN:AAD07420.1; PID:g2313453; TIGR:HP0352 CLASSIFICATION #superfamily flagellar switch protein fliG SUMMARY #length 343 #molecular-weight 38326 #checksum 9038 SEQUENCE /// ENTRY SMEBH1 #type complete TITLE flagellar hook-associated protein 1 - Salmonella typhimurium ALTERNATE_NAMES HAP1 protein ORGANISM #formal_name Salmonella typhimurium DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS S10366; S15358 REFERENCE S10361 !$#authors Homma, M.; DeRosier, D.J.; Macnab, R.M. !$#journal J. Mol. Biol. (1990) 213:819-832 !$#title Flagellar hook and hook-associated proteins of Salmonella !1typhimurium and their relationship to other axial components !1of the flagellum. !$#cross-references MUID:90294298; PMID:2193164 !$#accession S10366 !'##molecule_type DNA !'##residues 1-553 ##label HOM !'##cross-references EMBL:X51738; NID:g47678; PIDN:CAA36025.1; !1PID:g47679 REFERENCE S15353 !$#authors Jones, C.J.; Macnab, R.M.; Okino, H.; Aizawa, S.I. !$#journal J. Mol. Biol. (1990) 212:377-387 !$#title Stoichiometric analysis of the flagellar hook-(basal-body) !1complex of Salmonella typhimurium. !$#cross-references MUID:90204563; PMID:2181149 !$#accession S15358 !'##molecule_type protein !'##residues 2-5 ##label JON GENETICS !$#gene flgK !$#map_position 23 min FUNCTION !$#description connects the flagellar filament to the hook and is required !1for the last stage of flagellar assembly CLASSIFICATION #superfamily flagellar hook-associated protein 1 KEYWORDS flagellum FEATURE !$2-553 #product flagellar hook-associated protein 1 #status !8experimental #label MAT SUMMARY #length 553 #molecular-weight 59109 #checksum 2389 SEQUENCE /// ENTRY RGECA #type complete TITLE arabinose operon transcription regulator - Escherichia coli (strain K-12) ALTERNATE_NAMES arabinose operon regulatory protein ORGANISM #formal_name Escherichia coli DATE 31-Mar-1981 #sequence_revision 31-Mar-1981 #text_change 01-Mar-2002 ACCESSIONS A91473; A93712; S40580; A17248; H64727; I41135; A03554 REFERENCE A91473 !$#authors Wallace, R.G.; Lee, N.; Fowler, A.V. !$#journal Gene (1980) 12:179-190 !$#title The araC gene of Escherichia coli: transcriptional and !1translational start-points and complete nucleotide sequence. !$#cross-references MUID:81237780; PMID:7019009 !$#accession A91473 !'##molecule_type DNA !'##residues 1-292 ##label WAL !'##cross-references GB:V00256; NID:g40935; PIDN:CAA23507.1; PID:g40936 !'##experimental_source strain B/r REFERENCE A93712 !$#authors Miyada, C.G.; Horwitz, A.H.; Cass, L.G.; Timko, J.; Wilcox, !1G. !$#journal Nucleic Acids Res. (1980) 8:5267-5274 !$#title DNA sequence of the araC regulatory gene from Escherichia !1coli B/r. !$#cross-references MUID:81124262; PMID:7008027 !$#accession A93712 !'##molecule_type DNA !'##residues 1-292 ##label MIY !'##cross-references GB:V00256; NID:g40935; PIDN:CAA23507.1; PID:g40936 !'##experimental_source strain B/r REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40580 !'##status preliminary !'##molecule_type DNA !'##residues 1-292 ##label YUR !'##cross-references EMBL:D10483; NID:g216434; PIDN:BAA01335.1; !1PID:g216484 REFERENCE A17248 !$#authors Stoner, C.M.; Schleif, R. !$#journal J. Mol. Biol. (1982) 154:649-652 !$#title Is the amino acid but not the nucleotide sequence of the !1Escherichia coli araC gene conserved?. !$#cross-references MUID:82216830; PMID:6283093 !$#accession A17248 !'##molecule_type DNA !'##residues 1-292 ##label STO !'##cross-references GB:V00259; NID:g40949; PIDN:CAA23508.1; PID:g808965 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64727 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-292 ##label BLAT !'##cross-references GB:AE000117; GB:U00096; NID:g1786250; !1PIDN:AAC73175.1; PID:g1786251; UWGP:b0064 !'##experimental_source strain K-12, substrain MG1655 REFERENCE I41135 !$#authors Cass, L.G.; Horwitz, A.H.; Miyada, C.G.; Greenfield, L.; !1Wilcox, G. !$#journal Mol. Gen. Genet. (1980) 180:219-226 !$#title The araC regulatory gene mRNA contains a leader sequence. !$#cross-references MUID:81074345; PMID:6160371 !$#accession I41135 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-6,'E',8-61 ##label RES !'##cross-references GB:K01303; NID:g145317; PIDN:AAA23468.1; !1PID:g145318 GENETICS !$#gene araC !$#map_position 1 min FUNCTION !$#description controls the expression of at least six genes that are !1involved in the transport and catabolism of L-arabinose; !1regulates initiation of transcription of the araBAD operon; !1controls its own synthesis CLASSIFICATION #superfamily arabinose operon regulatory protein KEYWORDS DNA binding; homodimer; transcription regulation FEATURE !$197-216 #region helix-turn-helix motif SUMMARY #length 292 #molecular-weight 33384 #checksum 4061 SEQUENCE /// ENTRY RGEBAT #type complete TITLE arabinose operon regulatory protein - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 02-Apr-1982 #sequence_revision 13-Jun-1983 #text_change 16-Jul-1999 ACCESSIONS A03555 REFERENCE A03555 !$#authors Clarke, P.; Lin, H.C.; Wilcox, G. !$#journal Gene (1982) 18:157-163 !$#title The nucleotide sequence of the araC regulatory gene in !1Salmonella typhimurium LT2. !$#cross-references MUID:83028530; PMID:6751938 !$#accession A03555 !'##molecule_type DNA !'##residues 1-281 ##label CLA !'##cross-references GB:J01797; NID:g153870; PIDN:AAA27026.1; !1PID:g153871 !'##experimental_source strain LT2 GENETICS !$#gene araC !$#map_position 2 FUNCTION !$#description controls the expression of at least six genes that are !1involved in the transport and catabolism of L-arabinose; !1regulates initiation of transcription of the araBAD operon; !1controls its own synthesis !$#pathway arabinose catabolism CLASSIFICATION #superfamily arabinose operon regulatory protein KEYWORDS DNA binding; homodimer; transcription regulation FEATURE !$197-216 #region helix-turn-helix motif SUMMARY #length 281 #molecular-weight 32070 #checksum 5285 SEQUENCE /// ENTRY RGECMB #type complete TITLE melibiose operon regulatory protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 20-Jan-2003 ACCESSIONS A29625; S56347; E65221 REFERENCE A29625 !$#authors Webster, C.; Kempsell, K.; Booth, I.; Busby, S. !$#journal Gene (1987) 59:253-263 !$#title Organisation of the regulatory region of the Escherichia !1coli melibiose operon. !$#cross-references MUID:88137961; PMID:2830169 !$#accession A29625 !'##molecule_type DNA !'##residues 1-302 ##label WEB REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56347 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-302 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97018.1; !1PID:g536963 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65221 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-302 ##label BLAT !'##cross-references GB:AE000484; GB:U00096; NID:g2367352; !1PIDN:AAC77079.1; PID:g1790559; UWGP:b4118 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene melR !$#map_position 93 min FUNCTION !$#description may be a melibiose-induced activator for the melibiose !1operon promoter or it may in some other ways facilitate !1melibiose-dependent gene expression; however, its exact !1function is not yet define CLASSIFICATION #superfamily melibiose operon regulatory protein KEYWORDS DNA binding; transcription regulation SUMMARY #length 302 #molecular-weight 34928 #checksum 4357 SEQUENCE /// ENTRY RGEBHD #type complete TITLE mercuric resistance operon regulatory protein merP precursor - Shigella flexneri plasmid R100 ALTERNATE_NAMES mercuric-ion-binding protein; mercury scavenger protein ORGANISM #formal_name Shigella flexneri DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 16-Jul-1999 ACCESSIONS A03556 REFERENCE A03556 !$#authors Misra, T.K.; Brown, N.L.; Fritzinger, D.C.; Pridmore, R.D.; !1Barnes, W.M.; Haberstroh, L.; Silver, S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:5975-5979 !$#title Mercuric ion-resistance operons of plasmid R100 and !1transposon Tn501: the beginning of the operon including the !1regulatory region and the first two structural genes. !$#cross-references MUID:85014891; PMID:6091128 !$#accession A03556 !'##molecule_type DNA !'##residues 1-91 ##label MIS !'##cross-references GB:J01730; NID:g151742; PIDN:AAA92262.1; !1PID:g151751 GENETICS !$#gene merP; merC !$#genome plasmid CLASSIFICATION #superfamily mercuric resistance operon regulatory protein; !1heavy-metal-associated homology KEYWORDS mercury transport; metal binding; periplasmic space FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-91 #product mercuric resistance operon regulatory !8protein merP #status predicted #label MAT\ !$28-57 #domain heavy-metal-associated homology #label HMA\ !$33,36 #binding_site mercury (Cys) #status predicted SUMMARY #length 91 #molecular-weight 9414 #checksum 1936 SEQUENCE /// ENTRY S09524 #type complete TITLE mercuric resistance operon regulatory protein precursor - plasmid NR1 ALTERNATE_NAMES mercuric-ion-binding protein; mercury scavenger protein ORGANISM #formal_name plasmid NR1 DATE 16-Oct-1998 #sequence_revision 16-Oct-1998 #text_change 16-Jul-1999 ACCESSIONS S09524 REFERENCE S07447 !$#authors Barrineau, P.; Gilbert, P.; Jackson, W.J.; Jones, C.S.; !1Summers, A.O.; Wisdom, S. !$#journal J. Mol. Appl. Genet. (1984) 2:601-619 !$#title The DNA sequence of the mercury resistance operon of the !1IncFII plasmid NR1. !$#cross-references MUID:85159407; PMID:6530603 !$#accession S09524 !'##molecule_type DNA !'##residues 1-91 ##label BAR !'##cross-references EMBL:K03089; NID:g150389; PIDN:AAB59076.1; !1PID:g150394 GENETICS !$#gene merTB !$#genome plasmid CLASSIFICATION #superfamily mercuric resistance operon regulatory protein; !1heavy-metal-associated homology KEYWORDS mercury transport; metal binding; periplasmic space FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-91 #product mercuric resistance operon regulatory !8protein #status predicted #label MAT\ !$28-57 #domain heavy-metal-associated homology #label HMA\ !$33,36 #binding_site mercury (Cys) #status predicted SUMMARY #length 91 #molecular-weight 9428 #checksum 1987 SEQUENCE /// ENTRY RGPSHA #type complete TITLE mercuric resistance operon regulatory protein merP precursor - Pseudomonas aeruginosa transposon Tn501 ALTERNATE_NAMES mercuric-ion-binding protein; mercury scavenger protein ORGANISM #formal_name Pseudomonas aeruginosa DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 16-Jul-1999 ACCESSIONS A03557 REFERENCE A03556 !$#authors Misra, T.K.; Brown, N.L.; Fritzinger, D.C.; Pridmore, R.D.; !1Barnes, W.M.; Haberstroh, L.; Silver, S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:5975-5979 !$#title Mercuric ion-resistance operons of plasmid R100 and !1transposon Tn501: the beginning of the operon including the !1regulatory region and the first two structural genes. !$#cross-references MUID:85014891; PMID:6091128 !$#accession A03557 !'##molecule_type DNA !'##residues 1-91 ##label MIS !'##cross-references GB:K02503; NID:g154897; PIDN:AAA27434.1; !1PID:g154900 GENETICS !$#gene merP; merC CLASSIFICATION #superfamily mercuric resistance operon regulatory protein; !1heavy-metal-associated homology KEYWORDS mercury transport; metal binding; periplasmic space FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-91 #product mercuric resistance operon regulatory !8protein merP #status predicted #label MAT\ !$28-57 #domain heavy-metal-associated homology #label HMA\ !$33,36 #binding_site mercury (Cys) #status predicted SUMMARY #length 91 #molecular-weight 9491 #checksum 3731 SEQUENCE /// ENTRY C33858 #type complete TITLE mercuric resistance operon regulatory protein merP precursor - Serratia marcescens plasmid pDU1358 ALTERNATE_NAMES mercuric-ion-binding protein; mercury scavenger protein ORGANISM #formal_name Serratia marcescens DATE 09-Mar-1990 #sequence_revision 09-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS C33858; S21200 REFERENCE A33858 !$#authors Nucifora, G.; Chu, L.; Silver, S.; Misra, T.K. !$#journal J. Bacteriol. (1989) 171:4241-4247 !$#title Mercury operon regulation by the merR gene of the !1organomercurial resistance system of plasmid pDU1358. !$#cross-references MUID:89327136; PMID:2666393 !$#accession C33858 !'##status preliminary !'##molecule_type DNA !'##residues 1-91 ##label NUC !'##cross-references GB:M24940; NID:g150631; PIDN:AAA98223.1; !1PID:g150634 REFERENCE S21200 !$#authors Sahlman, L.; Jonsson, B.H. !$#journal Eur. J. Biochem. (1992) 205:375-381 !$#title Purification and properties of the mercuric-ion-binding !1protein MerP. !$#cross-references MUID:92209527; PMID:1555597 !$#accession S21200 !'##molecule_type protein !'##residues 20-24 ##label SAH !'##experimental_source plasmid cloned in Escherichia coli GENETICS !$#gene merP !$#genome plasmid CLASSIFICATION #superfamily mercuric resistance operon regulatory protein; !1heavy-metal-associated homology KEYWORDS mercury transport; metal binding; periplasmic space FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-91 #product mercuric resistance operon regulatory !8protein merP #status predicted #label MAT\ !$28-57 #domain heavy-metal-associated homology #label HMA\ !$33,36 #binding_site mercury (Cys) #status predicted SUMMARY #length 91 #molecular-weight 9548 #checksum 4361 SEQUENCE /// ENTRY S70144 #type complete TITLE mercuric resistance operon regulatory protein merP precursor - Xanthomonas sp. plasmid RP1 tranposon Tn5053 ALTERNATE_NAMES mercuric-ion-binding protein; mercury scavenger protein ORGANISM #formal_name Xanthomonas sp. DATE 16-Oct-1998 #sequence_revision 16-Oct-1998 #text_change 16-Jul-1999 ACCESSIONS S70144 REFERENCE S70140 !$#authors Kholodii, G.Y.; Mindlin, S.Z.; Bass, I.A.; Yurieva, O.V.; !1Minakhina, S.V.; Nikiforov, V.G. !$#journal Mol. Microbiol. (1995) 17:1189-1200 !$#title Four genes, two ends, and a res region are involved in !1transposition of Tn5053: a paradigm for a novel family of !1transposons carrying either a mer operon or an integron. !$#cross-references MUID:96130850; PMID:8594337 !$#accession S70144 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-91 ##label KHO !'##cross-references EMBL:L40585; NID:g710572; PIDN:AAA98324.1; !1PID:g710577 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1May 1995 GENETICS !$#gene merP !$#genome plasmid CLASSIFICATION #superfamily mercuric resistance operon regulatory protein; !1heavy-metal-associated homology KEYWORDS mercury transport; metal binding; periplasmic space FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-91 #product mercuric resistance operon regulatory !8protein merP #status predicted #label MAT\ !$28-57 #domain heavy-metal-associated homology #label HMA\ !$33,36 #binding_site mercury (Cys) #status predicted SUMMARY #length 91 #molecular-weight 9487 #checksum 3917 SEQUENCE /// ENTRY A64654 #type complete TITLE heavy-metal-binding protein HP1073 - Helicobacter pylori (strains 26695 and others) ALTERNATE_NAMES copper-ion-binding protein copP homolog ORGANISM #formal_name Helicobacter pylori DATE 16-Oct-1998 #sequence_revision 16-Oct-1998 #text_change 16-Jul-1999 ACCESSIONS A64654; S60900 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession A64654 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-66 ##label TOM !'##cross-references GB:AE000614; GB:AE000511; NID:g2314216; !1PIDN:AAD08120.1; PID:g2314224; TIGR:HP1073 !'##experimental_source strain 26695 REFERENCE S60899 !$#authors Ge, Z.; Hiratsuka, K.; Taylor, D.E. !$#journal Mol. Microbiol. (1995) 15:97-106 !$#title Nucleotide sequence and mutational analysis indicate that !1two Helicobacter pylori genes encode a P-type ATPase and a !1cation-binding protein associated with copper transport. !$#cross-references MUID:95272397; PMID:7752900 !$#accession S60900 !'##status preliminary !'##molecule_type DNA !'##residues 1-2,'V',4-12,'S',14-33,'AN',36-65,'I' ##label GEZ !'##cross-references EMBL:L33259; NID:g1518875; PIDN:AAB67321.1; !1PID:g495029 !'##experimental_source strain UA802, NCTC 11639 GENETICS !$#gene copP; HP1073 CLASSIFICATION #superfamily mercuric resistance operon regulatory protein; !1heavy-metal-associated homology KEYWORDS metal binding FEATURE !$7-36 #domain heavy-metal-associated homology #label HMA\ !$12,15 #binding_site transition metal ions (Cys) #status !8predicted SUMMARY #length 66 #molecular-weight 7196 #checksum 7534 SEQUENCE /// ENTRY B56085 #type complete TITLE copper homeostasis operon regulatory protein copZ - Enterococcus hirae ORGANISM #formal_name Enterococcus hirae DATE 16-Oct-1998 #sequence_revision 16-Oct-1998 #text_change 16-Jul-1999 ACCESSIONS B56085 REFERENCE A56085 !$#authors Odermatt, A.; Solioz, M. !$#journal J. Biol. Chem. (1995) 270:4349-4354 !$#title Two trans-acting metalloregulatory proteins controlling !1expression of the copper-ATPases of Enterococcus hirae. !$#cross-references MUID:95181419; PMID:7876197 !$#accession B56085 !'##molecule_type DNA !'##residues 1-69 ##label ODE !'##cross-references GB:Z46807; NID:g662918; PIDN:CAA86836.1; !1PID:g662921 GENETICS !$#gene copZ FUNCTION !$#description required for induction by copper of the cop operon, !1including the copA (see PIR:A45995) and copB (see !1PIR:B45995) ATPases; copZ acts as an antirepressor, perhaps !1by binding to the transcription repressor copY (see !1PIR:A56085) and releasing it from the promoter region CLASSIFICATION #superfamily mercuric resistance operon regulatory protein; !1heavy-metal-associated homology KEYWORDS metal binding; transcription regulation FEATURE !$7-36 #domain heavy-metal-associated homology #label HMA\ !$12,15 #binding_site copper (Cys) #status predicted SUMMARY #length 69 #molecular-weight 7653 #checksum 524 SEQUENCE /// ENTRY H64059 #type complete TITLE probable mercuric ion-binding protein HI0292 - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES periplasmic mercuric ion-binding protein merP homolog ORGANISM #formal_name Haemophilus influenzae DATE 16-Oct-1998 #sequence_revision 16-Oct-1998 #text_change 16-Jul-1999 ACCESSIONS H64059 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession H64059 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-68 ##label TIGR !'##cross-references GB:U32715; GB:L42023; NID:g1573254; !1PIDN:AAC21956.1; PID:g1573260; TIGR:HI0292 CLASSIFICATION #superfamily mercuric resistance operon regulatory protein; !1heavy-metal-associated homology KEYWORDS metal binding FEATURE !$8-37 #domain heavy-metal-associated homology #label HMA\ !$13,16 #binding_site mercury (Cys) #status predicted SUMMARY #length 68 #molecular-weight 7351 #checksum 9779 SEQUENCE /// ENTRY F64005 #type complete TITLE probable mercuric ion-binding protein HI0291 - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES periplasmic mercuric ion-binding protein merP homolog ORGANISM #formal_name Haemophilus influenzae DATE 16-Oct-1998 #sequence_revision 16-Oct-1998 #text_change 16-Jul-1999 ACCESSIONS F64005 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession F64005 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-68 ##label TIGR !'##cross-references GB:U32715; GB:L42023; NID:g1573254; !1PIDN:AAC21964.1; PID:g1573259; TIGR:HI0291 CLASSIFICATION #superfamily mercuric resistance operon regulatory protein; !1heavy-metal-associated homology KEYWORDS metal binding FEATURE !$8-37 #domain heavy-metal-associated homology #label HMA\ !$13,16 #binding_site mercury (Cys) #status predicted SUMMARY #length 68 #molecular-weight 7378 #checksum 9684 SEQUENCE /// ENTRY F70041 #type complete TITLE probable mercuric ion-binding protein yvgY - Bacillus subtilis ALTERNATE_NAMES periplasmic mercuric ion-binding protein merP homolog ORGANISM #formal_name Bacillus subtilis DATE 16-Oct-1998 #sequence_revision 16-Oct-1998 #text_change 16-Jun-2000 ACCESSIONS F70041 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F70041 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-69 ##label KUN !'##cross-references GB:Z99121; GB:AL009126; NID:g2635827; !1PIDN:CAB15356.1; PID:g2635864 !'##experimental_source strain 168 GENETICS !$#gene yvgY CLASSIFICATION #superfamily mercuric resistance operon regulatory protein; !1heavy-metal-associated homology KEYWORDS metal binding FEATURE !$8-37 #domain heavy-metal-associated homology #label HMA\ !$13,16 #binding_site mercury (Cys) #status predicted SUMMARY #length 69 #molecular-weight 7338 #checksum 393 SEQUENCE /// ENTRY BVECAR #type complete TITLE arsenical resistance operon repressor - Escherichia coli plasmid R773 ORGANISM #formal_name Escherichia coli DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS JS0448 REFERENCE JS0448 !$#authors San Francisco, M.J.D.; Hope, C.L.; Owolabi, J.B.; Tisa, !1L.S.; Rosen, B.P. !$#journal Nucleic Acids Res. (1990) 18:619-624 !$#title Identification of the metalloregulatory element of the !1plasmid-encoded arsenical resistance operon. !$#cross-references MUID:90174986; PMID:2408017 !$#accession JS0448 !'##molecule_type DNA !'##residues 1-117 ##label SAN !'##cross-references GB:X16045; NID:g42716; PIDN:CAA34168.1; PID:g42717 COMMENT This is a transcriptional repressor for the ars operon; it !1is a trans-acting regulatory protein which controls its own !1expression. GENETICS !$#gene arsR !$#genome plasmid CLASSIFICATION #superfamily arsenical resistance operon repressor KEYWORDS DNA binding; homodimer; repressor; transcription regulation SUMMARY #length 117 #molecular-weight 13198 #checksum 2047 SEQUENCE /// ENTRY B41903 #type complete TITLE arsenical resistance operon repressor - Staphylococcus aureus plasmid pI258 ORGANISM #formal_name Staphylococcus aureus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS B41903 REFERENCE A41903 !$#authors Ji, G.; Silver, S. !$#journal J. Bacteriol. (1992) 174:3684-3694 !$#title Regulation and expression of the arsenic resistance operon !1from Staphylococcus aureus plasmid pI258. !$#cross-references MUID:92276351; PMID:1534328 !$#accession B41903 !'##molecule_type DNA !'##residues 1-104 ##label JI1 !'##cross-references GB:M86824; NID:g150725; PIDN:AAA25636.1; !1PID:g150727 !'##note sequence extracted from NCBI backbone (NCBIN:104669, !1NCBIP:104671) COMMENT This is a transcriptional repressor for the ars operon; it !1is a trans-acting regulatory protein which controls its own !1expression. GENETICS !$#gene arsR !$#genome plasmid CLASSIFICATION #superfamily arsenical resistance operon repressor KEYWORDS DNA binding; homodimer; repressor; transcription regulation SUMMARY #length 104 #molecular-weight 11863 #checksum 241 SEQUENCE /// ENTRY A41902 #type complete TITLE arsenical resistance operon repressor - Staphylococcus xylosus plasmid pSX267 ORGANISM #formal_name Staphylococcus xylosus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 03-Feb-1994 ACCESSIONS A41902 REFERENCE A41902 !$#authors Rosenstein, R.; Peschel, A.; Wieland, B.; Gotz, F. !$#journal J. Bacteriol. (1992) 174:3676-3683 !$#title Expression and regulation of the antimonite, arsenite, and !1arsenate resistance operon of Staphylococcus xylosus plasmid !1pSX267. !$#cross-references MUID:92276350; PMID:1534327 !$#accession A41902 !'##molecule_type DNA !'##residues 1-104 ##label ROS !'##cross-references GB:M80565 !'##note sequence extracted from NCBI backbone (NCBIN:104639, !1NCBIP:104642) GENETICS !$#gene arsR !$#genome plasmid CLASSIFICATION #superfamily arsenical resistance operon repressor KEYWORDS DNA binding; homodimer; repressor; transcription regulation SUMMARY #length 104 #molecular-weight 11965 #checksum 9146 SEQUENCE /// ENTRY RGECNX #type complete TITLE nitrate/nitrite sensor protein narX (EC 2.7.3.-) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 30-Jun-1993 #text_change 01-Mar-2002 ACCESSIONS S26137; S04196; JS0117; C64869 REFERENCE S26137 !$#authors Cavicchioli, R.; Gunsalus, R.P. !$#submission submitted to the EMBL Data Library, April 1992 !$#accession S26137 !'##molecule_type DNA !'##residues 1-59 ##label CAV !'##cross-references EMBL:X65715; NID:g42097; PIDN:CAA46631.1; !1PID:g42098 !'##experimental_source strain MC4100 REFERENCE S04195 !$#authors Nohno, T.; Noji, S.; Taniguchi, S.; Saito, T. !$#journal Nucleic Acids Res. (1989) 17:2947-2957 !$#title The narX and narL genes encoding the nitrate-sensing !1regulators of Escherichia coli are homologous to a family of !1prokaryotic two-component regulatory genes. !$#cross-references MUID:89263708; PMID:2657652 !$#accession S04196 !'##molecule_type DNA !'##residues 1-41,'AAPMRST',49,'RDA',53-598 ##label NOH !'##cross-references EMBL:X13360 REFERENCE JS0117 !$#authors Stewart, V.; Parales Jr., J.; Merkel, S.M. !$#journal J. Bacteriol. (1989) 171:2229-2234 !$#title Structure of genes narL and narX of the nar (nitrate !1reductase) locus in Escherichia coli K-12. !$#cross-references MUID:89197802; PMID:2649492 !$#accession JS0117 !'##molecule_type DNA !'##residues 55-373,'G',375-598 ##label STE !'##cross-references GB:M24910; NID:g146922; PIDN:AAA24198.1; !1PID:g146923 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64869 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-598 ##label BLAT !'##cross-references GB:AE000220; GB:U00096; NID:g1787467; !1PIDN:AAC74306.1; PID:g1787474; UWGP:b1222 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene narX !$#map_position 27 min FUNCTION !$#description sensors narX and narQ each communicate nitrate and nitrite !1availability to the response regulators narL and narP; in !1the presence of nitrate, narX protein acts as a positive !1regulator (kinase) of both narL and narP activity; in the !1presence of nitrite, the narX protein acts primarily as a !1negative regulator (phosphatase) of narL activity but !1remains a positive regulator of narP activity !$#note contains P-box element, that is essential for nitrate !1sensing CLASSIFICATION #superfamily nitrate/nitrite sensor protein narX KEYWORDS autophosphorylation; phosphohistidine; phosphoprotein; !1phosphotransferase; sensory transduction; transmembrane !1protein; two-component regulatory system FEATURE !$15-37 #domain transmembrane #status predicted #label TM1\ !$158-174 #domain transmembrane #status predicted #label TM2\ !$399 #active_site His (phosphohistidine intermediate) !8#status predicted SUMMARY #length 598 #molecular-weight 67083 #checksum 1095 SEQUENCE /// ENTRY RGECUB #type complete TITLE sensor protein uhpB (EC 2.7.3.-) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1991 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS E65168; F41853; B26925; S30077 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65168 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-501 ##label BLAT !'##cross-references GB:AE000444; GB:U00096; NID:g2367258; !1PIDN:AAC76691.1; PID:g1790101; UWGP:b3668 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A41853 !$#authors Island, M.D.; Wei, B.Y.; Kadner, R.J. !$#journal J. Bacteriol. (1992) 174:2754-2762 !$#title Structure and function of the uhp genes for the sugar !1phosphate transport system in Escherichia coli and !1Salmonella typhimurium. !$#cross-references MUID:92234930; PMID:1569007 !$#accession F41853 !'##molecule_type DNA !'##residues 2-501 ##label ISL !'##cross-references GB:M89479; NID:g148116; PIDN:AAA24725.1; !1PID:g148118 !'##note the authors did not translate the codon for residue 350 !'##note this is a revision to the sequence from reference A30395 REFERENCE A30395 !$#authors Friedrich, M.J.; Kadner, R.J. !$#journal J. Bacteriol. (1987) 169:3556-3563 !$#title Nucleotide sequence of the uhp region of Escherichia coli. !$#cross-references MUID:87279903; PMID:3301805 !$#accession B26925 !'##molecule_type DNA !'##residues 2-337,'RRQREAERAAHRTTIA',354,'RLRR',359-458,'A',460-462, !1'NKVLASPECAT',474,'NG',477,489,'WHITHF',496,'SA',499, !1'HACQRFSTSTLCLRFDDVAVSESACR' ##label FRI !'##note this sequence has been revised in reference S30076 COMMENT This is one of the proteins involved in the expression of !1uhpT, a gene for hexose phosphate transport. GENETICS !$#gene uhpB !$#map_position 82 CLASSIFICATION #superfamily regulatory protein uhpB KEYWORDS autophosphorylation; phosphohistidine; phosphoprotein; !1phosphotransferase; sugar phosphate transport system; !1transmembrane protein FEATURE !$9-28 #domain transmembrane #status predicted #label TM1\ !$38-57 #domain transmembrane #status predicted #label TM2\ !$79-101 #domain transmembrane #status predicted #label TM3\ !$142-163 #domain transmembrane #status predicted #label TM4\ !$186-205 #domain transmembrane #status predicted #label TM5\ !$211-229 #domain transmembrane #status predicted #label TM6\ !$231-249 #domain transmembrane #status predicted #label TM7\ !$256-274 #domain transmembrane #status predicted #label TM8\ !$314 #active_site His (phosphohistidine intermediate) !8#status predicted SUMMARY #length 501 #molecular-weight 56436 #checksum 1591 SEQUENCE /// ENTRY RGBSDS #type complete TITLE degradative enzyme regulator / competence regulator degS - Bacillus subtilis ALTERNATE_NAMES two-component sensor histidine kinase degS ORGANISM #formal_name Bacillus subtilis DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jun-2000 ACCESSIONS B30191; A30190; B31097; B69614 REFERENCE A30191 !$#authors Henner, D.J.; Yang, M.; Ferrari, E. !$#journal J. Bacteriol. (1988) 170:5102-5109 !$#title Localization of Bacillus subtilis sacU(Hy) mutations to two !1linked genes with similarities to the conserved procaryotic !1family of two-component signalling systems. !$#cross-references MUID:89033891; PMID:3141378 !$#accession B30191 !'##molecule_type DNA !'##residues 1-385 ##label HEN !'##cross-references GB:M23558; NID:g143497; PIDN:AAA22732.1; !1PID:g143498 REFERENCE A30190 !$#authors Kunst, F.; Debarbouille, M.; Msadek, T.; Young, M.; Mauel, !1C.; Karamata, D.; Klier, A.; Rapoport, G.; Dedonder, R. !$#journal J. Bacteriol. (1988) 170:5093-5101 !$#title Deduced polypeptides encoded by the Bacillus subtilis sacU !1locus share homology with two-component sensor-regulator !1systems. !$#cross-references MUID:89033890; PMID:3141377 !$#accession A30190 !'##molecule_type DNA !'##residues 1-385 ##label KUN !'##cross-references GB:M23649; NID:g143500; PIDN:AAA22734.1; !1PID:g143501 REFERENCE A31097 !$#authors Tanaka, T.; Kawata, M. !$#journal J. Bacteriol. (1988) 170:3593-3600 !$#title Cloning and characterization of Bacillus subtilis iep, which !1has positive and negative effects on production of !1extracellular proteases. !$#cross-references MUID:88298669; PMID:3136143 !$#accession B31097 !'##molecule_type DNA !'##residues 253-385 ##label TAN !'##cross-references GB:M21658; NID:g143087; PIDN:AAA22544.1; !1PID:g143088 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69614 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-385 ##label KU2 !'##cross-references GB:Z99122; GB:AL009126; NID:g2636029; !1PIDN:CAB15567.1; PID:g2636076 !'##experimental_source strain 168 COMMENT This protein may be involved in the synthesis of degradative !1enzyme. GENETICS !$#gene degS CLASSIFICATION #superfamily regulatory protein degS KEYWORDS autophosphorylation; phosphohistidine; phosphoprotein FEATURE !$189 #active_site His (phosphohistidine intermediate) !8#status predicted SUMMARY #length 385 #molecular-weight 44957 #checksum 4386 SEQUENCE /// ENTRY XMBSTA #type complete TITLE transcription activator of extracellular enzyme genes tenA - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jun-2000 ACCESSIONS A39184; E69721; I40015 REFERENCE A39184 !$#authors Pang, A.S.H.; Nathoo, S.; Wong, S.L. !$#journal J. Bacteriol. (1991) 173:46-54 !$#title Cloning and characterization of a pair of novel genes that !1regulate production of extracellular enzymes in Bacillus !1subtilis. !$#cross-references MUID:91100316; PMID:1898926 !$#accession A39184 !'##molecule_type DNA !'##residues 1-236 ##label PAN !'##cross-references GB:M37776; GB:M73546; NID:g143728; PIDN:AAA22848.1; !1PID:g143729 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69721 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-236 ##label KUN !'##cross-references GB:Z99110; GB:AL009126; NID:g2633472; !1PIDN:CAB13022.1; PID:g2633519 !'##experimental_source strain 168 COMMENT This protein stimulates production of several extracellular !1enzymes at the transcriptional level. Products of the degS !1and degU genes are required for this effect. GENETICS !$#gene tenA !$#start_codon GTG CLASSIFICATION #superfamily transcription activator tenA KEYWORDS transcription regulation SUMMARY #length 236 #molecular-weight 27416 #checksum 9587 SEQUENCE /// ENTRY RGECDW #type complete TITLE transcription activator of D-serine dehydratase - Escherichia coli ORGANISM #formal_name Escherichia coli DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS A28674 REFERENCE A28674 !$#authors Palchaudhuri, S.; Patel, V.; McFall, E. !$#journal J. Bacteriol. (1988) 170:330-334 !$#title DNA sequence of the D-serine deaminase activator gene dsdC. !$#cross-references MUID:88086890; PMID:3275618 !$#accession A28674 !'##molecule_type DNA !'##residues 1-339 ##label PAL !'##cross-references GB:M19035; NID:g145807; PIDN:AAA23712.1; !1PID:g145809 COMMENT This protein activates transcription of the D-serine !1dehydratase structural gene 700- to 800-fold in the absence !1of cAMP-CAP and 3000- to 5000-fold in the presence of !1cAMP-CAP. GENETICS !$#gene dsdC CLASSIFICATION #superfamily D-serine dehydratase transcription activator KEYWORDS homodimer; transcription regulation; transmembrane protein SUMMARY #length 339 #molecular-weight 39148 #checksum 5503 SEQUENCE /// ENTRY XMBSTI #type complete TITLE regulatory protein tenI - Bacillus subtilis ALTERNATE_NAMES extracellular enzyme genes transcription activator tenI ORGANISM #formal_name Bacillus subtilis DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jun-2000 ACCESSIONS B39184; F69721; I40016 REFERENCE A39184 !$#authors Pang, A.S.H.; Nathoo, S.; Wong, S.L. !$#journal J. Bacteriol. (1991) 173:46-54 !$#title Cloning and characterization of a pair of novel genes that !1regulate production of extracellular enzymes in Bacillus !1subtilis. !$#cross-references MUID:91100316; PMID:1898926 !$#accession B39184 !'##molecule_type DNA !'##residues 1-205 ##label PAN !'##cross-references GB:M73546; GB:M37776; NID:g143728; PIDN:AAA22849.1; !1PID:g143730 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69721 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-205 ##label KUN !'##cross-references GB:Z99110; GB:AL009126; NID:g2633472; !1PIDN:CAB13023.1; PID:g2633520 !'##experimental_source strain 168 COMMENT This protein reduces the stimulatory effect of the tenA !1transcriptional activator on production of certain !1extracellular enzymes. GENETICS !$#gene tenI !$#start_codon GTG CLASSIFICATION #superfamily regulatory protein tenI KEYWORDS transcription regulation SUMMARY #length 205 #molecular-weight 22928 #checksum 6194 SEQUENCE /// ENTRY RGECOR #type complete TITLE osmosensor response regulator ompR - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 05-Apr-1983 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS H65135; A25024; A03560; S40044 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65135 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-239 ##label BLAT !'##cross-references GB:AE000416; GB:U00096; NID:g2367219; !1PIDN:AAC76430.1; PID:g1789809; UWGP:b3405 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A94671 !$#authors Comeau, D.E.; Ikenaka, K.; Tsung, K.; Inouye, M. !$#journal J. Bacteriol. (1985) 164:578-584 !$#title Primary characterization of the protein products of the !1Escherichia coli ompB locus: structure and regulation of !1synthesis of the OmpR and EnvZ proteins. !$#cross-references MUID:86033612; PMID:2997120 !$#accession A25024 !'##molecule_type DNA !'##residues 1-6,'N',8-239 ##label COM !'##experimental_source strain K12 REFERENCE A03560 !$#authors Wurtzel, E.T.; Chou, M.Y.; Inouye, M. !$#journal J. Biol. Chem. (1982) 257:13685-13691 !$#title Osmoregulation of gene expression. I. DNA sequence of the !1ompR gene of the ompB operon of Escherichia coli and !1characterization of its gene product. !$#cross-references MUID:83056871; PMID:6292199 !$#accession A03560 !'##molecule_type DNA !'##residues 1-6,'N',8-210,'WWKKIQRIRVT',232,'R',234,'S',236,'VW',239, !1'TSLYRTALKHEAIALLATKFICPYVIAHRHLAVRQPGDDLSGGAELRDFAEPPAV' !1##label WUR !'##note this sequence has been revised REFERENCE S40044 !$#authors Delgado, J.; Forst, S.; Harlocker, S.; Inouye, M. !$#journal Mol. Microbiol. (1993) 10:1037-1047 !$#title Identification of a phosphorylation site and functional !1analysis of conserved aspartic acid residues of OmpR, a !1transcriptional activator for ompF and ompC in Escherichia !1coli. !$#cross-references MUID:95020564; PMID:7934854 !$#accession S40044 !'##status preliminary !'##molecule_type protein !'##residues 47-58 ##label DEL COMMENT The amino-terminal moiety of this protein is required for !1the transcriptional expression of both major outer membrane !1protein genes ompF and ompC; its carboxyl-terminal moiety !1mediates the multimerization of the ompR protein. As a !1multimer, it turns on the expression of the ompC gene; as a !1monomer, it turns on the expression of the ompF gene. GENETICS !$#gene ompR !$#map_position 75 min CLASSIFICATION #superfamily ompR protein; response regulator homology KEYWORDS DNA binding; phosphoprotein; transcription regulation; !1two-component regulatory system FEATURE !$7-116 #domain response regulator homology #label RRH\ !$55 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 239 #molecular-weight 27353 #checksum 7449 SEQUENCE /// ENTRY JYECR #type complete TITLE dye resistance protein - Escherichia coli (strain K-12) ALTERNATE_NAMES aerobic respiration control protein ArcA; protein dye negative regulator in aerobic pathways ORGANISM #formal_name Escherichia coli DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 01-Mar-2002 ACCESSIONS A03561; S56625; H65255 REFERENCE A92515 !$#authors Drury, L.S.; Buxton, R.S. !$#journal J. Biol. Chem. (1985) 260:4236-4242 !$#title DNA sequence analysis of the dye gene of Escherichia coli !1reveals amino acid homology between the dye and ompR !1proteins. !$#cross-references MUID:85157583; PMID:2984198 !$#accession A03561 !'##molecule_type DNA !'##residues 1-238 ##label DRU !'##cross-references GB:M10044; NID:g145817; PIDN:AAA23718.1; !1PID:g145818 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56625 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-238 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97297.1; !1PID:g537241 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65255 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-238 ##label BLAT !'##cross-references GB:AE000510; GB:U00096; UWGP:b4401; NID:g1790858; !1PIDN:AAC77354.1; PID:g1790863 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene arcA; dye; fexA; msp; seg; sfrA !$#map_position 100 min FUNCTION !$#description regulatory protein, related to ompR, controlling resistance !1to dyes; required for expression of the alkaline phosphatase !1and ex factor F genes !$#note may also be involved in the osmoregulation of envelope !1proteins CLASSIFICATION #superfamily ompR protein; response regulator homology KEYWORDS DNA binding; osmoregulation; phosphoprotein; transcription !1regulation FEATURE !$6-114 #domain response regulator homology #label RRH\ !$54 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 238 #molecular-weight 27292 #checksum 3620 SEQUENCE /// ENTRY RGECFB #type complete TITLE transcription activator phoB - Escherichia coli (strain K-12) ALTERNATE_NAMES transcription regulator of phosphate regulon; transcription regulator phoB ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 01-Mar-2002 ACCESSIONS A24256; G64768 REFERENCE A24256 !$#authors Makino, K.; Shinagawa, H.; Amemura, M.; Nakata, A. !$#journal J. Mol. Biol. (1986) 190:37-44 !$#title Nucleotide sequence of the phoB gene, the positive !1regulatory gene for the phosphate regulon of Escherichia !1coli K-12. !$#cross-references MUID:87060980; PMID:3537313 !$#accession A24256 !'##molecule_type DNA !'##residues 1-229 ##label MAK !'##cross-references GB:X04026; NID:g42387; PIDN:CAA27659.1; PID:g42388 !'##experimental_source strain K12 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64768 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-229 ##label BLAT !'##cross-references GB:AE000146; GB:U00096; NID:g1786596; !1PIDN:AAC73502.1; PID:g1786599; UWGP:b0399 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene phoB !$#map_position 9 min FUNCTION !$#description transcription regulation; involved in transcription !1activation of the phosphate regulon !$#note phosphorylated phoB protein activates transcription of the !1phosphate regulon; phoB protein is phosphorylated by !1phosphorylated phoR protein; phoR protein is phosphorylated !1upon phosphate limitation !$#note in summary, when phosphate is limited phoB protein activates !1transcription of genes phoA, phoS, phoE, and ugpAB CLASSIFICATION #superfamily ompR protein; response regulator homology KEYWORDS DNA binding; phosphoprotein; transcription regulation; !1two-component regulatory system FEATURE !$5-116 #domain response regulator homology #label RRH\ !$53 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 229 #molecular-weight 26433 #checksum 5367 SEQUENCE /// ENTRY RGEBFT #type complete TITLE transcription regulator phoP - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS A32932; A37132 REFERENCE A32932 !$#authors Miller, S.I.; Kukral, A.M.; Mekalanos, J.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:5054-5058 !$#title A two-component regulatory system (phoP phoQ) controls !1Salmonella typhimurium virulence. !$#cross-references MUID:89296942; PMID:2544889 !$#accession A32932 !'##molecule_type DNA !'##residues 1-224 ##label MIL !'##cross-references GB:M24424; NID:g154265; PIDN:AAA27188.1; !1PID:g154266 REFERENCE A37132 !$#authors Groisman, E.A.; Chiao, E.; Lipps, C.J.; Heffron, F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:7077-7081 !$#title Salmonella typhimurium phoP virulence gene is a !1transcriptional regulator. !$#cross-references MUID:89386683; PMID:2674945 !$#accession A37132 !'##molecule_type DNA !'##residues 1-224 ##label GRO !'##cross-references GB:M25241; NID:g154263; PIDN:AAA27187.1; !1PID:g154264 GENETICS !$#gene phoP !$#map_position 25 min FUNCTION !$#description transcription regulation !$#note two-component regulatory system, phoP/phoQ, controls the !1expression of several genes; involved in regulation of acid !1phosphatase; phoP is phosphorylated by phoQ in response to !1enviromental signals CLASSIFICATION #superfamily ompR protein; response regulator homology KEYWORDS DNA binding; phosphoprotein; sensory transduction; !1transcription regulation; two-component regulatory system FEATURE !$4-113 #domain response regulator homology #label RRH\ !$52 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 224 #molecular-weight 25633 #checksum 8844 SEQUENCE /// ENTRY A41965 #type complete TITLE transcription regulator phoP - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli #variety strain K12 DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 01-Mar-2002 ACCESSIONS A41965; A41966; B43307; S19213; G64857; JU0379 REFERENCE A41965 !$#authors Groisman, E.A.; Heffron, F.; Solomon, F. !$#journal J. Bacteriol. (1992) 174:486-491 !$#title Molecular genetic analysis of the Escherichia coli phoP !1locus. !$#cross-references MUID:92105016; PMID:1530848 !$#accession A41965 !'##molecule_type DNA !'##residues 1-223 ##label GRO !'##note sequence extracted from NCBI backbone (NCBIN:75507, !1NCBIP:75509) REFERENCE A41966 !$#authors Kasahara, M.; Nakata, A.; Shinagawa, H. !$#journal J. Bacteriol. (1992) 174:492-498 !$#title Molecular analysis of the Escherichia coli phoP-phoQ operon. !$#cross-references MUID:92105017; PMID:1729240 !$#accession A41966 !'##molecule_type DNA !'##residues 1-223 ##label KAS !'##cross-references GB:D90393; NID:g216607; PIDN:BAA14390.1; !1PID:g216608 !'##note sequence extracted from NCBI backbone (NCBIN:75617, !1NCBIP:75619) REFERENCE A43307 !$#authors He, B.; Smith, J.M.; Zalkin, H. !$#journal J. Bacteriol. (1992) 174:130-136 !$#title Escherichia coli purB gene: cloning, nucleotide sequence, !1and regulation by purR. !$#cross-references MUID:92104952; PMID:1729205 !$#accession B43307 !'##molecule_type DNA !'##residues 1-50 ##label HE1 !'##cross-references GB:M74924; NID:g145202; PIDN:AAA92732.1; !1PID:g145204 !'##experimental_source strain K-12 !'##note sequence extracted from NCBI backbone (NCBIN:75230, !1NCBIP:75235) REFERENCE S19210 !$#authors Green, S.M.; Drabble, W.T. !$#submission submitted to the EMBL Data Library, May 1991 !$#description Molecular analysis of the purB-phoP region of Escherichia !1coli K12. !$#accession S19213 !'##molecule_type DNA !'##residues 1-24 ##label GRE !'##cross-references EMBL:X59307; NID:g42582; PIDN:CAA41997.1; !1PID:g42586 !'##experimental_source strain K-12 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64857 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-223 ##label BLAT !'##cross-references GB:AE000213; GB:U00096; NID:g1787371; !1PIDN:AAC74214.1; PID:g1787375; UWGP:b1130 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene phoP !$#map_position 25 min FUNCTION !$#description transcription regulation !$#note two-component regulatory system, phoP/phoQ, controls the !1expression of several genes; involved in regulation of acid !1phosphatase; phoP is phosphorylated by phoQ in response to !1enviromental signals CLASSIFICATION #superfamily ompR protein; response regulator homology KEYWORDS DNA binding; phosphoprotein; sensory transduction; !1transcription regulation; two-component regulatory system FEATURE !$3-112 #domain response regulator homology #label RRH\ !$51 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 223 #molecular-weight 25535 #checksum 2265 SEQUENCE /// ENTRY RGBSAP #type complete TITLE phosphate response regulator protein phoP - Bacillus subtilis ALTERNATE_NAMES alkaline phosphatase regulatory protein; regulatory protein phoP ORGANISM #formal_name Bacillus subtilis DATE 30-Sep-1991 #sequence_revision 02-Jul-1998 #text_change 16-Jun-2000 ACCESSIONS F69676; I40384; S26729; B27650; A27081 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69676 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-240 ##label KUN !'##cross-references GB:Z99118; GB:AL009126; NID:g2635200; !1PIDN:CAB14871.1; PID:g2635376 !'##experimental_source strain 168 REFERENCE I40379 !$#authors Jin, S.; Sonenshein, A.L. !$#journal J. Bacteriol. (1994) 176:4669-4679 !$#title Identification of two distinct Bacillus subtilis citrate !1synthase genes. !$#cross-references MUID:94321340; PMID:8045898 !$#accession I40384 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-6 ##label JIN !'##cross-references EMBL:U05257; NID:g1045295; PIDN:AAA96344.1; !1PID:g1045297 REFERENCE S26729 !$#authors Lee, J.W.; Hulett, F.M. !$#journal Nucleic Acids Res. (1992) 20:5848 !$#title Nucleotide sequence of the phoP gene encoding PhoP, the !1response regulator of the phosphate regulon of Bacillus !1subtilis. !$#cross-references MUID:93087210; PMID:1454550 !$#accession S26729 !'##molecule_type DNA !'##residues 1-123,'A',125-240 ##label LEE !'##cross-references EMBL:X67676; NID:g40055; PIDN:CAA47908.1; !1PID:g40056 REFERENCE A27650 !$#authors Seki, T.; Yoshikawa, H.; Takahashi, H.; Saito, H. !$#journal J. Bacteriol. (1988) 170:5935-5938 !$#title Nucleotide sequence of the Bacillus subtilis phoR gene. !$#cross-references MUID:89053932; PMID:3142862 !$#accession B27650 !'##molecule_type DNA !'##residues 212-240 ##label SEK1 !'##cross-references GB:M16775 REFERENCE A27081 !$#authors Seki, T.; Yoshikawa, H.; Takahashi, H.; Saito, H. !$#journal J. Bacteriol. (1987) 169:2913-2916 !$#title Cloning and nucleotide sequence of phoP, the regulatory gene !1for alkaline phosphatase and phosphodiesterase in Bacillus !1subtilis. !$#cross-references MUID:87250247; PMID:3036763 !$#accession A27081 !'##molecule_type DNA !'##residues 1-153,'I',155-210,'PT',212-240 ##label SEK2 !'##cross-references GB:M16775; NID:g143327; PIDN:AAA22661.1; !1PID:g143328 COMMENT This protein and phosphate response regulator histidine !1kinase phoR (see PIR:A27650) form the two-component !1regulatory system, which regulates the expression of genes !1involved in alkaline phosphatase and alkaline !1phosphodiesterase synthesis. GENETICS !$#gene phoP !$#map_position 71 min CLASSIFICATION #superfamily ompR protein; response regulator homology KEYWORDS DNA binding; phosphoprotein; sensory transduction; !1transcription regulation; two-component regulatory system FEATURE !$5-114 #domain response regulator homology #label RRH\ !$53 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 240 #molecular-weight 27683 #checksum 6975 SEQUENCE /// ENTRY RGKKOR #type complete TITLE regulatory protein ompR - red alga (Cyanidium caldarium) chloroplast ORGANISM #formal_name chloroplast Cyanidium caldarium DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS S20854; S25084 REFERENCE S20854 !$#authors Kessler, U.; Maid, U.; Zetsche, K. !$#journal Plant Mol. Biol. (1992) 18:777-780 !$#title An equivalent to bacterial ompR genes is encoded on the !1plastid genome of red algae. !$#cross-references MUID:92216053; PMID:1558950 !$#accession S20854 !'##molecule_type DNA !'##residues 1-255 ##label KES !'##cross-references EMBL:X62578; NID:g11278; PIDN:CAA44458.1; !1PID:g11279 REFERENCE S25084 !$#authors Maid, U.; Zetsche, K. !$#journal Plant Mol. Biol. (1992) 19:1001-1010 !$#title A 16 kb small single-copy region separates the plastid DNA !1inverted repeat of the unicellular red alga Cyanidium !1caldarium: physical mapping of the IR-flanking regions and !1nucleotide sequences of the psbD-psbC, rps16, 5S rRNA and !1rpl21 genes. !$#cross-references MUID:92379254; PMID:1511125 !$#accession S25084 !'##molecule_type DNA !'##residues 1-255 ##label MAI !'##cross-references EMBL:X62578; NID:g11278; PIDN:CAA44458.1; !1PID:g11279 GENETICS !$#gene ompR !$#genome chloroplast CLASSIFICATION #superfamily ompR protein; response regulator homology KEYWORDS chloroplast; DNA binding; phosphoprotein; transcription !1regulation FEATURE !$10-118 #domain response regulator homology #label RRH\ !$58 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 255 #molecular-weight 29448 #checksum 3139 SEQUENCE /// ENTRY QQECFJ #type complete TITLE transcription regulator creB - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 01-Mar-2002 ACCESSIONS B25038; S56622; E65255 REFERENCE A25038 !$#authors Amemura, M.; Makino, K.; Shinagawa, H.; Nakata, A. !$#journal J. Bacteriol. (1986) 168:294-302 !$#title Nucleotide sequence of the phoM region of Escherichia coli: !1four open reading frames may constitute an operon. !$#cross-references MUID:87008393; PMID:3531171 !$#accession B25038 !'##molecule_type DNA !'##residues 1-229 ##label AME !'##cross-references EMBL:M13608; NID:g147248; PIDN:AAA24374.1; !1PID:g147250 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56622 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-229 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97294.1; !1PID:g537238 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65255 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-229 ##label BLAT !'##cross-references GB:AE000510; GB:U00096; NID:g1790858; !1PIDN:AAC77351.1; PID:g1790860; UWGP:b4398 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene creB !$#map_position 100 min CLASSIFICATION #superfamily ompR protein; response regulator homology KEYWORDS phosphoprotein; transcription regulation FEATURE !$6-115 #domain response regulator homology #label RRH\ !$54 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 229 #molecular-weight 26125 #checksum 4267 SEQUENCE /// ENTRY S70164 #type complete TITLE copper resistance response regulator pcoR - Escherichia coli plasmid pRJ1004 ALTERNATE_NAMES transcription regulatory protein pcoR ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S70164; S52257 REFERENCE S70159 !$#authors Brown, N.L.; Barrett, S.R.; Camakaris, J.; Lee, B.T.O.; !1Rouch, D.A. !$#journal Mol. Microbiol. (1995) 17:1153-1166 !$#title Molecular genetics and transport analysis of the !1copper-resistance determinant (pco) from Escherichia coli !1plasmid pRJ1004. !$#cross-references MUID:96130847; PMID:8594334 !$#accession S70164 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-226 ##label BRO !'##cross-references EMBL:X83541 REFERENCE S52252 !$#authors Rouch, D.A.; Lee, B.T.O.; Barrett, S.R.; Rogers, S.D.; !1Camakaris, J.; Brown, N.L. !$#submission submitted to the EMBL Data Library, December 1994 !$#description Molecular genetics and transport analysis of the !1copper-resistance determinants (pco) from Escherichia coli !1plasmid pRJ1004. !$#accession S52257 !'##molecule_type DNA !'##residues 1-96,'D',98-226 ##label ROU !'##cross-references EMBL:X83541; NID:g619126; PIDN:CAA58529.1; !1PID:g619132 GENETICS !$#gene pcoR !$#genome plasmid pRJ1004 CLASSIFICATION #superfamily ompR protein; response regulator homology KEYWORDS phosphoprotein; transcription regulation; two-component !1regulatory system FEATURE !$4-113 #domain response regulator homology #label RRH\ !$52 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 226 #molecular-weight 25631 #checksum 3817 SEQUENCE /// ENTRY B47080 #type complete TITLE transcription activator copR - Pseudomonas syringae ORGANISM #formal_name Pseudomonas syringae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B47080; S46285 REFERENCE A47080 !$#authors Mills, S.D.; Jasalavich, C.A.; Cooksey, D.A. !$#journal J. Bacteriol. (1993) 175:1656-1664 !$#title A two-component regulatory system required for !1copper-inducible expression of the copper resistance operon !1of Pseudomonas syringae. !$#cross-references MUID:93194790; PMID:8449873 !$#accession B47080 !'##status preliminary !'##molecule_type DNA !'##residues 1-227 ##label MIL !'##cross-references GB:L05176; NID:g294346; PIDN:AAA25803.1; !1PID:g151181 !'##experimental_source pv. syringae !'##note sequence extracted from NCBI backbone (NCBIN:127412, !1NCBIP:127414) REFERENCE S46285 !$#authors Mills, S.D.; Lim, C.K.; Cooksey, D.A. !$#journal Mol. Gen. Genet. (1994) 244:341-351 !$#title Purification and characterization of CopR, a transcriptional !1activator protein that binds to a conserved domain (cop box) !1in copper-inducible promoters of Pseudomonas syringae. !$#cross-references MUID:94359456; PMID:8078459 !$#accession S46285 !'##status preliminary !'##molecule_type DNA !'##residues 1-8 ##label MI2 GENETICS !$#gene copR CLASSIFICATION #superfamily ompR protein; response regulator homology KEYWORDS DNA binding; phosphoprotein; transcription regulation FEATURE !$3-112 #domain response regulator homology #label RRH\ !$51 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 227 #molecular-weight 25470 #checksum 5567 SEQUENCE /// ENTRY C64159 #type complete TITLE transcription factor HI0837 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C64159 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession C64159 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-227 ##label TIGR !'##cross-references GB:U32765; GB:L42023; NID:g1573838; !1PIDN:AAC22495.1; PID:g1573851; TIGR:HI0837 CLASSIFICATION #superfamily ompR protein; response regulator homology KEYWORDS phosphoprotein FEATURE !$4-111 #domain response regulator homology #label RRH\ !$51 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 227 #molecular-weight 25727 #checksum 6849 SEQUENCE /// ENTRY C65197 #type complete TITLE transcription regulator cpxR - Escherichia coli (strain K-12) ALTERNATE_NAMES transcription factor (cpxA 5' region) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS C65197; S40856; I53679; S08331 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65197 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-232 ##label BLAT !'##cross-references GB:AE000466; GB:U00096; NID:g2367328; !1PIDN:AAC76894.1; PID:g2367329; UWGP:b3912 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S40802 !$#authors Plunkett III, G.; Burland, V.; Daniels, D.L.; Blattner, F.R. !$#journal Nucleic Acids Res. (1993) 21:3391-3398 !$#title Analysis of the Escherichia coli genome. III. DNA sequence !1of the region from 87.2 to 89.2 minutes. !$#cross-references MUID:93347969; PMID:8346018 !$#accession S40856 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-115,'X',117-232 ##label PLU !'##cross-references EMBL:L19201; NID:g304961; PIDN:AAB03045.1; !1PID:g305016 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1993 REFERENCE I53679 !$#authors Dong, J.; Iuchi, S.; Kwan, H.S.; Lu, Z.; Lin, E.C. !$#journal Gene (1993) 136:227-230 !$#title The deduced amino-acid sequence of the cloned cpxR gene !1suggests the protein is the cognate regulator for the !1membrane sensor, CpxA, in a two-component signal !1transduction system of Escherichia coli. !$#cross-references MUID:94124003; PMID:8294007 !$#accession I53679 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-232 ##label RES !'##cross-references GB:L14579; NID:g410156; PIDN:AAC36868.1; !1PID:g410157 REFERENCE S01377 !$#authors Weber, R.F.; Silverman, P.M. !$#journal J. Mol. Biol. (1988) 203:467-478 !$#title The Cpx proteins of Escherichia coli K12. Structure of the !1CpxA polypeptide as an inner membrane component. !$#cross-references MUID:89068697; PMID:3058985 !$#accession S08331 !'##molecule_type DNA !'##residues 138-232 ##label WEB !'##cross-references EMBL:X13307; NID:g41150; PIDN:CAA31686.1; !1PID:g41151 GENETICS !$#gene cpxR CLASSIFICATION #superfamily ompR protein; response regulator homology KEYWORDS phosphoprotein FEATURE !$4-111 #domain response regulator homology #label RRH\ !$51 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 232 #molecular-weight 26312 #checksum 1270 SEQUENCE /// ENTRY H65220 #type complete TITLE transcription regulator BasR/PmrA - Escherichia coli (strain K-12) ALTERNATE_NAMES response-regulator protein basR; signal transduction protein ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS H65220; JX0284; S56341 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65220 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-222 ##label BLAT !'##cross-references GB:AE000483; GB:U00096; NID:g2367351; !1PIDN:AAC77074.1; PID:g1790552; UWGP:b4113 !'##experimental_source strain K-12, substrain MG1655 REFERENCE JX0282 !$#authors Nagasawa, S.; Ishige, K.; Mizuno, T. !$#journal J. Biochem. (1993) 114:350-357 !$#title Novel members of the two-component signal transduction genes !1in Escherichia coli. !$#cross-references MUID:94110256; PMID:8282725 !$#accession JX0284 !'##molecule_type DNA !'##residues 1-28,'T',30-222 ##label NAG !'##cross-references GB:D14055; NID:g216536; PIDN:BAA03143.1; !1PID:g216538 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56341 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-222 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97012.1; !1PID:g536957 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 GENETICS !$#gene basR CLASSIFICATION #superfamily ompR protein; response regulator homology KEYWORDS DNA binding; phosphoprotein; signal transduction; !1transcription regulation; two-component regulatory system FEATURE !$3-112 #domain response regulator homology #label RRH\ !$51 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 222 #molecular-weight 25031 #checksum 6415 SEQUENCE /// ENTRY B40656 #type complete TITLE regulatory protein pmrA - Salmonella typhimurium (strain LT2) ORGANISM #formal_name Salmonella typhimurium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B40656 REFERENCE A40656 !$#authors Roland, K.L.; Martin, L.E.; Esther, C.R.; Spitznagel, J.K. !$#journal J. Bacteriol. (1993) 175:4154-4164 !$#title Spontaneous pmrA mutants of Salmonella typhimurium LT2 !1define a new two-component regulatory system with a possible !1role in virulence. !$#cross-references MUID:93308095; PMID:8391535 !$#accession B40656 !'##status preliminary !'##molecule_type DNA !'##residues 1-222 ##label ROL !'##cross-references GB:L13395 CLASSIFICATION #superfamily ompR protein; response regulator homology KEYWORDS DNA binding; phosphoprotein; transcription regulation FEATURE !$3-112 #domain response regulator homology #label RRH\ !$51 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 222 #molecular-weight 25053 #checksum 7591 SEQUENCE /// ENTRY S58232 #type complete TITLE PopP protein - Rhizobium leguminosarum ORGANISM #formal_name Rhizobium leguminosarum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S58232 REFERENCE S58232 !$#authors Yeoman, K.H.; Delgado, M.J.; Downie, J.A.; Johnston, A.W.B. !$#submission submitted to the EMBL Data Library, July 1995 !$#accession S58232 !'##status preliminary !'##molecule_type DNA !'##residues 1-223 ##label YEO !'##cross-references EMBL:X89983; NID:g929821; PIDN:CAA62008.1; !1PID:g929822 CLASSIFICATION #superfamily ompR protein; response regulator homology KEYWORDS phosphoprotein FEATURE !$3-112 #domain response regulator homology #label RRH\ !$51 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 223 #molecular-weight 24914 #checksum 75 SEQUENCE /// ENTRY S28674 #type complete TITLE hypothetical protein 2 - Rhizobium sp. (strain IC3342) ORGANISM #formal_name Rhizobium sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 11-May-2000 ACCESSIONS S28674 REFERENCE S28673 !$#authors Upadhyaya, N.M.; Scott, K.F.; Tucker, W.T.; Watson, J.M.; !1Dart, P.J. !$#journal Mol. Plant Microbe Interact. (1992) 5:129-143 !$#title Isolation and characterization of Rhizobium (IC3342) genes !1that determine leaf curl induction in pigeon pea. !$#cross-references MUID:92314428; PMID:1319772 !$#accession S28674 !'##molecule_type DNA !'##residues 1-238 ##label UPA !'##cross-references EMBL:M38698; NID:g152257; PIDN:AAA74221.1; !1PID:g152259 CLASSIFICATION #superfamily ompR protein; response regulator homology KEYWORDS phosphoprotein FEATURE !$4-111 #domain response regulator homology #label RRH\ !$51 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 238 #molecular-weight 26882 #checksum 9120 SEQUENCE /// ENTRY JX0283 #type complete TITLE response-regulator BaeR protein - Escherichia coli (strain K-12) ALTERNATE_NAMES signal transduction protein; transcription regulatory protein BaeR ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS JX0283; F64974 REFERENCE JX0282 !$#authors Nagasawa, S.; Ishige, K.; Mizuno, T. !$#journal J. Biochem. (1993) 114:350-357 !$#title Novel members of the two-component signal transduction genes !1in Escherichia coli. !$#cross-references MUID:94110256; PMID:8282725 !$#accession JX0283 !'##molecule_type DNA !'##residues 1-240 ##label NAG !'##cross-references GB:D14054; NID:g216530; PIDN:BAA03141.1; !1PID:g216533 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64974 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-240 ##label BLAT !'##cross-references GB:AE000297; GB:U00096; NID:g1788382; !1PIDN:AAC75140.1; PID:g1788394; UWGP:b2079 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene baeR CLASSIFICATION #superfamily ompR protein; response regulator homology KEYWORDS DNA binding; phosphoprotein; signal transduction; !1transcription regulation; two-component regulatory system FEATURE !$13-121 #domain response regulator homology #label RRH\ !$61 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 240 #molecular-weight 27656 #checksum 1015 SEQUENCE /// ENTRY A33861 #type complete TITLE trans-activating transcription regulator tctD - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A33861 REFERENCE A33861 !$#authors Widenhorn, K.A.; Somers, J.M.; Kay, W.W. !$#journal J. Bacteriol. (1989) 171:4436-4441 !$#title Genetic regulation of the tricarboxylate transport operon !1(tctI) of Salmonella typhimurium. !$#cross-references MUID:89327162; PMID:2666399 !$#accession A33861 !'##status preliminary !'##molecule_type DNA !'##residues 1-224 ##label WID !'##cross-references GB:M28368; NID:g295217; PIDN:AAA27232.1; !1PID:g295218 CLASSIFICATION #superfamily ompR protein; response regulator homology KEYWORDS phosphoprotein; transcription regulation FEATURE !$3-112 #domain response regulator homology #label RRH\ !$51 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 224 #molecular-weight 25407 #checksum 6563 SEQUENCE /// ENTRY S22632 #type complete TITLE petR protein - Rhodobacter capsulatus ORGANISM #formal_name Rhodobacter capsulatus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S22632; S21002 REFERENCE S22631 !$#authors Tokito, M.K.; Daldal, F. !$#journal Mol. Microbiol. (1992) 6:1645-1654 !$#title petR, located upstream of the fbcFBC operon encoding the !1cytochrome bc(1) complex, is homologous to bacterial !1response regulators and necessary for photosynthetic and !1respiratory growth of Rhodobacter capsulatus. !$#cross-references MUID:92356828; PMID:1323023 !$#accession S22632 !'##molecule_type DNA !'##residues 1-237 ##label TOK !'##cross-references EMBL:Z12113; NID:g49287; PIDN:CAA78098.1; !1PID:g2654368 GENETICS !$#gene petR CLASSIFICATION #superfamily ompR protein; response regulator homology KEYWORDS DNA binding; phosphoprotein; transcription regulation FEATURE !$9-117 #domain response regulator homology #label RRH\ !$57 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 237 #molecular-weight 26355 #checksum 1975 SEQUENCE /// ENTRY S32931 #type complete TITLE sensor protein sphS - Synechococcus sp. (strain PCC 7942) ORGANISM #formal_name Synechococcus sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S32931 REFERENCE S32931 !$#authors Aiba, H.; Nagaya, M.; Mizuno, T. !$#journal Mol. Microbiol. (1993) 8:81-91 !$#title Sensor and regulator proteins from the cyanobacterium !1Synechococcus species PCC7942 that belong to the bacterial !1signal-transduction protein families: implication in the !1adaptive response to phosphate limitation. !$#cross-references MUID:93268103; PMID:8497200 !$#accession S32931 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-257 ##label AIB !'##cross-references GB:D13172; NID:g391920; PIDN:BAA02453.1; !1PID:g391921 GENETICS !$#gene sphS CLASSIFICATION #superfamily ompR protein; response regulator homology KEYWORDS DNA binding; phosphoprotein; transcription regulation FEATURE !$26-144 #domain response regulator homology #label RRH\ !$83 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 257 #molecular-weight 29012 #checksum 7897 SEQUENCE /// ENTRY S76529 #type complete TITLE hypothetical protein - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S76529 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76529 !'##status preliminary !'##molecule_type DNA !'##residues 1-224 ##label KAN !'##cross-references EMBL:D64002; GB:AB001339; NID:g1001612; !1PIDN:BAA10375.1; PID:g1001644 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily ompR protein; response regulator homology FEATURE !$5-114 #domain response regulator homology #label RRH SUMMARY #length 224 #molecular-weight 25971 #checksum 3404 SEQUENCE /// ENTRY S76610 #type complete TITLE hypothetical protein - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S76610 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76610 !'##status preliminary !'##molecule_type DNA !'##residues 1-262 ##label KAN !'##cross-references EMBL:D64004; GB:AB001339; NID:g1001701; !1PIDN:BAA10554.1; PID:g1001717 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily ompR protein; response regulator homology KEYWORDS phosphoprotein FEATURE !$33-149 #domain response regulator homology #label RRH\ !$88 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 262 #molecular-weight 29926 #checksum 8162 SEQUENCE /// ENTRY S76708 #type complete TITLE sensory transduction system regulatory protein slr0115 - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein slr0115 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S76708 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76708 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-241 ##label KAN !'##cross-references EMBL:D64004; GB:AB001339; NID:g1001701; !1PIDN:BAA10652.1; PID:g1208484 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene ycf27-1 CLASSIFICATION #superfamily ompR protein; response regulator homology KEYWORDS phosphoprotein; transcription regulation FEATURE !$4-115 #domain response regulator homology #label RRH\ !$52 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 241 #molecular-weight 27276 #checksum 6918 SEQUENCE /// ENTRY S76823 #type complete TITLE hypothetical protein - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S76823 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76823 !'##status preliminary !'##molecule_type DNA !'##residues 1-234 ##label KAN !'##cross-references EMBL:D90916; GB:AB001339; NID:g1653715; !1PIDN:BAA18735.1; PID:g1653824 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily ompR protein; response regulator homology KEYWORDS phosphoprotein FEATURE !$3-112 #domain response regulator homology #label RRH\ !$51 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 234 #molecular-weight 26367 #checksum 7653 SEQUENCE /// ENTRY S77341 #type complete TITLE sensory transduction system regulatory protein slr1837 - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein slr1837 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S77341 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S77341 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-234 ##label KAN !'##cross-references EMBL:D90906; GB:AB001339; NID:g1652492; !1PIDN:BAA17444.1; PID:g1652523 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily ompR protein; response regulator homology KEYWORDS phosphoprotein FEATURE !$4-113 #domain response regulator homology #label RRH\ !$52 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 234 #molecular-weight 25655 #checksum 4241 SEQUENCE /// ENTRY S74926 #type complete TITLE sensory transduction system regulatory protein sll0649 - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein sll0649 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S74926 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74926 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-245 ##label KAN !'##cross-references EMBL:D90902; GB:AB001339; NID:g1652027; !1PIDN:BAA16966.1; PID:g1652041 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene phoP CLASSIFICATION #superfamily ompR protein; response regulator homology KEYWORDS phosphoprotein; transcription regulation FEATURE !$14-125 #domain response regulator homology #label RRH\ !$62 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 245 #molecular-weight 28428 #checksum 4659 SEQUENCE /// ENTRY A41838 #type complete TITLE transcription activator VanR - Enterococcus faecium ORGANISM #formal_name Enterococcus faecium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A41838 REFERENCE A41838 !$#authors Arthur, M.; Molinas, C.; Courvalin, P. !$#journal J. Bacteriol. (1992) 174:2582-2591 !$#title The VanS-VanR two-component regulatory system controls !1synthesis of depsipeptide peptidoglycan precursors in !1Enterococcus faecium BM4147. !$#cross-references MUID:92210502; PMID:1556077 !$#contents BM4147, pIP816 !$#accession A41838 !'##status preliminary !'##molecule_type DNA !'##residues 1-231 ##label ART !'##cross-references GB:M68910; NID:g148326; PIDN:AAA24787.1; !1PID:g148327 !'##note sequence extracted from NCBI backbone (NCBIN:94048, !1NCBIP:94051) CLASSIFICATION #superfamily ompR protein; response regulator homology KEYWORDS DNA binding; phosphoprotein; transcription regulation FEATURE !$5-113 #domain response regulator homology #label RRH\ !$53 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 231 #molecular-weight 26642 #checksum 4477 SEQUENCE /// ENTRY I40084 #type complete TITLE gtcR protein - Bacillus brevis ORGANISM #formal_name Bacillus brevis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS I40084; S43161 REFERENCE I40084 !$#authors Turgay, K.; Marahiel, M.A. !$#journal DNA Seq. (1995) 5:283-290 !$#cross-references MUID:96063019; PMID:7579582 !$#accession I40084 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-242 ##label RES !'##cross-references EMBL:X78502; NID:g468744; PIDN:CAA55264.1; !1PID:g468745 GENETICS !$#gene gtcR CLASSIFICATION #superfamily ompR protein; response regulator homology KEYWORDS phosphoprotein FEATURE !$5-113 #domain response regulator homology #label RRH\ !$53 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 242 #molecular-weight 28115 #checksum 4096 SEQUENCE /// ENTRY G69691 #type complete TITLE two-component response regulator involved in aerobic and anaer resD - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS G69691; S45559 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69691 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-240 ##label KUN !'##cross-references GB:Z99116; GB:AL009126; NID:g2634723; !1PIDN:CAB14244.1; PID:g2634747 !'##experimental_source strain 168 REFERENCE S45533 !$#authors Sorokin, A.; Zumstein, E.; Azevedo, V.; Ehrlich, S.D.; !1Serror, P. !$#submission submitted to the EMBL Data Library, November 1993 !$#accession S45559 !'##status preliminary !'##molecule_type DNA !'##residues 1-240 ##label SOR !'##cross-references EMBL:L09228; NID:g410114; PIDN:AAA67497.1; !1PID:g410141 GENETICS !$#gene resD CLASSIFICATION #superfamily ompR protein; response regulator homology KEYWORDS phosphoprotein FEATURE !$9-117 #domain response regulator homology #label RRH\ !$57 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 240 #molecular-weight 27485 #checksum 8506 SEQUENCE /// ENTRY S72906 #type complete TITLE phosphate sensor phoP - Mycobacterium leprae ALTERNATE_NAMES B2168_C3_248 protein ORGANISM #formal_name Mycobacterium leprae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 23-Mar-2001 ACCESSIONS S72906 REFERENCE S72586 !$#authors Smith, D.R.; Robison, K. !$#submission submitted to the EMBL Data Library, November 1993 !$#description Mycobacterium leprae cosmid B2168. !$#accession S72906 !'##status preliminary !'##molecule_type DNA !'##residues 1-198 ##label SMI !'##cross-references EMBL:U00018; NID:g467037; PIDN:AAA17242.1; !1PID:g467058 GENETICS !$#gene phoP !$#start_codon GTG CLASSIFICATION #superfamily ompR protein; response regulator homology KEYWORDS phosphoprotein FEATURE !$1-83 #domain response regulator homology #status atypical !8#label RRH\ !$23 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 198 #molecular-weight 21851 #checksum 1500 SEQUENCE /// ENTRY A45270 #type complete TITLE sensory response regulator homolog AfsQ1 - Streptomyces coelicolor ORGANISM #formal_name Streptomyces coelicolor DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A45270 REFERENCE A45270 !$#authors Ishizuka, H.; Horinouchi, S.; Kieser, H.M.; Hopwood, D.A.; !1Beppu, T. !$#journal J. Bacteriol. (1992) 174:7585-7594 !$#title A putative two-component regulatory system involved in !1secondary metabolism in Streptomyces spp. !$#cross-references MUID:93077438; PMID:1339426 !$#accession A45270 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-225 ##label ISH !'##cross-references GB:D10654; NID:g216982; PIDN:BAA01502.1; !1PID:g216983 !'##note sequence extracted from NCBI backbone (NCBIP:119102) CLASSIFICATION #superfamily ompR protein; response regulator homology KEYWORDS DNA binding; phosphoprotein; transcription regulation FEATURE !$4-112 #domain response regulator homology #label RRH\ !$52 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 225 #molecular-weight 25120 #checksum 5616 SEQUENCE /// ENTRY S15274 #type complete TITLE cutR protein - Streptomyces lividans ORGANISM #formal_name Streptomyces lividans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S15274 REFERENCE S15274 !$#authors Tseng, H.C.; Chen, C.W. !$#journal Mol. Microbiol. (1991) 5:1187-1196 !$#title A cloned ompR-like gene of Streptomyces lividans 66 !1suppresses defective melC1, a putative copper-transfer gene. !$#cross-references MUID:92065815; PMID:1956295 !$#accession S15274 !'##status preliminary !'##molecule_type DNA !'##residues 1-217 ##label TSE !'##cross-references EMBL:X58793; NID:g1279724; PIDN:CAA41599.1; !1PID:g581687 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily ompR protein; response regulator homology KEYWORDS DNA binding; phosphoprotein; transcription regulation FEATURE !$3-112 #domain response regulator homology #label RRH\ !$51 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 217 #molecular-weight 23914 #checksum 1391 SEQUENCE /// ENTRY F64137 #type complete TITLE regulatory protein basR homolog - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS F64137 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession F64137 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-221 ##label TIGR !'##cross-references GB:U32843; GB:L42023; NID:g1574554; !1PIDN:AAC23354.1; PID:g1574562; TIGR:HI1708 CLASSIFICATION #superfamily ompR protein; response regulator homology KEYWORDS phosphoprotein FEATURE !$3-112 #domain response regulator homology #label RRH\ !$51 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 221 #molecular-weight 24902 #checksum 5407 SEQUENCE /// ENTRY QQECF1 #type complete TITLE creA protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 01-Mar-2002 ACCESSIONS A25038; A46614; S56621; D65255; S27570 REFERENCE A25038 !$#authors Amemura, M.; Makino, K.; Shinagawa, H.; Nakata, A. !$#journal J. Bacteriol. (1986) 168:294-302 !$#title Nucleotide sequence of the phoM region of Escherichia coli: !1four open reading frames may constitute an operon. !$#cross-references MUID:87008393; PMID:3531171 !$#accession A25038 !'##molecule_type DNA !'##residues 1-157 ##label AME !'##cross-references EMBL:M13608; NID:g147248; PIDN:AAA24373.1; !1PID:g147249 REFERENCE JU0158 !$#authors Skarstad, K.; Thoeny, B.; Su Hwang, D.; Kornberg, A. !$#journal J. Biol. Chem. (1993) 268:5365-5370 !$#title A novel binding protein of the origin of the Escherichia !1coli chromosome. !$#cross-references MUID:93194823; PMID:8449900 !$#accession A46614 !'##molecule_type DNA !'##residues 1-28 ##label SKA !'##cross-references GB:M97495; NID:g147690; PIDN:AAA24568.1; !1PID:g147691; EMBL:M94042 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56621 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-157 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97293.1; !1PID:g537237 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65255 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-157 ##label BLAT !'##cross-references GB:AE000510; GB:U00096; NID:g1790858; !1PIDN:AAC77350.1; PID:g1790859; UWGP:b4397 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene creA !$#map_position 100 min CLASSIFICATION #superfamily creA protein SUMMARY #length 157 #molecular-weight 17108 #checksum 5064 SEQUENCE /// ENTRY S74913 #type complete TITLE sensory transduction system regulatory protein slr1400 - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein slr1400 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S74913 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74913 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-380 ##label KAN !'##cross-references EMBL:D90902; GB:AB001339; NID:g1652027; !1PIDN:BAA16953.1; PID:g1652028 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily sensory transduction system regulatory protein; !1response regulator homology; sensor histidine kinase !1homology KEYWORDS phosphoprotein FEATURE !$6-117 #domain response regulator homology #label RRH\ !$54 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 380 #molecular-weight 42043 #checksum 1952 SEQUENCE /// ENTRY S75131 #type complete TITLE sensory transduction system regulatory protein slr2099 - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein slr2099 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S75131 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75131 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-366 ##label KAN !'##cross-references EMBL:D90910; GB:AB001339; NID:g1652956; !1PIDN:BAA17993.1; PID:g1653076 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily sensory transduction system regulatory protein; !1response regulator homology; sensor histidine kinase !1homology KEYWORDS phosphoprotein; transcription regulation FEATURE !$13-124 #domain response regulator homology #label RRH\ !$61 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 366 #molecular-weight 40363 #checksum 3942 SEQUENCE /// ENTRY S75524 #type complete TITLE sensory transduction system regulatory protein sll1229 - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein sll1229 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S75524 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75524 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-378 ##label KAN !'##cross-references EMBL:D90911; GB:AB001339; NID:g1653083; !1PIDN:BAA18085.1; PID:g1653169 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily sensory transduction system regulatory protein; !1response regulator homology; sensor histidine kinase !1homology KEYWORDS phosphoprotein; transcription regulation FEATURE !$8-119 #domain response regulator homology #label RRH\ !$56 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 378 #molecular-weight 42382 #checksum 6718 SEQUENCE /// ENTRY S75023 #type complete TITLE sensory transduction histidine kinase sll1905 - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein sll1905 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S75023 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75023 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1014 ##label KAN !'##cross-references EMBL:D90910; GB:AB001339; NID:g1652956; !1PIDN:BAA17885.1; PID:g1652968 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily sensory transduction histidine kinase; response !1regulator homology KEYWORDS phosphoprotein FEATURE !$20-131 #domain response regulator homology #label RRH1\ !$293-542 #domain sensor histidine kinase homology #label SHK\ !$742-854 #domain response regulator homology #label RRH2\ !$68 #binding_site phosphate (Asp) (covalent) #status !8predicted\ !$790 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 1014 #molecular-weight 111604 #checksum 8928 SEQUENCE /// ENTRY S76291 #type complete TITLE sensory transduction system regulatory protein homolog sll0750 - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein sll0750; sensory transduction histidine kinase ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S76291 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76291 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-383 ##label KAN !'##cross-references EMBL:D64000; GB:AB001339; NID:g1001484; !1PIDN:BAA10143.1; PID:g1001516 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily sensory transduction system regulatory protein !1homolog SUMMARY #length 383 #molecular-weight 43435 #checksum 1930 SEQUENCE /// ENTRY F35718 #type complete TITLE phnE protein - Escherichia coli (strain K-12) ALTERNATE_NAMES hypothetical protein b4103 ORGANISM #formal_name Escherichia coli DATE 05-Oct-1990 #sequence_revision 02-Jun-1994 #text_change 01-Mar-2002 ACCESSIONS F35718; A42732; S56332; S56331; G65219; F65219 REFERENCE A35718 !$#authors Chen, C.M.; Ye, Q.Z.; Zhu, Z.; Wanner, B.L.; Walsh, C.T. !$#journal J. Biol. Chem. (1990) 265:4461-4471 !$#title Molecular biology of carbon-phosphorus bond cleavage. !1Cloning and sequencing of the phn (psiD) genes involved in !1alkylphosphonate uptake and C-P lyase activity in !1Escherichia coli B. !$#cross-references MUID:90170953; PMID:2155230 !$#accession F35718 !'##molecule_type DNA !'##residues 1-276 ##label CHE !'##cross-references GB:J05260; NID:g147192; PIDN:AAA24341.1; !1PID:g147198 !'##experimental_source strain B REFERENCE A42732 !$#authors Makino, K.; Kim, S.K.; Shinagawa, H.; Amemura, M.; Nakata, !1A. !$#journal J. Bacteriol. (1991) 173:2665-2672 !$#title Molecular analysis of the cryptic and functional phn operons !1for phosphonate use in Escherichia coli K-12. !$#cross-references MUID:91193228; PMID:1840580 !$#accession A42732 !'##molecule_type DNA !'##residues 1-276 ##label MAK !'##cross-references GB:D90227 !'##experimental_source functional mutant of strain K-12 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56332 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-157,'CWRCLSTPPACSPSCFPKRWKRLSPARWKAFAPPVPTSSKRSSTACC', !1161,'R' ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97003.1; !1PID:g536948 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 !$#accession S56331 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 'M',205-276 ##label BU2 !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97002.1; !1PID:g536947 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65219 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-157,'CWRCLSTPPACSPSCFPKRWKRLSPARWKAFAPPVPTSSKRSSTACC', !1161,'R' ##label BLAT !'##cross-references GB:AE000482; GB:U00096; NID:g2367349; !1PIDN:AAC77065.1; PID:g1790542; UWGP:b4104 !'##experimental_source strain K-12, substrain MG1655 !$#accession F65219 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 'M',205-276 ##label BLA2 !'##cross-references GB:AE000482; GB:U00096; NID:g2367349; !1PIDN:AAC77064.1; PID:g1790541; UWGP:b4103 !'##experimental_source strain K-12, substrain MG1655 COMMENT In wild-type strain K12, the phnE gene has an 8-bp !1insertion, which is absent from the strain B gene; this !1insertion causes a frameshift and the gene to be cryptic. !1However, spontaneous activation of the K-12 cryptic phnE !1gene is accompanied by loss of this 8-bp insertion after !1prolonged incubation. COMMENT The phnE gene belongs to an operon involved in !1alkylphosphonate uptake and C-P lyase; the exact function of !1this protein is not known. GENETICS !$#gene phnE !$#start_codon GTG CLASSIFICATION #superfamily phnE protein KEYWORDS alkylphosphonate uptake; transmembrane protein SUMMARY #length 276 #molecular-weight 30281 #checksum 101 SEQUENCE /// ENTRY RGBSHP #type complete TITLE regulatory protein hutP [similarity] - Bacillus subtilis ALTERNATE_NAMES histidine utilization operon transcription activator hutP ORGANISM #formal_name Bacillus subtilis DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 21-Jul-2000 ACCESSIONS S18809; F69643; T47090 REFERENCE S18808 !$#authors Oda, M.; Sugishita, A.; Furukawa, K. !$#journal J. Bacteriol. (1988) 170:3199-3205 !$#title Cloning and nucleotide sequences of histidase and regulatory !1genes in the Bacillus subtilis hut operon and positive !1regulation of the operon. !$#cross-references MUID:88257040; PMID:2454913 !$#accession S18809 !'##molecule_type DNA !'##residues 1-151 ##label ODA !'##cross-references EMBL:M20659; NID:g143074; PIDN:AAA22537.1; !1PID:g143075 !'##experimental_source strain 1A270 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69643 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-151 ##label KUN !'##cross-references GB:Z99124; GB:AL009126; NID:g2636442; !1PIDN:CAB15970.1; PID:g2636480 !'##experimental_source strain 168 REFERENCE Z24350 !$#authors Yoshida, K.; Sano, H.; Seki, S.; Oda, M.; Fujimura, M.; !1Fujita, Y. !$#journal Microbiology (1995) 141:337-343 !$#title Cloning and sequencing of a 29 kb region of the Bacillus !1subtilis genome containing the hut and wapA loci. !$#cross-references MUID:95219088; PMID:7704263 !$#accession T47090 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-151 ##label YOS !'##cross-references EMBL:D31856; NID:g603765; PIDN:BAA06645.1; !1PID:g603771 !'##experimental_source strain BGSC1A1 GENETICS !$#gene hutP !$#start_codon GTG FUNCTION !$#description involved in histidine degradation (hut operon); functions as !1positive regulator CLASSIFICATION #superfamily regulatory protein hutP KEYWORDS DNA binding; transcription regulation SUMMARY #length 151 #molecular-weight 16577 #checksum 3502 SEQUENCE /// ENTRY BVBSCB #type complete TITLE competence protein ComB (yuxH) - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jun-2000 ACCESSIONS C33591; A70025; I39807 REFERENCE A33591 !$#authors Weinrauch, Y.; Guillen, N.; Dubnau, D.A. !$#journal J. Bacteriol. (1989) 171:5362-5375 !$#title Sequence and transcription mapping of Bacillus subtilis !1competence genes comB and comA, one of which is related to a !1family of bacterial regulatory determinants. !$#cross-references MUID:90008771; PMID:2507523 !$#accession C33591 !'##molecule_type DNA !'##residues 1-409 ##label WEI !'##cross-references GB:M22855; NID:g142696; PIDN:AAA22318.1; !1PID:g142699 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A70025 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-409 ##label KUN !'##cross-references GB:Z99120; GB:AL009126; NID:g2635613; !1PIDN:CAB15162.1; PID:g2635669 !'##experimental_source strain 168 COMMENT This protein is required for the expression of the !1late-expressing competence genes in B. subtilis. GENETICS !$#gene yuxH; comB CLASSIFICATION #superfamily comB protein SUMMARY #length 409 #molecular-weight 47927 #checksum 4466 SEQUENCE /// ENTRY S26183 #type complete TITLE general stress protein gsiB - Bacillus subtilis ALTERNATE_NAMES glucose starvation inducible B ORGANISM #formal_name Bacillus subtilis DATE 22-Nov-1993 #sequence_revision 02-Jun-1994 #text_change 16-Jun-2000 ACCESSIONS S26183; H69637; S21381 REFERENCE S26181 !$#authors Mueller, J.P.; Bukusoglu, G.; Sonenshein, A.L. !$#journal J. Bacteriol. (1992) 174:4361-4373 !$#title Transcriptional regulation of Bacillus subtilis glucose !1starvation-inducible genes: control of gsiA by the ComP-ComA !1signal transduction system. !$#cross-references MUID:92325021; PMID:1378051 !$#accession S26183 !'##molecule_type DNA !'##residues 1-123 ##label MUE !'##cross-references EMBL:X56680; NID:g39933; PIDN:CAA40009.1; !1PID:g39934 !'##note the authors translated the codon AAA for residue 6 as Leu REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69637 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-123 ##label KUN !'##cross-references GB:Z99106; GB:AL009126; NID:g2632653; !1PIDN:CAB12247.1; PID:g2632740 !'##experimental_source strain 168 COMMENT This protein of unknown function is induced by glucose !1starvation or phosphate starvation but not amino acid !1starvation. GENETICS !$#gene gsiB CLASSIFICATION #superfamily gsiB protein KEYWORDS tandem repeat FEATURE !$13-117 #region 20-residue repeats !8(G-X-K-G-G-E-A-T-S-K-N-H-D-K-E-F-Y-Q-E-I) SUMMARY #length 123 #molecular-weight 13798 #checksum 9185 SEQUENCE /// ENTRY RGECAR #type complete TITLE aerobic respiration control sensor protein arcB (EC 2.7.3.-) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1991 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS D65112; JU0295; S11794 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65112 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-776 ##label BLAT !'##cross-references GB:AE000400; GB:U00096; NID:g2367203; !1PIDN:AAC76242.1; PID:g1789603; UWGP:b3210 !'##experimental_source strain K-12, substrain MG1655 REFERENCE JU0295 !$#authors Iuchi, S.; Matsuda, Z.; Fujiwara, T.; Lin, E.C.C. !$#journal Mol. Microbiol. (1990) 4:715-727 !$#title The arcB gene of Escherichia coli encodes a sensor-regulator !1protein for anaerobic repression of the arc modulon. !$#cross-references MUID:90355832; PMID:2201868 !$#accession JU0295 !'##molecule_type DNA !'##residues 1-468,'TG',469-776 ##label IUC !'##cross-references EMBL:X53315; NID:g40950; PIDN:CAA37397.1; !1PID:g40951 GENETICS !$#gene arcB !$#map_position 69.5 min CLASSIFICATION #superfamily aerobic respiration control sensor protein !1arcB; response regulator homology KEYWORDS autophosphorylation; phosphohistidine; phosphoprotein; !1phosphotransferase; sensory transduction; transcription !1regulation; transmembrane protein; two-component regulatory !1system FEATURE !$23-50 #domain transmembrane #status predicted #label TM1\ !$59-77 #domain transmembrane #status predicted #label TM2\ !$78-776 #domain intracellular #status predicted #label INT\ !$526-637 #domain response regulator homology #label RRH\ !$292 #binding_site phosphate (His) (covalent) #status !8predicted\ !$574 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 776 #molecular-weight 87824 #checksum 5082 SEQUENCE /// ENTRY RGECMT #type complete TITLE regulatory protein malT - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1989 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS E65137; A25641 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65137 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-901 ##label BLAT !'##cross-references GB:AE000418; GB:U00096; NID:g2367222; !1PIDN:AAC76443.1; PID:g2367223; UWGP:b3418 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A25641 !$#authors Cole, S.T.; Raibaud, O. !$#journal Gene (1986) 42:201-208 !$#title The nucleotide sequence of the malT gene encoding the !1positive regulator of the Escherichia coli maltose regulon. !$#cross-references MUID:86275993; PMID:3015733 !$#accession A25641 !'##molecule_type DNA !'##residues 1-191,'NE',194-901 ##label COL !'##cross-references GB:M13585; NID:g146716; PIDN:AAA83888.1; !1PID:g146717 COMMENT This protein is a positive regulator of the E. coli maltose !1regulon. GENETICS !$#gene malT !$#map_position 75 min CLASSIFICATION #superfamily regulatory protein malT KEYWORDS DNA binding; transcription regulation SUMMARY #length 901 #molecular-weight 103117 #checksum 402 SEQUENCE /// ENTRY RGKBAP #type complete TITLE nif-specific regulatory protein - Klebsiella pneumoniae ORGANISM #formal_name Klebsiella pneumoniae DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 16-Jul-1999 ACCESSIONS A91060; A93571; S02513; A03562 REFERENCE A91060 !$#authors Drummond, M.; Whitty, P.; Wootton, J. !$#journal EMBO J. (1986) 5:441-447 !$#title Sequence and domain relationships of ntrC and nifA from !1Klebsiella pneumoniae: homologies to other regulatory !1proteins. !$#cross-references MUID:86220124; PMID:3011408 !$#accession A91060 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-524 ##label DRU REFERENCE A93571 !$#authors Buikema, W.J.; Szeto, W.W.; Lemley, P.V.; Orme-Johnson, !1W.H.; Ausubel, F.M. !$#journal Nucleic Acids Res. (1985) 13:4539-4555 !$#title Nitrogen fixation specific regulatory genes of Klebsiella !1pneumoniae and Rhizobium meliloti share homology with the !1general nitrogen regulatory gene ntrC of Klebsiella !1pneumoniae. !$#cross-references MUID:85242120; PMID:2989799 !$#accession A93571 !'##molecule_type DNA !'##residues 1-484 ##label BUI !'##note this sequence has only 484 residues due to a frameshift caused !1by a missing G in the DNA sequence REFERENCE S01836 !$#authors Arnold, W.; Rump, A.; Klipp, W.; Priefer, U.B.; Puehler, A. !$#journal J. Mol. Biol. (1988) 203:715-738 !$#title Nucleotide sequence of a 24,206-base-pair DNA fragment !1carrying the entire nitrogen fixation gene cluster of !1Klebsiella pneumoniae. !$#cross-references MUID:89094839; PMID:3062178 !$#accession S02513 !'##molecule_type DNA !'##residues 1-524 ##label ARN !'##cross-references EMBL:X13303; NID:g43820; PIDN:CAA31682.1; !1PID:g43838 COMMENT This protein, a transcriptional activator, is required for !1activation of most nif operons, which are directly involved !1in nitrogen fixation. GENETICS !$#gene nifA CLASSIFICATION #superfamily nif-specific regulatory protein; RNA polymerase !1sigma factor interaction domain homology KEYWORDS DNA binding; P-loop; transcription regulation FEATURE !$212-433 #domain RNA polymerase sigma factor interaction !8domain homology #label SFI\ !$240-247 #region nucleotide-binding motif A (P-loop) #status !8atypical\ !$307-311 #region nucleotide-binding motif B SUMMARY #length 524 #molecular-weight 58632 #checksum 212 SEQUENCE /// ENTRY S01927 #type complete TITLE nif-specific regulatory protein - Azotobacter vinelandii ORGANISM #formal_name Azotobacter vinelandii DATE 28-Feb-1990 #sequence_revision 05-Apr-1995 #text_change 16-Jul-1999 ACCESSIONS S01927; A27733 REFERENCE S01926 !$#authors Bennet, L.T.; Cannon, F.; Dean, D.R. !$#journal Mol. Microbiol. (1988) 2:315-321 !$#title Nucleotide sequence and mutagenesis of the nifA gene from !1Azotobacter vinelandii. !$#cross-references MUID:88288044; PMID:2840552 !$#accession S01927 !'##molecule_type DNA !'##residues 1-522 ##label BEN !'##cross-references EMBL:Y00554; NID:g39258; PIDN:CAA68633.1; !1PID:g39260 REFERENCE A91866 !$#authors Joerger, R.D.; Bishop, P.E. !$#journal J. Bacteriol. (1988) 170:1475-1487 !$#title Nucleotide sequence and genetic analysis of the nifB-nifQ !1region from Azotobacter vinelandii. !$#cross-references MUID:88169465; PMID:2450865 !$#accession A27733 !'##molecule_type DNA !'##residues 394-522 ##label JOE !'##cross-references EMBL:J03411; NID:g142336; PIDN:AAA22147.1; !1PID:g142337 GENETICS !$#gene nifA CLASSIFICATION #superfamily nif-specific regulatory protein; RNA polymerase !1sigma factor interaction domain homology KEYWORDS DNA binding; P-loop; transcription regulation FEATURE !$211-432 #domain RNA polymerase sigma factor interaction !8domain homology #label SFI\ !$239-246 #region nucleotide-binding motif A (P-loop) #status !8atypical\ !$306-310 #region nucleotide-binding motif B SUMMARY #length 522 #molecular-weight 58122 #checksum 2623 SEQUENCE /// ENTRY RGZRAM #type complete TITLE nif-specific regulatory protein - Rhizobium meliloti ALTERNATE_NAMES nitrogen fixation regulatory protein ORGANISM #formal_name Rhizobium meliloti DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 16-Jul-1999 ACCESSIONS A03563; A24667 REFERENCE A93571 !$#authors Buikema, W.J.; Szeto, W.W.; Lemley, P.V.; Orme-Johnson, !1W.H.; Ausubel, F.M. !$#journal Nucleic Acids Res. (1985) 13:4539-4555 !$#title Nitrogen fixation specific regulatory genes of Klebsiella !1pneumoniae and Rhizobium meliloti share homology with the !1general nitrogen regulatory gene ntrC of Klebsiella !1pneumoniae. !$#cross-references MUID:85242120; PMID:2989799 !$#accession A03563 !'##molecule_type DNA !'##residues 1-541 ##label BUI !'##cross-references GB:X02615; NID:g46282; PIDN:CAA26470.1; PID:g46283 REFERENCE A24667 !$#authors Weber, G.; Reilander, H.; Puhler, A. !$#journal EMBO J. (1985) 4:2751-2756 !$#title Mapping and expression of a regulatory nitrogen fixation !1gene (fixD) of Rhizobium meliloti. !$#accession A24667 !'##molecule_type DNA !'##residues 1-541 ##label WEB COMMENT This protein, a transcriptional activator, is required for !1activation of most nif operons, which are directly involved !1in nitrogen fixation. GENETICS !$#gene nifA; fixD CLASSIFICATION #superfamily nif-specific regulatory protein; RNA polymerase !1sigma factor interaction domain homology KEYWORDS DNA binding; P-loop; transcription regulation FEATURE !$200-421 #domain RNA polymerase sigma factor interaction !8domain homology #label SFI\ !$228-235 #region nucleotide-binding motif A (P-loop) #status !8atypical\ !$295-299 #region nucleotide-binding motif B SUMMARY #length 541 #molecular-weight 59864 #checksum 6406 SEQUENCE /// ENTRY C25878 #type complete TITLE nif-specific regulatory protein - Rhizobium leguminosarum plasmid pRL6JI ORGANISM #formal_name Rhizobium leguminosarum DATE 16-Aug-1988 #sequence_revision 05-Apr-1995 #text_change 16-Jul-1999 ACCESSIONS C25878 REFERENCE A93661 !$#authors Gronger, P.; Manian, S.S.; Reilander, H.; O'Connell, M.; !1Priefer, U.B.; Puhler, A. !$#journal Nucleic Acids Res. (1987) 15:31-49 !$#title Organization and partial sequence of a DNA region of the !1Rhizobium leguminosarum symbiotic plasmid pRL6JI containing !1the genes fixABC, nifA, nifB and a novel open reading frame. !$#cross-references MUID:87146339; PMID:3029674 !$#accession C25878 !'##molecule_type DNA !'##residues 1-519 ##label GRO !'##cross-references GB:X05049; NID:g46199; PIDN:CAA28723.1; PID:g46202 COMMENT This protein, a transcriptional activator, is required for !1activation of most nif operons, which are directly involved !1in nitrogen fixation. GENETICS !$#gene nifA !$#genome plasmid CLASSIFICATION #superfamily nif-specific regulatory protein; RNA polymerase !1sigma factor interaction domain homology KEYWORDS DNA binding; P-loop; transcription regulation FEATURE !$177-398 #domain RNA polymerase sigma factor interaction !8domain homology #label SFI\ !$205-212 #region nucleotide-binding motif A (P-loop) #status !8atypical\ !$272-276 #region nucleotide-binding motif B SUMMARY #length 519 #molecular-weight 56179 #checksum 1527 SEQUENCE /// ENTRY S06965 #type complete TITLE nif-specific regulatory protein - Rhizobium leguminosarum ORGANISM #formal_name Rhizobium leguminosarum DATE 22-Jan-1993 #sequence_revision 05-Apr-1995 #text_change 16-Jul-1999 ACCESSIONS S06965 REFERENCE S06964 !$#authors Roelvink, P.W.; Hontelez, J.G.J.; van Kammen, A.; van den !1Bos, R.C. !$#journal Mol. Microbiol. (1989) 3:1441-1447 !$#title Nucleotide sequence of the regulatory nifA gene of Rhizobium !1leguminosarum PRE: transcriptional control sites and !1expression in Escherichia coli. !$#cross-references MUID:90136072; PMID:2693897 !$#accession S06965 !'##molecule_type DNA !'##residues 1-519 ##label ROE !'##cross-references EMBL:X17073; NID:g46208; PIDN:CAA34924.1; !1PID:g46210 COMMENT This protein, a transcriptional activator, is required for !1activation of most nif operons, which are directly involved !1in nitrogen fixation. GENETICS !$#gene nifA CLASSIFICATION #superfamily nif-specific regulatory protein; RNA polymerase !1sigma factor interaction domain homology KEYWORDS transcription regulation FEATURE !$177-398 #domain RNA polymerase sigma factor interaction !8domain homology #label SFI SUMMARY #length 519 #molecular-weight 56477 #checksum 3731 SEQUENCE /// ENTRY S06977 #type complete TITLE nif-specific regulatory protein - Azorhizobium caulinodans ORGANISM #formal_name Azorhizobium caulinodans DATE 22-Jan-1993 #sequence_revision 05-Apr-1995 #text_change 16-Jul-1999 ACCESSIONS S06977; S03933 REFERENCE S06977 !$#authors Ratet, P.; Pawlowski, K.; Schell, J.; de Bruijn, F.J. !$#journal Mol. Microbiol. (1989) 3:825-838 !$#title The Azorhizobium caulinodans nitrogen-fixation regulatory !1gene, nifA, is controlled by the cellular nitrogen and !1oxygen status. !$#cross-references MUID:89313312; PMID:2664425 !$#accession S06977 !'##molecule_type DNA !'##residues 1-615 ##label RAT !'##cross-references EMBL:X14716; NID:g38727; PIDN:CAA32836.1; !1PID:g38728 REFERENCE S03676 !$#authors Nees, D.W.; Stein, P.A.; Ludwig, R.A. !$#journal Nucleic Acids Res. (1988) 16:9839-9853 !$#title The Azorhizobium caulinodans nifA gene: identification of !1upstream-activating sequences including a new element, the !1'anaerobox'. !$#cross-references MUID:89041569; PMID:3186446 !$#accession S03933 !'##molecule_type DNA !'##residues 3-615 ##label NEE !'##cross-references EMBL:X08014; NID:g38725; PIDN:CAA30816.1; !1PID:g38726 COMMENT This protein, a transcriptional activator, is required for !1activation of most nif operons, which are directly involved !1in nitrogen fixation. GENETICS !$#gene nifA CLASSIFICATION #superfamily nif-specific regulatory protein; RNA polymerase !1sigma factor interaction domain homology KEYWORDS DNA binding; transcription regulation FEATURE !$256-477 #domain RNA polymerase sigma factor interaction !8domain homology #label SFI SUMMARY #length 615 #molecular-weight 66794 #checksum 2519 SEQUENCE /// ENTRY RGECAY #type complete TITLE transcription regulator tyrR - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 05-Apr-1995 #text_change 01-Mar-2002 ACCESSIONS A47086; A24209; F64881 REFERENCE A47086 !$#authors Yang, J.; Ganesan, S.; Sarsero, J.; Pittard, A.J. !$#journal J. Bacteriol. (1993) 175:1767-1776 !$#title A genetic analysis of various functions of the TyrR protein !1of Escherichia coli. !$#cross-references MUID:93194802; PMID:8449883 !$#accession A47086 !'##molecule_type DNA !'##residues 1-513 ##label YAN !'##cross-references GB:M12114; NID:g148091; PIDN:AAA24706.1; !1PID:g148092 !'##note sequence extracted from NCBI backbone (NCBIP:127622) !'##note correction of sequence reported in reference A24209 REFERENCE A24209 !$#authors Cornish, E.C.; Argyropoulos, V.P.; Pittard, J.; Davidson, !1B.E. !$#journal J. Biol. Chem. (1986) 261:403-410 !$#title Structure of the Escherichia coli K12 regulatory gene tyrR. !1Nucleotide sequence and sites of initiation of transcription !1and translation. !$#cross-references MUID:86085847; PMID:3001057 !$#accession A24209 !'##molecule_type DNA !'##residues 1-452,'AKMRWKVRWTKSPAVLNARY' ##label COR !'##experimental_source strain K12 !'##note this sequence has been corrected in reference A47086 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64881 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-513 ##label BLAT !'##cross-references GB:AE000230; GB:U00096; NID:g1787578; !1PIDN:AAC74405.1; PID:g1787583; UWGP:b1323 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene tyrR !$#map_position 29 min COMPLEX homodimer FUNCTION !$#description regulates expression of genes involved in aromatic amino !1acid biosynthesis and transport !$#note autogenously regulated; activity depends on concentrations !1of aromatic amino acids CLASSIFICATION #superfamily nif-specific regulatory protein; RNA polymerase !1sigma factor interaction domain homology KEYWORDS DNA binding; nucleotide binding; P-loop; transcription !1regulation FEATURE !$206-421 #domain RNA polymerase sigma factor interaction !8domain homology #label SFI\ !$234-241 #region nucleotide-binding motif A (P-loop) #status !8atypical\ !$294-298 #region nucleotide-binding motif B SUMMARY #length 513 #molecular-weight 57656 #checksum 6156 SEQUENCE /// ENTRY NIPSRP #type complete TITLE regulatory protein xylR - Pseudomonas putida plasmid TOL ORGANISM #formal_name Pseudomonas putida DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 28-May-1999 ACCESSIONS JT0327 REFERENCE JT0327 !$#authors Inouye, S.; Nakazawa, A.; Nakazawa, T. !$#journal Gene (1988) 66:301-306 !$#title Nucleotide sequence of the regulatory gene xylR of the TOL !1plasmid from Pseudomonas putida. !$#cross-references MUID:89006271; PMID:3169574 !$#accession JT0327 !'##molecule_type DNA !'##residues 1-566 ##label INO !'##cross-references GB:M10143; GB:M15819; GB:M20635; NID:g151662; !1PIDN:AAB59162.1; PID:g455334 COMMENT This regulatory protein is a transcriptional activator for !1the degradative pathway of aromatic hydrocarbons. GENETICS !$#gene xylR !$#genome plasmid CLASSIFICATION #superfamily nif-specific regulatory protein; RNA polymerase !1sigma factor interaction domain homology KEYWORDS DNA binding; P-loop; transcription regulation FEATURE !$1-210 #domain amino-terminal #label NHT\ !$211-229 #region interdomain linker #status predicted\ !$234-473 #domain interaction with RNA polymerase sigma factor !8#status predicted #label IRS\ !$235-457 #domain RNA polymerase sigma factor interaction !8domain homology #label SFI\ !$263-270 #region nucleotide-binding motif A (P-loop) #status !8atypical\ !$330-334 #region nucleotide-binding motif B\ !$515-558 #domain DNA binding #status predicted #label DNB SUMMARY #length 566 #molecular-weight 63743 #checksum 8448 SEQUENCE /// ENTRY A47078 #type complete TITLE phenol catabolic pathway positive regulator dmpR - Pseudomonas sp. plasmid ORGANISM #formal_name Pseudomonas sp. DATE 21-Sep-1993 #sequence_revision 05-Apr-1995 #text_change 01-Aug-1997 ACCESSIONS A47078 REFERENCE A47078 !$#authors Shingler, V.; Bartilson, M.; Moore, T. !$#journal J. Bacteriol. (1993) 175:1596-1604 !$#title Cloning and nucleotide sequence of the gene encoding the !1positive regulator (DmpR) of the phenol catabolic pathway !1encoded by pVI150 and identification of DmpR as a member of !1the NtrC family of transcriptional activators. !$#cross-references MUID:93194783; PMID:8449869 !$#contents pVI150 !$#accession A47078 !'##molecule_type DNA !'##residues 1-563 ##label SHI !'##cross-references GB:X68033 !'##experimental_source strain CF600 !'##note sequence extracted from NCBI backbone (NCBIN:127352, !1NCBIP:127353) GENETICS !$#gene dmpR !$#genome plasmid CLASSIFICATION #superfamily nif-specific regulatory protein; RNA polymerase !1sigma factor interaction domain homology KEYWORDS transcription regulation FEATURE !$235-457 #domain RNA polymerase sigma factor interaction !8domain homology #label SFI SUMMARY #length 563 #molecular-weight 63197 #checksum 5015 SEQUENCE /// ENTRY S47095 #type complete TITLE phhR protein - Pseudomonas putida ORGANISM #formal_name Pseudomonas putida DATE 13-Jan-1995 #sequence_revision 05-Apr-1995 #text_change 16-Jul-1999 ACCESSIONS S47095 REFERENCE S47095 !$#authors Ng, L.C.; Poh, C.L.; Shingler, V. !$#submission submitted to the EMBL Data Library, June 1994 !$#accession S47095 !'##molecule_type DNA !'##residues 1-563 ##label NGL !'##cross-references EMBL:X79599; NID:g498986; PIDN:CAA56111.1; !1PID:g498987 GENETICS !$#gene phhR CLASSIFICATION #superfamily nif-specific regulatory protein; RNA polymerase !1sigma factor interaction domain homology KEYWORDS P-loop; transcription regulation FEATURE !$235-457 #domain RNA polymerase sigma factor interaction !8domain homology #label SFI\ !$263-270 #region nucleotide-binding motif A (P-loop) #status !8atypical\ !$330-334 #region nucleotide-binding motif B SUMMARY #length 563 #molecular-weight 63205 #checksum 7791 SEQUENCE /// ENTRY F70010 #type complete TITLE transcription regulator Lrp/AsnC family homolog yugG - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS F70010 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F70010 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-166 ##label KUN !'##cross-references GB:Z99120; GB:AL009126; NID:g2635613; !1PIDN:CAB15130.1; PID:g2635637 !'##experimental_source strain 168 GENETICS !$#gene yugG CLASSIFICATION #superfamily transcription regulator yugG SUMMARY #length 166 #molecular-weight 18760 #checksum 8704 SEQUENCE /// ENTRY E69452 #type complete TITLE leucine responsive regulatory protein (lrp) homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS E69452 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession E69452 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-163 ##label KLE !'##cross-references GB:AE000990; GB:AE000782; NID:g2689313; !1PIDN:AAB89621.1; PID:g2648930; TIGR:AF1622 CLASSIFICATION #superfamily transcription regulator yugG SUMMARY #length 163 #molecular-weight 18932 #checksum 3538 SEQUENCE /// ENTRY C64390 #type complete TITLE probable transcription regulator - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C64390 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession C64390 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-156 ##label BUL !'##cross-references GB:U67519; GB:L77117; NID:g1591436; !1PIDN:AAB98719.1; PID:g1591440; TIGR:MJ0723 GENETICS !$#map_position FOR656706-657176 !$#start_codon TTG CLASSIFICATION #superfamily transcription regulator yugG SUMMARY #length 156 #molecular-weight 17730 #checksum 7689 SEQUENCE /// ENTRY S74043 #type complete TITLE transcription regulator homolog c0107 - Sulfolobus solfataricus ORGANISM #formal_name Sulfolobus solfataricus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S74043 REFERENCE S73076 !$#authors Sensen, C.W.; Klenk, H.P.; Singh, R.K.; Allard, G.; Chan, !1C.C.Y.; Liu, Q.Y.; Penny, S.L.; Young, F.; Schenk, M.E.; !1Gaasterland, T.; Doolittle, W.F.; Ragan, M.A.; Charlebois, !1R.L. !$#journal Mol. Microbiol. (1996) 22:175-191 !$#title Organizational characteristics and information content of an !1archaeal genome: 156 kb of sequence from Sulfolobus !1solfataricus P2. !$#cross-references MUID:97055432; PMID:8899719 !$#accession S74043 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-155 ##label SEN !'##cross-references EMBL:Y08256; NID:g1707679; PIDN:CAA69457.1; !1PID:g1707737 !'##experimental_source strain P2 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1September 1996 CLASSIFICATION #superfamily transcription regulator yugG SUMMARY #length 155 #molecular-weight 17702 #checksum 9404 SEQUENCE /// ENTRY B69309 #type complete TITLE transcription regulator AsnC family homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B69309 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession B69309 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-180 ##label KLE !'##cross-references GB:AE001071; GB:AE000782; NID:g2689394; !1PIDN:AAB90762.1; PID:g2650151; TIGR:AF0474 CLASSIFICATION #superfamily transcription regulator yugG SUMMARY #length 180 #molecular-weight 20744 #checksum 2070 SEQUENCE /// ENTRY A43650 #type complete TITLE transcription activator for bop [validated] - Halobacterium salinarum ALTERNATE_NAMES bacterio-opsin activator ORGANISM #formal_name Halobacterium salinarum DATE 18-Feb-2000 #sequence_revision 18-Feb-2000 #text_change 18-Feb-2000 ACCESSIONS A43650 REFERENCE A43650 !$#authors Leong, D.; Pfeifer, F.; Boyer, H.; Betlach, M. !$#journal J. Bacteriol. (1988) 170:4903-4909 !$#title Characterization of a second gene involved in bacterio-opsin !1gene expression in a halophilic archaebacterium. !$#cross-references MUID:89008114; PMID:3170488 !$#accession A43650 !'##molecule_type DNA !'##residues 1-674 ##label LEO !'##cross-references GB:M23247; NID:g148752; PID:g148753 !'##experimental_source strain NRC817 !'##note the source is designated as Halobacterium halobium GENETICS !$#gene bat FUNCTION !$#description may be involved in activating transcription of the bop and !1brp genes [validated, MUID:89008114] CLASSIFICATION #superfamily Halobacterium transcription activator for bop KEYWORDS transcription regulation SUMMARY #length 674 #molecular-weight 73322 #checksum 8735 SEQUENCE /// ENTRY RGKBCP #type complete TITLE nitrogen regulation protein I ntrC - Klebsiella pneumoniae ORGANISM #formal_name Klebsiella pneumoniae DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 28-May-1999 ACCESSIONS B91060; B93571; A03564 REFERENCE A91060 !$#authors Drummond, M.; Whitty, P.; Wootton, J. !$#journal EMBO J. (1986) 5:441-447 !$#title Sequence and domain relationships of ntrC and nifA from !1Klebsiella pneumoniae: homologies to other regulatory !1proteins. !$#cross-references MUID:86220124; PMID:3011408 !$#accession B91060 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-469 ##label DRU REFERENCE A93571 !$#authors Buikema, W.J.; Szeto, W.W.; Lemley, P.V.; Orme-Johnson, !1W.H.; Ausubel, F.M. !$#journal Nucleic Acids Res. (1985) 13:4539-4555 !$#title Nitrogen fixation specific regulatory genes of Klebsiella !1pneumoniae and Rhizobium meliloti share homology with the !1general nitrogen regulatory gene ntrC of Klebsiella !1pneumoniae. !$#cross-references MUID:85242120; PMID:2989799 !$#accession B93571 !'##molecule_type DNA !'##residues 1-143,'R',145-469 ##label BUI !'##cross-references GB:X02617; GB:M19277; NID:g43897; PIDN:CAA26473.1; !1PID:g43898 GENETICS !$#gene ntrC FUNCTION !$#description transcription regulator; can be both, a transacription !1activator and a repressor, depending on the nucleotide !1sequence of the regulatory regions with which it interacts !$#note ntrC probably activates transcription of a gene(s) whose !1product(s) in turn functions to relieve nifL inhibition !1under nitrogen-limiting conditions CLASSIFICATION #superfamily nitrogen assimilation regulatory protein ntrC; !1response regulator homology; RNA polymerase sigma factor !1interaction domain homology KEYWORDS ATP; DNA binding; P-loop; phosphoprotein; signal !1transduction; transcription regulation FEATURE !$6-115 #domain response regulator homology #label RRH\ !$140-362 #domain RNA polymerase sigma factor interaction !8domain homology #label SFI\ !$168-175 #region nucleotide-binding motif A (P-loop) #status !8atypical\ !$235-239 #region nucleotide-binding motif B\ !$54 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 469 #molecular-weight 52343 #checksum 7941 SEQUENCE /// ENTRY RGECGG #type complete TITLE nitrogen regulation protein I ntrC - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 01-Mar-2002 ACCESSIONS B30377; S40813; G65191; Q90553 REFERENCE A30377 !$#authors Miranda-Rios, J.; Sanchez-Pescador, R.; Urdea, M.; !1Covarrubias, A.A. !$#journal Nucleic Acids Res. (1987) 15:2757-2770 !$#title The complete nucleotide sequence of the glnALG operon of !1Escherichia coli K12. !$#cross-references MUID:87174797; PMID:2882477 !$#accession B30377 !'##molecule_type DNA !'##residues 1-468 ##label MIR !'##cross-references EMBL:X05173; NID:g41562; PIDN:CAA28808.1; !1PID:g41565 !'##experimental_source strain K-12 REFERENCE S40802 !$#authors Plunkett III, G.; Burland, V.; Daniels, D.L.; Blattner, F.R. !$#journal Nucleic Acids Res. (1993) 21:3391-3398 !$#title Analysis of the Escherichia coli genome. III. DNA sequence !1of the region from 87.2 to 89.2 minutes. !$#cross-references MUID:93347969; PMID:8346018 !$#accession S40813 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-141,'GEA',144-468 ##label PLU !'##cross-references EMBL:L19201; NID:g304961; PIDN:AAB03002.1; !1PID:g304973 !'##experimental_source strain K-12, substrain MG1655 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1993 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65191 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-141,'GEA',144-468 ##label BLAT !'##cross-references GB:AE000462; GB:U00096; NID:g1790295; !1PIDN:AAC76865.1; PID:g1790299; UWGP:b3868 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene glnG; ntrC; glnT !$#map_position 87 min FUNCTION !$#description de-uridylylated P-II forms a complex with nitrogen !1regulation protein II (ntrB); ntrB, when complexed with !1de-uridylylated P-II, dephosphorylates nitrogen regulation !1protein I (ntrC); the uridylylated form of P-II does not !1complex with ntrB; free ntrB phosphorylates nitrogen !1regulation protein I (ntrC) !$#note phosphorylated nitrogen regulation protein I (ntrC) !1activates transcription of the glutamine synthase (glnA) !1gene via interaction with sigma-54 factor (DNA-looping) for !1transcription activation: assembly of a multimeric ntrC !1complex at the enhancer DNA sequence CLASSIFICATION #superfamily nitrogen assimilation regulatory protein ntrC; !1response regulator homology; RNA polymerase sigma factor !1interaction domain homology KEYWORDS ATP; DNA binding; P-loop; phosphoprotein; signal !1transduction; transcription regulation FEATURE !$6-115 #domain response regulator homology #label RRH\ !$140-361 #domain RNA polymerase sigma factor interaction !8domain homology #label SFI\ !$167-174 #region nucleotide-binding motif A (P-loop) #status !8atypical\ !$234-238 #region nucleotide-binding motif B\ !$54 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 468 #molecular-weight 52196 #checksum 6001 SEQUENCE /// ENTRY S42745 #type complete TITLE nitrogen assimilation regulatory protein ntrC - Azospirillum brasilense ORGANISM #formal_name Azospirillum brasilense DATE 13-Jan-1995 #sequence_revision 05-Apr-1995 #text_change 16-Jul-1999 ACCESSIONS S42745; S35266 REFERENCE S42745 !$#authors Liang, Y. !$#submission submitted to the EMBL Data Library, August 1992 !$#accession S42745 !'##molecule_type DNA !'##residues 1-481 ##label LIA1 !'##cross-references EMBL:X67684; NID:g404254; PIDN:CAA47916.1; !1PID:g404256 REFERENCE S35265 !$#authors Liang, Y.Y.; Arsene, F.; Elmerich, C. !$#journal Mol. Gen. Genet. (1993) 240:188-196 !$#title Characterization of the ntrBC genes of Azospirillum !1brasilense Sp7: their involvement in the regulation of !1nitrogenase synthesis and activity. !$#cross-references MUID:93360897; PMID:8355653 !$#accession S35266 !'##molecule_type DNA !'##residues 1-3,'A',5-15,'D',18-481 ##label LIA2 !'##cross-references EMBL:X67684 COMMENT This protein may be part of a two-component regulatory !1system for nitrogen assimilation. COMMENT Under laboratory conditions of limited nitrogen, this !1protein is required for nif gene activation in free-living !1but not in symbiotic forms. GENETICS !$#gene ntrC CLASSIFICATION #superfamily nitrogen assimilation regulatory protein ntrC; !1response regulator homology; RNA polymerase sigma factor !1interaction domain homology KEYWORDS DNA binding; P-loop; phosphoprotein; transcription !1regulation; two-component regulatory system FEATURE !$6-115 #domain response regulator homology #label RRH\ !$141-362 #domain RNA polymerase sigma factor interaction !8domain homology #label SFI\ !$169-176 #region nucleotide-binding motif A (P-loop) #status !8atypical\ !$236-240 #region nucleotide-binding motif B\ !$451-470 #region helix-turn-helix motif\ !$54 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 481 #molecular-weight 53394 #checksum 3691 SEQUENCE /// ENTRY A26934 #type complete TITLE nitrogen assimilation regulatory protein ntrC - Rhizobium meliloti ORGANISM #formal_name Rhizobium meliloti DATE 19-Nov-1988 #sequence_revision 02-Jun-1994 #text_change 16-Jul-1999 ACCESSIONS A26934 REFERENCE A26934 !$#authors Szeto, W.W.; Nixon, B.T.; Ronson, C.W.; Ausubel, F.M. !$#journal J. Bacteriol. (1987) 169:1423-1432 !$#title Identification and characterization of the Rhizobium !1meliloti ntrC gene: R. meliloti has separate regulatory !1pathways for activation of nitrogen fixation genes in !1free-living and symbiotic cells. !$#cross-references MUID:87165745; PMID:2881918 !$#accession A26934 !'##molecule_type DNA !'##residues 1-482 ##label SZE !'##cross-references GB:M15810; NID:g152391; PIDN:AAA26346.1; !1PID:g152393 COMMENT This protein may be part of a two-component regulatory !1system for nitrogen assimilation. COMMENT Under laboratory conditions of limited nitrogen, this !1protein is required for nif gene activation in free-living !1but not in symbiotic forms. GENETICS !$#gene ntrC CLASSIFICATION #superfamily nitrogen assimilation regulatory protein ntrC; !1response regulator homology; RNA polymerase sigma factor !1interaction domain homology KEYWORDS DNA binding; P-loop; phosphoprotein; transcription !1regulation; two-component regulatory system FEATURE !$6-115 #domain response regulator homology #label RRH\ !$139-360 #domain RNA polymerase sigma factor interaction !8domain homology #label SFI\ !$167-174 #region nucleotide-binding motif A (P-loop) #status !8atypical\ !$234-238 #region nucleotide-binding motif B\ !$452-471 #region helix-turn-helix motif\ !$54 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 482 #molecular-weight 53585 #checksum 9950 SEQUENCE /// ENTRY B26499 #type complete TITLE nitrogen assimilation regulatory protein ntrC - Bradyrhizobium sp. ORGANISM #formal_name Bradyrhizobium sp. DATE 16-Aug-1988 #sequence_revision 02-Jun-1994 #text_change 16-Jul-1999 ACCESSIONS B26499 REFERENCE A94133 !$#authors Nixon, B.T.; Ronson, C.W.; Ausubel, F.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:7850-7854 !$#title Two-component regulatory systems responsive to environmental !1stimuli share strongly conserved domains with the nitrogen !1assimilation regulatory genes ntrB and ntrC. !$#cross-references MUID:87017043; PMID:3020561 !$#accession B26499 !'##molecule_type DNA !'##residues 1-480 ##label NIX !'##cross-references GB:M14227; NID:g152129; PIDN:AAA26239.1; !1PID:g152131 !'##note variety is strain RP501 isolated from Parasponia rigida nodules COMMENT This protein may be part of a two-component regulatory !1system for nitrogen assimilation. GENETICS !$#gene ntrC CLASSIFICATION #superfamily nitrogen assimilation regulatory protein ntrC; !1response regulator homology; RNA polymerase sigma factor !1interaction domain homology KEYWORDS DNA binding; P-loop; phosphoprotein; transcription !1regulation; two-component regulatory system FEATURE !$6-115 #domain response regulator homology #label RRH\ !$140-361 #domain RNA polymerase sigma factor interaction !8domain homology #label SFI\ !$168-175 #region nucleotide-binding motif A (P-loop) #status !8atypical\ !$235-239 #region nucleotide-binding motif B\ !$450-469 #region helix-turn-helix motif\ !$54 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 480 #molecular-weight 52893 #checksum 9656 SEQUENCE /// ENTRY A38449 #type complete TITLE regulatory protein algB - Pseudomonas aeruginosa ORGANISM #formal_name Pseudomonas aeruginosa DATE 12-Jul-1991 #sequence_revision 02-Jun-1994 #text_change 06-Oct-2000 ACCESSIONS A38449; S20030; B82960 REFERENCE A38449 !$#authors Wozniak, D.J.; Ohman, D.E. !$#journal J. Bacteriol. (1991) 173:1406-1413 !$#title Pseudomonas aeruginosa AlgB, a two-component response !1regulator of the NtrC family, is required for algD !1transcription. !$#cross-references MUID:91139582; PMID:1899859 !$#accession A38449 !'##molecule_type DNA !'##residues 1-449 ##label WOZ !'##cross-references GB:M62902; GB:M37765; NID:g150990; PIDN:AAA25700.1; !1PID:g150991 REFERENCE S20030 !$#authors Goldberg, J.B.; Dahnke, T. !$#journal Mol. Microbiol. (1992) 6:59-66 !$#title Pseudomonas aeruginosa AlgB, which modulates the expression !1of alginate, is a member of the NtrC subclass of prokaryotic !1regulators. !$#cross-references MUID:92149314; PMID:1738315 !$#accession S20030 !'##molecule_type DNA !'##residues 1-449 ##label GOL !'##cross-references EMBL:M82823 REFERENCE A82950 !$#authors Stover, C.K.; Pham, X.Q.; Erwin, A.L.; Mizoguchi, S.D.; !1Warrener, P.; Hickey, M.J.; Brinkman, F.S.L.; Hufnagle, !1W.O.; Kowalik, D.J.; Lagrou, M.; Garber, R.L.; Goltry, L.; !1Tolentino, E.; Westbrook-Wadman, S.; Yuan, Y.; Brody, L.L.; !1Coulter, S.N.; Folger, K.R.; Kas, A.; Larbig, K.; Lim, R.M.; !1Smith, K.A.; Spencer, D.H.; Wong, G.K.S.; Wu, Z.; Paulsen, !1I.T.; Reizer, J.; Saier, M.H.; Hancock, R.E.W.; Lory, S.; !1Olson, M.V. !$#journal Nature (2000) 406:959-964 !$#title Complete genome sequence of Pseudomonas aeruginosa PA01, an !1opportunistic pathogen. !$#cross-references MUID:20437337; PMID:10984043 !$#accession B82960 !'##status preliminary !'##molecule_type DNA !'##residues 1-449 ##label STO !'##cross-references GB:AE004961; GB:AE004091; NID:g9951814; !1PIDN:AAG08868.1; GSPDB:GN00131; PASP:PA5483 !'##experimental_source strain PAO1 COMMENT This protein is part of a two-component regulatory system !1for alginate biosynthesis. COMMENT Secretion of the polysaccharide alginate is responsible for !1mucoid colony morphology and resistance to phagocytosis, !1which is typical of chronic respiratory infections by this !1organism. GENETICS !$#gene algB; PA5483 !$#map_position 13 min CLASSIFICATION #superfamily nitrogen assimilation regulatory protein ntrC; !1response regulator homology; RNA polymerase sigma factor !1interaction domain homology KEYWORDS DNA binding; P-loop; phosphoprotein; transcription !1regulation; two-component regulatory system FEATURE !$11-120 #domain response regulator homology #label RRH\ !$147-369 #domain RNA polymerase sigma factor interaction !8domain homology #label SFI\ !$175-182 #region nucleotide-binding motif A (P-loop) #status !8atypical\ !$242-246 #region nucleotide-binding motif B\ !$426-445 #region helix-turn-helix motif\ !$59 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 449 #molecular-weight 49322 #checksum 559 SEQUENCE /// ENTRY B33862 #type complete TITLE transcription regulator hydG - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 09-Mar-1990 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS G65207; B33862 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65207 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-441 ##label BLAT !'##cross-references GB:AE000473; GB:U00096; NID:g2367336; !1PIDN:AAC76978.1; PID:g1790437; UWGP:b4004 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A33862 !$#authors Stoker, K.; Reijnders, W.N.M.; Oltmann, L.F.; Stouthamer, !1A.H. !$#journal J. Bacteriol. (1989) 171:4448-4456 !$#title Initial cloning and sequencing of hydHG, an operon !1homologous to ntrBC and regulating the labile hydrogenase !1activity in Escherichia coli K-12. !$#cross-references MUID:89327164; PMID:2666400 !$#accession B33862 !'##molecule_type DNA !'##residues 1-116,'WK',119,'R','S',123-160,'C',162-171,'AR',175-180, !1'GL',183-227,'P',229-236,'C',239-335,'RGKRFYA',343,'GL', !1347-384,'G',386-441 ##label STO !'##cross-references GB:M28369; NID:g146426; PIDN:AAA24004.1; !1PID:g146428 !'##note the authors translated the codon TGC for residue 161 as Ser COMMENT This protein may be part of a two-component regulatory !1system for the labile hydrogenase (hydrogenase 3). GENETICS !$#gene hydG CLASSIFICATION #superfamily nitrogen assimilation regulatory protein ntrC; !1response regulator homology; RNA polymerase sigma factor !1interaction domain homology KEYWORDS DNA binding; phosphoprotein; transcription regulation; !1two-component regulatory system FEATURE !$8-117 #domain response regulator homology #label RRH\ !$141-363 #domain RNA polymerase sigma factor interaction !8domain homology #label SFI\ !$421-440 #region helix-turn-helix motif\ !$56 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 441 #molecular-weight 48394 #checksum 4123 SEQUENCE /// ENTRY C33586 #type complete TITLE C4-dicarboxylate transport system regulatory protein - Rhizobium meliloti ORGANISM #formal_name Rhizobium meliloti DATE 16-Sep-1992 #sequence_revision 05-Apr-1995 #text_change 16-Jul-1999 ACCESSIONS C33586 REFERENCE A33586 !$#authors Jiang, J.; Gu, B.; Albright, L.M.; Nixon, B.T. !$#journal J. Bacteriol. (1989) 171:5244-5253 !$#title Conservation between coding and regulatory elements of !1Rhizobium meliloti and Rhizobium leguminosarum dct genes. !$#cross-references MUID:90008755; PMID:2793824 !$#accession C33586 !'##molecule_type DNA !'##residues 1-460 ##label JI3 !'##cross-references GB:M26531; NID:g152157; PIDN:AAA26250.1; !1PID:g152160 GENETICS !$#gene dctD CLASSIFICATION #superfamily nitrogen assimilation regulatory protein ntrC; !1response regulator homology; RNA polymerase sigma factor !1interaction domain homology KEYWORDS DNA binding; P-loop; phosphoprotein; transcription !1regulation; two-component regulatory system FEATURE !$7-116 #domain response regulator homology #label RRH\ !$145-367 #domain RNA polymerase sigma factor interaction !8domain homology #label SFI\ !$173-180 #region nucleotide-binding motif A (P-loop) #status !8atypical\ !$240-244 #region nucleotide-binding motif B\ !$55 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 460 #molecular-weight 50061 #checksum 6817 SEQUENCE /// ENTRY B26981 #type complete TITLE C4-dicarboxylate transport system regulatory protein - Rhizobium leguminosarum ORGANISM #formal_name Rhizobium leguminosarum DATE 20-Jun-1989 #sequence_revision 05-Apr-1995 #text_change 16-Jul-1999 ACCESSIONS B26981; S25703 REFERENCE A93675 !$#authors Ronson, C.W.; Astwood, P.M.; Nixon, B.T.; Ausubel, F.M. !$#journal Nucleic Acids Res. (1987) 15:7921-7934 !$#title Deduced products of C4-dicarboxylate transport regulatory !1genes of Rhizobium leguminosarum are homologous to nitrogen !1regulatory gene products. !$#cross-references MUID:88040418; PMID:3671068 !$#accession B26981 !'##molecule_type DNA !'##residues 1-448 ##label RON !'##cross-references EMBL:Z11529; NID:g46177; PIDN:CAA77620.1; !1PID:g46180 GENETICS !$#gene dctD CLASSIFICATION #superfamily nitrogen assimilation regulatory protein ntrC; !1response regulator homology; RNA polymerase sigma factor !1interaction domain homology KEYWORDS DNA binding; phosphoprotein; transcription regulation; !1two-component regulatory system FEATURE !$7-116 #domain response regulator homology #label RRH\ !$145-367 #domain RNA polymerase sigma factor interaction !8domain homology #label SFI\ !$55 #binding_site phosphate (Asp) (covalent) #status !8predicted SUMMARY #length 448 #molecular-weight 49484 #checksum 7269 SEQUENCE /// ENTRY RGASWA #type complete TITLE regulatory protein wetA - Emericella nidulans ORGANISM #formal_name Emericella nidulans, Aspergillus nidulans DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jul-1999 ACCESSIONS A39665 REFERENCE A39665 !$#authors Marshall, M.A.; Timberlake, W.E. !$#journal Mol. Cell. Biol. (1991) 11:55-62 !$#title Aspergillus nidulans wetA activates spore-specific gene !1expression. !$#cross-references MUID:91094871; PMID:1986246 !$#accession A39665 !'##molecule_type DNA !'##residues 1-555 ##label MAR !'##cross-references GB:M60528; GB:M35758; NID:g168108; PIDN:AAA33330.1; !1PID:g168109 COMMENT The products of the genes brlA, abaA, and wetA are required !1for activation of most genes involved in asexual !1reproductive development. GENETICS !$#gene wetA CLASSIFICATION #superfamily regulatory protein wetA KEYWORDS transcription regulation SUMMARY #length 555 #molecular-weight 60275 #checksum 5963 SEQUENCE /// ENTRY RGECK #type complete TITLE regulatory protein lysR - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 20-Sep-1984 #sequence_revision 20-Sep-1984 #text_change 01-Mar-2002 ACCESSIONS A03565; H65066 REFERENCE A92901 !$#authors Stragier, P.; Patte, J.C. !$#journal J. Mol. Biol. (1983) 168:333-350 !$#title Regulation of diaminopimelate decarboxylase synthesis in !1Escherichia coli. III. Nucleotide sequence and regulation of !1the lysR gene. !$#cross-references MUID:83294517; PMID:6350602 !$#accession A03565 !'##molecule_type DNA !'##residues 1-311 ##label STR !'##cross-references GB:J01614; NID:g146067; PIDN:AAA83862.1; !1PID:g146070 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65066 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-311 ##label BLAT !'##cross-references GB:AE000367; GB:U00096; NID:g1789195; !1PIDN:AAC75878.1; PID:g1789204; UWGP:b2839 !'##experimental_source strain K-12, substrain MG1655 COMMENT This dual-function regulatory protein is required for the !1expression of the lysA gene (encoding diaminopimelate !1decarboxylase) but represses the expression of its own gene. GENETICS !$#gene lysR !$#map_position 61 min CLASSIFICATION #superfamily regulatory protein lysR KEYWORDS DNA binding; transcription regulation FEATURE !$21-46 #region regulatory protein lysR motif SUMMARY #length 311 #molecular-weight 34364 #checksum 1454 SEQUENCE /// ENTRY RGECCB #type complete TITLE regulatory protein cysB - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 01-Mar-2002 ACCESSIONS A26695; A34564; S22374; F64875 REFERENCE A92642 !$#authors Ostrowski, J.; Jagura-Burdzy, G.; Kredich, N.M. !$#journal J. Biol. Chem. (1987) 262:5999-6005 !$#title DNA sequences of the cysB regions of Salmonella typhimurium !1and Escherichia coli. !$#cross-references MUID:87194810; PMID:3032952 !$#accession A26695 !'##molecule_type DNA !'##residues 1-324 ##label OST !'##cross-references GB:M15041; GB:J02687; NID:g145663; PIDN:AAA23642.1; !1PID:g145665 REFERENCE A34564 !$#authors Tei, H.; Watanabe, K.; Murata, K.; Kimura, A. !$#journal Biochem. Biophys. Res. Commun. (1990) 167:962-969 !$#title Analysis of the Escherichia coli K-12 CYSB gene and its !1product using the method of gene fusion. !$#cross-references MUID:90211344; PMID:2182030 !$#accession A34564 !'##molecule_type DNA !'##residues 1-324 ##label TEI !'##cross-references GB:M34332; NID:g145666; PIDN:AAA23643.1; !1PID:g145667 REFERENCE S22374 !$#authors Prodromou, C.; Artymiuk, P.J.; Guest, J.R. !$#journal Eur. J. Biochem. (1992) 204:599-609 !$#title The aconitase of Escherichia coli. Nucleotide sequence of !1the aconitase gene and amino acid sequence similarity with !1mitochondrial aconitases, the !1iron-responsive-element-binding protein and isopropylmalate !1isomerases. !$#cross-references MUID:92174916; PMID:1541275 !$#accession S22374 !'##molecule_type DNA !'##residues 249-324 ##label PRO !'##cross-references EMBL:X60293; NID:g40894; PIDN:CAA42833.1; !1PID:g40895 !'##experimental_source strain K-12, substrain W3110 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64875 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-324 ##label BLAT !'##cross-references GB:AE000225; GB:U00096; NID:g1787523; !1PIDN:AAC74357.1; PID:g1787530; UWGP:b1275 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene cysB !$#map_position 28 min FUNCTION !$#description a positive regulator of gene expression for the cysteine !1regulon, a system of genes involved in L-cysteine !1biosynthesis from inorganic sulfate !$#note inducer for cysB is acetylserine; autoregulation of cysB CLASSIFICATION #superfamily regulatory protein lysR KEYWORDS DNA binding; transcription regulation FEATURE !$19-44 #region regulatory protein lysR motif SUMMARY #length 324 #molecular-weight 36150 #checksum 792 SEQUENCE /// ENTRY RGEBCB #type complete TITLE regulatory protein cysB - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 16-Jul-1999 ACCESSIONS B26695 REFERENCE A92642 !$#authors Ostrowski, J.; Jagura-Burdzy, G.; Kredich, N.M. !$#journal J. Biol. Chem. (1987) 262:5999-6005 !$#title DNA sequences of the cysB regions of Salmonella typhimurium !1and Escherichia coli. !$#cross-references MUID:87194810; PMID:3032952 !$#accession B26695 !'##molecule_type DNA !'##residues 1-324 ##label OST !'##cross-references GB:M15040; GB:J02687; NID:g153925; PIDN:AAA27045.1; !1PID:g153927 GENETICS !$#gene cysB !$#map_position 33 min COMPLEX homotetramer FUNCTION !$#description a positive regulator of gene expression for the cysteine !1regulon, a system of genes involved in L-cysteine !1biosynthesis from inorganic sulfate !$#note inducer for cysB is acetylserine; autoregulation of cysB CLASSIFICATION #superfamily regulatory protein lysR KEYWORDS DNA binding; homotetramer; transcription regulation FEATURE !$19-44 #region regulatory protein lysR motif SUMMARY #length 324 #molecular-weight 36013 #checksum 205 SEQUENCE /// ENTRY S21410 #type complete TITLE nodulation protein nodD3 - Rhizobium loti ORGANISM #formal_name Rhizobium loti DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 22-Oct-1999 ACCESSIONS S21410 REFERENCE S21410 !$#authors Scott, D.B.; Young, C.A.; Collins-Emerson, J.M.; Terzaghi, !1E.A.; Rockman, E.S.; Lewis, P.E.; Pankhurst, C.E. !$#submission submitted to the EMBL Data Library, April 1992 !$#description Mutational and structural analysis of Rhizobium loti !1nodulation genes. !$#accession S21410 !'##status preliminary !'##molecule_type DNA !'##residues 1-301 ##label SCO !'##cross-references GB:U22899; EMBL:X65619; NID:g780549; !1PIDN:AAB50274.1; PID:g780551 GENETICS !$#gene nodD3 CLASSIFICATION #superfamily regulatory protein lysR KEYWORDS nodulation SUMMARY #length 301 #molecular-weight 34262 #checksum 7354 SEQUENCE /// ENTRY ZZZRDM #type complete TITLE nodulation protein nodD - Rhizobium meliloti ORGANISM #formal_name Rhizobium meliloti DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 16-Jul-1999 ACCESSIONS A03566; A25788; A28379 REFERENCE A90951 !$#authors Egelhoff, T.T.; Fisher, R.F.; Jacobs, T.W.; Mulligan, J.T.; !1Long, S.R. !$#journal DNA (1985) 4:241-248 !$#title Nucleotide sequence of Rhizobium meliloti 1021 nodulation !1genes: nodD is read divergently from modABC. !$#cross-references MUID:85229955; PMID:4006668 !$#accession A03566 !'##molecule_type DNA !'##residues 1-311 ##label EGE !'##cross-references GB:M11268 !'##experimental_source strain 1021 REFERENCE A92932 !$#authors Goettfert, M.; Horvath, B.; Kondorosi, E.; Putnoky, P.; !1Rodriguez-Quinones, F.; Kondorosi, A. !$#journal J. Mol. Biol. (1986) 191:411-420 !$#title At least two nodD genes are necessary for efficient !1nodulation of alfalfa by Rhizobium meliloti. !$#cross-references MUID:87141170; PMID:3820290 !$#accession A25788 !'##molecule_type DNA !'##residues 4-311 ##label GOE !'##cross-references GB:X04473; NID:g46293; PIDN:CAA28161.1; PID:g46294 !'##experimental_source strain 41 REFERENCE A91851 !$#authors Aguilar, O.M.; Reilaender, H.; Arnold, W.; Puehler, A. !$#journal J. Bacteriol. (1987) 169:5393-5400 !$#title Rhizobium meliloti nifN (fixF) gene is part of an operon !1regulated by a nifA-dependent promoter and codes for a !1polypeptide homologous to the nifK gene product. !$#cross-references MUID:88058743; PMID:3316182 !$#accession A28379 !'##molecule_type DNA !'##residues 91-311 ##label AGU !'##cross-references GB:M18272; NID:g152217; PIDN:AAA88518.1; !1PID:g152218 !'##experimental_source strain 2011 COMMENT This is one of the proteins, coded by nodulation genes, that !1are required for R. meliloti to invade and stimulate nodule !1formation in its leguminous hosts. Three nodD proteins (i.e. !1nodD1, nodD2, and nodD3) are used to mediate the !1host-specific activation of the nodABC genes and to optimize !1the interaction of R. meliloti with each of its hosts. GENETICS !$#gene nodD1 CLASSIFICATION #superfamily regulatory protein lysR KEYWORDS DNA binding; nodulation; transcription regulation FEATURE !$26-51 #region regulatory protein lysR motif SUMMARY #length 311 #molecular-weight 35245 #checksum 2126 SEQUENCE /// ENTRY B25788 #type complete TITLE nodulation protein nodD2 - Rhizobium meliloti ORGANISM #formal_name Rhizobium meliloti DATE 02-Jun-1988 #sequence_revision 13-Jan-1995 #text_change 20-Feb-1998 ACCESSIONS B25788; A35117 REFERENCE A92932 !$#authors Goettfert, M.; Horvath, B.; Kondorosi, E.; Putnoky, P.; !1Rodriguez-Quinones, F.; Kondorosi, A. !$#journal J. Mol. Biol. (1986) 191:411-420 !$#title At least two nodD genes are necessary for efficient !1nodulation of alfalfa by Rhizobium meliloti. !$#cross-references MUID:87141170; PMID:3820290 !$#accession B25788 !'##molecule_type DNA !'##residues 1-310 ##label GOE !'##cross-references GB:X04473 !'##experimental_source strain 41 REFERENCE A35117 !$#authors Honma, M.A.; Asomaning, M.; Ausubel, F.M. !$#journal J. Bacteriol. (1990) 172:901-911 !$#title Rhizobium meliloti nodD genes mediate host-specific !1activation of nodABC. !$#cross-references MUID:90130327; PMID:2298703 !$#accession A35117 !'##molecule_type DNA !'##residues 1-87,'D',89-107,'I',109-118,'V',120-255,'T',257-267,'P', !1269-310 ##label HON !'##cross-references GB:M29367 !'##experimental_source strain 1201 COMMENT This is one of the proteins, coded by nodulation genes, that !1are required for this bacterium to invade and stimulate !1nodule formation in its hosts. Three nodD proteins (nodD1, !1nodD2, and nodD3) are used to mediate the host-specific !1activation of the nodABC genes and to optimize the !1interaction of the bacterium with each of its hosts. GENETICS !$#gene nodD2 CLASSIFICATION #superfamily regulatory protein lysR KEYWORDS DNA binding; nodulation; transcription regulation FEATURE !$23-48 #region regulatory protein lysR motif SUMMARY #length 310 #molecular-weight 35301 #checksum 922 SEQUENCE /// ENTRY A25095 #type complete TITLE nodulation protein nodD - Rhizobium leguminosarum ORGANISM #formal_name Rhizobium leguminosarum DATE 05-Oct-1988 #sequence_revision 13-Jan-1995 #text_change 16-Jul-1999 ACCESSIONS A25095 REFERENCE A25095 !$#authors Shearman, C.A.; Rossen, L.; Johnston, A.W.B.; Downie, J.A. !$#journal EMBO J. (1986) 5:647-652 !$#title The Rhizobium leguminosarum nodulation gene nodF encodes a !1polypeptide similar to acyl-carrier protein and is regulated !1by nodD plus a factor in pea root exudate. !$#accession A25095 !'##molecule_type DNA !'##residues 1-303 ##label SHE !'##cross-references EMBL:Y00548; NID:g46212; PIDN:CAA68622.1; !1PID:g46218 GENETICS !$#gene nodD CLASSIFICATION #superfamily regulatory protein lysR KEYWORDS DNA binding; transcription regulation FEATURE !$23-48 #region regulatory protein lysR motif SUMMARY #length 303 #molecular-weight 34486 #checksum 9323 SEQUENCE /// ENTRY D23766 #type complete TITLE nodulation protein nodD - Rhizobium leguminosarum bv. trifolii ORGANISM #formal_name Rhizobium leguminosarum bv. trifolii DATE 21-May-1988 #sequence_revision 13-Jan-1995 #text_change 28-May-1999 ACCESSIONS D23766 REFERENCE A93614 !$#authors Schofield, P.R.; Watson, J.M. !$#journal Nucleic Acids Res. (1986) 14:2891-2903 !$#title DNA sequence of Rhizobium trifolii nodulation genes reveals !1a reiterated and potentially regulatory sequence preceding !1nodABC and nodFE. !$#cross-references MUID:86176774; PMID:3008100 !$#accession D23766 !'##molecule_type DNA !'##residues 1-318 ##label SCH !'##cross-references GB:X03721; NID:g46461; PIDN:CAA27354.1; PID:g46465 !'##experimental_source strain ANU843 COMMENT This is one of the proteins, coded by nodulation genes, that !1are required for this bacterium to invade and stimulate !1nodule formation in its hosts. It is involved in mediating !1the host-specific activation of the nodABC genes. GENETICS !$#gene nodD CLASSIFICATION #superfamily regulatory protein lysR KEYWORDS DNA binding; nodulation; transcription regulation FEATURE !$23-48 #region regulatory protein lysR motif SUMMARY #length 318 #molecular-weight 36099 #checksum 1242 SEQUENCE /// ENTRY S00054 #type complete TITLE nodulation protein nodD1 - Rhizobium sp. plasmid ORGANISM #formal_name Rhizobium sp. DATE 07-Sep-1990 #sequence_revision 13-Jan-1995 #text_change 16-Jul-1999 ACCESSIONS S00054 REFERENCE S00054 !$#authors Horvath, B.; Bachem, C.W.B.; Schell, J.; Kondorosi, A. !$#journal EMBO J. (1987) 6:841-848 !$#title Host-specific regulation of nodulation genes in Rhizobium is !1mediated by a plant-signal, interacting with the nodD gene !1product. !$#accession S00054 !'##molecule_type DNA !'##residues 1-322 ##label HOR !'##cross-references EMBL:Y00059; NID:g46434; PIDN:CAA68267.1; !1PID:g46435 !'##experimental_source strain MPIK3030 symbiotic plasmid COMMENT This is one of the proteins, coded by nodulation genes, that !1are required for this bacterium to invade and stimulate !1nodule formation in its hosts. It is involved in mediating !1the host-specific activation of the nodABC genes. GENETICS !$#gene nodD1 !$#genome plasmid CLASSIFICATION #superfamily regulatory protein lysR KEYWORDS DNA binding; nodulation; transcription regulation FEATURE !$23-48 #region regulatory protein lysR motif SUMMARY #length 322 #molecular-weight 36558 #checksum 252 SEQUENCE /// ENTRY A28663 #type complete TITLE nodulation protein nodD1 - Bradyrhizobium japonicum ORGANISM #formal_name Bradyrhizobium japonicum DATE 31-Dec-1988 #sequence_revision 13-Jan-1995 #text_change 16-Jul-1999 ACCESSIONS A28663 REFERENCE A28663 !$#authors Appelbaum, E.R.; Thompson, D.V.; Idler, K.; Chartrain, N. !$#journal J. Bacteriol. (1988) 170:12-20 !$#title Rhizobium japonicum USDA 191 has two nodD genes that differ !1in primary structure and function. !$#cross-references MUID:88086856; PMID:2826389 !$#accession A28663 !'##molecule_type DNA !'##residues 1-321 ##label APP !'##cross-references GB:M18971; NID:g152357; PIDN:AAA26334.1; !1PID:g152358 COMMENT This is one of the proteins, coded by nodulation genes, that !1are required for this bacterium to invade and stimulate !1nodule formation in its hosts. It is involved in mediating !1the host-specific activation of the nodABC genes. GENETICS !$#gene nodD1 CLASSIFICATION #superfamily regulatory protein lysR KEYWORDS DNA binding; nodulation; transcription regulation FEATURE !$23-48 #region regulatory protein lysR motif SUMMARY #length 321 #molecular-weight 36388 #checksum 8442 SEQUENCE /// ENTRY B28663 #type complete TITLE nodulation protein nodD2 - Bradyrhizobium japonicum ORGANISM #formal_name Bradyrhizobium japonicum DATE 31-Dec-1988 #sequence_revision 13-Jan-1995 #text_change 20-Feb-1998 ACCESSIONS B28663 REFERENCE A28663 !$#authors Appelbaum, E.R.; Thompson, D.V.; Idler, K.; Chartrain, N. !$#journal J. Bacteriol. (1988) 170:12-20 !$#title Rhizobium japonicum USDA 191 has two nodD genes that differ !1in primary structure and function. !$#cross-references MUID:88086856; PMID:2826389 !$#accession B28663 !'##molecule_type DNA !'##residues 1-312 ##label APP !'##cross-references GB:M18972 COMMENT This is one of the proteins, coded by nodulation genes, that !1are required for this bacterium to invade and stimulate !1nodule formation in its hosts. It is involved in mediating !1the host-specific activation of the nodABC genes. GENETICS !$#gene nodD2 CLASSIFICATION #superfamily regulatory protein lysR KEYWORDS DNA binding; nodulation; transcription regulation FEATURE !$23-48 #region regulatory protein lysR motif SUMMARY #length 312 #molecular-weight 35294 #checksum 9320 SEQUENCE /// ENTRY A40642 #type complete TITLE nodulation protein nodD1 - Rhizobium tropici ORGANISM #formal_name Rhizobium tropici DATE 21-Sep-1993 #sequence_revision 13-Jan-1995 #text_change 16-Jul-1999 ACCESSIONS A40642; S39577 REFERENCE A40642 !$#authors van Rhijn, P.J.; Feys, B.; Verreth, C.; Vanderleyden, J. !$#journal J. Bacteriol. (1993) 175:438-447 !$#title Multiple copies of nodD in Rhizobium tropici CIAT899 and !1BR816. !$#cross-references MUID:93123162; PMID:8419293 !$#accession A40642 !'##molecule_type DNA !'##residues 1-308 ##label VAN !'##cross-references GB:L01273; NID:g152359; PIDN:AAA26335.1; !1PID:g152360 !'##experimental_source strain CIAT899 !'##note sequence extracted from NCBI backbone (NCBIN:122448, !1NCBIP:122450) REFERENCE S39577 !$#authors Sousa, C.; Folch, J.L.; Boloix, P.; Megias, M.; Nava, N.; !1Quinto, C. !$#journal Mol. Microbiol. (1993) 9:1157-1168 !$#title A Rhizobium tropici DNA region carrying the amino-terminal !1half of a nodD gene and a nod-box-like sequence confers !1host-range extension. !$#cross-references MUID:95020647; PMID:7934929 !$#accession S39577 !'##molecule_type DNA !'##residues 1-308 ##label SOU !'##cross-references EMBL:L04660; NID:g152355; PIDN:AAA65533.1; !1PID:g152356 COMMENT This is one of the proteins, coded by nodulation genes, that !1are required for this bacterium to invade and stimulate !1nodule formation in its hosts. It is involved in mediating !1the host-specific activation of the nodABC genes. GENETICS !$#gene nodD1 CLASSIFICATION #superfamily regulatory protein lysR KEYWORDS DNA binding; nodulation; transcription regulation FEATURE !$23-48 #region regulatory protein lysR motif SUMMARY #length 308 #molecular-weight 35080 #checksum 141 SEQUENCE /// ENTRY B40642 #type complete TITLE nodulation protein nodD2 - Rhizobium tropici ORGANISM #formal_name Rhizobium tropici DATE 21-Sep-1993 #sequence_revision 13-Jan-1995 #text_change 16-Jul-1999 ACCESSIONS B40642 REFERENCE A40642 !$#authors van Rhijn, P.J.; Feys, B.; Verreth, C.; Vanderleyden, J. !$#journal J. Bacteriol. (1993) 175:438-447 !$#title Multiple copies of nodD in Rhizobium tropici CIAT899 and !1BR816. !$#cross-references MUID:93123162; PMID:8419293 !$#accession B40642 !'##molecule_type DNA !'##residues 1-314 ##label VAN !'##cross-references GB:L01272; NID:g152365; PIDN:AAA26338.1; !1PID:g152366 !'##experimental_source strain BR81699 !'##note sequence extracted from NCBI backbone (NCBIN:122456, !1NCBIP:122457) COMMENT This is one of the proteins, coded by nodulation genes, that !1are required for this bacterium to invade and stimulate !1nodule formation in its hosts. It is involved in mediating !1the host-specific activation of the nodABC genes. GENETICS !$#gene nodD2 CLASSIFICATION #superfamily regulatory protein lysR KEYWORDS DNA binding; nodulation; transcription regulation FEATURE !$23-48 #region regulatory protein lysR motif SUMMARY #length 314 #molecular-weight 35440 #checksum 8165 SEQUENCE /// ENTRY D26813 #type complete TITLE nodulation protein nodD - Bradyrhizobium sp. ORGANISM #formal_name Bradyrhizobium sp. DATE 19-Nov-1988 #sequence_revision 13-Jan-1995 #text_change 16-Jul-1999 ACCESSIONS D26813 REFERENCE A93615 !$#authors Scott, K.F. !$#journal Nucleic Acids Res. (1986) 14:2905-2919 !$#title Conserved nodulation genes from the non-legume symbiont !1Bradyrhizobium sp. (Parasponia). !$#cross-references MUID:86176775; PMID:3960737 !$#accession D26813 !'##molecule_type DNA !'##residues 1-338 ##label SCO !'##cross-references GB:X03720; NID:g39996; PIDN:CAA27346.1; PID:g39997 COMMENT This is one of the proteins, coded by nodulation genes, that !1are required for this bacterium to invade and stimulate !1nodule formation in its hosts. It is involved in mediating !1the host-specific activation of the nodABC genes. GENETICS !$#gene nodD CLASSIFICATION #superfamily regulatory protein lysR KEYWORDS DNA binding; nodulation; transcription regulation FEATURE !$23-48 #region regulatory protein lysR motif SUMMARY #length 338 #molecular-weight 38541 #checksum 8951 SEQUENCE /// ENTRY A35268 #type complete TITLE nudulation protein nodD - Azorhizobium caulinodans ORGANISM #formal_name Azorhizobium caulinodans DATE 10-Aug-1990 #sequence_revision 13-Jan-1995 #text_change 16-Jul-1999 ACCESSIONS A35268 REFERENCE A35268 !$#authors Goethals, K.; Van den Eede, G.; Van Montagu, M.; Holsters, !1M. !$#journal J. Bacteriol. (1990) 172:2658-2666 !$#title Identification and characterization of a functional nodD !1gene in Azorhizobium caulinodans ORS571. !$#cross-references MUID:90236930; PMID:2158977 !$#accession A35268 !'##molecule_type DNA !'##residues 1-314 ##label GOE !'##cross-references GB:M60872; NID:g152069; PIDN:AAA26190.1; !1PID:g152070 COMMENT This is one of the proteins, coded by nodulation genes, that !1are required for this bacterium to invade and stimulate !1nodule formation in its hosts. It is involved in mediating !1the host-specific activation of the nodABC genes. GENETICS !$#gene nodD CLASSIFICATION #superfamily regulatory protein lysR KEYWORDS DNA binding; nodulation; transcription regulation FEATURE !$23-48 #region regulatory protein lysR motif SUMMARY #length 314 #molecular-weight 35581 #checksum 2786 SEQUENCE /// ENTRY QQECE1 #type complete TITLE regulatory protein asnC - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 01-Mar-2002 ACCESSIONS A04434; H65177 REFERENCE A01191 !$#authors Nakamura, M.; Yamada, M.; Hirota, Y.; Sugimoto, K.; Oka, A.; !1Takanami, M. !$#journal Nucleic Acids Res. (1981) 9:4669-4676 !$#title Nucleotide sequence of the asnA gene coding for asparagine !1synthetase of E.coli K-12. !$#cross-references MUID:82059491; PMID:6117826 !$#accession A04434 !'##molecule_type DNA !'##residues 1-152 ##label NAK !'##cross-references GB:X02820 !'##experimental_source strain K12 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65177 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-152 ##label BLAT !'##cross-references GB:AE000451; GB:U00096; NID:g2367272; !1PIDN:AAC76766.1; PID:g1790182; UWGP:b3743 !'##experimental_source strain K-12, substrain MG1655 COMMENT This is a regulatory protein that controls expression of the !1asnA gene positively and its own synthesis negatively; the !1asnA gene codes for asparagine synthetase A. GENETICS !$#gene asnC !$#map_position 84 min CLASSIFICATION #superfamily regulatory protein asnC KEYWORDS DNA binding; transcription regulation SUMMARY #length 152 #molecular-weight 16887 #checksum 8459 SEQUENCE /// ENTRY RGECLR #type complete TITLE leucine-responsive transcription regulator lrp [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 01-Mar-2002 ACCESSIONS JH0412; I59240; H64827 REFERENCE JH0412 !$#authors Willins, D.A.; Ryan, C.W.; Platko, J.V.; Calvo, J.M. !$#journal J. Biol. Chem. (1991) 266:10768-10774 !$#title Characterization of Lrp, an Escherichia coli regulatory !1protein that mediates a global response to leucine. !$#cross-references MUID:91250369; PMID:2040596 !$#accession JH0412 !'##molecule_type DNA !'##residues 1-164 ##label WIL !'##cross-references GB:M35869; NID:g146664; PIDN:AAA24089.1; !1PID:g146665 REFERENCE I59240 !$#authors Ito, K.; Kawakami, K.; Nakamura, Y. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:302-306 !$#title Multiple control of Escherichia coli lysyl-tRNA synthetase !1expression involves a transcriptional repressor and a !1translational enhancer element. !$#cross-references MUID:93126364; PMID:7678344 !$#accession I59240 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-164 ##label RES !'##cross-references GB:D11105; NID:g216585; PIDN:BAA01880.1; !1PID:g216586 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64827 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-164 ##label BLAT !'##cross-references GB:AE000191; GB:U00096; NID:g1787115; !1PIDN:AAC73975.1; PID:g1787116; UWGP:b0889 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene lrp; alsB; livR COMPLEX homodimer [validated, MUID:91250369] FUNCTION !$#description activates a number of operons in response to the presence of !1exogenous leucine; regulates branched-chain amino acid !1transport genes CLASSIFICATION #superfamily regulatory protein asnC KEYWORDS DNA binding; homodimer; transcription regulation FEATURE !$2-164 #product leucine-responsive regulatory protein !8#status experimental #label MAT\ !$30-56 #region helix-turn-helix motif SUMMARY #length 164 #molecular-weight 18887 #checksum 1979 SEQUENCE /// ENTRY RGECMJ #type complete TITLE Met regulon regulatory protein metJ - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 01-Mar-2002 ACCESSIONS A22660; S40881; I54931; E65200 REFERENCE A22660 !$#authors Saint-Girons, I.; Duchange, N.; Cohen, G.N.; Zakin, M.M. !$#journal J. Biol. Chem. (1984) 259:14282-14285 !$#title Structure and autoregulation of the metJ regulatory gene in !1Escherichia coli. !$#cross-references MUID:85054884; PMID:6094549 !$#accession A22660 !'##molecule_type DNA !'##residues 1-105 ##label SAI !'##cross-references GB:M12869; NID:g146836; PIDN:AAA24163.1; !1PID:g146837 REFERENCE S40802 !$#authors Plunkett III, G.; Burland, V.; Daniels, D.L.; Blattner, F.R. !$#journal Nucleic Acids Res. (1993) 21:3391-3398 !$#title Analysis of the Escherichia coli genome. III. DNA sequence !1of the region from 87.2 to 89.2 minutes. !$#cross-references MUID:93347969; PMID:8346018 !$#accession S40881 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-105 ##label PLU !'##cross-references EMBL:L19201; NID:g304961; PIDN:AAB03070.1; !1PID:g305041 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1993 REFERENCE I54931 !$#authors Collier, C.D.; Johnson, J.R. !$#journal J. Bacteriol. (1990) 172:3918-3924 !$#title The Escherichia coli K-12 metJ193 allele contains a point !1mutation which alters the hydrophobic pocket responsible for !1in vitro binding of S-adenosylmethionine: Effects on cell !1growth and induction of met regulon expression. !$#cross-references MUID:90299817; PMID:2141834 !$#accession I54931 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-105 ##label RES !'##cross-references GB:M38202; NID:g146834; PIDN:AAA24162.1; !1PID:g146835 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65200 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-105 ##label BLAT !'##cross-references GB:AE000467; GB:U00096; NID:g1790356; !1PIDN:AAC76920.1; PID:g1790373; UWGP:b3938 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene metJ !$#map_position 89 min FUNCTION !$#description when combined with methionine, represses the expression of !1the methionine regulon; it is also autoregulated CLASSIFICATION #superfamily metJ protein KEYWORDS DNA binding; transcription regulation FEATURE !$2-105 #product Met regulon regulatory protein metJ #status !8predicted #label MAT SUMMARY #length 105 #molecular-weight 12141 #checksum 6426 SEQUENCE /// ENTRY RGECP2 #type complete TITLE nitrogen regulatory protein P-II.1 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 10-Nov-1995 #text_change 01-Mar-2002 ACCESSIONS C49940; S15991; A29307; S37753; H65032; S31961 REFERENCE A49940 !$#authors Liu, J.; Magasanik, B. !$#journal J. Bacteriol. (1993) 175:7441-7449 !$#title The glnB region of the Escherichia coli chromosome. !$#cross-references MUID:94042920; PMID:8226691 !$#accession C49940 !'##status preliminary !'##molecule_type DNA !'##residues 1-112 ##label LIU !'##cross-references GB:S67014; NID:g455660; PIDN:AAB28779.1; !1PID:g455663 !'##note sequence extracted from NCBI backbone (NCBIN:139878, !1NCBIP:139882) REFERENCE S15991 !$#authors Vasudevan, S.G.; Armarego, W.L.F.; Shaw, D.C.; Lilley, P.E.; !1Dixon, N.E.; Poole, R.K. !$#journal Mol. Gen. Genet. (1991) 226:49-58 !$#title Isolation and nucleotide sequence of the hmp gene that !1encodes a haemoglobin-like protein in Escherichia coli K-12. !$#cross-references MUID:91238719; PMID:2034230 !$#accession S15991 !'##status preliminary !'##molecule_type DNA !'##residues 1-112 ##label VAS !'##cross-references GB:X58872; NID:g41730; PIDN:CAA41683.1; PID:g41732 !'##experimental_source strain K-12 REFERENCE A29307 !$#authors Son, H.S.; Rhee, S.G. !$#journal J. Biol. Chem. (1987) 262:8690-8695 !$#title Cascade control of Escherichia coli glutamine synthetase: !1purification and properties of P-II protein and nucleotide !1sequence of its structural gene. !$#cross-references MUID:87250488; PMID:2885322 !$#accession A29307 !'##molecule_type DNA !'##residues 1-18,'R',20-80,'E',83-102,'VP' ##label SON !'##cross-references GB:M16778; NID:g146165; PIDN:AAA23883.1; !1PID:g146166 REFERENCE S36254 !$#authors van Heeswijk, W.C.; Rabenberg, M.; Westerhoff, H.V.; Kahn, !1D. !$#journal Mol. Microbiol. (1993) 9:443-457 !$#title The genes of the glutamine synthetase adenylylation cascade !1are not regulated by nitrogen in Escherichia coli. !$#cross-references MUID:94018640; PMID:8412694 !$#accession S37753 !'##status preliminary !'##molecule_type DNA !'##residues 1-12 ##label VAN !'##cross-references EMBL:Z21843; NID:g49395; PIDN:CAA79890.1; !1PID:g49397 !'##experimental_source strain K-12, substrain W3110 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65032 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-112 ##label BLAT !'##cross-references GB:AE000341; GB:U00096; NID:g1788899; !1PIDN:AAC75606.1; PID:g1788904; UWGP:b2553 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene glnB FUNCTION GEN !$#pathway nitrogen regulation pathway !$#note this protein participates indirectly in activation of !1glutamine synthase activity as well as in transcription !1activation of the glutamine synthase gene !$#note under nitrogen-limiting conditions it is covalently !1uridylylated; in nitrogen excess it is de-uridylylated; !1uridylylation and de-uridylylation are both catalyzed by the !1same protein, uridylyltransferase / uridylyl-removing enzyme !1which is regulated by the glutamine/alpha-ketoglutarate !1ratio FUNCTION NTRB !$#description de-uridylylated P-II forms a complex with nitrogen !1regulation protein II (ntrB); ntrB, when complexed with !1de-uridylylated P-II, dephosphorylates nitrogen regulation !1protein I (ntrC); the uridylylated form of P-II does not !1complex with ntrB; free ntrB phosphorylates nitrogen !1regulation protein I (ntrC) !$#note phosphorylated nitrogen regulation protein I (ntrC) !1activates transcription of the glutamine synthase (glnA) !1gene FUNCTION ATR !$#description uridylylated P-II forms a complex with adenylyltransferase; !1this complex adenylylates glutamine synthase; !1de-uridylylated protein does not form a complex !1adenylyltransferase; free adenylyltransferase deadenylylates !1glutamine synthase !$#note free glutamine synthase is active; adenylylated glutamine !1synthase is inactive CLASSIFICATION #superfamily regulatory protein P-II KEYWORDS phosphoprotein; signal transduction FEATURE !$51 #binding_site UMP (Tyr) (covalent) #status !8experimental SUMMARY #length 112 #molecular-weight 12425 #checksum 9901 SEQUENCE /// ENTRY RGECIY #type complete TITLE regulatory protein ilvY - Escherichia coli (strain K-12) ALTERNATE_NAMES ilvC activator ilvY ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 01-Mar-2002 ACCESSIONS B26287; H65180; S30671 REFERENCE A92575 !$#authors Wek, R.C.; Hatfield, G.W. !$#journal J. Biol. Chem. (1986) 261:2441-2450 !$#title Nucleotide sequence and in vivo expression of the ilvY and !1ilvC genes in Escherichia coli K12: transcription from !1divergent overlapping promoters. !$#cross-references MUID:86111952; PMID:3003115 !$#accession B26287 !'##molecule_type DNA !'##residues 1-297 ##label WEK !'##cross-references GB:M11689; GB:M14492; NID:g146474; PIDN:AAA24028.1; !1PID:g146476 !'##experimental_source strain K12 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65180 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-297 ##label BLAT !'##cross-references GB:AE000453; GB:U00096; NID:g2367276; !1PIDN:AAC77493.1; PID:g1790208; UWGP:b3773 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S30660 !$#authors Daniels, D.L.; Plunkett III, G.; Burland, V.; Blattner, F.R. !$#journal Science (1992) 257:771-778 !$#title Analysis of the Escherichia coli genome: DNA sequence of the !1region from 84.5 to 86.5 minutes. !$#cross-references MUID:92358234; PMID:1379743 !$#accession S30671 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 'V',2-297 ##label DAN !'##cross-references EMBL:M87049 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1992 COMMENT This protein activates the transcription of the ilvC gene in !1the presence of acetolactate or acetohydroxybutyrate. GENETICS !$#gene ilvY !$#map_position 85 min !$#start_codon GTG CLASSIFICATION #superfamily regulatory protein ilvY KEYWORDS DNA binding; transcription regulation SUMMARY #length 297 #molecular-weight 33204 #checksum 6316 SEQUENCE /// ENTRY RGECOX #type complete TITLE hydrogen peroxide-inducible genes activator - Escherichia coli (strain K-12) ALTERNATE_NAMES regulatory protein momR ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS D65203; JV0025; JV0039; S05384; PH0206; A33145; JU0049 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65203 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-305 ##label BLAT !'##cross-references GB:AE000470; GB:U00096; NID:g2367332; !1PIDN:AAC76943.1; PID:g1790399; UWGP:b3961 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A94223 !$#authors Christman, M.F.; Storz, G.; Ames, B.N. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:3484-3488 !$#title OxyR, a positive regulator of hydrogen peroxide-inducible !1genes in Escherichia coli and Salmonella typhimurium, is !1homologous to a family of bacterial regulatory proteins. !$#cross-references MUID:89264448; PMID:2471187 !$#accession JV0025 !'##molecule_type DNA !'##residues 1-153,'R',155-305 ##label CHR !'##cross-references GB:J04553; NID:g147041; PIDN:AAA24257.1; !1PID:g147042 REFERENCE A93130 !$#authors Tao, K.; Makino, K.; Yonei, S.; Nakata, A.; Shinagawa, H. !$#journal Mol. Gen. Genet. (1989) 218:371-376 !$#title Molecular cloning and nucleotide sequencing of oxyR, the !1positive regulatory gene of a regulon for an adaptive !1response to oxidative stress in Escherichia coli: homologies !1between OxyR protein and a family of bacterial activator !1proteins. !$#cross-references MUID:90066338; PMID:2511419 !$#accession JV0039 !'##molecule_type DNA !'##residues 1-305 ##label TAO !'##cross-references GB:X16531; NID:g42211; PIDN:CAA34534.1; PID:g42212 !'##note the authors translated the codon GAA for residue 40 as Gln REFERENCE S05384 !$#authors Boelker, M.; Kahmann, R. !$#journal EMBO J. (1989) 8:2403-2410 !$#title The Escherichia coli regulatory protein OxyR discriminates !1between methylated and unmethylated states of the phage Mu !1mom promoter. !$#cross-references MUID:90005448; PMID:2551682 !$#accession S05384 !'##molecule_type DNA !'##residues 1-305 ##label BOE !'##cross-references GB:X52666; NID:g42213; PIDN:CAA36893.1; PID:g42214 REFERENCE PH0206 !$#authors Tao, K.; Makino, K.; Yonei, S.; Nakata, A.; Shinagawa, H. !$#journal J. Biochem. (1991) 109:262-266 !$#title Purification and characterization of the Escherichia coli !1OxyR protein, the positive regulator for a hydrogen !1peroxide-inducible regulon. !$#cross-references MUID:91324308; PMID:1864839 !$#accession PH0206 !'##molecule_type protein !'##residues 1-6,'Q',8-10 ##label TA2 REFERENCE A33145 !$#authors Warne, S.R.; Varley, J.M.; Boulnois, G.J.; Norton, M.G. !$#journal J. Gen. Microbiol. (1990) 136:455-462 !$#title Identification and characterization of a gene that controls !1colony morphology and auto-aggregation in Escherichia coli !1K12. !$#cross-references MUID:90362028; PMID:2167922 !$#accession A33145 !'##molecule_type DNA !'##residues 1-248,'A',250-305 ##label WAR !'##cross-references GB:M34102; NID:g146879; PIDN:AAA24176.1; !1PID:g146880 GENETICS !$#gene oxyR; momR !$#map_position 89.6 min FUNCTION !$#description a positive transcription regulator required for hydrogen !1peroxide-inducible genes in Escherichia coli and Salmonella !1typhimurium. CLASSIFICATION #superfamily regulatory protein ilvY KEYWORDS DNA binding; transcription regulation SUMMARY #length 305 #molecular-weight 34276 #checksum 3667 SEQUENCE /// ENTRY QQECRG #type complete TITLE tdcA protein - Escherichia coli (strain K-12) ALTERNATE_NAMES tdcABC operon transcription activator ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS S46415; C65101; A32552; A26229; Q00397 REFERENCE S46415 !$#authors Ganduri, Y.L.; Sadda, S.R.; Datta, M.W.; Jambukeswaran, !1R.K.; Datta, P. !$#journal Mol. Gen. Genet. (1993) 240:395-402 !$#title TdcA, a transcriptional activator of the tdcABC operon of !1Escherichia coli, is a member of the LysR family of !1proteins. !$#cross-references MUID:94019244; PMID:8413189 !$#accession S46415 !'##molecule_type DNA !'##residues 1-312 ##label GAN REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65101 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-312 ##label BLAT !'##cross-references GB:AE000393; GB:U00096; NID:g1789499; !1PIDN:AAC76153.1; PID:g1789506; UWGP:b3118 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A26229 !$#authors Goss, T.J.; Datta, P. !$#journal Mol. Gen. Genet. (1985) 201:308-314 !$#title Molecular cloning and expression of the biodegradative !1threonine dehydratase gene (tdc) of Escherichia coli K12. !$#cross-references MUID:86117917; PMID:3003533 !$#accession A32552 !'##molecule_type DNA !'##residues 1-2,'A',4-312 ##label GOS !'##cross-references GB:M21312; GB:M15037; GB:M21274; NID:g147921; !1PIDN:AAA24659.1; PID:g147922 !'##note the authors translated the codon GCT for residue 3 as Thr and !1CAA for residue 215 as Glu GENETICS !$#gene tdcA !$#map_position 67 min CLASSIFICATION #superfamily regulatory protein ilvY KEYWORDS DNA binding; transcription regulation SUMMARY #length 312 #molecular-weight 34539 #checksum 3834 SEQUENCE /// ENTRY RGECMD #type complete TITLE modulator protein - Escherichia coli transposon Tn21 ORGANISM #formal_name Escherichia coli DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 24-Sep-1999 ACCESSIONS A03567 REFERENCE A90871 !$#authors Hyde, D.R.; Tu, C.P.T. !$#journal Cell (1985) 42:629-638 !$#title tnpM: a novel regulatory gene that enhances Tn21 !1transposition and suppresses cointegrate resolution. !$#cross-references MUID:85282620; PMID:2992807 !$#accession A03567 !'##molecule_type DNA !'##residues 1-116 ##label HYD !'##cross-references GB:AF071413; NID:g3513654; PIDN:AAC33910.1; !1PID:g3513660 COMMENT This protein enhances the Tn21 transposition by activating !1expression of the transposase gene and decreases the !1resolution of the cointegrated DNA by supressing expression !1of the resolvase gene. GENETICS !$#gene tnpM CLASSIFICATION #superfamily transposon Tn21 modulator protein KEYWORDS transcription regulation SUMMARY #length 116 #molecular-weight 12550 #checksum 631 SEQUENCE /// ENTRY RGECFF #type complete TITLE type 1 fimbriae regulatory protein fimB - Escherichia coli (strain K-12) ALTERNATE_NAMES recombinase fimB (involved in phase variation) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS S56537; B65245; A25111; S53063; I41210 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56537 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-200 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97208.1; !1PID:g537153 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65245 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-200 ##label BLAT !'##cross-references GB:AE000502; GB:U00096; NID:g2367374; !1PIDN:AAC77268.1; PID:g1790767; UWGP:b4312 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A91041 !$#authors Klemm, P. !$#journal EMBO J. (1986) 5:1389-1393 !$#title Two regulatory fim genes, fimB and fimE, control the phase !1variation of type 1 fimbriae in Escherichia coli. !$#cross-references MUID:86274643; PMID:2874022 !$#accession A25111 !'##molecule_type DNA !'##residues 1-84,'D',86-200 ##label KLE !'##cross-references GB:X03923; NID:g41458; PIDN:CAA27560.1; PID:g41459 REFERENCE S53063 !$#authors Marc, D.; Dho-Moulin, M. !$#submission submitted to the EMBL Data Library, September 1994 !$#description Hypervariable sites within the major subunit of type 1 !1fimbriae, identified through analysis of the fim gene !1cluster of an avian pathogenic strain of Escherichia coli. !$#accession S53063 !'##status preliminary !'##molecule_type DNA !'##residues 1-85,'I',87-200 ##label MAR !'##cross-references EMBL:Z37500; NID:g732680; PIDN:CAA85725.1; !1PID:g732681 REFERENCE I41210 !$#authors Schwan, W.R.; Seifert, H.S.; Duncan, J.L. !$#journal Mol. Gen. Genet. (1994) 242:623-630 !$#title Analysis of the fimB promoter region involved in type 1 !1pilus phase variation in Escherichia coli. !$#cross-references MUID:94166775; PMID:8121417 !$#accession I41210 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-12,'V',14-31,'G',33-70 ##label RES !'##cross-references GB:L07756; NID:g145965; PIDN:AAA23779.1; !1PID:g551805 COMMENT This is one of the two proteins that mediate the periodic !1inversion of a 300-bp DNA segment containing the promoter !1for the fimA gene, thereby controlling the transcription of !1this type 1 fimbrial protein structural gene; it turns the !1invertible segment to the "on" configuration, where the !1promoter points toward the fimA gene and leads the bacterium !1to a fimbriated state. GENETICS !$#gene fimB CLASSIFICATION #superfamily type 1 fimbriae regulatory protein fimE KEYWORDS transcription regulation SUMMARY #length 200 #molecular-weight 22993 #checksum 9855 SEQUENCE /// ENTRY RGECFE #type complete TITLE type 1 fimbriae regulatory protein fimE - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 01-Mar-2002 ACCESSIONS B25111; S56538; C65245; S53064 REFERENCE A91041 !$#authors Klemm, P. !$#journal EMBO J. (1986) 5:1389-1393 !$#title Two regulatory fim genes, fimB and fimE, control the phase !1variation of type 1 fimbriae in Escherichia coli. !$#cross-references MUID:86274643; PMID:2874022 !$#accession B25111 !'##molecule_type DNA !'##residues 1-198 ##label KLE !'##cross-references GB:X03923; NID:g41458; PIDN:CAA27561.1; PID:g581086 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56538 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-198 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97209.1; !1PID:g537154 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65245 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-198 ##label BLAT !'##cross-references GB:AE000502; GB:U00096; NID:g2367374; !1PIDN:AAC77269.1; PID:g1790768; UWGP:b4313 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S53063 !$#authors Marc, D.; Dho-Moulin, M. !$#submission submitted to the EMBL Data Library, September 1994 !$#description Hypervariable sites within the major subunit of type 1 !1fimbriae, identified through analysis of the fim gene !1cluster of an avian pathogenic strain of Escherichia coli. !$#accession S53064 !'##status preliminary !'##molecule_type DNA !'##residues 15-197,'A' ##label MAR !'##cross-references EMBL:Z37500; NID:g732680; PIDN:CAA85726.1; !1PID:g732682 GENETICS !$#gene fimE !$#map_position 98 min !$#start_codon GTG FUNCTION !$#description one of the two proteins that mediate the periodic inversion !1of a 300-bp DNA segment containing the promoter for the fimA !1gene, thereby controlling the expression of this type 1 !1fimbrial protein structural gene; it turns the invertible !1segment to the "off" configuration, where the promoter !1points away from the fimA gene and leads the bacterium to a !1nonfimbriated state CLASSIFICATION #superfamily type 1 fimbriae regulatory protein fimE KEYWORDS transcription regulation SUMMARY #length 198 #molecular-weight 23116 #checksum 6863 SEQUENCE /// ENTRY RPECW #type complete TITLE trp operon repressor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Oct-1980 #sequence_revision 29-Jul-1981 #text_change 01-Mar-2002 ACCESSIONS A03568; B93698; B41332; S56617; H65254 REFERENCE A93867 !$#authors Gunsalus, R.P.; Yanofsky, C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1980) 77:7117-7121 !$#title Nucleotide sequence and expression of Escherichia coli trpR, !1the structural gene for the trp aporepressor. !$#cross-references MUID:81175101; PMID:7012834 !$#accession A03568 !'##molecule_type DNA !'##residues 1-108 ##label GUN !'##cross-references GB:J01715; NID:g148059; PIDN:AAA72140.1; !1PID:g148060 REFERENCE A93698 !$#authors Singleton, C.K.; Roeder, W.D.; Bogosian, G.; Somerville, !1R.L.; Weith, H.L. !$#journal Nucleic Acids Res. (1980) 8:1551-1560 !$#title DNA sequence of the Escherichia coli trpR gene and !1prediction of the amino acid sequence of Trp repressor. !$#cross-references MUID:81053831; PMID:7001368 !$#accession B93698 !'##molecule_type DNA !'##residues 1-72,'MNSAQASRRLRVDLTA' ##label SIN !'##cross-references GB:J01715 REFERENCE A41332 !$#authors Engel, H.; Kazemier, B.; Keck, W. !$#journal J. Bacteriol. (1991) 173:6773-6782 !$#title Murein-metabolizing enzymes from Escherichia coli: sequence !1analysis and controlled overexpression of the slt gene, !1which encodes the soluble lytic transglycosylase. !$#cross-references MUID:92041559; PMID:1938883 !$#accession B41332 !'##molecule_type DNA !'##residues 1-24 ##label ENG !'##cross-references GB:M69185 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56617 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-108 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97289.1; !1PID:g537233 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65254 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-108 ##label BLAT !'##cross-references GB:AE000509; GB:U00096; NID:g2367383; !1PIDN:AAC77346.1; PID:g1790854; UWGP:b4393 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene trpR !$#map_position 100 min FUNCTION !$#description an aporepressor; when complexed with L-tryptophan it binds !1the operator region of the trp operon and prevents the !1initiation of transcription; the complex also regulates trp !1repressor biosynthesis by binding to its regulatory region CLASSIFICATION #superfamily trp repressor KEYWORDS DNA binding; repressor; transcription regulation SUMMARY #length 108 #molecular-weight 12355 #checksum 7231 SEQUENCE /// ENTRY D64097 #type complete TITLE trp operon repressor - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 18-Aug-1995 #sequence_revision 18-Aug-1995 #text_change 16-Jul-1999 ACCESSIONS D64097 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession D64097 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-101 ##label TIGR !'##cross-references GB:U32765; GB:L42023; NID:g1573838; !1PIDN:AAC22488.1; PID:g1573844; TIGR:HI0830 FUNCTION !$#description an aporepressor; when complexed with L-tryptophan it binds !1the operator region of the trp operon and prevents the !1initiation of transcription; the complex also regulates trp !1repressor biosynthesis by binding to its regulatory region CLASSIFICATION #superfamily trp repressor KEYWORDS DNA binding; repressor; transcription regulation SUMMARY #length 101 #molecular-weight 11872 #checksum 9849 SEQUENCE /// ENTRY RPECIL #type complete TITLE ile repressor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS S56449; B65234; B24412 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56449 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-89 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97120.1; !1PID:g537065 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65234 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-89 ##label BLAT !'##cross-references GB:AE000493; GB:U00096; NID:g2367360; !1PIDN:AAC77180.1; PID:g1790669; UWGP:b4223 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A92595 !$#authors Weiss, D.L.; Johnson, D.I.; Weith, H.L.; Somerville, R.L. !$#journal J. Biol. Chem. (1986) 261:9966-9971 !$#title Structural analysis of the ileR locus of Escherichia coli !1K12. !$#cross-references MUID:86278038; PMID:3525538 !$#accession B24412 !'##molecule_type DNA !'##residues 1-10,'M',12-59,'H',61-89,'EMPSNWALVIQ' ##label WEI !'##cross-references GB:M14018 COMMENT This protein negatively controls the expression of the thr !1and ilv operons; unlike most repressor proteins, it !1functions independently of attenuation. GENETICS !$#gene ileR; yjfA !$#map_position 99.5 min CLASSIFICATION #superfamily ile repressor KEYWORDS repressor; transcription regulation SUMMARY #length 89 #molecular-weight 10585 #checksum 442 SEQUENCE /// ENTRY RPECDO #type complete TITLE deoxyribose operon repressor - Escherichia coli (strain K-12) ALTERNATE_NAMES deo operon repressor ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 01-Mar-2002 ACCESSIONS A24076; H64821 REFERENCE A24076 !$#authors Valentin-Hansen, P.; Hojrup, P.; Short, S. !$#journal Nucleic Acids Res. (1985) 13:5927-5936 !$#title The primary structure of the deoR repressor from Escherichia !1coli K-12. !$#cross-references MUID:85297787; PMID:2994018 !$#accession A24076 !'##molecule_type DNA !'##residues 1-252 ##label VAL !'##cross-references GB:X02837; NID:g41259; PIDN:CAA26598.1; PID:g41260 !'##experimental_source strain K-12 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64821 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-252 ##label BLAT !'##cross-references GB:AE000186; GB:U00096; NID:g1787058; !1PIDN:AAC73927.1; PID:g1787063; UWGP:b0840 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene deoR; nucR !$#map_position 19 min FUNCTION !$#description regulates expression of the deoCABD genes, which encode !1nucleotide and deoxyribonucleotide catabolizing enzymes; !1negatively regulates expression of nupG and tsx !$#note induction by deoxyribose-5-phosphate CLASSIFICATION #superfamily deo operon repressor KEYWORDS DNA binding; homooctamer; nucleotide catabolism; !1transcription regulation FEATURE !$8-42 #region helix-turn-helix motif SUMMARY #length 252 #molecular-weight 28548 #checksum 1063 SEQUENCE /// ENTRY RGECFO #type complete TITLE fuc operon regulatory protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 01-Mar-2002 ACCESSIONS JS0188; A65063 REFERENCE S04702 !$#authors Lu, Z.; Lin, E.C.C. !$#journal Nucleic Acids Res. (1989) 17:4883-4884 !$#title The nucleotide sequence of Escherichia coli genes for !1L-fucose dissimilation. !$#cross-references MUID:89315234; PMID:2664711 !$#accession JS0188 !'##molecule_type DNA !'##residues 1-243 ##label LUZ !'##cross-references GB:X15025; NID:g41501; PIDN:CAA33130.1; PID:g41508 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65063 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-243 ##label BLAT !'##cross-references GB:AE000364; GB:U00096; NID:g2367162; !1PIDN:AAC75847.1; PID:g1789170; UWGP:b2805 !'##experimental_source strain K-12, substrain MG1655 COMMENT This protein is an activator for the fuc operon, which codes !1for proteins involved in an induced catabolic pathway for !1L-fucose. GENETICS !$#gene fucR !$#map_position 60 min CLASSIFICATION #superfamily fuc operon regulatory protein KEYWORDS DNA binding; L-fucose catabolism; L-fucose utilization; !1transcription regulation SUMMARY #length 243 #molecular-weight 27362 #checksum 451 SEQUENCE /// ENTRY RPECGP #type complete TITLE glycerol-3-phosphate regulon repressor - Escherichia coli ORGANISM #formal_name Escherichia coli DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 16-Jul-1999 ACCESSIONS A30282 REFERENCE A93685 !$#authors Choi, Y.L.; Kawase, S.; Nishida, T.; Sakai, H.; Komano, T.; !1Kawamukai, M.; Utsumi, R.; Kohara, Y.; Akiyama, K. !$#journal Nucleic Acids Res. (1988) 16:7732 !$#title Nucleotide sequence of the glpR gene encoding the repressor !1for the glycerol-3-phosphate regulon of Escherichia coli !1K12. !$#cross-references MUID:88319970; PMID:3045764 !$#accession A30282 !'##molecule_type DNA !'##residues 1-299 ##label CHO !'##cross-references EMBL:X07520; NID:g41582; PIDN:CAA30399.1; !1PID:g41585 !'##experimental_source strain K12 GENETICS !$#gene glpR !$#map_position 75 min CLASSIFICATION #superfamily glycerol-3-phosphate regulon repressor KEYWORDS DNA binding; repressor; transcription regulation SUMMARY #length 299 #molecular-weight 32402 #checksum 4746 SEQUENCE /// ENTRY XMECGF #type complete TITLE glycerol facilitator protein - Escherichia coli (strain K-12) ALTERNATE_NAMES glpF protein; glycerol diffusion facilitator ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 24-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS A42157; S40870; B65199; JU0022 REFERENCE A42157 !$#authors Weissenborn, D.L.; Wittekindt, N.; Larson, T.J. !$#journal J. Biol. Chem. (1992) 267:6122-6131 !$#title Structure and regulation of the glpFK operon encoding !1glycerol diffusion facilitator and glycerol kinase of !1Escherichia coli K-12. !$#cross-references MUID:92210584; PMID:1372899 !$#accession A42157 !'##status preliminary !'##molecule_type DNA !'##residues 1-281 ##label WEI !'##cross-references GB:M55990; NID:g146187; PIDN:AAA23886.1; !1PID:g146188 REFERENCE S40802 !$#authors Plunkett III, G.; Burland, V.; Daniels, D.L.; Blattner, F.R. !$#journal Nucleic Acids Res. (1993) 21:3391-3398 !$#title Analysis of the Escherichia coli genome. III. DNA sequence !1of the region from 87.2 to 89.2 minutes. !$#cross-references MUID:93347969; PMID:8346018 !$#accession S40870 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-281 ##label PLU !'##cross-references EMBL:L19201; NID:g304961; PIDN:AAB03059.1; !1PID:g305030 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1993 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65199 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-281 ##label BLAT !'##cross-references GB:AE000467; GB:U00096; NID:g1790356; !1PIDN:AAC76909.1; PID:g1790362; UWGP:b3927 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S04594 !$#authors Muramatsu, S.; Mizuno, T. !$#journal Nucleic Acids Res. (1989) 17:4378 !$#title Nucleotide sequence of the region encompassing the glpKF !1operon and its upstream region containing a bent DNA !1sequence of Escherichia coli. !$#cross-references MUID:89296490; PMID:2544860 !$#accession JU0022 !'##molecule_type DNA !'##residues 1-167,'V',169-281 ##label MUR !'##cross-references GB:X15054; NID:g41577; PIDN:CAA33153.1; PID:g41578 COMMENT This membrane protein facilitates the movement of glycerol !1across the cytoplasmic membrane. GENETICS !$#gene glpF !$#map_position 88 min CLASSIFICATION #superfamily glycerol facilitator protein KEYWORDS transmembrane protein SUMMARY #length 281 #molecular-weight 29780 #checksum 5286 SEQUENCE /// ENTRY QRECLH #type complete TITLE leucine transport protein livH - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS S47676; D65142; A24548; D37074 REFERENCE S47666 !$#authors Plunkett, G. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S47676 !'##molecule_type DNA !'##residues 1-308 ##label PLU !'##cross-references EMBL:U00039; NID:g466582; PIDN:AAB18432.1; !1PID:g466593 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65142 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-308 ##label BLAT !'##cross-references GB:AE000421; GB:U00096; NID:g1789854; !1PIDN:AAC76482.1; PID:g1789866; UWGP:b3457 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A24548 !$#authors Nazos, P.M.; Antonucci, T.K.; Landick, R.; Oxender, D.L. !$#journal J. Bacteriol. (1986) 166:565-573 !$#title Cloning and characterization of livH, the structural gene !1encoding a component of the leucine transport system in !1Escherichia coli. !$#cross-references MUID:86195847; PMID:3009409 !$#accession A24548 !'##molecule_type DNA !'##residues 1-252,'G',254-287,'P',289-308 ##label NAZ !'##cross-references GB:J05516; GB:K02178; GB:M10426; GB:M10427; !1GB:M13166; NID:g146630; PIDN:AAA83884.1; PID:g146633 REFERENCE A37074 !$#authors Adams, M.D.; Wagner, L.M.; Graddis, T.J.; Landick, R.; !1Antonucci, T.K.; Gibson, A.L.; Oxender, D.L. !$#journal J. Biol. Chem. (1990) 265:11436-11443 !$#title Nucleotide sequence and genetic characterization reveal six !1essential genes for the LIV-I and LS transport systems of !1Escherichia coli. !$#cross-references MUID:90307651; PMID:2195019 !$#accession D37074 !'##molecule_type DNA !'##residues 1-252,'G',254-287,'P',289-308 ##label ADA !'##cross-references GB:J05516; NID:g146630; PIDN:AAA83884.1; !1PID:g146633 COMMENT This protein is a component of the leucine-specific !1transport system, which is one of the two periplasmic !1binding protein-dependent transport systems of the !1high-affinity transport of the branched-chain amino acids in !1E. coli. GENETICS !$#gene livH !$#map_position 76 min CLASSIFICATION #superfamily leucine transport protein livH KEYWORDS branched-chain amino acid transport; leucine transport; !1transmembrane protein SUMMARY #length 308 #molecular-weight 32982 #checksum 9874 SEQUENCE /// ENTRY H69592 #type complete TITLE branched-chain amino acid transport protein azlD - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H69592; T44778 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69592 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-110 ##label KUN !'##cross-references GB:Z99117; GB:AL009126; NID:g2634966; !1PIDN:CAB14611.1; PID:g2635115 !'##experimental_source strain 168 REFERENCE Z22837 !$#authors Belitsky, B.R.; Gustafsson, M.C.U.; Sonenshein, A.L.; von !1Wachenfeldt, C. !$#journal J. Bacteriol. (1997) 179:5448-5457 !$#title An lrp-like gene of Bacillus subtilis involved in !1branched-chain amino acid transport. !$#cross-references MUID:97431495; PMID:9287000 !$#accession T44778 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-110 ##label BEL !'##cross-references EMBL:Y11043; NID:g1926275; PIDN:CAA71941.1; !1PID:g1926282 !'##experimental_source strain 1A1 GENETICS !$#gene azlD CLASSIFICATION #superfamily branched-chain amino acid transport protein !1azlD KEYWORDS branched-chain amino acid transport; transmembrane protein SUMMARY #length 110 #molecular-weight 11970 #checksum 340 SEQUENCE /// ENTRY E64041 #type complete TITLE branched-chain amino acid transport protein azlD homolog HI1737 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS E64041 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession E64041 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-109 ##label TIGR !'##cross-references GB:U32846; GB:L42023; NID:g3212237; !1PIDN:AAC23381.1; PID:g1574595; TIGR:HI1737 CLASSIFICATION #superfamily branched-chain amino acid transport protein !1azlD KEYWORDS branched-chain amino acid transport; transmembrane protein SUMMARY #length 109 #molecular-weight 12423 #checksum 3343 SEQUENCE /// ENTRY B64686 #type complete TITLE branched-chain amino acid transport protein azlD homolog HP1330 - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B64686 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession B64686 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-115 ##label TOM !'##cross-references GB:AE000634; GB:AE000511; NID:g2314489; !1PIDN:AAD08371.1; PID:g2314495; TIGR:HP1330 CLASSIFICATION #superfamily branched-chain amino acid transport protein !1azlD KEYWORDS branched-chain amino acid transport; transmembrane protein SUMMARY #length 115 #molecular-weight 13303 #checksum 3860 SEQUENCE /// ENTRY VXECS #type complete TITLE protein-export protein secB - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 01-Mar-2002 ACCESSIONS JS0126; S47830; C65161 REFERENCE A91601 !$#authors Kumamoto, C.A.; Nault, A.K. !$#journal Gene (1989) 75:167-175 !$#title Characterization of the Escherichia coli protein-export gene !1secB. !$#cross-references MUID:89252913; PMID:2656409 !$#accession JS0126 !'##molecule_type DNA !'##residues 1-155 ##label KUM !'##cross-references GB:M24489; GB:M24490; NID:g147796; PIDN:AAA83907.1; !1PID:g147797 !'##experimental_source strain K12 REFERENCE S47666 !$#authors Plunkett, G. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S47830 !'##molecule_type DNA !'##residues 1-155 ##label PLU !'##cross-references EMBL:U00039; NID:g466582; PIDN:AAB18586.1; !1PID:g466747 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65161 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-155 ##label BLAT !'##cross-references GB:AE000439; GB:U00096; NID:g1790036; !1PIDN:AAC76633.1; PID:g1790038; UWGP:b3609 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene secB FUNCTION !$#description one of the proteins required for the normal export of !1envelope proteins out of the cell cytoplasm; may be involved !1in the initiation of the exporting process CLASSIFICATION #superfamily protein-export protein secB KEYWORDS protein export SUMMARY #length 155 #molecular-weight 17277 #checksum 2479 SEQUENCE /// ENTRY JC1292 #type complete TITLE protein-export protein secB - Buchnera aphidicola ORGANISM #formal_name Buchnera aphidicola DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS JC1292 REFERENCE JC1291 !$#authors Lai, C.Y.; Baumann, P. !$#journal Gene (1992) 119:113-118 !$#title Sequence analysis of a DNA fragment from Buchnera aphidicola !1(an endosymbiont of aphids) containing genes homologous to !1dnaG, rpoD, cysE, and secB. !$#cross-references MUID:93012960; PMID:1398077 !$#accession JC1292 !'##molecule_type DNA !'##residues 1-154 ##label LAI !'##cross-references GB:M90644; NID:g144135; PIDN:AAA73231.1; !1PID:g144136 GENETICS !$#gene secB CLASSIFICATION #superfamily protein-export protein secB KEYWORDS protein export SUMMARY #length 154 #molecular-weight 18037 #checksum 2433 SEQUENCE /// ENTRY VXECSE #type complete TITLE preprotein translocase secE chain - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 01-Mar-2002 ACCESSIONS A35139; A32873; H65204 REFERENCE A35139 !$#authors Downing, W.L.; Sullivan, S.L.; Gottesman, M.E.; Dennis, P.P. !$#journal J. Bacteriol. (1990) 172:1621-1627 !$#title Sequence and transcriptional pattern of the essential !1Escherichia coli secE-nusG operon. !$#cross-references MUID:90170882; PMID:2137819 !$#accession A35139 !'##molecule_type DNA !'##residues 1-127 ##label DOW !'##cross-references GB:M30610; NID:g147798; PIDN:AAA24621.1; !1PID:g147800 REFERENCE A32873 !$#authors Schatz, P.J.; Riggs, P.D.; Jacq, A.; Fath, M.J.; Beckwith, !1J. !$#journal Genes Dev. (1989) 3:1035-1044 !$#title The secE gene encodes an integral membrane protein required !1for protein export in Escherichia coli. !$#cross-references MUID:89378734; PMID:2673920 !$#accession A32873 !'##molecule_type DNA !'##residues 1-127 ##label SCH REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65204 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-127 ##label BLAT !'##cross-references GB:AE000472; GB:U00096; NID:g2367333; !1PIDN:AAC76955.1; PID:g1790413; UWGP:b3981 !'##experimental_source strain K-12, substrain MG1655 COMMENT This integral inner membrane protein is an essential !1component of the protein-exporting apparatus. GENETICS !$#gene secE !$#map_position 90 min CLASSIFICATION #superfamily protein-export protein secE KEYWORDS inner membrane; protein export SUMMARY #length 127 #molecular-weight 13643 #checksum 8642 SEQUENCE /// ENTRY BVBY23 #type complete TITLE protein transport protein SEC23 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein P9705.14; protein YPR181c ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 03-Dec-1999 ACCESSIONS S05742; S59838 REFERENCE S05742 !$#authors Hicke, L.; Schekman, R. !$#journal EMBO J. (1989) 8:1677-1684 !$#title Yeast Sec23p acts in the cytoplasm to promote protein !1transport from the endoplasmic reticulum to the Golgi !1complex in vivo and in vitro. !$#cross-references MUID:89356640; PMID:2670558 !$#accession S05742 !'##molecule_type DNA !'##residues 1-768 ##label HIC !'##cross-references EMBL:X15474; NID:g4442; PIDN:CAA33501.1; PID:g4443 REFERENCE S59829 !$#authors Pauley, A. !$#submission submitted to the EMBL Data Library, April 1995 !$#description The sequence of S. cerevisiae cosmid 9705. !$#accession S59838 !'##molecule_type DNA !'##residues 1-768 ##label PAU !'##cross-references EMBL:U25842; NID:g786312; PIDN:AAB68114.1; !1PID:g786326; GSPDB:GN00016; MIPS:YPR181c GENETICS !$#gene SGD:SEC23; MIPS:YPR181c !'##cross-references SGD:S0006385; MIPS:YPR181c !$#map_position 16R CLASSIFICATION #superfamily SEC23 protein KEYWORDS transmembrane protein FEATURE !$144-160 #domain transmembrane #status predicted #label TM1\ !$284-300 #domain transmembrane #status predicted #label TM2\ !$648-664 #domain transmembrane #status predicted #label TM3 SUMMARY #length 768 #molecular-weight 85384 #checksum 5480 SEQUENCE /// ENTRY BVBYP1 #type complete TITLE CBP1 protein - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein HRA654; protein J0242; protein YJL209w ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 12-Nov-1999 ACCESSIONS S05829; S50776; S56999; S56996; S45164 REFERENCE S05829 !$#authors Dieckmann, C.L.; Homison, G.; Tzagoloff, A. !$#journal J. Biol. Chem. (1984) 259:4732-4738 !$#title Assembly of the mitochondrial membrane system. Nucleotide !1sequence of a yeast nuclear gene (CBP1) involved in 5' end !1processing of cytochrome b pre-mRNA. !$#cross-references MUID:84185566; PMID:6325407 !$#accession S05829 !'##molecule_type DNA !'##residues 1-654 ##label DIE !'##cross-references EMBL:K02647; NID:g171166; PIDN:AAA34474.1; !1PID:g171167 REFERENCE S50701 !$#authors Vandenbol, M.; Durand, P.; Bolle, P.A.; Dion, C.; !1Portetelle, D.; Hilger, F. !$#journal Yeast (1994) 10:1657-1662 !$#title Sequence analysis of a 40.2 kb DNA fragment located near the !1left telomere of yeast chromosome X. !$#cross-references MUID:95242842; PMID:7725802 !$#accession S50776 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-654 ##label VAW !'##cross-references EMBL:Z34098; NID:g496934; PIDN:CAA84002.1; !1PID:g496953 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1994 REFERENCE S56835 !$#authors Vandenbol, M.; Durand, P.; Portetelle, D.; Hilger, F. !$#submission submitted to the Protein Sequence Database, September 1995 !$#accession S56999 !'##molecule_type DNA !'##residues 1-654 ##label VAN !'##cross-references EMBL:Z49484; NID:g1015590; PIDN:CAA89506.1; !1PID:g1015591; GSPDB:GN00010; MIPS:YJL209w REFERENCE S56977 !$#authors Purnelle, B.; Coster, F.; Goffeau, A. !$#submission submitted to the Protein Sequence Database, September 1995 !$#accession S56996 !'##molecule_type DNA !'##residues 637-654 ##label PUR !'##cross-references EMBL:Z49484; GSPDB:GN00010; MIPS:YJL209w GENETICS !$#gene SGD:CBP1; MIPS:YJL209w !'##cross-references SGD:S0003745; MIPS:YJL209w !$#map_position 10L !$#genome nuclear FUNCTION !$#description pre-mRNA processing !$#note required for correct 5' terminal processing of cytochrome b !1pre-mRNA CLASSIFICATION #superfamily CBP1 protein KEYWORDS mitochondrion SUMMARY #length 654 #molecular-weight 76171 #checksum 1357 SEQUENCE /// ENTRY BVBY53 #type complete TITLE phosphomannomutase (EC 5.4.2.8) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YFL045c ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Jun-2000 ACCESSIONS S05874; S56210 REFERENCE S05874 !$#authors Bernstein, M.; Hoffmann, W.; Ammerer, G.; Schekman, R. !$#journal J. Cell Biol. (1985) 101:2374-2382 !$#title Characterization of a gene product (sec53p) required for !1protein assembly in the yeast endoplasmic reticulum. !$#cross-references MUID:86059690; PMID:3905826 !$#accession S05874 !'##molecule_type DNA !'##residues 1-254 ##label BER !'##cross-references EMBL:X03213; NID:g4444; PIDN:CAA26957.1; PID:g4445 REFERENCE S56186 !$#authors Murakami, Y.; Naitou, M.; Hagiwara, H.; Shibata, T.; Ozawa, !1M.; Sasanuma, S.I.; Sasanuma, M.; Tsuchiya, Y.; Soeda, E.; !1Yokoyama, K.; Yamazaki, M.; Tashiro, H.; Eki, T. !$#submission submitted to the EMBL Data Library, May 1995 !$#description Analysis of the nucleotide sequence of chromosome VI from !1Saccaromyces cerevisiae. !$#accession S56210 !'##molecule_type DNA !'##residues 1-254 ##label MUR !'##cross-references EMBL:D50617; NID:g836685; PIDN:BAA09196.1; !1PID:g836710; GSPDB:GN00006; MIPS:YFL045c GENETICS !$#gene SGD:SEC53; MIPS:YFL045c !'##cross-references SGD:S0001849; MIPS:YFL045c !$#map_position 6L CLASSIFICATION #superfamily SEC53 protein KEYWORDS intramolecular transferase; isomerase SUMMARY #length 254 #molecular-weight 29063 #checksum 5536 SEQUENCE /// ENTRY BVBYDP #type complete TITLE probable protein prenyltransferase (EC 2.5.1.-) RAM1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES DPR1 protein; protein D2412; protein YDL090c ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1991 #sequence_revision 23-Aug-1996 #text_change 16-Jun-2000 ACCESSIONS S67626; S67632; S07864; S67427 REFERENCE S67608 !$#authors Wambutt, R.; Wedler, H.; Wedler, E.; Scharfe, M. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67626 !'##molecule_type DNA !'##residues 1-431 ##label WAM !'##cross-references EMBL:Z74138; NID:g1431119; PIDN:CAA98656.1; !1PID:g1431120; GSPDB:GN00004; MIPS:YDL090c !'##experimental_source strain S288C REFERENCE S67629 !$#authors Ballesta, J.P.G.; Remacha, M.; Soler-Mira, A.; Jimenez, A.; !1Garcia-Cantalejo, J.M.; Boskovic, J.; del Rey, F.; Revuelta, !1J.L.; Buitrago, M.J.; Sanz, J.E. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67632 !'##molecule_type DNA !'##residues 1-431 ##label BAL !'##cross-references EMBL:Z74138; NID:g1431119; PIDN:CAA98656.1; !1PID:g1431120; GSPDB:GN00004; MIPS:YDL090c !'##experimental_source strain S288C REFERENCE S07864 !$#authors Goodman, L.E.; Perou, C.M.; Fujiyama, A.; Tamanoi, F. !$#journal Yeast (1988) 4:271-281 !$#title Structure and expression of yeast DPR1, a gene essential for !1the processing and intracellular localization of ras !1proteins. !$#cross-references MUID:89115553; PMID:3064491 !$#accession S07864 !'##molecule_type DNA !'##residues 1-134,'V',136-431 ##label GOO !'##cross-references EMBL:M22753 REFERENCE S67406 !$#authors Boskovic, J.; Saiz, J.E.; Soler-Mira, A.; Garcia-Cantalejo, !1J.; Revuelta, J.L.; Jiminez, A.; Ballesta, J.P.G.; del Rey, !1F.; Remacha, M. !$#submission submitted to the EMBL Data Library, February 1996 !$#accession S67427 !'##molecule_type DNA !'##residues 1-431 ##label BOS !'##cross-references EMBL:X95644; NID:g1199535; PIDN:CAA64921.1; !1PID:g1199557 GENETICS !$#gene SGD:RAM1; DPR1; STE16; MIPS:YDL090c !'##cross-references SGD:S0002248; MIPS:YDL090c !$#map_position 4L CLASSIFICATION #superfamily DPR1 protein KEYWORDS transferase SUMMARY #length 431 #molecular-weight 48189 #checksum 6691 SEQUENCE /// ENTRY UPECX #type complete TITLE D-Xylose uptake protein - Escherichia coli ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jul-1999 ACCESSIONS A24334 REFERENCE A24334 !$#authors Kurose, N.; Watanabe, K.; Kimura, A. !$#journal Nucleic Acids Res. (1986) 14:7115-7123 !$#title Nucleotide sequence of the gene responsible for D-xylose !1uptake in Escherichia coli. !$#cross-references MUID:87016348; PMID:3532033 !$#accession A24334 !'##molecule_type DNA !'##residues 1-61 ##label KUR !'##cross-references GB:X04387; NID:g43317; PIDN:CAA27976.1; PID:g43318 COMMENT This protein enables E. coli mutants to recover from a !1decrease in D-xylose uptake at low temperatures. GENETICS !$#map_position 80 min CLASSIFICATION #superfamily D-xylose uptake protein KEYWORDS xylose transport SUMMARY #length 61 #molecular-weight 6305 #checksum 8577 SEQUENCE /// ENTRY RPBPL #type complete TITLE repressor protein cI - phage lambda ORGANISM #formal_name phage lambda DATE 30-Nov-1979 #sequence_revision 13-Jun-1983 #text_change 16-Jul-1999 ACCESSIONS A14086; A94164; A19098; A13662; A03570; A33301 REFERENCE A93201 !$#authors Sauer, R.T. !$#journal Nature (1978) 276:301-302 !$#title DNA sequence of the bacteriophage lambda cI gene. !$#cross-references MUID:79053284; PMID:714163 !$#accession A14086 !'##molecule_type DNA !'##residues 1-237 ##label SAU1 !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96581.1; PID:g215147 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession A94164 !'##molecule_type DNA !'##residues 1-237 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession A19098 !'##molecule_type DNA !'##residues 1-66,'T',68-117,'K',119-237 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; GB:L05669; NID:g208643 !'##note accessions GB:L05669, NID:g208643 apply to a synthetic cloning !1vector REFERENCE A90408 !$#authors Sauer, R.T.; Anderegg, R. !$#journal Biochemistry (1978) 17:1092-1100 !$#title Primary structure of the lambda repressor. !$#cross-references MUID:78124173; PMID:629949 !$#accession A13662 !'##molecule_type protein !'##residues 2-237 ##label SAU2 REFERENCE A33301 !$#authors Bushman, F.D.; Shang, C.; Ptashne, M. !$#journal Cell (1989) 58:1163-1171 !$#title A single glutamic acid residue plays a key role in the !1transcriptional activation function of lambda repressor. !$#cross-references MUID:89376567; PMID:2570642 !$#contents annotation !$#note the authors studied functional properties of the repressor !1by site-directed mutagenesis COMMENT Repressor protein cI allows phage lambda to reside !1inactively in the chromosome of its host bacterium. This !1lysogenic state is maintained by binding of regulatory !1protein cI to the OR and OL operators, preventing !1transcription of proteins necessary for lytic development. COMMENT The active, homodimeric form binds more strongly to the !1lambda operator sites than does the monomer. COMMENT Bacterial cells harboring a lysogenic lambda phage are !1immune to further infection by lambda. The cI repressor !1protein inhibits the lytic development of any additional !1infecting phage particles. The region of the genome that !1codes for the cI repressor protein is known as the immunity !1region. GENETICS !$#gene cI !$#map_position 78.22-76.76 CLASSIFICATION #superfamily repressor protein cI KEYWORDS DNA binding; homodimer; monomer; repressor; transcription !1regulation FEATURE !$2-237 #product repressor protein cI #status experimental !8#label MAT\ !$34-53 #region helix-turn-helix motif SUMMARY #length 237 #molecular-weight 26212 #checksum 8029 SEQUENCE /// ENTRY RPBP22 #type complete TITLE repressor protein c2 - phage P22 ORGANISM #formal_name phage P22 #note host Salmonella sp. DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 28-May-1999 ACCESSIONS A03571; B03571 REFERENCE A90448 !$#authors Sauer, R.T.; Pan, J.; Hopper, P.; Hehir, K.; Brown, J.; !1Poteete, A.R. !$#journal Biochemistry (1981) 20:3591-3598 !$#title Primary structure of the phage P22 repressor and its gene !1c2. !$#cross-references MUID:81256447; PMID:7260059 !$#accession A03571 !'##molecule_type DNA !'##residues 1-216 ##label SAU !'##cross-references GB:V01153; GB:J02470; NID:g15654; PIDN:CAA24470.1; !1PID:g15655 !'##note in the mature form of the repressor protein the initiator !1formylmethionine is not formylated REFERENCE A92858 !$#authors Poteete, A.R.; Ptashne, M.; Ballivet, M.; Eisen, H. !$#journal J. Mol. Biol. (1980) 137:81-91 !$#title Operator sequences of bacteriophage P22 and 21. !$#cross-references MUID:80162854; PMID:6445008 !$#accession B03571 !'##molecule_type DNA !'##residues 1-5 ##label POT COMMENT The active, homodimeric form binds more strongly to the !1lambda operator sites than does the monomer. See PIR:RPBPL. GENETICS !$#gene c2 CLASSIFICATION #superfamily repressor protein cI KEYWORDS DNA binding; homodimer; monomer; repressor; transcription !1regulation FEATURE !$21-40 #region helix-turn-helix motif\ !$1 #modified_site N-formylmethionine #status absent SUMMARY #length 216 #molecular-weight 24068 #checksum 4729 SEQUENCE /// ENTRY RCBP4 #type complete TITLE regulatory protein cro - phage 434 ORGANISM #formal_name phage 434 DATE 15-Nov-1984 #sequence_revision 15-Nov-1984 #text_change 16-Jul-1999 ACCESSIONS A03572 REFERENCE A03572 !$#authors Grosschedl, R.; Schwarz, E. !$#journal Nucleic Acids Res. (1979) 6:867-881 !$#title Nucleotide sequence of the cro-cII-oop region of !1bacteriophage 434 DNA. !$#cross-references MUID:79179801; PMID:375198 !$#accession A03572 !'##molecule_type DNA !'##residues 1-71 ##label GRO !'##cross-references GB:V00635; GB:J02475; NID:g14988; PIDN:CAA23908.1; !1PID:g14989 COMMENT This protein functions analogously to the cro repressor of !1bacteriophage lambda. GENETICS !$#gene cro CLASSIFICATION #superfamily repressor protein cI KEYWORDS DNA binding; early protein; homodimer; monomer; !1transcription regulation FEATURE !$19-38 #region helix-turn-helix motif SUMMARY #length 71 #molecular-weight 8063 #checksum 1488 SEQUENCE /// ENTRY RGECPB #type complete TITLE transcription activator papB - Escherichia coli ALTERNATE_NAMES prfB protein ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jul-1999 ACCESSIONS B25121; S03798; S20049; S25215; A37325; S12275; S41550; !1S16394 REFERENCE A91031 !$#authors Baga, M.; Goransson, M.; Normark, S.; Uhlin, B.E. !$#journal EMBO J. (1985) 4:3887-3893 !$#title Transcriptional activation of a Pap pilus virulence operon !1from uropathogenic Escherichia coli. !$#cross-references MUID:86136032; PMID:2868893 !$#accession B25121 !'##molecule_type DNA !'##residues 1-104 ##label BAG !'##cross-references GB:X03391; GB:K01176; GB:X03392; NID:g42309; !1PIDN:CAA27125.1; PID:g42311 !'##experimental_source strain J96 REFERENCE S03797 !$#authors Blyn, L.B.; Braaten, B.A.; White-Ziegler, C.A.; Rolfson, !1D.H.; Low, D.A. !$#journal EMBO J. (1989) 8:613-620 !$#title Phase-variation of pyelonephritis-associated pili in !1Escherichia coli: evidence for transcriptional regulation. !$#cross-references MUID:89251590; PMID:2656260 !$#accession S03798 !'##molecule_type DNA !'##residues 1-104 ##label BLY1 !'##cross-references EMBL:X14471; NID:g42273; PIDN:CAA32631.1; !1PID:g42275 !'##experimental_source strain C1212 !'##genetics P17 !$#accession S20049 !'##molecule_type DNA !'##residues 1-104 ##label BLY2 !'##cross-references EMBL:X14472 !'##experimental_source strain C1212 !'##genetics P21 REFERENCE S25205 !$#authors Marklund, B.I.; Tennent, J.M.; Garcia, E.; Hamers, A.; Baga, !1M.; Lindberg, F.; Gaastra, W.; Normark, S. !$#journal Mol. Microbiol. (1992) 6:2225-2242 !$#title Horizontal gene transfer of the Escherichia coli pap and prs !1pili operons as a mechanism for the development of !1tissue-specific adhesive properties. !$#cross-references MUID:93023852; PMID:1357526 !$#accession S25215 !'##status preliminary !'##molecule_type DNA !'##residues 1-104 ##label MAR !'##cross-references EMBL:X61239; NID:g42290; PIDN:CAA43561.1; !1PID:g42292 !'##experimental_source strain J96 REFERENCE A37325 !$#authors Braaten, B.A.; Blyn, L.B.; Skinner, B.S.; Low, D.A. !$#journal J. Bacteriol. (1991) 173:1789-1800 !$#title Evidence for a methylation-blocking factor (mbf) locus !1involved in pap pilus expression and phase variation in !1Escherichia coli. !$#cross-references MUID:91154136; PMID:1671857 !$#accession A37325 !'##status preliminary !'##molecule_type DNA !'##residues 1-23 ##label BRA !'##cross-references GB:M63747; NID:g147086; PIDN:AAA24287.1; !1PID:g147088 REFERENCE S12275 !$#authors Blyn, L.B.; Braaten, B.A.; Low, D.A. !$#journal EMBO J. (1990) 9:4045-4054 !$#title Regulation of pap pilin phase variation by a mechanism !1involving differential Dam methylation states. !$#cross-references MUID:91065335; PMID:2147413 !$#accession S12275 !'##molecule_type DNA !'##residues 1-23 ##label BLY !'##cross-references GB:X55249; NID:g42288; PIDN:CAA38989.1; PID:g42289 REFERENCE S41549 !$#authors Morschhaeuser, J.; Vetter, V.; Emoedy, L.; Hacker, J. !$#journal Mol. Microbiol. (1994) 11:555-566 !$#title Adhesin regulatory genes within large, unstable DNA regions !1of pathogenic Escherichia coli: cross-talk between different !1adhesin gene clusters. !$#cross-references MUID:94203058; PMID:7908714 !$#accession S41550 !'##status preliminary !'##molecule_type DNA !'##residues 1-5,'I',7-9,'A',11-59,'T',61-67,'H',69-104 ##label MOR !'##cross-references EMBL:X76613; NID:g435270; PIDN:CAA54079.1; !1PID:g435272 GENETICS P17 !$#gene pap(17)B GENETICS P21 !$#gene pap(21)B !$#note E. coli strain C1212 contains two complete pap gene !1clusters, each encoding antigenetically distinct pilin !1monomers designated as pilin-17 and pilin-21 CLASSIFICATION #superfamily pap fimbrial activator protein papB KEYWORDS transcription regulation SUMMARY #length 104 #molecular-weight 11695 #checksum 1559 SEQUENCE /// ENTRY BVECFA #type complete TITLE fanA protein - Escherichia coli ALTERNATE_NAMES K99 pilin ORGANISM #formal_name Escherichia coli DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS A29112 REFERENCE A93671 !$#authors Roosendaal, E.; Boots, M.; de Graaf, F.K. !$#journal Nucleic Acids Res. (1987) 15:5973-5984 !$#title Two novel genes, fanA and fanB, involved in the biogenesis !1of K99 fimbriae. !$#cross-references MUID:87316863; PMID:2888075 !$#accession A29112 !'##molecule_type DNA !'##residues 1-93 ##label ROO !'##cross-references GB:X05797; NID:g41404; PIDN:CAA29238.1; PID:g41405 COMMENT This is one of two homologous proteins encoded by genes !1upstream of the fanC gene, which codes for K99 fimbrial !1protein. These two trans-acting polypeptides, fanA and fanB, !1are involved in regulating the expression of fanC. GENETICS !$#gene fanA CLASSIFICATION #superfamily pap fimbrial activator protein papB KEYWORDS transcription regulation SUMMARY #length 93 #molecular-weight 11052 #checksum 8981 SEQUENCE /// ENTRY BVECFB #type complete TITLE fanB protein - Escherichia coli ALTERNATE_NAMES K99 pilin ORGANISM #formal_name Escherichia coli DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS B29112 REFERENCE A93671 !$#authors Roosendaal, E.; Boots, M.; de Graaf, F.K. !$#journal Nucleic Acids Res. (1987) 15:5973-5984 !$#title Two novel genes, fanA and fanB, involved in the biogenesis !1of K99 fimbriae. !$#cross-references MUID:87316863; PMID:2888075 !$#accession B29112 !'##molecule_type DNA !'##residues 1-99 ##label ROO !'##cross-references GB:X05797; NID:g41404; PIDN:CAA29239.1; PID:g41406 COMMENT This is one of two homologous proteins encoded by genes !1upstream of the fanC gene, which codes for K99 fimbrial !1protein. These two trans-acting polypeptides, fanA and fanB, !1are involved in regulating the expression of fanC. GENETICS !$#gene fanB CLASSIFICATION #superfamily pap fimbrial activator protein papB KEYWORDS transcription regulation SUMMARY #length 99 #molecular-weight 11744 #checksum 7116 SEQUENCE /// ENTRY BVECDA #type complete TITLE cell division control protein dicA, phage protein-related - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 01-Mar-2002 ACCESSIONS S05260; S02246; B24328; E64912 REFERENCE S05260 !$#authors Bouche, J.P. !$#submission submitted to the EMBL Data Library, August 1988 !$#accession S05260 !'##molecule_type DNA !'##residues 1-135 ##label BOU !'##cross-references EMBL:X07465; NID:g312764; PIDN:CAA30349.1; !1PID:g41278 !'##experimental_source strain K12 REFERENCE S02245 !$#authors Bejar, S.; Bouche, F.; Bouche, J.P. !$#journal Mol. Gen. Genet. (1988) 212:11-19 !$#title Cell division inhibition gene dicB is regulated by a locus !1similar to lambdoid bacteriophage immunity loci. !$#cross-references MUID:88232418; PMID:2836697 !$#accession S02246 !'##molecule_type DNA !'##residues 1-79 ##label BEJ !'##cross-references EMBL:X07465 !'##experimental_source strain K12 REFERENCE A93636 !$#authors Bejar, S.; Cam, K.; Bouche, J.P. !$#journal Nucleic Acids Res. (1986) 14:6821-6833 !$#title Control of cell division in Escherichia coli. DNA sequence !1of dicA and of a second gene complementing mutation dicA1, !1dicC. !$#cross-references MUID:87016327; PMID:3532030 !$#accession B24328 !'##molecule_type DNA !'##residues 1-135 ##label BE2 !'##cross-references GB:X07465; GB:X04395; NID:g312764; PIDN:CAA30349.1; !1PID:g41278 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64912 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-135 ##label BLAT !'##cross-references GB:AE000253; GB:U00096; NID:g1787841; !1PIDN:AAC74643.1; PID:g1787853; UWGP:b1570 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene dicA !$#map_position 35 min FUNCTION !$#description repressor of cell division inhibition gene dicB CLASSIFICATION #superfamily dicA protein KEYWORDS cell division control; DNA binding; repressor; transcription !1regulation SUMMARY #length 135 #molecular-weight 15656 #checksum 9098 SEQUENCE /// ENTRY RGECPI #type complete TITLE transcription regulator papI - Escherichia coli ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jul-1999 ACCESSIONS A25121; S16393; S41549; A53886; S20048; S03797; S25214 REFERENCE A91031 !$#authors Baga, M.; Goransson, M.; Normark, S.; Uhlin, B.E. !$#journal EMBO J. (1985) 4:3887-3893 !$#title Transcriptional activation of a Pap pilus virulence operon !1from uropathogenic Escherichia coli. !$#cross-references MUID:86136032; PMID:2868893 !$#accession A25121 !'##molecule_type DNA !'##residues 1-77 ##label BAG !'##cross-references GB:X03391; GB:K01176; GB:X03392; NID:g42309; !1PIDN:CAA27124.1; PID:g42310 REFERENCE S16393 !$#authors Marklund, B.I.H. !$#submission submitted to the EMBL Data Library, August 1991 !$#accession S16393 !'##molecule_type DNA !'##residues 1-77 ##label MAR !'##cross-references EMBL:X61239; NID:g42290; PIDN:CAA43560.1; !1PID:g42291 !'##experimental_source strain J96 REFERENCE S41549 !$#authors Morschhaeuser, J.; Vetter, V.; Emoedy, L.; Hacker, J. !$#journal Mol. Microbiol. (1994) 11:555-566 !$#title Adhesin regulatory genes within large, unstable DNA regions !1of pathogenic Escherichia coli: cross-talk between different !1adhesin gene clusters. !$#cross-references MUID:94203058; PMID:7908714 !$#accession S41549 !'##status preliminary !'##molecule_type DNA !'##residues 1-46,'V',48-71,'S',73-77 ##label MOR !'##cross-references EMBL:X76613; NID:g435270; PIDN:CAA54078.1; !1PID:g435271 REFERENCE A53886 !$#authors Rhen, M.; Vaeisaenen-Rhen, V. !$#journal Microb. Pathog. (1987) 3:387-391 !$#title Nucleotide sequence analysis of a P fimbrial regulatory !1element of the uropathogenic Escherichia coli strain KS71 !1(04:K12). !$#cross-references MUID:89070275; PMID:2904639 !$#accession A53886 !'##status preliminary !'##molecule_type DNA !'##residues 1-44,'A',46-66,'K',68-71,'S',73-77 ##label RHE !'##cross-references GB:M57406; NID:g146568; PIDN:AAA24048.1; !1PID:g146569 !'##experimental_source strain KS71 REFERENCE S03797 !$#authors Blyn, L.B.; Braaten, B.A.; White-Ziegler, C.A.; Rolfson, !1D.H.; Low, D.A. !$#journal EMBO J. (1989) 8:613-620 !$#title Phase-variation of pyelonephritis-associated pili in !1Escherichia coli: evidence for transcriptional regulation. !$#cross-references MUID:89251590; PMID:2656260 !$#accession S20048 !'##molecule_type DNA !'##residues 1-44,'A',46-66,'K',68-71,'S',73-77 ##label BLY !'##cross-references EMBL:X14472; NID:g42279; PIDN:CAA32633.1; !1PID:g42280 !'##experimental_source strain C1212 !'##genetics P21 !$#accession S03797 !'##molecule_type DNA !'##residues 1-16,'D',18-44,'A',46-66,'K',68-71,'S',73-77 ##label BL2 !'##cross-references EMBL:X14471; NID:g42273; PIDN:CAA32630.1; !1PID:g42274 !'##experimental_source strain C1212 !'##genetics P17 REFERENCE S25205 !$#authors Marklund, B.I.; Tennent, J.M.; Garcia, E.; Hamers, A.; Baga, !1M.; Lindberg, F.; Gaastra, W.; Normark, S. !$#journal Mol. Microbiol. (1992) 6:2225-2242 !$#title Horizontal gene transfer of the Escherichia coli pap and prs !1pili operons as a mechanism for the development of !1tissue-specific adhesive properties. !$#cross-references MUID:93023852; PMID:1357526 !$#accession S25214 !'##molecule_type DNA !'##residues 1-77 ##label MAW !'##cross-references EMBL:X61239; NID:g42290; PIDN:CAA43560.1; !1PID:g42291 !'##experimental_source strain J96 !'##note in the authors translation an additional Ala is shown after !11-Met, consequently, residues 2-59 are displayed one codon !1to the left; 60-Tyr has not been translated GENETICS P21 !$#gene pap(21)I GENETICS P17 !$#gene pap(17)I CLASSIFICATION #superfamily P fimbrial transcription regulator KEYWORDS transcription regulation SUMMARY #length 77 #molecular-weight 8855 #checksum 3122 SEQUENCE /// ENTRY OUBP22 #type complete TITLE antirepressor protein ant - phage P22 ORGANISM #formal_name phage P22 #note host Salmonella spp. DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 16-Jul-1999 ACCESSIONS A03573 REFERENCE A92903 !$#authors Sauer, R.T.; Krovatin, W.; DeAnda, J.; Youderian, P.; !1Susskind, M.M. !$#journal J. Mol. Biol. (1983) 168:699-713 !$#title Primary structure of the ImmI immunity region of !1bacteriophage P22. !$#cross-references MUID:83294541; PMID:6350606 !$#accession A03573 !'##molecule_type DNA !'##residues 1-300 ##label SAU !'##cross-references GB:X01916; NID:g15637; PIDN:CAA25991.1; PID:g15640 !'##note residues 1-18 were confirmed by protein sequencing COMMENT This protein prevents the prophage P22 c2 repressor protein !1from binding to its operators and also inhibits the action !1of other prophage repressor proteins, including those of !1phages lambda and 434. The synthesis of antirepressor is !1negatively regulated by the protein products of the two !1other immI genes, mnt and arc. GENETICS !$#gene ant CLASSIFICATION #superfamily phage P22 antirepressor protein ant KEYWORDS transcription regulation SUMMARY #length 300 #molecular-weight 34649 #checksum 2101 SEQUENCE /// ENTRY RPECR1 #type complete TITLE tet repressor protein (Tn 1721) - Escherichia coli plasmid RP1 ORGANISM #formal_name Escherichia coli DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS A03574 REFERENCE A93486 !$#authors Waters, S.H.; Rogowsky, P.; Grinsted, J.; Altenbuchner, J.; !1Schmitt, R. !$#journal Nucleic Acids Res. (1983) 11:6089-6105 !$#title The tetracycline resistance determinants of RP1 and Tn1721: !1nucleotide sequence analysis. !$#cross-references MUID:83299270; PMID:6310527 !$#accession A03574 !'##molecule_type DNA !'##residues 1-216 ##label WAT !'##cross-references GB:X00006; NID:g42508; PIDN:CAA24908.1; PID:g42509 GENETICS !$#gene tetR !$#genome plasmid CLASSIFICATION #superfamily tetracycline repressor KEYWORDS antibiotic resistance; DNA binding; transcription regulation FEATURE !$25-46 #region helix-turn-helix #status predicted SUMMARY #length 216 #molecular-weight 23288 #checksum 1175 SEQUENCE /// ENTRY RPECYS #type complete TITLE tetracycline repressor - Escherichia coli plasmid pSC101 ORGANISM #formal_name Escherichia coli DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 16-Jul-1999 ACCESSIONS A03575 REFERENCE A03575 !$#authors Brow, M.A.D.; Pesin, R.; Sutcliffe, J.G. !$#journal Mol. Biol. Evol. (1985) 2:1-12 !$#title The tetracycline repressor of pSC101. !$#cross-references MUID:88216101; PMID:3916707 !$#accession A03575 !'##molecule_type DNA !'##residues 1-219 ##label BRO !'##cross-references GB:M36272; NID:g150945; PIDN:AAA25677.1; !1PID:g150946 COMMENT This protein is the repressor of the tetracycline resistance !1element; its amino-terminal region forms a helix-turn-helix !1structure and binds DNA. GENETICS !$#gene tetR !$#genome plasmid CLASSIFICATION #superfamily tetracycline repressor KEYWORDS antibiotic resistance; DNA binding; transcription regulation FEATURE !$24-46 #domain DNA binding #status predicted #label DBN\ !$25-46 #region helix-turn-helix #status predicted SUMMARY #length 219 #molecular-weight 24174 #checksum 9440 SEQUENCE /// ENTRY RPECTN #type complete TITLE repressor tetR - Escherichia coli transposon Tn10 ORGANISM #formal_name Escherichia coli DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 16-Jul-1999 ACCESSIONS A03576; S02667 REFERENCE A03576 !$#authors Postle, K.; Nguyen, T.T.; Bertrand, K.P. !$#journal Nucleic Acids Res. (1984) 12:4849-4863 !$#title Nucleotide sequence of the repressor gene of the TN10 !1tetracycline resistance determinant. !$#cross-references MUID:84247342; PMID:6330687 !$#accession A03576 !'##molecule_type DNA !'##residues 1-207 ##label POS !'##cross-references GB:X00694; NID:g43051; PIDN:CAA25291.1; PID:g43052 REFERENCE S02667 !$#authors Altschmied, L.; Baumeister, R.; Pfleiderer, K.; Hillen, W. !$#journal EMBO J. (1988) 7:4011-4017 !$#title A threonine to alanine exchange at position 40 of tet !1repressor alters the recognition of the sixth base pair of !1tet operator from GC to AT. !$#cross-references MUID:89091153; PMID:3208760 !$#accession S02667 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-100 ##label ALT !'##cross-references GB:J01830; NID:g154845 COMMENT This protein contains sequences similar to the DNA !1recognition regions of other DNA-binding proteins. GENETICS !$#gene tetR CLASSIFICATION #superfamily tetracycline repressor KEYWORDS antibiotic resistance; DNA binding; transcription regulation FEATURE !$25-46 #region helix-turn-helix #status predicted SUMMARY #length 207 #molecular-weight 23354 #checksum 5994 SEQUENCE /// ENTRY RCBPL #type complete TITLE regulatory protein cro [validated] - phage lambda ORGANISM #formal_name phage lambda DATE 31-Mar-1980 #sequence_revision 29-Jun-1981 #text_change 15-Sep-2000 ACCESSIONS B94614; D92891; B93195; A93189; A93190; A03577 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession B94614 !'##molecule_type DNA !'##residues 1-66 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession D92891 !'##molecule_type DNA !'##residues 1-66 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96582.1; PID:g215148 REFERENCE A93195 !$#authors Schwarz, E.; Scherer, G.; Hobom, G.; Kossel, H. !$#journal Nature (1978) 272:410-414 !$#title Nucleotide sequence of cro, cII and part of the O gene in !1phage lambda DNA. !$#cross-references MUID:78135462; PMID:264238 !$#contents lambda-dvh93 !$#accession B93195 !'##molecule_type DNA !'##residues 1-66 ##label SCH !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96582.1; PID:g215148 !'##note lambda-dvh93 is a bacteriophage lambda-derived E. coli plasmid REFERENCE A93189 !$#authors Roberts, T.M.; Shimatake, H.; Brady, C.; Rosenberg, M. !$#journal Nature (1977) 270:274-275 !$#title Sequence of cro gene of bacteriophage lambda. !$#cross-references MUID:78071724; PMID:593347 !$#accession A93189 !'##molecule_type DNA !'##residues 1-66 ##label ROB !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96582.1; PID:g215148 REFERENCE A93190 !$#authors Hsiang, M.W.; Cole, R.D.; Takeda, Y.; Echols, H. !$#journal Nature (1977) 270:275-277 !$#title Amino acid sequence of cro regulatory protein of !1bacteriophage lambda. !$#cross-references MUID:78071725; PMID:593348 !$#accession A93190 !'##molecule_type protein !'##residues 1-66 ##label HSI REFERENCE A93252 !$#authors Anderson, W.F.; Ohlendorf, D.H.; Takeda, Y.; Matthews, B.W. !$#journal Nature (1981) 290:754-758 !$#title Structure of the cro repressor from bacteriophage lambda and !1its interaction with DNA. !$#cross-references MUID:81173109; PMID:6452580 !$#contents annotation; X-ray crystallography, 2.8 angstroms REFERENCE A50100 !$#authors Ohlendorf, D.H.; Anderson, W.F.; Takeda, Y.; Matthews, B.W. !$#submission submitted to the Brookhaven Protein Data Bank, June 1987 !$#cross-references PDB:1CRO !$#contents annotation; X-ray crystallography, 2.2 angstroms, residues !11-66 REFERENCE A50653 !$#authors Brennan, R.G.; Roderick, S.L.; Takeda, Y.; Matthews, B.W. !$#submission submitted to the Brookhaven Protein Data Bank, September !11990 !$#cross-references PDB:4CRO !$#contents annotation; X-ray crystallography, 3.9 angstroms, residues !13-66 REFERENCE A36209 !$#authors Brennan, R.G.; Roderick, S.L.; Takeda, Y.; Matthews, B.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:8165-8169 !$#title Protein-DNA conformational changes in the crystal structure !1of a lambda Cro-operator complex. !$#cross-references MUID:91045958; PMID:2146682 !$#contents annotation; X-ray crystallography, 3.9 angstroms REFERENCE A65311 !$#authors Matsuo, H.; Shirakawa, M.; Kyogoku, Y. !$#submission submitted to the Brookhaven Protein Data Bank, June 1995 !$#cross-references PDB:1COP !$#contents annotation; conformation by (1)H-, (15)N- and (13)C-NMR, !1residues 1-66 REFERENCE A59015 !$#authors Matsuo, H.; Shirakawa, M.; Kyogoku, Y. !$#journal J. Mol. Biol. (1995) 254:668-680 !$#title Three-dimensional dimer structure of the lambda-Cro !1repressor in solution as determined by heteronuclear !1multidimensional NMR. !$#cross-references MUID:96102289; PMID:7500341 !$#contents annotation; conformation by (1)H-, (13)C- and (15)N-NMR GENETICS !$#gene cro !$#map_position 78.43-78.84 COMPLEX homodimer FUNCTION !$#description homodimer binds sequence specifically to DNA at the cro OR !1operator site repressing transcription of genes otherwise !1expressed in early phage development CLASSIFICATION #superfamily phage lambda regulatory protein cro KEYWORDS DNA binding; early protein; homodimer; transcription !1regulation FEATURE !$16-36 #region helix-turn-helix motif SUMMARY #length 66 #molecular-weight 7363 #checksum 8085 SEQUENCE /// ENTRY RGBP22 #type complete TITLE regulatory protein cro - phage P22 ORGANISM #formal_name phage P22 #note host Salmonella typhimurium DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS A25867 REFERENCE A90503 !$#authors Poteete, A.R.; Hehir, K.; Sauer, R.T. !$#journal Biochemistry (1986) 25:251-256 !$#title Bacteriophage P22 cro protein: sequence, purification, and !1properties. !$#cross-references MUID:86159692; PMID:3954988 !$#accession A25867 !'##molecule_type DNA !'##residues 1-61 ##label POT !'##cross-references GB:M12584; NID:g215271; PIDN:AAA32268.1; !1PID:g215272 GENETICS !$#gene cro CLASSIFICATION #superfamily phage P22 regulatory protein cro KEYWORDS DNA binding; transcription regulation SUMMARY #length 61 #molecular-weight 6828 #checksum 5828 SEQUENCE /// ENTRY RGBPHK #type complete TITLE regulatory protein cro - phage HK022 ORGANISM #formal_name phage HK022 #note host Escherichia coli DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Feb-1997 ACCESSIONS S06542 REFERENCE S04989 !$#authors Oberto, J.; Weisberg, R.A.; Gottesman, M.E. !$#journal J. Mol. Biol. (1989) 207:675-693 !$#title Structure and function of the nun gene and the immunity !1region of the lambdoid phage HK022. !$#cross-references MUID:89342456; PMID:2760929 !$#accession S06542 !'##molecule_type DNA !'##residues 1-70 ##label OBE GENETICS !$#gene cro CLASSIFICATION #superfamily phage HK022 regulatory protein cro KEYWORDS DNA binding; transcription regulation SUMMARY #length 70 #molecular-weight 7936 #checksum 3749 SEQUENCE /// ENTRY Z1BPHK #type complete TITLE regulatory protein cI - phage HK022 ORGANISM #formal_name phage HK022 #note host Escherichia coli DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Feb-1997 ACCESSIONS S06541 REFERENCE S04989 !$#authors Oberto, J.; Weisberg, R.A.; Gottesman, M.E. !$#journal J. Mol. Biol. (1989) 207:675-693 !$#title Structure and function of the nun gene and the immunity !1region of the lambdoid phage HK022. !$#cross-references MUID:89342456; PMID:2760929 !$#accession S06541 !'##molecule_type DNA !'##residues 1-208 ##label OBE GENETICS !$#gene cI CLASSIFICATION #superfamily phage HK022 regulatory protein cI KEYWORDS DNA binding; transcription regulation SUMMARY #length 208 #molecular-weight 23108 #checksum 2005 SEQUENCE /// ENTRY Z1BPC2 #type complete TITLE regulatory protein cI - phage P22 ORGANISM #formal_name phage P22 #note host Salmonella typhimurium DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 16-Jul-1999 ACCESSIONS A91518; A90503; A42966; A03578; B25867 REFERENCE A91518 !$#authors Backhaus, H.; Petri, J.B. !$#journal Gene (1984) 32:289-303 !$#title Sequence analysis of a region from the early right operon in !1phage P22 including the replication genes 18 and 12. !$#cross-references MUID:85155495; PMID:6241581 !$#accession A91518 !'##molecule_type DNA !'##residues 1-92 ##label REA !'##cross-references GB:M10074; NID:g215307; PIDN:AAA32274.1; !1PID:g215309 REFERENCE A90503 !$#authors Poteete, A.R.; Hehir, K.; Sauer, R.T. !$#journal Biochemistry (1986) 25:251-256 !$#title Bacteriophage P22 cro protein: sequence, purification, and !1properties. !$#cross-references MUID:86159692; PMID:3954988 !$#accession A90503 !'##molecule_type DNA !'##residues 1-92 ##label REB !'##cross-references GB:M12584; NID:g215271; PIDN:AAA32269.1; !1PID:g215273 REFERENCE A42966 !$#authors Ho, Y.S.; Pfarr, D.; Strickler, J.; Rosenberg, M. !$#journal J. Biol. Chem. (1992) 267:14388-14397 !$#title Characterization of the transcription activator protein C1 !1of bacteriophage P22. !$#cross-references MUID:92332555; PMID:1385814 !$#accession A42966 !'##molecule_type protein !'##residues 1-82,'D',84 ##label HO1 !'##note sequence extracted from NCBI backbone (NCBIP:108590) COMMENT This protein is related to the regulatory protein CII of !1bacteriophages lambda and 434. GENETICS !$#gene cI CLASSIFICATION #superfamily phage P22 regulatory protein cI KEYWORDS DNA binding; transcription regulation SUMMARY #length 92 #molecular-weight 10211 #checksum 1220 SEQUENCE /// ENTRY QCBP2L #type complete TITLE regulatory protein cII - phage lambda ORGANISM #formal_name phage lambda DATE 31-Mar-1980 #sequence_revision 24-Sep-1981 #text_change 16-Jul-1999 ACCESSIONS A03579; B03579; C03579; D03579 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession A03579 !'##molecule_type DNA !'##residues 1-97 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession B03579 !'##molecule_type DNA !'##residues 1-97 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96583.1; PID:g215149 REFERENCE A93195 !$#authors Schwarz, E.; Scherer, G.; Hobom, G.; Kossel, H. !$#journal Nature (1978) 272:410-414 !$#title Nucleotide sequence of cro, cII and part of the O gene in !1phage lambda DNA. !$#cross-references MUID:78135462; PMID:264238 !$#contents lambda-dvh93 !$#accession C03579 !'##molecule_type DNA !'##residues 1-79 ##label SCH !'##note lambda-dvh93 is a bacteriophage lambda-derived E. coli plasmid REFERENCE A91584 !$#authors Ovchinnikov, Y.A.; Guryev, S.O.; Krayev, A.S.; !1Monastyrskaya, G.S.; Skryabin, K.G.; Sverdlov, E.D.; !1Zakharyev, V.M.; Bayev, A.A. !$#journal Gene (1979) 6:235-249 !$#title Primary structure of an EcoRI fragment of lambdaimm434 DNA !1containing regions cI-cro of phage 434 and cII-0 of phage !1lambda. !$#cross-references MUID:80004841; PMID:478301 !$#contents lambda-imm434 !$#accession D03579 !'##molecule_type DNA !'##residues 1-79 ##label OVC !'##note lambda-imm434 is a hybrid of bacteriophages 434 and lambda; the !1cII protein coding region is in the lambda portion of the !1imm434 genome COMMENT This protein and the gene cIII product form a complex that !1is involved in the initiation of lysogeny. GENETICS !$#gene cII !$#map_position 79.0-79.6 (Lambda) CLASSIFICATION #superfamily phage P22 regulatory protein cI KEYWORDS DNA binding; early protein; transcription SUMMARY #length 97 #molecular-weight 11056 #checksum 8003 SEQUENCE /// ENTRY QCBP43 #type complete TITLE regulatory protein cII - phage 434 ORGANISM #formal_name phage 434 DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jul-1999 ACCESSIONS E03579; A03579 REFERENCE A03572 !$#authors Grosschedl, R.; Schwarz, E. !$#journal Nucleic Acids Res. (1979) 6:867-881 !$#title Nucleotide sequence of the cro-cII-oop region of !1bacteriophage 434 DNA. !$#cross-references MUID:79179801; PMID:375198 !$#accession E03579 !'##molecule_type DNA !'##residues 1-97 ##label GRO !'##cross-references GB:V00635; GB:J02475; NID:g14988; PIDN:CAA23909.1; !1PID:g14990 COMMENT This protein and the gene cIII product form a complex that !1is involved in the initiation of lysogeny. The complex binds !1at either of the cY regulatory sites preceding the cI !1repressor protein and integrase coding regions and induces !1transcription of these genes. GENETICS !$#gene cII CLASSIFICATION #superfamily phage P22 regulatory protein cI KEYWORDS DNA binding; early protein; transcription SUMMARY #length 97 #molecular-weight 11072 #checksum 8345 SEQUENCE /// ENTRY QCBP3L #type complete TITLE regulatory protein cIII - phage lambda ORGANISM #formal_name phage lambda DATE 02-Apr-1982 #sequence_revision 13-Jun-1983 #text_change 16-Jul-1999 ACCESSIONS C94614; E92891; A93737; A03580 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession C94614 !'##molecule_type DNA !'##residues 1-54 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession E92891 !'##molecule_type DNA !'##residues 1-54 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96573.1; PID:g215141 REFERENCE A93737 !$#authors Ineichen, K.; Shepherd, J.C.W.; Bickle, T.A. !$#journal Nucleic Acids Res. (1981) 9:4639-4653 !$#title The DNA sequence of the phage lambda genome between P-L and !1the gene bet. !$#cross-references MUID:82059489; PMID:6458018 !$#accession A93737 !'##molecule_type DNA !'##residues 1-54 ##label INE !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96573.1; PID:g215141 !'##note these authors do not agree with the assignment of the coding !1region for the sequence shown to gene cIII; the sequence !1that they have assigned as the gene cIII product is shown in !1the entry for the kil gene protein COMMENT This protein and the gene cII product form a complex that is !1involved in the initiation of lysogeny. The complex binds at !1either of the cY regulatory sites preceding the cI repressor !1protein and integrase coding regions and induces !1transcription of these genes. GENETICS !$#gene cIII !$#map_position 68.98-68.43 CLASSIFICATION #superfamily phage lambda regulatory protein cIII KEYWORDS transcription regulation SUMMARY #length 54 #molecular-weight 6047 #checksum 5163 SEQUENCE /// ENTRY QCBP22 #type complete TITLE regulatory protein cIII - phage P22 ORGANISM #formal_name phage P22 #note host Salmonella typhimurium DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Jul-1999 ACCESSIONS S04247 REFERENCE S04245 !$#authors Semerjian, A.V.; Malloy, D.C.; Poteete, A.R. !$#journal J. Mol. Biol. (1989) 207:1-13 !$#title Genetic structure of the bacteriophage P22 P(L) operon. !$#cross-references MUID:89293845; PMID:2738922 !$#accession S04247 !'##molecule_type DNA !'##residues 1-52 ##label SEM !'##cross-references GB:X15637; NID:g15646; PIDN:CAA33651.1; PID:g15651 GENETICS !$#gene cIII CLASSIFICATION #superfamily phage lambda regulatory protein cIII KEYWORDS transcription regulation SUMMARY #length 52 #molecular-weight 5734 #checksum 4155 SEQUENCE /// ENTRY QCBPHK #type complete TITLE regulatory protein cIII - phage HK022 ORGANISM #formal_name phage HK022 #note host Escherichia coli DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Jul-1999 ACCESSIONS S06538 REFERENCE S04989 !$#authors Oberto, J.; Weisberg, R.A.; Gottesman, M.E. !$#journal J. Mol. Biol. (1989) 207:675-693 !$#title Structure and function of the nun gene and the immunity !1region of the lambdoid phage HK022. !$#cross-references MUID:89342456; PMID:2760929 !$#accession S06538 !'##molecule_type DNA !'##residues 1-44 ##label OBE !'##cross-references GB:X16093; NID:g435309; PIDN:CAA34220.1; PID:g15764 GENETICS !$#gene cIII CLASSIFICATION #superfamily phage lambda regulatory protein cIII KEYWORDS transcription regulation SUMMARY #length 44 #molecular-weight 4994 #checksum 3954 SEQUENCE /// ENTRY VNBPL #type complete TITLE regulatory protein N - phage lambda ORGANISM #formal_name phage lambda DATE 31-Oct-1980 #sequence_revision 13-Jun-1983 #text_change 28-Jul-2000 ACCESSIONS D94614; F92891; B93737; A91612; A03581 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession D94614 !'##molecule_type DNA !'##residues 1-133 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession F92891 !'##molecule_type DNA !'##residues 1-133 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96578.1; PID:g508997 REFERENCE A93737 !$#authors Ineichen, K.; Shepherd, J.C.W.; Bickle, T.A. !$#journal Nucleic Acids Res. (1981) 9:4639-4653 !$#title The DNA sequence of the phage lambda genome between P-L and !1the gene bet. !$#cross-references MUID:82059489; PMID:6458018 !$#accession B93737 !'##molecule_type DNA !'##residues 1-133 ##label INE !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96578.1; PID:g508997 REFERENCE A91612 !$#authors Franklin, N.C.; Bennett, G.N. !$#journal Gene (1979) 8:107-119 !$#title The N protein of bacteriophage lambda, defined by its DNA !1sequence, is highly basic. !$#cross-references MUID:80135174; PMID:43815 !$#accession A91612 !'##molecule_type DNA !'##residues 1-133 ##label FRA !'##cross-references GB:V00637; NID:g15058; PIDN:CAA23975.1; PID:g15059 !'##note Met-27 may correspond to the in vivo initiator methionine COMMENT The N gene product regulates the transition from the early !1to the middle stage of lytic development. It is a !1transcription antitermination protein that prevents !1termination at the rho-dependent TL and TR transcription !1termination sites. GENETICS !$#gene N !$#map_position 73.07-72.24 CLASSIFICATION #superfamily phage lambda regulatory protein N KEYWORDS DNA binding; RNA binding; transcription regulation FEATURE !$31-37 #region arginine-rich RNA-binding pattern SUMMARY #length 133 #molecular-weight 15374 #checksum 9453 SEQUENCE /// ENTRY VNBPHK #type complete TITLE regulatory protein nun - phage HK022 ALTERNATE_NAMES transcription termination factor ORGANISM #formal_name phage HK022 #note host Escherichia coli DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 15-Oct-1999 ACCESSIONS S06539 REFERENCE S04989 !$#authors Oberto, J.; Weisberg, R.A.; Gottesman, M.E. !$#journal J. Mol. Biol. (1989) 207:675-693 !$#title Structure and function of the nun gene and the immunity !1region of the lambdoid phage HK022. !$#cross-references MUID:89342456; PMID:2760929 !$#accession S06539 !'##molecule_type DNA !'##residues 1-112 ##label OBE !'##cross-references GB:X16093; NID:g435309; PIDN:CAA34221.1; PID:g15765 GENETICS !$#gene nun CLASSIFICATION #superfamily phage HK022 regulatory protein nun KEYWORDS transcription termination SUMMARY #length 112 #molecular-weight 13108 #checksum 3649 SEQUENCE /// ENTRY IUBPU #type fragment TITLE cim protein - phage Mu (fragment) ORGANISM #formal_name phage Mu DATE 18-Dec-1981 #sequence_revision 18-Dec-1981 #text_change 31-Dec-1993 ACCESSIONS A03582 REFERENCE A03582 !$#authors Engler, J.A.; van Bree, M.P. !$#journal Gene (1981) 14:155-163 !$#title The nucleotide sequence and protein-coding capability of the !1transposable element IS5. !$#cross-references MUID:82028652; PMID:6269958 !$#accession A03582 !'##molecule_type DNA !'##residues 1-48 ##label ENG !'##note the authors translated the codon CNG for 44-X as Leu COMMENT Bacteriophage Mu is a temperate phage that is related to !1bacteriophage lambda. Temperate phages exhibit two !1alternative developmental cycles. In the lysogenic cycle, !1the phage becomes incorporated into the host genome and !1replicates along with the host. In the lytic cycle, the !1phage multiplies, forms mature phage particles, and lyses !1the host cell. Host cells harboring lysogenic Mu phages are !1immune to lytic infection by Mu. COMMENT Gene cim protein stimulates Mu immunity, presumably by a !1positive control of repressor synthesis. The cim gene is not !1necessary for lytic development. CLASSIFICATION #superfamily phage Mu cim protein SUMMARY #length 48 #checksum 1403 SEQUENCE /// ENTRY ZQBPL #type complete TITLE regulatory protein Q - phage lambda ORGANISM #formal_name phage lambda DATE 02-Apr-1982 #sequence_revision 13-Jun-1983 #text_change 16-Jul-1999 ACCESSIONS E94614; G92891; A91297; A03583 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession E94614 !'##molecule_type DNA !'##residues 1-207 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession G92891 !'##molecule_type DNA !'##residues 1-207 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96595.1; PID:g215161 REFERENCE A91297 !$#authors Petrov, N.A.; Karginov, V.A.; Mikriukov, N.N.; Serpinski, !1O.I.; Kravchenko, V.V. !$#journal FEBS Lett. (1981) 133:316-320 !$#title Complete nucleotide sequence of the bacteriophage lambda DNA !1region region containing gene Q and promoter rho-R. !$#cross-references MUID:82073288; PMID:6458514 !$#accession A91297 !'##molecule_type DNA !'##residues 1-204,'I',206-207 ##label PET COMMENT The Q gene protein regulates the transition from the middle !1to the late stage of lytic development. It has been proposed !1that, like the N protein, the Q gene product acts as a !1transcriptional antitermination protein. GENETICS !$#gene Q !$#map_position 90.48-91.76 CLASSIFICATION #superfamily phage lambda regulatory protein Q KEYWORDS DNA binding; transcription regulation SUMMARY #length 207 #molecular-weight 22473 #checksum 4544 SEQUENCE /// ENTRY RGBPS1 #type complete TITLE transcription initiation factor sigma - phage SPO1 ALTERNATE_NAMES regulatory protein sigma-gp28 ORGANISM #formal_name phage SPO1 #note host Bacillus subtilis DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 16-Jun-2000 ACCESSIONS A03584 REFERENCE A03584 !$#authors Costanzo, M.; Pero, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:1236-1240 !$#title Structure of a Bacillus subtilis bacteriophage SPO1 gene !1encoding a RNA polymerase sigma factor. !$#cross-references MUID:83144054; PMID:6402778 !$#accession A03584 !'##molecule_type DNA !'##residues 1-220 ##label COS !'##cross-references GB:V01375; NID:g15781; PIDN:CAA24664.1; !1PID:g4388648 COMMENT This protein binds to the bacterial core RNA polymerase to !1direct the recognition of phage middle gene promoters. GENETICS !$#gene 28 CLASSIFICATION #superfamily phage SPO1 regulatory protein sigma-gp28 KEYWORDS DNA binding; sigma factor; transcription initiation SUMMARY #length 220 #molecular-weight 25709 #checksum 8826 SEQUENCE /// ENTRY RGBPM2 #type complete TITLE regulatory protein mnt - phage P22 ORGANISM #formal_name phage P22 #note host Salmonella spp. DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 16-Jul-1999 ACCESSIONS A03585 REFERENCE A92903 !$#authors Sauer, R.T.; Krovatin, W.; DeAnda, J.; Youderian, P.; !1Susskind, M.M. !$#journal J. Mol. Biol. (1983) 168:699-713 !$#title Primary structure of the ImmI immunity region of !1bacteriophage P22. !$#cross-references MUID:83294541; PMID:6350606 !$#accession A03585 !'##molecule_type DNA !'##residues 1-83 ##label SAU !'##cross-references GB:X01916; NID:g15637; PIDN:CAA25989.1; PID:g15638 COMMENT This protein acts as a transcriptional repressor of genes !1ant and arc. GENETICS !$#gene mnt CLASSIFICATION #superfamily phage P22 regulatory protein mnt KEYWORDS DNA binding; repressor; transcription regulation SUMMARY #length 83 #molecular-weight 9678 #checksum 3603 SEQUENCE /// ENTRY RGBPA2 #type complete TITLE regulatory protein arc - phage P22 ORGANISM #formal_name phage P22 #note host Salmonella spp. DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 16-Jul-1999 ACCESSIONS A03586 REFERENCE A92903 !$#authors Sauer, R.T.; Krovatin, W.; DeAnda, J.; Youderian, P.; !1Susskind, M.M. !$#journal J. Mol. Biol. (1983) 168:699-713 !$#title Primary structure of the ImmI immunity region of !1bacteriophage P22. !$#cross-references MUID:83294541; PMID:6350606 !$#accession A03586 !'##molecule_type DNA !'##residues 1-53 ##label SAU !'##cross-references GB:X01916; NID:g15637; PIDN:CAA25990.1; PID:g15639 COMMENT This protein acts as a transcriptional repressor of its own !1gene arc and gene ant. GENETICS !$#gene arc CLASSIFICATION #superfamily phage P22 regulatory protein mnt KEYWORDS DNA binding; repressor; transcription regulation SUMMARY #length 53 #molecular-weight 6227 #checksum 9367 SEQUENCE /// ENTRY RGECRE #type complete TITLE regulatory protein rop - Escherichia coli plasmids ORGANISM #formal_name Escherichia coli DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 21-Jul-2000 ACCESSIONS A03587; A90923; A21164; B21164 REFERENCE A93930 !$#authors Cesareni, G.; Muesing, M.A.; Polisky, B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:6313-6317 !$#title Control of ColE1 DNA replication: the rop gene product !1negatively affects transcription from the replication primer !1promoter. !$#cross-references MUID:83065167; PMID:6183660 !$#accession A03587 !'##molecule_type DNA !'##residues 1-63 ##label CES !'##cross-references GB:J01573 !'##experimental_source plasmid colicin E1 !'##note this translation is not annotated in GenBank entry CE1ROP, !1release 117.0 REFERENCE A90923 !$#authors Sutcliffe, J.G. !$#journal Cold Spring Harb. Symp. Quant. Biol. (1979) 43:77-90 !$#title Complete nucleotide sequence of the Escherichia coli plasmid !1pBR322. !$#cross-references MUID:80002802; PMID:383387 !$#accession A90923 !'##molecule_type DNA !'##residues 1-63 ##label SUT !'##cross-references GB:J01749; PIDN:AAB59736.1 !'##experimental_source plasmid pBR322 REFERENCE A21164 !$#authors Som, T.; Tomizawa, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:3232-3236 !$#title Regulatory regions of ColE1 that are involved in !1determination of plasmid copy number. !$#cross-references MUID:83221569; PMID:6304700 !$#accession A21164 !'##molecule_type mRNA !'##residues 1-37,'EC',40-63 ##label SOM !'##cross-references GB:J01564 !'##experimental_source plasmid ColE1 !'##note the authors translated the codon TAC for residue 49 as Thr !'##note the sequence is revised in GenBank entry CE1COP, release 117, !1(PIDN:AAA87380.1) !$#accession B21164 !'##molecule_type mRNA !'##residues 1-40,'GDKAGKNM' ##label SO2 !'##cross-references GB:J01564 !'##experimental_source plasmid ColE1 !'##note the authors translated the codon AAC for residue 47 as Ser !'##note this sequence is derived from a deletion mutant in clone pnt209 GENETICS !$#gene rop !$#genome plasmid !$#start_codon GTG FUNCTION !$#description regulates plasmid DNA replication by modulating the !1initiation of transcription of the primer RNA precursor CLASSIFICATION #superfamily regulatory protein rop KEYWORDS plasmid DNA replication; transcription regulation SUMMARY #length 63 #molecular-weight 7228 #checksum 3310 SEQUENCE /// ENTRY WMEC15 #type complete TITLE ybgC protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 15-Oct-1982 #sequence_revision 30-Jun-1988 #text_change 01-Mar-2002 ACCESSIONS A25980; G64809 REFERENCE A91835 !$#authors Sun, T.P.; Webster, R.E. !$#journal J. Bacteriol. (1987) 169:2667-2674 !$#title Nucleotide sequence of a gene cluster involved in entry of E !1colicins and single-stranded DNA of infecting filamentous !1bacteriophages into Escherichia coli. !$#cross-references MUID:87222192; PMID:3294803 !$#accession A25980 !'##molecule_type DNA !'##residues 1-134 ##label SUN !'##cross-references GB:M16489; NID:g148021; PIDN:AAA83918.1; !1PID:g1128977 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64809 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-134 ##label BLAT !'##cross-references GB:AE000177; GB:U00096; NID:g1786955; !1PIDN:AAC73830.1; PID:g1786957; UWGP:b0736 !'##experimental_source strain K-12, substrain MG1655 COMMENT This is one of the proteins, encoded by the fii-tolAB gene !1cluster, that is involved in transporting colicins and !1getting them to their corresponding targets. GENETICS !$#gene ybgC !$#map_position 17 min !$#start_codon GTG CLASSIFICATION #superfamily 15.5K protein (tolAB operon 5' region) SUMMARY #length 134 #molecular-weight 15562 #checksum 9156 SEQUENCE /// ENTRY BVECTQ #type complete TITLE biopolymer transport protein tolQ - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 01-Mar-2002 ACCESSIONS B25980; H64809 REFERENCE A91835 !$#authors Sun, T.P.; Webster, R.E. !$#journal J. Bacteriol. (1987) 169:2667-2674 !$#title Nucleotide sequence of a gene cluster involved in entry of E !1colicins and single-stranded DNA of infecting filamentous !1bacteriophages into Escherichia coli. !$#cross-references MUID:87222192; PMID:3294803 !$#accession B25980 !'##molecule_type DNA !'##residues 1-230 ##label SUN !'##cross-references GB:M16489; NID:g148021; PIDN:AAA83919.1; !1PID:g1128978 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64809 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-230 ##label BLAT !'##cross-references GB:AE000177; GB:U00096; NID:g1786955; !1PIDN:AAC73831.1; PID:g1786958; UWGP:b0737 !'##experimental_source strain K-12, substrain MG1655 COMMENT This is one of the proteins, encoded by the fii-tolAB gene !1cluster, that is involved in transporting colicins and !1getting them to their corresponding targets. GENETICS !$#gene tolQ; fii !$#map_position 17 min !$#start_codon GTG CLASSIFICATION #superfamily biopolymer transport protein KEYWORDS transmembrane protein; transport protein FEATURE !$20-36 #domain transmembrane #status predicted #label TM1\ !$140-156 #domain transmembrane #status predicted #label TM2\ !$174-190 #domain transmembrane #status predicted #label TM3 SUMMARY #length 230 #molecular-weight 25597 #checksum 7545 SEQUENCE /// ENTRY BVECXB #type complete TITLE biopolymer transport ExbB protein ECs3890 [imported] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1991 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS D65087; JV0029 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65087 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-244 ##label BLAT !'##cross-references GB:AE000383; GB:U00096; NID:g2367184; !1PIDN:AAC76042.1; PID:g1789381; UWGP:b3006 !'##experimental_source strain K-12, substrain MG1655 REFERENCE JV0029 !$#authors Eick-Helmerich, K.; Braun, V. !$#journal J. Bacteriol. (1989) 171:5117-5126 !$#title Import of biopolymers into Escherichia coli: nucleotide !1sequences of the exbB and exbD genes are homologous to those !1of the tolQ and tolR genes, respectively. !$#cross-references MUID:89359155; PMID:2670903 !$#accession JV0029 !'##molecule_type DNA !'##residues 1-50,'L',52-235,'A',237-244 ##label EIC !'##cross-references GB:M28819; NID:g145866; PIDN:AAA23732.1; !1PID:g145868 COMMENT This protein is involved in transporting the group B !1colicins and getting them to their corresponding targets. GENETICS !$#gene exbB !$#map_position 65 min !$#start_codon GTG CLASSIFICATION #superfamily biopolymer transport protein KEYWORDS transmembrane protein FEATURE !$25-42 #domain transmembrane #status predicted #label TM1\ !$132-150 #domain transmembrane #status predicted #label TM2\ !$178-195 #domain transmembrane #status predicted #label TM3 SUMMARY #length 244 #molecular-weight 26287 #checksum 1326 SEQUENCE /// ENTRY H64057 #type complete TITLE biopolymer transport protein homolog HI0253 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS H64057 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession H64057 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-150 ##label TIGR !'##cross-references GB:U32711; GB:L42023; NID:g1573214; !1PIDN:AAC21919.1; PID:g1573219; TIGR:HI0253 CLASSIFICATION #superfamily biopolymer transport protein SUMMARY #length 150 #molecular-weight 16729 #checksum 1688 SEQUENCE /// ENTRY E64700 #type complete TITLE biopolymer transport protein - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS E64700 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession E64700 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-150 ##label TOM !'##cross-references GB:AE000644; GB:AE000511; NID:g2314609; !1PIDN:AAD08483.1; PID:g2314617; TIGR:HP1445 CLASSIFICATION #superfamily biopolymer transport protein SUMMARY #length 150 #molecular-weight 16638 #checksum 9678 SEQUENCE /// ENTRY C64687 #type complete TITLE biopolymer transport protein - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C64687 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession C64687 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-166 ##label TOM !'##cross-references GB:AE000635; GB:AE000511; NID:g2314502; !1PIDN:AAD08381.1; PID:g2314506; TIGR:HP1339 CLASSIFICATION #superfamily biopolymer transport protein SUMMARY #length 166 #molecular-weight 18288 #checksum 7707 SEQUENCE /// ENTRY BVECTR #type complete TITLE tolR protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 01-Mar-2002 ACCESSIONS C25980; A64810 REFERENCE A91835 !$#authors Sun, T.P.; Webster, R.E. !$#journal J. Bacteriol. (1987) 169:2667-2674 !$#title Nucleotide sequence of a gene cluster involved in entry of E !1colicins and single-stranded DNA of infecting filamentous !1bacteriophages into Escherichia coli. !$#cross-references MUID:87222192; PMID:3294803 !$#accession C25980 !'##molecule_type DNA !'##residues 1-142 ##label SUN !'##cross-references GB:M16489; NID:g148021; PIDN:AAA83921.1; !1PID:g1128980 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64810 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-142 ##label BLAT !'##cross-references GB:AE000177; GB:U00096; NID:g1786955; !1PIDN:AAC73832.1; PID:g1786959; UWGP:b0738 !'##experimental_source strain K-12, substrain MG1655 COMMENT This is one of the proteins, encoded by the fii-tolAB gene !1cluster, that is involved in transporting colicins and !1getting them to their corresponding targets. GENETICS !$#gene tolR !$#map_position 17 min CLASSIFICATION #superfamily tolR protein KEYWORDS transmembrane protein FEATURE !$18-34 #domain transmembrane #status predicted #label TMM SUMMARY #length 142 #molecular-weight 15383 #checksum 4056 SEQUENCE /// ENTRY BVECED #type complete TITLE biopolymer transport exbD protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 01-Mar-2002 ACCESSIONS JV0030; C65087 REFERENCE JV0029 !$#authors Eick-Helmerich, K.; Braun, V. !$#journal J. Bacteriol. (1989) 171:5117-5126 !$#title Import of biopolymers into Escherichia coli: nucleotide !1sequences of the exbB and exbD genes are homologous to those !1of the tolQ and tolR genes, respectively. !$#cross-references MUID:89359155; PMID:2670903 !$#accession JV0030 !'##molecule_type DNA !'##residues 1-141 ##label EIC !'##cross-references GB:M28819; NID:g145866; PIDN:AAA23733.1; !1PID:g145869 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65087 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-141 ##label BLAT !'##cross-references GB:AE000383; GB:U00096; NID:g2367184; !1PIDN:AAC76041.1; PID:g1789380; UWGP:b3005 !'##experimental_source strain K-12, substrain MG1655 COMMENT This protein is involved in transporting the group B !1colicins and getting them to their corresponding targets. GENETICS !$#gene exbD !$#map_position 65 min CLASSIFICATION #superfamily tolR protein KEYWORDS transmembrane protein FEATURE !$26-43 #domain transmembrane #status predicted #label TMM SUMMARY #length 141 #molecular-weight 15527 #checksum 1090 SEQUENCE /// ENTRY RGECRI #type complete TITLE regulatory protein RepI - Escherichia coli plasmids ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 19-Jan-1996 #text_change 16-Jul-1999 ACCESSIONS JH0130; PS0293; A25546 REFERENCE JH0123 !$#authors Scholz, P.; Haring, V.; Wittmann-Liebold, B.; Ashman, K.; !1Bagdasarian, M.; Scherzinger, E. !$#journal Gene (1989) 75:271-288 !$#title Complete nucleotide sequence and gene organization of the !1broad-host-range plasmid RSF1010. !$#cross-references MUID:89232758; PMID:2653965 !$#accession JH0130 !'##molecule_type DNA !'##residues 1-279 ##label SCH1 !'##cross-references GB:M28829; NID:g152577; PIDN:AAA26450.1; !1PID:g152586 !$#accession PS0293 !'##molecule_type protein !'##residues 2-54;274-279 ##label SCH2 !'##experimental_source plasmid RSF1010 !'##note plasmid RSF1010 is a naturally occurring broad-host-range !1plasmid belonging to the E. coli incompatibility group Q and !1encoding resistance to streptomycin and sulfonamides REFERENCE A25546 !$#authors Kim, K.; Meyer, R.J. !$#journal Nucleic Acids Res. (1986) 14:8027-8046 !$#title Copy-number of broad host-range plasmid R1162 is regulated !1by a small RNA. !$#cross-references MUID:87040771; PMID:2430262 !$#accession A25546 !'##molecule_type DNA !'##residues 1-93 ##label KIM !'##cross-references GB:X04499; NID:g45758; PIDN:CAA28184.1; PID:g45759 !'##experimental_source plasmid R1162 GENETICS !$#gene repI; repA !$#genome plasmid FUNCTION !$#description may possess three activities, an ATPase activity stimulated !1by single strand DNA, an ATP-dependent single strand !1DNA-binding activity and a helicase activity !$#note involved in regulating the plasmid copy-number CLASSIFICATION #superfamily regulatory protein RepI KEYWORDS plasmid copy control FEATURE !$2-279 #product regulatory protein RepI #status experimental !8#label REP SUMMARY #length 279 #molecular-weight 29909 #checksum 5145 SEQUENCE /// ENTRY BVECIB #type complete TITLE incB protein - phage P1 ORGANISM #formal_name phage P1 DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 16-Jul-1999 ACCESSIONS C23752 REFERENCE A92917 !$#authors Abeles, A.L.; Friedman, S.A.; Austin, S.J. !$#journal J. Mol. Biol. (1985) 185:261-272 !$#title Partition of unit-copy miniplasmids to daughter cells. III. !1The DNA sequence and functional organization of the P1 !1partition region. !$#cross-references MUID:86037206; PMID:3903163 !$#accession C23752 !'##molecule_type DNA !'##residues 1-208 ##label ABE !'##cross-references GB:K02380; GB:M24626; GB:X02954; NID:g215652; !1PIDN:AAA99232.1; PID:g215656 COMMENT This protein is thought to be cis acting and to contain the !1probable attachment site on the DNA for the cellular !1partition apparatus. GENETICS !$#gene incB !$#start_codon GTG CLASSIFICATION #superfamily incB protein SUMMARY #length 208 #molecular-weight 22671 #checksum 7595 SEQUENCE /// ENTRY BVECIC #type complete TITLE incC protein - plasmid RK2 ORGANISM #formal_name plasmid RK2 DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jul-1999 ACCESSIONS B24138; S02356 REFERENCE A93626 !$#authors Thomas, C.M.; Smith, C.A. !$#journal Nucleic Acids Res. (1986) 14:4453-4469 !$#title The trfB region of broad host range plasmid RK2: the !1nucleotide sequence reveals incC and key regulatory gene !1trfB/korA/korD as overlapping genes. !$#cross-references MUID:86232584; PMID:3520485 !$#accession B24138 !'##molecule_type DNA !'##residues 1-364 ##label THO !'##cross-references GB:X03962; GB:M24334; GB:X00082; NID:g45779; !1PIDN:CAA27595.1; PID:g45781 REFERENCE S02356 !$#authors Kornacki, J.A.; Balderes, P.J.; Figurski, D.H. !$#journal J. Mol. Biol. (1987) 198:211-222 !$#title Nucleotide sequence of korB, a replication control gene of !1broad host-range plasmid RK2. !$#cross-references MUID:88118923; PMID:3430606 !$#accession S02356 !'##molecule_type DNA !'##residues 342-364 ##label KOR !'##cross-references EMBL:X06543; NID:g43774; PIDN:CAA29789.1; !1PID:g43775 COMMENT This is one of the proteins encoded by the trfB operon; it !1is involved in plasmid maintenance and replication. GENETICS !$#gene incC !$#genome plasmid CLASSIFICATION #superfamily incC protein KEYWORDS plasmid maintenance; plasmid replication FEATURE !$1-364 #product incC large protein #status predicted #label !8NC1\ !$105-364 #product incC small protein #status predicted #label !8NC2 SUMMARY #length 364 #molecular-weight 38134 #checksum 7699 SEQUENCE /// ENTRY RGECKK #type complete TITLE transcription repressor korA - plasmid RK2 ORGANISM #formal_name plasmid RK2 DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 28-May-1999 ACCESSIONS A03588; A24138 REFERENCE A93493 !$#authors Bechhofer, D.H.; Figurski, D.H. !$#journal Nucleic Acids Res. (1983) 11:7453-7469 !$#title Map location and nucleotide sequence of korA, a key !1regulatory gene of promiscuous plasmid RK2. !$#cross-references MUID:84069779; PMID:6316262 !$#accession A03588 !'##molecule_type DNA !'##residues 1-101 ##label BEC !'##cross-references GB:X03962; GB:M24334; GB:X00082; NID:g45779; !1PIDN:CAA27596.1; PID:g45782 REFERENCE A93626 !$#authors Thomas, C.M.; Smith, C.A. !$#journal Nucleic Acids Res. (1986) 14:4453-4469 !$#title The trfB region of broad host range plasmid RK2: the !1nucleotide sequence reveals incC and key regulatory gene !1trfB/korA/korD as overlapping genes. !$#cross-references MUID:86232584; PMID:3520485 !$#accession A24138 !'##molecule_type DNA !'##residues 1-101 ##label THO !'##cross-references GB:X03962; GB:M24334; GB:X00082; NID:g45779; !1PIDN:CAA27596.1; PID:g45782 COMMENT This protein inhibits the activity of kilA, one of the !1plasmid kil genes that can be lethal to E. coli hosts. It !1represses the expression of the kor operon, which includes !1the incC gene, the korB gene, and its own gene. It is also a !1transcriptional repressor for trfA and kilB operons. GENETICS !$#gene korA (trfB) !$#map_position 55.1-55.6 !$#genome plasmid CLASSIFICATION #superfamily transcription repressor korA KEYWORDS DNA binding; transcription regulation SUMMARY #length 101 #molecular-weight 11306 #checksum 1603 SEQUENCE /// ENTRY RPECKB #type complete TITLE transcription repressor korB - plasmid RK2 ORGANISM #formal_name plasmid RK2 DATE 31-Mar-1988 #sequence_revision 03-Oct-1995 #text_change 16-Jul-1999 ACCESSIONS A26837; C24138; A39141; S02357 REFERENCE A26837 !$#authors Theophilus, B.D.M.; Thomas, C.M. !$#journal Nucleic Acids Res. (1987) 15:7443-7450 !$#title Nucleotide sequence of the transcriptional repressor gene !1korB which plays a key role in regulation of the copy number !1of broad host range plasmid RK2. !$#cross-references MUID:88015606; PMID:3309894 !$#accession A26837 !'##molecule_type DNA !'##residues 1-358 ##label THE !'##cross-references GB:Y00448; GB:M36479; GB:M38028; NID:g45773; !1PIDN:CAA68503.1; PID:g45774 REFERENCE A93626 !$#authors Thomas, C.M.; Smith, C.A. !$#journal Nucleic Acids Res. (1986) 14:4453-4469 !$#title The trfB region of broad host range plasmid RK2: the !1nucleotide sequence reveals incC and key regulatory gene !1trfB/korA/korD as overlapping genes. !$#cross-references MUID:86232584; PMID:3520485 !$#accession C24138 !'##molecule_type DNA !'##residues 1-114 ##label THO REFERENCE A39141 !$#authors Jagura-Burdzy, G.; Ibbotson, J.P.; Thomas, C.M. !$#journal J. Bacteriol. (1991) 173:826-833 !$#title The korF region of broad-host-range plasmid RK2 encodes two !1polypeptides with transcriptional repressor activity. !$#cross-references MUID:91100374; PMID:1987165 !$#accession A39141 !'##status preliminary !'##molecule_type DNA !'##residues 327-358 ##label JAG !'##cross-references GB:M36479 REFERENCE S02356 !$#authors Kornacki, J.A.; Balderes, P.J.; Figurski, D.H. !$#journal J. Mol. Biol. (1987) 198:211-222 !$#title Nucleotide sequence of korB, a replication control gene of !1broad host-range plasmid RK2. !$#cross-references MUID:88118923; PMID:3430606 !$#accession S02357 !'##molecule_type DNA !'##residues 1-358 ##label KOR !'##cross-references EMBL:X06543; NID:g43774; PIDN:CAA29790.1; !1PID:g43776 GENETICS !$#gene korB !$#genome plasmid FUNCTION !$#description a transcriptional repressor for trfA and kilB operons, which !1are involved in stable inheritance of the plasmid; probably !1also represses kilA gene CLASSIFICATION #superfamily transcription repressor korB KEYWORDS plasmid copy control; transcription regulation SUMMARY #length 358 #molecular-weight 39011 #checksum 1034 SEQUENCE /// ENTRY RPECTR #type complete TITLE conjugal transfer repressor finO - Escherichia coli plasmids ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 16-Jul-1999 ACCESSIONS A27757; S10663; JQ1342; S20552; S17347 REFERENCE A27757 !$#authors Yoshioka, Y.; Ohtsubo, H.; Ohtsubo, E. !$#journal J. Bacteriol. (1987) 169:619-623 !$#title Repressor gene finO in plasmids R100 and F: constitutive !1transfer of plasmid F is caused by insertion of IS3 into F !1finO. !$#cross-references MUID:87109048; PMID:3027040 !$#accession A27757 !'##molecule_type DNA !'##residues 1-186 ##label YOS1 !'##cross-references GB:M15196; NID:g151762; PIDN:AAA26061.1; !1PID:g151763 !'##experimental_source plasmid R-100 REFERENCE S10658 !$#authors Yoshioka, Y.; Fujita, Y.; Ohtsubo, E. !$#journal J. Mol. Biol. (1990) 214:39-53 !$#title Nucleotide sequence of the promoter-distal region of the tra !1operon of plasmid R100, including traI (DNA helicase I) and !1traD genes. !$#cross-references MUID:90317835; PMID:2164585 !$#accession S10663 !'##molecule_type DNA !'##residues 1-186 ##label YOS2 !'##cross-references EMBL:X55815; NID:g42620; PIDN:CAA39341.1; !1PID:g42627 !'##experimental_source plasmid R-100 REFERENCE JQ1338 !$#authors Cram, D.S.; Loh, S.M.; Cheah, K.C.; Skurray, R.A. !$#journal Gene (1991) 104:85-90 !$#title Sequence and conservation of genes at the distal end of the !1transfer region on plasmids F and R6-5. !$#cross-references MUID:92009201; PMID:1916281 !$#accession JQ1342 !'##molecule_type DNA !'##residues 1-71,'T',73-186 ##label CRA !'##cross-references GB:M38048; NID:g151835; PIDN:AAA98316.1; !1PID:g151838 !'##experimental_source plasmid R6-5 REFERENCE S20552 !$#authors van Biesen, T.; Frost, L.S. !$#journal Mol. Microbiol. (1992) 6:771-780 !$#title Differential levels of fertility inhibition among F-like !1plasmids are related to the cellular concentration of finO !1mRNA. !$#cross-references MUID:92244047; PMID:1374147 !$#accession S20552 !'##molecule_type DNA !'##residues 1-20,'V',22-53,'A',55-109,'HG',112-159,'A',161-185,'K' !1##label VAN !'##cross-references EMBL:X62481; NID:g42363; PIDN:CAA44348.1; !1PID:g42364 !'##experimental_source plasmid ColB2 COMMENT This protein is one of the components on the finOP fertility !1inhibition complex, which inhibits the expression of traJ !1gene, which in turn regulates the expression of some 20 !1transfer genes. The transfer genes are responsible for the !1process, called conjugal transfer, in which DNA is !1transmitted from one bacterial host to another. GENETICS !$#gene finO !$#genome plasmid CLASSIFICATION #superfamily conjugal transfer repressor finO KEYWORDS DNA binding; transcription regulation SUMMARY #length 186 #molecular-weight 21265 #checksum 4612 SEQUENCE /// ENTRY LFBSTT #type complete TITLE tet leader peptide - Bacillus subtilis ALTERNATE_NAMES tetracycline resistance leader peptide tetL ORGANISM #formal_name Bacillus subtilis DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jun-2000 ACCESSIONS S04802; S17282; H69721 REFERENCE JT0427 !$#authors Sakaguchi, R.; Amano, H.; Shishido, K. !$#journal Biochim. Biophys. Acta (1988) 950:441-444 !$#title Nucleotide sequence homology of the tetracycline-resistance !1determinant naturally maintained in Bacillus subtilis !1Marburg 168 chromosome and the tetracycline-resistance gene !1of B. subtilis plasmid pNS1981. !$#cross-references MUID:89000797; PMID:2844262 !$#accession S04802 !'##status translation not shown !'##molecule_type DNA !'##residues 1-20 ##label SAK !'##cross-references EMBL:X08034; NID:g40207; PIDN:CAA30826.1; !1PID:g40208 REFERENCE S17282 !$#authors Amano, H.; Sakaguchi, R.; Shishido, K. !$#journal FEMS Microbiol. Lett. (1991) 79:5-8 !$#title An insertion of Escherichia coli transposable element IS1K !1into the site immediately before tetracycline-resistance !1determinant of Bacillus subtilis chromosomal DNA fragment in !1cloning in E.coli. !$#accession S17282 !'##molecule_type DNA !'##residues 1-20 ##label AMA !'##cross-references EMBL:X58999; NID:g39964; PIDN:CAA41744.1; !1PID:g39965 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69721 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-20 ##label KUN !'##cross-references GB:Z99124; GB:AL009126; NID:g2636442; !1PIDN:CAB16115.1; PID:g2636625 !'##experimental_source strain 168 GENETICS !$#gene tetL CLASSIFICATION #superfamily tet leader peptide SUMMARY #length 20 #molecular-weight 2298 #checksum 6524 SEQUENCE /// ENTRY LFBSTU #type complete TITLE tet leader peptide - Bacillus cereus plasmid pBC16 ORGANISM #formal_name Bacillus cereus DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS S09233 REFERENCE S09233 !$#authors Palva, A.; Vidgren, G.; Simonen, M.; Rintala, H.; Laamanen, !1P. !$#journal Nucleic Acids Res. (1990) 18:1635 !$#title Nucleotide sequence of the tetracycline resistance gene of !1pBC16 from Bacillus cereus. !$#cross-references MUID:90221899; PMID:2109312 !$#accession S09233 !'##status translation not shown !'##molecule_type DNA !'##residues 1-20 ##label PAL !'##cross-references EMBL:X51366; NID:g39459; PIDN:CAA35750.1; !1PID:g39460 GENETICS !$#genome plasmid CLASSIFICATION #superfamily tet leader peptide SUMMARY #length 20 #molecular-weight 2253 #checksum 6416 SEQUENCE /// ENTRY LFECW #type complete TITLE trp operon leader peptide - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 18-Dec-1981 #sequence_revision 18-Dec-1981 #text_change 01-Mar-2002 ACCESSIONS A03589; S41637; D64874 REFERENCE A93746 !$#authors Yanofsky, C.; Platt, T.; Crawford, I.P.; Nichols, B.P.; !1Christie, G.E.; Horowitz, H.; van Cleemput, M.; Wu, A.M. !$#journal Nucleic Acids Res. (1981) 9:6647-6668 !$#title The complete nucleotide sequence of the tryptophan operon of !1Escherichia coli. !$#cross-references MUID:82150258; PMID:7038627 !$#accession A03589 !'##molecule_type DNA !'##residues 1-14 ##label YAN !'##cross-references GB:J01714; GB:M12471; GB:M12472; GB:M24865; !1GB:M25264; GB:M25593; GB:M59208; NID:g147953; !1PIDN:AAA57296.1; PID:g147954 REFERENCE S41637 !$#authors Ramesh, V. !$#journal Nucleic Acids Res. (1993) 21:5485-5488 !$#title NMR evidence for the RNA stem-loop structure involved in the !1transcription attenuation of E.coli trp operon. !$#cross-references MUID:94089403; PMID:7505428 !$#accession S41637 !'##molecule_type DNA !'##residues 1-14 ##label RAM REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64874 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-14 ##label BLAT !'##cross-references GB:AE000224; GB:U00096; NID:g1787509; !1PIDN:AAC74347.1; PID:g1787519; UWGP:b1265 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene trpL; trpEe !$#map_position 27 min FUNCTION !$#description involved in control of tryptophan operon transcription by !1attenuation CLASSIFICATION #superfamily trp leader peptide SUMMARY #length 14 #molecular-weight 1723 #checksum 8416 SEQUENCE /// ENTRY LFEBWC #type complete TITLE trp operon leader peptide - Citrobacter freundii ORGANISM #formal_name Citrobacter freundii DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 13-Nov-1998 ACCESSIONS A03592 REFERENCE A91792 !$#authors Blumenberg, M.; Yanofsky, C. !$#journal J. Bacteriol. (1982) 152:57-62 !$#title Evolutionary divergence of the Citrobacter freundii !1tryptophan operon regulatory region: comparison with other !1enteric bacteria. !$#cross-references MUID:83007061; PMID:6749821 !$#accession A03592 !'##molecule_type DNA !'##residues 1-14 ##label BLU GENETICS !$#gene trpL FUNCTION !$#description involved in control of tryptophan operon transcription by !1attenuation CLASSIFICATION #superfamily trp leader peptide SUMMARY #length 14 #molecular-weight 1720 #checksum 8436 SEQUENCE /// ENTRY LFEBWT #type complete TITLE trp operon leader peptide - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 02-Apr-1982 #sequence_revision 02-Apr-1982 #text_change 13-Nov-1998 ACCESSIONS A03590 REFERENCE A92850 !$#authors Lee, F.; Bertrand, K.; Bennett, G.; Yanofsky, C. !$#journal J. Mol. Biol. (1978) 121:193-217 !$#title Comparison of the nucleotide sequences of the initial !1transcribed regions of the tryptophan operons of Escherichia !1coli and Salmonella typhimurium. !$#cross-references MUID:78196931; PMID:351195 !$#accession A03590 !'##molecule_type DNA !'##residues 1-14 ##label LEE GENETICS !$#gene trpL; trpEe FUNCTION !$#description involved in control of tryptophan operon transcription by !1attenuation CLASSIFICATION #superfamily trp leader peptide SUMMARY #length 14 #molecular-weight 1635 #checksum 8290 SEQUENCE /// ENTRY LFSEW #type complete TITLE trp operon leader peptide - Serratia marcescens ORGANISM #formal_name Serratia marcescens DATE 18-Dec-1981 #sequence_revision 18-Dec-1981 #text_change 13-Nov-1998 ACCESSIONS A03591 REFERENCE A93202 !$#authors Miozzari, G.F.; Yanofsky, C. !$#journal Nature (1978) 276:684-689 !$#title The regulatory region of the trp operon of Serratia !1marcescens. !$#cross-references MUID:79093989; PMID:366432 !$#accession A03591 !'##molecule_type DNA !'##residues 1-28 ##label MIO GENETICS !$#gene trpL FUNCTION !$#description involved in control of tryptophan operon transcription by !1attenuation CLASSIFICATION #superfamily trp leader peptide SUMMARY #length 28 #molecular-weight 3391 #checksum 2187 SEQUENCE /// ENTRY LFTWWE #type complete TITLE probable trpEG leader peptide - Thermus aquaticus ORGANISM #formal_name Thermus aquaticus DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS S03315 REFERENCE S03315 !$#authors Sato, S.; Nakada, Y.; Kanaya, S.; Tanaka, T. !$#journal Biochim. Biophys. Acta (1988) 950:303-312 !$#title Molecular cloning and nucleotide sequence of Thermus !1thermophilus HB8 trpE and trpG. !$#cross-references MUID:89000781; PMID:2844259 !$#accession S03315 !'##molecule_type DNA !'##residues 1-11 ##label SAT !'##cross-references EMBL:X07744; NID:g48261; PIDN:CAA30565.1; !1PID:g48262 !'##note the source is designated as Thermus thermophilus HB8 GENETICS !$#gene trpL CLASSIFICATION #superfamily probable trpEG leader peptide SUMMARY #length 11 #molecular-weight 1228 #checksum 5152 SEQUENCE /// ENTRY LFECF #type complete TITLE phe operon leader peptide - Escherichia coli (strain K-12) ALTERNATE_NAMES attenuator peptide ORGANISM #formal_name Escherichia coli DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 01-Mar-2002 ACCESSIONS A03593; B36494; A65038 REFERENCE A03593 !$#authors Zurawski, G.; Brown, K.; Killingly, D.; Yanofsky, C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1978) 75:4271-4275 !$#title Nucleotide sequence of the leader region of the !1phenylalanine operon of Escherichia coli. !$#cross-references MUID:79033820; PMID:360214 !$#accession A03593 !'##molecule_type DNA !'##residues 1-15 ##label ZUR !'##cross-references GB:V00314; GB:J01658; NID:g42378; PIDN:CAA23600.1; !1PID:g42379 REFERENCE A36494 !$#authors Gavini, N.; Davidson, B.E. !$#journal J. Biol. Chem. (1990) 265:21532-21535 !$#title pheAo mutants of Escherichia coli have a defective pheA !1attenuator. !$#cross-references MUID:91072346; PMID:2254312 !$#accession B36494 !'##molecule_type DNA !'##residues 1-15 ##label GAV !'##cross-references GB:M58024; GB:J05694; NID:g147178; PIDN:AAA62783.1; !1PID:g147180 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65038 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-15 ##label BLAT !'##cross-references GB:AE000346; GB:U00096; NID:g2367141; !1PIDN:AAC75647.1; PID:g1788950; UWGP:b2598 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene pheL; pheAe !$#map_position 56 min CLASSIFICATION #superfamily pheA leader peptide SUMMARY #length 15 #molecular-weight 1924 #checksum 8772 SEQUENCE /// ENTRY LFECH #type complete TITLE his operon leader peptide - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 29-Jul-1981 #sequence_revision 29-Jul-1981 #text_change 01-Mar-2002 ACCESSIONS A03594; I41073; A64967 REFERENCE A03594 !$#authors Verde, P.; Frunzio, R.; di Nocera, P.P.; Blasi, F.; Bruni, !1C.B. !$#journal Nucleic Acids Res. (1981) 9:2075-2086 !$#title Identification, nucleotide sequence and expression of the !1regulatory region of the histidine operon of Escherichia !1coli K-12. !$#cross-references MUID:82059525; PMID:6170941 !$#accession A03594 !'##molecule_type DNA !'##residues 1-16 ##label VER !'##cross-references GB:V00284; GB:J01627; GB:J01628; NID:g41692; !1PIDN:CAA23548.1; PID:g581104 !'##note this protein is involved in the attenuation mechanism for the !1control of the expression of the his structural genes REFERENCE I41073 !$#authors Di Nocera, P.P.; Blasi, F.; Di Lauro, R.; Frunzio, R.; !1Bruni, C.B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1978) 75:4276-4280 !$#title Nucleotide sequence of the attenuator region of the !1histidine operon of Escherichia coli K-12. !$#cross-references MUID:79033821; PMID:360215 !$#accession I41073 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-16 ##label RES !'##cross-references EMBL:V00285; NID:g41701; PIDN:CAA23550.1; !1PID:g41702 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64967 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-16 ##label BLAT !'##cross-references GB:AE000293; GB:U00096; NID:g2367127; !1PIDN:AAC75079.1; PID:g1788329; UWGP:b2018 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene hisL CLASSIFICATION #superfamily his leader peptide KEYWORDS histidine biosynthesis SUMMARY #length 16 #molecular-weight 2081 #checksum 17 SEQUENCE /// ENTRY LFECT #type complete TITLE thr operon leader peptide - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 18-Dec-1981 #sequence_revision 18-Dec-1981 #text_change 01-Mar-2002 ACCESSIONS A03595; S56628; I55222; I56399; A64720 REFERENCE A03595 !$#authors Gardner, J.F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1979) 76:1706-1710 !$#title Regulation of the threonine operon: tandem threonine and !1isoleucine codons in the control region and translational !1control of transcription termination. !$#cross-references MUID:79201669; PMID:287010 !$#accession A03595 !'##molecule_type DNA !'##residues 1-21 ##label GAR !'##cross-references GB:J01706; GB:J01707; GB:J01708; GB:J01709; !1GB:V00360; GB:X00092; NID:g147977; PIDN:AAA83913.1; !1PID:g147978 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56628 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-21 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97300.1; !1PID:g537244 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE I55222 !$#authors Gardner, J.F. !$#journal J. Biol. Chem. (1982) 257:3896-3904 !$#title Initiation, pausing, and termination of transcription in the !1threonine operon regulatory region of Escherichia coli. !$#cross-references MUID:82142573; PMID:6277952 !$#accession I55222 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-21 ##label RES !'##cross-references EMBL:X68872; NID:g43073; PIDN:CAA48733.1; !1PID:g43074 REFERENCE I56399 !$#authors Lynn, S.P.; Bauer, C.E.; Chapman, K.A.; Gardner, J.F. !$#journal J. Mol. Biol. (1985) 183:529-541 !$#title Identification and characterization of mutants affecting !1transcription termination at the threonine operon !1attenuator. !$#cross-references MUID:85264808; PMID:2410621 !$#accession I56399 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-21 ##label RE2 !'##cross-references GB:M28570; NID:g290476; PIDN:AAA24672.1; !1PID:g290477 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64720 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-21 ##label BLAT !'##cross-references GB:AE000111; GB:U00096; NID:g1786181; !1PIDN:AAC73112.1; PID:g1786182; UWGP:b0001 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene thrL CLASSIFICATION #superfamily thr leader peptide SUMMARY #length 21 #molecular-weight 2138 #checksum 7721 SEQUENCE /// ENTRY LFECI #type complete TITLE ilvGMEDA operon leader peptide - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 18-Dec-1981 #sequence_revision 18-Dec-1981 #text_change 01-Mar-2002 ACCESSIONS A93841; B01112; S30664; A65180; A03596 REFERENCE A93841 !$#authors Nargang, F.E.; Subrahmanyam, C.S.; Umbarger, H.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1980) 77:1823-1827 !$#title Nucleotide sequence of ilvGEDA operon attenuator region of !1Escherichia coli. !$#cross-references MUID:80190138; PMID:6990415 !$#accession A93841 !'##molecule_type DNA !'##residues 1-32 ##label NAR !'##cross-references GB:V00289; NID:g41791; PIDN:CAA23555.1; PID:g41792 REFERENCE A01112 !$#authors Lawther, R.P.; Calhoun, D.H.; Adams, C.W.; Hauser, C.A.; !1Gray, J.; Hatfield, G.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:922-925 !$#title Molecular basis of valine resistance in Escherichia coli !1K-12. !$#cross-references MUID:81199435; PMID:7015336 !$#accession B01112 !'##molecule_type DNA !'##residues 1-32 ##label LAW !'##cross-references GB:V00290; NID:g41797; PIDN:CAA23557.1; PID:g41798 REFERENCE S30660 !$#authors Daniels, D.L.; Plunkett III, G.; Burland, V.; Blattner, F.R. !$#journal Science (1992) 257:771-778 !$#title Analysis of the Escherichia coli genome: DNA sequence of the !1region from 84.5 to 86.5 minutes. !$#cross-references MUID:92358234; PMID:1379743 !$#accession S30664 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-32 ##label DAN !'##cross-references EMBL:M87049; NID:g836656; PIDN:AAA67570.1; !1PID:g148174 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1992 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65180 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-32 ##label BLAT !'##cross-references GB:AE000453; GB:U00096; NID:g2367276; !1PIDN:AAC77487.1; PID:g1790202; UWGP:b3766 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ilvL CLASSIFICATION #superfamily ilvGEDA leader peptide SUMMARY #length 32 #molecular-weight 3231 #checksum 9640 SEQUENCE /// ENTRY LFEBIT #type complete TITLE ilvGEDA leader peptide - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS A04601; A03596 REFERENCE A04601 !$#authors Taillon, M.P.; Gotto, D.A.; Lawther, R.P. !$#journal Nucleic Acids Res. (1981) 9:3419-3432 !$#title The DNA sequence of the promoter-attenuator of the ilvGEDA !1operon of Salmonella typhimurium. !$#cross-references MUID:82014917; PMID:6269082 !$#accession A04601 !'##molecule_type DNA !'##residues 1-32 ##label TAI !'##cross-references GB:J01806; GB:M11654; NID:g154146; PIDN:AAA27152.1; !1PID:g154147 CLASSIFICATION #superfamily ilvGEDA leader peptide SUMMARY #length 32 #molecular-weight 3231 #checksum 9640 SEQUENCE /// ENTRY LFECIV #type complete TITLE ilvBN operon leader peptide - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 01-Mar-2002 ACCESSIONS A03597; A65169 REFERENCE A03597 !$#authors Friden, P.; Newman, T.; Freundlich, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:6156-6160 !$#title Nucleotide sequence of the ilvB promoter-regulatory region: !1a biosynthetic operon controlled by attenuation and cyclic !1AMP. !$#cross-references MUID:83065137; PMID:6292893 !$#accession A03597 !'##molecule_type DNA !'##residues 1-32 ##label FRI !'##cross-references GB:X02541; GB:J01633; GB:X01131; NID:g41783; !1PIDN:CAA26386.1; PID:g41784 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65169 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-32 ##label BLAT !'##cross-references GB:AE000445; GB:U00096; NID:g1790105; !1PIDN:AAC76695.1; PID:g1790106; UWGP:b3672 !'##experimental_source strain K-12, substrain MG1655 COMMENT This protein is involved in control of the biosynthesis of !1isoleucine, leucine, and valine. GENETICS !$#map_position 82 min CLASSIFICATION #superfamily ilvB leader peptide SUMMARY #length 32 #molecular-weight 3206 #checksum 1864 SEQUENCE /// ENTRY LFEBLT #type complete TITLE leu operon leader peptide - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 18-Dec-1981 #sequence_revision 18-Dec-1981 #text_change 17-Jul-1998 ACCESSIONS A03598 REFERENCE A03598 !$#authors Gemmill, R.M.; Wessler, S.R.; Keller, E.B.; Calvo, J.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1979) 76:4941-4945 !$#title leu operon of Salmonella typhimurium is controlled by an !1attenuation mechanism. !$#cross-references MUID:80056609; PMID:388423 !$#accession A03598 !'##molecule_type DNA !'##residues 1-28 ##label GEM !'##cross-references GB:J01807; NID:g154160 FUNCTION !$#description involved in control of leucine operon transcription by !1attenuation CLASSIFICATION #superfamily leu leader peptide SUMMARY #length 28 #molecular-weight 3103 #checksum 964 SEQUENCE /// ENTRY LFECL #type complete TITLE leu operon leader peptide - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 01-Mar-2002 ACCESSIONS A30376; C64729; I56372; Q00032 REFERENCE A30376 !$#authors Wessler, S.R.; Calvo, J.M. !$#journal J. Mol. Biol. (1981) 149:579-597 !$#title Control of leu operon expression in Escherichia coli by a !1transcription attenuation mechanism. !$#cross-references MUID:82078077; PMID:6171647 !$#accession A30376 !'##molecule_type DNA !'##residues 1-28 ##label WES !'##cross-references GB:J01642; NID:g146601; PIDN:AAA24065.1; !1PID:g146602 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64729 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-28 ##label BLAT !'##cross-references GB:AE000118; GB:U00096; NID:g1786262; !1PIDN:AAC73186.1; PID:g1786263; UWGP:b0075 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene leuL; leuLP !$#map_position 2 min FUNCTION !$#description involved in control of leucine operon transcription by !1attenuation CLASSIFICATION #superfamily leu leader peptide SUMMARY #length 28 #molecular-weight 3146 #checksum 1408 SEQUENCE /// ENTRY LFTWL #type complete TITLE leu leader peptide - Thermus aquaticus ORGANISM #formal_name Thermus aquaticus DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS S00901 REFERENCE S00901 !$#authors Croft, J.E.; Love, D.R.; Bergquist, P.L. !$#journal Mol. Gen. Genet. (1987) 210:490-497 !$#title Expression of leucine genes from an extremely thermophilic !1bacterium in Escherichia coli. !$#cross-references MUID:88121725; PMID:3323845 !$#accession S00901 !'##molecule_type DNA !'##residues 1-15 ##label CRO !'##cross-references EMBL:X06604; NID:g48244; PIDN:CAA29823.1; !1PID:g48245 !'##note the source is designated as Thermus thermophilus CLASSIFICATION #superfamily Thermus aquaticus leu leader peptide SUMMARY #length 15 #molecular-weight 1666 #checksum 9214 SEQUENCE /// ENTRY LPECBI #type complete TITLE pyrBI leader peptide - Escherichia coli (strain K-12) ALTERNATE_NAMES aspartate transcarbamoylase leader peptide ORGANISM #formal_name Escherichia coli DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 01-Mar-2002 ACCESSIONS A24926; A05109; A36599; S56472; A65237 REFERENCE A24926 !$#authors Roland, K.L.; Powell, F.E.; Turnbough Jr., C.L. !$#journal J. Bacteriol. (1985) 163:991-999 !$#title Role of translation and attenuation in the control of pyrBI !1operon expression in Escherichia coli K-12. !$#cross-references MUID:85289046; PMID:3928602 !$#accession A24926 !'##molecule_type DNA !'##residues 1-44 ##label ROL !'##cross-references GB:M10743; GB:M22060; NID:g147466; PIDN:AAA24478.1; !1PID:g147467 !'##experimental_source strain K12 REFERENCE A05109 !$#authors Turnbough Jr., C.L.; Hicks, K.L.; Donahue, J.P. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:368-372 !$#title Attenuation control of pyrBI operon expression in !1Escherichia coli K-12. !$#cross-references MUID:83169660; PMID:6300835 !$#accession A05109 !'##molecule_type DNA !'##residues 1-44 ##label TUR !'##experimental_source strain K12 REFERENCE A36599 !$#authors Donahue, J.P.; Turnbough Jr., C.L. !$#journal J. Biol. Chem. (1990) 265:19091-19099 !$#title Characterization of transcriptional initiation from !1promoters P-1 and P-2 of the pyrBI operon of Escherichia !1coli K12. !$#cross-references MUID:91035438; PMID:1699940 !$#accession A36599 !'##status preliminary !'##molecule_type DNA !'##residues 1-44 ##label DON !'##cross-references GB:J01670 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56472 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-44 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97143.1; !1PID:g537088 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65237 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-44 ##label BLAT !'##cross-references GB:AE000495; GB:U00096; NID:g2367361; !1PIDN:AAC77203.1; PID:g1790694; UWGP:b4246 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene pyrL; pyrBI !$#map_position 97 min CLASSIFICATION #superfamily pyrBI leader peptide SUMMARY #length 44 #molecular-weight 5098 #checksum 5100 SEQUENCE /// ENTRY LFEBYB #type complete TITLE pyrBI leader peptide - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS S00028 REFERENCE S00028 !$#authors Michaels, G.; Kelln, R.A.; Nargang, F.E. !$#journal Eur. J. Biochem. (1987) 166:55-61 !$#title Cloning, nucleotide sequence and expression of the pyrBI !1operon of Salmonella typhimurium LT2. !$#cross-references MUID:87246692; PMID:3036524 !$#accession S00028 !'##molecule_type DNA !'##residues 1-33 ##label MIC !'##cross-references GB:X05641; NID:g47861; PIDN:CAA29128.1; PID:g47862 CLASSIFICATION #superfamily pyrBI leader peptide SUMMARY #length 33 #molecular-weight 3797 #checksum 2940 SEQUENCE /// ENTRY LFECPE #type complete TITLE pyrE leader peptide - Escherichia coli ORGANISM #formal_name Escherichia coli DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 31-Mar-1993 ACCESSIONS A30400; A05110; Q00495 REFERENCE A30400 !$#authors Poulsen, P.; Bonekamp, F.; Jensen, K.F. !$#journal EMBO J. (1984) 3:1783-1790 !$#title Structure of the Escherichia coli pyrE operon and control of !1pyrE expression by a UTP modulated intercistronic !1attentuation. !$#cross-references MUID:85003588; PMID:6207018 !$#accession A30400 !'##molecule_type DNA !'##residues 1-12 ##label POU1 REFERENCE A05110 !$#authors Poulsen, P.; Jensen, K.F.; Valentin-Hansen, P.; Carlsson, !1P.; Lundberg, L.G. !$#journal Eur. J. Biochem. (1983) 135:223-229 !$#title Nucleotide sequence of the Escherichia coli pyrE gene and of !1the DNA in front of the protein-coding region. !$#cross-references MUID:83287414; PMID:6349999 !$#accession A05110 !'##molecule_type DNA !'##residues 1-12 ##label POU2 GENETICS !$#gene pyrE-LP !$#map_position 82 min CLASSIFICATION #superfamily pyrE leader peptide SUMMARY #length 12 #molecular-weight 1542 #checksum 6119 SEQUENCE /// ENTRY LFECFS #type complete TITLE pheST operon leader peptide - Escherichia coli (strain K-12) ALTERNATE_NAMES phenylalanyl-tRNA synthetase operon leader peptide ORGANISM #formal_name Escherichia coli DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 01-Mar-2002 ACCESSIONS S11551; I53984; C64930; S06908 REFERENCE A30391 !$#authors Fayat, G.; Mayaux, J.F.; Sacerdot, C.; Fromant, M.; !1Springer, M.; Grunberg-Manago, M.; Blanquet, S. !$#journal J. Mol. Biol. (1983) 171:239-261 !$#title Escherichia coli phenylalanyl-tRNA synthetase operon region. !1Evidence for an attenuation mechanism. Identification of the !1gene for the ribosomal protein L20. !$#cross-references MUID:84090239; PMID:6317865 !$#accession S11551 !'##molecule_type DNA !'##residues 1-14 ##label FAY !'##cross-references EMBL:V00291; NID:g43065; PIDN:CAA23563.1; !1PID:g43069 REFERENCE I53984 !$#authors Mayaux, J. !$#journal Gene (1984) 30:137-146 !$#title IS4 transposition in the attenuator region of the !1Escherichia coli pheS,T operon. !$#cross-references MUID:85077605; PMID:6096210 !$#accession I53984 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-14 ##label RES !'##cross-references GB:M13251; NID:g147182; PIDN:AAA24333.1; !1PID:g147185 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64930 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-14 ##label BLAT !'##cross-references GB:AE000266; GB:U00096; NID:g1787997; !1PIDN:AAC74785.1; PID:g1788008; UWGP:b1715 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene pheM !$#map_position 37 min FUNCTION !$#description probably involved in attenuation regulation of !1phenylalanyl-tRNA synthetase operon CLASSIFICATION #superfamily pheST leader peptide SUMMARY #length 14 #molecular-weight 1762 #checksum 8011 SEQUENCE /// ENTRY LFSAP9 #type complete TITLE ermC leader peptide - Staphylococcus aureus plasmids ORGANISM #formal_name Staphylococcus aureus DATE 29-Jul-1981 #sequence_revision 01-Sep-1981 #text_change 24-Sep-1999 ACCESSIONS B93717; B93866; A46568; S03586; A03599 REFERENCE A93717 !$#authors Gryczan, T.J.; Grandi, G.; Hahn, J.; Grandi, R.; Dubnau, D. !$#journal Nucleic Acids Res. (1980) 8:6081-6097 !$#title Conformational alteration of mRNA structure and the !1posttranscriptional regulation of erythro-mycin-induced drug !1resistance. !$#cross-references MUID:81124320; PMID:6162157 !$#accession B93717 !'##molecule_type DNA !'##residues 1-19 ##label GRY !'##cross-references GB:V01278; GB:J01755; GB:J01756; GB:J01757; !1GB:J01758; GB:V01279; GB:V01280; NID:g46555; !1PIDN:CAA24592.1; PID:g46559 REFERENCE A93866 !$#authors Horinouchi, S.; Weisblum, B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1980) 77:7079-7083 !$#title Posttranscriptional modification of mRNA conformation: !1mechanism that regulates erythromycin-induced resistance. !$#cross-references MUID:81175093; PMID:6938954 !$#accession B93866 !'##molecule_type DNA !'##residues 1-19 ##label HOR !'##cross-references GB:V01278; GB:J01755; GB:J01756; GB:J01757; !1GB:J01758; GB:V01279; GB:V01280; NID:g46555; !1PIDN:CAA24592.1; PID:g46559 !'##experimental_source plasmid pE194 !'##note this peptide is involved in the control mechanism of the !1synthesis of the erythromycin resistance protein REFERENCE A46568 !$#authors Catchpole, I.; Thomas, C.; Davies, A.; Dyke, K.G.H. !$#journal J. Gen. Microbiol. (1988) 134:697-709 !$#title The nucleotide sequence of Staphylococcus aureus plasmid !1pT48 conferring inducible !1macrolide-lincosamide-streptogramin B resistance and !1comparison with similar plasmids expressing constitutive !1resistance. !$#cross-references MUID:89036120; PMID:3141573 !$#accession A46568 !'##status preliminary !'##molecule_type DNA !'##residues 1-19 ##label CAT !'##cross-references GB:M19652; NID:g153070; PIDN:AAA20193.1; !1PID:g455359 !'##experimental_source plasmid pT48 REFERENCE S03586 !$#authors Mayford, M.; Weisblum, B. !$#journal J. Mol. Biol. (1989) 206:69-79 !$#title ermC leader peptide. Amino acid sequence critical for !1induction by translational attenuation. !$#cross-references MUID:89199652; PMID:2467989 !$#accession S03586 !'##molecule_type DNA !'##residues 1-19 ##label MAY GENETICS !$#genome plasmid CLASSIFICATION #superfamily ermC leader peptide SUMMARY #length 19 #molecular-weight 2210 #checksum 4970 SEQUENCE /// ENTRY LFSAME #type complete TITLE probable msrA leader peptide - Staphylococcus epidermidis ORGANISM #formal_name Staphylococcus epidermidis DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jul-1999 ACCESSIONS S11157 REFERENCE S11157 !$#authors Ross, J.I.; Eady, E.A.; Cove, J.H.; Cunliffe, W.J.; !1Baumberg, S.; Wootton, J.C. !$#journal Mol. Microbiol. (1990) 4:1207-1214 !$#title Inducible erythromycin resistance in staphylococci is !1encoded by a member of the ATP-binding transport super-gene !1family. !$#cross-references MUID:91041730; PMID:2233255 !$#accession S11157 !'##molecule_type DNA !'##residues 1-8 ##label ROS !'##cross-references EMBL:X52085; NID:g47000; PIDN:CAA36303.1; !1PID:g581653 CLASSIFICATION #superfamily probable msrA leader peptide SUMMARY #length 8 #molecular-weight 937 #checksum 2781 SEQUENCE /// ENTRY RQSACT #type complete TITLE repC protein - Staphylococcus aureus plasmids ORGANISM #formal_name Staphylococcus aureus DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 28-May-1999 ACCESSIONS A03600; S42236 REFERENCE A03600 !$#authors Novick, R.P.; Adler, G.K.; Majumder, S.; Khan, S.A.; !1Carleton, S.; Rosenblum, W.D.; Iordanescu, S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:4108-4112 !$#title Coding sequence for the pT181 repC product: a plasmid-coded !1protein uniquely required for replication. !$#cross-references MUID:82275073; PMID:6287465 !$#accession A03600 !'##molecule_type DNA !'##residues 1-314 ##label NOV !'##cross-references GB:J01764; GB:J01765; NID:g151679; PIDN:AAA26033.1; !1PID:g151680 !'##experimental_source plasmid pT181 !'##note this protein is specifically required and may be rate-limiting !1for replication of the plasmid in vivo REFERENCE S42236 !$#authors Noguchi, N.; Aoki, T.; Sasatsu, M.; Kono, M.; Shishido, K.; !1Ando, T. !$#journal FEMS Microbiol. Lett. (1986) 37:283-288 !$#title Determination of the complete nucleotide sequence of pNS1, a !1staphylococcal tetracycline-resistance plasmid propagated in !1Bacillus subtilis. !$#accession S42236 !'##status preliminary !'##molecule_type DNA !'##residues 269-314 ##label NOG !'##cross-references EMBL:M16217 !'##experimental_source plasmid pNS1 GENETICS !$#genome plasmid CLASSIFICATION #superfamily repC protein SUMMARY #length 314 #molecular-weight 37656 #checksum 2485 SEQUENCE /// ENTRY RQSAD2 #type complete TITLE repD protein - Staphylococcus aureus plasmid pC221 ORGANISM #formal_name Staphylococcus aureus DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 16-Jul-1999 ACCESSIONS A03601; S40419 REFERENCE A91033 !$#authors Brenner, D.G.; Shaw, W.V. !$#journal EMBO J. (1985) 4:561-568 !$#title The use of synthetic oligonucleotides with universal !1templates for rapid DNA sequencing: results with !1staphylococcal replicon pC21. !$#cross-references MUID:85257490; PMID:3860383 !$#accession A03601 !'##molecule_type DNA !'##residues 1-311 ##label BRE !'##cross-references GB:X02166; NID:g46545; PIDN:CAA26104.1; PID:g46547 REFERENCE S40418 !$#authors Projan, S.J.; Kornblum, J.; Moghazeh, S.L.; Edelman, I.; !1Gennaro, M.L.; Novick, R.P. !$#journal Mol. Gen. Genet. (1985) 199:452-464 !$#title Comparative sequence and functional analysis of pT181 and !1pC221, cognate plasmid replicons from Staphylococcus aureus. !$#cross-references MUID:85295465; PMID:2993795 !$#accession S40419 !'##status preliminary !'##molecule_type DNA !'##residues 1-311 ##label PRO !'##cross-references EMBL:X02529; NID:g46630; PIDN:CAA26366.1; !1PID:g46631 !'##note this sequence is homologous with that of repC protein, which is !1essential for replication of the staphylococcal plasmid !1pT181 GENETICS !$#gene repD !$#genome plasmid CLASSIFICATION #superfamily repC protein SUMMARY #length 311 #molecular-weight 37479 #checksum 6277 SEQUENCE /// ENTRY BVECRA #type complete TITLE repA protein - Escherichia coli plasmid mini-Rts-1 ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 28-May-1999 ACCESSIONS A23222 REFERENCE A23222 !$#authors Kamio, Y.; Tabuchi, A.; Itoh, Y.; Katagiri, H.; Terawaki, Y. !$#journal J. Bacteriol. (1984) 158:307-312 !$#title Complete nucleotide sequence of mini-Rts1 and its copy !1mutant. !$#cross-references MUID:84185439; PMID:6325393 !$#accession A23222 !'##molecule_type DNA !'##residues 1-288 ##label KAM !'##cross-references GB:K00053; NID:g152625; PIDN:AAA91589.1; !1PID:g455355 COMMENT This protein is essential for plasmid replication; it is !1involved in copy control functions. GENETICS !$#gene repA !$#genome plasmid CLASSIFICATION #superfamily repA protein KEYWORDS plasmid copy control; replication SUMMARY #length 288 #molecular-weight 32930 #checksum 1982 SEQUENCE /// ENTRY BVBPRA #type complete TITLE repA protein - phage P1 ALTERNATE_NAMES replication protein repA ORGANISM #formal_name phage P1 #note host Escherichia coli DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Feb-1997 ACCESSIONS A25329 REFERENCE A25329 !$#authors Abeles, A.L. !$#journal J. Biol. Chem. (1986) 261:3548-3555 !$#title P1 plasmid replication. Purification and DNA-binding !1activity of the replication protein RepA. !$#cross-references MUID:86140142; PMID:3949778 !$#accession A25329 !'##molecule_type DNA !'##residues 1-286 ##label ABE GENETICS !$#gene repA CLASSIFICATION #superfamily repA protein KEYWORDS DNA binding; DNA replication SUMMARY #length 286 #molecular-weight 32220 #checksum 7636 SEQUENCE /// ENTRY BVBPP7 #type complete TITLE repA protein - phage P7 ORGANISM #formal_name phage P7 DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS JC1326; S09597 REFERENCE JC1326 !$#authors Froehlich, B.J.; Scott, J.R. !$#journal Plasmid (1988) 19:121-133 !$#title A single amino acid difference between rep proteins of P1 !1and P7 affects plasmid copy number. !$#cross-references MUID:88336296; PMID:3047758 !$#accession JC1326 !'##molecule_type DNA !'##residues 1-286 ##label FRO !'##cross-references GB:J03308; NID:g215712; PIDN:AAA32438.1; !1PID:g215713 REFERENCE S06099 !$#authors Ludtke, D.N.; Eichorn, B.G.; Austin, S.J. !$#journal J. Mol. Biol. (1989) 209:393-406 !$#title Plasmid-partition functions of the P7 prophage. !$#cross-references MUID:90064501; PMID:2585492 !$#accession S09597 !'##molecule_type DNA !'##residues 239-286 ##label LUD !'##cross-references EMBL:X17529 GENETICS !$#gene repA CLASSIFICATION #superfamily repA protein KEYWORDS DNA replication SUMMARY #length 286 #molecular-weight 32234 #checksum 7552 SEQUENCE /// ENTRY IDECRP #type complete TITLE replication initiation protein - Escherichia coli plasmids ORGANISM #formal_name Escherichia coli DATE 18-Dec-1981 #sequence_revision 17-Dec-1982 #text_change 16-Jul-1999 ACCESSIONS A03602; B03602; S01773; S05591; A48662; C28378; I41109 REFERENCE A93119 !$#authors Rosen, J.; Ryder, T.; Inokuchi, H.; Ohtsubo, H.; Ohtsubo, E. !$#journal Mol. Gen. Genet. (1980) 179:527-537 !$#title Genes and sites involved in replication and incompatibility !1of an R100 plasmid derivative based on nucleotide sequence !1analysis. !$#cross-references MUID:81074309; PMID:7003300 !$#accession A03602 !'##molecule_type DNA !'##residues 1-285 ##label RO1 !'##cross-references GB:J01762; GB:J01761; GB:J01767; GB:J01768; !1NID:g151740; PIDN:AAA92257.1; PID:g294458 !'##experimental_source plasmid R100 REFERENCE A93253 !$#authors Rosen, J.; Ryder, T.; Ohtsubo, H.; Ohtsubo, E. !$#journal Nature (1981) 290:794-797 !$#title Role of RNA transcripts in replication incompatibility and !1copy number control in antibiotic resistance plasmid !1derivatives. !$#cross-references MUID:81173118; PMID:6163994 !$#accession B03602 !'##molecule_type DNA !'##residues 1-77 ##label ROS !'##experimental_source plamid R1 REFERENCE S01773 !$#authors Dong, X.; Womble, D.D.; Rownd, R.H. !$#journal J. Mol. Biol. (1988) 202:495-509 !$#title In-vivo studies on the cis-acting replication initiator !1protein of IncFII plasmid NR1. !$#cross-references MUID:89011975; PMID:3050127 !$#accession S01773 !'##molecule_type DNA !'##residues 1-285 ##label DON !'##cross-references EMBL:X12776; NID:g42707; PIDN:CAA31263.1; !1PID:g581213 !'##experimental_source plamid NR1 REFERENCE S05591 !$#authors Masai, H.; Arai, K.I. !$#journal Nucleic Acids Res. (1988) 16:6493-6514 !$#title RepA protein- and oriR-dependent initiation of R1 plasmid !1replication: identification of a rho-dependent transcription !1terminator required for cis-action of repA protein. !$#cross-references MUID:88289416; PMID:3041379 !$#accession S05591 !'##status translation not shown !'##molecule_type DNA !'##residues 270-285 ##label MAS !'##cross-references EMBL:X12587; NID:g41107; PIDN:CAA31100.1; !1PID:g41108 !'##experimental_source plamid R1 REFERENCE A48662 !$#authors Jiang, T.; Min, Y.N.; Liu, W.; Womble, D.D.; Rownd, R.H. !$#journal J. Bacteriol. (1993) 175:5350-5358 !$#title Insertion and deletion mutations in the repA4 region of the !1IncFII plasmid NR1 cause unstable inheritance. !$#cross-references MUID:93374828; PMID:8396115 !$#accession A48662 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 252-285 ##label JIA !'##experimental_source plamid NR1 REFERENCE A28378 !$#authors Dong, X.; Womble, D.D.; Rownd, R.H. !$#journal J. Bacteriol. (1987) 169:5353-5363 !$#title Transcriptional pausing in a region important for plasmid !1NR1 replication control. !$#cross-references MUID:88058738; PMID:2445727 !$#accession C28378 !'##status preliminary !'##molecule_type DNA !'##residues 1-50 ##label DO2 REFERENCE I41106 !$#authors Womble, D.D.; Sampathkumar, P.; Easton, A.M.; Luckow, V.A.; !1Rownd, R.H. !$#journal J. Mol. Biol. (1985) 181:395-410 !$#title Transcription of the replication control region of the !1IncFII R-plasmid NR1 in vitro and in vivo. !$#cross-references MUID:85160860; PMID:2580099 !$#accession I41109 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-285 ##label RES !'##cross-references EMBL:X02302; NID:g42132; PIDN:CAA26168.1; !1PID:g581144 GENETICS !$#gene repA1 !$#genome plasmid !$#start_codon GTG CLASSIFICATION #superfamily rep1 protein KEYWORDS plasmid copy control SUMMARY #length 285 #molecular-weight 32755 #checksum 5375 SEQUENCE /// ENTRY XMECR1 #type fragment TITLE rep1 protein - Escherichia coli plasmid ColV2-K94 (fragment) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 30-Sep-1993 ACCESSIONS A29845 REFERENCE A29845 !$#authors Weber, P.C.; Palchaudhuri, S. !$#journal J. Bacteriol. (1986) 166:1106-1112 !$#title Incompatibility repressor in a repA-like replicon of the !1IncFI plasmid ColV2-K94. !$#cross-references MUID:86223772; PMID:2423502 !$#accession A29845 !'##molecule_type DNA !'##residues 1-77 ##label WEB COMMENT This protein, essential for plasmid replication, is involved !1in copy control functions. It is a replication protein that !1is compatible with the repA replicon for the IncFII R !1plasmids. GENETICS !$#gene rep1 !$#genome plasmid !$#start_codon GTG CLASSIFICATION #superfamily rep1 protein KEYWORDS plasmid copy control; plasmid replication SUMMARY #length 77 #checksum 9904 SEQUENCE /// ENTRY MIEC77 #type complete TITLE microcin B17 precursor - Escherichia coli plasmid pMccB17 ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 01-Dec-1995 #text_change 16-Jul-1999 ACCESSIONS A25219; A32058; I41099; A58368; S67977 REFERENCE A25219 !$#authors Davagnino, J.; Herrero, M.; Furlong, D.; Moreno, F.; Kolter, !1R. !$#journal Proteins (1986) 1:230-238 !$#title The DNA replication inhibitor microcin B17 is a !1forty-three-amino-acid protein containing sixty percent !1glycine. !$#cross-references MUID:88217867; PMID:3329729 !$#accession A25219 !'##molecule_type DNA !'##residues 1-69 ##label DAV !'##cross-references GB:M15469; NID:g146787; PIDN:AAA24141.1; !1PID:g146788 REFERENCE A32058 !$#authors Genilloud, O.; Moreno, F.; Kolter, R. !$#journal J. Bacteriol. (1989) 171:1126-1135 !$#title DNA sequence, products, and transcriptional pattern of the !1genes involved in production of the DNA replication !1inhibitor microcin B17. !$#cross-references MUID:89123111; PMID:2644225 !$#accession A32058 !'##molecule_type DNA !'##residues 1-69 ##label GEN !'##cross-references GB:M24253; NID:g341145; PIDN:AAA72741.1; !1PID:g522290 REFERENCE I41099 !$#authors Connell, N.; Han, Z.; Moreno, F.; Kolter, R. !$#journal Mol. Microbiol. (1987) 1:195-201 !$#title An E. coli promoter induced by the cessation of growth. !$#cross-references MUID:88216163; PMID:2835580 !$#accession I41099 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-14 ##label CON !'##cross-references EMBL:X06417; NID:g41978; PIDN:CAA29725.1; !1PID:g41979 REFERENCE A58368 !$#authors Li, Y.M.; Milne, J.C.; Madison, L.L.; Kolter, R.; Walsh, !1C.T. !$#journal Science (1996) 274:1188-1193 !$#title From peptide precursors to oxazole and thiazole-containing !1peptide antibiotics: microcin B17 synthase. !$#cross-references MUID:97053605; PMID:8895467 !$#accession A58368 !'##molecule_type protein !'##residues 27-38 ##label LIY !'##experimental_source Escherichia coli strain ZK4(pY113) !'##note mass spectroscopy of peptides and biosynthetic intermediates REFERENCE A58375 !$#authors Yorgey, P.; Lee, J.; Koerdel, J.; Vivas, E.; Warner, P.; !1Jebaratnam, D.; Kolter, R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1994) 91:4519-4523 !$#title Posttranslational modifications in microcin B17 define an !1additional class of DNA gyrase inhibitor. !$#cross-references MUID:94240167; PMID:8183941 !$#contents annotation; (1)H-NMR spectroscopy of modified peptides REFERENCE S67977 !$#authors Bayer, A.; Freund, S.; Jung, G. !$#journal Eur. J. Biochem. (1995) 234:414-426 !$#title Post-translational heterocyclic backbone modifications in !1the 43-peptide antibiotic microcin B17. Structure !1elucidation and NMR study of a (13)C, (15)N-labelled gyrase !1inhibitor. !$#cross-references MUID:96128168; PMID:8536683 !$#accession S67977 !'##status preliminary !'##molecule_type protein !'##residues 27-38 ##label BAY GENETICS !$#gene mcbA !$#genome plasmid pMccB17 FUNCTION !$#description inhibits DNA gyrase, stopping DNA replication !$#note active against a large number of gram-negative enteric !1bacteria CLASSIFICATION #superfamily microcin KEYWORDS antibiotic; DNA replication inhibitor; oxazole/thiazole ring FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-69 #product microcin B17 #status experimental #label !8MAT\ !$39-40 #cross-link oxazole (Gly-Ser) #status experimental\ !$40-41 #cross-link thiazole (Ser-Cys) #status experimental\ !$47-48 #cross-link thiazole (Gly-Cys) #status experimental\ !$50-51 #cross-link thiazole (Gly-Cys) #status experimental\ !$54-55 #cross-link thiazole (Gly-Cys) #status experimental\ !$55-56 #cross-link oxazole (Cys-Ser) #status experimental\ !$61-62 #cross-link oxazole (Gly-Ser) #status experimental\ !$64-65 #cross-link oxazole (Gly-Ser) #status experimental SUMMARY #length 69 #molecular-weight 6013 #checksum 7709 SEQUENCE /// ENTRY BVECTH #type complete TITLE traH protein precursor - Escherichia coli plasmid F ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 17-Sep-1997 #text_change 16-Jul-1999 ACCESSIONS S20479; JS0123 REFERENCE S20479 !$#authors Firth, N.; Skurray, R. !$#journal Mol. Gen. Genet. (1992) 232:145-153 !$#title Characterization of the F plasmid bifunctional conjugation !1gene, traG. !$#cross-references MUID:92204127; PMID:1348105 !$#accession S20479 !'##molecule_type DNA !'##residues 1-458 ##label FIR !'##cross-references EMBL:M59763; NID:g148630; PIDN:AAA98080.1; !1PID:g148632 !'##note only a part of the nucleic acid sequence is shown, only a part !1of the translation is shown !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1991 REFERENCE A91600 !$#authors Ham, L.M.; Firth, N.; Skurray, R. !$#journal Gene (1989) 75:157-165 !$#title Nucleotide sequence of the F plasmid transfer gene, traH: !1identification of a new gene and a promoter within the !1transfer operon. !$#cross-references MUID:89252912; PMID:2656408 !$#accession JS0123 !'##molecule_type DNA !'##residues 1-253,'S',255-264,'S',266-268,'F',270-320,'R',322-337,'N', !1339-348,'LTRRCS',355,'FPAV' ##label HAM !'##cross-references GB:M24492; NID:g341175; PIDN:AAA98094.1; !1PID:g790750 !'##experimental_source strain K12 COMMENT This protein is involved in the assembly process of the !1F-pilus from its pilin subunits. COMMENT This protein is located in the periplasm and is closely !1associated with some inner membrane proteins. GENETICS !$#gene traH !$#genome plasmid F CLASSIFICATION #superfamily traH protein KEYWORDS F pilin formation FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-458 #product traH protein #status predicted #label MAT SUMMARY #length 458 #molecular-weight 50244 #checksum 251 SEQUENCE /// ENTRY BVECTL #type complete TITLE traL protein - Escherichia coli plasmid R1-19 ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 01-Mar-1996 #text_change 16-Jul-1999 ACCESSIONS S03311; B29332 REFERENCE S03309 !$#authors Koraimann, G.; Hoegenauer, G. !$#journal Nucleic Acids Res. (1989) 17:1283-1298 !$#title A stable core region of the tra operon mRNA of plasmid !1R1-19. !$#cross-references MUID:89160296; PMID:2564189 !$#accession S03311 !'##molecule_type DNA !'##residues 1-92 ##label KOR !'##cross-references EMBL:X13681; NID:g43119; PIDN:CAA31974.1; !1PID:g43123 REFERENCE A91799 !$#authors Frost, L.S.; Paranchych, W.; Willetts, N.S. !$#journal J. Bacteriol. (1984) 160:395-401 !$#title DNA sequence of the F traALE region that includes the gene !1for F pilin. !$#cross-references MUID:85006817; PMID:6090426 !$#accession B29332 !'##molecule_type DNA !'##residues 2-92 ##label FRO !'##cross-references GB:K01147; NID:g148640; PIDN:AAA24911.1; !1PID:g148645 GENETICS !$#gene traL !$#genome plasmid FUNCTION !$#description one of the proteins encoded by genes of the F transfer !1operon; it is a membrane protein involved in F pilin !1formation CLASSIFICATION #superfamily traL protein KEYWORDS F pilin formation; membrane protein SUMMARY #length 92 #molecular-weight 10510 #checksum 3502 SEQUENCE /// ENTRY C25161 #type complete TITLE traL protein - Salmonella typhimurium plasmid pED208 ORGANISM #formal_name Salmonella typhimurium DATE 16-Aug-1988 #sequence_revision 16-Aug-1988 #text_change 28-May-1999 ACCESSIONS C25161 REFERENCE A91828 !$#authors Finlay, B.B.; Frost, L.S.; Paranchych, W. !$#journal J. Bacteriol. (1986) 168:990-998 !$#title Nucleotide sequence of the traYALE region from IncFV plasmid !1pED208. !$#cross-references MUID:87056998; PMID:2877970 !$#accession C25161 !'##molecule_type DNA !'##residues 1-101 ##label FIN !'##cross-references GB:M14733; NID:g150662; PIDN:AAA25608.1; !1PID:g150665 GENETICS !$#gene traL !$#genome plasmid CLASSIFICATION #superfamily traL protein KEYWORDS membrane protein SUMMARY #length 101 #molecular-weight 12037 #checksum 4128 SEQUENCE /// ENTRY JCECMR #type complete TITLE traM protein - Escherichia coli plasmids ORGANISM #formal_name Escherichia coli DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 28-May-1999 ACCESSIONS A23956; A24544 REFERENCE A23956 !$#authors Koronakis, V.E.; Bauer, E.; Hogenauer, G. !$#journal Gene (1985) 36:79-86 !$#title The traM gene of the resistance plasmid R1: comparison with !1the corresponding sequence of the Escherichia coli F factor. !$#cross-references MUID:86056962; PMID:2998939 !$#accession A23956 !'##molecule_type DNA !'##residues 1-127 ##label KOR !'##note this sequence is from traM gene of plasmid R1 REFERENCE A24544 !$#authors Finlay, B.B.; Frost, L.S.; Paranchych, W. !$#journal J. Bacteriol. (1986) 166:368-374 !$#title Nucleotide sequences of the R1-19 plasmid transfer genes !1traM, finP, traJ, and traY and the traYZ promoter. !$#cross-references MUID:86195818; PMID:3009392 !$#accession A24544 !'##molecule_type DNA !'##residues 1-127 ##label FIN !'##cross-references GB:M19710; GB:M13168; NID:g150857; PIDN:AAA92656.1; !1PID:g150859 !'##note this sequence is from traM gene of plasmid R1-19 COMMENT This transfer gene protein is involved in the conjugation !1process of bacterial cells for the exchange of plasmid DNA. GENETICS !$#gene traM !$#genome plasmid CLASSIFICATION #superfamily traM protein KEYWORDS DNA binding; plasmid gene transfer SUMMARY #length 127 #molecular-weight 14446 #checksum 133 SEQUENCE /// ENTRY JCECMF #type complete TITLE traM protein - Escherichia coli plasmid F ORGANISM #formal_name Escherichia coli DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS A29331; JC6018 REFERENCE A29331 !$#authors Thompson, R.; Taylor, L. !$#journal Mol. Gen. Genet. (1982) 188:513-518 !$#title Promoter mapping and DNA sequencing of the F plasmid !1transfer genes traM and traJ. !$#cross-references MUID:83141056; PMID:6298579 !$#accession A29331 !'##molecule_type DNA !'##residues 1-127 ##label THO !'##cross-references GB:K01147; NID:g148640; PIDN:AAA24907.1; !1PID:g148641 REFERENCE JC6018 !$#authors Penfold, S.S.; Simon, J.; Frost, L.S. !$#journal Mol. Microbiol. (1996) 20:549-558 !$#title Regulation of the expression of the traM gene of the F sex !1factor of Escherichia coli. !$#cross-references MUID:96347127; PMID:8736534 !$#accession JC6018 !'##status preliminary !'##molecule_type DNA !'##residues 1-127 ##label PEN !'##cross-references GB:U11059 GENETICS !$#gene traM !$#genome plasmid FUNCTION !$#description this transfer gene protein is involved in the conjugation !1process of bacterial cells for the exchange of plasmid DNA CLASSIFICATION #superfamily traM protein KEYWORDS DNA binding; plasmid gene transfer SUMMARY #length 127 #molecular-weight 14507 #checksum 7868 SEQUENCE /// ENTRY JCECMK #type complete TITLE traM protein - Escherichia coli plasmid ColB4-K98 ORGANISM #formal_name Escherichia coli DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 28-May-1999 ACCESSIONS A25033 REFERENCE A25033 !$#authors Finlay, B.B.; Frost, L.S.; Paranchych, W. !$#journal J. Bacteriol. (1986) 168:132-139 !$#title Origin of transfer of Incf plasmids and nucleotide sequences !1of the type II oriT, traM, and traY alleles from ColB4-K98 !1and the type IV traY allele from R100-1. !$#cross-references MUID:87008371; PMID:3531163 !$#accession A25033 !'##molecule_type DNA !'##residues 1-127 ##label FIN !'##cross-references GB:M15134; NID:g144174; PIDN:AAB04664.1; !1PID:g144177 COMMENT This transfer gene protein is involved in the conjugation !1process of bacterial cells for the exchange of plasmid DNA. GENETICS !$#gene traM !$#genome plasmid CLASSIFICATION #superfamily traM protein KEYWORDS DNA binding; plasmid gene transfer SUMMARY #length 127 #molecular-weight 14542 #checksum 9263 SEQUENCE /// ENTRY BVECTE #type complete TITLE traE protein - Escherichia coli plasmid F ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jul-1999 ACCESSIONS C29332 REFERENCE A91799 !$#authors Frost, L.S.; Paranchych, W.; Willetts, N.S. !$#journal J. Bacteriol. (1984) 160:395-401 !$#title DNA sequence of the F traALE region that includes the gene !1for F pilin. !$#cross-references MUID:85006817; PMID:6090426 !$#accession C29332 !'##molecule_type DNA !'##residues 1-188 ##label FRO !'##cross-references GB:K01147; NID:g148640; PIDN:AAA24912.1; !1PID:g148646 GENETICS !$#gene traE !$#genome plasmid CLASSIFICATION #superfamily traE protein KEYWORDS F pilin formation; membrane protein SUMMARY #length 188 #molecular-weight 21220 #checksum 2981 SEQUENCE /// ENTRY BVECMA #type complete TITLE stable plasmid inheritance protein (F leading maintenance protein) - Escherichia coli plasmid pO157 ALTERNATE_NAMES flmA protein ORGANISM #formal_name Escherichia coli DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 18-Aug-2000 ACCESSIONS JS0432; S08305; T00291; T42190 REFERENCE JS0432 !$#authors Loh, S.M.; Cram, D.S.; Skurray, R.A. !$#journal Gene (1988) 66:259-268 !$#title Nucleotide sequence and transcriptional analysis of a third !1function (Flm) involved in F-plasmid maintenance. !$#cross-references MUID:89006267; PMID:3049248 !$#accession JS0432 !'##molecule_type DNA !'##residues 1-52 ##label LOH !'##cross-references GB:M97768; GB:M21120; GB:X17189; NID:g5702165; !1PIDN:AAA99216.1; PID:g148608 REFERENCE S08305 !$#authors Golub, E.I.; Panzer, H.A. !$#journal Mol. Gen. Genet. (1988) 214:353-357 !$#title The F factor of Escherichia coli carries a locus of stable !1plasmid inheritance stm, similar to the parB locus of !1plasmid RI. !$#cross-references MUID:89181537; PMID:3070354 !$#accession S08305 !'##molecule_type DNA !'##residues 1-44,'GYREVAA',45-52 ##label GOL !'##cross-references EMBL:X13521; NID:g42374; PIDN:CAA31872.1; !1PID:g42375 REFERENCE Z14127 !$#authors Makino, K.; Ishii, K.; Yasunaga, T.; Hattori, M.; Yokoyama, !1K.; Yatsudo, H.C.; Kubota, Y.; Yamaichi, Y.; Iida, T.; !1Yamamoto, K.; Honda, T.; Han, C.; Ohtsubo, A.; Kasamatsu, !1M.; Hayashi, T.; Kuhara, S.; Shinagawa, H. !$#journal DNA Res. (1998) 5:1-9 !$#title Complete nucleotide sequences of 93-kb and 3.3-kb plasmids !1of an enterohemorrhagic Escherichia coli O157:H7 derived !1from Sakai outbreak. !$#cross-references MUID:98290540; PMID:9628576 !$#accession T00291 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-52 ##label MAK !'##cross-references EMBL:AB011549; NID:g4589740; PIDN:BAA31810.1; !1PID:g3337051 !'##experimental_source strain EHEC O157:H7, substrain RIMD 0509952 REFERENCE Z22068 !$#authors Burland, V.; Shao, Y.; Perna, N.T.; Plunkett, G.; Sofia, !1H.J.; Blattner, F.R. !$#journal Nucleic Acids Res. (1998) 26:4196-4204 !$#title The complete DNA sequence and analysis of the large !1virulence plasmid of Escherichia coli O157:H7. !$#cross-references MUID:98391744; PMID:9722640 !$#accession T42190 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-52 ##label BUR !'##cross-references EMBL:AF074613; NID:g3822114; PIDN:AAC70158.1; !1PID:g3822204 !'##experimental_source strain EDL933; serotype O157:H7; plasmid pO157 GENETICS !$#gene flmA; stm; parB !$#map_position 62.8-64.2 min !$#genome plasmid CLASSIFICATION #superfamily flmA protein SUMMARY #length 52 #molecular-weight 6108 #checksum 5332 SEQUENCE /// ENTRY QQECR5 #type complete TITLE relF protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 23-Jan-1998 #text_change 01-Mar-2002 ACCESSIONS E64911; C22830 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64911 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-51 ##label BLAT !'##cross-references GB:AE000253; GB:U00096; NID:g1787841; !1PIDN:AAC74635.1; PID:g1787845; UWGP:b1562 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A22830 !$#authors Bech, F.W.; Jorgensen, S.T.; Diderichsen, B.; Karlstrom, !1O.H. !$#journal EMBO J. (1985) 4:1059-1066 !$#title Sequence of the relB transcription unit from Escherichia !1coli and identification of the relB gene. !$#cross-references MUID:85257499; PMID:2990907 !$#accession C22830 !'##molecule_type DNA !'##residues 1-36,'D',38-51 ##label BEC !'##cross-references GB:X02405; NID:g42699; PIDN:CAA26252.1; PID:g42702 GENETICS !$#gene relF !$#map_position 34 min FUNCTION !$#description overexpression of relF is toxic to Escherichia coli cells CLASSIFICATION #superfamily flmA protein SUMMARY #length 51 #molecular-weight 5737 #checksum 1452 SEQUENCE /// ENTRY C26870 #type complete TITLE srnB protein - Escherichia coli plasmids ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 24-Sep-1999 ACCESSIONS C26870; S08380; S06978 REFERENCE A91829 !$#authors Saadi, S.; Maas, W.K.; Hill, D.F.; Bergquist, P.L. !$#journal J. Bacteriol. (1987) 169:1836-1846 !$#title Nucleotide sequence analysis of RepFIC, a basic replicon !1present in IncFI plasmids P307 and F, and its relation to !1the RepA replicon of IncFII plasmids. !$#cross-references MUID:87194554; PMID:3032897 !$#accession C26870 !'##molecule_type DNA !'##residues 1-68 ##label SAA !'##cross-references GB:M16168; NID:g148597; PIDN:AAA99006.1; !1PID:g148600 !'##experimental_source plasmid P307 REFERENCE S08380 !$#authors Akimoto, S.; Ono, K.; Ono, T.; Ohnishi, Y. !$#journal FEMS Microbiol. Lett. (1986) 33:241-245 !$#title Nucleotide sequence of the F plasmid gene srnB that promotes !1degradation of stable RNA in Escherichia coli. !$#accession S08380 !'##molecule_type DNA !'##residues 1-68 ##label AKI !'##cross-references EMBL:X14442; NID:g45517; PIDN:CAA32614.1; !1PID:g45518 !'##experimental_source plasmid F GENETICS !$#gene srnB !$#genome plasmid CLASSIFICATION #superfamily flmA protein SUMMARY #length 68 #molecular-weight 7792 #checksum 126 SEQUENCE /// ENTRY S02763 #type complete TITLE pnd protein - Escherichia coli plasmid R16 ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S02763 REFERENCE S02763 !$#authors Sakikawa, T.; Akimoto, S.; Ohnishi, Y. !$#journal Biochim. Biophys. Acta (1989) 1007:158-166 !$#title The pnd gene in E. coli plasmid R16: nucleotide sequence and !1gene expression leading to cell Mg release and stable RNA !1degradation. !$#cross-references MUID:89150247; PMID:2465777 !$#accession S02763 !'##molecule_type DNA !'##residues 1-50 ##label SAK !'##cross-references EMBL:X12833; NID:g42453; PIDN:CAA31320.1; !1PID:g42454 GENETICS !$#gene pnd !$#genome plasmid CLASSIFICATION #superfamily flmA protein SUMMARY #length 50 #molecular-weight 5796 #checksum 8660 SEQUENCE /// ENTRY QUECTF #type complete TITLE transfer protein traF precursor - Escherichia coli plasmid F ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jul-1999 ACCESSIONS A31099; S23993; S17097 REFERENCE A31099 !$#authors Wu, J.H.; Kathir, P.; Ippen-Ihler, K. !$#journal J. Bacteriol. (1988) 170:3633-3639 !$#title The product of the F plasmid transfer operon gene, traF, is !1a periplasmic protein. !$#cross-references MUID:88298674; PMID:3042757 !$#accession A31099 !'##molecule_type DNA !'##residues 1-257 ##label WU1 REFERENCE S23990 !$#authors Maneewannakul, S.; Kathir, P.; Ippen-Ihler, K. !$#journal J. Mol. Biol. (1992) 225:299-311 !$#title Characterization of the F plasmid mating aggregation gene !1traN and of a new F transfer region locus trbE. !$#cross-references MUID:92277643; PMID:1593622 !$#accession S23993 !'##molecule_type DNA !'##residues 11-32 ##label MAN !'##cross-references EMBL:X61575; NID:g43125; PIDN:CAA43777.1; !1PID:g43129 COMMENT It is uncertain whether Met-1 or Met-11 is the initiator. GENETICS !$#gene traF !$#genome plasmid CLASSIFICATION #superfamily transfer protein traF KEYWORDS F pilin formation; periplasmic space; plasmid transfer FEATURE !$1-29 #domain signal sequence #status predicted #label SIG\ !$30-257 #product transfer protein traF #status predicted !8#label MAT SUMMARY #length 257 #molecular-weight 29164 #checksum 5732 SEQUENCE /// ENTRY BVECFQ #type complete TITLE finQ protein - Escherichia coli plasmid R820a ORGANISM #formal_name Escherichia coli DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jun-2000 ACCESSIONS JE0060 REFERENCE JE0060 !$#authors Ham, L.M.; Skurray, R. !$#journal Mol. Gen. Genet. (1989) 216:99-105 !$#title Molecular analysis and nucleotide sequence of finQ, a !1transcriptional inhibitor of the F plasmid transfer genes. !$#cross-references MUID:89281496; PMID:2543909 !$#accession JE0060 !'##molecule_type DNA !'##residues 1-342 ##label HAM !'##cross-references GB:X52664; NID:g41467; PIDN:CAA36892.1; !1PID:g1405551 COMMENT This is a transcriptional inhibitor of the F plasmid !1transfer gene. GENETICS !$#gene finQ !$#genome plasmid CLASSIFICATION #superfamily finQ protein KEYWORDS DNA binding; transcription regulation SUMMARY #length 342 #molecular-weight 39941 #checksum 1585 SEQUENCE /// ENTRY BVECAQ #type complete TITLE traQ protein - Escherichia coli plasmid F ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 28-May-1999 ACCESSIONS D32238 REFERENCE A32238 !$#authors Wu, J.H.; Ippen-Ihler, K. !$#journal J. Bacteriol. (1989) 171:213-221 !$#title Nucleotide sequence of traQ and adjacent loci in the !1Escherichia coli K-12 F-plasmid transfer operon. !$#cross-references MUID:89123020; PMID:2536655 !$#accession D32238 !'##molecule_type DNA !'##residues 1-94 ##label WU1 !'##cross-references GB:M20787; NID:g148622; PIDN:AAC63070.1; !1PID:g3712665 !'##experimental_source strain K12 COMMENT This membrane-associated protein is required for efficient !1expression of the 70-residue pilin peptide. The !1carboxyl-terminal one-third of the protein is very !1hydrophilic, and it is this region that interacts with the !1pilin precursor. GENETICS !$#gene traQ !$#genome plasmid CLASSIFICATION #superfamily traQ protein KEYWORDS F pilin formation; membrane protein SUMMARY #length 94 #molecular-weight 10866 #checksum 7642 SEQUENCE /// ENTRY BVECTY #type complete TITLE traY protein - Escherichia coli plasmid F ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 28-May-1999 ACCESSIONS B21874 REFERENCE A91507 !$#authors Fowler, T.; Taylor, L.; Thompson, R. !$#journal Gene (1983) 26:79-89 !$#title The control region of the F plasmid transfer operon: DNA !1sequence of the traJ and traY genes and characterisation of !1the traY -> Z promoter. !$#cross-references MUID:84159491; PMID:6368316 !$#accession B21874 !'##molecule_type DNA !'##residues 1-119 ##label FOW !'##cross-references GB:K01147; GB:K00381; NID:g148640; PIDN:AAA24909.1; !1PID:g148643 COMMENT This protein is required, together with traZ protein, for a !1strand-specific nicking event at oriT, the transfer origin !1of the plasmid. GENETICS !$#gene traY !$#genome plasmid CLASSIFICATION #superfamily traY protein KEYWORDS DNA binding SUMMARY #length 119 #molecular-weight 13862 #checksum 143 SEQUENCE /// ENTRY BVECRY #type complete TITLE traY protein - Escherichia coli plasmids ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 16-Jul-1999 ACCESSIONS C25033; C32014 REFERENCE A25033 !$#authors Finlay, B.B.; Frost, L.S.; Paranchych, W. !$#journal J. Bacteriol. (1986) 168:132-139 !$#title Origin of transfer of Incf plasmids and nucleotide sequences !1of the type II oriT, traM, and traY alleles from ColB4-K98 !1and the type IV traY allele from R100-1. !$#cross-references MUID:87008371; PMID:3531163 !$#accession C25033 !'##molecule_type DNA !'##residues 1-75 ##label FIN !'##cross-references GB:M15136; NID:g151788; PIDN:AAA26076.1; !1PID:g151789 !'##experimental_source plasmid R100-1 REFERENCE A32014 !$#authors Inamoto, S.; Yoshioka, Y.; Ohtsubo, E. !$#journal J. Bacteriol. (1988) 170:2749-2757 !$#title Identification and characterization of the products from the !1traJ and traY genes of plasmid R100. !$#cross-references MUID:88227859; PMID:2836369 !$#accession C32014 !'##molecule_type DNA !'##residues 1-75 ##label INA !'##cross-references GB:M20941; NID:g151778; PIDN:AAA26073.1; !1PID:g151781 !'##experimental_source plasmid R100 GENETICS !$#gene traY !$#genome plasmid !$#start_codon TTG FUNCTION !$#description involved in the conjugation process of bacterial cells for !1the exchange of plasmid DNA; also responsible for conjugal !1DNA metabolism CLASSIFICATION #superfamily traY protein KEYWORDS DNA binding; pilin formation; plasmid transfer SUMMARY #length 75 #molecular-weight 8542 #checksum 9469 SEQUENCE /// ENTRY BVECKY #type complete TITLE traY protein - Escherichia coli plasmid ColB4-K98 ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 28-May-1999 ACCESSIONS B25033 REFERENCE A25033 !$#authors Finlay, B.B.; Frost, L.S.; Paranchych, W. !$#journal J. Bacteriol. (1986) 168:132-139 !$#title Origin of transfer of Incf plasmids and nucleotide sequences !1of the type II oriT, traM, and traY alleles from ColB4-K98 !1and the type IV traY allele from R100-1. !$#cross-references MUID:87008371; PMID:3531163 !$#accession B25033 !'##molecule_type DNA !'##residues 1-75 ##label FIN !'##cross-references GB:M15135; NID:g144175; PIDN:AAB04665.1; !1PID:g144178 COMMENT This transfer gene protein is involved in the conjugation !1process of bacterial cells for the exchange of plasmid DNA. !1It is also responsible for conjugal DNA metabolism. GENETICS !$#gene traY !$#genome plasmid !$#start_codon GTG CLASSIFICATION #superfamily traY protein KEYWORDS DNA binding; pilin formation; plasmid transfer SUMMARY #length 75 #molecular-weight 9005 #checksum 9873 SEQUENCE /// ENTRY BVECTJ #type complete TITLE traJ protein - Escherichia coli plasmid F ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 21-Jul-2000 ACCESSIONS A21874; B29331; S26165; S26141 REFERENCE A91507 !$#authors Fowler, T.; Taylor, L.; Thompson, R. !$#journal Gene (1983) 26:79-89 !$#title The control region of the F plasmid transfer operon: DNA !1sequence of the traJ and traY genes and characterisation of !1the traY -> Z promoter. !$#cross-references MUID:84159491; PMID:6368316 !$#accession A21874 !'##molecule_type DNA !'##residues 1-229 ##label FOW !'##cross-references GB:K01147; GB:K00381; NID:g148640; PIDN:AAA24908.1; !1PID:g148642 REFERENCE A29331 !$#authors Thompson, R.; Taylor, L. !$#journal Mol. Gen. Genet. (1982) 188:513-518 !$#title Promoter mapping and DNA sequencing of the F plasmid !1transfer genes traM and traJ. !$#cross-references MUID:83141056; PMID:6298579 !$#accession B29331 !'##status preliminary !'##molecule_type DNA !'##residues 1-17 ##label THO !'##cross-references GB:X00545; NID:g42360; PIDN:CAA25217.1; PID:g42362 REFERENCE S26164 !$#authors Lopez, J.; Salazar, L.; Andres, I.; Ortiz, J.M.; Rodriguez, !1J.C. !$#journal Nucleic Acids Res. (1991) 19:3451 !$#title Nucleotide sequence of the oriT-traM-finP region of the !1haemolytic plasmid pSU316: comparison to F. !$#cross-references MUID:91288230; PMID:2062659 !$#accession S26165 !'##status preliminary; translation not shown !'##molecule_type DNA !'##residues 1-16 ##label LOP !'##cross-references EMBL:X55894; NID:g42552; PIDN:CAA39378.1; !1PID:g4490779 GENETICS !$#gene traJ !$#genome plasmid CLASSIFICATION #superfamily traJ protein KEYWORDS membrane protein; transcription regulation SUMMARY #length 229 #molecular-weight 27061 #checksum 8820 SEQUENCE /// ENTRY BVECRJ #type complete TITLE traJ protein - Escherichia coli plasmids ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 16-Jul-1999 ACCESSIONS A26021; S04679; B24544 REFERENCE A93125 !$#authors Koronakis, V.; Hogenauer, G. !$#journal Mol. Gen. Genet. (1986) 203:137-142 !$#title The sequences of the traJ gene and the 5' end of the traY !1gene of the resistance plasmid R1. !$#cross-references MUID:86230124; PMID:3012278 !$#accession A26021 !'##molecule_type DNA !'##residues 1-248 ##label KOR !'##experimental_source plasmid R1 !'##note Met-21 could also be the initiator Met of the protein REFERENCE S03309 !$#authors Koraimann, G.; Hoegenauer, G. !$#journal Nucleic Acids Res. (1989) 17:1283-1298 !$#title A stable core region of the tra operon mRNA of plasmid !1R1-19. !$#cross-references MUID:89160296; PMID:2564189 !$#accession S04679 !'##status preliminary !'##molecule_type mRNA !'##residues 238-248 ##label KO2 !'##cross-references EMBL:X13681; NID:g43119; PIDN:CAA31971.1; !1PID:g43120 !'##experimental_source plasmid R1-19 REFERENCE A24544 !$#authors Finlay, B.B.; Frost, L.S.; Paranchych, W. !$#journal J. Bacteriol. (1986) 166:368-374 !$#title Nucleotide sequences of the R1-19 plasmid transfer genes !1traM, finP, traJ, and traY and the traYZ promoter. !$#cross-references MUID:86195818; PMID:3009392 !$#accession B24544 !'##molecule_type DNA !'##residues 21-60,'R',62-220,'V' ##label FIN !'##cross-references GB:M19710; GB:M13168; NID:g150857; PIDN:AAA92657.1; !1PID:g150860 !'##experimental_source plasmid R1-19 GENETICS !$#gene traJ !$#genome plasmid FUNCTION !$#description a positively acting regulator CLASSIFICATION #superfamily plasmid R1 traJ protein KEYWORDS membrane protein; transcription regulation SUMMARY #length 248 #molecular-weight 28626 #checksum 3208 SEQUENCE /// ENTRY BVECTA #type complete TITLE trbA protein - Escherichia coli plasmid F ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 28-May-1999 ACCESSIONS A32238 REFERENCE A32238 !$#authors Wu, J.H.; Ippen-Ihler, K. !$#journal J. Bacteriol. (1989) 171:213-221 !$#title Nucleotide sequence of traQ and adjacent loci in the !1Escherichia coli K-12 F-plasmid transfer operon. !$#cross-references MUID:89123020; PMID:2536655 !$#accession A32238 !'##molecule_type DNA !'##residues 1-115 ##label WU1 !'##cross-references GB:M20787; NID:g148622; PIDN:AAC63065.1; !1PID:g148624 !'##experimental_source strain K12 GENETICS !$#gene trbA !$#genome plasmid CLASSIFICATION #superfamily trbA protein KEYWORDS F pilin formation; transmembrane protein SUMMARY #length 115 #molecular-weight 12944 #checksum 5357 SEQUENCE /// ENTRY BVECTB #type complete TITLE trbB protein precursor - Escherichia coli plasmid F ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 28-May-1999 ACCESSIONS E32238 REFERENCE A32238 !$#authors Wu, J.H.; Ippen-Ihler, K. !$#journal J. Bacteriol. (1989) 171:213-221 !$#title Nucleotide sequence of traQ and adjacent loci in the !1Escherichia coli K-12 F-plasmid transfer operon. !$#cross-references MUID:89123020; PMID:2536655 !$#accession E32238 !'##molecule_type DNA !'##residues 1-179 ##label WU1 !'##cross-references GB:M20787; NID:g148622; PIDN:AAC63067.1; !1PID:g148627 !'##experimental_source strain K12 GENETICS !$#gene trbB !$#genome plasmid CLASSIFICATION #superfamily trbB protein KEYWORDS F pilin formation; periplasmic space FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-179 #product trbB protein #status predicted #label MAT SUMMARY #length 179 #molecular-weight 19505 #checksum 963 SEQUENCE /// ENTRY BVECTF #type complete TITLE trbF protein - Escherichia coli plasmid F ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 24-Sep-1999 ACCESSIONS JS0124 REFERENCE A91600 !$#authors Ham, L.M.; Firth, N.; Skurray, R. !$#journal Gene (1989) 75:157-165 !$#title Nucleotide sequence of the F plasmid transfer gene, traH: !1identification of a new gene and a promoter within the !1transfer operon. !$#cross-references MUID:89252912; PMID:2656408 !$#accession JS0124 !'##molecule_type DNA !'##residues 1-126 ##label HAM !'##cross-references GB:M59763; NID:g148630; PIDN:AAA98079.1; !1PID:g148631 !'##experimental_source strain K12 COMMENT This protein is probably associated with the inner membrane. COMMENT The gene for this protein is cotranslated with the traH !1gene. GENETICS !$#gene trbF !$#genome plasmid CLASSIFICATION #superfamily trbF protein KEYWORDS transmembrane protein SUMMARY #length 126 #molecular-weight 14480 #checksum 8684 SEQUENCE /// ENTRY BVECAA #type complete TITLE artA protein - Escherichia coli plasmid F ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 28-May-1999 ACCESSIONS C32238 REFERENCE A32238 !$#authors Wu, J.H.; Ippen-Ihler, K. !$#journal J. Bacteriol. (1989) 171:213-221 !$#title Nucleotide sequence of traQ and adjacent loci in the !1Escherichia coli K-12 F-plasmid transfer operon. !$#cross-references MUID:89123020; PMID:2536655 !$#accession C32238 !'##molecule_type DNA !'##residues 1-104 ##label WU1 !'##cross-references GB:M20787; NID:g148622; PIDN:AAC63066.1; !1PID:g455195 !'##experimental_source strain K12 GENETICS !$#gene artA !$#genome plasmid CLASSIFICATION #superfamily artA protein SUMMARY #length 104 #molecular-weight 12130 #checksum 966 SEQUENCE /// ENTRY MZEC8 #type complete TITLE 58K mobilization protein - Escherichia coli plasmid CloDF13 ALTERNATE_NAMES protein B ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 16-Jul-1999 ACCESSIONS A29050; H28585 REFERENCE A91574 !$#authors van Putten, A.J.; Jochems, G.J.; de Lang, R.; Nijkamp, !1H.J.J. !$#journal Gene (1987) 51:171-178 !$#title Structure and nucleotide sequence of the region encoding the !1mobilization proteins of plasmid CloDF13. !$#cross-references MUID:87248075; PMID:3596243 !$#accession A29050 !'##molecule_type DNA !'##residues 1-529 ##label VAN REFERENCE A93765 !$#authors Nijkamp, H.J.J.; de Lang, R.; Stuitje, A.R.; van den Elzen, !1P.J.M.; Veltkamp, E.; van Putten, A.J. !$#journal Plasmid (1986) 16:135-160 !$#title The complete nucleotide sequence of the bacteriocinogenic !1plasmid CloDF13. !$#cross-references MUID:86314306; PMID:3749334 !$#accession H28585 !'##molecule_type DNA !'##residues 1-529 ##label NIJ !'##cross-references GB:X04466; GB:X00141; NID:g42320; PIDN:CAA28152.1; !1PID:g581178 !'##experimental_source strain K12 P678-54 !'##note the authors translated the codon GCC for residue 53 as Arg and !1ATG for residue 406 as Asn, omitted Phe-397, and included an !1additional Arg after Arg-391 COMMENT This is one of two proteins of the nonconjugative plasmid !1CloDF13 involved in plasmid transfer; the mobilization also !1requires a conjugative plasmid such as F or R. GENETICS !$#gene mobA !$#genome plasmid !$#start_codon GTG CLASSIFICATION #superfamily 58K mobilization protein KEYWORDS plasmid mobilization; replication SUMMARY #length 529 #molecular-weight 57840 #checksum 7854 SEQUENCE /// ENTRY ZTEC3 #type complete TITLE citrate utilization determinant - Escherichia coli transposon Tn3411 ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 28-May-1999 ACCESSIONS A23103 REFERENCE A23103 !$#authors Ishiguro, N.; Sato, G. !$#journal J. Bacteriol. (1985) 164:977-982 !$#title Nucleotide sequence of the gene determining plasmid-mediated !1citrate utilization. !$#cross-references MUID:86059246; PMID:2999087 !$#accession A23103 !'##molecule_type DNA !'##residues 1-431 ##label ISH !'##cross-references GB:M22041; GB:M11992; NID:g154974; PIDN:AAA98398.1; !1PID:g154976 !'##experimental_source strain K12 COMMENT This protein is involved in a system that enables E. coli to !1utilize citrate as a sole source of carbon and energy. GENETICS !$#gene cit CLASSIFICATION #superfamily citrate utilization determinant KEYWORDS membrane protein SUMMARY #length 431 #molecular-weight 47077 #checksum 6302 SEQUENCE /// ENTRY ZTEC6 #type complete TITLE citrate utilization determinant - Escherichia coli plasmid pWR60 ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 28-May-1999 ACCESSIONS B23104 REFERENCE A91810 !$#authors Sasatsu, M.; Misra, T.K.; Chu, L.; Laddaga, R.; Silver, S. !$#journal J. Bacteriol. (1985) 164:983-993 !$#title Cloning and DNA sequence of a plasmid-determined citrate !1utilization system in Escherichia coli. !$#cross-references MUID:86059247; PMID:2999088 !$#accession B23104 !'##molecule_type DNA !'##residues 1-431 ##label SAS !'##cross-references GB:M11559; NID:g151715; PIDN:AAA88472.1; !1PID:g1196801 GENETICS !$#genome plasmid CLASSIFICATION #superfamily citrate utilization determinant KEYWORDS membrane protein SUMMARY #length 431 #molecular-weight 46979 #checksum 6055 SEQUENCE /// ENTRY S32331 #type complete TITLE proline/betaine transport protein - Escherichia coli (strain K-12) ALTERNATE_NAMES proline permease II; proline porter II ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS S32331; S56339; F65220 REFERENCE S32331 !$#authors Culham, D.E.; Lasby, B.; Marangoni, A.G.; Milner, J.L.; !1Steer, B.A.; van Nues, R.W.; Wood, J.M. !$#journal J. Mol. Biol. (1993) 229:268-276 !$#title Isolation and sequencing of Escherichia coli gene proP !1reveals unusual structural features of the osmoregulatory !1proline/betaine transporter, ProP. !$#cross-references MUID:93132799; PMID:8421314 !$#accession S32331 !'##molecule_type DNA !'##residues 1-500 ##label CUL !'##cross-references EMBL:M83089; NID:g147356; PIDN:AAB00919.1; !1PID:g147357 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56339 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-500 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97010.1; !1PID:g536955 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65220 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-500 ##label BLAT !'##cross-references GB:AE000483; GB:U00096; NID:g2367351; !1PIDN:AAC77072.1; PID:g1790550; UWGP:b4111 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene proP !$#map_position 93 min FUNCTION !$#description involved in osmoregulatory response CLASSIFICATION #superfamily citrate utilization determinant KEYWORDS transmembrane protein; transport protein FEATURE !$62-78 #domain transmembrane #status predicted #label TM1\ !$98-114 #domain transmembrane #status predicted #label TM2\ !$173-189 #domain transmembrane #status predicted #label TM3\ !$201-217 #domain transmembrane #status predicted #label TM4\ !$298-314 #domain transmembrane #status predicted #label TM5\ !$330-346 #domain transmembrane #status predicted #label TM6\ !$349-365 #domain transmembrane #status predicted #label TM7\ !$395-411 #domain transmembrane #status predicted #label TM8\ !$417-433 #domain transmembrane #status predicted #label TM9 SUMMARY #length 500 #molecular-weight 54845 #checksum 93 SEQUENCE /// ENTRY BVECPA #type complete TITLE parA protein - phage P1 ORGANISM #formal_name phage P1 DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 16-Jul-1999 ACCESSIONS A23752 REFERENCE A92917 !$#authors Abeles, A.L.; Friedman, S.A.; Austin, S.J. !$#journal J. Mol. Biol. (1985) 185:261-272 !$#title Partition of unit-copy miniplasmids to daughter cells. III. !1The DNA sequence and functional organization of the P1 !1partition region. !$#cross-references MUID:86037206; PMID:3903163 !$#accession A23752 !'##molecule_type DNA !'##residues 1-398 ##label ABE !'##cross-references GB:K02380; GB:M24626; GB:X02954; NID:g215652; !1PIDN:AAA99230.1; PID:g215654 COMMENT This protein is essential for plasmid partition. It ensures !1the proper distribution of newly replicated plasmids to !1daughter cells during cell division. GENETICS !$#gene parA CLASSIFICATION #superfamily parA protein KEYWORDS cell division; plasmid partition SUMMARY #length 398 #molecular-weight 44269 #checksum 9367 SEQUENCE /// ENTRY BVECPB #type complete TITLE partition protein ParB - phage P1 ORGANISM #formal_name phage P1 DATE 31-Mar-1988 #sequence_revision 09-May-1997 #text_change 16-Jul-1999 ACCESSIONS B23752; A39981; S68590 REFERENCE A92917 !$#authors Abeles, A.L.; Friedman, S.A.; Austin, S.J. !$#journal J. Mol. Biol. (1985) 185:261-272 !$#title Partition of unit-copy miniplasmids to daughter cells. III. !1The DNA sequence and functional organization of the P1 !1partition region. !$#cross-references MUID:86037206; PMID:3903163 !$#accession B23752 !'##molecule_type DNA !'##residues 1-309,'RVTGRTRQDDCGISLERASIKSRSLKLSPFKFHY' ##label ABE !'##cross-references GB:X02954; NID:g42238; PIDN:CAA26699.1; PID:g42240 !'##note this sequence has been corrected in S68590 REFERENCE A39981 !$#authors Martin, K.A.; Friedman, S.A.; Austin, S.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:8544-8547 !$#title Partition site of the P1 plasmid. !$#cross-references MUID:88068625; PMID:3317415 !$#accession A39981 !'##molecule_type DNA !'##residues 'SIKSRSLKLSPFKFHY' ##label MAR !'##note this sequence has been corrected in S68590 REFERENCE S68590 !$#authors Lobocka, M.; Yarmolinsky, M. !$#journal J. Mol. Biol. (1996) 259:366-382 !$#title P1 plasmid partition: a mutational analysis of ParB. !$#cross-references MUID:96256516; PMID:8676375 !$#accession S68590 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 183-333 ##label LOB !'##cross-references EMBL:L01408; NID:g215642; PIDN:AAA32421.1; !1PID:g215643 !'##note this report corrects the sequence reported in A92917 and cited !1in A39981 COMMENT This protein is essential for plasmid (prophage) partition. !1It ensures the proper distribution of newly replicated !1plasmids to daughter cells during cell division. GENETICS !$#gene parB CLASSIFICATION #superfamily parB protein KEYWORDS cell division; DNA binding; plasmid partition SUMMARY #length 333 #molecular-weight 37440 #checksum 7997 SEQUENCE /// ENTRY BVECAF #type complete TITLE sopA protein - Escherichia coli plasmid F and pO157 ALTERNATE_NAMES plasmid partitioning protein ORGANISM #formal_name Escherichia coli DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 18-Aug-2000 ACCESSIONS A25783; T42168; S28095 REFERENCE A92934 !$#authors Mori, H.; Kondo, A.; Ohshima, A.; Ogura, T.; Hiraga, S. !$#journal J. Mol. Biol. (1986) 192:1-15 !$#title Structure and function of the F plasmid genes essential for !1partitioning. !$#cross-references MUID:87141188; PMID:3029390 !$#accession A25783 !'##molecule_type DNA !'##residues 1-388 ##label MOR !'##cross-references EMBL:X04619; NID:g42429; PIDN:CAA28295.1; !1PID:g42431 REFERENCE Z22068 !$#authors Burland, V.; Shao, Y.; Perna, N.T.; Plunkett, G.; Sofia, !1H.J.; Blattner, F.R. !$#journal Nucleic Acids Res. (1998) 26:4196-4204 !$#title The complete DNA sequence and analysis of the large !1virulence plasmid of Escherichia coli O157:H7. !$#cross-references MUID:98391744; PMID:9722640 !$#accession T42168 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-388 ##label BUR !'##cross-references EMBL:AF074613; NID:g3822114; PIDN:AAC70136.1; !1PID:g3822182 !'##experimental_source strain EDL933; serotype O157:H7; plasmid pO157 COMMENT This is one of the proteins coded by the sop region, which !1is responsible for correct partitioning of plasmid DNA into !1daughter cells. GENETICS !$#gene sopA !$#genome plasmid CLASSIFICATION #superfamily sopA protein KEYWORDS plasmid partition SUMMARY #length 388 #molecular-weight 43660 #checksum 4363 SEQUENCE /// ENTRY BVECCF #type complete TITLE sopC protein - Escherichia coli plasmid F ORGANISM #formal_name Escherichia coli DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS C25783; S28097 REFERENCE A92934 !$#authors Mori, H.; Kondo, A.; Ohshima, A.; Ogura, T.; Hiraga, S. !$#journal J. Mol. Biol. (1986) 192:1-15 !$#title Structure and function of the F plasmid genes essential for !1partitioning. !$#cross-references MUID:87141188; PMID:3029390 !$#accession C25783 !'##molecule_type DNA !'##residues 1-79 ##label MOR !'##cross-references EMBL:X04619; NID:g42429; PIDN:CAA28297.1; !1PID:g581191 COMMENT This cis-acting protein exhibits IncD incompatibility; it is !1one of the proteins coded by the sop region, which is !1responsible for correct partitioning of plasmid DNA into !1daughter cells. GENETICS !$#gene sopC !$#genome plasmid !$#start_codon GTG CLASSIFICATION #superfamily sopC protein SUMMARY #length 79 #molecular-weight 8147 #checksum 4852 SEQUENCE /// ENTRY RGECSS #type complete TITLE stringent starvation protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 01-Mar-2002 ACCESSIONS A26422; G65114 REFERENCE A26422 !$#authors Serizawa, H.; Fukuda, R. !$#journal Nucleic Acids Res. (1987) 15:1153-1163 !$#title Structure of the gene for the stringent starvation protein !1of Escherichia coli. !$#cross-references MUID:87146422; PMID:3029697 !$#accession A26422 !'##molecule_type DNA !'##residues 1-212 ##label SER !'##cross-references GB:X05088; NID:g42997; PIDN:CAA28740.1; PID:g42998 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65114 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-212 ##label BLAT !'##cross-references GB:AE000402; GB:U00096; NID:g1789619; !1PIDN:AAC76261.1; PID:g1789624; UWGP:b3229 !'##experimental_source strain K-12, substrain MG1655 COMMENT This protein, which forms an equimolar complex with the RNA !1polymerase holoenzyme but not with the core enzyme, is !1synthesized predominantly when cells are exposed to amino !1acid starvation, at which time it accounts for over 50% of !1the total protein synthesized. GENETICS !$#gene sspA (ssp) !$#map_position 69.5 min CLASSIFICATION #superfamily stringent starvation protein SUMMARY #length 212 #molecular-weight 24305 #checksum 6065 SEQUENCE /// ENTRY MZEC6 #type complete TITLE 16K mobilization protein - Escherichia coli plasmid CloDF13 ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 16-Jul-1999 ACCESSIONS B29050; G28585 REFERENCE A91574 !$#authors van Putten, A.J.; Jochems, G.J.; de Lang, R.; Nijkamp, !1H.J.J. !$#journal Gene (1987) 51:171-178 !$#title Structure and nucleotide sequence of the region encoding the !1mobilization proteins of plasmid CloDF13. !$#cross-references MUID:87248075; PMID:3596243 !$#accession B29050 !'##molecule_type DNA !'##residues 1-148 ##label VAN !'##note the authors translated the codon TGG for residue 85 as Gly REFERENCE A93765 !$#authors Nijkamp, H.J.J.; de Lang, R.; Stuitje, A.R.; van den Elzen, !1P.J.M.; Veltkamp, E.; van Putten, A.J. !$#journal Plasmid (1986) 16:135-160 !$#title The complete nucleotide sequence of the bacteriocinogenic !1plasmid CloDF13. !$#cross-references MUID:86314306; PMID:3749334 !$#accession G28585 !'##molecule_type DNA !'##residues 1-84,'G',86-148 ##label NIJ !'##cross-references GB:X04466; GB:J01558; GB:J01559; GB:J01560; !1GB:J01561; GB:J01562; GB:K02267; GB:K02333; GB:M16195; !1GB:M17497; GB:M23861; GB:M38599; GB:V00377; GB:X00141; !1GB:X00223; GB:X01287; NID:g42320; PIDN:CAA28151.1; !1PID:g42327 !'##experimental_source strain K12 P678-54 !'##note the authors translated the codon CTC for residue 126 as Ser GENETICS !$#genome plasmid CLASSIFICATION #superfamily 16K mobilization protein KEYWORDS plasmid mobilization; replication SUMMARY #length 148 #molecular-weight 16062 #checksum 5414 SEQUENCE /// ENTRY NXEC #type complete TITLE exclusion-determining protein - Escherichia coli plasmid R144 ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 28-May-1999 ACCESSIONS A24466 REFERENCE A24466 !$#authors Hartskeerl, R.; Overduin, P.; Hoekstra, W.; Tommassen, J. !$#journal Gene (1986) 42:107-111 !$#title Nucleotide sequence of the exclusion-determining locus of !1IncI plasmid R144. !$#cross-references MUID:86248673; PMID:3721199 !$#accession A24466 !'##molecule_type DNA !'##residues 1-220 ##label HAR !'##cross-references GB:M13492; NID:g151799; PIDN:AAA26077.1; !1PID:g151800 COMMENT Conjugative plasmids generally prevent the effective entry !1of donor DNA from other cells carrying identical (or closely !1related) plasmids by encoding a barrier in the cell !1envelope. In R144 this type of exclusion affects only DNA !1transfer. GENETICS !$#gene exc !$#genome plasmid CLASSIFICATION #superfamily exclusion-determining protein R144 SUMMARY #length 220 #molecular-weight 25756 #checksum 4505 SEQUENCE /// ENTRY BVECRD #type complete TITLE rod shape-determining protein mrdB - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 01-Mar-2002 ACCESSIONS JT0500; C28387; H64797 REFERENCE A32257 !$#authors Matsuzawa, H.; Asoh, S.; Kunai, K.; Muraiso, K.; Takasuga, !1A.; Ohta, T. !$#journal J. Bacteriol. (1989) 171:558-560 !$#title Nucleotide sequence of the rodA gene, responsible for the !1rod shape of Escherichia coli: rodA and the pbpA gene, !1encoding penicillin-binding protein 2, constitute the rodA !1operon. !$#cross-references MUID:89123070; PMID:2644207 !$#accession JT0500 !'##molecule_type DNA !'##residues 1-370 ##label MAT !'##cross-references GB:M22857; NID:g147693; PIDN:AAA24571.1; !1PID:g147695 REFERENCE A91853 !$#authors Takase, I.; Ishino, F.; Wachi, M.; Kamata, H.; Doi, M.; !1Asoh, S.; Matsuzawa, H.; Ohta, T.; Matsuhashi, M. !$#journal J. Bacteriol. (1987) 169:5692-5699 !$#title Genes encoding two lipoproteins in the leuS-dacA region of !1the Escherichia coli chromosome. !$#cross-references MUID:88058785; PMID:3316191 !$#accession C28387 !'##molecule_type DNA !'##residues 355-370 ##label TAK !'##cross-references GB:M18276; NID:g147658; PIDN:AAA24551.1; !1PID:g147659 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64797 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-370 ##label BLAT !'##cross-references GB:AE000168; GB:U00096; NID:g1786849; !1PIDN:AAC73735.1; PID:g1786853; UWGP:b0634 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene mrdB; rodA !$#map_position 15 min FUNCTION !$#description one of the proteins responsible for the rod shape of E.coli CLASSIFICATION #superfamily rod shape-determining protein KEYWORDS transmembrane protein FEATURE !$19-35 #domain transmembrane #status predicted #label TM1\ !$50-66 #domain transmembrane #status predicted #label TM2\ !$80-96 #domain transmembrane #status predicted #label TM3\ !$140-156 #domain transmembrane #status predicted #label TM4\ !$160-176 #domain transmembrane #status predicted #label TM5\ !$186-202 #domain transmembrane #status predicted #label TM6\ !$272-288 #domain transmembrane #status predicted #label TM7\ !$309-325 #domain transmembrane #status predicted #label TM8\ !$343-359 #domain transmembrane #status predicted #label TM9 SUMMARY #length 370 #molecular-weight 40476 #checksum 7054 SEQUENCE /// ENTRY CEECFW #type complete TITLE cell division protein ftsW - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 01-Mar-2002 ACCESSIONS A32581; S40599; A64731 REFERENCE A32581 !$#authors Ikeda, M.; Sato, T.; Wachi, M.; Jung, H.K.; Ishino, F.; !1Kobayashi, Y.; Matsuhashi, M. !$#journal J. Bacteriol. (1989) 171:6375-6378 !$#title Structural similarity among Escherichia coli FtsW and RodA !1proteins and Bacillus subtilis SpoVE protein, which function !1in cell division, cell elongation, and spore formation, !1respectively. !$#cross-references MUID:90036736; PMID:2509435 !$#accession A32581 !'##molecule_type DNA !'##residues 1-414 ##label IKE !'##cross-references GB:X55034; GB:M10429; NID:g40841; PIDN:CAA38866.1; !1PID:g40857 !'##note it is uncertain whether Met-1 or Met-31 is the initiator REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40599 !'##molecule_type DNA !'##residues 1-414 ##label YUR !'##cross-references EMBL:D10483; NID:g216434; PIDN:BAA01354.1; !1PID:g216503 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64731 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-414 ##label BLAT !'##cross-references GB:AE000118; GB:U00096; NID:g1786262; !1PIDN:AAC73200.1; PID:g1786277; UWGP:b0089 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ftsW !$#map_position 2 min CLASSIFICATION #superfamily rod shape-determining protein KEYWORDS cell division; cell wall; transmembrane protein FEATURE !$47-63 #domain transmembrane #status predicted #label TM1\ !$86-102 #domain transmembrane #status predicted #label TM2\ !$112-128 #domain transmembrane #status predicted #label TM3\ !$178-194 #domain transmembrane #status predicted #label TM4\ !$201-217 #domain transmembrane #status predicted #label TM5\ !$222-238 #domain transmembrane #status predicted #label TM6\ !$307-323 #domain transmembrane #status predicted #label TM7\ !$342-358 #domain transmembrane #status predicted #label TM8\ !$381-397 #domain transmembrane #status predicted #label TM9 SUMMARY #length 414 #molecular-weight 45987 #checksum 1024 SEQUENCE /// ENTRY SZBS5E #type complete TITLE stage V sporulation protein E - Bacillus subtilis ALTERNATE_NAMES spore cortex synthesis protein spoVE ORGANISM #formal_name Bacillus subtilis DATE 28-Dec-1987 #sequence_revision 06-Jan-1995 #text_change 16-Jun-2000 ACCESSIONS S10243; A29756; E47691; S22211; E69715 REFERENCE S10243 !$#authors Sato, T.; Theeragool, G.; Yamamoto, T.; Okamoto, M.; !1Kobayashi, Y. !$#journal Nucleic Acids Res. (1990) 18:4021 !$#title Revised nucleotide sequence of the sporulation gene spoVE !1from Bacillus subtilis. !$#cross-references MUID:90326557; PMID:2115675 !$#accession S10243 !'##status translation not shown !'##molecule_type DNA !'##residues 1-366 ##label SAT !'##cross-references EMBL:X51419; NID:g40189; PIDN:CAA35783.1; !1PID:g580937 REFERENCE A29756 !$#authors Bugaichuk, U.D.; Piggot, P.J. !$#journal J. Gen. Microbiol. (1986) 132:1883-1890 !$#title Nucleotide sequence of the Bacillus subtilis developmental !1gene spoVE. !$#cross-references MUID:87085411; PMID:3098901 !$#accession A29756 !'##molecule_type DNA !'##residues 'MVQIADGYLLFPS',87-366 ##label BUG !'##cross-references GB:M15742; NID:g143656; PIDN:AAA22807.1; !1PID:g143657 REFERENCE A47691 !$#authors Daniel, R.A.; Errington, J. !$#journal J. Gen. Microbiol. (1993) 139:361-370 !$#title DNA sequence of the murE-murD region of Bacillus subtilis !1168. !$#cross-references MUID:93171879; PMID:8436954 !$#contents 168 !$#accession E47691 !'##molecule_type DNA !'##residues 1-40 ##label DAN !'##note sequence extracted from NCBI backbone (NCBIN:125659, !1NCBIP:125665) REFERENCE S22211 !$#authors Henriques, D.O.; de Lencastre, H.; Piggot, P.J. !$#submission submitted to the EMBL Data Library, January 1992 !$#accession S22211 !'##molecule_type DNA !'##residues 343-366 ##label HEN !'##cross-references EMBL:X64259; NID:g39994; PIDN:CAA45557.1; !1PID:g580894 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69715 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-366 ##label KUN !'##cross-references GB:Z99111; GB:AL009126; NID:g2633699; !1PIDN:CAB13394.1; PID:g2633892 !'##experimental_source strain 168 GENETICS !$#gene spoVE !$#map_position 133 (degrees) !$#start_codon TTG CLASSIFICATION #superfamily rod shape-determining protein KEYWORDS sporulation; transmembrane protein SUMMARY #length 366 #molecular-weight 40132 #checksum 1239 SEQUENCE /// ENTRY BVECEB #type complete TITLE rod shape-determining protein envB - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1990 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS E65117; A31843; JS0145 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65117 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-367 ##label BLAT !'##cross-references GB:AE000404; GB:U00096; NID:g2367207; !1PIDN:AAC76283.1; PID:g1789649; UWGP:b3251 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A91887 !$#authors Doi, M.; Wachi, M.; Ishino, F.; Tomioka, S.; Ito, M.; !1Sakagami, Y.; Suzuki, A.; Matsuhashi, M. !$#journal J. Bacteriol. (1988) 170:4619-4624 !$#title Determinations of the DNA sequence of the mreB gene and of !1the gene products of the mre region that function in !1formation of the rod shape of Escherichia coli cells. !$#cross-references MUID:89008079; PMID:3049542 !$#accession A31843 !'##molecule_type DNA !'##residues 21-79,'NE',82-284,'I',286-296,'HT',299-367 ##label DOI !'##cross-references GB:M22055; NID:g146887; PIDN:AAA83891.1; !1PID:g1128967 !'##experimental_source strain K12 !'##note residues 21-32 were confirmed by protein sequencing COMMENT This protein plays a role in shape determination and !1mecillinam sensitivity of the cell. GENETICS !$#gene mreB; envB !$#map_position 71 min CLASSIFICATION #superfamily rod shape-determining protein envB SUMMARY #length 367 #molecular-weight 38972 #checksum 5194 SEQUENCE /// ENTRY JV0059 #type complete TITLE rod shape-determining protein mreC - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 07-Sep-1990 #sequence_revision 19-Jan-1996 #text_change 01-Mar-2002 ACCESSIONS JV0059; C31843; D65117; PS0033 REFERENCE JV0059 !$#authors Wachi, M.; Doi, M.; Okada, Y.; Matsuhashi, M. !$#journal J. Bacteriol. (1989) 171:6511-6516 !$#title New mre genes mreC and mreD, responsible for formation of !1the rod shape of Escherichia coli cells. !$#cross-references MUID:90078091; PMID:2687239 !$#accession JV0059 !'##molecule_type DNA !'##residues 1-367 ##label WAC !'##cross-references GB:M31792; NID:g146816; PIDN:AAA24155.1; !1PID:g146818 REFERENCE A91887 !$#authors Doi, M.; Wachi, M.; Ishino, F.; Tomioka, S.; Ito, M.; !1Sakagami, Y.; Suzuki, A.; Matsuhashi, M. !$#journal J. Bacteriol. (1988) 170:4619-4624 !$#title Determinations of the DNA sequence of the mreB gene and of !1the gene products of the mre region that function in !1formation of the rod shape of Escherichia coli cells. !$#cross-references MUID:89008079; PMID:3049542 !$#accession C31843 !'##molecule_type DNA !'##residues 1-128 ##label DOI !'##cross-references GB:M22055; NID:g146887; PIDN:AAA83892.1; !1PID:g146888 !'##experimental_source strain K12 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65117 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-367 ##label BLAT !'##cross-references GB:AE000404; GB:U00096; NID:g2367207; !1PIDN:AAC76282.1; PID:g1789648; UWGP:b3250 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene mreC !$#map_position 71 min FUNCTION !$#description plays a role in rod shape determination and mecillinam !1sensitivity of the cell CLASSIFICATION #superfamily rod shape-determining protein mreC SUMMARY #length 367 #molecular-weight 39530 #checksum 7346 SEQUENCE /// ENTRY BVECUI #type complete TITLE membrane-bound ATP synthase uncI [imported] - Escherichia coli (strain K-12) ALTERNATE_NAMES ATP synthase subunit atpI ORGANISM #formal_name Escherichia coli DATE 02-Apr-1982 #sequence_revision 15-Oct-1982 #text_change 01-Mar-2002 ACCESSIONS D30389; A23223; A34908; D65177; I52197; A04433 REFERENCE A30389 !$#authors Walker, J.E.; Gay, N.J.; Saraste, M.; Eberle, A.N. !$#journal Biochem. J. (1984) 224:799-815 !$#title DNA sequence around the Escherichia coli unc operon. !1Completion of the sequence of a 17 kilobase segment !1containing asnA, oriC, unc, glmS and phoS. !$#cross-references MUID:85121806; PMID:6395859 !$#accession D30389 !'##molecule_type DNA !'##residues 1-130 ##label WAL !'##cross-references GB:X01631; NID:g43256; PIDN:CAA25775.1; PID:g581248 REFERENCE A23223 !$#authors Kanazawa, H.; Kiyasu, T.; Noumi, T.; Futai, M. !$#journal J. Bacteriol. (1984) 158:300-306 !$#title Overproduction of subunit a of the F0 component of !1proton-translocation ATPase inhibits growth of Escherichia !1coli cells. !$#cross-references MUID:84185438; PMID:6325392 !$#accession A23223 !'##molecule_type DNA !'##residues 1-130 ##label KAN REFERENCE A34908 !$#authors Schneppe, B.; Deckers-Hebestreit, G.; Altendorf, K. !$#journal J. Biol. Chem. (1990) 265:389-395 !$#title Overproduction and purification of the uncI gene product of !1the ATP synthase of Escherichia coli. !$#cross-references MUID:90094427; PMID:2136739 !$#accession A34908 !'##status preliminary !'##molecule_type protein !'##residues 1-12 ##label SCH REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65177 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-130 ##label BLAT !'##cross-references GB:AE000450; GB:U00096; NID:g1790166; !1PIDN:AAC76762.1; PID:g1790177; UWGP:b3739 !'##experimental_source strain K-12, substrain MG1655 REFERENCE I52197 !$#authors Kanazawa, H.; Mabuchi, K.; Futai, M. !$#journal Biochem. Biophys. Res. Commun. (1982) 107:568-575 !$#title Nucleotide sequence of the promoter region of the gene !1cluster for proton-translocating ATPase from Escherichia !1coli and identification of the active promotor. !$#cross-references MUID:83022404; PMID:6215041 !$#accession I52197 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 'M',32-84 ##label RES !'##cross-references EMBL:V00313; NID:g42286; PIDN:CAA23599.1; !1PID:g581172 COMMENT The uncI gene is the first gene of the unc (or atp) operon. !1A possible function for this protein is to guide the !1assembly of the membrane sector of the proton transporting !1ATP synthase (EC 3.6.1.34) enzyme complex. GENETICS !$#gene atpI; uncI !$#map_position 84 min !$#start_codon GTG CLASSIFICATION #superfamily uncI protein KEYWORDS transmembrane protein SUMMARY #length 130 #molecular-weight 14104 #checksum 4271 SEQUENCE /// ENTRY BWUT8Q #type complete TITLE regulatory protein ESAG8c - Trypanosoma equiperdum ORGANISM #formal_name Trypanosoma equiperdum DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 01-Sep-2000 ACCESSIONS S16358 REFERENCE S16358 !$#authors Ross, D.T.; Raibaud, A.; Florent, I.C.; Sather, S.; Gross, !1M.K.; Storm, D.R.; Eisen, H. !$#journal EMBO J. (1991) 10:2047-2053 !$#title The trypanosome VSG expression site encodes adenylate !1cyclase and a leucine-rich putative regulatory gene. !$#cross-references MUID:91293076; PMID:2065652 !$#accession S16358 !'##molecule_type DNA !'##residues 1-630 ##label ROS !'##cross-references EMBL:X59385; NID:g10969; PIDN:CAA42028.1; !1PID:g10970 CLASSIFICATION #superfamily regulatory protein ESAG8c; RING finger homology KEYWORDS DNA binding; zinc finger FEATURE !$6-51 #domain RING finger homology #label RRN SUMMARY #length 630 #molecular-weight 69989 #checksum 2905 SEQUENCE /// ENTRY BWSAM1 #type complete TITLE mecR1 protein - Staphylococcus epidermidis ORGANISM #formal_name Staphylococcus epidermidis DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jul-1999 ACCESSIONS S18044 REFERENCE S18044 !$#authors Ryffel, C.; Tesch, W.; Kayser, F.H.; Berger-Baechi, B. !$#submission submitted to the EMBL Data Library, August 1990 !$#description Nucleotide sequence of the methicillin resistance regulatory !1locus mecR of Staphylococcus epidermidis. !$#accession S18044 !'##molecule_type DNA !'##residues 1-585 ##label RYF !'##cross-references EMBL:X54660; NID:g46995; PIDN:CAA38470.1; !1PID:g581652 GENETICS !$#gene mecR1 !$#start_codon GTG CLASSIFICATION #superfamily mecR1 protein; beta-lactamase OXA2 homology KEYWORDS antibiotic resistance FEATURE !$357-585 #domain beta-lactamase OXA2 homology #label OXA2 SUMMARY #length 585 #molecular-weight 68502 #checksum 6321 SEQUENCE /// ENTRY S11783 #type complete TITLE bla regulator protein blaR1 - Staphylococcus aureus plasmids ALTERNATE_NAMES probable beta-lactam receptor signal transducer protein ORGANISM #formal_name Staphylococcus aureus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S11783; S27371; S34445 REFERENCE S11779 !$#authors Rowland, S.J.; Dyke, K.G.H. !$#journal Mol. Microbiol. (1990) 4:961-975 !$#title Tn552, a novel transposable element from Staphylococcus !1aureus. !$#cross-references MUID:91014696; PMID:2170815 !$#accession S11783 !'##molecule_type DNA !'##residues 1-585 ##label ROW !'##cross-references EMBL:X52734 !'##experimental_source transposon Tn552 !'##note the authors translated the codon ATA for residue 149 as Ala, !1GCG for residue 262 as Ser, AAG for residue 426 as Arg, GTA !1for residue 545 as Ile, and ATT for residue 546 as Thr REFERENCE S27370 !$#authors Rowland, S.J. !$#submission submitted to the EMBL Data Library, April 1990 !$#accession S27371 !'##molecule_type DNA !'##residues 1-105,'S',107-585 ##label RO2 !'##cross-references EMBL:X52734; NID:g46754; PIDN:CAA36952.1; !1PID:g46759 !'##experimental_source transposon Tn552 REFERENCE S34444 !$#authors Wang, P.Z.; Projan, S.J.; Novick, R.P. !$#journal Nucleic Acids Res. (1991) 19:4000 !$#title Nucleotide sequence of beta-lactamase regulatory genes from !1staphylococcal plasmid pl258. !$#cross-references MUID:91319567; PMID:1861992 !$#accession S34445 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-585 ##label WAN !'##cross-references EMBL:M62650; NID:g152964; PIDN:AAA26602.1; !1PID:g152966 !'##experimental_source strain RN11, plasmid pl258 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1September 1991 GENETICS !$#gene blaR1 !$#genome plasmid !$#mobile_element transposon Tn552 CLASSIFICATION #superfamily mecR1 protein; beta-lactamase OXA2 homology KEYWORDS transmembrane protein FEATURE !$355-582 #domain beta-lactamase OXA2 homology #label OXA2 SUMMARY #length 585 #molecular-weight 69261 #checksum 1603 SEQUENCE /// ENTRY I39942 #type complete TITLE penicillinase antirepressor penJ - Bacillus licheniformis ORGANISM #formal_name Bacillus licheniformis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS I39942 REFERENCE I39940 !$#authors Imanaka, T.; Himeno, T.; Aiba, S. !$#journal J. Bacteriol. (1987) 169:3867-3872 !$#title Cloning and nucleotide sequence of the penicillinase !1antirepressor gene penJ of Bacillus licheniformis. !$#cross-references MUID:87307953; PMID:3040662 !$#accession I39942 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-601 ##label RES !'##cross-references GB:M22353; NID:g143300; PIDN:AAA22653.1; !1PID:g143304 CLASSIFICATION #superfamily mecR1 protein; beta-lactamase OXA2 homology FEATURE !$366-596 #domain beta-lactamase OXA2 homology #label OXA2 SUMMARY #length 601 #molecular-weight 68385 #checksum 3294 SEQUENCE /// ENTRY RGBSBI #type complete TITLE regulatory protein blaI - Bacillus licheniformis ALTERNATE_NAMES bla repressor; regulatory protein penI ORGANISM #formal_name Bacillus licheniformis DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jul-1999 ACCESSIONS S00093; S18502; I39789; A29114 REFERENCE S00093 !$#authors Nicholls, N.J.; Lampen, J.O. !$#journal FEBS Lett. (1987) 221:179-183 !$#title Repressor gene, blaI, for Bacillus licheniformis 749 !1beta-lactamase. !$#cross-references MUID:87304807; PMID:3305074 !$#accession S00093 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-128 ##label NIC REFERENCE S18502 !$#authors Himeno, T.; Imanaka, T.; Aiba, S. !$#journal J. Bacteriol. (1986) 168:1128-1132 !$#title Nucleotide sequence of the penicillinase repressor gene penI !1of Bacillus licheniformis and regulation of penP and penI by !1the repressor. !$#cross-references MUID:87057011; PMID:3096969 !$#accession S18502 !'##status preliminary !'##molecule_type DNA !'##residues 1-128 ##label HIM !'##cross-references EMBL:M14734; NID:g143292; PIDN:AAA22648.1; !1PID:g143294 REFERENCE I39789 !$#authors Kobayashi, T.; Zhu, Y.F.; Nicholls, N.J.; Lampen, J.O. !$#journal J. Bacteriol. (1987) 169:3873-3878 !$#title A second regulatory gene, blaR1, encoding a potential !1penicillin-binding protein required for induction of beta- !1lactamase in Bacillus licheniformis. !$#cross-references MUID:87307954; PMID:3040663 !$#accession I39789 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 106-128 ##label RES !'##cross-references GB:M17368; NID:g142596; PIDN:AAA22272.1; !1PID:g142597 GENETICS !$#gene blaI CLASSIFICATION #superfamily regulatory protein blaI KEYWORDS DNA binding; transcription regulation SUMMARY #length 128 #molecular-weight 15034 #checksum 1599 SEQUENCE /// ENTRY RGSAMI #type complete TITLE probable regulatory protein mecI - Staphylococcus epidermidis ORGANISM #formal_name Staphylococcus epidermidis DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 01-Aug-1997 ACCESSIONS S18045 REFERENCE S18044 !$#authors Ryffel, C.; Tesch, W.; Kayser, F.H.; Berger-Baechi, B. !$#submission submitted to the EMBL Data Library, August 1990 !$#description Nucleotide sequence of the methicillin resistance regulatory !1locus mecR of Staphylococcus epidermidis. !$#accession S18045 !'##molecule_type DNA !'##residues 1-110 ##label RYF !'##cross-references EMBL:X54660 GENETICS !$#gene mecI CLASSIFICATION #superfamily regulatory protein blaI KEYWORDS antibiotic resistance; DNA binding; transcription regulation SUMMARY #length 110 #molecular-weight 13467 #checksum 9441 SEQUENCE /// ENTRY I40444 #type complete TITLE Spo0A activation inhibitor soj - Bacillus subtilis ALTERNATE_NAMES forespore chromosome partitioning centromere-like function protein soj; hypothetical protein 4 (replication origin region); probable Spo0J regulation protein soj ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS I40444; S66021; D69709; S18080 REFERENCE I40435 !$#authors Ogasawara, N.; Yoshikawa, H. !$#journal Mol. Microbiol. (1992) 6:629-634 !$#title Genes and their organization in the replication origin !1region of the bacterial chromosome. !$#cross-references MUID:92204018; PMID:1552862 !$#accession I40444 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-253 ##label RES !'##cross-references EMBL:X62539; NID:g40020; PIDN:CAA44408.1; !1PID:g580906 REFERENCE S65967 !$#authors Ogasawara, N.; Nakai, S.; Yoshikawa, H. !$#journal DNA Res. (1994) 1:1-14 !$#title Systematic sequencing of the 180 kilobase region of the !1Bacillus subtilis chromosome containing the replication !1origin. !$#cross-references MUID:96051385; PMID:7584024 !$#accession S66021 !'##status preliminary !'##molecule_type DNA !'##residues 1-253 ##label OGA !'##cross-references EMBL:D26185; NID:g467326; PIDN:BAA05227.1; !1PID:g467381 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D69709 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-253 ##label KUN !'##cross-references GB:Z99124; GB:AL009126; NID:g2636442; !1PIDN:CAB16134.1; PID:g2636644 !'##experimental_source strain 168 GENETICS !$#gene soj !$#start_codon GTG CLASSIFICATION #superfamily regulatory protein spo0J SUMMARY #length 253 #molecular-weight 27543 #checksum 9478 SEQUENCE /// ENTRY S18097 #type complete TITLE regulatory protein spo0J homolog - Pseudomonas putida ORGANISM #formal_name Pseudomonas putida DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S18097 REFERENCE S18071 !$#authors Ogasawara, N.; Yoshikawa, H. !$#submission submitted to the EMBL Data Library, October 1991 !$#description Genes and their organization in replication origin region of !1bacterial chromosome. !$#accession S18097 !'##molecule_type DNA !'##residues 1-263 ##label OGA !'##cross-references EMBL:X62540; NID:g45705; PIDN:CAA44421.1; !1PID:g45713 !'##experimental_source strain TN2100 CLASSIFICATION #superfamily regulatory protein spo0J SUMMARY #length 263 #molecular-weight 28919 #checksum 8840 SEQUENCE /// ENTRY C64662 #type complete TITLE regulatory protein spo0J - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C64662 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession C64662 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-264 ##label TOM !'##cross-references GB:AE000620; GB:AE000511; NID:g2314293; !1PIDN:AAD08185.1; PID:g2314295; TIGR:HP1139 CLASSIFICATION #superfamily regulatory protein spo0J SUMMARY #length 264 #molecular-weight 29171 #checksum 613 SEQUENCE /// ENTRY S62837 #type complete TITLE protein soj homolog K05_orf270 - Mycoplasma pneumoniae (strain ATCC 29342) ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Dec-1999 ACCESSIONS S62837; S73480 REFERENCE S62797 !$#authors Hilbert, H.; Himmelreich, R.; Plagens, H.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:628-639 !$#title Sequence analysis of 56 kb from the genome of the bacterium !1Mycoplasma pneumoniae comprising the dnaA region, the atp !1operon and a cluster of ribosomal protein genes. !$#cross-references MUID:96177562; PMID:8604303 !$#accession S62837 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-270 ##label HIL !'##cross-references EMBL:U34816; NID:g1209514; PIDN:AAC43646.1; !1PID:g1209518 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1995 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73480 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-270 ##label HIM !'##cross-references EMBL:AE000017; GB:U00089; NID:g1673812; !1PIDN:AAB95802.1; PID:g1673815 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily regulatory protein spo0J SUMMARY #length 270 #molecular-weight 30081 #checksum 4625 SEQUENCE /// ENTRY BWAG6B #type complete TITLE T-6b protein - Agrobacterium tumefaciens plasmid pTiTm-4 ORGANISM #formal_name Agrobacterium tumefaciens DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jul-1999 ACCESSIONS S15451 REFERENCE S15450 !$#authors Bonnard, G.; Vincent, F.; Otten, L. !$#submission submitted to the EMBL Data Library, December 1990 !$#accession S15451 !'##molecule_type DNA !'##residues 1-207 ##label BON !'##cross-references EMBL:X56185; NID:g39133; PIDN:CAA39648.1; !1PID:g39136 GENETICS !$#gene T-6b !$#genome plasmid CLASSIFICATION #superfamily T-6b protein SUMMARY #length 207 #molecular-weight 22964 #checksum 5994 SEQUENCE /// ENTRY QQAG7T #type complete TITLE T-6b protein - Agrobacterium tumefaciens plasmid ORGANISM #formal_name Agrobacterium tumefaciens DATE 13-Aug-1986 #sequence_revision 13-Aug-1986 #text_change 12-Apr-1996 ACCESSIONS A04499; JQ0388 REFERENCE A91001 !$#authors Gielen, J.; De Beuckeleer, M.; Seurinck, J.; Deboeck, F.; De !1Greve, H.; Lemmers, M.; Van Montagu, M.; Schell, J. !$#journal EMBO J. (1984) 3:835-846 !$#title The complete nucleotide sequence of the TL-DNA of the !1Agrobacterium tumefaciens plasmid pTiAch5. !$#cross-references MUID:84207942; PMID:6327292 !$#accession A04499 !'##molecule_type DNA !'##residues 1-207 ##label GIE !'##experimental_source plasmid pTiAch5 REFERENCE JQ0388 !$#authors Spanier, K.; Schell, J.; Schreier, P.H. !$#journal Mol. Gen. Genet. (1989) 219:209-216 !$#title A functional analysis of T-DNA gene 6b: the fine tuning of !1cytokinin effects on shoot development. !$#cross-references MUID:90136509; PMID:2615760 !$#accession JQ0388 !'##molecule_type DNA !'##residues 1-118 ##label SPA !'##note Agrobacterium tumefaciens cause crown gall tumor, a neoplastic !1disease of many dicotyledonous plants GENETICS !$#gene 6b !$#genome plasmid FUNCTION !$#description reduces cytokinin activity within plant cells CLASSIFICATION #superfamily T-6b protein KEYWORDS crown gall tumor SUMMARY #length 207 #molecular-weight 23451 #checksum 4421 SEQUENCE /// ENTRY QQAG6T #type complete TITLE hypothetical protein 6 - Agrobacterium tumefaciens plasmids ORGANISM #formal_name Agrobacterium tumefaciens DATE 13-Aug-1986 #sequence_revision 13-Aug-1986 #text_change 16-Jul-1999 ACCESSIONS A04498; S28691 REFERENCE A91001 !$#authors Gielen, J.; De Beuckeleer, M.; Seurinck, J.; Deboeck, F.; De !1Greve, H.; Lemmers, M.; Van Montagu, M.; Schell, J. !$#journal EMBO J. (1984) 3:835-846 !$#title The complete nucleotide sequence of the TL-DNA of the !1Agrobacterium tumefaciens plasmid pTiAch5. !$#cross-references MUID:84207942; PMID:6327292 !$#accession A04498 !'##molecule_type DNA !'##residues 1-191 ##label GIE !'##cross-references GB:X00493; GB:J05108; GB:X00282; NID:g39062; !1PIDN:CAA25171.1; PID:g39071 !'##experimental_source plasmid pTiAch5 REFERENCE S28683 !$#authors Barker, R.F.; Idler, K.B.; Thompson, D.V.; Kemp, J.D. !$#journal Plant Mol. Biol. (1983) 2:335-350 !$#title Nucleotide sequence of the T-DNA region from the !1Agrobacterium tumefaciens octopine Ti plasmid pTi15955. !$#accession S28691 !'##status translation not shown !'##molecule_type DNA !'##residues 1-191 ##label BAR !'##cross-references EMBL:X00493; NID:g39062; PIDN:CAA25171.1; !1PID:g39071 !'##experimental_source plasmid pTi15955 GENETICS !$#genome plasmid CLASSIFICATION #superfamily T-6b protein KEYWORDS crown gall tumor SUMMARY #length 191 #molecular-weight 21466 #checksum 4198 SEQUENCE /// ENTRY S11872 #type complete TITLE rolB protein - Agrobacterium rhizogenes plasmid Ri ORGANISM #formal_name Agrobacterium rhizogenes DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S11872; S06065 REFERENCE S11872 !$#authors Bouchez, D.; Camilleri, C. !$#journal Plant Mol. Biol. (1990) 14:617-619 !$#title Identification of a putative rol B gene on the TR-DNA of the !1Agrobacterium rhizogenes A4 Ri plasmid. !$#cross-references MUID:91346650; PMID:2102840 !$#accession S11872 !'##status preliminary !'##molecule_type DNA !'##residues 1-274 ##label BOU !'##cross-references EMBL:X15952; NID:g38971; PIDN:CAA34076.1; !1PID:g38972 !'##note it is uncertain whether Met-1 or Met-15 is the initiator GENETICS !$#gene rolB !$#genome plasmid CLASSIFICATION #superfamily rolB protein SUMMARY #length 274 #molecular-weight 31253 #checksum 6408 SEQUENCE /// ENTRY C27259 #type complete TITLE hypothetical rolB protein - tree tobacco ORGANISM #formal_name Nicotiana glauca #common_name tree tobacco DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C27259 REFERENCE A93375 !$#authors Furner, I.J.; Huffman, G.A.; Amasino, R.M.; Garfinkel, D.J.; !1Gordon, M.P.; Nester, E.W. !$#journal Nature (1986) 319:422-427 !$#title An Agrobacterium transformation in the evolution of the !1genus Nicotiana. !$#accession C27259 !'##molecule_type DNA !'##residues 1-211 ##label FUR CLASSIFICATION #superfamily rolB protein SUMMARY #length 211 #molecular-weight 24861 #checksum 3050 SEQUENCE /// ENTRY B1AG55 #type complete TITLE virB1 protein precursor - Agrobacterium tumefaciens plasmids pTi15955 and pTiA6 ORGANISM #formal_name Agrobacterium tumefaciens DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS S00777; A28621; A27127 REFERENCE S00777 !$#authors Thompson, D.V.; Melchers, L.S.; Idler, K.B.; Schilperoort, !1R.A.; Hooykaas, P.J.J. !$#journal Nucleic Acids Res. (1988) 16:4621-4636 !$#title Analysis of the complete nucleotide sequence of the !1Agrobacterium tumefaciens virB operon. !$#cross-references MUID:88247765; PMID:2837739 !$#accession S00777 !'##molecule_type DNA !'##residues 1-239 ##label THO !'##cross-references EMBL:X06826; NID:g39195; PIDN:CAA29972.1; !1PID:g39196 !'##experimental_source strain 15955, plasmid pTi15955 REFERENCE A28621 !$#authors Ward, J.E.; Akiyoshi, D.E.; Regier, D.; Datta, A.; Gordon, !1M.P.; Nester, E.W. !$#journal J. Biol. Chem. (1988) 263:5804-5814 !$#title Characterization of the virB operon from an Agrobacterium !1tumefaciens Ti plasmid. !$#cross-references MUID:88186901; PMID:3281947 !$#accession A28621 !'##molecule_type DNA !'##residues 1-239 ##label WAR !'##cross-references GB:J03216; NID:g1196971; PIDN:AAA88645.1; !1PID:g1196972 !'##experimental_source plasmid pTiA6 GENETICS !$#genome plasmid CLASSIFICATION #superfamily tumor-inducing plasmid pTiC58 virB1 protein FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-239 #product virB1 protein #status predicted #label MAT SUMMARY #length 239 #molecular-weight 25952 #checksum 8289 SEQUENCE /// ENTRY B1AG58 #type complete TITLE virB1 protein precursor - Agrobacterium tumefaciens plasmid pTiC58 ORGANISM #formal_name Agrobacterium tumefaciens DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS S12341; S11826; S10516 REFERENCE S12341 !$#authors Shirasu, K.; Morel, P.; Kado, C.I. !$#journal Mol. Microbiol. (1990) 4:1153-1163 !$#title Characterization of the virB operon of an Agrobacterium !1tumefaciens Ti plasmid: nucleotide sequence and protein !1analysis. !$#cross-references MUID:91041724; PMID:2233252 !$#accession S12341 !'##molecule_type DNA !'##residues 1-245 ##label SHI !'##cross-references EMBL:J03320; NID:g154781; PIDN:AAA91591.1; !1PID:g154783 REFERENCE S11825 !$#authors Rogowsky, P.M.; Powell, B.S.; Shirasu, K.; Lin, T.S.; Morel, !1P.; Zyprian, E.M.; Steck, T.R.; Kado, C.I. !$#journal Plasmid (1990) 23:85-106 !$#title Molecular characterization of the vir regulon of !1Agrobacterium tumefaciens: complete nucleotide sequence and !1gene organization of the 28.63-kbp regulon cloned as a !1single unit. !$#cross-references MUID:90301800; PMID:2194232 !$#accession S11826 !'##status translation not shown !'##molecule_type DNA !'##residues 1-245 ##label ROG !'##cross-references EMBL:J03320; NID:g154781; PIDN:AAA91591.1; !1PID:g154783 REFERENCE S10516 !$#authors Kuldau, G.A.; de Vos, G.; Owen, J.; McCaffrey, G.; !1Zambryski, P. !$#journal Mol. Gen. Genet. (1990) 221:256-266 !$#title The virB operon of Agrobacterium tumefaciens pTiC58 encodes !111 open reading frames. !$#cross-references MUID:90318324; PMID:2370849 !$#accession S10516 !'##molecule_type DNA !'##residues 1-17,'P',19-84,'R',86-245 ##label KUL !'##cross-references EMBL:X53264 GENETICS !$#gene virB1 !$#genome plasmid CLASSIFICATION #superfamily tumor-inducing plasmid pTiC58 virB1 protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-245 #product virB1 protein #status predicted #label MAT SUMMARY #length 245 #molecular-weight 26038 #checksum 3185 SEQUENCE /// ENTRY B2AG55 #type complete TITLE virB2 protein precursor - Agrobacterium tumefaciens plasmid pTi15955 ORGANISM #formal_name Agrobacterium tumefaciens DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS S00778 REFERENCE S00777 !$#authors Thompson, D.V.; Melchers, L.S.; Idler, K.B.; Schilperoort, !1R.A.; Hooykaas, P.J.J. !$#journal Nucleic Acids Res. (1988) 16:4621-4636 !$#title Analysis of the complete nucleotide sequence of the !1Agrobacterium tumefaciens virB operon. !$#cross-references MUID:88247765; PMID:2837739 !$#accession S00778 !'##molecule_type DNA !'##residues 1-121 ##label THO !'##cross-references EMBL:X06826; NID:g39195; PIDN:CAA29973.1; !1PID:g39199 GENETICS !$#genome plasmid CLASSIFICATION #superfamily tumor-inducing plasmid pTiC58 virB2 protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-121 #product virB2 protein #status predicted #label MAT SUMMARY #length 121 #molecular-weight 12288 #checksum 9646 SEQUENCE /// ENTRY B2AGA6 #type complete TITLE virB2 protein - Agrobacterium tumefaciens plasmid pTiA6 ORGANISM #formal_name Agrobacterium tumefaciens DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS B28621; B27127 REFERENCE A28621 !$#authors Ward, J.E.; Akiyoshi, D.E.; Regier, D.; Datta, A.; Gordon, !1M.P.; Nester, E.W. !$#journal J. Biol. Chem. (1988) 263:5804-5814 !$#title Characterization of the virB operon from an Agrobacterium !1tumefaciens Ti plasmid. !$#cross-references MUID:88186901; PMID:3281947 !$#accession B28621 !'##molecule_type DNA !'##residues 1-121 ##label WAR !'##cross-references GB:J03216; NID:g1196971; PIDN:AAA88646.1; !1PID:g1196973 GENETICS !$#genome plasmid CLASSIFICATION #superfamily tumor-inducing plasmid pTiC58 virB2 protein SUMMARY #length 121 #molecular-weight 12373 #checksum 241 SEQUENCE /// ENTRY B2AG58 #type complete TITLE virB2 protein precursor - Agrobacterium tumefaciens plasmid pTiC58 ORGANISM #formal_name Agrobacterium tumefaciens DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS S12342; S11827; S10517 REFERENCE S12341 !$#authors Shirasu, K.; Morel, P.; Kado, C.I. !$#journal Mol. Microbiol. (1990) 4:1153-1163 !$#title Characterization of the virB operon of an Agrobacterium !1tumefaciens Ti plasmid: nucleotide sequence and protein !1analysis. !$#cross-references MUID:91041724; PMID:2233252 !$#accession S12342 !'##molecule_type DNA !'##residues 1-121 ##label SHI !'##cross-references EMBL:J03320; NID:g154781; PIDN:AAA91592.1; !1PID:g154784 REFERENCE S11825 !$#authors Rogowsky, P.M.; Powell, B.S.; Shirasu, K.; Lin, T.S.; Morel, !1P.; Zyprian, E.M.; Steck, T.R.; Kado, C.I. !$#journal Plasmid (1990) 23:85-106 !$#title Molecular characterization of the vir regulon of !1Agrobacterium tumefaciens: complete nucleotide sequence and !1gene organization of the 28.63-kbp regulon cloned as a !1single unit. !$#cross-references MUID:90301800; PMID:2194232 !$#accession S11827 !'##status translation not shown !'##molecule_type DNA !'##residues 1-121 ##label ROG !'##cross-references EMBL:J03320; NID:g154781; PIDN:AAA91592.1; !1PID:g154784 REFERENCE S10516 !$#authors Kuldau, G.A.; de Vos, G.; Owen, J.; McCaffrey, G.; !1Zambryski, P. !$#journal Mol. Gen. Genet. (1990) 221:256-266 !$#title The virB operon of Agrobacterium tumefaciens pTiC58 encodes !111 open reading frames. !$#cross-references MUID:90318324; PMID:2370849 !$#accession S10517 !'##molecule_type DNA !'##residues 1-121 ##label KUL !'##cross-references EMBL:X53264; NID:g39152; PIDN:CAA37355.1; !1PID:g39154 GENETICS !$#gene virB2 !$#genome plasmid CLASSIFICATION #superfamily tumor-inducing plasmid pTiC58 virB2 protein KEYWORDS crown gall tumor FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-121 #product virB2 protein #status predicted #label MAT SUMMARY #length 121 #molecular-weight 12318 #checksum 1371 SEQUENCE /// ENTRY B3AG55 #type complete TITLE virB3 protein - Agrobacterium tumefaciens plasmids pTi15955 and pTiA6 ORGANISM #formal_name Agrobacterium tumefaciens DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS S00779; C28621; C27127 REFERENCE S00777 !$#authors Thompson, D.V.; Melchers, L.S.; Idler, K.B.; Schilperoort, !1R.A.; Hooykaas, P.J.J. !$#journal Nucleic Acids Res. (1988) 16:4621-4636 !$#title Analysis of the complete nucleotide sequence of the !1Agrobacterium tumefaciens virB operon. !$#cross-references MUID:88247765; PMID:2837739 !$#accession S00779 !'##molecule_type DNA !'##residues 1-108 ##label THO !'##cross-references EMBL:X06826; NID:g39195; PIDN:CAA29974.1; !1PID:g39202 !'##experimental_source strain 15955, plasmid pTi15955 REFERENCE A28621 !$#authors Ward, J.E.; Akiyoshi, D.E.; Regier, D.; Datta, A.; Gordon, !1M.P.; Nester, E.W. !$#journal J. Biol. Chem. (1988) 263:5804-5814 !$#title Characterization of the virB operon from an Agrobacterium !1tumefaciens Ti plasmid. !$#cross-references MUID:88186901; PMID:3281947 !$#accession C28621 !'##molecule_type DNA !'##residues 1-108 ##label WAR !'##cross-references GB:J03216; NID:g1196971; PIDN:AAA88647.1; !1PID:g1196974 !'##experimental_source plasmid pTiA6 GENETICS !$#genome plasmid CLASSIFICATION #superfamily tumor-inducing plasmid pTiC58 virB3 protein SUMMARY #length 108 #molecular-weight 11760 #checksum 60 SEQUENCE /// ENTRY B3AG58 #type complete TITLE virB3 protein - Agrobacterium tumefaciens plasmid pTiC58 ORGANISM #formal_name Agrobacterium tumefaciens DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS S12343; S11828; S10518 REFERENCE S12341 !$#authors Shirasu, K.; Morel, P.; Kado, C.I. !$#journal Mol. Microbiol. (1990) 4:1153-1163 !$#title Characterization of the virB operon of an Agrobacterium !1tumefaciens Ti plasmid: nucleotide sequence and protein !1analysis. !$#cross-references MUID:91041724; PMID:2233252 !$#accession S12343 !'##molecule_type DNA !'##residues 1-108 ##label SHI !'##cross-references EMBL:J03320; NID:g154781; PIDN:AAA91593.1; !1PID:g154785 REFERENCE S11825 !$#authors Rogowsky, P.M.; Powell, B.S.; Shirasu, K.; Lin, T.S.; Morel, !1P.; Zyprian, E.M.; Steck, T.R.; Kado, C.I. !$#journal Plasmid (1990) 23:85-106 !$#title Molecular characterization of the vir regulon of !1Agrobacterium tumefaciens: complete nucleotide sequence and !1gene organization of the 28.63-kbp regulon cloned as a !1single unit. !$#cross-references MUID:90301800; PMID:2194232 !$#accession S11828 !'##status translation not shown !'##molecule_type DNA !'##residues 1-108 ##label ROG !'##cross-references EMBL:J03320; NID:g154781; PIDN:AAA91593.1; !1PID:g154785 REFERENCE S10516 !$#authors Kuldau, G.A.; de Vos, G.; Owen, J.; McCaffrey, G.; !1Zambryski, P. !$#journal Mol. Gen. Genet. (1990) 221:256-266 !$#title The virB operon of Agrobacterium tumefaciens pTiC58 encodes !111 open reading frames. !$#cross-references MUID:90318324; PMID:2370849 !$#accession S10518 !'##molecule_type DNA !'##residues 1-70,'L',72-91,'TL',94-108 ##label KUL !'##cross-references EMBL:X53264; NID:g39152; PIDN:CAA37356.1; !1PID:g39155 GENETICS !$#gene virB3 !$#genome plasmid CLASSIFICATION #superfamily tumor-inducing plasmid pTiC58 virB3 protein SUMMARY #length 108 #molecular-weight 11596 #checksum 9514 SEQUENCE /// ENTRY B4AGA6 #type complete TITLE virB4 protein precursor - Agrobacterium tumefaciens plasmids ALTERNATE_NAMES virB5 protein ORGANISM #formal_name Agrobacterium tumefaciens DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 19-Jan-2001 ACCESSIONS A30402; D28621; E28621; S00781; S00780; D27127; E27127 REFERENCE A30402 !$#authors Ward, J.E.; Akiyoshi, D.E.; Regier, D.; Datta, A.; Gordon, !1M.P.; Nester, E.W. !$#submission submitted to GenBank, December 1989 !$#accession A30402 !'##molecule_type DNA !'##residues 1-789 ##label WAR !'##cross-references GB:J03216 !'##experimental_source plasmid pTiA6 REFERENCE A35737 !$#authors Ward, J.E.; Akiyoshi, D.E.; Regier, D.; Datta, A.; Gordon, !1M.P.; Nester, E.W. !$#journal J. Biol. Chem. (1990) 265:4768 !$#cross-references MUID:90170994; PMID:2307685 !$#contents annotation; erratum REFERENCE A28621 !$#authors Ward, J.E.; Akiyoshi, D.E.; Regier, D.; Datta, A.; Gordon, !1M.P.; Nester, E.W. !$#journal J. Biol. Chem. (1988) 263:5804-5814 !$#title Characterization of the virB operon from an Agrobacterium !1tumefaciens Ti plasmid. !$#cross-references MUID:88186901; PMID:3281947 !$#accession D28621 !'##molecule_type DNA !'##residues 1-189,'RYG' ##label WAR2 !'##cross-references GB:J03216; GB:M14488; GB:M43452; NID:g1196971; !1PIDN:AAA88648.1; PID:g1196975 !$#accession E28621 !'##molecule_type DNA !'##residues 195-562,'RQER',568-789 ##label WAR3 !'##cross-references GB:J03216; GB:M14488; GB:M43452; NID:g1196971; !1PIDN:AAA88649.1; PID:g1196976 !'##experimental_source plasmid pTiA6 !'##note this sequence appeared in this publication as two separate !1reading frames REFERENCE S00777 !$#authors Thompson, D.V.; Melchers, L.S.; Idler, K.B.; Schilperoort, !1R.A.; Hooykaas, P.J.J. !$#journal Nucleic Acids Res. (1988) 16:4621-4636 !$#title Analysis of the complete nucleotide sequence of the !1Agrobacterium tumefaciens virB operon. !$#cross-references MUID:88247765; PMID:2837739 !$#accession S00781 !'##molecule_type DNA !'##residues 599-789 ##label THO !'##cross-references EMBL:X06826 !'##experimental_source plasmid pTi15955 !$#accession S00780 !'##molecule_type DNA !'##residues 1-562,'AQERGSNAGAGAMRLVGHLTAKLTK' ##label TH2 !'##cross-references EMBL:X06826 !'##experimental_source plasmid pTi15955 GENETICS !$#genome plasmid CLASSIFICATION #superfamily virB4 protein KEYWORDS crown gall tumor; nucleotide binding; P-loop FEATURE !$1-38 #domain signal sequence #status predicted #label SIG\ !$39-789 #product virB4 protein #status predicted #label MAT\ !$433-440 #region nucleotide-binding motif A (P-loop)\ !$461-466 #region nucleotide-binding motif B SUMMARY #length 789 #molecular-weight 87360 #checksum 2214 SEQUENCE /// ENTRY B4AG58 #type complete TITLE virB4 protein precursor - Agrobacterium tumefaciens plasmid pTiC58 ORGANISM #formal_name Agrobacterium tumefaciens DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 19-Jan-2001 ACCESSIONS S12344; S11829; S10519 REFERENCE S12341 !$#authors Shirasu, K.; Morel, P.; Kado, C.I. !$#journal Mol. Microbiol. (1990) 4:1153-1163 !$#title Characterization of the virB operon of an Agrobacterium !1tumefaciens Ti plasmid: nucleotide sequence and protein !1analysis. !$#cross-references MUID:91041724; PMID:2233252 !$#accession S12344 !'##molecule_type DNA !'##residues 1-788 ##label SHI !'##cross-references EMBL:J03320; NID:g154781; PIDN:AAA91594.1; !1PID:g154786 REFERENCE S11825 !$#authors Rogowsky, P.M.; Powell, B.S.; Shirasu, K.; Lin, T.S.; Morel, !1P.; Zyprian, E.M.; Steck, T.R.; Kado, C.I. !$#journal Plasmid (1990) 23:85-106 !$#title Molecular characterization of the vir regulon of !1Agrobacterium tumefaciens: complete nucleotide sequence and !1gene organization of the 28.63-kbp regulon cloned as a !1single unit. !$#cross-references MUID:90301800; PMID:2194232 !$#accession S11829 !'##status translation not shown !'##molecule_type DNA !'##residues 1-788 ##label ROG !'##cross-references EMBL:J03320; NID:g154781; PIDN:AAA91594.1; !1PID:g154786 REFERENCE S10516 !$#authors Kuldau, G.A.; de Vos, G.; Owen, J.; McCaffrey, G.; !1Zambryski, P. !$#journal Mol. Gen. Genet. (1990) 221:256-266 !$#title The virB operon of Agrobacterium tumefaciens pTiC58 encodes !111 open reading frames. !$#cross-references MUID:90318324; PMID:2370849 !$#accession S10519 !'##molecule_type DNA !'##residues 1-54,'A',56-58,'R',60-248,'R',250-488,'AP',490-525,'E', !1527-611,'A',613-788 ##label KUL !'##cross-references EMBL:X53264 GENETICS !$#gene virB4 !$#genome plasmid CLASSIFICATION #superfamily virB4 protein KEYWORDS nucleotide binding; P-loop FEATURE !$1-38 #domain signal sequence #status predicted #label SIG\ !$39-788 #product virB4 protein #status predicted #label MAT\ !$433-440 #region nucleotide-binding motif A (P-loop)\ !$461-466 #region nucleotide-binding motif B SUMMARY #length 788 #molecular-weight 87435 #checksum 3191 SEQUENCE /// ENTRY B6AG55 #type complete TITLE virB5 protein precursor - Agrobacterium tumefaciens plasmids pTi15955 and pTiA6 ALTERNATE_NAMES virB6 protein ORGANISM #formal_name Agrobacterium tumefaciens DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS S00782; F28621; F27127 REFERENCE S00777 !$#authors Thompson, D.V.; Melchers, L.S.; Idler, K.B.; Schilperoort, !1R.A.; Hooykaas, P.J.J. !$#journal Nucleic Acids Res. (1988) 16:4621-4636 !$#title Analysis of the complete nucleotide sequence of the !1Agrobacterium tumefaciens virB operon. !$#cross-references MUID:88247765; PMID:2837739 !$#accession S00782 !'##molecule_type DNA !'##residues 1-220 ##label THO !'##cross-references EMBL:X06826; NID:g39195; PIDN:CAA29976.1; !1PID:g39206 !'##experimental_source strain 15955, plasmid pTi15955 REFERENCE A28621 !$#authors Ward, J.E.; Akiyoshi, D.E.; Regier, D.; Datta, A.; Gordon, !1M.P.; Nester, E.W. !$#journal J. Biol. Chem. (1988) 263:5804-5814 !$#title Characterization of the virB operon from an Agrobacterium !1tumefaciens Ti plasmid. !$#cross-references MUID:88186901; PMID:3281947 !$#accession F28621 !'##molecule_type DNA !'##residues 1-220 ##label WAR !'##cross-references GB:J03216; NID:g1196971; PIDN:AAA88650.1; !1PID:g1196977 !'##experimental_source plasmid pTiA6 !'##note the authors translated the codon TTT for residue 25 as Pro !'##note this sequence was designated ORF 6 in this reference REFERENCE A35737 !$#authors Ward, J.E.; Akiyoshi, D.E.; Regier, D.; Datta, A.; Gordon, !1M.P.; Nester, E.W. !$#journal J. Biol. Chem. (1990) 265:4768 !$#cross-references MUID:90170994; PMID:2307685 !$#contents annotation; erratum !$#note this sequence was designated ORF 6 in this reference GENETICS !$#genome plasmid CLASSIFICATION #superfamily tumor-inducing plasmid pTiC58 virB5 protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-220 #product virB6 protein #status predicted #label MAT SUMMARY #length 220 #molecular-weight 23450 #checksum 8932 SEQUENCE /// ENTRY B5AG58 #type complete TITLE virB5 protein precursor - Agrobacterium tumefaciens plasmid pTiC58 ORGANISM #formal_name Agrobacterium tumefaciens DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS S12345; S11830; S10520 REFERENCE S12341 !$#authors Shirasu, K.; Morel, P.; Kado, C.I. !$#journal Mol. Microbiol. (1990) 4:1153-1163 !$#title Characterization of the virB operon of an Agrobacterium !1tumefaciens Ti plasmid: nucleotide sequence and protein !1analysis. !$#cross-references MUID:91041724; PMID:2233252 !$#accession S12345 !'##molecule_type DNA !'##residues 1-220 ##label SHI !'##cross-references EMBL:J03320; NID:g154781; PIDN:AAA91595.1; !1PID:g154787 REFERENCE S11825 !$#authors Rogowsky, P.M.; Powell, B.S.; Shirasu, K.; Lin, T.S.; Morel, !1P.; Zyprian, E.M.; Steck, T.R.; Kado, C.I. !$#journal Plasmid (1990) 23:85-106 !$#title Molecular characterization of the vir regulon of !1Agrobacterium tumefaciens: complete nucleotide sequence and !1gene organization of the 28.63-kbp regulon cloned as a !1single unit. !$#cross-references MUID:90301800; PMID:2194232 !$#accession S11830 !'##status translation not shown !'##molecule_type DNA !'##residues 1-220 ##label ROG !'##cross-references EMBL:J03320; NID:g154781; PIDN:AAA91595.1; !1PID:g154787 REFERENCE S10516 !$#authors Kuldau, G.A.; de Vos, G.; Owen, J.; McCaffrey, G.; !1Zambryski, P. !$#journal Mol. Gen. Genet. (1990) 221:256-266 !$#title The virB operon of Agrobacterium tumefaciens pTiC58 encodes !111 open reading frames. !$#cross-references MUID:90318324; PMID:2370849 !$#accession S10520 !'##molecule_type DNA !'##residues 1-220 ##label KUL !'##cross-references EMBL:X53264; NID:g39152; PIDN:CAA37358.1; !1PID:g39157 GENETICS !$#gene virB5 !$#genome plasmid CLASSIFICATION #superfamily tumor-inducing plasmid pTiC58 virB5 protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-220 #product virB5 protein #status predicted #label MAT SUMMARY #length 220 #molecular-weight 23269 #checksum 9222 SEQUENCE /// ENTRY B7AG55 #type complete TITLE virB6 protein - Agrobacterium tumefaciens plasmid pTi15955 ALTERNATE_NAMES virB7 protein ORGANISM #formal_name Agrobacterium tumefaciens DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS S00783 REFERENCE S00777 !$#authors Thompson, D.V.; Melchers, L.S.; Idler, K.B.; Schilperoort, !1R.A.; Hooykaas, P.J.J. !$#journal Nucleic Acids Res. (1988) 16:4621-4636 !$#title Analysis of the complete nucleotide sequence of the !1Agrobacterium tumefaciens virB operon. !$#cross-references MUID:88247765; PMID:2837739 !$#accession S00783 !'##molecule_type DNA !'##residues 1-295 ##label THO !'##cross-references EMBL:X06826; NID:g39195; PIDN:CAA29977.1; !1PID:g39209 GENETICS !$#genome plasmid CLASSIFICATION #superfamily tumor-inducing plasmid pTiC58 virB6 protein SUMMARY #length 295 #molecular-weight 31771 #checksum 8339 SEQUENCE /// ENTRY B6AGA6 #type complete TITLE virB6 protein - Agrobacterium tumefaciens plasmid pTiA6 ORGANISM #formal_name Agrobacterium tumefaciens DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS G28621; G27127 REFERENCE A28621 !$#authors Ward, J.E.; Akiyoshi, D.E.; Regier, D.; Datta, A.; Gordon, !1M.P.; Nester, E.W. !$#journal J. Biol. Chem. (1988) 263:5804-5814 !$#title Characterization of the virB operon from an Agrobacterium !1tumefaciens Ti plasmid. !$#cross-references MUID:88186901; PMID:3281947 !$#accession G28621 !'##molecule_type DNA !'##residues 1-295 ##label WAR !'##cross-references GB:J03216; NID:g1196971; PIDN:AAA88651.1; !1PID:g1196978 !'##note this sequence was designated ORF 7 in this reference REFERENCE A35737 !$#authors Ward, J.E.; Akiyoshi, D.E.; Regier, D.; Datta, A.; Gordon, !1M.P.; Nester, E.W. !$#journal J. Biol. Chem. (1990) 265:4768 !$#cross-references MUID:90170994; PMID:2307685 !$#contents annotation; erratum GENETICS !$#genome plasmid CLASSIFICATION #superfamily tumor-inducing plasmid pTiC58 virB6 protein SUMMARY #length 295 #molecular-weight 31721 #checksum 7811 SEQUENCE /// ENTRY B6AG58 #type complete TITLE virB6 protein - Agrobacterium tumefaciens plasmid pTiC58 ORGANISM #formal_name Agrobacterium tumefaciens DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS S12346; S11831; S10521 REFERENCE S12341 !$#authors Shirasu, K.; Morel, P.; Kado, C.I. !$#journal Mol. Microbiol. (1990) 4:1153-1163 !$#title Characterization of the virB operon of an Agrobacterium !1tumefaciens Ti plasmid: nucleotide sequence and protein !1analysis. !$#cross-references MUID:91041724; PMID:2233252 !$#accession S12346 !'##molecule_type DNA !'##residues 1-294 ##label SHI !'##cross-references EMBL:J03320; NID:g154781; PIDN:AAA91596.1; !1PID:g154788 REFERENCE S11825 !$#authors Rogowsky, P.M.; Powell, B.S.; Shirasu, K.; Lin, T.S.; Morel, !1P.; Zyprian, E.M.; Steck, T.R.; Kado, C.I. !$#journal Plasmid (1990) 23:85-106 !$#title Molecular characterization of the vir regulon of !1Agrobacterium tumefaciens: complete nucleotide sequence and !1gene organization of the 28.63-kbp regulon cloned as a !1single unit. !$#cross-references MUID:90301800; PMID:2194232 !$#accession S11831 !'##status translation not shown !'##molecule_type DNA !'##residues 1-294 ##label ROG !'##cross-references EMBL:J03320; NID:g154781; PIDN:AAA91596.1; !1PID:g154788 REFERENCE S10516 !$#authors Kuldau, G.A.; de Vos, G.; Owen, J.; McCaffrey, G.; !1Zambryski, P. !$#journal Mol. Gen. Genet. (1990) 221:256-266 !$#title The virB operon of Agrobacterium tumefaciens pTiC58 encodes !111 open reading frames. !$#cross-references MUID:90318324; PMID:2370849 !$#accession S10521 !'##molecule_type DNA !'##residues 1-267,'G',268-294 ##label KUL !'##cross-references EMBL:X53264; NID:g39152; PIDN:CAA37359.1; !1PID:g39158 GENETICS !$#gene virB6 !$#genome plasmid CLASSIFICATION #superfamily tumor-inducing plasmid pTiC58 virB6 protein SUMMARY #length 294 #molecular-weight 31803 #checksum 6124 SEQUENCE /// ENTRY B7AGA6 #type complete TITLE virB7 protein - Agrobacterium tumefaciens plasmid pTiA6 ORGANISM #formal_name Agrobacterium tumefaciens DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 03-Feb-1994 ACCESSIONS H28621; H27127 REFERENCE A28621 !$#authors Ward, J.E.; Akiyoshi, D.E.; Regier, D.; Datta, A.; Gordon, !1M.P.; Nester, E.W. !$#journal J. Biol. Chem. (1988) 263:5804-5814 !$#title Characterization of the virB operon from an Agrobacterium !1tumefaciens Ti plasmid. !$#cross-references MUID:88186901; PMID:3281947 !$#accession H28621 !'##molecule_type DNA !'##residues 1-55 ##label WAR !'##cross-references GB:J03216 !'##note this sequence was designated ORF 8 in this reference REFERENCE A35737 !$#authors Ward, J.E.; Akiyoshi, D.E.; Regier, D.; Datta, A.; Gordon, !1M.P.; Nester, E.W. !$#journal J. Biol. Chem. (1990) 265:4768 !$#cross-references MUID:90170994; PMID:2307685 !$#contents annotation; erratum GENETICS !$#genome plasmid CLASSIFICATION #superfamily tumor-inducing plasmid pTiC58 virB7 protein SUMMARY #length 55 #molecular-weight 5930 #checksum 8353 SEQUENCE /// ENTRY B7AG58 #type complete TITLE virB7 protein precursor - Agrobacterium tumefaciens plasmid pTiC58 ORGANISM #formal_name Agrobacterium tumefaciens DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS S12347; S11832; S10522 REFERENCE S12341 !$#authors Shirasu, K.; Morel, P.; Kado, C.I. !$#journal Mol. Microbiol. (1990) 4:1153-1163 !$#title Characterization of the virB operon of an Agrobacterium !1tumefaciens Ti plasmid: nucleotide sequence and protein !1analysis. !$#cross-references MUID:91041724; PMID:2233252 !$#accession S12347 !'##molecule_type DNA !'##residues 1-55 ##label SHI !'##cross-references EMBL:J03320; NID:g154781; PIDN:AAA91597.1; !1PID:g154789 REFERENCE S11825 !$#authors Rogowsky, P.M.; Powell, B.S.; Shirasu, K.; Lin, T.S.; Morel, !1P.; Zyprian, E.M.; Steck, T.R.; Kado, C.I. !$#journal Plasmid (1990) 23:85-106 !$#title Molecular characterization of the vir regulon of !1Agrobacterium tumefaciens: complete nucleotide sequence and !1gene organization of the 28.63-kbp regulon cloned as a !1single unit. !$#cross-references MUID:90301800; PMID:2194232 !$#accession S11832 !'##status translation not shown !'##molecule_type DNA !'##residues 1-55 ##label ROG !'##cross-references EMBL:J03320; NID:g154781; PIDN:AAA91597.1; !1PID:g154789 REFERENCE S10516 !$#authors Kuldau, G.A.; de Vos, G.; Owen, J.; McCaffrey, G.; !1Zambryski, P. !$#journal Mol. Gen. Genet. (1990) 221:256-266 !$#title The virB operon of Agrobacterium tumefaciens pTiC58 encodes !111 open reading frames. !$#cross-references MUID:90318324; PMID:2370849 !$#accession S10522 !'##molecule_type DNA !'##residues 1-12,'G',14-55 ##label KUL !'##cross-references EMBL:X53264; NID:g39152; PIDN:CAA37360.1; !1PID:g39159 GENETICS !$#gene virB7 !$#genome plasmid CLASSIFICATION #superfamily tumor-inducing plasmid pTiC58 virB7 protein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-55 #product virB7 protein #status predicted #label MAT SUMMARY #length 55 #molecular-weight 5902 #checksum 8461 SEQUENCE /// ENTRY B8AG55 #type complete TITLE virB8 protein precursor - Agrobacterium tumefaciens plasmid pTi15955 ORGANISM #formal_name Agrobacterium tumefaciens DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS S00784 REFERENCE S00777 !$#authors Thompson, D.V.; Melchers, L.S.; Idler, K.B.; Schilperoort, !1R.A.; Hooykaas, P.J.J. !$#journal Nucleic Acids Res. (1988) 16:4621-4636 !$#title Analysis of the complete nucleotide sequence of the !1Agrobacterium tumefaciens virB operon. !$#cross-references MUID:88247765; PMID:2837739 !$#accession S00784 !'##molecule_type DNA !'##residues 1-257 ##label THO !'##cross-references EMBL:X06826; NID:g39195; PIDN:CAA29978.1; !1PID:g39210 GENETICS !$#genome plasmid CLASSIFICATION #superfamily tumor-inducing plasmid pTiC58 virB8 protein FEATURE !$1-36 #domain signal sequence #status predicted #label SIG\ !$37-257 #product virB8 protein #status predicted #label MAT SUMMARY #length 257 #molecular-weight 28362 #checksum 173 SEQUENCE /// ENTRY B8AGA6 #type complete TITLE virB8 protein - Agrobacterium tumefaciens plasmid pTiA6 ORGANISM #formal_name Agrobacterium tumefaciens DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 03-Feb-1994 ACCESSIONS I28621; I27127 REFERENCE A28621 !$#authors Ward, J.E.; Akiyoshi, D.E.; Regier, D.; Datta, A.; Gordon, !1M.P.; Nester, E.W. !$#journal J. Biol. Chem. (1988) 263:5804-5814 !$#title Characterization of the virB operon from an Agrobacterium !1tumefaciens Ti plasmid. !$#cross-references MUID:88186901; PMID:3281947 !$#accession I28621 !'##molecule_type DNA !'##residues 1-230 ##label WAR !'##cross-references GB:J03216 !'##note this sequence was designated ORF 9 in this reference REFERENCE A35737 !$#authors Ward, J.E.; Akiyoshi, D.E.; Regier, D.; Datta, A.; Gordon, !1M.P.; Nester, E.W. !$#journal J. Biol. Chem. (1990) 265:4768 !$#cross-references MUID:90170994; PMID:2307685 !$#contents annotation; erratum GENETICS !$#genome plasmid CLASSIFICATION #superfamily tumor-inducing plasmid pTiC58 virB8 protein SUMMARY #length 230 #molecular-weight 25382 #checksum 2646 SEQUENCE /// ENTRY B8AG58 #type complete TITLE virB8 protein - Agrobacterium tumefaciens plasmid pTiC58 ORGANISM #formal_name Agrobacterium tumefaciens DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS S12348; S11833; S10523 REFERENCE S12341 !$#authors Shirasu, K.; Morel, P.; Kado, C.I. !$#journal Mol. Microbiol. (1990) 4:1153-1163 !$#title Characterization of the virB operon of an Agrobacterium !1tumefaciens Ti plasmid: nucleotide sequence and protein !1analysis. !$#cross-references MUID:91041724; PMID:2233252 !$#accession S12348 !'##molecule_type DNA !'##residues 1-237 ##label SHI !'##cross-references EMBL:J03320; NID:g154781; PIDN:AAA91598.1; !1PID:g154790 REFERENCE S11825 !$#authors Rogowsky, P.M.; Powell, B.S.; Shirasu, K.; Lin, T.S.; Morel, !1P.; Zyprian, E.M.; Steck, T.R.; Kado, C.I. !$#journal Plasmid (1990) 23:85-106 !$#title Molecular characterization of the vir regulon of !1Agrobacterium tumefaciens: complete nucleotide sequence and !1gene organization of the 28.63-kbp regulon cloned as a !1single unit. !$#cross-references MUID:90301800; PMID:2194232 !$#accession S11833 !'##status translation not shown !'##molecule_type DNA !'##residues 1-237 ##label ROG !'##cross-references EMBL:J03320; NID:g154781; PIDN:AAA91598.1; !1PID:g154790 REFERENCE S10516 !$#authors Kuldau, G.A.; de Vos, G.; Owen, J.; McCaffrey, G.; !1Zambryski, P. !$#journal Mol. Gen. Genet. (1990) 221:256-266 !$#title The virB operon of Agrobacterium tumefaciens pTiC58 encodes !111 open reading frames. !$#cross-references MUID:90318324; PMID:2370849 !$#accession S10523 !'##molecule_type DNA !'##residues 1-20,23-127,'SA',130-237 ##label KUL !'##cross-references EMBL:X53264; NID:g39152; PIDN:CAA37361.1; !1PID:g39160 GENETICS !$#gene virB8 !$#genome plasmid CLASSIFICATION #superfamily tumor-inducing plasmid pTiC58 virB8 protein SUMMARY #length 237 #molecular-weight 26393 #checksum 6263 SEQUENCE /// ENTRY B9AG55 #type complete TITLE virB9 protein precursor - Agrobacterium tumefaciens plasmids pTi15955 and pTiA6 ORGANISM #formal_name Agrobacterium tumefaciens DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS S00785; B30402; A27647; A35737; A26217 REFERENCE S00777 !$#authors Thompson, D.V.; Melchers, L.S.; Idler, K.B.; Schilperoort, !1R.A.; Hooykaas, P.J.J. !$#journal Nucleic Acids Res. (1988) 16:4621-4636 !$#title Analysis of the complete nucleotide sequence of the !1Agrobacterium tumefaciens virB operon. !$#cross-references MUID:88247765; PMID:2837739 !$#accession S00785 !'##molecule_type DNA !'##residues 1-293 ##label THO !'##cross-references EMBL:X06826; NID:g39195; PIDN:CAA29979.1; !1PID:g757730 !'##experimental_source strain 15955, plasmid pTi15955 REFERENCE A30402 !$#authors Ward, J.E.; Akiyoshi, D.E.; Regier, D.; Datta, A.; Gordon, !1M.P.; Nester, E.W. !$#submission submitted to GenBank, December 1989 !$#accession B30402 !'##molecule_type DNA !'##residues 1-293 ##label WAR !'##cross-references GB:J03216; NID:g1196971; PIDN:AAA88654.1; !1PID:g1196981 !'##experimental_source plasmid pTiA6 REFERENCE A28621 !$#authors Ward, J.E.; Akiyoshi, D.E.; Regier, D.; Datta, A.; Gordon, !1M.P.; Nester, E.W. !$#journal J. Biol. Chem. (1988) 263:5804-5814 !$#title Characterization of the virB operon from an Agrobacterium !1tumefaciens Ti plasmid. !$#cross-references MUID:88186901; PMID:3281947 !$#accession A27647 !'##molecule_type DNA !'##residues 1-271 ##label WA2 !'##cross-references GB:J03216 !'##experimental_source plasmid pTiA6 !'##note this sequence was designated the amino-terminal portion of ORF !110 in this reference REFERENCE A35737 !$#authors Ward, J.E.; Akiyoshi, D.E.; Regier, D.; Datta, A.; Gordon, !1M.P.; Nester, E.W. !$#journal J. Biol. Chem. (1990) 265:4768 !$#cross-references MUID:90170994; PMID:2307685 !$#contents erratum !$#accession A35737 !'##molecule_type DNA !'##residues 97-293 ##label WA3 !'##experimental_source plasmid pTiA6 GENETICS !$#genome plasmid CLASSIFICATION #superfamily tumor-inducing plasmid pTiC58 virB9 protein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-293 #product virB9 protein #status predicted #label MAT SUMMARY #length 293 #molecular-weight 32172 #checksum 543 SEQUENCE /// ENTRY B9AG58 #type complete TITLE virB9 protein precursor - Agrobacterium tumefaciens plasmid pTiC58 ORGANISM #formal_name Agrobacterium tumefaciens DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS S12349; S11834; S10524 REFERENCE S12341 !$#authors Shirasu, K.; Morel, P.; Kado, C.I. !$#journal Mol. Microbiol. (1990) 4:1153-1163 !$#title Characterization of the virB operon of an Agrobacterium !1tumefaciens Ti plasmid: nucleotide sequence and protein !1analysis. !$#cross-references MUID:91041724; PMID:2233252 !$#accession S12349 !'##molecule_type DNA !'##residues 1-293 ##label SHI !'##cross-references EMBL:J03320; NID:g154781; PIDN:AAA91599.1; !1PID:g154791 REFERENCE S11825 !$#authors Rogowsky, P.M.; Powell, B.S.; Shirasu, K.; Lin, T.S.; Morel, !1P.; Zyprian, E.M.; Steck, T.R.; Kado, C.I. !$#journal Plasmid (1990) 23:85-106 !$#title Molecular characterization of the vir regulon of !1Agrobacterium tumefaciens: complete nucleotide sequence and !1gene organization of the 28.63-kbp regulon cloned as a !1single unit. !$#cross-references MUID:90301800; PMID:2194232 !$#accession S11834 !'##status translation not shown !'##molecule_type DNA !'##residues 1-293 ##label ROG !'##cross-references EMBL:J03320; NID:g154781; PIDN:AAA91599.1; !1PID:g154791 REFERENCE S10516 !$#authors Kuldau, G.A.; de Vos, G.; Owen, J.; McCaffrey, G.; !1Zambryski, P. !$#journal Mol. Gen. Genet. (1990) 221:256-266 !$#title The virB operon of Agrobacterium tumefaciens pTiC58 encodes !111 open reading frames. !$#cross-references MUID:90318324; PMID:2370849 !$#accession S10524 !'##molecule_type DNA !'##residues 1-155,'R',157-293 ##label KUL !'##cross-references EMBL:X53264 GENETICS !$#gene virB9 !$#genome plasmid CLASSIFICATION #superfamily tumor-inducing plasmid pTiC58 virB9 protein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-293 #product virB9 protein #status predicted #label MAT SUMMARY #length 293 #molecular-weight 32141 #checksum 8937 SEQUENCE /// ENTRY B0AG55 #type complete TITLE virB10 protein - Agrobacterium tumefaciens plasmids ORGANISM #formal_name Agrobacterium tumefaciens DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS S00786; A27627; B35737; A26217; C30402 REFERENCE S00777 !$#authors Thompson, D.V.; Melchers, L.S.; Idler, K.B.; Schilperoort, !1R.A.; Hooykaas, P.J.J. !$#journal Nucleic Acids Res. (1988) 16:4621-4636 !$#title Analysis of the complete nucleotide sequence of the !1Agrobacterium tumefaciens virB operon. !$#cross-references MUID:88247765; PMID:2837739 !$#accession S00786 !'##molecule_type DNA !'##residues 1-409 ##label THO !'##cross-references EMBL:X06826; NID:g39195; PIDN:CAA29980.1; !1PID:g757731 !'##experimental_source plasmid pTi15955 !'##note it is uncertain whether Met-1 or Met-33 is the initiator REFERENCE A28621 !$#authors Ward, J.E.; Akiyoshi, D.E.; Regier, D.; Datta, A.; Gordon, !1M.P.; Nester, E.W. !$#journal J. Biol. Chem. (1988) 263:5804-5814 !$#title Characterization of the virB operon from an Agrobacterium !1tumefaciens Ti plasmid. !$#cross-references MUID:88186901; PMID:3281947 !$#accession A27627 !'##molecule_type DNA !'##residues 33-409 ##label WA2 !'##cross-references GB:J03216 !'##experimental_source plasmid pTiA6 !'##note this sequence was designated the carboxyl-terminal portion of !1ORF 10 in this reference REFERENCE A35737 !$#authors Ward, J.E.; Akiyoshi, D.E.; Regier, D.; Datta, A.; Gordon, !1M.P.; Nester, E.W. !$#journal J. Biol. Chem. (1990) 265:4768 !$#cross-references MUID:90170994; PMID:2307685 !$#contents erratum !$#accession B35737 !'##molecule_type DNA !'##residues 33-215 ##label WA1 !'##experimental_source plasmid pTiA6 GENETICS !$#genome plasmid CLASSIFICATION #superfamily tumor-inducing plasmid pTiC58 virB10 protein SUMMARY #length 409 #molecular-weight 44364 #checksum 8153 SEQUENCE /// ENTRY B0AG58 #type complete TITLE virB10 protein - Agrobacterium tumefaciens plasmid pTiC58 ORGANISM #formal_name Agrobacterium tumefaciens DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS S12350; S11835; S10525 REFERENCE S12341 !$#authors Shirasu, K.; Morel, P.; Kado, C.I. !$#journal Mol. Microbiol. (1990) 4:1153-1163 !$#title Characterization of the virB operon of an Agrobacterium !1tumefaciens Ti plasmid: nucleotide sequence and protein !1analysis. !$#cross-references MUID:91041724; PMID:2233252 !$#accession S12350 !'##molecule_type DNA !'##residues 1-377 ##label SHI !'##cross-references EMBL:J03320; NID:g154781; PIDN:AAA91600.1; !1PID:g154792 REFERENCE S11825 !$#authors Rogowsky, P.M.; Powell, B.S.; Shirasu, K.; Lin, T.S.; Morel, !1P.; Zyprian, E.M.; Steck, T.R.; Kado, C.I. !$#journal Plasmid (1990) 23:85-106 !$#title Molecular characterization of the vir regulon of !1Agrobacterium tumefaciens: complete nucleotide sequence and !1gene organization of the 28.63-kbp regulon cloned as a !1single unit. !$#cross-references MUID:90301800; PMID:2194232 !$#accession S11835 !'##status translation not shown !'##molecule_type DNA !'##residues 1-377 ##label ROG !'##cross-references EMBL:J03320; NID:g154781; PIDN:AAA91600.1; !1PID:g154792 REFERENCE S10516 !$#authors Kuldau, G.A.; de Vos, G.; Owen, J.; McCaffrey, G.; !1Zambryski, P. !$#journal Mol. Gen. Genet. (1990) 221:256-266 !$#title The virB operon of Agrobacterium tumefaciens pTiC58 encodes !111 open reading frames. !$#cross-references MUID:90318324; PMID:2370849 !$#accession S10525 !'##molecule_type DNA !'##residues 1-296,'A',298-377 ##label KUL !'##cross-references EMBL:X53264; NID:g39152; PIDN:CAA37363.1; !1PID:g39162 GENETICS !$#gene virB10 !$#genome plasmid CLASSIFICATION #superfamily tumor-inducing plasmid pTiC58 virB10 protein SUMMARY #length 377 #molecular-weight 40581 #checksum 8868 SEQUENCE /// ENTRY BXAG55 #type complete TITLE virB11 protein - Agrobacterium tumefaciens plasmid pTi15955 and pTiA6 ORGANISM #formal_name Agrobacterium tumefaciens DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS S00787; B27647; B26217 REFERENCE S00777 !$#authors Thompson, D.V.; Melchers, L.S.; Idler, K.B.; Schilperoort, !1R.A.; Hooykaas, P.J.J. !$#journal Nucleic Acids Res. (1988) 16:4621-4636 !$#title Analysis of the complete nucleotide sequence of the !1Agrobacterium tumefaciens virB operon. !$#cross-references MUID:88247765; PMID:2837739 !$#accession S00787 !'##molecule_type DNA !'##residues 1-343 ##label THO !'##cross-references EMBL:X06826; NID:g39195; PIDN:CAA29982.1; !1PID:g757733 !'##experimental_source strain 15955, plasmid pTi15955 REFERENCE A28621 !$#authors Ward, J.E.; Akiyoshi, D.E.; Regier, D.; Datta, A.; Gordon, !1M.P.; Nester, E.W. !$#journal J. Biol. Chem. (1988) 263:5804-5814 !$#title Characterization of the virB operon from an Agrobacterium !1tumefaciens Ti plasmid. !$#cross-references MUID:88186901; PMID:3281947 !$#accession B27647 !'##molecule_type DNA !'##residues 1-343 ##label WAR !'##cross-references GB:J03216 !'##experimental_source plasmid pTiA6 GENETICS !$#genome plasmid CLASSIFICATION #superfamily tumor-inducing plasmid pTiC58 virB11 protein SUMMARY #length 343 #molecular-weight 38008 #checksum 3883 SEQUENCE /// ENTRY BXAG58 #type complete TITLE virB11 protein - Agrobacterium tumefaciens plasmid pTiC58 ORGANISM #formal_name Agrobacterium tumefaciens DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS S12351; S11836; S10526; S10142 REFERENCE S12341 !$#authors Shirasu, K.; Morel, P.; Kado, C.I. !$#journal Mol. Microbiol. (1990) 4:1153-1163 !$#title Characterization of the virB operon of an Agrobacterium !1tumefaciens Ti plasmid: nucleotide sequence and protein !1analysis. !$#cross-references MUID:91041724; PMID:2233252 !$#accession S12351 !'##molecule_type DNA !'##residues 1-344 ##label SHI !'##cross-references EMBL:J03320; NID:g154781; PIDN:AAA91601.1; !1PID:g154793 !'##note the authors translated the codon GCT for residue 136 as Asp REFERENCE S11825 !$#authors Rogowsky, P.M.; Powell, B.S.; Shirasu, K.; Lin, T.S.; Morel, !1P.; Zyprian, E.M.; Steck, T.R.; Kado, C.I. !$#journal Plasmid (1990) 23:85-106 !$#title Molecular characterization of the vir regulon of !1Agrobacterium tumefaciens: complete nucleotide sequence and !1gene organization of the 28.63-kbp regulon cloned as a !1single unit. !$#cross-references MUID:90301800; PMID:2194232 !$#accession S11836 !'##status translation not shown !'##molecule_type DNA !'##residues 1-344 ##label ROG !'##cross-references EMBL:J03320; NID:g154781; PIDN:AAA91601.1; !1PID:g154793 REFERENCE S10516 !$#authors Kuldau, G.A.; de Vos, G.; Owen, J.; McCaffrey, G.; !1Zambryski, P. !$#journal Mol. Gen. Genet. (1990) 221:256-266 !$#title The virB operon of Agrobacterium tumefaciens pTiC58 encodes !111 open reading frames. !$#cross-references MUID:90318324; PMID:2370849 !$#accession S10526 !'##molecule_type DNA !'##residues 1-95 ##label KUL !'##cross-references EMBL:X53264 REFERENCE S03760 !$#authors Powell, B.S.; Powell, G.K.; Morris, R.O.; Rogowsky, P.M.; !1Kado, C.I. !$#journal Mol. Microbiol. (1987) 1:309-316 !$#title Nucleotide sequence of the virG locus of the Agrobacterium !1tumefaciens plasmid pTiC58. !$#cross-references MUID:88201669; PMID:3448462 !$#accession S10142 !'##status translation not shown !'##molecule_type DNA !'##residues 94-344 ##label POW !'##cross-references EMBL:Y00535; NID:g39219; PIDN:CAA68594.1; !1PID:g809650 GENETICS !$#gene virB11 !$#genome plasmid CLASSIFICATION #superfamily tumor-inducing plasmid pTiC58 virB11 protein SUMMARY #length 344 #molecular-weight 38095 #checksum 3788 SEQUENCE /// ENTRY S39643 #type complete TITLE acetate / acetoin utilization protein acuC - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S39643; E69582 REFERENCE S39641 !$#authors Grundy, F.J.; Waters, D.A.; Takova, T.Y.; Henkin, T.M. !$#journal Mol. Microbiol. (1993) 10:259-271 !$#title Identification of genes involved in utilization of acetate !1and acetoin in Bacillus subtilis. !$#cross-references MUID:95020526; PMID:7934817 !$#accession S39643 !'##molecule_type DNA !'##residues 1-387 ##label GRU !'##cross-references GB:L17309; NID:g861173; PIDN:AAA68284.1; !1PID:g348050 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69582 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-387 ##label KUN !'##cross-references GB:Z99119; GB:AL009126; NID:g2635411; !1PIDN:CAB14949.1; PID:g2635455 !'##experimental_source strain 168 GENETICS !$#gene acuC CLASSIFICATION #superfamily acetate utilization protein acuC; RPD3/acuC !1homology FEATURE !$6-312 #domain RPD3/acuC homology #label RAH1 SUMMARY #length 387 #molecular-weight 42990 #checksum 738 SEQUENCE /// ENTRY S22284 #type complete TITLE transcription regulator RPD3 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein N0305; protein YNL330c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 23-Mar-2001 ACCESSIONS S22284; S51336; S51285; S55859; S57393; S63313; S63311 REFERENCE S22284 !$#authors Vidal, M.; Gaber, R.F. !$#journal Mol. Cell. Biol. (1991) 11:6317-6327 !$#title RPD3 encodes a second factor required to achieve maximum !1positive and negative transcriptional states in !1Saccharomyces cerevisiae. !$#cross-references MUID:92049362; PMID:1944291 !$#accession S22284 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-433 ##label VID !'##cross-references GB:S66438; NID:g238961; PIDN:AAB20328.1; !1PID:g238962 REFERENCE S51334 !$#authors van Dyck, L.; Pascual-Ahuir, A.; Goffeau, A. !$#submission submitted to the EMBL Data Library, December 1994 !$#description A 8.2 kb DNA segment from chromosome XIV carries the RPD3 !1and PAS8 genes as well as the Saccharomyces cerevisiae !1homologue of the thiamine-repressed nmt1 gene and a !1chromosome III-duplicated gene for a putative aryl-alcohol !1dehydrogenase. !$#accession S51336 !'##molecule_type DNA !'##residues 1-433 ##label VAN !'##cross-references EMBL:X83226; NID:g642335; PIDN:CAA58228.1; !1PID:g642338 REFERENCE S51285 !$#authors Nicaud, J.J. !$#submission submitted to the EMBL Data Library, January 1995 !$#description Sequence analysis of a 13.9 Kb fragment of yeast chromosome !1XIV identifies the DAL82, RFA2 and MCK1 loci and six new !1ORF. !$#accession S51285 !'##molecule_type DNA !'##residues 1-201 ##label NIC !'##cross-references EMBL:Z46259; NID:g633655; PIDN:CAA86368.1; !1PID:g854536 REFERENCE S55859 !$#authors Maftahi, M.; Nicaud, J.M.; Levesque, H.; Gaillardin, C. !$#journal Yeast (1995) 11:567-572 !$#title Sequencing analysis of a 15.4 kb fragment of yeast !1chromosome XIV identifies the RPD3, PAS8 and KRE1 loci, and !1five new open reading frames. !$#cross-references MUID:95373280; PMID:7645347 !$#accession S55859 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-201 ##label MAF !'##cross-references EMBL:Z46259; NID:g633655; PIDN:CAA86368.1; !1PID:g854536 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1995 REFERENCE S57391 !$#authors van Dyck, L.; Pascual-Ahuir, A.; Purnelle, B.; Goffeau, A. !$#journal Yeast (1995) 11:987-991 !$#title An 8.2 kb DNA segment from chromosome XIV carries the RPD3 !1and PAS8 genes as well as the Saccharomyces cerevisiae !1homologue of the thiamine-repressed nmt1 gene and a !1chromosome III-duplicated gene for a putative aryl-alcohol !1dehydrogenase. !$#cross-references MUID:96021610; PMID:8533474 !$#accession S57393 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-433 ##label VAW !'##cross-references EMBL:X83226; NID:g642335; PIDN:CAA58228.1; !1PID:g642338 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1994 REFERENCE S63151 !$#authors Coster, F.; Jonniaux, J.L.; Goffeau, A.; Purnelle, B.; Van !1Dyck, L. !$#submission submitted to the Protein Sequence Database, April 1996 !$#accession S63313 !'##molecule_type DNA !'##residues 1-433 ##label COS !'##cross-references EMBL:Z71606; NID:g1302450; PIDN:CAA96263.1; !1PID:g1302451; GSPDB:GN00014; MIPS:YNL330c !'##experimental_source strain S288C REFERENCE S63287 !$#authors Maftahi, M.; Nicaud, J.M.; Levesque, H.; Gaillardin, C. !$#submission submitted to the Protein Sequence Database, April 1996 !$#accession S63311 !'##molecule_type DNA !'##residues 1-201 ##label MAW !'##cross-references EMBL:Z71606; GSPDB:GN00014; MIPS:YNL330c !'##experimental_source strain S288C GENETICS !$#gene SGD:RPD3; SDI2; SDS6; MIPS:YNL330c !'##cross-references SGD:S0005274; MIPS:YNL330c !$#map_position 14L FUNCTION !$#description transcription regulation CLASSIFICATION #superfamily RPD3 protein; RPD3/acuC homology KEYWORDS nucleus; transcription regulation FEATURE !$23-322 #domain RPD3/acuC homology #label RAH1 SUMMARY #length 433 #molecular-weight 48904 #checksum 3627 SEQUENCE /// ENTRY S60381 #type complete TITLE RPD3 protein homolog - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S60381; S43160 REFERENCE S60381 !$#authors Ladomery, M.R.; Lyons, S.; Sommerville, J. !$#submission submitted to the EMBL Data Library, December 1994 !$#accession S60381 !'##status preliminary !'##molecule_type mRNA !'##residues 1-480 ##label LAD !'##cross-references EMBL:X78454; NID:g773397; PIDN:CAA55211.1; !1PID:g602098 CLASSIFICATION #superfamily RPD3 protein; RPD3/acuC homology FEATURE !$13-312 #domain RPD3/acuC homology #label RAH1 SUMMARY #length 480 #molecular-weight 54747 #checksum 2787 SEQUENCE /// ENTRY RGBYGI #type complete TITLE regulatory protein ARG80 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YM9532.07; protein YMR042w; regulatory protein ARGRI ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 12-Nov-1999 ACCESSIONS S05822; S52891 REFERENCE S05822 !$#authors Dubois, E.; Bercy, J.; Messenguy, F. !$#journal Mol. Gen. Genet. (1987) 207:142-148 !$#title Characterization of two genes, ARGRI and ARGRIII required !1for specific regulation of arginine metabolism in yeast. !$#cross-references MUID:87257286; PMID:3298999 !$#accession S05822 !'##molecule_type DNA !'##residues 1-177 ##label DUB !'##cross-references EMBL:X05327; NID:g3373; PIDN:CAA28944.1; PID:g3374 !'##note the authors translated the codon CAC for residue 103 as Lys REFERENCE S52885 !$#authors Odell, C.; Bowman, S. !$#submission submitted to the EMBL Data Library, February 1995 !$#accession S52891 !'##molecule_type DNA !'##residues 1-177 ##label ODE !'##cross-references EMBL:Z48502; NID:g695715; PIDN:CAA88408.1; !1PID:g695722; GSPDB:GN00013; MIPS:YMR042w GENETICS !$#gene SGD:ARG80; ARGR1; MIPS:YMR042w !'##cross-references SGD:S0004645; MIPS:YMR042w !$#map_position 13R FUNCTION !$#description required for arginine-dependent activation of CAR1 CLASSIFICATION #superfamily regulatory protein ARGRI; serum response factor !1DNA-binding domain homology KEYWORDS DNA binding; nucleus; transcription regulation FEATURE !$79-134 #domain serum response factor DNA-binding domain !8homology #label SRF SUMMARY #length 177 #molecular-weight 19487 #checksum 617 SEQUENCE /// ENTRY BVBYD1 #type complete TITLE GCD1 protein - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein O5355; protein YOR260w ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1991 #sequence_revision 02-Aug-1996 #text_change 16-Jun-2000 ACCESSIONS S67157; S05727 REFERENCE S67143 !$#authors Jauniaux, J.C.; Poirey, R. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67157 !'##molecule_type DNA !'##residues 1-578 ##label JAU !'##cross-references EMBL:Z75168; NID:g1420586; PIDN:CAA99482.1; !1PID:g1420587; GSPDB:GN00015; MIPS:YOR260w !'##experimental_source strain S288C REFERENCE S05727 !$#authors Hill, D.E.; Struhl, K. !$#journal Nucleic Acids Res. (1988) 16:9253-9265 !$#title Molecular characterization of GCD1, a yeast gene required !1for general control of amino acid biosynthesis and !1cell-cycle initiation. !$#cross-references MUID:89016627; PMID:3050897 !$#accession S05727 !'##molecule_type DNA !'##residues 1-216,'A',218,'NNSN',223,'SLFIQKTKTQ',234,'GSQYFWN', !1241-490,'SV',493-502,'VRPLCCGA' ##label HIL !'##cross-references EMBL:X07846; NID:g3731; PIDN:CAA30693.1; PID:g3732 GENETICS !$#gene SGD:GCD1; MIPS:YOR260w !'##cross-references SGD:S0005786; MIPS:YOR260w !$#map_position 15R CLASSIFICATION #superfamily GCD1 protein SUMMARY #length 578 #molecular-weight 65699 #checksum 4429 SEQUENCE /// ENTRY RGBYR3 #type complete TITLE regulatory protein ARG82 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YD9395.06c; protein YDR173c; regulatory protein ARGRIII ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jun-2000 ACCESSIONS S05823; S49769 REFERENCE S05822 !$#authors Dubois, E.; Bercy, J.; Messenguy, F. !$#journal Mol. Gen. Genet. (1987) 207:142-148 !$#title Characterization of two genes, ARGRI and ARGRIII required !1for specific regulation of arginine metabolism in yeast. !$#cross-references MUID:87257286; PMID:3298999 !$#accession S05823 !'##molecule_type DNA !'##residues 1-355 ##label DUB !'##cross-references EMBL:X05328; NID:g3375; PIDN:CAA28945.1; PID:g3376 !'##note the authors translated the codon AAG for residue 54 as Arg and !1GAG for residue 112 as Asp REFERENCE S49764 !$#authors Murphy, L.; Harris, D.E. !$#submission submitted to the EMBL Data Library, November 1994 !$#accession S49769 !'##molecule_type DNA !'##residues 1-355 ##label MUR !'##cross-references EMBL:Z46727; NID:g1289283; PIDN:CAA86678.1; !1PID:g1289288; GSPDB:GN00004; MIPS:YDR173c GENETICS !$#gene SGD:ARG82; ARGR3; MIPS:YDR173c !'##cross-references SGD:S0002580; MIPS:YDR173c !$#map_position 4R FUNCTION !$#description responsible for repression of 6 genes and induction of 2 !1genes in response to arginine CLASSIFICATION #superfamily regulatory protein ARGRIII KEYWORDS nucleus; transcription regulation FEATURE !$282-301 #region aspartic acid-rich SUMMARY #length 355 #molecular-weight 40353 #checksum 315 SEQUENCE /// ENTRY S11910 #type complete TITLE nitrogen metabolic regulation protein nmr - Neurospora crassa ALTERNATE_NAMES nmr protein ORGANISM #formal_name Neurospora crassa DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S11910; S11924 REFERENCE S11910 !$#authors Young, J.L.; Jarai, G.; Fu, Y.H.; Marzluf, G.A. !$#journal Mol. Gen. Genet. (1990) 222:120-128 !$#title Nucleotide sequence and analysis of NMR, a negative-acting !1regulatory gene in the nitrogen circuit of Neurospora !1crassa. !$#cross-references MUID:91042412; PMID:2146484 !$#accession S11910 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-488 ##label YOU GENETICS !$#gene nmr CLASSIFICATION #superfamily nitrogen metabolic regulation protein nmr KEYWORDS nucleus; transcription regulation SUMMARY #length 488 #molecular-weight 54857 #checksum 9916 SEQUENCE /// ENTRY RGBYL3 #type complete TITLE regulatory protein LEU3 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein L9324.1; protein YLR451w ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 12-Nov-1999 ACCESSIONS S00638; A26914; S55973 REFERENCE S00638 !$#authors Zhou, K.; Brisco, P.R.G.; Hinkkanen, A.E.; Kohlhaw, G.B. !$#journal Nucleic Acids Res. (1987) 15:5261-5273 !$#title Structure of yeast regulatory gene LEU3 and evidence that !1LEU3 itself is under general amino acid control. !$#cross-references MUID:87259999; PMID:3299266 !$#accession S00638 !'##molecule_type DNA !'##residues 1-886 ##label ZHO !'##cross-references EMBL:Y00360; NID:g3872; PIDN:CAA68438.1; PID:g3873 REFERENCE A26914 !$#authors Friden, P.; Schimmel, P. !$#journal Mol. Cell. Biol. (1987) 7:2708-2717 !$#title LEU3 of Saccharomyces cerevisiae encodes a factor for !1control of RNA levels of a group of leucine-specific genes. !$#cross-references MUID:88038809; PMID:2823102 !$#accession A26914 !'##molecule_type DNA !'##residues 1-503,'I',505-886 ##label FRI !'##cross-references EMBL:M17222; NID:g171832; PIDN:AAA34741.1; !1PID:g171833 REFERENCE S55966 !$#authors Du, Z. !$#submission submitted to the EMBL Data Library, March 1995 !$#description The sequence of S. cerevisiae cosmid 9324. !$#accession S55973 !'##molecule_type DNA !'##residues 1-886 ##label DUZ !'##cross-references GB:U22382; NID:g717059; PIDN:AAB67526.1; !1PID:g717060; GSPDB:GN00012; MIPS:YLR451w !'##experimental_source strain S288C (AB972) GENETICS !$#gene SGD:LEU3; MIPS:YLR451w !'##cross-references SGD:S0004443; MIPS:YLR451w !$#map_position 12R CLASSIFICATION #superfamily regulatory protein LEU3; GAL4 zinc binuclear !1cluster homology KEYWORDS DNA binding; nucleus; transcription regulation; zinc finger FEATURE !$32-72 #domain GAL4 zinc binuclear cluster homology #label !8GAL4\ !$37-67 #region zinc finger CCCC motif\ !$678-697 #region aspartic acid/glutamic acid-rich SUMMARY #length 886 #molecular-weight 100152 #checksum 5394 SEQUENCE /// ENTRY TNBYR6 #type complete TITLE transcription regulator SWI1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein LPA1w; protein YPL016w; transcription regulator ADR6 ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 03-Dec-1999 ACCESSIONS S05728; S59677 REFERENCE S05728 !$#authors O'Hara, P.J.; Horowitz, H.; Eichinger, H.; Young, E.T. !$#journal Nucleic Acids Res. (1988) 16:10153-10169 !$#title The yeast ADR6 gene encodes homopolymeric amino acid !1sequences and a potential metal-binding domain. !$#cross-references MUID:89057455; PMID:3143101 !$#accession S05728 !'##molecule_type DNA !'##residues 1-1314 ##label OHA !'##cross-references EMBL:X12493; NID:g3346; PIDN:CAA31013.1; PID:g3347 REFERENCE S59677 !$#authors Hall, J.; Ahmed, A.; Bussey, H.; Fortin, N.; Friesen, J.D.; !1Storms, R.K.; Vo, D.H.; Wang, Y.; Winnett, E. !$#submission submitted to the EMBL Data Library, August 1995 !$#description The sequence of Saccharomyces cerevisiae chromosome XVI left !1arm. !$#accession S59677 !'##molecule_type DNA !'##residues 1-1314 ##label HAL !'##cross-references EMBL:U33335; NID:g965076; PIDN:AAB68089.1; !1PID:g965077; GSPDB:GN00016; MIPS:YPL016w GENETICS !$#gene SGD:SWI1; ADR6; MIPS:YPL016w !'##cross-references SGD:S0005937; MIPS:YPL016w !$#map_position 16L CLASSIFICATION #superfamily transcription regulator ADR6 KEYWORDS DNA binding; transcription regulation; zinc finger FEATURE !$7-65 #region asparagine/threonine-rich\ !$337-385 #region glutamine-rich\ !$1241-1258 #region zinc finger CCCC motif SUMMARY #length 1314 #molecular-weight 147937 #checksum 6916 SEQUENCE /// ENTRY RGBYH1 #type complete TITLE CYC1/CYP3 transcription activator - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein L9672.1; protein YLR256w; regulatory protein CYP1; regulatory protein HAP1 ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1991 #sequence_revision 23-Feb-1996 #text_change 12-Nov-1999 ACCESSIONS S59400; A31312; S15447; S05804; S15446 REFERENCE S59386 !$#authors Johnson, D. !$#submission submitted to the EMBL Data Library, February 1995 !$#description The sequence of S. cerevisiae cosmid 9672. !$#accession S59400 !'##molecule_type DNA !'##residues 1-1502 ##label JOH !'##cross-references EMBL:U20865; NID:g662330; PIDN:AAB67387.1; !1PID:g662331; GSPDB:GN00012; MIPS:YLR256w !'##experimental_source strain S288C (AB972) REFERENCE A31312 !$#authors Pfeifer, K.; Kim, K.S.; Kogan, S.; Guarente, L. !$#journal Cell (1989) 56:291-301 !$#title Functional dissection and sequence of yeast HAP1 activator. !$#cross-references MUID:89106221; PMID:2643482 !$#accession A31312 !'##molecule_type DNA !'##residues 1-144,'I',146-322,'R',324-454,'N',456-507,'M',509-586,'K', !1588-882,'N',884-959,'S',961-1150,'N',1152-1156,'P', !11158-1304,'Y',1306-1470,'LVDFYRADFPIWE' ##label PFE !'##cross-references EMBL:J03152; NID:g171645; PIDN:AAA34662.1; !1PID:g171646 REFERENCE S15447 !$#authors Creusot, F.; Verdiere, J.; Gaisne, M.; Slonimski, P.P. !$#journal J. Mol. Biol. (1988) 204:263-276 !$#title CYP1 (HAP1) regulator of oxygen-dependent gene expression in !1yeast. I. Overall organization of the protein sequence !1displays several novel structural domains. !$#cross-references MUID:89125585; PMID:2851658 !$#accession S15447 !'##molecule_type DNA !'##residues 1-62,'R',64-1305,'Y',1306-1470,'LVDFYRADFPIWE' ##label CRE1 !'##cross-references EMBL:X13793 !'##note the sequence is from mutant CYP1-18 GENETICS !$#gene SGD:HAP1; CYP1; MIPS:YLR256w !'##cross-references SGD:S0004246; MIPS:YLR256w !$#map_position 12R CLASSIFICATION #superfamily regulatory protein HAP1; GAL4 zinc binuclear !1cluster homology KEYWORDS DNA binding; heme binding; transcription regulation; zinc !1finger FEATURE !$1-148 #domain DNA binding #status predicted #label DNA\ !$59-98 #domain GAL4 zinc binuclear cluster homology #label !8GAL4\ !$64-84 #region zinc finger CCCC motif\ !$177-189 #region glutamine-rich\ !$245-445 #domain heme binding #status predicted #label HEM\ !$299-304,323-328, !$347-352,373-378, !$389-394,415-420 #region 6-residue repeats\ !$1308-1481 #domain activation element #status predicted #label !8ACT\ !$1388-1481 #region acidic SUMMARY #length 1502 #molecular-weight 166106 #checksum 7669 SEQUENCE /// ENTRY RGBYG4 #type complete TITLE regulatory protein GAL4 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein P1021; protein YPL248c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 21-Jul-2000 ACCESSIONS A05022; S61016; S65277; S12977 REFERENCE A05022 !$#authors Laughon, A.; Gesteland, R.F. !$#journal Mol. Cell. Biol. (1984) 4:260-267 !$#title Primary structure of the Saccharomyces cerevisiae GAL4 gene. !$#cross-references MUID:84141879; PMID:6366516 !$#accession A05022 !'##molecule_type DNA !'##residues 1-881 ##label LAU !'##cross-references EMBL:K01486; NID:g171557; PIDN:AAA34626.1; !1PID:g171558 REFERENCE S12977 !$#authors Gadhavi, P.L.; Raine, A.R.C.; Alefounder, P.R.; Laue, E.D. !$#journal FEBS Lett. (1990) 276:49-53 !$#title Complete assignment of the (1)H NMR spectrum and secondary !1structure of the DNA binding domain of GAL4. !$#cross-references MUID:91092433; PMID:2265711 !$#contents annotation; zinc finger REFERENCE S61010 !$#authors Pohl, T.M. !$#submission submitted to the EMBL Data Library, November 1995 !$#accession S61016 !'##molecule_type DNA !'##residues 1-881 ##label POH !'##cross-references EMBL:Z67751; NID:g1061234; PIDN:CAA91596.1; !1PID:g1061241 REFERENCE S64899 !$#authors Pohl, T.M. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S65277 !'##molecule_type DNA !'##residues 1-881 ##label POW !'##cross-references EMBL:Z73604; NID:g1370510; PIDN:CAA97969.1; !1PID:g1370511; GSPDB:GN00016; MIPS:YPL248c !'##experimental_source strain S288C (AB972) COMMENT This protein is a positive regulator for the gene expression !1of the galactose-induced genes. GENETICS !$#gene SGD:GAL4; MIPS:YPL248c !'##cross-references SGD:S0006169; MIPS:YPL248c !$#map_position 16L CLASSIFICATION #superfamily regulatory protein GAL4; GAL4 zinc binuclear !1cluster homology KEYWORDS DNA binding; galactose utilization; transcription !1regulation; zinc finger FEATURE !$6-43 #domain GAL4 zinc binuclear cluster homology #label !8GAL4\ !$11-38 #region zinc finger CCCC motif SUMMARY #length 881 #molecular-weight 99402 #checksum 2669 SEQUENCE /// ENTRY S52979 #type complete TITLE hypothetical protein 6 - Erwinia herbicola ORGANISM #formal_name Erwinia herbicola DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S52979 REFERENCE S52976 !$#authors Hundle, B.; Alberti, M.; Nievelstein, V.; Beyer, P.; !1Kleinig, H.; Armstrong, G.A.; Burke, D.H.; Hearst, J.E. !$#journal Mol. Gen. Genet. (1994) 245:406-416 !$#title Functional assignment of Erwinia herbicola Eho 10 carotenoid !1genes expressed in Escherichia coli. !$#cross-references MUID:95107236; PMID:7808389 !$#accession S52979 !'##status preliminary !'##molecule_type DNA !'##residues 1-347 ##label HUN !'##cross-references EMBL:M87280; NID:g148404; PIDN:AAA64978.1; !1PID:g148409 CLASSIFICATION #superfamily carotenoid biosynthesis protein homolog SUMMARY #length 347 #molecular-weight 37165 #checksum 6024 SEQUENCE /// ENTRY S75922 #type complete TITLE hypothetical protein sll1556 - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S75922 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75922 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-349 ##label KAN !'##cross-references EMBL:D90913; GB:AB001339; NID:g1653348; !1PIDN:BAA18381.1; PID:g1653467 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily carotenoid biosynthesis protein homolog SUMMARY #length 349 #molecular-weight 37542 #checksum 9241 SEQUENCE /// ENTRY F64407 #type complete TITLE carotenoid biosynthesis protein homolog - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F64407 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession F64407 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-359 ##label BUL !'##cross-references GB:U67530; GB:L77117; NID:g2826340; !1PIDN:AAB98867.1; PID:g1591547; TIGR:MJ0862 GENETICS !$#map_position REV786385-785306 CLASSIFICATION #superfamily carotenoid biosynthesis protein homolog SUMMARY #length 359 #molecular-weight 39875 #checksum 9796 SEQUENCE /// ENTRY G64814 #type complete TITLE molybdenum cofactor biosynthesis protein C [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES moaC protein ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS G64814; S35000; S31881 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64814 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-161 ##label BLAT !'##cross-references GB:AE000181; GB:U00096; NID:g1786998; !1PIDN:AAC73870.1; PID:g1787001; UWGP:b0783 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S34998 !$#authors Rivers, S.L.; McNairn, E.; Blasco, F.; Giordano, G.; Boxer, !1D.H. !$#journal Mol. Microbiol. (1993) 8:1071-1081 !$#title Molecular genetic analysis of the moa operon of Escherichia !1coli K-12 required for molybdenum cofactor biosynthesis. !$#cross-references MUID:93368423; PMID:8361352 !$#accession S35000 !'##status preliminary !'##molecule_type DNA !'##residues 1-16,'N',18-91,'RAQSG',98-161 ##label RIV !'##cross-references EMBL:X70420; NID:g42007; PIDN:CAA49863.1; !1PID:g42010 !'##note the authors translated the codon AAT for residue 17 as Asp GENETICS !$#gene moaC !$#map_position 18 min FUNCTION !$#description involved in molybdopterin biosynthesis [validated, !1MUID:93368423] CLASSIFICATION #superfamily molybdenum cofactor biosynthesis protein C SUMMARY #length 161 #molecular-weight 17467 #checksum 3084 SEQUENCE /// ENTRY F64619 #type complete TITLE molybdenum cofactor biosynthesis protein C - Helicobacter pylori (strain 26695 and isolate 8826) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS F64619; A47052 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession F64619 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-158 ##label TOM !'##cross-references GB:AE000592; GB:AE000511; NID:g2313929; !1PIDN:AAD07848.1; PID:g2313930; TIGR:HP0798 !'##experimental_source strain 26695 REFERENCE A47052 !$#authors Evans, D.G.; Karjalainen, T.K.; Evans Jr., D.J.; Graham, !1D.Y.; Lee, C.H. !$#journal J. Bacteriol. (1993) 175:674-683 !$#title Cloning, nucleotide sequence, and expression of a gene !1encoding an adhesin subunit protein of Helicobacter pylori. !$#cross-references MUID:93139035; PMID:7678592 !$#accession A47052 !'##status preliminary !'##molecule_type DNA !'##residues 8-46,'G',48-63,'A',65-107,'S',109-113,'GANECERRAFNHL' !1##label EVA !'##cross-references GB:X61574; NID:g732735; PIDN:CAA43772.1; PID:g48965 !'##experimental_source isolate 8826 !'##note sequence extracted from NCBI backbone (NCBIN:123532, !1NCBIP:123533) GENETICS !$#gene HP0798 CLASSIFICATION #superfamily molybdenum cofactor biosynthesis protein C SUMMARY #length 158 #molecular-weight 17271 #checksum 3799 SEQUENCE /// ENTRY RGBYG8 #type complete TITLE regulatory protein GAL80 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YM9827.01; protein YML051w ORGANISM #formal_name Saccharomyces cerevisiae DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 21-Jul-2000 ACCESSIONS A03606; S49810; S50941; A39075 REFERENCE A03606 !$#authors Nogi, Y.; Fukasawa, T. !$#journal Nucleic Acids Res. (1984) 12:9287-9298 !$#title Nucleotide sequence of the yeast regulatory gene GAL80. !$#cross-references MUID:85087937; PMID:6393054 !$#accession A03606 !'##molecule_type DNA !'##residues 1-435 ##label NOG !'##cross-references EMBL:X01667; NID:g3717; PIDN:CAA25827.1; PID:g3718 REFERENCE S49800 !$#authors Devlin, K.; Churcher, C. !$#submission submitted to the EMBL Data Library, November 1994 !$#accession S49810 !'##molecule_type DNA !'##residues 1-100,'E',102-127 ##label DEV !'##cross-references EMBL:Z46729; GSPDB:GN00013; MIPS:YML051w REFERENCE S50941 !$#authors Odell, C.; Bowman, S. !$#submission submitted to the EMBL Data Library, January 1995 !$#accession S50941 !'##molecule_type DNA !'##residues 118-435 ##label ODE !'##cross-references EMBL:Z47816; NID:g642303; PIDN:CAA87823.1; !1PID:g642304; GSPDB:GN00013; MIPS:YML051w REFERENCE A39075 !$#authors Yun, S.J.; Hiraoka, Y.; Nishizawa, M.; Takio, K.; Titani, !1K.; Nogi, Y.; Fukasawa, T. !$#journal J. Biol. Chem. (1991) 266:693-697 !$#title Purification and characterization of the yeast negative !1regulatory protein GAL80. !$#cross-references MUID:91093258; PMID:1985957 !$#accession A39075 !'##molecule_type protein !'##residues 2-4;29-33;162-171;410-416 ##label YUN COMMENT This protein is a negative regulator for the gene expression !1of the galactose-induced genes, which code for the enzymes !1used to convert galactose to glucose. GENETICS !$#gene SGD:GAL80; MIPS:YML051w !'##cross-references SGD:S0004515; MIPS:YML051w !$#map_position 13L CLASSIFICATION #superfamily regulatory protein GAL80 KEYWORDS acetylated amino end; DNA binding; transcription regulation FEATURE !$1 #modified_site acetylated amino end (Met) #status !8experimental SUMMARY #length 435 #molecular-weight 48309 #checksum 9312 SEQUENCE /// ENTRY RGBYP1 #type complete TITLE regulatory protein PPR1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein L1575; protein YLR014c; pyrimidine pathway regulatory protein 1 ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Jun-2000 ACCESSIONS S05877; S59276; S59799; S64836 REFERENCE S05877 !$#authors Kammerer, B.; Guyonvarch, A.; Hubert, J.C. !$#journal J. Mol. Biol. (1984) 180:239-250 !$#title Yeast regulatory gene PPR1. I. Nucleotide sequence, !1restriction map and codon usage. !$#cross-references MUID:85083082; PMID:6096561 !$#accession S05877 !'##molecule_type DNA !'##residues 1-904 ##label KAM !'##cross-references EMBL:X01739; NID:g4214; PIDN:CAA25876.1; PID:g4215 REFERENCE S59270 !$#authors Saville, S.P.; Atkinson, S.; Jamieson, L.; Pocklington, !1M.J.; Orr, E. !$#submission submitted to the EMBL Data Library, August 1995 !$#description A 7.8kb fragment from chromosome XII of Saccharomyces !1cerevisiae does not harbour PKC2. !$#accession S59276 !'##molecule_type DNA !'##residues 1-513 ##label SAV !'##cross-references EMBL:X90564; NID:g975221; PIDN:CAA62160.1; !1PID:g975228 !'##experimental_source strain S288C REFERENCE S59799 !$#authors Liljelund, P.; Losson, R.; Kammerer, B.; Lacroute, F. !$#journal J. Mol. Biol. (1984) 180:251-265 !$#title Yeast regulatory gene PPR1. II. Chromosomal localization, !1meiotic map, suppressibility, dominance/recessivity and !1dosage effect. !$#cross-references MUID:85083083; PMID:6096562 !$#accession S59799 !'##molecule_type DNA !'##residues 1-75 ##label LIL !'##cross-references EMBL:M29131; NID:g342049; PIDN:AAA70331.1; !1PID:g903888 REFERENCE S64742 !$#authors Vandenbol, M.; Portetelle, D.; Hilger, F. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64836 !'##molecule_type DNA !'##residues 1-904 ##label VAN !'##cross-references EMBL:Z73186; NID:g1360311; PIDN:CAA97536.1; !1PID:g1360312; GSPDB:GN00012; MIPS:YLR014c !'##note experimental_source strain S288C GENETICS !$#gene SGD:PPR1; MIPS:YLR014c !'##cross-references SGD:S0004004; MIPS:YLR014c !$#map_position 12R CLASSIFICATION #superfamily regulatory protein PPR1; GAL4 zinc binuclear !1cluster homology KEYWORDS DNA binding; transcription regulation; zinc finger FEATURE !$29-66 #domain GAL4 zinc binuclear cluster homology #label !8GAL4\ !$34-61 #region zinc finger CCCC motif SUMMARY #length 904 #molecular-weight 102723 #checksum 2418 SEQUENCE /// ENTRY RGBYS5 #type complete TITLE regulatory protein SNF5 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YBR2036; protein YBR289w ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1991 #sequence_revision 09-Sep-1994 #text_change 21-Jul-2000 ACCESSIONS S44551; S46171; A36375; S12067; S39145 REFERENCE S44537 !$#authors Holmstrom, K.; Brandt, T.; Kallesoe, T. !$#journal Yeast (1994) 10(Suppl.A):S47-S62 !$#title The sequence of a 32420 bp segment located on the right arm !1of chromosome II from Saccharomyces cerevisiae. !$#cross-references MUID:94378722; PMID:8091861 !$#accession S44551 !'##status translation not shown !'##molecule_type DNA !'##residues 1-905 ##label HOL !'##cross-references EMBL:X76053; NID:g600025; PIDN:CAA53652.1; !1PID:g429134 REFERENCE S46157 !$#authors Brandt, T.; Christiansen, C.; Holmstroem, K.; Kallesoe, T. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S46171 !'##molecule_type DNA !'##residues 1-905 ##label BRA !'##cross-references EMBL:Z36158; NID:g536741; PIDN:CAA85254.1; !1PID:g536742; GSPDB:GN00002; MIPS:YBR289w REFERENCE A36375 !$#authors Laurent, B.C.; Treitel, M.A.; Carlson, M. !$#journal Mol. Cell. Biol. (1990) 10:5616-5625 !$#title The SNF5 protein of Saccharomyces cerevisiae is a glutamine- !1and proline-rich transcriptional activator that affects !1expression of a broad spectrum of genes. !$#cross-references MUID:91042489; PMID:2233708 !$#accession A36375 !'##molecule_type DNA !'##residues 1-563,'D',565-905 ##label LAU !'##cross-references GB:M36482; NID:g172637; PIDN:AAA35062.1; !1PID:g172638 GENETICS !$#gene SGD:SNF5; MIPS:YBR289w !'##cross-references SGD:S0000493; MIPS:YBR289w !$#map_position 2R CLASSIFICATION #superfamily regulatory protein SNF5 KEYWORDS nucleus; transcription regulation FEATURE !$31-324 #region glutamine/proline-rich\ !$435-683 #region acidic\ !$714-882 #region proline-rich SUMMARY #length 905 #molecular-weight 102556 #checksum 4412 SEQUENCE /// ENTRY A36313 #type complete TITLE sucrose nonfermenting protein 6 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YHL025w ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 23-Mar-2001 ACCESSIONS A36313; S46839; S12294; S25456 REFERENCE A36313 !$#authors Estruch, F.; Carlson, M. !$#journal Mol. Cell. Biol. (1990) 10:2544-2553 !$#title SNF6 encodes a nuclear protein that is required for !1expression of many genes in Saccharomyces cerevisiae. !$#cross-references MUID:90258839; PMID:2188093 !$#accession A36313 !'##molecule_type DNA !'##residues 1-332 ##label EST !'##cross-references GB:M37132; NID:g172639; PIDN:AAA35063.1; !1PID:g172640 REFERENCE S46796 !$#authors Favello, T. !$#submission submitted to the EMBL Data Library, June 1994 !$#description The sequence of S. cerevisiae cosmid 9433. !$#accession S46839 !'##molecule_type DNA !'##residues 1-332 ##label FAV !'##cross-references EMBL:U11582; NID:g2289793; PID:g508761; !1GSPDB:GN00008; MIPS:YHL025w GENETICS !$#gene SGD:SNF6; MIPS:YHL025w !'##cross-references SGD:S0001017; MIPS:YHL025w !$#map_position 8L CLASSIFICATION #superfamily sucrose nonfermenting protein 6 KEYWORDS nucleus; transcription FEATURE !$2-10 #region nuclear location signal SUMMARY #length 332 #molecular-weight 37606 #checksum 716 SEQUENCE /// ENTRY S50614 #type complete TITLE regulatory protein SWI4 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES ART1 protein; cell-cycle box factor chain SWI4; protein YER111c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-Nov-1999 ACCESSIONS S50614; S07106; S35260 REFERENCE S50614 !$#authors Dietrich, F.S. !$#submission submitted to the EMBL Data Library, December 1994 !$#description The sequence of S. cerevisiae cosmids 9781, 8198, 9115, !19981, and lambda clones 3955 and 6052. !$#accession S50614 !'##molecule_type DNA !'##residues 1-1093 ##label DIE !'##cross-references EMBL:U18916; NID:g1384128; PIDN:AAC03209.1; !1PID:g603350; GSPDB:GN00005; MIPS:YER111c REFERENCE S07106 !$#authors Andrews, B.J.; Herskowitz, I. !$#journal Nature (1989) 342:830-833 !$#title The yeast SWI4 protein contains a motif present in !1developmental regulators and is part of a complex involved !1in cell-cycle-dependent transcription. !$#cross-references MUID:90098089; PMID:2689885 !$#accession S07106 !'##molecule_type DNA !'##residues 1-174,'T',176-430,'I',432-1053,'L',1055-1093 ##label AND !'##cross-references EMBL:X51606; NID:g4594; PIDN:CAA35949.1; !1PID:g666106 REFERENCE S35260 !$#authors Daniel, J. !$#journal Mol. Gen. Genet. (1993) 240:245-257 !$#title Potentially rapid walking in cellular regulatory networks !1using the gene-gene interference method in yeast. !$#cross-references MUID:93360904; PMID:8355657 !$#accession S35260 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 845-1093 ##label DAN GENETICS !$#gene SGD:SWI4; MIPS:YER111c !'##cross-references SGD:S0000913; MIPS:YER111c !$#map_position 5R CLASSIFICATION #superfamily regulatory protein SWI4; ankyrin repeat !1homology KEYWORDS DNA binding FEATURE !$201-727 #region asparagine/glutamine-rich\ !$520-552 #domain ankyrin repeat homology #label AN1 SUMMARY #length 1093 #molecular-weight 123805 #checksum 9961 SEQUENCE /// ENTRY RGBYS3 #type complete TITLE regulatory protein SIN3 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein O2385; protein YOL004w ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1991 #sequence_revision 02-Aug-1996 #text_change 16-Jun-2000 ACCESSIONS S66686; A36381; A41957; S12068; S22283 REFERENCE S66685 !$#authors Hughes, B.; Pohl, T.M. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S66686 !'##molecule_type DNA !'##residues 1-1536 ##label HUG !'##cross-references EMBL:Z74746; NID:g1419766; PIDN:CAA99003.1; !1PID:g1419767; GSPDB:GN00015; MIPS:YOL004w !'##experimental_source strain S288C REFERENCE A36381 !$#authors Wang, H.; Clark, I.; Nicholson, P.R.; Herskowitz, I.; !1Stillman, D.J. !$#journal Mol. Cell. Biol. (1990) 10:5927-5936 !$#title The Saccharomyces cerevisiae SIN3 gene, a negative regulator !1of HO, contains four paired amphipathic helix motifs. !$#cross-references MUID:91042523; PMID:2233725 !$#accession A36381 !'##molecule_type DNA !'##residues 1-510,'AQ',511-1536 ##label WAN !'##cross-references GB:M36822; NID:g172093; PIDN:AAA34839.1; !1PID:g172094 REFERENCE A41957 !$#authors Vidal, M.; Strich, R.; Esposito, R.E.; Gaber, R.F. !$#journal Mol. Cell. Biol. (1991) 11:6306-6316 !$#title RPD1 (SIN3/UME4) is required for maximal activation and !1repression of diverse yeast genes. !$#cross-references MUID:92049361; PMID:1944290 !$#accession A41957 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 227-285;414-441,'DE',444-472;667-725;1140-1200 ##label VID GENETICS !$#gene SGD:SIN3; SDI1; UME4; RPD1; MIPS:YOL004w !'##cross-references SGD:S0005364; MIPS:YOL004w !$#map_position 15L CLASSIFICATION #superfamily regulatory protein SIN3 KEYWORDS nucleus; transcription regulation FEATURE !$480-519 #region glutamine-rich SUMMARY #length 1536 #molecular-weight 174838 #checksum 9179 SEQUENCE /// ENTRY RGBYS2 #type complete TITLE regulatory protein SIR2 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein D2714; protein YDL042c; silent information regulator 2 ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jun-2000 ACCESSIONS S05891; S67575 REFERENCE S05891 !$#authors Shore, D.; Squire, M.; Nasmyth, K.A. !$#journal EMBO J. (1984) 3:2817-2823 !$#title Characterization of two genes required for the !1position-effect control of yeast mating-type genes. !$#cross-references MUID:85126876; PMID:6098447 !$#accession S05891 !'##molecule_type DNA !'##residues 1-562 ##label SHO !'##cross-references EMBL:X01419; NID:g4469; PIDN:CAA25667.1; PID:g4470 REFERENCE S67560 !$#authors Paulin, L.; Saren, A.M.; Laamanen, P. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67575 !'##molecule_type DNA !'##residues 1-562 ##label PAU !'##cross-references EMBL:Z74090; NID:g1431026; PIDN:CAA98600.1; !1PID:g1431027; GSPDB:GN00004; MIPS:YDL042c !'##experimental_source strain S288C GENETICS !$#gene SGD:SIR2; MIPS:YDL042c !'##cross-references SGD:S0002200; MIPS:YDL042c !$#map_position 4L CLASSIFICATION #superfamily regulatory protein SIR2 KEYWORDS DNA binding; transcription regulation SUMMARY #length 562 #molecular-weight 63261 #checksum 2881 SEQUENCE /// ENTRY RGBYI3 #type complete TITLE regulatory protein SIR3 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein L9753.10; protein YLR442c; silent information regulator 3 ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Dec-1991 #sequence_revision 23-Feb-1996 #text_change 12-Nov-1999 ACCESSIONS S59410; S05892 REFERENCE S59401 !$#authors Du, Z. !$#submission submitted to the EMBL Data Library, February 1995 !$#description The sequence of S. cerevisiae cosmid 9753. !$#accession S59410 !'##molecule_type DNA !'##residues 1-978 ##label DUZ !'##cross-references EMBL:U21094; NID:g665967; PIDN:AAB67522.1; !1PID:g665977; GSPDB:GN00012; MIPS:YLR442c !'##experimental_source strain S288C (AB972) REFERENCE S05891 !$#authors Shore, D.; Squire, M.; Nasmyth, K.A. !$#journal EMBO J. (1984) 3:2817-2823 !$#title Characterization of two genes required for the !1position-effect control of yeast mating-type genes. !$#cross-references MUID:85126876; PMID:6098447 !$#accession S05892 !'##molecule_type DNA !'##residues 1-330,'S',332-334,'P',336-404,'G',406-420,'Q',422-428,'KK', !1431-496,'V',498-586,'R',588-596,'V',598-668,'D',670-703,'G', !1705-711,'T',713-725,'N',727-827,'F',829,'L',831-924,'K', !1926-978 ##label SHO !'##cross-references EMBL:X01420; NID:g4471; PIDN:CAA25668.1; PID:g4472 GENETICS !$#gene SGD:SIR3; MIPS:YLR442c !'##cross-references SGD:S0004434; MIPS:YLR442c !$#map_position 12R CLASSIFICATION #superfamily regulatory protein SIR3 KEYWORDS DNA binding; nucleus; transcription regulation SUMMARY #length 978 #molecular-weight 111359 #checksum 632 SEQUENCE /// ENTRY RGBYC3 #type complete TITLE regulatory protein SNF4 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES CAT3 protein; protein G2945; protein YGL115w ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 21-Jul-2000 ACCESSIONS A38906; JT0316; S48508; S64125 REFERENCE A33480 !$#authors Celenza, J.L.; Eng, F.J.; Carlson, M. !$#journal Mol. Cell. Biol. (1989) 9:5045-5054 !$#title Molecular analysis of the SNF4 gene of Saccharomyces !1cerevisiae: evidence for physical association of the SNF4 !1protein with the SNF1 protein kinase. !$#cross-references MUID:90097921; PMID:2481228 !$#accession A38906 !'##molecule_type DNA !'##residues 1-322 ##label CEL !'##cross-references GB:M30470; NID:g172635; PIDN:AAA35061.1; !1PID:g172636 REFERENCE JT0316 !$#authors Schueller, H.J.; Entian, K.D. !$#journal Gene (1988) 67:247-257 !$#title Molecular characterization of yeast regulatory gene CAT3 !1necessary for glucose derepression and nuclear localization !1of its product. !$#cross-references MUID:89006284; PMID:3049255 !$#accession JT0316 !'##molecule_type DNA !'##residues 1-322 ##label SCH !'##cross-references GB:M21760; NID:g171164; PIDN:AAA34472.1; !1PID:g171165 REFERENCE S48507 !$#authors Doi, A.; Doi, K. !$#submission submitted to the EMBL Data Library, June 1993 !$#description Correct end of the ORF for the CDC20 gene of Saccharomyces !1cerevisiae. !$#accession S48508 !'##molecule_type DNA !'##residues 1-21 ##label DOI !'##cross-references EMBL:D16506; NID:g391938; PIDN:BAA03958.1; !1PID:g2160324 REFERENCE S64122 !$#authors Lauquin, G. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64125 !'##molecule_type DNA !'##residues 1-322 ##label LAU !'##cross-references EMBL:Z72637; NID:g1322666; PIDN:CAA96823.1; !1PID:g1322667; GSPDB:GN00007; MIPS:YGL115w !'##experimental_source strain S288C GENETICS !$#gene SGD:SNF4; CAT34; MIPS:YGL115w !'##cross-references SGD:S0003083; MIPS:YGL115w !$#map_position 7L FUNCTION !$#description involved in derepression of glucose-repressed genes CLASSIFICATION #superfamily CAT3 protein KEYWORDS nucleus; transcription regulation SUMMARY #length 322 #molecular-weight 36401 #checksum 2265 SEQUENCE /// ENTRY A44073 #type complete TITLE CIK1 protein - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YM9646.11; protein YMR198w ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1993 #sequence_revision 08-Mar-1996 #text_change 21-Jul-2000 ACCESSIONS A44073; S50927 REFERENCE A44073 !$#authors Page, B.D.; Snyder, M. !$#journal Genes Dev. (1992) 6:1414-1429 !$#title CIK1: a developmentally regulated spindle pole !1body-associated protein important for microtubule functions !1in Saccharomyces cerevisiae. !$#cross-references MUID:92354905; PMID:1644287 !$#accession A44073 !'##molecule_type DNA !'##residues 1-594 ##label PAG !'##cross-references EMBL:M96439; NID:g171221; PIDN:AAA34494.1; !1PID:g171222 !'##note sequence extracted from NCBI backbone (NCBIN:110670, !1NCBIP:110672) REFERENCE S50917 !$#authors Pearson, D.; Bowman, S. !$#submission submitted to the EMBL Data Library, January 1995 !$#accession S50927 !'##molecule_type DNA !'##residues 1-594 ##label PEA !'##cross-references EMBL:Z47815; NID:g642280; PIDN:CAA87820.1; !1PID:g642291; GSPDB:GN00013; MIPS:YMR198w GENETICS !$#gene SGD:CIK1; MIPS:YMR198w !'##cross-references SGD:S0004811; MIPS:YMR198w !$#map_position 13R CLASSIFICATION #superfamily CIK1 protein KEYWORDS coiled coil SUMMARY #length 594 #molecular-weight 69069 #checksum 7831 SEQUENCE /// ENTRY BVBY22 #type complete TITLE PET122 protein precursor - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YER153c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1991 #sequence_revision 30-Sep-1992 #text_change 23-Mar-2001 ACCESSIONS B36328; S50656; S05724; A46737; S12289 REFERENCE A36328 !$#authors Ohmen, J.D.; Burke, K.A.; McEwen, J.E. !$#journal Mol. Cell. Biol. (1990) 10:3027-3035 !$#title Divergent overlapping transcripts at the PET122 locus in !1Saccharomyces cerevisiae. !$#cross-references MUID:90258894; PMID:2160592 !$#accession B36328 !'##molecule_type DNA !'##residues 1-254 ##label OHM !'##cross-references GB:X07558 REFERENCE S50430 !$#authors Dietrich, F.S. !$#submission submitted to the EMBL Data Library, December 1994 !$#description The sequence of S. cerevisiae cosmids 8229, 9115, 9132, !19981, and lambda clones 7990 and 6134. !$#accession S50656 !'##molecule_type DNA !'##residues 1-254 ##label DIE !'##cross-references EMBL:U18917; NID:g603377; PIDN:AAB64680.1; !1PID:g603393; GSPDB:GN00005; MIPS:YER153c REFERENCE S05724 !$#authors Ohmen, J.D.; Kloeckener-Gruissem, B.; McEwen, J.E. !$#journal Nucleic Acids Res. (1988) 16:10783-10802 !$#title Molecular cloning and nucleotide sequence of the nuclear !1PET122 gene required for expression of the mitochondrial !1COX3 gene in S. cerevisae. !$#cross-references MUID:89083497; PMID:2849752 !$#accession S05724 !'##molecule_type DNA !'##residues 1-198,'KT',201-222,'DVCWRSSVKVIA',235,'CRCWMPN' ##label OH2 !'##cross-references EMBL:X07558 !'##note this sequence has been revised in reference A36328 REFERENCE A46737 !$#authors McMullin, T.W.; Fox, T.D. !$#journal J. Biol. Chem. (1993) 268:11737-11741 !$#title COX3 mRNA-specific translational activator proteins are !1associated with the inner mitochondrial membrane in !1Saccharomyces cerevisiae. !$#cross-references MUID:93280133; PMID:8389363 !$#accession A46737 !'##molecule_type protein !'##residues 9-19 ##label MCM GENETICS !$#gene SGD:PET122; MIPS:YER153c !'##cross-references SGD:S0000955; MIPS:YER153c !$#map_position 5R !$#genome nuclear CLASSIFICATION #superfamily PET122 protein KEYWORDS mitochondrion FEATURE !$1-8 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$9-254 #product PET122 protein #status experimental #label !8MAT SUMMARY #length 254 #molecular-weight 29155 #checksum 931 SEQUENCE /// ENTRY RGBYD2 #type complete TITLE translation regulator GCD2 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein G4615; protein YGR083c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jun-2000 ACCESSIONS S05809; S64378 REFERENCE S05809 !$#authors Paddon, C.J.; Hannig, E.M.; Hinnebusch, A.G. !$#journal Genetics (1989) 122:551-559 !$#title Amino acid sequence similarity between GCN3 and GCD2, !1positive and negative translational regulators of GCN4: !1evidence for antagonism by competition. !$#cross-references MUID:89339141; PMID:2668117 !$#accession S05809 !'##molecule_type DNA !'##residues 1-651 ##label PAD !'##cross-references EMBL:X15658; NID:g3733; PIDN:CAA33693.1; PID:g3734 REFERENCE S64356 !$#authors Wedler, H.; Scharfe, M.; Wedler, E.; Wambutt, R. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64378 !'##molecule_type DNA !'##residues 1-651 ##label WED !'##cross-references EMBL:Z72868; NID:g1323118; PIDN:CAA97085.1; !1PID:g1323119; GSPDB:GN00007; MIPS:YGR083c !'##experimental_source strain S288C GENETICS !$#gene SGD:GCD2; GCD12; MIPS:YGR083c !'##cross-references SGD:S0003315; MIPS:YGR083c !$#map_position 7R CLASSIFICATION #superfamily translation regulator GCD2 KEYWORDS P-loop; phosphoprotein FEATURE !$573-580 #region nucleotide-binding motif A (P-loop) #status !8atypical\ !$106 #binding_site phosphate (Ser) (covalent) (by !8cAMP-dependent kinase) #status predicted\ !$121 #binding_site phosphate (Thr) (covalent) (by !8cAMP-dependent kinase) #status predicted SUMMARY #length 651 #molecular-weight 70852 #checksum 8846 SEQUENCE /// ENTRY BVBYD9 #type complete TITLE RAD9 protein - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YD9934.02c; protein YDR217c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1991 #sequence_revision 16-Feb-1996 #text_change 05-Nov-1999 ACCESSIONS S59424; A32789; S05765 REFERENCE S59423 !$#authors Murphy, L.; Harris, D. !$#submission submitted to the EMBL Data Library, March 1995 !$#accession S59424 !'##molecule_type DNA !'##residues 1-1309 ##label MUR !'##cross-references EMBL:Z48612; NID:g728671; PIDN:CAA88497.1; !1PID:g728673; GSPDB:GN00004; MIPS:YDR217c !'##experimental_source strain AB972 REFERENCE A32789 !$#authors Schiestl, R.H.; Reynolds, P.; Prakash, S.; Prakash, L. !$#journal Mol. Cell. Biol. (1989) 9:1882-1896 !$#title Cloning and sequence analysis of the Saccharomyces !1cerevisiae RAD9 gene and further evidence that its product !1is required for cell cycle arrest induced by DNA damage. !$#cross-references MUID:89313732; PMID:2664461 !$#accession A32789 !'##molecule_type DNA !'##residues 1-432,'C',434-1309 ##label SCH !'##cross-references EMBL:M26049; NID:g172352; PIDN:AAA34954.1; !1PID:g172353 GENETICS !$#gene SGD:RAD9; MIPS:YDR217c !'##cross-references SGD:S0002625; MIPS:YDR217c !$#map_position 4R CLASSIFICATION #superfamily RAD9 protein SUMMARY #length 1309 #molecular-weight 148396 #checksum 2934 SEQUENCE /// ENTRY A24781 #type complete TITLE excision repair protein - human ALTERNATE_NAMES DNA repair protein ORGANISM #formal_name Homo sapiens #common_name man DATE 22-Oct-1999 #sequence_revision 22-Oct-1999 #text_change 22-Oct-1999 ACCESSIONS A32875; B32875; I55521; A24781 REFERENCE A90925 !$#authors Hoeijmakers, J.H.J.; van Duin, M.; Westerveld, A.; Yasui, !1A.; Bootsma, D. !$#journal Cold Spring Harb. Symp. Quant. Biol. (1986) 51:91-101 !$#title Identification of DNA repair genes in the human genome. !$#cross-references MUID:87217074; PMID:3034490 !$#accession A32875 !'##molecule_type DNA !'##residues 1-297 ##label HOE1 !'##cross-references GB:M28650; NID:g182176; PIDN:AAA35810.1; !1PID:g182177 !'##experimental_source clone pcDE !$#accession B32875 !'##molecule_type mRNA !'##residues 1-234,259-297 ##label HOE2 !'##cross-references GB:M28650 !'##experimental_source clone pcDE-72 REFERENCE I55521 !$#authors Hoeijmakers, J.H.J. !$#journal J. Cell Sci. Suppl. (1987) 6:111-125 !$#title Characterization of genes and proteins involved in excision !1repair of human cells. !$#cross-references MUID:88007932; PMID:2821019 !$#accession I55521 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-297 ##label HOE3 !'##cross-references GB:M28650; NID:g182176; PIDN:AAA35810.1; !1PID:g182177 REFERENCE A24781 !$#authors Van Duin, M.; De Wit, J.; Odijk, H.; Westerveld, A.; Yasui, !1A.; Koken, M.H.M.; Hoeijmakers, J.H.J.; Bootsma, D. !$#journal Cell (1986) 44:913-923 !$#title Molecular characterization of the human excision repair gene !1ERCC-1: cDNA cloning and amino acid homology with the yeast !1DNA repair gene RAD10. !$#cross-references MUID:86161680; PMID:2420469 !$#accession A24781 !'##molecule_type mRNA !'##residues 1-297 ##label VAN !'##cross-references GB:M13194; NID:g567007; PIDN:AAA52394.1; !1PID:g182174 GENETICS !$#gene GDB:ERCC1 !'##cross-references GDB:119111; OMIM:126380 !$#map_position 19q13.3-19q13.3 !$#introns 35/3; 107/3; 142/2; 175/3; 201/2; 234/3; 258/3; 281/3 CLASSIFICATION #superfamily excision repair protein KEYWORDS alternative splicing; DNA binding; nucleus FEATURE !$1-297 #product excision repair protein, long splice form !8#status predicted #label MATL\ !$1-234,259-297 #product excision repair protein, short splice form !8#status predicted #label MATS SUMMARY #length 297 #molecular-weight 32562 #checksum 6160 SEQUENCE /// ENTRY A24576 #type complete TITLE RAD10 protein - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YML095c ORGANISM #formal_name Saccharomyces cerevisiae DATE 08-Aug-1987 #sequence_revision 08-Mar-1996 #text_change 21-Jul-2000 ACCESSIONS A24576; S49631; S25394; B22726 REFERENCE A24576 !$#authors Reynolds, P.; Prakash, L.; Dumais, D.; Perozzi, G.; Prakash, !1S. !$#journal EMBO J. (1985) 4:3549-3552 !$#title Nucleotide sequence of the RAD10 gene of Saccharomyces !1cerevisiae. !$#cross-references MUID:86135994; PMID:3912171 !$#accession A24576 !'##molecule_type DNA !'##residues 1-210 ##label REY !'##cross-references EMBL:X05225; NID:g4262; PIDN:CAA28856.1; PID:g4263 REFERENCE S49627 !$#authors Gentles, S.; Bowman, S. !$#submission submitted to the EMBL Data Library, November 1994 !$#accession S49631 !'##molecule_type DNA !'##residues 1-210 ##label GEN !'##cross-references EMBL:Z46660; NID:g575702; PIDN:CAA86642.1; !1PID:g575707; GSPDB:GN00013; MIPS:YML095c REFERENCE S25394 !$#authors Weiss, W.A.; Friedberg, E.C. !$#journal EMBO J. (1985) 4:3907 !$#contents erratum !$#accession S25394 !'##molecule_type DNA !'##residues 170-210 ##label WEI !'##cross-references EMBL:X02591 !'##note this is a revision to the sequence from reference A91006 REFERENCE A91006 !$#authors Weiss, W.A.; Friedberg, E.C. !$#journal EMBO J. (1985) 4:1575-1582 !$#title Molecular cloning and characterization of the yeast RAD10 !1gene and expression of RAD10 protein in E. coli. !$#cross-references MUID:85284950; PMID:3896774 !$#accession B22726 !'##molecule_type DNA !'##residues 1-169,'EH',172-178,'M',191-192,'QNYVCSRIYST',196,'SI' !1##label WE2 !'##cross-references EMBL:X02591 !'##note this sequence has been revised in reference S25394 GENETICS !$#gene SGD:RAD10; MIPS:YML095c !'##cross-references SGD:S0004560; MIPS:YML095c !$#map_position 13L CLASSIFICATION #superfamily RAD10 protein KEYWORDS DNA binding; nucleus SUMMARY #length 210 #molecular-weight 24311 #checksum 5515 SEQUENCE /// ENTRY I38886 #type complete TITLE DNA excision repair protein XPAC - human ALTERNATE_NAMES xeroderma pigmentosum group A-complementing ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS I38886; S13290 REFERENCE I38886 !$#authors Satokata, I.; Iwai, K.; Matsuda, T.; Okada, Y.; Tanaka, K. !$#journal Gene (1993) 136:345-348 !$#title Genomic characterization of the human DNA excision !1repair-controlling gene XPAC. !$#cross-references MUID:94124028; PMID:8294029 !$#accession I38886 !'##status translation not shown !'##molecule_type DNA !'##residues 1-57 ##label RES !'##cross-references EMBL:U16815; NID:g595928; PIDN:AAB60404.1; !1PID:g595929 !'##note intron-exon junctions are also shown REFERENCE S13290 !$#authors Tanaka, K.; Miura, N.; Satokata, I.; Miyamoto, I.; Yoshida, !1M.C.; Satoh, Y.; Kondo, S.; Yasui, A.; Okayama, H.; Okada, !1Y. !$#journal Nature (1990) 348:73-76 !$#title Analysis of a human DNA excision repair gene involved in !1group A xeroderma pigmentosum and containing a zinc-finger !1domain. !$#cross-references MUID:91043046; PMID:2234061 !$#accession S13290 !'##status preliminary !'##molecule_type mRNA !'##residues 1-273 ##label TAN !'##cross-references GB:D14533; NID:g286028; PIDN:BAA03403.1; !1PID:g286029 GENETICS !$#gene GDB:XPA; XPAC !'##cross-references GDB:125363; OMIM:278700 !$#map_position 9q22.3-9q22.3 CLASSIFICATION #superfamily DNA excision repair protein XPAC KEYWORDS DNA excision; DNA repair SUMMARY #length 273 #molecular-weight 31368 #checksum 3556 SEQUENCE /// ENTRY S41498 #type complete TITLE DNA excision repair protein XPAC - mouse ALTERNATE_NAMES Xeroderma pigmentosum group A-complementing protein ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S41498 REFERENCE S41498 !$#authors van Oostrom, C.T.M.; de Vries, A.; Verbeek, S.J.; van !1Kreijl, C.F.; van Steeg, H. !$#journal Nucleic Acids Res. (1994) 22:11-14 !$#title Cloning and characterization of the mouse XPAC gene. !$#cross-references MUID:94173654; PMID:8127648 !$#accession S41498 !'##status preliminary; translation not shown !'##molecule_type mRNA !'##residues 1-272 ##label VAN !'##cross-references EMBL:X74351; NID:g440564; PIDN:CAA52393.1; !1PID:g440565 CLASSIFICATION #superfamily DNA excision repair protein XPAC KEYWORDS DNA binding; zinc finger SUMMARY #length 272 #molecular-weight 31399 #checksum 9768 SEQUENCE /// ENTRY JQ1324 #type complete TITLE DNA excision repair protein XPAC - African clawed frog ALTERNATE_NAMES xeroderma pigmentosum group A-complementing protein homolog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS JQ1324; JS0643 REFERENCE JQ1323 !$#authors Shimamoto, T.; Kohno, K.; Tanaka, K.; Okada, Y. !$#journal Biochem. Biophys. Res. Commun. (1991) 181:1231-1237 !$#title Molecular cloning of human XPAC gene homologs from chicken, !1Xenopus laevis and Drosophila melanogaster. !$#cross-references MUID:92109732; PMID:1764072 !$#accession JQ1324 !'##molecule_type mRNA !'##residues 1-267 ##label SHI !'##cross-references GB:D31894; NID:g505147; PIDN:BAA06692.1; !1PID:g505148 !'##experimental_source liver !$#accession JS0643 !'##molecule_type mRNA !'##residues 1-6,9-267 ##label SH2 CLASSIFICATION #superfamily DNA excision repair protein XPAC KEYWORDS DNA binding; DNA repair; nucleus; zinc finger FEATURE !$97-121 #region zinc finger SUMMARY #length 267 #molecular-weight 31180 #checksum 771 SEQUENCE /// ENTRY JQ1323 #type complete TITLE DNA excision repair protein XPAC - chicken ALTERNATE_NAMES Xeroderma pigmentosum group A-complementing protein ORGANISM #formal_name Gallus gallus #common_name chicken DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS JQ1323 REFERENCE JQ1323 !$#authors Shimamoto, T.; Kohno, K.; Tanaka, K.; Okada, Y. !$#journal Biochem. Biophys. Res. Commun. (1991) 181:1231-1237 !$#title Molecular cloning of human XPAC gene homologs from chicken, !1Xenopus laevis and Drosophila melanogaster. !$#cross-references MUID:92109732; PMID:1764072 !$#accession JQ1323 !'##molecule_type mRNA !'##residues 1-267 ##label SHI !'##cross-references GB:D31896; NID:g505066; PIDN:BAA06694.1; !1PID:g505067 !'##experimental_source embryo GENETICS !$#gene XPAC CLASSIFICATION #superfamily DNA excision repair protein XPAC KEYWORDS DNA binding; nucleus; zinc finger FEATURE !$99-123 #region zinc finger SUMMARY #length 267 #molecular-weight 30978 #checksum 8162 SEQUENCE /// ENTRY JQ1325 #type complete TITLE DNA excision repair protein XPAC - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES Xeroderma pigmentosum group A-complementing protein ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JQ1325 REFERENCE JQ1323 !$#authors Shimamoto, T.; Kohno, K.; Tanaka, K.; Okada, Y. !$#journal Biochem. Biophys. Res. Commun. (1991) 181:1231-1237 !$#title Molecular cloning of human XPAC gene homologs from chicken, !1Xenopus laevis and Drosophila melanogaster. !$#cross-references MUID:92109732; PMID:1764072 !$#accession JQ1325 !'##molecule_type mRNA !'##residues 1-296 ##label SHI GENETICS !$#gene XPAC !'##cross-references FlyBase:FBgn0004832 CLASSIFICATION #superfamily DNA excision repair protein XPAC KEYWORDS DNA binding; nucleus; zinc finger FEATURE !$126-150 #region zinc finger SUMMARY #length 296 #molecular-weight 33875 #checksum 9354 SEQUENCE /// ENTRY A35661 #type complete TITLE DNA excision repair cross-complementing protein ERCC3 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 17-Nov-2000 ACCESSIONS A35661; S40625 REFERENCE A35661 !$#authors Weeda, G.; van Ham, R.C.A.; Vermeulen, W.; Bootsma, D.; van !1der Eb, A.J.; Hoeijmakers, J.H.J. !$#journal Cell (1990) 62:777-791 !$#title A presumed DNA helicase encoded by ERCC-3 is involved in the !1human repair disorders xeroderma pigmentosum and Cockayne's !1syndrome. !$#cross-references MUID:90352711; PMID:2167179 !$#accession A35661 !'##molecule_type mRNA !'##residues 1-782 ##label WE1 !'##cross-references GB:M31899; NID:g182178; PIDN:AAA52396.1; !1PID:g182179 REFERENCE S40625 !$#authors Weeda, G.; Ma, L.; van Ham, R.C.A.; van der Eb, A.J.; !1Hoeijmakers, J.H.J. !$#journal Nucleic Acids Res. (1991) 19:6301-6308 !$#title Structure and expression of the human XPBC/ERCC-3 gene !1involved in DNA repair disorders xeroderma pigmentosum and !1Cockayne's syndrome. !$#cross-references MUID:92066484; PMID:1956789 !$#accession S40625 !'##molecule_type mRNA !'##residues 1-782 ##label WE2 !'##cross-references EMBL:M31899; NID:g182178; PID:g182179 GENETICS !$#gene GDB:ERCC3 !'##cross-references GDB:119881; OMIM:133510 !$#map_position 2q21-2q21 CLASSIFICATION #superfamily DNA excision repair cross-complementing protein !1ERCC3 KEYWORDS DNA binding; DNA repair; nucleus SUMMARY #length 782 #molecular-weight 89277 #checksum 1627 SEQUENCE /// ENTRY A48994 #type complete TITLE DNA excision repair cross-complementing protein ERCC3 - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 17-Nov-2000 ACCESSIONS A48994 REFERENCE A48994 !$#authors Weeda, G.; Ma, L.; van Ham, R.C.; Bootsma, D.; van der Eb, !1A.J.; Hoeijmakers, J.H. !$#journal Carcinogenesis (1991) 12:2361-2368 !$#title Characterization of the mouse homolog of the XPBC/ERCC-3 !1gene implicated in xeroderma pigmentosum and Cockayne's !1syndrome. !$#cross-references MUID:92083629; PMID:1747940 !$#accession A48994 !'##molecule_type mRNA !'##residues 1-783 ##label WEE !'##cross-references GB:S71186; NID:g240582; PIDN:AAB20614.1; !1PID:g240583 !'##note sequence extracted from NCBI backbone (NCBIN:71186, !1NCBIP:71188) CLASSIFICATION #superfamily DNA excision repair cross-complementing protein !1ERCC3 KEYWORDS DNA binding; DNA repair; nucleus SUMMARY #length 783 #molecular-weight 89126 #checksum 3997 SEQUENCE /// ENTRY A44223 #type complete TITLE DNA excision repair cross-complementing protein ERCC3 - fruit fly (Drosophila melanogaster) ALTERNATE_NAMES haywire protein ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 17-Nov-2000 ACCESSIONS A44223; S26719 REFERENCE A44223 !$#authors Mounkes, L.C.; Jones, R.S.; Liang, B.C.; Gelbart, W.; !1Fuller, M.T. !$#journal Cell (1992) 71:925-937 !$#title A Drosophila model for xeroderma pigmentosum and Cockayne's !1syndrome: haywire encodes the fly homolog of ERCC3, a human !1excision repair gene. !$#cross-references MUID:93092213; PMID:1458540 !$#accession A44223 !'##molecule_type mRNA !'##residues 1-802 ##label MOU !'##note sequence extracted from NCBI backbone (NCBIP:120231) REFERENCE S26718 !$#authors Koken, M.H.M.; Vreeken, C.; Bol, S.A.M.; Cheng, N.C.; !1Jaspers-Dekker, I.; Hoeijmakers, J.H.J.; Eeken, J.C.J.; !1Weeda, G.; Pastink, A. !$#journal Nucleic Acids Res. (1992) 20:5541-5548 !$#title Cloning and characterization of the Drosophila homolog of !1the xeroderma pigmentosum complementation-group B correcting !1gene, ERCC3. !$#cross-references MUID:93087159; PMID:1454518 !$#accession S26719 !'##molecule_type mRNA !'##residues 1-22,'AE',25-282,'AN',286-556,'M',557-802 ##label KOK !'##cross-references EMBL:X68309; NID:g11077; PIDN:CAA48386.1; !1PID:g11079 GENETICS !$#gene FlyBase:hay !'##cross-references FlyBase:FBgn0001179 CLASSIFICATION #superfamily DNA excision repair cross-complementing protein !1ERCC3 KEYWORDS DNA binding; DNA repair; nucleus SUMMARY #length 802 #molecular-weight 90687 #checksum 1083 SEQUENCE /// ENTRY S71206 #type complete TITLE DNA excision repair cross-complementing protein ERCC3 - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 17-Nov-2000 ACCESSIONS S71206 REFERENCE S71206 !$#authors Ribeiro, D.T.; Machado, C.R.; Menck, C.F.M. !$#submission submitted to the EMBL Data Library, June 1995 !$#description A cDNA from Arabidopsis thaliana homologue to XPB human DNA !1repair and TFIIH component. !$#accession S71206 !'##molecule_type mRNA !'##residues 1-757 ##label RIB !'##cross-references EMBL:U29168 CLASSIFICATION #superfamily DNA excision repair cross-complementing protein !1ERCC3 KEYWORDS DNA binding; DNA repair; nucleus SUMMARY #length 757 #molecular-weight 85963 #checksum 777 SEQUENCE /// ENTRY S31272 #type complete TITLE DNA excision repair cross-complementing protein ERCC3 [validated] - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YIL143c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 17-Nov-2000 ACCESSIONS S31272; S48391; S31246 REFERENCE S31272 !$#authors Gulyas, K.D.; Donahue, T.F. !$#journal Cell (1992) 69:1031-1042 !$#title SSL2, a suppressor of a stem-loop mutation in the HIS4 !1leader encodes the yeast homolog of human ERCC-3. !$#cross-references MUID:92298384; PMID:1318786 !$#accession S31272 !'##molecule_type DNA !'##residues 1-843 ##label GUL !'##cross-references EMBL:M94176; NID:g172723; PIDN:AAA35102.1; !1PID:g172724 REFERENCE S48373 !$#authors Churcher, C. !$#submission submitted to the EMBL Data Library, September 1994 !$#accession S48391 !'##molecule_type DNA !'##residues 1-843 ##label CHU !'##cross-references GB:Z47047; EMBL:Z38059; NID:g603997; PID:g763203; !1GSPDB:GN00009; MIPS:YIL143c REFERENCE S31246 !$#authors Park, E.; Guzder, S.N.; Koken, M.H.M.; Jaspers-Dekker, I.; !1Weeda, G.; Hoeijmakers, J.H.J.; Prakash, S.; Prakash, L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:11416-11420 !$#title RAD25 (SSL2), the yeast homolog of the human xeroderma !1pigmentosum group B DNA repair gene, is essential for !1viability. !$#cross-references MUID:93087538; PMID:1333609 !$#accession S31246 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-8,'S',10-47,'L',49-843 ##label PAR !'##cross-references EMBL:L01414; NID:g172326; PIDN:AAA34942.1; !1PID:g172327 GENETICS !$#gene SGD:SSL2; RAD25; LOM3; MIPS:YIL143c !'##cross-references SGD:S0001405; MIPS:YIL143c !$#map_position 9L FUNCTION !$#description essential for nucleotide excision repair and involved in the !1RNA polymerase II transcription initiation complex TFIIH !1[validated, MUID:96195586] !$#note the C-terminus of SSL2 (suppressor of stem loop) is !1essential for overall genomic excision repair and !1transcription-coupled repair [validated, MUID:94124529] CLASSIFICATION #superfamily DNA excision repair cross-complementing protein !1ERCC3 KEYWORDS DNA binding; DNA repair; nucleus SUMMARY #length 843 #molecular-weight 95340 #checksum 140 SEQUENCE /// ENTRY S59442 #type complete TITLE DNA repair protein RAD14 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YM8325.02c; protein YMR201c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 12-Nov-1999 ACCESSIONS S59442; S26709 REFERENCE S59441 !$#authors Odell, C.; Bowman, S. !$#submission submitted to the EMBL Data Library, March 1995 !$#accession S59442 !'##molecule_type DNA !'##residues 1-371 ##label ODE !'##cross-references EMBL:Z48755; NID:g736296; PIDN:CAA88642.1; !1PID:g736298; GSPDB:GN00013; MIPS:YMR201c !'##experimental_source strain AB972 REFERENCE S26709 !$#authors Bankmann, M.; Prakash, L.; Prakash, S. !$#journal Nature (1992) 355:555-558 !$#title Yeast RAD14 and human xeroderma pigmentosum group A !1DNA-repair genes encode homologous proteins. !$#cross-references MUID:92158051; PMID:1741034 !$#accession S26709 !'##molecule_type DNA !'##residues 125-371 ##label BAN !'##cross-references EMBL:X64064; NID:g4264; PIDN:CAA45420.1; PID:g4265 GENETICS !$#gene RAD14; SGD:S0004814 !'##cross-references MIPS:YMR201c; SGD:S0004814 !$#map_position 13R !$#introns 9/3 CLASSIFICATION #superfamily DNA repair protein RAD14 KEYWORDS ATP; DNA binding; DNA repair; zinc finger SUMMARY #length 371 #molecular-weight 43038 #checksum 3972 SEQUENCE /// ENTRY DDBY18 #type complete TITLE DNA repair protein RAD18 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YCR066w ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 21-Jul-2000 ACCESSIONS S05802; S22263; S19481; JS0082 REFERENCE S05802 !$#authors Jones, J.S.; Weber, S.; Prakash, L. !$#journal Nucleic Acids Res. (1988) 16:7119-7131 !$#title The Saccharomyces cerevisiae RAD18 gene encodes a protein !1that contains potential zinc finger domains for nucleic acid !1binding and a putative nucleotide binding sequence. !$#cross-references MUID:88303333; PMID:2970061 !$#accession S05802 !'##molecule_type DNA !'##residues 1-487 ##label JON !'##cross-references EMBL:X12588; NID:g4266; PIDN:CAA31101.1; PID:g4267 REFERENCE S22260 !$#authors Benit, P.; Chanet, R.; Fabre, F.; Faye, G.; Fukuhara, H.; !1Sor, F. !$#journal Yeast (1992) 8:147-153 !$#title Sequence of the sup61-RAD18 region on chromosome III of !1Saccharomyces cerevisiae. !$#cross-references MUID:92221691; PMID:1561837 !$#accession S22263 !'##molecule_type DNA !'##residues 1-487 ##label BEN !'##cross-references GB:X59720; EMBL:S93798; NID:g1907116; !1PIDN:CAA42281.1; PID:g1907206 REFERENCE S19477 !$#authors Antoine, G.; Benit, P.; Chanet, R.; Fabre, R.; Faye, G.; !1Fukuhara, H.; Mathieu, A.; Sor, F. !$#submission submitted to the Protein Sequence Database, March 1992 !$#accession S19481 !'##molecule_type DNA !'##residues 1-487 ##label ANT !'##cross-references EMBL:X59720; NID:g1907116; PIDN:CAA42281.1; !1PID:g1907206; GSPDB:GN00003; MIPS:YCR066w REFERENCE JS0082 !$#authors Chanet, R.; Magana-Schwencke, N.; Fabre, F. !$#journal Gene (1988) 74:543-547 !$#title Potential DNA-binding domains in the RAD18 gene product of !1Saccharomyces cerevisiae. !$#cross-references MUID:89232745; PMID:3073108 !$#accession JS0082 !'##molecule_type DNA !'##residues 1-487 ##label CHA !'##cross-references GB:M36405; NID:g172321; PIDN:AAA34932.1; !1PID:g172322 GENETICS !$#gene SGD:RAD18; MIPS:YCR066w !'##cross-references SGD:S0000662; MIPS:YCR066w !$#map_position 3R CLASSIFICATION #superfamily DNA repair protein RAD18; RING finger homology KEYWORDS ATP; DNA binding; DNA repair; zinc finger FEATURE !$24-71 #domain RING finger homology #label RNG\ !$28-65 #region zinc finger C3HC4 motif\ !$190-210 #region zinc finger CCHC motif\ !$366 #binding_site ATP (Lys) #status predicted SUMMARY #length 487 #molecular-weight 55230 #checksum 1135 SEQUENCE /// ENTRY S64859 #type complete TITLE DNA repair protein RAD5 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein L1767; protein YLR032w; REV2 protein ORGANISM #formal_name Saccharomyces cerevisiae DATE 01-Aug-1995 #sequence_revision 24-May-1996 #text_change 16-Jun-2000 ACCESSIONS S64859; S31301; S26983 REFERENCE S64845 !$#authors Obermaier, B.; Piravandi, E.; Rinke, M. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64859 !'##molecule_type DNA !'##residues 1-1169 ##label OBE !'##cross-references EMBL:Z73204; NID:g1360347; PIDN:CAA97556.1; !1PID:g1360348; GSPDB:GN00012; MIPS:YLR032w !'##experimental_source strain S288C REFERENCE S31301 !$#authors Johnson, R.E.; Henderson, S.T.; Petes, T.D.; Prakash, S.; !1Bankmann, M.; Prakash, L. !$#journal Mol. Cell. Biol. (1992) 12:3807-3818 !$#title Saccharomyces cerevisiae RAD5-encoded DNA repair protein !1contains DNA helicase and zinc-binding sequence motifs and !1affects the stability of simple repetitive sequences in the !1genome. !$#cross-references MUID:92375048; PMID:1324406 !$#accession S31301 !'##molecule_type DNA !'##residues 1-1169 ##label JOH !'##cross-references EMBL:M96644; NID:g172346; PIDN:AAA34951.1; !1PID:g172347 REFERENCE S26983 !$#authors Ahne, F.; Baur, M.; Eckardt-Schupp, F. !$#journal Curr. Genet. (1992) 22:277-282 !$#title The REV2 gene of Saccharomyces cerevisiae: cloning and DNA !1sequence. !$#cross-references MUID:93008350; PMID:1394508 !$#accession S26983 !'##molecule_type DNA !'##residues 402-477,'R',479-634,'N',636-845,'S',847-897,'S',899-972, !1'A',974-1062,'R' ##label AHN !'##cross-references EMBL:S46103; NID:g257211; PIDN:AAB23590.1; !1PID:g257212 GENETICS !$#gene SGD:RAD5; REV2; SNM2; MIPS:YLR032w !'##cross-references SGD:S0004022; MIPS:YLR032w !$#map_position 12R CLASSIFICATION #superfamily DNA repair protein RAD5; RING finger homology KEYWORDS DNA repair; leucine zipper; zinc finger FEATURE !$910-966 #domain RING finger homology #label RNG\ !$914-960 #region zinc finger C3HC4 motif SUMMARY #length 1169 #molecular-weight 134001 #checksum 8376 SEQUENCE /// ENTRY S41478 #type complete TITLE DNA repair protein rad8 - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES protein SPAC13G6.01c; rad8p helicase ORGANISM #formal_name Schizosaccharomyces pombe DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 06-Oct-2000 ACCESSIONS S41478; S41482; S62430; S55492; T37636; T38978 REFERENCE S41478 !$#authors Watts, F.Z. !$#submission submitted to the EMBL Data Library, August 1993 !$#accession S41478 !'##molecule_type DNA !'##residues 1-1133 ##label WAT !'##cross-references EMBL:X74615; NID:g443972; PIDN:CAA52686.1; !1PID:g443973 REFERENCE S41482 !$#authors Doe, C.L.; Murray, J.M.; Shayeghi, M.; Hoskins, M.; Lehmann, !1A.R.; Carr, A.M.; Watts, F.Z. !$#journal Nucleic Acids Res. (1993) 21:5964-5971 !$#title Cloning and characterisation of the Schizosaccharomyces !1pombe rad8 gene, a member of the SNF2 helicase family. !$#cross-references MUID:94119698; PMID:8290359 !$#accession S41482 !'##molecule_type DNA !'##residues !1524-542;573-581;652-669;680-701;741-750;874-925;1030-1059; !11069-1087 ##label DOE REFERENCE S62430 !$#authors Odell, C.; Bowman, S. !$#submission submitted to the EMBL Data Library, October 1995 !$#accession S62430 !'##molecule_type DNA !'##residues 1-1070 ##label ODE !'##cross-references EMBL:Z54308; NID:g1008985; PIDN:CAA91094.1; !1PID:g1008986 REFERENCE S55479 !$#authors Connor, R.; Churcher, C.M. !$#submission submitted to the EMBL Data Library, May 1995 !$#accession S55492 !'##molecule_type DNA !'##residues 1030-1133 ##label CON !'##cross-references EMBL:Z49811; NID:g854599; PIDN:CAA89964.1; !1PID:g871545 REFERENCE Z21734 !$#authors Odell, C.; Bowman, S.; Barrell, B.G.; Rajandream, M.A.; !1Walsh, S.V.; Wood, V. !$#submission submitted to the EMBL Data Library, October 1995 !$#accession T37636 !'##molecule_type DNA !'##residues 1-1070 ##label OD2 !'##cross-references EMBL:Z54308; PIDN:CAA91094.1; GSPDB:GN00066; !1SPDB:SPAC13G6.01c REFERENCE Z21821 !$#authors Connor, R.; Churcher, C.M.; Barrell, B.G.; Rajandream, M.A.; !1Walsh, S.V. !$#submission submitted to the EMBL Data Library, May 1995 !$#accession T38978 !'##molecule_type DNA !'##residues 1030-1133 ##label CO2 !'##cross-references EMBL:Z49811; PIDN:CAA89964.1; GSPDB:GN00066; !1SPDB:SPAC5H10.14c !'##experimental_source strain 972h-; cosmid c5H10 GENETICS !$#gene rad8; SPDB:SPAC5H10.14c !$#map_position 1L !$#introns #status absent CLASSIFICATION #superfamily DNA repair protein RAD5; RING finger homology KEYWORDS DNA binding; nucleus; zinc FEATURE !$873-928 #domain RING finger homology #label RNG SUMMARY #length 1133 #molecular-weight 128609 #checksum 7159 SEQUENCE /// ENTRY D69093 #type complete TITLE DNA repair protein Rad51 homolog - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS D69093 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession D69093 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-234 ##label MTH !'##cross-references GB:AE000927; GB:AE000666; NID:g2622822; !1PIDN:AAB86165.1; PID:g2622824 !'##experimental_source strain Delta H GENETICS !$#gene MTH1693 CLASSIFICATION #superfamily Methanococcus DNA repair protein RAD51 SUMMARY #length 234 #molecular-weight 26193 #checksum 8422 SEQUENCE /// ENTRY G64331 #type complete TITLE DNA repair protein RAD51 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G64331 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession G64331 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-212 ##label BUL !'##cross-references GB:U67480; GB:L77117; NID:g2826265; !1PIDN:AAB98241.1; PID:g1590984; TIGR:MJ0254 GENETICS !$#map_position FOR239969-240607 CLASSIFICATION #superfamily Methanococcus DNA repair protein RAD51 SUMMARY #length 212 #molecular-weight 23842 #checksum 3940 SEQUENCE /// ENTRY H69511 #type complete TITLE DNA repair protein REC homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS H69511 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession H69511 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-221 ##label KLE !'##cross-references GB:AE000959; GB:AE000782; NID:g2689282; !1PIDN:AAB89159.1; PID:g2648436; TIGR:AF2096 CLASSIFICATION #superfamily Methanococcus DNA repair protein RAD51 SUMMARY #length 221 #molecular-weight 24936 #checksum 5705 SEQUENCE /// ENTRY E71232 #type complete TITLE probable DNA repair protein - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E71232 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession E71232 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-228 ##label KAW !'##cross-references GB:AP000001; NID:g3236128; PIDN:BAA29188.1; !1PID:g3256505 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0119 CLASSIFICATION #superfamily Methanococcus DNA repair protein RAD51 SUMMARY #length 228 #molecular-weight 25536 #checksum 6286 SEQUENCE /// ENTRY JC1417 #type complete TITLE DNA repair protein sms - Escherichia coli (strain K-12) ALTERNATE_NAMES DNA repair protein radA ORGANISM #formal_name Escherichia coli DATE 30-Apr-1999 #sequence_revision 30-Apr-1999 #text_change 01-Mar-2002 ACCESSIONS JC1417; S56613; D65254; S18877 REFERENCE JC1417 !$#authors Neuwald, A.F.; Berg, D.E.; Stauffer, G.V. !$#journal Gene (1992) 120:1-9 !$#title Mutational analysis of the Escherichia coli serB promoter !1region reveals transcriptional linkage to a downstream gene. !$#cross-references MUID:93013006; PMID:1327967 !$#accession JC1417 !'##molecule_type DNA !'##residues 1-460 ##label NEU !'##cross-references EMBL:X63155; NID:g42970; PIDN:CAA44856.1; !1PID:g581233 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56613 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-460 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97285.1; !1PID:g537229 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65254 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-460 ##label BLAT !'##cross-references GB:AE000509; GB:U00096; NID:g2367383; !1PIDN:AAC77342.1; PID:g1790850; UWGP:b4389 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene sms; radA !$#start_codon GTG FUNCTION !$#description imparts resistance to the alkylating agent methylmethane !1sulfonate CLASSIFICATION #superfamily DNA repair protein sms KEYWORDS ATP; DNA binding; DNA repair; nucleotide binding; P-loop; !1zinc finger FEATURE !$11-28 #region zinc finger CCCC motif\ !$102-109 #region nucleotide-binding motif A (P-loop)\ !$173-178 #region nucleotide-binding motif B\ !$108 #binding_site ATP (Lys) #status predicted SUMMARY #length 460 #molecular-weight 49472 #checksum 7337 SEQUENCE /// ENTRY I64131 #type complete TITLE DNA repair protein sms - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES DNA repair protein radA ORGANISM #formal_name Haemophilus influenzae DATE 30-Apr-1999 #sequence_revision 30-Apr-1999 #text_change 19-Jan-2001 ACCESSIONS I64131 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession I64131 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-475 ##label TIGR !'##cross-references GB:U32833; GB:L42023; NID:g1574432; !1PIDN:AAC23242.1; PID:g1574440; TIGR:HI1597 GENETICS !$#gene sms; radA; HI1597 !$#start_codon GTG FUNCTION !$#description may impart resistance to DNA alkylation CLASSIFICATION #superfamily DNA repair protein sms KEYWORDS ATP; DNA binding; DNA repair; nucleotide binding; P-loop; !1zinc finger FEATURE !$28-45 #region zinc finger CCCC motif\ !$117-124 #region nucleotide-binding motif A (P-loop)\ !$188-193 #region nucleotide-binding motif B\ !$123 #binding_site ATP (Lys) #status predicted SUMMARY #length 475 #molecular-weight 51168 #checksum 2577 SEQUENCE /// ENTRY S66116 #type complete TITLE DNA repair protein sms - Bacillus subtilis ALTERNATE_NAMES DNA repair protein radA ORGANISM #formal_name Bacillus subtilis DATE 30-Apr-1999 #sequence_revision 30-Apr-1999 #text_change 19-Jan-2001 ACCESSIONS S66116; I40509; A69709 REFERENCE S65967 !$#authors Ogasawara, N.; Nakai, S.; Yoshikawa, H. !$#journal DNA Res. (1994) 1:1-14 !$#title Systematic sequencing of the 180 kilobase region of the !1Bacillus subtilis chromosome containing the replication !1origin. !$#cross-references MUID:96051385; PMID:7584024 !$#accession S66116 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-458 ##label OGA !'##cross-references EMBL:D26185; NID:g467326; PIDN:BAA05321.1; !1PID:g467475 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1993 REFERENCE I40507 !$#authors Msadek, T.; Kunst, F.; Rapoport, G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1994) 91:5788-5792 !$#title MecB of Bacillus subtilis, a member of the ClpC ATPase !1family, is a pleiotropic regulator controlling competence !1gene expression and growth at high temperature. !$#cross-references MUID:94286523; PMID:8016066 !$#accession I40509 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-260 ##label RES !'##cross-references EMBL:U02604; NID:g442358; PIDN:AAA19234.1; !1PID:g442361 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69709 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-458 ##label KUN !'##cross-references GB:Z99104; GB:AL009126; NID:g2632267; !1PIDN:CAB11863.1; PID:g2632354 !'##experimental_source strain 168 GENETICS !$#gene sms FUNCTION !$#description may impart resistance to DNA alkylation CLASSIFICATION #superfamily DNA repair protein sms KEYWORDS ATP; DNA binding; DNA repair; nucleotide binding; P-loop; !1zinc finger FEATURE !$10-27 #region zinc finger CCCC motif\ !$98-105 #region nucleotide-binding motif A (P-loop)\ !$170-175 #region nucleotide-binding motif B\ !$104 #binding_site ATP (Lys) #status predicted SUMMARY #length 458 #molecular-weight 49483 #checksum 6594 SEQUENCE /// ENTRY S76229 #type complete TITLE DNA repair protein sms - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES DNA repair protein radA ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 30-Apr-1999 #sequence_revision 30-Apr-1999 #text_change 19-Jan-2001 ACCESSIONS S76229 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76229 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-505 ##label KAN !'##cross-references EMBL:D90914; GB:AB001339; NID:g1653477; !1PIDN:BAA18488.1; PID:g1653575 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 FUNCTION !$#description may impart resistance to DNA alkylation CLASSIFICATION #superfamily DNA repair protein sms KEYWORDS ATP; DNA binding; DNA repair; nucleotide binding; P-loop; !1zinc finger FEATURE !$10-27 #region zinc finger CCCC motif\ !$107-114 #region nucleotide-binding motif A (P-loop)\ !$196-201 #region nucleotide-binding motif B\ !$113 #binding_site ATP (Lys) #status predicted SUMMARY #length 505 #molecular-weight 54191 #checksum 5575 SEQUENCE /// ENTRY C72126 #type complete TITLE DNA repair protein sms CP0722 [similarity] - Chlamydophila pneumoniae (strains CWL029 and AR39) ALTERNATE_NAMES DNA repair protein radA ORGANISM #formal_name Chlamydophila pneumoniae, Chlamydia pneumoniae DATE 30-Apr-1999 #sequence_revision 30-Apr-1999 #text_change 19-Jan-2001 ACCESSIONS C72126; D81545 REFERENCE A72000 !$#authors Kalman, S.; Mitchell, W.; Marathe, R.; Lammel, C.; Fan, J.; !1Olinger, L.; Grimwood, J.; Davis, R.W.; Stephens, R.S. !$#journal Nature Genet. (1999) 21:385-389 !$#title Comparative genomes of Clamydia pneumoniae and C. !1trachomatis. !$#cross-references MUID:99206606; PMID:10192388 !$#accession C72126 !'##molecule_type DNA !'##residues 1-453 ##label ARN !'##cross-references GB:AE001590; GB:AE001363; NID:g4376299; !1PIDN:AAD18206.1; PID:g4376308 !'##experimental_source strain CWL029 REFERENCE A81500 !$#authors Read, T.D.; Brunham, R.C.; Shen, C.; Gill, S.R.; Heidelberg, !1J.F.; White, O.; Hickey, E.K.; Peterson, J.; Utterback, T.; !1Berry, K.; Bass, S.; Linher, K.; Weidman, J.; Khouri, H.; !1Craven, B.; Bowman, C.; Dodson, R.; Gwinn, M.; Nelson, W.; !1DeBoy, R.; Kolonay, J.; McClarty, G.; Salzberg, S.L.; Eisen, !1J.; Fraser, C.M. !$#journal Nucleic Acids Res. (2000) 28:1397-1406 !$#title Genome sequences of Chlamydia trachomatis MoPn and Chlamydia !1pneumoniae AR39. !$#cross-references MUID:20150255; PMID:10684935 !$#accession D81545 !'##molecule_type DNA !'##residues 1-453 ##label REA !'##cross-references GB:AE002231; GB:AE002161; NID:g7189633; !1PIDN:AAF38527.1; PID:g7189636; GSPDB:GN00122; TIGR:CP0722 !'##experimental_source strain AR39, HL cells GENETICS !$#gene sms; CP0722 FUNCTION !$#description may impart resistance to DNA alkylation CLASSIFICATION #superfamily DNA repair protein sms KEYWORDS ATP; DNA binding; DNA repair; nucleotide binding; P-loop; !1zinc finger FEATURE !$11-28 #region zinc finger CCCC motif\ !$93-100 #region nucleotide-binding motif A (P-loop)\ !$165-170 #region nucleotide-binding motif B\ !$99 #binding_site ATP (Lys) #status predicted SUMMARY #length 453 #molecular-weight 49234 #checksum 3126 SEQUENCE /// ENTRY D71532 #type complete TITLE DNA repair protein sms - Chlamydia trachomatis (serotype D, strain UW3/Cx) ALTERNATE_NAMES DNA repair protein radA ORGANISM #formal_name Chlamydia trachomatis DATE 30-Apr-1999 #sequence_revision 30-Apr-1999 #text_change 19-Jan-2001 ACCESSIONS D71532 REFERENCE A71570 !$#authors Stephens, R.S.; Kalman, S.; Lammel, C.J.; Fan, J.; Marathe, !1R.; Aravind, L.; Mitchell, W.P.; Olinger, L.; Tatusov, R.L.; !1Zhao, Q.; Koonin, E.V.; Davis, R.W. !$#journal Science (1998) 282:754-759 !$#title Genome sequence of an obligate intracellular pathogen of !1humans: Chlamydia trachomatis. !$#cross-references MUID:99000809; PMID:9784136 !$#accession D71532 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-454 ##label ARN !'##cross-references GB:AE001302; GB:AE001273; NID:g3328708; !1PIDN:AAC67891.1; PID:g3328713 !'##experimental_source serotype D, strain UW-3/Cx GENETICS !$#gene sms FUNCTION !$#description may impart resistance to DNA alkylation CLASSIFICATION #superfamily DNA repair protein sms KEYWORDS ATP; DNA binding; DNA repair; nucleotide binding; P-loop; !1zinc finger FEATURE !$11-28 #region zinc finger CCCC motif\ !$94-101 #region nucleotide-binding motif A (P-loop)\ !$166-171 #region nucleotide-binding motif B\ !$100 #binding_site ATP (Lys) #status predicted SUMMARY #length 454 #molecular-weight 49783 #checksum 1085 SEQUENCE /// ENTRY G70349 #type complete TITLE DNA repair protein sms - Aquifex aeolicus ALTERNATE_NAMES DNA repair protein radA ORGANISM #formal_name Aquifex aeolicus DATE 30-Apr-1999 #sequence_revision 30-Apr-1999 #text_change 19-Jan-2001 ACCESSIONS G70349 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession G70349 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-444 ##label AQF !'##cross-references GB:AE000695; NID:g2983180; PIDN:AAC06790.1; !1PID:g2983190; GB:AE000657 !'##experimental_source strain VF5 GENETICS !$#gene sms FUNCTION !$#description may impart resistance to DNA alkylation CLASSIFICATION #superfamily DNA repair protein sms KEYWORDS ATP; DNA binding; DNA repair; nucleotide binding; P-loop; !1zinc finger FEATURE !$10-27 #region zinc finger CCCC motif\ !$91-98 #region nucleotide-binding motif A (P-loop)\ !$162-167 #region nucleotide-binding motif B\ !$97 #binding_site ATP (Lys) #status predicted SUMMARY #length 444 #molecular-weight 49047 #checksum 6964 SEQUENCE /// ENTRY D71960 #type complete TITLE DNA repair protein sms - Helicobacter pylori (strain J99) ALTERNATE_NAMES DNA repair protein radA ORGANISM #formal_name Helicobacter pylori #variety strain J99 DATE 30-Apr-1999 #sequence_revision 30-Apr-1999 #text_change 19-Jan-2001 ACCESSIONS D71960 REFERENCE A71800 !$#authors Alm, R.A.; Ling, L.S.L.; Moir, D.T.; King, B.L.; Brown, !1E.D.; Doig, P.C.; Smith, D.R.; Noonan, B.; Guild, B.C.; !1deJonge, B.L.; Carmel, G.; Tummino, P.J.; Caruso, A.; !1Uria-Nickelsen, M.; Mills, D.M.; Ives, C.; Gibson, R.; !1Merberg, D.; Mills, S.D.; Jiang, Q.; Taylor, D.E.; Vovis, !1G.F.; Trust, T.J. !$#journal Nature (1999) 397:176-180 !$#title Genomic sequence comparison of two unrelated isolates of the !1human gastric pathogen Helicobacter pylori. !$#cross-references MUID:99120557; PMID:9923682 !$#accession D71960 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-448 ##label ARN !'##cross-references GB:AE001459; GB:AE001439; NID:g4154723; !1PIDN:AAD05792.1; PID:g4154730 !'##experimental_source strain J99 GENETICS !$#gene radA; sms FUNCTION !$#description may impart resistance to DNA alkylation CLASSIFICATION #superfamily DNA repair protein sms KEYWORDS ATP; DNA binding; DNA repair; nucleotide binding; P-loop; !1zinc finger FEATURE !$10-27 #region zinc finger CCCC motif\ !$96-103 #region nucleotide-binding motif A (P-loop)\ !$168-173 #region nucleotide-binding motif B\ !$102 #binding_site ATP (Lys) #status predicted SUMMARY #length 448 #molecular-weight 49556 #checksum 9359 SEQUENCE /// ENTRY G64547 #type complete TITLE DNA repair protein sms - Helicobacter pylori (strain 26695) ALTERNATE_NAMES DNA repair protein radA ORGANISM #formal_name Helicobacter pylori DATE 30-Apr-1999 #sequence_revision 30-Apr-1999 #text_change 19-Jan-2001 ACCESSIONS G64547 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession G64547 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-456 ##label TOM !'##cross-references GB:AE000542; GB:AE000511; NID:g2313310; !1PIDN:AAD07290.1; PID:g2313313; TIGR:HP0223 GENETICS !$#gene HP0223; sms !$#start_codon GTG FUNCTION !$#description may impart resistance to DNA alkylation CLASSIFICATION #superfamily DNA repair protein sms KEYWORDS ATP; DNA binding; DNA repair; nucleotide binding; P-loop; !1zinc finger FEATURE !$18-35 #region zinc finger CCCC motif\ !$104-111 #region nucleotide-binding motif A (P-loop)\ !$176-181 #region nucleotide-binding motif B\ !$110 #binding_site ATP (Lys) #status predicted SUMMARY #length 456 #molecular-weight 50304 #checksum 241 SEQUENCE /// ENTRY A71659 #type complete TITLE DNA repair protein sms - Rickettsia prowazekii ALTERNATE_NAMES DNA repair protein radA ORGANISM #formal_name Rickettsia prowazekii DATE 30-Apr-1999 #sequence_revision 30-Apr-1999 #text_change 19-Jan-2001 ACCESSIONS A71659 REFERENCE A71630 !$#authors Andersson, S.G.E.; Zomorodipour, A.; Andersson, J.O.; !1Sicheritz-Ponten, T.; Alsmark, U.C.M.; Podowski, R.M.; !1Naeslund, A.K.; Eriksson, A.S.; Winkler, H.H.; Kurland, C.G. !$#journal Nature (1998) 396:133-140 !$#title The genome sequence of Rickettsia prowazekii and the origin !1of mitochondria. !$#cross-references MUID:99039499; PMID:9823893 !$#accession A71659 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-448 ##label AND !'##cross-references GB:AJ235272; GB:AJ235269; NID:g3861033; !1PIDN:CAA14995.1; PID:g3861095; GSPDB:GN00081 !'##experimental_source strain Madrid E GENETICS !$#gene radA; RP546; sms FUNCTION !$#description may impart resistance to DNA alkylation CLASSIFICATION #superfamily DNA repair protein sms KEYWORDS ATP; DNA binding; DNA repair; nucleotide binding; P-loop; !1zinc finger FEATURE !$13-30 #region zinc finger CCCC motif\ !$93-100 #region nucleotide-binding motif A (P-loop)\ !$167-172 #region nucleotide-binding motif B\ !$99 #binding_site ATP (Lys) #status predicted SUMMARY #length 448 #molecular-weight 49075 #checksum 9123 SEQUENCE /// ENTRY B70804 #type complete TITLE DNA repair protein sms - Mycobacterium tuberculosis (strain H37RV) ALTERNATE_NAMES DNA repair protein radA ORGANISM #formal_name Mycobacterium tuberculosis DATE 30-Apr-1999 #sequence_revision 30-Apr-1999 #text_change 19-Jan-2001 ACCESSIONS B70804 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession B70804 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-480 ##label COL !'##cross-references GB:AL022075; GB:AL123456; NID:g3261555; !1PIDN:CAA17854.1; PID:g2950408 !'##experimental_source strain H37Rv GENETICS !$#gene radA; sms; Rv3585 FUNCTION !$#description may impart resistance to DNA alkylation CLASSIFICATION #superfamily DNA repair protein sms KEYWORDS ATP; DNA binding; DNA repair; nucleotide binding; P-loop; !1zinc finger FEATURE !$10-27 #region zinc finger CCCC motif\ !$95-102 #region nucleotide-binding motif A (P-loop)\ !$169-174 #region nucleotide-binding motif B\ !$101 #binding_site ATP (Lys) #status predicted SUMMARY #length 480 #molecular-weight 49913 #checksum 2255 SEQUENCE /// ENTRY A71251 #type complete TITLE DNA repair protein sms - syphilis spirochete ALTERNATE_NAMES DNA repair protein radA ORGANISM #formal_name Treponema pallidum subsp. pallidum #common_name syphilis spirochete DATE 30-Apr-1999 #sequence_revision 30-Apr-1999 #text_change 19-Jan-2001 ACCESSIONS A71251 REFERENCE A71250 !$#authors Fraser, C.M.; Norris, S.J.; Weinstock, G.M.; White, O.; !1Sutton, G.G.; Dodson, R.; Gwinn, M.; Hickey, E.K.; Clayton, !1R.; Ketchum, K.A.; Sodergren, E.; Hardham, J.M.; McLeod, !1M.P.; Salzberg, S.; Peterson, J.; Khalak, H.; Richardson, !1D.; Howell, J.K.; Chidambaram, M.; Utterback, T.; McDonald, !1L.; Artiach, P.; Bowman, C.; Cotton, M.D.; Fujii, C.; !1Garland, S.; Hatch, B.; Horst, K.; Roberts, K.; Watthey, L.; !1Weidman, J.; Smith, H.O.; Venter, J.C. !$#journal Science (1998) 281:375-388 !$#title Complete genome sequence of Treponema pallidum, the syphilis !1spirochete. !$#cross-references MUID:98332770; PMID:9665876 !$#accession A71251 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-455 ##label COL !'##cross-references GB:AE001270; GB:AE000520; NID:g3323350; !1PIDN:AAC65973.1; PID:g3323351 !'##experimental_source strain Nichols GENETICS !$#gene TP1022; sms FUNCTION !$#description may impart resistance to DNA alkylation CLASSIFICATION #superfamily DNA repair protein sms KEYWORDS ATP; DNA binding; DNA repair; nucleotide binding; P-loop; !1zinc finger FEATURE !$11-28 #region zinc finger CCCC motif\ !$97-104 #region nucleotide-binding motif A (P-loop)\ !$166-171 #region nucleotide-binding motif B\ !$103 #binding_site ATP (Lys) #status predicted SUMMARY #length 455 #molecular-weight 49304 #checksum 2672 SEQUENCE /// ENTRY S60157 #type complete TITLE RING finger protein MAT1 - human ALTERNATE_NAMES cdk7-cyclin H assembly factor MAT1 ORGANISM #formal_name Homo sapiens #common_name man DATE 23-Aug-1996 #sequence_revision 01-Nov-1996 #text_change 19-Jan-2001 ACCESSIONS S60157; S60156 REFERENCE S60156 !$#authors Tassan, J.P.; Jaquenoud, M.; Fry, A.M.; Frutiger, S.; !1Hughes, G.J.; Nigg, E.A. !$#journal EMBO J. (1995) 14:5608-5617 !$#title In vitro assembly of a functional human CDK7-cyclin H !1complex requires MAT1, a novel 36 kDa RING finger protein. !$#cross-references MUID:96091133; PMID:8521818 !$#accession S60157 !'##molecule_type mRNA !'##residues 1-309 ##label TAS !'##cross-references EMBL:X87843; NID:g1089847; PIDN:CAA61112.1; !1PID:g1089848 !$#accession S60156 !'##molecule_type protein !'##residues 23-48;123-147 ##label TAW GENETICS !$#gene GDB:MNAT1; MAT1 !'##cross-references GDB:7037523; OMIM:602659 !$#map_position 14q23-14q23 CLASSIFICATION #superfamily RING finger protein MAT1; RING finger homology KEYWORDS zinc finger FEATURE !$2-55 #domain RING finger homology #label RNG\ !$6-49 #region zinc finger C3HC4 motif SUMMARY #length 309 #molecular-weight 35823 #checksum 1500 SEQUENCE /// ENTRY A57235 #type complete TITLE RING finger protein MAT1 - mouse ALTERNATE_NAMES CDK-activating kinase (CAK) assembly chain p36; CDK7-cyclin H assembly factor MAT1 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 01-Mar-1996 #sequence_revision 01-Mar-1996 #text_change 19-Jan-2001 ACCESSIONS A57235 REFERENCE A57235 !$#authors Fisher, R.P.; Jin, P.; Chamberlin, H.M.; Morgan, D.O. !$#journal Cell (1995) 83:47-57 !$#title Alternative mechanisms of CAK assembly require an assembly !1factor or an activating kinase. !$#cross-references MUID:96006524; PMID:7553872 !$#accession A57235 !'##molecule_type mRNA !'##residues 1-309 ##label FIS !'##cross-references GB:U35249; NID:g1015998; PIDN:AAA91741.1; !1PID:g1015999 FUNCTION !$#description promotes the assembly of cyclin H and CDK7 with itself into !1a soluble 175K form of CDK-activating kinase (CAK); !1dimerization of cyclin H with CDK7 can occur without this !1assembly protein following phosphorylation of CDK7 on a !1conserved Thr residue CLASSIFICATION #superfamily RING finger protein MAT1; RING finger homology KEYWORDS heterotrimer; zinc finger FEATURE !$2-55 #domain RING finger homology #label RNG\ !$6-49 #region zinc finger C3HC4 motif SUMMARY #length 309 #molecular-weight 35820 #checksum 436 SEQUENCE /// ENTRY RGBY54 #type complete TITLE translation activator PET54 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein 293; protein G8527; protein YGR222w ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 23-Mar-2001 ACCESSIONS S05778; B46737; S57685; S64546; S63901 REFERENCE S05778 !$#authors Costanzo, M.C.; Seaver, E.C.; Fox, T.D. !$#journal Genetics (1989) 122:297-305 !$#title The PET54 gene of Saccharomyces cerevisiae: characterization !1of a nuclear gene encoding a mitochondrial translational !1activator and subcellular localization of its product. !$#cross-references MUID:89357444; PMID:2548921 !$#accession S05778 !'##molecule_type DNA !'##residues 1-293 ##label COS !'##cross-references EMBL:X13427; NID:g4132; PIDN:CAA31784.1; PID:g4133 REFERENCE A46737 !$#authors McMullin, T.W.; Fox, T.D. !$#journal J. Biol. Chem. (1993) 268:11737-11741 !$#title COX3 mRNA-specific translational activator proteins are !1associated with the inner mitochondrial membrane in !1Saccharomyces cerevisiae. !$#cross-references MUID:93280133; PMID:8389363 !$#accession B46737 !'##molecule_type protein !'##residues 1-16 ##label MCM REFERENCE S57680 !$#authors van der Aart, Q.J.M.; Kleine, K.; Steensma, H.Y. !$#submission submitted to the EMBL Data Library, June 1995 !$#description Sequence analysis of the 43 KB !1CRM1-YLM9-PET54-SMI1-PHO81-YHB4-PFK1 region from the right !1arm of Saccharomyces cerevisiae chromosome VII. !$#accession S57685 !'##molecule_type DNA !'##residues 1-293 ##label VAN !'##cross-references EMBL:X87941; NID:g886908; PIDN:CAA61170.1; !1PID:g886914 !'##experimental_source strain S288C REFERENCE S64541 !$#authors van der Aart, Q.J.M.; Steensma, H.Y. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64546 !'##molecule_type DNA !'##residues 1-293 ##label VAW !'##cross-references EMBL:Z73007; NID:g1323399; PIDN:CAA97250.1; !1PID:g1323400; GSPDB:GN00007; MIPS:YGR222w !'##experimental_source strain S288C REFERENCE S63896 !$#authors van der Aart, Q.J.M.; Kleine, K.; Steensma, H.Y. !$#journal Yeast (1996) 12:385-390 !$#title Sequence analysis of the 43 kb !1CRM1-YLM9-PET54-DIE2-SMI1-PHO81-YHB4-PFK1 region from the !1right arm of Saccharomyces cerevisiae chromosome VII. !$#cross-references MUID:96267763; PMID:8701610 !$#accession S63901 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-293 ##label VAF !'##cross-references EMBL:X87941; NID:g886908; PIDN:CAA61170.1; !1PID:g886914 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1995 GENETICS !$#gene SGD:PET54; MIPS:YGR222w !'##cross-references SGD:S0003454; MIPS:YGR222w !$#map_position 7R !$#genome nuclear !$#note YGR222w CLASSIFICATION #superfamily translation activator PET54 KEYWORDS mitochondrion FEATURE !$1-293 #product translation activator PET54 #status !8experimental #label MAT SUMMARY #length 293 #molecular-weight 34637 #checksum 712 SEQUENCE /// ENTRY RGBYP4 #type complete TITLE PET494 protein precursor - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein N3436; protein YNR045w ORGANISM #formal_name Saccharomyces cerevisiae DATE 28-Dec-1987 #sequence_revision 17-May-1996 #text_change 19-Apr-2002 ACCESSIONS S63376; A26024; B41258 REFERENCE S63346 !$#authors Pohl, T.M. !$#submission submitted to the Protein Sequence Database, April 1996 !$#accession S63376 !'##molecule_type DNA !'##residues 1-489 ##label POH REFERENCE A26024 !$#authors Costanzo, M.C.; Mueller, P.P.; Strick, C.A.; Fox, T.D. !$#journal Mol. Gen. Genet. (1986) 202:294-301 !$#title Primary structure of wild-type and mutant alleles of the !1PET494 gene of Saccharomyces cerevisiae. !$#cross-references MUID:86202913; PMID:3010052 !$#accession A26024 !'##molecule_type DNA !'##residues 1-67,'S',69-489 ##label COS !'##cross-references GB:K03520; GB:X03539; NID:g172131; PIDN:AAA34857.1; !1PID:g172132 REFERENCE A41258 !$#authors Roy, A.; Lu, C.F.; Marykwas, D.L.; Lipke, P.N.; Kurjan, J. !$#journal Mol. Cell. Biol. (1991) 11:4196-4206 !$#title The AGA1 product is involved in cell surface attachment of !1the Saccharomyces cerevisiae cell adhesion glycoprotein !1a-agglutinin. !$#cross-references MUID:91304412; PMID:2072914 !$#accession B41258 !'##status translation not shown !'##molecule_type DNA !'##residues 1-67,'S',69-121 ##label ROY COMMENT This protein is essential for the expression of the !1mitochondrial gene for cytochrome-c oxidase chain III. GENETICS !'##cross-references SGD:S0005328 CLASSIFICATION #superfamily PET494 protein KEYWORDS mitochondrion; transmembrane protein FEATURE !$1-66 #domain transit peptide (mitochondrion) #status !8predicted #label TNP\ !$67-489 #product PET494 protein #status predicted #label MAT\ !$74-90 #domain transmembrane #status predicted #label TMM SUMMARY #length 489 #molecular-weight 57487 #checksum 4201 SEQUENCE /// ENTRY BWBYDL #type complete TITLE RAD50 protein - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein N0872; protein YNL250w ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jun-2000 ACCESSIONS S05808; S63223 REFERENCE S05808 !$#authors Alani, E.; Subbiah, S.; Kleckner, N. !$#journal Genetics (1989) 122:47-57 !$#title The yeast RAD50 gene encodes a predicted 153-kD protein !1containing a purine nucleotide-binding domain and two large !1heptad-repeat regions. !$#cross-references MUID:89276917; PMID:2659437 !$#accession S05808 !'##molecule_type DNA !'##residues 1-1312 ##label ALA !'##cross-references EMBL:X14814; NID:g4272; PIDN:CAA32919.1; PID:g4273 REFERENCE S63220 !$#authors Sen-Gupta, M.; Gueldener, U.; Beinhauer, J.; Fiedler, T.; !1Hegemann, J.H. !$#submission submitted to the Protein Sequence Database, April 1996 !$#accession S63223 !'##molecule_type DNA !'##residues 1-1312 ##label SEN !'##cross-references EMBL:Z71526; NID:g1302292; PIDN:CAA96157.1; !1PID:g1302293; GSPDB:GN00014; MIPS:YNL250w !'##experimental_source strain S288C GENETICS !$#gene SGD:RAD50; MIPS:YNL250w !'##cross-references SGD:S0005194; MIPS:YNL250w !$#map_position 14L CLASSIFICATION #superfamily RAD50 protein KEYWORDS ATP; coiled coil; DNA repair; meiosis; nucleus FEATURE !$177-421 #region heptad repeats\ !$743-995 #region heptad repeats\ !$40 #binding_site ATP (Lys) #status predicted SUMMARY #length 1312 #molecular-weight 152568 #checksum 4677 SEQUENCE /// ENTRY DDBYD4 #type complete TITLE excision repair protein RAD4 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES DNA repair protein RAD4; protein YER162c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1991 #sequence_revision 12-May-1995 #text_change 23-Mar-2001 ACCESSIONS S30814; A32832; JS0081; S50665; S05739 REFERENCE S30812 !$#authors Mulligan, J.T.; Dietrich, F.S.; Hennessey, K.M.; Sehl, P.; !1Komp, C.; Wei, Y.; Taylor, P.; Nakahara, K.; Roberts, D.; !1Davis, R.W. !$#submission submitted to the EMBL Data Library, February 1993 !$#accession S30814 !'##molecule_type DNA !'##residues 1-754 ##label MUL !'##cross-references GB:U18917; EMBL:L10718; NID:g603377; !1PIDN:AAB64689.1; PID:g603402 REFERENCE A32832 !$#authors Couto, L.B.; Friedberg, E.C. !$#journal J. Bacteriol. (1989) 171:1862-1869 !$#title Nucleotide sequence of the wild-type RAD4 gene of !1Saccharomyces cerevisiae and characterization of mutant rad4 !1alleles. !$#cross-references MUID:89197751; PMID:2649477 !$#accession A32832 !'##molecule_type DNA !'##residues 1-222,'V',224,'I',226-754 ##label COU !'##cross-references EMBL:M24928; NID:g172334; PIDN:AAA34945.1; !1PID:g172335 REFERENCE JS0081 !$#authors Gietz, R.D.; Prakash, S. !$#journal Gene (1988) 74:535-541 !$#title Cloning and nucleotide sequence analysis of the !1Saccharomyces cerevisiae RAD4 gene required for excision !1repair of UV-damaged DNA. !$#cross-references MUID:89232744; PMID:3073107 !$#accession JS0081 !'##molecule_type DNA !'##residues 1-222,'V',224,'I',226-754 ##label GIE !'##cross-references GB:M26050; NID:g172332; PIDN:AAA34944.1; !1PID:g172333 REFERENCE S50430 !$#authors Dietrich, F.S. !$#submission submitted to the EMBL Data Library, December 1994 !$#description The sequence of S. cerevisiae cosmids 8229, 9115, 9132, !19981, and lambda clones 7990 and 6134. !$#accession S50665 !'##molecule_type DNA !'##residues 1-754 ##label DIE !'##cross-references EMBL:U18917; NID:g603377; PIDN:AAB64689.1; !1PID:g603402; GSPDB:GN00005; MIPS:YER162c GENETICS !$#gene SGD:RAD4; MIPS:YER162c !'##cross-references SGD:S0000964; MIPS:YER162c !$#map_position 5R FUNCTION !$#description required for the incision step of excision repair of DNA !1damaged by UV and by other agents that distort the DNA helix CLASSIFICATION #superfamily DNA repair protein RAD4 KEYWORDS DNA binding; DNA repair FEATURE !$29-36 #region basic\ !$44-48 #region basic\ !$137-141 #region basic\ !$240-244 #region basic\ !$386-391 #region basic\ !$410-416 #region basic\ !$711-754 #region acidic SUMMARY #length 754 #molecular-weight 87203 #checksum 7350 SEQUENCE /// ENTRY DDBYD1 #type complete TITLE RAD1 protein - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein LPB9w; protein YPL022w ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 21-Jul-2000 ACCESSIONS A26129; S05878; S63460 REFERENCE A26129 !$#authors Reynolds, P.; Prakash, L.; Prakash, S. !$#journal Mol. Cell. Biol. (1987) 7:1012-1020 !$#title Nucleotide sequence and functional analysis of the RAD1 gene !1of Saccharomyces cerevisiae. !$#cross-references MUID:87172766; PMID:3550428 !$#accession A26129 !'##molecule_type DNA !'##residues 1-1100 ##label REY !'##cross-references EMBL:M15435; NID:g172324; PIDN:AAA34934.1; !1PID:g172325 REFERENCE S05878 !$#authors Yang, E.; Friedberg, E.C. !$#journal Mol. Cell. Biol. (1984) 4:2161-2169 !$#title Molecular cloning and nucleotide sequence analysis of the !1Saccharomyces cerevisiae RAD1 gene. !$#cross-references MUID:85061207; PMID:6095044 !$#accession S05878 !'##molecule_type DNA !'##residues 1-222,'N',224-882,'Y',884-885,'I',887-911,'K',913-922, !1'NYSSYIKQVIPG',935-947,'SHFKDYMVFLTPANCKYNPRVEIRT' ##label !1YAN !'##cross-references EMBL:K02070; NID:g172317; PIDN:AAA34929.1; !1PID:g172318 REFERENCE S63452 !$#authors Wang, Y.; Ahmed, A.; Bussey, H.; Fortin, N.; Friesen, J.D.; !1Hall, J.; Storms, R.K.; Vo, D.H.; Winnett, E. !$#submission submitted to the EMBL Data Library, September 1995 !$#accession S63460 !'##molecule_type DNA !'##residues 1-1100 ##label WAN !'##cross-references EMBL:U36624; NID:g1276642; PIDN:AAB68165.1; !1PID:g1039455; GSPDB:GN00016; MIPS:YPL022w GENETICS !$#gene SGD:RAD1; MIPS:YPL022w !'##cross-references SGD:S0005943; MIPS:YPL022w !$#map_position 16L CLASSIFICATION #superfamily RAD1 protein KEYWORDS DNA binding; DNA repair SUMMARY #length 1100 #molecular-weight 126369 #checksum 1360 SEQUENCE /// ENTRY BVBYK1 #type complete TITLE MAK31 protein - yeast (Saccharomyces cerevisiae) ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 19-Apr-2002 ACCESSIONS S07694 REFERENCE S07692 !$#authors Toh-e, A.; Sahashi, Y. !$#journal Yeast (1985) 1:159-171 !$#title The PET18 locus of Saccharomyces cerevisiae: a complex locus !1containing multiple genes. !$#cross-references MUID:89131254; PMID:3916862 !$#accession S07694 !'##molecule_type DNA !'##residues 1-88 ##label TOH !'##experimental_source strain MT13 GENETICS !$#gene SGD:MAK31; MAK31 !'##cross-references SGD:S0000614 !$#map_position 3R CLASSIFICATION #superfamily MAK31 protein SUMMARY #length 88 #molecular-weight 9724 #checksum 5414 SEQUENCE /// ENTRY BVBYK2 #type complete TITLE MAK32 protein - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YCR019w ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1991 #sequence_revision 30-Sep-1993 #text_change 16-Jun-2000 ACCESSIONS S19429; S07695 REFERENCE S19429 !$#authors Feldmann, H.; Mannhaupt, G.; Vetter, I. !$#submission submitted to the Protein Sequence Database, March 1992 !$#accession S19429 !'##molecule_type DNA !'##residues 1-363 ##label FEL !'##cross-references EMBL:X59720; NID:g1907116; PIDN:CAA42310.1; !1PID:g1907162; GSPDB:GN00003; MIPS:YCR019w REFERENCE S07692 !$#authors Toh-e, A.; Sahashi, Y. !$#journal Yeast (1985) 1:159-171 !$#title The PET18 locus of Saccharomyces cerevisiae: a complex locus !1containing multiple genes. !$#cross-references MUID:89131254; PMID:3916862 !$#accession S07695 !'##molecule_type DNA !'##residues 1-14,'I',15-81,83-282,'S',284-363 ##label TOH GENETICS !$#gene SGD:MAK32; MIPS:YCR019w !'##cross-references SGD:S0000612; MIPS:YCR019w !$#map_position 3R CLASSIFICATION #superfamily MAK32 protein SUMMARY #length 363 #molecular-weight 40783 #checksum 428 SEQUENCE /// ENTRY RGBYM3 #type complete TITLE regulatory protein MAL63 - yeast (Saccharomyces cerevisiae) (strain carlsbergensis) ALTERNATE_NAMES regulatory protein MAL6R ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jul-1999 ACCESSIONS S03814; S05840; S15526 REFERENCE S03814 !$#authors Sollitti, P.; Marmur, J. !$#journal Mol. Gen. Genet. (1988) 213:56-62 !$#title Primary structure of the regulatory gene from the MAL6 locus !1of Saccharomyces carlsbergensis. !$#cross-references MUID:89127146; PMID:2851710 !$#accession S03814 !'##molecule_type DNA !'##residues 1-473 ##label SOL !'##cross-references EMBL:X12576; NID:g3884; PIDN:CAA31088.1; PID:g3885 !'##note the source is designated as Saccharomyces carlsbergensis REFERENCE S05840 !$#authors Kim, J.; Michels, C.A. !$#journal Curr. Genet. (1988) 14:319-323 !$#title The MAL63 gene of Saccharomyces encodes a cysteine-zinc !1finger protein. !$#cross-references MUID:89106267; PMID:3145816 !$#accession S05840 !'##molecule_type DNA !'##residues 1-86,89-204,206-473 ##label KIM !'##cross-references EMBL:M36537; NID:g171884; PIDN:AAA34755.1; !1PID:g171885 !'##note the source is designated as Saccharomyces carlsbergensis REFERENCE S15526 !$#authors Kopetzki, E.; Zellner, E.; Schumacher, G.; Zimmermann, F.K. !$#journal Nucleic Acids Res. (1989) 17:5390 !$#title Nucleotide sequence of the Saccharomyces cerevisiae positive !1regulatory mutant gene MAL2-8(c)p. !$#cross-references MUID:89345105; PMID:2668884 !$#accession S15526 !'##molecule_type DNA !'##residues 1,'TL',4-6,'A',8-86,89-204,206-306,'W',308-473 ##label KOP !'##cross-references EMBL:M15241 !'##note this sequence is from mutant MAL2-8(c)p GENETICS !$#gene MAL63; MAL6R !$#map_position 8 CLASSIFICATION #superfamily regulatory protein MAL63; GAL4 zinc binuclear !1cluster homology KEYWORDS DNA binding; nucleus; transcription regulation; zinc finger FEATURE !$3-39 #domain GAL4 zinc binuclear cluster homology #label !8GAL4\ !$8-34 #region zinc finger SUMMARY #length 473 #molecular-weight 54895 #checksum 9950 SEQUENCE /// ENTRY BVBYMS #type complete TITLE MSI1 protein - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YBR1406; protein YBR195c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 05-Nov-1999 ACCESSIONS S07865; S34020; S46067 REFERENCE S07865 !$#authors Ruggieri, R.; Tanaka, K.; Nakafuku, M.; Kaziro, Y.; Toh-e, !1A.; Matsumoto, K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:8778-8782 !$#title MSI1, a negative regulator of the RAS-cAMP pathway in !1Saccharomyces cerevisiae. !$#cross-references MUID:90046875; PMID:2554329 !$#accession S07865 !'##molecule_type DNA !'##residues 1-422 ##label RUG !'##cross-references GB:M27300; NID:g172005; PIDN:AAA34804.1; !1PID:g172006 REFERENCE S33966 !$#authors Demolis, N.; Mallet, L.; Bussereau, F.; Jacquet, M. !$#journal Yeast (1993) 9:645-659 !$#title RIM2, MSI1 and PGI1 are located within an 8 kb segment of !1Saccharomyces cerevisiae chromosome II, which also contains !1the putative ribosomal gene L21 and a new putative essential !1gene with a leucine zipper motif. !$#cross-references MUID:93348777; PMID:8346681 !$#accession S34020 !'##status translation not shown !'##molecule_type DNA !'##residues 1-422 ##label DEM !'##cross-references EMBL:Z21487; NID:g311665; PIDN:CAA79682.1; !1PID:g311671 REFERENCE S46054 !$#authors Bussereau, F.; Demolis, N.; Jacquet, M.; Mallet, L. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S46067 !'##molecule_type DNA !'##residues 1-422 ##label BUS !'##cross-references EMBL:Z36064; NID:g536562; PIDN:CAA85157.1; !1PID:g536563; GSPDB:GN00002; MIPS:YBR195c GENETICS !$#gene SGD:MSI1; MIPS:YBR195c !'##cross-references SGD:S0000399; MIPS:YBR195c !$#map_position 2R CLASSIFICATION #superfamily MSI1 protein; WD repeat homology KEYWORDS duplication FEATURE !$196-230 #domain WD repeat homology #label WD1\ !$292-326 #domain WD repeat homology #label WD2\ !$335-371 #domain WD repeat homology #label WD3\ !$380-413 #domain WD repeat homology #label WD4 SUMMARY #length 422 #molecular-weight 47364 #checksum 6100 SEQUENCE /// ENTRY RGBY7K #type complete TITLE mitochondrial import protein, 27K - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein O5463w; protein YOR278w ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1991 #sequence_revision 02-Aug-1996 #text_change 16-Jun-2000 ACCESSIONS S67180; S05883; S72048 REFERENCE S67169 !$#authors Cheret, G.; Sor, F. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67180 !'##molecule_type DNA !'##residues 1-275 ##label CHE !'##cross-references EMBL:Z75186; NID:g1420620; PIDN:CAA99504.1; !1PID:g1420621; GSPDB:GN00015; MIPS:YOR278w !'##experimental_source strain S288C REFERENCE S05883 !$#authors Langgut, W.; Entrup, R.; Schweizer, E. !$#journal Curr. Genet. (1986) 11:177-184 !$#title Isolation of a nuclear yeast gene involved in the !1mitochondrial import of cytoplasmically synthesized !1precursor proteins. !$#cross-references MUID:88194672; PMID:2834088 !$#accession S05883 !'##molecule_type DNA !'##residues 1-230,'IY',238,'LRHRT',244,'H' ##label LAN !'##cross-references EMBL:X04694; NID:g4084; PIDN:CAA28399.1; PID:g4085 REFERENCE S72039 !$#authors Cheret, G.; Bernardi, A.; Sor, F. !$#journal Yeast (1996) 12:1059-1064 !$#title DNA sequence analysis of the VPH1-SNF2 region on chromosome !1XV of Saccharomyces cerevisiae. !$#cross-references MUID:97051594; PMID:8896271 !$#accession S72048 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-275 ##label CHW !'##cross-references EMBL:X89633; NID:g1279694; PIDN:CAA61783.1; !1PID:g1279703 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1995 GENETICS !$#gene SGD:HEM4; MIPS:YOR278w !'##cross-references MIPS:YOR278w; SGD:S0005804 !$#map_position 15R !$#genome nuclear CLASSIFICATION #superfamily mitochondrial import protein, 27K KEYWORDS mitochondrion SUMMARY #length 275 #molecular-weight 30911 #checksum 2068 SEQUENCE /// ENTRY RGBYM1 #type complete TITLE pheromone response pathway component SRM1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES cell cycle regulatory protein SRM1; protein G3139; protein YGL097w; PRP20 protein ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 21-Jul-2000 ACCESSIONS A32320; S12286; S64104; S05740 REFERENCE A32320 !$#authors Clark, K.L.; Sprague Jr., G.F. !$#journal Mol. Cell. Biol. (1989) 9:2682-2694 !$#title Yeast pheromone response pathway: characterization of a !1suppressor that restores mating to receptorless mutants. !$#cross-references MUID:89343986; PMID:2548085 !$#accession A32320 !'##molecule_type DNA !'##residues 1-482 ##label CLA !'##cross-references EMBL:M27013; NID:g341590; PIDN:AAA62268.1; !1PID:g666950 REFERENCE S12286 !$#authors Aebi, M.; Clark, M.W.; Vijayraghavan, U.; Abelson, J. !$#journal Mol. Gen. Genet. (1990) 224:72-80 !$#title A yeast mutant, PRP20, altered in mRNA metabolism and !1maintenance of the nuclear structure, is defective in a gene !1homologous to the human gene RCC1 which is involved in the !1control of chromosome condensation. !$#cross-references MUID:91117179; PMID:2277633 !$#accession S12286 !'##molecule_type DNA !'##residues 1-482 ##label AEB REFERENCE S64071 !$#authors Rieger, M.; Mueller-Auer, S.; Brueckner, M.; Schaefer, M. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64104 !'##molecule_type DNA !'##residues 1-482 ##label RIE !'##cross-references EMBL:Z72619; NID:g1322632; PIDN:CAA96803.1; !1PID:g1322633; GSPDB:GN00007; MIPS:YGL097w !'##experimental_source strain S288C GENETICS !$#gene SGD:SRM1; PRP20; MTR1; MIPS:YGL097w !'##cross-references SGD:S0003065; MIPS:YGL097w !$#map_position 7L CLASSIFICATION #superfamily pheromone response pathway component SRM1 KEYWORDS DNA binding; duplication; nucleus FEATURE !$46-102,103-183, !$184-239,240-292, !$293-348,349-412, !$413-467 #region duplication SUMMARY #length 482 #molecular-weight 53013 #checksum 1247 SEQUENCE /// ENTRY BVBYK6 #type complete TITLE MAK16 protein - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YAL025c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 21-Jul-2000 ACCESSIONS A35588; S51996; S05851 REFERENCE A35588 !$#authors Wickner, R.B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:6007-6011 !$#title Host function of MAK16: G(1) arrest by a mak16 mutant of !1Saccharomyces cerevisiae. !$#cross-references MUID:88320371; PMID:3045810 !$#accession A35588 !'##molecule_type DNA !'##residues 1-306 ##label WIC !'##cross-references EMBL:J03852; NID:g171878; PIDN:AAA34752.1; !1PID:g171880 REFERENCE S51956 !$#authors Bussey, H.; Kaback, D.B.; Zhong, W.; Vo, D.T.; Clark, M.W.; !1Fortin, N.; Hall, J.; Ouellette, B.F.F.; Keng, T.; Barton, !1A.B.; Su, Y.; Davies, C.K.; Storms, R.K. !$#submission submitted to the EMBL Data Library, August 1994 !$#description The sequence of chromosome 1 of Saccharomyces cerevisiae. !$#accession S51996 !'##molecule_type DNA !'##residues 1-306 ##label BUS !'##cross-references EMBL:U12980; NID:g1326053; PIDN:AAC05007.1; !1PID:g595561; GSPDB:GN00001; MIPS:YAL025c GENETICS !$#gene SGD:MAK16; MIPS:YAL025c !'##cross-references SGD:S0000023; MIPS:YAL025c !$#map_position 1L CLASSIFICATION #superfamily MAK16 protein KEYWORDS cell cycle control; phosphoprotein FEATURE !$139-144 #region nuclear location signal\ !$282-287 #region nuclear location signal SUMMARY #length 306 #molecular-weight 35694 #checksum 1464 SEQUENCE /// ENTRY A35622 #type complete TITLE nuclear pore protein NUP1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES nucleoporin; protein O3182; protein YOR098c; protein YOR3182c ORGANISM #formal_name Saccharomyces cerevisiae DATE 22-Jan-1993 #sequence_revision 08-Mar-1996 #text_change 21-Jul-2000 ACCESSIONS A35622; S61658; S66983 REFERENCE A35622 !$#authors Davis, L.I.; Fink, G.R. !$#journal Cell (1990) 61:965-978 !$#title The NUP1 gene encodes an essential component of the yeast !1nuclear pore complex. !$#cross-references MUID:90275616; PMID:2190694 !$#accession A35622 !'##molecule_type DNA !'##residues 1-1076 ##label DAV !'##cross-references EMBL:M33632; NID:g172055; PIDN:AAA34822.1; !1PID:g172056 !'##experimental_source strain S288C REFERENCE S61643 !$#authors Benes, V.; Andrade, M.A.; Rechmann, S.; Teodoru, C.; !1Banrevi, A.; Sander, C.; Valencia, A.; Ansorge, W.; Voss, H. !$#submission submitted to the EMBL Data Library, December 1995 !$#description Nucleotide sequence and analysis of a 130 kb fragment of !1yeast chromosome XV. !$#accession S61658 !'##molecule_type DNA !'##residues 1-1076 ##label BEN !'##cross-references EMBL:X94335; NID:g1262139; PIDN:CAA64020.1; !1PID:g1164945 REFERENCE S66965 !$#authors Voss, H.; Benes, V.; Rechmann, S.; Teodoru, C.; Schwager, !1C.; Paces, V.; Ansorge, W. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S66983 !'##molecule_type DNA !'##residues 1-1076 ##label VOS !'##cross-references EMBL:Z75006; NID:g1420274; PIDN:CAA99295.1; !1PID:g1420275; GSPDB:GN00015; MIPS:YOR098c !'##experimental_source strain S288C GENETICS !$#gene SGD:NUP1; MIPS:YOR098c !'##cross-references SGD:S0005624; MIPS:YOR098c !$#map_position 15R CLASSIFICATION #superfamily nuclear pore protein NUP1 SUMMARY #length 1076 #molecular-weight 113581 #checksum 9223 SEQUENCE /// ENTRY ERBYA #type complete TITLE coatomer complex alpha chain RET1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES gamma-alpha-COP protein; protein D1578; protein YDL145c ORGANISM #formal_name Saccharomyces cerevisiae DATE 12-Jul-1996 #sequence_revision 08-Nov-1996 #text_change 19-Apr-2002 ACCESSIONS S67692; S67693; S51282; A55288; B55288 REFERENCE S67688 !$#authors Baron, L.; Legros, Y.; Biteau, N.; Monnet, A.; Granotier, C. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67692 !'##molecule_type DNA !'##residues 1-1074 ##label BAR !'##cross-references EMBL:Z74193; GSPDB:GN00004; MIPS:YDL145c !'##experimental_source strain S288C REFERENCE S67693 !$#authors Perea, J.; Blugeon, C.; Delaveau, T.; Jacq, C. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67693 !'##molecule_type DNA !'##residues 799-1201 ##label PER !'##cross-references EMBL:Z74193; GSPDB:GN00004; MIPS:YDL145c !'##experimental_source strain S288C REFERENCE S51282 !$#authors Gerich, B.; Orci, L.; Tschochner, H.; Lottspeich, F.; !1Ravazolla, M.; Ammerdt, M.; Wieland, F.; Harter, C. !$#submission submitted to the EMBL Data Library, January 1995 !$#description Alpha-cop is a conserved subunit of coatomer and is !1essential for growth in S. cerevisiae. !$#accession S51282 !'##molecule_type DNA !'##residues 1-752,'L',754-904,'T',906-1005,'L',1007-1026,'NT',1029-1201 !1##label GER !'##cross-references EMBL:X83754; NID:g633647; PIDN:CAA58712.1; !1PID:g633648 REFERENCE A55288 !$#authors Letourneur, F.; Gaynor, E.C.; Hennecke, S.; Demolliere, C.; !1Duden, R.; Emr, S.D.; Riezman, H.; Cosson, P. !$#journal Cell (1994) 79:1199-1207 !$#title Coatomer is essential for retrieval of dilysine-tagged !1proteins to the endoplasmic reticulum. !$#cross-references MUID:95094295; PMID:8001155 !$#accession A55288 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type DNA !'##residues 1-361,'A',363-752,'L',754-904,'T',906-1005,'L',1007-1026, !1'NT',1029-1201 ##label HAR !'##cross-references GB:Z46617 !$#accession B55288 !'##molecule_type protein !'##residues 1-20 ##label HA2 GENETICS !$#gene SGD:COP1; RET1; MIPS:YDL145c !'##cross-references SGD:S0002304 !$#map_position 4L CLASSIFICATION #superfamily yeast coatomer complex alpha chain; WD repeat !1homology KEYWORDS duplication; transmembrane protein FEATURE !$6-40 #domain WD repeat homology #label WD1\ !$49-82 #domain WD repeat homology #label WD2\ !$91-124 #domain WD repeat homology #label WD3\ !$133-166 #domain WD repeat homology #label WD4\ !$205-238 #domain WD repeat homology #label WD5\ !$249-282 #domain WD repeat homology #label WD6\ !$912-928 #domain transmembrane #status predicted #label TMM SUMMARY #length 1201 #molecular-weight 135606 #checksum 5903 SEQUENCE /// ENTRY ERHUAH #type complete TITLE coatomer complex alpha chain homolog - human ALTERNATE_NAMES HEP-COP; xenopsin homolog; xenopsin-related peptide precursor CONTAINS xenin 25; xenopsin-related peptide ORGANISM #formal_name Homo sapiens #common_name man DATE 10-May-1996 #sequence_revision 08-Nov-1996 #text_change 21-Jul-2000 ACCESSIONS JC4668; A44317 REFERENCE JC4668 !$#authors Chow, V.T.K.; Quek, H.H. !$#journal Gene (1996) 169:223-227 !$#title HEP-COP, a novel human gene whose product is highly !1homologous to the alpha-subunit of the yeast coatomer !1protein complex. !$#cross-references MUID:96194806; PMID:8647451 !$#accession JC4668 !'##molecule_type mRNA !'##residues 1-1224 ##label CHO !'##cross-references GB:U24105; NID:g1638873; PIDN:AAB70879.1; !1PID:g1002369 !'##experimental_source Hep3B hepatocellular carcinoma cell REFERENCE A44317 !$#authors Feurle, G.E.; Hamscher, G.; Kusiek, R.; Meyer, H.E.; !1Metzger, J.W. !$#journal J. Biol. Chem. (1992) 267:22305-22309 !$#title Identification of xenin, a xenopsin-related peptide, in the !1human gastric mucosa and its effect on exocrine pancreatic !1secretion. !$#cross-references MUID:93054515; PMID:1429581 !$#accession A44317 !'##molecule_type protein !'##residues 1-25 ##label FEU !'##experimental_source gastric mucosa !'##note sequence extracted from NCBI backbone (NCBIP:117018) !'##note plasma levels of xenin 25, as determined by immunoassay, rise !1after meals and it appears to stimulate exocrine pancreatic !1secretion GENETICS !$#gene GDB:COPA; HEP-COP !'##cross-references GDB:4642787; OMIM:601924 !$#map_position 1q23-1q25 CLASSIFICATION #superfamily yeast coatomer complex alpha chain; WD repeat !1homology KEYWORDS duplication; hormone; plasma; stomach FEATURE !$1-25 #product xenin 25 #status experimental #label XNP\ !$5-38 #domain WD repeat homology #label WD1\ !$17-25 #product xenopsin-related peptide #status predicted !8#label XRP\ !$47-80 #domain WD repeat homology #label WD2\ !$89-122 #domain WD repeat homology #label WD3\ !$131-164 #domain WD repeat homology #label WD4\ !$201-234 #domain WD repeat homology #label WD5\ !$245-278 #domain WD repeat homology #label WD6 SUMMARY #length 1224 #molecular-weight 138331 #checksum 7132 SEQUENCE /// ENTRY BWBYD5 #type complete TITLE BUD5 protein - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YCR038c; protein YCR526; protein YCR721 ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jun-2000 ACCESSIONS S19450; S19752; S26405; A39933; A39934; S12920 REFERENCE S19446 !$#authors Dujon, B.; Fairhead, C.; Thierry, A. !$#submission submitted to the Protein Sequence Database, March 1992 !$#accession S19450 !'##molecule_type DNA !'##residues 1-538 ##label DUJ !'##cross-references EMBL:X59720; NID:g1907116; PIDN:CAA42305.1; !1PID:g1907180; GSPDB:GN00003; MIPS:YCR038c REFERENCE S19396 !$#authors Bolotin-Fukuhara, M.; Buhler, J.M.; Daignan-Fornier, B.; !1Doira, C.; Francingues-Gaillard, M.C.; Iborra, F.; Jacquet, !1M.; Pallier, C.; Raynal, A.; Soustelle, C. !$#submission submitted to the Protein Sequence Database, March 1992 !$#accession S19752 !'##molecule_type DNA !'##residues 1-538 ##label BOL !'##cross-references EMBL:X59720; NID:g1907116; PIDN:CAA42305.1; !1PID:g1907180; GSPDB:GN00003; MIPS:YCR038c REFERENCE S26405 !$#authors Jacquet, M.; Buhler, J.M.; Iborra, F.; Francingues-Gaillard, !1M.C.; Soustelle, C. !$#journal Yeast (1991) 7:881-888 !$#title The MAT locus revisited within a 9.8 kb fragment of !1chromosome III containing BUD5 and two new open reading !1frames. !$#cross-references MUID:92160397; PMID:1789011 !$#accession S26405 !'##molecule_type DNA !'##residues 1-296,'L',298-376,'S',378-538 ##label JAC !'##cross-references EMBL:X63853; NID:g3901; PIDN:CAA45334.1; PID:g3903 REFERENCE A39933 !$#authors Chant, J.; Corrado, K.; Pringle, J.R.; Herskowitz, I. !$#journal Cell (1991) 65:1213-1224 !$#title Yeast BUD5, encoding a putative GDP-GTP exchange factor, is !1necessary for bud site selection and interacts with bud !1formation gene BEM1. !$#cross-references MUID:91292524; PMID:1905981 !$#accession A39933 !'##molecule_type DNA !'##residues 1-5,'R',7-120,'D',122-296,'L',298-376,'S',378-538 ##label !1CHA !'##cross-references GB:M63552; NID:g171138; PIDN:AAA34460.1; !1PID:g171139 REFERENCE A39934 !$#authors Powers, S.; Gonzales, E.; Christensen, T.; Cubert, J.; !1Broek, D. !$#journal Cell (1991) 65:1225-1231 !$#title Functional cloning of BUD5, a CDC25-related gene from !1Saccharomyces cerevisiae that can suppress a !1dominant-negative RAS2 mutant. !$#cross-references MUID:91292525; PMID:1905982 !$#accession A39934 !'##molecule_type DNA !'##residues 1-5,'R',8-538 ##label POW !'##cross-references GB:M68938; NID:g171140; PIDN:AAA34462.1; !1PID:g171141 REFERENCE S12916 !$#authors Thierry, A.; Fairhead, C.; Dujon, B. !$#journal Yeast (1990) 6:521-534 !$#title The complete sequence of the 8.2 kb segment left of MAT on !1chromosome III reveals five ORFs, including a gene for a !1yeast ribokinase. !$#cross-references MUID:91181345; PMID:1964349 !$#accession S12920 !'##status translation not shown !'##molecule_type DNA !'##residues 183-538 ##label THI !'##cross-references EMBL:X56909; NID:g4489; PIDN:CAA40230.1; PID:g4494 GENETICS !$#gene SGD:BUD5; MIPS:YCR038c !'##cross-references SGD:S0000634; MIPS:YCR038c !$#map_position 3R CLASSIFICATION #superfamily BUD5 protein; CDC25-type guanine nucleotide !1exchange activator homology FEATURE !$304-536 #domain CDC25-type guanine nucleotide exchange !8activator homology #label SOS SUMMARY #length 538 #molecular-weight 62857 #checksum 7515 SEQUENCE /// ENTRY S22872 #type complete TITLE glyoxalase I activity-enhancing protein GAC - yeast (Saccharomyces cerevisiae) 2-mu plasmid ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 22-Oct-1999 ACCESSIONS S22872 REFERENCE S22872 !$#authors Inoue, Y.; Feng, L.; Bong-Young, C.; Ginya, H.; Murata, K.; !1Kimura, A. !$#journal Biotechnol. Appl. Biochem. (1990) 12:341-345 !$#title Nucleotide sequence of a gene which enhances the activity of !1glyoxalase I in Saccharomyces cerevisiae. !$#cross-references MUID:90297911; PMID:2193656 !$#accession S22872 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-106 ##label INO GENETICS !$#gene GAC !$#genome 2-mu plasmid CLASSIFICATION #superfamily glyoxalase I activity-enhancing protein GAC KEYWORDS zinc finger FEATURE !$76-102 #region zinc finger SUMMARY #length 106 #molecular-weight 12747 #checksum 697 SEQUENCE /// ENTRY A23438 #type complete TITLE probable DNA-binding protein SPT2 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YER161c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 23-Mar-2001 ACCESSIONS A23438; S30813; S50664; S20120; S05873 REFERENCE A23438 !$#authors Roeder, G.S.; Beard, C.; Smith, M.; Keranen, S. !$#journal Mol. Cell. Biol. (1985) 5:1543-1553 !$#title Isolation and characterization of the SPT2 gene, a negative !1regulator of Ty-controlled yeast gene expression. !$#cross-references MUID:85267670; PMID:2991744 !$#accession A23438 !'##molecule_type DNA !'##residues 1-333 ##label ROE !'##cross-references EMBL:M11165; NID:g172677; PIDN:AAA35083.1; !1PID:g172678 REFERENCE S30812 !$#authors Mulligan, J.T.; Dietrich, F.S.; Hennessey, K.M.; Sehl, P.; !1Komp, C.; Wei, Y.; Taylor, P.; Nakahara, K.; Roberts, D.; !1Davis, R.W. !$#submission submitted to the EMBL Data Library, February 1993 !$#accession S30813 !'##molecule_type DNA !'##residues 1-333 ##label MUL !'##cross-references GB:U18917; EMBL:L10718; NID:g603377; !1PIDN:AAB64688.1; PID:g603401 REFERENCE S50430 !$#authors Dietrich, F.S. !$#submission submitted to the EMBL Data Library, December 1994 !$#description The sequence of S. cerevisiae cosmids 8229, 9115, 9132, !19981, and lambda clones 7990 and 6134. !$#accession S50664 !'##molecule_type DNA !'##residues 1-333 ##label DIE !'##cross-references EMBL:U18917; NID:g603377; PIDN:AAB64688.1; !1PID:g603401; GSPDB:GN00005; MIPS:YER161c REFERENCE S20120 !$#authors Kruger, W.; Herskowitz, I. !$#journal Mol. Cell. Biol. (1991) 11:4135-4146 !$#title A negative regulator of HO transcription, SIN1 (SPT2), is a !1nonspecific DNA-binding protein related to HMG1. !$#cross-references MUID:91304406; PMID:2072912 !$#accession S20120 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type DNA !'##residues 116-197,'E',199-301 ##label KRU GENETICS !$#gene SGD:SPT2; SPM2; SIN1; MIPS:YER161c !'##cross-references SGD:S0000963; MIPS:YER161c !$#map_position 5R CLASSIFICATION #superfamily probable DNA-binding protein SPT2 KEYWORDS DNA binding; transcription regulation SUMMARY #length 333 #molecular-weight 38551 #checksum 8646 SEQUENCE /// ENTRY BWBYM1 #type complete TITLE TATA box-binding protein-associated factor chain TAFII150 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YCR042c; protein YCR724; TSM1 protein ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jun-2000 ACCESSIONS S19455; S19044; S26406; S19756; S62396 REFERENCE S19396 !$#authors Bolotin-Fukuhara, M.; Buhler, J.M.; Daignan-Fornier, B.; !1Doira, C.; Francingues-Gaillard, M.C.; Iborra, F.; Jacquet, !1M.; Pallier, C.; Raynal, A.; Soustelle, C. !$#submission submitted to the Protein Sequence Database, March 1992 !$#accession S19455 !'##molecule_type DNA !'##residues 1-1407 ##label BOL !'##cross-references EMBL:X59720; NID:g1907116; PIDN:CAA42290.1; !1PID:g1907184; GSPDB:GN00003; MIPS:YCR042c REFERENCE S19044 !$#authors Ray, B.L.; White, C.I.; Haber, J.E. !$#journal Curr. Genet. (1991) 20:25-31 !$#title The TSM1 gene of Saccharomyces cerevisiae overlaps the MAT !1locus. !$#cross-references MUID:92035068; PMID:1840512 !$#accession S19044 !'##molecule_type DNA !'##residues 1-322,'G',324-1407 ##label RAY !'##cross-references EMBL:M60486; NID:g173055; PIDN:AAA35179.1; !1PID:g173056 REFERENCE S26405 !$#authors Jacquet, M.; Buhler, J.M.; Iborra, F.; Francingues-Gaillard, !1M.C.; Soustelle, C. !$#journal Yeast (1991) 7:881-888 !$#title The MAT locus revisited within a 9.8 kb fragment of !1chromosome III containing BUD5 and two new open reading !1frames. !$#cross-references MUID:92160397; PMID:1789011 !$#accession S26406 !'##molecule_type DNA !'##residues 1-405,'D',407-745,'RI',746,'Q',748-952,'Y',954-1393,'FVYG' !1##label JAC !'##cross-references EMBL:X63853 !'##note this sequence has been revised in reference S19396 REFERENCE S19446 !$#authors Dujon, B.; Fairhead, C.; Thierry, A. !$#submission submitted to the Protein Sequence Database, March 1992 !$#accession S19756 !'##molecule_type DNA !'##residues 824-1407 ##label DUJ !'##cross-references EMBL:X59720; GSPDB:GN00003; MIPS:YCR042c REFERENCE S62390 !$#authors Poon, D.; Bai, Y.; Campbell, A.M.; Bjorklund, S.; Kim, Y.J.; !1Zhou, S.; Kornberg, R.D.; Weil, P.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1995) 92:8224-8228 !$#title Identification and characterization of a TFIID-like !1multiprotein complex from Saccharomyces cerevisiae. !$#cross-references MUID:95396770; PMID:7667272 !$#accession S62396 !'##molecule_type protein !'##residues 165-174;991-1000 ##label POO GENETICS !$#gene SGD:TSM1; TAF150; MIPS:YCR042c !'##cross-references SGD:S0000638; MIPS:YCR042c !$#map_position 3R CLASSIFICATION #superfamily TSM1 protein KEYWORDS transcription; transmembrane protein FEATURE !$41-58 #domain transmembrane #status predicted #label TM1\ !$887-903 #domain transmembrane #status predicted #label TM2\ !$1230-1246 #domain transmembrane #status predicted #label TM3 SUMMARY #length 1407 #molecular-weight 161470 #checksum 5585 SEQUENCE /// ENTRY S22853 #type complete TITLE datin - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES oligo(dA).oligo(dT)-binding protein; protein YM8339.06; protein YML113w ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 12-Nov-1999 ACCESSIONS S22853; S30600; S53959 REFERENCE S22852 !$#authors Winter, E.; Varshavsky, A. !$#journal EMBO J. (1989) 8:1867-1877 !$#title A DNA binding protein that recognizes oligo(dA)-oligo(dT) !1tracts. !$#cross-references MUID:89356664; PMID:2670564 !$#accession S22853 !'##molecule_type DNA !'##residues 1-248 ##label WIN1 !'##cross-references EMBL:X15478; NID:g3638; PIDN:CAA33505.1; PID:g3639 !$#accession S30600 !'##molecule_type protein !'##residues 'XX',3-12,'X',14,'X',16-23,'X',25 ##label WIN2 REFERENCE S53954 !$#authors Skelton, J.; Churcher, C.M. !$#submission submitted to the EMBL Data Library, May 1995 !$#accession S53959 !'##molecule_type DNA !'##residues 1-248 ##label SKE !'##cross-references EMBL:Z49210; NID:g798881; PIDN:CAA89105.1; !1PID:g798887; GSPDB:GN00013; MIPS:YML113w !'##experimental_source strain AB972 GENETICS !$#gene SGD:DAT1; MIPS:YML113w !'##cross-references SGD:S0004581; MIPS:YML113w !$#map_position 13L CLASSIFICATION #superfamily datin KEYWORDS DNA binding; tandem repeat FEATURE !$2-248 #product datin #status experimental #label MAT\ !$3-33 #region 13-residue repeats\ !$111-127 #region glutamine-rich\ !$155-188 #region asparagine-rich SUMMARY #length 248 #molecular-weight 27067 #checksum 8027 SEQUENCE /// ENTRY BWASBE #type complete TITLE bimE protein - Emericella nidulans ORGANISM #formal_name Emericella nidulans, Aspergillus nidulans DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jul-1999 ACCESSIONS A37879 REFERENCE A37879 !$#authors Engle, D.B.; Osmani, S.A.; Osmani, A.H.; Rosborough, S.; !1Xiang, X.; Morris, N.R. !$#journal J. Biol. Chem. (1990) 265:16132-16137 !$#title A negative regulator of mitosis in Aspergillus is a putative !1membrane-spanning protein. !$#cross-references MUID:90375468; PMID:1697851 !$#accession A37879 !'##molecule_type mRNA !'##residues 1-2073 ##label ENG !'##cross-references GB:M59705; GB:J05607; NID:g168026; PIDN:AAA51478.1; !1PID:g168027 !'##note in addition to three predicted transmembrane domains, there are !1several potential N-glycosylation sites, five possible sites !1for phosphorylation by cAMP-dependent protein kinase and one !1for casein kinase, and one sequence that resembles a nuclear !1localization signal COMMENT This protein is part of a regulatory pathway that includes !1the nimA protein kinase. It is required to prevent premature !1entry into mitosis. Mutations to this protein both cause !1cells to enter mitosis and prevent them from leaving !1mitosis. GENETICS !$#gene bimE CLASSIFICATION #superfamily bimE protein KEYWORDS cell cycle control; mitosis; transmembrane protein FEATURE !$1623-1643 #domain transmembrane #status predicted #label TM1\ !$1685-1703 #domain transmembrane #status predicted #label TM2\ !$1746-1764 #domain transmembrane #status predicted #label TM3 SUMMARY #length 2073 #molecular-weight 229177 #checksum 7408 SEQUENCE /// ENTRY BWSMNG #type complete TITLE strN protein - Streptomyces griseus ORGANISM #formal_name Streptomyces griseus DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS S18621; S19780 REFERENCE S18617 !$#authors Pissowotzki, K.; Mansouri, K.; Piepersberg, W. !$#journal Mol. Gen. Genet. (1991) 231:113-123 !$#title Genetics of streptomycin production in Streptomyces griseus: !1molecular structure and putative function of genes !1strELMB2N. !$#cross-references MUID:92092953; PMID:1661369 !$#accession S18621 !'##molecule_type DNA !'##residues 1-319 ##label PIS !'##cross-references EMBL:X62567; NID:g49009; PIDN:CAA44440.1; !1PID:g581675 !'##note the authors translated the codon GTC for residue 60 as Ser, CGG !1for residue 61 as Val, GAT fir residue 63 as Arg, and CCC !1for residue 119 as Phe !'##note the authors translated the initiation codon GTG for residue 1 !1as Val GENETICS !$#gene strN !$#start_codon GTG CLASSIFICATION #superfamily strN protein SUMMARY #length 319 #molecular-weight 35679 #checksum 1087 SEQUENCE /// ENTRY BWBY11 #type complete TITLE sporulation-specific protein SPO11 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YHL022c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 23-Mar-2001 ACCESSIONS S05854; S46836 REFERENCE S05854 !$#authors Atcheson, C.L.; DiDomenico, B.; Frackman, S.; Esposito, !1R.E.; Elder, R.T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:8035-8039 !$#title Isolation, DNA sequence, and regulation of a !1meiosis-specific eukaryotic recombination gene. !$#cross-references MUID:88068530; PMID:3317399 !$#accession S05854 !'##molecule_type DNA !'##residues 1-398 ##label ATC !'##cross-references EMBL:J02987; NID:g172658; PIDN:AAA65532.1; !1PID:g172660 !'##experimental_source strain REE526 REFERENCE S46796 !$#authors Favello, T. !$#submission submitted to the EMBL Data Library, June 1994 !$#description The sequence of S. cerevisiae cosmid 9433. !$#accession S46836 !'##molecule_type DNA !'##residues 1-398 ##label FAV !'##cross-references EMBL:U11582; NID:g2289793; PID:g508758; !1GSPDB:GN00008; MIPS:YHL022c GENETICS !$#gene SGD:SPO11; MIPS:YHL022c !'##cross-references SGD:S0001014; MIPS:YHL022c !$#map_position 8L FUNCTION !$#description required for meiotic recombination CLASSIFICATION #superfamily SPO11 protein KEYWORDS sporulation SUMMARY #length 398 #molecular-weight 45412 #checksum 4110 SEQUENCE /// ENTRY BVBYN1 #type complete TITLE RNA1 protein - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YM9959.17c; protein YMR235c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 21-Jul-2000 ACCESSIONS A32492; S21503; S37286; S57602; S05779 REFERENCE A32492 !$#authors Traglia, H.M.; Atkinson, N.S.; Hopper, A.K. !$#journal Mol. Cell. Biol. (1989) 9:2989-2999 !$#title Structural and functional analyses of Saccharomyces !1cerevisiae wild-type and mutant RNA1 genes. !$#cross-references MUID:89384559; PMID:2674676 !$#accession A32492 !'##molecule_type DNA !'##residues 1-407 ##label TRA1 !'##cross-references EMBL:M27142; NID:g172429; PIDN:AAA34983.1; !1PID:g172430 REFERENCE S21503 !$#authors Koh, S.S.; Young, S.R.; Young, H.S.; Hyen, S.K. !$#submission submitted to the EMBL Data Library, December 1989 !$#description Nucleotide sequence of RNA1 gene of S. cerevisiae. !$#accession S21503 !'##molecule_type DNA !'##residues 1-41,'E',43-184,'VREWIRSLLSSGFEKPLRS',204-407 ##label KOH !'##cross-references EMBL:X17376; NID:g4343; PIDN:CAA35248.1; PID:g4344 REFERENCE S37286 !$#authors Crouch, R.J. !$#submission submitted to the EMBL Data Library, January 1991 !$#accession S37286 !'##molecule_type DNA !'##residues 188-221,'S',223-407 ##label CRO !'##cross-references EMBL:X57160; NID:g4356; PIDN:CAA40449.1; PID:g4358 REFERENCE S57587 !$#authors Skelton, J.; Churcher, C.M. !$#submission submitted to the EMBL Data Library, June 1995 !$#accession S57602 !'##molecule_type DNA !'##residues 1-407 ##label SKE !'##cross-references EMBL:Z49939; NID:g887599; PIDN:CAA90206.1; !1PID:g887616; GSPDB:GN00013; MIPS:YMR235c !'##experimental_source strain AB972 GENETICS !$#gene SGD:RNA1; MIPS:YMR235c !'##cross-references SGD:S0004848; MIPS:YMR235c !$#map_position 13R CLASSIFICATION #superfamily RNA1 protein FEATURE !$348-375 #region acidic SUMMARY #length 407 #molecular-weight 45815 #checksum 258 SEQUENCE /// ENTRY S19516 #type complete TITLE RVS161 protein - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YCR009c ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 21-Jul-2000 ACCESSIONS S19516; S28651; S22849 REFERENCE S19420 !$#authors Goffeau, A.; Purnelle, B.; Skala, J. !$#submission submitted to the Protein Sequence Database, March 1992 !$#accession S19516 !'##molecule_type DNA !'##residues 1-265 ##label GOF !'##cross-references EMBL:X59720; NID:g1907116; PIDN:CAA42326.1; !1PID:g1907152; GSPDB:GN00003; MIPS:YCR009c REFERENCE S28651 !$#authors Crouzet, M.; Urdaci, M.; Dulau, L.; Aigle, M. !$#journal Yeast (1991) 7:727-743 !$#title Yeast mutant affected for viability upon nutrient !1starvation: characterization and cloning of the RVS161 gene. !$#cross-references MUID:92133163; PMID:1776363 !$#accession S28651 !'##molecule_type DNA !'##residues 1-94,'E',96-265 ##label CRO !'##cross-references EMBL:X63315; NID:g4417; PIDN:CAA44926.1; PID:g4418 REFERENCE S22849 !$#authors Urdaci, M.; Dulau, L.; Aigle, M.; Crouzet, M. !$#journal Yeast (1990) 6:173-176 !$#title Sequence of the yeast gene RVS161 located on chromosome III. !$#cross-references MUID:90224366; PMID:2183524 !$#accession S22849 !'##molecule_type DNA !'##residues 1-94,'E',96-265 ##label URD !'##cross-references EMBL:X63315; NID:g4417; PIDN:CAA44926.1; PID:g4418 REFERENCE S25353 !$#authors Skala, J.; Purnelle, B.; Goffeau, A. !$#journal Yeast (1992) 8:409-417 !$#title The complete sequence of a 10.8 kb segment distal of SUF2 on !1the right arm of chromosome III from Saccharomyces !1cerevisiae reveals seven open reading frames including the !1RVS161, ADP1 and PGK genes. !$#cross-references MUID:92327849; PMID:1626432 !$#contents annotation GENETICS !$#gene SGD:RVS161; MIPS:YCR009c !'##cross-references SGD:S0000602; MIPS:YCR009c !$#map_position 3R CLASSIFICATION #superfamily RVS161 protein; RVS161 protein homology FEATURE !$4-257 #domain RVS161 protein homology #label RVS SUMMARY #length 265 #molecular-weight 30250 #checksum 2223 SEQUENCE /// ENTRY S40887 #type complete TITLE RVS167 protein - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YDR388w ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Mar-1992 #sequence_revision 06-Feb-1995 #text_change 21-Jul-2000 ACCESSIONS S40887; S69672 REFERENCE S40887 !$#authors Bauer, F.; Urdaci, M.; Aigle, M.; Crouzet, M. !$#journal Mol. Cell. Biol. (1993) 13:5070-5084 !$#title Alteration of a yeast SH3 protein leads to conditional !1viability with defects in cytoskeletal and budding patterns. !$#cross-references MUID:93330299; PMID:8336735 !$#accession S40887 !'##molecule_type DNA !'##residues 1-482 ##label BAU !'##cross-references EMBL:M92092; NID:g172615; PIDN:AAA35051.1; !1PID:g172616 REFERENCE S69665 !$#authors Dietrich, F.S. !$#submission submitted to the EMBL Data Library, July 1995 !$#description The sequence of S. cerevisiae cosmids 9481, 9509, 9926, !19461, and lambda 3641. !$#accession S69672 !'##molecule_type DNA !'##residues 1-482 ##label DIE !'##cross-references EMBL:U32274; NID:g927313; PIDN:AAB64830.1; !1PID:g927321; GSPDB:GN00004; MIPS:YDR388w GENETICS !$#gene SGD:RVS167; MIPS:YDR388w !'##cross-references SGD:S0002796; MIPS:YDR388w !$#map_position 4R CLASSIFICATION #superfamily RVS167 protein; RVS161 protein homology; SH3 !1homology KEYWORDS transmembrane protein FEATURE !$4-270 #domain RVS161 protein homology #label RVS\ !$292-422 #region alanine/glycine/proline-rich\ !$428-477 #domain SH3 homology #label SH3 SUMMARY #length 482 #molecular-weight 52774 #checksum 2663 SEQUENCE /// ENTRY TRVKG1 #type complete TITLE terminal region recognition factor 1 - yeast (Kluyveromyces marxianus var. lactis) plasmid pGKl2 ALTERNATE_NAMES DNA-binding protein TRF1 ORGANISM #formal_name Kluyveromyces marxianus var. lactis, Candida sphaerica #note plasmid pGKl2, K2 DATE 30-Sep-1989 #sequence_revision 09-May-1997 #text_change 10-Sep-1999 ACCESSIONS S00968; S10336; S17251; A41628 REFERENCE S00959 !$#authors Tommasino, M.; Ricci, S.; Galeotti, C.L. !$#journal Nucleic Acids Res. (1988) 16:5863-5878 !$#title Genome organization of the killer plasmid pGKl2 from !1Kluyveromyces lactis. !$#cross-references MUID:88289339; PMID:3041369 !$#accession S00968 !'##molecule_type DNA !'##residues 1-103 ##label TOM !'##cross-references EMBL:X07776; NID:g2868; PIDN:CAA30611.1; PID:g2878 REFERENCE S10336 !$#authors Wilson, D.W.; Meacock, P.A. !$#journal Nucleic Acids Res. (1988) 16:8097-8112 !$#title Extranuclear gene expression in yeast: evidence for a !1plasmid-encoded RNA polymerase of unique structure. !$#cross-references MUID:88335549; PMID:3138657 !$#accession S10336 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-103 ##label WIL !'##cross-references EMBL:X07946; NID:g2883; PIDN:CAA30767.1; PID:g2884 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1988 REFERENCE A41628 !$#authors McNeel, D.G.; Tamanoi, F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:11398-11402 !$#title Terminal region recognition factor 1, a DNA-binding protein !1recognizing the inverted terminal repeats of the pGKl linear !1DNA plasmids. !$#cross-references MUID:92107957; PMID:1763054 !$#contents annotation; purification and activity after expression in E. !1coli REFERENCE S17251 !$#authors Tommasino, M. !$#journal Yeast (1991) 7:245-252 !$#title Killer system of Kluyveromyces lactis: the open reading !1frame 10 of the pGK12 plasmid encodes a putative DNA binding !1protein. !$#cross-references MUID:91353078; PMID:1882549 !$#accession S17251 !'##molecule_type DNA !'##residues 1-71;83-99 ##label TO2 !'##cross-references PIDN:AAB19610.1; PID:g234312; PIDN:AAB19611.1; !1PID:g234313 GENETICS !$#genome plasmid FUNCTION !$#description DNA binding; may play a role in the protein-primed !1initiation of the replication of the linear plasmid that !1encodes it CLASSIFICATION #superfamily DNA-binding protein TRF1 KEYWORDS DNA binding; DNA replication; plasmid replication SUMMARY #length 103 #molecular-weight 12061 #checksum 6721 SEQUENCE /// ENTRY S15969 #type complete TITLE terminal region recognition factor 1 - yeast (Saccharomyces kluyveri) plasmid pSKL ALTERNATE_NAMES DNA-binding protein TRF1 ORGANISM #formal_name Saccharomyces kluyveri DATE 19-Mar-1997 #sequence_revision 09-May-1997 #text_change 10-Sep-1999 ACCESSIONS S15969 REFERENCE S15960 !$#authors Hishinuma, F.; Hirai, K. !$#journal Mol. Gen. Genet. (1991) 226:97-106 !$#title Genome organization of the linear plasmid, pSKL, isolated !1from Saccharomyces kluyveri. !$#cross-references MUID:91238725; PMID:2034232 !$#accession S15969 !'##molecule_type DNA !'##residues 1-105 ##label HIS !'##cross-references EMBL:X54850; NID:g4868; PIDN:CAA38629.1; PID:g4878 GENETICS !$#genome plasmid FUNCTION !$#description this small, basic, DNA-binding protein is believed but not !1yet proven to play a role in the protein-primed initiation !1of the replication of the linear plasmid that encodes it CLASSIFICATION #superfamily DNA-binding protein TRF1 KEYWORDS DNA binding; DNA replication; plasmid replication SUMMARY #length 105 #molecular-weight 12145 #checksum 6148 SEQUENCE /// ENTRY RWBYS1 #type complete TITLE glycophospholipid-anchored surface glycoprotein GAS1 precursor - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES 115K glycoprotein; protein YM9952.09; protein YMR307w ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Dec-1991 #sequence_revision 03-Nov-1995 #text_change 28-Jan-2000 ACCESSIONS S53977; A39663; S20232; A40871; C49730; S12941; S13667 REFERENCE S53969 !$#authors Connor, R.; Churcher, C.M. !$#submission submitted to the EMBL Data Library, April 1995 !$#accession S53977 !'##molecule_type DNA !'##residues 1-559 ##label CON !'##cross-references EMBL:Z49212; NID:g798940; PIDN:CAA89140.1; !1PID:g798949; GSPDB:GN00013; MIPS:YMR307w REFERENCE A39663 !$#authors Nuoffer, C.; Jenoe, P.; Conzelmann, A.; Riezman, H. !$#journal Mol. Cell. Biol. (1991) 11:27-37 !$#title Determinants for glycophospholipid anchoring of the !1Saccharomyces cerevisiae GAS1 protein to the plasma !1membrane. !$#cross-references MUID:91094841; PMID:1824714 !$#accession A39663 !'##molecule_type DNA !'##residues 1-210,'A',212-559 ##label NUO1 !'##cross-references EMBL:X53424; NID:g3729; PIDN:CAA37512.1; PID:g3730 !$#accession S20232 !'##molecule_type protein !'##residues 'XX',25-39;237-240;435-437;189-190 ##label NUO2 REFERENCE A40871 !$#authors Vai, M.; Gatti, E.; Lacana, E.; Popolo, L.; Alberghina, L. !$#journal J. Biol. Chem. (1991) 266:12242-12248 !$#title Isolation and deduced amino acid sequence of the gene !1encoding gp115, a yeast glycophospholipid-anchored protein !1containing a serine-rich region. !$#cross-references MUID:91286239; PMID:2061310 !$#accession A40871 !'##molecule_type DNA !'##residues 1-559 ##label ALB !'##cross-references EMBL:X56399; NID:g3739; PIDN:CAA39809.1; PID:g3740 REFERENCE A49730 !$#authors Balzi, E.; Wang, M.; Leterme, S.; Van Dyck, L.; Goffeau, A. !$#journal J. Biol. Chem. (1994) 269:2206-2214 !$#title PDR5, a novel yeast multidrug resistance conferring !1transporter controlled by the transcription regulator PDR1. !$#cross-references MUID:94124579; PMID:8294477 !$#accession C49730 !'##molecule_type protein !'##residues 23-36 ##label BAL GENETICS !$#gene SGD:GAS1; GGP1; GP115; SGD:S0004924 !'##cross-references MIPS:YMR307w; SGD:S0004924 !$#map_position 13R CLASSIFICATION #superfamily glycophospholipid-anchored surface glycoprotein !1GAS1 KEYWORDS blocked carboxyl end; glycoprotein; lipoprotein; membrane !1protein; phosphatidylinositol linkage; phosphoprotein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-528 #product glycophospholipid-anchored surface !8glycoprotein GAS1 #status experimental #label MAT\ !$438-525 #region serine/threonine-rich\ !$529-559 #domain carboxyl-terminal propeptide #status !8predicted #label CTP\ !$40,57,95,149,165, !$253,283,321,409,495 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$528 #modified_site GPI-anchor ethanolamine amidated !8carboxyl end (Asn) (in mature form) #status !8experimental SUMMARY #length 559 #molecular-weight 59582 #checksum 3463 SEQUENCE /// ENTRY TVVPT4 #type complete TITLE large T antigen - rhesus polyomavirus ORGANISM #formal_name Polyomavirus maccacae 1 #common_name rhesus polyomavirus, SV40 DATE 30-Nov-1980 #sequence_revision 30-Nov-1980 #text_change 12-Dec-1997 ACCESSIONS B03631; B36763; A03607 REFERENCE A03631 !$#authors Reddy, V.B.; Thimmappaya, B.; Dhar, R.; Subramanian, K.N.; !1Zain, B.S.; Pan, J.; Ghosh, P.K.; Celma, M.L.; Weissman, !1S.M. !$#journal Science (1978) 200:494-502 !$#title The genome of simian virus 40. !$#cross-references MUID:78159686; PMID:205947 !$#accession B03631 !'##molecule_type DNA !'##residues 1-708 ##label RED REFERENCE A36763 !$#authors Fiers, W.; Contreras, R.; Haegeman, G.; Rogiers, R.; van de !1Voorde, A.; van Heuverswyn, H.; van Herreweghe, J.; !1Volckaert, G.; Ysebaert, M. !$#journal Nature (1978) 273:113-120 !$#title Complete nucleotide sequence of SV40 DNA. !$#cross-references MUID:78156432; PMID:205802 !$#accession B36763 !'##molecule_type DNA !'##residues 1-530,'Y',532-548,'P',550-551,'P',553-708 ##label FIE !'##experimental_source strain 776 COMMENT The initial 82 residues of the large T and small t antigens !1from SV40 are coded by the same nucleotide sequence. CLASSIFICATION #superfamily large T antigen; dnaJ amino-terminal homology KEYWORDS acetylated amino end FEATURE !$12-62 #domain dnaJ amino-terminal homology #status atypical !8#label DNJ\ !$1 #modified_site acetylated amino end (Met) #status !8experimental SUMMARY #length 708 #molecular-weight 81585 #checksum 2108 SEQUENCE /// ENTRY TVVPTB #type complete TITLE large T antigen - polyomavirus BK ORGANISM #formal_name Polyomavirus hominis 1 #common_name polyomavirus BK DATE 28-Feb-1981 #sequence_revision 28-Feb-1981 #text_change 16-Jul-1999 ACCESSIONS C03632; C36762; A92981; A03608 REFERENCE A03632 !$#authors Seif, I.; Khoury, G.; Dhar, R. !$#journal Cell (1979) 18:963-977 !$#title The genome of human papovavirus BKV. !$#cross-references MUID:80090082; PMID:229976 !$#accession C03632 !'##molecule_type DNA !'##residues 1-695 ##label SEI !'##cross-references GB:V01108; GB:J02038; NID:g60844; PIDN:CAA24300.1; !1PID:g60849 !'##experimental_source strain Dunlop REFERENCE A36762 !$#authors Yang, R.C.A.; Wu, R. !$#journal Science (1979) 206:456-462 !$#title BK virus DNA: complete nucleotide sequence of a human tumor !1virus. !$#cross-references MUID:80058557; PMID:228391 !$#accession C36762 !'##molecule_type DNA !'##residues 1-33,35-259,'N',261-334,'K',336,'V',338-445,'R',447-695 !1##label YAN !'##cross-references GB:V01109; GB:J02039; NID:g60851; PIDN:CAA24302.1; !1PID:g60852 !'##experimental_source strain MM REFERENCE A92981 !$#authors Yang, R.C.A.; Young, A.; Wu, R. !$#journal J. Virol. (1980) 34:416-430 !$#title BK virus DNA sequence coding for the t and T antigens and !1evaluation of methods for determining sequence homology. !$#cross-references MUID:80185151; PMID:6246273 !$#accession A92981 !'##molecule_type DNA !'##residues 1-695 ##label YA2 !'##experimental_source strain MM CLASSIFICATION #superfamily large T antigen; dnaJ amino-terminal homology KEYWORDS early protein; glycoprotein FEATURE !$12-62 #domain dnaJ amino-terminal homology #status atypical !8#label DNJ\ !$155 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 695 #molecular-weight 80505 #checksum 6985 SEQUENCE /// ENTRY TVVPAS #type complete TITLE large T antigen - polyomavirus BK (strain AS) ORGANISM #formal_name Polyomavirus hominis 1 #common_name polyomavirus BK #note host Homo sapiens (man) DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jul-1999 ACCESSIONS A33278 REFERENCE A33278 !$#authors Tavis, J.E.; Walker, D.L.; Gardner, S.D.; Frisque, R.J. !$#journal J. Virol. (1989) 63:901-911 !$#title Nucleotide sequence of the human polyomavirus AS virus, an !1antigenic variant of BK virus. !$#cross-references MUID:89095020; PMID:2536111 !$#accession A33278 !'##molecule_type DNA !'##residues 1-691 ##label TAV !'##cross-references GB:M23122; NID:g332774; PIDN:AAA46878.1; !1PID:g332775 COMMENT The DNA sequence was obtained from Genbank, release 61.0. GENETICS !$#introns 81/3 CLASSIFICATION #superfamily large T antigen; dnaJ amino-terminal homology KEYWORDS early protein; glycoprotein FEATURE !$12-62 #domain dnaJ amino-terminal homology #status atypical !8#label DNJ\ !$78,155 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 691 #molecular-weight 80128 #checksum 3286 SEQUENCE /// ENTRY TVVPTJ #type complete TITLE large T antigen - polyomavirus JC ORGANISM #formal_name Polyomavirus hominis 2 #common_name polyomavirus JC DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS A03609 REFERENCE A03633 !$#authors Frisque, R.J.; Bream, G.L.; Cannella, M.T. !$#journal J. Virol. (1984) 51:458-469 !$#title Human polyomavirus JC virus genome. !$#cross-references MUID:84268011; PMID:6086957 !$#accession A03609 !'##molecule_type DNA !'##residues 1-688 ##label FRI !'##cross-references GB:J02226; GB:J02227; EMBL:V01118; NID:g1083524; !1PIDN:AAA82102.1; PID:g332768 CLASSIFICATION #superfamily large T antigen; dnaJ amino-terminal homology KEYWORDS early protein FEATURE !$12-62 #domain dnaJ amino-terminal homology #status atypical !8#label DNJ SUMMARY #length 688 #molecular-weight 79310 #checksum 3769 SEQUENCE /// ENTRY TVVPBP #type complete TITLE large T antigen - bovine polyomavirus ORGANISM #formal_name Polyomavirus bovis #common_name bovine polyomavirus, WRSV DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jun-2000 ACCESSIONS JU0357 REFERENCE JU0357 !$#authors Schuurman, R.; Sol, C.; van der Noordaa, J. !$#journal J. Gen. Virol. (1990) 71:1723-1735 !$#title The complete nucleotide sequence of bovine polyomavirus. !$#cross-references MUID:90362059; PMID:2167926 !$#accession JU0357 !'##molecule_type DNA !'##residues 1-586 ##label SCH !'##cross-references GB:D13942; GB:D00755; GB:M74843; NID:g222302; !1PIDN:BAA03040.1; PID:g222303 CLASSIFICATION #superfamily large T antigen; dnaJ amino-terminal homology KEYWORDS early protein SUMMARY #length 586 #molecular-weight 67049 #checksum 1813 SEQUENCE /// ENTRY TVVPTL #type complete TITLE large T antigen - lymphotropic polyomavirus ORGANISM #formal_name Polyomavirus cercopitheci #common_name lymphotropic polyomavirus #note host (African green monkey) DATE 13-Aug-1986 #sequence_revision 13-Aug-1986 #text_change 12-Dec-1997 ACCESSIONS A03610 REFERENCE A03634 !$#authors Pawlita, M.; Clad, A.; zur Hausen, H. !$#journal Virology (1985) 143:196-211 !$#title Complete DNA sequence of lymphotropic papovavirus: prototype !1of a new species of the polyomavirus genus. !$#cross-references MUID:86045879; PMID:2998001 !$#accession A03610 !'##molecule_type DNA !'##residues 1-697 ##label PAW !'##note the authors translated the codon ATT for residue 401 as Thr GENETICS !$#introns 79/3 CLASSIFICATION #superfamily large T antigen; dnaJ amino-terminal homology KEYWORDS early protein FEATURE !$12-62 #domain dnaJ amino-terminal homology #status atypical !8#label DNJ SUMMARY #length 697 #molecular-weight 79762 #checksum 1514 SEQUENCE /// ENTRY TVVPT #type complete TITLE large T antigen - mouse polyomavirus ORGANISM #formal_name Polyomavirus muris #common_name mouse polyomavirus DATE 31-Jul-1980 #sequence_revision 31-Jul-1980 #text_change 16-Jul-1999 ACCESSIONS D03635; C36761; A03611 REFERENCE A03635 !$#authors Soeda, E.; Arrand, J.R.; Smolar, N.; Walsh, J.E.; Griffin, !1B.E. !$#journal Nature (1980) 283:445-453 !$#title Coding potential and regulatory signals of the polyoma virus !1genome. !$#cross-references MUID:80099647; PMID:6243401 !$#accession D03635 !'##molecule_type DNA !'##residues 1-785 ##label SOE !'##cross-references GB:J02288; GB:J02290; GB:J02291; GB:J02292; !1GB:K00932; GB:K00997; GB:K01041; GB:K01071; GB:K01072; !1GB:V01117; GB:V01147; NID:g332752; PIDN:AAB59901.1; !1PID:g332753 !'##experimental_source strain A2 REFERENCE A36761 !$#authors Friedmann, T.; Esty, A.; LaPorte, P.; Deininger, P. !$#journal Cell (1979) 17:715-724 !$#title The nucleotide sequence and genome organization of the !1polyoma early region: extensive nucleotide and amino acid !1homology with SV40. !$#cross-references MUID:80001963; PMID:225042 !$#accession C36761 !'##molecule_type DNA !'##residues 1-369,'SV',371-493,'DGV',496-645,'DYLD',650-777,'EYS' !1##label FRI !'##cross-references GB:J02289; GB:V01151; NID:g332759; PIDN:AAA46872.1; !1PID:g332760 !'##experimental_source strain 3 CLASSIFICATION #superfamily large T antigen; dnaJ amino-terminal homology KEYWORDS early protein FEATURE !$12-62 #domain dnaJ amino-terminal homology #status atypical !8#label DNJ SUMMARY #length 785 #molecular-weight 88090 #checksum 4546 SEQUENCE /// ENTRY TVVPCP #type complete TITLE large T antigen - mouse polyomavirus (strain Crawford small-plaque) ORGANISM #formal_name Polyomavirus muris #common_name mouse polyomavirus DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 12-Dec-1997 ACCESSIONS A28838; A94520 REFERENCE A28838 !$#authors Rothwell, V.M.; Folk, W.R. !$#journal J. Virol. (1983) 48:472-480 !$#title Comparison of the DNA sequence of the Crawford small-plaque !1variant of polyomavirus with those of polyomaviruses A2 and !1strain 3. !$#cross-references MUID:84011043; PMID:6312103 !$#accession A28838 !'##molecule_type DNA !'##residues 1-777 ##label RO1 !'##cross-references GB:K02737; NID:g332788 !'##note this ORF is not annotated in GenBank entry PLYCSP REFERENCE A94520 !$#authors Rothwell, V.M. !$#submission submitted to GenBank, November 1985 !$#accession A94520 !'##molecule_type DNA !'##residues 1-777 ##label RO2 !'##cross-references GB:K02737; NID:g332788 GENETICS !$#introns 79/3 CLASSIFICATION #superfamily large T antigen; dnaJ amino-terminal homology KEYWORDS early protein FEATURE !$12-62 #domain dnaJ amino-terminal homology #status atypical !8#label DNJ SUMMARY #length 777 #molecular-weight 87108 #checksum 6462 SEQUENCE /// ENTRY TVVPMK #type complete TITLE large T antigen - mouse polyomavirus (strain Kilham) ORGANISM #formal_name Polyomavirus muris #common_name mouse polyomavirus DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 12-Dec-1997 ACCESSIONS A37945 REFERENCE A37945 !$#authors Mayer, M.; Doerries, K. !$#journal Virology (1991) 181:469-480 !$#title Nucleotide sequence and genome organization of the murine !1polyomavirus, Kilham strain. !$#cross-references MUID:91196237; PMID:1849675 !$#accession A37945 !'##molecule_type DNA !'##residues 1-649 ##label MAY !'##cross-references GB:M55904 CLASSIFICATION #superfamily large T antigen; dnaJ amino-terminal homology KEYWORDS early protein FEATURE !$12-62 #domain dnaJ amino-terminal homology #status atypical !8#label DNJ SUMMARY #length 649 #molecular-weight 74836 #checksum 3073 SEQUENCE /// ENTRY TVVPTH #type complete TITLE large T antigen - hamster polyomavirus ORGANISM #formal_name hamster polyomavirus DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 16-Jul-1999 ACCESSIONS A03612 REFERENCE A03636 !$#authors Delmas, V.; Bastien, C.; Scherneck, S.; Feunteun, J. !$#journal EMBO J. (1985) 4:1279-1286 !$#title A new member of the polyomavirus family: the hamster !1papovavirus. Complete nucleotide sequence and transformation !1properties. !$#cross-references MUID:85230582; PMID:2988942 !$#accession A03612 !'##molecule_type DNA !'##residues 1-751 ##label DEL !'##cross-references GB:M26281; NID:g825486; PIDN:AAA67118.1; !1PID:g825489 GENETICS !$#introns 77/3 CLASSIFICATION #superfamily large T antigen; dnaJ amino-terminal homology KEYWORDS early protein FEATURE !$12-62 #domain dnaJ amino-terminal homology #status atypical !8#label DNJ SUMMARY #length 751 #molecular-weight 85987 #checksum 3251 SEQUENCE /// ENTRY TVVPBF #type complete TITLE large T antigen - budgerigar fledgling disease virus ORGANISM #formal_name budgerigar fledgling disease virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 31-Oct-1997 ACCESSIONS D29194 REFERENCE A29194 !$#authors Rott, O.; Kroeger, M.; Mueller, H.; Hobom, G. !$#journal Virology (1988) 165:74-86 !$#title The genome of budgerigar fledgling disease virus, an avian !1polyomavirus. !$#cross-references MUID:88265888; PMID:2838972 !$#accession D29194 !'##molecule_type DNA !'##residues 1-554 ##label ROT !'##cross-references GB:M20775 GENETICS !$#introns 83/3 CLASSIFICATION #superfamily large T antigen; dnaJ amino-terminal homology KEYWORDS early protein FEATURE !$6-54 #domain dnaJ amino-terminal homology #status atypical !8#label DNJ SUMMARY #length 554 #molecular-weight 63213 #checksum 300 SEQUENCE /// ENTRY TVVPM #type complete TITLE middle T antigen - mouse polyomavirus ORGANISM #formal_name Polyomavirus muris #common_name mouse polyomavirus DATE 31-Jul-1980 #sequence_revision 18-Aug-1982 #text_change 16-Jul-1999 ACCESSIONS A93718; B03635; A03613 REFERENCE A93718 !$#authors Deininger, P.L.; Esty, A.; LaPorte, P.; Hsu, H.; Friedmann, !1T. !$#journal Nucleic Acids Res. (1980) 8:855-860 !$#title The nucleotide sequence and restriction enzyme sites of the !1polyoma genome. !$#cross-references MUID:81053800; PMID:6253927 !$#accession A93718 !'##molecule_type DNA !'##residues 1-440 ##label DEI !'##experimental_source strain 3 REFERENCE A03635 !$#authors Soeda, E.; Arrand, J.R.; Smolar, N.; Walsh, J.E.; Griffin, !1B.E. !$#journal Nature (1980) 283:445-453 !$#title Coding potential and regulatory signals of the polyoma virus !1genome. !$#cross-references MUID:80099647; PMID:6243401 !$#accession B03635 !'##molecule_type DNA !'##residues 1-191,'K',212-346,'G',348-440 ##label SOE !'##cross-references GB:J02288; GB:J02290; GB:J02291; GB:J02292; !1GB:K00932; GB:K00997; GB:K01041; GB:K01071; GB:K01072; !1GB:V01117; GB:V01147; NID:g332752; PIDN:AAB59900.1; !1PID:g332754 !'##experimental_source strain A2 GENETICS !$#introns 192/1 CLASSIFICATION #superfamily middle T antigen; dnaJ amino-terminal homology KEYWORDS early protein SUMMARY #length 440 #molecular-weight 50831 #checksum 5838 SEQUENCE /// ENTRY TVVPMP #type complete TITLE middle T antigen - mouse polyomavirus (strain Crawford small-plaque) ORGANISM #formal_name Polyomavirus muris #common_name mouse polyomavirus DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 12-Dec-1997 ACCESSIONS B28838; B94520 REFERENCE A28838 !$#authors Rothwell, V.M.; Folk, W.R. !$#journal J. Virol. (1983) 48:472-480 !$#title Comparison of the DNA sequence of the Crawford small-plaque !1variant of polyomavirus with those of polyomaviruses A2 and !1strain 3. !$#cross-references MUID:84011043; PMID:6312103 !$#accession B28838 !'##molecule_type DNA !'##residues 1-421 ##label RO1 !'##cross-references GB:K02737; NID:g332788 !'##note this ORF is not annotated in GenBank entry PLYCSP REFERENCE A94520 !$#authors Rothwell, V.M. !$#submission submitted to GenBank, November 1985 !$#accession B94520 !'##molecule_type DNA !'##residues 1-421 ##label RO2 GENETICS !$#introns 192/1 CLASSIFICATION #superfamily middle T antigen; dnaJ amino-terminal homology KEYWORDS early protein FEATURE !$12-62 #domain dnaJ amino-terminal homology #status atypical !8#label DNJ SUMMARY #length 421 #molecular-weight 48651 #checksum 7637 SEQUENCE /// ENTRY TVVPMH #type complete TITLE middle T antigen - hamster polyomavirus ORGANISM #formal_name hamster polyomavirus DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 16-Jul-1999 ACCESSIONS A03615 REFERENCE A03636 !$#authors Delmas, V.; Bastien, C.; Scherneck, S.; Feunteun, J. !$#journal EMBO J. (1985) 4:1279-1286 !$#title A new member of the polyomavirus family: the hamster !1papovavirus. Complete nucleotide sequence and transformation !1properties. !$#cross-references MUID:85230582; PMID:2988942 !$#accession A03615 !'##molecule_type DNA !'##residues 1-401 ##label DEL !'##cross-references GB:M26281; NID:g825486; PIDN:AAA67117.1; !1PID:g825488 GENETICS !$#introns 194/2 CLASSIFICATION #superfamily middle T antigen; dnaJ amino-terminal homology KEYWORDS early protein FEATURE !$12-62 #domain dnaJ amino-terminal homology #status atypical !8#label DNJ SUMMARY #length 401 #molecular-weight 46562 #checksum 1501 SEQUENCE /// ENTRY TVVPA #type complete TITLE small T antigen - mouse polyomavirus ORGANISM #formal_name Polyomavirus muris #common_name mouse polyomavirus DATE 31-Jul-1980 #sequence_revision 31-Jul-1980 #text_change 24-Sep-1999 ACCESSIONS C03635; B36761; C28838; A03614 REFERENCE A03635 !$#authors Soeda, E.; Arrand, J.R.; Smolar, N.; Walsh, J.E.; Griffin, !1B.E. !$#journal Nature (1980) 283:445-453 !$#title Coding potential and regulatory signals of the polyoma virus !1genome. !$#cross-references MUID:80099647; PMID:6243401 !$#accession C03635 !'##molecule_type DNA !'##residues 1-195 ##label SOE !'##cross-references GB:J02288; GB:J02290; GB:J02291; GB:J02292; !1GB:K00932; GB:K00997; GB:K01041; GB:K01071; GB:K01072; !1GB:V01117; GB:V01147; NID:g332752; PIDN:AAB59899.1; !1PID:g332755 !'##experimental_source strain A2 REFERENCE A36761 !$#authors Friedmann, T.; Esty, A.; LaPorte, P.; Deininger, P. !$#journal Cell (1979) 17:715-724 !$#title The nucleotide sequence and genome organization of the !1polyoma early region: extensive nucleotide and amino acid !1homology with SV40. !$#cross-references MUID:80001963; PMID:225042 !$#accession B36761 !'##molecule_type DNA !'##residues 1-195 ##label FRI !'##cross-references GB:J02288; GB:J02290; GB:J02291; GB:J02292; !1GB:K00932; GB:K00997; GB:K01041; GB:K01071; GB:K01072; !1GB:V01117; GB:V01147; NID:g332752; PIDN:AAB59899.1; !1PID:g332755 !'##experimental_source strain 3 REFERENCE A28838 !$#authors Rothwell, V.M.; Folk, W.R. !$#journal J. Virol. (1983) 48:472-480 !$#title Comparison of the DNA sequence of the Crawford small-plaque !1variant of polyomavirus with those of polyomaviruses A2 and !1strain 3. !$#cross-references MUID:84011043; PMID:6312103 !$#accession C28838 !'##molecule_type DNA !'##residues 1-195 ##label ROT !'##cross-references GB:K02737; NID:g332788 !'##experimental_source strain Crawford small-plaque !'##note this ORF is not annotated in GenBank entry PLYCSP GENETICS !$#introns 192/1 CLASSIFICATION #superfamily small T antigen; dnaJ amino-terminal homology KEYWORDS early protein FEATURE !$12-62 #domain dnaJ amino-terminal homology #status atypical !8#label DNJ SUMMARY #length 195 #molecular-weight 22811 #checksum 2433 SEQUENCE /// ENTRY TVVPMA #type complete TITLE small T antigen - mouse polyomavirus (strain Kilham) ORGANISM #formal_name Polyomavirus muris #common_name mouse polyomavirus DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 12-Dec-1997 ACCESSIONS B37945 REFERENCE A37945 !$#authors Mayer, M.; Doerries, K. !$#journal Virology (1991) 181:469-480 !$#title Nucleotide sequence and genome organization of the murine !1polyomavirus, Kilham strain. !$#cross-references MUID:91196237; PMID:1849675 !$#accession B37945 !'##molecule_type DNA !'##residues 1-158 ##label MAY !'##cross-references GB:M55904 CLASSIFICATION #superfamily small T antigen; dnaJ amino-terminal homology KEYWORDS early protein FEATURE !$12-62 #domain dnaJ amino-terminal homology #status atypical !8#label DNJ SUMMARY #length 158 #molecular-weight 18798 #checksum 4007 SEQUENCE /// ENTRY TVVPAH #type complete TITLE small T antigen - hamster polyomavirus ORGANISM #formal_name hamster polyomavirus DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 16-Jul-1999 ACCESSIONS A03616 REFERENCE A03636 !$#authors Delmas, V.; Bastien, C.; Scherneck, S.; Feunteun, J. !$#journal EMBO J. (1985) 4:1279-1286 !$#title A new member of the polyomavirus family: the hamster !1papovavirus. Complete nucleotide sequence and transformation !1properties. !$#cross-references MUID:85230582; PMID:2988942 !$#accession A03616 !'##molecule_type DNA !'##residues 1-194 ##label DEL !'##cross-references GB:M26281; NID:g825486; PIDN:AAA67116.1; !1PID:g825487 GENETICS !$#introns 193/1 CLASSIFICATION #superfamily small T antigen; dnaJ amino-terminal homology KEYWORDS early protein FEATURE !$12-62 #domain dnaJ amino-terminal homology #status atypical !8#label DNJ SUMMARY #length 194 #molecular-weight 22625 #checksum 2072 SEQUENCE /// ENTRY TVVPAL #type complete TITLE small T antigen - lymphotropic polyomavirus ORGANISM #formal_name Polyomavirus cercopitheci #common_name lymphotropic polyomavirus #note host (African green monkey) DATE 13-Aug-1986 #sequence_revision 13-Aug-1986 #text_change 31-Oct-1997 ACCESSIONS A03617 REFERENCE A03634 !$#authors Pawlita, M.; Clad, A.; zur Hausen, H. !$#journal Virology (1985) 143:196-211 !$#title Complete DNA sequence of lymphotropic papovavirus: prototype !1of a new species of the polyomavirus genus. !$#cross-references MUID:86045879; PMID:2998001 !$#accession A03617 !'##molecule_type DNA !'##residues 1-189 ##label PAW CLASSIFICATION #superfamily small T antigen; dnaJ amino-terminal homology KEYWORDS early protein FEATURE !$12-62 #domain dnaJ amino-terminal homology #status atypical !8#label DNJ SUMMARY #length 189 #molecular-weight 22171 #checksum 1332 SEQUENCE /// ENTRY TVVPA4 #type complete TITLE small T antigen - rhesus polyomavirus ORGANISM #formal_name Polyomavirus maccacae 1 #common_name rhesus polyomavirus, SV40 DATE 30-Nov-1980 #sequence_revision 30-Nov-1980 #text_change 22-Oct-1999 ACCESSIONS C03631; C36763; A03618 REFERENCE A03631 !$#authors Reddy, V.B.; Thimmappaya, B.; Dhar, R.; Subramanian, K.N.; !1Zain, B.S.; Pan, J.; Ghosh, P.K.; Celma, M.L.; Weissman, !1S.M. !$#journal Science (1978) 200:494-502 !$#title The genome of simian virus 40. !$#cross-references MUID:78159686; PMID:205947 !$#accession C03631 !'##molecule_type DNA !'##residues 1-174 ##label RED !'##cross-references GB:J02400; GB:J02402; GB:J02403; GB:J02406; !1GB:J02407; GB:J02408; GB:J02409; GB:J02410; GB:J04139; !1GB:M24874; GB:M24914; GB:M28728; GB:V01380; NID:g965480; !1PIDN:AAB59925.1; PID:g335061 REFERENCE A36763 !$#authors Fiers, W.; Contreras, R.; Haegeman, G.; Rogiers, R.; van de !1Voorde, A.; van Heuverswyn, H.; van Herreweghe, J.; !1Volckaert, G.; Ysebaert, M. !$#journal Nature (1978) 273:113-120 !$#title Complete nucleotide sequence of SV40 DNA. !$#cross-references MUID:78156432; PMID:205802 !$#accession C36763 !'##molecule_type DNA !'##residues 1-174 ##label FIE !'##cross-references GB:V01380; NID:g62000; PIDN:CAA24673.1; PID:g62005 !'##experimental_source strain 776 COMMENT The initial 82 residues of the large T and small t antigens !1from SV40 are coded by the same nucleotide sequence. CLASSIFICATION #superfamily small T antigen; dnaJ amino-terminal homology KEYWORDS acetylated amino end; early protein FEATURE !$12-62 #domain dnaJ amino-terminal homology #status atypical !8#label DNJ\ !$1 #modified_site acetylated amino end (Met) #status !8experimental SUMMARY #length 174 #molecular-weight 20449 #checksum 2833 SEQUENCE /// ENTRY TVVPAB #type complete TITLE small T antigen - polyomavirus BK ORGANISM #formal_name Polyomavirus hominis 1 #common_name polyomavirus BK DATE 28-Feb-1981 #sequence_revision 28-Feb-1981 #text_change 22-Oct-1999 ACCESSIONS D03632; D36762; B92981; A03619 REFERENCE A03632 !$#authors Seif, I.; Khoury, G.; Dhar, R. !$#journal Cell (1979) 18:963-977 !$#title The genome of human papovavirus BKV. !$#cross-references MUID:80090082; PMID:229976 !$#accession D03632 !'##molecule_type DNA !'##residues 1-172 ##label SEI !'##cross-references GB:V01108; GB:J02038; NID:g60844; PIDN:CAA24301.1; !1PID:g60850 !'##experimental_source strain Dunlop REFERENCE A36762 !$#authors Yang, R.C.A.; Wu, R. !$#journal Science (1979) 206:456-462 !$#title BK virus DNA: complete nucleotide sequence of a human tumor !1virus. !$#cross-references MUID:80058557; PMID:228391 !$#accession D36762 !'##molecule_type DNA !'##residues 1-33,35-99,'MP' ##label YAN !'##cross-references GB:V01109; GB:J02039; NID:g60851; PIDN:CAA24303.1; !1PID:g60853 !'##experimental_source strain MM !'##note this sequence lacks residues 102-172 due to a deletion REFERENCE A92981 !$#authors Yang, R.C.A.; Young, A.; Wu, R. !$#journal J. Virol. (1980) 34:416-430 !$#title BK virus DNA sequence coding for the t and T antigens and !1evaluation of methods for determining sequence homology. !$#cross-references MUID:80185151; PMID:6246273 !$#accession B92981 !'##molecule_type DNA !'##residues 1-172 ##label YA2 !'##experimental_source strain MM CLASSIFICATION #superfamily small T antigen; dnaJ amino-terminal homology KEYWORDS early protein FEATURE !$12-62 #domain dnaJ amino-terminal homology #status atypical !8#label DNJ SUMMARY #length 172 #molecular-weight 20455 #checksum 5105 SEQUENCE /// ENTRY TVVPSS #type complete TITLE small T antigen - polyomavirus BK (strain AS) ORGANISM #formal_name Polyomavirus hominis 1 #common_name polyomavirus BK #note host Homo sapiens (man) DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jul-1999 ACCESSIONS B33278 REFERENCE A33278 !$#authors Tavis, J.E.; Walker, D.L.; Gardner, S.D.; Frisque, R.J. !$#journal J. Virol. (1989) 63:901-911 !$#title Nucleotide sequence of the human polyomavirus AS virus, an !1antigenic variant of BK virus. !$#cross-references MUID:89095020; PMID:2536111 !$#accession B33278 !'##molecule_type DNA !'##residues 1-172 ##label TAV !'##cross-references GB:M23122; NID:g332774; PIDN:AAA46883.1; !1PID:g332780 COMMENT The DNA sequence was obtained from Genbank, release 61.0. CLASSIFICATION #superfamily small T antigen; dnaJ amino-terminal homology KEYWORDS early protein; glycoprotein FEATURE !$12-62 #domain dnaJ amino-terminal homology #status atypical !8#label DNJ\ !$78 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 172 #molecular-weight 20454 #checksum 4748 SEQUENCE /// ENTRY TVVPAJ #type complete TITLE small T antigen - polyomavirus JC ORGANISM #formal_name Polyomavirus hominis 2 #common_name polyomavirus JC DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS A03620 REFERENCE A03633 !$#authors Frisque, R.J.; Bream, G.L.; Cannella, M.T. !$#journal J. Virol. (1984) 51:458-469 !$#title Human polyomavirus JC virus genome. !$#cross-references MUID:84268011; PMID:6086957 !$#accession A03620 !'##molecule_type DNA !'##residues 1-172 ##label FRI !'##cross-references GB:J02226; GB:J02227; EMBL:V01118; NID:g1083524; !1PIDN:AAA82103.1; PID:g332773 CLASSIFICATION #superfamily small T antigen; dnaJ amino-terminal homology KEYWORDS early protein FEATURE !$12-62 #domain dnaJ amino-terminal homology #status atypical !8#label DNJ SUMMARY #length 172 #molecular-weight 20237 #checksum 4528 SEQUENCE /// ENTRY TVVPBJ #type complete TITLE small T antigen - bovine polyomavirus ORGANISM #formal_name Polyomavirus bovis #common_name bovine polyomavirus, WRSV DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jun-2000 ACCESSIONS JU0358 REFERENCE JU0357 !$#authors Schuurman, R.; Sol, C.; van der Noordaa, J. !$#journal J. Gen. Virol. (1990) 71:1723-1735 !$#title The complete nucleotide sequence of bovine polyomavirus. !$#cross-references MUID:90362059; PMID:2167926 !$#accession JU0358 !'##molecule_type DNA !'##residues 1-124 ##label SCH !'##cross-references GB:D13942; GB:D00755; NID:g222302; PIDN:BAA03041.1; !1PID:g222304 CLASSIFICATION #superfamily bovine polyomavirus small T antigen; dnaJ !1amino-terminal homology KEYWORDS early protein FEATURE !$10-58 #domain dnaJ amino-terminal homology #status atypical !8#label DNJ SUMMARY #length 124 #molecular-weight 14011 #checksum 4495 SEQUENCE /// ENTRY TVVPBD #type complete TITLE small T antigen - budgerigar fledgling disease virus ORGANISM #formal_name budgerigar fledgling disease virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 12-Dec-1997 ACCESSIONS E29194 REFERENCE A29194 !$#authors Rott, O.; Kroeger, M.; Mueller, H.; Hobom, G. !$#journal Virology (1988) 165:74-86 !$#title The genome of budgerigar fledgling disease virus, an avian !1polyomavirus. !$#cross-references MUID:88265888; PMID:2838972 !$#accession E29194 !'##molecule_type DNA !'##residues 1-144 ##label ROT !'##cross-references GB:M20775 CLASSIFICATION #superfamily budgerigar fledgling disease virus small T !1antigen; dnaJ amino-terminal homology KEYWORDS early protein FEATURE !$6-54 #domain dnaJ amino-terminal homology #status atypical !8#label DNJ SUMMARY #length 144 #molecular-weight 16860 #checksum 5349 SEQUENCE /// ENTRY DNVPA4 #type complete TITLE DNA-binding protein - rhesus polyomavirus ALTERNATE_NAMES agnoprotein ORGANISM #formal_name Polyomavirus maccacae 1 #common_name rhesus polyomavirus, SV40 DATE 01-Sep-1981 #sequence_revision 01-Sep-1981 #text_change 22-Oct-1999 ACCESSIONS D03631; D36763; A03621 REFERENCE A03631 !$#authors Reddy, V.B.; Thimmappaya, B.; Dhar, R.; Subramanian, K.N.; !1Zain, B.S.; Pan, J.; Ghosh, P.K.; Celma, M.L.; Weissman, !1S.M. !$#journal Science (1978) 200:494-502 !$#title The genome of simian virus 40. !$#cross-references MUID:78159686; PMID:205947 !$#accession D03631 !'##molecule_type DNA !'##residues 1-62 ##label RED !'##cross-references GB:M99361; NID:g310670; PIDN:AAB59777.1; !1PID:g310671 REFERENCE A36763 !$#authors Fiers, W.; Contreras, R.; Haegeman, G.; Rogiers, R.; van de !1Voorde, A.; van Heuverswyn, H.; van Herreweghe, J.; !1Volckaert, G.; Ysebaert, M. !$#journal Nature (1978) 273:113-120 !$#title Complete nucleotide sequence of SV40 DNA. !$#cross-references MUID:78156432; PMID:205802 !$#accession D36763 !'##molecule_type DNA !'##residues 1-62 ##label FIE !'##cross-references GB:M99361; NID:g310670; PIDN:AAB59777.1; !1PID:g310671 !'##experimental_source strain 776 REFERENCE A93257 !$#authors Jay, G.; Nomura, S.; Anderson, C.W.; Khoury, G. !$#journal Nature (1981) 291:346-349 !$#title Identification of the SV40 agnogene product: a DNA binding !1protein. !$#cross-references MUID:81197675; PMID:6262654 !$#contents annotation; identification of the protein COMMENT This protein, encoded by the agnogene, is also called !1agnoprotein. It may have a regulatory role in nucleic !1acid-protein interactions. CLASSIFICATION #superfamily polyomavirus DNA-binding protein KEYWORDS DNA binding SUMMARY #length 62 #molecular-weight 7336 #checksum 7475 SEQUENCE /// ENTRY DNVPB #type complete TITLE DNA-binding protein - polyomavirus BK ALTERNATE_NAMES agnoprotein ORGANISM #formal_name Polyomavirus hominis 1 #common_name polyomavirus BK DATE 01-Sep-1981 #sequence_revision 01-Sep-1981 #text_change 16-Jun-2000 ACCESSIONS B03632; B36762; JQ0627; A03632 REFERENCE A03632 !$#authors Seif, I.; Khoury, G.; Dhar, R. !$#journal Cell (1979) 18:963-977 !$#title The genome of human papovavirus BKV. !$#cross-references MUID:80090082; PMID:229976 !$#accession B03632 !'##molecule_type DNA !'##residues 1-66 ##label SEI !'##cross-references GB:V01108; GB:J02038; NID:g60844; PIDN:CAA24296.1; !1PID:g60845 !'##experimental_source strain Dunlop REFERENCE A36762 !$#authors Yang, R.C.A.; Wu, R. !$#journal Science (1979) 206:456-462 !$#title BK virus DNA: complete nucleotide sequence of a human tumor !1virus. !$#cross-references MUID:80058557; PMID:228391 !$#accession B36762 !'##molecule_type DNA !'##residues 1-66 ##label YAN !'##cross-references GB:V01109; GB:J02039; NID:g60851; PIDN:CAA24304.1; !1PID:g60854 !'##experimental_source strain MM REFERENCE JQ0627 !$#authors Moens, U.; Sundsfjord, A.; Flegstad, T.; Traavik, T. !$#journal J. Gen. Virol. (1990) 71:1461-1471 !$#title BK virus early RNA transcripts in stably transformed cells: !1Enhanced levels induced by dibutyryl cAMP, forskolin and !112-0-tetradecanoylphorbol-13-acetate treatment. !$#cross-references MUID:90324932; PMID:2165132 !$#accession JQ0627 !'##molecule_type genomic RNA !'##residues 1-66 ##label MOE !'##cross-references DDBJ:D00678; NID:g222309; PIDN:BAA00584.1; !1PID:g222311 !'##experimental_source strain BKT-1B REFERENCE A93257 !$#authors Jay, G.; Nomura, S.; Anderson, C.W.; Khoury, G. !$#journal Nature (1981) 291:346-349 !$#title Identification of the SV40 agnogene product: a DNA binding !1protein. !$#cross-references MUID:81197675; PMID:6262654 !$#contents annotation; identification of the protein COMMENT This protein, encoded by the agnogene, is also called !1agnoprotein. It may have a regulatory role in nucleic !1acid-protein interactions. CLASSIFICATION #superfamily polyomavirus DNA-binding protein KEYWORDS DNA binding SUMMARY #length 66 #molecular-weight 7397 #checksum 8771 SEQUENCE /// ENTRY DNVPAS #type complete TITLE DNA-binding protein - polyomavirus BK (strain AS) ALTERNATE_NAMES agnoprotein ORGANISM #formal_name Polyomavirus hominis 1 #common_name polyomavirus BK #note host Homo sapiens (man) DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jul-1999 ACCESSIONS C33278 REFERENCE A33278 !$#authors Tavis, J.E.; Walker, D.L.; Gardner, S.D.; Frisque, R.J. !$#journal J. Virol. (1989) 63:901-911 !$#title Nucleotide sequence of the human polyomavirus AS virus, an !1antigenic variant of BK virus. !$#cross-references MUID:89095020; PMID:2536111 !$#accession C33278 !'##molecule_type DNA !'##residues 1-74 ##label TAV !'##cross-references GB:M23122; NID:g332774; PIDN:AAA46879.1; !1PID:g332776 COMMENT The DNA sequence was obtained from Genbank, release 61.0. CLASSIFICATION #superfamily polyomavirus DNA-binding protein KEYWORDS DNA binding SUMMARY #length 74 #molecular-weight 8328 #checksum 6405 SEQUENCE /// ENTRY DNVPJ #type complete TITLE DNA-binding protein - polyomavirus JC ALTERNATE_NAMES agnoprotein ORGANISM #formal_name Polyomavirus hominis 2 #common_name polyomavirus JC DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS A03623 REFERENCE A03633 !$#authors Frisque, R.J.; Bream, G.L.; Cannella, M.T. !$#journal J. Virol. (1984) 51:458-469 !$#title Human polyomavirus JC virus genome. !$#cross-references MUID:84268011; PMID:6086957 !$#accession A03623 !'##molecule_type DNA !'##residues 1-71 ##label FRI !'##cross-references GB:J02226; GB:J02227; EMBL:V01118; NID:g1083524; !1PIDN:AAA82098.1; PID:g332769 COMMENT This protein, encoded by the agnogene, may have a regulatory !1role in nucleic acid-protein interactions. CLASSIFICATION #superfamily polyomavirus DNA-binding protein KEYWORDS DNA binding SUMMARY #length 71 #molecular-weight 8081 #checksum 3350 SEQUENCE /// ENTRY DNVPBP #type complete TITLE DNA-binding protein - bovine polyomavirus ALTERNATE_NAMES agnoprotein ORGANISM #formal_name Polyomavirus bovis #common_name bovine polyomavirus, WRSV DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jun-2000 ACCESSIONS JU0361 REFERENCE JU0357 !$#authors Schuurman, R.; Sol, C.; van der Noordaa, J. !$#journal J. Gen. Virol. (1990) 71:1723-1735 !$#title The complete nucleotide sequence of bovine polyomavirus. !$#cross-references MUID:90362059; PMID:2167926 !$#accession JU0361 !'##molecule_type DNA !'##residues 1-118 ##label SCH !'##cross-references GB:D13942; GB:D00755; GB:M74843; NID:g222302; !1PIDN:BAA03036.1; PID:g222305 CLASSIFICATION #superfamily bovine polyomavirus DNA-binding protein KEYWORDS DNA binding SUMMARY #length 118 #molecular-weight 13138 #checksum 3850 SEQUENCE /// ENTRY DNVPBF #type complete TITLE DNA-binding protein - budgerigar fledgling disease virus ALTERNATE_NAMES agnoprotein ORGANISM #formal_name budgerigar fledgling disease virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS A29194 REFERENCE A29194 !$#authors Rott, O.; Kroeger, M.; Mueller, H.; Hobom, G. !$#journal Virology (1988) 165:74-86 !$#title The genome of budgerigar fledgling disease virus, an avian !1polyomavirus. !$#cross-references MUID:88265888; PMID:2838972 !$#accession A29194 !'##molecule_type DNA !'##residues 1-61 ##label ROT !'##cross-references GB:M20775; NID:g499657; PIDN:AAB59756.1; !1PID:g332793 CLASSIFICATION #superfamily budgerigar fledgling disease virus DNA-binding !1protein KEYWORDS DNA binding SUMMARY #length 61 #molecular-weight 6845 #checksum 9713 SEQUENCE /// ENTRY VVVP14 #type complete TITLE coat protein VP1 - rhesus polyomavirus ORGANISM #formal_name Polyomavirus maccacae 1 #common_name rhesus polyomavirus, SV40 DATE 30-Nov-1980 #sequence_revision 14-Nov-1983 #text_change 22-Oct-1999 ACCESSIONS E03631; E36763; A03624 REFERENCE A03631 !$#authors Reddy, V.B.; Thimmappaya, B.; Dhar, R.; Subramanian, K.N.; !1Zain, B.S.; Pan, J.; Ghosh, P.K.; Celma, M.L.; Weissman, !1S.M. !$#journal Science (1978) 200:494-502 !$#title The genome of simian virus 40. !$#cross-references MUID:78159686; PMID:205947 !$#accession E03631 !'##molecule_type DNA !'##residues 1-364 ##label RED REFERENCE A36763 !$#authors Fiers, W.; Contreras, R.; Haegeman, G.; Rogiers, R.; van de !1Voorde, A.; van Heuverswyn, H.; van Herreweghe, J.; !1Volckaert, G.; Ysebaert, M. !$#journal Nature (1978) 273:113-120 !$#title Complete nucleotide sequence of SV40 DNA. !$#cross-references MUID:78156432; PMID:205802 !$#accession E36763 !'##molecule_type DNA !'##residues 1-100,'L',102-364 ##label FIE !'##cross-references GB:V01380; NID:g62000; PIDN:CAA24671.1; PID:g62003 !'##experimental_source strain 776 REFERENCE A31426 !$#authors Babe, L.M.; Brew, K.; Matsuura, S.E.; Scott, W.A. !$#journal J. Biol. Chem. (1989) 264:2665-2671 !$#title Epitopes on the major capsid protein of simian virus 40. !$#cross-references MUID:89123359; PMID:2464591 !$#contents annotation; determination of immunoreactive domain; !1phosphorylation site CLASSIFICATION #superfamily polyomavirus coat protein VP1 KEYWORDS coat protein; phosphoprotein FEATURE !$340 #binding_site phosphate (Thr) (covalent) #status !8experimental SUMMARY #length 364 #molecular-weight 40165 #checksum 826 SEQUENCE /// ENTRY VVVP1B #type complete TITLE coat protein VP1 - polyomavirus BK ORGANISM #formal_name Polyomavirus hominis 1 #common_name polyomavirus BK DATE 28-Feb-1981 #sequence_revision 08-Oct-1981 #text_change 28-May-1999 ACCESSIONS E03632; E36762; A03625 REFERENCE A03632 !$#authors Seif, I.; Khoury, G.; Dhar, R. !$#journal Cell (1979) 18:963-977 !$#title The genome of human papovavirus BKV. !$#cross-references MUID:80090082; PMID:229976 !$#accession E03632 !'##molecule_type DNA !'##residues 1-362 ##label SEI !'##experimental_source strain Dunlop REFERENCE A36762 !$#authors Yang, R.C.A.; Wu, R. !$#journal Science (1979) 206:456-462 !$#title BK virus DNA: complete nucleotide sequence of a human tumor !1virus. !$#cross-references MUID:80058557; PMID:228391 !$#accession E36762 !'##molecule_type DNA !'##residues 1-218,'T',220-300,'L',302-362 ##label YAN !'##cross-references GB:V01109; GB:J02039; NID:g60851; PIDN:CAA24307.1; !1PID:g313799 !'##experimental_source strain MM CLASSIFICATION #superfamily polyomavirus coat protein VP1 KEYWORDS coat protein; glycoprotein FEATURE !$273 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 362 #molecular-weight 40108 #checksum 4857 SEQUENCE /// ENTRY VVVP1S #type complete TITLE coat protein VP1 - polyomavirus BK (strain AS) ORGANISM #formal_name Polyomavirus hominis 1 #common_name polyomavirus BK #note host Homo sapiens (man) DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jul-1999 ACCESSIONS D33278 REFERENCE A33278 !$#authors Tavis, J.E.; Walker, D.L.; Gardner, S.D.; Frisque, R.J. !$#journal J. Virol. (1989) 63:901-911 !$#title Nucleotide sequence of the human polyomavirus AS virus, an !1antigenic variant of BK virus. !$#cross-references MUID:89095020; PMID:2536111 !$#accession D33278 !'##molecule_type DNA !'##residues 1-362 ##label TAV !'##cross-references GB:M23122; NID:g332774; PIDN:AAA46882.1; !1PID:g332779 COMMENT The DNA sequence was obtained from Genbank, release 61.0. CLASSIFICATION #superfamily polyomavirus coat protein VP1 KEYWORDS coat protein; glycoprotein; late protein FEATURE !$273 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 362 #molecular-weight 40112 #checksum 6707 SEQUENCE /// ENTRY VVVP1J #type complete TITLE coat protein VP1 - polyomavirus JC ORGANISM #formal_name Polyomavirus hominis 2 #common_name polyomavirus JC DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS A03626 REFERENCE A03633 !$#authors Frisque, R.J.; Bream, G.L.; Cannella, M.T. !$#journal J. Virol. (1984) 51:458-469 !$#title Human polyomavirus JC virus genome. !$#cross-references MUID:84268011; PMID:6086957 !$#accession A03626 !'##molecule_type DNA !'##residues 1-354 ##label FRI !'##cross-references GB:J02226; GB:J02227; EMBL:V01118; NID:g1083524; !1PIDN:AAA82101.1; PID:g332772 CLASSIFICATION #superfamily polyomavirus coat protein VP1 KEYWORDS coat protein SUMMARY #length 354 #molecular-weight 39609 #checksum 7952 SEQUENCE /// ENTRY VVVP1L #type complete TITLE coat protein VP1 - lymphotropic polyomavirus ORGANISM #formal_name Polyomavirus cercopitheci #common_name lymphotropic polyomavirus #note host (African green monkey) DATE 13-Aug-1986 #sequence_revision 13-Aug-1986 #text_change 24-Feb-1994 ACCESSIONS A03627 REFERENCE A03634 !$#authors Pawlita, M.; Clad, A.; zur Hausen, H. !$#journal Virology (1985) 143:196-211 !$#title Complete DNA sequence of lymphotropic papovavirus: prototype !1of a new species of the polyomavirus genus. !$#cross-references MUID:86045879; PMID:2998001 !$#accession A03627 !'##molecule_type DNA !'##residues 1-368 ##label PAW !'##note the authors translated the codon GCT for residue 168 as His CLASSIFICATION #superfamily polyomavirus coat protein VP1 KEYWORDS coat protein; late protein SUMMARY #length 368 #molecular-weight 40022 #checksum 9733 SEQUENCE /// ENTRY VVVP1 #type complete TITLE coat protein VP1 - mouse polyomavirus (strain A2) ORGANISM #formal_name Polyomavirus muris #common_name mouse polyomavirus DATE 31-Jul-1980 #sequence_revision 08-Oct-1981 #text_change 16-Jul-1999 ACCESSIONS A03628 REFERENCE A03635 !$#authors Soeda, E.; Arrand, J.R.; Smolar, N.; Walsh, J.E.; Griffin, !1B.E. !$#journal Nature (1980) 283:445-453 !$#title Coding potential and regulatory signals of the polyoma virus !1genome. !$#cross-references MUID:80099647; PMID:6243401 !$#accession A03628 !'##molecule_type DNA !'##residues 1-383 ##label SOE !'##cross-references GB:J02288; GB:J02290; GB:J02291; GB:J02292; !1GB:K00932; GB:K00997; GB:K01041; GB:K01071; GB:K01072; !1GB:V01117; GB:V01147; NID:g332752; PIDN:AAB59902.1; !1PID:g332756 CLASSIFICATION #superfamily polyomavirus coat protein VP1 KEYWORDS coat protein SUMMARY #length 383 #molecular-weight 42452 #checksum 9242 SEQUENCE /// ENTRY VVVP13 #type complete TITLE coat protein VP1 - mouse polyomavirus (strain 3) ORGANISM #formal_name Polyomavirus muris #common_name mouse polyomavirus DATE 28-Feb-1981 #sequence_revision 08-Oct-1981 #text_change 16-Jul-1999 ACCESSIONS A03629 REFERENCE A36761 !$#authors Friedmann, T.; Esty, A.; LaPorte, P.; Deininger, P. !$#journal Cell (1979) 17:715-724 !$#title The nucleotide sequence and genome organization of the !1polyoma early region: extensive nucleotide and amino acid !1homology with SV40. !$#cross-references MUID:80001963; PMID:225042 !$#accession A03629 !'##molecule_type DNA !'##residues 1-384 ##label FRI !'##cross-references GB:J02289; GB:V01151; NID:g332759; PIDN:AAA46875.1; !1PID:g332763 CLASSIFICATION #superfamily polyomavirus coat protein VP1 KEYWORDS coat protein SUMMARY #length 384 #molecular-weight 42589 #checksum 6019 SEQUENCE /// ENTRY VVVPC1 #type complete TITLE coat protein VP1 - mouse polyomavirus (strain Crawford small-plaque) ORGANISM #formal_name Polyomavirus muris #common_name mouse polyomavirus DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 14-Nov-1997 ACCESSIONS D28838; C94520 REFERENCE A28838 !$#authors Rothwell, V.M.; Folk, W.R. !$#journal J. Virol. (1983) 48:472-480 !$#title Comparison of the DNA sequence of the Crawford small-plaque !1variant of polyomavirus with those of polyomaviruses A2 and !1strain 3. !$#cross-references MUID:84011043; PMID:6312103 !$#accession D28838 !'##molecule_type DNA !'##residues 1-384 ##label RO1 !'##cross-references GB:K02737; NID:g332788 !'##note this ORF is not annotated in GenBank entry PLYCSP REFERENCE A94520 !$#authors Rothwell, V.M. !$#submission submitted to GenBank, November 1985 !$#accession C94520 !'##molecule_type DNA !'##residues 1-384 ##label RO2 CLASSIFICATION #superfamily polyomavirus coat protein VP1 KEYWORDS coat protein; late protein SUMMARY #length 384 #molecular-weight 42461 #checksum 5507 SEQUENCE /// ENTRY VVVPK1 #type complete TITLE coat protein VP1 - mouse polyomavirus (strain Kilham) ORGANISM #formal_name Polyomavirus muris #common_name mouse polyomavirus DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 15-Nov-1996 ACCESSIONS C37945 REFERENCE A37945 !$#authors Mayer, M.; Doerries, K. !$#journal Virology (1991) 181:469-480 !$#title Nucleotide sequence and genome organization of the murine !1polyomavirus, Kilham strain. !$#cross-references MUID:91196237; PMID:1849675 !$#accession C37945 !'##molecule_type DNA !'##residues 1-372 ##label MAY !'##cross-references GB:M55904 CLASSIFICATION #superfamily polyomavirus coat protein VP1 KEYWORDS coat protein; late protein SUMMARY #length 372 #molecular-weight 41531 #checksum 6583 SEQUENCE /// ENTRY VVVPB1 #type complete TITLE coat protein VP1 - bovine polyomavirus ORGANISM #formal_name Polyomavirus bovis #common_name bovine polyomavirus, WRSV DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jun-2000 ACCESSIONS JU0359 REFERENCE JU0357 !$#authors Schuurman, R.; Sol, C.; van der Noordaa, J. !$#journal J. Gen. Virol. (1990) 71:1723-1735 !$#title The complete nucleotide sequence of bovine polyomavirus. !$#cross-references MUID:90362059; PMID:2167926 !$#accession JU0359 !'##molecule_type DNA !'##residues 1-365 ##label SCH !'##cross-references GB:D13942; GB:D00755; GB:M74843; NID:g222302; !1PIDN:BAA03039.1; PID:g222308 CLASSIFICATION #superfamily polyomavirus coat protein VP1 KEYWORDS coat protein; late protein SUMMARY #length 365 #molecular-weight 40514 #checksum 259 SEQUENCE /// ENTRY VVVP1H #type complete TITLE coat protein VP1 - hamster polyomavirus ORGANISM #formal_name hamster polyomavirus DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 16-Jul-1999 ACCESSIONS A03630 REFERENCE A03636 !$#authors Delmas, V.; Bastien, C.; Scherneck, S.; Feunteun, J. !$#journal EMBO J. (1985) 4:1279-1286 !$#title A new member of the polyomavirus family: the hamster !1papovavirus. Complete nucleotide sequence and transformation !1properties. !$#cross-references MUID:85230582; PMID:2988942 !$#accession A03630 !'##molecule_type DNA !'##residues 1-372 ##label DEL !'##cross-references GB:M26281; NID:g825486; PIDN:AAA67119.1; !1PID:g825490 CLASSIFICATION #superfamily polyomavirus coat protein VP1 KEYWORDS coat protein; late protein SUMMARY #length 372 #molecular-weight 40815 #checksum 8718 SEQUENCE /// ENTRY VVVPBD #type complete TITLE coat protein VP1 - budgerigar fledgling disease virus ORGANISM #formal_name budgerigar fledgling disease virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS C29194 REFERENCE A29194 !$#authors Rott, O.; Kroeger, M.; Mueller, H.; Hobom, G. !$#journal Virology (1988) 165:74-86 !$#title The genome of budgerigar fledgling disease virus, an avian !1polyomavirus. !$#cross-references MUID:88265888; PMID:2838972 !$#accession C29194 !'##molecule_type DNA !'##residues 1-343 ##label ROT !'##cross-references GB:M20775; NID:g499657; PIDN:AAB59759.1; !1PID:g332796 CLASSIFICATION #superfamily polyomavirus coat protein VP1 KEYWORDS coat protein; late protein SUMMARY #length 343 #molecular-weight 37413 #checksum 3286 SEQUENCE /// ENTRY VVVP24 #type complete TITLE coat protein VP2 - rhesus polyomavirus CONTAINS coat protein VP3 ORGANISM #formal_name Polyomavirus maccacae 1 #common_name rhesus polyomavirus, SV40 DATE 30-Nov-1980 #sequence_revision 08-Oct-1981 #text_change 22-Oct-1999 ACCESSIONS A03631; A36763 REFERENCE A03631 !$#authors Reddy, V.B.; Thimmappaya, B.; Dhar, R.; Subramanian, K.N.; !1Zain, B.S.; Pan, J.; Ghosh, P.K.; Celma, M.L.; Weissman, !1S.M. !$#journal Science (1978) 200:494-502 !$#title The genome of simian virus 40. !$#cross-references MUID:78159686; PMID:205947 !$#accession A03631 !'##molecule_type DNA !'##residues 1-352 ##label RED REFERENCE A36763 !$#authors Fiers, W.; Contreras, R.; Haegeman, G.; Rogiers, R.; van de !1Voorde, A.; van Heuverswyn, H.; van Herreweghe, J.; !1Volckaert, G.; Ysebaert, M. !$#journal Nature (1978) 273:113-120 !$#title Complete nucleotide sequence of SV40 DNA. !$#cross-references MUID:78156432; PMID:205802 !$#accession A36763 !'##molecule_type DNA !'##residues 1-62,'T',64-352 ##label FIE !'##cross-references GB:V01380; NID:g62000; PIDN:CAA24669.1; PID:g62001 !'##experimental_source strain 776 CLASSIFICATION #superfamily polyomavirus coat protein VP2 KEYWORDS late protein FEATURE !$119-352 #product coat protein VP3 #status predicted #label !8VP3 SUMMARY #length 352 #molecular-weight 38539 #checksum 5747 SEQUENCE /// ENTRY VVVP2B #type complete TITLE coat protein VP2 - polyomavirus BK CONTAINS coat protein VP3 ORGANISM #formal_name Polyomavirus hominis 1 #common_name polyomavirus BK DATE 28-Feb-1981 #sequence_revision 08-Oct-1981 #text_change 28-May-1999 ACCESSIONS A03632; A36762 REFERENCE A03632 !$#authors Seif, I.; Khoury, G.; Dhar, R. !$#journal Cell (1979) 18:963-977 !$#title The genome of human papovavirus BKV. !$#cross-references MUID:80090082; PMID:229976 !$#accession A03632 !'##molecule_type DNA !'##residues 1-351 ##label SEI !'##experimental_source strain Dunlop REFERENCE A36762 !$#authors Yang, R.C.A.; Wu, R. !$#journal Science (1979) 206:456-462 !$#title BK virus DNA: complete nucleotide sequence of a human tumor !1virus. !$#cross-references MUID:80058557; PMID:228391 !$#accession A36762 !'##molecule_type DNA !'##residues 1-311,'C',313-351 ##label YAN !'##cross-references GB:V01109; GB:J02039; NID:g60851; PIDN:CAA24305.1; !1PID:g60855 !'##experimental_source strain MM CLASSIFICATION #superfamily polyomavirus coat protein VP2 KEYWORDS late protein FEATURE !$120-351 #product coat protein VP3 #status predicted #label !8VP3 SUMMARY #length 351 #molecular-weight 38347 #checksum 2233 SEQUENCE /// ENTRY VVVPAS #type complete TITLE coat protein VP2 - polyomavirus BK (strain AS) CONTAINS coat protein VP3 ORGANISM #formal_name Polyomavirus hominis 1 #common_name polyomavirus BK DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jul-1999 ACCESSIONS E33278 REFERENCE A33278 !$#authors Tavis, J.E.; Walker, D.L.; Gardner, S.D.; Frisque, R.J. !$#journal J. Virol. (1989) 63:901-911 !$#title Nucleotide sequence of the human polyomavirus AS virus, an !1antigenic variant of BK virus. !$#cross-references MUID:89095020; PMID:2536111 !$#accession E33278 !'##molecule_type DNA !'##residues 1-351 ##label TAV !'##cross-references GB:M23122; NID:g332774; PIDN:AAA46880.1; !1PID:g332777 CLASSIFICATION #superfamily polyomavirus coat protein VP2 KEYWORDS glycoprotein; late protein FEATURE !$120-351 #product coat protein VP3 #status predicted #label !8VP3\ !$221 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 351 #molecular-weight 38303 #checksum 1628 SEQUENCE /// ENTRY VVVP2J #type complete TITLE coat protein VP2 - polyomavirus JC CONTAINS coat protein VP3 ORGANISM #formal_name Polyomavirus hominis 2 #common_name polyomavirus JC DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS A03633 REFERENCE A03633 !$#authors Frisque, R.J.; Bream, G.L.; Cannella, M.T. !$#journal J. Virol. (1984) 51:458-469 !$#title Human polyomavirus JC virus genome. !$#cross-references MUID:84268011; PMID:6086957 !$#accession A03633 !'##molecule_type DNA !'##residues 1-344 ##label FRI !'##cross-references GB:J02226; GB:J02227; EMBL:V01118; NID:g1083524; !1PIDN:AAA82099.1; PID:g332770 CLASSIFICATION #superfamily polyomavirus coat protein VP2 KEYWORDS late protein FEATURE !$120-344 #product coat protein VP3 #status predicted #label !8VP3 SUMMARY #length 344 #molecular-weight 37368 #checksum 2410 SEQUENCE /// ENTRY VVVP2L #type complete TITLE coat protein VP2 - lymphotropic polyomavirus CONTAINS coat protein VP3 ORGANISM #formal_name Polyomavirus cercopitheci #common_name lymphotropic polyomavirus #note host (African green monkey) DATE 13-Aug-1986 #sequence_revision 13-Aug-1986 #text_change 12-Apr-1996 ACCESSIONS A03634 REFERENCE A03634 !$#authors Pawlita, M.; Clad, A.; zur Hausen, H. !$#journal Virology (1985) 143:196-211 !$#title Complete DNA sequence of lymphotropic papovavirus: prototype !1of a new species of the polyomavirus genus. !$#cross-references MUID:86045879; PMID:2998001 !$#accession A03634 !'##molecule_type DNA !'##residues 1-356 ##label PAW CLASSIFICATION #superfamily polyomavirus coat protein VP2 KEYWORDS late protein FEATURE !$120-356 #product coat protein VP3 #status predicted #label !8VP3 SUMMARY #length 356 #molecular-weight 39535 #checksum 9232 SEQUENCE /// ENTRY VVVP2 #type complete TITLE coat protein VP2 - mouse polyomavirus CONTAINS coat protein VP3 ORGANISM #formal_name Polyomavirus muris #common_name mouse polyomavirus DATE 31-Jul-1980 #sequence_revision 08-Oct-1981 #text_change 16-Jul-1999 ACCESSIONS A03635; A36761 REFERENCE A03635 !$#authors Soeda, E.; Arrand, J.R.; Smolar, N.; Walsh, J.E.; Griffin, !1B.E. !$#journal Nature (1980) 283:445-453 !$#title Coding potential and regulatory signals of the polyoma virus !1genome. !$#cross-references MUID:80099647; PMID:6243401 !$#accession A03635 !'##molecule_type DNA !'##residues 1-319 ##label SOE !'##cross-references GB:J02288; GB:J02290; GB:J02291; GB:J02292; !1GB:K00932; GB:K00997; GB:K01041; GB:K01071; GB:K01072; !1GB:V01117; GB:V01147; NID:g332752; PIDN:AAB59904.1; !1PID:g332758 !'##experimental_source strain A2 REFERENCE A36761 !$#authors Friedmann, T.; Esty, A.; LaPorte, P.; Deininger, P. !$#journal Cell (1979) 17:715-724 !$#title The nucleotide sequence and genome organization of the !1polyoma early region: extensive nucleotide and amino acid !1homology with SV40. !$#cross-references MUID:80001963; PMID:225042 !$#accession A36761 !'##molecule_type DNA !'##residues 1-77,'N',79-218,'V',220-275,'PGGA',280-319 ##label FRI !'##cross-references GB:J02289; GB:V01151; NID:g332759; PIDN:AAA46877.1; !1PID:g332765 !'##experimental_source strain 3 CLASSIFICATION #superfamily polyomavirus coat protein VP2 KEYWORDS late protein FEATURE !$116-319 #product coat protein VP3 #status predicted #label !8VP3 SUMMARY #length 319 #molecular-weight 34800 #checksum 2886 SEQUENCE /// ENTRY VVVPC2 #type complete TITLE coat protein VP2 - mouse polyomavirus (strain Crawford small-plaque) CONTAINS coat protein VP3 ORGANISM #formal_name Polyomavirus muris #common_name mouse polyomavirus DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 14-Nov-1997 ACCESSIONS E28838 REFERENCE A28838 !$#authors Rothwell, V.M.; Folk, W.R. !$#journal J. Virol. (1983) 48:472-480 !$#title Comparison of the DNA sequence of the Crawford small-plaque !1variant of polyomavirus with those of polyomaviruses A2 and !1strain 3. !$#cross-references MUID:84011043; PMID:6312103 !$#accession E28838 !'##molecule_type DNA !'##residues 1-319 ##label ROT !'##cross-references GB:K02737; NID:g332788 !'##note this ORF is not annotated in GenBank entry PLYCSP CLASSIFICATION #superfamily polyomavirus coat protein VP2 KEYWORDS late protein FEATURE !$116-319 #product coat protein VP3 #status predicted #label !8VP3 SUMMARY #length 319 #molecular-weight 34827 #checksum 2781 SEQUENCE /// ENTRY VVVPK2 #type complete TITLE coat protein VP2 - mouse polyomavirus (strain Kilham) CONTAINS coat protein VP3 ORGANISM #formal_name Polyomavirus muris #common_name mouse polyomavirus DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 24-Feb-1994 ACCESSIONS D37945 REFERENCE A37945 !$#authors Mayer, M.; Doerries, K. !$#journal Virology (1991) 181:469-480 !$#title Nucleotide sequence and genome organization of the murine !1polyomavirus, Kilham strain. !$#cross-references MUID:91196237; PMID:1849675 !$#accession D37945 !'##molecule_type DNA !'##residues 1-341 ##label MAY !'##cross-references GB:M55904 CLASSIFICATION #superfamily polyomavirus coat protein VP2 KEYWORDS late protein FEATURE !$120-341 #product coat protein VP3 #status predicted #label !8VP3 SUMMARY #length 341 #molecular-weight 37311 #checksum 6793 SEQUENCE /// ENTRY VVVPB2 #type complete TITLE coat protein VP2 - bovine polyomavirus CONTAINS coat protein VP3 ORGANISM #formal_name Polyomavirus bovis #common_name bovine polyomavirus, WRSV DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jun-2000 ACCESSIONS JU0360 REFERENCE JU0357 !$#authors Schuurman, R.; Sol, C.; van der Noordaa, J. !$#journal J. Gen. Virol. (1990) 71:1723-1735 !$#title The complete nucleotide sequence of bovine polyomavirus. !$#cross-references MUID:90362059; PMID:2167926 !$#accession JU0360 !'##molecule_type DNA !'##residues 1-353 ##label SCH !'##cross-references GB:D13942; GB:D00755; GB:M74843; NID:g222302; !1PIDN:BAA03037.1; PID:g222306 CLASSIFICATION #superfamily polyomavirus coat protein VP2 KEYWORDS late protein FEATURE !$122-353 #product coat protein VP3 #status predicted #label !8VP3 SUMMARY #length 353 #molecular-weight 39146 #checksum 3910 SEQUENCE /// ENTRY VVVP2H #type complete TITLE coat protein VP2 - hamster polyomavirus CONTAINS coat protein VP3 ORGANISM #formal_name hamster polyomavirus DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 16-Jul-1999 ACCESSIONS A03636 REFERENCE A03636 !$#authors Delmas, V.; Bastien, C.; Scherneck, S.; Feunteun, J. !$#journal EMBO J. (1985) 4:1279-1286 !$#title A new member of the polyomavirus family: the hamster !1papovavirus. Complete nucleotide sequence and transformation !1properties. !$#cross-references MUID:85230582; PMID:2988942 !$#accession A03636 !'##molecule_type DNA !'##residues 1-345 ##label DEL !'##cross-references GB:M26281; NID:g825486; PIDN:AAA67121.1; !1PID:g825492 CLASSIFICATION #superfamily polyomavirus coat protein VP2 KEYWORDS late protein FEATURE !$125-345 #product coat protein VP3 #status predicted #label !8VP3 SUMMARY #length 345 #molecular-weight 38608 #checksum 1888 SEQUENCE /// ENTRY VVVPBF #type complete TITLE coat protein VP2 - budgerigar fledgling disease virus CONTAINS coat protein VP3 ORGANISM #formal_name budgerigar fledgling disease virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS B29194 REFERENCE A29194 !$#authors Rott, O.; Kroeger, M.; Mueller, H.; Hobom, G. !$#journal Virology (1988) 165:74-86 !$#title The genome of budgerigar fledgling disease virus, an avian !1polyomavirus. !$#cross-references MUID:88265888; PMID:2838972 !$#accession B29194 !'##molecule_type DNA !'##residues 1-341 ##label ROT !'##cross-references GB:M20775; NID:g499657; PIDN:AAB59757.1; !1PID:g332794 CLASSIFICATION #superfamily polyomavirus coat protein VP2 KEYWORDS late protein FEATURE !$107-341 #product coat protein VP3 #status predicted #label !8VP3 SUMMARY #length 341 #molecular-weight 37358 #checksum 4199 SEQUENCE /// ENTRY P1WL #type complete TITLE L1 protein - human papillomavirus type 1a ORGANISM #formal_name human papillomavirus type 1a DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 24-Feb-1994 ACCESSIONS A03637 REFERENCE A90970 !$#authors Danos, O.; Katinka, M.; Yaniv, M. !$#journal EMBO J. (1982) 1:231-236 !$#title Human papillomavirus 1a complete DNA sequence: a novel type !1of genome organization among papovaviridae. !$#cross-references MUID:84182467; PMID:6325156 !$#accession A03637 !'##molecule_type DNA !'##residues 1-508 ##label DAN CLASSIFICATION #superfamily papillomavirus L1 protein KEYWORDS late protein SUMMARY #length 508 #molecular-weight 57703 #checksum 9905 SEQUENCE /// ENTRY P1WL6 #type complete TITLE L1 protein - human papillomavirus type 6b ORGANISM #formal_name human papillomavirus type 6b DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 16-Jul-1999 ACCESSIONS A03638 REFERENCE A90975 !$#authors Schwarz, E.; Durst, M.; Demankowski, C.; Lattermann, O.; !1Zech, R.; Wolfsperger, E.; Suhai, S.; zur Hausen, H. !$#journal EMBO J. (1983) 2:2341-2348 !$#title DNA sequence and genome organization of genital human !1papillomavirus type 6b. !$#cross-references MUID:84131949; PMID:6321162 !$#accession A03638 !'##molecule_type DNA !'##residues 1-500 ##label SCH !'##cross-references GB:X00203; NID:g60955; PIDN:CAA25026.1; PID:g60964 CLASSIFICATION #superfamily papillomavirus L1 protein KEYWORDS late protein SUMMARY #length 500 #molecular-weight 55597 #checksum 3043 SEQUENCE /// ENTRY P1WL11 #type complete TITLE L1 protein - human papillomavirus type 11 ORGANISM #formal_name human papillomavirus type 11 DATE 13-Aug-1986 #sequence_revision 13-Aug-1986 #text_change 16-Jul-1999 ACCESSIONS A03639 REFERENCE A94338 !$#authors Dartmann, K.; Schwarz, E.; Gissmann, L.; zur Hausen, H. !$#journal Virology (1986) 151:124-130 !$#title The nucleotide sequence and genome organization of human !1papilloma virus type 11. !$#cross-references MUID:86181601; PMID:3008427 !$#accession A03639 !'##molecule_type DNA !'##residues 1-501 ##label DAR !'##cross-references GB:M14119; NID:g333026; PIDN:AAA46935.1; !1PID:g496201 CLASSIFICATION #superfamily papillomavirus L1 protein KEYWORDS late protein SUMMARY #length 501 #molecular-weight 55835 #checksum 9806 SEQUENCE /// ENTRY P1WL13 #type complete TITLE L1 protein - human papillomavirus type 13 ORGANISM #formal_name human papillomavirus type 13 #note host Homo sapiens (man) DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS H42955; A44889 REFERENCE A42955 !$#authors van Ranst, M.; Fuse, A.; Fiten, P.; Beuken, E.; Pfister, H.; !1Burk, R.D.; Opdenakker, G. !$#journal Virology (1992) 190:587-596 !$#title Human papillomavirus type 13 and pygmy chimpanzee !1papillomavirus type 1: Comparison of the genome !1organizations. !$#cross-references MUID:92391075; PMID:1325697 !$#accession H42955 !'##molecule_type DNA !'##residues 1-499 ##label VAN !'##cross-references EMBL:X62843; NID:g60295; PIDN:CAA44654.1; !1PID:g60303 REFERENCE A44889 !$#authors van den Brule, A.J.; Snijders, P.J.; Raaphorst, P.M.; !1Schrijnemakers, H.F.; Delius, H.; Gissmann, L.; Meijer, !1C.J.; Walboomers, J.M. !$#journal J. Clin. Microbiol. (1992) 30:1716-1721 !$#title General primer polymerase chain reaction in combination with !1sequence analysis for identification of potentially novel !1human papillomavirus genotypes in cervical lesions. !$#cross-references MUID:92332706; PMID:1321168 !$#accession A44889 !'##molecule_type DNA !'##residues 331-364 ##label VA2 !'##cross-references GB:S40235; NID:g251682; PIDN:AAB22562.1; !1PID:g251683 !'##experimental_source mucosotropic type 13, cervical smear !'##note sequence extracted from NCBI backbone (NCBIN:109389, !1NCBIP:109410) CLASSIFICATION #superfamily papillomavirus L1 protein KEYWORDS late protein SUMMARY #length 499 #molecular-weight 55773 #checksum 375 SEQUENCE /// ENTRY P1WLC1 #type complete TITLE L1 protein - pygmy chimpanzee papillomavirus (type 1) ORGANISM #formal_name pygmy chimpanzee papillomavirus DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS H36818 REFERENCE A42955 !$#authors van Ranst, M.; Fuse, A.; Fiten, P.; Beuken, E.; Pfister, H.; !1Burk, R.D.; Opdenakker, G. !$#journal Virology (1992) 190:587-596 !$#title Human papillomavirus type 13 and pygmy chimpanzee !1papillomavirus type 1: Comparison of the genome !1organizations. !$#cross-references MUID:92391075; PMID:1325697 !$#accession H36818 !'##molecule_type DNA !'##residues 1-502 ##label VAN !'##cross-references EMBL:X62844; NID:g61010; PIDN:CAA44662.1; !1PID:g61018 CLASSIFICATION #superfamily papillomavirus L1 protein KEYWORDS late protein SUMMARY #length 502 #molecular-weight 55718 #checksum 1945 SEQUENCE /// ENTRY P1WL41 #type complete TITLE L1 protein - human papillomavirus type 41 ORGANISM #formal_name human papillomavirus type 41 #note host Homo sapiens (man) DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 27-Jan-1995 ACCESSIONS H43550 REFERENCE A43550 !$#authors Hirt, L.; Hirsch-Behnam, A.; De Villiers, E.M. !$#journal Virus Res. (1990) 18:179-190 !$#title Nucleotide sequence of human papillomavirus (HPV) type 41: !1an unusual HPV type without a typical E2 binding site !1consensus sequence. !$#accession H43550 !'##status translation not shown !'##molecule_type DNA !'##residues 1-534 ##label HIR !'##cross-references EMBL:X56147 CLASSIFICATION #superfamily papillomavirus L1 protein KEYWORDS late protein SUMMARY #length 534 #molecular-weight 60949 #checksum 9283 SEQUENCE /// ENTRY P1WL42 #type complete TITLE L1 protein - human papillomavirus type 42 ORGANISM #formal_name human papillomavirus type 42 #note host Homo sapiens (man) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 27-Jan-1995 ACCESSIONS G39451 REFERENCE A39451 !$#authors Philipp, W.; Honore, N.; Sapp, M.; Cole, S.T.; Streeck, R.E. !$#journal Virology (1992) 186:331-334 !$#title Human papillomavirus type 42: new sequence, conserved genome !1organization. !$#cross-references MUID:92087479; PMID:1309278 !$#accession G39451 !'##status translation not shown !'##molecule_type DNA !'##residues 1-502 ##label PHI !'##cross-references GB:M73236 CLASSIFICATION #superfamily papillomavirus L1 protein KEYWORDS late protein SUMMARY #length 502 #molecular-weight 56165 #checksum 3403 SEQUENCE /// ENTRY P1WLHS #type complete TITLE major capsid protein L1 - human papillomavirus type 16 ORGANISM #formal_name human papillomavirus type 16 DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 20-Aug-1999 ACCESSIONS A03640; F44906; T10431 REFERENCE A22355 !$#authors Seedorf, K.; Krammer, G.; Durst, M.; Suhai, S.; Rowekamp, !1W.G. !$#journal Virology (1985) 145:181-185 !$#title Human papillomavirus type 16 DNA sequence. !$#cross-references MUID:85246220; PMID:2990099 !$#accession A03640 !'##molecule_type DNA !'##residues 1-531 ##label SEE !'##cross-references GB:K02718; NID:g333031; PIDN:AAA46943.1; !1PID:g333037 REFERENCE A44889 !$#authors van den Brule, A.J.; Snijders, P.J.; Raaphorst, P.M.; !1Schrijnemakers, H.F.; Delius, H.; Gissmann, L.; Meijer, !1C.J.; Walboomers, J.M. !$#journal J. Clin. Microbiol. (1992) 30:1716-1721 !$#title General primer polymerase chain reaction in combination with !1sequence analysis for identification of potentially novel !1human papillomavirus genotypes in cervical lesions. !$#cross-references MUID:92332706; PMID:1321168 !$#contents mucosotropic type 16, cervical smear !$#accession F44906 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 363-395 ##label VAN !'##note sequence extracted from NCBI backbone (NCBIP:109407) REFERENCE Z17014 !$#authors Kennedy, I.M.; Haddow, J.K.; Clements, J.B. !$#journal J. Virol. (1991) 65:2093-2097 !$#title A negative element in the human poapillomavirus type 16 !1genome acts at the level of late mRNA stability. !$#cross-references MUID:91162763; PMID:1848319 !$#accession T10431 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-531 ##label KEN !'##cross-references EMBL:K02718; NID:g333031; PIDN:AAA46943.1; !1PID:g333037 GENETICS !$#gene L1 CLASSIFICATION #superfamily papillomavirus L1 protein KEYWORDS late protein SUMMARY #length 531 #molecular-weight 59554 #checksum 4969 SEQUENCE /// ENTRY P1WL31 #type complete TITLE L1 protein - human papillomavirus type 31 ORGANISM #formal_name human papillomavirus type 31 #note host Homo sapiens (man) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS G32444 REFERENCE A94398 !$#authors Goldsborough, M.D.; DiSilvestre, D.; Temple, G.F.; Lorincz, !1A.T. !$#journal Virology (1989) 171:306-311 !$#title Nucleotide sequence of human papillomavirus type 31: a !1cervical neoplasia-associated virus. !$#cross-references MUID:89299478; PMID:2545036 !$#accession G32444 !'##status translation not shown !'##molecule_type DNA !'##residues 1-504 ##label GOL !'##cross-references GB:J04353; NID:g333048; PIDN:AAA46956.1; !1PID:g459922 CLASSIFICATION #superfamily papillomavirus L1 protein KEYWORDS late protein SUMMARY #length 504 #molecular-weight 56352 #checksum 7380 SEQUENCE /// ENTRY P1WL35 #type complete TITLE L1 protein - human papillomavirus type 35 ORGANISM #formal_name human papillomavirus type 35 #note host Homo sapiens (man) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS G40824; C44889 REFERENCE A40824 !$#authors Marich, J.E.; Pontsler, A.V.; Rice, S.M.; McGraw, K.A.; !1Dubensky, T.W. !$#journal Virology (1992) 186:770-776 !$#title The phylogenetic relationship and complete nucleotide !1sequence of human papillomavirus type 35. !$#cross-references MUID:92124753; PMID:1310198 !$#accession G40824 !'##status translation not shown !'##molecule_type DNA !'##residues 1-505 ##label MAR !'##cross-references GB:M74117; NID:g333050; PIDN:AAA46972.1; !1PID:g333058 REFERENCE A44889 !$#authors van den Brule, A.J.; Snijders, P.J.; Raaphorst, P.M.; !1Schrijnemakers, H.F.; Delius, H.; Gissmann, L.; Meijer, !1C.J.; Walboomers, J.M. !$#journal J. Clin. Microbiol. (1992) 30:1716-1721 !$#title General primer polymerase chain reaction in combination with !1sequence analysis for identification of potentially novel !1human papillomavirus genotypes in cervical lesions. !$#cross-references MUID:92332706; PMID:1321168 !$#accession C44889 !'##molecule_type DNA !'##residues 338-370 ##label VAN !'##cross-references GB:S40240; NID:g251686; PIDN:AAB22564.1; !1PID:g251687 !'##experimental_source mucosotropic type 35, cervical smear !'##note sequence extracted from NCBI backbone (NCBIN:109393, !1NCBIP:109408) CLASSIFICATION #superfamily papillomavirus L1 protein KEYWORDS late protein SUMMARY #length 505 #molecular-weight 56519 #checksum 2922 SEQUENCE /// ENTRY P1WL33 #type complete TITLE L1 protein - human papillomavirus type 33 ORGANISM #formal_name human papillomavirus type 33 DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 16-Jul-1999 ACCESSIONS A03641 REFERENCE A93020 !$#authors Cole, S.T.; Streeck, R.E. !$#journal J. Virol. (1986) 58:991-995 !$#title Genome organization and nucleotide sequence of human !1papillomavirus type 33, which is associated with cervical !1cancer. !$#cross-references MUID:86200464; PMID:3009902 !$#accession A03641 !'##molecule_type DNA !'##residues 1-499 ##label COL !'##cross-references GB:M12732; NID:g333049; PIDN:AAA46964.1; !1PID:g463183 CLASSIFICATION #superfamily papillomavirus L1 protein KEYWORDS late protein SUMMARY #length 499 #molecular-weight 55902 #checksum 8450 SEQUENCE /// ENTRY P1WL58 #type complete TITLE L1 protein - human papillomavirus type 58 ORGANISM #formal_name human papillomavirus type 58 #note host Homo sapiens (man) DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 21-Jul-2000 ACCESSIONS G36779 REFERENCE A36779 !$#authors Kirii, Y.; Iwamoto, S.; Matsukura, T. !$#journal Virology (1991) 185:424-427 !$#title Human papillomavirus type 58 DNA sequence. !$#cross-references MUID:92024102; PMID:1656594 !$#accession G36779 !'##status translation not shown !'##molecule_type DNA !'##residues 1-524 ##label KIR !'##cross-references GB:D90400; NID:g222386; PIDN:BAA31851.1; !1PID:g3337104 CLASSIFICATION #superfamily papillomavirus L1 protein KEYWORDS late protein SUMMARY #length 524 #molecular-weight 59038 #checksum 3601 SEQUENCE /// ENTRY P1WL18 #type complete TITLE L1 protein - human papillomavirus type 18 ORGANISM #formal_name human papillomavirus type 18 DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 24-Feb-1994 ACCESSIONS A26251 REFERENCE A92937 !$#authors Cole, S.T.; Danos, O. !$#journal J. Mol. Biol. (1987) 193:599-608 !$#title Nucleotide sequence and comparative analysis of the human !1papillomavirus type 18 genome. Phylogeny of papillomaviruses !1and repeated structure of the E6 and E7 gene products. !$#cross-references MUID:87283882; PMID:3039146 !$#accession A26251 !'##molecule_type DNA !'##residues 1-568 ##label COL CLASSIFICATION #superfamily papillomavirus L1 protein KEYWORDS late protein SUMMARY #length 568 #molecular-weight 63741 #checksum 6794 SEQUENCE /// ENTRY P1WLPR #type complete TITLE L1 protein - human papillomavirus type ME180 (provirus) ORGANISM #formal_name human papillomavirus type ME180 #note host Homo sapiens (man) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 28-Jul-2000 ACCESSIONS B40509 REFERENCE A40509 !$#authors Reuter, S.; Delius, H.; Kahn, T.; Hofmann, B.; zur Hausen, !1H.; Schwarz, E. !$#journal J. Virol. (1991) 65:5564-5568 !$#title Characterization of a novel human papillomavirus DNA in the !1cervical carcinoma cell line ME180. !$#cross-references MUID:91374616; PMID:1716694 !$#accession B40509 !'##status translation not shown !'##molecule_type DNA !'##residues 1-505 ##label REU !'##cross-references GB:M73258; NID:g184383; PIDN:AAF14010.1; !1PID:g6478870 CLASSIFICATION #superfamily papillomavirus L1 protein KEYWORDS late protein SUMMARY #length 505 #molecular-weight 56805 #checksum 4496 SEQUENCE /// ENTRY P1WL39 #type complete TITLE L1 protein - human papillomavirus type 39 ORGANISM #formal_name human papillomavirus type 39 #note host Homo sapiens (man) DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jul-1999 ACCESSIONS H38502 REFERENCE A38502 !$#authors Volpers, C.; Streeck, R.E. !$#journal Virology (1991) 181:419-423 !$#title Genome organization and nucleotide sequence of human !1papillomavirus type 39. !$#cross-references MUID:91135017; PMID:1847266 !$#accession H38502 !'##status translation not shown !'##molecule_type DNA !'##residues 1-505 ##label VOL !'##cross-references GB:M62849; EMBL:M38185; NID:g333245; !1PIDN:AAA47056.1; PID:g463192 CLASSIFICATION #superfamily papillomavirus L1 protein KEYWORDS late protein SUMMARY #length 505 #molecular-weight 56604 #checksum 2488 SEQUENCE /// ENTRY P1WL51 #type complete TITLE L1 protein - human papillomavirus type 51 ORGANISM #formal_name human papillomavirus type 51 #note host Homo sapiens (man) DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jul-1999 ACCESSIONS G40415; G44889 REFERENCE A40415 !$#authors Lungu, O.; Crum, C.P.; Silverstein, S.J. !$#journal J. Virol. (1991) 65:4216-4225 !$#title Biologic properties and nucleotide sequence analysis of !1human papillomavirus type 51. !$#cross-references MUID:91303675; PMID:1649326 !$#accession G40415 !'##status translation not shown !'##molecule_type DNA !'##residues 1-504 ##label LUN !'##cross-references GB:M62877 REFERENCE A44889 !$#authors van den Brule, A.J.; Snijders, P.J.; Raaphorst, P.M.; !1Schrijnemakers, H.F.; Delius, H.; Gissmann, L.; Meijer, !1C.J.; Walboomers, J.M. !$#journal J. Clin. Microbiol. (1992) 30:1716-1721 !$#title General primer polymerase chain reaction in combination with !1sequence analysis for identification of potentially novel !1human papillomavirus genotypes in cervical lesions. !$#cross-references MUID:92332706; PMID:1321168 !$#accession G44889 !'##molecule_type DNA !'##residues 337-369 ##label VAN !'##cross-references GB:S40272; NID:g251694; PIDN:AAB22568.1; !1PID:g251695 !'##experimental_source mucosotropic type 51, cervical smear !'##note sequence extracted from NCBI backbone (NCBIN:109397, !1NCBIP:109409) CLASSIFICATION #superfamily papillomavirus L1 protein KEYWORDS late protein SUMMARY #length 504 #molecular-weight 56314 #checksum 7345 SEQUENCE /// ENTRY P1WL8 #type complete TITLE L1 protein - human papillomavirus type 8 ORGANISM #formal_name human papillomavirus type 8 DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 07-Nov-1997 ACCESSIONS A03642 REFERENCE A93019 !$#authors Fuchs, P.G.; Iftner, T.; Weninger, J.; Pfister, H. !$#journal J. Virol. (1986) 58:626-634 !$#title Epidermodysplasia verruciformis-associated human !1papillomavirus 8: genomic sequence and comparative analysis. !$#cross-references MUID:86200410; PMID:3009874 !$#accession A03642 !'##molecule_type DNA !'##residues 1-514 ##label FUC !'##cross-references GB:M12737; NID:g333074 !'##note this ORF is not annotated in GenBank entry PPH8CG CLASSIFICATION #superfamily papillomavirus L1 protein KEYWORDS late protein SUMMARY #length 514 #molecular-weight 58561 #checksum 4118 SEQUENCE /// ENTRY P1WL5 #type complete TITLE L1 protein - human papillomavirus type 5 ORGANISM #formal_name human papillomavirus type 5 DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 24-Feb-1994 ACCESSIONS A26277 REFERENCE A94360 !$#authors Zachow, K.R.; Ostrow, R.S.; Faras, A.J. !$#journal Virology (1987) 158:251-254 !$#title Nucleotide sequence and genome organization of human !1papillomavirus type 5. !$#cross-references MUID:87207670; PMID:3033892 !$#accession A26277 !'##molecule_type DNA !'##residues 1-516 ##label ZAC CLASSIFICATION #superfamily papillomavirus L1 protein KEYWORDS late protein SUMMARY #length 516 #molecular-weight 58881 #checksum 9680 SEQUENCE /// ENTRY P1WLB5 #type complete TITLE L1 protein - human papillomavirus type 5b ORGANISM #formal_name human papillomavirus type 5b #note host Homo sapiens (man) DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jun-2000 ACCESSIONS G40480 REFERENCE A40480 !$#authors Yabe, Y.; Sakai, A.; Hitsumoto, T.; Kato, H.; Ogura, H. !$#journal Virology (1991) 183:793-798 !$#title A subtype of human papillomavirus 5 (HPV-5b) and its !1subgenomic segment amplified in a carcinoma: nucleotide !1sequences and genomic organizations. !$#cross-references MUID:91306467; PMID:1649510 !$#accession G40480 !'##status translation not shown !'##molecule_type DNA !'##residues 1-525 ##label YAB !'##cross-references GB:D90252; NID:g222395; PIDN:BAA14300.1; !1PID:g222404 CLASSIFICATION #superfamily papillomavirus L1 protein KEYWORDS late protein SUMMARY #length 525 #molecular-weight 59603 #checksum 3637 SEQUENCE /// ENTRY P1WL47 #type complete TITLE L1 protein - human papillomavirus type 47 ORGANISM #formal_name human papillomavirus type 47 #note host Homo sapiens (man) DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Jul-1999 ACCESSIONS G35324 REFERENCE A35324 !$#authors Kiyono, T.; Adachi, A.; Ishibashi, M. !$#journal Virology (1990) 177:401-405 !$#title Genome organization and taxonomic position of human !1papillomavirus type 47 inferred from its DNA sequence. !$#cross-references MUID:90281611; PMID:2162112 !$#accession G35324 !'##status translation not shown !'##molecule_type DNA !'##residues 1-514 ##label KIY !'##cross-references GB:M32305; NID:g333062; PIDN:AAA46982.1; !1PID:g333070 CLASSIFICATION #superfamily papillomavirus L1 protein KEYWORDS late protein SUMMARY #length 514 #molecular-weight 58283 #checksum 3124 SEQUENCE /// ENTRY S15620 #type complete TITLE L1 protein - human papillomavirus type 2a ORGANISM #formal_name human papillomavirus type 2a #note host Homo sapiens (man) DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 17-Feb-1994 ACCESSIONS S15620 REFERENCE S15614 !$#authors Hirsch-Behnam, A.; Delius, H.; de Villiers, E.M. !$#journal Virus Res. (1990) 18:81-98 !$#title A comparative sequence analysis of two human papillomavirus !1(HPV) types 2a and 57. !$#cross-references MUID:91188699; PMID:1964523 !$#accession S15620 !'##molecule_type DNA !'##residues 1-510 ##label HIR !'##cross-references EMBL:X55964 CLASSIFICATION #superfamily papillomavirus L1 protein KEYWORDS late protein SUMMARY #length 510 #molecular-weight 57193 #checksum 5538 SEQUENCE /// ENTRY S15627 #type complete TITLE L1 protein - human papillomavirus type 57 ORGANISM #formal_name human papillomavirus type 57 #note host Homo sapiens (man) DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS S15627 REFERENCE S15614 !$#authors Hirsch-Behnam, A.; Delius, H.; de Villiers, E.M. !$#journal Virus Res. (1990) 18:81-98 !$#title A comparative sequence analysis of two human papillomavirus !1(HPV) types 2a and 57. !$#cross-references MUID:91188699; PMID:1964523 !$#accession S15627 !'##molecule_type DNA !'##residues 1-510 ##label HIR !'##cross-references EMBL:X55965; NID:g60882; PIDN:CAA39436.1; !1PID:g60889 CLASSIFICATION #superfamily papillomavirus L1 protein KEYWORDS late protein SUMMARY #length 510 #molecular-weight 57239 #checksum 4160 SEQUENCE /// ENTRY P1WLR1 #type complete TITLE L1 protein - rhesus papillomavirus (type 1) ORGANISM #formal_name rhesus papillomavirus DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 27-Jan-1995 ACCESSIONS H38503 REFERENCE A38503 !$#authors Ostrow, R.S.; LaBresh, K.V.; Faras, A.J. !$#journal Virology (1991) 181:424-429 !$#title Characterization of the complete RhPV 1 genomic sequence and !1an integration locus from a metastatic tumor. !$#cross-references MUID:91135018; PMID:1847267 !$#accession H38503 !'##status translation not shown !'##molecule_type DNA !'##residues 1-354 ##label OST !'##cross-references EMBL:M37717 CLASSIFICATION #superfamily papillomavirus L1 protein KEYWORDS late protein SUMMARY #length 354 #molecular-weight 39606 #checksum 5876 SEQUENCE /// ENTRY P1WLRB #type complete TITLE L1 protein - cottontail rabbit papillomavirus ORGANISM #formal_name cottontail rabbit papillomavirus DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 24-Feb-1994 ACCESSIONS A03643 REFERENCE A94027 !$#authors Giri, I.; Danos, O.; Yaniv, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:1580-1584 !$#title Genomic structure of the cottontail rabbit (Shope) !1papillomavirus. !$#cross-references MUID:85166175; PMID:2984661 !$#accession A03643 !'##molecule_type DNA !'##residues 1-505 ##label GIR CLASSIFICATION #superfamily papillomavirus L1 protein KEYWORDS late protein SUMMARY #length 505 #molecular-weight 57932 #checksum 5831 SEQUENCE /// ENTRY P1WLB4 #type complete TITLE L1 protein - bovine papillomavirus type 4 ORGANISM #formal_name bovine papillomavirus type 4 DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jun-2000 ACCESSIONS B26214 REFERENCE A92795 !$#authors Patel, K.R.; Smith, K.T.; Campo, M.S. !$#journal J. Gen. Virol. (1987) 68:2117-2128 !$#title The nucleotide sequence and genome organization of bovine !1papillomavirus type 4. !$#cross-references MUID:87282264; PMID:3039043 !$#accession B26214 !'##molecule_type DNA !'##residues 1-506 ##label PAT !'##cross-references GB:D00146; NID:g222360; PIDN:BAA00101.1; !1PID:g222368 CLASSIFICATION #superfamily papillomavirus L1 protein KEYWORDS late protein SUMMARY #length 506 #molecular-weight 57902 #checksum 1543 SEQUENCE /// ENTRY P1WLB #type complete TITLE L1 protein - bovine papillomavirus type 1 ORGANISM #formal_name bovine papillomavirus type 1 DATE 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 28-Jul-2000 ACCESSIONS A03644 REFERENCE A93289 !$#authors Chen, E.Y.; Howley, P.M.; Levinson, A.D.; Seeburg, P.H. !$#journal Nature (1982) 299:529-534 !$#title The primary structure and genetic organization of the bovine !1papillomavirus type 1 genome. !$#cross-references MUID:83012974; PMID:6289124 !$#accession A03644 !'##molecule_type DNA !'##residues 1-495 ##label CHE !'##cross-references GB:X02346; GB:J02044; GB:M24622; GB:X00473; !1NID:g60965; PIDN:CAB46515.1; PID:g5419938 CLASSIFICATION #superfamily papillomavirus L1 protein KEYWORDS late protein SUMMARY #length 495 #molecular-weight 55551 #checksum 2832 SEQUENCE /// ENTRY P1WLB2 #type complete TITLE L1 protein - bovine papillomavirus type 2 ORGANISM #formal_name bovine papillomavirus type 2 DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 12-Jun-1998 ACCESSIONS A31169 REFERENCE A94519 !$#authors Groff, D.E.; Mitra, R.; Lancaster, W.D. !$#submission submitted to GenBank, May 1988 !$#accession A31169 !'##molecule_type DNA !'##residues 1-501 ##label GRO !'##cross-references GB:X01768; GB:M24326; NID:g60859 CLASSIFICATION #superfamily papillomavirus L1 protein KEYWORDS glycoprotein; late protein FEATURE !$214,342,489 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 501 #molecular-weight 56130 #checksum 1747 SEQUENCE /// ENTRY P1WLDP #type complete TITLE L1 protein - deer papillomavirus ORGANISM #formal_name deer papillomavirus DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 16-Jul-1999 ACCESSIONS A03645 REFERENCE A93013 !$#authors Groff, D.E.; Lancaster, W.D. !$#journal J. Virol. (1985) 56:85-91 !$#title Molecular cloning and nucleotide sequence of deer !1papillomavirus. !$#cross-references MUID:85293253; PMID:2993669 !$#accession A03645 !'##molecule_type DNA !'##residues 1-513 ##label GRO !'##cross-references GB:M11910; NID:g333021; PIDN:AAA66848.1; !1PID:g808795 CLASSIFICATION #superfamily papillomavirus L1 protein KEYWORDS late protein SUMMARY #length 513 #molecular-weight 58145 #checksum 4460 SEQUENCE /// ENTRY P1WLEP #type complete TITLE L1 protein - European elk papillomavirus ORGANISM #formal_name European elk papillomavirus DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 11-May-2000 ACCESSIONS A94457; A94506; G29499 REFERENCE A94457 !$#authors Eriksson, A. !$#citation unpublished results 1987, cited by GenBank !$#accession A94457 !'##molecule_type DNA !'##residues 1-501 ##label ERI !'##cross-references GB:M15953; NID:g333025; PIDN:AAA66861.1; !1PID:g484027 REFERENCE A94506 !$#authors Pettersson, U. !$#submission submitted to GenBank, August 1987 !$#accession A94506 !'##molecule_type DNA !'##residues 1-501 ##label PET !'##cross-references GB:M15953; NID:g333025; PIDN:AAA66861.1; !1PID:g484027 CLASSIFICATION #superfamily papillomavirus L1 protein KEYWORDS late protein SUMMARY #length 501 #molecular-weight 56459 #checksum 5734 SEQUENCE /// ENTRY P2WL #type complete TITLE L2 protein - human papillomavirus type 1a ORGANISM #formal_name human papillomavirus type 1a DATE 18-Aug-1982 #sequence_revision 28-Aug-1985 #text_change 16-Jul-1999 ACCESSIONS A03646 REFERENCE A90970 !$#authors Danos, O.; Katinka, M.; Yaniv, M. !$#journal EMBO J. (1982) 1:231-236 !$#title Human papillomavirus 1a complete DNA sequence: a novel type !1of genome organization among papovaviridae. !$#cross-references MUID:84182467; PMID:6325156 !$#accession A03646 !'##molecule_type DNA !'##residues 1-507 ##label DAN !'##cross-references GB:V01116; GB:X03321; NID:g60966; PIDN:CAA24317.1; !1PID:g1041634 CLASSIFICATION #superfamily papillomavirus L2 protein KEYWORDS late protein SUMMARY #length 507 #molecular-weight 55329 #checksum 78 SEQUENCE /// ENTRY P2WL6 #type complete TITLE L2 protein - human papillomavirus type 6b ORGANISM #formal_name human papillomavirus type 6b DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 16-Jul-1999 ACCESSIONS A03647 REFERENCE A90975 !$#authors Schwarz, E.; Durst, M.; Demankowski, C.; Lattermann, O.; !1Zech, R.; Wolfsperger, E.; Suhai, S.; zur Hausen, H. !$#journal EMBO J. (1983) 2:2341-2348 !$#title DNA sequence and genome organization of genital human !1papillomavirus type 6b. !$#cross-references MUID:84131949; PMID:6321162 !$#accession A03647 !'##molecule_type DNA !'##residues 1-459 ##label SCH !'##cross-references GB:X00203; NID:g60955; PIDN:CAA25025.1; PID:g60963 CLASSIFICATION #superfamily papillomavirus L2 protein KEYWORDS late protein SUMMARY #length 459 #molecular-weight 49391 #checksum 1431 SEQUENCE /// ENTRY P2WL11 #type complete TITLE L2 protein - human papillomavirus type 11 ORGANISM #formal_name human papillomavirus type 11 DATE 13-Aug-1986 #sequence_revision 13-Aug-1986 #text_change 16-Jul-1999 ACCESSIONS A03648 REFERENCE A94338 !$#authors Dartmann, K.; Schwarz, E.; Gissmann, L.; zur Hausen, H. !$#journal Virology (1986) 151:124-130 !$#title The nucleotide sequence and genome organization of human !1papilloma virus type 11. !$#cross-references MUID:86181601; PMID:3008427 !$#accession A03648 !'##molecule_type DNA !'##residues 1-455 ##label DAR !'##cross-references GB:M14119; NID:g333026; PIDN:AAA46934.1; !1PID:g496200 CLASSIFICATION #superfamily papillomavirus L2 protein KEYWORDS late protein SUMMARY #length 455 #molecular-weight 49096 #checksum 4747 SEQUENCE /// ENTRY P2WLC1 #type complete TITLE L2 protein - pygmy chimpanzee papillomavirus (type 1) ORGANISM #formal_name pygmy chimpanzee papillomavirus DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS G36818 REFERENCE A42955 !$#authors van Ranst, M.; Fuse, A.; Fiten, P.; Beuken, E.; Pfister, H.; !1Burk, R.D.; Opdenakker, G. !$#journal Virology (1992) 190:587-596 !$#title Human papillomavirus type 13 and pygmy chimpanzee !1papillomavirus type 1: Comparison of the genome !1organizations. !$#cross-references MUID:92391075; PMID:1325697 !$#accession G36818 !'##molecule_type DNA !'##residues 1-463 ##label VAN !'##cross-references EMBL:X62844; NID:g61010; PIDN:CAA44661.1; !1PID:g61017 CLASSIFICATION #superfamily papillomavirus L2 protein KEYWORDS late protein SUMMARY #length 463 #molecular-weight 49695 #checksum 5858 SEQUENCE /// ENTRY P2WLHS #type complete TITLE minor capsid protein L2 - human papillomavirus type 16 ORGANISM #formal_name human papillomavirus type 16 DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 20-Aug-1999 ACCESSIONS A03649; T10430 REFERENCE A22355 !$#authors Seedorf, K.; Krammer, G.; Durst, M.; Suhai, S.; Rowekamp, !1W.G. !$#journal Virology (1985) 145:181-185 !$#title Human papillomavirus type 16 DNA sequence. !$#cross-references MUID:85246220; PMID:2990099 !$#accession A03649 !'##molecule_type DNA !'##residues 1-473 ##label SEE !'##cross-references GB:K02718; NID:g333031; PIDN:AAA46942.1; !1PID:g333036 REFERENCE Z17014 !$#authors Kennedy, I.M.; Haddow, J.K.; Clements, J.B. !$#journal J. Virol. (1991) 65:2093-2097 !$#title A negative element in the human poapillomavirus type 16 !1genome acts at the level of late mRNA stability. !$#cross-references MUID:91162763; PMID:1848319 !$#accession T10430 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-473 ##label KEN !'##cross-references EMBL:K02718; NID:g333031; PIDN:AAA46942.1; !1PID:g333036 GENETICS !$#gene L2 CLASSIFICATION #superfamily papillomavirus L2 protein KEYWORDS late protein SUMMARY #length 473 #molecular-weight 50687 #checksum 7853 SEQUENCE /// ENTRY P2WL42 #type complete TITLE L2 protein - human papillomavirus type 42 ORGANISM #formal_name human papillomavirus type 42 #note host Homo sapiens (man) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 27-Jan-1995 ACCESSIONS H39451 REFERENCE A39451 !$#authors Philipp, W.; Honore, N.; Sapp, M.; Cole, S.T.; Streeck, R.E. !$#journal Virology (1992) 186:331-334 !$#title Human papillomavirus type 42: new sequence, conserved genome !1organization. !$#cross-references MUID:92087479; PMID:1309278 !$#accession H39451 !'##status translation not shown !'##molecule_type DNA !'##residues 1-477 ##label PHI !'##cross-references GB:M73236 CLASSIFICATION #superfamily papillomavirus L2 protein KEYWORDS late protein SUMMARY #length 477 #molecular-weight 51253 #checksum 4068 SEQUENCE /// ENTRY P2WL31 #type complete TITLE L2 protein - human papillomavirus type 31 ORGANISM #formal_name human papillomavirus type 31 #note host Homo sapiens (man) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS H32444 REFERENCE A94398 !$#authors Goldsborough, M.D.; DiSilvestre, D.; Temple, G.F.; Lorincz, !1A.T. !$#journal Virology (1989) 171:306-311 !$#title Nucleotide sequence of human papillomavirus type 31: a !1cervical neoplasia-associated virus. !$#cross-references MUID:89299478; PMID:2545036 !$#accession H32444 !'##status translation not shown !'##molecule_type DNA !'##residues 1-466 ##label GOL !'##cross-references GB:J04353; NID:g333048; PIDN:AAA46955.1; !1PID:g459921 CLASSIFICATION #superfamily papillomavirus L2 protein KEYWORDS late protein SUMMARY #length 466 #molecular-weight 49974 #checksum 7867 SEQUENCE /// ENTRY P2WL35 #type complete TITLE L2 protein - human papillomavirus type 35 ORGANISM #formal_name human papillomavirus type 35 #note host Homo sapiens (man) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS H40824 REFERENCE A40824 !$#authors Marich, J.E.; Pontsler, A.V.; Rice, S.M.; McGraw, K.A.; !1Dubensky, T.W. !$#journal Virology (1992) 186:770-776 !$#title The phylogenetic relationship and complete nucleotide !1sequence of human papillomavirus type 35. !$#cross-references MUID:92124753; PMID:1310198 !$#accession H40824 !'##status translation not shown !'##molecule_type DNA !'##residues 1-469 ##label MAR !'##cross-references GB:M74117; NID:g333050; PIDN:AAA46971.1; !1PID:g333057 CLASSIFICATION #superfamily papillomavirus L2 protein KEYWORDS late protein SUMMARY #length 469 #molecular-weight 50431 #checksum 798 SEQUENCE /// ENTRY P2WL33 #type complete TITLE L2 protein - human papillomavirus type 33 ORGANISM #formal_name human papillomavirus type 33 DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 16-Jul-1999 ACCESSIONS A03650 REFERENCE A93020 !$#authors Cole, S.T.; Streeck, R.E. !$#journal J. Virol. (1986) 58:991-995 !$#title Genome organization and nucleotide sequence of human !1papillomavirus type 33, which is associated with cervical !1cancer. !$#cross-references MUID:86200464; PMID:3009902 !$#accession A03650 !'##molecule_type DNA !'##residues 1-467 ##label COL !'##cross-references GB:M12732; NID:g333049; PIDN:AAA46963.1; !1PID:g463182 CLASSIFICATION #superfamily papillomavirus L2 protein KEYWORDS late protein SUMMARY #length 467 #molecular-weight 50595 #checksum 9246 SEQUENCE /// ENTRY P2WL58 #type complete TITLE L2 protein - human papillomavirus type 58 ORGANISM #formal_name human papillomavirus type 58 #note host Homo sapiens (man) DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 21-Jul-2000 ACCESSIONS H36779 REFERENCE A36779 !$#authors Kirii, Y.; Iwamoto, S.; Matsukura, T. !$#journal Virology (1991) 185:424-427 !$#title Human papillomavirus type 58 DNA sequence. !$#cross-references MUID:92024102; PMID:1656594 !$#accession H36779 !'##status translation not shown !'##molecule_type DNA !'##residues 1-472 ##label KIR !'##cross-references GB:D90400; NID:g222386; PIDN:BAA31850.1; !1PID:g3337103 CLASSIFICATION #superfamily papillomavirus L2 protein KEYWORDS late protein SUMMARY #length 472 #molecular-weight 50943 #checksum 5302 SEQUENCE /// ENTRY P2WLR1 #type complete TITLE L2 protein - rhesus papillomavirus (type 1) ORGANISM #formal_name rhesus papillomavirus DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 27-Jan-1995 ACCESSIONS G38503 REFERENCE A38503 !$#authors Ostrow, R.S.; LaBresh, K.V.; Faras, A.J. !$#journal Virology (1991) 181:424-429 !$#title Characterization of the complete RhPV 1 genomic sequence and !1an integration locus from a metastatic tumor. !$#cross-references MUID:91135018; PMID:1847267 !$#accession G38503 !'##status translation not shown !'##molecule_type DNA !'##residues 1-466 ##label OST !'##cross-references EMBL:M37717 CLASSIFICATION #superfamily papillomavirus L2 protein KEYWORDS late protein SUMMARY #length 466 #molecular-weight 49428 #checksum 4573 SEQUENCE /// ENTRY P2WL13 #type complete TITLE L2 protein - human papillomavirus type 13 ORGANISM #formal_name human papillomavirus type 13 #note host Homo sapiens (man) DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS G42955 REFERENCE A42955 !$#authors van Ranst, M.; Fuse, A.; Fiten, P.; Beuken, E.; Pfister, H.; !1Burk, R.D.; Opdenakker, G. !$#journal Virology (1992) 190:587-596 !$#title Human papillomavirus type 13 and pygmy chimpanzee !1papillomavirus type 1: Comparison of the genome !1organizations. !$#cross-references MUID:92391075; PMID:1325697 !$#accession G42955 !'##molecule_type DNA !'##residues 1-463 ##label VAN !'##cross-references EMBL:X62843; NID:g60295; PIDN:CAA44653.1; !1PID:g60302 CLASSIFICATION #superfamily papillomavirus L2 protein KEYWORDS late protein SUMMARY #length 463 #molecular-weight 49351 #checksum 3801 SEQUENCE /// ENTRY P2WL51 #type complete TITLE L2 protein - human papillomavirus type 51 ORGANISM #formal_name human papillomavirus type 51 #note host Homo sapiens (man) DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 27-Jan-1995 ACCESSIONS H40415 REFERENCE A40415 !$#authors Lungu, O.; Crum, C.P.; Silverstein, S.J. !$#journal J. Virol. (1991) 65:4216-4225 !$#title Biologic properties and nucleotide sequence analysis of !1human papillomavirus type 51. !$#cross-references MUID:91303675; PMID:1649326 !$#accession H40415 !'##status translation not shown !'##molecule_type DNA !'##residues 1-468 ##label LUN !'##cross-references GB:M62877 CLASSIFICATION #superfamily papillomavirus L2 protein KEYWORDS late protein SUMMARY #length 468 #molecular-weight 50720 #checksum 6971 SEQUENCE /// ENTRY P2WL18 #type complete TITLE L2 protein - human papillomavirus type 18 ORGANISM #formal_name human papillomavirus type 18 DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Jul-1999 ACCESSIONS B26251 REFERENCE A92937 !$#authors Cole, S.T.; Danos, O. !$#journal J. Mol. Biol. (1987) 193:599-608 !$#title Nucleotide sequence and comparative analysis of the human !1papillomavirus type 18 genome. Phylogeny of papillomaviruses !1and repeated structure of the E6 and E7 gene products. !$#cross-references MUID:87283882; PMID:3039146 !$#accession B26251 !'##molecule_type DNA !'##residues 1-462 ##label COL !'##cross-references GB:X05015; NID:g60975; PIDN:CAA28670.1; PID:g60982 CLASSIFICATION #superfamily papillomavirus L2 protein KEYWORDS late protein SUMMARY #length 462 #molecular-weight 49596 #checksum 3974 SEQUENCE /// ENTRY P2WLPR #type complete TITLE L2 protein - human papillomavirus type ME180 (provirus) ORGANISM #formal_name human papillomavirus type ME180 #note host Homo sapiens (man) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 28-Jul-2000 ACCESSIONS A40509 REFERENCE A40509 !$#authors Reuter, S.; Delius, H.; Kahn, T.; Hofmann, B.; zur Hausen, !1H.; Schwarz, E. !$#journal J. Virol. (1991) 65:5564-5568 !$#title Characterization of a novel human papillomavirus DNA in the !1cervical carcinoma cell line ME180. !$#cross-references MUID:91374616; PMID:1716694 !$#accession A40509 !'##status translation not shown !'##molecule_type DNA !'##residues 1-469 ##label REU !'##cross-references GB:M73258; NID:g184383; PIDN:AAF14009.1; !1PID:g6478869 CLASSIFICATION #superfamily papillomavirus L2 protein KEYWORDS late protein SUMMARY #length 469 #molecular-weight 50008 #checksum 375 SEQUENCE /// ENTRY P2WL39 #type complete TITLE L2 protein - human papillomavirus type 39 ORGANISM #formal_name human papillomavirus type 39 #note host Homo sapiens (man) DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jul-1999 ACCESSIONS G38502 REFERENCE A38502 !$#authors Volpers, C.; Streeck, R.E. !$#journal Virology (1991) 181:419-423 !$#title Genome organization and nucleotide sequence of human !1papillomavirus type 39. !$#cross-references MUID:91135017; PMID:1847266 !$#accession G38502 !'##status translation not shown !'##molecule_type DNA !'##residues 1-470 ##label VOL !'##cross-references GB:M62849; EMBL:M38185; NID:g333245; !1PIDN:AAA47055.1; PID:g463191 CLASSIFICATION #superfamily papillomavirus L2 protein KEYWORDS late protein SUMMARY #length 470 #molecular-weight 50219 #checksum 2951 SEQUENCE /// ENTRY S15619 #type complete TITLE L2 protein - human papillomavirus type 2a ORGANISM #formal_name human papillomavirus type 2a #note host Homo sapiens (man) DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 27-Jan-1995 ACCESSIONS S15619 REFERENCE S15614 !$#authors Hirsch-Behnam, A.; Delius, H.; de Villiers, E.M. !$#journal Virus Res. (1990) 18:81-98 !$#title A comparative sequence analysis of two human papillomavirus !1(HPV) types 2a and 57. !$#cross-references MUID:91188699; PMID:1964523 !$#accession S15619 !'##status translation not shown !'##molecule_type DNA !'##residues 1-524 ##label HIR !'##cross-references EMBL:X55964 CLASSIFICATION #superfamily papillomavirus L2 protein KEYWORDS late protein SUMMARY #length 524 #molecular-weight 56531 #checksum 2548 SEQUENCE /// ENTRY S15626 #type complete TITLE protein L2 - human papillomavirus type 57 ORGANISM #formal_name human papillomavirus type 57 #note host Homo sapiens (man) DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS S15626 REFERENCE S15614 !$#authors Hirsch-Behnam, A.; Delius, H.; de Villiers, E.M. !$#journal Virus Res. (1990) 18:81-98 !$#title A comparative sequence analysis of two human papillomavirus !1(HPV) types 2a and 57. !$#cross-references MUID:91188699; PMID:1964523 !$#accession S15626 !'##molecule_type DNA !'##residues 1-465 ##label HIR !'##cross-references EMBL:X55965; NID:g60882; PIDN:CAA39435.1; !1PID:g60888 CLASSIFICATION #superfamily papillomavirus L2 protein KEYWORDS late protein SUMMARY #length 465 #molecular-weight 49281 #checksum 2670 SEQUENCE /// ENTRY P2WL8 #type complete TITLE L2 protein - human papillomavirus type 8 ORGANISM #formal_name human papillomavirus type 8 DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 07-Nov-1997 ACCESSIONS A03651 REFERENCE A93019 !$#authors Fuchs, P.G.; Iftner, T.; Weninger, J.; Pfister, H. !$#journal J. Virol. (1986) 58:626-634 !$#title Epidermodysplasia verruciformis-associated human !1papillomavirus 8: genomic sequence and comparative analysis. !$#cross-references MUID:86200410; PMID:3009874 !$#accession A03651 !'##molecule_type DNA !'##residues 1-518 ##label FUC !'##cross-references GB:M12737; NID:g333074 !'##note this ORF is not annotated in GenBank entry PPH8CG CLASSIFICATION #superfamily papillomavirus L2 protein KEYWORDS late protein SUMMARY #length 518 #molecular-weight 56795 #checksum 2842 SEQUENCE /// ENTRY P2WL5 #type complete TITLE L2 protein - human papillomavirus type 5 ORGANISM #formal_name human papillomavirus type 5 DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 24-Feb-1994 ACCESSIONS B26277 REFERENCE A94360 !$#authors Zachow, K.R.; Ostrow, R.S.; Faras, A.J. !$#journal Virology (1987) 158:251-254 !$#title Nucleotide sequence and genome organization of human !1papillomavirus type 5. !$#cross-references MUID:87207670; PMID:3033892 !$#accession B26277 !'##molecule_type DNA !'##residues 1-518 ##label ZAC CLASSIFICATION #superfamily papillomavirus L2 protein KEYWORDS late protein SUMMARY #length 518 #molecular-weight 56769 #checksum 2429 SEQUENCE /// ENTRY P2WLB5 #type complete TITLE L2 protein - human papillomavirus type 5b ORGANISM #formal_name human papillomavirus type 5b #note host Homo sapiens (man) DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jun-2000 ACCESSIONS H40480 REFERENCE A40480 !$#authors Yabe, Y.; Sakai, A.; Hitsumoto, T.; Kato, H.; Ogura, H. !$#journal Virology (1991) 183:793-798 !$#title A subtype of human papillomavirus 5 (HPV-5b) and its !1subgenomic segment amplified in a carcinoma: nucleotide !1sequences and genomic organizations. !$#cross-references MUID:91306467; PMID:1649510 !$#accession H40480 !'##status translation not shown !'##molecule_type DNA !'##residues 1-518 ##label YAB !'##cross-references GB:D90252; NID:g222395; PIDN:BAA14298.1; !1PID:g222402 CLASSIFICATION #superfamily papillomavirus L2 protein KEYWORDS late protein SUMMARY #length 518 #molecular-weight 56836 #checksum 3110 SEQUENCE /// ENTRY P2WL47 #type complete TITLE L2 protein - human papillomavirus type 47 ORGANISM #formal_name human papillomavirus type 47 #note host Homo sapiens (man) DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Jul-1999 ACCESSIONS F35324 REFERENCE A35324 !$#authors Kiyono, T.; Adachi, A.; Ishibashi, M. !$#journal Virology (1990) 177:401-405 !$#title Genome organization and taxonomic position of human !1papillomavirus type 47 inferred from its DNA sequence. !$#cross-references MUID:90281611; PMID:2162112 !$#accession F35324 !'##status translation not shown !'##molecule_type DNA !'##residues 1-518 ##label KIY !'##cross-references GB:M32305; NID:g333062; PIDN:AAA46981.1; !1PID:g333069 CLASSIFICATION #superfamily papillomavirus L2 protein KEYWORDS late protein SUMMARY #length 518 #molecular-weight 56435 #checksum 124 SEQUENCE /// ENTRY P2WL41 #type complete TITLE L2 protein - human papillomavirus type 41 ORGANISM #formal_name human papillomavirus type 41 #note host Homo sapiens (man) DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS G43550 REFERENCE A43550 !$#authors Hirt, L.; Hirsch-Behnam, A.; De Villiers, E.M. !$#journal Virus Res. (1990) 18:179-190 !$#title Nucleotide sequence of human papillomavirus (HPV) type 41: !1an unusual HPV type without a typical E2 binding site !1consensus sequence. !$#accession G43550 !'##status translation not shown !'##molecule_type DNA !'##residues 1-554 ##label HIR !'##cross-references EMBL:X56147; NID:g60942; PIDN:CAA39618.1; !1PID:g60949 CLASSIFICATION #superfamily papillomavirus L2 protein KEYWORDS late protein SUMMARY #length 554 #molecular-weight 59974 #checksum 4791 SEQUENCE /// ENTRY P2WLRB #type complete TITLE L2 protein - cottontail rabbit papillomavirus ORGANISM #formal_name cottontail rabbit papillomavirus DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 24-Feb-1994 ACCESSIONS A03652 REFERENCE A94027 !$#authors Giri, I.; Danos, O.; Yaniv, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:1580-1584 !$#title Genomic structure of the cottontail rabbit (Shope) !1papillomavirus. !$#cross-references MUID:85166175; PMID:2984661 !$#accession A03652 !'##molecule_type DNA !'##residues 1-492 ##label GIR CLASSIFICATION #superfamily papillomavirus L2 protein KEYWORDS late protein SUMMARY #length 492 #molecular-weight 52803 #checksum 2284 SEQUENCE /// ENTRY P2WLB #type complete TITLE L2 protein - bovine papillomavirus type 1 ORGANISM #formal_name bovine papillomavirus type 1 DATE 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 28-Jul-2000 ACCESSIONS A03653 REFERENCE A93289 !$#authors Chen, E.Y.; Howley, P.M.; Levinson, A.D.; Seeburg, P.H. !$#journal Nature (1982) 299:529-534 !$#title The primary structure and genetic organization of the bovine !1papillomavirus type 1 genome. !$#cross-references MUID:83012974; PMID:6289124 !$#accession A03653 !'##molecule_type DNA !'##residues 1-469 ##label CHE !'##cross-references GB:X02346; GB:J02044; GB:M24622; GB:X00473; !1NID:g60965; PIDN:CAB57284.1; PID:g6010224 CLASSIFICATION #superfamily papillomavirus L2 protein KEYWORDS late protein SUMMARY #length 469 #molecular-weight 50014 #checksum 49 SEQUENCE /// ENTRY P2WLB2 #type complete TITLE L2 protein - bovine papillomavirus type 2 ORGANISM #formal_name bovine papillomavirus type 2 DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 12-Jun-1998 ACCESSIONS B31169 REFERENCE A94519 !$#authors Groff, D.E.; Mitra, R.; Lancaster, W.D. !$#submission submitted to GenBank, May 1988 !$#accession B31169 !'##molecule_type DNA !'##residues 1-495 ##label GRO !'##cross-references GB:X01768; GB:M24326; NID:g60859 CLASSIFICATION #superfamily papillomavirus L2 protein KEYWORDS glycoprotein; late protein FEATURE !$28,459,478 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 495 #molecular-weight 52957 #checksum 1879 SEQUENCE /// ENTRY P2WLB4 #type complete TITLE L2 protein - bovine papillomavirus type 4 ORGANISM #formal_name bovine papillomavirus type 4 DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jun-2000 ACCESSIONS A26214 REFERENCE A92795 !$#authors Patel, K.R.; Smith, K.T.; Campo, M.S. !$#journal J. Gen. Virol. (1987) 68:2117-2128 !$#title The nucleotide sequence and genome organization of bovine !1papillomavirus type 4. !$#cross-references MUID:87282264; PMID:3039043 !$#accession A26214 !'##molecule_type DNA !'##residues 1-357 ##label PAT !'##cross-references GB:D00146; NID:g222360; PIDN:BAA00100.1; !1PID:g222367 CLASSIFICATION #superfamily papillomavirus L2 protein KEYWORDS late protein SUMMARY #length 357 #molecular-weight 38725 #checksum 9353 SEQUENCE /// ENTRY P2WLDP #type complete TITLE L2 protein - deer papillomavirus ORGANISM #formal_name deer papillomavirus DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 16-Jul-1999 ACCESSIONS A03654 REFERENCE A93013 !$#authors Groff, D.E.; Lancaster, W.D. !$#journal J. Virol. (1985) 56:85-91 !$#title Molecular cloning and nucleotide sequence of deer !1papillomavirus. !$#cross-references MUID:85293253; PMID:2993669 !$#accession A03654 !'##molecule_type DNA !'##residues 1-493 ##label GRO !'##cross-references GB:M11910; NID:g333021; PIDN:AAA66846.1; !1PID:g808793 CLASSIFICATION #superfamily papillomavirus L2 protein KEYWORDS late protein SUMMARY #length 493 #molecular-weight 53727 #checksum 5119 SEQUENCE /// ENTRY P2WLEP #type complete TITLE L2 protein - European elk papillomavirus ORGANISM #formal_name European elk papillomavirus DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 11-May-2000 ACCESSIONS B94457; B94506; F29499 REFERENCE A94457 !$#authors Eriksson, A. !$#citation unpublished results 1987, cited by GenBank !$#accession B94457 !'##molecule_type DNA !'##residues 1-477 ##label ERI !'##cross-references GB:M15953; NID:g333025; PIDN:AAA66860.1; !1PID:g484026 REFERENCE A94506 !$#authors Pettersson, U. !$#submission submitted to GenBank, August 1987 !$#accession B94506 !'##molecule_type DNA !'##residues 1-477 ##label PET !'##cross-references GB:M15953; NID:g333025; PIDN:AAA66860.1; !1PID:g484026 CLASSIFICATION #superfamily papillomavirus L2 protein KEYWORDS late protein SUMMARY #length 477 #molecular-weight 51250 #checksum 2934 SEQUENCE /// ENTRY P3WLB5 #type complete TITLE L3 protein - human papillomavirus type 5b ORGANISM #formal_name human papillomavirus type 5b #note host Homo sapiens (man) DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jun-2000 ACCESSIONS I40480 REFERENCE A40480 !$#authors Yabe, Y.; Sakai, A.; Hitsumoto, T.; Kato, H.; Ogura, H. !$#journal Virology (1991) 183:793-798 !$#title A subtype of human papillomavirus 5 (HPV-5b) and its !1subgenomic segment amplified in a carcinoma: nucleotide !1sequences and genomic organizations. !$#cross-references MUID:91306467; PMID:1649510 !$#accession I40480 !'##status translation not shown !'##molecule_type DNA !'##residues 1-110 ##label YAB !'##cross-references GB:D90252; NID:g222395; PIDN:BAA14299.1; !1PID:g222403 CLASSIFICATION #superfamily papillomavirus type 5b L3 protein KEYWORDS late protein SUMMARY #length 110 #molecular-weight 13103 #checksum 7431 SEQUENCE /// ENTRY P3WLDP #type complete TITLE L3 protein - deer papillomavirus ORGANISM #formal_name deer papillomavirus DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Jul-1999 ACCESSIONS A22477 REFERENCE A93013 !$#authors Groff, D.E.; Lancaster, W.D. !$#journal J. Virol. (1985) 56:85-91 !$#title Molecular cloning and nucleotide sequence of deer !1papillomavirus. !$#cross-references MUID:85293253; PMID:2993669 !$#accession A22477 !'##molecule_type DNA !'##residues 1-35 ##label GRO !'##cross-references GB:M11910; NID:g333021; PIDN:AAA66847.1; !1PID:g808794 CLASSIFICATION #superfamily deer papillomavirus L3 protein KEYWORDS late protein SUMMARY #length 35 #molecular-weight 4239 #checksum 9754 SEQUENCE /// ENTRY P3WLB4 #type complete TITLE L3 protein - bovine papillomavirus type 4 ORGANISM #formal_name bovine papillomavirus type 4 DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jun-2000 ACCESSIONS C26214 REFERENCE A92795 !$#authors Patel, K.R.; Smith, K.T.; Campo, M.S. !$#journal J. Gen. Virol. (1987) 68:2117-2128 !$#title The nucleotide sequence and genome organization of bovine !1papillomavirus type 4. !$#cross-references MUID:87282264; PMID:3039043 !$#accession C26214 !'##molecule_type DNA !'##residues 1-113 ##label PAT !'##cross-references GB:D00146; NID:g222360; PIDN:BAA00102.1; !1PID:g222369 CLASSIFICATION #superfamily bovine papillomavirus type 4 L3 protein KEYWORDS late protein SUMMARY #length 113 #molecular-weight 12840 #checksum 357 SEQUENCE /// ENTRY W1WLE #type complete TITLE E1 protein - human papillomavirus type 1a ORGANISM #formal_name human papillomavirus type 1a DATE 18-Aug-1982 #sequence_revision 14-Nov-1983 #text_change 24-Feb-1994 ACCESSIONS A03655 REFERENCE A92993 !$#authors Danos, O.; Engel, L.W.; Chen, E.Y.; Yaniv, M.; Howley, P.M. !$#journal J. Virol. (1983) 46:557-566 !$#title Comparative analysis of the human type 1a and bovine type 1 !1papillomavirus genomes. !$#cross-references MUID:83189357; PMID:6302319 !$#accession A03655 !'##molecule_type DNA !'##residues 1-612 ##label DAN !'##note the authors translated the codon TCA for residue 274 as Arg, !1CCT for residue 279 as Ala, GAA for residue 362 as Ala, CTG !1for residue 476 as Ala, and GCT for residue 477 as Leu CLASSIFICATION #superfamily papillomavirus E1 protein KEYWORDS early protein SUMMARY #length 612 #molecular-weight 69955 #checksum 5251 SEQUENCE /// ENTRY W1WL8 #type complete TITLE E1 protein - human papillomavirus type 8 ORGANISM #formal_name human papillomavirus type 8 DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 07-Nov-1997 ACCESSIONS A03656 REFERENCE A93019 !$#authors Fuchs, P.G.; Iftner, T.; Weninger, J.; Pfister, H. !$#journal J. Virol. (1986) 58:626-634 !$#title Epidermodysplasia verruciformis-associated human !1papillomavirus 8: genomic sequence and comparative analysis. !$#cross-references MUID:86200410; PMID:3009874 !$#accession A03656 !'##molecule_type DNA !'##residues 1-603 ##label FUC !'##cross-references GB:M12737; NID:g333074 !'##note this ORF is not annotated in GenBank entry PPH8CG CLASSIFICATION #superfamily papillomavirus E1 protein KEYWORDS early protein SUMMARY #length 603 #molecular-weight 68821 #checksum 9854 SEQUENCE /// ENTRY W1WL5 #type complete TITLE E1 protein - human papillomavirus type 5 ORGANISM #formal_name human papillomavirus type 5 DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 24-Feb-1994 ACCESSIONS C26277 REFERENCE A94360 !$#authors Zachow, K.R.; Ostrow, R.S.; Faras, A.J. !$#journal Virology (1987) 158:251-254 !$#title Nucleotide sequence and genome organization of human !1papillomavirus type 5. !$#cross-references MUID:87207670; PMID:3033892 !$#accession C26277 !'##molecule_type DNA !'##residues 1-606 ##label ZAC CLASSIFICATION #superfamily papillomavirus E1 protein KEYWORDS early protein SUMMARY #length 606 #molecular-weight 69164 #checksum 7458 SEQUENCE /// ENTRY W1WLB5 #type complete TITLE E1 protein - human papillomavirus type 5b ORGANISM #formal_name human papillomavirus type 5b #note host Homo sapiens (man) DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jun-2000 ACCESSIONS A40480 REFERENCE A40480 !$#authors Yabe, Y.; Sakai, A.; Hitsumoto, T.; Kato, H.; Ogura, H. !$#journal Virology (1991) 183:793-798 !$#title A subtype of human papillomavirus 5 (HPV-5b) and its !1subgenomic segment amplified in a carcinoma: nucleotide !1sequences and genomic organizations. !$#cross-references MUID:91306467; PMID:1649510 !$#accession A40480 !'##status translation not shown !'##molecule_type DNA !'##residues 1-606 ##label YAB !'##cross-references GB:D90252; NID:g222395; PIDN:BAA14294.1; !1PID:g222400 CLASSIFICATION #superfamily papillomavirus E1 protein KEYWORDS early protein SUMMARY #length 606 #molecular-weight 69126 #checksum 7824 SEQUENCE /// ENTRY W1WL47 #type complete TITLE E1 protein - human papillomavirus type 47 ORGANISM #formal_name human papillomavirus type 47 #note host Homo sapiens (man) DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Jul-1999 ACCESSIONS C35324 REFERENCE A35324 !$#authors Kiyono, T.; Adachi, A.; Ishibashi, M. !$#journal Virology (1990) 177:401-405 !$#title Genome organization and taxonomic position of human !1papillomavirus type 47 inferred from its DNA sequence. !$#cross-references MUID:90281611; PMID:2162112 !$#accession C35324 !'##status translation not shown !'##molecule_type DNA !'##residues 1-605 ##label KIY !'##cross-references GB:M32305; NID:g333062; PIDN:AAA46978.1; !1PID:g333066 CLASSIFICATION #superfamily papillomavirus E1 protein KEYWORDS early protein SUMMARY #length 605 #molecular-weight 69185 #checksum 5901 SEQUENCE /// ENTRY W1WLB4 #type complete TITLE E1 protein - bovine papillomavirus type 4 ORGANISM #formal_name bovine papillomavirus type 4 DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jun-2000 ACCESSIONS D27129 REFERENCE A92795 !$#authors Patel, K.R.; Smith, K.T.; Campo, M.S. !$#journal J. Gen. Virol. (1987) 68:2117-2128 !$#title The nucleotide sequence and genome organization of bovine !1papillomavirus type 4. !$#cross-references MUID:87282264; PMID:3039043 !$#accession D27129 !'##molecule_type DNA !'##residues 1-405 ##label PAT !'##cross-references GB:D00146; NID:g222360; PIDN:BAA00096.1; !1PID:g222363 CLASSIFICATION #superfamily papillomavirus E1 protein KEYWORDS early protein SUMMARY #length 405 #molecular-weight 47174 #checksum 1040 SEQUENCE /// ENTRY W1WLRB #type complete TITLE E1 protein - cottontail rabbit papillomavirus ORGANISM #formal_name cottontail rabbit papillomavirus DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 24-Feb-1994 ACCESSIONS A03657 REFERENCE A94027 !$#authors Giri, I.; Danos, O.; Yaniv, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:1580-1584 !$#title Genomic structure of the cottontail rabbit (Shope) !1papillomavirus. !$#cross-references MUID:85166175; PMID:2984661 !$#accession A03657 !'##molecule_type DNA !'##residues 1-602 ##label GIR CLASSIFICATION #superfamily papillomavirus E1 protein KEYWORDS early protein SUMMARY #length 602 #molecular-weight 67943 #checksum 4676 SEQUENCE /// ENTRY W1WL6 #type complete TITLE E1 protein - human papillomavirus type 6b ORGANISM #formal_name human papillomavirus type 6b DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 16-Jul-1999 ACCESSIONS A03658 REFERENCE A90975 !$#authors Schwarz, E.; Durst, M.; Demankowski, C.; Lattermann, O.; !1Zech, R.; Wolfsperger, E.; Suhai, S.; zur Hausen, H. !$#journal EMBO J. (1983) 2:2341-2348 !$#title DNA sequence and genome organization of genital human !1papillomavirus type 6b. !$#cross-references MUID:84131949; PMID:6321162 !$#accession A03658 !'##molecule_type DNA !'##residues 1-649 ##label SCH !'##cross-references GB:X00203; NID:g60955; PIDN:CAA25020.1; PID:g60958 CLASSIFICATION #superfamily papillomavirus E1 protein KEYWORDS early protein SUMMARY #length 649 #molecular-weight 73265 #checksum 1933 SEQUENCE /// ENTRY W1WL11 #type complete TITLE E1 protein - human papillomavirus type 11 ORGANISM #formal_name human papillomavirus type 11 DATE 13-Aug-1986 #sequence_revision 13-Aug-1986 #text_change 16-Jul-1999 ACCESSIONS A03659 REFERENCE A94338 !$#authors Dartmann, K.; Schwarz, E.; Gissmann, L.; zur Hausen, H. !$#journal Virology (1986) 151:124-130 !$#title The nucleotide sequence and genome organization of human !1papilloma virus type 11. !$#cross-references MUID:86181601; PMID:3008427 !$#accession A03659 !'##molecule_type DNA !'##residues 1-649 ##label DAR !'##cross-references GB:M14119; NID:g333026; PIDN:AAA46929.1; !1PID:g496195 CLASSIFICATION #superfamily papillomavirus E1 protein KEYWORDS early protein SUMMARY #length 649 #molecular-weight 73529 #checksum 1226 SEQUENCE /// ENTRY W1WL13 #type complete TITLE E1 protein - human papillomavirus type 13 ORGANISM #formal_name human papillomavirus type 13 #note host Homo sapiens (man) DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS C42955 REFERENCE A42955 !$#authors van Ranst, M.; Fuse, A.; Fiten, P.; Beuken, E.; Pfister, H.; !1Burk, R.D.; Opdenakker, G. !$#journal Virology (1992) 190:587-596 !$#title Human papillomavirus type 13 and pygmy chimpanzee !1papillomavirus type 1: Comparison of the genome !1organizations. !$#cross-references MUID:92391075; PMID:1325697 !$#accession C42955 !'##molecule_type DNA !'##residues 1-646 ##label VAN !'##cross-references EMBL:X62843; NID:g60295; PIDN:CAA44649.1; !1PID:g60298 CLASSIFICATION #superfamily papillomavirus E1 protein KEYWORDS early protein SUMMARY #length 646 #molecular-weight 73094 #checksum 9316 SEQUENCE /// ENTRY W1WL33 #type complete TITLE E1 protein - human papillomavirus type 33 ORGANISM #formal_name human papillomavirus type 33 DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 16-Jul-1999 ACCESSIONS A03660 REFERENCE A93020 !$#authors Cole, S.T.; Streeck, R.E. !$#journal J. Virol. (1986) 58:991-995 !$#title Genome organization and nucleotide sequence of human !1papillomavirus type 33, which is associated with cervical !1cancer. !$#cross-references MUID:86200464; PMID:3009902 !$#accession A03660 !'##molecule_type DNA !'##residues 1-644 ##label COL !'##cross-references GB:M12732; NID:g333049; PIDN:AAA46960.1; !1PID:g463179 CLASSIFICATION #superfamily papillomavirus E1 protein KEYWORDS early protein SUMMARY #length 644 #molecular-weight 72468 #checksum 1651 SEQUENCE /// ENTRY W1WL58 #type complete TITLE E1 protein - human papillomavirus type 58 ORGANISM #formal_name human papillomavirus type 58 #note host Homo sapiens (man) DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 21-Jul-2000 ACCESSIONS A36779 REFERENCE A36779 !$#authors Kirii, Y.; Iwamoto, S.; Matsukura, T. !$#journal Virology (1991) 185:424-427 !$#title Human papillomavirus type 58 DNA sequence. !$#cross-references MUID:92024102; PMID:1656594 !$#accession A36779 !'##status translation not shown !'##molecule_type DNA !'##residues 1-644 ##label KIR !'##cross-references GB:D90400; NID:g222386; PIDN:BAA31847.1; !1PID:g3337100 CLASSIFICATION #superfamily papillomavirus E1 protein KEYWORDS early protein SUMMARY #length 644 #molecular-weight 72243 #checksum 1887 SEQUENCE /// ENTRY W1WLHS #type complete TITLE E1 protein - human papillomavirus type 16 ORGANISM #formal_name human papillomavirus type 16 DATE 28-May-1986 #sequence_revision 29-Oct-1999 #text_change 21-Jul-2000 ACCESSIONS T10424; A03661 REFERENCE Z17014 !$#authors Kennedy, I.M.; Haddow, J.K.; Clements, J.B. !$#journal J. Virol. (1991) 65:2093-2097 !$#title A negative element in the human poapillomavirus type 16 !1genome acts at the level of late mRNA stability. !$#cross-references MUID:91162763; PMID:1848319 !$#accession T10424 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-649 ##label KEN !'##cross-references EMBL:K02718; NID:g333031; PIDN:AAA46936.1; !1PID:g459912 REFERENCE A22355 !$#authors Seedorf, K.; Krammer, G.; Durst, M.; Suhai, S.; Rowekamp, !1W.G. !$#journal Virology (1985) 145:181-185 !$#title Human papillomavirus type 16 DNA sequence. !$#cross-references MUID:85246220; PMID:2990099 !$#accession A03661 !'##molecule_type DNA !'##residues 144-649 ##label SEE !'##cross-references GB:K02718; NID:g333031 GENETICS !$#gene E1 !$#introns 92/3 CLASSIFICATION #superfamily papillomavirus E1 protein KEYWORDS early protein SUMMARY #length 649 #molecular-weight 72938 #checksum 961 SEQUENCE /// ENTRY W1WL31 #type complete TITLE E1 protein - human papillomavirus type 31 ORGANISM #formal_name human papillomavirus type 31 #note host Homo sapiens (man) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS C32444 REFERENCE A94398 !$#authors Goldsborough, M.D.; DiSilvestre, D.; Temple, G.F.; Lorincz, !1A.T. !$#journal Virology (1989) 171:306-311 !$#title Nucleotide sequence of human papillomavirus type 31: a !1cervical neoplasia-associated virus. !$#cross-references MUID:89299478; PMID:2545036 !$#accession C32444 !'##status translation not shown !'##molecule_type DNA !'##residues 1-629 ##label GOL !'##cross-references GB:J04353; NID:g333048; PIDN:AAA46952.1; !1PID:g459918 CLASSIFICATION #superfamily papillomavirus E1 protein KEYWORDS early protein SUMMARY #length 629 #molecular-weight 71227 #checksum 6172 SEQUENCE /// ENTRY W1WL35 #type complete TITLE E1 protein - human papillomavirus type 35 ORGANISM #formal_name human papillomavirus type 35 #note host Homo sapiens (man) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS A40824 REFERENCE A40824 !$#authors Marich, J.E.; Pontsler, A.V.; Rice, S.M.; McGraw, K.A.; !1Dubensky, T.W. !$#journal Virology (1992) 186:770-776 !$#title The phylogenetic relationship and complete nucleotide !1sequence of human papillomavirus type 35. !$#cross-references MUID:92124753; PMID:1310198 !$#accession A40824 !'##status translation not shown !'##molecule_type DNA !'##residues 1-630 ##label MAR !'##cross-references GB:M74117; NID:g333050; PIDN:AAA46968.1; !1PID:g333053 CLASSIFICATION #superfamily papillomavirus E1 protein KEYWORDS early protein SUMMARY #length 630 #molecular-weight 71827 #checksum 9854 SEQUENCE /// ENTRY W1WL51 #type complete TITLE E1 protein - human papillomavirus type 51 ORGANISM #formal_name human papillomavirus type 51 #note host Homo sapiens (man) DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 27-Jan-1995 ACCESSIONS A40415 REFERENCE A40415 !$#authors Lungu, O.; Crum, C.P.; Silverstein, S.J. !$#journal J. Virol. (1991) 65:4216-4225 !$#title Biologic properties and nucleotide sequence analysis of !1human papillomavirus type 51. !$#cross-references MUID:91303675; PMID:1649326 !$#accession A40415 !'##status translation not shown !'##molecule_type DNA !'##residues 1-634 ##label LUN !'##cross-references GB:M62877 CLASSIFICATION #superfamily papillomavirus E1 protein KEYWORDS early protein SUMMARY #length 634 #molecular-weight 71684 #checksum 6865 SEQUENCE /// ENTRY W1WL18 #type complete TITLE E1 protein - human papillomavirus type 18 ORGANISM #formal_name human papillomavirus type 18 DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Jul-1999 ACCESSIONS C26165; C26251 REFERENCE A91068 !$#authors Seedorf, K.; Oltersdorf, T.; Kraemmer, G.; Roewekamp, W. !$#journal EMBO J. (1987) 6:139-144 !$#title Identification of early proteins of the human papilloma !1viruses type 16 (HPV 16) and type 18 (HPV 18) in cervical !1carcinoma cells. !$#cross-references MUID:87218459; PMID:3034571 !$#accession C26165 !'##molecule_type DNA !'##residues 1-274 ##label SEE !'##cross-references GB:X04773; NID:g60876; PIDN:CAA28468.1; PID:g60879 REFERENCE A92937 !$#authors Cole, S.T.; Danos, O. !$#journal J. Mol. Biol. (1987) 193:599-608 !$#title Nucleotide sequence and comparative analysis of the human !1papillomavirus type 18 genome. Phylogeny of papillomaviruses !1and repeated structure of the E6 and E7 gene products. !$#cross-references MUID:87283882; PMID:3039146 !$#accession C26251 !'##molecule_type DNA !'##residues 1-657 ##label COL !'##cross-references GB:X05015; NID:g60975; PIDN:CAA28666.1; PID:g60978 CLASSIFICATION #superfamily papillomavirus E1 protein KEYWORDS early protein SUMMARY #length 657 #molecular-weight 73736 #checksum 6717 SEQUENCE /// ENTRY W1WL39 #type complete TITLE E1 protein - human papillomavirus type 39 ORGANISM #formal_name human papillomavirus type 39 #note host Homo sapiens (man) DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jul-1999 ACCESSIONS C38502 REFERENCE A38502 !$#authors Volpers, C.; Streeck, R.E. !$#journal Virology (1991) 181:419-423 !$#title Genome organization and nucleotide sequence of human !1papillomavirus type 39. !$#cross-references MUID:91135017; PMID:1847266 !$#accession C38502 !'##status translation not shown !'##molecule_type DNA !'##residues 1-647 ##label VOL !'##cross-references GB:M62849; EMBL:M38185; NID:g333245; !1PIDN:AAA47052.1; PID:g463188 CLASSIFICATION #superfamily papillomavirus E1 protein KEYWORDS early protein SUMMARY #length 647 #molecular-weight 72833 #checksum 3846 SEQUENCE /// ENTRY W1WL42 #type complete TITLE E1 protein - human papillomavirus type 42 ORGANISM #formal_name human papillomavirus type 42 #note host Homo sapiens (man) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 27-Jan-1995 ACCESSIONS A39451 REFERENCE A39451 !$#authors Philipp, W.; Honore, N.; Sapp, M.; Cole, S.T.; Streeck, R.E. !$#journal Virology (1992) 186:331-334 !$#title Human papillomavirus type 42: new sequence, conserved genome !1organization. !$#cross-references MUID:92087479; PMID:1309278 !$#accession A39451 !'##status translation not shown !'##molecule_type DNA !'##residues 1-643 ##label PHI !'##cross-references GB:M73236 CLASSIFICATION #superfamily papillomavirus E1 protein KEYWORDS early protein SUMMARY #length 643 #molecular-weight 72055 #checksum 5858 SEQUENCE /// ENTRY S15616 #type complete TITLE E1 protein - human papillomavirus type 2a ORGANISM #formal_name human papillomavirus type 2a #note host Homo sapiens (man) DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 17-Feb-1994 ACCESSIONS S15616 REFERENCE S15614 !$#authors Hirsch-Behnam, A.; Delius, H.; de Villiers, E.M. !$#journal Virus Res. (1990) 18:81-98 !$#title A comparative sequence analysis of two human papillomavirus !1(HPV) types 2a and 57. !$#cross-references MUID:91188699; PMID:1964523 !$#accession S15616 !'##molecule_type DNA !'##residues 1-643 ##label HIR !'##cross-references EMBL:X55964 CLASSIFICATION #superfamily papillomavirus E1 protein KEYWORDS early protein SUMMARY #length 643 #molecular-weight 72418 #checksum 5111 SEQUENCE /// ENTRY S15623 #type complete TITLE E1 protein - human papillomavirus type 57 ORGANISM #formal_name human papillomavirus type 57 #note host Homo sapiens (man) DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS S15623 REFERENCE S15614 !$#authors Hirsch-Behnam, A.; Delius, H.; de Villiers, E.M. !$#journal Virus Res. (1990) 18:81-98 !$#title A comparative sequence analysis of two human papillomavirus !1(HPV) types 2a and 57. !$#cross-references MUID:91188699; PMID:1964523 !$#accession S15623 !'##molecule_type DNA !'##residues 1-643 ##label HIR !'##cross-references EMBL:X55965; NID:g60882; PIDN:CAA39432.1; !1PID:g60885 CLASSIFICATION #superfamily papillomavirus E1 protein KEYWORDS early protein SUMMARY #length 643 #molecular-weight 72478 #checksum 4906 SEQUENCE /// ENTRY W1WLR1 #type complete TITLE E1 protein - rhesus papillomavirus (type 1) ORGANISM #formal_name rhesus papillomavirus DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 27-Jan-1995 ACCESSIONS C38503 REFERENCE A38503 !$#authors Ostrow, R.S.; LaBresh, K.V.; Faras, A.J. !$#journal Virology (1991) 181:424-429 !$#title Characterization of the complete RhPV 1 genomic sequence and !1an integration locus from a metastatic tumor. !$#cross-references MUID:91135018; PMID:1847267 !$#accession C38503 !'##status translation not shown !'##molecule_type DNA !'##residues 1-625 ##label OST !'##cross-references EMBL:M37717 CLASSIFICATION #superfamily papillomavirus E1 protein KEYWORDS early protein SUMMARY #length 625 #molecular-weight 69720 #checksum 6595 SEQUENCE /// ENTRY W1WLC1 #type complete TITLE E1 protein - pygmy chimpanzee papillomavirus (type 1) ORGANISM #formal_name pygmy chimpanzee papillomavirus DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS C36818 REFERENCE A42955 !$#authors van Ranst, M.; Fuse, A.; Fiten, P.; Beuken, E.; Pfister, H.; !1Burk, R.D.; Opdenakker, G. !$#journal Virology (1992) 190:587-596 !$#title Human papillomavirus type 13 and pygmy chimpanzee !1papillomavirus type 1: Comparison of the genome !1organizations. !$#cross-references MUID:92391075; PMID:1325697 !$#accession C36818 !'##molecule_type DNA !'##residues 1-648 ##label VAN !'##cross-references EMBL:X62844; NID:g61010; PIDN:CAA44657.1; !1PID:g61013 CLASSIFICATION #superfamily papillomavirus E1 protein KEYWORDS early protein SUMMARY #length 648 #molecular-weight 73577 #checksum 6438 SEQUENCE /// ENTRY W1WL41 #type complete TITLE E1 protein - human papillomavirus type 41 ORGANISM #formal_name human papillomavirus type 41 #note host Homo sapiens (man) DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS C43550 REFERENCE A43550 !$#authors Hirt, L.; Hirsch-Behnam, A.; De Villiers, E.M. !$#journal Virus Res. (1990) 18:179-190 !$#title Nucleotide sequence of human papillomavirus (HPV) type 41: !1an unusual HPV type without a typical E2 binding site !1consensus sequence. !$#accession C43550 !'##status translation not shown !'##molecule_type DNA !'##residues 1-614 ##label HIR !'##cross-references EMBL:X56147; NID:g60942; PIDN:CAA39614.1; !1PID:g60945 CLASSIFICATION #superfamily papillomavirus E1 protein KEYWORDS early protein SUMMARY #length 614 #molecular-weight 70338 #checksum 6015 SEQUENCE /// ENTRY W1WLEB #type complete TITLE E1 protein - bovine papillomavirus type 1 ORGANISM #formal_name bovine papillomavirus type 1 DATE 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 28-Jul-2000 ACCESSIONS A03663 REFERENCE A93289 !$#authors Chen, E.Y.; Howley, P.M.; Levinson, A.D.; Seeburg, P.H. !$#journal Nature (1982) 299:529-534 !$#title The primary structure and genetic organization of the bovine !1papillomavirus type 1 genome. !$#cross-references MUID:83012974; PMID:6289124 !$#accession A03663 !'##molecule_type DNA !'##residues 1-605 ##label CHE !'##cross-references GB:X02346; GB:J02044; GB:M24622; GB:X00473; !1NID:g60965; PIDN:CAB46511.1; PID:g5419934 CLASSIFICATION #superfamily papillomavirus E1 protein KEYWORDS early protein SUMMARY #length 605 #molecular-weight 68189 #checksum 9601 SEQUENCE /// ENTRY W1WLB2 #type complete TITLE E1 protein - bovine papillomavirus type 2 ORGANISM #formal_name bovine papillomavirus type 2 DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 12-Jun-1998 ACCESSIONS C31169 REFERENCE A94519 !$#authors Groff, D.E.; Mitra, R.; Lancaster, W.D. !$#submission submitted to GenBank, May 1988 !$#accession C31169 !'##molecule_type DNA !'##residues 1-620 ##label GRO !'##cross-references GB:M20219; GB:M19551; NID:g332996 CLASSIFICATION #superfamily papillomavirus E1 protein KEYWORDS early protein; glycoprotein FEATURE !$72,109,173 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 620 #molecular-weight 69763 #checksum 9194 SEQUENCE /// ENTRY W1WLDP #type complete TITLE E1 protein - deer papillomavirus ORGANISM #formal_name deer papillomavirus #note host Odocoileus virginianus (American white-tailed deer) DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 24-Feb-1994 ACCESSIONS A03664 REFERENCE A93013 !$#authors Groff, D.E.; Lancaster, W.D. !$#journal J. Virol. (1985) 56:85-91 !$#title Molecular cloning and nucleotide sequence of deer !1papillomavirus. !$#cross-references MUID:85293253; PMID:2993669 !$#accession A03664 !'##molecule_type DNA !'##residues 1-613 ##label GRO CLASSIFICATION #superfamily papillomavirus E1 protein KEYWORDS early protein SUMMARY #length 613 #molecular-weight 68062 #checksum 8722 SEQUENCE /// ENTRY W1WLEP #type complete TITLE E1 protein - European elk papillomavirus ORGANISM #formal_name European elk papillomavirus DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 11-May-2000 ACCESSIONS C29499; C94457; C94506 REFERENCE A91567 !$#authors Ahola, H.; Bergman, P.; Stroem, A.C.; Moreno-Lopez, J.; !1Pettersson, U. !$#journal Gene (1986) 50:195-205 !$#title Organization and expression of the transforming region from !1the European elk papillomavirus (EEPV). !$#cross-references MUID:87219878; PMID:3034730 !$#accession C29499 !'##molecule_type DNA !'##residues 1-611 ##label AHO !'##cross-references GB:M15953; NID:g333025; PIDN:AAA66852.1; !1PID:g484018 REFERENCE A94457 !$#authors Eriksson, A. !$#citation unpublished results 1987, cited by GenBank !$#accession C94457 !'##molecule_type DNA !'##residues 1-611 ##label ERI !'##cross-references GB:M15953; NID:g333025; PIDN:AAA66852.1; !1PID:g484018 REFERENCE A94506 !$#authors Pettersson, U. !$#submission submitted to GenBank, August 1987 !$#accession C94506 !'##molecule_type DNA !'##residues 1-611 ##label PET !'##cross-references GB:M15953; NID:g333025; PIDN:AAA66852.1; !1PID:g484018 CLASSIFICATION #superfamily papillomavirus E1 protein KEYWORDS early protein SUMMARY #length 611 #molecular-weight 68110 #checksum 918 SEQUENCE /// ENTRY W2WLE #type complete TITLE E2 protein - human papillomavirus type 1a ORGANISM #formal_name human papillomavirus type 1a DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 16-Feb-1997 ACCESSIONS A03665 REFERENCE A90970 !$#authors Danos, O.; Katinka, M.; Yaniv, M. !$#journal EMBO J. (1982) 1:231-236 !$#title Human papillomavirus 1a complete DNA sequence: a novel type !1of genome organization among papovaviridae. !$#cross-references MUID:84182467; PMID:6325156 !$#accession A03665 !'##molecule_type DNA !'##residues 1-322 ##label DAN CLASSIFICATION #superfamily papillomavirus E2 protein KEYWORDS DNA binding; early protein; transcription regulation SUMMARY #length 322 #molecular-weight 36923 #checksum 9041 SEQUENCE /// ENTRY W2WL8 #type complete TITLE E2 protein - human papillomavirus type 8 ORGANISM #formal_name human papillomavirus type 8 DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 07-Nov-1997 ACCESSIONS A03666 REFERENCE A93019 !$#authors Fuchs, P.G.; Iftner, T.; Weninger, J.; Pfister, H. !$#journal J. Virol. (1986) 58:626-634 !$#title Epidermodysplasia verruciformis-associated human !1papillomavirus 8: genomic sequence and comparative analysis. !$#cross-references MUID:86200410; PMID:3009874 !$#accession A03666 !'##molecule_type DNA !'##residues 1-498 ##label FUC !'##cross-references GB:M12737; NID:g333074 !'##note this ORF is not annotated in GenBank entry PPH8CG CLASSIFICATION #superfamily papillomavirus E2 protein KEYWORDS DNA binding; early protein; transcription regulation SUMMARY #length 498 #molecular-weight 56329 #checksum 4521 SEQUENCE /// ENTRY W2WL5 #type complete TITLE E2 protein - human papillomavirus type 5 ORGANISM #formal_name human papillomavirus type 5 DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Feb-1997 ACCESSIONS D26277 REFERENCE A94360 !$#authors Zachow, K.R.; Ostrow, R.S.; Faras, A.J. !$#journal Virology (1987) 158:251-254 !$#title Nucleotide sequence and genome organization of human !1papillomavirus type 5. !$#cross-references MUID:87207670; PMID:3033892 !$#accession D26277 !'##molecule_type DNA !'##residues 1-514 ##label ZAC CLASSIFICATION #superfamily papillomavirus E2 protein KEYWORDS DNA binding; early protein; transcription regulation SUMMARY #length 514 #molecular-weight 57397 #checksum 1027 SEQUENCE /// ENTRY W2WLB5 #type complete TITLE E2 protein - human papillomavirus type 5b ORGANISM #formal_name human papillomavirus type 5b #note host Homo sapiens (man) DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jun-2000 ACCESSIONS B40480 REFERENCE A40480 !$#authors Yabe, Y.; Sakai, A.; Hitsumoto, T.; Kato, H.; Ogura, H. !$#journal Virology (1991) 183:793-798 !$#title A subtype of human papillomavirus 5 (HPV-5b) and its !1subgenomic segment amplified in a carcinoma: nucleotide !1sequences and genomic organizations. !$#cross-references MUID:91306467; PMID:1649510 !$#accession B40480 !'##status translation not shown !'##molecule_type DNA !'##residues 1-514 ##label YAB !'##cross-references GB:D90252; NID:g222395; PIDN:BAA14295.1; !1PID:g222401 CLASSIFICATION #superfamily papillomavirus E2 protein KEYWORDS DNA binding; early protein; transcription regulation SUMMARY #length 514 #molecular-weight 57750 #checksum 2110 SEQUENCE /// ENTRY W2WL47 #type complete TITLE E2 protein - human papillomavirus type 47 ORGANISM #formal_name human papillomavirus type 47 #note host Homo sapiens (man) DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Jul-1999 ACCESSIONS D35324 REFERENCE A35324 !$#authors Kiyono, T.; Adachi, A.; Ishibashi, M. !$#journal Virology (1990) 177:401-405 !$#title Genome organization and taxonomic position of human !1papillomavirus type 47 inferred from its DNA sequence. !$#cross-references MUID:90281611; PMID:2162112 !$#accession D35324 !'##status translation not shown !'##molecule_type DNA !'##residues 1-506 ##label KIY !'##cross-references GB:M32305; NID:g333062; PIDN:AAA46979.1; !1PID:g333067 CLASSIFICATION #superfamily papillomavirus E2 protein KEYWORDS DNA binding; early protein; transcription regulation SUMMARY #length 506 #molecular-weight 57478 #checksum 9705 SEQUENCE /// ENTRY W2WL41 #type complete TITLE E2 protein - human papillomavirus type 41 ORGANISM #formal_name human papillomavirus type 41 #note host Homo sapiens (man) DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Feb-1997 ACCESSIONS D43550 REFERENCE A43550 !$#authors Hirt, L.; Hirsch-Behnam, A.; De Villiers, E.M. !$#journal Virus Res. (1990) 18:179-190 !$#title Nucleotide sequence of human papillomavirus (HPV) type 41: !1an unusual HPV type without a typical E2 binding site !1consensus sequence. !$#accession D43550 !'##status translation not shown !'##molecule_type DNA !'##residues 1-384 ##label HIR !'##cross-references EMBL:X56147 CLASSIFICATION #superfamily papillomavirus E2 protein KEYWORDS DNA binding; early protein; transcription regulation SUMMARY #length 384 #molecular-weight 43883 #checksum 5893 SEQUENCE /// ENTRY W2WL6 #type complete TITLE E2 protein - human papillomavirus type 6b ORGANISM #formal_name human papillomavirus type 6b DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 16-Jul-1999 ACCESSIONS A03667 REFERENCE A90975 !$#authors Schwarz, E.; Durst, M.; Demankowski, C.; Lattermann, O.; !1Zech, R.; Wolfsperger, E.; Suhai, S.; zur Hausen, H. !$#journal EMBO J. (1983) 2:2341-2348 !$#title DNA sequence and genome organization of genital human !1papillomavirus type 6b. !$#cross-references MUID:84131949; PMID:6321162 !$#accession A03667 !'##molecule_type DNA !'##residues 1-368 ##label SCH !'##cross-references GB:X00203; NID:g60955; PIDN:CAA25021.1; PID:g60959 CLASSIFICATION #superfamily papillomavirus E2 protein KEYWORDS DNA binding; early protein; transcription regulation SUMMARY #length 368 #molecular-weight 42155 #checksum 8668 SEQUENCE /// ENTRY W2WLC1 #type complete TITLE E2 protein - pygmy chimpanzee papillomavirus (type 1) ORGANISM #formal_name pygmy chimpanzee papillomavirus DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS D36818 REFERENCE A42955 !$#authors van Ranst, M.; Fuse, A.; Fiten, P.; Beuken, E.; Pfister, H.; !1Burk, R.D.; Opdenakker, G. !$#journal Virology (1992) 190:587-596 !$#title Human papillomavirus type 13 and pygmy chimpanzee !1papillomavirus type 1: Comparison of the genome !1organizations. !$#cross-references MUID:92391075; PMID:1325697 !$#accession D36818 !'##molecule_type DNA !'##residues 1-377 ##label VAN !'##cross-references EMBL:X62844; NID:g61010; PIDN:CAA44658.1; !1PID:g61014 CLASSIFICATION #superfamily papillomavirus E2 protein KEYWORDS DNA binding; early protein; transcription regulation SUMMARY #length 377 #molecular-weight 43264 #checksum 6168 SEQUENCE /// ENTRY W2WL11 #type complete TITLE E2 protein - human papillomavirus type 11 ORGANISM #formal_name human papillomavirus type 11 DATE 13-Aug-1986 #sequence_revision 13-Aug-1986 #text_change 16-Jul-1999 ACCESSIONS A03668 REFERENCE A94338 !$#authors Dartmann, K.; Schwarz, E.; Gissmann, L.; zur Hausen, H. !$#journal Virology (1986) 151:124-130 !$#title The nucleotide sequence and genome organization of human !1papilloma virus type 11. !$#cross-references MUID:86181601; PMID:3008427 !$#accession A03668 !'##molecule_type DNA !'##residues 1-367 ##label DAR !'##cross-references GB:M14119; NID:g333026; PIDN:AAA46930.1; !1PID:g496196 CLASSIFICATION #superfamily papillomavirus E2 protein KEYWORDS DNA binding; early protein; transcription regulation SUMMARY #length 367 #molecular-weight 41709 #checksum 3316 SEQUENCE /// ENTRY W2WL13 #type complete TITLE E2 protein - human papillomavirus type 13 ORGANISM #formal_name human papillomavirus type 13 #note host Homo sapiens (man) DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS D42955 REFERENCE A42955 !$#authors van Ranst, M.; Fuse, A.; Fiten, P.; Beuken, E.; Pfister, H.; !1Burk, R.D.; Opdenakker, G. !$#journal Virology (1992) 190:587-596 !$#title Human papillomavirus type 13 and pygmy chimpanzee !1papillomavirus type 1: Comparison of the genome !1organizations. !$#cross-references MUID:92391075; PMID:1325697 !$#accession D42955 !'##molecule_type DNA !'##residues 1-377 ##label VAN !'##cross-references EMBL:X62843; NID:g60295; PIDN:CAA44650.1; !1PID:g60299 CLASSIFICATION #superfamily papillomavirus E2 protein KEYWORDS DNA binding; early protein; transcription regulation SUMMARY #length 377 #molecular-weight 43101 #checksum 6447 SEQUENCE /// ENTRY W2WL42 #type complete TITLE E2 protein - human papillomavirus type 42 ORGANISM #formal_name human papillomavirus type 42 #note host Homo sapiens (man) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Feb-1997 ACCESSIONS B39451 REFERENCE A39451 !$#authors Philipp, W.; Honore, N.; Sapp, M.; Cole, S.T.; Streeck, R.E. !$#journal Virology (1992) 186:331-334 !$#title Human papillomavirus type 42: new sequence, conserved genome !1organization. !$#cross-references MUID:92087479; PMID:1309278 !$#accession B39451 !'##status translation not shown !'##molecule_type DNA !'##residues 1-398 ##label PHI !'##cross-references GB:M73236 CLASSIFICATION #superfamily papillomavirus E2 protein KEYWORDS DNA binding; early protein; transcription regulation SUMMARY #length 398 #molecular-weight 45309 #checksum 6881 SEQUENCE /// ENTRY W2WLHS #type complete TITLE E2 protein - human papillomavirus type 16 ORGANISM #formal_name human papillomavirus type 16 DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 20-Aug-1999 ACCESSIONS A03669; T10429 REFERENCE A22355 !$#authors Seedorf, K.; Krammer, G.; Durst, M.; Suhai, S.; Rowekamp, !1W.G. !$#journal Virology (1985) 145:181-185 !$#title Human papillomavirus type 16 DNA sequence. !$#cross-references MUID:85246220; PMID:2990099 !$#accession A03669 !'##molecule_type DNA !'##residues 1-365 ##label SEE !'##cross-references GB:K02718; NID:g333031; PIDN:AAA46941.1; !1PID:g333035 REFERENCE Z17014 !$#authors Kennedy, I.M.; Haddow, J.K.; Clements, J.B. !$#journal J. Virol. (1991) 65:2093-2097 !$#title A negative element in the human poapillomavirus type 16 !1genome acts at the level of late mRNA stability. !$#cross-references MUID:91162763; PMID:1848319 !$#accession T10429 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-365 ##label KEN !'##cross-references EMBL:K02718; NID:g333031; PIDN:AAA46941.1; !1PID:g333035 GENETICS !$#gene E2 CLASSIFICATION #superfamily papillomavirus E2 protein KEYWORDS DNA binding; early protein; transcription regulation SUMMARY #length 365 #molecular-weight 41825 #checksum 5899 SEQUENCE /// ENTRY W2WL31 #type complete TITLE E2 protein - human papillomavirus type 31 ORGANISM #formal_name human papillomavirus type 31 #note host Homo sapiens (man) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS D32444 REFERENCE A94398 !$#authors Goldsborough, M.D.; DiSilvestre, D.; Temple, G.F.; Lorincz, !1A.T. !$#journal Virology (1989) 171:306-311 !$#title Nucleotide sequence of human papillomavirus type 31: a !1cervical neoplasia-associated virus. !$#cross-references MUID:89299478; PMID:2545036 !$#accession D32444 !'##status translation not shown !'##molecule_type DNA !'##residues 1-372 ##label GOL !'##cross-references GB:J04353; NID:g333048; PIDN:AAA46953.1; !1PID:g459919 CLASSIFICATION #superfamily papillomavirus E2 protein KEYWORDS DNA binding; early protein; transcription regulation SUMMARY #length 372 #molecular-weight 42104 #checksum 9656 SEQUENCE /// ENTRY W2WL35 #type complete TITLE E2 protein - human papillomavirus type 35 ORGANISM #formal_name human papillomavirus type 35 #note host Homo sapiens (man) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS B40824 REFERENCE A40824 !$#authors Marich, J.E.; Pontsler, A.V.; Rice, S.M.; McGraw, K.A.; !1Dubensky, T.W. !$#journal Virology (1992) 186:770-776 !$#title The phylogenetic relationship and complete nucleotide !1sequence of human papillomavirus type 35. !$#cross-references MUID:92124753; PMID:1310198 !$#accession B40824 !'##status translation not shown !'##molecule_type DNA !'##residues 1-367 ##label MAR !'##cross-references GB:M74117; NID:g333050; PIDN:AAA46969.1; !1PID:g333054 CLASSIFICATION #superfamily papillomavirus E2 protein KEYWORDS DNA binding; early protein; transcription regulation SUMMARY #length 367 #molecular-weight 41978 #checksum 5911 SEQUENCE /// ENTRY W2WL33 #type complete TITLE E2 protein - human papillomavirus type 33 ORGANISM #formal_name human papillomavirus type 33 DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 16-Jul-1999 ACCESSIONS A03670 REFERENCE A93020 !$#authors Cole, S.T.; Streeck, R.E. !$#journal J. Virol. (1986) 58:991-995 !$#title Genome organization and nucleotide sequence of human !1papillomavirus type 33, which is associated with cervical !1cancer. !$#cross-references MUID:86200464; PMID:3009902 !$#accession A03670 !'##molecule_type DNA !'##residues 1-353 ##label COL !'##cross-references GB:M12732; NID:g333049; PIDN:AAA46961.1; !1PID:g463180 CLASSIFICATION #superfamily papillomavirus E2 protein KEYWORDS DNA binding; early protein; transcription regulation SUMMARY #length 353 #molecular-weight 40253 #checksum 139 SEQUENCE /// ENTRY W2WL58 #type complete TITLE E2 protein - human papillomavirus type 58 ORGANISM #formal_name human papillomavirus type 58 #note host Homo sapiens (man) DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 21-Jul-2000 ACCESSIONS B36779 REFERENCE A36779 !$#authors Kirii, Y.; Iwamoto, S.; Matsukura, T. !$#journal Virology (1991) 185:424-427 !$#title Human papillomavirus type 58 DNA sequence. !$#cross-references MUID:92024102; PMID:1656594 !$#accession B36779 !'##status translation not shown !'##molecule_type DNA !'##residues 1-358 ##label KIR !'##cross-references GB:D90400; NID:g222386; PIDN:BAA31848.1; !1PID:g3337101 CLASSIFICATION #superfamily papillomavirus E2 protein KEYWORDS DNA binding; early protein; transcription regulation SUMMARY #length 358 #molecular-weight 40781 #checksum 9187 SEQUENCE /// ENTRY W2WL51 #type complete TITLE E2 protein - human papillomavirus type 51 ORGANISM #formal_name human papillomavirus type 51 #note host Homo sapiens (man) DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Feb-1997 ACCESSIONS B40415 REFERENCE A40415 !$#authors Lungu, O.; Crum, C.P.; Silverstein, S.J. !$#journal J. Virol. (1991) 65:4216-4225 !$#title Biologic properties and nucleotide sequence analysis of !1human papillomavirus type 51. !$#cross-references MUID:91303675; PMID:1649326 !$#accession B40415 !'##status translation not shown !'##molecule_type DNA !'##residues 1-358 ##label LUN !'##cross-references GB:M62877 CLASSIFICATION #superfamily papillomavirus E2 protein KEYWORDS DNA binding; early protein; transcription regulation SUMMARY #length 358 #molecular-weight 40908 #checksum 1816 SEQUENCE /// ENTRY W2WL18 #type complete TITLE E2 protein - human papillomavirus type 18 ORGANISM #formal_name human papillomavirus type 18 DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Jul-1999 ACCESSIONS D26251; S35634 REFERENCE A92937 !$#authors Cole, S.T.; Danos, O. !$#journal J. Mol. Biol. (1987) 193:599-608 !$#title Nucleotide sequence and comparative analysis of the human !1papillomavirus type 18 genome. Phylogeny of papillomaviruses !1and repeated structure of the E6 and E7 gene products. !$#cross-references MUID:87283882; PMID:3039146 !$#accession D26251 !'##molecule_type DNA !'##residues 1-365 ##label COL !'##cross-references GB:X05015; NID:g60975; PIDN:CAA28667.1; PID:g60979 REFERENCE S35634 !$#authors Meissner, J. !$#journal Nucleic Acids Res. (1993) 21:1041 !$#title TaqI is a single cut enzyme for HPV-18. !$#cross-references MUID:93197132; PMID:8383836 !$#accession S35634 !'##molecule_type DNA !'##residues 84-89,'A',91-93 ##label MEI !'##cross-references EMBL:L07917 CLASSIFICATION #superfamily papillomavirus E2 protein KEYWORDS DNA binding; early protein; transcription regulation SUMMARY #length 365 #molecular-weight 41379 #checksum 5567 SEQUENCE /// ENTRY W2WL39 #type complete TITLE E2 protein - human papillomavirus type 39 ORGANISM #formal_name human papillomavirus type 39 #note host Homo sapiens (man) DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jul-1999 ACCESSIONS D38502 REFERENCE A38502 !$#authors Volpers, C.; Streeck, R.E. !$#journal Virology (1991) 181:419-423 !$#title Genome organization and nucleotide sequence of human !1papillomavirus type 39. !$#cross-references MUID:91135017; PMID:1847266 !$#accession D38502 !'##status translation not shown !'##molecule_type DNA !'##residues 1-370 ##label VOL !'##cross-references GB:M62849; EMBL:M38185; NID:g333245; !1PIDN:AAA47053.1; PID:g463189 CLASSIFICATION #superfamily papillomavirus E2 protein KEYWORDS DNA binding; early protein; transcription regulation SUMMARY #length 370 #molecular-weight 42697 #checksum 8932 SEQUENCE /// ENTRY S15617 #type complete TITLE E2 protein - human papillomavirus type 2a ORGANISM #formal_name human papillomavirus type 2a #note host Homo sapiens (man) DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Feb-1997 ACCESSIONS S15617 REFERENCE S15614 !$#authors Hirsch-Behnam, A.; Delius, H.; de Villiers, E.M. !$#journal Virus Res. (1990) 18:81-98 !$#title A comparative sequence analysis of two human papillomavirus !1(HPV) types 2a and 57. !$#cross-references MUID:91188699; PMID:1964523 !$#accession S15617 !'##molecule_type DNA !'##residues 1-391 ##label HIR !'##cross-references EMBL:X55964 CLASSIFICATION #superfamily papillomavirus E2 protein KEYWORDS DNA binding; early protein; transcription regulation SUMMARY #length 391 #molecular-weight 43233 #checksum 734 SEQUENCE /// ENTRY S15624 #type complete TITLE E2 protein - human papillomavirus type 57 ORGANISM #formal_name human papillomavirus type 57 #note host Homo sapiens (man) DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS S15624 REFERENCE S15614 !$#authors Hirsch-Behnam, A.; Delius, H.; de Villiers, E.M. !$#journal Virus Res. (1990) 18:81-98 !$#title A comparative sequence analysis of two human papillomavirus !1(HPV) types 2a and 57. !$#cross-references MUID:91188699; PMID:1964523 !$#accession S15624 !'##molecule_type DNA !'##residues 1-383 ##label HIR !'##cross-references EMBL:X55965; NID:g60882; PIDN:CAA39433.1; !1PID:g60886 CLASSIFICATION #superfamily papillomavirus E2 protein KEYWORDS DNA binding; early protein; transcription regulation SUMMARY #length 383 #molecular-weight 42829 #checksum 9230 SEQUENCE /// ENTRY W2WLR1 #type complete TITLE E2 protein - rhesus papillomavirus (type 1) ORGANISM #formal_name rhesus papillomavirus DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Feb-1997 ACCESSIONS D38503 REFERENCE A38503 !$#authors Ostrow, R.S.; LaBresh, K.V.; Faras, A.J. !$#journal Virology (1991) 181:424-429 !$#title Characterization of the complete RhPV 1 genomic sequence and !1an integration locus from a metastatic tumor. !$#cross-references MUID:91135018; PMID:1847267 !$#accession D38503 !'##status translation not shown !'##molecule_type DNA !'##residues 1-366 ##label OST !'##cross-references EMBL:M37717 CLASSIFICATION #superfamily papillomavirus E2 protein KEYWORDS DNA binding; early protein; transcription regulation SUMMARY #length 366 #molecular-weight 41025 #checksum 2719 SEQUENCE /// ENTRY W2WLRB #type complete TITLE E2 protein - cottontail rabbit papillomavirus ORGANISM #formal_name cottontail rabbit papillomavirus DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 24-Feb-1994 ACCESSIONS A03671 REFERENCE A94027 !$#authors Giri, I.; Danos, O.; Yaniv, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:1580-1584 !$#title Genomic structure of the cottontail rabbit (Shope) !1papillomavirus. !$#cross-references MUID:85166175; PMID:2984661 !$#accession A03671 !'##molecule_type DNA !'##residues 1-390 ##label GIR CLASSIFICATION #superfamily papillomavirus E2 protein KEYWORDS early protein SUMMARY #length 390 #molecular-weight 44024 #checksum 7234 SEQUENCE /// ENTRY W2WLEB #type complete TITLE E2 protein - bovine papillomavirus type 1 ORGANISM #formal_name bovine papillomavirus type 1 DATE 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 28-Jul-2000 ACCESSIONS A03672 REFERENCE A93289 !$#authors Chen, E.Y.; Howley, P.M.; Levinson, A.D.; Seeburg, P.H. !$#journal Nature (1982) 299:529-534 !$#title The primary structure and genetic organization of the bovine !1papillomavirus type 1 genome. !$#cross-references MUID:83012974; PMID:6289124 !$#accession A03672 !'##molecule_type DNA !'##residues 1-306 ##label CHE !'##cross-references GB:X02346; GB:J02044; GB:M24622; GB:X00473; !1NID:g60965; PIDN:CAB46512.1; PID:g5419935 CLASSIFICATION #superfamily papillomavirus E2 protein KEYWORDS DNA binding; early protein; transcription regulation SUMMARY #length 306 #molecular-weight 34307 #checksum 1656 SEQUENCE /// ENTRY W2WLB2 #type complete TITLE E2 protein - bovine papillomavirus type 2 ORGANISM #formal_name bovine papillomavirus type 2 DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 12-Jun-1998 ACCESSIONS D31169 REFERENCE A94519 !$#authors Groff, D.E.; Mitra, R.; Lancaster, W.D. !$#submission submitted to GenBank, May 1988 !$#accession D31169 !'##molecule_type DNA !'##residues 1-422 ##label GRO !'##cross-references GB:M20219; GB:M19551; NID:g332996 CLASSIFICATION #superfamily papillomavirus E2 protein KEYWORDS DNA binding; early protein; glycoprotein; transcription !1regulation FEATURE !$135,367,412 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 422 #molecular-weight 46877 #checksum 6025 SEQUENCE /// ENTRY W2WLB4 #type complete TITLE E2 protein - bovine papillomavirus type 4 ORGANISM #formal_name bovine papillomavirus type 4 DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jun-2000 ACCESSIONS F27129 REFERENCE A92795 !$#authors Patel, K.R.; Smith, K.T.; Campo, M.S. !$#journal J. Gen. Virol. (1987) 68:2117-2128 !$#title The nucleotide sequence and genome organization of bovine !1papillomavirus type 4. !$#cross-references MUID:87282264; PMID:3039043 !$#accession F27129 !'##molecule_type DNA !'##residues 1-334 ##label PAT !'##cross-references GB:D00146; NID:g222360; PIDN:BAA00098.1; !1PID:g222365 CLASSIFICATION #superfamily papillomavirus E2 protein KEYWORDS DNA binding; early protein; transcription regulation SUMMARY #length 334 #molecular-weight 37203 #checksum 5374 SEQUENCE /// ENTRY W2WLDP #type complete TITLE E2 protein - deer papillomavirus ORGANISM #formal_name deer papillomavirus #note host Odocoileus virginianus (American white-tailed deer) DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 24-Feb-1994 ACCESSIONS A03673 REFERENCE A93013 !$#authors Groff, D.E.; Lancaster, W.D. !$#journal J. Virol. (1985) 56:85-91 !$#title Molecular cloning and nucleotide sequence of deer !1papillomavirus. !$#cross-references MUID:85293253; PMID:2993669 !$#accession A03673 !'##molecule_type DNA !'##residues 1-416 ##label GRO CLASSIFICATION #superfamily papillomavirus E2 protein KEYWORDS early protein SUMMARY #length 416 #molecular-weight 46298 #checksum 5997 SEQUENCE /// ENTRY W2WLEP #type complete TITLE E2 protein - European elk papillomavirus ORGANISM #formal_name European elk papillomavirus DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 11-May-2000 ACCESSIONS D29499; D94457; D94506 REFERENCE A91567 !$#authors Ahola, H.; Bergman, P.; Stroem, A.C.; Moreno-Lopez, J.; !1Pettersson, U. !$#journal Gene (1986) 50:195-205 !$#title Organization and expression of the transforming region from !1the European elk papillomavirus (EEPV). !$#cross-references MUID:87219878; PMID:3034730 !$#accession D29499 !'##molecule_type DNA !'##residues 1-415 ##label AHO !'##cross-references GB:M15953; NID:g333025; PIDN:AAA66854.1; !1PID:g484020 REFERENCE A94457 !$#authors Eriksson, A. !$#citation unpublished results 1987, cited by GenBank !$#accession D94457 !'##molecule_type DNA !'##residues 1-415 ##label ERI !'##cross-references GB:M15953; NID:g333025; PIDN:AAA66854.1; !1PID:g484020 REFERENCE A94506 !$#authors Pettersson, U. !$#submission submitted to GenBank, August 1987 !$#accession D94506 !'##molecule_type DNA !'##residues 1-415 ##label PET !'##cross-references GB:M15953; NID:g333025; PIDN:AAA66854.1; !1PID:g484020 CLASSIFICATION #superfamily papillomavirus E2 protein KEYWORDS early protein SUMMARY #length 415 #molecular-weight 46245 #checksum 5938 SEQUENCE /// ENTRY W3WLB2 #type complete TITLE E3 protein - bovine papillomavirus type 2 ORGANISM #formal_name bovine papillomavirus type 2 DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 16-Jul-1999 ACCESSIONS E31169 REFERENCE A94519 !$#authors Groff, D.E.; Mitra, R.; Lancaster, W.D. !$#submission submitted to GenBank, May 1988 !$#accession E31169 !'##molecule_type DNA !'##residues 1-95 ##label GRO !'##cross-references GB:M20219; GB:M19551; NID:g332996; PIDN:AAA66837.1; !1PID:g808784 CLASSIFICATION #superfamily bovine papillomavirus type 2 E3 protein KEYWORDS early protein SUMMARY #length 95 #molecular-weight 10158 #checksum 2410 SEQUENCE /// ENTRY W3WLB4 #type complete TITLE E3 protein - bovine papillomavirus type 4 ORGANISM #formal_name bovine papillomavirus type 4 DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jun-2000 ACCESSIONS E27129 REFERENCE A92795 !$#authors Patel, K.R.; Smith, K.T.; Campo, M.S. !$#journal J. Gen. Virol. (1987) 68:2117-2128 !$#title The nucleotide sequence and genome organization of bovine !1papillomavirus type 4. !$#cross-references MUID:87282264; PMID:3039043 !$#accession E27129 !'##molecule_type DNA !'##residues 1-98 ##label PAT !'##cross-references GB:D00146; NID:g222360; PIDN:BAA00097.1; !1PID:g222364 CLASSIFICATION #superfamily bovine papillomavirus type 4 E3 protein KEYWORDS early protein SUMMARY #length 98 #molecular-weight 11720 #checksum 5313 SEQUENCE /// ENTRY W4WL6 #type complete TITLE E4 protein - human papillomavirus type 6b ORGANISM #formal_name human papillomavirus type 6b DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Jul-1999 ACCESSIONS C20558 REFERENCE A90975 !$#authors Schwarz, E.; Durst, M.; Demankowski, C.; Lattermann, O.; !1Zech, R.; Wolfsperger, E.; Suhai, S.; zur Hausen, H. !$#journal EMBO J. (1983) 2:2341-2348 !$#title DNA sequence and genome organization of genital human !1papillomavirus type 6b. !$#cross-references MUID:84131949; PMID:6321162 !$#accession C20558 !'##molecule_type DNA !'##residues 1-109 ##label SCH !'##cross-references GB:X00203; NID:g60955; PIDN:CAA25022.1; PID:g60960 CLASSIFICATION #superfamily papillomavirus E4 protein KEYWORDS early protein SUMMARY #length 109 #molecular-weight 12214 #checksum 7869 SEQUENCE /// ENTRY W4WL11 #type complete TITLE E4 protein - human papillomavirus type 11 ORGANISM #formal_name human papillomavirus type 11 DATE 13-Aug-1986 #sequence_revision 13-Aug-1986 #text_change 16-Jul-1999 ACCESSIONS A03675 REFERENCE A94338 !$#authors Dartmann, K.; Schwarz, E.; Gissmann, L.; zur Hausen, H. !$#journal Virology (1986) 151:124-130 !$#title The nucleotide sequence and genome organization of human !1papilloma virus type 11. !$#cross-references MUID:86181601; PMID:3008427 !$#accession A03675 !'##molecule_type DNA !'##residues 1-108 ##label DAR !'##cross-references GB:M14119; NID:g333026; PIDN:AAA46931.1; !1PID:g496197 CLASSIFICATION #superfamily papillomavirus E4 protein KEYWORDS early protein SUMMARY #length 108 #molecular-weight 12144 #checksum 4415 SEQUENCE /// ENTRY W4WL13 #type complete TITLE E4 protein - human papillomavirus type 13 ORGANISM #formal_name human papillomavirus type 13 #note host Homo sapiens (man) DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS E42955 REFERENCE A42955 !$#authors van Ranst, M.; Fuse, A.; Fiten, P.; Beuken, E.; Pfister, H.; !1Burk, R.D.; Opdenakker, G. !$#journal Virology (1992) 190:587-596 !$#title Human papillomavirus type 13 and pygmy chimpanzee !1papillomavirus type 1: Comparison of the genome !1organizations. !$#cross-references MUID:92391075; PMID:1325697 !$#accession E42955 !'##molecule_type DNA !'##residues 1-118 ##label VAN !'##cross-references EMBL:X62843; NID:g60295; PIDN:CAA44651.1; !1PID:g60300 CLASSIFICATION #superfamily papillomavirus E4 protein KEYWORDS early protein SUMMARY #length 118 #molecular-weight 13275 #checksum 2225 SEQUENCE /// ENTRY W4WLC1 #type complete TITLE E4 protein - pygmy chimpanzee papillomavirus (type 1) ORGANISM #formal_name pygmy chimpanzee papillomavirus DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS E36818 REFERENCE A42955 !$#authors van Ranst, M.; Fuse, A.; Fiten, P.; Beuken, E.; Pfister, H.; !1Burk, R.D.; Opdenakker, G. !$#journal Virology (1992) 190:587-596 !$#title Human papillomavirus type 13 and pygmy chimpanzee !1papillomavirus type 1: Comparison of the genome !1organizations. !$#cross-references MUID:92391075; PMID:1325697 !$#accession E36818 !'##molecule_type DNA !'##residues 1-108 ##label VAN !'##cross-references EMBL:X62844; NID:g61010; PIDN:CAA44659.1; !1PID:g61015 CLASSIFICATION #superfamily papillomavirus E4 protein KEYWORDS early protein SUMMARY #length 108 #molecular-weight 12062 #checksum 4251 SEQUENCE /// ENTRY W4WL42 #type complete TITLE E4 protein - human papillomavirus type 42 ORGANISM #formal_name human papillomavirus type 42 #note host Homo sapiens (man) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS C39451 REFERENCE A39451 !$#authors Philipp, W.; Honore, N.; Sapp, M.; Cole, S.T.; Streeck, R.E. !$#journal Virology (1992) 186:331-334 !$#title Human papillomavirus type 42: new sequence, conserved genome !1organization. !$#cross-references MUID:92087479; PMID:1309278 !$#accession C39451 !'##status translation not shown !'##molecule_type DNA !'##residues 1-120 ##label PHI !'##cross-references GB:M73236; NID:g333211; PIDN:AAA47045.1; !1PID:g333216 CLASSIFICATION #superfamily papillomavirus E4 protein KEYWORDS early protein SUMMARY #length 120 #molecular-weight 13419 #checksum 2169 SEQUENCE /// ENTRY W4WL18 #type complete TITLE E4 protein - human papillomavirus type 18 ORGANISM #formal_name human papillomavirus type 18 DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Jul-1999 ACCESSIONS E26251 REFERENCE A92937 !$#authors Cole, S.T.; Danos, O. !$#journal J. Mol. Biol. (1987) 193:599-608 !$#title Nucleotide sequence and comparative analysis of the human !1papillomavirus type 18 genome. Phylogeny of papillomaviruses !1and repeated structure of the E6 and E7 gene products. !$#cross-references MUID:87283882; PMID:3039146 !$#accession E26251 !'##molecule_type DNA !'##residues 1-88 ##label COL !'##cross-references GB:X05015; NID:g60975; PIDN:CAA28668.1; PID:g60980 CLASSIFICATION #superfamily papillomavirus E4 protein KEYWORDS early protein SUMMARY #length 88 #molecular-weight 9857 #checksum 8473 SEQUENCE /// ENTRY W4WL39 #type complete TITLE E4 protein - human papillomavirus type 39 ORGANISM #formal_name human papillomavirus type 39 #note host Homo sapiens (man) DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 27-Jan-1995 ACCESSIONS E38502 REFERENCE A38502 !$#authors Volpers, C.; Streeck, R.E. !$#journal Virology (1991) 181:419-423 !$#title Genome organization and nucleotide sequence of human !1papillomavirus type 39. !$#cross-references MUID:91135017; PMID:1847266 !$#accession E38502 !'##status translation not shown !'##molecule_type DNA !'##residues 1-94 ##label VOL !'##cross-references EMBL:M38185 CLASSIFICATION #superfamily papillomavirus E4 protein KEYWORDS early protein SUMMARY #length 94 #molecular-weight 10441 #checksum 6508 SEQUENCE /// ENTRY W4WL51 #type complete TITLE E4 protein - human papillomavirus type 51 ORGANISM #formal_name human papillomavirus type 51 #note host Homo sapiens (man) DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 27-Jan-1995 ACCESSIONS C40415 REFERENCE A40415 !$#authors Lungu, O.; Crum, C.P.; Silverstein, S.J. !$#journal J. Virol. (1991) 65:4216-4225 !$#title Biologic properties and nucleotide sequence analysis of !1human papillomavirus type 51. !$#cross-references MUID:91303675; PMID:1649326 !$#accession C40415 !'##status translation not shown !'##molecule_type DNA !'##residues 1-87 ##label LUN !'##cross-references GB:M62877 CLASSIFICATION #superfamily papillomavirus E4 protein KEYWORDS early protein SUMMARY #length 87 #molecular-weight 9941 #checksum 5330 SEQUENCE /// ENTRY W4WLHS #type complete TITLE E4 protein - human papillomavirus type 16 ORGANISM #formal_name human papillomavirus type 16 DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 20-Aug-1999 ACCESSIONS A22355; T10425 REFERENCE A22355 !$#authors Seedorf, K.; Krammer, G.; Durst, M.; Suhai, S.; Rowekamp, !1W.G. !$#journal Virology (1985) 145:181-185 !$#title Human papillomavirus type 16 DNA sequence. !$#cross-references MUID:85246220; PMID:2990099 !$#accession A22355 !'##molecule_type DNA !'##residues 1-95 ##label SEE !'##cross-references GB:K02718; NID:g333031; PIDN:AAA46937.1; !1PID:g459913 REFERENCE Z17014 !$#authors Kennedy, I.M.; Haddow, J.K.; Clements, J.B. !$#journal J. Virol. (1991) 65:2093-2097 !$#title A negative element in the human poapillomavirus type 16 !1genome acts at the level of late mRNA stability. !$#cross-references MUID:91162763; PMID:1848319 !$#accession T10425 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-95 ##label KEN !'##cross-references EMBL:K02718; NID:g333031; PIDN:AAA46937.1; !1PID:g459913 GENETICS !$#gene E4 CLASSIFICATION #superfamily papillomavirus E4 protein KEYWORDS early protein SUMMARY #length 95 #molecular-weight 10594 #checksum 7625 SEQUENCE /// ENTRY W4WL31 #type complete TITLE E4 protein - human papillomavirus type 31 ORGANISM #formal_name human papillomavirus type 31 #note host Homo sapiens (man) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS E32444 REFERENCE A94398 !$#authors Goldsborough, M.D.; DiSilvestre, D.; Temple, G.F.; Lorincz, !1A.T. !$#journal Virology (1989) 171:306-311 !$#title Nucleotide sequence of human papillomavirus type 31: a !1cervical neoplasia-associated virus. !$#cross-references MUID:89299478; PMID:2545036 !$#accession E32444 !'##status translation not shown !'##molecule_type DNA !'##residues 1-102 ##label GOL !'##cross-references GB:J04353; NID:g333048; PIDN:AAA46949.1; !1PID:g459915 !'##note in GenBank entry PPH31A the initiation codon UUG for residue 1 !1is translated as Leu CLASSIFICATION #superfamily papillomavirus E4 protein KEYWORDS early protein SUMMARY #length 102 #molecular-weight 11284 #checksum 210 SEQUENCE /// ENTRY W4WL35 #type complete TITLE E4 protein - human papillomavirus type 35 ORGANISM #formal_name human papillomavirus type 35 #note host Homo sapiens (man) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 27-Jan-1995 ACCESSIONS C40824 REFERENCE A40824 !$#authors Marich, J.E.; Pontsler, A.V.; Rice, S.M.; McGraw, K.A.; !1Dubensky, T.W. !$#journal Virology (1992) 186:770-776 !$#title The phylogenetic relationship and complete nucleotide !1sequence of human papillomavirus type 35. !$#cross-references MUID:92124753; PMID:1310198 !$#accession C40824 !'##status translation not shown !'##molecule_type DNA !'##residues 1-96 ##label MAR !'##cross-references GB:M74117 CLASSIFICATION #superfamily papillomavirus E4 protein KEYWORDS early protein SUMMARY #length 96 #molecular-weight 10597 #checksum 1173 SEQUENCE /// ENTRY W4WL33 #type complete TITLE E1/E4 protein - human papillomavirus type 33 ORGANISM #formal_name human papillomavirus type 33 DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 29-Oct-1999 ACCESSIONS A03676; S19908; S23828 REFERENCE A93020 !$#authors Cole, S.T.; Streeck, R.E. !$#journal J. Virol. (1986) 58:991-995 !$#title Genome organization and nucleotide sequence of human !1papillomavirus type 33, which is associated with cervical !1cancer. !$#cross-references MUID:86200464; PMID:3009902 !$#accession A03676 !'##molecule_type DNA !'##residues 1-83 ##label COL !'##cross-references GB:M12732; NID:g333049; PIDN:AAA46957.1; !1PID:g463176 REFERENCE S19906 !$#authors Snijders, P.J.F.; van den Brule, A.J.C.; Schrijnemakers, !1H.F.J.; Raaphorst, P.M.C.; Meijer, C.J.L.M.; Walboomers, !1J.M.M. !$#submission submitted to the EMBL Data Library, January 1992 !$#description HPV type 33 in a tonsillar carcinoma generates its putative !1E7 mRNA via two E6 transcript species which are terminated !1at different early region poly (A) sites. !$#accession S19908 !'##molecule_type mRNA !'##residues 'MADPE',9-83 ##label SNI !'##cross-references EMBL:X64086; NID:g60282; PIDN:CAA45437.1; !1PID:g60285 !$#accession S23828 !'##molecule_type mRNA !'##residues 'MADPE',9-83 ##label SNW !'##cross-references EMBL:X64084; NID:g60273; PIDN:CAA45431.1; !1PID:g60277 CLASSIFICATION #superfamily papillomavirus E4 protein KEYWORDS early protein SUMMARY #length 83 #molecular-weight 9463 #checksum 7956 SEQUENCE /// ENTRY W4WL58 #type complete TITLE E4 protein - human papillomavirus type 58 ORGANISM #formal_name human papillomavirus type 58 #note host Homo sapiens (man) DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jun-2000 ACCESSIONS C36779 REFERENCE A36779 !$#authors Kirii, Y.; Iwamoto, S.; Matsukura, T. !$#journal Virology (1991) 185:424-427 !$#title Human papillomavirus type 58 DNA sequence. !$#cross-references MUID:92024102; PMID:1656594 !$#accession C36779 !'##status translation not shown !'##molecule_type DNA !'##residues 1-91 ##label KIR !'##cross-references GB:D90400; NID:g222386; PIDN:BAA14396.1; !1PID:g222390 CLASSIFICATION #superfamily papillomavirus E4 protein KEYWORDS early protein SUMMARY #length 91 #molecular-weight 10386 #checksum 6153 SEQUENCE /// ENTRY W4WLR1 #type complete TITLE E4 protein - rhesus papillomavirus (type 1) ORGANISM #formal_name rhesus papillomavirus DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 27-Jan-1995 ACCESSIONS E38503 REFERENCE A38503 !$#authors Ostrow, R.S.; LaBresh, K.V.; Faras, A.J. !$#journal Virology (1991) 181:424-429 !$#title Characterization of the complete RhPV 1 genomic sequence and !1an integration locus from a metastatic tumor. !$#cross-references MUID:91135018; PMID:1847267 !$#accession E38503 !'##status translation not shown !'##molecule_type DNA !'##residues 1-91 ##label OST !'##cross-references EMBL:M37717 CLASSIFICATION #superfamily papillomavirus E4 protein KEYWORDS early protein SUMMARY #length 91 #molecular-weight 9813 #checksum 5257 SEQUENCE /// ENTRY W4WL #type complete TITLE E4 protein - human papillomavirus type 1a ORGANISM #formal_name human papillomavirus type 1a DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 03-Feb-1994 ACCESSIONS A90970; A17475 REFERENCE A90970 !$#authors Danos, O.; Katinka, M.; Yaniv, M. !$#journal EMBO J. (1982) 1:231-236 !$#title Human papillomavirus 1a complete DNA sequence: a novel type !1of genome organization among papovaviridae. !$#cross-references MUID:84182467; PMID:6325156 !$#accession A90970 !'##molecule_type DNA !'##residues 1-84 ##label DAN REFERENCE A92993 !$#authors Danos, O.; Engel, L.W.; Chen, E.Y.; Yaniv, M.; Howley, P.M. !$#journal J. Virol. (1983) 46:557-566 !$#title Comparative analysis of the human type 1a and bovine type 1 !1papillomavirus genomes. !$#cross-references MUID:83189357; PMID:6302319 !$#contents annotation CLASSIFICATION #superfamily papillomavirus type 1a E4 protein KEYWORDS early protein SUMMARY #length 84 #molecular-weight 9316 #checksum 9155 SEQUENCE /// ENTRY A46315 #type complete TITLE E4 protein - human papillomavirus type 2 ORGANISM #formal_name human papillomavirus type 2 DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS A46315 REFERENCE A46315 !$#authors Doorbar, J.; Coneron, I.; Gallimore, P.H. !$#journal Virology (1989) 172:51-62 !$#title Sequence divergence yet conserved physical characteristics !1among the E4 proteins of cutaneous human papillomaviruses. !$#cross-references MUID:89370332; PMID:2549722 !$#accession A46315 !'##molecule_type DNA !'##residues 1-125 ##label DOO !'##cross-references GB:M28743; NID:g333134; PIDN:AAA47014.1; !1PID:g333135 CLASSIFICATION #superfamily papillomavirus type 2 E4 protein KEYWORDS early protein SUMMARY #length 125 #molecular-weight 13939 #checksum 3442 SEQUENCE /// ENTRY S15618 #type complete TITLE E4 protein - human papillomavirus type 2a ORGANISM #formal_name human papillomavirus type 2a #note host Homo sapiens (man) DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 17-Feb-1994 ACCESSIONS S15618 REFERENCE S15614 !$#authors Hirsch-Behnam, A.; Delius, H.; de Villiers, E.M. !$#journal Virus Res. (1990) 18:81-98 !$#title A comparative sequence analysis of two human papillomavirus !1(HPV) types 2a and 57. !$#cross-references MUID:91188699; PMID:1964523 !$#accession S15618 !'##molecule_type DNA !'##residues 1-132 ##label HIR !'##cross-references EMBL:X55964 CLASSIFICATION #superfamily papillomavirus type 2 E4 protein KEYWORDS early protein SUMMARY #length 132 #molecular-weight 14532 #checksum 4359 SEQUENCE /// ENTRY S15625 #type complete TITLE E4 protein - human papillomavirus type 57 ORGANISM #formal_name human papillomavirus type 57 #note host Homo sapiens (man) DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS S15625 REFERENCE S15614 !$#authors Hirsch-Behnam, A.; Delius, H.; de Villiers, E.M. !$#journal Virus Res. (1990) 18:81-98 !$#title A comparative sequence analysis of two human papillomavirus !1(HPV) types 2a and 57. !$#cross-references MUID:91188699; PMID:1964523 !$#accession S15625 !'##molecule_type DNA !'##residues 1-124 ##label HIR !'##cross-references EMBL:X55965; NID:g60882; PIDN:CAA39434.1; !1PID:g60887 CLASSIFICATION #superfamily papillomavirus type 2 E4 protein KEYWORDS early protein SUMMARY #length 124 #molecular-weight 13424 #checksum 5447 SEQUENCE /// ENTRY B46315 #type complete TITLE E4 protein - human papillomavirus type 4 ORGANISM #formal_name human papillomavirus type 4 DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS B46315 REFERENCE A46315 !$#authors Doorbar, J.; Coneron, I.; Gallimore, P.H. !$#journal Virology (1989) 172:51-62 !$#title Sequence divergence yet conserved physical characteristics !1among the E4 proteins of cutaneous human papillomaviruses. !$#cross-references MUID:89370332; PMID:2549722 !$#accession B46315 !'##molecule_type DNA !'##residues 1-147 ##label DOO !'##cross-references GB:M28744; NID:g333136; PIDN:AAA47015.1; !1PID:g333137 CLASSIFICATION #superfamily papillomavirus type 4 E4 protein KEYWORDS early protein SUMMARY #length 147 #molecular-weight 16854 #checksum 3230 SEQUENCE /// ENTRY W4WL5 #type complete TITLE E4 protein - human papillomavirus type 5 ORGANISM #formal_name human papillomavirus type 5 DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 24-Feb-1994 ACCESSIONS E26277 REFERENCE A94360 !$#authors Zachow, K.R.; Ostrow, R.S.; Faras, A.J. !$#journal Virology (1987) 158:251-254 !$#title Nucleotide sequence and genome organization of human !1papillomavirus type 5. !$#cross-references MUID:87207670; PMID:3033892 !$#accession E26277 !'##molecule_type DNA !'##residues 1-245 ##label ZAC CLASSIFICATION #superfamily papillomavirus type 5 E4 protein KEYWORDS early protein SUMMARY #length 245 #molecular-weight 25879 #checksum 420 SEQUENCE /// ENTRY W4WLB5 #type complete TITLE E4 protein - human papillomavirus type 5b ORGANISM #formal_name human papillomavirus type 5b #note host Homo sapiens (man) DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jun-2000 ACCESSIONS C40480 REFERENCE A40480 !$#authors Yabe, Y.; Sakai, A.; Hitsumoto, T.; Kato, H.; Ogura, H. !$#journal Virology (1991) 183:793-798 !$#title A subtype of human papillomavirus 5 (HPV-5b) and its !1subgenomic segment amplified in a carcinoma: nucleotide !1sequences and genomic organizations. !$#cross-references MUID:91306467; PMID:1649510 !$#accession C40480 !'##status translation not shown !'##molecule_type DNA !'##residues 1-245 ##label YAB !'##cross-references GB:D90252; NID:g222395; PIDN:BAA14296.1; !1PID:g222396 CLASSIFICATION #superfamily papillomavirus type 5 E4 protein KEYWORDS early protein SUMMARY #length 245 #molecular-weight 25622 #checksum 9243 SEQUENCE /// ENTRY W4WL8 #type complete TITLE E4 protein - human papillomavirus type 8 ORGANISM #formal_name human papillomavirus type 8 DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 07-Nov-1997 ACCESSIONS A03677 REFERENCE A93019 !$#authors Fuchs, P.G.; Iftner, T.; Weninger, J.; Pfister, H. !$#journal J. Virol. (1986) 58:626-634 !$#title Epidermodysplasia verruciformis-associated human !1papillomavirus 8: genomic sequence and comparative analysis. !$#cross-references MUID:86200410; PMID:3009874 !$#accession A03677 !'##molecule_type DNA !'##residues 1-229 ##label FUC !'##cross-references GB:M12737; NID:g333074 !'##note this ORF is not annotated in GenBank entry PPH8CG CLASSIFICATION #superfamily papillomavirus type 5 E4 protein KEYWORDS early protein SUMMARY #length 229 #molecular-weight 24205 #checksum 6837 SEQUENCE /// ENTRY W4WL47 #type complete TITLE E4 protein - human papillomavirus type 47 ORGANISM #formal_name human papillomavirus type 47 #note host Homo sapiens (man) DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Jul-1999 ACCESSIONS E35324 REFERENCE A35324 !$#authors Kiyono, T.; Adachi, A.; Ishibashi, M. !$#journal Virology (1990) 177:401-405 !$#title Genome organization and taxonomic position of human !1papillomavirus type 47 inferred from its DNA sequence. !$#cross-references MUID:90281611; PMID:2162112 !$#accession E35324 !'##status translation not shown !'##molecule_type DNA !'##residues 1-304 ##label KIY !'##cross-references GB:M32305; NID:g333062; PIDN:AAA46980.1; !1PID:g333068 CLASSIFICATION #superfamily papillomavirus type 5 E4 protein KEYWORDS early protein SUMMARY #length 304 #molecular-weight 33015 #checksum 9113 SEQUENCE /// ENTRY W4WLDP #type complete TITLE E4 protein - deer papillomavirus ORGANISM #formal_name deer papillomavirus DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Jul-1999 ACCESSIONS B22477 REFERENCE A93013 !$#authors Groff, D.E.; Lancaster, W.D. !$#journal J. Virol. (1985) 56:85-91 !$#title Molecular cloning and nucleotide sequence of deer !1papillomavirus. !$#cross-references MUID:85293253; PMID:2993669 !$#accession B22477 !'##molecule_type DNA !'##residues 1-122 ##label GRO !'##cross-references GB:M11910; NID:g333021; PIDN:AAA66845.1; !1PID:g808792 CLASSIFICATION #superfamily bovine papillomavirus E4 protein KEYWORDS early protein SUMMARY #length 122 #molecular-weight 13364 #checksum 8055 SEQUENCE /// ENTRY W4WLEB #type complete TITLE E4 protein - bovine papillomavirus type 1 ORGANISM #formal_name bovine papillomavirus type 1 DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 28-Jul-2000 ACCESSIONS A18151 REFERENCE A93289 !$#authors Chen, E.Y.; Howley, P.M.; Levinson, A.D.; Seeburg, P.H. !$#journal Nature (1982) 299:529-534 !$#title The primary structure and genetic organization of the bovine !1papillomavirus type 1 genome. !$#cross-references MUID:83012974; PMID:6289124 !$#accession A18151 !'##molecule_type DNA !'##residues 1-120 ##label CHE !'##cross-references GB:X02346; GB:J02044; GB:M24622; GB:X00473; !1NID:g60965; PIDN:CAB46514.1; PID:g5419937 REFERENCE A92993 !$#authors Danos, O.; Engel, L.W.; Chen, E.Y.; Yaniv, M.; Howley, P.M. !$#journal J. Virol. (1983) 46:557-566 !$#title Comparative analysis of the human type 1a and bovine type 1 !1papillomavirus genomes. !$#cross-references MUID:83189357; PMID:6302319 !$#contents annotation CLASSIFICATION #superfamily bovine papillomavirus E4 protein KEYWORDS early protein SUMMARY #length 120 #molecular-weight 12562 #checksum 3793 SEQUENCE /// ENTRY W4WLB2 #type complete TITLE E4 protein - bovine papillomavirus type 2 ORGANISM #formal_name bovine papillomavirus type 2 DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 12-Jun-1998 ACCESSIONS F31169 REFERENCE A94519 !$#authors Groff, D.E.; Mitra, R.; Lancaster, W.D. !$#submission submitted to GenBank, May 1988 !$#accession F31169 !'##molecule_type DNA !'##residues 1-118 ##label GRO !'##cross-references GB:M20219; GB:M19551; NID:g332996 CLASSIFICATION #superfamily bovine papillomavirus E4 protein KEYWORDS early protein SUMMARY #length 118 #molecular-weight 13498 #checksum 6946 SEQUENCE /// ENTRY W4WLB4 #type complete TITLE E4 protein - bovine papillomavirus type 4 ORGANISM #formal_name bovine papillomavirus type 4 DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 24-Feb-1994 ACCESSIONS G27129 REFERENCE A92795 !$#authors Patel, K.R.; Smith, K.T.; Campo, M.S. !$#journal J. Gen. Virol. (1987) 68:2117-2128 !$#title The nucleotide sequence and genome organization of bovine !1papillomavirus type 4. !$#cross-references MUID:87282264; PMID:3039043 !$#accession G27129 !'##molecule_type DNA !'##residues 1-107 ##label PAT CLASSIFICATION #superfamily bovine papillomavirus type 4 E4 protein KEYWORDS early protein SUMMARY #length 107 #molecular-weight 11846 #checksum 2636 SEQUENCE /// ENTRY W4WLRB #type complete TITLE E4 protein - cottontail rabbit papillomavirus ORGANISM #formal_name cottontail rabbit papillomavirus DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 24-Feb-1994 ACCESSIONS A03674 REFERENCE A94027 !$#authors Giri, I.; Danos, O.; Yaniv, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:1580-1584 !$#title Genomic structure of the cottontail rabbit (Shope) !1papillomavirus. !$#cross-references MUID:85166175; PMID:2984661 !$#accession A03674 !'##molecule_type DNA !'##residues 1-212 ##label GIR CLASSIFICATION #superfamily rabbit papillomavirus E4 protein KEYWORDS early protein SUMMARY #length 212 #molecular-weight 24104 #checksum 6642 SEQUENCE /// ENTRY W5WLB5 #type complete TITLE E5 protein - human papillomavirus type 5b ORGANISM #formal_name human papillomavirus type 5b #note host Homo sapiens (man) DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jun-2000 ACCESSIONS D40480 REFERENCE A40480 !$#authors Yabe, Y.; Sakai, A.; Hitsumoto, T.; Kato, H.; Ogura, H. !$#journal Virology (1991) 183:793-798 !$#title A subtype of human papillomavirus 5 (HPV-5b) and its !1subgenomic segment amplified in a carcinoma: nucleotide !1sequences and genomic organizations. !$#cross-references MUID:91306467; PMID:1649510 !$#accession D40480 !'##status translation not shown !'##molecule_type DNA !'##residues 1-168 ##label YAB !'##cross-references GB:D90252; NID:g222395; PIDN:BAA14297.1; !1PID:g222397 CLASSIFICATION #superfamily papillomavirus type 5b E5 protein KEYWORDS early protein SUMMARY #length 168 #molecular-weight 18741 #checksum 2858 SEQUENCE /// ENTRY W5WL42 #type complete TITLE E5 protein - human papillomavirus type 42 ORGANISM #formal_name human papillomavirus type 42 #note host Homo sapiens (man) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS D39451 REFERENCE A39451 !$#authors Philipp, W.; Honore, N.; Sapp, M.; Cole, S.T.; Streeck, R.E. !$#journal Virology (1992) 186:331-334 !$#title Human papillomavirus type 42: new sequence, conserved genome !1organization. !$#cross-references MUID:92087479; PMID:1309278 !$#accession D39451 !'##status translation not shown !'##molecule_type DNA !'##residues 1-95 ##label PHI !'##cross-references GB:M73236; NID:g333211; PIDN:AAA47046.1; !1PID:g333217 CLASSIFICATION #superfamily papillomavirus type 42 E5 protein KEYWORDS early protein SUMMARY #length 95 #molecular-weight 10592 #checksum 6096 SEQUENCE /// ENTRY W5WLHS #type complete TITLE E5 protein - human papillomavirus type 16 ORGANISM #formal_name human papillomavirus type 16 DATE 30-Sep-1987 #sequence_revision 31-Dec-1991 #text_change 03-Nov-2000 ACCESSIONS A30016; B22355; T10426 REFERENCE A30016 !$#authors Bubb, V.; McCance, D.J.; Schlegel, R. !$#journal Virology (1988) 163:243-246 !$#title DNA sequence of the HPV-16 E5 ORF and the structural !1conservation of its encoded protein. !$#cross-references MUID:88160059; PMID:2831662 !$#accession A30016 !'##molecule_type DNA !'##residues 1-83 ##label BUB REFERENCE A22355 !$#authors Seedorf, K.; Krammer, G.; Durst, M.; Suhai, S.; Rowekamp, !1W.G. !$#journal Virology (1985) 145:181-185 !$#title Human papillomavirus type 16 DNA sequence. !$#cross-references MUID:85246220; PMID:2990099 !$#accession B22355 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 'YCIHNITGVLFALLC',21-83 ##label SEE !'##cross-references GB:K02718; NID:g333031; PIDN:AAA46938.1; !1PID:g459914 REFERENCE Z17014 !$#authors Kennedy, I.M.; Haddow, J.K.; Clements, J.B. !$#journal J. Virol. (1991) 65:2093-2097 !$#title A negative element in the human poapillomavirus type 16 !1genome acts at the level of late mRNA stability. !$#cross-references MUID:91162763; PMID:1848319 !$#accession T10426 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 'YCIHNITGVLFALL',20-83 ##label KEN !'##cross-references EMBL:K02718; NID:g333031; PIDN:AAA46938.1; !1PID:g459914 GENETICS !$#gene E5 CLASSIFICATION #superfamily papillomavirus E5 protein KEYWORDS early protein SUMMARY #length 83 #molecular-weight 9401 #checksum 3423 SEQUENCE /// ENTRY W5WL31 #type complete TITLE E5 protein - human papillomavirus type 31 ORGANISM #formal_name human papillomavirus type 31 #note host Homo sapiens (man) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS F32444 REFERENCE A94398 !$#authors Goldsborough, M.D.; DiSilvestre, D.; Temple, G.F.; Lorincz, !1A.T. !$#journal Virology (1989) 171:306-311 !$#title Nucleotide sequence of human papillomavirus type 31: a !1cervical neoplasia-associated virus. !$#cross-references MUID:89299478; PMID:2545036 !$#accession F32444 !'##status translation not shown !'##molecule_type DNA !'##residues 1-84 ##label GOL !'##cross-references GB:J04353; NID:g333048; PIDN:AAA46954.1; !1PID:g459920 CLASSIFICATION #superfamily papillomavirus E5 protein KEYWORDS early protein SUMMARY #length 84 #molecular-weight 9536 #checksum 8574 SEQUENCE /// ENTRY W5WL35 #type complete TITLE E5 protein - human papillomavirus type 35 ORGANISM #formal_name human papillomavirus type 35 #note host Homo sapiens (man) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS D40824 REFERENCE A40824 !$#authors Marich, J.E.; Pontsler, A.V.; Rice, S.M.; McGraw, K.A.; !1Dubensky, T.W. !$#journal Virology (1992) 186:770-776 !$#title The phylogenetic relationship and complete nucleotide !1sequence of human papillomavirus type 35. !$#cross-references MUID:92124753; PMID:1310198 !$#accession D40824 !'##status translation not shown !'##molecule_type DNA !'##residues 1-81 ##label MAR !'##cross-references GB:M74117; NID:g333050; PIDN:AAA46970.1; !1PID:g333056 CLASSIFICATION #superfamily papillomavirus E5 protein KEYWORDS early protein SUMMARY #length 81 #molecular-weight 9000 #checksum 2006 SEQUENCE /// ENTRY W5WL33 #type complete TITLE E5 protein - human papillomavirus type 33 ORGANISM #formal_name human papillomavirus type 33 DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 16-Jul-1999 ACCESSIONS A03679 REFERENCE A93020 !$#authors Cole, S.T.; Streeck, R.E. !$#journal J. Virol. (1986) 58:991-995 !$#title Genome organization and nucleotide sequence of human !1papillomavirus type 33, which is associated with cervical !1cancer. !$#cross-references MUID:86200464; PMID:3009902 !$#accession A03679 !'##molecule_type DNA !'##residues 1-75 ##label COL !'##cross-references GB:M12732; NID:g333049; PIDN:AAA46962.1; !1PID:g463181 CLASSIFICATION #superfamily papillomavirus E5 protein KEYWORDS early protein SUMMARY #length 75 #molecular-weight 8906 #checksum 494 SEQUENCE /// ENTRY W5WL58 #type complete TITLE E5 protein - human papillomavirus type 58 ORGANISM #formal_name human papillomavirus type 58 #note host Homo sapiens (man) DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 21-Jul-2000 ACCESSIONS D36779 REFERENCE A36779 !$#authors Kirii, Y.; Iwamoto, S.; Matsukura, T. !$#journal Virology (1991) 185:424-427 !$#title Human papillomavirus type 58 DNA sequence. !$#cross-references MUID:92024102; PMID:1656594 !$#accession D36779 !'##status translation not shown !'##molecule_type DNA !'##residues 1-76 ##label KIR !'##cross-references GB:D90400; NID:g222386; PIDN:BAA31849.1; !1PID:g3337102 CLASSIFICATION #superfamily papillomavirus E5 protein KEYWORDS early protein SUMMARY #length 76 #molecular-weight 8953 #checksum 1825 SEQUENCE /// ENTRY W5WL51 #type complete TITLE E5 protein - human papillomavirus type 51 ORGANISM #formal_name human papillomavirus type 51 #note host Homo sapiens (man) DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 27-Jan-1995 ACCESSIONS D40415 REFERENCE A40415 !$#authors Lungu, O.; Crum, C.P.; Silverstein, S.J. !$#journal J. Virol. (1991) 65:4216-4225 !$#title Biologic properties and nucleotide sequence analysis of !1human papillomavirus type 51. !$#cross-references MUID:91303675; PMID:1649326 !$#accession D40415 !'##status translation not shown !'##molecule_type DNA !'##residues 1-84 ##label LUN !'##cross-references GB:M62877 CLASSIFICATION #superfamily papillomavirus E5 protein KEYWORDS early protein SUMMARY #length 84 #molecular-weight 9771 #checksum 5010 SEQUENCE /// ENTRY W5WL18 #type complete TITLE E5 protein - human papillomavirus type 18 ORGANISM #formal_name human papillomavirus type 18 DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Jul-1999 ACCESSIONS F26251 REFERENCE A92937 !$#authors Cole, S.T.; Danos, O. !$#journal J. Mol. Biol. (1987) 193:599-608 !$#title Nucleotide sequence and comparative analysis of the human !1papillomavirus type 18 genome. Phylogeny of papillomaviruses !1and repeated structure of the E6 and E7 gene products. !$#cross-references MUID:87283882; PMID:3039146 !$#accession F26251 !'##molecule_type DNA !'##residues 1-73 ##label COL !'##cross-references GB:X05015; NID:g60975; PIDN:CAA28669.1; PID:g60981 CLASSIFICATION #superfamily papillomavirus E5 protein KEYWORDS early protein SUMMARY #length 73 #molecular-weight 8299 #checksum 8795 SEQUENCE /// ENTRY W5WL39 #type complete TITLE E5 protein - human papillomavirus type 39 ORGANISM #formal_name human papillomavirus type 39 #note host Homo sapiens (man) DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jul-1999 ACCESSIONS F38502 REFERENCE A38502 !$#authors Volpers, C.; Streeck, R.E. !$#journal Virology (1991) 181:419-423 !$#title Genome organization and nucleotide sequence of human !1papillomavirus type 39. !$#cross-references MUID:91135017; PMID:1847266 !$#accession F38502 !'##status translation not shown !'##molecule_type DNA !'##residues 1-72 ##label VOL !'##cross-references GB:M62849; EMBL:M38185; NID:g333245; !1PIDN:AAA47054.1; PID:g463190 CLASSIFICATION #superfamily papillomavirus E5 protein KEYWORDS early protein SUMMARY #length 72 #molecular-weight 8569 #checksum 7057 SEQUENCE /// ENTRY W5WL6A #type complete TITLE E5A protein - human papillomavirus type 6b ORGANISM #formal_name human papillomavirus type 6b DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Jul-1999 ACCESSIONS A20558 REFERENCE A90975 !$#authors Schwarz, E.; Durst, M.; Demankowski, C.; Lattermann, O.; !1Zech, R.; Wolfsperger, E.; Suhai, S.; zur Hausen, H. !$#journal EMBO J. (1983) 2:2341-2348 !$#title DNA sequence and genome organization of genital human !1papillomavirus type 6b. !$#cross-references MUID:84131949; PMID:6321162 !$#accession A20558 !'##molecule_type DNA !'##residues 1-91 ##label SCH !'##cross-references GB:X00203; NID:g60955; PIDN:CAA25023.1; PID:g60961 CLASSIFICATION #superfamily papillomavirus E5 protein KEYWORDS early protein SUMMARY #length 91 #molecular-weight 10374 #checksum 6989 SEQUENCE /// ENTRY W5WL11 #type complete TITLE E5A protein - human papillomavirus type 11 ORGANISM #formal_name human papillomavirus type 11 DATE 13-Aug-1986 #sequence_revision 13-Aug-1986 #text_change 16-Jul-1999 ACCESSIONS A03680 REFERENCE A94338 !$#authors Dartmann, K.; Schwarz, E.; Gissmann, L.; zur Hausen, H. !$#journal Virology (1986) 151:124-130 !$#title The nucleotide sequence and genome organization of human !1papilloma virus type 11. !$#cross-references MUID:86181601; PMID:3008427 !$#accession A03680 !'##molecule_type DNA !'##residues 1-91 ##label DAR !'##cross-references GB:M14119; NID:g333026; PIDN:AAA46932.1; !1PID:g496198 CLASSIFICATION #superfamily papillomavirus E5 protein KEYWORDS early protein SUMMARY #length 91 #molecular-weight 10250 #checksum 5887 SEQUENCE /// ENTRY W5WL13 #type complete TITLE E5 protein - human papillomavirus type 13 ORGANISM #formal_name human papillomavirus type 13 #note host Homo sapiens (man) DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS F42955 REFERENCE A42955 !$#authors van Ranst, M.; Fuse, A.; Fiten, P.; Beuken, E.; Pfister, H.; !1Burk, R.D.; Opdenakker, G. !$#journal Virology (1992) 190:587-596 !$#title Human papillomavirus type 13 and pygmy chimpanzee !1papillomavirus type 1: Comparison of the genome !1organizations. !$#cross-references MUID:92391075; PMID:1325697 !$#accession F42955 !'##molecule_type DNA !'##residues 1-91 ##label VAN !'##cross-references EMBL:X62843; NID:g60295; PIDN:CAA44652.1; !1PID:g60301 CLASSIFICATION #superfamily papillomavirus E5 protein KEYWORDS early protein SUMMARY #length 91 #molecular-weight 10245 #checksum 6111 SEQUENCE /// ENTRY W5WLC1 #type complete TITLE E5 protein - pygmy chimpanzee papillomavirus (type 1) ORGANISM #formal_name pygmy chimpanzee papillomavirus DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS F36818 REFERENCE A42955 !$#authors van Ranst, M.; Fuse, A.; Fiten, P.; Beuken, E.; Pfister, H.; !1Burk, R.D.; Opdenakker, G. !$#journal Virology (1992) 190:587-596 !$#title Human papillomavirus type 13 and pygmy chimpanzee !1papillomavirus type 1: Comparison of the genome !1organizations. !$#cross-references MUID:92391075; PMID:1325697 !$#accession F36818 !'##molecule_type DNA !'##residues 1-94 ##label VAN !'##cross-references EMBL:X62844; NID:g61010; PIDN:CAA44660.1; !1PID:g61016 CLASSIFICATION #superfamily papillomavirus E5 protein KEYWORDS early protein SUMMARY #length 94 #molecular-weight 10717 #checksum 2923 SEQUENCE /// ENTRY W5WL41 #type complete TITLE E5 protein - human papillomavirus type 41 ORGANISM #formal_name human papillomavirus type 41 #note host Homo sapiens (man) DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS F43550 REFERENCE A43550 !$#authors Hirt, L.; Hirsch-Behnam, A.; De Villiers, E.M. !$#journal Virus Res. (1990) 18:179-190 !$#title Nucleotide sequence of human papillomavirus (HPV) type 41: !1an unusual HPV type without a typical E2 binding site !1consensus sequence. !$#accession F43550 !'##status translation not shown !'##molecule_type DNA !'##residues 1-78 ##label HIR !'##cross-references EMBL:X56147; NID:g60942; PIDN:CAA39617.1; !1PID:g60948 CLASSIFICATION #superfamily human papillomavirus type 41 E5 protein KEYWORDS early protein SUMMARY #length 78 #molecular-weight 8750 #checksum 1186 SEQUENCE /// ENTRY W5WL5A #type complete TITLE E5A protein - bovine papillomavirus type 4 ORGANISM #formal_name bovine papillomavirus type 4 DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jun-2000 ACCESSIONS H27129 REFERENCE A92795 !$#authors Patel, K.R.; Smith, K.T.; Campo, M.S. !$#journal J. Gen. Virol. (1987) 68:2117-2128 !$#title The nucleotide sequence and genome organization of bovine !1papillomavirus type 4. !$#cross-references MUID:87282264; PMID:3039043 !$#accession H27129 !'##molecule_type DNA !'##residues 1-48 ##label PAT !'##cross-references GB:D00146; NID:g222360; PIDN:BAA00099.1; !1PID:g222366 CLASSIFICATION #superfamily bovine papillomavirus type 4 E5A protein KEYWORDS early protein SUMMARY #length 48 #molecular-weight 5308 #checksum 8339 SEQUENCE /// ENTRY W5WLR1 #type complete TITLE E5 protein - rhesus papillomavirus (type 1) ORGANISM #formal_name rhesus papillomavirus DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 27-Jan-1995 ACCESSIONS F38503 REFERENCE A38503 !$#authors Ostrow, R.S.; LaBresh, K.V.; Faras, A.J. !$#journal Virology (1991) 181:424-429 !$#title Characterization of the complete RhPV 1 genomic sequence and !1an integration locus from a metastatic tumor. !$#cross-references MUID:91135018; PMID:1847267 !$#accession F38503 !'##status translation not shown !'##molecule_type DNA !'##residues 1-157 ##label OST !'##cross-references EMBL:M37717 CLASSIFICATION #superfamily rhesus papillomavirus E5 protein KEYWORDS early protein SUMMARY #length 157 #molecular-weight 17380 #checksum 8739 SEQUENCE /// ENTRY W5WLEB #type complete TITLE E5 protein - bovine papillomavirus type 1 ORGANISM #formal_name bovine papillomavirus type 1 DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 28-Jul-2000 ACCESSIONS G31169; E18151; S12366; B18151 REFERENCE A93289 !$#authors Chen, E.Y.; Howley, P.M.; Levinson, A.D.; Seeburg, P.H. !$#journal Nature (1982) 299:529-534 !$#title The primary structure and genetic organization of the bovine !1papillomavirus type 1 genome. !$#cross-references MUID:83012974; PMID:6289124 !$#accession G31169 !'##molecule_type DNA !'##residues 1-44 ##label CHE !'##cross-references GB:X02346; GB:J02044; GB:M24622; GB:X00473; !1NID:g60965; PIDN:CAB46513.1; PID:g5419936 REFERENCE A94289 !$#authors Schlegel, R.; Wade-Glass, M.; Rabson, M.S.; Yang, Y.C. !$#journal Science (1986) 233:464-467 !$#title The E5 transforming gene of bovine papillomavirus encodes a !1small, hydrophobic polypeptide. !$#cross-references MUID:86261794; PMID:3014660 !$#accession E18151 !'##molecule_type protein !'##residues 1-44 ##label SCH REFERENCE S12366 !$#authors Goldstein, D.J.; Schlegel, R. !$#journal EMBO J. (1990) 9:137-146 !$#title The E5 oncoprotein of bovine papillomavirus binds to a 16 kd !1cellular protein. !$#cross-references MUID:90107936; PMID:1688529 !$#accession S12366 !'##status preliminary !'##molecule_type protein !'##residues 1-44 ##label GOL COMMENT This protein is a small, membrane-associated, hydrophobic !1polypeptide. CLASSIFICATION #superfamily bovine papillomavirus E5 protein KEYWORDS early protein; membrane protein; transforming protein SUMMARY #length 44 #molecular-weight 5210 #checksum 4407 SEQUENCE /// ENTRY W5WLB2 #type complete TITLE E5 protein - bovine papillomavirus type 2 ORGANISM #formal_name bovine papillomavirus type 2 DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jul-1999 ACCESSIONS F18151; B18151; G31169 REFERENCE A94519 !$#authors Groff, D.E.; Mitra, R.; Lancaster, W.D. !$#submission submitted to GenBank, May 1988 !$#accession F18151 !'##molecule_type DNA !'##residues 1-44 ##label GRO !'##cross-references GB:M20219; GB:M19551; NID:g332996; PIDN:AAA66838.1; !1PID:g808785 COMMENT This protein is a small, membrane-associated, hydrophobic !1polypeptide. CLASSIFICATION #superfamily bovine papillomavirus E5 protein KEYWORDS early protein; membrane protein; transforming protein SUMMARY #length 44 #molecular-weight 5210 #checksum 4407 SEQUENCE /// ENTRY W5WLEP #type complete TITLE E5 protein - European elk papillomavirus ORGANISM #formal_name European elk papillomavirus DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 11-May-2000 ACCESSIONS E29499; E94457; E94506 REFERENCE A91567 !$#authors Ahola, H.; Bergman, P.; Stroem, A.C.; Moreno-Lopez, J.; !1Pettersson, U. !$#journal Gene (1986) 50:195-205 !$#title Organization and expression of the transforming region from !1the European elk papillomavirus (EEPV). !$#cross-references MUID:87219878; PMID:3034730 !$#accession E29499 !'##molecule_type DNA !'##residues 1-43 ##label AHO !'##cross-references GB:M15953; NID:g333025; PIDN:AAA66858.1; !1PID:g484024 REFERENCE A94457 !$#authors Eriksson, A. !$#citation unpublished results 1987, cited by GenBank !$#accession E94457 !'##molecule_type DNA !'##residues 1-43 ##label ERI !'##cross-references GB:M15953; NID:g333025; PIDN:AAA66858.1; !1PID:g484024 REFERENCE A94506 !$#authors Pettersson, U. !$#submission submitted to GenBank, August 1987 !$#accession E94506 !'##molecule_type DNA !'##residues 1-43 ##label PET !'##cross-references GB:M15953; NID:g333025; PIDN:AAA66858.1; !1PID:g484024 CLASSIFICATION #superfamily bovine papillomavirus E5 protein KEYWORDS early protein SUMMARY #length 43 #molecular-weight 5182 #checksum 1595 SEQUENCE /// ENTRY W5WLRD #type complete TITLE E5 protein - reindeer papillomavirus ORGANISM #formal_name reindeer papillomavirus #note host Rangifer tarandus (Swedish reindeer) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS A34088 REFERENCE A34088 !$#authors Moreno-Lopez, J.; Ahola, H.; Eriksson, A.; Bergman, P.; !1Pettersson, U. !$#journal J. Virol. (1987) 61:3394-3400 !$#title Reindeer papillomavirus transforming properties correlate !1with a highly conserved E5 region. !$#cross-references MUID:88036190; PMID:2822949 !$#accession A34088 !'##molecule_type DNA !'##residues 1-44 ##label MOR !'##cross-references GB:M18176; NID:g333298; PIDN:AAA79882.1; !1PID:g808799 CLASSIFICATION #superfamily bovine papillomavirus E5 protein KEYWORDS early protein SUMMARY #length 44 #molecular-weight 5212 #checksum 3916 SEQUENCE /// ENTRY W5WLRB #type complete TITLE E5 protein - cottontail rabbit papillomavirus ORGANISM #formal_name cottontail rabbit papillomavirus DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 24-Feb-1994 ACCESSIONS A03678 REFERENCE A94027 !$#authors Giri, I.; Danos, O.; Yaniv, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:1580-1584 !$#title Genomic structure of the cottontail rabbit (Shope) !1papillomavirus. !$#cross-references MUID:85166175; PMID:2984661 !$#accession A03678 !'##molecule_type DNA !'##residues 1-101 ##label GIR CLASSIFICATION #superfamily rabbit papillomavirus E5 protein KEYWORDS early protein SUMMARY #length 101 #molecular-weight 11339 #checksum 9906 SEQUENCE /// ENTRY W5WL1B #type complete TITLE E5B protein - human papillomavirus type 11 ORGANISM #formal_name human papillomavirus type 11 DATE 13-Aug-1986 #sequence_revision 13-Aug-1986 #text_change 16-Jul-1999 ACCESSIONS A03681 REFERENCE A94338 !$#authors Dartmann, K.; Schwarz, E.; Gissmann, L.; zur Hausen, H. !$#journal Virology (1986) 151:124-130 !$#title The nucleotide sequence and genome organization of human !1papilloma virus type 11. !$#cross-references MUID:86181601; PMID:3008427 !$#accession A03681 !'##molecule_type DNA !'##residues 1-74 ##label DAR !'##cross-references GB:M14119; NID:g333026; PIDN:AAA46933.1; !1PID:g496199 CLASSIFICATION #superfamily papillomavirus E5B protein KEYWORDS early protein SUMMARY #length 74 #molecular-weight 8507 #checksum 9137 SEQUENCE /// ENTRY W5WL6B #type complete TITLE E5B protein - human papillomavirus type 6b ORGANISM #formal_name human papillomavirus type 6b DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Jul-1999 ACCESSIONS B20558 REFERENCE A90975 !$#authors Schwarz, E.; Durst, M.; Demankowski, C.; Lattermann, O.; !1Zech, R.; Wolfsperger, E.; Suhai, S.; zur Hausen, H. !$#journal EMBO J. (1983) 2:2341-2348 !$#title DNA sequence and genome organization of genital human !1papillomavirus type 6b. !$#cross-references MUID:84131949; PMID:6321162 !$#accession B20558 !'##molecule_type DNA !'##residues 1-72 ##label SCH !'##cross-references GB:X00203; NID:g60955; PIDN:CAA25024.1; PID:g60962 CLASSIFICATION #superfamily papillomavirus E5B protein KEYWORDS early protein SUMMARY #length 72 #molecular-weight 8415 #checksum 3379 SEQUENCE /// ENTRY W5WL5B #type complete TITLE E5B protein - bovine papillomavirus type 4 ORGANISM #formal_name bovine papillomavirus type 4 DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 24-Feb-1994 ACCESSIONS I27129 REFERENCE A92795 !$#authors Patel, K.R.; Smith, K.T.; Campo, M.S. !$#journal J. Gen. Virol. (1987) 68:2117-2128 !$#title The nucleotide sequence and genome organization of bovine !1papillomavirus type 4. !$#cross-references MUID:87282264; PMID:3039043 !$#accession I27129 !'##molecule_type DNA !'##residues 1-95 ##label PAT CLASSIFICATION #superfamily bovine papillomavirus type 4 E5B protein KEYWORDS early protein SUMMARY #length 95 #molecular-weight 11026 #checksum 2178 SEQUENCE /// ENTRY W6WL18 #type complete TITLE E6 protein - human papillomavirus type 18 ORGANISM #formal_name human papillomavirus type 18 DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Jul-1999 ACCESSIONS A26165; G26251 REFERENCE A91068 !$#authors Seedorf, K.; Oltersdorf, T.; Kraemmer, G.; Roewekamp, W. !$#journal EMBO J. (1987) 6:139-144 !$#title Identification of early proteins of the human papilloma !1viruses type 16 (HPV 16) and type 18 (HPV 18) in cervical !1carcinoma cells. !$#cross-references MUID:87218459; PMID:3034571 !$#accession A26165 !'##molecule_type DNA !'##residues 1-158 ##label SEE !'##cross-references GB:X04773; NID:g60876; PIDN:CAA28466.1; PID:g60877 REFERENCE A92937 !$#authors Cole, S.T.; Danos, O. !$#journal J. Mol. Biol. (1987) 193:599-608 !$#title Nucleotide sequence and comparative analysis of the human !1papillomavirus type 18 genome. Phylogeny of papillomaviruses !1and repeated structure of the E6 and E7 gene products. !$#cross-references MUID:87283882; PMID:3039146 !$#accession G26251 !'##molecule_type DNA !'##residues 1-158 ##label COL !'##cross-references GB:X05015; NID:g60975; PIDN:CAA28664.1; PID:g60976 REFERENCE A92791 !$#authors Matlashewski, G.; Banks, L.; Wu-Liao, J.; Spence, P.; Pim, !1D.; Crawford, L. !$#journal J. Gen. Virol. (1986) 67:1909-1916 !$#title The expression of human papillomavirus type 18 E6 protein in !1bacteria and the production of anti-E6 antibodies. !$#cross-references MUID:86306665; PMID:3018129 !$#contents annotation; identification of the protein CLASSIFICATION #superfamily papillomavirus E6 protein KEYWORDS DNA binding; early protein; transforming protein; zinc !1finger FEATURE !$32-68 #region zinc finger CCCC motif\ !$105-141 #region zinc finger CCCC motif SUMMARY #length 158 #molecular-weight 18871 #checksum 487 SEQUENCE /// ENTRY W6WLPR #type complete TITLE E6 protein - human papillomavirus type ME180 (provirus) ORGANISM #formal_name human papillomavirus type ME180 #note host Homo sapiens (man) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Feb-1997 ACCESSIONS C40509 REFERENCE A40509 !$#authors Reuter, S.; Delius, H.; Kahn, T.; Hofmann, B.; zur Hausen, !1H.; Schwarz, E. !$#journal J. Virol. (1991) 65:5564-5568 !$#title Characterization of a novel human papillomavirus DNA in the !1cervical carcinoma cell line ME180. !$#cross-references MUID:91374616; PMID:1716694 !$#accession C40509 !'##status translation not shown !'##molecule_type DNA !'##residues 1-158 ##label REU !'##cross-references GB:M73258 CLASSIFICATION #superfamily papillomavirus E6 protein KEYWORDS DNA binding; early protein; zinc finger FEATURE !$32-68 #region zinc finger CCCC motif\ !$105-141 #region zinc finger CCCC motif SUMMARY #length 158 #molecular-weight 18738 #checksum 3173 SEQUENCE /// ENTRY W6WL39 #type complete TITLE E6 protein - human papillomavirus type 39 ORGANISM #formal_name human papillomavirus type 39 #note host Homo sapiens (man) DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jul-1999 ACCESSIONS A38502 REFERENCE A38502 !$#authors Volpers, C.; Streeck, R.E. !$#journal Virology (1991) 181:419-423 !$#title Genome organization and nucleotide sequence of human !1papillomavirus type 39. !$#cross-references MUID:91135017; PMID:1847266 !$#accession A38502 !'##status translation not shown !'##molecule_type DNA !'##residues 1-158 ##label VOL !'##cross-references GB:M62849; EMBL:M38185; NID:g333245; !1PIDN:AAA47050.1; PID:g463186 CLASSIFICATION #superfamily papillomavirus E6 protein KEYWORDS DNA binding; early protein; transforming protein; zinc !1finger FEATURE !$32-68 #region zinc finger CCCC motif\ !$105-141 #region zinc finger CCCC motif SUMMARY #length 158 #molecular-weight 18726 #checksum 3593 SEQUENCE /// ENTRY W6WLHS #type complete TITLE protein E6 - human papillomavirus type 16 ORGANISM #formal_name human papillomavirus type 16 DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 20-Aug-1999 ACCESSIONS A03682; T10427 REFERENCE A22355 !$#authors Seedorf, K.; Krammer, G.; Durst, M.; Suhai, S.; Rowekamp, !1W.G. !$#journal Virology (1985) 145:181-185 !$#title Human papillomavirus type 16 DNA sequence. !$#cross-references MUID:85246220; PMID:2990099 !$#accession A03682 !'##molecule_type DNA !'##residues 1-158 ##label SEE !'##cross-references GB:K02718; NID:g333031; PIDN:AAA46939.1; !1PID:g333032 REFERENCE Z17014 !$#authors Kennedy, I.M.; Haddow, J.K.; Clements, J.B. !$#journal J. Virol. (1991) 65:2093-2097 !$#title A negative element in the human poapillomavirus type 16 !1genome acts at the level of late mRNA stability. !$#cross-references MUID:91162763; PMID:1848319 !$#accession T10427 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-158 ##label KEN !'##cross-references EMBL:K02718; NID:g333031; PIDN:AAA46939.1; !1PID:g333032 GENETICS !$#gene E6 CLASSIFICATION #superfamily papillomavirus E6 protein KEYWORDS DNA binding; early protein; zinc finger FEATURE !$37-73 #region zinc finger CCCC motif\ !$110-146 #region zinc finger CCCC motif SUMMARY #length 158 #molecular-weight 19187 #checksum 9827 SEQUENCE /// ENTRY W6WL51 #type complete TITLE E6 protein - human papillomavirus type 51 ORGANISM #formal_name human papillomavirus type 51 #note host Homo sapiens (man) DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Feb-1997 ACCESSIONS E40415 REFERENCE A40415 !$#authors Lungu, O.; Crum, C.P.; Silverstein, S.J. !$#journal J. Virol. (1991) 65:4216-4225 !$#title Biologic properties and nucleotide sequence analysis of !1human papillomavirus type 51. !$#cross-references MUID:91303675; PMID:1649326 !$#accession E40415 !'##status translation not shown !'##molecule_type DNA !'##residues 1-151 ##label LUN !'##cross-references GB:M62877 CLASSIFICATION #superfamily papillomavirus E6 protein KEYWORDS DNA binding; early protein; zinc finger FEATURE !$30-66 #region zinc finger CCCC motif\ !$103-139 #region zinc finger CCCC motif SUMMARY #length 151 #molecular-weight 18134 #checksum 9025 SEQUENCE /// ENTRY W6WL31 #type complete TITLE E6 protein - human papillomavirus type 31 ORGANISM #formal_name human papillomavirus type 31 #note host Homo sapiens (man) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS A32444 REFERENCE A94398 !$#authors Goldsborough, M.D.; DiSilvestre, D.; Temple, G.F.; Lorincz, !1A.T. !$#journal Virology (1989) 171:306-311 !$#title Nucleotide sequence of human papillomavirus type 31: a !1cervical neoplasia-associated virus. !$#cross-references MUID:89299478; PMID:2545036 !$#accession A32444 !'##status translation not shown !'##molecule_type DNA !'##residues 1-149 ##label GOL !'##cross-references GB:J04353; NID:g333048; PIDN:AAA46950.1; !1PID:g459916 COMMENT This protein may be involved in the oncogenic potential of !1this virus. CLASSIFICATION #superfamily papillomavirus E6 protein KEYWORDS DNA binding; early protein; zinc finger FEATURE !$30-66 #region zinc finger CCCC motif\ !$103-139 #region zinc finger CCCC motif SUMMARY #length 149 #molecular-weight 17713 #checksum 1083 SEQUENCE /// ENTRY W6WL35 #type complete TITLE E6 protein - human papillomavirus type 35 ORGANISM #formal_name human papillomavirus type 35 #note host Homo sapiens (man) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 23-Mar-2001 ACCESSIONS E40824; S36521 REFERENCE A40824 !$#authors Marich, J.E.; Pontsler, A.V.; Rice, S.M.; McGraw, K.A.; !1Dubensky, T.W. !$#journal Virology (1992) 186:770-776 !$#title The phylogenetic relationship and complete nucleotide !1sequence of human papillomavirus type 35. !$#cross-references MUID:92124753; PMID:1310198 !$#accession E40824 !'##status translation not shown !'##molecule_type DNA !'##residues 1-149 ##label MAR !'##cross-references GB:M74117; NID:g333050; PIDN:AAA46966.1; !1PID:g333051 REFERENCE S36469 !$#authors Delius, H.; Hofmann, B. !$#submission submitted to the EMBL Data Library, August 1993 !$#description Primer-directed sequencing of human papillomavirus types. !$#accession S36521 !'##status preliminary !'##molecule_type DNA !'##residues 1-149 ##label DEL !'##cross-references EMBL:X74477; NID:g396997; PIDN:CAA52561.1; !1PID:g396998 !'##experimental_source strain 35H CLASSIFICATION #superfamily papillomavirus E6 protein KEYWORDS DNA binding; early protein; zinc finger FEATURE !$30-66 #region zinc finger CCCC motif\ !$103-139 #region zinc finger CCCC motif SUMMARY #length 149 #molecular-weight 18045 #checksum 914 SEQUENCE /// ENTRY W6WL33 #type complete TITLE E6 protein - human papillomavirus type 33 ORGANISM #formal_name human papillomavirus type 33 DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 16-Jul-1999 ACCESSIONS A03683 REFERENCE A93020 !$#authors Cole, S.T.; Streeck, R.E. !$#journal J. Virol. (1986) 58:991-995 !$#title Genome organization and nucleotide sequence of human !1papillomavirus type 33, which is associated with cervical !1cancer. !$#cross-references MUID:86200464; PMID:3009902 !$#accession A03683 !'##molecule_type DNA !'##residues 1-149 ##label COL !'##cross-references GB:M12732; NID:g333049; PIDN:AAA46958.1; !1PID:g463177 CLASSIFICATION #superfamily papillomavirus E6 protein KEYWORDS DNA binding; early protein; zinc finger FEATURE !$30-66 #region zinc finger CCCC motif\ !$103-139 #region zinc finger CCCC motif SUMMARY #length 149 #molecular-weight 17652 #checksum 636 SEQUENCE /// ENTRY W6WL58 #type complete TITLE E6 protein - human papillomavirus type 58 ORGANISM #formal_name human papillomavirus type 58 #note host Homo sapiens (man) DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 21-Jul-2000 ACCESSIONS E36779 REFERENCE A36779 !$#authors Kirii, Y.; Iwamoto, S.; Matsukura, T. !$#journal Virology (1991) 185:424-427 !$#title Human papillomavirus type 58 DNA sequence. !$#cross-references MUID:92024102; PMID:1656594 !$#accession E36779 !'##status translation not shown !'##molecule_type DNA !'##residues 1-149 ##label KIR !'##cross-references GB:D90400; NID:g222386; PIDN:BAA31845.1; !1PID:g3337098 CLASSIFICATION #superfamily papillomavirus E6 protein KEYWORDS DNA binding; early protein; zinc finger FEATURE !$30-66 #region zinc finger CCCC motif\ !$103-139 #region zinc finger CCCC motif SUMMARY #length 149 #molecular-weight 17794 #checksum 1553 SEQUENCE /// ENTRY W6WL56 #type complete TITLE E6 protein - human papillomavirus type 56 ORGANISM #formal_name human papillomavirus type 56 DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jul-1999 ACCESSIONS A33377; S36579 REFERENCE A33377 !$#authors Loerincz, A.T.; Quinn, A.P.; Goldsborough, M.D.; McAllister, !1P.; Temple, G.F. !$#journal J. Gen. Virol. (1989) 70:3099-3104 !$#title Human papillomavirus type 56: a new virus detected in !1cervical cancers. !$#cross-references MUID:90063558; PMID:2555440 !$#accession A33377 !'##molecule_type DNA !'##residues 1-155 ##label LOE REFERENCE S36469 !$#authors Delius, H.; Hofmann, B. !$#submission submitted to the EMBL Data Library, August 1993 !$#description Primer-directed sequencing of human papillomavirus types. !$#accession S36579 !'##status preliminary !'##molecule_type DNA !'##residues 1-155 ##label DEL !'##cross-references EMBL:X74483; NID:g397053; PIDN:CAA52596.1; !1PID:g397054 CLASSIFICATION #superfamily papillomavirus E6 protein KEYWORDS DNA binding; early protein; transforming protein; zinc !1finger FEATURE !$33-69 #region zinc finger CCCC motif\ !$106-142 #region zinc finger CCCC motif SUMMARY #length 155 #molecular-weight 18524 #checksum 2790 SEQUENCE /// ENTRY W6WLR1 #type complete TITLE E6 protein - rhesus papillomavirus (type 1) ORGANISM #formal_name rhesus papillomavirus DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Feb-1997 ACCESSIONS A38503 REFERENCE A38503 !$#authors Ostrow, R.S.; LaBresh, K.V.; Faras, A.J. !$#journal Virology (1991) 181:424-429 !$#title Characterization of the complete RhPV 1 genomic sequence and !1an integration locus from a metastatic tumor. !$#cross-references MUID:91135018; PMID:1847267 !$#accession A38503 !'##status translation not shown !'##molecule_type DNA !'##residues 1-191 ##label OST !'##cross-references EMBL:M37717 CLASSIFICATION #superfamily papillomavirus E6 protein KEYWORDS DNA binding; early protein; transforming protein; zinc !1finger FEATURE !$60-96 #region zinc finger CCCC motif\ !$133-169 #region zinc finger CCCC motif SUMMARY #length 191 #molecular-weight 22701 #checksum 7081 SEQUENCE /// ENTRY W6WLRB #type complete TITLE E6 protein - cottontail rabbit papillomavirus ORGANISM #formal_name cottontail rabbit papillomavirus DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 16-Feb-1997 ACCESSIONS A03686 REFERENCE A94027 !$#authors Giri, I.; Danos, O.; Yaniv, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:1580-1584 !$#title Genomic structure of the cottontail rabbit (Shope) !1papillomavirus. !$#cross-references MUID:85166175; PMID:2984661 !$#accession A03686 !'##molecule_type DNA !'##residues 1-273 ##label GIR CLASSIFICATION #superfamily papillomavirus E6 protein KEYWORDS DNA binding; early protein; zinc finger SUMMARY #length 273 #molecular-weight 29735 #checksum 679 SEQUENCE /// ENTRY W6WL11 #type complete TITLE E6 protein - human papillomavirus type 11 ORGANISM #formal_name human papillomavirus type 11 DATE 13-Aug-1986 #sequence_revision 13-Aug-1986 #text_change 16-Jul-1999 ACCESSIONS A03684 REFERENCE A94338 !$#authors Dartmann, K.; Schwarz, E.; Gissmann, L.; zur Hausen, H. !$#journal Virology (1986) 151:124-130 !$#title The nucleotide sequence and genome organization of human !1papilloma virus type 11. !$#cross-references MUID:86181601; PMID:3008427 !$#accession A03684 !'##molecule_type DNA !'##residues 1-150 ##label DAR !'##cross-references GB:M14119; NID:g333026; PIDN:AAA46927.1; !1PID:g496193 CLASSIFICATION #superfamily papillomavirus E6 protein KEYWORDS DNA binding; early protein; zinc finger FEATURE !$31-67 #region zinc finger CCCC motif\ !$104-140 #region zinc finger CCCC motif SUMMARY #length 150 #molecular-weight 17406 #checksum 1866 SEQUENCE /// ENTRY W6WL6 #type complete TITLE E6 protein - human papillomavirus type 6b ORGANISM #formal_name human papillomavirus type 6b DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Jul-1999 ACCESSIONS E20558 REFERENCE A90975 !$#authors Schwarz, E.; Durst, M.; Demankowski, C.; Lattermann, O.; !1Zech, R.; Wolfsperger, E.; Suhai, S.; zur Hausen, H. !$#journal EMBO J. (1983) 2:2341-2348 !$#title DNA sequence and genome organization of genital human !1papillomavirus type 6b. !$#cross-references MUID:84131949; PMID:6321162 !$#accession E20558 !'##molecule_type DNA !'##residues 1-150 ##label SCH !'##cross-references GB:X00203; NID:g60955; PIDN:CAA25018.1; PID:g60956 CLASSIFICATION #superfamily papillomavirus E6 protein KEYWORDS DNA binding; early protein; zinc finger FEATURE !$31-67 #region zinc finger CCCC motif\ !$104-140 #region zinc finger CCCC motif SUMMARY #length 150 #molecular-weight 17299 #checksum 1555 SEQUENCE /// ENTRY W6WL44 #type complete TITLE E6 protein - human papillomavirus type 44 ORGANISM #formal_name human papillomavirus type 44 #note host Homo sapiens (man) DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS B34144 REFERENCE A34144 !$#authors Loerincz, A.T.; Quinn, A.P.; Goldsborough, M.D.; Schmidt, !1B.J.; Temple, G.F. !$#journal J. Virol. (1989) 63:2829-2834 !$#title Cloning and partial DNA sequencing of two new human !1papillomavirus types associated with condylomas and !1low-grade cervical neoplasia. !$#cross-references MUID:89259065; PMID:2542593 !$#accession B34144 !'##molecule_type DNA !'##residues 1-150 ##label LOE !'##cross-references GB:M27023; NID:g341597; PIDN:AAA63454.1; !1PID:g703248 CLASSIFICATION #superfamily papillomavirus E6 protein KEYWORDS DNA binding; early protein; transforming protein; zinc !1finger FEATURE !$31-67 #region zinc finger CCCC motif\ !$104-140 #region zinc finger CCCC motif SUMMARY #length 150 #molecular-weight 17355 #checksum 5175 SEQUENCE /// ENTRY W6WL13 #type complete TITLE E6 protein - human papillomavirus type 13 ORGANISM #formal_name human papillomavirus type 13 #note host Homo sapiens (man) DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS A42955 REFERENCE A42955 !$#authors van Ranst, M.; Fuse, A.; Fiten, P.; Beuken, E.; Pfister, H.; !1Burk, R.D.; Opdenakker, G. !$#journal Virology (1992) 190:587-596 !$#title Human papillomavirus type 13 and pygmy chimpanzee !1papillomavirus type 1: Comparison of the genome !1organizations. !$#cross-references MUID:92391075; PMID:1325697 !$#accession A42955 !'##molecule_type DNA !'##residues 1-150 ##label VAN !'##cross-references EMBL:X62843; NID:g60295; PIDN:CAA44647.1; !1PID:g60296 CLASSIFICATION #superfamily papillomavirus E6 protein KEYWORDS DNA binding; early protein; transforming protein; zinc !1finger FEATURE !$31-67 #region zinc finger CCCC motif\ !$104-140 #region zinc finger CCCC motif SUMMARY #length 150 #molecular-weight 17328 #checksum 2995 SEQUENCE /// ENTRY W6WLC1 #type complete TITLE E6 protein - pygmy chimpanzee papillomavirus (type 1) ORGANISM #formal_name pygmy chimpanzee papillomavirus DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS A36818 REFERENCE A42955 !$#authors van Ranst, M.; Fuse, A.; Fiten, P.; Beuken, E.; Pfister, H.; !1Burk, R.D.; Opdenakker, G. !$#journal Virology (1992) 190:587-596 !$#title Human papillomavirus type 13 and pygmy chimpanzee !1papillomavirus type 1: Comparison of the genome !1organizations. !$#cross-references MUID:92391075; PMID:1325697 !$#accession A36818 !'##molecule_type DNA !'##residues 1-150 ##label VAN !'##cross-references EMBL:X62844; NID:g61010; PIDN:CAA44655.1; !1PID:g61011 CLASSIFICATION #superfamily papillomavirus E6 protein KEYWORDS DNA binding; early protein; transforming protein; zinc !1finger FEATURE !$31-67 #region zinc finger CCCC motif\ !$104-140 #region zinc finger CCCC motif SUMMARY #length 150 #molecular-weight 17492 #checksum 1112 SEQUENCE /// ENTRY W6WL43 #type complete TITLE E6 protein - human papillomavirus type 43 ORGANISM #formal_name human papillomavirus type 43 #note host Homo sapiens (man) DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS A34144 REFERENCE A34144 !$#authors Loerincz, A.T.; Quinn, A.P.; Goldsborough, M.D.; Schmidt, !1B.J.; Temple, G.F. !$#journal J. Virol. (1989) 63:2829-2834 !$#title Cloning and partial DNA sequencing of two new human !1papillomavirus types associated with condylomas and !1low-grade cervical neoplasia. !$#cross-references MUID:89259065; PMID:2542593 !$#accession A34144 !'##molecule_type DNA !'##residues 1-155 ##label LOE !'##cross-references GB:M27022; NID:g341596; PIDN:AAA63453.1; !1PID:g703247 CLASSIFICATION #superfamily papillomavirus E6 protein KEYWORDS DNA binding; early protein; transforming protein; zinc !1finger FEATURE !$31-67 #region zinc finger CCCC motif\ !$104-140 #region zinc finger CCCC motif SUMMARY #length 155 #molecular-weight 18196 #checksum 7200 SEQUENCE /// ENTRY W6WL42 #type complete TITLE E6 protein - human papillomavirus type 42 ORGANISM #formal_name human papillomavirus type 42 #note host Homo sapiens (man) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Feb-1997 ACCESSIONS E39451 REFERENCE A39451 !$#authors Philipp, W.; Honore, N.; Sapp, M.; Cole, S.T.; Streeck, R.E. !$#journal Virology (1992) 186:331-334 !$#title Human papillomavirus type 42: new sequence, conserved genome !1organization. !$#cross-references MUID:92087479; PMID:1309278 !$#accession E39451 !'##status translation not shown !'##molecule_type DNA !'##residues 1-150 ##label PHI !'##cross-references GB:M73236 CLASSIFICATION #superfamily papillomavirus E6 protein KEYWORDS DNA binding; early protein; zinc finger SUMMARY #length 150 #molecular-weight 17499 #checksum 4083 SEQUENCE /// ENTRY W6WL41 #type complete TITLE E6 protein - human papillomavirus type 41 ORGANISM #formal_name human papillomavirus type 41 #note host Homo sapiens (man) DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS A43550 REFERENCE A43550 !$#authors Hirt, L.; Hirsch-Behnam, A.; De Villiers, E.M. !$#journal Virus Res. (1990) 18:179-190 !$#title Nucleotide sequence of human papillomavirus (HPV) type 41: !1an unusual HPV type without a typical E2 binding site !1consensus sequence. !$#accession A43550 !'##status translation not shown !'##molecule_type DNA !'##residues 1-156 ##label HIR !'##cross-references EMBL:X56147; NID:g60942; PIDN:CAA39612.1; !1PID:g60943 CLASSIFICATION #superfamily papillomavirus E6 protein KEYWORDS DNA binding; early protein; transforming protein; zinc !1finger FEATURE !$42-78 #region zinc finger CCCC motif\ !$115-151 #region zinc finger CCCC motif SUMMARY #length 156 #molecular-weight 17302 #checksum 1115 SEQUENCE /// ENTRY W6WL #type complete TITLE E6 protein - human papillomavirus type 1a ORGANISM #formal_name human papillomavirus type 1a DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Jul-1999 ACCESSIONS B17475 REFERENCE A90970 !$#authors Danos, O.; Katinka, M.; Yaniv, M. !$#journal EMBO J. (1982) 1:231-236 !$#title Human papillomavirus 1a complete DNA sequence: a novel type !1of genome organization among papovaviridae. !$#cross-references MUID:84182467; PMID:6325156 !$#accession B17475 !'##molecule_type DNA !'##residues 1-140 ##label DAN !'##cross-references GB:V01116; GB:X03321; NID:g60966; PIDN:CAA24314.1; !1PID:g60967 REFERENCE A92993 !$#authors Danos, O.; Engel, L.W.; Chen, E.Y.; Yaniv, M.; Howley, P.M. !$#journal J. Virol. (1983) 46:557-566 !$#title Comparative analysis of the human type 1a and bovine type 1 !1papillomavirus genomes. !$#cross-references MUID:83189357; PMID:6302319 !$#contents annotation CLASSIFICATION #superfamily papillomavirus E6 protein KEYWORDS DNA binding; early protein; zinc finger SUMMARY #length 140 #molecular-weight 16317 #checksum 7528 SEQUENCE /// ENTRY W6WL8 #type complete TITLE E6 protein - human papillomavirus type 8 ORGANISM #formal_name human papillomavirus type 8 DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 07-Nov-1997 ACCESSIONS A03685 REFERENCE A93019 !$#authors Fuchs, P.G.; Iftner, T.; Weninger, J.; Pfister, H. !$#journal J. Virol. (1986) 58:626-634 !$#title Epidermodysplasia verruciformis-associated human !1papillomavirus 8: genomic sequence and comparative analysis. !$#cross-references MUID:86200410; PMID:3009874 !$#accession A03685 !'##molecule_type DNA !'##residues 1-155 ##label FUC !'##cross-references GB:M12737; NID:g333074 !'##note this ORF is not annotated in GenBank entry PPH8CG CLASSIFICATION #superfamily papillomavirus E6 protein KEYWORDS DNA binding; early protein; zinc finger FEATURE !$39-75 #region zinc finger CCCC motif\ !$112-148 #region zinc finger CCCC motif SUMMARY #length 155 #molecular-weight 17759 #checksum 1263 SEQUENCE /// ENTRY W6WL5 #type complete TITLE E6 protein - human papillomavirus type 5 ORGANISM #formal_name human papillomavirus type 5 DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Feb-1997 ACCESSIONS F26277 REFERENCE A94360 !$#authors Zachow, K.R.; Ostrow, R.S.; Faras, A.J. !$#journal Virology (1987) 158:251-254 !$#title Nucleotide sequence and genome organization of human !1papillomavirus type 5. !$#cross-references MUID:87207670; PMID:3033892 !$#accession F26277 !'##molecule_type DNA !'##residues 1-157 ##label ZAC CLASSIFICATION #superfamily papillomavirus E6 protein KEYWORDS DNA binding; early protein; zinc finger FEATURE !$41-77 #region zinc finger CCCC motif\ !$114-150 #region zinc finger CCCC motif SUMMARY #length 157 #molecular-weight 18091 #checksum 5313 SEQUENCE /// ENTRY W6WLB5 #type complete TITLE E6 protein - human papillomavirus type 5b ORGANISM #formal_name human papillomavirus type 5b #note host Homo sapiens (man) DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jun-2000 ACCESSIONS E40480 REFERENCE A40480 !$#authors Yabe, Y.; Sakai, A.; Hitsumoto, T.; Kato, H.; Ogura, H. !$#journal Virology (1991) 183:793-798 !$#title A subtype of human papillomavirus 5 (HPV-5b) and its !1subgenomic segment amplified in a carcinoma: nucleotide !1sequences and genomic organizations. !$#cross-references MUID:91306467; PMID:1649510 !$#accession E40480 !'##status translation not shown !'##molecule_type DNA !'##residues 1-157 ##label YAB !'##cross-references GB:D90252; NID:g222395; PIDN:BAA14292.1; !1PID:g222398 CLASSIFICATION #superfamily papillomavirus E6 protein KEYWORDS DNA binding; early protein; zinc finger FEATURE !$41-77 #region zinc finger CCCC motif\ !$114-150 #region zinc finger CCCC motif SUMMARY #length 157 #molecular-weight 18087 #checksum 5192 SEQUENCE /// ENTRY W6WL47 #type complete TITLE E6 protein - human papillomavirus type 47 ORGANISM #formal_name human papillomavirus type 47 #note host Homo sapiens (man) DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Jul-1999 ACCESSIONS A35324 REFERENCE A35324 !$#authors Kiyono, T.; Adachi, A.; Ishibashi, M. !$#journal Virology (1990) 177:401-405 !$#title Genome organization and taxonomic position of human !1papillomavirus type 47 inferred from its DNA sequence. !$#cross-references MUID:90281611; PMID:2162112 !$#accession A35324 !'##status translation not shown !'##molecule_type DNA !'##residues 1-156 ##label KIY !'##cross-references GB:M32305; NID:g333062; PIDN:AAA46976.1; !1PID:g333064 CLASSIFICATION #superfamily papillomavirus E6 protein KEYWORDS DNA binding; early protein; transforming protein; zinc !1finger FEATURE !$40-76 #region zinc finger CCCC motif\ !$113-149 #region zinc finger CCCC motif SUMMARY #length 156 #molecular-weight 18116 #checksum 6834 SEQUENCE /// ENTRY S15614 #type complete TITLE E6 protein - human papillomavirus type 2a ORGANISM #formal_name human papillomavirus type 2a #note host Homo sapiens (man) DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 23-Aug-1996 ACCESSIONS S15614 REFERENCE S15614 !$#authors Hirsch-Behnam, A.; Delius, H.; de Villiers, E.M. !$#journal Virus Res. (1990) 18:81-98 !$#title A comparative sequence analysis of two human papillomavirus !1(HPV) types 2a and 57. !$#cross-references MUID:91188699; PMID:1964523 !$#accession S15614 !'##molecule_type DNA !'##residues 1-159 ##label HIR !'##cross-references EMBL:X55964 CLASSIFICATION #superfamily papillomavirus E6 protein KEYWORDS DNA binding; early protein; transforming protein; zinc !1finger FEATURE !$35-71 #region zinc finger CCCC motif\ !$108-144 #region zinc finger CCCC motif SUMMARY #length 159 #molecular-weight 18301 #checksum 7918 SEQUENCE /// ENTRY S15621 #type complete TITLE E6 protein - human papillomavirus type 57 ORGANISM #formal_name human papillomavirus type 57 #note host Homo sapiens (man) DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS S15621 REFERENCE S15614 !$#authors Hirsch-Behnam, A.; Delius, H.; de Villiers, E.M. !$#journal Virus Res. (1990) 18:81-98 !$#title A comparative sequence analysis of two human papillomavirus !1(HPV) types 2a and 57. !$#cross-references MUID:91188699; PMID:1964523 !$#accession S15621 !'##molecule_type DNA !'##residues 1-153 ##label HIR !'##cross-references EMBL:X55965; NID:g60882; PIDN:CAA39430.1; !1PID:g60883 CLASSIFICATION #superfamily papillomavirus E6 protein KEYWORDS DNA binding; early protein; transforming protein; zinc !1finger FEATURE !$29-65 #region zinc finger CCCC motif\ !$102-138 #region zinc finger CCCC motif SUMMARY #length 153 #molecular-weight 17792 #checksum 9195 SEQUENCE /// ENTRY W6WLDP #type complete TITLE E6 protein - deer papillomavirus ORGANISM #formal_name deer papillomavirus DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 16-Jul-1999 ACCESSIONS A03687 REFERENCE A93013 !$#authors Groff, D.E.; Lancaster, W.D. !$#journal J. Virol. (1985) 56:85-91 !$#title Molecular cloning and nucleotide sequence of deer !1papillomavirus. !$#cross-references MUID:85293253; PMID:2993669 !$#accession A03687 !'##molecule_type DNA !'##residues 1-135 ##label GRO !'##cross-references GB:M11910; NID:g333021; PIDN:AAA66841.1; !1PID:g808788 CLASSIFICATION #superfamily papillomavirus E6 protein KEYWORDS DNA binding; early protein; zinc finger SUMMARY #length 135 #molecular-weight 15624 #checksum 9336 SEQUENCE /// ENTRY W6WLEP #type complete TITLE E6 protein - European elk papillomavirus ORGANISM #formal_name European elk papillomavirus DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 11-May-2000 ACCESSIONS A29499; F94457; F94506 REFERENCE A91567 !$#authors Ahola, H.; Bergman, P.; Stroem, A.C.; Moreno-Lopez, J.; !1Pettersson, U. !$#journal Gene (1986) 50:195-205 !$#title Organization and expression of the transforming region from !1the European elk papillomavirus (EEPV). !$#cross-references MUID:87219878; PMID:3034730 !$#accession A29499 !'##molecule_type DNA !'##residues 1-135 ##label AHO !'##cross-references GB:M15953; NID:g333025; PIDN:AAA66849.1; !1PID:g484015 REFERENCE A94457 !$#authors Eriksson, A. !$#citation unpublished results 1987, cited by GenBank !$#accession F94457 !'##molecule_type DNA !'##residues 1-135 ##label ERI !'##cross-references GB:M15953; NID:g333025; PIDN:AAA66849.1; !1PID:g484015 REFERENCE A94506 !$#authors Pettersson, U. !$#submission submitted to GenBank, August 1987 !$#accession F94506 !'##molecule_type DNA !'##residues 1-135 ##label PET !'##cross-references GB:M15953; NID:g333025; PIDN:AAA66849.1; !1PID:g484015 CLASSIFICATION #superfamily papillomavirus E6 protein KEYWORDS DNA binding; early protein; zinc finger SUMMARY #length 135 #molecular-weight 15869 #checksum 6246 SEQUENCE /// ENTRY W6WLEB #type complete TITLE E6 protein - bovine papillomavirus type 1 ORGANISM #formal_name bovine papillomavirus type 1 DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 28-Jul-2000 ACCESSIONS C18151 REFERENCE A93289 !$#authors Chen, E.Y.; Howley, P.M.; Levinson, A.D.; Seeburg, P.H. !$#journal Nature (1982) 299:529-534 !$#title The primary structure and genetic organization of the bovine !1papillomavirus type 1 genome. !$#cross-references MUID:83012974; PMID:6289124 !$#accession C18151 !'##molecule_type DNA !'##residues 1-137 ##label CHE !'##cross-references GB:X02346; GB:J02044; GB:M24622; GB:X00473; !1NID:g60965; PIDN:CAB46509.1; PID:g5419932 REFERENCE A92993 !$#authors Danos, O.; Engel, L.W.; Chen, E.Y.; Yaniv, M.; Howley, P.M. !$#journal J. Virol. (1983) 46:557-566 !$#title Comparative analysis of the human type 1a and bovine type 1 !1papillomavirus genomes. !$#cross-references MUID:83189357; PMID:6302319 !$#contents annotation REFERENCE A94282 !$#authors Androphy, E.J.; Schiller, J.T.; Lowy, D.R. !$#journal Science (1985) 230:442-445 !$#title Identification of the protein encoded by the E6 transforming !1gene of bovine papillomavirus. !$#cross-references MUID:86018841; PMID:2996134 !$#contents annotation; identification of the protein COMMENT This protein is present in the cell nucleus and the cellular !1membrane. CLASSIFICATION #superfamily papillomavirus E6 protein KEYWORDS DNA binding; early protein; transforming protein; zinc !1finger SUMMARY #length 137 #molecular-weight 15850 #checksum 8175 SEQUENCE /// ENTRY W6WLB2 #type complete TITLE E6 protein - bovine papillomavirus type 2 ORGANISM #formal_name bovine papillomavirus type 2 DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 12-Jun-1998 ACCESSIONS H31169 REFERENCE A94519 !$#authors Groff, D.E.; Mitra, R.; Lancaster, W.D. !$#submission submitted to GenBank, May 1988 !$#accession H31169 !'##molecule_type DNA !'##residues 1-139 ##label GRO !'##cross-references GB:M20219; GB:M19551; NID:g332996 CLASSIFICATION #superfamily papillomavirus E6 protein KEYWORDS DNA binding; early protein; zinc finger FEATURE !$17-55 #region zinc finger CCCC motif\ !$90-129 #region zinc finger CCCC motif SUMMARY #length 139 #molecular-weight 16093 #checksum 5019 SEQUENCE /// ENTRY W6WLB4 #type complete TITLE E6 protein - bovine papillomavirus type 4 ORGANISM #formal_name bovine papillomavirus type 4 DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 31-Dec-1993 ACCESSIONS B27129 REFERENCE A92795 !$#authors Patel, K.R.; Smith, K.T.; Campo, M.S. !$#journal J. Gen. Virol. (1987) 68:2117-2128 !$#title The nucleotide sequence and genome organization of bovine !1papillomavirus type 4. !$#cross-references MUID:87282264; PMID:3039043 !$#accession B27129 !'##molecule_type DNA !'##residues 1-99 ##label PAT !'##cross-references GB:X05817 CLASSIFICATION #superfamily bovine papillomavirus type 4 E6 protein KEYWORDS early protein SUMMARY #length 99 #molecular-weight 10951 #checksum 3081 SEQUENCE /// ENTRY W7WLHS #type complete TITLE E7 protein - human papillomavirus type 16 ORGANISM #formal_name human papillomavirus type 16 DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 20-Aug-1999 ACCESSIONS A03688; S12367; T10428 REFERENCE A22355 !$#authors Seedorf, K.; Krammer, G.; Durst, M.; Suhai, S.; Rowekamp, !1W.G. !$#journal Virology (1985) 145:181-185 !$#title Human papillomavirus type 16 DNA sequence. !$#cross-references MUID:85246220; PMID:2990099 !$#accession A03688 !'##molecule_type DNA !'##residues 1-98 ##label SEE !'##cross-references GB:K02718; NID:g333031; PIDN:AAA46940.1; !1PID:g333033 REFERENCE S12367 !$#authors Barbosa, M.S.; Edmonds, C.; Fisher, C.; Schiller, J.T.; !1Lowy, D.R.; Vousden, K.H. !$#journal EMBO J. (1990) 9:153-160 !$#title The region of the HPV E7 oncoprotein homologous to !1adenovirus E1a and SV40 large T antigen contains separate !1domains for Rb binding and casein kinase II phosphorylation. !$#cross-references MUID:90107938; PMID:2153075 !$#accession S12367 !'##status preliminary !'##molecule_type protein !'##residues 1-98 ##label BAR REFERENCE Z17014 !$#authors Kennedy, I.M.; Haddow, J.K.; Clements, J.B. !$#journal J. Virol. (1991) 65:2093-2097 !$#title A negative element in the human poapillomavirus type 16 !1genome acts at the level of late mRNA stability. !$#cross-references MUID:91162763; PMID:1848319 !$#accession T10428 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-98 ##label KEN !'##cross-references EMBL:K02718; NID:g333031; PIDN:AAA46940.1; !1PID:g333033 GENETICS !$#gene E7 CLASSIFICATION #superfamily papillomavirus E7 protein KEYWORDS DNA binding; early protein; transcription regulation; zinc !1finger FEATURE !$58-94 #region zinc finger CCCC motif SUMMARY #length 98 #molecular-weight 11022 #checksum 9842 SEQUENCE /// ENTRY W7WL31 #type complete TITLE E7 protein - human papillomavirus type 31 ORGANISM #formal_name human papillomavirus type 31 #note host Homo sapiens (man) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS B32444 REFERENCE A94398 !$#authors Goldsborough, M.D.; DiSilvestre, D.; Temple, G.F.; Lorincz, !1A.T. !$#journal Virology (1989) 171:306-311 !$#title Nucleotide sequence of human papillomavirus type 31: a !1cervical neoplasia-associated virus. !$#cross-references MUID:89299478; PMID:2545036 !$#accession B32444 !'##status translation not shown !'##molecule_type DNA !'##residues 1-98 ##label GOL !'##cross-references GB:J04353; NID:g333048; PIDN:AAA46951.1; !1PID:g459917 COMMENT This protein may be involved in the oncogenic potential of !1this virus. CLASSIFICATION #superfamily papillomavirus E7 protein KEYWORDS DNA binding; early protein; transcription regulation; zinc !1finger FEATURE !$58-94 #region zinc finger CCCC motif SUMMARY #length 98 #molecular-weight 10918 #checksum 2201 SEQUENCE /// ENTRY W7WL35 #type complete TITLE E7 protein - human papillomavirus type 35 ORGANISM #formal_name human papillomavirus type 35 #note host Homo sapiens (man) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 23-Mar-2001 ACCESSIONS F40824; S36522 REFERENCE A40824 !$#authors Marich, J.E.; Pontsler, A.V.; Rice, S.M.; McGraw, K.A.; !1Dubensky, T.W. !$#journal Virology (1992) 186:770-776 !$#title The phylogenetic relationship and complete nucleotide !1sequence of human papillomavirus type 35. !$#cross-references MUID:92124753; PMID:1310198 !$#accession F40824 !'##status translation not shown !'##molecule_type DNA !'##residues 1-99 ##label MAR !'##cross-references GB:M74117; NID:g333050; PIDN:AAA46967.1; !1PID:g333052 REFERENCE S36469 !$#authors Delius, H.; Hofmann, B. !$#submission submitted to the EMBL Data Library, August 1993 !$#description Primer-directed sequencing of human papillomavirus types. !$#accession S36522 !'##status preliminary !'##molecule_type DNA !'##residues 1-99 ##label DEL !'##cross-references EMBL:X74477; NID:g396997; PIDN:CAA52562.1; !1PID:g396999 !'##experimental_source strain 35H CLASSIFICATION #superfamily papillomavirus E7 protein KEYWORDS DNA binding; early protein; transcription regulation; zinc !1finger FEATURE !$59-95 #region zinc finger CCCC motif SUMMARY #length 99 #molecular-weight 10954 #checksum 3403 SEQUENCE /// ENTRY W7WL33 #type complete TITLE E7 protein - human papillomavirus type 33 ORGANISM #formal_name human papillomavirus type 33 DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 16-Jul-1999 ACCESSIONS A03689; S23831; S23827 REFERENCE A93020 !$#authors Cole, S.T.; Streeck, R.E. !$#journal J. Virol. (1986) 58:991-995 !$#title Genome organization and nucleotide sequence of human !1papillomavirus type 33, which is associated with cervical !1cancer. !$#cross-references MUID:86200464; PMID:3009902 !$#accession A03689 !'##molecule_type DNA !'##residues 1-97 ##label COL !'##cross-references GB:M12732; NID:g333049; PIDN:AAA46959.1; !1PID:g463178 REFERENCE S19906 !$#authors Snijders, P.J.F.; van den Brule, A.J.C.; Schrijnemakers, !1H.F.J.; Raaphorst, P.M.C.; Meijer, C.J.L.M.; Walboomers, !1J.M.M. !$#submission submitted to the EMBL Data Library, January 1992 !$#description HPV type 33 in a tonsillar carcinoma generates its putative !1E7 mRNA via two E6 transcript species which are terminated !1at different early region poly (A) sites. !$#accession S23831 !'##status preliminary !'##molecule_type mRNA !'##residues 1-97 ##label SNI !'##cross-references EMBL:X64085; NID:g60278; PIDN:CAA45434.1; !1PID:g60281; EMBL:X64084; NID:g60273; PID:g60276 CLASSIFICATION #superfamily papillomavirus E7 protein KEYWORDS DNA binding; early protein; transcription regulation; zinc !1finger FEATURE !$58-94 #region zinc finger CCCC motif SUMMARY #length 97 #molecular-weight 10837 #checksum 9340 SEQUENCE /// ENTRY W7WL58 #type complete TITLE E7 protein - human papillomavirus type 58 ORGANISM #formal_name human papillomavirus type 58 #note host Homo sapiens (man) DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 21-Jul-2000 ACCESSIONS F36779 REFERENCE A36779 !$#authors Kirii, Y.; Iwamoto, S.; Matsukura, T. !$#journal Virology (1991) 185:424-427 !$#title Human papillomavirus type 58 DNA sequence. !$#cross-references MUID:92024102; PMID:1656594 !$#accession F36779 !'##status translation not shown !'##molecule_type DNA !'##residues 1-98 ##label KIR !'##cross-references GB:D90400; NID:g222386; PIDN:BAA31846.1; !1PID:g3337099 CLASSIFICATION #superfamily papillomavirus E7 protein KEYWORDS DNA binding; early protein; transcription regulation; zinc !1finger FEATURE !$59-95 #region zinc finger CCCC motif SUMMARY #length 98 #molecular-weight 10819 #checksum 1776 SEQUENCE /// ENTRY W7WL11 #type complete TITLE E7 protein - human papillomavirus type 11 ORGANISM #formal_name human papillomavirus type 11 DATE 13-Aug-1986 #sequence_revision 13-Aug-1986 #text_change 16-Jul-1999 ACCESSIONS A03690 REFERENCE A94338 !$#authors Dartmann, K.; Schwarz, E.; Gissmann, L.; zur Hausen, H. !$#journal Virology (1986) 151:124-130 !$#title The nucleotide sequence and genome organization of human !1papilloma virus type 11. !$#cross-references MUID:86181601; PMID:3008427 !$#accession A03690 !'##molecule_type DNA !'##residues 1-98 ##label DAR !'##cross-references GB:M14119; NID:g333026; PIDN:AAA46928.1; !1PID:g496194 CLASSIFICATION #superfamily papillomavirus E7 protein KEYWORDS DNA binding; early protein; transcription regulation; zinc !1finger FEATURE !$58-94 #region zinc finger CCCC motif SUMMARY #length 98 #molecular-weight 10889 #checksum 1088 SEQUENCE /// ENTRY W7WL6 #type complete TITLE E7 protein - human papillomavirus type 6b ORGANISM #formal_name human papillomavirus type 6b DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Jul-1999 ACCESSIONS D20558 REFERENCE A90975 !$#authors Schwarz, E.; Durst, M.; Demankowski, C.; Lattermann, O.; !1Zech, R.; Wolfsperger, E.; Suhai, S.; zur Hausen, H. !$#journal EMBO J. (1983) 2:2341-2348 !$#title DNA sequence and genome organization of genital human !1papillomavirus type 6b. !$#cross-references MUID:84131949; PMID:6321162 !$#accession D20558 !'##molecule_type DNA !'##residues 1-98 ##label SCH !'##cross-references GB:X00203; NID:g60955; PIDN:CAA25019.1; PID:g60957 CLASSIFICATION #superfamily papillomavirus E7 protein KEYWORDS DNA binding; early protein; transcription regulation; zinc !1finger FEATURE !$58-94 #region zinc finger CCCC motif SUMMARY #length 98 #molecular-weight 10887 #checksum 1944 SEQUENCE /// ENTRY W7WL13 #type complete TITLE E7 protein - human papillomavirus type 13 ORGANISM #formal_name human papillomavirus type 13 #note host Homo sapiens (man) DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS B42955 REFERENCE A42955 !$#authors van Ranst, M.; Fuse, A.; Fiten, P.; Beuken, E.; Pfister, H.; !1Burk, R.D.; Opdenakker, G. !$#journal Virology (1992) 190:587-596 !$#title Human papillomavirus type 13 and pygmy chimpanzee !1papillomavirus type 1: Comparison of the genome !1organizations. !$#cross-references MUID:92391075; PMID:1325697 !$#accession B42955 !'##molecule_type DNA !'##residues 1-101 ##label VAN !'##cross-references EMBL:X62843; NID:g60295; PIDN:CAA44648.1; !1PID:g60297 CLASSIFICATION #superfamily papillomavirus E7 protein KEYWORDS DNA binding; early protein; transcription regulation; zinc !1finger FEATURE !$61-97 #region zinc finger CCCC motif SUMMARY #length 101 #molecular-weight 11048 #checksum 1068 SEQUENCE /// ENTRY W7WLC1 #type complete TITLE E7 protein - pygmy chimpanzee papillomavirus (type 1) ORGANISM #formal_name pygmy chimpanzee papillomavirus DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS B36818 REFERENCE A42955 !$#authors van Ranst, M.; Fuse, A.; Fiten, P.; Beuken, E.; Pfister, H.; !1Burk, R.D.; Opdenakker, G. !$#journal Virology (1992) 190:587-596 !$#title Human papillomavirus type 13 and pygmy chimpanzee !1papillomavirus type 1: Comparison of the genome !1organizations. !$#cross-references MUID:92391075; PMID:1325697 !$#accession B36818 !'##molecule_type DNA !'##residues 1-98 ##label VAN !'##cross-references EMBL:X62844; NID:g61010; PIDN:CAA44656.1; !1PID:g61012 CLASSIFICATION #superfamily papillomavirus E7 protein KEYWORDS DNA binding; early protein; transcription regulation; !1transforming protein; zinc finger FEATURE !$58-94 #region zinc finger CCCC motif SUMMARY #length 98 #molecular-weight 10742 #checksum 1791 SEQUENCE /// ENTRY W7WL41 #type complete TITLE E7 protein - human papillomavirus type 41 ORGANISM #formal_name human papillomavirus type 41 #note host Homo sapiens (man) DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 10-Sep-1999 ACCESSIONS B43550 REFERENCE A43550 !$#authors Hirt, L.; Hirsch-Behnam, A.; De Villiers, E.M. !$#journal Virus Res. (1990) 18:179-190 !$#title Nucleotide sequence of human papillomavirus (HPV) type 41: !1an unusual HPV type without a typical E2 binding site !1consensus sequence. !$#accession B43550 !'##status translation not shown !'##molecule_type DNA !'##residues 1-114 ##label HIR !'##cross-references EMBL:X56147; NID:g60942; PIDN:CAA39613.1; !1PID:g60944 CLASSIFICATION #superfamily papillomavirus E7 protein KEYWORDS DNA binding; early protein; transcription regulation; !1transforming protein; zinc finger FEATURE !$62-99 #region zinc finger CCCC motif SUMMARY #length 114 #molecular-weight 12804 #checksum 3935 SEQUENCE /// ENTRY W7WL42 #type complete TITLE E7 protein - human papillomavirus type 42 ORGANISM #formal_name human papillomavirus type 42 #note host Homo sapiens (man) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Feb-1997 ACCESSIONS F39451 REFERENCE A39451 !$#authors Philipp, W.; Honore, N.; Sapp, M.; Cole, S.T.; Streeck, R.E. !$#journal Virology (1992) 186:331-334 !$#title Human papillomavirus type 42: new sequence, conserved genome !1organization. !$#cross-references MUID:92087479; PMID:1309278 !$#accession F39451 !'##status translation not shown !'##molecule_type DNA !'##residues 1-93 ##label PHI !'##cross-references GB:M73236 CLASSIFICATION #superfamily papillomavirus E7 protein KEYWORDS DNA binding; early protein; transcription regulation SUMMARY #length 93 #molecular-weight 10679 #checksum 6450 SEQUENCE /// ENTRY W7WLR1 #type complete TITLE E7 protein - rhesus papillomavirus (type 1) ORGANISM #formal_name rhesus papillomavirus DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Feb-1997 ACCESSIONS B38503 REFERENCE A38503 !$#authors Ostrow, R.S.; LaBresh, K.V.; Faras, A.J. !$#journal Virology (1991) 181:424-429 !$#title Characterization of the complete RhPV 1 genomic sequence and !1an integration locus from a metastatic tumor. !$#cross-references MUID:91135018; PMID:1847267 !$#accession B38503 !'##status translation not shown !'##molecule_type DNA !'##residues 1-113 ##label OST !'##cross-references EMBL:M37717 CLASSIFICATION #superfamily papillomavirus E7 protein KEYWORDS DNA binding; early protein; transcription regulation SUMMARY #length 113 #molecular-weight 12818 #checksum 7614 SEQUENCE /// ENTRY W7WL51 #type complete TITLE E7 protein - human papillomavirus type 51 ORGANISM #formal_name human papillomavirus type 51 #note host Homo sapiens (man) DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Feb-1997 ACCESSIONS F40415 REFERENCE A40415 !$#authors Lungu, O.; Crum, C.P.; Silverstein, S.J. !$#journal J. Virol. (1991) 65:4216-4225 !$#title Biologic properties and nucleotide sequence analysis of !1human papillomavirus type 51. !$#cross-references MUID:91303675; PMID:1649326 !$#accession F40415 !'##status translation not shown !'##molecule_type DNA !'##residues 1-101 ##label LUN !'##cross-references GB:M62877 CLASSIFICATION #superfamily papillomavirus E7 protein KEYWORDS DNA binding; early protein; transcription regulation SUMMARY #length 101 #molecular-weight 11339 #checksum 1028 SEQUENCE /// ENTRY W7WL18 #type complete TITLE E7 protein - human papillomavirus type 18 ORGANISM #formal_name human papillomavirus type 18 DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Jul-1999 ACCESSIONS B26165; H26251 REFERENCE A91068 !$#authors Seedorf, K.; Oltersdorf, T.; Kraemmer, G.; Roewekamp, W. !$#journal EMBO J. (1987) 6:139-144 !$#title Identification of early proteins of the human papilloma !1viruses type 16 (HPV 16) and type 18 (HPV 18) in cervical !1carcinoma cells. !$#cross-references MUID:87218459; PMID:3034571 !$#accession B26165 !'##molecule_type DNA !'##residues 1-105 ##label SEE !'##cross-references GB:X04773; NID:g60876; PIDN:CAA28467.1; PID:g60878 REFERENCE A92937 !$#authors Cole, S.T.; Danos, O. !$#journal J. Mol. Biol. (1987) 193:599-608 !$#title Nucleotide sequence and comparative analysis of the human !1papillomavirus type 18 genome. Phylogeny of papillomaviruses !1and repeated structure of the E6 and E7 gene products. !$#cross-references MUID:87283882; PMID:3039146 !$#accession H26251 !'##molecule_type DNA !'##residues 1-105 ##label COL !'##cross-references GB:X05015; NID:g60975; PIDN:CAA28665.1; PID:g60977 CLASSIFICATION #superfamily papillomavirus E7 protein KEYWORDS DNA binding; early protein; transcription regulation SUMMARY #length 105 #molecular-weight 11995 #checksum 3076 SEQUENCE /// ENTRY W7WLPR #type complete TITLE E7 protein - human papillomavirus type ME180 (provirus) ORGANISM #formal_name human papillomavirus type ME180 #note host Homo sapiens (man) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 28-Jul-2000 ACCESSIONS D40509 REFERENCE A40509 !$#authors Reuter, S.; Delius, H.; Kahn, T.; Hofmann, B.; zur Hausen, !1H.; Schwarz, E. !$#journal J. Virol. (1991) 65:5564-5568 !$#title Characterization of a novel human papillomavirus DNA in the !1cervical carcinoma cell line ME180. !$#cross-references MUID:91374616; PMID:1716694 !$#accession D40509 !'##status translation not shown !'##molecule_type DNA !'##residues 1-110 ##label REU !'##cross-references GB:M73258; NID:g184383; PIDN:AAF14012.1; !1PID:g6478872 CLASSIFICATION #superfamily papillomavirus E7 protein KEYWORDS DNA binding; early protein; transcription regulation SUMMARY #length 110 #molecular-weight 12672 #checksum 2391 SEQUENCE /// ENTRY W7WL39 #type complete TITLE E7 protein - human papillomavirus type 39 ORGANISM #formal_name human papillomavirus type 39 #note host Homo sapiens (man) DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jul-1999 ACCESSIONS B38502 REFERENCE A38502 !$#authors Volpers, C.; Streeck, R.E. !$#journal Virology (1991) 181:419-423 !$#title Genome organization and nucleotide sequence of human !1papillomavirus type 39. !$#cross-references MUID:91135017; PMID:1847266 !$#accession B38502 !'##status translation not shown !'##molecule_type DNA !'##residues 1-109 ##label VOL !'##cross-references GB:M62849; EMBL:M38185; NID:g333245; !1PIDN:AAA47051.1; PID:g463187 CLASSIFICATION #superfamily papillomavirus E7 protein KEYWORDS DNA binding; early protein; transcription regulation SUMMARY #length 109 #molecular-weight 12497 #checksum 8555 SEQUENCE /// ENTRY W7WL8 #type complete TITLE E7 protein - human papillomavirus type 8 ORGANISM #formal_name human papillomavirus type 8 DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 07-Nov-1997 ACCESSIONS A03691 REFERENCE A93019 !$#authors Fuchs, P.G.; Iftner, T.; Weninger, J.; Pfister, H. !$#journal J. Virol. (1986) 58:626-634 !$#title Epidermodysplasia verruciformis-associated human !1papillomavirus 8: genomic sequence and comparative analysis. !$#cross-references MUID:86200410; PMID:3009874 !$#accession A03691 !'##molecule_type DNA !'##residues 1-103 ##label FUC !'##cross-references GB:M12737; NID:g333074 !'##note this ORF is not annotated in GenBank entry PPH8CG CLASSIFICATION #superfamily papillomavirus E7 protein KEYWORDS DNA binding; early protein; transcription regulation SUMMARY #length 103 #molecular-weight 11629 #checksum 4522 SEQUENCE /// ENTRY W7WL47 #type complete TITLE E7 protein - human papillomavirus type 47 ORGANISM #formal_name human papillomavirus type 47 #note host Homo sapiens (man) DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Jul-1999 ACCESSIONS B35324 REFERENCE A35324 !$#authors Kiyono, T.; Adachi, A.; Ishibashi, M. !$#journal Virology (1990) 177:401-405 !$#title Genome organization and taxonomic position of human !1papillomavirus type 47 inferred from its DNA sequence. !$#cross-references MUID:90281611; PMID:2162112 !$#accession B35324 !'##status translation not shown !'##molecule_type DNA !'##residues 1-103 ##label KIY !'##cross-references GB:M32305; NID:g333062; PIDN:AAA46977.1; !1PID:g333065 CLASSIFICATION #superfamily papillomavirus E7 protein KEYWORDS DNA binding; early protein; transcription regulation SUMMARY #length 103 #molecular-weight 11567 #checksum 3793 SEQUENCE /// ENTRY W7WL5 #type complete TITLE E7 protein - human papillomavirus type 5 ORGANISM #formal_name human papillomavirus type 5 DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Jul-1999 ACCESSIONS G26277 REFERENCE A94360 !$#authors Zachow, K.R.; Ostrow, R.S.; Faras, A.J. !$#journal Virology (1987) 158:251-254 !$#title Nucleotide sequence and genome organization of human !1papillomavirus type 5. !$#cross-references MUID:87207670; PMID:3033892 !$#accession G26277 !'##molecule_type DNA !'##residues 1-103 ##label ZAC !'##cross-references GB:M17463; NID:g333071; PIDN:AAA46984.1; !1PID:g484216 CLASSIFICATION #superfamily papillomavirus E7 protein KEYWORDS DNA binding; early protein; transcription regulation SUMMARY #length 103 #molecular-weight 11677 #checksum 4489 SEQUENCE /// ENTRY W7WLB5 #type complete TITLE E7 protein - human papillomavirus type 5b ORGANISM #formal_name human papillomavirus type 5b #note host Homo sapiens (man) DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jun-2000 ACCESSIONS F40480 REFERENCE A40480 !$#authors Yabe, Y.; Sakai, A.; Hitsumoto, T.; Kato, H.; Ogura, H. !$#journal Virology (1991) 183:793-798 !$#title A subtype of human papillomavirus 5 (HPV-5b) and its !1subgenomic segment amplified in a carcinoma: nucleotide !1sequences and genomic organizations. !$#cross-references MUID:91306467; PMID:1649510 !$#accession F40480 !'##status translation not shown !'##molecule_type DNA !'##residues 1-103 ##label YAB !'##cross-references GB:D90252; NID:g222395; PIDN:BAA14293.1; !1PID:g222399 CLASSIFICATION #superfamily papillomavirus E7 protein KEYWORDS DNA binding; early protein; transcription regulation SUMMARY #length 103 #molecular-weight 11699 #checksum 4246 SEQUENCE /// ENTRY W7WL #type complete TITLE E7 protein - human papillomavirus type 1a ORGANISM #formal_name human papillomavirus type 1a DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Jul-1999 ACCESSIONS C17475 REFERENCE A90970 !$#authors Danos, O.; Katinka, M.; Yaniv, M. !$#journal EMBO J. (1982) 1:231-236 !$#title Human papillomavirus 1a complete DNA sequence: a novel type !1of genome organization among papovaviridae. !$#cross-references MUID:84182467; PMID:6325156 !$#accession C17475 !'##molecule_type DNA !'##residues 1-93 ##label DAN !'##cross-references GB:V01116; GB:X03321; NID:g60966; PIDN:CAA24316.1; !1PID:g60969 REFERENCE A92993 !$#authors Danos, O.; Engel, L.W.; Chen, E.Y.; Yaniv, M.; Howley, P.M. !$#journal J. Virol. (1983) 46:557-566 !$#title Comparative analysis of the human type 1a and bovine type 1 !1papillomavirus genomes. !$#cross-references MUID:83189357; PMID:6302319 !$#contents annotation CLASSIFICATION #superfamily papillomavirus E7 protein KEYWORDS DNA binding; early protein; transcription regulation SUMMARY #length 93 #molecular-weight 10500 #checksum 7101 SEQUENCE /// ENTRY S15615 #type complete TITLE E7 protein - human papillomavirus type 2a ORGANISM #formal_name human papillomavirus type 2a #note host Homo sapiens (man) DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 10-Sep-1999 ACCESSIONS S15615 REFERENCE S15614 !$#authors Hirsch-Behnam, A.; Delius, H.; de Villiers, E.M. !$#journal Virus Res. (1990) 18:81-98 !$#title A comparative sequence analysis of two human papillomavirus !1(HPV) types 2a and 57. !$#cross-references MUID:91188699; PMID:1964523 !$#accession S15615 !'##molecule_type DNA !'##residues 1-92 ##label HIR !'##cross-references EMBL:X55964 CLASSIFICATION #superfamily papillomavirus E7 protein KEYWORDS DNA binding; early protein; transcription regulation; zinc !1finger FEATURE !$55-91 #region zinc finger CCCC motif SUMMARY #length 92 #molecular-weight 10369 #checksum 2642 SEQUENCE /// ENTRY S15622 #type complete TITLE E7 protein - human papillomavirus type 57 ORGANISM #formal_name human papillomavirus type 57 #note host Homo sapiens (man) DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 10-Sep-1999 ACCESSIONS S15622 REFERENCE S15614 !$#authors Hirsch-Behnam, A.; Delius, H.; de Villiers, E.M. !$#journal Virus Res. (1990) 18:81-98 !$#title A comparative sequence analysis of two human papillomavirus !1(HPV) types 2a and 57. !$#cross-references MUID:91188699; PMID:1964523 !$#accession S15622 !'##molecule_type DNA !'##residues 1-92 ##label HIR !'##cross-references EMBL:X55965; NID:g60882; PIDN:CAA39431.1; !1PID:g60884 CLASSIFICATION #superfamily papillomavirus E7 protein KEYWORDS DNA binding; early protein; transcription regulation; zinc !1finger FEATURE !$55-91 #region zinc finger CCCC motif SUMMARY #length 92 #molecular-weight 10376 #checksum 3978 SEQUENCE /// ENTRY W7WLRB #type complete TITLE E7 protein - cottontail rabbit papillomavirus ORGANISM #formal_name cottontail rabbit papillomavirus DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 16-Feb-1997 ACCESSIONS A03692 REFERENCE A94027 !$#authors Giri, I.; Danos, O.; Yaniv, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:1580-1584 !$#title Genomic structure of the cottontail rabbit (Shope) !1papillomavirus. !$#cross-references MUID:85166175; PMID:2984661 !$#accession A03692 !'##molecule_type DNA !'##residues 1-94 ##label GIR CLASSIFICATION #superfamily papillomavirus E7 protein KEYWORDS DNA binding; early protein; transcription regulation SUMMARY #length 94 #molecular-weight 10467 #checksum 7518 SEQUENCE /// ENTRY W7WLDP #type complete TITLE E7 protein - deer papillomavirus ORGANISM #formal_name deer papillomavirus DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 16-Feb-1997 ACCESSIONS A03693 REFERENCE A93013 !$#authors Groff, D.E.; Lancaster, W.D. !$#journal J. Virol. (1985) 56:85-91 !$#title Molecular cloning and nucleotide sequence of deer !1papillomavirus. !$#cross-references MUID:85293253; PMID:2993669 !$#accession A03693 !'##molecule_type DNA !'##residues 1-102 ##label GRO CLASSIFICATION #superfamily papillomavirus E7 protein KEYWORDS DNA binding; early protein; transcription regulation SUMMARY #length 102 #molecular-weight 11184 #checksum 6471 SEQUENCE /// ENTRY W7WLEP #type complete TITLE E7 protein - European elk papillomavirus ORGANISM #formal_name European elk papillomavirus DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 11-May-2000 ACCESSIONS B29499; G94457; G94506 REFERENCE A91567 !$#authors Ahola, H.; Bergman, P.; Stroem, A.C.; Moreno-Lopez, J.; !1Pettersson, U. !$#journal Gene (1986) 50:195-205 !$#title Organization and expression of the transforming region from !1the European elk papillomavirus (EEPV). !$#cross-references MUID:87219878; PMID:3034730 !$#accession B29499 !'##molecule_type DNA !'##residues 1-102 ##label AHO !'##cross-references GB:M15953; NID:g333025; PIDN:AAA66850.1; !1PID:g484016 REFERENCE A94457 !$#authors Eriksson, A. !$#citation unpublished results 1987, cited by GenBank !$#accession G94457 !'##molecule_type DNA !'##residues 1-102 ##label ERI !'##cross-references GB:M15953; NID:g333025; PIDN:AAA66850.1; !1PID:g484016 REFERENCE A94506 !$#authors Pettersson, U. !$#submission submitted to GenBank, August 1987 !$#accession G94506 !'##molecule_type DNA !'##residues 1-102 ##label PET !'##cross-references GB:M15953; NID:g333025; PIDN:AAA66850.1; !1PID:g484016 CLASSIFICATION #superfamily papillomavirus E7 protein KEYWORDS DNA binding; early protein; transcription regulation SUMMARY #length 102 #molecular-weight 11228 #checksum 6788 SEQUENCE /// ENTRY W7WLEB #type complete TITLE E7 protein - bovine papillomavirus type 1 ORGANISM #formal_name bovine papillomavirus type 1 DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 28-Jul-2000 ACCESSIONS D18151 REFERENCE A93289 !$#authors Chen, E.Y.; Howley, P.M.; Levinson, A.D.; Seeburg, P.H. !$#journal Nature (1982) 299:529-534 !$#title The primary structure and genetic organization of the bovine !1papillomavirus type 1 genome. !$#cross-references MUID:83012974; PMID:6289124 !$#accession D18151 !'##molecule_type DNA !'##residues 1-127 ##label CHE !'##cross-references GB:X02346; GB:J02044; GB:M24622; GB:X00473; !1NID:g60965; PIDN:CAB46510.1; PID:g5419933 REFERENCE A92993 !$#authors Danos, O.; Engel, L.W.; Chen, E.Y.; Yaniv, M.; Howley, P.M. !$#journal J. Virol. (1983) 46:557-566 !$#title Comparative analysis of the human type 1a and bovine type 1 !1papillomavirus genomes. !$#cross-references MUID:83189357; PMID:6302319 !$#contents annotation CLASSIFICATION #superfamily papillomavirus E7 protein KEYWORDS early protein SUMMARY #length 127 #molecular-weight 13636 #checksum 8448 SEQUENCE /// ENTRY W7WLB2 #type complete TITLE E7 protein - bovine papillomavirus type 2 ORGANISM #formal_name bovine papillomavirus type 2 DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 12-Jun-1998 ACCESSIONS I31169 REFERENCE A94519 !$#authors Groff, D.E.; Mitra, R.; Lancaster, W.D. !$#submission submitted to GenBank, May 1988 !$#accession I31169 !'##molecule_type DNA !'##residues 1-136 ##label GRO !'##cross-references GB:M20219; GB:M19551; NID:g332996 CLASSIFICATION #superfamily papillomavirus E7 protein KEYWORDS early protein SUMMARY #length 136 #molecular-weight 14446 #checksum 8921 SEQUENCE /// ENTRY W7WLB4 #type complete TITLE E7 protein - bovine papillomavirus type 4 ORGANISM #formal_name bovine papillomavirus type 4 DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 24-Feb-1994 ACCESSIONS C27129 REFERENCE A92795 !$#authors Patel, K.R.; Smith, K.T.; Campo, M.S. !$#journal J. Gen. Virol. (1987) 68:2117-2128 !$#title The nucleotide sequence and genome organization of bovine !1papillomavirus type 4. !$#cross-references MUID:87282264; PMID:3039043 !$#accession C27129 !'##molecule_type DNA !'##residues 1-76 ##label PAT CLASSIFICATION #superfamily bovine papillomavirus type 4 E7 protein KEYWORDS early protein SUMMARY #length 76 #molecular-weight 8740 #checksum 9527 SEQUENCE /// ENTRY W8WLB2 #type complete TITLE E8 protein - bovine papillomavirus type 2 ORGANISM #formal_name bovine papillomavirus type 2 DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 12-Jun-1998 ACCESSIONS A31178 REFERENCE A94519 !$#authors Groff, D.E.; Mitra, R.; Lancaster, W.D. !$#submission submitted to GenBank, May 1988 !$#accession A31178 !'##molecule_type DNA !'##residues 1-109 ##label GRO !'##cross-references GB:M20219; GB:M19551; NID:g332996 CLASSIFICATION #superfamily papillomavirus type 2 E8 protein KEYWORDS early protein SUMMARY #length 109 #molecular-weight 12844 #checksum 9971 SEQUENCE /// ENTRY W8WLB4 #type complete TITLE E8 protein - bovine papillomavirus type 4 ORGANISM #formal_name bovine papillomavirus type 4 DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jun-2000 ACCESSIONS A27129 REFERENCE A92795 !$#authors Patel, K.R.; Smith, K.T.; Campo, M.S. !$#journal J. Gen. Virol. (1987) 68:2117-2128 !$#title The nucleotide sequence and genome organization of bovine !1papillomavirus type 4. !$#cross-references MUID:87282264; PMID:3039043 !$#accession A27129 !'##molecule_type DNA !'##residues 1-52 ##label PAT !'##cross-references GB:D00146; NID:g222360; PIDN:BAA00094.1; !1PID:g222361 CLASSIFICATION #superfamily bovine papillomavirus type 4 E8 protein KEYWORDS early protein SUMMARY #length 52 #molecular-weight 6342 #checksum 6907 SEQUENCE /// ENTRY UYPVP1 #type complete TITLE noncapsid protein NS1 - bovine parvovirus ORGANISM #formal_name bovine parvovirus DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 08-Apr-1994 ACCESSIONS B26104 REFERENCE A26104 !$#authors Chen, K.C.; Shull, B.C.; Moses, E.A.; Lederman, M.; Stout, !1E.R.; Bates, R.C. !$#journal J. Virol. (1986) 60:1085-1097 !$#title Complete nucleotide sequence and genome organization of !1bovine parvovirus. !$#cross-references MUID:87061184; PMID:3783814 !$#accession B26104 !'##molecule_type DNA !'##residues 1-255 ##label CHE !'##cross-references EMBL:M14363; EMBL:M21972; EMBL:M21973; EMBL:M21974; !1EMBL:M21975 CLASSIFICATION #superfamily bovine parvovirus noncapsid protein NP1 KEYWORDS noncapsid protein SUMMARY #length 255 #molecular-weight 29800 #checksum 9746 SEQUENCE /// ENTRY UYAD1A #type complete TITLE noncapsid protein NS1 - adeno-associated virus type 2 CONTAINS noncapsid protein NS2 ORGANISM #formal_name adeno-associated virus type 2 DATE 05-Apr-1983 #sequence_revision 05-Apr-1983 #text_change 16-Jul-1999 ACCESSIONS A03694 REFERENCE A03694 !$#authors Srivastava, A.; Lusby, E.W.; Berns, K.I. !$#journal J. Virol. (1983) 45:555-564 !$#title Nucleotide sequence and organization of the adeno-associated !1virus 2 genome. !$#cross-references MUID:83164299; PMID:6300419 !$#accession A03694 !'##status translation not shown !'##molecule_type DNA !'##residues 1-536 ##label SRI !'##cross-references EMBL:J01901; NID:g209616; PIDN:AAA42372.1; !1PID:g209617; EMBL:M12405; EMBL:M12468; EMBL:M12469 GENETICS !$#introns 529/2 CLASSIFICATION #superfamily parvovirus noncapsid protein KEYWORDS noncapsid protein FEATURE !$225-536 #product noncapsid protein NS2 #status predicted !8#label NS2 SUMMARY #length 536 #molecular-weight 60754 #checksum 546 SEQUENCE /// ENTRY UYPVS1 #type complete TITLE noncapsid protein NS1 - bovine parvovirus ORGANISM #formal_name bovine parvovirus DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 16-Jul-1999 ACCESSIONS C26104 REFERENCE A26104 !$#authors Chen, K.C.; Shull, B.C.; Moses, E.A.; Lederman, M.; Stout, !1E.R.; Bates, R.C. !$#journal J. Virol. (1986) 60:1085-1097 !$#title Complete nucleotide sequence and genome organization of !1bovine parvovirus. !$#cross-references MUID:87061184; PMID:3783814 !$#accession C26104 !'##molecule_type DNA !'##residues 1-726 ##label CHE !'##cross-references EMBL:M14363; NID:g333454; PIDN:AAB59845.1; !1PID:g808803; EMBL:M21972; EMBL:M21973; EMBL:M21974; !1EMBL:M21975 CLASSIFICATION #superfamily parvovirus noncapsid protein KEYWORDS noncapsid protein SUMMARY #length 726 #molecular-weight 81188 #checksum 9654 SEQUENCE /// ENTRY UYPV19 #type complete TITLE noncapsid protein NS1 - parvovirus B19 (isolate Au) ORGANISM #formal_name parvovirus B19 #note host Homo sapiens (man) DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 16-Jul-1999 ACCESSIONS B24299 REFERENCE A24299 !$#authors Shade, R.O.; Blundell, M.C.; Cotmore, S.F.; Tattersall, P.; !1Astell, C.R. !$#journal J. Virol. (1986) 58:921-936 !$#title Nucleotide sequence and genome organization of human !1parvovirus B19 isolated from the serum of a child during !1aplastic crisis. !$#cross-references MUID:86200451; PMID:3701931 !$#accession B24299 !'##molecule_type DNA !'##residues 1-671 ##label SHA !'##cross-references EMBL:M13178; NID:g333375; PIDN:AAA66866.1; !1PID:g333376 CLASSIFICATION #superfamily parvovirus noncapsid protein KEYWORDS noncapsid protein SUMMARY #length 671 #molecular-weight 74097 #checksum 3577 SEQUENCE /// ENTRY UYPVV1 #type complete TITLE noncapsid protein NS1 - parvovirus H1 ORGANISM #formal_name parvovirus H1 #note host Homo sapiens (man) DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 16-Jul-1999 ACCESSIONS A03695 REFERENCE A03695 !$#authors Rhode III, S.L.; Paradiso, P.R. !$#journal J. Virol. (1983) 45:173-184 !$#title Parvovirus genome: nucleotide sequence of H-1 and mapping of !1its genes by hybrid-arrested translation. !$#cross-references MUID:83112183; PMID:6823009 !$#accession A03695 !'##molecule_type DNA !'##residues 1-672 ##label RHO !'##cross-references EMBL:X01457; NID:g60993; PIDN:CAA25689.1; !1PID:g60994; EMBL:J02198 CLASSIFICATION #superfamily parvovirus noncapsid protein KEYWORDS noncapsid protein SUMMARY #length 672 #molecular-weight 75993 #checksum 248 SEQUENCE /// ENTRY UYPV1M #type complete TITLE noncapsid protein NS1 - minute virus of mice ORGANISM #formal_name minute virus of mice, murine parvovirus DATE 14-Nov-1983 #sequence_revision 28-Aug-1985 #text_change 08-Apr-1994 ACCESSIONS A03696 REFERENCE A03696 !$#authors Astell, C.R.; Thomson, M.; Merchlinsky, M.; Ward, D.C. !$#journal Nucleic Acids Res. (1983) 11:999-1018 !$#title The complete DNA sequence of minute virus of mice, an !1autonomous parvovirus. !$#cross-references MUID:83143341; PMID:6298737 !$#accession A03696 !'##molecule_type DNA !'##residues 1-672 ##label AST !'##cross-references EMBL:V01115 CLASSIFICATION #superfamily parvovirus noncapsid protein KEYWORDS noncapsid protein SUMMARY #length 672 #molecular-weight 76248 #checksum 2609 SEQUENCE /// ENTRY UYPVIM #type complete TITLE noncapsid protein NS1 - minute virus of mice (strain MVMi) ORGANISM #formal_name minute virus of mice, murine parvovirus DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 16-Jul-1999 ACCESSIONS A23008; A29510 REFERENCE A23008 !$#authors Sahli, R.; McMaster, G.K.; Hirt, B. !$#journal Nucleic Acids Res. (1985) 13:3617-3633 !$#title DNA sequence comparison between two tissue-specific variants !1of the autonomous parvovirus, minute virus of mice. !$#cross-references MUID:85242059; PMID:3855242 !$#accession A23008 !'##molecule_type DNA !'##residues 1-721 ##label SAH !'##cross-references EMBL:X02481 REFERENCE A29510 !$#authors Astell, C.R.; Gardiner, E.M.; Tattersall, P. !$#journal J. Virol. (1986) 57:656-669 !$#title DNA sequence of the lymphotropic variant of minute virus of !1mice, MVM(i), and comparison with the DNA sequence of the !1fibrotropic prototype strain. !$#cross-references MUID:86115415; PMID:3502703 !$#accession A29510 !'##molecule_type DNA !'##residues 1-645,'I',647-721 ##label AST !'##cross-references EMBL:M12032; NID:g332289; PIDN:AAA69566.1; !1PID:g825477 CLASSIFICATION #superfamily parvovirus noncapsid protein KEYWORDS noncapsid protein SUMMARY #length 721 #molecular-weight 81862 #checksum 1408 SEQUENCE /// ENTRY A44276 #type complete TITLE noncapsid protein NS1 - parvovirus LuIII ORGANISM #formal_name parvovirus LuIII DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 26-Feb-1999 ACCESSIONS A44276 REFERENCE A44276 !$#authors Diffoot, N.; Chen, K.C.; Bates, R.C.; Lederma, M. !$#journal Virology (1993) 192:339-345 !$#title The complete nucleotide sequence of parvovirus LuIII and !1localization of a unique sequence possibly responsible for !1its encapsidation pattern. !$#cross-references MUID:93297126; PMID:8517025 !$#accession A44276 !'##status translation not shown !'##molecule_type DNA !'##residues 1-668 ##label DIF !'##cross-references GB:M81888 CLASSIFICATION #superfamily parvovirus noncapsid protein KEYWORDS noncapsid protein SUMMARY #length 668 #molecular-weight 75845 #checksum 5007 SEQUENCE /// ENTRY UYPVCP #type complete TITLE noncapsid protein NS1 - canine parvovirus (strain N) ORGANISM #formal_name canine parvovirus, CPV DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jul-1999 ACCESSIONS A29962 REFERENCE A29962 !$#authors Reed, A.P.; Jones, E.V.; Miller, T.J. !$#journal J. Virol. (1988) 62:266-276 !$#title Nucleotide sequence and genome organization of canine !1parvovirus. !$#cross-references MUID:88062992; PMID:2824850 !$#accession A29962 !'##molecule_type DNA !'##residues 1-668 ##label REE !'##cross-references EMBL:M19296; NID:g333438; PIDN:AAA67459.1; !1PID:g333439 CLASSIFICATION #superfamily parvovirus noncapsid protein KEYWORDS noncapsid protein SUMMARY #length 668 #molecular-weight 76764 #checksum 9548 SEQUENCE /// ENTRY UYPVME #type complete TITLE noncapsid protein NS1 - mink enteritis virus (strain Abashiri) ORGANISM #formal_name mink enteritis virus, MEV DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jun-2000 ACCESSIONS A38350 REFERENCE A38350 !$#authors Kariatsumari, T.; Horiuchi, M.; Hama, E.; Yaguchi, K.; !1Ishigurio, N.; Goto, H.; Shinagawa, M. !$#journal J. Gen. Virol. (1991) 72:867-875 !$#title Construction and nucleotide sequence analysis of an !1infectious DNA clone of the autonomous parvovirus, mink !1enteritis virus. !$#cross-references MUID:91202123; PMID:2016597 !$#accession A38350 !'##molecule_type DNA !'##residues 1-668 ##label KAR !'##cross-references GB:D00765; NID:g222435; PIDN:BAA00662.1; !1PID:g222436 CLASSIFICATION #superfamily parvovirus noncapsid protein KEYWORDS noncapsid protein SUMMARY #length 668 #molecular-weight 76736 #checksum 9074 SEQUENCE /// ENTRY UYPVFP #type complete TITLE noncapsid protein NS1 - feline panleukopenia virus (strain 193) ORGANISM #formal_name feline panleukopenia virus, FPLV DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jul-1999 ACCESSIONS A36608 REFERENCE A36608 !$#authors Martyn, J.C.; Davidson, B.E.; Studdert, M.J. !$#journal J. Gen. Virol. (1990) 71:2747-2753 !$#title Nucleotide sequence of feline panleukopenia virus: !1comparison with canine parvovirus identifies host-specific !1differences. !$#cross-references MUID:91073139; PMID:2174965 !$#accession A36608 !'##molecule_type DNA !'##residues 1-668 ##label MAR !'##cross-references GB:X55115; NID:g60863; PIDN:CAA38910.1; PID:g60864 CLASSIFICATION #superfamily parvovirus noncapsid protein KEYWORDS noncapsid protein SUMMARY #length 668 #molecular-weight 76768 #checksum 9731 SEQUENCE /// ENTRY UYPV1F #type fragment TITLE noncapsid protein NS1 - feline panleukopenia virus (fragment) ORGANISM #formal_name feline panleukopenia virus, FPLV DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 16-Jul-1999 ACCESSIONS A03697 REFERENCE A03697 !$#authors Carlson, J.; Rushlow, K.; Maxwell, I.; Maxwell, F.; Winston, !1S.; Hahn, W. !$#journal J. Virol. (1985) 55:574-587 !$#title Cloning and sequence of DNA encoding structural proteins of !1the autonomous parvovirus feline panleukopenia virus. !$#cross-references MUID:85265017; PMID:2991581 !$#accession A03697 !'##molecule_type DNA !'##residues 1-392 ##label CAR !'##cross-references EMBL:M10824; NID:g333474; PIDN:AAA47160.1; !1PID:g333475 CLASSIFICATION #superfamily parvovirus noncapsid protein KEYWORDS noncapsid protein SUMMARY #length 392 #checksum 856 SEQUENCE /// ENTRY UYPVPP #type complete TITLE noncapsid protein NS1 - porcine parvovirus (strain NADL-2) ORGANISM #formal_name porcine parvovirus DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jun-2000 ACCESSIONS A33302; B36217; A33743; A36217 REFERENCE A33302 !$#authors Ranz, A.I.; Manclus, J.J.; Diaz-Aroca, E.; Casal, J.I. !$#journal J. Gen. Virol. (1989) 70:2541-2553 !$#title Porcine parvovirus: DNA sequence and genome organization. !$#cross-references MUID:90010964; PMID:2794971 !$#accession A33302 !'##molecule_type DNA !'##residues 1-660 ##label RAN !'##cross-references EMBL:D00623; NID:g303754; PIDN:BAA00501.1; !1PID:g222358 REFERENCE A36217 !$#authors Vasudevacharya, J.; Basak, S.; Srinivas, R.V.; Compans, R.W. !$#journal Virology (1990) 178:611-616 !$#title The complete nucleotide sequence of an infectious clone of !1porcine parvovirus, strain NADL-2. !$#cross-references MUID:91021005; PMID:2219713 !$#accession B36217 !'##molecule_type DNA !'##residues 1-85,'R',87-273,'R',275-375,'V',377-620,'NLH',623-624, !1'PTPPD',630,'AIR',634,'P',635-660 ##label VAS !'##cross-references EMBL:M38367; NID:g332987; PIDN:AAA46920.1; !1PID:g332989 CLASSIFICATION #superfamily parvovirus noncapsid protein KEYWORDS noncapsid protein SUMMARY #length 660 #molecular-weight 75300 #checksum 4597 SEQUENCE /// ENTRY UYPVNA #type complete TITLE noncapsid protein NS1 - porcine parvovirus (strain NADL-2) (version 2) ALTERNATE_NAMES nonstructural protein NS-1 ORGANISM #formal_name porcine parvovirus DATE 31-Dec-1990 #sequence_revision 30-Sep-1991 #text_change 16-Jul-1999 ACCESSIONS A36217; A48472; A33743 REFERENCE A36217 !$#authors Vasudevacharya, J.; Basak, S.; Srinivas, R.V.; Compans, R.W. !$#journal Virology (1990) 178:611-616 !$#title The complete nucleotide sequence of an infectious clone of !1porcine parvovirus, strain NADL-2. !$#cross-references MUID:91021005; PMID:2219713 !$#accession A36217 !'##molecule_type DNA !'##residues 1-662 ##label VAS !'##cross-references EMBL:M38367; NID:g332987; PIDN:AAA46920.1; !1PID:g332989 !'##experimental_source strain NADL-2 REFERENCE A48472 !$#authors Bergeron, J.; Menezes, J.; Tijssen, P. !$#journal Virology (1993) 197:86-98 !$#title Genomic organization and mapping of transcription and !1translation products of the NADL-2 strain of porcine !1parvovirus. !$#cross-references MUID:94025614; PMID:8212598 !$#accession A48472 !'##status preliminary !'##molecule_type DNA !'##residues 1-662 ##label BER !'##experimental_source strain NADL-2, ATCC VR-742 !'##note sequence extracted from NCBI backbone (NCBIN:138789, !1NCBIP:138790) CLASSIFICATION #superfamily parvovirus noncapsid protein KEYWORDS noncapsid protein SUMMARY #length 662 #molecular-weight 75590 #checksum 2424 SEQUENCE /// ENTRY UYPVAP #type complete TITLE noncapsid protein NS1 - Aleutian mink disease virus (strain ADV-G) ALTERNATE_NAMES left-ORF protein ORGANISM #formal_name Aleutian mink disease virus DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 06-Jan-1995 ACCESSIONS A36760; A35529 REFERENCE A36760 !$#authors Bloom, M.E.; Alexandersen, S.; Perryman, S.; Lechner, D.; !1Wolfinbarger, J.B. !$#journal J. Virol. (1988) 62:2903-2915 !$#title Nucleotide sequence and genomic organization of Aleutian !1mink disease parvovirus (ADV): sequence comparisons between !1a nonpathogenic and a pathogenic strain of ADV. !$#cross-references MUID:88275062; PMID:2839709 !$#accession A36760 !'##molecule_type DNA !'##residues 1-620 ##label BL2 !'##cross-references EMBL:M20036 CLASSIFICATION #superfamily parvovirus noncapsid protein KEYWORDS noncapsid protein SUMMARY #length 620 #molecular-weight 70920 #checksum 6061 SEQUENCE /// ENTRY UYPVAD #type complete TITLE noncapsid protein NS1 - Aedes densovirus (strain GKV 002 002) ORGANISM #formal_name Aedes densovirus #note host Aedes aegypti (yellow fever mosquito) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 08-Apr-1994 ACCESSIONS A40784 REFERENCE A40784 !$#authors Afanasiev, B.N.; Galyov, E.E.; Buchatsky, L.P.; Kozlov, Y.V. !$#journal Virology (1991) 185:323-336 !$#title Nucleotide sequence and genomic organization of Aedes !1densonucleosis virus. !$#cross-references MUID:92024090; PMID:1833875 !$#accession A40784 !'##molecule_type DNA !'##residues 1-849 ##label AFA !'##cross-references GB:M37899 CLASSIFICATION #superfamily Aedes densovirus noncapsid protein NS1 KEYWORDS noncapsid protein SUMMARY #length 849 #molecular-weight 97542 #checksum 1776 SEQUENCE /// ENTRY UYPVF1 #type fragment TITLE nonstructural protein ORF1 - silkworm densovirus (isolate Ina) (fragment) ORGANISM #formal_name silkworm densovirus #note host Bombyx mori (silkworm) DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 16-Jul-1999 ACCESSIONS A26796 REFERENCE A26796 !$#authors Bando, H.; Kusuda, J.; Gojobori, T.; Maruyama, T.; Kawase, !1S. !$#journal J. Virol. (1987) 61:553-560 !$#title Organization and nucleotide sequence of a densovirus genome !1imply a host-dependent evolution of the parvoviruses. !$#cross-references MUID:87112952; PMID:3027382 !$#accession A26796 !'##molecule_type DNA !'##residues 1-430 ##label BAN !'##cross-references EMBL:M15123; NID:g323679; PIDN:AAA67696.1; !1PID:g807602 CLASSIFICATION #superfamily silkworm densovirus nonstructural protein ORF1 KEYWORDS nonstructural protein SUMMARY #length 430 #checksum 5951 SEQUENCE /// ENTRY UYPVF3 #type complete TITLE nonstructural protein ORF3 - silkworm densovirus (isolate Ina) ORGANISM #formal_name silkworm densovirus #note host Bombyx mori (silkworm) DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 16-Jul-1999 ACCESSIONS B26796 REFERENCE A26796 !$#authors Bando, H.; Kusuda, J.; Gojobori, T.; Maruyama, T.; Kawase, !1S. !$#journal J. Virol. (1987) 61:553-560 !$#title Organization and nucleotide sequence of a densovirus genome !1imply a host-dependent evolution of the parvoviruses. !$#cross-references MUID:87112952; PMID:3027382 !$#accession B26796 !'##molecule_type DNA !'##residues 1-167 ##label BAN !'##cross-references EMBL:M15123; NID:g323679; PIDN:AAA67697.1; !1PID:g807603 CLASSIFICATION #superfamily silkworm densovirus nonstructural protein ORF3 KEYWORDS nonstructural protein SUMMARY #length 167 #molecular-weight 18955 #checksum 5777 SEQUENCE /// ENTRY VCPV3A #type complete TITLE coat protein - adeno-associated virus type 2 ORGANISM #formal_name adeno-associated virus type 2 DATE 05-Apr-1983 #sequence_revision 05-Apr-1983 #text_change 16-Jul-1999 ACCESSIONS A03698 REFERENCE A03694 !$#authors Srivastava, A.; Lusby, E.W.; Berns, K.I. !$#journal J. Virol. (1983) 45:555-564 !$#title Nucleotide sequence and organization of the adeno-associated !1virus 2 genome. !$#cross-references MUID:83164299; PMID:6300419 !$#accession A03698 !'##status translation not shown !'##molecule_type DNA !'##residues 1-504 ##label SRI !'##cross-references EMBL:J01901; NID:g209616; PIDN:AAA42376.1; !1PID:g209621; EMBL:M12405; EMBL:M12468; EMBL:M12469 CLASSIFICATION #superfamily adeno-associated virus coat protein KEYWORDS coat protein SUMMARY #length 504 #molecular-weight 56366 #checksum 3862 SEQUENCE /// ENTRY VCPVF2 #type complete TITLE structural protein ORF2 - silkworm densovirus (isolate Ina) ORGANISM #formal_name silkworm densovirus #note host Bombyx mori (silkworm) DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 16-Jul-1999 ACCESSIONS C26796 REFERENCE A26796 !$#authors Bando, H.; Kusuda, J.; Gojobori, T.; Maruyama, T.; Kawase, !1S. !$#journal J. Virol. (1987) 61:553-560 !$#title Organization and nucleotide sequence of a densovirus genome !1imply a host-dependent evolution of the parvoviruses. !$#cross-references MUID:87112952; PMID:3027382 !$#accession C26796 !'##molecule_type DNA !'##residues 1-885 ##label BAN !'##cross-references EMBL:M15123; NID:g323679; PIDN:AAA67698.1; !1PID:g807604 CLASSIFICATION #superfamily silkworm densovirus structural protein ORF2 KEYWORDS structural protein SUMMARY #length 885 #molecular-weight 100958 #checksum 8690 SEQUENCE /// ENTRY VCPVAD #type complete TITLE coat protein VP1 - Aedes densovirus (strain GKV 002 002) ORGANISM #formal_name Aedes densovirus #note host Aedes aegypti (yellow fever mosquito) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 08-Apr-1994 ACCESSIONS D40784 REFERENCE A40784 !$#authors Afanasiev, B.N.; Galyov, E.E.; Buchatsky, L.P.; Kozlov, Y.V. !$#journal Virology (1991) 185:323-336 !$#title Nucleotide sequence and genomic organization of Aedes !1densonucleosis virus. !$#cross-references MUID:92024090; PMID:1833875 !$#accession D40784 !'##molecule_type DNA !'##residues 1-358 ##label AFA !'##cross-references GB:M37899 CLASSIFICATION #superfamily Aedes densovirus coat protein VP1 KEYWORDS coat protein; glycoprotein FEATURE !$46,60,106,117,147, !$280 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 358 #molecular-weight 40508 #checksum 380 SEQUENCE /// ENTRY VCPVB5 #type complete TITLE coat protein VP1 - bovine parvovirus CONTAINS coat protein VP2 ORGANISM #formal_name bovine parvovirus DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 16-Jul-1999 ACCESSIONS A26104 REFERENCE A26104 !$#authors Chen, K.C.; Shull, B.C.; Moses, E.A.; Lederman, M.; Stout, !1E.R.; Bates, R.C. !$#journal J. Virol. (1986) 60:1085-1097 !$#title Complete nucleotide sequence and genome organization of !1bovine parvovirus. !$#cross-references MUID:87061184; PMID:3783814 !$#accession A26104 !'##molecule_type DNA !'##residues 1-673 ##label CHE !'##cross-references EMBL:M14363; NID:g333454; PIDN:AAB59847.1; !1PID:g808805 CLASSIFICATION #superfamily parvovirus coat protein KEYWORDS coat protein FEATURE !$138-673 #product coat protein VP2 #status predicted #label !8VP2 SUMMARY #length 673 #molecular-weight 75103 #checksum 7794 SEQUENCE /// ENTRY VCPVV2 #type complete TITLE coat protein VP1 - parvovirus H1 ORGANISM #formal_name parvovirus H1 #note host Homo sapiens (man) DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 08-Apr-1994 ACCESSIONS A03699 REFERENCE A03695 !$#authors Rhode III, S.L.; Paradiso, P.R. !$#journal J. Virol. (1983) 45:173-184 !$#title Parvovirus genome: nucleotide sequence of H-1 and mapping of !1its genes by hybrid-arrested translation. !$#cross-references MUID:83112183; PMID:6823009 !$#accession A03699 !'##molecule_type DNA !'##residues 1-722 ##label RHO !'##cross-references EMBL:X01457; EMBL:J02198 CLASSIFICATION #superfamily parvovirus coat protein KEYWORDS coat protein SUMMARY #length 722 #molecular-weight 79737 #checksum 5722 SEQUENCE /// ENTRY VCPV2M #type complete TITLE coat protein VP1 - minute virus of mice ORGANISM #formal_name minute virus of mice, murine parvovirus DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 08-Apr-1994 ACCESSIONS A03700 REFERENCE A03696 !$#authors Astell, C.R.; Thomson, M.; Merchlinsky, M.; Ward, D.C. !$#journal Nucleic Acids Res. (1983) 11:999-1018 !$#title The complete DNA sequence of minute virus of mice, an !1autonomous parvovirus. !$#cross-references MUID:83143341; PMID:6298737 !$#accession A03700 !'##molecule_type DNA !'##residues 1-716 ##label AST !'##cross-references EMBL:V01115 CLASSIFICATION #superfamily parvovirus coat protein KEYWORDS coat protein SUMMARY #length 716 #molecular-weight 78707 #checksum 4110 SEQUENCE /// ENTRY VCPVIM #type complete TITLE coat protein VP1 - minute virus of mice (strain MVMi) ORGANISM #formal_name minute virus of mice, murine parvovirus DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 28-Jul-2000 ACCESSIONS B23008; B29510 REFERENCE A23008 !$#authors Sahli, R.; McMaster, G.K.; Hirt, B. !$#journal Nucleic Acids Res. (1985) 13:3617-3633 !$#title DNA sequence comparison between two tissue-specific variants !1of the autonomous parvovirus, minute virus of mice. !$#cross-references MUID:85242059; PMID:3855242 !$#accession B23008 !'##molecule_type DNA !'##residues 1-718 ##label SAH !'##cross-references EMBL:X02481; NID:g60918; PIDN:CAB46507.1; !1PID:g5419928 REFERENCE A29510 !$#authors Astell, C.R.; Gardiner, E.M.; Tattersall, P. !$#journal J. Virol. (1986) 57:656-669 !$#title DNA sequence of the lymphotropic variant of minute virus of !1mice, MVM(i), and comparison with the DNA sequence of the !1fibrotropic prototype strain. !$#cross-references MUID:86115415; PMID:3502703 !$#accession B29510 !'##molecule_type DNA !'##residues 1-143,'A',145-718 ##label AST !'##cross-references EMBL:M12032 CLASSIFICATION #superfamily parvovirus coat protein KEYWORDS coat protein SUMMARY #length 718 #molecular-weight 79002 #checksum 921 SEQUENCE /// ENTRY VCPVPP #type complete TITLE coat protein VP1 - porcine parvovirus CONTAINS coat protein VP2 ORGANISM #formal_name porcine parvovirus DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 12-Apr-1996 ACCESSIONS B33302 REFERENCE A33302 !$#authors Ranz, A.I.; Manclus, J.J.; Diaz-Aroca, E.; Casal, J.I. !$#journal J. Gen. Virol. (1989) 70:2541-2553 !$#title Porcine parvovirus: DNA sequence and genome organization. !$#cross-references MUID:90010964; PMID:2794971 !$#accession B33302 !'##molecule_type DNA !'##residues 1-723 ##label RAN !'##cross-references EMBL:D00623 GENETICS !$#introns 10/1 CLASSIFICATION #superfamily parvovirus coat protein KEYWORDS coat protein FEATURE !$145-723 #product coat protein VP2 #status predicted #label !8VP2 SUMMARY #length 723 #molecular-weight 80214 #checksum 5058 SEQUENCE /// ENTRY VCPVNA #type complete TITLE coat protein VP1 - porcine parvovirus (strain NADL-2) CONTAINS coat protein VP2 ORGANISM #formal_name porcine parvovirus DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS B33743; D48472 REFERENCE A33743 !$#authors Vasudevacharya, J.; Basak, S.; Srinivas, R.V.; Compans, R.W. !$#journal Virology (1989) 173:368-377 !$#title Nucleotide sequence analysis of the capsid genes and the !1right-hand terminal palindrome of porcine parvovirus, strain !1NADL-2. !$#cross-references MUID:90085785; PMID:2596019 !$#accession B33743 !'##molecule_type DNA !'##residues 1-729 ##label VAS !'##cross-references GB:M32787; NID:g332983; PIDN:AAA46917.1; !1PID:g332985 REFERENCE A48472 !$#authors Bergeron, J.; Menezes, J.; Tijssen, P. !$#journal Virology (1993) 197:86-98 !$#title Genomic organization and mapping of transcription and !1translation products of the NADL-2 strain of porcine !1parvovirus. !$#cross-references MUID:94025614; PMID:8212598 !$#accession D48472 !'##molecule_type DNA !'##residues 11-729 ##label BER !'##experimental_source NADL-2, ATCC VR-742 !'##note sequence extracted from NCBI backbone (NCBIN:138789, !1NCBIP:138794) GENETICS !$#introns 10/1 CLASSIFICATION #superfamily parvovirus coat protein KEYWORDS coat protein; glycoprotein FEATURE !$151-729 #product coat protein VP2 #status predicted #label !8VP2\ !$32,172,198,282,330, !$433,471,573,604,651 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 729 #molecular-weight 80946 #checksum 6201 SEQUENCE /// ENTRY A60006 #type complete TITLE coat protein VP1 - porcine parvovirus (strain 90HS) CONTAINS coat protein VP2 ORGANISM #formal_name porcine parvovirus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 30-Sep-1993 ACCESSIONS A60006 REFERENCE A60006 !$#authors Sakurai, M.; Nishimori, T.; Ushimi, C.; Nakajima, H. !$#journal Virus Res. (1989) 13:79-86 !$#title Nucleotide sequence of capsid protein gene of porcine !1parvovirus. !$#cross-references MUID:89319168; PMID:2750278 !$#accession A60006 !'##molecule_type DNA !'##residues 1-729 ##label SAK CLASSIFICATION #superfamily parvovirus coat protein KEYWORDS coat protein; glycoprotein FEATURE !$151-729 #product coat protein VP2 #status predicted #label !8VP2\ !$172,198,282,330, !$433,471,573,604,651 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 729 #molecular-weight 80938 #checksum 7041 SEQUENCE /// ENTRY VCPV1F #type complete TITLE coat protein VP1 - feline panleukopenia virus CONTAINS coat protein VP2 ORGANISM #formal_name feline panleukopenia virus, FPLV DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 16-Jul-1999 ACCESSIONS A03701 REFERENCE A03697 !$#authors Carlson, J.; Rushlow, K.; Maxwell, I.; Maxwell, F.; Winston, !1S.; Hahn, W. !$#journal J. Virol. (1985) 55:574-587 !$#title Cloning and sequence of DNA encoding structural proteins of !1the autonomous parvovirus feline panleukopenia virus. !$#cross-references MUID:85265017; PMID:2991581 !$#accession A03701 !'##molecule_type DNA !'##residues 1-727 ##label CAR !'##cross-references EMBL:M10824; NID:g333474; PIDN:AAA47161.1; !1PID:g333476 GENETICS !$#introns 11/1 CLASSIFICATION #superfamily parvovirus coat protein KEYWORDS coat protein FEATURE !$144-727 #product coat protein VP2 #status predicted #label !8VP2 SUMMARY #length 727 #molecular-weight 80343 #checksum 7604 SEQUENCE /// ENTRY VCPVFP #type complete TITLE coat protein VP1 - feline panleukopenia virus (strain 193) CONTAINS coat protein VP2 ORGANISM #formal_name feline panleukopenia virus, FPLV DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 12-Apr-1996 ACCESSIONS B36608 REFERENCE A36608 !$#authors Martyn, J.C.; Davidson, B.E.; Studdert, M.J. !$#journal J. Gen. Virol. (1990) 71:2747-2753 !$#title Nucleotide sequence of feline panleukopenia virus: !1comparison with canine parvovirus identifies host-specific !1differences. !$#cross-references MUID:91073139; PMID:2174965 !$#accession B36608 !'##molecule_type DNA !'##residues 1-727 ##label MAR !'##cross-references GB:X55115 CLASSIFICATION #superfamily parvovirus coat protein KEYWORDS coat protein FEATURE !$144-727 #product coat protein VP2 #status predicted #label !8VP2 SUMMARY #length 727 #molecular-weight 80386 #checksum 8396 SEQUENCE /// ENTRY VCPVCN #type complete TITLE coat protein VP1 - canine parvovirus (strain 780929) CONTAINS coat protein VP2 ORGANISM #formal_name canine parvovirus, CPV DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 12-Apr-1996 ACCESSIONS A03702 REFERENCE A03702 !$#authors Rhode III, S.L. !$#journal J. Virol. (1985) 54:630-633 !$#title Nucleotide sequence of the coat protein gene of canine !1parvovirus. !$#cross-references MUID:85185696; PMID:3989914 !$#accession A03702 !'##molecule_type DNA !'##residues 1-722 ##label RHO !'##cross-references EMBL:M10989 GENETICS !$#introns 11/1 CLASSIFICATION #superfamily parvovirus coat protein KEYWORDS coat protein FEATURE !$139-722 #product coat protein VP2 #status predicted #label !8VP2 SUMMARY #length 722 #molecular-weight 79860 #checksum 9359 SEQUENCE /// ENTRY VCPVCP #type complete TITLE coat protein VP1 - canine parvovirus (strain N) CONTAINS coat protein VP2 ORGANISM #formal_name canine parvovirus, CPV DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 12-Apr-1996 ACCESSIONS B29962 REFERENCE A29962 !$#authors Reed, A.P.; Jones, E.V.; Miller, T.J. !$#journal J. Virol. (1988) 62:266-276 !$#title Nucleotide sequence and genome organization of canine !1parvovirus. !$#cross-references MUID:88062992; PMID:2824850 !$#accession B29962 !'##molecule_type DNA !'##residues 1-748 ##label REE !'##cross-references EMBL:M19296 GENETICS !$#introns 26/3 CLASSIFICATION #superfamily parvovirus coat protein KEYWORDS coat protein FEATURE !$165-748 #product coat protein VP2 #status predicted #label !8VP2 SUMMARY #length 748 #molecular-weight 82715 #checksum 1969 SEQUENCE /// ENTRY VCPVCD #type complete TITLE coat protein VP1 - canine parvovirus (strain CPV-d) CONTAINS coat protein VP2 ORGANISM #formal_name canine parvovirus, CPV DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS A31163 REFERENCE A31163 !$#authors Parrish, C.R.; Aquadro, C.F.; Carmichael, L.E. !$#journal Virology (1988) 166:293-307 !$#title Canine host range and a specific epitope map along with !1variant sequences in the capsid protein gene of canine !1parvovirus and related feline, mink, and raccoon !1parvoviruses. !$#cross-references MUID:89020796; PMID:3176341 !$#accession A31163 !'##molecule_type DNA !'##residues 1-737 ##label PAR !'##cross-references EMBL:M23255; NID:g333467; PIDN:AAA47158.1; !1PID:g333468 GENETICS !$#introns 26/3 CLASSIFICATION #superfamily parvovirus coat protein KEYWORDS coat protein FEATURE !$584-737 #product coat protein VP2 #status predicted #label !8VP2 SUMMARY #length 737 #molecular-weight 81504 #checksum 1051 SEQUENCE /// ENTRY VCPVME #type complete TITLE coat protein VP1 - mink enteritis virus (strain Abashiri) CONTAINS coat protein VP2 ORGANISM #formal_name mink enteritis virus, MEV DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 12-Apr-1996 ACCESSIONS B38350 REFERENCE A38350 !$#authors Kariatsumari, T.; Horiuchi, M.; Hama, E.; Yaguchi, K.; !1Ishigurio, N.; Goto, H.; Shinagawa, M. !$#journal J. Gen. Virol. (1991) 72:867-875 !$#title Construction and nucleotide sequence analysis of an !1infectious DNA clone of the autonomous parvovirus, mink !1enteritis virus. !$#cross-references MUID:91202123; PMID:2016597 !$#accession B38350 !'##molecule_type DNA !'##residues 1-722 ##label KAR !'##cross-references GB:D00765 CLASSIFICATION #superfamily parvovirus coat protein KEYWORDS coat protein FEATURE !$139-722 #product coat protein VP2 #status predicted #label !8VP2 SUMMARY #length 722 #molecular-weight 79800 #checksum 1018 SEQUENCE /// ENTRY B44276 #type complete TITLE coat protein VP1 - parvovirus LuIII ORGANISM #formal_name parvovirus LuIII DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 26-Feb-1999 ACCESSIONS B44276 REFERENCE A44276 !$#authors Diffoot, N.; Chen, K.C.; Bates, R.C.; Lederma, M. !$#journal Virology (1993) 192:339-345 !$#title The complete nucleotide sequence of parvovirus LuIII and !1localization of a unique sequence possibly responsible for !1its encapsidation pattern. !$#cross-references MUID:93297126; PMID:8517025 !$#accession B44276 !'##status translation not shown !'##molecule_type DNA !'##residues 1-587 ##label DIF !'##cross-references GB:M81888 CLASSIFICATION #superfamily parvovirus coat protein KEYWORDS coat protein; glycoprotein FEATURE !$49,90,220,304,371, !$503,511,514,539,571 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 587 #molecular-weight 65429 #checksum 8869 SEQUENCE /// ENTRY VCPV19 #type complete TITLE coat protein VP1 - parvovirus B19 (strain Au) ORGANISM #formal_name parvovirus B19 #note host Homo sapiens (man) DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 16-Jul-1999 ACCESSIONS A24299 REFERENCE A24299 !$#authors Shade, R.O.; Blundell, M.C.; Cotmore, S.F.; Tattersall, P.; !1Astell, C.R. !$#journal J. Virol. (1986) 58:921-936 !$#title Nucleotide sequence and genome organization of human !1parvovirus B19 isolated from the serum of a child during !1aplastic crisis. !$#cross-references MUID:86200451; PMID:3701931 !$#accession A24299 !'##molecule_type DNA !'##residues 1-781 ##label SHA !'##cross-references EMBL:M13178; NID:g333375; PIDN:AAA66867.1; !1PID:g333377 CLASSIFICATION #superfamily parvovirus coat protein KEYWORDS coat protein SUMMARY #length 781 #molecular-weight 86015 #checksum 4038 SEQUENCE /// ENTRY VCPVAP #type complete TITLE coat protein VP1 - Aleutian mink disease virus (strain ADV-G) ALTERNATE_NAMES right-ORF protein ORGANISM #formal_name Aleutian mink disease virus DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 06-Jan-1995 ACCESSIONS B36760; A35529; B35529 REFERENCE A36760 !$#authors Bloom, M.E.; Alexandersen, S.; Perryman, S.; Lechner, D.; !1Wolfinbarger, J.B. !$#journal J. Virol. (1988) 62:2903-2915 !$#title Nucleotide sequence and genomic organization of Aleutian !1mink disease parvovirus (ADV): sequence comparisons between !1a nonpathogenic and a pathogenic strain of ADV. !$#cross-references MUID:88275062; PMID:2839709 !$#accession B36760 !'##molecule_type DNA !'##residues 1-702 ##label BL2 !'##cross-references EMBL:M20036 CLASSIFICATION #superfamily parvovirus coat protein KEYWORDS coat protein SUMMARY #length 702 #molecular-weight 79962 #checksum 6576 SEQUENCE /// ENTRY SAVLAH #type complete TITLE large surface antigen - hepatitis B virus (subtype ayw) CONTAINS major surface antigen; middle surface antigen ORGANISM #formal_name hepatitis B virus, HBV DATE 18-Dec-1981 #sequence_revision 18-Dec-1981 #text_change 07-May-1999 ACCESSIONS A03703; JQ2064; PQ0591 REFERENCE A93214 !$#authors Galibert, F.; Mandart, E.; Fitoussi, F.; Tiollais, P.; !1Charnay, P. !$#journal Nature (1979) 281:646-650 !$#title Nucleotide sequence of the hepatitis B virus genome (subtype !1ayw) in E. coli. !$#cross-references MUID:81012091; PMID:399327 !$#accession A03703 !'##molecule_type DNA !'##residues 1-389 ##label GAL !'##cross-references GB:J02203 REFERENCE JQ2044 !$#authors Norder, H.; Hammas, B.; Lee, S.D.; Bile, K.; Courouce, A.M.; !1Mushahwar, I.K.; Magnius, L.O. !$#journal J. Gen. Virol. (1993) 74:1341-1348 !$#title Genetic relatedness of hepatitis B viral strains of diverse !1geographical origin and natural variations in the primary !1structure of the surface antigen. !$#cross-references MUID:93329382; PMID:8336122 !$#accession JQ2064 !'##molecule_type DNA !'##residues 164-389 ##label NOR !'##experimental_source genogroup D, subtype ayw3 REFERENCE PQ0453 !$#authors Norder, H.; Courouce, A.M.; Magnius, L.O. !$#journal J. Gen. Virol. (1992) 73:3141-3145 !$#title Molecular basis of hepatitis B virus serotype variations !1within the four major subtypes. !$#cross-references MUID:93107848; PMID:1469353 !$#accession PQ0591 !'##molecule_type DNA !'##residues 264-343 ##label NO2 !'##experimental_source subtype ayw3, Kli GENETICS !$#gene pre-S1/pre-S2/S CLASSIFICATION #superfamily hepatitis B virus surface antigen KEYWORDS glycoprotein; surface antigen FEATURE !$109-389 #product middle surface antigen (gene pre-S2/S) !8#status predicted #label DSA\ !$164-389 #product major surface antigen (gene S) #status !8predicted #label MSA\ !$4,112,166 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 389 #molecular-weight 42766 #checksum 4046 SEQUENCE /// ENTRY SAVLBH #type complete TITLE large surface antigen - hepatitis B virus (subtype ayw, strain pHB320) CONTAINS major surface antigen; middle surface antigen ORGANISM #formal_name hepatitis B virus, HBV #note host Homo sapiens (man) DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 28-Jul-2000 ACCESSIONS A03704; PQ0585 REFERENCE A05237 !$#authors Bichko, V.; Pushko, P.; Dreilina, D.; Pumpen, P.; Gren, E. !$#journal FEBS Lett. (1985) 185:208-212 !$#title Subtype ayw variant of hepatitis B virus: DNA primary !1structure analysis. !$#cross-references MUID:85204397; PMID:3996597 !$#accession A03704 !'##molecule_type DNA !'##residues 1-389 ##label BIC !'##cross-references GB:X02496; NID:g62280; PIDN:CAB41701.1; !1PID:g4704321 REFERENCE PQ0453 !$#authors Norder, H.; Courouce, A.M.; Magnius, L.O. !$#journal J. Gen. Virol. (1992) 73:3141-3145 !$#title Molecular basis of hepatitis B virus serotype variations !1within the four major subtypes. !$#cross-references MUID:93107848; PMID:1469353 !$#accession PQ0585 !'##molecule_type DNA !'##residues 264-343 ##label NOR !'##experimental_source subtype ayw2, Tav GENETICS !$#gene pre-S1/pre-S2/S CLASSIFICATION #superfamily hepatitis B virus surface antigen KEYWORDS glycoprotein; surface antigen FEATURE !$109-389 #product middle surface antigen (gene pre-S2/S) !8#status predicted #label DSA\ !$164-389 #product major surface antigen (gene S) #status !8predicted #label MSA\ !$4,112,166 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 389 #molecular-weight 42745 #checksum 4536 SEQUENCE /// ENTRY SAVLAJ #type complete TITLE large surface antigen - hepatitis B virus (subtype adyw) CONTAINS major surface antigen; middle surface antigen ORGANISM #formal_name hepatitis B virus, HBV DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 15-Nov-1996 ACCESSIONS A93217; A03703 REFERENCE A93217 !$#authors Pasek, M.; Goto, T.; Gilbert, W.; Zink, B.; Schaller, H.; !1MacKay, P.; Leadbetter, G.; Murray, K. !$#journal Nature (1979) 282:575-579 !$#title Hepatitis B virus genes and their expression in E. coli. !$#cross-references MUID:81012115; PMID:399329 !$#accession A93217 !'##molecule_type DNA !'##residues 1-389 ##label PAS !'##cross-references GB:J02202 GENETICS !$#gene pre-S1/pre-S2/S CLASSIFICATION #superfamily hepatitis B virus surface antigen KEYWORDS glycoprotein; surface antigen FEATURE !$109-389 #product middle surface antigen (gene pre-S2/S) !8#status predicted #label DSA\ !$164-389 #product major surface antigen (gene S) #status !8predicted #label MSA\ !$4,112,166 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 389 #molecular-weight 42801 #checksum 3338 SEQUENCE /// ENTRY SAVLA1 #type complete TITLE large surface antigen - hepatitis B virus (strain alpha1) CONTAINS major surface antigen; middle surface antigen ORGANISM #formal_name hepatitis B virus, HBV DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jul-1999 ACCESSIONS B34773; JQ2082 REFERENCE A34773 !$#authors Tong, S.; Li, J.; Vitvitski, L.; Trepo, C. !$#journal Virology (1990) 176:596-603 !$#title Active hepatitis B virus replication in the presence of !1anti-HBe is associated with viral variants containing an !1inactive pre-C region. !$#cross-references MUID:90266476; PMID:2345966 !$#accession B34773 !'##status translation not shown !'##molecule_type DNA !'##residues 1-389 ##label TON !'##cross-references EMBL:M32138; NID:g329667; PIDN:AAA45502.1; !1PID:g329669 REFERENCE JQ2044 !$#authors Norder, H.; Hammas, B.; Lee, S.D.; Bile, K.; Courouce, A.M.; !1Mushahwar, I.K.; Magnius, L.O. !$#journal J. Gen. Virol. (1993) 74:1341-1348 !$#title Genetic relatedness of hepatitis B viral strains of diverse !1geographical origin and natural variations in the primary !1structure of the surface antigen. !$#cross-references MUID:93329382; PMID:8336122 !$#accession JQ2082 !'##molecule_type DNA !'##residues 164-389 ##label NOR !'##experimental_source genogroup D, subtype ayw2, strain HBV-alpha GENETICS !$#gene pre-S1/pre-S2/S !$#introns 111/3 CLASSIFICATION #superfamily hepatitis B virus surface antigen KEYWORDS glycoprotein; surface antigen FEATURE !$109-389 #product middle surface antigen (gene pre-S2/S) !8#status predicted #label DSA\ !$164-389 #product major surface antigen (gene S) #status !8predicted #label MSA\ !$4,112,166 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 389 #molecular-weight 42733 #checksum 3781 SEQUENCE /// ENTRY SAVLA #type complete TITLE large surface antigen - hepatitis B virus (subtype adr) CONTAINS major surface antigen; middle surface antigen ORGANISM #formal_name hepatitis B virus, HBV DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 07-May-1999 ACCESSIONS A03705; S04569; JQ2107; PQ0608 REFERENCE A93460 !$#authors Ono, Y.; Onda, H.; Sasada, R.; Igarashi, K.; Sugino, Y.; !1Nishioka, K. !$#journal Nucleic Acids Res. (1983) 11:1747-1757 !$#title The complete nucleotide sequences of the cloned hepatitis B !1virus DNA; subtype adr and adw. !$#cross-references MUID:83168919; PMID:6300776 !$#accession A03705 !'##molecule_type DNA !'##residues 1-400 ##label ONO !'##cross-references GB:V00867 REFERENCE S04568 !$#authors Rho, H.M.; Kim, K.; Hyun, S.W.; Kim, Y.S. !$#journal Nucleic Acids Res. (1989) 17:2124 !$#title The nucleotide sequence and reading frames of a mutant !1hepatitis B virus subtype adr. !$#cross-references MUID:89183619; PMID:2928116 !$#accession S04569 !'##status translation not shown !'##molecule_type DNA !'##residues 1-50,'R',52-66,'YP',69-129,'V',131-142,'P',144-164,'S', !1166-176,'S',178-338,'G',340-400 ##label RHO !'##cross-references EMBL:X14193 REFERENCE JQ2044 !$#authors Norder, H.; Hammas, B.; Lee, S.D.; Bile, K.; Courouce, A.M.; !1Mushahwar, I.K.; Magnius, L.O. !$#journal J. Gen. Virol. (1993) 74:1341-1348 !$#title Genetic relatedness of hepatitis B viral strains of diverse !1geographical origin and natural variations in the primary !1structure of the surface antigen. !$#cross-references MUID:93329382; PMID:8336122 !$#accession JQ2107 !'##molecule_type DNA !'##residues 175-400 ##label NOR !'##experimental_source genogroup C, subtype adr, strain pBRHBadr4 REFERENCE PQ0453 !$#authors Norder, H.; Courouce, A.M.; Magnius, L.O. !$#journal J. Gen. Virol. (1992) 73:3141-3145 !$#title Molecular basis of hepatitis B virus serotype variations !1within the four major subtypes. !$#cross-references MUID:93107848; PMID:1469353 !$#accession PQ0608 !'##molecule_type DNA !'##residues 275-354 ##label NO2 !'##experimental_source subtype adrq+, Bau GENETICS !$#gene pre-S1/pre-S2/S CLASSIFICATION #superfamily hepatitis B virus surface antigen KEYWORDS glycoprotein; surface antigen FEATURE !$120-400 #product middle surface antigen (gene pre-S2/S) !8#status predicted #label DSA\ !$175-400 #product major surface antigen (gene S) #status !8predicted #label MSA\ !$15,123,177 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 400 #molecular-weight 43685 #checksum 4043 SEQUENCE /// ENTRY SAVLVD #type complete TITLE large surface antigen - hepatitis B virus (subtype adw2) CONTAINS major surface antigen; middle surface antigen ORGANISM #formal_name hepatitis B virus, HBV DATE 31-Jul-1980 #sequence_revision 14-Nov-1983 #text_change 16-Jul-1999 ACCESSIONS A03706; C93212; PQ0453; PQ0569 REFERENCE A94409 !$#authors Valenzuela, P.; Quiroga, M.; Zaldivar, J.; Gray, P.; Rutter, !1W.J. !$#book Animal Virus Genetics, Field, B.N., Jaenisch, R., and Fox, !1C.F., eds., pp.57-70, Academic Press, New York, 1980 !$#accession A03706 !'##molecule_type DNA !'##residues 1-400 ##label VAL REFERENCE A93212 !$#authors Valenzuela, P.; Gray, P.; Quiroga, M.; Zaldivar, J.; !1Goodman, H.M.; Rutter, W.J. !$#journal Nature (1979) 280:815-819 !$#title Nucleotide sequence of the gene coding for the major protein !1of hepatitis B virus surface antigen. !$#cross-references MUID:79244739; PMID:471053 !$#contents Dane particles !$#accession C93212 !'##molecule_type DNA !'##residues 175-400 ##label VA2 !'##cross-references GB:J02205; NID:g329718; PIDN:AAA45524.1; !1PID:g329719 !'##note Dane particles are 42-nm, spherical particulate structures !1found in the plasma of individuals infected with hepatitis B !1virus !'##note the Dane particle is probably the hepatitis B virion REFERENCE PQ0453 !$#authors Norder, H.; Courouce, A.M.; Magnius, L.O. !$#journal J. Gen. Virol. (1992) 73:3141-3145 !$#title Molecular basis of hepatitis B virus serotype variations !1within the four major subtypes. !$#cross-references MUID:93107848; PMID:1469353 !$#accession PQ0453 !'##molecule_type DNA !'##residues 275-354 ##label NOR1 !'##experimental_source donor code Meg !$#accession PQ0569 !'##molecule_type DNA !'##residues 275-354 ##label NOR2 !'##experimental_source donor code Wie GENETICS !$#gene pre-S1/pre-S2/S CLASSIFICATION #superfamily hepatitis B virus surface antigen KEYWORDS glycoprotein; surface antigen FEATURE !$120-400 #product middle surface antigen (gene pre-S2/S) !8#status predicted #label DSA\ !$175-400 #product major surface antigen (gene S) #status !8predicted #label MSA\ !$15,123,177 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 400 #molecular-weight 43704 #checksum 3925 SEQUENCE /// ENTRY SAVLVE #type complete TITLE large surface antigen - hepatitis B virus (subtype adw) CONTAINS major surface antigen; middle surface antigen ORGANISM #formal_name hepatitis B virus, HBV DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 07-May-1999 ACCESSIONS A93460; JQ2044; A03706 REFERENCE A93460 !$#authors Ono, Y.; Onda, H.; Sasada, R.; Igarashi, K.; Sugino, Y.; !1Nishioka, K. !$#journal Nucleic Acids Res. (1983) 11:1747-1757 !$#title The complete nucleotide sequences of the cloned hepatitis B !1virus DNA; subtype adr and adw. !$#cross-references MUID:83168919; PMID:6300776 !$#accession A93460 !'##molecule_type DNA !'##residues 1-389 ##label ONO !'##cross-references GB:V00866; GB:J02201 REFERENCE JQ2044 !$#authors Norder, H.; Hammas, B.; Lee, S.D.; Bile, K.; Courouce, A.M.; !1Mushahwar, I.K.; Magnius, L.O. !$#journal J. Gen. Virol. (1993) 74:1341-1348 !$#title Genetic relatedness of hepatitis B viral strains of diverse !1geographical origin and natural variations in the primary !1structure of the surface antigen. !$#cross-references MUID:93329382; PMID:8336122 !$#accession JQ2044 !'##molecule_type DNA !'##residues 164-389 ##label NOR !'##experimental_source genogroup A, subtype adw2, strain pHBV933 GENETICS !$#gene pre-S1/pre-S2/S CLASSIFICATION #superfamily hepatitis B virus surface antigen KEYWORDS glycoprotein; surface antigen FEATURE !$109-389 #product middle surface antigen (gene pre-S2/S) !8#status predicted #label DSA\ !$164-389 #product major surface antigen (gene S) #status !8predicted #label MSA\ !$4,26,112,166 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 389 #molecular-weight 42354 #checksum 5882 SEQUENCE /// ENTRY SAVLKS #type complete TITLE large surface antigen - hepatitis B virus (subtype adw, strain 991) CONTAINS major surface antigen; middle surface antigen ORGANISM #formal_name hepatitis B virus, HBV DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jul-1999 ACCESSIONS S10383 REFERENCE S10380 !$#authors Koechel, H.G.; Schueler, A.; Lottmann, S.; Thomssen, R. !$#submission submitted to the EMBL Data Library, February 1990 !$#accession S10383 !'##molecule_type DNA !'##residues 1-400 ##label KOE !'##cross-references EMBL:X51970; NID:g1155012; PIDN:CAA36230.1; !1PID:g908857 GENETICS !$#gene pre-S1/pre-S2/S !$#introns 123/2 CLASSIFICATION #superfamily hepatitis B virus surface antigen KEYWORDS glycoprotein; surface antigen FEATURE !$120-400 #product middle surface antigen (gene pre-2/S) !8#status predicted #label DSA\ !$175-400 #product major surface antigen (gene S) #status !8predicted #label MSA\ !$15,123,177 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 400 #molecular-weight 43695 #checksum 3044 SEQUENCE /// ENTRY SAVLHV #type complete TITLE major surface antigen - hepatitis B virus ORGANISM #formal_name hepatitis B virus, HBV #note host Homo sapiens (man) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS JT0293 REFERENCE JT0293 !$#authors Rivkina, M.B.; Lunin, V.G.; Mahov, A.M.; Tikchonenko, T.I.; !1Kukain, R.A. !$#journal Gene (1988) 64:285-296 !$#title Nucleotide sequence of integrated hepatitis B virus DNA and !1human flanking regions in the genome of the PLC/PRF/5 cell !1line. !$#cross-references MUID:88297159; PMID:2841200 !$#accession JT0293 !'##molecule_type DNA !'##residues 1-226 ##label RIV !'##cross-references GB:M21030; NID:g329702; PIDN:AAA45516.1; !1PID:g329703 GENETICS !$#gene S CLASSIFICATION #superfamily hepatitis B virus surface antigen KEYWORDS glycoprotein; surface antigen FEATURE !$3 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 226 #molecular-weight 25476 #checksum 4374 SEQUENCE /// ENTRY JQ1577 #type complete TITLE major surface antigen - hepatitis B virus (subtype ayw1) ORGANISM #formal_name hepatitis B virus, HBV #note host Homo sapiens (man) DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 28-May-1999 ACCESSIONS JQ1577; JQ2049; PQ0573 REFERENCE JQ1570 !$#authors Norder, H.; Hammas, B.; Loefdahl, S.; Courouce, A.M.; !1Magnius, L.O. !$#journal J. Gen. Virol. (1992) 73:1201-1208 !$#title Comparison of the amino acid sequences of nine different !1serotypes of hepatitis B surface antigen and genomic !1classification of the corresponding hepatitis B virus !1strains. !$#cross-references MUID:92268879; PMID:1588323 !$#accession JQ1577 !'##molecule_type DNA !'##residues 1-226 ##label NOR !'##cross-references GB:X75669; NID:g416076; PIDN:CAA53365.1; !1PID:g416077 !'##experimental_source subtype ayw1, strain CNTS-5 REFERENCE JQ2044 !$#authors Norder, H.; Hammas, B.; Lee, S.D.; Bile, K.; Courouce, A.M.; !1Mushahwar, I.K.; Magnius, L.O. !$#journal J. Gen. Virol. (1993) 74:1341-1348 !$#title Genetic relatedness of hepatitis B viral strains of diverse !1geographical origin and natural variations in the primary !1structure of the surface antigen. !$#cross-references MUID:93329382; PMID:8336122 !$#contents genogroup A !$#accession JQ2049 !'##molecule_type DNA !'##residues 1-226 ##label NO2 !'##experimental_source subtype ayw1, strain Mam REFERENCE PQ0453 !$#authors Norder, H.; Courouce, A.M.; Magnius, L.O. !$#journal J. Gen. Virol. (1992) 73:3141-3145 !$#title Molecular basis of hepatitis B virus serotype variations !1within the four major subtypes. !$#cross-references MUID:93107848; PMID:1469353 !$#accession PQ0573 !'##molecule_type DNA !'##residues 101-180 ##label NO3 !'##experimental_source subtype ayw1, strain Mam GENETICS !$#gene S CLASSIFICATION #superfamily hepatitis B virus surface antigen KEYWORDS glycoprotein; surface antigen FEATURE !$3 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 226 #molecular-weight 25431 #checksum 3337 SEQUENCE /// ENTRY JQ1578 #type complete TITLE major surface antigen - hepatitis B virus (subtype ayw4) ORGANISM #formal_name hepatitis B virus, HBV #note host Homo sapiens (man) DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 07-May-1999 ACCESSIONS JQ1578; JQ2084; PQ0594 REFERENCE JQ1570 !$#authors Norder, H.; Hammas, B.; Loefdahl, S.; Courouce, A.M.; !1Magnius, L.O. !$#journal J. Gen. Virol. (1992) 73:1201-1208 !$#title Comparison of the amino acid sequences of nine different !1serotypes of hepatitis B surface antigen and genomic !1classification of the corresponding hepatitis B virus !1strains. !$#cross-references MUID:92268879; PMID:1588323 !$#accession JQ1578 !'##molecule_type DNA !'##residues 1-226 ##label NOR !'##experimental_source subtype ayw4, CNTS-13 REFERENCE JQ2044 !$#authors Norder, H.; Hammas, B.; Lee, S.D.; Bile, K.; Courouce, A.M.; !1Mushahwar, I.K.; Magnius, L.O. !$#journal J. Gen. Virol. (1993) 74:1341-1348 !$#title Genetic relatedness of hepatitis B viral strains of diverse !1geographical origin and natural variations in the primary !1structure of the surface antigen. !$#cross-references MUID:93329382; PMID:8336122 !$#accession JQ2084 !'##molecule_type DNA !'##residues 1-226 ##label NO2 !'##experimental_source subtype ayw4, strain Kou REFERENCE PQ0453 !$#authors Norder, H.; Courouce, A.M.; Magnius, L.O. !$#journal J. Gen. Virol. (1992) 73:3141-3145 !$#title Molecular basis of hepatitis B virus serotype variations !1within the four major subtypes. !$#cross-references MUID:93107848; PMID:1469353 !$#accession PQ0594 !'##molecule_type DNA !'##residues 101-180 ##label NO3 !'##experimental_source subtype ayw4, strain Kou GENETICS !$#gene S CLASSIFICATION #superfamily hepatitis B virus surface antigen KEYWORDS surface antigen SUMMARY #length 226 #molecular-weight 25326 #checksum 791 SEQUENCE /// ENTRY JQ1579 #type complete TITLE major surface antigen - hepatitis B virus (subtype adw4q-) ORGANISM #formal_name hepatitis B virus, HBV #note host Homo sapiens (man) DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 28-May-1999 ACCESSIONS JQ1579; JQ2117 REFERENCE JQ1570 !$#authors Norder, H.; Hammas, B.; Loefdahl, S.; Courouce, A.M.; !1Magnius, L.O. !$#journal J. Gen. Virol. (1992) 73:1201-1208 !$#title Comparison of the amino acid sequences of nine different !1serotypes of hepatitis B surface antigen and genomic !1classification of the corresponding hepatitis B virus !1strains. !$#cross-references MUID:92268879; PMID:1588323 !$#accession JQ1579 !'##molecule_type DNA !'##residues 1-226 ##label NOR !'##cross-references GB:X75661; NID:g416088; PIDN:CAA53348.1; !1PID:g416089 !'##experimental_source subtype adw4q-, strain CNTS-36 REFERENCE JQ2044 !$#authors Norder, H.; Hammas, B.; Lee, S.D.; Bile, K.; Courouce, A.M.; !1Mushahwar, I.K.; Magnius, L.O. !$#journal J. Gen. Virol. (1993) 74:1341-1348 !$#title Genetic relatedness of hepatitis B viral strains of diverse !1geographical origin and natural variations in the primary !1structure of the surface antigen. !$#cross-references MUID:93329382; PMID:8336122 !$#contents genogroup F !$#accession JQ2117 !'##molecule_type DNA !'##residues 1-226 ##label NO2 !'##experimental_source subtype adw4q-, strain Car GENETICS !$#gene S CLASSIFICATION #superfamily hepatitis B virus surface antigen KEYWORDS glycoprotein; surface antigen FEATURE !$3 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 226 #molecular-weight 25081 #checksum 1465 SEQUENCE /// ENTRY JQ1580 #type complete TITLE major surface antigen - hepatitis B virus (subtype adw4q-, strains CNTS-38 and Fou) ORGANISM #formal_name hepatitis B virus, HBV #note host Homo sapiens (man) DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 07-May-1999 ACCESSIONS JQ1580; JQ2118; PQ0599 REFERENCE JQ1570 !$#authors Norder, H.; Hammas, B.; Loefdahl, S.; Courouce, A.M.; !1Magnius, L.O. !$#journal J. Gen. Virol. (1992) 73:1201-1208 !$#title Comparison of the amino acid sequences of nine different !1serotypes of hepatitis B surface antigen and genomic !1classification of the corresponding hepatitis B virus !1strains. !$#cross-references MUID:92268879; PMID:1588323 !$#accession JQ1580 !'##molecule_type DNA !'##residues 1-226 ##label NOR !'##experimental_source subtype adw4q-, strain CNTS-38 REFERENCE JQ2044 !$#authors Norder, H.; Hammas, B.; Lee, S.D.; Bile, K.; Courouce, A.M.; !1Mushahwar, I.K.; Magnius, L.O. !$#journal J. Gen. Virol. (1993) 74:1341-1348 !$#title Genetic relatedness of hepatitis B viral strains of diverse !1geographical origin and natural variations in the primary !1structure of the surface antigen. !$#cross-references MUID:93329382; PMID:8336122 !$#contents genogroup F !$#accession JQ2118 !'##molecule_type DNA !'##residues 1-226 ##label NO2 !'##experimental_source subtype adw4q-, strain Rou REFERENCE PQ0453 !$#authors Norder, H.; Courouce, A.M.; Magnius, L.O. !$#journal J. Gen. Virol. (1992) 73:3141-3145 !$#title Molecular basis of hepatitis B virus serotype variations !1within the four major subtypes. !$#cross-references MUID:93107848; PMID:1469353 !$#accession PQ0599 !'##molecule_type DNA !'##residues 101-180 ##label NO3 !'##experimental_source subtype adw4q-, strain Rou GENETICS !$#gene S CLASSIFICATION #superfamily hepatitis B virus surface antigen KEYWORDS glycoprotein; surface antigen FEATURE !$3 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 226 #molecular-weight 25213 #checksum 2503 SEQUENCE /// ENTRY JQ1581 #type complete TITLE major surface antigen - hepatitis B virus (subtype adrq-) ORGANISM #formal_name hepatitis B virus, HBV #note host Homo sapiens (man) DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 07-May-1999 ACCESSIONS JQ1581; JQ2093 REFERENCE JQ1570 !$#authors Norder, H.; Hammas, B.; Loefdahl, S.; Courouce, A.M.; !1Magnius, L.O. !$#journal J. Gen. Virol. (1992) 73:1201-1208 !$#title Comparison of the amino acid sequences of nine different !1serotypes of hepatitis B surface antigen and genomic !1classification of the corresponding hepatitis B virus !1strains. !$#cross-references MUID:92268879; PMID:1588323 !$#accession JQ1581 !'##molecule_type DNA !'##residues 1-226 ##label NOR !'##experimental_source subtype adrq-, strain CNTS-HMA REFERENCE JQ2044 !$#authors Norder, H.; Hammas, B.; Lee, S.D.; Bile, K.; Courouce, A.M.; !1Mushahwar, I.K.; Magnius, L.O. !$#journal J. Gen. Virol. (1993) 74:1341-1348 !$#title Genetic relatedness of hepatitis B viral strains of diverse !1geographical origin and natural variations in the primary !1structure of the surface antigen. !$#cross-references MUID:93329382; PMID:8336122 !$#contents genogroup C !$#accession JQ2093 !'##molecule_type DNA !'##residues 1-226 ##label NO2 !'##experimental_source subtype adrq-, strain HMA GENETICS !$#gene S CLASSIFICATION #superfamily hepatitis B virus surface antigen KEYWORDS glycoprotein; surface antigen FEATURE !$3 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 226 #molecular-weight 25388 #checksum 3836 SEQUENCE /// ENTRY SAVLN1 #type complete TITLE major surface antigen - hepatitis B virus (subtype adr, strain NC-1) ORGANISM #formal_name hepatitis B virus, HBV #note host Homo sapiens (man) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 08-Apr-1994 ACCESSIONS JC1002 REFERENCE JC1002 !$#authors Qi, Z.H.; Yan, J.; Xiong, W.J.; Cai, L.W. !$#journal Chinese Biochem. J. (1988) 4:201-209 !$#title Determination of the nucleotide sequence and studies on the !1structure of hepatitis B virus (HBV) adr NC-1 surface !1antigen (HBsAg) gene. !$#accession JC1002 !'##molecule_type DNA !'##residues 1-226 ##label QIZ GENETICS !$#gene S CLASSIFICATION #superfamily hepatitis B virus surface antigen KEYWORDS surface antigen SUMMARY #length 226 #molecular-weight 25397 #checksum 2726 SEQUENCE /// ENTRY SAVLAD #type complete TITLE major surface antigen - hepatitis B virus (subtype ad) ORGANISM #formal_name hepatitis B virus, HBV #note host Homo sapiens (man) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS PL0053 REFERENCE PL0053 !$#authors Okamoto, H.; Omi, S.; Wang, Y.; Itoh, Y.; Tsuda, F.; Tanaka, !1T.; Akahane, Y.; Miyakawa, Y.; Mayumi, M. !$#journal Mol. Immunol. (1989) 26:197-205 !$#title The loss of subtypic determinants in alleles, d/y or w/r, on !1hepatitis B surface antigen. !$#cross-references MUID:89143494; PMID:2465492 !$#accession PL0053 !'##molecule_type DNA !'##residues 1-226 ##label OKA !'##cross-references GB:M27765; NID:g329706; PIDN:AAA45518.1; !1PID:g329707 GENETICS !$#gene S CLASSIFICATION #superfamily hepatitis B virus surface antigen KEYWORDS glycoprotein; surface antigen FEATURE !$3 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 226 #molecular-weight 25348 #checksum 2848 SEQUENCE /// ENTRY SAVLAR #type complete TITLE major surface antigen - hepatitis B virus (subtype ar) ORGANISM #formal_name hepatitis B virus, HBV #note host Homo sapiens (man) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS PL0056 REFERENCE PL0053 !$#authors Okamoto, H.; Omi, S.; Wang, Y.; Itoh, Y.; Tsuda, F.; Tanaka, !1T.; Akahane, Y.; Miyakawa, Y.; Mayumi, M. !$#journal Mol. Immunol. (1989) 26:197-205 !$#title The loss of subtypic determinants in alleles, d/y or w/r, on !1hepatitis B surface antigen. !$#cross-references MUID:89143494; PMID:2465492 !$#accession PL0056 !'##molecule_type DNA !'##residues 1-226 ##label OKA !'##cross-references GB:M27766; NID:g329708; PIDN:AAA45519.1; !1PID:g329709 GENETICS !$#gene S CLASSIFICATION #superfamily hepatitis B virus surface antigen KEYWORDS surface antigen SUMMARY #length 226 #molecular-weight 25377 #checksum 2766 SEQUENCE /// ENTRY JQ1570 #type complete TITLE major surface antigen - hepatitis B virus (subtype ayw1, strain P1) ORGANISM #formal_name hepatitis B virus, HBV #note host Homo sapiens (man) DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 28-May-1999 ACCESSIONS JQ1570 REFERENCE JQ1570 !$#authors Norder, H.; Hammas, B.; Loefdahl, S.; Courouce, A.M.; !1Magnius, L.O. !$#journal J. Gen. Virol. (1992) 73:1201-1208 !$#title Comparison of the amino acid sequences of nine different !1serotypes of hepatitis B surface antigen and genomic !1classification of the corresponding hepatitis B virus !1strains. !$#cross-references MUID:92268879; PMID:1588323 !$#accession JQ1570 !'##molecule_type DNA !'##residues 1-226 ##label NOR !'##cross-references GB:X75660; NID:g416078; PIDN:CAA53347.1; !1PID:g416079 GENETICS !$#gene S CLASSIFICATION #superfamily hepatitis B virus surface antigen KEYWORDS surface antigen SUMMARY #length 226 #molecular-weight 25374 #checksum 3461 SEQUENCE /// ENTRY JQ1571 #type complete TITLE major surface antigen - hepatitis B virus (subtype ayw2) ORGANISM #formal_name hepatitis B virus, HBV #note host Homo sapiens (man) DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 28-May-1999 ACCESSIONS JQ1571; JQ2074 REFERENCE JQ1570 !$#authors Norder, H.; Hammas, B.; Loefdahl, S.; Courouce, A.M.; !1Magnius, L.O. !$#journal J. Gen. Virol. (1992) 73:1201-1208 !$#title Comparison of the amino acid sequences of nine different !1serotypes of hepatitis B surface antigen and genomic !1classification of the corresponding hepatitis B virus !1strains. !$#cross-references MUID:92268879; PMID:1588323 !$#accession JQ1571 !'##molecule_type DNA !'##residues 1-226 ##label NOR !'##cross-references GB:X75662; NID:g416086; PIDN:CAA53349.1; !1PID:g416087 !'##experimental_source subtype ayw2, strain P2 REFERENCE JQ2044 !$#authors Norder, H.; Hammas, B.; Lee, S.D.; Bile, K.; Courouce, A.M.; !1Mushahwar, I.K.; Magnius, L.O. !$#journal J. Gen. Virol. (1993) 74:1341-1348 !$#title Genetic relatedness of hepatitis B viral strains of diverse !1geographical origin and natural variations in the primary !1structure of the surface antigen. !$#cross-references MUID:93329382; PMID:8336122 !$#contents genogroup D !$#accession JQ2074 !'##molecule_type DNA !'##residues 1-226 ##label NO2 !'##experimental_source subtype ayw2, strain Ren GENETICS !$#gene S CLASSIFICATION #superfamily hepatitis B virus surface antigen KEYWORDS glycoprotein; surface antigen FEATURE !$3 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 226 #molecular-weight 25460 #checksum 3809 SEQUENCE /// ENTRY JQ1572 #type complete TITLE major surface antigen - hepatitis B virus (subtype ayw3, strain P3) ORGANISM #formal_name hepatitis B virus, HBV #note host Homo sapiens (man) DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 07-May-1999 ACCESSIONS JQ1572 REFERENCE JQ1570 !$#authors Norder, H.; Hammas, B.; Loefdahl, S.; Courouce, A.M.; !1Magnius, L.O. !$#journal J. Gen. Virol. (1992) 73:1201-1208 !$#title Comparison of the amino acid sequences of nine different !1serotypes of hepatitis B surface antigen and genomic !1classification of the corresponding hepatitis B virus !1strains. !$#cross-references MUID:92268879; PMID:1588323 !$#accession JQ1572 !'##molecule_type DNA !'##residues 1-226 ##label NOR GENETICS !$#gene S CLASSIFICATION #superfamily hepatitis B virus surface antigen KEYWORDS glycoprotein; surface antigen FEATURE !$3 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 226 #molecular-weight 25494 #checksum 3784 SEQUENCE /// ENTRY JQ1573 #type complete TITLE major surface antigen - hepatitis B virus (subtype ayw4, strains P4 and Bas) ORGANISM #formal_name hepatitis B virus, HBV #note host Homo sapiens (man) DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 07-May-1999 ACCESSIONS JQ1573; JQ2086 REFERENCE JQ1570 !$#authors Norder, H.; Hammas, B.; Loefdahl, S.; Courouce, A.M.; !1Magnius, L.O. !$#journal J. Gen. Virol. (1992) 73:1201-1208 !$#title Comparison of the amino acid sequences of nine different !1serotypes of hepatitis B surface antigen and genomic !1classification of the corresponding hepatitis B virus !1strains. !$#cross-references MUID:92268879; PMID:1588323 !$#accession JQ1573 !'##molecule_type DNA !'##residues 1-226 ##label NOR !'##experimental_source subtype ayw4, strain P4 REFERENCE JQ2044 !$#authors Norder, H.; Hammas, B.; Lee, S.D.; Bile, K.; Courouce, A.M.; !1Mushahwar, I.K.; Magnius, L.O. !$#journal J. Gen. Virol. (1993) 74:1341-1348 !$#title Genetic relatedness of hepatitis B viral strains of diverse !1geographical origin and natural variations in the primary !1structure of the surface antigen. !$#cross-references MUID:93329382; PMID:8336122 !$#accession JQ2086 !'##molecule_type DNA !'##residues 1-226 ##label NO2 !'##experimental_source subtype ayw4, strain Bas GENETICS !$#gene S CLASSIFICATION #superfamily hepatitis B virus surface antigen KEYWORDS surface antigen SUMMARY #length 226 #molecular-weight 25268 #checksum 1238 SEQUENCE /// ENTRY JQ1574 #type complete TITLE major surface antigen - hepatitis B virus (subtype ayr, strain P5) ORGANISM #formal_name hepatitis B virus, HBV #note host Homo sapiens (man) DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 28-May-1999 ACCESSIONS JQ1574 REFERENCE JQ1570 !$#authors Norder, H.; Hammas, B.; Loefdahl, S.; Courouce, A.M.; !1Magnius, L.O. !$#journal J. Gen. Virol. (1992) 73:1201-1208 !$#title Comparison of the amino acid sequences of nine different !1serotypes of hepatitis B surface antigen and genomic !1classification of the corresponding hepatitis B virus !1strains. !$#cross-references MUID:92268879; PMID:1588323 !$#accession JQ1574 !'##molecule_type DNA !'##residues 1-226 ##label NOR !'##cross-references GB:X75667; NID:g416080; PIDN:CAA53363.1; !1PID:g416081 GENETICS !$#gene S CLASSIFICATION #superfamily hepatitis B virus surface antigen KEYWORDS glycoprotein; surface antigen FEATURE !$3 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 226 #molecular-weight 25518 #checksum 1297 SEQUENCE /// ENTRY JQ1575 #type complete TITLE major surface antigen - hepatitis B virus ALTERNATE_NAMES envelope protein; HBs antigen CONTAINS surface antigen pre-S1 (large envelope protein); surface antigen pre-S2 (middle envelope protein); surface antigen S (small envelope protein) ORGANISM #formal_name hepatitis B virus, HBV #variety subtype adw2 DATE 31-Dec-1993 #sequence_revision 22-Oct-1999 #text_change 22-Oct-1999 ACCESSIONS S47411; JQ1575 REFERENCE S47404 !$#authors Plucienniczak, A. !$#submission submitted to the EMBL Data Library, August 1994 !$#description Molecular cloning and sequencing of two complete genomes of !1polish isolates of human hepatitis B virus. !$#accession S47411 !'##molecule_type DNA !'##residues 1-400 ##label PLU !'##cross-references EMBL:Z35717; NID:g527440; PIDN:CAA84792.1; !1PID:g527444 !'##experimental_source subtype adw2 REFERENCE JQ1570 !$#authors Norder, H.; Hammas, B.; Loefdahl, S.; Courouce, A.M.; !1Magnius, L.O. !$#journal J. Gen. Virol. (1992) 73:1201-1208 !$#title Comparison of the amino acid sequences of nine different !1serotypes of hepatitis B surface antigen and genomic !1classification of the corresponding hepatitis B virus !1strains. !$#cross-references MUID:92268879; PMID:1588323 !$#accession JQ1575 !'##molecule_type DNA !'##residues 175-400 ##label NOR !'##cross-references GB:X75666; NID:g416074; PIDN:CAA53362.1; !1PID:g416075 !'##experimental_source subtype adw2, strain P6 GENETICS !$#gene S !$#introns 122/3 CLASSIFICATION #superfamily hepatitis B virus surface antigen KEYWORDS glycoprotein; surface antigen FEATURE !$1-400 #product surface antigen pre-S1 (large envelope !8protein) #status predicted #label PS1\ !$1-119 #domain pre-S1 domain #status predicted #label PRE1\ !$120-400 #product surface antigen pre-S2 (middle envelope !8protein) #status predicted #label PS2\ !$120-174 #domain pre-S2 domain #status predicted #label PRE2\ !$175-400 #product surface antigen S (small envelope protein) !8#status predicted #label PSD\ !$177 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 400 #molecular-weight 43693 #checksum 3027 SEQUENCE /// ENTRY JQ1576 #type complete TITLE major surface antigen - hepatitis B virus (subtype adr, strain P8) ORGANISM #formal_name hepatitis B virus, HBV #note host Homo sapiens (man) DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 28-May-1999 ACCESSIONS JQ1576; PQ0605 REFERENCE JQ1570 !$#authors Norder, H.; Hammas, B.; Loefdahl, S.; Courouce, A.M.; !1Magnius, L.O. !$#journal J. Gen. Virol. (1992) 73:1201-1208 !$#title Comparison of the amino acid sequences of nine different !1serotypes of hepatitis B surface antigen and genomic !1classification of the corresponding hepatitis B virus !1strains. !$#cross-references MUID:92268879; PMID:1588323 !$#accession JQ1576 !'##molecule_type DNA !'##residues 1-226 ##label NOR !'##cross-references GB:X75792; NID:g416082; PIDN:CAA53435.1; !1PID:g416083 REFERENCE PQ0453 !$#authors Norder, H.; Courouce, A.M.; Magnius, L.O. !$#journal J. Gen. Virol. (1992) 73:3141-3145 !$#title Molecular basis of hepatitis B virus serotype variations !1within the four major subtypes. !$#cross-references MUID:93107848; PMID:1469353 !$#accession PQ0605 !'##molecule_type DNA !'##residues 101-180 ##label NO2 !'##experimental_source subtype adrq+, Oll GENETICS !$#gene S CLASSIFICATION #superfamily hepatitis B virus surface antigen KEYWORDS glycoprotein; surface antigen FEATURE !$3 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 226 #molecular-weight 25435 #checksum 2041 SEQUENCE /// ENTRY SAVLJ1 #type complete TITLE large surface antigen - hepatitis B virus (subtype adw, strain Japan/pJDW233) CONTAINS major surface antigen; middle surface antigen ORGANISM #formal_name hepatitis B virus, HBV DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 14-Nov-1997 ACCESSIONS G28925 REFERENCE JS0253 !$#authors Okamoto, H.; Tsuda, F.; Sakugawa, H.; Sastrosoewignjo, R.I.; !1Imai, M.; Miyakawa, Y.; Mayumi, M. !$#journal J. Gen. Virol. (1988) 69:2575-2583 !$#title Typing hepatitis B virus by homology in nucleotide sequence: !1comparison of surface antigen subtypes. !$#cross-references MUID:89010694; PMID:3171552 !$#accession G28925 !'##molecule_type DNA !'##residues 1-389 ##label OKA !'##cross-references GB:D00329; NID:g221497 GENETICS !$#gene pre-S1/pre-S2/S CLASSIFICATION #superfamily hepatitis B virus surface antigen KEYWORDS glycoprotein; surface antigen FEATURE !$109-389 #product middle surface antigen (gene pre-S2/S) !8#status predicted #label DSA\ !$175-389 #product major surface antigen (gene S) #status !8predicted #label MSA\ !$4,112 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 389 #molecular-weight 42603 #checksum 3679 SEQUENCE /// ENTRY SAVLJ2 #type complete TITLE large surface antigen - hepatitis B virus (subtype adw, strain Okinawa/pODW282) CONTAINS major surface antigen; middle surface antigen ORGANISM #formal_name hepatitis B virus, HBV DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 14-Nov-1997 ACCESSIONS H28925 REFERENCE JS0253 !$#authors Okamoto, H.; Tsuda, F.; Sakugawa, H.; Sastrosoewignjo, R.I.; !1Imai, M.; Miyakawa, Y.; Mayumi, M. !$#journal J. Gen. Virol. (1988) 69:2575-2583 !$#title Typing hepatitis B virus by homology in nucleotide sequence: !1comparison of surface antigen subtypes. !$#cross-references MUID:89010694; PMID:3171552 !$#accession H28925 !'##molecule_type DNA !'##residues 1-389 ##label OKA !'##cross-references GB:D00330; NID:g221498 GENETICS !$#gene pre-S1/pre-S2/S CLASSIFICATION #superfamily hepatitis B virus surface antigen KEYWORDS glycoprotein; surface antigen FEATURE !$109-389 #product middle surface antigen (gene pre-S2/S) !8#status predicted #label DSA\ !$164-389 #product major surface antigen (gene S) #status !8predicted #label MSA\ !$4,112 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 389 #molecular-weight 42408 #checksum 3800 SEQUENCE /// ENTRY SAVLJ3 #type complete TITLE large surface antigen - hepatitis B virus (subtype adw, strain Indonesia/pIDW420) CONTAINS major surface antigen; middle surface antigen ORGANISM #formal_name hepatitis B virus, HBV DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 07-May-1999 ACCESSIONS I28925; PQ0570 REFERENCE JS0253 !$#authors Okamoto, H.; Tsuda, F.; Sakugawa, H.; Sastrosoewignjo, R.I.; !1Imai, M.; Miyakawa, Y.; Mayumi, M. !$#journal J. Gen. Virol. (1988) 69:2575-2583 !$#title Typing hepatitis B virus by homology in nucleotide sequence: !1comparison of surface antigen subtypes. !$#cross-references MUID:89010694; PMID:3171552 !$#accession I28925 !'##molecule_type DNA !'##residues 1-389 ##label OKA !'##cross-references GB:D00331; NID:g221499 !'##experimental_source subtype adw, strain Indonesia/pIDW420 REFERENCE PQ0453 !$#authors Norder, H.; Courouce, A.M.; Magnius, L.O. !$#journal J. Gen. Virol. (1992) 73:3141-3145 !$#title Molecular basis of hepatitis B virus serotype variations !1within the four major subtypes. !$#cross-references MUID:93107848; PMID:1469353 !$#accession PQ0570 !'##molecule_type DNA !'##residues 264-343 ##label NOR !'##experimental_source subtype adw2, Sru GENETICS !$#gene pre-S1/pre-S2/S CLASSIFICATION #superfamily hepatitis B virus surface antigen KEYWORDS glycoprotein; surface antigen FEATURE !$109-389 #product middle surface antigen (gene pre-S2/S) !8#status predicted #label DSA\ !$164-389 #product major surface antigen (gene S) #status !8predicted #label MSA\ !$4,112 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 389 #molecular-weight 42653 #checksum 5149 SEQUENCE /// ENTRY SAVLCP #type complete TITLE large surface antigen - hepatitis B virus CONTAINS major surface antigen; middle surface antigen ORGANISM #formal_name hepatitis B virus, HBV DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jun-2000 ACCESSIONS C28885; JQ2123 REFERENCE A92796 !$#authors Vaudin, M.; Wolstenholme, A.J.; Tsiquaye, K.N.; Zuckerman, !1A.J.; Harrison, T.J. !$#journal J. Gen. Virol. (1988) 69:1383-1389 !$#title The complete nucleotide sequence of the genome of a !1hepatitis B virus isolated from a naturally infected !1chimpanzee. !$#cross-references MUID:88258473; PMID:2838576 !$#accession C28885 !'##molecule_type DNA !'##residues 1-389 ##label VAU !'##cross-references GB:D00220; NID:g221505; PIDN:BAA00159.1; !1PID:g221508 !'##experimental_source strain LSH, chimpanzee !'##note the authors translated the codon GAG for residue 327 as Gln REFERENCE JQ2044 !$#authors Norder, H.; Hammas, B.; Lee, S.D.; Bile, K.; Courouce, A.M.; !1Mushahwar, I.K.; Magnius, L.O. !$#journal J. Gen. Virol. (1993) 74:1341-1348 !$#title Genetic relatedness of hepatitis B viral strains of diverse !1geographical origin and natural variations in the primary !1structure of the surface antigen. !$#cross-references MUID:93329382; PMID:8336122 !$#accession JQ2123 !'##molecule_type DNA !'##residues 164-389 ##label NOR !'##experimental_source subtype adw2, strain adwLSH GENETICS !$#gene pre-S1/pre-S2/S; S CLASSIFICATION #superfamily hepatitis B virus surface antigen KEYWORDS glycoprotein; surface antigen FEATURE !$109-389 #product middle surface antigen (gene pre-S2/S) !8#status predicted #label DSA\ !$164-389 #product major surface antigen (gene S) #status !8predicted #label MSA\ !$4,112,166 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 389 #molecular-weight 42539 #checksum 1921 SEQUENCE /// ENTRY SAVLC #type complete TITLE large surface antigen - woodchuck hepatitis virus (clone 1) CONTAINS major surface antigen; middle surface antigen ORGANISM #formal_name woodchuck hepatitis virus DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 16-Jul-1999 ACCESSIONS A03707 REFERENCE A92986 !$#authors Galibert, F.; Chen, T.N.; Mandart, E. !$#journal J. Virol. (1982) 41:51-65 !$#title Nucleotide sequence of a cloned woodchuck hepatitis virus !1genome: comparison with the hepatitis B virus sequence. !$#cross-references MUID:82216969; PMID:7086958 !$#accession A03707 !'##molecule_type DNA !'##residues 1-426 ##label GAL !'##cross-references GB:J02442; NID:g336126; PIDN:AAA46760.1; !1PID:g336128 GENETICS !$#gene pre-S1/pre-S2/S CLASSIFICATION #superfamily hepatitis B virus surface antigen KEYWORDS glycoprotein; surface antigen FEATURE !$145-426 #product middle surface antigen (gene pre-S2/S) !8#status predicted #label DSA\ !$205-426 #product major surface antigen (gene S) #status !8predicted #label MSA\ !$32,147,346 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 426 #molecular-weight 48403 #checksum 8435 SEQUENCE /// ENTRY SAVLC2 #type complete TITLE large surface antigen - woodchuck hepatitis virus (clone 2) CONTAINS major surface antigen; middle surface antigen ORGANISM #formal_name woodchuck hepatitis virus #note variety subtype 2 DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 16-Jul-1999 ACCESSIONS A03708 REFERENCE A93015 !$#authors Kodama, K.; Ogasawara, N.; Yoshikawa, H.; Murakami, S. !$#journal J. Virol. (1985) 56:978-986 !$#title Nucleotide sequence of a cloned woodchuck hepatitis virus !1genome: evolutional relationship between hepadnaviruses. !$#cross-references MUID:86062931; PMID:3855246 !$#accession A03708 !'##molecule_type DNA !'##residues 1-431 ##label KOD !'##cross-references GB:M11082; NID:g336132; PIDN:AAA19182.1; !1PID:g336133 GENETICS !$#gene pre-S1/pre-S2/S CLASSIFICATION #superfamily hepatitis B virus surface antigen KEYWORDS glycoprotein; surface antigen FEATURE !$150-431 #product middle surface antigen (gene pre-S2/S) !8#status predicted #label DSA\ !$210-431 #product major surface antigen (gene S) #status !8predicted #label MSA\ !$32,94,152 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 431 #molecular-weight 48954 #checksum 9460 SEQUENCE /// ENTRY SAVL7 #type complete TITLE large surface antigen - woodchuck hepatitis virus (clone 7) CONTAINS major surface antigen; middle surface antigen ORGANISM #formal_name woodchuck hepatitis virus DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jul-1999 ACCESSIONS D29969 REFERENCE A94368 !$#authors Cohen, J.I.; Miller, R.H.; Rosenblum, B.; Denniston, K.; !1Gerin, J.L.; Purcell, R.H. !$#journal Virology (1988) 162:12-20 !$#title Sequence comparison of woodchuck hepatitis virus replicative !1forms shows conservation of the genome. !$#cross-references MUID:88101359; PMID:3336938 !$#accession D29969 !'##molecule_type DNA !'##residues 1-431 ##label COH !'##cross-references GB:M18752; NID:g336136; PIDN:AAA46766.1; !1PID:g336137 GENETICS !$#gene pre-S1/pre-S2/S CLASSIFICATION #superfamily hepatitis B virus surface antigen KEYWORDS glycoprotein; surface antigen FEATURE !$150-431 #product middle surface antigen (gene pre-S2/S) !8#status predicted #label DSA\ !$210-431 #product major surface antigen (gene S) #status !8predicted #label MSA\ !$32,94,152 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 431 #molecular-weight 48948 #checksum 9551 SEQUENCE /// ENTRY SAVLW8 #type complete TITLE large surface antigen - woodchuck hepatitis virus (clone 8) CONTAINS major surface antigen; middle surface antigen ORGANISM #formal_name woodchuck hepatitis virus DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 12-Jun-1998 ACCESSIONS B32397 REFERENCE A94222 !$#authors Girones, R.; Cote, P.J.; Hornbuckle, W.E.; Tennant, B.C.; !1Gerin, J.L.; Purcell, R.H.; Miller, R.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:1846-1849 !$#title Complete nucleotide sequence of a molecular clone of !1woodchuck hepatitis virus that is infectious in the natural !1host. !$#cross-references MUID:89184524; PMID:2928306 !$#accession B32397 !'##molecule_type DNA !'##residues 1-431 ##label GIR !'##cross-references GB:J04514 GENETICS !$#gene pre-S1/pre-S2/S CLASSIFICATION #superfamily hepatitis B virus surface antigen KEYWORDS glycoprotein; surface antigen FEATURE !$150-431 #product middle surface antigen (gene pre-S2/S) !8#status predicted #label DSA\ !$210-431 #product major surface antigen (gene S) #status !8predicted #label MSA\ !$32,94,152 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 431 #molecular-weight 49006 #checksum 9335 SEQUENCE /// ENTRY SAVL59 #type complete TITLE large surface antigen - woodchuck hepatitis virus (clone 59) CONTAINS major surface antigen; middle surface antigen ORGANISM #formal_name woodchuck hepatitis virus DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jul-1999 ACCESSIONS H29969 REFERENCE A94368 !$#authors Cohen, J.I.; Miller, R.H.; Rosenblum, B.; Denniston, K.; !1Gerin, J.L.; Purcell, R.H. !$#journal Virology (1988) 162:12-20 !$#title Sequence comparison of woodchuck hepatitis virus replicative !1forms shows conservation of the genome. !$#cross-references MUID:88101359; PMID:3336938 !$#accession H29969 !'##molecule_type DNA !'##residues 1-431 ##label COH !'##cross-references GB:M19183; NID:g336141; PIDN:AAA46762.1; !1PID:g336142 GENETICS !$#gene pre-S1/pre-S2/S CLASSIFICATION #superfamily hepatitis B virus surface antigen KEYWORDS glycoprotein; surface antigen FEATURE !$150-431 #product middle surface antigen (gene pre-S2/S) !8#status predicted #label DSA\ !$210-431 #product major surface antigen (gene S) #status !8predicted #label MSA\ !$32,94,152 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 431 #molecular-weight 49018 #checksum 1103 SEQUENCE /// ENTRY SAVL64 #type complete TITLE middle surface antigen precursor - woodchuck hepatitis virus (clone 64) CONTAINS major surface antigen ORGANISM #formal_name woodchuck hepatitis virus DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 16-Jul-1999 ACCESSIONS B29498 REFERENCE A91568 !$#authors Etiemble, J.; Moeroey, T.; Trepo, C.; Tiollais, P.; Buendia, !1M.A. !$#journal Gene (1986) 50:207-214 !$#title Nucleotide sequence of the woodchuck hepatitis virus surface !1antigen mRNAs and the variability of three overlapping viral !1genes. !$#cross-references MUID:87219879; PMID:3582979 !$#accession B29498 !'##molecule_type mRNA !'##residues 1-282 ##label ETI !'##cross-references GB:M15954; NID:g893289; PIDN:AAA69574.1; !1PID:g336156 GENETICS !$#gene pre-S2/S CLASSIFICATION #superfamily hepatitis B virus surface antigen KEYWORDS glycoprotein; surface antigen FEATURE !$1-60 #domain signal sequence #status predicted #label SIG\ !$61-282 #product major surface antigen (gene S) #status !8predicted #label MSA\ !$3 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 282 #molecular-weight 32052 #checksum 8514 SEQUENCE /// ENTRY SAVLS #type complete TITLE large surface antigen - ground squirrel hepatitis virus CONTAINS major surface antigen; middle surface antigen ORGANISM #formal_name ground squirrel hepatitis virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 15-Nov-1996 ACCESSIONS A03709 REFERENCE A93000 !$#authors Seeger, C.; Ganem, D.; Varmus, H.E. !$#journal J. Virol. (1984) 51:367-375 !$#title Nucleotide sequence of an infectious molecularly cloned !1genome of ground squirrel hepatitis virus. !$#cross-references MUID:84267998; PMID:6086950 !$#accession A03709 !'##molecule_type DNA !'##residues 1-428 ##label SEE !'##cross-references GB:K02715 GENETICS !$#gene pre-S1/pre-S2/S CLASSIFICATION #superfamily hepatitis B virus surface antigen KEYWORDS glycoprotein; surface antigen FEATURE !$147-428 #product middle surface antigen (gene pre-S2/S) !8#status predicted #label DSA\ !$207-428 #product major surface antigen (gene S) #status !8predicted #label MSA\ !$149 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 428 #molecular-weight 48382 #checksum 144 SEQUENCE /// ENTRY SAVLD #type complete TITLE large surface antigen - duck hepatitis virus CONTAINS major surface antigen; middle surface antigen ORGANISM #formal_name duck hepatitis virus, DHBV DATE 20-Sep-1984 #sequence_revision 20-Sep-1984 #text_change 13-Mar-1997 ACCESSIONS A03710; S12845 REFERENCE A92997 !$#authors Mandart, E.; Kay, A.; Galibert, F. !$#journal J. Virol. (1984) 49:782-792 !$#title Nucleotide sequence of a cloned duck hepatitis B virus !1genome: comparison with woodchuck and human hepatitis B !1virus sequences. !$#cross-references MUID:84138772; PMID:6699938 !$#accession A03710 !'##molecule_type DNA !'##residues 1-364 ##label MAN !'##cross-references GB:K01834 REFERENCE S12843 !$#authors Mattes, F.; Tong, S.; Teubner, K.; Blum, H.E. !$#journal Nucleic Acids Res. (1990) 18:6140 !$#title Complete nucleotide sequence of a German duck hepatitis B !1virus. !$#cross-references MUID:91045092; PMID:2235507 !$#accession S12845 !'##status translation not shown !'##molecule_type DNA !'##residues 36-364 ##label MAT !'##cross-references EMBL:X12798 GENETICS !$#gene pre-S1/pre-S2/S CLASSIFICATION #superfamily hepatitis B virus surface antigen KEYWORDS glycoprotein; surface antigen FEATURE !$89-364 #product middle surface antigen (gene pre-S2/S) !8#status predicted #label DSA\ !$198-364 #product major surface antigen (gene S) #status !8predicted #label MSA\ !$32,170,296 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 364 #molecular-weight 40312 #checksum 460 SEQUENCE /// ENTRY SAVLBD #type complete TITLE large surface antigen - duck hepatitis virus (strain S5) CONTAINS major surface antigen; middle surface antigen ORGANISM #formal_name duck hepatitis virus, DHBV #note host (Shanghai brown duck) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 04-Oct-1996 ACCESSIONS C33746 REFERENCE A33746 !$#authors Uchida, M.; Esumi, M.; Shikata, T. !$#journal Virology (1989) 173:600-606 !$#title Molecular cloning and sequence analysis of duck hepatitis B !1virus genomes of a new variant isolated from Shanghai ducks. !$#cross-references MUID:90085807; PMID:2596031 !$#accession C33746 !'##molecule_type DNA !'##residues 1-366 ##label UCH !'##cross-references GB:M32990 GENETICS !$#gene pre-S1/pre-S2/S CLASSIFICATION #superfamily hepatitis B virus surface antigen KEYWORDS glycoprotein; surface antigen FEATURE !$89-366 #product middle surface antigen (gene pre-S2/S) !8#status predicted #label DSA\ !$200-366 #product major surface antigen (gene S) #status !8predicted #label MSA\ !$170,298 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 366 #molecular-weight 40897 #checksum 680 SEQUENCE /// ENTRY SAVLWD #type complete TITLE large surface antigen - duck hepatitis virus (strain S31) CONTAINS major surface antigen; middle surface antigen ORGANISM #formal_name duck hepatitis virus, DHBV #note host (Shanghai white duck) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 04-Oct-1996 ACCESSIONS D33746 REFERENCE A33746 !$#authors Uchida, M.; Esumi, M.; Shikata, T. !$#journal Virology (1989) 173:600-606 !$#title Molecular cloning and sequence analysis of duck hepatitis B !1virus genomes of a new variant isolated from Shanghai ducks. !$#cross-references MUID:90085807; PMID:2596031 !$#accession D33746 !'##molecule_type DNA !'##residues 1-366 ##label UCH !'##cross-references GB:M32990 GENETICS !$#gene pre-S1/pre-S2/S CLASSIFICATION #superfamily hepatitis B virus surface antigen KEYWORDS glycoprotein; surface antigen FEATURE !$89-366 #product middle surface antigen (gene pre-S2/S) !8#status predicted #label DSA\ !$200-366 #product major surface antigen (gene S) #status !8predicted #label MSA\ !$170,298 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 366 #molecular-weight 40858 #checksum 9521 SEQUENCE /// ENTRY SAVLWE #type complete TITLE large surface antigen - duck hepatitis virus (strain China) CONTAINS major surface antigen; middle surface antigen ORGANISM #formal_name duck hepatitis virus, DHBV DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS S12842 REFERENCE S12840 !$#authors Tong, S.; Mattes, F.; Teubner, K.; Blum, H.E. !$#journal Nucleic Acids Res. (1990) 18:6139 !$#title Complete nucleotide sequence of a Chinese duck hepatitis B !1virus. !$#cross-references MUID:91045091; PMID:2235506 !$#accession S12842 !'##status translation not shown !'##molecule_type DNA !'##residues 1-365 ##label TON !'##cross-references GB:M21953; NID:g325435; PIDN:AAA45746.1; !1PID:g325438 GENETICS !$#gene pre-S1/pre-S2/S CLASSIFICATION #superfamily hepatitis B virus surface antigen KEYWORDS glycoprotein; surface antigen FEATURE !$89-365 #product middle surface antigen (gene pre-S2/S) !8#status predicted #label DSA\ !$199-365 #product major surface antigen (gene S) #status !8predicted #label MSA\ !$297 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 365 #molecular-weight 40511 #checksum 54 SEQUENCE /// ENTRY SAVLHH #type complete TITLE large surface antigen - heron hepatitis virus CONTAINS major surface antigen; middle surface antigen ORGANISM #formal_name heron hepatitis virus, HHBV #note host Ardea cinerea (gray heron) DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS B30082 REFERENCE A93037 !$#authors Sprengel, R.; Kaleta, E.F.; Will, H. !$#journal J. Virol. (1988) 62:3832-3839 !$#title Isolation and characterization of a hepatitis B virus !1endemic in herons. !$#cross-references MUID:88333160; PMID:3418788 !$#accession B30082 !'##molecule_type DNA !'##residues 1-335 ##label SPR !'##cross-references GB:M22056; NID:g325452; PIDN:AAA45739.1; !1PID:g325455 GENETICS !$#gene pre-S1/pre-S2/S CLASSIFICATION #superfamily hepatitis B virus surface antigen KEYWORDS glycoprotein; surface antigen FEATURE !$130-335 #product middle surface antigen (gene pre-S2/S) !8#status predicted #label DSA\ !$167-335 #product major surface antigen (gene S) #status !8predicted #label MSA\ !$265 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 335 #molecular-weight 37218 #checksum 9723 SEQUENCE /// ENTRY NKVLAH #type complete TITLE e antigen precursor / core antigen - hepatitis B virus (subtype ayw4, isolate hb321 and others) ALTERNATE_NAMES HBe antigen precursor / HBc antigen; pre-C/C antigen CONTAINS core antigen; e antigen ORGANISM #formal_name hepatitis B virus, HBV #variety subtype ayw4, isolate hb321; isolate patient Ferracuti'83; isolate patient Castag'83; isolate patient Sanna'84; isolate patient Licheri-1'85; isolate patient Flore-1'86; isolate patient Licheri'83 DATE 18-Dec-1981 #sequence_revision 08-Nov-1996 #text_change 16-Jul-1999 ACCESSIONS S47405; S53191; S53209; S53234; S53264; S53249; S53262; !1S53277; A03711 REFERENCE S47404 !$#authors Plucienniczak, A. !$#submission submitted to the EMBL Data Library, August 1994 !$#description Molecular cloning and sequencing of two complete genomes of !1polish isolates of human hepatitis B virus. !$#accession S47405 !'##molecule_type DNA !'##residues 1-212 ##label PLU !'##cross-references EMBL:Z35716; NID:g527435; PIDN:CAA84786.1; !1PID:g527437 !'##experimental_source subtype ayw4, isolate hb321 REFERENCE S53112 !$#authors Lai, M.E.; Mazzoleni, A.P.; Porru, A.; Balestrieri, A. !$#submission submitted to the EMBL Data Library, March 1995 !$#accession S53191 !'##molecule_type DNA !'##residues 1-212 ##label LAI !'##cross-references EMBL:X85283; NID:g736088; PIDN:CAA59593.1; !1PID:g736090 !'##experimental_source isolate patient Ferracuti'83 !$#accession S53209 !'##molecule_type DNA !'##residues 1-212 ##label LA2 !'##cross-references EMBL:X85290; NID:g736114; PIDN:CAA59609.1; !1PID:g736116 !'##experimental_source isolate patient Castag'83 !$#accession S53234 !'##molecule_type DNA !'##residues 1-212 ##label LA3 !'##cross-references EMBL:X85300; NID:g736150; PIDN:CAA59631.1; !1PID:g736152 !'##experimental_source isolate patient Sanna'84 !$#accession S53264 !'##molecule_type DNA !'##residues 1-212 ##label LA4 !'##cross-references EMBL:X85313; NID:g736194; PIDN:CAA59659.1; !1PID:g736196 !'##experimental_source isolate patient Licheri-1'85 !$#accession S53249 !'##molecule_type DNA !'##residues 1-212 ##label LA5 !'##cross-references EMBL:X85306; NID:g736172; PIDN:CAA59644.1; !1PID:g736174 !'##experimental_source isolate patient Flore-1'86 !$#accession S53262 !'##molecule_type DNA !'##residues 1-212 ##label LA6 !'##cross-references EMBL:X85312; NID:g736191; PIDN:CAA59657.1; !1PID:g736193 !'##experimental_source isolate patient Licheri'83 !$#accession S53277 !'##molecule_type DNA !'##residues 30-212 ##label LA7 !'##cross-references EMBL:X85317; NID:g736211; PIDN:CAA59669.1; !1PID:g736214 !'##experimental_source patient Giordo-2'86 !'##note due to a stop codon between the alternative initiators the e !1antigen precursor cannot be processed REFERENCE A93214 !$#authors Galibert, F.; Mandart, E.; Fitoussi, F.; Tiollais, P.; !1Charnay, P. !$#journal Nature (1979) 281:646-650 !$#title Nucleotide sequence of the hepatitis B virus genome (subtype !1ayw) in E. coli. !$#cross-references MUID:81012091; PMID:399327 !$#accession A03711 !'##molecule_type DNA !'##residues 1-212 ##label GAL !'##cross-references GB:J02203; NID:g329640; PIDN:AAA45489.1; !1PID:g329642 !'##experimental_source subtype ayw GENETICS !$#gene C CLASSIFICATION #superfamily hepatitis B virus core antigen KEYWORDS alternative initiators; core protein FEATURE !$1-29 #domain signal sequence #status predicted #label SIG\ !$30-212 #product core antigen #status predicted #label CAG\ !$30-178 #product e antigen #status predicted #label EAG\ !$179-212 #domain carboxyl-terminal propeptide #link EAG !8#status predicted #label ECP SUMMARY #length 212 #molecular-weight 24350 #checksum 782 SEQUENCE /// ENTRY NKVLBH #type complete TITLE e antigen precursor / core antigen - hepatitis B virus (subtype ayw, strain pHB320) ALTERNATE_NAMES HBe antigen precursor / HBc antigen; pre-C/C antigen CONTAINS core antigen; e antigen ORGANISM #formal_name hepatitis B virus, HBV #variety subtype ayw, strain pHB320 #note host Homo sapiens (man) DATE 17-Mar-1987 #sequence_revision 08-Nov-1996 #text_change 28-Jul-2000 ACCESSIONS A03712 REFERENCE A05237 !$#authors Bichko, V.; Pushko, P.; Dreilina, D.; Pumpen, P.; Gren, E. !$#journal FEBS Lett. (1985) 185:208-212 !$#title Subtype ayw variant of hepatitis B virus: DNA primary !1structure analysis. !$#cross-references MUID:85204397; PMID:3996597 !$#accession A03712 !'##molecule_type DNA !'##residues 1-212 ##label BIC !'##cross-references GB:X02496; NID:g62280; PIDN:CAB41698.1; !1PID:g4704318 !'##experimental_source subtype ayw, strain pHB320 GENETICS !$#gene C CLASSIFICATION #superfamily hepatitis B virus core antigen KEYWORDS alternative initiators; core protein FEATURE !$1-29 #domain signal sequence #status predicted #label SIG\ !$30-212 #product core antigen #status predicted #label CAG\ !$30-178 #product e antigen #status predicted #label EAG\ !$179-212 #domain carboxyl-terminal propeptide #link EAG !8#status predicted #label ECP SUMMARY #length 212 #molecular-weight 24363 #checksum 478 SEQUENCE /// ENTRY NKVLA2 #type complete TITLE core antigen - hepatitis B virus (subtype adyw) ORGANISM #formal_name hepatitis B virus, HBV #variety subtype adyw DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS B93217; A03711 REFERENCE A93217 !$#authors Pasek, M.; Goto, T.; Gilbert, W.; Zink, B.; Schaller, H.; !1MacKay, P.; Leadbetter, G.; Murray, K. !$#journal Nature (1979) 282:575-579 !$#title Hepatitis B virus genes and their expression in E. coli. !$#cross-references MUID:81012115; PMID:399329 !$#accession B93217 !'##molecule_type DNA !'##residues 1-183 ##label PAS !'##cross-references GB:J02202; NID:g329637; PIDN:AAA45486.1; !1PID:g329638 !'##experimental_source subtype adyw !'##note due to a stop codon between the alternative initiators the e !1antigen precursor cannot be produced GENETICS !$#gene C CLASSIFICATION #superfamily hepatitis B virus core antigen KEYWORDS core protein FEATURE !$1-183 #product core antigen #status predicted #label MAT SUMMARY #length 183 #molecular-weight 21042 #checksum 1824 SEQUENCE /// ENTRY NKVLA3 #type complete TITLE e antigen precursor / core antigen - hepatitis B virus (subtype adw2) ALTERNATE_NAMES HBe antigen precursor / HBc antigen; pre-C/C antigen CONTAINS core antigen; e antigen ORGANISM #formal_name hepatitis B virus, HBV #variety subtype adw2 DATE 30-Jun-1992 #sequence_revision 08-Nov-1996 #text_change 15-Aug-1997 ACCESSIONS C94409; A03711 REFERENCE A94409 !$#authors Valenzuela, P.; Quiroga, M.; Zaldivar, J.; Gray, P.; Rutter, !1W.J. !$#book Animal Virus Genetics, Field, B.N., Jaenisch, R., and Fox, !1C.F., eds., pp.57-70, Academic Press, New York, 1980 !$#accession C94409 !'##molecule_type DNA !'##residues 1-214 ##label VAL !'##cross-references EMBL:X02763 !'##experimental_source subtype adw2 GENETICS !$#gene C CLASSIFICATION #superfamily hepatitis B virus core antigen KEYWORDS alternative initiators; core protein FEATURE !$1-29 #domain signal sequence #status predicted #label SIG\ !$30-214 #product core antigen #status predicted #label CAG\ !$30-178 #product e antigen #status predicted #label EAG\ !$179-214 #domain carboxyl-terminal propeptide #link EAG !8#status predicted #label ECP SUMMARY #length 214 #molecular-weight 24580 #checksum 7323 SEQUENCE /// ENTRY NKVLA4 #type complete TITLE e antigen precursor / core antigen - hepatitis B virus (subtype adr and others) ALTERNATE_NAMES HBe antigen precursor / HBc antigen; pre-C/C antigen CONTAINS core antigen; e antigen ORGANISM #formal_name hepatitis B virus, HBV #variety subtypes adr; adr4; adw; 09D09HCC DATE 30-Jun-1992 #sequence_revision 08-Nov-1996 #text_change 28-Jul-2000 ACCESSIONS A93480; C28925; B93460; S35530; T13467; A03711 REFERENCE A93480 !$#authors Fujiyama, A.; Miyanohara, A.; Nozaki, C.; Yoneyama, T.; !1Ohtomo, N.; Matsubara, K. !$#journal Nucleic Acids Res. (1983) 11:4601-4610 !$#title Cloning and structural analyses of hepatitis B virus DNAs, !1subtype adr. !$#cross-references MUID:83246570; PMID:6306594 !$#accession A93480 !'##molecule_type DNA !'##residues 1-212 ##label FUJ !'##cross-references GB:X01587; NID:g59404; PIDN:CAA25745.1; PID:g59407 !'##experimental_source subtype adr4 REFERENCE JS0253 !$#authors Okamoto, H.; Tsuda, F.; Sakugawa, H.; Sastrosoewignjo, R.I.; !1Imai, M.; Miyakawa, Y.; Mayumi, M. !$#journal J. Gen. Virol. (1988) 69:2575-2583 !$#title Typing hepatitis B virus by homology in nucleotide sequence: !1comparison of surface antigen subtypes. !$#cross-references MUID:89010694; PMID:3171552 !$#accession C28925 !'##status translation not shown !'##molecule_type DNA !'##residues 1-212 ##label OKA !'##cross-references EMBL:D00331; NID:g221499 !'##experimental_source subtype adw, strain Indonesia/pIDW420 REFERENCE A93460 !$#authors Ono, Y.; Onda, H.; Sasada, R.; Igarashi, K.; Sugino, Y.; !1Nishioka, K. !$#journal Nucleic Acids Res. (1983) 11:1747-1757 !$#title The complete nucleotide sequences of the cloned hepatitis B !1virus DNA; subtype adr and adw. !$#cross-references MUID:83168919; PMID:6300776 !$#accession B93460 !'##molecule_type DNA !'##residues 30-212 ##label ONO !'##cross-references GB:V00867 !'##experimental_source subtype adr !'##note due to a missing start codon for pre-C the e antigen precursor !1cannot be produced REFERENCE S35527 !$#authors Mukaide, M.; Kumazawa, T.; Hoshi, A.; Kawaguchi, R.; Hikiji, !1K. !$#journal Nucleic Acids Res. (1992) 20:6105 !$#title The complete nucleotide sequence of hepatitis B virus, !1subtype adr (SRADR) and phylogenetic analysis. !$#cross-references MUID:93096607; PMID:1461746 !$#accession S35530 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-212 ##label MUK !'##cross-references EMBL:D12980; NID:g221500; PIDN:BAA02357.1; !1PID:g221504 !'##experimental_source subtype adr !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1992 REFERENCE Z17684 !$#authors Takahashi, K.; Akahane, Y.; Hino, K.; Ohta, Y.; Mishiro, S. !$#journal Arch. Virol. (1998) 143:2313-2326 !$#title Hepatitis B virus genomic sequence in the circulation of !1hepatocellular carcinoma patients: comparative analysis of !140 full-length isolates. !$#cross-references MUID:99129050; PMID:9930189 !$#accession T13467 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-212 ##label TAK !'##cross-references EMBL:AB014368; NID:g3551304; PIDN:BAA32862.1; !1PID:g3551306 !'##experimental_source Japanese patient with hepatocellular carcinoma !1isolate 09D09HCC GENETICS !$#gene C CLASSIFICATION #superfamily hepatitis B virus core antigen KEYWORDS alternative initiators; core protein FEATURE !$1-29 #domain signal sequence #status predicted #label SIG\ !$30-212 #product core antigen #status predicted #label CAG\ !$30-178 #product e antigen #status predicted #label EAG\ !$179-212 #domain carboxyl-terminal propeptide #link EAG !8#status predicted #label ECP SUMMARY #length 212 #molecular-weight 24329 #checksum 9837 SEQUENCE /// ENTRY NKVLA6 #type complete TITLE e antigen precursor / core antigen - hepatitis B virus (subtype adw) ALTERNATE_NAMES HBe antigen precursor / HBc antigen; pre-C/C antigen CONTAINS core antigen; e antigen ORGANISM #formal_name hepatitis B virus, HBV #variety subtype adw DATE 30-Jun-1992 #sequence_revision 08-Nov-1996 #text_change 15-Aug-1997 ACCESSIONS C93460; A03711 REFERENCE A93460 !$#authors Ono, Y.; Onda, H.; Sasada, R.; Igarashi, K.; Sugino, Y.; !1Nishioka, K. !$#journal Nucleic Acids Res. (1983) 11:1747-1757 !$#title The complete nucleotide sequences of the cloned hepatitis B !1virus DNA; subtype adr and adw. !$#cross-references MUID:83168919; PMID:6300776 !$#accession C93460 !'##molecule_type DNA !'##residues 1-214 ##label ONO !'##cross-references GB:V00866 GENETICS !$#gene C CLASSIFICATION #superfamily hepatitis B virus core antigen KEYWORDS alternative initiators; core protein FEATURE !$1-29 #domain signal sequence #status predicted #label SIG\ !$30-214 #product core antigen #status predicted #label CAG\ !$30-178 #product e antigen #status predicted #label EAG\ !$179-214 #domain carboxyl-terminal propeptide #link EAG !8#status predicted #label ECP SUMMARY #length 214 #molecular-weight 24642 #checksum 7868 SEQUENCE /// ENTRY NKVLJ1 #type complete TITLE e antigen precursor / core antigen - hepatitis B virus (subtype adw, strain Japan/pJDW233) ALTERNATE_NAMES HBe antigen precursor / HBc antigen; pre-C/C antigen CONTAINS core antigen; e antigen ORGANISM #formal_name hepatitis B virus, HBV #variety subtype adw, strain Japan/pJDW233 DATE 31-Mar-1990 #sequence_revision 08-Nov-1996 #text_change 14-Nov-1997 ACCESSIONS A28925 REFERENCE JS0253 !$#authors Okamoto, H.; Tsuda, F.; Sakugawa, H.; Sastrosoewignjo, R.I.; !1Imai, M.; Miyakawa, Y.; Mayumi, M. !$#journal J. Gen. Virol. (1988) 69:2575-2583 !$#title Typing hepatitis B virus by homology in nucleotide sequence: !1comparison of surface antigen subtypes. !$#cross-references MUID:89010694; PMID:3171552 !$#accession A28925 !'##status translation not shown !'##molecule_type DNA !'##residues 1-212 ##label OKA !'##cross-references EMBL:D00329; NID:g221498 !'##experimental_source subtype adw, strain Japan/pJDW233 GENETICS !$#gene C CLASSIFICATION #superfamily hepatitis B virus core antigen KEYWORDS alternative initiators; core protein FEATURE !$1-29 #domain signal sequence #status predicted #label SIG\ !$30-212 #product core antigen #status predicted #label CAG\ !$30-178 #product e antigen #status predicted #label EAG\ !$179-212 #domain carboxyl-terminal propeptide #link EAG !8#status predicted #label ECP SUMMARY #length 212 #molecular-weight 24444 #checksum 1042 SEQUENCE /// ENTRY NKVLJ2 #type complete TITLE e antigen precursor / core antigen - hepatitis B virus (subtype adw, strain Okinawa/pODW282) ALTERNATE_NAMES HBe antigen precursor / HBc antigen; pre-C/C antigen CONTAINS core antigen; e antigen ORGANISM #formal_name hepatitis B virus, HBV #variety subtype adw, strain Okinawa/pODW282 DATE 31-Mar-1990 #sequence_revision 08-Nov-1996 #text_change 14-Nov-1997 ACCESSIONS B28925 REFERENCE JS0253 !$#authors Okamoto, H.; Tsuda, F.; Sakugawa, H.; Sastrosoewignjo, R.I.; !1Imai, M.; Miyakawa, Y.; Mayumi, M. !$#journal J. Gen. Virol. (1988) 69:2575-2583 !$#title Typing hepatitis B virus by homology in nucleotide sequence: !1comparison of surface antigen subtypes. !$#cross-references MUID:89010694; PMID:3171552 !$#accession B28925 !'##status translation not shown !'##molecule_type DNA !'##residues 1-212 ##label OKA !'##cross-references EMBL:D00330; NID:g221498 !'##experimental_source subtype adw, strain Okinawa/pODW282 GENETICS !$#gene C CLASSIFICATION #superfamily hepatitis B virus core antigen KEYWORDS alternative initiators; core protein FEATURE !$1-29 #domain signal sequence #status predicted #label SIG\ !$30-212 #product core antigen #status predicted #label CAG\ !$30-178 #product e antigen #status predicted #label EAG\ !$179-212 #domain carboxyl-terminal propeptide #link EAG !8#status predicted #label ECP SUMMARY #length 212 #molecular-weight 24315 #checksum 565 SEQUENCE /// ENTRY NKVLKS #type complete TITLE e antigen precursor / core antigen - hepatitis B virus (subtype adw, strain 991) ALTERNATE_NAMES HBe antigen precursor / HBc antigen; pre-C/C antigen CONTAINS core antigen; e antigen ORGANISM #formal_name hepatitis B virus, HBV #variety subtype adw isolate HBV 991 DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 05-Sep-1997 ACCESSIONS S10381 REFERENCE S10380 !$#authors Koechel, H.G.; Schueler, A.; Lottmann, S.; Thomssen, R. !$#submission submitted to the EMBL Data Library, February 1990 !$#accession S10381 !'##molecule_type DNA !'##residues 1-214 ##label KOE !'##cross-references EMBL:X51970; NID:g1155012; PID:g60433 GENETICS !$#gene C CLASSIFICATION #superfamily hepatitis B virus core antigen KEYWORDS alternative initiators; core protein FEATURE !$1-29 #domain signal sequence #status predicted #label SIG\ !$30-214 #product core antigen #status predicted #label CAG\ !$30-178 #product e antigen #status predicted #label EAG\ !$179-214 #domain carboxyl-terminal propeptide #link EAG !8#status predicted #label ECP SUMMARY #length 214 #molecular-weight 24722 #checksum 7954 SEQUENCE /// ENTRY NKVLA1 #type complete TITLE e antigen precursor / core antigen - hepatitis B virus (strain alpha1) ALTERNATE_NAMES HBe antigen precursor / HBc antigen; pre-C/C antigen CONTAINS core antigen; e antigen ORGANISM #formal_name hepatitis B virus, HBV #variety strain alpha1 DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 15-Aug-1997 ACCESSIONS A34773 REFERENCE A34773 !$#authors Tong, S.; Li, J.; Vitvitski, L.; Trepo, C. !$#journal Virology (1990) 176:596-603 !$#title Active hepatitis B virus replication in the presence of !1anti-HBe is associated with viral variants containing an !1inactive pre-C region. !$#cross-references MUID:90266476; PMID:2345966 !$#accession A34773 !'##status translation not shown !'##molecule_type DNA !'##residues 1-211 ##label TON !'##cross-references EMBL:M32138 GENETICS !$#gene C !$#introns 27/3 CLASSIFICATION #superfamily hepatitis B virus core antigen KEYWORDS alternative initiators; core protein FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-211 #product core antigen #status predicted #label CAG\ !$29-177 #product e antigen #status predicted #label EAG\ !$178-211 #domain carboxyl-terminal propeptide #link EAG !8#status predicted #label ECP SUMMARY #length 211 #molecular-weight 24208 #checksum 7952 SEQUENCE /// ENTRY NKVLCP #type complete TITLE core antigen - hepatitis B virus (strain LSH, chimpanzee) ALTERNATE_NAMES HBc antigen ORGANISM #formal_name hepatitis B virus, HBV #variety strain LSH, chimpanzee DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jun-2000 ACCESSIONS A28885 REFERENCE A92796 !$#authors Vaudin, M.; Wolstenholme, A.J.; Tsiquaye, K.N.; Zuckerman, !1A.J.; Harrison, T.J. !$#journal J. Gen. Virol. (1988) 69:1383-1389 !$#title The complete nucleotide sequence of the genome of a !1hepatitis B virus isolated from a naturally infected !1chimpanzee. !$#cross-references MUID:88258473; PMID:2838576 !$#accession A28885 !'##molecule_type DNA !'##residues 1-183 ##label VAU !'##cross-references EMBL:D00220; NID:g221505; PIDN:BAA00157.1; !1PID:g221506 !'##experimental_source strain LSH, chimpanzee !'##note due to a stop codon between the alternative initiators the e !1antigen precursor cannot be processed GENETICS !$#gene C CLASSIFICATION #superfamily hepatitis B virus core antigen KEYWORDS core protein SUMMARY #length 183 #molecular-weight 20999 #checksum 2447 SEQUENCE /// ENTRY NKVLH3 #type complete TITLE core antigen - hepatitis B virus ORGANISM #formal_name hepatitis B virus, HBV #note host Homo sapiens (man) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 01-Aug-1997 ACCESSIONS A37182 REFERENCE A37182 !$#authors Bhat, R.A.; Ulrich, P.P.; Vyas, G.N. !$#journal Hepatology (1990) 11:271-276 !$#title Molecular characterization of a new variant of hepatitis B !1virus in a persistently infected homosexual man. !$#cross-references MUID:90169850; PMID:2307406 !$#accession A37182 !'##molecule_type DNA !'##residues 1-195 ##label BHA GENETICS !$#gene C CLASSIFICATION #superfamily hepatitis B virus core antigen KEYWORDS core protein SUMMARY #length 195 #molecular-weight 22461 #checksum 1050 SEQUENCE /// ENTRY NKVLC #type complete TITLE core antigen - woodchuck hepatitis virus ORGANISM #formal_name woodchuck hepatitis virus DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 16-Jul-1999 ACCESSIONS C32397; B29969; A03713; F29969 REFERENCE A92986 !$#authors Galibert, F.; Chen, T.N.; Mandart, E. !$#journal J. Virol. (1982) 41:51-65 !$#title Nucleotide sequence of a cloned woodchuck hepatitis virus !1genome: comparison with the hepatitis B virus sequence. !$#cross-references MUID:82216969; PMID:7086958 !$#accession C32397 !'##molecule_type DNA !'##residues 1-188 ##label GAL !'##cross-references GB:J02442; NID:g336126; PIDN:AAA46761.1; !1PID:g336129 !'##experimental_source woodchuck hepatitis virus 1 REFERENCE A94222 !$#authors Girones, R.; Cote, P.J.; Hornbuckle, W.E.; Tennant, B.C.; !1Gerin, J.L.; Purcell, R.H.; Miller, R.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:1846-1849 !$#title Complete nucleotide sequence of a molecular clone of !1woodchuck hepatitis virus that is infectious in the natural !1host. !$#cross-references MUID:89184524; PMID:2928306 !$#accession B29969 !'##molecule_type DNA !'##residues 1-188 ##label GIR !'##cross-references GB:J04514; NID:g336146; PIDN:AAA46772.1; !1PID:g336149 !'##experimental_source woodchuck hepatitis virus 8 REFERENCE A94368 !$#authors Cohen, J.I.; Miller, R.H.; Rosenblum, B.; Denniston, K.; !1Gerin, J.L.; Purcell, R.H. !$#journal Virology (1988) 162:12-20 !$#title Sequence comparison of woodchuck hepatitis virus replicative !1forms shows conservation of the genome. !$#cross-references MUID:88101359; PMID:3336938 !$#accession A03713 !'##molecule_type DNA !'##residues 1-188 ##label COH !'##cross-references GB:M19183; NID:g336141; PIDN:AAA46765.1; !1PID:g336145 !'##experimental_source woodchuck hepatitis virus 59 !$#accession F29969 !'##molecule_type DNA !'##residues 1-188 ##label CO2 !'##cross-references GB:M18752; NID:g336136; PIDN:AAA46769.1; !1PID:g336140 !'##experimental_source woodchuck hepatitis virus 7 CLASSIFICATION #superfamily hepatitis B virus core antigen KEYWORDS core protein SUMMARY #length 188 #molecular-weight 21693 #checksum 5872 SEQUENCE /// ENTRY NKVLC2 #type complete TITLE core antigen - woodchuck hepatitis virus (clone 2) ORGANISM #formal_name woodchuck hepatitis virus DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 16-Jul-1999 ACCESSIONS A03714 REFERENCE A93015 !$#authors Kodama, K.; Ogasawara, N.; Yoshikawa, H.; Murakami, S. !$#journal J. Virol. (1985) 56:978-986 !$#title Nucleotide sequence of a cloned woodchuck hepatitis virus !1genome: evolutional relationship between hepadnaviruses. !$#cross-references MUID:86062931; PMID:3855246 !$#accession A03714 !'##molecule_type DNA !'##residues 1-187 ##label KOD !'##cross-references GB:M11082; NID:g336132; PIDN:AAA19185.1; !1PID:g336135 CLASSIFICATION #superfamily hepatitis B virus core antigen KEYWORDS core protein SUMMARY #length 187 #molecular-weight 21579 #checksum 4707 SEQUENCE /// ENTRY NKVLS #type complete TITLE core antigen - ground squirrel hepatitis virus ORGANISM #formal_name ground squirrel hepatitis virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS A03715 REFERENCE A93000 !$#authors Seeger, C.; Ganem, D.; Varmus, H.E. !$#journal J. Virol. (1984) 51:367-375 !$#title Nucleotide sequence of an infectious molecularly cloned !1genome of ground squirrel hepatitis virus. !$#cross-references MUID:84267998; PMID:6086950 !$#accession A03715 !'##molecule_type DNA !'##residues 1-217 ##label SEE !'##cross-references GB:K02715; NID:g325400; PIDN:AAA46755.1; !1PID:g325401 CLASSIFICATION #superfamily hepatitis B virus core antigen SUMMARY #length 217 #molecular-weight 25189 #checksum 7690 SEQUENCE /// ENTRY NKVLD #type complete TITLE core antigen - duck hepatitis virus ORGANISM #formal_name duck hepatitis virus, DHBV DATE 20-Sep-1984 #sequence_revision 20-Sep-1984 #text_change 16-Jul-1999 ACCESSIONS A03716; S12846 REFERENCE A92997 !$#authors Mandart, E.; Kay, A.; Galibert, F. !$#journal J. Virol. (1984) 49:782-792 !$#title Nucleotide sequence of a cloned duck hepatitis B virus !1genome: comparison with woodchuck and human hepatitis B !1virus sequences. !$#cross-references MUID:84138772; PMID:6699938 !$#accession A03716 !'##molecule_type DNA !'##residues 1-305 ##label MAN !'##cross-references GB:K01834; NID:g325431; PIDN:AAA45741.1; !1PID:g325432 REFERENCE S12843 !$#authors Mattes, F.; Tong, S.; Teubner, K.; Blum, H.E. !$#journal Nucleic Acids Res. (1990) 18:6140 !$#title Complete nucleotide sequence of a German duck hepatitis B !1virus. !$#cross-references MUID:91045092; PMID:2235507 !$#accession S12846 !'##status translation not shown !'##molecule_type DNA !'##residues 1-168 ##label MAT !'##cross-references EMBL:X12798 CLASSIFICATION #superfamily hepatitis B virus core antigen SUMMARY #length 305 #molecular-weight 34981 #checksum 3831 SEQUENCE /// ENTRY NKVLBD #type complete TITLE core antigen - duck hepatitis virus (strain S5) ORGANISM #formal_name duck hepatitis virus, DHBV #note host (Shanghai brown duck) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 01-Aug-1997 ACCESSIONS E33746 REFERENCE A33746 !$#authors Uchida, M.; Esumi, M.; Shikata, T. !$#journal Virology (1989) 173:600-606 !$#title Molecular cloning and sequence analysis of duck hepatitis B !1virus genomes of a new variant isolated from Shanghai ducks. !$#cross-references MUID:90085807; PMID:2596031 !$#accession E33746 !'##status translation not shown !'##molecule_type DNA !'##residues 1-305 ##label UCH GENETICS !$#introns 168/3 CLASSIFICATION #superfamily hepatitis B virus core antigen KEYWORDS core protein SUMMARY #length 305 #molecular-weight 34866 #checksum 3097 SEQUENCE /// ENTRY NKVLWD #type complete TITLE core antigen - duck hepatitis virus (strain S31) ORGANISM #formal_name duck hepatitis virus, DHBV #note host (Shanghai white duck) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 01-Aug-1997 ACCESSIONS F33746 REFERENCE A33746 !$#authors Uchida, M.; Esumi, M.; Shikata, T. !$#journal Virology (1989) 173:600-606 !$#title Molecular cloning and sequence analysis of duck hepatitis B !1virus genomes of a new variant isolated from Shanghai ducks. !$#cross-references MUID:90085807; PMID:2596031 !$#accession F33746 !'##status translation not shown !'##molecule_type DNA !'##residues 1-305 ##label UCH GENETICS !$#introns 168/3 CLASSIFICATION #superfamily hepatitis B virus core antigen KEYWORDS core protein SUMMARY #length 305 #molecular-weight 34929 #checksum 2538 SEQUENCE /// ENTRY NKVLDS #type complete TITLE core antigen - duck hepatitis virus (isolate Shanghai) ORGANISM #formal_name duck hepatitis virus, DHBV DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS S12840 REFERENCE S12840 !$#authors Tong, S.; Mattes, F.; Teubner, K.; Blum, H.E. !$#journal Nucleic Acids Res. (1990) 18:6139 !$#title Complete nucleotide sequence of a Chinese duck hepatitis B !1virus. !$#cross-references MUID:91045091; PMID:2235506 !$#accession S12840 !'##status translation not shown !'##molecule_type DNA !'##residues 1-305 ##label TON !'##cross-references EMBL:M21953; NID:g325435; PIDN:AAA45744.1; !1PID:g325436 CLASSIFICATION #superfamily hepatitis B virus core antigen KEYWORDS core protein SUMMARY #length 305 #molecular-weight 34896 #checksum 3632 SEQUENCE /// ENTRY NKVLHH #type complete TITLE core antigen - heron hepatitis virus ORGANISM #formal_name heron hepatitis virus, HHBV #note host Ardea cinerea (gray heron) DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS C30082 REFERENCE A93037 !$#authors Sprengel, R.; Kaleta, E.F.; Will, H. !$#journal J. Virol. (1988) 62:3832-3839 !$#title Isolation and characterization of a hepatitis B virus !1endemic in herons. !$#cross-references MUID:88333160; PMID:3418788 !$#accession C30082 !'##molecule_type DNA !'##residues 1-305 ##label SPR !'##cross-references GB:M22056; NID:g325452; PIDN:AAA45737.1; !1PID:g325453 CLASSIFICATION #superfamily hepatitis B virus core antigen KEYWORDS core protein SUMMARY #length 305 #molecular-weight 34925 #checksum 7412 SEQUENCE /// ENTRY SAVLDV #type complete TITLE delta large antigen - hepatitis delta virus (chimpanzee isolate) ALTERNATE_NAMES HDag ORGANISM #formal_name hepatitis delta virus DATE 30-Sep-1987 #sequence_revision 31-Dec-1990 #text_change 01-Aug-1997 ACCESSIONS A26176; A30028 REFERENCE A26176 !$#authors Wang, K.S.; Choo, Q.L.; Weiner, A.J.; Ou, J.H.; Najarian, !1R.C.; Thayer, R.M.; Mullenbach, G.T.; Denniston, K.J.; !1Gerin, J.L.; Houghton, M. !$#journal Nature (1986) 323:508-514 !$#title Structure, sequence and expression of the hepatitis delta !1(delta) viral genome. !$#cross-references MUID:87014821; PMID:3762705 !$#accession A26176 !'##molecule_type genomic RNA !'##residues 1-161 ##label WAN !'##cross-references GB:X04451 !'##note the nucleotide sequence contains a frameshift error in codon !1162 that has been corrected in reference A30028 REFERENCE A30028 !$#authors Wang, K.S.; Choo, Q.L.; Weiner, A.J.; Ou, J.H.; Najarian, !1R.C.; Thayer, R.M.; Mullenbach, G.T.; Denniston, K.J.; !1Gerin, J.L.; Houghton, M. !$#journal Nature (1987) 328:456 !$#contents corrections !$#accession A30028 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type genomic RNA !'##residues 1-214 ##label WA2 !'##cross-references GB:M21012 !'##note this corrects a frameshift error in codon 162 of the published !1sequence COMMENT This virus is a replication-defective hepatitis B virus. CLASSIFICATION #superfamily hepatitis delta virus large antigen KEYWORDS core protein; lipoprotein; methylated carboxyl end; !1prenylated cysteine FEATURE !$2-211 #product delta large antigen #status predicted #label !8MAT\ !$211 #binding_site farnesyl (Cys) (covalent) #status !8predicted\ !$211 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted SUMMARY #length 214 #molecular-weight 24078 #checksum 6717 SEQUENCE /// ENTRY SAVLWC #type complete TITLE delta large antigen - hepatitis delta virus (woodchuck isolate) ALTERNATE_NAMES HDag ORGANISM #formal_name hepatitis delta virus DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 01-Aug-1997 ACCESSIONS A30054 REFERENCE A30054 !$#authors Kuo, M.Y.P.; Goldberg, J.; Coates, L.; Mason, W.; Gerin, J.; !1Taylor, J. !$#journal J. Virol. (1988) 62:1855-1861 !$#title Molecular cloning of hepatitis delta virus RNA from an !1infected woodchuck liver: sequence, structure, and !1applications. !$#cross-references MUID:88215010; PMID:3367426 !$#accession A30054 !'##molecule_type genomic RNA !'##residues 1-205 ##label KUO !'##cross-references GB:M21012 COMMENT This virus is a replication-defective hepatitis B virus. CLASSIFICATION #superfamily hepatitis delta virus large antigen KEYWORDS core protein FEATURE !$2-205 #product delta large antigen #status predicted #label !8MAT SUMMARY #length 205 #molecular-weight 23047 #checksum 9013 SEQUENCE /// ENTRY SAVLH1 #type complete TITLE delta large antigen - hepatitis delta virus ALTERNATE_NAMES HDag ORGANISM #formal_name hepatitis delta virus #note host Homo sapiens (man) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jun-2000 ACCESSIONS A35219 REFERENCE A35219 !$#authors Saldanha, J.A.; Thomas, H.C.; Monjardino, J.P. !$#journal J. Gen. Virol. (1990) 71:1603-1606 !$#title Cloning and sequencing of RNA of hepatitis delta virus !1isolated from human serum. !$#cross-references MUID:90324949; PMID:2374010 !$#accession A35219 !'##molecule_type genomic RNA !'##residues 1-195 ##label SAL !'##cross-references GB:D01075; NID:g221689; PIDN:BAA00874.1; !1PID:g221690 COMMENT This virus is a replication-defective hepatitis B virus. CLASSIFICATION #superfamily hepatitis delta virus large antigen KEYWORDS core protein FEATURE !$2-195 #product delta large antigen #status predicted #label !8MAT SUMMARY #length 195 #molecular-weight 21937 #checksum 8056 SEQUENCE /// ENTRY SAVLDN #type complete TITLE delta large antigen - hepatitis delta virus (strain Nauru) ALTERNATE_NAMES HDAg ORGANISM #formal_name hepatitis delta virus DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jul-1999 ACCESSIONS A36212 REFERENCE A36212 !$#authors Chao, Y.C.; Chang, M.F.; Gust, I.; Lai, M.M.C. !$#journal Virology (1990) 178:384-392 !$#title Sequence conservation and divergence of hepatitis delta !1virus RNA. !$#cross-references MUID:91020976; PMID:2219700 !$#accession A36212 !'##molecule_type genomic RNA !'##residues 1-214 ##label CHA !'##cross-references EMBL:M34325; EMBL:M58629; NID:g329994; !1PIDN:AAB59753.1; PID:g329995 REFERENCE A58234 !$#authors Otto, J.C.; Casey, P.J. !$#journal J. Biol. Chem. (1996) 271:4569-4572 !$#title The hepatitis delta virus large antigen is farnesylated both !1in vitro and in animal cells. !$#cross-references MUID:96214864; PMID:8617711 !$#contents annotation; confirmation of farnesylation rather than !1geranyl-geranylation CLASSIFICATION #superfamily hepatitis delta virus large antigen KEYWORDS core protein; lipoprotein; methylated carboxyl end; !1prenylated cysteine FEATURE !$2-211 #product delta large antigen #status predicted #label !8MAT\ !$211 #binding_site farnesyl (Cys) (covalent) #status !8experimental\ !$211 #modified_site methyl ester carboxyl end (Cys) (in !8mature form) #status predicted SUMMARY #length 214 #molecular-weight 24180 #checksum 7658 SEQUENCE /// ENTRY SAVLL1 #type complete TITLE delta large antigen - hepatitis delta virus (strain Lebanon-1) ALTERNATE_NAMES HDag ORGANISM #formal_name hepatitis delta virus #note host Homo sapiens (man) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 01-Aug-1997 ACCESSIONS A40247 REFERENCE A40247 !$#authors Lee, C.M.; Bih, F.Y.; Chao, Y.C.; Govindarajan, S.; Lai, !1M.M.C. !$#journal Virology (1992) 188:265-273 !$#title Evolution of hepatitis delta virus RNA during chronic !1infection. !$#cross-references MUID:92230225; PMID:1566577 !$#accession A40247 !'##molecule_type genomic RNA !'##residues 1-195 ##label LEE !'##cross-references GB:M84917 COMMENT This virus is a replication-defective hepatitis B virus. CLASSIFICATION #superfamily hepatitis delta virus large antigen KEYWORDS core protein FEATURE !$2-195 #product delta large antigen #status predicted #label !8MAT SUMMARY #length 195 #molecular-weight 21846 #checksum 7099 SEQUENCE /// ENTRY SAVLDM #type complete TITLE delta large antigen - hepatitis delta virus (strain Japanese M-1) ALTERNATE_NAMES HDag ORGANISM #formal_name hepatitis delta virus DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jun-2000 ACCESSIONS A36409 REFERENCE A36409 !$#authors Imazeki, F.; Omata, M.; Ohto, M. !$#journal J. Virol. (1990) 64:5594-5599 !$#title Heterogeneity and evolution rates of delta virus RNA !1sequences. !$#cross-references MUID:91012805; PMID:2214027 !$#accession A36409 !'##molecule_type genomic RNA !'##residues 1-195 ##label IMA !'##cross-references GB:D90190; GB:M58299; NID:g221691; PIDN:BAA14214.1; !1PID:g221692 CLASSIFICATION #superfamily hepatitis delta virus large antigen KEYWORDS core protein FEATURE !$2-195 #product delta large antigen #status predicted #label !8MAT SUMMARY #length 195 #molecular-weight 21811 #checksum 7815 SEQUENCE /// ENTRY SAVLDS #type complete TITLE delta large antigen - hepatitis delta virus (isolate Japanese S-1) ALTERNATE_NAMES HDag ORGANISM #formal_name hepatitis delta virus DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jun-2000 ACCESSIONS B36409; S18678 REFERENCE A36409 !$#authors Imazeki, F.; Omata, M.; Ohto, M. !$#journal J. Virol. (1990) 64:5594-5599 !$#title Heterogeneity and evolution rates of delta virus RNA !1sequences. !$#cross-references MUID:91012805; PMID:2214027 !$#accession B36409 !'##molecule_type genomic RNA !'##residues 1-195 ##label IMA1 !'##cross-references GB:D90192; GB:M58303; NID:g221695; PIDN:BAA14216.1; !1PID:g221696 !'##experimental_source isolate Japanese S-1 REFERENCE S18678 !$#authors Imazeki, F.; Omata, M.; Ohto, M. !$#journal Nucleic Acids Res. (1991) 19:5439 !$#title Complete nucleotide sequence of hepatitis delta virus RNA in !1Japan. !$#cross-references MUID:92020244; PMID:1923832 !$#accession S18678 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type genomic RNA !'##residues 1-195 ##label IMA2 !'##cross-references EMBL:X60193; NID:g59497; PIDN:CAA42749.1; !1PID:g59498 !'##experimental_source isolate Japanese S-1 !'##note note this sequence was submitted to the EMBL Data Library, June !11991 CLASSIFICATION #superfamily hepatitis delta virus large antigen KEYWORDS core protein FEATURE !$2-195 #product delta large antigen #status predicted #label !8MAT SUMMARY #length 195 #molecular-weight 21928 #checksum 8464 SEQUENCE /// ENTRY QQVLD1 #type complete TITLE gene X protein - hepatitis B virus (subtype ayw) ORGANISM #formal_name hepatitis B virus, HBV DATE 24-Sep-1981 #sequence_revision 24-Sep-1981 #text_change 08-Apr-1994 ACCESSIONS A03719 REFERENCE A93214 !$#authors Galibert, F.; Mandart, E.; Fitoussi, F.; Tiollais, P.; !1Charnay, P. !$#journal Nature (1979) 281:646-650 !$#title Nucleotide sequence of the hepatitis B virus genome (subtype !1ayw) in E. coli. !$#cross-references MUID:81012091; PMID:399327 !$#accession A03719 !'##molecule_type DNA !'##residues 1-154 ##label GAL !'##cross-references GB:J02203; GB:V01460 GENETICS !$#gene X CLASSIFICATION #superfamily hepatitis B virus gene X protein SUMMARY #length 154 #molecular-weight 16565 #checksum 3107 SEQUENCE /// ENTRY QQVLBH #type complete TITLE gene X protein - hepatitis B virus (subtype ayw, strain pHB320) ORGANISM #formal_name hepatitis B virus, HBV #variety subtype ayw, strain pHB320 DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 28-Jul-2000 ACCESSIONS A05237; S53144; S53173; S53195; S53210; S53217; S53222; !1S53224; S53235; S53237; S53239; S53241; S53243; S53245; !1S53250; S53252; S53256; S53261; S53263; S53271; S53273; !1S53275; S53278; S53280 REFERENCE A05237 !$#authors Bichko, V.; Pushko, P.; Dreilina, D.; Pumpen, P.; Gren, E. !$#journal FEBS Lett. (1985) 185:208-212 !$#title Subtype ayw variant of hepatitis B virus: DNA primary !1structure analysis. !$#cross-references MUID:85204397; PMID:3996597 !$#accession A05237 !'##status translation not shown !'##molecule_type DNA !'##residues 1-154 ##label BIC !'##cross-references EMBL:X02496; NID:g62280; PIDN:CAB41697.1; !1PID:g4704317 !'##experimental_source subtype ayw, strain pHB320 REFERENCE S53112 !$#authors Lai, M.E.; Mazzoleni, A.P.; Porru, A.; Balestrieri, A. !$#submission submitted to the EMBL Data Library, March 1995 !$#accession S53144 !'##molecule_type DNA !'##residues 124-154 ##label LAI !'##cross-references EMBL:X85267; NID:g736025; PIDN:CAA59548.1; !1PID:g736026; EMBL:X85284; EMBL:X85291; EMBL:X85295; !1EMBL:X85296; EMBL:X85301; EMBL:X85302; EMBL:X85303; !1EMBL:X85259; EMBL:X85304; EMBL:X85305; EMBL:X85307; !1EMBL:X85308; EMBL:X85310; EMBL:X85312; EMBL:X85313; !1EMBL:X85315; EMBL:X85316; EMBL:X85317; EMBL:X85318; !1EMBL:X85319; EMBL:X85294 !'##experimental_source isolate patient Pintus'85 et al. !$#accession S53173 !'##molecule_type DNA !'##residues 124-154 ##label LA2 !'##cross-references EMBL:X85277; NID:g736065; PIDN:CAA59575.1; !1PID:g736066 !'##experimental_source isolate patient Bio'90 GENETICS !$#gene X CLASSIFICATION #superfamily hepatitis B virus gene X protein SUMMARY #length 154 #molecular-weight 16644 #checksum 4637 SEQUENCE /// ENTRY A48345 #type complete TITLE gene X protein - hepatitis B virus ORGANISM #formal_name hepatitis B virus, HBV DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS A48345 REFERENCE A48345 !$#authors Repp, R.; Keller, C.; Borkhardt, A.; Csecke, A.; Schaefer, !1S.; Gerlich, W.H.; Lampert, F. !$#journal Arch. Virol. (1992) 125:299-304 !$#title Detection of a hepatitis B virus variant with a truncated X !1gene and enhancer II. !$#cross-references MUID:92352333; PMID:1642555 !$#accession A48345 !'##molecule_type DNA !'##residues 1-154 ##label REP !'##cross-references GB:S41175; NID:g252539; PIDN:AAB22732.1; !1PID:g252540 !'##note sequence extracted from NCBI backbone (NCBIN:109912, !1NCBIP:109913) GENETICS !$#gene X CLASSIFICATION #superfamily hepatitis B virus gene X protein SUMMARY #length 154 #molecular-weight 16642 #checksum 3694 SEQUENCE /// ENTRY B48345 #type complete TITLE gene X protein, truncated form - hepatitis B virus ORGANISM #formal_name hepatitis B virus, HBV DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS B48345 REFERENCE A48345 !$#authors Repp, R.; Keller, C.; Borkhardt, A.; Csecke, A.; Schaefer, !1S.; Gerlich, W.H.; Lampert, F. !$#journal Arch. Virol. (1992) 125:299-304 !$#title Detection of a hepatitis B virus variant with a truncated X !1gene and enhancer II. !$#cross-references MUID:92352333; PMID:1642555 !$#accession B48345 !'##molecule_type DNA !'##residues 1-134 ##label REP !'##cross-references GB:S41176; NID:g252541; PIDN:AAB22733.1; !1PID:g252542 !'##note sequence extracted from NCBI backbone (NCBIN:109914, !1NCBIP:109915) GENETICS !$#gene X CLASSIFICATION #superfamily hepatitis B virus gene X protein SUMMARY #length 134 #molecular-weight 14647 #checksum 8649 SEQUENCE /// ENTRY QQVLA1 #type complete TITLE gene X protein - hepatitis B virus (strain alpha1) ORGANISM #formal_name hepatitis B virus, HBV DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jul-1999 ACCESSIONS D34773 REFERENCE A34773 !$#authors Tong, S.; Li, J.; Vitvitski, L.; Trepo, C. !$#journal Virology (1990) 176:596-603 !$#title Active hepatitis B virus replication in the presence of !1anti-HBe is associated with viral variants containing an !1inactive pre-C region. !$#cross-references MUID:90266476; PMID:2345966 !$#accession D34773 !'##status translation not shown !'##molecule_type DNA !'##residues 1-154 ##label TON !'##cross-references EMBL:M32138; NID:g329667; PIDN:AAA45504.1; !1PID:g329671 GENETICS !$#gene X CLASSIFICATION #superfamily hepatitis B virus gene X protein SUMMARY #length 154 #molecular-weight 16671 #checksum 4262 SEQUENCE /// ENTRY QQVLAW #type complete TITLE gene X protein - hepatitis B virus (subtype adw and adw2) ORGANISM #formal_name hepatitis B virus, HBV DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 30-Jun-1998 ACCESSIONS A31289; B94409; A03719 REFERENCE A31289 !$#authors Lo, S.J.; Chien, M.L.; Lee, Y.H.W. !$#journal Virology (1988) 167:289-292 !$#title Characteristics of the X gene of hepatitis B virus. !$#cross-references MUID:89045656; PMID:3188399 !$#accession A31289 !'##molecule_type DNA !'##residues 1-154 ##label LOS !'##experimental_source subtype adw REFERENCE A94409 !$#authors Valenzuela, P.; Quiroga, M.; Zaldivar, J.; Gray, P.; Rutter, !1W.J. !$#book Animal Virus Genetics, Field, B.N., Jaenisch, R., and Fox, !1C.F., eds., pp.57-70, Academic Press, New York, 1980 !$#accession B94409 !'##molecule_type DNA !'##residues 1-154 ##label VAL !'##experimental_source subtype adw2 GENETICS !$#gene X CLASSIFICATION #superfamily hepatitis B virus gene X protein SUMMARY #length 154 #molecular-weight 16583 #checksum 2606 SEQUENCE /// ENTRY QQVLKS #type complete TITLE gene X protein - hepatitis B virus (subtype adw, strain 991) ORGANISM #formal_name hepatitis B virus, HBV DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jul-1999 ACCESSIONS S10380 REFERENCE S10380 !$#authors Koechel, H.G.; Schueler, A.; Lottmann, S.; Thomssen, R. !$#submission submitted to the EMBL Data Library, February 1990 !$#accession S10380 !'##molecule_type DNA !'##residues 1-154 ##label KOE !'##cross-references EMBL:X51970; NID:g1155012; PIDN:CAA36231.1; !1PID:g60432 GENETICS !$#gene X CLASSIFICATION #superfamily hepatitis B virus gene X protein SUMMARY #length 154 #molecular-weight 16553 #checksum 2531 SEQUENCE /// ENTRY QQVLCP #type complete TITLE gene X protein - hepatitis B virus (strain LSH, chimpanzee) ORGANISM #formal_name hepatitis B virus, HBV DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jun-2000 ACCESSIONS D28885 REFERENCE A92796 !$#authors Vaudin, M.; Wolstenholme, A.J.; Tsiquaye, K.N.; Zuckerman, !1A.J.; Harrison, T.J. !$#journal J. Gen. Virol. (1988) 69:1383-1389 !$#title The complete nucleotide sequence of the genome of a !1hepatitis B virus isolated from a naturally infected !1chimpanzee. !$#cross-references MUID:88258473; PMID:2838576 !$#accession D28885 !'##molecule_type DNA !'##residues 1-154 ##label VAU !'##cross-references GB:D00220; NID:g221505; PIDN:BAA00160.1; !1PID:g221509 GENETICS !$#gene X CLASSIFICATION #superfamily hepatitis B virus gene X protein SUMMARY #length 154 #molecular-weight 16759 #checksum 4686 SEQUENCE /// ENTRY QQVLC1 #type complete TITLE gene X protein - woodchuck hepatitis virus (clone 1) ORGANISM #formal_name woodchuck hepatitis virus DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 12-Jun-1998 ACCESSIONS A03720 REFERENCE A92986 !$#authors Galibert, F.; Chen, T.N.; Mandart, E. !$#journal J. Virol. (1982) 41:51-65 !$#title Nucleotide sequence of a cloned woodchuck hepatitis virus !1genome: comparison with the hepatitis B virus sequence. !$#cross-references MUID:82216969; PMID:7086958 !$#accession A03720 !'##molecule_type DNA !'##residues 1-141 ##label GAL GENETICS !$#gene X CLASSIFICATION #superfamily hepatitis B virus gene X protein SUMMARY #length 141 #molecular-weight 15221 #checksum 3171 SEQUENCE /// ENTRY QQVL64 #type complete TITLE gene X protein - woodchuck hepatitis virus (clone 64) ORGANISM #formal_name woodchuck hepatitis virus DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 16-Jul-1999 ACCESSIONS C29498 REFERENCE A91568 !$#authors Etiemble, J.; Moeroey, T.; Trepo, C.; Tiollais, P.; Buendia, !1M.A. !$#journal Gene (1986) 50:207-214 !$#title Nucleotide sequence of the woodchuck hepatitis virus surface !1antigen mRNAs and the variability of three overlapping viral !1genes. !$#cross-references MUID:87219879; PMID:3582979 !$#accession C29498 !'##molecule_type mRNA !'##residues 1-141 ##label ETI !'##cross-references GB:M15954; NID:g893289; PIDN:AAA69575.1; !1PID:g893290 GENETICS !$#gene X CLASSIFICATION #superfamily hepatitis B virus gene X protein SUMMARY #length 141 #molecular-weight 15207 #checksum 2738 SEQUENCE /// ENTRY QQVL7 #type complete TITLE gene X protein - woodchuck hepatitis virus (clone 7) ORGANISM #formal_name woodchuck hepatitis virus DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jul-1999 ACCESSIONS A29969 REFERENCE A94368 !$#authors Cohen, J.I.; Miller, R.H.; Rosenblum, B.; Denniston, K.; !1Gerin, J.L.; Purcell, R.H. !$#journal Virology (1988) 162:12-20 !$#title Sequence comparison of woodchuck hepatitis virus replicative !1forms shows conservation of the genome. !$#cross-references MUID:88101359; PMID:3336938 !$#accession A29969 !'##molecule_type DNA !'##residues 1-141 ##label COH !'##cross-references GB:M18752; NID:g336136; PIDN:AAA46768.1; !1PID:g336139 GENETICS !$#gene X CLASSIFICATION #superfamily hepatitis B virus gene X protein SUMMARY #length 141 #molecular-weight 15231 #checksum 2890 SEQUENCE /// ENTRY QQVLW8 #type complete TITLE gene X protein - woodchuck hepatitis virus (clone 8) ORGANISM #formal_name woodchuck hepatitis virus DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 12-Jun-1998 ACCESSIONS D32397 REFERENCE A94222 !$#authors Girones, R.; Cote, P.J.; Hornbuckle, W.E.; Tennant, B.C.; !1Gerin, J.L.; Purcell, R.H.; Miller, R.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:1846-1849 !$#title Complete nucleotide sequence of a molecular clone of !1woodchuck hepatitis virus that is infectious in the natural !1host. !$#cross-references MUID:89184524; PMID:2928306 !$#accession D32397 !'##molecule_type DNA !'##residues 1-141 ##label GIR !'##cross-references GB:J04514; NID:g336146 GENETICS !$#gene X CLASSIFICATION #superfamily hepatitis B virus gene X protein SUMMARY #length 141 #molecular-weight 15186 #checksum 2862 SEQUENCE /// ENTRY QQVL59 #type complete TITLE gene X protein - woodchuck hepatitis virus (clone 59) ORGANISM #formal_name woodchuck hepatitis virus DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jul-1999 ACCESSIONS E29969 REFERENCE A94368 !$#authors Cohen, J.I.; Miller, R.H.; Rosenblum, B.; Denniston, K.; !1Gerin, J.L.; Purcell, R.H. !$#journal Virology (1988) 162:12-20 !$#title Sequence comparison of woodchuck hepatitis virus replicative !1forms shows conservation of the genome. !$#cross-references MUID:88101359; PMID:3336938 !$#accession E29969 !'##molecule_type DNA !'##residues 1-141 ##label COH !'##cross-references GB:M19183; NID:g336141; PIDN:AAA46764.1; !1PID:g336144 GENETICS !$#gene X CLASSIFICATION #superfamily hepatitis B virus gene X protein SUMMARY #length 141 #molecular-weight 15271 #checksum 3473 SEQUENCE /// ENTRY QQVLS #type complete TITLE gene X protein - ground squirrel hepatitis virus ORGANISM #formal_name ground squirrel hepatitis virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS A03721 REFERENCE A93000 !$#authors Seeger, C.; Ganem, D.; Varmus, H.E. !$#journal J. Virol. (1984) 51:367-375 !$#title Nucleotide sequence of an infectious molecularly cloned !1genome of ground squirrel hepatitis virus. !$#cross-references MUID:84267998; PMID:6086950 !$#accession A03721 !'##molecule_type DNA !'##residues 1-138 ##label SEE !'##cross-references GB:K02715; NID:g325400; PIDN:AAA46758.1; !1PID:g325404 GENETICS !$#gene X CLASSIFICATION #superfamily hepatitis B virus gene X protein SUMMARY #length 138 #molecular-weight 15057 #checksum 6413 SEQUENCE /// ENTRY WMBECT #type complete TITLE major early 30K protein - human cytomegalovirus (strain Eisenhardt) ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS A26899 REFERENCE A26899 !$#authors Hutchinson, N.I.; Tocci, M.J. !$#journal Virology (1986) 155:172-182 !$#title Characterization of a major early gene from the human !1cytomegalovirus long inverted repeat; predicted amino acid !1sequence of a 30-kDa protein encoded by the 1.2-kb mRNA. !$#cross-references MUID:87044086; PMID:3022468 !$#accession A26899 !'##molecule_type mRNA !'##residues 1-254 ##label HUT !'##cross-references EMBL:M14789; NID:g330601; PIDN:AAA45978.1; !1PID:g330602 CLASSIFICATION #superfamily cytomegalovirus major early 30K protein KEYWORDS early protein SUMMARY #length 254 #molecular-weight 29692 #checksum 9183 SEQUENCE /// ENTRY WMBECX #type complete TITLE major early 30K protein - human cytomegalovirus (strain AD169) ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 #note host Homo sapiens (man) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jun-2000 ACCESSIONS S09756 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09756 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-82 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35455.1; !1PID:g59598 !'##note possible protein-coding frames are given !'##note the DNA sequence was submitted to EMBL, December 1989, in !1computer-readable form CLASSIFICATION #superfamily cytomegalovirus major early 30K protein KEYWORDS early protein SUMMARY #length 82 #molecular-weight 9717 #checksum 3953 SEQUENCE /// ENTRY EDBEIC #type complete TITLE immediate-early protein - human cytomegalovirus (strain Towne) ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 DATE 20-Sep-1984 #sequence_revision 20-Sep-1984 #text_change 16-Jul-1999 ACCESSIONS A03722; S34420 REFERENCE A03722 !$#authors Stenberg, R.M.; Thomsen, D.R.; Stinski, M.F. !$#journal J. Virol. (1984) 49:190-199 !$#title Structural analysis of the major immediate early gene of !1human cytomegalovirus. !$#cross-references MUID:84090395; PMID:6317889 !$#accession A03722 !'##molecule_type DNA !'##residues 1-491 ##label STE !'##note the authors translated the codons GAG, TCC, and CGT for !1residues 245, 313, and 392 as Gly, Cys, and Ala, !1respectively REFERENCE S34420 !$#authors Chapman, B.S.; Thayer, R.M.; Vincent, K.A.; Haigwood, N.L. !$#journal Nucleic Acids Res. (1991) 19:3979-3986 !$#title Effect of intron A from human cytomegalovirus (Towne) !1immediate-early gene on heterologous expression in mammalian !1cells. !$#cross-references MUID:91319560; PMID:1650459 !$#accession S34420 !'##status translation not shown !'##molecule_type DNA !'##residues 1-48 ##label CHA !'##cross-references EMBL:M60321; NID:g330624; PIDN:AAA45982.1; !1PID:g330625 GENETICS !$#introns 24/2 CLASSIFICATION #superfamily cytomegalovirus immediate-early protein SUMMARY #length 491 #molecular-weight 55178 #checksum 4380 SEQUENCE /// ENTRY EDBEM5 #type complete TITLE immediate-early protein - human cytomegalovirus (strain AD169) ALTERNATE_NAMES UL123 protein ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 #note host Homo sapiens (man) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jun-2000 ACCESSIONS S09890 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09890 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-491 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35325.1; !1PID:g1813973 !'##note possible protein-coding frames are given !'##note the DNA sequence was submitted to EMBL, December 1989, in !1computer-readable form GENETICS !$#introns 24/2; 86/1 CLASSIFICATION #superfamily cytomegalovirus immediate-early protein KEYWORDS immediate-early protein SUMMARY #length 491 #molecular-weight 55109 #checksum 4163 SEQUENCE /// ENTRY EDBEMT #type complete TITLE immediate-early protein IE2 - murine cytomegalovirus ORGANISM #formal_name murine cytomegalovirus, murine herpesvirus 1 DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jul-1999 ACCESSIONS A38470 REFERENCE A38470 !$#authors Messerle, M.; Keil, G.M.; Koszinowski, U.H. !$#journal J. Virol. (1991) 65:1638-1643 !$#title Structure and expression of murine cytomegalovirus !1immediate-early gene 2. !$#cross-references MUID:91140765; PMID:1847480 !$#accession A38470 !'##molecule_type DNA !'##residues 1-391 ##label MES !'##cross-references EMBL:M64230; NID:g330549; PIDN:AAA45949.1; !1PID:g330550 CLASSIFICATION #superfamily murine cytomegalovirus immediate-early protein !1IE2 KEYWORDS early protein SUMMARY #length 391 #molecular-weight 43801 #checksum 8276 SEQUENCE /// ENTRY EDBEMC #type complete TITLE immediate-early phosphoprotein pp89 - murine cytomegalovirus (strain Smith) ORGANISM #formal_name murine cytomegalovirus, murine herpesvirus 1 DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 07-Nov-1997 ACCESSIONS A27823 REFERENCE A27823 !$#authors Keil, G.M.; Ebeling-Keil, A.; Koszinowski, U.H. !$#journal J. Virol. (1987) 61:1901-1908 !$#title Sequence and structural organization of murine !1cytomegalovirus immediate-early gene 1. !$#cross-references MUID:87198940; PMID:3033321 !$#accession A27823 !'##molecule_type DNA !'##residues 1-595 ##label KEI !'##cross-references GB:L06816; NID:g330543 !'##experimental_source ATCC VR-194 GENETICS !$#gene ieI !$#introns 36/2; 100/1 CLASSIFICATION #superfamily murine cytomegalovirus immediate-early !1phosphoprotein pp89 KEYWORDS early protein; phosphoprotein SUMMARY #length 595 #molecular-weight 66708 #checksum 7489 SEQUENCE /// ENTRY EDBESM #type complete TITLE immediate-early protein IE3 - murine cytomegalovirus (strain Smith) ORGANISM #formal_name murine cytomegalovirus, murine herpesvirus 1 DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 08-Apr-1994 ACCESSIONS A40835 REFERENCE A40835 !$#authors Messerle, M.; Buehler, B.; Keil, G.M.; Koszinowski, U.H. !$#journal J. Virol. (1992) 66:27-36 !$#title Structural organization, expression, and functional !1characterization of the murine cytomegalovirus !1immediate-early gene 3. !$#cross-references MUID:92085392; PMID:1309246 !$#accession A40835 !'##molecule_type mRNA !'##residues 1-611 ##label MES !'##cross-references GB:M77846 CLASSIFICATION #superfamily murine cytomegalovirus immediate-early !1phosphoprotein pp89 KEYWORDS immediate-early protein SUMMARY #length 611 #molecular-weight 68102 #checksum 6339 SEQUENCE /// ENTRY EDBE17 #type complete TITLE immediate-early protein IE68 - human herpesvirus 1 ORGANISM #formal_name human herpesvirus 1 #note host Homo sapiens (man) DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 16-Jul-1999 ACCESSIONS A03723 REFERENCE A00656 !$#authors McGeoch, D.J.; Dolan, A.; Donald, S.; Rixon, F.J. !$#journal J. Mol. Biol. (1985) 181:1-13 !$#title Sequence determination and genetic content of the short !1unique region in the genome of herpes simplex virus type 1. !$#cross-references MUID:85160822; PMID:2984429 !$#accession A03723 !'##molecule_type DNA !'##residues 1-420 ##label MCG !'##cross-references GB:X02138; NID:g59865; PIDN:CAA26055.1; PID:g59866 !'##experimental_source strain 17 CLASSIFICATION #superfamily herpesvirus immediate-early protein IE68 KEYWORDS early protein SUMMARY #length 420 #molecular-weight 46524 #checksum 1664 SEQUENCE /// ENTRY EDBE63 #type complete TITLE immediate-early protein IE68 - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS B27345; I27345 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession B27345 !'##molecule_type DNA !'##residues 1-278 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27946.1; !1PID:g60052 GENETICS !$#gene 63; 70 CLASSIFICATION #superfamily herpesvirus immediate-early protein IE68 KEYWORDS early protein SUMMARY #length 278 #molecular-weight 30495 #checksum 6320 SEQUENCE /// ENTRY EDBEF7 #type complete TITLE immediate-early protein IE68 - equine herpesvirus 1 (strain Ab4p) ALTERNATE_NAMES in vitro host-range factor ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS B36802 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession B36802 !'##molecule_type DNA !'##residues 1-293 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02500.1; !1PID:g330856 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 65 CLASSIFICATION #superfamily herpesvirus immediate-early protein IE68 KEYWORDS early protein SUMMARY #length 293 #molecular-weight 32117 #checksum 5391 SEQUENCE /// ENTRY EDBE12 #type fragment TITLE immediate-early protein IE68 - equine herpesvirus 1 (subtype 2) (fragment) ORGANISM #formal_name equine herpesvirus 1 DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jun-2000 ACCESSIONS D28134 REFERENCE A28134 !$#authors Cullinane, A.A.; Rixon, F.J.; Davison, A.J. !$#journal J. Gen. Virol. (1988) 69:1575-1590 !$#title Characterization of the genome of equine herpesvirus 1 !1subtype 2. !$#cross-references MUID:88274328; PMID:2839595 !$#accession D28134 !'##molecule_type DNA !'##residues 1-273 ##label CUL !'##cross-references GB:D00318; NID:g221815; PIDN:BAA00221.1; !1PID:g221819 CLASSIFICATION #superfamily herpesvirus immediate-early protein IE68 KEYWORDS early protein SUMMARY #length 273 #checksum 6453 SEQUENCE /// ENTRY EDBESP #type complete TITLE immediate-early protein RSp40 - suid herpesvirus 1 (strain Ka) ORGANISM #formal_name suid herpesvirus 1 DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 08-Apr-1994 ACCESSIONS A36255 REFERENCE A36255 !$#authors Zhang, G.; Leader, D.P. !$#journal J. Gen. Virol. (1990) 71:2433-2441 !$#title The structure of the pseudorabies virus genome at the end of !1the inverted repeat sequences proximal to the junction with !1the short unique region. !$#cross-references MUID:91037977; PMID:2172457 !$#accession A36255 !'##molecule_type DNA !'##residues 1-364 ##label ZHA CLASSIFICATION #superfamily herpesvirus immediate-early protein IE68 KEYWORDS early protein SUMMARY #length 364 #molecular-weight 39613 #checksum 3864 SEQUENCE /// ENTRY EDBEQ3 #type complete TITLE immediate-early protein - saimiriine herpesvirus 1 (strain 11) ORGANISM #formal_name saimiriine herpesvirus 1 #note host Saimiri sciureus (common squirrel monkey) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS G36813; S20244 REFERENCE A36806 !$#authors Albrecht, J. !$#submission submitted to the EMBL Data Library, January 1992 !$#description Primary structure of the herpesvirus saimiri genome. !$#accession G36813 !'##molecule_type DNA !'##residues 1-407 ##label ALB !'##cross-references GB:X64346; NID:g60320; PIDN:CAA45696.1; PID:g60394 REFERENCE A37309 !$#authors Albrecht, J.C.; Nicholas, J.; Biller, D.; Cameron, K.R.; !1Biesinger, B.; Newman, C.; Wittmann, S.; Craxton, M.A.; !1Coleman, H.; Fleckenstein, B.; Honess, R.W. !$#journal J. Virol. (1992) 66:5047-5058 !$#title Primary structure of the herpesvirus saimiri genome. !$#cross-references MUID:92333688; PMID:1321287 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given REFERENCE S20243 !$#authors Nicholas, J.; Cameron, K.R.; Honess, R.W. !$#journal Nature (1992) 355:362-365 !$#title Herpesvirus saimiri encodes homologues of G protein-coupled !1receptors and cyclins. !$#cross-references MUID:92115001; PMID:1309943 !$#accession S20244 !'##status preliminary !'##molecule_type DNA !'##residues 1-407 ##label NIC !'##cross-references GB:S76368; NID:g243351; PIDN:AAB21116.1; !1PID:g243353 GENETICS !$#gene 73 CLASSIFICATION #superfamily herpesvirus immediate-early protein IE68 KEYWORDS early protein SUMMARY #length 407 #molecular-weight 46617 #checksum 2367 SEQUENCE /// ENTRY A45351 #type complete TITLE immediate-early protein 1 - saimiriine herpesvirus 1 (strain 11) ORGANISM #formal_name saimiriine herpesvirus 1 #note host Saimiri sciureus (common squirrel monkey) DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jul-1999 ACCESSIONS A45351; E36807 REFERENCE A45351 !$#authors Nicholas, J.; Smith, E.P.; Coles, L.; Honess, R. !$#journal Virology (1990) 179:189-200 !$#title Gene expression in cells infected with gammaherpesvirus !1saimiri: properties of transcripts from two immediate-early !1genes. !$#cross-references MUID:91021021; PMID:1699352 !$#accession A45351 !'##molecule_type mRNA !'##residues 1-249 ##label NIC !'##cross-references GB:M60286; NID:g331040; PIDN:AAA46155.1; !1PID:g331041 REFERENCE A36806 !$#authors Albrecht, J. !$#submission submitted to the EMBL Data Library, January 1992 !$#description Primary structure of the herpesvirus saimiri genome. !$#accession E36807 !'##molecule_type DNA !'##residues 1-249 ##label ALB !'##cross-references GB:X64346; NID:g60320; PIDN:CAA45637.1; PID:g60335 REFERENCE A37309 !$#authors Albrecht, J.C.; Nicholas, J.; Biller, D.; Cameron, K.R.; !1Biesinger, B.; Newman, C.; Wittmann, S.; Craxton, M.A.; !1Coleman, H.; Fleckenstein, B.; Honess, R.W. !$#journal J. Virol. (1992) 66:5047-5058 !$#title Primary structure of the herpesvirus saimiri genome. !$#cross-references MUID:92333688; PMID:1321287 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given CLASSIFICATION #superfamily saimiri herpesvirus immediate-early protein 1 KEYWORDS early protein SUMMARY #length 249 #molecular-weight 28273 #checksum 8308 SEQUENCE /// ENTRY B45351 #type complete TITLE immediate-early protein 2 - saimiriine herpesvirus 1 (strain 11) ALTERNATE_NAMES hypothetical protein ORF13 ORGANISM #formal_name saimiriine herpesvirus 1 #note host Saimiri sciureus (common squirrel monkey) DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jul-1999 ACCESSIONS B45351; D36807 REFERENCE A45351 !$#authors Nicholas, J.; Smith, E.P.; Coles, L.; Honess, R. !$#journal Virology (1990) 179:189-200 !$#title Gene expression in cells infected with gammaherpesvirus !1saimiri: properties of transcripts from two immediate-early !1genes. !$#cross-references MUID:91021021; PMID:1699352 !$#accession B45351 !'##molecule_type mRNA !'##residues 1-151 ##label NIC !'##cross-references GB:M60286; NID:g331040; PIDN:AAA46156.1; !1PID:g331042 REFERENCE A36806 !$#authors Albrecht, J. !$#submission submitted to the EMBL Data Library, January 1992 !$#description Primary structure of the herpesvirus saimiri genome. !$#accession D36807 !'##molecule_type DNA !'##residues 1-151 ##label ALB !'##cross-references GB:X64346; NID:g60320; PIDN:CAA45636.1; PID:g60334 REFERENCE A37309 !$#authors Albrecht, J.C.; Nicholas, J.; Biller, D.; Cameron, K.R.; !1Biesinger, B.; Newman, C.; Wittmann, S.; Craxton, M.A.; !1Coleman, H.; Fleckenstein, B.; Honess, R.W. !$#journal J. Virol. (1992) 66:5047-5058 !$#title Primary structure of the herpesvirus saimiri genome. !$#cross-references MUID:92333688; PMID:1321287 !$#contents annotation; protein-coding frames !$#note neither protein nor nucleotide sequence is given GENETICS !$#gene 13 CLASSIFICATION #superfamily saimiri herpesvirus immediate-early protein 2 KEYWORDS early protein SUMMARY #length 151 #molecular-weight 17180 #checksum 2395 SEQUENCE /// ENTRY EDBE51 #type complete TITLE immediate-early-5 protein - human herpesvirus 1 ORGANISM #formal_name human herpesvirus 1 DATE 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 16-Jul-1999 ACCESSIONS A93454; A92789; A03724 REFERENCE A93454 !$#authors Watson, R.J.; Vande Woude, G.F. !$#journal Nucleic Acids Res. (1982) 10:979-991 !$#title DNA sequence of an immediate-early gene (IE mRNA-5) of !1herpes simplex virus type I. !$#cross-references MUID:82150256; PMID:6278443 !$#accession A93454 !'##molecule_type DNA !'##residues 1-88 ##label WAT !'##cross-references GB:J02220; GB:J02219; NID:g330126; PIDN:AAA45795.1; !1PID:g330127 REFERENCE A92789 !$#authors Murchie, M.J.; McGeoch, D.J. !$#journal J. Gen. Virol. (1982) 62:1-15 !$#title DNA sequence analysis of an immediate-early gene region of !1the herpes simplex virus type 1 genome (map coordinates !10.950 to 0.978). !$#cross-references MUID:83032477; PMID:6290591 !$#accession A92789 !'##molecule_type DNA !'##residues 1-13,'T',15-88 ##label MUR !'##cross-references GB:L00036; GB:L00037; GB:M12354; GB:M12355; !1GB:M12506; GB:M30738; GB:X00428; NID:g291490; !1PIDN:AAA96676.1; PID:g291492 GENETICS !$#map_position 0.938-0.964 CLASSIFICATION #superfamily herpesvirus immediate-early protein KEYWORDS early protein SUMMARY #length 88 #molecular-weight 9806 #checksum 4775 SEQUENCE /// ENTRY EDBE75 #type complete TITLE immediate-early protein IE175 - human herpesvirus 1 ORGANISM #formal_name human herpesvirus 1 DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jun-2000 ACCESSIONS A23510 REFERENCE A23510 !$#authors McGeoch, D.J.; Dolan, A.; Donald, S.; Brauer, D.H.K. !$#journal Nucleic Acids Res. (1986) 14:1727-1745 !$#title Complete DNA sequence of the short repeat region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:86148504; PMID:3005980 !$#accession A23510 !'##molecule_type DNA !'##residues 1-1298 ##label MCG !'##cross-references GB:X14112; GB:D00317; GB:D00374; GB:S40593; !1NID:g1944536; PIDN:CAA32286.1; PID:g59558 COMMENT This protein acts at the transcriptional regulatory level !1and is required throughout the infectious cycle. GENETICS !$#gene IE3 !$#map_position short repeat region (IR-s) CLASSIFICATION #superfamily herpesvirus immediate-early protein IE175 KEYWORDS DNA binding; early protein; transcription regulation SUMMARY #length 1298 #molecular-weight 132842 #checksum 2820 SEQUENCE /// ENTRY EDBEE1 #type complete TITLE immediate-early protein - equine herpesvirus 1 ORGANISM #formal_name equine herpesvirus 1 DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jul-1999 ACCESSIONS A33764 REFERENCE A33764 !$#authors Grundy, F.J.; Baumann, R.P.; O'Callaghan, D.J. !$#journal Virology (1989) 172:223-236 !$#title DNA sequence and comparative analyses of the equine !1herpesvirus type 1 immediate early gene. !$#cross-references MUID:89370304; PMID:2549711 !$#accession A33764 !'##molecule_type DNA !'##residues 1-1487 ##label GRU !'##cross-references GB:J04366; NID:g330910; PIDN:AAA46089.1; !1PID:g330911 CLASSIFICATION #superfamily herpesvirus immediate-early protein IE175 KEYWORDS DNA binding; early protein; transcription regulation SUMMARY #length 1487 #molecular-weight 154715 #checksum 1918 SEQUENCE /// ENTRY EDBEF6 #type complete TITLE 155K transcription activator - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS A36802 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession A36802 !'##molecule_type DNA !'##residues 1-1487 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02499.1; !1PID:g330855 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 64 CLASSIFICATION #superfamily herpesvirus immediate-early protein IE175 KEYWORDS DNA binding; early protein; transcription regulation SUMMARY #length 1487 #molecular-weight 154867 #checksum 2748 SEQUENCE /// ENTRY EDBEIF #type complete TITLE immediate-early protein IE180 - suid herpesvirus 1 (strain Indiana-Funkhauser) ORGANISM #formal_name suid herpesvirus 1 DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Feb-1997 ACCESSIONS S04713 REFERENCE S04713 !$#authors Cheung, A.K. !$#journal Nucleic Acids Res. (1989) 17:4637-4646 !$#title DNA nucleotide sequence analysis of the immediate-early gene !1of pseudorabies virus. !$#cross-references MUID:89315207; PMID:2546124 !$#accession S04713 !'##molecule_type DNA !'##residues 1-1460 ##label CHE CLASSIFICATION #superfamily herpesvirus immediate-early protein IE175 KEYWORDS DNA binding; early protein; transcription regulation SUMMARY #length 1460 #molecular-weight 152851 #checksum 5209 SEQUENCE /// ENTRY A45344 #type complete TITLE immediate-early protein - suid herpesvirus 1 (strain Kaplan) ORGANISM #formal_name suid herpesvirus 1 DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jul-1999 ACCESSIONS A45344 REFERENCE A45344 !$#authors Vlcek, C.; Kozmik, Z.; Paces, V.; Schirm, S.; Schwyzer, M. !$#journal Virology (1990) 179:365-377 !$#title Pseudorabies virus immediate-early gene overlaps with an !1oppositely oriented open reading frame: characterization of !1their promoter and enhancer regions. !$#cross-references MUID:91021039; PMID:2171211 !$#accession A45344 !'##status translation not shown !'##molecule_type DNA !'##residues 1-1446 ##label VLC !'##cross-references GB:M34651; NID:g334070; PIDN:AAA47470.1; !1PID:g334071 CLASSIFICATION #superfamily herpesvirus immediate-early protein IE175 KEYWORDS DNA binding; early protein; transcription regulation SUMMARY #length 1446 #molecular-weight 148639 #checksum 6195 SEQUENCE /// ENTRY EDBEGA #type complete TITLE immediate-early protein IE175 - Marek's disease virus (strain GA) ALTERNATE_NAMES infected cell protein 4 ORGANISM #formal_name Marek's disease virus DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS A42991 REFERENCE A42991 !$#authors Anderson, A.S.; Francesconi, A.; Morgan, R.W. !$#journal Virology (1992) 189:657-667 !$#title Complete nucleotide sequence of the Marek's disease virus !1ICP4 gene. !$#cross-references MUID:92351564; PMID:1322594 !$#accession A42991 !'##molecule_type DNA !'##residues 1-1415 ##label AND !'##cross-references GB:M75729; NID:g330950; PIDN:AAA46111.1; !1PID:g330951 CLASSIFICATION #superfamily herpesvirus immediate-early protein IE175 KEYWORDS DNA binding; early protein; transcription regulation SUMMARY #length 1415 #molecular-weight 154935 #checksum 3228 SEQUENCE /// ENTRY EDBE11 #type complete TITLE immediate-early protein IE110 - human herpesvirus 1 (strain 17) ORGANISM #formal_name human herpesvirus 1 DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 17-Mar-2000 ACCESSIONS A29152 REFERENCE A29152 !$#authors Perry, L.J.; Rixon, F.J.; Everett, R.D.; Frame, M.C.; !1McGeoch, D.J. !$#journal J. Gen. Virol. (1986) 67:2365-2380 !$#title Characterization of the IE110 gene of herpes simplex virus !1type 1. !$#cross-references MUID:87059760; PMID:3023529 !$#accession A29152 !'##molecule_type DNA !'##residues 1-775 ##label PER !'##cross-references GB:X04614; NID:g59832; PIDN:CAA28285.1; PID:g59833 GENETICS !$#introns 19/3; 242/1 CLASSIFICATION #superfamily herpesvirus immediate-early protein IE110; RING !1finger homology KEYWORDS DNA binding; early protein; transcription regulation; zinc !1finger FEATURE !$112-162 #domain RING finger homology #label RNG\ !$116-156 #region zinc finger C3HC4 motif SUMMARY #length 775 #molecular-weight 78456 #checksum 7216 SEQUENCE /// ENTRY EDBEXD #type complete TITLE immediate-early protein RL2 - human herpesvirus 2 (strain HG52) ALTERNATE_NAMES RL2 protein ORGANISM #formal_name human herpesvirus 2 #note host Homo sapiens (man) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-Jan-2001 ACCESSIONS JQ1501 REFERENCE JQ1494 !$#authors McGeoch, D.J.; Cunningham, C.; McIntyre, G.; Dolan, A. !$#journal J. Gen. Virol. (1991) 72:3057-3075 !$#title Comparative sequence analysis of the long repeat regions and !1adjoining parts of the long unique regions in the genomes of !1herpes simplex viruses types 1 and 2. !$#cross-references MUID:92113549; PMID:1662697 !$#accession JQ1501 !'##molecule_type DNA !'##residues 1-825 ##label MCG !'##cross-references GB:D10471; DDBJ:D01128; NID:g221784; !1PIDN:BAA23427.1; PID:g2626942 GENETICS !$#gene RL2 !$#introns 25/3; 252/1 CLASSIFICATION #superfamily herpesvirus immediate-early protein IE110; RING !1finger homology KEYWORDS DNA binding; immediate-early protein; tandem repeat; !1transcription regulation; zinc finger FEATURE !$122-172 #domain RING finger homology #label RNG\ !$126-166 #region zinc finger C3HC4 motif\ !$589-623 #region 5-residue repeats (A-S-S-S-S) SUMMARY #length 825 #molecular-weight 81985 #checksum 1516 SEQUENCE /// ENTRY EDBE22 #type complete TITLE immediate-early protein IER2.9 - bovine herpesvirus 1 (strain K22) ALTERNATE_NAMES early protein ER2.6; p135 protein ORGANISM #formal_name bovine herpesvirus 1 DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 17-Mar-2000 ACCESSIONS A38209 REFERENCE A38209 !$#authors Wirth, U.V.; Fraefel, C.; Vogt, B.; Vlcek, C.; Paces, V.; !1Schwyzer, M. !$#journal J. Virol. (1992) 66:2763-2772 !$#title Immediate-early RNA 2.9 and early RNA 2.6 of bovine !1herpesvirus 1 are 3' coterminal and encode a putative zinc !1finger transactivator protein. !$#cross-references MUID:92219360; PMID:1313901 !$#accession A38209 !'##molecule_type DNA !'##residues 1-676 ##label WIR !'##cross-references GB:M84464; NID:g330767; PIDN:AAA46061.1; !1PID:g330768 CLASSIFICATION #superfamily herpesvirus immediate-early protein IE110; RING !1finger homology KEYWORDS DNA binding; immediate-early protein; transcription !1regulation; zinc finger FEATURE !$9-57 #domain RING finger homology #label RNG\ !$13-51 #region zinc finger C3HC4 motif\ !$284-331 #region acidic SUMMARY #length 676 #molecular-weight 67700 #checksum 6854 SEQUENCE /// ENTRY EDBE23 #type complete TITLE immediate-early protein IER2.9 - bovine herpesvirus 1 (strain Jura) ALTERNATE_NAMES early protein ER2.6; p135 protein ORGANISM #formal_name bovine herpesvirus 1 DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 17-Mar-2000 ACCESSIONS B38209 REFERENCE A38209 !$#authors Wirth, U.V.; Fraefel, C.; Vogt, B.; Vlcek, C.; Paces, V.; !1Schwyzer, M. !$#journal J. Virol. (1992) 66:2763-2772 !$#title Immediate-early RNA 2.9 and early RNA 2.6 of bovine !1herpesvirus 1 are 3' coterminal and encode a putative zinc !1finger transactivator protein. !$#cross-references MUID:92219360; PMID:1313901 !$#accession B38209 !'##molecule_type DNA !'##residues 1-676 ##label WIR !'##cross-references GB:M84465; NID:g330769; PIDN:AAA46062.1; !1PID:g330770 CLASSIFICATION #superfamily herpesvirus immediate-early protein IE110; RING !1finger homology KEYWORDS DNA binding; immediate-early protein; transcription !1regulation; zinc finger FEATURE !$9-57 #domain RING finger homology #label RNG\ !$13-51 #region zinc finger C3HC4 motif\ !$284-331 #region acidic SUMMARY #length 676 #molecular-weight 67878 #checksum 8700 SEQUENCE /// ENTRY EDBED9 #type complete TITLE immediate-early protein IE1 - bovine herpesvirus 4 (strain DN-599) ORGANISM #formal_name bovine herpesvirus 4 DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS A40504 REFERENCE A40504 !$#authors van Santen, V.L. !$#journal J. Virol. (1991) 65:5211-5224 !$#title Characterization of the bovine herpesvirus 4 major !1immediate-early transcript. !$#cross-references MUID:91374570; PMID:1716688 !$#accession A40504 !'##molecule_type mRNA !'##residues 1-285 ##label VAN !'##cross-references GB:M60043; NID:g330758; PIDN:AAA96266.1; !1PID:g330759 CLASSIFICATION #superfamily bovine herpesvirus 4 immediate-early protein !1IE1 KEYWORDS DNA binding; immediate-early protein; transcription !1regulation SUMMARY #length 285 #molecular-weight 32692 #checksum 1240 SEQUENCE /// ENTRY EDBEM4 #type complete TITLE 45K immediate-early-2 protein - human cytomegalovirus (strain AD169) ALTERNATE_NAMES UL122 protein ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 #note host Homo sapiens (man) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jun-2000 ACCESSIONS S09889 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09889 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-411 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35324.1; !1PID:g1813972 !'##note possible protein-coding frames are given !'##note the DNA sequence was submitted to EMBL, December 1989, in !1computer-readable form CLASSIFICATION #superfamily cytomegalovirus immediate-early-2 protein KEYWORDS DNA binding; immediate-early protein; transcription !1regulation SUMMARY #length 411 #molecular-weight 44831 #checksum 9295 SEQUENCE /// ENTRY EDBE4T #type complete TITLE 45K immediate-early-2 protein - human cytomegalovirus (strain Towne) CONTAINS 27K immediate-early-2 protein; amino end of minor immediate-early-2 protein ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS A33347; A03726 REFERENCE A33347 !$#authors Stenberg, R.M.; Depto, A.S.; Fortney, J.; Nelson, J.A. !$#journal J. Virol. (1989) 63:2699-2708 !$#title Regulated expression of early and late RNAs and proteins !1from the human cytomegalovirus immediate-early gene region. !$#cross-references MUID:89259051; PMID:2542583 !$#accession A33347 !'##molecule_type DNA !'##residues 1-410 ##label STE !'##cross-references GB:M26973; NID:g341563; PIDN:AAA57208.1; !1PID:g602309 REFERENCE A03725 !$#authors Stenberg, R.M.; Witte, P.R.; Stinski, M.F. !$#journal J. Virol. (1985) 56:665-675 !$#title Multiple spliced and unspliced transcripts from human !1cytomegalovirus immediate-early region 2 and evidence for a !1common initiation site within immediate-early region 1. !$#cross-references MUID:86062894; PMID:2999423 !$#accession A03726 !'##molecule_type DNA !'##residues 1-195,351-410 ##label STE2 !'##cross-references GB:M11298; NID:g330552; PIDN:AAA45950.1; !1PID:g330553 CLASSIFICATION #superfamily cytomegalovirus immediate-early-2 protein KEYWORDS alternative splicing; DNA binding; immediate-early protein; !1transcription regulation FEATURE !$1-195,351-410 #product 27K immediate-early-2 protein #status !8predicted #label IMM\ !$1-195,351-409 #product minor immediate-early-2 protein (fragment) !8#status predicted #label IMN SUMMARY #length 410 #molecular-weight 44773 #checksum 8155 SEQUENCE /// ENTRY EDBE3T #type complete TITLE 30K immediate-early-2 protein - human cytomegalovirus (strain Towne) ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 16-Jul-1999 ACCESSIONS A03725 REFERENCE A03725 !$#authors Stenberg, R.M.; Witte, P.R.; Stinski, M.F. !$#journal J. Virol. (1985) 56:665-675 !$#title Multiple spliced and unspliced transcripts from human !1cytomegalovirus immediate-early region 2 and evidence for a !1common initiation site within immediate-early region 1. !$#cross-references MUID:86062894; PMID:2999423 !$#accession A03725 !'##molecule_type DNA !'##residues 1-280 ##label STE !'##cross-references GB:M11298; NID:g330552; PIDN:AAA45952.1; !1PID:g330555 CLASSIFICATION #superfamily cytomegalovirus immediate-early-2 protein KEYWORDS alternative splicing; immediate-early protein SUMMARY #length 280 #molecular-weight 30329 #checksum 3972 SEQUENCE /// ENTRY WMBE65 #type complete TITLE 65K lower matrix phosphoprotein - human cytomegalovirus (strain AD169) ALTERNATE_NAMES protein UL83 ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 16-Jul-1999 ACCESSIONS A26793; S09847 REFERENCE A93028 !$#authors Rueger, B.; Klages, S.; Walla, B.; Albrecht, J.; !1Fleckenstein, B.; Tomlinson, P.; Barrell, B. !$#journal J. Virol. (1987) 61:446-453 !$#title Primary structure and transcription of the genes coding for !1the two virion phosphoproteins pp65 and pp71 of human !1cytomegalovirus. !$#cross-references MUID:87112940; PMID:3027374 !$#accession A26793 !'##molecule_type DNA !'##residues 1-561 ##label RUE !'##cross-references GB:M15120 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09847 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-561 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35357.1; !1PID:g1780861 !'##note this sequence was submitted to the EMBL Data Library, December !11989 GENETICS !$#introns 93/3 CLASSIFICATION #superfamily cytomegalovirus lower matrix phosphoprotein KEYWORDS matrix protein; phosphoprotein SUMMARY #length 561 #molecular-weight 62898 #checksum 7914 SEQUENCE /// ENTRY WMBETW #type complete TITLE 65K lower matrix phosphoprotein - human cytomegalovirus (strain Towne) ALTERNATE_NAMES 65K tegument protein ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 #note host Homo sapiens (man) DATE 31-Mar-1992 #sequence_revision 17-Feb-1994 #text_change 17-Feb-1994 ACCESSIONS A46342; A39149 REFERENCE A46342 !$#authors Pande, H.; Lee, T.D.; Churchill, M.A.; Zaia, J.A. !$#journal Virology (1990) 178:6-14 !$#title Structural analysis of a 64-kDa major structural protein of !1human cytomegalovirus (Towne): identification of a !1phosphorylation site and comparison to pp65 of HCMV (AD169). !$#cross-references MUID:90357792; PMID:2167561 !$#accession A46342 !'##molecule_type protein !'##residues 1-561 ##label PA1 REFERENCE A39149 !$#authors Pande, H.; Campo, K.; Tanamachi, B.; Zaia, J.A. !$#journal Virology (1991) 182:220-228 !$#title Human cytomegalovirus strain Towne pp65 gene: nucleotide !1sequence and expression in Escherichia coli. !$#cross-references MUID:91220654; PMID:1850902 !$#accession A39149 !'##molecule_type DNA !'##residues 11-561 ##label PA2 !'##cross-references GB:M67443 !'##note the authors translated the codon AAT for residue 478 as Asp CLASSIFICATION #superfamily cytomegalovirus lower matrix phosphoprotein KEYWORDS matrix protein; phosphoprotein SUMMARY #length 561 #molecular-weight 62972 #checksum 6987 SEQUENCE /// ENTRY WMBETE #type complete TITLE 65K early nonstructural protein - human cytomegalovirus (strain Towne) ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 #note host Homo sapiens (man) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS A41808 REFERENCE A41808 !$#authors He, Y.S.; Xu, L.; Huang, E.S. !$#journal J. Virol. (1992) 66:1098-1108 !$#title Characterization of human cytomegalovirus UL84 early gene !1and identification of its putative protein product. !$#cross-references MUID:92114132; PMID:1309892 !$#accession A41808 !'##molecule_type mRNA !'##residues 1-587 ##label HEY !'##cross-references GB:M81432; NID:g330541; PIDN:AAA45947.1; !1PID:g330542 CLASSIFICATION #superfamily human cytomegalovirus 65K early nonstructural !1protein KEYWORDS leucine zipper; nonstructural protein FEATURE !$114-135 #region leucine zipper motif\ !$325-373 #region leucine zipper motif SUMMARY #length 587 #molecular-weight 65387 #checksum 6601 SEQUENCE /// ENTRY WMBEDE #type complete TITLE 65K early nonstructural protein - human cytomegalovirus (strain AD169) ALTERNATE_NAMES UL84 protein ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 #note host Homo sapiens (man) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS S09848 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09848 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-586 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35358.1; !1PID:g1780862 !'##note this sequence was submitted to the EMBL Data Library, December !11989 CLASSIFICATION #superfamily human cytomegalovirus 65K early nonstructural !1protein KEYWORDS leucine zipper; nonstructural protein FEATURE !$114-135 #region leucine zipper motif\ !$324-372 #region leucine zipper motif SUMMARY #length 586 #molecular-weight 65428 #checksum 7604 SEQUENCE /// ENTRY WMBES1 #type complete TITLE 71K upper matrix phosphoprotein - human cytomegalovirus (strain AD169) ALTERNATE_NAMES protein UL82 ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 16-Jul-1999 ACCESSIONS B26793; S09846 REFERENCE A93028 !$#authors Rueger, B.; Klages, S.; Walla, B.; Albrecht, J.; !1Fleckenstein, B.; Tomlinson, P.; Barrell, B. !$#journal J. Virol. (1987) 61:446-453 !$#title Primary structure and transcription of the genes coding for !1the two virion phosphoproteins pp65 and pp71 of human !1cytomegalovirus. !$#cross-references MUID:87112940; PMID:3027374 !$#accession B26793 !'##molecule_type DNA !'##residues 1-559 ##label RUE !'##cross-references GB:M15120; NID:g330650; PIDN:AAA45997.1; !1PID:g330652 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09846 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-559 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35356.1; !1PID:g1780860 !'##note this sequence was submitted to the EMBL Data Library, December !11989 CLASSIFICATION #superfamily cytomegalovirus upper matrix phosphoprotein KEYWORDS matrix protein; phosphoprotein SUMMARY #length 559 #molecular-weight 61948 #checksum 9730 SEQUENCE /// ENTRY VGBE48 #type complete TITLE early glycoprotein gp48 precursor - human cytomegalovirus (strain Towne) ALTERNATE_NAMES early glycoprotein UL4 ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 #note host Homo sapiens (man) DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jul-1999 ACCESSIONS A32390 REFERENCE A32390 !$#authors Chang, C.P.; Vesole, D.H.; Nelson, J.; Oldstone, M.B.A.; !1Stinski, M.F. !$#journal J. Virol. (1989) 63:3330-3337 !$#title Identification and expression of a human cytomegalovirus !1early glycoprotein. !$#cross-references MUID:89311622; PMID:2545908 !$#accession A32390 !'##molecule_type DNA !'##residues 1-148 ##label CHA !'##cross-references GB:M28127; NID:g330512; PIDN:AAA45937.1; !1PID:g330513 CLASSIFICATION #superfamily cytomegalovirus early glycoprotein gp48 KEYWORDS early protein; glycoprotein FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-148 #product early glycoprotein gp48 #status predicted !8#label MAT\ !$22,44,49,57,65,104, !$108,118,135,144 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 148 #molecular-weight 17151 #checksum 5389 SEQUENCE /// ENTRY VGBEY9 #type complete TITLE early glycoprotein gp48 precursor - human cytomegalovirus (strain AD169) ALTERNATE_NAMES early glycoprotein UL4 ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 #note host Homo sapiens (man) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS S09767 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09767 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-152 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35437.1; !1PID:g59609 !'##note possible protein-coding frames are given !'##note the DNA sequence was submitted to the EMBL Data Library, !1December 1989, in computer-readable form CLASSIFICATION #superfamily cytomegalovirus early glycoprotein gp48 KEYWORDS early protein; glycoprotein FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-152 #product early glycoprotein gp48 #status predicted !8#label MAT\ !$48,53,61,69,108, !$112,122,139,148 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 152 #molecular-weight 17750 #checksum 4564 SEQUENCE /// ENTRY QQBEC1 #type complete TITLE HKLF1 protein - human cytomegalovirus (strain AD169) ALTERNATE_NAMES hypothetical protein TRL1 ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 28-Jul-2000 ACCESSIONS A26078; S09750 REFERENCE A92935 !$#authors Weston, K.; Barrell, B.G. !$#journal J. Mol. Biol. (1986) 192:177-208 !$#title Sequence of the short unique region, short repeats, and part !1of the long repeats of human cytomegalovirus. !$#cross-references MUID:87169717; PMID:3031311 !$#accession A26078 !'##molecule_type DNA !'##residues 1-311 ##label WES !'##cross-references EMBL:X04650; NID:g59801; PIDN:CAB37093.1; !1PID:g4456174 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09750 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-311 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35449.1; !1PID:g59592 !'##note this sequence was submitted to the EMBL Data Library, December !11989 GENETICS !$#gene HKLF1 CLASSIFICATION #superfamily cytomegalovirus HKLF1 protein SUMMARY #length 311 #molecular-weight 34821 #checksum 263 SEQUENCE /// ENTRY QQBES6 #type complete TITLE UL20 protein precursor - human cytomegalovirus (strain AD169) ALTERNATE_NAMES T cell receptor gamma chain homolog HCMVUL20 ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 #note host Homo sapiens (man) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS S09783; A57006 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09783 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-340 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35419.1; !1PID:g59625 !'##note possible protein-coding frames are given !'##note the DNA sequence was submitted to EMBL, December 1989, in !1computer-readable form REFERENCE A57006 !$#authors Beck, S.; Barrell, B. !$#journal DNA Seq. (1991) 2:33-38 !$#title An HCMV reading frame which has similarity with both the V !1and C regions of the TCR gamma chain. !$#cross-references MUID:92199241; PMID:1666312 !$#accession A57006 !'##molecule_type DNA !'##residues 1-340 ##label BEC !'##cross-references GB:X17403; NID:g59591; PIDN:CAA35419.1; PID:g59625 !'##note sequence extracted from NCBI backbone (NCBIN:89332, !1NCBIP:89335) CLASSIFICATION #superfamily cytomegalovirus UL20 protein KEYWORDS transmembrane protein FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-340 #product hypothetical UL20 protein #status predicted !8#label MAT\ !$218-249 #domain transmembrane #status predicted #label TMM SUMMARY #length 340 #molecular-weight 38701 #checksum 7883 SEQUENCE /// ENTRY QQBET2 #type complete TITLE UL25 protein - human cytomegalovirus (strain AD169) ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 #note host Homo sapiens (man) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS S09788 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09788 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-656 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35424.1; !1PID:g59630 !'##note possible protein-coding frames are given !'##note the DNA sequence was submitted to EMBL, December 1989, in !1computer-readable form CLASSIFICATION #superfamily cytomegalovirus UL25 protein SUMMARY #length 656 #molecular-weight 73539 #checksum 7985 SEQUENCE /// ENTRY QQBEC2 #type complete TITLE HKRFX protein - human cytomegalovirus (strain AD169) ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 28-Jul-2000 ACCESSIONS B26078 REFERENCE A92935 !$#authors Weston, K.; Barrell, B.G. !$#journal J. Mol. Biol. (1986) 192:177-208 !$#title Sequence of the short unique region, short repeats, and part !1of the long repeats of human cytomegalovirus. !$#cross-references MUID:87169717; PMID:3031311 !$#accession B26078 !'##molecule_type DNA !'##residues 1-277 ##label WES !'##cross-references EMBL:X04650; NID:g59801; PIDN:CAB37094.1; !1PID:g4456175 GENETICS !$#gene HKRFX CLASSIFICATION #superfamily cytomegalovirus HKRFX protein SUMMARY #length 277 #molecular-weight 29115 #checksum 4671 SEQUENCE /// ENTRY QQBEU2 #type complete TITLE UL35 protein - human cytomegalovirus (strain AD169) ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 #note host Homo sapiens (man) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS S09798 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09798 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-640 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35394.1; !1PID:g59640 !'##note possible protein-coding frames are given !'##note the DNA sequence was submitted to EMBL, December 1989, in !1computer-readable form CLASSIFICATION #superfamily cytomegalovirus UL35 protein SUMMARY #length 640 #molecular-weight 72528 #checksum 3703 SEQUENCE /// ENTRY QQBEC3 #type complete TITLE HQRF1 protein - human cytomegalovirus (strain AD169) ALTERNATE_NAMES hypothetical protein IRS1 ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS C26078; S09914 REFERENCE A92935 !$#authors Weston, K.; Barrell, B.G. !$#journal J. Mol. Biol. (1986) 192:177-208 !$#title Sequence of the short unique region, short repeats, and part !1of the long repeats of human cytomegalovirus. !$#cross-references MUID:87169717; PMID:3031311 !$#accession C26078 !'##molecule_type DNA !'##residues 1-846 ##label WES !'##cross-references EMBL:X04650; NID:g59801; PIDN:CAA28312.1; !1PID:g59803 !'##experimental_source strain AD169 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09914 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-846 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35311.1; !1PID:g1780931 !'##experimental_source strain AD169 !'##note this sequence was submitted to the EMBL Data Library, December !11989 GENETICS !$#gene HQRF1 CLASSIFICATION #superfamily cytomegalovirus HQRF1 protein SUMMARY #length 846 #molecular-weight 91047 #checksum 2604 SEQUENCE /// ENTRY QQBEE3 #type complete TITLE HHLF1 protein - human cytomegalovirus (strain AD169) ALTERNATE_NAMES hypothetical protein TRS1 ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 28-Jul-2000 ACCESSIONS C27349; S09951 REFERENCE A92935 !$#authors Weston, K.; Barrell, B.G. !$#journal J. Mol. Biol. (1986) 192:177-208 !$#title Sequence of the short unique region, short repeats, and part !1of the long repeats of human cytomegalovirus. !$#cross-references MUID:87169717; PMID:3031311 !$#accession C27349 !'##molecule_type DNA !'##residues 1-788 ##label WES !'##cross-references EMBL:X04650; NID:g59801; PIDN:CAB37121.1; !1PID:g4456203 !'##experimental_source strain AD169 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09951 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-788 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35269.1; !1PID:g1780968 !'##experimental_source strain AD169 !'##note this sequence was submitted to the EMBL Data Library, December !11989 GENETICS !$#gene HHLF1 CLASSIFICATION #superfamily cytomegalovirus HQRF1 protein SUMMARY #length 788 #molecular-weight 83981 #checksum 7858 SEQUENCE /// ENTRY QQBEU5 #type complete TITLE UL37 protein precursor - human cytomegalovirus (strain AD169) ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 #note host Homo sapiens (man) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jun-2000 ACCESSIONS S09801 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09801 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-487 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35396.1; !1PID:g1813966 !'##note possible protein-coding frames are given !'##note the DNA sequence was submitted to EMBL, December 1989, in !1computer-readable form GENETICS !$#introns 163/2; 177/3 CLASSIFICATION #superfamily cytomegalovirus UL37 protein KEYWORDS transmembrane protein FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-487 #product UL37 protein #status predicted #label MAT\ !$429-459 #domain transmembrane #status predicted #label TMM SUMMARY #length 487 #molecular-weight 56124 #checksum 8889 SEQUENCE /// ENTRY QQBEC4 #type complete TITLE HQLF3 protein - human cytomegalovirus (strain AD169) ALTERNATE_NAMES hypothetical protein US1 ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 28-Jul-2000 ACCESSIONS D26078; S09915 REFERENCE A92935 !$#authors Weston, K.; Barrell, B.G. !$#journal J. Mol. Biol. (1986) 192:177-208 !$#title Sequence of the short unique region, short repeats, and part !1of the long repeats of human cytomegalovirus. !$#cross-references MUID:87169717; PMID:3031311 !$#accession D26078 !'##molecule_type DNA !'##residues 1-212 ##label WES !'##cross-references EMBL:X04650; NID:g59801; PIDN:CAB37095.1; !1PID:g4456176 !'##experimental_source strain AD169 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09915 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-212 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35312.1; !1PID:g1780932 !'##experimental_source strain AD169 !'##note this sequence was submitted to the EMBL Data Library, December !11989 !'##note this reading frame extends between two stop codons and does not !1begin with a start codon GENETICS !$#gene HQLF3 CLASSIFICATION #superfamily cytomegalovirus HQLF3 protein SUMMARY #length 212 #molecular-weight 23481 #checksum 3208 SEQUENCE /// ENTRY QQBED6 #type complete TITLE HHRF6 protein - human cytomegalovirus (strain AD169) ALTERNATE_NAMES hypothetical protein US31 ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 #note host Homo sapiens (man) DATE 30-Sep-1989 #sequence_revision 22-Oct-1999 #text_change 16-Jun-2000 ACCESSIONS S09945; F27216 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09945 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-197 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35263.1; !1PID:g1780962 !'##note this sequence was submitted to the EMBL Data Library, December !11989 !'##note this reading frame extends between two stop codons and does not !1begin with a start codon REFERENCE A92935 !$#authors Weston, K.; Barrell, B.G. !$#journal J. Mol. Biol. (1986) 192:177-208 !$#title Sequence of the short unique region, short repeats, and part !1of the long repeats of human cytomegalovirus. !$#cross-references MUID:87169717; PMID:3031311 !$#accession F27216 !'##molecule_type DNA !'##residues 37-197 ##label WES !'##cross-references EMBL:X04650; NID:g59801; PIDN:CAA28342.1; !1PID:g59811 GENETICS !$#gene HHRF6 CLASSIFICATION #superfamily cytomegalovirus HQLF3 protein SUMMARY #length 197 #molecular-weight 22935 #checksum 1579 SEQUENCE /// ENTRY QQBED8 #type complete TITLE HHRF7 protein - human cytomegalovirus (strain AD169) ALTERNATE_NAMES hypothetical protein US32 ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS H27216; S09946 REFERENCE A92935 !$#authors Weston, K.; Barrell, B.G. !$#journal J. Mol. Biol. (1986) 192:177-208 !$#title Sequence of the short unique region, short repeats, and part !1of the long repeats of human cytomegalovirus. !$#cross-references MUID:87169717; PMID:3031311 !$#accession H27216 !'##molecule_type DNA !'##residues 1-183 ##label WES !'##cross-references EMBL:X04650; NID:g59801; PIDN:CAA28343.1; !1PID:g59812 !'##experimental_source strain AD169 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09946 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-183 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35264.1; !1PID:g1780963 !'##experimental_source strain AD169 !'##note this sequence was submitted to the EMBL Data Library, December !11989 GENETICS !$#gene HHRF7 CLASSIFICATION #superfamily cytomegalovirus HQLF3 protein SUMMARY #length 183 #molecular-weight 22057 #checksum 5951 SEQUENCE /// ENTRY QQBEC5 #type complete TITLE HQLF2 protein precursor - human cytomegalovirus (strain AD169) ALTERNATE_NAMES hypothetical protein US2 ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 28-Jul-2000 ACCESSIONS E26078; S09916 REFERENCE A92935 !$#authors Weston, K.; Barrell, B.G. !$#journal J. Mol. Biol. (1986) 192:177-208 !$#title Sequence of the short unique region, short repeats, and part !1of the long repeats of human cytomegalovirus. !$#cross-references MUID:87169717; PMID:3031311 !$#accession E26078 !'##molecule_type DNA !'##residues 1-199 ##label WES !'##cross-references EMBL:X04650; NID:g59801; PIDN:CAB37096.1; !1PID:g4456177 !'##experimental_source strain AD169 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09916 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-199 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35313.1; !1PID:g1780933 !'##experimental_source strain AD169 !'##note this sequence was submitted to the EMBL Data Library, December !11989 GENETICS !$#gene HQLF2 CLASSIFICATION #superfamily cytomegalovirus HQLF2 protein KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-199 #product hypothetical protein US2 #status predicted !8#label MAT\ !$161-186 #domain transmembrane #status predicted #label TMM\ !$68 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 199 #molecular-weight 23111 #checksum 5247 SEQUENCE /// ENTRY QQBEA7 #type complete TITLE UL69 protein - human cytomegalovirus (strain AD169) ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 #note host Homo sapiens (man) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS S09832 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09832 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-744 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35384.1; !1PID:g1780846 !'##note possible protein-coding frames are given !'##note the DNA sequence was submitted to EMBL, December 1989, in !1computer-readable form CLASSIFICATION #superfamily cytomegalovirus UL69 protein KEYWORDS transcription regulation SUMMARY #length 744 #molecular-weight 82677 #checksum 9591 SEQUENCE /// ENTRY QQBEC6 #type complete TITLE HQLF1 precursor - human cytomegalovirus (strain AD169) ALTERNATE_NAMES hypothetical protein US3 ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 28-Jul-2000 ACCESSIONS F26078; S09917 REFERENCE A92935 !$#authors Weston, K.; Barrell, B.G. !$#journal J. Mol. Biol. (1986) 192:177-208 !$#title Sequence of the short unique region, short repeats, and part !1of the long repeats of human cytomegalovirus. !$#cross-references MUID:87169717; PMID:3031311 !$#accession F26078 !'##molecule_type DNA !'##residues 1-186 ##label WES !'##cross-references EMBL:X04650; NID:g59801; PIDN:CAB37097.1; !1PID:g4456178 !'##experimental_source strain AD169 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09917 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-186 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35314.1; !1PID:g1780934 !'##experimental_source strain AD169 !'##note this sequence was submitted to the EMBL Data Library, December !11989 GENETICS !$#gene HQLF1 CLASSIFICATION #superfamily cytomegalovirus HQLF1 protein KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-186 #product hypothetical protein US3 #status predicted !8#label MAT\ !$160-182 #domain transmembrane #status predicted #label TMM\ !$60 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 186 #molecular-weight 21574 #checksum 3671 SEQUENCE /// ENTRY QQBEC7 #type complete TITLE HXLF6 protein precursor - human cytomegalovirus (strain AD169) ALTERNATE_NAMES hypothetical protein US6 ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 28-Jul-2000 ACCESSIONS G26078; S09920 REFERENCE A92935 !$#authors Weston, K.; Barrell, B.G. !$#journal J. Mol. Biol. (1986) 192:177-208 !$#title Sequence of the short unique region, short repeats, and part !1of the long repeats of human cytomegalovirus. !$#cross-references MUID:87169717; PMID:3031311 !$#accession G26078 !'##molecule_type DNA !'##residues 1-183 ##label WES !'##cross-references EMBL:X04650; NID:g59801; PIDN:CAB37098.1; !1PID:g4456179 !'##experimental_source strain AD169 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09920 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-183 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35273.1; !1PID:g1780937 !'##experimental_source strain AD169 !'##note this sequence was submitted to the EMBL Data Library, December !11989 GENETICS !$#gene HXLF6 CLASSIFICATION #superfamily cytomegalovirus HXLF6 protein KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-183 #product hypothetical protein US6 #status predicted !8#label MAT\ !$143-172 #domain transmembrane #status predicted #label TMM\ !$52 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 183 #molecular-weight 20639 #checksum 5087 SEQUENCE /// ENTRY QQBEC8 #type complete TITLE HXLF5 protein precursor - human cytomegalovirus (strain AD169) ALTERNATE_NAMES hypothetical protein US7 ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 28-Jul-2000 ACCESSIONS H26078; S09921 REFERENCE A92935 !$#authors Weston, K.; Barrell, B.G. !$#journal J. Mol. Biol. (1986) 192:177-208 !$#title Sequence of the short unique region, short repeats, and part !1of the long repeats of human cytomegalovirus. !$#cross-references MUID:87169717; PMID:3031311 !$#accession H26078 !'##molecule_type DNA !'##residues 1-225 ##label WES !'##cross-references EMBL:X04650; NID:g59801; PIDN:CAB37099.1; !1PID:g4456180 !'##experimental_source strain AD169 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09921 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-225 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35274.1; !1PID:g1780938 !'##experimental_source strain AD169 !'##note this sequence was submitted to the EMBL Data Library, December !11989 GENETICS !$#gene HXLF5 CLASSIFICATION #superfamily cytomegalovirus HXLF5 protein KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-225 #product hypothetical protein US7 #status predicted !8#label MAT\ !$168-192 #domain transmembrane #status predicted #label TMM\ !$69,205 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 225 #molecular-weight 26269 #checksum 6959 SEQUENCE /// ENTRY QQBEC9 #type complete TITLE HXLF4 protein precursor - human cytomegalovirus (strain AD169) ALTERNATE_NAMES hypothetical protein US8 ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 DATE 30-Sep-1989 #sequence_revision 29-Oct-1999 #text_change 29-Oct-1999 ACCESSIONS S09922; I26078 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09922 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-227 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35275.1; !1PID:g1780939 !'##note this sequence was submitted to the EMBL Data Library, December !11989 REFERENCE A92935 !$#authors Weston, K.; Barrell, B.G. !$#journal J. Mol. Biol. (1986) 192:177-208 !$#title Sequence of the short unique region, short repeats, and part !1of the long repeats of human cytomegalovirus. !$#cross-references MUID:87169717; PMID:3031311 !$#accession I26078 !'##molecule_type DNA !'##residues 'RRLTGEAA',1-227 ##label WES !'##cross-references EMBL:X04650; NID:g59801 GENETICS !$#gene HXLF4 CLASSIFICATION #superfamily cytomegalovirus HXLF4 protein KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-227 #product HXLF4 protein #status predicted #label MAT\ !$179-199 #domain transmembrane #status predicted #label TMM\ !$61 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 227 #molecular-weight 26633 #checksum 7393 SEQUENCE /// ENTRY QQBED1 #type complete TITLE HHLF5 protein - human cytomegalovirus (strain AD169) ALTERNATE_NAMES hypothetical protein US26 ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 28-Jul-2000 ACCESSIONS A27216; S09940 REFERENCE A92935 !$#authors Weston, K.; Barrell, B.G. !$#journal J. Mol. Biol. (1986) 192:177-208 !$#title Sequence of the short unique region, short repeats, and part !1of the long repeats of human cytomegalovirus. !$#cross-references MUID:87169717; PMID:3031311 !$#accession A27216 !'##molecule_type DNA !'##residues 1-603 ##label WES !'##cross-references EMBL:X04650; NID:g59801; PIDN:CAB37117.1; !1PID:g4456199 !'##experimental_source strain AD169 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09940 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-603 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35293.1; !1PID:g1780957 !'##experimental_source strain AD169 !'##note this sequence was submitted to the EMBL Data Library, December !11989 GENETICS !$#gene HHLF5 CLASSIFICATION #superfamily cytomegalovirus HHLF5 protein SUMMARY #length 603 #molecular-weight 70020 #checksum 2854 SEQUENCE /// ENTRY QQBEG6 #type complete TITLE HWLF1 protein - human cytomegalovirus (strain AD169) ALTERNATE_NAMES hypothetical protein US22 ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 28-Jul-2000 ACCESSIONS F27231; S09936 REFERENCE A92935 !$#authors Weston, K.; Barrell, B.G. !$#journal J. Mol. Biol. (1986) 192:177-208 !$#title Sequence of the short unique region, short repeats, and part !1of the long repeats of human cytomegalovirus. !$#cross-references MUID:87169717; PMID:3031311 !$#accession F27231 !'##molecule_type DNA !'##residues 1-593 ##label WES !'##cross-references EMBL:X04650; NID:g59801; PIDN:CAB37114.1; !1PID:g4456195 !'##experimental_source strain AD169 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09936 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-593 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35289.1; !1PID:g1780953 !'##experimental_source strain AD169 !'##note this sequence was submitted to the EMBL Data Library, December !11989 !'##note this reading frame extends between two stop codons and does not !1begin with a start codon GENETICS !$#gene HWLF1 CLASSIFICATION #superfamily cytomegalovirus HHLF5 protein SUMMARY #length 593 #molecular-weight 66969 #checksum 969 SEQUENCE /// ENTRY QQBEG7 #type complete TITLE HHLF7 protein - human cytomegalovirus (strain AD169) ALTERNATE_NAMES hypothetical protein HHLF7; hypothetical protein US23 ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS G27231; S09937 REFERENCE A92935 !$#authors Weston, K.; Barrell, B.G. !$#journal J. Mol. Biol. (1986) 192:177-208 !$#title Sequence of the short unique region, short repeats, and part !1of the long repeats of human cytomegalovirus. !$#cross-references MUID:87169717; PMID:3031311 !$#accession G27231 !'##molecule_type DNA !'##residues 1-598 ##label WES !'##cross-references EMBL:X04650 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09937 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 7-598 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35290.1; !1PID:g1780954 !'##note this sequence was submitted to the EMBL Data Library, December !11989 GENETICS !$#gene HHLF7; US23 CLASSIFICATION #superfamily cytomegalovirus HHLF5 protein SUMMARY #length 598 #molecular-weight 69488 #checksum 2458 SEQUENCE /// ENTRY QQBET1 #type complete TITLE hypothetical protein UL24 - human cytomegalovirus (strain AD169) ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 #note host Homo sapiens (man) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS S09787 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09787 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-358 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35423.1; !1PID:g59629 !'##note possible protein-coding frames are given !'##note the DNA sequence was submitted to EMBL, December 1989, in !1computer-readable form CLASSIFICATION #superfamily cytomegalovirus HHLF5 protein SUMMARY #length 358 #molecular-weight 40186 #checksum 9333 SEQUENCE /// ENTRY QQBED4 #type complete TITLE HHRF4 protein - human cytomegalovirus (strain AD169) ALTERNATE_NAMES hypothetical protein US29 ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS D27216; S09943 REFERENCE A92935 !$#authors Weston, K.; Barrell, B.G. !$#journal J. Mol. Biol. (1986) 192:177-208 !$#title Sequence of the short unique region, short repeats, and part !1of the long repeats of human cytomegalovirus. !$#cross-references MUID:87169717; PMID:3031311 !$#accession D27216 !'##molecule_type DNA !'##residues 1-462 ##label WES !'##cross-references EMBL:X04650; NID:g59801; PIDN:CAA28339.1; !1PID:g59808 !'##experimental_source strain AD169 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09943 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-462 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35261.1; !1PID:g1780960 !'##experimental_source strain AD169 !'##note this sequence was submitted to the EMBL Data Library, December !11989 GENETICS !$#gene HHRF4 CLASSIFICATION #superfamily cytomegalovirus HHRF4 protein SUMMARY #length 462 #molecular-weight 51066 #checksum 1830 SEQUENCE /// ENTRY QQBED5 #type complete TITLE HHRF5 protein - human cytomegalovirus (strain AD169) ALTERNATE_NAMES hypothetical protein US30 ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS E27216; S09944 REFERENCE A92935 !$#authors Weston, K.; Barrell, B.G. !$#journal J. Mol. Biol. (1986) 192:177-208 !$#title Sequence of the short unique region, short repeats, and part !1of the long repeats of human cytomegalovirus. !$#cross-references MUID:87169717; PMID:3031311 !$#accession E27216 !'##molecule_type DNA !'##residues 1-349 ##label WES !'##cross-references EMBL:X04650; NID:g59801; PIDN:CAA28340.1; !1PID:g59809 !'##experimental_source strain AD169 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09944 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-349 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35262.1; !1PID:g1780961 !'##experimental_source strain AD169 !'##note this sequence was submitted to the EMBL Data Library, December !11989 GENETICS !$#gene HHRF5 CLASSIFICATION #superfamily cytomegalovirus HHRF5 protein SUMMARY #length 349 #molecular-weight 39114 #checksum 6141 SEQUENCE /// ENTRY QQBED7 #type complete TITLE HHLF4 protein - human cytomegalovirus (strain AD169) ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 28-Jul-2000 ACCESSIONS G27216 REFERENCE A92935 !$#authors Weston, K.; Barrell, B.G. !$#journal J. Mol. Biol. (1986) 192:177-208 !$#title Sequence of the short unique region, short repeats, and part !1of the long repeats of human cytomegalovirus. !$#cross-references MUID:87169717; PMID:3031311 !$#accession G27216 !'##molecule_type DNA !'##residues 1-172 ##label WES !'##cross-references EMBL:X04650; NID:g59801; PIDN:CAB37118.1; !1PID:g4456200 GENETICS !$#gene HHLF4 CLASSIFICATION #superfamily cytomegalovirus HHLF4 protein SUMMARY #length 172 #molecular-weight 18223 #checksum 9697 SEQUENCE /// ENTRY QQBED9 #type complete TITLE HHLF3 protein - human cytomegalovirus (strain AD169) ALTERNATE_NAMES hypothetical protein US33 ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 28-Jul-2000 ACCESSIONS I27216; S09948 REFERENCE A92935 !$#authors Weston, K.; Barrell, B.G. !$#journal J. Mol. Biol. (1986) 192:177-208 !$#title Sequence of the short unique region, short repeats, and part !1of the long repeats of human cytomegalovirus. !$#cross-references MUID:87169717; PMID:3031311 !$#accession I27216 !'##molecule_type DNA !'##residues 1-137 ##label WES !'##cross-references EMBL:X04650; NID:g59801; PIDN:CAB37119.1; !1PID:g4456201 !'##experimental_source strain AD169 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09948 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-137 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35266.1; !1PID:g1780965 !'##experimental_source strain AD169 !'##note this sequence was submitted to the EMBL Data Library, December !11989 !'##note this reading frame extends between two stop codons and does not !1begin with a start codon GENETICS !$#gene HHLF3 CLASSIFICATION #superfamily cytomegalovirus HHLF3 protein SUMMARY #length 137 #molecular-weight 15774 #checksum 5884 SEQUENCE /// ENTRY QQBEE1 #type complete TITLE HHRF8 protein precursor - human cytomegalovirus (strain AD169) ALTERNATE_NAMES hypothetical protein US34 ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS A27349; S09947 REFERENCE A92935 !$#authors Weston, K.; Barrell, B.G. !$#journal J. Mol. Biol. (1986) 192:177-208 !$#title Sequence of the short unique region, short repeats, and part !1of the long repeats of human cytomegalovirus. !$#cross-references MUID:87169717; PMID:3031311 !$#accession A27349 !'##molecule_type DNA !'##residues 1-163 ##label WES !'##cross-references EMBL:X04650; NID:g59801; PIDN:CAA28345.1; !1PID:g59813 !'##experimental_source strain AD169 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09947 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-163 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35265.1; !1PID:g1780964 !'##experimental_source strain AD169 !'##note this sequence was submitted to the EMBL Data Library, December !11989 GENETICS !$#gene HHRF8 CLASSIFICATION #superfamily cytomegalovirus HHRF8 protein KEYWORDS glycoprotein FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-163 #product hypothetical protein US34 #status predicted !8#label MAT\ !$55,79,133,152 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 163 #molecular-weight 17766 #checksum 5306 SEQUENCE /// ENTRY QQBEE2 #type complete TITLE hypothetical protein US35 - human cytomegalovirus (strain AD169) ALTERNATE_NAMES hypothetical protein HHLF2 ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 #note host Homo sapiens (man) DATE 30-Sep-1989 #sequence_revision 13-Mar-1997 #text_change 28-Jul-2000 ACCESSIONS S09949; B27349 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09949 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-109 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35267.1; !1PID:g1780966 !'##note this sequence was submitted to the EMBL Data Library, December !11989 !'##note this reading frame extends between two stop codons and does not !1begin with a start codon REFERENCE A92935 !$#authors Weston, K.; Barrell, B.G. !$#journal J. Mol. Biol. (1986) 192:177-208 !$#title Sequence of the short unique region, short repeats, and part !1of the long repeats of human cytomegalovirus. !$#cross-references MUID:87169717; PMID:3031311 !$#accession B27349 !'##molecule_type DNA !'##residues 58-109 ##label WES !'##cross-references EMBL:X04650; NID:g59801; PIDN:CAB37120.1; !1PID:g4456202 GENETICS !$#gene HHLF2 CLASSIFICATION #superfamily cytomegalovirus HHLF2 protein SUMMARY #length 109 #molecular-weight 12966 #checksum 2468 SEQUENCE /// ENTRY QQBEF1 #type complete TITLE HXLF3 protein precursor - human cytomegalovirus (strain AD169) ALTERNATE_NAMES hypothetical protein US9 ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 28-Jul-2000 ACCESSIONS A27230; S09923 REFERENCE A92935 !$#authors Weston, K.; Barrell, B.G. !$#journal J. Mol. Biol. (1986) 192:177-208 !$#title Sequence of the short unique region, short repeats, and part !1of the long repeats of human cytomegalovirus. !$#cross-references MUID:87169717; PMID:3031311 !$#accession A27230 !'##molecule_type DNA !'##residues 1-247 ##label WES !'##cross-references EMBL:X04650; NID:g59801; PIDN:CAB37101.1; !1PID:g4456182 !'##experimental_source strain AD169 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09923 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-247 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35276.1; !1PID:g1780940 !'##experimental_source strain AD169 !'##note this sequence was submitted to the EMBL Data Library, December !11989 GENETICS !$#gene HXLF3 CLASSIFICATION #superfamily cytomegalovirus HXLF3 protein KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-247 #product hypothetical protein US9 #status predicted !8#label MAT\ !$205-222 #domain transmembrane #status predicted #label TMM\ !$97,158 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 247 #molecular-weight 28053 #checksum 1637 SEQUENCE /// ENTRY QQBEF2 #type complete TITLE HXLF2 protein precursor - human cytomegalovirus (strain AD169) ALTERNATE_NAMES hypothetical protein US10 ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 28-Jul-2000 ACCESSIONS B27230; S09924 REFERENCE A92935 !$#authors Weston, K.; Barrell, B.G. !$#journal J. Mol. Biol. (1986) 192:177-208 !$#title Sequence of the short unique region, short repeats, and part !1of the long repeats of human cytomegalovirus. !$#cross-references MUID:87169717; PMID:3031311 !$#accession B27230 !'##molecule_type DNA !'##residues 1-185 ##label WES !'##cross-references EMBL:X04650; NID:g59801; PIDN:CAB37102.1; !1PID:g4456183 !'##experimental_source strain AD169 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09924 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-185 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35277.1; !1PID:g1780941 !'##experimental_source strain AD169 !'##note this sequence was submitted to the EMBL Data Library, December !11989 GENETICS !$#gene HXLF2 CLASSIFICATION #superfamily cytomegalovirus HXLF2 protein KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-185 #product hypothetical protein US10 #status predicted !8#label MAT\ !$152-172 #domain transmembrane #status predicted #label TMM\ !$111,143 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 185 #molecular-weight 20771 #checksum 7770 SEQUENCE /// ENTRY QQBEF3 #type complete TITLE HXLF1 protein precursor - human cytomegalovirus (strain AD169) ALTERNATE_NAMES hypothetical protein US11 ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 28-Jul-2000 ACCESSIONS C27230; S09925 REFERENCE A92935 !$#authors Weston, K.; Barrell, B.G. !$#journal J. Mol. Biol. (1986) 192:177-208 !$#title Sequence of the short unique region, short repeats, and part !1of the long repeats of human cytomegalovirus. !$#cross-references MUID:87169717; PMID:3031311 !$#accession C27230 !'##molecule_type DNA !'##residues 1-215 ##label WES !'##cross-references EMBL:X04650; NID:g59801; PIDN:CAB37103.1; !1PID:g4456184 !'##experimental_source strain AD169 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09925 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-215 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35278.1; !1PID:g1780942 !'##experimental_source strain AD169 !'##note this sequence was submitted to the EMBL Data Library, December !11989 GENETICS !$#gene HXLF1 CLASSIFICATION #superfamily cytomegalovirus HXLF1 protein KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-215 #product hypothetical protein US11 #status predicted !8#label MAT\ !$179-200 #domain transmembrane #status predicted #label TMM\ !$73 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 215 #molecular-weight 25264 #checksum 4490 SEQUENCE /// ENTRY QQBEF4 #type complete TITLE HVLF6 protein - human cytomegalovirus (strain AD169) ALTERNATE_NAMES hypothetical protein US12 ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 28-Jul-2000 ACCESSIONS D27230; S09926 REFERENCE A92935 !$#authors Weston, K.; Barrell, B.G. !$#journal J. Mol. Biol. (1986) 192:177-208 !$#title Sequence of the short unique region, short repeats, and part !1of the long repeats of human cytomegalovirus. !$#cross-references MUID:87169717; PMID:3031311 !$#accession D27230 !'##molecule_type DNA !'##residues 1-281 ##label WES !'##cross-references EMBL:X04650; NID:g59801; PIDN:CAB37104.1; !1PID:g4456185 !'##experimental_source strain AD169 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09926 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-281 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35279.1; !1PID:g1780943 !'##experimental_source strain AD169 !'##note this sequence was submitted to the EMBL Data Library, December !11989 GENETICS !$#gene HVLF6 CLASSIFICATION #superfamily cytomegalovirus HVLF6 protein SUMMARY #length 281 #molecular-weight 32469 #checksum 7923 SEQUENCE /// ENTRY QQBEF5 #type complete TITLE HVLF5 protein - human cytomegalovirus (strain AD169) ALTERNATE_NAMES hypothetical protein US13 ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 28-Jul-2000 ACCESSIONS E27230; S09927 REFERENCE A92935 !$#authors Weston, K.; Barrell, B.G. !$#journal J. Mol. Biol. (1986) 192:177-208 !$#title Sequence of the short unique region, short repeats, and part !1of the long repeats of human cytomegalovirus. !$#cross-references MUID:87169717; PMID:3031311 !$#accession E27230 !'##molecule_type DNA !'##residues 1-261 ##label WES !'##cross-references EMBL:X04650; NID:g59801; PIDN:CAB37105.1; !1PID:g4456186 !'##experimental_source strain AD169 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09927 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-261 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35280.1; !1PID:g1780944 !'##experimental_source strain AD169 !'##note this sequence was submitted to the EMBL Data Library, December !11989 GENETICS !$#gene HVLF5 CLASSIFICATION #superfamily cytomegalovirus HVLF5 protein SUMMARY #length 261 #molecular-weight 29460 #checksum 5416 SEQUENCE /// ENTRY QQBEF6 #type complete TITLE HVLF4 protein - human cytomegalovirus (strain AD169) ALTERNATE_NAMES hypothetical protein US14 ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 22-Oct-1999 ACCESSIONS F27230; S09928 REFERENCE A92935 !$#authors Weston, K.; Barrell, B.G. !$#journal J. Mol. Biol. (1986) 192:177-208 !$#title Sequence of the short unique region, short repeats, and part !1of the long repeats of human cytomegalovirus. !$#cross-references MUID:87169717; PMID:3031311 !$#accession F27230 !'##molecule_type DNA !'##residues 1-328 ##label WES !'##cross-references EMBL:X04650 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09928 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 19-328 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35281.1; !1PID:g1780945 !'##note this sequence was submitted to the EMBL Data Library, December !11989 GENETICS !$#gene HVLF4 CLASSIFICATION #superfamily cytomegalovirus HVLF5 protein SUMMARY #length 328 #molecular-weight 35958 #checksum 4268 SEQUENCE /// ENTRY QQBEF7 #type complete TITLE HVLF3 protein - human cytomegalovirus (strain AD169) ALTERNATE_NAMES hypothetical protein US15 ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 28-Jul-2000 ACCESSIONS G27230; S09929 REFERENCE A92935 !$#authors Weston, K.; Barrell, B.G. !$#journal J. Mol. Biol. (1986) 192:177-208 !$#title Sequence of the short unique region, short repeats, and part !1of the long repeats of human cytomegalovirus. !$#cross-references MUID:87169717; PMID:3031311 !$#accession G27230 !'##molecule_type DNA !'##residues 1-484 ##label WES !'##cross-references EMBL:X04650; NID:g59801; PIDN:CAB37107.1; !1PID:g4456188 !'##experimental_source strain AD169 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09929 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-484 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35282.1; !1PID:g1780946 !'##experimental_source strain AD169 !'##note this sequence was submitted to the EMBL Data Library, December !11989 !'##note this reading frame extends between two stop codons and does not !1begin with a start codon GENETICS !$#gene HVLF3 CLASSIFICATION #superfamily cytomegalovirus HVLF3 protein SUMMARY #length 484 #molecular-weight 53048 #checksum 1060 SEQUENCE /// ENTRY QQBEF8 #type complete TITLE HVLF2 protein - human cytomegalovirus (strain AD169) ALTERNATE_NAMES hypothetical protein HVLF2; hypothetical protein US16 ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS H27230; S09930 REFERENCE A92935 !$#authors Weston, K.; Barrell, B.G. !$#journal J. Mol. Biol. (1986) 192:177-208 !$#title Sequence of the short unique region, short repeats, and part !1of the long repeats of human cytomegalovirus. !$#cross-references MUID:87169717; PMID:3031311 !$#accession H27230 !'##molecule_type DNA !'##residues 1-313 ##label WES !'##cross-references EMBL:X04650 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09930 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 5-313 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35283.1; !1PID:g1780947 !'##note this sequence was submitted to the EMBL Data Library, December !11989 GENETICS !$#gene HVLF2; US16 CLASSIFICATION #superfamily cytomegalovirus HVLF2 protein SUMMARY #length 313 #molecular-weight 35081 #checksum 760 SEQUENCE /// ENTRY QQBEG1 #type complete TITLE HVLF1 protein - human cytomegalovirus (strain AD169) ALTERNATE_NAMES hypothetical protein US17 ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 28-Jul-2000 ACCESSIONS A27231; S09931 REFERENCE A92935 !$#authors Weston, K.; Barrell, B.G. !$#journal J. Mol. Biol. (1986) 192:177-208 !$#title Sequence of the short unique region, short repeats, and part !1of the long repeats of human cytomegalovirus. !$#cross-references MUID:87169717; PMID:3031311 !$#accession A27231 !'##molecule_type DNA !'##residues 1-293 ##label WES !'##cross-references EMBL:X04650; NID:g59801; PIDN:CAB37109.1; !1PID:g4456190 !'##experimental_source strain AD169 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09931 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-293 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35284.1; !1PID:g1780948 !'##experimental_source strain AD169 !'##note this sequence was submitted to the EMBL Data Library, December !11989 GENETICS !$#gene HVLF1 CLASSIFICATION #superfamily cytomegalovirus HVLF1 protein SUMMARY #length 293 #molecular-weight 31908 #checksum 8812 SEQUENCE /// ENTRY QQBEG2 #type complete TITLE HWLF5 protein - human cytomegalovirus ALTERNATE_NAMES probable transmembrane protein US18 ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 28-Jul-2000 ACCESSIONS B27231; C45678; S09932 REFERENCE A92935 !$#authors Weston, K.; Barrell, B.G. !$#journal J. Mol. Biol. (1986) 192:177-208 !$#title Sequence of the short unique region, short repeats, and part !1of the long repeats of human cytomegalovirus. !$#cross-references MUID:87169717; PMID:3031311 !$#accession B27231 !'##molecule_type DNA !'##residues 1-274 ##label WES !'##cross-references EMBL:X04650; NID:g59801; PIDN:CAB37110.1; !1PID:g4456191 !'##experimental_source strain AD169 REFERENCE A45678 !$#authors Guo, Y.W.; Huang, E.S. !$#journal J. Virol. (1993) 67:2043-2054 !$#title Characterization of a structurally tricistronic gene of !1human cytomegalovirus composed of U(s)18, U(s)19, and U !1(s)20. !$#cross-references MUID:93188154; PMID:8383226 !$#accession C45678 !'##molecule_type DNA !'##residues 1-274 ##label GUO !'##cross-references GB:L04998; NID:g291530; PIDN:AAA45991.1; !1PID:g291533 !'##experimental_source strain Towne !'##note sequence extracted from NCBI backbone (NCBIN:126964, !1NCBIP:126967) REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09932 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-274 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35285.1; !1PID:g1780949 !'##experimental_source strain AD169 !'##note this sequence was submitted to the EMBL Data Library, December !11989 GENETICS !$#gene US18; HWLF5 !$#note this protein is encoded by a monocystronic late mRNA and !1also as the third of three proteins by a polycistronic early !1mRNA from the same gene CLASSIFICATION #superfamily cytomegalovirus HVLF1 protein SUMMARY #length 274 #molecular-weight 30193 #checksum 3759 SEQUENCE /// ENTRY QQBEG4 #type complete TITLE HWLF3 protein - human cytomegalovirus (strain AD169) ALTERNATE_NAMES hypothetical protein US20 ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 #note host Homo sapiens (man) DATE 30-Sep-1989 #sequence_revision 22-Oct-1999 #text_change 28-Jul-2000 ACCESSIONS S09934; D27231 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09934 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-357 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35287.1; !1PID:g1780951 !'##note this sequence was submitted to the EMBL Data Library, December !11989 !'##note this reading frame extends between two stop codons and does not !1begin with a start codon REFERENCE A92935 !$#authors Weston, K.; Barrell, B.G. !$#journal J. Mol. Biol. (1986) 192:177-208 !$#title Sequence of the short unique region, short repeats, and part !1of the long repeats of human cytomegalovirus. !$#cross-references MUID:87169717; PMID:3031311 !$#accession D27231 !'##molecule_type DNA !'##residues 104-357 ##label WES !'##cross-references EMBL:X04650; NID:g59801; PIDN:CAB37112.1; !1PID:g4456193 GENETICS !$#gene HWLF3 CLASSIFICATION #superfamily cytomegalovirus HVLF1 protein SUMMARY #length 357 #molecular-weight 39888 #checksum 3658 SEQUENCE /// ENTRY QQBEG3 #type complete TITLE HWLF4 protein - human cytomegalovirus (strain AD169) ALTERNATE_NAMES probable transmembrane protein US19 ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 28-Jul-2000 ACCESSIONS C27231; S09933; B45678 REFERENCE A92935 !$#authors Weston, K.; Barrell, B.G. !$#journal J. Mol. Biol. (1986) 192:177-208 !$#title Sequence of the short unique region, short repeats, and part !1of the long repeats of human cytomegalovirus. !$#cross-references MUID:87169717; PMID:3031311 !$#accession C27231 !'##molecule_type DNA !'##residues 1-240 ##label WES !'##cross-references EMBL:X04650; NID:g59801; PIDN:CAB37111.1; !1PID:g4456192 !'##experimental_source strain AD169 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09933 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-240 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35286.1; !1PID:g1780950 !'##experimental_source strain AD169 !'##note this sequence was submitted to the EMBL Data Library, December !11989 REFERENCE A45678 !$#authors Guo, Y.W.; Huang, E.S. !$#journal J. Virol. (1993) 67:2043-2054 !$#title Characterization of a structurally tricistronic gene of !1human cytomegalovirus composed of U(s)18, U(s)19, and U !1(s)20. !$#cross-references MUID:93188154; PMID:8383226 !$#accession B45678 !'##molecule_type DNA !'##residues 1-240 ##label GUO !'##cross-references GB:L04998; NID:g291530; PIDN:AAA45990.1; !1PID:g291532 !'##experimental_source strain Towne !'##note sequence extracted from NCBI backbone (NCBIN:126964, !1NCBIP:126966) GENETICS !$#gene US19; HWLF4 !$#note a single genetic locus encodes encodes two major classes of !1mRNA that share a common 3' region and polyadenylation !1signal; the longer class encodes three expressed proteins in !1nonoverlapping open reading frames; this protein is encoded !1by the middle of the three CLASSIFICATION #superfamily cytomegalovirus HWLF4 protein SUMMARY #length 240 #molecular-weight 26422 #checksum 2248 SEQUENCE /// ENTRY QQBEG5 #type complete TITLE HWLF2 protein - human cytomegalovirus (strain AD169) ALTERNATE_NAMES hypothetical protein US21 ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 28-Jul-2000 ACCESSIONS E27231; S09935 REFERENCE A92935 !$#authors Weston, K.; Barrell, B.G. !$#journal J. Mol. Biol. (1986) 192:177-208 !$#title Sequence of the short unique region, short repeats, and part !1of the long repeats of human cytomegalovirus. !$#cross-references MUID:87169717; PMID:3031311 !$#accession E27231 !'##molecule_type DNA !'##residues 1-239 ##label WES !'##cross-references EMBL:X04650; NID:g59801; PIDN:CAB37113.1; !1PID:g4456194 !'##experimental_source strain AD169 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09935 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-239 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35288.1; !1PID:g1780952 !'##experimental_source strain AD169 !'##note this sequence was submitted to the EMBL Data Library, December !11989 GENETICS !$#gene HWLF2 CLASSIFICATION #superfamily cytomegalovirus HWLF2 protein SUMMARY #length 239 #molecular-weight 26584 #checksum 4968 SEQUENCE /// ENTRY QQBEG8 #type complete TITLE HHLF6 protein - human cytomegalovirus (strain AD169) ALTERNATE_NAMES hypothetical protein US24 ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 28-Jul-2000 ACCESSIONS H27231; S09938 REFERENCE A92935 !$#authors Weston, K.; Barrell, B.G. !$#journal J. Mol. Biol. (1986) 192:177-208 !$#title Sequence of the short unique region, short repeats, and part !1of the long repeats of human cytomegalovirus. !$#cross-references MUID:87169717; PMID:3031311 !$#accession H27231 !'##molecule_type DNA !'##residues 1-500 ##label WES !'##cross-references EMBL:X04650; NID:g59801; PIDN:CAB37116.1; !1PID:g4456197 !'##experimental_source strain AD169 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09938 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-500 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35291.1; !1PID:g1780955 !'##experimental_source strain AD169 !'##note this sequence was submitted to the EMBL Data Library, December !11989 GENETICS !$#gene HHLF6 CLASSIFICATION #superfamily cytomegalovirus HHLF6 protein SUMMARY #length 500 #molecular-weight 57926 #checksum 1267 SEQUENCE /// ENTRY QQBEG9 #type complete TITLE HHRF1 protein - human cytomegalovirus (strain AD169) ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 24-Oct-1997 ACCESSIONS I27231 REFERENCE A92935 !$#authors Weston, K.; Barrell, B.G. !$#journal J. Mol. Biol. (1986) 192:177-208 !$#title Sequence of the short unique region, short repeats, and part !1of the long repeats of human cytomegalovirus. !$#cross-references MUID:87169717; PMID:3031311 !$#accession I27231 !'##molecule_type DNA !'##residues 1-156 ##label WES !'##cross-references EMBL:X04650 GENETICS !$#gene HHRF1 CLASSIFICATION #superfamily cytomegalovirus HHRF1 protein SUMMARY #length 156 #molecular-weight 17396 #checksum 6719 SEQUENCE /// ENTRY WMBEH8 #type complete TITLE infected cell protein ICP18.5 - human herpesvirus 1 (strain F) ORGANISM #formal_name human herpesvirus 1 DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jul-1999 ACCESSIONS A26101 REFERENCE A26101 !$#authors Pellett, P.E.; Jenkins, F.J.; Ackermann, M.; Sarmiento, M.; !1Roizman, B. !$#journal J. Virol. (1986) 60:1134-1140 !$#title Transcription initiation sites and nucleotide sequence of a !1herpes simplex virus 1 gene conserved in the Epstein-Barr !1virus genome and reported to affect the transport of viral !1glycoproteins. !$#cross-references MUID:87061190; PMID:3023664 !$#accession A26101 !'##molecule_type DNA !'##residues 1-780 ##label PEL !'##cross-references GB:M14164; GB:M12398; NID:g330084; PIDN:AAA45775.1; !1PID:g330085 COMMENT This protein may affect translocation of herpes simplex !1virus glycoproteins to membranes. GENETICS !$#gene ICP18.5 CLASSIFICATION #superfamily herpesvirus infected cell protein ICP18.5 KEYWORDS capsid assembly SUMMARY #length 780 #molecular-weight 83845 #checksum 1671 SEQUENCE /// ENTRY WMBEK8 #type complete TITLE infected cell protein ICP18.5 - human herpesvirus 1 (strain Angelotti) ORGANISM #formal_name human herpesvirus 1 #note host Homo sapiens (man) DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jul-1999 ACCESSIONS A26987 REFERENCE A26987 !$#authors Knopf, C.W. !$#journal Nucleic Acids Res. (1987) 15:8109-8110 !$#title The nucleotide sequence of the herpes simplex virus type 1 !1late gene ICP18.5 of strain Angelotti. !$#cross-references MUID:88040433; PMID:2823222 !$#accession A26987 !'##molecule_type DNA !'##residues 1-785 ##label KNO !'##cross-references GB:Y00453; NID:g60416; PIDN:CAA68508.1; PID:g60417 COMMENT This protein is involved in the translocation of viral !1glycoproteins to membranes. CLASSIFICATION #superfamily herpesvirus infected cell protein ICP18.5 KEYWORDS capsid assembly; late protein SUMMARY #length 785 #molecular-weight 85607 #checksum 2371 SEQUENCE /// ENTRY WMBEW8 #type complete TITLE infected cell protein ICP18.5 - human herpesvirus 1 (strain 17) ORGANISM #formal_name human herpesvirus 1 #note host Homo sapiens (man) DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jun-2000 ACCESSIONS A30085 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession A30085 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-785 ##label MCG !'##cross-references GB:X14112; NID:g1944536; PIDN:CAA32321.1; !1PID:g59528; GB:D00317 CLASSIFICATION #superfamily herpesvirus infected cell protein ICP18.5 KEYWORDS capsid assembly; late protein SUMMARY #length 785 #molecular-weight 85577 #checksum 2333 SEQUENCE /// ENTRY WMBEBH #type complete TITLE infected cell protein ICP18.5 - bovine herpesvirus 2 (strain BMV) ORGANISM #formal_name bovine herpesvirus 2 DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 11-Nov-1996 ACCESSIONS B29242 REFERENCE A94381 !$#authors Hammerschmidt, W.; Conraths, F.; Mankertz, J.; Pauli, G.; !1Ludwig, H.; Buhk, H.J. !$#journal Virology (1988) 165:388-405 !$#title Conservation of a gene cluster including glycoprotein B in !1bovine herpesvirus type 2 (BHV-2) and herpes simplex virus !1type 1 (HSV-1). !$#cross-references MUID:88306231; PMID:2841793 !$#accession B29242 !'##status translation not shown !'##molecule_type DNA !'##residues 1-664 ##label HAM !'##cross-references GB:M21628 CLASSIFICATION #superfamily herpesvirus infected cell protein ICP18.5 KEYWORDS capsid assembly SUMMARY #length 664 #molecular-weight 72367 #checksum 8190 SEQUENCE /// ENTRY WMBEPR #type complete TITLE infected cell protein ICP18.5 - suid herpesvirus 1 (strain Becker) ORGANISM #formal_name suid herpesvirus 1 DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS A33779 REFERENCE S04145 !$#authors Pederson, N.E.; Enquist, L.W. !$#journal Nucleic Acids Res. (1989) 17:3597 !$#title The nucleotide sequence of a pseudorabies virus gene similar !1to ICP18.5 of herpes simplex virus type 1. !$#cross-references MUID:89263808; PMID:2542904 !$#accession A33779 !'##molecule_type DNA !'##residues 1-724 ##label PED !'##cross-references GB:X14573; NID:g61407; PIDN:CAA32712.1; PID:g61409 CLASSIFICATION #superfamily herpesvirus infected cell protein ICP18.5 KEYWORDS capsid assembly; late protein SUMMARY #length 724 #molecular-weight 78881 #checksum 5788 SEQUENCE /// ENTRY WMBE56 #type complete TITLE infected cell protein ICP18.5 - human cytomegalovirus (strain AD169) ALTERNATE_NAMES HFLF0 protein ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 #note host Homo sapiens (man) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS S09819 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09819 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-850 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35371.1; !1PID:g1780834 !'##note possible protein-coding frames are given !'##note the DNA sequence was submitted to EMBL, December 1989, in !1computer-readable form CLASSIFICATION #superfamily herpesvirus infected cell protein ICP18.5 KEYWORDS capsid assembly SUMMARY #length 850 #molecular-weight 95867 #checksum 6125 SEQUENCE /// ENTRY B44051 #type complete TITLE infected cell protein ICP18.5 - murine cytomegalovirus (strain Smith) ORGANISM #formal_name murine cytomegalovirus, murine herpesvirus 1 DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS B44051; S23219 REFERENCE A44051 !$#authors Messerle, M.; Keil, G.M.; Schneider, K.; Koszinowski, U.H. !$#journal Virology (1992) 191:355-367 !$#title Characterization of the murine cytomegalovirus genes !1encoding the major DNA binding protein and the ICP18.5 !1homolog. !$#cross-references MUID:93033129; PMID:1329325 !$#accession B44051 !'##molecule_type DNA !'##residues 1-798 ##label MES !'##cross-references GB:X67021; NID:g60534; PIDN:CAA47415.1; PID:g60536 !'##experimental_source ATCC VR-194 CLASSIFICATION #superfamily herpesvirus infected cell protein ICP18.5 KEYWORDS capsid assembly; glycoprotein; late protein FEATURE !$319,675 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 798 #molecular-weight 89100 #checksum 5753 SEQUENCE /// ENTRY WZBE30 #type complete TITLE gene 30 protein - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS D27214 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession D27214 !'##molecule_type DNA !'##residues 1-770 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27913.1; !1PID:g60019 GENETICS !$#gene 30 CLASSIFICATION #superfamily herpesvirus infected cell protein ICP18.5 KEYWORDS capsid assembly SUMMARY #length 770 #molecular-weight 86971 #checksum 3254 SEQUENCE /// ENTRY WZBEC5 #type complete TITLE infected cell protein ICP18.5 - equine herpesvirus 1 ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Jun-1993 #text_change 11-Nov-1996 ACCESSIONS F36798; JQ0847 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession F36798 !'##molecule_type DNA !'##residues 1-766 ##label TEL !'##cross-references GB:M86664 !'##experimental_source strain Ab4p REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given REFERENCE JQ0846 !$#authors Bell, C.W.; Whalley, J.M. !$#submission submitted to JIPID, January 1991 !$#accession JQ0847 !'##molecule_type DNA !'##residues 1-766 ##label BEL GENETICS !$#gene 32 CLASSIFICATION #superfamily herpesvirus infected cell protein ICP18.5 KEYWORDS capsid assembly SUMMARY #length 766 #molecular-weight 84383 #checksum 7606 SEQUENCE /// ENTRY WMBE38 #type complete TITLE infected cell protein ICP34.5 - human herpesvirus 1 (strain F) ORGANISM #formal_name human herpesvirus 1 DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jul-1999 ACCESSIONS A27768 REFERENCE A27768 !$#authors Chou, J.; Roizman, B. !$#journal J. Virol. (1986) 57:629-637 !$#title The terminal a sequence of the herpes simplex virus genome !1contains the promoter of a gene located in the repeat !1sequences of the L component. !$#cross-references MUID:86115412; PMID:3003394 !$#accession A27768 !'##molecule_type DNA !'##residues 1-358 ##label CHO !'##cross-references GB:M12240; NID:g330122; PIDN:AAA45794.1; !1PID:g330123 COMMENT This protein accumulates late in infection predominantly in !1the cytoplasm of the infected cell. GENETICS !$#gene ICP34.5 CLASSIFICATION #superfamily herpesvirus infected cell protein ICP34.5 KEYWORDS tandem repeat FEATURE !$175-204 #region 3-residue repeats (A-T-P) SUMMARY #length 358 #molecular-weight 37053 #checksum 784 SEQUENCE /// ENTRY JQ1682 #type complete TITLE infected cell protein ICP34.5 - human herpesvirus 1 (strain 17) ORGANISM #formal_name human herpesvirus 1 DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 26-Feb-1999 ACCESSIONS JQ1682 REFERENCE JQ1682 !$#authors Dolan, A.; McKie, E.; MacLean, A.R.; McGeoch, D.J. !$#journal J. Gen. Virol. (1992) 73:971-973 !$#title Status of the ICP34.5 gene in herpes simplex virus type 1 !1strain 17. !$#cross-references MUID:92341080; PMID:1321882 !$#accession JQ1682 !'##molecule_type DNA !'##residues 1-248 ##label DOL !'##cross-references GB:S40593 GENETICS !$#gene ICP34.5 CLASSIFICATION #superfamily herpesvirus infected cell protein ICP34.5 KEYWORDS tandem repeat FEATURE !$161-175 #region 3-residue repeats (A-T-P) SUMMARY #length 248 #molecular-weight 26185 #checksum 7517 SEQUENCE /// ENTRY WMBEXE #type complete TITLE infected cell protein ICP34.5 - human herpesvirus 2 (strain HG52) ALTERNATE_NAMES RL1 protein ORGANISM #formal_name human herpesvirus 2 #note host Homo sapiens (man) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS JQ1502 REFERENCE JQ1494 !$#authors McGeoch, D.J.; Cunningham, C.; McIntyre, G.; Dolan, A. !$#journal J. Gen. Virol. (1991) 72:3057-3075 !$#title Comparative sequence analysis of the long repeat regions and !1adjoining parts of the long unique regions in the genomes of !1herpes simplex viruses types 1 and 2. !$#cross-references MUID:92113549; PMID:1662697 !$#accession JQ1502 !'##molecule_type DNA !'##residues 1-261 ##label MCG !'##cross-references GB:D10471; DDBJ:D01128; NID:g221784; !1PIDN:BAA23428.1; PID:g2626943 GENETICS !$#gene RL1 !$#introns 165/3 CLASSIFICATION #superfamily herpesvirus infected cell protein ICP34.5 KEYWORDS tandem repeat FEATURE !$3-12 #region 5-residue repeats (R-R-R-G-P)\ !$16-31 #region 8-residue repeats (P-R-P-G-A-P-A-V) SUMMARY #length 261 #molecular-weight 27908 #checksum 7258 SEQUENCE /// ENTRY WMBEPN #type complete TITLE 28K protein - suid herpesvirus 1 (strain NIA-3) ORGANISM #formal_name suid herpesvirus 1 DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jun-2000 ACCESSIONS B36654; PQ0077 REFERENCE A36654 !$#authors van Zijl, M.; van der Gulden, H.; de Wind, N.; Gielkens, A.; !1Berns, A. !$#journal J. Gen. Virol. (1990) 71:1747-1755 !$#title Identification of two genes in the unique short region of !1pseudorabies virus; comparison with herpes simplex virus and !1varicella-zoster virus. !$#cross-references MUID:90362061; PMID:2167928 !$#accession B36654 !'##molecule_type DNA !'##residues 1-256 ##label VAN !'##cross-references GB:D10452; GB:D01117; NID:g222586; PIDN:BAA01246.1; !1PID:g222587 REFERENCE PQ0077 !$#authors Zhang, G.; Leader, D.P. !$#submission submitted to JIPID, June 1990 !$#description The structure of the pseudorabies virus genome at the end of !1inverted repeat sequences proximal to the junction with the !1short unique region. !$#accession PQ0077 !'##molecule_type DNA !'##residues 201-256 ##label ZHA !'##experimental_source strain Ka CLASSIFICATION #superfamily herpesvirus US2 protein SUMMARY #length 256 #molecular-weight 27757 #checksum 3021 SEQUENCE /// ENTRY QQBE72 #type complete TITLE US2 protein - human herpesvirus 1 ORGANISM #formal_name human herpesvirus 1 #note host Homo sapiens (man) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS A05238 REFERENCE A00656 !$#authors McGeoch, D.J.; Dolan, A.; Donald, S.; Rixon, F.J. !$#journal J. Mol. Biol. (1985) 181:1-13 !$#title Sequence determination and genetic content of the short !1unique region in the genome of herpes simplex virus type 1. !$#cross-references MUID:85160822; PMID:2984429 !$#accession A05238 !'##molecule_type DNA !'##residues 1-291 ##label MCG !'##cross-references GB:X02138; NID:g59865; PIDN:CAA26056.1; PID:g59868 !'##experimental_source strain 17 GENETICS !$#gene US2 CLASSIFICATION #superfamily herpesvirus US2 protein SUMMARY #length 291 #molecular-weight 32470 #checksum 6171 SEQUENCE /// ENTRY WZBEF9 #type complete TITLE gene 68 protein - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS E36802 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession E36802 !'##molecule_type DNA !'##residues 1-418 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02503.1; !1PID:g330859 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 68 CLASSIFICATION #superfamily herpesvirus US2 protein SUMMARY #length 418 #molecular-weight 46788 #checksum 1947 SEQUENCE /// ENTRY B48338 #type complete TITLE gene 68 protein - equine herpesvirus 4 ORGANISM #formal_name equine herpesvirus 4 #note host Equus caballus (domestic horse) DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 21-Jul-2000 ACCESSIONS B48338; T42611 REFERENCE A48338 !$#authors Nagesha, H.S.; Crabb, B.S.; Studdert, M.J. !$#journal Arch. Virol. (1993) 128:143-154 !$#title Analysis of the nucleotide sequence of five genes at the !1left end of the unique short region of the equine !1herpesvirus 4 genome. !$#cross-references MUID:93119267; PMID:8380320 !$#accession B48338 !'##molecule_type DNA !'##residues 1-324 ##label NAG !'##cross-references GB:M89634; NID:g330929; PIDN:AAA46101.1; !1PID:g330931 !'##experimental_source strain 1942 !'##note sequence extracted from NCBI backbone (NCBIN:121741, !1NCBIP:121743) REFERENCE Z22173 !$#authors Telford, E.A.; Watson, M.S.; Perry, J.; Cullinane, A.A.; !1Davison, A.J. !$#journal J. Gen. Virol. (1998) 79:1197-1203 !$#title The DNA sequence of equine herpesvirus-4. !$#cross-references MUID:98264497; PMID:9603335 !$#accession T42611 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-324 ##label TEL !'##cross-references EMBL:AF030027; NID:g2605950; PIDN:AAC59587.1; !1PID:g2606015 !'##experimental_source strain NS80567 GENETICS !$#gene 68 CLASSIFICATION #superfamily herpesvirus US2 protein SUMMARY #length 324 #molecular-weight 36456 #checksum 9094 SEQUENCE /// ENTRY QQBE74 #type complete TITLE US4 protein - human herpesvirus 1 ORGANISM #formal_name human herpesvirus 1 #note host Homo sapiens (man) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS A05239 REFERENCE A00656 !$#authors McGeoch, D.J.; Dolan, A.; Donald, S.; Rixon, F.J. !$#journal J. Mol. Biol. (1985) 181:1-13 !$#title Sequence determination and genetic content of the short !1unique region in the genome of herpes simplex virus type 1. !$#cross-references MUID:85160822; PMID:2984429 !$#accession A05239 !'##molecule_type DNA !'##residues 1-238 ##label MCG !'##cross-references GB:X02138; NID:g59865; PIDN:CAA26058.1; PID:g59870 !'##experimental_source strain 17 GENETICS !$#gene US4 CLASSIFICATION #superfamily herpesvirus US4 protein SUMMARY #length 238 #molecular-weight 25238 #checksum 5333 SEQUENCE /// ENTRY QQBE75 #type complete TITLE glycoprotein J - human herpesvirus 1 ORGANISM #formal_name human herpesvirus 1 #note host Homo sapiens (man) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS A05240 REFERENCE A00656 !$#authors McGeoch, D.J.; Dolan, A.; Donald, S.; Rixon, F.J. !$#journal J. Mol. Biol. (1985) 181:1-13 !$#title Sequence determination and genetic content of the short !1unique region in the genome of herpes simplex virus type 1. !$#cross-references MUID:85160822; PMID:2984429 !$#accession A05240 !'##molecule_type DNA !'##residues 1-92 ##label MCG !'##cross-references GB:L00036; NID:g291490; PIDN:AAA96683.1; !1PID:g291499 !'##experimental_source strain 17 GENETICS !$#gene US5 CLASSIFICATION #superfamily herpesvirus US5 protein KEYWORDS glycoprotein FEATURE !$30 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 92 #molecular-weight 9556 #checksum 6364 SEQUENCE /// ENTRY JQ1745 #type complete TITLE glycoprotein J - cercopithecine herpesvirus 1 ORGANISM #formal_name cercopithecine herpesvirus 1 DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS JQ1745 REFERENCE JQ1745 !$#authors Bennett, A.M.; Harrington, L.; Kelly, D.C. !$#journal J. Gen. Virol. (1992) 73:2963-2967 !$#title Nucleotide sequence analysis of genes encoding glycoproteins !1D and J in simian herpes B virus. !$#cross-references MUID:93057369; PMID:1331298 !$#accession JQ1745 !'##molecule_type DNA !'##residues 1-117 ##label BEN !'##cross-references GB:S48101; NID:g259588; PIDN:AAB24128.1; !1PID:g259589 CLASSIFICATION #superfamily herpesvirus US5 protein KEYWORDS glycoprotein FEATURE !$36,46,58 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 117 #molecular-weight 11614 #checksum 8335 SEQUENCE /// ENTRY QQBE77 #type complete TITLE glycoprotein I precursor - human herpesvirus 1 (strain 17) ORGANISM #formal_name human herpesvirus 1 #note host Homo sapiens (man) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS A05243 REFERENCE A00656 !$#authors McGeoch, D.J.; Dolan, A.; Donald, S.; Rixon, F.J. !$#journal J. Mol. Biol. (1985) 181:1-13 !$#title Sequence determination and genetic content of the short !1unique region in the genome of herpes simplex virus type 1. !$#cross-references MUID:85160822; PMID:2984429 !$#accession A05243 !'##molecule_type DNA !'##residues 1-390 ##label MCG !'##cross-references GB:L00036; NID:g291490; PIDN:AAA96681.1; !1PID:g291497 GENETICS !$#gene US7 CLASSIFICATION #superfamily herpesvirus US7 protein KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-390 #product glycoprotein I #status predicted #label GPI\ !$277-293 #domain transmembrane #status predicted #label TMN\ !$156,175,257 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 390 #molecular-weight 41369 #checksum 3280 SEQUENCE /// ENTRY QQBE88 #type complete TITLE glycoprotein I precursor - human herpesvirus 2 (strain 333) ORGANISM #formal_name human herpesvirus 2 #note host Homo sapiens (man) DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS A05246 REFERENCE A05246 !$#authors Hodgman, T.C.; Minson, A.C. !$#journal Virology (1986) 153:1-11 !$#title The herpes simplex virus type 2 equivalent of the herpes !1simplex virus type 1 US7 gene and its flanking sequences. !$#cross-references MUID:86291145; PMID:3016980 !$#accession A05246 !'##molecule_type DNA !'##residues 1-372 ##label HOD !'##cross-references EMBL:M14886; NID:g330311; PIDN:AAA45861.1; !1PID:g330313 GENETICS !$#map_position 0.919-0.927 CLASSIFICATION #superfamily herpesvirus US7 protein KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-372 #product glycoprotein I #status predicted #label GPI\ !$255-282 #domain transmembrane #status predicted #label TMN\ !$156,169,175,243 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 372 #molecular-weight 39548 #checksum 462 SEQUENCE /// ENTRY WMBE6H #type complete TITLE transcription regulator B701 - human herpesvirus 6 (strain U1102) ORGANISM #formal_name human herpesvirus 6 #note host Homo sapiens (man) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 02-Jul-1998 ACCESSIONS A42186 REFERENCE A42186 !$#authors Geng, Y.; Chandran, B.; Josephs, S.F.; Wood, C. !$#journal J. Virol. (1992) 66:1564-1570 !$#title Identification and characterization of a human herpesvirus 6 !1gene segment that trans activates the human immunodeficiency !1virus type 1 promoter. !$#cross-references MUID:92148942; PMID:1310766 !$#accession A42186 !'##molecule_type DNA !'##residues 1-143 ##label GEN !'##cross-references GB:M81789 COMMENT This protein can trans activate the human immunodeficiency !1virus type 1 promoter. CLASSIFICATION #superfamily human herpesvirus 6 transcription regulator !1B701 KEYWORDS transcription SUMMARY #length 143 #molecular-weight 16385 #checksum 9347 SEQUENCE /// ENTRY IXBE1F #type complete TITLE alpha trans-inducing protein - human herpesvirus 1 ORGANISM #formal_name human herpesvirus 1 DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 16-Jul-1999 ACCESSIONS A03727 REFERENCE A03727 !$#authors Pellett, P.E.; McKnight, J.L.C.; Jenkins, F.J.; Roizman, B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:5870-5874 !$#title Nucleotide sequence and predicted amino acid sequence of a !1protein encoded in a small herpes simplex virus DNA fragment !1capable of trans-inducing alpha genes. !$#cross-references MUID:85298259; PMID:2994050 !$#accession A03727 !'##molecule_type DNA !'##residues 1-479 ##label PEL !'##cross-references GB:K03350; NID:g330054; PIDN:AAA45766.1; !1PID:g330055 !'##experimental_source strain F COMMENT This protein induces transcription of the alpha genes. GENETICS !$#map_position 0.680-0.689 CLASSIFICATION #superfamily herpesvirus alpha trans-inducing protein KEYWORDS DNA binding; trans-inducing protein; transcription SUMMARY #length 479 #molecular-weight 53053 #checksum 3746 SEQUENCE /// ENTRY IXBE17 #type complete TITLE alpha trans-inducing protein - human herpesvirus 1 (strain 17) ALTERNATE_NAMES major tegument protein; UL48 protein; Vmw65 protein ORGANISM #formal_name human herpesvirus 1 DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Jun-2000 ACCESSIONS A24118; C30089 REFERENCE A24118 !$#authors Dalrymple, M.A.; McGeoch, D.J.; Davison, A.J.; Preston, C.M. !$#journal Nucleic Acids Res. (1985) 13:7865-7879 !$#title DNA sequence of the herpes simplex virus type 1 gene whose !1product is responsible for transcriptional activation of !1immediate early promoters. !$#cross-references MUID:86067203; PMID:2999707 !$#accession A24118 !'##molecule_type DNA !'##residues 1-490 ##label DAL !'##cross-references GB:X03141; NID:g59834; PIDN:CAA26913.1; PID:g59835 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession C30089 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-490 ##label MCG !'##cross-references GB:X14112; NID:g1944536; PIDN:CAA32298.1; !1PID:g59548; GB:D00317 GENETICS !$#gene UL48 !$#map_position 0.669-0.685 CLASSIFICATION #superfamily herpesvirus alpha trans-inducing protein KEYWORDS DNA binding; trans-inducing protein; transcription SUMMARY #length 490 #molecular-weight 54345 #checksum 3996 SEQUENCE /// ENTRY IXBE33 #type complete TITLE alpha trans-inducing protein - human herpesvirus 2 (strain 333) ALTERNATE_NAMES virion transactivator protein Vmw65 ORGANISM #formal_name human herpesvirus 2 #note host Homo sapiens (man) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Feb-1997 ACCESSIONS A41562 REFERENCE A41562 !$#authors Greaves, R.F.; O'Hare, P. !$#journal J. Virol. (1991) 65:6705-6713 !$#title Sequence, function, and regulation of the Vmw65 gene of !1herpes simplex virus type 2. !$#cross-references MUID:92046332; PMID:1658370 !$#accession A41562 !'##molecule_type DNA !'##residues 1-490 ##label GRE !'##cross-references GB:M75098 CLASSIFICATION #superfamily herpesvirus alpha trans-inducing protein KEYWORDS DNA binding; trans-inducing protein; transcription SUMMARY #length 490 #molecular-weight 54603 #checksum 9613 SEQUENCE /// ENTRY IXBE10 #type complete TITLE alpha trans-inducing protein - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS A27342 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession A27342 !'##molecule_type DNA !'##residues 1-410 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27893.1; !1PID:g59999 GENETICS !$#gene 10 CLASSIFICATION #superfamily herpesvirus alpha trans-inducing protein KEYWORDS DNA binding; trans-inducing protein; transcription SUMMARY #length 410 #molecular-weight 46575 #checksum 4604 SEQUENCE /// ENTRY IXBEA1 #type complete TITLE alpha trans-inducing protein - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS D36796 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession D36796 !'##molecule_type DNA !'##residues 1-479 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02447.1; !1PID:g330804 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 12 CLASSIFICATION #superfamily herpesvirus alpha trans-inducing protein KEYWORDS DNA binding; trans-inducing protein; transcription SUMMARY #length 479 #molecular-weight 53646 #checksum 2372 SEQUENCE /// ENTRY QQBE79 #type complete TITLE tegument protein - human herpesvirus 1 ORGANISM #formal_name human herpesvirus 1 #note host Homo sapiens (man) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jun-2000 ACCESSIONS A05241 REFERENCE A00656 !$#authors McGeoch, D.J.; Dolan, A.; Donald, S.; Rixon, F.J. !$#journal J. Mol. Biol. (1985) 181:1-13 !$#title Sequence determination and genetic content of the short !1unique region in the genome of herpes simplex virus type 1. !$#cross-references MUID:85160822; PMID:2984429 !$#accession A05241 !'##molecule_type DNA !'##residues 1-90 ##label MCG !'##cross-references GB:X14112; NID:g1944536; PIDN:CAA32274.1; !1PID:g59567 !'##experimental_source strain 17 CLASSIFICATION #superfamily human herpesvirus tegument protein; herpesvirus !1tegument protein homology FEATURE !$31-83 #domain herpesvirus tegument protein homology #label !8HTP SUMMARY #length 90 #molecular-weight 10026 #checksum 1386 SEQUENCE /// ENTRY QQBECE #type complete TITLE tegument protein - cercopithecine herpesvirus 1 ORGANISM #formal_name cercopithecine herpesvirus 1 DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS JQ1406 REFERENCE JQ1406 !$#authors Killeen, A.M.; Harrington, L.; Wall, L.V.M.; Kelly, D.C. !$#journal J. Gen. Virol. (1992) 73:195-199 !$#title Nucleotide sequence analysis of a homologue of herpes !1simplex virus type 1 gene US9 found in the genome of simian !1herpes B virus. !$#cross-references MUID:92113572; PMID:1309859 !$#accession JQ1406 !'##molecule_type DNA !'##residues 1-90 ##label KIL !'##cross-references GB:S75996; NID:g243000; PIDN:AAB21002.1; !1PID:g243002 CLASSIFICATION #superfamily human herpesvirus tegument protein; herpesvirus !1tegument protein homology FEATURE !$30-82 #domain herpesvirus tegument protein homology #label !8HTP SUMMARY #length 90 #molecular-weight 9930 #checksum 9175 SEQUENCE /// ENTRY WZBE65 #type complete TITLE tegument protein - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS D27345 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession D27345 !'##molecule_type DNA !'##residues 1-102 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27948.1; !1PID:g60054 CLASSIFICATION #superfamily human herpesvirus tegument protein; herpesvirus !1tegument protein homology FEATURE !$43-95 #domain herpesvirus tegument protein homology #label !8HTP SUMMARY #length 102 #molecular-weight 11436 #checksum 3971 SEQUENCE /// ENTRY GIBEPR #type complete TITLE tegument protein - suid herpesvirus 1 (strain Rice) ORGANISM #formal_name suid herpesvirus 1 #note host Sus scrofa domestica (domestic pig) DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 16-Jul-1999 ACCESSIONS A27815 REFERENCE A27815 !$#authors Petrovskis, E.A.; Post, L.E. !$#journal Virology (1987) 159:193-195 !$#title A small open reading frame in pseudorabies virus and !1implications for evolutionary relationships between !1herpesviruses. !$#cross-references MUID:87265472; PMID:3037781 !$#accession A27815 !'##molecule_type DNA !'##residues 1-106 ##label PET !'##cross-references GB:M16769; NID:g334041; PIDN:AAA47462.1; !1PID:g334042 CLASSIFICATION #superfamily human herpesvirus tegument protein; herpesvirus !1tegument protein homology FEATURE !$48-100 #domain herpesvirus tegument protein homology #label !8HTP SUMMARY #length 106 #molecular-weight 11377 #checksum 8866 SEQUENCE /// ENTRY A46113 #type complete TITLE tegument protein - cercopithecine herpesvirus 9 (strain DHV) ORGANISM #formal_name cercopithecine herpesvirus 9 DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS A46113 REFERENCE A46113 !$#authors Fletcher III, T.M.; Gray, W.L. !$#journal Virology (1993) 193:762-773 !$#title DNA sequence and genetic organization of the unique short !1(Us) region of the simian varicella virus genome. !$#cross-references MUID:93212509; PMID:8384754 !$#accession A46113 !'##molecule_type DNA !'##residues 1-77 ##label FLE !'##cross-references GB:L07067; NID:g310715; PIDN:AAA47886.1; !1PID:g310716 CLASSIFICATION #superfamily human herpesvirus tegument protein; herpesvirus !1tegument protein homology FEATURE !$39-77 #domain herpesvirus tegument protein homology #status !8atypical #label HTP SUMMARY #length 77 #molecular-weight 8997 #checksum 2954 SEQUENCE /// ENTRY TEBE12 #type complete TITLE tegument protein - equine herpesvirus 1 (subtype 2) ORGANISM #formal_name equine herpesvirus 1 DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jun-2000 ACCESSIONS B28134 REFERENCE A28134 !$#authors Cullinane, A.A.; Rixon, F.J.; Davison, A.J. !$#journal J. Gen. Virol. (1988) 69:1575-1590 !$#title Characterization of the genome of equine herpesvirus 1 !1subtype 2. !$#cross-references MUID:88274328; PMID:2839595 !$#accession B28134 !'##molecule_type DNA !'##residues 1-220 ##label CUL !'##cross-references GB:D00318; NID:g221815; PIDN:BAA00219.1; !1PID:g221817 CLASSIFICATION #superfamily equine herpesvirus tegument protein; !1herpesvirus tegument protein homology FEATURE !$161-213 #domain herpesvirus tegument protein homology #label !8HTP SUMMARY #length 220 #molecular-weight 22922 #checksum 6598 SEQUENCE /// ENTRY TEBEG6 #type complete TITLE tegument protein - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS D36803 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession D36803 !'##molecule_type DNA !'##residues 1-219 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02511.1; !1PID:g330867 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given CLASSIFICATION #superfamily equine herpesvirus tegument protein; !1herpesvirus tegument protein homology FEATURE !$160-212 #domain herpesvirus tegument protein homology #label !8HTP SUMMARY #length 219 #molecular-weight 22418 #checksum 5316 SEQUENCE /// ENTRY TEBEKA #type complete TITLE tegument protein - equine herpesvirus 1 (strain Kentucky A) ALTERNATE_NAMES ORF5 protein ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS A43378; PQ0147 REFERENCE A43378 !$#authors Flowers, C.C.; O'Callaghan, D.J. !$#journal Virology (1992) 190:307-315 !$#title The equine herpesvirus type 1 (EHV-1) homolog of herpes !1simplex virus type 1 US9 and the nature of a major deletion !1within the unique short segment of the EHV-1 KyA strain !1genome. !$#cross-references MUID:92410608; PMID:1326805 !$#accession A43378 !'##molecule_type DNA !'##residues 1-219 ##label FLO !'##cross-references GB:M86931; NID:g330935; PIDN:AAA46105.1; !1PID:g330936 REFERENCE JQ0998 !$#authors Elton, D.M.; Halliburton, I.W.; Killington, R.A.; Meredith, !1D.M.; Bonass, W.A. !$#journal Gene (1991) 101:203-208 !$#title Sequence analysis of the 4.7-kb BamHI-EcoRI fragment of the !1equine herpesvirus type-1 short unique region. !$#cross-references MUID:91276272; PMID:1647359 !$#accession PQ0147 !'##molecule_type DNA !'##residues 1-76 ##label ELT !'##cross-references GB:M36299 CLASSIFICATION #superfamily equine herpesvirus tegument protein; !1herpesvirus tegument protein homology FEATURE !$160-212 #domain herpesvirus tegument protein homology #label !8HTP SUMMARY #length 219 #molecular-weight 22358 #checksum 5498 SEQUENCE /// ENTRY TEBEHC #type complete TITLE tegument protein - human cytomegalovirus ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 16-Jul-1999 ACCESSIONS A25316 REFERENCE A25316 !$#authors Davis, M.G.; Huang, E.S. !$#journal J. Virol. (1985) 56:7-11 !$#title Nucleotide sequence of a human cytomegalovirus DNA fragment !1encoding a 67-kilodalton phosphorylated viral protein. !$#cross-references MUID:85293251; PMID:2993668 !$#accession A25316 !'##molecule_type DNA !'##residues 1-549 ##label DAV !'##cross-references GB:M11911; NID:g330633; PIDN:AAA45986.1; !1PID:g330634 !'##note the authors translated the codon TAC for residue 139 as Thr and !1AGG for residue 446 as Lys COMMENT The tegument is a granular zone surrounding the capsid. COMMENT This viral structural protein may have important functions, !1such as protein kinase activity, DNA binding, and possible !1transcriptional activation of immediate-early genes. GENETICS !$#map_position 0.37-0.39 CLASSIFICATION #superfamily cytomegalovirus tegument protein KEYWORDS DNA binding SUMMARY #length 549 #molecular-weight 61577 #checksum 8963 SEQUENCE /// ENTRY VGBEGX #type complete TITLE secreted glycoprotein gX - suid herpesvirus 1 ORGANISM #formal_name suid herpesvirus 1 DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 16-Jul-1999 ACCESSIONS A21879 REFERENCE A21879 !$#authors Rea, T.J.; Timmins, J.G.; Long, G.W.; Post, L.E. !$#journal J. Virol. (1985) 54:21-29 !$#title Mapping and sequence of the gene for the pseudorabies virus !1glycoprotein which accumulates in the medium of infected !1cells. !$#cross-references MUID:85135070; PMID:2983115 !$#accession A21879 !'##molecule_type DNA !'##residues 1-498 ##label REA !'##cross-references GB:M10986; NID:g334060; PIDN:AAC35206.1; !1PID:g334061 CLASSIFICATION #superfamily pseudorabies virus glycoprotein gX KEYWORDS glycoprotein FEATURE !$56,86,142,226,443 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 498 #molecular-weight 53721 #checksum 6721 SEQUENCE /// ENTRY VGBEG2 #type complete TITLE glycoprotein G precursor - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS G36802 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession G36802 !'##molecule_type DNA !'##residues 1-411 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02505.1; !1PID:g330861 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 70 CLASSIFICATION #superfamily pseudorabies virus glycoprotein gX KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-411 #product glycoprotein G #status predicted #label MAT\ !$363-379 #domain transmembrane #status predicted #label TMN\ !$83,138,222,245,317, !$392 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 411 #molecular-weight 45269 #checksum 2696 SEQUENCE /// ENTRY VGBEKA #type complete TITLE glycoprotein gX precursor - equine herpesvirus 1 (strain Kentucky A) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS B42538 REFERENCE A42538 !$#authors Colle III, C.F.; Flowers, C.C.; O'Callaghan, D.J. !$#journal Virology (1992) 188:545-557 !$#title Open reading frames encoding a protein kinase, homolog of !1glycoprotein gX of pseudorabies virus, and a novel !1glycoprotein map within the unique short segment of equine !1herpesvirus type 1. !$#cross-references MUID:92263758; PMID:1316673 !$#accession B42538 !'##molecule_type DNA !'##residues 1-373 ##label COL !'##cross-references GB:M87497; NID:g330878; PIDN:AAA46071.1; !1PID:g330881 CLASSIFICATION #superfamily pseudorabies virus glycoprotein gX KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-373 #product glycoprotein gX #status predicted #label !8GGX\ !$353-369 #domain transmembrane #status predicted #label TMN\ !$83,138,222,245,317 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 373 #molecular-weight 40954 #checksum 7609 SEQUENCE /// ENTRY VGBEGF #type complete TITLE glycoprotein G precursor - equine herpesvirus 4 (strain 405/ 76) ORGANISM #formal_name equine herpesvirus 4 #note host equus caballus (domestic horse) DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS A43375; D48338 REFERENCE A43375 !$#authors Crabb, B.S.; Nagesha, H.S.; Studdert, M.J. !$#journal Virology (1992) 190:143-154 !$#title Identification of equine herpesvirus 4 glycoprotein G: a !1type-specific, secreted glycoprotein. !$#cross-references MUID:92410589; PMID:1529525 !$#accession A43375 !'##molecule_type DNA !'##residues 1-405 ##label CRA !'##cross-references GB:S44796; NID:g255461; PIDN:AAB23267.1; !1PID:g255462 REFERENCE A48338 !$#authors Nagesha, H.S.; Crabb, B.S.; Studdert, M.J. !$#journal Arch. Virol. (1993) 128:143-154 !$#title Analysis of the nucleotide sequence of five genes at the !1left end of the unique short region of the equine !1herpesvirus 4 genome. !$#cross-references MUID:93119267; PMID:8380320 !$#accession D48338 !'##molecule_type DNA !'##residues 1-405 ##label NAG !'##cross-references GB:M89634; NID:g330929; PIDN:AAA46103.1; !1PID:g330933 !'##note sequence extracted from NCBI backbone (NCBIN:121741, !1NCBIP:121745) CLASSIFICATION #superfamily pseudorabies virus glycoprotein gX KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-405 #product glycoprotein G #status predicted #label GPG\ !$389-405 #domain transmembrane #status predicted #label TMN\ !$83,138,174,221,288 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 405 #molecular-weight 44803 #checksum 3385 SEQUENCE /// ENTRY VGBEX1 #type complete TITLE glycoprotein X precursor - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS H36802 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession H36802 !'##molecule_type DNA !'##residues 1-797 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02506.1; !1PID:g330862 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 71 CLASSIFICATION #superfamily equine herpesvirus glycoprotein X; equine !1herpesvirus 1 glycoprotein homology KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-797 #product glycoprotein X #status predicted #label MAT\ !$23-465 #region serine/threonine-rich\ !$489-797 #domain equine herpesvirus 1 glycoprotein homology !8#label EHG\ !$766-790 #domain transmembrane #status predicted #label TMN\ !$590 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 797 #molecular-weight 80342 #checksum 6547 SEQUENCE /// ENTRY VGBEKG #type complete TITLE glycoprotein precursor - equine herpesvirus 1 (strain Kentucky A) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS C42538 REFERENCE A42538 !$#authors Colle III, C.F.; Flowers, C.C.; O'Callaghan, D.J. !$#journal Virology (1992) 188:545-557 !$#title Open reading frames encoding a protein kinase, homolog of !1glycoprotein gX of pseudorabies virus, and a novel !1glycoprotein map within the unique short segment of equine !1herpesvirus type 1. !$#cross-references MUID:92263758; PMID:1316673 !$#accession C42538 !'##molecule_type DNA !'##residues 1-383 ##label COL !'##cross-references GB:M87497; NID:g330878; PIDN:AAA46072.1; !1PID:g330882 CLASSIFICATION #superfamily equine herpesvirus 1 glycoprotein; equine !1herpesvirus 1 glycoprotein homology KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-383 #product glycoprotein #status predicted #label GPT\ !$75-383 #domain equine herpesvirus 1 glycoprotein homology !8#label EHG\ !$354-371 #domain transmembrane #status predicted #label TMN\ !$48,128 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 383 #molecular-weight 41027 #checksum 9682 SEQUENCE /// ENTRY VGBE50 #type complete TITLE glycoprotein D precursor - suid herpesvirus 1 (strain Rice) ORGANISM #formal_name suid herpesvirus 1 #note host Sus scrofa domestica (domestic pig) DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jul-1999 ACCESSIONS A27788 REFERENCE A27788 !$#authors Petrovskis, E.A.; Timmins, J.G.; Armentrout, M.A.; !1Marchioli, C.C.; Yancey Jr., R.J.; Post, L.E. !$#journal J. Virol. (1986) 59:216-223 !$#title DNA sequence of the gene for pseudorabies virus gp50, a !1glycoprotein without N-linked glycosylation. !$#cross-references MUID:86281819; PMID:3016293 !$#accession A27788 !'##molecule_type DNA !'##residues 1-402 ##label PET !'##cross-references GB:M14001; NID:g334051; PIDN:AAC35203.1; !1PID:g334052 CLASSIFICATION #superfamily herpesvirus glycoprotein D KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-402 #product glycoprotein D #status predicted #label GPD\ !$362-378 #domain transmembrane #status predicted #label TMN SUMMARY #length 402 #molecular-weight 44501 #checksum 457 SEQUENCE /// ENTRY VGBED1 #type complete TITLE glycoprotein D - human herpesvirus 1 ORGANISM #formal_name human herpesvirus 1 DATE 05-Apr-1983 #sequence_revision 05-Apr-1983 #text_change 16-Jul-1999 ACCESSIONS A94268; B90945; A03729 REFERENCE A94268 !$#authors Watson, R.J.; Weis, J.H.; Salstrom, J.S.; Enquist, L.W. !$#journal Science (1982) 218:381-384 !$#title Herpes simplex virus type-1 glycoprotein D gene: nucleotide !1sequence and expression in Escherichia coli. !$#cross-references MUID:83016630; PMID:6289440 !$#accession A94268 !'##molecule_type DNA !'##residues 1-394 ##label WAT !'##cross-references GB:J02217; NID:g330100; PIDN:AAA45785.1; !1PID:g330101 !'##experimental_source strain Patton !'##note a strongly hydrophobic region of 25 amino acids between !1residues 340 and 364 is followed by a strongly basic region, !1which probably serves to anchor the glycoprotein in the !1membrane REFERENCE A90945 !$#authors Lasky, L.A.; Dowbenko, D.J. !$#journal DNA (1984) 3:23-29 !$#title DNA sequence analysis of the type-common glycoprotein-D !1genes of herpes simplex virus types 1 and 2. !$#cross-references MUID:84131549; PMID:6321120 !$#accession B90945 !'##molecule_type DNA !'##residues 1-3,'A',5-70,'N',72-83,85-269,'R',271-282,'P',284-364,'R', !1366-394 ##label LAS !'##experimental_source strain Hzt CLASSIFICATION #superfamily herpesvirus glycoprotein D KEYWORDS glycoprotein; transmembrane protein FEATURE !$119,146,287 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 394 #molecular-weight 43346 #checksum 7462 SEQUENCE /// ENTRY VGBEDZ #type complete TITLE glycoprotein D precursor - human herpesvirus 1 (strain Hzt) ORGANISM #formal_name human herpesvirus 1 DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 09-Sep-1994 ACCESSIONS A90945; A03729 REFERENCE A90945 !$#authors Lasky, L.A.; Dowbenko, D.J. !$#journal DNA (1984) 3:23-29 !$#title DNA sequence analysis of the type-common glycoprotein-D !1genes of herpes simplex virus types 1 and 2. !$#cross-references MUID:84131549; PMID:6321120 !$#accession A90945 !'##molecule_type DNA !'##residues 1-393 ##label LAS !'##cross-references GB:K02372 CLASSIFICATION #superfamily herpesvirus glycoprotein D KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-393 #product glycoprotein D #status predicted #label GPD\ !$341-360 #domain transmembrane #status predicted #label TMN\ !$118,145,286 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 393 #molecular-weight 43209 #checksum 3332 SEQUENCE /// ENTRY VGBE17 #type complete TITLE glycoprotein D precursor - human herpesvirus 1 (strain 17) ORGANISM #formal_name human herpesvirus 1 #note host Homo sapiens (man) DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 16-Jun-2000 ACCESSIONS A03730 REFERENCE A00656 !$#authors McGeoch, D.J.; Dolan, A.; Donald, S.; Rixon, F.J. !$#journal J. Mol. Biol. (1985) 181:1-13 !$#title Sequence determination and genetic content of the short !1unique region in the genome of herpes simplex virus type 1. !$#cross-references MUID:85160822; PMID:2984429 !$#accession A03730 !'##molecule_type DNA !'##residues 1-394 ##label MCG !'##cross-references GB:X14112; NID:g1944536; PIDN:CAA32283.1; !1PID:g59564 CLASSIFICATION #superfamily herpesvirus glycoprotein D KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-394 #product glycoprotein D #status predicted #label GPD\ !$342-358 #domain transmembrane #status predicted #label TMN\ !$119,146,287 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 394 #molecular-weight 43346 #checksum 8269 SEQUENCE /// ENTRY A47627 #type complete TITLE glycoprotein D precursor - human herpesvirus 1 (strain ANG) ORGANISM #formal_name human herpesvirus 1 DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS A47627 REFERENCE A47627 !$#authors Izumi, K.M.; Stevens, J.G. !$#journal J. Exp. Med. (1990) 172:487-496 !$#title Molecular and biological characterization of a herpes !1simplex virus type 1 (HSV-1) neuroinvasiveness gene. !$#cross-references MUID:90324869; PMID:2165127 !$#accession A47627 !'##molecule_type DNA !'##residues 1-394 ##label IZU !'##cross-references GB:X54361; NID:g60414; PIDN:CAA38245.1; PID:g60415 CLASSIFICATION #superfamily herpesvirus glycoprotein D KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-394 #product glycoprotein D #status predicted #label GPD\ !$342-360 #domain transmembrane #status predicted #label TMN\ !$119,146,287 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 394 #molecular-weight 43303 #checksum 8030 SEQUENCE /// ENTRY VGBED2 #type complete TITLE glycoprotein D - human herpesvirus 2 ORGANISM #formal_name human herpesvirus 2 DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 16-Jul-1999 ACCESSIONS A03731 REFERENCE A90945 !$#authors Lasky, L.A.; Dowbenko, D.J. !$#journal DNA (1984) 3:23-29 !$#title DNA sequence analysis of the type-common glycoprotein-D !1genes of herpes simplex virus types 1 and 2. !$#cross-references MUID:84131549; PMID:6321120 !$#accession A03731 !'##molecule_type DNA !'##residues 1-393 ##label LAS !'##cross-references GB:K02373; NID:g330270; PIDN:AAA45842.1; !1PID:g330271 CLASSIFICATION #superfamily herpesvirus glycoprotein D KEYWORDS glycoprotein; transmembrane protein FEATURE !$119,146,287 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 393 #molecular-weight 43147 #checksum 713 SEQUENCE /// ENTRY VGBE33 #type complete TITLE glycoprotein D precursor - human herpesvirus 2 (strain 333) ORGANISM #formal_name human herpesvirus 2 #note host Homo sapiens (man) DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 16-Jul-1999 ACCESSIONS A03732 REFERENCE A03732 !$#authors Watson, R.J. !$#journal Gene (1983) 26:307-312 !$#title DNA sequence of the herpes simplex virus type 2 glycoprotein !1D gene. !$#cross-references MUID:84159516; PMID:6323270 !$#accession A03732 !'##molecule_type DNA !'##residues 1-393 ##label WAT !'##cross-references GB:K01408; NID:g330268; PIDN:AAA45841.1; !1PID:g330269 CLASSIFICATION #superfamily herpesvirus glycoprotein D KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-393 #product glycoprotein D #status predicted #label GPD\ !$340-356 #domain transmembrane #status predicted #label TMN\ !$119,146,287 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 393 #molecular-weight 43163 #checksum 698 SEQUENCE /// ENTRY JQ1746 #type complete TITLE glycoprotein D precursor - cercopithecine herpesvirus 1 ORGANISM #formal_name cercopithecine herpesvirus 1 DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS JQ1746 REFERENCE JQ1745 !$#authors Bennett, A.M.; Harrington, L.; Kelly, D.C. !$#journal J. Gen. Virol. (1992) 73:2963-2967 !$#title Nucleotide sequence analysis of genes encoding glycoproteins !1D and J in simian herpes B virus. !$#cross-references MUID:93057369; PMID:1331298 !$#accession JQ1746 !'##molecule_type DNA !'##residues 1-395 ##label BEN !'##cross-references GB:S48101; NID:g259588; PIDN:AAB24129.1; !1PID:g259590 CLASSIFICATION #superfamily herpesvirus glycoprotein D KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-395 #product glycoprotein D #status predicted #label GPD\ !$343-362 #domain transmembrane #status predicted #label TMN\ !$119,287 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 395 #molecular-weight 42643 #checksum 8753 SEQUENCE /// ENTRY VGBE67 #type complete TITLE glycoprotein D precursor - human herpesvirus 3 ALTERNATE_NAMES glycoprotein IV ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS F27345 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession F27345 !'##molecule_type DNA !'##residues 1-354 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27950.1; !1PID:g60056 GENETICS !$#gene 67 CLASSIFICATION #superfamily herpesvirus glycoprotein D KEYWORDS glycoprotein; phosphoprotein; transmembrane protein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-354 #product glycoprotein D #status predicted #label GPD\ !$279-295 #domain transmembrane #status predicted #label TMN\ !$33,47,67,116 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 354 #molecular-weight 39364 #checksum 7590 SEQUENCE /// ENTRY VGBEIB #type complete TITLE glycoprotein D precursor - bovine herpesvirus 1 (strain P8-2) ORGANISM #formal_name bovine herpesvirus 1 DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jul-1999 ACCESSIONS A36548 REFERENCE A36548 !$#authors Tikoo, S.K.; Fitzpatrick, D.R.; Babiuk, L.A.; Zamb, T.J. !$#journal J. Virol. (1990) 64:5132-5142 !$#title Molecular cloning, sequencing, and expression of functional !1bovine herpesvirus 1 glycoprotein gIV in transfected bovine !1cells. !$#cross-references MUID:90376470; PMID:2168991 !$#accession A36548 !'##molecule_type DNA !'##residues 1-417 ##label TIK !'##cross-references GB:M59846; NID:g330745; PIDN:AAA46050.1; !1PID:g330746 CLASSIFICATION #superfamily herpesvirus glycoprotein D KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-417 #product glycoprotein D #status predicted #label MAT\ !$361-389 #domain transmembrane #status predicted #label TMN\ !$41,102 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 417 #molecular-weight 44924 #checksum 8801 SEQUENCE /// ENTRY VGBEEA #type complete TITLE glycoprotein D precursor - equine herpesvirus 1 (strain Kentucky A) ORGANISM #formal_name equine herpesvirus 1 DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jul-1999 ACCESSIONS A38518 REFERENCE A38518 !$#authors Flowers, C.C.; Eastman, E.M.; O'Callaghan, D.J. !$#journal Virology (1991) 180:175-184 !$#title Sequence analysis of a glycoprotein D gene homolog within !1the unique short segment of the EHV-1 genome. !$#cross-references MUID:91082407; PMID:1845821 !$#accession A38518 !'##molecule_type DNA !'##residues 1-442 ##label FLO !'##cross-references EMBL:M62923; NID:g330892; PIDN:AAA46081.1; !1PID:g330893 CLASSIFICATION #superfamily herpesvirus glycoprotein D KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-442 #product glycoprotein D #status predicted #label MAT\ !$404-422 #domain transmembrane #status predicted #label TM2\ !$103,111,347,396 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 442 #molecular-weight 49907 #checksum 1030 SEQUENCE /// ENTRY VGBEG3 #type complete TITLE glycoprotein D precursor - equine herpesvirus 1 ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS I36802; B36646; PQ0146 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession I36802 !'##molecule_type DNA !'##residues 1-452 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02507.1; !1PID:g330863 !'##experimental_source strain Ab4p REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given REFERENCE A36646 !$#authors Audonnet, J.C.; Winslow, J.; Allen, G.; Paoletti, E. !$#journal J. Gen. Virol. (1990) 71:2969-2978 !$#title Equine herpesvirus type 1 unique short fragment encodes !1glycoproteins with homology to herpes simplex virus type 1 !1gD, gI and gE. !$#cross-references MUID:91108393; PMID:2177089 !$#accession B36646 !'##molecule_type DNA !'##residues 1-452 ##label AUD !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02507.1; !1PID:g330863 !'##experimental_source strain Kentucky D REFERENCE JQ0998 !$#authors Elton, D.M.; Halliburton, I.W.; Killington, R.A.; Meredith, !1D.M.; Bonass, W.A. !$#journal Gene (1991) 101:203-208 !$#title Sequence analysis of the 4.7-kb BamHI-EcoRI fragment of the !1equine herpesvirus type-1 short unique region. !$#cross-references MUID:91276272; PMID:1647359 !$#accession PQ0146 !'##molecule_type DNA !'##residues 292-452 ##label ELT !'##cross-references GB:M36299; NID:g330787; PIDN:AAA66546.1; !1PID:g808672 GENETICS !$#gene 72 CLASSIFICATION #superfamily herpesvirus glycoprotein D KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-452 #product glycoprotein D #status predicted #label MAT\ !$399-419 #domain hydrophobic #label HYD\ !$404-422 #domain transmembrane #status predicted #label TM2\ !$103,111,347,396 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$347,396 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 452 #molecular-weight 51099 #checksum 9427 SEQUENCE /// ENTRY C46113 #type complete TITLE glycoprotein D precursor - cercopithecine herpesvirus 9 (strain DHV) ALTERNATE_NAMES membrane glycoprotein 1 ORGANISM #formal_name cercopithecine herpesvirus 9 DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS C46113 REFERENCE A46113 !$#authors Fletcher III, T.M.; Gray, W.L. !$#journal Virology (1993) 193:762-773 !$#title DNA sequence and genetic organization of the unique short !1(Us) region of the simian varicella virus genome. !$#cross-references MUID:93212509; PMID:8384754 !$#accession C46113 !'##molecule_type DNA !'##residues 1-353 ##label FLE !'##cross-references GB:L07067; NID:g310715; PIDN:AAA47888.1; !1PID:g310718 CLASSIFICATION #superfamily herpesvirus glycoprotein D KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-353 #product glycoprotein D #status predicted #label GPD\ !$275-293 #domain transmembrane #status predicted #label TMN\ !$40,75,84,122,138, !$227,252 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 353 #molecular-weight 40470 #checksum 7032 SEQUENCE /// ENTRY VGBEGI #type complete TITLE glycoprotein E - suid herpesvirus 1 ORGANISM #formal_name suid herpesvirus 1 #note host Sus scrofa domestica (domestic pig) DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jul-1999 ACCESSIONS B29012 REFERENCE A93021 !$#authors Petrovskis, E.A.; Timmins, J.G.; Post, L.E. !$#journal J. Virol. (1986) 60:185-193 !$#title Use of lambda-gt11 to isolate genes for two pseudorabies !1virus glycoproteins with homology to herpes simplex virus !1and varicella-zoster virus glycoproteins. !$#cross-references MUID:86308235; PMID:3018284 !$#accession B29012 !'##molecule_type DNA !'##residues 1-577 ##label PET !'##cross-references GB:M14336; NID:g334055; PIDN:AAC35205.1; !1PID:g334057 !'##experimental_source strain Rice CLASSIFICATION #superfamily herpesvirus glycoprotein E KEYWORDS glycoprotein FEATURE !$87,93,185,258,343 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 577 #molecular-weight 62325 #checksum 3581 SEQUENCE /// ENTRY VGBE18 #type complete TITLE glycoprotein E - human herpesvirus 1 ALTERNATE_NAMES US8 ORGANISM #formal_name human herpesvirus 1 DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 16-Jul-1999 ACCESSIONS A03733; A45696 REFERENCE A00656 !$#authors McGeoch, D.J.; Dolan, A.; Donald, S.; Rixon, F.J. !$#journal J. Mol. Biol. (1985) 181:1-13 !$#title Sequence determination and genetic content of the short !1unique region in the genome of herpes simplex virus type 1. !$#cross-references MUID:85160822; PMID:2984429 !$#accession A03733 !'##molecule_type DNA !'##residues 1-550 ##label MCG !'##cross-references GB:X02138; NID:g59865; PIDN:CAA26062.1; PID:g59882 !'##experimental_source strain 17 REFERENCE A45696 !$#authors Georgopoulou, U.; Michaelidou, A.; Roizman, B.; !1Mavromara-Nazos, P. !$#journal J. Virol. (1993) 67:3961-3968 !$#title Identification of a new transcriptional unit that yields a !1gene product within the unique sequences of the short !1component of the herpes simplex virus 1 genome. !$#cross-references MUID:93287213; PMID:8389914 !$#accession A45696 !'##status preliminary !'##molecule_type DNA !'##residues 438-550 ##label GEO !'##cross-references GB:S62895; NID:g386127; PIDN:AAB27080.1; !1PID:g386128 !'##experimental_source R35 !'##note sequence extracted from NCBI backbone (NCBIN:133646, !1NCBIP:133647) CLASSIFICATION #superfamily herpesvirus glycoprotein E KEYWORDS glycoprotein FEATURE !$124,243,501 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 550 #molecular-weight 59093 #checksum 2163 SEQUENCE /// ENTRY VGBE2E #type fragment TITLE glycoprotein E - equine herpesvirus 1 (subtype 2) (fragment) ORGANISM #formal_name equine herpesvirus 1 DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jun-2000 ACCESSIONS A28134 REFERENCE A28134 !$#authors Cullinane, A.A.; Rixon, F.J.; Davison, A.J. !$#journal J. Gen. Virol. (1988) 69:1575-1590 !$#title Characterization of the genome of equine herpesvirus 1 !1subtype 2. !$#cross-references MUID:88274328; PMID:2839595 !$#accession A28134 !'##molecule_type DNA !'##residues 1-255 ##label CUL !'##cross-references GB:D00318; NID:g221815; PIDN:BAA00218.1; !1PID:g221816 CLASSIFICATION #superfamily herpesvirus glycoprotein E KEYWORDS glycoprotein FEATURE !$111-130 #domain transmembrane #status predicted #label TRM SUMMARY #length 255 #checksum 8935 SEQUENCE /// ENTRY VGBEKD #type complete TITLE glycoprotein E precursor - equine herpesvirus 1 (strain Kentucky D) ORGANISM #formal_name equine herpesvirus 1 DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 09-Sep-1994 ACCESSIONS D36646 REFERENCE A36646 !$#authors Audonnet, J.C.; Winslow, J.; Allen, G.; Paoletti, E. !$#journal J. Gen. Virol. (1990) 71:2969-2978 !$#title Equine herpesvirus type 1 unique short fragment encodes !1glycoproteins with homology to herpes simplex virus type 1 !1gD, gI and gE. !$#cross-references MUID:91108393; PMID:2177089 !$#accession D36646 !'##molecule_type DNA !'##residues 1-552 ##label AUD CLASSIFICATION #superfamily herpesvirus glycoprotein E KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-552 #product glycoprotein E #status predicted #label MAT\ !$411-427 #domain transmembrane #status predicted #label TMN\ !$47,122,243,293 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 552 #molecular-weight 61493 #checksum 9090 SEQUENCE /// ENTRY VGBEG5 #type complete TITLE glycoprotein E precursor - equine herpesvirus 1 (strains Ab4p and Abl) ALTERNATE_NAMES hypothetical 61K protein; ORF3 protein ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS B36803; B61162; JQ0999 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession B36803 !'##molecule_type DNA !'##residues 1-550 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02509.1; !1PID:g330865 !'##experimental_source strain Ab4p REFERENCE A61162 !$#authors Elton, D.M.; Bonass, W.A.; Killington, R.A.; Meredith, D.M.; !1Halliburton, I.W. !$#journal Am. J. Vet. Res. (1991) 52:1252-1257 !$#title Location of open reading frames coding for equine !1herpesvirus type-1 glycoproteins with homology to gE and gI !1of herpes simplex virus. !$#cross-references MUID:92027094; PMID:1656822 !$#accession B61162 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type DNA !'##residues 185-357 ##label EL2 !'##experimental_source strain Abl !'##note translation of nucleotide sequence is not complete REFERENCE JQ0998 !$#authors Elton, D.M.; Halliburton, I.W.; Killington, R.A.; Meredith, !1D.M.; Bonass, W.A. !$#journal Gene (1991) 101:203-208 !$#title Sequence analysis of the 4.7-kb BamHI-EcoRI fragment of the !1equine herpesvirus type-1 short unique region. !$#cross-references MUID:91276272; PMID:1647359 !$#accession JQ0999 !'##molecule_type DNA !'##residues 1-550 ##label ELT !'##cross-references GB:M36299; NID:g330787; PIDN:AAA66548.1; !1PID:g330789 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 74 CLASSIFICATION #superfamily herpesvirus glycoprotein E KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-550 #product glycoprotein E #status predicted #label MAT\ !$409-425 #domain transmembrane #status predicted #label TM1\ !$47,109,122,241,291 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 550 #molecular-weight 61182 #checksum 299 SEQUENCE /// ENTRY VGBE68 #type complete TITLE glycoprotein E - human herpesvirus 3 ALTERNATE_NAMES glycoprotein gI ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS G27345 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession G27345 !'##molecule_type DNA !'##residues 1-623 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27951.1; !1PID:g60057 GENETICS !$#gene 68 CLASSIFICATION #superfamily herpesvirus glycoprotein E KEYWORDS glycoprotein FEATURE !$266,327,437,577 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 623 #molecular-weight 69956 #checksum 7163 SEQUENCE /// ENTRY D46113 #type complete TITLE glycoprotein E precursor - cercopithecine herpesvirus 9 (strain DHV) ALTERNATE_NAMES membrane glycoprotein 2 ORGANISM #formal_name cercopithecine herpesvirus 9 DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS D46113 REFERENCE A46113 !$#authors Fletcher III, T.M.; Gray, W.L. !$#journal Virology (1993) 193:762-773 !$#title DNA sequence and genetic organization of the unique short !1(Us) region of the simian varicella virus genome. !$#cross-references MUID:93212509; PMID:8384754 !$#accession D46113 !'##molecule_type DNA !'##residues 1-604 ##label FLE !'##cross-references GB:L07067; NID:g310715; PIDN:AAA47889.1; !1PID:g310719 CLASSIFICATION #superfamily herpesvirus glycoprotein E KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-604 #product glycoprotein E #status predicted #label MAT\ !$527-544 #domain transmembrane #status predicted #label TM1\ !$117,249,303,419,505 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 604 #molecular-weight 67583 #checksum 5026 SEQUENCE /// ENTRY VGBEF2 #type complete TITLE glycoprotein F - human herpesvirus 2 ORGANISM #formal_name human herpesvirus 2 DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 28-May-1999 ACCESSIONS A03734 REFERENCE A03734 !$#authors Dowbenko, D.J.; Lasky, L.A. !$#journal J. Virol. (1984) 52:154-163 !$#title Extensive homology between the herpes simplex virus type 2 !1glycoprotein F gene and the herpes simplex virus type 1 !1glycoprotein C gene. !$#cross-references MUID:85009847; PMID:6090692 !$#accession A03734 !'##molecule_type DNA !'##residues 1-479 ##label DOW !'##cross-references GB:X01456; GB:K02721; NID:g59892; PIDN:CAA25687.1; !1PID:g59893 !'##note the authors translated the codon ACC for residue 9 as Ala CLASSIFICATION #superfamily herpesvirus glycoprotein F KEYWORDS glycoprotein FEATURE !$40,51,116,149,165, !$330 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 479 #molecular-weight 51667 #checksum 6570 SEQUENCE /// ENTRY VGBEF4 #type complete TITLE glycoprotein C - human herpesvirus 1 (strain 17) ORGANISM #formal_name human herpesvirus 1 DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jun-2000 ACCESSIONS H30088 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession H30088 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-511 ##label MCG !'##cross-references GB:X14112; NID:g1944536; PIDN:CAA32294.1; !1PID:g59544; GB:D00317 GENETICS !$#gene UL44 CLASSIFICATION #superfamily herpesvirus glycoprotein F KEYWORDS glycoprotein; transmembrane protein FEATURE !$42,70,74,108,109, !$148,181,197,362 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 511 #molecular-weight 54998 #checksum 6880 SEQUENCE /// ENTRY VGBE1K #type complete TITLE glycoprotein C - human herpesvirus 1 (strain KOS) ORGANISM #formal_name human herpesvirus 1 DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS A20857 REFERENCE A20857 !$#authors Frink, R.J.; Eisenberg, R.; Cohen, G.; Wagner, E.K. !$#journal J. Virol. (1983) 45:634-647 !$#title Detailed analysis of the portion of the herpes simplex virus !1type 1 genome encoding glycoprotein C. !$#cross-references MUID:83164308; PMID:6300426 !$#accession A20857 !'##molecule_type DNA !'##residues 1-511 ##label FRI !'##cross-references GB:J02216; NID:g330091; PIDN:AAA45779.1; !1PID:g330092 CLASSIFICATION #superfamily herpesvirus glycoprotein F KEYWORDS glycoprotein; transmembrane protein FEATURE !$481-497 #domain transmembrane #status predicted #label TMN\ !$42,70,74,108,109, !$148,181,197,362 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 511 #molecular-weight 55011 #checksum 6197 SEQUENCE /// ENTRY VGBEPB #type complete TITLE glycoprotein gIII precursor - suid herpesvirus 1 ORGANISM #formal_name suid herpesvirus 1 DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Jul-1999 ACCESSIONS A26097 REFERENCE A26097 !$#authors Robbins, A.K.; Watson, R.J.; Whealy, M.E.; Hays, W.W.; !1Enquist, L.W. !$#journal J. Virol. (1986) 58:339-347 !$#title Characterization of a Pseudorabies virus glycoprotein gene !1with homology to herpes simplex virus type 1 and type 2 !1glycoprotein C. !$#cross-references MUID:86200375; PMID:3009851 !$#accession A26097 !'##molecule_type DNA !'##residues 1-479 ##label ROB !'##cross-references GB:M12778; NID:g334049; PIDN:AAA47464.1; !1PID:g334050 !'##experimental_source strain Becker CLASSIFICATION #superfamily herpesvirus glycoprotein F KEYWORDS glycoprotein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-479 #product glycoprotein gIII #status predicted #label !8GPG\ !$40,84,169,192,220, !$228,285,302 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 479 #molecular-weight 51206 #checksum 1630 SEQUENCE /// ENTRY VGBEHB #type complete TITLE glycoprotein gIII precursor - bovine herpesvirus 1 (strain Cooper) ORGANISM #formal_name bovine herpesvirus 1 DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS A32593 REFERENCE A32593 !$#authors Fitzpatrick, D.R.; Babiuk, L.A.; Zamb, T.J. !$#journal Virology (1989) 173:46-57 !$#title Nucleotide sequence of bovine herpesvirus type 1 !1glycoprotein gIII, a structural model for gIII as a new !1member of the immunoglobulin superfamily, and implications !1for the homologous glycoproteins of other herpesviruses. !$#cross-references MUID:90051093; PMID:2554578 !$#accession A32593 !'##molecule_type DNA !'##residues 1-521 ##label FIT !'##cross-references GB:M27491; NID:g330754; PIDN:AAA46054.1; !1PID:g330755 CLASSIFICATION #superfamily herpesvirus glycoprotein F KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-521 #product glycoprotein gIII #status predicted #label !8GPG\ !$467-500 #domain transmembrane #status predicted #label TMN\ !$93,111,164,208 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 521 #molecular-weight 55384 #checksum 887 SEQUENCE /// ENTRY VGBE14 #type complete TITLE glycoprotein gpV - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS E27342 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession E27342 !'##molecule_type DNA !'##residues 1-560 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27897.1; !1PID:g60003 GENETICS !$#gene 14 CLASSIFICATION #superfamily herpesvirus glycoprotein F KEYWORDS glycoprotein FEATURE !$206,325,344,432,461 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 560 #molecular-weight 61352 #checksum 4781 SEQUENCE /// ENTRY VGBEEH #type complete TITLE glycoprotein gp13 precursor - equine herpesvirus 1 ALTERNATE_NAMES glycoprotein gC ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 24-Sep-1999 ACCESSIONS A28149; A32980; H36796 REFERENCE A28149 !$#authors Allen, G.P.; Coogle, L.D. !$#journal J. Virol. (1988) 62:2850-2858 !$#title Characterization of an equine herpesvirus type 1 gene !1encoding a glycoprotein (gp13) with homology to herpes !1simplex virus glycoprotein C. !$#cross-references MUID:88275055; PMID:2455821 !$#accession A28149 !'##molecule_type DNA !'##residues 1-468 ##label ALL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02451.1; !1PID:g330808 !'##experimental_source strain Kentucky T431 !'##note the authors translated the codon ACA for residue 43 as Pro REFERENCE A32980 !$#authors Guo, P.; Goebel, S.; Davis, S.; Perkus, M.E.; Languet, B.; !1Desmettre, P.; Allen, G.; Paoletti, E. !$#journal J. Virol. (1989) 63:4189-4198 !$#title Expression in recombinant vaccinia virus of the equine !1herpesvirus 1 gene encoding glycoprotein gp13 and protection !1of immunized animals. !$#cross-references MUID:89382761; PMID:2550665 !$#accession A32980 !'##molecule_type DNA !'##residues 1-468 ##label GUO !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02451.1; !1PID:g330808 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession H36796 !'##molecule_type DNA !'##residues 1-468 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02451.1; !1PID:g330808 !'##experimental_source strain Ab4p REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 16 CLASSIFICATION #superfamily herpesvirus glycoprotein F KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-30 #domain signal sequence #status predicted #label SIG\ !$31-468 #product glycoprotein gp13 #status predicted #label !8MAT\ !$46,57,62,92,100, !$131,203,208,269 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 468 #molecular-weight 50889 #checksum 3525 SEQUENCE /// ENTRY B46114 #type complete TITLE glycoprotein gp13 precursor - equine herpesvirus 1 (strain Kentucky A) ALTERNATE_NAMES glycoprotein C ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS B46114 REFERENCE A46114 !$#authors Matsumura, T.; Smith, R.H.; O'Callaghan, D.J. !$#journal Virology (1993) 193:910-923 !$#title DNA sequence and transcriptional analyses of the region of !1the equine herpesvirus type 1 Kentucky A strain genome !1encoding glycoprotein C. !$#cross-references MUID:93212524; PMID:8384760 !$#accession B46114 !'##molecule_type DNA !'##residues 1-468 ##label MAT !'##cross-references GB:S57839; NID:g298846; PIDN:AAB25944.1; !1PID:g298848 CLASSIFICATION #superfamily herpesvirus glycoprotein F KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-30 #domain signal sequence #status predicted #label SIG\ !$31-468 #product glycoprotein gp13 #status predicted #label !8GPT\ !$432-451 #domain transmembrane #status predicted #label TMN\ !$46,57,62,92,100, !$131,203,208,269 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 468 #molecular-weight 50859 #checksum 3024 SEQUENCE /// ENTRY B45343 #type complete TITLE glycoprotein gp13 precursor - equine herpesvirus 4 ALTERNATE_NAMES glycoprotein gC ORGANISM #formal_name equine herpesvirus 4 DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jul-1999 ACCESSIONS B45343 REFERENCE A45343 !$#authors Nicolson, L.; Onions, D.E. !$#journal Virology (1990) 179:378-387 !$#title The nucleotide sequence of the equine herpesvirus 4 gC gene !1homologue. !$#cross-references MUID:91021040; PMID:2171212 !$#accession B45343 !'##molecule_type DNA !'##residues 1-485 ##label NIC !'##cross-references GB:M58031; NID:g330894; PIDN:AAA46083.1; !1PID:g330896 GENETICS !$#gene 16 CLASSIFICATION #superfamily herpesvirus glycoprotein F KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-30 #domain signal sequence #status predicted #label SIG\ !$31-485 #product glycoprotein gp13 #status predicted #label !8GGP\ !$60,61,66,67,72,108, !$116,147,220,225,286 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 485 #molecular-weight 52509 #checksum 5788 SEQUENCE /// ENTRY VGBEMH #type complete TITLE glycoprotein gp57-65 precursor - Marek's disease virus ORGANISM #formal_name Marek's disease virus #note host Gallus gallus (chicken) DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS A28843 REFERENCE A28843 !$#authors Coussens, P.M.; Velicer, L.F. !$#journal J. Virol. (1988) 62:2373-2379 !$#title Structure and complete nucleotide sequence of the Marek's !1disease herpesvirus gp57-65 gene. !$#cross-references MUID:88230597; PMID:2836620 !$#accession A28843 !'##molecule_type DNA !'##residues 1-505 ##label COU !'##cross-references GB:M20001; NID:g330962; PIDN:AAA46114.1; !1PID:g330963 CLASSIFICATION #superfamily herpesvirus glycoprotein F KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-505 #product glycoprotein gp57-65 #status predicted !8#label GLC\ !$45,90,99,119,211, !$353,399,428,470 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 505 #molecular-weight 56809 #checksum 6438 SEQUENCE /// ENTRY VGBEMA #type complete TITLE glycoprotein A precursor - Marek's disease virus (type 1, strain BC-1) ALTERNATE_NAMES glycoprotein C ORGANISM #formal_name Marek's disease virus #note host Gallus gallus (chicken) DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 09-Sep-1994 ACCESSIONS JS0388 REFERENCE A22818 !$#authors Ihara, T.; Kato, A.; Ueda, S.; Ishihama, A.; Hirai, K. !$#journal Virus Genes (1989) 3:127-140 !$#title Comparison of the sequence of the secretory glycoprotein A !1(gA) gene between Md5 and BC-1 strains of Marek's disease !1virus type 1. !$#cross-references MUID:90142542; PMID:2559540 !$#accession JS0388 !'##molecule_type DNA !'##residues 1-501 ##label IHA CLASSIFICATION #superfamily herpesvirus glycoprotein F KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-501 #product glycoprotein A #status predicted #label GPA\ !$463-495 #domain transmembrane #status predicted #label TMN\ !$46,91,100,120,212, !$354,400,429 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 501 #molecular-weight 56134 #checksum 3973 SEQUENCE /// ENTRY VGBEMB #type complete TITLE glycoprotein A precursor - Marek's disease virus (type 1, strain Md5) ALTERNATE_NAMES glycoprotein C ORGANISM #formal_name Marek's disease virus #note host Gallus gallus (chicken) DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 09-Sep-1994 ACCESSIONS A22818 REFERENCE A22818 !$#authors Ihara, T.; Kato, A.; Ueda, S.; Ishihama, A.; Hirai, K. !$#journal Virus Genes (1989) 3:127-140 !$#title Comparison of the sequence of the secretory glycoprotein A !1(gA) gene between Md5 and BC-1 strains of Marek's disease !1virus type 1. !$#cross-references MUID:90142542; PMID:2559540 !$#accession A22818 !'##molecule_type DNA !'##residues 1-501 ##label IHA CLASSIFICATION #superfamily herpesvirus glycoprotein F KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-501 #product glycoprotein A #status predicted #label GPA\ !$463-495 #domain transmembrane #status predicted #label TMN\ !$46,91,100,120,212, !$354,400,429 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 501 #molecular-weight 56088 #checksum 4237 SEQUENCE /// ENTRY A60005 #type complete TITLE glycoprotein A precursor - Marek's disease virus (strain RB-1B) ALTERNATE_NAMES glycoprotein C ORGANISM #formal_name Marek's disease virus #note host Gallus gallus (chicken) DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 07-May-1999 ACCESSIONS A60005 REFERENCE A60005 !$#authors Binns, M.M.; Ross, N.L.J. !$#journal Virus Res. (1989) 12:371-382 !$#title Nucleotide sequence of the Marek's disease virus (MDV) RB-1B !1A antigen gene and the identification of the MDV A antigen !1as the herpes simplex virus-1 glycoprotein C homologue. !$#cross-references MUID:89269090; PMID:2543160 !$#accession A60005 !'##molecule_type DNA !'##residues 1-501 ##label BIN CLASSIFICATION #superfamily herpesvirus glycoprotein F KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-501 #product glycoprotein A #status predicted #label GPA\ !$463-492 #domain transmembrane #status predicted #label TMN\ !$46,91,100,120,212, !$354,400,429 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 501 #molecular-weight 56104 #checksum 4309 SEQUENCE /// ENTRY VGBETC #type complete TITLE glycoprotein A - turkey herpesvirus (strain FC126) ORGANISM #formal_name turkey herpesvirus #note host Meleagris gallopavo (common turkey) DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS JE0066; S06175 REFERENCE JE0066 !$#authors Bandyopadhyay, P.K. !$#journal Gene (1989) 79:361-367 !$#title Characterization of a highly transcribed DNA region of !1herpesvirus of turkeys. !$#cross-references MUID:90006765; PMID:2792768 !$#accession JE0066 !'##molecule_type mRNA !'##residues 1-373 ##label BAN !'##cross-references GB:M27832; GB:X13371; NID:g330942; PIDN:AAA46110.1; !1PID:g330943 CLASSIFICATION #superfamily herpesvirus glycoprotein F KEYWORDS glycoprotein FEATURE !$91,111,203,345 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 373 #molecular-weight 41597 #checksum 6895 SEQUENCE /// ENTRY VGBETA #type complete TITLE glycoprotein A - turkey herpesvirus (strain H2) ORGANISM #formal_name turkey herpesvirus #note host Meleagris gallopavo (common turkey) DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Feb-1997 ACCESSIONS JQ0162; JS0351 REFERENCE JQ0162 !$#authors Kato, A.; Sato, I.; Ihara, T.; Ueda, S.; Ishihama, A.; !1Hirai, K. !$#journal Gene (1989) 84:399-405 !$#title Homology between herpesvirus of turkey and Marek's disease !1virus type-1 DNAs within two co-linearly arranged open !1reading frames, one encoding glycoprotein A. !$#cross-references MUID:90128284; PMID:2558972 !$#accession JQ0162 !'##molecule_type DNA !'##residues 1-489 ##label KAT GENETICS !$#gene gA CLASSIFICATION #superfamily herpesvirus glycoprotein F KEYWORDS glycoprotein; transmembrane protein FEATURE !$92,112,204,346,392 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 489 #molecular-weight 54718 #checksum 7910 SEQUENCE /// ENTRY A60408 #type complete TITLE glycoprotein gp57-65 precursor - turkey herpesvirus (strain FC126) ORGANISM #formal_name turkey herpesvirus #note host Meleagris gallopavo (common turkey) DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 05-Jan-1996 ACCESSIONS A60408 REFERENCE A60408 !$#authors Coussens, P.M.; Wilson, M.R.; Camp, H.; Roehl, H.; Isfort, !1R.J.; Velicer, L.F. !$#journal Virus Genes (1990) 3:291-307 !$#title Characterization of the gene encoding herpesvirus of turkeys !1gp57-65: comparison to Marek's disease virus gp57-65 and !1herpes simplex virus glycoprotein C. !$#cross-references MUID:90273669; PMID:2161583 !$#accession A60408 !'##molecule_type DNA !'##residues 1-523 ##label COU CLASSIFICATION #superfamily herpesvirus glycoprotein F KEYWORDS glycoprotein; transmembrane protein FEATURE !$60-523 #product glycoprotein gp57-65 #status predicted !8#label GLC\ !$494-515 #domain transmembrane #status predicted #label TMN\ !$126,146,238,380,426 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 523 #molecular-weight 58587 #checksum 7475 SEQUENCE /// ENTRY WMBETA #type complete TITLE 23.5K protein - turkey herpesvirus (strain H2) ORGANISM #formal_name turkey herpesvirus #note host Meleagris gallopavo (common turkey) DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 08-Apr-1994 ACCESSIONS JQ0163; JS0352 REFERENCE JQ0162 !$#authors Kato, A.; Sato, I.; Ihara, T.; Ueda, S.; Ishihama, A.; !1Hirai, K. !$#journal Gene (1989) 84:399-405 !$#title Homology between herpesvirus of turkey and Marek's disease !1virus type-1 DNAs within two co-linearly arranged open !1reading frames, one encoding glycoprotein A. !$#cross-references MUID:90128284; PMID:2558972 !$#accession JQ0163 !'##molecule_type DNA !'##residues 1-212 ##label KAT CLASSIFICATION #superfamily turkey herpesvirus 23.5K protein KEYWORDS glycoprotein FEATURE !$97 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 212 #molecular-weight 23480 #checksum 5268 SEQUENCE /// ENTRY WMBEMA #type complete TITLE 23.5K protein - Marek's disease virus (type 1, strain BC-1) ORGANISM #formal_name Marek's disease virus #note host Gallus gallus (chicken) DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 08-Apr-1994 ACCESSIONS JS0389 REFERENCE A22818 !$#authors Ihara, T.; Kato, A.; Ueda, S.; Ishihama, A.; Hirai, K. !$#journal Virus Genes (1989) 3:127-140 !$#title Comparison of the sequence of the secretory glycoprotein A !1(gA) gene between Md5 and BC-1 strains of Marek's disease !1virus type 1. !$#cross-references MUID:90142542; PMID:2559540 !$#accession JS0389 !'##molecule_type DNA !'##residues 1-211 ##label IHA CLASSIFICATION #superfamily turkey herpesvirus 23.5K protein SUMMARY #length 211 #molecular-weight 23551 #checksum 9793 SEQUENCE /// ENTRY WMBEMB #type complete TITLE 23.5K protein - Marek's disease virus (type 1, strains Md5 and GA) ALTERNATE_NAMES UL45h protein ORGANISM #formal_name Marek's disease virus #note host Gallus gallus (chicken) DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS B22818; JQ2207 REFERENCE A22818 !$#authors Ihara, T.; Kato, A.; Ueda, S.; Ishihama, A.; Hirai, K. !$#journal Virus Genes (1989) 3:127-140 !$#title Comparison of the sequence of the secretory glycoprotein A !1(gA) gene between Md5 and BC-1 strains of Marek's disease !1virus type 1. !$#cross-references MUID:90142542; PMID:2559540 !$#accession B22818 !'##molecule_type DNA !'##residues 1-211 ##label IHA !'##experimental_source strain Md5 REFERENCE JQ2199 !$#authors Yanagida, N.; Yoshida, S.; Nazerian, K.; Lee, L.F. !$#journal J. Gen. Virol. (1993) 74:1837-1845 !$#title Nucleotide and predicted amino acid sequences of Marek's !1disease virus homologues of herpes simplex virus major !1tegument proteins. !$#cross-references MUID:93389438; PMID:8397281 !$#accession JQ2207 !'##molecule_type DNA !'##residues 1-211 ##label YAN !'##cross-references GB:L10283; NID:g388703; PIDN:AAA03152.1; !1PID:g388710 !'##experimental_source strain GA CLASSIFICATION #superfamily turkey herpesvirus 23.5K protein SUMMARY #length 211 #molecular-weight 23507 #checksum 382 SEQUENCE /// ENTRY WMBEAK #type complete TITLE 38K phosphoprotein - Marek's disease virus (strain GA) ORGANISM #formal_name Marek's disease virus DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS A40836 REFERENCE A40836 !$#authors Chen, X.; Sondermeijer, P.J.A.; Velicer, L.F. !$#journal J. Virol. (1992) 66:85-94 !$#title Identification of a unique Marek's disease virus gene which !1encodes a 38-kilodalton phosphoprotein and is expressed in !1both lytically infected cells and latently infected !1lymphoblastoid tumor cells. !$#cross-references MUID:92085442; PMID:1309266 !$#accession A40836 !'##molecule_type mRNA !'##residues 1-290 ##label CHE !'##cross-references GB:M73484; NID:g330956; PIDN:AAA46112.1; !1PID:g330957 !'##note the authors translated the codons TGG for residue 104 as Gln, !1and GAA for residue 121 as Ser CLASSIFICATION #superfamily turkey herpesvirus 1 38K phosphoprotein KEYWORDS phosphoprotein; transmembrane protein SUMMARY #length 290 #molecular-weight 31169 #checksum 688 SEQUENCE /// ENTRY WMBE1M #type complete TITLE 38K phosphoprotein - Marek's disease virus ORGANISM #formal_name Marek's disease virus DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS A41560; B48555 REFERENCE A41560 !$#authors Cui, Z.; Lee, L.F.; Liu, J.L.; Kung, H.J. !$#journal J. Virol. (1991) 65:6509-6515 !$#title Structural analysis and transcriptional mapping of the !1Marek's disease virus gene encoding pp38, an antigen !1associated with transformed cells. !$#cross-references MUID:92046309; PMID:1658357 !$#accession A41560 !'##molecule_type DNA !'##residues 1-290 ##label CUI !'##cross-references GB:M74036 !'##experimental_source strain Md11/75c/R2 REFERENCE A48555 !$#authors Ross, N.; Binns, M.M.; Sanderson, M.; Schat, K.A. !$#journal Virus Genes (1993) 7:33-51 !$#title Alterations in DNA sequence and RNA transcription of the Bam !1HI-H fragment accompany attenuation of oncogenic Marek's !1disease herpesvirus. !$#cross-references MUID:93227567; PMID:8385839 !$#accession B48555 !'##molecule_type DNA !'##residues 1-290 ##label ROS !'##cross-references GB:S58431; NID:g299456; PIDN:AAB26136.1; !1PID:g299458 !'##experimental_source strain HPRS16 !'##note sequence extracted from NCBI backbone (NCBIN:129299, !1NCBIP:129313) CLASSIFICATION #superfamily turkey herpesvirus 1 38K phosphoprotein KEYWORDS phosphoprotein; transmembrane protein SUMMARY #length 290 #molecular-weight 31097 #checksum 792 SEQUENCE /// ENTRY VGBEG1 #type complete TITLE glycoprotein H precursor - human herpesvirus 1 (strain 17) ORGANISM #formal_name human herpesvirus 1 DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jun-2000 ACCESSIONS A24018; D30084; B24187 REFERENCE A24018 !$#authors McGeoch, D.J.; Davison, A.J. !$#journal Nucleic Acids Res. (1986) 14:4281-4292 !$#title DNA sequence of the herpes simplex virus type 1 gene !1encoding glycoprotein gH, and identification of homologues !1in the genomes of varicella-zoster virus and Epstein-Barr !1virus. !$#cross-references MUID:86232558; PMID:3012465 !$#accession A24018 !'##molecule_type DNA !'##residues 1-838 ##label MCG !'##cross-references GB:X03896; NID:g59850; PIDN:CAA27534.1; PID:g59852 !'##note strain 17 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession D30084 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-838 ##label MC2 !'##cross-references GB:D10879; NID:g221721; PIDN:BAA01668.1; !1PID:g221743; GB:D00317 !'##note strain 17 REFERENCE A94342 !$#authors Gompels, U.; Minson, A. !$#journal Virology (1986) 153:230-247 !$#title The properties and sequence of glycoprotein H of herpes !1simplex virus type 1. !$#cross-references MUID:86291165; PMID:3016991 !$#accession B24187 !'##molecule_type DNA !'##residues 1-14,'A',16-137,'A',139-149,'T',151-283,'A',285-838 ##label !1GOM !'##cross-references GB:M14884; NID:g330213; PIDN:AAA45815.1; !1PID:g330216 !'##note strain HFEM GENETICS !$#gene UL22 CLASSIFICATION #superfamily herpesvirus glycoprotein H KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-838 #product glycoprotein H #status predicted #label GPH\ !$798-824 #domain transmembrane #status predicted #label TM2\ !$73,120,216,332,437, !$670,784 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 838 #molecular-weight 90365 #checksum 456 SEQUENCE /// ENTRY VGBE37 #type complete TITLE glycoprotein H - human herpesvirus 3 ALTERNATE_NAMES glycoprotein III ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS B27341 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession B27341 !'##molecule_type DNA !'##residues 1-841 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27920.1; !1PID:g60026 GENETICS !$#gene 37 CLASSIFICATION #superfamily herpesvirus glycoprotein H KEYWORDS glycoprotein FEATURE !$18,45,83,217,317, !$499,522,560,760,783 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 841 #molecular-weight 93651 #checksum 1938 SEQUENCE /// ENTRY VGBEPK #type complete TITLE glycoprotein H precursor - suid herpesvirus 1 (strain Ka) ORGANISM #formal_name suid herpesvirus 1 DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS A39990 REFERENCE A39990 !$#authors Klupp, B.G.; Mettenleiter, T.C. !$#journal Virology (1991) 182:732-741 !$#title Sequence and expression of the glycoprotein gH gene of !1pseudorabies virus. !$#cross-references MUID:91220723; PMID:1850925 !$#accession A39990 !'##molecule_type DNA !'##residues 1-686 ##label KLU !'##cross-references GB:M61196; NID:g334058; PIDN:AAA47466.1; !1PID:g334059 CLASSIFICATION #superfamily herpesvirus glycoprotein H KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-30 #domain signal sequence #status predicted #label SIG\ !$31-686 #product glycoprotein H #status predicted #label GPH\ !$647-667 #domain transmembrane #status predicted #label TMN\ !$77,162,542,604,627 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 686 #molecular-weight 71950 #checksum 5850 SEQUENCE /// ENTRY VGBENA #type complete TITLE glycoprotein H precursor - suid herpesvirus 1 (strain NIA-3) ORGANISM #formal_name suid herpesvirus 1 DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS A42000; S16737 REFERENCE A42000 !$#authors Peeters, B.; de Wind, N.; Broer, R.; Gielkens, A.; Moormann, !1R. !$#journal J. Virol. (1992) 66:3888-3892 !$#title Glycoprotein H of pseudorabies virus is essential for entry !1and cell-to-cell spread of the virus. !$#cross-references MUID:92260665; PMID:1316488 !$#accession A42000 !'##molecule_type DNA !'##residues 1-686 ##label PEE !'##cross-references GB:X61696; NID:g61352; PIDN:CAA43862.1; PID:g61353 CLASSIFICATION #superfamily herpesvirus glycoprotein H KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-30 #domain signal sequence #status predicted #label SIG\ !$31-686 #product glycoprotein H #status predicted #label GPH\ !$647-667 #domain transmembrane #status predicted #label TMN\ !$77,162,542,604,627 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 686 #molecular-weight 71832 #checksum 5392 SEQUENCE /// ENTRY VGBE41 #type complete TITLE glycoprotein H precursor - equine herpesvirus 4 ALTERNATE_NAMES envelope protein ORGANISM #formal_name equine herpesvirus 4 DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 21-Jul-2000 ACCESSIONS A36656; T42583 REFERENCE A36656 !$#authors Nicolson, L.; Cullinane, A.A.; Onions, D.E. !$#journal J. Gen. Virol. (1990) 71:1793-1800 !$#title The nucleotide sequence of an equine herpesvirus 4 gene !1homologue of the herpes simplex virus 1 glycoprotein H gene. !$#cross-references MUID:90362066; PMID:2167933 !$#accession A36656 !'##molecule_type DNA !'##residues 1-855 ##label NIC !'##cross-references GB:D14486; GB:D00683; NID:g221820; PIDN:BAA03379.1; !1PID:g221823 REFERENCE Z22173 !$#authors Telford, E.A.; Watson, M.S.; Perry, J.; Cullinane, A.A.; !1Davison, A.J. !$#journal J. Gen. Virol. (1998) 79:1197-1203 !$#title The DNA sequence of equine herpesvirus-4. !$#cross-references MUID:98264497; PMID:9603335 !$#accession T42583 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-855 ##label TEL !'##cross-references EMBL:AF030027; NID:g2605950; PIDN:AAC59556.1; !1PID:g2605984 !'##experimental_source strain NS80567 GENETICS !$#gene 39 CLASSIFICATION #superfamily herpesvirus glycoprotein H KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-855 #product glycoprotein H #status predicted #label MAT\ !$509-525 #domain transmembrane #status predicted #label TM1\ !$548-566 #domain transmembrane #status predicted #label TM2\ !$571-587 #domain transmembrane #status predicted #label TM3\ !$816-846 #domain transmembrane #status predicted #label TM4\ !$42,48,52,68,126, !$189,217,503,679, !$773,796 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 855 #molecular-weight 94085 #checksum 5430 SEQUENCE /// ENTRY VGBED3 #type complete TITLE glycoprotein H precursor - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 24-Sep-1999 ACCESSIONS E36799; S08030; S01996; B56627 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession E36799 !'##molecule_type DNA !'##residues 1-848 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02475.1; !1PID:g330832 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given REFERENCE S08030 !$#authors Robertson, G.R.; Scott, N.A.; Miller, J.M.; Sabine, M.; !1Zheng, M.; Bell, C.W.; Whalley, J.M. !$#submission submitted to the EMBL Data Library, January 1990 !$#accession S08030 !'##molecule_type DNA !'##residues 1-848 ##label ROB !'##cross-references EMBL:X51324; NID:g59236; PIDN:CAA35707.1; !1PID:g59237 REFERENCE S01993 !$#authors Robertson, G.R.; Whalley, J.M. !$#journal Nucleic Acids Res. (1988) 16:11303-11317 !$#title Evolution of the herpes thymidine kinase: identification and !1comparison of the equine herpesvirus 1 thymidine kinase gene !1reveals similarity to a cell-encoded thymidylate kinase. !$#cross-references MUID:89083562; PMID:2849761 !$#accession S01996 !'##molecule_type DNA !'##residues 1-256 ##label ROB2 !'##cross-references EMBL:X13209; NID:g59229; PIDN:CAA31600.1; !1PID:g59233 REFERENCE A56627 !$#authors Robertson, G.R.; Scott, N.A.; Miller, J.M.; Sabine, M.; !1Zheng, M.; Bell, C.W.; Whalley, J.M. !$#journal DNA Seq. (1991) 1:241-249 !$#title Sequence characteristics of a gene in equine herpesvirus 1 !1homologous to glycoprotein H of herpes simplex virus. !$#cross-references MUID:92216126; PMID:1666854 !$#accession B56627 !'##molecule_type DNA !'##residues 1-848 ##label RO2 !'##cross-references GB:X51324; GB:S93400; NID:g59236; PIDN:CAA35707.1; !1PID:g59237 !'##experimental_source strain HVS 25A !'##note sequence extracted from NCBI backbone (NCBIN:93400, !1NCBIP:93441) GENETICS !$#gene 39 !$#map_position 0.47-0.49 map units CLASSIFICATION #superfamily herpesvirus glycoprotein H KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-848 #product glycoprotein H #status predicted #label MAT\ !$502-518 #domain transmembrane #status predicted #label TM1\ !$541-559 #domain transmembrane #status predicted #label TM2\ !$564-581 #domain transmembrane #status predicted #label TM3\ !$809-829 #domain transmembrane #status predicted #label TM4\ !$36,41,45,60,119, !$182,210,496,672, !$766,789 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 848 #molecular-weight 92841 #checksum 7503 SEQUENCE /// ENTRY VGBEHC #type complete TITLE glycoprotein H precursor - human cytomegalovirus (strain AD169) ALTERNATE_NAMES hypothetical protein UL75 ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 #note host Homo sapiens (man) DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jul-1999 ACCESSIONS A29888; S09838 REFERENCE A29888 !$#authors Cranage, M.P.; Smith, G.L.; Bell, S.E.; Hart, H.; Brown, C.; !1Bankier, A.T.; Tomlinson, P.; Barrell, B.G.; Minson, T.C. !$#journal J. Virol. (1988) 62:1416-1422 !$#title Identification and expression of a human cytomegalovirus !1glycoprotein with homology to the Epstein-Barr virus BXLF2 !1product, varicella-zoster virus gpIII, and herpes simplex !1virus type 1 glycoprotein H. !$#cross-references MUID:88155782; PMID:2831402 !$#accession A29888 !'##molecule_type DNA !'##residues 1-743 ##label CRA !'##cross-references GB:M19882; NID:g330514; PIDN:AAA45938.1; !1PID:g330515 !'##experimental_source strain AD169 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09838 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-743 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35390.1; !1PID:g1780852 !'##experimental_source strain AD169 !'##note this sequence was submitted to the EMBL Data Library, December !11989 CLASSIFICATION #superfamily herpesvirus glycoprotein H KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-743 #product glycoprotein H #status predicted #label MAT\ !$718-738 #domain transmembrane #status predicted #label TMM\ !$56,63,68,193,642, !$701 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 743 #molecular-weight 84451 #checksum 2001 SEQUENCE /// ENTRY VGBEHT #type complete TITLE glycoprotein H precursor - human cytomegalovirus (strain Towne) ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 #note host Homo sapiens (man) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS A30182 REFERENCE A30182 !$#authors Pachl, C.; Probert, W.S.; Hermsen, K.M.; Masiarz, F.R.; !1Rasmussen, L.; Merigan, T.C.; Spaete, R.R. !$#journal Virology (1989) 169:418-426 !$#title The human cytomegalovirus strain Towne glycoprotein H gene !1encodes glycoprotein p86. !$#cross-references MUID:89204913; PMID:2539698 !$#accession A30182 !'##molecule_type DNA !'##residues 1-742 ##label PAC !'##cross-references GB:M25271; NID:g330539; PIDN:AAA45946.1; !1PID:g330540 CLASSIFICATION #superfamily herpesvirus glycoprotein H KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-742 #product glycoprotein H #status predicted #label GPH\ !$718-736 #domain transmembrane #status predicted #label TMN\ !$55,62,67,192,641, !$700 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 742 #molecular-weight 84274 #checksum 1820 SEQUENCE /// ENTRY VGBEH6 #type complete TITLE glycoprotein H precursor - human herpesvirus 6 (strains U1102, GS, and AJ) ORGANISM #formal_name human herpesvirus 6 DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 24-Sep-1999 ACCESSIONS A40511; JQ2382; PQ0846; D56653; PQ0847 REFERENCE A40511 !$#authors Josephs, S.F.; Ablashi, D.V.; Salahuddin, S.Z.; Jagodzinski, !1L.L.; Wong-Staal, F.; Gallo, R.C. !$#journal J. Virol. (1991) 65:5597-5604 !$#title Identification of the human herpesvirus 6 glycoprotein H and !1putative large tegument protein genes. !$#cross-references MUID:91374623; PMID:1654455 !$#accession A40511 !'##molecule_type DNA !'##residues 1-694 ##label JOS !'##cross-references GB:S57509; NID:g235428; PIDN:AAB19779.1; !1PID:g235431 !'##experimental_source strain GS, clone pZVB43 REFERENCE JQ2382 !$#authors Gompels, U.A.; Carrigan, D.R.; Carss, A.L.; Arno, J. !$#journal J. Gen. Virol. (1993) 74:613-622 !$#title Two groups of human herpesvirus 6 identified by sequence !1analyses of laboratory strains and variants from Hodgkin's !1lymphoma and bone marrow transplant patients. !$#cross-references MUID:93224882; PMID:8385692 !$#accession JQ2382 !'##molecule_type DNA !'##residues 1-694 ##label GOM !'##cross-references GB:X83413; NID:g853961; PIDN:CAA58382.1; !1PID:g854027 !'##experimental_source strain AJ !$#accession PQ0846 !'##molecule_type DNA !'##residues 1-65 ##label GOM1 !'##experimental_source strain GS REFERENCE A56653 !$#authors Gompels, U.A.; Carss, A.L.; Sun, N.; Arrand, J.R. !$#journal DNA Seq. (1992) 3:25-39 !$#title Infectivity determinants encoded in a conserved gene block !1of human herpesvirus-6. !$#cross-references MUID:93091236; PMID:1333836 !$#accession D56653 !'##molecule_type DNA !'##residues 1-694 ##label GO2 !'##cross-references GB:X83413; NID:g853961; PIDN:CAA58382.1; !1PID:g854027 !'##experimental_source strain U1102 !'##note sequence extracted from NCBI backbone (NCBIN:120533, !1NCBIP:121866) CLASSIFICATION #superfamily herpesvirus glycoprotein H KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-694 #product glycoprotein H #status predicted #label GPH\ !$554-570 #domain transmembrane #status predicted #label TM1\ !$668-684 #domain transmembrane #status predicted #label TM2\ !$21,24,51,76,148, !$206,337,365,384, !$411,538,573,593,652 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 694 #molecular-weight 79554 #checksum 9041 SEQUENCE /// ENTRY QQBE6L #type complete TITLE glycoprotein H - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 03-Aug-1984 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS A93065; A36827; A03795; S33046 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession A93065 !'##molecule_type DNA !'##residues 1-116 ##label BAN !'##cross-references EMBL:V01555 REFERENCE A38059 !$#authors Farrell, P.J.; Barrell, B.G. !$#submission submitted to the EMBL Data Library, June 1984 !$#description DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#accession A36827 !'##molecule_type DNA !'##residues 1-706 ##label FAR !'##cross-references EMBL:V01555; NID:g59074; PIDN:CAA24797.1; !1PID:g1334905 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region !$#note neither amino acid nor nucleotide sequence is given CLASSIFICATION #superfamily herpesvirus glycoprotein H KEYWORDS glycoprotein; transmembrane protein FEATURE !$60,435,549,604,664 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 706 #molecular-weight 78321 #checksum 5730 SEQUENCE /// ENTRY VGBE11 #type complete TITLE glycoprotein H precursor - saimiriine herpesvirus 1 (strain 11) ORGANISM #formal_name saimiriine herpesvirus 1 #note host Saimiri sciureus (common squirrel monkey) DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jun-2000 ACCESSIONS JQ0010; D33374 REFERENCE JQ0010 !$#authors Gompels, U.A.; Craxton, M.A.; Honess, R.W. !$#journal J. Gen. Virol. (1988) 69:2819-2829 !$#title Conservation of glycoprotein H (gH) in herpesviruses: !1nucleotide sequence of the gH gene from Herpesvirus saimiri. !$#cross-references MUID:89036162; PMID:2846759 !$#accession JQ0010 !'##molecule_type DNA !'##residues 1-717 ##label GOM !'##cross-references GB:D00400; NID:g221845; PIDN:BAA00302.1; !1PID:g221846 REFERENCE A33374 !$#authors Honess, R.W.; Craxton, M.A.; Williams, L.; Gompels, U.A. !$#journal J. Gen. Virol. (1989) 70:3003-3013 !$#title A comparative analysis of the sequence of the thymidine !1kinase gene of a gammaherpesvirus, herpesvirus saimiri. !$#cross-references MUID:90063548; PMID:2555434 !$#accession D33374 !'##molecule_type DNA !'##residues 1-60 ##label HON !'##cross-references GB:D00543; NID:g221853; PIDN:BAA00433.1; !1PID:g221857 CLASSIFICATION #superfamily herpesvirus glycoprotein H KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-717 #product glycoprotein H #status predicted #label MAT\ !$689-709 #domain transmembrane #status predicted #label TMM\ !$43,59,80,128,444, !$560,613,675 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 717 #molecular-weight 82583 #checksum 8073 SEQUENCE /// ENTRY JQ1622 #type complete TITLE glycoprotein H precursor - murine cytomegalovirus (strain K181) ORGANISM #formal_name murine cytomegalovirus, murine herpesvirus 1 DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jun-2000 ACCESSIONS JQ1622 REFERENCE JQ1622 !$#authors Xu, J.; Ballas, P.B.; Lyons, P.A.; Shellam, G.R.; Scalzo, !1A.A. !$#journal J. Gen. Virol. (1992) 73:1849-1854 !$#title Identification of the glycoprotein H gene of murine !1cytomegalovirus. !$#cross-references MUID:92333274; PMID:1321219 !$#accession JQ1622 !'##molecule_type DNA !'##residues 1-724 ##label XUJ !'##cross-references GB:D10089; NID:g221798; PIDN:BAA00984.1; !1PID:g221799 CLASSIFICATION #superfamily herpesvirus glycoprotein H KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-14 #domain signal sequence #status predicted #label SIG\ !$15-724 #product glycoprotein H #status predicted #label MAT\ !$695-717 #domain transmembrane #status predicted #label TMM\ !$38,50,319,459,612, !$620,680 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 724 #molecular-weight 80386 #checksum 7950 SEQUENCE /// ENTRY JQ2042 #type complete TITLE glycoprotein H precursor - Marek's disease virus (type 1) ORGANISM #formal_name Marek's disease virus #note host Gallus gallus (chicken) DATE 24-Feb-1994 #sequence_revision 24-Feb-1994 #text_change 07-May-1999 ACCESSIONS JQ2042 REFERENCE JQ2042 !$#authors Scott, S.D.; Smith, G.D.; Ross, N.L.J.; Binns, M.M. !$#journal J. Gen. Virol. (1993) 74:1185-1190 !$#title Identification and sequence analysis of the homologues of !1the herpes simplex virus type 1 glycoprotein H in Marek's !1disease virus and the herpesvirus of turkeys. !$#cross-references MUID:93286575; PMID:8389802 !$#accession JQ2042 !'##molecule_type DNA !'##residues 1-813 ##label SCO !'##cross-references GB:S62554 CLASSIFICATION #superfamily herpesvirus glycoprotein H KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-813 #product glycoprotein H #status predicted #label MAT\ !$624-640 #region hydrophobic #status predicted\ !$772-788 #domain transmembrane #status predicted #label TMN\ !$62,116,247,279,410, !$434,469,576,727,750 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 813 #molecular-weight 90945 #checksum 1488 SEQUENCE /// ENTRY JQ2043 #type complete TITLE glycoprotein H precursor - turkey herpesvirus ORGANISM #formal_name turkey herpesvirus DATE 24-Feb-1994 #sequence_revision 24-Feb-1994 #text_change 07-May-1999 ACCESSIONS JQ2043 REFERENCE JQ2042 !$#authors Scott, S.D.; Smith, G.D.; Ross, N.L.J.; Binns, M.M. !$#journal J. Gen. Virol. (1993) 74:1185-1190 !$#title Identification and sequence analysis of the homologues of !1the herpes simplex virus type 1 glycoprotein H in Marek's !1disease virus and the herpesvirus of turkeys. !$#cross-references MUID:93286575; PMID:8389802 !$#accession JQ2043 !'##molecule_type DNA !'##residues 1-808 ##label SCO !'##cross-references GB:S62554 CLASSIFICATION #superfamily herpesvirus glycoprotein H KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-808 #product glycoprotein H #status predicted #label MAT\ !$616-632 #region hydrophobic #status predicted\ !$771-787 #domain transmembrane #status predicted #label TMN\ !$44,60,114,240,272, !$431,461,719,742 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 808 #molecular-weight 91102 #checksum 6919 SEQUENCE /// ENTRY VGBE63 #type complete TITLE glycoprotein gp63 - suid herpesvirus 1 ORGANISM #formal_name suid herpesvirus 1 #note host Sus scrofa domestica (domestic pig) DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jul-1999 ACCESSIONS A29012 REFERENCE A93021 !$#authors Petrovskis, E.A.; Timmins, J.G.; Post, L.E. !$#journal J. Virol. (1986) 60:185-193 !$#title Use of lambda-gt11 to isolate genes for two pseudorabies !1virus glycoproteins with homology to herpes simplex virus !1and varicella-zoster virus glycoproteins. !$#cross-references MUID:86308235; PMID:3018284 !$#accession A29012 !'##molecule_type DNA !'##residues 1-350 ##label PET !'##cross-references GB:M14336; NID:g334055; PIDN:AAC35204.1; !1PID:g334056 !'##experimental_source strain Rice CLASSIFICATION #superfamily pseudorabies virus glycoprotein gp63 KEYWORDS glycoprotein; transmembrane protein FEATURE !$11-27 #domain transmembrane #status predicted #label TM1\ !$286-308 #domain transmembrane #status predicted #label TM2\ !$56,73,153,256,262, !$275 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 350 #molecular-weight 36773 #checksum 1031 SEQUENCE /// ENTRY VGBEE9 #type complete TITLE glycoprotein gp63 precursor - equine herpesvirus 1 ALTERNATE_NAMES glycoprotein I precursor; hypothetical 46K protein; ORF2 protein ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jul-1999 ACCESSIONS C36646; JQ0998; A36803 REFERENCE A36646 !$#authors Audonnet, J.C.; Winslow, J.; Allen, G.; Paoletti, E. !$#journal J. Gen. Virol. (1990) 71:2969-2978 !$#title Equine herpesvirus type 1 unique short fragment encodes !1glycoproteins with homology to herpes simplex virus type 1 !1gD, gI and gE. !$#cross-references MUID:91108393; PMID:2177089 !$#accession C36646 !'##molecule_type DNA !'##residues 1-424 ##label AUD !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02508.1; !1PID:g330864 !'##experimental_source strain Kentucky D REFERENCE JQ0998 !$#authors Elton, D.M.; Halliburton, I.W.; Killington, R.A.; Meredith, !1D.M.; Bonass, W.A. !$#journal Gene (1991) 101:203-208 !$#title Sequence analysis of the 4.7-kb BamHI-EcoRI fragment of the !1equine herpesvirus type-1 short unique region. !$#cross-references MUID:91276272; PMID:1647359 !$#accession JQ0998 !'##molecule_type DNA !'##residues 1-424 ##label ELT !'##cross-references GB:M36299; NID:g330787; PIDN:AAA66547.1; !1PID:g330788 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession A36803 !'##molecule_type DNA !'##residues 1-424 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02508.1; !1PID:g330864 !'##experimental_source strain Ab4p REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 73 CLASSIFICATION #superfamily pseudorabies virus glycoprotein gp63 KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-424 #product glycoprotein gp63 #status predicted #label !8MAT\ !$320-336 #domain transmembrane #status predicted #label TM1\ !$35,67,78,121,131, !$236,307 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 424 #molecular-weight 46392 #checksum 1229 SEQUENCE /// ENTRY MMBEK1 #type complete TITLE cell fusion protein precursor - human herpesvirus 1 (strain KOS) ALTERNATE_NAMES UL53 protein ORGANISM #formal_name human herpesvirus 1 #note host Homo sapiens (man) DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 16-Jul-1999 ACCESSIONS A03735; A40819 REFERENCE A03735 !$#authors Debroy, C.; Pederson, N.; Person, S. !$#journal Virology (1985) 145:36-48 !$#title Nucleotide sequence of a herpes simplex virus type 1 gene !1that causes cell fusion. !$#cross-references MUID:85246224; PMID:2990101 !$#accession A03735 !'##molecule_type DNA !'##residues 1-338 ##label DEB !'##cross-references GB:M11316; NID:g330046; PIDN:AAA45765.1; !1PID:g330047 REFERENCE A40819 !$#authors Ramaswamy, R.; Holland, T.C. !$#journal Virology (1992) 186:579-587 !$#title In vitro characterization of the HSV-1 UL53 gene product. !$#cross-references MUID:92124732; PMID:1310186 !$#accession A40819 !'##molecule_type protein !'##residues 1-30 ##label RAM GENETICS !$#gene UL53 !$#map_position 0.732-0.745 CLASSIFICATION #superfamily herpesvirus cell fusion protein KEYWORDS glycoprotein; membrane fusion; transmembrane protein FEATURE !$1-30 #domain signal sequence #status experimental #label !8SIG\ !$31-338 #product cell fusion protein #status predicted #label !8MAT\ !$125-141 #domain transmembrane #status predicted #label TM1\ !$222-238 #domain transmembrane #status predicted #label TM2\ !$249-265 #domain transmembrane #status predicted #label TM3\ !$311-327 #domain transmembrane #status predicted #label TM4\ !$48,58 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 338 #molecular-weight 37526 #checksum 4138 SEQUENCE /// ENTRY MMBEK2 #type complete TITLE cell fusion protein precursor - human herpesvirus 1 ALTERNATE_NAMES syncytial protein ORGANISM #formal_name human herpesvirus 1 DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jun-2000 ACCESSIONS A94358; A43039; A26346; H30089 REFERENCE A94358 !$#authors Pogue-Geile, K.L.; Spear, P.G. !$#journal Virology (1987) 157:67-74 !$#title The single base pair substitution responsible for the Syn !1phenotype of herpes simplex virus type 1, strain MP. !$#cross-references MUID:87151121; PMID:3029967 !$#accession A94358 !'##molecule_type DNA !'##residues 1-338 ##label POG !'##cross-references GB:M16610; NID:g330205; PIDN:AAA45810.1; !1PID:g330206 !'##experimental_source strain mP !'##note the mutant strain MP differs from that shown in having 40-Val REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession A43039 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-338 ##label MCG !'##cross-references GB:X14112; NID:g1944536; PIDN:CAA32289.1; !1PID:g59553; GB:D00317 !'##experimental_source strain 17 CLASSIFICATION #superfamily herpesvirus cell fusion protein KEYWORDS glycoprotein; membrane fusion; transmembrane protein FEATURE !$1-30 #domain signal sequence #status predicted #label SIG\ !$31-338 #product cell fusion protein #status predicted #label !8CFP\ !$123-139 #domain transmembrane #status predicted #label TM1\ !$222-238 #domain transmembrane #status predicted #label TM2\ !$249-265 #domain transmembrane #status predicted #label TM3\ !$307-323 #domain transmembrane #status predicted #label TM4\ !$48,58 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 338 #molecular-weight 37572 #checksum 3324 SEQUENCE /// ENTRY MMBEHB #type fragment TITLE cell fusion protein - human herpesvirus 2 (strain HG52) (fragment) ORGANISM #formal_name human herpesvirus 2 #note host Homo sapiens (man) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jun-2000 ACCESSIONS PQ0333 REFERENCE JQ1494 !$#authors McGeoch, D.J.; Cunningham, C.; McIntyre, G.; Dolan, A. !$#journal J. Gen. Virol. (1991) 72:3057-3075 !$#title Comparative sequence analysis of the long repeat regions and !1adjoining parts of the long unique regions in the genomes of !1herpes simplex viruses types 1 and 2. !$#cross-references MUID:92113549; PMID:1662697 !$#accession PQ0333 !'##molecule_type DNA !'##residues 1-136 ##label MCG !'##cross-references GB:D10471; DDBJ:D01128; NID:g221784; !1PIDN:BAA01268.1; PID:g221787 GENETICS !$#gene UL53 CLASSIFICATION #superfamily herpesvirus cell fusion protein KEYWORDS membrane fusion; transmembrane protein FEATURE !$1-136 #product cell fusion protein (fragment) #status !8predicted #label CFP\ !$20-36 #domain transmembrane #status predicted #label TM2\ !$47-63 #domain transmembrane #status predicted #label TM3\ !$105-121 #domain transmembrane #status predicted #label TM4 SUMMARY #length 136 #checksum 38 SEQUENCE /// ENTRY MMBE5 #type complete TITLE cell fusion protein precursor - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS E27212 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession E27212 !'##molecule_type DNA !'##residues 1-340 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27888.1; !1PID:g59994 GENETICS !$#gene 5 CLASSIFICATION #superfamily herpesvirus cell fusion protein KEYWORDS membrane fusion; transmembrane protein FEATURE !$1-31 #domain signal sequence #status predicted #label SIG\ !$32-340 #product cell fusion protein #status predicted #label !8CFP\ !$115-137 #domain transmembrane #status predicted #label TM1\ !$220-238 #domain transmembrane #status predicted #label TM3\ !$251-269 #domain transmembrane #status predicted #label TM4\ !$307-322 #domain transmembrane #status predicted #label TM5 SUMMARY #length 340 #molecular-weight 38576 #checksum 7827 SEQUENCE /// ENTRY MMBEA5 #type complete TITLE cell fusion protein precursor - equine herpesvirus 1 ALTERNATE_NAMES syncytial protein ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS G36795; A42746 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession G36795 !'##molecule_type DNA !'##residues 1-343 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02441.1; !1PID:g330798 !'##experimental_source strain Ab4p REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given REFERENCE A42746 !$#authors Zhao, Y.; Holden, V.R.; Harty, R.N.; O'Callaghan, D.J. !$#journal J. Virol. (1992) 66:5363-5372 !$#title Identification and transcriptional analyses of the UL3 and !1UL4 genes of equine herpesvirus 1, homologs of the ICP27 and !1glycoprotein K genes of herpes simplex virus. !$#cross-references MUID:92365125; PMID:1323700 !$#accession A42746 !'##molecule_type DNA !'##residues 1-343 ##label ZHA !'##cross-references GB:S43139 !'##experimental_source strain Kentucky A GENETICS !$#gene 6 CLASSIFICATION #superfamily herpesvirus cell fusion protein KEYWORDS glycoprotein; membrane fusion; transmembrane protein FEATURE !$1-31 #domain signal sequence #status predicted #label SIG\ !$32-343 #product cell fusion protein #status predicted #label !8CFP\ !$118-140 #domain transmembrane #status predicted #label TM1\ !$156-176 #domain transmembrane #status predicted #label TM2\ !$223-242 #domain transmembrane #status predicted #label TM3\ !$254-272 #domain transmembrane #status predicted #label TM4\ !$312-328 #domain transmembrane #status predicted #label TM5\ !$57,89 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 343 #molecular-weight 38044 #checksum 1760 SEQUENCE /// ENTRY WMBE51 #type complete TITLE UL10 protein - human herpesvirus 1 ORGANISM #formal_name human herpesvirus 1 #note host Homo sapiens (man) DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 16-Jun-2000 ACCESSIONS A03736; A30083 REFERENCE A93620 !$#authors McGeoch, D.J.; Dolan, A.; Frame, M.C. !$#journal Nucleic Acids Res. (1986) 14:3435-3448 !$#title DNA sequence of the region in the genome of herpes simplex !1virus type 1 containing the exonuclease gene and !1neighbouring genes. !$#cross-references MUID:86205244; PMID:3010237 !$#accession A03736 !'##molecule_type DNA !'##residues 1-473 ##label MCG !'##cross-references GB:X03839; NID:g59841; PIDN:CAA27451.1; PID:g59842 !'##experimental_source strain 17 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession A30083 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-473 ##label MC2 !'##cross-references GB:X14112; NID:g1944536; PIDN:CAA32346.1; !1PID:g59510; GB:D00317 !'##experimental_source strain 17 COMMENT This is probably a membrane-associated or transmembrane !1protein. GENETICS !$#gene UL10 !$#map_position 0.16-0.20 CLASSIFICATION #superfamily herpesvirus 51K protein KEYWORDS transmembrane protein SUMMARY #length 473 #molecular-weight 51392 #checksum 9462 SEQUENCE /// ENTRY WZBE50 #type complete TITLE gene 50 protein - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS F27344 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession F27344 !'##molecule_type DNA !'##residues 1-435 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27934.1; !1PID:g60040 GENETICS !$#gene 50 CLASSIFICATION #superfamily herpesvirus 51K protein SUMMARY #length 435 #molecular-weight 48671 #checksum 3965 SEQUENCE /// ENTRY WZBEE4 #type complete TITLE 49.2K membrane protein - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS G36800 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession G36800 !'##molecule_type DNA !'##residues 1-450 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02487.1; !1PID:g330843 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 52 CLASSIFICATION #superfamily herpesvirus 51K protein KEYWORDS transmembrane protein FEATURE !$37-53 #domain transmembrane #status predicted #label TM1\ !$111-127 #domain transmembrane #status predicted #label TM2\ !$156-173 #domain transmembrane #status predicted #label TM3\ !$179-195 #domain transmembrane #status predicted #label TM4\ !$241-257 #domain transmembrane #status predicted #label TM5\ !$271-287 #domain transmembrane #status predicted #label TM6\ !$297-314 #domain transmembrane #status predicted #label TM7\ !$341-358 #domain transmembrane #status predicted #label TM8 SUMMARY #length 450 #molecular-weight 49221 #checksum 9416 SEQUENCE /// ENTRY WMBE11 #type complete TITLE UL11 protein - human herpesvirus 1 ORGANISM #formal_name human herpesvirus 1 #note host Homo sapiens (man) DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 16-Jun-2000 ACCESSIONS A03737; B30083 REFERENCE A93620 !$#authors McGeoch, D.J.; Dolan, A.; Frame, M.C. !$#journal Nucleic Acids Res. (1986) 14:3435-3448 !$#title DNA sequence of the region in the genome of herpes simplex !1virus type 1 containing the exonuclease gene and !1neighbouring genes. !$#cross-references MUID:86205244; PMID:3010237 !$#accession A03737 !'##molecule_type DNA !'##residues 1-96 ##label MCG !'##cross-references GB:X03839; NID:g59841; PIDN:CAA27452.1; PID:g59843 !'##experimental_source strain 17 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession B30083 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-96 ##label MC2 !'##cross-references GB:X14112; NID:g1944536; PIDN:CAA32347.1; !1PID:g59512; GB:D00317 !'##experimental_source strain 17 GENETICS !$#gene UL11 !$#map_position 0.16-0.20 CLASSIFICATION #superfamily herpesvirus 10K protein SUMMARY #length 96 #molecular-weight 10487 #checksum 6237 SEQUENCE /// ENTRY WMBE21 #type complete TITLE UL14 protein - human herpesvirus 1 ORGANISM #formal_name human herpesvirus 1 #note host Homo sapiens (man) DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 16-Jun-2000 ACCESSIONS A03739; E30083 REFERENCE A93620 !$#authors McGeoch, D.J.; Dolan, A.; Frame, M.C. !$#journal Nucleic Acids Res. (1986) 14:3435-3448 !$#title DNA sequence of the region in the genome of herpes simplex !1virus type 1 containing the exonuclease gene and !1neighbouring genes. !$#cross-references MUID:86205244; PMID:3010237 !$#accession A03739 !'##molecule_type DNA !'##residues 1-215 ##label MCG !'##cross-references GB:X03839; NID:g59841; PIDN:CAA27455.1; PID:g59846 !'##experimental_source strain 17 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession E30083 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-215 ##label MC2 !'##cross-references GB:X14112; GB:D10879; GB:D00317; NID:g221721; !1PIDN:BAA01660.1; PID:g221736 !'##experimental_source strain 17 GENETICS !$#gene UL14 !$#map_position 0.16-0.20 CLASSIFICATION #superfamily herpesvirus 23K protein SUMMARY #length 215 #molecular-weight 23456 #checksum 7624 SEQUENCE /// ENTRY WZBE46 #type complete TITLE gene 46 protein - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS B27344 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession B27344 !'##molecule_type DNA !'##residues 1-199 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27929.1; !1PID:g60035 GENETICS !$#gene 46 CLASSIFICATION #superfamily herpesvirus 23K protein SUMMARY #length 199 #molecular-weight 22545 #checksum 8442 SEQUENCE /// ENTRY WZBEE1 #type complete TITLE gene 48 protein - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS C36800 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession C36800 !'##molecule_type DNA !'##residues 1-317 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02483.1; !1PID:g330839 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 48 CLASSIFICATION #superfamily herpesvirus 23K protein SUMMARY #length 317 #molecular-weight 35815 #checksum 6973 SEQUENCE /// ENTRY WZBEE3 #type complete TITLE UL14 protein - suid herpesvirus 1 (strain NIA-3) ORGANISM #formal_name suid herpesvirus 1 DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS A42744 REFERENCE A42744 !$#authors de Wind, N.; Domen, J.; Berns, A. !$#journal J. Virol. (1992) 66:5200-5209 !$#title Herpesviruses encode an unusual protein-serine/threonine !1kinase which is nonessential for growth in cultured cells. !$#cross-references MUID:92365105; PMID:1323689 !$#accession A42744 !'##molecule_type DNA !'##residues 1-159 ##label DEW !'##cross-references GB:M94870; NID:g334092; PIDN:AAA47480.1; !1PID:g334093 GENETICS !$#gene UL14 CLASSIFICATION #superfamily herpesvirus 23K protein SUMMARY #length 159 #molecular-weight 17928 #checksum 7312 SEQUENCE /// ENTRY WZBE1 #type complete TITLE gene 1 protein - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS A27212 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession A27212 !'##molecule_type DNA !'##residues 1-108 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27884.1; !1PID:g59990 GENETICS !$#gene 1 CLASSIFICATION #superfamily varicella-zoster virus gene 1 protein SUMMARY #length 108 #molecular-weight 12104 #checksum 2286 SEQUENCE /// ENTRY WZBE2 #type complete TITLE gene 2 protein - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS B27212 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession B27212 !'##molecule_type DNA !'##residues 1-238 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27885.1; !1PID:g59991 GENETICS !$#gene 2 CLASSIFICATION #superfamily varicella-zoster virus gene 2 protein SUMMARY #length 238 #molecular-weight 25984 #checksum 1948 SEQUENCE /// ENTRY WZBEA2 #type complete TITLE gene 3 protein - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS D36795 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession D36795 !'##molecule_type DNA !'##residues 1-257 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02438.1; !1PID:g330795 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 3 CLASSIFICATION #superfamily varicella-zoster virus gene 2 protein SUMMARY #length 257 #molecular-weight 28022 #checksum 756 SEQUENCE /// ENTRY WZBEKA #type complete TITLE gene 3 protein - equine herpesvirus 1 (strain Kentucky A) ALTERNATE_NAMES L1 protein ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 20-Apr-2001 ACCESSIONS A43490 REFERENCE A43490 !$#authors Yalamanchili, R.R.; Raengsakulrach, B.; O'Callaghan, D.J. !$#journal Virus Res. (1991) 18:109-116 !$#title Equine herpesvirus 1 sequence near the left terminus codes !1for two open reading frames. !$#cross-references MUID:91253259; PMID:1645901 !$#accession A43490 !'##molecule_type DNA !'##residues 1-258 ##label YAL !'##cross-references GB:X59003; NID:g59243; PIDN:CAA41749.1; PID:g59244 GENETICS !$#gene 3 CLASSIFICATION #superfamily varicella-zoster virus gene 2 protein SUMMARY #length 258 #molecular-weight 28361 #checksum 3155 SEQUENCE /// ENTRY WZBE3 #type complete TITLE gene 3 protein - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS C27212 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession C27212 !'##molecule_type DNA !'##residues 1-179 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27886.1; !1PID:g59992 GENETICS !$#gene 3 CLASSIFICATION #superfamily varicella-zoster virus gene 3 protein SUMMARY #length 179 #molecular-weight 19150 #checksum 2091 SEQUENCE /// ENTRY WMBEY5 #type complete TITLE UL55 protein - human herpesvirus 1 (strain 17) ORGANISM #formal_name human herpesvirus 1 DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jun-2000 ACCESSIONS A30090 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession A30090 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-186 ##label MCG !'##cross-references GB:X14112; NID:g1944536; PIDN:CAA32291.1; !1PID:g59555; GB:D00317 GENETICS !$#gene UL55 CLASSIFICATION #superfamily varicella-zoster virus gene 3 protein SUMMARY #length 186 #molecular-weight 20492 #checksum 7740 SEQUENCE /// ENTRY B48560 #type complete TITLE UL55 protein - human herpesvirus 1 (strain HFEM) ORGANISM #formal_name human herpesvirus 1 DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 04-Mar-1994 ACCESSIONS B48560 REFERENCE A48560 !$#authors Rosen-Wolff, A.; Frank, S.; Raab, K.; Moyal, M.; Becker, Y.; !1Darai, G. !$#journal Virus Res. (1992) 25:189-199 !$#title Determination of the coding capacity of the BamHI DNA !1fragment B of apathogenic Herpes simplex virus type 1 strain !1HFEM by DNA nucleotide sequence analysis. !$#cross-references MUID:93070559; PMID:1332274 !$#accession B48560 !'##molecule_type DNA !'##residues 1-186 ##label ROS !'##note sequence extracted from NCBI backbone (NCBIN:117573, !1NCBIP:117576) GENETICS !$#gene UL55 CLASSIFICATION #superfamily varicella-zoster virus gene 3 protein SUMMARY #length 186 #molecular-weight 20491 #checksum 7890 SEQUENCE /// ENTRY WMBEXB #type complete TITLE UL55 protein - human herpesvirus 2 (strain HG52) ORGANISM #formal_name human herpesvirus 2 #note host Homo sapiens (man) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jun-2000 ACCESSIONS JQ1499 REFERENCE JQ1494 !$#authors McGeoch, D.J.; Cunningham, C.; McIntyre, G.; Dolan, A. !$#journal J. Gen. Virol. (1991) 72:3057-3075 !$#title Comparative sequence analysis of the long repeat regions and !1adjoining parts of the long unique regions in the genomes of !1herpes simplex viruses types 1 and 2. !$#cross-references MUID:92113549; PMID:1662697 !$#accession JQ1499 !'##molecule_type DNA !'##residues 1-186 ##label MCG !'##cross-references GB:D10471; DDBJ:D01128; NID:g221784; !1PIDN:BAA01270.1; PID:g221789 GENETICS !$#gene UL55 CLASSIFICATION #superfamily varicella-zoster virus gene 3 protein SUMMARY #length 186 #molecular-weight 20441 #checksum 7062 SEQUENCE /// ENTRY WZBEA3 #type complete TITLE gene 4 protein - equine herpesvirus 1 ALTERNATE_NAMES L2 protein ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 20-Apr-2001 ACCESSIONS E36795; B43490 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession E36795 !'##molecule_type DNA !'##residues 1-200 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02439.1; !1PID:g330796 !'##experimental_source strain Ab4p REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given REFERENCE A43490 !$#authors Yalamanchili, R.R.; Raengsakulrach, B.; O'Callaghan, D.J. !$#journal Virus Res. (1991) 18:109-116 !$#title Equine herpesvirus 1 sequence near the left terminus codes !1for two open reading frames. !$#cross-references MUID:91253259; PMID:1645901 !$#accession B43490 !'##molecule_type DNA !'##residues 1-200 ##label YAL !'##cross-references GB:X59003; NID:g59243; PIDN:CAA41750.1; PID:g59245 !'##experimental_source strain Kentucky A GENETICS !$#gene 4 CLASSIFICATION #superfamily varicella-zoster virus gene 3 protein SUMMARY #length 200 #molecular-weight 22380 #checksum 9028 SEQUENCE /// ENTRY WZBE4 #type complete TITLE gene 4 protein - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS D27212 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession D27212 !'##molecule_type DNA !'##residues 1-452 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27887.1; !1PID:g59993 GENETICS !$#gene 4 CLASSIFICATION #superfamily varicella-zoster virus gene 4 protein KEYWORDS transcription regulation SUMMARY #length 452 #molecular-weight 51542 #checksum 254 SEQUENCE /// ENTRY WMBEY4 #type complete TITLE UL54 protein - human herpesvirus 1 (strain 17) ORGANISM #formal_name human herpesvirus 1 DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jun-2000 ACCESSIONS I30089 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession I30089 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-512 ##label MCG !'##cross-references GB:X14112; NID:g1944536; PIDN:CAA32290.1; !1PID:g59554; GB:D00317 GENETICS !$#gene UL54 CLASSIFICATION #superfamily varicella-zoster virus gene 4 protein KEYWORDS transcription regulation SUMMARY #length 512 #molecular-weight 55252 #checksum 5523 SEQUENCE /// ENTRY A48560 #type complete TITLE UL54 protein - human herpesvirus 1 (strain HFEM) ORGANISM #formal_name human herpesvirus 1 DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Feb-1997 ACCESSIONS A48560 REFERENCE A48560 !$#authors Rosen-Wolff, A.; Frank, S.; Raab, K.; Moyal, M.; Becker, Y.; !1Darai, G. !$#journal Virus Res. (1992) 25:189-199 !$#title Determination of the coding capacity of the BamHI DNA !1fragment B of apathogenic Herpes simplex virus type 1 strain !1HFEM by DNA nucleotide sequence analysis. !$#cross-references MUID:93070559; PMID:1332274 !$#accession A48560 !'##molecule_type DNA !'##residues 1-511 ##label ROS !'##note sequence extracted from NCBI backbone (NCBIN:117573, !1NCBIP:117574) GENETICS !$#gene UL54 CLASSIFICATION #superfamily varicella-zoster virus gene 4 protein KEYWORDS transcription regulation SUMMARY #length 511 #molecular-weight 55142 #checksum 1309 SEQUENCE /// ENTRY WMBEXA #type complete TITLE UL54 protein - human herpesvirus 2 (strain HG52) ORGANISM #formal_name human herpesvirus 2 #note host Homo sapiens (man) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jun-2000 ACCESSIONS JQ1498 REFERENCE JQ1494 !$#authors McGeoch, D.J.; Cunningham, C.; McIntyre, G.; Dolan, A. !$#journal J. Gen. Virol. (1991) 72:3057-3075 !$#title Comparative sequence analysis of the long repeat regions and !1adjoining parts of the long unique regions in the genomes of !1herpes simplex viruses types 1 and 2. !$#cross-references MUID:92113549; PMID:1662697 !$#accession JQ1498 !'##molecule_type DNA !'##residues 1-512 ##label MCG !'##cross-references GB:D10471; DDBJ:D01128; NID:g221784; !1PIDN:BAA01269.1; PID:g221788 GENETICS !$#gene UL54 CLASSIFICATION #superfamily varicella-zoster virus gene 4 protein KEYWORDS transcription regulation SUMMARY #length 512 #molecular-weight 54958 #checksum 4201 SEQUENCE /// ENTRY WZBEA4 #type complete TITLE transcription activator - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS F36795 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession F36795 !'##molecule_type DNA !'##residues 1-470 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02440.1; !1PID:g330797 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 5 CLASSIFICATION #superfamily varicella-zoster virus gene 4 protein KEYWORDS transcription regulation SUMMARY #length 470 #molecular-weight 51320 #checksum 535 SEQUENCE /// ENTRY B42746 #type complete TITLE transcription activator - equine herpesvirus 1 (strain Kentucky A) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 02-Jul-1998 ACCESSIONS B42746 REFERENCE A42746 !$#authors Zhao, Y.; Holden, V.R.; Harty, R.N.; O'Callaghan, D.J. !$#journal J. Virol. (1992) 66:5363-5372 !$#title Identification and transcriptional analyses of the UL3 and !1UL4 genes of equine herpesvirus 1, homologs of the ICP27 and !1glycoprotein K genes of herpes simplex virus. !$#cross-references MUID:92365125; PMID:1323700 !$#accession B42746 !'##molecule_type DNA !'##residues 1-470 ##label ZHA !'##cross-references GB:S43139 CLASSIFICATION #superfamily varicella-zoster virus gene 4 protein KEYWORDS transcription regulation; zinc finger FEATURE !$441-466 #region zinc finger SUMMARY #length 470 #molecular-weight 51389 #checksum 567 SEQUENCE /// ENTRY WZBE7 #type complete TITLE gene 7 protein - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS G27212 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession G27212 !'##molecule_type DNA !'##residues 1-259 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27890.1; !1PID:g59996 GENETICS !$#gene 7 CLASSIFICATION #superfamily varicella-zoster virus gene 7 protein SUMMARY #length 259 #molecular-weight 28246 #checksum 7081 SEQUENCE /// ENTRY WMBEY1 #type complete TITLE UL51 protein - human herpesvirus 1 (strain 17) ORGANISM #formal_name human herpesvirus 1 DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jun-2000 ACCESSIONS F30089 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession F30089 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-244 ##label MCG !'##cross-references GB:X14112; NID:g1944536; PIDN:CAA32302.1; !1PID:g59551; GB:D00317 GENETICS !$#gene UL51 CLASSIFICATION #superfamily varicella-zoster virus gene 7 protein SUMMARY #length 244 #molecular-weight 25470 #checksum 6808 SEQUENCE /// ENTRY WZBEA7 #type complete TITLE gene 8 protein - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS I36795 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession I36795 !'##molecule_type DNA !'##residues 1-245 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02443.1; !1PID:g330800 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 8 CLASSIFICATION #superfamily varicella-zoster virus gene 7 protein SUMMARY #length 245 #molecular-weight 26365 #checksum 1342 SEQUENCE /// ENTRY WZBE9 #type complete TITLE gene 9 protein - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS I27212 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession I27212 !'##molecule_type DNA !'##residues 1-302 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27892.1; !1PID:g59998 GENETICS !$#gene 9 CLASSIFICATION #superfamily varicella-zoster virus gene 9 protein SUMMARY #length 302 #molecular-weight 32846 #checksum 3700 SEQUENCE /// ENTRY WMBEF9 #type complete TITLE UL49 protein - human herpesvirus 1 (strain 17) ORGANISM #formal_name human herpesvirus 1 DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jun-2000 ACCESSIONS D30089 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession D30089 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-301 ##label MCG !'##cross-references GB:X14112; NID:g1944536; PIDN:CAA32299.1; !1PID:g59549; GB:D00317 GENETICS !$#gene UL49 CLASSIFICATION #superfamily varicella-zoster virus gene 9 protein SUMMARY #length 301 #molecular-weight 32254 #checksum 3872 SEQUENCE /// ENTRY WZBEA9 #type complete TITLE 33.2K tegument protein - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS C36796 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession C36796 !'##molecule_type DNA !'##residues 1-304 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02446.1; !1PID:g330803 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 11 CLASSIFICATION #superfamily varicella-zoster virus gene 9 protein SUMMARY #length 304 #molecular-weight 33240 #checksum 5777 SEQUENCE /// ENTRY TNBE11 #type complete TITLE 91.8K alpha trans-inducing protein - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS B27342 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession B27342 !'##molecule_type DNA !'##residues 1-819 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27894.1; !1PID:g60000 GENETICS !$#gene 11 CLASSIFICATION #superfamily herpesvirus 70.5K alpha trans-inducing protein KEYWORDS trans-inducing protein; transcription regulation SUMMARY #length 819 #molecular-weight 91829 #checksum 604 SEQUENCE /// ENTRY TNBE70 #type complete TITLE 70.5K alpha trans-inducing protein - human herpesvirus 1 (strain F) ORGANISM #formal_name human herpesvirus 1 DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS A26133 REFERENCE A93031 !$#authors McKnight, J.L.C.; Pellett, P.E.; Jenkins, F.J.; Roizman, B. !$#journal J. Virol. (1987) 61:992-1001 !$#title Characterization and nucleotide sequence of two herpes !1simplex virus 1 genes whose products modulate !1alpha-trans-inducing factor-dependent activation of alpha !1genes. !$#cross-references MUID:87141362; PMID:3029433 !$#accession A26133 !'##molecule_type DNA !'##residues 1-664 ##label MCK !'##cross-references GB:M15621; NID:g330056; PIDN:AAA45767.1; !1PID:g330057 COMMENT This protein may reduce transcriptional activity of the !1alpha genes. CLASSIFICATION #superfamily herpesvirus 70.5K alpha trans-inducing protein KEYWORDS trans-inducing protein; transcription regulation SUMMARY #length 664 #molecular-weight 70526 #checksum 2153 SEQUENCE /// ENTRY TNBEF7 #type complete TITLE 73.8K alpha trans-inducing protein - human herpesvirus 1 (strain 17) ORGANISM #formal_name human herpesvirus 1 DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jun-2000 ACCESSIONS B30089 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession B30089 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-693 ##label MCG !'##cross-references GB:X14112; NID:g1944536; PIDN:CAA32297.1; !1PID:g59547; GB:D00317 GENETICS !$#gene UL47 CLASSIFICATION #superfamily herpesvirus 70.5K alpha trans-inducing protein KEYWORDS trans-inducing protein; transcription regulation SUMMARY #length 693 #molecular-weight 73816 #checksum 7173 SEQUENCE /// ENTRY TNBEEH #type complete TITLE 97K alpha trans-inducing protein - equine herpesvirus 4 (strain MD) ALTERNATE_NAMES tegument protein ORGANISM #formal_name equine herpesvirus 4 DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 21-Jul-2000 ACCESSIONS A37992; S36708 REFERENCE A37992 !$#authors Whittaker, G.R.; Riggio, M.P.; Halliburton, I.W.; !1Killington, R.A.; Allen, G.P.; Meredith, D.M. !$#journal J. Virol. (1991) 65:2320-2326 !$#title Antigenic and protein sequence homology between VP13/14, a !1herpes simplex virus type 1 tegument protein, and gp10, a !1glycoprotein of equine herpesvirus 1 and 4. !$#cross-references MUID:91202570; PMID:1850013 !$#accession A37992 !'##molecule_type DNA !'##residues 1-872 ##label WHI !'##cross-references EMBL:X17684; NID:g2578026; PIDN:CAA35672.1; !1PID:g59221 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1989 CLASSIFICATION #superfamily herpesvirus 70.5K alpha trans-inducing protein KEYWORDS trans-inducing protein; transcription regulation SUMMARY #length 872 #molecular-weight 97376 #checksum 7102 SEQUENCE /// ENTRY TNBEA1 #type complete TITLE 97K alpha trans-inducing protein - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS E36796 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession E36796 !'##molecule_type DNA !'##residues 1-871 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02448.1; !1PID:g330805 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 13 CLASSIFICATION #superfamily herpesvirus 70.5K alpha trans-inducing protein KEYWORDS trans-inducing protein; transcription SUMMARY #length 871 #molecular-weight 96970 #checksum 2982 SEQUENCE /// ENTRY TNBEB1 #type complete TITLE 80.7K alpha trans-inducing protein - bovine herpesvirus 1 (strain P8-2) ALTERNATE_NAMES BHV-1 protein homolog; VP8 protein ORGANISM #formal_name bovine herpesvirus 1 DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jun-2000 ACCESSIONS JQ1435; S24227 REFERENCE JQ1435 !$#authors Carpenter, D.E.; Misra, V. !$#journal J. Gen. Virol. (1991) 72:3077-3084 !$#title The most abundant protein in bovine herpes 1 virions is a !1homologue of herpes simplex virus type 1 UL47. !$#cross-references MUID:92113550; PMID:1662698 !$#accession JQ1435 !'##molecule_type DNA !'##residues 1-742 ##label CAR !'##cross-references GB:Z11610; NID:g1065725; PIDN:CAA77683.1; !1PID:g1067128 COMMENT This protein is synthesized in the later stages of infection !1and is a phosphoprotein. GENETICS !$#gene VP8 !$#map_position 0.088-0.108 CLASSIFICATION #superfamily herpesvirus 70.5K alpha trans-inducing protein KEYWORDS trans-inducing protein; transcription SUMMARY #length 742 #molecular-weight 80743 #checksum 4009 SEQUENCE /// ENTRY JQ1893 #type complete TITLE 80.7K alpha trans-inducing protein - bovine herpesvirus 1 (strain 34) ALTERNATE_NAMES VP8 protein; VP8 tegument protein ORGANISM #formal_name bovine herpesvirus 1 DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS JQ1893 REFERENCE JQ1893 !$#authors LaBoissiere, S.; Trudel, M.; Simard, C. !$#journal J. Gen. Virol. (1992) 73:2941-2947 !$#title Characterization and transcript mapping of a bovine !1herpesvirus type 1 gene encoding a polypeptide homologous to !1the herpes simplex virus type 1 major tegument proteins !1VP13/14. !$#cross-references MUID:93057366; PMID:1331296 !$#accession JQ1893 !'##molecule_type DNA !'##residues 1-739 ##label LAB !'##cross-references GB:M84469; NID:g330773; PIDN:AAA46064.1; !1PID:g330774 GENETICS !$#gene VP8 CLASSIFICATION #superfamily herpesvirus 70.5K alpha trans-inducing protein KEYWORDS trans-inducing protein; transcription SUMMARY #length 739 #molecular-weight 80756 #checksum 8371 SEQUENCE /// ENTRY TNBE12 #type complete TITLE 74K alpha trans-inducing protein - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS C27342 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession C27342 !'##molecule_type DNA !'##residues 1-661 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27895.1; !1PID:g60001 GENETICS !$#gene 12 CLASSIFICATION #superfamily herpesvirus 77K alpha trans-inducing protein KEYWORDS trans-inducing protein; transcription regulation SUMMARY #length 661 #molecular-weight 74272 #checksum 7006 SEQUENCE /// ENTRY TNBE77 #type complete TITLE 77K alpha trans-inducing protein - human herpesvirus 1 (strain F) ORGANISM #formal_name human herpesvirus 1 DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS B26133 REFERENCE A93031 !$#authors McKnight, J.L.C.; Pellett, P.E.; Jenkins, F.J.; Roizman, B. !$#journal J. Virol. (1987) 61:992-1001 !$#title Characterization and nucleotide sequence of two herpes !1simplex virus 1 genes whose products modulate !1alpha-trans-inducing factor-dependent activation of alpha !1genes. !$#cross-references MUID:87141362; PMID:3029433 !$#accession B26133 !'##molecule_type DNA !'##residues 1-715 ##label MCK !'##cross-references GB:M15621; NID:g330056; PIDN:AAA45768.1; !1PID:g330058 COMMENT This protein may enhance transcriptional activity of the !1alpha genes. CLASSIFICATION #superfamily herpesvirus 77K alpha trans-inducing protein KEYWORDS trans-inducing protein; transcription regulation SUMMARY #length 715 #molecular-weight 77356 #checksum 1578 SEQUENCE /// ENTRY TNBEF6 #type complete TITLE 77K alpha trans-inducing protein - human herpesvirus 1 (strain 17) ORGANISM #formal_name human herpesvirus 1 DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jun-2000 ACCESSIONS A30089 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession A30089 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-718 ##label MCG !'##cross-references GB:X14112; GB:D10879; GB:D00317; NID:g221721; !1PIDN:BAA01692.1; PID:g221767 COMMENT This protein may enhance transcriptional activity of the !1alpha genes. GENETICS !$#gene UL46 CLASSIFICATION #superfamily herpesvirus 77K alpha trans-inducing protein KEYWORDS trans-inducing protein; transcription regulation SUMMARY #length 718 #molecular-weight 78243 #checksum 353 SEQUENCE /// ENTRY TNBEA2 #type complete TITLE 82.3K alpha trans-inducing protein - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS F36796 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession F36796 !'##molecule_type DNA !'##residues 1-747 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02449.1; !1PID:g330806 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 14 CLASSIFICATION #superfamily herpesvirus 77K alpha trans-inducing protein KEYWORDS trans-inducing protein; transcription SUMMARY #length 747 #molecular-weight 82309 #checksum 7288 SEQUENCE /// ENTRY WMBEX7 #type complete TITLE UL7 protein - human herpesvirus 1 (strain 17) ORGANISM #formal_name human herpesvirus 1 DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jun-2000 ACCESSIONS G28133 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession G28133 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-296 ##label MCG !'##cross-references GB:X14112; NID:g1944536; PIDN:CAA32343.1; !1PID:g59508; GB:D00317 GENETICS !$#gene UL7 CLASSIFICATION #superfamily herpesvirus UL7 protein SUMMARY #length 296 #molecular-weight 33059 #checksum 8178 SEQUENCE /// ENTRY WMBEX8 #type complete TITLE UL8 protein - human herpesvirus 1 (strain 17) ORGANISM #formal_name human herpesvirus 1 DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jun-2000 ACCESSIONS C29890; H28133 REFERENCE A93040 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Dolan, A.; McNab, D.; Perry, !1L.J.; Taylor, P.; Challberg, M.D. !$#journal J. Virol. (1988) 62:444-453 !$#title Structures of herpes simplex virus type 1 genes required for !1replication of virus DNA. !$#cross-references MUID:88091053; PMID:2826807 !$#accession C29890 !'##molecule_type DNA !'##residues 1-750 ##label MCG !'##cross-references GB:M19120; NID:g330226; PIDN:AAA45823.1; !1PID:g330235 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession H28133 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-750 ##label MCG2 !'##cross-references GB:X14112; NID:g1944536; PIDN:CAA32344.1; !1PID:g59509; GB:D00317 COMMENT This protein is required for replication of viral DNA. GENETICS !$#gene UL8 CLASSIFICATION #superfamily herpesvirus UL8 protein KEYWORDS DNA biosynthesis SUMMARY #length 750 #molecular-weight 79925 #checksum 2199 SEQUENCE /// ENTRY WMBEF3 #type complete TITLE UL43 protein - human herpesvirus 1 (strain 17) ORGANISM #formal_name human herpesvirus 1 DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jun-2000 ACCESSIONS G30088 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession G30088 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-434 ##label MCG !'##cross-references GB:X14112; NID:g1944536; PIDN:CAA32306.1; !1PID:g59543; GB:D00317 GENETICS !$#gene UL43 CLASSIFICATION #superfamily herpesvirus UL43 protein SUMMARY #length 434 #molecular-weight 44908 #checksum 2327 SEQUENCE /// ENTRY WMBEF5 #type complete TITLE UL45 protein - human herpesvirus 1 (strain 17) ORGANISM #formal_name human herpesvirus 1 DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jun-2000 ACCESSIONS I30088 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession I30088 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-172 ##label MCG !'##cross-references GB:X14112; NID:g1944536; PIDN:CAA32295.1; !1PID:g59545; GB:D00317 GENETICS !$#gene UL45 CLASSIFICATION #superfamily herpesvirus UL45 protein SUMMARY #length 172 #molecular-weight 18180 #checksum 8678 SEQUENCE /// ENTRY WMBEY6 #type complete TITLE UL56 protein - human herpesvirus 1 (strain 17) ORGANISM #formal_name human herpesvirus 1 DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jun-2000 ACCESSIONS B30090 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession B30090 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-197 ##label MCG !'##cross-references GB:X14112; GB:D10879; GB:D00317; NID:g221721; !1PIDN:BAA01702.1; PID:g221777 GENETICS !$#gene UL56 CLASSIFICATION #superfamily herpesvirus UL56 protein SUMMARY #length 197 #molecular-weight 21183 #checksum 6901 SEQUENCE /// ENTRY WMBEXC #type complete TITLE UL56 protein - human herpesvirus 2 (strain HG52) ORGANISM #formal_name human herpesvirus 2 #note host Homo sapiens (man) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jun-2000 ACCESSIONS JQ1500 REFERENCE JQ1494 !$#authors McGeoch, D.J.; Cunningham, C.; McIntyre, G.; Dolan, A. !$#journal J. Gen. Virol. (1991) 72:3057-3075 !$#title Comparative sequence analysis of the long repeat regions and !1adjoining parts of the long unique regions in the genomes of !1herpes simplex viruses types 1 and 2. !$#cross-references MUID:92113549; PMID:1662697 !$#accession JQ1500 !'##molecule_type DNA !'##residues 1-235 ##label MCG !'##cross-references GB:D10471; GB:D01128; NID:g221784; PIDN:BAA01271.1; !1PID:g221790 GENETICS !$#gene UL56 CLASSIFICATION #superfamily herpesvirus UL56 protein SUMMARY #length 235 #molecular-weight 24715 #checksum 8206 SEQUENCE /// ENTRY C48560 #type complete TITLE UL56 protein - human herpesvirus 1 (strain HFEM) ORGANISM #formal_name human herpesvirus 1 DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 04-Mar-1994 ACCESSIONS C48560 REFERENCE A48560 !$#authors Rosen-Wolff, A.; Frank, S.; Raab, K.; Moyal, M.; Becker, Y.; !1Darai, G. !$#journal Virus Res. (1992) 25:189-199 !$#title Determination of the coding capacity of the BamHI DNA !1fragment B of apathogenic Herpes simplex virus type 1 strain !1HFEM by DNA nucleotide sequence analysis. !$#cross-references MUID:93070559; PMID:1332274 !$#accession C48560 !'##molecule_type DNA !'##residues 1-233 ##label ROS !'##note sequence extracted from NCBI backbone (NCBIN:117573, !1NCBIP:117577) GENETICS !$#gene UL56 CLASSIFICATION #superfamily herpesvirus UL56 protein SUMMARY #length 233 #molecular-weight 25296 #checksum 784 SEQUENCE /// ENTRY WZBE15 #type complete TITLE gene 15 protein - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS F27342 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession F27342 !'##molecule_type DNA !'##residues 1-406 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27898.1; !1PID:g60004 GENETICS !$#gene 15 CLASSIFICATION #superfamily varicella-zoster virus gene 15 protein SUMMARY #length 406 #molecular-weight 44524 #checksum 8776 SEQUENCE /// ENTRY WZBEB1 #type complete TITLE gene 17 protein - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS I36796 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession I36796 !'##molecule_type DNA !'##residues 1-401 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02452.1; !1PID:g330809 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 17 CLASSIFICATION #superfamily varicella-zoster virus gene 15 protein SUMMARY #length 401 #molecular-weight 43205 #checksum 1560 SEQUENCE /// ENTRY WZBE16 #type complete TITLE gene 16 protein - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS G27342 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession G27342 !'##molecule_type DNA !'##residues 1-408 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27899.1; !1PID:g60005 GENETICS !$#gene 16 CLASSIFICATION #superfamily varicella-zoster virus gene 16 protein KEYWORDS DNA binding SUMMARY #length 408 #molecular-weight 46090 #checksum 765 SEQUENCE /// ENTRY WMBE42 #type complete TITLE DNA-binding protein - human herpesvirus 1 (strain 17) ALTERNATE_NAMES UL42 protein ORGANISM #formal_name human herpesvirus 1 #note host Homo sapiens (man) DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jun-2000 ACCESSIONS D29890; F30088 REFERENCE A93040 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Dolan, A.; McNab, D.; Perry, !1L.J.; Taylor, P.; Challberg, M.D. !$#journal J. Virol. (1988) 62:444-453 !$#title Structures of herpes simplex virus type 1 genes required for !1replication of virus DNA. !$#cross-references MUID:88091053; PMID:2826807 !$#accession D29890 !'##molecule_type DNA !'##residues 1-488 ##label MCG !'##cross-references GB:M19121; NID:g330227; PIDN:AAA45824.1; !1PID:g330236 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession F30088 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-488 ##label MC2 !'##cross-references GB:X14112; NID:g1944536; PIDN:CAA32305.1; !1PID:g59542; GB:D00317 COMMENT This protein is required for replication of viral DNA. GENETICS !$#gene UL42 CLASSIFICATION #superfamily varicella-zoster virus gene 16 protein KEYWORDS DNA binding; DNA biosynthesis SUMMARY #length 488 #molecular-weight 51159 #checksum 687 SEQUENCE /// ENTRY WZBEB2 #type complete TITLE DNA polymerase processivity factor - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS A36797 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession A36797 !'##molecule_type DNA !'##residues 1-405 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02453.1; !1PID:g330810 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 18 CLASSIFICATION #superfamily varicella-zoster virus gene 16 protein KEYWORDS DNA binding; DNA biosynthesis SUMMARY #length 405 #molecular-weight 45086 #checksum 4317 SEQUENCE /// ENTRY WZBE17 #type complete TITLE gene 17 protein - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS H27342 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession H27342 !'##molecule_type DNA !'##residues 1-455 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27900.1; !1PID:g60006 GENETICS !$#gene 17 CLASSIFICATION #superfamily varicella-zoster virus gene 17 protein SUMMARY #length 455 #molecular-weight 51368 #checksum 3936 SEQUENCE /// ENTRY WMBEF1 #type complete TITLE UL41 protein - human herpesvirus 1 (strain 17) ORGANISM #formal_name human herpesvirus 1 DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jun-2000 ACCESSIONS E30088 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession E30088 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-489 ##label MCG !'##cross-references GB:X14112; NID:g1944536; PIDN:CAA32304.1; !1PID:g59541; GB:D00317 GENETICS !$#gene UL41 CLASSIFICATION #superfamily varicella-zoster virus gene 17 protein SUMMARY #length 489 #molecular-weight 54917 #checksum 5108 SEQUENCE /// ENTRY WZBEB3 #type complete TITLE host shutoff virion protein - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS B36797 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession B36797 !'##molecule_type DNA !'##residues 1-497 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02454.1; !1PID:g330811 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 19 CLASSIFICATION #superfamily varicella-zoster virus gene 17 protein SUMMARY #length 497 #molecular-weight 56542 #checksum 5134 SEQUENCE /// ENTRY A46117 #type complete TITLE host shutoff virion protein - suid herpesvirus 1 (strain Ka) ALTERNATE_NAMES VHS protein ORGANISM #formal_name suid herpesvirus 1 DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 04-Mar-1994 ACCESSIONS A46117 REFERENCE A46117 !$#authors Berthomme, H.; Jacquemont, B.; Epstein, A. !$#journal Virology (1993) 193:1028-1032 !$#title The pseudorabies virus host-shutoff homolog gene: nucleotide !1sequence and comparison with alphaherpesvirus protein !1counterparts. !$#cross-references MUID:93212483; PMID:8384744 !$#accession A46117 !'##molecule_type DNA !'##residues 1-365 ##label BER !'##cross-references GB:S57917 !'##note the authors translated the codon CCG for residue 277 as Arg CLASSIFICATION #superfamily varicella-zoster virus gene 17 protein SUMMARY #length 365 #molecular-weight 40910 #checksum 8709 SEQUENCE /// ENTRY WZBE20 #type complete TITLE gene 20 protein - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS B27343 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession B27343 !'##molecule_type DNA !'##residues 1-483 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27903.1; !1PID:g60009 GENETICS !$#gene 20 CLASSIFICATION #superfamily varicella-zoster virus gene 20 protein KEYWORDS capsid assembly; DNA binding SUMMARY #length 483 #molecular-weight 53971 #checksum 2550 SEQUENCE /// ENTRY WMBEZ8 #type complete TITLE UL38 protein - human herpesvirus 1 (strain 17) ORGANISM #formal_name human herpesvirus 1 DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jun-2000 ACCESSIONS B30088 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession B30088 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-465 ##label MCG !'##cross-references GB:X14112; NID:g1944536; PIDN:CAA32313.1; !1PID:g59538; GB:D00317 GENETICS !$#gene UL38 CLASSIFICATION #superfamily varicella-zoster virus gene 20 protein KEYWORDS capsid assembly; DNA binding SUMMARY #length 465 #molecular-weight 50263 #checksum 1228 SEQUENCE /// ENTRY WMBE44 #type complete TITLE maturation protein - human herpesvirus 1 (strain A44) ORGANISM #formal_name human herpesvirus 1 #note host Homo sapiens (man) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS A31478 REFERENCE A31478 !$#authors Pertuiset, B.; Boccara, M.; Cebrian, J.; Berthelot, N.; !1Chousterman, S.; Puvion-Dutilleul, F.; Sisman, J.; !1Sheldrick, P. !$#journal J. Virol. (1989) 63:2169-2179 !$#title Physical mapping and nucleotide sequence of a herpes simplex !1virus type 1 gene required for capsid assembly. !$#cross-references MUID:89199774; PMID:2539510 !$#accession A31478 !'##molecule_type DNA !'##residues 1-465 ##label PER !'##cross-references GB:M22962; GB:M18454; NID:g330062; PIDN:AAA45769.1; !1PID:g330063 CLASSIFICATION #superfamily varicella-zoster virus gene 20 protein KEYWORDS capsid assembly; DNA binding SUMMARY #length 465 #molecular-weight 50232 #checksum 2147 SEQUENCE /// ENTRY WMBEHT #type complete TITLE capsid protein ICP32/P19c - human herpesvirus 2 ORGANISM #formal_name human herpesvirus 2 DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jul-1999 ACCESSIONS A34111 REFERENCE A34111 !$#authors Yei, S.; Chowdhury, S.I.; Bhat, B.M.; Conley, A.J.; Wold, !1W.S.M.; Batterson, W. !$#journal J. Virol. (1990) 64:1124-1134 !$#title Identification and characterization of the herpes simplex !1virus type 2 gene encoding the essential capsid protein !1ICP32/VP19c. !$#cross-references MUID:90156509; PMID:2154597 !$#accession A34111 !'##molecule_type DNA !'##residues 1-466 ##label YEI !'##cross-references GB:M61774; NID:g330274; PIDN:AAA45844.1; !1PID:g330275 CLASSIFICATION #superfamily varicella-zoster virus gene 20 protein KEYWORDS capsid assembly; capsid protein SUMMARY #length 466 #molecular-weight 50468 #checksum 881 SEQUENCE /// ENTRY WZBEB4 #type complete TITLE 51.3K capsid protein - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS E36797 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession E36797 !'##molecule_type DNA !'##residues 1-465 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02457.1; !1PID:g330814 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 22 CLASSIFICATION #superfamily varicella-zoster virus gene 20 protein KEYWORDS capsid assembly; capsid protein SUMMARY #length 465 #molecular-weight 51306 #checksum 759 SEQUENCE /// ENTRY WZBE21 #type complete TITLE gene 21 protein - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS C27343 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession C27343 !'##molecule_type DNA !'##residues 1-1038 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27904.1; !1PID:g60010 GENETICS !$#gene 21 CLASSIFICATION #superfamily varicella-zoster virus gene 21 protein SUMMARY #length 1038 #molecular-weight 115779 #checksum 5482 SEQUENCE /// ENTRY WMBEH7 #type complete TITLE UL37 protein - human herpesvirus 1 (strain 17) ORGANISM #formal_name human herpesvirus 1 DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jun-2000 ACCESSIONS A30088 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession A30088 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1123 ##label MCG !'##cross-references GB:X14112; NID:g1944536; PIDN:CAA32312.1; !1PID:g59537; GB:D00317 GENETICS !$#gene UL37 CLASSIFICATION #superfamily varicella-zoster virus gene 21 protein SUMMARY #length 1123 #molecular-weight 120555 #checksum 2296 SEQUENCE /// ENTRY WZBEB5 #type complete TITLE gene 23 protein - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS F36797 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession F36797 !'##molecule_type DNA !'##residues 1-1020 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02458.1; !1PID:g330815 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 23 CLASSIFICATION #superfamily varicella-zoster virus gene 21 protein SUMMARY #length 1020 #molecular-weight 111610 #checksum 285 SEQUENCE /// ENTRY WZBE22 #type complete TITLE gene 22 protein - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS D27343 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession D27343 !'##molecule_type DNA !'##residues 1-2763 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27905.1; !1PID:g60011 GENETICS !$#gene 22 CLASSIFICATION #superfamily varicella-zoster virus gene 22 protein SUMMARY #length 2763 #molecular-weight 306339 #checksum 6847 SEQUENCE /// ENTRY WMBEH6 #type complete TITLE UL36 protein - human herpesvirus 1 (strain 17) ORGANISM #formal_name human herpesvirus 1 DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jun-2000 ACCESSIONS I30085 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession I30085 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-3164 ##label MCG !'##cross-references GB:X14112; NID:g1944536; PIDN:CAA32311.1; !1PID:g59536; GB:D00317 GENETICS !$#gene UL36 CLASSIFICATION #superfamily varicella-zoster virus gene 22 protein SUMMARY #length 3164 #molecular-weight 335858 #checksum 8069 SEQUENCE /// ENTRY WZBEB6 #type complete TITLE 367K tegument protein - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS G36797 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession G36797 !'##molecule_type DNA !'##residues 1-3421 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02459.1; !1PID:g330816 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 24 CLASSIFICATION #superfamily varicella-zoster virus gene 22 protein SUMMARY #length 3421 #molecular-weight 367079 #checksum 2318 SEQUENCE /// ENTRY WZBEZ4 #type complete TITLE 240K tegument protein (clone pZVH14) - human herpesvirus 6 (strain GS) ORGANISM #formal_name human herpesvirus 6 #note host Homo sapiens (man) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS H40511 REFERENCE A40511 !$#authors Josephs, S.F.; Ablashi, D.V.; Salahuddin, S.Z.; Jagodzinski, !1L.L.; Wong-Staal, F.; Gallo, R.C. !$#journal J. Virol. (1991) 65:5597-5604 !$#title Identification of the human herpesvirus 6 glycoprotein H and !1putative large tegument protein genes. !$#cross-references MUID:91374623; PMID:1654455 !$#accession H40511 !'##molecule_type DNA !'##residues 1-2077 ##label JOS !'##cross-references GB:S57540; NID:g235435; PIDN:AAB19786.1; !1PID:g235439 CLASSIFICATION #superfamily varicella-zoster virus 240K tegument protein SUMMARY #length 2077 #molecular-weight 239908 #checksum 5261 SEQUENCE /// ENTRY WZBE23 #type complete TITLE gene 23 protein - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS E27343 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession E27343 !'##molecule_type DNA !'##residues 1-235 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27906.1; !1PID:g60012 GENETICS !$#gene 23 CLASSIFICATION #superfamily varicella-zoster virus gene 23 protein; human !1herpesvirus 1 UL35 protein homology FEATURE !$16-104 #domain human herpesvirus 1 UL35 protein homology !8#label UL35 SUMMARY #length 235 #molecular-weight 24417 #checksum 6198 SEQUENCE /// ENTRY WMBEH5 #type complete TITLE UL35 protein - human herpesvirus 1 (strain 17) ORGANISM #formal_name human herpesvirus 1 DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jun-2000 ACCESSIONS H30085 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession H30085 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-112 ##label MCG !'##cross-references GB:X14112; NID:g1944536; PIDN:CAA32310.1; !1PID:g59535; GB:D00317 GENETICS !$#gene UL35 CLASSIFICATION #superfamily human herpesvirus 1 UL35 protein; human !1herpesvirus 1 UL35 protein homology FEATURE !$9-100 #domain human herpesvirus 1 UL35 protein homology !8#label UL35 SUMMARY #length 112 #molecular-weight 12096 #checksum 6178 SEQUENCE /// ENTRY WZBEB7 #type complete TITLE 13.6K capsid protein - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS H36797 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession H36797 !'##molecule_type DNA !'##residues 1-119 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02460.1; !1PID:g330817 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 25 CLASSIFICATION #superfamily human herpesvirus 1 UL35 protein; human !1herpesvirus 1 UL35 protein homology KEYWORDS capsid protein FEATURE !$19-110 #domain human herpesvirus 1 UL35 protein homology !8#label UL35 SUMMARY #length 119 #molecular-weight 13596 #checksum 4224 SEQUENCE /// ENTRY WZBE24 #type complete TITLE gene 24 protein - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS F27343 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession F27343 !'##molecule_type DNA !'##residues 1-269 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27907.1; !1PID:g60013 GENETICS !$#gene 24 CLASSIFICATION #superfamily varicella-zoster virus gene 24 protein SUMMARY #length 269 #molecular-weight 30452 #checksum 5812 SEQUENCE /// ENTRY WMBEH4 #type complete TITLE UL34 protein - human herpesvirus 1 (strain 17) ORGANISM #formal_name human herpesvirus 1 DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jun-2000 ACCESSIONS G30085 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession G30085 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-275 ##label MCG !'##cross-references GB:X14112; NID:g1944536; PIDN:CAA32309.1; !1PID:g59534; GB:D00317 GENETICS !$#gene UL34 CLASSIFICATION #superfamily varicella-zoster virus gene 24 protein SUMMARY #length 275 #molecular-weight 29790 #checksum 5767 SEQUENCE /// ENTRY WZBEB8 #type complete TITLE gene 26 protein - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS I36797 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession I36797 !'##molecule_type DNA !'##residues 1-275 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02461.1; !1PID:g330818 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 26 CLASSIFICATION #superfamily varicella-zoster virus gene 24 protein SUMMARY #length 275 #molecular-weight 30680 #checksum 9217 SEQUENCE /// ENTRY WZBE25 #type complete TITLE gene 25 protein - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS G27343 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession G27343 !'##molecule_type DNA !'##residues 1-156 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27909.1; !1PID:g60015 GENETICS !$#gene 25 CLASSIFICATION #superfamily varicella-zoster virus gene 25 protein SUMMARY #length 156 #molecular-weight 17461 #checksum 684 SEQUENCE /// ENTRY WMBEH3 #type complete TITLE UL33 protein - human herpesvirus 1 (strain 17) ORGANISM #formal_name human herpesvirus 1 DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jun-2000 ACCESSIONS F30085 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession F30085 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-130 ##label MCG !'##cross-references GB:X14112; NID:g1944536; PIDN:CAA32308.1; !1PID:g59532; GB:D00317 GENETICS !$#gene UL33 CLASSIFICATION #superfamily varicella-zoster virus gene 25 protein SUMMARY #length 130 #molecular-weight 14437 #checksum 7400 SEQUENCE /// ENTRY WZBEB9 #type complete TITLE gene 27 protein - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS A36798 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession A36798 !'##molecule_type DNA !'##residues 1-162 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02462.1; !1PID:g330819 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 27 CLASSIFICATION #superfamily varicella-zoster virus gene 25 protein SUMMARY #length 162 #molecular-weight 17994 #checksum 9529 SEQUENCE /// ENTRY WZBE32 #type complete TITLE gene 32 protein - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS F27214 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession F27214 !'##molecule_type DNA !'##residues 1-143 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27915.1; !1PID:g60021 GENETICS !$#gene 32 CLASSIFICATION #superfamily varicella-zoster virus gene 32 protein SUMMARY #length 143 #molecular-weight 15981 #checksum 7527 SEQUENCE /// ENTRY WZBEC7 #type complete TITLE gene 34 protein - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS H36798 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession H36798 !'##molecule_type DNA !'##residues 1-160 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02469.1; !1PID:g330826 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 34 CLASSIFICATION #superfamily varicella-zoster virus gene 32 protein SUMMARY #length 160 #molecular-weight 17306 #checksum 9257 SEQUENCE /// ENTRY WZBE38 #type complete TITLE gene 38 protein - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS C27341 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession C27341 !'##molecule_type DNA !'##residues 1-541 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27921.1; !1PID:g60027 GENETICS !$#gene 38 CLASSIFICATION #superfamily varicella-zoster virus gene 38 protein SUMMARY #length 541 #molecular-weight 60398 #checksum 4545 SEQUENCE /// ENTRY WMBEW1 #type complete TITLE UL21 protein - human herpesvirus 1 (strain 17) ORGANISM #formal_name human herpesvirus 1 DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jun-2000 ACCESSIONS C30084 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession C30084 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-535 ##label MCG !'##cross-references GB:X14112; NID:g1944536; PIDN:CAA32334.1; !1PID:g59521; GB:D00317 GENETICS !$#gene UL21 CLASSIFICATION #superfamily varicella-zoster virus gene 38 protein SUMMARY #length 535 #molecular-weight 57641 #checksum 7651 SEQUENCE /// ENTRY A44195 #type complete TITLE UL21 protein homolog - suid herpesvirus 1 (strain NIA-3) ORGANISM #formal_name suid herpesvirus 1 DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS A44195 REFERENCE A44195 !$#authors de Wind, N.; Wagenaar, F.; Pol, J.; Kimman, T.; Berns, A. !$#journal J. Virol. (1992) 66:7096-7103 !$#title The pseudorabies virus homolog of the herpes simplex virus !1UL21 gene product is a capsid protein which is involved in !1capsid maturation. !$#cross-references MUID:93059656; PMID:1331512 !$#accession A44195 !'##molecule_type DNA !'##residues 1-523 ##label DEA !'##cross-references GB:M95285; NID:g334080; PIDN:AAA47474.1; !1PID:g334083 CLASSIFICATION #superfamily varicella-zoster virus gene 38 protein KEYWORDS leucine zipper FEATURE !$106-127 #region leucine zipper motif SUMMARY #length 523 #molecular-weight 55019 #checksum 4328 SEQUENCE /// ENTRY WZBED4 #type complete TITLE gene 40 protein - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS F36799 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession F36799 !'##molecule_type DNA !'##residues 1-530 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02476.1; !1PID:g330833 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 40 CLASSIFICATION #superfamily varicella-zoster virus gene 38 protein SUMMARY #length 530 #molecular-weight 57915 #checksum 2715 SEQUENCE /// ENTRY WZBE39 #type complete TITLE gene 39 protein - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS D27341 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession D27341 !'##molecule_type DNA !'##residues 1-240 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27922.1; !1PID:g60028 GENETICS !$#gene 39 CLASSIFICATION #superfamily varicella-zoster virus gene 39 protein SUMMARY #length 240 #molecular-weight 27079 #checksum 7188 SEQUENCE /// ENTRY WMBEWN #type complete TITLE UL20 protein - human herpesvirus 1 (strain 17) ORGANISM #formal_name human herpesvirus 1 DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jun-2000 ACCESSIONS B30084 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession B30084 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-222 ##label MCG !'##cross-references GB:X14112; NID:g1944536; PIDN:CAA32333.1; !1PID:g59520; GB:D00317 GENETICS !$#gene UL20 CLASSIFICATION #superfamily varicella-zoster virus gene 39 protein SUMMARY #length 222 #molecular-weight 24231 #checksum 5542 SEQUENCE /// ENTRY WZBED5 #type complete TITLE 26.5K membrane protein - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS G36799 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession G36799 !'##molecule_type DNA !'##residues 1-239 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02477.1; !1PID:g330834 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 41 CLASSIFICATION #superfamily varicella-zoster virus gene 39 protein KEYWORDS transmembrane protein FEATURE !$65-81 #domain transmembrane #status predicted #label TM1\ !$140-156 #domain transmembrane #status predicted #label TM2\ !$189-208 #domain transmembrane #status predicted #label TM3 SUMMARY #length 239 #molecular-weight 26535 #checksum 1891 SEQUENCE /// ENTRY WZBE41 #type complete TITLE gene 41 protein - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS F27341 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession F27341 !'##molecule_type DNA !'##residues 1-316 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27924.1; !1PID:g60030 GENETICS !$#gene 41 CLASSIFICATION #superfamily varicella-zoster virus gene 41 protein SUMMARY #length 316 #molecular-weight 34389 #checksum 9989 SEQUENCE /// ENTRY WZBED7 #type complete TITLE 33.8K capsid protein - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS I36799 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession I36799 !'##molecule_type DNA !'##residues 1-314 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02479.1; !1PID:g330836 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 43 CLASSIFICATION #superfamily varicella-zoster virus gene 41 protein KEYWORDS capsid protein SUMMARY #length 314 #molecular-weight 33841 #checksum 5859 SEQUENCE /// ENTRY WMBET8 #type complete TITLE UL18 protein - human herpesvirus 1 (strain 17) ALTERNATE_NAMES capsid protein VP23 ORGANISM #formal_name human herpesvirus 1 DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jun-2000 ACCESSIONS I30083; PQ0546 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession I30083 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-318 ##label MCG !'##cross-references GB:X14112; NID:g1944536; PIDN:CAA32331.1; !1PID:g59518; GB:D00317 REFERENCE PQ0544 !$#authors Davison, M.D.; Rixon, F.J.; Davison, A.J. !$#journal J. Gen. Virol. (1992) 73:2709-2713 !$#title Identification of genes encoding two capsid proteins (VP24 !1and VP26) of herpes simplex virus type 1. !$#cross-references MUID:93019027; PMID:1328483 !$#accession PQ0546 !'##molecule_type protein !'##residues 1-13 ##label DAV !'##experimental_source strain 17 GENETICS !$#gene UL18 CLASSIFICATION #superfamily varicella-zoster virus gene 41 protein KEYWORDS capsid protein SUMMARY #length 318 #molecular-weight 34270 #checksum 7650 SEQUENCE /// ENTRY WZBE43 #type complete TITLE gene 43 protein - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS H27341 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession H27341 !'##molecule_type DNA !'##residues 1-676 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27926.1; !1PID:g60032 GENETICS !$#gene 43 CLASSIFICATION #superfamily varicella-zoster virus gene 43 protein SUMMARY #length 676 #molecular-weight 73908 #checksum 4254 SEQUENCE /// ENTRY WMBET7 #type complete TITLE UL17 protein - human herpesvirus 1 (strain 17) ORGANISM #formal_name human herpesvirus 1 DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jun-2000 ACCESSIONS H30083 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession H30083 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-703 ##label MCG !'##cross-references GB:X14112; NID:g1944536; PIDN:CAA32329.1; !1PID:g59517; GB:D00317 GENETICS !$#gene UL17 CLASSIFICATION #superfamily varicella-zoster virus gene 43 protein SUMMARY #length 703 #molecular-weight 74581 #checksum 3162 SEQUENCE /// ENTRY WZBED8 #type complete TITLE gene 45 protein - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS A36800 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession A36800 !'##molecule_type DNA !'##residues 1-706 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02481.1; !1PID:g330837 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 45 CLASSIFICATION #superfamily varicella-zoster virus gene 43 protein SUMMARY #length 706 #molecular-weight 76320 #checksum 8937 SEQUENCE /// ENTRY WZBE44 #type complete TITLE gene 44 protein - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS I27341 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession I27341 !'##molecule_type DNA !'##residues 1-363 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27927.1; !1PID:g60033 GENETICS !$#gene 44 CLASSIFICATION #superfamily varicella-zoster virus gene 44 protein SUMMARY #length 363 #molecular-weight 40244 #checksum 258 SEQUENCE /// ENTRY WZBED9 #type complete TITLE gene 46 protein - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS B36800 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession B36800 !'##molecule_type DNA !'##residues 1-370 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02482.1; !1PID:g330838 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 46 CLASSIFICATION #superfamily varicella-zoster virus gene 44 protein SUMMARY #length 370 #molecular-weight 40802 #checksum 5428 SEQUENCE /// ENTRY WMBET6 #type complete TITLE UL16 protein - human herpesvirus 1 (strain 17) ORGANISM #formal_name human herpesvirus 1 DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jun-2000 ACCESSIONS G30083 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession G30083 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-373 ##label MCG !'##cross-references GB:X14112; NID:g1944536; PIDN:CAA32328.1; !1PID:g59516; GB:D00317 GENETICS !$#gene UL16 CLASSIFICATION #superfamily varicella-zoster virus gene 44 protein SUMMARY #length 373 #molecular-weight 40442 #checksum 4482 SEQUENCE /// ENTRY WZBE49 #type complete TITLE gene 49 protein - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS E27344 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession E27344 !'##molecule_type DNA !'##residues 1-81 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27932.1; !1PID:g60038 GENETICS !$#gene 49 CLASSIFICATION #superfamily varicella-zoster virus gene 49 protein SUMMARY #length 81 #molecular-weight 8908 #checksum 6823 SEQUENCE /// ENTRY WZBE51 #type complete TITLE gene 51 protein - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS G27344 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession G27344 !'##molecule_type DNA !'##residues 1-835 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27933.1; !1PID:g60039 GENETICS !$#gene 51 CLASSIFICATION #superfamily varicella-zoster virus gene 51 protein KEYWORDS DNA binding SUMMARY #length 835 #molecular-weight 94374 #checksum 6744 SEQUENCE /// ENTRY WMBEU9 #type complete TITLE gene UL9 protein - human herpesvirus 1 (strain 17) ORGANISM #formal_name human herpesvirus 1 #note host Homo sapiens (man) DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jun-2000 ACCESSIONS B29890; I28133 REFERENCE A93040 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Dolan, A.; McNab, D.; Perry, !1L.J.; Taylor, P.; Challberg, M.D. !$#journal J. Virol. (1988) 62:444-453 !$#title Structures of herpes simplex virus type 1 genes required for !1replication of virus DNA. !$#cross-references MUID:88091053; PMID:2826807 !$#accession B29890 !'##molecule_type DNA !'##residues 1-851 ##label MCG !'##cross-references GB:M19120; NID:g330226; PIDN:AAA45822.1; !1PID:g330234 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession I28133 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-851 ##label MC2 !'##cross-references GB:D10879; NID:g221721; PIDN:BAA01655.1; !1PID:g221731; GB:D00317 GENETICS !$#gene UL9 FUNCTION !$#description required for replication of viral DNA CLASSIFICATION #superfamily varicella-zoster virus gene 51 protein KEYWORDS DNA binding; DNA biosynthesis SUMMARY #length 851 #molecular-weight 94261 #checksum 5609 SEQUENCE /// ENTRY WZBEE5 #type complete TITLE gene 53 protein - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS H36800 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession H36800 !'##molecule_type DNA !'##residues 1-887 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02488.1; !1PID:g330844 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 53 CLASSIFICATION #superfamily varicella-zoster virus gene 51 protein KEYWORDS DNA binding SUMMARY #length 887 #molecular-weight 97275 #checksum 9738 SEQUENCE /// ENTRY WZBE52 #type complete TITLE gene 52 protein - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS H27344 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession H27344 !'##molecule_type DNA !'##residues 1-771 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27935.1; !1PID:g60041 GENETICS !$#gene 52 CLASSIFICATION #superfamily varicella-zoster virus gene 52 protein SUMMARY #length 771 #molecular-weight 86347 #checksum 8722 SEQUENCE /// ENTRY WZBEE6 #type complete TITLE 77.8K DNA helicase/primase-associated protein - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS I36800 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession I36800 !'##molecule_type DNA !'##residues 1-716 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02489.1; !1PID:g330845 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 54 CLASSIFICATION #superfamily varicella-zoster virus gene 52 protein SUMMARY #length 716 #molecular-weight 77772 #checksum 2089 SEQUENCE /// ENTRY WZBE53 #type complete TITLE gene 53 protein - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS A27215 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession A27215 !'##molecule_type DNA !'##residues 1-331 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27936.1; !1PID:g60042 GENETICS !$#gene 53 CLASSIFICATION #superfamily varicella-zoster virus gene 53 protein SUMMARY #length 331 #molecular-weight 37418 #checksum 5142 SEQUENCE /// ENTRY WZBEE7 #type complete TITLE gene 55 protein - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS A36801 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession A36801 !'##molecule_type DNA !'##residues 1-303 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02490.1; !1PID:g330846 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 55 CLASSIFICATION #superfamily varicella-zoster virus gene 53 protein SUMMARY #length 303 #molecular-weight 33854 #checksum 162 SEQUENCE /// ENTRY WZBE56 #type complete TITLE gene 56 protein - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS D27215 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession D27215 !'##molecule_type DNA !'##residues 1-244 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27939.1; !1PID:g60045 GENETICS !$#gene 56 CLASSIFICATION #superfamily varicella-zoster virus gene 56 protein SUMMARY #length 244 #molecular-weight 27167 #checksum 3095 SEQUENCE /// ENTRY WMBEX4 #type complete TITLE UL4 protein - human herpesvirus 1 (strain 17) ORGANISM #formal_name human herpesvirus 1 DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jun-2000 ACCESSIONS D28133 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession D28133 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-199 ##label MCG !'##cross-references GB:X14112; NID:g1944536; PIDN:CAA32340.1; !1PID:g59505; GB:D00317 GENETICS !$#gene UL4 CLASSIFICATION #superfamily varicella-zoster virus gene 56 protein SUMMARY #length 199 #molecular-weight 21517 #checksum 9309 SEQUENCE /// ENTRY WMBEHL #type complete TITLE UL4 protein - human herpesvirus 2 (strain HG52) ORGANISM #formal_name human herpesvirus 2 #note host Homo sapiens (man) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jun-2000 ACCESSIONS JQ1497 REFERENCE JQ1494 !$#authors McGeoch, D.J.; Cunningham, C.; McIntyre, G.; Dolan, A. !$#journal J. Gen. Virol. (1991) 72:3057-3075 !$#title Comparative sequence analysis of the long repeat regions and !1adjoining parts of the long unique regions in the genomes of !1herpes simplex viruses types 1 and 2. !$#cross-references MUID:92113549; PMID:1662697 !$#accession JQ1497 !'##molecule_type DNA !'##residues 1-201 ##label MCG !'##cross-references GB:D10470; DDBJ:D01127; NID:g221791; !1PIDN:BAA21332.1; PID:g2252468 GENETICS !$#gene UL4 CLASSIFICATION #superfamily varicella-zoster virus gene 56 protein SUMMARY #length 201 #molecular-weight 21806 #checksum 7507 SEQUENCE /// ENTRY WZBEF1 #type complete TITLE gene 58 protein - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS D36801 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession D36801 !'##molecule_type DNA !'##residues 1-225 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02493.1; !1PID:g330849 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 58 CLASSIFICATION #superfamily varicella-zoster virus gene 56 protein SUMMARY #length 225 #molecular-weight 24287 #checksum 367 SEQUENCE /// ENTRY WZBE57 #type complete TITLE gene 57 protein - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS E27215 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession E27215 !'##molecule_type DNA !'##residues 1-71 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27940.1; !1PID:g60046 GENETICS !$#gene 57 CLASSIFICATION #superfamily varicella-zoster virus gene 57 protein SUMMARY #length 71 #molecular-weight 8080 #checksum 6892 SEQUENCE /// ENTRY WZBE58 #type complete TITLE gene 58 protein - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS F27215 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession F27215 !'##molecule_type DNA !'##residues 1-221 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27941.1; !1PID:g60047 GENETICS !$#gene 58 CLASSIFICATION #superfamily varicella-zoster virus gene 58 protein SUMMARY #length 221 #molecular-weight 25094 #checksum 439 SEQUENCE /// ENTRY WMBEX3 #type complete TITLE UL3 protein - human herpesvirus 1 (strain 17) ORGANISM #formal_name human herpesvirus 1 DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jun-2000 ACCESSIONS C28133 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession C28133 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-235 ##label MCG !'##cross-references GB:X14112; NID:g1944536; PIDN:CAA32339.1; !1PID:g59504; GB:D00317 GENETICS !$#gene UL3 CLASSIFICATION #superfamily varicella-zoster virus gene 58 protein SUMMARY #length 235 #molecular-weight 25609 #checksum 9298 SEQUENCE /// ENTRY WMBEHK #type complete TITLE UL3 protein - human herpesvirus 2 (strain HG52) ORGANISM #formal_name human herpesvirus 2 #note host Homo sapiens (man) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jun-2000 ACCESSIONS JQ1496 REFERENCE JQ1494 !$#authors McGeoch, D.J.; Cunningham, C.; McIntyre, G.; Dolan, A. !$#journal J. Gen. Virol. (1991) 72:3057-3075 !$#title Comparative sequence analysis of the long repeat regions and !1adjoining parts of the long unique regions in the genomes of !1herpes simplex viruses types 1 and 2. !$#cross-references MUID:92113549; PMID:1662697 !$#accession JQ1496 !'##molecule_type DNA !'##residues 1-233 ##label MCG !'##cross-references GB:D10470; DDBJ:D01127; NID:g221791; !1PIDN:BAA01266.1; PID:g221794 GENETICS !$#gene UL3 CLASSIFICATION #superfamily varicella-zoster virus gene 58 protein SUMMARY #length 233 #molecular-weight 25649 #checksum 467 SEQUENCE /// ENTRY WZBEF2 #type complete TITLE gene 60 protein - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS F36801 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession F36801 !'##molecule_type DNA !'##residues 1-212 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02495.1; !1PID:g330851 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 60 CLASSIFICATION #superfamily varicella-zoster virus gene 58 protein SUMMARY #length 212 #molecular-weight 23682 #checksum 507 SEQUENCE /// ENTRY WZBE60 #type complete TITLE gene 60 protein - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS H27215 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession H27215 !'##molecule_type DNA !'##residues 1-159 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27943.1; !1PID:g60049 GENETICS !$#gene 60 CLASSIFICATION #superfamily varicella-zoster virus gene 60 protein SUMMARY #length 159 #molecular-weight 17617 #checksum 4068 SEQUENCE /// ENTRY WMBEX1 #type complete TITLE UL1 protein - human herpesvirus 1 (strain 17) ORGANISM #formal_name human herpesvirus 1 DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jun-2000 ACCESSIONS A28133 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession A28133 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-224 ##label MCG !'##cross-references GB:X14112; NID:g1944536; PIDN:CAA32337.1; !1PID:g59502; GB:D00317 GENETICS !$#gene UL1 CLASSIFICATION #superfamily varicella-zoster virus gene 60 protein SUMMARY #length 224 #molecular-weight 24933 #checksum 1464 SEQUENCE /// ENTRY WMBEHG #type complete TITLE UL1 protein - human herpesvirus 2 (strain HG52) ORGANISM #formal_name human herpesvirus 2 #note host Homo sapiens (man) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jun-2000 ACCESSIONS JQ1494 REFERENCE JQ1494 !$#authors McGeoch, D.J.; Cunningham, C.; McIntyre, G.; Dolan, A. !$#journal J. Gen. Virol. (1991) 72:3057-3075 !$#title Comparative sequence analysis of the long repeat regions and !1adjoining parts of the long unique regions in the genomes of !1herpes simplex viruses types 1 and 2. !$#cross-references MUID:92113549; PMID:1662697 !$#accession JQ1494 !'##molecule_type DNA !'##residues 1-224 ##label MCG !'##cross-references GB:D10470; DDBJ:D01127; NID:g221791; !1PIDN:BAA01264.1; PID:g221792 GENETICS !$#gene UL1 CLASSIFICATION #superfamily varicella-zoster virus gene 60 protein SUMMARY #length 224 #molecular-weight 25192 #checksum 2478 SEQUENCE /// ENTRY WZBEF4 #type complete TITLE gene 62 protein - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS H36801 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession H36801 !'##molecule_type DNA !'##residues 1-218 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02497.1; !1PID:g330853 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 62 CLASSIFICATION #superfamily varicella-zoster virus gene 60 protein SUMMARY #length 218 #molecular-weight 24425 #checksum 7344 SEQUENCE /// ENTRY WZBE61 #type complete TITLE gene 61 protein - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 17-Mar-2000 ACCESSIONS I27215 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession I27215 !'##molecule_type DNA !'##residues 1-467 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27944.1; !1PID:g60050 GENETICS !$#gene 61 CLASSIFICATION #superfamily varicella-zoster virus gene 61 protein; RING !1finger homology KEYWORDS DNA binding; transcription regulation; zinc finger FEATURE !$15-63 #domain RING finger homology #label RNG\ !$19-57 #region zinc finger C3HC4 motif SUMMARY #length 467 #molecular-weight 50916 #checksum 4143 SEQUENCE /// ENTRY WZBEF5 #type complete TITLE 59K transcription activator - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 17-Mar-2000 ACCESSIONS I36801 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession I36801 !'##molecule_type DNA !'##residues 1-532 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02498.1; !1PID:g330854 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 63 CLASSIFICATION #superfamily varicella-zoster virus gene 63 protein; RING !1finger homology KEYWORDS DNA binding; transcription regulation; zinc finger FEATURE !$4-52 #domain RING finger homology #label RNG\ !$8-46 #region zinc finger C3HC4 motif SUMMARY #length 532 #molecular-weight 58629 #checksum 1389 SEQUENCE /// ENTRY WZBE62 #type complete TITLE gene 62 protein - human herpesvirus 3 ALTERNATE_NAMES gene 71 protein ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS A27345 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession A27345 !'##molecule_type DNA !'##residues 1-1310 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27945.1; !1PID:g60051 GENETICS !$#gene 62; 71 CLASSIFICATION #superfamily varicella-zoster virus gene 62 protein KEYWORDS DNA binding; transcription regulation SUMMARY #length 1310 #molecular-weight 139996 #checksum 6298 SEQUENCE /// ENTRY WZBE64 #type complete TITLE gene 64 protein - human herpesvirus 3 ALTERNATE_NAMES gene 69 protein ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS C27345; H27345 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession C27345 !'##molecule_type DNA !'##residues 1-180 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27947.1; !1PID:g60053 COMMENT Gene 64 protein and gene 69 protein are identical. GENETICS !$#gene 64; 69 CLASSIFICATION #superfamily herpesvirus 28K protein SUMMARY #length 180 #molecular-weight 19868 #checksum 4653 SEQUENCE /// ENTRY WMBES2 #type complete TITLE 28K protein - equine herpesvirus 1 (subtype 2) ORGANISM #formal_name equine herpesvirus 1 DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jun-2000 ACCESSIONS C28134 REFERENCE A28134 !$#authors Cullinane, A.A.; Rixon, F.J.; Davison, A.J. !$#journal J. Gen. Virol. (1988) 69:1575-1590 !$#title Characterization of the genome of equine herpesvirus 1 !1subtype 2. !$#cross-references MUID:88274328; PMID:2839595 !$#accession C28134 !'##molecule_type DNA !'##residues 1-259 ##label CUL !'##cross-references GB:D00318; NID:g221815; PIDN:BAA00220.1; !1PID:g221818 CLASSIFICATION #superfamily herpesvirus 28K protein SUMMARY #length 259 #molecular-weight 27754 #checksum 9778 SEQUENCE /// ENTRY WZBEF8 #type complete TITLE gene 66 protein - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS C36802 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession C36802 !'##molecule_type DNA !'##residues 1-236 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02501.1; !1PID:g330857 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 66 CLASSIFICATION #superfamily herpesvirus 28K protein SUMMARY #length 236 #molecular-weight 25033 #checksum 8396 SEQUENCE /// ENTRY WZBEK1 #type complete TITLE IR5 protein - equine herpesvirus 1 (strain Kentucky A) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS A42541 REFERENCE A42541 !$#authors Holden, V.R.; Yalamanchili, R.R.; Harty, R.N.; O'Callaghan, !1D.J. !$#journal Virology (1992) 188:704-713 !$#title Identification and characterization of an equine herpesvirus !11 late gene encoding a potential zinc finger. !$#cross-references MUID:92263774; PMID:1316680 !$#accession A42541 !'##molecule_type DNA !'##residues 1-236 ##label HOL !'##cross-references GB:M84521; NID:g330917; PIDN:AAA46093.1; !1PID:g330918 GENETICS !$#gene IR5 CLASSIFICATION #superfamily herpesvirus 28K protein KEYWORDS zinc finger FEATURE !$138-150 #region zinc finger SUMMARY #length 236 #molecular-weight 24990 #checksum 8390 SEQUENCE /// ENTRY QQBE07 #type complete TITLE US10 protein - human herpesvirus 1 ORGANISM #formal_name human herpesvirus 1 #note host Homo sapiens (man) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 31-Oct-1997 ACCESSIONS A05242 REFERENCE A00656 !$#authors McGeoch, D.J.; Dolan, A.; Donald, S.; Rixon, F.J. !$#journal J. Mol. Biol. (1985) 181:1-13 !$#title Sequence determination and genetic content of the short !1unique region in the genome of herpes simplex virus type 1. !$#cross-references MUID:85160822; PMID:2984429 !$#accession A05242 !'##molecule_type DNA !'##residues 1-312 ##label MCG !'##cross-references GB:X02138 !'##experimental_source strain 17 GENETICS !$#gene US10 CLASSIFICATION #superfamily herpesvirus 28K protein SUMMARY #length 312 #molecular-weight 34055 #checksum 9678 SEQUENCE /// ENTRY WMBEHA #type complete TITLE 52K immediate-early protein - saimiriine herpesvirus 1 (strain 11) ORGANISM #formal_name saimiriine herpesvirus 1 #note host Saimiri sciureus (common squirrel monkey) DATE 30-Sep-1989 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS A36812 REFERENCE A36806 !$#authors Albrecht, J. !$#submission submitted to the EMBL Data Library, January 1992 !$#description Primary structure of the herpesvirus saimiri genome. !$#accession A36812 !'##molecule_type DNA !'##residues 1-417 ##label ALB !'##cross-references GB:X64346; NID:g60320; PIDN:CAA45680.1; PID:g60378 REFERENCE A37309 !$#authors Albrecht, J.C.; Nicholas, J.; Biller, D.; Cameron, K.R.; !1Biesinger, B.; Newman, C.; Wittmann, S.; Craxton, M.A.; !1Coleman, H.; Fleckenstein, B.; Honess, R.W. !$#journal J. Virol. (1992) 66:5047-5058 !$#title Primary structure of the herpesvirus saimiri genome. !$#cross-references MUID:92333688; PMID:1321287 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 57 !$#introns 7/3 CLASSIFICATION #superfamily saimiri herpesvirus 52K immediate-early protein KEYWORDS early protein; transcription regulation SUMMARY #length 417 #molecular-weight 46815 #checksum 3108 SEQUENCE /// ENTRY WMBEHS #type complete TITLE membrane antigen p140 - saimiriine herpesvirus 1 (strain 11) ORGANISM #formal_name saimiriine herpesvirus 1 DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 16-Jul-1999 ACCESSIONS A27837 REFERENCE A27837 !$#authors Cameron, K.R.; Stamminger, T.; Craxton, M.; Bodemer, W.; !1Honess, R.W.; Fleckenstein, B. !$#journal J. Virol. (1987) 61:2063-2070 !$#title The 160,000-Mr virion protein encoded at the right end of !1the herpesvirus saimiri genome is homologous to the 140, !1000-Mr membrane antigen encoded at the left end of the !1Epstein-Barr virus genome. !$#cross-references MUID:87226386; PMID:3035208 !$#accession A27837 !'##molecule_type DNA !'##residues 1-1299 ##label CAM !'##cross-references GB:M16755; NID:g331049; PIDN:AAA66573.1; !1PID:g808693 CLASSIFICATION #superfamily Herpesvirus saimiri membrane antigen p140 KEYWORDS membrane protein SUMMARY #length 1299 #molecular-weight 143229 #checksum 4229 SEQUENCE /// ENTRY QQBE1 #type complete TITLE membrane antigen p140 - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS A03740; S04560; S32973 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession A03740 !'##molecule_type DNA !'##residues 1-1318 ##label BAN !'##cross-references EMBL:V01555; NID:g59074; PIDN:CAA24862.1; !1PID:g59075 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region REFERENCE S00735 !$#authors Walls, D.; Perricaudet, M.; Gannon, F. !$#journal Nucleic Acids Res. (1988) 16:2859-2872 !$#title The analysis of EBV proteins which are antigenic in vivo. !$#cross-references MUID:88217505; PMID:2835748 !$#accession S04560 !'##molecule_type DNA !'##residues 327-365 ##label WAL !'##cross-references EMBL:X07530 CLASSIFICATION #superfamily Herpesvirus saimiri membrane antigen p140 KEYWORDS membrane protein; surface antigen SUMMARY #length 1318 #molecular-weight 142843 #checksum 6424 SEQUENCE /// ENTRY QQBE2 #type complete TITLE BCRF1 protein - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS A03741; S32974 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession A03741 !'##molecule_type DNA !'##residues 1-170 ##label BAN !'##cross-references EMBL:V01555; NID:g59074; PIDN:CAA24863.1; !1PID:g59076 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region CLASSIFICATION #superfamily interleukin-10 SUMMARY #length 170 #molecular-weight 19914 #checksum 9877 SEQUENCE /// ENTRY QQBE3 #type complete TITLE BHLF1 protein - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 23-Aug-1997 ACCESSIONS A03742 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession A03742 !'##molecule_type DNA !'##residues 1-660 ##label BAN REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region COMMENT The sequence contains four perfect repeats (residues !1149-273, 274-398, 399-523, and 524-648). CLASSIFICATION #superfamily human herpesvirus 4 BHLF1 protein SUMMARY #length 660 #molecular-weight 66244 #checksum 8900 SEQUENCE /// ENTRY QQBE4 #type complete TITLE BHRF1 protein - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 23-Aug-1997 ACCESSIONS C93065; A03743 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession C93065 !'##molecule_type DNA !'##residues 1-191 ##label BAN REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region CLASSIFICATION #superfamily human herpesvirus 4 BHRF1 protein KEYWORDS transmembrane protein SUMMARY #length 191 #molecular-weight 21893 #checksum 4171 SEQUENCE /// ENTRY QQBEW2 #type complete TITLE UL53 protein - human cytomegalovirus (strain AD169) ALTERNATE_NAMES HFRF2 protein ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 #note host Homo sapiens (man) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS S09816 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09816 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-376 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35412.1; !1PID:g1780831 !'##note possible protein-coding frames are given !'##note the DNA sequence was submitted to EMBL, December 1989, in !1computer-readable form CLASSIFICATION #superfamily varicella-zoster virus gene 27 protein SUMMARY #length 376 #molecular-weight 42312 #checksum 4952 SEQUENCE /// ENTRY QQBE6S #type fragment TITLE XIRF2 protein - human herpesvirus 6 (strain U1102) (fragment) ORGANISM #formal_name human herpesvirus 6 DATE 30-Sep-1992 #sequence_revision 29-Oct-1999 #text_change 21-Jul-2000 ACCESSIONS T09331; A40898 REFERENCE Z16644 !$#authors Nicholas, J.; Martin, M. !$#journal J. Virol. (1994) 68:597-610 !$#title Nucleotide sequence analysis of a 38.5-kilobase-pair region !1of the genome of human herpesvirus 6 encoding human !1cytomegalovirus immediate-early gene homologs and !1transactivating functions. !$#cross-references MUID:94118404; PMID:8289364 !$#accession T09331 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-265 ##label NIC !'##cross-references EMBL:L25528; NID:g451932; PIDN:AAA16744.1; !1PID:g451962 REFERENCE A40898 !$#authors Teo, I.A.; Griffin, B.E.; Jones, M.D. !$#journal J. Virol. (1991) 65:4670-4680 !$#title Characterization of the DNA polymerase gene of human !1herpesvirus 6. !$#cross-references MUID:91333007; PMID:1651403 !$#accession A40898 !'##molecule_type DNA !'##residues 86-265 ##label TEO !'##cross-references GB:M63804; NID:g325467; PIDN:AAA74630.1; !1PID:g325468 GENETICS !$#gene XIRF2 CLASSIFICATION #superfamily varicella-zoster virus gene 27 protein SUMMARY #length 265 #checksum 9900 SEQUENCE /// ENTRY QQBE5 #type complete TITLE BFLF2 protein - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 31-Dec-1993 ACCESSIONS D93065; A03744 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession D93065 !'##molecule_type DNA !'##residues 1-318 ##label BAN REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region CLASSIFICATION #superfamily varicella-zoster virus gene 27 protein SUMMARY #length 318 #molecular-weight 35360 #checksum 5326 SEQUENCE /// ENTRY WZBE27 #type complete TITLE gene 27 protein - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS A27214 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession A27214 !'##molecule_type DNA !'##residues 1-333 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27910.1; !1PID:g60016 GENETICS !$#gene 27 CLASSIFICATION #superfamily varicella-zoster virus gene 27 protein SUMMARY #length 333 #molecular-weight 38236 #checksum 9250 SEQUENCE /// ENTRY WMBEH1 #type complete TITLE UL31 protein - human herpesvirus 1 (strain 17) ORGANISM #formal_name human herpesvirus 1 DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jun-2000 ACCESSIONS D30085 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession D30085 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-306 ##label MCG !'##cross-references GB:X14112; NID:g1944536; PIDN:CAA32324.1; !1PID:g59531; GB:D00317 GENETICS !$#gene UL31 CLASSIFICATION #superfamily varicella-zoster virus gene 27 protein SUMMARY #length 306 #molecular-weight 33953 #checksum 6890 SEQUENCE /// ENTRY WZBEC2 #type complete TITLE gene 29 protein - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS C36798 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession C36798 !'##molecule_type DNA !'##residues 1-326 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02464.1; !1PID:g330821 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 29 CLASSIFICATION #superfamily varicella-zoster virus gene 27 protein SUMMARY #length 326 #molecular-weight 36525 #checksum 610 SEQUENCE /// ENTRY WZBEQ1 #type complete TITLE gene 69 protein - saimiriine herpesvirus 1 (strain 11) ORGANISM #formal_name saimiriine herpesvirus 1 #note host Saimiri sciureus (common squirrel monkey) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS D36813 REFERENCE A36806 !$#authors Albrecht, J. !$#submission submitted to the EMBL Data Library, January 1992 !$#description Primary structure of the herpesvirus saimiri genome. !$#accession D36813 !'##molecule_type DNA !'##residues 1-261 ##label ALB !'##cross-references GB:X64346; NID:g60320; PIDN:CAA45692.1; PID:g60390 REFERENCE A37309 !$#authors Albrecht, J.C.; Nicholas, J.; Biller, D.; Cameron, K.R.; !1Biesinger, B.; Newman, C.; Wittmann, S.; Craxton, M.A.; !1Coleman, H.; Fleckenstein, B.; Honess, R.W. !$#journal J. Virol. (1992) 66:5047-5058 !$#title Primary structure of the herpesvirus saimiri genome. !$#cross-references MUID:92333688; PMID:1321287 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 69 CLASSIFICATION #superfamily varicella-zoster virus gene 27 protein SUMMARY #length 261 #molecular-weight 29784 #checksum 5471 SEQUENCE /// ENTRY QQBE6 #type complete TITLE BFLF1 protein - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS E93065; A03745; S32989 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession E93065 !'##molecule_type DNA !'##residues 1-525 ##label BAN !'##cross-references EMBL:V01555; NID:g59074; PIDN:CAA24878.1; !1PID:g1334849 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region CLASSIFICATION #superfamily varicella-zoster virus gene 26 protein SUMMARY #length 525 #molecular-weight 57911 #checksum 6255 SEQUENCE /// ENTRY WZBE26 #type complete TITLE gene 26 protein - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS H27343 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession H27343 !'##molecule_type DNA !'##residues 1-585 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27908.1; !1PID:g60014 GENETICS !$#gene 26 CLASSIFICATION #superfamily varicella-zoster virus gene 26 protein SUMMARY #length 585 #molecular-weight 65694 #checksum 3475 SEQUENCE /// ENTRY WMBEH2 #type complete TITLE UL32 protein - human herpesvirus 1 (strain 17) ORGANISM #formal_name human herpesvirus 1 DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jun-2000 ACCESSIONS E30085 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession E30085 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-596 ##label MCG !'##cross-references GB:X14112; NID:g1944536; PIDN:CAA32307.1; !1PID:g59533; GB:D00317 GENETICS !$#gene UL32 CLASSIFICATION #superfamily varicella-zoster virus gene 26 protein KEYWORDS glycoprotein FEATURE !$245,451,452 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 596 #molecular-weight 63949 #checksum 607 SEQUENCE /// ENTRY WZBEC1 #type complete TITLE gene 28 protein - equine herpesvirus 1 (strain Ab4p) ALTERNATE_NAMES glycoprotein 300 ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS B36798; JQ1897 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession B36798 !'##molecule_type DNA !'##residues 1-620 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02463.1; !1PID:g330820 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given REFERENCE JQ1897 !$#authors Whittaker, G.R.; Bonass, W.A.; Elton, D.M.; Halliburton, !1I.W.; Killington, R.A.; Meredith, D.M. !$#journal J. Gen. Virol. (1992) 73:2933-2940 !$#title Glycoprotein 300 is encoded by gene 28 of equine herpesvirus !1type 1: a new family of herpesvirus membrane proteins? !$#cross-references MUID:93057365; PMID:1331295 !$#accession JQ1897 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-620 ##label WHI !'##experimental_source strain Ab-1 GENETICS !$#gene 28 CLASSIFICATION #superfamily varicella-zoster virus gene 26 protein KEYWORDS glycoprotein; transmembrane protein FEATURE !$42,221,340 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 620 #molecular-weight 67300 #checksum 6200 SEQUENCE /// ENTRY WZBEP9 #type complete TITLE gene 68 protein - saimiriine herpesvirus 1 (strain 11) ORGANISM #formal_name saimiriine herpesvirus 1 #note host Saimiri sciureus (common squirrel monkey) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS C36813 REFERENCE A36806 !$#authors Albrecht, J. !$#submission submitted to the EMBL Data Library, January 1992 !$#description Primary structure of the herpesvirus saimiri genome. !$#accession C36813 !'##molecule_type DNA !'##residues 1-436 ##label ALB !'##cross-references GB:X64346; NID:g60320; PIDN:CAA45691.1; PID:g60389 REFERENCE A37309 !$#authors Albrecht, J.C.; Nicholas, J.; Biller, D.; Cameron, K.R.; !1Biesinger, B.; Newman, C.; Wittmann, S.; Craxton, M.A.; !1Coleman, H.; Fleckenstein, B.; Honess, R.W. !$#journal J. Virol. (1992) 66:5047-5058 !$#title Primary structure of the herpesvirus saimiri genome. !$#cross-references MUID:92333688; PMID:1321287 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 68 CLASSIFICATION #superfamily varicella-zoster virus gene 26 protein SUMMARY #length 436 #molecular-weight 49131 #checksum 4562 SEQUENCE /// ENTRY QQBEW1 #type complete TITLE UL52 protein - human cytomegalovirus (strain AD169) ALTERNATE_NAMES HFRF1 protein ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 #note host Homo sapiens (man) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS S09815 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09815 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-668 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35411.1; !1PID:g1780830 !'##note possible protein-coding frames are given !'##note the DNA sequence was submitted to EMBL, December 1989, in !1computer-readable form CLASSIFICATION #superfamily varicella-zoster virus gene 26 protein SUMMARY #length 668 #molecular-weight 74120 #checksum 3376 SEQUENCE /// ENTRY QQBE7 #type complete TITLE BFRF1 protein - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus #note host Homo sapiens (man) DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS F93065; A03746; S32990 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession F93065 !'##molecule_type DNA !'##residues 1-336 ##label BAN !'##cross-references EMBL:V01555; NID:g59074; PIDN:CAA24879.1; !1PID:g1334850 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region CLASSIFICATION #superfamily human herpesvirus 4 BFRF1 protein SUMMARY #length 336 #molecular-weight 37632 #checksum 9598 SEQUENCE /// ENTRY QQBEP8 #type complete TITLE gene 67 protein - saimiriine herpesvirus 1 (strain 11) ORGANISM #formal_name saimiriine herpesvirus 1 #note host Saimiri sciureus (common squirrel monkey) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS B36813 REFERENCE A36806 !$#authors Albrecht, J. !$#submission submitted to the EMBL Data Library, January 1992 !$#description Primary structure of the herpesvirus saimiri genome. !$#accession B36813 !'##molecule_type DNA !'##residues 1-235 ##label ALB !'##cross-references GB:X64346; NID:g60320; PIDN:CAA45690.1; PID:g60388 REFERENCE A37309 !$#authors Albrecht, J.C.; Nicholas, J.; Biller, D.; Cameron, K.R.; !1Biesinger, B.; Newman, C.; Wittmann, S.; Craxton, M.A.; !1Coleman, H.; Fleckenstein, B.; Honess, R.W. !$#journal J. Virol. (1992) 66:5047-5058 !$#title Primary structure of the herpesvirus saimiri genome. !$#cross-references MUID:92333688; PMID:1321287 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 67 CLASSIFICATION #superfamily human herpesvirus 4 BFRF1 protein SUMMARY #length 235 #molecular-weight 26886 #checksum 2564 SEQUENCE /// ENTRY QQBE8 #type complete TITLE BPLF1 protein - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS G93065; A03747; S32993 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession G93065 !'##molecule_type DNA !'##residues 1-3149 ##label BAN !'##cross-references EMBL:V01555; NID:g59074; PIDN:CAA24839.1; !1PID:g1334853 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region CLASSIFICATION #superfamily human herpesvirus 4 BPLF1 protein SUMMARY #length 3149 #molecular-weight 337955 #checksum 7480 SEQUENCE /// ENTRY QQBE9 #type complete TITLE BORF1 protein - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus #note host Homo sapiens (man) DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS H93065; A03748; S32994 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession H93065 !'##molecule_type DNA !'##residues 1-364 ##label BAN !'##cross-references EMBL:V01555; NID:g59074; PIDN:CAA24840.1; !1PID:g1334854 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region CLASSIFICATION #superfamily human herpesvirus 4 BORF1 protein KEYWORDS capsid assembly; DNA binding SUMMARY #length 364 #molecular-weight 39190 #checksum 6899 SEQUENCE /// ENTRY QQBEP7 #type complete TITLE gene 62 protein - saimiriine herpesvirus 1 (strain 11) ORGANISM #formal_name saimiriine herpesvirus 1 #note host Saimiri sciureus (common squirrel monkey) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS F36812 REFERENCE A36806 !$#authors Albrecht, J. !$#submission submitted to the EMBL Data Library, January 1992 !$#description Primary structure of the herpesvirus saimiri genome. !$#accession F36812 !'##molecule_type DNA !'##residues 1-330 ##label ALB !'##cross-references GB:X64346; NID:g60320; PIDN:CAA45685.1; PID:g60383 REFERENCE A37309 !$#authors Albrecht, J.C.; Nicholas, J.; Biller, D.; Cameron, K.R.; !1Biesinger, B.; Newman, C.; Wittmann, S.; Craxton, M.A.; !1Coleman, H.; Fleckenstein, B.; Honess, R.W. !$#journal J. Virol. (1992) 66:5047-5058 !$#title Primary structure of the herpesvirus saimiri genome. !$#cross-references MUID:92333688; PMID:1321287 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 62 CLASSIFICATION #superfamily human herpesvirus 4 BORF1 protein KEYWORDS capsid assembly; DNA binding SUMMARY #length 330 #molecular-weight 37385 #checksum 9610 SEQUENCE /// ENTRY QQBE1L #type complete TITLE glycoprotein B - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 16-Jul-1999 ACCESSIONS A03749; S33055 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession A03749 !'##molecule_type DNA !'##residues 1-857 ##label BAN !'##cross-references EMBL:V01555; NID:g59074; PIDN:CAA24806.1; !1PID:g1334914 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region CLASSIFICATION #superfamily herpesvirus glycoprotein B KEYWORDS glycoprotein; transmembrane protein FEATURE !$76,163,290,329,348, !$395,436,563,629 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 857 #molecular-weight 95638 #checksum 8779 SEQUENCE /// ENTRY VGBEB1 #type complete TITLE glycoprotein B precursor - human herpesvirus 1 (strain F) ORGANISM #formal_name human herpesvirus 1 DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 16-Jul-1999 ACCESSIONS A03750 REFERENCE A03750 !$#authors Pellett, P.E.; Kousoulas, K.G.; Pereira, L.; Roizman, B. !$#journal J. Virol. (1985) 53:243-253 !$#title Anatomy of the herpes simplex virus 1 strain F glycoprotein !1B gene: primary sequence and predicted protein structure of !1the wild type and of monoclonal antibody-resistant mutants. !$#cross-references MUID:85083254; PMID:2981343 !$#accession A03750 !'##molecule_type DNA !'##residues 1-903 ##label PEL !'##cross-references GB:M14164; GB:M12398; NID:g330084; PIDN:AAA45776.1; !1PID:g330086 CLASSIFICATION #superfamily herpesvirus glycoprotein B KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-29 #domain signal sequence #status predicted #label SIG\ !$30-903 #product glycoprotein B #status predicted #label MAT\ !$726-746 #domain transmembrane #status predicted #label TM1\ !$751-771 #domain transmembrane #status predicted #label TM2\ !$774-794 #domain transmembrane #status predicted #label TM3\ !$86,140,254,397,429, !$477,488,673,818,887 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$115-572,132-528, !$206-270,363-411, !$595-632 #disulfide_bonds #status predicted SUMMARY #length 903 #molecular-weight 100103 #checksum 6478 SEQUENCE /// ENTRY VGBEK1 #type complete TITLE glycoprotein B precursor - human herpesvirus 1 (strain KOS) ORGANISM #formal_name human herpesvirus 1 DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 16-Jul-1999 ACCESSIONS A03751 REFERENCE A03751 !$#authors Bzik, D.J.; Fox, B.A.; DeLuca, N.A.; Person, S. !$#journal Virology (1984) 133:301-314 !$#title Nucleotide sequence specifying the glycoprotein gene, gB, of !1herpes simplex virus type 1. !$#cross-references MUID:84174058; PMID:6324454 !$#accession A03751 !'##molecule_type DNA !'##residues 1-903 ##label BZI !'##cross-references GB:K01760; NID:g330082; PIDN:AAA45774.1; !1PID:g330083 CLASSIFICATION #superfamily herpesvirus glycoprotein B KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-30 #domain signal sequence #status predicted #label SIG\ !$31-903 #product glycoprotein B #status predicted #label MAT\ !$726-746 #domain transmembrane #status predicted #label TM1\ !$751-771 #domain transmembrane #status predicted #label TM2\ !$774-794 #domain transmembrane #status predicted #label TM3\ !$76,86,140,254,397, !$429,477,488,673, !$818,887 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$115-572,132-528, !$206-270,363-411, !$595-632 #disulfide_bonds #status predicted SUMMARY #length 903 #molecular-weight 100473 #checksum 7330 SEQUENCE /// ENTRY VGBEW7 #type complete TITLE glycoprotein B precursor - human herpesvirus 1 (strain 17) ORGANISM #formal_name human herpesvirus 1 DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jun-2000 ACCESSIONS I30084 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession I30084 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-904 ##label MCG !'##cross-references GB:X14112; GB:D00317; GB:D00374; GB:S40593; !1NID:g1944536; PIDN:CAA32320.1; PID:g59527; GB:D10879; !1NID:g221721; PID:g221748 GENETICS !$#gene UL27 CLASSIFICATION #superfamily herpesvirus glycoprotein B KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-30 #domain signal sequence #status predicted #label SIG\ !$31-904 #product glycoprotein B #status predicted #label MAT\ !$727-746 #domain transmembrane #status predicted #label TM1\ !$752-771 #domain transmembrane #status predicted #label TM2\ !$774-795 #domain transmembrane #status predicted #label TM3\ !$87,141,255,398,430, !$478,489,674,819,888 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$116-573,133-529, !$207-271,364-412, !$596-633 #disulfide_bonds #status predicted SUMMARY #length 904 #molecular-weight 100292 #checksum 9684 SEQUENCE /// ENTRY VGBEK2 #type complete TITLE glycoprotein B precursor - human herpesvirus 2 (strain HG52) ORGANISM #formal_name human herpesvirus 2 DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jul-1999 ACCESSIONS A25611 REFERENCE A25611 !$#authors Bzik, D.J.; Debroy, C.; Fox, B.A.; Pederson, N.E.; Person, !1S. !$#journal Virology (1986) 155:322-333 !$#title The nucleotide sequence of the gB glycoprotein gene of HSV-2 !1and comparison with the corresponding gene of HSV-1. !$#cross-references MUID:87071654; PMID:3024391 !$#accession A25611 !'##molecule_type DNA !'##residues 1-904 ##label BZI !'##cross-references GB:M14923; NID:g330254; PIDN:AAA66440.1; !1PID:g330255 REFERENCE A58366 !$#authors Norais, N.; Tang, D.; Kaur, S.; Chamberlain, S.H.; Masiarz, !1F.R.; Burke, R.L.; Marcus, F. !$#journal J. Virol. (1996) 70:7379-7387 !$#title Disulfide bonds of herpes simplex virus type 2 glycoprotein !1gB. !$#cross-references MUID:97048015; PMID:8892856 !$#contents annotation; tryptic peptide disulfide bond assignments CLASSIFICATION #superfamily herpesvirus glycoprotein B KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-904 #product glycoprotein B #status predicted #label MAT\ !$724-744 #domain transmembrane #status predicted #label TM1\ !$749-769 #domain transmembrane #status predicted #label TM2\ !$772-792 #domain transmembrane #status predicted #label TM3\ !$82,136,250,393,425, !$473,486,671 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$111-570,128-526, !$202-266,359-407, !$593-630 #disulfide_bonds #status experimental SUMMARY #length 904 #molecular-weight 100059 #checksum 8956 SEQUENCE /// ENTRY VGBEB2 #type complete TITLE glycoprotein B precursor - human herpesvirus 2 (strain 333) ORGANISM #formal_name human herpesvirus 2 DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 16-Jul-1999 ACCESSIONS A26790; A45928 REFERENCE A26790 !$#authors Stuve, L.L.; Brown-Shimer, S.; Pachl, C.; Najarian, R.; !1Dina, D.; Burke, R.L. !$#journal J. Virol. (1987) 61:326-335 !$#title Structure and expression of the herpes simplex virus type 2 !1glycoprotein gB gene. !$#cross-references MUID:87112925; PMID:3027364 !$#accession A26790 !'##molecule_type DNA !'##residues 1-904 ##label STU !'##cross-references GB:M15118; NID:g330256; PIDN:AAA45837.1; !1PID:g330257 REFERENCE A45928 !$#authors Zwaagstra, J.C.; Leung, W.C. !$#journal Can. J. Microbiol. (1987) 33:879-887 !$#title The nucleotide sequence of herpes simplex virus type 2 (333) !1glycoprotein gB2 and analysis of predicted antigenic sites. !$#cross-references MUID:88079667; PMID:2446730 !$#accession A45928 !'##molecule_type DNA !'##residues 1-34,'AWPTV',42-307,'T',309-481,'R',483-609,'M',611-664, !1'R',666-904 ##label ZWA !'##cross-references GB:M24771; NID:g341245; PIDN:AAA60540.1; !1PID:g623400 !'##note the authors translated the codon ATG for residue 610 as Ile CLASSIFICATION #superfamily herpesvirus glycoprotein B KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-904 #product glycoprotein B #status predicted #label MAT\ !$724-744 #domain transmembrane #status predicted #label TM1\ !$749-769 #domain transmembrane #status predicted #label TM2\ !$772-792 #domain transmembrane #status predicted #label TM3\ !$82,136,250,393,425, !$473,486,671 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$111-570,128-526, !$202-266,359-407, !$593-630 #disulfide_bonds #status predicted SUMMARY #length 904 #molecular-weight 100186 #checksum 9674 SEQUENCE /// ENTRY VGBESA #type complete TITLE glycoprotein B precursor - simian herpesvirus SA8 (strain B264) ORGANISM #formal_name simian herpesvirus SA8 DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS JQ1332 REFERENCE JQ1332 !$#authors Borchers, K.; Weigelt, W.; Buhk, H.J.; Ludwig, H.; Mankertz, !1J. !$#journal J. Gen. Virol. (1991) 72:2299-2304 !$#title Conserved domains of glycoprotein B (gB) of the monkey !1virus, simian agent 8, identified by comparison with !1herpesvirus gBs. !$#cross-references MUID:91374035; PMID:1895066 !$#accession JQ1332 !'##molecule_type DNA !'##residues 1-885 ##label BOR !'##cross-references EMBL:X56935; NID:g60438; PIDN:CAA40256.1; !1PID:g60439 CLASSIFICATION #superfamily herpesvirus glycoprotein B KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-885 #product glycoprotein B #status predicted #label MAT\ !$712-732 #domain transmembrane #status predicted #label TM1\ !$737-752 #domain transmembrane #status predicted #label TM2\ !$760-780 #domain transmembrane #status predicted #label TM3\ !$68,122,379,411,659 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$97-558,114-514, !$188-252,345-393, !$581-618 #disulfide_bonds #status predicted SUMMARY #length 885 #molecular-weight 97811 #checksum 5195 SEQUENCE /// ENTRY VGBEBG #type complete TITLE glycoprotein gI precursor - bovine herpesvirus 1 ALTERNATE_NAMES glycoprotein 11a; glycoprotein 16; glycoprotein g130; glycoprotein GVP-6 ORGANISM #formal_name bovine herpesvirus 1 DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS A31166 REFERENCE A31166 !$#authors Misra, V.; Nelson, R.; Smith, M. !$#journal Virology (1988) 166:542-549 !$#title Sequence of a bovine herpesvirus type-1 glycoprotein gene !1that is homologous to the herpes simplex gene for the !1glycoprotein gB. !$#cross-references MUID:89020821; PMID:2845660 !$#accession A31166 !'##molecule_type DNA !'##residues 1-928 ##label MIS !'##cross-references GB:M23257; NID:g340858; PIDN:AAA46013.1; !1PID:g511852 !'##note the authors translated the codon CTG for residue 534 as Ser CLASSIFICATION #superfamily herpesvirus glycoprotein B KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-67 #domain signal sequence #status predicted #label SIG\ !$68-928 #product glycoprotein gI #status predicted #label !8GGI\ !$756-824 #domain transmembrane #status predicted #label TMN\ !$105,153,442,484, !$579,637,703 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 928 #molecular-weight 102177 #checksum 7121 SEQUENCE /// ENTRY VGBEBC #type complete TITLE glycoprotein gI precursor - bovine herpesvirus 1 (strain Colorado-1[Cooper-1]) ALTERNATE_NAMES glycoprotein 11a; glycoprotein 16; glycoprotein g130; glycoprotein GVP-6 CONTAINS glycoprotein gIb; glycoprotein gIc ORGANISM #formal_name bovine herpesvirus 1 DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS A28877; A43380 REFERENCE A28877 !$#authors Whitbeck, J.C.; Bello, L.J.; Lawrence, W.C. !$#journal J. Virol. (1988) 62:3319-3327 !$#title Comparison of the bovine herpesvirus 1 gI gene and the !1herpes simplex virus type 1 gB gene. !$#cross-references MUID:88300884; PMID:2841484 !$#accession A28877 !'##molecule_type DNA !'##residues 1-932 ##label WHI !'##cross-references GB:M21474; NID:g330756; PIDN:AAA46055.1; !1PID:g330757 REFERENCE A43380 !$#authors van Drunen Littel-van den Hurk, S.; Parker, M.D.; !1Fitzpatrick, D.R.; van den Hurk, J.V.; Campos, M.; Babiuk, !1L.A.; Zamb, T. !$#journal Virology (1992) 190:378-392 !$#title Structural, functional, and immunological characterization !1of bovine herpesvirus-1 glycoprotein gl expressed by !1recombinant baculovirus. !$#cross-references MUID:92410615; PMID:1326809 !$#accession A43380 !'##molecule_type protein !'##residues 68-87;505-516 ##label VAN CLASSIFICATION #superfamily herpesvirus glycoprotein B KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-67 #domain signal sequence #status predicted #label SIG\ !$68-932 #product glycoprotein gI #status predicted #label !8GGI\ !$68-504 #product glycoprotein gIb #status predicted #label !8GIB\ !$505-932 #product glycoprotein gIc #status predicted #label !8GIC\ !$759-827 #domain transmembrane #status predicted #label TMN\ !$105,153,441,483, !$640,706 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 932 #molecular-weight 101194 #checksum 5344 SEQUENCE /// ENTRY VGBEBH #type complete TITLE glycoprotein B precursor - bovine herpesvirus 2 (strain BMV) ORGANISM #formal_name bovine herpesvirus 2 DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS C29242 REFERENCE A94381 !$#authors Hammerschmidt, W.; Conraths, F.; Mankertz, J.; Pauli, G.; !1Ludwig, H.; Buhk, H.J. !$#journal Virology (1988) 165:388-405 !$#title Conservation of a gene cluster including glycoprotein B in !1bovine herpesvirus type 2 (BHV-2) and herpes simplex virus !1type 1 (HSV-1). !$#cross-references MUID:88306231; PMID:2841793 !$#accession C29242 !'##status translation not shown !'##molecule_type DNA !'##residues 1-917 ##label HAM !'##cross-references GB:M21628; NID:g330752; PIDN:AAA46053.1; !1PID:g330753 CLASSIFICATION #superfamily herpesvirus glycoprotein B KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-917 #product glycoprotein B #status predicted #label GPB\ !$578-594 #domain transmembrane #status predicted #label TM1\ !$770-786 #domain transmembrane #status predicted #label TM2\ !$795-811 #domain transmembrane #status predicted #label TM3\ !$48,110,164,278,421, !$453,505,564,692 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 917 #molecular-weight 101882 #checksum 9379 SEQUENCE /// ENTRY VGBEPS #type complete TITLE glycoprotein gII precursor - suid herpesvirus 1 ORGANISM #formal_name suid herpesvirus 1 DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jul-1999 ACCESSIONS A29159 REFERENCE A29159 !$#authors Robbins, A.K.; Dorney, D.J.; Wathen, M.W.; Whealy, M.E.; !1Gold, C.; Watson, R.J.; Holland, L.E.; Weed, S.D.; Levine, !1M.; Glorioso, J.C.; Enquist, L.W. !$#journal J. Virol. (1987) 61:2691-2701 !$#title The pseudorabies virus gII gene is closely related to the gB !1glycoprotein gene of herpes simplex virus. !$#cross-references MUID:87284141; PMID:3039163 !$#accession A29159 !'##molecule_type DNA !'##residues 1-913 ##label ROB !'##cross-references GB:M17321; NID:g334053; PIDN:AAA47465.1; !1PID:g334054 !'##note the authors translated the codon GAC for residue 860 as Asn CLASSIFICATION #superfamily herpesvirus glycoprotein B KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-40 #domain signal sequence #status predicted #label SIG\ !$751-819 #domain transmembrane #status predicted #label TMM\ !$820-913 #domain intracellular #status predicted #label INT\ !$151,261,441,516, !$633,697 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 913 #molecular-weight 100233 #checksum 2800 SEQUENCE /// ENTRY VGBEQH #type complete TITLE glycoprotein B precursor - equine herpesvirus 4 (strain 1942) ORGANISM #formal_name equine herpesvirus 4 DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS A31880 REFERENCE A31880 !$#authors Riggio, M.P.; Cullinane, A.A.; Onions, D.E. !$#journal J. Virol. (1989) 63:1123-1133 !$#title Identification and nucleotide sequence of the glycoprotein !1gB gene of equine herpesvirus 4. !$#cross-references MUID:89125704; PMID:2915378 !$#accession A31880 !'##molecule_type DNA !'##residues 1-919 ##label RIG !'##cross-references GB:M26171; NID:g341446; PIDN:AAA46106.1; !1PID:g514920 CLASSIFICATION #superfamily herpesvirus glycoprotein B KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-919 #product glycoprotein B #status predicted #label GPB\ !$740-809 #domain transmembrane #status predicted #label TMN\ !$106,216,321,364, !$438,456,493,499, !$666,688 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 919 #molecular-weight 103710 #checksum 2141 SEQUENCE /// ENTRY VGBE2H #type complete TITLE glycoprotein B precursor - equine herpesvirus 1 (isolate HVS 25A) ORGANISM #formal_name equine herpesvirus 1 DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 05-Jan-1996 ACCESSIONS A31241; JQ0008 REFERENCE A31241 !$#authors Whalley, J.M.; Robertson, G.R.; Scott, N.A.; Hudson, G.C.; !1Bell, C.W.; Woodworth, L.M. !$#journal J. Gen. Virol. (1989) 70:383-394 !$#title Identification and nucleotide sequence of a gene in equine !1herpesvirus 1 analogous to the herpes simplex virus gene !1encoding the major envelope glycoprotein gB. !$#cross-references MUID:89279217; PMID:2543744 !$#accession A31241 !'##molecule_type DNA !'##residues 1-980 ##label WHA CLASSIFICATION #superfamily herpesvirus glycoprotein B KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-85 #domain signal sequence #status predicted #label SIG\ !$70-78 #domain transmembrane #status predicted #label TN1\ !$86-980 #product glycoprotein B #status predicted #label MAT\ !$853-868 #domain transmembrane #status predicted #label TN2\ !$165,275,380,423, !$497,514,515,560, !$727,749,952,971 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 980 #molecular-weight 109931 #checksum 6964 SEQUENCE /// ENTRY VGBEC6 #type complete TITLE glycoprotein B precursor - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS G36798 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession G36798 !'##molecule_type DNA !'##residues 1-980 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02468.1; !1PID:g330825 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 33 CLASSIFICATION #superfamily herpesvirus glycoprotein B KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-85 #domain signal sequence #status predicted #label SIG\ !$67-78 #domain transmembrane #status predicted #label TM1\ !$86-980 #product glycoprotein B #status predicted #label MAT\ !$850-868 #domain transmembrane #status predicted #label TM2\ !$165,275,380,423, !$497,514,515,560, !$727,749,952,971 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 980 #molecular-weight 109805 #checksum 6750 SEQUENCE /// ENTRY VGBERB #type complete TITLE glycoprotein B precursor - Marek's disease virus (strain RB1B) ORGANISM #formal_name Marek's disease virus DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jun-2000 ACCESSIONS A32402; B32402 REFERENCE A32402 !$#authors Ross, L.J.N.; Sanderson, M.; Scott, S.D.; Binns, M.M.; Doel, !1T.; Milne, B. !$#journal J. Gen. Virol. (1989) 70:1789-1804 !$#title Nucleotide sequence and characterization of the Marek's !1disease virus homologue of glycoprotein B of herpes simplex !1virus. !$#cross-references MUID:89293086; PMID:2544666 !$#accession A32402 !'##molecule_type DNA !'##residues 1-865 ##label ROS !'##cross-references GB:D13713; EMBL:D00506; NID:g221836; !1PIDN:BAA02866.1; PID:g221837 !$#accession B32402 !'##molecule_type protein !'##residues 250-271;304-330 ##label ROS2 CLASSIFICATION #superfamily herpesvirus glycoprotein B KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-865 #product glycoprotein B #status predicted #label GPB\ !$709-728 #domain transmembrane #status predicted #label TN1\ !$732-752 #domain transmembrane #status predicted #label TN2\ !$27,184,332,364,406, !$425,631 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 865 #molecular-weight 98091 #checksum 7888 SEQUENCE /// ENTRY B48349 #type complete TITLE glycoprotein B precursor - ateline herpesvirus 1 (strain Lennette) ORGANISM #formal_name ateline herpesvirus 1 DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 09-Sep-1994 ACCESSIONS B48349 REFERENCE A48349 !$#authors Eberle, R.; Black, D. !$#journal Arch. Virol. (1993) 129:167-182 !$#title Sequence analysis of herpes simplex virus gB gene homologs !1of two platyrrhine monkey alpha-herpesviruses. !$#cross-references MUID:93228440; PMID:8385913 !$#accession B48349 !'##molecule_type DNA !'##residues 1-933 ##label EBE !'##note sequence extracted from NCBI backbone (NCBIN:129063, !1NCBIP:129065) CLASSIFICATION #superfamily herpesvirus glycoprotein B KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-35 #domain signal sequence #status predicted #label SIG\ !$36-933 #product glycoprotein B #status predicted #label MAT\ !$775-794 #domain transmembrane #status predicted #label TM1\ !$801-818 #domain transmembrane #status predicted #label TM2\ !$107,161,418,450, !$697,747 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 933 #molecular-weight 101475 #checksum 4215 SEQUENCE /// ENTRY D48349 #type complete TITLE glycoprotein B precursor - saimiriine herpesvirus 1 (strain MV-5-4-PSL) ORGANISM #formal_name saimiriine herpesvirus 1 DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 09-Sep-1994 ACCESSIONS D48349 REFERENCE A48349 !$#authors Eberle, R.; Black, D. !$#journal Arch. Virol. (1993) 129:167-182 !$#title Sequence analysis of herpes simplex virus gB gene homologs !1of two platyrrhine monkey alpha-herpesviruses. !$#cross-references MUID:93228440; PMID:8385913 !$#accession D48349 !'##molecule_type DNA !'##residues 1-920 ##label EBE !'##note sequence extracted from NCBI backbone (NCBIN:129066, !1NCBIP:129068) CLASSIFICATION #superfamily herpesvirus glycoprotein B KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-35 #domain signal sequence #status predicted #label SIG\ !$36-920 #product glycoprotein B #status predicted #label MAT\ !$576-592 #region hydrophobic\ !$761-780 #domain transmembrane #status predicted #label TM1\ !$787-804 #domain transmembrane #status predicted #label TM2\ !$98,119,152,409,441, !$683,733 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 920 #molecular-weight 101575 #checksum 41 SEQUENCE /// ENTRY VGBEC1 #type complete TITLE glycoprotein B precursor - human cytomegalovirus (strain AD169) ALTERNATE_NAMES protein HFLF1; protein UL55 ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jul-1999 ACCESSIONS A25365; S09818 REFERENCE A25365 !$#authors Cranage, M.P.; Kouzarides, T.; Bankier, A.T.; Satchwell, S.; !1Weston, K.; Tomlinson, P.; Barrell, B.; Hart, H.; Bell, !1S.E.; Minson, A.C.; Smith, G.L. !$#journal EMBO J. (1986) 5:3057-3063 !$#title Identification of the human cytomegalovirus glycoprotein B !1gene and induction of neutralizing antibodies via its !1expression in recombinant vaccinia virus. !$#cross-references MUID:87080291; PMID:3024973 !$#accession A25365 !'##molecule_type DNA !'##residues 1-906 ##label CRA !'##cross-references GB:X04606; NID:g59798; PIDN:CAA28274.1; PID:g59799 !'##experimental_source strain AD169 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09818 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-906 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35414.1; !1PID:g1780833 !'##experimental_source strain AD169 !'##note this sequence was submitted to the EMBL Data Library, December !11989 CLASSIFICATION #superfamily herpesvirus glycoprotein B KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-906 #product glycoprotein B #status predicted #label MAT\ !$748-773 #domain transmembrane #status predicted #label TMM\ !$37,68,73,85,208, !$281,286,302,341, !$383,405,409,417, !$447,452,464,465, !$523,554,585,863 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 906 #molecular-weight 102003 #checksum 9153 SEQUENCE /// ENTRY VGBETE #type complete TITLE glycoprotein B precursor - human cytomegalovirus (strain Towne) CONTAINS glycoprotein gp55 ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 #note host Homo sapiens (man) DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jul-1999 ACCESSIONS A31288 REFERENCE A31288 !$#authors Spaete, R.R.; Thayer, R.M.; Probert, W.S.; Masiarz, F.R.; !1Chamberlain, S.H.; Rasmussen, L.; Merigan, T.C.; Pachl, C. !$#journal Virology (1988) 167:207-225 !$#title Human cytomegalovirus strain Towne glycoprotein B is !1processed by proteolytic cleavage. !$#cross-references MUID:89045645; PMID:2460994 !$#accession A31288 !'##molecule_type DNA !'##residues 1-907 ##label SPA !'##cross-references GB:M22343; NID:g330480; PIDN:AAA45920.1; !1PID:g330481 CLASSIFICATION #superfamily herpesvirus glycoprotein B KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$461-907 #product glycoprotein gp55 #status predicted #label !8GP5\ !$715-748 #domain transmembrane #status predicted #label TM1\ !$751-773 #domain transmembrane #status predicted #label TM2\ !$68,73,85,208,281, !$286,302,341,383, !$405,409,417,447, !$452,456,466,524, !$555,586,864 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 907 #molecular-weight 101953 #checksum 1003 SEQUENCE /// ENTRY VGBEMC #type complete TITLE glycoprotein B precursor - murine cytomegalovirus (strain Smith [ATCC VR-194]) ORGANISM #formal_name murine cytomegalovirus, murine herpesvirus 1 DATE 30-Jun-1992 #sequence_revision 30-Jun-1993 #text_change 09-Sep-1994 ACCESSIONS A41992; A40780; S23220 REFERENCE A41992 !$#authors Rapp, M.; Messerle, M.; Buehler, B.; Tannheimer, M.; Keil, !1G.M.; Koszinowski, U.H. !$#journal J. Virol. (1992) 66:4399-4406 !$#title Identification of the murine cytomegalovirus glycoprotein B !1gene and its expression by recombinant vaccinia virus. !$#cross-references MUID:92292266; PMID:1318410 !$#accession A41992 !'##molecule_type mRNA !'##residues 1-928 ##label RAP !'##cross-references GB:M86302 REFERENCE A40780 !$#authors Elliott, R.; Clark, C.; Jaquish, D.; Spector, D.H. !$#journal Virology (1991) 185:169-186 !$#title Transcription analysis and sequence of the putative murine !1cytomegalovirus DNA polymerase gene. !$#cross-references MUID:92024072; PMID:1718083 !$#accession A40780 !'##molecule_type DNA !'##residues 514-521,'R',523-526,'E',528-555,'T',557-561,'V',563-582, !1'Q',584-586,'K',588-616,'V',618-671,'D',673-674,'Q',676-806, !1'QRSAAAR',807-889,'T',891-928 ##label ELL !'##cross-references GB:M73549 CLASSIFICATION #superfamily herpesvirus glycoprotein B KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-36 #domain signal sequence #status predicted #label SIG\ !$37-928 #product glycoprotein B #status predicted #label GPB\ !$757-804 #domain transmembrane #status predicted #label TMN\ !$93,223,315,354,398, !$429,470,487,618,667 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 928 #molecular-weight 104208 #checksum 7606 SEQUENCE /// ENTRY A44047 #type complete TITLE glycoprotein B precursor - human herpesvirus 6 (strain GS) ORGANISM #formal_name human herpesvirus 6 DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS A44047 REFERENCE A44047 !$#authors Chou, S.; Marousek, G.I. !$#journal Virology (1992) 191:523-528 !$#title Homology of the envelope glycoprotein B of human !1herpesvirus-6 and cytomegalovirus. !$#cross-references MUID:93033157; PMID:1329336 !$#accession A44047 !'##molecule_type DNA !'##residues 1-830 ##label CHO !'##cross-references GB:M97928; NID:g325474; PIDN:AAA43847.1; !1PID:g325475 CLASSIFICATION #superfamily herpesvirus glycoprotein B KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-395,400-830 #product glycoprotein B #status predicted #label GPB\ !$24-395 #domain gp116 #status predicted #label G116\ !$400-830 #domain gp55 #status predicted #label G55\ !$656-674 #domain transmembrane #status predicted #label TM1\ !$693-710 #domain transmembrane #status predicted #label TM2\ !$155,228,247,286, !$329,355,361,486 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 830 #molecular-weight 93266 #checksum 5599 SEQUENCE /// ENTRY B44047 #type complete TITLE glycoprotein B precursor - human herpesvirus 6 (strain Z29) ORGANISM #formal_name human herpesvirus 6 DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 19-Jan-1996 ACCESSIONS B44047 REFERENCE A44047 !$#authors Chou, S.; Marousek, G.I. !$#journal Virology (1992) 191:523-528 !$#title Homology of the envelope glycoprotein B of human !1herpesvirus-6 and cytomegalovirus. !$#cross-references MUID:93033157; PMID:1329336 !$#accession B44047 !'##molecule_type DNA !'##residues 1-830 ##label CHO !'##cross-references GB:M97927 CLASSIFICATION #superfamily herpesvirus glycoprotein B KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-395,400-830 #product glycoprotein B #status predicted #label GPB\ !$24-395 #domain gp116 #status predicted #label G116\ !$400-830 #domain gp55 #status predicted #label G55\ !$656-674 #domain transmembrane #status predicted #label TM1\ !$693-710 #domain transmembrane #status predicted #label TM2\ !$155,247,286,329, !$361,486 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 830 #molecular-weight 93165 #checksum 7957 SEQUENCE /// ENTRY VGBE6S #type complete TITLE glycoprotein B - human herpesvirus 6 (strain U1102) ALTERNATE_NAMES glycoprotein B homolog CONTAINS 58K glycoprotein; 64K glycoprotein ORGANISM #formal_name human herpesvirus 6 #note host Homo sapiens (man) DATE 30-Sep-1992 #sequence_revision 19-Oct-1995 #text_change 16-Jul-1999 ACCESSIONS JQ1989; C40898 REFERENCE PQ0616 !$#authors Ellinger, K.; Neipel, F.; Foa-Tomasi, L.; Campadelli-Fiume, !1G.; Fleckenstein, B. !$#journal J. Gen. Virol. (1993) 74:495-500 !$#title The glycoprotein B homologue of human herpesvirus 6. !$#cross-references MUID:93187613; PMID:8383182 !$#accession JQ1989 !'##molecule_type DNA !'##residues 1-831 ##label ELL !'##cross-references GB:Z18287 REFERENCE A40898 !$#authors Teo, I.A.; Griffin, B.E.; Jones, M.D. !$#journal J. Virol. (1991) 65:4670-4680 !$#title Characterization of the DNA polymerase gene of human !1herpesvirus 6. !$#cross-references MUID:91333007; PMID:1651403 !$#accession C40898 !'##molecule_type DNA !'##residues 573-831 ##label TEO !'##cross-references GB:M63804; NID:g325467; PIDN:AAA74632.1; !1PID:g325470 CLASSIFICATION #superfamily herpesvirus glycoprotein B KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-396 #product 58K glycoprotein #status predicted #label !8G58\ !$401-831 #product 64K glycoprotein #status predicted #label !8G64\ !$667-686 #domain transmembrane #status predicted #label TM1\ !$694-711 #domain transmembrane #status predicted #label TM2\ !$155,228,248,287, !$308,330,356,362,487 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 831 #molecular-weight 93401 #checksum 8421 SEQUENCE /// ENTRY VGBE31 #type complete TITLE glycoprotein B - human herpesvirus 3 ALTERNATE_NAMES glycoprotein II ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS E27214 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession E27214 !'##molecule_type DNA !'##residues 1-868 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27914.1; !1PID:g60020 GENETICS !$#gene 31 CLASSIFICATION #superfamily herpesvirus glycoprotein B KEYWORDS glycoprotein; transmembrane protein FEATURE !$697-713 #domain transmembrane #status predicted #label TM1\ !$726-742 #domain transmembrane #status predicted #label TM2\ !$84,194,372,416,440, !$494,557,623,781, !$836,864 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 868 #molecular-weight 98066 #checksum 4094 SEQUENCE /// ENTRY VGBESM #type complete TITLE glycoprotein B precursor - saimiriine herpesvirus 1 (strain 11) ORGANISM #formal_name saimiriine herpesvirus 1 DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jul-1999 ACCESSIONS D34126 REFERENCE A34126 !$#authors Albrecht, J.C.; Fleckenstein, B. !$#journal Virology (1990) 174:533-542 !$#title Structural organization of the conserved gene block of !1Herpesvirus saimiri coding for DNA polymerase, glycoprotein !1B, and major DNA binding protein. !$#cross-references MUID:90163221; PMID:2154888 !$#accession D34126 !'##molecule_type DNA !'##residues 1-808 ##label ALB !'##cross-references GB:M31122; NID:g331052; PIDN:AAA46164.1; !1PID:g331056 CLASSIFICATION #superfamily herpesvirus glycoprotein B KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-808 #product glycoprotein B #status predicted #label GLB\ !$675-692 #domain transmembrane #status predicted #label TM1\ !$702-722 #domain transmembrane #status predicted #label TM2\ !$30,158,239,251,285, !$331,344,355,361, !$471,532,569,587, !$598,727 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 808 #molecular-weight 91694 #checksum 9448 SEQUENCE /// ENTRY VGBEIL #type complete TITLE glycoprotein B precursor - infectious laryngotracheitis virus (strain Thorne V882) ORGANISM #formal_name infectious laryngotracheitis virus #note host Gallus gallus (chicken) DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jun-2000 ACCESSIONS A38478; JQ0951 REFERENCE A38478 !$#authors Griffin, A.M. !$#journal J. Gen. Virol. (1991) 72:393-398 !$#title The nucleotide sequence of the glycoprotein gB gene of !1infectious laryngotracheitis virus: analysis and !1evolutionary relationship to the homologous gene from other !1herpesviruses. !$#cross-references MUID:91132136; PMID:1847176 !$#accession A38478 !'##molecule_type DNA !'##residues 1-883 ##label GRI !'##cross-references GB:D00818; NID:g221905; PIDN:BAA00699.1; !1PID:g221907 COMMENT This transmembrane protein is essential for viral !1infectivity. GENETICS !$#gene gB CLASSIFICATION #superfamily herpesvirus glycoprotein B KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-883 #product glycoprotein #status predicted #label GCP\ !$725-744 #domain transmembrane #status predicted #label TM1\ !$751-771 #domain transmembrane #status predicted #label TM2\ !$102,121,211,262, !$360,579,635,649 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 883 #molecular-weight 100160 #checksum 4968 SEQUENCE /// ENTRY VGBEIS #type complete TITLE glycoprotein B precursor - infectious laryngotracheitis virus (strain SA-2) ORGANISM #formal_name infectious laryngotracheitis virus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 09-Sep-1994 ACCESSIONS A40567 REFERENCE A40567 !$#authors Kongsuwan, K.; Prideaux, C.T.; Johnson, M.A.; Sheppard, M.; !1Fahey, K.J. !$#journal Virology (1991) 184:404-410 !$#title Nucleotide sequence of the gene encoding infectious !1laryngotracheitis virus glycoprotein B. !$#cross-references MUID:91335774; PMID:1840710 !$#accession A40567 !'##molecule_type DNA !'##residues 1-883 ##label KON !'##cross-references GB:M64927 CLASSIFICATION #superfamily herpesvirus glycoprotein B KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-883 #product glycoprotein B #status predicted #label GPB\ !$725-744 #domain transmembrane #status predicted #label TM1\ !$751-771 #domain transmembrane #status predicted #label TM2\ !$40,102,121,211,262, !$360,579,635,649 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 883 #molecular-weight 100142 #checksum 6911 SEQUENCE /// ENTRY XPBEA9 #type complete TITLE large structural phosphoprotein pp150 - human cytomegalovirus (strain AD169) ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 16-Jul-1999 ACCESSIONS A29533; S09795 REFERENCE A29533 !$#authors Jahn, G.; Kouzarides, T.; Mach, M.; Scholl, B.C.; Plachter, !1B.; Traupe, B.; Preddie, E.; Satchwell, S.C.; Fleckenstein, !1B.; Barrell, B.G. !$#journal J. Virol. (1987) 61:1358-1367 !$#title Map position and nucleotide sequence of the gene for the !1large structural phosphoprotein of human cytomegalovirus. !$#cross-references MUID:87198858; PMID:3033266 !$#accession A29533 !'##molecule_type DNA !'##residues 1-1048 ##label JAH !'##cross-references GB:M16022; NID:g330643; PIDN:AAA45992.1; !1PID:g330644 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09795 !'##molecule_type DNA !'##residues 1-1048 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35431.1; !1PID:g59637 GENETICS !$#map_position 0.160-0.186 CLASSIFICATION #superfamily human cytomegalovirus large structural !1phosphoprotein; large structural phosphoprotein homology KEYWORDS phosphoprotein FEATURE !$2-366 #domain large structural phosphoprotein homology !8#label CLS SUMMARY #length 1048 #molecular-weight 112687 #checksum 1571 SEQUENCE /// ENTRY XPBE12 #type complete TITLE major antigenic structural protein p100 - human herpesvirus 6 (strain U1102) ORGANISM #formal_name human herpesvirus 6 DATE 30-Jun-1993 #sequence_revision 29-Oct-1999 #text_change 21-Jul-2000 ACCESSIONS T09303; A42533 REFERENCE Z16644 !$#authors Nicholas, J.; Martin, M. !$#journal J. Virol. (1994) 68:597-610 !$#title Nucleotide sequence analysis of a 38.5-kilobase-pair region !1of the genome of human herpesvirus 6 encoding human !1cytomegalovirus immediate-early gene homologs and !1transactivating functions. !$#cross-references MUID:94118404; PMID:8289364 !$#accession T09303 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-871 ##label NIC !'##cross-references EMBL:L25528; NID:g451932; PIDN:AAA16716.1; !1PID:g451934 REFERENCE A42533 !$#authors Neipel, F.; Ellinger, K.; Fleckenstein, B. !$#journal J. Virol. (1992) 66:3918-3924 !$#title Gene for the major antigenic structural protein (p100) of !1human herpesvirus 6. !$#cross-references MUID:92260671; PMID:1374813 !$#accession A42533 !'##molecule_type DNA !'##residues 2-871 ##label NEI !'##cross-references GB:M87287; NID:g330673; PIDN:AAA46012.1; !1PID:g330674 GENETICS !$#gene P1LF1 CLASSIFICATION #superfamily human herpesvirus large structural !1phosphoprotein; large structural phosphoprotein homology KEYWORDS phosphoprotein FEATURE !$7-368 #domain large structural phosphoprotein homology !8#label CLS SUMMARY #length 871 #molecular-weight 97185 #checksum 1901 SEQUENCE /// ENTRY WMBE28 #type complete TITLE structural phosphoprotein pp28 - human cytomegalovirus (strain AD169) ALTERNATE_NAMES protein UL99 ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS A28842; S09864 REFERENCE A28842 !$#authors Meyer, H.; Bankier, A.T.; Landini, M.P.; Brown, C.M.; !1Barrell, B.G.; Rueger, B.; Mach, M. !$#journal J. Virol. (1988) 62:2243-2250 !$#title Identification and procaryotic expression of the gene coding !1for the highly immunogenic 28-kilodalton structural !1phosphoprotein (pp28) of human cytomegalovirus. !$#cross-references MUID:88230581; PMID:2836608 !$#accession A28842 !'##molecule_type DNA !'##residues 1-190 ##label MEY !'##cross-references GB:M21013; NID:g330631; PIDN:AAA45985.1; !1PID:g330632 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09864 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-190 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35335.1; !1PID:g1780878 !'##note this sequence was submitted to the EMBL Data Library, December !11989 CLASSIFICATION #superfamily cytomegalovirus structural phosphosprotein pp28 KEYWORDS phosphoprotein SUMMARY #length 190 #molecular-weight 20923 #checksum 3317 SEQUENCE /// ENTRY QQBEB8 #type complete TITLE UL80 protein - human cytomegalovirus (strain AD169) CONTAINS capsid assembly protein; viral proteinase (EC 3.4.21.-) ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 #note host Homo sapiens (man) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS S09843; S51034; S51035 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09843 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-708 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35353.1; !1PID:g1780857 !'##note possible protein-coding frames are given !'##note the DNA sequence was submitted to EMBL, December 1989, in !1computer-readable form REFERENCE S51034 !$#authors Stevens, J.T.; Mapelli, C.; Tsao, J.; Hail, M.; O'Boyle II, !1D.; Weinheimer, S.P.; Diianni, C.L. !$#journal Eur. J. Biochem. (1994) 226:361-367 !$#title In vitro proteolytic activity and active-site identification !1of the human cytomegalovirus protease. !$#cross-references MUID:95094793; PMID:8001553 !$#accession S51034 !'##molecule_type protein !'##residues 110-131,'X',133-134 ##label ST2 !'##note assembly protein release site (Ala-256-Ser-257) and maturation !1site (Ala-643-Ser-644) shown in vitro CLASSIFICATION #superfamily cytomegalovirus capsid assembly protein KEYWORDS capsid assembly; hydrolase; serine proteinase FEATURE !$1-256 #product viral proteinase #status predicted #label !8PMAT\ !$336-708 #product capsid assembly protein #status predicted !8#label CAP\ !$132 #active_site Ser #status experimental\ !$256-257 #cleavage_site Ala-Ser (viral proteinase) #status !8experimental\ !$643-644 #cleavage_site Ala-Ser (viral proteinase) #status !8experimental SUMMARY #length 708 #molecular-weight 73851 #checksum 5590 SEQUENCE /// ENTRY WMBECB #type complete TITLE 64K capsid assembly protein - simian cytomegalovirus (strain Colburn) ORGANISM #formal_name simian cytomegalovirus DATE 31-Dec-1989 #sequence_revision 31-Dec-1992 #text_change 08-Apr-1994 ACCESSIONS A40414; A30176 REFERENCE A40414 !$#authors Welch, A.R.; McNally, L.M.; Gibson, W. !$#journal J. Virol. (1991) 65:4091-4100 !$#title Cytomegalovirus assembly protein nested gene family: four !13'-coterminal transcripts encode four in-frame, overlapping !1proteins. !$#cross-references MUID:91303658; PMID:1649317 !$#accession A40414 !'##molecule_type mRNA !'##residues 1-590 ##label WEL !'##cross-references GB:M64627 REFERENCE A30176 !$#authors Robson, L.; Gibson, W. !$#journal J. Virol. (1989) 63:669-676 !$#title Primate cytomegalovirus assembly protein: genome location !1and nucleotide sequence. !$#cross-references MUID:89094993; PMID:2536099 !$#accession A30176 !'##molecule_type mRNA !'##residues 281-590 ##label ROB CLASSIFICATION #superfamily cytomegalovirus capsid assembly protein KEYWORDS capsid assembly FEATURE !$166-590 #product 46K capsid assembly protein #status !8predicted #label CAC\ !$281-590 #product 34K capsid assembly protein #status !8predicted #label CAD\ !$349-590 #product 27K capsid assembly protein #status !8predicted #label CAE SUMMARY #length 590 #molecular-weight 63887 #checksum 2455 SEQUENCE /// ENTRY QQBE10 #type complete TITLE BOLF1 protein - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS A43041; A03752; S32995 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession A43041 !'##molecule_type DNA !'##residues 1-1239 ##label BAN !'##cross-references EMBL:V01555; NID:g59074; PIDN:CAA24841.1; !1PID:g1334855 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region CLASSIFICATION #superfamily human herpesvirus 4 BOLF1 protein SUMMARY #length 1239 #molecular-weight 132747 #checksum 5366 SEQUENCE /// ENTRY QQBE13 #type complete TITLE BMRF1 protein - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus #note host Homo sapiens (man) DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS B43041; A03754; S32998 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession B43041 !'##molecule_type DNA !'##residues 1-404 ##label BAN !'##cross-references EMBL:V01555; NID:g59074; PIDN:CAA24844.1; !1PID:g1334858 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region CLASSIFICATION #superfamily human herpesvirus 4 BMRF1 protein KEYWORDS DNA binding; transcription regulation SUMMARY #length 404 #molecular-weight 43373 #checksum 9559 SEQUENCE /// ENTRY QQBEP4 #type complete TITLE gene 59 protein - saimiriine herpesvirus 1 (strain 11) ORGANISM #formal_name saimiriine herpesvirus 1 #note host Saimiri sciureus (common squirrel monkey) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS C36812 REFERENCE A36806 !$#authors Albrecht, J. !$#submission submitted to the EMBL Data Library, January 1992 !$#description Primary structure of the herpesvirus saimiri genome. !$#accession C36812 !'##molecule_type DNA !'##residues 1-368 ##label ALB !'##cross-references GB:X64346; NID:g60320; PIDN:CAA45682.1; PID:g60380 REFERENCE A37309 !$#authors Albrecht, J.C.; Nicholas, J.; Biller, D.; Cameron, K.R.; !1Biesinger, B.; Newman, C.; Wittmann, S.; Craxton, M.A.; !1Coleman, H.; Fleckenstein, B.; Honess, R.W. !$#journal J. Virol. (1992) 66:5047-5058 !$#title Primary structure of the herpesvirus saimiri genome. !$#cross-references MUID:92333688; PMID:1321287 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 59 CLASSIFICATION #superfamily human herpesvirus 4 BMRF1 protein SUMMARY #length 368 #molecular-weight 40453 #checksum 1797 SEQUENCE /// ENTRY QQBE14 #type complete TITLE BMRF2 protein - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus #note host Homo sapiens (man) DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS C43041; A03755; S32999 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession C43041 !'##molecule_type DNA !'##residues 1-357 ##label BAN !'##cross-references EMBL:V01555; NID:g59074; PIDN:CAA24845.1; !1PID:g1334859 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region CLASSIFICATION #superfamily human herpesvirus 4 BMRF2 protein SUMMARY #length 357 #molecular-weight 39515 #checksum 6705 SEQUENCE /// ENTRY QQBEP3 #type complete TITLE gene 58 protein - saimiriine herpesvirus 1 (strain 11) ORGANISM #formal_name saimiriine herpesvirus 1 #note host Saimiri sciureus (common squirrel monkey) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS B36812 REFERENCE A36806 !$#authors Albrecht, J. !$#submission submitted to the EMBL Data Library, January 1992 !$#description Primary structure of the herpesvirus saimiri genome. !$#accession B36812 !'##molecule_type DNA !'##residues 1-357 ##label ALB !'##cross-references GB:X64346; NID:g60320; PIDN:CAA45681.1; PID:g60379 REFERENCE A37309 !$#authors Albrecht, J.C.; Nicholas, J.; Biller, D.; Cameron, K.R.; !1Biesinger, B.; Newman, C.; Wittmann, S.; Craxton, M.A.; !1Coleman, H.; Fleckenstein, B.; Honess, R.W. !$#journal J. Virol. (1992) 66:5047-5058 !$#title Primary structure of the herpesvirus saimiri genome. !$#cross-references MUID:92333688; PMID:1321287 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 58 CLASSIFICATION #superfamily human herpesvirus 4 BMRF2 protein SUMMARY #length 357 #molecular-weight 40526 #checksum 4157 SEQUENCE /// ENTRY QQBE15 #type complete TITLE BSLF1 protein - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS D43041; A03756; S33002 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession D43041 !'##molecule_type DNA !'##residues 1-874 ##label BAN !'##cross-references EMBL:V01555; NID:g59074; PIDN:CAA24848.1; !1PID:g1334862 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region CLASSIFICATION #superfamily varicella-zoster virus gene 6 protein SUMMARY #length 874 #molecular-weight 98040 #checksum 2933 SEQUENCE /// ENTRY QQBEHA #type complete TITLE BSLF1 protein - saimiriine herpesvirus 1 (strain 11) ORGANISM #formal_name saimiriine herpesvirus 1 #note host Saimiri sciureus (common squirrel monkey) DATE 30-Sep-1989 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS I36811 REFERENCE A36806 !$#authors Albrecht, J. !$#submission submitted to the EMBL Data Library, January 1992 !$#description Primary structure of the herpesvirus saimiri genome. !$#accession I36811 !'##molecule_type DNA !'##residues 1-835 ##label ALB !'##cross-references GB:X64346; NID:g60320; PIDN:CAA45678.1; PID:g60376 REFERENCE A37309 !$#authors Albrecht, J.C.; Nicholas, J.; Biller, D.; Cameron, K.R.; !1Biesinger, B.; Newman, C.; Wittmann, S.; Craxton, M.A.; !1Coleman, H.; Fleckenstein, B.; Honess, R.W. !$#journal J. Virol. (1992) 66:5047-5058 !$#title Primary structure of the herpesvirus saimiri genome. !$#cross-references MUID:92333688; PMID:1321287 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 56 CLASSIFICATION #superfamily varicella-zoster virus gene 6 protein SUMMARY #length 835 #molecular-weight 96127 #checksum 1688 SEQUENCE /// ENTRY WZBE6 #type complete TITLE gene 6 protein - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS F27212 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession F27212 !'##molecule_type DNA !'##residues 1-1083 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27889.1; !1PID:g59995 GENETICS !$#gene 6 CLASSIFICATION #superfamily varicella-zoster virus gene 6 protein SUMMARY #length 1083 #molecular-weight 122546 #checksum 6197 SEQUENCE /// ENTRY WMBE52 #type complete TITLE UL52 protein - human herpesvirus 1 (strain 17) ORGANISM #formal_name human herpesvirus 1 #note host Homo sapiens (man) DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jun-2000 ACCESSIONS E29890; G30089 REFERENCE A93040 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Dolan, A.; McNab, D.; Perry, !1L.J.; Taylor, P.; Challberg, M.D. !$#journal J. Virol. (1988) 62:444-453 !$#title Structures of herpes simplex virus type 1 genes required for !1replication of virus DNA. !$#cross-references MUID:88091053; PMID:2826807 !$#accession E29890 !'##molecule_type DNA !'##residues 1-1058 ##label MCG !'##cross-references GB:M19122; NID:g330228; PIDN:AAA45826.1; !1PID:g330238 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession G30089 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1058 ##label MC2 !'##cross-references GB:D10879; NID:g221721; PIDN:BAA01698.1; !1PID:g221773; GB:D00317 COMMENT This protein is required for replication of viral DNA. GENETICS !$#gene UL52 CLASSIFICATION #superfamily varicella-zoster virus gene 6 protein KEYWORDS DNA biosynthesis SUMMARY #length 1058 #molecular-weight 114422 #checksum 3254 SEQUENCE /// ENTRY WZBEA6 #type complete TITLE 119K DNA helicase/primase-associated protein - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS H36795 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession H36795 !'##molecule_type DNA !'##residues 1-1081 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02442.1; !1PID:g330799 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 7 CLASSIFICATION #superfamily varicella-zoster virus gene 6 protein SUMMARY #length 1081 #molecular-weight 118962 #checksum 1679 SEQUENCE /// ENTRY QQBE16 #type complete TITLE BSRF1 protein - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus #note host Homo sapiens (man) DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS E43041; A03757; S33003 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession E43041 !'##molecule_type DNA !'##residues 1-218 ##label BAN !'##cross-references EMBL:V01555; NID:g59074; PIDN:CAA24849.1; !1PID:g1334863 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region CLASSIFICATION #superfamily human herpesvirus 4 BSRF1 protein SUMMARY #length 218 #molecular-weight 23861 #checksum 2914 SEQUENCE /// ENTRY QQBEP2 #type complete TITLE gene 55 protein - saimiriine herpesvirus 1 (strain 11) ORGANISM #formal_name saimiriine herpesvirus 1 #note host Saimiri sciureus (common squirrel monkey) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS H36811 REFERENCE A36806 !$#authors Albrecht, J. !$#submission submitted to the EMBL Data Library, January 1992 !$#description Primary structure of the herpesvirus saimiri genome. !$#accession H36811 !'##molecule_type DNA !'##residues 1-200 ##label ALB !'##cross-references GB:X64346; NID:g60320; PIDN:CAA45679.1; PID:g60377 REFERENCE A37309 !$#authors Albrecht, J.C.; Nicholas, J.; Biller, D.; Cameron, K.R.; !1Biesinger, B.; Newman, C.; Wittmann, S.; Craxton, M.A.; !1Coleman, H.; Fleckenstein, B.; Honess, R.W. !$#journal J. Virol. (1992) 66:5047-5058 !$#title Primary structure of the herpesvirus saimiri genome. !$#cross-references MUID:92333688; PMID:1321287 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 55 CLASSIFICATION #superfamily human herpesvirus 4 BSRF1 protein SUMMARY #length 200 #molecular-weight 22308 #checksum 9512 SEQUENCE /// ENTRY QQBE18 #type complete TITLE BLRF1 protein - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS F43041; A03759; S33005 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession F43041 !'##molecule_type DNA !'##residues 1-102 ##label BAN !'##cross-references EMBL:V01555; NID:g59074; PIDN:CAA24851.1; !1PID:g1334865 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region CLASSIFICATION #superfamily cytomegalovirus UL73 protein SUMMARY #length 102 #molecular-weight 10944 #checksum 4990 SEQUENCE /// ENTRY QQBEN9 #type complete TITLE gene 53 protein - saimiriine herpesvirus 1 (strain 11) ORGANISM #formal_name saimiriine herpesvirus 1 #note host Saimiri sciureus (common squirrel monkey) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS F36811 REFERENCE A36806 !$#authors Albrecht, J. !$#submission submitted to the EMBL Data Library, January 1992 !$#description Primary structure of the herpesvirus saimiri genome. !$#accession F36811 !'##molecule_type DNA !'##residues 1-90 ##label ALB !'##cross-references GB:X64346; NID:g60320; PIDN:CAA45676.1; PID:g60374 REFERENCE A37309 !$#authors Albrecht, J.C.; Nicholas, J.; Biller, D.; Cameron, K.R.; !1Biesinger, B.; Newman, C.; Wittmann, S.; Craxton, M.A.; !1Coleman, H.; Fleckenstein, B.; Honess, R.W. !$#journal J. Virol. (1992) 66:5047-5058 !$#title Primary structure of the herpesvirus saimiri genome. !$#cross-references MUID:92333688; PMID:1321287 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 53 CLASSIFICATION #superfamily cytomegalovirus UL73 protein SUMMARY #length 90 #molecular-weight 10405 #checksum 2485 SEQUENCE /// ENTRY QQBEB2 #type complete TITLE UL73 glycoprotein precursor - human cytomegalovirus (strain AD169) ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 #note host Homo sapiens (man) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS S09836 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09836 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-138 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35388.1; !1PID:g1780850 !'##note possible protein-coding frames are given !'##note the DNA sequence was submitted to EMBL, December 1989, in !1computer-readable form CLASSIFICATION #superfamily cytomegalovirus UL73 protein KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-138 #product UL73 glycoprotein #status predicted #label !8MAT\ !$102-122 #domain transmembrane #status predicted #label TMM\ !$22,23,129 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 138 #molecular-weight 14868 #checksum 2305 SEQUENCE /// ENTRY QQBE19 #type complete TITLE BLRF2 protein - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS G43041; A03760; S33006 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession G43041 !'##molecule_type DNA !'##residues 1-162 ##label BAN !'##cross-references EMBL:V01555; NID:g59074; PIDN:CAA24852.1; !1PID:g1334866 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region CLASSIFICATION #superfamily human herpesvirus 4 BLRF2 protein SUMMARY #length 162 #molecular-weight 17687 #checksum 4709 SEQUENCE /// ENTRY QQBE20 #type complete TITLE BLLF2 protein - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS H43041; A03761; S33007 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession H43041 !'##molecule_type DNA !'##residues 1-148 ##label BAN !'##cross-references EMBL:V01555; NID:g59074; PIDN:CAA24853.1; !1PID:g1334867 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region CLASSIFICATION #superfamily human herpesvirus 4 BLLF2 protein SUMMARY #length 148 #molecular-weight 16651 #checksum 3843 SEQUENCE /// ENTRY QQBE21 #type complete TITLE membrane antigen gp350 - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 28-Jul-2000 ACCESSIONS A43042; S33008; S33009; A03762 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession A43042 !'##molecule_type DNA !'##residues 1-907 ##label BAN !'##cross-references GB:V01555; GB:J02070; GB:K01729; GB:K01730; !1GB:V01554; GB:X00498; GB:X00499; GB:X00784; NID:g59074; !1PIDN:CAA24854.1; PID:g1334868 REFERENCE S32973 !$#authors Farrell, P.J. !$#submission submitted to the EMBL Data Library, March 1988 !$#accession S33008 !'##status preliminary !'##molecule_type DNA !'##residues 1-907 ##label FAR !'##cross-references EMBL:V01555; NID:g59074; PIDN:CAA24855.1; !1PID:g1334869 !$#accession S33009 !'##status preliminary !'##molecule_type DNA !'##residues 1-907 ##label FA2 !'##cross-references EMBL:V01555; NID:g59074; PIDN:CAA24855.1; !1PID:g1334869 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region CLASSIFICATION #superfamily Epstein-Barr virus membrane antigen gp350 SUMMARY #length 907 #molecular-weight 94431 #checksum 1566 SEQUENCE /// ENTRY QQBE22 #type complete TITLE membrane antigen gp220 - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 31-Dec-1993 ACCESSIONS B43042; A03763 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession B43042 !'##molecule_type DNA !'##residues 1-710 ##label BAN REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region CLASSIFICATION #superfamily Epstein-Barr virus membrane antigen gp220 SUMMARY #length 710 #molecular-weight 75170 #checksum 5968 SEQUENCE /// ENTRY QQBE23 #type complete TITLE BLRF3 protein - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS C43042; A03764 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession C43042 !'##molecule_type DNA !'##residues 1-119 ##label BAN !'##cross-references GB:V01555; GB:J02070; GB:K01729; GB:K01730; !1GB:V01554; GB:X00498; GB:X00499; GB:X00784; NID:g59074; !1PIDN:CAA24856.1; PID:g1632791 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region CLASSIFICATION #superfamily human herpesvirus 4 nuclear antigen EBNA-3A SUMMARY #length 119 #molecular-weight 12832 #checksum 9405 SEQUENCE /// ENTRY QQBE24 #type complete TITLE nuclear antigen EBNA-3B - human herpesvirus 4 (strain B95-8) ALTERNATE_NAMES BERF2A/BERF2B protein; latent protein; nuclear antigen EBNA-4A ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus #variety strain B95-8 DATE 25-Feb-1985 #sequence_revision 06-Dec-1996 #text_change 16-Jun-2000 ACCESSIONS S33012; D43042; A03765; S33011; S33013 REFERENCE S32973 !$#authors Farrell, P.J. !$#submission submitted to the EMBL Data Library, March 1988 !$#accession S33012 !'##molecule_type DNA !'##residues 1-938 ##label FAR !'##cross-references EMBL:V01555; NID:g59074; PIDN:CAA24858.1; !1PID:g1632792 !'##experimental_source strain B95-8 !'##note the coding region of this protein has been revised in EMBL !1release 49 REFERENCE S71848 !$#authors Kerdiles, B.; Walls, D.; Triki, H.; Perricaudet, M.; Joab, !1I. !$#journal J. Virol. (1990) 64:1812-1816 !$#title cDNA cloning and transient expression of the Epstein-Barr !1virus- determined nuclear antigen EBNA3A in human cells and !1identification of novel transcripts from its coding region. !$#cross-references MUID:90204695; PMID:2157061 !$#contents annotation; protein coding region REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession D43042 !'##molecule_type DNA !'##residues 1-119,'VRGT' ##label BAN !'##cross-references EMBL:V01555 !'##experimental_source strain B95-8 !'##note the coding region has been revised in reference S32973 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region GENETICS !$#introns 119/3 CLASSIFICATION #superfamily human herpesvirus 4 nuclear antigen EBNA-3B KEYWORDS nucleus SUMMARY #length 938 #molecular-weight 102860 #checksum 8433 SEQUENCE /// ENTRY QQBE25 #type complete TITLE BERF3 protein - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 23-Aug-1997 ACCESSIONS E43042; A03766; S33014 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession E43042 !'##molecule_type DNA !'##residues 1-148 ##label BAN !'##cross-references EMBL:V01555 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region CLASSIFICATION #superfamily human herpesvirus 4 nuclear antigen EBNA-3C SUMMARY #length 148 #molecular-weight 16717 #checksum 8378 SEQUENCE /// ENTRY KIBETE #type complete TITLE thymidine kinase (EC 2.7.1.21) BXLF1 - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 19-Jan-2001 ACCESSIONS A00615; S33048 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession A00615 !'##molecule_type DNA !'##residues 1-607 ##label BAN !'##cross-references GB:V01555 REFERENCE S32973 !$#authors Farrell, P.J. !$#submission submitted to the EMBL Data Library, March 1988 !$#accession S33048 !'##status preliminary !'##molecule_type DNA !'##residues 1-205,'N',207-607 ##label FAR !'##cross-references EMBL:V01555; NID:g59074; PIDN:CAA24799.1; !1PID:g1334907 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region REFERENCE A91046 !$#authors Littler, E.; Zeuthen, J.; McBride, A.A.; Sorensen, E.T.; !1Powell, K.L.; Walsh-Arrand, J.E.; Arrand, J.R. !$#journal EMBO J. (1986) 5:1959-1966 !$#title Identification of an Epstein-Barr virus-coded thymidine !1kinase. !$#cross-references MUID:87004565; PMID:3019675 !$#contents annotation CLASSIFICATION #superfamily Epstein-Barr virus BXLF1 protein; herpesvirus !1thymidine kinase homology KEYWORDS ATP; DNA biosynthesis; nucleotide binding; P-loop; !1phosphotransferase FEATURE !$284-569 #domain herpesvirus thymidine kinase homology #label !8HTK\ !$291-298 #region nucleotide-binding motif A (P-loop)\ !$388-392 #region nucleotide-binding motif B\ !$297 #binding_site ATP (Lys) #status predicted SUMMARY #length 607 #molecular-weight 67189 #checksum 3928 SEQUENCE /// ENTRY A60030 #type complete TITLE thymidine kinase (EC 2.7.1.21) - alcelaphine herpesvirus 1 ORGANISM #formal_name alcelaphine herpesvirus 1 DATE 30-Sep-1993 #sequence_revision 05-May-2000 #text_change 19-Jan-2001 ACCESSIONS T03116; A60030 REFERENCE Z14840 !$#authors Ensser, A.; Pflanz, R.; Fleckenstein, B. !$#journal J. Virol. (1997) 71:6517-6525 !$#title Primary structure of the alcelaphine herpesvirus 1 genome. !$#cross-references MUID:97404659; PMID:9261371 !$#accession T03116 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-561 ##label ENS !'##cross-references EMBL:AF005370; NID:g2337967; PIDN:AAC58068.1; !1PID:g2337984 !'##experimental_source strain C50 from host Connochaetes taurinus !1taurinus REFERENCE A60030 !$#authors Hsu, D.; Shih, L.M.; Zee, Y.C. !$#journal Arch. Virol. (1990) 113:53-60 !$#title Nucleotide sequence of a 3.5 kilobase fragment of malignant !1catarrhal fever virus strain WC11. !$#cross-references MUID:90351277; PMID:2167059 !$#accession A60030 !'##molecule_type DNA !'##residues 1-51,53,'SVARRVEVQ',63,'VNPGLK',70-92,94,'WKLHLSTR', !1103-135,'V',137-472,'R',474-557, !1'LRSISFSSSQVFSTMLFLILLCVTGAQAITTPAPPRPATTTPRRGVTSAPLIVPASSSE !1LIVTLDGTFHSVTIDMTEIRQYVRQEIIEALWNASHVFESLETTYNRYKDVYRFTDQSIR !1VNTRGSCQLVKK' ##label HSU FUNCTION !$#description catalyzes ATP-dependent phosphorylation of thymidine CLASSIFICATION #superfamily Epstein-Barr virus BXLF1 protein; herpesvirus !1thymidine kinase homology KEYWORDS ATP; DNA biosynthesis; nucleotide binding; P-loop; !1phosphotransferase FEATURE !$238-521 #domain herpesvirus thymidine kinase homology #label !8HTK\ !$245-252 #region nucleotide-binding motif A (P-loop)\ !$343-347 #region nucleotide-binding motif B\ !$251 #binding_site ATP (Lys) #status predicted SUMMARY #length 561 #molecular-weight 62795 #checksum 7997 SEQUENCE /// ENTRY QQBE26 #type complete TITLE BZLF2 protein - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS F43042; A03767; S33016 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession F43042 !'##molecule_type DNA !'##residues 1-223 ##label BAN !'##cross-references EMBL:V01555; NID:g59074; PIDN:CAA24860.1; !1PID:g1334876 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region CLASSIFICATION #superfamily human herpesvirus 4 BZLF2 protein SUMMARY #length 223 #molecular-weight 25257 #checksum 3908 SEQUENCE /// ENTRY QQBE27 #type complete TITLE BZLF1 protein - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 23-Aug-1997 ACCESSIONS G43042; A03768; S33017 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession G43042 !'##molecule_type DNA !'##residues 1-200 ##label BAN !'##cross-references EMBL:V01555 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region CLASSIFICATION #superfamily human herpesvirus 4 BZLF1 protein KEYWORDS DNA binding; transcription regulation SUMMARY #length 200 #molecular-weight 21482 #checksum 5619 SEQUENCE /// ENTRY QQBE28 #type complete TITLE BRRF1 protein - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS H43042; A03769; S33018 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession H43042 !'##molecule_type DNA !'##residues 1-310 ##label BAN !'##cross-references EMBL:V01555; NID:g59074; PIDN:CAA24813.1; !1PID:g1334877 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region CLASSIFICATION #superfamily human herpesvirus 4 BRRF1 protein SUMMARY #length 310 #molecular-weight 35319 #checksum 8805 SEQUENCE /// ENTRY QQBE3L #type complete TITLE probable membrane protein - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 16-Jul-1999 ACCESSIONS A03770; S33053 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession A03770 !'##molecule_type DNA !'##residues 1-312 ##label BAN !'##cross-references EMBL:V01555; NID:g59074; PIDN:CAA24804.1; !1PID:g1334912 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region CLASSIFICATION #superfamily Epstein-Barr virus membrane protein SUMMARY #length 312 #molecular-weight 34518 #checksum 2354 SEQUENCE /// ENTRY QQBE29 #type complete TITLE BRLF1 protein - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS A43043; A03771; S33019 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession A43043 !'##molecule_type DNA !'##residues 1-605 ##label BAN !'##cross-references EMBL:V01555; NID:g59074; PIDN:CAA24814.1; !1PID:g1334878 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region CLASSIFICATION #superfamily human herpesvirus 4 BRLF1 protein KEYWORDS DNA binding; transcription regulation SUMMARY #length 605 #molecular-weight 66594 #checksum 4207 SEQUENCE /// ENTRY QQBE30 #type complete TITLE BRRF2 protein - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS B43043; A03772; S33020 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession B43043 !'##molecule_type DNA !'##residues 1-537 ##label BAN !'##cross-references EMBL:V01555; NID:g59074; PIDN:CAA24815.1; !1PID:g1334879 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region CLASSIFICATION #superfamily human herpesvirus 4 BRRF2 protein SUMMARY #length 537 #molecular-weight 56954 #checksum 467 SEQUENCE /// ENTRY QQBE31 #type complete TITLE nuclear antigen EBNA1 - human herpesvirus 4 ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 22-Oct-1999 ACCESSIONS C43043; S42440; A03773; S33021 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession C43043 !'##molecule_type DNA !'##residues 1-641 ##label BAN !'##cross-references EMBL:V01555; NID:g59074; PIDN:CAA24816.1; !1PID:g1334880 !'##experimental_source strain B95-8 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region REFERENCE S42440 !$#authors Sample, J.; Hummel, M.; Braun, D.; Birkenbach, M.; Kieff, E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:5096-5100 !$#title Nucleotide sequences of mRNAs encoding Epstein-Barr virus !1nuclear proteins: a probable transcriptional initiation !1site. !$#cross-references MUID:86259739; PMID:3460083 !$#accession S42440 !'##status preliminary !'##molecule_type mRNA !'##residues 1-66 ##label SAM !'##cross-references EMBL:M13941; NID:g330399; PIDN:AAA45889.1; !1PID:g555157 CLASSIFICATION #superfamily Epstein-Barr virus nuclear antigen KEYWORDS DNA binding; transcription regulation SUMMARY #length 641 #molecular-weight 56427 #checksum 8480 SEQUENCE /// ENTRY S12566 #type complete TITLE translation initiation factor eIF-4B - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 29-Sep-1999 ACCESSIONS S12566 REFERENCE S12566 !$#authors Milburn, S.C.; Hershey, J.W.B.; Davies, M.V.; Kelleher, K.; !1Kaufman, R.J. !$#journal EMBO J. (1990) 9:2783-2790 !$#title Cloning and expression of eukaryotic initiation factor 4B !1cDNA: sequence determination identifies a common RNA !1recognition motif. !$#cross-references MUID:90360989; PMID:2390971 !$#accession S12566 !'##molecule_type mRNA !'##residues 1-611 ##label MIL !'##cross-references EMBL:X55733; NID:g288099; PIDN:CAA39265.1; !1PID:g288100 !'##note part of this sequence was confirmed by protein sequencing GENETICS !$#gene GDB:EIF4B; EIF-4B !'##cross-references GDB:126410; OMIM:603928 CLASSIFICATION #superfamily human translation initiation factor eIF-4B; !1ribonucleoprotein repeat homology KEYWORDS blocked amino end; protein biosynthesis; RNA binding FEATURE !$97-163 #domain ribonucleoprotein repeat homology #label RRM2 SUMMARY #length 611 #molecular-weight 69223 #checksum 2050 SEQUENCE /// ENTRY B45344 #type complete TITLE probable nuclear antigen - suid herpesvirus 1 (strain Kaplan) ORGANISM #formal_name suid herpesvirus 1 DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jul-1999 ACCESSIONS B45344 REFERENCE A45344 !$#authors Vlcek, C.; Kozmik, Z.; Paces, V.; Schirm, S.; Schwyzer, M. !$#journal Virology (1990) 179:365-377 !$#title Pseudorabies virus immediate-early gene overlaps with an !1oppositely oriented open reading frame: characterization of !1their promoter and enhancer regions. !$#cross-references MUID:91021039; PMID:2171211 !$#accession B45344 !'##status translation not shown !'##molecule_type DNA !'##residues 1-1733 ##label VLC !'##cross-references GB:M34651; NID:g334070; PIDN:AAA47471.1; !1PID:g334072 CLASSIFICATION #superfamily pseudorabies virus 1 nuclear antigen SUMMARY #length 1733 #molecular-weight 172166 #checksum 3282 SEQUENCE /// ENTRY QQBEV2 #type complete TITLE UL44 protein - human cytomegalovirus (strain AD169) ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 #note host Homo sapiens (man) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS S09807 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09807 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-433 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35403.1; !1PID:g1780822 !'##note possible protein-coding frames are given !'##note the DNA sequence was submitted to EMBL, December 1989, in !1computer-readable form CLASSIFICATION #superfamily human herpesvirus 6 P41 protein KEYWORDS nucleus SUMMARY #length 433 #molecular-weight 46233 #checksum 7201 SEQUENCE /// ENTRY QQBEHG #type complete TITLE early nuclear antigen P41 - human herpesvirus 6 (strain U1102 GS) ORGANISM #formal_name human herpesvirus 6 DATE 30-Jun-1992 #sequence_revision 21-Jul-2000 #text_change 21-Jul-2000 ACCESSIONS JQ2007; A39923 REFERENCE JQ2007 !$#authors Agulnick, A.D.; Thompson, J.R.; Iyengar, S.; Pearson, G.; !1Ablashi, D.; Ricciardi, R.P. !$#journal J. Gen. Virol. (1993) 74:1003-1009 !$#title Identification of a DNA-binding protein of human herpesvirus !16, a putative DNA polymerase stimulatory factor. !$#cross-references MUID:93286553; PMID:8389796 !$#accession JQ2007 !'##molecule_type mRNA !'##residues 1-368 ##label AGU !'##cross-references GB:L12003; NID:g325490; PIDN:AAA43855.1; !1PID:g325491 !'##experimental_source strain U1102 GS REFERENCE A39923 !$#authors Chang, C.K.; Balachandran, N. !$#journal J. Virol. (1991) 65:2884-2894 !$#title Identification, characterization, and sequence analysis of a !1cDNA encoding a phosphoprotein of human herpesvirus 6. !$#cross-references MUID:91237802; PMID:1851860 !$#accession A39923 !'##molecule_type DNA !'##residues 1-308,'G',310-320,'E',322-361, !1'EAEMRRLTDSFILGLAKGAVIPGLYTFRMTEGRSPLGQIGVLITVAISFLLTFKRFDPR !1FYKPIGDFKIVFLSLMAPKLPSLLSAVVMICLIFSEMRLRMILSRCVMIMPSYSPAVFTG !1IMVSLFFKSQMFDDYSVLITAASLLPITVRYGWMIRSSGFLLGLQKYRPILKSTSFREVD !1LKCLVKFTVEFLLLFTILWIGKMFLSMPKSNHLFFLTVVNNVFFKLNVFKALRARWWRSY !1RDL' ##label CHA !'##cross-references GB:M62700 !'##experimental_source strain U1102 GS !'##note the sequence is revised in GenBank entry HH6P41A, release 117, !1(PIDN:AAA43853.1) CLASSIFICATION #superfamily human herpesvirus 6 P41 protein KEYWORDS glycoprotein; phosphoprotein; transmembrane protein FEATURE !$38,51,231,331 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 368 #molecular-weight 41912 #checksum 7045 SEQUENCE /// ENTRY QQBE32 #type complete TITLE BKRF2 protein - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS D43043; A03774; S33022 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession D43043 !'##molecule_type DNA !'##residues 1-137 ##label BAN !'##cross-references EMBL:V01555; NID:g59074; PIDN:CAA24817.1; !1PID:g1334881 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region CLASSIFICATION #superfamily human herpesvirus 4 BKRF2 protein SUMMARY #length 137 #molecular-weight 15080 #checksum 5358 SEQUENCE /// ENTRY QQBE33 #type complete TITLE BBRF1 protein - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS E43043; A03775; S33025 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession E43043 !'##molecule_type DNA !'##residues 1-613 ##label BAN !'##cross-references EMBL:V01555; NID:g59074; PIDN:CAA24820.1; !1PID:g1334884 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region CLASSIFICATION #superfamily varicella-zoster virus gene 54 protein SUMMARY #length 613 #molecular-weight 68456 #checksum 9692 SEQUENCE /// ENTRY QQBEN6 #type complete TITLE gene 43 protein - saimiriine herpesvirus 1 (strain 11) ORGANISM #formal_name saimiriine herpesvirus 1 #note host Saimiri sciureus (common squirrel monkey) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS E36810 REFERENCE A36806 !$#authors Albrecht, J. !$#submission submitted to the EMBL Data Library, January 1992 !$#description Primary structure of the herpesvirus saimiri genome. !$#accession E36810 !'##molecule_type DNA !'##residues 1-563 ##label ALB !'##cross-references GB:X64346; NID:g60320; PIDN:CAA45667.1; PID:g60365 REFERENCE A37309 !$#authors Albrecht, J.C.; Nicholas, J.; Biller, D.; Cameron, K.R.; !1Biesinger, B.; Newman, C.; Wittmann, S.; Craxton, M.A.; !1Coleman, H.; Fleckenstein, B.; Honess, R.W. !$#journal J. Virol. (1992) 66:5047-5058 !$#title Primary structure of the herpesvirus saimiri genome. !$#cross-references MUID:92333688; PMID:1321287 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 43 CLASSIFICATION #superfamily varicella-zoster virus gene 54 protein SUMMARY #length 563 #molecular-weight 63946 #checksum 8429 SEQUENCE /// ENTRY WZBE54 #type complete TITLE gene 54 protein - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS B27215 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession B27215 !'##molecule_type DNA !'##residues 1-769 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27937.1; !1PID:g60043 GENETICS !$#gene 54 CLASSIFICATION #superfamily varicella-zoster virus gene 54 protein SUMMARY #length 769 #molecular-weight 86780 #checksum 2268 SEQUENCE /// ENTRY WMBEX6 #type complete TITLE UL6 protein - human herpesvirus 1 (strain 17) ORGANISM #formal_name human herpesvirus 1 DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jun-2000 ACCESSIONS F28133 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession F28133 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-676 ##label MCG !'##cross-references GB:X14112; NID:g1944536; PIDN:CAA32342.1; !1PID:g59506; GB:D00317 GENETICS !$#gene UL6 CLASSIFICATION #superfamily varicella-zoster virus gene 54 protein SUMMARY #length 676 #molecular-weight 74091 #checksum 1805 SEQUENCE /// ENTRY QQBEK3 #type complete TITLE UL104 protein - human cytomegalovirus (strain AD169) ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 #note host Homo sapiens (man) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS S09870 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09870 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-697 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35341.1; !1PID:g1780884 !'##note possible protein-coding frames are given !'##note the DNA sequence was submitted to EMBL, December 1989, in !1computer-readable form CLASSIFICATION #superfamily varicella-zoster virus gene 54 protein SUMMARY #length 697 #molecular-weight 78506 #checksum 8602 SEQUENCE /// ENTRY WZBEE8 #type complete TITLE gene 56 protein - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS B36801 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession B36801 !'##molecule_type DNA !'##residues 1-753 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02491.1; !1PID:g330847 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 56 CLASSIFICATION #superfamily varicella-zoster virus gene 54 protein SUMMARY #length 753 #molecular-weight 83992 #checksum 7279 SEQUENCE /// ENTRY QQBE34 #type complete TITLE BBLF4 protein - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS F43043; A03776; S33026 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession F43043 !'##molecule_type DNA !'##residues 1-809 ##label BAN !'##cross-references EMBL:V01555; NID:g59074; PIDN:CAA24821.1; !1PID:g1334885 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region CLASSIFICATION #superfamily varicella-zoster virus gene 55 protein SUMMARY #length 809 #molecular-weight 89853 #checksum 6134 SEQUENCE /// ENTRY QQBEN7 #type complete TITLE helicase (EC 3.6.1.-) - saimiriine herpesvirus 1 (strain 11) ORGANISM #formal_name saimiriine herpesvirus 1 #note host Saimiri sciureus (common squirrel monkey) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-Jan-2001 ACCESSIONS F36810 REFERENCE A36806 !$#authors Albrecht, J. !$#submission submitted to the EMBL Data Library, January 1992 !$#description Primary structure of the herpesvirus saimiri genome. !$#accession F36810 !'##molecule_type DNA !'##residues 1-781 ##label ALB !'##cross-references GB:X64346; NID:g60320; PIDN:CAA45666.1; PID:g60364 REFERENCE A37309 !$#authors Albrecht, J.C.; Nicholas, J.; Biller, D.; Cameron, K.R.; !1Biesinger, B.; Newman, C.; Wittmann, S.; Craxton, M.A.; !1Coleman, H.; Fleckenstein, B.; Honess, R.W. !$#journal J. Virol. (1992) 66:5047-5058 !$#title Primary structure of the herpesvirus saimiri genome. !$#cross-references MUID:92333688; PMID:1321287 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 44 CLASSIFICATION #superfamily varicella-zoster virus gene 55 protein KEYWORDS ATP; DNA binding; DNA repair; DNA replication; hydrolase; !1nucleotide binding; P-loop FEATURE !$64-71 #region nucleotide-binding motif A (P-loop) SUMMARY #length 781 #molecular-weight 88254 #checksum 8232 SEQUENCE /// ENTRY WZBE55 #type complete TITLE gene 55 protein - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 19-Jan-2001 ACCESSIONS C27215 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession C27215 !'##molecule_type DNA !'##residues 1-881 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27938.1; !1PID:g60044 GENETICS !$#gene 55 CLASSIFICATION #superfamily varicella-zoster virus gene 55 protein KEYWORDS nucleotide binding; P-loop FEATURE !$90-97 #region nucleotide-binding motif A (P-loop) SUMMARY #length 881 #molecular-weight 98848 #checksum 7593 SEQUENCE /// ENTRY WMBEU5 #type complete TITLE gene UL5 protein - human herpesvirus 1 (strain 17) ORGANISM #formal_name human herpesvirus 1 #note host Homo sapiens (man) DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 19-Jan-2001 ACCESSIONS A29890; E28133 REFERENCE A93040 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Dolan, A.; McNab, D.; Perry, !1L.J.; Taylor, P.; Challberg, M.D. !$#journal J. Virol. (1988) 62:444-453 !$#title Structures of herpes simplex virus type 1 genes required for !1replication of virus DNA. !$#cross-references MUID:88091053; PMID:2826807 !$#accession A29890 !'##molecule_type DNA !'##residues 1-882 ##label MCG REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession E28133 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-882 ##label MC2 !'##cross-references GB:D10879; NID:g221721; PIDN:BAA01651.1; !1PID:g221727; GB:D00317 COMMENT This protein is required for replication of viral DNA. CLASSIFICATION #superfamily varicella-zoster virus gene 55 protein KEYWORDS DNA biosynthesis; nucleotide binding; P-loop FEATURE !$97-104 #region nucleotide-binding motif A (P-loop) SUMMARY #length 882 #molecular-weight 98715 #checksum 7218 SEQUENCE /// ENTRY WMBEHQ #type fragment TITLE UL5 protein - human herpesvirus 2 (strain HG52) (fragment) ORGANISM #formal_name human herpesvirus 2 #note host Homo sapiens (man) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jun-2000 ACCESSIONS PQ0332 REFERENCE JQ1494 !$#authors McGeoch, D.J.; Cunningham, C.; McIntyre, G.; Dolan, A. !$#journal J. Gen. Virol. (1991) 72:3057-3075 !$#title Comparative sequence analysis of the long repeat regions and !1adjoining parts of the long unique regions in the genomes of !1herpes simplex viruses types 1 and 2. !$#cross-references MUID:92113549; PMID:1662697 !$#accession PQ0332 !'##molecule_type DNA !'##residues 1-783 ##label MCG !'##cross-references GB:D10470; DDBJ:D01127; NID:g221791; !1PIDN:BAA01267.1; PID:g221795 GENETICS !$#gene UL5 CLASSIFICATION #superfamily varicella-zoster virus gene 55 protein SUMMARY #length 783 #checksum 2608 SEQUENCE /// ENTRY WZBEE9 #type complete TITLE 99.5K DNA helicase/primase-associated protein - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 19-Jan-2001 ACCESSIONS C36801 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession C36801 !'##molecule_type DNA !'##residues 1-881 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02492.1; !1PID:g330848 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 57 CLASSIFICATION #superfamily varicella-zoster virus gene 55 protein KEYWORDS nucleotide binding; P-loop FEATURE !$105-112 #region nucleotide-binding motif A (P-loop) SUMMARY #length 881 #molecular-weight 99452 #checksum 1295 SEQUENCE /// ENTRY QQBEK2 #type complete TITLE UL105 protein - human cytomegalovirus (strain AD169) ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 #note host Homo sapiens (man) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS S09869 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09869 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-956 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35340.1; !1PID:g1780883 !'##note possible protein-coding frames are given !'##note the DNA sequence was submitted to EMBL, December 1989, in !1computer-readable form CLASSIFICATION #superfamily varicella-zoster virus gene 55 protein SUMMARY #length 956 #molecular-weight 106499 #checksum 8769 SEQUENCE /// ENTRY QQBE35 #type complete TITLE BBRF3 protein - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS G43043; A03777; S33030 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession G43043 !'##molecule_type DNA !'##residues 1-405 ##label BAN !'##cross-references EMBL:V01555; NID:g59074; PIDN:CAA24825.1; !1PID:g1334889 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region CLASSIFICATION #superfamily cytomegalovirus UL100 protein SUMMARY #length 405 #molecular-weight 45792 #checksum 4554 SEQUENCE /// ENTRY QQBEN5 #type complete TITLE integral membrane protein - saimiriine herpesvirus 1 (strain 11) ORGANISM #formal_name saimiriine herpesvirus 1 #note host Saimiri sciureus (common squirrel monkey) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS A36810 REFERENCE A36806 !$#authors Albrecht, J. !$#submission submitted to the EMBL Data Library, January 1992 !$#description Primary structure of the herpesvirus saimiri genome. !$#accession A36810 !'##molecule_type DNA !'##residues 1-366 ##label ALB !'##cross-references GB:X64346; NID:g60320; PIDN:CAA45662.1; PID:g60360 REFERENCE A37309 !$#authors Albrecht, J.C.; Nicholas, J.; Biller, D.; Cameron, K.R.; !1Biesinger, B.; Newman, C.; Wittmann, S.; Craxton, M.A.; !1Coleman, H.; Fleckenstein, B.; Honess, R.W. !$#journal J. Virol. (1992) 66:5047-5058 !$#title Primary structure of the herpesvirus saimiri genome. !$#cross-references MUID:92333688; PMID:1321287 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 39 CLASSIFICATION #superfamily cytomegalovirus UL100 protein KEYWORDS transmembrane protein FEATURE !$18-34 #domain transmembrane #status predicted #label TM1\ !$87-103 #domain transmembrane #status predicted #label TM2\ !$152-168 #domain transmembrane #status predicted #label TM3\ !$214-230 #domain transmembrane #status predicted #label TM4\ !$236-252 #domain transmembrane #status predicted #label TM5\ !$274-290 #domain transmembrane #status predicted #label TM6\ !$305-321 #domain transmembrane #status predicted #label TM7 SUMMARY #length 366 #molecular-weight 42182 #checksum 7071 SEQUENCE /// ENTRY QQBEJ7 #type complete TITLE UL100 protein - human cytomegalovirus (strain AD169) ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 #note host Homo sapiens (man) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS S09865 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09865 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-372 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35336.1; !1PID:g1780879 !'##note possible protein-coding frames are given !'##note the DNA sequence was submitted to EMBL, December 1989, in !1computer-readable form CLASSIFICATION #superfamily cytomegalovirus UL100 protein SUMMARY #length 372 #molecular-weight 42861 #checksum 5107 SEQUENCE /// ENTRY QQBE36 #type complete TITLE BBLF1 protein - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS H43043; A03778; S33031 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession H43043 !'##molecule_type DNA !'##residues 1-75 ##label BAN !'##cross-references EMBL:V01555; NID:g59074; PIDN:CAA24826.1; !1PID:g1334890 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region CLASSIFICATION #superfamily human herpesvirus 4 BBLF1 protein SUMMARY #length 75 #molecular-weight 8470 #checksum 5818 SEQUENCE /// ENTRY QQBE4L #type complete TITLE probable glycoprotein - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 16-Jul-1999 ACCESSIONS A03780; S33052 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession A03780 !'##molecule_type DNA !'##residues 1-248 ##label BAN !'##cross-references EMBL:V01555; NID:g59074; PIDN:CAA24803.1; !1PID:g1334911 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region CLASSIFICATION #superfamily Epstein-Barr virus glycoprotein KEYWORDS glycoprotein FEATURE !$27,45,73,83,92,95, !$104,116,131,144 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 248 #molecular-weight 27076 #checksum 534 SEQUENCE /// ENTRY QQBEM8 #type complete TITLE gene 29 protein - saimiriine herpesvirus 1 (strain 11) ORGANISM #formal_name saimiriine herpesvirus 1 #note host Saimiri sciureus (common squirrel monkey) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS I36808 REFERENCE A36806 !$#authors Albrecht, J. !$#submission submitted to the EMBL Data Library, January 1992 !$#description Primary structure of the herpesvirus saimiri genome. !$#accession I36808 !'##molecule_type DNA !'##residues 1-683 ##label ALB !'##cross-references GB:X64346; NID:g60320; PIDN:CAA45657.1; PID:g60355 REFERENCE A37309 !$#authors Albrecht, J.C.; Nicholas, J.; Biller, D.; Cameron, K.R.; !1Biesinger, B.; Newman, C.; Wittmann, S.; Craxton, M.A.; !1Coleman, H.; Fleckenstein, B.; Honess, R.W. !$#journal J. Virol. (1992) 66:5047-5058 !$#title Primary structure of the herpesvirus saimiri genome. !$#cross-references MUID:92333688; PMID:1321287 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 29 !$#introns 303/3 CLASSIFICATION #superfamily herpesvirus 38K protein SUMMARY #length 683 #molecular-weight 77049 #checksum 6500 SEQUENCE /// ENTRY QQBEI5 #type complete TITLE UL89 protein - human cytomegalovirus (strain AD169) ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 #note host Homo sapiens (man) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 17-Feb-1995 ACCESSIONS S09853 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09853 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-724 ##label CHE !'##cross-references EMBL:X17403 !'##note possible protein-coding frames are given !'##note the DNA sequence was submitted to EMBL, December 1989, in !1computer-readable form CLASSIFICATION #superfamily herpesvirus 38K protein SUMMARY #length 724 #molecular-weight 82587 #checksum 2949 SEQUENCE /// ENTRY QQBEH6 #type complete TITLE 12L protein - human herpesvirus 6 (strain Uganda-1102) ORGANISM #formal_name human herpesvirus 6 DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 08-Apr-1994 ACCESSIONS A33560 REFERENCE A33560 !$#authors Lawrence, G.L.; Chee, M.; Craxton, M.A.; Gompels, U.A.; !1Honess, R.W.; Barrell, B.G. !$#journal J. Virol. (1990) 64:287-299 !$#title Human herpesvirus 6 is closely related to human !1cytomegalovirus. !$#cross-references MUID:90080132; PMID:2152817 !$#accession A33560 !'##molecule_type DNA !'##residues 1-667 ##label LAW !'##cross-references GB:M28243 CLASSIFICATION #superfamily herpesvirus 38K protein SUMMARY #length 667 #molecular-weight 76331 #checksum 3640 SEQUENCE /// ENTRY WMBET5 #type complete TITLE UL15 protein - human herpesvirus 1 (strain 17) ORGANISM #formal_name human herpesvirus 1 DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jun-2000 ACCESSIONS F30083; A43970 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession F30083 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-735 ##label MCG !'##cross-references GB:X14112; NID:g1944536; PIDN:CAA32330.1; !1PID:g59501; GB:D00317 GENETICS !$#gene UL15 !$#introns 343/3 CLASSIFICATION #superfamily herpesvirus 38K protein SUMMARY #length 735 #molecular-weight 80922 #checksum 8412 SEQUENCE /// ENTRY WMBE31 #type complete TITLE 38K protein - human herpesvirus 1 ORGANISM #formal_name human herpesvirus 1 #note host Homo sapiens (man) DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 16-Jul-1999 ACCESSIONS A03781 REFERENCE A93620 !$#authors McGeoch, D.J.; Dolan, A.; Frame, M.C. !$#journal Nucleic Acids Res. (1986) 14:3435-3448 !$#title DNA sequence of the region in the genome of herpes simplex !1virus type 1 containing the exonuclease gene and !1neighbouring genes. !$#cross-references MUID:86205244; PMID:3010237 !$#accession A03781 !'##molecule_type DNA !'##residues 1-344 ##label HOM !'##cross-references GB:X03839; NID:g59841; PIDN:CAA27456.1; PID:g59847 !'##experimental_source strain 17 GENETICS !$#map_position 0.16-0.20 CLASSIFICATION #superfamily herpesvirus 38K protein SUMMARY #length 344 #molecular-weight 38440 #checksum 1146 SEQUENCE /// ENTRY WZBE45 #type complete TITLE gene 45 protein - human herpesvirus 3 CONTAINS gene 42 protein ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 28-Jul-2000 ACCESSIONS A27344 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession A27344 !'##molecule_type DNA !'##residues 1-747 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAB55553.1; !1PID:g5869808 GENETICS !$#gene 45 CLASSIFICATION #superfamily herpesvirus 38K protein FEATURE !$353-747 #product gene 42 protein #status predicted #label GFP SUMMARY #length 747 #molecular-weight 82756 #checksum 3835 SEQUENCE /// ENTRY WZBEA1 #type complete TITLE DNA-packaging protein - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS A36795 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession A36795 !'##molecule_type DNA !'##residues 1-734 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02480.1; !1PID:g330792 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 44 !$#introns 345/1 CLASSIFICATION #superfamily herpesvirus 38K protein KEYWORDS DNA packaging SUMMARY #length 734 #molecular-weight 81077 #checksum 8886 SEQUENCE /// ENTRY QQBE38 #type complete TITLE BGRF1 protein - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS A43044; A03782; S33034 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession A43044 !'##molecule_type DNA !'##residues 1-325 ##label BAN !'##cross-references EMBL:V01555; NID:g59074; PIDN:CAA24829.1; !1PID:g1334893 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region CLASSIFICATION #superfamily herpesvirus 38K protein SUMMARY #length 325 #molecular-weight 36462 #checksum 3547 SEQUENCE /// ENTRY QQBE39 #type complete TITLE BGLF3 protein - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS B43044; A03783; S33035 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession B43044 !'##molecule_type DNA !'##residues 1-332 ##label BAN !'##cross-references EMBL:V01555; NID:g59074; PIDN:CAA24830.1; !1PID:g1334894 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region CLASSIFICATION #superfamily human herpesvirus 4 BGLF3 protein SUMMARY #length 332 #molecular-weight 37708 #checksum 9723 SEQUENCE /// ENTRY QQBEN3 #type complete TITLE gene 34 protein - saimiriine herpesvirus 1 (strain 11) ORGANISM #formal_name saimiriine herpesvirus 1 #note host Saimiri sciureus (common squirrel monkey) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS E36809 REFERENCE A36806 !$#authors Albrecht, J. !$#submission submitted to the EMBL Data Library, January 1992 !$#description Primary structure of the herpesvirus saimiri genome. !$#accession E36809 !'##molecule_type DNA !'##residues 1-316 ##label ALB !'##cross-references GB:X64346; NID:g60320; PIDN:CAA45656.1; PID:g60354 REFERENCE A37309 !$#authors Albrecht, J.C.; Nicholas, J.; Biller, D.; Cameron, K.R.; !1Biesinger, B.; Newman, C.; Wittmann, S.; Craxton, M.A.; !1Coleman, H.; Fleckenstein, B.; Honess, R.W. !$#journal J. Virol. (1992) 66:5047-5058 !$#title Primary structure of the herpesvirus saimiri genome. !$#cross-references MUID:92333688; PMID:1321287 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 34 CLASSIFICATION #superfamily human herpesvirus 4 BGLF3 protein SUMMARY #length 316 #molecular-weight 36256 #checksum 9269 SEQUENCE /// ENTRY QQBE40 #type complete TITLE BGLF2 protein - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS C43044; JQ1381; A03784; A03794; S33036 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession C43044 !'##molecule_type DNA !'##residues 1-336 ##label BAN !'##cross-references EMBL:V01555; NID:g59074; PIDN:CAA24831.1; !1PID:g1334895 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region !$#note neither amino acid nor nucleotide sequence is given REFERENCE JQ1381 !$#authors Chen, M.R.; Hsu, T.Y.; Lin, S.W.; Chen, J.Y.; Yang, C.S. !$#journal J. Gen. Virol. (1991) 72:3047-3055 !$#title Cloning and characterization of cDNA clones corresponding to !1transcripts from the BamHI G region of the Epstein-Barr !1virus genome and expression of BGLF2. !$#cross-references MUID:92113548; PMID:1662696 !$#accession JQ1381 !'##molecule_type mRNA !'##residues 1-336 ##label CHE !'##cross-references GB:S77132; NID:g243314; PIDN:AAB21113.1; !1PID:g243315 CLASSIFICATION #superfamily Epstein-Barr virus BGLF2 protein SUMMARY #length 336 #molecular-weight 36888 #checksum 8731 SEQUENCE /// ENTRY QQBEN2 #type complete TITLE gene 33 protein - saimiriine herpesvirus 1 (strain 11) ORGANISM #formal_name saimiriine herpesvirus 1 #note host Saimiri sciureus (common squirrel monkey) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS D36809 REFERENCE A36806 !$#authors Albrecht, J. !$#submission submitted to the EMBL Data Library, January 1992 !$#description Primary structure of the herpesvirus saimiri genome. !$#accession D36809 !'##molecule_type DNA !'##residues 1-330 ##label ALB !'##cross-references GB:X64346; NID:g60320; PIDN:CAA45655.1; PID:g60353 REFERENCE A37309 !$#authors Albrecht, J.C.; Nicholas, J.; Biller, D.; Cameron, K.R.; !1Biesinger, B.; Newman, C.; Wittmann, S.; Craxton, M.A.; !1Coleman, H.; Fleckenstein, B.; Honess, R.W. !$#journal J. Virol. (1992) 66:5047-5058 !$#title Primary structure of the herpesvirus saimiri genome. !$#cross-references MUID:92333688; PMID:1321287 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 33 CLASSIFICATION #superfamily Epstein-Barr virus BGLF2 protein SUMMARY #length 330 #molecular-weight 36993 #checksum 1601 SEQUENCE /// ENTRY QQBE41 #type complete TITLE BGLF1 protein - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS D43044; A03785; S33037 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession D43044 !'##molecule_type DNA !'##residues 1-507 ##label BAN !'##cross-references EMBL:V01555; NID:g59074; PIDN:CAA24832.1; !1PID:g1334896 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region CLASSIFICATION #superfamily human herpesvirus 4 BGLF1 protein SUMMARY #length 507 #molecular-weight 54462 #checksum 5997 SEQUENCE /// ENTRY QQBEN1 #type complete TITLE gene 32 protein - saimiriine herpesvirus 1 (strain 11) ORGANISM #formal_name saimiriine herpesvirus 1 #note host Saimiri sciureus (common squirrel monkey) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS C36809 REFERENCE A36806 !$#authors Albrecht, J. !$#submission submitted to the EMBL Data Library, January 1992 !$#description Primary structure of the herpesvirus saimiri genome. !$#accession C36809 !'##molecule_type DNA !'##residues 1-441 ##label ALB !'##cross-references GB:X64346; NID:g60320; PIDN:CAA45654.1; PID:g60352 REFERENCE A37309 !$#authors Albrecht, J.C.; Nicholas, J.; Biller, D.; Cameron, K.R.; !1Biesinger, B.; Newman, C.; Wittmann, S.; Craxton, M.A.; !1Coleman, H.; Fleckenstein, B.; Honess, R.W. !$#journal J. Virol. (1992) 66:5047-5058 !$#title Primary structure of the herpesvirus saimiri genome. !$#cross-references MUID:92333688; PMID:1321287 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 32 CLASSIFICATION #superfamily human herpesvirus 4 BGLF1 protein SUMMARY #length 441 #molecular-weight 50830 #checksum 6349 SEQUENCE /// ENTRY QQBEM9 #type complete TITLE gene 31 protein - saimiriine herpesvirus 1 (strain 11) ORGANISM #formal_name saimiriine herpesvirus 1 #note host Saimiri sciureus (common squirrel monkey) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS B36809 REFERENCE A36806 !$#authors Albrecht, J. !$#submission submitted to the EMBL Data Library, January 1992 !$#description Primary structure of the herpesvirus saimiri genome. !$#accession B36809 !'##molecule_type DNA !'##residues 1-208 ##label ALB !'##cross-references GB:X64346; NID:g60320; PIDN:CAA45653.1; PID:g60351 REFERENCE A37309 !$#authors Albrecht, J.C.; Nicholas, J.; Biller, D.; Cameron, K.R.; !1Biesinger, B.; Newman, C.; Wittmann, S.; Craxton, M.A.; !1Coleman, H.; Fleckenstein, B.; Honess, R.W. !$#journal J. Virol. (1992) 66:5047-5058 !$#title Primary structure of the herpesvirus saimiri genome. !$#cross-references MUID:92333688; PMID:1321287 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 31 CLASSIFICATION #superfamily cytomegalovirus UL92 protein SUMMARY #length 208 #molecular-weight 24347 #checksum 2680 SEQUENCE /// ENTRY QQBE42 #type complete TITLE BDLF4 protein - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS E43044; A03786; S33038 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession E43044 !'##molecule_type DNA !'##residues 1-225 ##label BAN !'##cross-references EMBL:V01555; NID:g59074; PIDN:CAA24833.1; !1PID:g1334897 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region CLASSIFICATION #superfamily cytomegalovirus UL92 protein SUMMARY #length 225 #molecular-weight 25448 #checksum 2446 SEQUENCE /// ENTRY QQBEI8 #type complete TITLE UL92 protein - human cytomegalovirus (strain AD169) ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 #note host Homo sapiens (man) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS S09856 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09856 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-201 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35366.1; !1PID:g1780870 !'##note possible protein-coding frames are given !'##note the DNA sequence was submitted to EMBL, December 1989, in !1computer-readable form CLASSIFICATION #superfamily cytomegalovirus UL92 protein SUMMARY #length 201 #molecular-weight 22511 #checksum 6679 SEQUENCE /// ENTRY QQBEH8 #type complete TITLE 9R protein - human herpesvirus 6 (strain Uganda-1102) ORGANISM #formal_name human herpesvirus 6 DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jul-1999 ACCESSIONS I33560 REFERENCE A33560 !$#authors Lawrence, G.L.; Chee, M.; Craxton, M.A.; Gompels, U.A.; !1Honess, R.W.; Barrell, B.G. !$#journal J. Virol. (1990) 64:287-299 !$#title Human herpesvirus 6 is closely related to human !1cytomegalovirus. !$#cross-references MUID:90080132; PMID:2152817 !$#accession I33560 !'##molecule_type DNA !'##residues 1-216 ##label LAW !'##cross-references GB:M68963; GB:M28243; NID:g325494; PIDN:AAA65572.1; !1PID:g325504 CLASSIFICATION #superfamily cytomegalovirus UL92 protein SUMMARY #length 216 #molecular-weight 24782 #checksum 1253 SEQUENCE /// ENTRY QQBE43 #type complete TITLE membrane antigen gp85 - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS F43044; A03787; S33040 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession F43044 !'##molecule_type DNA !'##residues 1-234 ##label BAN !'##cross-references EMBL:V01555; NID:g59074; PIDN:CAA24835.1; !1PID:g1334899 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region CLASSIFICATION #superfamily Epstein-Barr virus membrane antigen gp85 SUMMARY #length 234 #molecular-weight 23791 #checksum 8909 SEQUENCE /// ENTRY QQBE44 #type complete TITLE BDLF2 protein - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS G43044; A03788; S33041 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession G43044 !'##molecule_type DNA !'##residues 1-420 ##label BAN !'##cross-references EMBL:V01555; NID:g59074; PIDN:CAA24836.1; !1PID:g1334900 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region CLASSIFICATION #superfamily human herpesvirus 4 BDLF2 protein SUMMARY #length 420 #molecular-weight 46168 #checksum 2796 SEQUENCE /// ENTRY VCBEM7 #type complete TITLE major capsid protein - saimiriine herpesvirus 1 (strain 11) ORGANISM #formal_name saimiriine herpesvirus 1 #note host Saimiri sciureus (common squirrel monkey) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS E36808 REFERENCE A36806 !$#authors Albrecht, J. !$#submission submitted to the EMBL Data Library, January 1992 !$#description Primary structure of the herpesvirus saimiri genome. !$#accession E36808 !'##molecule_type DNA !'##residues 1-1371 ##label ALB !'##cross-references GB:X64346; NID:g60320; PIDN:CAA45648.1; PID:g60346 REFERENCE A37309 !$#authors Albrecht, J.C.; Nicholas, J.; Biller, D.; Cameron, K.R.; !1Biesinger, B.; Newman, C.; Wittmann, S.; Craxton, M.A.; !1Coleman, H.; Fleckenstein, B.; Honess, R.W. !$#journal J. Virol. (1992) 66:5047-5058 !$#title Primary structure of the herpesvirus saimiri genome. !$#cross-references MUID:92333688; PMID:1321287 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 25 CLASSIFICATION #superfamily varicella-zoster virus major capsid protein KEYWORDS capsid protein SUMMARY #length 1371 #molecular-weight 154354 #checksum 5536 SEQUENCE /// ENTRY QQBE45 #type complete TITLE major capsid protein - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS H43044; A03789; S33043 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession H43044 !'##molecule_type DNA !'##residues 1-1381 ##label BAN !'##cross-references EMBL:V01555; NID:g59074; PIDN:CAA24794.1; !1PID:g1334902 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region CLASSIFICATION #superfamily varicella-zoster virus major capsid protein SUMMARY #length 1381 #molecular-weight 153916 #checksum 4675 SEQUENCE /// ENTRY VCBE17 #type complete TITLE major capsid protein - human herpesvirus 1 (strain 17) ORGANISM #formal_name human herpesvirus 1 DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 16-Jun-2000 ACCESSIONS A27239; A30084 REFERENCE A27239 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:2279-2286 !$#title DNA sequence of the major capsid protein gene of herpes !1simplex virus type 1. !$#cross-references MUID:87010565; PMID:3020164 !$#accession A27239 !'##molecule_type DNA !'##residues 1-1374 ##label DAV !'##cross-references GB:X04467; NID:g59857; PIDN:CAA28154.1; PID:g59859 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession A30084 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1374 ##label MCG !'##cross-references GB:X14112; NID:g1944536; PIDN:CAA32332.1; !1PID:g59519; GB:D00317 GENETICS !$#gene UL19 CLASSIFICATION #superfamily varicella-zoster virus major capsid protein KEYWORDS capsid protein SUMMARY #length 1374 #molecular-weight 149082 #checksum 2612 SEQUENCE /// ENTRY VCBE40 #type complete TITLE major capsid protein - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS E27341 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession E27341 !'##molecule_type DNA !'##residues 1-1396 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27923.1; !1PID:g60029 GENETICS !$#gene 40 CLASSIFICATION #superfamily varicella-zoster virus major capsid protein KEYWORDS capsid protein SUMMARY #length 1396 #molecular-weight 154978 #checksum 1457 SEQUENCE /// ENTRY VCBED6 #type complete TITLE major capsid protein - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS H36799 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession H36799 !'##molecule_type DNA !'##residues 1-1376 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02478.1; !1PID:g330835 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 42 CLASSIFICATION #superfamily varicella-zoster virus major capsid protein KEYWORDS capsid protein SUMMARY #length 1376 #molecular-weight 152182 #checksum 7079 SEQUENCE /// ENTRY VCBES5 #type complete TITLE major capsid protein - suid herpesvirus 1 (strain Indiana 5) ORGANISM #formal_name suid herpesvirus 1 DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 08-Apr-1994 ACCESSIONS A40777 REFERENCE A40777 !$#authors Yamada, S.; Imada, T.; Watanabe, W.; Honda, Y.; !1Nakajima-Iijima, S.; Shimizu, Y.; Sekikawa, K. !$#journal Virology (1991) 185:56-66 !$#title Nucleotide sequence and transcriptional mapping of the major !1capsid protein gene of pseudorabies virus. !$#cross-references MUID:92024125; PMID:1718089 !$#accession A40777 !'##molecule_type DNA !'##residues 1-1330 ##label YAM !'##cross-references GB:M95285 CLASSIFICATION #superfamily varicella-zoster virus major capsid protein KEYWORDS capsid protein SUMMARY #length 1330 #molecular-weight 145936 #checksum 9927 SEQUENCE /// ENTRY VCBECA #type complete TITLE major capsid protein - human cytomegalovirus (strain AD169) ALTERNATE_NAMES protein HaLF1; protein UL86 ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS A31882; S09850 REFERENCE A31882 !$#authors Chee, M.; Rudolph, S.A.; Plachter, B.; Barrell, B.; Jahn, G. !$#journal J. Virol. (1989) 63:1345-1353 !$#title Identification of the major capsid protein gene of human !1cytomegalovirus. !$#cross-references MUID:89125729; PMID:2536837 !$#accession A31882 !'##molecule_type DNA !'##residues 1-1370 ##label CH1 !'##cross-references GB:M25411; NID:g330612; PIDN:AAA51532.1; !1PID:g330613 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09850 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1370 ##label CH2 !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35360.1; !1PID:g1780864 !'##note this sequence was submitted to the EMBL Data Library, December !11989 CLASSIFICATION #superfamily varicella-zoster virus major capsid protein KEYWORDS capsid protein; coat protein SUMMARY #length 1370 #molecular-weight 153871 #checksum 8058 SEQUENCE /// ENTRY VCBEH6 #type complete TITLE major capsid protein - human herpesvirus 6 (strain Uganda-1102) ORGANISM #formal_name human herpesvirus 6 #note host Homo sapiens (man) DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 06-Jan-1995 ACCESSIONS E33560; A33941 REFERENCE A33560 !$#authors Lawrence, G.L.; Chee, M.; Craxton, M.A.; Gompels, U.A.; !1Honess, R.W.; Barrell, B.G. !$#journal J. Virol. (1990) 64:287-299 !$#title Human herpesvirus 6 is closely related to human !1cytomegalovirus. !$#cross-references MUID:90080132; PMID:2152817 !$#accession E33560 !'##molecule_type DNA !'##residues 1-1345 ##label LAW !'##cross-references GB:M28243 REFERENCE A33941 !$#authors Littler, E.; Lawrence, G.; Liu, M.Y.; Barrell, B.G.; Arrand, !1J.R. !$#journal J. Virol. (1990) 64:714-722 !$#title Identification, cloning, and expression of the major capsid !1protein gene of human herpesvirus 6. !$#cross-references MUID:90112641; PMID:2153237 !$#accession A33941 !'##molecule_type DNA !'##residues 1-1345 ##label LIT CLASSIFICATION #superfamily varicella-zoster virus major capsid protein KEYWORDS capsid protein; coat protein SUMMARY #length 1345 #molecular-weight 151950 #checksum 3268 SEQUENCE /// ENTRY A47521 #type complete TITLE capsid protein - giardiavirus GLV ORGANISM #formal_name giardiavirus, GLV DATE 21-Jan-1994 #sequence_revision 13-Feb-1998 #text_change 16-Jul-1999 ACCESSIONS A47521 REFERENCE A47521 !$#authors Wang, A.L.; Yang, H.M.; Shen, K.A.; Wang, C.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:8595-8599 !$#title Giardiavirus double-stranded RNA genome encodes a capsid !1polypeptide and a gag-pol-like fusion protein by a !1translation frameshift. !$#cross-references MUID:93391401; PMID:8378334 !$#contents host Giardia lamblia !$#accession A47521 !'##molecule_type genomic RNA !'##residues 1-886 ##label WAN !'##cross-references GB:L13218; NID:g1352866; PIDN:AAB01578.1; !1PID:g1352867 !'##note sequence modified after extraction from NCBI backbone !1(NCBIN:137593, NCBIP:137594) CLASSIFICATION #superfamily giardiavirus capsid protein KEYWORDS capsid protein SUMMARY #length 886 #molecular-weight 98423 #checksum 1449 SEQUENCE /// ENTRY WMBEL1 #type complete TITLE latency-related protein 1 - human herpesvirus 1 (strain F) ORGANISM #formal_name human herpesvirus 1 #note host Homo sapiens (man) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 10-Sep-1999 ACCESSIONS A33337 REFERENCE A94388 !$#authors Wechsler, S.L.; Nesburn, A.B.; Zwaagstra, J.; Ghiasi, H. !$#journal Virology (1989) 168:168-172 !$#title Sequence of the latency-related gene of herpes simplex virus !1type 1. !$#cross-references MUID:89085598; PMID:2535901 !$#accession A33337 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-340 ##label WEC !'##cross-references GB:J04323; NID:g330133; PIDN:AAA45799.1; !1PID:g330134 GENETICS !$#introns 249/2 CLASSIFICATION #superfamily herpesvirus latency-related protein 1 KEYWORDS tandem repeat FEATURE !$26-41 #region 16-residue tandem repeat\ !$42-57 #region 16-residue tandem repeat\ !$58-73 #region 16-residue tandem repeat SUMMARY #length 340 #molecular-weight 35604 #checksum 4407 SEQUENCE /// ENTRY WMBEL2 #type complete TITLE latency-related protein 2 - human herpesvirus 1 (strain F) ORGANISM #formal_name human herpesvirus 1 #note host Homo sapiens (man) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS B33337 REFERENCE A94388 !$#authors Wechsler, S.L.; Nesburn, A.B.; Zwaagstra, J.; Ghiasi, H. !$#journal Virology (1989) 168:168-172 !$#title Sequence of the latency-related gene of herpes simplex virus !1type 1. !$#cross-references MUID:89085598; PMID:2535901 !$#accession B33337 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-107 ##label WEC !'##cross-references GB:J04323; NID:g330133; PIDN:AAA45800.1; !1PID:g330135 CLASSIFICATION #superfamily herpesvirus latency-related protein 2 KEYWORDS tandem repeat FEATURE !$2-49 #region 16-residue repeats SUMMARY #length 107 #molecular-weight 11915 #checksum 8646 SEQUENCE /// ENTRY DNBE17 #type complete TITLE tandem-repeated DNA-binding protein - human herpesvirus 1 ORGANISM #formal_name human herpesvirus 1 #note host Homo sapiens (man) DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 16-Jul-1999 ACCESSIONS A03728 REFERENCE A00656 !$#authors McGeoch, D.J.; Dolan, A.; Donald, S.; Rixon, F.J. !$#journal J. Mol. Biol. (1985) 181:1-13 !$#title Sequence determination and genetic content of the short !1unique region in the genome of herpes simplex virus type 1. !$#cross-references MUID:85160822; PMID:2984429 !$#accession A03728 !'##molecule_type DNA !'##residues 1-161 ##label MCG !'##cross-references GB:X02138; NID:g59865; PIDN:CAA26065.1; PID:g757867 !'##experimental_source strain 17 CLASSIFICATION #superfamily herpesvirus tandem-repeated DNA-binding protein KEYWORDS DNA binding; tandem repeat FEATURE !$85-156 #region 6-residue repeats SUMMARY #length 161 #molecular-weight 17757 #checksum 4894 SEQUENCE /// ENTRY DNBEV1 #type complete TITLE major DNA-binding protein UL29 - human herpesvirus 1 (strain 17) ORGANISM #formal_name human herpesvirus 1 #note host Homo sapiens (man) DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 16-Jun-2000 ACCESSIONS A03790; B30085 REFERENCE A93601 !$#authors Quinn, J.P.; McGeoch, D.J. !$#journal Nucleic Acids Res. (1985) 13:8143-8163 !$#title DNA sequence of the region in the genome of herpes simplex !1virus type 1 containing the genes for DNA polymerase and the !1major DNA binding protein. !$#cross-references MUID:86067223; PMID:2999714 !$#accession A03790 !'##molecule_type DNA !'##residues 1-1196 ##label QUI !'##cross-references GB:X03181; GB:M12356; NID:g59862; PIDN:CAA26940.1; !1PID:g59863 !'##experimental_source strain 17 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession B30085 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1196 ##label MCG !'##cross-references GB:D10879; NID:g221721; PIDN:BAA01675.1; !1PID:g221750; GB:D00317 GENETICS !$#gene UL29 !$#map_position 0.38-0.409 CLASSIFICATION #superfamily herpesvirus DNA-binding protein KEYWORDS DNA binding SUMMARY #length 1196 #molecular-weight 128349 #checksum 3643 SEQUENCE /// ENTRY DNBEKS #type complete TITLE DNA-binding protein - human herpesvirus 1 (strain KOS1.1) ORGANISM #formal_name human herpesvirus 1 #note host Homo sapiens (man) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS A28601 REFERENCE A28601 !$#authors Gao, M.; Bouchey, J.; Curtin, K.; Knipe, D.M. !$#journal Virology (1988) 163:319-329 !$#title Genetic identification of a portion of the herpes simplex !1virus ICP8 protein required for DNA-binding. !$#cross-references MUID:88179536; PMID:2833010 !$#accession A28601 !'##molecule_type DNA !'##residues 1-1196 ##label GAO !'##cross-references GB:M20165; NID:g330120; PIDN:AAA45793.1; !1PID:g330121 GENETICS !$#map_position 0.38-0.409 CLASSIFICATION #superfamily herpesvirus DNA-binding protein KEYWORDS DNA binding SUMMARY #length 1196 #molecular-weight 128314 #checksum 3356 SEQUENCE /// ENTRY DNBEHF #type complete TITLE DNA-binding protein - human herpesvirus 1 (strain F) ORGANISM #formal_name human herpesvirus 1 #note host Homo sapiens (man) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 07-Jun-1996 ACCESSIONS D29242 REFERENCE A94381 !$#authors Hammerschmidt, W.; Conraths, F.; Mankertz, J.; Pauli, G.; !1Ludwig, H.; Buhk, H.J. !$#journal Virology (1988) 165:388-405 !$#title Conservation of a gene cluster including glycoprotein B in !1bovine herpesvirus type 2 (BHV-2) and herpes simplex virus !1type 1 (HSV-1). !$#cross-references MUID:88306231; PMID:2841793 !$#accession D29242 !'##molecule_type DNA !'##residues 1-1196 ##label HAM !'##cross-references GB:M21629 CLASSIFICATION #superfamily herpesvirus DNA-binding protein KEYWORDS DNA binding SUMMARY #length 1196 #molecular-weight 128373 #checksum 4846 SEQUENCE /// ENTRY A48350 #type complete TITLE DNA-binding protein - human herpesvirus 2 ORGANISM #formal_name human herpesvirus 2 #note host Homo sapiens (man) DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 31-May-1996 ACCESSIONS A48350 REFERENCE A48350 !$#authors Toh, Y.; Liu, Y.; Tanaka, S.; Mori, R. !$#journal Arch. Virol. (1993) 129:183-196 !$#title Nucleotide sequence of the major DNA-binding protein gene of !1herpes simplex virus type 2 and a comparison with the type !11. !$#cross-references MUID:93228441; PMID:8385914 !$#accession A48350 !'##molecule_type DNA !'##residues 1-1197 ##label TOH !'##note sequence extracted from NCBI backbone (NCBIN:129069, !1NCBIP:129070) GENETICS !$#map_position 0.375-0.405 CLASSIFICATION #superfamily herpesvirus DNA-binding protein KEYWORDS DNA binding; zinc finger FEATURE !$499-512 #region zinc finger SUMMARY #length 1197 #molecular-weight 128459 #checksum 565 SEQUENCE /// ENTRY DNBEBG #type complete TITLE DNA-binding protein - bovine herpesvirus 2 (strain BMV) ORGANISM #formal_name bovine herpesvirus 2 DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 07-Jun-1996 ACCESSIONS A29242 REFERENCE A94381 !$#authors Hammerschmidt, W.; Conraths, F.; Mankertz, J.; Pauli, G.; !1Ludwig, H.; Buhk, H.J. !$#journal Virology (1988) 165:388-405 !$#title Conservation of a gene cluster including glycoprotein B in !1bovine herpesvirus type 2 (BHV-2) and herpes simplex virus !1type 1 (HSV-1). !$#cross-references MUID:88306231; PMID:2841793 !$#accession A29242 !'##molecule_type DNA !'##residues 1-1186 ##label HAM !'##cross-references GB:M21628 CLASSIFICATION #superfamily herpesvirus DNA-binding protein KEYWORDS DNA binding SUMMARY #length 1186 #molecular-weight 127286 #checksum 6435 SEQUENCE /// ENTRY DNBE29 #type complete TITLE DNA-binding protein - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS C27214 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession C27214 !'##molecule_type DNA !'##residues 1-1204 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27912.1; !1PID:g60018 GENETICS !$#gene 29 CLASSIFICATION #superfamily herpesvirus DNA-binding protein KEYWORDS DNA binding SUMMARY #length 1204 #molecular-weight 132139 #checksum 7611 SEQUENCE /// ENTRY DNBEC4 #type complete TITLE DNA-binding protein - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS E36798 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession E36798 !'##molecule_type DNA !'##residues 1-1209 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02466.1; !1PID:g330823 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 31 CLASSIFICATION #superfamily herpesvirus DNA-binding protein KEYWORDS DNA binding SUMMARY #length 1209 #molecular-weight 129982 #checksum 7276 SEQUENCE /// ENTRY QQBEW4 #type complete TITLE DNA-binding protein - human cytomegalovirus (strain AD169) ALTERNATE_NAMES UL57 protein ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 #note host Homo sapiens (man) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS S09820 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09820 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1235 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35372.1; !1PID:g1780835 !'##note possible protein-coding frames are given !'##note the DNA sequence was submitted to EMBL, December 1989, in !1computer-readable form CLASSIFICATION #superfamily herpesvirus DNA-binding protein KEYWORDS DNA binding SUMMARY #length 1235 #molecular-weight 133878 #checksum 5786 SEQUENCE /// ENTRY A44051 #type complete TITLE DNA-binding protein - murine cytomegalovirus (strain Smith) ORGANISM #formal_name murine cytomegalovirus, murine herpesvirus 1 DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS A44051; S23218 REFERENCE A44051 !$#authors Messerle, M.; Keil, G.M.; Schneider, K.; Koszinowski, U.H. !$#journal Virology (1992) 191:355-367 !$#title Characterization of the murine cytomegalovirus genes !1encoding the major DNA binding protein and the ICP18.5 !1homolog. !$#cross-references MUID:93033129; PMID:1329325 !$#accession A44051 !'##molecule_type DNA !'##residues 1-1191 ##label MES !'##cross-references GB:X67021; NID:g60534; PIDN:CAA47414.1; PID:g60535 !'##experimental_source ATCC VR-194 CLASSIFICATION #superfamily herpesvirus DNA-binding protein KEYWORDS DNA binding; zinc finger FEATURE !$473-484 #region zinc finger SUMMARY #length 1191 #molecular-weight 131639 #checksum 6727 SEQUENCE /// ENTRY QQBE47 #type complete TITLE DNA-binding protein - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS A43045; A03791; S33057 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession A43045 !'##molecule_type DNA !'##residues 1-1128 ##label BAN !'##cross-references EMBL:V01555; NID:g59074; PIDN:CAA24808.1; !1PID:g1334916 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region CLASSIFICATION #superfamily herpesvirus DNA-binding protein KEYWORDS DNA binding SUMMARY #length 1128 #molecular-weight 123121 #checksum 7865 SEQUENCE /// ENTRY DNBEM1 #type complete TITLE DNA-binding protein - saimiriine herpesvirus 1 (strain 11) ORGANISM #formal_name saimiriine herpesvirus 1 #note host Saimiri sciureus (common squirrel monkey) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS G36806 REFERENCE A36806 !$#authors Albrecht, J. !$#submission submitted to the EMBL Data Library, January 1992 !$#description Primary structure of the herpesvirus saimiri genome. !$#accession G36806 !'##molecule_type DNA !'##residues 1-1128 ##label ALB !'##cross-references GB:X64346; NID:g60320; PIDN:CAA45629.1; PID:g60327 REFERENCE A37309 !$#authors Albrecht, J.C.; Nicholas, J.; Biller, D.; Cameron, K.R.; !1Biesinger, B.; Newman, C.; Wittmann, S.; Craxton, M.A.; !1Coleman, H.; Fleckenstein, B.; Honess, R.W. !$#journal J. Virol. (1992) 66:5047-5058 !$#title Primary structure of the herpesvirus saimiri genome. !$#cross-references MUID:92333688; PMID:1321287 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 6 CLASSIFICATION #superfamily herpesvirus DNA-binding protein KEYWORDS DNA binding SUMMARY #length 1128 #molecular-weight 127457 #checksum 3206 SEQUENCE /// ENTRY QQBE48 #type complete TITLE BARF1 protein - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS B43045; A03792; S33058 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession B43045 !'##molecule_type DNA !'##residues 1-221 ##label BAN !'##cross-references EMBL:V01555; NID:g59074; PIDN:CAA24809.1; !1PID:g1334917 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region CLASSIFICATION #superfamily human herpesvirus 4 BARF1 protein SUMMARY #length 221 #molecular-weight 24471 #checksum 8613 SEQUENCE /// ENTRY QQBE49 #type complete TITLE BALF1 protein - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS C43045; A03793; S33059 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession C43045 !'##molecule_type DNA !'##residues 1-220 ##label BAN !'##cross-references EMBL:V01555; NID:g59074; PIDN:CAA24810.1; !1PID:g1334918 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region CLASSIFICATION #superfamily human herpesvirus 4 BALF1 protein SUMMARY #length 220 #molecular-weight 25148 #checksum 8062 SEQUENCE /// ENTRY QQBE50 #type complete TITLE latent membrane protein - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Feb-1997 ACCESSIONS D43045; A03794 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession D43045 !'##molecule_type DNA !'##residues 1-386 ##label BAN REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region CLASSIFICATION #superfamily Epstein-Barr virus latent membrane protein KEYWORDS transmembrane protein SUMMARY #length 386 #molecular-weight 41982 #checksum 6693 SEQUENCE /// ENTRY LABERJ #type complete TITLE latent membrane protein - human herpesvirus 4 (strain Raji) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus #note host Homo sapiens (man) DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Jul-1999 ACCESSIONS C28918 REFERENCE A28918 !$#authors Hatfull, G.; Bankier, A.T.; Barrell, B.G.; Farrell, P.J. !$#journal Virology (1988) 164:334-340 !$#title Sequence analysis of Raji Epstein-Barr virus DNA. !$#cross-references MUID:88219520; PMID:2835854 !$#accession C28918 !'##molecule_type DNA !'##residues 1-386 ##label HAT !'##cross-references GB:M20868; NID:g330380; PIDN:AAA66532.1; !1PID:g330381 GENETICS !$#introns 90/1; 118/3 CLASSIFICATION #superfamily Epstein-Barr virus latent membrane protein KEYWORDS membrane protein SUMMARY #length 386 #molecular-weight 42061 #checksum 8042 SEQUENCE /// ENTRY LABECA #type complete TITLE latent membrane protein LMP1 - human herpesvirus 4 (strain CAO) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS JQ1434; G00065; S21660 REFERENCE JQ1434 !$#authors Hu, L.F.; Zabarovsky, E.R.; Chen, F.; Cao, S.L.; Ernberg, !1I.; Klein, G.; Winberg, G. !$#journal J. Gen. Virol. (1991) 72:2399-2409 !$#title Isolation and sequencing of the Epstein-Barr virus BNLF-1 !1gene (LMP1) from a Chinese nasopharyngeal carcinoma. !$#cross-references MUID:92013956; PMID:1681026 !$#accession JQ1434 !'##molecule_type DNA !'##residues 1-404 ##label HUL !'##cross-references EMBL:X58140; NID:g22937; PIDN:CAA41148.1; !1PID:g22938 !'##note the authors translated the codon AAA for residue 358 as Ala !'##note warning: the organism was shown incorrectly as Homo sapiens in !1GenBank accession X58140, release 100.0 COMMENT Unlike Epstein-Barr nuclear antigen 1 (EBNA-1) (see !1PIR:S42440), which is expressed in all EBV-infected cells, !1this protein appears associated with transformation and is !1found in a majority of nasopharyngeal carcinoma tumor !1biopsies. GENETICS !$#gene LMP1; BNLF-1 !$#introns 90/1; 119/1 CLASSIFICATION #superfamily Epstein-Barr virus latent membrane protein KEYWORDS oncogene; tandem repeat; transmembrane protein FEATURE !$25-45 #domain transmembrane #status predicted #label TM1\ !$51-71 #domain transmembrane #status predicted #label TM2\ !$76-97 #domain transmembrane #status predicted #label TM3\ !$104-124 #domain transmembrane #status predicted #label TM4\ !$140-160 #domain transmembrane #status predicted #label TM5\ !$166-186 #domain transmembrane #status predicted #label TM6\ !$256-332 #region 11-residue repeats (P-D-N-T-D-D-N-G-P-Q-D) SUMMARY #length 404 #molecular-weight 43769 #checksum 7535 SEQUENCE /// ENTRY QQBE1R #type complete TITLE BXRF1 (EC-RF1) protein - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 16-Jul-1999 ACCESSIONS A03796; S33047 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession A03796 !'##molecule_type DNA !'##residues 1-248 ##label BAN !'##cross-references EMBL:V01555; NID:g59074; PIDN:CAA24798.1; !1PID:g1334906 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region CLASSIFICATION #superfamily varicella-zoster virus gene 35 protein SUMMARY #length 248 #molecular-weight 27062 #checksum 5780 SEQUENCE /// ENTRY WZBE35 #type complete TITLE gene 35 protein - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS I27214 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession I27214 !'##molecule_type DNA !'##residues 1-258 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27918.1; !1PID:g60024 GENETICS !$#gene 35 CLASSIFICATION #superfamily varicella-zoster virus gene 35 protein SUMMARY #length 258 #molecular-weight 28975 #checksum 507 SEQUENCE /// ENTRY WMBEW4 #type complete TITLE UL24 protein - human herpesvirus 1 (strain 17) ORGANISM #formal_name human herpesvirus 1 DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jun-2000 ACCESSIONS F30084 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession F30084 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-269 ##label MCG !'##cross-references GB:X14112; NID:g1944536; PIDN:CAA32316.1; !1PID:g59523; GB:D00317 GENETICS !$#gene UL24 CLASSIFICATION #superfamily varicella-zoster virus gene 35 protein SUMMARY #length 269 #molecular-weight 29476 #checksum 4138 SEQUENCE /// ENTRY WZBED1 #type complete TITLE gene 37 protein - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS C36799 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession C36799 !'##molecule_type DNA !'##residues 1-272 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02473.1; !1PID:g330830 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 37 CLASSIFICATION #superfamily varicella-zoster virus gene 35 protein SUMMARY #length 272 #molecular-weight 29188 #checksum 3404 SEQUENCE /// ENTRY C43675 #type complete TITLE 32K protein - infectious laryngotracheitis virus (strain Thorne) ORGANISM #formal_name infectious laryngotracheitis virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jun-2000 ACCESSIONS C43675 REFERENCE A43675 !$#authors Griffin, A.M.; Boursnell, M.E.G. !$#journal J. Gen. Virol. (1990) 71:841-850 !$#title Analysis of the nucleotide sequence of DNA from the region !1of the thymidine kinase gene of infectious laryngotracheitis !1virus; potential evolutionary relationships between the !1herpesvirus subfamilies. !$#cross-references MUID:90218031; PMID:2157797 !$#accession C43675 !'##molecule_type DNA !'##residues 1-287 ##label GRI !'##cross-references GB:D00565; NID:g221899; PIDN:BAA00441.1; !1PID:g221902 CLASSIFICATION #superfamily varicella-zoster virus gene 35 protein SUMMARY #length 287 #molecular-weight 32149 #checksum 3783 SEQUENCE /// ENTRY QQBEB4 #type complete TITLE UL76 protein - human cytomegalovirus (strain AD169) ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 #note host Homo sapiens (man) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS S09839 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09839 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-325 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35391.1; !1PID:g1780853 !'##note possible protein-coding frames are given !'##note the DNA sequence was submitted to EMBL, December 1989, in !1computer-readable form CLASSIFICATION #superfamily varicella-zoster virus gene 35 protein SUMMARY #length 325 #molecular-weight 36069 #checksum 6779 SEQUENCE /// ENTRY WZBEM6 #type complete TITLE gene 20 protein - saimiriine herpesvirus 1 (strain 11) ORGANISM #formal_name saimiriine herpesvirus 1 #note host Saimiri sciureus (common squirrel monkey) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS B36808 REFERENCE A36806 !$#authors Albrecht, J. !$#submission submitted to the EMBL Data Library, January 1992 !$#description Primary structure of the herpesvirus saimiri genome. !$#accession B36808 !'##molecule_type DNA !'##residues 1-303 ##label ALB !'##cross-references GB:X64346; NID:g60320; PIDN:CAA45644.1; PID:g60342 REFERENCE A37309 !$#authors Albrecht, J.C.; Nicholas, J.; Biller, D.; Cameron, K.R.; !1Biesinger, B.; Newman, C.; Wittmann, S.; Craxton, M.A.; !1Coleman, H.; Fleckenstein, B.; Honess, R.W. !$#journal J. Virol. (1992) 66:5047-5058 !$#title Primary structure of the herpesvirus saimiri genome. !$#cross-references MUID:92333688; PMID:1321287 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 20 CLASSIFICATION #superfamily varicella-zoster virus gene 35 protein SUMMARY #length 303 #molecular-weight 34942 #checksum 8863 SEQUENCE /// ENTRY QQBE2R #type complete TITLE BVRF1 (EC-RF2) protein - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 16-Jul-1999 ACCESSIONS A03797; S04559 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession A03797 !'##molecule_type DNA !'##residues 1-570 ##label BAN !'##cross-references GB:V01555; GB:J02070; GB:K01729; GB:K01730; !1GB:V01554; GB:X00498; GB:X00499; GB:X00784; NID:g59074; !1PIDN:CAA24800.1; PID:g1334908 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region REFERENCE S00735 !$#authors Walls, D.; Perricaudet, M.; Gannon, F. !$#journal Nucleic Acids Res. (1988) 16:2859-2872 !$#title The analysis of EBV proteins which are antigenic in vivo. !$#cross-references MUID:88217505; PMID:2835748 !$#accession S04559 !'##molecule_type DNA !'##residues 426-446 ##label WAL !'##cross-references EMBL:X07531 CLASSIFICATION #superfamily varicella-zoster virus gene 34 protein KEYWORDS membrane protein; surface antigen SUMMARY #length 570 #molecular-weight 62460 #checksum 4406 SEQUENCE /// ENTRY WZBE34 #type complete TITLE gene 34 protein - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS H27214 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession H27214 !'##molecule_type DNA !'##residues 1-579 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27917.1; !1PID:g60023 GENETICS !$#gene 34 CLASSIFICATION #superfamily varicella-zoster virus gene 34 protein SUMMARY #length 579 #molecular-weight 65185 #checksum 9134 SEQUENCE /// ENTRY B43675 #type complete TITLE 64K protein - infectious laryngotracheitis virus (strain Thorne) ORGANISM #formal_name infectious laryngotracheitis virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jun-2000 ACCESSIONS B43675 REFERENCE A43675 !$#authors Griffin, A.M.; Boursnell, M.E.G. !$#journal J. Gen. Virol. (1990) 71:841-850 !$#title Analysis of the nucleotide sequence of DNA from the region !1of the thymidine kinase gene of infectious laryngotracheitis !1virus; potential evolutionary relationships between the !1herpesvirus subfamilies. !$#cross-references MUID:90218031; PMID:2157797 !$#accession B43675 !'##molecule_type DNA !'##residues 1-572 ##label GRI !'##cross-references GB:D00565; NID:g221899; PIDN:BAA00440.1; !1PID:g221901 CLASSIFICATION #superfamily varicella-zoster virus gene 34 protein SUMMARY #length 572 #molecular-weight 64110 #checksum 9265 SEQUENCE /// ENTRY WMBEW5 #type complete TITLE UL25 protein - human herpesvirus 1 (strain 17) ORGANISM #formal_name human herpesvirus 1 DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jun-2000 ACCESSIONS G30084 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession G30084 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-580 ##label MCG !'##cross-references GB:X14112; NID:g1944536; PIDN:CAA32317.1; !1PID:g59525; GB:D00317 GENETICS !$#gene UL25 CLASSIFICATION #superfamily varicella-zoster virus gene 34 protein SUMMARY #length 580 #molecular-weight 62669 #checksum 4594 SEQUENCE /// ENTRY WZBEC9 #type complete TITLE gene 36 protein - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS B36799 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession B36799 !'##molecule_type DNA !'##residues 1-587 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02472.1; !1PID:g330829 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 36 CLASSIFICATION #superfamily varicella-zoster virus gene 34 protein SUMMARY #length 587 #molecular-weight 63691 #checksum 2693 SEQUENCE /// ENTRY QQBEB5 #type complete TITLE UL77 protein - human cytomegalovirus (strain AD169) ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 #note host Homo sapiens (man) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS S09840 REFERENCE S09749 !$#authors Chee, M.S.; Bankier, A.T.; Beck, S.; Bohni, R.; Brown, C.M.; !1Cerny, R.; Horsnell, T.; Hutchison III, C.A.; Kouzarides, !1T.; Martignetti, J.A.; Preddie, E.; Satchwell, S.C.; !1Tomlinson, P.; Weston, K.M.; Barrell, B.G. !$#journal Curr. Top. Microbiol. Immunol. (1990) 154:125-169 !$#title Analysis of the protein-coding content of the sequence of !1human cytomegalovirus strain AD169. !$#cross-references MUID:90269039; PMID:2161319 !$#accession S09840 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-642 ##label CHE !'##cross-references EMBL:X17403; NID:g59591; PIDN:CAA35392.1; !1PID:g1780854 !'##note possible protein-coding frames are given !'##note the DNA sequence was submitted to EMBL, December 1989, in !1computer-readable form CLASSIFICATION #superfamily varicella-zoster virus gene 34 protein SUMMARY #length 642 #molecular-weight 71186 #checksum 1613 SEQUENCE /// ENTRY WZBEM5 #type complete TITLE gene 19 protein - saimiriine herpesvirus 1 (strain 11) ORGANISM #formal_name saimiriine herpesvirus 1 #note host Saimiri sciureus (common squirrel monkey) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS A36808 REFERENCE A36806 !$#authors Albrecht, J. !$#submission submitted to the EMBL Data Library, January 1992 !$#description Primary structure of the herpesvirus saimiri genome. !$#accession A36808 !'##molecule_type DNA !'##residues 1-543 ##label ALB !'##cross-references GB:X64346; NID:g60320; PIDN:CAA45642.1; PID:g60340 REFERENCE A37309 !$#authors Albrecht, J.C.; Nicholas, J.; Biller, D.; Cameron, K.R.; !1Biesinger, B.; Newman, C.; Wittmann, S.; Craxton, M.A.; !1Coleman, H.; Fleckenstein, B.; Honess, R.W. !$#journal J. Virol. (1992) 66:5047-5058 !$#title Primary structure of the herpesvirus saimiri genome. !$#cross-references MUID:92333688; PMID:1321287 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 19 CLASSIFICATION #superfamily varicella-zoster virus gene 34 protein SUMMARY #length 543 #molecular-weight 61484 #checksum 3936 SEQUENCE /// ENTRY QQBE3R #type complete TITLE BVRF2 (EC-RF3) protein - human herpesvirus 4 (strain B95-8) CONTAINS BVRF2 (EC-RF3a) protein ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 16-Jul-1999 ACCESSIONS A03798; S33049; S33050; S33051 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession A03798 !'##molecule_type DNA !'##residues 1-605 ##label BAN !'##cross-references EMBL:V01555; NID:g59074; PIDN:CAA24801.1; !1PID:g1334909 REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region CLASSIFICATION #superfamily varicella-zoster virus gene 33 protein FEATURE !$261-605 #product BVRF2 (EC-RF3a) protein #status predicted !8#label BVR SUMMARY #length 605 #molecular-weight 64101 #checksum 3254 SEQUENCE /// ENTRY WZBE33 #type complete TITLE gene 33 protein - human herpesvirus 3 ORGANISM #formal_name human herpesvirus 3, varicella-zoster virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS G27214 REFERENCE A27345 !$#authors Davison, A.J.; Scott, J.E. !$#journal J. Gen. Virol. (1986) 67:1759-1816 !$#title The complete DNA sequence of varicella-zoster virus. !$#cross-references MUID:86306657; PMID:3018124 !$#accession G27214 !'##molecule_type DNA !'##residues 1-605 ##label DAV !'##cross-references EMBL:X04370; NID:g59989; PIDN:CAA27916.1; !1PID:g60022 GENETICS !$#gene 33 CLASSIFICATION #superfamily varicella-zoster virus gene 33 protein SUMMARY #length 605 #molecular-weight 66046 #checksum 8450 SEQUENCE /// ENTRY WMBEW6 #type complete TITLE capsid protein - human herpesvirus 1 (strain 17) ORGANISM #formal_name human herpesvirus 1 DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jun-2000 ACCESSIONS H30084 REFERENCE A30083 !$#authors McGeoch, D.J.; Dalrymple, M.A.; Davison, A.J.; Dolan, A.; !1Frame, M.C.; McNab, D.; Perry, L.J.; Scott, J.E.; Taylor, P. !$#journal J. Gen. Virol. (1988) 69:1531-1574 !$#title The complete DNA sequence of the long unique region in the !1genome of herpes simplex virus type 1. !$#cross-references MUID:88274327; PMID:2839594 !$#accession H30084 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-635 ##label MCG !'##cross-references GB:X14112; NID:g1944536; PIDN:CAA32318.1; !1PID:g59526; GB:D00317 GENETICS !$#gene UL26 CLASSIFICATION #superfamily varicella-zoster virus gene 33 protein KEYWORDS capsid protein SUMMARY #length 635 #molecular-weight 66470 #checksum 411 SEQUENCE /// ENTRY A43675 #type complete TITLE capsid protein p40 - infectious laryngotracheitis virus ORGANISM #formal_name infectious laryngotracheitis virus DATE 30-Sep-1993 #sequence_revision 22-Oct-1999 #text_change 16-Jun-2000 ACCESSIONS S13444; A43675 REFERENCE S13444 !$#authors Griffin, A.M. !$#journal Nucleic Acids Res. (1990) 18:3664 !$#title The complete sequence of the capsid p40 gene from infectious !1laryngotracheitis virus. !$#cross-references MUID:90301509; PMID:2163526 !$#accession S13444 !'##status preliminary !'##molecule_type DNA !'##residues 1-586 ##label NUC !'##cross-references GB:D00565; NID:g221899; PIDN:BAA00439.1; !1PID:g221900 REFERENCE A43675 !$#authors Griffin, A.M.; Boursnell, M.E.G. !$#journal J. Gen. Virol. (1990) 71:841-850 !$#title Analysis of the nucleotide sequence of DNA from the region !1of the thymidine kinase gene of infectious laryngotracheitis !1virus; potential evolutionary relationships between the !1herpesvirus subfamilies. !$#cross-references MUID:90218031; PMID:2157797 !$#accession A43675 !'##molecule_type DNA !'##residues 1-516,'EF' ##label GRI !'##cross-references GB:D00565 !'##experimental_source strain Thorne CLASSIFICATION #superfamily varicella-zoster virus gene 33 protein KEYWORDS capsid protein SUMMARY #length 586 #molecular-weight 65335 #checksum 6645 SEQUENCE /// ENTRY WZBEC8 #type complete TITLE 68.6K capsid protein - equine herpesvirus 1 (strain Ab4p) ORGANISM #formal_name equine herpesvirus 1 #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS I36798 REFERENCE A36805 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#submission submitted to GenBank, March 1992 !$#description The DNA sequence of equine herpesvirus-1. !$#accession I36798 !'##molecule_type DNA !'##residues 1-646 ##label TEL !'##cross-references GB:M86664; NID:g330791; PIDN:AAB02470.1; !1PID:g330827 REFERENCE A41831 !$#authors Telford, E.A.R.; Watson, M.S.; McBride, K.; Davison, A.J. !$#journal Virology (1992) 189:304-316 !$#title The DNA sequence of equine herpesvirus-1. !$#cross-references MUID:92295566; PMID:1318606 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 35 CLASSIFICATION #superfamily varicella-zoster virus gene 33 protein KEYWORDS capsid protein SUMMARY #length 646 #molecular-weight 68579 #checksum 1850 SEQUENCE /// ENTRY WZBEM4 #type complete TITLE gene 17 protein - saimiriine herpesvirus 1 (strain 11) ORGANISM #formal_name saimiriine herpesvirus 1 #note host Saimiri sciureus (common squirrel monkey) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS H36807 REFERENCE A36806 !$#authors Albrecht, J. !$#submission submitted to the EMBL Data Library, January 1992 !$#description Primary structure of the herpesvirus saimiri genome. !$#accession H36807 !'##molecule_type DNA !'##residues 1-475 ##label ALB !'##cross-references GB:X64346; NID:g60320; PIDN:CAA45641.1; PID:g60339 REFERENCE A37309 !$#authors Albrecht, J.C.; Nicholas, J.; Biller, D.; Cameron, K.R.; !1Biesinger, B.; Newman, C.; Wittmann, S.; Craxton, M.A.; !1Coleman, H.; Fleckenstein, B.; Honess, R.W. !$#journal J. Virol. (1992) 66:5047-5058 !$#title Primary structure of the herpesvirus saimiri genome. !$#cross-references MUID:92333688; PMID:1321287 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 17 CLASSIFICATION #superfamily varicella-zoster virus gene 33 protein SUMMARY #length 475 #molecular-weight 52820 #checksum 3991 SEQUENCE /// ENTRY QQBE4R #type complete TITLE EC-RF4 protein - human herpesvirus 4 (strain B95-8) ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 23-Aug-1997 ACCESSIONS A03799 REFERENCE A93065 !$#authors Bankier, A.T.; Deininger, P.L.; Farrell, P.J.; Barrell, B.G. !$#journal Mol. Biol. Med. (1983) 1:21-45 !$#title Sequence analysis of the 17,166 bp EcoRI fragment C of B95-8 !1Epstein-Barr virus. !$#cross-references MUID:85035713; PMID:6092825 !$#accession A03799 !'##molecule_type DNA !'##residues 1-289 ##label BAN REFERENCE A03794 !$#authors Baer, R.; Bankier, A.T.; Biggin, M.D.; Deininger, P.L.; !1Farrell, P.J.; Gibson, T.J.; Hatfull, G.; Hudson, G.S.; !1Satchwell, S.C.; Seguin, C.; Tuffnell, P.S.; Barrell, B.G. !$#journal Nature (1984) 310:207-211 !$#title DNA sequence and expression of the B95-8 Epstein-Barr virus !1genome. !$#cross-references MUID:84270667; PMID:6087149 !$#contents annotation; protein coding region CLASSIFICATION #superfamily human herpesvirus 4 EC-RF4 protein SUMMARY #length 289 #molecular-weight 29810 #checksum 4533 SEQUENCE /// ENTRY WMBELM #type complete TITLE membrane protein LMP-2A - human herpesvirus 4 CONTAINS membrane protein LMP-2B ORGANISM #formal_name human herpesvirus 4, Epstein-Barr virus #note host Homo sapiens (man) DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jul-1999 ACCESSIONS A30178; B30178; S00392 REFERENCE A30178 !$#authors Sample, J.; Liebowitz, D.; Kieff, E. !$#journal J. Virol. (1989) 63:933-937 !$#title Two related Epstein-Barr virus membrane proteins are encoded !1by separate genes. !$#cross-references MUID:89095024; PMID:2536113 !$#accession A30178 !'##molecule_type mRNA !'##residues 1-497 ##label SAM !'##cross-references GB:M24212; NID:g522186; PIDN:AAA45887.1; !1PID:g522187 !$#accession B30178 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 120-497 ##label SA2 REFERENCE S00392 !$#authors Laux, G.; Perricaudet, M.; Farrell, P.J. !$#journal EMBO J. (1988) 7:769-774 !$#title A spliced Epstein-Barr virus gene expressed in immortalized !1lymphocytes is created by circularization of the linear !1viral genome. !$#cross-references MUID:88283646; PMID:2840285 !$#accession S00392 !'##molecule_type mRNA !'##residues 1-497 ##label LAU !'##cross-references EMBL:Y00835; NID:g59183; PIDN:CAA68762.1; !1PID:g59184 GENETICS !$#gene terminal !$#introns 140/2; 212/1; 245/1; 328/1; 355/1; 412/1; 484/1 CLASSIFICATION #superfamily Epstein-Barr virus membrane protein LMP-2A KEYWORDS glycoprotein; transmembrane protein FEATURE !$120-497 #product membrane protein LMP-2B #status predicted !8#label LMB\ !$122-141 #domain transmembrane #status predicted #label TMA\ !$150-168 #domain transmembrane #status predicted #label TMB\ !$178-198 #domain transmembrane #status predicted #label TMC\ !$208-235 #domain transmembrane #status predicted #label TMD\ !$242-259 #domain transmembrane #status predicted #label TME\ !$267-288 #domain transmembrane #status predicted #label TMF\ !$300-316 #domain transmembrane #status predicted #label TMG\ !$321-339 #domain transmembrane #status predicted #label TMH\ !$355-373 #domain transmembrane #status predicted #label TMI\ !$392-411 #domain transmembrane #status predicted #label TMJ\ !$419-443 #domain transmembrane #status predicted #label TMK\ !$450-470 #domain transmembrane #status predicted #label TML\ !$27,320,417 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 497 #molecular-weight 53011 #checksum 38 SEQUENCE /// ENTRY QQBE8H #type complete TITLE hypothetical 13K protein (transforming region) - human cytomegalovirus (strain AD169) ORGANISM #formal_name human cytomegalovirus, human herpesvirus 5 DATE 20-Sep-1984 #sequence_revision 20-Sep-1984 #text_change 17-Jul-1998 ACCESSIONS A03800 REFERENCE A03800 !$#authors Nelson, J.A.; Fleckenstein, B.; Jahn, G.; Galloway, D.A.; !1McDougall, J.K. !$#journal J. Virol. (1984) 49:109-115 !$#title Structure of the transforming region of human !1cytomegalovirus AD169. !$#cross-references MUID:84090384; PMID:6317885 !$#accession A03800 !'##molecule_type DNA !'##residues 1-118 ##label NEL CLASSIFICATION #superfamily human cytomegalovirus hypothetical 13K protein SUMMARY #length 118 #molecular-weight 13412 #checksum 5271 SEQUENCE /// ENTRY JVBEIV #type complete TITLE DNA-packaging protein - ictalurid herpesvirus 1 (strain auburn 1) ALTERNATE_NAMES terminase ORGANISM #formal_name ictalurid herpesvirus 1 #note host Ictalurus punctatus (channel catfish) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS A36786 REFERENCE A36804 !$#authors Davison, A.J. !$#submission submitted to GenBank, January 1992 !$#description Channel catfish virus: a new type of herpesvirus. !$#accession A36786 !'##molecule_type DNA !'##residues 1-852 ##label DAV !'##cross-references GB:M75136; NID:g331209; PIDN:AAA88166.1; !1PID:g331210 REFERENCE A39447 !$#authors Davison, A.J. !$#journal Virology (1992) 186:9-14 !$#title Channel catfish virus: a new type of herpesvirus. !$#cross-references MUID:92087490; PMID:1727613 !$#contents annotation !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 62 !$#introns 401/3; 587/3 CLASSIFICATION #superfamily ictalurid herpesvirus DNA packaging protein KEYWORDS DNA packaging SUMMARY #length 852 #molecular-weight 95127 #checksum 8882 SEQUENCE /// ENTRY MMBEI1 #type complete TITLE 14.6K membrane protein - ictalurid herpesvirus 1 (strain auburn 1) ORGANISM #formal_name ictalurid herpesvirus 1 #note host Ictalurus punctatus (channel catfish) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS G36786 REFERENCE A36804 !$#authors Davison, A.J. !$#submission submitted to GenBank, January 1992 !$#description Channel catfish virus: a new type of herpesvirus. !$#accession G36786 !'##molecule_type DNA !'##residues 1-138 ##label DAV !'##cross-references GB:M75136; NID:g331209; PIDN:AAA88109.1; !1PID:g331216 REFERENCE A39447 !$#authors Davison, A.J. !$#journal Virology (1992) 186:9-14 !$#title Channel catfish virus: a new type of herpesvirus. !$#cross-references MUID:92087490; PMID:1727613 !$#contents annotation !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 6 CLASSIFICATION #superfamily ictalurid herpesvirus 14.6K membrane protein KEYWORDS transmembrane protein FEATURE !$4-20 #domain transmembrane #status predicted #label TM1\ !$37-53 #domain transmembrane #status predicted #label TM2 SUMMARY #length 138 #molecular-weight 14648 #checksum 6371 SEQUENCE /// ENTRY MMBEI2 #type complete TITLE 15.6K membrane protein - ictalurid herpesvirus 1 (strain auburn 1) ORGANISM #formal_name ictalurid herpesvirus 1 #note host Ictalurus punctatus (channel catfish) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS H36786 REFERENCE A36804 !$#authors Davison, A.J. !$#submission submitted to GenBank, January 1992 !$#description Channel catfish virus: a new type of herpesvirus. !$#accession H36786 !'##molecule_type DNA !'##residues 1-140 ##label DAV !'##cross-references GB:M75136; NID:g331209; PIDN:AAA88110.1; !1PID:g331217 REFERENCE A39447 !$#authors Davison, A.J. !$#journal Virology (1992) 186:9-14 !$#title Channel catfish virus: a new type of herpesvirus. !$#cross-references MUID:92087490; PMID:1727613 !$#contents annotation !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 7 CLASSIFICATION #superfamily ictalurid herpesvirus 15.6K membrane protein KEYWORDS transmembrane protein FEATURE !$44-60 #domain transmembrane #status predicted #label TMN SUMMARY #length 140 #molecular-weight 15615 #checksum 7690 SEQUENCE /// ENTRY MMBEI3 #type complete TITLE 25.5K membrane protein - ictalurid herpesvirus 1 (strain auburn 1) ORGANISM #formal_name ictalurid herpesvirus 1 #note host Ictalurus punctatus (channel catfish) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS I36786 REFERENCE A36804 !$#authors Davison, A.J. !$#submission submitted to GenBank, January 1992 !$#description Channel catfish virus: a new type of herpesvirus. !$#accession I36786 !'##molecule_type DNA !'##residues 1-232 ##label DAV !'##cross-references GB:M75136; NID:g331209; PIDN:AAA88111.1; !1PID:g331218 REFERENCE A39447 !$#authors Davison, A.J. !$#journal Virology (1992) 186:9-14 !$#title Channel catfish virus: a new type of herpesvirus. !$#cross-references MUID:92087490; PMID:1727613 !$#contents annotation !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 8 CLASSIFICATION #superfamily ictalurid herpesvirus 25.5K membrane protein KEYWORDS transmembrane protein FEATURE !$166-182 #domain transmembrane #status predicted #label TM1\ !$195-211 #domain transmembrane #status predicted #label TM2 SUMMARY #length 232 #molecular-weight 25466 #checksum 8650 SEQUENCE /// ENTRY MMBEI4 #type complete TITLE 15.9K membrane protein - ictalurid herpesvirus 1 (strain auburn 1) ORGANISM #formal_name ictalurid herpesvirus 1 #note host Ictalurus punctatus (channel catfish) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS B36787 REFERENCE A36804 !$#authors Davison, A.J. !$#submission submitted to GenBank, January 1992 !$#description Channel catfish virus: a new type of herpesvirus. !$#accession B36787 !'##molecule_type DNA !'##residues 1-151 ##label DAV !'##cross-references GB:M75136; NID:g331209; PIDN:AAA88113.1; !1PID:g331220 REFERENCE A39447 !$#authors Davison, A.J. !$#journal Virology (1992) 186:9-14 !$#title Channel catfish virus: a new type of herpesvirus. !$#cross-references MUID:92087490; PMID:1727613 !$#contents annotation !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 10 CLASSIFICATION #superfamily ictalurid herpesvirus 15.9K membrane protein KEYWORDS transmembrane protein FEATURE !$7-23 #domain transmembrane #status predicted #label TM1\ !$107-123 #domain transmembrane #status predicted #label TM2 SUMMARY #length 151 #molecular-weight 15933 #checksum 3825 SEQUENCE /// ENTRY MMBEI5 #type complete TITLE 23.2K membrane protein - ictalurid herpesvirus 1 (strain auburn 1) ORGANISM #formal_name ictalurid herpesvirus 1 #note host Ictalurus punctatus (channel catfish) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS B36788 REFERENCE A36804 !$#authors Davison, A.J. !$#submission submitted to GenBank, January 1992 !$#description Channel catfish virus: a new type of herpesvirus. !$#accession B36788 !'##molecule_type DNA !'##residues 1-204 ##label DAV !'##cross-references GB:M75136; NID:g331209; PIDN:AAA88122.1; !1PID:g331229 REFERENCE A39447 !$#authors Davison, A.J. !$#journal Virology (1992) 186:9-14 !$#title Channel catfish virus: a new type of herpesvirus. !$#cross-references MUID:92087490; PMID:1727613 !$#contents annotation !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 19 CLASSIFICATION #superfamily ictalurid herpesvirus 23.2K membrane protein KEYWORDS transmembrane protein FEATURE !$4-22 #domain transmembrane #status predicted #label TM1\ !$90-106 #domain transmembrane #status predicted #label TM2 SUMMARY #length 204 #molecular-weight 23212 #checksum 5564 SEQUENCE /// ENTRY MMBEI6 #type complete TITLE 16.9K membrane protein - ictalurid herpesvirus 1 (strain auburn 1) ORGANISM #formal_name ictalurid herpesvirus 1 #note host Ictalurus punctatus (channel catfish) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS G36791 REFERENCE A36804 !$#authors Davison, A.J. !$#submission submitted to GenBank, January 1992 !$#description Channel catfish virus: a new type of herpesvirus. !$#accession G36791 !'##molecule_type DNA !'##residues 1-154 ##label DAV !'##cross-references GB:M75136; NID:g331209; PIDN:AAA88154.1; !1PID:g331261 REFERENCE A39447 !$#authors Davison, A.J. !$#journal Virology (1992) 186:9-14 !$#title Channel catfish virus: a new type of herpesvirus. !$#cross-references MUID:92087490; PMID:1727613 !$#contents annotation !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 51 CLASSIFICATION #superfamily ictalurid herpesvirus 16.9K membrane protein KEYWORDS transmembrane protein FEATURE !$5-23 #domain transmembrane #status predicted #label TM1\ !$34-50 #domain transmembrane #status predicted #label TM2\ !$88-107 #domain transmembrane #status predicted #label TM3 SUMMARY #length 154 #molecular-weight 16872 #checksum 7671 SEQUENCE /// ENTRY MMBEI7 #type complete TITLE 38.1K membrane protein - ictalurid herpesvirus 1 (strain auburn 1) ORGANISM #formal_name ictalurid herpesvirus 1 #note host Ictalurus punctatus (channel catfish) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS F36792 REFERENCE A36804 !$#authors Davison, A.J. !$#submission submitted to GenBank, January 1992 !$#description Channel catfish virus: a new type of herpesvirus. !$#accession F36792 !'##molecule_type DNA !'##residues 1-345 ##label DAV !'##cross-references GB:M75136; NID:g331209; PIDN:AAA88162.1; !1PID:g331269 REFERENCE A39447 !$#authors Davison, A.J. !$#journal Virology (1992) 186:9-14 !$#title Channel catfish virus: a new type of herpesvirus. !$#cross-references MUID:92087490; PMID:1727613 !$#contents annotation !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 59 CLASSIFICATION #superfamily ictalurid herpesvirus 38.1K membrane protein KEYWORDS transmembrane protein FEATURE !$46-63 #domain transmembrane #status predicted #label TM1\ !$101-118 #domain transmembrane #status predicted #label TM2\ !$147-165 #domain transmembrane #status predicted #label TM3\ !$265-286 #domain transmembrane #status predicted #label TM4 SUMMARY #length 345 #molecular-weight 38135 #checksum 227 SEQUENCE /// ENTRY ZBBEI1 #type complete TITLE 17K zinc-binding protein - ictalurid herpesvirus 1 (strain auburn 1) ORGANISM #formal_name ictalurid herpesvirus 1 #note host Ictalurus punctatus (channel catfish) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS A36787 REFERENCE A36804 !$#authors Davison, A.J. !$#submission submitted to GenBank, January 1992 !$#description Channel catfish virus: a new type of herpesvirus. !$#accession A36787 !'##molecule_type DNA !'##residues 1-158 ##label DAV !'##cross-references GB:M75136; NID:g331209; PIDN:AAA88112.1; !1PID:g331219 REFERENCE A39447 !$#authors Davison, A.J. !$#journal Virology (1992) 186:9-14 !$#title Channel catfish virus: a new type of herpesvirus. !$#cross-references MUID:92087490; PMID:1727613 !$#contents annotation !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 9 CLASSIFICATION #superfamily ictalurid herpesvirus 17K zinc binding protein KEYWORDS zinc finger SUMMARY #length 158 #molecular-weight 17082 #checksum 2134 SEQUENCE /// ENTRY ZBBEI2 #type complete TITLE 30.2K zinc-binding protein - ictalurid herpesvirus 1 (strain auburn 1) ORGANISM #formal_name ictalurid herpesvirus 1 #note host Ictalurus punctatus (channel catfish) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS C36787 REFERENCE A36804 !$#authors Davison, A.J. !$#submission submitted to GenBank, January 1992 !$#description Channel catfish virus: a new type of herpesvirus. !$#accession C36787 !'##molecule_type DNA !'##residues 1-281 ##label DAV !'##cross-references GB:M75136; NID:g331209; PIDN:AAA88114.1; !1PID:g331221 REFERENCE A39447 !$#authors Davison, A.J. !$#journal Virology (1992) 186:9-14 !$#title Channel catfish virus: a new type of herpesvirus. !$#cross-references MUID:92087490; PMID:1727613 !$#contents annotation !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 11 CLASSIFICATION #superfamily ictalurid herpesvirus 30.2K zinc binding !1protein KEYWORDS zinc finger SUMMARY #length 281 #molecular-weight 30256 #checksum 6813 SEQUENCE /// ENTRY ZBBEI3 #type complete TITLE 33.1K zinc-binding protein - ictalurid herpesvirus 1 (strain auburn 1) ORGANISM #formal_name ictalurid herpesvirus 1 #note host Ictalurus punctatus (channel catfish) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS D36787 REFERENCE A36804 !$#authors Davison, A.J. !$#submission submitted to GenBank, January 1992 !$#description Channel catfish virus: a new type of herpesvirus. !$#accession D36787 !'##molecule_type DNA !'##residues 1-299 ##label DAV !'##cross-references GB:M75136; NID:g331209; PIDN:AAA88115.1; !1PID:g331222 REFERENCE A39447 !$#authors Davison, A.J. !$#journal Virology (1992) 186:9-14 !$#title Channel catfish virus: a new type of herpesvirus. !$#cross-references MUID:92087490; PMID:1727613 !$#contents annotation !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 12 CLASSIFICATION #superfamily ictalurid herpesvirus 33.1K zinc binding !1protein KEYWORDS zinc finger SUMMARY #length 299 #molecular-weight 33108 #checksum 2 SEQUENCE /// ENTRY ZBBEI4 #type complete TITLE 44.1K zinc-binding protein - ictalurid herpesvirus 1 (strain auburn 1) ORGANISM #formal_name ictalurid herpesvirus 1 #note host Ictalurus punctatus (channel catfish) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS D36794 REFERENCE A36804 !$#authors Davison, A.J. !$#submission submitted to GenBank, January 1992 !$#description Channel catfish virus: a new type of herpesvirus. !$#accession D36794 !'##molecule_type DNA !'##residues 1-400 ##label DAV !'##cross-references GB:M75136; NID:g331209; PIDN:AAA88180.1; !1PID:g331286 REFERENCE A39447 !$#authors Davison, A.J. !$#journal Virology (1992) 186:9-14 !$#title Channel catfish virus: a new type of herpesvirus. !$#cross-references MUID:92087490; PMID:1727613 !$#contents annotation !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 78 CLASSIFICATION #superfamily ictalurid herpesvirus 44.1K zinc binding !1protein KEYWORDS zinc finger SUMMARY #length 400 #molecular-weight 44167 #checksum 3354 SEQUENCE /// ENTRY VGBEI1 #type complete TITLE 149K glycoprotein - ictalurid herpesvirus 1 (strain auburn 1) ORGANISM #formal_name ictalurid herpesvirus 1 #note host Ictalurus punctatus (channel catfish) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS B36791 REFERENCE A36804 !$#authors Davison, A.J. !$#submission submitted to GenBank, January 1992 !$#description Channel catfish virus: a new type of herpesvirus. !$#accession B36791 !'##molecule_type DNA !'##residues 1-1355 ##label DAV !'##cross-references GB:M75136; NID:g331209; PIDN:AAA88149.1; !1PID:g331256 REFERENCE A39447 !$#authors Davison, A.J. !$#journal Virology (1992) 186:9-14 !$#title Channel catfish virus: a new type of herpesvirus. !$#cross-references MUID:92087490; PMID:1727613 !$#contents annotation !$#note neither amino acid nor nucleotide sequence is given GENETICS !$#gene 46 CLASSIFICATION #superfamily ictalurid herpesvirus 149K glycoprotein KEYWORDS glycoprotein FEATURE !$81,112,129,169,173, !$192,542,655,682, !$744,780,811,815, !$860,865,868,882, !$895,1195,1213,1225, !$1267,1274 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1355 #molecular-weight 149119 #checksum 820 SEQUENCE /// ENTRY PYXRCP #type complete TITLE polyhedrin - Bombyx mori cytoplasmic polyhedrosis virus ORGANISM #formal_name Bombyx mori cytoplasmic polyhedrosis virus, BmCPV #note host Bombyx mori (silkworm) DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jul-1999 ACCESSIONS A29961 REFERENCE A29961 !$#authors Arella, M.; Lavallee, C.; Belloncik, S.; Furuichi, Y. !$#journal J. Virol. (1988) 62:211-217 !$#title Molecular cloning and characterization of cytoplasmic !1polyhedrosis virus polyhedrin and a viable deletion mutant !1gene. !$#cross-references MUID:88062986; PMID:3275433 !$#accession A29961 !'##molecule_type genomic RNA !'##residues 1-248 ##label ARE !'##cross-references GB:M19112; NID:g332496; PIDN:AAA46694.1; !1PID:g332497 GENETICS !$#map_position segment 10 CLASSIFICATION #superfamily cytoplasmic polyhedrosis virus polyhedrin KEYWORDS glycoprotein; polyhedrin FEATURE !$28,77,86,237 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 248 #molecular-weight 28457 #checksum 7776 SEQUENCE /// ENTRY A46330 #type complete TITLE polyhedrin - Euxoa scandens cytoplasmic polyhedrosis virus ORGANISM #formal_name Euxoa scandens cytoplasmic polyhedrosis virus, EsCPV DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS A46330 REFERENCE A46330 !$#authors Fossiez, F.; Belloncik, S.; Arella, M. !$#journal Virology (1989) 169:462-465 !$#title Nucleotide sequence of the polyhedrin gene of Euxoa scandens !1cytoplasmic polyhedrosis virus (EsCPV). !$#cross-references MUID:89204919; PMID:2650462 !$#accession A46330 !'##molecule_type genomic RNA !'##residues 1-269 ##label FOS !'##cross-references GB:J04338; NID:g323374; PIDN:AAA42915.1; !1PID:g323375 GENETICS !$#map_position segment 10 CLASSIFICATION #superfamily Euxoa scandens cytoplasmic polyhedrosis virus !1polyhedrin KEYWORDS glycoprotein; polyhedrin FEATURE !$31,97,121 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 269 #molecular-weight 30189 #checksum 3906 SEQUENCE /// ENTRY PYNVSM #type complete TITLE polyhedrin - Bombyx mori nuclear polyhedrosis virus ORGANISM #formal_name Bombyx mori nuclear polyhedrosis virus, BmSNPV #note host Bombyx mori (silkworm) DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 31-Mar-2000 ACCESSIONS A03802; A03801 REFERENCE A03802 !$#authors Iatrou, K.; Ito, K.; Witkiewicz, H. !$#journal J. Virol. (1985) 54:436-445 !$#title Polyhedrin gene of Bombyx mori nuclear polyhedrosis virus. !$#cross-references MUID:85185672; PMID:3886932 !$#accession A03802 !'##molecule_type DNA !'##residues 1-245 ##label IAT !'##cross-references GB:M10043; NID:g332498; PIDN:AAA46734.1; !1PID:g332499 REFERENCE A03801 !$#authors Kozlov, E.A.; Levitina, T.L.; Katsman, M.S.; Gusak, N.M.; !1Serebryany, S.B. !$#journal Bioorg. Khim. (1978) 4:1048-1053 !$#title Reconstruction of the polypeptide chain of the inclusion !1body protein of the silkworm nuclear polyhedrosis virus. !1Complete amino acid sequence. !$#accession A03801 !'##molecule_type protein !'##residues 2-39,'EH',42-115,'V',116-142,'EN',146-213,'AS',216-218,'Q', !1220-245 ##label KOZ !'##note this is a final paper in a series giving the experimental !1details involved in elucidating the sequence CLASSIFICATION #superfamily nuclear polyhedrosis virus polyhedrin KEYWORDS polyhedrin FEATURE !$2-245 #product polyhedrin #status experimental #label MAT SUMMARY #length 245 #molecular-weight 28829 #checksum 8512 SEQUENCE /// ENTRY PYNVNV #type complete TITLE polyhedrin - Bombyx mori nuclear polyhedrosis virus (strain NPV) ORGANISM #formal_name Bombyx mori nuclear polyhedrosis virus, BmSNPV #note host Bombyx mori (silkworm) DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 08-Apr-1994 ACCESSIONS A26276 REFERENCE A26276 !$#authors Serebryani, S.B.; Levitina, T.L.; Kautsman, M.L.; Radavski, !1Y.L.; Gusak, N.M.; Ovander, M.N.; Sucharenko, N.V.; Kozlov, !1E.A. !$#journal J. Invertebr. Pathol. (1977) 30:442-443 !$#accession A26276 !'##molecule_type protein !'##residues 1-241 ##label SER CLASSIFICATION #superfamily nuclear polyhedrosis virus polyhedrin KEYWORDS polyhedrin SUMMARY #length 241 #molecular-weight 28220 #checksum 5561 SEQUENCE /// ENTRY PYNVA2 #type complete TITLE major occlusion body polyhedrin protein - Autographa californica nuclear polyhedrosis virus ORGANISM #formal_name Autographa californica nuclear polyhedrosis virus, AcMNPV #note host Autographa californica (alfalfa looper); dsDNA virus DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 24-Nov-1999 ACCESSIONS A03803; G40781; H72850 REFERENCE A03803 !$#authors Hooft van Iddekinge, B.J.L.; Smith, G.E.; Summers, M.D. !$#journal Virology (1983) 131:561-565 !$#title Nucleotide sequence of the polyhedrin gene of Autographa !1californica nuclear polyhedrosis virus. !$#accession A03803 !'##molecule_type DNA !'##residues 1-245 ##label HOO !'##experimental_source strain E2 REFERENCE A40781 !$#authors Possee, R.D.; Sun, T.P.; Howard, S.C.; Ayres, M.D.; !1Hill-Perkins, M.; Gearing, K.L. !$#journal Virology (1991) 185:229-241 !$#title Nucleotide sequence of the Autographa californica nuclear !1polyhedrosis 9.4 kbp EcoRI-I and -R (polyhedrin gene) !1region. !$#cross-references MUID:92024079; PMID:1926775 !$#accession G40781 !'##molecule_type DNA !'##residues 1-245 ##label POS !'##cross-references GB:M75679; NID:g332448; PIDN:AAA46704.1; !1PID:g332449 !'##experimental_source strain C6 REFERENCE A72850 !$#authors Ayres, M.D.; Howard, S.C.; Kuzio, J.; Lopez-Ferber, M.; !1Possee, R.D. !$#journal Virology (1994) 202:586-605 !$#title The complete DNA sequence of Autographa californica nuclear !1polyhedrosis virus. !$#cross-references MUID:94303173; PMID:8030224 !$#accession H72850 !'##status preliminary !'##molecule_type DNA !'##residues 1-245 ##label AYR !'##cross-references GB:L22858; NID:g510708; PIDN:AAA66638.1; !1PID:g559077 GENETICS !$#gene Ac-PH CLASSIFICATION #superfamily nuclear polyhedrosis virus polyhedrin KEYWORDS polyhedrin SUMMARY #length 245 #molecular-weight 28642 #checksum 7142 SEQUENCE /// ENTRY PYNVTM #type complete TITLE polyhedrin - Orgyia pseudotsugata single-capsid nuclear polyhedrosis virus ORGANISM #formal_name Orgyia pseudotsugata single-capsid nuclear polyhedrosis virus, OpSNPV #note host Orgyia pseudotsugata (Douglas-fir tussock moth) DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 16-Jul-1999 ACCESSIONS A25418 REFERENCE A25418 !$#authors Leisy, D.; Nesson, M.; Pearson, M.; Rohrmann, G.; Beaudreau, !1G. !$#journal J. Gen. Virol. (1986) 67:1073-1079 !$#title Location and nucleotide sequence of the Orgyia pseudotsugata !1single nucleocapsid nuclear polyhedrosis virus polyhedrin !1gene. !$#cross-references MUID:86226186; PMID:3011971 !$#accession A25418 !'##molecule_type DNA !'##residues 1-246 ##label LEI !'##cross-references GB:M32433; NID:g332534; PIDN:AAA46739.1; !1PID:g332535 CLASSIFICATION #superfamily nuclear polyhedrosis virus polyhedrin KEYWORDS polyhedrin SUMMARY #length 246 #molecular-weight 28890 #checksum 757 SEQUENCE /// ENTRY PYNVPF #type complete TITLE polyhedrin - Panolis flammea multicapsid nuclear polyhedrosis virus ORGANISM #formal_name Panolis flammea multicapsid nuclear polyhedrosis virus, PfMNPV DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jun-2000 ACCESSIONS A31814 REFERENCE A31814 !$#authors Oakey, R.; Cameron, I.R.; Davis, B.; Davis, E.; Possee, R.D. !$#journal J. Gen. Virol. (1989) 70:769-775 !$#title Analysis of transcription initiation in the Panolis flammea !1nuclear polyhedrosis virus polyhedrin gene. !$#cross-references MUID:89279257; PMID:2659729 !$#accession A31814 !'##molecule_type DNA !'##residues 1-246 ##label OAK !'##cross-references GB:D00437; NID:g222269; PIDN:BAA00338.1; !1PID:g222270 CLASSIFICATION #superfamily nuclear polyhedrosis virus polyhedrin KEYWORDS late protein; nucleus; polyhedrin SUMMARY #length 246 #molecular-weight 28935 #checksum 2636 SEQUENCE /// ENTRY A42756 #type complete TITLE polyhedrin - Mamestra brassicae nuclear polyhedrosis virus (strain Oxford) ORGANISM #formal_name Mamestra brassicae nuclear polyhedrosis virus, MbMNPV DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jul-1999 ACCESSIONS A42756 REFERENCE A42756 !$#authors Cameron, I.R.; Possee, R.D. !$#journal Virus Res. (1989) 12:183-199 !$#title Conservation of polyhedrin gene promoter function between !1Autographa californica and Mamestra brassicae nuclear !1polyhedrosis viruses. !$#cross-references MUID:89269078; PMID:2658411 !$#accession A42756 !'##molecule_type DNA !'##residues 1-246 ##label CAM !'##cross-references GB:M20927; NID:g332521; PIDN:AAA69768.1; !1PID:g332522 CLASSIFICATION #superfamily nuclear polyhedrosis virus polyhedrin KEYWORDS nucleus; polyhedrin SUMMARY #length 246 #molecular-weight 28965 #checksum 3683 SEQUENCE /// ENTRY PYNVPA #type complete TITLE polyhedrin - Agrotis segetum nuclear polyhedrosis virus ORGANISM #formal_name Agrotis segetum nuclear polyhedrosis virus DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 08-Apr-1994 ACCESSIONS B40233 REFERENCE A40233 !$#authors Kozlov, E.A.; Rodnin, N.V.; Levitina, T.L.; Gusak, N.M.; !1Radomskij, N.F.; Palchikovskaya, L.J. !$#journal Virology (1992) 189:320-323 !$#title The amino acid sequence determination of a granulin and !1polyhedrin from two baculoviruses infecting Agrotis segetum. !$#cross-references MUID:92295569; PMID:1604817 !$#accession B40233 !'##molecule_type protein !'##residues 1-246 ##label KOZ CLASSIFICATION #superfamily nuclear polyhedrosis virus polyhedrin KEYWORDS late protein; nucleus; polyhedrin SUMMARY #length 246 #molecular-weight 28918 #checksum 9433 SEQUENCE /// ENTRY JQ1607 #type complete TITLE polyhedrin - Anticarsia gemmatalis nuclear polyhedrosis virus (strain 2D) ORGANISM #formal_name Anticarsia gemmatalis nuclear polyhedrosis virus, AnMNPV DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jun-2000 ACCESSIONS JQ1607; PQ0390 REFERENCE JQ1607 !$#authors Zanotto, P.M.A.; Sampaio, M.J.A.; Johnson, D.W.; Rocha, !1T.L.; Maruniak, J.E. !$#journal J. Gen. Virol. (1992) 73:1049-1056 !$#title The Anticarsia gemmatalis nuclear polyhedrosis virus !1polyhedrin gene region: sequence analysis, gene product and !1structural comparisons. !$#cross-references MUID:92268862; PMID:1588315 !$#accession JQ1607 !'##molecule_type DNA !'##residues 1-245 ##label ZAN !'##cross-references GB:Y17753; NID:g3319868; PIDN:CAA76844.1; !1PID:g3319870 !$#accession PQ0390 !'##molecule_type protein !'##residues 1-41,'QQ',44-102,'M',104-111,'N',113;115;124-189;192,'Q', !1194-212;220-245 ##label ZA2 CLASSIFICATION #superfamily nuclear polyhedrosis virus polyhedrin KEYWORDS polyhedrin SUMMARY #length 245 #molecular-weight 28705 #checksum 8666 SEQUENCE /// ENTRY PYNVPM #type complete TITLE polyhedrin - Orgyia pseudotsugata multicapsid nuclear polyhedrosis virus ORGANISM #formal_name Orgyia pseudotsugata multicapsid nuclear polyhedrosis virus, OpMNPV #note host Orgyia pseudotsugata (Douglas-fir tussock moth) DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jul-1999 ACCESSIONS A24188 REFERENCE A24188 !$#authors Leisy, D.; Rohrmann, G.; Beaudreau, G. !$#journal Virology (1986) 153:280-288 !$#title The nucleotide sequence of the polyhedrin gene region from !1the multicapsid baculovirus of Orgyia pseudotsugata. !$#cross-references MUID:86291169; PMID:3526710 !$#accession A24188 !'##molecule_type DNA !'##residues 1-245 ##label LEI !'##cross-references GB:M14885; NID:g763521; PIDN:AAA64926.1; !1PID:g332539 CLASSIFICATION #superfamily nuclear polyhedrosis virus polyhedrin KEYWORDS polyhedrin SUMMARY #length 245 #molecular-weight 28818 #checksum 8672 SEQUENCE /// ENTRY JQ1868 #type complete TITLE polyhedrin - Spodoptera exigua nuclear polyhedrosis virus (strain US) ORGANISM #formal_name Spodoptera exigua nuclear polyhedrosis virus, SeMNPV DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS JQ1868; S24649 REFERENCE JQ1868 !$#authors van Strien, E.A.; Zuidema, D.; Goldbach, R.W.; Vlak, J.M. !$#journal J. Gen. Virol. (1992) 73:2813-2821 !$#title Nucleotide sequence and transcriptional analysis of the !1polyhedrin gene of Spodoptera exigua nuclear polyhedrosis !1virus. !$#cross-references MUID:93057353; PMID:1431809 !$#accession JQ1868 !'##molecule_type DNA !'##residues 1-246 ##label VAN !'##cross-references GB:X67243; NID:g61955; PIDN:CAA47668.1; PID:g61956 CLASSIFICATION #superfamily nuclear polyhedrosis virus polyhedrin KEYWORDS polyhedrin SUMMARY #length 246 #molecular-weight 28950 #checksum 2613 SEQUENCE /// ENTRY PYNVSF #type complete TITLE polyhedrin - Spodoptera frugiperda nuclear polyhedrosis virus ORGANISM #formal_name Spodoptera frugiperda nuclear polyhedrosis virus, SfMNPV #note host Spodoptera frugiperda DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS A31472 REFERENCE A31472 !$#authors Gonzalez, M.A.; Smith, G.E.; Summers, M.D. !$#journal Virology (1989) 170:160-175 !$#title Insertion of the SfMNPV polyhedrin gene into an AcMNPV !1polyhedrin deletion mutant during viral infection. !$#cross-references MUID:89243172; PMID:2655273 !$#accession A31472 !'##molecule_type DNA !'##residues 1-246 ##label GON !'##cross-references GB:M25054; NID:g332476; PIDN:AAA46736.1; !1PID:g332477; GB:J04333; NID:g332543; PID:g332544 CLASSIFICATION #superfamily nuclear polyhedrosis virus polyhedrin KEYWORDS polyhedrin SUMMARY #length 246 #molecular-weight 28945 #checksum 1750 SEQUENCE /// ENTRY PYNVLD #type complete TITLE polyhedrin - Lymantria dispar nuclear polyhedrosis virus ORGANISM #formal_name Lymantria dispar nuclear polyhedrosis virus, LdMNPV #note host Lymantria dispar (gypsy moth) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 05-Nov-1999 ACCESSIONS JT0388; A61463; T30348 REFERENCE JT0388 !$#authors Smith, I.R.L.; van Beek, N.A.M.; Podgwaite, J.D.; Wood, H.A. !$#journal Gene (1988) 71:97-105 !$#title Physical map and polyhedrin gene sequence of Lymantria !1dispar nuclear polyhedrosis virus. !$#cross-references MUID:89108053; PMID:3063616 !$#accession JT0388 !'##molecule_type DNA !'##residues 1-245 ##label SMI !'##cross-references GB:M23176 REFERENCE A61463 !$#authors Chang, M.T.; Lanner-Herrera, C.; Fikes, M. !$#journal J. Invertebr. Pathol. (1989) 53:241-246 !$#title Nucleotide sequence of Lymantria dispar nuclear polyhedrosis !1virus polyhedrin gene. !$#cross-references MUID:89256732; PMID:2656870 !$#accession A61463 !'##molecule_type DNA !'##residues 1-245 ##label CHA REFERENCE Z20836 !$#authors Kuzio, J.; Pearson, M.N.; Harwood, S.H.; Funk, C.J.; Evans, !1J.T.; Slavicek, J.M.; Rohrmann, G.F. !$#journal Virology (1999) 253:17-34 !$#title Sequence and analysis of the genome of a baculovirus !1pathogenic for Lymantria dispar. !$#cross-references MUID:99124785; PMID:9887315 !$#accession T30348 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-245 ##label KUZ !'##cross-references EMBL:AF081810; PIDN:AAC70186.1 CLASSIFICATION #superfamily nuclear polyhedrosis virus polyhedrin KEYWORDS late protein; nucleus; polyhedrin SUMMARY #length 245 #molecular-weight 28772 #checksum 893 SEQUENCE /// ENTRY PYNVGA #type complete TITLE granulin - Agrotis segetum granulosis virus ORGANISM #formal_name Agrotis segetum granulosis virus, AsGV DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 08-Apr-1994 ACCESSIONS A40233 REFERENCE A40233 !$#authors Kozlov, E.A.; Rodnin, N.V.; Levitina, T.L.; Gusak, N.M.; !1Radomskij, N.F.; Palchikovskaya, L.J. !$#journal Virology (1992) 189:320-323 !$#title The amino acid sequence determination of a granulin and !1polyhedrin from two baculoviruses infecting Agrotis segetum. !$#cross-references MUID:92295569; PMID:1604817 !$#accession A40233 !'##molecule_type protein !'##residues 1-247 ##label KOZ CLASSIFICATION #superfamily nuclear polyhedrosis virus polyhedrin KEYWORDS late protein; polyhedrin SUMMARY #length 247 #molecular-weight 29141 #checksum 1859 SEQUENCE /// ENTRY A46542 #type complete TITLE granulin - Trichoplusia ni granulosis virus ORGANISM #formal_name Trichoplusia ni granulosis virus, TnGV DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS A46542 REFERENCE A46542 !$#authors Akiyoshi, D.; Chakerian, R.; Rohrmann, G.F.; Nesson, M.H.; !1Beaudreau, G.S. !$#journal Virology (1985) 141:328-332 !$#title Cloning and sequencing of the granulin gene from the !1Trichoplusia ni granulosis virus. !$#cross-references MUID:86098652; PMID:4082501 !$#accession A46542 !'##molecule_type DNA !'##residues 1-248 ##label AKI !'##cross-references GB:K02910; NID:g325406; PIDN:AAA43834.1; !1PID:g325407 CLASSIFICATION #superfamily nuclear polyhedrosis virus polyhedrin KEYWORDS late protein; polyhedrin SUMMARY #length 248 #molecular-weight 29217 #checksum 2143 SEQUENCE /// ENTRY WMNVPM #type complete TITLE P10 protein - Orgyia pseudotsugata multicapsid nuclear polyhedrosis virus ORGANISM #formal_name Orgyia pseudotsugata multicapsid nuclear polyhedrosis virus, OpMNPV #note host Orgyia pseudotsugata (Douglas-fir tussock moth) DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jul-1999 ACCESSIONS A24186 REFERENCE A24186 !$#authors Leisy, D.J.; Rohrmann, G.F.; Nesson, M.; Beaudreau, G.S. !$#journal Virology (1986) 153:157-167 !$#title Nucleotide sequencing and transcriptional mapping of the !1Orgyia pseudotsugata multicapsid nuclear polyhedrosis virus !1p10 gene. !$#cross-references MUID:86291160; PMID:3526709 !$#accession A24186 !'##molecule_type DNA !'##residues 1-92 ##label LEI !'##cross-references GB:M14883; NID:g332529; PIDN:AAA46725.1; !1PID:g332530 !'##note the authors translated the codon AAG for residue 3 as Leu CLASSIFICATION #superfamily nuclear polyhedrosis virus P10 protein KEYWORDS late protein SUMMARY #length 92 #molecular-weight 10086 #checksum 4817 SEQUENCE /// ENTRY WMNVIA #type complete TITLE immediate-early protein IE-N - Autographa californica nuclear polyhedrosis virus ORGANISM #formal_name Autographa californica nuclear polyhedrosis virus, AcMNPV DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jul-1999 ACCESSIONS A39150 REFERENCE A39150 !$#authors Carson, D.D.; Summers, M.D.; Guarino, L.A. !$#journal Virology (1991) 182:279-286 !$#title Molecular analysis of a baculovirus regulatory gene. !$#cross-references MUID:91220660; PMID:2024466 !$#accession A39150 !'##molecule_type DNA !'##residues 1-408 ##label CAR !'##cross-references GB:M59422; NID:g332437; PIDN:AAA46701.1; !1PID:g332438 CLASSIFICATION #superfamily AcMNPV immediate-early protein IE-N KEYWORDS DNA binding; early protein; tandem repeat; transcription !1regulation FEATURE !$34-49 #region 7-residue repeats\ !$51-58 #region 4-residue repeats\ !$190-196 #region glutamine-rich SUMMARY #length 408 #molecular-weight 47092 #checksum 3251 SEQUENCE /// ENTRY WMNVP1 #type complete TITLE immediate-early protein IE-2 - Orgyia pseudotsugata multicapsid nuclear polyhedrosis virus ALTERNATE_NAMES trans-activator IE-2 ORGANISM #formal_name Orgyia pseudotsugata multicapsid nuclear polyhedrosis virus, OpMNPV DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS A42190 REFERENCE A42190 !$#authors Theilmann, D.A.; Stewart, S. !$#journal Virology (1992) 187:84-96 !$#title Molecular analysis of the trans-activating IE-2 gene of !1Orgyia pseudotsugata multicapsid nuclear polyhedrosis virus. !$#cross-references MUID:92142536; PMID:1736546 !$#accession A42190 !'##molecule_type DNA !'##residues 1-405 ##label THE !'##cross-references GB:M83827; NID:g332540; PIDN:AAA46749.1; !1PID:g332541 CLASSIFICATION #superfamily AcMNPV immediate-early protein IE-N KEYWORDS DNA binding; early protein; transcription regulation SUMMARY #length 405 #molecular-weight 45669 #checksum 8395 SEQUENCE /// ENTRY WMNV35 #type complete TITLE early 35K protein, apoptosis inhibitor - Autographa californica nuclear polyhedrosis virus ORGANISM #formal_name Autographa californica nuclear polyhedrosis virus, AcMNPV DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 24-Nov-1999 ACCESSIONS A27840; H72866 REFERENCE A93026 !$#authors Friesen, P.D.; Miller, L.K. !$#journal J. Virol. (1987) 61:2264-2272 !$#title Divergent transcription of early 35- and 94-kilodalton !1protein genes encoded by the HindIII K genome fragment of !1the baculovirus Autographa californica nuclear polyhedrosis !1virus. !$#cross-references MUID:87226411; PMID:3035225 !$#accession A27840 !'##molecule_type DNA !'##residues 1-299 ##label FRI !'##cross-references GB:M16821; NID:g332445; PIDN:AAA46703.1; !1PID:g332447 !'##experimental_source strain L-1 REFERENCE A72850 !$#authors Ayres, M.D.; Howard, S.C.; Kuzio, J.; Lopez-Ferber, M.; !1Possee, R.D. !$#journal Virology (1994) 202:586-605 !$#title The complete DNA sequence of Autographa californica nuclear !1polyhedrosis virus. !$#cross-references MUID:94303173; PMID:8030224 !$#accession H72866 !'##status preliminary !'##molecule_type DNA !'##residues 1-299 ##label AYR !'##cross-references GB:L22858; NID:g510708; PIDN:AAA66765.1; !1PID:g559204 GENETICS !$#gene Ac-35K/p35 CLASSIFICATION #superfamily Autographa californica nuclear polyhedrosis !1virus early 35K protein KEYWORDS early protein SUMMARY #length 299 #molecular-weight 34828 #checksum 6776 SEQUENCE /// ENTRY WMNV94 #type complete TITLE early 94K protein - Autographa californica nuclear polyhedrosis virus (strain L-1) ORGANISM #formal_name Autographa californica nuclear polyhedrosis virus, AcMNPV DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 16-Jul-1999 ACCESSIONS B27840 REFERENCE A93026 !$#authors Friesen, P.D.; Miller, L.K. !$#journal J. Virol. (1987) 61:2264-2272 !$#title Divergent transcription of early 35- and 94-kilodalton !1protein genes encoded by the HindIII K genome fragment of !1the baculovirus Autographa californica nuclear polyhedrosis !1virus. !$#cross-references MUID:87226411; PMID:3035225 !$#accession B27840 !'##molecule_type DNA !'##residues 1-803 ##label FRI !'##cross-references GB:M16821; NID:g332445; PIDN:AAA46702.1; !1PID:g332446 CLASSIFICATION #superfamily Autographa californica nuclear polyhedrosis !1virus early 94K protein KEYWORDS early protein SUMMARY #length 803 #molecular-weight 94539 #checksum 1078 SEQUENCE /// ENTRY WMNVEM #type complete TITLE EcoRI-T medium (ETM) AcOrf-48 protein - Autographa californica nuclear polyhedrosis virus ORGANISM #formal_name Autographa californica nuclear polyhedrosis virus, AcMNPV DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 24-Nov-1999 ACCESSIONS B28147; H72855 REFERENCE A93034 !$#authors Crawford, A.M.; Miller, L.K. !$#journal J. Virol. (1988) 62:2773-2781 !$#title Characterization of an early gene accelerating expression of !1late genes of the baculovirus Autographa californica nuclear !1polyhedrosis virus. !$#cross-references MUID:88275045; PMID:3292791 !$#accession B28147 !'##molecule_type DNA !'##residues 1-113 ##label CRA !'##cross-references GB:M20718; NID:g332418; PIDN:AAA21098.1; !1PID:g332420 REFERENCE A72850 !$#authors Ayres, M.D.; Howard, S.C.; Kuzio, J.; Lopez-Ferber, M.; !1Possee, R.D. !$#journal Virology (1994) 202:586-605 !$#title The complete DNA sequence of Autographa californica nuclear !1polyhedrosis virus. !$#cross-references MUID:94303173; PMID:8030224 !$#accession H72855 !'##status preliminary !'##molecule_type DNA !'##residues 1-113 ##label AYR !'##cross-references GB:L22858; NID:g510708; PIDN:AAA66678.1; !1PID:g559117 GENETICS !$#gene AcOrf-48 CLASSIFICATION #superfamily Autographa californica nuclear polyhedrosis !1virus EcoRI-T medium protein KEYWORDS early protein SUMMARY #length 113 #molecular-weight 12873 #checksum 8710 SEQUENCE /// ENTRY WMNVES #type complete TITLE EcoRI-T small (ETS) AcOrf-47 protein - Autographa californica nuclear polyhedrosis virus ORGANISM #formal_name Autographa californica nuclear polyhedrosis virus, AcMNPV DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 24-Nov-1999 ACCESSIONS C28147; G72855 REFERENCE A93034 !$#authors Crawford, A.M.; Miller, L.K. !$#journal J. Virol. (1988) 62:2773-2781 !$#title Characterization of an early gene accelerating expression of !1late genes of the baculovirus Autographa californica nuclear !1polyhedrosis virus. !$#cross-references MUID:88275045; PMID:3292791 !$#accession C28147 !'##molecule_type DNA !'##residues 1-88 ##label CRA !'##cross-references GB:M20718; NID:g332418; PIDN:AAA21099.1; !1PID:g332421 REFERENCE A72850 !$#authors Ayres, M.D.; Howard, S.C.; Kuzio, J.; Lopez-Ferber, M.; !1Possee, R.D. !$#journal Virology (1994) 202:586-605 !$#title The complete DNA sequence of Autographa californica nuclear !1polyhedrosis virus. !$#cross-references MUID:94303173; PMID:8030224 !$#accession G72855 !'##status preliminary !'##molecule_type DNA !'##residues 1-88 ##label AYR !'##cross-references GB:L22858; NID:g510708; PIDN:AAA66677.1; !1PID:g559116 GENETICS !$#gene AcOrf-47 CLASSIFICATION #superfamily Autographa californica nuclear polyhedrosis !1virus EcoRI-T small protein KEYWORDS early protein SUMMARY #length 88 #molecular-weight 10482 #checksum 1667 SEQUENCE /// ENTRY RGNVBV #type complete TITLE trans-activating transcription regulator - Autographa californica nuclear polyhedrosis virus ORGANISM #formal_name Autographa californica nuclear polyhedrosis virus, AcMNPV DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 16-Jul-1999 ACCESSIONS A27838 REFERENCE A27838 !$#authors Guarino, L.A.; Summers, M.D. !$#journal J. Virol. (1987) 61:2091-2099 !$#title Nucleotide sequence and temporal expression of a baculovirus !1regulatory gene. !$#accession A27838 !'##molecule_type DNA !'##residues 1-581 ##label GUA !'##cross-references GB:M16820; NID:g332435; PIDN:AAA46699.1; !1PID:g332436 !'##note this ORF is not annotated in GenBank entry P22TPRO CLASSIFICATION #superfamily Autographa californica nuclear polyhedrosis !1virus trans-activating transcription regulator KEYWORDS alternative splicing; transcription regulation SUMMARY #length 581 #molecular-weight 66856 #checksum 1440 SEQUENCE /// ENTRY RGNVE2 #type complete TITLE trans-activating transcription regulator - Autographa californica nuclear polyhedrosis virus (strain E2) ALTERNATE_NAMES gene IE-1 protein ORGANISM #formal_name Autographa californica nuclear polyhedrosis virus, AcMNPV DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS A28874 REFERENCE A28874 !$#authors Chisholm, G.E.; Henner, D.J. !$#journal J. Virol. (1988) 62:3193-3200 !$#title Multiple early transcripts and splicing of the Autographa !1californica nuclear polyhedrosis virus IE-1 gene. !$#cross-references MUID:88300868; PMID:3043024 !$#accession A28874 !'##molecule_type DNA !'##residues 1-582 ##label CHI !'##cross-references GB:M21884; NID:g332432; PIDN:AAA46696.1; !1PID:g332434 CLASSIFICATION #superfamily Autographa californica nuclear polyhedrosis !1virus trans-activating transcription regulator KEYWORDS alternative splicing; early protein; transcription !1regulation SUMMARY #length 582 #molecular-weight 66823 #checksum 2231 SEQUENCE /// ENTRY RGNVPM #type complete TITLE trans-activating transcription regulator - Orgyia pseudotsugata multicapsid nuclear polyhedrosis virus ALTERNATE_NAMES IE-1 protein ORGANISM #formal_name Orgyia pseudotsugata multicapsid nuclear polyhedrosis virus, OpMNPV DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jul-1999 ACCESSIONS A38544 REFERENCE A38544 !$#authors Theilmann, D.A.; Stewart, S. !$#journal Virology (1991) 180:492-508 !$#title Identification and characterization of the IE-1 gene of !1Orgyia pseudotsugata multicapsid nuclear polyhedrosis virus. !$#cross-references MUID:91111968; PMID:1989381 !$#accession A38544 !'##molecule_type DNA !'##residues 1-560 ##label THE !'##cross-references EMBL:M63414; NID:g332527; PIDN:AAA46700.1; !1PID:g332528 CLASSIFICATION #superfamily Autographa californica nuclear polyhedrosis !1virus trans-activating transcription regulator KEYWORDS alternative splicing; early protein; transcription SUMMARY #length 560 #molecular-weight 64315 #checksum 7071 SEQUENCE /// ENTRY WMNVP6 #type complete TITLE p26 protein - Autographa californica nuclear polyhedrosis virus ORGANISM #formal_name Autographa californica nuclear polyhedrosis virus, AcMNPV DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 24-Nov-1999 ACCESSIONS A29150; A72867 REFERENCE A29150 !$#authors Liu, A.; Qin, J.; Rankin, C.; Hardin, S.E.; Weaver, R.F. !$#journal J. Gen. Virol. (1986) 67:2565-2570 !$#title Nucleotide sequence of a portion of the Autographa !1californica nuclear polyhedrosis virus genome containing the !1EcoRI site-rich region (hr5) and an open reading frame just !15' of the p10 gene. !$#cross-references MUID:87059784; PMID:3023539 !$#accession A29150 !'##molecule_type DNA !'##residues 1-240 ##label LIU !'##cross-references EMBL:X04611; NID:g58669; PIDN:CAA28280.1; !1PID:g58670 !'##experimental_source strain L1 REFERENCE A72850 !$#authors Ayres, M.D.; Howard, S.C.; Kuzio, J.; Lopez-Ferber, M.; !1Possee, R.D. !$#journal Virology (1994) 202:586-605 !$#title The complete DNA sequence of Autographa californica nuclear !1polyhedrosis virus. !$#cross-references MUID:94303173; PMID:8030224 !$#accession A72867 !'##status preliminary !'##molecule_type DNA !'##residues 1-240 ##label AYR !'##cross-references GB:L22858; NID:g510708; PIDN:AAA66766.1; !1PID:g559205 GENETICS !$#gene p26; Ac-p26 CLASSIFICATION #superfamily nuclear polyhedrosis virus p26 protein KEYWORDS glycoprotein; late protein FEATURE !$106,170,193 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 240 #molecular-weight 27282 #checksum 4545 SEQUENCE /// ENTRY WMNV26 #type complete TITLE p26 protein [similarity] - Orgyia pseudotsugata multicapsid nuclear polyhedrosis virus ORGANISM #formal_name Orgyia pseudotsugata multicapsid nuclear polyhedrosis virus, OpMNPV DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 01-Sep-2000 ACCESSIONS A27405; T10401 REFERENCE A27405 !$#authors Bicknell, J.N.; Leisy, D.J.; Rohrmann, G.F.; Beaudreau, G.S. !$#journal Virology (1987) 161:589-592 !$#title Comparison of the p26 gene region of two baculoviruses. !$#cross-references MUID:88072101; PMID:3686831 !$#accession A27405 !'##molecule_type DNA !'##residues 1-230 ##label BIC !'##cross-references GB:M18367; NID:g332531; PIDN:AAA46727.1; !1PID:g332532 !'##note the authors translated the codon CGC for residue 205 as Ala REFERENCE Z17011 !$#authors Ahrens, C.A.; Russell, R.R.; Funk, C.J.; Evans, J.; Harwood, !1S.; Rohrmann, G.F. !$#journal Virology (1997) 229:381-399 !$#title The sequence of the Orgyia pseudotsugata multinucleocapsid !1nuclear polyhedrosis virus genome. !$#cross-references MUID:97271300; PMID:9126251 !$#accession T10401 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-230 ##label AHR !'##cross-references EMBL:U75930; NID:g2934903; PID:g1911378 CLASSIFICATION #superfamily nuclear polyhedrosis virus p26 protein KEYWORDS glycoprotein; late protein FEATURE !$200 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 230 #molecular-weight 25565 #checksum 5187 SEQUENCE /// ENTRY WMNV74 #type complete TITLE p74 protein - Autographa californica nuclear polyhedrosis virus ORGANISM #formal_name Autographa californica nuclear polyhedrosis virus, AcMNPV DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS A33750 REFERENCE A33750 !$#authors Kuzio, J.; Jaques, R.; Faulkner, P. !$#journal Virology (1989) 173:759-763 !$#title Identification of p74, a gene essential for virulence of !1baculovirus occlusion bodies. !$#cross-references MUID:90085829; PMID:2688302 !$#accession A33750 !'##molecule_type DNA !'##residues 1-645 ##label KUZ !'##cross-references GB:M31301; NID:g332464; PIDN:AAA46729.1; !1PID:g332466 CLASSIFICATION #superfamily nuclear polyhedrosis virus p74 protein SUMMARY #length 645 #molecular-weight 73903 #checksum 8956 SEQUENCE /// ENTRY VHNVAC #type complete TITLE nucleocapsid protein - Autographa californica nuclear polyhedrosis virus ALTERNATE_NAMES arginine-rich 6.9K protein ORGANISM #formal_name Autographa californica nuclear polyhedrosis virus, AcMNPV DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 24-Nov-1999 ACCESSIONS A26593; E72862 REFERENCE A26593 !$#authors Wilson, M.E.; Mainprize, T.H.; Friesen, P.D.; Miller, L.K. !$#journal J. Virol. (1987) 61:661-666 !$#title Location, transcription, and sequence of a baculovirus gene !1encoding a small arginine-rich polypeptide. !$#cross-references MUID:87112972; PMID:3543402 !$#accession A26593 !'##molecule_type mRNA !'##residues 1-55 ##label WIL !'##cross-references GB:M15370; NID:g332483; PIDN:AAA46745.1; !1PID:g332484 REFERENCE A72850 !$#authors Ayres, M.D.; Howard, S.C.; Kuzio, J.; Lopez-Ferber, M.; !1Possee, R.D. !$#journal Virology (1994) 202:586-605 !$#title The complete DNA sequence of Autographa californica nuclear !1polyhedrosis virus. !$#cross-references MUID:94303173; PMID:8030224 !$#accession E72862 !'##status preliminary !'##molecule_type DNA !'##residues 1-55 ##label AYR !'##cross-references GB:L22858; NID:g510708; PIDN:AAA66730.1; !1PID:g559169 GENETICS !$#gene Ac-p6.9 CLASSIFICATION #superfamily Autographa californica nuclear polyhedrosis !1virus nucleocapsid protein KEYWORDS nucleocapsid SUMMARY #length 55 #molecular-weight 6885 #checksum 7075 SEQUENCE /// ENTRY VHNVBM #type complete TITLE nucleocapsid protein DNA binding P6.9 orf100 - Bombyx mori nuclear polyhedrosis virus (isolate T3) ALTERNATE_NAMES DNA-binding protein ORGANISM #formal_name Bombyx mori nuclear polyhedrosis virus, BmSNPV #variety isolate T3 DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 11-May-2000 ACCESSIONS A38554; T41841 REFERENCE A38554 !$#authors Maeda, S.; Kamita, S.G.; Kataoka, H. !$#journal Virology (1991) 180:807-810 !$#title The basic DNA-binding protein of Bombyx mori nuclear !1polyhedrosis virus: the existence of an additional arginine !1repeat. !$#cross-references MUID:91112001; PMID:1703373 !$#accession A38554 !'##molecule_type DNA !'##residues 1-65 ##label MAE !'##cross-references EMBL:M63416; NID:g332494; PIDN:AAA46691.1; !1PID:g332495 REFERENCE Z22020 !$#authors Gomi, S.; Majima, K.; Maeda, S. !$#journal J. Gen. Virol. (1999) 80:1323-1337 !$#title Sequence analysis of the genome of Bombyx mori !1nucleopolyhedrovirus. !$#cross-references MUID:99281911; PMID:10355780 !$#accession T41841 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-65 ##label KAM !'##cross-references EMBL:L33180; PIDN:AAC63770.1 !'##experimental_source isolate T3 CLASSIFICATION #superfamily Autographa californica nuclear polyhedrosis !1virus nucleocapsid protein KEYWORDS DNA binding; late protein; nucleocapsid SUMMARY #length 65 #molecular-weight 8078 #checksum 7112 SEQUENCE /// ENTRY VHNVMN #type complete TITLE nucleocapsid protein - Orgyia pseudotsugata multicapsid nuclear polyhedrosis virus ORGANISM #formal_name Orgyia pseudotsugata multicapsid nuclear polyhedrosis virus, OpMNPV DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 13-Sep-1997 ACCESSIONS D34526 REFERENCE A34526 !$#authors Russell, R.L.Q.; Rohrmann, G.F. !$#journal J. Gen. Virol. (1990) 71:551-560 !$#title The p6.5 gene region of a nuclear polyhedrosis virus of !1Orgyia pseudotsugata: DNA sequence and transcriptional !1analysis of four late genes. !$#cross-references MUID:90188300; PMID:2179466 !$#accession D34526 !'##molecule_type DNA !'##residues 1-51 ##label RUS CLASSIFICATION #superfamily Autographa californica nuclear polyhedrosis !1virus nucleocapsid protein KEYWORDS late protein; nucleocapsid SUMMARY #length 51 #molecular-weight 6209 #checksum 7322 SEQUENCE /// ENTRY DNNVAL #type complete TITLE DNA-binding protein - Autographa californica nuclear polyhedrosis virus ORGANISM #formal_name Autographa californica nuclear polyhedrosis virus, AcMNPV DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 24-Nov-1999 ACCESSIONS A33324; A72861 REFERENCE A33324 !$#authors Thiem, S.M.; Miller, L.K. !$#journal J. Virol. (1989) 63:4489-4497 !$#title A baculovirus gene with a novel transcription pattern !1encodes a polypeptide with a zinc finger and a leucine !1zipper. !$#cross-references MUID:90012293; PMID:2507791 !$#accession A33324 !'##molecule_type DNA !'##residues 1-264 ##label THI !'##cross-references GB:M26529; NID:g309612; PIDN:AAA46754.1; !1PID:g309613 !'##experimental_source strain L-1 REFERENCE A72850 !$#authors Ayres, M.D.; Howard, S.C.; Kuzio, J.; Lopez-Ferber, M.; !1Possee, R.D. !$#journal Virology (1994) 202:586-605 !$#title The complete DNA sequence of Autographa californica nuclear !1polyhedrosis virus. !$#cross-references MUID:94303173; PMID:8030224 !$#accession A72861 !'##status preliminary !'##molecule_type DNA !'##residues 1-264 ##label AYR !'##cross-references GB:L22858; NID:g510708; PIDN:AAA66718.1; !1PID:g559157 GENETICS !$#gene Ac-cg30 CLASSIFICATION #superfamily baculovirus DNA-binding protein KEYWORDS DNA binding; zinc finger SUMMARY #length 264 #molecular-weight 30092 #checksum 6530 SEQUENCE /// ENTRY WMNV29 #type complete TITLE AcOrf-16 DA26 protein - Autographa californica nuclear polyhedrosis virus ALTERNATE_NAMES orf1 protein ORGANISM #formal_name Autographa californica nuclear polyhedrosis virus, AcMNPV DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 24-Nov-1999 ACCESSIONS A29891; A34765; A44221; H72851 REFERENCE A93041 !$#authors Guarino, L.A.; Summers, M.D. !$#journal J. Virol. (1988) 62:463-471 !$#title Functional mapping of Autographa californica nuclear !1polyhedrosis virus genes required for late gene expression. !$#cross-references MUID:88091055; PMID:2826808 !$#accession A29891 !'##molecule_type DNA !'##residues 1-225 ##label GUA !'##cross-references EMBL:M18857; NID:g332482; PIDN:AAA66808.1; !1PID:g808753 REFERENCE A34765 !$#authors O'Reilly, D.R.; Passarelli, A.L.; Goldman, I.F.; Miller, !1L.K. !$#journal J. Gen. Virol. (1990) 71:1029-1037 !$#title Characterization of the DA26 gene in a hypervariable region !1of the Autographa californica nuclear polyhedrosis virus !1genome. !$#cross-references MUID:90264832; PMID:2189022 !$#accession A34765 !'##molecule_type DNA !'##residues 1-225 ##label OAR !'##cross-references GB:M22619; GB:M33904; NID:g332422; PIDN:AAA69846.1; !1PID:g896308 REFERENCE A44221 !$#authors Braunagel, S.C.; Daniel, K.D.; Reilly, L.M.; Guarino, L.A.; !1Hong, T.; Summers, M.D. !$#journal Virology (1992) 191:1003-1008 !$#title Sequence, genomic organization of the EcoRI-A fragment of !1Autographa californica nuclear polyhedrosis virus, and !1identification of a viral-encoded protein resembling the !1outer capsid protein VP8 of rotavirus. !$#cross-references MUID:93079853; PMID:1333113 !$#accession A44221 !'##status preliminary !'##molecule_type DNA !'##residues 1-225 ##label BRA !'##cross-references GB:S52569 REFERENCE A72850 !$#authors Ayres, M.D.; Howard, S.C.; Kuzio, J.; Lopez-Ferber, M.; !1Possee, R.D. !$#journal Virology (1994) 202:586-605 !$#title The complete DNA sequence of Autographa californica nuclear !1polyhedrosis virus. !$#cross-references MUID:94303173; PMID:8030224 !$#accession H72851 !'##status preliminary !'##molecule_type DNA !'##residues 1-225 ##label AYR !'##cross-references GB:L22858; NID:g510708; PIDN:AAA66646.1; !1PID:g559085 COMMENT The gene is located in a 3-kilobase XbaI genome fragment. COMMENT This protein is required for viral late gene expression. GENETICS !$#gene AcOrf-16 CLASSIFICATION #superfamily Autographa californica nuclear polyhedrosis !1virus DA26 protein KEYWORDS early protein SUMMARY #length 225 #molecular-weight 25910 #checksum 3565 SEQUENCE /// ENTRY WMNV25 #type complete TITLE 25K protein - Autographa californica nuclear polyhedrosis virus (strain E2) ORGANISM #formal_name Autographa californica nuclear polyhedrosis virus, AcMNPV DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jul-1999 ACCESSIONS A31292; A30862 REFERENCE A31292 !$#authors Beames, B.; Summers, M.D. !$#journal Virology (1989) 168:344-353 !$#title Location and nucleotide sequence of the 25K protein missing !1from baculovirus few polyhedra (FP) mutants. !$#cross-references MUID:89130947; PMID:2644735 !$#accession A31292 !'##molecule_type DNA !'##residues 1-212 ##label BEA !'##cross-references GB:M22537; GB:M23428; NID:g332381; PIDN:AAA46679.1; !1PID:g332382 CLASSIFICATION #superfamily nuclear polyhedrosis virus 25K protein SUMMARY #length 212 #molecular-weight 25000 #checksum 4419 SEQUENCE /// ENTRY WMNV15 #type complete TITLE 18.5K protein - Autographa californica nuclear polyhedrosis virus ORGANISM #formal_name Autographa californica nuclear polyhedrosis virus, AcMNPV DATE 30-Jun-1989 #sequence_revision 22-Oct-1999 #text_change 01-Dec-2000 ACCESSIONS B44221; B29891; A72852 REFERENCE A44221 !$#authors Braunagel, S.C.; Daniel, K.D.; Reilly, L.M.; Guarino, L.A.; !1Hong, T.; Summers, M.D. !$#journal Virology (1992) 191:1003-1008 !$#title Sequence, genomic organization of the EcoRI-A fragment of !1Autographa californica nuclear polyhedrosis virus, and !1identification of a viral-encoded protein resembling the !1outer capsid protein VP8 of rotavirus. !$#cross-references MUID:93079853; PMID:1333113 !$#accession B44221 !'##status preliminary !'##molecule_type DNA !'##residues 1-208 ##label BRA !'##cross-references GB:S52569 REFERENCE A93041 !$#authors Guarino, L.A.; Summers, M.D. !$#journal J. Virol. (1988) 62:463-471 !$#title Functional mapping of Autographa californica nuclear !1polyhedrosis virus genes required for late gene expression. !$#cross-references MUID:88091055; PMID:2826808 !$#accession B29891 !'##molecule_type DNA !'##residues 1-163,'K' ##label GUA !'##cross-references GB:M18857; NID:g332482; PIDN:AAA66809.1; !1PID:g808754 REFERENCE A72850 !$#authors Ayres, M.D.; Howard, S.C.; Kuzio, J.; Lopez-Ferber, M.; !1Possee, R.D. !$#journal Virology (1994) 202:586-605 !$#title The complete DNA sequence of Autographa californica nuclear !1polyhedrosis virus. !$#cross-references MUID:94303173; PMID:8030224 !$#accession A72852 !'##status preliminary !'##molecule_type DNA !'##residues 1-163,'K' ##label AYR !'##cross-references GB:L22858; NID:g510708; PIDN:AAA66647.1; !1PID:g559086 COMMENT The gene is located in a 3-kilobase XbaI genome fragment. COMMENT This protein is required for viral late gene expression. GENETICS !$#gene AcOrf-17 CLASSIFICATION #superfamily Autographa californica nuclear polyhedrosis !1virus 18.5K protein KEYWORDS early protein SUMMARY #length 208 #molecular-weight 23741 #checksum 4926 SEQUENCE /// ENTRY WMNV49 #type complete TITLE 40.9K protein - Autographa californica nuclear polyhedrosis virus ORGANISM #formal_name Autographa californica nuclear polyhedrosis virus, AcMNPV DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jul-1999 ACCESSIONS C29891 REFERENCE A93041 !$#authors Guarino, L.A.; Summers, M.D. !$#journal J. Virol. (1988) 62:463-471 !$#title Functional mapping of Autographa californica nuclear !1polyhedrosis virus genes required for late gene expression. !$#cross-references MUID:88091055; PMID:2826808 !$#accession C29891 !'##molecule_type DNA !'##residues 1-353 ##label GUA !'##cross-references GB:M18857; NID:g332482; PIDN:AAA66810.1; !1PID:g808755 COMMENT The gene is located in a 3-kilobase XbaI genome fragment. COMMENT This protein is required for viral late gene expression. CLASSIFICATION #superfamily Autographa californica nuclear polyhedrosis !1virus 40.9K protein KEYWORDS early protein SUMMARY #length 353 #molecular-weight 40866 #checksum 2165 SEQUENCE /// ENTRY VCNVL1 #type complete TITLE major capsid protein - Autographa californica nuclear polyhedrosis virus ORGANISM #formal_name Autographa californica nuclear polyhedrosis virus, AcMNPV #note host Autographa californica (alfalfa looper); dsDNA virus DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 24-Nov-1999 ACCESSIONS A31476; B72861 REFERENCE A31476 !$#authors Thiem, S.M.; Miller, L.K. !$#journal J. Virol. (1989) 63:2008-2018 !$#title Identification, sequence, and transcriptional mapping of the !1major capsid protein gene of the baculovirus Autographa !1californica nuclear polyhedrosis virus. !$#cross-references MUID:89199756; PMID:2649691 !$#accession A31476 !'##molecule_type DNA !'##residues 1-347 ##label THI !'##cross-references GB:M22978; NID:g348685; PIDN:AAA02580.1; !1PID:g332394 !'##experimental_source strain L-1 REFERENCE A72850 !$#authors Ayres, M.D.; Howard, S.C.; Kuzio, J.; Lopez-Ferber, M.; !1Possee, R.D. !$#journal Virology (1994) 202:586-605 !$#title The complete DNA sequence of Autographa californica nuclear !1polyhedrosis virus. !$#cross-references MUID:94303173; PMID:8030224 !$#accession B72861 !'##status preliminary !'##molecule_type DNA !'##residues 1-347 ##label AYR !'##cross-references GB:L22858; NID:g510708; PIDN:AAA66719.1; !1PID:g559158 GENETICS !$#gene Ac-vp39 CLASSIFICATION #superfamily baculovirus major capsid protein KEYWORDS capsid protein; coat protein; late protein SUMMARY #length 347 #molecular-weight 38951 #checksum 5942 SEQUENCE /// ENTRY VCNVP1 #type complete TITLE major capsid protein - Orgyia pseudotsugata multicapsid nuclear polyhedrosis virus ORGANISM #formal_name Orgyia pseudotsugata multicapsid nuclear polyhedrosis virus, OpMNPV #note host Orgyia pseudotsugata (Douglas-fir tussock moth) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS A31293; A34216 REFERENCE A31293 !$#authors Blissard, G.W.; Quant-Russell, R.L.; Rohrmann, G.F.; !1Beaudreau, G.S. !$#journal Virology (1989) 168:354-362 !$#title Nucleotide sequence, transcriptional mapping, and temporal !1expression of the gene encoding p39, a major structural !1protein of the multicapsid nuclear polyhedrosis virus of !1Orgyia pseudotsugata. !$#cross-references MUID:89130948; PMID:2644736 !$#accession A31293 !'##molecule_type mRNA !'##residues 1-351 ##label BLI !'##cross-references GB:M21042; NID:g332523; PIDN:AAA46688.1; !1PID:g332524 REFERENCE A34216 !$#authors Gross, C.H.; Rohrmann, G.F. !$#journal BioTechniques (1990) 8:196-202 !$#title Mapping unprocessed epitopes using deletion mutagenesis of !1gene fusions. !$#cross-references MUID:90198269; PMID:1690561 !$#accession A34216 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 45-108 ##label GRO CLASSIFICATION #superfamily baculovirus major capsid protein KEYWORDS capsid protein; coat protein; glycoprotein; late protein FEATURE !$235 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 351 #molecular-weight 39462 #checksum 2256 SEQUENCE /// ENTRY JQ1582 #type complete TITLE major capsid protein - Lymantria dispar nuclear polyhedrosis virus ALTERNATE_NAMES coat protein; p39 protein ORGANISM #formal_name Lymantria dispar nuclear polyhedrosis virus, LdMNPV DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jun-2000 ACCESSIONS JQ1582 REFERENCE JQ1582 !$#authors Bjornson, R.M.; Rohrmann, G.F. !$#journal J. Gen. Virol. (1992) 73:1505-1508 !$#title Nucleotide sequence of the p39-capsid gene region of the !1lymantria dispar nuclear polyhedrosis virus. !$#cross-references MUID:92300346; PMID:1607869 !$#accession JQ1582 !'##molecule_type DNA !'##residues 1-356 ##label BJO !'##cross-references GB:D10835; NID:g221989; PIDN:BAA19869.1; !1PID:g2077949 CLASSIFICATION #superfamily baculovirus major capsid protein KEYWORDS capsid protein; coat protein; glycoprotein; late protein FEATURE !$74,153,295 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 356 #molecular-weight 39640 #checksum 6274 SEQUENCE /// ENTRY VCNV87 #type complete TITLE p87 capsid protein - Orgyia pseudotsugata multicapsid nuclear polyhedrosis virus ORGANISM #formal_name Orgyia pseudotsugata multicapsid nuclear polyhedrosis virus, OpMNPV #note host Orgyia pseudotsugata (Douglas-fir tussock moth) DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jun-2000 ACCESSIONS A34602 REFERENCE A34602 !$#authors Mueller, R.; Pearson, M.N.; Russell, R.L.Q.; Rohrmann, G.F. !$#journal Virology (1990) 176:133-144 !$#title A capsid-associated protein of the multicapsid nuclear !1polyhedrosis virus of Orgyia pseudotsugata: genetic !1location, sequence, transcriptional mapping, and !1immunocytochemical characterization. !$#cross-references MUID:90232722; PMID:2184573 !$#accession A34602 !'##molecule_type DNA !'##residues 1-624 ##label MUE !'##cross-references GB:D13959; GB:D00514; NID:g222193; PIDN:BAA03061.1; !1PID:g222199 !'##note the authors translated the codon TAC for residue 281 as Thr CLASSIFICATION #superfamily baculovirus p87 capsid protein KEYWORDS capsid protein; tandem repeat FEATURE !$256-280 #region 12-residue repeats (P-L-Q-E/ !8D-Q-M-P-P-Q-T-P-A)\ !$281-306,312-324 #region 13-residue repeats !8(A-Q-T-P-A-Q-Q-P-S-Q-P-T-P) SUMMARY #length 624 #molecular-weight 70696 #checksum 223 SEQUENCE /// ENTRY VCNVH3 #type complete TITLE capsid-associated protein - Autographa californica nuclear polyhedrosis virus ORGANISM #formal_name Autographa californica nuclear polyhedrosis virus, AcMNPV DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 24-Nov-1999 ACCESSIONS A43376; A72863; S27897 REFERENCE A43376 !$#authors Lu, A.; Carstens, E.B. !$#journal Virology (1992) 190:201-209 !$#title Nucleotide sequence and transcriptional analysis of the p80 !1gene of Autographa californica nuclear polyhedrosis virus: a !1homologue of the Orgyia pseudotsugata nuclear polyhedrosis !1virus capsid-associated gene. !$#cross-references MUID:92410596; PMID:1529529 !$#accession A43376 !'##molecule_type DNA !'##residues 1-691 ##label LUA !'##cross-references GB:M94914; NID:g332467; PIDN:AAA46732.1; !1PID:g332469 !'##experimental_source strain HR3 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1992 REFERENCE A72850 !$#authors Ayres, M.D.; Howard, S.C.; Kuzio, J.; Lopez-Ferber, M.; !1Possee, R.D. !$#journal Virology (1994) 202:586-605 !$#title The complete DNA sequence of Autographa californica nuclear !1polyhedrosis virus. !$#cross-references MUID:94303173; PMID:8030224 !$#accession A72863 !'##status preliminary !'##molecule_type DNA !'##residues 1-691 ##label AYR !'##cross-references GB:L22858; NID:g510708; PIDN:AAA66734.1; !1PID:g559173 GENETICS !$#gene p80; Ac-vp80 !$#map_position 67.2-68.5 CLASSIFICATION #superfamily baculovirus p87 capsid protein KEYWORDS capsid protein; glycoprotein FEATURE !$2,71,102,319 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 691 #molecular-weight 79878 #checksum 6228 SEQUENCE /// ENTRY VGNVAC #type complete TITLE major envelope glycoprotein - Autographa californica nuclear polyhedrosis virus (isolate HR3) ORGANISM #formal_name Autographa californica nuclear polyhedrosis virus, AcMNPV #note host Autographa californica (alfalfa looper) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS A31883 REFERENCE A31883 !$#authors Whitford, M.; Stewart, S.; Kuzio, J.; Faulkner, P. !$#journal J. Virol. (1989) 63:1393-1399 !$#title Identification and sequence analysis of a gene encoding !1gp67, an abundant envelope glycoprotein of the baculovirus !1Autographa californica nuclear polyhedrosis virus. !$#cross-references MUID:89125735; PMID:2644449 !$#accession A31883 !'##molecule_type DNA !'##residues 1-529 ##label WHI !'##cross-references GB:M25420; NID:g293985; PIDN:AAA72759.1; !1PID:g293986 CLASSIFICATION #superfamily baculovirus major envelope glycoprotein KEYWORDS envelope protein; glycoprotein; transmembrane protein FEATURE !$5,177,215,372,402, !$443 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 529 #molecular-weight 60622 #checksum 4665 SEQUENCE /// ENTRY VGNVPC #type complete TITLE major envelope glycoprotein precursor - Orgyia pseudotsugata multicapsid nuclear polyhedrosis virus ORGANISM #formal_name Orgyia pseudotsugata multicapsid nuclear polyhedrosis virus, OpMNPV #note host Orgyia pseudotsugata (Douglas-fir tussock moth) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS A30232; A30855 REFERENCE A30232 !$#authors Blissard, G.W.; Rohrmann, G.F. !$#journal Virology (1989) 170:537-555 !$#title Location, sequence, transcriptional mapping, and temporal !1expression of the gp64 envelope glycoprotein gene of the !1Orgyia pseudotsugata multicapsid nuclear polyhedrosis virus. !$#cross-references MUID:89268475; PMID:2658304 !$#accession A30232 !'##molecule_type mRNA !'##residues 1-509 ##label BLI !'##cross-references GB:M22446; NID:g332525; PIDN:AAA46693.1; !1PID:g332526 CLASSIFICATION #superfamily baculovirus major envelope glycoprotein KEYWORDS envelope protein; glycoprotein; transmembrane protein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-509 #product major envelope glycoprotein #status !8predicted #label MEG\ !$486-502 #domain transmembrane #status predicted #label TMM\ !$156,189,194,351, !$381,423,474 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 509 #molecular-weight 58179 #checksum 3425 SEQUENCE /// ENTRY VGIVDH #type complete TITLE envelope glycoprotein - Dhori virus (strain India/1313/61) ORGANISM #formal_name Dhori virus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS A34679 REFERENCE A34679 !$#authors Freedman-Faulstich, E.Z.; Fuller, F.J. !$#journal Virology (1990) 175:10-18 !$#title Nucleotide sequence of the tick-borne, orthomyxo-like Dhori/ !1Indian/1313/61 virus envelope gene. !$#cross-references MUID:90177204; PMID:2309437 !$#accession A34679 !'##molecule_type mRNA !'##residues 1-521 ##label FRE !'##cross-references EMBL:M34002; NID:g335189; PIDN:AAA47907.1; !1PID:g335190 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily baculovirus major envelope glycoprotein KEYWORDS envelope protein; glycoprotein; transmembrane protein FEATURE !$44,158,189,396 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 521 #molecular-weight 58675 #checksum 1216 SEQUENCE /// ENTRY VGIVTH #type complete TITLE envelope glycoprotein - Thogoto virus (strain SiAr126) ALTERNATE_NAMES surface glycoprotein 75 ORGANISM #formal_name Thogoto virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS A40821 REFERENCE A40821 !$#authors Morse, M.A.; Marriott, A.C.; Nuttall, P.A. !$#journal Virology (1992) 186:640-646 !$#title The glycoprotein of Thogoto virus (a tick-borne !1orthomyxo-like virus) is related to the baculovirus !1glycoprotein gp64. !$#cross-references MUID:92124738; PMID:1733105 !$#accession A40821 !'##molecule_type genomic RNA !'##residues 1-512 ##label MOR !'##cross-references GB:M77280; NID:g335213; PIDN:AAA47918.1; !1PID:g335214 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily baculovirus major envelope glycoprotein KEYWORDS envelope protein; glycoprotein; transmembrane protein FEATURE !$185,263,289,378,416 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 512 #molecular-weight 57550 #checksum 454 SEQUENCE /// ENTRY JQ1747 #type complete TITLE membrane protein - Dhori virus (strain India/1313/61) ORGANISM #formal_name Dhori virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS JQ1747; S27904 REFERENCE JQ1747 !$#authors Clay, W.C.; Fuller, F.J. !$#journal J. Gen. Virol. (1992) 73:2609-2616 !$#title Nucleotide sequence of the tick-borne orthomyxo-like Dhori/ !1India/1313/61 virus membrane protein gene. !$#cross-references MUID:93019015; PMID:1402803 !$#accession JQ1747 !'##molecule_type genomic RNA !'##residues 1-270 ##label CLA !'##cross-references GB:M95567; NID:g323663; PIDN:AAA42966.1; !1PID:g323664 CLASSIFICATION #superfamily Dhori virus membrane protein KEYWORDS membrane protein SUMMARY #length 270 #molecular-weight 30458 #checksum 4670 SEQUENCE /// ENTRY VMNVPC #type complete TITLE 32K polyhedral envelope protein - Orgyia pseudotsugata multicapsid nuclear polyhedrosis virus ORGANISM #formal_name Orgyia pseudotsugata multicapsid nuclear polyhedrosis virus, OpMNPV #note host Orgyia pseudotsugata (Douglas-fir tussock moth) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jun-2000 ACCESSIONS A30120; C30857; JT0430 REFERENCE A30120 !$#authors Gombart, A.F.; Pearson, M.N.; Rohrmann, G.F.; Beaudreau, !1G.S. !$#journal Virology (1989) 169:182-193 !$#title A baculovirus polyhedral envelope-associated protein: !1genetic location, nucleotide sequence, and !1immunocytochemical characterization. !$#cross-references MUID:89163253; PMID:2646825 !$#accession A30120 !'##molecule_type DNA !'##residues 1-297 ##label GOM !'##cross-references GB:D13796; NID:g222210; PIDN:BAA02951.1; !1PID:g222212 GENETICS !$#map_position 87.70 min CLASSIFICATION #superfamily baculovirus polyhedral envelope protein KEYWORDS envelope protein; tandem repeat FEATURE !$112-116,117-121 #region 5-residue repeats SUMMARY #length 297 #molecular-weight 32378 #checksum 6576 SEQUENCE /// ENTRY JQ1559 #type complete TITLE polyhedron envelope protein - Lymantria dispar nuclear polyhedrosis virus ORGANISM #formal_name Lymantria dispar nuclear polyhedrosis virus, LdMNPV #note host Lymantria dispar (gypsy moth) DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jun-2000 ACCESSIONS JQ1559 REFERENCE PQ0339 !$#authors Bjornson, R.M.; Rohrmann, G.F. !$#journal J. Gen. Virol. (1992) 73:1499-1504 !$#title Nucleotide sequence of the polyhedron envelope protein gene !1region of the Lymantria dispar nuclear polyhedrosis virus. !$#cross-references MUID:92300345; PMID:1607868 !$#accession JQ1559 !'##molecule_type DNA !'##residues 1-312 ##label BJO !'##cross-references GB:D37947; GB:D10836; NID:g532333; PIDN:BAA07164.1; !1PID:g221993 CLASSIFICATION #superfamily baculovirus polyhedral envelope protein KEYWORDS envelope protein SUMMARY #length 312 #molecular-weight 33827 #checksum 566 SEQUENCE /// ENTRY WMNV38 #type complete TITLE PE-38 protein - Orgyia pseudotsugata multicapsid nuclear polyhedrosis virus ORGANISM #formal_name Orgyia pseudotsugata multicapsid nuclear polyhedrosis virus, OpMNPV DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS A42191 REFERENCE A42191 !$#authors Theilmann, D.A.; Stewart, S. !$#journal Virology (1992) 187:97-106 !$#title Tandemly repeated sequence at the 3' end of the IE-2 gene of !1the baculovirus Orgyia pseudotsugata multicapsid nuclear !1polyhedrosis virus is an enhancer element. !$#cross-references MUID:92142537; PMID:1736547 !$#accession A42191 !'##molecule_type DNA !'##residues 1-307 ##label THE !'##cross-references GB:M83827; NID:g332540; PIDN:AAA46750.1; !1PID:g332542 CLASSIFICATION #superfamily Orgyia pseudotsugata nuclear polyhedrosis virus !1PE-38 protein KEYWORDS DNA binding; early protein SUMMARY #length 307 #molecular-weight 34714 #checksum 9723 SEQUENCE /// ENTRY A43681 #type complete TITLE immediate-early protein PE-38 - Autographa californica nuclear polyhedrosis virus ORGANISM #formal_name Autographa californica nuclear polyhedrosis virus, AcMNPV DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS A43681 REFERENCE A43681 !$#authors Krappa, R.; Knebel-Moersdorf, D. !$#journal J. Virol. (1991) 65:805-812 !$#title Identification of the very early transcribed baculovirus !1gene PE-38. !$#cross-references MUID:91101290; PMID:1987375 !$#accession A43681 !'##molecule_type DNA !'##residues 1-321 ##label KRA !'##cross-references GB:M62488; NID:g332470; PIDN:AAA46733.1; !1PID:g332471 CLASSIFICATION #superfamily Orgyia pseudotsugata nuclear polyhedrosis virus !1PE-38 protein KEYWORDS DNA binding; immediate-early protein SUMMARY #length 321 #molecular-weight 37524 #checksum 7426 SEQUENCE /// ENTRY WMNV41 #type complete TITLE glycoprotein gp41 - Autographa californica nuclear polyhedrosis virus (isolate HR3) ORGANISM #formal_name Autographa californica nuclear polyhedrosis virus, AcMNPV DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS A42738 REFERENCE A42738 !$#authors Whitford, M.; Faulkner, P. !$#journal J. Virol. (1992) 66:4763-4768 !$#title Nucleotide sequence and transcriptional analysis of a gene !1encoding gp41, a structural glycoprotein of the baculovirus !1Autographa californica nuclear polyhedrosis virus. !$#cross-references MUID:92333656; PMID:1629955 !$#accession A42738 !'##molecule_type DNA !'##residues 1-354 ##label WHI !'##cross-references GB:M86592; NID:g293983; PIDN:AAA46695.1; !1PID:g293984 CLASSIFICATION #superfamily Autographa californica nuclear polyhedrosis !1virus glycoprotein gp41 KEYWORDS glycoprotein; late protein FEATURE !$128 #binding_site carbohydrate (Thr) (covalent) #status !8predicted SUMMARY #length 354 #molecular-weight 39574 #checksum 3253 SEQUENCE /// ENTRY A44278 #type complete TITLE structural protein p40 - Helicoverpa zea nuclear polyhedrosis virus (isolate HzS-15) ORGANISM #formal_name Helicoverpa zea nuclear polyhedrosis virus, HzSNPV DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS A44278 REFERENCE A44278 !$#authors Ma, S.W.; Corsaro, B.G.; Klebba, P.E.; Fraser, M.J. !$#journal Virology (1993) 192:224-233 !$#title Cloning and sequence analysis of a p40 structural protein !1gene of Helicoverpa zea nuclear polyhedrosis virus. !$#cross-references MUID:93297109; PMID:8517018 !$#accession A44278 !'##molecule_type DNA !'##residues 1-322 ##label MAA !'##cross-references GB:L04747; NID:g332517; PIDN:AAA46747.1; !1PID:g332518 CLASSIFICATION #superfamily Autographa californica nuclear polyhedrosis !1virus glycoprotein gp41 KEYWORDS late protein SUMMARY #length 322 #molecular-weight 36564 #checksum 3472 SEQUENCE /// ENTRY WMNVTN #type complete TITLE 104K glycoprotein - Trichoplusia ni granulosis virus ORGANISM #formal_name Trichoplusia ni granulosis virus, TnGV DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jun-2000 ACCESSIONS JQ1328 REFERENCE JQ1328 !$#authors Hashimoto, Y.; Corsaro, B.G.; Granados, R.R. !$#journal J. Gen. Virol. (1991) 72:2645-2651 !$#title Location and nucleotide sequence of the gene encoding the !1viral enhancing factor of the Trichoplusia ni granulosis !1virus. !$#cross-references MUID:92044434; PMID:1940861 !$#accession JQ1328 !'##molecule_type DNA !'##residues 1-901 ##label HAS !'##cross-references GB:D12617; NID:g221443; PIDN:BAA02141.1; !1PID:g221444 !'##note the authors translated the codon CTA for residue 12 as Val COMMENT This protein is involved in disruption of the peritrophic !1membrane and fusion of nucleocapsids with midgut cells. CLASSIFICATION #superfamily Trichoplusia ni granulosis virus 104K !1glycoprotein KEYWORDS glycoprotein FEATURE !$65,265,306,339,349, !$540,594,595,621, !$642,683,698 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 901 #molecular-weight 104321 #checksum 2723 SEQUENCE /// ENTRY DNPDPW #type complete TITLE repeat element protein - Campoletis sonorensis virus ORGANISM #formal_name Campoletis sonorensis virus, CsV #note host Campoletis sonorensis (parasitic wasp); Heliothis virescens DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS A31823 REFERENCE A31823 !$#authors Theilmann, D.A.; Summers, M.D. !$#journal Virology (1988) 167:329-341 !$#title Identification and comparison of Campoletis sonorensis virus !1transcripts expressed from four genomic segments in the !1insect hosts Campoletis sonorensis and Heliothis virescens. !$#cross-references MUID:89073734; PMID:3201745 !$#accession A31823 !'##molecule_type mRNA !'##residues 1-235 ##label THE !'##cross-references GB:M23437; GB:M16998; NID:g323408; PIDN:AAA42923.1; !1PID:g323409 COMMENT The genome of this virus consists of at least 28 closed !1circular superhelical DNA segments; three of them contain !1homologous DNA sequences that code for one or several !1tandem-repeated element proteins. CLASSIFICATION #superfamily parasitic wasp virus repeat element protein FEATURE !$57-235 #domain repeat element #label RPE SUMMARY #length 235 #molecular-weight 28044 #checksum 4181 SEQUENCE /// ENTRY Q4ADB2 #type complete TITLE early E4 17K protein 1 - human adenovirus 2 CONTAINS early E4 10K protein ORGANISM #formal_name Mastadenovirus h2 #common_name human adenovirus 2 #note host Homo sapiens (man) DATE 02-Apr-1982 #sequence_revision 02-Apr-1982 #text_change 12-Apr-1996 ACCESSIONS A03804 REFERENCE A93733 !$#authors Herisse, J.; Rigolet, M.; Dupont de Dinechin, S.; Galibert, !1F. !$#journal Nucleic Acids Res. (1981) 9:4023-4042 !$#title Nucleotide sequence of adenovirus 2 DNA fragment encoding !1for the carboxylic region of the fiber protein and the !1entire E4 region. !$#cross-references MUID:82059444; PMID:6985482 !$#accession A03804 !'##molecule_type DNA !'##residues 1-153 ##label HER !'##note these probable proteins and the introns in the coding regions !1were assigned by correlating EM data, S1 digestion studies, !1and the consensus sequences for intron splicing GENETICS !$#map_position 91.8-95.2 !$#introns 61/3 CLASSIFICATION #superfamily adenovirus early E4 17K protein KEYWORDS early protein FEATURE !$56-153 #product early E4 10K protein #status predicted !8#label TPP SUMMARY #length 153 #molecular-weight 17404 #checksum 5366 SEQUENCE /// ENTRY Q4ADC2 #type complete TITLE early E4 34K protein - human adenovirus 2 ORGANISM #formal_name Mastadenovirus h2 #common_name human adenovirus 2 #note host Homo sapiens (man) DATE 02-Apr-1982 #sequence_revision 02-Apr-1982 #text_change 04-Mar-1994 ACCESSIONS A03805 REFERENCE A93733 !$#authors Herisse, J.; Rigolet, M.; Dupont de Dinechin, S.; Galibert, !1F. !$#journal Nucleic Acids Res. (1981) 9:4023-4042 !$#title Nucleotide sequence of adenovirus 2 DNA fragment encoding !1for the carboxylic region of the fiber protein and the !1entire E4 region. !$#cross-references MUID:82059444; PMID:6985482 !$#accession A03805 !'##molecule_type DNA !'##residues 1-294 ##label HER !'##note this probable protein was assigned by correlating EM data and !1S1 digestion studies GENETICS !$#map_position 92.6-95.2 CLASSIFICATION #superfamily adenovirus early E4 34K protein KEYWORDS early protein SUMMARY #length 294 #molecular-weight 34116 #checksum 8260 SEQUENCE /// ENTRY Q4ADM1 #type complete TITLE early E4 33K protein - mouse adenovirus 1 ORGANISM #formal_name Mastadenovirus mus1 #common_name mouse adenovirus 1 #note host Mus musculus (house mouse) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 04-Mar-1994 ACCESSIONS A38519 REFERENCE A38519 !$#authors Ball, A.O.; Beard, C.W.; Villegas, P.; Spindler, K.R. !$#journal Virology (1991) 180:257-265 !$#title Early region 4 sequence and biological comparison of two !1isolates of mouse adenovirus type 1. !$#cross-references MUID:91082417; PMID:1845825 !$#accession A38519 !'##molecule_type DNA !'##residues 1-288 ##label BAL !'##cross-references GB:M37187 CLASSIFICATION #superfamily adenovirus early E4 34K protein KEYWORDS early protein SUMMARY #length 288 #molecular-weight 32888 #checksum 8764 SEQUENCE /// ENTRY Q4ADD2 #type complete TITLE early E4 13K protein - human adenovirus 2 ORGANISM #formal_name Mastadenovirus h2 #common_name human adenovirus 2 #note host Homo sapiens (man) DATE 02-Apr-1982 #sequence_revision 02-Apr-1982 #text_change 04-Mar-1994 ACCESSIONS A03806 REFERENCE A93733 !$#authors Herisse, J.; Rigolet, M.; Dupont de Dinechin, S.; Galibert, !1F. !$#journal Nucleic Acids Res. (1981) 9:4023-4042 !$#title Nucleotide sequence of adenovirus 2 DNA fragment encoding !1for the carboxylic region of the fiber protein and the !1entire E4 region. !$#cross-references MUID:82059444; PMID:6985482 !$#accession A03806 !'##molecule_type DNA !'##residues 1-114 ##label HER !'##note this probable protein was assigned by correlating EM data and !1S1 digestion studies GENETICS !$#map_position 95.0-96.0 CLASSIFICATION #superfamily adenovirus early E4 13K protein KEYWORDS early protein SUMMARY #length 114 #molecular-weight 13321 #checksum 5762 SEQUENCE /// ENTRY Q4ADE2 #type complete TITLE early E4 11K protein - human adenovirus 2 ORGANISM #formal_name Mastadenovirus h2 #common_name human adenovirus 2 #note host Homo sapiens (man) DATE 02-Apr-1982 #sequence_revision 02-Apr-1982 #text_change 04-Mar-1994 ACCESSIONS A03807 REFERENCE A93733 !$#authors Herisse, J.; Rigolet, M.; Dupont de Dinechin, S.; Galibert, !1F. !$#journal Nucleic Acids Res. (1981) 9:4023-4042 !$#title Nucleotide sequence of adenovirus 2 DNA fragment encoding !1for the carboxylic region of the fiber protein and the !1entire E4 region. !$#cross-references MUID:82059444; PMID:6985482 !$#accession A03807 !'##molecule_type DNA !'##residues 1-116 ##label HER !'##note this protein was assigned by correlating EM data and S1 !1digestion studies GENETICS !$#map_position 96.0-97.0 CLASSIFICATION #superfamily adenovirus early E4 11K protein KEYWORDS early protein SUMMARY #length 116 #molecular-weight 13255 #checksum 6011 SEQUENCE /// ENTRY Q4ADE5 #type complete TITLE early E4 11K protein - human adenovirus 5 ORGANISM #formal_name Mastadenovirus h5 #common_name human adenovirus 5 #note host Homo sapiens (man) DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 22-Oct-1999 ACCESSIONS B03807; A03807 REFERENCE A92890 !$#authors Sarnow, P.; Hearing, P.; Anderson, C.W.; Reich, N.; Levine, !1A.J. !$#journal J. Mol. Biol. (1982) 162:565-583 !$#title Identification and characterization of an immunologically !1conserved adenovirus early region 11,000 M-r protein and its !1association with the nuclear matrix. !$#cross-references MUID:83164198; PMID:7166756 !$#accession B03807 !'##molecule_type DNA !'##residues 1-116 ##label SAR !'##cross-references GB:X02998; GB:J01969; GB:J01973; GB:J01975; !1GB:V00028; NID:g58501; PIDN:CAA26757.1; PID:g58502 GENETICS !$#map_position 96.0-97.0 CLASSIFICATION #superfamily adenovirus early E4 11K protein KEYWORDS early protein SUMMARY #length 116 #molecular-weight 13298 #checksum 6308 SEQUENCE /// ENTRY Q4ADG2 #type complete TITLE early E4 31K protein - human adenovirus 2 CONTAINS 14K protein 1; 14K protein 2; 17K protein; 20K protein; 24K protein; 27K protein; 28K protein ORGANISM #formal_name Mastadenovirus h2 #common_name human adenovirus 2 #note host Homo sapiens (man) DATE 02-Apr-1982 #sequence_revision 02-Apr-1982 #text_change 12-Apr-1996 ACCESSIONS A03808 REFERENCE A93733 !$#authors Herisse, J.; Rigolet, M.; Dupont de Dinechin, S.; Galibert, !1F. !$#journal Nucleic Acids Res. (1981) 9:4023-4042 !$#title Nucleotide sequence of adenovirus 2 DNA fragment encoding !1for the carboxylic region of the fiber protein and the !1entire E4 region. !$#cross-references MUID:82059444; PMID:6985482 !$#accession A03808 !'##molecule_type DNA !'##residues 1-283 ##label HER !'##note these proteins and the introns in the coding regions were !1assigned by correlating EM data, S1 digestion studies, and !1the consensus sequences for intron splicing COMMENT The 31K protein sequence is shown. COMMENT The early 14K protein 1 consists of Met-Gln followed by !1residues 122-255. COMMENT The early 14K protein 2 consists of residues 1-121 followed !1by Val-Arg-Gln-Ala-Ser-Asn-Val. GENETICS !$#introns 121/3; 256/1 CLASSIFICATION #superfamily adenovirus E4 protein KEYWORDS early protein FEATURE !$1-255 #product early E4 28K protein #status predicted !8#label EPE\ !$1-121,160-283 #product early E4 27K protein #status predicted !8#label EPA\ !$1-121,223-255 #product early E4 17K protein 2 #status predicted !8#label EBC\ !$1-121,160-255 #product early E4 24K protein #status predicted !8#label EPD\ !$1-121,223-283 #product early E4 20K protein #status predicted !8#label EPB SUMMARY #length 283 #molecular-weight 31846 #checksum 4810 SEQUENCE /// ENTRY Q1AD55 #type complete TITLE early E1B 55K protein I - human adenovirus 5 ORGANISM #formal_name Mastadenovirus h5 #common_name human adenovirus 5 #note host Homo sapiens (man) DATE 02-Apr-1982 #sequence_revision 02-Apr-1982 #text_change 16-Jul-1999 ACCESSIONS A03809 REFERENCE A90814 !$#authors Bos, J.L.; Polder, L.J.; Bernards, R.; Schrier, P.I.; van !1den Elsen, P.J.; van der Eb, A.J.; van Ormondt, H. !$#journal Cell (1981) 27:121-131 !$#title The 2.2 kb E1b mRNA of human Ad12 and Ad5 codes for two !1tumor antigens starting at different AUG triplets. !$#cross-references MUID:82115327; PMID:7326748 !$#accession A03809 !'##molecule_type mRNA !'##residues 1-496 ##label BOS !'##cross-references GB:X02996; GB:J01967; GB:J01968; GB:J01970; !1GB:J01971; GB:J01972; GB:J01974; GB:J01976; GB:J01977; !1GB:J01978; GB:J01979; GB:K00515; GB:V00025; GB:V00026; !1GB:V00027; GB:V00029; NID:g58484; PIDN:CAA26743.1; !1PID:g58491 GENETICS !$#map_position 5.5-9.6 CLASSIFICATION #superfamily adenovirus early E1B protein I KEYWORDS early protein SUMMARY #length 496 #molecular-weight 54999 #checksum 2702 SEQUENCE /// ENTRY Q1AD52 #type complete TITLE early E1B 55K protein I - human adenovirus 2 ORGANISM #formal_name Mastadenovirus h2 #common_name human adenovirus 2 #note host Homo sapiens (man) DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 04-Mar-1994 ACCESSIONS B03809; A03809 REFERENCE A92351 !$#authors Gingeras, T.R.; Sciaky, D.; Gelinas, R.E.; Bing-Dong, J.; !1Yen, C.E.; Kelly, M.M.; Bullock, P.A.; Parsons, B.L.; !1O'Neill, K.E.; Roberts, R.J. !$#journal J. Biol. Chem. (1982) 257:13475-13491 !$#title Nucleotide sequences from the adenovirus-2 genome. !$#cross-references MUID:83056843; PMID:7142161 !$#accession B03809 !'##molecule_type DNA !'##residues 1-495 ##label GIN GENETICS !$#map_position 5.5-9.6 CLASSIFICATION #superfamily adenovirus early E1B protein I KEYWORDS early protein SUMMARY #length 495 #molecular-weight 54895 #checksum 1799 SEQUENCE /// ENTRY WMAD55 #type complete TITLE early E1B 55K protein I - human adenovirus 7 ORGANISM #formal_name Mastadenovirus h7 #common_name human adenovirus 7 #note host Homo sapiens (man) DATE 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 16-Jul-1999 ACCESSIONS A03810 REFERENCE A91494 !$#authors Dijkema, R.; Dekker, B.M.M.; van Ormondt, H. !$#journal Gene (1982) 18:143-156 !$#title Gene organization of the transforming region of adenovirus !1type 7 DNA. !$#cross-references MUID:83028529; PMID:6290319 !$#accession A03810 !'##molecule_type DNA !'##residues 1-492 ##label DIJ !'##cross-references GB:X03000; GB:J01981; GB:J01982; GB:J01983; !1GB:J01984; GB:J01985; GB:J01988; GB:J01989; GB:J01990; !1GB:J01992; GB:V00032; GB:V00033; GB:V00038; NID:g58514; !1PIDN:CAA26763.1; PID:g58519 CLASSIFICATION #superfamily adenovirus early E1B protein I KEYWORDS early protein SUMMARY #length 492 #molecular-weight 54702 #checksum 5095 SEQUENCE /// ENTRY WMAD9 #type complete TITLE early E1B 9K protein I - human adenovirus 7 ORGANISM #formal_name Mastadenovirus h7 #common_name human adenovirus 7 #note host Homo sapiens (man) DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 16-Jul-1999 ACCESSIONS A03811 REFERENCE A91494 !$#authors Dijkema, R.; Dekker, B.M.M.; van Ormondt, H. !$#journal Gene (1982) 18:143-156 !$#title Gene organization of the transforming region of adenovirus !1type 7 DNA. !$#cross-references MUID:83028529; PMID:6290319 !$#accession A03811 !'##molecule_type DNA !'##residues 1-88 ##label DIJ !'##cross-references GB:X03000; GB:J01981; GB:J01982; GB:J01983; !1GB:J01984; GB:J01985; GB:J01988; GB:J01989; GB:J01990; !1GB:J01992; GB:V00032; GB:V00033; GB:V00038; NID:g58514; !1PIDN:CAA26761.1; PID:g58520 COMMENT Residues 1-86 are identical with residues 1-86 of the E1B !155K protein I. CLASSIFICATION #superfamily adenovirus early E1B protein I KEYWORDS early protein SUMMARY #length 88 #molecular-weight 9017 #checksum 2946 SEQUENCE /// ENTRY WMADMA #type complete TITLE early E1B 50K protein I - mouse adenovirus 1 ORGANISM #formal_name Mastadenovirus mus1 #common_name mouse adenovirus 1 DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS C31158 REFERENCE A93038 !$#authors Ball, A.O.; Williams, M.E.; Spindler, K.R. !$#journal J. Virol. (1988) 62:3947-3957 !$#title Identification of mouse adenovirus type 1 early region 1: !1DNA sequence and a conserved transactivating function. !$#cross-references MUID:89012162; PMID:3172335 !$#accession C31158 !'##molecule_type DNA !'##residues 1-447 ##label BAL !'##cross-references GB:M22245; GB:J03353; NID:g209746; PIDN:AAA42429.1; !1PID:g209752 CLASSIFICATION #superfamily adenovirus early E1B protein I KEYWORDS early protein SUMMARY #length 447 #molecular-weight 50556 #checksum 3369 SEQUENCE /// ENTRY ERAD24 #type complete TITLE early E1B 54K protein I - human adenovirus 12 ORGANISM #formal_name Mastadenovirus h12 #common_name human adenovirus 12 #note host Homo sapiens (man) DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 16-Jul-1999 ACCESSIONS A03812; B03812; S33930 REFERENCE A93745 !$#authors Kimura, T.; Sawada, Y.; Shinawawa, M.; Shimizu, Y.; Shiroki, !1K.; Shimojo, H.; Sugisaki, H.; Takanami, M.; Uemizu, Y.; !1Fujinaga, K. !$#journal Nucleic Acids Res. (1981) 9:6571-6589 !$#title Nucleotide sequence of the transforming early region E1b of !1adenovirus type 12 DNA: structure and gene organization, and !1comparison with those of adenovirus type 5 DNA. !$#cross-references MUID:82105565; PMID:6275367 !$#accession A03812 !'##molecule_type DNA !'##residues 1-482 ##label KIM !'##cross-references GB:X73487; NID:g313361; PIDN:CAA51879.1; !1PID:g313364 REFERENCE A90814 !$#authors Bos, J.L.; Polder, L.J.; Bernards, R.; Schrier, P.I.; van !1den Elsen, P.J.; van der Eb, A.J.; van Ormondt, H. !$#journal Cell (1981) 27:121-131 !$#title The 2.2 kb E1b mRNA of human Ad12 and Ad5 codes for two !1tumor antigens starting at different AUG triplets. !$#cross-references MUID:82115327; PMID:7326748 !$#accession B03812 !'##molecule_type mRNA !'##residues 1-482 ##label BOS REFERENCE S33928 !$#authors Sprengel, J. !$#submission submitted to the EMBL Data Library, June 1993 !$#accession S33930 !'##status preliminary !'##molecule_type DNA !'##residues 1-482 ##label SPR !'##cross-references EMBL:X73487; NID:g313361; PIDN:CAA51879.1; !1PID:g313364 CLASSIFICATION #superfamily adenovirus early E1B protein I KEYWORDS early protein SUMMARY #length 482 #molecular-weight 53935 #checksum 4446 SEQUENCE /// ENTRY WMADP6 #type complete TITLE early E1B 53K protein I - human adenovirus 40 ORGANISM #formal_name Mastadenovirus h40 #common_name human adenovirus 40 DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS C29195 REFERENCE A94383 !$#authors Ishino, M.; Ohashi, Y.; Emoto, T.; Sawada, Y.; Fujinaga, K. !$#journal Virology (1988) 165:95-102 !$#title Characterization of adenovirus type 40 E1 region. !$#cross-references MUID:88265890; PMID:2968714 !$#accession C29195 !'##molecule_type DNA !'##residues 1-475 ##label ISH !'##cross-references GB:M21276; NID:g209763; PIDN:AAA42444.1; !1PID:g209767 CLASSIFICATION #superfamily adenovirus early E1B protein I KEYWORDS early protein SUMMARY #length 475 #molecular-weight 53045 #checksum 3526 SEQUENCE /// ENTRY WMADF6 #type complete TITLE early E1B 52K protein I - human adenovirus 41 ORGANISM #formal_name Mastadenovirus h41 #common_name human adenovirus 41 DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jul-1999 ACCESSIONS F27333; B40249 REFERENCE A27333 !$#authors van Loon, A.E.; Ligtenberg, M.; Reemst, A.M.C.B.; !1Sussenbach, J.S.; Rozijn, T.H. !$#journal Gene (1987) 58:109-126 !$#title Structure and organization of the left-terminal DNA regions !1of fastidious adenovirus types 40 and 41. !$#cross-references MUID:88084437; PMID:2961652 !$#accession F27333 !'##molecule_type DNA !'##residues 1-472 ##label VAN !'##cross-references GB:M18289; NID:g209778; PIDN:AAA42452.1; !1PID:g209781 REFERENCE A40249 !$#authors Allard, A.; Wadell, G. !$#journal Virology (1992) 188:319-330 !$#title The E1B transcription map of the enteric adenovirus type 41. !$#cross-references MUID:92230230; PMID:1533079 !$#accession B40249 !'##molecule_type DNA !'##residues 1-54;57-233,'P',235-472 ##label ALL !'##cross-references GB:M87544 CLASSIFICATION #superfamily adenovirus early E1B protein I KEYWORDS early protein SUMMARY #length 472 #molecular-weight 52157 #checksum 4733 SEQUENCE /// ENTRY ERADC2 #type complete TITLE early E1B 49K protein I - canine adenovirus 2 (strain Tront A 26-61) ORGANISM #formal_name Mastadenovirus can2 #common_name canine adenovirus 2 #note host Canis lupis familiaris (dog) DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS C34165 REFERENCE A34165 !$#authors Shibata, R.; Shinagawa, M.; Iida, Y.; Tsukiyama, T. !$#journal Virology (1989) 172:460-467 !$#title Nucleotide sequence of E1 region of canine adenovirus type !12. !$#cross-references MUID:90021176; PMID:2800332 !$#accession C34165 !'##molecule_type DNA !'##residues 1-438 ##label SHI !'##cross-references GB:J04368; NID:g209884; PIDN:AAA42472.1; !1PID:g209887 CLASSIFICATION #superfamily adenovirus early E1B protein I KEYWORDS early protein SUMMARY #length 438 #molecular-weight 48865 #checksum 6411 SEQUENCE /// ENTRY ERADT4 #type complete TITLE early E1B 44K protein I - tree shrew adenovirus ORGANISM #formal_name Mastadenovirus tup #common_name tree shrew adenovirus DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 21-Jul-2000 ACCESSIONS A03813 REFERENCE A91522 !$#authors Flugel, R.M.; Bannert, H.; Suhai, S.; Darai, G. !$#journal Gene (1985) 34:73-80 !$#title The nucleotide sequence of the early region of the Tupaia !1adenovirus DNA corresponding to the oncogenic region E1b of !1human adenovirus 7. !$#cross-references MUID:85232053; PMID:3159623 !$#accession A03813 !'##molecule_type DNA !'##residues 1-391 ##label FLU !'##cross-references GB:M10054; NID:g210025; PIDN:AAA42531.1; !1PID:g210027 !'##note the host is identified as Tupaia belangeri CLASSIFICATION #superfamily adenovirus early E1B protein I KEYWORDS early protein SUMMARY #length 391 #molecular-weight 43541 #checksum 6920 SEQUENCE /// ENTRY Q1AD25 #type complete TITLE early E1B 21K protein II - human adenovirus 5 ORGANISM #formal_name Mastadenovirus h5 #common_name human adenovirus 5 #note host Homo sapiens (man) DATE 02-Apr-1982 #sequence_revision 02-Apr-1982 #text_change 16-Jun-2000 ACCESSIONS A03814 REFERENCE A90814 !$#authors Bos, J.L.; Polder, L.J.; Bernards, R.; Schrier, P.I.; van !1den Elsen, P.J.; van der Eb, A.J.; van Ormondt, H. !$#journal Cell (1981) 27:121-131 !$#title The 2.2 kb E1b mRNA of human Ad12 and Ad5 codes for two !1tumor antigens starting at different AUG triplets. !$#cross-references MUID:82115327; PMID:7326748 !$#accession A03814 !'##molecule_type mRNA !'##residues 1-176 ##label BOS !'##cross-references GB:X02996; GB:J01967; GB:J01968; GB:J01970; !1GB:J01971; GB:J01972; GB:J01974; GB:J01976; GB:J01977; !1GB:J01978; GB:J01979; GB:K00515; GB:V00025; GB:V00026; !1GB:V00027; GB:V00029; NID:g58484; PIDN:CAA26741.1; !1PID:g58490 GENETICS !$#map_position 4.7-6.1 CLASSIFICATION #superfamily adenovirus early E1B protein II KEYWORDS early protein SUMMARY #length 176 #molecular-weight 20614 #checksum 374 SEQUENCE /// ENTRY Q1AD22 #type complete TITLE early E1B 21K protein II - human adenovirus 2 ORGANISM #formal_name Mastadenovirus h2 #common_name human adenovirus 2 #note host Homo sapiens (man) DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 04-Mar-1994 ACCESSIONS B03814; A03814 REFERENCE A92351 !$#authors Gingeras, T.R.; Sciaky, D.; Gelinas, R.E.; Bing-Dong, J.; !1Yen, C.E.; Kelly, M.M.; Bullock, P.A.; Parsons, B.L.; !1O'Neill, K.E.; Roberts, R.J. !$#journal J. Biol. Chem. (1982) 257:13475-13491 !$#title Nucleotide sequences from the adenovirus-2 genome. !$#cross-references MUID:83056843; PMID:7142161 !$#accession B03814 !'##molecule_type DNA !'##residues 1-175 ##label GIN GENETICS !$#map_position 4.7-6.1 CLASSIFICATION #superfamily adenovirus early E1B protein II KEYWORDS early protein SUMMARY #length 175 #molecular-weight 20514 #checksum 9865 SEQUENCE /// ENTRY WMAD21 #type complete TITLE early E1B 21K protein II - human adenovirus 7 ORGANISM #formal_name Mastadenovirus h7 #common_name human adenovirus 7 #note host Homo sapiens (man) DATE 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 16-Jul-1999 ACCESSIONS A03815 REFERENCE A91494 !$#authors Dijkema, R.; Dekker, B.M.M.; van Ormondt, H. !$#journal Gene (1982) 18:143-156 !$#title Gene organization of the transforming region of adenovirus !1type 7 DNA. !$#cross-references MUID:83028529; PMID:6290319 !$#accession A03815 !'##molecule_type DNA !'##residues 1-178 ##label DIJ !'##cross-references GB:X03000; GB:J01981; GB:J01982; GB:J01983; !1GB:J01984; GB:J01985; GB:J01988; GB:J01989; GB:J01990; !1GB:J01992; GB:V00032; GB:V00033; GB:V00038; NID:g58514; !1PIDN:CAA26762.1; PID:g58518 CLASSIFICATION #superfamily adenovirus early E1B protein II KEYWORDS early protein SUMMARY #length 178 #molecular-weight 20574 #checksum 8806 SEQUENCE /// ENTRY WMAD19 #type complete TITLE early E1B 17K protein II - human adenovirus 4 ORGANISM #formal_name Mastadenovirus h4 #common_name human adenovirus 4 #note host Homo sapiens (man) DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 16-Jul-1999 ACCESSIONS B25614 REFERENCE A94347 !$#authors Tokunaga, O.; Yaegashi, T.; Lowe, J.; Dobbs, L.; !1Padmanabhan, R. !$#journal Virology (1986) 155:418-433 !$#title Sequence analysis in the E1 region of adenovirus type 4 DNA. !$#cross-references MUID:87071662; PMID:2947381 !$#accession B25614 !'##molecule_type DNA !'##residues 1-142 ##label TOK !'##cross-references GB:M14918; NID:g209874; PIDN:AAA67093.1; !1PID:g807571 CLASSIFICATION #superfamily adenovirus early E1B protein II KEYWORDS early protein SUMMARY #length 142 #molecular-weight 16817 #checksum 1738 SEQUENCE /// ENTRY ERAD21 #type complete TITLE early E1B 19K protein II - human adenovirus 12 ORGANISM #formal_name Mastadenovirus h12 #common_name human adenovirus 12 #note host Homo sapiens (man) DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 16-Jul-1999 ACCESSIONS A03816; B03816; S33929 REFERENCE A90814 !$#authors Bos, J.L.; Polder, L.J.; Bernards, R.; Schrier, P.I.; van !1den Elsen, P.J.; van der Eb, A.J.; van Ormondt, H. !$#journal Cell (1981) 27:121-131 !$#title The 2.2 kb E1b mRNA of human Ad12 and Ad5 codes for two !1tumor antigens starting at different AUG triplets. !$#cross-references MUID:82115327; PMID:7326748 !$#accession A03816 !'##molecule_type mRNA !'##residues 1-163 ##label BOS REFERENCE A93745 !$#authors Kimura, T.; Sawada, Y.; Shinawawa, M.; Shimizu, Y.; Shiroki, !1K.; Shimojo, H.; Sugisaki, H.; Takanami, M.; Uemizu, Y.; !1Fujinaga, K. !$#journal Nucleic Acids Res. (1981) 9:6571-6589 !$#title Nucleotide sequence of the transforming early region E1b of !1adenovirus type 12 DNA: structure and gene organization, and !1comparison with those of adenovirus type 5 DNA. !$#cross-references MUID:82105565; PMID:6275367 !$#accession B03816 !'##molecule_type DNA !'##residues 1-163 ##label KIM !'##cross-references GB:X73487; NID:g313361; PIDN:CAA51878.1; !1PID:g313363 REFERENCE S33928 !$#authors Sprengel, J. !$#submission submitted to the EMBL Data Library, June 1993 !$#accession S33929 !'##status preliminary !'##molecule_type DNA !'##residues 1-163 ##label SPR !'##cross-references EMBL:X73487; NID:g313361; PIDN:CAA51878.1; !1PID:g313363 CLASSIFICATION #superfamily adenovirus early E1B protein II KEYWORDS early protein SUMMARY #length 163 #molecular-weight 19125 #checksum 9071 SEQUENCE /// ENTRY WMADP5 #type complete TITLE early E1B 20K protein II - human adenovirus 40 ORGANISM #formal_name Mastadenovirus h40 #common_name human adenovirus 40 DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS B29195 REFERENCE A94383 !$#authors Ishino, M.; Ohashi, Y.; Emoto, T.; Sawada, Y.; Fujinaga, K. !$#journal Virology (1988) 165:95-102 !$#title Characterization of adenovirus type 40 E1 region. !$#cross-references MUID:88265890; PMID:2968714 !$#accession B29195 !'##molecule_type DNA !'##residues 1-166 ##label ISH !'##cross-references GB:M21276; NID:g209763; PIDN:AAA42443.1; !1PID:g209766 CLASSIFICATION #superfamily adenovirus early E1B protein II KEYWORDS early protein SUMMARY #length 166 #molecular-weight 18943 #checksum 6903 SEQUENCE /// ENTRY WMADF5 #type complete TITLE early E1B 20K protein II - human adenovirus 41 ORGANISM #formal_name Mastadenovirus h41 #common_name human adenovirus 41 DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jul-1999 ACCESSIONS E27333; A40249 REFERENCE A27333 !$#authors van Loon, A.E.; Ligtenberg, M.; Reemst, A.M.C.B.; !1Sussenbach, J.S.; Rozijn, T.H. !$#journal Gene (1987) 58:109-126 !$#title Structure and organization of the left-terminal DNA regions !1of fastidious adenovirus types 40 and 41. !$#cross-references MUID:88084437; PMID:2961652 !$#accession E27333 !'##molecule_type DNA !'##residues 1-170 ##label VAN !'##cross-references GB:M18289; NID:g209778; PIDN:AAA42451.1; !1PID:g209780 REFERENCE A40249 !$#authors Allard, A.; Wadell, G. !$#journal Virology (1992) 188:319-330 !$#title The E1B transcription map of the enteric adenovirus type 41. !$#cross-references MUID:92230230; PMID:1533079 !$#accession A40249 !'##molecule_type DNA !'##residues 1-156;159-170 ##label ALL !'##cross-references GB:M87544; NID:g209890; PIDN:AAA42474.1; !1PID:g209891 CLASSIFICATION #superfamily adenovirus early E1B protein II KEYWORDS early protein SUMMARY #length 170 #molecular-weight 19618 #checksum 2554 SEQUENCE /// ENTRY Q1ADMA #type complete TITLE early E1B 20K protein II - mouse adenovirus 1 ORGANISM #formal_name Mastadenovirus mus1 #common_name mouse adenovirus 1 DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS B31158 REFERENCE A93038 !$#authors Ball, A.O.; Williams, M.E.; Spindler, K.R. !$#journal J. Virol. (1988) 62:3947-3957 !$#title Identification of mouse adenovirus type 1 early region 1: !1DNA sequence and a conserved transactivating function. !$#cross-references MUID:89012162; PMID:3172335 !$#accession B31158 !'##molecule_type DNA !'##residues 1-175 ##label BAL !'##cross-references GB:M22245; GB:J03353; NID:g209746; PIDN:AAA42428.1; !1PID:g209751 CLASSIFICATION #superfamily adenovirus early E1B protein II KEYWORDS early protein SUMMARY #length 175 #molecular-weight 20000 #checksum 1019 SEQUENCE /// ENTRY C60010 #type complete TITLE early E1B 20K protein II - canine adenovirus 1 ORGANISM #formal_name Mastadenovirus can1 #common_name canine adenovirus 1 #note host Canis lupis familiaris (dog) DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 07-May-1999 ACCESSIONS C60010 REFERENCE A60010 !$#authors Spibey, N.; McClory, R.S.; Cavanagh, H.M.A. !$#journal Virus Res. (1989) 14:241-256 !$#title Identification and nucleotide sequence of the early region 1 !1from canine adenovirus types 1 and 2. !$#cross-references MUID:90163565; PMID:2623943 !$#accession C60010 !'##molecule_type DNA !'##residues 1-169 ##label SPI CLASSIFICATION #superfamily adenovirus early E1B protein II KEYWORDS early protein SUMMARY #length 169 #molecular-weight 19364 #checksum 7497 SEQUENCE /// ENTRY WMADN2 #type complete TITLE early E1B 15K protein II - canine adenovirus 2 (strain Tront A 26-61) ORGANISM #formal_name Mastadenovirus can2 #common_name canine adenovirus 2 #note host Canis lupis familiaris (dog) DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS B34165 REFERENCE A34165 !$#authors Shibata, R.; Shinagawa, M.; Iida, Y.; Tsukiyama, T. !$#journal Virology (1989) 172:460-467 !$#title Nucleotide sequence of E1 region of canine adenovirus type !12. !$#cross-references MUID:90021176; PMID:2800332 !$#accession B34165 !'##molecule_type DNA !'##residues 1-133 ##label SHI !'##cross-references GB:J04368; NID:g209884; PIDN:AAA42471.1; !1PID:g209886 CLASSIFICATION #superfamily adenovirus early E1B protein II KEYWORDS early protein SUMMARY #length 133 #molecular-weight 15219 #checksum 5920 SEQUENCE /// ENTRY D60010 #type complete TITLE early E1B 20K protein II - canine adenovirus 2 ORGANISM #formal_name Mastadenovirus can2 #common_name canine adenovirus 2 #note host Canis lupis familiaris (dog) DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 07-May-1999 ACCESSIONS D60010 REFERENCE A60010 !$#authors Spibey, N.; McClory, R.S.; Cavanagh, H.M.A. !$#journal Virus Res. (1989) 14:241-256 !$#title Identification and nucleotide sequence of the early region 1 !1from canine adenovirus types 1 and 2. !$#cross-references MUID:90163565; PMID:2623943 !$#accession D60010 !'##molecule_type DNA !'##residues 1-170 ##label SPI CLASSIFICATION #superfamily adenovirus early E1B protein II KEYWORDS early protein SUMMARY #length 170 #molecular-weight 19366 #checksum 8396 SEQUENCE /// ENTRY ERADT5 #type complete TITLE early E1B 15K protein II - tree shrew adenovirus ORGANISM #formal_name Mastadenovirus tup #common_name tree shrew adenovirus DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 21-Jul-2000 ACCESSIONS A03817 REFERENCE A91522 !$#authors Flugel, R.M.; Bannert, H.; Suhai, S.; Darai, G. !$#journal Gene (1985) 34:73-80 !$#title The nucleotide sequence of the early region of the Tupaia !1adenovirus DNA corresponding to the oncogenic region E1b of !1human adenovirus 7. !$#cross-references MUID:85232053; PMID:3159623 !$#accession A03817 !'##molecule_type DNA !'##residues 1-137 ##label FLU !'##cross-references GB:M10054; NID:g210025; PIDN:AAA42530.1; !1PID:g210026 !'##note the host is identified as Tupaia belangeri CLASSIFICATION #superfamily adenovirus early E1B protein II KEYWORDS early protein SUMMARY #length 137 #molecular-weight 15117 #checksum 6790 SEQUENCE /// ENTRY ERAD42 #type complete TITLE early E3B 14K protein - human adenovirus 2 ORGANISM #formal_name Mastadenovirus h2 #common_name human adenovirus 2 #note host Homo sapiens (man) DATE 29-Jul-1981 #sequence_revision 08-Oct-1981 #text_change 04-Mar-1994 ACCESSIONS A03818 REFERENCE A93722 !$#authors Herisse, J.; Galibert, F. !$#journal Nucleic Acids Res. (1981) 9:1229-1240 !$#title Nucleotide sequence of the EcoRI E fragment of adenovirus 2 !1genome. !$#cross-references MUID:81198965; PMID:6262722 !$#accession A03818 !'##molecule_type DNA !'##residues 1-128 ##label HER CLASSIFICATION #superfamily adenovirus early E3B 14K protein KEYWORDS early protein SUMMARY #length 128 #molecular-weight 14738 #checksum 9020 SEQUENCE /// ENTRY ERAD29 #type complete TITLE early E3B 14K protein - human adenovirus 3 ALTERNATE_NAMES early E3B 15.3K protein ORGANISM #formal_name Mastadenovirus h3 #common_name human adenovirus 3 DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 16-Jul-1999 ACCESSIONS A27623 REFERENCE A91566 !$#authors Signaes, C.; Akusjaervi, G.; Pettersson, U. !$#journal Gene (1986) 50:173-184 !$#title Region E3 of human adenoviruses; differences between the !1oncogenic adenovirus-3 and the non-oncogenic adenovirus-2. !$#cross-references MUID:87219876; PMID:3582978 !$#accession A27623 !'##molecule_type DNA !'##residues 1-136 ##label SIG !'##cross-references GB:M15952; NID:g209901; PIDN:AAA42489.1; !1PID:g209910 CLASSIFICATION #superfamily adenovirus early E3B 14K protein KEYWORDS early protein SUMMARY #length 136 #molecular-weight 15266 #checksum 8383 SEQUENCE /// ENTRY ERAD74 #type complete TITLE early E3B 15.3K protein - human adenovirus 7 (strain Gomen) ORGANISM #formal_name Mastadenovirus h7 #common_name human adenovirus 7 #note host Homo sapiens (man) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS E31830 REFERENCE A94386 !$#authors Hong, J.S.; Mullis, K.G.; Engler, J.A. !$#journal Virology (1988) 167:545-553 !$#title Characterization of the early region 3 and fiber genes of !1Ad7. !$#cross-references MUID:89073758; PMID:2849239 !$#accession E31830 !'##molecule_type DNA !'##residues 1-135 ##label HON !'##cross-references GB:M23696; NID:g341012; PIDN:AAA53253.1; !1PID:g576460 CLASSIFICATION #superfamily adenovirus early E3B 14K protein KEYWORDS early protein SUMMARY #length 135 #molecular-weight 15363 #checksum 8529 SEQUENCE /// ENTRY ERAD45 #type complete TITLE early E3B 14K protein - human adenovirus 5 ORGANISM #formal_name Mastadenovirus h5 #common_name human adenovirus 5 #note host Homo sapiens (man) DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 16-Jul-1999 ACCESSIONS A03819 REFERENCE A94335 !$#authors Cladaras, C.; Wold, W.S.M. !$#journal Virology (1985) 140:28-43 !$#title DNA sequence of the early E3 transcription unit of !1adenovirus 5. !$#cross-references MUID:85092388; PMID:2981456 !$#accession A03819 !'##molecule_type DNA !'##residues 1-128 ##label CLA !'##cross-references GB:X03002; NID:g58503; PIDN:CAA26787.1; PID:g58510 CLASSIFICATION #superfamily adenovirus early E3B 14K protein KEYWORDS early protein SUMMARY #length 128 #molecular-weight 14598 #checksum 9064 SEQUENCE /// ENTRY ERAD52 #type complete TITLE early E3B 14.5K protein - human adenovirus 2 ORGANISM #formal_name Mastadenovirus h2 #common_name human adenovirus 2 #note host Homo sapiens (man) DATE 29-Jul-1981 #sequence_revision 08-Oct-1981 #text_change 16-Feb-1997 ACCESSIONS A03820 REFERENCE A93722 !$#authors Herisse, J.; Galibert, F. !$#journal Nucleic Acids Res. (1981) 9:1229-1240 !$#title Nucleotide sequence of the EcoRI E fragment of adenovirus 2 !1genome. !$#cross-references MUID:81198965; PMID:6262722 !$#accession A03820 !'##molecule_type DNA !'##residues 1-130 ##label HER CLASSIFICATION #superfamily adenovirus early E3B 14.5K protein KEYWORDS early protein; transmembrane protein SUMMARY #length 130 #molecular-weight 14529 #checksum 5456 SEQUENCE /// ENTRY ERAD28 #type complete TITLE early E3B 14.5K protein - human adenovirus 3 ALTERNATE_NAMES early E3B 15.2K glycoprotein ORGANISM #formal_name Mastadenovirus h3 #common_name human adenovirus 3 DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 16-Jul-1999 ACCESSIONS I29500 REFERENCE A91566 !$#authors Signaes, C.; Akusjaervi, G.; Pettersson, U. !$#journal Gene (1986) 50:173-184 !$#title Region E3 of human adenoviruses; differences between the !1oncogenic adenovirus-3 and the non-oncogenic adenovirus-2. !$#cross-references MUID:87219876; PMID:3582978 !$#accession I29500 !'##molecule_type DNA !'##residues 1-134 ##label SIG !'##cross-references GB:M15952; NID:g209901; PIDN:AAA42488.1; !1PID:g209909 CLASSIFICATION #superfamily adenovirus early E3B 14.5K protein KEYWORDS early protein; glycoprotein; transmembrane protein FEATURE !$128 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 134 #molecular-weight 15239 #checksum 557 SEQUENCE /// ENTRY ERAD78 #type complete TITLE early E3B 14.9K protein - human adenovirus 7 (strain Gomen) ORGANISM #formal_name Mastadenovirus h7 #common_name human adenovirus 7 #note host Homo sapiens (man) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS D31830; S52805 REFERENCE A94386 !$#authors Hong, J.S.; Mullis, K.G.; Engler, J.A. !$#journal Virology (1988) 167:545-553 !$#title Characterization of the early region 3 and fiber genes of !1Ad7. !$#cross-references MUID:89073758; PMID:2849239 !$#accession D31830 !'##molecule_type DNA !'##residues 1-134 ##label HON !'##cross-references GB:M23696; NID:g341012; PIDN:AAA53252.1; !1PID:g576459 REFERENCE S52798 !$#authors Kajon, A.E.; Wadell, G. !$#submission submitted to the EMBL Data Library, April 1995 !$#description Sequence analysis of the E3 region and fiber gene of human !1adenovirus 7h. !$#accession S52805 !'##status preliminary !'##molecule_type DNA !'##residues 1-94,'N',96-102,'V',104-134 ##label KAJ !'##cross-references EMBL:Z48954; NID:g762955; PIDN:CAA88814.1; !1PID:g762963 CLASSIFICATION #superfamily adenovirus early E3B 14.5K protein KEYWORDS early protein; glycoprotein; transmembrane protein FEATURE !$128 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 134 #molecular-weight 15214 #checksum 9654 SEQUENCE /// ENTRY ERAD26 #type complete TITLE early E3 9K glycoprotein - human adenovirus 3 ORGANISM #formal_name Mastadenovirus h3 #common_name human adenovirus 3 DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 16-Jul-1999 ACCESSIONS G29500 REFERENCE A91566 !$#authors Signaes, C.; Akusjaervi, G.; Pettersson, U. !$#journal Gene (1986) 50:173-184 !$#title Region E3 of human adenoviruses; differences between the !1oncogenic adenovirus-3 and the non-oncogenic adenovirus-2. !$#cross-references MUID:87219876; PMID:3582978 !$#accession G29500 !'##molecule_type DNA !'##residues 1-77 ##label SIG !'##cross-references GB:M15952; NID:g209901; PIDN:AAA42486.1; !1PID:g209907 CLASSIFICATION #superfamily adenovirus early E3 9K glycoprotein KEYWORDS early protein; glycoprotein FEATURE !$7 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 77 #molecular-weight 9014 #checksum 4017 SEQUENCE /// ENTRY ERAD79 #type complete TITLE early E3 7.7K protein - human adenovirus 7 (strain Gomen) ORGANISM #formal_name Mastadenovirus h7 #common_name human adenovirus 7 #note host Homo sapiens (man) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS B31830 REFERENCE A94386 !$#authors Hong, J.S.; Mullis, K.G.; Engler, J.A. !$#journal Virology (1988) 167:545-553 !$#title Characterization of the early region 3 and fiber genes of !1Ad7. !$#cross-references MUID:89073758; PMID:2849239 !$#accession B31830 !'##molecule_type DNA !'##residues 1-66 ##label HON !'##cross-references GB:M23696; NID:g341012; PIDN:AAA53250.1; !1PID:g576457 CLASSIFICATION #superfamily adenovirus early E3 9K glycoprotein KEYWORDS early protein; glycoprotein FEATURE !$7,24 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 66 #molecular-weight 7666 #checksum 1262 SEQUENCE /// ENTRY ERAD27 #type complete TITLE early E3 10.3K protein - human adenovirus 3 ORGANISM #formal_name Mastadenovirus h3 #common_name human adenovirus 3 #note host Homo sapiens (man) DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 07-Nov-1997 ACCESSIONS C31830; H29500 REFERENCE A91566 !$#authors Signaes, C.; Akusjaervi, G.; Pettersson, U. !$#journal Gene (1986) 50:173-184 !$#title Region E3 of human adenoviruses; differences between the !1oncogenic adenovirus-3 and the non-oncogenic adenovirus-2. !$#cross-references MUID:87219876; PMID:3582978 !$#accession C31830 !'##molecule_type DNA !'##residues 1-91 ##label SIG !'##cross-references GB:M15952; NID:g209901 !'##note the GenBank entry ADRE3AA PID:g209908 differs from the !1published sequence in having codon CCT rather than GCT for !114-Ala CLASSIFICATION #superfamily adenovirus early E3 10.3K protein KEYWORDS early protein; transmembrane protein SUMMARY #length 91 #molecular-weight 10330 #checksum 9429 SEQUENCE /// ENTRY ERAD77 #type complete TITLE early E3 10.3K protein - human adenovirus 7 (strain Gomen) ORGANISM #formal_name Mastadenovirus h7 #common_name human adenovirus 7 DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jul-1999 ACCESSIONS G31830; S52804; C31830; H29500 REFERENCE A94386 !$#authors Hong, J.S.; Mullis, K.G.; Engler, J.A. !$#journal Virology (1988) 167:545-553 !$#title Characterization of the early region 3 and fiber genes of !1Ad7. !$#cross-references MUID:89073758; PMID:2849239 !$#accession G31830 !'##molecule_type DNA !'##residues 1-91 ##label HON !'##cross-references GB:M23696; NID:g341012; PIDN:AAA53251.1; !1PID:g576458 REFERENCE S52798 !$#authors Kajon, A.E.; Wadell, G. !$#submission submitted to the EMBL Data Library, April 1995 !$#description Sequence analysis of the E3 region and fiber gene of human !1adenovirus 7h. !$#accession S52804 !'##status preliminary !'##molecule_type DNA !'##residues 1-91 ##label KAJ !'##cross-references EMBL:Z48954; NID:g762955; PIDN:CAA88813.1; !1PID:g762962 CLASSIFICATION #superfamily adenovirus early E3 10.3K protein KEYWORDS early protein; transmembrane protein SUMMARY #length 91 #molecular-weight 10330 #checksum 9429 SEQUENCE /// ENTRY ERAD31 #type complete TITLE early E3A 12.1K protein - human adenovirus 3 ORGANISM #formal_name Mastadenovirus h3 #common_name human adenovirus 3 DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 16-Jul-1999 ACCESSIONS B29500 REFERENCE A91566 !$#authors Signaes, C.; Akusjaervi, G.; Pettersson, U. !$#journal Gene (1986) 50:173-184 !$#title Region E3 of human adenoviruses; differences between the !1oncogenic adenovirus-3 and the non-oncogenic adenovirus-2. !$#cross-references MUID:87219876; PMID:3582978 !$#accession B29500 !'##molecule_type DNA !'##residues 1-106 ##label SIG !'##cross-references GB:M15952; NID:g209901; PIDN:AAA42481.1; !1PID:g209902 CLASSIFICATION #superfamily adenovirus early E3 12K protein KEYWORDS early protein; glycoprotein FEATURE !$77 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 106 #molecular-weight 12124 #checksum 4164 SEQUENCE /// ENTRY ERAD51 #type complete TITLE early E3A 12.5K protein - human adenovirus 5 ORGANISM #formal_name Mastadenovirus h5 #common_name human adenovirus 5 #note host Homo sapiens (man) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS A05244 REFERENCE A94335 !$#authors Cladaras, C.; Wold, W.S.M. !$#journal Virology (1985) 140:28-43 !$#title DNA sequence of the early E3 transcription unit of !1adenovirus 5. !$#cross-references MUID:85092388; PMID:2981456 !$#accession A05244 !'##molecule_type DNA !'##residues 1-107 ##label CLA !'##cross-references GB:X03002; NID:g58503; PIDN:CAA26781.1; PID:g58504 CLASSIFICATION #superfamily adenovirus early E3 12K protein KEYWORDS early protein SUMMARY #length 107 #molecular-weight 12347 #checksum 8778 SEQUENCE /// ENTRY ERADT1 #type complete TITLE early E3A 12.5K protein - human adenovirus 2 ORGANISM #formal_name Mastadenovirus h2 #common_name human adenovirus 2 #note host Homo sapiens (man) DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 26-Feb-1999 ACCESSIONS A42536 REFERENCE A42536 !$#authors Hawkins, L.K.; Wold, W.S.M. !$#journal Virology (1992) 188:486-494 !$#title A 12,500 MW protein is coded by region E3 of adenovirus. !$#cross-references MUID:92263751; PMID:1585632 !$#accession A42536 !'##molecule_type DNA !'##residues 1-107 ##label HAW CLASSIFICATION #superfamily adenovirus early E3 12K protein KEYWORDS early protein SUMMARY #length 107 #molecular-weight 12394 #checksum 2001 SEQUENCE /// ENTRY ERAD53 #type complete TITLE early E3A 10.5K protein - human adenovirus 5 ORGANISM #formal_name Mastadenovirus h5 #common_name human adenovirus 5 #note host Homo sapiens (man) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS A05245 REFERENCE A94335 !$#authors Cladaras, C.; Wold, W.S.M. !$#journal Virology (1985) 140:28-43 !$#title DNA sequence of the early E3 transcription unit of !1adenovirus 5. !$#cross-references MUID:85092388; PMID:2981456 !$#accession A05245 !'##molecule_type DNA !'##residues 1-93 ##label CLA !'##cross-references GB:X03002; NID:g58503; PIDN:CAA26784.1; PID:g58507 CLASSIFICATION #superfamily adenovirus early E3A 10.5K protein KEYWORDS early protein; transmembrane protein SUMMARY #length 93 #molecular-weight 10523 #checksum 6925 SEQUENCE /// ENTRY ERAD32 #type complete TITLE early E3 16K glycoprotein - human adenovirus 3 ORGANISM #formal_name Mastadenovirus h3 #common_name human adenovirus 3 DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 16-Jul-1999 ACCESSIONS C29500 REFERENCE A91566 !$#authors Signaes, C.; Akusjaervi, G.; Pettersson, U. !$#journal Gene (1986) 50:173-184 !$#title Region E3 of human adenoviruses; differences between the !1oncogenic adenovirus-3 and the non-oncogenic adenovirus-2. !$#cross-references MUID:87219876; PMID:3582978 !$#accession C29500 !'##molecule_type DNA !'##residues 1-146 ##label SIG !'##cross-references GB:M15952; NID:g209901; PIDN:AAA42482.1; !1PID:g209903 CLASSIFICATION #superfamily adenovirus early E3 16K glycoprotein KEYWORDS early protein; glycoprotein FEATURE !$51,84 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 146 #molecular-weight 16047 #checksum 8422 SEQUENCE /// ENTRY ERAD34 #type complete TITLE early E3 20.1K glycoprotein - human adenovirus 3 ORGANISM #formal_name Mastadenovirus h3 #common_name human adenovirus 3 DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 16-Jul-1999 ACCESSIONS E29500 REFERENCE A91566 !$#authors Signaes, C.; Akusjaervi, G.; Pettersson, U. !$#journal Gene (1986) 50:173-184 !$#title Region E3 of human adenoviruses; differences between the !1oncogenic adenovirus-3 and the non-oncogenic adenovirus-2. !$#cross-references MUID:87219876; PMID:3582978 !$#accession E29500 !'##molecule_type DNA !'##residues 1-179 ##label SIG !'##cross-references GB:M15952; NID:g209901; PIDN:AAA42484.1; !1PID:g209905 CLASSIFICATION #superfamily adenovirus early E3 20.1K glycoprotein KEYWORDS early protein; glycoprotein FEATURE !$29,57,70,75,123 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 179 #molecular-weight 20058 #checksum 6665 SEQUENCE /// ENTRY ERAD23 #type complete TITLE early E3 20.3K glycoprotein - human adenovirus 35 ORGANISM #formal_name Mastadenovirus h35 #common_name human adenovirus 35 #note host Homo sapiens (man) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS C31162; JC4769 REFERENCE A93039 !$#authors Flomenberg, P.R.; Chen, M.; Horwitz, M.S. !$#journal J. Virol. (1988) 62:4431-4437 !$#title Sequence and genetic organization of adenovirus type 35 !1early region 3. !$#cross-references MUID:89012230; PMID:3172347 !$#accession C31162 !'##molecule_type DNA !'##residues 1-181 ##label FLO !'##cross-references GB:M23195; NID:g516584; PIDN:AAA42437.1; !1PID:g516587 REFERENCE JC4765 !$#authors Basler, C.F.; Droguett, G.; Horwitz, M.S. !$#journal Gene (1996) 170:249-254 !$#title Sequence of the immunoregulatory early region 3 and flanking !1sequences of adenovirus type 35. !$#cross-references MUID:96235144; PMID:8666254 !$#accession JC4769 !'##molecule_type DNA !'##residues 1-181 ##label BAS !'##cross-references GB:U32664; NID:g984529; PIDN:AAA75326.1; !1PID:g984534 GENETICS !$#gene E3 region CLASSIFICATION #superfamily adenovirus early E3 20.1K glycoprotein KEYWORDS early protein; glycoprotein FEATURE !$29,57,70,75 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 181 #molecular-weight 20365 #checksum 8985 SEQUENCE /// ENTRY B44057 #type complete TITLE early E3 20.3K glycoprotein - human adenovirus 11 (strain Slobiski) ORGANISM #formal_name Mastadenovirus h11 #common_name human adenovirus 11 #note host Homo sapiens (man) DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 31-Dec-1993 ACCESSIONS B44057 REFERENCE A44057 !$#authors Mei, Y.F.; Wadell, G. !$#journal Virology (1992) 191:125-133 !$#title The nucleotide sequence of adenovirus type 11 early 3 !1region: comparison of genome type Ad11p and Ad11a. !$#cross-references MUID:93033102; PMID:1413499 !$#accession B44057 !'##molecule_type DNA !'##residues 1-181 ##label MEI !'##cross-references GB:M94458 CLASSIFICATION #superfamily adenovirus early E3 20.1K glycoprotein KEYWORDS early protein; glycoprotein FEATURE !$29,57,70,75 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 181 #molecular-weight 20335 #checksum 8149 SEQUENCE /// ENTRY F44057 #type complete TITLE early E3 20.3K glycoprotein - human adenovirus 11 (strain BC34) ORGANISM #formal_name Mastadenovirus h11 #common_name human adenovirus 11 #note host Homo sapiens (man) DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 31-Dec-1993 ACCESSIONS F44057 REFERENCE A44057 !$#authors Mei, Y.F.; Wadell, G. !$#journal Virology (1992) 191:125-133 !$#title The nucleotide sequence of adenovirus type 11 early 3 !1region: comparison of genome type Ad11p and Ad11a. !$#cross-references MUID:93033102; PMID:1413499 !$#accession F44057 !'##molecule_type DNA !'##residues 1-181 ##label MEI !'##cross-references GB:M94459 CLASSIFICATION #superfamily adenovirus early E3 20.1K glycoprotein KEYWORDS early protein; glycoprotein FEATURE !$29,57,70,75 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 181 #molecular-weight 20324 #checksum 9344 SEQUENCE /// ENTRY ERAD35 #type complete TITLE early E3 20.5K glycoprotein - human adenovirus 3 ORGANISM #formal_name Mastadenovirus h3 #common_name human adenovirus 3 DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 16-Jul-1999 ACCESSIONS F29500 REFERENCE A91566 !$#authors Signaes, C.; Akusjaervi, G.; Pettersson, U. !$#journal Gene (1986) 50:173-184 !$#title Region E3 of human adenoviruses; differences between the !1oncogenic adenovirus-3 and the non-oncogenic adenovirus-2. !$#cross-references MUID:87219876; PMID:3582978 !$#accession F29500 !'##molecule_type DNA !'##residues 1-189 ##label SIG !'##cross-references GB:M15952; NID:g209901; PIDN:AAA42485.1; !1PID:g209906 !'##note the authors translated the codon ATG for residue 161 as Ile and !1TTG for 165 as Phe CLASSIFICATION #superfamily adenovirus early E3 20.5K glycoprotein KEYWORDS early protein; glycoprotein FEATURE !$73,137 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 189 #molecular-weight 20531 #checksum 7413 SEQUENCE /// ENTRY ERAD75 #type complete TITLE early E3 20.6K glycoprotein - human adenovirus 7 (strain Gomen) ORGANISM #formal_name Mastadenovirus h7 #common_name human adenovirus 7 #note host Homo sapiens (man) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 07-Nov-1997 ACCESSIONS A31830 REFERENCE A94386 !$#authors Hong, J.S.; Mullis, K.G.; Engler, J.A. !$#journal Virology (1988) 167:545-553 !$#title Characterization of the early region 3 and fiber genes of !1Ad7. !$#cross-references MUID:89073758; PMID:2849239 !$#accession A31830 !'##molecule_type DNA !'##residues 1-189 ##label HON !'##cross-references GB:M23696; NID:g341012 !'##note the GenBank entry ADRH7FIBER PID:g576456 differs from the !1published sequence in having codon AGT rather than ACT for !110-Thr CLASSIFICATION #superfamily adenovirus early E3 20.5K glycoprotein KEYWORDS early protein; glycoprotein FEATURE !$73,137 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 189 #molecular-weight 20573 #checksum 7330 SEQUENCE /// ENTRY ERAD86 #type complete TITLE early E3 20.6K glycoprotein - human adenovirus 35 ORGANISM #formal_name Mastadenovirus h35 #common_name human adenovirus 35 #note host Homo sapiens (man) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS D31162; JC4770 REFERENCE A93039 !$#authors Flomenberg, P.R.; Chen, M.; Horwitz, M.S. !$#journal J. Virol. (1988) 62:4431-4437 !$#title Sequence and genetic organization of adenovirus type 35 !1early region 3. !$#cross-references MUID:89012230; PMID:3172347 !$#accession D31162 !'##molecule_type DNA !'##residues 1-187 ##label FLO !'##cross-references GB:M23195; NID:g516584; PIDN:AAA42438.1; !1PID:g516588 REFERENCE JC4765 !$#authors Basler, C.F.; Droguett, G.; Horwitz, M.S. !$#journal Gene (1996) 170:249-254 !$#title Sequence of the immunoregulatory early region 3 and flanking !1sequences of adenovirus type 35. !$#cross-references MUID:96235144; PMID:8666254 !$#accession JC4770 !'##molecule_type DNA !'##residues 1-187 ##label BAS !'##cross-references GB:U32664; NID:g984529; PIDN:AAA75327.1; !1PID:g984535 GENETICS !$#gene E3 region CLASSIFICATION #superfamily adenovirus early E3 20.5K glycoprotein KEYWORDS early protein; glycoprotein FEATURE !$30,73,117,122,134, !$135 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 187 #molecular-weight 20618 #checksum 7110 SEQUENCE /// ENTRY C44057 #type complete TITLE early E3 20.6K glycoprotein - human adenovirus 11 (strain Slobiski) ORGANISM #formal_name Mastadenovirus h11 #common_name human adenovirus 11 #note host Homo sapiens (man) DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 31-Dec-1993 ACCESSIONS C44057 REFERENCE A44057 !$#authors Mei, Y.F.; Wadell, G. !$#journal Virology (1992) 191:125-133 !$#title The nucleotide sequence of adenovirus type 11 early 3 !1region: comparison of genome type Ad11p and Ad11a. !$#cross-references MUID:93033102; PMID:1413499 !$#accession C44057 !'##molecule_type DNA !'##residues 1-187 ##label MEI !'##cross-references GB:M94458 CLASSIFICATION #superfamily adenovirus early E3 20.5K glycoprotein KEYWORDS early protein; glycoprotein FEATURE !$30,73,117,134,135 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 187 #molecular-weight 20592 #checksum 6405 SEQUENCE /// ENTRY G44057 #type complete TITLE early E3 20.6K glycoprotein - human adenovirus 11 (strain BC34) ORGANISM #formal_name Mastadenovirus h11 #common_name human adenovirus 11 #note host Homo sapiens (man) DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 31-Dec-1993 ACCESSIONS G44057 REFERENCE A44057 !$#authors Mei, Y.F.; Wadell, G. !$#journal Virology (1992) 191:125-133 !$#title The nucleotide sequence of adenovirus type 11 early 3 !1region: comparison of genome type Ad11p and Ad11a. !$#cross-references MUID:93033102; PMID:1413499 !$#accession G44057 !'##molecule_type DNA !'##residues 1-183 ##label MEI !'##cross-references GB:M94459 CLASSIFICATION #superfamily adenovirus early E3 20.5K glycoprotein KEYWORDS early protein; glycoprotein FEATURE !$30,73,117,134,135 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 183 #molecular-weight 20226 #checksum 3039 SEQUENCE /// ENTRY Q6ADE #type complete TITLE early E3 18.5K glycoprotein - human adenovirus 2 ORGANISM #formal_name Mastadenovirus h2 #common_name human adenovirus 2 #note host Homo sapiens (man) DATE 31-Dec-1980 #sequence_revision 08-Oct-1981 #text_change 16-Feb-1997 ACCESSIONS A03821 REFERENCE A93702 !$#authors Herisse, J.; Courtois, G.; Galibert, F. !$#journal Nucleic Acids Res. (1980) 8:2173-2192 !$#title Nucleotide sequence of the EcoRI D fragment of adenovirus 2 !1genome. !$#cross-references MUID:81053687; PMID:6253880 !$#accession A03821 !'##molecule_type DNA !'##residues 1-159 ##label HER CLASSIFICATION #superfamily adenovirus early E3 18.5K glycoprotein KEYWORDS early protein; glycoprotein; transmembrane protein FEATURE !$29,78 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 159 #molecular-weight 18438 #checksum 1773 SEQUENCE /// ENTRY ERADA5 #type complete TITLE early E3 18.5K glycoprotein - human adenovirus 5 ORGANISM #formal_name Mastadenovirus h5 #common_name human adenovirus 5 #note host Homo sapiens (man) DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 16-Jul-1999 ACCESSIONS A03822; A22515 REFERENCE A94335 !$#authors Cladaras, C.; Wold, W.S.M. !$#journal Virology (1985) 140:28-43 !$#title DNA sequence of the early E3 transcription unit of !1adenovirus 5. !$#cross-references MUID:85092388; PMID:2981456 !$#accession A03822 !'##molecule_type DNA !'##residues 1-160 ##label CLA !'##cross-references GB:X03002; NID:g58503; PIDN:CAA26783.1; PID:g58506 REFERENCE A22515 !$#authors Wold, W.S.M.; Cladaras, C.; Deutscher, S.L.; Kapoor, Q.S. !$#journal J. Biol. Chem. (1985) 260:2424-2431 !$#title The 19-kDa glycoprotein coded by region E3 of adenovirus. !$#cross-references MUID:85130985; PMID:3882694 !$#accession A22515 !'##molecule_type DNA !'##residues 1-160 ##label WOL !'##cross-references GB:M12406; NID:g209911; PIDN:AAA42492.1; !1PID:g209912 CLASSIFICATION #superfamily adenovirus early E3 18.5K glycoprotein KEYWORDS early protein; glycoprotein; transmembrane protein FEATURE !$30,79 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 160 #molecular-weight 18502 #checksum 5869 SEQUENCE /// ENTRY ERAD33 #type complete TITLE early E3 18.5K glycoprotein - human adenovirus 3 ALTERNATE_NAMES early E3 19.2K glycoprotein ORGANISM #formal_name Mastadenovirus h3 #common_name human adenovirus 3 DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 16-Jul-1999 ACCESSIONS D29500 REFERENCE A91566 !$#authors Signaes, C.; Akusjaervi, G.; Pettersson, U. !$#journal Gene (1986) 50:173-184 !$#title Region E3 of human adenoviruses; differences between the !1oncogenic adenovirus-3 and the non-oncogenic adenovirus-2. !$#cross-references MUID:87219876; PMID:3582978 !$#accession D29500 !'##molecule_type DNA !'##residues 1-172 ##label SIG !'##cross-references GB:M15952; NID:g209901; PIDN:AAA42483.1; !1PID:g209904 CLASSIFICATION #superfamily adenovirus early E3 18.5K glycoprotein KEYWORDS early protein; glycoprotein; transmembrane protein FEATURE !$36,68,72,102 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 172 #molecular-weight 19239 #checksum 6989 SEQUENCE /// ENTRY ERAD85 #type complete TITLE early E3 18.5K glycoprotein - human adenovirus 35 ORGANISM #formal_name Mastadenovirus h35 #common_name human adenovirus 35 DATE 31-Mar-1990 #sequence_revision 22-Oct-1999 #text_change 22-Oct-1999 ACCESSIONS JC4768; A31162 REFERENCE JC4765 !$#authors Basler, C.F.; Droguett, G.; Horwitz, M.S. !$#journal Gene (1996) 170:249-254 !$#title Sequence of the immunoregulatory early region 3 and flanking !1sequences of adenovirus type 35. !$#cross-references MUID:96235144; PMID:8666254 !$#accession JC4768 !'##molecule_type DNA !'##residues 1-166 ##label BAS !'##cross-references GB:U32664; NID:g984529; PIDN:AAA75325.1; !1PID:g984533 REFERENCE A93039 !$#authors Flomenberg, P.R.; Chen, M.; Horwitz, M.S. !$#journal J. Virol. (1988) 62:4431-4437 !$#title Sequence and genetic organization of adenovirus type 35 !1early region 3. !$#cross-references MUID:89012230; PMID:3172347 !$#accession A31162 !'##molecule_type DNA !'##residues 1-45,'F',47,'LSADGK',54-166 ##label FLO !'##cross-references GB:M23195; NID:g516584; PIDN:AAA42435.1; !1PID:g516585 COMMENT This protein is involved for interaction with class-1 major !1histocompatibility complex. GENETICS !$#gene E3 CLASSIFICATION #superfamily adenovirus early E3 18.5K glycoprotein KEYWORDS early protein; glycoprotein; transmembrane protein FEATURE !$31,63,67,97 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 166 #molecular-weight 18575 #checksum 6367 SEQUENCE /// ENTRY A44057 #type complete TITLE early E3 18.5K glycoprotein - human adenovirus 11 (strain Slobiski) ORGANISM #formal_name Mastadenovirus h11 #common_name human adenovirus 11 #note host Homo sapiens (man) DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Feb-1997 ACCESSIONS A44057 REFERENCE A44057 !$#authors Mei, Y.F.; Wadell, G. !$#journal Virology (1992) 191:125-133 !$#title The nucleotide sequence of adenovirus type 11 early 3 !1region: comparison of genome type Ad11p and Ad11a. !$#cross-references MUID:93033102; PMID:1413499 !$#accession A44057 !'##molecule_type DNA !'##residues 1-166 ##label MEI !'##cross-references GB:M94458 CLASSIFICATION #superfamily adenovirus early E3 18.5K glycoprotein KEYWORDS early protein; glycoprotein; transmembrane protein FEATURE !$31,63,67,97 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 166 #molecular-weight 18575 #checksum 6367 SEQUENCE /// ENTRY E44057 #type complete TITLE early E3 18.5K glycoprotein - human adenovirus 11 (strain BC34) ORGANISM #formal_name Mastadenovirus h11 #common_name human adenovirus 11 #note host Homo sapiens (man) DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Feb-1997 ACCESSIONS E44057 REFERENCE A44057 !$#authors Mei, Y.F.; Wadell, G. !$#journal Virology (1992) 191:125-133 !$#title The nucleotide sequence of adenovirus type 11 early 3 !1region: comparison of genome type Ad11p and Ad11a. !$#cross-references MUID:93033102; PMID:1413499 !$#accession E44057 !'##molecule_type DNA !'##residues 1-166 ##label MEI !'##cross-references GB:M94459 CLASSIFICATION #superfamily adenovirus early E3 18.5K glycoprotein KEYWORDS early protein; glycoprotein; transmembrane protein FEATURE !$31,63,67,97 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 166 #molecular-weight 18547 #checksum 6685 SEQUENCE /// ENTRY ERAD64 #type complete TITLE early E3 6.4K protein - human adenovirus 35 ORGANISM #formal_name Mastadenovirus h35 #common_name human adenovirus 35 #note host Homo sapiens (man) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS B31162 REFERENCE A93039 !$#authors Flomenberg, P.R.; Chen, M.; Horwitz, M.S. !$#journal J. Virol. (1988) 62:4431-4437 !$#title Sequence and genetic organization of adenovirus type 35 !1early region 3. !$#cross-references MUID:89012230; PMID:3172347 !$#accession B31162 !'##molecule_type DNA !'##residues 1-61 ##label FLO !'##cross-references GB:M23195; NID:g516584; PIDN:AAA42436.1; !1PID:g516586 CLASSIFICATION #superfamily adenovirus early E3 6.4K protein KEYWORDS early protein SUMMARY #length 61 #molecular-weight 6440 #checksum 8129 SEQUENCE /// ENTRY ERADMS #type complete TITLE early E3 17.7K glycoprotein - mouse adenovirus 1 ORGANISM #formal_name Mastadenovirus mus1 #common_name mouse adenovirus 1 #note host Mus musculus (house mouse) DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS B33382 REFERENCE A33382 !$#authors Raviprakash, K.S.; Grunhaus, A.; El Kholy, M.A.; Horwitz, !1M.S. !$#journal J. Virol. (1989) 63:5455-5458 !$#title The mouse adenovirus type 1 contains an unusual E3 region. !$#cross-references MUID:90064816; PMID:2531236 !$#accession B33382 !'##molecule_type DNA !'##residues 1-161 ##label RAV !'##cross-references GB:M30594; NID:g209755; PIDN:AAA42433.1; !1PID:g209757 CLASSIFICATION #superfamily mouse adenovirus early E3 protein KEYWORDS early protein; glycoprotein; transmembrane protein FEATURE !$14,87 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 161 #molecular-weight 17699 #checksum 5548 SEQUENCE /// ENTRY ERADD1 #type complete TITLE early E3 13K glycoprotein - canine adenovirus 1 (strain Glaxo) ORGANISM #formal_name Mastadenovirus can1 #common_name canine adenovirus 1 DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS B40318 REFERENCE A40318 !$#authors Dragulev, B.P.; Sira, S.; Abouhaidar, M.G.; Campbell, J.B. !$#journal Virology (1991) 183:298-305 !$#title Sequence analysis of putative E3 and fiber genomic regions !1of two strains of canine adenovirus type 1. !$#cross-references MUID:91272490; PMID:1828920 !$#accession B40318 !'##molecule_type DNA !'##residues 1-117 ##label DRA !'##cross-references GB:M60937; NID:g210036; PIDN:AAA42534.1; !1PID:g210038 CLASSIFICATION #superfamily dog adenovirus early E3 13K glycoprotein KEYWORDS early protein; glycoprotein FEATURE !$25 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 117 #molecular-weight 13311 #checksum 2091 SEQUENCE /// ENTRY ERADD2 #type complete TITLE early E3 22K glycoprotein - canine adenovirus 1 (strain Glaxo) ORGANISM #formal_name Mastadenovirus can1 #common_name canine adenovirus 1 DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS C40318 REFERENCE A40318 !$#authors Dragulev, B.P.; Sira, S.; Abouhaidar, M.G.; Campbell, J.B. !$#journal Virology (1991) 183:298-305 !$#title Sequence analysis of putative E3 and fiber genomic regions !1of two strains of canine adenovirus type 1. !$#cross-references MUID:91272490; PMID:1828920 !$#accession C40318 !'##molecule_type DNA !'##residues 1-195 ##label DRA !'##cross-references GB:M60937; NID:g210036; PIDN:AAA42535.1; !1PID:g210039 CLASSIFICATION #superfamily dog adenovirus early E3 22K glycoprotein KEYWORDS early protein; glycoprotein FEATURE !$20,61,76,88,126,139 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 195 #molecular-weight 22232 #checksum 3020 SEQUENCE /// ENTRY ERAD65 #type complete TITLE early E1A 6K protein - human adenovirus 5 ORGANISM #formal_name Mastadenovirus h5 #common_name human adenovirus 5 DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 04-Mar-1994 ACCESSIONS A03825 REFERENCE A91471 !$#authors van Ormondt, H.; Maat, J.; van Beveren, C.P. !$#journal Gene (1980) 11:299-309 !$#title The nucleotide sequence of the transforming early region E1 !1of adenovirus type 5 DNA. !$#cross-references MUID:81165537; PMID:6260576 !$#accession A03825 !'##molecule_type DNA !'##residues 1-55 ##label VAN GENETICS !$#introns 26/3 CLASSIFICATION #superfamily adenovirus early E1A 6K protein KEYWORDS alternative splicing; early protein SUMMARY #length 55 #molecular-weight 6156 #checksum 9075 SEQUENCE /// ENTRY WMAD67 #type complete TITLE early E1A 6K protein - human adenovirus 7 ORGANISM #formal_name Mastadenovirus h7 #common_name human adenovirus 7 #note host Homo sapiens (man) DATE 18-Dec-1981 #sequence_revision 18-Dec-1981 #text_change 05-Jun-1998 ACCESSIONS A03827 REFERENCE A91477 !$#authors Dijkema, R.; Dekker, B.M.M.; van Ormondt, H.; de Waard, A.; !1Maat, J.; Boyer, H.W. !$#journal Gene (1980) 12:287-299 !$#title Gene organization of the transforming region of weakly !1oncogenic adenovirus type 7: the E1a region. !$#cross-references MUID:81237792; PMID:6985480 !$#accession A03827 !'##molecule_type DNA !'##residues 1-57 ##label DIJ COMMENT For the early E1A 28K and E1A 24K protein alternative splice !1forms see PIR:WMAD87. CLASSIFICATION #superfamily adenovirus early E1A 6K protein KEYWORDS alternative splicing; early protein SUMMARY #length 57 #molecular-weight 6771 #checksum 6865 SEQUENCE /// ENTRY Q2AD2 #type complete TITLE early E1A 32K protein - human adenovirus 2 CONTAINS early E1A 26K protein ORGANISM #formal_name Mastadenovirus h2 #common_name human adenovirus 2 #note host Homo sapiens (man) DATE 31-Oct-1980 #sequence_revision 08-Oct-1981 #text_change 16-Feb-1997 ACCESSIONS A03824; B03824 REFERENCE A93215 !$#authors Perricaudet, M.; Akusjarvi, G.; Virtanen, A.; Pettersson, U. !$#journal Nature (1979) 281:694-696 !$#title Structure of two spliced mRNAs from the transforming region !1of human subgroup C adenoviruses. !$#cross-references MUID:81012104; PMID:551290 !$#accession A03824 !'##molecule_type DNA !'##residues 1-289 ##label PER REFERENCE A92351 !$#authors Gingeras, T.R.; Sciaky, D.; Gelinas, R.E.; Bing-Dong, J.; !1Yen, C.E.; Kelly, M.M.; Bullock, P.A.; Parsons, B.L.; !1O'Neill, K.E.; Roberts, R.J. !$#journal J. Biol. Chem. (1982) 257:13475-13491 !$#title Nucleotide sequences from the adenovirus-2 genome. !$#cross-references MUID:83056843; PMID:7142161 !$#accession B03824 !'##molecule_type DNA !'##residues 1-67,'E',69-80,'F',82-289 ##label GIN CLASSIFICATION #superfamily adenovirus early E1A protein KEYWORDS alternative splicing; DNA binding; early protein; !1transcription regulation; zinc finger FEATURE !$1-139,186-289 #product early E1A 26K protein #status predicted !8#label E1A SUMMARY #length 289 #molecular-weight 31851 #checksum 969 SEQUENCE /// ENTRY Q2AD5 #type complete TITLE early E1A 32K protein - human adenovirus 5 CONTAINS early E1A 26K protein ORGANISM #formal_name Mastadenovirus h5 #common_name human adenovirus 5 #note host Homo sapiens (man) DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Feb-1997 ACCESSIONS C03824; A03824 REFERENCE A91471 !$#authors van Ormondt, H.; Maat, J.; van Beveren, C.P. !$#journal Gene (1980) 11:299-309 !$#title The nucleotide sequence of the transforming early region E1 !1of adenovirus type 5 DNA. !$#cross-references MUID:81165537; PMID:6260576 !$#accession C03824 !'##molecule_type DNA !'##residues 1-289 ##label VAN CLASSIFICATION #superfamily adenovirus early E1A protein KEYWORDS alternative splicing; DNA binding; early protein; !1transcription regulation; zinc finger FEATURE !$1-139,186-289 #product early E1A 26K protein #status predicted !8#label E1A SUMMARY #length 289 #molecular-weight 31851 #checksum 44 SEQUENCE /// ENTRY WMAD87 #type complete TITLE early E1A 28K protein - human adenovirus 7 CONTAINS early E1A 24K protein ORGANISM #formal_name Mastadenovirus h7 #common_name human adenovirus 7 #note host Homo sapiens (man) DATE 18-Dec-1981 #sequence_revision 18-Dec-1981 #text_change 05-Jun-1998 ACCESSIONS A03826 REFERENCE A91477 !$#authors Dijkema, R.; Dekker, B.M.M.; van Ormondt, H.; de Waard, A.; !1Maat, J.; Boyer, H.W. !$#journal Gene (1980) 12:287-299 !$#title Gene organization of the transforming region of weakly !1oncogenic adenovirus type 7: the E1a region. !$#cross-references MUID:81237792; PMID:6985480 !$#accession A03826 !'##molecule_type DNA !'##residues 1-261 ##label DIJ COMMENT For the early E1A 6K protein alternative splice form see !1PIR:WMAD67. CLASSIFICATION #superfamily adenovirus early E1A protein KEYWORDS alternative splicing; DNA binding; early protein; !1transcription regulation; zinc finger FEATURE !$1-163,195-261 #product early E1A 24K protein #status predicted !8#label E4K SUMMARY #length 261 #molecular-weight 28385 #checksum 884 SEQUENCE /// ENTRY WMAD84 #type complete TITLE early E1A 28K protein - human adenovirus 4 ORGANISM #formal_name Mastadenovirus h4 #common_name human adenovirus 4 #note host Homo sapiens (man) DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 16-Jul-1999 ACCESSIONS A25614 REFERENCE A94347 !$#authors Tokunaga, O.; Yaegashi, T.; Lowe, J.; Dobbs, L.; !1Padmanabhan, R. !$#journal Virology (1986) 155:418-433 !$#title Sequence analysis in the E1 region of adenovirus type 4 DNA. !$#cross-references MUID:87071662; PMID:2947381 !$#accession A25614 !'##molecule_type DNA !'##residues 1-257 ##label TOK !'##cross-references GB:M14918; NID:g209874; PIDN:AAA67091.1; !1PID:g825435 GENETICS !$#introns 189/2 CLASSIFICATION #superfamily adenovirus early E1A protein KEYWORDS DNA binding; early protein; transcription regulation; zinc !1finger SUMMARY #length 257 #molecular-weight 28095 #checksum 4452 SEQUENCE /// ENTRY WMADC2 #type complete TITLE early E1A 25K protein - canine adenovirus 2 (strain Tront A 26-61) ORGANISM #formal_name Mastadenovirus can2 #common_name canine adenovirus 2 #note host Canis lupis familiaris (dog) DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 22-Oct-1999 ACCESSIONS A34165 REFERENCE A34165 !$#authors Shibata, R.; Shinagawa, M.; Iida, Y.; Tsukiyama, T. !$#journal Virology (1989) 172:460-467 !$#title Nucleotide sequence of E1 region of canine adenovirus type !12. !$#cross-references MUID:90021176; PMID:2800332 !$#accession A34165 !'##molecule_type DNA !'##residues 1-232 ##label SHI !'##cross-references GB:J04368; NID:g209884; PIDN:AAA42470.1; !1PID:g209885 GENETICS !$#introns 172/1 CLASSIFICATION #superfamily adenovirus early E1A protein KEYWORDS early protein; transcription regulation SUMMARY #length 232 #molecular-weight 25346 #checksum 9667 SEQUENCE /// ENTRY B60010 #type complete TITLE early E1A 20K protein - canine adenovirus 2 ORGANISM #formal_name Mastadenovirus can2 #common_name canine adenovirus 2 #note host Canis lupis familiaris (dog) DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 07-May-1999 ACCESSIONS B60010 REFERENCE A60010 !$#authors Spibey, N.; McClory, R.S.; Cavanagh, H.M.A. !$#journal Virus Res. (1989) 14:241-256 !$#title Identification and nucleotide sequence of the early region 1 !1from canine adenovirus types 1 and 2. !$#cross-references MUID:90163565; PMID:2623943 !$#accession B60010 !'##molecule_type DNA !'##residues 1-171 ##label SPI CLASSIFICATION #superfamily adenovirus early E1A protein KEYWORDS early protein; transcription regulation SUMMARY #length 171 #molecular-weight 18942 #checksum 6121 SEQUENCE /// ENTRY A60010 #type complete TITLE early E1A 20K protein - canine adenovirus 1 ORGANISM #formal_name Mastadenovirus can1 #common_name canine adenovirus 1 #note host Canis lupis familiaris (dog) DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 07-May-1999 ACCESSIONS A60010 REFERENCE A60010 !$#authors Spibey, N.; McClory, R.S.; Cavanagh, H.M.A. !$#journal Virus Res. (1989) 14:241-256 !$#title Identification and nucleotide sequence of the early region 1 !1from canine adenovirus types 1 and 2. !$#cross-references MUID:90163565; PMID:2623943 !$#accession A60010 !'##molecule_type DNA !'##residues 1-175 ##label SPI CLASSIFICATION #superfamily adenovirus early E1A protein KEYWORDS early protein; transcription regulation SUMMARY #length 175 #molecular-weight 19507 #checksum 8199 SEQUENCE /// ENTRY AQADG2 #type complete TITLE early E1A 29.6K protein - human adenovirus 12 CONTAINS early E1A 26K protein ORGANISM #formal_name Mastadenovirus h12 #common_name human adenovirus 12 #note host Homo sapiens (man) DATE 31-Mar-1981 #sequence_revision 31-Mar-1981 #text_change 22-Oct-1999 ACCESSIONS A03828; B03828; S33928 REFERENCE A90797 !$#authors Sugisaki, H.; Sugimoto, K.; Takanami, M.; Shiroki, K.; !1Saito, I.; Shimojo, H.; Sawada, Y.; Uemizu, Y.; Uesugi, S.; !1Fujinaga, K. !$#journal Cell (1980) 20:777-786 !$#title Structure and gene organization in the transforming hind !1III- G fragment of Ad12. !$#cross-references MUID:81022638; PMID:6251973 !$#accession A03828 !'##molecule_type DNA !'##residues 1-266 ##label SUG !'##cross-references GB:V00004; GB:J01906; GB:J01908; GB:J01909; !1GB:J01910; GB:J01913; GB:J01914; GB:K01430; NID:g58449; !1PIDN:CAA23400.1; PID:g58450 REFERENCE A93237 !$#authors Perricaudet, M.; le Moullec, J.M.; Tiollais, P.; Pettersson, !1U. !$#journal Nature (1980) 288:174-176 !$#title Structure of two adenovirus type 12 transforming !1polypeptides and their evolutionary implications. !$#cross-references MUID:81052432; PMID:7432516 !$#accession B03828 !'##molecule_type DNA !'##residues 1-266 ##label PER REFERENCE S33928 !$#authors Sprengel, J. !$#submission submitted to the EMBL Data Library, June 1993 !$#accession S33928 !'##status preliminary !'##molecule_type DNA !'##residues 1-190,'KCAMGGGR' ##label SPR !'##cross-references EMBL:X73487; NID:g313361; PIDN:CAA51877.1; !1PID:g313362 COMMENT This protein is one of several that control the expression !1of the other early transforming units. CLASSIFICATION #superfamily adenovirus early E1A protein KEYWORDS alternative splicing; DNA binding; early protein; !1transcription regulation; zinc finger FEATURE !$1-159,191-266 #product early E1A 26K protein #status predicted !8#label EAP SUMMARY #length 266 #molecular-weight 29691 #checksum 5966 SEQUENCE /// ENTRY WMADF3 #type complete TITLE early E1A 27K protein - human adenovirus 40 CONTAINS early E1A 15K protein; early E1A 24K protein ORGANISM #formal_name Mastadenovirus h40 #common_name human adenovirus 40 #note host Homo sapiens (man) DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 22-Oct-1999 ACCESSIONS A27333; A29195; B27333; C27333 REFERENCE A27333 !$#authors van Loon, A.E.; Ligtenberg, M.; Reemst, A.M.C.B.; !1Sussenbach, J.S.; Rozijn, T.H. !$#journal Gene (1987) 58:109-126 !$#title Structure and organization of the left-terminal DNA regions !1of fastidious adenovirus types 40 and 41. !$#cross-references MUID:88084437; PMID:2961652 !$#accession A27333 !'##molecule_type DNA !'##residues 1-249 ##label VAN !'##cross-references GB:M18288; NID:g209768; PIDN:AAA42447.1; !1PID:g209771 REFERENCE A94383 !$#authors Ishino, M.; Ohashi, Y.; Emoto, T.; Sawada, Y.; Fujinaga, K. !$#journal Virology (1988) 165:95-102 !$#title Characterization of adenovirus type 40 E1 region. !$#cross-references MUID:88265890; PMID:2968714 !$#accession A29195 !'##molecule_type DNA !'##residues 1-249 ##label ISH !'##cross-references GB:L19443; NID:g303969; PIDN:AAC13949.1; !1PID:g303971 CLASSIFICATION #superfamily adenovirus early E1A protein KEYWORDS alternative splicing; DNA binding; early protein; !1transcription regulation; zinc finger FEATURE !$1-148,177-249 #product early E1A 24K protein #status predicted !8#label EA2\ !$1-62,177-249 #product early E1A 15K protein #status predicted !8#label EA1 SUMMARY #length 249 #molecular-weight 27481 #checksum 2202 SEQUENCE /// ENTRY WMADF4 #type complete TITLE early E1A 27K protein - human adenovirus 41 ORGANISM #formal_name Mastadenovirus h41 #common_name human adenovirus 41 DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jul-1999 ACCESSIONS D27333 REFERENCE A27333 !$#authors van Loon, A.E.; Ligtenberg, M.; Reemst, A.M.C.B.; !1Sussenbach, J.S.; Rozijn, T.H. !$#journal Gene (1987) 58:109-126 !$#title Structure and organization of the left-terminal DNA regions !1of fastidious adenovirus types 40 and 41. !$#cross-references MUID:88084437; PMID:2961652 !$#accession D27333 !'##molecule_type DNA !'##residues 1-251 ##label VAN !'##cross-references GB:M18289; NID:g209778; PIDN:AAA42450.1; !1PID:g209779 GENETICS !$#introns 181/1 CLASSIFICATION #superfamily adenovirus early E1A protein KEYWORDS alternative splicing; DNA binding; early protein; !1transcription regulation; zinc finger SUMMARY #length 251 #molecular-weight 27476 #checksum 4258 SEQUENCE /// ENTRY ERADTA #type complete TITLE early E1A 17K protein - tree shrew adenovirus ORGANISM #formal_name Mastadenovirus tup #common_name tree shrew adenovirus DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 21-Jul-2000 ACCESSIONS A03829 REFERENCE A03829 !$#authors Brinckmann, U.; Darai, G.; Flugel, R.M. !$#journal EMBO J. (1983) 2:2185-2188 !$#title Tupaia (tree shrew) adenovirus DNA: sequence of the !1left-hand fragment corresponding to the transforming early !1region of human adenoviruses. !$#cross-references MUID:84131930; PMID:6321152 !$#accession A03829 !'##molecule_type DNA !'##residues 1-162 ##label BRI !'##cross-references GB:X03001; GB:V01485; GB:X00207; NID:g58557 !'##note the host is identified as Tupaia belangeri CLASSIFICATION #superfamily adenovirus early E1A protein KEYWORDS early protein SUMMARY #length 162 #molecular-weight 17824 #checksum 4226 SEQUENCE /// ENTRY WMADM1 #type complete TITLE early E1A 20K protein - mouse adenovirus 1 ORGANISM #formal_name Mastadenovirus mus1 #common_name mouse adenovirus 1 DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS A31158 REFERENCE A93038 !$#authors Ball, A.O.; Williams, M.E.; Spindler, K.R. !$#journal J. Virol. (1988) 62:3947-3957 !$#title Identification of mouse adenovirus type 1 early region 1: !1DNA sequence and a conserved transactivating function. !$#cross-references MUID:89012162; PMID:3172335 !$#accession A31158 !'##molecule_type DNA !'##residues 1-189 ##label BAL !'##cross-references GB:M22245; GB:J03353; NID:g209746; PIDN:AAA42427.1; !1PID:g209750 CLASSIFICATION #superfamily mouse adenovirus early E1A protein KEYWORDS early protein; transcription regulation SUMMARY #length 189 #molecular-weight 20527 #checksum 3208 SEQUENCE /// ENTRY WMAD51 #type complete TITLE late 33K protein - human adenovirus 5 ORGANISM #formal_name Mastadenovirus h5 #common_name human adenovirus 5 #note host Homo sapiens (man) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 04-Mar-1994 ACCESSIONS F39449 REFERENCE A39449 !$#authors Chroboczek, J.; Bieber, F.; Jacrot, B. !$#journal Virology (1992) 186:280-285 !$#title The sequence of the genome of adenovirus type 5 and its !1comparison with the genome of adenovirus type 2. !$#cross-references MUID:92087470; PMID:1727603 !$#accession F39449 !'##molecule_type DNA !'##residues 1-229 ##label CHR !'##cross-references GB:M73260 CLASSIFICATION #superfamily adenovirus late 33K protein KEYWORDS late protein SUMMARY #length 229 #molecular-weight 25164 #checksum 9588 SEQUENCE /// ENTRY WMAD52 #type complete TITLE late L1 52K protein - human adenovirus 2 ORGANISM #formal_name Mastadenovirus h2 #common_name human adenovirus 2 #note host Homo sapiens (man) DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS A03830 REFERENCE A92461 !$#authors Roberts, R.J.; O'Neill, K.E.; Yen, C.E. !$#journal J. Biol. Chem. (1984) 259:13968-13975 !$#title DNA sequences from the adenovirus 2 genome. !$#cross-references MUID:85054833; PMID:6334081 !$#accession A03830 !'##molecule_type DNA !'##residues 1-415 ##label ROB !'##cross-references GB:J01917; NID:g209811; PIDN:AAA92209.1; !1PID:g209825 CLASSIFICATION #superfamily adenovirus late L1 52K protein KEYWORDS late protein SUMMARY #length 415 #molecular-weight 46995 #checksum 6743 SEQUENCE /// ENTRY WMAD65 #type complete TITLE late L1 52K protein - human adenovirus 5 ORGANISM #formal_name Mastadenovirus h5 #common_name human adenovirus 5 #note host Homo sapiens (man) DATE 17-Mar-1987 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS G39449; A03831 REFERENCE A39449 !$#authors Chroboczek, J.; Bieber, F.; Jacrot, B. !$#journal Virology (1992) 186:280-285 !$#title The sequence of the genome of adenovirus type 5 and its !1comparison with the genome of adenovirus type 2. !$#cross-references MUID:92087470; PMID:1727603 !$#accession G39449 !'##molecule_type DNA !'##residues 1-415 ##label CHR REFERENCE A91508 !$#authors Dekker, B.M.M.; van Ormondt, H. !$#journal Gene (1984) 27:115-120 !$#title The nucleotide sequence of fragment HindIII-C of human !1adenovirus type 5 DNA (map positions 17.1-31.7). !$#cross-references MUID:84183604; PMID:6325298 !$#accession A03831 !'##molecule_type DNA !'##residues 1-173 ##label DEK !'##cross-references GB:X02996; GB:J01967; NID:g58484; PIDN:CAA26751.1; !1PID:g58497 CLASSIFICATION #superfamily adenovirus late L1 52K protein KEYWORDS late protein SUMMARY #length 415 #molecular-weight 47059 #checksum 7888 SEQUENCE /// ENTRY S33936 #type complete TITLE late 52K protein - human adenovirus 12 ORGANISM #formal_name Mastadenovirus h12 #common_name human adenovirus 12 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S33936 REFERENCE S33928 !$#authors Sprengel, J. !$#submission submitted to the EMBL Data Library, June 1993 !$#accession S33936 !'##status preliminary !'##molecule_type DNA !'##residues 1-373 ##label SPR !'##cross-references EMBL:X73487; NID:g313361; PIDN:CAA51885.1; !1PID:g313370 CLASSIFICATION #superfamily adenovirus late L1 52K protein SUMMARY #length 373 #molecular-weight 42330 #checksum 3837 SEQUENCE /// ENTRY WMADH2 #type complete TITLE late L2 mu core protein precursor - human adenovirus 2 ORGANISM #formal_name Mastadenovirus h2 #common_name human adenovirus 2 #note host Homo sapiens (man) DATE 30-Sep-1989 #sequence_revision 30-Jun-1993 #text_change 31-Dec-1993 ACCESSIONS D03837; A30970 REFERENCE A03837 !$#authors Alestroem, P.; Akusjaervi, G.; Lager, M.; Yeh-kai, L.; !1Pettersson, U. !$#journal J. Biol. Chem. (1984) 259:13980-13985 !$#title Genes encoding the core proteins of adenovirus type 2. !$#cross-references MUID:85054835; PMID:6094534 !$#accession D03837 !'##molecule_type DNA !'##residues 1-80 ##label ALE !'##cross-references GB:J01917 REFERENCE A30970 !$#authors Weber, J.M.; Anderson, C.W. !$#journal J. Virol. (1988) 62:1741-1745 !$#title Identification of the gene coding for the precursor of !1adenovirus core protein X. !$#cross-references MUID:88188260; PMID:3357209 !$#accession A30970 !'##molecule_type protein !'##residues 2-80 ##label WEB GENETICS !$#map_position 49.2-49.9 CLASSIFICATION #superfamily adenovirus late L2 mu core protein KEYWORDS core protein; DNA binding; late protein FEATURE !$32-50 #product late L2 mu core protein #status experimental !8#label MAT SUMMARY #length 80 #molecular-weight 8846 #checksum 6583 SEQUENCE /// ENTRY A45393 #type complete TITLE late L2 mu core protein precursor - human adenovirus 12 (strain Huie) ORGANISM #formal_name Mastadenovirus h12 #common_name human adenovirus 12 DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS A45393; C45393; S33940 REFERENCE A45393 !$#authors Freimuth, P.; Anderson, C.W. !$#journal Virology (1993) 193:348-355 !$#title Human adenovirus serotype 12 virion precursors pMu and pVI !1are cleaved at amino-terminal and carboxy-terminal sites !1that conform to the adenovirus 2 endoproteinase cleavage !1consensus sequence. !$#cross-references MUID:93174944; PMID:8438575 !$#accession A45393 !'##molecule_type DNA !'##residues 1-72 ##label FRE !'##cross-references GB:L02237; NID:g209993; PIDN:AAA42515.1; !1PID:g209994 !$#accession C45393 !'##molecule_type protein !'##residues 28-42 ##label FR2 REFERENCE S33928 !$#authors Sprengel, J. !$#submission submitted to the EMBL Data Library, June 1993 !$#accession S33940 !'##status preliminary !'##molecule_type DNA !'##residues 1-72 ##label SPR !'##cross-references EMBL:X73487; NID:g313361; PIDN:CAA51889.1; !1PID:g313374 CLASSIFICATION #superfamily adenovirus late L2 mu core protein KEYWORDS core protein; DNA binding; late protein FEATURE !$28-42 #product late L2 mu core protein #status experimental !8#label MAT SUMMARY #length 72 #molecular-weight 7971 #checksum 3913 SEQUENCE /// ENTRY DQAD62 #type complete TITLE probable DNA-binding protein - human adenovirus 2 ORGANISM #formal_name Mastadenovirus h2 #common_name human adenovirus 2 DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 12-Jun-1998 ACCESSIONS A93421; C92351; C92352; A03832 REFERENCE A93421 !$#authors Virtanen, A.; Alestrom, P.; Persson, H.; Katze, M.G.; !1Pettersson, U. !$#journal Nucleic Acids Res. (1982) 10:2539-2548 !$#title An adenovirus agnogene. !$#cross-references MUID:82196890; PMID:6281734 !$#accession A93421 !'##molecule_type DNA !'##residues 1-145 ##label VIR REFERENCE A92351 !$#authors Gingeras, T.R.; Sciaky, D.; Gelinas, R.E.; Bing-Dong, J.; !1Yen, C.E.; Kelly, M.M.; Bullock, P.A.; Parsons, B.L.; !1O'Neill, K.E.; Roberts, R.J. !$#journal J. Biol. Chem. (1982) 257:13475-13491 !$#title Nucleotide sequences from the adenovirus-2 genome. !$#cross-references MUID:83056843; PMID:7142161 !$#accession C92351 !'##molecule_type DNA !'##residues 1-145 ##label GIN REFERENCE A92352 !$#authors Alestrom, P.; Akusjarvi, G.; Pettersson, M.; Pettersson, U. !$#journal J. Biol. Chem. (1982) 257:13492-13498 !$#title DNA sequence analysis of the region encoding the terminal !1protein and the hypothetical N-gene product of adenovirus !1type 2. !$#cross-references MUID:83056844; PMID:7142162 !$#accession C92352 !'##molecule_type DNA !'##residues 1-145 ##label ALE COMMENT This protein, also called agnoprotein, may have a regulatory !1role in nucleic acid-protein interactions. GENETICS !$#map_position 21.3-22.2 !$#introns 138/3 CLASSIFICATION #superfamily adenovirus DNA-binding protein KEYWORDS DNA binding SUMMARY #length 145 #molecular-weight 16102 #checksum 9880 SEQUENCE /// ENTRY W7AD25 #type complete TITLE early E2A DNA-binding protein - human adenovirus 5 ORGANISM #formal_name Mastadenovirus h5 #common_name human adenovirus 5 #note host Homo sapiens (man) DATE 30-Apr-1981 #sequence_revision 02-Apr-1982 #text_change 23-Feb-1997 ACCESSIONS A03833 REFERENCE A93735 !$#authors Kruijer, W.; van Schaik, F.M.A.; Sussenbach, J.S. !$#journal Nucleic Acids Res. (1981) 9:4439-4457 !$#title Structure and organization of the gene coding for the DNA !1binding protein of adenovirus type 5. !$#cross-references MUID:82059474; PMID:6117824 !$#accession A03833 !'##molecule_type DNA !'##residues 1-529 ##label KRU GENETICS !$#map_position 59.1-71.4 CLASSIFICATION #superfamily adenovirus early E2A DNA-binding protein KEYWORDS DNA binding; early protein; phosphoprotein; zinc finger SUMMARY #length 529 #molecular-weight 59139 #checksum 803 SEQUENCE /// ENTRY W7AD22 #type complete TITLE early E2A DNA-binding protein - human adenovirus 2 ORGANISM #formal_name Mastadenovirus h2 #common_name human adenovirus 2 #note host Homo sapiens (man) DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 23-Feb-1997 ACCESSIONS B03833; C03833; A03833 REFERENCE A93434 !$#authors Kruijer, W.; Van Schaik, F.M.A.; Sussenbach, J.S. !$#journal Nucleic Acids Res. (1982) 10:4493-4500 !$#title Nucleotide sequence of the gene encoding adenovirus type 2 !1DNA binding protein. !$#cross-references MUID:83038612; PMID:6985485 !$#accession B03833 !'##molecule_type DNA !'##residues 1-529 ##label KRU REFERENCE A93720 !$#authors Akusjarvi, G.; Zabielski, J.; Perricaudet, M.; Pettersson, !1U. !$#journal Nucleic Acids Res. (1981) 9:1-17 !$#title The sequence of the 3' non-coding region of the hexon mRNA !1discloses a novel adenovirus gene. !$#cross-references MUID:81150446; PMID:6259616 !$#accession C03833 !'##molecule_type DNA !'##residues 438-529 ##label AKU GENETICS !$#map_position 59.1-71.4 CLASSIFICATION #superfamily adenovirus early E2A DNA-binding protein KEYWORDS DNA binding; early protein; phosphoprotein; zinc finger SUMMARY #length 529 #molecular-weight 59086 #checksum 2059 SEQUENCE /// ENTRY ERADA4 #type complete TITLE early E2A DNA-binding protein - human adenovirus 4 ORGANISM #formal_name Mastadenovirus h4 #common_name human adenovirus 4 #note host Homo sapiens (man) DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 16-Jul-1999 ACCESSIONS A23324 REFERENCE A23324 !$#authors Kitchingman, G.R. !$#journal Virology (1985) 146:90-101 !$#title Sequence of the DNA-binding protein of a human subgroup E !1adenovirus (type 4): comparisons with subgroup A (type 12), !1subgroup B (type 7), and subgroup C (type 5). !$#cross-references MUID:85301976; PMID:4041089 !$#accession A23324 !'##molecule_type DNA !'##residues 1-512 ##label KIT !'##cross-references GB:M12407; NID:g209872; PIDN:AAA42465.1; !1PID:g209873 GENETICS !$#map_position 61-67 CLASSIFICATION #superfamily adenovirus early E2A DNA-binding protein KEYWORDS DNA binding; early protein; phosphoprotein; zinc finger SUMMARY #length 512 #molecular-weight 57367 #checksum 6144 SEQUENCE /// ENTRY ERADA7 #type complete TITLE early E2A DNA-binding protein - human adenovirus 7 ORGANISM #formal_name Mastadenovirus h7 #common_name human adenovirus 7 #note host Homo sapiens (man) DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 16-Jul-1999 ACCESSIONS A03834 REFERENCE A03834 !$#authors Quinn, C.O.; Kitchingman, G.R. !$#journal J. Biol. Chem. (1984) 259:5003-5009 !$#title Sequence of the DNA-binding protein gene of a human subgroup !1B adenovirus (type 7). Comparisons with subgroup C (type 5) !1and subgroup A (type 12). !$#cross-references MUID:84185604; PMID:6325415 !$#accession A03834 !'##molecule_type DNA !'##residues 1-517 ##label QUI !'##cross-references GB:K02530; NID:g209936; PIDN:AAA42508.1; !1PID:g209937 CLASSIFICATION #superfamily adenovirus early E2A DNA-binding protein KEYWORDS DNA binding; early protein; phosphoprotein; zinc finger SUMMARY #length 517 #molecular-weight 58306 #checksum 1093 SEQUENCE /// ENTRY ERAD12 #type complete TITLE early E2A DNA-binding protein - human adenovirus 12 ORGANISM #formal_name Mastadenovirus h12 #common_name human adenovirus 12 #note host Homo sapiens (man) DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 16-Jul-1999 ACCESSIONS A03835; S33944 REFERENCE A03835 !$#authors Kruijer, W.; van Schaik, F.M.A.; Speijer, J.G.; Sussenbach, !1J.S. !$#journal Virology (1983) 128:140-153 !$#title Structure and function of adenovirus DNA binding protein: !1comparison of the amino acid sequences of the Ad5 and Ad12 !1proteins derived from the nucleotide sequence of the !1corresponding genes. !$#cross-references MUID:83277521; PMID:6308889 !$#accession A03835 !'##molecule_type DNA !'##residues 1-484 ##label KRU !'##cross-references GB:V01483; NID:g58462; PIDN:CAA24732.1; PID:g58464 REFERENCE S33928 !$#authors Sprengel, J. !$#submission submitted to the EMBL Data Library, June 1993 !$#accession S33944 !'##status preliminary !'##molecule_type DNA !'##residues 1-484 ##label SPR !'##cross-references EMBL:X73487; NID:g313361; PIDN:CAA51893.1; !1PID:g313378 CLASSIFICATION #superfamily adenovirus early E2A DNA-binding protein KEYWORDS DNA binding; early protein; phosphoprotein; zinc finger SUMMARY #length 484 #molecular-weight 54998 #checksum 8562 SEQUENCE /// ENTRY ERAD40 #type complete TITLE early E2A DNA-binding protein - human adenovirus 40 ORGANISM #formal_name Mastadenovirus h40 #common_name human adenovirus 40 DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS A28645 REFERENCE A94371 !$#authors Vos, H.L.; van der Lee, F.M.; Reemst, A.M.C.B.; van Loon, !1A.E.; Sussenbach, J.S. !$#journal Virology (1988) 163:1-10 !$#title The genes encoding the DNA binding protein and the 23K !1protease of adenovirus types 40 and 41. !$#cross-references MUID:88160034; PMID:3279700 !$#accession A28645 !'##molecule_type DNA !'##residues 1-473 ##label VOS !'##cross-references GB:L19443; NID:g303969; PIDN:AAC13969.1; !1PID:g303991 CLASSIFICATION #superfamily adenovirus early E2A DNA-binding protein KEYWORDS DNA binding; early protein; phosphoprotein; zinc finger SUMMARY #length 473 #molecular-weight 53335 #checksum 7790 SEQUENCE /// ENTRY ERAD41 #type complete TITLE early E2A DNA-binding protein - human adenovirus 41 ORGANISM #formal_name Mastadenovirus h41 #common_name human adenovirus 41 DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS D28645; S10206 REFERENCE A94371 !$#authors Vos, H.L.; van der Lee, F.M.; Reemst, A.M.C.B.; van Loon, !1A.E.; Sussenbach, J.S. !$#journal Virology (1988) 163:1-10 !$#title The genes encoding the DNA binding protein and the 23K !1protease of adenovirus types 40 and 41. !$#cross-references MUID:88160034; PMID:3279700 !$#accession D28645 !'##molecule_type DNA !'##residues 1-474 ##label VOS !'##cross-references GB:M21163; NID:g209865; PIDN:AAA42463.1; !1PID:g209870 REFERENCE S10206 !$#authors Slemenda, S.B.; Pieniazek, N.J.; Velarde Jr., J.; Pieniazek, !1D.; Luftig, R.B. !$#journal Nucleic Acids Res. (1990) 18:3069 !$#title Nucleotide sequence of the region coding for 100K and 33K !1proteins of human enteric adenovirus type 41 (Tak). !$#cross-references MUID:90272433; PMID:2349115 !$#accession S10206 !'##status translation not shown !'##molecule_type DNA !'##residues 1-33 ##label SLE !'##cross-references EMBL:X52532; NID:g58438; PIDN:CAA36759.1; !1PID:g58439 CLASSIFICATION #superfamily adenovirus early E2A DNA-binding protein KEYWORDS DNA binding; early protein; phosphoprotein; zinc finger SUMMARY #length 474 #molecular-weight 53658 #checksum 6783 SEQUENCE /// ENTRY FOAD72 #type complete TITLE major core protein VII precursor - human adenovirus 2 ORGANISM #formal_name Mastadenovirus h2 #common_name human adenovirus 2 #note host Homo sapiens (man) DATE 18-Apr-1984 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS C03837; A03836 REFERENCE A03837 !$#authors Alestroem, P.; Akusjaervi, G.; Lager, M.; Yeh-kai, L.; !1Pettersson, U. !$#journal J. Biol. Chem. (1984) 259:13980-13985 !$#title Genes encoding the core proteins of adenovirus type 2. !$#cross-references MUID:85054835; PMID:6094534 !$#accession C03837 !'##molecule_type DNA !'##residues 1-198 ##label ALE !'##cross-references GB:J01917; NID:g209811; PIDN:AAA92212.1; !1PID:g209828 REFERENCE A03836 !$#authors Sung, M.T.; Cao, T.M.; Coleman, R.T.; Budelier, K.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:2902-2906 !$#title Gene and protein sequences of adenovirus protein VII, a !1hybrid basic chromosomal protein. !$#cross-references MUID:83221511; PMID:6574459 !$#accession A03836 !'##molecule_type DNA !'##residues 1-111;113-198 ##label SUN !'##cross-references GB:J01917 GENETICS !$#map_position 43-45 CLASSIFICATION #superfamily adenovirus major core protein VII KEYWORDS core protein; late protein FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-198 #product major core protein VII #status predicted !8#label MCP SUMMARY #length 198 #molecular-weight 21992 #checksum 2271 SEQUENCE /// ENTRY FOADH5 #type fragment TITLE major core protein VII precursor - human adenovirus 5 (fragment) ORGANISM #formal_name Mastadenovirus h5 #common_name human adenovirus 5 #note host Homo sapiens (man) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS PT0067 REFERENCE JT0337 !$#authors Neumann, R.; Chroboczek, J.; Jacrot, B. !$#journal Gene (1988) 69:153-157 !$#title Determination of the nucleotide sequence for the penton-base !1gene of human adenovirus type 5. !$#cross-references MUID:89137988; PMID:3224820 !$#accession PT0067 !'##molecule_type DNA !'##residues 1-136 ##label NEU !'##cross-references GB:M22141; NID:g210001; PIDN:AAA42520.1; !1PID:g554592 CLASSIFICATION #superfamily adenovirus major core protein VII KEYWORDS core protein; late protein FEATURE !$25-136 #product major core protein VII (fragment) #status !8predicted #label ACP SUMMARY #length 136 #checksum 7401 SEQUENCE /// ENTRY B46116 #type complete TITLE major core protein VII precursor - canine adenovirus 1 (strain Utrecht) ALTERNATE_NAMES PVII protein ORGANISM #formal_name Mastadenovirus can1 #common_name canine adenovirus 1 DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 04-Mar-1994 ACCESSIONS B46116 REFERENCE A46116 !$#authors Cai, F.; Weber, J.M. !$#journal Virology (1993) 193:986-988 !$#title Primary structure of the canine adenovirus PVII protein: !1functional implications. !$#cross-references MUID:93212535; PMID:8460501 !$#accession B46116 !'##molecule_type DNA !'##residues 1-132 ##label CAI !'##cross-references GB:S57840 CLASSIFICATION #superfamily adenovirus major core protein VII KEYWORDS core protein; late protein FEATURE !$24-132 #product major core protein VII #status predicted !8#label MCP SUMMARY #length 132 #molecular-weight 14627 #checksum 6013 SEQUENCE /// ENTRY FOADM2 #type complete TITLE minor core protein pV - human adenovirus 2 ORGANISM #formal_name Mastadenovirus h2 #common_name human adenovirus 2 #note host Homo sapiens (man) DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 04-Mar-1994 ACCESSIONS A03837 REFERENCE A03837 !$#authors Alestroem, P.; Akusjaervi, G.; Lager, M.; Yeh-kai, L.; !1Pettersson, U. !$#journal J. Biol. Chem. (1984) 259:13980-13985 !$#title Genes encoding the core proteins of adenovirus type 2. !$#cross-references MUID:85054835; PMID:6094534 !$#accession A03837 !'##molecule_type DNA !'##residues 1-369 ##label ALE CLASSIFICATION #superfamily adenovirus minor core protein pV KEYWORDS core protein; late protein SUMMARY #length 369 #molecular-weight 41720 #checksum 8602 SEQUENCE /// ENTRY FOADM5 #type complete TITLE minor core protein pV - human adenovirus 5 ORGANISM #formal_name Mastadenovirus h5 #common_name human adenovirus 5 #note host Homo sapiens (man) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS C39449 REFERENCE A39449 !$#authors Chroboczek, J.; Bieber, F.; Jacrot, B. !$#journal Virology (1992) 186:280-285 !$#title The sequence of the genome of adenovirus type 5 and its !1comparison with the genome of adenovirus type 2. !$#cross-references MUID:92087470; PMID:1727603 !$#accession C39449 !'##molecule_type DNA !'##residues 1-368 ##label CHR !'##cross-references GB:M73260; GB:M29978; NID:g209842; PIDN:AAA96409.1; !1PID:g209846 CLASSIFICATION #superfamily adenovirus minor core protein pV KEYWORDS core protein; late protein SUMMARY #length 368 #molecular-weight 41446 #checksum 5293 SEQUENCE /// ENTRY WMADL2 #type fragment TITLE late 100K protein - human adenovirus 2 (fragment) ORGANISM #formal_name Mastadenovirus h2 #common_name human adenovirus 2 DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 04-Mar-1994 ACCESSIONS B03838; A03838 REFERENCE A91583 !$#authors Galibert, F.; Herisse, J.; Courtois, G. !$#journal Gene (1979) 6:1-22 !$#title Nucleotide sequence of the EcoRI-F fragment of adenovirus 2 !1genome. !$#cross-references MUID:80004828; PMID:478297 !$#accession B03838 !'##molecule_type DNA !'##residues 1-296 ##label GAL COMMENT The 100K protein is a late nonstructural protein involved in !1transport of hexon from cytoplasm to the nucleus. GENETICS !$#map_position 66.4-71.4 CLASSIFICATION #superfamily adenovirus late 100K protein KEYWORDS late protein SUMMARY #length 296 #checksum 2215 SEQUENCE /// ENTRY WMAD15 #type complete TITLE late 100K protein - human adenovirus 5 ORGANISM #formal_name Mastadenovirus h5 #common_name human adenovirus 5 DATE 02-Apr-1982 #sequence_revision 30-Sep-1992 #text_change 05-Sep-1997 ACCESSIONS A39449; A03838 REFERENCE A39449 !$#authors Chroboczek, J.; Bieber, F.; Jacrot, B. !$#journal Virology (1992) 186:280-285 !$#title The sequence of the genome of adenovirus type 5 and its !1comparison with the genome of adenovirus type 2. !$#cross-references MUID:92087470; PMID:1727603 !$#accession A39449 !'##molecule_type DNA !'##residues 1-807 ##label CHR !'##cross-references GB:M73260 REFERENCE A93735 !$#authors Kruijer, W.; van Schaik, F.M.A.; Sussenbach, J.S. !$#journal Nucleic Acids Res. (1981) 9:4439-4457 !$#title Structure and organization of the gene coding for the DNA !1binding protein of adenovirus type 5. !$#cross-references MUID:82059474; PMID:6117824 !$#accession A03838 !'##molecule_type DNA !'##residues 1-593 ##label KRU !'##cross-references GB:J01966; NID:g209789; PID:g209807 COMMENT The 100K protein is a late nonstructural protein involved in !1transport of hexon from cytoplasm to the nucleus. GENETICS !$#map_position 66.4-71.4 CLASSIFICATION #superfamily adenovirus late 100K protein KEYWORDS late protein; nonstructural protein SUMMARY #length 807 #molecular-weight 90212 #checksum 5990 SEQUENCE /// ENTRY WMAD40 #type fragment TITLE late 100K protein - human adenovirus 40 (fragment) ORGANISM #formal_name Mastadenovirus h40 #common_name human adenovirus 40 DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 07-Nov-1997 ACCESSIONS C28645 REFERENCE A94371 !$#authors Vos, H.L.; van der Lee, F.M.; Reemst, A.M.C.B.; van Loon, !1A.E.; Sussenbach, J.S. !$#journal Virology (1988) 163:1-10 !$#title The genes encoding the DNA binding protein and the 23K !1protease of adenovirus types 40 and 41. !$#cross-references MUID:88160034; PMID:3279700 !$#accession C28645 !'##molecule_type DNA !'##residues 1-438 ##label VOS !'##cross-references GB:L19443; NID:g303969 CLASSIFICATION #superfamily adenovirus late 100K protein KEYWORDS late protein SUMMARY #length 438 #checksum 2203 SEQUENCE /// ENTRY WMAD41 #type complete TITLE late 100K protein - human adenovirus 41 ORGANISM #formal_name Mastadenovirus h41 #common_name human adenovirus 41 DATE 30-Sep-1989 #sequence_revision 19-Oct-1995 #text_change 16-Jul-1999 ACCESSIONS S10207; F28645 REFERENCE S10206 !$#authors Slemenda, S.B.; Pieniazek, N.J.; Velarde Jr., J.; Pieniazek, !1D.; Luftig, R.B. !$#journal Nucleic Acids Res. (1990) 18:3069 !$#title Nucleotide sequence of the region coding for 100K and 33K !1proteins of human enteric adenovirus type 41 (Tak). !$#cross-references MUID:90272433; PMID:2349115 !$#accession S10207 !'##status translation not shown !'##molecule_type DNA !'##residues 1-777 ##label SLE !'##cross-references EMBL:X52532; NID:g58438; PIDN:CAA36760.1; !1PID:g58440 REFERENCE A94371 !$#authors Vos, H.L.; van der Lee, F.M.; Reemst, A.M.C.B.; van Loon, !1A.E.; Sussenbach, J.S. !$#journal Virology (1988) 163:1-10 !$#title The genes encoding the DNA binding protein and the 23K !1protease of adenovirus types 40 and 41. !$#cross-references MUID:88160034; PMID:3279700 !$#accession F28645 !'##molecule_type DNA !'##residues 1-579 ##label VOS !'##cross-references GB:X52532; NID:g58438; PIDN:CAA36760.1; PID:g58440 CLASSIFICATION #superfamily adenovirus late 100K protein KEYWORDS late protein SUMMARY #length 777 #molecular-weight 87308 #checksum 1860 SEQUENCE /// ENTRY UZADP2 #type complete TITLE terminal protein precursor - human adenovirus 2 ALTERNATE_NAMES Bellett protein ORGANISM #formal_name Mastadenovirus h2 #common_name human adenovirus 2 DATE 05-Apr-1983 #sequence_revision 31-Dec-1991 #text_change 24-Apr-1998 ACCESSIONS A92353; B92351; B92352; A03839 REFERENCE A92353 !$#authors Smart, J.E.; Stillman, B.W. !$#journal J. Biol. Chem. (1982) 257:13499-13506 !$#title Adenovirus terminal protein precursor. Partial amino acid !1sequence and the site of covalent linkage to virus DNA. !$#cross-references MUID:83056845; PMID:7142163 !$#accession A92353 !'##molecule_type DNA !'##residues 1-653 ##label SMA !'##note this protein is covalently attached to the termini of !1replicating DNA in vivo and nascent DNA synthesized in vitro REFERENCE A92351 !$#authors Gingeras, T.R.; Sciaky, D.; Gelinas, R.E.; Bing-Dong, J.; !1Yen, C.E.; Kelly, M.M.; Bullock, P.A.; Parsons, B.L.; !1O'Neill, K.E.; Roberts, R.J. !$#journal J. Biol. Chem. (1982) 257:13475-13491 !$#title Nucleotide sequences from the adenovirus-2 genome. !$#cross-references MUID:83056843; PMID:7142161 !$#accession B92351 !'##molecule_type DNA !'##residues 1-653 ##label GIN REFERENCE A92352 !$#authors Alestrom, P.; Akusjarvi, G.; Pettersson, M.; Pettersson, U. !$#journal J. Biol. Chem. (1982) 257:13492-13498 !$#title DNA sequence analysis of the region encoding the terminal !1protein and the hypothetical N-gene product of adenovirus !1type 2. !$#cross-references MUID:83056844; PMID:7142162 !$#accession B92352 !'##molecule_type DNA !'##residues 1-653 ##label ALE COMMENT This gene is located on E2B region of the genome. FUNCTION !$#description precursor form primes viral DNA replication by a covalent !1bond to deoxycytosine at the 5' terminus, then is cleaved to !1mature form during virion maturation CLASSIFICATION #superfamily adenovirus terminal protein KEYWORDS DNA replication; early protein; genome-linked protein; !1phosphoprotein FEATURE !$562 #binding_site phosphoryl-DNA (Ser) (covalent) #status !8experimental SUMMARY #length 653 #molecular-weight 74697 #checksum 6021 SEQUENCE /// ENTRY UZADP5 #type complete TITLE terminal protein precursor - human adenovirus 5 ALTERNATE_NAMES Bellett protein ORGANISM #formal_name Mastadenovirus h5 #common_name human adenovirus 5 #note host Homo sapiens (man) DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 16-Jul-1999 ACCESSIONS A03840 REFERENCE A91508 !$#authors Dekker, B.M.M.; van Ormondt, H. !$#journal Gene (1984) 27:115-120 !$#title The nucleotide sequence of fragment HindIII-C of human !1adenovirus type 5 DNA (map positions 17.1-31.7). !$#cross-references MUID:84183604; PMID:6325298 !$#accession A03840 !'##molecule_type DNA !'##residues 1-653 ##label DEK !'##cross-references EMBL:X02996; NID:g58484; PIDN:CAA26750.1; !1PID:g58496 REFERENCE A30626 !$#authors Desiderio, S.V.; Kelly Jr., T.J. !$#journal J. Mol. Biol. (1981) 145:319-337 !$#title Structure of the linkage between adenovirus DNA and the 55, !1000 molecular weight terminal protein. !$#cross-references MUID:81267318; PMID:7265205 !$#contents annotation; chemical characterization of covalent linkage !1between protein and DNA FUNCTION !$#description precursor form primes viral DNA replication by a covalent !1bond to deoxycytosine at the 5' terminus, then is cleaved to !1mature form during virion maturation CLASSIFICATION #superfamily adenovirus terminal protein KEYWORDS DNA replication; genome-linked protein; phosphoprotein FEATURE !$562 #binding_site phosphoryl-DNA (Ser) (covalent) #status !8experimental SUMMARY #length 653 #molecular-weight 74654 #checksum 6306 SEQUENCE /// ENTRY UZADP7 #type complete TITLE terminal protein precursor - human adenovirus 7 ALTERNATE_NAMES Bellett protein ORGANISM #formal_name Mastadenovirus h7 #common_name human adenovirus 7 DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 16-Jul-1999 ACCESSIONS A03841 REFERENCE A91498 !$#authors Engler, J.A.; Hoppe, M.S.; van Bree, M.P. !$#journal Gene (1983) 21:145-159 !$#title The nucleotide sequence of the genes encoded in early region !12b of human adenovirus type 7. !$#cross-references MUID:83183660; PMID:6301944 !$#accession A03841 !'##molecule_type DNA !'##residues 1-640 ##label ENG !'##cross-references GB:X03000; GB:J01981; GB:J01982; GB:J01983; !1GB:J01984; GB:J01985; GB:J01988; GB:J01989; GB:J01990; !1GB:J01992; GB:V00032; GB:V00033; GB:V00038; NID:g58514; !1PIDN:CAA26775.1; PID:g58532 FUNCTION !$#description precursor form primes viral DNA replication by a covalent !1bond to deoxycytosine at the 5' terminus, then is cleaved to !1mature form during virion maturation CLASSIFICATION #superfamily adenovirus terminal protein KEYWORDS DNA replication; genome-linked protein; phosphoprotein FEATURE !$549 #binding_site phosphoryl-DNA (Ser) (covalent) #status !8predicted SUMMARY #length 640 #molecular-weight 73745 #checksum 5331 SEQUENCE /// ENTRY UZAD12 #type complete TITLE terminal protein precursor - human adenovirus 12 ALTERNATE_NAMES Bellett protein ORGANISM #formal_name Mastadenovirus h12 #common_name human adenovirus 12 #note host Homo sapiens (man) DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 29-Oct-1999 ACCESSIONS B25770; S33935 REFERENCE A91557 !$#authors Shu, L.; Hong, J.S.; Wei, Y.F.; Engler, J.A. !$#journal Gene (1986) 46:187-195 !$#title Nucleotide sequence of the genes encoded in early region 2b !1of human adenovirus type 12. !$#cross-references MUID:87106854; PMID:3803925 !$#accession B25770 !'##molecule_type DNA !'##residues 1-606 ##label SHU REFERENCE S33928 !$#authors Sprengel, J. !$#submission submitted to the EMBL Data Library, June 1993 !$#accession S33935 !'##status preliminary !'##molecule_type DNA !'##residues 1-247,'L',249-404,'EL',407-606 ##label SPR !'##cross-references EMBL:X73487; NID:g313361; PIDN:CAA51884.1; !1PID:g313369 COMMENT This gene is located on E2B region of the genome. FUNCTION !$#description precursor form primes viral DNA replication by a covalent !1bond to deoxycytosine at the 5' terminus, then is cleaved to !1mature form during virion maturation CLASSIFICATION #superfamily adenovirus terminal protein KEYWORDS DNA replication; early protein; genome-linked protein; !1phosphoprotein FEATURE !$515 #binding_site phosphoryl-DNA (Ser) (covalent) #status !8predicted SUMMARY #length 606 #molecular-weight 69452 #checksum 7702 SEQUENCE /// ENTRY Q4ADA5 #type complete TITLE maturation (pIVa2) protein - human adenovirus 5 ORGANISM #formal_name Mastadenovirus h5 #common_name human adenovirus 5 DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 17-Feb-1995 ACCESSIONS A03842 REFERENCE A91489 !$#authors van Beveren, C.P.; Maat, J.; Dekker, B.M.M.; van Ormondt, H. !$#journal Gene (1981) 16:179-189 !$#title The nucleotide sequence of the gene for protein IVa2 and of !1the 5' leader segment of the major late mRNAs of adenovirus !1type 5. !$#cross-references MUID:82211779; PMID:7343420 !$#accession A03842 !'##molecule_type DNA !'##residues 1-449 ##label VAN !'##note the authors translated the codon ATC for residue 368 as Thr GENETICS !$#introns 5/1 CLASSIFICATION #superfamily adenovirus maturation protein KEYWORDS late protein SUMMARY #length 449 #molecular-weight 50887 #checksum 6102 SEQUENCE /// ENTRY Q4ADA2 #type complete TITLE maturation (pIVa2) protein - human adenovirus 2 ORGANISM #formal_name Mastadenovirus h2 #common_name human adenovirus 2 DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 04-Mar-1994 ACCESSIONS B03842; A03842 REFERENCE A92351 !$#authors Gingeras, T.R.; Sciaky, D.; Gelinas, R.E.; Bing-Dong, J.; !1Yen, C.E.; Kelly, M.M.; Bullock, P.A.; Parsons, B.L.; !1O'Neill, K.E.; Roberts, R.J. !$#journal J. Biol. Chem. (1982) 257:13475-13491 !$#title Nucleotide sequences from the adenovirus-2 genome. !$#cross-references MUID:83056843; PMID:7142161 !$#accession B03842 !'##molecule_type DNA !'##residues 1-449 ##label GIN GENETICS !$#introns 5/1 CLASSIFICATION #superfamily adenovirus maturation protein KEYWORDS late protein SUMMARY #length 449 #molecular-weight 50881 #checksum 6350 SEQUENCE /// ENTRY Q4ADA7 #type complete TITLE maturation (pIVa2) protein - human adenovirus 7 ORGANISM #formal_name Mastadenovirus h7 #common_name human adenovirus 7 DATE 05-Apr-1983 #sequence_revision 05-Apr-1983 #text_change 17-Feb-1995 ACCESSIONS A03843 REFERENCE A03843 !$#authors Engler, J.A.; van Bree, M.P. !$#journal Gene (1982) 19:71-80 !$#title The nucleotide sequence of the gene encoding protein IVa2 in !1human adenovirus type 7. !$#cross-references MUID:83054637; PMID:6292051 !$#accession A03843 !'##molecule_type DNA !'##residues 1-448 ##label ENG !'##note the authors translated the codon CCG for residue 66 as Glu CLASSIFICATION #superfamily adenovirus maturation protein SUMMARY #length 448 #molecular-weight 50678 #checksum 3823 SEQUENCE /// ENTRY Q5ADB2 #type complete TITLE polypeptide VI precursor - human adenovirus 2 ORGANISM #formal_name Mastadenovirus h2 #common_name human adenovirus 2 DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 25-Apr-1997 ACCESSIONS A03844 REFERENCE A03844 !$#authors Akusjarvi, G.; Persson, H. !$#journal J. Virol. (1981) 38:469-482 !$#title Gene and mRNA for precursor polypeptide VI from adenovirus !1type 2. !$#cross-references MUID:81218454; PMID:6985479 !$#accession A03844 !'##molecule_type DNA !'##residues 1-250 ##label AKU GENETICS !$#map_position 48.8-51.1 CLASSIFICATION #superfamily adenovirus polypeptide VI FEATURE !$34-239 #product polypeptide VI #status predicted #label MAT SUMMARY #length 250 #molecular-weight 27013 #checksum 9763 SEQUENCE /// ENTRY Q5ADB5 #type complete TITLE polypeptide VI precursor - human adenovirus 5 ORGANISM #formal_name Mastadenovirus h5 #common_name human adenovirus 5 #note host Homo sapiens (man) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS D39449 REFERENCE A39449 !$#authors Chroboczek, J.; Bieber, F.; Jacrot, B. !$#journal Virology (1992) 186:280-285 !$#title The sequence of the genome of adenovirus type 5 and its !1comparison with the genome of adenovirus type 2. !$#cross-references MUID:92087470; PMID:1727603 !$#accession D39449 !'##molecule_type DNA !'##residues 1-250 ##label CHR !'##cross-references GB:M73260; GB:M29978; NID:g209842; PIDN:AAA96411.1; !1PID:g209848 CLASSIFICATION #superfamily adenovirus polypeptide VI FEATURE !$34-239 #product polypeptide VI #status predicted #label MAT SUMMARY #length 250 #molecular-weight 26995 #checksum 404 SEQUENCE /// ENTRY B45393 #type complete TITLE polypeptide VI precursor - human adenovirus 12 (strain Huie) ORGANISM #formal_name Mastadenovirus h12 #common_name human adenovirus 12 DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS B45393; D45393; S33941 REFERENCE A45393 !$#authors Freimuth, P.; Anderson, C.W. !$#journal Virology (1993) 193:348-355 !$#title Human adenovirus serotype 12 virion precursors pMu and pVI !1are cleaved at amino-terminal and carboxy-terminal sites !1that conform to the adenovirus 2 endoproteinase cleavage !1consensus sequence. !$#cross-references MUID:93174944; PMID:8438575 !$#accession B45393 !'##molecule_type DNA !'##residues 1-265 ##label FRE !'##cross-references GB:L02237; NID:g209993; PIDN:AAA42516.1; !1PID:g209995 !$#accession D45393 !'##molecule_type protein !'##residues 34-254 ##label FR2 REFERENCE S33928 !$#authors Sprengel, J. !$#submission submitted to the EMBL Data Library, June 1993 !$#accession S33941 !'##status preliminary !'##molecule_type DNA !'##residues 1-265 ##label SPR !'##cross-references EMBL:X73487; NID:g313361; PIDN:CAA51890.1; !1PID:g313375 CLASSIFICATION #superfamily adenovirus polypeptide VI FEATURE !$34-254 #product polypeptide VI #status experimental #label !8MAT SUMMARY #length 265 #molecular-weight 28912 #checksum 7248 SEQUENCE /// ENTRY ERADF2 #type complete TITLE fiber protein - human adenovirus 2 ORGANISM #formal_name Mastadenovirus h2 #common_name human adenovirus 2 DATE 29-Jul-1981 #sequence_revision 02-Apr-1982 #text_change 30-Sep-1993 ACCESSIONS A93722; A93733; A03845 REFERENCE A93722 !$#authors Herisse, J.; Galibert, F. !$#journal Nucleic Acids Res. (1981) 9:1229-1240 !$#title Nucleotide sequence of the EcoRI E fragment of adenovirus 2 !1genome. !$#cross-references MUID:81198965; PMID:6262722 !$#accession A93722 !'##molecule_type DNA !'##residues 1-411 ##label HE1 REFERENCE A93733 !$#authors Herisse, J.; Rigolet, M.; Dupont de Dinechin, S.; Galibert, !1F. !$#journal Nucleic Acids Res. (1981) 9:4023-4042 !$#title Nucleotide sequence of adenovirus 2 DNA fragment encoding !1for the carboxylic region of the fiber protein and the !1entire E4 region. !$#cross-references MUID:82059444; PMID:6985482 !$#accession A93733 !'##molecule_type DNA !'##residues 382-582 ##label HE2 GENETICS !$#map_position 86.4-91.4 CLASSIFICATION #superfamily adenovirus fiber protein SUMMARY #length 582 #molecular-weight 61918 #checksum 9854 SEQUENCE /// ENTRY ERADF5 #type complete TITLE fiber protein - human adenovirus 5 ORGANISM #formal_name Mastadenovirus h5 #common_name human adenovirus 5 #note host Homo sapiens (man) DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jul-1999 ACCESSIONS A27404 REFERENCE A27404 !$#authors Chroboczek, J.; Jacrot, B. !$#journal Virology (1987) 161:549-554 !$#title The sequence of adenovirus fiber: similarities and !1differences between serotypes 2 and 5. !$#cross-references MUID:88072096; PMID:3686830 !$#accession A27404 !'##molecule_type DNA !'##residues 1-581 ##label CHR !'##cross-references GB:M18369; NID:g209930; PIDN:AAA42504.1; !1PID:g209931 CLASSIFICATION #superfamily adenovirus fiber protein KEYWORDS fiber protein; glycoprotein; homotrimer FEATURE !$77,82,231,232,314, !$322,469,500,537 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 581 #molecular-weight 61584 #checksum 6497 SEQUENCE /// ENTRY ERADF3 #type complete TITLE fiber protein - human adenovirus 3 ORGANISM #formal_name Mastadenovirus h3 #common_name human adenovirus 3 #note host Homo sapiens (man) DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 16-Jul-1999 ACCESSIONS A03846 REFERENCE A03846 !$#authors Signas, C.; Akusjarvi, G.; Pettersson, U. !$#journal J. Virol. (1985) 53:672-678 !$#title Adenovirus 3 fiber polypeptide gene: implications for the !1structure of the fiber protein. !$#cross-references MUID:85108162; PMID:2982041 !$#accession A03846 !'##molecule_type DNA !'##residues 1-319 ##label SIG !'##cross-references GB:X01998; GB:M12411; NID:g58473; PIDN:CAA26029.1; !1PID:g58474; NID:g209926; PID:g209928 !'##note the authors translated the codon GAA for residue 146 as Asp CLASSIFICATION #superfamily adenovirus fiber protein KEYWORDS fiber protein; glycoprotein; homotrimer FEATURE !$92,130,188 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 319 #molecular-weight 34815 #checksum 2111 SEQUENCE /// ENTRY ERADF7 #type complete TITLE fiber protein - human adenovirus 7 (strain Gomen) ORGANISM #formal_name Mastadenovirus h7 #common_name human adenovirus 7 #note host Homo sapiens (man) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS F31830 REFERENCE A94386 !$#authors Hong, J.S.; Mullis, K.G.; Engler, J.A. !$#journal Virology (1988) 167:545-553 !$#title Characterization of the early region 3 and fiber genes of !1Ad7. !$#cross-references MUID:89073758; PMID:2849239 !$#accession F31830 !'##molecule_type DNA !'##residues 1-325 ##label HON !'##cross-references GB:M23696; NID:g341012; PIDN:AAA53254.1; !1PID:g576461 CLASSIFICATION #superfamily adenovirus fiber protein KEYWORDS early protein; fiber protein; glycoprotein; homotrimer FEATURE !$81,192,284 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 325 #molecular-weight 35223 #checksum 6755 SEQUENCE /// ENTRY ERADF4 #type complete TITLE 60.5K fiber protein - human adenovirus 40 ORGANISM #formal_name Mastadenovirus h40 #common_name human adenovirus 40 #note host Homo sapiens (man) DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 22-Oct-1999 ACCESSIONS B30336 REFERENCE A30336 !$#authors Kidd, A.H.; Erasmus, M.J. !$#journal Virology (1989) 172:134-144 !$#title Sequence characterization of the adenovirus 40 fiber gene. !$#cross-references MUID:89370295; PMID:2773314 !$#accession B30336 !'##molecule_type DNA !'##residues 1-547 ##label KID !'##cross-references GB:M28822; NID:g409548; PIDN:AAA03234.1; !1PID:g209776 CLASSIFICATION #superfamily adenovirus fiber protein KEYWORDS early protein; fiber protein; glycoprotein; homotrimer FEATURE !$98,128,216,244,333, !$342,382,405,467 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 547 #molecular-weight 59113 #checksum 2107 SEQUENCE /// ENTRY ERADN2 #type complete TITLE 60.5K fiber protein - human adenovirus 41 ORGANISM #formal_name Mastadenovirus h41 #common_name human adenovirus 41 #note host Homo sapiens (man) DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS A34145; B45352; S09218; S06685 REFERENCE A34145 !$#authors Pieniazek, N.J.; Slemenda, S.B.; Pieniazek, D.; Velarde Jr., !1J.; Luftig, R.B. !$#journal Nucleic Acids Res. (1989) 17:9474 !$#title Sequence of human enteric adenovirus type 41 Tak fiber !1protein. !$#cross-references MUID:90067947; PMID:2587268 !$#accession A34145 !'##molecule_type DNA !'##residues 1-562 ##label PIE !'##cross-references EMBL:X16583; NID:g58566; PIDN:CAA34600.1; !1PID:g58567 !'##experimental_source strain Tak REFERENCE A45352 !$#authors Kidd, A.H.; Erasmus, M.J.; Tiemessen, C.T. !$#journal Virology (1990) 179:139-150 !$#title Fiber sequence heterogeneity in subgroup F adenoviruses. !$#cross-references MUID:91021015; PMID:2219717 !$#accession B45352 !'##molecule_type DNA !'##residues 1-562 ##label KID !'##cross-references GB:M60327; NID:g209932; PIDN:AAA42506.1; !1PID:g209934 !'##experimental_source strain FB585 REFERENCE S09217 !$#authors Pieniazek, N.J.; Slemenda, S.B.; Pieniazek, D.; Velarde Jr., !1J.; Luftig, R.B. !$#journal Nucleic Acids Res. (1990) 18:1901 !$#title Human enteric adenovirus type 41 (Tak) contains a second !1fiber protein gene. !$#cross-references MUID:90245595; PMID:2336370 !$#accession S09218 !'##molecule_type DNA !'##residues 1-14 ##label PI2 !'##cross-references EMBL:X17016; NID:g58478; PIDN:CAA34883.1; !1PID:g58480 !'##experimental_source strain Tak CLASSIFICATION #superfamily adenovirus fiber protein KEYWORDS early protein; fiber protein; glycoprotein; homotrimer FEATURE !$98,128,216,233,244, !$357,397,420,482 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 562 #molecular-weight 60600 #checksum 9341 SEQUENCE /// ENTRY ERADN1 #type complete TITLE 41K fiber protein - human adenovirus 41 ORGANISM #formal_name Mastadenovirus h41 #common_name human adenovirus 41 #note host Homo sapiens (man) DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jul-1999 ACCESSIONS S09217; A45352; S20695 REFERENCE S09217 !$#authors Pieniazek, N.J.; Slemenda, S.B.; Pieniazek, D.; Velarde Jr., !1J.; Luftig, R.B. !$#journal Nucleic Acids Res. (1990) 18:1901 !$#title Human enteric adenovirus type 41 (Tak) contains a second !1fiber protein gene. !$#cross-references MUID:90245595; PMID:2336370 !$#accession S09217 !'##molecule_type DNA !'##residues 1-387 ##label PIE !'##cross-references EMBL:X17016; NID:g58478; PIDN:CAA34882.1; !1PID:g58479 !'##experimental_source strain Tak REFERENCE A45352 !$#authors Kidd, A.H.; Erasmus, M.J.; Tiemessen, C.T. !$#journal Virology (1990) 179:139-150 !$#title Fiber sequence heterogeneity in subgroup F adenoviruses. !$#cross-references MUID:91021015; PMID:2219717 !$#accession A45352 !'##molecule_type DNA !'##residues 337-387 ##label KID !'##cross-references GB:M60327; NID:g209932; PIDN:AAA42505.1; !1PID:g209933 !'##experimental_source strain FB585 REFERENCE S20688 !$#authors Pienaziek, N.J.; Slemenda, S.B.; Pienazek, D.; Velarde Jr., !1J.; Luftig, R.B. !$#submission submitted to the EMBL Data Library, March 1990 !$#description Characterisation of the early region E3 of the human enteric !1adenovirus type 41 Tak. !$#accession S20695 !'##molecule_type DNA !'##residues 1-58 ##label PI2 !'##cross-references EMBL:X52198; NID:g58660; PIDN:CAA36450.1; !1PID:g58668 CLASSIFICATION #superfamily adenovirus fiber protein KEYWORDS early protein SUMMARY #length 387 #molecular-weight 41397 #checksum 9214 SEQUENCE /// ENTRY ERADY4 #type complete TITLE 41K fiber protein - human adenovirus 40 ORGANISM #formal_name Mastadenovirus h40 #common_name human adenovirus 40 #note host Homo sapiens (man) DATE 30-Jun-1990 #sequence_revision 31-Mar-1992 #text_change 03-May-1996 ACCESSIONS A40048; A30336 REFERENCE A40048 !$#authors Kidd, A.H. !$#submission submitted to the Protein Sequence Database, January 1992 !$#accession A40048 !'##molecule_type DNA !'##residues 1-387 ##label KID1 REFERENCE A30336 !$#authors Kidd, A.H.; Erasmus, M.J. !$#journal Virology (1989) 172:134-144 !$#title Sequence characterization of the adenovirus 40 fiber gene. !$#cross-references MUID:89370295; PMID:2773314 !$#accession A30336 !'##molecule_type DNA !'##residues 163-387 ##label KID2 !'##cross-references GB:M28822 CLASSIFICATION #superfamily adenovirus fiber protein KEYWORDS early protein SUMMARY #length 387 #molecular-weight 41376 #checksum 320 SEQUENCE /// ENTRY ERADFM #type complete TITLE fiber protein - mouse adenovirus 1 ORGANISM #formal_name Mastadenovirus mus1 #common_name mouse adenovirus 1 #note host Mus musculus (house mouse) DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS C33382 REFERENCE A33382 !$#authors Raviprakash, K.S.; Grunhaus, A.; El Kholy, M.A.; Horwitz, !1M.S. !$#journal J. Virol. (1989) 63:5455-5458 !$#title The mouse adenovirus type 1 contains an unusual E3 region. !$#cross-references MUID:90064816; PMID:2531236 !$#accession C33382 !'##molecule_type DNA !'##residues 1-613 ##label RAV !'##cross-references GB:M30594; NID:g209755; PIDN:AAA42434.1; !1PID:g209758 CLASSIFICATION #superfamily adenovirus fiber protein KEYWORDS early protein; fiber protein; glycoprotein; homotrimer FEATURE !$242,397,445,576 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 613 #molecular-weight 66801 #checksum 3443 SEQUENCE /// ENTRY ERADDG #type complete TITLE fiber protein - canine adenovirus 1 (strain Glaxo) ORGANISM #formal_name Mastadenovirus can1 #common_name canine adenovirus 1 DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS D40318 REFERENCE A40318 !$#authors Dragulev, B.P.; Sira, S.; Abouhaidar, M.G.; Campbell, J.B. !$#journal Virology (1991) 183:298-305 !$#title Sequence analysis of putative E3 and fiber genomic regions !1of two strains of canine adenovirus type 1. !$#cross-references MUID:91272490; PMID:1828920 !$#accession D40318 !'##molecule_type DNA !'##residues 1-543 ##label DRA !'##cross-references GB:M60937; NID:g210036; PIDN:AAA42536.1; !1PID:g210040 CLASSIFICATION #superfamily adenovirus fiber protein KEYWORDS fiber protein; glycoprotein; homotrimer FEATURE !$47,242,319,375,379, !$400,438,450,493 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 543 #molecular-weight 57029 #checksum 3288 SEQUENCE /// ENTRY XZAD32 #type complete TITLE penton protein (III) - human adenovirus 2 ORGANISM #formal_name Mastadenovirus h2 #common_name human adenovirus 2 #note host Homo sapiens (man) DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS A03847; B03837 REFERENCE A92461 !$#authors Roberts, R.J.; O'Neill, K.E.; Yen, C.E. !$#journal J. Biol. Chem. (1984) 259:13968-13975 !$#title DNA sequences from the adenovirus 2 genome. !$#cross-references MUID:85054833; PMID:6334081 !$#accession A03847 !'##molecule_type DNA !'##residues 1-571 ##label ROB !'##cross-references GB:J01917; NID:g209811; PIDN:AAA92211.1; !1PID:g209827 REFERENCE A03837 !$#authors Alestroem, P.; Akusjaervi, G.; Lager, M.; Yeh-kai, L.; !1Pettersson, U. !$#journal J. Biol. Chem. (1984) 259:13980-13985 !$#title Genes encoding the core proteins of adenovirus type 2. !$#cross-references MUID:85054835; PMID:6094534 !$#accession B03837 !'##molecule_type DNA !'##residues 295-571 ##label ALE !'##cross-references GB:J01917 CLASSIFICATION #superfamily adenovirus penton protein KEYWORDS late protein SUMMARY #length 571 #molecular-weight 63254 #checksum 3314 SEQUENCE /// ENTRY XZADH5 #type complete TITLE penton protein (III) - human adenovirus 5 ORGANISM #formal_name Mastadenovirus h5 #common_name human adenovirus 5 #note host Homo sapiens (man) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS JT0337 REFERENCE JT0337 !$#authors Neumann, R.; Chroboczek, J.; Jacrot, B. !$#journal Gene (1988) 69:153-157 !$#title Determination of the nucleotide sequence for the penton-base !1gene of human adenovirus type 5. !$#cross-references MUID:89137988; PMID:3224820 !$#accession JT0337 !'##molecule_type DNA !'##residues 1-571 ##label NEU !'##cross-references GB:M22141; NID:g210001; PIDN:AAA42519.1; !1PID:g210003 CLASSIFICATION #superfamily adenovirus penton protein KEYWORDS late protein SUMMARY #length 571 #molecular-weight 63292 #checksum 3774 SEQUENCE /// ENTRY S33938 #type complete TITLE penton protein (III) - human adenovirus 12 ORGANISM #formal_name Mastadenovirus h12 #common_name human adenovirus 12 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S33938 REFERENCE S33928 !$#authors Sprengel, J. !$#submission submitted to the EMBL Data Library, June 1993 !$#accession S33938 !'##status preliminary !'##molecule_type DNA !'##residues 1-497 ##label SPR !'##cross-references EMBL:X73487; NID:g313361; PIDN:CAA51887.1; !1PID:g313372 CLASSIFICATION #superfamily adenovirus penton protein SUMMARY #length 497 #molecular-weight 56393 #checksum 2182 SEQUENCE /// ENTRY S41389 #type complete TITLE penton protein (III) - human adenovirus 3 ALTERNATE_NAMES penton base protein ORGANISM #formal_name Mastadenovirus h3 #common_name human adenovirus 3 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S41389 REFERENCE S41388 !$#authors Cuzange, A.; Chroboczek, J.; Jacrot, B. !$#submission submitted to the EMBL Data Library, January 1994 !$#description The penton base of human adenovirus type 3 has the RGD !1motif. !$#accession S41389 !'##molecule_type DNA !'##residues 1-544 ##label CUZ !'##cross-references EMBL:Z29487; NID:g444048; PIDN:CAA82622.1; !1PID:g444050 !'##experimental_source serotype 3 CLASSIFICATION #superfamily adenovirus penton protein SUMMARY #length 544 #molecular-weight 61816 #checksum 8903 SEQUENCE /// ENTRY XZAD10 #type complete TITLE penton protein (III) - fowl adenovirus 10 (strain SA2) ALTERNATE_NAMES penton base protein ORGANISM #formal_name Aviadenovirus gal10 #common_name fowl adenovirus 10 DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS A42546 REFERENCE A42546 !$#authors Sheppard, M.; Trist, H. !$#journal Virology (1992) 188:881-886 !$#title Characterization of the avian adenovirus penton base. !$#cross-references MUID:92263795; PMID:1316685 !$#accession A42546 !'##molecule_type DNA !'##residues 1-525 ##label SHE !'##cross-references GB:M87008; NID:g209999; PIDN:AAA42517.1; !1PID:g210000 CLASSIFICATION #superfamily adenovirus penton protein KEYWORDS late protein SUMMARY #length 525 #molecular-weight 57405 #checksum 5352 SEQUENCE /// ENTRY HXAD2 #type complete TITLE hexon protein - human adenovirus 2 (tentative sequence) ALTERNATE_NAMES late protein 2 ORGANISM #formal_name Mastadenovirus h2 #common_name human adenovirus 2 #note host Homo sapiens (man) DATE 02-Apr-1982 #sequence_revision 28-Aug-1985 #text_change 31-Mar-2000 ACCESSIONS A94597; A92327; A93720; A03848 REFERENCE A94597 !$#authors Alestrom, P.; Akusjarvi, G.; Pettersson, M.; Pettersson, U. !$#submission submitted to the Atlas, November 1982 !$#contents revisions !$#accession A94597 !'##molecule_type DNA !'##residues 145-165;450-457 ##label ALE REFERENCE A92327 !$#authors Jornvall, H.; Akusjarvi, G.; Alestrom, P.; von !1Bahr-Lindstrom, H.; Pettersson, U.; Appella, E.; Fowler, !1A.V.; Philipson, L. !$#journal J. Biol. Chem. (1981) 256:6181-6186 !$#title The adenovirus hexon protein. The primary structure of the !1polypeptide and its correlation with the hexon gene. !$#cross-references MUID:81215564; PMID:6263909 !$#accession A92327 !'##molecule_type protein !'##residues 1-454;456-967 ##label JOR !'##note this is the final paper of a series giving the experimental !1details !'##note sequences of residues 1-101, 239-261, 275-301, 317-325, !1329-364, 501-525, 529-550, 612-628, and 800-967 were !1confirmed by the corresponding nucleotide sequences !'##note the sequences of residues 146-159 and 234-235 were assigned !1based on preliminary data REFERENCE A93720 !$#authors Akusjarvi, G.; Zabielski, J.; Perricaudet, M.; Pettersson, !1U. !$#journal Nucleic Acids Res. (1981) 9:1-17 !$#title The sequence of the 3' non-coding region of the hexon mRNA !1discloses a novel adenovirus gene. !$#cross-references MUID:81150446; PMID:6259616 !$#accession A93720 !'##molecule_type DNA !'##residues 922-966 ##label AKU COMMENT This protein is one of the structural proteins in the viral !1coat and is synthesized during late infection. GENETICS !$#map_position 51.7-61.3 CLASSIFICATION #superfamily adenovirus hexon protein KEYWORDS acetylated amino end; coat protein; hexon protein; late !1protein FEATURE !$1 #modified_site acetylated amino end (Ala) #status !8experimental SUMMARY #length 967 #molecular-weight 108934 #checksum 8240 SEQUENCE /// ENTRY HXAD5 #type complete TITLE hexon protein - human adenovirus 5 ORGANISM #formal_name Mastadenovirus h5 #common_name human adenovirus 5 #note host Homo sapiens (man) DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 22-Oct-1999 ACCESSIONS A03849 REFERENCE A03849 !$#authors Kinloch, R.; Mackay, N.; Mautner, V. !$#journal J. Biol. Chem. (1984) 259:6431-6436 !$#title Adenovirus hexon. Sequence comparison of subgroup C !1serotypes 2 and 5. !$#cross-references MUID:84212465; PMID:6202684 !$#accession A03849 !'##molecule_type DNA !'##residues 1-952 ##label KIN !'##cross-references GB:X02997; GB:J01966; GB:J01980; GB:K02368; !1GB:V00029; GB:V00030; NID:g58498; PIDN:CAA26753.1; !1PID:g58500 GENETICS !$#map_position 51.6-59.7 CLASSIFICATION #superfamily adenovirus hexon protein KEYWORDS hexon protein SUMMARY #length 952 #molecular-weight 108006 #checksum 3066 SEQUENCE /// ENTRY HXAD41 #type complete TITLE hexon protein - human adenovirus 41 ORGANISM #formal_name Mastadenovirus h41 #common_name human adenovirus 41 #note host Homo sapiens (man) DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS A31040; S08657 REFERENCE A31040 !$#authors Toogood, C.I.A.; Hay, R.T. !$#journal J. Gen. Virol. (1988) 69:2291-2301 !$#title DNA sequence of the adenovirus type 41 hexon gene and !1predicted structure of the protein. !$#cross-references MUID:88316213; PMID:3411299 !$#accession A31040 !'##molecule_type DNA !'##residues 1-925 ##label TOO !'##cross-references EMBL:X51783; NID:g58562; PIDN:CAA36079.1; !1PID:g58564 COMMENT This protein is one of the structural proteins in the viral !1coat. CLASSIFICATION #superfamily adenovirus hexon protein KEYWORDS coat protein; hexon protein; late protein SUMMARY #length 925 #molecular-weight 103975 #checksum 3670 SEQUENCE /// ENTRY HXAD40 #type complete TITLE hexon protein - human adenovirus 40 (strain Dugan) ORGANISM #formal_name Mastadenovirus h40 #common_name human adenovirus 40 #note host Homo sapiens (man) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS A33611; S08659 REFERENCE A33611 !$#authors Toogood, C.I.A.; Murali, R.; Burnett, R.M.; Hay, R.T. !$#journal J. Gen. Virol. (1989) 70:3203-3214 !$#title The adenovirus type 40 hexon: sequence, predicted structure !1and relationship to other adenovirus hexons. !$#cross-references MUID:90111698; PMID:2481711 !$#accession A33611 !'##molecule_type DNA !'##residues 1-923 ##label TOO !'##cross-references EMBL:X51782; NID:g58560; PIDN:CAA36077.1; !1PID:g58561 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1February 1990 CLASSIFICATION #superfamily adenovirus hexon protein KEYWORDS coat protein; hexon protein; late protein SUMMARY #length 923 #molecular-weight 103979 #checksum 7291 SEQUENCE /// ENTRY HXADB3 #type complete TITLE hexon protein - bovine adenovirus 3 ORGANISM #formal_name Mastadenovirus bos3 #common_name bovine adenovirus 3 DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 16-Jul-1999 ACCESSIONS A03850; S11459 REFERENCE A03850 !$#authors Hu, S.L.; Hays, W.W.; Potts, D.E. !$#journal J. Virol. (1984) 49:604-608 !$#title Sequence homology between bovine and human adenoviruses. !$#cross-references MUID:84115091; PMID:6694264 !$#accession A03850 !'##molecule_type DNA !'##residues 1-911 ##label HUS !'##cross-references GB:K01264; NID:g209938; PIDN:AAA42509.1; !1PID:g209939 REFERENCE S11459 !$#authors Cai, F.; Bourbonniere, M.; Tang, D.; Hu, S.L.; Weber, J.M. !$#journal Nucleic Acids Res. (1990) 18:5568 !$#title Nucleotide and deduced amino acid sequence of the bovine !1adenovirus type 3 proteinase. !$#cross-references MUID:91016865; PMID:2216745 !$#accession S11459 !'##status translation not shown !'##molecule_type DNA !'##residues 877-911 ##label CAI !'##cross-references EMBL:X53990 CLASSIFICATION #superfamily adenovirus hexon protein KEYWORDS hexon protein SUMMARY #length 911 #molecular-weight 103052 #checksum 2498 SEQUENCE /// ENTRY SXAD32 #type complete TITLE peripentonal hexon-associated protein (IIIA) - human adenovirus 2 ORGANISM #formal_name Mastadenovirus h2 #common_name human adenovirus 2 #note host Homo sapiens (man) DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS A03851 REFERENCE A92461 !$#authors Roberts, R.J.; O'Neill, K.E.; Yen, C.E. !$#journal J. Biol. Chem. (1984) 259:13968-13975 !$#title DNA sequences from the adenovirus 2 genome. !$#cross-references MUID:85054833; PMID:6334081 !$#accession A03851 !'##molecule_type DNA !'##residues 1-585 ##label ROB !'##cross-references GB:J01917; NID:g209811; PIDN:AAA92210.1; !1PID:g209826 CLASSIFICATION #superfamily adenovirus peripentonal hexon-associated !1protein KEYWORDS late protein SUMMARY #length 585 #molecular-weight 65286 #checksum 2375 SEQUENCE /// ENTRY SXADH5 #type complete TITLE peripentonal hexon-associated protein (IIIA) - human adenovirus 5 ORGANISM #formal_name Mastadenovirus h5 #common_name human adenovirus 5 #note host Homo sapiens (man) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS B39449; PT0066 REFERENCE A39449 !$#authors Chroboczek, J.; Bieber, F.; Jacrot, B. !$#journal Virology (1992) 186:280-285 !$#title The sequence of the genome of adenovirus type 5 and its !1comparison with the genome of adenovirus type 2. !$#cross-references MUID:92087470; PMID:1727603 !$#accession B39449 !'##molecule_type DNA !'##residues 1-585 ##label CHR !'##cross-references GB:M73260; GB:M29978; NID:g209842; PIDN:AAA96407.1; !1PID:g289094 REFERENCE JT0337 !$#authors Neumann, R.; Chroboczek, J.; Jacrot, B. !$#journal Gene (1988) 69:153-157 !$#title Determination of the nucleotide sequence for the penton-base !1gene of human adenovirus type 5. !$#cross-references MUID:89137988; PMID:3224820 !$#accession PT0066 !'##molecule_type DNA !'##residues 469-585 ##label NEU !'##cross-references GB:M22141; NID:g210001; PIDN:AAA42518.1; !1PID:g210002 CLASSIFICATION #superfamily adenovirus peripentonal hexon-associated !1protein KEYWORDS hexon-associated protein; late protein SUMMARY #length 585 #molecular-weight 65252 #checksum 2483 SEQUENCE /// ENTRY SXAD82 #type complete TITLE hexon-associated protein (VIII) - human adenovirus 2 ORGANISM #formal_name Mastadenovirus h2 #common_name human adenovirus 2 DATE 31-Dec-1980 #sequence_revision 02-Apr-1982 #text_change 30-Sep-1993 ACCESSIONS A91583; A93702; A03852 REFERENCE A91583 !$#authors Galibert, F.; Herisse, J.; Courtois, G. !$#journal Gene (1979) 6:1-22 !$#title Nucleotide sequence of the EcoRI-F fragment of adenovirus 2 !1genome. !$#cross-references MUID:80004828; PMID:478297 !$#accession A91583 !'##molecule_type DNA !'##residues 1-54 ##label GAL REFERENCE A93702 !$#authors Herisse, J.; Courtois, G.; Galibert, F. !$#journal Nucleic Acids Res. (1980) 8:2173-2192 !$#title Nucleotide sequence of the EcoRI D fragment of adenovirus 2 !1genome. !$#cross-references MUID:81053687; PMID:6253880 !$#accession A93702 !'##molecule_type DNA !'##residues 54-227 ##label HER GENETICS !$#map_position 75.3-77.3 CLASSIFICATION #superfamily adenovirus hexon-associated protein (VIII) KEYWORDS hexon-associated protein SUMMARY #length 227 #molecular-weight 24703 #checksum 90 SEQUENCE /// ENTRY SXAD85 #type complete TITLE hexon-associated protein (VIII) - human adenovirus 5 ORGANISM #formal_name Mastadenovirus h5 #common_name human adenovirus 5 #note host Homo sapiens (man) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS E39449 REFERENCE A39449 !$#authors Chroboczek, J.; Bieber, F.; Jacrot, B. !$#journal Virology (1992) 186:280-285 !$#title The sequence of the genome of adenovirus type 5 and its !1comparison with the genome of adenovirus type 2. !$#cross-references MUID:92087470; PMID:1727603 !$#accession E39449 !'##molecule_type DNA !'##residues 1-227 ##label CHR !'##cross-references GB:M73260; GB:M29978; NID:g209842; PIDN:AAA96413.1; !1PID:g454806 CLASSIFICATION #superfamily adenovirus hexon-associated protein (VIII) KEYWORDS hexon-associated protein SUMMARY #length 227 #molecular-weight 24686 #checksum 69 SEQUENCE /// ENTRY SXAD41 #type complete TITLE hexon-associated protein (VIII) - human adenovirus 41 ORGANISM #formal_name Mastadenovirus h41 #common_name human adenovirus 41 #note host Homo sapiens (man) DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jul-1999 ACCESSIONS A30920; S10214; S20688 REFERENCE S04851 !$#authors Pieniazek, N.; Velarde Jr., J.; Pieniazek, D.; Luftig, R.B. !$#journal Nucleic Acids Res. (1989) 17:5398 !$#title Nucleotide sequence of human enteric adenovirus type 41 !1hexon-associated protein VIII precursor (pVIII) including !1the early region E3 promoter. !$#cross-references MUID:89345113; PMID:2762136 !$#accession A30920 !'##molecule_type DNA !'##residues 1-233 ##label PIE !'##cross-references GB:X15137; GB:M24099; NID:g58481; PIDN:CAA33237.1; !1PID:g58483 !'##experimental_source strain TAK REFERENCE S10206 !$#authors Slemenda, S.B.; Pieniazek, N.J.; Velarde Jr., J.; Pieniazek, !1D.; Luftig, R.B. !$#journal Nucleic Acids Res. (1990) 18:3069 !$#title Nucleotide sequence of the region coding for 100K and 33K !1proteins of human enteric adenovirus type 41 (Tak). !$#cross-references MUID:90272433; PMID:2349115 !$#accession S10214 !'##status translation not shown !'##molecule_type DNA !'##residues 1-47 ##label SLE !'##cross-references EMBL:X52532; NID:g58438; PIDN:CAA36768.1; !1PID:g58448 REFERENCE S20688 !$#authors Pienaziek, N.J.; Slemenda, S.B.; Pienazek, D.; Velarde Jr., !1J.; Luftig, R.B. !$#submission submitted to the EMBL Data Library, March 1990 !$#description Characterisation of the early region E3 of the human enteric !1adenovirus type 41 Tak. !$#accession S20688 !'##status preliminary !'##molecule_type DNA !'##residues 47-233 ##label PI2 !'##cross-references EMBL:X52198; NID:g58660; PIDN:CAA36443.1; !1PID:g58661 CLASSIFICATION #superfamily adenovirus hexon-associated protein (VIII) KEYWORDS hexon-associated protein SUMMARY #length 233 #molecular-weight 25309 #checksum 9033 SEQUENCE /// ENTRY SXAD31 #type fragment TITLE hexon-associated protein (VIII) - human adenovirus 3 (fragment) ORGANISM #formal_name Mastadenovirus h3 #common_name human adenovirus 3 DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 07-Nov-1997 ACCESSIONS A29500 REFERENCE A91566 !$#authors Signaes, C.; Akusjaervi, G.; Pettersson, U. !$#journal Gene (1986) 50:173-184 !$#title Region E3 of human adenoviruses; differences between the !1oncogenic adenovirus-3 and the non-oncogenic adenovirus-2. !$#cross-references MUID:87219876; PMID:3582978 !$#accession A29500 !'##molecule_type DNA !'##residues 1-135 ##label SIG !'##cross-references GB:M15952; NID:g209901 !'##note this ORF is not annotated in GenBank entry ADRE3AA CLASSIFICATION #superfamily adenovirus hexon-associated protein (VIII) KEYWORDS hexon-associated protein SUMMARY #length 135 #checksum 3328 SEQUENCE /// ENTRY SXADMS #type complete TITLE hexon-associated protein (VIII) - mouse adenovirus 1 ORGANISM #formal_name Mastadenovirus mus1 #common_name mouse adenovirus 1 #note host Mus musculus (house mouse) DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS A33382 REFERENCE A33382 !$#authors Raviprakash, K.S.; Grunhaus, A.; El Kholy, M.A.; Horwitz, !1M.S. !$#journal J. Virol. (1989) 63:5455-5458 !$#title The mouse adenovirus type 1 contains an unusual E3 region. !$#cross-references MUID:90064816; PMID:2531236 !$#accession A33382 !'##molecule_type DNA !'##residues 1-215 ##label RAV !'##cross-references GB:M30594; NID:g209755; PIDN:AAA42432.1; !1PID:g209756 CLASSIFICATION #superfamily adenovirus hexon-associated protein (VIII) KEYWORDS hexon-associated protein SUMMARY #length 215 #molecular-weight 23272 #checksum 1135 SEQUENCE /// ENTRY SXAD95 #type complete TITLE hexon-associated protein (IX) - human adenovirus 5 ORGANISM #formal_name Mastadenovirus h5 #common_name human adenovirus 5 DATE 31-Oct-1980 #sequence_revision 02-Apr-1982 #text_change 16-Jul-1999 ACCESSIONS A03853; B03853 REFERENCE A90814 !$#authors Bos, J.L.; Polder, L.J.; Bernards, R.; Schrier, P.I.; van !1den Elsen, P.J.; van der Eb, A.J.; van Ormondt, H. !$#journal Cell (1981) 27:121-131 !$#title The 2.2 kb E1b mRNA of human Ad12 and Ad5 codes for two !1tumor antigens starting at different AUG triplets. !$#cross-references MUID:82115327; PMID:7326748 !$#accession A03853 !'##molecule_type mRNA !'##residues 1-140 ##label BOS !'##cross-references GB:X02996; GB:J01967; GB:J01968; GB:J01970; !1GB:J01971; GB:J01972; GB:J01974; GB:J01976; GB:J01977; !1GB:J01978; GB:J01979; GB:K00515; GB:V00025; GB:V00026; !1GB:V00027; GB:V00029; NID:g58484; PIDN:CAA26746.1; !1PID:g58493 !'##note the authors translated the codon GTC for residue 39 as Cys REFERENCE A91469 !$#authors Maat, J.; van Beveren, C.P.; van Ormondt, H. !$#journal Gene (1980) 10:27-38 !$#title The nucleotide sequence of adenovirus type 5 early region !1E1: the region between map positions 8.0 (HindIII site) and !111.8 (SmaI site). !$#cross-references MUID:81005097; PMID:6250944 !$#accession B03853 !'##molecule_type DNA !'##residues 1-140 ##label MAA !'##cross-references GB:X02996; GB:J01967; GB:J01968; GB:J01970; !1GB:J01971; GB:J01972; GB:J01974; GB:J01976; GB:J01977; !1GB:J01978; GB:J01979; GB:K00515; GB:V00025; GB:V00026; !1GB:V00027; GB:V00029; NID:g58484; PIDN:CAA26746.1; !1PID:g58493 COMMENT This protein is a structural component of the virion. It may !1have an additional role during adenovirus multiplication. CLASSIFICATION #superfamily adenovirus hexon-associated protein (IX) KEYWORDS hexon-associated protein SUMMARY #length 140 #molecular-weight 14458 #checksum 2527 SEQUENCE /// ENTRY SXAD92 #type complete TITLE hexon-associated protein (IX) - human adenovirus 2 ORGANISM #formal_name Mastadenovirus h2 #common_name human adenovirus 2 DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 30-Sep-1993 ACCESSIONS C03853; D03853; A03853 REFERENCE A90793 !$#authors Alestrom, P.; Akusjarvi, G.; Perricaudet, M.; Mathews, M.B.; !1Klessig, D.F.; Pettersson, U. !$#journal Cell (1980) 19:671-681 !$#title The gene for polypeptide IX of adenovirus type 2 and its !1unspliced messenger RNA. !$#cross-references MUID:80155185; PMID:6985473 !$#accession C03853 !'##molecule_type DNA !'##residues 1-140 ##label ALE REFERENCE A92351 !$#authors Gingeras, T.R.; Sciaky, D.; Gelinas, R.E.; Bing-Dong, J.; !1Yen, C.E.; Kelly, M.M.; Bullock, P.A.; Parsons, B.L.; !1O'Neill, K.E.; Roberts, R.J. !$#journal J. Biol. Chem. (1982) 257:13475-13491 !$#title Nucleotide sequences from the adenovirus-2 genome. !$#cross-references MUID:83056843; PMID:7142161 !$#accession D03853 !'##molecule_type DNA !'##residues 1,'SA',4-140 ##label GIN COMMENT This protein is a structural component of the virion. It may !1have an additional role during adenovirus multiplication. CLASSIFICATION #superfamily adenovirus hexon-associated protein (IX) KEYWORDS hexon-associated protein SUMMARY #length 140 #molecular-weight 14442 #checksum 2491 SEQUENCE /// ENTRY SXAD97 #type complete TITLE hexon-associated protein - human adenovirus 7 ALTERNATE_NAMES polypeptide IX ORGANISM #formal_name Mastadenovirus h7 #common_name human adenovirus 7 DATE 18-Dec-1981 #sequence_revision 18-Dec-1981 #text_change 05-Jun-1998 ACCESSIONS A03854 REFERENCE A91480 !$#authors Dijkema, R.; Maat, J.; Dekker, B.M.M.; van Ormondt, H.; !1Boyer, H.W. !$#journal Gene (1981) 13:375-385 !$#title The gene for polypeptide IX of human adenovirus type 7. !$#cross-references MUID:81261948; PMID:6266923 !$#accession A03854 !'##molecule_type DNA !'##residues 1-138 ##label DIJ CLASSIFICATION #superfamily adenovirus hexon-associated protein (IX) KEYWORDS hexon-associated protein SUMMARY #length 138 #molecular-weight 14107 #checksum 314 SEQUENCE /// ENTRY SXAD93 #type complete TITLE hexon-associated protein (IX) - human adenovirus 3 ORGANISM #formal_name Mastadenovirus h3 #common_name human adenovirus 3 DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jul-1999 ACCESSIONS B03854; A03854 REFERENCE A91481 !$#authors Engler, J.A. !$#journal Gene (1981) 13:387-394 !$#title The nucleotide sequence of the polypeptide IX gene of human !1adenovirus type 3. !$#cross-references MUID:81261949; PMID:7262560 !$#accession B03854 !'##molecule_type DNA !'##residues 1-138 ##label ENG !'##cross-references GB:J01962; NID:g209966; PIDN:AAA42510.1; !1PID:g209967 CLASSIFICATION #superfamily adenovirus hexon-associated protein (IX) KEYWORDS hexon-associated protein SUMMARY #length 138 #molecular-weight 14107 #checksum 314 SEQUENCE /// ENTRY SXAD12 #type complete TITLE hexon-associated protein (IX) - human adenovirus 12 ORGANISM #formal_name Mastadenovirus h12 #common_name human adenovirus 12 DATE 02-Apr-1982 #sequence_revision 02-Apr-1982 #text_change 16-Jul-1999 ACCESSIONS A90814; A93745; S33931; A03855 REFERENCE A90814 !$#authors Bos, J.L.; Polder, L.J.; Bernards, R.; Schrier, P.I.; van !1den Elsen, P.J.; van der Eb, A.J.; van Ormondt, H. !$#journal Cell (1981) 27:121-131 !$#title The 2.2 kb E1b mRNA of human Ad12 and Ad5 codes for two !1tumor antigens starting at different AUG triplets. !$#cross-references MUID:82115327; PMID:7326748 !$#accession A90814 !'##molecule_type mRNA !'##residues 1-144 ##label BOS REFERENCE A93745 !$#authors Kimura, T.; Sawada, Y.; Shinawawa, M.; Shimizu, Y.; Shiroki, !1K.; Shimojo, H.; Sugisaki, H.; Takanami, M.; Uemizu, Y.; !1Fujinaga, K. !$#journal Nucleic Acids Res. (1981) 9:6571-6589 !$#title Nucleotide sequence of the transforming early region E1b of !1adenovirus type 12 DNA: structure and gene organization, and !1comparison with those of adenovirus type 5 DNA. !$#cross-references MUID:82105565; PMID:6275367 !$#accession A93745 !'##molecule_type DNA !'##residues 1-144 ##label KIM !'##cross-references GB:X73487; NID:g313361; PIDN:CAA51880.1; !1PID:g313365 REFERENCE S33928 !$#authors Sprengel, J. !$#submission submitted to the EMBL Data Library, June 1993 !$#accession S33931 !'##status preliminary !'##molecule_type DNA !'##residues 1-144 ##label SPR !'##cross-references EMBL:X73487; NID:g313361; PIDN:CAA51880.1; !1PID:g313365 GENETICS !$#map_position 9.4-10.7 CLASSIFICATION #superfamily adenovirus hexon-associated protein (IX) SUMMARY #length 144 #molecular-weight 15017 #checksum 738 SEQUENCE /// ENTRY SXADF1 #type complete TITLE hexon-associated protein (IX) - human adenovirus 41 ORGANISM #formal_name Mastadenovirus h41 #common_name human adenovirus 41 #note host Homo sapiens (man) DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS C40249 REFERENCE A40249 !$#authors Allard, A.; Wadell, G. !$#journal Virology (1992) 188:319-330 !$#title The E1B transcription map of the enteric adenovirus type 41. !$#cross-references MUID:92230230; PMID:1533079 !$#accession C40249 !'##molecule_type DNA !'##residues 1-133 ##label ALL !'##cross-references GB:M87544; NID:g209890; PIDN:AAA42476.1; !1PID:g209893 CLASSIFICATION #superfamily adenovirus hexon-associated protein (IX) KEYWORDS hexon-associated protein SUMMARY #length 133 #molecular-weight 13626 #checksum 7852 SEQUENCE /// ENTRY SXADC2 #type complete TITLE hexon-associated protein (IX) - canine adenovirus 2 (strain Tront A 26-61) ORGANISM #formal_name Mastadenovirus can2 #common_name canine adenovirus 2 #note host Canis lupis familiaris (dog) DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 22-Oct-1999 ACCESSIONS D34165 REFERENCE A34165 !$#authors Shibata, R.; Shinagawa, M.; Iida, Y.; Tsukiyama, T. !$#journal Virology (1989) 172:460-467 !$#title Nucleotide sequence of E1 region of canine adenovirus type !12. !$#cross-references MUID:90021176; PMID:2800332 !$#accession D34165 !'##molecule_type DNA !'##residues 1-103 ##label SHI !'##cross-references GB:J04368; NID:g209884; PIDN:AAA42473.1; !1PID:g209888 CLASSIFICATION #superfamily adenovirus hexon-associated protein (IX) KEYWORDS hexon-associated protein SUMMARY #length 103 #molecular-weight 11428 #checksum 9744 SEQUENCE /// ENTRY SXAD9T #type complete TITLE hexon-associated protein (IX) - tree shrew adenovirus ORGANISM #formal_name Mastadenovirus tup #common_name tree shrew adenovirus DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 21-Jul-2000 ACCESSIONS A03856 REFERENCE A91522 !$#authors Flugel, R.M.; Bannert, H.; Suhai, S.; Darai, G. !$#journal Gene (1985) 34:73-80 !$#title The nucleotide sequence of the early region of the Tupaia !1adenovirus DNA corresponding to the oncogenic region E1b of !1human adenovirus 7. !$#cross-references MUID:85232053; PMID:3159623 !$#accession A03856 !'##molecule_type DNA !'##residues 1-122 ##label FLU !'##cross-references GB:M10054; NID:g210025; PIDN:AAA42532.1; !1PID:g210028 !'##note the host is identified as Tupaia belangeri CLASSIFICATION #superfamily adenovirus hexon-associated protein (IX) KEYWORDS hexon-associated protein SUMMARY #length 122 #molecular-weight 13491 #checksum 1839 SEQUENCE /// ENTRY WMVZ11 #type complete TITLE 11K protein - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 16-Jul-1999 ACCESSIONS A22955 REFERENCE A22955 !$#authors Bertholet, C.; Drillien, R.; Wittek, R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:2096-2100 !$#title One hundred base pairs of 5' flanking sequence of a vaccinia !1virus late gene are sufficient to temporally regulate late !1transcription. !$#cross-references MUID:85166279; PMID:3856886 !$#accession A22955 !'##molecule_type DNA !'##residues 1-101 ##label BER !'##cross-references GB:M11107; NID:g335692; PIDN:AAA48278.1; !1PID:g335693 CLASSIFICATION #superfamily vaccinia virus 11K protein KEYWORDS DNA binding; late protein; structural protein SUMMARY #length 101 #molecular-weight 11435 #checksum 1698 SEQUENCE /// ENTRY WMVZ12 #type complete TITLE 11K protein - vaccinia virus ALTERNATE_NAMES F17L protein ORGANISM #formal_name vaccinia virus DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 16-Jul-1999 ACCESSIONS A25726; D42508 REFERENCE A25726 !$#authors Tsao, H.; Ren, G.F.; Chu, C.M. !$#journal J. Virol. (1986) 57:693-696 !$#title Gene coding for the late 11,000-dalton polypeptide of the !1Tian Tan strain of vaccinia virus and its 5'-flanking !1region: nucleotide sequence. !$#cross-references MUID:86115421; PMID:3944848 !$#accession A25726 !'##molecule_type DNA !'##residues 1-101 ##label TSA !'##cross-references GB:M12698; NID:g335298; PIDN:AAA47960.1; !1PID:g335299 !'##experimental_source strain Tian Tan REFERENCE A33172 !$#authors Johnson, G.P. !$#submission submitted to GenBank, June 1990 !$#accession D42508 !'##molecule_type DNA !'##residues 1-101 ##label JOH !'##experimental_source strain Copenhagen CLASSIFICATION #superfamily vaccinia virus 11K protein KEYWORDS DNA binding; late protein; structural protein SUMMARY #length 101 #molecular-weight 11336 #checksum 1522 SEQUENCE /// ENTRY WMVZ14 #type complete TITLE 14K cell fusion protein - vaccinia virus ORGANISM #formal_name vaccinia virus DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 29-Oct-1999 ACCESSIONS A27173; S29911 REFERENCE A27173 !$#authors Rodriguez, J.F.; Esteban, M. !$#journal J. Virol. (1987) 61:3550-3554 !$#title Mapping and nucleotide sequence of the vaccinia virus gene !1that encodes a 14-kilodalton fusion protein. !$#cross-references MUID:88036210; PMID:2822962 !$#accession A27173 !'##molecule_type DNA !'##residues 1-110 ##label ROD !'##cross-references GB:M18173; NID:g335628; PIDN:AAA48248.1; !1PID:g335629 !'##note the authors translated the codon GGA for residue 8 as Lys and !1AAT for residue 43 as Asp REFERENCE S29907 !$#authors Amegadzie, B.Y. !$#submission submitted to the EMBL Data Library, January 1991 !$#accession S29911 !'##status preliminary !'##molecule_type DNA !'##residues 1-28,'DR',31-33,'Q',35-110 ##label AME !'##cross-references EMBL:X57318; NID:g62239; PIDN:CAA40577.1; !1PID:g62244 CLASSIFICATION #superfamily vaccinia virus 14K cell fusion protein KEYWORDS glycoprotein; membrane fusion FEATURE !$2-110 #product 14K cell fusion protein #status predicted !8#label MAT\ !$60 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 110 #molecular-weight 12572 #checksum 1070 SEQUENCE /// ENTRY WMVZ2U #type complete TITLE 14K cell fusion protein - vaccinia virus (strain Copenhagen) ALTERNATE_NAMES A27L protein ORGANISM #formal_name vaccinia virus #note host Homo sapiens (man) DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Jul-1999 ACCESSIONS B42520 REFERENCE A42501 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:517-563 !$#title Appendix to "The complete DNA sequence of vaccinia virus". !$#accession B42520 !'##molecule_type DNA !'##residues 1-110 ##label GOE !'##cross-references GB:M35027; NID:g335317; PIDN:AAA48152.1; !1PID:g335500 !'##experimental_source strain Copenhagen REFERENCE A42531 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:247-266 !$#title The complete DNA sequence of vaccinia virus. !$#cross-references MUID:91021027; PMID:2219722 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given CLASSIFICATION #superfamily vaccinia virus 14K cell fusion protein KEYWORDS glycoprotein; membrane fusion FEATURE !$2-110 #product 14K cell fusion protein #status predicted !8#label MAT\ !$60 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 110 #molecular-weight 12616 #checksum 1145 SEQUENCE /// ENTRY WMVZ65 #type complete TITLE 14K cell fusion protein - vaccinia virus (strain WR, 65-16) ORGANISM #formal_name vaccinia virus DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jul-1999 ACCESSIONS A37076 REFERENCE A37076 !$#authors Gong, S.; Lai, C.; Esteban, M. !$#journal Virology (1990) 178:81-91 !$#title Vaccinia virus induces cell fusion at acid pH and this !1activity is mediated by the N-terminus of the 14-kDa virus !1envelope protein. !$#cross-references MUID:90357795; PMID:2389560 !$#accession A37076 !'##molecule_type DNA !'##residues 1-136 ##label GON !'##cross-references EMBL:M37086; NID:g335300; PIDN:AAA47961.1; !1PID:g335301 CLASSIFICATION #superfamily vaccinia virus 14K cell fusion protein KEYWORDS glycoprotein; membrane fusion FEATURE !$2-136 #product 14K cell fusion protein #status predicted !8#label MAT\ !$86 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 136 #molecular-weight 15837 #checksum 1776 SEQUENCE /// ENTRY WMVZRF #type complete TITLE 10K cell fusion protein - Orf virus ORGANISM #formal_name Orf virus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 25-Oct-1996 ACCESSIONS A38711 REFERENCE A38711 !$#authors Naase, M.; Nicholson, B.H.; Fraser, K.M.; Mercer, A.A.; !1Robinson, A.J. !$#journal J. Gen. Virol. (1991) 72:1177-1181 !$#title An orf virus sequence showing homology to the 14K 'fusion' !1protein of vaccinia virus. !$#cross-references MUID:91237357; PMID:2033392 !$#accession A38711 !'##molecule_type DNA !'##residues 1-89 ##label NAA CLASSIFICATION #superfamily vaccinia virus 14K cell fusion protein KEYWORDS glycoprotein; membrane fusion FEATURE !$2-89 #product 10K cell fusion protein #status predicted !8#label MAT\ !$18 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 89 #molecular-weight 10050 #checksum 7780 SEQUENCE /// ENTRY WMVZM2 #type complete TITLE HM2 protein - sheep pox virus (isolate Kenya sheep-1, KS-1) ORGANISM #formal_name sheep pox virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS B33325 REFERENCE A33325 !$#authors Gershon, P.D.; Ansell, D.M.; Black, D.N. !$#journal J. Virol. (1989) 63:4703-4708 !$#title A comparison of the genome organization of capripoxvirus !1with that of the orthopoxviruses. !$#cross-references MUID:90012320; PMID:2795717 !$#accession B33325 !'##molecule_type DNA !'##residues 1-148 ##label GER !'##cross-references GB:M30039; NID:g323258; PIDN:AAC32898.1; !1PID:g323260 CLASSIFICATION #superfamily vaccinia virus 14K cell fusion protein FEATURE !$2-148 #product HM2 protein #status predicted #label MAT SUMMARY #length 148 #molecular-weight 17387 #checksum 5379 SEQUENCE /// ENTRY WMVZM3 #type complete TITLE HM3 protein - sheep pox virus (isolate Kenya sheep-1, KS-1) ORGANISM #formal_name sheep pox virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS C33325 REFERENCE A33325 !$#authors Gershon, P.D.; Ansell, D.M.; Black, D.N. !$#journal J. Virol. (1989) 63:4703-4708 !$#title A comparison of the genome organization of capripoxvirus !1with that of the orthopoxviruses. !$#cross-references MUID:90012320; PMID:2795717 !$#accession C33325 !'##molecule_type DNA !'##residues 1-140 ##label GER !'##cross-references GB:M30039; NID:g323258; PIDN:AAC32899.1; !1PID:g323261 CLASSIFICATION #superfamily sheep pox virus HM3 protein SUMMARY #length 140 #molecular-weight 16202 #checksum 660 SEQUENCE /// ENTRY WMVZG4 #type complete TITLE G4R protein - Amsacta moorei poxvirus ORGANISM #formal_name Amsacta moorei poxvirus DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 08-Apr-1994 ACCESSIONS D41561 REFERENCE A41561 !$#authors Hall, R.L.; Moyer, R.W. !$#journal J. Virol. (1991) 65:6516-6527 !$#title Identification, cloning, and sequencing of a fragment of !1Amsacta moorei entomopoxvirus DNA containing the spheroidin !1gene and three vaccinia virus-related open reading frames. !$#cross-references MUID:92046310; PMID:1942245 !$#accession D41561 !'##molecule_type DNA !'##residues 1-143 ##label HAL !'##cross-references GB:M77182 CLASSIFICATION #superfamily sheep pox virus HM3 protein SUMMARY #length 143 #molecular-weight 16602 #checksum 8119 SEQUENCE /// ENTRY WMVA16 #type complete TITLE B21R 16K protein - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jun-2000 ACCESSIONS C30175; JQ1815 REFERENCE A30175 !$#authors Kotwal, G.J.; Moss, B. !$#journal J. Virol. (1989) 63:600-606 !$#title Vaccinia virus encodes two proteins that are structurally !1related to members of the plasma serine protease inhibitor !1superfamily. !$#cross-references MUID:89094985; PMID:2783466 !$#accession C30175 !'##molecule_type DNA !'##residues 1-134 ##label KOT !'##cross-references GB:D11079; NID:g222717; PIDN:BAA01851.1; !1PID:g222766 REFERENCE JQ1767 !$#authors Smith, G.L.; Chan, Y.S.; Howard, S.T. !$#journal J. Gen. Virol. (1991) 72:1349-1376 !$#title Nucleotide sequence of 42kbp of vaccinia virus strain WR !1from near the right inverted terminal repeat. !$#cross-references MUID:91259063; PMID:2045793 !$#accession JQ1815 !'##molecule_type DNA !'##residues 1-134 ##label SMI !'##cross-references DDBJ:D11079; NID:g222717; PIDN:BAA01851.1; !1PID:g222766 CLASSIFICATION #superfamily vaccinia virus 16K protein SUMMARY #length 134 #molecular-weight 16022 #checksum 4772 SEQUENCE /// ENTRY WMVZ21 #type complete TITLE 21.5K protein - vaccinia virus (strain WR) ALTERNATE_NAMES B23R protein ORGANISM #formal_name vaccinia virus DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS D30175; JQ1817 REFERENCE A30175 !$#authors Kotwal, G.J.; Moss, B. !$#journal J. Virol. (1989) 63:600-606 !$#title Vaccinia virus encodes two proteins that are structurally !1related to members of the plasma serine protease inhibitor !1superfamily. !$#cross-references MUID:89094985; PMID:2783466 !$#accession D30175 !'##molecule_type DNA !'##residues 1-190 ##label KOT !'##cross-references GB:M24217; NID:g335815; PIDN:AAA48345.1; !1PID:g335819 REFERENCE JQ1767 !$#authors Smith, G.L.; Chan, Y.S.; Howard, S.T. !$#journal J. Gen. Virol. (1991) 72:1349-1376 !$#title Nucleotide sequence of 42kbp of vaccinia virus strain WR !1from near the right inverted terminal repeat. !$#cross-references MUID:91259063; PMID:2045793 !$#accession JQ1817 !'##molecule_type DNA !'##residues 1-123 ##label SMI !'##cross-references DDBJ:D11079 CLASSIFICATION #superfamily vaccinia virus 21.5K protein SUMMARY #length 190 #molecular-weight 21538 #checksum 9236 SEQUENCE /// ENTRY WMVZ28 #type complete TITLE 28K protein - vaccinia virus ALTERNATE_NAMES F5 protein ORGANISM #formal_name vaccinia virus DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 16-Jul-1999 ACCESSIONS A03867 REFERENCE A03867 !$#authors Weir, J.P.; Moss, B. !$#journal J. Virol. (1984) 51:662-669 !$#title Regulation of expression and nucleotide sequence of a late !1vaccinia virus gene. !$#cross-references MUID:84292442; PMID:6088791 !$#accession A03867 !'##molecule_type DNA !'##residues 1-251 ##label WEI !'##cross-references GB:K02376; NID:g335718; PIDN:AAA48300.1; !1PID:g335719 COMMENT This protein is synthesized after viral DNA replication. CLASSIFICATION #superfamily vaccinia virus 28K protein KEYWORDS late protein SUMMARY #length 251 #molecular-weight 28456 #checksum 8349 SEQUENCE /// ENTRY WMVZF5 #type complete TITLE 28K protein - vaccinia virus (strain WR) ALTERNATE_NAMES F5 protein ORGANISM #formal_name vaccinia virus DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 28-May-1999 ACCESSIONS D23092 REFERENCE A23092 !$#authors Plucienniczak, A.; Schroeder, E.; Zettlmeissl, G.; Streeck, !1R.E. !$#journal Nucleic Acids Res. (1985) 13:985-998 !$#title Nucleotide sequence of a cluster of early and late genes in !1a conserved segment of the vaccinia virus genome. !$#cross-references MUID:85215527; PMID:2987815 !$#accession D23092 !'##molecule_type DNA !'##residues 1-251 ##label PLU !'##cross-references GB:X01978; GB:J02424; GB:J02425; GB:K02376; !1GB:M15211; GB:V01537; NID:g61387; PIDN:CAA26013.1; !1PID:g61392 COMMENT This protein is synthesized after viral DNA replication. CLASSIFICATION #superfamily vaccinia virus 28K protein KEYWORDS late protein SUMMARY #length 251 #molecular-weight 28456 #checksum 7989 SEQUENCE /// ENTRY WMVZP5 #type complete TITLE F5 protein - fowlpox virus (strain HP444) ORGANISM #formal_name fowlpox virus DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jun-2000 ACCESSIONS JS0225 REFERENCE JS0220 !$#authors Binns, M.M.; Tomley, F.M.; Campbell, J.; Boursnell, M.E.G. !$#journal J. Gen. Virol. (1988) 69:1275-1283 !$#title Comparison of a conserved region in fowlpox virus and !1vaccinia virus genomes and the translocation of the fowlpox !1virus thymidine kinase gene. !$#cross-references MUID:88258470; PMID:2838574 !$#accession JS0225 !'##molecule_type DNA !'##residues 1-253 ##label BIN !'##cross-references GB:D00320; NID:g221401; PIDN:BAA00228.1; !1PID:g221407 CLASSIFICATION #superfamily vaccinia virus 28K protein SUMMARY #length 253 #molecular-weight 28345 #checksum 8223 SEQUENCE /// ENTRY WMVZ32 #type complete TITLE 32.5K protein - vaccinia virus ORGANISM #formal_name vaccinia virus DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 16-Jul-1999 ACCESSIONS A03868; PS0042 REFERENCE A03868 !$#authors Gillard, S.; Spehner, D.; Drillien, R.; Kirn, A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:5573-5577 !$#title Localization and sequence of a vaccinia virus gene required !1for multiplication in human cells. !$#cross-references MUID:86287300; PMID:3461450 !$#accession A03868 !'##molecule_type DNA !'##residues 1-284 ##label GIL !'##cross-references EMBL:M14319; NID:g335716; PIDN:AAA48299.1; !1PID:g335717 REFERENCE JS0211 !$#authors Boursnell, M.E.G.; Foulds, I.J.; Campbell, J.I.; Binns, M.M. !$#journal J. Gen. Virol. (1988) 69:2995-3003 !$#title Non-essential genes in the vaccinia virus HindIII K !1fragment: a gene related to serine protease inhibitors and a !1gene related to the 37K vaccinia virus major envelope !1antigen. !$#cross-references MUID:89067908; PMID:3264331 !$#accession PS0042 !'##molecule_type DNA !'##residues 1-17 ##label BOU !'##cross-references GB:D00382 CLASSIFICATION #superfamily vaccinia virus 32.5K protein; ankyrin repeat !1homology FEATURE !$29-61 #domain ankyrin repeat homology #label AN1\ !$62-92 #domain ankyrin repeat homology #label AN2\ !$93-112 #domain ankyrin repeat homology #status atypical !8#label AN3 SUMMARY #length 284 #molecular-weight 32538 #checksum 6553 SEQUENCE /// ENTRY WMVZF7 #type complete TITLE BamHI-ORF7 protein - fowlpox virus (isolate HP-438[Munich]) ORGANISM #formal_name fowlpox virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jun-2000 ACCESSIONS G29963 REFERENCE JT0442 !$#authors Tomley, F.; Binns, M.; Campbell, J.; Boursnell, M. !$#journal J. Gen. Virol. (1988) 69:1025-1040 !$#title Sequence analysis of an 11.2 kilobase, near-terminal, BamHI !1fragment of fowlpox virus. !$#cross-references MUID:88229622; PMID:2836548 !$#accession G29963 !'##molecule_type DNA !'##residues 1-410 ##label TOM !'##cross-references GB:D00295; NID:g221380; PIDN:BAA00199.1; !1PID:g221390 CLASSIFICATION #superfamily fowlpox virus BamHI-ORF7 protein; ankyrin !1repeat homology KEYWORDS early protein FEATURE !$33-65 #domain ankyrin repeat homology #label AN1\ !$66-98 #domain ankyrin repeat homology #label AN2\ !$100-132 #domain ankyrin repeat homology #label AN3\ !$133-165 #domain ankyrin repeat homology #label AN4\ !$166-198 #domain ankyrin repeat homology #label AN5 SUMMARY #length 410 #molecular-weight 46873 #checksum 5788 SEQUENCE /// ENTRY WMVZ35 #type complete TITLE 35K major secreted protein - vaccinia virus (strain Lister) ORGANISM #formal_name vaccinia virus DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jun-2000 ACCESSIONS A36640 REFERENCE A36640 !$#authors Patel, A.H.; Gaffney, D.F.; Subak-Sharpe, J.H.; Stow, N.D. !$#journal J. Gen. Virol. (1990) 71:2013-2021 !$#title DNA sequence of the gene encoding a major secreted protein !1of vaccinia virus, strain Lister. !$#cross-references MUID:91011347; PMID:2212991 !$#accession A36640 !'##molecule_type DNA !'##residues 1-258 ##label PAT !'##cross-references EMBL:D00612; NID:g222690; PIDN:BAA00487.1; !1PID:g222691 CLASSIFICATION #superfamily vaccinia virus 35K major secreted protein SUMMARY #length 258 #molecular-weight 27831 #checksum 7393 SEQUENCE /// ENTRY WMVZ37 #type complete TITLE major envelope antigen - vaccinia virus ORGANISM #formal_name vaccinia virus #note host Homo sapiens (man) DATE 13-Aug-1986 #sequence_revision 13-Aug-1986 #text_change 16-Jul-1999 ACCESSIONS A03869 REFERENCE A03869 !$#authors Hirt, P.; Hiller, G.; Wittek, R. !$#journal J. Virol. (1986) 58:757-764 !$#title Localization and fine structure of a vaccinia virus gene !1encoding an envelope antigen. !$#cross-references MUID:86200431; PMID:3701927 !$#accession A03869 !'##molecule_type DNA !'##residues 1-372 ##label HIR !'##cross-references GB:M12882; NID:g335610; PIDN:AAA48235.1; !1PID:g335611 CLASSIFICATION #superfamily vaccinia virus major envelope antigen KEYWORDS envelope protein; transmembrane protein SUMMARY #length 372 #molecular-weight 41795 #checksum 1728 SEQUENCE /// ENTRY WMVZCN #type complete TITLE major envelope antigen - vaccinia virus (strain Copenhagen) ORGANISM #formal_name vaccinia virus #note host Homo sapiens (man) DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jul-1999 ACCESSIONS I42507 REFERENCE A42501 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:517-563 !$#title Appendix to "The complete DNA sequence of vaccinia virus". !$#accession I42507 !'##molecule_type DNA !'##residues 1-372 ##label GOE !'##cross-references GB:M35027; NID:g335317; PIDN:AAA48031.1; !1PID:g335379 REFERENCE A42531 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:247-266 !$#title The complete DNA sequence of vaccinia virus. !$#cross-references MUID:91021027; PMID:2219722 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given CLASSIFICATION #superfamily vaccinia virus major envelope antigen KEYWORDS envelope protein; transmembrane protein SUMMARY #length 372 #molecular-weight 41823 #checksum 2127 SEQUENCE /// ENTRY WMVZID #type complete TITLE major envelope antigen - vaccinia virus (strain IHD-J) ORGANISM #formal_name vaccinia virus #note host Homo sapiens (man) DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jul-1999 ACCESSIONS A40339 REFERENCE A40339 !$#authors Schmutz, C.; Payne, L.G.; Gubser, J.; Wittek, R. !$#journal J. Virol. (1991) 65:3435-3442 !$#title A mutation in the gene encoding the vaccinia virus 37,000-Mr !1protein confers resistance to an inhibitor of virus !1envelopment and release. !$#cross-references MUID:91251190; PMID:2041074 !$#accession A40339 !'##molecule_type DNA !'##residues 1-372 ##label SCH !'##cross-references GB:M60412; NID:g335612; PIDN:AAA48236.1; !1PID:g335613 CLASSIFICATION #superfamily vaccinia virus major envelope antigen KEYWORDS envelope protein; transmembrane protein SUMMARY #length 372 #molecular-weight 41805 #checksum 1710 SEQUENCE /// ENTRY WMVZM1 #type complete TITLE major envelope antigen - molluscum contagiosum virus (type 1) ORGANISM #formal_name molluscum contagiosum virus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jul-1999 ACCESSIONS A40340 REFERENCE A40340 !$#authors Blake, N.W.; Porter, C.D.; Archard, L.C. !$#journal J. Virol. (1991) 65:3583-3589 !$#title Characterization of a molluscum contagiosum virus homolog of !1the vaccinia virus p37K major envelope antigen. !$#cross-references MUID:91251209; PMID:2041084 !$#accession A40340 !'##molecule_type DNA !'##residues 1-388 ##label BLA !'##cross-references GB:M63486; NID:g332147; PIDN:AAA46548.1; !1PID:g332148 CLASSIFICATION #superfamily vaccinia virus major envelope antigen KEYWORDS envelope protein; transmembrane protein SUMMARY #length 388 #molecular-weight 42862 #checksum 8909 SEQUENCE /// ENTRY WMVZU2 #type complete TITLE major envelope antigen - molluscum contagiosum virus (type 2) ORGANISM #formal_name molluscum contagiosum virus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Feb-1997 ACCESSIONS B40340 REFERENCE A40340 !$#authors Blake, N.W.; Porter, C.D.; Archard, L.C. !$#journal J. Virol. (1991) 65:3583-3589 !$#title Characterization of a molluscum contagiosum virus homolog of !1the vaccinia virus p37K major envelope antigen. !$#cross-references MUID:91251209; PMID:2041084 !$#accession B40340 !'##molecule_type DNA !'##residues 1-388 ##label BLA !'##cross-references GB:M63486 CLASSIFICATION #superfamily vaccinia virus major envelope antigen KEYWORDS envelope protein; transmembrane protein SUMMARY #length 388 #molecular-weight 42660 #checksum 7133 SEQUENCE /// ENTRY A44216 #type complete TITLE major envelope antigen - fowlpox virus ALTERNATE_NAMES hypothetical protein 251; ORF1 protein ORGANISM #formal_name fowlpox virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 03-Nov-2000 ACCESSIONS A44216; PQ0505; S27933 REFERENCE A44216 !$#authors Calvert, J.G.; Ogawa, R.; Yanagida, N.; Nazerian, K. !$#journal Virology (1992) 191:783-792 !$#title Identification and functional analysis of the fowlpox virus !1homolog of the vaccinia virus p37K major envelope antigen !1gene. !$#cross-references MUID:93079881; PMID:1333124 !$#accession A44216 !'##molecule_type DNA !'##residues 1-377 ##label CAL !'##cross-references GB:M88587; NID:g325374; PIDN:AAA43819.1; !1PID:g325376 !'##note the authors translated the codon ATA for residue 220 as His REFERENCE JQ1894 !$#authors Ogawa, R.; Calvert, J.G.; Yanagida, N.; Nazerian, K. !$#journal J. Gen. Virol. (1993) 74:55-64 !$#title Insertional inactivation of a fowlpox virus homologue of the !1vaccinia virus F12L gene inhibits the release of enveloped !1virions. !$#cross-references MUID:93139784; PMID:8380837 !$#accession PQ0505 !'##molecule_type DNA !'##residues 127-377 ##label OGA !'##cross-references GB:M88588; NID:g333522; PIDN:AAA47186.1; !1PID:g333523 !'##note submitted to the EMBL Data Library, May 1992 CLASSIFICATION #superfamily vaccinia virus major envelope antigen KEYWORDS envelope protein SUMMARY #length 377 #molecular-weight 43021 #checksum 1982 SEQUENCE /// ENTRY WMVZK3 #type complete TITLE K3 protein - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jun-2000 ACCESSIONS JS0213 REFERENCE JS0211 !$#authors Boursnell, M.E.G.; Foulds, I.J.; Campbell, J.I.; Binns, M.M. !$#journal J. Gen. Virol. (1988) 69:2995-3003 !$#title Non-essential genes in the vaccinia virus HindIII K !1fragment: a gene related to serine protease inhibitors and a !1gene related to the 37K vaccinia virus major envelope !1antigen. !$#cross-references MUID:89067908; PMID:3264331 !$#accession JS0213 !'##molecule_type DNA !'##residues 1-424 ##label BOU !'##cross-references GB:D00382; NID:g222704; PIDN:BAA00289.1; !1PID:g222708 CLASSIFICATION #superfamily vaccinia virus major envelope antigen KEYWORDS envelope protein SUMMARY #length 424 #molecular-weight 48873 #checksum 843 SEQUENCE /// ENTRY WMVZCX #type complete TITLE K4L protein - vaccinia virus (strain Copenhagen) ORGANISM #formal_name vaccinia virus #note host Homo sapiens (man) DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jul-1999 ACCESSIONS C42505 REFERENCE A42501 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:517-563 !$#title Appendix to "The complete DNA sequence of vaccinia virus". !$#accession C42505 !'##molecule_type DNA !'##residues 1-424 ##label GOE !'##cross-references GB:M35027; NID:g335317; PIDN:AAA48010.1; !1PID:g335358 REFERENCE A42531 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:247-266 !$#title The complete DNA sequence of vaccinia virus. !$#cross-references MUID:91021027; PMID:2219722 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given CLASSIFICATION #superfamily vaccinia virus major envelope antigen KEYWORDS envelope protein SUMMARY #length 424 #molecular-weight 48877 #checksum 835 SEQUENCE /// ENTRY WMVZ4 #type complete TITLE 42K protein - vaccinia virus ORGANISM #formal_name vaccinia virus DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 30-Sep-1993 ACCESSIONS A03870 REFERENCE A92988 !$#authors Venkatesan, S.; Gershowitz, A.; Moss, B. !$#journal J. Virol. (1982) 44:637-646 !$#title Complete nucleotide sequences of two adjacent early vaccinia !1virus genes located within the inverted terminal repetition. !$#cross-references MUID:83059924; PMID:7143577 !$#accession A03870 !'##molecule_type DNA !'##residues 1-331 ##label VEN CLASSIFICATION #superfamily vaccinia virus 42K protein SUMMARY #length 331 #molecular-weight 38504 #checksum 5611 SEQUENCE /// ENTRY WZVZB4 #type complete TITLE 37K HindIII-C protein - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS D33348 REFERENCE A94385 !$#authors Kotwal, G.J.; Moss, B. !$#journal Virology (1988) 167:524-537 !$#title Analysis of a large cluster of nonessential genes deleted !1from a vaccinia virus terminal transposition mutant. !$#cross-references MUID:89073756; PMID:2849238 !$#accession D33348 !'##molecule_type DNA !'##residues 1-315 ##label KOT !'##cross-references GB:M22812; NID:g335691; PIDN:AAA69604.1; !1PID:g893313 CLASSIFICATION #superfamily vaccinia virus 42K protein KEYWORDS early protein SUMMARY #length 315 #molecular-weight 37211 #checksum 2611 SEQUENCE /// ENTRY WMVZFV #type complete TITLE BamHI-ORF1 protein - fowlpox virus (isolate HP-438[Munich]) ORGANISM #formal_name fowlpox virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jun-2000 ACCESSIONS A29963 REFERENCE JT0442 !$#authors Tomley, F.; Binns, M.; Campbell, J.; Boursnell, M. !$#journal J. Gen. Virol. (1988) 69:1025-1040 !$#title Sequence analysis of an 11.2 kilobase, near-terminal, BamHI !1fragment of fowlpox virus. !$#cross-references MUID:88229622; PMID:2836548 !$#accession A29963 !'##molecule_type DNA !'##residues 1-418 ##label TOM !'##cross-references GB:D00295; NID:g221380; PIDN:BAA00190.1; !1PID:g221381 CLASSIFICATION #superfamily vaccinia virus 42K protein KEYWORDS early protein SUMMARY #length 418 #molecular-weight 48294 #checksum 7665 SEQUENCE /// ENTRY WMVZF4 #type complete TITLE BamHI-ORF4 protein - fowlpox virus (isolate HP-438[Munich]) ORGANISM #formal_name fowlpox virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jun-2000 ACCESSIONS D29963 REFERENCE JT0442 !$#authors Tomley, F.; Binns, M.; Campbell, J.; Boursnell, M. !$#journal J. Gen. Virol. (1988) 69:1025-1040 !$#title Sequence analysis of an 11.2 kilobase, near-terminal, BamHI !1fragment of fowlpox virus. !$#cross-references MUID:88229622; PMID:2836548 !$#accession D29963 !'##molecule_type DNA !'##residues 1-140 ##label TOM !'##cross-references GB:D00295; NID:g221380; PIDN:BAA00196.1; !1PID:g221387 CLASSIFICATION #superfamily fowlpox virus BamHI-ORF4 protein KEYWORDS early protein SUMMARY #length 140 #molecular-weight 16507 #checksum 4782 SEQUENCE /// ENTRY WMVZFF #type complete TITLE BamHI-ORF5 protein - fowlpox virus (isolate HP-438[Munich]) ORGANISM #formal_name fowlpox virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jun-2000 ACCESSIONS E29963 REFERENCE JT0442 !$#authors Tomley, F.; Binns, M.; Campbell, J.; Boursnell, M. !$#journal J. Gen. Virol. (1988) 69:1025-1040 !$#title Sequence analysis of an 11.2 kilobase, near-terminal, BamHI !1fragment of fowlpox virus. !$#cross-references MUID:88229622; PMID:2836548 !$#accession E29963 !'##molecule_type DNA !'##residues 1-105 ##label TOM !'##cross-references GB:D00295; NID:g221380; PIDN:BAA00197.1; !1PID:g221388 CLASSIFICATION #superfamily fowlpox virus BamHI-ORF5 protein KEYWORDS early protein SUMMARY #length 105 #molecular-weight 12574 #checksum 2378 SEQUENCE /// ENTRY WMVZF6 #type complete TITLE BamHI-ORF6 protein - fowlpox virus (isolate HP-438[Munich]) ORGANISM #formal_name fowlpox virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jun-2000 ACCESSIONS F29963 REFERENCE JT0442 !$#authors Tomley, F.; Binns, M.; Campbell, J.; Boursnell, M. !$#journal J. Gen. Virol. (1988) 69:1025-1040 !$#title Sequence analysis of an 11.2 kilobase, near-terminal, BamHI !1fragment of fowlpox virus. !$#cross-references MUID:88229622; PMID:2836548 !$#accession F29963 !'##molecule_type DNA !'##residues 1-151 ##label TOM !'##cross-references GB:D00295; NID:g221380; PIDN:BAA00198.1; !1PID:g221389 CLASSIFICATION #superfamily fowlpox virus BamHI-ORF6 protein KEYWORDS early protein SUMMARY #length 151 #molecular-weight 17967 #checksum 7869 SEQUENCE /// ENTRY WMVZFT #type complete TITLE BamHI-ORF10 protein - fowlpox virus (isolate HP-438[Munich]) ORGANISM #formal_name fowlpox virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jun-2000 ACCESSIONS A30087 REFERENCE JT0442 !$#authors Tomley, F.; Binns, M.; Campbell, J.; Boursnell, M. !$#journal J. Gen. Virol. (1988) 69:1025-1040 !$#title Sequence analysis of an 11.2 kilobase, near-terminal, BamHI !1fragment of fowlpox virus. !$#cross-references MUID:88229622; PMID:2836548 !$#accession A30087 !'##molecule_type DNA !'##residues 1-280 ##label TOM !'##cross-references GB:D00295; NID:g221380; PIDN:BAA00205.1; !1PID:g221396 CLASSIFICATION #superfamily fowlpox virus BamHI-ORF6 protein KEYWORDS early protein SUMMARY #length 280 #molecular-weight 33039 #checksum 8790 SEQUENCE /// ENTRY WMVZF9 #type complete TITLE BamHI-ORF9 protein - fowlpox virus (isolate HP-438[Munich]) ORGANISM #formal_name fowlpox virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jun-2000 ACCESSIONS I29963 REFERENCE JT0442 !$#authors Tomley, F.; Binns, M.; Campbell, J.; Boursnell, M. !$#journal J. Gen. Virol. (1988) 69:1025-1040 !$#title Sequence analysis of an 11.2 kilobase, near-terminal, BamHI !1fragment of fowlpox virus. !$#cross-references MUID:88229622; PMID:2836548 !$#accession I29963 !'##molecule_type DNA !'##residues 1-67 ##label TOM !'##cross-references GB:D00295; NID:g221380; PIDN:BAA00204.1; !1PID:g221395 CLASSIFICATION #superfamily fowlpox virus BamHI-ORF9 protein KEYWORDS early protein SUMMARY #length 67 #molecular-weight 7928 #checksum 1272 SEQUENCE /// ENTRY WMVZTW #type complete TITLE BamHI-ORF12 protein - fowlpox virus (isolate HP-438[Munich]) ORGANISM #formal_name fowlpox virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jun-2000 ACCESSIONS C30087 REFERENCE JT0442 !$#authors Tomley, F.; Binns, M.; Campbell, J.; Boursnell, M. !$#journal J. Gen. Virol. (1988) 69:1025-1040 !$#title Sequence analysis of an 11.2 kilobase, near-terminal, BamHI !1fragment of fowlpox virus. !$#cross-references MUID:88229622; PMID:2836548 !$#accession C30087 !'##molecule_type DNA !'##residues 1-188 ##label TOM !'##cross-references GB:D00295; NID:g221380; PIDN:BAA00207.1; !1PID:g221398 CLASSIFICATION #superfamily fowlpox virus BamHI-ORF12 protein KEYWORDS early protein SUMMARY #length 188 #molecular-weight 22462 #checksum 1253 SEQUENCE /// ENTRY WMVZTH #type fragment TITLE BamHI-ORF13 protein - fowlpox virus (isolate HP-438[Munich]) (fragment) ORGANISM #formal_name fowlpox virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jun-2000 ACCESSIONS D30087 REFERENCE JT0442 !$#authors Tomley, F.; Binns, M.; Campbell, J.; Boursnell, M. !$#journal J. Gen. Virol. (1988) 69:1025-1040 !$#title Sequence analysis of an 11.2 kilobase, near-terminal, BamHI !1fragment of fowlpox virus. !$#cross-references MUID:88229622; PMID:2836548 !$#accession D30087 !'##molecule_type DNA !'##residues 1-172 ##label TOM !'##cross-references GB:D00295; NID:g221380; PIDN:BAA00209.1; !1PID:g221400 CLASSIFICATION #superfamily fowlpox virus BamHI-ORF13 protein KEYWORDS early protein SUMMARY #length 172 #checksum 6507 SEQUENCE /// ENTRY WMVZ3W #type complete TITLE major core protein P4a - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus #note host Homo sapiens (man) DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS A43497 REFERENCE A43497 !$#authors Van Meir, E.; Wittek, R. !$#journal Arch. Virol. (1988) 102:19-27 !$#title Fine structure of the vaccinia virus gene encoding the !1precursor of the major core protein 4a. !$#cross-references MUID:89061367; PMID:3196167 !$#accession A43497 !'##molecule_type DNA !'##residues 1-891 ##label VAN !'##cross-references GB:M27634; NID:g335592; PIDN:AAA69585.1; !1PID:g335593 CLASSIFICATION #superfamily vaccinia virus major core protein P4a KEYWORDS core protein SUMMARY #length 891 #molecular-weight 102273 #checksum 9024 SEQUENCE /// ENTRY WMVZ3S #type complete TITLE major core protein P4a - vaccinia virus (strain Copenhagen) ALTERNATE_NAMES A10L protein ORGANISM #formal_name vaccinia virus #note host Homo sapiens (man) DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Jul-1999 ACCESSIONS C42518 REFERENCE A42501 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:517-563 !$#title Appendix to "The complete DNA sequence of vaccinia virus". !$#accession C42518 !'##molecule_type DNA !'##residues 1-891 ##label GOE !'##cross-references GB:M35027; NID:g335317; PIDN:AAA48129.1; !1PID:g335477 !'##experimental_source strain Copenhagen REFERENCE A42531 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:247-266 !$#title The complete DNA sequence of vaccinia virus. !$#cross-references MUID:91021027; PMID:2219722 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given CLASSIFICATION #superfamily vaccinia virus major core protein P4a KEYWORDS core protein SUMMARY #length 891 #molecular-weight 102283 #checksum 962 SEQUENCE /// ENTRY WMVZR0 #type complete TITLE 9K protein - vaccinia virus ORGANISM #formal_name vaccinia virus DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jul-1999 ACCESSIONS A23768 REFERENCE A93617 !$#authors Weinrich, S.L.; Hruby, D.E. !$#journal Nucleic Acids Res. (1986) 14:3003-3016 !$#title A tandemly-oriented late gene cluster within the vaccinia !1virus genome. !$#cross-references MUID:86176781; PMID:3008103 !$#accession A23768 !'##molecule_type DNA !'##residues 1-76 ##label WEI !'##cross-references GB:X03729; NID:g60836; PIDN:CAA27365.1; PID:g60837 !'##experimental_source strain WR COMMENT This protein is probably synthesized after viral DNA !1replication. CLASSIFICATION #superfamily vaccinia virus 9K protein KEYWORDS late protein SUMMARY #length 76 #molecular-weight 8954 #checksum 9397 SEQUENCE /// ENTRY WMVZR1 #type complete TITLE 26.3K late gene transactivator - vaccinia virus ALTERNATE_NAMES A2L protein ORGANISM #formal_name vaccinia virus DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 18-Feb-2000 ACCESSIONS B23768; D42517; T37388 REFERENCE A93617 !$#authors Weinrich, S.L.; Hruby, D.E. !$#journal Nucleic Acids Res. (1986) 14:3003-3016 !$#title A tandemly-oriented late gene cluster within the vaccinia !1virus genome. !$#cross-references MUID:86176781; PMID:3008103 !$#accession B23768 !'##molecule_type DNA !'##residues 1-224 ##label WEI !'##cross-references GB:X03729; NID:g60836; PIDN:CAA27366.1; PID:g60838 !'##experimental_source strain WR REFERENCE A33172 !$#authors Johnson, G.P. !$#submission submitted to GenBank, June 1990 !$#accession D42517 !'##molecule_type DNA !'##residues 1-224 ##label JOH !'##experimental_source strain Copenhagen REFERENCE Z20877 !$#authors Antoine, G.; Scheiflinger, F.; Falkner, F.G.; Dorner, F. !$#submission submitted to the EMBL Data Library, March 1997 !$#description The complete genomic sequence of the Modified Vaccinia !1Ankara (MVA) strain. !$#accession T37388 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-224 ##label ANT !'##cross-references EMBL:U94848; PIDN:AAB96455.1 !'##experimental_source strain Ankara COMMENT This protein is probably synthesized after viral DNA !1replication. GENETICS !$#note MVA112L CLASSIFICATION #superfamily vaccinia virus 26K protein KEYWORDS late protein; transcription regulation SUMMARY #length 224 #molecular-weight 26289 #checksum 606 SEQUENCE /// ENTRY WMVZR2 #type complete TITLE 17K protein - vaccinia virus ORGANISM #formal_name vaccinia virus DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 24-Sep-1999 ACCESSIONS C23768; A26351; A40246 REFERENCE A93617 !$#authors Weinrich, S.L.; Hruby, D.E. !$#journal Nucleic Acids Res. (1986) 14:3003-3016 !$#title A tandemly-oriented late gene cluster within the vaccinia !1virus genome. !$#cross-references MUID:86176781; PMID:3008103 !$#accession C23768 !'##molecule_type DNA !'##residues 1-150 ##label WEI !'##cross-references GB:X03729; NID:g60836; PIDN:CAA27367.1; PID:g60839 !'##experimental_source strain WR REFERENCE A94353 !$#authors Baldick Jr., C.J.; Moss, B. !$#journal Virology (1987) 156:138-145 !$#title Resistance of vaccinia virus to rifampicin conferred by a !1single nucleotide substitution near the predicted NH2 !1terminus of a gene encoding an Mr 62,000 polypeptide. !$#cross-references MUID:87122144; PMID:3811229 !$#accession A26351 !'##molecule_type DNA !'##residues 1-150 ##label BAL !'##cross-references GB:M16556; NID:g335729; PIDN:AAA48304.1; !1PID:g335730 REFERENCE A40246 !$#authors Carpenter, M.S.; DeLange, A.M. !$#journal Virology (1992) 188:233-244 !$#title Identification of a temperature-sensitive mutant of vaccinia !1virus defective in late but not intermediate gene !1expression. !$#cross-references MUID:92230221; PMID:1566576 !$#accession A40246 !'##molecule_type genomic RNA !'##residues 1-150 ##label CAR !'##cross-references GB:M86531; NID:g335303; PIDN:AAB59802.1; !1PID:g335304 !'##experimental_source strain WR, mutant tsC63 COMMENT This protein is probably synthesized after viral DNA !1replication. CLASSIFICATION #superfamily vaccinia virus 17K protein KEYWORDS late protein; transcription regulation SUMMARY #length 150 #molecular-weight 16906 #checksum 2139 SEQUENCE /// ENTRY FOVZZW #type complete TITLE major core protein P4b precursor - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 16-Jul-1999 ACCESSIONS A03871 REFERENCE A03871 !$#authors Rosel, J.; Moss, B. !$#journal J. Virol. (1985) 56:830-838 !$#title Transcriptional and translational mapping and nucleotide !1sequence analysis of a vaccinia virus gene encoding the !1precursor of the major core polypeptide 4b. !$#cross-references MUID:86062913; PMID:2999438 !$#accession A03871 !'##molecule_type DNA !'##residues 1-643 ##label ROS !'##cross-references GB:M11079; NID:g335714; PIDN:AAA48298.1; !1PID:g335715 CLASSIFICATION #superfamily vaccinia virus major core protein P4b KEYWORDS core protein FEATURE !$1-61 #domain leader peptide #status predicted #label LDR\ !$62-643 #product major core protein P4b #status predicted !8#label MAT SUMMARY #length 643 #molecular-weight 72498 #checksum 6741 SEQUENCE /// ENTRY FOVZ5R #type complete TITLE major core protein P4b precursor - vaccinia virus (strain Copenhagen) ALTERNATE_NAMES A3L protein ORGANISM #formal_name vaccinia virus #note host Homo sapiens (man) DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Jul-1999 ACCESSIONS E42517 REFERENCE A42501 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:517-563 !$#title Appendix to "The complete DNA sequence of vaccinia virus". !$#accession E42517 !'##molecule_type DNA !'##residues 1-644 ##label GOE !'##cross-references GB:M35027; NID:g335317; PIDN:AAA48118.1; !1PID:g335466 !'##experimental_source strain Copenhagen REFERENCE A42531 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:247-266 !$#title The complete DNA sequence of vaccinia virus. !$#cross-references MUID:91021027; PMID:2219722 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given CLASSIFICATION #superfamily vaccinia virus major core protein P4b KEYWORDS core protein FEATURE !$1-61 #domain leader peptide #status predicted #label LDR\ !$62-644 #product major core protein P4b #status predicted !8#label MAT SUMMARY #length 644 #molecular-weight 72624 #checksum 8615 SEQUENCE /// ENTRY FOVZFV #type complete TITLE major core protein P4b precursor - fowlpox virus (strain HP444) ORGANISM #formal_name fowlpox virus DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS A31474 REFERENCE A31474 !$#authors Binns, M.M.; Boursnell, M.E.G.; Tomley, F.M.; Campbell, J. !$#journal Virology (1989) 170:288-291 !$#title Analysis of the fowlpoxvirus gene encoding the 4b core !1polypeptide and demonstration that it possesses efficient !1promoter sequences. !$#cross-references MUID:89243190; PMID:2541544 !$#accession A31474 !'##molecule_type DNA !'##residues 1-657 ##label BIN !'##cross-references GB:M25781; NID:g341394; PIDN:AAA43817.1; !1PID:g538350 CLASSIFICATION #superfamily vaccinia virus major core protein P4b KEYWORDS core protein FEATURE !$1-60 #domain leader peptide #status predicted #label LDR\ !$61-657 #product major core protein P4b #status predicted !8#label MAT SUMMARY #length 657 #molecular-weight 75216 #checksum 6649 SEQUENCE /// ENTRY FOVZM1 #type complete TITLE M1 protein - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 21-Jan-2000 ACCESSIONS A29196; A33349 REFERENCE A94377 !$#authors Tamin, A.; Villarreal, E.C.; Weinrich, S.L.; Hruby, D.E. !$#journal Virology (1988) 165:141-150 !$#title Nucleotide sequence and molecular genetic analysis of the !1vaccinia virus HindIII N/M region encoding the genes !1responsible for resistance to alpha-amanitin. !$#cross-references MUID:88265853; PMID:3388767 !$#accession A29196 !'##molecule_type DNA !'##residues 1-421 ##label TAM !'##cross-references GB:M20779 REFERENCE A94385 !$#authors Kotwal, G.J.; Moss, B. !$#journal Virology (1988) 167:524-537 !$#title Analysis of a large cluster of nonessential genes deleted !1from a vaccinia virus terminal transposition mutant. !$#cross-references MUID:89073756; PMID:2849238 !$#accession A33349 !'##molecule_type DNA !'##residues 163-421 ##label KOT !'##cross-references GB:M22812; NID:g335691; PIDN:AAA69610.1; !1PID:g893319 COMMENT This protein may be responsible for resistance to !1alpha-amanitin. CLASSIFICATION #superfamily vaccinia virus M1 protein; ankyrin repeat !1homology; WD repeat homology KEYWORDS early protein FEATURE !$46-78 #domain WD repeat homology #label WD1\ !$46-78 #domain ankyrin repeat homology #label ANR\ !$79-103 #domain WD repeat homology #label WD2\ !$182-215 #domain WD repeat homology #label WD3\ !$216-249 #domain WD repeat homology #label WD4 SUMMARY #length 421 #molecular-weight 48024 #checksum 1591 SEQUENCE /// ENTRY FOVZN2 #type complete TITLE N2 protein - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS A94377; A94385; B29196; I33348 REFERENCE A94377 !$#authors Tamin, A.; Villarreal, E.C.; Weinrich, S.L.; Hruby, D.E. !$#journal Virology (1988) 165:141-150 !$#title Nucleotide sequence and molecular genetic analysis of the !1vaccinia virus HindIII N/M region encoding the genes !1responsible for resistance to alpha-amanitin. !$#cross-references MUID:88265853; PMID:3388767 !$#accession A94377 !'##molecule_type DNA !'##residues 1-175 ##label TAM !'##cross-references GB:M20779; NID:g335720; PIDN:AAA69612.1; !1PID:g893321 REFERENCE A94385 !$#authors Kotwal, G.J.; Moss, B. !$#journal Virology (1988) 167:524-537 !$#title Analysis of a large cluster of nonessential genes deleted !1from a vaccinia virus terminal transposition mutant. !$#cross-references MUID:89073756; PMID:2849238 !$#accession A94385 !'##molecule_type DNA !'##residues 1-175 ##label KOT !'##cross-references GB:M22812; NID:g335691; PIDN:AAA69609.1; !1PID:g893318 COMMENT This protein may be responsible for resistance to !1alpha-amanitin. CLASSIFICATION #superfamily vaccinia virus N2 protein KEYWORDS early protein SUMMARY #length 175 #molecular-weight 20852 #checksum 2135 SEQUENCE /// ENTRY QQVZP1 #type complete TITLE F1 protein - vaccinia virus (strain Copenhagen) ALTERNATE_NAMES G9R protein ORGANISM #formal_name vaccinia virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS E42512 REFERENCE A33172 !$#authors Johnson, G.P. !$#submission submitted to GenBank, June 1990 !$#accession E42512 !'##molecule_type DNA !'##residues 1-340 ##label JOH !'##cross-references GB:M35027; NID:g335317; PIDN:AAA48075.1; !1PID:g335423 CLASSIFICATION #superfamily vaccinia virus F1 protein SUMMARY #length 340 #molecular-weight 38786 #checksum 1472 SEQUENCE /// ENTRY QQVZF1 #type fragment TITLE F1 protein - vaccinia virus (strain WR) (fragment) ORGANISM #formal_name vaccinia virus DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 28-May-1999 ACCESSIONS A23092 REFERENCE A23092 !$#authors Plucienniczak, A.; Schroeder, E.; Zettlmeissl, G.; Streeck, !1R.E. !$#journal Nucleic Acids Res. (1985) 13:985-998 !$#title Nucleotide sequence of a cluster of early and late genes in !1a conserved segment of the vaccinia virus genome. !$#cross-references MUID:85215527; PMID:2987815 !$#accession A23092 !'##molecule_type DNA !'##residues 1-303 ##label PLU !'##cross-references GB:X01978; GB:J02424; GB:J02425; GB:K02376; !1GB:M15211; GB:V01537; NID:g61387; PIDN:CAA26009.1; !1PID:g61388 COMMENT It is unknown whether this protein is synthesized before or !1after viral DNA replication. CLASSIFICATION #superfamily vaccinia virus F1 protein SUMMARY #length 303 #checksum 4882 SEQUENCE /// ENTRY WMVZP1 #type complete TITLE F1 protein - fowlpox virus (strain HP444) ORGANISM #formal_name fowlpox virus DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jun-2000 ACCESSIONS JS0221 REFERENCE JS0220 !$#authors Binns, M.M.; Tomley, F.M.; Campbell, J.; Boursnell, M.E.G. !$#journal J. Gen. Virol. (1988) 69:1275-1283 !$#title Comparison of a conserved region in fowlpox virus and !1vaccinia virus genomes and the translocation of the fowlpox !1virus thymidine kinase gene. !$#cross-references MUID:88258470; PMID:2838574 !$#accession JS0221 !'##molecule_type DNA !'##residues 1-336 ##label BIN !'##cross-references GB:D00320; NID:g221401; PIDN:BAA00224.1; !1PID:g221403 CLASSIFICATION #superfamily vaccinia virus F1 protein SUMMARY #length 336 #molecular-weight 38092 #checksum 1375 SEQUENCE /// ENTRY QQVZF2 #type complete TITLE F2 protein - vaccinia virus ORGANISM #formal_name vaccinia virus DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 08-Apr-1994 ACCESSIONS B23092 REFERENCE A23092 !$#authors Plucienniczak, A.; Schroeder, E.; Zettlmeissl, G.; Streeck, !1R.E. !$#journal Nucleic Acids Res. (1985) 13:985-998 !$#title Nucleotide sequence of a cluster of early and late genes in !1a conserved segment of the vaccinia virus genome. !$#cross-references MUID:85215527; PMID:2987815 !$#accession B23092 !'##molecule_type DNA !'##residues 1-250 ##label PLU !'##experimental_source strain WR COMMENT This protein is probably synthesized after viral DNA !1replication. CLASSIFICATION #superfamily vaccinia virus F2 protein KEYWORDS late protein SUMMARY #length 250 #molecular-weight 27280 #checksum 4335 SEQUENCE /// ENTRY WMVZP2 #type complete TITLE F2 protein - fowlpox virus (strain HP444) ORGANISM #formal_name fowlpox virus DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jun-2000 ACCESSIONS JS0222 REFERENCE JS0220 !$#authors Binns, M.M.; Tomley, F.M.; Campbell, J.; Boursnell, M.E.G. !$#journal J. Gen. Virol. (1988) 69:1275-1283 !$#title Comparison of a conserved region in fowlpox virus and !1vaccinia virus genomes and the translocation of the fowlpox !1virus thymidine kinase gene. !$#cross-references MUID:88258470; PMID:2838574 !$#accession JS0222 !'##molecule_type DNA !'##residues 1-243 ##label BIN !'##cross-references GB:D00320; NID:g221401; PIDN:BAA00225.1; !1PID:g221404 CLASSIFICATION #superfamily vaccinia virus F2 protein SUMMARY #length 243 #molecular-weight 26620 #checksum 5087 SEQUENCE /// ENTRY QQVZF3 #type complete TITLE F3 protein - vaccinia virus ORGANISM #formal_name vaccinia virus DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 28-May-1999 ACCESSIONS C23092 REFERENCE A23092 !$#authors Plucienniczak, A.; Schroeder, E.; Zettlmeissl, G.; Streeck, !1R.E. !$#journal Nucleic Acids Res. (1985) 13:985-998 !$#title Nucleotide sequence of a cluster of early and late genes in !1a conserved segment of the vaccinia virus genome. !$#cross-references MUID:85215527; PMID:2987815 !$#accession C23092 !'##molecule_type DNA !'##residues 1-92 ##label PLU !'##cross-references GB:X01978; GB:J02424; GB:J02425; GB:K02376; !1GB:M15211; GB:V01537; NID:g61387; PIDN:CAA26011.1; !1PID:g61390 !'##experimental_source strain WR COMMENT It is unknown whether this protein is synthesized before or !1after viral DNA replication. CLASSIFICATION #superfamily vaccinia virus F3 protein SUMMARY #length 92 #molecular-weight 10776 #checksum 3242 SEQUENCE /// ENTRY WMVZP3 #type complete TITLE F3 protein - fowlpox virus (strain HP444) ORGANISM #formal_name fowlpox virus DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jun-2000 ACCESSIONS JS0223 REFERENCE JS0220 !$#authors Binns, M.M.; Tomley, F.M.; Campbell, J.; Boursnell, M.E.G. !$#journal J. Gen. Virol. (1988) 69:1275-1283 !$#title Comparison of a conserved region in fowlpox virus and !1vaccinia virus genomes and the translocation of the fowlpox !1virus thymidine kinase gene. !$#cross-references MUID:88258470; PMID:2838574 !$#accession JS0223 !'##molecule_type DNA !'##residues 1-96 ##label BIN !'##cross-references GB:D00320; NID:g221401; PIDN:BAA00226.1; !1PID:g221405 CLASSIFICATION #superfamily vaccinia virus F3 protein SUMMARY #length 96 #molecular-weight 11250 #checksum 7731 SEQUENCE /// ENTRY QQVZF4 #type complete TITLE F4 protein - vaccinia virus ORGANISM #formal_name vaccinia virus DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 28-May-1999 ACCESSIONS A26216; K23092 REFERENCE A23092 !$#authors Plucienniczak, A.; Schroeder, E.; Zettlmeissl, G.; Streeck, !1R.E. !$#journal Nucleic Acids Res. (1985) 13:985-998 !$#title Nucleotide sequence of a cluster of early and late genes in !1a conserved segment of the vaccinia virus genome. !$#cross-references MUID:85215527; PMID:2987815 !$#accession A26216 !'##molecule_type DNA !'##residues 1-350 ##label PLU !'##cross-references GB:X01978; GB:J02424; GB:J02425; GB:K02376; !1GB:M15211; GB:V01537; NID:g61387; PIDN:CAA26012.1; !1PID:g61391 !'##experimental_source strain WR COMMENT This protein is probably synthesized after viral DNA !1replication. CLASSIFICATION #superfamily vaccinia virus F4 protein KEYWORDS late protein SUMMARY #length 350 #molecular-weight 40620 #checksum 8769 SEQUENCE /// ENTRY WMVZP4 #type complete TITLE F4 protein - fowlpox virus (strain HP444) ORGANISM #formal_name fowlpox virus DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jun-2000 ACCESSIONS JS0224 REFERENCE JS0220 !$#authors Binns, M.M.; Tomley, F.M.; Campbell, J.; Boursnell, M.E.G. !$#journal J. Gen. Virol. (1988) 69:1275-1283 !$#title Comparison of a conserved region in fowlpox virus and !1vaccinia virus genomes and the translocation of the fowlpox !1virus thymidine kinase gene. !$#cross-references MUID:88258470; PMID:2838574 !$#accession JS0224 !'##molecule_type DNA !'##residues 1-301 ##label BIN !'##cross-references GB:D00320; NID:g221401; PIDN:BAA00227.1; !1PID:g221406 CLASSIFICATION #superfamily vaccinia virus F4 protein SUMMARY #length 301 #molecular-weight 35367 #checksum 8233 SEQUENCE /// ENTRY S46850 #type complete TITLE J8R protein - variola virus ALTERNATE_NAMES A55R protein (C-terminal) ORGANISM #formal_name variola virus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 22-Oct-2001 ACCESSIONS S46850; G36854 REFERENCE S46842 !$#authors Kolykhalov, A.A.; Blinov, V.M.; Frolov, I.V.; Totmenin, !1A.V.; Shchelkunov, S.N.; Sandakhchiev, L.S. !$#submission submitted to the EMBL Data Library, April 1992 !$#description Nucleotide sequence analysis of the region of variola virus !1HindIII-J genome fragment. !$#accession S46850 !'##status preliminary !'##molecule_type DNA !'##residues 1-172 ##label KOL !'##cross-references EMBL:X67118; NID:g516399; PIDN:CAA47551.1; !1PID:g516409 !'##experimental_source strain India-1967, isolate Ind3 REFERENCE A36859 !$#authors Blinov, V.M. !$#submission submitted to GenBank, November 1992 !$#accession G36854 !'##status preliminary !'##molecule_type DNA !'##residues 1-172 ##label BLI !'##cross-references GB:X69198; NID:g456758; PIDN:CAA49107.1; !1PID:g457057 !'##experimental_source strain India-1967, ssp. major, isolate Ind3 CLASSIFICATION #superfamily J8R protein SUMMARY #length 172 #molecular-weight 19960 #checksum 6098 SEQUENCE /// ENTRY JQ1861 #type complete TITLE 30R protein - variola major virus ORGANISM #formal_name variola major virus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 22-Oct-2001 ACCESSIONS JQ1861; T28597 REFERENCE JQ1832 !$#authors Aguado, B.; Selmes, I.P.; Smith, G.L. !$#journal J. Gen. Virol. (1992) 73:2887-2902 !$#title Nucleotide sequence of 21.8 kbp of variola major virus !1strain Harvey and comparison with vaccinia virus. !$#cross-references MUID:93057361; PMID:1331292 !$#accession JQ1861 !'##molecule_type DNA !'##residues 1-172 ##label AGU !'##experimental_source strain Harver REFERENCE Z20488 !$#authors Massung, R.F.; Esposito, J.J.; Liu, L.I.; Qi, J.; Utterback, !1T.R.; Knight, J.C.; Aubin, L.; Yuran, T.E.; Parsons, J.M.; !1Loparev, V.N. !$#journal Nature (1993) 366:748-751 !$#title Potential virulence determinants in terminal regions of !1variola smallpox virus genome. !$#cross-references MUID:94088747; PMID:8264798 !$#accession T28597 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-172 ##label MAS !'##cross-references EMBL:L22579; NID:g623595; PIDN:AAA60907.1; !1PID:g439076 !'##experimental_source strain Bangladesh 1975 CLASSIFICATION #superfamily J8R protein SUMMARY #length 172 #molecular-weight 19960 #checksum 6098 SEQUENCE /// ENTRY JQ1860 #type complete TITLE J7R protein - variola major virus (strains India-1967 and Harvey) ALTERNATE_NAMES 29R protein ORGANISM #formal_name variola major virus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 22-Oct-2001 ACCESSIONS S46849; F36854; JQ1860 REFERENCE S46842 !$#authors Kolykhalov, A.A.; Blinov, V.M.; Frolov, I.V.; Totmenin, !1A.V.; Shchelkunov, S.N.; Sandakhchiev, L.S. !$#submission submitted to the EMBL Data Library, April 1992 !$#description Nucleotide sequence analysis of the region of variola virus !1HindIII-J genome fragment. !$#accession S46849 !'##molecule_type DNA !'##residues 1-71 ##label KOL !'##cross-references EMBL:X67118; NID:g516399; PIDN:CAA47550.1; !1PID:g516408 !'##experimental_source strain India-1967, isolate Ind3 REFERENCE A36859 !$#authors Blinov, V.M. !$#submission submitted to GenBank, November 1992 !$#accession F36854 !'##molecule_type DNA !'##residues 1-71 ##label BLI !'##cross-references GB:X69198; NID:g456758; PIDN:CAA49106.1; !1PID:g457056 !'##experimental_source strain India-1967, ssp. major, isolate Ind3 REFERENCE JQ1832 !$#authors Aguado, B.; Selmes, I.P.; Smith, G.L. !$#journal J. Gen. Virol. (1992) 73:2887-2902 !$#title Nucleotide sequence of 21.8 kbp of variola major virus !1strain Harvey and comparison with vaccinia virus. !$#cross-references MUID:93057361; PMID:1331292 !$#accession JQ1860 !'##molecule_type DNA !'##residues 1-71 ##label AGU !'##experimental_source strain Harvey CLASSIFICATION #superfamily J7R protein SUMMARY #length 71 #molecular-weight 8218 #checksum 5305 SEQUENCE /// ENTRY QQVZF6 #type complete TITLE F6 protein - vaccinia virus ALTERNATE_NAMES L5R protein ORGANISM #formal_name vaccinia virus DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 28-May-1999 ACCESSIONS E23092; C42513 REFERENCE A23092 !$#authors Plucienniczak, A.; Schroeder, E.; Zettlmeissl, G.; Streeck, !1R.E. !$#journal Nucleic Acids Res. (1985) 13:985-998 !$#title Nucleotide sequence of a cluster of early and late genes in !1a conserved segment of the vaccinia virus genome. !$#cross-references MUID:85215527; PMID:2987815 !$#accession E23092 !'##molecule_type DNA !'##residues 1-128 ##label PLU !'##cross-references GB:X01978; GB:J02424; GB:J02425; GB:K02376; !1GB:M15211; GB:V01537; NID:g61387; PIDN:CAA26014.1; !1PID:g61393 !'##experimental_source strain WR REFERENCE A33172 !$#authors Johnson, G.P. !$#submission submitted to GenBank, June 1990 !$#accession C42513 !'##molecule_type DNA !'##residues 1-128 ##label JOH !'##experimental_source strain Copenhagen COMMENT It is not known whether this protein is synthesized before !1or after viral DNA replication. CLASSIFICATION #superfamily vaccinia virus F6 protein SUMMARY #length 128 #molecular-weight 15044 #checksum 2653 SEQUENCE /// ENTRY WMVZP6 #type complete TITLE F6 protein - fowlpox virus (strain HP444) ORGANISM #formal_name fowlpox virus DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jun-2000 ACCESSIONS JS0226 REFERENCE JS0220 !$#authors Binns, M.M.; Tomley, F.M.; Campbell, J.; Boursnell, M.E.G. !$#journal J. Gen. Virol. (1988) 69:1275-1283 !$#title Comparison of a conserved region in fowlpox virus and !1vaccinia virus genomes and the translocation of the fowlpox !1virus thymidine kinase gene. !$#cross-references MUID:88258470; PMID:2838574 !$#accession JS0226 !'##molecule_type DNA !'##residues 1-129 ##label BIN !'##cross-references GB:D00320; NID:g221401; PIDN:BAA00229.1; !1PID:g221408 CLASSIFICATION #superfamily vaccinia virus F6 protein SUMMARY #length 129 #molecular-weight 14745 #checksum 2120 SEQUENCE /// ENTRY QQVZF7 #type complete TITLE F7 protein - vaccinia virus ORGANISM #formal_name vaccinia virus DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 28-May-1999 ACCESSIONS F23092 REFERENCE A23092 !$#authors Plucienniczak, A.; Schroeder, E.; Zettlmeissl, G.; Streeck, !1R.E. !$#journal Nucleic Acids Res. (1985) 13:985-998 !$#title Nucleotide sequence of a cluster of early and late genes in !1a conserved segment of the vaccinia virus genome. !$#cross-references MUID:85215527; PMID:2987815 !$#accession F23092 !'##molecule_type DNA !'##residues 1-153 ##label PLU !'##cross-references GB:X01978; GB:J02424; GB:J02425; GB:K02376; !1GB:M15211; GB:V01537; NID:g61387; PIDN:CAA26015.1; !1PID:g61394 !'##experimental_source strain WR COMMENT It is unknown whether this protein is synthesized before or !1after viral DNA replication. CLASSIFICATION #superfamily vaccinia virus F7 protein SUMMARY #length 153 #molecular-weight 17921 #checksum 1805 SEQUENCE /// ENTRY QQVZCP #type complete TITLE F7 protein - sheep pox virus (isolate Kenya sheep-1, KS-1) ORGANISM #formal_name sheep pox virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jun-2000 ACCESSIONS A31813 REFERENCE A31813 !$#authors Gershon, P.D.; Black, D.N. !$#journal J. Gen. Virol. (1989) 70:525-533 !$#title The nucleotide sequence around the capripoxvirus thymidine !1kinase gene reveals a gene shared specifically with !1leporipoxvirus. !$#cross-references MUID:89279233; PMID:2732700 !$#accession A31813 !'##molecule_type DNA !'##residues 1-147 ##label GER !'##cross-references GB:D00423; NID:g221120; PIDN:BAA00323.1; !1PID:g221122 CLASSIFICATION #superfamily vaccinia virus F7 protein SUMMARY #length 147 #molecular-weight 17381 #checksum 6724 SEQUENCE /// ENTRY QQVZM2 #type complete TITLE F7 protein - myxoma virus ALTERNATE_NAMES MF7 protein ORGANISM #formal_name myxoma virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS JQ1422 REFERENCE JQ1421 !$#authors Jackson, R.J.; Bults, H.G. !$#journal J. Gen. Virol. (1992) 73:323-328 !$#title The myxoma virus thymidine kinase gene: sequence and !1transcriptional mapping. !$#cross-references MUID:92166739; PMID:1538190 !$#accession JQ1422 !'##molecule_type DNA !'##residues 1-148 ##label JAC !'##cross-references GB:X52655; NID:g987956; PIDN:CAA36879.1; PID:g60615 CLASSIFICATION #superfamily vaccinia virus F7 protein SUMMARY #length 148 #molecular-weight 17108 #checksum 5813 SEQUENCE /// ENTRY WMVZP7 #type complete TITLE F7 protein - fowlpox virus (strain HP444) ORGANISM #formal_name fowlpox virus DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jun-2000 ACCESSIONS JS0227 REFERENCE JS0220 !$#authors Binns, M.M.; Tomley, F.M.; Campbell, J.; Boursnell, M.E.G. !$#journal J. Gen. Virol. (1988) 69:1275-1283 !$#title Comparison of a conserved region in fowlpox virus and !1vaccinia virus genomes and the translocation of the fowlpox !1virus thymidine kinase gene. !$#cross-references MUID:88258470; PMID:2838574 !$#accession JS0227 !'##molecule_type DNA !'##residues 1-148 ##label BIN !'##cross-references GB:D00320; NID:g221401; PIDN:BAA00230.1; !1PID:g221409 CLASSIFICATION #superfamily vaccinia virus F7 protein SUMMARY #length 148 #molecular-weight 16953 #checksum 7732 SEQUENCE /// ENTRY S46847 #type complete TITLE hypothetical protein J6R - variola major virus (strains India-1967 and Harvey) ALTERNATE_NAMES 28R protein; A52R protein (middle) ORGANISM #formal_name variola major virus DATE 24-Nov-1999 #sequence_revision 24-Nov-1999 #text_change 24-May-2001 ACCESSIONS S46847; E36854; JQ1859 REFERENCE S46842 !$#authors Kolykhalov, A.A.; Blinov, V.M.; Frolov, I.V.; Totmenin, !1A.V.; Shchelkunov, S.N.; Sandakhchiev, L.S. !$#submission submitted to the EMBL Data Library, April 1992 !$#description Nucleotide sequence analysis of the region of variola virus !1HindIII-J genome fragment. !$#accession S46847 !'##molecule_type DNA !'##residues 1-71 ##label KOL !'##cross-references EMBL:X67118; NID:g516399; PIDN:CAA47548.1; !1PID:g516406 !'##experimental_source strain India-1967, isolate Ind3 REFERENCE A36859 !$#authors Blinov, V.M. !$#submission submitted to GenBank, November 1992 !$#accession E36854 !'##molecule_type DNA !'##residues 1-71 ##label BLI !'##cross-references GB:X69198; NID:g456758; PIDN:CAA49105.1; !1PID:g457055 !'##experimental_source strain India-1967, ssp. major, isolate Ind3 REFERENCE JQ1832 !$#authors Aguado, B.; Selmes, I.P.; Smith, G.L. !$#journal J. Gen. Virol. (1992) 73:2887-2902 !$#title Nucleotide sequence of 21.8 kbp of variola major virus !1strain Harvey and comparison with vaccinia virus. !$#cross-references MUID:93057361; PMID:1331292 !$#accession JQ1859 !'##molecule_type DNA !'##residues 1-67 ##label AGU !'##experimental_source strain Harvey CLASSIFICATION #superfamily variola major virus hypothetical protein J6R SUMMARY #length 71 #molecular-weight 8460 #checksum 188 SEQUENCE /// ENTRY D36852 #type complete TITLE hypothetical protein A39R - variola major virus (strains India-1967 and Harvey) ALTERNATE_NAMES 10R protein; A38R protein; vaccinia virus A36R protein ORGANISM #formal_name variola major virus DATE 24-Nov-1999 #sequence_revision 24-Nov-1999 #text_change 23-Mar-2001 ACCESSIONS D36852; S46866; JQ1841 REFERENCE A36859 !$#authors Blinov, V.M. !$#submission submitted to GenBank, November 1992 !$#accession D36852 !'##molecule_type DNA !'##residues 1-216 ##label BLI !'##cross-references GB:X69198; NID:g456758; PIDN:CAA49084.1; !1PID:g457034 !'##experimental_source strain India-1967, ssp. major, isolate Ind3 REFERENCE S46841 !$#authors Kolykhalov, A.A.; Blinov, V.M.; Frolov, I.V.; Totmenin, !1A.V.; Shchelkunov, S.N.; Sandakhchiev, L.S. !$#submission submitted to the EMBL Data Library, April 1992 !$#description Nucleotide sequence analysis of the region of variola virus !1XhoI-E genome fragment. !$#accession S46866 !'##molecule_type DNA !'##residues 1-216 ##label KOL !'##cross-references EMBL:X67115; NID:g516412; PIDN:CAA47510.1; !1PID:g516426 !'##experimental_source strain India-1967, isolate Ind3 REFERENCE JQ1832 !$#authors Aguado, B.; Selmes, I.P.; Smith, G.L. !$#journal J. Gen. Virol. (1992) 73:2887-2902 !$#title Nucleotide sequence of 21.8 kbp of variola major virus !1strain Harvey and comparison with vaccinia virus. !$#cross-references MUID:93057361; PMID:1331292 !$#accession JQ1841 !'##molecule_type DNA !'##residues 1-216 ##label AGU !'##experimental_source strain Harvey CLASSIFICATION #superfamily variola major virus hypothetical protein A39R KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-25 #domain transmembrane #status predicted #label TMM\ !$50,60,79,99,134, !$139,166 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 216 #molecular-weight 24492 #checksum 4162 SEQUENCE /// ENTRY T28580 #type complete TITLE hypothetical protein A38R - variola major virus (strain Bangladesh-1975) ALTERNATE_NAMES 10R protein; A36R protein; A39R protein ORGANISM #formal_name variola major virus DATE 24-Nov-1999 #sequence_revision 24-Nov-1999 #text_change 21-Jul-2000 ACCESSIONS T28580 REFERENCE Z20488 !$#authors Massung, R.F.; Esposito, J.J.; Liu, L.I.; Qi, J.; Utterback, !1T.R.; Knight, J.C.; Aubin, L.; Yuran, T.E.; Parsons, J.M.; !1Loparev, V.N. !$#journal Nature (1993) 366:748-751 !$#title Potential virulence determinants in terminal regions of !1variola smallpox virus genome. !$#cross-references MUID:94088747; PMID:8264798 !$#accession T28580 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-216 ##label MAS !'##cross-references EMBL:L22579; NID:g623595; PIDN:AAA60890.1; !1PID:g439059 !'##experimental_source strain Bangladesh 1975 CLASSIFICATION #superfamily variola major virus hypothetical protein A39R KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-25 #domain transmembrane #status predicted #label TMM\ !$50,60,79,99,134, !$139,166 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 216 #molecular-weight 24491 #checksum 4512 SEQUENCE /// ENTRY B42521 #type complete TITLE hypothetical protein A36R - vaccinia virus (strains WR and Copenhagen) ALTERNATE_NAMES 10R protein; A38R protein; A39R protein; SalL6R protein ORGANISM #formal_name vaccinia virus DATE 24-Nov-1999 #sequence_revision 24-Nov-1999 #text_change 16-Jun-2000 ACCESSIONS JQ1772; S29919; B42521 REFERENCE JQ1767 !$#authors Smith, G.L.; Chan, Y.S.; Howard, S.T. !$#journal J. Gen. Virol. (1991) 72:1349-1376 !$#title Nucleotide sequence of 42kbp of vaccinia virus strain WR !1from near the right inverted terminal repeat. !$#cross-references MUID:91259063; PMID:2045793 !$#accession JQ1772 !'##molecule_type DNA !'##residues 1-221 ##label SMI !'##cross-references DDBJ:D11079; NID:g222717; PIDN:BAA01808.1; !1PID:g222723 !'##experimental_source strain WR REFERENCE S29907 !$#authors Amegadzie, B.Y. !$#submission submitted to the EMBL Data Library, January 1991 !$#accession S29919 !'##status preliminary !'##molecule_type DNA !'##residues 1-221 ##label AME !'##cross-references EMBL:X57318; NID:g62239; PIDN:CAA40585.1; !1PID:g62252 REFERENCE A33172 !$#authors Johnson, G.P. !$#submission submitted to GenBank, June 1990 !$#accession B42521 !'##status preliminary !'##molecule_type DNA !'##residues 1-221 ##label JOH !'##experimental_source strain Copenhagen CLASSIFICATION #superfamily variola major virus hypothetical protein A39R KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-25 #domain transmembrane #status predicted #label TMM\ !$50,79,99,134,140, !$157,167 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 221 #molecular-weight 25133 #checksum 3355 SEQUENCE /// ENTRY G36852 #type complete TITLE hypothetical protein A42R - variola major virus (strains India-1967 and Harvey) ALTERNATE_NAMES 13R protein ORGANISM #formal_name variola major virus DATE 24-Nov-1999 #sequence_revision 24-Nov-1999 #text_change 24-Nov-1999 ACCESSIONS G36852; JQ1844 REFERENCE A36859 !$#authors Blinov, V.M. !$#submission submitted to GenBank, November 1992 !$#accession G36852 !'##molecule_type DNA !'##residues 1-74 ##label BLI !'##cross-references GB:X69198; NID:g456758; PIDN:CAA49089.1; !1PID:g457039 REFERENCE JQ1832 !$#authors Aguado, B.; Selmes, I.P.; Smith, G.L. !$#journal J. Gen. Virol. (1992) 73:2887-2902 !$#title Nucleotide sequence of 21.8 kbp of variola major virus !1strain Harvey and comparison with vaccinia virus. !$#cross-references MUID:93057361; PMID:1331292 !$#accession JQ1844 !'##molecule_type DNA !'##residues 1-69 ##label AGU !'##experimental_source strain Harvey CLASSIFICATION #superfamily variola major virus hypothetical protein A42R SUMMARY #length 74 #molecular-weight 8465 #checksum 9593 SEQUENCE /// ENTRY I36853 #type complete TITLE hypothetical protein J1L - variola major virus (strains India-1967, Bangladesh-1975, and Harvey) ALTERNATE_NAMES 22L protein; 23L protein; A47L protein homolog ORGANISM #formal_name variola major virus DATE 24-Nov-1999 #sequence_revision 24-Nov-1999 #text_change 24-May-2001 ACCESSIONS I36853; S46841; JQ1854; JQ1853; T28592 REFERENCE A36859 !$#authors Blinov, V.M. !$#submission submitted to GenBank, November 1992 !$#accession I36853 !'##molecule_type DNA !'##residues 1-244 ##label BLI !'##cross-references GB:X69198; NID:g456758; PIDN:CAA49100.1; !1PID:g457050 !'##experimental_source strain India-1967, isolate Ind3 REFERENCE S46842 !$#authors Kolykhalov, A.A.; Blinov, V.M.; Frolov, I.V.; Totmenin, !1A.V.; Shchelkunov, S.N.; Sandakhchiev, L.S. !$#submission submitted to the EMBL Data Library, April 1992 !$#description Nucleotide sequence analysis of the region of variola virus !1HindIII-J genome fragment. !$#accession S46841 !'##molecule_type DNA !'##residues 1-87 ##label KOL !'##cross-references EMBL:X67118; NID:g516399; PIDN:CAA47542.1; !1PID:g516400 !'##experimental_source strain India-1967, isolate Ind3 REFERENCE JQ1832 !$#authors Aguado, B.; Selmes, I.P.; Smith, G.L. !$#journal J. Gen. Virol. (1992) 73:2887-2902 !$#title Nucleotide sequence of 21.8 kbp of variola major virus !1strain Harvey and comparison with vaccinia virus. !$#cross-references MUID:93057361; PMID:1331292 !$#accession JQ1854 !'##molecule_type DNA !'##residues 1-87 ##label AGU !'##experimental_source strain Harvey !$#accession JQ1853 !'##molecule_type DNA !'##residues 110-244 ##label AG2 !'##experimental_source strain Harvey REFERENCE Z20488 !$#authors Massung, R.F.; Esposito, J.J.; Liu, L.I.; Qi, J.; Utterback, !1T.R.; Knight, J.C.; Aubin, L.; Yuran, T.E.; Parsons, J.M.; !1Loparev, V.N. !$#journal Nature (1993) 366:748-751 !$#title Potential virulence determinants in terminal regions of !1variola smallpox virus genome. !$#cross-references MUID:94088747; PMID:8264798 !$#accession T28592 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-244 ##label MAS !'##cross-references EMBL:L22579; NID:g623595; PIDN:AAA60902.1; !1PID:g439071 !'##experimental_source strain Bangladesh-1975 GENETICS !$#gene J1L CLASSIFICATION #superfamily variola major virus hypothetical protein J1L SUMMARY #length 244 #molecular-weight 28389 #checksum 7917 SEQUENCE /// ENTRY QQVZF9 #type complete TITLE poly(A) polymerase subunit - vaccinia virus ALTERNATE_NAMES F9 protein; mRNA maturation bifunctional enzyme VP39 CONTAINS mRNA (nucleoside-2'-O-)-methyltransferase (EC 2.1.1.57) (VP39); polynucleotide adenylyltransferase (EC 2.7.7.19) non-catalytic small chain VP39 ORGANISM #formal_name vaccinia virus DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 18-Feb-2000 ACCESSIONS H23092; A42693; T37363 REFERENCE A23092 !$#authors Plucienniczak, A.; Schroeder, E.; Zettlmeissl, G.; Streeck, !1R.E. !$#journal Nucleic Acids Res. (1985) 13:985-998 !$#title Nucleotide sequence of a cluster of early and late genes in !1a conserved segment of the vaccinia virus genome. !$#cross-references MUID:85215527; PMID:2987815 !$#accession H23092 !'##molecule_type DNA !'##residues 1-333 ##label PLU !'##cross-references GB:X01978; GB:J02424; GB:J02425; GB:K02376; !1GB:M15211; GB:V01537; NID:g61387; PIDN:CAA26017.1; !1PID:g61396 !'##experimental_source strain WR REFERENCE A58200 !$#authors Hodel, A.E.; Gershon, P.D.; Shi, X.; Quiocho, F.A. !$#journal Cell (1996) 85:247-256 !$#title The 1.85 angstroms structure of vaccinia protein VP39: a !1bifunctional enzyme that participates in the modification of !1both mRNA ends. !$#cross-references MUID:96200776; PMID:8612277 !$#contents annotation; X-ray structure of variant with cofactor at 1.85 !1anstroms resolution REFERENCE A42693 !$#authors Schnierle, B.S.; Gershon, P.D.; Moss, B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:2897-2901 !$#title Cap-specific mRNA (nucleoside-O(2'-)-methyltransferase and !1poly(A) polymerase stimulatory activities of vaccinia virus !1are mediated by a single protein. !$#cross-references MUID:92212937; PMID:1313572 !$#accession A42693 !'##status preliminary !'##molecule_type protein !'##residues 196-205;210-219;247-256,'F' ##label SCH REFERENCE Z20877 !$#authors Antoine, G.; Scheiflinger, F.; Falkner, F.G.; Dorner, F. !$#submission submitted to the EMBL Data Library, March 1997 !$#description The complete genomic sequence of the Modified Vaccinia !1Ankara (MVA) strain. !$#accession T37363 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-333 ##label ANT !'##cross-references EMBL:U94848; PIDN:AAB96504.1 !'##experimental_source strain Ankara COMMENT This protein is synthesized before viral DNA replication. GENETICS !$#note MVA087R FUNCTION 5PRI !$#description acts as an mRNA cap-specific mRNA !1(nucleoside-2'-O-)-methyltransferase FUNCTION 3PRI !$#description acts as small subunit of heterodimeric poly(A) polymerase CLASSIFICATION #superfamily vaccinia virus F9 protein KEYWORDS cytosol; early protein; heterodimer; methyltransferase; mRNA !1capping; multifunctional enzyme; nucleotidyltransferase; RNA !1binding; S-adenosylmethionine SUMMARY #length 333 #molecular-weight 38888 #checksum 699 SEQUENCE /// ENTRY QQVZC9 #type fragment TITLE F9 protein - sheep pox virus (isolate Kenya sheep-1, KS-1) (fragment) ORGANISM #formal_name sheep pox virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jun-2000 ACCESSIONS D31813 REFERENCE A31813 !$#authors Gershon, P.D.; Black, D.N. !$#journal J. Gen. Virol. (1989) 70:525-533 !$#title The nucleotide sequence around the capripoxvirus thymidine !1kinase gene reveals a gene shared specifically with !1leporipoxvirus. !$#cross-references MUID:89279233; PMID:2732700 !$#accession D31813 !'##molecule_type DNA !'##residues 1-220 ##label GER !'##cross-references GB:D00423; NID:g221120; PIDN:BAA00326.1; !1PID:g221125 CLASSIFICATION #superfamily vaccinia virus F9 protein KEYWORDS early protein SUMMARY #length 220 #checksum 2963 SEQUENCE /// ENTRY WMVZP9 #type fragment TITLE F9 protein - fowlpox virus (strain HP444) (fragment) ORGANISM #formal_name fowlpox virus DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jun-2000 ACCESSIONS PS0044 REFERENCE JS0220 !$#authors Binns, M.M.; Tomley, F.M.; Campbell, J.; Boursnell, M.E.G. !$#journal J. Gen. Virol. (1988) 69:1275-1283 !$#title Comparison of a conserved region in fowlpox virus and !1vaccinia virus genomes and the translocation of the fowlpox !1virus thymidine kinase gene. !$#cross-references MUID:88258470; PMID:2838574 !$#accession PS0044 !'##molecule_type DNA !'##residues 1-206 ##label BIN !'##cross-references GB:D00320; NID:g221401; PIDN:BAA00231.1; !1PID:g221410 CLASSIFICATION #superfamily vaccinia virus F9 protein SUMMARY #length 206 #checksum 3989 SEQUENCE /// ENTRY QQVZEL #type complete TITLE F11 protein - vaccinia virus ORGANISM #formal_name vaccinia virus DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 28-May-1999 ACCESSIONS B26216; L23092 REFERENCE A23092 !$#authors Plucienniczak, A.; Schroeder, E.; Zettlmeissl, G.; Streeck, !1R.E. !$#journal Nucleic Acids Res. (1985) 13:985-998 !$#title Nucleotide sequence of a cluster of early and late genes in !1a conserved segment of the vaccinia virus genome. !$#cross-references MUID:85215527; PMID:2987815 !$#accession B26216 !'##molecule_type DNA !'##residues 1-124 ##label PLU !'##cross-references GB:X01978; GB:J02424; GB:J02425; GB:K02376; !1GB:M15211; GB:V01537; NID:g61387; PIDN:CAA26019.1; !1PID:g61398 !'##experimental_source strain WR COMMENT It is unknown whether this protein is synthesized before or !1after viral DNA replication. CLASSIFICATION #superfamily vaccinia virus F11 protein SUMMARY #length 124 #molecular-weight 14240 #checksum 7870 SEQUENCE /// ENTRY QQVZ1 #type complete TITLE mRNA capping enzyme large chain - vaccinia virus ALTERNATE_NAMES D1R protein; hypothetical protein A-844 CONTAINS mRNA (guanine-N7-)-methyltransferase (EC 2.1.1.56); mRNA guanylyltransferase (EC 2.7.7.50) ORGANISM #formal_name vaccinia virus #note host Homo sapiens (man) DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 16-Jul-1999 ACCESSIONS A03872; A35784; A53795 REFERENCE A01146 !$#authors Niles, E.G.; Condit, R.C.; Caro, P.; Davidson, K.; Matusick, !1L.; Seto, J. !$#journal Virology (1986) 153:96-112 !$#title Nucleotide sequence and genetic map of the 16-kb vaccinia !1virus HindIII D fragment. !$#cross-references MUID:86291159; PMID:3739227 !$#accession A03872 !'##molecule_type DNA !'##residues 1-844 ##label NIL !'##cross-references GB:M15058; NID:g335640; PIDN:AAA48253.1; !1PID:g335641 !'##experimental_source strain WR REFERENCE A35784 !$#authors Guo, P.; Moss, B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:4023-4027 !$#title Interaction and mutual stabilization of the two subunits of !1vaccinia virus mRNA capping enzyme coexpressed in !1Escherichia coli. !$#cross-references MUID:90272646; PMID:2161527 !$#accession A35784 !'##molecule_type protein !'##residues 1,'X',3-8,'X',10-15,'X',17-20;498-517 ##label GUO REFERENCE A53795 !$#authors Higman, M.A.; Niles, E.G. !$#journal J. Biol. Chem. (1994) 269:14982-14987 !$#title Location of the S-adenosyl-L-methionine binding region of !1the vaccinia virus mRNA (guanine-7-)methyltransferase. !$#cross-references MUID:94253053; PMID:8195133 !$#accession A53795 !'##molecule_type protein !'##residues 498-507;762-767;806-811 ##label HIG COMPLEX heterodimer with mRNA capping enzyme small chain (see !1PIR:QQVZ22) FUNCTION MTF !$#description as mRNA (guanine-N7-)-methyltransferase catalyzes the !1formation of N7-methylguanine triphosphate 5'-capped mRNA !1from S-adenosyl-L-methionine and guanine triphosphate !15'-capped mRNA FUNCTION GTF !$#description as mRNA guanylyltransferase catalyzes the formation of !1guanine triphosphate 5'-capped mRNA and pyrophosphate from !1GTP and mRNA 5'-diphosphate CLASSIFICATION #superfamily poxvirus mRNA capping enzyme large chain KEYWORDS heterodimer; methyltransferase; mRNA capping; !1nucleotidyltransferase; phosphoprotein; S-adenosylmethionine FEATURE !$499-579,806-844 #region S-adenosylmethionine binding #status !8predicted\ !$260 #active_site Lys (covalent GMP-binding) #status !8predicted SUMMARY #length 844 #molecular-weight 96733 #checksum 8206 SEQUENCE /// ENTRY QQVZVC #type complete TITLE mRNA capping enzyme large chain - vaccinia virus (strain Copenhagen) ALTERNATE_NAMES D1R protein CONTAINS mRNA (guanine-N7-)-methyltransferase (EC 2.1.1.56); mRNA guanylyltransferase (EC 2.7.7.50) ORGANISM #formal_name vaccinia virus #note host Homo sapiens (man) DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jul-1999 ACCESSIONS I42514 REFERENCE A42501 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:517-563 !$#title Appendix to "The complete DNA sequence of vaccinia virus". !$#accession I42514 !'##molecule_type DNA !'##residues 1-844 ##label GOE !'##cross-references GB:M35027; NID:g335317; PIDN:AAA48095.1; !1PID:g335443 REFERENCE A42531 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:247-266 !$#title The complete DNA sequence of vaccinia virus. !$#cross-references MUID:91021027; PMID:2219722 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given COMPLEX heterodimer with mRNA capping enzyme small chain (see !1PIR:QQVZ22) FUNCTION MTF !$#description as mRNA (guanine-N7-)-methyltransferase catalyzes the !1formation of N7-methylguanine triphosphate 5'-capped mRNA !1from S-adenosyl-L-methionine and guanine triphosphate !15'-capped mRNA FUNCTION GTF !$#description as mRNA guanylyltransferase catalyzes the formation of !1guanine triphosphate 5'-capped mRNA and pyrophosphate from !1GTP and mRNA 5'-diphosphate CLASSIFICATION #superfamily poxvirus mRNA capping enzyme large chain KEYWORDS heterodimer; methyltransferase; mRNA capping; !1nucleotidyltransferase; phosphoprotein; S-adenosylmethionine FEATURE !$499-579,806-844 #region S-adenosylmethionine binding #status !8predicted\ !$260 #active_site Lys (covalent GMP-binding) #status !8predicted SUMMARY #length 844 #molecular-weight 96732 #checksum 7829 SEQUENCE /// ENTRY QQVZRA #type complete TITLE mRNA guanylyltransferase (EC 2.7.7.50) large chain - rabbit fibroma virus ALTERNATE_NAMES D3R protein; mRNA capping enzyme large chain ORGANISM #formal_name rabbit fibroma virus, Shope fibroma virus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jul-1999 ACCESSIONS A40478 REFERENCE A40478 !$#authors Upton, C.; Stuart, D.; McFadden, G. !$#journal Virology (1991) 183:773-777 !$#title Identification and DNA sequence of the large subunit of the !1capping enzyme from Shope fibroma virus. !$#cross-references MUID:91306463; PMID:1649507 !$#accession A40478 !'##molecule_type DNA !'##residues 1-836 ##label UPT !'##cross-references GB:M63902; NID:g333605; PIDN:AAA47224.1; !1PID:g333606 CLASSIFICATION #superfamily poxvirus mRNA capping enzyme large chain KEYWORDS mRNA capping; nucleotidyltransferase; phosphoprotein FEATURE !$256 #active_site Lys (covalent GMP-binding) #status !8predicted SUMMARY #length 836 #molecular-weight 97018 #checksum 5351 SEQUENCE /// ENTRY A45391 #type complete TITLE mRNA guanylyltransferase (EC 2.7.7.50) large chain - African swine fever virus (strain BA71V) ALTERNATE_NAMES mRNA capping enzyme large chain ORGANISM #formal_name African swine fever virus, ASFV DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS A45391 REFERENCE A45391 !$#authors Pena, L.; Yanez, R.J.; Revilla, Y.; Vinuela, E.; Salas, M.L. !$#journal Virology (1993) 193:319-328 !$#title African swine fever virus guanylyltransferase. !$#cross-references MUID:93174941; PMID:8382399 !$#accession A45391 !'##molecule_type DNA !'##residues 1-868 ##label PEN !'##cross-references GB:L07263; NID:g210615; PIDN:AAA42692.1; !1PID:g210616 CLASSIFICATION #superfamily poxvirus mRNA capping enzyme large chain KEYWORDS mRNA capping; nucleotidyltransferase; phosphoprotein FEATURE !$282 #active_site Lys (covalent GMP-binding) #status !8predicted SUMMARY #length 868 #molecular-weight 99968 #checksum 337 SEQUENCE /// ENTRY QQVZ2 #type complete TITLE hypothetical 9.2K protein - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 16-Jul-1999 ACCESSIONS A03873 REFERENCE A01146 !$#authors Niles, E.G.; Condit, R.C.; Caro, P.; Davidson, K.; Matusick, !1L.; Seto, J. !$#journal Virology (1986) 153:96-112 !$#title Nucleotide sequence and genetic map of the 16-kb vaccinia !1virus HindIII D fragment. !$#cross-references MUID:86291159; PMID:3739227 !$#accession A03873 !'##molecule_type DNA !'##residues 1-84 ##label NIL !'##cross-references GB:M15058; NID:g335640; PIDN:AAA48254.1; !1PID:g335642 CLASSIFICATION #superfamily vaccinia virus hypothetical 9.2K protein SUMMARY #length 84 #molecular-weight 9153 #checksum 7727 SEQUENCE /// ENTRY D42516 #type complete TITLE hypothetical 9.2K protein - vaccinia virus (strain Copenhagen) ALTERNATE_NAMES D-ORF-A protein ORGANISM #formal_name vaccinia virus #note host Homo sapiens (man) DATE 17-Jul-1998 #sequence_revision 17-Jul-1998 #text_change 16-Jul-1999 ACCESSIONS D42516 REFERENCE A33172 !$#authors Johnson, G.P. !$#submission submitted to GenBank, June 1990 !$#accession D42516 !'##molecule_type DNA !'##residues 1-84 ##label JOH !'##cross-references GB:M35027; NID:g335317; PIDN:AAA48096.1; !1PID:g335444 CLASSIFICATION #superfamily vaccinia virus hypothetical 9.2K protein SUMMARY #length 84 #molecular-weight 9187 #checksum 7661 SEQUENCE /// ENTRY QQVZA5 #type complete TITLE A5L protein - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus #note host Homo sapiens (man) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 08-Apr-1994 ACCESSIONS A41806 REFERENCE A41806 !$#authors Ahn, B.Y.; Rosel, J.; Cole, N.B.; Moss, B. !$#journal J. Virol. (1992) 66:971-982 !$#title Identification and expression of rpo19, a vaccinia virus !1gene encoding a 19-kilodalton DNA-dependent RNA polymerase !1subunit. !$#cross-references MUID:92114202; PMID:1731116 !$#accession A41806 !'##molecule_type DNA !'##residues 1-281 ##label AHN !'##cross-references GB:M76473 CLASSIFICATION #superfamily vaccinia virus A5L protein SUMMARY #length 281 #molecular-weight 30927 #checksum 5161 SEQUENCE /// ENTRY QQVZA7 #type complete TITLE A7L protein - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus #note host Homo sapiens (man) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 08-Apr-1994 ACCESSIONS C41806 REFERENCE A41806 !$#authors Ahn, B.Y.; Rosel, J.; Cole, N.B.; Moss, B. !$#journal J. Virol. (1992) 66:971-982 !$#title Identification and expression of rpo19, a vaccinia virus !1gene encoding a 19-kilodalton DNA-dependent RNA polymerase !1subunit. !$#cross-references MUID:92114202; PMID:1731116 !$#accession C41806 !'##molecule_type DNA !'##residues 1-371 ##label AHN !'##cross-references GB:M76473 CLASSIFICATION #superfamily vaccinia virus A7L protein SUMMARY #length 371 #molecular-weight 43006 #checksum 7884 SEQUENCE /// ENTRY QQVZ3 #type complete TITLE D2L protein - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus #note host Homo sapiens (man) DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 16-Jul-1999 ACCESSIONS A03874 REFERENCE A01146 !$#authors Niles, E.G.; Condit, R.C.; Caro, P.; Davidson, K.; Matusick, !1L.; Seto, J. !$#journal Virology (1986) 153:96-112 !$#title Nucleotide sequence and genetic map of the 16-kb vaccinia !1virus HindIII D fragment. !$#cross-references MUID:86291159; PMID:3739227 !$#accession A03874 !'##molecule_type DNA !'##residues 1-146 ##label NIL !'##cross-references GB:M15058; NID:g335640; PIDN:AAA48255.1; !1PID:g335643 CLASSIFICATION #superfamily vaccinia virus D2L protein SUMMARY #length 146 #molecular-weight 16946 #checksum 3641 SEQUENCE /// ENTRY QQVZCH #type complete TITLE D2L 16.9K protein - vaccinia virus (strain Ankara and Copenhagen) ORGANISM #formal_name vaccinia virus #note host Homo sapiens (man) DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 18-Feb-2000 ACCESSIONS A42515; T37375 REFERENCE A42501 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:517-563 !$#title Appendix to "The complete DNA sequence of vaccinia virus". !$#accession A42515 !'##molecule_type DNA !'##residues 1-146 ##label GOE !'##cross-references GB:M35027; NID:g335317; PIDN:AAA48097.1; !1PID:g335445 REFERENCE A42531 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:247-266 !$#title The complete DNA sequence of vaccinia virus. !$#cross-references MUID:91021027; PMID:2219722 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given REFERENCE Z20877 !$#authors Antoine, G.; Scheiflinger, F.; Falkner, F.G.; Dorner, F. !$#submission submitted to the EMBL Data Library, March 1997 !$#description The complete genomic sequence of the Modified Vaccinia !1Ankara (MVA) strain. !$#accession T37375 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-146 ##label ANT !'##cross-references EMBL:U94848; PIDN:AAB96449.1 !'##experimental_source strain Ankara GENETICS !$#note MVA099L CLASSIFICATION #superfamily vaccinia virus D2L protein SUMMARY #length 146 #molecular-weight 16904 #checksum 3398 SEQUENCE /// ENTRY QQVZRB #type complete TITLE D4L protein - rabbit fibroma virus ORGANISM #formal_name rabbit fibroma virus, Shope fibroma virus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jul-1999 ACCESSIONS B40478 REFERENCE A40478 !$#authors Upton, C.; Stuart, D.; McFadden, G. !$#journal Virology (1991) 183:773-777 !$#title Identification and DNA sequence of the large subunit of the !1capping enzyme from Shope fibroma virus. !$#cross-references MUID:91306463; PMID:1649507 !$#accession B40478 !'##molecule_type DNA !'##residues 1-143 ##label UPT !'##cross-references GB:M63902; NID:g333605; PIDN:AAA47225.1; !1PID:g454842 CLASSIFICATION #superfamily vaccinia virus D2L protein SUMMARY #length 143 #molecular-weight 16573 #checksum 8419 SEQUENCE /// ENTRY QQVZW1 #type complete TITLE G2R IBT-dependent protein - vaccinia virus ORGANISM #formal_name vaccinia virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Feb-2000 ACCESSIONS A39986; G42511; T37348 REFERENCE A39986 !$#authors Meis, R.J.; Condit, R.C. !$#journal Virology (1991) 182:442-454 !$#title Genetic and molecular biological characterization of a !1vaccinia virus gene which renders the virus dependent on !1isatin-beta-thiosemicarbazone (IBT). !$#cross-references MUID:91220694; PMID:2024483 !$#accession A39986 !'##molecule_type DNA !'##residues 1-220 ##label MEI !'##cross-references GB:J03399; GB:M59847; NID:g335662; PIDN:AAB59813.1; !1PID:g335673 !'##experimental_source strain WR REFERENCE A33172 !$#authors Johnson, G.P. !$#submission submitted to GenBank, June 1990 !$#accession G42511 !'##molecule_type DNA !'##residues 1-220 ##label JOH !'##experimental_source strain Copenhagen REFERENCE Z20877 !$#authors Antoine, G.; Scheiflinger, F.; Falkner, F.G.; Dorner, F. !$#submission submitted to the EMBL Data Library, March 1997 !$#description The complete genomic sequence of the Modified Vaccinia !1Ankara (MVA) strain. !$#accession T37348 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-220 ##label ANT !'##cross-references EMBL:U94848; PIDN:AAB96492.1 !'##experimental_source strain Ankara GENETICS !$#note MVA072R CLASSIFICATION #superfamily vaccinia virus G2R protein KEYWORDS early protein SUMMARY #length 220 #molecular-weight 25743 #checksum 9280 SEQUENCE /// ENTRY QQVZ4 #type complete TITLE hypothetical 8.5K protein - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 16-Jul-1999 ACCESSIONS A03875 REFERENCE A01146 !$#authors Niles, E.G.; Condit, R.C.; Caro, P.; Davidson, K.; Matusick, !1L.; Seto, J. !$#journal Virology (1986) 153:96-112 !$#title Nucleotide sequence and genetic map of the 16-kb vaccinia !1virus HindIII D fragment. !$#cross-references MUID:86291159; PMID:3739227 !$#accession A03875 !'##molecule_type DNA !'##residues 1-80 ##label NIL !'##cross-references GB:M15058; NID:g335640; PIDN:AAA48256.1; !1PID:g335644 CLASSIFICATION #superfamily vaccinia virus hypothetical 8.5K protein SUMMARY #length 80 #molecular-weight 8531 #checksum 8899 SEQUENCE /// ENTRY E42516 #type complete TITLE hypothetical 8.5K protein - vaccinia virus (strain Copenhagen) ALTERNATE_NAMES D-ORF-B protein ORGANISM #formal_name vaccinia virus #note host Homo sapiens (man) DATE 17-Jul-1998 #sequence_revision 17-Jul-1998 #text_change 16-Jul-1999 ACCESSIONS E42516 REFERENCE A33172 !$#authors Johnson, G.P. !$#submission submitted to GenBank, June 1990 !$#accession E42516 !'##molecule_type DNA !'##residues 1-80 ##label JOH !'##cross-references GB:M35027; NID:g335317; PIDN:AAA48098.1; !1PID:g335446 CLASSIFICATION #superfamily vaccinia virus hypothetical 8.5K protein SUMMARY #length 80 #molecular-weight 8471 #checksum 9521 SEQUENCE /// ENTRY QQVZ5 #type complete TITLE D3R protein - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus #note host Homo sapiens (man) DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 16-Jul-1999 ACCESSIONS A03876 REFERENCE A01146 !$#authors Niles, E.G.; Condit, R.C.; Caro, P.; Davidson, K.; Matusick, !1L.; Seto, J. !$#journal Virology (1986) 153:96-112 !$#title Nucleotide sequence and genetic map of the 16-kb vaccinia !1virus HindIII D fragment. !$#cross-references MUID:86291159; PMID:3739227 !$#accession A03876 !'##molecule_type DNA !'##residues 1-237 ##label NIL !'##cross-references GB:M15058; NID:g335640; PIDN:AAA48257.1; !1PID:g335645 CLASSIFICATION #superfamily vaccinia virus D3R protein SUMMARY #length 237 #molecular-weight 27991 #checksum 1188 SEQUENCE /// ENTRY QQVZCG #type complete TITLE D3R protein - vaccinia virus (strain Copenhagen) ORGANISM #formal_name vaccinia virus #note host Homo sapiens (man) DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jul-1999 ACCESSIONS B42515 REFERENCE A42501 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:517-563 !$#title Appendix to "The complete DNA sequence of vaccinia virus". !$#accession B42515 !'##molecule_type DNA !'##residues 1-237 ##label GOE !'##cross-references GB:M35027; NID:g335317; PIDN:AAA48099.1; !1PID:g335447 REFERENCE A42531 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:247-266 !$#title The complete DNA sequence of vaccinia virus. !$#cross-references MUID:91021027; PMID:2219722 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given CLASSIFICATION #superfamily vaccinia virus D3R protein SUMMARY #length 237 #molecular-weight 27974 #checksum 764 SEQUENCE /// ENTRY QQVZRC #type complete TITLE D5R protein - rabbit fibroma virus ORGANISM #formal_name rabbit fibroma virus, Shope fibroma virus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jul-1999 ACCESSIONS C40478 REFERENCE A40478 !$#authors Upton, C.; Stuart, D.; McFadden, G. !$#journal Virology (1991) 183:773-777 !$#title Identification and DNA sequence of the large subunit of the !1capping enzyme from Shope fibroma virus. !$#cross-references MUID:91306463; PMID:1649507 !$#accession C40478 !'##molecule_type DNA !'##residues 1-241 ##label UPT !'##cross-references GB:M63902; NID:g333605; PIDN:AAA47226.1; !1PID:g333608 CLASSIFICATION #superfamily vaccinia virus D3R protein SUMMARY #length 241 #molecular-weight 27936 #checksum 4973 SEQUENCE /// ENTRY QQVZ7 #type complete TITLE hypothetical protein D-69 - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 10-Sep-1999 ACCESSIONS A03878 REFERENCE A01146 !$#authors Niles, E.G.; Condit, R.C.; Caro, P.; Davidson, K.; Matusick, !1L.; Seto, J. !$#journal Virology (1986) 153:96-112 !$#title Nucleotide sequence and genetic map of the 16-kb vaccinia !1virus HindIII D fragment. !$#cross-references MUID:86291159; PMID:3739227 !$#accession A03878 !'##molecule_type DNA !'##residues 1-69 ##label NIL !'##cross-references GB:M15058 CLASSIFICATION #superfamily vaccinia virus D-ORF-C protein SUMMARY #length 69 #molecular-weight 7321 #checksum 3478 SEQUENCE /// ENTRY QQVZ9 #type complete TITLE hypothetical protein D-72 - vaccinia virus ALTERNATE_NAMES D-ORF-D protein ORGANISM #formal_name vaccinia virus DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 10-Sep-1999 ACCESSIONS A03880; G42516 REFERENCE A01146 !$#authors Niles, E.G.; Condit, R.C.; Caro, P.; Davidson, K.; Matusick, !1L.; Seto, J. !$#journal Virology (1986) 153:96-112 !$#title Nucleotide sequence and genetic map of the 16-kb vaccinia !1virus HindIII D fragment. !$#cross-references MUID:86291159; PMID:3739227 !$#accession A03880 !'##molecule_type DNA !'##residues 1-72 ##label NIL !'##cross-references GB:M15058; NID:g335640; PIDN:AAA48260.1; !1PID:g335648 !'##experimental_source strain WR REFERENCE A33172 !$#authors Johnson, G.P. !$#submission submitted to GenBank, June 1990 !$#accession G42516 !'##molecule_type DNA !'##residues 1-72 ##label JOH !'##experimental_source strain Copenhagen CLASSIFICATION #superfamily vaccinia virus hypothetical D-ORF-D protein SUMMARY #length 72 #molecular-weight 7877 #checksum 3986 SEQUENCE /// ENTRY QQVZ10 #type complete TITLE hypothetical protein D-80 - vaccinia virus ALTERNATE_NAMES D-ORF-E protein ORGANISM #formal_name vaccinia virus DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 10-Sep-1999 ACCESSIONS A03881; H42516 REFERENCE A01146 !$#authors Niles, E.G.; Condit, R.C.; Caro, P.; Davidson, K.; Matusick, !1L.; Seto, J. !$#journal Virology (1986) 153:96-112 !$#title Nucleotide sequence and genetic map of the 16-kb vaccinia !1virus HindIII D fragment. !$#cross-references MUID:86291159; PMID:3739227 !$#accession A03881 !'##molecule_type DNA !'##residues 1-80 ##label NIL !'##cross-references GB:M15058; NID:g335640; PIDN:AAA48261.1; !1PID:g335649 !'##experimental_source strain WR REFERENCE A33172 !$#authors Johnson, G.P. !$#submission submitted to GenBank, June 1990 !$#accession H42516 !'##molecule_type DNA !'##residues 1-80 ##label JOH !'##experimental_source strain Copenhagen CLASSIFICATION #superfamily vaccinia virus hypothetical D-ORF-E protein SUMMARY #length 80 #molecular-weight 9319 #checksum 756 SEQUENCE /// ENTRY QQVZ12 #type complete TITLE hypothetical protein F-63 - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 10-Sep-1999 ACCESSIONS A03883 REFERENCE A01146 !$#authors Niles, E.G.; Condit, R.C.; Caro, P.; Davidson, K.; Matusick, !1L.; Seto, J. !$#journal Virology (1986) 153:96-112 !$#title Nucleotide sequence and genetic map of the 16-kb vaccinia !1virus HindIII D fragment. !$#cross-references MUID:86291159; PMID:3739227 !$#accession A03883 !'##molecule_type DNA !'##residues 1-63 ##label NIL !'##cross-references GB:M15058 CLASSIFICATION #superfamily vaccinia virus hypothetical 7.4K protein SUMMARY #length 63 #molecular-weight 7437 #checksum 191 SEQUENCE /// ENTRY QQVZ13 #type complete TITLE RNA polymerase subunit rpo18 - vaccinia virus (strain Ankara and WR) ORGANISM #formal_name vaccinia virus DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 18-Feb-2000 ACCESSIONS A03884; T37380 REFERENCE A01146 !$#authors Niles, E.G.; Condit, R.C.; Caro, P.; Davidson, K.; Matusick, !1L.; Seto, J. !$#journal Virology (1986) 153:96-112 !$#title Nucleotide sequence and genetic map of the 16-kb vaccinia !1virus HindIII D fragment. !$#cross-references MUID:86291159; PMID:3739227 !$#accession A03884 !'##molecule_type DNA !'##residues 1-161 ##label NIL !'##cross-references GB:M15058; NID:g335640; PIDN:AAA48263.1; !1PID:g335651 REFERENCE Z20877 !$#authors Antoine, G.; Scheiflinger, F.; Falkner, F.G.; Dorner, F. !$#submission submitted to the EMBL Data Library, March 1997 !$#description The complete genomic sequence of the Modified Vaccinia !1Ankara (MVA) strain. !$#accession T37380 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-161 ##label ANT !'##cross-references EMBL:U94848; PIDN:AAB96516.1 !'##experimental_source strain Ankara GENETICS !$#note MVA104R CLASSIFICATION #superfamily variola virus DNA-directed RNA polymerase chain !1D7R SUMMARY #length 161 #molecular-weight 17911 #checksum 7860 SEQUENCE /// ENTRY QQVZ15 #type complete TITLE D9R protein - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 16-Jul-1999 ACCESSIONS A03885 REFERENCE A01146 !$#authors Niles, E.G.; Condit, R.C.; Caro, P.; Davidson, K.; Matusick, !1L.; Seto, J. !$#journal Virology (1986) 153:96-112 !$#title Nucleotide sequence and genetic map of the 16-kb vaccinia !1virus HindIII D fragment. !$#cross-references MUID:86291159; PMID:3739227 !$#accession A03885 !'##molecule_type DNA !'##residues 1-213 ##label NIL !'##cross-references GB:M15058; NID:g335640; PIDN:AAA48265.1; !1PID:g335653 CLASSIFICATION #superfamily vaccinia virus D9R protein; mutT domain !1homology FEATURE !$106-140 #domain mutT domain homology #label MUTT SUMMARY #length 213 #molecular-weight 24994 #checksum 5415 SEQUENCE /// ENTRY F36847 #type complete TITLE F9R protein - variola virus (strain India-1967) ALTERNATE_NAMES D9R protein ORGANISM #formal_name variola virus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 23-Mar-2001 ACCESSIONS F36847; S33113 REFERENCE A36859 !$#authors Blinov, V.M. !$#submission submitted to GenBank, November 1992 !$#accession F36847 !'##status preliminary !'##molecule_type DNA !'##residues 1-213 ##label BLI !'##cross-references GB:X69198; NID:g456758; PIDN:CAA49040.1; !1PID:g297279 REFERENCE S33069 !$#authors Shchelkunov, S.N.; Blinov, V.M.; Totmenin, A.V.; !1Marennikova, S.S.; Kolykhalov, A.A.; Frolov, I.V.; !1Chizhikov, V.E.; Gytorov, V.V.; Gashikov, P.V.; Belanov, !1E.F.; Belavin, P.A.; Resenchuk, S.M.; Andzhaparidze, O.G.; !1Sandakhchiev, L.S. !$#journal Virus Res. (1993) 27:25-35 !$#title Nucleotide sequence analysis of variola virus HindIII M, L, !1I genome fragments. !$#cross-references MUID:93190624; PMID:8383392 !$#accession S33113 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-213 ##label SHC !'##cross-references EMBL:X67119; NID:g62330; PIDN:CAA47598.1; !1PID:g62375 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1992 CLASSIFICATION #superfamily vaccinia virus D9R protein; mutT domain !1homology FEATURE !$106-140 #domain mutT domain homology #label MUTT SUMMARY #length 213 #molecular-weight 24982 #checksum 6279 SEQUENCE /// ENTRY B36819 #type complete TITLE C10 protein - rabbit fibroma virus ORGANISM #formal_name rabbit fibroma virus, Shope fibroma virus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B36819 REFERENCE A41700 !$#authors Strayer, D.S.; Jerng, H.H.; O'Connor, K. !$#journal Virology (1991) 185:585-595 !$#title Sequence and analysis of a portion of the genomes of Shope !1fibroma virus and malignant rabbit fibroma virus that is !1important for viral replication in lymphocytes. !$#cross-references MUID:92074222; PMID:1660196 !$#accession B36819 !'##status translation not shown !'##molecule_type DNA !'##residues 1-218 ##label STR !'##cross-references GB:M32743 CLASSIFICATION #superfamily vaccinia virus D9R protein; mutT domain !1homology FEATURE !$111-145 #domain mutT domain homology #label MUTT SUMMARY #length 218 #molecular-weight 25211 #checksum 9710 SEQUENCE /// ENTRY QQVZ16 #type complete TITLE hypothetical protein A-248 - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 16-Jul-1999 ACCESSIONS A03886 REFERENCE A01146 !$#authors Niles, E.G.; Condit, R.C.; Caro, P.; Davidson, K.; Matusick, !1L.; Seto, J. !$#journal Virology (1986) 153:96-112 !$#title Nucleotide sequence and genetic map of the 16-kb vaccinia !1virus HindIII D fragment. !$#cross-references MUID:86291159; PMID:3739227 !$#accession A03886 !'##molecule_type DNA !'##residues 1-248 ##label NIL !'##cross-references GB:M15058; NID:g335640; PIDN:AAA48266.1; !1PID:g335654 CLASSIFICATION #superfamily vaccinia virus D10R protein; mutT domain !1homology FEATURE !$121-155 #domain mutT domain homology #label MUTT SUMMARY #length 248 #molecular-weight 28913 #checksum 7854 SEQUENCE /// ENTRY QQVZ18 #type complete TITLE hypothetical protein B-69 - vaccinia virus ALTERNATE_NAMES D-ORF-F protein ORGANISM #formal_name vaccinia virus DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 10-Sep-1999 ACCESSIONS A03888; I42516 REFERENCE A01146 !$#authors Niles, E.G.; Condit, R.C.; Caro, P.; Davidson, K.; Matusick, !1L.; Seto, J. !$#journal Virology (1986) 153:96-112 !$#title Nucleotide sequence and genetic map of the 16-kb vaccinia !1virus HindIII D fragment. !$#cross-references MUID:86291159; PMID:3739227 !$#accession A03888 !'##molecule_type DNA !'##residues 1-69 ##label NIL !'##cross-references GB:M15058; NID:g335640; PIDN:AAA48268.1; !1PID:g335656 !'##experimental_source strain WR REFERENCE A33172 !$#authors Johnson, G.P. !$#submission submitted to GenBank, June 1990 !$#accession I42516 !'##molecule_type DNA !'##residues 1-69 ##label JOH !'##experimental_source strain Copenhagen CLASSIFICATION #superfamily vaccinia virus hypothetical D-ORF-F protein SUMMARY #length 69 #molecular-weight 7773 #checksum 2311 SEQUENCE /// ENTRY QQVZ19 #type complete TITLE hypothetical protein B-90 - vaccinia virus ALTERNATE_NAMES D-ORF-G protein ORGANISM #formal_name vaccinia virus DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 10-Sep-1999 ACCESSIONS A03889; A42517 REFERENCE A01146 !$#authors Niles, E.G.; Condit, R.C.; Caro, P.; Davidson, K.; Matusick, !1L.; Seto, J. !$#journal Virology (1986) 153:96-112 !$#title Nucleotide sequence and genetic map of the 16-kb vaccinia !1virus HindIII D fragment. !$#cross-references MUID:86291159; PMID:3739227 !$#accession A03889 !'##molecule_type DNA !'##residues 1-90 ##label NIL !'##cross-references GB:M15058 !'##experimental_source strain WR REFERENCE A33172 !$#authors Johnson, G.P. !$#submission submitted to GenBank, June 1990 !$#accession A42517 !'##molecule_type DNA !'##residues 1-90 ##label JOH !'##experimental_source strain Copenhagen CLASSIFICATION #superfamily vaccinia virus hypothetical D-ORF-G protein SUMMARY #length 90 #molecular-weight 10387 #checksum 9772 SEQUENCE /// ENTRY QQVZ20 #type complete TITLE hypothetical protein A-61 - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 10-Sep-1999 ACCESSIONS A03890 REFERENCE A01146 !$#authors Niles, E.G.; Condit, R.C.; Caro, P.; Davidson, K.; Matusick, !1L.; Seto, J. !$#journal Virology (1986) 153:96-112 !$#title Nucleotide sequence and genetic map of the 16-kb vaccinia !1virus HindIII D fragment. !$#cross-references MUID:86291159; PMID:3739227 !$#accession A03890 !'##molecule_type DNA !'##residues 1-61 ##label NIL !'##cross-references GB:M15058; NID:g335640; PIDN:AAA48269.1; !1PID:g335657 CLASSIFICATION #superfamily vaccinia virus hypothetical 7.2K protein SUMMARY #length 61 #molecular-weight 7229 #checksum 1141 SEQUENCE /// ENTRY QQVZ22 #type complete TITLE mRNA capping enzyme small chain - vaccinia virus ALTERNATE_NAMES 33K protein; hypothetical protein D-287 CONTAINS mRNA (guanine-N7-)-methyltransferase (EC 2.1.1.56); mRNA guanylyltransferase (EC 2.7.7.50) ORGANISM #formal_name vaccinia virus #note host Homo sapiens (man) DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 16-Jul-1999 ACCESSIONS A03892; A40413; E23768; B35784 REFERENCE A01146 !$#authors Niles, E.G.; Condit, R.C.; Caro, P.; Davidson, K.; Matusick, !1L.; Seto, J. !$#journal Virology (1986) 153:96-112 !$#title Nucleotide sequence and genetic map of the 16-kb vaccinia !1virus HindIII D fragment. !$#cross-references MUID:86291159; PMID:3739227 !$#accession A03892 !'##molecule_type DNA !'##residues 1-287 ##label NIL !'##cross-references GB:M15058; NID:g335640; PIDN:AAA48270.1; !1PID:g335658 !'##experimental_source strain WR REFERENCE A40413 !$#authors Carpenter, M.S.; DeLange, A.M. !$#journal J. Virol. (1991) 65:4042-4050 !$#title A temperature-sensitive lesion in the small subunit of the !1vaccinia virus-encoded mRNA capping enzyme causes a defect !1in viral telomere resolution. !$#cross-references MUID:91303652; PMID:1649315 !$#accession A40413 !'##molecule_type mRNA !'##residues 1-241 ##label CAR !'##cross-references GB:M64430 REFERENCE A93617 !$#authors Weinrich, S.L.; Hruby, D.E. !$#journal Nucleic Acids Res. (1986) 14:3003-3016 !$#title A tandemly-oriented late gene cluster within the vaccinia !1virus genome. !$#cross-references MUID:86176781; PMID:3008103 !$#accession E23768 !'##molecule_type DNA !'##residues 1-133,'N',135-287 ##label WEI !'##cross-references GB:X03729; NID:g60836; PIDN:CAA27369.1; PID:g60841 REFERENCE A35784 !$#authors Guo, P.; Moss, B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:4023-4027 !$#title Interaction and mutual stabilization of the two subunits of !1vaccinia virus mRNA capping enzyme coexpressed in !1Escherichia coli. !$#cross-references MUID:90272646; PMID:2161527 !$#accession B35784 !'##molecule_type protein !'##residues 1-20 ##label GUO COMPLEX heterodimer with mRNA-capping enzyme large chain (see !1PIR:QQVZ1) FUNCTION MTF !$#description as mRNA (guanine-N7-)-methyltransferase catalyzes the !1formation of N7-methylguanine triphosphate 5'-capped mRNA !1from S-adenosyl-L-methionine and guanine triphosphate !15'-capped mRNA FUNCTION GTF !$#description as mRNA guanylyltransferase catalyzes the formation of !1guanine triphosphate 5'-capped mRNA and pyrophosphate from !1GTP and mRNA 5'-diphosphate CLASSIFICATION #superfamily vaccinia virus mRNA capping enzyme small chain KEYWORDS heterodimer; methyltransferase; mRNA capping; !1nucleotidyltransferase; S-adenosylmethionine SUMMARY #length 287 #molecular-weight 33351 #checksum 9927 SEQUENCE /// ENTRY QQVZ23 #type complete TITLE hypothetical protein B-62 - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 10-Sep-1999 ACCESSIONS A03893 REFERENCE A01146 !$#authors Niles, E.G.; Condit, R.C.; Caro, P.; Davidson, K.; Matusick, !1L.; Seto, J. !$#journal Virology (1986) 153:96-112 !$#title Nucleotide sequence and genetic map of the 16-kb vaccinia !1virus HindIII D fragment. !$#cross-references MUID:86291159; PMID:3739227 !$#accession A03893 !'##molecule_type DNA !'##residues 1-62 ##label NIL !'##cross-references GB:M15058; NID:g335640; PIDN:AAA48271.1; !1PID:g335659 CLASSIFICATION #superfamily vaccinia virus hypothetical 7K protein SUMMARY #length 62 #molecular-weight 7019 #checksum 1045 SEQUENCE /// ENTRY QQVZ24 #type complete TITLE hypothetical protein A-72 - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 10-Sep-1999 ACCESSIONS A03894 REFERENCE A01146 !$#authors Niles, E.G.; Condit, R.C.; Caro, P.; Davidson, K.; Matusick, !1L.; Seto, J. !$#journal Virology (1986) 153:96-112 !$#title Nucleotide sequence and genetic map of the 16-kb vaccinia !1virus HindIII D fragment. !$#cross-references MUID:86291159; PMID:3739227 !$#accession A03894 !'##molecule_type DNA !'##residues 1-72 ##label NIL !'##cross-references GB:M15058; NID:g335640; PIDN:AAA48272.1; !1PID:g335660 CLASSIFICATION #superfamily vaccinia virus hypothetical 8.7K protein SUMMARY #length 72 #molecular-weight 8657 #checksum 9881 SEQUENCE /// ENTRY QQVZ25 #type complete TITLE rifampicin resistance - vaccinia virus (strain Ankara) ALTERNATE_NAMES D13L protein ORGANISM #formal_name vaccinia virus #note host Homo sapiens (man) DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 18-Feb-2000 ACCESSIONS C01146; A94353; C42516; D23768; T37386; A03895; B26351 REFERENCE A01146 !$#authors Niles, E.G.; Condit, R.C.; Caro, P.; Davidson, K.; Matusick, !1L.; Seto, J. !$#journal Virology (1986) 153:96-112 !$#title Nucleotide sequence and genetic map of the 16-kb vaccinia !1virus HindIII D fragment. !$#cross-references MUID:86291159; PMID:3739227 !$#accession C01146 !'##molecule_type DNA !'##residues 1-551 ##label NIL !'##cross-references GB:M15058; NID:g335640; PIDN:AAA48273.1; !1PID:g335661 !'##experimental_source strain WR REFERENCE A94353 !$#authors Baldick Jr., C.J.; Moss, B. !$#journal Virology (1987) 156:138-145 !$#title Resistance of vaccinia virus to rifampicin conferred by a !1single nucleotide substitution near the predicted NH2 !1terminus of a gene encoding an Mr 62,000 polypeptide. !$#cross-references MUID:87122144; PMID:3811229 !$#accession A94353 !'##molecule_type DNA !'##residues 1-551 ##label BAL !'##cross-references GB:M16556; NID:g335729; PIDN:AAA48305.1; !1PID:g335731 !'##experimental_source strain WR REFERENCE A33172 !$#authors Johnson, G.P. !$#submission submitted to GenBank, June 1990 !$#accession C42516 !'##molecule_type DNA !'##residues 1-551 ##label JOH !'##experimental_source strain Copenhagen REFERENCE A93617 !$#authors Weinrich, S.L.; Hruby, D.E. !$#journal Nucleic Acids Res. (1986) 14:3003-3016 !$#title A tandemly-oriented late gene cluster within the vaccinia !1virus genome. !$#cross-references MUID:86176781; PMID:3008103 !$#accession D23768 !'##molecule_type DNA !'##residues 1-551 ##label WEI !'##cross-references GB:X03729; NID:g60836; PIDN:CAA27368.1; PID:g60840 REFERENCE Z20877 !$#authors Antoine, G.; Scheiflinger, F.; Falkner, F.G.; Dorner, F. !$#submission submitted to the EMBL Data Library, March 1997 !$#description The complete genomic sequence of the Modified Vaccinia !1Ankara (MVA) strain. !$#accession T37386 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-551 ##label ANT !'##cross-references EMBL:U94848; PIDN:AAB96453.1 !'##experimental_source strain Ankara GENETICS !$#note MVA110L CLASSIFICATION #superfamily variola virus N3L protein KEYWORDS antibiotic resistance SUMMARY #length 551 #molecular-weight 61890 #checksum 6935 SEQUENCE /// ENTRY QQVZ6 #type complete TITLE D4 protein - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus DATE 04-Dec-1986 #sequence_revision 31-Mar-1989 #text_change 16-Jul-1999 ACCESSIONS A93025; D01146; A03877; A29534 REFERENCE A93025 !$#authors Roseman, N.A.; Hruby, D.E. !$#journal J. Virol. (1987) 61:1398-1406 !$#title Nucleotide sequence and transcript organization of a region !1of the vaccinia virus genome which encodes a constitutively !1expressed gene required for DNA replication. !$#cross-references MUID:87198863; PMID:3033268 !$#accession A93025 !'##molecule_type DNA !'##residues 1-218 ##label ROS !'##cross-references GB:M16021; NID:g335828; PIDN:AAA69628.1; !1PID:g893339 REFERENCE A01146 !$#authors Niles, E.G.; Condit, R.C.; Caro, P.; Davidson, K.; Matusick, !1L.; Seto, J. !$#journal Virology (1986) 153:96-112 !$#title Nucleotide sequence and genetic map of the 16-kb vaccinia !1virus HindIII D fragment. !$#cross-references MUID:86291159; PMID:3739227 !$#accession D01146 !'##molecule_type DNA !'##residues 1-162,'F',164-218 ##label NIL !'##cross-references GB:M15058; NID:g335640; PIDN:AAA48258.1; !1PID:g335646 GENETICS !$#gene ts17 CLASSIFICATION #superfamily vaccinia virus D4 protein KEYWORDS DNA replication SUMMARY #length 218 #molecular-weight 25068 #checksum 6154 SEQUENCE /// ENTRY QQVZ8 #type complete TITLE D5 protein - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 16-Jul-1999 ACCESSIONS B93025; E01146; B49593; A03879; B29534 REFERENCE A93025 !$#authors Roseman, N.A.; Hruby, D.E. !$#journal J. Virol. (1987) 61:1398-1406 !$#title Nucleotide sequence and transcript organization of a region !1of the vaccinia virus genome which encodes a constitutively !1expressed gene required for DNA replication. !$#cross-references MUID:87198863; PMID:3033268 !$#accession B93025 !'##molecule_type DNA !'##residues 1-785 ##label ROS !'##cross-references GB:M16021; NID:g335828; PIDN:AAA69629.1; !1PID:g893340 REFERENCE A01146 !$#authors Niles, E.G.; Condit, R.C.; Caro, P.; Davidson, K.; Matusick, !1L.; Seto, J. !$#journal Virology (1986) 153:96-112 !$#title Nucleotide sequence and genetic map of the 16-kb vaccinia !1virus HindIII D fragment. !$#cross-references MUID:86291159; PMID:3739227 !$#accession E01146 !'##molecule_type DNA !'##residues 1-785 ##label NIL !'##cross-references GB:M15058; NID:g335640; PIDN:AAA48259.1; !1PID:g335647 REFERENCE A49593 !$#authors Millns, A.K.; Carpenter, M.S.; DeLange, A.M. !$#journal Virology (1994) 198:504-513 !$#title The vaccinia virus-encoded uracil DNA glycosylase has an !1essential role in viral DNA replication. !$#cross-references MUID:94120724; PMID:8291232 !$#accession B49593 !'##status preliminary !'##molecule_type DNA !'##residues 1-75 ##label MIL !'##cross-references GB:L24385 GENETICS !$#gene ts17; D5R CLASSIFICATION #superfamily vaccinia virus D5 protein KEYWORDS DNA replication SUMMARY #length 785 #molecular-weight 90356 #checksum 7807 SEQUENCE /// ENTRY QQVZ11 #type complete TITLE early transcription factor 70K chain - vaccinia virus (strain WR) ALTERNATE_NAMES D6 protein; VETF light chain ORGANISM #formal_name vaccinia virus DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 16-Jul-1999 ACCESSIONS F01146; C93025; B35796; A03882; C29534 REFERENCE A01146 !$#authors Niles, E.G.; Condit, R.C.; Caro, P.; Davidson, K.; Matusick, !1L.; Seto, J. !$#journal Virology (1986) 153:96-112 !$#title Nucleotide sequence and genetic map of the 16-kb vaccinia !1virus HindIII D fragment. !$#cross-references MUID:86291159; PMID:3739227 !$#accession F01146 !'##molecule_type DNA !'##residues 1-637 ##label NIL !'##cross-references GB:M15058; NID:g335640; PIDN:AAA48262.1; !1PID:g335650 REFERENCE A93025 !$#authors Roseman, N.A.; Hruby, D.E. !$#journal J. Virol. (1987) 61:1398-1406 !$#title Nucleotide sequence and transcript organization of a region !1of the vaccinia virus genome which encodes a constitutively !1expressed gene required for DNA replication. !$#cross-references MUID:87198863; PMID:3033268 !$#accession C93025 !'##molecule_type DNA !'##residues 1-197 ##label ROS !'##cross-references GB:M16021; NID:g335828; PIDN:AAA69630.1; !1PID:g893341 REFERENCE A35796 !$#authors Gershon, P.D.; Moss, B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:4401-4405 !$#title Early transcription factor subunits are encoded by vaccinia !1virus late genes. !$#cross-references MUID:90272720; PMID:2190222 !$#accession B35796 !'##molecule_type protein !'##residues 220-234;459-473;580-595 ##label GER GENETICS !$#gene D6R; ts17 COMPLEX VETF is a heterodimer of 82K and 70K chains; it may be !1associated with RNA polymerase and capping enzyme in a !1transcription complex. FUNCTION !$#description RNA polymerase, VETF, and capping enzyme are the only !1required proteins for the in vitro transcription of early !1genes; VETF has an associated DNA-dependent ATPase activity CLASSIFICATION #superfamily vaccinia virus early transcription factor 70K !1chain KEYWORDS transcription regulation SUMMARY #length 637 #molecular-weight 73830 #checksum 7448 SEQUENCE /// ENTRY C43497 #type complete TITLE early transcription factor 82K chain - vaccinia virus (strain WR) ALTERNATE_NAMES A7L protein; A8L protein; VETF heavy chain ORGANISM #formal_name vaccinia virus DATE 12-Jan-1993 #sequence_revision 19-Apr-1996 #text_change 16-Jul-1999 ACCESSIONS C43497; A35796; D41806 REFERENCE A43497 !$#authors Van Meir, E.; Wittek, R. !$#journal Arch. Virol. (1988) 102:19-27 !$#title Fine structure of the vaccinia virus gene encoding the !1precursor of the major core protein 4a. !$#cross-references MUID:89061367; PMID:3196167 !$#accession C43497 !'##molecule_type DNA !'##residues 1-533,'LHLILFSC' ##label VAN !'##cross-references GB:M27634; NID:g335592; PIDN:AAA69587.1; !1PID:g530974 REFERENCE A35796 !$#authors Gershon, P.D.; Moss, B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:4401-4405 !$#title Early transcription factor subunits are encoded by vaccinia !1virus late genes. !$#cross-references MUID:90272720; PMID:2190222 !$#accession A35796 !'##molecule_type protein !'##residues 1-15 ##label GER REFERENCE A41806 !$#authors Ahn, B.Y.; Rosel, J.; Cole, N.B.; Moss, B. !$#journal J. Virol. (1992) 66:971-982 !$#title Identification and expression of rpo19, a vaccinia virus !1gene encoding a 19-kilodalton DNA-dependent RNA polymerase !1subunit. !$#cross-references MUID:92114202; PMID:1731116 !$#accession D41806 !'##molecule_type DNA !'##residues 526-710 ##label AHN !'##cross-references GB:M76473; NID:g335803; PIDN:AAA48338.1; !1PID:g335805 GENETICS !$#gene A7L; A8L COMPLEX VETF is a heterodimer of 82K and 70K chains; it may be !1associated with RNA polymerase and capping enzyme in a !1transcription complex. FUNCTION !$#description RNA polymerase, VETF, and capping enzyme are the only !1required proteins for the in vitro transcription of early !1genes; VETF has an associated DNA-dependent ATPase activity CLASSIFICATION #superfamily vaccinia virus early transcription factor 82K !1chain KEYWORDS late protein; transcription regulation SUMMARY #length 710 #molecular-weight 82272 #checksum 9208 SEQUENCE /// ENTRY I42517 #type complete TITLE early transcription factor 82K chain - vaccinia virus (strain Copenhagen) ALTERNATE_NAMES A7L protein; VETF heavy chain ORGANISM #formal_name vaccinia virus #note host Homo sapiens (man) DATE 09-Nov-1990 #sequence_revision 19-Apr-1996 #text_change 01-Aug-1997 ACCESSIONS I42517 REFERENCE A33172 !$#authors Johnson, G.P. !$#submission submitted to GenBank, June 1990 !$#accession I42517 !'##molecule_type DNA !'##residues 1-710 ##label JOH GENETICS !$#gene A7L COMPLEX VETF is a heterodimer of 82K and 70K chains; it may be !1associated with RNA polymerase and capping enzyme in a !1transcription complex. FUNCTION !$#description RNA polymerase, VETF, and capping enzyme are the only !1required proteins for the in vitro transcription of early !1genes; VETF has an associated DNA-dependent ATPase activity CLASSIFICATION #superfamily vaccinia virus early transcription factor 82K !1chain KEYWORDS late protein; transcription regulation SUMMARY #length 710 #molecular-weight 82328 #checksum 9621 SEQUENCE /// ENTRY H36848 #type complete TITLE early transcription factor 82K chain - variola virus (strain India-1967) ORGANISM #formal_name variola virus DATE 30-Sep-1993 #sequence_revision 19-Apr-1996 #text_change 23-Mar-2001 ACCESSIONS H36848; S46893 REFERENCE A36859 !$#authors Blinov, V.M. !$#submission submitted to GenBank, November 1992 !$#accession H36848 !'##molecule_type DNA !'##residues 1-710 ##label BLI !'##cross-references GB:X69198; NID:g456758; PIDN:CAA49052.1; !1PID:g297290 REFERENCE S46890 !$#authors Volchov, V.E.; Blinov, V.M.; Totmenin, A.V.; Shchelkunov, !1S.N.; Sandakhchiev, L.S. !$#submission submitted to the EMBL Data Library, April 1992 !$#description Nucleotide sequence analysis of the region of variola virus !1XhoI-G genome fragment. !$#accession S46893 !'##molecule_type DNA !'##residues 1-710 ##label VOL !'##cross-references EMBL:X67116; NID:g516451; PIDN:CAA47515.1; !1PID:g516455 COMPLEX VETF is a heterodimer of 82K and 70K chains; it may be !1associated with RNA polymerase and capping enzyme in a !1transcription complex. FUNCTION !$#description RNA polymerase, VETF, and capping enzyme are the only !1required proteins for the in vitro transcription of early !1genes; VETF has an associated DNA-dependent ATPase activity CLASSIFICATION #superfamily vaccinia virus early transcription factor 82K !1chain KEYWORDS late protein; transcription regulation SUMMARY #length 710 #molecular-weight 82477 #checksum 952 SEQUENCE /// ENTRY QQVZH2 #type complete TITLE H2 protein - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 24-Oct-1997 ACCESSIONS B24481 REFERENCE A93022 !$#authors Rosel, J.L.; Earl, P.L.; Weir, J.P.; Moss, B. !$#journal J. Virol. (1986) 60:436-449 !$#title Conserved TAAATG sequence at the transcriptional and !1translational initiation sites of vaccinia virus late genes !1deduced by structural and functional analysis of the HindIII !1H genome fragment. !$#cross-references MUID:87036903; PMID:3021979 !$#accession B24481 !'##molecule_type DNA !'##residues 1-189 ##label ROS !'##cross-references GB:M13209 CLASSIFICATION #superfamily vaccinia virus H2 protein KEYWORDS late protein SUMMARY #length 189 #molecular-weight 21501 #checksum 7319 SEQUENCE /// ENTRY QQVZH3 #type complete TITLE H3 protein - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jul-1999 ACCESSIONS C24481 REFERENCE A93022 !$#authors Rosel, J.L.; Earl, P.L.; Weir, J.P.; Moss, B. !$#journal J. Virol. (1986) 60:436-449 !$#title Conserved TAAATG sequence at the transcriptional and !1translational initiation sites of vaccinia virus late genes !1deduced by structural and functional analysis of the HindIII !1H genome fragment. !$#cross-references MUID:87036903; PMID:3021979 !$#accession C24481 !'##molecule_type DNA !'##residues 1-324 ##label ROS !'##cross-references GB:M13209; NID:g335739; PIDN:AAB59838.1; !1PID:g335743 CLASSIFICATION #superfamily vaccinia virus H3 protein KEYWORDS late protein SUMMARY #length 324 #molecular-weight 37504 #checksum 7902 SEQUENCE /// ENTRY QQVZH4 #type complete TITLE H4L protein - vaccinia virus ALTERNATE_NAMES H4 protein ORGANISM #formal_name vaccinia virus #note host Homo sapiens (man) DATE 31-Mar-1988 #sequence_revision 22-Oct-1999 #text_change 22-Oct-1999 ACCESSIONS D42514; D24481 REFERENCE A33172 !$#authors Johnson, G.P. !$#submission submitted to GenBank, June 1990 !$#accession D42514 !'##status preliminary !'##molecule_type DNA !'##residues 1-795 ##label JOH !'##experimental_source strain Copenhagen REFERENCE A93022 !$#authors Rosel, J.L.; Earl, P.L.; Weir, J.P.; Moss, B. !$#journal J. Virol. (1986) 60:436-449 !$#title Conserved TAAATG sequence at the transcriptional and !1translational initiation sites of vaccinia virus late genes !1deduced by structural and functional analysis of the HindIII !1H genome fragment. !$#cross-references MUID:87036903; PMID:3021979 !$#accession D24481 !'##molecule_type DNA !'##residues 617-718,'R',721-795 ##label ROS !'##cross-references GB:M13209; NID:g335739; PIDN:AAB59839.1; !1PID:g893337 !'##experimental_source (strain WR) CLASSIFICATION #superfamily vaccinia virus H4 protein KEYWORDS late protein SUMMARY #length 795 #molecular-weight 93558 #checksum 1713 SEQUENCE /// ENTRY QQVZH5 #type complete TITLE H5 protein - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jul-1999 ACCESSIONS E24481 REFERENCE A93022 !$#authors Rosel, J.L.; Earl, P.L.; Weir, J.P.; Moss, B. !$#journal J. Virol. (1986) 60:436-449 !$#title Conserved TAAATG sequence at the transcriptional and !1translational initiation sites of vaccinia virus late genes !1deduced by structural and functional analysis of the HindIII !1H genome fragment. !$#cross-references MUID:87036903; PMID:3021979 !$#accession E24481 !'##molecule_type DNA !'##residues 1-575 ##label ROS !'##cross-references GB:M13209; NID:g335739; PIDN:AAB59840.1; !1PID:g335744 CLASSIFICATION #superfamily vaccinia virus H5 protein KEYWORDS late protein SUMMARY #length 575 #molecular-weight 67555 #checksum 8321 SEQUENCE /// ENTRY QQVZH6 #type complete TITLE VLTF-4, late transcription factor - vaccinia virus (strain Ankara and WR) ALTERNATE_NAMES 35K antigen; Ag35 envelope protein ORGANISM #formal_name vaccinia virus DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 18-Feb-2000 ACCESSIONS F24481; A31824; T37371 REFERENCE A93022 !$#authors Rosel, J.L.; Earl, P.L.; Weir, J.P.; Moss, B. !$#journal J. Virol. (1986) 60:436-449 !$#title Conserved TAAATG sequence at the transcriptional and !1translational initiation sites of vaccinia virus late genes !1deduced by structural and functional analysis of the HindIII !1H genome fragment. !$#cross-references MUID:87036903; PMID:3021979 !$#accession F24481 !'##molecule_type DNA !'##residues 1-203 ##label ROS !'##cross-references GB:M13209; NID:g335739; PIDN:AAB59841.1; !1PID:g335745 REFERENCE A94384 !$#authors Gordon, J.; Kovala, T.; Dales, S. !$#journal Virology (1988) 167:361-369 !$#title Molecular characterization of a prominent antigen of the !1vaccinia virus envelope. !$#cross-references MUID:89073737; PMID:2462305 !$#accession A31824 !'##molecule_type DNA !'##residues 1-203 ##label GOR !'##cross-references GB:M23648; NID:g340994; PIDN:AAA47962.1; !1PID:g530972 REFERENCE Z20877 !$#authors Antoine, G.; Scheiflinger, F.; Falkner, F.G.; Dorner, F. !$#submission submitted to the EMBL Data Library, March 1997 !$#description The complete genomic sequence of the Modified Vaccinia !1Ankara (MVA) strain. !$#accession T37371 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-203 ##label ANT !'##cross-references EMBL:U94848; PIDN:AAB96508.1 !'##experimental_source strain Ankara COMMENT This protein is a component of the viral envelope. GENETICS !$#note MVA095R CLASSIFICATION #superfamily vaccinia virus H6 protein KEYWORDS envelope protein; late protein SUMMARY #length 203 #molecular-weight 22300 #checksum 7620 SEQUENCE /// ENTRY QQVZH8 #type fragment TITLE H8 protein - vaccinia virus (strain WR) (fragment) ORGANISM #formal_name vaccinia virus DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jul-1999 ACCESSIONS H24481 REFERENCE A93022 !$#authors Rosel, J.L.; Earl, P.L.; Weir, J.P.; Moss, B. !$#journal J. Virol. (1986) 60:436-449 !$#title Conserved TAAATG sequence at the transcriptional and !1translational initiation sites of vaccinia virus late genes !1deduced by structural and functional analysis of the HindIII !1H genome fragment. !$#cross-references MUID:87036903; PMID:3021979 !$#accession H24481 !'##molecule_type DNA !'##residues 1-129 ##label ROS !'##cross-references GB:M13209; NID:g335739; PIDN:AAB59843.1; !1PID:g335746 CLASSIFICATION #superfamily vaccinia virus H8 protein KEYWORDS late protein SUMMARY #length 129 #checksum 9052 SEQUENCE /// ENTRY QQVZ28 #type complete TITLE H8 protein - vaccinia virus (strain Copenhagen) ALTERNATE_NAMES H7R protein ORGANISM #formal_name vaccinia virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS G42514 REFERENCE A33172 !$#authors Johnson, G.P. !$#submission submitted to GenBank, June 1990 !$#accession G42514 !'##molecule_type DNA !'##residues 1-146 ##label JOH !'##cross-references GB:M35027; NID:g335317; PIDN:AAA48094.1; !1PID:g335442 CLASSIFICATION #superfamily vaccinia virus H8 protein KEYWORDS late protein SUMMARY #length 146 #molecular-weight 16912 #checksum 7613 SEQUENCE /// ENTRY WMVZK2 #type complete TITLE K2 protein - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jun-2000 ACCESSIONS JS0212 REFERENCE JS0211 !$#authors Boursnell, M.E.G.; Foulds, I.J.; Campbell, J.I.; Binns, M.M. !$#journal J. Gen. Virol. (1988) 69:2995-3003 !$#title Non-essential genes in the vaccinia virus HindIII K !1fragment: a gene related to serine protease inhibitors and a !1gene related to the 37K vaccinia virus major envelope !1antigen. !$#cross-references MUID:89067908; PMID:3264331 !$#accession JS0212 !'##molecule_type DNA !'##residues 1-88 ##label BOU !'##cross-references GB:D00382; NID:g222704; PIDN:BAA00288.1; !1PID:g222707 CLASSIFICATION #superfamily vaccinia virus K2 protein SUMMARY #length 88 #molecular-weight 10556 #checksum 5328 SEQUENCE /// ENTRY WMVZK4 #type complete TITLE K4 protein - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jun-2000 ACCESSIONS JS0214 REFERENCE JS0211 !$#authors Boursnell, M.E.G.; Foulds, I.J.; Campbell, J.I.; Binns, M.M. !$#journal J. Gen. Virol. (1988) 69:2995-3003 !$#title Non-essential genes in the vaccinia virus HindIII K !1fragment: a gene related to serine protease inhibitors and a !1gene related to the 37K vaccinia virus major envelope !1antigen. !$#cross-references MUID:89067908; PMID:3264331 !$#accession JS0214 !'##molecule_type DNA !'##residues 1-44 ##label BOU !'##cross-references GB:D00382; NID:g222704; PIDN:BAA00290.1; !1PID:g222709 CLASSIFICATION #superfamily vaccinia virus K4 protein SUMMARY #length 44 #molecular-weight 5350 #checksum 5485 SEQUENCE /// ENTRY WMVZK5 #type complete TITLE K5 protein - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jun-2000 ACCESSIONS JS0215 REFERENCE JS0211 !$#authors Boursnell, M.E.G.; Foulds, I.J.; Campbell, J.I.; Binns, M.M. !$#journal J. Gen. Virol. (1988) 69:2995-3003 !$#title Non-essential genes in the vaccinia virus HindIII K !1fragment: a gene related to serine protease inhibitors and a !1gene related to the 37K vaccinia virus major envelope !1antigen. !$#cross-references MUID:89067908; PMID:3264331 !$#accession JS0215 !'##molecule_type DNA !'##residues 1-134 ##label BOU !'##cross-references GB:D00382; NID:g222704; PIDN:BAA00291.1; !1PID:g222710 CLASSIFICATION #superfamily vaccinia virus K5 protein SUMMARY #length 134 #molecular-weight 15145 #checksum 8434 SEQUENCE /// ENTRY WMVZK6 #type complete TITLE K6 protein - vaccinia virus ALTERNATE_NAMES K6L protein ORGANISM #formal_name vaccinia virus DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jun-2000 ACCESSIONS JS0216; E42505 REFERENCE JS0211 !$#authors Boursnell, M.E.G.; Foulds, I.J.; Campbell, J.I.; Binns, M.M. !$#journal J. Gen. Virol. (1988) 69:2995-3003 !$#title Non-essential genes in the vaccinia virus HindIII K !1fragment: a gene related to serine protease inhibitors and a !1gene related to the 37K vaccinia virus major envelope !1antigen. !$#cross-references MUID:89067908; PMID:3264331 !$#accession JS0216 !'##molecule_type DNA !'##residues 1-81 ##label BOU !'##cross-references GB:D00382; NID:g222704; PIDN:BAA00292.1; !1PID:g222711 !'##experimental_source strain WR REFERENCE A33172 !$#authors Johnson, G.P. !$#submission submitted to GenBank, June 1990 !$#accession E42505 !'##molecule_type DNA !'##residues 1-81 ##label JOH !'##experimental_source strain Copenhagen CLASSIFICATION #superfamily vaccinia virus K6 protein SUMMARY #length 81 #molecular-weight 9097 #checksum 7477 SEQUENCE /// ENTRY WMVZK7 #type complete TITLE K7 protein 28R - vaccinia virus (strains Ankara and Copenhagen) ORGANISM #formal_name vaccinia virus #variety strain Ankara DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jun-2000 ACCESSIONS JS0217; F42505; T30778 REFERENCE JS0211 !$#authors Boursnell, M.E.G.; Foulds, I.J.; Campbell, J.I.; Binns, M.M. !$#journal J. Gen. Virol. (1988) 69:2995-3003 !$#title Non-essential genes in the vaccinia virus HindIII K !1fragment: a gene related to serine protease inhibitors and a !1gene related to the 37K vaccinia virus major envelope !1antigen. !$#cross-references MUID:89067908; PMID:3264331 !$#accession JS0217 !'##molecule_type DNA !'##residues 1-149 ##label BOU !'##cross-references GB:D00382; NID:g222704; PIDN:BAA00293.1; !1PID:g222712 !'##experimental_source strain WR REFERENCE A33172 !$#authors Johnson, G.P. !$#submission submitted to GenBank, June 1990 !$#accession F42505 !'##molecule_type DNA !'##residues 1-149 ##label JOH !'##experimental_source strain Copenhagen REFERENCE Z20877 !$#authors Antoine, G.; Scheiflinger, F.; Falkner, F.G.; Dorner, F. !$#submission submitted to the EMBL Data Library, March 1997 !$#description The complete genomic sequence of the Modified Vaccinia !1Ankara (MVA) strain. !$#accession T30778 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-149 ##label ANT !'##cross-references EMBL:U94848; PIDN:AAB96484.1 !'##experimental_source strain Ankara GENETICS !$#note MVA028R CLASSIFICATION #superfamily vaccinia virus K7 protein SUMMARY #length 149 #molecular-weight 17468 #checksum 7422 SEQUENCE /// ENTRY WMVZK8 #type complete TITLE K8 protein - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jun-2000 ACCESSIONS JS0218 REFERENCE JS0211 !$#authors Boursnell, M.E.G.; Foulds, I.J.; Campbell, J.I.; Binns, M.M. !$#journal J. Gen. Virol. (1988) 69:2995-3003 !$#title Non-essential genes in the vaccinia virus HindIII K !1fragment: a gene related to serine protease inhibitors and a !1gene related to the 37K vaccinia virus major envelope !1antigen. !$#cross-references MUID:89067908; PMID:3264331 !$#accession JS0218 !'##molecule_type DNA !'##residues 1-64 ##label BOU !'##cross-references GB:D00382; NID:g222704; PIDN:BAA00294.1; !1PID:g222713 CLASSIFICATION #superfamily vaccinia virus K8 protein SUMMARY #length 64 #molecular-weight 7472 #checksum 360 SEQUENCE /// ENTRY WZVZI2 #type complete TITLE I2 protein 8.5K - vaccinia virus (strains Copenhagen, Ankara, WR and L-IVP) ALTERNATE_NAMES I2L protein ORGANISM #formal_name vaccinia virus DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 18-Feb-2000 ACCESSIONS B29889; G42510; PN0119; T37339 REFERENCE A29889 !$#authors Schmitt, J.F.C.; Stunnenberg, H.G. !$#journal J. Virol. (1988) 62:1889-1897 !$#title Sequence and transcriptional analysis of the vaccinia virus !1HindIII I fragment. !$#cross-references MUID:88215015; PMID:2835495 !$#accession B29889 !'##molecule_type DNA !'##residues 1-73 ##label SCH !'##cross-references GB:J03399; NID:g335662; PIDN:AAB59804.1; !1PID:g335664 !'##experimental_source strain WR REFERENCE A33172 !$#authors Johnson, G.P. !$#submission submitted to GenBank, June 1990 !$#accession G42510 !'##molecule_type DNA !'##residues 1-73 ##label JOH !'##experimental_source strain Copenhagen REFERENCE PN0119 !$#authors Rjazankina, O.I.; Shchelkunov, S.N.; Muravlev, A.I.; !1Netesova, N.A.; Mikrjukov, N.N.; Gutorov, V.V.; Nikulin, !1A.E.; Kulichkov, V.A.; Malygin, E.G. !$#journal Mol. Biol. (Mosk.) (1990) 24:968-976 !$#title The molecular biological study of vaccinia virus genome II; !1localization and fine structure of the vaccinia virus genes !1encoding 36K and 12K polypeptides. !$#cross-references MUID:91066899; PMID:2250685 !$#accession PN0119 !'##molecule_type DNA !'##residues 1-73 ##label RJA !'##experimental_source strain L-IVP REFERENCE Z20877 !$#authors Antoine, G.; Scheiflinger, F.; Falkner, F.G.; Dorner, F. !$#submission submitted to the EMBL Data Library, March 1997 !$#description The complete genomic sequence of the Modified Vaccinia !1Ankara (MVA) strain. !$#accession T37339 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-73 ##label ANT !'##cross-references EMBL:U94848; PIDN:AAB96434.1 !'##experimental_source strain Ankara GENETICS !$#gene I2 !$#note MVA063L CLASSIFICATION #superfamily vaccinia virus I2 protein KEYWORDS late protein SUMMARY #length 73 #molecular-weight 8499 #checksum 8238 SEQUENCE /// ENTRY WZVZI3 #type complete TITLE I3 protein - vaccinia virus ALTERNATE_NAMES I3L protein ORGANISM #formal_name vaccinia virus DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 29-Oct-1999 ACCESSIONS C29889; H42510; PS0395 REFERENCE A29889 !$#authors Schmitt, J.F.C.; Stunnenberg, H.G. !$#journal J. Virol. (1988) 62:1889-1897 !$#title Sequence and transcriptional analysis of the vaccinia virus !1HindIII I fragment. !$#cross-references MUID:88215015; PMID:2835495 !$#accession C29889 !'##molecule_type DNA !'##residues 1-269 ##label SCH !'##cross-references GB:J03399; NID:g335662; PIDN:AAB59805.1; !1PID:g335665 !'##experimental_source strain WR REFERENCE A33172 !$#authors Johnson, G.P. !$#submission submitted to GenBank, June 1990 !$#accession H42510 !'##status preliminary !'##molecule_type DNA !'##residues 1-163,'A',165-194,'I',196-269 ##label JOH !'##experimental_source strain Copenhagen REFERENCE PN0119 !$#authors Rjazankina, O.I.; Shchelkunov, S.N.; Muravlev, A.I.; !1Netesova, N.A.; Mikrjukov, N.N.; Gutorov, V.V.; Nikulin, !1A.E.; Kulichkov, V.A.; Malygin, E.G. !$#journal Mol. Biol. (Mosk.) (1990) 24:968-976 !$#title The molecular biological study of vaccinia virus genome II; !1localization and fine structure of the vaccinia virus genes !1encoding 36K and 12K polypeptides. !$#cross-references MUID:91066899; PMID:2250685 !$#accession PS0395 !'##molecule_type DNA !'##residues 242-269 ##label RJA !'##experimental_source strain L-IVP COMMENT This protein is synthesized in the early as well as the late !1phase of infection. GENETICS !$#gene I3 CLASSIFICATION #superfamily vaccinia virus I3 protein KEYWORDS early protein; late protein SUMMARY #length 269 #molecular-weight 29997 #checksum 2329 SEQUENCE /// ENTRY WZVZI5 #type complete TITLE I5 protein - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jul-1999 ACCESSIONS E29889 REFERENCE A29889 !$#authors Schmitt, J.F.C.; Stunnenberg, H.G. !$#journal J. Virol. (1988) 62:1889-1897 !$#title Sequence and transcriptional analysis of the vaccinia virus !1HindIII I fragment. !$#cross-references MUID:88215015; PMID:2835495 !$#accession E29889 !'##molecule_type DNA !'##residues 1-79 ##label SCH !'##cross-references GB:J03399; NID:g335662; PIDN:AAB59807.1; !1PID:g335667 GENETICS !$#gene I5 CLASSIFICATION #superfamily vaccinia virus I5 protein KEYWORDS late protein SUMMARY #length 79 #molecular-weight 8744 #checksum 5994 SEQUENCE /// ENTRY WMVZ44 #type complete TITLE I5 protein - fowlpox virus (strain HP444) ORGANISM #formal_name fowlpox virus DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jun-2000 ACCESSIONS JS0228; D48563 REFERENCE JS0220 !$#authors Binns, M.M.; Tomley, F.M.; Campbell, J.; Boursnell, M.E.G. !$#journal J. Gen. Virol. (1988) 69:1275-1283 !$#title Comparison of a conserved region in fowlpox virus and !1vaccinia virus genomes and the translocation of the fowlpox !1virus thymidine kinase gene. !$#cross-references MUID:88258470; PMID:2838574 !$#accession JS0228 !'##molecule_type DNA !'##residues 1-81 ##label BI1 !'##cross-references GB:D00321; NID:g221411; PIDN:BAA00232.1; !1PID:g221412 REFERENCE A48563 !$#authors Binns, M.M.; Boursnell, M.E.; Skinner, M.A. !$#journal Virus Res. (1992) 24:161-172 !$#title Gene translocations in poxviruses: the fowlpox virus !1thymidine kinase gene is flanked by 15 bp direct repeats and !1occupies the locus which in vaccinia virus is occupied by !1the ribonucleotide reductase large subunit gene. !$#cross-references MUID:92410746; PMID:1326827 !$#accession D48563 !'##molecule_type DNA !'##residues 1-81 ##label BI2 !'##cross-references GB:AJ223385; NID:g3123522; PIDN:CAA11296.1; !1PID:g3123533 !'##note sequence extracted from NCBI backbone (NCBIN:113549, !1NCBIP:113553) GENETICS !$#gene I5 CLASSIFICATION #superfamily vaccinia virus I5 protein SUMMARY #length 81 #molecular-weight 9123 #checksum 973 SEQUENCE /// ENTRY WMVZP0 #type complete TITLE FP0 protein - fowlpox virus (strain HP444) ORGANISM #formal_name fowlpox virus DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jun-2000 ACCESSIONS JS0220 REFERENCE JS0220 !$#authors Binns, M.M.; Tomley, F.M.; Campbell, J.; Boursnell, M.E.G. !$#journal J. Gen. Virol. (1988) 69:1275-1283 !$#title Comparison of a conserved region in fowlpox virus and !1vaccinia virus genomes and the translocation of the fowlpox !1virus thymidine kinase gene. !$#cross-references MUID:88258470; PMID:2838574 !$#accession JS0220 !'##molecule_type DNA !'##residues 1-260 ##label BIN !'##cross-references GB:D00320; NID:g221401; PIDN:BAA00223.1; !1PID:g221402 CLASSIFICATION #superfamily fowlpox virus FP0 protein KEYWORDS transcription regulation SUMMARY #length 260 #molecular-weight 29853 #checksum 465 SEQUENCE /// ENTRY WZVZI6 #type complete TITLE I6 43.5K protein - vaccinia virus ALTERNATE_NAMES I6L protein ORGANISM #formal_name vaccinia virus DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 18-Feb-2000 ACCESSIONS F29889; B42511; T37343 REFERENCE A29889 !$#authors Schmitt, J.F.C.; Stunnenberg, H.G. !$#journal J. Virol. (1988) 62:1889-1897 !$#title Sequence and transcriptional analysis of the vaccinia virus !1HindIII I fragment. !$#cross-references MUID:88215015; PMID:2835495 !$#accession F29889 !'##molecule_type DNA !'##residues 1-382 ##label SCH !'##cross-references GB:J03399; NID:g335662; PIDN:AAB59808.1; !1PID:g335668 !'##experimental_source strain WR REFERENCE A33172 !$#authors Johnson, G.P. !$#submission submitted to GenBank, June 1990 !$#accession B42511 !'##molecule_type DNA !'##residues 1-382 ##label JOH !'##experimental_source strain Copenhagen REFERENCE Z20877 !$#authors Antoine, G.; Scheiflinger, F.; Falkner, F.G.; Dorner, F. !$#submission submitted to the EMBL Data Library, March 1997 !$#description The complete genomic sequence of the Modified Vaccinia !1Ankara (MVA) strain. !$#accession T37343 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-382 ##label ANT !'##cross-references EMBL:U94848; PIDN:AAB96438.1 !'##experimental_source strain Ankara GENETICS !$#gene I6 !$#note MVA067L CLASSIFICATION #superfamily vaccinia virus I6 protein KEYWORDS glycoprotein FEATURE !$117,138,184,230, !$267,321 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 382 #molecular-weight 43453 #checksum 6907 SEQUENCE /// ENTRY E48563 #type complete TITLE I6 protein - fowlpox virus (strain HP444) ORGANISM #formal_name fowlpox virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jun-2000 ACCESSIONS E48563 REFERENCE A48563 !$#authors Binns, M.M.; Boursnell, M.E.; Skinner, M.A. !$#journal Virus Res. (1992) 24:161-172 !$#title Gene translocations in poxviruses: the fowlpox virus !1thymidine kinase gene is flanked by 15 bp direct repeats and !1occupies the locus which in vaccinia virus is occupied by !1the ribonucleotide reductase large subunit gene. !$#cross-references MUID:92410746; PMID:1326827 !$#accession E48563 !'##molecule_type DNA !'##residues 1-390 ##label BIN !'##cross-references GB:AJ223385; NID:g3123522; PIDN:CAA11297.1; !1PID:g3123534 !'##note sequence extracted from NCBI backbone (NCBIN:113549, !1NCBIP:113554) GENETICS !$#gene I6 CLASSIFICATION #superfamily vaccinia virus I6 protein KEYWORDS glycoprotein FEATURE !$32,140,237,387 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 390 #molecular-weight 45297 #checksum 1294 SEQUENCE /// ENTRY WZVZI7 #type complete TITLE I7 protein - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jul-1999 ACCESSIONS G29889; A38497 REFERENCE A29889 !$#authors Schmitt, J.F.C.; Stunnenberg, H.G. !$#journal J. Virol. (1988) 62:1889-1897 !$#title Sequence and transcriptional analysis of the vaccinia virus !1HindIII I fragment. !$#cross-references MUID:88215015; PMID:2835495 !$#accession G29889 !'##molecule_type DNA !'##residues 1-423 ##label SCH !'##cross-references GB:J03399; NID:g335662; PIDN:AAB59809.1; !1PID:g335669 REFERENCE A38497 !$#authors Fathi, Z.; Condit, R.C. !$#journal Virology (1991) 181:258-272 !$#title Genetic and molecular biological characterization of a !1vaccinia virus temperature-sensitive complementation group !1affecting a virion component. !$#cross-references MUID:91134989; PMID:1994576 !$#accession A38497 !'##molecule_type DNA !'##residues 1-215 ##label FAT !'##cross-references EMBL:M29901 GENETICS !$#gene I7 CLASSIFICATION #superfamily vaccinia virus I7 protein KEYWORDS late protein SUMMARY #length 423 #molecular-weight 49010 #checksum 4129 SEQUENCE /// ENTRY F48563 #type complete TITLE I7 protein - fowlpox virus (strain HP444) ORGANISM #formal_name fowlpox virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jun-2000 ACCESSIONS F48563 REFERENCE A48563 !$#authors Binns, M.M.; Boursnell, M.E.; Skinner, M.A. !$#journal Virus Res. (1992) 24:161-172 !$#title Gene translocations in poxviruses: the fowlpox virus !1thymidine kinase gene is flanked by 15 bp direct repeats and !1occupies the locus which in vaccinia virus is occupied by !1the ribonucleotide reductase large subunit gene. !$#cross-references MUID:92410746; PMID:1326827 !$#accession F48563 !'##molecule_type DNA !'##residues 1-421 ##label BIN !'##cross-references GB:AJ223385; NID:g3123522; PIDN:CAA11298.1; !1PID:g3123535 !'##note sequence extracted from NCBI backbone (NCBIN:113549, !1NCBIP:113555) GENETICS !$#gene I7 CLASSIFICATION #superfamily vaccinia virus I7 protein KEYWORDS late protein SUMMARY #length 421 #molecular-weight 48621 #checksum 8049 SEQUENCE /// ENTRY WZVZG1 #type complete TITLE G1L protein - Amsacta moorei poxvirus ORGANISM #formal_name Amsacta moorei poxvirus DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS A41561 REFERENCE A41561 !$#authors Hall, R.L.; Moyer, R.W. !$#journal J. Virol. (1991) 65:6516-6527 !$#title Identification, cloning, and sequencing of a fragment of !1Amsacta moorei entomopoxvirus DNA containing the spheroidin !1gene and three vaccinia virus-related open reading frames. !$#cross-references MUID:92046310; PMID:1942245 !$#accession A41561 !'##molecule_type DNA !'##residues 1-464 ##label HAL !'##cross-references GB:M77182; NID:g209631; PIDN:AAA42379.1; !1PID:g209632 CLASSIFICATION #superfamily vaccinia virus I7 protein KEYWORDS late protein SUMMARY #length 464 #molecular-weight 55541 #checksum 9465 SEQUENCE /// ENTRY WZVZG2 #type complete TITLE G2R protein - Amsacta moorei poxvirus ORGANISM #formal_name Amsacta moorei poxvirus DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS B41561 REFERENCE A41561 !$#authors Hall, R.L.; Moyer, R.W. !$#journal J. Virol. (1991) 65:6516-6527 !$#title Identification, cloning, and sequencing of a fragment of !1Amsacta moorei entomopoxvirus DNA containing the spheroidin !1gene and three vaccinia virus-related open reading frames. !$#cross-references MUID:92046310; PMID:1942245 !$#accession B41561 !'##molecule_type DNA !'##residues 1-225 ##label HAL !'##cross-references GB:M77182; NID:g209631; PIDN:AAA42380.1; !1PID:g209633 CLASSIFICATION #superfamily Amsacta moorei poxvirus G2R protein SUMMARY #length 225 #molecular-weight 26008 #checksum 7244 SEQUENCE /// ENTRY WZVZG3 #type complete TITLE G3L protein - Amsacta moorei poxvirus ORGANISM #formal_name Amsacta moorei poxvirus DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS C41561 REFERENCE A41561 !$#authors Hall, R.L.; Moyer, R.W. !$#journal J. Virol. (1991) 65:6516-6527 !$#title Identification, cloning, and sequencing of a fragment of !1Amsacta moorei entomopoxvirus DNA containing the spheroidin !1gene and three vaccinia virus-related open reading frames. !$#cross-references MUID:92046310; PMID:1942245 !$#accession C41561 !'##molecule_type DNA !'##residues 1-78 ##label HAL !'##cross-references GB:M77182; NID:g209631; PIDN:AAA42381.1; !1PID:g209634 CLASSIFICATION #superfamily Amsacta moorei poxvirus G3L protein SUMMARY #length 78 #molecular-weight 8834 #checksum 6294 SEQUENCE /// ENTRY WZVZI8 #type complete TITLE I8 protein - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus DATE 30-Jun-1989 #sequence_revision 30-Sep-1992 #text_change 19-Jan-2001 ACCESSIONS B38497; H29889 REFERENCE A38497 !$#authors Fathi, Z.; Condit, R.C. !$#journal Virology (1991) 181:258-272 !$#title Genetic and molecular biological characterization of a !1vaccinia virus temperature-sensitive complementation group !1affecting a virion component. !$#cross-references MUID:91134989; PMID:1994576 !$#accession B38497 !'##molecule_type DNA !'##residues 1-676 ##label FAT !'##cross-references GB:J03399; EMBL:M29901; NID:g335662; !1PIDN:AAB59810.1; PID:g335670 REFERENCE A29889 !$#authors Schmitt, J.F.C.; Stunnenberg, H.G. !$#journal J. Virol. (1988) 62:1889-1897 !$#title Sequence and transcriptional analysis of the vaccinia virus !1HindIII I fragment. !$#cross-references MUID:88215015; PMID:2835495 !$#accession H29889 !'##molecule_type DNA !'##residues 1-99 ##label SCH !'##cross-references GB:J03399 !'##note the authors translated the codons TAC, AGT, GAA, CAC, ACA, ATA, !1and AGC for residues 93-99 as Ile, Tyr, Leu, Glu, His, Thr, !1and Ile, respectively GENETICS !$#gene I8 CLASSIFICATION #superfamily vaccinia virus I8 protein KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$185-192 #region nucleotide-binding motif A (P-loop)\ !$292-297 #region nucleotide-binding motif B\ !$296-299 #region DEXH motif SUMMARY #length 676 #molecular-weight 77599 #checksum 5125 SEQUENCE /// ENTRY G48563 #type complete TITLE I8 protein - fowlpox virus (strain HP444) ORGANISM #formal_name fowlpox virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 19-Jan-2001 ACCESSIONS G48563 REFERENCE A48563 !$#authors Binns, M.M.; Boursnell, M.E.; Skinner, M.A. !$#journal Virus Res. (1992) 24:161-172 !$#title Gene translocations in poxviruses: the fowlpox virus !1thymidine kinase gene is flanked by 15 bp direct repeats and !1occupies the locus which in vaccinia virus is occupied by !1the ribonucleotide reductase large subunit gene. !$#cross-references MUID:92410746; PMID:1326827 !$#accession G48563 !'##molecule_type DNA !'##residues 1-682 ##label BIN !'##cross-references GB:AJ223385; NID:g3123522; PIDN:CAA11299.1; !1PID:g3123536 !'##note sequence extracted from NCBI backbone (NCBIN:113549, !1NCBIP:113556) GENETICS !$#gene I8 CLASSIFICATION #superfamily vaccinia virus I8 protein KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$194-201 #region nucleotide-binding motif A (P-loop)\ !$299-304 #region nucleotide-binding motif B\ !$303-306 #region DEXH motif SUMMARY #length 682 #molecular-weight 79807 #checksum 482 SEQUENCE /// ENTRY WZVZA1 #type complete TITLE 21.7K HindIII-C protein - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 08-Sep-2000 ACCESSIONS A31829 REFERENCE A94385 !$#authors Kotwal, G.J.; Moss, B. !$#journal Virology (1988) 167:524-537 !$#title Analysis of a large cluster of nonessential genes deleted !1from a vaccinia virus terminal transposition mutant. !$#cross-references MUID:89073756; PMID:2849238 !$#accession A31829 !'##molecule_type DNA !'##residues 1-184 ##label KOT !'##cross-references GB:M22812; NID:g335691; PIDN:AAA69592.1; !1PID:g893301 CLASSIFICATION #superfamily vaccinia virus 21.7K HindIII-C protein; RING !1finger homology KEYWORDS early protein SUMMARY #length 184 #molecular-weight 21604 #checksum 2786 SEQUENCE /// ENTRY WZVZA2 #type complete TITLE 7K HindIII-C protein - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS B31829 REFERENCE A94385 !$#authors Kotwal, G.J.; Moss, B. !$#journal Virology (1988) 167:524-537 !$#title Analysis of a large cluster of nonessential genes deleted !1from a vaccinia virus terminal transposition mutant. !$#cross-references MUID:89073756; PMID:2849238 !$#accession B31829 !'##molecule_type DNA !'##residues 1-68 ##label KOT !'##cross-references GB:M22812; NID:g335691; PIDN:AAA69593.1; !1PID:g893302 CLASSIFICATION #superfamily vaccinia virus 7K HindIII-C protein SUMMARY #length 68 #molecular-weight 7814 #checksum 2966 SEQUENCE /// ENTRY WZVZA7 #type complete TITLE 5K HindIII-C protein - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS G31829 REFERENCE A94385 !$#authors Kotwal, G.J.; Moss, B. !$#journal Virology (1988) 167:524-537 !$#title Analysis of a large cluster of nonessential genes deleted !1from a vaccinia virus terminal transposition mutant. !$#cross-references MUID:89073756; PMID:2849238 !$#accession G31829 !'##molecule_type DNA !'##residues 1-60 ##label KOT !'##cross-references GB:M22812; NID:g335691; PIDN:AAA69598.1; !1PID:g893307 CLASSIFICATION #superfamily vaccinia virus 5K HindIII-C protein KEYWORDS early protein SUMMARY #length 60 #molecular-weight 5680 #checksum 8511 SEQUENCE /// ENTRY WZVZA9 #type complete TITLE 20K HindIII-C protein - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS I31829 REFERENCE A94385 !$#authors Kotwal, G.J.; Moss, B. !$#journal Virology (1988) 167:524-537 !$#title Analysis of a large cluster of nonessential genes deleted !1from a vaccinia virus terminal transposition mutant. !$#cross-references MUID:89073756; PMID:2849238 !$#accession I31829 !'##molecule_type DNA !'##residues 1-177 ##label KOT !'##cross-references GB:M22812; NID:g335691; PIDN:AAA69600.1; !1PID:g893309 CLASSIFICATION #superfamily vaccinia virus 20K HindIII-C protein KEYWORDS late protein SUMMARY #length 177 #molecular-weight 20753 #checksum 4882 SEQUENCE /// ENTRY WZVZB1 #type complete TITLE vaccinia virus 18K HindIII-C protein - vaccinia virus (strain Ankara and WR) ALTERNATE_NAMES C7L protein; host range protein ORGANISM #formal_name vaccinia virus #variety strain Ankara DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 28-Jan-2000 ACCESSIONS A33348; G42503; T30771 REFERENCE A94385 !$#authors Kotwal, G.J.; Moss, B. !$#journal Virology (1988) 167:524-537 !$#title Analysis of a large cluster of nonessential genes deleted !1from a vaccinia virus terminal transposition mutant. !$#cross-references MUID:89073756; PMID:2849238 !$#accession A33348 !'##molecule_type DNA !'##residues 1-150 ##label KOT !'##cross-references GB:M22812; NID:g335691; PIDN:AAA69601.1; !1PID:g893310 !'##experimental_source strain WR REFERENCE A33172 !$#authors Johnson, G.P. !$#submission submitted to GenBank, June 1990 !$#accession G42503 !'##molecule_type DNA !'##residues 1-150 ##label JOH !'##experimental_source strain Copenhagen REFERENCE Z20877 !$#authors Antoine, G.; Scheiflinger, F.; Falkner, F.G.; Dorner, F. !$#submission submitted to the EMBL Data Library, March 1997 !$#description The complete genomic sequence of the Modified Vaccinia !1Ankara (MVA) strain. !$#accession T30771 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-150 ##label ANT !'##cross-references EMBL:U94848; PIDN:AAB96405.1 !'##experimental_source strain Ankara GENETICS !$#note MVA018L CLASSIFICATION #superfamily vaccinia virus 18K HindIII-C protein KEYWORDS early protein SUMMARY #length 150 #molecular-weight 17998 #checksum 3972 SEQUENCE /// ENTRY WZVZCP #type complete TITLE CF8a protein - sheep pox virus (isolate Kenya sheep-1, KS-1) ORGANISM #formal_name sheep pox virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jun-2000 ACCESSIONS C31813 REFERENCE A31813 !$#authors Gershon, P.D.; Black, D.N. !$#journal J. Gen. Virol. (1989) 70:525-533 !$#title The nucleotide sequence around the capripoxvirus thymidine !1kinase gene reveals a gene shared specifically with !1leporipoxvirus. !$#cross-references MUID:89279233; PMID:2732700 !$#accession C31813 !'##molecule_type DNA !'##residues 1-197 ##label GER !'##cross-references GB:D00423; NID:g221120; PIDN:BAA00325.1; !1PID:g221124 CLASSIFICATION #superfamily vaccinia virus 18K HindIII-C protein KEYWORDS early protein SUMMARY #length 197 #molecular-weight 23069 #checksum 7899 SEQUENCE /// ENTRY WZVZSW #type complete TITLE SwF8a protein - swinepox virus ORGANISM #formal_name swinepox virus DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jul-1999 ACCESSIONS C37949 REFERENCE A37949 !$#authors Schnitzlein, W.M.; Tripathy, D.N. !$#journal Virology (1991) 181:727-732 !$#title Identification and nucleotide sequence of the thymidine !1kinase gene of swinepox virus. !$#cross-references MUID:91196265; PMID:1840707 !$#accession C37949 !'##molecule_type DNA !'##residues 1-185 ##label SCH !'##cross-references EMBL:M59931; NID:g335128; PIDN:AAA47892.1; !1PID:g335131 CLASSIFICATION #superfamily vaccinia virus 18K HindIII-C protein KEYWORDS early protein SUMMARY #length 185 #molecular-weight 21751 #checksum 5446 SEQUENCE /// ENTRY WZVZM3 #type complete TITLE MF8a protein - myxoma virus ORGANISM #formal_name myxoma virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS JQ1423 REFERENCE JQ1421 !$#authors Jackson, R.J.; Bults, H.G. !$#journal J. Gen. Virol. (1992) 73:323-328 !$#title The myxoma virus thymidine kinase gene: sequence and !1transcriptional mapping. !$#cross-references MUID:92166739; PMID:1538190 !$#accession JQ1423 !'##molecule_type DNA !'##residues 1-158 ##label JAC !'##cross-references GB:X52655; NID:g987956; PIDN:CAA36881.1; !1PID:g987957 CLASSIFICATION #superfamily vaccinia virus 18K HindIII-C protein KEYWORDS early protein SUMMARY #length 158 #molecular-weight 18392 #checksum 8946 SEQUENCE /// ENTRY WZVZB2 #type complete TITLE 17K HindIII-C protein - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS B33348 REFERENCE A94385 !$#authors Kotwal, G.J.; Moss, B. !$#journal Virology (1988) 167:524-537 !$#title Analysis of a large cluster of nonessential genes deleted !1from a vaccinia virus terminal transposition mutant. !$#cross-references MUID:89073756; PMID:2849238 !$#accession B33348 !'##molecule_type DNA !'##residues 1-151 ##label KOT !'##cross-references GB:M22812; NID:g335691; PIDN:AAA69602.1; !1PID:g893311 CLASSIFICATION #superfamily vaccinia virus 17K HindIII-C protein KEYWORDS early protein SUMMARY #length 151 #molecular-weight 17322 #checksum 5592 SEQUENCE /// ENTRY WMVZN1 #type complete TITLE T3A protein - sheep pox virus (strain InS-1) ORGANISM #formal_name sheep pox virus DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jul-1999 ACCESSIONS A33869 REFERENCE A33869 !$#authors Gershon, P.D.; Black, D.N. !$#journal Virology (1989) 172:350-354 !$#title A capripoxvirus pseudogene whose only intact homologs are in !1other poxvirus genomes. !$#cross-references MUID:89370320; PMID:2773324 !$#accession A33869 !'##molecule_type DNA !'##residues 1-159 ##label GER !'##cross-references GB:M28823; NID:g323263; PIDN:AAC32901.1; !1PID:g323264 CLASSIFICATION #superfamily vaccinia virus 17K HindIII-C protein SUMMARY #length 159 #molecular-weight 17879 #checksum 8850 SEQUENCE /// ENTRY WZVZB3 #type complete TITLE 24K HindIII-C protein - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS C33348 REFERENCE A94385 !$#authors Kotwal, G.J.; Moss, B. !$#journal Virology (1988) 167:524-537 !$#title Analysis of a large cluster of nonessential genes deleted !1from a vaccinia virus terminal transposition mutant. !$#cross-references MUID:89073756; PMID:2849238 !$#accession C33348 !'##molecule_type DNA !'##residues 1-204 ##label KOT !'##cross-references GB:M22812; NID:g335691; PIDN:AAA69603.1; !1PID:g893312 CLASSIFICATION #superfamily vaccinia virus 24K HindIII-C protein KEYWORDS early protein SUMMARY #length 204 #molecular-weight 24489 #checksum 3023 SEQUENCE /// ENTRY WZVZB6 #type complete TITLE 59K HindIII-C protein - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS F33348 REFERENCE A94385 !$#authors Kotwal, G.J.; Moss, B. !$#journal Virology (1988) 167:524-537 !$#title Analysis of a large cluster of nonessential genes deleted !1from a vaccinia virus terminal transposition mutant. !$#cross-references MUID:89073756; PMID:2849238 !$#accession F33348 !'##molecule_type DNA !'##residues 1-512 ##label KOT !'##cross-references GB:M22812; NID:g335691; PIDN:AAA69606.1; !1PID:g893315 CLASSIFICATION #superfamily vaccinia virus 59K HindIII-C protein SUMMARY #length 512 #molecular-weight 59241 #checksum 961 SEQUENCE /// ENTRY WZVZB7 #type complete TITLE 27K HindIII-C protein - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS G33348 REFERENCE A94385 !$#authors Kotwal, G.J.; Moss, B. !$#journal Virology (1988) 167:524-537 !$#title Analysis of a large cluster of nonessential genes deleted !1from a vaccinia virus terminal transposition mutant. !$#cross-references MUID:89073756; PMID:2849238 !$#accession G33348 !'##molecule_type DNA !'##residues 1-229 ##label KOT !'##cross-references GB:M22812; NID:g335691; PIDN:AAA69607.1; !1PID:g893316 CLASSIFICATION #superfamily vaccinia virus 27K HindIII-C protein KEYWORDS early protein SUMMARY #length 229 #molecular-weight 27028 #checksum 1386 SEQUENCE /// ENTRY WZVZB8 #type complete TITLE 13.8K HindIII-N protein - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS H33348 REFERENCE A94385 !$#authors Kotwal, G.J.; Moss, B. !$#journal Virology (1988) 167:524-537 !$#title Analysis of a large cluster of nonessential genes deleted !1from a vaccinia virus terminal transposition mutant. !$#cross-references MUID:89073756; PMID:2849238 !$#accession H33348 !'##molecule_type DNA !'##residues 1-117 ##label KOT !'##cross-references GB:M22812; NID:g335691; PIDN:AAA69608.1; !1PID:g893317 CLASSIFICATION #superfamily vaccinia virus 13.8K HindIII-N protein SUMMARY #length 117 #molecular-weight 13961 #checksum 676 SEQUENCE /// ENTRY SAVZVV #type complete TITLE surface antigen precursor - vaccinia virus ORGANISM #formal_name vaccinia virus #note host Homo sapiens (man) DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jun-2000 ACCESSIONS A35522 REFERENCE A35522 !$#authors Ueda, Y.; Morikawa, S.; Matsuura, Y. !$#journal Virology (1990) 177:588-594 !$#title Identification and nucleotide sequence of the gene encoding !1a surface antigen induced by vaccinia virus. !$#cross-references MUID:90320131; PMID:2196742 !$#accession A35522 !'##molecule_type mRNA !'##residues 1-351 ##label UED !'##cross-references EMBL:D90076; NID:g222769; PIDN:BAA14116.1; !1PID:g222770 CLASSIFICATION #superfamily vaccinia virus surface antigen; immunoglobulin !1homology KEYWORDS glycoprotein; surface antigen FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-351 #product surface antigen #status predicted #label !8SAT\ !$265-335 #domain immunoglobulin homology #label IMM\ !$117,182,261,269 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 351 #molecular-weight 40701 #checksum 4233 SEQUENCE /// ENTRY SAVZVC #type complete TITLE surface antigen precursor - vaccinia virus (strain Copenhagen) ORGANISM #formal_name vaccinia virus #note host Homo sapiens (man) DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 21-Jan-2000 ACCESSIONS I42527 REFERENCE A42501 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:517-563 !$#title Appendix to "The complete DNA sequence of vaccinia virus". !$#accession I42527 !'##molecule_type DNA !'##residues 1-353 ##label GOE !'##cross-references GB:M35027; NID:g335317; PIDN:AAA48218.1; !1PID:g335566 REFERENCE A42531 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:247-266 !$#title The complete DNA sequence of vaccinia virus. !$#cross-references MUID:91021027; PMID:2219722 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given CLASSIFICATION #superfamily vaccinia virus surface antigen; immunoglobulin !1homology KEYWORDS glycoprotein; surface antigen FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-353 #product surface antigen #status predicted #label !8SAT\ !$267-337 #domain immunoglobulin homology #label IMM\ !$119,184,263,271 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 353 #molecular-weight 40952 #checksum 4859 SEQUENCE /// ENTRY SAVZWR #type complete TITLE surface antigen precursor - vaccinia virus (strain WR) ALTERNATE_NAMES B18R protein ORGANISM #formal_name vaccinia virus #note host Homo sapiens (man) DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jun-2000 ACCESSIONS B38472; JQ1812; JQ0930 REFERENCE A38472 !$#authors Smith, G.L.; Chan, Y.S. !$#journal J. Gen. Virol. (1991) 72:511-518 !$#title Two vaccinia virus proteins structurally related to the !1interleukin-1 receptor and the immunoglobulin superfamily. !$#cross-references MUID:91170931; PMID:1826022 !$#accession B38472 !'##molecule_type DNA !'##residues 1-351 ##label SM1 !'##cross-references GB:D01019; NID:g222698; PIDN:BAA00826.1; !1PID:g222699 REFERENCE JQ1767 !$#authors Smith, G.L.; Chan, Y.S.; Howard, S.T. !$#journal J. Gen. Virol. (1991) 72:1349-1376 !$#title Nucleotide sequence of 42kbp of vaccinia virus strain WR !1from near the right inverted terminal repeat. !$#cross-references MUID:91259063; PMID:2045793 !$#accession JQ1812 !'##molecule_type DNA !'##residues 1-351 ##label SM2 !'##cross-references DDBJ:D11079; NID:g222717; PIDN:BAA01848.1; !1PID:g222763; DDBJ:D01019; NID:g222698; PID:g222699 CLASSIFICATION #superfamily vaccinia virus surface antigen; immunoglobulin !1homology KEYWORDS glycoprotein; surface antigen FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-351 #product surface antigen #status predicted #label !8SFA\ !$66-131 #domain immunoglobulin homology #label IMM1\ !$165-223 #domain immunoglobulin homology #label IMM2\ !$265-335 #domain immunoglobulin homology #label IMM3\ !$73-129,172-221, !$272-333 #disulfide_bonds #status predicted\ !$117,182,261,269 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 351 #molecular-weight 40731 #checksum 3777 SEQUENCE /// ENTRY WMVZ15 #type complete TITLE B15R protein precursor - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus #note host Homo sapiens (man) DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jun-2000 ACCESSIONS A38472; JQ0929 REFERENCE A38472 !$#authors Smith, G.L.; Chan, Y.S. !$#journal J. Gen. Virol. (1991) 72:511-518 !$#title Two vaccinia virus proteins structurally related to the !1interleukin-1 receptor and the immunoglobulin superfamily. !$#cross-references MUID:91170931; PMID:1826022 !$#accession A38472 !'##molecule_type DNA !'##residues 1-326 ##label SMI !'##cross-references GB:D01018; NID:g222696; PIDN:BAA00825.1; !1PID:g222697 CLASSIFICATION #superfamily vaccinia virus B15R protein; immunoglobulin !1homology KEYWORDS glycoprotein FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-326 #product B15R protein #status predicted #label BRP\ !$41-101 #domain immunoglobulin homology #label IMM1\ !$136-196 #domain immunoglobulin homology #label IMM2\ !$235-311 #domain immunoglobulin homology #label IMM3\ !$48-99,143-194, !$242-309 #disulfide_bonds #status predicted\ !$80,103,113,206,237 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 326 #molecular-weight 36593 #checksum 2119 SEQUENCE /// ENTRY HRVZCP #type complete TITLE host range protein - cowpox virus ORGANISM #formal_name cowpox virus DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 30-May-1997 ACCESSIONS A29887 REFERENCE A29887 !$#authors Spehner, D.; Gillard, S.; Drillien, R.; Kirn, A. !$#journal J. Virol. (1988) 62:1297-1304 !$#title A cowpox virus gene required for multiplication in Chinese !1hamster ovary cells. !$#cross-references MUID:88155768; PMID:2831390 !$#accession A29887 !'##molecule_type DNA !'##residues 1-668 ##label SPE !'##cross-references GB:M19531 CLASSIFICATION #superfamily cowpox virus host range protein; ankyrin repeat !1homology; vaccinia virus 13.6K HindIII-C protein homology; !1vaccinia virus 27.4K HindIII-C protein homology; vaccinia !1virus 8.6K HindIII-C protein homology; vaccinia virus 8.8K !1HindIII-C protein homology KEYWORDS early protein FEATURE !$1-69 #domain vaccinia virus 8.6K HindIII-C protein !8homology #label VHC\ !$85-146 #domain vaccinia virus 8.8K HindIII-C protein !8homology #label VHH\ !$280-393 #domain vaccinia virus 13.6K HindIII-C protein !8homology #label VVP\ !$438-666 #domain vaccinia virus 27.4K HindIII-C protein !8homology #label VHP SUMMARY #length 668 #molecular-weight 77234 #checksum 3779 SEQUENCE /// ENTRY WZVZA3 #type complete TITLE 27.4K HindIII-C protein - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS C31829 REFERENCE A94385 !$#authors Kotwal, G.J.; Moss, B. !$#journal Virology (1988) 167:524-537 !$#title Analysis of a large cluster of nonessential genes deleted !1from a vaccinia virus terminal transposition mutant. !$#cross-references MUID:89073756; PMID:2849238 !$#accession C31829 !'##molecule_type DNA !'##residues 1-237 ##label KOT !'##cross-references GB:M22812; NID:g335691; PIDN:AAA69594.1; !1PID:g893303 CLASSIFICATION #superfamily vaccinia virus 27.4K HindIII-C protein; !1vaccinia virus 27.4K HindIII-C protein homology KEYWORDS early protein FEATURE !$7-235 #domain vaccinia virus 27.4K HindIII-C protein !8homology #label VHP SUMMARY #length 237 #molecular-weight 27443 #checksum 9363 SEQUENCE /// ENTRY WZVZA4 #type complete TITLE 13.6K HindIII-C protein - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS D31829 REFERENCE A94385 !$#authors Kotwal, G.J.; Moss, B. !$#journal Virology (1988) 167:524-537 !$#title Analysis of a large cluster of nonessential genes deleted !1from a vaccinia virus terminal transposition mutant. !$#cross-references MUID:89073756; PMID:2849238 !$#accession D31829 !'##molecule_type DNA !'##residues 1-115 ##label KOT !'##cross-references GB:M22812; NID:g335691; PIDN:AAA69595.1; !1PID:g893304 CLASSIFICATION #superfamily vaccinia virus 13.6K HindIII-C protein; !1vaccinia virus 13.6K HindIII-C protein homology KEYWORDS early protein FEATURE !$1-108 #domain vaccinia virus 13.6K HindIII-C protein !8homology #label VVP SUMMARY #length 115 #molecular-weight 13624 #checksum 3574 SEQUENCE /// ENTRY WZVZA6 #type complete TITLE 8.6K HindIII-C protein - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS F31829 REFERENCE A94385 !$#authors Kotwal, G.J.; Moss, B. !$#journal Virology (1988) 167:524-537 !$#title Analysis of a large cluster of nonessential genes deleted !1from a vaccinia virus terminal transposition mutant. !$#cross-references MUID:89073756; PMID:2849238 !$#accession F31829 !'##molecule_type DNA !'##residues 1-71 ##label KOT !'##cross-references GB:M22812; NID:g335691; PIDN:AAA69597.1; !1PID:g893306 CLASSIFICATION #superfamily vaccinia virus 8.6K HindIII-C protein; vaccinia !1virus 8.6K HindIII-C protein homology KEYWORDS early protein FEATURE !$1-69 #domain vaccinia virus 8.6K HindIII-C protein !8homology #label VHC SUMMARY #length 71 #molecular-weight 8525 #checksum 3720 SEQUENCE /// ENTRY WZVZA5 #type complete TITLE 8.8K HindIII-C protein - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS E31829 REFERENCE A94385 !$#authors Kotwal, G.J.; Moss, B. !$#journal Virology (1988) 167:524-537 !$#title Analysis of a large cluster of nonessential genes deleted !1from a vaccinia virus terminal transposition mutant. !$#cross-references MUID:89073756; PMID:2849238 !$#accession E31829 !'##molecule_type DNA !'##residues 1-77 ##label KOT !'##cross-references GB:M22812; NID:g335691; PIDN:AAA69596.1; !1PID:g893305 CLASSIFICATION #superfamily vaccinia virus 8.8K HindIII-C protein; vaccinia !1virus 8.8K HindIII-C protein homology KEYWORDS early protein FEATURE !$5-66 #domain vaccinia virus 8.8K HindIII-C protein !8homology #label VHH SUMMARY #length 77 #molecular-weight 8829 #checksum 1099 SEQUENCE /// ENTRY WZVZA8 #type complete TITLE 74K HindIII-C protein - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS H31829 REFERENCE A94385 !$#authors Kotwal, G.J.; Moss, B. !$#journal Virology (1988) 167:524-537 !$#title Analysis of a large cluster of nonessential genes deleted !1from a vaccinia virus terminal transposition mutant. !$#cross-references MUID:89073756; PMID:2849238 !$#accession H31829 !'##molecule_type DNA !'##residues 1-634 ##label KOT !'##cross-references GB:M22812; NID:g335691; PIDN:AAA69599.1; !1PID:g893308 CLASSIFICATION #superfamily vaccinia virus 74K HindIII-C protein; vaccinia !1virus 27.4K HindIII-C protein homology; vaccinia virus 8.8K !1HindIII-C protein homology KEYWORDS early protein FEATURE !$54-114 #domain vaccinia virus 8.8K HindIII-C protein !8homology #label VHH\ !$392-630 #domain vaccinia virus 27.4K HindIII-C protein !8homology #label VHP SUMMARY #length 634 #molecular-weight 74684 #checksum 4198 SEQUENCE /// ENTRY WMVZ9T #type complete TITLE A-type inclusion protein 2 - vaccinia virus (strain Copenhagen) ALTERNATE_NAMES A25L protein ORGANISM #formal_name vaccinia virus #note host Homo sapiens (man) DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Jul-1999 ACCESSIONS I42519 REFERENCE A42501 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:517-563 !$#title Appendix to "The complete DNA sequence of vaccinia virus". !$#accession I42519 !'##molecule_type DNA !'##residues 1-65 ##label GOE !'##cross-references GB:M35027; NID:g335317; PIDN:AAA48150.1; !1PID:g335498 !'##experimental_source strain Copenhagen REFERENCE A42531 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:247-266 !$#title The complete DNA sequence of vaccinia virus. !$#cross-references MUID:91021027; PMID:2219722 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given CLASSIFICATION #superfamily vaccinia virus A-type inclusion protein KEYWORDS inclusion protein SUMMARY #length 65 #molecular-weight 7465 #checksum 908 SEQUENCE /// ENTRY WMVZAI #type complete TITLE A-type inclusion protein - cowpox virus (strain CPRO6) ORGANISM #formal_name cowpox virus DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jun-2000 ACCESSIONS JQ0006; S01495 REFERENCE JQ0006 !$#authors Funahashi, S.; Sato, T.; Shida, H. !$#journal J. Gen. Virol. (1988) 69:35-47 !$#title Cloning and characterization of the gene encoding the major !1protein of the A-type inclusion body of cowpox virus. !$#cross-references MUID:88089536; PMID:2826668 !$#accession JQ0006 !'##molecule_type DNA !'##residues 1-1284 ##label FUN !'##cross-references GB:D00319; NID:g221140; PIDN:BAA00222.1; !1PID:g221141 REFERENCE S01494 !$#authors Patel, D.D.; Pickup, D.J. !$#journal EMBO J. (1987) 6:3787-3794 !$#title Messenger RNAs of a strongly-expressed late gene of cowpox !1virus contain 5'-terminal poly(A) sequences. !$#cross-references MUID:88111568; PMID:2828037 !$#accession S01495 !'##molecule_type DNA !'##residues 1-109 ##label PAT !'##cross-references EMBL:X06343 CLASSIFICATION #superfamily cowpox virus A-type inclusion protein KEYWORDS inclusion protein SUMMARY #length 1284 #molecular-weight 150328 #checksum 1804 SEQUENCE /// ENTRY WMVZ94 #type complete TITLE A-type inclusion protein - vaccinia virus (strain WR) ORGANISM #formal_name vaccinia virus #note host Homo sapiens (man) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 29-Oct-1999 ACCESSIONS A41701; A40825; S29908 REFERENCE A41701 !$#authors De Carlos, A.; Paez, E. !$#journal Virology (1991) 185:768-778 !$#title Isolation and characterization of mutants of vaccinia virus !1with a modified 94-kDa inclusion protein. !$#cross-references MUID:92074241; PMID:1962448 !$#accession A41701 !'##molecule_type DNA !'##residues 1-725 ##label DEC !'##cross-references GB:M76371; NID:g335683; PIDN:AAA48275.1; !1PID:g335684 REFERENCE A40825 !$#authors Amegadzie, B.Y.; Sisler, J.R.; Moss, B. !$#journal Virology (1992) 186:777-782 !$#title Frame-shift mutations within the vaccinia virus A-type !1inclusion protein gene. !$#cross-references MUID:92124754; PMID:1733111 !$#accession A40825 !'##molecule_type DNA !'##residues 1-586,'KQ',589-609,'R',611-618;620-682,'S',684-725 ##label !1AME !'##cross-references GB:M61187; NID:g335782; PIDN:AAA48321.1; !1PID:g335784 REFERENCE S29907 !$#authors Amegadzie, B.Y. !$#submission submitted to the EMBL Data Library, January 1991 !$#accession S29908 !'##status preliminary !'##molecule_type DNA !'##residues 1-586,'KQ',589-609,'R',611-618,620-682,'S',684-725 ##label !1AM2 !'##cross-references EMBL:X57318; NID:g62239; PIDN:CAA40574.1; !1PID:g62241 CLASSIFICATION #superfamily cowpox virus A-type inclusion protein KEYWORDS inclusion protein SUMMARY #length 725 #molecular-weight 84400 #checksum 7660 SEQUENCE /// ENTRY WMVZ1U #type complete TITLE A-type inclusion protein 1 - vaccinia virus (strain Copenhagen) ALTERNATE_NAMES A26L protein ORGANISM #formal_name vaccinia virus #note host Homo sapiens (man) DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Jul-1999 ACCESSIONS A42520 REFERENCE A42501 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:517-563 !$#title Appendix to "The complete DNA sequence of vaccinia virus". !$#accession A42520 !'##molecule_type DNA !'##residues 1-322 ##label GOE !'##cross-references GB:M35027; NID:g335317; PIDN:AAA48151.1; !1PID:g335499 !'##experimental_source strain Copenhagen REFERENCE A42531 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:247-266 !$#title The complete DNA sequence of vaccinia virus. !$#cross-references MUID:91021027; PMID:2219722 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given CLASSIFICATION #superfamily cowpox virus A-type inclusion protein KEYWORDS inclusion protein SUMMARY #length 322 #molecular-weight 37319 #checksum 101 SEQUENCE /// ENTRY WMVZMX #type complete TITLE M9-R protein - myxoma virus (strain Lausanne) ORGANISM #formal_name myxoma virus DATE 30-Jun-1989 #sequence_revision 19-Oct-1995 #text_change 22-Oct-2001 ACCESSIONS A36418; B26131 REFERENCE A36418 !$#authors Upton, C.; Macen, J.L.; Wishart, D.S.; McFadden, G. !$#journal Virology (1990) 179:618-631 !$#title Myxoma virus and malignant rabbit fibroma virus encode a !1serpin-like protein important for virus virulence. !$#cross-references MUID:91049428; PMID:2173255 !$#accession A36418 !'##status preliminary !'##molecule_type DNA !'##residues 1-509 ##label UPT !'##cross-references GB:M15806; EMBL:M35234; NID:g332299; !1PIDN:AAA46627.1; PID:g332301 REFERENCE A93024 !$#authors Upton, C.; Macen, J.L.; McFadden, G. !$#journal J. Virol. (1987) 61:1271-1275 !$#title Mapping and sequencing of a gene from myxoma virus that is !1related to those encoding epidermal growth factor and !1transforming growth factor alpha. !$#cross-references MUID:87141350; PMID:3029424 !$#accession B26131 !'##molecule_type DNA !'##residues 1-235 ##label UP2 CLASSIFICATION #superfamily myxoma virus M9-R protein; POZ domain homology FEATURE !$1-104 #domain POZ domain homology #label POZ SUMMARY #length 509 #molecular-weight 57930 #checksum 6855 SEQUENCE /// ENTRY WMVZN2 #type complete TITLE T4 protein - sheep pox virus (strain InS-1) ORGANISM #formal_name sheep pox virus DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jul-1999 ACCESSIONS B33869 REFERENCE A33869 !$#authors Gershon, P.D.; Black, D.N. !$#journal Virology (1989) 172:350-354 !$#title A capripoxvirus pseudogene whose only intact homologs are in !1other poxvirus genomes. !$#cross-references MUID:89370320; PMID:2773324 !$#accession B33869 !'##molecule_type DNA !'##residues 1-240 ##label GER !'##cross-references GB:M28823; NID:g323263; PIDN:AAC32902.1; !1PID:g323265 CLASSIFICATION #superfamily capripoxvirus T4 protein SUMMARY #length 240 #molecular-weight 27414 #checksum 3134 SEQUENCE /// ENTRY WMVZN4 #type complete TITLE T4 protein - sheep pox virus (strain KS-1) ORGANISM #formal_name sheep pox virus DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jul-1999 ACCESSIONS D33869 REFERENCE A33869 !$#authors Gershon, P.D.; Black, D.N. !$#journal Virology (1989) 172:350-354 !$#title A capripoxvirus pseudogene whose only intact homologs are in !1other poxvirus genomes. !$#cross-references MUID:89370320; PMID:2773324 !$#accession D33869 !'##molecule_type DNA !'##residues 1-240 ##label GER !'##cross-references GB:M28824; NID:g323266; PIDN:AAC32896.1; !1PID:g323268 CLASSIFICATION #superfamily capripoxvirus T4 protein SUMMARY #length 240 #molecular-weight 27459 #checksum 3297 SEQUENCE /// ENTRY WMVZN3 #type complete TITLE T3C protein - sheep pox virus (strain KS-1) ORGANISM #formal_name sheep pox virus DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jul-1999 ACCESSIONS C33869 REFERENCE A33869 !$#authors Gershon, P.D.; Black, D.N. !$#journal Virology (1989) 172:350-354 !$#title A capripoxvirus pseudogene whose only intact homologs are in !1other poxvirus genomes. !$#cross-references MUID:89370320; PMID:2773324 !$#accession C33869 !'##molecule_type DNA !'##residues 1-131 ##label GER !'##cross-references GB:M28824; NID:g323266; PIDN:AAC32895.1; !1PID:g323267 CLASSIFICATION #superfamily capripoxvirus T3C protein SUMMARY #length 131 #molecular-weight 15487 #checksum 3771 SEQUENCE /// ENTRY PYVZAM #type complete TITLE spheroidin precursor - Amsacta moorei poxvirus ORGANISM #formal_name Amsacta moorei poxvirus DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS JQ1436; PQ0289; E41561 REFERENCE JQ1436 !$#authors Banville, M.; Dumas, F.; Trifiro, S.; Arif, B.; Richardson, !1C. !$#journal J. Gen. Virol. (1992) 73:559-566 !$#title The predicted amino acid sequence of the spheroidin protein !1from Amsacta moorei entomopoxvirus: lack of homology between !1major occlusion body proteins of different poxviruses. !$#cross-references MUID:92185464; PMID:1545219 !$#accession JQ1436 !'##molecule_type DNA !'##residues 1-1003 ##label BAN !'##cross-references GB:M75889; NID:g209629; PIDN:AAA42378.1; !1PID:g209630 !$#accession PQ0289 !'##molecule_type protein !'##residues 2-7,'X',9-11,'X',13;86-90,'X',92-98,'X', !1100-102;532-540;728-750;786-802;810-819;828-838 ##label BAN1 REFERENCE A41561 !$#authors Hall, R.L.; Moyer, R.W. !$#journal J. Virol. (1991) 65:6516-6527 !$#title Identification, cloning, and sequencing of a fragment of !1Amsacta moorei entomopoxvirus DNA containing the spheroidin !1gene and three vaccinia virus-related open reading frames. !$#cross-references MUID:92046310; PMID:1942245 !$#accession E41561 !'##molecule_type DNA !'##residues 1-1003 ##label HAL !'##cross-references GB:M77182; NID:g209631; PIDN:AAA42383.1; !1PID:g209636 COMMENT This protein is a major component of the occlusion body !1which serves to protect the virions from the environment. CLASSIFICATION #superfamily Amsacta moorei poxvirus spheroidin KEYWORDS acetylated amino end; glycoprotein; leucine zipper FEATURE !$2-1003 #product spheroidin #status experimental #label MAT\ !$119-140 #region leucine zipper motif\ !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental\ !$47,109,204,210,259, !$510,529,547,561, !$799,901,922,955 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$537,799 #binding_site carbohydrate (Asn) (covalent) #status !8absent SUMMARY #length 1003 #molecular-weight 114869 #checksum 7301 SEQUENCE /// ENTRY PYVZCB #type complete TITLE spheroidin precursor - Choristoneura biennis poxvirus ORGANISM #formal_name Choristoneura biennis poxvirus DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS A34743 REFERENCE A34743 !$#authors Yuen, L.; Dionne, J.; Arif, B.; Richardson, C. !$#journal Virology (1990) 175:427-433 !$#title Identification and sequencing of the spheroidin gene of !1Choristoneura biennis entomopoxvirus. !$#cross-references MUID:90223988; PMID:2327073 !$#accession A34743 !'##molecule_type DNA !'##residues 1-341 ##label YUE !'##cross-references EMBL:M34140; NID:g323273; PIDN:AAA42887.1; !1PID:g323274 COMMENT This protein appears to be essential for viral replication. CLASSIFICATION #superfamily spheroidin KEYWORDS glycoprotein; replication FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-341 #product spheroidin #status predicted #label SPD\ !$176,196 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 341 #molecular-weight 38709 #checksum 832 SEQUENCE /// ENTRY WMNV34 #type complete TITLE fusolin, spindle body protein precursor - Autographa californica nuclear polyhedrosis virus ALTERNATE_NAMES spheroidin precursor homolog ORGANISM #formal_name Autographa californica nuclear polyhedrosis virus, AcMNPV #note host Autographa californica (alfalfa looper); dsDNA virus DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jun-2000 ACCESSIONS A34036; A36387; A72858 REFERENCE A34036 !$#authors Wu, J.; Miller, L.K. !$#journal J. Gen. Virol. (1989) 70:2449-2459 !$#title Sequence, transcription and translation of a late gene of !1the Autographa californica nuclear polyhedrosis virus !1encoding a 34.8K polypeptide. !$#cross-references MUID:89381697; PMID:2674327 !$#accession A34036 !'##molecule_type DNA !'##residues 1-302 ##label WUJ !'##cross-references EMBL:D00583; NID:g222179; PIDN:BAA00461.1; !1PID:g2160357 REFERENCE A36387 !$#authors Vialard, J.E.; Yuen, L.; Richardson, C.D. !$#journal J. Virol. (1990) 64:5804-5811 !$#title Identification and characterization of a baculovirus !1occlusion body glycoprotein which resembles spheroidin, an !1entomopoxvirus protein. !$#cross-references MUID:91056548; PMID:2243377 !$#accession A36387 !'##molecule_type DNA !'##residues 1-302 ##label VIA REFERENCE A72850 !$#authors Ayres, M.D.; Howard, S.C.; Kuzio, J.; Lopez-Ferber, M.; !1Possee, R.D. !$#journal Virology (1994) 202:586-605 !$#title The complete DNA sequence of Autographa californica nuclear !1polyhedrosis virus. !$#cross-references MUID:94303173; PMID:8030224 !$#accession A72858 !'##status preliminary !'##molecule_type DNA !'##residues 1-302 ##label AYR !'##cross-references GB:L22858; NID:g510708; PIDN:AAA66694.1; !1PID:g559133 COMMENT This protein appears to be essential for viral replication. GENETICS !$#gene Ac-gp37 CLASSIFICATION #superfamily spheroidin KEYWORDS glycoprotein; replication FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-302 #product spheroidin #status predicted #label SPD\ !$193,293 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 302 #molecular-weight 34798 #checksum 3724 SEQUENCE /// ENTRY EDXF3 #type complete TITLE immediate-early protein - frog virus 3 ORGANISM #formal_name frog virus 3, FV3 DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 02-May-1994 ACCESSIONS A03896 REFERENCE A03896 !$#authors Willis, D.; Foglesong, D.; Granoff, A. !$#journal J. Virol. (1984) 53:905-912 !$#title Nucleotide sequence of an immediate-early frog virus 3 gene. !$#accession A03896 !'##molecule_type DNA !'##residues 1-157 ##label WIL CLASSIFICATION #superfamily frog virus 3 immediate-early protein KEYWORDS early protein SUMMARY #length 157 #molecular-weight 17660 #checksum 6844 SEQUENCE /// ENTRY EDXFI3 #type complete TITLE immediate-early protein - frog virus 3 ORGANISM #formal_name frog virus 3, FV3 DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS A29886 REFERENCE A29886 !$#authors Beckman, W.; Tham, T.N.; Aubertin, A.M.; Willis, D.B. !$#journal J. Virol. (1988) 62:1271-1277 !$#title Structure and regulation of the immediate-early frog virus 3 !1gene that encodes ICR489. !$#cross-references MUID:88155764; PMID:2831387 !$#accession A29886 !'##molecule_type DNA !'##residues 1-394 ##label BEC !'##cross-references GB:M19872; NID:g325385; PIDN:AAA43824.1; !1PID:g325386 CLASSIFICATION #superfamily frog virus 3 immediate-early protein KEYWORDS early protein SUMMARY #length 394 #molecular-weight 45790 #checksum 6727 SEQUENCE /// ENTRY RPXFIL #type complete TITLE repetitive protein ORF4 - Chilo iridescent virus (type 6) ORGANISM #formal_name Chilo iridescent virus DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jul-1999 ACCESSIONS D31828 REFERENCE A31828 !$#authors Fischer, M.; Schnitzler, P.; Scholz, J.; Roesen-Wolff, A.; !1Delius, H.; Darai, G. !$#journal Virology (1988) 167:497-506 !$#title DNA nucleotide sequence analysis of the PvuII DNA fragment L !1of the genome of insect iridescent virus type 6 reveals a !1complex cluster of multiple tandem, overlapping, and !1interdigitated repetitive DNA elements. !$#cross-references MUID:89073753; PMID:3201751 !$#accession D31828 !'##molecule_type DNA !'##residues 1-118 ##label FIS !'##cross-references GB:M23625; NID:g331325; PIDN:AAA66589.1; !1PID:g808707 CLASSIFICATION #superfamily insect iridescent virus repetitive protein SUMMARY #length 118 #molecular-weight 12042 #checksum 5223 SEQUENCE /// ENTRY RPXFIM #type complete TITLE repetitive protein ORF5 - Chilo iridescent virus (type 6) ORGANISM #formal_name Chilo iridescent virus DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 13-Sep-1996 ACCESSIONS E31828 REFERENCE A31828 !$#authors Fischer, M.; Schnitzler, P.; Scholz, J.; Roesen-Wolff, A.; !1Delius, H.; Darai, G. !$#journal Virology (1988) 167:497-506 !$#title DNA nucleotide sequence analysis of the PvuII DNA fragment L !1of the genome of insect iridescent virus type 6 reveals a !1complex cluster of multiple tandem, overlapping, and !1interdigitated repetitive DNA elements. !$#cross-references MUID:89073753; PMID:3201751 !$#accession E31828 !'##molecule_type DNA !'##residues 1-333 ##label FIS CLASSIFICATION #superfamily insect iridescent virus repetitive protein SUMMARY #length 333 #molecular-weight 32375 #checksum 6646 SEQUENCE /// ENTRY RPXFIK #type complete TITLE repetitive protein ORF3 - Chilo iridescent virus (type 6) ORGANISM #formal_name Chilo iridescent virus DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jul-1999 ACCESSIONS C31828 REFERENCE A31828 !$#authors Fischer, M.; Schnitzler, P.; Scholz, J.; Roesen-Wolff, A.; !1Delius, H.; Darai, G. !$#journal Virology (1988) 167:497-506 !$#title DNA nucleotide sequence analysis of the PvuII DNA fragment L !1of the genome of insect iridescent virus type 6 reveals a !1complex cluster of multiple tandem, overlapping, and !1interdigitated repetitive DNA elements. !$#cross-references MUID:89073753; PMID:3201751 !$#accession C31828 !'##molecule_type DNA !'##residues 1-118 ##label FIS !'##cross-references GB:M23625; NID:g331325; PIDN:AAA66588.1; !1PID:g808706 CLASSIFICATION #superfamily insect iridescent virus repetitive protein SUMMARY #length 118 #molecular-weight 12127 #checksum 7324 SEQUENCE /// ENTRY RPXFII #type complete TITLE repetitive protein ORF1 - Chilo iridescent virus (type 6) ORGANISM #formal_name Chilo iridescent virus DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jul-1999 ACCESSIONS A31828 REFERENCE A31828 !$#authors Fischer, M.; Schnitzler, P.; Scholz, J.; Roesen-Wolff, A.; !1Delius, H.; Darai, G. !$#journal Virology (1988) 167:497-506 !$#title DNA nucleotide sequence analysis of the PvuII DNA fragment L !1of the genome of insect iridescent virus type 6 reveals a !1complex cluster of multiple tandem, overlapping, and !1interdigitated repetitive DNA elements. !$#cross-references MUID:89073753; PMID:3201751 !$#accession A31828 !'##molecule_type DNA !'##residues 1-127 ##label FIS !'##cross-references GB:M23625; NID:g331325; PIDN:AAA66586.1; !1PID:g808704 CLASSIFICATION #superfamily insect iridescent virus repetitive protein SUMMARY #length 127 #molecular-weight 13259 #checksum 4024 SEQUENCE /// ENTRY RPXFIJ #type complete TITLE repetitive protein ORF2 - Chilo iridescent virus (type 6) ORGANISM #formal_name Chilo iridescent virus DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jul-1999 ACCESSIONS B31828 REFERENCE A31828 !$#authors Fischer, M.; Schnitzler, P.; Scholz, J.; Roesen-Wolff, A.; !1Delius, H.; Darai, G. !$#journal Virology (1988) 167:497-506 !$#title DNA nucleotide sequence analysis of the PvuII DNA fragment L !1of the genome of insect iridescent virus type 6 reveals a !1complex cluster of multiple tandem, overlapping, and !1interdigitated repetitive DNA elements. !$#cross-references MUID:89073753; PMID:3201751 !$#accession B31828 !'##molecule_type DNA !'##residues 1-126 ##label FIS !'##cross-references GB:M23625; NID:g331325; PIDN:AAA66587.1; !1PID:g808705 CLASSIFICATION #superfamily insect iridescent virus repetitive protein SUMMARY #length 126 #molecular-weight 13371 #checksum 6065 SEQUENCE /// ENTRY VCXFAS #type complete TITLE major capsid protein - African swine fever virus (strain BA71V) ORGANISM #formal_name African swine fever virus, ASFV DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jul-1999 ACCESSIONS A34745 REFERENCE A34745 !$#authors Lopez-Otin, C.; Freije, J.M.P.; Parra, F.; Mendez, E.; !1Vinuela, E. !$#journal Virology (1990) 175:477-484 !$#title Mapping and sequence of the gene coding for protein p72, the !1major capsid protein of African swine fever virus. !$#cross-references MUID:90223993; PMID:2327074 !$#accession A34745 !'##molecule_type DNA !'##residues 1-646 ##label LOP !'##cross-references EMBL:M34142; NID:g210647; PIDN:AAA42730.1; !1PID:g210648 CLASSIFICATION #superfamily African swine fever virus major capsid protein KEYWORDS capsid protein SUMMARY #length 646 #molecular-weight 73192 #checksum 403 SEQUENCE /// ENTRY VCXFTI #type complete TITLE major capsid protein - Tipula iridescent virus (type 1) ORGANISM #formal_name Tipula iridescent virus #note host Tipula paludosa (European crane fly) DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jul-1999 ACCESSIONS A33558 REFERENCE A33558 !$#authors Tajbakhsh, S.; Lee, P.E.; Watson, D.C.; Seligy, V.L. !$#journal J. Virol. (1990) 64:125-136 !$#title Molecular cloning, characterization, and expression of the !1Tipula iridescent virus capsid gene. !$#cross-references MUID:90080113; PMID:2293661 !$#accession A33558 !'##molecule_type DNA !'##residues 1-464 ##label TAJ !'##cross-references EMBL:M33542; NID:g331317; PIDN:AAA46245.1; !1PID:g331318 CLASSIFICATION #superfamily Tipula iridescent virus major capsid protein KEYWORDS capsid protein SUMMARY #length 464 #molecular-weight 50833 #checksum 6095 SEQUENCE /// ENTRY VCXFSI #type complete TITLE major capsid protein - Simulium iridescent virus (type 22) ORGANISM #formal_name Simulium iridescent virus #note host Simulium spp. (blackfly) DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jul-1999 ACCESSIONS B37075; C37075 REFERENCE A37075 !$#authors Cameron, I.R. !$#journal Virology (1990) 178:35-42 !$#title Identification and characterization of the gene encoding the !1major structural protein of insect iridescent virus type 22. !$#cross-references MUID:90357789; PMID:2389558 !$#accession B37075 !'##molecule_type DNA !'##residues 1-472 ##label CAM !'##cross-references EMBL:M32799; NID:g331321; PIDN:AAA66585.1; !1PID:g331322 !$#accession C37075 !'##molecule_type protein !'##residues 72-81;89-116 ##label CA2 CLASSIFICATION #superfamily Tipula iridescent virus major capsid protein KEYWORDS capsid protein SUMMARY #length 472 #molecular-weight 51992 #checksum 5185 SEQUENCE /// ENTRY JQ2215 #type complete TITLE major capsid protein - Chilo iridescent virus ORGANISM #formal_name Chilo iridescent virus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JQ2215 REFERENCE JQ2215 !$#authors Stohwasser, R.; Raab, K.; Schnitzler, P.; Janssen, W.; !1Darai, G. !$#journal J. Gen. Virol. (1993) 74:873-879 !$#title Identification of the gene encoding the major capsid protein !1of insect iridescent virus type 6 by polymerase chain !1reaction. !$#cross-references MUID:93260401; PMID:8492091 !$#accession JQ2215 !'##molecule_type DNA !'##residues 1-467 ##label STO !'##cross-references GB:M99395; NID:g292992; PIDN:AAA46246.1; !1PID:g292993 !'##note the authors translated codon GTT for residue 231 as Tyr, codon !1TAT for residue 328 as Ser, codon CTT for residue 331 as Ile CLASSIFICATION #superfamily Tipula iridescent virus major capsid protein KEYWORDS capsid protein SUMMARY #length 467 #molecular-weight 51398 #checksum 4691 SEQUENCE /// ENTRY VCXECV #type complete TITLE major capsid protein - Chlorella virus PBCV-1 ORGANISM #formal_name Chlorella virus PBCV-1 DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 29-Oct-1999 ACCESSIONS A40245; T17933 REFERENCE A40245 !$#authors Graves, M.V.; Meints, R.H. !$#journal Virology (1992) 188:198-207 !$#title Characterization of the major capsid protein and cloning of !1its gene from algal virus PBCV-1. !$#cross-references MUID:92230218; PMID:1566573 !$#accession A40245 !'##molecule_type DNA !'##residues 1-437 ##label GRA !'##cross-references GB:M85052; NID:g323323; PIDN:AAA88828.1; !1PID:g323324 REFERENCE Z18806 !$#authors Graves, M.V.; Van Etten, J.L. !$#submission submitted to the EMBL Data Library, May 1999 !$#accession T17933 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-437 ##label GR2 !'##cross-references EMBL:U42580; NID:g4028896; PIDN:AAC96798.1 !'##experimental_source specific host Chlorella strain NC64A GENETICS !$#note A430L CLASSIFICATION #superfamily Tipula iridescent virus major capsid protein KEYWORDS coat protein; glycoprotein FEATURE !$47,189,370,376 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 437 #molecular-weight 48165 #checksum 6798 SEQUENCE /// ENTRY KIXFFV #type complete TITLE major capsid protein - lymphocystis disease virus (isolate flounder) CONTAINS thymidine kinase (EC 2.7.1.21) ORGANISM #formal_name lymphocystis disease virus, LCDV DATE 31-Dec-1992 #sequence_revision 13-Mar-1997 #text_change 07-May-1999 ACCESSIONS JQ2345; A39995 REFERENCE JQ2345 !$#authors Schnitzler, P.; Darai, G. !$#journal J. Gen. Virol. (1993) 74:2143-2150 !$#title Identification of the gene encoding the major capsid protein !1of fish lymphocystis disease virus. !$#cross-references MUID:94014998; PMID:8409939 !$#accession JQ2345 !'##molecule_type DNA !'##residues 1-459 ##label SCH !'##experimental_source isolate flounder REFERENCE A39995 !$#authors Schnitzler, P.; Handermann, M.; Szepe, O.; Darai, G. !$#journal Virology (1991) 182:835-840 !$#title The primary structure of the thymidine kinase gene of fish !1lymphocystis disease virus. !$#cross-references MUID:91220734; PMID:2024501 !$#accession A39995 !'##molecule_type DNA !'##residues 142-459 ##label SC2 !'##cross-references GB:M61115; NID:g325366; PID:g325367 !'##experimental_source strain F !'##note this is probably a thymidine kinase GENETICS !$#gene tk CLASSIFICATION #superfamily Tipula iridescent virus major capsid protein KEYWORDS phosphotransferase SUMMARY #length 459 #molecular-weight 51346 #checksum 4122 SEQUENCE /// ENTRY WMXFB1 #type complete TITLE I226R protein - African swine fever virus (strain BA71V) ORGANISM #formal_name African swine fever virus, ASFV DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS A39448 REFERENCE A39448 !$#authors Rodriguez, J.M.; Salas, M.L.; Vinuela, E. !$#journal Virology (1992) 186:40-52 !$#title Genes homologous to ubiquitin-conjugating proteins and !1eukaryotic transcription factor SII in African swine fever !1virus. !$#cross-references MUID:92087485; PMID:1309282 !$#accession A39448 !'##molecule_type DNA !'##residues 1-226 ##label ROD !'##cross-references GB:M77121; NID:g210618; PIDN:AAA42699.1; !1PID:g210619 CLASSIFICATION #superfamily African swine fever virus I226R protein SUMMARY #length 226 #molecular-weight 27005 #checksum 1639 SEQUENCE /// ENTRY WMXFB2 #type complete TITLE I243L protein - African swine fever virus (strain BA71V) ORGANISM #formal_name African swine fever virus, ASFV DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS B39448 REFERENCE A39448 !$#authors Rodriguez, J.M.; Salas, M.L.; Vinuela, E. !$#journal Virology (1992) 186:40-52 !$#title Genes homologous to ubiquitin-conjugating proteins and !1eukaryotic transcription factor SII in African swine fever !1virus. !$#cross-references MUID:92087485; PMID:1309282 !$#accession B39448 !'##molecule_type DNA !'##residues 1-243 ##label ROD !'##cross-references GB:M77121; NID:g210618; PIDN:AAA42700.1; !1PID:g210620 COMMENT This protein may be a transcription factor. CLASSIFICATION #superfamily African swine fever virus I243L protein SUMMARY #length 243 #molecular-weight 28558 #checksum 332 SEQUENCE /// ENTRY WMXFB3 #type complete TITLE I73R protein - African swine fever virus (strain BA71V) ORGANISM #formal_name African swine fever virus, ASFV DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS C39448 REFERENCE A39448 !$#authors Rodriguez, J.M.; Salas, M.L.; Vinuela, E. !$#journal Virology (1992) 186:40-52 !$#title Genes homologous to ubiquitin-conjugating proteins and !1eukaryotic transcription factor SII in African swine fever !1virus. !$#cross-references MUID:92087485; PMID:1309282 !$#accession C39448 !'##molecule_type DNA !'##residues 1-73 ##label ROD !'##cross-references GB:M77121; NID:g210618; PIDN:AAA42701.1; !1PID:g210621 CLASSIFICATION #superfamily African swine fever virus I73R protein SUMMARY #length 73 #molecular-weight 8521 #checksum 9200 SEQUENCE /// ENTRY WMXFB4 #type complete TITLE I329L protein - African swine fever virus (strain BA71V) ORGANISM #formal_name African swine fever virus, ASFV DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS D39448 REFERENCE A39448 !$#authors Rodriguez, J.M.; Salas, M.L.; Vinuela, E. !$#journal Virology (1992) 186:40-52 !$#title Genes homologous to ubiquitin-conjugating proteins and !1eukaryotic transcription factor SII in African swine fever !1virus. !$#cross-references MUID:92087485; PMID:1309282 !$#accession D39448 !'##molecule_type DNA !'##residues 1-329 ##label ROD !'##cross-references GB:M77121; NID:g210618; PIDN:AAA42702.1; !1PID:g210622 CLASSIFICATION #superfamily African swine fever virus I329L protein KEYWORDS transmembrane protein SUMMARY #length 329 #molecular-weight 38541 #checksum 4724 SEQUENCE /// ENTRY WMXFB5 #type complete TITLE I78L protein - African swine fever virus (strain BA71V) ORGANISM #formal_name African swine fever virus, ASFV DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS E39448 REFERENCE A39448 !$#authors Rodriguez, J.M.; Salas, M.L.; Vinuela, E. !$#journal Virology (1992) 186:40-52 !$#title Genes homologous to ubiquitin-conjugating proteins and !1eukaryotic transcription factor SII in African swine fever !1virus. !$#cross-references MUID:92087485; PMID:1309282 !$#accession E39448 !'##molecule_type DNA !'##residues 1-78 ##label ROD !'##cross-references GB:M77121; NID:g210618; PIDN:AAA42703.1; !1PID:g210623 CLASSIFICATION #superfamily African swine fever virus I78L protein SUMMARY #length 78 #molecular-weight 8982 #checksum 5904 SEQUENCE /// ENTRY WMXFB6 #type complete TITLE I177L protein - African swine fever virus (strain BA71V) ORGANISM #formal_name African swine fever virus, ASFV DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS G39448 REFERENCE A39448 !$#authors Rodriguez, J.M.; Salas, M.L.; Vinuela, E. !$#journal Virology (1992) 186:40-52 !$#title Genes homologous to ubiquitin-conjugating proteins and !1eukaryotic transcription factor SII in African swine fever !1virus. !$#cross-references MUID:92087485; PMID:1309282 !$#accession G39448 !'##molecule_type DNA !'##residues 1-177 ##label ROD !'##cross-references GB:M77121; NID:g210618; PIDN:AAA42705.1; !1PID:g210625 CLASSIFICATION #superfamily African swine fever virus I177L protein KEYWORDS transmembrane protein SUMMARY #length 177 #molecular-weight 20440 #checksum 1296 SEQUENCE /// ENTRY WMXFB7 #type complete TITLE I196L protein - African swine fever virus (strain BA71V) ORGANISM #formal_name African swine fever virus, ASFV DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS H39448 REFERENCE A39448 !$#authors Rodriguez, J.M.; Salas, M.L.; Vinuela, E. !$#journal Virology (1992) 186:40-52 !$#title Genes homologous to ubiquitin-conjugating proteins and !1eukaryotic transcription factor SII in African swine fever !1virus. !$#cross-references MUID:92087485; PMID:1309282 !$#accession H39448 !'##molecule_type DNA !'##residues 1-196 ##label ROD !'##cross-references GB:M77121; NID:g210618; PIDN:AAA42706.1; !1PID:g210626 CLASSIFICATION #superfamily African swine fever virus I196L protein SUMMARY #length 196 #molecular-weight 21961 #checksum 2572 SEQUENCE /// ENTRY WMXF12 #type complete TITLE P12 attachment protein - African swine fever virus (strain BA71V) ALTERNATE_NAMES p12 protein ORGANISM #formal_name African swine fever virus, ASFV DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 26-Feb-1999 ACCESSIONS A41998 REFERENCE A41998 !$#authors Alcami, A.; Angulo, A.; Lopez-Otin, C.; Munoz, M.; Freije, !1J.M.P.; Carrascosa, A.L.; Vinuela, E. !$#journal J. Virol. (1992) 66:3860-3868 !$#title Amino acid sequence and structural properties of protein !1p12, an African swine fever virus attachment protein. !$#cross-references MUID:92260660; PMID:1583732 !$#accession A41998 !'##molecule_type DNA !'##residues 1-61 ##label ALC !'##cross-references GB:M84177 CLASSIFICATION #superfamily African swine fever virus P12 attachment !1protein KEYWORDS glycoprotein; transmembrane protein FEATURE !$15-31 #domain transmembrane #status predicted #label TMN\ !$53 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 61 #molecular-weight 6679 #checksum 6954 SEQUENCE /// ENTRY JQ1626 #type complete TITLE attachment protein G - turkey rhinotracheitis virus ORGANISM #formal_name turkey rhinotracheitis virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jul-1999 ACCESSIONS JQ1626 REFERENCE PQ0405 !$#authors Ling, R.; Easton, A.J.; Pringle, C.R. !$#journal J. Gen. Virol. (1992) 73:1709-1715 !$#title Sequence analysis of the 22K, SH and G genes of turkey !1rhinotracheitis virus and their intergenic regions reveals a !1gene order different from that of other pneumoviruses. !$#cross-references MUID:92333255; PMID:1629697 !$#accession JQ1626 !'##molecule_type mRNA !'##residues 1-391 ##label LIN !'##cross-references GB:S40185; NID:g251600; PIDN:AAB22547.1; !1PID:g251605 GENETICS !$#gene G CLASSIFICATION #superfamily turkey rhinotracheitis virus attachment protein !1G KEYWORDS glycoprotein FEATURE !$173,255,303,339 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 391 #molecular-weight 42981 #checksum 4458 SEQUENCE /// ENTRY WMXF30 #type complete TITLE P30 phosphoprotein - African swine fever virus ORGANISM #formal_name African swine fever virus, ASFV DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS A40237 REFERENCE A40237 !$#authors Afonso, C.L.; Alcaraz, C.; Brun, A.; Sussman, M.D.; Onisk, !1D.V.; Escribano, J.M.; Rock, D.L. !$#journal Virology (1992) 189:368-373 !$#title Characterization of P30, a highly antigenic membrane and !1secreted protein of African swine fever virus. !$#cross-references MUID:92295579; PMID:1604821 !$#accession A40237 !'##molecule_type DNA !'##residues 1-194 ##label AFO !'##cross-references GB:M88336; NID:g210645; PIDN:AAA42729.1; !1PID:g210646 CLASSIFICATION #superfamily African swine fever virus P30 phosphoprotein KEYWORDS phosphoprotein FEATURE !$8,43,103,117,128 #binding_site phosphate (Ser) (covalent) #status !8predicted\ !$57,121 #binding_site phosphate (Thr) (covalent) #status !8predicted SUMMARY #length 194 #molecular-weight 22348 #checksum 9938 SEQUENCE /// ENTRY GNNY1P #type complete TITLE genome polyprotein (version 1) - human poliovirus 1 (strain Mahoney) CONTAINS coat protein VP1; coat protein VP2; coat protein VP3; coat protein VP4; core protein P2-3b; core protein P2-5b; core protein P2-X; genome-linked protein VPg; probable proteinase P3-7c; protein P3-1b; protein P3-2; RNA-directed RNA polymerase (EC 2.7.7.48) P3-4b ORGANISM #formal_name human poliovirus 1 DATE 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 16-Jul-1999 ACCESSIONS A93258; A90800; A03897 REFERENCE A93258 !$#authors Kitamura, N.; Semler, B.L.; Rothberg, P.G.; Larsen, G.R.; !1Adler, C.J.; Dorner, A.J.; Emini, E.A.; Hanecak, R.; Lee, !1J.J.; van der Werf, S.; Anderson, C.W.; Wimmer, E. !$#journal Nature (1981) 291:547-553 !$#title Primary structure, gene organization and polypeptide !1expression of poliovirus RNA. !$#cross-references MUID:81220953; PMID:6264310 !$#accession A93258 !'##molecule_type genomic RNA !'##residues 1-2207 ##label KIT1 !'##cross-references GB:V01148; NID:g61236; PIDN:CAA24446.1; PID:g61237 !'##note the amino acid sequence of VPg (residues 1543-1564) was also !1determined and agrees with that shown REFERENCE A90800 !$#authors Kitamura, N.; Adler, C.J.; Rothberg, P.G.; Martinko, J.; !1Nathenson, S.G.; Wimmer, E. !$#journal Cell (1980) 21:295-302 !$#title The genome-linked protein of picornaviruses. VII. Genetic !1mapping of poliovirus VPg by protein and RNA sequence !1studies. !$#cross-references MUID:81001866; PMID:6250717 !$#accession A90800 !'##molecule_type genomic RNA !'##residues 1539-1574 ##label KIT2 !'##note the amino end of VPg corresponds to residue 1543; a choice !1between the two potential carboxyl cleavage sites, after !1residue 1564 or 1569, could not be made; the partial !1sequence of this protein obtained by radiochemical !1microsequence analysis agrees with that predicted by the !1virion RNA REFERENCE A30637 !$#authors Rothberg, P.G.; Harris, T.J.; Nomoto, A.; Wimmer, E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1978) 75:4868-4872 !$#title O4-(5'-Uridylyl)tyrosine is the bond between the !1genome-linked protein and the RNA of poliovirus. !$#cross-references MUID:79116223; PMID:217003 !$#contents annotation; chemical characterization COMMENT VPg is linked by Tyr-1545 to the uridylate residue at the 5' !1end of the genome RNA. It is required to initiate RNA !1synthesis and it may also be involved in morphogenesis. COMMENT Coat proteins VP2 and VP3 and the RNA-directed RNA !1polymerase are related to their counterparts in !1foot-and-mouth disease virus. CLASSIFICATION #superfamily poliovirus genome polyprotein KEYWORDS genome-linked protein; nucleotidyltransferase; !1phosphoprotein; polyprotein FEATURE !$2-69 #product coat protein VP4 #status predicted #label !8VP4\ !$70-340 #product coat protein VP2 #status predicted #label !8VP2\ !$341-578 #product coat protein VP3 #status predicted #label !8VP3\ !$579-880 #product coat protein VP1 #status predicted #label !8VP1\ !$881-1455 #product core protein P2-3b #status predicted #label !8P23\ !$1030-1455 #product core protein P2-5b #status predicted #label !8P25\ !$1127-1455 #product core protein P2-X #status predicted #label !8P2X\ !$1456-2207 #product protein P3-1b #status predicted #label P31\ !$1543-1564 #product genome-linked protein VPg #status predicted !8#label VPG\ !$1565-2207 #product protein P3-2 #status predicted #label P32\ !$1565-1746 #product probable proteinase P3-7c #status predicted !8#label P37\ !$1747-2207 #product RNA-directed RNA polymerase P3-4b #status !8predicted #label P34\ !$1545 #binding_site phosphoryl-RNA (Tyr) (covalent) #status !8experimental SUMMARY #length 2207 #molecular-weight 246540 #checksum 7480 SEQUENCE /// ENTRY GNNY2P #type complete TITLE genome polyprotein (version 2) - human poliovirus 1 (strain Mahoney) ORGANISM #formal_name human poliovirus 1 DATE 18-Dec-1981 #sequence_revision 18-Dec-1981 #text_change 21-Jul-2000 ACCESSIONS A03898 REFERENCE A03898 !$#authors Racaniello, V.R.; Baltimore, D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:4887-4891 !$#title Molecular cloning of poliovirus cDNA and determination of !1the complete nucleotide sequence of the viral genome. !$#cross-references MUID:82060159; PMID:6272282 !$#accession A03898 !'##molecule_type genomic RNA !'##residues 1-2209 ##label RAC !'##cross-references GB:J02281; NID:g61252; PIDN:CAA24461.1; PID:g61253 !'##note the authors translated the codon TTC for residue 464 as Ser REFERENCE A30636 !$#authors Ambros, V.; Baltimore, D. !$#journal J. Biol. Chem. (1978) 253:5263-5266 !$#title Protein is linked to the 5' end of poliovirus RNA by a !1phosphodiester linkage to tyrosine. !$#cross-references MUID:78218195; PMID:209034 !$#contents annotation; chemical characterization CLASSIFICATION #superfamily poliovirus genome polyprotein KEYWORDS genome-linked protein; nucleotidyltransferase; !1phosphoprotein; polyprotein FEATURE !$2-69 #product coat protein VP4 #status predicted #label !8VP4\ !$70-341 #product coat protein VP2 #status predicted #label !8VP2\ !$342-579 #product coat protein VP3 #status predicted #label !8VP3\ !$580-881 #product coat protein VP1 #status predicted #label !8VP1\ !$882-1456 #product core protein P2-3b #status predicted #label !8P23\ !$1031-1456 #product core protein P2-5b #status predicted #label !8P25\ !$1128-1456 #product core protein P2-X #status predicted #label !8P2X\ !$1457-2209 #product protein P3-1b #status predicted #label P31\ !$1544-1565 #product genome-linked protein VPg #status predicted !8#label VPG\ !$1566-2209 #product protein P3-2 #status predicted #label P32\ !$1566-1748 #product probable proteinase P3-7c #status predicted !8#label P37\ !$1749-2209 #product RNA-directed RNA polymerase P3-4b #status !8predicted #label P34\ !$1546 #binding_site phosphoryl-RNA (Tyr) (covalent) #status !8experimental SUMMARY #length 2209 #molecular-weight 246538 #checksum 7583 SEQUENCE /// ENTRY GNNY3P #type complete TITLE genome polyprotein - human poliovirus 1 (strain Sabin) ORGANISM #formal_name human poliovirus 1 DATE 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 16-Jul-1999 ACCESSIONS A03899 REFERENCE A03899 !$#authors Nomoto, A.; Omata, T.; Toyoda, H.; Kuge, S.; Horie, H.; !1Kataoka, Y.; Genba, Y.; Nakano, Y.; Imura, N. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:5793-5797 !$#title Complete nucleotide sequence of the attenuated poliovirus !1Sabin 1 strain genome. !$#cross-references MUID:83299876; PMID:6310545 !$#accession A03899 !'##molecule_type genomic RNA !'##residues 1-2209 ##label NOM !'##cross-references GB:V01150; GB:J02282; GB:J02285; GB:J02286; !1GB:V01133; NID:g61257; PIDN:CAA24465.1; PID:g61258 !'##note this virus is a live vaccine strain derived from the Mahoney !1strain by spontaneous mutations during the attenuation !1process CLASSIFICATION #superfamily poliovirus genome polyprotein KEYWORDS genome-linked protein; phosphoprotein; polyprotein FEATURE !$2-69 #product coat protein VP4 #status predicted #label !8VP4\ !$70-341 #product coat protein VP2 #status predicted #label !8VP2\ !$342-579 #product coat protein VP3 #status predicted #label !8VP3\ !$580-881 #product coat protein VP1 #status predicted #label !8VP1\ !$882-1456 #product core protein P2-3b #status predicted #label !8P23\ !$1031-1456 #product core protein P2-5b #status predicted #label !8P25\ !$1128-1456 #product core protein P2-X #status predicted #label !8P2X\ !$1457-2209 #product protein P3-1b #status predicted #label P31\ !$1544-1565 #product genome-linked protein VPg #status predicted !8#label VPG\ !$1566-2209 #product protein P3-2 #status predicted #label P32\ !$1566-1748 #product probable proteinase P3-7c #status predicted !8#label P37\ !$1749-2209 #product RNA-directed RNA polymerase P3-4b #status !8predicted #label P34\ !$1546 #binding_site phosphoryl-RNA (Tyr) (covalent) #status !8predicted SUMMARY #length 2209 #molecular-weight 246576 #checksum 5033 SEQUENCE /// ENTRY GNNY5P #type complete TITLE genome polyprotein - human poliovirus 2 (strain Lansing) CONTAINS coat protein VP1; coat protein VP2; coat protein VP3; coat protein VP4; genome-linked protein VPg; nonstructural protein 2B; nonstructural protein 2C; nonstructural protein 3A; proteinase (EC 3.4.-.-) 2A; proteinase (EC 3.4.-.-) 3C; RNA-directed RNA polymerase (EC 2.7.7.48) 3D ORGANISM #formal_name human poliovirus 2 DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jul-1999 ACCESSIONS A29507 REFERENCE A29507 !$#authors La Monica, N.; Meriam, C.; Racaniello, V.R. !$#journal J. Virol. (1986) 57:515-525 !$#title Mapping of sequences required for mouse neurovirulence of !1poliovirus type 2 Lansing. !$#cross-references MUID:86115399; PMID:3003384 !$#accession A29507 !'##molecule_type genomic RNA !'##residues 1-2207 ##label LAM !'##cross-references GB:M12197; NID:g332890; PIDN:AAA46912.1; !1PID:g332891 CLASSIFICATION #superfamily poliovirus genome polyprotein KEYWORDS coat protein; genome-linked protein; hydrolase; !1nonstructural protein; nucleotidyltransferase; !1phosphoprotein; polyprotein; proteinase FEATURE !$1-69 #product coat protein VP4 #status predicted #label !8VP4\ !$70-340 #product coat protein VP2 #status predicted #label !8VP2\ !$341-578 #product coat protein VP3 #status predicted #label !8VP3\ !$579-879 #product coat protein VP1 #status predicted #label !8VP1\ !$880-1028 #product proteinase 2A #status predicted #label P2A\ !$1029-1125 #product nonstructural protein 2B #status predicted !8#label N2B\ !$1126-1454 #product nonstructural protein 2C #status predicted !8#label N2C\ !$1455-1541 #product nonstructural protein 3A #status predicted !8#label N3A\ !$1542-1563 #product genome-linked protein VPg #status predicted !8#label VPG\ !$1564-1746 #product proteinase 3C #status predicted #label P3C\ !$1747-2207 #product RNA-directed RNA polymerase #status !8predicted #label RRP\ !$1544 #binding_site phosphoryl-RNA (Tyr) (covalent) #status !8predicted SUMMARY #length 2207 #molecular-weight 245829 #checksum 666 SEQUENCE /// ENTRY GNNY2W #type complete TITLE genome polyprotein - human poliovirus 2 (strain W-2) CONTAINS coat protein 1A; coat protein 1B; coat protein 1C; coat protein 1D; genome-linked protein VPg; nonstructural protein 2B; nonstructural protein 2C; nonstructural protein 3A; proteinase 2A; proteinase 3C; RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name human poliovirus 2 DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 05-Jun-1998 ACCESSIONS A34032 REFERENCE A34032 !$#authors Pevear, D.C.; Oh, C.K.; Cunningham, L.L.; Calenoff, M.; !1Jubelt, B. !$#journal J. Gen. Virol. (1990) 71:43-52 !$#title Localization of genomic regions specific for the attenuated, !1mouse-adapted poliovirus type 2 strain W-2. !$#cross-references MUID:90155230; PMID:2154539 !$#accession A34032 !'##molecule_type genomic RNA !'##residues 1-2205 ##label PEV CLASSIFICATION #superfamily poliovirus genome polyprotein KEYWORDS coat protein; genome-linked protein; nonstructural protein; !1nucleotidyltransferase; phosphoprotein; polyprotein; !1proteinase FEATURE !$1-69 #product coat protein 1A #status predicted #label !8VP4\ !$70-340 #product coat protein 1B #status predicted #label !8VP2\ !$341-578 #product coat protein 1C #status predicted #label !8VP3\ !$579-879 #product coat protein 1D #status predicted #label !8VP1\ !$880-1028 #product proteinase 2A #status predicted #label P2A\ !$1029-1125 #product nonstructural protein 2B #status predicted !8#label P2B\ !$1126-1454 #product nonstructural protein 2C #status predicted !8#label P2C\ !$1455-1541 #product nonstructural protein 3A #status predicted !8#label P3A\ !$1542-1563 #product genome-linked protein VPg #status predicted !8#label VPG\ !$1564-1746 #product proteinase 3C #status predicted #label P3C\ !$1747-2205 #product RNA-directed RNA polymerase #status !8predicted #label RRP\ !$1544 #binding_site phosphoryl-RNA (Tyr) (covalent) #status !8predicted SUMMARY #length 2205 #molecular-weight 245701 #checksum 6218 SEQUENCE /// ENTRY GNNY4P #type complete TITLE genome polyprotein - human poliovirus 3 (strain Sabin vaccine P3/Leon/37, P3/Leon/12a[1]b) CONTAINS coat protein VP1; coat protein VP2; coat protein VP3; coat protein VP4; core protein P2-3b; core protein P2-5b; core protein P2-X; genome-linked protein VPg; probable proteinase P3-7c; protein P3-1b; protein P3-2; RNA-directed RNA polymerase (EC 2.7.7.48) P3-4b ORGANISM #formal_name human poliovirus 3 DATE 19-Feb-1984 #sequence_revision 03-Aug-1984 #text_change 16-Jul-1999 ACCESSIONS A93987; A93484; S42524; A03900 REFERENCE A93987 !$#authors Stanway, G.; Hughes, P.J.; Mountford, R.C.; Reeve, P.; !1Minor, P.D.; Schild, G.C.; Almond, J.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:1539-1543 !$#title Comparison of the complete nucleotide sequences of the !1genomes of the neurovirulent poliovirus P3/Leon/37 and its !1attenuated Sabin vaccine derivative P3/Leon 12a-1b. !$#cross-references MUID:84170338; PMID:6324200 !$#accession A93987 !'##molecule_type genomic RNA !'##residues 1-2206 ##label ST1 !'##cross-references GB:K01392; NID:g332895; PIDN:AAA46914.1; !1PID:g332896 !'##experimental_source strain Sabin vaccine P3/Leon/37 !'##note the strain Sabin vaccine P3/Leon/37 is the progenitor of the !1strain Sabin vaccine p3/Leon 12a[1]b !'##note the authors translated the codon GAU for residue 497 as Gly REFERENCE A93484 !$#authors Stanway, G.; Cann, A.J.; Hauptmann, R.; Hughes, P.; Clarke, !1L.D.; Mountford, R.C.; Minor, P.D.; Schild, G.C.; Almond, !1J.W. !$#journal Nucleic Acids Res. (1983) 11:5629-5643 !$#title The nucleotide sequence of poliovirus type 3 lon 12 a-1b: !1comparison with poliovirus type 1. !$#cross-references MUID:83299239; PMID:6310508 !$#accession A93484 !'##molecule_type genomic RNA !'##residues 1-430,'F',432-863,'R',865-907,'A',909-2206 ##label ST2 !'##cross-references GB:X00925; GB:K00043; NID:g61154; PIDN:CAA25444.1; !1PID:g61155 !'##experimental_source strain Sabin vaccine P3/Leon 12a[1]b !'##note the authors translated the codon GAU for residue 497 as Gly REFERENCE S42524 !$#authors Stanway, G.; Cann, A.J.; Hauptmann, R.; Mountford, R.C.; !1Clarke, L.D.; Reeve, P.; Minor, P.D.; Schild, G.C.; Almond, !1J.W. !$#journal Eur. J. Biochem. (1983) 135:529-533 !$#title Nucleic acid sequence of the region of the genome encoding !1capsid protein VP1 of neurovirulent and attenuated type 3 !1polioviruses. !$#cross-references MUID:84004370; PMID:6311539 !$#accession S42524 !'##molecule_type genomic RNA !'##residues 579-878 ##label STA !'##cross-references EMBL:V01540; NID:g61153; PIDN:CAA24780.1; !1PID:g929811 !'##experimental_source strain Sabin vaccine P3/Leon/37 COMMENT Coat proteins VP2 and VP3 and the RNA-directed RNA !1polymerase are related to their counterparts in !1foot-and-mouth disease virus. CLASSIFICATION #superfamily poliovirus genome polyprotein KEYWORDS genome-linked protein; nucleotidyltransferase; !1phosphoprotein FEATURE !$2-69 #product coat protein VP4 #status predicted #label !8VP4\ !$70-340 #product coat protein VP2 #status predicted #label !8VP2\ !$341-578 #product coat protein VP3 #status predicted #label !8VP3\ !$579-878 #product coat protein VP1 #status predicted #label !8VP1\ !$879-1453 #product core protein P2-3b #status predicted #label !8P23\ !$1027-1453 #product core protein P2-5b #status predicted #label !8P25\ !$1124-1453 #product core protein P2-X #status predicted #label !8P2X\ !$1454-2206 #product protein P3-1b #status predicted #label P31\ !$1541-1562 #product genome-linked protein VPg #status predicted !8#label VPG\ !$1563-2206 #product protein P3-2 #status predicted #label P32\ !$1563-1745 #product probable proteinase P3-7c #status predicted !8#label P37\ !$1746-2206 #product RNA-directed RNA polymerase P3-4b #status !8predicted #label P34\ !$1543 #binding_site phosphoryl-RNA (Tyr) (covalent) #status !8predicted SUMMARY #length 2206 #molecular-weight 246163 #checksum 7111 SEQUENCE /// ENTRY GNNY27 #type complete TITLE genome polyprotein - human poliovirus 3 (strain 23127) CONTAINS coat protein VP1; coat protein VP2; coat protein VP3; coat protein VP4; core protein P2-3b; core protein P2-5b; core protein P2-X; genome-linked protein VPg; protein P3-1b; proteinase; RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name human poliovirus 3 DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 16-Jul-1999 ACCESSIONS A27245 REFERENCE A27245 !$#authors Hughes, P.J.; Evans, D.M.A.; Minor, P.D.; Schild, G.C.; !1Almond, J.W.; Stanway, G. !$#journal J. Gen. Virol. (1986) 67:2093-2102 !$#title The nucleotide sequence of a type 3 poliovirus isolated !1during a recent outbreak of poliomyelitis in Finland. !$#cross-references MUID:87010550; PMID:3020156 !$#accession A27245 !'##molecule_type genomic RNA !'##residues 1-2206 ##label HUG !'##cross-references GB:X04468; NID:g61112; PIDN:CAA28155.1; PID:g61113 CLASSIFICATION #superfamily poliovirus genome polyprotein KEYWORDS coat protein; core protein; genome-linked protein; !1nucleotidyltransferase; phosphoprotein; polyprotein; !1proteinase FEATURE !$1-69 #product coat protein VP4 #status predicted #label !8VP4\ !$70-340 #product coat protein VP2 #status predicted #label !8VP2\ !$341-578 #product coat protein VP3 #status predicted #label !8VP3\ !$579-878 #product coat protein VP1 #status predicted #label !8VP1\ !$879-1027 #product core protein P2-3b #status predicted #label !8P3B\ !$1028-1124 #product core protein P2-5b #status predicted #label !8P5B\ !$1125-1453 #product core protein P2-X #status predicted #label !8P2X\ !$1454-1540 #product protein P3-1b #status predicted #label P1B\ !$1541-1562 #product genome-linked protein VPg #status predicted !8#label VPG\ !$1563-1745 #product proteinase #status predicted #label PTS\ !$1746-2206 #product RNA-directed RNA polymerase #status !8predicted #label RNS\ !$1543 #binding_site phosphoryl-RNA (Tyr) (covalent) #status !8predicted SUMMARY #length 2206 #molecular-weight 245731 #checksum 265 SEQUENCE /// ENTRY GNNY21 #type complete TITLE genome polyprotein - coxsackievirus A21 (strain Coe) CONTAINS coat protein 1A; coat protein 1B; coat protein 1C; coat protein 1D; core protein 2A; core protein 2B; core protein 2C; genome-linked protein VPg; protein 3A; proteinase; RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name coxsackievirus A21 DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jun-2000 ACCESSIONS A33373 REFERENCE A33373 !$#authors Hughes, P.J.; North, C.; Minor, P.D.; Stanway, G. !$#journal J. Gen. Virol. (1989) 70:2943-2952 !$#title The complete nucleotide sequence of coxsackievirus A21. !$#cross-references MUID:90063544; PMID:2584950 !$#accession A33373 !'##molecule_type genomic RNA !'##residues 1-2206 ##label HUG !'##cross-references GB:D00538; NID:g221147; PIDN:BAA00426.1; !1PID:g221148 CLASSIFICATION #superfamily poliovirus genome polyprotein KEYWORDS coat protein; core protein; genome-linked protein; !1nucleotidyltransferase; phosphoprotein; polyprotein; !1proteinase FEATURE !$1-69 #product coat protein 1A #status predicted #label !8VP4\ !$70-341 #product coat protein 1B #status predicted #label !8VP2\ !$342-578 #product coat protein 1C #status predicted #label !8VP3\ !$579-881 #product coat protein 1D #status predicted #label !8VP1\ !$882-1028 #product core protein 2A #status predicted #label !8PA2\ !$1029-1125 #product core protein 2B #status predicted #label !8PB2\ !$1126-1453 #product core protein 2C #status predicted #label !8PC2\ !$1454-1540 #product protein 3A #status predicted #label PA3\ !$1541-1562 #product genome-linked protein VPg #status predicted !8#label PB3\ !$1563-1745 #product proteinase #status predicted #label PC3\ !$1746-2206 #product RNA-directed RNA polymerase #status !8predicted #label PD3\ !$1543 #binding_site phosphoryl-RNA (Tyr) (covalent) #status !8predicted SUMMARY #length 2206 #molecular-weight 246049 #checksum 3669 SEQUENCE /// ENTRY A48548 #type complete TITLE genome polyprotein - coxsackievirus A24 (strain EH24/70) CONTAINS coat protein 1A; coat protein 1B; coat protein 1C; coat protein 1D; core protein 2A; core protein 2B; core protein 2C; genome-linked protein VPg; protein 3A; proteinase; RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name coxsackievirus A24 DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 05-Jun-1998 ACCESSIONS A48548 REFERENCE A48548 !$#authors Supanaranond, K.; Takeda, N.; Yamazaki, S. !$#journal Virus Genes (1992) 6:149-158 !$#title The complete nucleotide sequence of a variant of !1Coxsackievirus A24, an agent causing acute hemorrhagic !1conjunctivitis. !$#cross-references MUID:92271460; PMID:1317075 !$#accession A48548 !'##molecule_type genomic RNA !'##residues 1-2214 ##label SUP !'##note sequence extracted from NCBI backbone (NCBIN:104525, !1NCBIP:104526) CLASSIFICATION #superfamily poliovirus genome polyprotein KEYWORDS coat protein; core protein; genome-linked protein; !1nucleotidyltransferase; phosphoprotein; polyprotein; !1proteinase FEATURE !$1-69 #product coat protein 1A #status predicted #label !8VP4\ !$70-340 #product coat protein 1B #status predicted #label !8VP2\ !$341-577 #product coat protein 1C #status predicted #label !8VP3\ !$578-888 #product coat protein 1D #status predicted #label !8VP1\ !$889-1035 #product core protein 2A #status predicted #label !8PA2\ !$1036-1132 #product core protein 2B #status predicted #label !8PB2\ !$1133-1461 #product core protein 2C #status predicted #label !8PC2\ !$1462-1548 #product protein 3A #status predicted #label PA3\ !$1549-1570 #product genome-linked protein VPg #status predicted !8#label PB3\ !$1571-1753 #product proteinase #status predicted #label PC3\ !$1754-2214 #product RNA-directed RNA polymerase #status !8predicted #label PD3\ !$1551 #binding_site phosphoryl-RNA (Tyr) (covalent) #status !8predicted SUMMARY #length 2214 #molecular-weight 247212 #checksum 7748 SEQUENCE /// ENTRY GNNYH4 #type complete TITLE genome polyprotein - human rhinovirus 14 CONTAINS coat protein VP1; coat protein VP2; coat protein VP3; coat protein VP4; core protein P2-A; core protein P2-B; core protein P2-C; core protein P3-A; genome-linked protein VPg; proteinase; RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name human rhinovirus 14 DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 05-Jun-1998 ACCESSIONS A03901 REFERENCE A03901 !$#authors Stanway, G.; Hughes, P.J.; Mountford, R.C.; Minor, P.D.; !1Almond, J.W. !$#journal Nucleic Acids Res. (1984) 12:7859-7875 !$#title The complete nucleotide sequence of a common cold virus: !1human rhinovirus 14. !$#cross-references MUID:85037949; PMID:6093056 !$#accession A03901 !'##molecule_type genomic RNA !'##residues 1-2179 ##label STA CLASSIFICATION #superfamily poliovirus genome polyprotein KEYWORDS genome-linked protein; nucleotidyltransferase; !1phosphoprotein FEATURE !$1-69 #product coat protein VP4 #status predicted #label !8VP4\ !$70-331 #product coat protein VP2 #status predicted #label !8VP2\ !$332-567 #product coat protein VP3 #status predicted #label !8VP3\ !$568-856 #product coat protein VP1 #status predicted #label !8VP1\ !$857-1002 #product core protein P2-A #status predicted #label !8P2A\ !$1003-1099 #product core protein P2-B #status predicted #label !8P2B\ !$1100-1429 #product core protein P2-C #status predicted #label !8P2C\ !$1430-1514 #product core protein P3-A #status predicted #label !8P3A\ !$1515-1537 #product genome-linked protein VPg #status predicted !8#label VPG\ !$1538-1719 #product proteinase #status predicted #label PRT\ !$1720-2179 #product RNA-directed RNA polymerase #status !8predicted #label RNA\ !$1517 #binding_site phosphoryl-RNA (Tyr) (covalent) #status !8predicted SUMMARY #length 2179 #molecular-weight 242989 #checksum 5096 SEQUENCE /// ENTRY GNNYH2 #type complete TITLE genome polyprotein - human rhinovirus 2 CONTAINS coat protein VP1; coat protein VP2; coat protein VP3; coat protein VP4; core protein P2-A; core protein P2-B; core protein P2-C; core protein P3-A; genome-linked protein VPg; proteinase; RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name human rhinovirus 2 DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 05-Jun-1998 ACCESSIONS A03902 REFERENCE A03902 !$#authors Skern, T.; Sommergruber, W.; Blaas, D.; Gruendler, P.; !1Fraundorfer, F.; Pieler, C.; Fogy, I.; Kuechler, E. !$#journal Nucleic Acids Res. (1985) 13:2111-2126 !$#title Human rhinovirus 2: complete nucleotide sequence and !1proteolytic processing signals in the capsid protein region. !$#cross-references MUID:85215603; PMID:2987843 !$#accession A03902 !'##molecule_type genomic RNA !'##residues 1-2150 ##label SKE CLASSIFICATION #superfamily poliovirus genome polyprotein KEYWORDS coat protein; core protein; genome-linked protein; !1nucleotidyltransferase; phosphoprotein; polyprotein; !1proteinase FEATURE !$1-69 #product coat protein VP4 #status predicted #label !8VP4\ !$70-330 #product coat protein VP2 #status predicted #label !8VP2\ !$331-567 #product coat protein VP3 #status predicted #label !8VP3\ !$568-856 #product coat protein VP1 #status predicted #label !8VP1\ !$857-992 #product core protein P2-A #status predicted #label !8P2A\ !$993-1087 #product core protein P2-B #status predicted #label !8P2B\ !$1088-1409 #product core protein P2-C #status predicted #label !8P2C\ !$1410-1486 #product core protein P3-A #status predicted #label !8P3A\ !$1487-1507 #product genome-linked protein VPg #status predicted !8#label VPG\ !$1508-1690 #product proteinase #status predicted #label PTS\ !$1691-2150 #product RNA-directed RNA polymerase #status !8predicted #label RAS\ !$1489 #binding_site phosphoryl-RNA (Tyr) (covalent) #status !8predicted SUMMARY #length 2150 #molecular-weight 241948 #checksum 9941 SEQUENCE /// ENTRY GNNY1B #type complete TITLE genome polyprotein - human rhinovirus 1B CONTAINS coat protein VP1; coat protein VP2; coat protein VP3; coat protein VP4; core protein P2-A; core protein P2-B; core protein P2-C; core protein P3-A; genome-linked protein VPg; proteinase; RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name human rhinovirus 1B #note host Homo sapiens (man) DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jun-2000 ACCESSIONS A28699 REFERENCE A28699 !$#authors Hughes, P.J.; North, C.; Jellis, C.H.; Minor, P.D.; Stanway, !1G. !$#journal J. Gen. Virol. (1988) 69:49-58 !$#title The nucleotide sequence of human rhinovirus 1B: molecular !1relationships within the rhinovirus genus. !$#cross-references MUID:88089537; PMID:2826669 !$#accession A28699 !'##molecule_type genomic RNA !'##residues 1-2157 ##label HUG !'##cross-references GB:D00239; NID:g221708; PIDN:BAA00168.1; !1PID:g221709 CLASSIFICATION #superfamily poliovirus genome polyprotein KEYWORDS coat protein; core protein; genome-linked protein; !1nucleotidyltransferase; phosphoprotein; proteinase FEATURE !$1-69 #product coat protein VP4 #status predicted #label !8VP4\ !$70-332 #product coat protein VP2 #status predicted #label !8VP2\ !$333-570 #product coat protein VP3 #status predicted #label !8VP3\ !$571-857 #product coat protein VP1 #status predicted #label !8VP1\ !$858-999 #product core protein P2-A #status predicted #label !8P2A\ !$1000-1094 #product core protein P2-B #status predicted #label !8P2B\ !$1095-1416 #product core protein P2-C #status predicted #label !8P2C\ !$1417-1493 #product core protein P3-A #status predicted #label !8P3A\ !$1494-1514 #product genome-linked protein VPg #status predicted !8#label VPG\ !$1515-1697 #product proteinase #status predicted #label PTS\ !$1698-2157 #product RNA-directed RNA polymerase #status !8predicted #label RNS\ !$1496 #binding_site phosphoryl-RNA (Tyr) (covalent) #status !8predicted SUMMARY #length 2157 #molecular-weight 242313 #checksum 3785 SEQUENCE /// ENTRY GNNY89 #type complete TITLE genome polyprotein - human rhinovirus 89 CONTAINS coat protein VP1; coat protein VP2; coat protein VP3; coat protein VP4; core protein P2-A; core protein P2-B; core protein P2-C; core protein P3-A; genome-linked protein VPg; proteinase; RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name human rhinovirus 89 DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jul-1999 ACCESSIONS A29862 REFERENCE A29862 !$#authors Duechler, M.; Skern, T.; Sommergruber, W.; Neubauer, C.; !1Gruendler, P.; Fogy, I.; Blaas, D.; Kuechler, E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:2605-2609 !$#title Evolutionary relationships within the human rhinovirus !1genus: comparison of serotypes 89, 2, and 14. !$#cross-references MUID:87204179; PMID:3033653 !$#accession A29862 !'##molecule_type genomic RNA !'##residues 1-2164 ##label DUE !'##cross-references GB:M16248; NID:g330039; PIDN:AAA45762.1; !1PID:g330040 CLASSIFICATION #superfamily poliovirus genome polyprotein KEYWORDS coat protein; core protein; genome-linked protein; !1nucleotidyltransferase; phosphoprotein; proteinase FEATURE !$1-69 #product coat protein VP4 #status predicted #label !8VP4\ !$70-536 #product coat protein VP2 #status predicted #label !8VP2\ !$537-574 #product coat protein VP3 #status predicted #label !8VP3\ !$575-872 #product coat protein VP1 #status predicted #label !8VP1\ !$873-1008 #product core protein P2-A #status predicted #label !8P2A\ !$1009-1103 #product core protein P2-B #status predicted #label !8P2B\ !$1104-1424 #product core protein P2-C #status predicted #label !8P2C\ !$1425-1500 #product core protein P3-A #status predicted #label !8P3A\ !$1501-1521 #product genome-linked protein VPg #status predicted !8#label VPG\ !$1522-1704 #product proteinase #status predicted #label PTS\ !$1705-2164 #product RNA-directed RNA polymerase #status !8predicted #label PMS\ !$1503 #binding_site phosphoryl-RNA (Tyr) (covalent) #status !8predicted SUMMARY #length 2164 #molecular-weight 241063 #checksum 8810 SEQUENCE /// ENTRY GNNYB3 #type complete TITLE genome polyprotein - coxsackievirus B3 (strain Nancy) CONTAINS coat protein VP1; coat protein VP2; coat protein VP3; coat protein VP4; core protein P2-A; core protein P2-B; core protein P2-C; core protein P3-A; genome-linked protein VPg; proteinase (EC 3.4.-.-); RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name coxsackievirus B3 #note host Homo sapiens (man) DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 05-Jun-1998 ACCESSIONS A26354; B00725 REFERENCE A26354 !$#authors Lindberg, A.M.; Stalhandske, P.O.K.; Pettersson, U. !$#journal Virology (1987) 156:50-63 !$#title Genome of coxsackievirus B3. !$#cross-references MUID:87122156; PMID:3027968 !$#accession A26354 !'##molecule_type genomic RNA !'##residues 1-2185 ##label LIN !'##cross-references GB:K02709 REFERENCE A00725 !$#authors Stalhandske, P.O.K.; Lindberg, M.; Pettersson, U. !$#journal J. Virol. (1984) 51:742-746 !$#title Replicase gene of coxsackievirus B3. !$#cross-references MUID:84292451; PMID:6088796 !$#accession B00725 !'##molecule_type genomic RNA !'##residues 1724-1733,'D',1735-2185 ##label STA !'##cross-references GB:M16572 CLASSIFICATION #superfamily poliovirus genome polyprotein KEYWORDS coat protein; core protein; genome-linked protein; !1hydrolase; nucleotidyltransferase; phosphoprotein; !1polyprotein; proteinase FEATURE !$1-69 #product coat protein VP4 #status predicted #label !8VP4\ !$70-332 #product coat protein VP2 #status predicted #label !8VP2\ !$333-570 #product coat protein VP3 #status predicted #label !8VP3\ !$571-880 #product coat protein VP1 #status predicted #label !8VP1\ !$881-1001 #product core protein P2-A #status predicted #label !8P2A\ !$1002-1100 #product core protein P2-B #status predicted #label !8P2B\ !$1101-1429 #product core protein P2-C #status predicted #label !8P2C\ !$1430-1518 #product core protein P3-A #status predicted #label !8P3A\ !$1519-1540 #product genome-linked protein VPg #status predicted !8#label VPG\ !$1541-1723 #product proteinase #status predicted #label PTS\ !$1724-2185 #product RNA-directed RNA polymerase #status !8predicted #label RNS\ !$1521 #binding_site phosphoryl-RNA (Tyr) (covalent) #status !8predicted SUMMARY #length 2185 #molecular-weight 243189 #checksum 9443 SEQUENCE /// ENTRY GNNYBT #type complete TITLE genome polyprotein - coxsackievirus B3 CONTAINS coat protein 1A; coat protein 1B; coat protein 1C; coat protein 1D; core protein 2A; core protein 2B; core protein 2C; genome-linked protein VPg; protein 3A; proteinase; RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name coxsackievirus B3 DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS A34664 REFERENCE A34664 !$#authors Klump, W.M.; Bergmann, I.; Mueller, B.C.; Ameis, D.; !1Kandolf, R. !$#journal J. Virol. (1990) 64:1573-1583 !$#title Complete nucleotide sequence of infectious coxsackievirus B3 !1cDNA: two initial 5' uridine residues are regained during !1plus-strand RNA synthesis. !$#cross-references MUID:90204667; PMID:2157045 !$#accession A34664 !'##molecule_type genomic RNA !'##residues 1-2185 ##label KLU !'##cross-references GB:M33854; NID:g323419; PIDN:AAA42931.1; !1PID:g323420 CLASSIFICATION #superfamily poliovirus genome polyprotein KEYWORDS coat protein; core protein; genome-linked protein; !1nucleotidyltransferase; phosphoprotein; proteinase FEATURE !$1-69 #product coat protein 1A #status predicted #label !8VP4\ !$70-332 #product coat protein 1B #status predicted #label !8VP2\ !$333-570 #product coat protein 1C #status predicted #label !8VP3\ !$571-880 #product coat protein 1D #status predicted #label !8VP1\ !$881-1001 #product core protein 2A #status predicted #label !8PA2\ !$1002-1100 #product core protein 2B #status predicted #label !8PB2\ !$1101-1429 #product core protein 2C #status predicted #label !8PC2\ !$1430-1518 #product protein 3A #status predicted #label PA3\ !$1519-1540 #product genome-linked protein VPg #status predicted !8#label PB3\ !$1541-1723 #product proteinase #status predicted #label PC3\ !$1724-2185 #product RNA-directed RNA polymerase #status !8predicted #label PD3\ !$1521 #binding_site phosphoryl-RNA (Tyr) (covalent) #status !8predicted SUMMARY #length 2185 #molecular-weight 243451 #checksum 7699 SEQUENCE /// ENTRY GNNYB1 #type complete TITLE genome polyprotein - coxsackievirus B1 CONTAINS coat protein 1A; coat protein 1B; coat protein 1C; coat protein 1D; core protein 2A; core protein 2B; core protein 2C; genome-linked protein VPg; protein 3A; proteinase; RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name coxsackievirus B1 DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS A26353 REFERENCE A26353 !$#authors Iizuka, N.; Kuge, S.; Nomoto, A. !$#journal Virology (1987) 156:64-73 !$#title Complete nucleotide sequence of the genome of coxsackievirus !1B1. !$#cross-references MUID:87122157; PMID:3027969 !$#accession A26353 !'##molecule_type genomic RNA !'##residues 1-2182 ##label IIZ !'##cross-references GB:M16560; NID:g323417; PIDN:AAC00531.1; !1PID:g323418 CLASSIFICATION #superfamily poliovirus genome polyprotein KEYWORDS coat protein; core protein; genome-linked protein; !1nucleotidyltransferase; phosphoprotein; polyprotein; !1proteinase FEATURE !$1-69 #product coat protein 1A #status predicted #label !8P1A\ !$70-332 #product coat protein 1B #status predicted #label !8P1B\ !$333-570 #product coat protein 1C #status predicted #label !8P1C\ !$571-848 #product coat protein 1D #status predicted #label !8P1D\ !$849-998 #product core protein 2A #status predicted #label !8C2A\ !$999-1097 #product core protein 2B #status predicted #label !8C2B\ !$1098-1426 #product core protein 2C #status predicted #label !8C2C\ !$1427-1515 #product protein 3A #status predicted #label P3A\ !$1516-1537 #product genome-linked protein VPg #status predicted !8#label VPG\ !$1538-1720 #product proteinase #status predicted #label PTS\ !$1721-2182 #product RNA-directed RNA polymerase #status !8predicted #label RNS\ !$1518 #binding_site phosphoryl-RNA (Tyr) (covalent) #status !8predicted SUMMARY #length 2182 #molecular-weight 243945 #checksum 4153 SEQUENCE /// ENTRY GNNYB4 #type complete TITLE genome polyprotein - coxsackievirus B4 CONTAINS coat protein 1A; coat protein 1B; coat protein 1C; coat protein 1D; core protein 2A; core protein 2B; core protein 2C; genome-linked protein VPg; protein 3A; proteinase; RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name coxsackievirus B4 DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 16-Jul-1999 ACCESSIONS A27170; A45576; B45576 REFERENCE A27170 !$#authors Jenkins, O.; Booth, J.D.; Minor, P.D.; Almond, J.W. !$#journal J. Gen. Virol. (1987) 68:1835-1848 !$#title The complete nucleotide sequence of coxsackievirus B4 and !1its comparison to other members of the Picornaviridae. !$#cross-references MUID:87253111; PMID:3037008 !$#accession A27170 !'##molecule_type genomic RNA !'##residues 1-2183 ##label JEN REFERENCE A45576 !$#authors Ramsingh, A.; Araki, H.; Bryant, S.; Hixson, A. !$#journal Virus Res. (1992) 23:281-292 !$#title Identification of candidate sequences that determine !1virulence in Coxsackievirus B4. !$#cross-references MUID:92327833; PMID:1320798 !$#accession A45576 !'##molecule_type genomic RNA !'##residues 569-696,'T',698-852 ##label RAM !'##cross-references GB:S39291; NID:g250908; PIDN:AAB22445.1; !1PID:g250909 !'##experimental_source B4, virulent strain !'##note sequence inconsistent with the nucleotide translation !'##note sequence extracted from NCBI backbone (NCBIN:108105, !1NCBIP:108106) !$#accession B45576 !'##molecule_type genomic RNA !'##residues 70-203,'A',205-231,'E',233-269,'A',271-330 ##label RA2 !'##cross-references GB:S39291; NID:g250908; PIDN:AAB22446.1; !1PID:g250910 !'##experimental_source B4, virulent strain !'##note sequence extracted from NCBI backbone (NCBIN:108105, !1NCBIP:108107) CLASSIFICATION #superfamily poliovirus genome polyprotein KEYWORDS coat protein; core protein; genome-linked protein; !1nucleotidyltransferase; phosphoprotein; polyprotein; !1proteinase FEATURE !$1-69 #product coat protein 1A #status predicted #label !8C1A\ !$70-330 #product coat protein 1B #status predicted #label !8C1B\ !$331-568 #product coat protein 1C #status predicted #label !8C1C\ !$569-852 #product coat protein 1D #status predicted #label !8C1D\ !$853-999 #product core protein 2A #status predicted #label !8C2A\ !$1000-1098 #product core protein 2B #status predicted #label !8C2B\ !$1099-1427 #product core protein 2C #status predicted #label !8C2C\ !$1428-1516 #product protein 3A #status predicted #label P3A\ !$1517-1538 #product genome-linked protein VPg #status predicted !8#label VPG\ !$1539-1721 #product proteinase #status predicted #label PTS\ !$1722-2183 #product RNA-directed RNA polymerase #status !8predicted #label RPS\ !$1519 #binding_site phosphoryl-RNA (Tyr) (covalent) #status !8predicted SUMMARY #length 2183 #molecular-weight 243958 #checksum 474 SEQUENCE /// ENTRY JQ2021 #type complete TITLE genome polyprotein - coxsackievirus B5 (strain 1954/UK/85) CONTAINS coat protein 1A; coat protein 1B; coat protein 1C; coat protein 1D; core protein 2A; core protein 2B; core protein 2C; genome-linked protein VPg; protein 3A; proteinase; RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name coxsackievirus B5 DATE 24-Feb-1994 #sequence_revision 24-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS JQ2021 REFERENCE JQ2021 !$#authors Zhang, G.; Wilsden, G.; Knowles, N.J.; McCauley, J.W. !$#journal J. Gen. Virol. (1993) 74:845-853 !$#title Complete nucleotide sequence of a coxsackie B5 virus and its !1relationship to swine vesicular disease virus. !$#cross-references MUID:93260398; PMID:8388019 !$#accession JQ2021 !'##molecule_type genomic RNA !'##residues 1-2185 ##label ZHA !'##cross-references GB:X67706; NID:g59045; PIDN:CAA47944.1; PID:g59046 CLASSIFICATION #superfamily poliovirus genome polyprotein KEYWORDS coat protein; core protein; genome-linked protein; !1nucleotidyltransferase; phosphoprotein; polyprotein; !1proteinase FEATURE !$1-69 #product coat protein 1A #status predicted #label !8C1A\ !$70-330 #product coat protein 1B #status predicted #label !8C1B\ !$331-568 #product coat protein 1C #status predicted #label !8C1C\ !$569-851 #product coat protein 1D #status predicted #label !8C1D\ !$852-1001 #product core protein 2A #status predicted #label !8C2A\ !$1002-1100 #product core protein 2B #status predicted #label !8C2B\ !$1101-1429 #product core protein 2C #status predicted #label !8C2C\ !$1430-1518 #product protein 3A #status predicted #label P3A\ !$1519-1540 #product genome-linked protein VPg #status predicted !8#label VPG\ !$1541-1723 #product proteinase #status predicted #label PTS\ !$1724-2185 #product RNA-directed RNA polymerase #status !8predicted #label RPS\ !$1521 #binding_site phosphoryl-RNA (Tyr) (covalent) #status !8predicted SUMMARY #length 2185 #molecular-weight 243298 #checksum 8752 SEQUENCE /// ENTRY GNNYA9 #type complete TITLE genome polyprotein - coxsackievirus A9 (strain Griggs) CONTAINS coat protein 1A; coat protein 1B; coat protein 1C; coat protein 1D; core protein 2A; core protein 2B; core protein 2C; genome-linked protein VPg; protein 3A; proteinase; RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name coxsackievirus A9 DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 05-Jun-1998 ACCESSIONS JQ0523 REFERENCE JQ0523 !$#authors Chang, K.H.; Auvinen, P.; Hyypiae, T.; Stanway, G. !$#journal J. Gen. Virol. (1989) 70:3269-3280 !$#title The nucleotide sequence of coxsackievirus A9: implications !1for receptor binding and enterovirus classification. !$#cross-references MUID:90111704; PMID:2558158 !$#accession JQ0523 !'##molecule_type mRNA !'##residues 1-2201 ##label CHA CLASSIFICATION #superfamily poliovirus genome polyprotein KEYWORDS coat protein; core protein; genome-linked protein; !1nucleotidyltransferase; phosphoprotein; polyprotein; !1proteinase FEATURE !$1-69 #product coat protein 1A #status predicted #label !8VP4\ !$70-330 #product coat protein 1B #status predicted #label !8VP2\ !$331-568 #product coat protein 1C #status predicted #label !8VP3\ !$569-870 #product coat protein 1D #status predicted #label !8VP1\ !$871-1017 #product core protein 2A #status predicted #label !82AP\ !$1018-1116 #product core protein 2B #status predicted #label !82BP\ !$1117-1445 #product core protein 2C #status predicted #label !82CP\ !$1446-1534 #product protein 3A #status predicted #label P3A\ !$1535-1556 #product genome-linked protein VPg #status predicted !8#label VPG\ !$1557-1739 #product proteinase #status predicted #label PTS\ !$1740-2201 #product RNA-directed RNA polymerase #status !8predicted #label RPS\ !$1537 #binding_site phosphoryl-RNA (Tyr) (covalent) #status !8predicted SUMMARY #length 2201 #molecular-weight 246494 #checksum 2763 SEQUENCE /// ENTRY GNNYSV #type complete TITLE genome polyprotein - swine vesicular disease virus (strain UKG/27/72) CONTAINS coat protein VP1; coat protein VP2; coat protein VP3; coat protein VP4; core protein P2-3b; core protein P2-5b; core protein P2-X; genome-linked protein VPg; protein P3-1b; proteinase; RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name swine vesicular disease virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS S11670; A30061 REFERENCE S11670 !$#authors Seechurn, P.; Knowles, N.J.; McCauley, J.W. !$#journal Virus Res. (1990) 16:255-274 !$#title The complete nucleotide sequence of a pathogenic swine !1vesicular disease virus. !$#cross-references MUID:90364770; PMID:2168111 !$#accession S11670 !'##molecule_type genomic RNA !'##residues 1-2185 ##label SEE !'##cross-references EMBL:X54521; NID:g61167; PIDN:CAA38377.1; !1PID:g61168 !'##note submitted to the Protein Sequence Database, April 1989 CLASSIFICATION #superfamily poliovirus genome polyprotein KEYWORDS coat protein; core protein; genome-linked protein; !1hydrolase; nucleotidyltransferase; phosphoprotein; !1polyprotein; proteinase FEATURE !$1-69 #product coat protein VP4 #status predicted #label !8VP4\ !$70-330 #product coat protein VP2 #status predicted #label !8VP2\ !$331-568 #product coat protein VP3 #status predicted #label !8VP3\ !$569-851 #product coat protein VP1 #status predicted #label !8VP1\ !$852-1001 #product core protein P2-3b #status predicted #label !8P2A\ !$1002-1100 #product core protein P2-5b #status predicted #label !8P2B\ !$1101-1429 #product core protein P2-X #status predicted #label !8P2C\ !$1430-1518 #product protein P3-1b #status predicted #label P3A\ !$1519-1540 #product genome-linked protein VPg #status predicted !8#label P3B\ !$1541-1723 #product proteinase 3C #status predicted #label P3C\ !$1724-2185 #product RNA-directed RNA polymerase #status !8predicted #label P3D\ !$1521 #binding_site phosphoryl-RNA (Tyr) (covalent) #status !8predicted SUMMARY #length 2185 #molecular-weight 243363 #checksum 5260 SEQUENCE /// ENTRY GNNYSH #type complete TITLE genome polyprotein - swine vesicular disease virus (strain H/3'76) CONTAINS coat protein VP1; coat protein VP2; coat protein VP3; coat protein VP4; core protein P2-3b; core protein P2-5b; core protein P2-X; genome-linked protein VPg; protein P3-1b; proteinase; RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name swine vesicular disease virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jun-2000 ACCESSIONS A31331 REFERENCE A31331 !$#authors Inoue, T.; Suzuki, T.; Sekiguchi, K. !$#journal J. Gen. Virol. (1989) 70:919-934 !$#title The complete nucleotide sequence of swine vesicular disease !1virus. !$#cross-references MUID:89279274; PMID:2543767 !$#accession A31331 !'##molecule_type genomic RNA !'##residues 1-2185 ##label INO !'##cross-references GB:D00435; NID:g1228947; PIDN:BAA00337.1; !1PID:g222630 CLASSIFICATION #superfamily poliovirus genome polyprotein KEYWORDS coat protein; core protein; genome-linked protein; !1hydrolase; nucleotidyltransferase; phosphoprotein; !1polyprotein; proteinase FEATURE !$1-69 #product coat protein VP4 #status predicted #label !8VP4\ !$70-330 #product coat protein VP2 #status predicted #label !8VP2\ !$331-568 #product coat protein VP3 #status predicted #label !8VP3\ !$569-851 #product coat protein VP1 #status predicted #label !8VP1\ !$852-1001 #product core protein P2-3b #status predicted #label !8P2A\ !$1002-1100 #product core protein P2-5b #status predicted #label !8P2B\ !$1101-1429 #product core protein P2-X #status predicted #label !8P2C\ !$1430-1518 #product protein P3-1b #status predicted #label P3A\ !$1519-1540 #product genome-linked protein VPg #status predicted !8#label P3B\ !$1541-1723 #product proteinase 3C #status predicted #label P3C\ !$1724-2185 #product RNA-directed RNA polymerase #status !8predicted #label P3D\ !$1521 #binding_site phosphoryl-RNA (Tyr) (covalent) #status !8predicted SUMMARY #length 2185 #molecular-weight 243164 #checksum 3838 SEQUENCE /// ENTRY GNNYEC #type fragment TITLE genome polyprotein - echovirus 11 (strain Gregory) (fragment) CONTAINS carboxyl end of coat protein 1D; core protein 2A; core protein 2B; core protein 2C; genome-linked protein VPg; protein 3A; proteinase; RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name echovirus 11 DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jun-2000 ACCESSIONS A36642 REFERENCE A36642 !$#authors Auvinen, P.; Hyypiae, T. !$#journal J. Gen. Virol. (1990) 71:2133-2139 !$#title Echoviruses include genetically distinct serotypes. !$#cross-references MUID:91011360; PMID:2170575 !$#accession A36642 !'##molecule_type genomic RNA !'##residues 1-1374 ##label AUV !'##cross-references GB:D10582; GB:D01068; NID:g465394; PIDN:BAA01439.1; !1PID:g465395 CLASSIFICATION #superfamily poliovirus genome polyprotein KEYWORDS coat protein; core protein; genome-linked protein; !1nucleotidyltransferase; phosphoprotein; polyprotein; !1proteinase FEATURE !$1-43 #product coat protein 1D (fragment) #status predicted !8#label VP1\ !$44-190 #product core protein 2A #status predicted #label !82AP\ !$191-289 #product core protein 2B #status predicted #label !82BP\ !$290-618 #product core protein 2C #status predicted #label !82CP\ !$619-707 #product protein 3A #status predicted #label P3A\ !$708-729 #product genome-linked protein VPg #status predicted !8#label VPG\ !$730-912 #product proteinase #status predicted #label PTS\ !$913-1374 #product RNA-directed RNA polymerase #status !8predicted #label RPS\ !$710 #binding_site phosphoryl-RNA (Tyr) (covalent) #status !8predicted SUMMARY #length 1374 #checksum 1466 SEQUENCE /// ENTRY GNNYBE #type complete TITLE genome polyprotein - bovine enterovirus (strain VG-5-27) CONTAINS coat protein VP1; coat protein VP2; coat protein VP3; coat protein VP4; core protein P2-A; core protein P2-B; core protein P2-C; core protein P3-A; genome-linked protein VPg; proteinase; RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name bovine enterovirus DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jun-2000 ACCESSIONS A29824 REFERENCE A29824 !$#authors Earle, J.A.P.; Skuce, R.A.; Fleming, C.S.; Hoey, E.M.; !1Martin, S.J. !$#journal J. Gen. Virol. (1988) 69:253-263 !$#title The complete nucleotide sequence of a bovine enterovirus. !$#cross-references MUID:88117392; PMID:2828511 !$#accession A29824 !'##molecule_type genomic RNA !'##residues 1-2175 ##label EAR !'##cross-references GB:D00214; NID:g2696866; PIDN:BAA24003.1 CLASSIFICATION #superfamily poliovirus genome polyprotein KEYWORDS coat protein; core protein; genome-linked protein; !1nucleotidyltransferase; phosphoprotein; proteinase FEATURE !$1-69 #product coat protein VP4 #status predicted #label !8VP4\ !$70-317 #product coat protein VP2 #status predicted #label !8VP2\ !$318-559 #product coat protein VP3 #status predicted #label !8VP3\ !$560-840 #product coat protein VP1 #status predicted #label !8VP1\ !$841-990 #product core protein P2-A #status predicted #label !8P2A\ !$991-1089 #product core protein P2-B #status predicted #label !8P2B\ !$1090-1419 #product core protein P2-C #status predicted #label !8P2C\ !$1420-1508 #product core protein P3-A #status predicted #label !8P3A\ !$1509-1531 #product genome-linked protein VPg #status predicted !8#label VPG\ !$1532-1714 #product proteinase #status predicted #label PTS\ !$1715-2175 #product RNA-directed RNA polymerase #status !8predicted #label RPS\ !$1511 #binding_site phosphoryl-RNA (Tyr) (covalent) #status !8predicted SUMMARY #length 2175 #molecular-weight 242502 #checksum 7260 SEQUENCE /// ENTRY GNNYE7 #type complete TITLE genome polyprotein - human enterovirus 70 (strain J670/71) CONTAINS coat protein 1A; coat protein 1B; coat protein 1C; coat protein 1D; core protein 2A; core protein 2B; core protein 2C; genome-linked protein VPg; protein 3A; proteinase (EC 3.4.-.-) 3C; RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name human enterovirus 70 DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 05-Jun-1998 ACCESSIONS A36253 REFERENCE A36253 !$#authors Ryan, M.D.; Jenkins, O.; Hughes, P.J.; Brown, A.; Knowles, !1N.J.; Booth, D.; Minor, P.D.; Almond, J.W. !$#journal J. Gen. Virol. (1990) 71:2291-2299 !$#title The complete nucleotide sequence of enterovirus type 70: !1relationships with other members of the Picornaviridae. !$#cross-references MUID:91037960; PMID:2172447 !$#accession A36253 !'##molecule_type genomic RNA !'##residues 1-2194 ##label RYA !'##cross-references GB:D00820 CLASSIFICATION #superfamily poliovirus genome polyprotein KEYWORDS coat protein; core protein; genome-linked protein; !1hydrolase; nucleotidyltransferase; phosphoprotein; !1polyprotein FEATURE !$1-69 #product coat protein 1A #status predicted #label !8VP4\ !$70-319 #product coat protein 1B #status predicted #label !8VP2\ !$320-561 #product coat protein 1C #status predicted #label !8VP3\ !$562-871 #product coat protein 1D #status predicted #label !8VP1\ !$872-1014 #product core protein 2A #status predicted #label !8P2A\ !$1015-1113 #product core protein 2B #status predicted #label !8P2B\ !$1114-1443 #product core protein 2C #status predicted #label !8P2C\ !$1444-1532 #product protein 3A #status predicted #label P3A\ !$1533-1554 #product genome-linked protein VPg #status predicted !8#label VPG\ !$1555-1737 #product proteinase 3C #status predicted #label P3C\ !$1738-2194 #product RNA-directed RNA polymerase #status !8predicted #label RRP\ !$1535 #binding_site phosphoryl-RNA (Tyr) (covalent) #status !8predicted SUMMARY #length 2194 #molecular-weight 244607 #checksum 3885 SEQUENCE /// ENTRY GNNYHM #type complete TITLE genome polyprotein - human hepatitis A virus (strain HM-175, wild type) CONTAINS coat protein 1A; coat protein 1B; coat protein 1C; coat protein 1D; core protein 2A; core protein 2B; core protein 2C; cysteine proteinase (EC 3.4.22.-), protein 3C; protein 3A; protein 3B; RNA-directed RNA polymerase (EC 2.7.7.48), protein 3D ORGANISM #formal_name human hepatitis A virus #note host Homo sapiens (man) DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jul-1999 ACCESSIONS A25981 REFERENCE A25981 !$#authors Cohen, J.I.; Ticehurst, J.R.; Purcell, R.H.; Buckler-White, !1A.; Baroudy, B.M. !$#journal J. Virol. (1987) 61:50-59 !$#title Complete nucleotide sequence of wild-type hepatitis A virus: !1comparison with different strains of hepatitis A virus and !1other picornaviruses. !$#cross-references MUID:87061253; PMID:3023706 !$#accession A25981 !'##molecule_type genomic RNA !'##residues 1-2227 ##label COH !'##cross-references EMBL:M14707; NID:g329582; PIDN:AAA45465.1; !1PID:g329583 CLASSIFICATION #superfamily hepatitis A virus genome polyprotein KEYWORDS coat protein; core protein; cysteine proteinase; hydrolase; !1nucleotidyltransferase; polyprotein FEATURE !$1-23 #product coat protein 1A #status predicted #label !8VP4\ !$24-245 #product coat protein 1B #status predicted #label !8VP2\ !$246-491 #product coat protein 1C #status predicted #label !8VP3\ !$492-791 #product coat protein 1D #status predicted #label !8VP1\ !$792-980 #product core protein 2A #status predicted #label !8C2A\ !$981-1087 #product core protein 2B #status predicted #label !8C2B\ !$1088-1422 #product core protein 2C #status predicted #label !8C2C\ !$1423-1496 #product protein 3A #status predicted #label C3A\ !$1497-1519 #product protein 3B #status predicted #label C3B\ !$1520-1738 #product cysteine proteinase, protein 3C #status !8predicted #label C3C\ !$1739-2227 #product RNA-directed RNA polymerase, protein 3D !8#status predicted #label C3D SUMMARY #length 2227 #molecular-weight 251506 #checksum 1963 SEQUENCE /// ENTRY GNNYHR #type complete TITLE genome polyprotein - human hepatitis A virus CONTAINS coat protein 1A; coat protein 1B; coat protein 1C; core protein 2A; core protein 2B; core protein 2C; cysteine proteinase (EC 3.4.22.-), protein 3C; protein 3A; protein 3B; RNA-directed RNA polymerase (EC 2.7.7.48), protein 3D ORGANISM #formal_name human hepatitis A virus #note host Homo sapiens (man) DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 16-Jul-1999 ACCESSIONS A03903 REFERENCE A03903 !$#authors Najarian, R.; Caput, D.; Gee, W.; Potter, S.J.; Renard, A.; !1Merryweather, J.; van Nest, G.; Dina, D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:2627-2631 !$#title Primary structure and gene organization of human hepatitis A !1virus. !$#cross-references MUID:85190549; PMID:2986127 !$#accession A03903 !'##molecule_type genomic RNA !'##residues 1-2227 ##label NAJ !'##cross-references GB:K02990; NID:g329596; PIDN:AAA45472.1; !1PID:g329597 CLASSIFICATION #superfamily hepatitis A virus genome polyprotein KEYWORDS coat protein; core protein; cysteine proteinase; hydrolase; !1nucleotidyltransferase; polyprotein FEATURE !$1-245 #product coat protein 1A #status predicted #label !8C1A\ !$246-491 #product coat protein 1B #status predicted #label !8C1B\ !$492-836 #product coat protein 1C #status predicted #label !8C1C\ !$837-980 #product core protein 2A #status predicted #label !8C2A\ !$981-1076 #product core protein 2B #status predicted #label !8C2B\ !$1077-1422 #product core protein 2C #status predicted #label !8C2C\ !$1423-1484 #product protein 3A #status predicted #label C3A\ !$1485-1507 #product protein 3B #status predicted #label C3B\ !$1508-1678 #product cysteine proteinase, protein 3C #status !8predicted #label C3C\ !$1679-2227 #product RNA-directed RNA polymerase, protein 3D !8#status predicted #label C3D SUMMARY #length 2227 #molecular-weight 251898 #checksum 1208 SEQUENCE /// ENTRY GNNYMK #type complete TITLE genome polyprotein - human hepatitis A virus (strain HM-175/ 7MK-5, attenuated HAV) CONTAINS coat protein 1A; coat protein 1B; coat protein 1C; core protein 2A; core protein 2B; core protein 2C; cysteine proteinase (EC 3.4.22.-), protein 3C; protein 3A; protein 3B; RNA-directed RNA polymerase (EC 2.7.7.48), protein 3D ORGANISM #formal_name human hepatitis A virus #note host Homo sapiens (man) DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 16-Jul-1999 ACCESSIONS A94149; A25914; A94508 REFERENCE A94149 !$#authors Cohen, J.I.; Rosenblum, B.; Ticehurst, J.R.; Daemer, R.J.; !1Feinstone, S.M.; Purcell, R.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:2497-2501 !$#title Complete nucleotide sequence of an attenuated hepatitis A !1virus: comparison with wild-type virus. !$#cross-references MUID:87175701; PMID:3031686 !$#accession A94149 !'##status nucleic acid sequence not shown !'##molecule_type genomic RNA !'##residues 1-2227 ##label COH !'##cross-references EMBL:M16632; NID:g329594; PIDN:AAA45471.1; !1PID:g329595 !'##note submitted to GenBank, August 1987 CLASSIFICATION #superfamily hepatitis A virus genome polyprotein KEYWORDS coat protein; core protein; cysteine proteinase; hydrolase; !1nucleotidyltransferase; polyprotein FEATURE !$1-245 #product coat protein 1A #status predicted #label !8P1A\ !$246-491 #product coat protein 1B #status predicted #label !8P1B\ !$492-836 #product coat protein 1C #status predicted #label !8P1C\ !$837-980 #product core protein 2A #status predicted #label !8P2A\ !$981-1076 #product core protein 2B #status predicted #label !8P2B\ !$1077-1422 #product core protein 2C #status predicted #label !8P2C\ !$1423-1484 #product protein 3A #status predicted #label P3A\ !$1485-1507 #product protein 3B #status predicted #label P3B\ !$1508-1678 #product cysteine proteinase, protein 3C #status !8predicted #label P3C\ !$1679-2227 #product RNA-directed RNA polymerase, protein 3D !8#status predicted #label P3D SUMMARY #length 2227 #molecular-weight 251515 #checksum 3810 SEQUENCE /// ENTRY GNNYHB #type complete TITLE genome polyprotein - human hepatitis A virus (strain MBB) CONTAINS coat protein 1A; coat protein 1B; coat protein 1C; coat protein 1D; core protein 2A; core protein 2B; core protein 2C; cysteine proteinase (EC 3.4.22.-), protein 3C; genome-linked protein VPg; protein 3A; RNA-directed RNA polymerase (EC 2.7.7.48), protein 3D ORGANISM #formal_name human hepatitis A virus #note host Homo sapiens (man) DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 10-May-1996 ACCESSIONS JS0303 REFERENCE JS0303 !$#authors Paul, A.V.; Tada, H.; von der Helm, K.; Wissel, T.; Kiehn, !1R.; Wimmer, E.; Deinhardt, F. !$#journal Virus Res. (1987) 8:153-171 !$#title The entire nucleotide sequence of the genome of human !1hepatitis A virus (isolate MBB). !$#cross-references MUID:88045071; PMID:2823500 !$#accession JS0303 !'##molecule_type genomic RNA !'##residues 1-2227 ##label PAU !'##cross-references EMBL:M20273 CLASSIFICATION #superfamily hepatitis A virus genome polyprotein KEYWORDS coat protein; core protein; cysteine proteinase; !1genome-linked protein; hydrolase; nucleotidyltransferase; !1polyprotein FEATURE !$1-23 #product coat protein 1A #status predicted #label !8VP4\ !$24-246 #product coat protein 1B #status predicted #label !8VP2\ !$247-491 #product coat protein 1C #status predicted #label !8VP3\ !$492-836 #product coat protein 1D #status predicted #label !8VP1\ !$837-980 #product core protein 2A #status predicted #label !8P2A\ !$981-1108 #product core protein 2B #status predicted #label !8P2B\ !$1109-1438 #product core protein 2C #status predicted #label !8P2C\ !$1439-1496 #product protein 3A #status predicted #label P3A\ !$1497-1519 #product genome-linked protein VPg #status predicted !8#label VPG\ !$1520-1736 #product cysteine proteinase, protein 3C #status !8predicted #label P3C\ !$1737-2227 #product RNA-directed RNA polymerase, protein 3D !8#status predicted #label P3D SUMMARY #length 2227 #molecular-weight 251413 #checksum 2170 SEQUENCE /// ENTRY GNNYHA #type fragment TITLE genome polyprotein - human hepatitis A virus (strain CR326) (fragment) CONTAINS coat protein 1A; coat protein 1B; coat protein 1C; core protein 2A ORGANISM #formal_name human hepatitis A virus #note host Homo sapiens (man) DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 16-Jul-1999 ACCESSIONS A03904 REFERENCE A03904 !$#authors Linemeyer, D.L.; Menke, J.G.; Martin-Gallardo, A.; Hughes, !1J.V.; Young, A.; Mitra, S.W. !$#journal J. Virol. (1985) 54:247-255 !$#title Molecular cloning and partial sequencing of hepatitis A !1viral cDNA. !$#cross-references MUID:85185648; PMID:2985793 !$#accession A03904 !'##molecule_type genomic RNA !'##residues 1-852 ##label LIN !'##cross-references EMBL:M10033; NID:g329592; PIDN:AAA45470.1; !1PID:g329593 CLASSIFICATION #superfamily hepatitis A virus genome polyprotein KEYWORDS coat protein; core protein; polyprotein FEATURE !$1-245 #product coat protein 1A #status predicted #label !8C1A\ !$246-491 #product coat protein 1B #status predicted #label !8C1B\ !$492-836 #product coat protein 1C #status predicted #label !8C1C\ !$837-852 #product core protein 2A (fragment) #status predicted !8#label C2A SUMMARY #length 852 #checksum 5560 SEQUENCE /// ENTRY GNNYSA #type complete TITLE genome polyprotein - simian hepatitis A virus (strain AGM-27) CONTAINS coat protein 1A; coat protein 1B; coat protein 1C; coat protein 1D; core protein 2A; core protein 2B; core protein 2C; protein 3A; protein 3B; protein 3C; protein 3D; RNA polymerase ORGANISM #formal_name simian hepatitis A virus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jun-2000 ACCESSIONS A30470; S04885; S03965 REFERENCE A30470 !$#authors Tsarev, S.A. !$#submission submitted to JIPID, April 1991 !$#accession A30470 !'##molecule_type genomic RNA !'##residues 1-2230 ##label TSA !'##cross-references GB:D00924; NID:g222597; PIDN:BAA00766.1; !1PID:g222598 REFERENCE JQ1080 !$#authors Tsarev, S.A.; Emerson, S.U.; Balayan, M.S.; Ticehurst, J.; !1Purcell, R.H. !$#journal J. Gen. Virol. (1991) 72:1677-1683 !$#title Simian hepatitis A virus (HAV) strain AGM-27: comparison of !1genome structure and growth in cell culture with other HAV !1strains. !$#cross-references MUID:91311420; PMID:1649901 !$#contents annotation !$#note neither amino acid nor nucleotide sequence is given REFERENCE S04885 !$#authors Balayan, M.S.; Kusov, Y.Y.; Andjaparidze, A.G.; Tsarev, !1S.A.; Sverdlov, E.D.; Chizhikov, V.E.; Blinov, V.M.; !1Vasilenko, S.K. !$#submission submitted to the EMBL Data Library, May 1989 !$#accession S04885 !'##molecule_type genomic RNA !'##residues 1750-2164 ##label BAL1 !'##cross-references EMBL:X15461; NID:g61971; PIDN:CAA33490.1; !1PID:g930268 REFERENCE S03965 !$#authors Balayan, M.S.; Kusov, Y.Y.; Andjaparidze, A.G.; Tsarev, !1S.A.; Sverdlov, E.D.; Chizhikov, V.E.; Blinov, V.M.; !1Vasilenko, S.K. !$#journal FEBS Lett. (1989) 247:425-428 !$#title Variations in genome fragments coding for RNA polymerase in !1human and simian hepatitis A viruses. !$#cross-references MUID:89232168; PMID:2541023 !$#accession S03965 !'##molecule_type genomic RNA !'##residues 1960-2164 ##label BAL2 !'##cross-references EMBL:X15461 CLASSIFICATION #superfamily hepatitis A virus genome polyprotein KEYWORDS coat protein; core protein; polyprotein FEATURE !$1-27 #product coat protein 1A #status predicted #label !8C1A\ !$28-249 #product coat protein 1B #status predicted #label !8C1B\ !$250-495 #product coat protein 1C #status predicted #label !8C1C\ !$496-795 #product coat protein 1D #status predicted #label !8C1D\ !$796-984 #product core protein 2A #status predicted #label !8C2A\ !$985-1091 #product core protein 2B #status predicted #label !8C2B\ !$1092-1426 #product core protein 2C #status predicted #label !8C2C\ !$1427-1498 #product protein 3A #status predicted #label P3A\ !$1499-1521 #product protein 3B #status predicted #label P3B\ !$1522-1741 #product protein 3C #status predicted #label P3C\ !$1742-2230 #product protein 3D #status predicted #label P3D SUMMARY #length 2230 #molecular-weight 251296 #checksum 6800 SEQUENCE /// ENTRY GNNYS2 #type fragment TITLE genome polyprotein - simian hepatitis A virus (strain CY-145) (fragment) CONTAINS amino end of core protein 2A; coat protein 1A; coat protein 1B; coat protein 1C; coat protein 1D ORGANISM #formal_name simian hepatitis A virus #note host Macaca fascicularis (cynomolgus macaque) DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS JQ1180 REFERENCE JQ1180 !$#authors Nainan, O.V.; Margolis, H.S.; Robertson, B.H.; Balayan, M.; !1Brinton, M.A. !$#journal J. Gen. Virol. (1991) 72:1685-1689 !$#title Sequence analysis of a new hepatitis A virus naturally !1infecting cynomolgus macaques (Macaca fascicularis). !$#cross-references MUID:91311421; PMID:1649902 !$#accession JQ1180 !'##molecule_type genomic RNA !'##residues 1-839 ##label NAI !'##cross-references GB:M59286; NID:g329599; PIDN:AAA45473.1; !1PID:g555083 CLASSIFICATION #superfamily hepatitis A virus genome polyprotein KEYWORDS coat protein; core protein; glycoprotein; polyprotein FEATURE !$1-23 #product coat protein 1A #status predicted #label !8VP0\ !$24-245 #product coat protein 1B #status predicted #label !8VP3\ !$246-491 #product coat protein 1C #status predicted #label !8VP1\ !$492-839 #product core protein 2A (fragment) #status predicted !8#label P2P\ !$261,312,728,756 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 839 #checksum 1768 SEQUENCE /// ENTRY GNNYE #type complete TITLE genome polyprotein - encephalomyocarditis virus CONTAINS coat protein VP1; coat protein VP2; coat protein VP3; coat protein VP4; core protein P2-A; core protein P2-B; core protein P2-C; core protein P3-A; genome-linked protein VPg; proteinase (EC 3.4.-.-); RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name encephalomyocarditis virus, EMCV #note host Homo sapiens (man) DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 16-Jul-1999 ACCESSIONS A03906; JN0383 REFERENCE A03906 !$#authors Palmenberg, A.C.; Kirby, E.M.; Janda, M.R.; Drake, N.L.; !1Duke, G.M.; Potratz, K.F.; Collett, M.S. !$#journal Nucleic Acids Res. (1984) 12:2969-2985 !$#title The nucleotide and deduced amino acid sequences of the !1encephalomyocarditis viral polyprotein coding region. !$#cross-references MUID:84169586; PMID:6324136 !$#accession A03906 !'##molecule_type genomic RNA !'##residues 1-2290 ##label PAL !'##cross-references GB:X00463; NID:g61034; PIDN:CAA25152.1; PID:g61035 REFERENCE JN0383 !$#authors Petrov, N.A.; Chizhikov, V.E.; Blinov, V.M.; Karginov, V.A.; !1Mikryukov, N.N.; Gutorov, V.V.; Grishaev, M.P.; Beklemishev, !1A.B.; Vassilenko, S.K. !$#journal Bioorg. Khim. (1984) 10:274-279 !$#title Nucleotide sequence of the 3'-terminus of !1encephalomyocarditis virus RNA. !$#cross-references MUID:85022788; PMID:6091680 !$#accession JN0383 !'##molecule_type genomic RNA !'##residues 1337-1396,'L',1398-1517,'A',1519-1536,'E',1538-1556,'S', !11558-1611,'T',1613-1915,'N',1917-1986,'IH',1989-2007,'I', !12009-2048,'H',2050-2193,'K',2195-2290 ##label PET !'##cross-references GB:M54935 !'##note the authors translated the codon CAU for residue 713 as Thr and !1AAC for residue 857 as Asp CLASSIFICATION #superfamily foot-and-mouth disease virus genome polyprotein KEYWORDS coat protein; core protein; genome-linked protein; !1hydrolase; nucleotidyltransferase; polyprotein; proteinase FEATURE !$1-67 #domain leader peptide #status predicted #label LDP\ !$68-136 #product coat protein VP4 #status predicted #label !8VP4\ !$137-391 #product coat protein VP2 #status predicted #label !8VP2\ !$392-622 #product coat protein VP3 #status predicted #label !8VP3\ !$623-910 #product coat protein VP1 #status predicted #label !8VP1\ !$911-1056 #product core protein P2-A #status predicted #label !8P2A\ !$1057-1192 #product core protein P2-B #status predicted #label !8P2B\ !$1193-1517 #product core protein P2-C #status predicted #label !8P2C\ !$1518-1605 #product core protein P3-A #status predicted #label !8P3A\ !$1606-1625 #product genome-linked protein VPg #status predicted !8#label VPG\ !$1626-1830 #product proteinase #status predicted #label PTS\ !$1831-2290 #product RNA-directed RNA polymerase #status !8predicted #label RDP SUMMARY #length 2290 #molecular-weight 255756 #checksum 8698 SEQUENCE /// ENTRY GNNYED #type complete TITLE genome polyprotein - encephalomyocarditis virus (strain EMC-D, diabetogenic) CONTAINS coat protein VP1; coat protein VP2; coat protein VP3; coat protein VP4; core protein P2-A; core protein P2-B; core protein P2-C; core protein P3-A; genome-linked protein VPg; proteinase (EC 3.4.-.-); RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name encephalomyocarditis virus, EMCV #note host Homo sapiens (man) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 13-Mar-1998 ACCESSIONS A31473; A60498 REFERENCE A94395 !$#authors Bae, Y.S.; Eun, H.M.; Yoon, J.W. !$#journal Virology (1989) 170:282-287 !$#title Genomic differences between the diabetogenic and !1nondiabetogenic variants of encephalomyocarditis virus. !$#cross-references MUID:89243189; PMID:2541543 !$#accession A31473 !'##molecule_type genomic RNA !'##residues 1-2292 ##label BAE !'##note the authors translated the codon ATG for residue 1079 as Asn !1and GAC for residue 1564 as Val REFERENCE A60498 !$#authors Bae, Y.S.; Eun, H.M.; Yoon, J.W. !$#journal Diabetes (1989) 38:316-320 !$#title Molecular identification of diabetogenic viral gene. !$#cross-references MUID:89137787; PMID:2537245 !$#accession A60498 !'##molecule_type genomic RNA !'##residues 1-1522,'D',1524-2292 ##label BA2 CLASSIFICATION #superfamily foot-and-mouth disease virus genome polyprotein KEYWORDS coat protein; core protein; genome-linked protein; !1hydrolase; nucleotidyltransferase; polyprotein; proteinase FEATURE !$1-67 #domain leader peptide #status predicted #label LDP\ !$68-137 #product coat protein VP4 #status predicted #label !8VP4\ !$138-393 #product coat protein VP2 #status predicted #label !8VP2\ !$394-624 #product coat protein VP3 #status predicted #label !8VP3\ !$625-901 #product coat protein VP1 #status predicted #label !8VP1\ !$902-1058 #product core protein P2-A #status predicted #label !8P2A\ !$1059-1194 #product core protein P2-B #status predicted #label !8P2B\ !$1195-1519 #product core protein P2-C #status predicted #label !8P2C\ !$1520-1607 #product core protein P3-A #status predicted #label !8P3A\ !$1608-1627 #product genome-linked protein VPg #status predicted !8#label VPG\ !$1628-1832 #product proteinase #status predicted #label PTS\ !$1833-2292 #product RNA-directed RNA polymerase #status !8predicted #label RDP SUMMARY #length 2292 #molecular-weight 255382 #checksum 3920 SEQUENCE /// ENTRY GNNYEB #type complete TITLE genome polyprotein - encephalomyocarditis virus (strain EMC-B, nondiabetogenic) CONTAINS coat protein VP1; coat protein VP2; coat protein VP3; coat protein VP4; core protein P2-A; core protein P2-B; core protein P2-C; core protein P3-A; genome-linked protein VPg; proteinase (EC 3.4.-.-); RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name encephalomyocarditis virus, EMCV #note host Homo sapiens (man) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 13-Mar-1998 ACCESSIONS B31473; B60498 REFERENCE A94395 !$#authors Bae, Y.S.; Eun, H.M.; Yoon, J.W. !$#journal Virology (1989) 170:282-287 !$#title Genomic differences between the diabetogenic and !1nondiabetogenic variants of encephalomyocarditis virus. !$#cross-references MUID:89243189; PMID:2541543 !$#accession B31473 !'##molecule_type genomic RNA !'##residues 1-2292 ##label BAE !'##note the authors translated the codon ATG for residue 1079 as Asn !1and GAC for residue 1564 as Val REFERENCE A60498 !$#authors Bae, Y.S.; Eun, H.M.; Yoon, J.W. !$#journal Diabetes (1989) 38:316-320 !$#title Molecular identification of diabetogenic viral gene. !$#cross-references MUID:89137787; PMID:2537245 !$#accession B60498 !'##molecule_type genomic RNA !'##residues 1-15;17-2292 ##label BA2 CLASSIFICATION #superfamily foot-and-mouth disease virus genome polyprotein KEYWORDS coat protein; core protein; genome-linked protein; !1hydrolase; nucleotidyltransferase; polyprotein; proteinase FEATURE !$1-67 #domain leader peptide #status predicted #label LDP\ !$68-137 #product coat protein VP4 #status predicted #label !8VP4\ !$138-393 #product coat protein VP2 #status predicted #label !8VP2\ !$394-624 #product coat protein VP3 #status predicted #label !8VP3\ !$625-901 #product coat protein VP1 #status predicted #label !8VP1\ !$902-1058 #product core protein P2-A #status predicted #label !8P2A\ !$1059-1194 #product core protein P2-B #status predicted #label !8P2B\ !$1195-1519 #product core protein P2-C #status predicted #label !8P2C\ !$1520-1607 #product core protein P3-A #status predicted #label !8P3A\ !$1608-1627 #product genome-linked protein VPg #status predicted !8#label VPG\ !$1628-1832 #product proteinase #status predicted #label PTS\ !$1833-2292 #product RNA-directed RNA polymerase #status !8predicted #label RDP SUMMARY #length 2292 #molecular-weight 255495 #checksum 6728 SEQUENCE /// ENTRY GNNYMV #type fragment TITLE genome polyprotein - Mengo virus (strain 37A) (fragment) CONTAINS coat protein VP1; coat protein VP2; coat protein VP3; coat protein VP4 ORGANISM #formal_name Mengo virus DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 27-Jan-1995 ACCESSIONS A43379 REFERENCE A43379 !$#authors Mann, L.M.; Anderson, K.; Luo, M.; Bond, C.W. !$#journal Virology (1992) 190:337-345 !$#title Molecular and structural basis of hemagglutination in !1mengovirus. !$#cross-references MUID:92410611; PMID:1326807 !$#accession A43379 !'##molecule_type genomic RNA !'##residues 1-900 ##label MAN !'##cross-references GB:M88547 !'##note only the translation of the VP1 nucleotide sequence is given CLASSIFICATION #superfamily foot-and-mouth disease virus genome polyprotein KEYWORDS coat protein; polyprotein FEATURE !$1-67 #domain leader peptide #status predicted #label LDP\ !$68-137 #product coat protein VP4 #status predicted #label !8VP4\ !$138-393 #product coat protein VP2 #status predicted #label !8VP2\ !$394-624 #product coat protein VP3 #status predicted #label !8VP3\ !$625-900 #product coat protein VP1 #status predicted #label !8VP1 SUMMARY #length 900 #checksum 6872 SEQUENCE /// ENTRY GNNYTM #type complete TITLE genome polyprotein - murine poliovirus (strain BeAn 8386) CONTAINS probable proteinase (EC 3.4.-.-); protein 1A; protein 1B; protein 1C; protein 1D; protein 2A; protein 2B; protein 2C; protein 3A; protein 3B; protein 3C; protein 3D ORGANISM #formal_name murine poliovirus, Theiler's encephalomyelitis virus DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 16-Jul-1999 ACCESSIONS A29535 REFERENCE A29535 !$#authors Pevear, D.C.; Calenoff, M.; Rozhon, E.; Lipton, H.L. !$#journal J. Virol. (1987) 61:1507-1516 !$#title Analysis of the complete nucleotide sequence of the !1picornavirus Theiler's murine encephalomyelitis virus !1indicates that it is closely related to cardioviruses. !$#cross-references MUID:87198877; PMID:3033278 !$#accession A29535 !'##molecule_type genomic RNA !'##residues 1-2303 ##label PEV !'##cross-references GB:M16020; NID:g335239; PIDN:AAA47930.1; !1PID:g335240 CLASSIFICATION #superfamily foot-and-mouth disease virus genome polyprotein KEYWORDS coat protein; core protein; genome-linked protein; !1hydrolase; polyprotein; proteinase FEATURE !$1-76 #domain leader peptide #status predicted #label LDP\ !$77-147 #product protein 1A (coat protein VP4) #status !8predicted #label VP4\ !$148-414 #product protein 1B (coat protein VP2) #status !8predicted #label VP2\ !$415-646 #product protein 1C (coat protein VP3) #status !8predicted #label VP3\ !$647-922 #product protein 1D (coat protein VP1) #status !8predicted #label VP1\ !$923-1061 #product protein 2A (core protein P2-3b) #status !8predicted #label P2A\ !$1062-1191 #product protein 2B (core protein P2-5b) #status !8predicted #label P2B\ !$1192-1517 #product protein 2C (core protein P2-X) #status !8predicted #label P2C\ !$1518-1605 #product protein 3A (protein P3-1b) #status predicted !8#label P3A\ !$1606-1625 #product protein 3B (genome-linked protein VPg) !8#status predicted #label P3B\ !$1626-1842 #product protein 3C (probable proteinase) #status !8predicted #label P3C\ !$1843-2303 #product protein 3D (probable RNA-directed RNA !8polymerase) #status predicted #label P3D SUMMARY #length 2303 #molecular-weight 256292 #checksum 6169 SEQUENCE /// ENTRY GNNYTN #type complete TITLE genome polyprotein - murine poliovirus (strain DA) CONTAINS coat protein VP1; coat protein VP2; coat protein VP3; coat protein VP4; core protein P2-3b; core protein P2-5b; core protein P2-X; genome-linked protein VPg; probable proteinase (EC 3.4.-.-); protein P3-1b; RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name murine poliovirus, Theiler's encephalomyelitis virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS A31228 REFERENCE A31228 !$#authors Ohara, Y.; Stein, S.; Fu, J.; Stillman, L.; Klaman, L.; !1Roos, R.P. !$#journal Virology (1988) 164:245-255 !$#title Molecular cloning and sequence determination of DA strain of !1Theiler's murine encephalomyelitis viruses. !$#cross-references MUID:88206072; PMID:2834872 !$#accession A31228 !'##molecule_type genomic RNA !'##residues 1-2301 ##label OHA !'##cross-references GB:M20301; NID:g335219; PIDN:AAA47928.1; !1PID:g335220 CLASSIFICATION #superfamily foot-and-mouth disease virus genome polyprotein KEYWORDS coat protein; core protein; genome-linked protein; !1hydrolase; nucleotidyltransferase; polyprotein; proteinase FEATURE !$1-76 #domain leader peptide #status predicted #label LDP\ !$77-147 #product protein 1A (coat protein VP4) #status !8predicted #label VP4\ !$148-414 #product protein 1B (coat protein VP2) #status !8predicted #label VP2\ !$415-646 #product protein 1C (coat protein VP3) #status !8predicted #label VP3\ !$647-920 #product protein 1D (coat protein VP1) #status !8predicted #label VP1\ !$921-1062 #product protein 2A (core protein P2-3b) #status !8predicted #label P2A\ !$1063-1189 #product protein 2B (core protein P2-5b) #status !8predicted #label P2B\ !$1190-1515 #product protein 2C (core protein P2-X) #status !8predicted #label P2C\ !$1516-1603 #product protein 3A (protein P3-1b) #status predicted !8#label P3A\ !$1604-1623 #product protein 3B (genome-linked protein VPg) !8#status predicted #label P3B\ !$1624-1840 #product protein 3C (probable proteinase) #status !8predicted #label P3C\ !$1841-2301 #product protein 3D (probable RNA-directed RNA !8polymerase) #status predicted #label P3D SUMMARY #length 2301 #molecular-weight 256159 #checksum 3 SEQUENCE /// ENTRY GNNYTP #type complete TITLE genome polyprotein - murine poliovirus (strain GDVII) CONTAINS probable proteinase (EC 3.4.-.-); protein 1A; protein 1B; protein 1C; protein 1D; protein 2A; protein 2B; protein 2C; protein 3A; protein 3B; protein 3C; protein 3D ORGANISM #formal_name murine poliovirus, Theiler's encephalomyelitis virus DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS A29193 REFERENCE A29193 !$#authors Pevear, D.C.; Borkowski, J.; Calenoff, M.; Oh, C.K.; !1Ostrowski, B.; Lipton, H.L. !$#journal Virology (1988) 165:1-12 !$#title Insights into Theiler's virus neurovirulence based on a !1genomic comparison of the neurovirulent GDVII and less !1virulent BeAn strains. !$#cross-references MUID:88265847; PMID:2838951 !$#accession A29193 !'##molecule_type genomic RNA !'##residues 1-2303 ##label PEV !'##cross-references GB:M20562; NID:g335221; PIDN:AAA96329.1; !1PID:g1256538 CLASSIFICATION #superfamily foot-and-mouth disease virus genome polyprotein KEYWORDS coat protein; core protein; genome-linked protein; !1hydrolase; polyprotein; proteinase FEATURE !$1-76 #domain leader peptide #status predicted #label LDP\ !$77-147 #product protein 1A (coat protein VP4) #status !8predicted #label VP4\ !$148-414 #product protein 1B (coat protein VP2) #status !8predicted #label VP2\ !$415-646 #product protein 1C (coat protein VP3) #status !8predicted #label VP3\ !$647-922 #product protein 1D (coat protein VP1) #status !8predicted #label VP1\ !$923-1064 #product protein 2A (core protein P2-3b) #status !8predicted #label P2A\ !$1065-1191 #product protein 2B (core protein P2-5b) #status !8predicted #label P2B\ !$1192-1517 #product protein 2C (core protein P2-X) #status !8predicted #label P2C\ !$1518-1605 #product protein 3A (protein P3-1b) #status predicted !8#label P3A\ !$1606-1625 #product protein 3B (genome-linked protein VPg) !8#status predicted #label P3B\ !$1626-1842 #product protein 3C (probable proteinase) #status !8predicted #label P3C\ !$1843-2303 #product protein 3D (probable RNA-directed RNA !8polymerase) #status predicted #label P3D SUMMARY #length 2303 #molecular-weight 256370 #checksum 9232 SEQUENCE /// ENTRY GNNYF #type complete TITLE genome polyprotein - foot-and-mouth disease virus O (strains O1K and O1BFS) CONTAINS coat protein VP1; coat protein VP2; coat protein VP3; coat protein VP4; core protein p12; core protein p14; core protein P20b; core protein p34; core protein P56; core protein VPg; nonstructural protein p20a ORGANISM #formal_name Aphthovirus O #common_name foot-and-mouth disease virus O #note host Artiodactyla (cloven-footed mammals) DATE 01-Sep-1981 #sequence_revision 27-Nov-1985 #text_change 16-Jul-1999 ACCESSIONS A03907; A37503; S03342 REFERENCE A03907 !$#authors Forss, S.; Strebel, K.; Beck, E.; Schaller, H. !$#journal Nucleic Acids Res. (1984) 12:6587-6601 !$#title Nucleotide sequence and genome organization of !1foot-and-mouth disease virus. !$#cross-references MUID:84297249; PMID:6089122 !$#accession A03907 !'##molecule_type mRNA !'##residues 1-2332 ##label FOR !'##cross-references GB:X00871; NID:g61076; PIDN:CAA25416.1; PID:g61078 !'##experimental_source strain O1K REFERENCE A37503 !$#authors Makoff, A.J.; Paynter, C.A.; Rowlands, D.J.; Boothroyd, J.C. !$#journal Nucleic Acids Res. (1982) 10:8285-8295 !$#title Comparison of the amino acid sequence of the major immunogen !1from three serotypes of foot and mouth disease virus. !$#cross-references MUID:83143292; PMID:6298715 !$#accession A37503 !'##molecule_type genomic RNA !'##residues 715-779,'V',781-807,'R',809-860,'S',862-951 ##label MAK !'##cross-references GB:J02185; NID:g210435; PIDN:AAA42635.1; !1PID:g210436 !'##experimental_source strain O1BFS REFERENCE S03342 !$#authors Acharya, R.; Fry, E.; Stuart, D.; Fox, G.; Rowlands, D.; !1Brown, F. !$#journal Nature (1989) 337:709-716 !$#title The three-dimensional structure of foot-and-mouth disease !1virus at 2.9 A resolution. !$#cross-references MUID:89143740; PMID:2537470 !$#contents annotation; X-ray crystallography, 2,9 angstroms COMMENT The coat protein VP1 contains the main antigenic !1determinants of the virion; therefore, changes in its !1sequence must be responsible for the high antigenic !1variability of the virus. COMMENT Coat proteins VP2 and VP3 are related to the poliovirus coat !1proteins VP2 and VP3. CLASSIFICATION #superfamily foot-and-mouth disease virus genome polyprotein KEYWORDS coat protein; core protein; nonstructural protein; !1polyprotein FEATURE !$1-217 #product nonstructural protein p20a #status predicted !8#label NPA\ !$218-286 #product coat protein VP4 #status predicted #label !8VP4\ !$287-504 #product coat protein VP2 #status predicted #label !8VP2\ !$505-724 #product coat protein VP3 #status predicted #label !8VP3\ !$725-937 #product coat protein VP1 #status predicted #label !8VP1\ !$938-1107 #product core protein p12 #status predicted #label !8C12\ !$1108-1425 #product core protein p34 #status predicted #label !8P34\ !$1426-1578 #product core protein p14 #status predicted #label !8C14\ !$1579-1649 #product genome-linked protein VPg #status predicted !8#label VPG\ !$1650-1862 #product nonstructural protein p20b #status predicted !8#label P20\ !$1863-2332 #product RNA-directed RNA polymerase #status !8predicted #label P56 SUMMARY #length 2332 #molecular-weight 258925 #checksum 4170 SEQUENCE /// ENTRY GNNYC1 #type fragment TITLE genome polyprotein - foot-and-mouth disease virus C (fragment) CONTAINS amino end of core protein p12; coat protein VP1; coat protein VP2; coat protein VP3; coat protein VP4; nonstructural protein p20a ORGANISM #formal_name Aphthovirus C #common_name foot-and-mouth disease virus C #note host Artiodactyla (cloven-footed mammals) DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jun-2000 ACCESSIONS A20288 REFERENCE A20288 !$#authors Beck, E.; Forss, S.; Strebel, K.; Cattaneo, R.; Feil, G. !$#journal Nucleic Acids Res. (1983) 11:7873-7885 !$#title Structure of the FMDV translation initiation site and of the !1structural proteins. !$#cross-references MUID:84069809; PMID:6316275 !$#accession A20288 !'##molecule_type mRNA !'##residues 1-1011 ##label BEC !'##cross-references GB:X00130; NID:g4456719; PIDN:CAA24960.2; !1PID:g4456720 CLASSIFICATION #superfamily foot-and-mouth disease virus genome polyprotein KEYWORDS coat protein; core protein; nonstructural protein; !1polyprotein FEATURE !$1-217 #product nonstructural protein p20a #status predicted !8#label NPA\ !$218-286 #product coat protein VP4 #status predicted #label !8VP4\ !$287-504 #product coat protein VP2 #status predicted #label !8VP2\ !$505-723 #product coat protein VP3 #status predicted #label !8VP3\ !$724-932 #product coat protein VP1 #status predicted #label !8VP1\ !$933-1011 #product core protein p12 (fragment) #status !8predicted #label CPB SUMMARY #length 1011 #checksum 8033 SEQUENCE /// ENTRY GNNY2F #type complete TITLE genome polyprotein - foot-and-mouth disease virus A (strain A[10]61) CONTAINS coat protein VP1; coat protein VP2; coat protein VP3; coat protein VP4; core protein p52; genome-linked protein VPg1; genome-linked protein VPg2; genome-linked protein VPg3; nonstructural protein p20a; nonstructural protein p20b; RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name Aphthovirus A #common_name foot-and-mouth disease virus A DATE 17-Dec-1982 #sequence_revision 28-Aug-1985 #text_change 16-Jul-1999 ACCESSIONS A93508; A91491; S30753 REFERENCE A93508 !$#authors Carroll, A.R.; Rowlands, D.J.; Clarke, B.E. !$#journal Nucleic Acids Res. (1984) 12:2461-2472 !$#title The complete nucleotide sequence of the RNA coding for the !1primary translation product of foot and mouth disease virus. !$#cross-references MUID:84169547; PMID:6324120 !$#accession A93508 !'##molecule_type genomic RNA !'##residues 1-2333 ##label CAR !'##cross-references GB:X00429 REFERENCE A91491 !$#authors Boothroyd, J.C.; Harris, T.J.R.; Rowlands, D.J.; Lowe, P.A. !$#journal Gene (1982) 17:153-161 !$#title The nucleotide sequence of cDNA coding for the structural !1proteins of foot-and-mouth disease virus. !$#cross-references MUID:82211814; PMID:6282711 !$#accession A91491 !'##molecule_type genomic RNA !'##residues 115-395,'C',397-631,'L',633-1048 ##label BOO !'##cross-references GB:V01130; NID:g61048; PIDN:CAA24361.1; !1PID:g1335402 REFERENCE S30753 !$#authors Sangar, D.V.; Newton, S.E.; Rowlands, D.J.; Clarke, B.E. !$#journal Nucleic Acids Res. (1987) 15:3305-3315 !$#title All foot and mouth disease virus serotypes initiate protein !1synthesis at two separate AUGs. !$#cross-references MUID:87203363; PMID:3033601 !$#accession S30753 !'##molecule_type genomic RNA !'##residues 1-32 ##label SAN !'##cross-references EMBL:M31575; NID:g210486; PIDN:AAA42655.1; !1PID:g210487 CLASSIFICATION #superfamily foot-and-mouth disease virus genome polyprotein KEYWORDS coat protein; core protein; genome-linked protein; !1nonstructural protein; nucleotidyltransferase; polyprotein FEATURE !$1-204 #product nonstructural protein p20a #status predicted !8#label NPA\ !$205-286 #product coat protein VP4 #status predicted #label !8VP4\ !$287-504 #product coat protein VP2 #status predicted #label !8VP2\ !$505-725 #product coat protein VP3 #status predicted #label !8VP3\ !$726-937 #product coat protein VP1 #status predicted #label !8VP1\ !$938-1578 #product core protein p52 #status predicted #label !8CPP\ !$1579-1601 #product genome-linked protein VPg1 #status predicted !8#label GL1\ !$1602-1625 #product genome-linked protein VPg2 #status predicted !8#label GL2\ !$1626-1649 #product genome-linked protein VPg3 #status predicted !8#label GL3\ !$1650-1863 #product nonstructural protein p20b #status predicted !8#label NPB\ !$1864-2333 #product RNA-directed RNA polymerase #status !8predicted #label RRP SUMMARY #length 2333 #molecular-weight 259646 #checksum 7155 SEQUENCE /// ENTRY GNNY4F #type complete TITLE genome polyprotein - foot-and-mouth disease virus A (strain A12) CONTAINS coat protein VP1; coat protein VP2; coat protein VP3; coat protein VP4; core protein p14; core protein p19; core protein p41; core protein X; genome-linked protein VPg1; genome-linked protein VPg2; genome-linked protein VPg3; nonstructural protein p20a; proteinase (EC 3.4.-.-); RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name Aphthovirus A #common_name foot-and-mouth disease virus A DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Jul-1999 ACCESSIONS A25794 REFERENCE A25794 !$#authors Robertson, B.H.; Grubman, M.J.; Weddell, G.N.; Moore, D.M.; !1Welsh, J.D.; Fischer, T.; Dowbenko, D.J.; Yansura, D.G.; !1Small, B.; Kleid, D.G. !$#journal J. Virol. (1985) 54:651-660 !$#title Nucleotide and amino acid sequence coding for polypeptides !1of foot-and-mouth disease virus type A12. !$#cross-references MUID:85211015; PMID:2987518 !$#accession A25794 !'##molecule_type genomic RNA !'##residues 1-2332 ##label ROB !'##cross-references GB:M10975; NID:g210306; PIDN:AAA42593.1; !1PID:g210307 CLASSIFICATION #superfamily foot-and-mouth disease virus genome polyprotein KEYWORDS coat protein; core protein; genome-linked protein; !1hydrolase; nonstructural protein; nucleotidyltransferase; !1polyprotein; proteinase FEATURE !$1-216 #product nonstructural protein p20a #status predicted !8#label NPA\ !$217-285 #product coat protein VP4 #status predicted #label !8VP4\ !$286-503 #product coat protein VP2 #status predicted #label !8VP2\ !$504-723 #product coat protein VP3 #status predicted #label !8VP3\ !$724-937 #product coat protein VP1 #status predicted #label !8VP1\ !$938-953 #product core protein X #status predicted #label CPX\ !$954-1107 #product core protein p14 #status predicted #label !8C14\ !$1108-1425 #product core protein p41 #status predicted #label !8C41\ !$1426-1578 #product core protein p19 #status predicted #label !8C19\ !$1579-1601 #product genome-linked protein VPg1 #status predicted !8#label VG1\ !$1602-1625 #product genome-linked protein VPg2 #status predicted !8#label VG2\ !$1626-1649 #product genome-linked protein VPg3 #status predicted !8#label VG3\ !$1650-1862 #product proteinase #status predicted #label PTS\ !$1863-2332 #product RNA-directed RNA polymerase #status !8predicted #label RRP SUMMARY #length 2332 #molecular-weight 259408 #checksum 6669 SEQUENCE /// ENTRY GNWVTC #type complete TITLE genome polyprotein - hepatitis C virus CONTAINS capsid protein C; envelope protein M; hepacivirin (EC 3.4.21.98) (nonstructural protein NS3); major envelope protein E; nonstructural protein NS1; nonstructural protein NS2; nonstructural protein NS4a; nonstructural protein NS4b; nonstructural protein NS5 ORGANISM #formal_name hepatitis C virus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 19-Jan-2001 ACCESSIONS A38465 REFERENCE A38465 !$#authors Takamizawa, A.; Mori, C.; Fuke, I.; Manabe, S.; Murakami, !1S.; Fujita, J.; Onishi, E.; Andoh, T.; Yoshida, I.; Okayama, !1H. !$#journal J. Virol. (1991) 65:1105-1113 !$#title Structure and organization of the hepatitis C virus genome !1isolated from human carriers. !$#cross-references MUID:91140698; PMID:1847440 !$#accession A38465 !'##molecule_type genomic RNA !'##residues 1-3010 ##label TAK !'##cross-references EMBL:M58335; NID:g329770; PIDN:AAA72945.1; !1PID:g329771 CLASSIFICATION #superfamily hepatitis C virus genome polyprotein KEYWORDS ATP; capsid protein; envelope protein; glycoprotein; !1hydrolase; nonstructural protein; nucleotide binding; !1P-loop; polyprotein; serine proteinase; transmembrane !1protein FEATURE !$2-115 #product capsid protein C #status predicted #label !8CPC\ !$116-191 #product envelope protein M #status predicted #label !8EPM\ !$192-389 #product major envelope protein E #status predicted !8#label MEE\ !$390-729 #product nonstructural protein NS1 #status predicted !8#label NS1\ !$730-1006 #product nonstructural protein NS2 #status predicted !8#label NS2\ !$1007-1615 #product hepacivirin #status predicted #label NS3\ !$1230-1237 #region nucleotide-binding motif A (P-loop)\ !$1312-1317 #region nucleotide-binding motif B\ !$1316-1319 #region DEXH motif\ !$1616-1862 #product nonstructural protein NS4a #status predicted !8#label N4A\ !$1863-2013 #product nonstructural protein NS4b #status predicted !8#label N4B\ !$2014-3010 #product nonstructural protein NS5 #status predicted !8#label NS5\ !$196,209,234,250, !$305,325,417,423, !$430,448,532,540, !$556,576,623,645, !$1213,1255,2041, !$2077,2240,2529,2788 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 3010 #molecular-weight 327190 #checksum 7196 SEQUENCE /// ENTRY GNWVCJ #type complete TITLE genome polyprotein - hepatitis C virus (strain J) CONTAINS capsid protein C; envelope protein M; major envelope protein E; nonstructural protein NS1; nonstructural protein NS2; hepacivirin (EC 3.4.21.98) (nonstructural protein NS3); nonstructural protein NS4a; nonstructural protein NS4b; nonstructural protein NS5 ORGANISM #formal_name hepatitis C virus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 19-Jan-2001 ACCESSIONS A39253; PS0086 REFERENCE A39253 !$#authors Kato, N.; Hijikata, M.; Ootsuyama, Y.; Nakagawa, M.; !1Ohkoshi, S.; Sugimura, T.; Shimotohno, K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:9524-9528 !$#title Molecular cloning of the human hepatitis C virus genome from !1Japanese patients with non-A, non-B hepatitis. !$#cross-references MUID:91088550; PMID:2175903 !$#accession A39253 !'##molecule_type genomic RNA !'##residues 1-3010 ##label KAT !'##cross-references GB:D90208; NID:g221610; PIDN:BAA14233.1; !1PID:g221611 REFERENCE PS0085 !$#authors Kato, N.; Ohkoshi, S.; Shimotohno, K. !$#journal Proc. Jpn. Acad. (1989) 65B:219-223 !$#title Japanese isolates of the non-A, non-B hepatitis viral genome !1show sequence variations from the original isolate in the !1U.S.A. !$#accession PS0086 !'##molecule_type genomic RNA !'##residues 2650-2707 ##label KA2 !'##experimental_source Japanese isolate COMMENT The cleavage sites of this polyprotein have not been !1determined. CLASSIFICATION #superfamily hepatitis C virus genome polyprotein KEYWORDS ATP; glycoprotein; hydrolase; nucleotide binding; P-loop; !1polyprotein; serine proteinase; transmembrane protein FEATURE !$2-115 #product capsid protein C #status predicted #label !8CPC\ !$116-191 #product envelope protein M #status predicted #label !8EPM\ !$192-389 #product major envelope protein E #status predicted !8#label MEE\ !$390-729 #product nonstructural protein NS1 #status predicted !8#label NS1\ !$730-1006 #product nonstructural protein NS2 #status predicted !8#label NS2\ !$1007-1615 #product hepacivirin #status predicted #label NS3\ !$1230-1237 #region nucleotide-binding motif A (P-loop)\ !$1312-1317 #region nucleotide-binding motif B\ !$1316-1319 #region DEXH motif\ !$1616-1862 #product nonstructural protein NS4a #status predicted !8#label N4A\ !$1863-2013 #product nonstructural protein NS4b #status predicted !8#label N4B\ !$2014-3010 #product nonstructural protein NS5 #status predicted !8#label NS5\ !$196,209,234,250, !$305,325,417,423, !$430,448,532,556, !$576,623,645,1213, !$1255,2041,2077, !$2240,2788 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 3010 #molecular-weight 327018 #checksum 4397 SEQUENCE /// ENTRY A45573 #type complete TITLE genome polyprotein - hepatitis C virus (strain JT) CONTAINS capsid protein C; envelope protein M; hepacivirin (EC 3.4.21.98) (nonstructural protein NS3); major envelope protein E; nonstructural protein NS1; nonstructural protein NS2; nonstructural protein NS4a; nonstructural protein NS4b; nonstructural protein NS5 ORGANISM #formal_name hepatitis C virus DATE 19-May-2000 #sequence_revision 19-May-2000 #text_change 19-Jan-2001 ACCESSIONS A45573 REFERENCE A45573 !$#authors Tanaka, T.; Kato, N.; Nakagawa, M.; Ootsuyama, Y.; Cho, !1M.J.; Nakazawa, T.; Hijikata, M.; Ishimura, Y.; Shimotohno, !1K. !$#journal Virus Res. (1992) 23:39-53 !$#title Molecular cloning of hepatitis C virus genome from a single !1Japanese carrier: sequence variation within the same !1individual and among infected individuals. !$#cross-references MUID:92295714; PMID:1318627 !$#accession A45573 !'##status preliminary !'##molecule_type DNA !'##residues 1-3010 ##label TAN !'##cross-references GB:D11168; GB:D01171; NID:g221612; PIDN:BAA01943.1; !1PID:g221613 !'##experimental_source HCV-JT !'##note sequence extracted from NCBI backbone (NCBIN:106206, !1NCBIP:106207) CLASSIFICATION #superfamily hepatitis C virus genome polyprotein KEYWORDS ATP; glycoprotein; hydrolase; nucleotide binding; P-loop; !1polyprotein; serine proteinase; transmembrane protein FEATURE !$2-115 #product capsid protein C #status predicted #label !8CPC\ !$116-191 #product envelope protein M #status predicted #label !8EPM\ !$192-389 #product major envelope protein E #status predicted !8#label MEE\ !$390-729 #product nonstructural protein NS1 #status predicted !8#label NS1\ !$730-1006 #product nonstructural protein NS2 #status predicted !8#label NS2\ !$1007-1615 #product hepacivirin #status predicted #label NS3\ !$1230-1237 #region nucleotide-binding motif A (P-loop)\ !$1312-1317 #region nucleotide-binding motif B\ !$1316-1319 #region DEXH motif\ !$1616-1862 #product nonstructural protein NS4a #status predicted !8#label N4A\ !$1863-2013 #product nonstructural protein NS4b #status predicted !8#label N4B\ !$2014-3010 #product nonstructural protein NS5 #status predicted !8#label NS5 SUMMARY #length 3010 #molecular-weight 326574 #checksum 7499 SEQUENCE /// ENTRY S18030 #type complete TITLE genome polyprotein - hepatitis C virus (isolate JK1) CONTAINS capsid protein C; envelope protein M; hepacivirin (EC 3.4.21.98) (nonstructural protein NS3); major envelope protein E; nonstructural protein NS1; nonstructural protein NS2; nonstructural protein NS4a; nonstructural protein NS4b; nonstructural protein NS5 ORGANISM #formal_name hepatitis C virus #variety isolate JK1 DATE 19-May-2000 #sequence_revision 19-May-2000 #text_change 23-Mar-2001 ACCESSIONS S18030; S33570; A48332; S18029 REFERENCE S18028 !$#authors Honda, M.; Kaneko, S.; Masashi, U.; Kobayashi, K.; Murakami, !1S. !$#submission submitted to the EMBL Data Library, September 1991 !$#description A whole genome of hepatitis C virus cDNA was isolated from a !1single patient's liver tissue RNA. !$#accession S18030 !'##molecule_type genomic RNA !'##residues 1-3010 ##label HON !'##cross-references EMBL:X61596; NID:g59478; PIDN:CAA43793.1; !1PID:g59479 !'##experimental_source isolate JK1 from an individual REFERENCE A48332 !$#authors Honda, M.; Kaneko, S.; Unoura, M.; Kobayashi, K.; Murakami, !1S. !$#journal Arch. Virol. (1993) 128:163-169 !$#title Sequence analysis of putative structural regions of !1hepatitis C virus isolated from 5 Japanese patients with !1hepatocellular carcinoma. !$#cross-references MUID:93119270; PMID:8380322 !$#accession S33570 !'##molecule_type genomic RNA !'##residues 1-547,'T',549-621,'V',623-624,'S',626-652,'DL',655-761,'T', !1763-782 ##label HOW !'##cross-references EMBL:X61591 !'##note this sequence is inconsistent with the nucleotide translation !'##note the authors translated the codon AGG for residue 43 as Pro, TGG !1for residue 320 as Asp, GAT for residue 321 as Trp, GGT for !1residue 470 as Pro, CCC for residue 471 as Gly, TAC for !1residue 701 as Trp, and TTC for residue 771 as Ser !'##note sequence extracted from NCBI backbone (NCBIN:121747, !1NCBIP:121748) CLASSIFICATION #superfamily hepatitis C virus genome polyprotein KEYWORDS ATP; glycoprotein; hydrolase; nucleotide binding; P-loop; !1polyprotein; serine proteinase; transmembrane protein FEATURE !$2-115 #product capsid protein C #status predicted #label !8CPC\ !$116-191 #product envelope protein M #status predicted #label !8EPM\ !$192-389 #product major envelope protein E #status predicted !8#label MEE\ !$390-729 #product nonstructural protein NS1 #status predicted !8#label NS1\ !$730-1006 #product nonstructural protein NS2 #status predicted !8#label NS2\ !$1007-1615 #product hepacivirin #status predicted #label NS3\ !$1230-1237 #region nucleotide-binding motif A (P-loop)\ !$1312-1317 #region nucleotide-binding motif B\ !$1316-1319 #region DEXH motif\ !$1616-1862 #product nonstructural protein NS4a #status predicted !8#label N4A\ !$1863-2013 #product nonstructural protein NS4b #status predicted !8#label N4B\ !$2014-3010 #product nonstructural protein NS5 #status predicted !8#label NS5\ !$196,209,234,250, !$305,417,423,448, !$532,540,556,576, !$623,645 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 3010 #molecular-weight 327179 #checksum 7818 SEQUENCE /// ENTRY GNWVTW #type complete TITLE genome polyprotein - hepatitis C virus (strain Taiwan) CONTAINS capsid protein C; envelope protein M; hepacivirin (EC 3.4.21.98) (nonstructural protein NS3); major envelope protein E; nonstructural protein NS1; nonstructural protein NS2; nonstructural protein NS4a; nonstructural protein NS4b; nonstructural protein NS5 ORGANISM #formal_name hepatitis C virus #note host Homo sapiens (man) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-Jan-2001 ACCESSIONS A40244 REFERENCE A40244 !$#authors Chen, P.J.; Lin, M.H.; Tai, K.F.; Liu, P.C.; Lin, C.J.; !1Chen, D.S. !$#journal Virology (1992) 188:102-113 !$#title The Taiwanese hepatitis C virus genome: sequence !1determination and mapping the 5' termini of viral genomic !1and antigenomic RNA. !$#cross-references MUID:92230206; PMID:1314449 !$#accession A40244 !'##molecule_type genomic RNA !'##residues 1-3010 ##label CHE !'##cross-references GB:M84754 CLASSIFICATION #superfamily hepatitis C virus genome polyprotein KEYWORDS ATP; capsid protein; envelope protein; glycoprotein; !1hydrolase; nonstructural protein; nucleotide binding; !1P-loop; polyprotein; serine proteinase FEATURE !$1-115 #product capsid protein C #status predicted #label !8CPC\ !$116-191 #product envelope protein M #status predicted #label !8EPM\ !$192-389 #product major envelope protein E #status predicted !8#label MEE\ !$390-729 #product nonstructural protein NS1 #status predicted !8#label NS1\ !$730-1006 #product nonstructural protein NS2 #status predicted !8#label NS2\ !$1007-1615 #product hepacivirin #status predicted #label NS3\ !$1230-1237 #region nucleotide-binding motif A (P-loop)\ !$1312-1317 #region nucleotide-binding motif B\ !$1316-1319 #region DEXH motif\ !$1616-1862 #product nonstructural protein NS4a #status predicted !8#label N4A\ !$1863-2013 #product nonstructural protein NS4b #status predicted !8#label N4B\ !$2014-3010 #product nonstructural protein NS5 #status predicted !8#label NS5\ !$196,209,233,234, !$250,305,325,417, !$423,430,448,532, !$540,556,576,623, !$645,1213,1255,2041, !$2077,2240,2529,2788 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 3010 #molecular-weight 327048 #checksum 7835 SEQUENCE /// ENTRY GNWVC3 #type complete TITLE genome polyprotein - hepatitis C virus (strain HCV-1) CONTAINS capsid protein C; envelope protein M; hepacivirin (EC 3.4.21.98) (nonstructural protein NS3); major envelope protein E; nonstructural protein NS1; nonstructural protein NS2; nonstructural protein NS4a; nonstructural protein NS4b; nonstructural protein NS5 ORGANISM #formal_name hepatitis C virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 19-Jan-2001 ACCESSIONS A39166; PQ0403; PQ0404 REFERENCE A39166 !$#authors Choo, Q.L.; Richman, K.H.; Han, J.H.; Berger, K.; Lee, C.; !1Dong, C.; Gallegos, C.; Coit, D.; Medina-Selby, A.; Barr, !1P.J.; Weiner, A.J.; Bradley, D.W.; Kuo, G.; Houghton, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:2451-2455 !$#title Genetic organization and diversity of the hepatitis C virus. !$#cross-references MUID:91172826; PMID:1848704 !$#accession A39166 !'##molecule_type mRNA !'##residues 1-3011 ##label CHO !'##cross-references GB:M62321; NID:g329873; PIDN:AAA45676.1; !1PID:g329874 REFERENCE PQ0393 !$#authors Chan, S.W.; McOmish, F.; Holmes, E.C.; Dow, B.; Peutherer, !1J.F.; Follett, E.; Yap, P.L.; Simmonds, P. !$#journal J. Gen. Virol. (1992) 73:1131-1141 !$#title Analysis of a new hepatitis C virus type and its !1phylogenetic relationship to existing variants. !$#cross-references MUID:92268871; PMID:1316939 !$#accession PQ0403 !'##molecule_type genomic RNA !'##residues 1577-1633 ##label CHA !'##cross-references DDBJ:D10128 !'##experimental_source isolates E-b16 !$#accession PQ0404 !'##status preliminary !'##molecule_type genomic RNA !'##residues 1577-1633 ##label CH2 !'##experimental_source isolates E-b17 CLASSIFICATION #superfamily hepatitis C virus genome polyprotein KEYWORDS ATP; capsid protein; envelope protein; glycoprotein; !1hydrolase; nonstructural protein; nucleotide binding; !1P-loop; polyprotein; serine proteinase; transmembrane !1protein FEATURE !$1-115 #product capsid protein C #status predicted #label !8CPC\ !$116-191 #product envelope protein M #status predicted #label !8EPM\ !$192-389 #product major envelope protein E #status predicted !8#label MEE\ !$390-729 #product nonstructural protein NS1 #status predicted !8#label NS1\ !$730-1006 #product nonstructural protein NS2 #status predicted !8#label NS2\ !$1007-1615 #product hepacivirin #status predicted #label NS3\ !$1230-1237 #region nucleotide-binding motif A (P-loop)\ !$1312-1317 #region nucleotide-binding motif B\ !$1316-1319 #region DEXH motif\ !$1616-1862 #product nonstructural protein NS4a #status predicted !8#label N4A\ !$1863-2013 #product nonstructural protein NS4b #status predicted !8#label N4B\ !$2014-3011 #product nonstructural protein NS5 #status predicted !8#label NS5\ !$196,209,234,305, !$325,417,423,430, !$448,476,532,540, !$556,576,623,645, !$1213,1255,2041, !$2077,2240,2364, !$2550,2789 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 3011 #molecular-weight 327199 #checksum 8610 SEQUENCE /// ENTRY GNWVCH #type complete TITLE genome polyprotein - hepatitis C virus (strain H) CONTAINS capsid protein C; envelope protein M; hepacivirin (EC 3.4.21.98) (nonstructural protein NS3); major envelope protein E; nonstructural protein NS1; nonstructural protein NS2; nonstructural protein NS4a; nonstructural protein NS4b; nonstructural protein NS5 ORGANISM #formal_name hepatitis C virus #note host Homo sapiens (man) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-Jan-2001 ACCESSIONS A36814; A41546 REFERENCE A36814 !$#authors Inchauspe, G.; Zebedee, S.; Lee, D.H.; Sugitani, M.; Nasoff, !1M.; Prince, A.M. !$#submission submitted to GenBank, July 1992 !$#description Genomic structure of the human prototype strain H of !1hepatitis C virus: comparison with American and Japanese !1isolates. !$#accession A36814 !'##molecule_type genomic RNA !'##residues 1-3011 ##label INC !'##cross-references GB:M67463; NID:g329737; PIDN:AAA45534.1; !1PID:g329738 REFERENCE A41546 !$#authors Inchauspe, G.; Zebedee, S.; Lee, D.H.; Sugitani, M.; Nasoff, !1M.; Prince, A.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:10292-10296 !$#title Genomic structure of the human prototype strain H of !1hepatitis C virus: comparison with American and Japanese !1isolates. !$#cross-references MUID:92052256; PMID:1658800 !$#contents annotation !$#note neither amino acid nor nucleotide sequence is given CLASSIFICATION #superfamily hepatitis C virus genome polyprotein KEYWORDS ATP; capsid protein; envelope protein; glycoprotein; !1hydrolase; nonstructural protein; nucleotide binding; !1P-loop; polyprotein; serine proteinase; transmembrane !1protein FEATURE !$1-115 #product capsid protein C #status predicted #label !8CPC\ !$116-191 #product envelope protein M #status predicted #label !8EPM\ !$192-389 #product major envelope protein E #status predicted !8#label MEE\ !$390-729 #product nonstructural protein NS1 #status predicted !8#label NS1\ !$730-1006 #product nonstructural protein NS2 #status predicted !8#label NS2\ !$1007-1615 #product hepacivirin #status predicted #label NS3\ !$1230-1237 #region nucleotide-binding motif A (P-loop)\ !$1312-1317 #region nucleotide-binding motif B\ !$1316-1319 #region DEXH motif\ !$1616-1862 #product nonstructural protein NS4a #status predicted !8#label N4A\ !$1863-2013 #product nonstructural protein NS4b #status predicted !8#label N4B\ !$2014-3011 #product nonstructural protein NS5 #status predicted !8#label NS5\ !$196,209,234,305, !$325,417,423,430, !$448,476,532,540, !$556,576,623,645, !$1213,1255,2041, !$2240,2364,2789 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 3011 #molecular-weight 327143 #checksum 438 SEQUENCE /// ENTRY S40770 #type complete TITLE genome polyprotein - hepatitis C virus CONTAINS capsid protein C; envelope protein M; hepacivirin (EC 3.4.21.98) (nonstructural protein NS3); major envelope protein E; nonstructural protein NS1; nonstructural protein NS2; nonstructural protein NS4a; nonstructural protein NS4b; nonstructural protein NS5 ORGANISM #formal_name hepatitis C virus DATE 19-May-2000 #sequence_revision 19-May-2000 #text_change 19-Jan-2001 ACCESSIONS S40770; PC1285 REFERENCE S40770 !$#authors Okamoto, H. !$#submission submitted to the EMBL Data Library, March 1992 !$#accession S40770 !'##molecule_type genomic RNA !'##residues 1-3011 ##label OKA !'##cross-references EMBL:D10749; NID:g221586; PIDN:BAA01582.1; !1PID:g221587 REFERENCE PC1284 !$#authors Okamoto, H.; Okada, S.; Sugiyama, Y.; Yotsumoto, S.; Tanaka, !1T.; Yoshizawa, H.; Tsuda, F.; Miyakawa, Y.; Mayumi, M. !$#journal Jpn. J. Exp. Med. (1990) 60:167-177 !$#title The 5'-terminal sequence of the hepatitis C virus genome. !$#cross-references MUID:91013116; PMID:2170712 !$#accession PC1285 !'##molecule_type genomic RNA !'##residues 1-513 ##label OK2 !'##cross-references GB:D00831; NID:g221511; PIDN:BAA00705.1; !1PID:g221512 !'##experimental_source isolate HC-J1 CLASSIFICATION #superfamily hepatitis C virus genome polyprotein KEYWORDS ATP; glycoprotein; hydrolase; nucleotide binding; P-loop; !1polyprotein; serine proteinase; transmembrane protein FEATURE !$2-115 #product capsid protein C #status predicted #label !8CPC\ !$116-191 #product envelope protein M #status predicted #label !8EPM\ !$192-389 #product major envelope protein E #status predicted !8#label MEE\ !$390-729 #product nonstructural protein NS1 #status predicted !8#label NS1\ !$730-1006 #product nonstructural protein NS2 #status predicted !8#label NS2\ !$1007-1615 #product hepacivirin #status predicted #label NS3\ !$1230-1237 #region nucleotide-binding motif A (P-loop)\ !$1312-1317 #region nucleotide-binding motif B\ !$1316-1319 #region DEXH motif\ !$1616-1862 #product nonstructural protein NS4a #status predicted !8#label N4A\ !$1863-2013 #product nonstructural protein NS4b #status predicted !8#label N4B\ !$2014-3011 #product nonstructural protein NS5 #status predicted !8#label NS5 SUMMARY #length 3011 #molecular-weight 327114 #checksum 5911 SEQUENCE /// ENTRY JC5620 #type complete TITLE genome polyprotein - hepatitis C virus (isolate EUH1480) CONTAINS capsid protein C; envelope protein M; hepacivirin (EC 3.4.21.98) (nonstructural protein NS3); major envelope protein E; nonstructural protein NS1; nonstructural protein NS2; nonstructural protein NS4a; nonstructural protein NS4b; nonstructural protein NS5 ORGANISM #formal_name hepatitis C virus DATE 19-May-2000 #sequence_revision 19-May-2000 #text_change 19-Jan-2001 ACCESSIONS JC5620 REFERENCE JC5620 !$#authors Chamberlain, R.W.; Adams, N.J.; Taylor, L.A.; Simmonds, P.; !1Elliott, R.M. !$#journal Biochem. Biophys. Res. Commun. (1997) 236:44-49 !$#title The complete coding sequence of hepatitis C virus genotype !15a, the predominant genotype in South Africa. !$#cross-references MUID:97366593; PMID:9223423 !$#accession JC5620 !'##molecule_type mRNA !'##residues 1-3014 ##label CHA !'##cross-references GB:Y13184 !'##experimental_source genotype 5a, which predominates in South Africa !'##note the translation of the nucleotide sequence is not complete in !1this paper CLASSIFICATION #superfamily hepatitis C virus genome polyprotein KEYWORDS ATP; glycoprotein; hydrolase; nucleotide binding; P-loop; !1polyprotein; serine proteinase; transmembrane protein FEATURE !$2-115 #product capsid protein C #status predicted #label !8CPC\ !$116-191 #product envelope protein M #status predicted #label !8EPM\ !$192-389 #product major envelope protein E #status predicted !8#label MEE\ !$384-408 #region hypervariable #status predicted\ !$390-730 #product nonstructural protein NS1 #status predicted !8#label NS1\ !$731-1007 #product nonstructural protein NS2 #status predicted !8#label NS2\ !$1008-1616 #product hepacivirin #status predicted #label NS3\ !$1231-1238 #region nucleotide-binding motif A (P-loop)\ !$1313-1318 #region nucleotide-binding motif B\ !$1317-1320 #region DEXH motif\ !$1617-1863 #product nonstructural protein NS4a #status predicted !8#label N4A\ !$1864-2014 #product nonstructural protein NS4b #status predicted !8#label N4B\ !$2015-3014 #product nonstructural protein NS5 #status predicted !8#label NS5\ !$2210-2249 #region interferon sensitivity determining #status !8predicted SUMMARY #length 3014 #molecular-weight 327750 #checksum 8693 SEQUENCE /// ENTRY JQ1303 #type complete TITLE genome polyprotein - hepatitis C virus (isolate HC-J6) CONTAINS capsid protein C; envelope protein M; hepacivirin (EC 3.4.21.98) (nonstructural protein NS3); major envelope protein E; nonstructural protein NS1; nonstructural protein NS2; nonstructural protein NS4a; nonstructural protein NS4b; nonstructural protein NS5 ORGANISM #formal_name hepatitis C virus DATE 19-May-2000 #sequence_revision 19-May-2000 #text_change 17-Nov-2000 ACCESSIONS JQ1303 REFERENCE JQ1303 !$#authors Okamoto, H.; Okada, S.; Sugiyama, Y.; Kurai, K.; Iizuka, H.; !1Machida, A.; Miyakawa, Y.; Mayumi, M. !$#journal J. Gen. Virol. (1991) 72:2697-2704 !$#title Nucleotide sequence of the genomic RNA of hepatitis C virus !1isolated from a human carrier: comparison with reported !1isolates for conserved and divergent regions. !$#cross-references MUID:92044440; PMID:1658196 !$#accession JQ1303 !'##molecule_type genomic RNA !'##residues 1-3033 ##label OKA !'##cross-references GB:D00944; NID:g221650; PIDN:BAA00792.1; !1PID:g221651 !'##experimental_source isolate HC-J6 from a Japanese individual CLASSIFICATION #superfamily hepatitis C virus genome polyprotein KEYWORDS ATP; glycoprotein; hydrolase; P-loop; polyprotein; serine !1proteinase; transmembrane protein FEATURE !$2-115 #product capsid protein C #status predicted #label !8CPC\ !$116-191 #product envelope protein M #status predicted #label !8EPM\ !$192-389 #product major envelope protein E #status predicted !8#label MEE\ !$390-733 #product nonstructural protein NS1 #status predicted !8#label NS1\ !$734-1010 #product nonstructural protein NS2 #status predicted !8#label NS2\ !$1011-1619 #product hepacivirin #status predicted #label NS3\ !$1316-1321 #region nucleotide-binding motif B\ !$1320-1323 #region DEXH motif\ !$1620-1866 #product nonstructural protein NS4a #status predicted !8#label N4A\ !$1867-2017 #product nonstructural protein NS4b #status predicted !8#label N4B\ !$2018-3033 #product nonstructural protein NS5 #status predicted !8#label NO5\ !$196,209,234,305, !$325,417,423,430, !$448,477,534,542, !$558,578,627,649, !$1091,1217,1259, !$2038,2811 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 3033 #molecular-weight 329166 #checksum 17 SEQUENCE /// ENTRY GNWVJ8 #type complete TITLE genome polyprotein - hepatitis C virus (strain HC-J8) CONTAINS capsid protein C; envelope protein M; hepacivirin (EC 3.4.21.98) (nonstructural protein NS3); major envelope protein E; nonstructural protein NS1; nonstructural protein NS2; nonstructural protein NS4a; nonstructural protein NS4b; nonstructural protein NS5 ORGANISM #formal_name hepatitis C virus DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-Jan-2001 ACCESSIONS A40250; PQ0397; PQ0559 REFERENCE A40250 !$#authors Okamoto, H.; Kurai, K.; Okada, S.I.; Yamamoto, K.; Lizuka, !1H.; Tanaka, T.; Fukuda, S.; Tsuda, F.; Mishiro, S. !$#journal Virology (1992) 188:331-341 !$#title Full-length sequence of a hepatitis C virus genome having !1poor homology to reported isolates: comparative study of !1four distinct genotypes. !$#cross-references MUID:92230232; PMID:1314459 !$#accession A40250 !'##molecule_type genomic RNA !'##residues 1-3033 ##label OKA !'##cross-references GB:D10988; GB:D01221; NID:g221608; PIDN:BAA01761.1; !1PID:g221609 REFERENCE PQ0393 !$#authors Chan, S.W.; McOmish, F.; Holmes, E.C.; Dow, B.; Peutherer, !1J.F.; Follett, E.; Yap, P.L.; Simmonds, P. !$#journal J. Gen. Virol. (1992) 73:1131-1141 !$#title Analysis of a new hepatitis C virus type and its !1phylogenetic relationship to existing variants. !$#cross-references MUID:92268871; PMID:1316939 !$#accession PQ0397 !'##molecule_type genomic RNA !'##residues 2678-2754 ##label CHA !'##cross-references DDBJ:D10134 !'##experimental_source isolate E-b12 REFERENCE PQ0554 !$#authors Kato, N.; Ootsuyama, Y.; Ohkoshi, S.; Nakazawa, T.; Mori, !1S.; Hijikata, M.; Shimotohno, K. !$#journal Biochem. Biophys. Res. Commun. (1991) 181:279-285 !$#title Distribution of plural HCV types in Japan. !$#cross-references MUID:92068204; PMID:1720309 !$#accession PQ0559 !'##molecule_type mRNA !'##residues 2678-2729 ##label KAT !'##cross-references GB:D10562; GB:D90518; NID:g221523; PIDN:BAA01418.1; !1PID:g221524 CLASSIFICATION #superfamily hepatitis C virus genome polyprotein KEYWORDS ATP; capsid protein; envelope protein; glycoprotein; !1hydrolase; nonstructural protein; nucleotide binding; !1P-loop; polyprotein; serine proteinase; transmembrane !1protein FEATURE !$1-115 #product capsid protein C #status predicted #label !8CPC\ !$116-191 #product envelope protein M #status predicted #label !8EPM\ !$192-389 #product major envelope protein E #status predicted !8#label MEE\ !$390-733 #product nonstructural protein NS1 #status predicted !8#label NS1\ !$734-1010 #product nonstructural protein NS2 #status predicted !8#label NS2\ !$1011-1619 #product hepacivirin #status predicted #label NS3\ !$1234-1241 #region nucleotide-binding motif A (P-loop)\ !$1316-1321 #region nucleotide-binding motif B\ !$1320-1323 #region DEXH motif\ !$1620-1866 #product nonstructural protein NS4a #status predicted !8#label N4A\ !$1867-2017 #product nonstructural protein NS4b #status predicted !8#label N4B\ !$2018-3033 #product nonstructural protein NS5 #status predicted !8#label NS5\ !$196,209,233,299, !$305,417,423,430, !$448,477,534,542, !$558,578,627,649, !$1091,1217,1259, !$2038,2359,2811 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 3033 #molecular-weight 330179 #checksum 9378 SEQUENCE /// ENTRY GNWVY #type complete TITLE genome polyprotein - yellow fever virus (strain 17D) CONTAINS capsid protein C; envelope protein M; major envelope protein E; nonstructural protein NS1; nonstructural protein NS2a; nonstructural protein NS2b; nonstructural protein NS3; nonstructural protein NS4a; nonstructural protein NS4b; nonstructural protein NS5 ORGANISM #formal_name yellow fever virus DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 19-Jan-2001 ACCESSIONS A03914 REFERENCE A03914 !$#authors Rice, C.M.; Lenches, E.M.; Eddy, S.R.; Shin, S.J.; Sheets, !1R.L.; Strauss, J.H. !$#journal Science (1985) 229:726-733 !$#title Nucleotide sequence of yellow fever virus: implications for !1flavivirus gene expression and evolution. !$#cross-references MUID:85272570; PMID:4023707 !$#accession A03914 !'##molecule_type genomic RNA !'##residues 1-3411 ##label RIC !'##cross-references GB:X03700; GB:K02749; NID:g59338; PIDN:CAA27332.1; !1PID:g59339 CLASSIFICATION #superfamily yellow fever virus genome polyprotein KEYWORDS ATP; capsid protein; envelope protein; glycoprotein; !1nonstructural protein; nucleotide binding; P-loop; !1polyprotein; transmembrane protein FEATURE !$2-210 #product capsid protein C #status predicted #label !8CPC\ !$211-285 #product envelope protein M #status predicted #label !8EPM\ !$249-269 #domain transmembrane #status predicted #label TM1\ !$271-285 #domain transmembrane #status predicted #label TM2\ !$286-778 #product major envelope protein E #status predicted !8#label MEE\ !$740-753 #domain transmembrane #status predicted #label TM3\ !$755-778 #domain transmembrane #status predicted #label TM4\ !$779-1187 #product nonstructural protein NS1 #status predicted !8#label NS1\ !$1159-1180 #domain transmembrane #status predicted #label TM5\ !$1188-1354 #product nonstructural protein NS2a #status predicted !8#label N2A\ !$1355-1484 #product nonstructural protein NS2b #status predicted !8#label N2B\ !$1485-2107 #product nonstructural protein NS3 #status predicted !8#label NS3\ !$1682-1689 #region nucleotide-binding motif A (P-loop)\ !$1769-1774 #region nucleotide-binding motif B\ !$1773-1776 #region DEAH motif\ !$2108-2394 #product nonstructural protein NS4a #status predicted !8#label N4A\ !$2395-2506 #product nonstructural protein NS4b #status predicted !8#label N4B\ !$2507-3411 #product nonstructural protein NS5 #status predicted !8#label NS5\ !$134,150,172,266, !$594,755,908,986, !$1796,2062,2320, !$2346,2408,2467, !$2720,2734,2740 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 3411 #molecular-weight 379516 #checksum 8719 SEQUENCE /// ENTRY GNWVYP #type complete TITLE genome polyprotein - yellow fever virus (strain Pasteur 17D-204) CONTAINS capsid protein C; envelope protein M; major envelope protein E; nonstructural protein NS1; nonstructural protein NS2a; nonstructural protein NS2b; nonstructural protein NS3; nonstructural protein NS4a; nonstructural protein NS4b; nonstructural protein NS5 ORGANISM #formal_name yellow fever virus DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 19-Jan-2001 ACCESSIONS S07757 REFERENCE S07757 !$#authors Dupuy, A.; Despres, P.; Cahour, A.; Girard, M.; Bouloy, M. !$#journal Nucleic Acids Res. (1989) 17:3989 !$#title Nucleotide sequence comparison of the genome of two 17D-204 !1yellow fever vaccines. !$#cross-references MUID:89282413; PMID:2734112 !$#accession S07757 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type genomic RNA !'##residues 1-3411 ##label DUP !'##cross-references EMBL:X15062; NID:g62289; PIDN:CAB37419.1; !1PID:g4456986 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1989, in computer-readable form CLASSIFICATION #superfamily yellow fever virus genome polyprotein KEYWORDS ATP; capsid protein; envelope protein; glycoprotein; !1nonstructural protein; nucleotide binding; P-loop; !1polyprotein; transmembrane protein FEATURE !$2-210 #product capsid protein C #status predicted #label !8CPC\ !$105-125 #domain transmembrane #status predicted #label TM1\ !$211-285 #product envelope protein M #status predicted #label !8EPM\ !$271-289 #domain transmembrane #status predicted #label TM2\ !$286-778 #product major envelope protein E #status predicted !8#label MEE\ !$736-753 #domain transmembrane #status predicted #label TM3\ !$756-778 #domain transmembrane #status predicted #label TM4\ !$779-1187 #product nonstructural protein NS1 #status predicted !8#label NS1\ !$1133-1151 #domain transmembrane #status predicted #label TM5\ !$1160-1179 #domain transmembrane #status predicted #label TM6\ !$1188-1354 #product nonstructural protein NS2a #status predicted !8#label N2A\ !$1355-1484 #product nonstructural protein NS2b #status predicted !8#label N2B\ !$1485-2107 #product nonstructural protein NS3 #status predicted !8#label NS3\ !$1682-1689 #region nucleotide-binding motif A (P-loop)\ !$1769-1774 #region nucleotide-binding motif B\ !$1773-1776 #region DEAH motif\ !$2108-2394 #product nonstructural protein NS4a #status predicted !8#label N4A\ !$2395-2506 #product nonstructural protein NS4b #status predicted !8#label N4B\ !$2507-3411 #product nonstructural protein NS5 #status predicted !8#label NS5\ !$134,150,172,594, !$908,986,1796,2062, !$2320,2346,2408, !$2467,2720,2734,2740 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 3411 #molecular-weight 379528 #checksum 8417 SEQUENCE /// ENTRY GNWVY8 #type fragment TITLE genome polyprotein - yellow fever virus (strain 1899/81) (fragment) CONTAINS amino end of nonstructural protein NS1; capsid protein C; envelope protein M; major envelope protein E ORGANISM #formal_name yellow fever virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 19-Jan-2001 ACCESSIONS JU0374 REFERENCE JU0374 !$#authors Ballinger-Crabtree, M.E.; Miller, B.R. !$#journal J. Gen. Virol. (1990) 71:2115-2121 !$#title Partial nucleotide sequence of South American yellow fever !1virus strain 1899/81: structural proteins and NS1. !$#cross-references MUID:91011358; PMID:2145394 !$#accession JU0374 !'##molecule_type genomic RNA !'##residues 1-1163 ##label BAL !'##cross-references GB:D14458; GB:D00739; NID:g222777; PIDN:BAA03355.1; !1PID:g222778 CLASSIFICATION #superfamily yellow fever virus genome polyprotein KEYWORDS capsid protein; envelope protein; glycoprotein; !1nonstructural protein; nucleotide binding; P-loop; !1polyprotein; transmembrane protein FEATURE !$2-121 #product capsid protein C #status predicted #label !8CAP\ !$106-122 #domain transmembrane #status predicted #label TM1\ !$122-285 #product envelope protein M #status predicted #label !8PRM\ !$251-267 #domain transmembrane #status predicted #label TM2\ !$271-287 #domain transmembrane #status predicted #label TM3\ !$286-778 #product major envelope protein E #status predicted !8#label ENP\ !$733-753 #domain transmembrane #status predicted #label TM4\ !$762-778 #domain transmembrane #status predicted #label TM5\ !$779-1163 #product nonstructural protein NS1 (fragment) #status !8predicted #label NS1\ !$1068-1075 #region nucleotide-binding motif A (P-loop)\ !$1133-1151 #domain transmembrane #status predicted #label TM6\ !$134,150,172,266, !$554,594,755,908,986 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1163 #checksum 7170 SEQUENCE /// ENTRY GNWVWV #type complete TITLE genome polyprotein - West Nile virus CONTAINS core protein V2; membrane-associated glycoprotein NV2 precursor; membrane-associated nonglycosylated protein V1; membrane-associated protein V3 precursor; nonstructural protein NV4 precursor; nonstructural protein NV5 ORGANISM #formal_name West Nile virus DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 19-Jan-2001 ACCESSIONS A25256 REFERENCE A25256 !$#authors Castle, E.; Leidner, U.; Nowak, T.; Wengler, G.; Wengler, G. !$#journal Virology (1986) 149:10-26 !$#title Primary structure of the West Nile flavivirus genome region !1coding for all nonstructural proteins. !$#cross-references MUID:86124703; PMID:3753811 !$#accession A25256 !'##molecule_type genomic RNA !'##residues 1-3430 ##label CAS !'##cross-references GB:M10103; GB:M12294; NID:g336167; PIDN:AAA48498.1; !1PID:g336168 !'##note parts of this sequence, including the amino ends of the mature !1proteins, were determined by protein sequencing CLASSIFICATION #superfamily yellow fever virus genome polyprotein KEYWORDS ATP; core protein; glycoprotein; membrane-associated !1protein; nucleotide binding; P-loop; polyprotein FEATURE !$1-92 #product core protein V2 #status predicted #label !8CV2\ !$105-233 #product membrane-associated glycoprotein NV2 !8precursor #status predicted #label NV2\ !$105-123 #domain nonterminal signal sequence #status predicted !8#label 2SS\ !$124-233 #product membrane-associated glycoprotein NV2 #status !8predicted #label 2NV\ !$216-233 #product membrane-associated nonglycosylated protein !8V1 #status predicted #label NV1\ !$275-787 #product membrane-associated glycoprotein V3 !8precursor #status predicted #label NV3\ !$275-290 #domain nonterminal signal sequence #status predicted !8#label 3SS\ !$291-787 #product membrane-associated glycoprotein V3 #status !8predicted #label 3NV\ !$788-2109 #product nonstructural protein NV4 #status predicted !8#label NV4\ !$1695-1702 #region nucleotide-binding motif A (P-loop)\ !$1782-1787 #region nucleotide-binding motif B\ !$1786-1789 #region DEAH motif\ !$2580-3427 #product nonstructural protein NV5 #status predicted !8#label NV5\ !$138,917,962,994, !$1289,1659,1966, !$2336,2459,2489, !$2573,2739,2759, !$2864,2902 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 3430 #molecular-weight 379627 #checksum 9721 SEQUENCE /// ENTRY GNWVKV #type complete TITLE genome polyprotein - Kunjin virus (strain MRM61C) CONTAINS capsid protein C; envelope protein E; membrane protein M; nonstructural protein NS1; nonstructural protein NS2a; nonstructural protein NS2b; nonstructural protein NS3; nonstructural protein NS4a; nonstructural protein NS4b; nonstructural protein NS5 ORGANISM #formal_name Kunjin virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 19-Jan-2001 ACCESSIONS A28697 REFERENCE A28697 !$#authors Coia, G.; Parker, M.D.; Speight, G.; Byrne, M.E.; Westaway, !1E.G. !$#journal J. Gen. Virol. (1988) 69:1-21 !$#title Nucleotide and complete amino acid sequences of Kunjin !1virus: definitive gene order and characteristics of the !1virus-specified proteins. !$#cross-references MUID:88089524; PMID:2826659 !$#accession A28697 !'##molecule_type genomic RNA !'##residues 1-3433 ##label COI !'##cross-references GB:D00246; NID:g221966; PIDN:BAA00176.1; !1PID:g221967 CLASSIFICATION #superfamily yellow fever virus genome polyprotein KEYWORDS ATP; capsid protein; envelope protein; membrane protein; !1nonstructural protein; nucleotide binding; P-loop; !1polyprotein FEATURE !$2-123 #product capsid protein C #status predicted #label !8CPC\ !$124-290 #product membrane protein M precursor #status !8predicted #label MPP\ !$124-215 #domain nonterminal signal sequence #status predicted !8#label SIG\ !$216-290 #product membrane protein M #status predicted #label !8MPM\ !$291-791 #product envelope protein E #status predicted #label !8EPE\ !$792-1143 #product nonstructural protein NS1 #status predicted !8#label NS1\ !$1144-1374 #product nonstructural protein NS2a #status predicted !8#label N2A\ !$1375-1505 #product nonstructural protein NS2b #status predicted !8#label N2B\ !$1506-2124 #product nonstructural protein NS3 #status predicted !8#label NS3\ !$1699-1706 #region nucleotide-binding motif A (P-loop)\ !$1786-1791 #region nucleotide-binding motif B\ !$1790-1793 #region DEAH motif\ !$2125-2273 #product nonstructural protein NS4a #status predicted !8#label N4A\ !$2274-2528 #product nonstructural protein NS4b #status predicted !8#label N4B\ !$2529-3433 #product nonstructural protein NS5 #status predicted !8#label NS5 SUMMARY #length 3433 #molecular-weight 381366 #checksum 8215 SEQUENCE /// ENTRY GNWVJE #type complete TITLE genome polyprotein - Japanese encephalitis virus (strain JaOArS982 wild type) CONTAINS capsid protein C; envelope protein E; membrane protein M; nonstructural protein NS1; nonstructural protein NS2a; nonstructural protein NS2b; nonstructural protein NS3; nonstructural protein NS4a; nonstructural protein NS4b; nonstructural protein NS5 ORGANISM #formal_name Japanese encephalitis virus DATE 30-Jun-1988 #sequence_revision 30-Sep-1989 #text_change 19-Jan-2001 ACCESSIONS A27403; A48387; A26465 REFERENCE A94367 !$#authors Sumiyoshi, H.; Mori, C.; Fuke, I.; Morita, K.; Kuhara, S.; !1Kondou, J.; Kikuchi, Y.; Nagamatu, H.; Igarashi, A. !$#journal Virology (1987) 161:497-510 !$#title Complete nucleotide sequence of the Japanese encephalitis !1virus genome RNA. !$#cross-references MUID:88072090; PMID:3686827 !$#accession A27403 !'##molecule_type genomic RNA !'##residues 1-3432 ##label SUM !'##cross-references GB:M18370; NID:g331329; PIDN:AAA81554.1; !1PID:g331330 REFERENCE A48387 !$#authors Chen, W.R.; Rico-Hesse, R.; Tesh, R.B. !$#journal Am. J. Trop. Med. Hyg. (1992) 47:61-69 !$#title A new genotype of Japanese encephalitis virus from !1Indonesia. !$#cross-references MUID:92344001; PMID:1322071 !$#accession A48387 !'##molecule_type genomic RNA !'##residues 121-200 ##label CHE !'##experimental_source isolate JaOArS982 !'##note sequence extracted from NCBI backbone (NCBIN:109245, !1NCBIP:109246) CLASSIFICATION #superfamily yellow fever virus genome polyprotein KEYWORDS ATP; capsid protein; envelope protein; glycoprotein; !1nonstructural protein; nucleotide binding; P-loop; !1polyprotein; transmembrane protein FEATURE !$2-127 #product capsid protein C #status predicted #label !8CAP\ !$44-60 #domain transmembrane #status predicted #label TN1\ !$112-127 #domain transmembrane #status predicted #label TN2\ !$128-294 #product membrane protein M precursor #status !8predicted #label GLC\ !$128-219 #domain nonterminal signal sequence #status predicted !8#label SIG\ !$220-294 #product membrane protein M #status predicted #label !8GLM\ !$280-294 #domain transmembrane #status predicted #label TN3\ !$295-794 #product envelope protein E #status predicted #label !8ENV\ !$774-790 #domain transmembrane #status predicted #label TN4\ !$795-1206 #product nonstructural protein NS1 #status predicted !8#label NS1\ !$1207-1373 #product nonstructural protein NS2a #status predicted !8#label N2A\ !$1374-1504 #product nonstructural protein NS2b #status predicted !8#label N2B\ !$1505-2123 #product nonstructural protein NS3 #status predicted !8#label NS3\ !$1698-1705 #region nucleotide-binding motif A (P-loop)\ !$1785-1790 #region nucleotide-binding motif B\ !$1789-1792 #region DEAH motif\ !$2124-2412 #product nonstructural protein NS4a #status predicted !8#label N4A\ !$2413-2527 #product nonstructural protein NS4b #status predicted !8#label N4B\ !$2528-3432 #product nonstructural protein NS5 #status predicted !8#label NS5\ !$142,448,924,1001, !$1594,1950,2463, !$2491,2761,2866,2904 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 3432 #molecular-weight 380164 #checksum 8986 SEQUENCE /// ENTRY GNWVJS #type complete TITLE genome polyprotein - Japanese encephalitis virus (strain SA-14) CONTAINS capsid protein; envelope protein; membrane protein; nonstructural protein NS1; nonstructural protein NS2a; nonstructural protein NS2b; nonstructural protein NS3; nonstructural protein NS4a; nonstructural protein NS4b; nonstructural protein NS5 ORGANISM #formal_name Japanese encephalitis virus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 19-Jan-2001 ACCESSIONS A35519 REFERENCE A35519 !$#authors Nitayaphan, S.; Grant, J.A.; Chang, G.J.J.; Trent, D.W. !$#journal Virology (1990) 177:541-552 !$#title Nucleotide sequence of the virulent SA-14 strain of Japanese !1encephalitis virus and its attenuated vaccine derivative, !1SA-14-14-2. !$#cross-references MUID:90320126; PMID:2371768 !$#accession A35519 !'##molecule_type genomic RNA !'##residues 1-3432 ##label NIT !'##cross-references GB:M55506; NID:g331331; PIDN:AAA46248.1; !1PID:g331332 CLASSIFICATION #superfamily yellow fever virus genome polyprotein KEYWORDS ATP; capsid protein; envelope protein; glycoprotein; !1nonstructural protein; nucleotide binding; P-loop; !1polyprotein; transmembrane protein FEATURE !$1-127 #product capsid protein #status predicted #label CAP\ !$46-67 #domain transmembrane #status predicted #label TN1\ !$110-127 #domain transmembrane #status predicted #label TN2\ !$128-294 #product membrane protein I precursor #status !8predicted #label GLC\ !$128-219 #domain nonterminal signal sequence #status predicted !8#label SIG\ !$220-294 #product membrane protein II #status predicted #label !8GLM\ !$280-294 #domain transmembrane #status predicted #label TN3\ !$295-794 #product envelope protein #status predicted #label !8ENV\ !$745-767 #domain transmembrane #status predicted #label TN4\ !$774-792 #domain transmembrane #status predicted #label TN5\ !$795-1206 #product nonstructural protein NS1 #status predicted !8#label NS1\ !$1178-1197 #domain transmembrane #status predicted #label TN6\ !$1207-1373 #product nonstructural protein NS2a #status predicted !8#label N2A\ !$1374-1504 #product nonstructural protein NS2b #status predicted !8#label N2B\ !$1505-2123 #product nonstructural protein NS3 #status predicted !8#label NS3\ !$1698-1705 #region nucleotide-binding motif A (P-loop)\ !$1785-1790 #region nucleotide-binding motif B\ !$1789-1792 #region DEAH motif\ !$2124-2412 #product nonstructural protein NS4a #status predicted !8#label N4A\ !$2413-2527 #product nonstructural protein NS4b #status predicted !8#label N4B\ !$2528-3432 #product nonstructural protein NS5 #status predicted !8#label NS5\ !$142,448,924,1001, !$1594,1950,2463, !$2491,2761,2866,2904 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 3432 #molecular-weight 380209 #checksum 289 SEQUENCE /// ENTRY GNWVJF #type fragment TITLE genome polyprotein - Japanese encephalitis virus (strain Nakayama) (fragment) CONTAINS amino end of nonstructural protein NS3; carboxyl end of capsid protein C; envelope protein E; membrane protein M; nonstructural protein NS1; nonstructural protein NS2a; nonstructural protein NS2b ORGANISM #formal_name Japanese encephalitis virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 17-Nov-2000 ACCESSIONS A27844 REFERENCE A27844 !$#authors McAda, P.C.; Mason, P.W.; Schmaljohn, C.S.; Dalrymple, J.M.; !1Mason, T.L.; Fournier, M.J. !$#journal Virology (1987) 158:348-360 !$#title Partial nucleotide sequence of the Japanese encephalitis !1virus genome. !$#cross-references MUID:87236200; PMID:3035787 !$#accession A27844 !'##molecule_type genomic RNA !'##residues 1-1440 ##label MCA !'##cross-references GB:M16574; NID:g331336; PIDN:AAA46251.1; !1PID:g331337 CLASSIFICATION #superfamily yellow fever virus genome polyprotein KEYWORDS capsid protein; envelope protein; glycoprotein; membrane !1protein; nonstructural protein; polyprotein FEATURE !$1-53 #product capsid protein C #status predicted #label !8CPC\ !$54-222 #product membrane protein M precursor #status !8predicted #label MPP\ !$54-146 #domain nonterminal signal sequence #status predicted !8#label SIG\ !$147-222 #product membrane protein M #status predicted #label !8MPM\ !$223-722 #product envelope protein E #status predicted #label !8EPE\ !$723-1136 #product nonstructural protein NS1 #status predicted !8#label NS1\ !$1137-1301 #product nonstructural protein NS2a #status predicted !8#label N2A\ !$1302-1432 #product nonstructural protein NS2b #status predicted !8#label N2B\ !$1433-1440 #product nonstructural protein NS3 (fragment) #status !8predicted #label NS3\ !$68,80,376,852,929 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1440 #checksum 9201 SEQUENCE /// ENTRY GNWVMV #type complete TITLE genome polyprotein - Murray Valley encephalitis virus (strain Australia) CONTAINS capsid protein; envelope protein; membrane protein; nonstructural protein NS1; nonstructural protein NS2a; nonstructural protein NS2b; nonstructural protein NS3; nonstructural protein NS4a; nonstructural protein NS4b; nonstructural protein NS5 ORGANISM #formal_name Murray Valley encephalitis virus DATE 30-Jun-1988 #sequence_revision 17-Feb-1994 #text_change 19-Jan-2001 ACCESSIONS A24635; A60288 REFERENCE A24635 !$#authors Dalgarno, L.; Trent, D.W.; Strauss, J.H.; Rice, C.M. !$#journal J. Mol. Biol. (1986) 187:309-323 !$#title Partial nucleotide sequence of the Murray Valley !1encephalitis virus genome: comparison of the encoded !1polypeptides with yellow fever virus structural and !1non-structural proteins. !$#cross-references MUID:86200215; PMID:3009829 !$#accession A24635 !'##molecule_type genomic RNA !'##residues 1-1780 ##label DAL !'##cross-references GB:X03467; NID:g59329; PIDN:CAA27184.1; PID:g755731 REFERENCE A60288 !$#authors Lee, E.; Fernon, C.; Simpson, R.; Weir, R.C.; Rice, C.M.; !1Dalgarno, L. !$#journal Virus Genes (1990) 4:197-213 !$#title Sequence of the 3' half of the Murray Valley encephalitis !1virus genome and mapping of the nonstructural proteins NS1, !1NS3, and NS5. !$#cross-references MUID:91102934; PMID:1702914 !$#accession A60288 !'##molecule_type genomic RNA !'##residues 1504-1778,'V',1780-3434 ##label LEE CLASSIFICATION #superfamily yellow fever virus genome polyprotein KEYWORDS ATP; capsid protein; envelope protein; glycoprotein; !1nonstructural protein; nucleotide binding; P-loop; !1polyprotein; transmembrane protein FEATURE !$1-125 #product capsid protein #status predicted #label CAP\ !$126-292 #product membrane protein precursor #status predicted !8#label GLC\ !$126-217 #domain nonterminal signal sequence #status predicted !8#label SIG\ !$218-292 #product membrane protein #status predicted #label !8GLM\ !$278-292 #domain transmembrane #status predicted #label TN1\ !$293-793 #product envelope protein #status predicted #label !8ENV\ !$773-791 #domain transmembrane #status predicted #label TN2\ !$794-1205 #product nonstructural protein NS1 #status predicted !8#label NS1\ !$1206-1372 #product nonstructural protein NS2a #status predicted !8#label N2A\ !$1373-1503 #product nonstructural protein NS2b #status predicted !8#label N2B\ !$1504-2122 #product nonstructural protein NS3 #status predicted !8#label NS3\ !$1697-1704 #region nucleotide-binding motif A (P-loop)\ !$1784-1789 #region nucleotide-binding motif B\ !$1788-1791 #region DEAH motif\ !$2123-2414 #product nonstructural protein NS4a #status predicted !8#label N4A\ !$2415-2529 #product nonstructural protein NS4b #status predicted !8#label N4B\ !$2530-3434 #product nonstructural protein NS5 #status predicted !8#label NS5\ !$73,140,446 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 3434 #molecular-weight 380603 #checksum 7036 SEQUENCE /// ENTRY GNWVS5 #type fragment TITLE genome polyprotein - St. Louis encephalitis virus (strain MS1-7) (fragment) CONTAINS capsid protein C; envelope protein M; major envelope protein E; nonstructural protein NS1; nonstructural protein NS2a; nonstructural protein NS2b; nonstructural protein NS3 ORGANISM #formal_name St. Louis encephalitis virus DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 17-Nov-2000 ACCESSIONS A27531 REFERENCE A27531 !$#authors Trent, D.W.; Kinney, R.M.; Johnson, B.J.B.; Vorndam, A.V.; !1Grant, J.A.; Deubel, V.; Rice, C.M.; Hahn, C. !$#journal Virology (1987) 156:293-304 !$#title Partial nucleotide sequence of St. Louis encephalitis virus !1RNA: structural proteins, NS1, ns2a, and ns2b. !$#cross-references MUID:87122172; PMID:3027980 !$#accession A27531 !'##molecule_type genomic RNA !'##residues 1-1525 ##label TRE !'##cross-references GB:M16614; NID:g334865 CLASSIFICATION #superfamily yellow fever virus genome polyprotein KEYWORDS capsid protein; envelope protein; glycoprotein; !1nonstructural protein; polyprotein; transmembrane protein FEATURE !$1-119 #product capsid protein C #status predicted #label !8CPC\ !$108-119 #domain transmembrane #status predicted #label TM1\ !$120-288 #product envelope protein prM #status predicted !8#label EPP\ !$214-288 #product envelope protein M #status predicted #label !8EPM\ !$253-268 #domain transmembrane #status predicted #label TM2\ !$274-288 #domain transmembrane #status predicted #label TM3\ !$289-789 #product major envelope protein E #status predicted !8#label EPE\ !$751-762 #domain transmembrane #status predicted #label TM4\ !$768-787 #domain transmembrane #status predicted #label TM5\ !$790-1203 #product nonstructural protein NS1 #status predicted !8#label NS1\ !$1173-1188 #domain transmembrane #status predicted #label TM6\ !$1204-1368 #product nonstructural protein NS2a #status predicted !8#label NSA\ !$1369-1499 #product nonstructural protein NS2b #status predicted !8#label NSB\ !$1500-1525 #product nonstructural protein NS3 #status predicted !8#label NS3\ !$136,269,442,602, !$919,964,996,1189 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1525 #checksum 1190 SEQUENCE /// ENTRY GNWVDP #type complete TITLE genome polyprotein - dengue virus type 2 (strain PR159/S1) CONTAINS capsid protein; envelope protein; membrane protein; nonstructural protein NS1; nonstructural protein NS2a; nonstructural protein NS2b; nonstructural protein NS3; nonstructural protein NS4a; nonstructural protein NS4b; nonstructural protein NS5 ORGANISM #formal_name dengue virus type 2 DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 19-Jan-2001 ACCESSIONS A29972 REFERENCE A29972 !$#authors Hahn, Y.S.; Galler, R.; Hunkapiller, T.; Dalrymple, J.M.; !1Strauss, J.H.; Strauss, E.G. !$#journal Virology (1988) 162:167-180 !$#title Nucleotide sequence of dengue 2 RNA and comparison of the !1encoded proteins with those of other flaviviruses. !$#cross-references MUID:88101365; PMID:2827375 !$#accession A29972 !'##molecule_type genomic RNA !'##residues 1-3388 ##label HAH !'##cross-references GB:M19197; NID:g323654; PIDN:AAA42962.1; !1PID:g323655 CLASSIFICATION #superfamily yellow fever virus genome polyprotein KEYWORDS ATP; capsid protein; envelope protein; glycoprotein; !1membrane protein; nonstructural protein; nucleotide binding; !1P-loop FEATURE !$2-114 #product capsid protein #status predicted #label CAP\ !$115-280 #product membrane protein precursor #status predicted !8#label MPP\ !$115-205 #domain nonterminal signal sequence #status predicted !8#label SIG\ !$206-280 #product membrane protein #status predicted #label !8MMP\ !$281-775 #product envelope protein #status predicted #label !8ENP\ !$776-1188 #product nonstructural protein NS1 #status predicted !8#label NS1\ !$1189-1345 #product nonstructural protein NS2a #status predicted !8#label N2A\ !$1346-1475 #product nonstructural protein NS2b #status predicted !8#label N2B\ !$1476-2090 #product nonstructural protein NS3 #status predicted !8#label NS3\ !$1668-1675 #region nucleotide-binding motif A (P-loop)\ !$1755-1760 #region nucleotide-binding motif B\ !$1759-1762 #region DEAH motif\ !$2091-2376 #product nonstructural protein NS4a #status predicted !8#label N4A\ !$2377-2488 #product nonstructural protein NS4b #status predicted !8#label N4B\ !$2489-3388 #product nonstructural protein NS5 #status predicted !8#label NS5\ !$183,347,433,905, !$982,1134,1174,1329, !$1369,2298,2302, !$2384,2454,2482, !$2641,2662,2701,2711 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 3388 #molecular-weight 379216 #checksum 9589 SEQUENCE /// ENTRY GNWVJA #type complete TITLE genome polyprotein - dengue virus type 2 (strain Jamaica) CONTAINS capsid protein C; envelope protein E; membrane-associated protein M; nonstructural protein NS1; nonstructural protein NS2a; nonstructural protein NS2b; nonstructural protein NS3; nonstructural protein NS4a; nonstructural protein NS4b; nonstructural protein NS5 ORGANISM #formal_name dengue virus type 2 DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 19-Jan-2001 ACCESSIONS A94346; A94378; A25613; A29199 REFERENCE A94346 !$#authors Deubel, V.; Kinney, R.M.; Trent, D.W. !$#journal Virology (1986) 155:365-377 !$#title Nucleotide sequence and deduced amino acid sequence of the !1structural proteins of dengue type 2 virus, Jamaica !1genotype. !$#cross-references MUID:87071658; PMID:3024394 !$#accession A94346 !'##molecule_type genomic RNA !'##residues 1-791 ##label DE1 !'##cross-references GB:M15975 REFERENCE A94378 !$#authors Deubel, V.; Kinney, R.M.; Trent, D.W. !$#journal Virology (1988) 165:234-244 !$#title Nucleotide sequence and deduced amino acid sequence of the !1nonstructural proteins of dengue type 2 virus, Jamaica !1genotype: comparative analysis of the full-length genome. !$#cross-references MUID:88265864; PMID:3388770 !$#accession A94378 !'##molecule_type genomic RNA !'##residues 792-3391 ##label DE2 !'##cross-references GB:M20558 CLASSIFICATION #superfamily yellow fever virus genome polyprotein KEYWORDS ATP; capsid protein; envelope protein; glycoprotein; !1nonstructural protein; nucleotide binding; P-loop; !1polyprotein; transmembrane protein FEATURE !$2-114 #product capsid protein C #status predicted #label !8CPC\ !$43-59 #domain transmembrane #status predicted #label TM1\ !$101-117 #domain transmembrane #status predicted #label TM2\ !$115-280 #product membrane-associated protein M precursor !8#status predicted #label MPP\ !$115-205 #domain nonterminal signal sequence #status predicted !8#label SIG\ !$206-280 #product membrane-associated protein M #status !8predicted #label MPM\ !$268-284 #domain transmembrane #status predicted #label TM3\ !$281-775 #product envelope protein E #status predicted #label !8EPE\ !$727-743 #domain transmembrane #status predicted #label TM4\ !$757-773 #domain transmembrane #status predicted #label TM5\ !$776-1127 #product nonstructural protein NS1 #status predicted !8#label NS1\ !$1128-1345 #product nonstructural protein NS2a #status predicted !8#label N2A\ !$1346-1474 #product nonstructural protein NS2b #status predicted !8#label N2B\ !$1475-2093 #product nonstructural protein NS3 #status predicted !8#label NS3\ !$1668-1675 #region nucleotide-binding motif A (P-loop)\ !$1755-1760 #region nucleotide-binding motif B\ !$1759-1762 #region DEAH motif\ !$2094-2243 #product nonstructural protein NS4a #status predicted !8#label N4A\ !$2244-2491 #product nonstructural protein NS4b #status predicted !8#label N4B\ !$2492-3391 #product nonstructural protein NS5 #status predicted !8#label NS5\ !$183,347,433 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 3391 #molecular-weight 379247 #checksum 2759 SEQUENCE /// ENTRY GNWV16 #type complete TITLE genome polyprotein - dengue virus type 2 (strain 16681) CONTAINS capsid protein C; envelope protein E; membrane-associated protein M; nonstructural protein NS1; nonstructural protein NS2a; nonstructural protein NS2b; nonstructural protein NS3; nonstructural protein NS4a; nonstructural protein NS4b; nonstructural protein NS5 ORGANISM #formal_name dengue virus type 2 DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-Jan-2001 ACCESSIONS A42451; A43496; A43763 REFERENCE A42451 !$#authors Blok, J.; McWilliam, S.M.; Butler, H.C.; Gibbs, A.J.; !1Weiller, G.; Herring, B.L.; Hemsley, A.C.; Aaskov, J.G.; !1Yoksan, S.; Bhamarapravati, N. !$#journal Virology (1992) 187:573-590 !$#title Comparison of a dengue-2 virus and its candidate vaccine !1derivative: sequence relationships with the flaviviruses and !1other viruses. !$#cross-references MUID:92188532; PMID:1312269 !$#accession A42451 !'##molecule_type genomic RNA !'##residues 1-3391 ##label BLO !'##cross-references GB:M84727; GB:M85259; NID:g323472; PIDN:AAA73185.1; !1PID:g323473 CLASSIFICATION #superfamily yellow fever virus genome polyprotein KEYWORDS ATP; capsid protein; envelope protein; glycoprotein; !1nonstructural protein; nucleotide binding; P-loop; !1polyprotein; transmembrane protein FEATURE !$1-114 #product capsid protein C #status predicted #label !8CPC\ !$115-280 #product membrane-associated protein M precursor !8#status predicted #label MPP\ !$115-205 #domain nonterminal signal sequence #status predicted !8#label SIG\ !$206-280 #product membrane-associated protein M #status !8predicted #label MPM\ !$268-284 #domain transmembrane #status predicted #label TM1\ !$281-775 #product envelope protein E #status predicted #label !8EPE\ !$727-743 #domain transmembrane #status predicted #label TM2\ !$757-773 #domain transmembrane #status predicted #label TM3\ !$776-1127 #product nonstructural protein NS1 #status predicted !8#label NS1\ !$1128-1345 #product nonstructural protein NS2a #status predicted !8#label N2A\ !$1346-1474 #product nonstructural protein NS2b #status predicted !8#label N2B\ !$1475-2093 #product nonstructural protein NS3 #status predicted !8#label NS3\ !$1668-1675 #region nucleotide-binding motif A (P-loop)\ !$1755-1760 #region nucleotide-binding motif B\ !$1759-1762 #region DEAH motif\ !$2094-2243 #product nonstructural protein NS4a #status predicted !8#label N4A\ !$2244-2491 #product nonstructural protein NS4b #status predicted !8#label N4B\ !$2492-3391 #product nonstructural protein NS5 #status predicted !8#label NS5\ !$183,347,433 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 3391 #molecular-weight 379544 #checksum 9567 SEQUENCE /// ENTRY GNWV26 #type complete TITLE genome polyprotein - dengue virus type 2 (strain 16681-PDK53) CONTAINS capsid protein C; envelope protein E; membrane-associated protein M; nonstructural protein NS1; nonstructural protein NS2a; nonstructural protein NS2b; nonstructural protein NS3; nonstructural protein NS4a; nonstructural protein NS4b; nonstructural protein NS5 ORGANISM #formal_name dengue virus type 2 DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-Jan-2001 ACCESSIONS B42451 REFERENCE A42451 !$#authors Blok, J.; McWilliam, S.M.; Butler, H.C.; Gibbs, A.J.; !1Weiller, G.; Herring, B.L.; Hemsley, A.C.; Aaskov, J.G.; !1Yoksan, S.; Bhamarapravati, N. !$#journal Virology (1992) 187:573-590 !$#title Comparison of a dengue-2 virus and its candidate vaccine !1derivative: sequence relationships with the flaviviruses and !1other viruses. !$#cross-references MUID:92188532; PMID:1312269 !$#accession B42451 !'##molecule_type genomic RNA !'##residues 1-3391 ##label BLO !'##cross-references GB:M85259 CLASSIFICATION #superfamily yellow fever virus genome polyprotein KEYWORDS ATP; capsid protein; envelope protein; glycoprotein; !1nonstructural protein; nucleotide binding; P-loop; !1polyprotein; transmembrane protein FEATURE !$1-114 #product capsid protein C #status predicted #label !8CPC\ !$50-66 #domain transmembrane #status predicted #label TM1\ !$102-118 #domain transmembrane #status predicted #label TM2\ !$115-280 #product membrane-associated protein M precursor !8#status predicted #label MPP\ !$115-205 #domain nonterminal signal sequence #status predicted !8#label SIG\ !$206-280 #product membrane-associated protein M #status !8predicted #label MPM\ !$268-284 #domain transmembrane #status predicted #label TM3\ !$281-775 #product envelope protein E #status predicted #label !8EPE\ !$727-743 #domain transmembrane #status predicted #label TM4\ !$757-773 #domain transmembrane #status predicted #label TM5\ !$776-1127 #product nonstructural protein NS1 #status predicted !8#label NS1\ !$1128-1345 #product nonstructural protein NS2a #status predicted !8#label N2A\ !$1158-1174 #domain transmembrane #status predicted #label TM6\ !$1272-1288 #domain transmembrane #status predicted #label TM7\ !$1294-1310 #domain transmembrane #status predicted #label TM8\ !$1346-1474 #product nonstructural protein NS2b #status predicted !8#label N2B\ !$1351-1367 #domain transmembrane #status predicted #label TM9\ !$1373-1389 #domain transmembrane #status predicted #label TMA\ !$1448-1464 #domain transmembrane #status predicted #label TMB\ !$1475-2093 #product nonstructural protein NS3 #status predicted !8#label NS3\ !$1668-1675 #region nucleotide-binding motif A (P-loop)\ !$1755-1760 #region nucleotide-binding motif B\ !$1759-1762 #region DEAH motif\ !$2094-2243 #product nonstructural protein NS4a #status predicted !8#label N4A\ !$2148-2164 #domain transmembrane #status predicted #label TMC\ !$2174-2190 #domain transmembrane #status predicted #label TMD\ !$2197-2213 #domain transmembrane #status predicted #label TME\ !$2227-2243 #domain transmembrane #status predicted #label TMF\ !$2244-2491 #product nonstructural protein NS4b #status predicted !8#label N4B\ !$2352-2368 #domain transmembrane #status predicted #label TMG\ !$2411-2427 #domain transmembrane #status predicted #label TMH\ !$2492-3391 #product nonstructural protein NS5 #status predicted !8#label NS5\ !$183,347,433,905, !$982,1134,1174,1329, !$2301,2305,2346, !$2387,2457,2485, !$2644,2665,2704,2714 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 3391 #molecular-weight 379881 #checksum 9150 SEQUENCE /// ENTRY GNWVD2 #type fragment TITLE genome polyprotein - dengue virus type 2 (strain D2-04) (fragment) CONTAINS capsid protein C; envelope protein E; membrane-associated protein M; nonstructural protein NS1 ORGANISM #formal_name dengue virus type 2 DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 17-Nov-2000 ACCESSIONS JC1007; JC1005 REFERENCE JC1007 !$#authors Yang, P.Y.; Lam, S.K. !$#journal Chinese J. Microbiol. Immunol. (1991) 11:341-344 !$#title The nucleotide and encoded amino acid sequences of the !1structural protein gene of D2-04 virus strain isolated in !1China. !$#accession JC1007 !'##molecule_type genomic RNA !'##residues 1-775 ##label YAN !'##note the authors translated the codons TTA for residue 53 as Phe, !1AGT for residue 136 as Arg, TTT for residue 139 as Val, TTT !1for residue 155 as Pro, CGT for residue 194 as Cys, TGC for !1residue 235 as Arg, GGC for residue 266 as Ala, and CAG for !1residue 272 as Leu REFERENCE JC1005 !$#authors Yan, P.Y.; Kautner, I.M.; Koh, C.L.; Lam, S.K. !$#journal Chinese J. Microbiol. Immunol. (1991) 11:9-12 !$#title Nucleotide and encoded amino acid sequences of the !1nonstructural protein NS1 gene of a dengue-2 virus isolated !1in China. !$#accession JC1005 !'##molecule_type genomic RNA !'##residues 776-1127 ##label YA2 !'##note the authors translated the codons GTG for residue 899 as Leu, !1CTG for residue 952 as Val, and GAT for residue 971 as Ala CLASSIFICATION #superfamily yellow fever virus genome polyprotein KEYWORDS capsid protein; envelope protein; glycoprotein; !1membrane-associated protein; nonstructural protein; !1polyprotein; transmembrane protein FEATURE !$1-114 #product capsid protein C #status predicted #label !8CAP\ !$101-117 #domain transmembrane #status predicted #label TM1\ !$115-280 #product membrane-associated protein M precursor !8#status predicted #label MAM\ !$115-205 #domain nonterminal signal sequence #status predicted !8#label SIG\ !$206-280 #product membrane-associated protein M #status !8predicted #label MEM\ !$281-775 #product envelope protein E #status predicted #label !8ENV\ !$727-743 #domain transmembrane #status predicted #label TM2\ !$757-773 #domain transmembrane #status predicted #label TM3\ !$776-1127 #product nonstructural protein NS1 #status predicted !8#label NPN\ !$183,347,433,905,982 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1127 #checksum 8507 SEQUENCE /// ENTRY GNWVDF #type complete TITLE genome polyprotein - dengue virus type 4 CONTAINS capsid protein; envelope protein; membrane protein; nonstructural protein 5; nonstructural protein NS1; nonstructural protein NS2a; nonstructural protein NS2b; nonstructural protein NS3; nonstructural protein NS4a; nonstructural protein NS4b ORGANISM #formal_name dengue virus type 4 DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 19-Jan-2001 ACCESSIONS A94352; A94364; A26897; A29121 REFERENCE A94352 !$#authors Zhao, B.; Mackow, E.; Buckler-White, A.; Markoff, L.; !1Chanock, R.M.; Lai, C.J.; Makino, Y. !$#journal Virology (1986) 155:77-88 !$#title Cloning full-length dengue type 4 viral DNA sequences: !1analysis of genes coding for structural proteins. !$#cross-references MUID:87044106; PMID:3022479 !$#accession A94352 !'##molecule_type genomic RNA !'##residues 1-776 ##label ZHA !'##cross-references GB:M14931 REFERENCE A94364 !$#authors Mackow, E.; Makino, Y.; Zhao, B.; Zhang, Y.M.; Markoff, L.; !1Buckler-White, A.; Guiler, M.; Chanock, R.; Lai, C.J. !$#journal Virology (1987) 159:217-228 !$#title The nucleotide sequence of dengue type 4 virus: analysis of !1genes coding for nonstructural proteins. !$#cross-references MUID:87293881; PMID:3039728 !$#accession A94364 !'##molecule_type genomic RNA !'##residues 774-3386 ##label MAC !'##cross-references GB:M17255 CLASSIFICATION #superfamily yellow fever virus genome polyprotein KEYWORDS ATP; capsid protein; envelope protein; glycoprotein; !1nonstructural protein; nucleotide binding; P-loop; !1polyprotein; transmembrane protein FEATURE !$2-113 #product capsid protein #status predicted #label CAP\ !$42-58 #domain transmembrane #status predicted #label TM1\ !$100-116 #domain transmembrane #status predicted #label TM2\ !$114-279 #product membrane protein precursor #status predicted !8#label MEP\ !$114-204 #domain nonterminal signal sequence #status predicted !8#label SIG\ !$205-279 #product membrane protein #status predicted #label !8MEM\ !$267-283 #domain transmembrane #status predicted #label TM3\ !$280-773 #product envelope protein #status predicted #label !8ENV\ !$728-744 #domain transmembrane #status predicted #label TM4\ !$753-769 #domain transmembrane #status predicted #label TM5\ !$774-1184 #product nonstructural protein NS1 #status predicted !8#label NS1\ !$1157-1179 #domain transmembrane #status predicted #label TM6\ !$1185-1343 #product nonstructural protein NS2a #status predicted !8#label N2A\ !$1344-1473 #product nonstructural protein NS2b #status predicted !8#label N2B\ !$1474-2091 #product nonstructural protein NS3 #status predicted !8#label NS3\ !$1666-1673 #region nucleotide-binding motif A (P-loop)\ !$1753-1758 #region nucleotide-binding motif B\ !$1757-1760 #region DEAH motif\ !$2092-2374 #product nonstructural protein NS4a #status predicted !8#label N4A\ !$2375-2486 #product nonstructural protein NS4b #status predicted !8#label N4B\ !$2487-3386 #product nonstructural protein NS5 #status predicted !8#label NS5\ !$182,346,432,750, !$903,980,2296,2300, !$2341,2382,2452, !$2582,2639,2699, !$2719,2913,3310 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 3386 #molecular-weight 378907 #checksum 1042 SEQUENCE /// ENTRY A42551 #type complete TITLE genome polyprotein - dengue virus type 1 (strain Singapore S275/90) CONTAINS capsid protein; envelope protein; membrane protein; nonstructural protein NS1; nonstructural protein NS2a; nonstructural protein NS2b; nonstructural protein NS3; nonstructural protein NS4a; nonstructural protein NS4b; nonstructural protein NS5 ORGANISM #formal_name dengue virus type 1 DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 19-Jan-2001 ACCESSIONS A42551 REFERENCE A42551 !$#authors Fu, J.; Tan, B.H.; Yap, E.H.; Chan, Y.C.; Tan, Y.H. !$#journal Virology (1992) 188:953-958 !$#title Full-length cDNA sequence of dengue type 1 virus (Singapore !1strain S275/90). !$#cross-references MUID:92263809; PMID:1585663 !$#accession A42551 !'##molecule_type genomic RNA !'##residues 1-3396 ##label FUJ !'##cross-references GB:M87512 CLASSIFICATION #superfamily yellow fever virus genome polyprotein KEYWORDS ATP; capsid protein; envelope protein; glycoprotein; !1nonstructural protein; nucleotide binding; P-loop; !1polyprotein; transmembrane protein FEATURE !$1-114 #product capsid protein #status predicted #label CAP\ !$115-281 #product membrane protein precursor #status predicted !8#label MEP\ !$115-204 #domain nonterminal signal sequence #status predicted !8#label SIG\ !$205-281 #product membrane protein #status predicted #label !8MEM\ !$267-279 #domain transmembrane #status predicted #label TM1\ !$282-774 #product envelope protein #status predicted #label !8ENV\ !$753-769 #domain transmembrane #status predicted #label TM2\ !$775-1127 #product nonstructural protein NS1 #status predicted !8#label NS1\ !$1128-1344 #product nonstructural protein NS2a #status predicted !8#label N2A\ !$1345-1474 #product nonstructural protein NS2b #status predicted !8#label N2B\ !$1475-2093 #product nonstructural protein NS3 #status predicted !8#label NS3\ !$1668-1675 #region nucleotide-binding motif A (P-loop)\ !$1755-1760 #region nucleotide-binding motif B\ !$1759-1762 #region DEAH motif\ !$2094-2243 #product nonstructural protein NS4a #status predicted !8#label N4A\ !$2244-2492 #product nonstructural protein NS4b #status predicted !8#label N4B\ !$2493-3396 #product nonstructural protein NS5 #status predicted !8#label NS5\ !$183,347,433 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 3396 #molecular-weight 379561 #checksum 3242 SEQUENCE /// ENTRY GNWVD3 #type complete TITLE genome polyprotein - dengue virus type 3 CONTAINS capsid protein; envelope protein; membrane protein; nonstructural protein NS1; nonstructural protein NS2a; nonstructural protein NS2b; nonstructural protein NS3; nonstructural protein NS4a; nonstructural protein NS4b; nonstructural protein NS5 ORGANISM #formal_name dengue virus type 3 DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 19-Jan-2001 ACCESSIONS A34774 REFERENCE A34774 !$#authors Osatomi, K.; Sumiyoshi, H. !$#journal Virology (1990) 176:643-647 !$#title Complete nucleotide sequence of dengue type 3 virus genome !1RNA. !$#cross-references MUID:90266483; PMID:2345967 !$#accession A34774 !'##molecule_type genomic RNA !'##residues 1-3390 ##label OSA !'##cross-references GB:M93130; NID:g323468; PIDN:AAA99437.1; !1PID:g323469 CLASSIFICATION #superfamily yellow fever virus genome polyprotein KEYWORDS ATP; capsid protein; envelope protein; glycoprotein; !1nonstructural protein; nucleotide binding; P-loop; !1polyprotein; transmembrane protein FEATURE !$1-114 #product capsid protein #status predicted #label CAP\ !$46-67 #domain transmembrane #status predicted #label TM1\ !$115-280 #product membrane protein precursor #status predicted !8#label MEP\ !$115-205 #domain nonterminal signal sequence #status predicted !8#label SIG\ !$206-280 #product membrane protein #status predicted #label !8MEM\ !$266-280 #domain transmembrane #status predicted #label TM3\ !$281-773 #product envelope protein #status predicted #label !8ENV\ !$724-746 #domain transmembrane #status predicted #label TM4\ !$753-771 #domain transmembrane #status predicted #label TM5\ !$774-1184 #product nonstructural protein NS1 #status predicted !8#label NS1\ !$1156-1175 #domain transmembrane #status predicted #label TM6\ !$1185-1343 #product nonstructural protein NS2a #status predicted !8#label N2A\ !$1344-1473 #product nonstructural protein NS2b #status predicted !8#label N2B\ !$1474-2092 #product nonstructural protein NS3 #status predicted !8#label NS3\ !$1667-1674 #region nucleotide-binding motif A (P-loop)\ !$1754-1759 #region nucleotide-binding motif B\ !$1758-1761 #region DEAH motif\ !$2093-2378 #product nonstructural protein NS4a #status predicted !8#label N4A\ !$2379-2490 #product nonstructural protein NS4b #status predicted !8#label N4B\ !$2491-3390 #product nonstructural protein NS5 #status predicted !8#label NS5\ !$183,347,433,750, !$903,980,1132,1188, !$1661,2300,2304, !$2386,2456,2702,2712 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 3390 #molecular-weight 378061 #checksum 1535 SEQUENCE /// ENTRY GNWVWP #type fragment TITLE genome polyprotein - dengue virus type 1 (strain Western Pacific) (fragment) CONTAINS capsid protein C; envelope protein E; membrane-associated protein M; nonstructural protein NS1; nonstructural protein NS2a ORGANISM #formal_name dengue virus type 1 DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 19-Jan-2001 ACCESSIONS A27032 REFERENCE A27032 !$#authors Mason, P.W.; McAda, P.C.; Mason, T.L.; Fournier, M.J. !$#journal Virology (1987) 161:262-267 !$#title Sequence of the dengue-1 virus genome in the region encoding !1the three structural proteins and the major nonstructural !1protein NS1. !$#cross-references MUID:88044504; PMID:3672932 !$#accession A27032 !'##molecule_type genomic RNA !'##residues 1-1226 ##label MAS !'##cross-references GB:M23027; NID:g511850; PIDN:AAA42940.1; !1PID:g511851 CLASSIFICATION #superfamily yellow fever virus genome polyprotein KEYWORDS capsid protein; envelope protein; glycoprotein; !1nonstructural protein; nucleotide binding; P-loop; !1polyprotein; transmembrane protein FEATURE !$2-114 #product capsid protein C #status predicted #label !8CPC\ !$43-59 #domain transmembrane #status predicted #label TM1\ !$101-117 #domain transmembrane #status predicted #label TM2\ !$115-280 #product membrane-associated protein M precursor !8#status predicted #label MPP\ !$115-205 #domain nonterminal signal sequence #status predicted !8#label SIG\ !$206-280 #product membrane-associated protein M #status !8predicted #label MPM\ !$268-284 #domain transmembrane #status predicted #label TM3\ !$281-775 #product envelope protein E #status predicted #label !8EPE\ !$384-391 #region nucleotide-binding motif A (P-loop)\ !$727-743 #domain transmembrane #status predicted #label TM4\ !$757-773 #domain transmembrane #status predicted #label TM5\ !$776-1127 #product nonstructural protein NS1 #status predicted !8#label NS1\ !$1128-1226 #product nonstructural protein NS2a (fragment) !8#status predicted #label N2A\ !$183,347,433,905, !$982,1190 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1226 #checksum 4326 SEQUENCE /// ENTRY GNWVTB #type complete TITLE genome polyprotein - tick-borne encephalitis virus (strain Sofjin) CONTAINS capsid protein C; envelope protein M; envelope protein prM; major envelope protein E; nonstructural protein NS1; nonstructural protein NS2a; nonstructural protein NS2b; nonstructural protein NS3; nonstructural protein NS4a; nonstructural protein NS4b; nonstructural protein NS5 ORGANISM #formal_name tick-borne encephalitis virus DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 19-Jan-2001 ACCESSIONS A33776; A24055; B24055; S06414 REFERENCE A33776 !$#authors Pletnev, A.G.; Yamshchikov, V.F.; Blinov, V.M. !$#journal Virology (1990) 174:250-263 !$#title Nucleotide sequence of the genome and complete amino acid !1sequence of the polyprotein of tick-borne encephalitis !1virus. !$#cross-references MUID:90101381; PMID:2136778 !$#accession A33776 !'##molecule_type genomic RNA !'##residues 1-3412 ##label PLE !'##cross-references GB:X07755 REFERENCE A91360 !$#authors Pletnev, A.G.; Yamshchikov, V.F.; Blinov, V.M. !$#journal FEBS Lett. (1986) 200:317-321 !$#title Tick-borne encephalitis virus genome: the nucleotide !1sequence coding for virion structural proteins. !$#cross-references MUID:86220766; PMID:3709796 !$#accession A24055 !'##molecule_type genomic RNA !'##residues 1-62,'V',64-101,'A',103-508,'T',510-683 ##label PL2 !$#accession B24055 !'##molecule_type genomic RNA !'##residues 242,'SG',245-246,358-359,'EHEESD',366,'A',758-849,'D', !1851-1002 ##label PL3 CLASSIFICATION #superfamily yellow fever virus genome polyprotein KEYWORDS ATP; capsid protein; envelope protein; glycoprotein; !1nonstructural protein; nucleotide binding; P-loop; !1polyprotein; transmembrane protein FEATURE !$2-112 #product capsid protein C #status predicted #label !8CPC\ !$113-205 #product envelope protein prM #status predicted !8#label PRM\ !$206-280 #product envelope protein M #status predicted #label !8PMM\ !$281-776 #product major envelope protein E #status predicted !8#label PPE\ !$777-1190 #product nonstructural protein NS1 #status predicted !8#label NS1\ !$1191-1358 #product nonstructural protein NS2a #status predicted !8#label N2A\ !$1359-1489 #product nonstructural protein NS2b #status predicted !8#label N2B\ !$1490-2110 #product nonstructural protein NS3 #status predicted !8#label NS3\ !$1671-1678 #region nucleotide-binding motif A (P-loop)\ !$1775-1780 #region nucleotide-binding motif B\ !$1779-1782 #region DEAH motif\ !$2111-2259 #product nonstructural protein NS4a #status predicted !8#label N4A\ !$2260-2510 #product nonstructural protein NS4b #status predicted !8#label N4B\ !$2511-3412 #product nonstructural protein NS5 #status predicted !8#label NS5\ !$144,434,641,753, !$861,983,999,1228, !$1649,1988,2044, !$2052,2447,2466, !$2685,2725 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 3412 #molecular-weight 377979 #checksum 7007 SEQUENCE /// ENTRY GNWVNE #type complete TITLE genome polyprotein - tick-borne encephalitis virus (subtype Western, strain Neudoerfl) CONTAINS capsid protein C; envelope protein E; membrane protein M; nonstructural protein NS1; nonstructural protein NS2a; nonstructural protein NS2b; nonstructural protein NS3; nonstructural protein NS4a; nonstructural protein NS4b; nonstructural protein NS5 ORGANISM #formal_name tick-borne encephalitis virus DATE 31-Dec-1989 #sequence_revision 30-Jun-1991 #text_change 19-Jan-2001 ACCESSIONS A31052; A32596 REFERENCE A31052 !$#authors Mandl, C.W.; Heinz, F.X.; Kunz, C. !$#journal Virology (1988) 166:197-205 !$#title Sequence of the structural proteins of tick-borne !1encephalitis virus (Western subtype) and comparative !1analysis with other flaviviruses. !$#cross-references MUID:88322870; PMID:3413985 !$#accession A31052 !'##molecule_type genomic RNA !'##residues 1-779 ##label MAN1 !'##cross-references GB:M21498 REFERENCE A32596 !$#authors Mandl, C.W.; Heinz, F.X.; Stoeckl, E.; Kunz, C. !$#journal Virology (1989) 173:291-301 !$#title Genome sequence of tick-borne encephalitis virus (Western !1subtype) and comparative analysis of nonstructural proteins !1with other flaviviruses. !$#cross-references MUID:90051080; PMID:2554575 !$#accession A32596 !'##molecule_type genomic RNA !'##residues 767-3414 ##label MAN2 !'##cross-references GB:M27157 CLASSIFICATION #superfamily yellow fever virus genome polyprotein KEYWORDS ATP; capsid protein; envelope protein; glycoprotein; !1nonstructural protein; nucleotide binding; P-loop; !1polyprotein; transmembrane protein FEATURE !$2-116 #product capsid protein C #status predicted #label !8CPC\ !$117-280 #product membrane protein M precursor #status !8predicted #label MPP\ !$117-205 #domain nonterminal signal sequence #status predicted !8#label SIG\ !$206-280 #product membrane protein M #status predicted #label !8MPM\ !$246-264 #domain transmembrane #status predicted #label TM1\ !$281-776 #product envelope protein E #status predicted #label !8EPE\ !$738-751 #domain transmembrane #status predicted #label TM2\ !$777-1128 #product nonstructural protein NS1 #status predicted !8#label NS1\ !$1129-1358 #product nonstructural protein NS2a #status predicted !8#label N2A\ !$1359-1489 #product nonstructural protein NS2b #status predicted !8#label N2B\ !$1490-2110 #product nonstructural protein NS3 #status predicted !8#label NS3\ !$1688-1695 #region nucleotide-binding motif A (P-loop)\ !$1775-1780 #region nucleotide-binding motif B\ !$1779-1782 #region DEAH motif\ !$2111-2259 #product nonstructural protein NS4a #status predicted !8#label N4A\ !$2260-2511 #product nonstructural protein NS4b #status predicted !8#label N4B\ !$2512-3414 #product nonstructural protein NS5 #status predicted !8#label NS5\ !$144,434,641,753, !$861,983,999,1649, !$1988,2044,2447, !$2529,2686,2726 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 3414 #molecular-weight 378383 #checksum 1083 SEQUENCE /// ENTRY A42545 #type fragment TITLE genome polyprotein - Langat virus (strain TP21) (fragment) CONTAINS nonstructural protein NS1; nonstructural protein NS2a; nonstructural protein NS2b; nonstructural protein NS3; nonstructural protein NS4a; nonstructural protein NS4b; nonstructural protein NS5 ORGANISM #formal_name Langat virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 19-Jan-2001 ACCESSIONS A42545; A61409; C61409 REFERENCE A42545 !$#authors Iacono-Connors, L.C.; Schmaljohn, C.S. !$#journal Virology (1992) 188:875-880 !$#title Cloning and sequence analysis of the genes encoding the !1nonstructural proteins of Langat virus and comparative !1analysis with other flaviviruses. !$#cross-references MUID:92263794; PMID:1316684 !$#accession A42545 !'##molecule_type genomic RNA !'##residues 1-2638 ##label IAC !'##cross-references GB:S35365; NID:g249315; PIDN:AAB22165.1; !1PID:g249316 REFERENCE A61409 !$#authors Guirakhoo, F.; Heinz, F.X.; Mandl, C.W.; Holzmann, H.; Kunz, !1C.; Gresikova, M. !$#journal J. Gen. Virol. (1991) 72:333-338 !$#title The relationship between the flaviviruses Skalica and Langat !1as revealed by monoclonal antibodies, peptide mapping and !1RNA sequence analysis. !$#cross-references MUID:91132129; PMID:1847173 !$#accession A61409 !'##status not compared with conceptual translation !'##molecule_type genomic RNA !'##residues 319-337 ##label GUI !$#accession C61409 !'##status not compared with conceptual translation !'##molecule_type genomic RNA !'##residues 877-994 ##label GU2 CLASSIFICATION #superfamily yellow fever virus genome polyprotein KEYWORDS glycoprotein; nonstructural protein; nucleotide binding; !1P-loop; polyprotein; transmembrane protein FEATURE !$1-352 #product nonstructural protein NS1 #status predicted !8#label NS1\ !$353-582 #product nonstructural protein NS2a #status predicted !8#label N2A\ !$583-713 #product nonstructural protein NS2b #status predicted !8#label N2B\ !$714-1334 #product nonstructural protein NS3 #status predicted !8#label NS3\ !$912-919 #region nucleotide-binding motif A (P-loop)\ !$1335-1483 #product nonstructural protein NS4a #status predicted !8#label N4A\ !$1484-1735 #product nonstructural protein NS4b #status predicted !8#label N4B\ !$1736-2638 #product nonstructural protein NS5 #status predicted !8#label NS5\ !$85,207,223,873, !$1212,1671,1950 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 2638 #checksum 4027 SEQUENCE /// ENTRY JQ1882 #type complete TITLE envelope glycoprotein E - louping ill virus (strain LI/31) ORGANISM #formal_name louping ill virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 17-Nov-2000 ACCESSIONS JQ1882 REFERENCE JQ1882 !$#authors Gao, G.F.; Jiang, W.R.; Hussain, M.H.; Venugopal, K.; !1Gritsun, T.S.; Reid, H.W.; Gould, E.A. !$#journal J. Gen. Virol. (1993) 74:109-114 !$#title Sequencing and antigenic studies of a Norwegian virus !1isolated from encephalomyelitic sheep confirm the existence !1of louping ill virus outside Great Britain and Ireland. !$#cross-references MUID:93139771; PMID:8380831 !$#accession JQ1882 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-496 ##label GAO !'##cross-references GB:D12937; NID:g221981; PIDN:BAA02313.1; !1PID:g221982 COMMENT This protein is synthesized as a genome polyprotein. GENETICS !$#gene E CLASSIFICATION #superfamily yellow fever virus genome polyprotein KEYWORDS envelope protein; glycoprotein; transmembrane protein FEATURE !$448-465 #domain transmembrane #status predicted #label TMN\ !$480-496 #region hydrophobic\ !$154 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 496 #molecular-weight 53613 #checksum 1513 SEQUENCE /// ENTRY JQ1883 #type complete TITLE envelope glycoprotein E - louping ill virus (strain LI/K) ORGANISM #formal_name louping ill virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 17-Nov-2000 ACCESSIONS JQ1883 REFERENCE JQ1882 !$#authors Gao, G.F.; Jiang, W.R.; Hussain, M.H.; Venugopal, K.; !1Gritsun, T.S.; Reid, H.W.; Gould, E.A. !$#journal J. Gen. Virol. (1993) 74:109-114 !$#title Sequencing and antigenic studies of a Norwegian virus !1isolated from encephalomyelitic sheep confirm the existence !1of louping ill virus outside Great Britain and Ireland. !$#cross-references MUID:93139771; PMID:8380831 !$#accession JQ1883 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-496 ##label GAO !'##cross-references GB:D12935; NID:g221983; PIDN:BAA02311.1; !1PID:g221984 COMMENT This protein is synthesized as a genome polyprotein. GENETICS !$#gene E CLASSIFICATION #superfamily yellow fever virus genome polyprotein KEYWORDS envelope protein; glycoprotein; transmembrane protein FEATURE !$448-465 #domain transmembrane #status predicted #label TMN\ !$480-496 #region hydrophobic\ !$154 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 496 #molecular-weight 53631 #checksum 1417 SEQUENCE /// ENTRY JQ1884 #type complete TITLE envelope glycoprotein E - louping ill virus (strain LI/Nor) ORGANISM #formal_name louping ill virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 17-Nov-2000 ACCESSIONS JQ1884 REFERENCE JQ1882 !$#authors Gao, G.F.; Jiang, W.R.; Hussain, M.H.; Venugopal, K.; !1Gritsun, T.S.; Reid, H.W.; Gould, E.A. !$#journal J. Gen. Virol. (1993) 74:109-114 !$#title Sequencing and antigenic studies of a Norwegian virus !1isolated from encephalomyelitic sheep confirm the existence !1of louping ill virus outside Great Britain and Ireland. !$#cross-references MUID:93139771; PMID:8380831 !$#accession JQ1884 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-496 ##label GAO !'##cross-references GB:D12936; NID:g221985; PIDN:BAA02312.1; !1PID:g221986 COMMENT This protein is synthesized as a genome polyprotein. GENETICS !$#gene E CLASSIFICATION #superfamily yellow fever virus genome polyprotein KEYWORDS envelope protein; glycoprotein; transmembrane protein FEATURE !$448-465 #domain transmembrane #status predicted #label TMN\ !$480-496 #region hydrophobic\ !$154 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 496 #molecular-weight 53649 #checksum 1443 SEQUENCE /// ENTRY A42996 #type complete TITLE genome polyprotein - mosquito cell fusing agent CONTAINS capsid protein C; envelope protein E; membrane-associated protein M; nonstructural protein NS1; nonstructural protein NS2a; nonstructural protein NS2b; nonstructural protein NS3; nonstructural protein NS4a; nonstructural protein NS4b ORGANISM #formal_name mosquito cell fusing agent #note host Aedes aegypti (yellow fever mosquito) DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 17-Nov-2000 ACCESSIONS A42996; S27906 REFERENCE A42996 !$#authors Cammisa-Parks, H.; Cisar, L.A.; Kane, A.; Stollar, V. !$#journal Virology (1992) 189:511-524 !$#title The complete nucleotide sequence of cell fusing agent (CFA): !1homology between the nonstructural proteins encoded by CFA !1and the nonstructural proteins encoded by arthropod-borne !1flaviviruses. !$#cross-references MUID:92351550; PMID:1322586 !$#accession A42996 !'##molecule_type genomic RNA !'##residues 1-3341 ##label CAM !'##cross-references GB:M91671; NID:g336190; PIDN:AAA48509.1; !1PID:g336191 CLASSIFICATION #superfamily yellow fever virus genome polyprotein KEYWORDS ATP; capsid protein; envelope protein; glycoprotein; !1nonstructural protein; P-loop; polyprotein; transmembrane !1protein FEATURE !$1-136 #product capsid protein C #status predicted #label !8CPC\ !$137-278 #product membrane-associated protein M precursor !8#status predicted #label MPP\ !$245-261 #domain transmembrane #status predicted #label TM1\ !$279-705 #product envelope protein E #status predicted #label !8EPE\ !$670-686 #domain transmembrane #status predicted #label TM2\ !$706-1095 #product nonstructural protein NS1 #status predicted !8#label NS1\ !$1096-1327 #product nonstructural protein NS2a #status predicted !8#label N2A\ !$1328-1451 #product nonstructural protein NS2b #status predicted !8#label N2B\ !$1452-2028 #product nonstructural protein NS3 #status predicted !8#label NS3\ !$1640-1647 #region nucleotide-binding motif A (P-loop) #status !8atypical\ !$1725-1730 #region nucleotide-binding motif B\ !$1729-1732 #region DEXH motif\ !$2029-2196 #product nonstructural protein NS4a #status predicted !8#label N4A\ !$2197-2454 #product nonstructural protein NS4b #status predicted !8#label N4B\ !$2455-3341 #product nonstructural protein NS5 #status predicted !8#label NS5\ !$157,243,339,399, !$411,575,611,794, !$896,993,1027 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 3341 #molecular-weight 373263 #checksum 3705 SEQUENCE /// ENTRY GNWVBV #type complete TITLE genome polyprotein - bovine viral diarrhea virus ORGANISM #formal_name bovine viral diarrhea virus, BVDV DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 19-Jan-2001 ACCESSIONS A29198; A61161 REFERENCE A29198 !$#authors Collett, M.S.; Larson, R.; Gold, C.; Strick, D.; Anderson, !1D.K.; Purchio, A.F. !$#journal Virology (1988) 165:191-199 !$#title Molecular cloning and nucleotide sequence of the pestivirus !1bovine viral diarrhea virus. !$#cross-references MUID:88265858; PMID:2838957 !$#accession A29198 !'##molecule_type genomic RNA !'##residues 1-3988 ##label COL !'##experimental_source isolate NADL REFERENCE A61161 !$#authors Ward, P.; Misra, V. !$#journal Am. J. Vet. Res. (1991) 52:1231-1236 !$#title Detection of bovine viral diarrhea virus, using degenerate !1oligonucleotide primers and the polymerase chain reaction. !$#cross-references MUID:92027091; PMID:1656820 !$#accession A61161 !'##molecule_type genomic RNA !'##residues 2054-2072 ##label WAR !'##experimental_source isolate V1352 !'##note authors translated the codon ATA for residue 18 as Thr CLASSIFICATION #superfamily pestivirus genome polyprotein KEYWORDS ATP; glycoprotein; nucleotide binding; P-loop; polyprotein FEATURE !$2-234 #product viral proteinase p20 #status predicted !8#label VPT\ !$548-1115 #product major envelope glycoprotein gp55 #status !8predicted #label EGP\ !$1905-1912 #region nucleotide-binding motif A (P-loop)\ !$1996-2001 #region nucleotide-binding motif B\ !$2000-2003 #region DEXH motif\ !$272,281,296,365, !$370,413,487,597, !$809,922,990,1357, !$1419,1451,1803, !$2224,2307,2584, !$2772,2981,3778, !$3867,3883 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 3988 #molecular-weight 449062 #checksum 5663 SEQUENCE /// ENTRY A44217 #type complete TITLE genome polyprotein - bovine viral diarrhea virus (strain SD-1) ORGANISM #formal_name bovine viral diarrhea virus, BVDV DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 19-Jan-2001 ACCESSIONS A44217 REFERENCE A44217 !$#authors Deng, R.; Brock, K.V. !$#journal Virology (1992) 191:867-879 !$#title Molecular cloning and nucleotide sequence of a pestivirus !1genome, noncytopathic bovine viral diarrhea virus strain !1SD-1. !$#cross-references MUID:93079889; PMID:1333126 !$#accession A44217 !'##molecule_type genomic RNA !'##residues 1-3898 ##label DEN !'##cross-references GB:M96751; NID:g289507; PIDN:AAA42860.1; !1PID:g289508 !'##note this polyprotein may be cleaved into several mature proteins, !1including p20 protein, p14 protein, gp48 protein, gp25 !1protein, gp53 protein, p54 protein, p80 protein, p10 !1protein, p58 protein, and p75 protein; the cleavage sites !1are not reported CLASSIFICATION #superfamily pestivirus genome polyprotein KEYWORDS ATP; glycoprotein; nucleotide binding; P-loop; polyprotein; !1RNA binding; zinc finger FEATURE !$2-234 #product viral proteinase p20 #status predicted !8#label VPT\ !$253-265 #region hydrophobic\ !$546-1115 #product major envelope glycoprotein gp55 #status !8predicted #label EGP\ !$547-562 #region hydrophobic\ !$556-670 #region hydrophobic\ !$675-694 #region hydrophobic\ !$1031-1046 #region hydrophobic\ !$1074-1099 #region hydrophobic\ !$1149-1164 #region hydrophobic\ !$1217-1238 #region hydrophobic\ !$1252-1269 #region hydrophobic\ !$1271-1292 #region hydrophobic\ !$1293-1304 #region hydrophobic\ !$1357-1373 #region hydrophobic\ !$1484-1512 #region zinc finger\ !$1815-1822 #region nucleotide-binding motif A (P-loop)\ !$1906-1911 #region nucleotide-binding motif B\ !$1910-1913 #region DEAH motif\ !$2562-2582 #region hydrophobic\ !$272,281,296,335, !$365,370,413,487, !$597,809,878,922, !$990,1357,1419,1713, !$2134,2217,2494, !$2682,2751,2891, !$2988,3688,3777,3793 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 3898 #molecular-weight 437805 #checksum 8806 SEQUENCE /// ENTRY GNWVHC #type complete TITLE genome polyprotein - hog cholera virus (strain Alfort) ORGANISM #formal_name hog cholera virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 19-Jan-2001 ACCESSIONS A34037 REFERENCE A34037 !$#authors Meyers, G.; Ruemenapf, T.; Thiel, H.J. !$#journal Virology (1989) 171:555-567 !$#title Molecular cloning and nucleotide sequence of the genome of !1hog cholera virus. !$#cross-references MUID:89348014; PMID:2763466 !$#accession A34037 !'##molecule_type genomic RNA !'##residues 1-3898 ##label MEY !'##cross-references GB:J04358; NID:g325462; PIDN:AAA43844.1; !1PID:g325463 CLASSIFICATION #superfamily pestivirus genome polyprotein KEYWORDS ATP; glycoprotein; nucleotide binding; P-loop; polyprotein; !1transmembrane protein FEATURE !$2-231 #product viral proteinase p20 #status predicted !8#label VPT\ !$545-1111 #product major envelope glycoprotein gp55 #status !8predicted #label EGP\ !$1815-1822 #region nucleotide-binding motif A (P-loop)\ !$1906-1911 #region nucleotide-binding motif B\ !$1910-1913 #region DEXH motif\ !$157,269,274,278, !$293,362,367,410, !$425,500,594,805, !$810,918,949,986, !$1713,2134,2217, !$2494,2787,2815, !$2891,3211,3316, !$3689,3698,3794 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 3898 #molecular-weight 438560 #checksum 4600 SEQUENCE /// ENTRY GNWVHB #type complete TITLE genome polyprotein - hog cholera virus (strain Brescia) ORGANISM #formal_name hog cholera virus DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 19-Jan-2001 ACCESSIONS A35317 REFERENCE A35317 !$#authors Moormann, R.J.M.; Warmerdam, P.A.M.; Van Der Meer, B.; !1Schaaper, W.M.M.; Wensvoort, G.; Hulst, M.M. !$#journal Virology (1990) 177:184-198 !$#title Molecular cloning and nucleotide sequence of hog cholera !1virus strain Brescia and mapping of the genomic region !1encoding envelope protein E1. !$#cross-references MUID:90281581; PMID:2162104 !$#accession A35317 !'##molecule_type genomic RNA !'##residues 1-3898 ##label MOO !'##cross-references GB:M31768; NID:g325460; PIDN:AAA43843.1; !1PID:g325461 COMMENT The cleavage sites of this polyprotein have not been !1determined. CLASSIFICATION #superfamily pestivirus genome polyprotein KEYWORDS ATP; glycoprotein; nucleotide binding; P-loop; polyprotein; !1transmembrane protein FEATURE !$2-231 #product viral proteinase p20 #status predicted !8#label VPT\ !$545-1111 #product major envelope glycoprotein gp55 #status !8predicted #label EGP\ !$1031-1052 #domain transmembrane #status predicted #label TMN\ !$1815-1822 #region nucleotide-binding motif A (P-loop)\ !$1906-1911 #region nucleotide-binding motif B\ !$1910-1913 #region DEXH motif\ !$157,269,278,332, !$362,410,425,500, !$513,594,805,810, !$874,918,949,1713, !$2134,2217,2419, !$2494,2787,2815, !$2891,3103,3193, !$3211,3316,3689, !$3698,3794 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 3898 #molecular-weight 438427 #checksum 6677 SEQUENCE /// ENTRY VHWV #type complete TITLE structural polyprotein - Semliki Forest virus CONTAINS 6K peptide; coat protein; membrane glycoprotein E1; membrane glycoprotein E2; membrane glycoprotein E3 ORGANISM #formal_name Semliki Forest virus DATE 31-Mar-1981 #sequence_revision 24-Sep-1981 #text_change 16-Jul-1999 ACCESSIONS A93861; A93238; E37264; F21774; S42460; A03915 REFERENCE A93861 !$#authors Garoff, H.; Frischauf, A.M.; Simons, K.; Lehrach, H.; !1Delius, H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1980) 77:6376-6380 !$#title The capsid protein of Semliki Forest virus has clusters of !1basic amino acids and prolines in its amino-terminal region. !$#cross-references MUID:81101055; PMID:6935652 !$#accession A93861 !'##molecule_type genomic RNA !'##residues 1-305 ##label GAR REFERENCE A93238 !$#authors Garoff, H.; Frischauf, A.M.; Simons, K.; Lehrach, H.; !1Delius, H. !$#journal Nature (1980) 288:236-241 !$#title Nucleotide sequence of cDNA coding for Semliki forest virus !1membrane glycoproteins. !$#cross-references MUID:81052444; PMID:6985476 !$#accession A93238 !'##molecule_type genomic RNA !'##residues 266-1253 ##label GAR2 REFERENCE A21774 !$#authors Bell, J.R.; Kinney, R.M.; Trent, D.W.; Strauss, E.G.; !1Strauss, J.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:4702-4706 !$#title An evolutionary tree relating eight alphaviruses, based on !1amino-terminal sequences of their glycoproteins. !$#cross-references MUID:84272701; PMID:6087344 !$#accession E37264 !'##status preliminary !'##molecule_type protein !'##residues 334-402 ##label BEL !$#accession F21774 !'##status preliminary !'##molecule_type protein !'##residues 816-881 ##label BE2 REFERENCE S42460 !$#authors Santagati, M.G.; Itaranta, P.; Maatta, J.; Salmi, A.; !1Hinkkanen, A. !$#submission submitted to the EMBL Data Library, March 1994 !$#description Molecular analaysis of Semliki forest virus pathogenesis in !1BALB/c mice by using virus chimera constructed in vitro. !$#accession S42460 !'##molecule_type mRNA !'##residues 756-815 ##label SAN !'##cross-references EMBL:X78111; NID:g460829; PIDN:CAA55001.1; !1PID:g939973 CLASSIFICATION #superfamily togavirus structural polyprotein KEYWORDS glycoprotein FEATURE !$1-267 #product coat protein #status predicted #label CTP\ !$268-333 #product membrane glycoprotein E3 #status predicted !8#label GP3\ !$334-755 #product membrane glycoprotein E2 #status !8experimental #label GP2\ !$756-815 #product 6K peptide #status predicted #label 6KP\ !$816-1253 #product membrane glycoprotein E1 #status !8experimental #label GP1\ !$280 #binding_site (or 327) carbohydrate (Asn) (covalent) !8#status experimental\ !$533,595,956 #binding_site carbohydrate (Asn) (covalent) #status !8experimental SUMMARY #length 1253 #molecular-weight 138016 #checksum 9814 SEQUENCE /// ENTRY VHWVRA #type complete TITLE structural polyprotein - Ross River virus (strain NB5092 mouse-avirulent) CONTAINS capsid protein C; nonstructural 6K protein; spike protein E1; spike protein E2; spike protein E3 ORGANISM #formal_name Ross River virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS B28605 REFERENCE A94373 !$#authors Faragher, S.G.; Meek, A.D.J.; Rice, C.M.; Dalgarno, L. !$#journal Virology (1988) 163:509-526 !$#title Genome sequences of a mouse-avirulent and a mouse-virulent !1strain of Ross River virus. !$#cross-references MUID:88179556; PMID:2833022 !$#accession B28605 !'##molecule_type genomic RNA !'##residues 1-1254 ##label FAR !'##cross-references GB:M20162; NID:g333921; PIDN:AAA96330.1; !1PID:g1256539 CLASSIFICATION #superfamily togavirus structural polyprotein KEYWORDS capsid protein; nonstructural protein; polyprotein; spike !1protein FEATURE !$1-270 #product capsid protein C #status predicted #label !8CPC\ !$271-334 #product spike protein E3 #status predicted #label !8SP3\ !$335-756 #product spike protein E2 #status predicted #label !8SP2\ !$757-816 #product nonstructural 6K protein #status predicted !8#label NNP\ !$817-1254 #product spike protein E1 #status predicted #label !8SP1 SUMMARY #length 1254 #molecular-weight 138682 #checksum 669 SEQUENCE /// ENTRY VHWV48 #type fragment TITLE structural polyprotein - Ross River virus (strain T48) (fragment) CONTAINS spike protein E2 ORGANISM #formal_name Ross River virus DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS A31833 REFERENCE A94387 !$#authors Burness, A.T.H.; Pardoe, I.; Faragher, S.G.; Vrati, S.; !1Dalgarno, L. !$#journal Virology (1988) 167:639-643 !$#title Genetic stability of Ross River virus during epidemic spread !1in nonimmune humans. !$#cross-references MUID:89073770; PMID:2849242 !$#accession A31833 !'##molecule_type genomic RNA !'##residues 1-422 ##label BUR !'##cross-references GB:M23708; NID:g333917; PIDN:AAA47405.1; !1PID:g333918 CLASSIFICATION #superfamily togavirus structural polyprotein KEYWORDS glycoprotein; polyprotein; spike protein FEATURE !$1-422 #product spike protein E2 #status predicted #label !8SPE\ !$200,262 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 422 #checksum 4321 SEQUENCE /// ENTRY VHWV70 #type fragment TITLE structural polyprotein - Ross River virus (strain 213970) (fragment) CONTAINS spike protein E2 ORGANISM #formal_name Ross River virus DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS B31833 REFERENCE A94387 !$#authors Burness, A.T.H.; Pardoe, I.; Faragher, S.G.; Vrati, S.; !1Dalgarno, L. !$#journal Virology (1988) 167:639-643 !$#title Genetic stability of Ross River virus during epidemic spread !1in nonimmune humans. !$#cross-references MUID:89073770; PMID:2849242 !$#accession B31833 !'##molecule_type genomic RNA !'##residues 1-422 ##label BUR !'##cross-references GB:M23709; NID:g333919; PIDN:AAA47406.1; !1PID:g333920 CLASSIFICATION #superfamily togavirus structural polyprotein KEYWORDS glycoprotein; polyprotein; spike protein FEATURE !$1-422 #product spike protein E2 #status predicted #label !8SPE\ !$200,262 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 422 #checksum 6877 SEQUENCE /// ENTRY VHWVN2 #type complete TITLE structural polyprotein - O'nyong-nyong virus (strain Gulu) CONTAINS 6K protein; coat protein C; membrane glycoprotein E1; membrane glycoprotein E2; membrane glycoprotein E3 ORGANISM #formal_name O'nyong-nyong virus #note host Anopheles gambiae DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS B34680 REFERENCE A34680 !$#authors Levinson, R.S.; Strauss, J.H.; Strauss, E.G. !$#journal Virology (1990) 175:110-123 !$#title Complete sequence of the genomic RNA of O'nyong-nyong virus !1and its use in the construction of alphavirus phylogenetic !1trees. !$#cross-references MUID:90177206; PMID:2155505 !$#accession B34680 !'##molecule_type genomic RNA !'##residues 1-1247 ##label LEV !'##cross-references GB:M20303; GB:M33999; NID:g332558; PIDN:AAA46785.1; !1PID:g332560 CLASSIFICATION #superfamily togavirus structural polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; transmembrane !1protein FEATURE !$1-260 #product coat protein C #status predicted #label CPC\ !$261-324 #product membrane glycoprotein E3 #status predicted !8#label GE3\ !$325-747 #product membrane glycoprotein E2 #status predicted !8#label GE2\ !$692-708 #domain transmembrane #status predicted #label TM1\ !$726-742 #domain transmembrane #status predicted #label TM2\ !$748-808 #product 6K protein #status predicted #label GPT\ !$763-780 #domain transmembrane #status predicted #label TM3\ !$785-803 #domain transmembrane #status predicted #label TM4\ !$809-1247 #product membrane glycoprotein E1 #status predicted !8#label GE1\ !$1225-1242 #domain transmembrane #status predicted #label TM5\ !$272,587,597,669,949 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1247 #molecular-weight 137969 #checksum 7030 SEQUENCE /// ENTRY VHWVSB #type fragment TITLE structural polyprotein - Sindbis virus (strain AR339 derived wild type SB) (fragment) ORGANISM #formal_name Sindbis virus DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 16-Jul-1999 ACCESSIONS A25894 REFERENCE A25894 !$#authors Davis, N.L.; Fuller, F.J.; Dougherty, W.G.; Olmsted, R.A.; !1Johnston, R.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:6771-6775 !$#title A single nucleotide change in the E2 glycoprotein gene of !1Sindbis virus affects penetration rate in cell culture and !1virulence in neonatal mice. !$#cross-references MUID:86313659; PMID:3462725 !$#accession A25894 !'##molecule_type genomic RNA !'##residues 1-423 ##label DAV !'##cross-references GB:M13818; NID:g334105; PIDN:AAA47485.1; !1PID:g334106 CLASSIFICATION #superfamily togavirus structural polyprotein KEYWORDS glycoprotein; membrane protein; polyprotein FEATURE !$1-423 #product membrane glycoprotein E2 #status predicted !8#label MG2\ !$196,318 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 423 #checksum 406 SEQUENCE /// ENTRY VHWVB #type complete TITLE structural polyprotein - Sindbis virus (strain HRSP) CONTAINS 6K protein; coat protein C; membrane glycoprotein E1; membrane glycoprotein E2; membrane glycoprotein E3 ORGANISM #formal_name Sindbis virus DATE 29-Jul-1981 #sequence_revision 03-Aug-1984 #text_change 16-Jul-1999 ACCESSIONS A03916 REFERENCE A94331 !$#authors Strauss, E.G.; Rice, C.M.; Strauss, J.H. !$#journal Virology (1984) 133:92-110 !$#title Complete nucleotide sequence of the genomic RNA of Sindbis !1virus. !$#cross-references MUID:84148439; PMID:6322438 !$#accession A03916 !'##molecule_type genomic RNA !'##residues 1-1245 ##label STR !'##cross-references GB:J02363; GB:J02364; NID:g334100; PIDN:AAA96976.1; !1PID:g334103 CLASSIFICATION #superfamily togavirus structural polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; transmembrane !1protein FEATURE !$1-264 #product coat protein C #status predicted #label CPC\ !$265-328 #product membrane glycoprotein E3 #status predicted !8#label GE3\ !$329-751 #product membrane glycoprotein E2 #status predicted !8#label GE2\ !$696-712 #domain transmembrane #status predicted #label TM1\ !$728-746 #domain transmembrane #status predicted #label TM2\ !$752-806 #product 6K protein #status predicted #label GP6\ !$768-784 #domain transmembrane #status predicted #label TM3\ !$786-802 #domain transmembrane #status predicted #label TM4\ !$807-1245 #product membrane glycoprotein E1 #status predicted !8#label GE1\ !$1216-1234 #domain transmembrane #status predicted #label TM5\ !$278,524,646,945, !$1051 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1245 #molecular-weight 136765 #checksum 9343 SEQUENCE /// ENTRY VHWVB2 #type complete TITLE structural polyprotein - Sindbis virus (strain HRLP) CONTAINS 6K protein; coat protein C; membrane glycoprotein E1; membrane glycoprotein E2; membrane glycoprotein E3 ORGANISM #formal_name Sindbis virus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 09-Sep-1994 ACCESSIONS B03916; A03916 REFERENCE A93871 !$#authors Rice, C.M.; Strauss, J.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:2062-2066 !$#title Nucleotide sequence of the 26S mRNA of Sindbis virus and !1deduced sequence of the encoded virus structural proteins. !$#cross-references MUID:81223817; PMID:6941270 !$#accession B03916 !'##molecule_type genomic RNA !'##residues 1-1245 ##label RIC !'##cross-references GB:J02363 CLASSIFICATION #superfamily togavirus structural polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; transmembrane !1protein FEATURE !$1-264 #product coat protein C #status predicted #label CPC\ !$265-328 #product membrane glycoprotein E3 #status predicted !8#label GE3\ !$329-751 #product membrane glycoprotein E2 #status predicted !8#label GE2\ !$696-712 #domain transmembrane #status predicted #label TM1\ !$728-746 #domain transmembrane #status predicted #label TM2\ !$752-806 #product 6K protein #status predicted #label GP6\ !$768-784 #domain transmembrane #status predicted #label TM3\ !$786-802 #domain transmembrane #status predicted #label TM4\ !$807-1245 #product membrane glycoprotein E1 #status predicted !8#label GE1\ !$1216-1234 #domain transmembrane #status predicted #label TM5\ !$278,524,646,945, !$1051 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1245 #molecular-weight 136721 #checksum 9460 SEQUENCE /// ENTRY VHWV82 #type complete TITLE structural polyprotein - Ockelbo virus (strain Edsbyn 82-5) CONTAINS 6K protein; coat protein C; membrane glycoprotein E1; membrane glycoprotein E2; membrane glycoprotein E3 ORGANISM #formal_name Ockelbo virus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS B39991 REFERENCE A39991 !$#authors Shirako, Y.; Niklasson, B.; Dalrymple, J.M.; Strauss, E.G.; !1Strauss, J.H. !$#journal Virology (1991) 182:753-764 !$#title Structure of the Ockelbo virus genome and its relationship !1to other Sindbis viruses. !$#cross-references MUID:91220725; PMID:1673813 !$#accession B39991 !'##molecule_type genomic RNA !'##residues 1-1245 ##label SHI !'##cross-references GB:M69205; NID:g334111; PIDN:AAA96973.1; !1PID:g334113 CLASSIFICATION #superfamily togavirus structural polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; transmembrane !1protein FEATURE !$1-264 #product coat protein C #status predicted #label CPC\ !$265-328 #product membrane glycoprotein E3 #status predicted !8#label GE3\ !$329-751 #product membrane glycoprotein E2 #status predicted !8#label GE2\ !$696-712 #domain transmembrane #status predicted #label TM1\ !$728-746 #domain transmembrane #status predicted #label TM2\ !$752-806 #product 6K protein #status predicted #label GP6\ !$768-784 #domain transmembrane #status predicted #label TM3\ !$786-802 #domain transmembrane #status predicted #label TM4\ !$807-1245 #product membrane glycoprotein E1 #status predicted !8#label GE1\ !$1216-1234 #domain transmembrane #status predicted #label TM5\ !$278,524,646,945, !$1051 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1245 #molecular-weight 136648 #checksum 8881 SEQUENCE /// ENTRY VHWVWE #type complete TITLE structural polyprotein - western equine encephalomyelitis virus (strain BFS1703) CONTAINS 6K protein; coat protein C; membrane glycoprotein E1; membrane glycoprotein E2; membrane glycoprotein E3 ORGANISM #formal_name western equine encephalomyelitis virus DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Jul-1999 ACCESSIONS A35587 REFERENCE A35587 !$#authors Hahn, C.S.; Lustig, S.; Strauss, E.G.; Strauss, J.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:5997-6001 !$#title Western equine encephalitis virus is a recombinant virus. !$#cross-references MUID:88320369; PMID:3413072 !$#accession A35587 !'##molecule_type genomic RNA !'##residues 1-1236 ##label HAH !'##cross-references GB:J03854; NID:g323728; PIDN:AAA42999.1; !1PID:g323730 CLASSIFICATION #superfamily togavirus structural polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; transmembrane !1protein FEATURE !$1-259 #product coat protein C #status predicted #label CPC\ !$260-319 #product membrane glycoprotein E3 #status predicted !8#label MG3\ !$320-742 #product membrane glycoprotein E2 #status predicted !8#label MG2\ !$684-702 #domain transmembrane #status predicted #label TN1\ !$719-737 #domain transmembrane #status predicted #label TN2\ !$743-797 #product 6K protein #status predicted #label K6P\ !$758-775 #domain transmembrane #status predicted #label TN3\ !$777-793 #domain transmembrane #status predicted #label TN4\ !$798-1236 #product membrane glycoprotein E1 #status predicted !8#label MG1\ !$1206-1227 #domain transmembrane #status predicted #label TN5\ !$50,270,515,637,724, !$936,1042 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1236 #molecular-weight 136081 #checksum 9246 SEQUENCE /// ENTRY VHWVEE #type complete TITLE structural polyprotein - eastern equine encephalomyelitis virus (strain 82V-2137) CONTAINS 6K protein; coat protein C; membrane glycoprotein E1; membrane glycoprotein E2; membrane glycoprotein E3 ORGANISM #formal_name eastern equine encephalomyelitis virus DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 16-Jul-1999 ACCESSIONS A26816 REFERENCE A26816 !$#authors Chang, G.J.J.; Trent, D.W. !$#journal J. Gen. Virol. (1987) 68:2129-2142 !$#title Nucleotide sequence of the genome region encoding the 26S !1mRNA of eastern equine encephalomyelitis virus and the !1deduced amino acid sequence of the viral structural !1proteins. !$#cross-references MUID:87282265; PMID:2886548 !$#accession A26816 !'##molecule_type mRNA !'##residues 1-1239 ##label CHA !'##cross-references EMBL:X05816; NID:g62074; PIDN:CAA29261.1; !1PID:g62075 CLASSIFICATION #superfamily togavirus structural polyprotein KEYWORDS coat protein; glycoprotein; transmembrane protein FEATURE !$1-259 #product coat protein C #status predicted #label CPC\ !$260-322 #product membrane glycoprotein E3 #status predicted !8#label MG3\ !$261-277 #domain transmembrane #status predicted #label TN1\ !$323-742 #product membrane glycoprotein E2 #status predicted !8#label MG2\ !$684-701 #domain transmembrane #status predicted #label TN2\ !$727-737 #domain transmembrane #status predicted #label TN3\ !$743-798 #product 6K protein #status predicted #label K6P\ !$777-798 #domain transmembrane #status predicted #label TN4\ !$799-1239 #product membrane glycoprotein E1 #status predicted !8#label MG1\ !$1211-1235 #domain transmembrane #status predicted #label TN5\ !$49,270,624,637,932 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1239 #molecular-weight 137431 #checksum 4158 SEQUENCE /// ENTRY VHWVEV #type complete TITLE structural polyprotein - eastern equine encephalomyelitis virus (strain VA33[Ten Broeck]) CONTAINS 6K protein; coat protein C; membrane glycoprotein E1; membrane glycoprotein E2; membrane glycoprotein E3 ORGANISM #formal_name eastern equine encephalomyelitis virus #note host Equus caballus (domestic horse) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS A39992 REFERENCE A39992 !$#authors Weaver, S.C.; Scott, T.W.; Rico-Hesse, R. !$#journal Virology (1991) 182:774-784 !$#title Molecular evolution of eastern equine encephalomyelitis !1virus in North America. !$#cross-references MUID:91220727; PMID:2024496 !$#accession A39992 !'##molecule_type genomic RNA !'##residues 1-1240 ##label WEA !'##cross-references GB:M69094; NID:g323696; PIDN:AAA42980.1; !1PID:g323697 !'##note the authors translated the codon AGC for residue 836 as Arg and !1GUU for residue 1174 as Ile CLASSIFICATION #superfamily togavirus structural polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; transmembrane !1protein FEATURE !$1-260 #product coat protein C #status predicted #label CPC\ !$259-276 #domain transmembrane #status predicted #label TM1\ !$261-323 #product membrane glycoprotein E3 #status predicted !8#label EG3\ !$324-743 #product membrane glycoprotein E2 #status predicted !8#label EG2\ !$695-712 #domain transmembrane #status predicted #label TM2\ !$722-738 #domain transmembrane #status predicted #label TM3\ !$744-799 #product 6K protein #status predicted #label KP6\ !$781-799 #domain transmembrane #status predicted #label TM4\ !$800-1240 #product membrane glycoprotein E1 #status predicted !8#label EG1\ !$1212-1236 #domain transmembrane #status predicted #label TM5\ !$49,271,625,638,834, !$933 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1240 #molecular-weight 137290 #checksum 7491 SEQUENCE /// ENTRY VHWVVE #type complete TITLE structural polyprotein - Venezuelan equine encephalitis virus (strain TC-83) CONTAINS 6K peptide; coat protein; membrane glycoprotein E1; membrane glycoprotein E2; membrane glycoprotein E3 ORGANISM #formal_name Venezuelan equine encephalitis virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 16-Jul-1999 ACCESSIONS A27871 REFERENCE A27871 !$#authors Johnson, B.J.B.; Kinney, R.M.; Kost, C.L.; Trent, D.W. !$#journal J. Gen. Virol. (1986) 67:1951-1960 !$#title Molecular determinants of alphavirus neurovirulence: !1nucleotide and deduced protein sequence changes during !1attenuation of Venezuelan equine encephalitis virus. !$#cross-references MUID:86306669; PMID:3755750 !$#accession A27871 !'##molecule_type mRNA !'##residues 1-1254 ##label JOH !'##cross-references GB:X04368; NID:g58621; PIDN:CAA27883.1; PID:g58622 !'##note the authors translated the codon UUC for residues 19 and 27 as !1Ile and ACC for residue 30 as Ile CLASSIFICATION #superfamily togavirus structural polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; transmembrane !1protein FEATURE !$1-275 #product coat protein #status predicted #label COP\ !$276-334 #product membrane glycoprotein E3 #status predicted !8#label GP3\ !$335-757 #product membrane glycoprotein E2 #status predicted !8#label GP2\ !$702-718 #domain transmembrane #status predicted #label TM1\ !$758-812 #product 6K protein #status predicted #label PIP\ !$774-790 #domain transmembrane #status predicted #label TM2\ !$792-808 #domain transmembrane #status predicted #label TM3\ !$813-1254 #product membrane glycoprotein E1 #status predicted !8#label GP1\ !$1231-1247 #domain transmembrane #status predicted #label TM4\ !$47,286,546,625,652, !$946 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1254 #molecular-weight 138485 #checksum 3034 SEQUENCE /// ENTRY VHWVVT #type complete TITLE structural polyprotein - Venezuelan equine encephalitis virus (strain TRD) CONTAINS 6K protein; coat protein; membrane glycoprotein E1; membrane glycoprotein E2; membrane glycoprotein E3 ORGANISM #formal_name Venezuelan equine encephalitis virus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS B31467; A47612 REFERENCE A31467 !$#authors Kinney, R.M.; Johnson, B.J.B.; Welch, J.B.; Tsuchiya, K.R.; !1Trent, D.W. !$#journal Virology (1989) 170:19-30 !$#title The full-length nucleotide sequences of the virulent !1Trinidad donkey strain of Venezuelan equine encephalitis !1virus and its attenuated vaccine derivative, strain TC-83. !$#cross-references MUID:89243175; PMID:2524126 !$#accession B31467 !'##molecule_type mRNA !'##residues 1-1254 ##label KI1 !'##cross-references GB:J04332; NID:g323708; PIDN:AAB02519.1; !1PID:g323710 REFERENCE A47612 !$#authors Kinney, R.M.; Johnson, B.J.B.; Brown, V.L.; Trent, D.W. !$#journal Virology (1986) 152:400-413 !$#title Nucleotide sequence of the 26 S mRNA of the virulent !1Trinidad donkey strain of Venezuelan equine encephalitis !1virus and deduced sequence of the encoded structural !1proteins. !$#cross-references MUID:86263392; PMID:3088830 !$#accession A47612 !'##molecule_type mRNA !'##residues 1-542,'K',544-810,'P',812-1254 ##label KI2 !'##cross-references GB:L01442 CLASSIFICATION #superfamily togavirus structural polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; transmembrane !1protein FEATURE !$1-275 #product coat protein #status predicted #label CTP\ !$276-334 #product membrane glycoprotein E3 #status predicted !8#label MG3\ !$335-757 #product membrane glycoprotein E2 #status predicted !8#label MG2\ !$701-718 #domain transmembrane #status predicted #label TM1\ !$758-812 #product 6K protein #status predicted #label KP6\ !$774-790 #domain transmembrane #status predicted #label TM2\ !$795-813 #domain transmembrane #status predicted #label TM3\ !$813-1254 #product membrane glycoprotein E1 #status predicted !8#label MG1\ !$1231-1248 #domain transmembrane #status predicted #label TM4\ !$47,286,546,652,946 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1254 #molecular-weight 138350 #checksum 2798 SEQUENCE /// ENTRY B44213 #type complete TITLE structural polyprotein - Venezuelan equine encephalitis virus (strain P676) CONTAINS 6K protein; coat protein; membrane glycoprotein E1; membrane glycoprotein E2; membrane glycoprotein E3 ORGANISM #formal_name Venezuelan equine encephalitis virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS B44213 REFERENCE A44213 !$#authors Kinney, R.M.; Tsuchiya, K.R.; Sneider, J.M.; Trent, D.W. !$#journal Virology (1992) 191:569-580 !$#title Genetic evidence that epizootic Venezuelan equine !1encephalitis (VEE) viruses may have evolved from enzootic !1VEE subtype I-D virus. !$#cross-references MUID:93079859; PMID:1448915 !$#accession B44213 !'##molecule_type genomic RNA !'##residues 1-1255 ##label KIN !'##cross-references GB:L04653; NID:g290609; PIDN:AAC19319.1; !1PID:g290611 CLASSIFICATION #superfamily togavirus structural polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; transmembrane !1protein FEATURE !$1-275 #product coat protein #status predicted #label CTP\ !$276-334 #product membrane glycoprotein E3 #status predicted !8#label MG3\ !$335-757 #product membrane glycoprotein E2 #status predicted !8#label MG2\ !$702-722 #domain transmembrane #status predicted #label TM1\ !$758-813 #product 6K protein #status predicted #label KP6\ !$795-814 #domain transmembrane #status predicted #label TM2\ !$814-1255 #product membrane glycoprotein E1 #status predicted !8#label MG1\ !$1232-1249 #domain transmembrane #status predicted #label TM3\ !$47,286,652,947 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1255 #molecular-weight 138213 #checksum 2153 SEQUENCE /// ENTRY D44213 #type complete TITLE structural polyprotein - Venezuelan equine encephalitis virus (strain 3880) ORGANISM #formal_name Venezuelan equine encephalitis virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS D44213 REFERENCE A44213 !$#authors Kinney, R.M.; Tsuchiya, K.R.; Sneider, J.M.; Trent, D.W. !$#journal Virology (1992) 191:569-580 !$#title Genetic evidence that epizootic Venezuelan equine !1encephalitis (VEE) viruses may have evolved from enzootic !1VEE subtype I-D virus. !$#cross-references MUID:93079859; PMID:1448915 !$#accession D44213 !'##molecule_type genomic RNA !'##residues 1-1255 ##label KIN !'##cross-references GB:L00930; NID:g323706; PIDN:AAC19325.1; !1PID:g1375091 CLASSIFICATION #superfamily togavirus structural polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; transmembrane !1protein FEATURE !$1-275 #product coat protein #status predicted #label CTP\ !$276-334 #product membrane glycoprotein E3 #status predicted !8#label MG3\ !$335-757 #product membrane glycoprotein E2 #status predicted !8#label MG2\ !$702-722 #domain transmembrane #status predicted #label TM1\ !$758-813 #product 6K protein #status predicted #label KP6\ !$795-814 #domain transmembrane #status predicted #label TM2\ !$814-1255 #product membrane glycoprotein E1 #status predicted !8#label MG1\ !$1232-1249 #domain transmembrane #status predicted #label TM3\ !$47,286,652,947 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1255 #molecular-weight 138297 #checksum 1961 SEQUENCE /// ENTRY JQ1978 #type complete TITLE structural polyprotein - Venezuelan equine encephalitis virus (subtype II, strain Everglades Fe3-7c) CONTAINS 6K protein; coat protein; membrane glycoprotein E1; membrane glycoprotein E2; membrane glycoprotein E3 ORGANISM #formal_name Venezuelan equine encephalitis virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS JQ1978 REFERENCE JQ1978 !$#authors Sneider, J.M.; Kinney, R.M.; Tsuchiya, K.R.; Trent, D.W. !$#journal J. Gen. Virol. (1993) 74:519-523 !$#title Molecular evidence that epizootic Venezuelan equine !1encephalitis (VEE) I-AB viruses are not evolutionary !1derivatives of enzootic VEE subtype I-E or II viruses. !$#cross-references MUID:93187617; PMID:8445371 !$#accession JQ1978 !'##molecule_type mRNA !'##residues 1-1254 ##label SNE !'##cross-references GB:L04598; NID:g290612; PIDN:AAA42984.1; !1PID:g290614 CLASSIFICATION #superfamily togavirus structural polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; transmembrane !1protein FEATURE !$1-274 #product coat protein #status predicted #label CTP\ !$275-333 #product membrane glycoprotein E3 #status predicted !8#label MG3\ !$334-756 #product membrane glycoprotein E2 #status predicted !8#label MG2\ !$701-721 #domain transmembrane #status predicted #label TM1\ !$757-812 #product 6K protein #status predicted #label KP6\ !$794-813 #domain transmembrane #status predicted #label TM2\ !$813-1254 #product membrane glycoprotein E1 #status predicted !8#label MG1\ !$1231-1248 #domain transmembrane #status predicted #label TM3\ !$47,285,545,651,946 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1254 #molecular-weight 138337 #checksum 7087 SEQUENCE /// ENTRY JQ1979 #type complete TITLE structural polyprotein - Venezuelan equine encephalitis virus (subtype I, strain MenaII) CONTAINS 6K protein; coat protein; membrane glycoprotein E1; membrane glycoprotein E2; membrane glycoprotein E3 ORGANISM #formal_name Venezuelan equine encephalitis virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS JQ1979 REFERENCE JQ1978 !$#authors Sneider, J.M.; Kinney, R.M.; Tsuchiya, K.R.; Trent, D.W. !$#journal J. Gen. Virol. (1993) 74:519-523 !$#title Molecular evidence that epizootic Venezuelan equine !1encephalitis (VEE) I-AB viruses are not evolutionary !1derivatives of enzootic VEE subtype I-E or II viruses. !$#cross-references MUID:93187617; PMID:8445371 !$#accession JQ1979 !'##molecule_type mRNA !'##residues 1-1254 ##label SNE !'##cross-references GB:L04599; NID:g290619; PIDN:AAA42990.1; !1PID:g290621 CLASSIFICATION #superfamily togavirus structural polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; transmembrane !1protein FEATURE !$1-274 #product coat protein #status predicted #label CTP\ !$275-333 #product membrane glycoprotein E3 #status predicted !8#label MG3\ !$334-756 #product membrane glycoprotein E2 #status predicted !8#label MG2\ !$701-721 #domain transmembrane #status predicted #label TM1\ !$757-812 #product 6K protein #status predicted #label KP6\ !$794-813 #domain transmembrane #status predicted #label TM2\ !$813-1254 #product membrane glycoprotein E1 #status predicted !8#label MG1\ !$1231-1248 #domain transmembrane #status predicted #label TM3\ !$47,285,651,946 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1254 #molecular-weight 138342 #checksum 881 SEQUENCE /// ENTRY GNWVR4 #type complete TITLE structural polyprotein - rubella virus (strain Therien) CONTAINS capsid protein; membrane glycoprotein E1; membrane glycoprotein E2 ORGANISM #formal_name rubella virus DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 21-Jul-2000 ACCESSIONS A29822; A26884; B29811; B35320; A32270; B32270 REFERENCE A29822 !$#authors Takkinen, K.; Vidgren, G.; Ekstrand, J.; Hellman, U.; !1Kalkkinen, N.; Wernstedt, C.; Pettersson, R.F. !$#journal J. Gen. Virol. (1988) 69:603-612 !$#title Nucleotide sequence of the rubella virus capsid protein gene !1reveals an unusually high G/C content. !$#cross-references MUID:88171449; PMID:3351478 !$#accession A29822 !'##molecule_type genomic RNA !'##residues 1-319 ##label TAK !'##cross-references GB:D00242; NID:g222578; PIDN:BAA00172.1; !1PID:g222579 REFERENCE A32270 !$#authors Vidgren, G.; Takkinen, K.; Kalkkinen, N.; Kaariainen, L.; !1Pettersson, R.F. !$#journal J. Gen. Virol. (1987) 68:2347-2357 !$#title Nucleotide sequence of the genes coding for the membrane !1glycoproteins E1 and E2 of rubella virus. !$#cross-references MUID:88009948; PMID:3655744 !$#accession A26884 !'##molecule_type genomic RNA !'##residues 268-1063 ##label VID !'##cross-references GB:D00156; NID:g222576; PIDN:BAA28178.1; !1PID:g3133179 REFERENCE A29811 !$#authors Frey, T.K.; Marr, L.D. !$#journal Gene (1988) 62:85-99 !$#title Sequence of the region coding for virion proteins C and E2 !1and the carboxy terminus of the nonstructural proteins of !1rubella virus: comparison with alphaviruses. !$#cross-references MUID:88226020; PMID:2836271 !$#accession B29811 !'##molecule_type genomic RNA !'##residues 1-86,'T',88-162,'E',164-318,'C',320-394,'D',396-544,'L', !1546-621 ##label FRE !'##cross-references GB:M18901 REFERENCE A35320 !$#authors Dominguez, G.; Wang, C.Y.; Frey, T.K. !$#journal Virology (1990) 177:225-238 !$#title Sequence of the genome RNA of rubella virus: evidence for !1genetic rearrangement during Togavirus evolution. !$#cross-references MUID:90281585; PMID:2353453 !$#accession B35320 !'##molecule_type genomic RNA !'##residues 1-86,'T',88-162,'E',164-318,'C',320-394,'D',396-544,'L', !1546-958,'L',960-990,'T',992-1036,'I',1038-1063 ##label FR2 !'##cross-references GB:M15240; GB:M32735; NID:g333971; PIDN:AAA88529.1; !1PID:g333973 CLASSIFICATION #superfamily rubella virus structural polyprotein KEYWORDS capsid protein; glycoprotein; polyprotein; transmembrane !1protein FEATURE !$2-277 #product capsid protein #status predicted #label CAP\ !$278-562 #product membrane glycoprotein E2 precursor #status !8predicted #label PG2\ !$278-299 #domain nonterminal signal sequence #status predicted !8#label E2S\ !$300-562 #product membrane glycoprotein E2 #status predicted !8#label GL2\ !$539-555 #domain transmembrane #status predicted #label TM2\ !$563-1063 #product membrane glycoprotein E1 precursor #status !8predicted #label PG1\ !$563-582 #domain nonterminal signal sequence #status predicted !8#label E1S\ !$583-1063 #product membrane glycoprotein E1 #status predicted !8#label GL1\ !$1032-1050 #domain transmembrane #status predicted #label TM3\ !$353,371,410,429, !$658,759,791 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1063 #molecular-weight 114606 #checksum 2319 SEQUENCE /// ENTRY GNWVRA #type complete TITLE structural polyprotein - rubella virus (strain RA27/3 vaccine) CONTAINS capsid protein; membrane glycoprotein E1; membrane glycoprotein E2 ORGANISM #formal_name rubella virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS S04800 REFERENCE S04800 !$#authors Nakhasi, H.L.; Thomas, D.; Zheng, D.; Liu, T.Y. !$#journal Nucleic Acids Res. (1989) 17:4393-4394 !$#title Nucleotide sequence of capsid, E2 and E1 protein genes of !1rubella virus vaccine strain RA27/3. !$#cross-references MUID:89296505; PMID:2740235 !$#accession S04800 !'##molecule_type mRNA !'##residues 1-1063 ##label NAK !'##cross-references GB:X14871; NID:g61915; PIDN:CAA33016.1; PID:g61916 !'##note the authors translated the codon CGC for residue 207 as Val and !1AGC for residue 275 as Arg CLASSIFICATION #superfamily rubella virus structural polyprotein KEYWORDS capsid protein; glycoprotein; polyprotein; transmembrane !1protein FEATURE !$1-300 #product capsid protein C #status predicted #label !8NPC\ !$278-298 #domain transmembrane #status predicted #label TM1\ !$301-582 #product membrane glycoprotein E2 #status predicted !8#label E2G\ !$539-555 #domain transmembrane #status predicted #label TM2\ !$583-1063 #product membrane glycoprotein E1 #status predicted !8#label E1G\ !$1032-1050 #domain transmembrane #status predicted #label TM3\ !$353,371,410,429, !$658,759,791 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1063 #molecular-weight 114762 #checksum 3992 SEQUENCE /// ENTRY GNWV77 #type complete TITLE structural polyprotein - rubella virus (strain HPV77) CONTAINS capsid protein; membrane glycoprotein E1; membrane glycoprotein E2 ORGANISM #formal_name rubella virus DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS JQ0087 REFERENCE JQ0087 !$#authors Zheng, D.; Dickens, L.; Liu, T.Y.; Nakhasi, H.L. !$#journal Gene (1989) 82:343-349 !$#title Nucleotide sequence of the 24S subgenomic messenger RNA of a !1vaccine strain (HPV77) of rubella virus: comparison with a !1wild-type strain (M33). !$#cross-references MUID:90060825; PMID:2583526 !$#accession JQ0087 !'##molecule_type mRNA !'##residues 1-1063 ##label ZHE !'##cross-references GB:M30776; NID:g333974; PIDN:AAA47421.1; !1PID:g333975 CLASSIFICATION #superfamily rubella virus structural polyprotein KEYWORDS capsid protein; glycoprotein; polyprotein; transmembrane !1protein FEATURE !$1-300 #product capsid protein #status predicted #label CAP\ !$278-298 #domain transmembrane #status predicted #label TM1\ !$301-582 #product membrane glycoprotein E2 #status predicted !8#label EN2\ !$539-555 #domain transmembrane #status predicted #label TM2\ !$583-1063 #product membrane glycoprotein E1 #status predicted !8#label EN1\ !$1032-1050 #domain transmembrane #status predicted #label TM3\ !$353,371,429,658, !$759,791 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1063 #molecular-weight 114713 #checksum 1956 SEQUENCE /// ENTRY GNWVR3 #type complete TITLE structural polyprotein - rubella virus (strain M33) CONTAINS capsid protein; membrane glycoprotein E1; membrane glycoprotein E2 ORGANISM #formal_name rubella virus DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jul-1999 ACCESSIONS A27505 REFERENCE A27505 !$#authors Clarke, D.M.; Loo, T.W.; Hui, I.; Chong, P.; Gillam, S. !$#journal Nucleic Acids Res. (1987) 15:3041-3057 !$#title Nucleotide sequence and in vitro expression of rubella virus !124S subgenomic messenger RNA encoding the structural !1proteins E1, E2 and C. !$#cross-references MUID:87174825; PMID:3562245 !$#accession A27505 !'##molecule_type mRNA !'##residues 1-992 ##label CLA !'##cross-references GB:X05259; NID:g62093; PIDN:CAA28880.1; PID:g62094 CLASSIFICATION #superfamily rubella virus structural polyprotein KEYWORDS capsid protein; glycoprotein; polyprotein; transmembrane !1protein FEATURE !$1-299 #product capsid protein #status predicted #label NCP\ !$277-297 #domain transmembrane #status predicted #label TM1\ !$300-580 #product membrane glycoprotein E2 #status predicted !8#label ME2\ !$410-428 #domain transmembrane #status predicted #label TM2\ !$515-533 #domain transmembrane #status predicted #label TM3\ !$535-553 #domain transmembrane #status predicted #label TM4\ !$581-992 #product membrane glycoprotein E1 #status predicted !8#label ME1\ !$583-601 #domain transmembrane #status predicted #label TM5\ !$664-682 #domain transmembrane #status predicted #label TM6\ !$965-983 #domain transmembrane #status predicted #label TM7\ !$352,370,428,656, !$757,789 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 992 #molecular-weight 106904 #checksum 7511 SEQUENCE /// ENTRY GNWVR1 #type fragment TITLE structural polyprotein - rubella virus (fragment) CONTAINS carboxyl end of membrane glycoprotein E2; membrane glycoprotein E1 ORGANISM #formal_name rubella virus DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jul-1999 ACCESSIONS A25340 REFERENCE A25340 !$#authors Nakhasi, H.L.; Meyer, B.C.; Liu, T.Y. !$#journal J. Biol. Chem. (1986) 261:16616-16621 !$#title Rubella virus cDNA: sequence and expression of E1 envelope !1protein. !$#cross-references MUID:87057359; PMID:3023358 !$#accession A25340 !'##molecule_type mRNA !'##residues 1-522 ##label NAK !'##cross-references GB:J02620; NID:g333976; PIDN:AAA47423.1; !1PID:g333977 CLASSIFICATION #superfamily rubella virus structural polyprotein KEYWORDS glycoprotein; polyprotein; transmembrane protein FEATURE !$1-92 #product membrane glycoprotein E2 (carboxyl end) !8#status predicted #label ME2\ !$93-522 #product membrane glycoprotein E1 #status predicted !8#label ME1\ !$93-112 #domain transmembrane #status predicted #label TMN\ !$37,188,289,321 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 522 #checksum 4307 SEQUENCE /// ENTRY MNWVRN #type complete TITLE nonstructural polyprotein - rubella virus (strain Therien) CONTAINS nonstructural protein NS1; nonstructural protein NS2; nonstructural protein NS3; nonstructural protein NS4 ORGANISM #formal_name rubella virus DATE 30-Sep-1989 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS A35320; A29811 REFERENCE A35320 !$#authors Dominguez, G.; Wang, C.Y.; Frey, T.K. !$#journal Virology (1990) 177:225-238 !$#title Sequence of the genome RNA of rubella virus: evidence for !1genetic rearrangement during Togavirus evolution. !$#cross-references MUID:90281585; PMID:2353453 !$#accession A35320 !'##molecule_type genomic RNA !'##residues 1-2205 ##label DOM !'##cross-references GB:M15240; NID:g333971; PIDN:AAA88528.1; !1PID:g333972 REFERENCE A29811 !$#authors Frey, T.K.; Marr, L.D. !$#journal Gene (1988) 62:85-99 !$#title Sequence of the region coding for virion proteins C and E2 !1and the carboxy terminus of the nonstructural proteins of !1rubella virus: comparison with alphaviruses. !$#cross-references MUID:88226020; PMID:2836271 !$#accession A29811 !'##molecule_type genomic RNA !'##residues 1737-2205 ##label FRE !'##cross-references GB:M15240 COMMENT The cleavage sites of this polyprotein have not been !1determined. CLASSIFICATION #superfamily rubella virus nonstructural polyprotein KEYWORDS nonstructural protein SUMMARY #length 2205 #molecular-weight 240219 #checksum 5498 SEQUENCE /// ENTRY MNWVS #type complete TITLE nonstructural polyprotein - Sindbis virus CONTAINS nonstructural NS2; nonstructural protein NS1; nonstructural protein NS3; nonstructural protein NS4 ORGANISM #formal_name Sindbis virus DATE 19-Feb-1984 #sequence_revision 03-Aug-1984 #text_change 04-Oct-1996 ACCESSIONS A03917 REFERENCE A94331 !$#authors Strauss, E.G.; Rice, C.M.; Strauss, J.H. !$#journal Virology (1984) 133:92-110 !$#title Complete nucleotide sequence of the genomic RNA of Sindbis !1virus. !$#cross-references MUID:84148439; PMID:6322438 !$#accession A03917 !'##molecule_type genomic RNA !'##residues 1-2512 ##label STR !'##experimental_source strain HRSP !'##note readthrough of the terminator UGA between codons UAC for !11896-Tyr and CUA for 1897-Leu occurs CLASSIFICATION #superfamily Semliki Forest virus nonstructural protein KEYWORDS polyprotein FEATURE !$1-540 #product nonstructural protein NS1 #status predicted !8#label NS1\ !$541-1347 #product nonstructural protein NS2 #status predicted !8#label NS2\ !$1348-1896 #product nonstructural protein NS3 #status predicted !8#label NS3\ !$1897-2512 #product nonstructural protein NS4 #status predicted !8#label NS4 SUMMARY #length 2512 #molecular-weight 279547 #checksum 7528 SEQUENCE /// ENTRY MNWV82 #type complete TITLE nonstructural polyprotein - Ockelbo virus (strain Edsbyn 82-5) CONTAINS nonstructural protein NS1; nonstructural protein NS2; nonstructural protein NS3; nonstructural protein NS4 ORGANISM #formal_name Ockelbo virus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 08-Apr-1994 ACCESSIONS A39991 REFERENCE A39991 !$#authors Shirako, Y.; Niklasson, B.; Dalrymple, J.M.; Strauss, E.G.; !1Strauss, J.H. !$#journal Virology (1991) 182:753-764 !$#title Structure of the Ockelbo virus genome and its relationship !1to other Sindbis viruses. !$#cross-references MUID:91220725; PMID:1673813 !$#accession A39991 !'##molecule_type genomic RNA !'##residues 1-2514 ##label SHI !'##cross-references GB:M69205 CLASSIFICATION #superfamily Semliki Forest virus nonstructural protein KEYWORDS nonstructural protein; polyprotein FEATURE !$1-540 #product nonstructural protein NS1 #status predicted !8#label NS1\ !$541-1347 #product nonstructural protein NS2 #status predicted !8#label NS2\ !$1348-1898 #product nonstructural protein NS3 #status predicted !8#label NS3\ !$1899-2514 #product nonstructural protein NS4 #status predicted !8#label NS4 SUMMARY #length 2514 #molecular-weight 279643 #checksum 3491 SEQUENCE /// ENTRY MNWVSF #type complete TITLE nonstructural polyprotein - Semliki Forest virus CONTAINS nonstructural protein nsP1; nonstructural protein nsP2; nonstructural protein nsP3; nonstructural protein nsP4 ORGANISM #formal_name Semliki Forest virus DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jul-1999 ACCESSIONS A23592 REFERENCE A23592 !$#authors Takkinen, K. !$#journal Nucleic Acids Res. (1986) 14:5667-5682 !$#title Complete nucleotide sequence of the nonstructural protein !1genes of Semliki Forest virus. !$#cross-references MUID:86286581; PMID:3488539 !$#accession A23592 !'##molecule_type genomic RNA !'##residues 1-2431 ##label TAK !'##cross-references EMBL:X04129; NID:g58614; PIDN:CAA27741.1; !1PID:g58615 CLASSIFICATION #superfamily Semliki Forest virus nonstructural protein KEYWORDS nonstructural protein; polyprotein FEATURE !$1-537 #product nonstructural protein nsP1 #status predicted !8#label NS1\ !$538-1335 #product nonstructural protein nsP2 #status predicted !8#label NS2\ !$1336-1817 #product nonstructural protein nsP3 #status predicted !8#label NS3\ !$1818-2431 #product nonstructural protein nsP4 #status predicted !8#label NS4 SUMMARY #length 2431 #molecular-weight 269286 #checksum 354 SEQUENCE /// ENTRY MNWVRA #type complete TITLE nonstructural polyprotein - Ross River virus (strain NB5092 mouse-avirulent) CONTAINS nonstructural protein NS1; nonstructural protein NS2; nonstructural protein NS3; nonstructural protein NS4 ORGANISM #formal_name Ross River virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 12-Jun-1998 ACCESSIONS A28605 REFERENCE A94373 !$#authors Faragher, S.G.; Meek, A.D.J.; Rice, C.M.; Dalgarno, L. !$#journal Virology (1988) 163:509-526 !$#title Genome sequences of a mouse-avirulent and a mouse-virulent !1strain of Ross River virus. !$#cross-references MUID:88179556; PMID:2833022 !$#accession A28605 !'##molecule_type genomic RNA !'##residues 1-2479 ##label FAR COMMENT Readthrough of the terminator codon UGA occurs between the !1codons UUC for 1862-Phe and CUA for 1863-Leu. CLASSIFICATION #superfamily Semliki Forest virus nonstructural protein KEYWORDS nonstructural protein; polyprotein FEATURE !$1-533 #product nonstructural protein NS1 #status predicted !8#label NS1\ !$534-1331 #product nonstructural protein NS2 #status predicted !8#label NS2\ !$1332-1868 #product nonstructural protein NS3 #status predicted !8#label NS3\ !$1869-2479 #product nonstructural protein NS4 #status predicted !8#label NS4 SUMMARY #length 2479 #molecular-weight 276436 #checksum 6009 SEQUENCE /// ENTRY MNWVN2 #type complete TITLE nonstructural polyprotein - O'nyong-nyong virus (strain Gulu) CONTAINS nonstructural protein NS1; nonstructural protein NS2; nonstructural protein NS3; nonstructural protein NS4 ORGANISM #formal_name O'nyong-nyong virus #note host Anopheles gambiae DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS A34680; B28614 REFERENCE A34680 !$#authors Levinson, R.S.; Strauss, J.H.; Strauss, E.G. !$#journal Virology (1990) 175:110-123 !$#title Complete sequence of the genomic RNA of O'nyong-nyong virus !1and its use in the construction of alphavirus phylogenetic !1trees. !$#cross-references MUID:90177206; PMID:2155505 !$#accession A34680 !'##molecule_type genomic RNA !'##residues 1-2514 ##label LEV !'##cross-references GB:M20303; GB:M33999; NID:g332558; PIDN:AAA46784.1; !1PID:g332559 REFERENCE A28614 !$#authors Strauss, E.G.; Levinson, R.; Rice, C.M.; Dalrymple, J.; !1Strauss, J.H. !$#journal Virology (1988) 164:265-274 !$#title Nonstructural proteins nsP3 and nsP4 of Ross River and !1O'nyong-nyong viruses: sequence and comparison with those of !1other alphaviruses. !$#cross-references MUID:88206074; PMID:2834873 !$#accession B28614 !'##molecule_type genomic RNA !'##residues 1334-2492,'T',2494-2514 ##label STR CLASSIFICATION #superfamily Semliki Forest virus nonstructural protein KEYWORDS nonstructural protein FEATURE !$1-535 #product nonstructural protein NS1 #status predicted !8#label NS1\ !$536-1333 #product nonstructural protein NS2 #status predicted !8#label NS2\ !$1334-1903 #product nonstructural protein NS3 #status predicted !8#label NS3\ !$1904-2514 #product nonstructural protein NS4 #status predicted !8#label NS4 SUMMARY #length 2514 #molecular-weight 280115 #checksum 4832 SEQUENCE /// ENTRY MNWVTD #type complete TITLE nonstructural polyprotein - Venezuelan equine encephalitis virus (strain TRD) CONTAINS nonstructural protein NS1; nonstructural protein NS2; nonstructural protein NS3; nonstructural protein NS4 ORGANISM #formal_name Venezuelan equine encephalitis virus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 08-Apr-1994 ACCESSIONS A31467 REFERENCE A31467 !$#authors Kinney, R.M.; Johnson, B.J.B.; Welch, J.B.; Tsuchiya, K.R.; !1Trent, D.W. !$#journal Virology (1989) 170:19-30 !$#title The full-length nucleotide sequences of the virulent !1Trinidad donkey strain of Venezuelan equine encephalitis !1virus and its attenuated vaccine derivative, strain TC-83. !$#cross-references MUID:89243175; PMID:2524126 !$#accession A31467 !'##molecule_type mRNA !'##residues 1-2492 ##label KIN !'##cross-references GB:J04332 !'##note readthrough of the terminator UGA between codons CAA for !11879-Gln and CGG for 1880-Arg occurs CLASSIFICATION #superfamily Semliki Forest virus nonstructural protein KEYWORDS nonstructural protein; polyprotein FEATURE !$1-535 #product nonstructural protein NS1 #status predicted !8#label NS1\ !$536-1329 #product nonstructural protein NS2 #status predicted !8#label NS2\ !$1330-1879 #product nonstructural protein NS3 #status predicted !8#label NS3\ !$1880-2492 #product nonstructural protein NS4 #status predicted !8#label NS4 SUMMARY #length 2492 #molecular-weight 277902 #checksum 8861 SEQUENCE /// ENTRY A44213 #type complete TITLE nonstructural polyprotein - Venezuelan equine encephalitis virus (strain P676) CONTAINS nonstructural protein NS1; nonstructural protein NS2; nonstructural protein NS3; nonstructural protein NS4 ORGANISM #formal_name Venezuelan equine encephalitis virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 17-Feb-1994 ACCESSIONS A44213 REFERENCE A44213 !$#authors Kinney, R.M.; Tsuchiya, K.R.; Sneider, J.M.; Trent, D.W. !$#journal Virology (1992) 191:569-580 !$#title Genetic evidence that epizootic Venezuelan equine !1encephalitis (VEE) viruses may have evolved from enzootic !1VEE subtype I-D virus. !$#cross-references MUID:93079859; PMID:1448915 !$#accession A44213 !'##molecule_type genomic RNA !'##residues 1-2492 ##label KIN !'##cross-references GB:L04653 !'##note readthrough the terminator UGA occurs between the codons CAA !1for residue 1879-Gln and CGG for residue 1880-Arg CLASSIFICATION #superfamily Semliki Forest virus nonstructural protein KEYWORDS nonstructural protein; polyprotein FEATURE !$1-535 #product nonstructural protein NS1 #status predicted !8#label NS1\ !$536-1329 #product nonstructural protein NS2 #status predicted !8#label NS2\ !$1330-1879 #product nonstructural protein NS3 #status predicted !8#label NS3\ !$1880-2492 #product nonstructural protein NS4 #status predicted !8#label NS4 SUMMARY #length 2492 #molecular-weight 277836 #checksum 5930 SEQUENCE /// ENTRY C44213 #type complete TITLE nonstructural polyprotein - Venezuelan equine encephalitis virus (strain 3880) CONTAINS nonstructural protein NS1; nonstructural protein NS2; nonstructural protein NS3; nonstructural protein NS4 ORGANISM #formal_name Venezuelan equine encephalitis virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 17-Feb-1994 ACCESSIONS C44213 REFERENCE A44213 !$#authors Kinney, R.M.; Tsuchiya, K.R.; Sneider, J.M.; Trent, D.W. !$#journal Virology (1992) 191:569-580 !$#title Genetic evidence that epizootic Venezuelan equine !1encephalitis (VEE) viruses may have evolved from enzootic !1VEE subtype I-D virus. !$#cross-references MUID:93079859; PMID:1448915 !$#accession C44213 !'##molecule_type genomic RNA !'##residues 1-2492 ##label KIN !'##cross-references GB:L00930 !'##note readthrough the terminator UGA occurs between the codons CAA !1for residue 1879-Gln and CGG for residue 1880-Arg CLASSIFICATION #superfamily Semliki Forest virus nonstructural protein KEYWORDS nonstructural protein; polyprotein FEATURE !$1-535 #product nonstructural protein NS1 #status predicted !8#label NS1\ !$536-1329 #product nonstructural protein NS2 #status predicted !8#label NS2\ !$1330-1879 #product nonstructural protein NS3 #status predicted !8#label NS3\ !$1880-2492 #product nonstructural protein NS4 #status predicted !8#label NS4 SUMMARY #length 2492 #molecular-weight 277967 #checksum 21 SEQUENCE /// ENTRY MNWVM #type fragment TITLE nonstructural protein NS72 - Middelburg virus (fragment) ORGANISM #formal_name Middelburg virus DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 31-Dec-1993 ACCESSIONS A03918 REFERENCE A03918 !$#authors Strauss, E.G.; Rice, C.M.; Strauss, J.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:5271-5275 !$#title Sequence coding for the alphavirus nonstructural proteins is !1interrupted by an opal termination codon. !$#cross-references MUID:83299955; PMID:6577423 !$#accession A03918 !'##molecule_type genomic RNA !'##residues 1-994 ##label STR !'##note readthrough of the terminator UGA between codons GCA for !1378-Ala and CUA for 379-Leu may occur CLASSIFICATION #superfamily Semliki Forest virus nonstructural protein SUMMARY #length 994 #checksum 4596 SEQUENCE /// ENTRY WMWVBD #type complete TITLE 24K antigen - borna disease virus ORGANISM #formal_name borna disease virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS JQ1407; PQ0279; S15568 REFERENCE JQ1407 !$#authors Thierer, J.; Riehle, H.; Grebenstein, O.; Binz, T.; Herzog, !1S.; Thiedemann, N.; Stitz, L.; Rott, R.; Lottspeich, F.; !1Niemann, H. !$#journal J. Gen. Virol. (1992) 73:413-416 !$#title The 24K protein of Borna disease virus. !$#cross-references MUID:92166750; PMID:1538196 !$#accession JQ1407 !'##molecule_type mRNA !'##residues 1-201 ##label THI !'##cross-references EMBL:X60701; NID:g60640; PIDN:CAA43112.1; !1PID:g60641 !$#accession PQ0279 !'##molecule_type protein !'##residues 37-44;77-89;95-103;133-139;159-167 ##label TH2 CLASSIFICATION #superfamily borna disease virus 24K antigen SUMMARY #length 201 #molecular-weight 22461 #checksum 3218 SEQUENCE /// ENTRY QQMVTM #type complete TITLE superantigen Mtv(C3H) - mouse mammary tumor virus (provirus) ALTERNATE_NAMES Pr73 ORGANISM #formal_name mouse mammary tumor virus, MMTV DATE 18-Dec-1981 #sequence_revision 21-Jan-1997 #text_change 26-Feb-1999 ACCESSIONS S26389; A03919 REFERENCE S26388 !$#authors Majors, J.E.; Varmus, H.E. !$#journal J. Virol. (1983) 47:495-504 !$#title Nucleotide sequencing of an apparent proviral copy of env !1mRNA defines determinants of expression of the mouse mammary !1tumor virus env gene. !$#cross-references MUID:84011009; PMID:6312081 !$#accession S26389 !'##molecule_type DNA !'##residues 1-319 ##label MAJ !'##cross-references EMBL:K00556 !'##note the authors translated the codon GAA for residue 253 as Gly REFERENCE A03919 !$#authors Donehower, L.A.; Huang, A.L.; Hager, G.L. !$#journal J. Virol. (1981) 37:226-238 !$#title Regulatory and coding potential of the mouse mammary tumor !1virus long terminal redundancy. !$#cross-references MUID:81170700; PMID:6260976 !$#accession A03919 !'##molecule_type mRNA !'##residues 122-206,'P',208-309,'A',311-319 ##label DON !'##experimental_source strain C3H !'##note this protein is translated from a portion of the long terminal !1repeat region (LTR) CLASSIFICATION #superfamily superantigen Mtv7 KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-45 #domain intracellular #status predicted #label INT\ !$46-67 #domain transmembrane #status predicted #label TMM\ !$68-319 #domain extracellular #status predicted #label EXT\ !$79,89,93,131,146 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 319 #molecular-weight 36895 #checksum 4179 SEQUENCE /// ENTRY QQEV3M #type complete TITLE MTV superantigen - mouse mammary tumor virus (strain GR, clone H) ALTERNATE_NAMES Pr73 ORGANISM #formal_name mouse mammary tumor virus, MMTV DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 16-Jul-1999 ACCESSIONS A03920; S14282 REFERENCE A03920 !$#authors Fasel, N.; Pearson, K.; Buetti, E.; Diggelmann, H. !$#journal EMBO J. (1982) 1:3-7 !$#title The region of mouse mammary tumor virus DNA containing the !1long terminal repeat includes a long coding sequence and !1signals for hormonally regulated transcription. !$#cross-references MUID:84182450; PMID:6325151 !$#accession A03920 !'##molecule_type DNA !'##residues 1-320 ##label FAS !'##cross-references GB:V01175; GB:X16475; NID:g61619; PIDN:CAA24500.1; !1PID:g61620 !'##experimental_source strain GR, clone H !'##note this protein is translated from a portion of the long terminal !1repeat region (LTR) with the A of the initiation codon !1outside the LTR REFERENCE S14282 !$#authors Acha-Orbea, H.; Shakhov, A.N.; Scarpellino, L.; Kolb, E.; !1Mueller, V.; Vessaz-Shaw, A.; Fuchs, R.; Bloechlinger, K.; !1Rollini, P.; Billotte, J.; Sarafidou, M.; MacDonald, H.R.; !1Diggelmann, H. !$#journal Nature (1991) 350:207-211 !$#title Clonal deletion of V beta 14-bearing T cells in mice !1transgenic for mammary tumour virus. !$#cross-references MUID:91172317; PMID:1848685 !$#contents annotation CLASSIFICATION #superfamily superantigen Mtv7 SUMMARY #length 320 #molecular-weight 36968 #checksum 5039 SEQUENCE /// ENTRY QQMV6M #type complete TITLE MTV superantigen - mouse mammary tumor virus (strain GR) ALTERNATE_NAMES Pr73 ORGANISM #formal_name mouse mammary tumor virus, MMTV DATE 05-Apr-1983 #sequence_revision 05-Apr-1983 #text_change 31-Dec-1996 ACCESSIONS A03921 REFERENCE A03921 !$#authors Kennedy, N.; Knedlitschek, G.; Groner, B.; Hynes, N.E.; !1Herrlich, P.; Michalides, R.; van Ooyen, A.J.J. !$#journal Nature (1982) 295:622-624 !$#title Long terminal repeats of endogenous mouse mammary tumour !1virus contain a long open reading frame which extends into !1adjacent sequences. !$#cross-references MUID:82125504; PMID:6276778 !$#accession A03921 !'##molecule_type DNA !'##residues 1-324 ##label KEN !'##experimental_source strain GR !'##note the authors translated the codon AAG for residues 33 and 247 as !1Leu CLASSIFICATION #superfamily superantigen Mtv7 SUMMARY #length 324 #molecular-weight 37220 #checksum 6534 SEQUENCE /// ENTRY FOFV1R #type complete TITLE gag polyprotein - Rous sarcoma virus CONTAINS core protein 15; core protein p10; core protein p19; core protein p27; inner coat protein p12 ORGANISM #formal_name Rous sarcoma virus #note host Gallus gallus (chicken) DATE 01-Sep-1981 #sequence_revision 27-Nov-1985 #text_change 24-Sep-1999 ACCESSIONS A90834; A91465; S02807; A03922 REFERENCE A90834 !$#authors Schwartz, D.; Tizard, R.; Gilbert, W. !$#journal Cell (1983) 32:853-869 !$#title Nucleotide sequence of Rous sarcoma virus. !$#cross-references MUID:83155662; PMID:6299578 !$#accession A90834 !'##molecule_type genomic RNA !'##residues 1-701 ##label SCH !'##cross-references GB:J02342; GB:J02021; GB:J02343; NID:g210171; !1PIDN:AAB59932.1; PID:g210175 !'##experimental_source strain Prague C !'##note as a result of base variations, a different version of this !1sequence may exist having 204-Pro, 343-Asp, 396-Thr, !1446-Ala, 487-Val, 539-Asp, 561-Thr, 623-Thr, 634-Val, !1635-Asp, 636-Thr, and 641-Val REFERENCE A91465 !$#authors Misono, K.S.; Sharief, F.S.; Leis, J. !$#journal Fed. Proc. (1980) 39:1611 !$#accession A91465 !'##molecule_type protein !'##residues 489-504,'S',506-535,'E',537-566,568-577 ##label MIS !'##experimental_source strain Prague C !'##note the amidation state of residue 498 was not determined REFERENCE S02806 !$#authors Leis, J.; Phillips, N.; Fu, X.; Tuazon, P.T.; Traugh, J.A. !$#journal Eur. J. Biochem. (1989) 179:415-422 !$#title Phosphorylation of avian retrovirus matrix protein by Ca !1(2+)/phospholipid-dependent protein kinase. !$#cross-references MUID:89137119; PMID:2537209 !$#accession S02807 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-155 ##label LEI COMMENT This protein is synthesized as a gag-pol polyprotein. COMMENT The function of p15 is not clear; it may be an essential !1protease that cleaves the PR76 polyprotein. GENETICS !$#gene gag CLASSIFICATION #superfamily avian retrovirus gag polyprotein KEYWORDS core protein; inner coat protein; polyprotein FEATURE !$1-175 #product core protein p19 #status predicted #label !8C19\ !$178-239 #product core protein p10 #status predicted #label !8C10\ !$240-479 #product core protein p27 #status predicted #label !8C27\ !$489-577 #product inner coat protein p12 #status experimental !8#label C12\ !$578-701 #product core protein p15 #status predicted #label !8C15 SUMMARY #length 701 #molecular-weight 74526 #checksum 7556 SEQUENCE /// ENTRY FOFVF #type complete TITLE gag polyprotein - Fujinami sarcoma virus CONTAINS core protein p10; core protein p19; core protein p27 ORGANISM #formal_name Fujinami sarcoma virus #note host Gallus gallus (chicken) DATE 05-Apr-1983 #sequence_revision 27-Nov-1985 #text_change 12-Apr-1996 ACCESSIONS A03926 REFERENCE A00636 !$#authors Shibuya, M.; Hanafusa, H. !$#journal Cell (1982) 30:787-795 !$#title Nucleotide sequence of Fujinami sarcoma virus: evolutionary !1relationship of its transforming gene with transforming !1genes of other sarcoma viruses. !$#cross-references MUID:83050964; PMID:6291784 !$#accession A03926 !'##molecule_type genomic RNA !'##residues 1-309 ##label SHI COMMENT This protein is synthesized as a gag-fps polyprotein. GENETICS !$#gene gag CLASSIFICATION #superfamily avian retrovirus gag polyprotein KEYWORDS core protein; polyprotein FEATURE !$1-171 #product core protein p19 #status predicted #label !8C19\ !$174-235 #product core protein p10 #status predicted #label !8C10\ !$236-308 #product core protein p27 #status predicted #label !8C27 SUMMARY #length 309 #molecular-weight 32082 #checksum 8131 SEQUENCE /// ENTRY FOFVG9 #type complete TITLE gag polyprotein - avian sarcoma virus Y73 CONTAINS core protein p10; core protein p19 ORGANISM #formal_name avian sarcoma virus Y73 #note host Gallus gallus (chicken) DATE 18-Aug-1982 #sequence_revision 27-Nov-1985 #text_change 12-Apr-1996 ACCESSIONS A03927 REFERENCE A00633 !$#authors Kitamura, N.; Kitamura, A.; Toyoshima, K.; Hirayama, Y.; !1Yoshida, M. !$#journal Nature (1982) 297:205-208 !$#title Avian sarcoma virus Y73 genome sequence and structural !1similarity of its transforming gene product to that of Rous !1sarcoma virus. !$#cross-references MUID:82195528; PMID:6281656 !$#accession A03927 !'##molecule_type genomic RNA !'##residues 1-284 ##label KIT COMMENT This protein is synthesized as a gag-yes polyprotein. GENETICS !$#gene gag CLASSIFICATION #superfamily avian retrovirus gag polyprotein KEYWORDS core protein; polyprotein FEATURE !$1-177 #product core protein p19 #status predicted #label !8C19\ !$180-241 #product core protein p10 #status predicted #label !8C10 SUMMARY #length 284 #molecular-weight 29465 #checksum 2525 SEQUENCE /// ENTRY FOMVGS #type complete TITLE gag polyprotein - simian sarcoma virus CONTAINS core protein p15; core shell protein p30; inner coat protein p12; nucleoprotein p10 ORGANISM #formal_name simian sarcoma virus DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 20-Mar-1998 ACCESSIONS A03928 REFERENCE A03982 !$#authors Devare, S.G.; Reddy, E.P.; Law, J.D.; Robbins, K.C.; !1Aaronson, S.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:731-735 !$#title Nucleotide sequence of the simian sarcoma virus genome: !1demonstration that its acquired cellular sequences encode !1the transforming gene product p28(sis). !$#cross-references MUID:83144004; PMID:6298772 !$#accession A03928 !'##molecule_type genomic RNA !'##residues 1-512 ##label DEV !'##cross-references GB:J02394; NID:g555279; PID:g332620 GENETICS !$#gene gag CLASSIFICATION #superfamily mammalian retrovirus gag polyprotein I KEYWORDS polyprotein FEATURE !$1-128 #product core protein p15 #status predicted #label !8P15\ !$129-196 #product inner coat protein p12 #status predicted !8#label P12\ !$197-455 #product core shell protein p30 #status predicted !8#label P30\ !$456-512 #product nucleoprotein p10 #status predicted #label !8P10 SUMMARY #length 512 #molecular-weight 56893 #checksum 2043 SEQUENCE /// ENTRY FOLJGL #type complete TITLE gag polyprotein - gibbon ape leukemia virus CONTAINS core protein p10; core protein p12; core protein p15; core protein p30 ORGANISM #formal_name gibbon ape leukemia virus DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS A32595 REFERENCE A32595 !$#authors Delassus, S.; Sonigo, P.; Wain-Hobson, S. !$#journal Virology (1989) 173:205-213 !$#title Genetic organization of gibbon ape leukemia virus. !$#cross-references MUID:90051069; PMID:2683360 !$#accession A32595 !'##molecule_type genomic RNA !'##residues 1-520 ##label DEL !'##cross-references GB:M26927; NID:g332610; PIDN:AAA46809.1; !1PID:g332611 GENETICS !$#gene gag CLASSIFICATION #superfamily mammalian retrovirus gag polyprotein I KEYWORDS core protein FEATURE !$1-125 #product core protein p15 #status predicted #label !8P15\ !$126-195 #product core protein p12 #status predicted #label !8P12\ !$196-454 #product core protein p30 #status predicted #label !8P30\ !$455-520 #product core protein p10 #status predicted #label !8P10 SUMMARY #length 520 #molecular-weight 58109 #checksum 9057 SEQUENCE /// ENTRY FOVW5S #type complete TITLE gag polyprotein - Friend spleen focus-forming virus CONTAINS core protein p15; inner coat protein p12 ORGANISM #formal_name Friend spleen focus-forming virus DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 16-Jul-1999 ACCESSIONS A03929 REFERENCE A93966 !$#authors Clark, S.P.; Mak, T.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:5037-5041 !$#title Complete nucleotide sequence of an infectious clone of !1Friend spleen focus-forming provirus: gp55 is an envelope !1fusion glycoprotein. !$#cross-references MUID:83273746; PMID:6576374 !$#accession A03929 !'##molecule_type DNA !'##residues 1-187 ##label CLA !'##cross-references GB:K00021; NID:g331924; PIDN:AAA46486.1; !1PID:g331925 GENETICS !$#gene gag CLASSIFICATION #superfamily mammalian retrovirus gag polyprotein I KEYWORDS polyprotein FEATURE !$1-129 #product core protein p15 #status predicted #label !8P15\ !$130-187 #product inner coat protein p12 #status predicted !8#label P12 SUMMARY #length 187 #molecular-weight 20804 #checksum 5773 SEQUENCE /// ENTRY FOMV1M #type complete TITLE gag polyprotein - Moloney murine leukemia virus CONTAINS core protein p15; core shell protein p30; inner coat protein p12; nucleoprotein p10 ORGANISM #formal_name Moloney murine leukemia virus #note host Mus sp. (mouse) DATE 01-Sep-1981 #sequence_revision 27-Nov-1985 #text_change 24-Jul-1997 ACCESSIONS A03930 REFERENCE A93265 !$#authors Shinnick, T.M.; Lerner, R.A.; Sutcliffe, J.G. !$#journal Nature (1981) 293:543-548 !$#title Nucleotide sequence of Moloney murine leukaemia virus. !$#cross-references MUID:82035843; PMID:6169994 !$#accession A03930 !'##molecule_type genomic RNA !'##residues 1-538 ##label SHI !'##experimental_source clone pMLV-1 COMMENT This protein is synthesized as a gag-pol polyprotein. GENETICS !$#gene gag CLASSIFICATION #superfamily mammalian retrovirus gag polyprotein I KEYWORDS core protein; inner coat protein; nucleoprotein; polyprotein FEATURE !$2-131 #product core protein p15 #status predicted #label !8C15\ !$132-215 #product inner coat protein p12 #status predicted !8#label C12\ !$216-478 #product core shell protein p30 #status predicted !8#label C30\ !$479-534 #product nucleoprotein p10 #status predicted #label !8C10 SUMMARY #length 538 #molecular-weight 60786 #checksum 9177 SEQUENCE /// ENTRY FOMVM #type complete TITLE gag polyprotein - Moloney murine sarcoma virus CONTAINS core protein p15; core shell protein p30; inner coat protein p12; nucleoprotein p10 ORGANISM #formal_name Moloney murine sarcoma virus DATE 18-Dec-1981 #sequence_revision 18-Dec-1981 #text_change 16-Jul-1999 ACCESSIONS A94261; B00645; A03932 REFERENCE A94261 !$#authors Reddy, E.P.; Smith, M.J.; Aaronson, S.A. !$#journal Science (1981) 214:445-450 !$#title Complete nucleotide sequence and organization of the Moloney !1murine sarcoma virus genome. !$#cross-references MUID:82039559; PMID:6170110 !$#accession A94261 !'##molecule_type genomic RNA !'##residues 1-538 ##label RED !'##cross-references GB:J02266; NID:g331973; PIDN:AAA46499.1; !1PID:g331974 !'##experimental_source provirus REFERENCE A00645 !$#authors Van Beveren, C.; van Straaten, F.; Galleshaw, J.A.; Verma, !1I.M. !$#journal Cell (1981) 27:97-108 !$#title Nucleotide sequence of the genome of a murine sarcoma virus. !$#cross-references MUID:82115347; PMID:6173134 !$#accession B00645 !'##molecule_type DNA !'##residues 1-518,'K',520-538 ##label VAN !'##cross-references GB:V01185; GB:J02263; NID:g61647; PIDN:CAA24507.1; !1PID:g61648 !'##experimental_source clone 124, circular GENETICS !$#gene gag CLASSIFICATION #superfamily mammalian retrovirus gag polyprotein I KEYWORDS polyprotein FEATURE !$2-131 #product core protein p15 #status predicted #label !8P15\ !$132-215 #product inner coat protein p12 #status predicted !8#label P12\ !$216-478 #product core shell protein p30 #status predicted !8#label P30\ !$479-534 #product nucleoprotein p10 #status predicted #label !8P10 SUMMARY #length 538 #molecular-weight 61209 #checksum 590 SEQUENCE /// ENTRY FOMVMU #type complete TITLE gag polyprotein - Moloney murine sarcoma virus (strain MuSVts110) ALTERNATE_NAMES core polyprotein CONTAINS core protein p15; core shell protein p30; inner coat protein p12 ORGANISM #formal_name Moloney murine sarcoma virus DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 26-Feb-1999 ACCESSIONS A42745 REFERENCE A42745 !$#authors Huai, L.; Chiocca, S.M.; Gilbreth, M.A.; Ainsworth, J.R.; !1Bishop, L.A.; Murphy Jr., E.C. !$#journal J. Virol. (1992) 66:5329-5337 !$#title Moloney murine sarcoma virus MuSVts110 DNA: cloning, !1nucleotide sequence, and gene expression. !$#cross-references MUID:92365121; PMID:1501276 !$#accession A42745 !'##molecule_type DNA !'##residues 1-468 ##label HUA !'##cross-references GB:M96854 GENETICS !$#gene gag CLASSIFICATION #superfamily mammalian retrovirus gag polyprotein I KEYWORDS coat protein; core protein; polyprotein FEATURE !$2-131 #product core protein p15 #status predicted #label !8P15\ !$132-215 #product inner coat protein p12 #status predicted !8#label P12\ !$216-468 #product core shell protein p30 #status predicted !8#label P30 SUMMARY #length 468 #molecular-weight 52681 #checksum 3522 SEQUENCE /// ENTRY FOMVGV #type complete TITLE gag polyprotein - AKV murine leukemia virus CONTAINS core protein p15; core shell protein p30; inner coat protein p12; nucleoprotein p10 ORGANISM #formal_name AKV murine leukemia virus #note host Mus sp. (mouse) DATE 03-Aug-1984 #sequence_revision 27-Nov-1985 #text_change 16-Jul-1999 ACCESSIONS A03933 REFERENCE A92995 !$#authors Herr, W. !$#journal J. Virol. (1984) 49:471-478 !$#title Nucleotide sequence of AKV murine leukemia virus. !$#cross-references MUID:84115072; PMID:6319746 !$#accession A03933 !'##molecule_type genomic RNA !'##residues 1-537 ##label HER !'##cross-references GB:J01998; GB:J01999; GB:K00016; GB:K00017; !1GB:K00018; GB:K01394; NID:g331993; PIDN:AAB03090.1; !1PID:g331994 COMMENT This protein is synthesized as a gag-pol polyprotein. GENETICS !$#gene gag CLASSIFICATION #superfamily mammalian retrovirus gag polyprotein I KEYWORDS core protein; inner coat protein; nucleoprotein; polyprotein FEATURE !$1-129 #product core protein p15 #status predicted #label !8C15\ !$130-214 #product inner coat protein p12 #status predicted !8#label C12\ !$215-477 #product core shell protein p30 #status predicted !8#label C30\ !$478-537 #product nucleoprotein p10 #status predicted #label !8C10 SUMMARY #length 537 #molecular-weight 60557 #checksum 9930 SEQUENCE /// ENTRY FOMVFB #type fragment TITLE gag polyprotein - FBR murine osteosarcoma virus (provirus) (fragment) CONTAINS amino end of core shell protein p30; core protein p15; inner coat protein p12 ORGANISM #formal_name FBR murine osteosarcoma virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 24-Jul-1997 ACCESSIONS A23244 REFERENCE A23244 !$#authors Van Beveren, C.; Enami, S.; Curran, T.; Verma, I.M. !$#journal Virology (1984) 135:229-243 !$#title FBR murine osteosarcoma virus. II. Nucleotide sequence of !1the provirus reveals that the genome contains sequences !1acquired from two cellular genes. !$#cross-references MUID:84225828; PMID:6203215 !$#accession A23244 !'##molecule_type mRNA !'##residues 1-310 ##label VAN !'##cross-references EMBL:K02712 COMMENT This protein is synthesized as a gag-fos-fox polyprotein. GENETICS !$#gene gag CLASSIFICATION #superfamily mammalian retrovirus gag polyprotein I KEYWORDS core protein; inner coat protein; polyprotein FEATURE !$1-129 #product core protein p15 #status predicted #label !8P15\ !$130-214 #product inner coat protein p12 #status predicted !8#label P12\ !$215-310 #product core shell protein p30 (fragment) #status !8predicted #label P30 SUMMARY #length 310 #checksum 2722 SEQUENCE /// ENTRY FOMVRV #type complete TITLE gag polyprotein - radiation murine leukemia virus CONTAINS core protein p15; core shell protein p30; inner coat protein p12; nucleoprotein p10 ORGANISM #formal_name radiation murine leukemia virus DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 16-Jul-1999 ACCESSIONS A26183 REFERENCE A94362 !$#authors Merregaert, J.; Janowski, M.; Reddy, E.P. !$#journal Virology (1987) 158:88-102 !$#title Nucleotide sequence of a radiation leukemia virus genome. !$#cross-references MUID:87207680; PMID:3033897 !$#accession A26183 !'##molecule_type DNA !'##residues 1-537 ##label MER !'##cross-references GB:K03363; GB:M18449; NID:g332032; PIDN:AAA46518.1; !1PID:g332033 GENETICS !$#gene gag CLASSIFICATION #superfamily mammalian retrovirus gag polyprotein I KEYWORDS core protein; inner coat protein; nucleoprotein; polyprotein FEATURE !$1-129 #product core protein p15 #status predicted #label !8P15\ !$130-214 #product inner coat protein p12 #status predicted !8#label P12\ !$215-477 #product core shell protein p30 #status predicted !8#label P30\ !$478-537 #product nucleoprotein p10 #status predicted #label !8P10 SUMMARY #length 537 #molecular-weight 60784 #checksum 9194 SEQUENCE /// ENTRY FOMVMB #type complete TITLE gag polyprotein - murine leukemia virus (strain BM5 ECO) CONTAINS core protein p15; core shell protein p30; inner coat protein p12; nucleoprotein p10 ORGANISM #formal_name murine leukemia virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS A40416 REFERENCE A40416 !$#authors Chattopadhyay, S.K.; Sengupta, D.N.; Fredrickson, T.N.; !1Morse III, H.C.; Hartley, J.W. !$#journal J. Virol. (1991) 65:4232-4241 !$#title Characteristics and contributions of defective, ecotropic, !1and mink cell focus-inducing viruses involved in a !1retrovirus-induced immunodeficiency syndrome of mice. !$#cross-references MUID:91303677; PMID:1649328 !$#accession A40416 !'##molecule_type DNA !'##residues 1-537 ##label CHA !'##cross-references GB:M64095; NID:g332014; PIDN:AAA46510.1; !1PID:g332015 GENETICS !$#gene gag CLASSIFICATION #superfamily mammalian retrovirus gag polyprotein I KEYWORDS core protein; inner coat protein; nucleoprotein; polyprotein FEATURE !$1-129 #product core protein p15 #status predicted #label !8CP1\ !$130-214 #product inner coat protein p12 #status predicted !8#label ICP\ !$215-477 #product core shell protein p30 #status predicted !8#label CSP\ !$478-537 #product nucleoprotein p10 #status predicted #label !8NP1 SUMMARY #length 537 #molecular-weight 60422 #checksum 9155 SEQUENCE /// ENTRY FOMVME #type complete TITLE gag polyprotein - murine leukemia virus (strain DEF27) CONTAINS core protein p15; core shell protein p30; inner coat protein p12; nucleoprotein p10 ORGANISM #formal_name murine leukemia virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 24-Jul-1997 ACCESSIONS B40416 REFERENCE A40416 !$#authors Chattopadhyay, S.K.; Sengupta, D.N.; Fredrickson, T.N.; !1Morse III, H.C.; Hartley, J.W. !$#journal J. Virol. (1991) 65:4232-4241 !$#title Characteristics and contributions of defective, ecotropic, !1and mink cell focus-inducing viruses involved in a !1retrovirus-induced immunodeficiency syndrome of mice. !$#cross-references MUID:91303677; PMID:1649328 !$#accession B40416 !'##molecule_type DNA !'##residues 1-536 ##label CHA !'##cross-references GB:M64096 GENETICS !$#gene gag CLASSIFICATION #superfamily mammalian retrovirus gag polyprotein I KEYWORDS core protein; inner coat protein; nucleoprotein; polyprotein FEATURE !$1-129 #product core protein p15 #status predicted #label !8CP1\ !$130-213 #product inner coat protein p12 #status predicted !8#label ICP\ !$214-476 #product core shell protein p30 #status predicted !8#label CSP\ !$477-536 #product nucleoprotein p10 #status predicted #label !8NP1 SUMMARY #length 536 #molecular-weight 60890 #checksum 7358 SEQUENCE /// ENTRY FOMVHL #type complete TITLE gag polyprotein - HoMuLV murine leukemia virus CONTAINS core protein p10; core protein p12; core protein p15; core protein p30 ORGANISM #formal_name HoMuLV murine leukemia virus #note host Mus hortulanus (European mouse) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS A32594 REFERENCE A32594 !$#authors Voytek, P.; Kozak, C.A. !$#journal Virology (1989) 173:58-67 !$#title Nucleotide sequence and mode of transmission of the wild !1mouse ecotropic virus, HoMuLV. !$#cross-references MUID:90051094; PMID:2554579 !$#accession A32594 !'##molecule_type DNA !'##residues 1-540 ##label VOY !'##cross-references GB:M26528; GB:J04372; NID:g329579; PIDN:AAA45464.1; !1PID:g329580 !'##note the authors translated the codon TGG for residue 401 as Gln GENETICS !$#gene gag CLASSIFICATION #superfamily mammalian retrovirus gag polyprotein I KEYWORDS core protein; polyprotein FEATURE !$2-129 #product core protein p15 #status predicted #label !8CP5\ !$130-217 #product core protein p12 #status predicted #label !8CP2\ !$218-480 #product core protein p30 #status predicted #label !8CP3\ !$481-540 #product core protein p10 #status predicted #label !8CP1 SUMMARY #length 540 #molecular-weight 61382 #checksum 1516 SEQUENCE /// ENTRY FOMVDU #type complete TITLE gag polyprotein - Duplan murine leukemia virus CONTAINS core protein p15; core shell protein p30; inner coat protein p12; nucleoprotein p10 ORGANISM #formal_name Duplan murine leukemia virus DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS S03901 REFERENCE S03901 !$#authors Aziz, D.C.; Hanna, Z.; Jolicoeur, P. !$#journal Nature (1989) 338:505-508 !$#title Severe immunodeficiency disease induced by a defective !1murine leukaemia virus. !$#cross-references MUID:89181946; PMID:2538760 !$#accession S03901 !'##molecule_type DNA !'##residues 1-529 ##label AZI !'##cross-references EMBL:X14576; NID:g61652; PIDN:CAA32715.1; !1PID:g61653 GENETICS !$#gene gag CLASSIFICATION #superfamily mammalian retrovirus gag polyprotein I KEYWORDS core protein; inner coat protein; nucleoprotein; polyprotein FEATURE !$2-129 #product core protein p15 #status predicted #label !8P15\ !$130-206 #product inner coat protein p12 #status predicted !8#label P12\ !$207-469 #product core shell protein p30 #status predicted !8#label P30\ !$470-525 #product nucleoprotein p10 #status predicted #label !8P10 SUMMARY #length 529 #molecular-weight 60318 #checksum 5212 SEQUENCE /// ENTRY FOMVGC #type complete TITLE gag polyprotein - feline sarcoma virus (strain Gardner-Arnstein) CONTAINS core protein p12; core protein p15; core protein p30 ORGANISM #formal_name feline sarcoma virus #note host Felis sp. (cat) DATE 05-Apr-1983 #sequence_revision 27-Nov-1985 #text_change 12-Apr-1996 ACCESSIONS A03934; B03934 REFERENCE A92990 !$#authors Hampe, A.; Gobet, M.; Even, J.; Sherr, C.J.; Galibert, F. !$#journal J. Virol. (1983) 45:466-472 !$#title Nucleotide sequences of feline sarcoma virus long terminal !1repeats and 5' leaders show extensive homology to those of !1other mammalian retroviruses. !$#cross-references MUID:83112218; PMID:6296453 !$#accession A03934 !'##molecule_type DNA !'##residues 1-78 ##label HAM REFERENCE A00651 !$#authors Hampe, A.; Laprevotte, I.; Galibert, F.; Fedele, L.A.; !1Sherr, C.J. !$#journal Cell (1982) 30:775-785 !$#title Nucleotide sequences of feline retroviral oncogenes (v-fes) !1provide evidence for a family of typrosine-specific protein !1kinase genes. !$#cross-references MUID:83050963; PMID:6183005 !$#accession B03934 !'##molecule_type DNA !'##residues 78-425 ##label HAM2 COMMENT This protein is synthesized as a gag-fes polyprotein. GENETICS !$#gene gag CLASSIFICATION #superfamily mammalian retrovirus gag polyprotein I KEYWORDS core protein; polyprotein FEATURE !$78-204 #product core protein p15 #status predicted #label !8C15\ !$205-274 #product core protein p12 #status predicted #label !8C12\ !$275-425 #product core protein p30 #status predicted #label !8C30 SUMMARY #length 425 #molecular-weight 47008 #checksum 2517 SEQUENCE /// ENTRY FOMVCS #type complete TITLE gag polyprotein - feline sarcoma virus (strain Snyder-Theilen) CONTAINS core protein p12; core protein p15; core protein p30 ORGANISM #formal_name feline sarcoma virus #note host Felis sp. (cat) DATE 05-Apr-1983 #sequence_revision 27-Nov-1985 #text_change 12-Apr-1996 ACCESSIONS A03935; B03935 REFERENCE A92990 !$#authors Hampe, A.; Gobet, M.; Even, J.; Sherr, C.J.; Galibert, F. !$#journal J. Virol. (1983) 45:466-472 !$#title Nucleotide sequences of feline sarcoma virus long terminal !1repeats and 5' leaders show extensive homology to those of !1other mammalian retroviruses. !$#cross-references MUID:83112218; PMID:6296453 !$#accession A03935 !'##molecule_type DNA !'##residues 1-75 ##label HAM REFERENCE A00651 !$#authors Hampe, A.; Laprevotte, I.; Galibert, F.; Fedele, L.A.; !1Sherr, C.J. !$#journal Cell (1982) 30:775-785 !$#title Nucleotide sequences of feline retroviral oncogenes (v-fes) !1provide evidence for a family of typrosine-specific protein !1kinase genes. !$#cross-references MUID:83050963; PMID:6183005 !$#accession B03935 !'##molecule_type DNA !'##residues 75-371 ##label HAM2 COMMENT This protein is synthesized as a gag-fes polyprotein. GENETICS !$#gene gag CLASSIFICATION #superfamily mammalian retrovirus gag polyprotein I KEYWORDS core protein; polyprotein FEATURE !$75-201 #product core protein p15 #status predicted #label !8C15\ !$202-271 #product core protein p12 #status predicted #label !8C12\ !$272-371 #product core protein p30 #status predicted #label !8C30 SUMMARY #length 371 #molecular-weight 40829 #checksum 4397 SEQUENCE /// ENTRY FOMVMD #type complete TITLE gag polyprotein - feline sarcoma virus (strain McDonough) CONTAINS core protein p10; core protein p12; core protein p15; core protein p30 ORGANISM #formal_name feline sarcoma virus #note host Felis sp. (cat) DATE 18-Apr-1984 #sequence_revision 27-Nov-1985 #text_change 04-Dec-1994 ACCESSIONS A03938 REFERENCE A00654 !$#authors Hampe, A.; Gobet, M.; Sherr, C.J.; Galibert, F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:85-89 !$#title Nucleotide sequence of the feline retroviral oncogene v-fms !1shows unexpected homology with oncogenes encoding !1tyrosine-specific protein kinases. !$#cross-references MUID:84119469; PMID:6582485 !$#accession A03938 !'##molecule_type DNA !'##residues 1-536 ##label HAM COMMENT This protein is synthesized as a gag-fms polyprotein. GENETICS !$#gene gag CLASSIFICATION #superfamily mammalian retrovirus gag polyprotein I KEYWORDS core protein; polyprotein FEATURE !$1-77 #domain leader peptide #status predicted #label LDP\ !$78-204 #product core protein p15 #status predicted #label !8C15\ !$205-274 #product core protein p12 #status predicted #label !8C12\ !$275-522 #product core protein p30 #status predicted #label !8P30\ !$523-536 #product core protein p10 #status predicted #label !8P10 SUMMARY #length 536 #molecular-weight 60234 #checksum 8308 SEQUENCE /// ENTRY FOMVVB #type complete TITLE gag polyprotein - baboon endogenous virus CONTAINS core protein p15; core shell protein p30; inner coat protein p12; nucleoprotein p10 ORGANISM #formal_name baboon endogenous virus strain M7 #note host Papio sp. (baboon) DATE 19-Feb-1984 #sequence_revision 27-Nov-1985 #text_change 18-Jul-2001 ACCESSIONS A03939 REFERENCE A03939 !$#authors Tamura, T. !$#journal J. Virol. (1983) 47:137-145 !$#title Provirus of M7 baboon endogenous virus: nucleotide sequence !1of the gag-pol region. !$#cross-references MUID:83241915; PMID:6408267 !$#accession A03939 !'##molecule_type DNA !'##residues 1-532 ##label TAM COMMENT This protein is synthesized as a gag-pol polyprotein. GENETICS !$#gene gag CLASSIFICATION #superfamily mammalian retrovirus gag polyprotein I KEYWORDS core protein; inner coat protein; nucleoprotein; polyprotein FEATURE !$1-111 #product inner coat protein p12 #status predicted !8#label C12\ !$112-218 #product core protein p15 #status predicted #label !8C15\ !$219-472 #product core shell protein p30 #status predicted !8#label C30\ !$473-532 #product nucleoprotein p10 #status predicted #label !8C10 SUMMARY #length 532 #molecular-weight 59616 #checksum 8122 SEQUENCE /// ENTRY FOMVM7 #type complete TITLE gag polyprotein - baboon endogenous virus (strain M7) CONTAINS core protein p15; core shell protein p30; inner coat protein p12; nucleoprotein p10 ORGANISM #formal_name baboon endogenous virus #note host Papio sp. (baboon) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jun-2000 ACCESSIONS JT0260 REFERENCE JT0260 !$#authors Kato, S.; Matsuo, K.; Nishimura, N.; Takahashi, N.; Takano, !1T. !$#journal Jpn. J. Genet. (1987) 62:127-137 !$#title The entire nucleotide sequence of baboon endogenous virus !1DNA: a chimeric genome structure of murine type C and simian !1type D retroviruses. !$#accession JT0260 !'##molecule_type DNA !'##residues 1-537 ##label KAT !'##cross-references GB:D10032; GB:D00088; NID:g218567; PIDN:BAA00923.1; !1PID:g218568 COMMENT This protein is synthesized as a gag-pol polyprotein. GENETICS !$#gene gag CLASSIFICATION #superfamily mammalian retrovirus gag polyprotein I KEYWORDS core protein; inner coat protein; nucleoprotein; polyprotein FEATURE !$1-112 #product inner coat protein p12 #status predicted !8#label INP\ !$113-226 #product core protein p15 #status predicted #label !8CPP\ !$227-477 #product core shell protein p30 #status predicted !8#label CSP\ !$478-537 #product nucleoprotein p10 #status predicted #label !8NPP SUMMARY #length 537 #molecular-weight 60623 #checksum 8978 SEQUENCE /// ENTRY FOVDA #type fragment TITLE gag polyprotein - avian spleen necrosis virus (fragment) CONTAINS core protein p15; core shell protein p30; inner coat protein p12 ORGANISM #formal_name avian spleen necrosis virus DATE 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 16-Jul-1999 ACCESSIONS A93904; A92985; A03940 REFERENCE A93904 !$#authors O'Rear, J.J.; Temin, H.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:1230-1234 !$#title Spontaneous changes in nucleotide sequence in proviruses of !1spleen necrosis virus, an avian retrovirus. !$#cross-references MUID:82174569; PMID:6951170 !$#contents provirus !$#accession A93904 !'##molecule_type DNA !'##residues 1-313 ##label ORE !'##cross-references GB:V01200; NID:g61757; PIDN:CAA24513.1; PID:g61758 REFERENCE A92985 !$#authors Oroszlan, S.; Barbacid, M.; Copeland, T.D.; Aaronson, S.A.; !1Gilden, R.V. !$#journal J. Virol. (1981) 39:845-854 !$#title Chemical and immunological characterization of the major !1structural protein (p28) of MMC-1, a rhesus monkey !1endogenous type C virus: homology with the major structural !1protein of avian reticuloendotheliosis virus. !$#cross-references MUID:82033276; PMID:6169843 !$#accession A92985 !'##molecule_type protein !'##residues 200-209,'G',211-230,'X',232-233,'XF' ##label ORO GENETICS !$#gene gag CLASSIFICATION #superfamily mammalian retrovirus gag polyprotein I KEYWORDS polyprotein FEATURE !$1-133 #product core protein p15 #status predicted #label !8P15\ !$134-199 #product inner coat protein p12 #status predicted !8#label P12\ !$200-313 #product core shell protein p30 (fragment) #status !8predicted #label P30 SUMMARY #length 313 #checksum 735 SEQUENCE /// ENTRY FOMVMM #type complete TITLE gag polyprotein - mouse mammary tumor virus ORGANISM #formal_name mouse mammary tumor virus, MMTV DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 16-Jul-1999 ACCESSIONS A26795 REFERENCE A93030 !$#authors Moore, R.; Dixon, M.; Smith, R.; Peters, G.; Dickson, C. !$#journal J. Virol. (1987) 61:480-490 !$#title Complete nucleotide sequence of a milk-transmitted mouse !1mammary tumor virus: two frameshift suppression events are !1required for translation of gag and pol. !$#cross-references MUID:87112944; PMID:3027377 !$#accession A26795 !'##molecule_type DNA !'##residues 1-591 ##label MOO !'##cross-references EMBL:M15122; NID:g332127; PIDN:AAA46543.1; !1PID:g332130 GENETICS !$#gene gag CLASSIFICATION #superfamily mouse mammary tumor virus gag polyprotein KEYWORDS core protein; DNA binding; polyprotein SUMMARY #length 591 #molecular-weight 66269 #checksum 4227 SEQUENCE /// ENTRY FOMVGR #type fragment TITLE gag polyprotein - mouse mammary tumor virus (strain GR) (fragment) ORGANISM #formal_name mouse mammary tumor virus, MMTV DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS A03941 REFERENCE A03941 !$#authors Fasel, N.; Buetti, E.; Firzlaff, J.; Pearson, K.; !1Diggelmann, H. !$#journal Nucleic Acids Res. (1983) 11:6943-6955 !$#title Nucleotide sequence of the 5' noncoding region and part of !1the gag gene of mouse mammary tumor virus; identification of !1the 5' splicing site for subgenomic mRNAs. !$#cross-references MUID:84041495; PMID:6314267 !$#accession A03941 !'##molecule_type DNA !'##residues 1-353 ##label FAS !'##cross-references GB:X00018; NID:g61621; PIDN:CAA24916.1; PID:g61622 CLASSIFICATION #superfamily mouse mammary tumor virus gag polyprotein KEYWORDS polyprotein SUMMARY #length 353 #checksum 5120 SEQUENCE /// ENTRY FOLJGB #type complete TITLE gag polyprotein - bovine leukemia virus ALTERNATE_NAMES core polyprotein CONTAINS core protein p12; core protein p15; core protein p24 ORGANISM #formal_name bovine leukemia virus, BLV #note host Bos sp. (cattle) DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 31-Mar-2000 ACCESSIONS A94063; A93812; A91311; A03942 REFERENCE A94063 !$#authors Sagata, N.; Yasunaga, T.; Tsuzuku-Kawamura, J.; Ohishi, K.; !1Ogawa, Y.; Ikawa, Y. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:677-681 !$#title Complete nucleotide sequence of the genome of bovine !1leukemia virus: its evolutionary relationship to other !1retroviruses. !$#cross-references MUID:85140159; PMID:2983308 !$#accession A94063 !'##molecule_type DNA !'##residues 1-392 ##label SAG !'##cross-references GB:K02120; NID:g210767; PIDN:AAA42784.1; !1PID:g210768 !'##note core protein p15 is a phosphorylated basic gag product !'##note core protein p12 is a genome-binding protein with repeated !1sequences !'##note the authors translated the codon TAT for residue 7 as Thr and !1TAC for residue 43 as Thr REFERENCE A93812 !$#authors Oroszlan, S.; Copeland, T.D.; Henderson, L.E.; Stephenson, !1J.R.; Gilden, R.V. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1979) 76:2996-3000 !$#title Amino-terminal sequence of bovine leukemia virus major !1internal protein: Homology with mammalian type C virus p30 !1structural proteins. !$#cross-references MUID:79223918; PMID:223166 !$#accession A93812 !'##molecule_type protein !'##residues 110-164 ##label ORO REFERENCE A91311 !$#authors Copeland, T.D.; Morgan, M.A.; Oroszlan, S. !$#journal FEBS Lett. (1983) 156:37-40 !$#title Complete amino acid sequence of the nucleic acid-binding !1protein of bovine leukemia virus. !$#cross-references MUID:83210199; PMID:6303852 !$#accession A91311 !'##molecule_type protein !'##residues 324-392 ##label COP GENETICS !$#gene gag CLASSIFICATION #superfamily mammalian retrovirus gag polyprotein II KEYWORDS core protein; duplication; phosphoprotein; polyprotein FEATURE !$1-109 #product core protein p15 #status predicted #label !8P15\ !$110-323 #product core protein p24 #status predicted #label !8P24\ !$324-392 #product core protein p12 #status experimental #label !8P12\ !$342-362,367-387 #region duplication SUMMARY #length 392 #molecular-weight 42531 #checksum 9762 SEQUENCE /// ENTRY FOLJGA #type complete TITLE gag polyprotein - bovine leukemia virus (strain Australia) ALTERNATE_NAMES core polyprotein CONTAINS core protein p12; core protein p15; core protein p24 ORGANISM #formal_name bovine leukemia virus, BLV DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 28-Jul-2000 ACCESSIONS JQ0554 REFERENCE JQ0554 !$#authors Coulston, J.; Naif, H.; Brandon, R.; Kumar, S.; Khan, S.; !1Daniel, R.C.W.; Lavin, M.F. !$#journal J. Gen. Virol. (1990) 71:1737-1746 !$#title Molecular cloning and sequencing of an Australian isolate of !1proviral bovine leukaemia virus DNA: comparison with other !1isolates. !$#cross-references MUID:90362060; PMID:2167927 !$#accession JQ0554 !'##molecule_type DNA !'##residues 1-392 ##label COU !'##cross-references DDBJ:D00647; NID:g2920795; PIDN:BAA00543.1; !1PID:g221053 GENETICS !$#gene gag CLASSIFICATION #superfamily mammalian retrovirus gag polyprotein II KEYWORDS core protein; duplication; polyprotein; tandem repeat FEATURE !$1-109 #product core protein p15 #status predicted #label !8MAT\ !$110-323 #product core protein p24 #status predicted #label !8MAC\ !$324-392 #product core protein p12 #status predicted #label !8MAO\ !$342-362,367-387 #region 21-residue repeats SUMMARY #length 392 #molecular-weight 42766 #checksum 6587 SEQUENCE /// ENTRY FOLJGH #type complete TITLE probable gag polyprotein - human T-cell lymphotropic virus type 1 ORGANISM #formal_name human T-cell lymphotropic virus type 1, HTLV-1 #note host Homo sapiens (man) DATE 14-Nov-1983 #sequence_revision 27-Nov-1985 #text_change 26-Apr-1996 ACCESSIONS B93954; A91315; A03943 REFERENCE A93954 !$#authors Seiki, M.; Hattori, S.; Hirayama, Y.; Yoshida, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:3618-3622 !$#title Human adult T-cell leukemia virus: complete nucleotide !1sequence of the provirus genome integrated in leukemia cell !1DNA. !$#cross-references MUID:83221647; PMID:6304725 !$#accession B93954 !'##molecule_type DNA !'##residues 1-429 ##label SEI !'##experimental_source strain ATK REFERENCE A91315 !$#authors Copeland, T.D.; Oroszlan, S.; Kalyanaraman, V.S.; !1Sarngadharan, M.G.; Gallo, R.C. !$#journal FEBS Lett. (1983) 162:390-395 !$#title Complete amino acid sequence of human T-cell leukemia virus !1structural protein p15. !$#cross-references MUID:84029174; PMID:6313426 !$#accession A91315 !'##molecule_type protein !'##residues 345-415,'T',417-429 ##label COP COMMENT This protein is synthesized as a gag-pol polyprotein. GENETICS !$#gene gag CLASSIFICATION #superfamily mammalian retrovirus gag polyprotein II KEYWORDS core protein; polyprotein FEATURE !$1-344 #product gag polyprotein #status predicted #label !8GAG\ !$345-429 #product protein p15 #status experimental #label C15 SUMMARY #length 429 #molecular-weight 47496 #checksum 8481 SEQUENCE /// ENTRY FOLJCN #type complete TITLE gag polyprotein - human T-cell lymphotropic virus type 1 (isolate Caribbean) CONTAINS major core protein p19; major core protein p24; nucleic acid-binding protein p15 ORGANISM #formal_name human T-cell lymphotropic virus type 1, HTLV-1 #note host Homo sapiens (man) DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jun-2000 ACCESSIONS A28136 REFERENCE A92797 !$#authors Malik, K.T.A.; Even, J.; Karpas, A. !$#journal J. Gen. Virol. (1988) 69:1695-1710 !$#title Molecular cloning and complete nucleotide sequence of an !1adult T cell leukaemia virus/human T cell leukaemia virus !1type I (ATLV/HTLV-I) isolate of Caribbean origin: !1relationship to other members of the ATLV/HTLV-I subgroup. !$#cross-references MUID:88274338; PMID:2899128 !$#accession A28136 !'##molecule_type DNA !'##residues 1-429 ##label MAL !'##cross-references GB:D13784; GB:D00294; NID:g221866; PIDN:BAA02929.1; !1PID:g221867 GENETICS !$#gene gag CLASSIFICATION #superfamily mammalian retrovirus gag polyprotein II KEYWORDS core protein; polyprotein FEATURE !$1-130 #product major core protein p19 #status predicted !8#label P19\ !$131-344 #product major core protein p24 #status predicted !8#label P24\ !$345-429 #product nucleic acid-binding protein p15 #status !8predicted #label P15 SUMMARY #length 429 #molecular-weight 47514 #checksum 7728 SEQUENCE /// ENTRY FOLJH2 #type complete TITLE gag polyprotein - human T-cell lymphotropic virus type 2 ALTERNATE_NAMES core polyprotein CONTAINS core protein p12; core protein p15; core protein p24 ORGANISM #formal_name human T-cell lymphotropic virus type 2, HTLV-2 #note host Homo sapiens (man) DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 16-Jul-1999 ACCESSIONS A03944 REFERENCE A94042 !$#authors Shimotohno, K.; Takahashi, Y.; Shimizu, N.; Gojobori, T.; !1Golde, D.W.; Chen, I.S.Y.; Miwa, M.; Sugimura, T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:3101-3105 !$#title Complete nucleotide sequence of an infectious clone of human !1T-cell leukemia virus type II: an open reading frame for the !1protease gene. !$#cross-references MUID:85216449; PMID:2582407 !$#accession A03944 !'##molecule_type DNA !'##residues 1-433 ##label SHI !'##cross-references GB:M10060; NID:g329559; PIDN:AAB59884.1; !1PID:g329562 !'##note the authors translated the codon TAC for residues 197 and 249 !1as Thr GENETICS !$#gene gag CLASSIFICATION #superfamily mammalian retrovirus gag polyprotein II KEYWORDS core protein; polyprotein FEATURE !$1-136 #product core protein p15 #status predicted #label !8P15\ !$137-214 #product core protein p24 #status predicted #label !8P24\ !$215-433 #product core protein p12 #status predicted #label !8P12 SUMMARY #length 433 #molecular-weight 48028 #checksum 5219 SEQUENCE /// ENTRY FOVWH3 #type complete TITLE gag polyprotein - human immunodeficiency virus type 1 (isolate HTLV-III, BH10) ALTERNATE_NAMES core polyprotein CONTAINS core protein p15; core protein p17; core protein p24 ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 #note host Homo sapiens (man) DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 16-Jul-1999 ACCESSIONS A03945 REFERENCE A93353 !$#authors Ratner, L.; Haseltine, W.; Patarca, R.; Livak, K.J.; !1Starcich, B.; Josephs, S.F.; Doran, E.R.; Rafalski, J.A.; !1Whitehorn, E.A.; Baumeister, K.; Ivanoff, L.; Petteway Jr., !1S.R.; Pearson, M.L.; Lautenberger, J.A.; Papas, T.S.; !1Ghrayeb, J.; Chang, N.T.; Gallo, R.C.; Wong-Staal, F. !$#journal Nature (1985) 313:277-284 !$#title Complete nucleotide sequence of the AIDS virus, HTLV-III. !$#cross-references MUID:85111123; PMID:2578615 !$#accession A03945 !'##molecule_type DNA !'##residues 1-512 ##label RAT !'##cross-references GB:M15654; GB:K02008; GB:K02009; GB:K02010; !1NID:g326383; PIDN:AAA44201.1; PID:g326388 COMMENT Cleavage sites that yield the mature core proteins remain to !1be determined. GENETICS !$#gene gag CLASSIFICATION #superfamily AIDS-related virus gag polyprotein KEYWORDS AIDS; core protein; immunodeficiency; polyprotein FEATURE !$1-132 #product core protein p17 #status predicted #label !8P17\ !$133-391 #product core protein p24 #status predicted #label !8P24\ !$392-512 #product core protein p15 #status predicted #label !8P15 SUMMARY #length 512 #molecular-weight 57256 #checksum 2212 SEQUENCE /// ENTRY FOVWLV #type complete TITLE gag polyprotein - human immunodeficiency virus type 1 (isolate LAV-1a) ALTERNATE_NAMES assemblin; core polyprotein; gag precursor CONTAINS capsid antigen core protein p24CA; core protein p1; core protein p6; matrix antigen core protein p17MA; nucleocapsid core protein p7NC ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 #note host Homo sapiens (man) DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 05-Dec-1998 ACCESSIONS A03946 REFERENCE A90866 !$#authors Wain-Hobson, S.; Sonigo, P.; Danos, O.; Cole, S.; Alizon, M. !$#journal Cell (1985) 40:9-17 !$#title Nucleotide sequence of the AIDS virus, LAV. !$#cross-references MUID:85099333; PMID:2981635 !$#accession A03946 !'##molecule_type DNA !'##residues 1-500 ##label WAI GENETICS !$#gene gag CLASSIFICATION #superfamily AIDS-related virus gag polyprotein KEYWORDS AIDS; blocked amino end; core protein; immunodeficiency; !1lipoprotein; myristylation; nucleocapsid; phosphoprotein; !1polyprotein; zinc finger FEATURE !$2-500 #product gag precursor (assemblin) #status predicted !8#label GAG\ !$2-132 #product matrix antigen core protein p17MA #status !8predicted #label P17\ !$20-32 #region nuclear location signal\ !$110-114 #region nuclear location signal\ !$133-363 #product capsid antigen core protein p24CA #status !8predicted #label P24\ !$364-377 #product core protein p2 #status predicted #label !8CP2\ !$378-432 #product nucleocapsid core protein p7NC #status !8predicted #label CP7\ !$392-405 #region zinc finger CCHC motif\ !$413-426 #region zinc finger CCHC motif\ !$433-448 #product core protein p1 #status predicted #label !8CP1\ !$449-500 #product core protein p6 #status predicted #label !8CP6\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$392,395,400,405 #binding_site zinc (Cys, Cys, His, Cys) #status !8experimental\ !$413,416,421,426 #binding_site zinc (Cys, Cys, His, Cys) #status !8experimental SUMMARY #length 500 #molecular-weight 55905 #checksum 4968 SEQUENCE /// ENTRY A44001 #type complete TITLE gag polyprotein - human immunodeficiency virus type 1 (strain YU-2) ALTERNATE_NAMES core polyprotein CONTAINS core protein p15; core protein p17; core protein p24 ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 #note host Homo sapiens (man) DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 31-Jan-1997 ACCESSIONS A44001 REFERENCE A44001 !$#authors Li, Y.; Hui, H.; Burgess, C.J.; Price, R.W.; Sharp, P.M.; !1Hahn, B.H.; Shaw, G.M. !$#journal J. Virol. (1992) 66:6587-6600 !$#title Complete nucleotide sequence, genome organization, and !1biological properties of human immunodeficiency virus type 1 !1in vivo: evidence for limited defectiveness and !1complementation. !$#cross-references MUID:93021387; PMID:1404605 !$#accession A44001 !'##molecule_type DNA !'##residues 1-500 ##label LIY !'##cross-references GB:M93258 GENETICS !$#gene gag CLASSIFICATION #superfamily AIDS-related virus gag polyprotein KEYWORDS AIDS; core protein; immunodeficiency; polyprotein FEATURE !$1-132 #product core protein p17 #status predicted #label !8P17\ !$133-391 #product core protein p24 #status predicted #label !8P24\ !$392-500 #product core protein p15 #status predicted #label !8P15 SUMMARY #length 500 #molecular-weight 55791 #checksum 3889 SEQUENCE /// ENTRY FOLJND #type complete TITLE gag polyprotein - human immunodeficiency virus type 1 (isolate NDK) ALTERNATE_NAMES core polyprotein CONTAINS core protein p15; core protein p17; core protein p24 ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 #note host Homo sapiens (man) DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jul-1999 ACCESSIONS JQ0065 REFERENCE JQ0065 !$#authors Spire, B.; Sire, J.; Zachar, V.; Rey, F.; Barre-Sinoussi, !1F.; Galibert, F.; Hampe, A.; Chermann, J.C. !$#journal Gene (1989) 81:275-284 !$#title Nucleotide sequence of HIV1-NDK: a highly cytopathic strain !1of the human immunodeficiency virus. !$#cross-references MUID:90034200; PMID:2806917 !$#accession JQ0065 !'##molecule_type DNA !'##residues 1-497 ##label SPI !'##cross-references GB:M27323; NID:g328154; PIDN:AAA44868.1; !1PID:g328157 GENETICS !$#gene gag CLASSIFICATION #superfamily AIDS-related virus gag polyprotein KEYWORDS AIDS; core protein; immunodeficiency; polyprotein FEATURE !$1-129 #product core protein p17 #status predicted #label !8C17\ !$130-389 #product core protein p24 #status predicted #label !8C24\ !$390-497 #product core protein p15 #status predicted #label !8C15 SUMMARY #length 497 #molecular-weight 55283 #checksum 2121 SEQUENCE /// ENTRY FOVWH4 #type complete TITLE gag polyprotein - human immunodeficiency virus type 1 (isolate CDC-451) ALTERNATE_NAMES core polyprotein CONTAINS core protein p15; core protein p17; core protein p24 ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 16-Jul-1999 ACCESSIONS A25523 REFERENCE A94136 !$#authors Desai, S.M.; Kalyanaraman, V.S.; Casey, J.M.; Srinivasan, !1A.; Andersen, P.R.; Devare, S.G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:8380-8384 !$#title Molecular cloning and primary nucleotide sequence analysis !1of a distinct human immunodeficiency virus isolate reveal !1significant divergence in its genomic sequences. !$#cross-references MUID:87041461; PMID:3490666 !$#accession A25523 !'##molecule_type DNA !'##residues 1-500 ##label DES !'##cross-references GB:M13136; NID:g326459; PIDN:AAA44306.1; !1PID:g326462 GENETICS !$#gene gag CLASSIFICATION #superfamily AIDS-related virus gag polyprotein KEYWORDS core protein; polyprotein FEATURE !$1-132 #product core protein p17 #status predicted #label !8P17\ !$133-391 #product core protein p24 #status predicted #label !8P24\ !$392-500 #product core protein p15 #status predicted #label !8P15 SUMMARY #length 500 #molecular-weight 55928 #checksum 4337 SEQUENCE /// ENTRY FOVWA2 #type complete TITLE gag polyprotein - human immunodeficiency virus type 1 (isolate ARV-2) ALTERNATE_NAMES core polyprotein CONTAINS core protein p15; core protein p17; core protein p24 ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 #note host Homo sapiens (man) DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 16-Jul-1999 ACCESSIONS A03947 REFERENCE A04003 !$#authors Sanchez-Pescador, R.; Power, M.D.; Barr, P.J.; Steimer, !1K.S.; Stempien, M.M.; Brown-Shimer, S.L.; Gee, W.W.; Renard, !1A.; Randolph, A.; Levy, J.A.; Dina, D.; Luciw, P.A. !$#journal Science (1985) 227:484-492 !$#title Nucleotide sequence and expression of an AIDS-associated !1retrovirus (ARV-2). !$#cross-references MUID:85090453; PMID:2578227 !$#accession A03947 !'##molecule_type DNA !'##residues 1-502 ##label SAN !'##cross-references GB:K02007; NID:g328658; PIDN:AAB59875.1; !1PID:g328661 COMMENT Cleavage sites that yield the mature core proteins remain to !1be determined. GENETICS !$#gene gag CLASSIFICATION #superfamily AIDS-related virus gag polyprotein KEYWORDS AIDS; core protein; immunodeficiency; polyprotein FEATURE !$1-134 #product core protein p17 #status predicted #label !8P17\ !$135-393 #product core protein p24 #status predicted #label !8P24\ !$394-502 #product core protein p15 #status predicted #label !8P15 SUMMARY #length 502 #molecular-weight 56066 #checksum 2771 SEQUENCE /// ENTRY FOVWVL #type complete TITLE gag polyprotein - human immunodeficiency virus type 1 (isolate LV) ALTERNATE_NAMES assemblin; core polyprotein; gag precursor CONTAINS capsid antigen core protein p24CA; core protein p1; core protein p6; matrix antigen core protein p17MA; nucleocapsid core protein p7NC ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 05-Dec-1998 ACCESSIONS A03948 REFERENCE A93355 !$#authors Muesing, M.A.; Smith, D.H.; Cabradilla, C.D.; Benton, C.V.; !1Lasky, L.A.; Capon, D.J. !$#journal Nature (1985) 313:450-458 !$#title Nucleic acid structure and expression of the human AIDS/ !1lymphadenopathy retrovirus. !$#cross-references MUID:85111157; PMID:2982104 !$#accession A03948 !'##molecule_type DNA !'##residues 1-478 ##label MUE GENETICS !$#gene gag CLASSIFICATION #superfamily AIDS-related virus gag polyprotein KEYWORDS AIDS; blocked amino end; core protein; immunodeficiency; !1lipoprotein; myristylation; nucleocapsid; phosphoprotein; !1polyprotein; zinc finger FEATURE !$2-478 #product gag precursor (assemblin) #status predicted !8#label GAG\ !$2-132 #product matrix antigen core protein p17MA #status !8predicted #label P17\ !$20-32 #region nuclear location signal\ !$110-114 #region nuclear location signal\ !$133-363 #product capsid antigen core protein p24CA #status !8predicted #label P24\ !$364-377 #product core protein p2 #status predicted #label !8CP2\ !$378-432 #product nucleocapsid core protein p7NC #status !8predicted #label CP7\ !$392-405 #region zinc finger CCHC motif\ !$413-426 #region zinc finger CCHC motif\ !$2 #modified_site myristylated amino end (Gly) (in !8mature form) #status predicted\ !$392,395,400,405 #binding_site zinc (Cys, Cys, His, Cys) #status !8experimental\ !$413,416,421,426 #binding_site zinc (Cys, Cys, His, Cys) #status !8experimental SUMMARY #length 478 #molecular-weight 53553 #checksum 4245 SEQUENCE /// ENTRY A38068 #type complete TITLE gag polyprotein - human immunodeficiency virus type 1 (strain MN) ALTERNATE_NAMES core polyprotein CONTAINS core protein p1; core protein p17; core protein p2; core protein p24; core protein p6; core protein p7 ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 #note host Homo sapiens (man) DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 26-Feb-1999 ACCESSIONS A38068 REFERENCE A38068 !$#authors Henderson, L.E.; Bowers, M.A.; Sowder II, R.C.; Serabyn, !1S.A.; Johnson, D.G.; Bess Jr., J.W.; Arthur, L.O.; Bryant, !1D.K.; Fenselau, C. !$#journal J. Virol. (1992) 66:1856-1865 !$#title Gag proteins of the highly replicative MN strain of human !1immunodeficiency virus type 1: posttranslational !1modifications, proteolytic processings, and complete amino !1acid sequences. !$#cross-references MUID:92194415; PMID:1548743 !$#accession A38068 !'##molecule_type protein !'##residues 1-506 ##label HEN GENETICS !$#gene gag CLASSIFICATION #superfamily AIDS-related virus gag polyprotein KEYWORDS AIDS; core protein; immunodeficiency; polyprotein FEATURE !$1-134 #product core protein p17 #status experimental #label !8P17\ !$135-365 #product core protein p24 #status experimental #label !8P24\ !$366-379 #product core protein p2 #status experimental #label !8PP2\ !$380-434 #product core protein p7 #status experimental #label !8PP7\ !$435-450 #product core protein p1 #status experimental #label !8PP1\ !$451-506 #product core protein p6 #status experimental #label !8PP6 SUMMARY #length 506 #molecular-weight 56629 #checksum 2740 SEQUENCE /// ENTRY FOLJSI #type complete TITLE gag polyprotein - simian immunodeficiency virus SIVcpz ALTERNATE_NAMES core polyprotein ORGANISM #formal_name simian immunodeficiency virus SIVcpz #note host Pan troglodytes (chimpanzee) DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jul-1999 ACCESSIONS S09983 REFERENCE S09983 !$#authors Huet, T.; Cheynier, R.; Meyerhans, A.; Roelants, G.; !1Wain-Hobson, S. !$#journal Nature (1990) 345:356-359 !$#title Genetic organization of a chimpanzee lentivirus related to !1HIV-1. !$#cross-references MUID:90259077; PMID:2188136 !$#accession S09983 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-508 ##label HUE !'##cross-references EMBL:X52154; NID:g58866; PIDN:CAA36401.1; !1PID:g58867 GENETICS !$#gene gag CLASSIFICATION #superfamily AIDS-related virus gag polyprotein KEYWORDS AIDS; core protein; immunodeficiency; polyprotein SUMMARY #length 508 #molecular-weight 55962 #checksum 5802 SEQUENCE /// ENTRY FOLJG2 #type complete TITLE gag polyprotein - human immunodeficiency virus type 2 (isolate ROD) ALTERNATE_NAMES core polyprotein CONTAINS core protein p16; core protein p26 ORGANISM #formal_name human immunodeficiency virus type 2, HIV-2 DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Jul-1999 ACCESSIONS A26262 REFERENCE A26262 !$#authors Guyader, M.; Emerman, M.; Sonigo, P.; Clavel, F.; !1Montagnier, L.; Alizon, M. !$#journal Nature (1987) 326:662-669 !$#title Genome organization and transactivation of the human !1immuno-deficiency virus type 2. !$#cross-references MUID:87173056; PMID:3031510 !$#accession A26262 !'##molecule_type DNA !'##residues 1-522 ##label GUY !'##cross-references GB:M15390; NID:g1332361; PIDN:AAB00763.1; !1PID:g325745 GENETICS !$#gene gag CLASSIFICATION #superfamily AIDS-related virus gag polyprotein KEYWORDS AIDS; core protein; immunodeficiency; polyprotein FEATURE !$1-135 #product core protein p16 #status predicted #label !8P16\ !$136-522 #product core protein p26 #status predicted #label !8P26 SUMMARY #length 522 #molecular-weight 58374 #checksum 5389 SEQUENCE /// ENTRY FOLJST #type complete TITLE gag polyprotein - human immunodeficiency virus type 2 (isolate ST) ALTERNATE_NAMES core polyprotein CONTAINS core protein p16; core protein p26 ORGANISM #formal_name human immunodeficiency virus type 2, HIV-2 #note host Homo sapiens (man) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS A33943 REFERENCE A33943 !$#authors Kumar, P.; Hui, H.; Kappes, J.C.; Haggarty, B.S.; Hoxie, !1J.A.; Arya, S.K.; Shaw, G.M.; Hahn, B.H. !$#journal J. Virol. (1990) 64:890-901 !$#title Molecular characterization of an attenuated human !1immunodeficiency virus type 2 isolate. !$#cross-references MUID:90112662; PMID:2296086 !$#accession A33943 !'##molecule_type genomic RNA !'##residues 1-521 ##label KUM !'##cross-references GB:M31113; NID:g1339798; PIDN:AAB01351.1; !1PID:g325755 GENETICS !$#gene gag CLASSIFICATION #superfamily AIDS-related virus gag polyprotein KEYWORDS core protein; polyprotein FEATURE !$1-135 #product core protein p16 #status predicted #label !8CP1\ !$136-521 #product core protein p26 #status predicted #label !8CP2 SUMMARY #length 521 #molecular-weight 58302 #checksum 1265 SEQUENCE /// ENTRY FOLJCA #type complete TITLE gag polyprotein - human immunodeficiency virus type 2 (isolate CAM2/Guinea-Bissau) ALTERNATE_NAMES core polyprotein CONTAINS core protein p16; core protein p26 ORGANISM #formal_name human immunodeficiency virus type 2, HIV-2 #note host Homo sapiens (man) DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jun-2000 ACCESSIONS A38475; JQ0973 REFERENCE A38475 !$#authors Tristem, M.; Hill, F.; Karpas, A. !$#journal J. Gen. Virol. (1991) 72:721-724 !$#title Nucleotide sequence of a Guinea-Bissau-derived human !1immunodeficiency virus type 2 proviral clone (HIV-2-CAM2). !$#cross-references MUID:91170959; PMID:2005437 !$#accession A38475 !'##molecule_type DNA !'##residues 1-521 ##label TRI !'##cross-references GB:D00835; NID:g3153166; PIDN:BAA00709.1; !1PID:g221468 GENETICS !$#gene gag CLASSIFICATION #superfamily AIDS-related virus gag polyprotein KEYWORDS AIDS; core protein; immunodeficiency; polyprotein FEATURE !$1-135 #product core protein p16 #status predicted #label !8P16\ !$136-521 #product core protein p26 #status predicted #label !8P26 SUMMARY #length 521 #molecular-weight 58022 #checksum 328 SEQUENCE /// ENTRY FOLJG3 #type complete TITLE gag polyprotein - simian immunodeficiency virus (macaque isolate) ORGANISM #formal_name simian immunodeficiency virus, SIV DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jul-1999 ACCESSIONS A28887 REFERENCE A28887 !$#authors Chakrabarti, L.; Guyader, M.; Alizon, M.; Daniel, M.D.; !1Desrosiers, R.C.; Tiollais, P.; Sonigo, P. !$#journal Nature (1987) 328:543-547 !$#title Sequence of simian immunodeficiency virus from macaque and !1its relationship to other human and simian retroviruses. !$#cross-references MUID:87287230; PMID:3649576 !$#accession A28887 !'##molecule_type DNA !'##residues 1-506 ##label CHA !'##cross-references GB:Y00277; GB:M16403; NID:g61730; PIDN:CAA68379.1; !1PID:g61731 GENETICS !$#gene gag CLASSIFICATION #superfamily AIDS-related virus gag polyprotein KEYWORDS core protein; polyprotein SUMMARY #length 506 #molecular-weight 56436 #checksum 1358 SEQUENCE /// ENTRY FOLJG5 #type complete TITLE gag polyprotein - simian immunodeficiency virus (African green monkey isolate) CONTAINS core protein p17; core protein p24 ORGANISM #formal_name simian immunodeficiency virus, SIV DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 24-Oct-1997 ACCESSIONS A28873 REFERENCE A28873 !$#authors Franchini, G.; Gurgo, C.; Guo, H.G.; Gallo, R.C.; Collalti, !1E.; Fargnoli, K.A.; Hall, L.F.; Wong-Staal, F.; Reitz Jr., !1M.S. !$#journal Nature (1987) 328:539-543 !$#title Sequence of simian immunodeficiency virus and its !1relationship to the human immunodeficiency viruses. !$#cross-references MUID:87287229; PMID:3497350 !$#accession A28873 !'##molecule_type DNA !'##residues 1-506 ##label FRA !'##cross-references EMBL:M19499 GENETICS !$#gene gag CLASSIFICATION #superfamily AIDS-related virus gag polyprotein KEYWORDS core protein; polyprotein FEATURE !$1-115 #product core protein p17 #status predicted #label !8P17\ !$116-506 #product core protein p24 #status predicted #label !8P24 SUMMARY #length 506 #molecular-weight 56725 #checksum 3469 SEQUENCE /// ENTRY FOLJTM #type complete TITLE gag polyprotein - simian immunodeficiency virus (strain stm) ALTERNATE_NAMES core polyprotein CONTAINS core protein p17; core protein p24 ORGANISM #formal_name simian immunodeficiency virus, SIV #note host Macaca arctoides (stump-tailed macaque) DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS A41565 REFERENCE A41565 !$#authors Khan, A.S.; Galvin, T.A.; Lowenstine, L.J.; Jennings, M.B.; !1Gardner, M.B.; Buckler, C.E. !$#journal J. Virol. (1991) 65:7061-7065 !$#title A highly divergent simian immunodeficiency virus (SIVstm) !1recovered from stored stump-tailed macaque tissues. !$#cross-references MUID:92046379; PMID:1942258 !$#accession A41565 !'##molecule_type DNA !'##residues 1-510 ##label KHA !'##cross-references GB:X60667; NID:g60527; PIDN:CAA43084.1; PID:g60528 GENETICS !$#gene gag CLASSIFICATION #superfamily AIDS-related virus gag polyprotein KEYWORDS core protein; polyprotein FEATURE !$1-115 #product core protein p17 #status predicted #label !8P17\ !$116-510 #product core protein p24 #status predicted #label !8P24 SUMMARY #length 510 #molecular-weight 56523 #checksum 1858 SEQUENCE /// ENTRY FOLJGG #type complete TITLE gag polyprotein - human immunodeficiency virus type 2 (isolate GH-1) ALTERNATE_NAMES core polyprotein ORGANISM #formal_name human immunodeficiency virus type 2, HIV-2 #note host Homo sapiens (man) DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jul-1999 ACCESSIONS JS0327 REFERENCE JS0327 !$#authors Hasegawa, A.; Tsujimoto, H.; Maki, N.; Ishikawa, K.; Miura, !1T.; Fukasawa, M.; Miki, K.; Hayami, M. !$#journal AIDS Res. Hum. Retroviruses (1989) 5:593-604 !$#title Sequence of a distinct HIV-2 isolate from Ghana showing !1significant divergence in its genome. !$#cross-references MUID:90122350; PMID:2611042 !$#accession JS0327 !'##molecule_type DNA !'##residues 1-522 ##label HAS !'##cross-references GB:M30895; GB:D00477; NID:g325709; PIDN:AAA43932.1; !1PID:g325713 !'##note this sequence was submitted to JIPID, October 1989 COMMENT Cleavage sites that yield the mature core proteins remain to !1be determined. GENETICS !$#gene gag CLASSIFICATION #superfamily AIDS-related virus gag polyprotein KEYWORDS AIDS; core protein; polyprotein SUMMARY #length 522 #molecular-weight 58206 #checksum 9538 SEQUENCE /// ENTRY FOLJG4 #type complete TITLE gag polyprotein - simian immunodeficiency virus (African green monkey isolate) ORGANISM #formal_name simian immunodeficiency virus, SIV DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 28-Jul-2000 ACCESSIONS A30045 REFERENCE A30045 !$#authors Fukasawa, M.; Miura, T.; Hasegawa, A.; Morikawa, S.; !1Tsujimoto, H.; Miki, K.; Kitamura, T.; Hayami, M. !$#journal Nature (1988) 333:457-461 !$#title Sequence of simian immunodeficiency virus from African green !1monkey, a new member of the HIV/SIV group. !$#cross-references MUID:88232906; PMID:3374586 !$#accession A30045 !'##molecule_type DNA !'##residues 1-519 ##label FUK !'##cross-references EMBL:X07805; NID:g61748; PIDN:CAA30657.1; !1PID:g4469305 GENETICS !$#gene gag CLASSIFICATION #superfamily AIDS-related virus gag polyprotein KEYWORDS core protein; polyprotein SUMMARY #length 519 #molecular-weight 58143 #checksum 4687 SEQUENCE /// ENTRY FOLJEV #type complete TITLE gag polyprotein - equine infectious anemia virus ALTERNATE_NAMES core polyprotein CONTAINS core protein 9; core protein p11; core protein p15; core protein p26 ORGANISM #formal_name equine infectious anemia virus #note host Equus caballus (domestic horse) DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 16-Jul-1999 ACCESSIONS A03949; A27842; A41991 REFERENCE A03949 !$#authors Stephens, R.M.; Casey, J.W.; Rice, N.R. !$#journal Science (1986) 231:589-594 !$#title Equine infectious anemia virus gag and pol genes: !1relatedness to visna and AIDS virus. !$#cross-references MUID:86122873; PMID:3003905 !$#accession A03949 !'##molecule_type DNA !'##residues 1-486 ##label STE !'##cross-references GB:M16575; GB:K03334; GB:M11337; GB:M14855; !1NID:g323836; PIDN:AAB59861.1; PID:g323837 REFERENCE A27842 !$#authors Kawakami, T.; Sherman, L.; Dahlberg, J.; Gazit, A.; Yaniv, !1A.; Tronick, S.R.; Aaronson, S.A. !$#journal Virology (1987) 158:300-312 !$#title Nucleotide sequence analysis of equine infectious anemia !1virus proviral DNA. !$#cross-references MUID:87236196; PMID:3035786 !$#accession A27842 !'##molecule_type DNA !'##residues 1-486 ##label KAW !'##cross-references GB:M16575; GB:K03334; GB:M11337; GB:M14855; !1NID:g323836; PIDN:AAB59861.1; PID:g323837 !'##experimental_source clone 1369 REFERENCE A41991 !$#authors Perry, S.T.; Flaherty, M.T.; Kelley, M.J.; Clabough, D.L.; !1Tronick, S.R.; Coggins, L.; Whetter, L.; Lengel, C.R.; !1Fuller, F. !$#journal J. Virol. (1992) 66:4085-4097 !$#title The surface envelope protein gene region of equine !1infectious anemia virus is not an important determinant of !1tropism in vitro. !$#cross-references MUID:92292230; PMID:1318398 !$#accession A41991 !'##molecule_type DNA !'##residues 1-486 ##label PER !'##cross-references GB:M87581; NID:g290627; PIDN:AAA43003.1; !1PID:g290628 !'##experimental_source strain CL22 GENETICS !$#gene gag CLASSIFICATION #superfamily AIDS-related virus gag polyprotein KEYWORDS core protein; polyprotein FEATURE !$1-124 #product core protein p15 #status predicted #label !8P15\ !$125-359 #product core protein p26 #status predicted #label !8P26\ !$360-435 #product core protein p11 #status predicted #label !8P11\ !$436-486 #product core protein p9 #status predicted #label P09 SUMMARY #length 486 #molecular-weight 54808 #checksum 3630 SEQUENCE /// ENTRY FOLJVS #type complete TITLE gag polyprotein - Maedi/Visna virus (strain 1514) ALTERNATE_NAMES core polyprotein CONTAINS core protein p14; core protein p16; core protein p25 ORGANISM #formal_name Maedi/Visna virus #note host Homo sapiens (man) DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 12-Apr-1996 ACCESSIONS A03950 REFERENCE A90869 !$#authors Sonigo, P.; Alizon, M.; Staskus, K.; Klatzmann, D.; Cole, !1S.; Danos, O.; Retzel, E.; Tiollais, P.; Haase, A.; !1Wain-Hobson, S. !$#journal Cell (1985) 42:369-382 !$#title Nucleotide sequence of the visna lentivirus: relationship to !1the AIDS virus. !$#cross-references MUID:85254938; PMID:2410140 !$#accession A03950 !'##molecule_type DNA !'##residues 1-442 ##label SON GENETICS !$#gene gag CLASSIFICATION #superfamily AIDS-related virus gag polyprotein KEYWORDS core protein; polyprotein FEATURE !$1-143 #product core protein p16 #status predicted #label !8P16\ !$144-363 #product core protein p25 #status predicted #label !8P25\ !$364-442 #product core protein p14 #status predicted #label !8P14 SUMMARY #length 442 #molecular-weight 49865 #checksum 6968 SEQUENCE /// ENTRY A45390 #type complete TITLE gag polyprotein - Maedi/Visna virus (strain KV1772) (provirus) ALTERNATE_NAMES core polyprotein CONTAINS core protein p14; core protein p16; core protein p25 ORGANISM #formal_name Maedi/Visna virus #note host Homo sapiens (man) DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS A45390 REFERENCE A45390 !$#authors Andresson, O.S.; Elser, J.E.; Tobin, G.J.; Greenwood, J.D.; !1Gonda, M.A.; Georgsson, G.; Andresdottir, V.; !1Benediktsdottir, E.; Carlsdottir, H.M.; Maentylae, E.O.; !1Rafnar, B.; Palsson, P.A.; Casey, J.W.; Petursson, G. !$#journal Virology (1993) 193:89-105 !$#title Nucleotide sequence and biological properties of a !1pathogenic proviral molecular clone of neurovirulent visna !1virus. !$#cross-references MUID:93174981; PMID:8382414 !$#accession A45390 !'##molecule_type DNA !'##residues 1-442 ##label AND !'##cross-references GB:S55323; NID:g265825; PIDN:AAB25459.1; !1PID:g265826 GENETICS !$#gene gag CLASSIFICATION #superfamily AIDS-related virus gag polyprotein KEYWORDS core protein; polyprotein FEATURE !$1-143 #product core protein p16 #status predicted #label !8P16\ !$144-363 #product core protein p25 #status predicted #label !8P25\ !$364-442 #product core protein p14 #status predicted #label !8P14 SUMMARY #length 442 #molecular-weight 49856 #checksum 7310 SEQUENCE /// ENTRY A46335 #type complete TITLE gag polyprotein - Maedi/Visna-related virus SA-OMVV ALTERNATE_NAMES core polyprotein CONTAINS core protein p14; core protein p16; core protein p25 ORGANISM #formal_name Maedi/Visna-related virus SA-OMVV DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS A46335 REFERENCE A46335 !$#authors Querat, G.; Audoly, G.; Sonigo, P.; Vigne, R. !$#journal Virology (1990) 175:434-447 !$#title Nucleotide sequence analysis of SA-OMVV, a visna-related !1ovine lentivirus: phylogenetic history of lentiviruses. !$#cross-references MUID:90223989; PMID:2158181 !$#accession A46335 !'##molecule_type DNA !'##residues 1-446 ##label QUE !'##cross-references GB:M31646; NID:g808756; PIDN:AAA66811.1; !1PID:g332548 GENETICS !$#gene gag CLASSIFICATION #superfamily AIDS-related virus gag polyprotein KEYWORDS core protein; polyprotein FEATURE !$1-143 #product core protein p16 #status predicted #label !8P16\ !$144-363 #product core protein p25 #status predicted #label !8P25\ !$364-442 #product core protein p14 #status predicted #label !8P14 SUMMARY #length 446 #molecular-weight 50550 #checksum 3444 SEQUENCE /// ENTRY A45345 #type complete TITLE gag polyprotein - caprine arthritis-encephalitis virus (strain CO) ALTERNATE_NAMES core polyprotein CONTAINS core protein p14; core protein p16; core protein p25 ORGANISM #formal_name caprine arthritis-encephalitis virus, CAEV DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 26-Feb-1999 ACCESSIONS A45345 REFERENCE A45345 !$#authors Saltarelli, M.; Querat, G.; Konings, D.A.M.; Vigne, R.; !1Clements, J.E. !$#journal Virology (1990) 179:347-364 !$#title Nucleotide sequence and transcriptional analysis of !1molecular clones of CAEV which generate infectious virus. !$#cross-references MUID:91021037; PMID:2171210 !$#accession A45345 !'##molecule_type mRNA !'##residues 1-441 ##label SAL !'##cross-references GB:M33677 GENETICS !$#gene gag CLASSIFICATION #superfamily AIDS-related virus gag polyprotein KEYWORDS core protein; polyprotein FEATURE !$1-146 #product core protein p16 #status predicted #label !8P16\ !$147-358 #product core protein p25 #status predicted #label !8P25\ !$359-441 #product core protein p14 #status predicted #label !8P14 SUMMARY #length 441 #molecular-weight 49909 #checksum 8625 SEQUENCE /// ENTRY FOLJFP #type complete TITLE gag polyprotein - feline immunodeficiency virus (strain Petaluma) ALTERNATE_NAMES core polyprotein CONTAINS core protein p10; core protein p15; core protein p24 ORGANISM #formal_name feline immunodeficiency virus #note host Felis silvestris catus (domestic cat) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 12-Apr-1996 ACCESSIONS A33543 REFERENCE A33543 !$#authors Talbott, R.L.; Sparger, E.E.; Lovelace, K.M.; Fitch, W.M.; !1Pedersen, N.C.; Luciw, P.A.; Elder, J.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:5743-5747 !$#title Nucleotide sequence and genomic organization of feline !1immunodeficiency virus. !$#cross-references MUID:89345543; PMID:2762293 !$#accession A33543 !'##molecule_type DNA !'##residues 1-450 ##label TAL GENETICS !$#gene gag CLASSIFICATION #superfamily AIDS-related virus gag polyprotein KEYWORDS core protein; polyprotein FEATURE !$1-135 #product core protein p15 #status predicted #label !8P15\ !$136-358 #product core protein p24 #status predicted #label !8P24\ !$363-450 #product core protein p10 #status predicted #label !8P10 SUMMARY #length 450 #molecular-weight 49243 #checksum 3531 SEQUENCE /// ENTRY FOLJSA #type complete TITLE gag polyprotein - simian AIDS retrovirus SRV-1 ALTERNATE_NAMES core polyprotein CONTAINS core phosphoprotein p18; core protein p10; core protein p12; core protein p14; core protein p27; core protein p4 ORGANISM #formal_name simian AIDS retrovirus SRV-1 #note host Macaca mulatta (rhesus macaque) DATE 13-Aug-1986 #sequence_revision 13-Aug-1986 #text_change 16-Jul-1999 ACCESSIONS A03951 REFERENCE A94711 !$#authors Power, M.D.; Marx, P.A.; Bryant, M.L.; Gardner, M.B.; Barr, !1P.J.; Luciw, P.A. !$#journal Science (1986) 231:1567-1572 !$#title Nucleotide sequence of SRV-1, a type D simian acquired !1immune deficiency syndrome retrovirus. !$#cross-references MUID:86151668; PMID:3006247 !$#accession A03951 !'##molecule_type DNA !'##residues 1-658 ##label POW !'##cross-references GB:M11841; NID:g334746; PIDN:AAA47730.1; !1PID:g334747 GENETICS !$#gene gag CLASSIFICATION #superfamily AIDS-related virus gag polyprotein KEYWORDS AIDS; core protein; immunodeficiency; phosphoprotein; !1polyprotein FEATURE !$1-162 #product core protein p10 #status predicted #label !8P10\ !$163-217 #product core phosphoprotein p18 #status predicted !8#label P18\ !$218-300 #product core protein p12 #status predicted #label !8P12\ !$301-526 #product core protein p27 #status predicted #label !8P27\ !$527-622 #product core protein p14 #status predicted #label !8P14\ !$623-658 #product core protein p4 #status predicted #label P04 SUMMARY #length 658 #molecular-weight 73195 #checksum 9732 SEQUENCE /// ENTRY FOLJMP #type complete TITLE gag polyprotein - Mason-Pfizer monkey virus CONTAINS probable core protein p10; probable core protein p12; probable core protein p14; probable core protein p27; probable core protein p4; probable core protein pp24 ORGANISM #formal_name Mason-Pfizer monkey virus DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 16-Jul-1999 ACCESSIONS A25839 REFERENCE A90878 !$#authors Sonigo, P.; Barker, C.; Hunter, E.; Wain-Hobson, S. !$#journal Cell (1986) 45:375-385 !$#title Nucleotide sequence of Mason-Pfizer monkey virus: an !1immunosuppressive D-type retrovirus. !$#cross-references MUID:86189951; PMID:2421920 !$#accession A25839 !'##molecule_type DNA !'##residues 1-657 ##label SON !'##cross-references GB:M12349; NID:g334702; PIDN:AAA47710.1; !1PID:g334703 !'##experimental_source clone 6A GENETICS !$#gene gag CLASSIFICATION #superfamily AIDS-related virus gag polyprotein KEYWORDS core protein; polyprotein FEATURE !$1-100 #product core protein p10 #status predicted #label !8P10\ !$101-216 #product core protein pp24 #status predicted #label !8PP2\ !$217-299 #product core protein p12 #status predicted #label !8P12\ !$300-526 #product core protein p27 #status predicted #label !8P27\ !$527-621 #product core protein p14 #status predicted #label !8P14\ !$622-657 #product core protein p4 #status predicted #label PP4 SUMMARY #length 657 #molecular-weight 73110 #checksum 5259 SEQUENCE /// ENTRY FOMVJA #type complete TITLE gag polyprotein - sheep pulmonary adenomatosis virus ALTERNATE_NAMES core polyprotein CONTAINS core protein p10; core protein p12; core protein p14; core protein p18; core protein p27; core protein p4 ORGANISM #formal_name sheep pulmonary adenomatosis virus DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS A42740 REFERENCE A42740 !$#authors York, D.F.; Vigne, R.; Verwoerd, D.W.; Querat, G. !$#journal J. Virol. (1992) 66:4930-4939 !$#title Nucleotide sequence of the jaagsiekte retrovirus, an !1exogenous and endogenous type D and B retrovirus of sheep !1and goats. !$#cross-references MUID:92333675; PMID:1629959 !$#accession A42740 !'##molecule_type genomic RNA !'##residues 1-612 ##label YOR !'##cross-references GB:M80216; NID:g331338; PIDN:AAA89180.1; !1PID:g331339 GENETICS !$#gene gag CLASSIFICATION #superfamily AIDS-related virus gag polyprotein KEYWORDS core protein; polyprotein FEATURE !$1-147 #product core protein p10 #status predicted #label !8CP1\ !$148-167 #product core protein p18 #status predicted #label !8CP2\ !$168-256 #product core protein p12 #status predicted #label !8CP3\ !$257-476 #product core protein p27 #status predicted #label !8CP4\ !$477-579 #product core protein p14 #status predicted #label !8CP5\ !$580-612 #product core protein p4 #status predicted #label CP6 SUMMARY #length 612 #molecular-weight 68089 #checksum 7454 SEQUENCE /// ENTRY FOLJHD #type complete TITLE gag polyprotein - squirrel monkey retrovirus SMRV-H CONTAINS core protein p16; core protein p19; probable core protein p10; probable core protein p35 ORGANISM #formal_name squirrel monkey retrovirus SMRV-H DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS A31827 REFERENCE A31827 !$#authors Oda, T.; Ikeda, S.; Watanabe, S.; Hatsushika, M.; Akiyama, !1K.; Mitsunobu, F. !$#journal Virology (1988) 167:468-476 !$#title Molecular cloning, complete nucleotide sequence, and gene !1structure of the provirus genome of a retrovirus produced in !1a human lymphoblastoid cell line. !$#cross-references MUID:89073750; PMID:3201749 !$#accession A31827 !'##molecule_type DNA !'##residues 1-740 ##label ODA !'##cross-references GB:M23385; NID:g332626; PIDN:AAA66451.1; !1PID:g807672 GENETICS !$#gene gag CLASSIFICATION #superfamily AIDS-related virus gag polyprotein KEYWORDS core protein; polyprotein FEATURE !$1-163 #product core protein p19 #status predicted #label !8CP9\ !$164-318 #product core protein p16 #status predicted #label !8CP6\ !$319-648 #product core protein p35 #status predicted #label !8CP5\ !$649-740 #product core protein p10 #status predicted #label !8CP1 SUMMARY #length 740 #molecular-weight 80543 #checksum 6052 SEQUENCE /// ENTRY FOLJBT #type complete TITLE gag polyprotein - bovine immunodeficiency virus (isolate 127) ALTERNATE_NAMES core polyprotein ORGANISM #formal_name bovine immunodeficiency virus DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jul-1999 ACCESSIONS A34742 REFERENCE A34742 !$#authors Garvey, K.J.; Oberste, M.S.; Elser, J.E.; Braun, M.J.; !1Gonda, M.A. !$#journal Virology (1990) 175:391-409 !$#title Nucleotide sequence and genome organization of biologically !1active proviruses of the bovine immunodeficiency-like virus. !$#cross-references MUID:90223985; PMID:2183467 !$#accession A34742 !'##molecule_type genomic RNA !'##residues 1-476 ##label GAR !'##cross-references GB:M32690; NID:g210706; PIDN:AAA91270.1; !1PID:g210707 GENETICS !$#gene gag CLASSIFICATION #superfamily AIDS-related virus gag polyprotein KEYWORDS AIDS; core protein; immunodeficiency; polyprotein FEATURE !$1-133 #product core protein p15 #status predicted #label !8P15\ !$134-360 #product core protein p25 #status predicted #label !8P25\ !$361-476 #product core protein p13 #status predicted #label !8P13 SUMMARY #length 476 #molecular-weight 53440 #checksum 3275 SEQUENCE /// ENTRY FOHYIH #type complete TITLE retrovirus-related gag polyprotein - golden hamster intracisternal A-particle H18 ALTERNATE_NAMES core polyprotein ORGANISM #formal_name golden hamster intracisternal A-particle H18 #note host Mesocricetus auratus (golden hamster) DATE 13-Aug-1986 #sequence_revision 13-Aug-1986 #text_change 30-Sep-1993 ACCESSIONS A03952 REFERENCE A93012 !$#authors Ono, M.; Toh, H.; Miyata, T.; Awaya, T. !$#journal J. Virol. (1985) 55:387-394 !$#title Nucleotide sequence of the Syrian hamster intracisternal !1A-particle gene: close evolutionary relationship of type A !1particle gene to types B and D oncovirus genes. !$#cross-references MUID:85264989; PMID:2991563 !$#accession A03952 !'##molecule_type DNA !'##residues 1-572 ##label ONO GENETICS !$#gene gag !$#introns 344/3; 487/3 CLASSIFICATION #superfamily AIDS-related virus gag polyprotein KEYWORDS core protein; polyprotein SUMMARY #length 572 #molecular-weight 63930 #checksum 4714 SEQUENCE /// ENTRY FOMSIA #type complete TITLE retrovirus-related gag polyprotein - mouse intracisternal A-particle MIA14 ORGANISM #formal_name mouse intracisternal A-particle MIA14 #note host Mus musculus (house mouse) DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 25-May-1996 ACCESSIONS A26787 REFERENCE A93027 !$#authors Mietz, J.A.; Grossman, Z.; Lueders, K.K.; Kuff, E.L. !$#journal J. Virol. (1987) 61:3020-3029 !$#title Nucleotide sequence of a complete mouse intracisternal !1A-particle genome: relationship to known aspects of particle !1assembly and function. !$#cross-references MUID:87311859; PMID:3041022 !$#accession A26787 !'##molecule_type DNA !'##residues 1-827 ##label MIE !'##cross-references GB:K01572; GB:K01573; GB:M17551; GB:M23189 COMMENT This particle is a defective retrovirus. GENETICS !$#gene gag CLASSIFICATION #superfamily AIDS-related virus gag polyprotein KEYWORDS core protein; polyprotein SUMMARY #length 827 #molecular-weight 91507 #checksum 9570 SEQUENCE /// ENTRY FOMSIE #type complete TITLE retrovirus-related gag polyprotein - mouse intracisternal A-particle MIAE ALTERNATE_NAMES core polyprotein ORGANISM #formal_name mouse intracisternal A-particle MIAE #note host Mus musculus (house mouse) DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 30-Jun-1993 ACCESSIONS B41305 REFERENCE A41305 !$#authors Reuss, F.U.; Schaller, H.C. !$#journal J. Virol. (1991) 65:5702-5709 !$#title cDNA sequence and genomic characterization of intracisternal !1A-particle-related retroviral elements containing an !1envelope gene. !$#cross-references MUID:92015460; PMID:1920613 !$#accession B41305 !'##molecule_type mRNA !'##residues 1-255 ##label REU !'##cross-references GB:M73818 !'##note readthrough of the terminator UAA occurs between the codons for !1218-Met and 219-Ala COMMENT This particle is a defective retrovirus. GENETICS !$#gene gag CLASSIFICATION #superfamily AIDS-related virus gag polyprotein KEYWORDS core protein; polyprotein SUMMARY #length 255 #molecular-weight 28609 #checksum 9830 SEQUENCE /// ENTRY FOLJSP #type complete TITLE gag polyprotein - human foamy virus ALTERNATE_NAMES core polyprotein ORGANISM #formal_name human foamy virus #note host Homo sapiens (man) DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS A28880 REFERENCE A93033 !$#authors Maurer, B.; Bannert, H.; Darai, G.; Fluegel, R.M. !$#journal J. Virol. (1988) 62:1590-1597 !$#title Analysis of the primary structure of the long terminal !1repeat and the gag and pol genes of the human !1spumaretrovirus. !$#cross-references MUID:88188241; PMID:2451755 !$#accession A28880 !'##molecule_type genomic RNA !'##residues 1-811 ##label MAU !'##cross-references GB:M19427; NID:g330974; PIDN:AAA66555.1; !1PID:g330975 GENETICS !$#gene gag CLASSIFICATION #superfamily foamy virus gag polyprotein KEYWORDS core protein; polyprotein SUMMARY #length 811 #molecular-weight 89613 #checksum 4360 SEQUENCE /// ENTRY FOLJLK #type complete TITLE gag polyprotein - simian foamy virus (type 3, strain LK3) ALTERNATE_NAMES core polyprotein ORGANISM #formal_name simian foamy virus #note host (African green monkey) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 08-Apr-1994 ACCESSIONS A40820 REFERENCE A40820 !$#authors Renne, R.; Friedl, E.; Schweizer, M.; Fleps, U.; Turek, R.; !1Neumann-Haefelin, D. !$#journal Virology (1992) 186:597-608 !$#title Genomic organization and expression of simian foamy virus !1type 3 (SFV-3). !$#cross-references MUID:92124734; PMID:1310187 !$#accession A40820 !'##molecule_type DNA !'##residues 1-643 ##label REN !'##cross-references GB:M74895 GENETICS !$#gene gag CLASSIFICATION #superfamily foamy virus gag polyprotein KEYWORDS core protein; polyprotein SUMMARY #length 643 #molecular-weight 69785 #checksum 4102 SEQUENCE /// ENTRY QQMSLL #type complete TITLE retrovirus-related leucine zipper protein p40 - mouse retrotransposon ALTERNATE_NAMES L1Md repetitive element ORF1; ORF-1137 ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Mar-1989 #sequence_revision 08-Jan-1999 #text_change 16-Jul-1999 ACCESSIONS A58927; A24906; A23430 REFERENCE A93072 !$#authors Loeb, D.D.; Padgett, R.W.; Hardies, S.C.; Shehee, W.R.; !1Comer, M.B.; Edgell, M.H.; Hutchison III, C.A. !$#journal Mol. Cell. Biol. (1986) 6:168-182 !$#title The sequence of a large L1Md element reveals a tandemly !1repeated 5' end and several features found in !1retrotransposons. !$#cross-references MUID:87064284; PMID:3023821 !$#accession A58927 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-357 ##label LOE1 !'##cross-references GB:M13002; NID:g200849; PIDN:AAA66023.1; !1PID:g804787 !'##note sequence constructed using the first potential start codon for !1ORF1 !$#accession A24906 !'##molecule_type DNA !'##residues 'QSHLKNKLLTVTTKTASFRDYQ',1-357 ##label LOE2 !'##cross-references GB:M13002; NID:g200849 !'##note sequence shown in Fig. 2 CLASSIFICATION #superfamily retrovirus-related leucine zipper protein p40 KEYWORDS leucine zipper SUMMARY #length 357 #molecular-weight 41226 #checksum 5051 SEQUENCE /// ENTRY FOFFGY #type complete TITLE retrovirus-related gag polyprotein homolog - fruit fly (Drosophila melanogaster) retrotransposon gypsy ORGANISM #formal_name Drosophila melanogaster DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 16-Jul-1999 ACCESSIONS A25666 REFERENCE A93071 !$#authors Marlor, R.L.; Parkhurst, S.M.; Corces, V.G. !$#journal Mol. Cell. Biol. (1986) 6:1129-1134 !$#title The Drosophila melanogaster gypsy transposable element !1encodes putative gene products homologous to retroviral !1proteins. !$#cross-references MUID:87064379; PMID:3023871 !$#accession A25666 !'##molecule_type DNA !'##residues 1-451 ##label MAR !'##cross-references GB:M12927; NID:g157583; PIDN:AAA70218.1; !1PID:g495769 !'##note the authors translated the codon CAA for residue 264 as Glu GENETICS !$#gene FlyBase:gypsy/gag !'##cross-references FlyBase:FBgn0014965 CLASSIFICATION #superfamily fruit fly gag polyprotein KEYWORDS core protein; polyprotein SUMMARY #length 451 #molecular-weight 50675 #checksum 8260 SEQUENCE /// ENTRY OFFFCP #type complete TITLE copia polyprotein - fruit fly (Drosophila melanogaster) retrotransposon copia CONTAINS copia protein, 31K; copia protein, 48K; proteinase ORGANISM #formal_name Drosophila melanogaster DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 16-Jul-1999 ACCESSIONS A03324; S03612; S14835 REFERENCE A03324 !$#authors Mount, S.M.; Rubin, G.M. !$#journal Mol. Cell. Biol. (1985) 5:1630-1638 !$#title Complete nucleotide sequence of the Drosophila transposable !1element copia: homology between copia and retroviral !1proteins. !$#cross-references MUID:85267679; PMID:2410772 !$#accession A03324 !'##molecule_type DNA !'##residues 1-1409 ##label MOU !'##cross-references GB:M11240; NID:g158615; PIDN:AAA74497.1; !1PID:g950318 REFERENCE S03612 !$#authors Miller, K.; Rosenbaum, J.; Zbrzezna, V.; Pogo, A.O. !$#journal Nucleic Acids Res. (1989) 17:2134 !$#title The nucleotide sequence of Drosophila melanogaster !1copia-specific 2.1-kb mRNA. !$#cross-references MUID:89183629; PMID:2538806 !$#accession S03612 !'##molecule_type mRNA !'##residues 1-391,1375-1409 ##label MIL !'##cross-references EMBL:X13719; NID:g7745; PIDN:CAA31997.1; PID:g7746 REFERENCE S14835 !$#authors Yoshioka, K.; Honma, H.; Zushi, M.; Kondo, S.; Togashi, S.; !1Miyake, T.; Shiba, T. !$#journal EMBO J. (1990) 9:535-541 !$#title Virus-like particle formation of Drosophila copia through !1autocatalytic processing. !$#cross-references MUID:90151630; PMID:1689241 !$#accession S14835 !'##molecule_type DNA !'##residues 1-391,1375-1409 ##label YOS !'##cross-references EMBL:X54147; NID:g7749; PIDN:CAA38086.1; PID:g7750 GENETICS !$#gene FlyBase:copia !'##cross-references FlyBase:FBgn0000349 !$#mobile_element retrotransposon copia CLASSIFICATION #superfamily retrovirus-related polyprotein KEYWORDS polyprotein; proteinase FEATURE !$2-433 #product copia protein, 48K #status predicted #label !8MAT1\ !$2-270 #product copia protein, 31K #status predicted #label !8MAT2\ !$271-433 #product proteinase #status predicted #label MAT3 SUMMARY #length 1409 #molecular-weight 162817 #checksum 7263 SEQUENCE /// ENTRY S05465 #type complete TITLE retrovirus-related polyprotein - Arabidopsis thaliana retrotransposon Ta1-3 ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S05465; A46200; A53226; D60767 REFERENCE S05465 !$#authors Voytas, D.F.; Ausubel, F.M. !$#journal Nature (1988) 336:242-244 !$#title A copia-like transposable element family in Arabidopsis !1thaliana. !$#cross-references MUID:89057095; PMID:2904123 !$#accession S05465 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1291 ##label VOY !'##cross-references EMBL:X13291; NID:g16533; PIDN:CAA31653.1; !1PID:g16534 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1988 REFERENCE A46200 !$#authors Voytas, D.F.; Cummings, M.P.; Koniczny, A.; Ausubel, F.M.; !1Rodermel, S.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:7124-7128 !$#title copia-like retrotransposons are ubiquitous among plants. !$#cross-references MUID:92357784; PMID:1379734 !$#accession A46200 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 960-1048 ##label VOW !'##note sequence extracted from NCBI backbone (NCBIP:112126) REFERENCE A53226 !$#authors Konieczny, A.; Voytas, D.F.; Cummings, M.P.; Ausubel, F.M. !$#journal Genetics (1991) 127:801-809 !$#title A superfamily of Arabidopsis thaliana retrotransposons. !$#cross-references MUID:91231174; PMID:1709409 !$#accession A53226 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 960-1048 ##label KON REFERENCE A60767 !$#authors Voytas, D.F.; Konieczny, A.; Cummings, M.P.; Ausubel, F.M. !$#journal Genetics (1990) 126:713-721 !$#title The structure, distribution and evolution of the Ta1 !1retrotransposable element family of Arabidopsis thaliana. !$#cross-references MUID:91065506; PMID:2174394 !$#accession D60767 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1251-1291 ##label VO2 CLASSIFICATION #superfamily retrovirus-related polyprotein KEYWORDS polyprotein SUMMARY #length 1291 #molecular-weight 146793 #checksum 6675 SEQUENCE /// ENTRY S04273 #type complete TITLE retrovirus-related reverse transcriptase homolog - common tobacco retrotransposon copia-like ORGANISM #formal_name Nicotiana tabacum #common_name common tobacco DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S04273 REFERENCE S04273 !$#authors Grandbastien, M.A.; Spielmann, A.; Caboche, M. !$#journal Nature (1989) 337:376-380 !$#title Tnt1, a mobile retroviral-like transposable element of !1tobacco isolated by plant cell genetics. !$#cross-references MUID:89097311; PMID:2536143 !$#accession S04273 !'##status preliminary; translation not shown !'##molecule_type DNA !'##residues 1-1328 ##label GRA !'##cross-references EMBL:X13777; NID:g20044; PIDN:CAA32025.1; !1PID:g20045 CLASSIFICATION #superfamily retrovirus-related polyprotein SUMMARY #length 1328 #molecular-weight 151076 #checksum 8067 SEQUENCE /// ENTRY S32437 #type complete TITLE pol polyprotein - Volvox carteri f. nagariensis retrotransposon Osser CONTAINS endonuclease; gag protein; proteinase; reverse transcriptase; RNase H ORGANISM #formal_name Volvox carteri f. nagariensis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S32437 REFERENCE S32437 !$#authors Lindauer, A.; Fraser, D.; Bruederlein, M.; Schmitt, R. !$#journal FEBS Lett. (1993) 319:261-266 !$#title Reverse transcriptase families and a copia-like !1retrotransposon, Osser, in the green alga Volvox carteri. !$#cross-references MUID:93209362; PMID:7681411 !$#accession S32437 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1462 ##label LIN !'##cross-references EMBL:X69552; NID:g288596; PIDN:CAA49283.1; !1PID:g288597 !'##experimental_source strain HK10 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1992 !'##note biosynthesis of this protein involves a +1 frameshift between !1codons 1052 and 1053 GENETICS !$#gene pol !$#mobile_element retrotransposon Osser CLASSIFICATION #superfamily retrovirus-related polyprotein KEYWORDS polyprotein SUMMARY #length 1462 #molecular-weight 161131 #checksum 3630 SEQUENCE /// ENTRY GNFV1R #type complete TITLE pol polyprotein - Rous sarcoma virus CONTAINS endonuclease (EC 3.1.-.-); RNA-directed DNA polymerase (EC 2.7.7.49) ORGANISM #formal_name Rous sarcoma virus #note host Gallus gallus (chicken) DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 16-Jun-2000 ACCESSIONS A03955; S26418 REFERENCE A90834 !$#authors Schwartz, D.; Tizard, R.; Gilbert, W. !$#journal Cell (1983) 32:853-869 !$#title Nucleotide sequence of Rous sarcoma virus. !$#cross-references MUID:83155662; PMID:6299578 !$#accession A03955 !'##molecule_type genomic RNA !'##residues 1-895 ##label SCH !'##cross-references GB:V01197; NID:g61695; PID:g1335587 !'##experimental_source strain Prague C !'##note as a result of base variations, a different version of this !1sequence may exist having 14-Ser, 16-Arg, 176-Arg, 199-Lys, !1247-Thr, 304-Gln, 474-Val, 535-Gly, 867-Gly, and 869-Lys REFERENCE S26417 !$#authors Kashuba, V.I.; Rynditch, A.V.; Dostalova, V.; Hlozanek, I.; !1Zubak, S.V.; Kavsan, V.M. !$#submission submitted to the EMBL Data Library, September 1992 !$#description Molecular cloning and DNA sequence analysis of duck-adapted !1variant of Rous sarcoma virus (da Pr-RSV-C). !$#accession S26418 !'##status preliminary !'##molecule_type DNA !'##residues 1-47,'V',49-303,'Q',305-497,'A',499-565,'K',567-672,'A', !1674-895 ##label KAS !'##cross-references EMBL:X68524; NID:g61903; PIDN:CAA48535.1; !1PID:g1334937 COMMENT This protein is synthesized as a gag-pol polyprotein. GENETICS !$#gene pol CLASSIFICATION #superfamily pol polyprotein KEYWORDS endonuclease; hydrolase; nucleotidyltransferase; !1polyprotein; reverse transcriptase SUMMARY #length 895 #molecular-weight 98661 #checksum 8 SEQUENCE /// ENTRY GNMV1M #type complete TITLE HIV-1 retropepsin (EC 3.4.23.16) - Moloney murine leukemia virus CONTAINS nuclease (EC 3.1.-.-); retropepsin (EC 3.4.23.16); RNA-directed DNA polymerase (EC 2.7.7.49) ORGANISM #formal_name Moloney murine leukemia virus #note host Mus spp. (mouse) DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 03-Jun-2002 ACCESSIONS A03956 REFERENCE A93265 !$#authors Shinnick, T.M.; Lerner, R.A.; Sutcliffe, J.G. !$#journal Nature (1981) 293:543-548 !$#title Nucleotide sequence of Moloney murine leukaemia virus. !$#cross-references MUID:82035843; PMID:6169994 !$#accession A03956 !'##molecule_type genomic RNA !'##residues 1-1199 ##label SHI !'##experimental_source clone pMLV-1 !'##note the pol polyprotein contains reverse transcriptase (about 80, !1000 daltons) and possibly a nuclease or protease (up to 52, !1000 daltons); however, the precise boundaries of the protein !1(s) have not yet been defined COMMENT This protein is synthesized as a gag-pol polyprotein. GENETICS !$#gene pol CLASSIFICATION #superfamily pol polyprotein KEYWORDS aspartic proteinase; hydrolase; nucleotidyltransferase; !1polyprotein; reverse transcriptase FEATURE !$3-102 #product retropepsin #status predicted #label RTP\ !$27 #active_site Asp (shared with dimeric partner) !8#status predicted SUMMARY #length 1199 #molecular-weight 133928 #checksum 8162 SEQUENCE /// ENTRY GNMVGV #type complete TITLE HIV-1 retropepsin (EC 3.4.23.16) - AKV murine leukemia virus CONTAINS nuclease (EC 3.1.-.-); retropepsin (EC 3.4.23.16); RNA-directed DNA polymerase (EC 2.7.7.49) ORGANISM #formal_name AKV murine leukemia virus #note host Mus spp. (mouse) DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 03-Jun-2002 ACCESSIONS B92995; B93448; A03957 REFERENCE A92995 !$#authors Herr, W. !$#journal J. Virol. (1984) 49:471-478 !$#title Nucleotide sequence of AKV murine leukemia virus. !$#cross-references MUID:84115072; PMID:6319746 !$#accession B92995 !'##molecule_type genomic RNA !'##residues 1-1196 ##label HER REFERENCE A93448 !$#authors Herr, W.; Corbin, V.; Gilbert, W. !$#journal Nucleic Acids Res. (1982) 10:6931-6944 !$#title Nucleotide sequence of the 3' half of AKV. !$#cross-references MUID:83090450; PMID:6294621 !$#accession B93448 !'##molecule_type DNA !'##residues 353-995,997-1196 ##label HE2 COMMENT This protein is synthesized as a gag-pol polyprotein. COMMENT The pol polyprotein contains reverse transcriptase and !1possibly a nuclease or protease. However, the precise !1boundaries of the protein(s) have not been defined. GENETICS !$#gene pol CLASSIFICATION #superfamily pol polyprotein KEYWORDS aspartic proteinase; hydrolase; nucleotidyltransferase; !1polyprotein; reverse transcriptase FEATURE !$3-102 #product retropepsin #status predicted #label RTP\ !$27 #active_site Asp (shared with dimeric partner) !8#status predicted SUMMARY #length 1196 #molecular-weight 133357 #checksum 3799 SEQUENCE /// ENTRY GNMVRV #type complete TITLE HIV-1 retropepsin (EC 3.4.23.16) - radiation murine leukemia virus CONTAINS nuclease (EC 3.1.-.-); retropepsin (EC 3.4.23.16); RNA-directed DNA polymerase (EC 2.7.7.49) ORGANISM #formal_name radiation murine leukemia virus DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 03-Jun-2002 ACCESSIONS B26183 REFERENCE A94362 !$#authors Merregaert, J.; Janowski, M.; Reddy, E.P. !$#journal Virology (1987) 158:88-102 !$#title Nucleotide sequence of a radiation leukemia virus genome. !$#cross-references MUID:87207680; PMID:3033897 !$#accession B26183 !'##molecule_type DNA !'##residues 1-1196 ##label MER !'##cross-references GB:K03363; GB:M18449; NID:g332032 COMMENT The pol polyprotein contains reverse transcriptase and !1possibly a nuclease or protease. However, the precise !1boundaries of the protein(s) have not been defined. GENETICS !$#gene pol CLASSIFICATION #superfamily pol polyprotein KEYWORDS aspartic proteinase; hydrolase; nucleotidyltransferase; !1polyprotein; reverse transcriptase FEATURE !$3-102 #product retropepsin #status predicted #label RTP\ !$27 #active_site Asp (shared with dimeric partner) !8#status predicted SUMMARY #length 1196 #molecular-weight 133322 #checksum 2996 SEQUENCE /// ENTRY GNVWK #type fragment TITLE pol polyprotein - AKR murine leukemia virus (fragment) ORGANISM #formal_name AKR murine leukemia virus DATE 05-Apr-1983 #sequence_revision 05-Apr-1983 #text_change 04-Oct-1996 ACCESSIONS A03958 REFERENCE A93448 !$#authors Herr, W.; Corbin, V.; Gilbert, W. !$#journal Nucleic Acids Res. (1982) 10:6931-6944 !$#title Nucleotide sequence of the 3' half of AKV. !$#cross-references MUID:83090450; PMID:6294621 !$#accession A03958 !'##molecule_type DNA !'##residues 1-843 ##label HER GENETICS !$#gene pol CLASSIFICATION #superfamily pol polyprotein KEYWORDS polyprotein SUMMARY #length 843 #checksum 754 SEQUENCE /// ENTRY GNLJGL #type complete TITLE HIV-1 retropepsin (EC 3.4.23.16) - gibbon ape leukemia virus CONTAINS nuclease (EC 3.1.-.-); retropepsin (EC 3.4.23.16); RNA-directed DNA polymerase (EC 2.7.7.49) ORGANISM #formal_name gibbon ape leukemia virus DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Jun-2002 ACCESSIONS B32595 REFERENCE A32595 !$#authors Delassus, S.; Sonigo, P.; Wain-Hobson, S. !$#journal Virology (1989) 173:205-213 !$#title Genetic organization of gibbon ape leukemia virus. !$#cross-references MUID:90051069; PMID:2683360 !$#accession B32595 !'##molecule_type genomic RNA !'##residues 1-1165 ##label DEL !'##cross-references GB:M26927; NID:g332610; PIDN:AAA46810.1; !1PID:g332612 COMMENT The pol polyprotein contains reverse transcriptase and !1possibly an endonuclease or a protease. However, the precise !1boundaries of the proteins have not been determined. GENETICS !$#gene pol CLASSIFICATION #superfamily pol polyprotein KEYWORDS aspartic proteinase; endonuclease; hydrolase; !1nucleotidyltransferase; polyprotein; reverse transcriptase FEATURE !$3-102 #product retropepsin #status predicted #label RTP\ !$27 #active_site Asp (shared with dimeric partner) !8#status predicted SUMMARY #length 1165 #molecular-weight 129886 #checksum 2824 SEQUENCE /// ENTRY GNMVM7 #type complete TITLE HIV-1 retropepsin (EC 3.4.23.16) - baboon endogenous virus (strain M7) CONTAINS endonuclease (EC 3.1.-.-); retropepsin (EC 3.4.23.16); RNA-directed DNA polymerase (EC 2.7.7.49) ORGANISM #formal_name baboon endogenous virus #note host Papio sp. (baboon) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 03-Jun-2002 ACCESSIONS JT0261 REFERENCE JT0260 !$#authors Kato, S.; Matsuo, K.; Nishimura, N.; Takahashi, N.; Takano, !1T. !$#journal Jpn. J. Genet. (1987) 62:127-137 !$#title The entire nucleotide sequence of baboon endogenous virus !1DNA: a chimeric genome structure of murine type C and simian !1type D retroviruses. !$#accession JT0261 !'##molecule_type DNA !'##residues 1-1189 ##label KAT !'##cross-references GB:X05470 COMMENT This protein is synthesized as a gag-pol polyprotein. GENETICS !$#gene pol CLASSIFICATION #superfamily pol polyprotein KEYWORDS aspartic proteinase; endonuclease; hydrolase; !1nucleotidyltransferase; reverse transcriptase FEATURE !$1-120 #product proteinase #status predicted #label PTN\ !$3-102 #product retropepsin #status predicted #label RTP\ !$121-797 #product RNA-directed DNA polymerase #status !8predicted #label REV\ !$798-1189 #product endonuclease #status predicted #label EDE\ !$27 #active_site Asp (shared with dimeric partner) !8#status predicted SUMMARY #length 1189 #molecular-weight 132245 #checksum 8761 SEQUENCE /// ENTRY GNMVCE #type fragment TITLE pol polyprotein - feline endogenous virus ECE1 (fragment) CONTAINS endonuclease (EC 3.1.-.-); RNA-directed DNA polymerase (EC 2.7.7.49) ORGANISM #formal_name feline endogenous virus ECE1 #note host Felis silvestris catus (domestic cat) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 08-Apr-1994 ACCESSIONS S12813; S12814 REFERENCE S12812 !$#authors Moehring, R. !$#submission submitted to the EMBL Data Library, February 1990 !$#accession S12813 !'##molecule_type DNA !'##residues 1-1046 ##label MOE !'##cross-references EMBL:X51929 GENETICS !$#gene pol CLASSIFICATION #superfamily pol polyprotein KEYWORDS hydrolase; nucleotidyltransferase; polyprotein FEATURE !$1-647 #product RNA-directed DNA polymerase (fragment) !8#status predicted #label RTP\ !$648-1046 #product endonuclease #status predicted #label EDC SUMMARY #length 1046 #checksum 8085 SEQUENCE /// ENTRY GNMVMM #type complete TITLE pol polyprotein - mouse mammary tumor virus ORGANISM #formal_name mouse mammary tumor virus, MMTV DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 24-Oct-1997 ACCESSIONS C26795 REFERENCE A93030 !$#authors Moore, R.; Dixon, M.; Smith, R.; Peters, G.; Dickson, C. !$#journal J. Virol. (1987) 61:480-490 !$#title Complete nucleotide sequence of a milk-transmitted mouse !1mammary tumor virus: two frameshift suppression events are !1required for translation of gag and pol. !$#cross-references MUID:87112944; PMID:3027377 !$#accession C26795 !'##molecule_type DNA !'##residues 1-899 ##label MOO !'##cross-references EMBL:M15122 GENETICS !$#gene pol CLASSIFICATION #superfamily pol polyprotein KEYWORDS polyprotein; reverse transcriptase SUMMARY #length 899 #molecular-weight 102177 #checksum 4321 SEQUENCE /// ENTRY GNLJGB #type complete TITLE pol polyprotein - bovine leukemia virus CONTAINS endonuclease (EC 3.1.-.-); RNA-directed DNA polymerase (EC 2.7.7.49) ORGANISM #formal_name bovine leukemia virus, BLV #note host Bos sp. (cattle) DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 01-May-1998 ACCESSIONS A03960 REFERENCE A94063 !$#authors Sagata, N.; Yasunaga, T.; Tsuzuku-Kawamura, J.; Ohishi, K.; !1Ogawa, Y.; Ikawa, Y. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:677-681 !$#title Complete nucleotide sequence of the genome of bovine !1leukemia virus: its evolutionary relationship to other !1retroviruses. !$#cross-references MUID:85140159; PMID:2983308 !$#accession A03960 !'##molecule_type DNA !'##residues 1-852 ##label SAG !'##note the authors translated the codon TTC for residue 104 as Ser and !1CTA for residue 473 as Lys COMMENT Specific enzymatic cleavages may yield mature proteins !1including reverse transcriptase and endonuclease. However, !1exact cleavage sites are undetermined. GENETICS !$#gene pol CLASSIFICATION #superfamily pol polyprotein KEYWORDS endonuclease; hydrolase; nucleotidyltransferase; !1polyprotein; reverse transcriptase SUMMARY #length 852 #molecular-weight 95182 #checksum 1732 SEQUENCE /// ENTRY GNLJGA #type complete TITLE pol polyprotein - bovine leukemia virus (strain Australia) CONTAINS endonuclease (EC 3.1.-.-); RNA-directed DNA polymerase (EC 2.7.7.49) ORGANISM #formal_name bovine leukemia virus, BLV #note host Bos sp. (cattle) DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 28-Jul-2000 ACCESSIONS JQ0555 REFERENCE JQ0554 !$#authors Coulston, J.; Naif, H.; Brandon, R.; Kumar, S.; Khan, S.; !1Daniel, R.C.W.; Lavin, M.F. !$#journal J. Gen. Virol. (1990) 71:1737-1746 !$#title Molecular cloning and sequencing of an Australian isolate of !1proviral bovine leukaemia virus DNA: comparison with other !1isolates. !$#cross-references MUID:90362060; PMID:2167927 !$#accession JQ0555 !'##molecule_type DNA !'##residues 1-852 ##label COU !'##cross-references DDBJ:D00647; NID:g2920795; PIDN:BAA00544.1; !1PID:g221052 !'##note this reading frame extends between two stop codons and does not !1begin with a start codon !'##note the authors translated the codon CCC for residue 514 as Gln COMMENT The precise boundary between RNA-directed DNA polymerase and !1endonuclease has not been determined. GENETICS !$#gene pol CLASSIFICATION #superfamily pol polyprotein KEYWORDS endonuclease; hydrolase; nucleotidyltransferase; !1polyprotein; reverse transcriptase SUMMARY #length 852 #molecular-weight 95441 #checksum 3418 SEQUENCE /// ENTRY GNLJGH #type complete TITLE pol polyprotein - human T-cell lymphotropic virus type 1 CONTAINS nuclease (EC 3.1.-.-); proteinase (EC 3.4.-.-); RNA-directed DNA polymerase (EC 2.7.7.49) ORGANISM #formal_name human T-cell lymphotropic virus type 1, HTLV-1 #note host Homo sapiens (man) DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 16-Jul-1999 ACCESSIONS A03961; S02391 REFERENCE A93954 !$#authors Seiki, M.; Hattori, S.; Hirayama, Y.; Yoshida, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:3618-3622 !$#title Human adult T-cell leukemia virus: complete nucleotide !1sequence of the provirus genome integrated in leukemia cell !1DNA. !$#cross-references MUID:83221647; PMID:6304725 !$#accession A03961 !'##molecule_type DNA !'##residues 1-896 ##label SEI !'##cross-references GB:J02029; GB:M33896; NID:g425135; PIDN:AAA96673.1; !1PID:g331148 !'##experimental_source strain ATK !'##note the authors translated the codon CGT for residue 15 as Leu and !1GAG for residue 351 as Gln REFERENCE S02391 !$#authors Bangham, C.R.M.; Daenke, S.; Phillips, R.E.; Cruickshank, !1J.K.; Bell, J.I. !$#journal EMBO J. (1988) 7:4179-4184 !$#title Enzymatic amplification of exogenous and endogenous !1retroviral sequences from DNA of patients with tropical !1spastic paraparesis. !$#cross-references MUID:89210803; PMID:2468487 !$#accession S02391 !'##molecule_type DNA !'##residues 69-185 ##label BAN !'##cross-references EMBL:X14144; NID:g61567; PIDN:CAA32360.1; !1PID:g930258 !'##note 116-Lys was also found COMMENT This protein is synthesized as a gag-pol polyprotein. COMMENT The pol polyprotein contains reverse transcriptase and !1possibly a nuclease or protease. However, the precise !1boundaries of the protein(s) have not been defined. GENETICS !$#gene pol CLASSIFICATION #superfamily pol polyprotein KEYWORDS hydrolase; nucleotidyltransferase; polyprotein; reverse !1transcriptase SUMMARY #length 896 #molecular-weight 100140 #checksum 1897 SEQUENCE /// ENTRY GNLJCN #type complete TITLE pol polyprotein - human T-cell lymphotropic virus type 1 (isolate Caribbean) CONTAINS endonuclease (EC 3.1.-.-); RNA-directed DNA polymerase (EC 2.7.7.49) ORGANISM #formal_name human T-cell lymphotropic virus type 1, HTLV-1 #note host Homo sapiens (man) DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jun-2000 ACCESSIONS C28136 REFERENCE A92797 !$#authors Malik, K.T.A.; Even, J.; Karpas, A. !$#journal J. Gen. Virol. (1988) 69:1695-1710 !$#title Molecular cloning and complete nucleotide sequence of an !1adult T cell leukaemia virus/human T cell leukaemia virus !1type I (ATLV/HTLV-I) isolate of Caribbean origin: !1relationship to other members of the ATLV/HTLV-I subgroup. !$#cross-references MUID:88274338; PMID:2899128 !$#accession C28136 !'##molecule_type DNA !'##residues 1-896 ##label MAL !'##cross-references GB:D13784; GB:D00294; NID:g221866; PIDN:BAA02931.1; !1PID:g221869 COMMENT The pol polyprotein contains reverse transcriptase and !1possibly a nuclease or a protease. However, the precise !1boundaries of the proteins have not been defined. GENETICS !$#gene pol CLASSIFICATION #superfamily pol polyprotein KEYWORDS hydrolase; nucleotidyltransferase; polyprotein; reverse !1transcriptase SUMMARY #length 896 #molecular-weight 100198 #checksum 2617 SEQUENCE /// ENTRY GNLJH2 #type complete TITLE pol polyprotein - human T-cell lymphotropic virus type 2 CONTAINS endonuclease (EC 3.1.-.-); RNA-directed DNA polymerase (EC 2.7.7.49) ORGANISM #formal_name human T-cell lymphotropic virus type 2, HTLV-2 #note host Homo sapiens (man) DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 31-Jan-1997 ACCESSIONS A03962 REFERENCE A94042 !$#authors Shimotohno, K.; Takahashi, Y.; Shimizu, N.; Gojobori, T.; !1Golde, D.W.; Chen, I.S.Y.; Miwa, M.; Sugimura, T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:3101-3105 !$#title Complete nucleotide sequence of an infectious clone of human !1T-cell leukemia virus type II: an open reading frame for the !1protease gene. !$#cross-references MUID:85216449; PMID:2582407 !$#accession A03962 !'##molecule_type DNA !'##residues 1-982 ##label SHI !'##note the authors translated the codon TCC for residue 637 as Ala COMMENT Specific enzymatic cleavages may yield mature proteins !1including reverse transcriptase and endonuclease. However, !1exact cleavage sites are undetermined. GENETICS !$#gene pol CLASSIFICATION #superfamily pol polyprotein KEYWORDS AIDS; endonuclease; hydrolase; immunodeficiency; !1nucleotidyltransferase; polyprotein; reverse transcriptase SUMMARY #length 982 #molecular-weight 109869 #checksum 3105 SEQUENCE /// ENTRY GNLJSA #type complete TITLE pol polyprotein - simian AIDS retrovirus SRV-1 CONTAINS endonuclease (EC 3.1.-.-); RNA-directed DNA polymerase (EC 2.7.7.49) ORGANISM #formal_name simian AIDS retrovirus SRV-1 #note host Macaca mulatta (rhesus macaque) DATE 13-Aug-1986 #sequence_revision 13-Aug-1986 #text_change 16-Jul-1999 ACCESSIONS A03963 REFERENCE A94711 !$#authors Power, M.D.; Marx, P.A.; Bryant, M.L.; Gardner, M.B.; Barr, !1P.J.; Luciw, P.A. !$#journal Science (1986) 231:1567-1572 !$#title Nucleotide sequence of SRV-1, a type D simian acquired !1immune deficiency syndrome retrovirus. !$#cross-references MUID:86151668; PMID:3006247 !$#accession A03963 !'##molecule_type DNA !'##residues 1-867 ##label POW !'##cross-references GB:M11841; NID:g334746; PIDN:AAA47732.1; !1PID:g334749 COMMENT The pol polyprotein contains reverse transcriptase and !1endonuclease; however, the precise boundaries of the !1proteins have not been defined. GENETICS !$#gene pol CLASSIFICATION #superfamily pol polyprotein KEYWORDS AIDS; endonuclease; hydrolase; immunodeficiency; !1nucleotidyltransferase; polyprotein; reverse transcriptase SUMMARY #length 867 #molecular-weight 98361 #checksum 641 SEQUENCE /// ENTRY GNLJMP #type complete TITLE pol polyprotein (clone 6A) - Mason-Pfizer monkey virus CONTAINS endonuclease (EC 3.1.-.-); RNA-directed DNA polymerase (EC 2.7.7.49) ORGANISM #formal_name Mason-Pfizer monkey virus DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 16-Jul-1999 ACCESSIONS C25839 REFERENCE A90878 !$#authors Sonigo, P.; Barker, C.; Hunter, E.; Wain-Hobson, S. !$#journal Cell (1986) 45:375-385 !$#title Nucleotide sequence of Mason-Pfizer monkey virus: an !1immunosuppressive D-type retrovirus. !$#cross-references MUID:86189951; PMID:2421920 !$#accession C25839 !'##molecule_type DNA !'##residues 1-867 ##label SON !'##cross-references GB:M12349; NID:g334702; PIDN:AAA47711.1; !1PID:g334704 COMMENT The pol polyprotein contains reverse transcriptase and !1endonuclease; however, the precise boundaries of the !1proteins have not been defined. GENETICS !$#gene pol CLASSIFICATION #superfamily pol polyprotein KEYWORDS AIDS; endonuclease; hydrolase; immunodeficiency; !1nucleotidyltransferase; polyprotein; reverse transcriptase SUMMARY #length 867 #molecular-weight 98404 #checksum 179 SEQUENCE /// ENTRY GNLJHD #type complete TITLE pol polyprotein - squirrel monkey retrovirus SMRV-H (SMRV-HLB) CONTAINS endonuclease (EC 3.1.-.-); RNA-directed DNA polymerase (EC 2.7.7.49) ORGANISM #formal_name squirrel monkey retrovirus SMRV-H DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 01-May-1998 ACCESSIONS C31827 REFERENCE A31827 !$#authors Oda, T.; Ikeda, S.; Watanabe, S.; Hatsushika, M.; Akiyama, !1K.; Mitsunobu, F. !$#journal Virology (1988) 167:468-476 !$#title Molecular cloning, complete nucleotide sequence, and gene !1structure of the provirus genome of a retrovirus produced in !1a human lymphoblastoid cell line. !$#cross-references MUID:89073750; PMID:3201749 !$#accession C31827 !'##molecule_type DNA !'##residues 1-888 ##label ODA COMMENT The pol polyprotein contains reverse transcriptase and !1endonuclease; however, the precise boundaries of the !1proteins have not been determined. GENETICS !$#gene pol CLASSIFICATION #superfamily pol polyprotein KEYWORDS endonuclease; hydrolase; nucleotidyltransferase; !1polyprotein; reverse transcriptase SUMMARY #length 888 #molecular-weight 99165 #checksum 5059 SEQUENCE /// ENTRY GNMVJA #type complete TITLE pol polyprotein - sheep pulmonary adenomatosis virus CONTAINS endonuclease (EC 3.1.-.-); RNA-directed DNA polymerase (EC 2.7.7.49) ORGANISM #formal_name sheep pulmonary adenomatosis virus DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 08-Apr-1994 ACCESSIONS C42740 REFERENCE A42740 !$#authors York, D.F.; Vigne, R.; Verwoerd, D.W.; Querat, G. !$#journal J. Virol. (1992) 66:4930-4939 !$#title Nucleotide sequence of the jaagsiekte retrovirus, an !1exogenous and endogenous type D and B retrovirus of sheep !1and goats. !$#cross-references MUID:92333675; PMID:1629959 !$#accession C42740 !'##molecule_type genomic RNA !'##residues 1-870 ##label YOR !'##cross-references GB:M80216 COMMENT This protein is likely to be expressed as a gag-pol !1polyprotein. COMMENT The precise boundary between RNA-directed DNA polymerase and !1endonuclease has not been determined. GENETICS !$#gene pol !$#start_codon UCA CLASSIFICATION #superfamily pol polyprotein KEYWORDS endonuclease; hydrolase; nucleotidyltransferase; !1polyprotein; reverse transcriptase SUMMARY #length 870 #molecular-weight 99312 #checksum 4310 SEQUENCE /// ENTRY GNHYIH #type complete TITLE retrovirus-related pol polyprotein - golden hamster intracisternal A-particle H18 ALTERNATE_NAMES reverse transcriptase ORGANISM #formal_name golden hamster intracisternal A-particle H18 #note host Mesocricetus auratus (golden hamster) DATE 13-Aug-1986 #sequence_revision 13-Aug-1986 #text_change 30-Sep-1993 ACCESSIONS A03964 REFERENCE A93012 !$#authors Ono, M.; Toh, H.; Miyata, T.; Awaya, T. !$#journal J. Virol. (1985) 55:387-394 !$#title Nucleotide sequence of the Syrian hamster intracisternal !1A-particle gene: close evolutionary relationship of type A !1particle gene to types B and D oncovirus genes. !$#cross-references MUID:85264989; PMID:2991563 !$#accession A03964 !'##molecule_type DNA !'##residues 1-863 ##label ONO COMMENT Readthrough of three terminators may occur: TAA between !1codons ATT for 660-Ile and AAA for 661-Lys, TAG between !1codons TCC for 832-Ser and TAT for 833-Tyr, and TAG between !1codons CCC for 859-Pro and ATT for 860-Ile. GENETICS !$#gene pol !$#introns 315/3 CLASSIFICATION #superfamily pol polyprotein KEYWORDS polyprotein; reverse transcriptase SUMMARY #length 863 #molecular-weight 97036 #checksum 6044 SEQUENCE /// ENTRY GNMSIA #type complete TITLE retrovirus-related pol polyprotein - mouse intracisternal A-particle MIA14 ORGANISM #formal_name mouse intracisternal A-particle MIA14 #note host Mus musculus (house mouse) DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 30-Jun-1993 ACCESSIONS B26787 REFERENCE A93027 !$#authors Mietz, J.A.; Grossman, Z.; Lueders, K.K.; Kuff, E.L. !$#journal J. Virol. (1987) 61:3020-3029 !$#title Nucleotide sequence of a complete mouse intracisternal !1A-particle genome: relationship to known aspects of particle !1assembly and function. !$#cross-references MUID:87311859; PMID:3041022 !$#accession B26787 !'##molecule_type DNA !'##residues 1-867 ##label MIE !'##note the authors translated the codon TGG for residue 64 as Asp, AAC !1for residue 92 as Ala, GCC for residue 106 as Arg, and ATC !1for residue 139 as Ala COMMENT The DNA sequence was obtained from GenBank, release 55.0. COMMENT This particle is a defective retrovirus. GENETICS !$#gene pol CLASSIFICATION #superfamily pol polyprotein KEYWORDS polyprotein; reverse transcriptase SUMMARY #length 867 #molecular-weight 97778 #checksum 7242 SEQUENCE /// ENTRY GNMSIP #type complete TITLE retrovirus-related pol polyprotein - mouse intracisternal A-particle MIAIL3 ORGANISM #formal_name mouse intracisternal A-particle MIAIL3 #note host Mus musculus (house mouse) DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jul-1999 ACCESSIONS A23597 REFERENCE A23597 !$#authors Ymer, S.; Tucker, W.Q.J.; Campbell, H.D.; Young, I.G. !$#journal Nucleic Acids Res. (1986) 14:5901-5918 !$#title Nucleotide sequence of the intracisternal A-particle genome !1inserted 5' to the interleukin-3 gene of the leukaemia cell !1line WEHI-3B. !$#cross-references MUID:86286596; PMID:3016667 !$#accession A23597 !'##molecule_type DNA !'##residues 1-814 ##label YME !'##cross-references GB:X04120; NID:g51502; PIDN:CAA27732.1; PID:g51503 COMMENT This particle is a defective retrovirus. CLASSIFICATION #superfamily pol polyprotein KEYWORDS polyprotein; reverse transcriptase SUMMARY #length 814 #molecular-weight 91000 #checksum 8662 SEQUENCE /// ENTRY GNVWH3 #type complete TITLE HIV-1 retropepsin (EC 3.4.23.16) - human immunodeficiency virus type 1 (isolate HTLV-III, BH10) CONTAINS endonuclease (EC 3.1.-.-); retropepsin (EC 3.4.23.16); RNA-directed DNA polymerase (EC 2.7.7.49) ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 #note host Homo sapiens (man) DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 03-Jun-2002 ACCESSIONS A03965 REFERENCE A93353 !$#authors Ratner, L.; Haseltine, W.; Patarca, R.; Livak, K.J.; !1Starcich, B.; Josephs, S.F.; Doran, E.R.; Rafalski, J.A.; !1Whitehorn, E.A.; Baumeister, K.; Ivanoff, L.; Petteway Jr., !1S.R.; Pearson, M.L.; Lautenberger, J.A.; Papas, T.S.; !1Ghrayeb, J.; Chang, N.T.; Gallo, R.C.; Wong-Staal, F. !$#journal Nature (1985) 313:277-284 !$#title Complete nucleotide sequence of the AIDS virus, HTLV-III. !$#cross-references MUID:85111123; PMID:2578615 !$#accession A03965 !'##molecule_type DNA !'##residues 1-1015 ##label RAT !'##cross-references GB:M15654; GB:K02008; GB:K02009; GB:K02010; !1NID:g326383; PIDN:AAA44198.1; PID:g326385 COMMENT Specific enzymatic cleavages may yield mature proteins !1including protease, reverse transcriptase, and endonuclease. !1However, exact cleavage sites are undetermined. GENETICS !$#gene pol CLASSIFICATION #superfamily pol polyprotein KEYWORDS AIDS; aspartic proteinase; endonuclease; hydrolase; !1immunodeficiency; nucleotidyltransferase; polyprotein; !1reverse transcriptase FEATURE !$69-167 #product retropepsin #status predicted #label RTP\ !$93 #active_site Asp (shared with dimeric partner) !8#status experimental SUMMARY #length 1015 #molecular-weight 115020 #checksum 1889 SEQUENCE /// ENTRY GNVWLV #type complete TITLE HIV-1 retropepsin (EC 3.4.23.16) - human immunodeficiency virus type 1 (isolate LAV-1a) CONTAINS endonuclease (EC 3.1.-.-); retropepsin (EC 3.4.23.16); RNA-directed DNA polymerase (EC 2.7.7.49) ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 #note host Homo sapiens (man) DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 03-Jun-2002 ACCESSIONS A03966 REFERENCE A90866 !$#authors Wain-Hobson, S.; Sonigo, P.; Danos, O.; Cole, S.; Alizon, M. !$#journal Cell (1985) 40:9-17 !$#title Nucleotide sequence of the AIDS virus, LAV. !$#cross-references MUID:85099333; PMID:2981635 !$#accession A03966 !'##molecule_type DNA !'##residues 1-1003 ##label WAI COMMENT Specific enzymatic cleavages may yield mature proteins !1including protease, reverse transcriptase, and endonuclease. !1However, exact cleavage sites are undetermined. GENETICS !$#gene pol CLASSIFICATION #superfamily pol polyprotein KEYWORDS AIDS; aspartic proteinase; endonuclease; hydrolase; !1immunodeficiency; nucleotidyltransferase; polyprotein; !1reverse transcriptase FEATURE !$57-155 #product retropepsin #status predicted #label RTP\ !$81 #active_site Asp (shared with dimeric partner) !8#status experimental SUMMARY #length 1003 #molecular-weight 113759 #checksum 4947 SEQUENCE /// ENTRY GNVWVL #type complete TITLE HIV-1 retropepsin (EC 3.4.23.16) - human immunodeficiency virus type 1 (isolate LV) CONTAINS endonuclease (EC 3.1.-.-); retropepsin (EC 3.4.23.16); RNA-directed DNA polymerase (EC 2.7.7.49) ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 03-Jun-2002 ACCESSIONS A03967 REFERENCE A93355 !$#authors Muesing, M.A.; Smith, D.H.; Cabradilla, C.D.; Benton, C.V.; !1Lasky, L.A.; Capon, D.J. !$#journal Nature (1985) 313:450-458 !$#title Nucleic acid structure and expression of the human AIDS/ !1lymphadenopathy retrovirus. !$#cross-references MUID:85111157; PMID:2982104 !$#accession A03967 !'##molecule_type DNA !'##residues 1-1012 ##label MUE COMMENT Specific enzymatic cleavages may yield mature proteins !1including protease, reverse transcriptase, and endonuclease. !1However, exact cleavage sites are undetermined. GENETICS !$#gene pol CLASSIFICATION #superfamily pol polyprotein KEYWORDS AIDS; aspartic proteinase; endonuclease; hydrolase; !1immunodeficiency; nucleotidyltransferase; polyprotein; !1reverse transcriptase FEATURE !$66-164 #product retropepsin #status predicted #label RTP\ !$90 #active_site Asp (shared with dimeric partner) !8#status experimental SUMMARY #length 1012 #molecular-weight 114569 #checksum 1416 SEQUENCE /// ENTRY GNVWA2 #type complete TITLE HIV-1 retropepsin (EC 3.4.23.16) - human immunodeficiency virus type 1 (isolate ARV-2) CONTAINS endonuclease (EC 3.1.-.-); retropepsin (EC 3.4.23.16); RNA-directed DNA polymerase (EC 2.7.7.49) ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 #note host Homo sapiens (man) DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 03-Jun-2002 ACCESSIONS A03968 REFERENCE A04003 !$#authors Sanchez-Pescador, R.; Power, M.D.; Barr, P.J.; Steimer, !1K.S.; Stempien, M.M.; Brown-Shimer, S.L.; Gee, W.W.; Renard, !1A.; Randolph, A.; Levy, J.A.; Dina, D.; Luciw, P.A. !$#journal Science (1985) 227:484-492 !$#title Nucleotide sequence and expression of an AIDS-associated !1retrovirus (ARV-2). !$#cross-references MUID:85090453; PMID:2578227 !$#accession A03968 !'##molecule_type DNA !'##residues 1-1003 ##label SAN !'##cross-references GB:K02007; NID:g328658; PIDN:AAB59876.1; !1PID:g328662 COMMENT Specific enzymatic cleavages may yield mature proteins !1including protease, reverse transcriptase, and endonuclease. !1However, exact cleavage sites are undetermined. GENETICS !$#gene pol CLASSIFICATION #superfamily pol polyprotein KEYWORDS AIDS; aspartic proteinase; endonuclease; hydrolase; !1immunodeficiency; nucleotidyltransferase; polyprotein; !1reverse transcriptase FEATURE !$57-147 #product retropepsin #status predicted #label RTP\ !$81 #active_site Asp (shared with dimeric partner) !8#status predicted SUMMARY #length 1003 #molecular-weight 113723 #checksum 267 SEQUENCE /// ENTRY B44001 #type complete TITLE HIV-1 retropepsin (EC 3.4.23.16) - human immunodeficiency virus type 1 (strain YU-2) CONTAINS endonuclease (EC 3.1.-.-); retropepsin (EC 3.4.23.16); RNA-directed DNA polymerase (EC 2.7.7.49) ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 #note host Homo sapiens (man) DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 03-Jun-2002 ACCESSIONS B44001 REFERENCE A44001 !$#authors Li, Y.; Hui, H.; Burgess, C.J.; Price, R.W.; Sharp, P.M.; !1Hahn, B.H.; Shaw, G.M. !$#journal J. Virol. (1992) 66:6587-6600 !$#title Complete nucleotide sequence, genome organization, and !1biological properties of human immunodeficiency virus type 1 !1in vivo: evidence for limited defectiveness and !1complementation. !$#cross-references MUID:93021387; PMID:1404605 !$#accession B44001 !'##molecule_type DNA !'##residues 1-1003 ##label LIY !'##cross-references GB:M93258 COMMENT This protein is synthesized as a gag-pol polyprotein. COMMENT Specific enzymatic cleavages may yield mature proteins !1including proteinase, RNA-directed DNA polymerse, and !1endonuclease. However, exact cleavage sites are !1undetermined. GENETICS !$#gene pol CLASSIFICATION #superfamily pol polyprotein KEYWORDS AIDS; aspartic proteinase; endonuclease; hydrolase; !1immunodeficiency; nucleotidyltransferase; polyprotein; !1reverse transcriptase FEATURE !$57-155 #product retropepsin #status predicted #label RTP\ !$81 #active_site Asp (shared with dimeric partner) !8#status predicted SUMMARY #length 1003 #molecular-weight 113794 #checksum 4403 SEQUENCE /// ENTRY GNLJND #type complete TITLE HIV-1 retropepsin (EC 3.4.23.16) - human immunodeficiency virus type 1 (isolate NDK) CONTAINS endonuclease (EC 3.1.-.-); retropepsin (EC 3.4.23.16); RNA-directed DNA polymerase (EC 2.7.7.49) ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 #note host Homo sapiens (man) DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Jun-2002 ACCESSIONS JQ0067 REFERENCE JQ0065 !$#authors Spire, B.; Sire, J.; Zachar, V.; Rey, F.; Barre-Sinoussi, !1F.; Galibert, F.; Hampe, A.; Chermann, J.C. !$#journal Gene (1989) 81:275-284 !$#title Nucleotide sequence of HIV1-NDK: a highly cytopathic strain !1of the human immunodeficiency virus. !$#cross-references MUID:90034200; PMID:2806917 !$#accession JQ0067 !'##molecule_type DNA !'##residues 1-1002 ##label SPI !'##cross-references GB:M27323; NID:g328154; PIDN:AAA44869.1; !1PID:g328158 COMMENT Specific enzymatic cleavages may yield mature proteins !1including protease, reverse transcriptase, and endonuclease. !1However, exact cleavage sites are undetermined. GENETICS !$#gene pol CLASSIFICATION #superfamily pol polyprotein KEYWORDS AIDS; aspartic proteinase; endonuclease; hydrolase; !1immunodeficiency; nucleotidyltransferase; polyprotein; !1reverse transcriptase FEATURE !$56-154 #product retropepsin #status predicted #label RTP\ !$80 #active_site Asp (shared with dimeric partner) !8#status predicted SUMMARY #length 1002 #molecular-weight 113621 #checksum 9917 SEQUENCE /// ENTRY GNLJSI #type complete TITLE HIV-1 retropepsin (EC 3.4.23.16) - simian immunodeficiency virus SIVcpz CONTAINS endonuclease (EC 3.1.-.-); retropepsin (EC 3.4.23.16); RNA-directed DNA polymerase (EC 2.7.7.49) ORGANISM #formal_name simian immunodeficiency virus SIVcpz #note host Pan troglodytes (chimpanzee) DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Jun-2002 ACCESSIONS S09984 REFERENCE S09983 !$#authors Huet, T.; Cheynier, R.; Meyerhans, A.; Roelants, G.; !1Wain-Hobson, S. !$#journal Nature (1990) 345:356-359 !$#title Genetic organization of a chimpanzee lentivirus related to !1HIV-1. !$#cross-references MUID:90259077; PMID:2188136 !$#accession S09984 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1027 ##label HUE !'##cross-references EMBL:X52154 COMMENT Specific enzymatic cleavages may yield mature proteins !1including protease, reverse transcriptase, and endonuclease. !1However, exact cleavage sites are undetermined. GENETICS !$#gene pol CLASSIFICATION #superfamily pol polyprotein KEYWORDS AIDS; aspartic proteinase; endonuclease; hydrolase; !1immunodeficiency; nucleotidyltransferase; polyprotein; !1reverse transcriptase FEATURE !$81-180 #product retropepsin #status predicted #label RTP\ !$105 #active_site Asp (shared with dimeric partner) !8#status predicted SUMMARY #length 1027 #molecular-weight 116930 #checksum 3468 SEQUENCE /// ENTRY GNLJG2 #type complete TITLE HIV-1 retropepsin (EC 3.4.23.16) - human immunodeficiency virus type 2 (isolate ROD) CONTAINS endonuclease (EC 3.1.-.-); retropepsin (EC 3.4.23.16); RNA-directed DNA polymerase (EC 2.7.7.49) ORGANISM #formal_name human immunodeficiency virus type 2, HIV-2 DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 03-Jun-2002 ACCESSIONS B26262 REFERENCE A26262 !$#authors Guyader, M.; Emerman, M.; Sonigo, P.; Clavel, F.; !1Montagnier, L.; Alizon, M. !$#journal Nature (1987) 326:662-669 !$#title Genome organization and transactivation of the human !1immuno-deficiency virus type 2. !$#cross-references MUID:87173056; PMID:3031510 !$#accession B26262 !'##molecule_type DNA !'##residues 1-1036 ##label GUY !'##cross-references GB:M15390 COMMENT Specific enzymatic cleavages may yield mature proteins !1including protease, reverse transcriptase, and endonuclease. !1However, exact cleavage sites are undetermined. GENETICS !$#gene pol CLASSIFICATION #superfamily pol polyprotein KEYWORDS AIDS; aspartic proteinase; endonuclease; hydrolase; !1immunodeficiency; nucleotidyltransferase; polyprotein; !1reverse transcriptase FEATURE !$86-184 #product retropepsin #status predicted #label RTP\ !$110 #active_site Asp (shared with dimeric partner) !8#status predicted SUMMARY #length 1036 #molecular-weight 117080 #checksum 1189 SEQUENCE /// ENTRY GNLJST #type complete TITLE HIV-1 retropepsin (EC 3.4.23.16) - human immunodeficiency virus type 2 (isolate ST) CONTAINS endonuclease (EC 3.1.-.-); retropepsin (EC 3.4.23.16); RNA-directed DNA polymerase (EC 2.7.7.49) ORGANISM #formal_name human immunodeficiency virus type 2, HIV-2 #note host Homo sapiens (man) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Jun-2002 ACCESSIONS B33943 REFERENCE A33943 !$#authors Kumar, P.; Hui, H.; Kappes, J.C.; Haggarty, B.S.; Hoxie, !1J.A.; Arya, S.K.; Shaw, G.M.; Hahn, B.H. !$#journal J. Virol. (1990) 64:890-901 !$#title Molecular characterization of an attenuated human !1immunodeficiency virus type 2 isolate. !$#cross-references MUID:90112662; PMID:2296086 !$#accession B33943 !'##molecule_type genomic RNA !'##residues 1-1055 ##label KUM COMMENT The pol polyprotein contains reverse transcriptase and !1endonuclease. However, the precise boundary of the proteins !1has not been determined. GENETICS !$#gene pol CLASSIFICATION #superfamily pol polyprotein KEYWORDS aspartic proteinase; endonuclease; hydrolase; !1nucleotidyltransferase; reverse transcriptase FEATURE !$105-203 #product retropepsin #status predicted #label RTP\ !$129 #active_site Asp (shared with dimeric partner) !8#status predicted SUMMARY #length 1055 #molecular-weight 119767 #checksum 4167 SEQUENCE /// ENTRY GNLJCA #type complete TITLE HIV-1 retropepsin (EC 3.4.23.16) - human immunodeficiency virus type 2 (isolate CAM2/Guinea-Bissau) CONTAINS endonuclease (EC 3.1.-.-); retropepsin (EC 3.4.23.16); RNA-directed DNA polymerase (EC 2.7.7.49) ORGANISM #formal_name human immunodeficiency virus type 2, HIV-2 #note host Homo sapiens (man) DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 03-Jun-2002 ACCESSIONS B38475; JQ0974 REFERENCE A38475 !$#authors Tristem, M.; Hill, F.; Karpas, A. !$#journal J. Gen. Virol. (1991) 72:721-724 !$#title Nucleotide sequence of a Guinea-Bissau-derived human !1immunodeficiency virus type 2 proviral clone (HIV-2-CAM2). !$#cross-references MUID:91170959; PMID:2005437 !$#accession B38475 !'##molecule_type DNA !'##residues 1-1034 ##label TRI !'##note readthrough of the terminator TGA may occur between codons ATT !1for 564-Ile and GGA for 565-Gly COMMENT The cleavage sites of this polyprotein have not been !1determined. GENETICS !$#gene pol CLASSIFICATION #superfamily pol polyprotein KEYWORDS AIDS; aspartic proteinase; endonuclease; hydrolase; !1immunodeficiency; nucleotidyltransferase; reverse !1transcriptase FEATURE !$85-183 #product retropepsin #status predicted #label RTP\ !$109 #active_site Asp (shared with dimeric partner) !8#status predicted SUMMARY #length 1034 #molecular-weight 117194 #checksum 9580 SEQUENCE /// ENTRY GNLJGG #type complete TITLE HIV-1 retropepsin (EC 3.4.23.16) - human immunodeficiency virus type 2 (isolate GH-1) CONTAINS endonuclease (EC 3.1.-.-); retropepsin (EC 3.4.23.16); RNA-directed DNA polymerase (EC 2.7.7.49) ORGANISM #formal_name human immunodeficiency virus type 2, HIV-2 #note host Homo sapiens (man) DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 03-Jun-2002 ACCESSIONS JS0328 REFERENCE JS0327 !$#authors Hasegawa, A.; Tsujimoto, H.; Maki, N.; Ishikawa, K.; Miura, !1T.; Fukasawa, M.; Miki, K.; Hayami, M. !$#journal AIDS Res. Hum. Retroviruses (1989) 5:593-604 !$#title Sequence of a distinct HIV-2 isolate from Ghana showing !1significant divergence in its genome. !$#cross-references MUID:90122350; PMID:2611042 !$#accession JS0328 !'##molecule_type DNA !'##residues 1-1035 ##label HAS !'##note this sequence was submitted to JIPID, October 1989 COMMENT Cleavage sites that yield the mature proteins remain to be !1determined. GENETICS !$#gene pol !$#start_codon ACA CLASSIFICATION #superfamily pol polyprotein KEYWORDS AIDS; aspartic proteinase; endonuclease; hydrolase; !1nucleotidyltransferase; polyprotein; reverse transcriptase FEATURE !$85-183 #product retropepsin #status predicted #label RTP\ !$109 #active_site Asp (shared with dimeric partner) !8#status predicted SUMMARY #length 1035 #molecular-weight 117149 #checksum 3429 SEQUENCE /// ENTRY GNLJG3 #type complete TITLE HIV-1 retropepsin (EC 3.4.23.16) - simian immunodeficiency virus (macaque isolate) CONTAINS endonuclease (EC 3.1.-.-); retropepsin (EC 3.4.23.16); RNA-directed DNA polymerase (EC 2.7.7.49) ORGANISM #formal_name simian immunodeficiency virus, SIV DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 03-Jun-2002 ACCESSIONS B28887 REFERENCE A28887 !$#authors Chakrabarti, L.; Guyader, M.; Alizon, M.; Daniel, M.D.; !1Desrosiers, R.C.; Tiollais, P.; Sonigo, P. !$#journal Nature (1987) 328:543-547 !$#title Sequence of simian immunodeficiency virus from macaque and !1its relationship to other human and simian retroviruses. !$#cross-references MUID:87287230; PMID:3649576 !$#accession B28887 !'##molecule_type DNA !'##residues 1-1056 ##label CHA !'##cross-references GB:Y00277; GB:M16403; NID:g61730; PIDN:CAA68380.1; !1PID:g1335590 COMMENT Specific enzymatic cleavages may yield mature proteins !1including protease, reverse transcriptase, and endonuclease. !1However, exact cleavage sites are undetermined. GENETICS !$#gene pol CLASSIFICATION #superfamily pol polyprotein KEYWORDS aspartic proteinase; hydrolase; nucleotidyltransferase; !1polyprotein; reverse transcriptase FEATURE !$106-204 #product retropepsin #status predicted #label RTP\ !$130 #active_site Asp (shared with dimeric partner) !8#status predicted SUMMARY #length 1056 #molecular-weight 119742 #checksum 7749 SEQUENCE /// ENTRY GNLJG5 #type complete TITLE HIV-1 retropepsin (EC 3.4.23.16) - simian immunodeficiency virus (African green monkey isolate) CONTAINS endonuclease (EC 3.1.-.-); retropepsin (EC 3.4.23.16); RNA-directed DNA polymerase (EC 2.7.7.49) ORGANISM #formal_name simian immunodeficiency virus, SIV DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 03-Jun-2002 ACCESSIONS B28873 REFERENCE A28873 !$#authors Franchini, G.; Gurgo, C.; Guo, H.G.; Gallo, R.C.; Collalti, !1E.; Fargnoli, K.A.; Hall, L.F.; Wong-Staal, F.; Reitz Jr., !1M.S. !$#journal Nature (1987) 328:539-543 !$#title Sequence of simian immunodeficiency virus and its !1relationship to the human immunodeficiency viruses. !$#cross-references MUID:87287229; PMID:3497350 !$#accession B28873 !'##molecule_type DNA !'##residues 1-1054 ##label FRA !'##cross-references EMBL:M19499 COMMENT Specific enzymatic cleavages may yield mature proteins !1including protease, reverse transcriptase, and endonuclease. !1However, exact cleavage sites are undetermined. GENETICS !$#gene pol CLASSIFICATION #superfamily pol polyprotein KEYWORDS aspartic proteinase; hydrolase; nucleotidyltransferase; !1polyprotein; reverse transcriptase FEATURE !$106-204 #product retropepsin #status predicted #label RTP\ !$130 #active_site Asp (shared with dimeric partner) !8#status predicted SUMMARY #length 1054 #molecular-weight 120190 #checksum 9773 SEQUENCE /// ENTRY GNLJG4 #type complete TITLE HIV-1 retropepsin (EC 3.4.23.16) - simian immunodeficiency virus (African green monkey isolate) CONTAINS endonuclease (EC 3.1.-.-); retropepsin (EC 3.4.23.16); RNA-directed DNA polymerase (EC 2.7.7.49) ORGANISM #formal_name simian immunodeficiency virus, SIV DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 03-Jun-2002 ACCESSIONS B30045 REFERENCE A30045 !$#authors Fukasawa, M.; Miura, T.; Hasegawa, A.; Morikawa, S.; !1Tsujimoto, H.; Miki, K.; Kitamura, T.; Hayami, M. !$#journal Nature (1988) 333:457-461 !$#title Sequence of simian immunodeficiency virus from African green !1monkey, a new member of the HIV/SIV group. !$#cross-references MUID:88232906; PMID:3374586 !$#accession B30045 !'##molecule_type DNA !'##residues 1-1061 ##label FUK !'##cross-references EMBL:X07805; NID:g61748; PID:g1335593 COMMENT Specific enzymatic cleavages may yield mature proteins !1including protease, reverse transcriptase, and endonuclease. !1However, exact cleavage sites are undetermined. GENETICS !$#gene pol CLASSIFICATION #superfamily pol polyprotein KEYWORDS aspartic proteinase; hydrolase; nucleotidyltransferase; !1polyprotein; reverse transcriptase FEATURE !$111-210 #product retropepsin #status predicted #label RTP\ !$134 #active_site Asp (shared with dimeric partner) !8#status predicted SUMMARY #length 1061 #molecular-weight 120612 #checksum 1286 SEQUENCE /// ENTRY GNLJBT #type complete TITLE HIV-1 retropepsin (EC 3.4.23.16) - bovine immunodeficiency virus (isolate 127) CONTAINS endonuclease (EC 3.1.-.-); retropepsin (EC 3.4.23.16); RNA-directed DNA polymerase (EC 2.7.7.49) ORGANISM #formal_name bovine immunodeficiency virus DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 03-Jun-2002 ACCESSIONS B34742 REFERENCE A34742 !$#authors Garvey, K.J.; Oberste, M.S.; Elser, J.E.; Braun, M.J.; !1Gonda, M.A. !$#journal Virology (1990) 175:391-409 !$#title Nucleotide sequence and genome organization of biologically !1active proviruses of the bovine immunodeficiency-like virus. !$#cross-references MUID:90223985; PMID:2183467 !$#accession B34742 !'##molecule_type genomic RNA !'##residues 1-1053 ##label GAR !'##cross-references GB:M32690 COMMENT Specific enzymatic cleavages may yield mature proteins !1including protease, reverse transcriptase, and endonuclease. !1However, exact cleavage sites are undetermined. GENETICS !$#gene pol CLASSIFICATION #superfamily pol polyprotein KEYWORDS AIDS; aspartic proteinase; endonuclease; hydrolase; !1immunodeficiency; nucleotidyltransferase; polyprotein; !1reverse transcriptase FEATURE !$50-143 #product retropepsin #status predicted #label RTP\ !$144-774 #product RNA-directed DNA polymerase #status !8predicted #label REV\ !$775-1053 #product endonuclease #status predicted #label ENC\ !$75 #active_site Asp (shared with dimeric partner) !8#status predicted SUMMARY #length 1053 #molecular-weight 120658 #checksum 1471 SEQUENCE /// ENTRY B46335 #type complete TITLE HIV-1 retropepsin (EC 3.4.23.16) - Maedi/Visna virus (strain SA-OMVV) CONTAINS endonuclease (EC 3.1.-.-); retropepsin (EC 3.4.23.16); RNA-directed DNA polymerase (EC 2.7.7.49) ORGANISM #formal_name Maedi/Visna virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 03-Jun-2002 ACCESSIONS B46335 REFERENCE A46335 !$#authors Querat, G.; Audoly, G.; Sonigo, P.; Vigne, R. !$#journal Virology (1990) 175:434-447 !$#title Nucleotide sequence analysis of SA-OMVV, a visna-related !1ovine lentivirus: phylogenetic history of lentiviruses. !$#cross-references MUID:90223989; PMID:2158181 !$#accession B46335 !'##molecule_type DNA !'##residues 1-1086 ##label QUE !'##cross-references GB:M31646 COMMENT This protein is synthesized as a gag-pol polyprotein. COMMENT Specific enzymatic cleavages may yield mature proteins !1including proteinase, RNA-directed DNA polymerase, and !1endonuclease. However, exact cleavage sites are !1undetermined. GENETICS !$#gene pol CLASSIFICATION #superfamily pol polyprotein KEYWORDS AIDS; aspartic proteinase; endonuclease; hydrolase; !1immunodeficiency; nucleotidyltransferase; polyprotein; !1reverse transcriptase FEATURE !$20-120 #product retropepsin #status predicted #label RTP\ !$129-841 #product RNA-directed DNA polymerase #status !8predicted #label REV\ !$842-1086 #product endonuclease #status predicted #label ENC\ !$44 #active_site Asp (shared with dimeric partner) !8#status predicted SUMMARY #length 1086 #molecular-weight 124515 #checksum 1059 SEQUENCE /// ENTRY GNLJVS #type complete TITLE HIV-1 retropepsin (EC 3.4.23.16) - Maedi/Visna virus (strain 1514) CONTAINS endonuclease (EC 3.1.-.-); retropepsin (EC 3.4.23.16); RNA-directed DNA polymerase (EC 2.7.7.49) ORGANISM #formal_name Maedi/Visna virus #note host Homo sapiens (man) DATE 28-Feb-1986 #sequence_revision 31-Dec-1993 #text_change 03-Jun-2002 ACCESSIONS A03969 REFERENCE A90869 !$#authors Sonigo, P.; Alizon, M.; Staskus, K.; Klatzmann, D.; Cole, !1S.; Danos, O.; Retzel, E.; Tiollais, P.; Haase, A.; !1Wain-Hobson, S. !$#journal Cell (1985) 42:369-382 !$#title Nucleotide sequence of the visna lentivirus: relationship to !1the AIDS virus. !$#cross-references MUID:85254938; PMID:2410140 !$#accession A03969 !'##molecule_type DNA !'##residues 1-1101 ##label SON !'##cross-references GB:M10608 COMMENT Specific enzymatic cleavages may yield mature proteins !1including proteinase, RNA-directed DNA polymerase, and !1endonuclease. However, exact cleavage sites are !1undetermined. GENETICS !$#gene pol CLASSIFICATION #superfamily pol polyprotein KEYWORDS AIDS; aspartic proteinase; endonuclease; hydrolase; !1immunodeficiency; nucleotidyltransferase; polyprotein; !1reverse transcriptase FEATURE !$35-135 #product retropepsin #status predicted #label RTP\ !$144-856 #product RNA-directed DNA polymerase #status !8predicted #label REV\ !$857-1101 #product endonuclease #status predicted #label ENC\ !$59 #active_site Asp (shared with dimeric partner) !8#status predicted SUMMARY #length 1101 #molecular-weight 126152 #checksum 7118 SEQUENCE /// ENTRY B45390 #type complete TITLE HIV-1 retropepsin (EC 3.4.23.16) - Maedi/Visna virus (strain KV1772) (provirus) CONTAINS endonuclease (EC 3.1.-.-); retropepsin (EC 3.4.23.16); RNA-directed DNA polymerase (EC 2.7.7.49) ORGANISM #formal_name Maedi/Visna virus #note host Homo sapiens (man) DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 03-Jun-2002 ACCESSIONS B45390 REFERENCE A45390 !$#authors Andresson, O.S.; Elser, J.E.; Tobin, G.J.; Greenwood, J.D.; !1Gonda, M.A.; Georgsson, G.; Andresdottir, V.; !1Benediktsdottir, E.; Carlsdottir, H.M.; Maentylae, E.O.; !1Rafnar, B.; Palsson, P.A.; Casey, J.W.; Petursson, G. !$#journal Virology (1993) 193:89-105 !$#title Nucleotide sequence and biological properties of a !1pathogenic proviral molecular clone of neurovirulent visna !1virus. !$#cross-references MUID:93174981; PMID:8382414 !$#accession B45390 !'##molecule_type DNA !'##residues 1-1101 ##label AND !'##cross-references GB:S55323; NID:g265825; PIDN:AAB25460.1; !1PID:g265827 COMMENT Specific enzymatic cleavages may yield mature proteins !1including proteinase, RNA-directed DNA polymerase, and !1endonuclease. However, exact cleavage sites are !1undetermined. GENETICS !$#gene pol CLASSIFICATION #superfamily pol polyprotein KEYWORDS AIDS; aspartic proteinase; endonuclease; hydrolase; !1immunodeficiency; nucleotidyltransferase; polyprotein; !1reverse transcriptase FEATURE !$35-135 #product retropepsin #status predicted #label RTP\ !$144-856 #product RNA-directed DNA polymerase #status !8predicted #label REV\ !$857-1101 #product endonuclease #status predicted #label ENC\ !$59 #active_site Asp (shared with dimeric partner) !8#status predicted SUMMARY #length 1101 #molecular-weight 126178 #checksum 8167 SEQUENCE /// ENTRY B45345 #type complete TITLE HIV-1 retropepsin (EC 3.4.23.16) - caprine arthritis-encephalitis virus (strain CO) CONTAINS endonuclease (EC 3.1.-.-); retropepsin (EC 3.4.23.16); RNA-directed DNA polymerase (EC 2.7.7.49) ORGANISM #formal_name caprine arthritis-encephalitis virus, CAEV DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 03-Jun-2002 ACCESSIONS B45345 REFERENCE A45345 !$#authors Saltarelli, M.; Querat, G.; Konings, D.A.M.; Vigne, R.; !1Clements, J.E. !$#journal Virology (1990) 179:347-364 !$#title Nucleotide sequence and transcriptional analysis of !1molecular clones of CAEV which generate infectious virus. !$#cross-references MUID:91021037; PMID:2171210 !$#accession B45345 !'##molecule_type mRNA !'##residues 1-1109 ##label SAL !'##cross-references GB:M33677 COMMENT This protein may be synthesized as a gag-pol polyprotein. GENETICS !$#gene pol CLASSIFICATION #superfamily pol polyprotein KEYWORDS aspartic proteinase; endonuclease; hydrolase; !1nucleotidyltransferase; polyprotein; reverse transcriptase FEATURE !$44-144 #product retropepsin #status predicted #label RTP\ !$153-865 #product RNA-directed DNA polymerase #status !8predicted #label RDN\ !$866-1109 #product endonuclease #status predicted #label EDN\ !$68 #active_site Asp (shared with dimeric partner) !8#status predicted SUMMARY #length 1109 #molecular-weight 127678 #checksum 3760 SEQUENCE /// ENTRY GNLJFP #type complete TITLE HIV-1 retropepsin (EC 3.4.23.16) - feline immunodeficiency virus (strain Petaluma) CONTAINS endonuclease (EC 3.1.-.-); retropepsin (EC 3.4.23.16); RNA-directed DNA polymerase (EC 2.7.7.49) ORGANISM #formal_name feline immunodeficiency virus #note host Felis silvestris catus (domestic cat) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 03-Jun-2002 ACCESSIONS B33543 REFERENCE A33543 !$#authors Talbott, R.L.; Sparger, E.E.; Lovelace, K.M.; Fitch, W.M.; !1Pedersen, N.C.; Luciw, P.A.; Elder, J.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:5743-5747 !$#title Nucleotide sequence and genomic organization of feline !1immunodeficiency virus. !$#cross-references MUID:89345543; PMID:2762293 !$#accession B33543 !'##molecule_type DNA !'##residues 1-1124 ##label TAL COMMENT Specific enzymatic cleavages may yield mature proteins !1including protease, reverse transcriptase, and endonuclease. !1However, exact cleavage sites are undetermined. GENETICS !$#gene pol CLASSIFICATION #superfamily pol polyprotein KEYWORDS AIDS; aspartic proteinase; endonuclease; hydrolase; !1immunodeficiency; nucleotidyltransferase; polyprotein; !1reverse transcriptase FEATURE !$44-154 #product retropepsin #status predicted #label RTP\ !$157-715 #product RNA-directed DNA polymerase #status !8predicted #label REV\ !$847-1124 #product endonuclease #status predicted #label ENS\ !$68 #active_site Asp (shared with dimeric partner) !8#status predicted SUMMARY #length 1124 #molecular-weight 127493 #checksum 6111 SEQUENCE /// ENTRY GNLJEV #type complete TITLE HIV-1 retropepsin (EC 3.4.23.16) - equine infectious anemia virus CONTAINS endonuclease (EC 3.1.-.-); retropepsin (EC 3.4.23.16); RNA-directed DNA polymerase (EC 2.7.7.49) ORGANISM #formal_name equine infectious anemia virus #note host (horse) DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 03-Jun-2002 ACCESSIONS A03970 REFERENCE A03949 !$#authors Stephens, R.M.; Casey, J.W.; Rice, N.R. !$#journal Science (1986) 231:589-594 !$#title Equine infectious anemia virus gag and pol genes: !1relatedness to visna and AIDS virus. !$#cross-references MUID:86122873; PMID:3003905 !$#accession A03970 !'##molecule_type DNA !'##residues 1-1145 ##label STE GENETICS !$#gene pol CLASSIFICATION #superfamily pol polyprotein KEYWORDS AIDS; aspartic proteinase; endonuclease; hydrolase; !1immunodeficiency; nucleotidyltransferase; polyprotein; !1reverse transcriptase FEATURE !$81-184 #product retropepsin #status predicted #label RTP\ !$196-913 #product RNA-directed DNA polymerase #status !8predicted #label REV\ !$914-1145 #product endonuclease #status predicted #label EDS\ !$105 #active_site Asp (shared with dimeric partner) !8#status predicted SUMMARY #length 1145 #molecular-weight 129519 #checksum 8855 SEQUENCE /// ENTRY GNLJEW #type complete TITLE HIV-1 retropepsin (EC 3.4.23.16) - equine infectious anemia virus CONTAINS endonuclease; retropepsin (EC 3.4.23.16); reverse transcriptase ORGANISM #formal_name equine infectious anemia virus #note host Equus caballus (domestic horse) DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 03-Jun-2002 ACCESSIONS B27842 REFERENCE A27842 !$#authors Kawakami, T.; Sherman, L.; Dahlberg, J.; Gazit, A.; Yaniv, !1A.; Tronick, S.R.; Aaronson, S.A. !$#journal Virology (1987) 158:300-312 !$#title Nucleotide sequence analysis of equine infectious anemia !1virus proviral DNA. !$#cross-references MUID:87236196; PMID:3035786 !$#accession B27842 !'##molecule_type DNA !'##residues 1-1146 ##label KAW !'##cross-references GB:M16575; NID:g323836 GENETICS !$#gene pol CLASSIFICATION #superfamily pol polyprotein KEYWORDS aspartic proteinase; endonuclease; hydrolase; polyprotein; !1reverse transcriptase FEATURE !$81-184 #product retropepsin #status predicted #label RTP\ !$196-914 #product RNA-directed DNA polymerase #status !8predicted #label REV\ !$915-1146 #product endonuclease #status predicted #label END\ !$105 #active_site Asp (shared with dimeric partner) !8#status predicted SUMMARY #length 1146 #molecular-weight 129509 #checksum 6341 SEQUENCE /// ENTRY GNLJ22 #type complete TITLE HIV-1 retropepsin (EC 3.4.23.16) - equine infectious anemia virus (strain CL22) CONTAINS endonuclease (EC 3.1.-.-); retropepsin (EC 3.4.23.16); RNA-directed DNA polymerase (EC 2.7.7.49) ORGANISM #formal_name equine infectious anemia virus #note host Equus caballus (domestic horse) DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 03-Jun-2002 ACCESSIONS B41991 REFERENCE A41991 !$#authors Perry, S.T.; Flaherty, M.T.; Kelley, M.J.; Clabough, D.L.; !1Tronick, S.R.; Coggins, L.; Whetter, L.; Lengel, C.R.; !1Fuller, F. !$#journal J. Virol. (1992) 66:4085-4097 !$#title The surface envelope protein gene region of equine !1infectious anemia virus is not an important determinant of !1tropism in vitro. !$#cross-references MUID:92292230; PMID:1318398 !$#accession B41991 !'##molecule_type DNA !'##residues 1-1146 ##label PER !'##cross-references GB:M87581 GENETICS !$#gene pol !$#start_codon ACA CLASSIFICATION #superfamily pol polyprotein KEYWORDS aspartic proteinase; endonuclease; hydrolase; !1nucleotidyltransferase; polyprotein; reverse transcriptase FEATURE !$81-184 #product retropepsin #status predicted #label RTP\ !$196-914 #product RNA-directed DNA polymerase #status !8predicted #label REV\ !$915-1146 #product endonuclease #status predicted #label END\ !$105 #active_site Asp (shared with dimeric partner) !8#status predicted SUMMARY #length 1146 #molecular-weight 129508 #checksum 6671 SEQUENCE /// ENTRY GNLJSP #type complete TITLE pol polyprotein - human foamy virus ORGANISM #formal_name human foamy virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS A93033; A91074; A29685; B28880 REFERENCE A93033 !$#authors Maurer, B.; Bannert, H.; Darai, G.; Fluegel, R.M. !$#journal J. Virol. (1988) 62:1590-1597 !$#title Analysis of the primary structure of the long terminal !1repeat and the gag and pol genes of the human !1spumaretrovirus. !$#cross-references MUID:88188241; PMID:2451755 !$#accession A93033 !'##molecule_type genomic RNA !'##residues 1-545 ##label RSA !'##cross-references GB:M19427; NID:g330974; PIDN:AAA66556.1; !1PID:g808677 REFERENCE A91074 !$#authors Fluegel, R.M.; Rethwilm, A.; Maurer, B.; Darai, G. !$#journal EMBO J. (1987) 6:2077-2084 !$#title Nucleotide sequence analysis of the env gene and its !1flanking regions of the human spumaretrovirus reveals two !1novel genes. !$#cross-references MUID:88004420; PMID:2820721 !$#accession A91074 !'##molecule_type genomic RNA !'##residues 544-886 ##label RSB GENETICS !$#gene pol CLASSIFICATION #superfamily pol polyprotein KEYWORDS polyprotein; reverse transcriptase SUMMARY #length 886 #molecular-weight 100359 #checksum 4387 SEQUENCE /// ENTRY GNLJLK #type complete TITLE pol polyprotein - simian foamy virus (type 3, strain LK3) CONTAINS proteinase (EC 3.4.-.-); RNA-directed DNA polymerase (EC 2.7.7.49) ORGANISM #formal_name simian foamy virus #note host (African green monkey) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS B40820 REFERENCE A40820 !$#authors Renne, R.; Friedl, E.; Schweizer, M.; Fleps, U.; Turek, R.; !1Neumann-Haefelin, D. !$#journal Virology (1992) 186:597-608 !$#title Genomic organization and expression of simian foamy virus !1type 3 (SFV-3). !$#cross-references MUID:92124734; PMID:1310187 !$#accession B40820 !'##molecule_type DNA !'##residues 1-1157 ##label REN !'##cross-references GB:M74895; NID:g334870; PIDN:AAA47796.1; !1PID:g334872 COMMENT This polyprotein is probably synthesized as a gag-pol !1polyprotein by a +1 frameshift. GENETICS !$#gene pol CLASSIFICATION #superfamily pol polyprotein KEYWORDS hydrolase; nucleotidyltransferase; polyprotein SUMMARY #length 1157 #molecular-weight 131224 #checksum 3436 SEQUENCE /// ENTRY GNFF17 #type complete TITLE retrovirus-related pol polyprotein - fruit fly (Drosophila melanogaster) retrotransposon 17.6 ALTERNATE_NAMES reverse transcriptase ORGANISM #formal_name Drosophila melanogaster DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 16-Jun-2000 ACCESSIONS A03971 REFERENCE A93349 !$#authors Saigo, K.; Kugimiya, W.; Matsuo, Y.; Inouye, S.; Yoshioka, !1K.; Yuki, S. !$#journal Nature (1984) 312:659-661 !$#title Identification of the coding sequence for a reverse !1transcriptase-like enzyme in a transposable genetic element !1in Drosophila melanogaster. !$#cross-references MUID:85061628; PMID:6209583 !$#accession A03971 !'##molecule_type DNA !'##residues 1-1058 ##label SAI !'##cross-references GB:X01472; GB:J01060; GB:J01061; NID:g8142; !1PIDN:CAA25702.1; PID:g1335613 GENETICS !$#gene FlyBase:17.6 !'##cross-references FlyBase:FBgn0000004 CLASSIFICATION #superfamily pol polyprotein KEYWORDS polyprotein; reverse transcriptase SUMMARY #length 1058 #molecular-weight 122697 #checksum 3902 SEQUENCE /// ENTRY GNFFG1 #type complete TITLE HIV-1 retropepsin (EC 3.4.23.16) - fruit fly (Drosophila melanogaster) retrotransposon gypsy CONTAINS retropepsin (EC 3.4.23.16) ORGANISM #formal_name Drosophila melanogaster DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 03-Jun-2002 ACCESSIONS B25666; A23769 REFERENCE A93071 !$#authors Marlor, R.L.; Parkhurst, S.M.; Corces, V.G. !$#journal Mol. Cell. Biol. (1986) 6:1129-1134 !$#title The Drosophila melanogaster gypsy transposable element !1encodes putative gene products homologous to retroviral !1proteins. !$#cross-references MUID:87064379; PMID:3023871 !$#accession B25666 !'##molecule_type DNA !'##residues 1-1035 ##label MAR !'##note the authors translated the codons CAG for residue 99 and CAA !1for residue 710 as Glu REFERENCE A23769 !$#authors Yuki, S.; Ishimaru, S.; Inouye, S.; Saigo, K. !$#journal Nucleic Acids Res. (1986) 14:3017-3030 !$#title Identification of genes for reverse transcriptase-like !1enzymes in two Drosophila retrotransposons, 412 and gypsy; a !1rapid detection method of reverse transcriptase genes using !1YXDD box probes. !$#cross-references MUID:86176782; PMID:2421255 !$#accession A23769 !'##molecule_type DNA !'##residues 21-30,'AR',33-59,'R',61-231,'S',233-489,'V',491-882,'T', !1884-922,'S',924-946,'NQLR' ##label YUK !'##cross-references GB:X03734; NID:g8036; PIDN:CAA27371.1; PID:g929567 GENETICS !$#gene FlyBase:gypsy/pol !'##cross-references FlyBase:FBgn0014966 CLASSIFICATION #superfamily pol polyprotein KEYWORDS aspartic proteinase; hydrolase; polyprotein; reverse !1transcriptase FEATURE !$5-106 #product retropepsin #status predicted #label RTP\ !$29 #active_site Asp (shared with dimeric partner) !8#status predicted SUMMARY #length 1035 #molecular-weight 117817 #checksum 4114 SEQUENCE /// ENTRY GNFF42 #type complete TITLE HIV-1 retropepsin (EC 3.4.23.16) - fruit fly (Drosophila melanogaster) retrotransposon 412 CONTAINS retropepsin (EC 3.4.23.16) ORGANISM #formal_name Drosophila melanogaster DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 03-Jun-2002 ACCESSIONS D29349 REFERENCE A91171 !$#authors Yuki, S.; Inouye, S.; Ishimaru, S.; Saigo, K. !$#journal Eur. J. Biochem. (1986) 158:403-410 !$#title Nucleotide sequence characterization of a Drosophila !1retrotransposon, 412. !$#cross-references MUID:86274717; PMID:2426108 !$#accession D29349 !'##molecule_type DNA !'##residues 1-1237 ##label YUK !'##cross-references GB:X04132; GB:X03733; NID:g8500; PIDN:CAA27750.1; !1PID:g1335652 !'##note the authors translated the codon CAA for residue 21 as Lys GENETICS !$#gene FlyBase:412 !'##cross-references FlyBase:FBgn0000006 CLASSIFICATION #superfamily pol polyprotein KEYWORDS aspartic proteinase; hydrolase; polyprotein; reverse !1transcriptase FEATURE !$39-133 #product retropepsin #status predicted #label RTP\ !$63 #active_site Asp (shared with dimeric partner) !8#status predicted SUMMARY #length 1237 #molecular-weight 143041 #checksum 6456 SEQUENCE /// ENTRY GNMSLL #type complete TITLE retrovirus-related reverse transcriptase homolog - mouse retrotransposon ALTERNATE_NAMES L1Md repetitive element ORF-2; LINE-1 hypothetical protein; ORF 3900; pol polyprotein homolog ORGANISM #formal_name Mus musculus #common_name house mouse DATE 31-Mar-1989 #sequence_revision 08-Jan-1999 #text_change 16-Jun-2000 ACCESSIONS B58927; B24906; I49130; A23772; B23430 REFERENCE A93072 !$#authors Loeb, D.D.; Padgett, R.W.; Hardies, S.C.; Shehee, W.R.; !1Comer, M.B.; Edgell, M.H.; Hutchison III, C.A. !$#journal Mol. Cell. Biol. (1986) 6:168-182 !$#title The sequence of a large L1Md element reveals a tandemly !1repeated 5' end and several features found in !1retrotransposons. !$#cross-references MUID:87064284; PMID:3023821 !$#accession B58927 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-1281 ##label LOE1 !'##cross-references GB:M13002; NID:g200849; PIDN:AAA66024.1; !1PID:g804788 !'##note sequence constructed using the first potential start codon for !1ORF2 !$#accession B24906 !'##molecule_type DNA !'##residues 'NNQESNHSTNQKEDSHKNR',1-1281 ##label LOE2 !'##cross-references GB:M13002; NID:g200849 !'##note sequence shown in Fig. 2 REFERENCE I49129 !$#authors Martin, S.L.; Martin, S.L. !$#journal Gene (1995) 153:261-266 !$#title Characterization of a LINE-1 cDNA that originated from RNA !1present in ribonucleoprotein particles: implications for the !1structure of an active mouse LINE-1. !$#cross-references MUID:95180729; PMID:7533116 !$#accession I49130 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-85,'L',87-358,'K',360-706,'F',708-735,'A',737-760,'W', !1762-927,'D',929-1281 ##label RES !'##cross-references EMBL:U15647; NID:g558906; PIDN:AAA67727.1; !1PID:g558908 REFERENCE A23772 !$#authors Mottez, E.; Rogan, P.K.; Manuelidis, L. !$#journal Nucleic Acids Res. (1986) 14:3119-3136 !$#title Conservation in the 5' region of the long interspersed mouse !1L1 repeat: implications of comparative sequence analysis. !$#cross-references MUID:86176789; PMID:3008107 !$#accession A23772 !'##molecule_type DNA !'##residues 'NNQESNHSTNQKEDSHKNR',1-245,'K',247-423,'SYTQQNWKTWTKWTN', !1439,'WTDTRYQS' ##label MOT !'##cross-references GB:X03725; NID:g52829; PIDN:CAA27363.1; !1PID:g1334115 CLASSIFICATION #superfamily pol polyprotein KEYWORDS reverse transcriptase SUMMARY #length 1281 #molecular-weight 149579 #checksum 8097 SEQUENCE /// ENTRY RROBHM #type complete TITLE RNA-directed DNA polymerase homolog - evening primrose mitochondrion ALTERNATE_NAMES reverse transcriptase homolog ORGANISM #formal_name mitochondrion Oenothera villaricae #common_name evening primrose DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS S01101 REFERENCE S01101 !$#authors Schuster, W.; Brennicke, A. !$#journal EMBO J. (1987) 6:2857-2863 !$#title Plastid, nuclear and reverse transcriptase sequences in the !1mitochondrial genome of Oenothera: is genetic information !1transferred between organelles via RNA? !$#accession S01101 !'##molecule_type DNA !'##residues 1-142 ##label SCH !'##cross-references EMBL:X06034; NID:g13196; PIDN:CAA29429.1; !1PID:g13197 !'##note the authors translated the codon CGG for residue 48 as Trp, !1assuming a special genetic code for plant mitochondria GENETICS !$#genome mitochondrion CLASSIFICATION #superfamily RNA-directed DNA polymerase homolog KEYWORDS mitochondrion SUMMARY #length 142 #molecular-weight 16799 #checksum 6914 SEQUENCE /// ENTRY VCMSIA #type complete TITLE env polyprotein precursor - mouse intracisternal A-particle MIAE ALTERNATE_NAMES coat polyprotein CONTAINS surface protein; transmembrane protein ORGANISM #formal_name mouse intracisternal A-particle MIAE #note host Mus musculus (house mouse) DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 01-Mar-1996 ACCESSIONS A41305 REFERENCE A41305 !$#authors Reuss, F.U.; Schaller, H.C. !$#journal J. Virol. (1991) 65:5702-5709 !$#title cDNA sequence and genomic characterization of intracisternal !1A-particle-related retroviral elements containing an !1envelope gene. !$#cross-references MUID:92015460; PMID:1920613 !$#accession A41305 !'##molecule_type mRNA !'##residues 1-584 ##label REU !'##cross-references GB:M73818 !'##note readthrough of three terminators occurs: UGA between codons for !171-Thr and 72-Ala, UGA between codons for 111-His and !1112-Arg, and UAA between codons for 394-Val and 395-Ser COMMENT This particle is a defective retrovirus. GENETICS !$#gene env CLASSIFICATION #superfamily intracisternal A-particle env polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; transmembrane !1protein FEATURE !$1-526 #domain extracellular #status predicted #label EXT\ !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-584 #product env polyprotein #status predicted #label !8ENV\ !$26-362 #product surface protein #status predicted #label !8SUP\ !$26-362 #region hydrophilic #status predicted\ !$359-362 #region cleavage processing #status predicted\ !$363-584 #product transmembrane protein #status predicted !8#label TMP\ !$364-392 #region hydrophobic #status predicted\ !$527-547 #domain transmembrane #status predicted #label TM1\ !$548-584 #domain intracellular #status predicted #label INT\ !$19,58,77,98,129, !$140,147,230,276, !$285,311,319,463, !$469,481,501 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 584 #molecular-weight 65024 #checksum 3351 SEQUENCE /// ENTRY VCMVM #type complete TITLE env polyprotein - mouse mammary tumor virus (strain GR) CONTAINS coat protein gp36; coat protein gp52 ORGANISM #formal_name mouse mammary tumor virus, MMTV DATE 18-Apr-1984 #sequence_revision 18-Apr-1984 #text_change 04-Dec-1994 ACCESSIONS A03972 REFERENCE A03972 !$#authors Redmond, S.M.S.; Dickson, C. !$#journal EMBO J. (1983) 2:125-131 !$#title Sequence and expression of the mouse mammary tumour virus !1env gene. !$#accession A03972 !'##molecule_type DNA !'##residues 1-688 ##label RED GENETICS !$#gene env CLASSIFICATION #superfamily type A retrovirus env polyprotein KEYWORDS coat protein; glycoprotein; polyprotein FEATURE !$1-98 #domain leader peptide #status predicted #label LPT\ !$99-474 #product coat protein gp52 #status predicted #label !8GP1\ !$475-688 #product coat protein gp36 #status predicted #label !8GP2\ !$127,143,297,498,557 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 688 #molecular-weight 77220 #checksum 8999 SEQUENCE /// ENTRY VCMVMM #type complete TITLE env polyprotein - mouse mammary tumor virus CONTAINS coat protein gp36; coat protein gp52 ORGANISM #formal_name mouse mammary tumor virus, MMTV DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 16-Jul-1999 ACCESSIONS D26795 REFERENCE A93030 !$#authors Moore, R.; Dixon, M.; Smith, R.; Peters, G.; Dickson, C. !$#journal J. Virol. (1987) 61:480-490 !$#title Complete nucleotide sequence of a milk-transmitted mouse !1mammary tumor virus: two frameshift suppression events are !1required for translation of gag and pol. !$#cross-references MUID:87112944; PMID:3027377 !$#accession D26795 !'##molecule_type DNA !'##residues 1-688 ##label MOO !'##cross-references EMBL:M15122; NID:g332127; PIDN:AAA46544.1; !1PID:g332131 GENETICS !$#gene env CLASSIFICATION #superfamily type A retrovirus env polyprotein KEYWORDS coat protein; glycoprotein; polyprotein FEATURE !$1-97 #domain leader peptide #status predicted #label LPT\ !$98-456 #product coat protein gp52 #status predicted #label !8GP1\ !$457-688 #product coat protein gp36 #status predicted #label !8GP2\ !$127,143,297,498,557 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 688 #molecular-weight 77176 #checksum 1478 SEQUENCE /// ENTRY VCMVJA #type complete TITLE env polyprotein precursor - sheep pulmonary adenomatosis virus ALTERNATE_NAMES coat polyprotein CONTAINS coat protein gp36; coat protein gp52 ORGANISM #formal_name sheep pulmonary adenomatosis virus DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS E42740 REFERENCE A42740 !$#authors York, D.F.; Vigne, R.; Verwoerd, D.W.; Querat, G. !$#journal J. Virol. (1992) 66:4930-4939 !$#title Nucleotide sequence of the jaagsiekte retrovirus, an !1exogenous and endogenous type D and B retrovirus of sheep !1and goats. !$#cross-references MUID:92333675; PMID:1629959 !$#accession E42740 !'##molecule_type genomic RNA !'##residues 1-615 ##label YOR !'##cross-references GB:M80216; NID:g331338; PIDN:AAA89184.1; !1PID:g331342 GENETICS !$#gene env CLASSIFICATION #superfamily type A retrovirus env polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; transmembrane !1protein FEATURE !$1-79 #domain signal sequence #status predicted #label SIG\ !$80-378 #product coat protein gp52 #status predicted #label !8CP1\ !$379-615 #product coat protein gp36 #status predicted #label !8CP2\ !$379-402 #domain transmembrane #status predicted #label TM1\ !$403-615 #domain intracellular #status predicted #label INT\ !$555-571 #domain transmembrane #status predicted #label TM2\ !$108,127,178,219,275 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 615 #molecular-weight 69343 #checksum 8020 SEQUENCE /// ENTRY VCFFGY #type complete TITLE retrovirus-related env polyprotein homolog - fruit fly (Drosophila melanogaster) retrotransposon gypsy ORGANISM #formal_name Drosophila melanogaster DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 22-Jan-1999 ACCESSIONS C25666 REFERENCE A93071 !$#authors Marlor, R.L.; Parkhurst, S.M.; Corces, V.G. !$#journal Mol. Cell. Biol. (1986) 6:1129-1134 !$#title The Drosophila melanogaster gypsy transposable element !1encodes putative gene products homologous to retroviral !1proteins. !$#cross-references MUID:87064379; PMID:3023871 !$#accession C25666 !'##molecule_type DNA !'##residues 1-509 ##label MAR COMMENT The DNA sequence was obtained from GenBank, release 54.0. GENETICS !$#gene FlyBase:gypsy/env !'##cross-references FlyBase:FBgn0014964 CLASSIFICATION #superfamily fruit fly env polyprotein KEYWORDS coat protein; polyprotein SUMMARY #length 509 #molecular-weight 56852 #checksum 2927 SEQUENCE /// ENTRY VCLJFP #type complete TITLE env polyprotein precursor - feline immunodeficiency virus (strain Petaluma) ALTERNATE_NAMES coat polyprotein CONTAINS surface glycoprotein; transmembrane glycoprotein ORGANISM #formal_name feline immunodeficiency virus #note host Felis silvestris catus (domestic cat) DATE 31-Dec-1990 #sequence_revision 31-Dec-1993 #text_change 09-Sep-1994 ACCESSIONS D33543 REFERENCE A33543 !$#authors Talbott, R.L.; Sparger, E.E.; Lovelace, K.M.; Fitch, W.M.; !1Pedersen, N.C.; Luciw, P.A.; Elder, J.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:5743-5747 !$#title Nucleotide sequence and genomic organization of feline !1immunodeficiency virus. !$#cross-references MUID:89345543; PMID:2762293 !$#accession D33543 !'##molecule_type DNA !'##residues 1-856 ##label TAL !'##cross-references GB:M25381 COMMENT This protein lacks an N-terminal signal sequence, and one of !1the three internal hydrophobic regions may serve this !1function. GENETICS !$#gene env CLASSIFICATION #superfamily feline immunodeficiency virus env polyprotein KEYWORDS capsid protein; coat protein; glycoprotein; polyprotein; !1transmembrane protein FEATURE !$1-611 #product surface glycoprotein #status predicted !8#label SGP\ !$95-111 #region hydrophobic\ !$151-169 #region hydrophobic\ !$612-856 #product transmembrane glycoprotein #status predicted !8#label TGP\ !$616-640 #region hydrophobic\ !$786-812 #domain transmembrane #status predicted #label TMN\ !$220,258,269,274, !$298,330,336,342, !$418,422,448,481, !$499,518,531,548, !$551,717,721,729,737 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 856 #molecular-weight 97941 #checksum 5474 SEQUENCE /// ENTRY A45394 #type complete TITLE env polyprotein precursor - feline immunodeficiency virus (strain UT-113) ALTERNATE_NAMES coat polyprotein CONTAINS surface glycoprotein; transmembrane glycoprotein ORGANISM #formal_name feline immunodeficiency virus #note host Felis silvestris catus (domestic cat) DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS A45394; S16030 REFERENCE A45394 !$#authors Verschoor, E.J.; Hulskotte, E.G.J.; Ederveen, J.; Koolen, !1M.J.M.; Horzinek, M.C.; Rottier, P.J.M. !$#journal Virology (1993) 193:433-438 !$#title Post-translational processing of the feline immunodeficiency !1virus envelope precursor protein. !$#cross-references MUID:93174954; PMID:8382405 !$#accession A45394 !'##molecule_type mRNA !'##residues 1-856 ##label VER !'##cross-references EMBL:X60725; NID:g1092; PIDN:CAA43131.1; PID:g1093 COMMENT This protein lacks an N-terminal signal sequence, and one of !1the three internal hydrophobic regions may serve this !1function. GENETICS !$#gene env CLASSIFICATION #superfamily feline immunodeficiency virus env polyprotein KEYWORDS capsid protein; coat protein; glycoprotein; polyprotein; !1transmembrane protein FEATURE !$1-611 #product surface glycoprotein #status predicted !8#label SGP\ !$95-111 #region hydrophobic\ !$151-169 #region hydrophobic\ !$612-856 #product transmembrane glycoprotein #status predicted !8#label TGP\ !$616-640 #region hydrophobic\ !$786-812 #domain transmembrane #status predicted #label TMN\ !$220,258,269,274, !$298,330,336,342, !$418,422,448,469, !$481,499,518,531, !$548,551,556,717, !$721,729,737 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 856 #molecular-weight 98475 #checksum 7620 SEQUENCE /// ENTRY JQ2003 #type complete TITLE env polyprotein - feline immunodeficiency virus (strain UK2) ALTERNATE_NAMES coat polyprotein CONTAINS surface glycoprotein; transmembrane glycoprotein ORGANISM #formal_name feline immunodeficiency virus #note host Felis silvestris catus (domestic cat) DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS JQ2003; S29954 REFERENCE JQ2003 !$#authors Rigby, M.A.; Holmes, E.C.; Pistello, M.; Mackay, A.; Brown, !1A.J.L.; Neil, J.C. !$#journal J. Gen. Virol. (1993) 74:425-436 !$#title Evolution of structural proteins of feline immunodeficiency !1virus: Molecular epidemiology and evidence of selection for !1change. !$#cross-references MUID:93187604; PMID:8383177 !$#accession JQ2003 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-855 ##label RIG !'##cross-references GB:X69494; NID:g59267; PIDN:CAA49248.1; PID:g59268 GENETICS !$#gene env CLASSIFICATION #superfamily feline immunodeficiency virus env polyprotein KEYWORDS capsid protein; coat protein; glycoprotein; polyprotein; !1transmembrane protein FEATURE !$1-610 #product surface glycoprotein #status predicted !8#label SPR\ !$95-111 #region hydrophobic\ !$151-178 #region hydrophobic\ !$611-855 #product transmembrane glycoprotein #status predicted !8#label TMP\ !$611-648 #region hydrophobic\ !$786-802 #domain transmembrane #status predicted #label TMN\ !$258,269,274,298, !$418,548,551,716, !$720,728,736 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 855 #molecular-weight 98373 #checksum 4101 SEQUENCE /// ENTRY JQ2004 #type complete TITLE env polyprotein - feline immunodeficiency virus (strain UK8) ALTERNATE_NAMES coat polyprotein CONTAINS surface glycoprotein; transmembrane glycoprotein ORGANISM #formal_name feline immunodeficiency virus #note host Felis silvestris catus (domestic cat) DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 07-May-1999 ACCESSIONS JQ2004 REFERENCE JQ2003 !$#authors Rigby, M.A.; Holmes, E.C.; Pistello, M.; Mackay, A.; Brown, !1A.J.L.; Neil, J.C. !$#journal J. Gen. Virol. (1993) 74:425-436 !$#title Evolution of structural proteins of feline immunodeficiency !1virus: Molecular epidemiology and evidence of selection for !1change. !$#cross-references MUID:93187604; PMID:8383177 !$#accession JQ2004 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-855 ##label RIG !'##cross-references GB:X69496 GENETICS !$#gene env CLASSIFICATION #superfamily feline immunodeficiency virus env polyprotein KEYWORDS capsid protein; coat protein; glycoprotein; polyprotein; !1transmembrane protein FEATURE !$1-610 #product surface glycoprotein #status predicted !8#label SPR\ !$95-111 #region hydrophobic\ !$151-172 #region hydrophobic\ !$611-855 #product transmembrane glycoprotein #status predicted !8#label TMP\ !$611-648 #region hydrophobic\ !$786-802 #domain transmembrane #status predicted #label TMN\ !$258,269,274,298, !$418,548,551,716, !$720,728,736 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 855 #molecular-weight 97810 #checksum 9530 SEQUENCE /// ENTRY VCLJH3 #type complete TITLE env polyprotein precursor - human immunodeficiency virus type 1 (isolate HTLV-III, BH10) ALTERNATE_NAMES coat polyprotein ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 #note host Homo sapiens (man) DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 16-Jul-1999 ACCESSIONS A03973 REFERENCE A93353 !$#authors Ratner, L.; Haseltine, W.; Patarca, R.; Livak, K.J.; !1Starcich, B.; Josephs, S.F.; Doran, E.R.; Rafalski, J.A.; !1Whitehorn, E.A.; Baumeister, K.; Ivanoff, L.; Petteway Jr., !1S.R.; Pearson, M.L.; Lautenberger, J.A.; Papas, T.S.; !1Ghrayeb, J.; Chang, N.T.; Gallo, R.C.; Wong-Staal, F. !$#journal Nature (1985) 313:277-284 !$#title Complete nucleotide sequence of the AIDS virus, HTLV-III. !$#cross-references MUID:85111123; PMID:2578615 !$#accession A03973 !'##molecule_type DNA !'##residues 1-856 ##label RAT !'##cross-references GB:M15654; GB:K02008; GB:K02009; GB:K02010; !1NID:g326383; PIDN:AAA44205.1; PID:g326392 GENETICS !$#gene env CLASSIFICATION #superfamily type E retrovirus env polyprotein KEYWORDS AIDS; capsid protein; coat protein; glycoprotein; !1immunodeficiency; polyprotein; transmembrane protein FEATURE !$1-30 #domain signal sequence #status predicted #label SIG\ !$31-511 #product exterior membrane glycoprotein #status !8predicted #label EXT\ !$512-856 #product transmembrane glycoprotein #status predicted !8#label TMM\ !$88,136,141,156,160, !$186,197,230,234, !$241,262,276,289, !$295,301,332,339, !$356,386,392,397, !$406,448,463 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$611,616,625,637, !$674,750,816 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 856 #molecular-weight 97224 #checksum 8008 SEQUENCE /// ENTRY VCLJVL #type complete TITLE env polyprotein precursor - human immunodeficiency virus type 1 (isolate LV) ALTERNATE_NAMES coat polyprotein ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 #note host Homo sapiens (man) DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 16-Jul-1999 ACCESSIONS A03974 REFERENCE A93355 !$#authors Muesing, M.A.; Smith, D.H.; Cabradilla, C.D.; Benton, C.V.; !1Lasky, L.A.; Capon, D.J. !$#journal Nature (1985) 313:450-458 !$#title Nucleic acid structure and expression of the human AIDS/ !1lymphadenopathy retrovirus. !$#cross-references MUID:85111157; PMID:2982104 !$#accession A03974 !'##molecule_type DNA !'##residues 1-856 ##label MUE !'##cross-references GB:K02083; NID:g555008; PIDN:AAB59873.1; !1PID:g328559 GENETICS !$#gene env CLASSIFICATION #superfamily type E retrovirus env polyprotein KEYWORDS AIDS; capsid protein; coat protein; glycoprotein; !1immunodeficiency; polyprotein; transmembrane protein FEATURE !$1-30 #domain signal sequence #status predicted #label SIG\ !$31-511 #product exterior membrane glycoprotein #status !8predicted #label EXT\ !$512-856 #product transmembrane glycoprotein #status predicted !8#label TMM\ !$88,136,141,156,160, !$186,197,230,234, !$241,262,276,289, !$295,301,332,339, !$356,386,392,397, !$406,448,463 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$611,616,625,637, !$674,750,816 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 856 #molecular-weight 97339 #checksum 7968 SEQUENCE /// ENTRY VCLJLV #type complete TITLE env polyprotein precursor - human immunodeficiency virus type 1 (isolate LAV-1a) ALTERNATE_NAMES coat polyprotein ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 #note host Homo sapiens (man) DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 16-Jul-1999 ACCESSIONS A03975 REFERENCE A90866 !$#authors Wain-Hobson, S.; Sonigo, P.; Danos, O.; Cole, S.; Alizon, M. !$#journal Cell (1985) 40:9-17 !$#title Nucleotide sequence of the AIDS virus, LAV. !$#cross-references MUID:85099333; PMID:2981635 !$#accession A03975 !'##molecule_type DNA !'##residues 1-861 ##label WAI !'##cross-references GB:K02013; NID:g326417; PIDN:AAB59751.1; !1PID:g326424 GENETICS !$#gene env CLASSIFICATION #superfamily type E retrovirus env polyprotein KEYWORDS AIDS; capsid protein; coat protein; glycoprotein; !1immunodeficiency; polyprotein; transmembrane protein FEATURE !$1-30 #domain signal sequence #status predicted #label SIG\ !$31-516 #product exterior membrane glycoprotein #status !8predicted #label EXT\ !$517-861 #product transmembrane glycoprotein #status predicted !8#label TMM\ !$88,136,141,146,161, !$165,191,202,239, !$246,267,281,294, !$300,306,337,344, !$361,391,397,402, !$411,453,468 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$616,621,630,642, !$679,755,821 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 861 #molecular-weight 97487 #checksum 5733 SEQUENCE /// ENTRY H44001 #type complete TITLE env polyprotein precursor - human immunodeficiency virus type 1 (strain YU-2) ALTERNATE_NAMES coat polyprotein CONTAINS coat protein gp120; coat protein gp41 ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 #note host Homo sapiens (man) DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 09-Sep-1994 ACCESSIONS H44001 REFERENCE A44001 !$#authors Li, Y.; Hui, H.; Burgess, C.J.; Price, R.W.; Sharp, P.M.; !1Hahn, B.H.; Shaw, G.M. !$#journal J. Virol. (1992) 66:6587-6600 !$#title Complete nucleotide sequence, genome organization, and !1biological properties of human immunodeficiency virus type 1 !1in vivo: evidence for limited defectiveness and !1complementation. !$#cross-references MUID:93021387; PMID:1404605 !$#accession H44001 !'##molecule_type DNA !'##residues 1-843 ##label LIY !'##cross-references GB:M93258 GENETICS !$#gene env CLASSIFICATION #superfamily type E retrovirus env polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; transmembrane !1protein FEATURE !$1-29 #domain signal sequence #status predicted #label SIG\ !$19-35 #region hydrophobic\ !$30-489 #product coat protein gp120 #status predicted #label !8GP1\ !$490-843 #product coat protein gp41 #status predicted #label !8GP2\ !$499-515 #region hydrophobic\ !$673-689 #region hydrophobic\ !$738-755 #domain transmembrane #status predicted #label TMN\ !$87,129,135,138,154, !$158,184,193,230, !$237,258,272,285, !$291,297,327,351, !$381,389,395,400, !$435,450,598,603, !$612,624 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 843 #molecular-weight 95647 #checksum 551 SEQUENCE /// ENTRY VCLJBR #type complete TITLE env polyprotein - human immunodeficiency virus type 1 (isolate BR) ALTERNATE_NAMES coat polyprotein CONTAINS coat protein gp120; coat protein gp41 ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 #note host Homo sapiens (man) DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Feb-1997 ACCESSIONS A31667 REFERENCE A94389 !$#authors Anand, R.; Thayer, R.; Srinivasan, A.; Nayyar, S.; Gardner, !1M.; Luciw, P.; Dandekar, S. !$#journal Virology (1989) 168:79-89 !$#title Biological and molecular characterization of human !1immunodeficiency virus (HIV-1-BR) from the brain of a !1patient with progressive dementia. !$#cross-references MUID:89085613; PMID:2789516 !$#accession A31667 !'##molecule_type DNA !'##residues 1-852 ##label ANA CLASSIFICATION #superfamily type E retrovirus env polyprotein KEYWORDS capsid protein; coat protein; polyprotein; transmembrane !1protein FEATURE !$1-516 #product coat protein gp120 #status predicted #label !8CP1\ !$517-852 #product coat protein gp41 #status predicted #label !8CP2 SUMMARY #length 852 #molecular-weight 97217 #checksum 3011 SEQUENCE /// ENTRY VCLJ3W #type complete TITLE env polyprotein precursor - human immunodeficiency virus type 1 (isolate WMJ1) CONTAINS coat protein gp120; coat protein gp41 ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 07-Nov-1997 ACCESSIONS A24774 REFERENCE A24774 !$#authors Starcich, B.R.; Hahn, B.H.; Shaw, G.M.; McNeely, P.D.; !1Modrow, S.; Wolf, H.; Parks, E.S.; Parks, W.P.; Josephs, !1S.F.; Gallo, R.C.; Wong-Staal, F. !$#journal Cell (1986) 45:637-648 !$#title Identification and characterization of conserved and !1variable regions in the envelope gene of HTLV-III/LAV, the !1retrovirus of AIDS. !$#cross-references MUID:86218077; PMID:2423250 !$#accession A24774 !'##molecule_type DNA !'##residues 1-856 ##label STA !'##cross-references GB:K03455; GB:M38432; NID:g1906382 GENETICS !$#gene env CLASSIFICATION #superfamily type E retrovirus env polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; transmembrane !1protein FEATURE !$1-29 #domain signal sequence #status predicted #label SIG\ !$30-501 #product coat protein gp120 #status predicted #label !8GP1\ !$502-847 #product coat protein gp41 #status predicted #label !8GP2\ !$87,134,140,151,155, !$183,197,234,241, !$262,276,289,295, !$331,338,354,360, !$390,394,404,447, !$459,611,616,625,637 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 856 #molecular-weight 97525 #checksum 4520 SEQUENCE /// ENTRY VCLJA2 #type complete TITLE env polyprotein precursor - human immunodeficiency virus type 1 (isolate ARV-2) ALTERNATE_NAMES coat polyprotein ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 #note host Homo sapiens (man) DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 16-Jul-1999 ACCESSIONS A03976 REFERENCE A04003 !$#authors Sanchez-Pescador, R.; Power, M.D.; Barr, P.J.; Steimer, !1K.S.; Stempien, M.M.; Brown-Shimer, S.L.; Gee, W.W.; Renard, !1A.; Randolph, A.; Levy, J.A.; Dina, D.; Luciw, P.A. !$#journal Science (1985) 227:484-492 !$#title Nucleotide sequence and expression of an AIDS-associated !1retrovirus (ARV-2). !$#cross-references MUID:85090453; PMID:2578227 !$#accession A03976 !'##molecule_type DNA !'##residues 1-855 ##label SAN !'##cross-references GB:K02007; NID:g328658; PIDN:AAB59882.1; !1PID:g328666 GENETICS !$#gene env CLASSIFICATION #superfamily type E retrovirus env polyprotein KEYWORDS AIDS; capsid protein; coat protein; glycoprotein; !1immunodeficiency; polyprotein; transmembrane protein FEATURE !$1-30 #domain signal sequence #status predicted #label SIG\ !$31-509 #product exterior membrane glycoprotein #status !8predicted #label EXT\ !$510-855 #product transmembrane glycoprotein #status predicted !8#label TMM\ !$87,129,140,158,184, !$190,200,244,265, !$292,298,304,334, !$341,358,364,388, !$394,400,408,445,458 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$610,624,636,815 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 855 #molecular-weight 97437 #checksum 4340 SEQUENCE /// ENTRY VCLJH4 #type complete TITLE env polyprotein - human immunodeficiency virus type 1 (isolate CDC-451) ALTERNATE_NAMES coat polyprotein CONTAINS coat protein gp120; coat protein gp41 ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 16-Jul-1999 ACCESSIONS C25523 REFERENCE A94136 !$#authors Desai, S.M.; Kalyanaraman, V.S.; Casey, J.M.; Srinivasan, !1A.; Andersen, P.R.; Devare, S.G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:8380-8384 !$#title Molecular cloning and primary nucleotide sequence analysis !1of a distinct human immunodeficiency virus isolate reveal !1significant divergence in its genomic sequences. !$#cross-references MUID:87041461; PMID:3490666 !$#accession C25523 !'##molecule_type DNA !'##residues 1-868 ##label DES !'##cross-references GB:M13137; NID:g326460; PIDN:AAA44311.1; !1PID:g326467 GENETICS !$#gene env CLASSIFICATION #superfamily type E retrovirus env polyprotein KEYWORDS capsid protein; coat protein; glycoprotein; polyprotein; !1transmembrane protein FEATURE !$1-521 #product coat protein gp120 #status predicted #label !8GP1\ !$522-868 #product coat protein gp41 #status predicted #label !8GP2\ !$89,138,139,142,166, !$195,198,208,245, !$252,273,287,300, !$312,342,349,365, !$371,395,405,409, !$459,473,623,628, !$637,649,828 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 868 #molecular-weight 98698 #checksum 8580 SEQUENCE /// ENTRY VCLJKB #type complete TITLE env polyprotein precursor - human immunodeficiency virus type 1 (strain KB-1-gp41) ALTERNATE_NAMES coat polyprotein CONTAINS coat protein gp120; coat protein gp41 ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 #note host Homo sapiens (man) DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 01-Mar-1996 ACCESSIONS A42995 REFERENCE A42995 !$#authors Shimizu, H.; Hasebe, F.; Tsuchie, H.; Morikawa, S.; !1Ushijima, H.; Kitamura, T. !$#journal Virology (1992) 189:534-546 !$#title Analysis of a human immunodeficiency virus type 1 isolate !1carrying a truncated transmembrane glycoprotein. !$#cross-references MUID:92351552; PMID:1322587 !$#accession A42995 !'##molecule_type mRNA !'##residues 1-861 ##label SHI !'##cross-references GB:S41266; GB:D01206 GENETICS !$#gene env CLASSIFICATION #superfamily type E retrovirus env polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; transmembrane !1protein FEATURE !$1-689 #domain extracellular #status predicted #label EXT\ !$1-33 #domain signal sequence #status predicted #label SIG\ !$17-33 #region hydrophobic #status predicted\ !$34-517 #product coat protein gp120 #status predicted #label !8CP1\ !$514-517 #region cleavage processing #status predicted\ !$518-861 #product coat protein gp41 #status predicted #label !8CP2\ !$518-534 #region hydrophobic #status predicted\ !$690-711 #domain transmembrane #status predicted #label TM1\ !$712-861 #domain intracellular #status predicted #label INT\ !$756-772 #region hydrophobic #status predicted\ !$93,141,145,146,163, !$191,192,237,241, !$248,269,283,296, !$308,338,345,361, !$367,397,403,408, !$414,449,465,468, !$617,622,631,643 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 861 #molecular-weight 98115 #checksum 2740 SEQUENCE /// ENTRY VCLJKX #type complete TITLE env polyprotein precursor - human immunodeficiency virus type 1 (strain KB-1-gp32) ALTERNATE_NAMES coat polyprotein CONTAINS coat protein gp120; coat protein gp32 ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 #note host Homo sapiens (man) DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 01-Mar-1996 ACCESSIONS B42995 REFERENCE A42995 !$#authors Shimizu, H.; Hasebe, F.; Tsuchie, H.; Morikawa, S.; !1Ushijima, H.; Kitamura, T. !$#journal Virology (1992) 189:534-546 !$#title Analysis of a human immunodeficiency virus type 1 isolate !1carrying a truncated transmembrane glycoprotein. !$#cross-references MUID:92351552; PMID:1322587 !$#accession B42995 !'##molecule_type mRNA !'##residues 1-729 ##label SHI !'##cross-references GB:S41266; GB:D01206 GENETICS !$#gene env CLASSIFICATION #superfamily type E retrovirus env polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; transmembrane !1protein FEATURE !$1-689 #domain extracellular #status predicted #label EXT\ !$1-33 #domain signal sequence #status predicted #label SIG\ !$17-33 #region hydrophobic #status predicted\ !$34-517 #product coat protein gp120 #status predicted #label !8CP1\ !$514-517 #region cleavage processing #status predicted\ !$518-729 #product coat protein gp32 #status predicted #label !8CP2\ !$518-534 #region hydrophobic #status predicted\ !$690-711 #domain transmembrane #status predicted #label TM1\ !$712-729 #domain intracellular #status predicted #label INT\ !$93,141,145,146,163, !$191,192,237,241, !$248,269,283,296, !$308,338,345,361, !$367,397,403,408, !$414,449,465,468, !$617,622,631,643 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 729 #molecular-weight 82962 #checksum 1066 SEQUENCE /// ENTRY VCLJSI #type complete TITLE env polyprotein precursor - simian immunodeficiency virus SIVcpz ALTERNATE_NAMES coat polyprotein CONTAINS coat protein gp120; coat protein gp41 ORGANISM #formal_name simian immunodeficiency virus SIVcpz #note host Pan troglodytes (chimpanzee) DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jul-1999 ACCESSIONS S09990 REFERENCE S09983 !$#authors Huet, T.; Cheynier, R.; Meyerhans, A.; Roelants, G.; !1Wain-Hobson, S. !$#journal Nature (1990) 345:356-359 !$#title Genetic organization of a chimpanzee lentivirus related to !1HIV-1. !$#cross-references MUID:90259077; PMID:2188136 !$#accession S09990 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-854 ##label HUE !'##cross-references EMBL:X52154; NID:g58866; PIDN:CAA36407.1; !1PID:g58874 GENETICS !$#gene env CLASSIFICATION #superfamily type E retrovirus env polyprotein KEYWORDS AIDS; capsid protein; coat protein; glycoprotein; !1immunodeficiency; polyprotein; transmembrane protein FEATURE !$1-30 #domain signal sequence #status predicted #label SIG\ !$31-500 #product coat protein gp120 #status predicted #label !8CP1\ !$501-854 #product coat protein gp41 #status predicted #label !8CP2\ !$501-517 #domain transmembrane #status predicted #label TM1\ !$675-693 #domain transmembrane #status predicted #label TM2\ !$805-821 #domain transmembrane #status predicted #label TM3\ !$134,140,143,154, !$158,186,195,239, !$260,267,274,299, !$331,336,351,356, !$384,392,426,432, !$446,450,601,608, !$616,628 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 854 #molecular-weight 95803 #checksum 1071 SEQUENCE /// ENTRY VCLJND #type complete TITLE env polyprotein precursor - human immunodeficiency virus type 1 (isolate NDK) ALTERNATE_NAMES coat polyprotein CONTAINS coat protein gp120; coat protein gp41 ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 #note host Homo sapiens (man) DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jul-1999 ACCESSIONS JQ0066 REFERENCE JQ0065 !$#authors Spire, B.; Sire, J.; Zachar, V.; Rey, F.; Barre-Sinoussi, !1F.; Galibert, F.; Hampe, A.; Chermann, J.C. !$#journal Gene (1989) 81:275-284 !$#title Nucleotide sequence of HIV1-NDK: a highly cytopathic strain !1of the human immunodeficiency virus. !$#cross-references MUID:90034200; PMID:2806917 !$#accession JQ0066 !'##molecule_type DNA !'##residues 1-846 ##label SPI !'##cross-references GB:M27323; NID:g328154; PIDN:AAA44873.1; !1PID:g328162 !'##note the authors translated the codon GCG for residue 523 as Arg GENETICS !$#gene env CLASSIFICATION #superfamily type E retrovirus env polyprotein KEYWORDS AIDS; capsid protein; coat protein; glycoprotein; !1immunodeficiency; polyprotein; transmembrane protein FEATURE !$1-29 #domain signal sequence #status predicted #label SIG\ !$30-501 #product coat protein gp120 #status predicted #label !8CP1\ !$502-846 #product coat protein gp41 #status predicted #label !8CP2\ !$502-520 #domain transmembrane #status predicted #label TM1\ !$674-692 #domain transmembrane #status predicted #label TM2\ !$87,129,151,179,182, !$229,236,257,271, !$284,290,351,382, !$388,392,395,401, !$438,451,452,601, !$606,615,627 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 846 #molecular-weight 96475 #checksum 2624 SEQUENCE /// ENTRY VCLJZR #type complete TITLE env polyprotein precursor - human immunodeficiency virus Zr-6 ALTERNATE_NAMES coat polyprotein ORGANISM #formal_name human immunodeficiency virus Zr-6 DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Jul-1999 ACCESSIONS D26192 REFERENCE A26192 !$#authors Srinivasan, A.; Anand, R.; York, D.; Ranganathan, P.; !1Feorino, P.; Schochetman, G.; Curran, J.; Kalyanaraman, !1V.S.; Luciw, P.A.; Sanchez-Pescador, R. !$#journal Gene (1987) 52:71-82 !$#title Molecular characterization of human immunodeficiency virus !1from Zaire: nucleotide sequence analysis identifies !1conserved and variable domains in the envelope gene. !$#cross-references MUID:87248097; PMID:3036660 !$#accession D26192 !'##molecule_type DNA !'##residues 1-855 ##label SRI !'##cross-references GB:K03458; GB:M16322; NID:g329398; PIDN:AAA45380.1; !1PID:g329403 GENETICS !$#gene env CLASSIFICATION #superfamily type E retrovirus env polyprotein KEYWORDS AIDS; capsid protein; coat protein; glycoprotein; !1immunodeficiency; polyprotein; transmembrane protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-855 #product env polyprotein #status predicted #label !8MAT\ !$20-500 #product exterior membrane glycoprotein #status !8predicted #label EXT\ !$501-855 #product transmembrane glycoprotein #status predicted !8#label TMM\ !$87,129,140,145,154, !$158,186,189,199, !$236,243,264,278, !$291,297,333,340, !$355,386,392,398, !$404,443,447,460, !$461,464,610,615, !$624,636,673 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 855 #molecular-weight 96970 #checksum 4779 SEQUENCE /// ENTRY VCLJMN #type complete TITLE env polyprotein precursor - human immunodeficiency virus type 1 (isolate MN) ALTERNATE_NAMES coat polyprotein ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 #note host Homo sapiens (man) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Feb-1997 ACCESSIONS A28922 REFERENCE A28922 !$#authors Gurgo, C.; Guo, H.G.; Franchini, G.; Aldovini, A.; Collalti, !1E.; Farrell, K.; Wong-Staal, F.; Gallo, R.C.; Reitz Jr., !1M.S. !$#journal Virology (1988) 164:531-536 !$#title Envelope sequences of two new United States HIV-1 isolates. !$#cross-references MUID:88219542; PMID:3369091 !$#accession A28922 !'##molecule_type DNA !'##residues 1-859 ##label GUR GENETICS !$#gene env CLASSIFICATION #superfamily type E retrovirus env polyprotein KEYWORDS capsid protein; coat protein; glycoprotein; polyprotein; !1transmembrane protein FEATURE !$1-29 #domain signal sequence #status predicted #label SIG\ !$30-859 #product env polyprotein #status predicted #label !8EPP\ !$87,129,135,140,141, !$146,161,165,191, !$202,246,267,281, !$294,300,336,343, !$359,365,389,395, !$401,408,409,416, !$451,468,615,620, !$629,641,819 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 859 #molecular-weight 97476 #checksum 6456 SEQUENCE /// ENTRY VCLJSC #type complete TITLE env polyprotein precursor - human immunodeficiency virus type 1 (isolate SC) ALTERNATE_NAMES coat polyprotein ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 #note host Homo sapiens (man) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Feb-1997 ACCESSIONS B28922 REFERENCE A28922 !$#authors Gurgo, C.; Guo, H.G.; Franchini, G.; Aldovini, A.; Collalti, !1E.; Farrell, K.; Wong-Staal, F.; Gallo, R.C.; Reitz Jr., !1M.S. !$#journal Virology (1988) 164:531-536 !$#title Envelope sequences of two new United States HIV-1 isolates. !$#cross-references MUID:88219542; PMID:3369091 !$#accession B28922 !'##molecule_type DNA !'##residues 1-861 ##label GUR GENETICS !$#gene env CLASSIFICATION #superfamily type E retrovirus env polyprotein KEYWORDS capsid protein; coat protein; glycoprotein; polyprotein; !1transmembrane protein FEATURE !$1-29 #domain signal sequence #status predicted #label SIG\ !$30-861 #product env polyprotein #status predicted #label !8EPP\ !$87,129,135,140,143, !$159,163,187,198, !$234,241,262,276, !$295,301,302,333, !$340,356,362,386, !$396,405,410,447, !$462,616,621,630, !$642,679,821 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 861 #molecular-weight 97668 #checksum 8218 SEQUENCE /// ENTRY A44963 #type complete TITLE env polyprotein precursor - human immunodeficiency virus type 1 (isolate Z321) ALTERNATE_NAMES coat polyprotein CONTAINS coat protein gp120; coat protein gp41 ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 #note host Homo sapiens (man) DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 28-May-1999 ACCESSIONS A44963 REFERENCE A44963 !$#authors Srinivasan, A.; York, D.; Butler Jr., D.; Jannoun-Nasr, R.; !1Getchell, J.; McCormick, J.; Ou, C.Y.; Myers, G.; Smith, T.; !1Chen, E.; Flaggs, G.; Berman, P.; Schochetman, G.; !1Kalyanaraman, S. !$#journal AIDS Res. Hum. Retroviruses (1989) 5:121-129 !$#title Molecular characterization of HIV-1 isolated from a serum !1collected in 1976: nucleotide sequence comparison to recent !1isolates and generation of hybrid HIV. !$#cross-references MUID:89228766; PMID:2713163 !$#accession A44963 !'##molecule_type DNA !'##residues 1-856 ##label SRI !'##cross-references GB:M15896; NID:g329392; PIDN:AAB53948.1; !1PID:g329394 GENETICS !$#gene env CLASSIFICATION #superfamily type E retrovirus env polyprotein KEYWORDS capsid protein; coat protein; glycoprotein; polyprotein; !1transmembrane protein FEATURE !$1-29 #domain signal sequence #status predicted #label SIG\ !$30-520 #product coat protein gp120 #status predicted #label !8CP1\ !$521-856 #product coat protein gp41 #status predicted #label !8CP2\ !$684-705 #domain transmembrane #status predicted #label TMN\ !$87,132,138,152,156, !$183,198,242,263, !$277,294,302,339, !$393,398,402,411, !$448,461,462,465, !$611,616,637 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 856 #molecular-weight 96909 #checksum 8151 SEQUENCE /// ENTRY VCLJG2 #type complete TITLE env polyprotein precursor - human immunodeficiency virus type 2 (isolate ROD) ALTERNATE_NAMES coat polyprotein ORGANISM #formal_name human immunodeficiency virus type 2, HIV-2 DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Jul-1999 ACCESSIONS C26262 REFERENCE A26262 !$#authors Guyader, M.; Emerman, M.; Sonigo, P.; Clavel, F.; !1Montagnier, L.; Alizon, M. !$#journal Nature (1987) 326:662-669 !$#title Genome organization and transactivation of the human !1immuno-deficiency virus type 2. !$#cross-references MUID:87173056; PMID:3031510 !$#contents proviral DNA !$#accession C26262 !'##molecule_type DNA !'##residues 1-858 ##label GUY !'##cross-references GB:M15390; NID:g1332361; PIDN:AAB00770.1; !1PID:g325749 GENETICS !$#gene env CLASSIFICATION #superfamily type E retrovirus env polyprotein KEYWORDS AIDS; capsid protein; coat protein; glycoprotein; !1immunodeficiency; polyprotein; transmembrane protein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-858 #product env polyprotein #status predicted #label !8MAT\ !$18-501 #product exterior membrane glycoprotein #status !8predicted #label EXT\ !$502-858 #product transmembrane glycoprotein #status predicted !8#label TMM\ !$34,67,76,119,120, !$151,166,179,192, !$193,196,206,238, !$241,248,272,278, !$289,300,367,371, !$400,410,447,463, !$466,611,620,636 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 858 #molecular-weight 98836 #checksum 9821 SEQUENCE /// ENTRY VCLJST #type complete TITLE env polyprotein precursor - human immunodeficiency virus type 2 (isolate ST) ALTERNATE_NAMES coat polyprotein CONTAINS surface glycoprotein gp120; transmembrane glycoprotein gp41 ORGANISM #formal_name human immunodeficiency virus type 2, HIV-2 #note host Homo sapiens (man) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 09-Sep-1994 ACCESSIONS H33943 REFERENCE A33943 !$#authors Kumar, P.; Hui, H.; Kappes, J.C.; Haggarty, B.S.; Hoxie, !1J.A.; Arya, S.K.; Shaw, G.M.; Hahn, B.H. !$#journal J. Virol. (1990) 64:890-901 !$#title Molecular characterization of an attenuated human !1immunodeficiency virus type 2 isolate. !$#cross-references MUID:90112662; PMID:2296086 !$#accession H33943 !'##molecule_type genomic RNA !'##residues 1-859 ##label KUM !'##cross-references EMBL:M86924 GENETICS !$#gene env CLASSIFICATION #superfamily type E retrovirus env polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; transmembrane !1protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-859 #product env polyprotein #status predicted #label !8ENV\ !$20-501 #product surface glycoprotein gp120 #status predicted !8#label SGG\ !$506-859 #product transmembrane glycoprotein gp41 #status !8predicted #label TGG\ !$507-523 #region hydrophobic\ !$675-694 #domain transmembrane #status predicted #label TMN\ !$36,69,78,113,119, !$131,137,145,160, !$173,186,200,232, !$235,242,266,272, !$283,294,304,359, !$392,402,405,442, !$457,460,605,614,630 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 859 #molecular-weight 99025 #checksum 4186 SEQUENCE /// ENTRY VCLJS4 #type complete TITLE env polyprotein precursor - human immunodeficiency virus type 2 (isolate ST/24.1C/2) ALTERNATE_NAMES coat polyprotein CONTAINS surface glycoprotein gp120; transmembrane glycoprotein gp41 ORGANISM #formal_name human immunodeficiency virus type 2, HIV-2 #note host Homo sapiens (man) DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS A42535 REFERENCE A42535 !$#authors Mulligan, M.J.; Yamshchikov, G.V.; Ritter Jr., G.D.; Gao, !1F.; Jin, M.J.; Nail, C.D.; Spies, C.P.; Hahn, B.H.; Compans, !1R.W. !$#journal J. Virol. (1992) 66:3971-3975 !$#title Cytoplasmic domain truncation enhances fusion activity by !1the exterior glycoprotein complex of human immunodeficiency !1virus type 2 in selected cell types. !$#cross-references MUID:92260681; PMID:1583738 !$#accession A42535 !'##molecule_type DNA !'##residues 1-712 ##label MUL !'##cross-references GB:M86924; NID:g325760; PIDN:AAA43938.1; !1PID:g325761 GENETICS !$#gene env CLASSIFICATION #superfamily type E retrovirus env polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; transmembrane !1protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-712 #product env polyprotein #status predicted #label !8ENV\ !$20-501 #product surface glycoprotein gp120 #status predicted !8#label SGG\ !$506-712 #product transmembrane glycoprotein gp41 #status !8predicted #label TPG\ !$507-523 #region hydrophobic\ !$675-694 #domain transmembrane #status predicted #label TMN\ !$36,69,78,113,119, !$131,137,145,160, !$173,200,232,235, !$242,266,272,283, !$294,304,359,392, !$402,405,442,457, !$460,605,614,630 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 712 #molecular-weight 81723 #checksum 5409 SEQUENCE /// ENTRY VCLJCT #type complete TITLE env polyprotein precursor - human immunodeficiency virus type 2 (isolate CAM2/Guinea-Bissau) ALTERNATE_NAMES coat polyprotein ORGANISM #formal_name human immunodeficiency virus type 2, HIV-2 #note host Homo sapiens (man) DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jun-2000 ACCESSIONS F38475; JQ0978 REFERENCE A38475 !$#authors Tristem, M.; Hill, F.; Karpas, A. !$#journal J. Gen. Virol. (1991) 72:721-724 !$#title Nucleotide sequence of a Guinea-Bissau-derived human !1immunodeficiency virus type 2 proviral clone (HIV-2-CAM2). !$#cross-references MUID:91170959; PMID:2005437 !$#accession F38475 !'##molecule_type DNA !'##residues 1-859 ##label TRI !'##cross-references GB:D00835; NID:g3153166; PIDN:BAA00716.1; !1PID:g221472 COMMENT The cleavage sites of this polyprotein have not been !1determined. GENETICS !$#gene env CLASSIFICATION #superfamily type E retrovirus env polyprotein KEYWORDS AIDS; coat protein; glycoprotein; immunodeficiency; !1polyprotein; transmembrane protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-859 #product env polyprotein #status predicted #label !8ENP\ !$38,71,115,148,163, !$176,188,195,205, !$237,247,271,277, !$288,299,309,343, !$366,398,411,448, !$463,467,612,621,637 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 859 #molecular-weight 99017 #checksum 1825 SEQUENCE /// ENTRY VCLJGG #type complete TITLE env polyprotein precursor - human immunodeficiency virus type 2 (isolate GH-1) ALTERNATE_NAMES coat polyprotein ORGANISM #formal_name human immunodeficiency virus type 2, HIV-2 #note host Homo sapiens (man) DATE 30-Jun-1990 #sequence_revision 26-Jan-1996 #text_change 16-Feb-1997 ACCESSIONS JS0334 REFERENCE JS0327 !$#authors Hasegawa, A.; Tsujimoto, H.; Maki, N.; Ishikawa, K.; Miura, !1T.; Fukasawa, M.; Miki, K.; Hayami, M. !$#journal AIDS Res. Hum. Retroviruses (1989) 5:593-604 !$#title Sequence of a distinct HIV-2 isolate from Ghana showing !1significant divergence in its genome. !$#cross-references MUID:90122350; PMID:2611042 !$#accession JS0334 !'##molecule_type DNA !'##residues 1-852 ##label HAS !'##note this sequence was submitted to JIPID, October 1989 !'##note readthrough of the UAG stop codon at 739 may occur COMMENT Cleavage sites that yield the mature coat proteins are not !1determined. GENETICS !$#gene env CLASSIFICATION #superfamily type E retrovirus env polyprotein KEYWORDS AIDS; coat protein; glycoprotein; polyprotein; transmembrane !1protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-852 #product env polyprotein #status predicted #label !8MAT\ !$739 #region amber stop codon\ !$36,69,113,117,118, !$132,141,169,182, !$197,229,232,263, !$269,280,291,301, !$356,362,389,402, !$439,454,457,602, !$611,627,781 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 852 #molecular-weight 97600 #checksum 3523 SEQUENCE /// ENTRY VCLJS2 #type complete TITLE env polyprotein precursor - simian immunodeficiency virus SIVagm (type 3, isolate STLV-3agm) CONTAINS coat protein gp120; coat protein gp32; hypothetical protein env-extn ORGANISM #formal_name simian immunodeficiency virus SIVagm DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 07-Nov-1997 ACCESSIONS C26737 REFERENCE A26737 !$#authors Hirsch, V.; Riedel, N.; Mullins, J.I. !$#journal Cell (1987) 49:307-319 !$#title The genome organization of STLV-3 is similar to that of the !1AIDS virus except for a truncated transmembrane protein. !$#cross-references MUID:87187627; PMID:3646094 !$#accession C26737 !'##molecule_type DNA !'##residues 1-880 ##label HIR !'##cross-references GB:M19499; NID:g334657 GENETICS !$#gene env CLASSIFICATION #superfamily type E retrovirus env polyprotein KEYWORDS AIDS; capsid protein; coat protein; glycoprotein; !1polyprotein FEATURE !$1-527 #product coat protein gp120 #status predicted #label !8GPS\ !$528-735 #product coat protein gp32 #status predicted #label !8GPT\ !$736-880 #product hypothetical env-extn protein #status !8predicted #label ETN\ !$37,70,114,148,173, !$186,200,204,214, !$246,249,280,286, !$297,308,318,373, !$379,462,478,627, !$636,652,760 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 880 #molecular-weight 101245 #checksum 699 SEQUENCE /// ENTRY VCLJG5 #type complete TITLE env polyprotein - simian immunodeficiency virus (African green monkey isolate) CONTAINS coat protein gp120; coat protein gp32 ORGANISM #formal_name simian immunodeficiency virus, SIV DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jul-1999 ACCESSIONS D28873; S55074; S55068; S54796; S55069; S55070; S55071 REFERENCE A28873 !$#authors Franchini, G.; Gurgo, C.; Guo, H.G.; Gallo, R.C.; Collalti, !1E.; Fargnoli, K.A.; Hall, L.F.; Wong-Staal, F.; Reitz Jr., !1M.S. !$#journal Nature (1987) 328:539-543 !$#title Sequence of simian immunodeficiency virus and its !1relationship to the human immunodeficiency viruses. !$#cross-references MUID:87287229; PMID:3497350 !$#accession D28873 !'##molecule_type DNA !'##residues 1-889 ##label FRA !'##cross-references EMBL:M19499 REFERENCE S54796 !$#authors Whatmore, A.; Cook, N.; Hall, G.; Sharpe, S.; Rud, E.; !1Cranage, M. !$#submission submitted to the EMBL Data Library, April 1995 !$#description Repair and evolution of nef in vivo modulates SIV virulence. !$#accession S55074 !'##molecule_type DNA !'##residues 847-889 ##label WHA !'##cross-references EMBL:X86729; NID:g840893; PIDN:CAA60404.1; !1PID:g861126 !'##experimental_source developmental stage week 37 !$#accession S55068 !'##molecule_type DNA !'##residues 848-889 ##label WH2 !'##cross-references EMBL:X86724; NID:g840887; PIDN:CAA60394.1; !1PID:g840888 !'##experimental_source developmental stage week 2 !$#accession S54796 !'##molecule_type DNA !'##residues 848-889 ##label WHW !'##cross-references EMBL:X86726; NID:g840886; PIDN:CAA60398.1; !1PID:g861120 !'##experimental_source developmental stage week 17 !$#accession S55069 !'##molecule_type DNA !'##residues 848-889 ##label WHF !'##cross-references EMBL:X86731; NID:g840895; PIDN:CAA60408.1; !1PID:g861130 !'##experimental_source developmental stage week 45 !$#accession S55070 !'##molecule_type DNA !'##residues 848-889 ##label WHZ !'##cross-references EMBL:X86725; NID:g840897; PIDN:CAA60396.1; !1PID:g861134 !'##experimental_source developmental stage week 8 !$#accession S55071 !'##molecule_type DNA !'##residues 848-889 ##label WHY !'##cross-references EMBL:X86730; NID:g840894; PIDN:CAA60406.1; !1PID:g861128 !'##experimental_source developmental stage week 41 GENETICS !$#gene env CLASSIFICATION #superfamily type E retrovirus env polyprotein KEYWORDS AIDS; capsid protein; coat protein; immunodeficiency; !1polyprotein; transmembrane protein FEATURE !$1-536 #product coat protein gp120 #status predicted #label !8GP1\ !$537-889 #product coat protein gp32 #status predicted #label !8GP2 SUMMARY #length 889 #molecular-weight 102156 #checksum 2221 SEQUENCE /// ENTRY VCLJG3 #type complete TITLE env polyprotein - simian immunodeficiency virus (macaque isolate) ORGANISM #formal_name simian immunodeficiency virus, SIV DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 07-Nov-1997 ACCESSIONS H28887 REFERENCE A28887 !$#authors Chakrabarti, L.; Guyader, M.; Alizon, M.; Daniel, M.D.; !1Desrosiers, R.C.; Tiollais, P.; Sonigo, P. !$#journal Nature (1987) 328:543-547 !$#title Sequence of simian immunodeficiency virus from macaque and !1its relationship to other human and simian retroviruses. !$#cross-references MUID:87287230; PMID:3649576 !$#accession H28887 !'##molecule_type DNA !'##residues 1-881 ##label CHA !'##cross-references GB:Y00277; GB:M16403; NID:g61730 GENETICS !$#gene env CLASSIFICATION #superfamily type E retrovirus env polyprotein KEYWORDS AIDS; capsid protein; coat protein; immunodeficiency; !1polyprotein; transmembrane protein SUMMARY #length 881 #molecular-weight 101086 #checksum 7553 SEQUENCE /// ENTRY VCLJG4 #type complete TITLE env polyprotein - simian immunodeficiency virus (African green monkey isolate) ORGANISM #formal_name simian immunodeficiency virus, SIV DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 24-Oct-1997 ACCESSIONS G30045 REFERENCE A30045 !$#authors Fukasawa, M.; Miura, T.; Hasegawa, A.; Morikawa, S.; !1Tsujimoto, H.; Miki, K.; Kitamura, T.; Hayami, M. !$#journal Nature (1988) 333:457-461 !$#title Sequence of simian immunodeficiency virus from African green !1monkey, a new member of the HIV/SIV group. !$#cross-references MUID:88232906; PMID:3374586 !$#accession G30045 !'##molecule_type DNA !'##residues 1-864 ##label FUK !'##cross-references EMBL:X07805 GENETICS !$#gene env CLASSIFICATION #superfamily type E retrovirus env polyprotein KEYWORDS AIDS; capsid protein; coat protein; immunodeficiency; !1polyprotein; transmembrane protein SUMMARY #length 864 #molecular-weight 98914 #checksum 4510 SEQUENCE /// ENTRY VCLJBT #type complete TITLE env polyprotein precursor - bovine immunodeficiency virus (isolate 127) ALTERNATE_NAMES coat polyprotein CONTAINS coat protein gp40; coat protein gp62 ORGANISM #formal_name bovine immunodeficiency virus DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 31-Jan-1997 ACCESSIONS E34742 REFERENCE A34742 !$#authors Garvey, K.J.; Oberste, M.S.; Elser, J.E.; Braun, M.J.; !1Gonda, M.A. !$#journal Virology (1990) 175:391-409 !$#title Nucleotide sequence and genome organization of biologically !1active proviruses of the bovine immunodeficiency-like virus. !$#cross-references MUID:90223985; PMID:2183467 !$#accession E34742 !'##molecule_type genomic RNA !'##residues 1-904 ##label GAR !'##cross-references GB:M32690 GENETICS !$#gene env CLASSIFICATION #superfamily BIV env polyprotein KEYWORDS AIDS; capsid protein; coat protein; glycoprotein; !1immunodeficiency; polyprotein; transmembrane protein FEATURE !$1-13 #domain signal sequence #status predicted #label SIG\ !$14-555 #product coat protein gp62 #status predicted #label !8GP1\ !$556-904 #product coat protein gp40 #status predicted #label !8GP2\ !$556-572 #domain transmembrane #status predicted #label TN1\ !$729-747 #domain transmembrane #status predicted #label TN2\ !$827-843 #domain transmembrane #status predicted #label TN3\ !$131,255,277,296, !$329,367,376,385, !$410,427,432,452, !$491,509,541,597, !$663,694,877 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 904 #molecular-weight 102368 #checksum 5598 SEQUENCE /// ENTRY VCLJEV #type complete TITLE env polyprotein precursor - equine infectious anemia virus CONTAINS coat protein gp45; coat protein gp90 ORGANISM #formal_name equine infectious anemia virus #note host Equus caballus (domestic horse) DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 12-Apr-1996 ACCESSIONS A25610; B25610 REFERENCE A25610 !$#authors Rushlow, K.; Olsen, K.; Stiegler, G.; Payne, S.L.; !1Montelaro, R.C.; Issel, C.J. !$#journal Virology (1986) 155:309-321 !$#title Lentivirus genomic organization: the complete nucleotide !1sequence of the env gene region of equine infectious anemia !1virus. !$#cross-references MUID:87071653; PMID:2431539 !$#accession A25610 !'##molecule_type DNA !'##residues 1-859 ##label RUS GENETICS !$#gene env CLASSIFICATION #superfamily equine infectious anemia virus env polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; transmembrane !1protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-444 #product coat protein gp90 #status predicted #label !8GPP\ !$445-859 #product coat protein gp45 #status predicted #label !8GGP\ !$446-472 #domain transmembrane #status predicted #label TN1\ !$617-636 #domain transmembrane #status predicted #label TMN\ !$40,112,141,148,186, !$214,233,244,340, !$368,399,406,411, !$483,490,550,557,752 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 859 #molecular-weight 97085 #checksum 7501 SEQUENCE /// ENTRY VCLJ22 #type complete TITLE env polyprotein precursor - equine infectious anemia virus (strain CL22) ALTERNATE_NAMES coat polyprotein CONTAINS coat protein gp45; coat protein gp90 ORGANISM #formal_name equine infectious anemia virus #note host Equus caballus (domestic horse) DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS C41991 REFERENCE A41991 !$#authors Perry, S.T.; Flaherty, M.T.; Kelley, M.J.; Clabough, D.L.; !1Tronick, S.R.; Coggins, L.; Whetter, L.; Lengel, C.R.; !1Fuller, F. !$#journal J. Virol. (1992) 66:4085-4097 !$#title The surface envelope protein gene region of equine !1infectious anemia virus is not an important determinant of !1tropism in vitro. !$#cross-references MUID:92292230; PMID:1318398 !$#accession C41991 !'##molecule_type DNA !'##residues 1-859 ##label PER !'##cross-references GB:M87581; NID:g290627; PIDN:AAA43005.1; !1PID:g290630 GENETICS !$#gene env CLASSIFICATION #superfamily equine infectious anemia virus env polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; transmembrane !1protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-859 #product env polyprotein #status predicted #label !8ENV\ !$23-444 #product coat protein gp90 #status predicted #label !8GPP\ !$445-859 #product coat protein gp45 #status predicted #label !8GGP\ !$446-472 #region hydrophobic\ !$615-636 #domain transmembrane #status predicted #label TMN\ !$40,112,141,148,186, !$214,233,244,340, !$368,399,406,411, !$483,490,550,557 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 859 #molecular-weight 97140 #checksum 7212 SEQUENCE /// ENTRY VCLJEW #type complete TITLE env polyprotein precursor (clone 1369) - equine infectious anemia virus CONTAINS coat protein gp45; coat protein gp90 ORGANISM #formal_name equine infectious anemia virus #note host Equus caballus (domestic horse) DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 07-Nov-1997 ACCESSIONS C27842 REFERENCE A27842 !$#authors Kawakami, T.; Sherman, L.; Dahlberg, J.; Gazit, A.; Yaniv, !1A.; Tronick, S.R.; Aaronson, S.A. !$#journal Virology (1987) 158:300-312 !$#title Nucleotide sequence analysis of equine infectious anemia !1virus proviral DNA. !$#cross-references MUID:87236196; PMID:3035786 !$#accession C27842 !'##molecule_type DNA !'##residues 1-859 ##label KAW !'##cross-references GB:M16575; NID:g323836 GENETICS !$#gene env CLASSIFICATION #superfamily equine infectious anemia virus env polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; transmembrane !1protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-444 #product coat protein gp90 #status predicted #label !8GP1\ !$445-859 #product coat protein gp45 #status predicted #label !8GP2\ !$446-472 #domain transmembrane #status predicted #label TN1\ !$617-636 #domain transmembrane #status predicted #label TMN\ !$40,112,141,148,186, !$214,233,244,340, !$368,399,406,411, !$483,490,550,557,752 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 859 #molecular-weight 97373 #checksum 7628 SEQUENCE /// ENTRY VCLJE1 #type complete TITLE env polyprotein precursor (clone P3.2-1) - equine infectious anemia virus CONTAINS coat protein gp45; coat protein gp90 ORGANISM #formal_name equine infectious anemia virus #note host Equus caballus (domestic horse) DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Jul-1999 ACCESSIONS A34027 REFERENCE A34027 !$#authors Payne, S.L.; Fang, F.D.; Liu, C.P.; Dhruva, B.R.; Rwambo, !1P.; Issel, C.J.; Montelaro, R.C. !$#journal Virology (1987) 161:321-331 !$#title Antigenic variation and lentivirus persistence: variations !1in envelope gene sequences during EIAV infection resemble !1changes reported for sequential isolates of HIV. !$#cross-references MUID:88072070; PMID:2825406 !$#accession A34027 !'##molecule_type genomic RNA !'##residues 1-859 ##label PAY !'##cross-references GB:M18385; NID:g323830; PIDN:AAA66407.1; !1PID:g323831 GENETICS !$#gene env CLASSIFICATION #superfamily equine infectious anemia virus env polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; transmembrane !1protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-444 #product coat protein gp90 #status predicted #label !8CP1\ !$75-93 #domain transmembrane #status predicted #label TM1\ !$445-859 #product coat protein gp45 #status predicted #label !8CP2\ !$446-462 #domain transmembrane #status predicted #label TM2\ !$614-636 #domain transmembrane #status predicted #label TM3\ !$787-807 #domain transmembrane #status predicted #label TM4\ !$816-835 #domain transmembrane #status predicted #label TM5\ !$40,112,141,148,186, !$214,233,244,340, !$368,399,406,411, !$422,483,490,550, !$557,752 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 859 #molecular-weight 97140 #checksum 7314 SEQUENCE /// ENTRY VCLJE2 #type complete TITLE env polyprotein precursor (clone P3.2-2) - equine infectious anemia virus CONTAINS coat protein gp45; coat protein gp90 ORGANISM #formal_name equine infectious anemia virus #note host Equus caballus (domestic horse) DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Jul-1999 ACCESSIONS B34027 REFERENCE A34027 !$#authors Payne, S.L.; Fang, F.D.; Liu, C.P.; Dhruva, B.R.; Rwambo, !1P.; Issel, C.J.; Montelaro, R.C. !$#journal Virology (1987) 161:321-331 !$#title Antigenic variation and lentivirus persistence: variations !1in envelope gene sequences during EIAV infection resemble !1changes reported for sequential isolates of HIV. !$#cross-references MUID:88072070; PMID:2825406 !$#accession B34027 !'##molecule_type genomic RNA !'##residues 1-859 ##label PAY !'##cross-references GB:M18386; NID:g323832; PIDN:AAA66408.1; !1PID:g323833 GENETICS !$#gene env CLASSIFICATION #superfamily equine infectious anemia virus env polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; transmembrane !1protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-444 #product coat protein gp90 #status predicted #label !8CP1\ !$75-93 #domain transmembrane #status predicted #label TM1\ !$445-859 #product coat protein gp45 #status predicted #label !8CP2\ !$446-462 #domain transmembrane #status predicted #label TM2\ !$614-636 #domain transmembrane #status predicted #label TM3\ !$787-807 #domain transmembrane #status predicted #label TM4\ !$816-835 #domain transmembrane #status predicted #label TM5\ !$40,112,141,148,184, !$201,214,233,244, !$282,313,340,346, !$368,399,406,411, !$422,483,490,550, !$557,752 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 859 #molecular-weight 97188 #checksum 8969 SEQUENCE /// ENTRY VCLJE3 #type complete TITLE env polyprotein precursor (clone P3.2-3) - equine infectious anemia virus CONTAINS coat protein gp45; coat protein gp90 ORGANISM #formal_name equine infectious anemia virus #note host Equus caballus (domestic horse) DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Jul-1999 ACCESSIONS C34027 REFERENCE A34027 !$#authors Payne, S.L.; Fang, F.D.; Liu, C.P.; Dhruva, B.R.; Rwambo, !1P.; Issel, C.J.; Montelaro, R.C. !$#journal Virology (1987) 161:321-331 !$#title Antigenic variation and lentivirus persistence: variations !1in envelope gene sequences during EIAV infection resemble !1changes reported for sequential isolates of HIV. !$#cross-references MUID:88072070; PMID:2825406 !$#accession C34027 !'##molecule_type genomic RNA !'##residues 1-859 ##label PAY !'##cross-references GB:M18387; NID:g323834; PIDN:AAA66409.1; !1PID:g323835 GENETICS !$#gene env CLASSIFICATION #superfamily equine infectious anemia virus env polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; transmembrane !1protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-444 #product coat protein gp90 #status predicted #label !8CP1\ !$75-93 #domain transmembrane #status predicted #label TM1\ !$445-859 #product coat protein gp45 #status predicted #label !8CP2\ !$446-462 #domain transmembrane #status predicted #label TM2\ !$614-636 #domain transmembrane #status predicted #label TM3\ !$787-807 #domain transmembrane #status predicted #label TM4\ !$816-835 #domain transmembrane #status predicted #label TM5\ !$40,112,141,148,186, !$214,233,244,340, !$368,399,406,411, !$422,483,490,550, !$557,752 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 859 #molecular-weight 97065 #checksum 6289 SEQUENCE /// ENTRY VCLJE4 #type complete TITLE env polyprotein precursor (clone P3.2-5) - equine infectious anemia virus CONTAINS coat protein gp45; coat protein gp90 ORGANISM #formal_name equine infectious anemia virus #note host Equus caballus (domestic horse) DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Jul-1999 ACCESSIONS D34027 REFERENCE A34027 !$#authors Payne, S.L.; Fang, F.D.; Liu, C.P.; Dhruva, B.R.; Rwambo, !1P.; Issel, C.J.; Montelaro, R.C. !$#journal Virology (1987) 161:321-331 !$#title Antigenic variation and lentivirus persistence: variations !1in envelope gene sequences during EIAV infection resemble !1changes reported for sequential isolates of HIV. !$#cross-references MUID:88072070; PMID:2825406 !$#accession D34027 !'##molecule_type genomic RNA !'##residues 1-860 ##label PAY !'##cross-references GB:M18388; NID:g323841; PIDN:AAA66410.1; !1PID:g323842 GENETICS !$#gene env CLASSIFICATION #superfamily equine infectious anemia virus env polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; transmembrane !1protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-445 #product coat protein gp90 #status predicted #label !8CP1\ !$75-93 #domain transmembrane #status predicted #label TM1\ !$446-860 #product coat protein gp45 #status predicted #label !8CP2\ !$447-463 #domain transmembrane #status predicted #label TM2\ !$615-637 #domain transmembrane #status predicted #label TM3\ !$788-808 #domain transmembrane #status predicted #label TM4\ !$817-836 #domain transmembrane #status predicted #label TM5\ !$40,112,141,148,186, !$201,214,235,244, !$308,337,340,346, !$369,400,407,412, !$423,484,491,551, !$558,753 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 860 #molecular-weight 97020 #checksum 7989 SEQUENCE /// ENTRY VCLJWS #type complete TITLE env polyprotein precursor - equine infectious anemia virus (strain WSU5) CONTAINS coat protein gp45; coat protein gp90 ORGANISM #formal_name equine infectious anemia virus #note host Equus caballus (domestic horse) DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Jul-1999 ACCESSIONS S07589 REFERENCE S07589 !$#authors McGuire, T.C.; Lacy, P.A.; O'Rourke, K.I. !$#journal Nucleic Acids Res. (1990) 18:196 !$#title cDNA sequence of the env gene of a pathogenic equine !1infectious anemia lentivirus variant. !$#cross-references MUID:90174929; PMID:2155398 !$#accession S07589 !'##status translation not shown !'##molecule_type genomic RNA !'##residues 1-859 ##label MCG !'##cross-references EMBL:X16988; NID:g59246; PIDN:CAA34856.1; !1PID:g59247 GENETICS !$#gene env CLASSIFICATION #superfamily equine infectious anemia virus env polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; transmembrane !1protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-444 #product coat protein gp90 #status predicted #label !8GP1\ !$75-93 #domain transmembrane #status predicted #label TM1\ !$445-859 #product coat protein gp45 #status predicted #label !8GP2\ !$446-462 #domain transmembrane #status predicted #label TM2\ !$614-636 #domain transmembrane #status predicted #label TM3\ !$787-807 #domain transmembrane #status predicted #label TM4\ !$816-835 #domain transmembrane #status predicted #label TM5\ !$40,112,141,148,186, !$214,233,244,313, !$340,368,399,406, !$411,483,490,550, !$557,752 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 859 #molecular-weight 97105 #checksum 8021 SEQUENCE /// ENTRY VCLJVS #type complete TITLE env polyprotein precursor - Maedi/Visna virus (strain 1514) ALTERNATE_NAMES coat polyprotein ORGANISM #formal_name Maedi/Visna virus #note host Homo sapiens (man) DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 16-Feb-1997 ACCESSIONS A03977 REFERENCE A90869 !$#authors Sonigo, P.; Alizon, M.; Staskus, K.; Klatzmann, D.; Cole, !1S.; Danos, O.; Retzel, E.; Tiollais, P.; Haase, A.; !1Wain-Hobson, S. !$#journal Cell (1985) 42:369-382 !$#title Nucleotide sequence of the visna lentivirus: relationship to !1the AIDS virus. !$#cross-references MUID:85254938; PMID:2410140 !$#accession A03977 !'##molecule_type DNA !'##residues 1-982 ##label SON GENETICS !$#gene env CLASSIFICATION #superfamily visna lentivirus type E retrovirus env !1polyprotein KEYWORDS capsid protein; coat protein; glycoprotein; polyprotein; !1transmembrane protein FEATURE !$1-100 #domain signal sequence #status predicted #label SIG\ !$101-656 #product exterior membrane glycoprotein #status !8predicted #label EXT\ !$657-982 #product transmembrane glycoprotein #status predicted !8#label TMM\ !$140,161,206,258, !$298,364,370,381, !$387,403,414,435, !$439,470,475,481, !$491,501,515,527, !$537,542,543,568 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$697,764,771,787,821 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 982 #molecular-weight 113978 #checksum 8142 SEQUENCE /// ENTRY E45390 #type complete TITLE env polyprotein precursor - Maedi/Visna virus (strain KV1772) (provirus) ALTERNATE_NAMES coat polyprotein CONTAINS exterior membrane glycoprotein; transmembrane glycoprotein ORGANISM #formal_name Maedi/Visna virus #note host Homo sapiens (man) DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS E45390 REFERENCE A45390 !$#authors Andresson, O.S.; Elser, J.E.; Tobin, G.J.; Greenwood, J.D.; !1Gonda, M.A.; Georgsson, G.; Andresdottir, V.; !1Benediktsdottir, E.; Carlsdottir, H.M.; Maentylae, E.O.; !1Rafnar, B.; Palsson, P.A.; Casey, J.W.; Petursson, G. !$#journal Virology (1993) 193:89-105 !$#title Nucleotide sequence and biological properties of a !1pathogenic proviral molecular clone of neurovirulent visna !1virus. !$#cross-references MUID:93174981; PMID:8382414 !$#accession E45390 !'##molecule_type DNA !'##residues 1-983 ##label AND !'##cross-references GB:S55323; NID:g265825; PIDN:AAB25463.1; !1PID:g265830 GENETICS !$#gene env CLASSIFICATION #superfamily visna lentivirus type E retrovirus env !1polyprotein KEYWORDS capsid protein; coat protein; glycoprotein; polyprotein; !1transmembrane protein FEATURE !$1-100 #domain signal sequence #status predicted #label SIG\ !$101-656 #product exterior membrane glycoprotein #status !8predicted #label EXT\ !$657-983 #product transmembrane glycoprotein #status predicted !8#label TMM\ !$836-852 #domain transmembrane #status predicted #label TMN\ !$140,161,206,258, !$298,364,381,387, !$403,414,435,439, !$470,475,481,491, !$501,515,527,537, !$542,543,568,697, !$765,772,788,822 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 983 #molecular-weight 113939 #checksum 9332 SEQUENCE /// ENTRY G46335 #type complete TITLE env polyprotein precursor - Maedi/Visna virus (strain SA-OMVV) ALTERNATE_NAMES coat polyprotein CONTAINS exterior membrane glycoprotein; transmembrane glycoprotein ORGANISM #formal_name Maedi/Visna virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS G46335 REFERENCE A46335 !$#authors Querat, G.; Audoly, G.; Sonigo, P.; Vigne, R. !$#journal Virology (1990) 175:434-447 !$#title Nucleotide sequence analysis of SA-OMVV, a visna-related !1ovine lentivirus: phylogenetic history of lentiviruses. !$#cross-references MUID:90223989; PMID:2158181 !$#accession G46335 !'##molecule_type DNA !'##residues 1-990 ##label QUE !'##cross-references GB:M31646; NID:g808756; PIDN:AAA66817.1; !1PID:g332551 GENETICS !$#gene env CLASSIFICATION #superfamily visna lentivirus type E retrovirus env !1polyprotein KEYWORDS capsid protein; coat protein; glycoprotein; polyprotein; !1transmembrane protein FEATURE !$1-101 #domain signal sequence #status predicted #label SIG\ !$102-662 #product exterior membrane glycoprotein #status !8predicted #label EXT\ !$663-990 #product transmembrane glycoprotein #status predicted !8#label TMM\ !$663-689 #region hydrophobic\ !$842-863 #domain transmembrane #status predicted #label TMN\ !$141,162,207,259, !$299,363,386,402, !$413,434,438,469, !$474,480,490,500, !$514,526,536,542, !$550,560,567,703, !$771,778,794 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 990 #molecular-weight 114498 #checksum 9058 SEQUENCE /// ENTRY VCLJC6 #type complete TITLE env polyprotein precursor - caprine arthritis-encephalitis virus (strain 63) ALTERNATE_NAMES coat polyprotein CONTAINS surface protein; transmembrane protein ORGANISM #formal_name caprine arthritis-encephalitis virus, CAEV DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 01-Mar-1996 ACCESSIONS A41307 REFERENCE A41307 !$#authors Knowles Jr., D.P.; Cheevers, W.P.; McGuire, T.C.; !1Brassfield, A.L.; Harwood, W.G.; Stem, T.A. !$#journal J. Virol. (1991) 65:5744-5750 !$#title Structure and genetic variability of envelope glycoproteins !1of two antigenic variants of caprine arthritis-encephalitis !1lentivirus. !$#cross-references MUID:92015464; PMID:1656067 !$#accession A41307 !'##molecule_type mRNA !'##residues 1-964 ##label KNO !'##cross-references GB:M60855 GENETICS !$#gene env CLASSIFICATION #superfamily visna lentivirus type E retrovirus env !1polyprotein KEYWORDS capsid protein; coat protein; glycoprotein; polyprotein; !1transmembrane protein FEATURE !$1-631 #domain extracellular #status predicted #label EX1\ !$1-60 #domain signal sequence #status predicted #label SIG\ !$61-964 #product env polyprotein #status predicted #label !8ENV\ !$61-630 #product surface protein #status predicted #label !8SUP\ !$627-630 #region cleavage processing #status predicted\ !$631-964 #product transmembrane protein #status predicted !8#label TMP\ !$631-659 #domain transmembrane #status predicted #label TM1\ !$660-794 #domain intracellular #status predicted #label INT\ !$795-836 #domain transmembrane #status predicted #label TM2\ !$837-964 #domain extracellular #status predicted #label EX2\ !$51,98,131,176,331, !$348,379,404,435, !$441,467,481,493, !$509,534 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 964 #molecular-weight 110930 #checksum 695 SEQUENCE /// ENTRY VCLJCC #type complete TITLE env polyprotein precursor - caprine arthritis-encephalitis virus (strain Co) ALTERNATE_NAMES coat polyprotein CONTAINS surface protein; transmembrane protein ORGANISM #formal_name caprine arthritis-encephalitis virus, CAEV DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS B41307; E45345 REFERENCE A41307 !$#authors Knowles Jr., D.P.; Cheevers, W.P.; McGuire, T.C.; !1Brassfield, A.L.; Harwood, W.G.; Stem, T.A. !$#journal J. Virol. (1991) 65:5744-5750 !$#title Structure and genetic variability of envelope glycoproteins !1of two antigenic variants of caprine arthritis-encephalitis !1lentivirus. !$#cross-references MUID:92015464; PMID:1656067 !$#accession B41307 !'##molecule_type mRNA !'##residues 1-966 ##label KNO !'##cross-references GB:M60855 REFERENCE A45345 !$#authors Saltarelli, M.; Querat, G.; Konings, D.A.M.; Vigne, R.; !1Clements, J.E. !$#journal Virology (1990) 179:347-364 !$#title Nucleotide sequence and transcriptional analysis of !1molecular clones of CAEV which generate infectious virus. !$#cross-references MUID:91021037; PMID:2171210 !$#accession E45345 !'##molecule_type genomic RNA !'##residues 1-40,'Q',42-46,'Q',48-54,'P',56-833,'Q',835-935,'DC', !1938-940,'A',942,'ED' ##label SAL !'##cross-references GB:M33677; NID:g323294; PIDN:AAA91829.1; !1PID:g323299 GENETICS !$#gene env CLASSIFICATION #superfamily visna lentivirus type E retrovirus env !1polyprotein KEYWORDS capsid protein; coat protein; glycoprotein; polyprotein; !1transmembrane protein FEATURE !$1-63 #domain signal sequence #status predicted #label SIG\ !$64-966 #product env polyprotein #status predicted #label !8ENV\ !$64-632 #product surface protein #status predicted #label !8SUP\ !$629-632 #region cleavage processing #status predicted\ !$633-966 #product transmembrane protein #status predicted !8#label TMP\ !$633-661 #region hydrophobic #status predicted\ !$797-838 #domain transmembrane #status predicted #label TM1\ !$101,134,179,220, !$334,351,357,382, !$407,438,443,469, !$483,495,511,536 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 966 #molecular-weight 110291 #checksum 9500 SEQUENCE /// ENTRY VCLJB #type complete TITLE env polyprotein - bovine leukemia virus ALTERNATE_NAMES coat polyprotein CONTAINS coat protein gp30; coat protein gp51 ORGANISM #formal_name bovine leukemia virus, BLV #note host Bos sp. (cattle) DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 16-Jul-1999 ACCESSIONS B94063; A94332; S29359; A03978 REFERENCE A94063 !$#authors Sagata, N.; Yasunaga, T.; Tsuzuku-Kawamura, J.; Ohishi, K.; !1Ogawa, Y.; Ikawa, Y. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:677-681 !$#title Complete nucleotide sequence of the genome of bovine !1leukemia virus: its evolutionary relationship to other !1retroviruses. !$#cross-references MUID:85140159; PMID:2983308 !$#accession B94063 !'##molecule_type DNA !'##residues 1-515 ##label SAG !'##cross-references GB:K02120; NID:g210767; PIDN:AAA42786.1; !1PID:g210770 !'##note the authors translated the codon CTC for residue 403 as Arg and !1CGC for residue 404 as Leu REFERENCE A94332 !$#authors Schultz, A.M.; Copeland, T.D.; Oroszlan, S. !$#journal Virology (1984) 135:417-427 !$#title The envelope proteins of bovine leukemia virus: purification !1and sequence analysis. !$#cross-references MUID:84251704; PMID:6204444 !$#accession A94332 !'##molecule_type protein !'##residues 34-71;302-310,'S',312-313 ##label SCH REFERENCE S29356 !$#authors Rice, N.R.; Stephens, R.M.; Burny, A.; Gilden, R.V. !$#journal Virology (1985) 142:357-377 !$#title The gag and pol genes of bovine leukemia virus: nucleotide !1sequence and analysis. !$#cross-references MUID:86045859; PMID:2997990 !$#accession S29359 !'##molecule_type DNA !'##residues 1-22 ##label RIC !'##cross-references EMBL:M10987; NID:g210784; PIDN:AAA42796.1; !1PID:g210787 GENETICS !$#gene env CLASSIFICATION #superfamily type C retrovirus env polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; transmembrane !1protein FEATURE !$1-33 #domain leader peptide #status predicted #label LDP\ !$17-28 #domain transmembrane #status predicted #label TM1\ !$34-301 #product coat protein gp51 #status predicted #label !8CPA\ !$268-297 #domain transmembrane #status predicted #label TM2\ !$302-515 #product coat protein gp30 #status predicted #label !8CPB\ !$303-328 #domain transmembrane #status predicted #label TM3\ !$438-457 #domain transmembrane #status predicted #label TM4\ !$67,129,203,230,251, !$256,271,287,351,398 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 515 #molecular-weight 58472 #checksum 5031 SEQUENCE /// ENTRY VCLJGA #type complete TITLE env polyprotein precursor - bovine leukemia virus (strain Australia) ALTERNATE_NAMES coat polyprotein CONTAINS coat protein gp30; coat protein gp51 ORGANISM #formal_name bovine leukemia virus, BLV #note host Bos sp. (cattle) DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 28-Jul-2000 ACCESSIONS JQ0556 REFERENCE JQ0554 !$#authors Coulston, J.; Naif, H.; Brandon, R.; Kumar, S.; Khan, S.; !1Daniel, R.C.W.; Lavin, M.F. !$#journal J. Gen. Virol. (1990) 71:1737-1746 !$#title Molecular cloning and sequencing of an Australian isolate of !1proviral bovine leukaemia virus DNA: comparison with other !1isolates. !$#cross-references MUID:90362060; PMID:2167927 !$#accession JQ0556 !'##molecule_type DNA !'##residues 1-515 ##label COU !'##cross-references DDBJ:D00647; NID:g2920795; PIDN:BAA00545.1; !1PID:g221054 GENETICS !$#gene env CLASSIFICATION #superfamily type C retrovirus env polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; transmembrane !1protein FEATURE !$1-303 #domain extracellular #status predicted #label EX1\ !$1-33 #domain signal sequence #status predicted #label SIG\ !$34-515 #product env polyprotein #status predicted #label !8ENV\ !$34-301 #product coat protein gp51 #status predicted #label !8MAT\ !$298-301 #region cleavage processing #status predicted\ !$302-515 #product coat protein gp30 #status predicted #label !8MAC\ !$304-320 #domain transmembrane #status predicted #label TM1\ !$321-440 #domain intracellular #status predicted #label INT\ !$441-457 #domain transmembrane #status predicted #label TM2\ !$458-515 #domain extracellular #status predicted #label EX2\ !$129,203,230,251, !$256,271,287 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 515 #molecular-weight 58445 #checksum 4795 SEQUENCE /// ENTRY VCVWH #type complete TITLE env polyprotein - human T-cell lymphotropic virus type 1 ORGANISM #formal_name human T-cell lymphotropic virus type 1, HTLV-1 DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 16-Jul-1999 ACCESSIONS A03979 REFERENCE A93954 !$#authors Seiki, M.; Hattori, S.; Hirayama, Y.; Yoshida, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:3618-3622 !$#title Human adult T-cell leukemia virus: complete nucleotide !1sequence of the provirus genome integrated in leukemia cell !1DNA. !$#cross-references MUID:83221647; PMID:6304725 !$#accession A03979 !'##molecule_type DNA !'##residues 1-488 ##label SEI !'##cross-references GB:J02029; GB:M33896; NID:g425135; PIDN:AAA96674.1; !1PID:g331149 !'##experimental_source strain ATK GENETICS !$#gene env CLASSIFICATION #superfamily type C retrovirus env polyprotein KEYWORDS polyprotein SUMMARY #length 488 #molecular-weight 53948 #checksum 656 SEQUENCE /// ENTRY VCLJCN #type complete TITLE env polyprotein - human T-cell lymphotropic virus type 1 (isolate Caribbean) CONTAINS coat protein p21; surface glycoprotein gp46 ORGANISM #formal_name human T-cell lymphotropic virus type 1, HTLV-1 #note host Homo sapiens (man) DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jun-2000 ACCESSIONS D28136 REFERENCE A92797 !$#authors Malik, K.T.A.; Even, J.; Karpas, A. !$#journal J. Gen. Virol. (1988) 69:1695-1710 !$#title Molecular cloning and complete nucleotide sequence of an !1adult T cell leukaemia virus/human T cell leukaemia virus !1type I (ATLV/HTLV-I) isolate of Caribbean origin: !1relationship to other members of the ATLV/HTLV-I subgroup. !$#cross-references MUID:88274338; PMID:2899128 !$#accession D28136 !'##molecule_type DNA !'##residues 1-488 ##label MAL !'##cross-references GB:D13784; GB:D00294; NID:g221866; PIDN:BAA02932.1; !1PID:g221870 GENETICS !$#gene env CLASSIFICATION #superfamily type C retrovirus env polyprotein KEYWORDS coat protein; glycoprotein; polyprotein FEATURE !$1-312 #product surface glycoprotein gp46 #status predicted !8#label SGP\ !$313-488 #product coat protein p21 #status predicted #label !8TMP\ !$140,222,244,272,404 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 488 #molecular-weight 53912 #checksum 1432 SEQUENCE /// ENTRY VCLJMT #type complete TITLE env polyprotein - human T-cell lymphotropic virus type 1 (isolate MT-2) CONTAINS coat protein p21; surface glycoprotein gp46 ORGANISM #formal_name human T-cell lymphotropic virus type 1, HTLV-1 #note host Homo sapiens (man) DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS A35323; G41281 REFERENCE A35323 !$#authors Gray, G.S.; White, M.; Bartman, T.; Mann, D. !$#journal Virology (1990) 177:391-395 !$#title Envelope gene sequence of HTLV-1 isolate MT-2 and its !1comparison with other HTLV-1 isolates. !$#cross-references MUID:90281609; PMID:2353464 !$#accession A35323 !'##molecule_type DNA !'##residues 1-488 ##label GRA !'##cross-references GB:M37747; NID:g331085; PIDN:AAA46185.1; !1PID:g331086 !'##experimental_source isolate MT-2 REFERENCE A41281 !$#authors Gessain, A.; Yanagihara, R.; Franchini, G.; Garruto, R.M.; !1Jenkins, C.L.; Ajdukiewicz, A.B.; Gallo, R.C.; Gajdusek, !1D.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:7694-7698 !$#title Highly divergent molecular variants of human T-lymphotropic !1virus type I from isolated populations in Papua New Guinea !1and the Solomon Islands. !$#cross-references MUID:91352055; PMID:1881912 !$#accession G41281 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type DNA !'##residues 290-463 ##label GES !'##cross-references GB:M73745 !'##experimental_source strain Bellona 1 GENETICS !$#gene env CLASSIFICATION #superfamily type C retrovirus env polyprotein KEYWORDS coat protein; glycoprotein; polyprotein FEATURE !$1-312 #product surface glycoprotein gp46 #status predicted !8#label SGG\ !$313-488 #product coat protein p21 #status predicted #label !8CPP\ !$140,222,244,272,404 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 488 #molecular-weight 53856 #checksum 696 SEQUENCE /// ENTRY VCLJT2 #type complete TITLE env polyprotein - human T-cell lymphotropic virus type 2 ORGANISM #formal_name human T-cell lymphotropic virus type 2, HTLV-2 DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 04-Oct-1996 ACCESSIONS A03980 REFERENCE A03980 !$#authors Sodroski, J.; Patarca, R.; Perkins, D.; Briggs, D.; Lee, !1T.H.; Essex, M.; Coligan, J.; Wong-Staal, F.; Gallo, R.C.; !1Haseltine, W.A. !$#journal Science (1984) 225:421-424 !$#title Sequence of the envelope glycoprotein gene of type II human !1T lymphotropic virus. !$#cross-references MUID:84250189; PMID:6204380 !$#accession A03980 !'##molecule_type genomic RNA !'##residues 1-486 ##label SOD GENETICS !$#gene env CLASSIFICATION #superfamily type C retrovirus env polyprotein KEYWORDS polyprotein SUMMARY #length 486 #molecular-weight 54184 #checksum 8444 SEQUENCE /// ENTRY VCLJH2 #type complete TITLE env polyprotein - human T-cell lymphotropic virus type 2 ALTERNATE_NAMES coat polyprotein CONTAINS coat protein gp30; coat protein gp51 ORGANISM #formal_name human T-cell lymphotropic virus type 2, HTLV-2 #note host Homo sapiens (man) DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 16-Jul-1999 ACCESSIONS A03981 REFERENCE A94042 !$#authors Shimotohno, K.; Takahashi, Y.; Shimizu, N.; Gojobori, T.; !1Golde, D.W.; Chen, I.S.Y.; Miwa, M.; Sugimura, T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:3101-3105 !$#title Complete nucleotide sequence of an infectious clone of human !1T-cell leukemia virus type II: an open reading frame for the !1protease gene. !$#cross-references MUID:85216449; PMID:2582407 !$#accession A03981 !'##molecule_type DNA !'##residues 1-486 ##label SHI !'##cross-references GB:M10060; NID:g329559; PIDN:AAB59887.1; !1PID:g329564 GENETICS !$#gene env CLASSIFICATION #superfamily type C retrovirus env polyprotein KEYWORDS capsid protein; coat protein; glycoprotein; polyprotein FEATURE !$1-308 #product coat protein gp51 #status predicted #label !8CP1\ !$309-486 #product coat protein gp30 #status predicted #label !8CP2\ !$136,218,240,286 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$400 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 486 #molecular-weight 54158 #checksum 7884 SEQUENCE /// ENTRY VCLJGL #type complete TITLE env polyprotein precursor - gibbon ape leukemia virus CONTAINS knob protein gp70; spike protein p15E ORGANISM #formal_name gibbon ape leukemia virus DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS C32595 REFERENCE A32595 !$#authors Delassus, S.; Sonigo, P.; Wain-Hobson, S. !$#journal Virology (1989) 173:205-213 !$#title Genetic organization of gibbon ape leukemia virus. !$#cross-references MUID:90051069; PMID:2683360 !$#accession C32595 !'##molecule_type genomic RNA !'##residues 1-667 ##label DEL !'##cross-references GB:M26927; NID:g332610; PIDN:AAA46811.1; !1PID:g332613 GENETICS !$#gene env CLASSIFICATION #superfamily type C retrovirus env polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; spike protein; !1transmembrane protein FEATURE !$1-42 #domain signal sequence #status predicted #label SIG\ !$43-489 #product knob protein gp70 #status predicted #label !8KPG\ !$490-667 #product spike protein p15E #status predicted #label !8SPP\ !$492-508 #domain transmembrane #status predicted #label TM1\ !$637-653 #domain transmembrane #status predicted #label TM2\ !$301,344,415,421, !$433,453,623 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 667 #molecular-weight 73729 #checksum 6637 SEQUENCE /// ENTRY VCMVHL #type complete TITLE env polyprotein precursor - HoMuLV murine leukemia virus CONTAINS knob protein gp76; spike protein p15E ORGANISM #formal_name HoMuLV murine leukemia virus #note host Mus hortulanus (European mouse) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 12-Apr-1996 ACCESSIONS B32594 REFERENCE A32594 !$#authors Voytek, P.; Kozak, C.A. !$#journal Virology (1989) 173:58-67 !$#title Nucleotide sequence and mode of transmission of the wild !1mouse ecotropic virus, HoMuLV. !$#cross-references MUID:90051094; PMID:2554579 !$#accession B32594 !'##molecule_type DNA !'##residues 1-666 ##label VOY !'##note the authors translated the codon CTT for residue 451 as Pro GENETICS !$#gene env CLASSIFICATION #superfamily type C retrovirus env polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; spike protein; !1transmembrane protein FEATURE !$1-30 #domain signal sequence #status predicted #label SIG\ !$31-466 #product knob protein gp76 #status predicted #label !8KPG\ !$467-666 #product spike protein p15E #status predicted #label !8SPP\ !$473-489 #domain transmembrane #status predicted #label TM1\ !$607-623 #domain transmembrane #status predicted #label TM2\ !$42,197,290,324,356, !$363,431,599 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 666 #molecular-weight 73034 #checksum 5336 SEQUENCE /// ENTRY VCFMLV #type fragment TITLE env polyprotein - Friend murine leukemia virus (fragment) CONTAINS envelope glycoprotein gp71; R protein; spike protein p15E ORGANISM #formal_name Friend murine leukemia virus DATE 17-Dec-1982 #sequence_revision 29-Oct-1999 #text_change 29-Oct-1999 ACCESSIONS S20285; A03995 REFERENCE S20285 !$#authors Linder, M.; Linder, D.; Hahnen, J.; Schott, H.H.; Stirm, S. !$#journal Eur. J. Biochem. (1992) 203:65-73 !$#title Localization of the intrachain disulfide bonds of the !1envelope glycoprotein 71 from Friend murine leukemia virus. !$#cross-references MUID:92111586; PMID:1730242 !$#accession S20285 !'##molecule_type protein !'##residues 1-445 ##label LIN REFERENCE A03995 !$#authors Chen, R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:5788-5792 !$#title Complete amino acid sequence and glycosylation sites of !1glycoprotein gp71A of Friend murine leukemia virus. !$#cross-references MUID:83299875; PMID:6310544 !$#accession A03995 !'##molecule_type protein !'##residues 1-183,'G',185-445 ##label CHE !'##note gp71A is the major envelope protein GENETICS !$#gene env CLASSIFICATION #superfamily type C retrovirus env polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; spike protein; !1transmembrane protein FEATURE !$1-445 #product envelope glycoprotein gp71 #status predicted !8#label GP1\ !$12,168,302,334,341, !$374,410 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$46-98,72-87,73-83, !$121-141,133-146, !$178-184,312-315, !$342-396,361-373, !$403-416 #disulfide_bonds #status experimental\ !$268,277,279,304,309 #binding_site carbohydrate (Thr) (covalent) #status !8predicted\ !$273,275 #binding_site carbohydrate (Ser) (covalent) #status !8predicted SUMMARY #length 445 #checksum 7485 SEQUENCE /// ENTRY VCVWEM #type complete TITLE env polyprotein - Moloney murine leukemia virus CONTAINS knob protein gp70; R protein; spike protein p15E ORGANISM #formal_name Moloney murine leukemia virus DATE 01-Sep-1981 #sequence_revision 24-Sep-1981 #text_change 16-Jul-1999 ACCESSIONS A93265; A93235; A93848; A03983 REFERENCE A93265 !$#authors Shinnick, T.M.; Lerner, R.A.; Sutcliffe, J.G. !$#journal Nature (1981) 293:543-548 !$#title Nucleotide sequence of Moloney murine leukaemia virus. !$#cross-references MUID:82035843; PMID:6169994 !$#accession A93265 !'##molecule_type genomic RNA !'##residues 1-665 ##label SHI !'##cross-references GB:J02255; GB:J02256; GB:J02257; GB:M76668; !1NID:g331934; PIDN:AAB59943.1; PID:g331936 !'##experimental_source clone pMLV-1 REFERENCE A93235 !$#authors Sutcliffe, J.G.; Shinnick, T.M.; Green, N.; Liu, F.T.; !1Niman, H.L.; Lerner, R.A. !$#journal Nature (1980) 287:801-805 !$#title Chemical synthesis of a polypeptide predicted from !1nucleotide sequence allows detection of a new retroviral !1gene product. !$#cross-references MUID:81052384; PMID:6159543 !$#accession A93235 !'##molecule_type genomic RNA !'##residues 496-665 ##label SUT1 !'##experimental_source provirus REFERENCE A93848 !$#authors Sutcliffe, J.G.; Shinnick, T.M.; Verma, I.M.; Lerner, R.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1980) 77:3302-3306 !$#title Nucleotide sequence of Moloney leukemia virus: 3' end !1reveals details of replication, analogy to bacterial !1transposons, and an unexpected gene. !$#cross-references MUID:81013872; PMID:6251454 !$#accession A93848 !'##molecule_type DNA !'##residues 484-662,'CEF' ##label SUT2 !'##experimental_source provirus, clone pMLV-201 GENETICS !$#gene env CLASSIFICATION #superfamily type C retrovirus env polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; spike protein; !1transmembrane protein FEATURE !$34-469 #product knob protein gp70 #status predicted #label !8KNB\ !$470-649 #product spike protein p15E #status predicted #label !8SPK\ !$650-665 #product R protein #status predicted #label RPT\ !$45,199,326,358,398, !$434 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 665 #molecular-weight 73301 #checksum 7546 SEQUENCE /// ENTRY VCVWEK #type complete TITLE env polyprotein - AKV murine leukemia virus CONTAINS knob protein gp76; R protein; spike protein p15E ORGANISM #formal_name AKV murine leukemia virus DATE 05-Apr-1983 #sequence_revision 03-Aug-1984 #text_change 16-Jul-1999 ACCESSIONS A92995; A93448; A03984 REFERENCE A92995 !$#authors Herr, W. !$#journal J. Virol. (1984) 49:471-478 !$#title Nucleotide sequence of AKV murine leukemia virus. !$#cross-references MUID:84115072; PMID:6319746 !$#accession A92995 !'##molecule_type genomic RNA !'##residues 1-669 ##label HER !'##cross-references GB:J01998; GB:J01999; GB:K00016; GB:K00017; !1GB:K00018; GB:K01394; NID:g331993; PIDN:AAB03092.1; !1PID:g331996 REFERENCE A93448 !$#authors Herr, W.; Corbin, V.; Gilbert, W. !$#journal Nucleic Acids Res. (1982) 10:6931-6944 !$#title Nucleotide sequence of the 3' half of AKV. !$#cross-references MUID:83090450; PMID:6294621 !$#accession A93448 !'##molecule_type DNA !'##residues 1-34,'R',36-462,'K',464-591,'K',593-669 ##label HE2 GENETICS !$#gene env CLASSIFICATION #superfamily type C retrovirus env polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; spike protein; !1transmembrane protein FEATURE !$1-31 #domain signal sequence #status predicted #label SIG\ !$32-470 #product knob protein gp76 #status predicted #label !8KNB\ !$471-650 #product spike protein p15E #status predicted #label !8SPK\ !$651-669 #product R protein #status predicted #label RPT\ !$43,199,327,359,399 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 669 #molecular-weight 73756 #checksum 1198 SEQUENCE /// ENTRY VCMVVR #type complete TITLE env polyprotein precursor - radiation murine leukemia virus ALTERNATE_NAMES coat polyprotein CONTAINS coat protein gp76; coat protein p15E; R protein ORGANISM #formal_name radiation murine leukemia virus DATE 31-Mar-1989 #sequence_revision 31-Mar-1993 #text_change 07-Nov-1997 ACCESSIONS C26183 REFERENCE A94362 !$#authors Merregaert, J.; Janowski, M.; Reddy, E.P. !$#journal Virology (1987) 158:88-102 !$#title Nucleotide sequence of a radiation leukemia virus genome. !$#cross-references MUID:87207680; PMID:3033897 !$#accession C26183 !'##molecule_type DNA !'##residues 1-665 ##label MER !'##cross-references GB:K03363; GB:M18449; NID:g332032 GENETICS !$#gene env CLASSIFICATION #superfamily type C retrovirus env polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; spike protein; !1transmembrane protein FEATURE !$1-31 #domain signal sequence #status predicted #label SIG\ !$32-665 #product env polyprotein #status predicted #label !8ENV\ !$32-604 #domain extracellular #status predicted #label EXT\ !$32-467 #product coat protein gp76 #status predicted #label !8GP1\ !$464-467 #region cleavage processing #status predicted\ !$468-644 #product coat protein p15E #status predicted #label !8GP2\ !$474-490 #region hydrophobic #status predicted\ !$605-621 #domain transmembrane #status predicted #label TM1\ !$622-665 #domain intracellular #status predicted #label INT\ !$645-665 #product R protein #status predicted #label RPP\ !$43,199,211,324,356, !$396,400,432 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 665 #molecular-weight 73083 #checksum 1391 SEQUENCE /// ENTRY VCMVKA #type complete TITLE env polyprotein precursor - radiation murine leukemia virus (strain Kaplan) ALTERNATE_NAMES coat polyprotein CONTAINS coat protein gp76; coat protein p15E; R protein ORGANISM #formal_name radiation murine leukemia virus DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS B42743 REFERENCE A42743 !$#authors Poliquin, L.; Bergeron, D.; Fortier, J.L.; Paquette, Y.; !1Bergeron, R.; Rassart, E. !$#journal J. Virol. (1992) 66:5141-5146 !$#title Determinants of thymotropism in Kaplan radiation leukemia !1virus and nucleotide sequence of its envelope region. !$#cross-references MUID:92333703; PMID:1629969 !$#accession B42743 !'##molecule_type DNA !'##residues 1-665 ##label POL !'##cross-references GB:M93052; NID:g332065; PIDN:AAA46526.1; !1PID:g332067 GENETICS !$#gene env CLASSIFICATION #superfamily type C retrovirus env polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; spike protein; !1transmembrane protein FEATURE !$1-31 #domain signal sequence #status predicted #label SIG\ !$32-665 #product env polyprotein #status predicted #label !8ENV\ !$32-604 #domain extracellular #status predicted #label EXT\ !$32-467 #product coat protein gp76 #status predicted #label !8GP1\ !$464-467 #region cleavage processing #status predicted\ !$468-644 #product coat protein p15E #status predicted #label !8GP2\ !$474-490 #region hydrophobic #status predicted\ !$605-621 #domain transmembrane #status predicted #label TM1\ !$622-665 #domain intracellular #status predicted #label INT\ !$645-665 #product R protein #status predicted #label RPP\ !$43,199,211,324,356, !$396,400,432 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 665 #molecular-weight 73085 #checksum 2495 SEQUENCE /// ENTRY VCMVPV #type complete TITLE env polyprotein precursor - Friend murine leukemia virus (strain PVC-211) ALTERNATE_NAMES coat polyprotein CONTAINS knob protein gp76; R protein; spike protein p15E ORGANISM #formal_name Friend murine leukemia virus DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS A38210; S35476 REFERENCE A38210 !$#authors Masuda, M.; Remington, M.P.; Hoffman, P.M.; Ruscetti, S.K. !$#journal J. Virol. (1992) 66:2798-2806 !$#title Molecular characterization of a neuropathogenic and !1nonerythroleukemogenic variant of Friend murine leukemia !1virus PVC-211. !$#cross-references MUID:92219364; PMID:1560524 !$#accession A38210 !'##molecule_type DNA !'##residues 1-676 ##label SPE !'##cross-references GB:M93134; NID:g331898; PIDN:AAA46478.1; !1PID:g331901 REFERENCE S35474 !$#authors Remington, M.P.; Hoffman, P.M.; Ruscetti, S.K.; Masuda, M. !$#journal Nucleic Acids Res. (1992) 20:3249 !$#title Complete nucleotide sequence of a neuropathogenic variant of !1Friend murine leukemia virus PVC-211. !$#cross-references MUID:92319660; PMID:1620621 !$#accession S35476 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-676 ##label REM !'##cross-references EMBL:M93134; NID:g331898; PIDN:AAA46478.1; !1PID:g331901 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1992 GENETICS !$#gene env CLASSIFICATION #superfamily type C retrovirus env polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; spike protein; !1transmembrane protein FEATURE !$1-35 #domain signal sequence #status predicted #label SIG\ !$36-676 #product env polyprotein #status predicted #label !8ENV\ !$36-619 #domain extracellular #status predicted #label EXT\ !$36-479 #product knob protein gp76 #status predicted #label !8KGP\ !$476-479 #region cleavage processing #status predicted\ !$480-659 #product spike protein p15E #status predicted #label !8SPP\ !$486-502 #region hydrophobic #status predicted\ !$620-636 #domain transmembrane #status predicted #label TM1\ !$637-676 #domain intracellular #status predicted #label INT\ !$660-676 #product R protein #status predicted #label RPT\ !$46,202,336,368,408, !$444 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 676 #molecular-weight 73945 #checksum 3395 SEQUENCE /// ENTRY VCVWFS #type complete TITLE env polyprotein - mink cell focus-forming virus ALTERNATE_NAMES coat polyprotein CONTAINS knob protein gp70; R protein; spike protein p15E ORGANISM #formal_name mink cell focus-forming virus DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 23-Aug-1997 ACCESSIONS A31668 REFERENCE A31668 !$#authors Chattopadhyay, S.K.; Baroudy, B.M.; Holmes, K.L.; !1Fredrickson, T.N.; Lander, M.R.; Morse III, H.C.; Hartley, !1J.W. !$#journal Virology (1989) 168:90-100 !$#title Biologic and molecular genetic characteristics of a unique !1MCF virus that is highly leukemogenic in ecotropic !1virus-negative mice. !$#cross-references MUID:89085614; PMID:2535909 !$#accession A31668 !'##molecule_type DNA !'##residues 1-636 ##label CHA GENETICS !$#gene env CLASSIFICATION #superfamily type C retrovirus env polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; spike protein; !1transmembrane protein FEATURE !$1-30 #domain signal sequence #status predicted #label SIG\ !$31-440 #product knob protein gp70 #status predicted #label !8GP7\ !$441-620 #product spike protein p15E #status predicted #label !8P1E\ !$621-636 #product R protein #status predicted #label RPT\ !$43,58,297,329,369, !$405 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 636 #molecular-weight 69113 #checksum 8603 SEQUENCE /// ENTRY VCVWM1 #type complete TITLE env polyprotein - mink cell focus-forming virus CONTAINS knob protein gp70; R protein; spike protein p15E ORGANISM #formal_name mink cell focus-forming virus DATE 20-Sep-1984 #sequence_revision 20-Sep-1984 #text_change 16-Jul-1999 ACCESSIONS A03987; B03987 REFERENCE A03987 !$#authors Mark, G.E.; Rapp, U.R. !$#journal J. Virol. (1984) 49:530-539 !$#title Envelope gene sequence of two in vitro-generated mink cell !1focus-forming murine leukemia viruses which contain the !1entire gp70 sequence of the endogenous nonecotropic parent. !$#cross-references MUID:84115078; PMID:6319752 !$#accession A03987 !'##molecule_type DNA !'##residues 1-640 ##label MAR !'##cross-references GB:K02725; NID:g331614; PIDN:AAA46375.1; !1PID:g331616 !'##experimental_source clone CI-3 !$#accession B03987 !'##molecule_type DNA !'##residues 1-314,543-640 ##label MA2 !'##experimental_source clone CI-4 CLASSIFICATION #superfamily type C retrovirus env polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; spike protein; !1transmembrane protein FEATURE !$1-30 #domain signal sequence #status predicted #label SIG\ !$31-441 #product knob protein gp70 #status predicted #label !8KNB\ !$442-621 #product spike protein #status predicted #label SPK\ !$622-640 #product R protein #status predicted #label RPT\ !$43,58,297,329,336, !$369 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 640 #molecular-weight 69726 #checksum 1810 SEQUENCE /// ENTRY VCVWM2 #type complete TITLE env polyprotein - Friend mink cell focus-forming virus CONTAINS knob protein gp70; spike protein p15E ORGANISM #formal_name Friend mink cell focus-forming virus DATE 20-Sep-1984 #sequence_revision 20-Sep-1984 #text_change 16-Jul-1999 ACCESSIONS A03989 REFERENCE A03989 !$#authors Koch, W.; Zimmermann, W.; Oliff, A.; Friedrich, R. !$#journal J. Virol. (1984) 49:828-840 !$#title Molecular analysis of the envelope gene and long terminal !1repeat of Friend mink cell focus-inducing virus: !1implications for the functions of these sequences. !$#cross-references MUID:84138778; PMID:6321768 !$#accession A03989 !'##molecule_type DNA !'##residues 1-627 ##label KOC !'##cross-references GB:M12528; NID:g331918; PIDN:AAA46483.1; !1PID:g331920 GENETICS !$#gene env CLASSIFICATION #superfamily type C retrovirus env polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; spike protein; !1transmembrane protein FEATURE !$1-32 #domain signal sequence #status predicted #label SIG\ !$33-431 #product knob protein gp70 #status predicted #label !8KNB\ !$432-627 #product spike protein p15E #status predicted #label !8SPK\ !$43,58,288,320,360, !$364,396 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 627 #molecular-weight 68327 #checksum 7097 SEQUENCE /// ENTRY VCMVRV #type complete TITLE env polyprotein precursor - Rauscher mink cell focus-forming virus CONTAINS coat protein p12E; coat protein p15E; knob protein gp70 ORGANISM #formal_name Rauscher mink cell focus-forming virus DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 16-Jul-1999 ACCESSIONS A03990 REFERENCE A93011 !$#authors Vogt, M.; Haggblom, C.; Swift, S.; Haas, M. !$#journal J. Virol. (1985) 55:184-192 !$#title Envelope gene and long terminal repeat determine the !1different biological properties of Rauscher, Friend, and !1Moloney mink cell focus-inducing viruses. !$#cross-references MUID:85237696; PMID:4009793 !$#accession A03990 !'##molecule_type DNA !'##residues 1-640 ##label VOG !'##cross-references GB:M10100; NID:g332068; PIDN:AAA46528.1; !1PID:g332070 GENETICS !$#gene env CLASSIFICATION #superfamily type C retrovirus env polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; spike protein; !1transmembrane protein FEATURE !$1-32 #domain signal sequence #status predicted #label SIG\ !$33-443 #product knob protein gp70 #status predicted #label !8KBP\ !$444-640 #product coat protein p15E #status predicted #label !8PFE\ !$444-623 #product coat protein p12E #status predicted #label !8PTE\ !$43,58,300,332,339, !$372,408,576 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 640 #molecular-weight 70071 #checksum 7876 SEQUENCE /// ENTRY VCMVSR #type complete TITLE env polyprotein - Rauscher spleen focus-forming virus ALTERNATE_NAMES coat polyprotein CONTAINS coat protein gp70; coat protein p15E ORGANISM #formal_name Rauscher spleen focus-forming virus DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 16-Jul-1999 ACCESSIONS A03988 REFERENCE A93001 !$#authors Bestwick, R.K.; Boswell, B.A.; Kabat, D. !$#journal J. Virol. (1984) 51:695-705 !$#title Molecular cloning of biologically active Rauscher spleen !1focus-forming virus and the sequences of its env gene and !1long terminal repeat. !$#cross-references MUID:84292446; PMID:6088793 !$#accession A03988 !'##molecule_type DNA !'##residues 1-408 ##label BES !'##cross-references GB:K02375; NID:g331998; PIDN:AAA46505.1; !1PID:g332000 GENETICS !$#gene env CLASSIFICATION #superfamily type C retrovirus env polyprotein KEYWORDS coat protein; glycoprotein; polyprotein FEATURE !$1-33 #domain leader peptide #status predicted #label LDP\ !$34-333 #product coat protein gp70 #status predicted #label !8CPA\ !$334-408 #product coat protein p15E #status predicted #label !8CPE\ !$43,58,297,329,378 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 408 #molecular-weight 44940 #checksum 7669 SEQUENCE /// ENTRY VCMVCE #type complete TITLE env polyprotein - feline endogenous virus ECE1 CONTAINS glycoprotein gp70; transmembrane protein p15E ORGANISM #formal_name feline endogenous virus ECE1 #note host Felis silvestris catus (domestic cat) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 23-Aug-1997 ACCESSIONS S12815; S12816 REFERENCE S12812 !$#authors Moehring, R. !$#submission submitted to the EMBL Data Library, February 1990 !$#accession S12815 !'##molecule_type DNA !'##residues 1-671 ##label MOE !'##cross-references EMBL:X51929 GENETICS !$#gene env CLASSIFICATION #superfamily type C retrovirus env polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; spike protein; !1transmembrane protein FEATURE !$1-470 #product glycoprotein gp70 #status predicted #label !8GPT\ !$471-671 #product transmembrane protein p15E #status predicted !8#label TPP\ !$169,281,326,331, !$355,358,415,435 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 671 #molecular-weight 75151 #checksum 7114 SEQUENCE /// ENTRY VCMVSA #type complete TITLE env polyprotein precursor - feline leukemia virus (strain Sarma) ALTERNATE_NAMES coat polyprotein CONTAINS knob protein gp70; spike protein p15E ORGANISM #formal_name feline leukemia virus DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jul-1999 ACCESSIONS A29013 REFERENCE A29013 !$#authors Riedel, N.; Hoover, E.A.; Gasper, P.W.; Nicolson, M.O.; !1Mullins, J.I. !$#journal J. Virol. (1986) 60:242-250 !$#title Molecular analysis and pathogenesis of the feline aplastic !1anemia retrovirus, feline leukemia virus C-Sarma. !$#cross-references MUID:86308240; PMID:3018287 !$#accession A29013 !'##molecule_type DNA !'##residues 1-639 ##label RIE !'##cross-references GB:M14331; NID:g323898; PIDN:AAA43049.1; !1PID:g323899 GENETICS !$#gene env CLASSIFICATION #superfamily type C retrovirus env polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; spike protein; !1transmembrane protein FEATURE !$1-33 #domain signal sequence #status predicted #label SIG\ !$34-442 #product knob protein #status predicted #label NOB\ !$443-639 #product spike protein #status predicted #label SPK\ !$35,43,58,299,304, !$328,331,387,407,575 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 639 #molecular-weight 71161 #checksum 4476 SEQUENCE /// ENTRY VCVWGF #type complete TITLE env polyprotein - feline leukemia virus (strain Gardner-Arnstein) CONTAINS knob protein gp70; R protein; spike protein p15E ORGANISM #formal_name feline leukemia virus #note host Felis sp. (cat) DATE 20-Sep-1984 #sequence_revision 20-Sep-1984 #text_change 16-Jul-1999 ACCESSIONS A03991 REFERENCE A92996 !$#authors Nunberg, J.H.; Williams, M.E.; Innis, M.A. !$#journal J. Virol. (1984) 49:629-632 !$#title Nucleotide sequences of the envelope genes to two isolates !1of feline leukemia virus subgroup B. !$#cross-references MUID:84115095; PMID:6319767 !$#accession A03991 !'##molecule_type DNA !'##residues 1-662 ##label NUN !'##cross-references GB:K01209; NID:g323910; PIDN:AAA43052.1; !1PID:g323911 REFERENCE A25982 !$#authors Elder, J.H.; McGee, J.S.; Munson, M.; Houghten, R.A.; !1Kloetzer, W.; Bittle, J.L.; Grant, C.K. !$#journal J. Virol. (1987) 61:8-15 !$#title Localization of neutralizing regions of the envelope gene of !1feline leukemia virus by using anti-synthetic peptide !1antibodies. !$#cross-references MUID:87061257; PMID:2431166 !$#contents annotation; peptide synthesis !$#note 27 peptides synthesized GENETICS !$#gene env CLASSIFICATION #superfamily type C retrovirus env polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; spike protein; !1transmembrane protein FEATURE !$1-33 #domain signal sequence #status predicted #label SIG\ !$34-465 #product knob protein gp70 #status predicted #label !8KPG\ !$466-645 #product spike protein p15E #status predicted #label !8SKP\ !$646-662 #product R protein #status predicted #label RRP\ !$43,58,286,322,327, !$351,354,394,410,430 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 662 #molecular-weight 73149 #checksum 3854 SEQUENCE /// ENTRY VCVWSF #type fragment TITLE env polyprotein - feline leukemia virus (strain Snyder-Theilen) (fragment) CONTAINS knob protein gp70; spike protein p15E ORGANISM #formal_name feline leukemia virus #note host Felis sp. (cat) DATE 20-Sep-1984 #sequence_revision 20-Sep-1984 #text_change 23-Aug-1997 ACCESSIONS A03992 REFERENCE A92996 !$#authors Nunberg, J.H.; Williams, M.E.; Innis, M.A. !$#journal J. Virol. (1984) 49:629-632 !$#title Nucleotide sequences of the envelope genes to two isolates !1of feline leukemia virus subgroup B. !$#cross-references MUID:84115095; PMID:6319767 !$#accession A03992 !'##molecule_type DNA !'##residues 1-534 ##label NUN GENETICS !$#gene env CLASSIFICATION #superfamily type C retrovirus env polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; spike protein; !1transmembrane protein FEATURE !$1-33 #domain signal sequence #status predicted #label SIG\ !$34-465 #product knob protein gp70 #status predicted #label !8KGP\ !$466-534 #product spike protein (fragment) #status predicted !8#label ASP\ !$43,58,286,322,327, !$351,354,430 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 534 #checksum 4476 SEQUENCE /// ENTRY VCMVFG #type complete TITLE env polyprotein - feline leukemia virus (strain A/Glasgow-1) ALTERNATE_NAMES coat polyprotein CONTAINS coat protein p15E; knob protein gp70 ORGANISM #formal_name feline leukemia virus DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 12-Apr-1996 ACCESSIONS A24300 REFERENCE A24300 !$#authors Stewart, M.A.; Warnock, M.; Wheeler, A.; Wilkie, N.; !1Mullins, J.I.; Onions, D.E.; Neil, J.C. !$#journal J. Virol. (1986) 58:825-834 !$#title Nucleotide sequences of a feline leukemia virus subgroup A !1envelope gene and long terminal repeat and evidence for the !1recombinational origin of subgroup B viruses. !$#cross-references MUID:86200439; PMID:3009890 !$#accession A24300 !'##molecule_type DNA !'##residues 1-642 ##label STE !'##note the authors translated the codon GCT for residue 158 as Thr and !1ACC for residue 331 as Asn GENETICS !$#gene env CLASSIFICATION #superfamily type C retrovirus env polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; spike protein; !1transmembrane protein FEATURE !$1-33 #domain signal sequence #status predicted #label SIG\ !$34-445 #product knob protein gp70 #status predicted #label !8GP7\ !$446-642 #product coat protein p15E #status predicted #label !8PII\ !$35,43,58,91,267, !$302,307,334,374, !$390,410,578 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 642 #molecular-weight 71040 #checksum 4006 SEQUENCE /// ENTRY VCMVLB #type fragment TITLE env polyprotein - feline leukemia virus (strain lambda-B1) (fragment) CONTAINS coat protein gp70; coat protein p15E ORGANISM #formal_name feline leukemia virus DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 16-Jul-1999 ACCESSIONS A27172 REFERENCE A27172 !$#authors Nicolaisen-Strouss, K.; Kumar, H.P.M.; Fitting, T.; Grant, !1C.K.; Elder, J.H. !$#journal J. Virol. (1987) 61:3410-3415 !$#title Natural feline leukemia virus variant escapes neutralization !1by a monoclonal antibody via an amino acid change outside !1the antibody-binding epitope. !$#cross-references MUID:88036192; PMID:2444714 !$#accession A27172 !'##molecule_type DNA !'##residues 1-662 ##label NIC !'##cross-references GB:J03448; NID:g323896; PIDN:AAA43048.1; !1PID:g323897 GENETICS !$#gene env CLASSIFICATION #superfamily type C retrovirus env polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; spike protein; !1transmembrane protein FEATURE !$1-33 #domain signal sequence #status predicted #label SIG\ !$34-465 #product coat protein gp70 #status predicted #label !8GPS\ !$466-662 #product coat protein p15E #status predicted #label !8GPT\ !$43,58,286,322,327, !$351,354,430 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 662 #checksum 4713 SEQUENCE /// ENTRY VCMVFP #type complete TITLE env polyprotein precursor (clone CFE-6) - feline leukemia virus (provirus) CONTAINS coat protein gp70; coat protein p15E ORGANISM #formal_name feline leukemia virus #note host Felis silvestris catus (domestic cat) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS A31479 REFERENCE A31479 !$#authors Kumar, D.V.; Berry, B.T.; Roy-Burman, P. !$#journal J. Virol. (1989) 63:2379-2384 !$#title Nucleotide sequence and distinctive characteristics of the !1env gene of endogenous feline leukemia provirus. !$#cross-references MUID:89199802; PMID:2539525 !$#accession A31479 !'##molecule_type DNA !'##residues 1-668 ##label KUM !'##cross-references GB:M25425; NID:g163849; PIDN:AAA30809.1; !1PID:g163850 GENETICS !$#gene env CLASSIFICATION #superfamily type C retrovirus env polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; spike protein; !1transmembrane protein FEATURE !$1-33 #domain signal sequence #status predicted #label SIG\ !$34-465 #product coat protein gp70 #status predicted #label !8GUP\ !$466-668 #product coat protein p15E #status predicted #label !8TPP\ !$43,58,286,322,327, !$351,354,394,410, !$430,597 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 668 #molecular-weight 74298 #checksum 2204 SEQUENCE /// ENTRY VCMVSS #type complete TITLE env polyprotein precursor - feline sarcoma virus (strain SM) CONTAINS coat protein gp70; coat protein p15E ORGANISM #formal_name feline sarcoma virus #note host Felis silvestris catus (domestic cat) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 12-Apr-1996 ACCESSIONS A33741 REFERENCE A33741 !$#authors Guilhot, S.; Hampe, A.; D'Auriol, L.; Galibert, F. !$#journal Virology (1987) 161:252-258 !$#title Nucleotide sequence analysis of the LTRs and env genes of !1SM-FeSV and GA-FeSV. !$#cross-references MUID:88044502; PMID:2823466 !$#accession A33741 !'##molecule_type DNA !'##residues 1-645 ##label GUI GENETICS !$#gene env CLASSIFICATION #superfamily type C retrovirus env polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; spike protein; !1transmembrane protein FEATURE !$1-36 #domain signal sequence #status predicted #label SIG\ !$37-448 #product coat protein gp70 #status predicted #label !8GUP\ !$449-645 #product coat protein p15E #status predicted #label !8GUQ\ !$38,46,61,270,305, !$310,334,337,377, !$393,413,581 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 645 #molecular-weight 71608 #checksum 7431 SEQUENCE /// ENTRY VCMVS2 #type complete TITLE env polyprotein precursor - feline sarcoma virus (strain GA) CONTAINS coat protein gp70; coat protein p15E ORGANISM #formal_name feline sarcoma virus #note host Felis silvestris catus (domestic cat) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 12-Apr-1996 ACCESSIONS B33741 REFERENCE A33741 !$#authors Guilhot, S.; Hampe, A.; D'Auriol, L.; Galibert, F. !$#journal Virology (1987) 161:252-258 !$#title Nucleotide sequence analysis of the LTRs and env genes of !1SM-FeSV and GA-FeSV. !$#cross-references MUID:88044502; PMID:2823466 !$#accession B33741 !'##molecule_type DNA !'##residues 1-642 ##label GUI GENETICS !$#gene env CLASSIFICATION #superfamily type C retrovirus env polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; spike protein; !1transmembrane protein FEATURE !$1-32 #domain signal sequence #status predicted #label SIG\ !$33-445 #product coat protein gp70 #status predicted #label !8GUP\ !$446-642 #product coat protein p15E #status predicted #label !8GUQ\ !$34,42,57,267,302, !$307,331,334,374, !$390,410,578 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 642 #molecular-weight 71064 #checksum 2110 SEQUENCE /// ENTRY VCMVCB #type complete TITLE env polyprotein - Cas-Br-E murine leukemia virus CONTAINS coat protein p15E; knob protein gp70 precursor ORGANISM #formal_name Cas-Br-E murine leukemia virus DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jul-1999 ACCESSIONS B26103 REFERENCE A26103 !$#authors Rassart, E.; Nelbach, L.; Jolicoeur, P. !$#journal J. Virol. (1986) 60:910-919 !$#title Cas-Br-E murine leukemia virus: sequencing of the !1paralytogenic region of its genome and derivation of !1specific probes to study its origin and the structure of its !1recombinant genomes in leukemic tissues. !$#cross-references MUID:87061215; PMID:3023680 !$#accession B26103 !'##molecule_type DNA !'##residues 1-661 ##label RAS !'##cross-references GB:M14702; NID:g332016; PIDN:AAA46512.1; !1PID:g332018 GENETICS !$#gene env CLASSIFICATION #superfamily type C retrovirus env polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; spike protein; !1transmembrane protein FEATURE !$1-33 #domain signal sequence #status predicted #label SIG\ !$34-465 #product knob protein gp70 #status predicted #label !8KOP\ !$466-661 #product coat protein p15E #status predicted #label !8PTE\ !$43,186,199,322,361, !$394,430,598 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 661 #molecular-weight 72624 #checksum 7142 SEQUENCE /// ENTRY VCVW5S #type complete TITLE env polyprotein (version 1) - Friend spleen focus-forming virus CONTAINS knob protein gp70; spike protein p15E ORGANISM #formal_name Friend spleen focus-forming virus DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 16-Jul-1999 ACCESSIONS A03993 REFERENCE A93966 !$#authors Clark, S.P.; Mak, T.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:5037-5041 !$#title Complete nucleotide sequence of an infectious clone of !1Friend spleen focus-forming provirus: gp55 is an envelope !1fusion glycoprotein. !$#cross-references MUID:83273746; PMID:6576374 !$#accession A03993 !'##molecule_type DNA !'##residues 1-409 ##label CLA !'##cross-references GB:K00021; NID:g331924; PIDN:AAA46487.1; !1PID:g331926 GENETICS !$#gene env CLASSIFICATION #superfamily type C retrovirus env polyprotein KEYWORDS polyprotein FEATURE !$1-32 #domain signal sequence #status predicted #label SIG\ !$33-331 #product knob protein gp70 #status predicted #label !8KNB\ !$332-409 #product spike protein p15E #status predicted #label !8SPK SUMMARY #length 409 #molecular-weight 44776 #checksum 9047 SEQUENCE /// ENTRY VCVW2S #type complete TITLE env polyprotein (version 2) - Friend spleen focus-forming virus CONTAINS knob protein gp70; spike protein p15E ORGANISM #formal_name Friend spleen focus-forming virus DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 28-May-1999 ACCESSIONS A03994 REFERENCE A03994 !$#authors Wolff, L.; Scolnick, E.; Ruscetti, S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:4718-4722 !$#title Envelope gene of the Friend spleen focus-forming virus: !1deletion and insertions in 3' gp70/p15E-encoding region have !1resulted in unique features in the primary structure of its !1protein product. !$#cross-references MUID:83273687; PMID:6308646 !$#accession A03994 !'##molecule_type DNA !'##residues 1-409 ##label WOL !'##cross-references GB:V01552; GB:J02357; NID:g62284; PIDN:CAA24793.1; !1PID:g62285 !'##experimental_source strain Lilly-Steeves GENETICS !$#gene env CLASSIFICATION #superfamily type C retrovirus env polyprotein KEYWORDS polyprotein FEATURE !$1-29 #domain signal sequence #status predicted #label SIG\ !$30-331 #product knob protein gp70 #status predicted #label !8KNB\ !$332-409 #product spike protein p15E #status predicted #label !8SPK SUMMARY #length 409 #molecular-weight 44700 #checksum 8190 SEQUENCE /// ENTRY VCVWB6 #type complete TITLE env polyprotein precursor - Friend spleen focus-forming virus (strain BB6) ALTERNATE_NAMES coat polyprotein CONTAINS knob protein gp70; spike protein p15E ORGANISM #formal_name Friend spleen focus-forming virus DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 08-Apr-1994 ACCESSIONS A41995 REFERENCE A41995 !$#authors Majumdar, M.K.; Cho, C.L.; Fox, M.T.; Eckner, K.L.; Kozak, !1S.; Kabat, D.; Geib, R.W. !$#journal J. Virol. (1992) 66:3652-3660 !$#title Mutations in the env gene of Friend spleen focus-forming !1virus overcome Fv-2(r)-mediated resistance to Friend !1virus-induced erythroleukemia. !$#cross-references MUID:92260637; PMID:1583724 !$#accession A41995 !'##molecule_type DNA !'##residues 1-356 ##label MAJ !'##cross-references GB:M90673 GENETICS !$#gene env CLASSIFICATION #superfamily type C retrovirus env polyprotein KEYWORDS coat protein; glycoprotein; polyprotein FEATURE !$1-33 #domain signal sequence #status predicted #label SIG\ !$34-356 #product env polyprotein #status predicted #label !8ENV\ !$34-330 #product knob protein gp70 #status predicted #label !8KPG\ !$331-356 #product spike protein p15E #status predicted #label !8SPP\ !$335-351 #region hydrophobic #status predicted\ !$43,58,296,328 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 356 #molecular-weight 38777 #checksum 9657 SEQUENCE /// ENTRY VCFVER #type complete TITLE env polyprotein - Rous sarcoma virus (strain Prague C) CONTAINS coat protein gp37; coat protein gp85 ORGANISM #formal_name Rous sarcoma virus DATE 01-Sep-1981 #sequence_revision 17-Dec-1982 #text_change 16-Jun-2000 ACCESSIONS A03996; S26419; S03602 REFERENCE A00632 !$#authors Schwartz, D.; Tizard, R.; Gilbert, W. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession A03996 !'##molecule_type genomic RNA !'##residues 1-603 ##label SCH !'##note as a result of base variations, a different version of this !1sequence may exist having 17-Glu, 134-Ser, 158-Ser, 334-Thr, !1383-Thr, 392-Val, 522-Glu, 541-Leu, and 567-Val REFERENCE S26417 !$#authors Kashuba, V.I.; Rynditch, A.V.; Dostalova, V.; Hlozanek, I.; !1Zubak, S.V.; Kavsan, V.M. !$#submission submitted to the EMBL Data Library, September 1992 !$#description Molecular cloning and DNA sequence analysis of duck-adapted !1variant of Rous sarcoma virus (da Pr-RSV-C). !$#accession S26419 !'##molecule_type DNA !'##residues 27-133,'S',135-145,'A',147-157,'S',159-312,'A',314-324, !1'KTT',328-331,'S',333-338,'K',340-388,'L',390-394,'S', !1396-447,'P',449-507,'Y',509-566,'V',568-603 ##label KAS !'##cross-references EMBL:X68524; NID:g61903; PIDN:CAA48536.1; !1PID:g1334938 REFERENCE S03602 !$#authors Kashuba, V.I.; Zubak, S.V.; Rynditch, A.V.; Kavsan, V.M.; !1Hlozanek, I.; Svoboda, J. !$#journal Nucleic Acids Res. (1989) 17:2120 !$#title The nucleotide sequence of the region of src gene deletion !1in transformation-defective Rous sarcoma virus adapted to !1semi-permissive host cells. !$#cross-references MUID:89183615; PMID:2538803 !$#accession S03602 !'##status translation not shown !'##molecule_type DNA !'##residues 511-566,'V',568-603 ##label KAW !'##cross-references EMBL:X13818; NID:g61893; PIDN:CAA32051.1; !1PID:g833169 GENETICS !$#gene env CLASSIFICATION #superfamily type C retrovirus env polyprotein KEYWORDS polyprotein FEATURE !$65-603 #product coat protein gp85 #status predicted #label !8P85\ !$406-603 #product coat protein gp37 #status predicted #label !8P37 SUMMARY #length 603 #molecular-weight 65660 #checksum 5554 SEQUENCE /// ENTRY VCFV37 #type fragment TITLE coat protein gp37 - Rous sarcoma virus (fragment) ORGANISM #formal_name Rous sarcoma virus DATE 18-Dec-1981 #sequence_revision 19-Feb-1984 #text_change 24-Sep-1999 ACCESSIONS B38017; B38018; A03997 REFERENCE A38017 !$#authors Czernilofsky, A.P.; Levinson, A.D.; Varmus, H.E.; Bishop, !1J.M.; Tischer, E.; Goodman, H. !$#journal Nature (1983) 301:736-738 !$#title Corrections to the nucleotide sequence of the src gene of !1Rous sarcoma virus. !$#cross-references MUID:83141780; PMID:6298633 !$#accession B38017 !'##molecule_type DNA !'##residues 1-246 ##label CZE !'##cross-references GB:L29199; GB:J02018; GB:J02026; GB:J02352; !1GB:K01194; GB:K01195; GB:N00021; NID:g459672; !1PIDN:AAA42562.1; PID:g459676 !'##experimental_source strain Schmidt-Ruppin REFERENCE A38018 !$#authors Takeya, T.; Feldman, R.A.; Hanafusa, H. !$#journal J. Virol. (1982) 44:1-11 !$#title DNA sequence of the viral and cellular src gene of chickens: !1I. Complete nucleotide sequence of an EcoRI fragment of !1recovered avian sarcoma virus which codes for gp37 and !1pp60-src. !$#cross-references MUID:83059858; PMID:6292477 !$#accession B38018 !'##molecule_type DNA !'##residues 1-20,'N',22-27,'I',29,'A',31-42,'V',44-78,'K',80-144,'H', !1146-168,'P',170-211,'IV',214-216,'I',218-237,'Y',239-246 !1##label TAK !'##cross-references GB:K00928; NID:g210187; PIDN:AAA42564.1; !1PID:g210188 !'##experimental_source strain Schmidt-Ruppin GENETICS !$#gene env CLASSIFICATION #superfamily type C retrovirus env polyprotein SUMMARY #length 246 #checksum 7807 SEQUENCE /// ENTRY VCFVUR #type complete TITLE coat protein gp37 - avian sarcoma virus UR2 ALTERNATE_NAMES env protein gp37 ORGANISM #formal_name avian sarcoma virus UR2 #note host Gallus gallus (chicken) DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 12-May-1994 ACCESSIONS A03998 REFERENCE A00635 !$#authors Neckameyer, W.S.; Wang, L.H. !$#journal J. Virol. (1985) 53:879-884 !$#title Nucleotide sequence of avian sarcoma virus UR2 and !1comparison of its transforming gene with other members of !1the tyrosine protein kinase oncogene family. !$#cross-references MUID:85135034; PMID:2983097 !$#accession A03998 !'##molecule_type genomic RNA !'##residues 1-174 ##label NEC GENETICS !$#gene env CLASSIFICATION #superfamily type C retrovirus env polyprotein KEYWORDS coat protein; polyprotein SUMMARY #length 174 #molecular-weight 19337 #checksum 4721 SEQUENCE /// ENTRY VCFVAS #type complete TITLE env polyprotein - avian spleen necrosis virus ALTERNATE_NAMES coat polyprotein CONTAINS coat protein gp22; coat protein gp73 ORGANISM #formal_name avian spleen necrosis virus DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 01-Mar-1996 ACCESSIONS A38212 REFERENCE A38212 !$#authors Kewalramani, V.N.; Panganiban, A.T.; Emerman, M. !$#journal J. Virol. (1992) 66:3026-3031 !$#title Spleen necrosis virus, an avian immunosuppressive !1retrovirus, shares a receptor with the type D simian !1retroviruses. !$#cross-references MUID:92219390; PMID:1313915 !$#accession A38212 !'##molecule_type DNA !'##residues 1-567 ##label KEW !'##cross-references GB:M87666 GENETICS !$#gene env CLASSIFICATION #superfamily type C retrovirus env polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; transmembrane !1protein FEATURE !$1-401 #domain extracellular #status predicted #label EXT\ !$1-397 #product coat protein gp73 #status predicted #label !8CP1\ !$363-379 #region hydrophobic #status predicted\ !$394-397 #region cleavage processing #status predicted\ !$398-567 #product coat protein gp22 #status predicted #label !8CP2\ !$402-418 #domain transmembrane #status predicted #label TM1\ !$419-567 #domain intracellular #status predicted #label INT\ !$245,274,306,328,335 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 567 #molecular-weight 61596 #checksum 2285 SEQUENCE /// ENTRY VCVDAR #type complete TITLE env polyprotein - avian reticuloendotheliosis virus ALTERNATE_NAMES coat polyprotein CONTAINS coat protein gp22; coat protein gp73 ORGANISM #formal_name avian reticuloendotheliosis virus DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 04-Dec-1994 ACCESSIONS A03999 REFERENCE A93003 !$#authors Wilhelmsen, K.C.; Eggleton, K.; Temin, H.M. !$#journal J. Virol. (1984) 52:172-182 !$#title Nucleotide acid sequences of the oncogene v-rel in !1reticuloendotheliosis virus strain T and its cellular !1homolog, the proto-oncogene c-rel. !$#cross-references MUID:85009850; PMID:6090694 !$#accession A03999 !'##molecule_type DNA !'##residues 1-582 ##label WIL !'##experimental_source strain A !'##note strain A is a helper virus of the strain T COMMENT Enzymatic cleavages of env polyprotein may yield mature !1proteins including coat proteins gp73 and gp22. However, !1exact cleavage sites are undetermined. GENETICS !$#gene env CLASSIFICATION #superfamily type C retrovirus env polyprotein KEYWORDS coat protein; polyprotein SUMMARY #length 582 #molecular-weight 64138 #checksum 1162 SEQUENCE /// ENTRY VCLJSA #type complete TITLE env polyprotein - simian AIDS retrovirus SRV-1 ALTERNATE_NAMES coat polyprotein CONTAINS coat protein gp20; coat protein gp70 ORGANISM #formal_name simian AIDS retrovirus SRV-1 #note host Macaca mulatta (rhesus macaque) DATE 13-Aug-1986 #sequence_revision 13-Aug-1986 #text_change 16-Jul-1999 ACCESSIONS A04000 REFERENCE A94711 !$#authors Power, M.D.; Marx, P.A.; Bryant, M.L.; Gardner, M.B.; Barr, !1P.J.; Luciw, P.A. !$#journal Science (1986) 231:1567-1572 !$#title Nucleotide sequence of SRV-1, a type D simian acquired !1immune deficiency syndrome retrovirus. !$#cross-references MUID:86151668; PMID:3006247 !$#accession A04000 !'##molecule_type DNA !'##residues 1-587 ##label POW !'##cross-references GB:M11841; NID:g334746; PIDN:AAA47733.1; !1PID:g334750 COMMENT The env polyprotein contains coat protein gp70 and coat !1protein gp20; however, the precise boundaries of the protein !1have not been defined. GENETICS !$#gene env CLASSIFICATION #superfamily type C retrovirus env polyprotein KEYWORDS capsid protein; coat protein; glycoprotein; polyprotein FEATURE !$120,237,266,271, !$277,280,295,308, !$322,328,340,358, !$488,585 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 587 #molecular-weight 64474 #checksum 2704 SEQUENCE /// ENTRY VCLJMP #type complete TITLE env polyprotein - Mason-Pfizer monkey virus ALTERNATE_NAMES coat polyprotein CONTAINS coat protein gp20; coat protein gp70 ORGANISM #formal_name Mason-Pfizer monkey virus DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 16-Jul-1999 ACCESSIONS D25839 REFERENCE A90878 !$#authors Sonigo, P.; Barker, C.; Hunter, E.; Wain-Hobson, S. !$#journal Cell (1986) 45:375-385 !$#title Nucleotide sequence of Mason-Pfizer monkey virus: an !1immunosuppressive D-type retrovirus. !$#cross-references MUID:86189951; PMID:2421920 !$#accession D25839 !'##molecule_type DNA !'##residues 1-586 ##label SON !'##cross-references GB:M12349; NID:g334702; PIDN:AAA47712.1; !1PID:g334705 !'##experimental_source clone 6A GENETICS !$#gene env CLASSIFICATION #superfamily type C retrovirus env polyprotein KEYWORDS capsid protein; coat protein; glycoprotein; polyprotein FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-394 #product coat protein gp70 #status predicted #label !8GP7\ !$395-586 #product coat protein gp20 #status predicted #label !8GP2\ !$120,237,264,276, !$291,304,318,324, !$339,357,487 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 586 #molecular-weight 63882 #checksum 3146 SEQUENCE /// ENTRY VCMVM7 #type complete TITLE env polyprotein - baboon endogenous virus (strain M7) ALTERNATE_NAMES coat polyprotein CONTAINS coat protein gp70; coat protein p20E ORGANISM #formal_name baboon endogenous virus #note host Papio sp. (baboon) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS JT0262 REFERENCE JT0260 !$#authors Kato, S.; Matsuo, K.; Nishimura, N.; Takahashi, N.; Takano, !1T. !$#journal Jpn. J. Genet. (1987) 62:127-137 !$#title The entire nucleotide sequence of baboon endogenous virus !1DNA: a chimeric genome structure of murine type C and simian !1type D retroviruses. !$#accession JT0262 !'##molecule_type DNA !'##residues 1-563 ##label KAT !'##cross-references GB:M16550; NID:g509586; PIDN:AAA87333.1; !1PID:g332599 GENETICS !$#gene env CLASSIFICATION #superfamily type C retrovirus env polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; transmembrane !1protein FEATURE !$1-376 #product coat protein gp70 #status predicted #label !8CGP\ !$377-563 #product coat protein p20E #status predicted #label !8CPP\ !$437-449 #region immunosuppressive peptide #status predicted\ !$113,219,229,264, !$282,292,306,312, !$321,339,469 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 563 #molecular-weight 61879 #checksum 3481 SEQUENCE /// ENTRY VCLJHD #type complete TITLE env polyprotein precursor - squirrel monkey retrovirus SMRV-H ALTERNATE_NAMES coat polyprotein CONTAINS coat protein gp20; outer membrane protein ORGANISM #formal_name squirrel monkey retrovirus SMRV-H DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS D31827 REFERENCE A31827 !$#authors Oda, T.; Ikeda, S.; Watanabe, S.; Hatsushika, M.; Akiyama, !1K.; Mitsunobu, F. !$#journal Virology (1988) 167:468-476 !$#title Molecular cloning, complete nucleotide sequence, and gene !1structure of the provirus genome of a retrovirus produced in !1a human lymphoblastoid cell line. !$#cross-references MUID:89073750; PMID:3201749 !$#accession D31827 !'##molecule_type DNA !'##residues 1-575 ##label ODA !'##cross-references GB:M23385; NID:g332626; PIDN:AAA66455.1; !1PID:g332627 GENETICS !$#gene env CLASSIFICATION #superfamily type C retrovirus env polyprotein KEYWORDS capsid protein; coat protein; glycoprotein; polyprotein; !1transmembrane protein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-386 #product outer membrane protein #status predicted !8#label OMP\ !$387-575 #product coat protein gp20 #status predicted #label !8TMP\ !$387-403 #domain transmembrane #status predicted #label TM1\ !$447-481 #region immunosuppressive peptide\ !$518-534 #domain transmembrane #status predicted #label TM2\ !$126,239,266,271, !$302,316,322,349,479 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 575 #molecular-weight 62245 #checksum 8534 SEQUENCE /// ENTRY VCLJSP #type complete TITLE env polyprotein - human foamy virus ALTERNATE_NAMES coat polyprotein ORGANISM #formal_name human foamy virus #note host Homo sapiens (man) DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS C29685 REFERENCE A91074 !$#authors Fluegel, R.M.; Rethwilm, A.; Maurer, B.; Darai, G. !$#journal EMBO J. (1987) 6:2077-2084 !$#title Nucleotide sequence analysis of the env gene and its !1flanking regions of the human spumaretrovirus reveals two !1novel genes. !$#cross-references MUID:88004420; PMID:2820721 !$#accession C29685 !'##molecule_type genomic RNA !'##residues 1-985 ##label FLU !'##cross-references GB:X05591; GB:Y00070; NID:g61759; PIDN:CAA29086.1; !1PID:g61762 GENETICS !$#gene env CLASSIFICATION #superfamily foamy virus env polyprotein KEYWORDS coat protein; polyprotein; transmembrane protein FEATURE !$64-87 #domain transmembrane #status predicted #label TN1\ !$579-595 #domain transmembrane #status predicted #label TN2\ !$936-972 #domain transmembrane #status predicted #label TN3 SUMMARY #length 985 #molecular-weight 113494 #checksum 7371 SEQUENCE /// ENTRY VCLJSF #type complete TITLE env polyprotein - simian foamy virus (type 1) ALTERNATE_NAMES coat polyprotein ORGANISM #formal_name simian foamy virus DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS B33562; A39924 REFERENCE A33562 !$#authors Mergia, A.; Shaw, K.E.S.; Lackner, J.E.; Luciw, P.A. !$#journal J. Virol. (1990) 64:406-410 !$#title Relationship of the env genes and the endonuclease domain of !1the pol genes of simian foamy virus type 1 and human foamy !1virus. !$#cross-references MUID:90080148; PMID:2152825 !$#accession B33562 !'##molecule_type DNA !'##residues 1-985 ##label MER !'##cross-references GB:M33561; NID:g334867; PIDN:AAA47794.1; !1PID:g334869 GENETICS !$#gene env CLASSIFICATION #superfamily foamy virus env polyprotein KEYWORDS coat protein; polyprotein; transmembrane protein FEATURE !$64-87 #domain transmembrane #status predicted #label TN1\ !$579-595 #domain transmembrane #status predicted #label TN2\ !$958-978 #domain transmembrane #status predicted #label TN3 SUMMARY #length 985 #molecular-weight 113156 #checksum 9426 SEQUENCE /// ENTRY VCLJLK #type complete TITLE env polyprotein - simian foamy virus (type 3, strain LK3) ALTERNATE_NAMES coat polyprotein ORGANISM #formal_name simian foamy virus #note host (African green monkey) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 09-Sep-1994 ACCESSIONS C40820 REFERENCE A40820 !$#authors Renne, R.; Friedl, E.; Schweizer, M.; Fleps, U.; Turek, R.; !1Neumann-Haefelin, D. !$#journal Virology (1992) 186:597-608 !$#title Genomic organization and expression of simian foamy virus !1type 3 (SFV-3). !$#cross-references MUID:92124734; PMID:1310187 !$#accession C40820 !'##molecule_type DNA !'##residues 1-982 ##label REN !'##cross-references GB:M74895 GENETICS !$#gene env CLASSIFICATION #superfamily foamy virus env polyprotein KEYWORDS coat protein; glycoprotein; polyprotein; transmembrane !1protein FEATURE !$68-91 #domain transmembrane #status predicted #label TN1\ !$577-592 #domain transmembrane #status predicted #label TN2\ !$933-952 #domain transmembrane #status predicted #label TN3\ !$17,25,109,141,183, !$309,346,390,404, !$412,484,522,551, !$776,802,827 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 982 #molecular-weight 113313 #checksum 6753 SEQUENCE /// ENTRY WMLJSP #type complete TITLE S1 protein - human foamy virus ORGANISM #formal_name human foamy virus #note host Homo sapiens (man) DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 08-Apr-1994 ACCESSIONS B29685 REFERENCE A91074 !$#authors Fluegel, R.M.; Rethwilm, A.; Maurer, B.; Darai, G. !$#journal EMBO J. (1987) 6:2077-2084 !$#title Nucleotide sequence analysis of the env gene and its !1flanking regions of the human spumaretrovirus reveals two !1novel genes. !$#cross-references MUID:88004420; PMID:2820721 !$#accession B29685 !'##molecule_type genomic RNA !'##residues 1-107 ##label FLU COMMENT The RNA sequence was obtained from GenBank, release 58.0. CLASSIFICATION #superfamily foamy virus S1 protein SUMMARY #length 107 #molecular-weight 12183 #checksum 6510 SEQUENCE /// ENTRY WMLJB1 #type complete TITLE bel-1 protein - human foamy virus ORGANISM #formal_name human foamy virus DATE 30-Sep-1989 #sequence_revision 21-Nov-1998 #text_change 16-Jul-1999 ACCESSIONS S13140; D29685 REFERENCE S13140 !$#authors Fluegel, R.M.; Rethwilm, A.; Maurer, B.; Darai, G. !$#journal EMBO J. (1990) 9:3806 !$#title Nucleotide sequence analysis of the env gene and its !1flanking regions of the human spumaretrovirus reveals two !1novel genes. !$#accession S13140 !'##molecule_type genomic RNA !'##residues 1-300 ##label EMB REFERENCE A91074 !$#authors Fluegel, R.M.; Rethwilm, A.; Maurer, B.; Darai, G. !$#journal EMBO J. (1987) 6:2077-2084 !$#title Nucleotide sequence analysis of the env gene and its !1flanking regions of the human spumaretrovirus reveals two !1novel genes. !$#cross-references MUID:88004420; PMID:2820721 !$#accession D29685 !'##molecule_type genomic RNA !'##residues 'LLLRNLK',44-237,'V',239-241 ##label FLU !'##cross-references GB:U21247; NID:g1850916; PIDN:AAB48115.1; !1PID:g1850921 CLASSIFICATION #superfamily foamy virus bel-1 protein KEYWORDS transcription regulation SUMMARY #length 300 #molecular-weight 33885 #checksum 1929 SEQUENCE /// ENTRY WMLJLK #type complete TITLE bel-1 protein - simian foamy virus (type 3, strain LK3) ORGANISM #formal_name simian foamy virus #note host (African green monkey) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 01-Aug-1997 ACCESSIONS D40820 REFERENCE A40820 !$#authors Renne, R.; Friedl, E.; Schweizer, M.; Fleps, U.; Turek, R.; !1Neumann-Haefelin, D. !$#journal Virology (1992) 186:597-608 !$#title Genomic organization and expression of simian foamy virus !1type 3 (SFV-3). !$#cross-references MUID:92124734; PMID:1310187 !$#accession D40820 !'##molecule_type DNA !'##residues 1-298 ##label REN !'##cross-references GB:M74895 COMMENT This protein is a transcriptional transactivator. GENETICS !$#gene bel-1 CLASSIFICATION #superfamily foamy virus bel-1 protein KEYWORDS transcription regulation SUMMARY #length 298 #molecular-weight 33724 #checksum 7087 SEQUENCE /// ENTRY WMLJS1 #type complete TITLE bel-1 protein - simian foamy virus (type 1) ORGANISM #formal_name simian foamy virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS B39924 REFERENCE A39924 !$#authors Mergia, A.; Shaw, K.E.S.; Pratt-Lowe, E.; Barry, P.A.; !1Luciw, P.A. !$#journal J. Virol. (1991) 65:2903-2909 !$#title Identification of the simian foamy virus transcriptional !1transactivator gene (taf). !$#cross-references MUID:91237804; PMID:1851862 !$#accession B39924 !'##molecule_type DNA !'##residues 1-308 ##label MER !'##cross-references GB:M74039; NID:g334878; PIDN:AAA47802.1; !1PID:g454845 COMMENT This protein is a transcriptional transactivator. GENETICS !$#gene bel-1; taf CLASSIFICATION #superfamily foamy virus bel-1 protein KEYWORDS transcription regulation SUMMARY #length 308 #molecular-weight 35279 #checksum 2574 SEQUENCE /// ENTRY WMLJB2 #type complete TITLE bel-2 protein - human foamy virus ORGANISM #formal_name human foamy virus #note host Homo sapiens (man) DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jun-2000 ACCESSIONS E29685 REFERENCE A91074 !$#authors Fluegel, R.M.; Rethwilm, A.; Maurer, B.; Darai, G. !$#journal EMBO J. (1987) 6:2077-2084 !$#title Nucleotide sequence analysis of the env gene and its !1flanking regions of the human spumaretrovirus reveals two !1novel genes. !$#cross-references MUID:88004420; PMID:2820721 !$#accession E29685 !'##molecule_type genomic RNA !'##residues 1-364 ##label FLU !'##cross-references GB:X05592; GB:Y00070; NID:g61766; PIDN:CAA29088.1; !1PID:g1335594 CLASSIFICATION #superfamily foamy virus bel-2 protein SUMMARY #length 364 #molecular-weight 41401 #checksum 8723 SEQUENCE /// ENTRY WMLJBT #type complete TITLE bel-2 protein - simian foamy virus (type 3, strain LK3) ORGANISM #formal_name simian foamy virus #note host (African green monkey) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 08-Apr-1994 ACCESSIONS E40820 REFERENCE A40820 !$#authors Renne, R.; Friedl, E.; Schweizer, M.; Fleps, U.; Turek, R.; !1Neumann-Haefelin, D. !$#journal Virology (1992) 186:597-608 !$#title Genomic organization and expression of simian foamy virus !1type 3 (SFV-3). !$#cross-references MUID:92124734; PMID:1310187 !$#accession E40820 !'##molecule_type DNA !'##residues 1-388 ##label REN !'##cross-references GB:M74895 GENETICS !$#gene bel-2 CLASSIFICATION #superfamily foamy virus bel-2 protein SUMMARY #length 388 #molecular-weight 44555 #checksum 7823 SEQUENCE /// ENTRY WMLJS2 #type complete TITLE bel-2 protein - simian foamy virus (type 1) ORGANISM #formal_name simian foamy virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS C39924 REFERENCE A39924 !$#authors Mergia, A.; Shaw, K.E.S.; Pratt-Lowe, E.; Barry, P.A.; !1Luciw, P.A. !$#journal J. Virol. (1991) 65:2903-2909 !$#title Identification of the simian foamy virus transcriptional !1transactivator gene (taf). !$#cross-references MUID:91237804; PMID:1851862 !$#accession C39924 !'##molecule_type DNA !'##residues 1-403 ##label MER !'##cross-references GB:M74039; NID:g334878; PIDN:AAA47803.1; !1PID:g454846 GENETICS !$#gene bel-2 CLASSIFICATION #superfamily foamy virus bel-2 protein SUMMARY #length 403 #molecular-weight 45701 #checksum 9754 SEQUENCE /// ENTRY WMVW8M #type complete TITLE 18K protein - Abelson murine leukemia virus ORGANISM #formal_name Abelson murine leukemia virus DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 16-Jul-1999 ACCESSIONS A04001 REFERENCE A93955 !$#authors Reddy, E.P.; Smith, M.J.; Srinivasan, A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:3623-3627 !$#title Nucleotide sequence of Abelson murine leukemia virus genome: !1structural similarity of its transforming gene product to !1other onc gene products with tyrosine-specific kinase !1activity. !$#cross-references MUID:83221648; PMID:6304726 !$#accession A04001 !'##molecule_type DNA !'##residues 1-163 ##label RED !'##cross-references GB:V01541; GB:J02009; NID:g61487; PIDN:CAA24782.1; !1PID:g61489 CLASSIFICATION #superfamily murine leukemia virus 18K protein SUMMARY #length 163 #molecular-weight 17090 #checksum 8117 SEQUENCE /// ENTRY ASLJS3 #type complete TITLE vif protein - human immunodeficiency virus type 1 ALTERNATE_NAMES orf-Q protein; sor protein ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 DATE 17-May-1985 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS A04002; A36757; A36756; A36765; S42971 REFERENCE A94093 !$#authors Arya, S.K.; Gallo, R.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:2209-2213 !$#title Three novel genes of human T-lymphotropic virus type III: !1immune reactivity of their products with sera from acquired !1immune deficiency syndrome patients. !$#cross-references MUID:86177573; PMID:3008154 !$#accession A04002 !'##molecule_type DNA !'##residues 1-192 ##label ARY !'##cross-references GB:M11840; NID:g328453; PIDN:AAA44997.1; !1PID:g328454 !'##experimental_source isolate HTLV-III, 12 REFERENCE A93353 !$#authors Ratner, L.; Haseltine, W.; Patarca, R.; Livak, K.J.; !1Starcich, B.; Josephs, S.F.; Doran, E.R.; Rafalski, J.A.; !1Whitehorn, E.A.; Baumeister, K.; Ivanoff, L.; Petteway Jr., !1S.R.; Pearson, M.L.; Lautenberger, J.A.; Papas, T.S.; !1Ghrayeb, J.; Chang, N.T.; Gallo, R.C.; Wong-Staal, F. !$#journal Nature (1985) 313:277-284 !$#title Complete nucleotide sequence of the AIDS virus, HTLV-III. !$#cross-references MUID:85111123; PMID:2578615 !$#accession A36757 !'##molecule_type DNA !'##residues 1-192 ##label RAT !'##cross-references GB:M15654; NID:g326383; PIDN:AAA44202.1; !1PID:g326389 !'##experimental_source isolate HTLV-III, BH10 REFERENCE A90866 !$#authors Wain-Hobson, S.; Sonigo, P.; Danos, O.; Cole, S.; Alizon, M. !$#journal Cell (1985) 40:9-17 !$#title Nucleotide sequence of the AIDS virus, LAV. !$#cross-references MUID:85099333; PMID:2981635 !$#accession A36756 !'##molecule_type DNA !'##residues 1-192 ##label WAI !'##cross-references GB:K02013; NID:g326417; PIDN:AAB59748.1; !1PID:g326421 !'##experimental_source isolate LAV-1a REFERENCE A93355 !$#authors Muesing, M.A.; Smith, D.H.; Cabradilla, C.D.; Benton, C.V.; !1Lasky, L.A.; Capon, D.J. !$#journal Nature (1985) 313:450-458 !$#title Nucleic acid structure and expression of the human AIDS/ !1lymphadenopathy retrovirus. !$#cross-references MUID:85111157; PMID:2982104 !$#accession A36765 !'##molecule_type DNA !'##residues 1-192 ##label MUE !'##cross-references GB:X01762 !'##experimental_source isolate LV REFERENCE S42940 !$#authors Wieland, U.; Hartmann, J.; Suhr, H.; Salzberger, B.; Eggers, !1H.J.; Kuehn, J.E. !$#submission submitted to the EMBL Data Library, March 1994 !$#description In vivo genetic variability of the HIV-1 gene. !$#accession S42971 !'##status preliminary !'##molecule_type DNA !'##residues 1-192 ##label WIE !'##cross-references EMBL:Z30632; NID:g459506; PIDN:CAA83109.1; !1PID:g459507 GENETICS !$#gene vif CLASSIFICATION #superfamily AIDS vif protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 192 #molecular-weight 22513 #checksum 1114 SEQUENCE /// ENTRY ASLJNA #type complete TITLE vif protein - human immunodeficiency virus type 1 (isolate NIT-A) ALTERNATE_NAMES orf-Q protein; sor protein ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 #note host Homo sapiens (man) DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 31-Jan-1997 ACCESSIONS A41308 REFERENCE A41308 !$#authors Sakai, K.; Ma, X.; Gordienko, I.; Volsky, D.J. !$#journal J. Virol. (1991) 65:5765-5773 !$#title Recombinational analysis of a natural noncytopathic human !1immunodeficiency virus type 1 (HIV-1) isolate: role of the !1vif gene in HIV-1 infection kinetics and cytopathicity. !$#cross-references MUID:92015467; PMID:1920615 !$#accession A41308 !'##molecule_type DNA !'##residues 1-192 ##label SAK GENETICS !$#gene vif CLASSIFICATION #superfamily AIDS vif protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 192 #molecular-weight 22611 #checksum 1454 SEQUENCE /// ENTRY ASLJND #type complete TITLE vif protein - human immunodeficiency virus type 1 (isolate NDK) ALTERNATE_NAMES orf-Q protein; sor protein ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 #note host Homo sapiens (man) DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jul-1999 ACCESSIONS JQ0069 REFERENCE JQ0065 !$#authors Spire, B.; Sire, J.; Zachar, V.; Rey, F.; Barre-Sinoussi, !1F.; Galibert, F.; Hampe, A.; Chermann, J.C. !$#journal Gene (1989) 81:275-284 !$#title Nucleotide sequence of HIV1-NDK: a highly cytopathic strain !1of the human immunodeficiency virus. !$#cross-references MUID:90034200; PMID:2806917 !$#accession JQ0069 !'##molecule_type DNA !'##residues 1-192 ##label SPI !'##cross-references GB:M27323; NID:g328154; PIDN:AAA44870.1; !1PID:g328159 GENETICS !$#gene vif CLASSIFICATION #superfamily AIDS vif protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 192 #molecular-weight 22556 #checksum 698 SEQUENCE /// ENTRY ASLJO1 #type complete TITLE vif protein - human immunodeficiency virus type 1 (isolate ARV-2) ALTERNATE_NAMES orf-Q protein; sor protein ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 #note host Homo sapiens (man) DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 16-Jul-1999 ACCESSIONS A04003 REFERENCE A04003 !$#authors Sanchez-Pescador, R.; Power, M.D.; Barr, P.J.; Steimer, !1K.S.; Stempien, M.M.; Brown-Shimer, S.L.; Gee, W.W.; Renard, !1A.; Randolph, A.; Levy, J.A.; Dina, D.; Luciw, P.A. !$#journal Science (1985) 227:484-492 !$#title Nucleotide sequence and expression of an AIDS-associated !1retrovirus (ARV-2). !$#cross-references MUID:85090453; PMID:2578227 !$#accession A04003 !'##molecule_type DNA !'##residues 1-192 ##label SAN !'##cross-references GB:K02007; NID:g328658; PIDN:AAB59877.1; !1PID:g328663 GENETICS !$#gene vif CLASSIFICATION #superfamily AIDS vif protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 192 #molecular-weight 22460 #checksum 147 SEQUENCE /// ENTRY C44001 #type complete TITLE vif protein - human immunodeficiency virus type 1 (strain YU-2) ALTERNATE_NAMES orf-Q protein; sor protein ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 #note host Homo sapiens (man) DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 31-Jan-1997 ACCESSIONS C44001 REFERENCE A44001 !$#authors Li, Y.; Hui, H.; Burgess, C.J.; Price, R.W.; Sharp, P.M.; !1Hahn, B.H.; Shaw, G.M. !$#journal J. Virol. (1992) 66:6587-6600 !$#title Complete nucleotide sequence, genome organization, and !1biological properties of human immunodeficiency virus type 1 !1in vivo: evidence for limited defectiveness and !1complementation. !$#cross-references MUID:93021387; PMID:1404605 !$#accession C44001 !'##molecule_type DNA !'##residues 1-192 ##label LIY !'##cross-references GB:M93258 GENETICS !$#gene vif CLASSIFICATION #superfamily AIDS vif protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 192 #molecular-weight 22602 #checksum 1446 SEQUENCE /// ENTRY ASLJZR #type complete TITLE vif protein - human immunodeficiency virus Zr-6 ALTERNATE_NAMES orf-Q protein; sor protein ORGANISM #formal_name human immunodeficiency virus Zr-6 DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Jul-1999 ACCESSIONS B26192 REFERENCE A26192 !$#authors Srinivasan, A.; Anand, R.; York, D.; Ranganathan, P.; !1Feorino, P.; Schochetman, G.; Curran, J.; Kalyanaraman, !1V.S.; Luciw, P.A.; Sanchez-Pescador, R. !$#journal Gene (1987) 52:71-82 !$#title Molecular characterization of human immunodeficiency virus !1from Zaire: nucleotide sequence analysis identifies !1conserved and variable domains in the envelope gene. !$#cross-references MUID:87248097; PMID:3036660 !$#accession B26192 !'##molecule_type DNA !'##residues 1-188 ##label SRI !'##cross-references GB:K03458; GB:M16322; NID:g329398; PIDN:AAA45379.1; !1PID:g329402 GENETICS !$#gene vif CLASSIFICATION #superfamily AIDS vif protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 188 #molecular-weight 22159 #checksum 5227 SEQUENCE /// ENTRY ASLJSI #type complete TITLE vif protein - simian immunodeficiency virus SIVcpz ALTERNATE_NAMES orf-Q protein; sor protein ORGANISM #formal_name simian immunodeficiency virus SIVcpz #note host Pan troglodytes (chimpanzee) DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jul-1999 ACCESSIONS S09985 REFERENCE S09983 !$#authors Huet, T.; Cheynier, R.; Meyerhans, A.; Roelants, G.; !1Wain-Hobson, S. !$#journal Nature (1990) 345:356-359 !$#title Genetic organization of a chimpanzee lentivirus related to !1HIV-1. !$#cross-references MUID:90259077; PMID:2188136 !$#accession S09985 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-193 ##label HUE !'##cross-references EMBL:X52154; NID:g58866; PIDN:CAA36402.1; !1PID:g58869 GENETICS !$#gene vif CLASSIFICATION #superfamily AIDS vif protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 193 #molecular-weight 23048 #checksum 2602 SEQUENCE /// ENTRY ASLJS2 #type complete TITLE vif protein - human immunodeficiency virus type 2 (isolate ROD) ALTERNATE_NAMES orf-Q protein; sor protein ORGANISM #formal_name human immunodeficiency virus type 2, HIV-2 DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Jul-1999 ACCESSIONS G26262 REFERENCE A26262 !$#authors Guyader, M.; Emerman, M.; Sonigo, P.; Clavel, F.; !1Montagnier, L.; Alizon, M. !$#journal Nature (1987) 326:662-669 !$#title Genome organization and transactivation of the human !1immuno-deficiency virus type 2. !$#cross-references MUID:87173056; PMID:3031510 !$#accession G26262 !'##molecule_type DNA !'##residues 1-215 ##label GUY !'##cross-references GB:M15390; NID:g1332361; PIDN:AAB00765.1; !1PID:g325746 GENETICS !$#gene vif CLASSIFICATION #superfamily AIDS vif protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 215 #molecular-weight 25512 #checksum 5404 SEQUENCE /// ENTRY ASLJSW #type complete TITLE vif protein - human immunodeficiency virus type 2 (isolate ST) ALTERNATE_NAMES orf-Q protein; sor protein ORGANISM #formal_name human immunodeficiency virus type 2, HIV-2 #note host Homo sapiens (man) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS C33943 REFERENCE A33943 !$#authors Kumar, P.; Hui, H.; Kappes, J.C.; Haggarty, B.S.; Hoxie, !1J.A.; Arya, S.K.; Shaw, G.M.; Hahn, B.H. !$#journal J. Virol. (1990) 64:890-901 !$#title Molecular characterization of an attenuated human !1immunodeficiency virus type 2 isolate. !$#cross-references MUID:90112662; PMID:2296086 !$#accession C33943 !'##molecule_type genomic RNA !'##residues 1-215 ##label KUM !'##cross-references GB:M31113; NID:g1339798; PIDN:AAB01353.1; !1PID:g325756 GENETICS !$#gene vif CLASSIFICATION #superfamily AIDS vif protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 215 #molecular-weight 25355 #checksum 4170 SEQUENCE /// ENTRY ASLJCW #type complete TITLE vif protein - human immunodeficiency virus type 2 (isolate CAM2/Guinea-Bissau) ALTERNATE_NAMES orf-Q protein; sor protein ORGANISM #formal_name human immunodeficiency virus type 2, HIV-2 #note host Homo sapiens (man) DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jun-2000 ACCESSIONS C38475; JQ0975 REFERENCE A38475 !$#authors Tristem, M.; Hill, F.; Karpas, A. !$#journal J. Gen. Virol. (1991) 72:721-724 !$#title Nucleotide sequence of a Guinea-Bissau-derived human !1immunodeficiency virus type 2 proviral clone (HIV-2-CAM2). !$#cross-references MUID:91170959; PMID:2005437 !$#accession C38475 !'##molecule_type DNA !'##residues 1-215 ##label TRI !'##cross-references GB:D00835; NID:g3153166; PIDN:BAA00711.1; !1PID:g221469 GENETICS !$#gene vif CLASSIFICATION #superfamily AIDS vif protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 215 #molecular-weight 25321 #checksum 4213 SEQUENCE /// ENTRY ASLJGG #type complete TITLE vif protein - human immunodeficiency virus type 2 (isolate GH-1) ALTERNATE_NAMES orf-Q protein; sor protein ORGANISM #formal_name human immunodeficiency virus type 2, HIV-2 #note host Homo sapiens (man) DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jul-1999 ACCESSIONS JS0329 REFERENCE JS0327 !$#authors Hasegawa, A.; Tsujimoto, H.; Maki, N.; Ishikawa, K.; Miura, !1T.; Fukasawa, M.; Miki, K.; Hayami, M. !$#journal AIDS Res. Hum. Retroviruses (1989) 5:593-604 !$#title Sequence of a distinct HIV-2 isolate from Ghana showing !1significant divergence in its genome. !$#cross-references MUID:90122350; PMID:2611042 !$#accession JS0329 !'##molecule_type DNA !'##residues 1-215 ##label HAS !'##cross-references GB:M30895; GB:D00477; NID:g325709; PIDN:AAA43934.1; !1PID:g325715 !'##note this sequence was submitted to JIPID, October 1989 GENETICS !$#gene vif CLASSIFICATION #superfamily AIDS vif protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 215 #molecular-weight 25612 #checksum 4843 SEQUENCE /// ENTRY ASLJSM #type complete TITLE vif protein - simian immunodeficiency virus (macaque isolate) ALTERNATE_NAMES orf-Q protein; sor protein ORGANISM #formal_name simian immunodeficiency virus, SIV DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jul-1999 ACCESSIONS C28887 REFERENCE A28887 !$#authors Chakrabarti, L.; Guyader, M.; Alizon, M.; Daniel, M.D.; !1Desrosiers, R.C.; Tiollais, P.; Sonigo, P. !$#journal Nature (1987) 328:543-547 !$#title Sequence of simian immunodeficiency virus from macaque and !1its relationship to other human and simian retroviruses. !$#cross-references MUID:87287230; PMID:3649576 !$#accession C28887 !'##molecule_type DNA !'##residues 1-214 ##label CHA !'##cross-references GB:Y00277; GB:M16403; NID:g61730; PIDN:CAA68381.1; !1PID:g61733 GENETICS !$#gene vif CLASSIFICATION #superfamily AIDS vif protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 214 #molecular-weight 25329 #checksum 245 SEQUENCE /// ENTRY ASLJG5 #type complete TITLE vif protein - simian immunodeficiency virus (African green monkey isolate) ALTERNATE_NAMES orf-Q protein; sor protein ORGANISM #formal_name simian immunodeficiency virus, SIV DATE 30-Jun-1989 #sequence_revision 30-Sep-1992 #text_change 24-Oct-1997 ACCESSIONS C28873 REFERENCE A28873 !$#authors Franchini, G.; Gurgo, C.; Guo, H.G.; Gallo, R.C.; Collalti, !1E.; Fargnoli, K.A.; Hall, L.F.; Wong-Staal, F.; Reitz Jr., !1M.S. !$#journal Nature (1987) 328:539-543 !$#title Sequence of simian immunodeficiency virus and its !1relationship to the human immunodeficiency viruses. !$#cross-references MUID:87287229; PMID:3497350 !$#accession C28873 !'##molecule_type DNA !'##residues 1-214 ##label FRA !'##cross-references EMBL:M19499 GENETICS !$#gene vif CLASSIFICATION #superfamily AIDS vif protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 214 #molecular-weight 25253 #checksum 8005 SEQUENCE /// ENTRY ASLJG4 #type complete TITLE vif protein - simian immunodeficiency virus (African green monkey isolate) ALTERNATE_NAMES orf-Q protein; sor protein ORGANISM #formal_name simian immunodeficiency virus, SIV DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 28-Jul-2000 ACCESSIONS C30045 REFERENCE A30045 !$#authors Fukasawa, M.; Miura, T.; Hasegawa, A.; Morikawa, S.; !1Tsujimoto, H.; Miki, K.; Kitamura, T.; Hayami, M. !$#journal Nature (1988) 333:457-461 !$#title Sequence of simian immunodeficiency virus from African green !1monkey, a new member of the HIV/SIV group. !$#cross-references MUID:88232906; PMID:3374586 !$#accession C30045 !'##molecule_type DNA !'##residues 1-235 ##label FUK !'##cross-references EMBL:X07805; NID:g61748; PIDN:CAA30659.1; !1PID:g4469307 GENETICS !$#gene vif CLASSIFICATION #superfamily AIDS vif protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 235 #molecular-weight 27571 #checksum 7899 SEQUENCE /// ENTRY ASLJBT #type complete TITLE vif protein - bovine immunodeficiency virus (isolate 127) ALTERNATE_NAMES orf-Q protein; sor protein ORGANISM #formal_name bovine immunodeficiency virus DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jul-1999 ACCESSIONS C34742 REFERENCE A34742 !$#authors Garvey, K.J.; Oberste, M.S.; Elser, J.E.; Braun, M.J.; !1Gonda, M.A. !$#journal Virology (1990) 175:391-409 !$#title Nucleotide sequence and genome organization of biologically !1active proviruses of the bovine immunodeficiency-like virus. !$#cross-references MUID:90223985; PMID:2183467 !$#accession C34742 !'##molecule_type genomic RNA !'##residues 1-198 ##label GAR !'##cross-references GB:M32690; NID:g210706; PIDN:AAA91272.1; !1PID:g210709 GENETICS !$#gene vif CLASSIFICATION #superfamily BIV vif protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 198 #molecular-weight 22828 #checksum 2644 SEQUENCE /// ENTRY ASLJFP #type complete TITLE vif protein - feline immunodeficiency virus (strain Petaluma) ALTERNATE_NAMES orf-Q protein; sor protein ORGANISM #formal_name feline immunodeficiency virus #note host Felis silvestris catus (domestic cat) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 31-Jan-1997 ACCESSIONS C33543 REFERENCE A33543 !$#authors Talbott, R.L.; Sparger, E.E.; Lovelace, K.M.; Fitch, W.M.; !1Pedersen, N.C.; Luciw, P.A.; Elder, J.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:5743-5747 !$#title Nucleotide sequence and genomic organization of feline !1immunodeficiency virus. !$#cross-references MUID:89345543; PMID:2762293 !$#accession C33543 !'##molecule_type DNA !'##residues 1-263 ##label TAL GENETICS !$#gene vif CLASSIFICATION #superfamily FIV vif protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 263 #molecular-weight 30440 #checksum 5276 SEQUENCE /// ENTRY QQLJVS #type complete TITLE vif protein - Maedi/Visna virus ALTERNATE_NAMES orf-Q protein; sor protein ORGANISM #formal_name Maedi/Visna virus #note host Homo sapiens (man) DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 16-Jul-1999 ACCESSIONS A04004; C45390 REFERENCE A90869 !$#authors Sonigo, P.; Alizon, M.; Staskus, K.; Klatzmann, D.; Cole, !1S.; Danos, O.; Retzel, E.; Tiollais, P.; Haase, A.; !1Wain-Hobson, S. !$#journal Cell (1985) 42:369-382 !$#title Nucleotide sequence of the visna lentivirus: relationship to !1the AIDS virus. !$#cross-references MUID:85254938; PMID:2410140 !$#accession A04004 !'##molecule_type DNA !'##residues 1-230 ##label SON !'##cross-references GB:M10608 !'##experimental_source strain 1514 REFERENCE A45390 !$#authors Andresson, O.S.; Elser, J.E.; Tobin, G.J.; Greenwood, J.D.; !1Gonda, M.A.; Georgsson, G.; Andresdottir, V.; !1Benediktsdottir, E.; Carlsdottir, H.M.; Maentylae, E.O.; !1Rafnar, B.; Palsson, P.A.; Casey, J.W.; Petursson, G. !$#journal Virology (1993) 193:89-105 !$#title Nucleotide sequence and biological properties of a !1pathogenic proviral molecular clone of neurovirulent visna !1virus. !$#cross-references MUID:93174981; PMID:8382414 !$#accession C45390 !'##molecule_type DNA !'##residues 1-230 ##label AND !'##cross-references GB:S55323; NID:g265825; PIDN:AAB25461.1; !1PID:g265828 !'##experimental_source strain KV1772, provirus GENETICS !$#gene vif CLASSIFICATION #superfamily Visna virus vif protein SUMMARY #length 230 #molecular-weight 28138 #checksum 1683 SEQUENCE /// ENTRY C46335 #type complete TITLE vif protein - Maedi/Visna virus (strain SA-OMVV) ALTERNATE_NAMES orf-Q protein; sor protein ORGANISM #formal_name Maedi/Visna virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS C46335 REFERENCE A46335 !$#authors Querat, G.; Audoly, G.; Sonigo, P.; Vigne, R. !$#journal Virology (1990) 175:434-447 !$#title Nucleotide sequence analysis of SA-OMVV, a visna-related !1ovine lentivirus: phylogenetic history of lentiviruses. !$#cross-references MUID:90223989; PMID:2158181 !$#accession C46335 !'##molecule_type DNA !'##residues 1-228 ##label QUE !'##cross-references GB:M31646; NID:g808756; PIDN:AAA66813.1; !1PID:g332549 GENETICS !$#gene vif CLASSIFICATION #superfamily Visna virus vif protein SUMMARY #length 228 #molecular-weight 28027 #checksum 521 SEQUENCE /// ENTRY C45345 #type complete TITLE vif protein - caprine arthritis-encephalitis virus (strain CO) ALTERNATE_NAMES orf-Q protein; sor protein ORGANISM #formal_name caprine arthritis-encephalitis virus, CAEV DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jul-1999 ACCESSIONS C45345 REFERENCE A45345 !$#authors Saltarelli, M.; Querat, G.; Konings, D.A.M.; Vigne, R.; !1Clements, J.E. !$#journal Virology (1990) 179:347-364 !$#title Nucleotide sequence and transcriptional analysis of !1molecular clones of CAEV which generate infectious virus. !$#cross-references MUID:91021037; PMID:2171210 !$#accession C45345 !'##molecule_type mRNA !'##residues 1-229 ##label SAL !'##cross-references GB:M33677; NID:g323294; PIDN:AAA91827.1; !1PID:g323297 GENETICS !$#gene vif CLASSIFICATION #superfamily Visna virus vif protein SUMMARY #length 229 #molecular-weight 28051 #checksum 2055 SEQUENCE /// ENTRY ASLJH3 #type complete TITLE nef protein - human immunodeficiency virus type 1 (isolate HTLV-III, BH10) ALTERNATE_NAMES 3'-orf protein; orf-F protein ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 #note host Homo sapiens (man) DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 31-Jan-1997 ACCESSIONS A04005 REFERENCE A93353 !$#authors Ratner, L.; Haseltine, W.; Patarca, R.; Livak, K.J.; !1Starcich, B.; Josephs, S.F.; Doran, E.R.; Rafalski, J.A.; !1Whitehorn, E.A.; Baumeister, K.; Ivanoff, L.; Petteway Jr., !1S.R.; Pearson, M.L.; Lautenberger, J.A.; Papas, T.S.; !1Ghrayeb, J.; Chang, N.T.; Gallo, R.C.; Wong-Staal, F. !$#journal Nature (1985) 313:277-284 !$#title Complete nucleotide sequence of the AIDS virus, HTLV-III. !$#cross-references MUID:85111123; PMID:2578615 !$#accession A04005 !'##molecule_type DNA !'##residues 1-205 ##label RAT GENETICS !$#gene nef; 3'-orf; orf-F CLASSIFICATION #superfamily AIDS nef protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 205 #molecular-weight 23257 #checksum 9185 SEQUENCE /// ENTRY ASLJ12 #type complete TITLE nef protein - human immunodeficiency virus type 1 (isolate HTLV-III, 12) ALTERNATE_NAMES 3'-orf protein; orf-F protein ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 #note host Homo sapiens (man) DATE 04-Dec-1986 #sequence_revision 31-Dec-1991 #text_change 16-Jul-1999 ACCESSIONS A04006 REFERENCE A94093 !$#authors Arya, S.K.; Gallo, R.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:2209-2213 !$#title Three novel genes of human T-lymphotropic virus type III: !1immune reactivity of their products with sera from acquired !1immune deficiency syndrome patients. !$#cross-references MUID:86177573; PMID:3008154 !$#accession A04006 !'##molecule_type DNA !'##residues 1-206 ##label ARY !'##cross-references EMBL:M11840; NID:g328453; PIDN:AAA45001.1; !1PID:g328458 GENETICS !$#gene nef; 3'-orf; orf-F CLASSIFICATION #superfamily AIDS nef protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 206 #molecular-weight 23366 #checksum 2348 SEQUENCE /// ENTRY ASLJVL #type complete TITLE nef protein - human immunodeficiency virus type 1 (isolate LV) ALTERNATE_NAMES 3'-orf protein; orf-F protein ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 16-Jul-1999 ACCESSIONS A04007 REFERENCE A93355 !$#authors Muesing, M.A.; Smith, D.H.; Cabradilla, C.D.; Benton, C.V.; !1Lasky, L.A.; Capon, D.J. !$#journal Nature (1985) 313:450-458 !$#title Nucleic acid structure and expression of the human AIDS/ !1lymphadenopathy retrovirus. !$#cross-references MUID:85111157; PMID:2982104 !$#accession A04007 !'##molecule_type DNA !'##residues 1-206 ##label MUE !'##cross-references GB:K02083; NID:g555008; PIDN:AAB59874.1; !1PID:g328560 GENETICS !$#gene nef; 3'-orf; orf-F CLASSIFICATION #superfamily AIDS nef protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 206 #molecular-weight 23352 #checksum 2558 SEQUENCE /// ENTRY ASLJFV #type complete TITLE nef protein - human immunodeficiency virus type 1 (isolate LAV-1a) ALTERNATE_NAMES 3'-orf protein; orf-F protein ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 #note host Homo sapiens (man) DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 16-Jul-1999 ACCESSIONS A04008; S14609 REFERENCE A90866 !$#authors Wain-Hobson, S.; Sonigo, P.; Danos, O.; Cole, S.; Alizon, M. !$#journal Cell (1985) 40:9-17 !$#title Nucleotide sequence of the AIDS virus, LAV. !$#cross-references MUID:85099333; PMID:2981635 !$#accession A04008 !'##molecule_type DNA !'##residues 1-206 ##label WAI !'##cross-references GB:K02013; NID:g326417; PIDN:AAB59752.1; !1PID:g326425 !'##experimental_source isolate LAV-1a REFERENCE S14607 !$#authors Ciccarelli, R.B. !$#submission submitted to the EMBL Data Library, March 1991 !$#accession S14609 !'##status preliminary !'##molecule_type DNA !'##residues 1-206 ##label CIC !'##cross-references EMBL:X58780; NID:g60113; PIDN:CAA41585.1; !1PID:g60114 GENETICS !$#gene nef; 3'-orf; orf-F CLASSIFICATION #superfamily AIDS nef protein KEYWORDS AIDS; immunodeficiency; phosphoprotein SUMMARY #length 206 #molecular-weight 23342 #checksum 3491 SEQUENCE /// ENTRY ASLJO2 #type complete TITLE nef protein - human immunodeficiency virus type 1 (isolate ARV-2) ALTERNATE_NAMES 3'-orf protein; orf-F protein ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 #note host Homo sapiens (man) DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 16-Jul-1999 ACCESSIONS A04009 REFERENCE A04003 !$#authors Sanchez-Pescador, R.; Power, M.D.; Barr, P.J.; Steimer, !1K.S.; Stempien, M.M.; Brown-Shimer, S.L.; Gee, W.W.; Renard, !1A.; Randolph, A.; Levy, J.A.; Dina, D.; Luciw, P.A. !$#journal Science (1985) 227:484-492 !$#title Nucleotide sequence and expression of an AIDS-associated !1retrovirus (ARV-2). !$#cross-references MUID:85090453; PMID:2578227 !$#accession A04009 !'##molecule_type DNA !'##residues 1-210 ##label SAN !'##cross-references GB:K02007; NID:g328658; PIDN:AAB59883.1; !1PID:g328667 GENETICS !$#gene nef; 3'-orf; orf-F CLASSIFICATION #superfamily AIDS nef protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 210 #molecular-weight 24042 #checksum 3853 SEQUENCE /// ENTRY ASLJBR #type complete TITLE nef protein - human immunodeficiency virus type 1 (isolate BR) ALTERNATE_NAMES 3'-orf protein; orf-F protein ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 #note host Homo sapiens (man) DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jul-1999 ACCESSIONS D31667; S21993; S21995; S21997; S21999; S21991 REFERENCE A94389 !$#authors Anand, R.; Thayer, R.; Srinivasan, A.; Nayyar, S.; Gardner, !1M.; Luciw, P.; Dandekar, S. !$#journal Virology (1989) 168:79-89 !$#title Biological and molecular characterization of human !1immunodeficiency virus (HIV-1-BR) from the brain of a !1patient with progressive dementia. !$#cross-references MUID:89085613; PMID:2789516 !$#accession D31667 !'##molecule_type DNA !'##residues 1-218 ##label ANA !'##cross-references GB:M21098; NID:g326426; PIDN:AAA44222.1; !1PID:g326431 REFERENCE S21990 !$#authors Steuler, H.; Storch-Hagenlocher, B.; Wildemann, B.; Hacke, !1W. !$#submission submitted to the EMBL Data Library, July 1991 !$#description Distinct populations of HIV-1 in blood and cerebrospinal !1fluid as determined by direct sequencing. !$#accession S21993 !'##molecule_type DNA !'##residues 1-7 ##label STE !'##cross-references EMBL:X61358; NID:g60177; PIDN:CAA43629.1; !1PID:g584027; EMBL:X61357; NID:g60175; PID:g584026 !$#accession S21995 !'##molecule_type DNA !'##residues 1-7 ##label ST2 !'##cross-references EMBL:X61355; NID:g60179; PIDN:CAA43623.1; !1PID:g584028; EMBL:X61357; NID:g60175; PID:g584026 !$#accession S21997 !'##molecule_type DNA !'##residues 1-7 ##label ST3 !'##cross-references EMBL:X61356; NID:g60181; PIDN:CAA43625.1; !1PID:g1129140; EMBL:X61357; NID:g60175; PID:g584026 !$#accession S21999 !'##molecule_type DNA !'##residues 1-7 ##label ST4 !'##cross-references EMBL:X61359; NID:g60182; PIDN:CAA43631.1; !1PID:g584030 GENETICS !$#gene nef; 3'-orf; orf-F CLASSIFICATION #superfamily AIDS nef protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 218 #molecular-weight 25032 #checksum 9211 SEQUENCE /// ENTRY I44001 #type complete TITLE nef protein - human immunodeficiency virus type 1 (strain YU-2) ALTERNATE_NAMES 3'-orf protein; orf-F protein ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 #note host Homo sapiens (man) DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 23-Feb-1997 ACCESSIONS I44001 REFERENCE A44001 !$#authors Li, Y.; Hui, H.; Burgess, C.J.; Price, R.W.; Sharp, P.M.; !1Hahn, B.H.; Shaw, G.M. !$#journal J. Virol. (1992) 66:6587-6600 !$#title Complete nucleotide sequence, genome organization, and !1biological properties of human immunodeficiency virus type 1 !1in vivo: evidence for limited defectiveness and !1complementation. !$#cross-references MUID:93021387; PMID:1404605 !$#accession I44001 !'##molecule_type DNA !'##residues 1-214 ##label LIY !'##cross-references GB:M93258 GENETICS !$#gene nef; 3'-orf; orf-F CLASSIFICATION #superfamily AIDS nef protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 214 #molecular-weight 24532 #checksum 5715 SEQUENCE /// ENTRY QQLJZR #type complete TITLE nef protein - human immunodeficiency virus Zr-6 ALTERNATE_NAMES 3'-orf protein; orf-F protein ORGANISM #formal_name human immunodeficiency virus Zr-6 DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Jul-1999 ACCESSIONS F26192 REFERENCE A26192 !$#authors Srinivasan, A.; Anand, R.; York, D.; Ranganathan, P.; !1Feorino, P.; Schochetman, G.; Curran, J.; Kalyanaraman, !1V.S.; Luciw, P.A.; Sanchez-Pescador, R. !$#journal Gene (1987) 52:71-82 !$#title Molecular characterization of human immunodeficiency virus !1from Zaire: nucleotide sequence analysis identifies !1conserved and variable domains in the envelope gene. !$#cross-references MUID:87248097; PMID:3036660 !$#accession F26192 !'##molecule_type DNA !'##residues 1-212 ##label SRI !'##cross-references GB:K03458; GB:M16322; NID:g329398; PIDN:AAA45381.1; !1PID:g329404 GENETICS !$#gene nef; 3'-orf; orf-F CLASSIFICATION #superfamily AIDS nef protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 212 #molecular-weight 24415 #checksum 1724 SEQUENCE /// ENTRY QQLJND #type complete TITLE nef protein - human immunodeficiency virus type 1 (isolate NDK) ALTERNATE_NAMES 3'-orf protein; orf-F protein ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 #note host Homo sapiens (man) DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jul-1999 ACCESSIONS JQ0068 REFERENCE JQ0065 !$#authors Spire, B.; Sire, J.; Zachar, V.; Rey, F.; Barre-Sinoussi, !1F.; Galibert, F.; Hampe, A.; Chermann, J.C. !$#journal Gene (1989) 81:275-284 !$#title Nucleotide sequence of HIV1-NDK: a highly cytopathic strain !1of the human immunodeficiency virus. !$#cross-references MUID:90034200; PMID:2806917 !$#accession JQ0068 !'##molecule_type DNA !'##residues 1-207 ##label SPI !'##cross-references GB:M27323; NID:g328154; PIDN:AAA44874.1; !1PID:g328163 GENETICS !$#gene nef CLASSIFICATION #superfamily AIDS nef protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 207 #molecular-weight 23748 #checksum 6484 SEQUENCE /// ENTRY B44963 #type complete TITLE nef protein - human immunodeficiency virus type 1 (isolate Z321) ALTERNATE_NAMES 3'-orf protein; orf-F protein ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 #note host Homo sapiens (man) DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 28-May-1999 ACCESSIONS B44963 REFERENCE A44963 !$#authors Srinivasan, A.; York, D.; Butler Jr., D.; Jannoun-Nasr, R.; !1Getchell, J.; McCormick, J.; Ou, C.Y.; Myers, G.; Smith, T.; !1Chen, E.; Flaggs, G.; Berman, P.; Schochetman, G.; !1Kalyanaraman, S. !$#journal AIDS Res. Hum. Retroviruses (1989) 5:121-129 !$#title Molecular characterization of HIV-1 isolated from a serum !1collected in 1976: nucleotide sequence comparison to recent !1isolates and generation of hybrid HIV. !$#cross-references MUID:89228766; PMID:2713163 !$#accession B44963 !'##molecule_type DNA !'##residues 1-205 ##label SRI !'##cross-references GB:M15896; NID:g329392; PIDN:AAB53951.1; !1PID:g329397 GENETICS !$#gene nef; 3'-orf; orf-F CLASSIFICATION #superfamily AIDS nef protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 205 #molecular-weight 23306 #checksum 430 SEQUENCE /// ENTRY ASLJIK #type complete TITLE nef protein - simian immunodeficiency virus SIVcpz ALTERNATE_NAMES 3'-orf protein; orf-F protein ORGANISM #formal_name simian immunodeficiency virus SIVcpz #note host Pan troglodytes (chimpanzee) DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jul-1999 ACCESSIONS S09991 REFERENCE S09983 !$#authors Huet, T.; Cheynier, R.; Meyerhans, A.; Roelants, G.; !1Wain-Hobson, S. !$#journal Nature (1990) 345:356-359 !$#title Genetic organization of a chimpanzee lentivirus related to !1HIV-1. !$#cross-references MUID:90259077; PMID:2188136 !$#accession S09991 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-205 ##label HUE !'##cross-references EMBL:X52154; NID:g58866; PIDN:CAA36408.1; !1PID:g58877 GENETICS !$#gene nef CLASSIFICATION #superfamily AIDS nef protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 205 #molecular-weight 23850 #checksum 4050 SEQUENCE /// ENTRY ASLJH2 #type complete TITLE nef protein - human immunodeficiency virus type 2 (isolate ROD) ALTERNATE_NAMES 3'-orf protein; orf-F protein ORGANISM #formal_name human immunodeficiency virus type 2, HIV-2 DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Jul-1999 ACCESSIONS D26262 REFERENCE A26262 !$#authors Guyader, M.; Emerman, M.; Sonigo, P.; Clavel, F.; !1Montagnier, L.; Alizon, M. !$#journal Nature (1987) 326:662-669 !$#title Genome organization and transactivation of the human !1immuno-deficiency virus type 2. !$#cross-references MUID:87173056; PMID:3031510 !$#contents proviral DNA !$#accession D26262 !'##molecule_type DNA !'##residues 1-256 ##label GUY !'##cross-references GB:M15390; NID:g1332361; PIDN:AAB00771.1; !1PID:g325750 GENETICS !$#gene nef; 3'-orf; orf-F CLASSIFICATION #superfamily AIDS nef protein KEYWORDS AIDS; immunodeficiency; phosphoprotein SUMMARY #length 256 #molecular-weight 29566 #checksum 6374 SEQUENCE /// ENTRY ASLJSZ #type complete TITLE nef protein - human immunodeficiency virus type 2 (isolate ST) ALTERNATE_NAMES 3'-orf protein; orf-F protein ORGANISM #formal_name human immunodeficiency virus type 2, HIV-2 #note host Homo sapiens (man) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS I33943 REFERENCE A33943 !$#authors Kumar, P.; Hui, H.; Kappes, J.C.; Haggarty, B.S.; Hoxie, !1J.A.; Arya, S.K.; Shaw, G.M.; Hahn, B.H. !$#journal J. Virol. (1990) 64:890-901 !$#title Molecular characterization of an attenuated human !1immunodeficiency virus type 2 isolate. !$#cross-references MUID:90112662; PMID:2296086 !$#accession I33943 !'##molecule_type genomic RNA !'##residues 1-255 ##label KUM !'##cross-references GB:M31113; NID:g1339798; PIDN:AAB01359.1; !1PID:g325759 GENETICS !$#gene nef CLASSIFICATION #superfamily AIDS nef protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 255 #molecular-weight 29136 #checksum 5863 SEQUENCE /// ENTRY ASLJCZ #type complete TITLE nef protein - human immunodeficiency virus type 2 (isolate CAM2/Guinea-Bissau) ALTERNATE_NAMES 3'-orf protein; orf-F protein ORGANISM #formal_name human immunodeficiency virus type 2, HIV-2 #note host Homo sapiens (man) DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jun-2000 ACCESSIONS G38475; JQ0979 REFERENCE A38475 !$#authors Tristem, M.; Hill, F.; Karpas, A. !$#journal J. Gen. Virol. (1991) 72:721-724 !$#title Nucleotide sequence of a Guinea-Bissau-derived human !1immunodeficiency virus type 2 proviral clone (HIV-2-CAM2). !$#cross-references MUID:91170959; PMID:2005437 !$#accession G38475 !'##molecule_type DNA !'##residues 1-260 ##label TRI !'##cross-references GB:D00835; NID:g3153166; PIDN:BAA00717.1; !1PID:g221473 GENETICS !$#gene nef CLASSIFICATION #superfamily AIDS nef protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 260 #molecular-weight 29707 #checksum 3561 SEQUENCE /// ENTRY ASLJGN #type complete TITLE nef protein - human immunodeficiency virus type 2 (isolate GH-1) ALTERNATE_NAMES 3'-orf protein; orf-F protein ORGANISM #formal_name human immunodeficiency virus type 2, HIV-2 #note host Homo sapiens (man) DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jul-1999 ACCESSIONS JS0335 REFERENCE JS0327 !$#authors Hasegawa, A.; Tsujimoto, H.; Maki, N.; Ishikawa, K.; Miura, !1T.; Fukasawa, M.; Miki, K.; Hayami, M. !$#journal AIDS Res. Hum. Retroviruses (1989) 5:593-604 !$#title Sequence of a distinct HIV-2 isolate from Ghana showing !1significant divergence in its genome. !$#cross-references MUID:90122350; PMID:2611042 !$#accession JS0335 !'##molecule_type DNA !'##residues 1-255 ##label HAS !'##cross-references GB:M30895; GB:D00477; NID:g325709; PIDN:AAA43937.1; !1PID:g325718 !'##note this sequence was submitted to JIPID, October 1989 GENETICS !$#gene nef CLASSIFICATION #superfamily AIDS nef protein KEYWORDS AIDS SUMMARY #length 255 #molecular-weight 29249 #checksum 4866 SEQUENCE /// ENTRY ASLJRT #type complete TITLE nef protein - simian immunodeficiency virus SIVagm (type 3, isolate STLV-3agm) ALTERNATE_NAMES 3'-orf protein ORGANISM #formal_name simian immunodeficiency virus SIVagm DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 07-Nov-1997 ACCESSIONS F26737 REFERENCE A26737 !$#authors Hirsch, V.; Riedel, N.; Mullins, J.I. !$#journal Cell (1987) 49:307-319 !$#title The genome organization of STLV-3 is similar to that of the !1AIDS virus except for a truncated transmembrane protein. !$#cross-references MUID:87187627; PMID:3646094 !$#accession F26737 !'##molecule_type DNA !'##residues 1-263 ##label HIR !'##cross-references GB:M19499; NID:g334657 !'##note the authors translated the codon GGG for residue 25 as Arg GENETICS !$#gene nef; 3'-orf CLASSIFICATION #superfamily AIDS nef protein KEYWORDS AIDS SUMMARY #length 263 #molecular-weight 30245 #checksum 5913 SEQUENCE /// ENTRY ASLJM5 #type complete TITLE nef protein - simian immunodeficiency virus (African green monkey isolate) ALTERNATE_NAMES 3'-orf protein ORGANISM #formal_name simian immunodeficiency virus, SIV DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 24-Oct-1997 ACCESSIONS E28873 REFERENCE A28873 !$#authors Franchini, G.; Gurgo, C.; Guo, H.G.; Gallo, R.C.; Collalti, !1E.; Fargnoli, K.A.; Hall, L.F.; Wong-Staal, F.; Reitz Jr., !1M.S. !$#journal Nature (1987) 328:539-543 !$#title Sequence of simian immunodeficiency virus and its !1relationship to the human immunodeficiency viruses. !$#cross-references MUID:87287229; PMID:3497350 !$#accession E28873 !'##molecule_type DNA !'##residues 1-211 ##label FRA !'##cross-references EMBL:M19499 GENETICS !$#gene nef; 3'-orf CLASSIFICATION #superfamily AIDS nef protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 211 #molecular-weight 24328 #checksum 3275 SEQUENCE /// ENTRY ASLJM3 #type complete TITLE nef protein - simian immunodeficiency virus (macaque isolate) ALTERNATE_NAMES 3'-orf protein ORGANISM #formal_name simian immunodeficiency virus, SIV DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jul-1999 ACCESSIONS I28887 REFERENCE A28887 !$#authors Chakrabarti, L.; Guyader, M.; Alizon, M.; Daniel, M.D.; !1Desrosiers, R.C.; Tiollais, P.; Sonigo, P. !$#journal Nature (1987) 328:543-547 !$#title Sequence of simian immunodeficiency virus from macaque and !1its relationship to other human and simian retroviruses. !$#cross-references MUID:87287230; PMID:3649576 !$#accession I28887 !'##molecule_type DNA !'##residues 1-262 ##label CHA !'##cross-references GB:Y00277; GB:M16403; NID:g61730; PIDN:CAA68389.1; !1PID:g61740 GENETICS !$#gene nef; 3'-orf CLASSIFICATION #superfamily AIDS nef protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 262 #molecular-weight 30287 #checksum 18 SEQUENCE /// ENTRY ASLJMA #type complete TITLE nef protein - simian immunodeficiency virus SIVmac (isolate mac1A11) ALTERNATE_NAMES 3'-orf protein ORGANISM #formal_name simian immunodeficiency virus SIVmac DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 31-Jan-1997 ACCESSIONS A42747 REFERENCE A42747 !$#authors Unger, R.E.; Marthas, M.L.; Pratt-Lowe, E.; Padrid, P.A.; !1Luciw, P.A. !$#journal J. Virol. (1992) 66:5432-5442 !$#title The nef gene of simian immunodeficiency virus SIVmac1A11. !$#cross-references MUID:92365133; PMID:1501282 !$#accession A42747 !'##molecule_type DNA !'##residues 1-263 ##label UNG GENETICS !$#gene nef CLASSIFICATION #superfamily AIDS nef protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 263 #molecular-weight 30620 #checksum 5774 SEQUENCE /// ENTRY ASLJM4 #type complete TITLE nef protein - simian immunodeficiency virus (African green monkey isolate) ALTERNATE_NAMES 3'-orf protein ORGANISM #formal_name simian immunodeficiency virus, SIV DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 28-Jul-2000 ACCESSIONS H30045 REFERENCE A30045 !$#authors Fukasawa, M.; Miura, T.; Hasegawa, A.; Morikawa, S.; !1Tsujimoto, H.; Miki, K.; Kitamura, T.; Hayami, M. !$#journal Nature (1988) 333:457-461 !$#title Sequence of simian immunodeficiency virus from African green !1monkey, a new member of the HIV/SIV group. !$#cross-references MUID:88232906; PMID:3374586 !$#accession H30045 !'##molecule_type DNA !'##residues 1-229 ##label FUK !'##cross-references EMBL:X07805; NID:g61748; PIDN:CAA30664.1; !1PID:g4469312 GENETICS !$#gene nef; 3'-orf CLASSIFICATION #superfamily AIDS nef protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 229 #molecular-weight 26655 #checksum 2262 SEQUENCE /// ENTRY ASLJEW #type complete TITLE nef protein (clone 1369) - equine infectious anemia virus (clone 1369) ALTERNATE_NAMES 3'-orf protein ORGANISM #formal_name equine infectious anemia virus #note host Equus caballus (domestic horse) DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 07-Nov-1997 ACCESSIONS D27842 REFERENCE A27842 !$#authors Kawakami, T.; Sherman, L.; Dahlberg, J.; Gazit, A.; Yaniv, !1A.; Tronick, S.R.; Aaronson, S.A. !$#journal Virology (1987) 158:300-312 !$#title Nucleotide sequence analysis of equine infectious anemia !1virus proviral DNA. !$#cross-references MUID:87236196; PMID:3035786 !$#accession D27842 !'##molecule_type DNA !'##residues 1-135 ##label KAW !'##cross-references GB:M16575; NID:g323836 GENETICS !$#gene nef; 3'-orf CLASSIFICATION #superfamily equine infectious anemia virus nef protein KEYWORDS transcription regulation SUMMARY #length 135 #molecular-weight 15988 #checksum 3032 SEQUENCE /// ENTRY ASLJ22 #type complete TITLE nef protein - equine infectious anemia virus ALTERNATE_NAMES rev protein ORGANISM #formal_name equine infectious anemia virus DATE 30-Jun-1993 #sequence_revision 13-Mar-1997 #text_change 16-Jun-2000 ACCESSIONS B46357; F41991; C40680 REFERENCE A46357 !$#authors Noiman, S.; Gazit, A.; Tori, O.; Sherman, L.; Miki, T.; !1Tronick, S.R.; Yaniv, A. !$#journal Virology (1990) 176:280-288 !$#title Identification of sequences encoding the equine infectious !1anemia virus tat gene. !$#cross-references MUID:90232740; PMID:2158694 !$#accession B46357 !'##status preliminary !'##molecule_type mRNA !'##residues 1-165 ##label NOI !'##cross-references GB:M36592; NID:g1374814; PIDN:AAB02404.1; !1PID:g323820 REFERENCE A41991 !$#authors Perry, S.T.; Flaherty, M.T.; Kelley, M.J.; Clabough, D.L.; !1Tronick, S.R.; Coggins, L.; Whetter, L.; Lengel, C.R.; !1Fuller, F. !$#journal J. Virol. (1992) 66:4085-4097 !$#title The surface envelope protein gene region of equine !1infectious anemia virus is not an important determinant of !1tropism in vitro. !$#cross-references MUID:92292230; PMID:1318398 !$#accession F41991 !'##molecule_type DNA !'##residues 31-165 ##label PER !'##cross-references GB:M87581; NID:g290627; PIDN:AAA43006.1; !1PID:g290631 !'##experimental_source strain CL22 REFERENCE A40680 !$#authors Rosin-Arbesfeld, R.; Rivlin, M.; Noiman, S.; Mashiah, P.; !1Yaniv, A.; Miki, T.; Tronick, S.R.; Gazit, A. !$#journal J. Virol. (1993) 67:5640-5646 !$#title Structural and functional characterization of rev-like !1transcripts of equine infectious anemia virus. !$#cross-references MUID:93353644; PMID:8394464 !$#accession C40680 !'##status preliminary !'##molecule_type mRNA !'##residues 'DP',8-9,'SRGE',14,'T',16,'VFWRC',18,'WP',21,'H',23-24,'T', !126,32-165 ##label ROS !'##cross-references GB:X63058; NID:g436316; PIDN:CAA44782.1; !1PID:g1334985 GENETICS !$#gene nef CLASSIFICATION #superfamily equine infectious anemia virus nef protein KEYWORDS nucleus; transcription regulation SUMMARY #length 165 #molecular-weight 19810 #checksum 7578 SEQUENCE /// ENTRY ASLJF2 #type complete TITLE probable nef protein - feline immunodeficiency virus (strain Petaluma) ALTERNATE_NAMES 3'-orf protein; orf-F protein ORGANISM #formal_name feline immunodeficiency virus #note host Felis silvestris catus (domestic cat) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 23-Feb-1997 ACCESSIONS E33543 REFERENCE A33543 !$#authors Talbott, R.L.; Sparger, E.E.; Lovelace, K.M.; Fitch, W.M.; !1Pedersen, N.C.; Luciw, P.A.; Elder, J.H. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:5743-5747 !$#title Nucleotide sequence and genomic organization of feline !1immunodeficiency virus. !$#cross-references MUID:89345543; PMID:2762293 !$#accession E33543 !'##molecule_type DNA !'##residues 1-124 ##label TAL !'##note readthrough of the terminators TGA and TAA occurs between !1codons TGC for 29-Cys and GTT for 30-Val, and between codons !1TTG for 53-Leu and GGT for 54-Gly, respectively GENETICS !$#gene nef CLASSIFICATION #superfamily FIV nef protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 124 #molecular-weight 14920 #checksum 8810 SEQUENCE /// ENTRY D46335 #type complete TITLE W protein - Maedi/Visna virus (strain SA-OMVV) ORGANISM #formal_name Maedi/Visna virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS D46335 REFERENCE A46335 !$#authors Querat, G.; Audoly, G.; Sonigo, P.; Vigne, R. !$#journal Virology (1990) 175:434-447 !$#title Nucleotide sequence analysis of SA-OMVV, a visna-related !1ovine lentivirus: phylogenetic history of lentiviruses. !$#cross-references MUID:90223989; PMID:2158181 !$#accession D46335 !'##molecule_type DNA !'##residues 1-86 ##label QUE !'##cross-references GB:M31646; NID:g808756; PIDN:AAA66814.1; !1PID:g808758 GENETICS !$#gene W CLASSIFICATION #superfamily Maedi virus W protein SUMMARY #length 86 #molecular-weight 9748 #checksum 1552 SEQUENCE /// ENTRY TNLJVS #type complete TITLE trans-activating transcription regulator - Maedi/Visna virus ALTERNATE_NAMES tat protein ORGANISM #formal_name Maedi/Visna virus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jul-1999 ACCESSIONS A32184 REFERENCE A32184 !$#authors Davis, J.L.; Clements, J.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:414-418 !$#title Characterization of a cDNA clone encoding the visna virus !1transactivating protein. !$#cross-references MUID:89098943; PMID:2536163 !$#accession A32184 !'##molecule_type mRNA !'##residues 1-94 ##label DAV !'##cross-references GB:M23047; EMBL:J04163; NID:g533272; !1PIDN:AAA48364.1; PID:g533273 GENETICS !$#gene tat CLASSIFICATION #superfamily Visna virus trans-activating transcription !1regulator KEYWORDS transcription SUMMARY #length 94 #molecular-weight 11234 #checksum 3642 SEQUENCE /// ENTRY QQLJVX #type complete TITLE trans-activating transcription regulator - Maedi/Visna virus (strain K1514) ALTERNATE_NAMES tat protein ORGANISM #formal_name Maedi/Visna virus DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 16-Jul-1999 ACCESSIONS A04010; B32441 REFERENCE A90869 !$#authors Sonigo, P.; Alizon, M.; Staskus, K.; Klatzmann, D.; Cole, !1S.; Danos, O.; Retzel, E.; Tiollais, P.; Haase, A.; !1Wain-Hobson, S. !$#journal Cell (1985) 42:369-382 !$#title Nucleotide sequence of the visna lentivirus: relationship to !1the AIDS virus. !$#cross-references MUID:85254938; PMID:2410140 !$#accession A04010 !'##molecule_type DNA !'##residues 1-94 ##label SON !'##cross-references EMBL:M10608 REFERENCE A32441 !$#authors Gourdou, I.; Mazarin, V.; Querat, G.; Sauze, N.; Vigne, R. !$#journal Virology (1989) 171:170-178 !$#title The open reading frame S of visna virus genome is a !1trans-activating gene. !$#cross-references MUID:89299455; PMID:2545028 !$#accession B32441 !'##molecule_type mRNA !'##residues 1-14,'A',16-36,'G',38-94 ##label GOU !'##cross-references EMBL:J04359; NID:g335866; PIDN:AAA75436.1; !1PID:g987001 GENETICS !$#gene tat CLASSIFICATION #superfamily Visna virus trans-activating transcription !1regulator KEYWORDS transcription SUMMARY #length 94 #molecular-weight 11280 #checksum 3985 SEQUENCE /// ENTRY D45390 #type complete TITLE trans-activating transcription regulator - Maedi/Visna virus (strain KV1772) (provirus) ALTERNATE_NAMES tat protein ORGANISM #formal_name Maedi/Visna virus #note host Homo sapiens (man) DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS D45390 REFERENCE A45390 !$#authors Andresson, O.S.; Elser, J.E.; Tobin, G.J.; Greenwood, J.D.; !1Gonda, M.A.; Georgsson, G.; Andresdottir, V.; !1Benediktsdottir, E.; Carlsdottir, H.M.; Maentylae, E.O.; !1Rafnar, B.; Palsson, P.A.; Casey, J.W.; Petursson, G. !$#journal Virology (1993) 193:89-105 !$#title Nucleotide sequence and biological properties of a !1pathogenic proviral molecular clone of neurovirulent visna !1virus. !$#cross-references MUID:93174981; PMID:8382414 !$#accession D45390 !'##molecule_type DNA !'##residues 1-94 ##label AND !'##cross-references GB:S55323; NID:g265825; PIDN:AAB25462.1; !1PID:g265829 GENETICS !$#gene tat CLASSIFICATION #superfamily Visna virus trans-activating transcription !1regulator KEYWORDS transcription SUMMARY #length 94 #molecular-weight 11232 #checksum 3988 SEQUENCE /// ENTRY E46335 #type complete TITLE trans-activating transcription regulator - Maedi/Visna virus (strain SA-OMVV) ALTERNATE_NAMES tat protein ORGANISM #formal_name Maedi/Visna virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS E46335 REFERENCE A46335 !$#authors Querat, G.; Audoly, G.; Sonigo, P.; Vigne, R. !$#journal Virology (1990) 175:434-447 !$#title Nucleotide sequence analysis of SA-OMVV, a visna-related !1ovine lentivirus: phylogenetic history of lentiviruses. !$#cross-references MUID:90223989; PMID:2158181 !$#accession E46335 !'##molecule_type DNA !'##residues 1-94 ##label QUE !'##cross-references GB:M31646; NID:g808756; PIDN:AAA66815.1; !1PID:g332550 GENETICS !$#gene tat CLASSIFICATION #superfamily Visna virus trans-activating transcription !1regulator KEYWORDS transcription SUMMARY #length 94 #molecular-weight 11285 #checksum 3098 SEQUENCE /// ENTRY D45345 #type complete TITLE trans-activating transcription regulator - caprine arthritis-encephalitis virus (strain CO) ALTERNATE_NAMES tat protein ORGANISM #formal_name caprine arthritis-encephalitis virus, CAEV DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jul-1999 ACCESSIONS D45345 REFERENCE A45345 !$#authors Saltarelli, M.; Querat, G.; Konings, D.A.M.; Vigne, R.; !1Clements, J.E. !$#journal Virology (1990) 179:347-364 !$#title Nucleotide sequence and transcriptional analysis of !1molecular clones of CAEV which generate infectious virus. !$#cross-references MUID:91021037; PMID:2171210 !$#accession D45345 !'##molecule_type mRNA !'##residues 1-87 ##label SAL !'##cross-references GB:M33677; NID:g323294; PIDN:AAA91828.1; !1PID:g323298 GENETICS !$#gene tat CLASSIFICATION #superfamily Visna virus trans-activating transcription !1regulator KEYWORDS transcription SUMMARY #length 87 #molecular-weight 10626 #checksum 5309 SEQUENCE /// ENTRY TNLJH1 #type complete TITLE trans-activating transcription regulator - human T-cell lymphotropic virus type 1 ALTERNATE_NAMES x-lor protein ORGANISM #formal_name human T-cell lymphotropic virus type 1, HTLV-1 #note host Homo sapiens (man) DATE 25-Feb-1985 #sequence_revision 28-Aug-1985 #text_change 02-Jul-1998 ACCESSIONS A93954; A04011 REFERENCE A93954 !$#authors Seiki, M.; Hattori, S.; Hirayama, Y.; Yoshida, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:3618-3622 !$#title Human adult T-cell leukemia virus: complete nucleotide !1sequence of the provirus genome integrated in leukemia cell !1DNA. !$#cross-references MUID:83221647; PMID:6304725 !$#accession A93954 !'##molecule_type DNA !'##residues 1-358 ##label SEI !'##experimental_source strain ATK REFERENCE A94280 !$#authors Chen, I.S.Y.; Slamon, D.J.; Rosenblatt, J.D.; Shah, N.P.; !1Quan, S.G.; Wachsman, W. !$#journal Science (1985) 229:54-58 !$#title The x gene is essential for HTLV replication. !$#cross-references MUID:85244620; PMID:2990037 !$#contents annotation; experimental details COMMENT By in vitro mutagenesis of the tat gene, it was demonstrated !1that the presence of a functional tat gene product was !1necessary for efficient HTLV transcription. GENETICS !$#gene tat CLASSIFICATION #superfamily leukemia virus trans-activating transcription !1regulator KEYWORDS transcription regulation SUMMARY #length 358 #molecular-weight 39984 #checksum 1711 SEQUENCE /// ENTRY TNLJCN #type complete TITLE trans-activating transcription regulator - human T-cell lymphotropic virus type 1 (isolate Caribbean) ALTERNATE_NAMES pX protein; x-lor protein ORGANISM #formal_name human T-cell lymphotropic virus type 1, HTLV-1 #note host Homo sapiens (man) DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 02-Jul-1998 ACCESSIONS E28136 REFERENCE A92797 !$#authors Malik, K.T.A.; Even, J.; Karpas, A. !$#journal J. Gen. Virol. (1988) 69:1695-1710 !$#title Molecular cloning and complete nucleotide sequence of an !1adult T cell leukaemia virus/human T cell leukaemia virus !1type I (ATLV/HTLV-I) isolate of Caribbean origin: !1relationship to other members of the ATLV/HTLV-I subgroup. !$#cross-references MUID:88274338; PMID:2899128 !$#accession E28136 !'##molecule_type DNA !'##residues 1-358 ##label MAL !'##cross-references GB:D13784; GB:D00294; NID:g221866 !'##note this ORF is not annotated in GenBank entry HTVPRCAR GENETICS !$#gene tat !$#introns 1/3 CLASSIFICATION #superfamily leukemia virus trans-activating transcription !1regulator KEYWORDS transcription regulation SUMMARY #length 358 #molecular-weight 40026 #checksum 1729 SEQUENCE /// ENTRY TNLJH2 #type complete TITLE trans-activating transcription regulator - human T-cell lymphotropic virus type 2 ORGANISM #formal_name human T-cell lymphotropic virus type 2, HTLV-2 #note host Homo sapiens (man) DATE 28-Feb-1986 #sequence_revision 28-Feb-1986 #text_change 02-Jul-1998 ACCESSIONS A04012 REFERENCE A94042 !$#authors Shimotohno, K.; Takahashi, Y.; Shimizu, N.; Gojobori, T.; !1Golde, D.W.; Chen, I.S.Y.; Miwa, M.; Sugimura, T. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:3101-3105 !$#title Complete nucleotide sequence of an infectious clone of human !1T-cell leukemia virus type II: an open reading frame for the !1protease gene. !$#cross-references MUID:85216449; PMID:2582407 !$#accession A04012 !'##molecule_type DNA !'##residues 1-337 ##label SHI GENETICS !$#gene tat CLASSIFICATION #superfamily leukemia virus trans-activating transcription !1regulator KEYWORDS transcription regulation SUMMARY #length 337 #molecular-weight 37948 #checksum 7638 SEQUENCE /// ENTRY TNLJT2 #type complete TITLE trans-activating transcription regulator - human T-cell lymphotropic virus type 2 ORGANISM #formal_name human T-cell lymphotropic virus type 2, HTLV-2 #note host Homo sapiens (man) DATE 25-Feb-1985 #sequence_revision 28-Feb-1986 #text_change 02-Jul-1998 ACCESSIONS A04013 REFERENCE A04013 !$#authors Haseltine, W.A.; Sodroski, J.; Patarca, R.; Briggs, D.; !1Perkins, D.; Wong-Staal, F. !$#journal Science (1984) 225:419-421 !$#title Structure of 3' terminal region of type II human T !1lymphotropic virus: evidence for new coding region. !$#cross-references MUID:84250188; PMID:6330894 !$#accession A04013 !'##molecule_type genomic RNA !'##residues 1-337 ##label HAS GENETICS !$#gene tat CLASSIFICATION #superfamily leukemia virus trans-activating transcription !1regulator KEYWORDS transcription regulation SUMMARY #length 337 #molecular-weight 37856 #checksum 6355 SEQUENCE /// ENTRY QQLJX1 #type fragment TITLE trans-activating transcription regulator - bovine leukemia virus (fragment) ORGANISM #formal_name bovine leukemia virus, BLV #note host Bos sp. (cattle) DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 02-Jul-1998 ACCESSIONS A04014 REFERENCE A94063 !$#authors Sagata, N.; Yasunaga, T.; Tsuzuku-Kawamura, J.; Ohishi, K.; !1Ogawa, Y.; Ikawa, Y. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:677-681 !$#title Complete nucleotide sequence of the genome of bovine !1leukemia virus: its evolutionary relationship to other !1retroviruses. !$#cross-references MUID:85140159; PMID:2983308 !$#accession A04014 !'##molecule_type DNA !'##residues 1-308 ##label SAG CLASSIFICATION #superfamily leukemia virus trans-activating transcription !1regulator SUMMARY #length 308 #checksum 7882 SEQUENCE /// ENTRY QQLJX2 #type fragment TITLE trans-activating transcription regulator - bovine leukemia virus (fragment) ORGANISM #formal_name bovine leukemia virus, BLV #note host Bos sp. (cattle) DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 02-Jul-1998 ACCESSIONS A04015 REFERENCE A94063 !$#authors Sagata, N.; Yasunaga, T.; Tsuzuku-Kawamura, J.; Ohishi, K.; !1Ogawa, Y.; Ikawa, Y. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:677-681 !$#title Complete nucleotide sequence of the genome of bovine !1leukemia virus: its evolutionary relationship to other !1retroviruses. !$#cross-references MUID:85140159; PMID:2983308 !$#accession A04015 !'##molecule_type DNA !'##residues 1-148 ##label SAG CLASSIFICATION #superfamily leukemia virus trans-activating transcription !1regulator SUMMARY #length 148 #checksum 8760 SEQUENCE /// ENTRY QQLJX3 #type fragment TITLE trans-activating transcription regulator - bovine leukemia virus (fragment) ORGANISM #formal_name bovine leukemia virus, BLV #note host Bos sp. (cattle) DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 02-Jul-1998 ACCESSIONS A04016 REFERENCE A94063 !$#authors Sagata, N.; Yasunaga, T.; Tsuzuku-Kawamura, J.; Ohishi, K.; !1Ogawa, Y.; Ikawa, Y. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:677-681 !$#title Complete nucleotide sequence of the genome of bovine !1leukemia virus: its evolutionary relationship to other !1retroviruses. !$#cross-references MUID:85140159; PMID:2983308 !$#accession A04016 !'##molecule_type DNA !'##residues 1-119 ##label SAG CLASSIFICATION #superfamily leukemia virus trans-activating transcription !1regulator SUMMARY #length 119 #checksum 4285 SEQUENCE /// ENTRY TNLJ12 #type complete TITLE trans-activating transcription regulator - human immunodeficiency virus type 1 (isolate HTLV-III, 12) ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 #note host Homo sapiens (man) DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 02-Jul-1998 ACCESSIONS A04017 REFERENCE A94093 !$#authors Arya, S.K.; Gallo, R.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:2209-2213 !$#title Three novel genes of human T-lymphotropic virus type III: !1immune reactivity of their products with sera from acquired !1immune deficiency syndrome patients. !$#cross-references MUID:86177573; PMID:3008154 !$#accession A04017 !'##molecule_type DNA !'##residues 1-95 ##label ARY GENETICS !$#gene tat CLASSIFICATION #superfamily AIDS trans-activating transcription regulator KEYWORDS AIDS; immunodeficiency; transcription regulation SUMMARY #length 95 #molecular-weight 10770 #checksum 2338 SEQUENCE /// ENTRY E44001 #type complete TITLE trans-activating transcription regulator - human immunodeficiency virus type 1 (strain YU-2) ALTERNATE_NAMES tat protein ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 #note host Homo sapiens (man) DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 02-Jul-1998 ACCESSIONS E44001 REFERENCE A44001 !$#authors Li, Y.; Hui, H.; Burgess, C.J.; Price, R.W.; Sharp, P.M.; !1Hahn, B.H.; Shaw, G.M. !$#journal J. Virol. (1992) 66:6587-6600 !$#title Complete nucleotide sequence, genome organization, and !1biological properties of human immunodeficiency virus type 1 !1in vivo: evidence for limited defectiveness and !1complementation. !$#cross-references MUID:93021387; PMID:1404605 !$#accession E44001 !'##molecule_type DNA !'##residues 1-101 ##label LIY !'##cross-references GB:M93258 GENETICS !$#gene tat !$#introns 72/2 CLASSIFICATION #superfamily AIDS trans-activating transcription regulator KEYWORDS AIDS; immunodeficiency; transcription regulation SUMMARY #length 101 #molecular-weight 11594 #checksum 3783 SEQUENCE /// ENTRY TNLJH4 #type complete TITLE trans-activating transcription regulator - human immunodeficiency virus type 1 (isolate CDC-451) ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 02-Jul-1998 ACCESSIONS B25523 REFERENCE A94136 !$#authors Desai, S.M.; Kalyanaraman, V.S.; Casey, J.M.; Srinivasan, !1A.; Andersen, P.R.; Devare, S.G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:8380-8384 !$#title Molecular cloning and primary nucleotide sequence analysis !1of a distinct human immunodeficiency virus isolate reveal !1significant divergence in its genomic sequences. !$#cross-references MUID:87041461; PMID:3490666 !$#accession B25523 !'##molecule_type DNA !'##residues 1-72 ##label DES !'##cross-references GB:M13137; NID:g326460 !'##note the GenBank entry ADRE3AA PID:g209908 differs from the !1published sequence in translating the stop codon TAA as Pro !1and reading in phase 3 for 28 residues GENETICS !$#gene tat CLASSIFICATION #superfamily AIDS trans-activating transcription regulator KEYWORDS transcription regulation SUMMARY #length 72 #molecular-weight 8418 #checksum 6032 SEQUENCE /// ENTRY TNLJBR #type complete TITLE trans-activating transcription regulator - human immunodeficiency virus type 1 (isolate BR) ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 #note host Homo sapiens (man) DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 02-Jul-1998 ACCESSIONS B31667 REFERENCE A94389 !$#authors Anand, R.; Thayer, R.; Srinivasan, A.; Nayyar, S.; Gardner, !1M.; Luciw, P.; Dandekar, S. !$#journal Virology (1989) 168:79-89 !$#title Biological and molecular characterization of human !1immunodeficiency virus (HIV-1-BR) from the brain of a !1patient with progressive dementia. !$#cross-references MUID:89085613; PMID:2789516 !$#accession B31667 !'##molecule_type DNA !'##residues 1-29 ##label ANA GENETICS !$#gene tat CLASSIFICATION #superfamily AIDS trans-activating transcription regulator KEYWORDS transcription regulation SUMMARY #length 29 #molecular-weight 2967 #checksum 3506 SEQUENCE /// ENTRY TNLJZR #type complete TITLE trans-activating transcription regulator - human immunodeficiency virus Zr-6 ORGANISM #formal_name human immunodeficiency virus Zr-6 DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Jul-1999 ACCESSIONS C26192 REFERENCE A26192 !$#authors Srinivasan, A.; Anand, R.; York, D.; Ranganathan, P.; !1Feorino, P.; Schochetman, G.; Curran, J.; Kalyanaraman, !1V.S.; Luciw, P.A.; Sanchez-Pescador, R. !$#journal Gene (1987) 52:71-82 !$#title Molecular characterization of human immunodeficiency virus !1from Zaire: nucleotide sequence analysis identifies !1conserved and variable domains in the envelope gene. !$#cross-references MUID:87248097; PMID:3036660 !$#accession C26192 !'##molecule_type DNA !'##residues 1-86 ##label SRI !'##cross-references GB:K03458; GB:M16322; NID:g329398; PIDN:AAA45377.1; !1PID:g329400 GENETICS !$#gene tat !$#introns 72/3 CLASSIFICATION #superfamily AIDS trans-activating transcription regulator KEYWORDS AIDS; immunodeficiency; transcription regulation SUMMARY #length 86 #molecular-weight 9736 #checksum 827 SEQUENCE /// ENTRY TNLJND #type complete TITLE trans-activating transcription regulator - human immunodeficiency virus type 1 (isolate NDK) ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 #note host Homo sapiens (man) DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jul-1999 ACCESSIONS JQ0071 REFERENCE JQ0065 !$#authors Spire, B.; Sire, J.; Zachar, V.; Rey, F.; Barre-Sinoussi, !1F.; Galibert, F.; Hampe, A.; Chermann, J.C. !$#journal Gene (1989) 81:275-284 !$#title Nucleotide sequence of HIV1-NDK: a highly cytopathic strain !1of the human immunodeficiency virus. !$#cross-references MUID:90034200; PMID:2806917 !$#accession JQ0071 !'##molecule_type DNA !'##residues 1-86 ##label SPI !'##cross-references GB:M27323; NID:g328154; PIDN:AAA44866.1; !1PID:g328155 GENETICS !$#gene tat CLASSIFICATION #superfamily AIDS trans-activating transcription regulator KEYWORDS AIDS; immunodeficiency; transcription SUMMARY #length 86 #molecular-weight 9711 #checksum 369 SEQUENCE /// ENTRY TNLJSI #type complete TITLE trans-activating transcription regulator - simian immunodeficiency virus SIVcpz ORGANISM #formal_name simian immunodeficiency virus SIVcpz #note host Pan troglodytes (chimpanzee) DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jul-1999 ACCESSIONS S09987 REFERENCE S09983 !$#authors Huet, T.; Cheynier, R.; Meyerhans, A.; Roelants, G.; !1Wain-Hobson, S. !$#journal Nature (1990) 345:356-359 !$#title Genetic organization of a chimpanzee lentivirus related to !1HIV-1. !$#cross-references MUID:90259077; PMID:2188136 !$#accession S09987 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-100 ##label HUE !'##cross-references EMBL:X52154; NID:g58866; PIDN:CAA36404.1; !1PID:g763084 GENETICS !$#gene tat !$#introns 73/2 CLASSIFICATION #superfamily AIDS trans-activating transcription regulator KEYWORDS AIDS; immunodeficiency; transcription SUMMARY #length 100 #molecular-weight 11209 #checksum 9680 SEQUENCE /// ENTRY TNLJG2 #type complete TITLE trans-activating transcription regulator - human immunodeficiency virus type 2 (isolate ROD) ORGANISM #formal_name human immunodeficiency virus type 2, HIV-2 DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Jul-1999 ACCESSIONS E26262 REFERENCE A26262 !$#authors Guyader, M.; Emerman, M.; Sonigo, P.; Clavel, F.; !1Montagnier, L.; Alizon, M. !$#journal Nature (1987) 326:662-669 !$#title Genome organization and transactivation of the human !1immuno-deficiency virus type 2. !$#cross-references MUID:87173056; PMID:3031510 !$#contents proviral DNA !$#accession E26262 !'##molecule_type DNA !'##residues 1-130 ##label GUY !'##cross-references GB:M15390; NID:g1332361; PIDN:AAB00768.1; !1PID:g325743 GENETICS !$#gene tat !$#introns 99/3 CLASSIFICATION #superfamily AIDS trans-activating transcription regulator KEYWORDS AIDS; immunodeficiency; transcription regulation SUMMARY #length 130 #molecular-weight 14720 #checksum 6449 SEQUENCE /// ENTRY TNLJST #type complete TITLE trans-activating transcription regulator - human immunodeficiency virus type 2 (isolate ST) ALTERNATE_NAMES tat protein ORGANISM #formal_name human immunodeficiency virus type 2, HIV-2 #note host Homo sapiens (man) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS F33943 REFERENCE A33943 !$#authors Kumar, P.; Hui, H.; Kappes, J.C.; Haggarty, B.S.; Hoxie, !1J.A.; Arya, S.K.; Shaw, G.M.; Hahn, B.H. !$#journal J. Virol. (1990) 64:890-901 !$#title Molecular characterization of an attenuated human !1immunodeficiency virus type 2 isolate. !$#cross-references MUID:90112662; PMID:2296086 !$#accession F33943 !'##molecule_type genomic RNA !'##residues 1-130 ##label KUM !'##cross-references GB:M31113; NID:g1339798; PIDN:AAB01356.1; !1PID:g325753 GENETICS !$#gene tat !$#introns 99/2 CLASSIFICATION #superfamily AIDS trans-activating transcription regulator KEYWORDS transcription SUMMARY #length 130 #molecular-weight 14383 #checksum 3232 SEQUENCE /// ENTRY TNLJCA #type complete TITLE trans-activating transcription regulator - human immunodeficiency virus type 2 (isolate CAM2/Guinea-Bissau) ALTERNATE_NAMES tat protein ORGANISM #formal_name human immunodeficiency virus type 2, HIV-2 #note host Homo sapiens (man) DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jun-2000 ACCESSIONS I38475; JQ0981 REFERENCE A38475 !$#authors Tristem, M.; Hill, F.; Karpas, A. !$#journal J. Gen. Virol. (1991) 72:721-724 !$#title Nucleotide sequence of a Guinea-Bissau-derived human !1immunodeficiency virus type 2 proviral clone (HIV-2-CAM2). !$#cross-references MUID:91170959; PMID:2005437 !$#accession I38475 !'##molecule_type DNA !'##residues 1-133 ##label TRI !'##cross-references GB:D00835; NID:g3153166; PIDN:BAA00714.1; !1PID:g221467 GENETICS !$#gene tat !$#introns 102/2 CLASSIFICATION #superfamily AIDS trans-activating transcription regulator KEYWORDS transcription SUMMARY #length 133 #molecular-weight 14850 #checksum 6948 SEQUENCE /// ENTRY TNLJGG #type complete TITLE trans-activating transcription regulator - human immunodeficiency virus type 2 (isolate GH-1) ALTERNATE_NAMES tat protein ORGANISM #formal_name human immunodeficiency virus type 2, HIV-2 #note host Homo sapiens (man) DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jul-1999 ACCESSIONS JS0332 REFERENCE JS0327 !$#authors Hasegawa, A.; Tsujimoto, H.; Maki, N.; Ishikawa, K.; Miura, !1T.; Fukasawa, M.; Miki, K.; Hayami, M. !$#journal AIDS Res. Hum. Retroviruses (1989) 5:593-604 !$#title Sequence of a distinct HIV-2 isolate from Ghana showing !1significant divergence in its genome. !$#cross-references MUID:90122350; PMID:2611042 !$#accession JS0332 !'##molecule_type DNA !'##residues 1-130 ##label HAS !'##cross-references GB:M30895; GB:D00477; NID:g325709; PIDN:AAA43929.1; !1PID:g325710 !'##note this sequence was submitted to JIPID, October 1989 GENETICS !$#gene tat !$#introns 99/2 CLASSIFICATION #superfamily AIDS trans-activating transcription regulator KEYWORDS AIDS; transcription regulation SUMMARY #length 130 #molecular-weight 14580 #checksum 5383 SEQUENCE /// ENTRY TNLJS2 #type complete TITLE trans-activating transcription regulator - simian immunodeficiency virus SIVagm (type 3, isolate STLV-3agm) ORGANISM #formal_name simian immunodeficiency virus SIVagm DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 02-Jul-1998 ACCESSIONS A26737 REFERENCE A26737 !$#authors Hirsch, V.; Riedel, N.; Mullins, J.I. !$#journal Cell (1987) 49:307-319 !$#title The genome organization of STLV-3 is similar to that of the !1AIDS virus except for a truncated transmembrane protein. !$#cross-references MUID:87187627; PMID:3646094 !$#accession A26737 !'##molecule_type DNA !'##residues 1-106 ##label HIR !'##cross-references GB:M19499; NID:g334657 !'##note the authors translated the codon GAC for residue 9 as Asn GENETICS !$#gene tat !$#introns 74/2 CLASSIFICATION #superfamily AIDS trans-activating transcription regulator KEYWORDS AIDS; transcription SUMMARY #length 106 #molecular-weight 12166 #checksum 7558 SEQUENCE /// ENTRY TNLJG3 #type complete TITLE trans-activating transcription regulator - simian immunodeficiency virus (macaque isolate) ORGANISM #formal_name simian immunodeficiency virus, SIV DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 02-Jul-1998 ACCESSIONS F28887 REFERENCE A28887 !$#authors Chakrabarti, L.; Guyader, M.; Alizon, M.; Daniel, M.D.; !1Desrosiers, R.C.; Tiollais, P.; Sonigo, P. !$#journal Nature (1987) 328:543-547 !$#title Sequence of simian immunodeficiency virus from macaque and !1its relationship to other human and simian retroviruses. !$#cross-references MUID:87287230; PMID:3649576 !$#accession F28887 !'##molecule_type DNA !'##residues 1-129 ##label CHA !'##cross-references GB:Y00277; GB:M16403; NID:g61730 GENETICS !$#gene tat !$#introns 98/3 CLASSIFICATION #superfamily AIDS trans-activating transcription regulator KEYWORDS AIDS; immunodeficiency; transcription SUMMARY #length 129 #molecular-weight 14416 #checksum 412 SEQUENCE /// ENTRY TNLJG4 #type complete TITLE trans-activating transcription regulator - simian immunodeficiency virus (African green monkey isolate) ORGANISM #formal_name simian immunodeficiency virus, SIV DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 28-Jul-2000 ACCESSIONS E30045 REFERENCE A30045 !$#authors Fukasawa, M.; Miura, T.; Hasegawa, A.; Morikawa, S.; !1Tsujimoto, H.; Miki, K.; Kitamura, T.; Hayami, M. !$#journal Nature (1988) 333:457-461 !$#title Sequence of simian immunodeficiency virus from African green !1monkey, a new member of the HIV/SIV group. !$#cross-references MUID:88232906; PMID:3374586 !$#accession E30045 !'##molecule_type DNA !'##residues 1-100 ##label FUK !'##cross-references EMBL:X07805; NID:g61748; PIDN:CAA30661.1; !1PID:g4469309 GENETICS !$#gene tat !$#introns 73/2 CLASSIFICATION #superfamily AIDS trans-activating transcription regulator KEYWORDS AIDS; immunodeficiency; transcription SUMMARY #length 100 #molecular-weight 11387 #checksum 9282 SEQUENCE /// ENTRY A48344 #type complete TITLE trans-activating transcription regulator - simian immunodeficiency virus (isolate African mandrill) ORGANISM #formal_name simian immunodeficiency virus, SIV DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 02-Jul-1998 ACCESSIONS A48344 REFERENCE A48344 !$#authors Sakai, H.; Sakuragi, J.; Sakuragi, S.; Shibata, R.; Hayami, !1M.; Ishimoto, A.; Adachi, A. !$#journal Arch. Virol. (1992) 125:1-14 !$#title Genetic characterization of simian immunodeficiency virus !1isolated from an African mandrill. !$#cross-references MUID:92352315; PMID:1642547 !$#accession A48344 !'##molecule_type DNA !'##residues 1-116 ##label SAK !'##note sequence extracted from NCBI backbone (NCBIP:109904) GENETICS !$#gene tat CLASSIFICATION #superfamily AIDS trans-activating transcription regulator KEYWORDS AIDS; immunodeficiency; transcription SUMMARY #length 116 #molecular-weight 13311 #checksum 6491 SEQUENCE /// ENTRY TNLJBT #type complete TITLE trans-activating transcription regulator - bovine immunodeficiency virus (isolate 127) ORGANISM #formal_name bovine immunodeficiency virus DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 02-Jul-1998 ACCESSIONS D34742 REFERENCE A34742 !$#authors Garvey, K.J.; Oberste, M.S.; Elser, J.E.; Braun, M.J.; !1Gonda, M.A. !$#journal Virology (1990) 175:391-409 !$#title Nucleotide sequence and genome organization of biologically !1active proviruses of the bovine immunodeficiency-like virus. !$#cross-references MUID:90223985; PMID:2183467 !$#accession D34742 !'##molecule_type genomic RNA !'##residues 1-145 ##label GAR !'##cross-references GB:M32690 GENETICS !$#gene tat !$#introns 103/3 CLASSIFICATION #superfamily AIDS trans-activating transcription regulator KEYWORDS AIDS; immunodeficiency; transcription SUMMARY #length 145 #molecular-weight 16526 #checksum 8842 SEQUENCE /// ENTRY TNLJS1 #type complete TITLE trans-activating transcription regulator Tat [validated] - equine infectious anemia virus ALTERNATE_NAMES S1 ORF; tat protein; trans-activator protein ORGANISM #formal_name equine infectious anemia virus DATE 30-Jun-1993 #sequence_revision 29-Jan-1999 #text_change 15-Sep-2000 ACCESSIONS A46357; A45711; D41991; S51177 REFERENCE A46357 !$#authors Noiman, S.; Gazit, A.; Tori, O.; Sherman, L.; Miki, T.; !1Tronick, S.R.; Yaniv, A. !$#journal Virology (1990) 176:280-288 !$#title Identification of sequences encoding the equine infectious !1anemia virus tat gene. !$#cross-references MUID:90232740; PMID:2158694 !$#accession A46357 !'##molecule_type mRNA !'##residues 1-75 ##label NOI !'##cross-references GB:M36592; NID:g1374814; PIDN:AAB02403.1; !1PID:g1374815 !'##note the authors used the codon CUG for residue 1 as an initiator !1and translated it as Leu REFERENCE A45711 !$#authors Beisel, C.E.; Edwards, J.F.; Dunn, L.L.; Rice, N.R. !$#journal J. Virol. (1993) 67:832-842 !$#title Analysis of multiple mRNAs from pathogenic equine infectious !1anemia virus (EIAV) in an acutely infected horse reveals a !1novel protein, Ttm, derived from the carboxy terminus of the !1EIAV transmembrane protein. !$#cross-references MUID:93124578; PMID:8419648 !$#accession A45711 !'##molecule_type mRNA !'##residues 1-31,'G',33-51,'P',53-75 ##label BEI !'##cross-references GB:M93674; NID:g290632; PIDN:AAB59741.1; !1PID:g290634 !'##note sequence extracted from NCBI backbone (NCBIN:122349, !1NCBIP:122353) REFERENCE A41991 !$#authors Perry, S.T.; Flaherty, M.T.; Kelley, M.J.; Clabough, D.L.; !1Tronick, S.R.; Coggins, L.; Whetter, L.; Lengel, C.R.; !1Fuller, F. !$#journal J. Virol. (1992) 66:4085-4097 !$#title The surface envelope protein gene region of equine !1infectious anemia virus is not an important determinant of !1tropism in vitro. !$#cross-references MUID:92292230; PMID:1318398 !$#accession D41991 !'##molecule_type DNA !'##residues 'VLL',29-75 ##label PER !'##cross-references GB:M87581; NID:g290627 !'##experimental_source clone CL22 !'##note this ORF from Fig. 5 is not annotated in GenBank entry EIACGIP, !1release 109.0 REFERENCE S51177 !$#authors Sticht, H.; Willbold, D.; Ejchart, A.; Rosin-Arbesfeld, R.; !1Yaniv, A.; Gazit, A.; Roesch, P. !$#journal Eur. J. Biochem. (1994) 225:855-861 !$#title Trifluoroethanol stabilizes a helix-turn-helix motif in !1equine infectious-anemia-virus trans-activator protein. !$#cross-references MUID:95045562; PMID:7957222 !$#contents annotation !$#note conformation study of engineered sequence REFERENCE A52862 !$#authors Roesch, P.; Sticht, H. !$#submission submitted to the Brookhaven Protein Data Bank, September !11994 !$#cross-references PDB:1TVS !$#contents annotation; conformation by (1)H-NMR, residues 1-75 !$#note recombinant form expressed in Escherichia coli REFERENCE A58937 !$#authors Sticht, H.; Willbold, D.; Bayer, P.; Ejchart, A.; Herrmann, !1F.; Rosin-Arbesfeld, R.; Gazit, A.; Yaniv, A.; Frank, R.; !1Roesch, P. !$#journal Eur. J. Biochem. (1993) 218:973-976 !$#title Equine infectious anemia virus Tat is a predominantly !1helical protein. !$#cross-references MUID:94109398; PMID:7506657 !$#contents annotation; conformation by (1)H-NMR REFERENCE A66778 !$#authors Roesch, P.; Willbold, D. !$#submission submitted to the Brookhaven Protein Data Bank, July 1994 !$#cross-references PDB:1TVT !$#contents annotation; conformation by (1)H- and (15)N-NMR, residues !11-75 !$#note engineered recombinant form expressed in Escherichia coli REFERENCE A58936 !$#authors Willbold, D.; Rosin-Arbesfeld, R.; Sticht, H.; Frank, R.; !1Roesch, P. !$#journal Science (1994) 264:1584-1587 !$#title Structure of the equine infectious anemia virus Tat protein. !$#cross-references MUID:94261831; PMID:7515512 !$#contents annotation; conformation by (1)H-, and (15)N-NMR REFERENCE A53347 !$#authors Willbold, D.; Krueger, U.; Frank, R.; Rosin-Arbesfeld, R.; !1Gazit, A.; Yaniv, A.; Roesch, P. !$#journal Biochemistry (1993) 32:8439-8445 !$#title Sequence-specific resonance assignments of the (1)H-NMR !1spectra of a synthetic, biologically active EIAV Tat !1protein. !$#cross-references MUID:93363572; PMID:8395203 !$#contents annotation; conformation by (1)H-NMR GENETICS !$#gene tat !$#start_codon CTG CLASSIFICATION #superfamily equine infectious anemia virus trans-activating !1transcription regulator KEYWORDS transcription regulation FEATURE !$55-63 #region nuclear location signal SUMMARY #length 75 #molecular-weight 8395 #checksum 8876 SEQUENCE /// ENTRY VKLJH3 #type complete TITLE trans-regulatory splicing protein - human immunodeficiency virus type 1 (isolate HTLV-III) ALTERNATE_NAMES anti-repression trans-activator ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 #note host Homo sapiens (man) DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 23-Feb-1997 ACCESSIONS A04018 REFERENCE A04018 !$#authors Sodroski, J.; Goh, W.C.; Rosen, C.; Dayton, A.; Terwilliger, !1E.; Haseltine, W. !$#journal Nature (1986) 321:412-417 !$#title A second post-transcriptional trans-activator gene required !1for HTLV-III replication. !$#cross-references MUID:86230863; PMID:3012355 !$#accession A04018 !'##molecule_type DNA !'##residues 1-116 ##label SOD GENETICS !$#gene trs; art !$#introns 25/3 CLASSIFICATION #superfamily AIDS trans-regulatory splicing protein KEYWORDS AIDS; immunodeficiency; RNA binding; transcription !1regulation FEATURE !$34-46 #region arginine-rich RNA-binding pattern SUMMARY #length 116 #molecular-weight 13038 #checksum 6274 SEQUENCE /// ENTRY F44001 #type complete TITLE trans-regulatory splicing protein - human immunodeficiency virus type 1 (strain YU-2) ALTERNATE_NAMES anti-repression trans-activator ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 #note host Homo sapiens (man) DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 23-Feb-1997 ACCESSIONS F44001 REFERENCE A44001 !$#authors Li, Y.; Hui, H.; Burgess, C.J.; Price, R.W.; Sharp, P.M.; !1Hahn, B.H.; Shaw, G.M. !$#journal J. Virol. (1992) 66:6587-6600 !$#title Complete nucleotide sequence, genome organization, and !1biological properties of human immunodeficiency virus type 1 !1in vivo: evidence for limited defectiveness and !1complementation. !$#cross-references MUID:93021387; PMID:1404605 !$#accession F44001 !'##molecule_type DNA !'##residues 1-116 ##label LIY !'##cross-references GB:M93258 GENETICS !$#gene trs; art !$#introns 26/1 CLASSIFICATION #superfamily AIDS trans-regulatory splicing protein KEYWORDS AIDS; immunodeficiency; RNA binding; transcription !1regulation FEATURE !$34-46 #region arginine-rich RNA-binding pattern SUMMARY #length 116 #molecular-weight 13086 #checksum 9029 SEQUENCE /// ENTRY VKLJND #type complete TITLE trans-regulatory splicing protein - human immunodeficiency virus type 1 (isolate NDK) ALTERNATE_NAMES anti-repression trans-activator; art protein; rev protein; trs protein ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 #note host Homo sapiens (man) DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 23-Feb-1997 ACCESSIONS JQ0072 REFERENCE JQ0065 !$#authors Spire, B.; Sire, J.; Zachar, V.; Rey, F.; Barre-Sinoussi, !1F.; Galibert, F.; Hampe, A.; Chermann, J.C. !$#journal Gene (1989) 81:275-284 !$#title Nucleotide sequence of HIV1-NDK: a highly cytopathic strain !1of the human immunodeficiency virus. !$#cross-references MUID:90034200; PMID:2806917 !$#accession JQ0072 !'##molecule_type DNA !'##residues 1-115 ##label SPI !'##cross-references GB:M27323 GENETICS !$#gene rev; trs; art CLASSIFICATION #superfamily AIDS trans-regulatory splicing protein KEYWORDS AIDS; immunodeficiency; RNA binding; splicing protein; !1transcription regulation FEATURE !$33-45 #region arginine-rich RNA-binding pattern SUMMARY #length 115 #molecular-weight 12858 #checksum 5684 SEQUENCE /// ENTRY VKLJBR #type complete TITLE trans-regulatory splicing protein - human immunodeficiency virus type 1 (isolate BR) ALTERNATE_NAMES anti-repression trans-activator ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 #note host Homo sapiens (man) DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 23-Feb-1997 ACCESSIONS C31667 REFERENCE A94389 !$#authors Anand, R.; Thayer, R.; Srinivasan, A.; Nayyar, S.; Gardner, !1M.; Luciw, P.; Dandekar, S. !$#journal Virology (1989) 168:79-89 !$#title Biological and molecular characterization of human !1immunodeficiency virus (HIV-1-BR) from the brain of a !1patient with progressive dementia. !$#cross-references MUID:89085613; PMID:2789516 !$#accession C31667 !'##molecule_type DNA !'##residues 1-90 ##label ANA GENETICS !$#gene trs; art CLASSIFICATION #superfamily AIDS trans-regulatory splicing protein KEYWORDS RNA binding; splicing protein; transcription regulation FEATURE !$8-20 #region arginine-rich RNA-binding pattern SUMMARY #length 90 #molecular-weight 10074 #checksum 2662 SEQUENCE /// ENTRY VKLJSI #type complete TITLE trans-regulatory splicing protein - simian immunodeficiency virus SIVcpz ALTERNATE_NAMES anti-repression trans-activator; art protein; rev protein; trs protein ORGANISM #formal_name simian immunodeficiency virus SIVcpz #note host Pan troglodytes (chimpanzee) DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jul-1999 ACCESSIONS S09988 REFERENCE S09983 !$#authors Huet, T.; Cheynier, R.; Meyerhans, A.; Roelants, G.; !1Wain-Hobson, S. !$#journal Nature (1990) 345:356-359 !$#title Genetic organization of a chimpanzee lentivirus related to !1HIV-1. !$#cross-references MUID:90259077; PMID:2188136 !$#accession S09988 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-124 ##label HUE !'##cross-references EMBL:X52154; NID:g58866; PIDN:CAA36405.1; !1PID:g763085 GENETICS !$#gene rev; trs; art !$#introns 27/1 CLASSIFICATION #superfamily AIDS trans-regulatory splicing protein KEYWORDS AIDS; immunodeficiency; splicing protein; transcription !1regulation SUMMARY #length 124 #molecular-weight 13701 #checksum 987 SEQUENCE /// ENTRY VKLJG2 #type complete TITLE trans-regulatory splicing protein - human immunodeficiency virus type 2 (isolate ROD) ALTERNATE_NAMES anti-repression trans-activator ORGANISM #formal_name human immunodeficiency virus type 2, HIV-2 DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Jul-1999 ACCESSIONS F26262 REFERENCE A26262 !$#authors Guyader, M.; Emerman, M.; Sonigo, P.; Clavel, F.; !1Montagnier, L.; Alizon, M. !$#journal Nature (1987) 326:662-669 !$#title Genome organization and transactivation of the human !1immuno-deficiency virus type 2. !$#cross-references MUID:87173056; PMID:3031510 !$#contents proviral DNA !$#accession F26262 !'##molecule_type DNA !'##residues 1-100 ##label GUY !'##cross-references GB:M15390; NID:g1332361; PIDN:AAB00769.1; !1PID:g325744 GENETICS !$#gene trs; art !$#introns 23/3 CLASSIFICATION #superfamily AIDS trans-regulatory splicing protein KEYWORDS AIDS; immunodeficiency; splicing protein; transcription !1regulation SUMMARY #length 100 #molecular-weight 11726 #checksum 1053 SEQUENCE /// ENTRY VKLJST #type complete TITLE trans-regulatory splicing protein - human immunodeficiency virus type 2 (isolate ST) ALTERNATE_NAMES anti-repression trans-activator; art protein; rev protein; trs protein ORGANISM #formal_name human immunodeficiency virus type 2, HIV-2 #note host Homo sapiens (man) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS G33943 REFERENCE A33943 !$#authors Kumar, P.; Hui, H.; Kappes, J.C.; Haggarty, B.S.; Hoxie, !1J.A.; Arya, S.K.; Shaw, G.M.; Hahn, B.H. !$#journal J. Virol. (1990) 64:890-901 !$#title Molecular characterization of an attenuated human !1immunodeficiency virus type 2 isolate. !$#cross-references MUID:90112662; PMID:2296086 !$#accession G33943 !'##molecule_type genomic RNA !'##residues 1-107 ##label KUM !'##cross-references GB:M31113; NID:g1339798; PIDN:AAB01357.1; !1PID:g325754 GENETICS !$#gene rev; trs; art !$#introns 24/1 CLASSIFICATION #superfamily AIDS trans-regulatory splicing protein KEYWORDS splicing protein; transcription regulation SUMMARY #length 107 #molecular-weight 12576 #checksum 6359 SEQUENCE /// ENTRY VKLJCA #type complete TITLE trans-regulatory splicing protein - human immunodeficiency virus type 2 (isolate CAM2/Guinea-Bissau) ALTERNATE_NAMES antirepression trans-activator; art protein; rev protein; trs protein ORGANISM #formal_name human immunodeficiency virus type 2, HIV-2 #note host Homo sapiens (man) DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jun-2000 ACCESSIONS H38475; JQ0980 REFERENCE A38475 !$#authors Tristem, M.; Hill, F.; Karpas, A. !$#journal J. Gen. Virol. (1991) 72:721-724 !$#title Nucleotide sequence of a Guinea-Bissau-derived human !1immunodeficiency virus type 2 proviral clone (HIV-2-CAM2). !$#cross-references MUID:91170959; PMID:2005437 !$#accession H38475 !'##molecule_type DNA !'##residues 1-100 ##label TRI !'##cross-references GB:D00835; NID:g3153166; PIDN:BAA00715.1; !1PID:g221466 GENETICS !$#gene rev !$#introns 24/1 CLASSIFICATION #superfamily AIDS trans-regulatory splicing protein KEYWORDS splicing protein; transcription regulation SUMMARY #length 100 #molecular-weight 11860 #checksum 552 SEQUENCE /// ENTRY VKLJGG #type complete TITLE trans-regulatory splicing protein - human immunodeficiency virus type 2 (isolate GH-1) ALTERNATE_NAMES rev protein ORGANISM #formal_name human immunodeficiency virus type 2, HIV-2 #note host Homo sapiens (man) DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jul-1999 ACCESSIONS JS0333 REFERENCE JS0327 !$#authors Hasegawa, A.; Tsujimoto, H.; Maki, N.; Ishikawa, K.; Miura, !1T.; Fukasawa, M.; Miki, K.; Hayami, M. !$#journal AIDS Res. Hum. Retroviruses (1989) 5:593-604 !$#title Sequence of a distinct HIV-2 isolate from Ghana showing !1significant divergence in its genome. !$#cross-references MUID:90122350; PMID:2611042 !$#accession JS0333 !'##molecule_type DNA !'##residues 1-103 ##label HAS !'##cross-references GB:M30895; GB:D00477; NID:g325709; PIDN:AAA43930.1; !1PID:g325711 !'##note this sequence was submitted to JIPID, October 1989 GENETICS !$#gene rev !$#introns 24/1 CLASSIFICATION #superfamily AIDS trans-regulatory splicing protein KEYWORDS AIDS; transcription regulation SUMMARY #length 103 #molecular-weight 12049 #checksum 844 SEQUENCE /// ENTRY VKLJS2 #type complete TITLE trans-regulatory splicing protein - simian immunodeficiency virus SIVagm (type 3, isolate STLV-3agm) ORGANISM #formal_name simian immunodeficiency virus SIVagm DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 07-Nov-1997 ACCESSIONS B26737 REFERENCE A26737 !$#authors Hirsch, V.; Riedel, N.; Mullins, J.I. !$#journal Cell (1987) 49:307-319 !$#title The genome organization of STLV-3 is similar to that of the !1AIDS virus except for a truncated transmembrane protein. !$#cross-references MUID:87187627; PMID:3646094 !$#accession B26737 !'##molecule_type DNA !'##residues 1-108 ##label HIR !'##cross-references GB:M19499; NID:g334657 GENETICS !$#gene trs; art !$#introns 24/1 CLASSIFICATION #superfamily AIDS trans-regulatory splicing protein KEYWORDS AIDS; splicing protein; transcription regulation SUMMARY #length 108 #molecular-weight 12689 #checksum 171 SEQUENCE /// ENTRY VKLJG3 #type complete TITLE trans-regulatory splicing protein - simian immunodeficiency virus (macaque isolate) ORGANISM #formal_name simian immunodeficiency virus, SIV DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 07-Nov-1997 ACCESSIONS G28887 REFERENCE A28887 !$#authors Chakrabarti, L.; Guyader, M.; Alizon, M.; Daniel, M.D.; !1Desrosiers, R.C.; Tiollais, P.; Sonigo, P. !$#journal Nature (1987) 328:543-547 !$#title Sequence of simian immunodeficiency virus from macaque and !1its relationship to other human and simian retroviruses. !$#cross-references MUID:87287230; PMID:3649576 !$#accession G28887 !'##molecule_type DNA !'##residues 1-106 ##label CHA !'##cross-references GB:Y00277; GB:M16403; NID:g61730 GENETICS !$#gene trs; art !$#introns 23/3 CLASSIFICATION #superfamily AIDS trans-regulatory splicing protein KEYWORDS AIDS; immunodeficiency; splicing protein; transcription !1regulation SUMMARY #length 106 #molecular-weight 12329 #checksum 2536 SEQUENCE /// ENTRY VKLJG4 #type complete TITLE trans-regulatory splicing protein - simian immunodeficiency virus (African green monkey isolate) ORGANISM #formal_name simian immunodeficiency virus, SIV DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 28-Jul-2000 ACCESSIONS F30045 REFERENCE A30045 !$#authors Fukasawa, M.; Miura, T.; Hasegawa, A.; Morikawa, S.; !1Tsujimoto, H.; Miki, K.; Kitamura, T.; Hayami, M. !$#journal Nature (1988) 333:457-461 !$#title Sequence of simian immunodeficiency virus from African green !1monkey, a new member of the HIV/SIV group. !$#cross-references MUID:88232906; PMID:3374586 !$#accession F30045 !'##molecule_type DNA !'##residues 1-84 ##label FUK !'##cross-references EMBL:X07805; NID:g61748; PIDN:CAA30662.1; !1PID:g4469310 GENETICS !$#gene trs; art !$#introns 21/1 CLASSIFICATION #superfamily AIDS trans-regulatory splicing protein KEYWORDS AIDS; immunodeficiency; splicing protein; transcription !1regulation SUMMARY #length 84 #molecular-weight 10012 #checksum 8418 SEQUENCE /// ENTRY B48344 #type complete TITLE trans-regulatory splicing protein - simian immunodeficiency virus (isolate African mandrill) ORGANISM #formal_name simian immunodeficiency virus, SIV DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS B48344 REFERENCE A48344 !$#authors Sakai, H.; Sakuragi, J.; Sakuragi, S.; Shibata, R.; Hayami, !1M.; Ishimoto, A.; Adachi, A. !$#journal Arch. Virol. (1992) 125:1-14 !$#title Genetic characterization of simian immunodeficiency virus !1isolated from an African mandrill. !$#cross-references MUID:92352315; PMID:1642547 !$#accession B48344 !'##molecule_type DNA !'##residues 1-96 ##label SAK !'##cross-references GB:M62884; NID:g334737; PIDN:AAA47726.1; !1PID:g334741 !'##note sequence extracted from NCBI backbone (NCBIP:109905) GENETICS !$#gene trs; art CLASSIFICATION #superfamily AIDS trans-regulatory splicing protein KEYWORDS AIDS; immunodeficiency; splicing protein; transcription !1regulation SUMMARY #length 96 #molecular-weight 10894 #checksum 7702 SEQUENCE /// ENTRY VKLJBT #type complete TITLE trans-regulatory splicing protein - bovine immunodeficiency virus (isolate 127) ALTERNATE_NAMES anti-repression trans-activator; art protein; rev protein; trs protein ORGANISM #formal_name bovine immunodeficiency virus DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 23-Feb-1997 ACCESSIONS H34742 REFERENCE A34742 !$#authors Garvey, K.J.; Oberste, M.S.; Elser, J.E.; Braun, M.J.; !1Gonda, M.A. !$#journal Virology (1990) 175:391-409 !$#title Nucleotide sequence and genome organization of biologically !1active proviruses of the bovine immunodeficiency-like virus. !$#cross-references MUID:90223985; PMID:2183467 !$#accession H34742 !'##molecule_type genomic RNA !'##residues 1-179 ##label GAR !'##cross-references GB:M32690 GENETICS !$#gene rev; trs; art !$#introns 13/3 CLASSIFICATION #superfamily BIV trans-regulatory splicing protein KEYWORDS AIDS; immunodeficiency; splicing protein; transcription !1regulation SUMMARY #length 179 #molecular-weight 20236 #checksum 2943 SEQUENCE /// ENTRY VKLJVS #type complete TITLE trans-regulatory splicing protein - Maedi/Visna virus ALTERNATE_NAMES antirepression trans-activator; art protein; rev protein; trs protein ORGANISM #formal_name Maedi/Visna virus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jul-1999 ACCESSIONS B32184 REFERENCE A32184 !$#authors Davis, J.L.; Clements, J.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:414-418 !$#title Characterization of a cDNA clone encoding the visna virus !1transactivating protein. !$#cross-references MUID:89098943; PMID:2536163 !$#accession B32184 !'##molecule_type mRNA !'##residues 1-167 ##label DAV !'##cross-references GB:M23048; EMBL:J04163; NID:g533270; !1PIDN:AAA48363.1; PID:g533271 GENETICS !$#gene rev CLASSIFICATION #superfamily Visna virus trans-regulatory splicing protein KEYWORDS splicing protein; transcription regulation SUMMARY #length 167 #molecular-weight 19209 #checksum 3636 SEQUENCE /// ENTRY VKLJVA #type complete TITLE trans-regulatory splicing protein - Maedi/Visna virus (strain K1514) ALTERNATE_NAMES antirepression trans-activator; art protein; rev protein; trs protein ORGANISM #formal_name Maedi/Visna virus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 23-Feb-1997 ACCESSIONS A32441 REFERENCE A32441 !$#authors Gourdou, I.; Mazarin, V.; Querat, G.; Sauze, N.; Vigne, R. !$#journal Virology (1989) 171:170-178 !$#title The open reading frame S of visna virus genome is a !1trans-activating gene. !$#cross-references MUID:89299455; PMID:2545028 !$#accession A32441 !'##molecule_type mRNA !'##residues 1-167 ##label GOU !'##cross-references EMBL:J04359 GENETICS !$#gene rev CLASSIFICATION #superfamily Visna virus trans-regulatory splicing protein KEYWORDS splicing protein; transcription regulation SUMMARY #length 167 #molecular-weight 19225 #checksum 3252 SEQUENCE /// ENTRY F45390 #type complete TITLE trans-regulatory splicing protein - Maedi/Visna virus (strain KV1772) (provirus) ALTERNATE_NAMES antirepression trans-activator; art protein; rev protein; trs protein ORGANISM #formal_name Maedi/Visna virus #note host Homo sapiens (man) DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS F45390 REFERENCE A45390 !$#authors Andresson, O.S.; Elser, J.E.; Tobin, G.J.; Greenwood, J.D.; !1Gonda, M.A.; Georgsson, G.; Andresdottir, V.; !1Benediktsdottir, E.; Carlsdottir, H.M.; Maentylae, E.O.; !1Rafnar, B.; Palsson, P.A.; Casey, J.W.; Petursson, G. !$#journal Virology (1993) 193:89-105 !$#title Nucleotide sequence and biological properties of a !1pathogenic proviral molecular clone of neurovirulent visna !1virus. !$#cross-references MUID:93174981; PMID:8382414 !$#accession F45390 !'##molecule_type DNA !'##residues 1-167 ##label AND !'##cross-references GB:S55323; NID:g265825; PIDN:AAB25464.1; !1PID:g265831 GENETICS !$#gene rev CLASSIFICATION #superfamily Visna virus trans-regulatory splicing protein KEYWORDS splicing protein; transcription regulation SUMMARY #length 167 #molecular-weight 19163 #checksum 3487 SEQUENCE /// ENTRY F46335 #type complete TITLE trans-regulatory splicing protein - Maedi/Visna virus (strain SA-OMVV) ALTERNATE_NAMES antirepression trans-activator; art protein; rev protein; trs protein ORGANISM #formal_name Maedi/Visna virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS F46335 REFERENCE A46335 !$#authors Querat, G.; Audoly, G.; Sonigo, P.; Vigne, R. !$#journal Virology (1990) 175:434-447 !$#title Nucleotide sequence analysis of SA-OMVV, a visna-related !1ovine lentivirus: phylogenetic history of lentiviruses. !$#cross-references MUID:90223989; PMID:2158181 !$#accession F46335 !'##molecule_type DNA !'##residues 1-144 ##label QUE !'##cross-references GB:M31646; NID:g808756; PIDN:AAA66816.1; !1PID:g332547 GENETICS !$#gene rev CLASSIFICATION #superfamily Visna virus trans-regulatory splicing protein KEYWORDS splicing protein; transcription regulation SUMMARY #length 144 #molecular-weight 16546 #checksum 9151 SEQUENCE /// ENTRY VKLJCE #type complete TITLE trans-regulatory splicing-like protein - caprine arthritis-encephalitis virus ALTERNATE_NAMES rev-like protein ORGANISM #formal_name caprine arthritis-encephalitis virus, CAEV DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS A40479 REFERENCE A40479 !$#authors Kalinski, H.; Yaniv, A.; Mashiah, P.; Miki, T.; Tronick, !1S.R.; Gazit, A. !$#journal Virology (1991) 183:786-792 !$#title rev-like transcripts of caprine arthritis encephalitis !1virus. !$#cross-references MUID:91306466; PMID:1649509 !$#accession A40479 !'##molecule_type mRNA !'##residues 1-133 ##label KAL !'##cross-references GB:M63105; NID:g323291; PIDN:AAA42893.1; !1PID:g323292 GENETICS !$#gene rev CLASSIFICATION #superfamily caprine arthritis-encephalitis virus rev-like !1protein KEYWORDS splicing protein; transcription regulation SUMMARY #length 133 #molecular-weight 15267 #checksum 9837 SEQUENCE /// ENTRY F45345 #type complete TITLE trans-regulatory splicing-like protein - caprine arthritis-encephalitis virus (strain CO) ALTERNATE_NAMES rev-like protein ORGANISM #formal_name caprine arthritis-encephalitis virus, CAEV DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 26-Feb-1999 ACCESSIONS F45345 REFERENCE A45345 !$#authors Saltarelli, M.; Querat, G.; Konings, D.A.M.; Vigne, R.; !1Clements, J.E. !$#journal Virology (1990) 179:347-364 !$#title Nucleotide sequence and transcriptional analysis of !1molecular clones of CAEV which generate infectious virus. !$#cross-references MUID:91021037; PMID:2171210 !$#accession F45345 !'##molecule_type mRNA !'##residues 1-133 ##label SAL !'##cross-references GB:M33677 GENETICS !$#gene rev !$#introns 38/1 CLASSIFICATION #superfamily caprine arthritis-encephalitis virus rev-like !1protein KEYWORDS splicing protein; transcription regulation SUMMARY #length 133 #molecular-weight 15283 #checksum 2628 SEQUENCE /// ENTRY ASLJR2 #type complete TITLE vpr protein - human immunodeficiency virus type 2 (isolate ROD) ALTERNATE_NAMES orf-R protein ORGANISM #formal_name human immunodeficiency virus type 2, HIV-2 DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Jul-1999 ACCESSIONS H26262 REFERENCE A26262 !$#authors Guyader, M.; Emerman, M.; Sonigo, P.; Clavel, F.; !1Montagnier, L.; Alizon, M. !$#journal Nature (1987) 326:662-669 !$#title Genome organization and transactivation of the human !1immuno-deficiency virus type 2. !$#cross-references MUID:87173056; PMID:3031510 !$#accession H26262 !'##molecule_type DNA !'##residues 1-105 ##label GUY !'##cross-references GB:M15390; NID:g1332361; PIDN:AAB00767.1; !1PID:g325748 GENETICS !$#gene vpr CLASSIFICATION #superfamily AIDS vpr protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 105 #molecular-weight 11794 #checksum 4077 SEQUENCE /// ENTRY ASLJSY #type complete TITLE vpr protein - human immunodeficiency virus type 2 (isolate ST) ALTERNATE_NAMES orf-R protein ORGANISM #formal_name human immunodeficiency virus type 2, HIV-2 #note host Homo sapiens (man) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS E33943 REFERENCE A33943 !$#authors Kumar, P.; Hui, H.; Kappes, J.C.; Haggarty, B.S.; Hoxie, !1J.A.; Arya, S.K.; Shaw, G.M.; Hahn, B.H. !$#journal J. Virol. (1990) 64:890-901 !$#title Molecular characterization of an attenuated human !1immunodeficiency virus type 2 isolate. !$#cross-references MUID:90112662; PMID:2296086 !$#accession E33943 !'##molecule_type genomic RNA !'##residues 1-104 ##label KUM !'##cross-references GB:M31113; NID:g1339798; PIDN:AAB01355.1; !1PID:g325752 GENETICS !$#gene vpr CLASSIFICATION #superfamily AIDS vpr protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 104 #molecular-weight 11775 #checksum 2017 SEQUENCE /// ENTRY ASLJCY #type complete TITLE vpr protein - human immunodeficiency virus type 2 (isolate CAM2/Guinea-Bissau) ALTERNATE_NAMES orf-R protein ORGANISM #formal_name human immunodeficiency virus type 2, HIV-2 #note host Homo sapiens (man) DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jun-2000 ACCESSIONS E38475; JQ0977 REFERENCE A38475 !$#authors Tristem, M.; Hill, F.; Karpas, A. !$#journal J. Gen. Virol. (1991) 72:721-724 !$#title Nucleotide sequence of a Guinea-Bissau-derived human !1immunodeficiency virus type 2 proviral clone (HIV-2-CAM2). !$#cross-references MUID:91170959; PMID:2005437 !$#accession E38475 !'##molecule_type DNA !'##residues 1-104 ##label TRI !'##cross-references GB:D00835; NID:g3153166; PIDN:BAA00713.1; !1PID:g221471 GENETICS !$#gene vpr CLASSIFICATION #superfamily AIDS vpr protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 104 #molecular-weight 11769 #checksum 9301 SEQUENCE /// ENTRY ASLJGR #type complete TITLE vpr protein - human immunodeficiency virus type 2 (isolate GH-1) ALTERNATE_NAMES orf-R protein ORGANISM #formal_name human immunodeficiency virus type 2, HIV-2 #note host Homo sapiens (man) DATE 30-Jun-1990 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS JS0331 REFERENCE JS0327 !$#authors Hasegawa, A.; Tsujimoto, H.; Maki, N.; Ishikawa, K.; Miura, !1T.; Fukasawa, M.; Miki, K.; Hayami, M. !$#journal AIDS Res. Hum. Retroviruses (1989) 5:593-604 !$#title Sequence of a distinct HIV-2 isolate from Ghana showing !1significant divergence in its genome. !$#cross-references MUID:90122350; PMID:2611042 !$#accession JS0331 !'##molecule_type DNA !'##residues 1-105 ##label HAS !'##cross-references GB:M30895; NID:g325709; PIDN:AAA43936.1; !1PID:g325717 GENETICS !$#gene vpr CLASSIFICATION #superfamily AIDS vpr protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 105 #molecular-weight 11997 #checksum 4732 SEQUENCE /// ENTRY ASLJRS #type complete TITLE vpr protein - simian immunodeficiency virus SIVagm (type 3, isolate STLV-3agm) ALTERNATE_NAMES orf-R protein ORGANISM #formal_name simian immunodeficiency virus SIVagm DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 07-Nov-1997 ACCESSIONS E26737 REFERENCE A26737 !$#authors Hirsch, V.; Riedel, N.; Mullins, J.I. !$#journal Cell (1987) 49:307-319 !$#title The genome organization of STLV-3 is similar to that of the !1AIDS virus except for a truncated transmembrane protein. !$#cross-references MUID:87187627; PMID:3646094 !$#accession E26737 !'##molecule_type DNA !'##residues 1-122 ##label HIR !'##cross-references GB:M19499; NID:g334657 GENETICS !$#gene vpr CLASSIFICATION #superfamily AIDS vpr protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 122 #molecular-weight 14104 #checksum 3334 SEQUENCE /// ENTRY ASLJR3 #type complete TITLE vpr protein - simian immunodeficiency virus (macaque isolate) ALTERNATE_NAMES orf-R protein ORGANISM #formal_name simian immunodeficiency virus, SIV DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jul-1999 ACCESSIONS E28887 REFERENCE A28887 !$#authors Chakrabarti, L.; Guyader, M.; Alizon, M.; Daniel, M.D.; !1Desrosiers, R.C.; Tiollais, P.; Sonigo, P. !$#journal Nature (1987) 328:543-547 !$#title Sequence of simian immunodeficiency virus from macaque and !1its relationship to other human and simian retroviruses. !$#cross-references MUID:87287230; PMID:3649576 !$#accession E28887 !'##molecule_type DNA !'##residues 1-101 ##label CHA !'##cross-references GB:Y00277; GB:M16403; NID:g61730; PIDN:CAA68383.1; !1PID:g61735 GENETICS !$#gene vpr CLASSIFICATION #superfamily AIDS vpr protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 101 #molecular-weight 11461 #checksum 893 SEQUENCE /// ENTRY ASLJSC #type complete TITLE vpr protein - simian immunodeficiency virus SIVcpz ALTERNATE_NAMES orf-R protein ORGANISM #formal_name simian immunodeficiency virus SIVcpz #note host Pan troglodytes (chimpanzee) DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jul-1999 ACCESSIONS S09986 REFERENCE S09983 !$#authors Huet, T.; Cheynier, R.; Meyerhans, A.; Roelants, G.; !1Wain-Hobson, S. !$#journal Nature (1990) 345:356-359 !$#title Genetic organization of a chimpanzee lentivirus related to !1HIV-1. !$#cross-references MUID:90259077; PMID:2188136 !$#accession S09986 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-96 ##label HUE !'##cross-references EMBL:X52154; NID:g58866; PIDN:CAA36403.1; !1PID:g58870 GENETICS !$#gene vpr CLASSIFICATION #superfamily AIDS vpr protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 96 #molecular-weight 11376 #checksum 8760 SEQUENCE /// ENTRY D44001 #type complete TITLE vpr protein - human immunodeficiency virus type 1 (strain YU-2) ALTERNATE_NAMES orf-R protein ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 #note host Homo sapiens (man) DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 31-Jan-1997 ACCESSIONS D44001 REFERENCE A44001 !$#authors Li, Y.; Hui, H.; Burgess, C.J.; Price, R.W.; Sharp, P.M.; !1Hahn, B.H.; Shaw, G.M. !$#journal J. Virol. (1992) 66:6587-6600 !$#title Complete nucleotide sequence, genome organization, and !1biological properties of human immunodeficiency virus type 1 !1in vivo: evidence for limited defectiveness and !1complementation. !$#cross-references MUID:93021387; PMID:1404605 !$#accession D44001 !'##molecule_type DNA !'##residues 1-97 ##label LIY !'##cross-references GB:M93258 GENETICS !$#gene vpr CLASSIFICATION #superfamily AIDS vpr protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 97 #molecular-weight 11475 #checksum 9525 SEQUENCE /// ENTRY ASLJNK #type complete TITLE vpu protein - human immunodeficiency virus type 1 (isolate NDK) ALTERNATE_NAMES orf-X protein ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 #note host Homo sapiens (man) DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jul-1999 ACCESSIONS JQ0070 REFERENCE JQ0065 !$#authors Spire, B.; Sire, J.; Zachar, V.; Rey, F.; Barre-Sinoussi, !1F.; Galibert, F.; Hampe, A.; Chermann, J.C. !$#journal Gene (1989) 81:275-284 !$#title Nucleotide sequence of HIV1-NDK: a highly cytopathic strain !1of the human immunodeficiency virus. !$#cross-references MUID:90034200; PMID:2806917 !$#accession JQ0070 !'##molecule_type DNA !'##residues 1-81 ##label SPI !'##cross-references GB:M27323; NID:g328154; PIDN:AAA44872.1; !1PID:g328161 GENETICS !$#gene vpu CLASSIFICATION #superfamily HIV-1 vpu protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 81 #molecular-weight 9382 #checksum 7697 SEQUENCE /// ENTRY G44001 #type complete TITLE vpu protein - human immunodeficiency virus type 1 (strain YU-2) ALTERNATE_NAMES orf-X protein ORGANISM #formal_name human immunodeficiency virus type 1, HIV-1 #note host Homo sapiens (man) DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 31-Jan-1997 ACCESSIONS G44001 REFERENCE A44001 !$#authors Li, Y.; Hui, H.; Burgess, C.J.; Price, R.W.; Sharp, P.M.; !1Hahn, B.H.; Shaw, G.M. !$#journal J. Virol. (1992) 66:6587-6600 !$#title Complete nucleotide sequence, genome organization, and !1biological properties of human immunodeficiency virus type 1 !1in vivo: evidence for limited defectiveness and !1complementation. !$#cross-references MUID:93021387; PMID:1404605 !$#accession G44001 !'##molecule_type DNA !'##residues 1-81 ##label LIY !'##cross-references GB:M93258 GENETICS !$#gene vpu !$#start_codon CTG CLASSIFICATION #superfamily HIV-1 vpu protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 81 #molecular-weight 9210 #checksum 8642 SEQUENCE /// ENTRY ASLJSK #type complete TITLE vpu protein - simian immunodeficiency virus SIVcpz ALTERNATE_NAMES orf-X protein ORGANISM #formal_name simian immunodeficiency virus SIVcpz #note host Pan troglodytes (chimpanzee) DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jul-1999 ACCESSIONS S09989 REFERENCE S09983 !$#authors Huet, T.; Cheynier, R.; Meyerhans, A.; Roelants, G.; !1Wain-Hobson, S. !$#journal Nature (1990) 345:356-359 !$#title Genetic organization of a chimpanzee lentivirus related to !1HIV-1. !$#cross-references MUID:90259077; PMID:2188136 !$#accession S09989 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-88 ##label HUE !'##cross-references EMBL:X52154; NID:g58866; PIDN:CAA36406.1; !1PID:g58873 GENETICS !$#gene vpu CLASSIFICATION #superfamily HIV-1 vpu protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 88 #molecular-weight 10565 #checksum 2836 SEQUENCE /// ENTRY ASLJX2 #type complete TITLE vpu protein - human immunodeficiency virus type 2 (isolate ROD) ALTERNATE_NAMES orf-X protein; vpx protein ORGANISM #formal_name human immunodeficiency virus type 2, HIV-2 DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Jul-1999 ACCESSIONS I26262 REFERENCE A26262 !$#authors Guyader, M.; Emerman, M.; Sonigo, P.; Clavel, F.; !1Montagnier, L.; Alizon, M. !$#journal Nature (1987) 326:662-669 !$#title Genome organization and transactivation of the human !1immuno-deficiency virus type 2. !$#cross-references MUID:87173056; PMID:3031510 !$#accession I26262 !'##molecule_type DNA !'##residues 1-112 ##label GUY !'##cross-references GB:M15390; NID:g1332361; PIDN:AAB00766.1; !1PID:g325747 GENETICS !$#gene vpu CLASSIFICATION #superfamily AIDS vpu protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 112 #molecular-weight 12815 #checksum 8240 SEQUENCE /// ENTRY ASLJSX #type complete TITLE vpu protein - human immunodeficiency virus type 2 (isolate ST) ALTERNATE_NAMES orf-X protein; vpx protein ORGANISM #formal_name human immunodeficiency virus type 2, HIV-2 #note host Homo sapiens (man) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS D33943 REFERENCE A33943 !$#authors Kumar, P.; Hui, H.; Kappes, J.C.; Haggarty, B.S.; Hoxie, !1J.A.; Arya, S.K.; Shaw, G.M.; Hahn, B.H. !$#journal J. Virol. (1990) 64:890-901 !$#title Molecular characterization of an attenuated human !1immunodeficiency virus type 2 isolate. !$#cross-references MUID:90112662; PMID:2296086 !$#accession D33943 !'##molecule_type genomic RNA !'##residues 1-112 ##label KUM !'##cross-references GB:M31113; NID:g1339798; PIDN:AAB01354.1; !1PID:g325757 GENETICS !$#gene vpu CLASSIFICATION #superfamily AIDS vpu protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 112 #molecular-weight 12678 #checksum 7035 SEQUENCE /// ENTRY ASLJCX #type complete TITLE vpu protein - human immunodeficiency virus type 2 (isolate CAM2/Guinea-Bissau) ALTERNATE_NAMES orf-X protein; vpx protein ORGANISM #formal_name human immunodeficiency virus type 2, HIV-2 #note host Homo sapiens (man) DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jun-2000 ACCESSIONS D38475; JQ0976 REFERENCE A38475 !$#authors Tristem, M.; Hill, F.; Karpas, A. !$#journal J. Gen. Virol. (1991) 72:721-724 !$#title Nucleotide sequence of a Guinea-Bissau-derived human !1immunodeficiency virus type 2 proviral clone (HIV-2-CAM2). !$#cross-references MUID:91170959; PMID:2005437 !$#accession D38475 !'##molecule_type DNA !'##residues 1-112 ##label TRI !'##cross-references GB:D00835; NID:g3153166; PIDN:BAA00712.1; !1PID:g221470 GENETICS !$#gene vpu CLASSIFICATION #superfamily AIDS vpu protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 112 #molecular-weight 12820 #checksum 6822 SEQUENCE /// ENTRY ASLJGH #type complete TITLE vpu protein - human immunodeficiency virus type 2 (isolate GH-1) ALTERNATE_NAMES orf-X protein; vpx protein ORGANISM #formal_name human immunodeficiency virus type 2, HIV-2 #note host Homo sapiens (man) DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jul-1999 ACCESSIONS JS0330 REFERENCE JS0327 !$#authors Hasegawa, A.; Tsujimoto, H.; Maki, N.; Ishikawa, K.; Miura, !1T.; Fukasawa, M.; Miki, K.; Hayami, M. !$#journal AIDS Res. Hum. Retroviruses (1989) 5:593-604 !$#title Sequence of a distinct HIV-2 isolate from Ghana showing !1significant divergence in its genome. !$#cross-references MUID:90122350; PMID:2611042 !$#accession JS0330 !'##molecule_type DNA !'##residues 1-112 ##label HAS !'##cross-references GB:M30895; GB:D00477; NID:g325709; PIDN:AAA43935.1; !1PID:g325716 !'##note this sequence was submitted to JIPID, October 1989 GENETICS !$#gene vpu CLASSIFICATION #superfamily AIDS vpu protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 112 #molecular-weight 12819 #checksum 6780 SEQUENCE /// ENTRY ASLJST #type complete TITLE vpu protein - simian immunodeficiency virus SIVagm (type 3, isolate STLV-3agm) ALTERNATE_NAMES orf-X protein ORGANISM #formal_name simian immunodeficiency virus SIVagm DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 31-Jan-1997 ACCESSIONS D26737 REFERENCE A26739 !$#authors Hirsch, V. !$#submission submitted to GenBank, June 1987 !$#accession D26737 !'##molecule_type DNA !'##residues 1-112 ##label HIR GENETICS !$#gene vpu CLASSIFICATION #superfamily AIDS vpu protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 112 #molecular-weight 13219 #checksum 4847 SEQUENCE /// ENTRY ASLJX3 #type complete TITLE vpu protein - simian immunodeficiency virus (macaque isolate) ALTERNATE_NAMES orf-X protein ORGANISM #formal_name simian immunodeficiency virus, SIV DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jul-1999 ACCESSIONS D28887 REFERENCE A28887 !$#authors Chakrabarti, L.; Guyader, M.; Alizon, M.; Daniel, M.D.; !1Desrosiers, R.C.; Tiollais, P.; Sonigo, P. !$#journal Nature (1987) 328:543-547 !$#title Sequence of simian immunodeficiency virus from macaque and !1its relationship to other human and simian retroviruses. !$#cross-references MUID:87287230; PMID:3649576 !$#accession D28887 !'##molecule_type DNA !'##residues 1-112 ##label CHA !'##cross-references GB:Y00277; GB:M16403; NID:g61730; PIDN:CAA68382.1; !1PID:g61734 GENETICS !$#gene vpu CLASSIFICATION #superfamily AIDS vpu protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 112 #molecular-weight 12906 #checksum 4172 SEQUENCE /// ENTRY ASLJX4 #type complete TITLE vpu protein - simian immunodeficiency virus (African green monkey isolate) ALTERNATE_NAMES orf-X protein ORGANISM #formal_name simian immunodeficiency virus, SIV DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 28-Jul-2000 ACCESSIONS D30045 REFERENCE A30045 !$#authors Fukasawa, M.; Miura, T.; Hasegawa, A.; Morikawa, S.; !1Tsujimoto, H.; Miki, K.; Kitamura, T.; Hayami, M. !$#journal Nature (1988) 333:457-461 !$#title Sequence of simian immunodeficiency virus from African green !1monkey, a new member of the HIV/SIV group. !$#cross-references MUID:88232906; PMID:3374586 !$#accession D30045 !'##molecule_type DNA !'##residues 1-119 ##label FUK !'##cross-references EMBL:X07805; NID:g61748; PIDN:CAA30660.1; !1PID:g4469308 GENETICS !$#gene vpu CLASSIFICATION #superfamily AIDS vpu protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 119 #molecular-weight 14340 #checksum 3993 SEQUENCE /// ENTRY ASLJCE #type complete TITLE vpu protein - caprine arthritis-encephalitis virus ALTERNATE_NAMES orf-X protein; upx protein ORGANISM #formal_name caprine arthritis-encephalitis virus, CAEV DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 08-Apr-1994 ACCESSIONS B40479 REFERENCE A40479 !$#authors Kalinski, H.; Yaniv, A.; Mashiah, P.; Miki, T.; Tronick, !1S.R.; Gazit, A. !$#journal Virology (1991) 183:786-792 !$#title rev-like transcripts of caprine arthritis encephalitis !1virus. !$#cross-references MUID:91306466; PMID:1649509 !$#accession B40479 !'##molecule_type mRNA !'##residues 1-73 ##label KAL !'##cross-references GB:M63106 GENETICS !$#gene vpu CLASSIFICATION #superfamily caprine arthritis-encephalitis virus vpu !1protein SUMMARY #length 73 #molecular-weight 8326 #checksum 6041 SEQUENCE /// ENTRY ASMVJA #type complete TITLE vpu protein - sheep pulmonary adenomatosis virus ALTERNATE_NAMES orf-X protein; vpx protein ORGANISM #formal_name sheep pulmonary adenomatosis virus DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS D42740 REFERENCE A42740 !$#authors York, D.F.; Vigne, R.; Verwoerd, D.W.; Querat, G. !$#journal J. Virol. (1992) 66:4930-4939 !$#title Nucleotide sequence of the jaagsiekte retrovirus, an !1exogenous and endogenous type D and B retrovirus of sheep !1and goats. !$#cross-references MUID:92333675; PMID:1629959 !$#accession D42740 !'##molecule_type genomic RNA !'##residues 1-166 ##label YOR !'##cross-references GB:M80216; NID:g331338; PIDN:AAA89183.1; !1PID:g331341 GENETICS !$#gene vpu CLASSIFICATION #superfamily sheep pulmonary adenomatosis virus vpu protein SUMMARY #length 166 #molecular-weight 19356 #checksum 7638 SEQUENCE /// ENTRY ASLJBW #type complete TITLE orf-W protein - bovine immunodeficiency virus (isolate 127) ORGANISM #formal_name bovine immunodeficiency virus DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 31-Jan-1997 ACCESSIONS F34742 REFERENCE A34742 !$#authors Garvey, K.J.; Oberste, M.S.; Elser, J.E.; Braun, M.J.; !1Gonda, M.A. !$#journal Virology (1990) 175:391-409 !$#title Nucleotide sequence and genome organization of biologically !1active proviruses of the bovine immunodeficiency-like virus. !$#cross-references MUID:90223985; PMID:2183467 !$#accession F34742 !'##molecule_type genomic RNA !'##residues 1-54 ##label GAR !'##cross-references GB:M32690 GENETICS !$#gene orf-W CLASSIFICATION #superfamily AIDS orf-W protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 54 #molecular-weight 6620 #checksum 6705 SEQUENCE /// ENTRY ASLJBY #type complete TITLE orf-Y protein - bovine immunodeficiency virus (isolate 127) ORGANISM #formal_name bovine immunodeficiency virus DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 31-Jan-1997 ACCESSIONS G34742 REFERENCE A34742 !$#authors Garvey, K.J.; Oberste, M.S.; Elser, J.E.; Braun, M.J.; !1Gonda, M.A. !$#journal Virology (1990) 175:391-409 !$#title Nucleotide sequence and genome organization of biologically !1active proviruses of the bovine immunodeficiency-like virus. !$#cross-references MUID:90223985; PMID:2183467 !$#accession G34742 !'##molecule_type genomic RNA !'##residues 1-80 ##label GAR !'##cross-references GB:M32690 GENETICS !$#gene orf-Y CLASSIFICATION #superfamily AIDS orf-Y protein KEYWORDS AIDS; immunodeficiency SUMMARY #length 80 #molecular-weight 9549 #checksum 354 SEQUENCE /// ENTRY WMHUE2 #type complete TITLE HIV-EP2 enhancer-binding protein - human ALTERNATE_NAMES finger protein, 275K; human immunodeficiency virus enhancer-binding protein EP2; major histocompatibility complex-binding protein 2 ORGANISM #formal_name Homo sapiens #common_name man DATE 31-Mar-1993 #sequence_revision 07-Jul-1995 #text_change 21-Jul-2000 ACCESSIONS S26661; A39829; A38253 REFERENCE S26661 !$#authors van't Veer, L.J.; Lutz, P.M.; Isselbacher, K.J.; Bernards, !1R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:8971-8975 !$#title Structure and expression of major histocompatibility !1complex-binding protein 2, a 275-kDa zinc finger protein !1that binds to an enhancer of major histocompatibility !1complex class I genes. !$#cross-references MUID:93028387; PMID:1409593 !$#accession S26661 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-2500 ##label VAN !'##cross-references EMBL:X65644; NID:g38259; PIDN:CAA46596.1; !1PID:g38260 REFERENCE A39829 !$#authors Nomura, N.; Zhao, M.J.; Nagase, T.; Maekawa, T.; Ishizaki, !1R.; Tabata, S.; Ishii, S. !$#journal J. Biol. Chem. (1991) 266:8590-8594 !$#title HIV-EP2, a new member of the gene family encoding the human !1immunodeficiency virus type 1 enhancer-binding protein. !1Comparison with HIV-EP1/PRDII-BF1/MBP-1. !$#cross-references MUID:91217105; PMID:2022670 !$#accession A39829 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 668-2144,'R',2146-2500 ##label NOM !'##cross-references GB:M60119; NID:g2661140; PIDN:AAB88218.1; !1PID:g182120 REFERENCE A38253 !$#authors Rustgi, A.K.; Van't Veer, L.J.; Bernards, R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:8707-8710 !$#title Two genes encode factors with NF-kappaB- and H2TF1-like !1DNA-binding properties. !$#cross-references MUID:91062349; PMID:2247438 !$#accession A38253 !'##molecule_type mRNA !'##residues 1851-1990 ##label RUS !'##cross-references GB:M61744; GB:M33920; NID:g187404; PIDN:AAA36202.1; !1PID:g187405 GENETICS !$#gene GDB:HIVEP2 !'##cross-references GDB:129086; OMIM:143054 !$#map_position 6q23-6q24 CLASSIFICATION #superfamily HIV-EP2 enhancer-binding protein KEYWORDS DNA binding; duplication; metal binding; transcription !1regulation; zinc finger FEATURE !$242-298 #region DNA binding #status predicted\ !$245-265 #region zinc finger CCHH motif\ !$273-295 #region zinc finger CCHH motif\ !$991-997 #region nuclear location signal\ !$1004-1036 #region serine-rich\ !$1852-1908 #region DNA binding #status predicted\ !$1855-1875 #region zinc finger CCHH motif\ !$1883-1905 #region zinc finger CCHH motif\ !$1953-1977 #region acidic SUMMARY #length 2500 #molecular-weight 274880 #checksum 1469 SEQUENCE /// ENTRY QQIHPC #type complete TITLE 11K protein - porcine transmissible gastroenteritis virus ORGANISM #formal_name porcine transmissible gastroenteritis virus #note host Sus scrofa domestica (domestic pig) DATE 04-Dec-1986 #sequence_revision 22-Oct-1999 #text_change 22-Oct-1999 ACCESSIONS S03937; A04019 REFERENCE S01738 !$#authors Rasschaert, D.; Gelfi, J.; Laude, H. !$#journal Biochimie (1987) 69:591-600 !$#title Enteric coronavirus TGEV: partial sequence of the genomic !1RNA, its organization and expression. !$#cross-references MUID:88078100; PMID:2825819 !$#accession S03937 !'##molecule_type mRNA !'##residues 1-78 ##label RAS !'##cross-references EMBL:X06371; NID:g58995; PIDN:CAA29675.1; !1PID:g59002 !'##experimental_source strain Purdue-115 REFERENCE A94340 !$#authors Kapke, P.A.; Brian, D.A. !$#journal Virology (1986) 151:41-49 !$#title Sequence analysis of the porcine transmissible !1gastroenteritis coronavirus nucleocapsid protein gene. !$#cross-references MUID:86181608; PMID:3008432 !$#accession A04019 !'##molecule_type genomic RNA !'##residues 1-29,'D',31-77,'V' ##label KAP !'##cross-references GB:M14878; NID:g335209; PIDN:AAA47916.1; !1PID:g335212 !'##experimental_source strain Purdue CLASSIFICATION #superfamily feline infectious peritonitis virus 11K protein SUMMARY #length 78 #molecular-weight 9130 #checksum 5901 SEQUENCE /// ENTRY S24283 #type complete TITLE 9K protein - porcine respiratory virus (strain 86/137004) ALTERNATE_NAMES NS7 protein ORGANISM #formal_name porcine respiratory virus #variety strain 86/137004 DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jul-1999 ACCESSIONS S24283; F36607 REFERENCE S24279 !$#authors Britton, P.; Mawditt, K.L.; Page, K.W. !$#journal Virus Res. (1991) 21:181-198 !$#title The cloning and sequencing of the virion protein genes from !1a British isolate of porcine respiratory coronavirus: !1comparison with transmissible gastroenteritis virus genes. !$#cross-references MUID:92116634; PMID:1662846 !$#accession S24283 !'##molecule_type genomic RNA !'##residues 1-78 ##label BRI !'##cross-references EMBL:X60056; NID:g61342; PIDN:CAA42658.1; !1PID:g61347 !'##experimental_source strain 86/137004 REFERENCE A36607 !$#authors Rasschaert, D.; Duarte, M.; Laude, H. !$#journal J. Gen. Virol. (1990) 71:2599-2607 !$#title Porcine respiratory coronavirus differs from transmissible !1gastroenteritis virus by a few genomic deletions. !$#cross-references MUID:91073120; PMID:2174956 !$#accession F36607 !'##status preliminary !'##molecule_type genomic RNA !'##residues 1-78 ##label RAS !'##cross-references GB:Z24675; NID:g395057; PIDN:CAA80842.1; !1PID:g395063 !'##experimental_source strain RM4 CLASSIFICATION #superfamily feline infectious peritonitis virus 11K protein SUMMARY #length 78 #molecular-weight 9058 #checksum 5477 SEQUENCE /// ENTRY WMIHFI #type complete TITLE 11K protein - feline infectious peritonitis virus (strain 79-1146) ORGANISM #formal_name feline infectious peritonitis virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS A31825 REFERENCE A31825 !$#authors De Groot, R.J.; Andeweg, A.C.; Horzinek, M.C.; Spaan, W.J.M. !$#journal Virology (1988) 167:370-376 !$#title Sequence analysis of the 3' end of the feline coronavirus !1FIPV 79-1146 genome: comparison with the genome of porcine !1coronavirus TGEV reveals large insertions. !$#cross-references MUID:89073738; PMID:3201747 !$#accession A31825 !'##molecule_type genomic RNA !'##residues 1-101 ##label DEG !'##cross-references GB:M23694; NID:g323930; PIDN:AAA43063.1; !1PID:g323931 CLASSIFICATION #superfamily feline infectious peritonitis virus 11K protein SUMMARY #length 101 #molecular-weight 11232 #checksum 4626 SEQUENCE /// ENTRY D44056 #type complete TITLE 11K protein - feline enteric coronavirus (strain 79-1683) ALTERNATE_NAMES 6a protein ORGANISM #formal_name feline enteric coronavirus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jul-1999 ACCESSIONS D44056 REFERENCE A44056 !$#authors Vennema, H.; Rossen, J.W.A.; Wesseling, J.; Horzinek, M.C.; !1Rottier, P.J.M. !$#journal Virology (1992) 191:134-140 !$#title Genomic organization and expression of the 3' end of the !1canine and feline enteric coronaviruses. !$#cross-references MUID:93033103; PMID:1329312 !$#accession D44056 !'##molecule_type genomic RNA !'##residues 1-101 ##label VEN !'##cross-references GB:X66718; NID:g297773; PIDN:CAA47249.1; !1PID:g297774 CLASSIFICATION #superfamily feline infectious peritonitis virus 11K protein SUMMARY #length 101 #molecular-weight 11246 #checksum 4576 SEQUENCE /// ENTRY B44056 #type complete TITLE 11K protein - canine coronavirus (strain K378) ALTERNATE_NAMES 6a protein ORGANISM #formal_name canine coronavirus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jul-1999 ACCESSIONS B44056 REFERENCE A44056 !$#authors Vennema, H.; Rossen, J.W.A.; Wesseling, J.; Horzinek, M.C.; !1Rottier, P.J.M. !$#journal Virology (1992) 191:134-140 !$#title Genomic organization and expression of the 3' end of the !1canine and feline enteric coronaviruses. !$#cross-references MUID:93033103; PMID:1329312 !$#accession B44056 !'##molecule_type genomic RNA !'##residues 1-101 ##label VEN !'##cross-references GB:X66717; NID:g58849; PIDN:CAA47247.1; PID:g58851 CLASSIFICATION #superfamily feline infectious peritonitis virus 11K protein SUMMARY #length 101 #molecular-weight 11491 #checksum 4286 SEQUENCE /// ENTRY JQ1726 #type complete TITLE 11K protein - canine coronavirus (strain Insavc-1) ALTERNATE_NAMES 7a protein ORGANISM #formal_name canine coronavirus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 07-May-1999 ACCESSIONS JQ1726 REFERENCE PQ0481 !$#authors Horsburgh, B.C.; Brierley, I.; Brown, T.D.K. !$#journal J. Gen. Virol. (1992) 73:2849-2862 !$#title Analysis of a 9.6 kb sequence from the 3' end of canine !1coronavirus genomic RNA. !$#cross-references MUID:93057357; PMID:1431811 !$#accession JQ1726 !'##molecule_type genomic RNA !'##residues 1-101 ##label HOR !'##cross-references DDBJ:D13096 CLASSIFICATION #superfamily feline infectious peritonitis virus 11K protein SUMMARY #length 101 #molecular-weight 11547 #checksum 4338 SEQUENCE /// ENTRY QQIHFI #type complete TITLE 22K protein - feline infectious peritonitis virus (strain 79-1146) ORGANISM #formal_name feline infectious peritonitis virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS B31825 REFERENCE A31825 !$#authors De Groot, R.J.; Andeweg, A.C.; Horzinek, M.C.; Spaan, W.J.M. !$#journal Virology (1988) 167:370-376 !$#title Sequence analysis of the 3' end of the feline coronavirus !1FIPV 79-1146 genome: comparison with the genome of porcine !1coronavirus TGEV reveals large insertions. !$#cross-references MUID:89073738; PMID:3201747 !$#accession B31825 !'##molecule_type genomic RNA !'##residues 1-206 ##label DEG !'##cross-references GB:M23694; NID:g323930; PIDN:AAA43064.1; !1PID:g323932 CLASSIFICATION #superfamily feline infectious peritonitis virus 22K protein SUMMARY #length 206 #molecular-weight 24007 #checksum 8293 SEQUENCE /// ENTRY C44056 #type complete TITLE 22K protein - canine coronavirus (strain K378) ALTERNATE_NAMES 6b protein ORGANISM #formal_name canine coronavirus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jul-1999 ACCESSIONS C44056 REFERENCE A44056 !$#authors Vennema, H.; Rossen, J.W.A.; Wesseling, J.; Horzinek, M.C.; !1Rottier, P.J.M. !$#journal Virology (1992) 191:134-140 !$#title Genomic organization and expression of the 3' end of the !1canine and feline enteric coronaviruses. !$#cross-references MUID:93033103; PMID:1329312 !$#accession C44056 !'##molecule_type genomic RNA !'##residues 1-213 ##label VEN !'##cross-references GB:X66717; NID:g58849; PIDN:CAA47248.1; PID:g58852 CLASSIFICATION #superfamily feline infectious peritonitis virus 22K protein SUMMARY #length 213 #molecular-weight 24982 #checksum 9358 SEQUENCE /// ENTRY JQ1727 #type complete TITLE 22K protein - canine coronavirus (strain Insavc-1) ALTERNATE_NAMES 7b protein ORGANISM #formal_name canine coronavirus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jun-2000 ACCESSIONS JQ1727 REFERENCE PQ0481 !$#authors Horsburgh, B.C.; Brierley, I.; Brown, T.D.K. !$#journal J. Gen. Virol. (1992) 73:2849-2862 !$#title Analysis of a 9.6 kb sequence from the 3' end of canine !1coronavirus genomic RNA. !$#cross-references MUID:93057357; PMID:1431811 !$#accession JQ1727 !'##molecule_type genomic RNA !'##residues 1-213 ##label HOR !'##cross-references DDBJ:D13096; NID:g406193; PIDN:BAA02416.1; !1PID:g406203 CLASSIFICATION #superfamily feline infectious peritonitis virus 22K protein SUMMARY #length 213 #molecular-weight 24928 #checksum 9184 SEQUENCE /// ENTRY E44056 #type complete TITLE 22K protein - feline enteric coronavirus (strain 79-1683) ALTERNATE_NAMES 6b protein ORGANISM #formal_name feline enteric coronavirus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jul-1999 ACCESSIONS E44056 REFERENCE A44056 !$#authors Vennema, H.; Rossen, J.W.A.; Wesseling, J.; Horzinek, M.C.; !1Rottier, P.J.M. !$#journal Virology (1992) 191:134-140 !$#title Genomic organization and expression of the 3' end of the !1canine and feline enteric coronaviruses. !$#cross-references MUID:93033103; PMID:1329312 !$#accession E44056 !'##molecule_type genomic RNA !'##residues 1-176 ##label VEN !'##cross-references GB:X66718; NID:g297773; PIDN:CAA47250.1; !1PID:g297775 CLASSIFICATION #superfamily feline infectious peritonitis virus 22K protein SUMMARY #length 176 #molecular-weight 20209 #checksum 4452 SEQUENCE /// ENTRY QQIHI1 #type complete TITLE 3c protein - avian infectious bronchitis virus (strain KB8523) ORGANISM #formal_name avian infectious bronchitis virus, IBV DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS E29249 REFERENCE A29249 !$#authors Sutou, S.; Sato, S.; Okabe, T.; Nakai, M.; Sasaki, N. !$#journal Virology (1988) 165:589-595 !$#title Cloning and sequencing of genes encoding structural proteins !1of avian infectious bronchitis virus. !$#cross-references MUID:88306251; PMID:2841803 !$#accession E29249 !'##molecule_type genomic RNA !'##residues 1-109 ##label SUT !'##cross-references GB:M21515; NID:g808698; PIDN:AAA66580.1; !1PID:g808700 COMMENT This protein may be involved in viral replication. CLASSIFICATION #superfamily avian infectious bronchitis virus 3c protein KEYWORDS replication SUMMARY #length 109 #molecular-weight 12300 #checksum 3614 SEQUENCE /// ENTRY WMIHB3 #type complete TITLE 3c protein - avian infectious bronchitis virus ORGANISM #formal_name avian infectious bronchitis virus, IBV DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 29-Oct-1999 ACCESSIONS C41038; C23771 REFERENCE A41038 !$#authors Liu, D.X.; Cavanagh, D.; Green, P.; Inglis, S.C. !$#journal Virology (1991) 184:531-544 !$#title A polycistronic mRNA specified by the coronavirus infectious !1bronchitis virus. !$#cross-references MUID:91361544; PMID:1653486 !$#accession C41038 !'##molecule_type genomic RNA !'##residues 1-109 ##label LIU !'##cross-references GB:X59819 !'##experimental_source strain Beaudette REFERENCE A93618 !$#authors Niesters, H.G.M.; Zijderveld, A.J.; Seifert, W.F.; Lenstra, !1J.A.; Bleumink-Pluym, N.M.C.; Horzinek, M.C.; van der !1Zeijst, B.A.M. !$#journal Nucleic Acids Res. (1986) 14:3144 !$#title Infectious bronchitis virus RNA D encodes three potential !1translation products. !$#cross-references MUID:86176792; PMID:3960740 !$#accession C23771 !'##molecule_type mRNA !'##residues 1-21,'F',23-101,'V',103-109 ##label NIE !'##cross-references GB:X03723; NID:g58944; PIDN:CAA27360.1; PID:g58947 !'##experimental_source vaccine strain M41 COMMENT This protein may be involved in viral replication. CLASSIFICATION #superfamily avian infectious bronchitis virus 3c protein KEYWORDS replication SUMMARY #length 109 #molecular-weight 12379 #checksum 1046 SEQUENCE /// ENTRY WMIHB6 #type complete TITLE 3c protein - avian infectious bronchitis virus (strain USA/ M41/41) ORGANISM #formal_name avian infectious bronchitis virus, IBV DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 08-Apr-1994 ACCESSIONS F41038 REFERENCE A41038 !$#authors Liu, D.X.; Cavanagh, D.; Green, P.; Inglis, S.C. !$#journal Virology (1991) 184:531-544 !$#title A polycistronic mRNA specified by the coronavirus infectious !1bronchitis virus. !$#cross-references MUID:91361544; PMID:1653486 !$#accession F41038 !'##molecule_type genomic RNA !'##residues 1-109 ##label LIU !'##cross-references GB:X59819 COMMENT This protein may be involved in viral replication. CLASSIFICATION #superfamily avian infectious bronchitis virus 3c protein KEYWORDS replication SUMMARY #length 109 #molecular-weight 12421 #checksum 1761 SEQUENCE /// ENTRY WMIHB9 #type complete TITLE 3c protein - avian infectious bronchitis virus (strain Portugal/322/82) ORGANISM #formal_name avian infectious bronchitis virus, IBV DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 08-Apr-1994 ACCESSIONS I41038 REFERENCE A41038 !$#authors Liu, D.X.; Cavanagh, D.; Green, P.; Inglis, S.C. !$#journal Virology (1991) 184:531-544 !$#title A polycistronic mRNA specified by the coronavirus infectious !1bronchitis virus. !$#cross-references MUID:91361544; PMID:1653486 !$#accession I41038 !'##molecule_type genomic RNA !'##residues 1-93 ##label LIU !'##cross-references GB:X59819 COMMENT This protein may be involved in viral replication. CLASSIFICATION #superfamily avian infectious bronchitis virus 3c protein KEYWORDS replication SUMMARY #length 93 #molecular-weight 10542 #checksum 7959 SEQUENCE /// ENTRY WMIH23 #type complete TITLE 3c protein - avian infectious bronchitis virus (strain UK/ 68/84) ORGANISM #formal_name avian infectious bronchitis virus, IBV DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 08-Apr-1994 ACCESSIONS C36816 REFERENCE A41038 !$#authors Liu, D.X.; Cavanagh, D.; Green, P.; Inglis, S.C. !$#journal Virology (1991) 184:531-544 !$#title A polycistronic mRNA specified by the coronavirus infectious !1bronchitis virus. !$#cross-references MUID:91361544; PMID:1653486 !$#accession C36816 !'##molecule_type genomic RNA !'##residues 1-106 ##label LIU !'##cross-references GB:X59820 COMMENT This protein may be involved in viral replication. CLASSIFICATION #superfamily avian infectious bronchitis virus 3c protein KEYWORDS replication SUMMARY #length 106 #molecular-weight 11882 #checksum 9572 SEQUENCE /// ENTRY WMIH26 #type complete TITLE 3c protein - avian infectious bronchitis virus (strain UK/ 183/66) ORGANISM #formal_name avian infectious bronchitis virus, IBV DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 08-Apr-1994 ACCESSIONS F36816 REFERENCE A41038 !$#authors Liu, D.X.; Cavanagh, D.; Green, P.; Inglis, S.C. !$#journal Virology (1991) 184:531-544 !$#title A polycistronic mRNA specified by the coronavirus infectious !1bronchitis virus. !$#cross-references MUID:91361544; PMID:1653486 !$#accession F36816 !'##molecule_type genomic RNA !'##residues 1-107 ##label LIU !'##cross-references GB:X59820 COMMENT This protein may be involved in viral replication. CLASSIFICATION #superfamily avian infectious bronchitis virus 3c protein KEYWORDS replication SUMMARY #length 107 #molecular-weight 12017 #checksum 3394 SEQUENCE /// ENTRY QQIHI2 #type complete TITLE hypothetical protein ORF2 - avian infectious bronchitis virus (strain KB8523) ORGANISM #formal_name avian infectious bronchitis virus, IBV DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 10-Sep-1999 ACCESSIONS F29249 REFERENCE A29249 !$#authors Sutou, S.; Sato, S.; Okabe, T.; Nakai, M.; Sasaki, N. !$#journal Virology (1988) 165:589-595 !$#title Cloning and sequencing of genes encoding structural proteins !1of avian infectious bronchitis virus. !$#cross-references MUID:88306251; PMID:2841803 !$#accession F29249 !'##molecule_type genomic RNA !'##residues 1-82 ##label SUT !'##cross-references GB:M21515; NID:g808698; PIDN:AAA66582.1; !1PID:g808701 CLASSIFICATION #superfamily avian infectious bronchitis virus hypothetical !1protein 2 SUMMARY #length 82 #molecular-weight 9392 #checksum 9289 SEQUENCE /// ENTRY WMIHB1 #type complete TITLE 3a protein - avian infectious bronchitis virus (strain Beaudette) ORGANISM #formal_name avian infectious bronchitis virus, IBV DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 08-Apr-1994 ACCESSIONS A41038 REFERENCE A41038 !$#authors Liu, D.X.; Cavanagh, D.; Green, P.; Inglis, S.C. !$#journal Virology (1991) 184:531-544 !$#title A polycistronic mRNA specified by the coronavirus infectious !1bronchitis virus. !$#cross-references MUID:91361544; PMID:1653486 !$#accession A41038 !'##molecule_type genomic RNA !'##residues 1-57 ##label LIU !'##cross-references GB:X59819 CLASSIFICATION #superfamily avian infectious bronchitis virus 3a protein SUMMARY #length 57 #molecular-weight 6668 #checksum 7863 SEQUENCE /// ENTRY WMIHB4 #type complete TITLE 3a protein - avian infectious bronchitis virus (strain USA/ M41/41) ORGANISM #formal_name avian infectious bronchitis virus, IBV DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 08-Apr-1994 ACCESSIONS D41038 REFERENCE A41038 !$#authors Liu, D.X.; Cavanagh, D.; Green, P.; Inglis, S.C. !$#journal Virology (1991) 184:531-544 !$#title A polycistronic mRNA specified by the coronavirus infectious !1bronchitis virus. !$#cross-references MUID:91361544; PMID:1653486 !$#accession D41038 !'##molecule_type genomic RNA !'##residues 1-57 ##label LIU !'##cross-references GB:X59819 CLASSIFICATION #superfamily avian infectious bronchitis virus 3a protein SUMMARY #length 57 #molecular-weight 6592 #checksum 6827 SEQUENCE /// ENTRY WMIHB7 #type complete TITLE 3a protein - avian infectious bronchitis virus (strain Portugal/322/82) ORGANISM #formal_name avian infectious bronchitis virus, IBV DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 08-Apr-1994 ACCESSIONS G41038 REFERENCE A41038 !$#authors Liu, D.X.; Cavanagh, D.; Green, P.; Inglis, S.C. !$#journal Virology (1991) 184:531-544 !$#title A polycistronic mRNA specified by the coronavirus infectious !1bronchitis virus. !$#cross-references MUID:91361544; PMID:1653486 !$#accession G41038 !'##molecule_type genomic RNA !'##residues 1-57 ##label LIU !'##cross-references GB:X59819 CLASSIFICATION #superfamily avian infectious bronchitis virus 3a protein SUMMARY #length 57 #molecular-weight 6588 #checksum 7223 SEQUENCE /// ENTRY WMIH21 #type complete TITLE 3a protein - avian infectious bronchitis virus (strain UK/ 68/84) ORGANISM #formal_name avian infectious bronchitis virus, IBV DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 08-Apr-1994 ACCESSIONS A36816 REFERENCE A41038 !$#authors Liu, D.X.; Cavanagh, D.; Green, P.; Inglis, S.C. !$#journal Virology (1991) 184:531-544 !$#title A polycistronic mRNA specified by the coronavirus infectious !1bronchitis virus. !$#cross-references MUID:91361544; PMID:1653486 !$#accession A36816 !'##molecule_type genomic RNA !'##residues 1-57 ##label LIU !'##cross-references GB:X59820 CLASSIFICATION #superfamily avian infectious bronchitis virus 3a protein SUMMARY #length 57 #molecular-weight 6600 #checksum 8132 SEQUENCE /// ENTRY WMIH24 #type complete TITLE 3a protein - avian infectious bronchitis virus (strain UK/ 183/66) ORGANISM #formal_name avian infectious bronchitis virus, IBV DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 08-Apr-1994 ACCESSIONS D36816 REFERENCE A41038 !$#authors Liu, D.X.; Cavanagh, D.; Green, P.; Inglis, S.C. !$#journal Virology (1991) 184:531-544 !$#title A polycistronic mRNA specified by the coronavirus infectious !1bronchitis virus. !$#cross-references MUID:91361544; PMID:1653486 !$#accession D36816 !'##molecule_type genomic RNA !'##residues 1-57 ##label LIU !'##cross-references GB:X59820 CLASSIFICATION #superfamily avian infectious bronchitis virus 3a protein SUMMARY #length 57 #molecular-weight 6622 #checksum 7751 SEQUENCE /// ENTRY WMIHB2 #type complete TITLE 3b protein - avian infectious bronchitis virus (strain Beaudette) ORGANISM #formal_name avian infectious bronchitis virus, IBV DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 08-Apr-1994 ACCESSIONS B41038 REFERENCE A41038 !$#authors Liu, D.X.; Cavanagh, D.; Green, P.; Inglis, S.C. !$#journal Virology (1991) 184:531-544 !$#title A polycistronic mRNA specified by the coronavirus infectious !1bronchitis virus. !$#cross-references MUID:91361544; PMID:1653486 !$#accession B41038 !'##molecule_type genomic RNA !'##residues 1-64 ##label LIU !'##cross-references GB:X59819 CLASSIFICATION #superfamily avian infectious bronchitis virus 3b protein SUMMARY #length 64 #molecular-weight 7442 #checksum 7203 SEQUENCE /// ENTRY WMIHB5 #type complete TITLE 3b protein - avian infectious bronchitis virus ORGANISM #formal_name avian infectious bronchitis virus, IBV DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS E41038; B23771 REFERENCE A41038 !$#authors Liu, D.X.; Cavanagh, D.; Green, P.; Inglis, S.C. !$#journal Virology (1991) 184:531-544 !$#title A polycistronic mRNA specified by the coronavirus infectious !1bronchitis virus. !$#cross-references MUID:91361544; PMID:1653486 !$#accession E41038 !'##molecule_type genomic RNA !'##residues 1-64 ##label LIU !'##cross-references GB:X59819 !'##experimental_source strain USA/M41/41 REFERENCE A93618 !$#authors Niesters, H.G.M.; Zijderveld, A.J.; Seifert, W.F.; Lenstra, !1J.A.; Bleumink-Pluym, N.M.C.; Horzinek, M.C.; van der !1Zeijst, B.A.M. !$#journal Nucleic Acids Res. (1986) 14:3144 !$#title Infectious bronchitis virus RNA D encodes three potential !1translation products. !$#cross-references MUID:86176792; PMID:3960740 !$#accession B23771 !'##molecule_type mRNA !'##residues 1-64 ##label NIE !'##cross-references GB:X03723; NID:g58944; PIDN:CAA27359.1; PID:g58946 !'##experimental_source vaccine strain M41 CLASSIFICATION #superfamily avian infectious bronchitis virus 3b protein SUMMARY #length 64 #molecular-weight 7414 #checksum 7077 SEQUENCE /// ENTRY WMIHB8 #type complete TITLE 3b protein - avian infectious bronchitis virus (strain Portugal/322/82) ORGANISM #formal_name avian infectious bronchitis virus, IBV DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 08-Apr-1994 ACCESSIONS H41038 REFERENCE A41038 !$#authors Liu, D.X.; Cavanagh, D.; Green, P.; Inglis, S.C. !$#journal Virology (1991) 184:531-544 !$#title A polycistronic mRNA specified by the coronavirus infectious !1bronchitis virus. !$#cross-references MUID:91361544; PMID:1653486 !$#accession H41038 !'##molecule_type genomic RNA !'##residues 1-64 ##label LIU !'##cross-references GB:X59819 CLASSIFICATION #superfamily avian infectious bronchitis virus 3b protein SUMMARY #length 64 #molecular-weight 7323 #checksum 7898 SEQUENCE /// ENTRY WMIH22 #type complete TITLE 3b protein - avian infectious bronchitis virus (strain UK/ 68/84) ORGANISM #formal_name avian infectious bronchitis virus, IBV DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 08-Apr-1994 ACCESSIONS B36816 REFERENCE A41038 !$#authors Liu, D.X.; Cavanagh, D.; Green, P.; Inglis, S.C. !$#journal Virology (1991) 184:531-544 !$#title A polycistronic mRNA specified by the coronavirus infectious !1bronchitis virus. !$#cross-references MUID:91361544; PMID:1653486 !$#accession B36816 !'##molecule_type genomic RNA !'##residues 1-64 ##label LIU !'##cross-references GB:X59820 CLASSIFICATION #superfamily avian infectious bronchitis virus 3b protein SUMMARY #length 64 #molecular-weight 7438 #checksum 7320 SEQUENCE /// ENTRY WMIH25 #type complete TITLE 3b protein - avian infectious bronchitis virus (strain UK/ 183/66) ORGANISM #formal_name avian infectious bronchitis virus, IBV DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 08-Apr-1994 ACCESSIONS E36816 REFERENCE A41038 !$#authors Liu, D.X.; Cavanagh, D.; Green, P.; Inglis, S.C. !$#journal Virology (1991) 184:531-544 !$#title A polycistronic mRNA specified by the coronavirus infectious !1bronchitis virus. !$#cross-references MUID:91361544; PMID:1653486 !$#accession E36816 !'##molecule_type genomic RNA !'##residues 1-64 ##label LIU !'##cross-references GB:X59820 CLASSIFICATION #superfamily avian infectious bronchitis virus 3b protein SUMMARY #length 64 #molecular-weight 7331 #checksum 6954 SEQUENCE /// ENTRY VFIHB1 #type complete TITLE F1 protein - avian infectious bronchitis virus (strain Beaudette) ORGANISM #formal_name avian infectious bronchitis virus, IBV DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS A33094 REFERENCE A33094 !$#authors Boursnell, M.E.G.; Brown, T.D.K.; Foulds, I.J.; Green, P.F.; !1Tomley, F.M.; Binns, M.M. !$#journal J. Gen. Virol. (1987) 68:57-77 !$#title Completion of the sequence of the genome of the coronavirus !1avian infectious bronchitis virus. !$#cross-references MUID:87111468; PMID:3027249 !$#accession A33094 !'##molecule_type genomic RNA !'##residues 1-3951 ##label BOU !'##cross-references GB:M94356; GB:M29496; NID:g331170; PIDN:AAA46223.1; !1PID:g331172 CLASSIFICATION #superfamily avian infectious bronchitis virus F1 protein SUMMARY #length 3951 #molecular-weight 441122 #checksum 7210 SEQUENCE /// ENTRY MMWVEV #type complete TITLE membrane protein - equine arteritis virus ORGANISM #formal_name equine arteritis virus #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS G39925 REFERENCE A39925 !$#authors Den Boon, J.A.; Snijder, E.J.; Chirnside, E.D.; De Vries, !1A.A.F.; Horzinek, M.C.; Spaan, W.J.M. !$#journal J. Virol. (1991) 65:2910-2920 !$#title Equine arteritis virus is not a togavirus but belongs to the !1coronaviruslike superfamily. !$#cross-references MUID:91237805; PMID:1851863 !$#accession G39925 !'##molecule_type genomic RNA !'##residues 1-162 ##label DEN !'##cross-references EMBL:X53459; NID:g62065; PIDN:CAA37545.1; !1PID:g62072 CLASSIFICATION #superfamily equine arteritis virus membrane protein KEYWORDS transmembrane protein FEATURE !$26-42 #domain transmembrane #status predicted #label TM1\ !$44-60 #domain transmembrane #status predicted #label TM2\ !$64-81 #domain transmembrane #status predicted #label TM3 SUMMARY #length 162 #molecular-weight 17744 #checksum 7097 SEQUENCE /// ENTRY VMWJBV #type complete TITLE envelope protein E - Berne virus ORGANISM #formal_name Berne virus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS A39989; S15570 REFERENCE A39989 !$#authors Den Boon, J.A.; Snijder, E.J.; Locker, J.K.; Horzinek, M.C.; !1Rottier, P.J.M. !$#journal Virology (1991) 182:655-663 !$#title Another triple-spanning envelope protein among !1intracellularly budding RNA viruses: the torovirus E !1protein. !$#cross-references MUID:91220715; PMID:2024492 !$#accession A39989 !'##molecule_type genomic RNA !'##residues 1-233 ##label DEN !'##cross-references GB:X52505; NID:g58768; PIDN:CAA36747.1; PID:g58769 REFERENCE S15570 !$#authors Boon den, J.A.; Snijder, E.J.; Horzinek, M.C.; Rottier, !1P.J.M. !$#submission submitted to the EMBL Data Library, February 1990 !$#accession S15570 !'##status preliminary !'##molecule_type mRNA !'##residues 1-233 ##label BOO !'##cross-references EMBL:X52505; NID:g58768; PIDN:CAA36747.1; !1PID:g58769 CLASSIFICATION #superfamily Berne virus envelope protein E KEYWORDS envelope protein SUMMARY #length 233 #molecular-weight 26548 #checksum 8949 SEQUENCE /// ENTRY VGIHE1 #type complete TITLE E1 membrane glycoprotein - murine hepatitis virus (strain A59) ALTERNATE_NAMES matrix glycoprotein ORGANISM #formal_name murine hepatitis virus, MHV DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 24-Sep-1999 ACCESSIONS A04020 REFERENCE A04020 !$#authors Armstrong, J.; Niemann, H.; Smeekens, S.; Rottier, P.; !1Warren, G. !$#journal Nature (1984) 308:751-752 !$#title Sequence and topology of a model intracellular membrane !1protein, E1 glycoprotein, from a coronavirus. !$#cross-references MUID:84191468; PMID:6325918 !$#accession A04020 !'##molecule_type genomic RNA !'##residues 1-228 ##label ARM !'##cross-references GB:X00509; GB:J02252; NID:g58965; PIDN:CAA25197.1; !1PID:g58966 CLASSIFICATION #superfamily coronavirus E1 membrane glycoprotein KEYWORDS glycoprotein; transmembrane protein FEATURE !$30-45 #domain transmembrane #status predicted #label TM1\ !$51-73 #domain transmembrane #status predicted #label TM2\ !$82-103 #domain transmembrane #status predicted #label TM3\ !$2,3 #binding_site carbohydrate (Ser) (covalent) #status !8predicted\ !$4,5 #binding_site carbohydrate (Thr) (covalent) #status !8predicted\ !$27 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 228 #molecular-weight 26027 #checksum 2383 SEQUENCE /// ENTRY VGIHJH #type complete TITLE E1 membrane glycoprotein - murine hepatitis virus (strain JHM) ALTERNATE_NAMES matrix glycoprotein ORGANISM #formal_name murine hepatitis virus, MHV DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jul-1999 ACCESSIONS A25304 REFERENCE A25304 !$#authors Pfleiderer, M.; Skinner, M.A.; Siddell, S.G. !$#journal Nucleic Acids Res. (1986) 14:6338 !$#title Coronavirus MHV-JHM: nucleotide sequence of the mRNA that !1encodes the membrane protein. !$#cross-references MUID:86312899; PMID:3748812 !$#accession A25304 !'##molecule_type mRNA !'##residues 1-228 ##label PFL !'##cross-references GB:X04223; NID:g58968; PIDN:CAA27802.1; PID:g58969 CLASSIFICATION #superfamily coronavirus E1 membrane glycoprotein KEYWORDS glycoprotein; matrix protein; transmembrane protein FEATURE !$30-45 #domain transmembrane #status predicted #label TM1\ !$51-73 #domain transmembrane #status predicted #label TM2\ !$82-103 #domain transmembrane #status predicted #label TM3\ !$2,3 #binding_site carbohydrate (Ser) (covalent) #status !8predicted\ !$4,5 #binding_site carbohydrate (Thr) (covalent) #status !8predicted\ !$27 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 228 #molecular-weight 26051 #checksum 3872 SEQUENCE /// ENTRY VGIHBC #type complete TITLE E1 membrane glycoprotein - bovine coronavirus ALTERNATE_NAMES matrix glycoprotein ORGANISM #formal_name bovine coronavirus DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 16-Jul-1999 ACCESSIONS A26347; A60378 REFERENCE A94357 !$#authors Lapps, W.; Hogue, B.G.; Brian, D.A. !$#journal Virology (1987) 157:47-57 !$#title Sequence analysis of the bovine coronavirus nucleocapsid and !1matrix protein genes. !$#cross-references MUID:87151119; PMID:3029965 !$#accession A26347 !'##molecule_type genomic RNA !'##residues 1-230 ##label LAP !'##cross-references GB:M16620; NID:g323354; PIDN:AAA66396.1; !1PID:g807591 !'##experimental_source strain Mebus REFERENCE A60378 !$#authors Savoysky, E.; Boireau, P.; Finance, C.; Laporte, J. !$#journal Res. Virol. (1990) 141:411-425 !$#title Sequence and analysis of BECV F15 matrix protein. !$#cross-references MUID:91180461; PMID:1706882 !$#accession A60378 !'##molecule_type mRNA !'##residues 1-230 ##label SAV !'##experimental_source strain F15 GENETICS !$#gene M CLASSIFICATION #superfamily coronavirus E1 membrane glycoprotein KEYWORDS glycoprotein; matrix protein; transmembrane protein FEATURE !$27-42 #domain transmembrane #status predicted #label TM1\ !$56-72 #domain transmembrane #status predicted #label TM2\ !$83-102 #domain transmembrane #status predicted #label TM3\ !$2,3,28 #binding_site carbohydrate (Ser) (covalent) #status !8experimental\ !$5,6,14 #binding_site carbohydrate (Thr) (covalent) #status !8experimental\ !$26 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 230 #molecular-weight 26372 #checksum 3799 SEQUENCE /// ENTRY JQ1749 #type complete TITLE E1 membrane glycoprotein - human coronavirus (strain OC43) ALTERNATE_NAMES matrix glycoprotein ORGANISM #formal_name human coronavirus #note host Homo sapiens (man) DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS JQ1749 REFERENCE JQ1749 !$#authors Mounir, S.; Talbot, P.J. !$#journal J. Gen. Virol. (1992) 73:2731-2736 !$#title Sequence analysis of the membrane protein gene of human !1coronavirus OC43 and evidence for O-glycosylation. !$#cross-references MUID:93019031; PMID:1402806 !$#accession JQ1749 !'##molecule_type genomic RNA !'##residues 1-230 ##label MOU !'##cross-references GB:M93390; NID:g329574; PIDN:AAA45462.1; !1PID:g329575 GENETICS !$#gene M CLASSIFICATION #superfamily coronavirus E1 membrane glycoprotein KEYWORDS glycoprotein; matrix protein; transmembrane protein FEATURE !$29-43 #domain transmembrane #status predicted #label TM1\ !$56-72 #domain transmembrane #status predicted #label TM2\ !$83-99 #domain transmembrane #status predicted #label TM3\ !$2,3,28 #binding_site carbohydrate (Ser) (covalent) #status !8experimental\ !$5,6,14 #binding_site carbohydrate (Thr) (covalent) #status !8experimental\ !$26 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 230 #molecular-weight 26418 #checksum 2598 SEQUENCE /// ENTRY VGIHPC #type complete TITLE E1 membrane glycoprotein precursor - porcine transmissible gastroenteritis virus (strain Purdue-115) ALTERNATE_NAMES matrix glycoprotein ORGANISM #formal_name porcine transmissible gastroenteritis virus DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 16-Jul-1999 ACCESSIONS A26961; A43565; S03935 REFERENCE A26961 !$#authors Laude, H.; Rasschaert, D.; Huet, J.C. !$#journal J. Gen. Virol. (1987) 68:1687-1693 !$#title Sequence and N-terminal processing of the transmembrane !1protein E1 of the coronavirus transmissible gastroenteritis !1virus. !$#cross-references MUID:87224815; PMID:3035066 !$#accession A26961 !'##molecule_type genomic RNA !'##residues 1-262 ##label LAU !'##cross-references GB:X05598; NID:g59003; PIDN:CAA29091.1; PID:g732631 REFERENCE A43565 !$#authors Kapke, P.A.; Tung, F.Y.; Brian, D.A.; Woods, R.D.; Wesley, !1R. !$#journal Adv. Exp. Med. Biol. (1987) 218:117-122 !$#title Nucleotide sequence of the porcine transmissible !1gastroenteritis coronovirus matrix protein gene. !$#cross-references MUID:88130167; PMID:2829520 !$#accession A43565 !'##molecule_type genomic RNA !'##residues 1-79,'A',81-143,'K',145-194,'G',196-262 ##label KAP !'##cross-references GB:M21627 REFERENCE S01738 !$#authors Rasschaert, D.; Gelfi, J.; Laude, H. !$#journal Biochimie (1987) 69:591-600 !$#title Enteric coronavirus TGEV: partial sequence of the genomic !1RNA, its organization and expression. !$#cross-references MUID:88078100; PMID:2825819 !$#accession S03935 !'##molecule_type mRNA !'##residues 1-262 ##label RAS !'##cross-references EMBL:X06371 CLASSIFICATION #superfamily coronavirus E1 membrane glycoprotein KEYWORDS glycoprotein; matrix protein; transmembrane protein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-262 #product E1 membrane glycoprotein #status predicted !8#label MAT\ !$56-72 #domain transmembrane #status predicted #label TM1\ !$85-101 #domain transmembrane #status predicted #label TM2\ !$117-134 #domain transmembrane #status predicted #label TM3\ !$32 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 262 #molecular-weight 29612 #checksum 8254 SEQUENCE /// ENTRY MFIHPC #type complete TITLE E1 membrane glycoprotein - porcine transmissible gastroenteritis virus (strain Purdue) ALTERNATE_NAMES matrix glycoprotein ORGANISM #formal_name porcine transmissible gastroenteritis virus DATE 04-Dec-1986 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS A29241; A04021 REFERENCE A94380 !$#authors Kapke, P.A.; Tung, F.Y.T.; Hogue, B.G.; Brian, D.A.; Woods, !1R.D.; Wesley, R. !$#journal Virology (1988) 165:367-376 !$#title The amino-terminal signal peptide on the porcine !1transmissible gastroenteritis coronavirus matrix protein is !1not an absolute requirement for membrane translocation and !1glycosylation. !$#cross-references MUID:88306229; PMID:2841792 !$#accession A29241 !'##molecule_type genomic RNA !'##residues 1-289 ##label KAP !'##cross-references GB:M21627; GB:M27409; NID:g335206; PIDN:AAA47912.1; !1PID:g335207 GENETICS !$#gene M CLASSIFICATION #superfamily coronavirus E1 membrane glycoprotein KEYWORDS glycoprotein; matrix protein; membrane protein FEATURE !$59,82,278 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 289 #molecular-weight 32715 #checksum 3522 SEQUENCE /// ENTRY S24281 #type complete TITLE E1 membrane glycoprotein precursor - porcine respiratory virus (strain 86/137004) ALTERNATE_NAMES matrix glycoprotein ORGANISM #formal_name porcine respiratory virus #variety strain 86/137004 DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jul-1999 ACCESSIONS S24281; S21310 REFERENCE S24279 !$#authors Britton, P.; Mawditt, K.L.; Page, K.W. !$#journal Virus Res. (1991) 21:181-198 !$#title The cloning and sequencing of the virion protein genes from !1a British isolate of porcine respiratory coronavirus: !1comparison with transmissible gastroenteritis virus genes. !$#cross-references MUID:92116634; PMID:1662846 !$#accession S24281 !'##molecule_type genomic RNA !'##residues 1-262 ##label BRI !'##cross-references EMBL:X60056; NID:g61342; PIDN:CAA42656.1; !1PID:g61345; EMBL:X55980; NID:g61337; PID:g61340 !'##experimental_source strain 86/137004 CLASSIFICATION #superfamily coronavirus E1 membrane glycoprotein KEYWORDS glycoprotein; matrix protein; transmembrane protein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-262 #product E1 membrane glycoprotein #status predicted !8#label EMG\ !$54-72 #domain transmembrane #status predicted #label TM1\ !$86-104 #domain transmembrane #status predicted #label TM2\ !$112-134 #domain transmembrane #status predicted #label TM3\ !$32 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 262 #molecular-weight 29610 #checksum 7811 SEQUENCE /// ENTRY MFIH79 #type complete TITLE E1 membrane glycoprotein precursor - feline infectious peritonitis virus (strain 79-1146) ALTERNATE_NAMES M glycoprotein; matrix glycoprotein ORGANISM #formal_name feline infectious peritonitis virus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jul-1999 ACCESSIONS A38498 REFERENCE A38498 !$#authors Vennema, H.; De Groot, R.J.; Harbour, D.A.; Horzinek, M.C.; !1Spaan, W.J.M. !$#journal Virology (1991) 181:327-335 !$#title Primary structure of the membrane and nucleocapsid protein !1genes of feline infectious peritonitis virus and !1immunogenicity of recombinant vaccinia viruses in kittens. !$#cross-references MUID:91134997; PMID:1847259 !$#accession A38498 !'##molecule_type genomic RNA !'##residues 1-262 ##label VEN !'##cross-references EMBL:X56496; NID:g58918; PIDN:CAA39850.1; !1PID:g58919 CLASSIFICATION #superfamily coronavirus E1 membrane glycoprotein KEYWORDS glycoprotein; matrix protein; transmembrane protein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-262 #product E1 membrane glycoprotein #status predicted !8#label MAT\ !$51-72 #domain transmembrane #status predicted #label TM1\ !$85-101 #domain transmembrane #status predicted #label TM2\ !$112-129 #domain transmembrane #status predicted #label TM3\ !$32,55,251 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 262 #molecular-weight 29832 #checksum 9480 SEQUENCE /// ENTRY JQ1724 #type complete TITLE E1 membrane glycoprotein precursor - canine coronavirus (strain Insavc-1) ALTERNATE_NAMES matrix glycoprotein ORGANISM #formal_name canine coronavirus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jun-2000 ACCESSIONS JQ1724 REFERENCE PQ0481 !$#authors Horsburgh, B.C.; Brierley, I.; Brown, T.D.K. !$#journal J. Gen. Virol. (1992) 73:2849-2862 !$#title Analysis of a 9.6 kb sequence from the 3' end of canine !1coronavirus genomic RNA. !$#cross-references MUID:93057357; PMID:1431811 !$#accession JQ1724 !'##molecule_type genomic RNA !'##residues 1-262 ##label HOR !'##cross-references DDBJ:D13096; NID:g406193; PIDN:BAA02413.1; !1PID:g406200 GENETICS !$#gene M CLASSIFICATION #superfamily coronavirus E1 membrane glycoprotein KEYWORDS glycoprotein; matrix protein; transmembrane protein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-262 #product E1 membrane glycoprotein #status predicted !8#label MAT\ !$56-72 #domain transmembrane #status predicted #label TM1\ !$85-101 #domain transmembrane #status predicted #label TM2\ !$115-134 #domain transmembrane #status predicted #label TM3\ !$32,55 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$33,57 #binding_site carbohydrate (Ser) (covalent) #status !8predicted\ !$44 #binding_site carbohydrate (Thr) (covalent) #status !8predicted SUMMARY #length 262 #molecular-weight 29508 #checksum 7704 SEQUENCE /// ENTRY MMIHHC #type complete TITLE E1 membrane glycoprotein - human coronavirus (strain 229E) ALTERNATE_NAMES M glycoprotein; matrix glycoprotein; membrane glycoprotein ORGANISM #formal_name human coronavirus #note host Homo sapiens (man) DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Jul-1999 ACCESSIONS A34127; A44952; S05464 REFERENCE A34127 !$#authors Jouvenne, P.; Richardson, C.D.; Schreiber, S.S.; Lai, !1M.M.C.; Talbot, P.J. !$#journal Virology (1990) 174:608-612 !$#title Sequence analysis of the membrane protein gene of human !1coronavirus 229E. !$#cross-references MUID:90163229; PMID:2305554 !$#accession A34127 !'##molecule_type genomic RNA !'##residues 1-225 ##label JOU !'##cross-references GB:M33560; NID:g329572; PIDN:AAA45461.1; !1PID:g329573 REFERENCE A44952 !$#authors Raabe, T.; Siddell, S.G. !$#journal Arch. Virol. (1989) 107:323-328 !$#title Nucleotide sequence of the gene encoding the membrane !1protein of human coronavirus 229 E. !$#cross-references MUID:90055844; PMID:2818210 !$#accession A44952 !'##molecule_type genomic RNA !'##residues 1-42,'F',44-80,'FF',83-190,'C',192-225 ##label RAA REFERENCE A34038 !$#authors Raabe, T.; Siddell, S. !$#journal Nucleic Acids Res. (1989) 17:6387 !$#title Nucleotide sequence of the human coronavirus HCV 229E mRNA 4 !1and mRNA 5 unique regions. !$#cross-references MUID:89366667; PMID:2701946 !$#accession S05464 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-12 ##label RA2 !'##cross-references EMBL:X15654 CLASSIFICATION #superfamily coronavirus E1 membrane glycoprotein KEYWORDS glycoprotein; matrix protein; transmembrane protein FEATURE !$19-35 #domain transmembrane #status predicted #label TM1\ !$48-64 #domain transmembrane #status predicted #label TM2\ !$76-92 #domain transmembrane #status predicted #label TM3\ !$5,190,214 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 225 #molecular-weight 25852 #checksum 2539 SEQUENCE /// ENTRY MMIHIV #type complete TITLE E1 membrane glycoprotein - avian infectious bronchitis virus ALTERNATE_NAMES matrix glycoprotein ORGANISM #formal_name avian infectious bronchitis virus, IBV DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 24-Sep-1999 ACCESSIONS A04022 REFERENCE A04022 !$#authors Boursnell, M.E.G.; Brown, T.D.K.; Binns, M.M. !$#journal Virus Res. (1984) 1:303-313 !$#title Sequence of the membrane protein gene from avian coronavirus !1IBV. !$#cross-references MUID:85170518; PMID:6099661 !$#accession A04022 !'##molecule_type genomic RNA !'##residues 1-225 ##label BOU !'##cross-references GB:M95169; GB:M27569; NID:g292951; PIDN:AAA70239.1; !1PID:g292958 CLASSIFICATION #superfamily coronavirus E1 membrane glycoprotein KEYWORDS glycoprotein; transmembrane protein FEATURE !$23-42 #domain transmembrane #status predicted #label TM1\ !$52-72 #domain transmembrane #status predicted #label TM2\ !$76-98 #domain transmembrane #status predicted #label TM3\ !$3,6 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 225 #molecular-weight 25475 #checksum 6783 SEQUENCE /// ENTRY MMIHIB #type complete TITLE E1 membrane glycoprotein - avian infectious bronchitis virus (strain Beaudette M42) ALTERNATE_NAMES matrix glycoprotein ORGANISM #formal_name avian infectious bronchitis virus, IBV DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 25-Oct-1996 ACCESSIONS A27080 REFERENCE A27080 !$#authors Machamer, C.E.; Rose, J.K. !$#journal J. Cell Biol. (1987) 105:1205-1214 !$#title A specific transmembrane domain of a coronavirus E1 !1glycoprotein is required for its retention in the Golgi !1region. !$#cross-references MUID:88007845; PMID:2821010 !$#accession A27080 !'##status nucleic acid sequence not shown !'##molecule_type genomic RNA !'##residues 1-225 ##label MAC GENETICS !$#gene E1 CLASSIFICATION #superfamily coronavirus E1 membrane glycoprotein KEYWORDS glycoprotein; transmembrane protein FEATURE !$21-42 #domain transmembrane #status predicted #label TM1\ !$52-72 #domain transmembrane #status predicted #label TM2\ !$78-101 #domain transmembrane #status predicted #label TM3\ !$3,6 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 225 #molecular-weight 25477 #checksum 6635 SEQUENCE /// ENTRY MMIHAI #type complete TITLE E1 membrane glycoprotein - avian infectious bronchitis virus (strain KB8523) ALTERNATE_NAMES matrix glycoprotein ORGANISM #formal_name avian infectious bronchitis virus, IBV DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 25-Oct-1996 ACCESSIONS C29249 REFERENCE A29249 !$#authors Sutou, S.; Sato, S.; Okabe, T.; Nakai, M.; Sasaki, N. !$#journal Virology (1988) 165:589-595 !$#title Cloning and sequencing of genes encoding structural proteins !1of avian infectious bronchitis virus. !$#cross-references MUID:88306251; PMID:2841803 !$#accession C29249 !'##molecule_type genomic RNA !'##residues 1-225 ##label SUT CLASSIFICATION #superfamily coronavirus E1 membrane glycoprotein KEYWORDS glycoprotein; matrix protein; transmembrane protein FEATURE !$21-42 #domain transmembrane #status predicted #label TN1\ !$52-72 #domain transmembrane #status predicted #label TN2\ !$78-101 #domain transmembrane #status predicted #label TN3\ !$3,6 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 225 #molecular-weight 25567 #checksum 4257 SEQUENCE /// ENTRY MMIH68 #type complete TITLE E1 membrane glycoprotein - avian infectious bronchitis virus (strain 6/82) ALTERNATE_NAMES matrix glycoprotein ORGANISM #formal_name avian infectious bronchitis virus, IBV DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 24-Sep-1999 ACCESSIONS A23649 REFERENCE A23649 !$#authors Binns, M.M.; Boursnell, M.E.G.; Tomley, F.M.; Brown, T.D.K. !$#journal Nucleic Acids Res. (1986) 14:5558 !$#title Nucleotide sequence encoding the membrane protein of the IBV !1strain 6/82. !$#cross-references MUID:86286562; PMID:3016650 !$#accession A23649 !'##molecule_type genomic RNA !'##residues 1-225 ##label BIN !'##cross-references GB:X04107; NID:g58949; PIDN:CAA27727.1; PID:g58950 CLASSIFICATION #superfamily coronavirus E1 membrane glycoprotein KEYWORDS glycoprotein; transmembrane protein FEATURE !$23-39 #domain transmembrane #status predicted #label TM1\ !$52-68 #domain transmembrane #status predicted #label TM2\ !$78-94 #domain transmembrane #status predicted #label TM3\ !$3,6 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 225 #molecular-weight 25465 #checksum 4535 SEQUENCE /// ENTRY VGIHE2 #type complete TITLE E2 glycoprotein precursor - porcine transmissible gastroenteritis virus (strain Purdue-115) ALTERNATE_NAMES spike glycoprotein ORGANISM #formal_name porcine transmissible gastroenteritis virus #variety strain Purdue-115 DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 24-Sep-1999 ACCESSIONS A27106; S01738 REFERENCE A27106 !$#authors Rasschaert, D.; Laude, H. !$#journal J. Gen. Virol. (1987) 68:1883-1890 !$#title The predicted primary structure of the peplomer protein E2 !1of the porcine coronavirus transmissible gastroenteritis !1virus. !$#cross-references MUID:87253116; PMID:3037011 !$#accession A27106 !'##molecule_type genomic RNA !'##residues 1-1447 ##label RAS !'##cross-references GB:X05695; GB:D00118; NID:g59007; PIDN:CAA29175.1; !1PID:g59008 !'##experimental_source strain Purdue-115 REFERENCE S01738 !$#authors Rasschaert, D.; Gelfi, J.; Laude, H. !$#journal Biochimie (1987) 69:591-600 !$#title Enteric coronavirus TGEV: partial sequence of the genomic !1RNA, its organization and expression. !$#cross-references MUID:88078100; PMID:2825819 !$#accession S01738 !'##molecule_type genomic RNA !'##residues 1434-1447 ##label RAW !'##cross-references EMBL:X06371 !'##experimental_source strain Purdue-115 CLASSIFICATION #superfamily coronavirus E2 glycoprotein KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-1447 #product E2 glycoprotein #status predicted #label !8MAT\ !$1387-1431 #domain transmembrane #status predicted #label TMM\ !$26,42,71,94,243, !$250,285,334,345, !$362,403,447,514, !$530,552,592,702, !$723,778,817,832, !$838,919,1072,1198, !$1292,1309,1322, !$1334,1339,1356,1369 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1447 #molecular-weight 160133 #checksum 6227 SEQUENCE /// ENTRY VGIHE3 #type complete TITLE E2 glycoprotein precursor - porcine transmissible gastroenteritis virus (strain Purdue) ALTERNATE_NAMES peplomer protein; spike glycoprotein ORGANISM #formal_name porcine transmissible gastroenteritis virus DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 12-Apr-1996 ACCESSIONS JS0336 REFERENCE JS0336 !$#authors Jacobs, L.; de Groot, R.; van der Zeijst, B.A.M.; Horzinek, !1M.C.; Spaan, W. !$#journal Virus Res. (1987) 8:363-371 !$#title The nucleotide sequence of the peplomer gene of porcine !1transmissible gastroenteritis virus (TGEV): comparison with !1the sequence of the peplomer protein of feline infectious !1peritonitis virus (FIPV). !$#cross-references MUID:88129049; PMID:2829461 !$#accession JS0336 !'##molecule_type mRNA !'##residues 1-1447 ##label JAC CLASSIFICATION #superfamily coronavirus E2 glycoprotein KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-1447 #product E2 glycoprotein #status predicted #label !8MAT\ !$1387-1431 #domain transmembrane #status predicted #label TMM\ !$26,42,71,94,243, !$250,285,334,345, !$362,403,447,514, !$530,552,592,702, !$723,778,817,832, !$838,919,1072,1198, !$1292,1309,1322, !$1334,1339,1356,1369 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1447 #molecular-weight 160167 #checksum 5735 SEQUENCE /// ENTRY VGIHFS #type complete TITLE E2 glycoprotein precursor - porcine transmissible gastroenteritis virus (strain FS772/70) ALTERNATE_NAMES peplomer glycoprotein; spike glycoprotein ORGANISM #formal_name porcine transmissible gastroenteritis virus DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS B43489; S11728 REFERENCE A43489 !$#authors Britton, P.; Page, K.W. !$#journal Virus Res. (1990) 18:71-80 !$#title Sequence of the S gene from a virulent British field isolate !1of transmissible gastroenteritis virus. !$#cross-references MUID:91188698; PMID:1964522 !$#accession B43489 !'##molecule_type mRNA !'##residues 1-1449 ##label BRI !'##cross-references GB:X53128; NID:g61377; PIDN:CAA37285.1; PID:g61379 CLASSIFICATION #superfamily coronavirus E2 glycoprotein KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-1449 #product E2 glycoprotein #status predicted #label !8E2G\ !$1027-1043 #region hydrophobic\ !$1395-1411 #domain transmembrane #status predicted #label TMN\ !$26,42,71,94,243, !$250,285,334,345, !$362,375,405,449, !$516,532,554,594, !$704,725,780,819, !$834,840,921,1074, !$1200,1294,1311, !$1324,1336,1341, !$1358,1371 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1449 #molecular-weight 159957 #checksum 921 SEQUENCE /// ENTRY A43573 #type complete TITLE E2 glycoprotein precursor - porcine transmissible gastroenteritis virus (strain Miller) ALTERNATE_NAMES peplomer glycoprotein; spike glycoprotein ORGANISM #formal_name porcine transmissible gastroenteritis virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jul-1999 ACCESSIONS A43573 REFERENCE A43573 !$#authors Wesley, R.D. !$#journal Adv. Exp. Med. Biol. (1990) 276:301-306 !$#title Nucleotide sequence of the E2-peplomer protein gene and !1partial nucleotide sequence of the upstream polymerase gene !1of transmissible gastroenteritis virus (Miller strain). !$#cross-references MUID:91353366; PMID:1966416 !$#accession A43573 !'##molecule_type genomic RNA !'##residues 1-1449 ##label WES !'##cross-references GB:S51223; NID:g234109; PIDN:AAB19567.1; !1PID:g234110 !'##note the authors translated the codon GAA for residue 388 as Cys CLASSIFICATION #superfamily coronavirus E2 glycoprotein KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-1449 #product E2 glycoprotein #status predicted #label !8E2G\ !$1027-1043 #region hydrophobic\ !$1391-1411 #domain transmembrane #status predicted #label TMN\ !$26,42,71,94,243, !$250,285,334,345, !$362,375,405,449, !$516,532,554,594, !$704,725,780,819, !$834,840,921,1074, !$1200,1294,1311, !$1324,1336,1341, !$1358,1371 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1449 #molecular-weight 159889 #checksum 2767 SEQUENCE /// ENTRY S24284 #type complete TITLE E2 glycoprotein precursor - porcine respiratory virus (strain 86/137004) ALTERNATE_NAMES peplomer glycoprotein; spike glycoprotein ORGANISM #formal_name porcine respiratory virus #variety strain 86/137004 DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jul-1999 ACCESSIONS S24284; S21871 REFERENCE S24279 !$#authors Britton, P.; Mawditt, K.L.; Page, K.W. !$#journal Virus Res. (1991) 21:181-198 !$#title The cloning and sequencing of the virion protein genes from !1a British isolate of porcine respiratory coronavirus: !1comparison with transmissible gastroenteritis virus genes. !$#cross-references MUID:92116634; PMID:1662846 !$#accession S24284 !'##molecule_type genomic RNA !'##residues 1-1225 ##label BRI !'##cross-references EMBL:X60089; NID:g58983; PIDN:CAA42686.1; !1PID:g58984 !'##experimental_source strain 86/137004 CLASSIFICATION #superfamily coronavirus E2 glycoprotein KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-1225 #product E2 glycoprotein #status predicted #label !8E2G\ !$1167-1187 #domain transmembrane #status predicted #label TMN\ !$26,61,110,121,138, !$151,181,225,256, !$292,308,330,338, !$370,480,501,556, !$595,610,616,697, !$850,976,1070,1087, !$1100,1112,1117, !$1134,1147 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1225 #molecular-weight 134728 #checksum 4997 SEQUENCE /// ENTRY VGIH79 #type complete TITLE E2 glycoprotein precursor - feline infectious peritonitis virus (strain 79-1146) ALTERNATE_NAMES peplomer glycoprotein; spike glycoprotein ORGANISM #formal_name feline infectious peritonitis virus DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 24-Sep-1999 ACCESSIONS A27171 REFERENCE A27171 !$#authors De Groot, R.J.; Maduro, J.; Lenstra, J.A.; Horzinek, M.C.; !1Van Der Zeijst, B.A.M.; Spaan, W.J.M. !$#journal J. Gen. Virol. (1987) 68:2639-2646 !$#title cDNA cloning and sequence analysis of the gene encoding the !1peplomer protein of feline infectious peritonitis virus. !$#cross-references MUID:88034948; PMID:3312491 !$#accession A27171 !'##molecule_type genomic RNA !'##residues 1-1452 ##label DEG !'##cross-references GB:X06170; GB:D00150; NID:g58915; PIDN:CAA29535.1; !1PID:g58916 CLASSIFICATION #superfamily coronavirus E2 glycoprotein KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$1-19 #domain transmembrane #status predicted #label TM1\ !$20-1452 #product spike glycoprotein #status predicted #label !8SPG\ !$1394-1414 #domain transmembrane #status predicted #label TM2\ !$29,95,174,208,234, !$241,288,337,348, !$365,408,452,483, !$519,535,557,565, !$707,728,783,822, !$837,843,924,1077, !$1203,1297,1314, !$1327,1339,1344, !$1361,1374 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1452 #molecular-weight 160469 #checksum 6856 SEQUENCE /// ENTRY JQ1719 #type complete TITLE E2 glycoprotein precursor - canine coronavirus (strain Insavc-1) ALTERNATE_NAMES spike glycoprotein ORGANISM #formal_name canine coronavirus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jun-2000 ACCESSIONS JQ1719 REFERENCE PQ0481 !$#authors Horsburgh, B.C.; Brierley, I.; Brown, T.D.K. !$#journal J. Gen. Virol. (1992) 73:2849-2862 !$#title Analysis of a 9.6 kb sequence from the 3' end of canine !1coronavirus genomic RNA. !$#cross-references MUID:93057357; PMID:1431811 !$#accession JQ1719 !'##molecule_type genomic RNA !'##residues 1-1451 ##label HOR !'##cross-references DDBJ:D13096; NID:g406193; PIDN:BAA02408.1; !1PID:g406195 GENETICS !$#gene S CLASSIFICATION #superfamily coronavirus E2 glycoprotein KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-1451 #product spike glycoprotein #status predicted #label !8MAT\ !$1394-1412 #domain transmembrane #status predicted #label TMM\ !$28,66,94,142,175, !$209,235,242,289, !$338,349,366,379, !$409,453,520,536, !$557,707,728,783, !$821,836,842,923, !$1076,1202,1296, !$1313,1326,1343, !$1360,1373 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1451 #molecular-weight 160466 #checksum 4257 SEQUENCE /// ENTRY VGIHHC #type complete TITLE E2 glycoprotein precursor - human coronavirus (strain 229E) ALTERNATE_NAMES peplomer glycoprotein; S glycoprotein; spike glycoprotein ORGANISM #formal_name human coronavirus #note host Homo sapiens (man) DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jun-2000 ACCESSIONS A34766; S05460 REFERENCE A34766 !$#authors Raabe, T.; Schelle-Prinz, B.; Siddell, S.G. !$#journal J. Gen. Virol. (1990) 71:1065-1073 !$#title Nucleotide sequence of the gene encoding the spike !1glycoprotein of human coronavirus HCV 229E. !$#cross-references MUID:90264837; PMID:2345367 !$#accession A34766 !'##molecule_type mRNA !'##residues 1-1173 ##label RAA !'##cross-references EMBL:X16816; NID:g58926; PIDN:CAA34723.1; !1PID:g58927 !'##experimental_source strain 229E REFERENCE A34038 !$#authors Raabe, T.; Siddell, S. !$#journal Nucleic Acids Res. (1989) 17:6387 !$#title Nucleotide sequence of the human coronavirus HCV 229E mRNA 4 !1and mRNA 5 unique regions. !$#cross-references MUID:89366667; PMID:2701946 !$#accession S05460 !'##status translation not shown !'##molecule_type mRNA !'##residues 1159-1173 ##label RA2 !'##cross-references EMBL:X15654; NID:g58921; PIDN:CAA33680.1; !1PID:g1334827 CLASSIFICATION #superfamily coronavirus E2 glycoprotein KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-1173 #product E2 glycoprotein #status predicted #label !8MAT\ !$1116-1138 #domain transmembrane #status predicted #label TMN\ !$23,62,98,147,171, !$176,220,243,326, !$333,440,464,518, !$538,542,568,581, !$587,663,671,930, !$1015,1020,1037, !$1049,1061,1066, !$1076,1082,1096 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1173 #molecular-weight 128638 #checksum 7399 SEQUENCE /// ENTRY VGIHIB #type complete TITLE E2 glycoprotein precursor - avian infectious bronchitis virus (strain D274) ALTERNATE_NAMES peplomer protein; spike protein CONTAINS E2 glycoprotein subunit S1; E2 glycoprotein subunit S2 ORGANISM #formal_name avian infectious bronchitis virus, IBV DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS A34300 REFERENCE A34300 !$#authors Jordi, B.J.A.M.; Kremers, D.A.W.M.; Kusters, H.G.; van der !1Zeijst, B.A.M. !$#journal Nucleic Acids Res. (1989) 17:6726 !$#title Nucleotide sequence of the gene coding for the peplomer !1protein (=spike protein) of infectious bronchitis virus, !1strain D274. !$#cross-references MUID:89386000; PMID:2550899 !$#accession A34300 !'##status translation not shown !'##molecule_type genomic RNA !'##residues 1-1154 ##label JOR !'##cross-references EMBL:X15832; NID:g58951; PIDN:CAA33837.1; !1PID:g58952 !'##note it is uncertain if residue 761 is Phe or Leu CLASSIFICATION #superfamily coronavirus E2 glycoprotein KEYWORDS glycoprotein; peplomer protein; spike protein FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-538 #product E2 glycoprotein subunit S1 #status predicted !8#label GS1\ !$539-1154 #product E2 glycoprotein subunit S2 #status predicted !8#label GS2\ !$23,74,102,139,145, !$164,179,213,238, !$248,265,272,277, !$280,307,426,448, !$514,531,543,580, !$592,670,677,948, !$961,980,1015,1039, !$1052,1075 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1154 #molecular-weight 127502 #checksum 5448 SEQUENCE /// ENTRY VGIHD6 #type fragment TITLE E2 glycoprotein precursor - avian infectious bronchitis virus (strain D3896) (fragment) ALTERNATE_NAMES peplomer glycoprotein; S glycoprotein; S1 glycoprotein; spike glycoprotein CONTAINS amino end of E2 glycoprotein subunit S2; E2 glycoprotein subunit S1 ORGANISM #formal_name avian infectious bronchitis virus, IBV DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS S10175 REFERENCE S10175 !$#authors Koch, G.; Kant, A. !$#journal Nucleic Acids Res. (1990) 18:3063-3064 !$#title Nucleotide and amino acid sequence of the S1 subunit of the !1spike glycoprotein of avian infectious bronchitis virus, !1strain D3896. !$#cross-references MUID:90272429; PMID:2161519 !$#accession S10175 !'##molecule_type mRNA !'##residues 1-550 ##label KOC !'##cross-references EMBL:X52084; NID:g58955; PIDN:CAA36302.1; !1PID:g58956 CLASSIFICATION #superfamily coronavirus E2 glycoprotein KEYWORDS glycoprotein FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-538 #product E2 glycoprotein subunit S1 #status predicted !8#label ES1\ !$539-550 #product E2 glycoprotein subunit S2 #status predicted !8#label ES2\ !$23,51,74,102,139, !$145,164,179,213, !$238,248,265,272, !$277,307,426,448, !$514,531,543 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 550 #checksum 644 SEQUENCE /// ENTRY VGIHAK #type complete TITLE E2 glycoprotein precursor - avian infectious bronchitis virus (strain KB8523) ALTERNATE_NAMES peplomer protein; spike protein CONTAINS E2 glycoprotein subunit S1; E2 glycoprotein subunit S2 ORGANISM #formal_name avian infectious bronchitis virus, IBV DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS B29249 REFERENCE A29249 !$#authors Sutou, S.; Sato, S.; Okabe, T.; Nakai, M.; Sasaki, N. !$#journal Virology (1988) 165:589-595 !$#title Cloning and sequencing of genes encoding structural proteins !1of avian infectious bronchitis virus. !$#cross-references MUID:88306251; PMID:2841803 !$#accession B29249 !'##molecule_type genomic RNA !'##residues 1-1162 ##label SUT !'##cross-references GB:M21515; NID:g808698; PIDN:AAA66578.1; !1PID:g331187 CLASSIFICATION #superfamily coronavirus E2 glycoprotein KEYWORDS glycoprotein; peplomer protein; spike protein FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-537 #product E2 glycoprotein subunit S1 #status predicted !8#label GS1\ !$538-1162 #product E2 glycoprotein subunit S2 #status predicted !8#label GS2\ !$51,77,103,144,163, !$178,212,237,247, !$264,271,276,283, !$306,425,447,513, !$530,579,591,669, !$676,714,947,960, !$979,1014,1051,1058, !$1074 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1162 #molecular-weight 128537 #checksum 6496 SEQUENCE /// ENTRY VGIH59 #type complete TITLE E2 glycoprotein precursor - murine hepatitis virus (strain A59) ALTERNATE_NAMES peplomer glycoprotein; spike glycoprotein ORGANISM #formal_name murine hepatitis virus, MHV DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 12-Apr-1996 ACCESSIONS A27402 REFERENCE A27402 !$#authors Luytjes, W.; Sturman, L.S.; Bredenbeek, P.J.; Charite, J.; !1van der Zeijst, B.A.M.; Horzinek, M.C.; Spaan, W.J.M. !$#journal Virology (1987) 161:479-487 !$#title Primary structure of the glycoprotein E2 of coronavirus !1MHV-A59 and identification of the trypsin cleavage site. !$#cross-references MUID:88072088; PMID:2825419 !$#accession A27402 !'##molecule_type genomic RNA !'##residues 1-1324 ##label LUY CLASSIFICATION #superfamily coronavirus E2 glycoprotein KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-1324 #product E2 glycoprotein #status predicted #label !8E2G\ !$17-717 #product 90B glycoprotein #status predicted #label !8EGB\ !$718-1324 #product 90A glycoprotein #status predicted #label !8EGA\ !$1266-1286 #domain transmembrane #status predicted #label TMN\ !$31,60,192,247,357, !$435,442,530,625, !$657,665,688,737, !$754,844,893,1126, !$1180,1190,1209, !$1225,1246,1318 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1324 #molecular-weight 145963 #checksum 7500 SEQUENCE /// ENTRY VGIHMJ #type complete TITLE E2 glycoprotein precursor - murine hepatitis virus (strain JHM) ALTERNATE_NAMES peplomer glycoprotein; spike glycoprotein CONTAINS 90A glycoprotein; 90B glycoprotein ORGANISM #formal_name murine hepatitis virus, MHV DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 24-Sep-1999 ACCESSIONS A33095 REFERENCE A33095 !$#authors Schmidt, I.; Skinner, M.; Siddell, S. !$#journal J. Gen. Virol. (1987) 68:47-56 !$#title Nucleotide sequence of the gene encoding the surface !1projection glycoprotein of coronavirus MHV-JHM. !$#cross-references MUID:87111467; PMID:3027248 !$#accession A33095 !'##molecule_type genomic RNA !'##residues 1-1235 ##label SCH !'##cross-references GB:X04797; GB:D00093; GB:M34437; NID:g58979; !1PIDN:CAA28484.1; PID:g58980 CLASSIFICATION #superfamily coronavirus E2 glycoprotein KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-10 #domain signal sequence #status predicted #label SIG\ !$11-1235 #product E2 glycoprotein #status predicted #label !8E2G\ !$11-628 #product 90B glycoprotein #status predicted #label !8EGB\ !$629-1235 #product 90A glycoprotein #status predicted #label !8EGA\ !$1175-1208 #domain transmembrane #status predicted #label TMN\ !$31,60,134,192,357, !$435,442,536,568, !$576,599,648,665, !$755,804,1037,1091, !$1101,1120,1136, !$1157,1229 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1235 #molecular-weight 136653 #checksum 9154 SEQUENCE /// ENTRY VGIHJ2 #type complete TITLE E2 glycoprotein precursor - murine hepatitis virus (strain wild type MHV-4) ALTERNATE_NAMES peplomer glycoprotein; spike glycoprotein CONTAINS 90A glycoprotein; 90B glycoprotein ORGANISM #formal_name murine hepatitis virus, MHV DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Jul-1999 ACCESSIONS A33748 REFERENCE A33748 !$#authors Parker, S.E.; Gallagher, T.M.; Buchmeier, M.J. !$#journal Virology (1989) 173:664-673 !$#title Sequence analysis reveals extensive polymorphism and !1evidence of deletions within the E2 glycoprotein gene of !1several strains of murine hepatitis virus. !$#cross-references MUID:90085815; PMID:2556846 !$#accession A33748 !'##molecule_type genomic RNA !'##residues 1-1376 ##label PAR !'##cross-references GB:M32789; NID:g331846; PIDN:AAA46456.1; !1PID:g331847 CLASSIFICATION #superfamily coronavirus E2 glycoprotein KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-14 #domain signal sequence #status predicted #label SIG\ !$15-1376 #product E2 glycoprotein #status predicted #label !8E2G\ !$15-769 #product 90B glycoprotein #status predicted #label !8EGB\ !$770-1376 #product 90A glycoprotein #status predicted #label !8EGA\ !$1321-1338 #domain transmembrane #status predicted #label TMN\ !$31,60,134,192,357, !$435,442,582,677, !$709,717,740,789, !$806,896,945,1178, !$1232,1242,1261, !$1277,1298,1370 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1376 #molecular-weight 151881 #checksum 4481 SEQUENCE /// ENTRY JQ1534 #type complete TITLE E2 glycoprotein precursor - murine hepatitis virus (strain JHM cl-2) ALTERNATE_NAMES peplomer glycoprotein; spike glycoprotein CONTAINS 90A glycoprotein; 90B glycoprotein ORGANISM #formal_name murine hepatitis virus, MHV DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 07-May-1999 ACCESSIONS JQ1534 REFERENCE JQ1534 !$#authors Taguchi, F.; Ikeda, T.; Shida, H. !$#journal J. Gen. Virol. (1992) 73:1065-1072 !$#title Molecular cloning and expression of a spike protein of !1neurovirulent murine coronavirus JHMV variant cl-2. !$#cross-references MUID:92268864; PMID:1316938 !$#accession JQ1534 !'##molecule_type mRNA !'##residues 1-1376 ##label TAG !'##cross-references DDBJ:D10255 !'##note the authors translated the codon TTT for residue 8 as Leu, GGG !1for residue 14 as Phe, ACT for residue 135 as Ser, and CGC !1for residue 1141 as Thr CLASSIFICATION #superfamily coronavirus E2 glycoprotein KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-14 #domain signal sequence #status predicted #label SIG\ !$15-1376 #product E2 glycoprotein #status predicted #label !8E2G\ !$15-769 #product 90B glycoprotein #status predicted #label !8EGB\ !$770-1376 #product 90A glycoprotein #status predicted #label !8EGA\ !$1318-1339 #domain transmembrane #status predicted #label TMM\ !$31,60,134,192,357, !$435,677,709,717, !$789,806,945,1232, !$1242,1261,1277,1298 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1376 #molecular-weight 152040 #checksum 4480 SEQUENCE /// ENTRY VGIHNM #type complete TITLE E2 glycoprotein precursor - bovine coronavirus (strain Mebus) ALTERNATE_NAMES peplomer glycoprotein; S glycoprotein; spike glycoprotein CONTAINS 90A glycoprotein; 90B glycoprotein ORGANISM #formal_name bovine coronavirus DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS A34607 REFERENCE A34607 !$#authors Abraham, S.; Kienzle, T.E.; Lapps, W.; Brian, D.A. !$#journal Virology (1990) 176:296-301 !$#title Deduced sequence of the bovine coronavirus spike protein and !1identification of the internal proteolytic cleavage site. !$#cross-references MUID:90232743; PMID:2184576 !$#accession A34607 !'##molecule_type genomic RNA !'##residues 1-1363 ##label ABR !'##cross-references GB:M31053; NID:g323361; PIDN:AAA66399.1; !1PID:g323362 CLASSIFICATION #superfamily coronavirus E2 glycoprotein KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-1363 #product E2 glycoprotein #status predicted #label !8E2G\ !$18-768 #product 90B glycoprotein #status predicted #label !8EGB\ !$769-1363 #product 90A glycoprotein #status predicted #label !8EGA\ !$1312-1328 #domain transmembrane #status predicted #label TMN\ !$59,133,198,359,437, !$444,649,676,696, !$714,739,788,895, !$937,1194,1224,1234, !$1253,1267,1288 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1363 #molecular-weight 150809 #checksum 7580 SEQUENCE /// ENTRY VGIHQU #type complete TITLE E2 glycoprotein precursor - bovine coronavirus (strain Quebec) ALTERNATE_NAMES peplomer glycoprotein; S glycoprotein; spike glycoprotein CONTAINS 90A glycoprotein; 90B glycoprotein ORGANISM #formal_name bovine coronavirus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 07-Oct-1994 ACCESSIONS A34147 REFERENCE A34147 !$#authors Parker, M.D.; Yoo, D.; Cox, G.J.; Babiuk, L.A. !$#journal J. Gen. Virol. (1990) 71:263-270 !$#title Primary structure of the S peplomer gene of bovine !1coronavirus and surface expression in insect cells. !$#cross-references MUID:90171910; PMID:2155283 !$#accession A34147 !'##molecule_type genomic RNA !'##residues 1-1363 ##label PAR !'##cross-references GB:D00662 !'##note in the authors' translation residues 23-31 are shown after !1residue 34 and, consequently, residues 32-34 are displaced !1nine codons to the left !'##note the authors translated the codons UCU, AUU, and AGC for !1residues 35-37 as Ile, Ser, and Thr, respectively !'##note the authors translated the codons CCA, GAU, ACU, CCA, CCU, CCA, !1GAA, GAU, CCU and GAA for residues 10, 18, 163, 168, 264, !1303, 792, 825, 898, and 1125 as Phe, Arg, Tyr, Phe, Phe, !1Phe, Gly, Glu, Phe, and Gly, respectively CLASSIFICATION #superfamily coronavirus E2 glycoprotein KEYWORDS glycoprotein; peplomer protein; spike protein; transmembrane !1protein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-1363 #product E2 glycoprotein #status predicted #label !8E2P\ !$18-768 #product 90B glycoprotein #status predicted #label !8E9B\ !$769-1363 #product 90A glycoprotein #status predicted #label !8E9A\ !$1312-1328 #domain transmembrane #status predicted #label TMN\ !$59,133,198,359,437, !$649,676,696,714, !$739,788,895,937, !$1194,1224,1234, !$1253,1267,1288 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1363 #molecular-weight 150868 #checksum 6831 SEQUENCE /// ENTRY VGIHF1 #type complete TITLE E2 glycoprotein precursor - bovine coronavirus (strain F15) ALTERNATE_NAMES peplomer glycoprotein; S glycoprotein; spike glycoprotein CONTAINS 90A glycoprotein; 90B glycoprotein ORGANISM #formal_name bovine coronavirus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jun-2000 ACCESSIONS A34151 REFERENCE A34151 !$#authors Boireau, P.; Cruciere, C.; Laporte, J. !$#journal J. Gen. Virol. (1990) 71:487-492 !$#title Nucleotide sequence of the glycoprotein S gene of bovine !1enteric coronavirus and comparison with the S proteins of !1two mouse hepatitis virus strains. !$#cross-references MUID:90171938; PMID:2155300 !$#accession A34151 !'##molecule_type genomic RNA !'##residues 1-1363 ##label BOI !'##cross-references GB:D00731; NID:g221136; PIDN:BAA00631.1; !1PID:g221137 CLASSIFICATION #superfamily coronavirus E2 glycoprotein KEYWORDS glycoprotein; peplomer protein; spike protein; transmembrane !1protein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-1363 #product E2 glycoprotein #status predicted #label !8E2P\ !$18-768 #product 90B glycoprotein #status predicted #label !8E9B\ !$769-1363 #product 90A glycoprotein #status predicted #label !8E9A\ !$1312-1328 #domain transmembrane #status predicted #label TMN\ !$59,133,198,359,437, !$444,649,676,696, !$714,739,788,895, !$937,1194,1224,1234, !$1253,1267,1288 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1363 #molecular-weight 150746 #checksum 5372 SEQUENCE /// ENTRY VGIHL9 #type complete TITLE E2 glycoprotein precursor - bovine coronavirus (strain L9) ALTERNATE_NAMES peplomer glycoprotein; S glycoprotein; spike glycoprotein CONTAINS 90A glycoprotein; 90B glycoprotein ORGANISM #formal_name bovine coronavirus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS A40320 REFERENCE A40320 !$#authors Zhang, X.; Kousoulas, K.G.; Storz, J. !$#journal Virology (1991) 183:397-404 !$#title Comparison of the nucleotide and deduced amino acid !1sequences of the S genes specified by virulent and avirulent !1strains of bovine coronaviruses. !$#cross-references MUID:91272503; PMID:2053289 !$#accession A40320 !'##molecule_type genomic RNA !'##residues 1-1363 ##label ZHA !'##cross-references GB:M64667; NID:g323355; PIDN:AAA42907.1; !1PID:g323356 CLASSIFICATION #superfamily coronavirus E2 glycoprotein KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-1363 #product E2 glycoprotein #status predicted #label !8E2G\ !$18-768 #product 90B glycoprotein #status predicted #label !8EGB\ !$769-1363 #product 90A glycoprotein #status predicted #label !8EGA\ !$1312-1328 #domain transmembrane #status predicted #label TMN\ !$59,133,198,359,437, !$444,676,696,714, !$739,788,895,937, !$1194,1224,1234, !$1253,1267,1288 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1363 #molecular-weight 150805 #checksum 5554 SEQUENCE /// ENTRY VGIHVA #type complete TITLE E2 glycoprotein precursor - bovine coronavirus (strain vaccine) ALTERNATE_NAMES peplomer glycoprotein; S glycoprotein; spike glycoprotein CONTAINS 90A glycoprotein; 90B glycoprotein ORGANISM #formal_name bovine coronavirus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 12-Apr-1996 ACCESSIONS B40320 REFERENCE A40320 !$#authors Zhang, X.; Kousoulas, K.G.; Storz, J. !$#journal Virology (1991) 183:397-404 !$#title Comparison of the nucleotide and deduced amino acid !1sequences of the S genes specified by virulent and avirulent !1strains of bovine coronaviruses. !$#cross-references MUID:91272503; PMID:2053289 !$#accession B40320 !'##molecule_type genomic RNA !'##residues 1-1363 ##label ZHA !'##cross-references GB:M64668 CLASSIFICATION #superfamily coronavirus E2 glycoprotein KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-1363 #product E2 glycoprotein #status predicted #label !8E2G\ !$18-768 #product 90B glycoprotein #status predicted #label !8EGB\ !$769-1363 #product 90A glycoprotein #status predicted #label !8EGA\ !$1312-1328 #domain transmembrane #status predicted #label TMN\ !$59,133,198,359,437, !$444,649,676,696, !$714,739,788,895, !$937,1194,1224,1234, !$1253,1267,1288 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1363 #molecular-weight 150858 #checksum 7279 SEQUENCE /// ENTRY VGIHLY #type complete TITLE E2 glycoprotein precursor - bovine coronavirus (strain LY-138) ALTERNATE_NAMES peplomer glycoprotein; S glycoprotein; spike glycoprotein CONTAINS 90A glycoprotein; 90B glycoprotein ORGANISM #formal_name bovine coronavirus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 12-Apr-1996 ACCESSIONS C40320 REFERENCE A40320 !$#authors Zhang, X.; Kousoulas, K.G.; Storz, J. !$#journal Virology (1991) 183:397-404 !$#title Comparison of the nucleotide and deduced amino acid !1sequences of the S genes specified by virulent and avirulent !1strains of bovine coronaviruses. !$#cross-references MUID:91272503; PMID:2053289 !$#accession C40320 !'##molecule_type genomic RNA !'##residues 1-1363 ##label ZHA !'##cross-references GB:M64669 CLASSIFICATION #superfamily coronavirus E2 glycoprotein KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-1363 #product E2 glycoprotein #status predicted #label !8E2G\ !$18-768 #product 90B glycoprotein #status predicted #label !8EGB\ !$769-1363 #product 90A glycoprotein #status predicted #label !8EGA\ !$1312-1328 #domain transmembrane #status predicted #label TMN\ !$59,133,198,359,437, !$444,649,676,696, !$714,739,788,895, !$937,1194,1224,1234, !$1253,1267,1288 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1363 #molecular-weight 150781 #checksum 7311 SEQUENCE /// ENTRY JQ2168 #type complete TITLE E2 glycoprotein precursor - human coronavirus (strain OC43) ALTERNATE_NAMES peplomer glycoprotein; S glycoprotein; spike glycoprotein CONTAINS 90A glycoprotein; 90B glycoprotein ORGANISM #formal_name human coronavirus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS JQ2168 REFERENCE JQ2168 !$#authors Mounir, S.; Talbot, P.J. !$#journal J. Gen. Virol. (1993) 74:1981-1987 !$#title Molecular characterization of the S protein gene of human !1coronavirus OC43. !$#cross-references MUID:93389458; PMID:8376972 !$#accession JQ2168 !'##molecule_type genomic RNA !'##residues 1-1353 ##label MOU !'##cross-references GB:L14643; NID:g306155; PIDN:AAA03055.1; !1PID:g306156 CLASSIFICATION #superfamily coronavirus E2 glycoprotein KEYWORDS glycoprotein; leucine zipper; transmembrane protein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-1353 #product E2 glycoprotein #status predicted #label !8E2G\ !$18-757 #product 90B glycoprotein #status predicted #label !8EGB\ !$758-1353 #product 90A glycoprotein #status predicted #label !8EGA\ !$1263-1284 #region leucine zipper motif\ !$1299-1318 #domain transmembrane #status predicted #label TMN\ !$59,133,146,202,363, !$441,496,639,666, !$686,704,729,778, !$885,927,1184,1214, !$1224,1243,1257,1278 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1353 #molecular-weight 150087 #checksum 7548 SEQUENCE /// ENTRY VHIHMJ #type complete TITLE nucleocapsid protein - murine hepatitis virus (strain JHM) ORGANISM #formal_name murine hepatitis virus, MHV DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 24-Sep-1999 ACCESSIONS A04024 REFERENCE A04024 !$#authors Skinner, M.A.; Siddell, S.G. !$#journal Nucleic Acids Res. (1983) 11:5045-5054 !$#title Coronavirus JHM: nucleotide sequence of the mRNA that !1encodes nucleocapsid protein. !$#cross-references MUID:83272950; PMID:6308569 !$#accession A04024 !'##molecule_type genomic RNA !'##residues 1-455 ##label SKI !'##cross-references GB:X00990; GB:K00757; GB:M25875; NID:g58972; !1PIDN:CAA25497.1; PID:g58973 COMMENT This genome is negative, linear, single-stranded RNA. CLASSIFICATION #superfamily coronavirus nucleocapsid protein KEYWORDS glycoprotein; nucleocapsid FEATURE !$410,423 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 455 #molecular-weight 49714 #checksum 4400 SEQUENCE /// ENTRY D45340 #type complete TITLE nucleocapsid protein - murine hepatitis virus (strain 1) ORGANISM #formal_name murine hepatitis virus, MHV DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jul-1999 ACCESSIONS D45340 REFERENCE A45340 !$#authors Parker, M.M.; Masters, P.S. !$#journal Virology (1990) 179:463-468 !$#title Sequence comparison of the N genes of five strains of the !1coronavirus mouse hepatitis virus suggests a three domain !1structure for the nucleocapsid protein. !$#cross-references MUID:91021052; PMID:2171216 !$#accession D45340 !'##molecule_type mRNA !'##residues 1-455 ##label PAR !'##cross-references GB:M35253; NID:g331813; PIDN:AAA46439.1; !1PID:g331814 GENETICS !$#gene N CLASSIFICATION #superfamily coronavirus nucleocapsid protein KEYWORDS glycoprotein; nucleocapsid FEATURE !$410,423 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 455 #molecular-weight 49694 #checksum 3822 SEQUENCE /// ENTRY A45340 #type complete TITLE nucleocapsid protein - murine hepatitis virus (strain A59) ORGANISM #formal_name murine hepatitis virus, MHV #variety strain A59 DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jul-1999 ACCESSIONS A45340; A04023; A47310 REFERENCE A45340 !$#authors Parker, M.M.; Masters, P.S. !$#journal Virology (1990) 179:463-468 !$#title Sequence comparison of the N genes of five strains of the !1coronavirus mouse hepatitis virus suggests a three domain !1structure for the nucleocapsid protein. !$#cross-references MUID:91021052; PMID:2171216 !$#accession A45340 !'##molecule_type genomic RNA !'##residues 1-454 ##label PAR !'##cross-references GB:M35256; NID:g331826; PIDN:AAA46447.1; !1PID:g331827 REFERENCE A04023 !$#authors Armstrong, J.; Smeekens, S.; Rottier, P. !$#journal Nucleic Acids Res. (1983) 11:883-891 !$#title Sequence of the nucleocapsid gene from murine coronavirus !1MHV-A59. !$#cross-references MUID:83168908; PMID:6687635 !$#accession A04023 !'##molecule_type genomic RNA !'##residues 1-108,'AVLLKHLMGSRSNYCPDGIFTILAQGPMLEPVMETALKES', !1'SGLQTAKRTPIPALILSKGTQAVMRLFLLGLRPARYCLRA', !1'FMLKALEGLHLLADLVRGHNPVGQIM',215-261,'K',263-454 ##label ARM !'##cross-references GB:X00509; GB:J02252; NID:g58965 REFERENCE A47310 !$#authors Schaad, M.C.; Baric, R.S. !$#journal Virology (1993) 196:190-198 !$#title Evidence for new transcriptional units encoded at the 3' end !1of the mouse hepatitis virus genome. !$#cross-references MUID:93362405; PMID:8395114 !$#accession A47310 !'##molecule_type mRNA !'##residues 301-454 ##label SCH !'##cross-references GB:S64884; NID:g408334; PIDN:AAB27902.1; !1PID:g408335 !'##note sequence extracted from NCBI backbone (NCBIN:136580, !1NCBIP:136581) GENETICS !$#gene N CLASSIFICATION #superfamily coronavirus nucleocapsid protein KEYWORDS glycoprotein; nucleocapsid FEATURE !$409,422 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 454 #molecular-weight 49729 #checksum 832 SEQUENCE /// ENTRY B45340 #type complete TITLE nucleocapsid protein - murine hepatitis virus (strain 3) ORGANISM #formal_name murine hepatitis virus, MHV DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jul-1999 ACCESSIONS B45340 REFERENCE A45340 !$#authors Parker, M.M.; Masters, P.S. !$#journal Virology (1990) 179:463-468 !$#title Sequence comparison of the N genes of five strains of the !1coronavirus mouse hepatitis virus suggests a three domain !1structure for the nucleocapsid protein. !$#cross-references MUID:91021052; PMID:2171216 !$#accession B45340 !'##molecule_type mRNA !'##residues 1-454 ##label PAR !'##cross-references GB:M35254; NID:g331821; PIDN:AAA46444.1; !1PID:g331822 GENETICS !$#gene N CLASSIFICATION #superfamily coronavirus nucleocapsid protein KEYWORDS glycoprotein; nucleocapsid FEATURE !$409,422 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 454 #molecular-weight 49687 #checksum 577 SEQUENCE /// ENTRY C45340 #type complete TITLE nucleocapsid protein - murine hepatitis virus (strain S) ORGANISM #formal_name murine hepatitis virus, MHV DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jul-1999 ACCESSIONS C45340 REFERENCE A45340 !$#authors Parker, M.M.; Masters, P.S. !$#journal Virology (1990) 179:463-468 !$#title Sequence comparison of the N genes of five strains of the !1coronavirus mouse hepatitis virus suggests a three domain !1structure for the nucleocapsid protein. !$#cross-references MUID:91021052; PMID:2171216 !$#accession C45340 !'##molecule_type mRNA !'##residues 1-454 ##label PAR !'##cross-references GB:M35255; NID:g331879; PIDN:AAA46468.1; !1PID:g331880 GENETICS !$#gene N CLASSIFICATION #superfamily coronavirus nucleocapsid protein KEYWORDS glycoprotein; nucleocapsid FEATURE !$409,422 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 454 #molecular-weight 49587 #checksum 9300 SEQUENCE /// ENTRY A45396 #type complete TITLE nucleocapsid protein - rat coronavirus (strain 681) ORGANISM #formal_name rat coronavirus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jun-2000 ACCESSIONS A45396 REFERENCE A45396 !$#authors Kunita, S.; Mori, M.; Terada, E. !$#journal Virology (1993) 193:520-523 !$#title Sequence analysis of the nucleocapsid protein gene of rat !1coronavirus SDAV-681. !$#cross-references MUID:93174973; PMID:8438589 !$#accession A45396 !'##molecule_type genomic RNA !'##residues 1-454 ##label KUN !'##cross-references GB:D10760; NID:g222584; PIDN:BAA01591.1; !1PID:g222585 GENETICS !$#gene N CLASSIFICATION #superfamily coronavirus nucleocapsid protein KEYWORDS glycoprotein; nucleocapsid FEATURE !$159,423 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 454 #molecular-weight 49437 #checksum 496 SEQUENCE /// ENTRY VHIHBC #type complete TITLE nucleocapsid protein - bovine coronavirus (strain Mebus) ORGANISM #formal_name bovine coronavirus DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 16-Jul-1999 ACCESSIONS B26347 REFERENCE A94357 !$#authors Lapps, W.; Hogue, B.G.; Brian, D.A. !$#journal Virology (1987) 157:47-57 !$#title Sequence analysis of the bovine coronavirus nucleocapsid and !1matrix protein genes. !$#cross-references MUID:87151119; PMID:3029965 !$#accession B26347 !'##molecule_type genomic RNA !'##residues 1-448 ##label LAP !'##cross-references GB:M16620; NID:g323354; PIDN:AAA66397.1; !1PID:g807592 GENETICS !$#gene N CLASSIFICATION #superfamily coronavirus nucleocapsid protein KEYWORDS glycoprotein; nucleocapsid FEATURE !$17,221,336,388,408, !$421 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 448 #molecular-weight 49374 #checksum 2294 SEQUENCE /// ENTRY VHIHN1 #type complete TITLE nucleocapsid protein - bovine coronavirus (strain F15) ORGANISM #formal_name bovine coronavirus DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jul-1999 ACCESSIONS S06399 REFERENCE S06399 !$#authors Cruciere, C.; Laporte, J. !$#journal Ann. Inst. Pasteur Virol. (1988) 139:123-138 !$#title Sequence and analysis of bovine enteritic coronavirus (F15) !1genome. I. - Sequence of the gene coding for the !1nucleocapsid protein; analysis of the predicted protein. !$#cross-references MUID:89087718; PMID:3207501 !$#accession S06399 !'##molecule_type genomic RNA !'##residues 1-448 ##label CRU !'##cross-references EMBL:M36656; NID:g210700; PIDN:AAA42758.1; !1PID:g210701 !'##note the source is designated as bovine enteritic coronavirus !'##note the sequence from Fig. 6 is inconsistent with that from Fig. 4 !1in lacking 33-Ser, 70-Thr, 106-Arg, 144-Gly, 181-Val, and !1218-Asn GENETICS !$#gene N CLASSIFICATION #superfamily coronavirus nucleocapsid protein KEYWORDS glycoprotein; nucleocapsid FEATURE !$17,221,336,388,408, !$421 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 448 #molecular-weight 49442 #checksum 3878 SEQUENCE /// ENTRY A60003 #type complete TITLE nucleocapsid protein - human coronavirus (strain OC43) ORGANISM #formal_name human coronavirus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 26-Feb-1999 ACCESSIONS A60003 REFERENCE A60003 !$#authors Kamahora, T.; Soe, L.H.; Lai, M.M.C. !$#journal Virus Res. (1989) 12:1-9 !$#title Sequence analysis of nucleocapsid gene and leader RNA of !1human coronavirus OC43. !$#cross-references MUID:89243809; PMID:2541577 !$#accession A60003 !'##molecule_type genomic RNA !'##residues 1-448 ##label KAM GENETICS !$#gene N CLASSIFICATION #superfamily coronavirus nucleocapsid protein KEYWORDS glycoprotein; nucleocapsid FEATURE !$17,221,336,388,408, !$421 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 448 #molecular-weight 49315 #checksum 4534 SEQUENCE /// ENTRY VHIHPC #type complete TITLE nucleocapsid protein - porcine transmissible gastroenteritis virus ORGANISM #formal_name porcine transmissible gastroenteritis virus DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 29-Oct-1999 ACCESSIONS A04025; S03936 REFERENCE A94340 !$#authors Kapke, P.A.; Brian, D.A. !$#journal Virology (1986) 151:41-49 !$#title Sequence analysis of the porcine transmissible !1gastroenteritis coronavirus nucleocapsid protein gene. !$#cross-references MUID:86181608; PMID:3008432 !$#accession A04025 !'##molecule_type genomic RNA !'##residues 1-382 ##label KAP !'##cross-references GB:M14878; NID:g335209; PIDN:AAA47915.1; !1PID:g335211 !'##experimental_source strain Purdue REFERENCE S01738 !$#authors Rasschaert, D.; Gelfi, J.; Laude, H. !$#journal Biochimie (1987) 69:591-600 !$#title Enteric coronavirus TGEV: partial sequence of the genomic !1RNA, its organization and expression. !$#cross-references MUID:88078100; PMID:2825819 !$#accession S03936 !'##molecule_type mRNA !'##residues 1-236,'W',238-375,'N',377-382 ##label RAS !'##cross-references EMBL:X06371; NID:g58995; PIDN:CAA29674.1; !1PID:g59001 !'##experimental_source strain Purdue-115 CLASSIFICATION #superfamily coronavirus nucleocapsid protein KEYWORDS glycoprotein; nucleocapsid FEATURE !$134,154,172,267,364 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 382 #molecular-weight 43422 #checksum 9027 SEQUENCE /// ENTRY S24282 #type complete TITLE nucleocapsid protein - porcine respiratory virus (strain 86/ 137004) ALTERNATE_NAMES N protein ORGANISM #formal_name porcine respiratory virus #variety strain 86/137004 DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jul-1999 ACCESSIONS S24282; S21311 REFERENCE S24279 !$#authors Britton, P.; Mawditt, K.L.; Page, K.W. !$#journal Virus Res. (1991) 21:181-198 !$#title The cloning and sequencing of the virion protein genes from !1a British isolate of porcine respiratory coronavirus: !1comparison with transmissible gastroenteritis virus genes. !$#cross-references MUID:92116634; PMID:1662846 !$#accession S24282 !'##molecule_type genomic RNA !'##residues 1-382 ##label BRI !'##cross-references EMBL:X60056; NID:g61342; PIDN:CAA42657.1; !1PID:g61346; EMBL:X55980 !'##experimental_source strain 86/137004 GENETICS !$#gene N CLASSIFICATION #superfamily coronavirus nucleocapsid protein KEYWORDS glycoprotein; nucleocapsid FEATURE !$134,154,172,267,364 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 382 #molecular-weight 43553 #checksum 8915 SEQUENCE /// ENTRY A44056 #type complete TITLE nucleocapsid protein - canine coronavirus (strain K378) ALTERNATE_NAMES N protein ORGANISM #formal_name canine coronavirus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jul-1999 ACCESSIONS A44056 REFERENCE A44056 !$#authors Vennema, H.; Rossen, J.W.A.; Wesseling, J.; Horzinek, M.C.; !1Rottier, P.J.M. !$#journal Virology (1992) 191:134-140 !$#title Genomic organization and expression of the 3' end of the !1canine and feline enteric coronaviruses. !$#cross-references MUID:93033103; PMID:1329312 !$#accession A44056 !'##molecule_type genomic RNA !'##residues 1-382 ##label VEN !'##cross-references GB:X66717; NID:g58849; PIDN:CAA47246.1; PID:g58850 GENETICS !$#gene N CLASSIFICATION #superfamily coronavirus nucleocapsid protein KEYWORDS glycoprotein; nucleocapsid FEATURE !$28,134,154,172,364 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 382 #molecular-weight 43332 #checksum 8572 SEQUENCE /// ENTRY VHIH79 #type complete TITLE nucleocapsid protein - feline infectious peritonitis virus (strain 79-1146) ORGANISM #formal_name feline infectious peritonitis virus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jul-1999 ACCESSIONS B38498 REFERENCE A38498 !$#authors Vennema, H.; De Groot, R.J.; Harbour, D.A.; Horzinek, M.C.; !1Spaan, W.J.M. !$#journal Virology (1991) 181:327-335 !$#title Primary structure of the membrane and nucleocapsid protein !1genes of feline infectious peritonitis virus and !1immunogenicity of recombinant vaccinia viruses in kittens. !$#cross-references MUID:91134997; PMID:1847259 !$#accession B38498 !'##molecule_type genomic RNA !'##residues 1-377 ##label VEN !'##cross-references EMBL:X56496; NID:g58918; PIDN:CAA39851.1; !1PID:g58920 CLASSIFICATION #superfamily coronavirus nucleocapsid protein KEYWORDS glycoprotein; nucleocapsid FEATURE !$134,154,158,172 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 377 #molecular-weight 42745 #checksum 3426 SEQUENCE /// ENTRY JQ1725 #type complete TITLE nucleocapsid protein - canine coronavirus (strain Insavc-1) ORGANISM #formal_name canine coronavirus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jun-2000 ACCESSIONS JQ1725 REFERENCE PQ0481 !$#authors Horsburgh, B.C.; Brierley, I.; Brown, T.D.K. !$#journal J. Gen. Virol. (1992) 73:2849-2862 !$#title Analysis of a 9.6 kb sequence from the 3' end of canine !1coronavirus genomic RNA. !$#cross-references MUID:93057357; PMID:1431811 !$#accession JQ1725 !'##molecule_type genomic RNA !'##residues 1-381 ##label HOR !'##cross-references DDBJ:D13096; NID:g406193; PIDN:BAA02414.1; !1PID:g406201 GENETICS !$#gene N CLASSIFICATION #superfamily coronavirus nucleocapsid protein KEYWORDS glycoprotein; nucleocapsid FEATURE !$134,172,363 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 381 #molecular-weight 43412 #checksum 6081 SEQUENCE /// ENTRY VHIH2E #type complete TITLE nucleocapsid protein - human coronavirus (strain 229E) ORGANISM #formal_name human coronavirus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS A30119; A61059 REFERENCE A30119 !$#authors Schreiber, S.S.; Kamahora, T.; Lai, M.M.C. !$#journal Virology (1989) 169:142-151 !$#title Sequence analysis of the nucleocapsid protein gene of human !1coronavirus 229E. !$#cross-references MUID:89163248; PMID:2922924 !$#accession A30119 !'##molecule_type genomic RNA !'##residues 1-389 ##label SCH !'##cross-references GB:J04419; GB:M22052; NID:g329576; PIDN:AAA45463.1; !1PID:g329577 REFERENCE A61059 !$#authors Myint, S.; Harmsen, D.; Raabe, T.; Siddell, S.G. !$#journal J. Med. Virol. (1990) 31:165-172 !$#title Characterization of a nucleic acid probe for the diagnosis !1of human coronavirus 229E infections. !$#cross-references MUID:90354818; PMID:2167350 !$#accession A61059 !'##molecule_type genomic RNA !'##residues 1-34,'P',36-114,'Y',116,'V',118-159,'R',161-174,'N', !1176-243,'MQ',246-350,'H',352-377,'V',379-389 ##label MYI CLASSIFICATION #superfamily coronavirus nucleocapsid protein KEYWORDS glycoprotein; nucleocapsid FEATURE !$169,216,260,355,362 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 389 #molecular-weight 43414 #checksum 1137 SEQUENCE /// ENTRY VHIHAI #type complete TITLE nucleocapsid protein - avian infectious bronchitis virus (strain KB8523) ORGANISM #formal_name avian infectious bronchitis virus, IBV DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS D29249 REFERENCE A29249 !$#authors Sutou, S.; Sato, S.; Okabe, T.; Nakai, M.; Sasaki, N. !$#journal Virology (1988) 165:589-595 !$#title Cloning and sequencing of genes encoding structural proteins !1of avian infectious bronchitis virus. !$#cross-references MUID:88306251; PMID:2841803 !$#accession D29249 !'##molecule_type genomic RNA !'##residues 1-409 ##label SUT !'##cross-references GB:M21515; NID:g808698; PIDN:AAA66583.1; !1PID:g331189 CLASSIFICATION #superfamily coronavirus nucleocapsid protein KEYWORDS glycoprotein; nucleocapsid FEATURE !$32 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 409 #molecular-weight 44937 #checksum 483 SEQUENCE /// ENTRY A48559 #type complete TITLE nucleocapsid protein - avian infectious bronchitis virus (strain Gray) ORGANISM #formal_name avian infectious bronchitis virus, IBV DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS A48559 REFERENCE A48559 !$#authors Williams, A.K.; Wang, L.; Sneed, L.W.; Collisson, E.W. !$#journal Virus Res. (1992) 25:213-222 !$#title Comparative analyses of the nucleocapsid genes of several !1strains of infectious bronchitis virus and other !1coronaviruses. !$#cross-references MUID:93070560; PMID:1332275 !$#accession A48559 !'##molecule_type genomic RNA !'##residues 1-409 ##label WIL !'##cross-references GB:S48137; NID:g259290; PIDN:AAB24054.1; !1PID:g259291 !'##note sequence extracted from NCBI backbone (NCBIN:117580, !1NCBIP:117581) CLASSIFICATION #superfamily coronavirus nucleocapsid protein KEYWORDS glycoprotein; nucleocapsid FEATURE !$32 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 409 #molecular-weight 45249 #checksum 2196 SEQUENCE /// ENTRY VHIHG1 #type complete TITLE nucleocapsid protein - avian infectious bronchitis virus (strain Gray) ORGANISM #formal_name avian infectious bronchitis virus, IBV DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 20-Feb-1998 ACCESSIONS A43574 REFERENCE A43574 !$#authors Collisson, E.W.; Williams, A.K.; Vonder Haar, R.; Li, W.; !1Sneed, L.W. !$#journal Adv. Exp. Med. Biol. (1990) 276:373-377 !$#title Sequence comparisons of the 3' end of the genomes of five !1strains of avian infectious bronchitis virus. !$#cross-references MUID:91353378; PMID:1966426 !$#accession A43574 !'##molecule_type genomic RNA !'##residues 1-409 ##label COL !'##cross-references GB:S55229 CLASSIFICATION #superfamily coronavirus nucleocapsid protein KEYWORDS glycoprotein; nucleocapsid FEATURE !$32 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 409 #molecular-weight 44952 #checksum 519 SEQUENCE /// ENTRY VHWVEA #type complete TITLE nucleocapsid protein (clones WV015, WV033, AV221, PB106) - equine arteritis virus ORGANISM #formal_name equine arteritis virus #note host Equus caballus (domestic horse) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS H39925; S10159; S10160 REFERENCE A39925 !$#authors Den Boon, J.A.; Snijder, E.J.; Chirnside, E.D.; De Vries, !1A.A.F.; Horzinek, M.C.; Spaan, W.J.M. !$#journal J. Virol. (1991) 65:2910-2920 !$#title Equine arteritis virus is not a togavirus but belongs to the !1coronaviruslike superfamily. !$#cross-references MUID:91237805; PMID:1851863 !$#accession H39925 !'##molecule_type genomic RNA !'##residues 1-110 ##label DEN !'##cross-references EMBL:X53459; NID:g62065; PIDN:CAA37546.1; !1PID:g62073 REFERENCE S10158 !$#authors de Vries, A.A.F.; Chirnside, E.D.; Bredenbeek, P.J.; !1Gravestein, L.A.; Horzinek, M.C.; Spaan, W.J.M. !$#journal Nucleic Acids Res. (1990) 18:3241-3247 !$#title All subgenomic mRNAs of equine arteritis virus contain a !1common leader sequence. !$#cross-references MUID:90287699; PMID:2162519 !$#accession S10159 !'##status translation not shown !'##molecule_type genomic RNA !'##residues 1-110 ##label VR1 !'##cross-references EMBL:X52275; NID:g59072; PIDN:CAA36518.1; !1PID:g59073 !$#accession S10160 !'##status translation not shown !'##molecule_type genomic RNA !'##residues 1-110 ##label VR2 !'##cross-references EMBL:X52276; NID:g59068; PIDN:CAA36519.1; !1PID:g59069 !'##experimental_source clone PB106 CLASSIFICATION #superfamily equine arteritis virus nucleocapsid protein KEYWORDS nucleocapsid SUMMARY #length 110 #molecular-weight 12300 #checksum 6780 SEQUENCE /// ENTRY MNIH32 #type complete TITLE 32K nonstructural protein - bovine coronavirus (strain Quebec) ORGANISM #formal_name bovine coronavirus DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jul-1999 ACCESSIONS A34039 REFERENCE A34039 !$#authors Cox, G.J.; Parker, M.D.; Babiuk, L.A. !$#journal Nucleic Acids Res. (1989) 17:5847 !$#title The sequence of cDNA of bovine coronavirus 32K nonstructural !1gene. !$#cross-references MUID:89345182; PMID:2762160 !$#accession A34039 !'##molecule_type genomic RNA !'##residues 1-277 ##label COX !'##cross-references EMBL:X15445; NID:g58906; PIDN:CAA33485.1; !1PID:g58907 CLASSIFICATION #superfamily bovine coronavirus 32K nonstructural protein KEYWORDS nonstructural protein SUMMARY #length 277 #molecular-weight 31896 #checksum 3792 SEQUENCE /// ENTRY MNIHMH #type complete TITLE 30K nonstructural protein - murine hepatitis virus (strain A59) ORGANISM #formal_name murine hepatitis virus, MHV DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS A31165 REFERENCE A31165 !$#authors Luytjes, W.; Bredenbeek, P.J.; Noten, A.F.H.; Horzinek, !1M.C.; Spaan, W.J.M. !$#journal Virology (1988) 166:415-422 !$#title Sequence of mouse hepatitis virus A59 mRNA 2: indications !1for RNA recombination between coronaviruses and influenza C !1virus. !$#cross-references MUID:89020808; PMID:2845655 !$#accession A31165 !'##molecule_type genomic RNA !'##residues 1-261 ##label LUY !'##cross-references GB:M23256; NID:g331829; PIDN:AAA46450.1; !1PID:g331831 CLASSIFICATION #superfamily bovine coronavirus 32K nonstructural protein KEYWORDS nonstructural protein SUMMARY #length 261 #molecular-weight 30392 #checksum 7194 SEQUENCE /// ENTRY MNIHJH #type complete TITLE 30K nonstructural protein - murine hepatitis virus (strain JHM-Wb3) ALTERNATE_NAMES NS2 protein ORGANISM #formal_name murine hepatitis virus, MHV DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jul-1999 ACCESSIONS A36542 REFERENCE A36542 !$#authors Schwarz, B.; Routledge, E.; Siddell, S.G. !$#journal J. Virol. (1990) 64:4784-4791 !$#title Murine coronavirus nonstructural protein ns2 is not !1essential for virus replication in transformed cells. !$#cross-references MUID:90376431; PMID:2168966 !$#accession A36542 !'##molecule_type genomic RNA !'##residues 1-265 ##label SCH !'##cross-references GB:M57954; NID:g308953; PIDN:AAA46463.1; !1PID:g308954 CLASSIFICATION #superfamily bovine coronavirus 32K nonstructural protein KEYWORDS nonstructural protein SUMMARY #length 265 #molecular-weight 30873 #checksum 9155 SEQUENCE /// ENTRY MNIHMS #type complete TITLE nonstructural protein NS4 - murine hepatitis virus (strain S) ORGANISM #formal_name murine hepatitis virus, MHV DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 08-Apr-1994 ACCESSIONS A40512 REFERENCE A40512 !$#authors Yokomori, K.; Lai, M.M.C. !$#journal J. Virol. (1991) 65:5605-5608 !$#title Mouse hepatitis virus S RNA sequence reveals that !1nonstructural proteins ns4 and ns5a are not essential for !1murine coronavirus replication. !$#cross-references MUID:91374624; PMID:1654456 !$#accession A40512 !'##molecule_type genomic RNA !'##residues 1-124 ##label YOK !'##cross-references GB:M64835 CLASSIFICATION #superfamily murine hepatitis virus nonstructural protein !1NS4 KEYWORDS nonstructural protein SUMMARY #length 124 #molecular-weight 13334 #checksum 3530 SEQUENCE /// ENTRY B48354 #type complete TITLE nonstructural protein 4b - murine hepatitis virus (strain A59) ORGANISM #formal_name murine hepatitis virus, MHV DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS B48354 REFERENCE A48354 !$#authors Weiss, S.R.; Zoltick, P.W.; Leibowitz, J.L. !$#journal Arch. Virol. (1993) 129:301-309 !$#title The ns4 gene of mouse hepatitis virus (MHV), strain A 59 !1contains two ORFs and thus differs from ns4 of the JHM and S !1strains. !$#cross-references MUID:93228453; PMID:8385918 !$#accession B48354 !'##molecule_type genomic RNA !'##residues 1-106 ##label WEI !'##cross-references GB:S58172; NID:g299093; PIDN:AAB26099.1; !1PID:g299095 !'##note sequence extracted from NCBI backbone (NCBIN:129089, !1NCBIP:129091) CLASSIFICATION #superfamily murine hepatitis virus nonstructural protein !1NS4 KEYWORDS nonstructural protein SUMMARY #length 106 #molecular-weight 11675 #checksum 6584 SEQUENCE /// ENTRY MNIHHC #type complete TITLE nonstructural protein 4 - human coronavirus (strain 229E) ORGANISM #formal_name human coronavirus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS A34038 REFERENCE A34038 !$#authors Raabe, T.; Siddell, S. !$#journal Nucleic Acids Res. (1989) 17:6387 !$#title Nucleotide sequence of the human coronavirus HCV 229E mRNA 4 !1and mRNA 5 unique regions. !$#cross-references MUID:89366667; PMID:2701946 !$#accession A34038 !'##molecule_type genomic RNA !'##residues 1-133 ##label RAA !'##cross-references EMBL:X15654; NID:g58921; PIDN:CAA33682.1; !1PID:g58923 CLASSIFICATION #superfamily coronavirus nonstructural protein 4 KEYWORDS nonstructural protein SUMMARY #length 133 #molecular-weight 15299 #checksum 1227 SEQUENCE /// ENTRY MNIHH2 #type complete TITLE nonstructural protein 5A - human coronavirus (strain 229E) ORGANISM #formal_name human coronavirus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS B34038 REFERENCE A34038 !$#authors Raabe, T.; Siddell, S. !$#journal Nucleic Acids Res. (1989) 17:6387 !$#title Nucleotide sequence of the human coronavirus HCV 229E mRNA 4 !1and mRNA 5 unique regions. !$#cross-references MUID:89366667; PMID:2701946 !$#accession B34038 !'##molecule_type genomic RNA !'##residues 1-88 ##label RAA !'##cross-references EMBL:X15654; NID:g58921; PIDN:CAA33683.1; !1PID:g58924 CLASSIFICATION #superfamily coronavirus nonstructural protein 5A KEYWORDS nonstructural protein SUMMARY #length 88 #molecular-weight 10223 #checksum 4131 SEQUENCE /// ENTRY MNIHH3 #type complete TITLE nonstructural protein 5B - human coronavirus (strain 229E) ORGANISM #formal_name human coronavirus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS C34038 REFERENCE A34038 !$#authors Raabe, T.; Siddell, S. !$#journal Nucleic Acids Res. (1989) 17:6387 !$#title Nucleotide sequence of the human coronavirus HCV 229E mRNA 4 !1and mRNA 5 unique regions. !$#cross-references MUID:89366667; PMID:2701946 !$#accession C34038 !'##molecule_type genomic RNA !'##residues 1-77 ##label RAA !'##cross-references EMBL:X15654; NID:g58921; PIDN:CAA33684.1; !1PID:g58925 CLASSIFICATION #superfamily coronavirus nonstructural protein 5B KEYWORDS nonstructural protein SUMMARY #length 77 #molecular-weight 9098 #checksum 3043 SEQUENCE /// ENTRY MNIHB2 #type complete TITLE nonstructural protein NS2 - bovine coronavirus ORGANISM #formal_name bovine coronavirus DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Jul-1999 ACCESSIONS S08408; C46346 REFERENCE S08408 !$#authors Woloszyn, N.; Boireau, P.; Laporte, J. !$#journal Nucleic Acids Res. (1990) 18:1303 !$#title Nucleotide sequence of the bovine enteric coronavirus BECV !1F15 mRNA 5 and mRNA 6 unique regions. !$#cross-references MUID:90206809; PMID:2320429 !$#accession S08408 !'##molecule_type mRNA !'##residues 1-109 ##label WOL !'##cross-references EMBL:X51347; NID:g58684; PIDN:CAA35740.1; !1PID:g58685 !'##experimental_source strain F15 !'##note the source is designated as bovine enteric coronavirus REFERENCE A46346 !$#authors Abraham, S.; Kienzle, T.E.; Lapps, W.E.; Brian, D.A. !$#journal Virology (1990) 177:488-495 !$#title Sequence and expression analysis of potential nonstructural !1proteins of 4.9, 4.8, 12.7, and 9.5 kDa encoded between the !1spike and membrane protein genes of the bovine coronavirus. !$#cross-references MUID:90320120; PMID:2142556 !$#accession C46346 !'##molecule_type genomic RNA !'##residues 1-109 ##label ABR !'##cross-references GB:M31054; NID:g323363; PIDN:AAA42913.1; !1PID:g323367 !'##experimental_source strain Mebus CLASSIFICATION #superfamily bovine coronavirus nonstructural protein NS2 KEYWORDS nonstructural protein SUMMARY #length 109 #molecular-weight 12806 #checksum 2083 SEQUENCE /// ENTRY A44275 #type complete TITLE nonstructural protein NS2 - human coronavirus (strain OC43) ORGANISM #formal_name human coronavirus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS A44275 REFERENCE A44275 !$#authors Mounir, S.; Talbot, P.J. !$#journal Virology (1993) 192:355-360 !$#title Human coronavirus OC43 RNA 4 lacks two open reading frames !1located downstream of the S gene of bovine coronavirus. !$#cross-references MUID:93297129; PMID:8517026 !$#accession A44275 !'##molecule_type mRNA !'##residues 1-109 ##label MOU !'##cross-references GB:M99576; NID:g329567; PIDN:AAA02569.1; !1PID:g329568 CLASSIFICATION #superfamily bovine coronavirus nonstructural protein NS2 KEYWORDS nonstructural protein SUMMARY #length 109 #molecular-weight 12935 #checksum 1613 SEQUENCE /// ENTRY MNIHB3 #type complete TITLE nonstructural protein NS3 - bovine coronavirus (strain F15) ORGANISM #formal_name bovine coronavirus DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Jul-1999 ACCESSIONS S08409 REFERENCE S08408 !$#authors Woloszyn, N.; Boireau, P.; Laporte, J. !$#journal Nucleic Acids Res. (1990) 18:1303 !$#title Nucleotide sequence of the bovine enteric coronavirus BECV !1F15 mRNA 5 and mRNA 6 unique regions. !$#cross-references MUID:90206809; PMID:2320429 !$#accession S08409 !'##molecule_type mRNA !'##residues 1-84 ##label WOL !'##cross-references EMBL:X51347; NID:g58684; PIDN:CAA35741.1; !1PID:g58686 !'##note the source is designated as bovine enteric coronavirus CLASSIFICATION #superfamily bovine coronavirus nonstructural protein NS3 KEYWORDS nonstructural protein SUMMARY #length 84 #molecular-weight 9584 #checksum 5519 SEQUENCE /// ENTRY D46346 #type complete TITLE nonstructural protein NS3 - bovine coronavirus (strain Mebus) ORGANISM #formal_name bovine coronavirus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS D46346 REFERENCE A46346 !$#authors Abraham, S.; Kienzle, T.E.; Lapps, W.E.; Brian, D.A. !$#journal Virology (1990) 177:488-495 !$#title Sequence and expression analysis of potential nonstructural !1proteins of 4.9, 4.8, 12.7, and 9.5 kDa encoded between the !1spike and membrane protein genes of the bovine coronavirus. !$#cross-references MUID:90320120; PMID:2142556 !$#accession D46346 !'##molecule_type genomic RNA !'##residues 1-84 ##label ABR !'##cross-references GB:M31054; NID:g323363; PIDN:AAA42914.1; !1PID:g323368 CLASSIFICATION #superfamily bovine coronavirus nonstructural protein NS3 KEYWORDS nonstructural protein SUMMARY #length 84 #molecular-weight 9542 #checksum 4724 SEQUENCE /// ENTRY B44275 #type complete TITLE nonstructural protein NS3 - human coronavirus (strain OC43) ORGANISM #formal_name human coronavirus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS B44275 REFERENCE A44275 !$#authors Mounir, S.; Talbot, P.J. !$#journal Virology (1993) 192:355-360 !$#title Human coronavirus OC43 RNA 4 lacks two open reading frames !1located downstream of the S gene of bovine coronavirus. !$#cross-references MUID:93297129; PMID:8517026 !$#accession B44275 !'##molecule_type mRNA !'##residues 1-84 ##label MOU !'##cross-references GB:M99576; NID:g329567; PIDN:AAA02570.1; !1PID:g329569 CLASSIFICATION #superfamily bovine coronavirus nonstructural protein NS3 KEYWORDS nonstructural protein SUMMARY #length 84 #molecular-weight 9538 #checksum 5886 SEQUENCE /// ENTRY MNIHM5 #type complete TITLE nonstructural protein NS5 - murine hepatitis virus (strain S) ORGANISM #formal_name murine hepatitis virus, MHV DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 08-Apr-1994 ACCESSIONS B40512 REFERENCE A40512 !$#authors Yokomori, K.; Lai, M.M.C. !$#journal J. Virol. (1991) 65:5605-5608 !$#title Mouse hepatitis virus S RNA sequence reveals that !1nonstructural proteins ns4 and ns5a are not essential for !1murine coronavirus replication. !$#cross-references MUID:91374624; PMID:1654456 !$#accession B40512 !'##molecule_type genomic RNA !'##residues 1-88 ##label YOK !'##cross-references GB:M64835 CLASSIFICATION #superfamily bovine coronavirus nonstructural protein NS3 KEYWORDS nonstructural protein SUMMARY #length 88 #molecular-weight 10111 #checksum 5871 SEQUENCE /// ENTRY QQIHBC #type complete TITLE hypothetical protein (gene N internal ORF) - bovine coronavirus (strain Mebus) ALTERNATE_NAMES IORF protein ORGANISM #formal_name bovine coronavirus DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 16-Jul-1999 ACCESSIONS C26347 REFERENCE A94357 !$#authors Lapps, W.; Hogue, B.G.; Brian, D.A. !$#journal Virology (1987) 157:47-57 !$#title Sequence analysis of the bovine coronavirus nucleocapsid and !1matrix protein genes. !$#cross-references MUID:87151119; PMID:3029965 !$#accession C26347 !'##molecule_type genomic RNA !'##residues 1-207 ##label LAP !'##cross-references GB:M16620; NID:g323354; PIDN:AAA66398.1; !1PID:g807593 CLASSIFICATION #superfamily coronavirus gene N internal ORF SUMMARY #length 207 #molecular-weight 23054 #checksum 2457 SEQUENCE /// ENTRY JQ1174 #type complete TITLE hypothetical protein (gene N internal ORF) - turkey coronavirus ALTERNATE_NAMES IORF protein ORGANISM #formal_name turkey coronavirus DATE 17-Jul-1998 #sequence_revision 17-Jul-1998 #text_change 17-Jul-1998 ACCESSIONS JQ1174 REFERENCE JQ1172 !$#authors Verbeek, A.; Tijssen, P. !$#journal J. Gen. Virol. (1991) 72:1659-1666 !$#title Sequence analysis of the turkey enteric coronavirus !1nucleocapsid and membrane protein genes: a close genomic !1relationship with bovine coronavirus. !$#cross-references MUID:91311418; PMID:1856695 !$#accession JQ1174 !'##molecule_type genomic RNA !'##residues 1-207 ##label VER !'##experimental_source strain Minnesota COMMENT The gene encoding this protein is located within the !1nucleocapsid (N) gene. CLASSIFICATION #superfamily coronavirus gene N internal ORF SUMMARY #length 207 #molecular-weight 23005 #checksum 2094 SEQUENCE /// ENTRY S06869 #type complete TITLE hypothetical protein (gene N internal ORF) - bovine coronavirus (strain F15) ALTERNATE_NAMES IORF protein ORGANISM #formal_name bovine coronavirus DATE 17-Jul-1998 #sequence_revision 17-Jul-1998 #text_change 16-Jul-1999 ACCESSIONS S06869 REFERENCE S06399 !$#authors Cruciere, C.; Laporte, J. !$#journal Ann. Inst. Pasteur Virol. (1988) 139:123-138 !$#title Sequence and analysis of bovine enteritic coronavirus (F15) !1genome. I. - Sequence of the gene coding for the !1nucleocapsid protein; analysis of the predicted protein. !$#cross-references MUID:89087718; PMID:3207501 !$#accession S06869 !'##molecule_type genomic RNA !'##residues 1-207 ##label CRU !'##cross-references EMBL:M36656; NID:g210700; PIDN:AAA42759.1; !1PID:g210702 !'##note the source is designated as bovine enteritic coronavirus COMMENT The gene encoding this protein is located within the !1nucleocapsid (N) gene. CLASSIFICATION #superfamily coronavirus gene N internal ORF SUMMARY #length 207 #molecular-weight 23001 #checksum 1368 SEQUENCE /// ENTRY F45340 #type complete TITLE hypothetical protein (gene N internal ORF) - murine hepatitis virus (strain 3) ALTERNATE_NAMES IORF protein ORGANISM #formal_name murine hepatitis virus, MHV DATE 17-Jul-1998 #sequence_revision 17-Jul-1998 #text_change 16-Jul-1999 ACCESSIONS F45340 REFERENCE A45340 !$#authors Parker, M.M.; Masters, P.S. !$#journal Virology (1990) 179:463-468 !$#title Sequence comparison of the N genes of five strains of the !1coronavirus mouse hepatitis virus suggests a three domain !1structure for the nucleocapsid protein. !$#cross-references MUID:91021052; PMID:2171216 !$#accession F45340 !'##molecule_type mRNA !'##residues 1-207 ##label PAR !'##cross-references GB:M35254; NID:g331821; PIDN:AAA46445.1; !1PID:g331823 COMMENT The gene encoding this protein is located within the !1nucleocapsid (N) gene. CLASSIFICATION #superfamily coronavirus gene N internal ORF SUMMARY #length 207 #molecular-weight 22616 #checksum 9236 SEQUENCE /// ENTRY E45340 #type complete TITLE hypothetical protein (gene N internal ORF) - murine hepatitis virus (strain A59) ALTERNATE_NAMES IORF protein ORGANISM #formal_name murine hepatitis virus, MHV DATE 17-Jul-1998 #sequence_revision 17-Jul-1998 #text_change 16-Jul-1999 ACCESSIONS E45340 REFERENCE A45340 !$#authors Parker, M.M.; Masters, P.S. !$#journal Virology (1990) 179:463-468 !$#title Sequence comparison of the N genes of five strains of the !1coronavirus mouse hepatitis virus suggests a three domain !1structure for the nucleocapsid protein. !$#cross-references MUID:91021052; PMID:2171216 !$#accession E45340 !'##molecule_type mRNA !'##residues 1-207 ##label PAR !'##cross-references GB:M35256; NID:g331826; PIDN:AAA46448.1; !1PID:g331828 COMMENT The gene encoding this protein is located within the !1nucleocapsid (N) gene. CLASSIFICATION #superfamily coronavirus gene N internal ORF SUMMARY #length 207 #molecular-weight 22586 #checksum 9440 SEQUENCE /// ENTRY H45340 #type complete TITLE hypothetical protein (gene N internal ORF) - murine hepatitis virus (strain 1) ALTERNATE_NAMES IORF protein ORGANISM #formal_name murine hepatitis virus, MHV DATE 17-Jul-1998 #sequence_revision 17-Jul-1998 #text_change 16-Jul-1999 ACCESSIONS H45340 REFERENCE A45340 !$#authors Parker, M.M.; Masters, P.S. !$#journal Virology (1990) 179:463-468 !$#title Sequence comparison of the N genes of five strains of the !1coronavirus mouse hepatitis virus suggests a three domain !1structure for the nucleocapsid protein. !$#cross-references MUID:91021052; PMID:2171216 !$#accession H45340 !'##molecule_type mRNA !'##residues 1-207 ##label PAR !'##cross-references GB:M35253; NID:g331813; PIDN:AAA46440.1; !1PID:g331815 COMMENT The gene encoding this protein is located within the !1nucleocapsid (N) gene. CLASSIFICATION #superfamily coronavirus gene N internal ORF SUMMARY #length 207 #molecular-weight 22888 #checksum 161 SEQUENCE /// ENTRY G45340 #type complete TITLE hypothetical protein (gene N internal ORF) - murine hepatitis virus (strain S) ALTERNATE_NAMES IORF protein ORGANISM #formal_name murine hepatitis virus, MHV DATE 17-Jul-1998 #sequence_revision 17-Jul-1998 #text_change 16-Jul-1999 ACCESSIONS G45340 REFERENCE A45340 !$#authors Parker, M.M.; Masters, P.S. !$#journal Virology (1990) 179:463-468 !$#title Sequence comparison of the N genes of five strains of the !1coronavirus mouse hepatitis virus suggests a three domain !1structure for the nucleocapsid protein. !$#cross-references MUID:91021052; PMID:2171216 !$#accession G45340 !'##molecule_type mRNA !'##residues 1-207 ##label PAR !'##cross-references GB:M35255; NID:g331879; PIDN:AAA46469.1; !1PID:g331881 COMMENT The gene encoding this protein is located within the !1nucleocapsid (N) gene. CLASSIFICATION #superfamily coronavirus gene N internal ORF SUMMARY #length 207 #molecular-weight 22901 #checksum 421 SEQUENCE /// ENTRY VHNZ1 #type complete TITLE nucleocapsid protein (version 1) - human respiratory syncytial virus ORGANISM #formal_name human respiratory syncytial virus DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 16-Jul-1999 ACCESSIONS A23316 REFERENCE A23316 !$#authors Collins, P.L.; Anderson, K.; Langer, S.J.; Wertz, G.W. !$#journal Virology (1985) 146:69-77 !$#title Correct sequence for the major nucleocapsid protein mRNA of !1respiratory syncytial virus. !$#cross-references MUID:85301974; PMID:3839952 !$#accession A23316 !'##molecule_type mRNA !'##residues 1-391 ##label COL !'##cross-references GB:M11486; GB:K01459; GB:K02719; GB:K03348; !1GB:K03349; GB:M11217; GB:M11244; GB:M11487; GB:M11505; !1GB:M11514; GB:M11631; GB:M12966; GB:X00001; GB:X02221; !1NID:g333925; PIDN:AAB59852.1; PID:g333928 !'##note the authors translated the codon GGA for residue 143 as Ala GENETICS !$#gene N CLASSIFICATION #superfamily respiratory syncytial virus nucleocapsid !1protein KEYWORDS nucleocapsid SUMMARY #length 391 #molecular-weight 43451 #checksum 3758 SEQUENCE /// ENTRY VHNZ #type complete TITLE nucleocapsid protein (version 2) - human respiratory syncytial virus ORGANISM #formal_name human respiratory syncytial virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS A04026 REFERENCE A04026 !$#authors Elango, N.; Venkatesan, S. !$#journal Nucleic Acids Res. (1983) 11:5941-5951 !$#title Amino acid sequence of respiratory syncytial virus capsid !1protein. !$#cross-references MUID:83299261; PMID:6310521 !$#accession A04026 !'##molecule_type mRNA !'##residues 1-467 ##label ELA !'##cross-references GB:X00001; NID:g61215; PIDN:CAA24906.1; PID:g61216 GENETICS !$#gene N CLASSIFICATION #superfamily respiratory syncytial virus nucleocapsid !1protein KEYWORDS nucleocapsid SUMMARY #length 467 #molecular-weight 51534 #checksum 7871 SEQUENCE /// ENTRY VHNZ3 #type complete TITLE nucleocapsid protein - human respiratory syncytial virus (strain 18537) ALTERNATE_NAMES nucleoprotein ORGANISM #formal_name human respiratory syncytial virus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jun-2000 ACCESSIONS C32063 REFERENCE A32063 !$#authors Johnson, P.R.; Collins, P.L. !$#journal J. Gen. Virol. (1989) 70:1539-1547 !$#title The 1B (NS2), 1C (NS1) and N proteins of human respiratory !1syncytial virus (RSV) of antigenic subgroups A and B: !1sequence conservation and divergence within RSV genomic RNA. !$#cross-references MUID:89279331; PMID:2525176 !$#accession C32063 !'##molecule_type mRNA !'##residues 1-391 ##label JOH !'##cross-references EMBL:D00736; NID:g222559; PIDN:BAA00637.1; !1PID:g222562 GENETICS !$#gene N CLASSIFICATION #superfamily respiratory syncytial virus nucleocapsid !1protein KEYWORDS nucleocapsid; nucleoprotein SUMMARY #length 391 #molecular-weight 43415 #checksum 4272 SEQUENCE /// ENTRY VHNZB4 #type complete TITLE nucleocapsid protein - bovine respiratory syncytial virus (strain A51908) ALTERNATE_NAMES nucleoprotein ORGANISM #formal_name bovine respiratory syncytial virus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS A38525 REFERENCE A38525 !$#authors Samal, S.K.; Zamora, M.; McPhillips, T.H.; Mohanty, S.B. !$#journal Virology (1991) 180:453-456 !$#title Molecular cloning and sequence analysis of bovine !1respiratory syncytial virus mRNA encoding the major !1nucleocapsid protein. !$#cross-references MUID:91082446; PMID:1984667 !$#accession A38525 !'##molecule_type mRNA !'##residues 1-391 ##label SAM !'##cross-references GB:M35076; NID:g210834; PIDN:AAA42812.1; !1PID:g210835 CLASSIFICATION #superfamily respiratory syncytial virus nucleocapsid !1protein KEYWORDS nucleocapsid; nucleoprotein SUMMARY #length 391 #molecular-weight 43445 #checksum 8060 SEQUENCE /// ENTRY JQ1533 #type complete TITLE nucleocapsid protein - bovine respiratory syncytial virus (strain 391-2) ALTERNATE_NAMES nucleoprotein ORGANISM #formal_name bovine respiratory syncytial virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS JQ1533 REFERENCE JQ1533 !$#authors Amann, V.L.; Lerch, R.A.; Anderson, K.; Wertz, G.W. !$#journal J. Gen. Virol. (1992) 73:999-1003 !$#title Bovine respiratory syncytial virus nucleocapsid protein: !1mRNA sequence analysis and expression from recombinant !1vaccinia virus vectors. !$#cross-references MUID:92341085; PMID:1634882 !$#accession JQ1533 !'##molecule_type mRNA !'##residues 1-391 ##label AMA !'##cross-references GB:S40504; NID:g251865; PIDN:AAB22601.1; !1PID:g251866 GENETICS !$#gene N CLASSIFICATION #superfamily respiratory syncytial virus nucleocapsid !1protein KEYWORDS nucleocapsid; nucleoprotein SUMMARY #length 391 #molecular-weight 43557 #checksum 7467 SEQUENCE /// ENTRY VHNZPM #type complete TITLE nucleocapsid protein - pneumonia virus of mice ALTERNATE_NAMES nucleoprotein ORGANISM #formal_name pneumonia virus of mice DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jun-2000 ACCESSIONS A38474 REFERENCE A38474 !$#authors Barr, J.; Chambers, P.; Pringle, C.R.; Easton, A.J. !$#journal J. Gen. Virol. (1991) 72:677-685 !$#title Sequence of the major nucleocapsid protein gene of pneumonia !1virus of mice: sequence comparisons suggest structural !1homology between nucleocapsid proteins of pneumoviruses, !1paramyxoviruses, rhabdoviruses and filoviruses. !$#cross-references MUID:91170952; PMID:1848602 !$#accession A38474 !'##molecule_type genomic RNA !'##residues 1-393 ##label BAR !'##cross-references GB:D10331; GB:D01100; NID:g222336; PIDN:BAA01177.1; !1PID:g222339 GENETICS !$#gene N CLASSIFICATION #superfamily respiratory syncytial virus nucleocapsid !1protein KEYWORDS nucleocapsid; nucleoprotein SUMMARY #length 393 #molecular-weight 43135 #checksum 4102 SEQUENCE /// ENTRY VHNZMV #type complete TITLE nucleocapsid protein - measles virus ORGANISM #formal_name measles virus DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 16-Jul-1999 ACCESSIONS A04027 REFERENCE A93006 !$#authors Rozenblatt, S.; Eizenberg, O.; Ben-Levy, R.; Lavie, V.; !1Bellini, W.J. !$#journal J. Virol. (1985) 53:684-690 !$#title Sequence homology within the morbilliviruses. !$#cross-references MUID:85108164; PMID:3838193 !$#accession A04027 !'##molecule_type genomic RNA !'##residues 1-523 ##label ROZ !'##cross-references GB:X01999; GB:M10297; NID:g60926; PIDN:CAA26031.1; !1PID:g60927 CLASSIFICATION #superfamily paramyxovirus nucleocapsid protein KEYWORDS nucleocapsid SUMMARY #length 523 #molecular-weight 58104 #checksum 3046 SEQUENCE /// ENTRY A48556 #type complete TITLE nucleocapsid protein - measles virus (strain AIK-C) ALTERNATE_NAMES nucleoprotein ORGANISM #formal_name measles virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS A48556 REFERENCE A48556 !$#authors Mori, T.; Sasaki, K.; Hashimoto, H.; Makino, S. !$#journal Virus Genes (1993) 7:67-81 !$#title Molecular cloning and complete nucleotide sequence of !1genomic RNA of the AIK-C strain of attenuated measles virus. !$#cross-references MUID:93227570; PMID:8470368 !$#accession A48556 !'##molecule_type genomic RNA !'##residues 1-525 ##label MOR !'##cross-references GB:S58435; NID:g299460; PIDN:AAB26141.1; !1PID:g299461 !'##note sequence extracted from NCBI backbone (NCBIN:129264, !1NCBIP:129267) GENETICS !$#gene NP CLASSIFICATION #superfamily paramyxovirus nucleocapsid protein KEYWORDS nucleocapsid; nucleoprotein SUMMARY #length 525 #molecular-weight 58131 #checksum 1123 SEQUENCE /// ENTRY VHNZMH #type complete TITLE nucleocapsid protein - measles virus (strain Halle) ALTERNATE_NAMES nucleoprotein ORGANISM #formal_name measles virus #variety strain Halle DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS A34040; S03685 REFERENCE A34040 !$#authors Buckland, R.; Gerald, C.; Barker, D.; Wild, F. !$#journal Nucleic Acids Res. (1988) 16:11821 !$#title Cloning and sequencing of the nucleoprotein gene of measles !1virus (Halle strain). !$#cross-references MUID:89098336; PMID:3211755 !$#accession A34040 !'##molecule_type mRNA !'##residues 1-525 ##label BUC !'##cross-references GB:X13480; NID:g60991; PIDN:CAA31831.1; PID:g60992 !'##experimental_source strain Halle CLASSIFICATION #superfamily paramyxovirus nucleocapsid protein KEYWORDS nucleocapsid; nucleoprotein SUMMARY #length 525 #molecular-weight 58159 #checksum 1428 SEQUENCE /// ENTRY JU0272 #type complete TITLE nucleocapsid protein - subacute sclerosing panencephalitis virus (strain Yamagata-1) ALTERNATE_NAMES nucleoprotein ORGANISM #formal_name subacute sclerosing panencephalitis virus, SSPEV DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jun-2000 ACCESSIONS JU0272 REFERENCE JU0272 !$#authors Komase, K.; Kasaoka, T.; Yoshikawa, Y.; Sato, T.A.; !1Yamanouchi, K. !$#journal Virus Genes (1990) 4:137-149 !$#title Molecular analysis of structural protein genes of the !1Yamagata-1 strain of defective subacute sclerosing !1panencephalitis virus. I. Nucleotide sequence of the !1nucleoprotein gene. !$#cross-references MUID:90385699; PMID:1698325 !$#accession JU0272 !'##molecule_type mRNA !'##residues 1-525 ##label KOM !'##cross-references GB:D10550; NID:g222262; PIDN:BAA01407.1; !1PID:g222263 GENETICS !$#gene N CLASSIFICATION #superfamily paramyxovirus nucleocapsid protein KEYWORDS nucleocapsid; nucleoprotein SUMMARY #length 525 #molecular-weight 58417 #checksum 1270 SEQUENCE /// ENTRY VHNZCV #type fragment TITLE nucleocapsid protein - canine distemper virus (fragment) ORGANISM #formal_name canine distemper virus DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 14-Nov-1997 ACCESSIONS A04028 REFERENCE A93006 !$#authors Rozenblatt, S.; Eizenberg, O.; Ben-Levy, R.; Lavie, V.; !1Bellini, W.J. !$#journal J. Virol. (1985) 53:684-690 !$#title Sequence homology within the morbilliviruses. !$#cross-references MUID:85108164; PMID:3838193 !$#accession A04028 !'##molecule_type genomic RNA !'##residues 1-514 ##label ROZ !'##cross-references GB:M10242; NID:g323245 !'##note the codons given for residues 54-Lys (AAU) and 55-Ile (GUC) are !1inconsistent with the authors' translation CLASSIFICATION #superfamily paramyxovirus nucleocapsid protein KEYWORDS nucleocapsid SUMMARY #length 514 #checksum 3877 SEQUENCE /// ENTRY VHNZMY #type complete TITLE nucleocapsid protein - mumps virus (strain Miyahara) ORGANISM #formal_name mumps virus DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS A35314 REFERENCE A35314 !$#authors Tanabayashi, K.; Takeuchi, K.; Hishiyama, M.; Yamada, A.; !1Tsurudome, M.; Ito, Y.; Sugiura, A. !$#journal Virology (1990) 177:124-130 !$#title Nucleotide sequence of the leader and nucleocapsid protein !1gene of mumps virus and epitope mapping with the in vitro !1expressed nucleocapsid protein. !$#cross-references MUID:90281575; PMID:1693800 !$#accession A35314 !'##molecule_type genomic RNA !'##residues 1-549 ##label TAN !'##cross-references GB:M37750; NID:g332279; PIDN:AAA46619.1; !1PID:g332280 GENETICS !$#gene NP CLASSIFICATION #superfamily paramyxovirus nucleocapsid protein KEYWORDS nucleocapsid SUMMARY #length 549 #molecular-weight 61366 #checksum 3785 SEQUENCE /// ENTRY VHNZSB #type complete TITLE nucleocapsid protein - mumps virus (strain SBL-1) ALTERNATE_NAMES nucleoprotein ORGANISM #formal_name mumps virus DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS A42759 REFERENCE A42759 !$#authors Elango, N. !$#journal Virus Res. (1989) 12:77-86 !$#title The mumps virus nucleocapsid mRNA sequence and homology !1among the Paramyxoviridae proteins. !$#cross-references MUID:89243816; PMID:2718626 !$#accession A42759 !'##molecule_type mRNA !'##residues 1-553 ##label ELA !'##cross-references GB:X57997; NID:g60578; PIDN:CAA41061.1; PID:g60579 GENETICS !$#gene NP CLASSIFICATION #superfamily paramyxovirus nucleocapsid protein KEYWORDS nucleocapsid; nucleoprotein SUMMARY #length 553 #molecular-weight 61786 #checksum 1127 SEQUENCE /// ENTRY VHNZP2 #type complete TITLE nucleocapsid protein - parainfluenza virus type 2 (strain Toshiba) ALTERNATE_NAMES nucleoprotein ORGANISM #formal_name parainfluenza virus type 2 DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jul-1999 ACCESSIONS A36420; S16659 REFERENCE A36420 !$#authors Yuasa, T.; Bando, H.; Kawano, M.; Tsurudome, M.; Nishio, M.; !1Kondo, K.; Komada, H.; Ito, Y. !$#journal Virology (1990) 179:777-784 !$#title Sequence analyses of the 3' genome end and NP gene of human !1parainfluenza type 2 virus: sequence variation of the !1gene-starting signal and the conserved 3' end. !$#cross-references MUID:91049444; PMID:2173261 !$#accession A36420 !'##molecule_type genomic RNA !'##residues 1-542 ##label YUA !'##cross-references GB:M55320; GB:M62624; NID:g332736; PIDN:AAA46865.1; !1PID:g332737 !'##experimental_source strain Toshiba REFERENCE S16659 !$#authors Kawano, M.; Okamoto, K.; Bando, H.; Kondo, K.; Tsurudome, !1M.; Komada, H.; Nishio, M.; Ito, Y. !$#journal Nucleic Acids Res. (1991) 19:2739-2746 !$#title Characterizations of the human parainfluenza type 2 virus !1gene encoding the L protein and the intergenic sequences. !$#cross-references MUID:91252221; PMID:1645865 !$#accession S16659 !'##molecule_type genomic RNA !'##residues 1-542 ##label KAW !'##cross-references EMBL:X57559; NID:g61985; PIDN:CAA40783.1; !1PID:g61986 !'##experimental_source strain Toshiba CLASSIFICATION #superfamily paramyxovirus nucleocapsid protein KEYWORDS nucleocapsid; nucleoprotein SUMMARY #length 542 #molecular-weight 61120 #checksum 626 SEQUENCE /// ENTRY VHNZSV #type complete TITLE nucleocapsid protein - Sendai virus (strain Z) ORGANISM #formal_name Sendai virus DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 24-Jul-1997 ACCESSIONS A04029 REFERENCE A00726 !$#authors Shioda, T.; Hidaka, Y.; Kanda, T.; Shibuta, H.; Nomoto, A.; !1Iwasaki, K. !$#journal Nucleic Acids Res. (1983) 11:7317-7330 !$#title Sequence of 3,687 nucleotides from the 3' end of Sendai !1virus genome RNA and the predicted amino acid sequences of !1viral NP, P and C proteins. !$#cross-references MUID:84069769; PMID:6316257 !$#accession A04029 !'##molecule_type genomic RNA !'##residues 1-524 ##label SHI GENETICS !$#gene NP CLASSIFICATION #superfamily paramyxovirus nucleocapsid protein KEYWORDS nucleocapsid SUMMARY #length 524 #molecular-weight 57081 #checksum 3279 SEQUENCE /// ENTRY VHNZT1 #type complete TITLE nucleocapsid protein - parainfluenza virus type 1 ALTERNATE_NAMES nucleoprotein ORGANISM #formal_name parainfluenza virus type 1 DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jun-2000 ACCESSIONS A38401 REFERENCE A38401 !$#authors Lyn, D.; Gill, D.S.; Scroggs, R.A.; Portner, A. !$#journal J. Gen. Virol. (1991) 72:983-987 !$#title The nucleoproteins of human parainfluenza virus type 1 and !1Sendai virus share amino acid sequences and antigenic and !1structural determinants. !$#cross-references MUID:91202138; PMID:1707951 !$#accession A38401 !'##molecule_type mRNA !'##residues 1-524 ##label LYN !'##cross-references GB:D01070; NID:g222271; PIDN:BAA00873.1; !1PID:g222272 CLASSIFICATION #superfamily paramyxovirus nucleocapsid protein KEYWORDS nucleocapsid; nucleoprotein SUMMARY #length 524 #molecular-weight 57544 #checksum 5730 SEQUENCE /// ENTRY VHNZP1 #type complete TITLE nucleocapsid protein (clone 4-31) - parainfluenza virus type 1 ALTERNATE_NAMES nucleoprotein ORGANISM #formal_name parainfluenza virus type 1 DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 24-Jul-1997 ACCESSIONS A38501 REFERENCE A38501 !$#authors Matsuoka, Y.; Ray, R. !$#journal Virology (1991) 181:403-407 !$#title Sequence analysis and expression of the human parainfluenza !1type 1 virus nucleoprotein gene. !$#cross-references MUID:91135013; PMID:1847263 !$#accession A38501 !'##molecule_type mRNA !'##residues 1-524 ##label MAT !'##cross-references EMBL:M36051 CLASSIFICATION #superfamily paramyxovirus nucleocapsid protein KEYWORDS nucleocapsid; nucleoprotein SUMMARY #length 524 #molecular-weight 57534 #checksum 6322 SEQUENCE /// ENTRY A48341 #type complete TITLE nucleocapsid protein - parainfluenza virus type 1 (strains A1426, 86-315, 62M-753) ALTERNATE_NAMES nucleoprotein ORGANISM #formal_name parainfluenza virus type 1 DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS A48341 REFERENCE A48341 !$#authors Miyahara, K.; Kitada, S.; Yoshimoto, M.; Matsumura, H.; !1Kawano, M.; Komada, H.; Tsurudome, M.; Kusagawa, S.; Nishio, !1M.; Ito, Y. !$#journal Arch. Virol. (1992) 124:255-268 !$#title Molecular evolution of human paramyxoviruses. Nucleotide !1sequence analyses of the human parainfluenza type 1 virus NP !1and M protein genes and construction of phylogenetic trees !1for all the human paramyxoviruses. !$#cross-references MUID:92296894; PMID:1605738 !$#accession A48341 !'##molecule_type genomic RNA !'##residues 1-524 ##label MIY !'##cross-references GB:S38060; NID:g250340; PIDN:AAB22343.1; !1PID:g250341 !'##note sequence extracted from NCBI backbone (NCBIN:106078, !1NCBIP:106079) GENETICS !$#gene NP CLASSIFICATION #superfamily paramyxovirus nucleocapsid protein KEYWORDS nucleocapsid; nucleoprotein SUMMARY #length 524 #molecular-weight 57736 #checksum 7060 SEQUENCE /// ENTRY VHNZP3 #type complete TITLE nucleocapsid protein - parainfluenza virus type 3 ORGANISM #formal_name parainfluenza virus type 3 #note host Homo sapiens (man) DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jun-2000 ACCESSIONS A24285; A27009 REFERENCE A94341 !$#authors Sanchez, A.; Banerjee, A.K.; Furuichi, Y.; Richardson, M.A. !$#journal Virology (1986) 152:171-180 !$#title Conserved structures among the nucleocapsid proteins of the !1paramyxoviridae: complete nucleotide sequence of human !1parainfluenza virus type 3 NP mRNA. !$#cross-references MUID:86237101; PMID:3012866 !$#accession A24285 !'##molecule_type mRNA !'##residues 1-515 ##label SAN !'##cross-references GB:D10025; GB:D00027; NID:g3327816; !1PIDN:BAA00915.1; PID:g222276 REFERENCE A92792 !$#authors Jambou, R.C.; Elango, N.; Venkatesan, S.; Collins, P.L. !$#journal J. Gen. Virol. (1986) 67:2543-2548 !$#title Complete sequence of the major nucleocapsid protein gene of !1human parainfluenza type 3 virus: comparison with other !1negative strand viruses. !$#cross-references MUID:87059780; PMID:2878059 !$#accession A27009 !'##molecule_type mRNA !'##residues 1-515 ##label JAM !'##cross-references GB:X04612; NID:g60905; PIDN:CAA28282.1; PID:g60906 CLASSIFICATION #superfamily paramyxovirus nucleocapsid protein KEYWORDS nucleocapsid SUMMARY #length 515 #molecular-weight 57827 #checksum 575 SEQUENCE /// ENTRY VHNZB3 #type complete TITLE nucleocapsid protein - parainfluenza virus type 3 ORGANISM #formal_name parainfluenza virus type 3 DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 16-Jul-1999 ACCESSIONS A27502 REFERENCE A93658 !$#authors Sakai, Y.; Suzu, S.; Shioda, T.; Shibuta, H. !$#journal Nucleic Acids Res. (1987) 15:2927-2944 !$#title Nucleotide sequence of the bovine parainfluenza 3 virus !1genome: its 3' end and the genes of NP, P, C and M proteins. !$#cross-references MUID:87174818; PMID:3031614 !$#accession A27502 !'##molecule_type genomic RNA !'##residues 1-515 ##label SAK !'##cross-references EMBL:Y00114; NID:g60891; PIDN:CAA68293.1; !1PID:g60892 GENETICS !$#gene NP CLASSIFICATION #superfamily paramyxovirus nucleocapsid protein KEYWORDS nucleocapsid SUMMARY #length 515 #molecular-weight 57354 #checksum 3990 SEQUENCE /// ENTRY VHNZ4A #type complete TITLE nucleocapsid protein - parainfluenza virus type 4A (strain Toshiba) ORGANISM #formal_name parainfluenza virus type 4A DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS A33772 REFERENCE A33772 !$#authors Kondo, K.; Bando, H.; Kawano, M.; Tsurudome, M.; Komada, H.; !1Nishio, M.; Ito, Y. !$#journal Virology (1990) 174:1-8 !$#title Sequencing analyses and comparison of parainfluenza virus !1type 4A and 4B NP protein genes. !$#cross-references MUID:90101365; PMID:2152988 !$#accession A33772 !'##molecule_type mRNA !'##residues 1-551 ##label KON !'##cross-references GB:M32982; NID:g332581; PIDN:AAA46801.1; !1PID:g332582 GENETICS !$#gene NP CLASSIFICATION #superfamily paramyxovirus nucleocapsid protein KEYWORDS nucleocapsid SUMMARY #length 551 #molecular-weight 62561 #checksum 1381 SEQUENCE /// ENTRY VHNZ4B #type complete TITLE nucleocapsid protein - parainfluenza virus type 4B (strain 68-333) ORGANISM #formal_name parainfluenza virus type 4B DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS B33772 REFERENCE A33772 !$#authors Kondo, K.; Bando, H.; Kawano, M.; Tsurudome, M.; Komada, H.; !1Nishio, M.; Ito, Y. !$#journal Virology (1990) 174:1-8 !$#title Sequencing analyses and comparison of parainfluenza virus !1type 4A and 4B NP protein genes. !$#cross-references MUID:90101365; PMID:2152988 !$#accession B33772 !'##molecule_type mRNA !'##residues 1-551 ##label KON !'##cross-references GB:M32983; NID:g332583; PIDN:AAA46802.1; !1PID:g332584 GENETICS !$#gene NP CLASSIFICATION #superfamily paramyxovirus nucleocapsid protein KEYWORDS nucleocapsid SUMMARY #length 551 #molecular-weight 62425 #checksum 3444 SEQUENCE /// ENTRY VHIWEB #type complete TITLE nucleocapsid protein - Ebola virus (subtype Zaire, strain Mayinga) ALTERNATE_NAMES major nucleoprotein ORGANISM #formal_name Ebola virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS A31471 REFERENCE A31471 !$#authors Sanchez, A.; Kiley, M.P.; Holloway, B.P.; McCormick, J.B.; !1Auperin, D.D. !$#journal Virology (1989) 170:81-91 !$#title The nucleoprotein gene of Ebola virus: Cloning, sequencing, !1and in vitro expression. !$#cross-references MUID:89243211; PMID:2718390 !$#accession A31471 !'##molecule_type genomic RNA !'##residues 1-739 ##label SAN !'##cross-references GB:J04337; NID:g323686; PIDN:AAA42977.1; !1PID:g323687 GENETICS !$#gene NP CLASSIFICATION #superfamily filovirus nucleocapsid protein KEYWORDS nucleocapsid SUMMARY #length 739 #molecular-weight 83279 #checksum 6009 SEQUENCE /// ENTRY VHIWMV #type complete TITLE nucleocapsid protein - Marburg virus ALTERNATE_NAMES major nucleoprotein ORGANISM #formal_name Marburg virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS JQ1408 REFERENCE JQ1408 !$#authors Sanchez, A.; Kiley, M.P.; Klenk, H.D.; Feldmann, H. !$#journal J. Gen. Virol. (1992) 73:347-357 !$#title Sequence analysis of the Marburg virus nucleoprotein gene: !1comparison to Ebola virus and other non-segmented !1negative-strand RNA viruses. !$#cross-references MUID:92166742; PMID:1538192 !$#accession JQ1408 !'##molecule_type mRNA !'##residues 1-695 ##label SAN !'##cross-references GB:M72714; NID:g332180; PIDN:AAA46563.1; !1PID:g332181 GENETICS !$#gene NP CLASSIFICATION #superfamily filovirus nucleocapsid protein KEYWORDS nucleocapsid SUMMARY #length 695 #molecular-weight 77861 #checksum 9530 SEQUENCE /// ENTRY VHWJBV #type complete TITLE nucleocapsid protein - Berne virus (strain P138/72) ORGANISM #formal_name Berne virus DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jun-2000 ACCESSIONS A33613 REFERENCE A33613 !$#authors Snijder, E.J.; Den Boon, J.A.; Spaan, W.J.M.; Verjans, !1G.M.G.M.; Horzinek, M.C. !$#journal J. Gen. Virol. (1989) 70:3363-3370 !$#title Identification and primary structure of the gene encoding !1the Berne virus nucleocapsid protein. !$#cross-references MUID:90111714; PMID:2607340 !$#accession A33613 !'##molecule_type genomic RNA !'##residues 1-160 ##label SNI !'##cross-references GB:D00563; NID:g221066; PIDN:BAA00437.1; !1PID:g221067 GENETICS !$#gene N CLASSIFICATION #superfamily Berne virus nucleocapsid protein KEYWORDS nucleocapsid SUMMARY #length 160 #molecular-weight 18289 #checksum 1380 SEQUENCE /// ENTRY VGWJBV #type complete TITLE peplomer glycoprotein precursor - Berne virus (strain P138/ 72) ORGANISM #formal_name Berne virus DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS A36759 REFERENCE A36759 !$#authors Snijder, E.J.; Den Boon, J.A.; Spaan, W.J.M.; Weiss, M.; !1Horzinek, M.C. !$#journal Virology (1990) 178:355-363 !$#title Primary structure and post-translational processing of the !1Berne virus peplomer protein. !$#cross-references MUID:91020973; PMID:2219698 !$#accession A36759 !'##molecule_type genomic RNA !'##residues 1-1581 ##label SNI !'##cross-references GB:X52506; NID:g62059; PIDN:CAA36748.1; PID:g62060 GENETICS !$#gene P CLASSIFICATION #superfamily Berne virus peplomer glycoprotein KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-1581 #product peplomer glycoprotein #status predicted !8#label PGP\ !$1547-1572 #domain transmembrane #status predicted #label TMN\ !$25,310,384,494,574, !$935,969,1267,1297, !$1327,1385,1389, !$1428,1431,1438, !$1483,1487,1495,1515 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1581 #molecular-weight 178331 #checksum 7631 SEQUENCE /// ENTRY RRNZSV #type complete TITLE polymerase-associated nucleocapsid phosphoprotein - Sendai virus (strain Z) ORGANISM #formal_name Sendai virus DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 16-Jul-1999 ACCESSIONS A00726 REFERENCE A00726 !$#authors Shioda, T.; Hidaka, Y.; Kanda, T.; Shibuta, H.; Nomoto, A.; !1Iwasaki, K. !$#journal Nucleic Acids Res. (1983) 11:7317-7330 !$#title Sequence of 3,687 nucleotides from the 3' end of Sendai !1virus genome RNA and the predicted amino acid sequences of !1viral NP, P and C proteins. !$#cross-references MUID:84069769; PMID:6316257 !$#accession A00726 !'##molecule_type genomic RNA !'##residues 1-568 ##label SHI !'##cross-references GB:X00087; NID:g60928; PIDN:CAA24946.1; PID:g60930 COMMENT This protein may be a component of the active polymerase. GENETICS !$#gene P CLASSIFICATION #superfamily parainfluenza virus polymerase-associated !1nucleocapsid phosphoprotein KEYWORDS nucleocapsid; phosphoprotein SUMMARY #length 568 #molecular-weight 62026 #checksum 2795 SEQUENCE /// ENTRY RRNZHS #type complete TITLE polymerase-associated nucleocapsid phosphoprotein - Sendai virus (strain Harris) ORGANISM #formal_name Sendai virus DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 24-Jul-1997 ACCESSIONS A28985 REFERENCE A28985 !$#authors Giorgi, C.; Blumberg, B.M.; Kolakofsky, D. !$#journal Cell (1983) 35:829-836 !$#title Sendai virus contains overlapping genes expressed from a !1single mRNA. !$#cross-references MUID:84082108; PMID:6317203 !$#accession A28985 !'##molecule_type mRNA !'##residues 1-568 ##label GIO GENETICS !$#gene P CLASSIFICATION #superfamily parainfluenza virus polymerase-associated !1nucleocapsid phosphoprotein KEYWORDS nucleocapsid; phosphoprotein SUMMARY #length 568 #molecular-weight 62004 #checksum 2527 SEQUENCE /// ENTRY RRNZSF #type complete TITLE polymerase-associated nucleocapsid phosphoprotein - Sendai virus (strain Fushimi) ORGANISM #formal_name Sendai virus DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Jul-1999 ACCESSIONS S06922 REFERENCE S06922 !$#authors Neubert, W.J. !$#journal Nucleic Acids Res. (1989) 17:10101 !$#title Cloning and sequencing of the polymerase gene (P) of Sendai !1virus (strain Fushimi). !$#cross-references MUID:90098777; PMID:2557576 !$#accession S06922 !'##molecule_type mRNA !'##residues 1-568 ##label NEU !'##cross-references GB:X17008; NID:g62011; PIDN:CAA34871.1; PID:g62012 GENETICS !$#gene P CLASSIFICATION #superfamily parainfluenza virus polymerase-associated !1nucleocapsid phosphoprotein KEYWORDS nucleocapsid; phosphoprotein SUMMARY #length 568 #molecular-weight 62032 #checksum 2173 SEQUENCE /// ENTRY RRNZS6 #type complete TITLE polymerase-associated nucleocapsid phosphoprotein - Sendai virus (strain 6/94) ORGANISM #formal_name Sendai virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS S06923 REFERENCE S06923 !$#authors Homann, H.E.; Neubert, W.J. !$#journal Nucleic Acids Res. (1989) 17:10102 !$#title Cloning and sequencing of the polymerase gene (P) of Sendai !1virus (strain 6/94). !$#cross-references MUID:90098778; PMID:2557577 !$#accession S06923 !'##molecule_type mRNA !'##residues 1-568 ##label HOM !'##cross-references GB:X17007; NID:g62006; PIDN:CAA34867.1; PID:g62007 GENETICS !$#gene P CLASSIFICATION #superfamily parainfluenza virus polymerase-associated !1nucleocapsid phosphoprotein KEYWORDS nucleocapsid; phosphoprotein SUMMARY #length 568 #molecular-weight 62177 #checksum 1757 SEQUENCE /// ENTRY RRNZ39 #type complete TITLE polymerase-associated nucleocapsid phosphoprotein - parainfluenza virus type 1 (strain C39) ORGANISM #formal_name parainfluenza virus type 1 DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS A39929 REFERENCE A39929 !$#authors Matsuoka, Y.; Curran, J.; Pelet, T.; Kolakofsky, D.; Ray, !1R.; Compans, R.W. !$#journal J. Virol. (1991) 65:3406-3410 !$#title The P gene of human parainfluenza virus type 1 encodes P and !1C proteins but not a cysteine-rich V protein. !$#cross-references MUID:91237868; PMID:1851888 !$#accession A39929 !'##molecule_type mRNA !'##residues 1-568 ##label MAT !'##cross-references GB:M37792; NID:g332741; PIDN:AAA46868.1; !1PID:g332742 CLASSIFICATION #superfamily parainfluenza virus polymerase-associated !1nucleocapsid phosphoprotein KEYWORDS nucleocapsid; phosphoprotein SUMMARY #length 568 #molecular-weight 64660 #checksum 5014 SEQUENCE /// ENTRY RRNZ35 #type complete TITLE polymerase-associated nucleocapsid phosphoprotein - parainfluenza virus type 1 (strain C35) ORGANISM #formal_name parainfluenza virus type 1 DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 24-Jul-1997 ACCESSIONS A40234 REFERENCE A40234 !$#authors Power, U.F.; Ryan, K.W.; Portner, A. !$#journal Virology (1992) 189:340-343 !$#title The P genes of human parainfluenza virus type 1 clinical !1isolates are polycistronic and microheterogeneous. !$#cross-references MUID:92295573; PMID:1318610 !$#accession A40234 !'##molecule_type genomic RNA !'##residues 1-568 ##label POW !'##cross-references GB:M74081 CLASSIFICATION #superfamily parainfluenza virus polymerase-associated !1nucleocapsid phosphoprotein KEYWORDS nucleocapsid; phosphoprotein SUMMARY #length 568 #molecular-weight 64685 #checksum 4167 SEQUENCE /// ENTRY RRNZ73 #type complete TITLE polymerase-associated nucleocapsid phosphoprotein - parainfluenza virus type 1 (strain CI-5/73) ORGANISM #formal_name parainfluenza virus type 1 DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 24-Jul-1997 ACCESSIONS C40234 REFERENCE A40234 !$#authors Power, U.F.; Ryan, K.W.; Portner, A. !$#journal Virology (1992) 189:340-343 !$#title The P genes of human parainfluenza virus type 1 clinical !1isolates are polycistronic and microheterogeneous. !$#cross-references MUID:92295573; PMID:1318610 !$#accession C40234 !'##molecule_type genomic RNA !'##residues 1-568 ##label POW !'##cross-references GB:M74082 CLASSIFICATION #superfamily parainfluenza virus polymerase-associated !1nucleocapsid phosphoprotein KEYWORDS nucleocapsid; phosphoprotein SUMMARY #length 568 #molecular-weight 64675 #checksum 8468 SEQUENCE /// ENTRY RRNZ83 #type complete TITLE polymerase-associated nucleocapsid phosphoprotein - parainfluenza virus type 1 (strain CI-14/83) ORGANISM #formal_name parainfluenza virus type 1 DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS E40234 REFERENCE A40234 !$#authors Power, U.F.; Ryan, K.W.; Portner, A. !$#journal Virology (1992) 189:340-343 !$#title The P genes of human parainfluenza virus type 1 clinical !1isolates are polycistronic and microheterogeneous. !$#cross-references MUID:92295573; PMID:1318610 !$#accession E40234 !'##molecule_type genomic RNA !'##residues 1-568 ##label POW !'##cross-references GB:M74080; NID:g332679; PIDN:AAA46830.1; !1PID:g332681 CLASSIFICATION #superfamily parainfluenza virus polymerase-associated !1nucleocapsid phosphoprotein KEYWORDS nucleocapsid; phosphoprotein SUMMARY #length 568 #molecular-weight 64585 #checksum 6630 SEQUENCE /// ENTRY RRNZP3 #type complete TITLE polymerase-associated nucleocapsid phosphoprotein - parainfluenza virus type 3 (strain 47885) ORGANISM #formal_name parainfluenza virus type 3 #note host Homo sapiens (man) DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 24-Jul-1997 ACCESSIONS A27010 REFERENCE A92793 !$#authors Spriggs, M.K.; Collins, P.L. !$#journal J. Gen. Virol. (1986) 67:2705-2719 !$#title Sequence analysis of the P and C protein genes of human !1parainfluenza virus type 3: patterns of amino acid sequence !1homology among paramyxovirus proteins. !$#cross-references MUID:87085488; PMID:3025346 !$#accession A27010 !'##molecule_type mRNA !'##residues 1-602 ##label SPR COMMENT This protein may be a component of the active polymerase. GENETICS !$#gene P CLASSIFICATION #superfamily parainfluenza virus polymerase-associated !1nucleocapsid phosphoprotein KEYWORDS nucleocapsid; phosphoprotein SUMMARY #length 602 #molecular-weight 67564 #checksum 5701 SEQUENCE /// ENTRY RRNZP4 #type complete TITLE polymerase-associated nucleocapsid phosphoprotein (version 1) - parainfluenza virus type 3 ORGANISM #formal_name parainfluenza virus type 3 #note host Homo sapiens (man) DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 24-Jul-1997 ACCESSIONS A94355; A24189 REFERENCE A94355 !$#authors Luk, D.; Sanchez, A.; Banerjee, A.K. !$#journal Virology (1987) 156:193-194 !$#contents erratum !$#accession A94355 !'##molecule_type mRNA !'##residues 1-604 ##label LU1 !'##cross-references GB:M14890 REFERENCE A94343 !$#authors Luk, D.; Sanchez, A.; Banerjee, A.K. !$#journal Virology (1986) 153:318-325 !$#title Messenger RNA encoding the phosphoprotein (P) gene of human !1parainfluenza virus 3 is bicistronic. !$#cross-references MUID:86291173; PMID:3016995 !$#accession A24189 !'##molecule_type mRNA !'##residues 1-603,'AKDQIKKTTPNK' ##label LU2 !'##note this sequence has been corrected in reference A94355 COMMENT This protein may be a component of the active polymerase. GENETICS !$#gene P CLASSIFICATION #superfamily parainfluenza virus polymerase-associated !1nucleocapsid phosphoprotein KEYWORDS nucleocapsid; phosphoprotein SUMMARY #length 604 #molecular-weight 67661 #checksum 579 SEQUENCE /// ENTRY RRNZP5 #type complete TITLE polymerase-associated nucleocapsid phosphoprotein (version 2) - parainfluenza virus type 3 ORGANISM #formal_name parainfluenza virus type 3 #note host Homo sapiens (man) DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 24-Jul-1997 ACCESSIONS A26896 REFERENCE A94348 !$#authors Galinski, M.S.; Mink, M.A.; Lambert, D.M.; Wechsler, S.L.; !1Pons, M.W. !$#journal Virology (1986) 155:46-60 !$#title Molecular cloning and sequence analysis of the human !1parainfluenza 3 virus mRNA encoding the P and C proteins. !$#cross-references MUID:87044104; PMID:3022477 !$#accession A26896 !'##molecule_type mRNA !'##residues 1-603 ##label GAL COMMENT The RNA sequence was obtained from GenBank, release 52.0. COMMENT This protein may be a component of the active polymerase. GENETICS !$#gene P CLASSIFICATION #superfamily parainfluenza virus polymerase-associated !1nucleocapsid phosphoprotein KEYWORDS nucleocapsid; phosphoprotein SUMMARY #length 603 #molecular-weight 67654 #checksum 9312 SEQUENCE /// ENTRY RRNZB3 #type complete TITLE polymerase-associated nucleocapsid phosphoprotein - parainfluenza virus type 3 ORGANISM #formal_name parainfluenza virus type 3 DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 16-Jul-1999 ACCESSIONS B27502 REFERENCE A93658 !$#authors Sakai, Y.; Suzu, S.; Shioda, T.; Shibuta, H. !$#journal Nucleic Acids Res. (1987) 15:2927-2944 !$#title Nucleotide sequence of the bovine parainfluenza 3 virus !1genome: its 3' end and the genes of NP, P, C and M proteins. !$#cross-references MUID:87174818; PMID:3031614 !$#accession B27502 !'##molecule_type genomic RNA !'##residues 1-596 ##label SAK !'##cross-references EMBL:Y00114; NID:g60891; PIDN:CAA68294.1; !1PID:g60893 COMMENT This protein may be a component of the active polymerase. GENETICS !$#gene P CLASSIFICATION #superfamily parainfluenza virus polymerase-associated !1nucleocapsid phosphoprotein KEYWORDS nucleocapsid; phosphoprotein SUMMARY #length 596 #molecular-weight 66409 #checksum 1913 SEQUENCE /// ENTRY RRNZSP #type complete TITLE polymerase-associated nucleocapsid phosphoprotein - simian paramyxovirus SV5 (strain W3) ALTERNATE_NAMES P protein; phosphoprotein P ORGANISM #formal_name simian paramyxovirus SV5 DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 24-Jul-1997 ACCESSIONS B31594 REFERENCE A90902 !$#authors Thomas, S.M.; Lamb, R.A.; Paterson, R.G. !$#journal Cell (1988) 54:891-902 !$#title Two mRNAs that differ by two nontemplated nucleotides encode !1the amino coterminal proteins P and V of the paramyxovirus !1SV5. !$#cross-references MUID:88311091; PMID:3044614 !$#accession B31594 !'##molecule_type mRNA; genomic RNA !'##residues 1-392 ##label THO !'##cross-references GB:J03142 COMMENT Protein P is encoded by the gene for protein V; during mRNA !1synthesis, a nontemplated addition of two G's produces a !1two-base shift in the reading frame. As a result, the !1sequence of residues 1-164 is identical in both proteins, !1whereas the carboxyl-terminal regions are different. GENETICS !$#gene V CLASSIFICATION #superfamily simian paramyxovirus P protein; V/P protein !1homology KEYWORDS alternative splicing; nucleocapsid; phosphoprotein; RNA !1editing FEATURE !$1-164 #domain V/P protein homology #label VPN SUMMARY #length 392 #molecular-weight 42106 #checksum 8912 SEQUENCE /// ENTRY RRNZVT #type complete TITLE polymerase-associated nucleocapsid phosphoprotein - parainfluenza virus type 2 (strain Toshiba) ALTERNATE_NAMES P protein; phosphoprotein P ORGANISM #formal_name parainfluenza virus type 2 DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 24-Jul-1997 ACCESSIONS B35313 REFERENCE A35313 !$#authors Ohgimoto, S.; Bando, H.; Kawano, M.; Okamoto, K.; Kondo, K.; !1Tsurudome, M.; Nishio, M.; Ito, Y. !$#journal Virology (1990) 177:116-123 !$#title Sequence analysis of P gene of human parainfluenza type 2 !1virus: P and cysteine-rich proteins are translated by two !1mRNAs that differ by two nontemplated G residues. !$#cross-references MUID:90281574; PMID:2162103 !$#accession B35313 !'##molecule_type mRNA; genomic RNA !'##residues 1-395 ##label OHG !'##cross-references GB:M37751 COMMENT Protein P is encoded by the gene for protein V; during mRNA !1synthesis, a nontemplated addition of two G's produces a !1two-base shift in the reading frame. As a result, the !1sequence of residues 1-163 is identical in both proteins, !1whereas the carboxyl-terminal regions are different. GENETICS !$#gene V CLASSIFICATION #superfamily simian paramyxovirus P protein; V/P protein !1homology KEYWORDS nucleocapsid; phosphoprotein; RNA editing FEATURE !$1-163 #domain V/P protein homology #label VPN SUMMARY #length 395 #molecular-weight 42152 #checksum 5833 SEQUENCE /// ENTRY RRNZP2 #type complete TITLE polymerase-associated nucleocapsid phosphoprotein - parainfluenza virus type 2 ALTERNATE_NAMES P protein; phosphoprotein P ORGANISM #formal_name parainfluenza virus type 2 DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 24-Jul-1997 ACCESSIONS B35322 REFERENCE A35322 !$#authors Southern, J.A.; Precious, B.; Randall, R.E. !$#journal Virology (1990) 177:388-390 !$#title Two nontemplated nucleotide additions are required to !1generate the P mRNA of parainfluenza virus type 2 since the !1RNA genome encodes protein V. !$#cross-references MUID:90281608; PMID:2162111 !$#accession B35322 !'##molecule_type genomic RNA !'##residues 1-395 ##label SOU !'##cross-references GB:M37748 COMMENT Protein P is encoded by the gene for protein V; during mRNA !1synthesis, a nontemplated addition of two G's produces a !1two-base shift in the reading frame. As a result, the !1sequence of residues 1-163 is identical in both proteins, !1whereas the carboxyl-terminal regions are different. GENETICS !$#gene V CLASSIFICATION #superfamily simian paramyxovirus P protein; V/P protein !1homology KEYWORDS alternative splicing; nucleocapsid; phosphoprotein; RNA !1editing FEATURE !$1-163 #domain V/P protein homology #label VPN SUMMARY #length 395 #molecular-weight 42027 #checksum 4610 SEQUENCE /// ENTRY A43685 #type complete TITLE polymerase-associated nucleocapsid phosphoprotein - parainfluenza virus type 4A (strain Toshiba) ALTERNATE_NAMES P protein; phosphoprotein P ORGANISM #formal_name parainfluenza virus type 4A DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jul-1999 ACCESSIONS A43685 REFERENCE A43685 !$#authors Kondo, K.; Bando, H.; Tsurudome, M.; Kawano, M.; Nishio, M.; !1Ito, Y. !$#journal Virology (1990) 178:321-326 !$#title Sequence analysis of the phosphoprotein (P) genes of human !1parainfluenza type 4A and 4B viruses and RNA editing at !1transcript of the P genes: the number of G residues added is !1imprecise. !$#cross-references MUID:90357784; PMID:2167560 !$#accession A43685 !'##molecule_type mRNA !'##residues 1-399 ##label KON !'##cross-references GB:M55975; NID:g332587; PIDN:AAA46804.1; !1PID:g332588 GENETICS !$#gene P !$#introns 153/3 CLASSIFICATION #superfamily simian paramyxovirus P protein; V/P protein !1homology KEYWORDS alternative splicing; nucleocapsid; phosphoprotein; RNA !1editing FEATURE !$1-153 #domain V/P protein homology #label VPN SUMMARY #length 399 #molecular-weight 44068 #checksum 6654 SEQUENCE /// ENTRY C43685 #type complete TITLE polymerase-associated nucleocapsid phosphoprotein - parainfluenza virus type 4B (strain 68-333) ALTERNATE_NAMES P protein; phosphoprotein P ORGANISM #formal_name parainfluenza virus type 4B DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jul-1999 ACCESSIONS C43685 REFERENCE A43685 !$#authors Kondo, K.; Bando, H.; Tsurudome, M.; Kawano, M.; Nishio, M.; !1Ito, Y. !$#journal Virology (1990) 178:321-326 !$#title Sequence analysis of the phosphoprotein (P) genes of human !1parainfluenza type 4A and 4B viruses and RNA editing at !1transcript of the P genes: the number of G residues added is !1imprecise. !$#cross-references MUID:90357784; PMID:2167560 !$#accession C43685 !'##molecule_type mRNA !'##residues 1-399 ##label KON !'##cross-references GB:M55975 GENETICS !$#gene P !$#introns 153/3 CLASSIFICATION #superfamily simian paramyxovirus P protein; V/P protein !1homology KEYWORDS alternative splicing; nucleocapsid; phosphoprotein; RNA !1editing FEATURE !$1-153 #domain V/P protein homology #label VPN SUMMARY #length 399 #molecular-weight 44135 #checksum 8430 SEQUENCE /// ENTRY RRNZYA #type complete TITLE polymerase-associated nucleocapsid phosphoprotein - mumps virus (strain Miyahara) ALTERNATE_NAMES P protein; phosphoprotein P ORGANISM #formal_name mumps virus DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jun-2000 ACCESSIONS JU0066 REFERENCE JU0066 !$#authors Takeuchi, K.; Hishiyama, M.; Yamada, A.; Sugiura, A. !$#journal J. Gen. Virol. (1988) 69:2043-2049 !$#title Molecular cloning and sequence analysis of the mumps virus !1gene encoding the P protein: mumps virus P gene is !1monocistronic. !$#cross-references MUID:88299965; PMID:3404121 !$#accession JU0066 !'##molecule_type genomic RNA !'##residues 1-391 ##label TAK !'##cross-references GB:D00352; NID:g222147; PIDN:BAA00260.1; !1PID:g222148 COMMENT Protein P is encoded by the gene for protein V; during mRNA !1synthesis, a nontemplated addition of two G's produces a !1two-base shift in the reading frame. As a result, the !1sequence of residues 1-155 is identical in both proteins, !1whereas the carboxyl-terminal regions are different. GENETICS !$#gene V CLASSIFICATION #superfamily simian paramyxovirus P protein; V/P protein !1homology KEYWORDS alternative splicing; nucleocapsid; phosphoprotein; RNA !1editing FEATURE !$1-155 #domain V/P protein homology #label VPN SUMMARY #length 391 #molecular-weight 41587 #checksum 1202 SEQUENCE /// ENTRY RRNZED #type complete TITLE polymerase-associated nucleocapsid phosphoprotein - mumps virus (strain Enders) ALTERNATE_NAMES P protein; phosphoprotein P ORGANISM #formal_name mumps virus DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jun-2000 ACCESSIONS JU0067 REFERENCE JU0066 !$#authors Takeuchi, K.; Hishiyama, M.; Yamada, A.; Sugiura, A. !$#journal J. Gen. Virol. (1988) 69:2043-2049 !$#title Molecular cloning and sequence analysis of the mumps virus !1gene encoding the P protein: mumps virus P gene is !1monocistronic. !$#cross-references MUID:88299965; PMID:3404121 !$#accession JU0067 !'##molecule_type genomic RNA !'##residues 1-391 ##label TAK !'##cross-references GB:D00351; NID:g222141; PIDN:BAA00259.1; !1PID:g222142 COMMENT Protein P is encoded by the gene for protein V; during mRNA !1synthesis, a nontemplated addition of two G's produces a !1two-base shift in the reading frame. As a result, the !1sequence of residues 1-155 is identical in both proteins, !1whereas the carboxyl-terminal regions are different. GENETICS !$#gene V CLASSIFICATION #superfamily simian paramyxovirus P protein; V/P protein !1homology KEYWORDS alternative splicing; nucleocapsid; phosphoprotein; RNA !1editing FEATURE !$1-155 #domain V/P protein homology #label VPN SUMMARY #length 391 #molecular-weight 41650 #checksum 504 SEQUENCE /// ENTRY RRNZMS #type complete TITLE polymerase-associated nucleocapsid phosphoprotein - mumps virus (strain SBL-1) ALTERNATE_NAMES P protein; phosphoprotein P ORGANISM #formal_name mumps virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS A30118 REFERENCE A30118 !$#authors Elango, N.; Koevamees, J.; Norrby, E. !$#journal Virology (1989) 169:62-67 !$#title Sequence analysis of the mumps virus mRNA encoding the P !1protein. !$#cross-references MUID:89163268; PMID:2922928 !$#accession A30118 !'##molecule_type mRNA !'##residues 1-390 ##label ELA !'##cross-references GB:M24731; NID:g537590; PIDN:AAA74752.1; !1PID:g537591 COMMENT Protein P is encoded by the gene for protein V; during mRNA !1synthesis, a nontemplated addition of two G's produces a !1two-base shift in the reading frame. As a result, the !1sequence of residues 1-155 is identical in both proteins, !1whereas the carboxyl-terminal regions are different. GENETICS !$#gene V CLASSIFICATION #superfamily simian paramyxovirus P protein; V/P protein !1homology KEYWORDS alternative splicing; nucleocapsid; phosphoprotein; RNA !1editing FEATURE !$1-155 #domain V/P protein homology #label VPN SUMMARY #length 390 #molecular-weight 41569 #checksum 7032 SEQUENCE /// ENTRY RRNZND #type complete TITLE polymerase-associated nucleocapsid phosphoprotein - Newcastle disease virus (strain Australia-Victoria) ALTERNATE_NAMES P protein; phosphoprotein P CONTAINS 29K nonstructural protein C; 38K nonstructural protein C ORGANISM #formal_name Newcastle disease virus DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jul-1999 ACCESSIONS A28613 REFERENCE A28613 !$#authors McGinnes, L.; McQuain, C.; Morrison, T. !$#journal Virology (1988) 164:256-264 !$#title The P protein and the nonstructural 38K and 29K proteins of !1Newcastle disease virus are derived from the same open !1reading frame. !$#cross-references MUID:88206073; PMID:3363866 !$#accession A28613 !'##molecule_type mRNA !'##residues 1-395 ##label MCG !'##cross-references GB:M20302; NID:g332373; PIDN:AAA66628.1; !1PID:g332374 GENETICS !$#gene P/C CLASSIFICATION #superfamily simian paramyxovirus P protein; V/P protein !1homology KEYWORDS nucleocapsid; phosphoprotein FEATURE !$82-395 #product 38K nonstructural protein C #status !8predicted #label NP1\ !$120-395 #product 29K nonstructural protein C #status !8predicted #label NP2 SUMMARY #length 395 #molecular-weight 42129 #checksum 8300 SEQUENCE /// ENTRY RRNZ #type complete TITLE phosphoprotein P - human respiratory syncytial virus (strain A2) ORGANISM #formal_name human respiratory syncytial virus DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 16-Jul-1999 ACCESSIONS A04037 REFERENCE A04037 !$#authors Satake, M.; Elango, N.; Venkatesan, S. !$#journal J. Virol. (1984) 52:991-994 !$#title Sequence analysis of the respiratory syncytial virus !1phosphoprotein gene. !$#cross-references MUID:85033973; PMID:6548527 !$#accession A04037 !'##molecule_type mRNA !'##residues 1-241 ##label SAT !'##cross-references GB:M11486; GB:K02719; NID:g333925; PIDN:AAB59853.1; !1PID:g333929 GENETICS !$#gene P CLASSIFICATION #superfamily respiratory syncytial virus phosphoprotein P KEYWORDS phosphoprotein SUMMARY #length 241 #molecular-weight 27148 #checksum 8036 SEQUENCE /// ENTRY RRNZPP #type complete TITLE phosphoprotein P - human respiratory syncytial virus (strain Long) ORGANISM #formal_name human respiratory syncytial virus DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jul-1999 ACCESSIONS S07428 REFERENCE S07428 !$#authors Lopez, J.A.; Villanueva, N.; Melero, J.A.; Portela, A. !$#journal Virus Res. (1988) 10:249-262 !$#title Nucleotide sequence of the fusion and phosphoprotein genes !1of human respiratory syncytial (RS) virus Long strain: !1evidence of subtype genetic heterogeneity. !$#cross-references MUID:88323192; PMID:3414184 !$#accession S07428 !'##molecule_type mRNA !'##residues 1-241 ##label LOP !'##cross-references EMBL:M22644; NID:g333949; PIDN:AAA47415.1; !1PID:g333950 GENETICS !$#gene P CLASSIFICATION #superfamily respiratory syncytial virus phosphoprotein P KEYWORDS phosphoprotein SUMMARY #length 241 #molecular-weight 27147 #checksum 8808 SEQUENCE /// ENTRY RRNZ18 #type complete TITLE phosphoprotein P - human respiratory syncytial virus (strain 18537) ORGANISM #formal_name human respiratory syncytial virus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jun-2000 ACCESSIONS A34150 REFERENCE A34150 !$#authors Johnson, P.R.; Collins, P.L. !$#journal J. Gen. Virol. (1990) 71:481-485 !$#title Sequence comparison of the phosphoprotein mRNAs of antigenic !1subgroups A and B of human respiratory syncytial virus !1identifies a highly divergent domain in the predicted !1protein. !$#cross-references MUID:90171937; PMID:2307966 !$#accession A34150 !'##molecule_type mRNA !'##residues 1-241 ##label JOH !'##cross-references GB:D00736; GB:D00527; NID:g222559; PIDN:BAA00638.1; !1PID:g222563 GENETICS !$#gene P CLASSIFICATION #superfamily respiratory syncytial virus phosphoprotein P KEYWORDS phosphoprotein SUMMARY #length 241 #molecular-weight 26978 #checksum 7437 SEQUENCE /// ENTRY JQ1641 #type complete TITLE phosphoprotein P - bovine respiratory syncytial virus (strain A51908) ORGANISM #formal_name bovine respiratory syncytial virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jul-1999 ACCESSIONS JQ1641 REFERENCE JQ1641 !$#authors Mallipeddi, S.K.; Samal, S.K. !$#journal J. Gen. Virol. (1992) 73:2441-2444 !$#title Sequence comparison between the phosphoprotein mRNAs of !1human and bovine respiratory syncytial viruses identifies a !1divergent domain in the predicted protein. !$#cross-references MUID:93019071; PMID:1402819 !$#accession JQ1641 !'##molecule_type mRNA !'##residues 1-241 ##label MAL !'##cross-references GB:M93127; NID:g210836; PIDN:AAA42815.1; !1PID:g210837 !'##note the authors translated the codon AAA for residue 3 as Phe GENETICS !$#gene P CLASSIFICATION #superfamily respiratory syncytial virus phosphoprotein P KEYWORDS phosphoprotein SUMMARY #length 241 #molecular-weight 27254 #checksum 7858 SEQUENCE /// ENTRY RRNZM #type complete TITLE polymerase-associated nucleocapsid phosphoprotein - measles virus ALTERNATE_NAMES phosphoprotein P ORGANISM #formal_name measles virus DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 16-Jul-1999 ACCESSIONS A04038 REFERENCE A93007 !$#authors Bellini, W.J.; Englund, G.; Rozenblatt, S.; Arnheiter, H.; !1Richardson, C.D. !$#journal J. Virol. (1985) 53:908-919 !$#title Measles virus P gene codes for two proteins. !$#cross-references MUID:85135038; PMID:3882996 !$#accession A04038 !'##molecule_type mRNA !'##residues 1-507 ##label BEL !'##cross-references GB:M10456; NID:g331803; PIDN:AAA46437.1; !1PID:g331804 !'##note the authors translated the codon GAG for residue 233 as Asp and !1CGC for residue 234 as Ala GENETICS !$#gene P CLASSIFICATION #superfamily measles virus phosphoprotein P KEYWORDS nucleocapsid; phosphoprotein SUMMARY #length 507 #molecular-weight 54056 #checksum 9471 SEQUENCE /// ENTRY B48556 #type complete TITLE polymerase-associated nucleocapsid phosphoprotein - measles virus (strain AIK-C) ALTERNATE_NAMES phosphoprotein P ORGANISM #formal_name measles virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS B48556 REFERENCE A48556 !$#authors Mori, T.; Sasaki, K.; Hashimoto, H.; Makino, S. !$#journal Virus Genes (1993) 7:67-81 !$#title Molecular cloning and complete nucleotide sequence of !1genomic RNA of the AIK-C strain of attenuated measles virus. !$#cross-references MUID:93227570; PMID:8470368 !$#accession B48556 !'##molecule_type genomic RNA !'##residues 1-507 ##label MOR !'##cross-references GB:S58435; NID:g299460; PIDN:AAB26142.1; !1PID:g299462 !'##note sequence extracted from NCBI backbone (NCBIN:129264, !1NCBIP:129268) GENETICS !$#gene P CLASSIFICATION #superfamily measles virus phosphoprotein P KEYWORDS nucleocapsid; phosphoprotein SUMMARY #length 507 #molecular-weight 54100 #checksum 665 SEQUENCE /// ENTRY A43387 #type complete TITLE polymerase-associated nucleocapsid phosphoprotein - rinderpest virus (strain Kabete "O") ALTERNATE_NAMES phosphoprotein P ORGANISM #formal_name rinderpest virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS A43387 REFERENCE A43387 !$#authors Yamanaka, M.; Dale, B.; Crisp, T.; Cordell, B.; Grubman, M.; !1Yilma, T. !$#journal Virology (1992) 190:553-556 !$#title Sequence analysis and editing of the phosphoprotein (P) gene !1of rinderpest virus. !$#cross-references MUID:92410646; PMID:1529555 !$#accession A43387 !'##molecule_type mRNA !'##residues 1-507 ##label YAM !'##cross-references GB:S44819; NID:g255490; PIDN:AAB23268.1; !1PID:g255491 GENETICS !$#gene P CLASSIFICATION #superfamily measles virus phosphoprotein P KEYWORDS nucleocapsid; phosphoprotein SUMMARY #length 507 #molecular-weight 54341 #checksum 1968 SEQUENCE /// ENTRY RRNZCV #type complete TITLE polymerase-associated nucleocapsid phosphoprotein - canine distemper virus ALTERNATE_NAMES phosphoprotein P ORGANISM #formal_name canine distemper virus DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 24-Sep-1999 ACCESSIONS B23778 REFERENCE A23778 !$#authors Barrett, T.; Shrimpton, S.B.; Russell, S.E.H. !$#journal Virus Res. (1985) 3:367-372 !$#title Nucleotide sequence of the entire protein coding region of !1canine distemper virus polymerase-associated (P) protein !1mRNA. !$#cross-references MUID:86072821; PMID:3000106 !$#accession B23778 !'##molecule_type mRNA !'##residues 1-507 ##label BAR !'##cross-references GB:M32418; NID:g323247; PIDN:AAA42880.1; !1PID:g323248 GENETICS !$#gene P CLASSIFICATION #superfamily measles virus phosphoprotein P KEYWORDS nucleocapsid; phosphoprotein SUMMARY #length 507 #molecular-weight 54879 #checksum 6415 SEQUENCE /// ENTRY JQ1563 #type complete TITLE polymerase-associated nucleocapsid phosphoprotein - phocine distemper virus ALTERNATE_NAMES phosphoprotein P ORGANISM #formal_name phocine distemper virus DATE 31-Dec-1993 #sequence_revision 22-Oct-1999 #text_change 16-Jun-2000 ACCESSIONS JQ1609; JQ1563 REFERENCE JQ1608 !$#authors Blixenkrone-Moeller, M.; Sharma, B.; Varsanyi, T.M.; Hu, A.; !1Norrby, E.; Koevamees, J. !$#journal J. Gen. Virol. (1992) 73:885-893 !$#title Sequence analysis of the genes encoding the nucleocapsid !1protein and phosphoprotein (P) of phocid distemper virus, !1and editing of the P gene transcript. !$#cross-references MUID:92341068; PMID:1634877 !$#accession JQ1609 !'##molecule_type genomic RNA !'##residues 1-507 ##label BLI !'##cross-references GB:X75960; NID:g440570; PIDN:CAA53573.1; !1PID:g440571 REFERENCE JQ1563 !$#authors Curran, M.D.; Rima, B.K. !$#journal J. Gen. Virol. (1992) 73:1587-1591 !$#title The genes encoding the phospho- and matrix proteins of !1phocine distemper virus. !$#cross-references MUID:92300361; PMID:1535099 !$#accession JQ1563 !'##molecule_type genomic RNA !'##residues 1-191,'A',193-223,'A',225-392,'DV',395-507 ##label CUR !'##cross-references DDBJ:D10371; NID:g222246; PIDN:BAA01203.1; !1PID:g222248 !'##experimental_source strain Ulster/88 GENETICS !$#gene P/V; P CLASSIFICATION #superfamily measles virus phosphoprotein P KEYWORDS nucleocapsid; phosphoprotein SUMMARY #length 507 #molecular-weight 54776 #checksum 8576 SEQUENCE /// ENTRY MNNZSP #type complete TITLE nonstructural protein V - simian paramyxovirus SV5 (strain W3) ORGANISM #formal_name simian paramyxovirus SV5 DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jul-1999 ACCESSIONS A31594 REFERENCE A90902 !$#authors Thomas, S.M.; Lamb, R.A.; Paterson, R.G. !$#journal Cell (1988) 54:891-902 !$#title Two mRNAs that differ by two nontemplated nucleotides encode !1the amino coterminal proteins P and V of the paramyxovirus !1SV5. !$#cross-references MUID:88311091; PMID:3044614 !$#accession A31594 !'##molecule_type mRNA !'##residues 1-222 ##label THO !'##cross-references GB:J03142; NID:g335118; PIDN:AAA47882.1; !1PID:g335119 GENETICS !$#gene V CLASSIFICATION #superfamily simian paramyxovirus nonstructural protein V; !1V/P protein homology KEYWORDS alternative splicing; metal binding; nonstructural protein FEATURE !$1-164 #domain V/P protein homology #label VPN\ !$190-211 #domain metal binding #status predicted #label MTB SUMMARY #length 222 #molecular-weight 23935 #checksum 9493 SEQUENCE /// ENTRY JQ0597 #type complete TITLE nonstructural protein V - mumps virus ALTERNATE_NAMES nonstructural protein NS1 CONTAINS nonstructural protein NS2 ORGANISM #formal_name mumps virus DATE 30-Sep-1993 #sequence_revision 22-Jul-1994 #text_change 16-Jun-2000 ACCESSIONS JQ0597; JQ0602 REFERENCE JQ0596 !$#authors Elliott, G.D.; Yeo, R.P.; Afzal, M.A.; Simpson, E.J.B.; !1Curran, J.A.; Rima, B.K. !$#journal J. Gen. Virol. (1990) 71:1555-1560 !$#title Strain-variable editing during transcription of the P gene !1of mumps virus may lead to the generation of non-structural !1proteins NS1(V) and NS2. !$#cross-references MUID:90324941; PMID:2165137 !$#accession JQ0597 !'##molecule_type genomic RNA !'##residues 1-224 ##label ELL !'##cross-references GB:D00663; NID:g222149; PIDN:BAA00559.1; !1PID:g222151 !'##experimental_source strain SBL1 !$#accession JQ0602 !'##molecule_type genomic RNA !'##residues 1-169 ##label EL2 GENETICS !$#gene V CLASSIFICATION #superfamily simian paramyxovirus nonstructural protein V; !1V/P protein homology KEYWORDS alternative splicing; metal binding; nonstructural protein FEATURE !$1-169 #product nonstructural protein NS2 #status predicted !8#label NS2\ !$1-155 #domain V/P protein homology #label VPN\ !$189-210 #domain metal binding #status predicted #label MTB SUMMARY #length 224 #molecular-weight 24011 #checksum 6219 SEQUENCE /// ENTRY MNNZVT #type complete TITLE nonstructural protein V - parainfluenza virus type 2 (strain Toshiba) ORGANISM #formal_name parainfluenza virus type 2 DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS A35313; S16660 REFERENCE A35313 !$#authors Ohgimoto, S.; Bando, H.; Kawano, M.; Okamoto, K.; Kondo, K.; !1Tsurudome, M.; Nishio, M.; Ito, Y. !$#journal Virology (1990) 177:116-123 !$#title Sequence analysis of P gene of human parainfluenza type 2 !1virus: P and cysteine-rich proteins are translated by two !1mRNAs that differ by two nontemplated G residues. !$#cross-references MUID:90281574; PMID:2162103 !$#accession A35313 !'##molecule_type genomic RNA !'##residues 1-225 ##label OHG !'##cross-references GB:M37751; NID:g332585; PIDN:AAA46803.1; !1PID:g332586 !'##note this sequence (without the nontemplated addition of two G !1residues during mRNA synthesis) was confirmed by mRNA !1sequencing REFERENCE S16659 !$#authors Kawano, M.; Okamoto, K.; Bando, H.; Kondo, K.; Tsurudome, !1M.; Komada, H.; Nishio, M.; Ito, Y. !$#journal Nucleic Acids Res. (1991) 19:2739-2746 !$#title Characterizations of the human parainfluenza type 2 virus !1gene encoding the L protein and the intergenic sequences. !$#cross-references MUID:91252221; PMID:1645865 !$#accession S16660 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type genomic RNA !'##residues 1-225 ##label KAW !'##cross-references EMBL:X57559; NID:g61985; PIDN:CAA40784.1; !1PID:g61987 !'##experimental_source strain Toshiba !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1March 1991 GENETICS !$#gene V !$#note during mRNA synthesis, a nontemplated addition of two G's to !1a run of seven G's in the genomic sequence may or may not !1occur; the addition changes the reading frame to encode the !1phosphoprotein P (see entry RRNZVT) CLASSIFICATION #superfamily simian paramyxovirus nonstructural protein V; !1V/P protein homology KEYWORDS metal binding; nonstructural protein FEATURE !$1-163 #domain V/P protein homology #label VPN\ !$193-214 #domain metal binding #status predicted #label MTB SUMMARY #length 225 #molecular-weight 24151 #checksum 8406 SEQUENCE /// ENTRY MNNZP2 #type complete TITLE nonstructural protein V - parainfluenza virus type 2 ORGANISM #formal_name parainfluenza virus type 2 DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS A35322 REFERENCE A35322 !$#authors Southern, J.A.; Precious, B.; Randall, R.E. !$#journal Virology (1990) 177:388-390 !$#title Two nontemplated nucleotide additions are required to !1generate the P mRNA of parainfluenza virus type 2 since the !1RNA genome encodes protein V. !$#cross-references MUID:90281608; PMID:2162111 !$#accession A35322 !'##molecule_type genomic RNA !'##residues 1-225 ##label SOU !'##cross-references GB:M37748; NID:g332593; PIDN:AAA46808.1; !1PID:g332594 GENETICS !$#gene V CLASSIFICATION #superfamily simian paramyxovirus nonstructural protein V; !1V/P protein homology KEYWORDS alternative splicing; metal binding; nonstructural protein FEATURE !$1-163 #domain V/P protein homology #label VPN\ !$193-214 #domain metal binding #status predicted #label MTB SUMMARY #length 225 #molecular-weight 24121 #checksum 7342 SEQUENCE /// ENTRY JQ2040 #type complete TITLE nonstructural protein V - simian paramyxovirus SV41 ORGANISM #formal_name simian paramyxovirus SV41 DATE 24-Feb-1994 #sequence_revision 24-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS JQ2040 REFERENCE JQ2040 !$#authors Kawano, M.; Tsurudome, M.; Oki, N.; Nishio, M.; Komada, H.; !1Matsumura, H.; Kusagawa, S.; Ohta, H.; Ito, Y. !$#journal J. Gen. Virol. (1993) 74:911-916 !$#title Sequence determination of the P gene of simian virus 41: !1presence of irregular deletions near the RNA-editing sites !1of paramyxoviruses. !$#cross-references MUID:93260408; PMID:8492098 !$#accession JQ2040 !'##molecule_type genomic RNA !'##residues 1-225 ##label KAW !'##cross-references GB:S60811; NID:g385516; PIDN:AAB26639.1; !1PID:g385517 GENETICS !$#gene V CLASSIFICATION #superfamily simian paramyxovirus nonstructural protein V; !1V/P protein homology KEYWORDS alternative splicing; nonstructural protein FEATURE !$1-163 #domain V/P protein homology #label VPN SUMMARY #length 225 #molecular-weight 24048 #checksum 7082 SEQUENCE /// ENTRY B43685 #type complete TITLE nonstructural protein V - parainfluenza virus type 4A (strain Toshiba) ORGANISM #formal_name parainfluenza virus type 4A DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jul-1999 ACCESSIONS B43685 REFERENCE A43685 !$#authors Kondo, K.; Bando, H.; Tsurudome, M.; Kawano, M.; Nishio, M.; !1Ito, Y. !$#journal Virology (1990) 178:321-326 !$#title Sequence analysis of the phosphoprotein (P) genes of human !1parainfluenza type 4A and 4B viruses and RNA editing at !1transcript of the P genes: the number of G residues added is !1imprecise. !$#cross-references MUID:90357784; PMID:2167560 !$#accession B43685 !'##molecule_type mRNA !'##residues 1-229 ##label KON !'##cross-references GB:M55975; NID:g332587; PIDN:AAA46805.1; !1PID:g332589 GENETICS !$#gene V CLASSIFICATION #superfamily simian paramyxovirus nonstructural protein V; !1V/P protein homology KEYWORDS alternative splicing; nonstructural protein FEATURE !$1-153 #domain V/P protein homology #label VPN SUMMARY #length 229 #molecular-weight 25483 #checksum 6809 SEQUENCE /// ENTRY D43685 #type complete TITLE nonstructural protein V - parainfluenza virus type 4B (strain 68-333) ORGANISM #formal_name parainfluenza virus type 4B DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jul-1999 ACCESSIONS D43685 REFERENCE A43685 !$#authors Kondo, K.; Bando, H.; Tsurudome, M.; Kawano, M.; Nishio, M.; !1Ito, Y. !$#journal Virology (1990) 178:321-326 !$#title Sequence analysis of the phosphoprotein (P) genes of human !1parainfluenza type 4A and 4B viruses and RNA editing at !1transcript of the P genes: the number of G residues added is !1imprecise. !$#cross-references MUID:90357784; PMID:2167560 !$#accession D43685 !'##molecule_type mRNA !'##residues 1-229 ##label KON !'##cross-references GB:M55975 GENETICS !$#gene V CLASSIFICATION #superfamily simian paramyxovirus nonstructural protein V; !1V/P protein homology KEYWORDS alternative splicing; nonstructural protein FEATURE !$1-153 #domain V/P protein homology #label VPN SUMMARY #length 229 #molecular-weight 25566 #checksum 6328 SEQUENCE /// ENTRY A46343 #type complete TITLE nonstructural protein V - mumps virus (strain Miyahara) ORGANISM #formal_name mumps virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 15-Jun-1996 ACCESSIONS A46343 REFERENCE A46343 !$#authors Takeuchi, K.; Tanabayashi, K.; Hishiyama, M.; Yamada, Y.K.; !1Yamada, A.; Sugiura, A. !$#journal Virology (1990) 178:247-253 !$#title Detection and characterization of mumps virus V protein. !$#cross-references MUID:90357771; PMID:2389552 !$#accession A46343 !'##molecule_type mRNA !'##residues 1-224 ##label TAK GENETICS !$#gene V CLASSIFICATION #superfamily simian paramyxovirus nonstructural protein V; !1V/P protein homology KEYWORDS alternative splicing; metal binding; nonstructural protein FEATURE !$1-155 #domain V/P protein homology #label VPN\ !$189-210 #domain metal binding #status predicted #label MTB SUMMARY #length 224 #molecular-weight 24133 #checksum 7460 SEQUENCE /// ENTRY JQ1565 #type complete TITLE nonstructural protein V - phocine distemper virus (strain Ulster/88) ALTERNATE_NAMES phosphoprotein V ORGANISM #formal_name phocine distemper virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS JQ1565; S21376 REFERENCE JQ1563 !$#authors Curran, M.D.; Rima, B.K. !$#journal J. Gen. Virol. (1992) 73:1587-1591 !$#title The genes encoding the phospho- and matrix proteins of !1phocine distemper virus. !$#cross-references MUID:92300361; PMID:1535099 !$#accession JQ1565 !'##molecule_type genomic RNA !'##residues 1-299 ##label CUR !'##cross-references DDBJ:D10371 !'##experimental_source strain Ulster/88 REFERENCE S21376 !$#authors Barrett, T.; Goatley, L.G.; Haas, L. !$#submission submitted to the EMBL Data Library, April 1992 !$#accession S21376 !'##status preliminary !'##molecule_type mRNA !'##residues 1-299 ##label BAR !'##cross-references EMBL:X65512; NID:g60636; PIDN:CAA46485.1; !1PID:g60637 GENETICS !$#gene V CLASSIFICATION #superfamily phocine distemper virus nonstructural protein V KEYWORDS nonstructural protein; phosphoprotein SUMMARY #length 299 #molecular-weight 33501 #checksum 6731 SEQUENCE /// ENTRY MNNZ1B #type complete TITLE nonstructural protein 1B - human respiratory syncytial virus ORGANISM #formal_name human respiratory syncytial virus DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 16-Jul-1999 ACCESSIONS B94336; C93010; A04032 REFERENCE A94336 !$#authors Collins, P.L.; Wertz, G.W. !$#journal Virology (1985) 143:442-451 !$#title Nucleotide sequences of the 1B and 1C nonstructural protein !1mRNAs of human respiratory syncytial virus. !$#cross-references MUID:86045905; PMID:2998021 !$#accession B94336 !'##molecule_type genomic RNA !'##residues 1-124 ##label COL !'##cross-references GB:M11486; GB:K01459; GB:K02719; GB:K03348; !1GB:K03349; GB:M11217; GB:M11244; GB:M11487; GB:M11505; !1GB:M11514; GB:M11631; GB:M12966; GB:X00001; GB:X02221; !1NID:g333925; PIDN:AAB59851.1; PID:g333927 REFERENCE A93010 !$#authors Elango, N.; Satake, M.; Venkatesan, S. !$#journal J. Virol. (1985) 55:101-110 !$#title mRNA sequence of three respiratory syncytial virus genes !1encoding two nonstructural proteins and a 22K structural !1protein. !$#cross-references MUID:85237684; PMID:4009789 !$#accession C93010 !'##molecule_type genomic RNA !'##residues 1-54,'R',56-124 ##label ELA !'##cross-references GB:M11486 GENETICS !$#gene 1B CLASSIFICATION #superfamily respiratory syncytial virus nonstructural !1protein 1B KEYWORDS nonstructural protein SUMMARY #length 124 #molecular-weight 14674 #checksum 5322 SEQUENCE /// ENTRY MNNZ15 #type complete TITLE nonstructural protein 1B - human respiratory syncytial virus (strain 18537) ALTERNATE_NAMES nonstructural protein NS2 ORGANISM #formal_name human respiratory syncytial virus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jun-2000 ACCESSIONS B32063 REFERENCE A32063 !$#authors Johnson, P.R.; Collins, P.L. !$#journal J. Gen. Virol. (1989) 70:1539-1547 !$#title The 1B (NS2), 1C (NS1) and N proteins of human respiratory !1syncytial virus (RSV) of antigenic subgroups A and B: !1sequence conservation and divergence within RSV genomic RNA. !$#cross-references MUID:89279331; PMID:2525176 !$#accession B32063 !'##molecule_type mRNA !'##residues 1-124 ##label JOH !'##cross-references EMBL:D00736; NID:g222559; PIDN:BAA00636.1; !1PID:g222561 GENETICS !$#gene 1B CLASSIFICATION #superfamily respiratory syncytial virus nonstructural !1protein 1B KEYWORDS nonstructural protein SUMMARY #length 124 #molecular-weight 14624 #checksum 5832 SEQUENCE /// ENTRY MNNZ1C #type complete TITLE nonstructural protein 1C - human respiratory syncytial virus ORGANISM #formal_name human respiratory syncytial virus DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 16-Jul-1999 ACCESSIONS A94336; A93010; A04033 REFERENCE A94336 !$#authors Collins, P.L.; Wertz, G.W. !$#journal Virology (1985) 143:442-451 !$#title Nucleotide sequences of the 1B and 1C nonstructural protein !1mRNAs of human respiratory syncytial virus. !$#cross-references MUID:86045905; PMID:2998021 !$#accession A94336 !'##molecule_type genomic RNA !'##residues 1-139 ##label COL !'##cross-references GB:M11486; GB:K01459; GB:K02719; GB:K03348; !1GB:K03349; GB:M11217; GB:M11244; GB:M11487; GB:M11505; !1GB:M11514; GB:M11631; GB:M12966; GB:X00001; GB:X02221; !1NID:g333925; PIDN:AAB59850.1; PID:g333926 REFERENCE A93010 !$#authors Elango, N.; Satake, M.; Venkatesan, S. !$#journal J. Virol. (1985) 55:101-110 !$#title mRNA sequence of three respiratory syncytial virus genes !1encoding two nonstructural proteins and a 22K structural !1protein. !$#cross-references MUID:85237684; PMID:4009789 !$#accession A93010 !'##molecule_type genomic RNA !'##residues 1-139 ##label ELA !'##cross-references GB:M11486; NID:g333925; PIDN:AAB59850.1; !1PID:g333926 GENETICS !$#gene 1C CLASSIFICATION #superfamily respiratory syncytial virus nonstructural !1protein 1C KEYWORDS nonstructural protein SUMMARY #length 139 #molecular-weight 15567 #checksum 5479 SEQUENCE /// ENTRY MNNZ18 #type complete TITLE nonstructural protein 1C - human respiratory syncytial virus (strain 18537) ALTERNATE_NAMES nonstructural protein NS1 ORGANISM #formal_name human respiratory syncytial virus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jun-2000 ACCESSIONS A32063 REFERENCE A32063 !$#authors Johnson, P.R.; Collins, P.L. !$#journal J. Gen. Virol. (1989) 70:1539-1547 !$#title The 1B (NS2), 1C (NS1) and N proteins of human respiratory !1syncytial virus (RSV) of antigenic subgroups A and B: !1sequence conservation and divergence within RSV genomic RNA. !$#cross-references MUID:89279331; PMID:2525176 !$#accession A32063 !'##molecule_type mRNA !'##residues 1-139 ##label JOH !'##cross-references EMBL:D00736; NID:g222559; PIDN:BAA00635.1; !1PID:g222560 GENETICS !$#gene 1C CLASSIFICATION #superfamily respiratory syncytial virus nonstructural !1protein 1C KEYWORDS nonstructural protein SUMMARY #length 139 #molecular-weight 15512 #checksum 5560 SEQUENCE /// ENTRY MNNZ1G #type complete TITLE gene 1 protein - pneumonia virus of mice ORGANISM #formal_name pneumonia virus of mice DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 08-Apr-1994 ACCESSIONS JQ1255 REFERENCE JQ1255 !$#authors Chambers, P.; Pringle, C.R.; Easton, A.J. !$#journal J. Gen. Virol. (1991) 72:2545-2549 !$#title Genes 1 and 2 of pneumonia virus of mice encode proteins !1which have little homology with the 1C and 1B proteins of !1human respiratory syncytial virus. !$#cross-references MUID:92013975; PMID:1919530 !$#accession JQ1255 !'##molecule_type mRNA !'##residues 1-107 ##label CHA !'##cross-references DDBJ:D01100 GENETICS !$#gene 1 CLASSIFICATION #superfamily mouse pneumonia virus gene 1 protein SUMMARY #length 107 #molecular-weight 12268 #checksum 5613 SEQUENCE /// ENTRY MNNZ2G #type complete TITLE gene 2 protein - pneumonia virus of mice ORGANISM #formal_name pneumonia virus of mice DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 08-Apr-1994 ACCESSIONS JQ1256 REFERENCE JQ1255 !$#authors Chambers, P.; Pringle, C.R.; Easton, A.J. !$#journal J. Gen. Virol. (1991) 72:2545-2549 !$#title Genes 1 and 2 of pneumonia virus of mice encode proteins !1which have little homology with the 1C and 1B proteins of !1human respiratory syncytial virus. !$#cross-references MUID:92013975; PMID:1919530 !$#accession JQ1256 !'##molecule_type mRNA !'##residues 1-152 ##label CHA !'##cross-references DDBJ:D01100 GENETICS !$#gene 2 CLASSIFICATION #superfamily mouse pneumonia virus gene 2 protein SUMMARY #length 152 #molecular-weight 17842 #checksum 7356 SEQUENCE /// ENTRY JQ1623 #type complete TITLE envelope-associated 22K protein - turkey rhinotracheitis virus ORGANISM #formal_name turkey rhinotracheitis virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jul-1999 ACCESSIONS JQ1623 REFERENCE PQ0405 !$#authors Ling, R.; Easton, A.J.; Pringle, C.R. !$#journal J. Gen. Virol. (1992) 73:1709-1715 !$#title Sequence analysis of the 22K, SH and G genes of turkey !1rhinotracheitis virus and their intergenic regions reveals a !1gene order different from that of other pneumoviruses. !$#cross-references MUID:92333255; PMID:1629697 !$#accession JQ1623 !'##molecule_type mRNA !'##residues 1-186 ##label LIN !'##cross-references GB:S40185; NID:g251600; PIDN:AAB22544.1; !1PID:g251602 GENETICS !$#gene 22K CLASSIFICATION #superfamily respiratory syncytial virus envelope-associated !122K protein KEYWORDS glycoprotein FEATURE !$86 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 186 #molecular-weight 20986 #checksum 2051 SEQUENCE /// ENTRY WMNZ22 #type complete TITLE envelope-associated 22K protein - human respiratory syncytial virus ORGANISM #formal_name human respiratory syncytial virus DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 16-Jul-1999 ACCESSIONS B93010; A93009; A04034 REFERENCE A93010 !$#authors Elango, N.; Satake, M.; Venkatesan, S. !$#journal J. Virol. (1985) 55:101-110 !$#title mRNA sequence of three respiratory syncytial virus genes !1encoding two nonstructural proteins and a 22K structural !1protein. !$#cross-references MUID:85237684; PMID:4009789 !$#accession B93010 !'##molecule_type genomic RNA !'##residues 1-194 ##label ELA !'##cross-references GB:M11486; NID:g333925; PIDN:AAB59860.1; !1PID:g333934 REFERENCE A93009 !$#authors Collins, P.L.; Wertz, G.W. !$#journal J. Virol. (1985) 54:65-71 !$#title The envelope-associated 22K protein of human respiratory !1syncytial virus: nucleotide sequence of the mRNA and a !1related polytranscript. !$#cross-references MUID:85135082; PMID:3838351 !$#accession A93009 !'##molecule_type genomic RNA !'##residues 1-194 ##label COL !'##cross-references GB:M11486; GB:K01459; GB:K02719; GB:K03348; !1GB:K03349; GB:M11217; GB:M11244; GB:M11487; GB:M11505; !1GB:M11514; GB:M11631; GB:M12966; GB:X00001; GB:X02221; !1NID:g333925; PIDN:AAB59860.1; PID:g333934 GENETICS !$#gene 22K CLASSIFICATION #superfamily respiratory syncytial virus envelope-associated !122K protein KEYWORDS glycoprotein FEATURE !$89,191 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 194 #molecular-weight 22154 #checksum 9828 SEQUENCE /// ENTRY WMNZBA #type complete TITLE matrix glycoprotein M2 - bovine respiratory syncytial virus (strain A51908) ORGANISM #formal_name bovine respiratory syncytial virus DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS JQ1482 REFERENCE JQ1481 !$#authors Zamora, M.; Samal, S.K. !$#journal J. Gen. Virol. (1992) 73:737-741 !$#title Sequence analysis of M2 mRNA of bovine respiratory syncytial !1virus obtained from an F-M2 dicistronic mRNA suggests !1structural homology with that of human respiratory syncytial !1virus. !$#cross-references MUID:92185490; PMID:1312130 !$#accession JQ1482 !'##molecule_type mRNA !'##residues 1-186 ##label ZAM !'##cross-references GB:M82816; NID:g210823; PIDN:AAA42805.1; !1PID:g210825 GENETICS !$#gene M2 CLASSIFICATION #superfamily respiratory syncytial virus envelope-associated !122K protein KEYWORDS glycoprotein FEATURE !$54,89 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 186 #molecular-weight 21351 #checksum 6337 SEQUENCE /// ENTRY VGNZA2 #type complete TITLE cell fusion glycoprotein precursor - human respiratory syncytial virus (strain A2) ALTERNATE_NAMES F protein CONTAINS cell fusion glycoprotein F1; cell fusion glycoprotein F2 ORGANISM #formal_name human respiratory syncytial virus #note host Homo sapiens (man) DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 16-Jul-1999 ACCESSIONS A04035 REFERENCE A04035 !$#authors Collins, P.L.; Huang, Y.T.; Wertz, G.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:7683-7687 !$#title Nucleotide sequence of the gene encoding the fusion (F) !1glycoprotein of human respiratory syncytial virus. !$#cross-references MUID:85088471; PMID:6096849 !$#accession A04035 !'##molecule_type mRNA !'##residues 1-574 ##label COL !'##cross-references GB:M11486; GB:K01459; GB:K02719; GB:K03348; !1GB:K03349; GB:M11217; GB:M11244; GB:M11487; GB:M11505; !1GB:M11514; GB:M11631; GB:M12966; GB:X00001; GB:X02221; !1NID:g333925; PIDN:AAB59858.1; PID:g333933 COMMENT This protein directs fusion of viral and cellular membranes, !1resulting in viral penetration, and can direct fusion of !1infected cells with adjoining cells, resulting in the !1formation of syncytia. CLASSIFICATION #superfamily cell fusion glycoprotein KEYWORDS glycoprotein; membrane fusion; transmembrane protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-136 #product cell fusion glycoprotein F2 #status !8predicted #label F2P\ !$137-574 #product cell fusion glycoprotein F1 #status !8predicted #label F1P\ !$525-550 #domain transmembrane #status predicted #label TM1\ !$27,70,116,126,500 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 574 #molecular-weight 63453 #checksum 7984 SEQUENCE /// ENTRY VGNZR2 #type complete TITLE cell fusion glycoprotein precursor - human respiratory syncytial virus (strain RSS-2) CONTAINS cell fusion glycoprotein F1; cell fusion glycoprotein F2 ORGANISM #formal_name human respiratory syncytial virus #note host Homo sapiens (man) DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 25-Oct-1996 ACCESSIONS A27494 REFERENCE A27494 !$#authors Baybutt, H.N.; Pringle, C.R. !$#journal J. Gen. Virol. (1987) 68:2789-2796 !$#title Molecular cloning and sequencing of the F and 22K membrane !1protein genes of the RSS-2 strain of respiratory syncytial !1virus. !$#cross-references MUID:88061203; PMID:3681264 !$#accession A27494 !'##molecule_type genomic RNA !'##residues 1-574 ##label BAY GENETICS !$#gene F CLASSIFICATION #superfamily cell fusion glycoprotein KEYWORDS glycoprotein; membrane fusion; transmembrane protein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-136 #product cell fusion glycoprotein F2 #status !8predicted #label F2P\ !$137-574 #product cell fusion glycoprotein F1 #status !8predicted #label F1P\ !$526-549 #domain transmembrane #status predicted #label TM1\ !$27,70,116,120,126, !$500 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 574 #molecular-weight 63350 #checksum 7190 SEQUENCE /// ENTRY VGNZL #type complete TITLE cell fusion glycoprotein precursor - human respiratory syncytial virus (strain Long) CONTAINS cell fusion glycoprotein F1; cell fusion glycoprotein F2 ORGANISM #formal_name human respiratory syncytial virus #note host Homo sapiens (man) DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jul-1999 ACCESSIONS S07944; A33218 REFERENCE S07428 !$#authors Lopez, J.A.; Villanueva, N.; Melero, J.A.; Portela, A. !$#journal Virus Res. (1988) 10:249-262 !$#title Nucleotide sequence of the fusion and phosphoprotein genes !1of human respiratory syncytial (RS) virus Long strain: !1evidence of subtype genetic heterogeneity. !$#cross-references MUID:88323192; PMID:3414184 !$#accession S07944 !'##molecule_type mRNA !'##residues 1-574 ##label LOP !'##cross-references EMBL:M22643; NID:g333938; PIDN:AAA47409.1; !1PID:g333939 !$#accession A33218 !'##molecule_type protein !'##residues 137-141 ##label LOP2 GENETICS !$#gene F CLASSIFICATION #superfamily cell fusion glycoprotein KEYWORDS glycoprotein; membrane fusion; transmembrane protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-136 #product cell fusion glycoprotein F2 #status !8predicted #label F2P\ !$137-574 #product cell fusion glycoprotein F1 #status !8experimental #label F1P\ !$525-550 #domain transmembrane #status predicted #label TM1\ !$27,70,116,120,126, !$500 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 574 #molecular-weight 63431 #checksum 6479 SEQUENCE /// ENTRY VGNZHB #type complete TITLE cell fusion glycoprotein precursor - human respiratory syncytial virus (strain 18537, subgroup B) ALTERNATE_NAMES F protein CONTAINS cell fusion glycoprotein F1; cell fusion glycoprotein F2 ORGANISM #formal_name human respiratory syncytial virus #note host Homo sapiens (man) DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jun-2000 ACCESSIONS A28929 REFERENCE A28929 !$#authors Johnson, P.R.; Collins, P.L. !$#journal J. Gen. Virol. (1988) 69:2623-2628 !$#title The fusion glycoproteins of human respiratory syncytial !1virus of subgroups A and B: sequence conservation provides a !1structural basis for antigenic relatedness. !$#cross-references MUID:89010699; PMID:3171553 !$#accession A28929 !'##molecule_type mRNA !'##residues 1-574 ##label JOH !'##cross-references GB:D00334; NID:g222564; PIDN:BAA00240.1; !1PID:g222565 GENETICS !$#gene F CLASSIFICATION #superfamily cell fusion glycoprotein KEYWORDS glycoprotein; membrane fusion; transmembrane protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-136 #product cell fusion glycoprotein F2 #status !8predicted #label F2P\ !$137-574 #product cell fusion glycoprotein F1 #status !8predicted #label F1P\ !$137-158 #domain transmembrane #status predicted #label TM1\ !$525-550 #domain transmembrane #status predicted #label TM2\ !$27,70,116,120,126, !$500 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 574 #molecular-weight 63688 #checksum 9281 SEQUENCE /// ENTRY VGNZBS #type complete TITLE cell fusion glycoprotein precursor - bovine respiratory syncytial virus (strain RB94) CONTAINS cell fusion glycoprotein F1; cell fusion glycoprotein F2 ORGANISM #formal_name bovine respiratory syncytial virus DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jun-2000 ACCESSIONS JH0233 REFERENCE JH0233 !$#authors Walravens, K.; Kettmann, R.; Collard, A.; Coppe, P.; Burny, !1A. !$#journal J. Gen. Virol. (1990) 71:3009-3014 !$#title Sequence comparison between the fusion protein of human and !1bovine respiratory syncytial viruses. !$#cross-references MUID:91108398; PMID:1703214 !$#accession JH0233 !'##molecule_type mRNA !'##residues 1-574 ##label WAL !'##cross-references GB:D00953; NID:g221061; PIDN:BAA00798.1; !1PID:g221062 GENETICS !$#gene F CLASSIFICATION #superfamily cell fusion glycoprotein KEYWORDS glycoprotein; membrane fusion; transmembrane protein FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-136 #product cell fusion glycoprotein F2 #status !8predicted #label F2P\ !$137-574 #product cell fusion glycoprotein F1 #status !8experimental #label F1P\ !$525-549 #domain transmembrane #status predicted #label TM1\ !$27,70,120,500,569 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 574 #molecular-weight 63630 #checksum 6492 SEQUENCE /// ENTRY VGNZBR #type complete TITLE cell fusion glycoprotein precursor - bovine respiratory syncytial virus (strain 391-2) CONTAINS cell fusion glycoprotein F1; cell fusion glycoprotein F2 ORGANISM #formal_name bovine respiratory syncytial virus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jul-1999 ACCESSIONS A38492 REFERENCE A38492 !$#authors Lerch, R.A.; Anderson, K.; Amann, V.L.; Wertz, G.W. !$#journal Virology (1991) 181:118-131 !$#title Nucleotide sequence analysis of the bovine respiratory !1syncytial virus fusion protein mRNA and expression from a !1recombinant vaccinia virus. !$#cross-references MUID:91134972; PMID:1994571 !$#accession A38492 !'##molecule_type mRNA !'##residues 1-574 ##label LER !'##cross-references EMBL:M58350; NID:g210828; PIDN:AAA42808.1; !1PID:g210829 GENETICS !$#gene F CLASSIFICATION #superfamily cell fusion glycoprotein KEYWORDS glycoprotein; membrane fusion; transmembrane protein FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-136 #product cell fusion glycoprotein F2 #status !8predicted #label F2P\ !$137-574 #product cell fusion glycoprotein F1 #status !8predicted #label F1P\ !$137-154 #domain transmembrane #status predicted #label TM1\ !$528-549 #domain transmembrane #status predicted #label TM2\ !$27,120,500,569 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 574 #molecular-weight 63821 #checksum 5637 SEQUENCE /// ENTRY VGNZBA #type complete TITLE cell fusion glycoprotein precursor - bovine respiratory syncytial virus (strain A51908) CONTAINS cell fusion glycoprotein F1; cell fusion glycoprotein F2 ORGANISM #formal_name bovine respiratory syncytial virus DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS JQ1481 REFERENCE JQ1481 !$#authors Zamora, M.; Samal, S.K. !$#journal J. Gen. Virol. (1992) 73:737-741 !$#title Sequence analysis of M2 mRNA of bovine respiratory syncytial !1virus obtained from an F-M2 dicistronic mRNA suggests !1structural homology with that of human respiratory syncytial !1virus. !$#cross-references MUID:92185490; PMID:1312130 !$#accession JQ1481 !'##molecule_type mRNA !'##residues 1-572 ##label ZAM !'##cross-references GB:M82816; NID:g210823; PIDN:AAA42804.1; !1PID:g210824 GENETICS !$#gene F CLASSIFICATION #superfamily cell fusion glycoprotein KEYWORDS glycoprotein; membrane fusion; transmembrane protein FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-136 #product cell fusion glycoprotein F2 #status !8predicted #label F2P\ !$137-572 #product cell fusion glycoprotein F1 #status !8predicted #label F1P\ !$138-154 #domain transmembrane #status predicted #label TM1\ !$524-540 #domain transmembrane #status predicted #label TM2\ !$27,70,120,498,567 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 572 #molecular-weight 63443 #checksum 7829 SEQUENCE /// ENTRY VGNZTR #type complete TITLE cell fusion glycoprotein precursor - turkey rhinotracheitis virus (strain UK/3B/85) ALTERNATE_NAMES F glycoprotein CONTAINS cell fusion glycoprotein F1; cell fusion glycoprotein F2 ORGANISM #formal_name turkey rhinotracheitis virus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 20-Apr-2001 ACCESSIONS JQ0938; PQ0405; A54332 REFERENCE JQ0938 !$#authors Yu, Q.; Davis, P.J.; Barrett, T.; Binns, M.M.; Boursnell, !1M.E.G.; Cavanagh, D. !$#journal J. Gen. Virol. (1991) 72:75-81 !$#title Deduced amino acid sequence of the fusion glycoprotein of !1turkey rhinotracheitis virus has greater identity with that !1of human respiratory syncytial virus, a pneumovirus, than !1that of paramyxoviruses and morbilliviruses. !$#cross-references MUID:91116323; PMID:1990068 !$#accession JQ0938 !'##molecule_type mRNA !'##residues 1-538 ##label YUQ !'##cross-references GB:D00850; NID:g222678; PIDN:BAA00726.1; !1PID:g222679 REFERENCE PQ0405 !$#authors Ling, R.; Easton, A.J.; Pringle, C.R. !$#journal J. Gen. Virol. (1992) 73:1709-1715 !$#title Sequence analysis of the 22K, SH and G genes of turkey !1rhinotracheitis virus and their intergenic regions reveals a !1gene order different from that of other pneumoviruses. !$#cross-references MUID:92333255; PMID:1629697 !$#accession PQ0405 !'##molecule_type mRNA !'##residues 500-538 ##label LIN !'##cross-references GB:S40185; NID:g251600; PIDN:AAB22543.1; !1PID:g251601 REFERENCE A54332 !$#authors Yu, Q.; Davis, P.J.; Barrett, T.; Binns, M.M.; Boursnell, !1M.E.G.; Cavanagh, D. !$#journal J. Gen. Virol. (1991) 72:75-81 !$#title Deduced amino acid sequence of the fusion glycoprotein of !1turkey rhinotracheitis virus has greater identity with that !1of human respiratory syncytial virus, a pneumovirus, than !1that of paramyxoviruses and morbilliviruses. !$#cross-references MUID:91116323; PMID:1990068 !$#accession A54332 !'##molecule_type mRNA !'##residues 1-538 ##label YUA !'##cross-references GB:D00856 !'##note authors translated the codon TTG for residue 427 as Gly GENETICS !$#gene F CLASSIFICATION #superfamily cell fusion glycoprotein KEYWORDS glycoprotein; membrane fusion; transmembrane protein FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-102 #product cell fusion glycoprotein F2 #status !8predicted #label F2P\ !$103-538 #product cell fusion glycoprotein F1 #status !8predicted #label F1P\ !$491-513 #domain transmembrane #status predicted #label TMN\ !$57,353 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 538 #molecular-weight 58728 #checksum 5016 SEQUENCE /// ENTRY JQ1619 #type complete TITLE cell fusion glycoprotein precursor - pneumonia virus of mice ALTERNATE_NAMES F protein CONTAINS cell fusion glycoprotein F1; cell fusion glycoprotein F2 ORGANISM #formal_name pneumonia virus of mice DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 25-Oct-1996 ACCESSIONS JQ1619 REFERENCE JQ1619 !$#authors Chambers, P.; Pringle, C.R.; Easton, A.J. !$#journal J. Gen. Virol. (1992) 73:1717-1724 !$#title Sequence analysis of the gene encoding the fusion !1glycoprotein of pneumonia virus of mice suggests possible !1conserved secondary structure elements in paramyxovirus !1fusion glycoprotein. !$#cross-references MUID:92333256; PMID:1629698 !$#accession JQ1619 !'##molecule_type mRNA !'##residues 1-537 ##label CHA !'##cross-references GB:S40186 GENETICS !$#gene F CLASSIFICATION #superfamily cell fusion glycoprotein KEYWORDS glycoprotein; membrane fusion; transmembrane protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-101 #product cell fusion glycoprotein F2 #status !8predicted #label FG2\ !$102-537 #product cell fusion glycoprotein F1 #status !8predicted #label FG1\ !$491-514 #domain transmembrane #status predicted #label TMM\ !$463,488 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 537 #molecular-weight 59366 #checksum 8950 SEQUENCE /// ENTRY VGNZSV #type complete TITLE cell fusion glycoprotein precursor - Sendai virus (strain Z) ORGANISM #formal_name Sendai virus DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 16-Jul-1999 ACCESSIONS A04036 REFERENCE A00878 !$#authors Shioda, T.; Iwasaki, K.; Shibuta, H. !$#journal Nucleic Acids Res. (1986) 14:1545-1563 !$#title Determination of the complete nucleotide sequence of the !1Sendai virus genome RNA and the predicted amino acid !1sequences of the F, HN and L proteins. !$#cross-references MUID:86148492; PMID:3005975 !$#accession A04036 !'##molecule_type genomic RNA !'##residues 1-565 ##label SHI !'##cross-references GB:X03614; NID:g60898; PIDN:CAA27275.1; PID:g60904 GENETICS !$#gene F CLASSIFICATION #superfamily parainfluenza virus cell fusion protein KEYWORDS glycoprotein; membrane fusion; transmembrane protein FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-116 #product cell fusion glycoprotein F2 #status !8predicted #label FG2\ !$117-565 #product cell fusion glycoprotein F1 #status !8predicted #label FG1\ !$104,245,259,449 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 565 #molecular-weight 61582 #checksum 2648 SEQUENCE /// ENTRY VGNZSH #type complete TITLE cell fusion glycoprotein precursor - Sendai virus (strain HVJ) CONTAINS fusion glycoprotein F1; fusion glycoprotein F2 ORGANISM #formal_name Sendai virus DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Jul-1999 ACCESSIONS A24516 REFERENCE A24516 !$#authors Miura, N.; Ohtsuka, E.; Yamaberi, N.; Ikehara, M.; Uchida, !1T.; Okada, Y. !$#journal Gene (1985) 38:271-274 !$#title Use of the deoxyinosine-containing probe to isolate and !1sequence cDNA encoding the fusion (F) glycoprotein of Sendai !1virus (HVJ). !$#cross-references MUID:86056987; PMID:2998947 !$#accession A24516 !'##molecule_type genomic RNA !'##residues 1-565 ##label MIU !'##cross-references GB:M12396; NID:g334931; PIDN:AAA47809.1; !1PID:g334932 GENETICS !$#gene F CLASSIFICATION #superfamily parainfluenza virus cell fusion protein KEYWORDS glycoprotein; membrane fusion; transmembrane protein FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-116 #product cell fusion glycoprotein F2 #status !8predicted #label FG2\ !$117-565 #product cell fusion glycoprotein F1 #status !8predicted #label FG1\ !$104,245,449 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 565 #molecular-weight 61644 #checksum 2599 SEQUENCE /// ENTRY VGNZFS #type complete TITLE cell fusion glycoprotein precursor - Sendai virus (strain Fushimi) CONTAINS fusion glycoprotein F1; fusion glycoprotein F2 ORGANISM #formal_name Sendai virus DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jun-2000 ACCESSIONS A30037 REFERENCE A30037 !$#authors Itoh, M.; Shibuta, H.; Homma, M. !$#journal J. Gen. Virol. (1987) 68:2939-2944 !$#title Single amino acid substitution of Sendai virus at the !1cleavage site of the fusion protein confers trypsin !1resistance. !$#cross-references MUID:88061218; PMID:2824671 !$#accession A30037 !'##molecule_type genomic RNA !'##residues 1-565 ##label ITO !'##cross-references GB:D00152; NID:g222618; PIDN:BAA00107.1; !1PID:g222619 GENETICS !$#gene F CLASSIFICATION #superfamily parainfluenza virus cell fusion protein KEYWORDS glycoprotein; membrane fusion; transmembrane protein FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-116 #product cell fusion glycoprotein F2 #status !8predicted #label FG2\ !$117-565 #product cell fusion glycoprotein F1 #status !8predicted #label FG1\ !$104,245,449 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 565 #molecular-weight 61552 #checksum 4067 SEQUENCE /// ENTRY VGNZ11 #type complete TITLE cell fusion glycoprotein precursor - Sendai virus (strain C39) CONTAINS fusion glycoprotein F1; fusion glycoprotein F2 ORGANISM #formal_name Sendai virus DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jul-1999 ACCESSIONS A31287; S11284 REFERENCE A31287 !$#authors Merson, J.R.; Hull, R.A.; Estes, M.K.; Kasel, J.A. !$#journal Virology (1988) 167:97-105 !$#title Molecular cloning and sequence determination of the fusion !1protein gene of human parainfluenza virus type 1. !$#cross-references MUID:89045674; PMID:2847427 !$#accession A31287 !'##molecule_type mRNA !'##residues 1-555 ##label MER !'##cross-references GB:M22347; NID:g332579; PIDN:AAA46800.1; !1PID:g332580 !'##experimental_source strain C39 REFERENCE S11266 !$#authors Richardson, C.D.; Scheid, A.; Choppin, P.W. !$#journal Virology (1980) 105:205-222 !$#title Specific inhibition of paramyxovirus and myxovirus !1replication by oligopeptides with amino acid sequences !1similar to those at the N-termini of the F1 or HA2 viral !1polypeptides. !$#cross-references MUID:81016739; PMID:7414950 !$#accession S11284 !'##molecule_type protein !'##residues 113-132 ##label RIC GENETICS !$#gene F CLASSIFICATION #superfamily parainfluenza virus cell fusion protein KEYWORDS glycoprotein; membrane fusion; transmembrane protein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-112 #product cell fusion glycoprotein F2 #status !8predicted #label FF2\ !$113-555 #product cell fusion glycoprotein F1 #status !8predicted #label FF1\ !$113-138 #domain transmembrane #status predicted #label TM1\ !$498-519 #domain transmembrane #status predicted #label TM2\ !$100,241,529,552 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 555 #molecular-weight 60785 #checksum 5982 SEQUENCE /// ENTRY VGNZH3 #type complete TITLE cell fusion glycoprotein precursor - parainfluenza virus type 3 ORGANISM #formal_name parainfluenza virus type 3 #note host Homo sapiens (man) DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 16-Jul-1999 ACCESSIONS A26764; A45602 REFERENCE A26764 !$#authors Cote, M.J.; Storey, D.G.; Kang, C.Y.; Dimock, K. !$#journal J. Gen. Virol. (1987) 68:1003-1010 !$#title Nucleotide sequence of the coding and flanking regions of !1the human parainfluenza virus type 3 fusion glycoprotein !1gene. !$#cross-references MUID:87197191; PMID:3033123 !$#accession A26764 !'##molecule_type genomic RNA !'##residues 1-539 ##label COT !'##cross-references GB:X05303; NID:g60869; PIDN:CAA28932.1; PID:g758206 !'##note the authors translated the codons GGT for residue 191 and CAA !1for residues 479 and 489 as Glu REFERENCE A45602 !$#authors Prinoski, K.; Cote, M.J.; Kang, C.Y.; Dimock, K. !$#journal Virus Res. (1992) 22:55-69 !$#title Evolution of the fusion protein gene of human parainfluenza !1virus 3. !$#cross-references MUID:92160382; PMID:1311137 !$#accession A45602 !'##molecule_type genomic RNA !'##residues 1-327,'V',329-449,'A',451-539 ##label PRI !'##cross-references GB:S82195; NID:g245568; PIDN:AAB21447.1; !1PID:g245569 !'##note sequence extracted from NCBI backbone (NCBIN:82195, !1NCBIP:82201) GENETICS !$#gene F CLASSIFICATION #superfamily parainfluenza virus cell fusion protein KEYWORDS glycoprotein; membrane fusion; transmembrane protein FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-109 #product cell fusion glycoprotein F2 #status !8predicted #label F2P\ !$110-539 #product cell fusion glycoprotein F1 #status !8predicted #label F1P\ !$110-135 #domain transmembrane #status predicted #label TM1\ !$494-516 #domain transmembrane #status predicted #label TM2\ !$238,359,446,508 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 539 #molecular-weight 60035 #checksum 5808 SEQUENCE /// ENTRY A47610 #type complete TITLE cell fusion glycoprotein precursor - parainfluenza virus type 3 (strain 47885) CONTAINS fusion glycoprotein F1; fusion glycoprotein F2 ORGANISM #formal_name parainfluenza virus type 3 #note host Homo sapiens (man) DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 07-May-1999 ACCESSIONS A47610 REFERENCE A47610 !$#authors Spriggs, M.K.; Olmsted, R.A.; Venkatesan, S.; Coligan, J.E.; !1Collins, P.L. !$#journal Virology (1986) 152:241-251 !$#title Fusion glycoprotein of human parainfluenza virus type 3: !1nucleotide sequence of the gene, direct identification of !1the cleavage-activation site, and comparison with other !1paramyxoviruses. !$#cross-references MUID:86237106; PMID:3012869 !$#accession A47610 !'##molecule_type mRNA !'##residues 1-539 ##label SPR !'##cross-references GB:M14892 GENETICS !$#gene F CLASSIFICATION #superfamily parainfluenza virus cell fusion protein KEYWORDS glycoprotein; membrane fusion; transmembrane protein FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-109 #product cell fusion glycoprotein F2 #status !8predicted #label F2P\ !$110-539 #product cell fusion glycoprotein F1 #status !8predicted #label F1P\ !$110-135 #region hydrophobic\ !$494-514 #domain transmembrane #status predicted #label TMN\ !$33,238,359,446 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 539 #molecular-weight 60020 #checksum 4450 SEQUENCE /// ENTRY VGNZB3 #type complete TITLE cell fusion glycoprotein precursor - parainfluenza virus type 3 ORGANISM #formal_name parainfluenza virus type 3 DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 24-Oct-1997 ACCESSIONS A27218 REFERENCE A93659 !$#authors Suzu, S.; Sakai, Y.; Shioda, T.; Shibuta, H. !$#journal Nucleic Acids Res. (1987) 15:2945-2958 !$#title Nucleotide sequence of the bovine parainfluenza 3 virus !1genome: the genes of the F and HN glycoproteins. !$#cross-references MUID:87174819; PMID:3031615 !$#accession A27218 !'##molecule_type genomic RNA !'##residues 1-540 ##label SUZ !'##cross-references EMBL:Y00114 GENETICS !$#gene F CLASSIFICATION #superfamily parainfluenza virus cell fusion protein KEYWORDS glycoprotein; membrane fusion; transmembrane protein FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-109 #product cell fusion glycoprotein F2 #status !8predicted #label GF2\ !$110-540 #product cell fusion glycoprotein F1 #status !8predicted #label GF1\ !$118-134 #domain transmembrane #status predicted #label TM2\ !$496-512 #domain transmembrane #status predicted #label TM3\ !$101,238,359,402, !$446,508 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 540 #molecular-weight 59993 #checksum 7482 SEQUENCE /// ENTRY E48556 #type complete TITLE cell fusion glycoprotein precursor - measles virus (strain AIK-C) ORGANISM #formal_name measles virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS E48556 REFERENCE A48556 !$#authors Mori, T.; Sasaki, K.; Hashimoto, H.; Makino, S. !$#journal Virus Genes (1993) 7:67-81 !$#title Molecular cloning and complete nucleotide sequence of !1genomic RNA of the AIK-C strain of attenuated measles virus. !$#cross-references MUID:93227570; PMID:8470368 !$#accession E48556 !'##molecule_type genomic RNA !'##residues 1-550 ##label MOR !'##cross-references GB:S58435; NID:g299460; PIDN:AAB26145.1; !1PID:g299465 !'##note sequence extracted from NCBI backbone (NCBIN:129264, !1NCBIP:129272) GENETICS !$#gene F CLASSIFICATION #superfamily parainfluenza virus cell fusion protein KEYWORDS glycoprotein; membrane fusion; transmembrane protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-107 #product cell fusion glycoprotein F2 #status !8predicted #label FF2\ !$108-550 #product cell fusion glycoprotein F1 #status !8predicted #label FF1\ !$113-138 #region hydrophobic\ !$495-514 #domain transmembrane #status predicted #label TMM\ !$6,29,61,67 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 550 #molecular-weight 59540 #checksum 5075 SEQUENCE /// ENTRY VGNZMV #type complete TITLE cell fusion glycoprotein precursor - measles virus ORGANISM #formal_name measles virus DATE 31-Mar-1988 #sequence_revision 31-Mar-1989 #text_change 16-Jun-2000 ACCESSIONS A26962; A25616; PQ0380; PQ0384 REFERENCE A92794 !$#authors Buckland, R.; Gerald, C.; Barker, R.; Wild, T.F. !$#journal J. Gen. Virol. (1987) 68:1695-1703 !$#title Fusion glycoprotein of measles virus: nucleotide sequence of !1the gene and comparison with other paramyxoviruses. !$#cross-references MUID:87224816; PMID:3585281 !$#accession A26962 !'##molecule_type mRNA !'##residues 1-553 ##label BUC !'##cross-references GB:D00090; NID:g222061; PIDN:BAA00056.1; !1PID:g222062 !'##experimental_source strain Halle REFERENCE A94350 !$#authors Richardson, C.; Hull, D.; Greer, P.; Hasel, K.; Berkovich, !1A.; Englund, G.; Bellini, W.; Rima, B.; Lazzarini, R. !$#journal Virology (1986) 155:508-523 !$#title The nucleotide sequence of the mRNA encoding the fusion !1protein of measles virus (Edmonston strain): a comparison of !1fusion proteins from several different paramyxoviruses. !$#cross-references MUID:87071668; PMID:3788062 !$#accession A25616 !'##molecule_type mRNA !'##residues 4-553 ##label RIC !'##cross-references GB:M14915; NID:g331762; PIDN:AAA46423.1; !1PID:g331763 !'##experimental_source strain Edmonston REFERENCE PQ0374 !$#authors Schulz, T.F.; Hoad, J.G.; Whitby, D.; Tizard, E.J.; Dillon, !1M.J.; Weiss, R.A. !$#journal J. Gen. Virol. (1992) 73:1581-1586 !$#title A measles virus isolate from a child with Kawasaki disease: !1sequence comparison with contemporaneous isolates from !1'classical' cases. !$#cross-references MUID:92300360; PMID:1607874 !$#accession PQ0380 !'##molecule_type genomic RNA !'##residues 272-553 ##label SCH1 !'##experimental_source isolate CL !$#accession PQ0384 !'##molecule_type genomic RNA !'##residues 272-553 ##label SCH2 !'##experimental_source isolate SE GENETICS !$#gene F CLASSIFICATION #superfamily parainfluenza virus cell fusion protein KEYWORDS glycoprotein; membrane fusion; transmembrane protein FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-110 #product cell fusion glycoprotein F2 #status !8predicted #label FF2\ !$111-553 #product cell fusion glycoprotein F1 #status !8predicted #label FF1\ !$501-517 #domain transmembrane #status predicted #label TMN\ !$32,64,70 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 553 #molecular-weight 59863 #checksum 5706 SEQUENCE /// ENTRY JU0274 #type complete TITLE cell fusion glycoprotein precursor - subacute sclerosing panencephalitis virus (strain Yamagata-1) CONTAINS fusion glycoprotein F1; fusion glycoprotein F2 ORGANISM #formal_name subacute sclerosing panencephalitis virus, SSPEV DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jun-2000 ACCESSIONS JU0274 REFERENCE JU0274 !$#authors Komase, K.; Haga, T.; Yoshikawa, Y.; Sato, T.A.; Yamanouchi, !1K. !$#journal Virus Genes (1990) 4:173-181 !$#title Molecular analysis of structural protein genes of the !1Yamagata-1 strain of defective subacute sclerosing !1panencephalitis virus. IV. Nucleotide sequence of the fusion !1gene. !$#cross-references MUID:90385702; PMID:1698327 !$#accession JU0274 !'##molecule_type mRNA !'##residues 1-534 ##label KOM !'##cross-references EMBL:D10548; NID:g222256; PIDN:BAA01405.1; !1PID:g222257 !'##note the authors translated the codon GTA for residue 459 as Gly and !1GGG for residue 460 as Val GENETICS !$#gene F CLASSIFICATION #superfamily parainfluenza virus cell fusion protein KEYWORDS glycoprotein; membrane fusion; transmembrane protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-107 #product cell fusion glycoprotein F2 #status !8predicted #label FF2\ !$108-534 #product cell fusion glycoprotein F1 #status !8predicted #label FF1\ !$498-514 #domain transmembrane #status predicted #label TMN\ !$6,29,61,67 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 534 #molecular-weight 57963 #checksum 8311 SEQUENCE /// ENTRY VGNZRL #type complete TITLE cell fusion glycoprotein precursor - rinderpest virus (strain L) CONTAINS fusion glycoprotein F1; fusion glycoprotein F2 ORGANISM #formal_name rinderpest virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS A28921 REFERENCE A28921 !$#authors Tsukiyama, K.; Yoshikawa, Y.; Yamanouchi, K. !$#journal Virology (1988) 164:523-530 !$#title Fusion glycoprotein (F) of rinderpest virus: entire !1nucleotide sequence of the F mRNA, and several features of !1the F protein. !$#cross-references MUID:88219541; PMID:3285575 !$#accession A28921 !'##molecule_type mRNA !'##residues 1-546 ##label TSU !'##cross-references GB:M20870; NID:g333898; PIDN:AAA47399.1; !1PID:g333899 GENETICS !$#gene F CLASSIFICATION #superfamily parainfluenza virus cell fusion protein KEYWORDS glycoprotein; membrane fusion; transmembrane protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-104 #product cell fusion glycoprotein F2 #status !8predicted #label FG2\ !$105-546 #product cell fusion glycoprotein F1 #status !8predicted #label FG1\ !$109-133 #domain transmembrane #status predicted #label TN1\ !$485-513 #domain transmembrane #status predicted #label TN2\ !$25,57,63 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 546 #molecular-weight 58911 #checksum 5680 SEQUENCE /// ENTRY VGNZRK #type complete TITLE cell fusion glycoprotein precursor - rinderpest virus (strain Kabete O) CONTAINS fusion glycoprotein F1; fusion glycoprotein F2 ORGANISM #formal_name rinderpest virus DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 25-Oct-1996 ACCESSIONS A31051 REFERENCE A31051 !$#authors Hsu, D.; Yamanaka, M.; Miller, J.; Dale, B.; Grubman, M.; !1Yilma, T. !$#journal Virology (1988) 166:149-153 !$#title Cloning of the fusion gene of rinderpest virus: comparative !1sequence analysis with other morbilliviruses. !$#cross-references MUID:88322864; PMID:3413983 !$#accession A31051 !'##molecule_type genomic RNA !'##residues 1-546 ##label HSU GENETICS !$#gene F CLASSIFICATION #superfamily parainfluenza virus cell fusion protein KEYWORDS glycoprotein; membrane fusion; transmembrane protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-108 #product cell fusion glycoprotein F2 #status !8predicted #label FF1\ !$109-546 #product cell fusion glycoprotein F1 #status !8predicted #label FF2\ !$109-134 #domain transmembrane #status predicted #label TN1\ !$491-513 #domain transmembrane #status predicted #label TN2\ !$25,57,63,518 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 546 #molecular-weight 58747 #checksum 2641 SEQUENCE /// ENTRY VGNZCD #type complete TITLE cell fusion glycoprotein precursor - canine distemper virus CONTAINS fusion protein F1; fusion protein F2 ORGANISM #formal_name canine distemper virus DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS JS0321 REFERENCE JS0321 !$#authors Barrett, T.; Clarke, D.K.; Evans, S.A.; Rima, B.K. !$#journal Virus Res. (1987) 8:373-386 !$#title The nucleotide sequence of the gene encoding the F protein !1of canine distemper virus: a comparison of the deduced amino !1acid sequence with other paramyxoviruses. !$#cross-references MUID:88129050; PMID:3433924 !$#accession JS0321 !'##molecule_type mRNA !'##residues 1-662 ##label BAR !'##cross-references GB:M21849; NID:g323241; PIDN:AAA42878.1; !1PID:g323242 GENETICS !$#gene F CLASSIFICATION #superfamily parainfluenza virus cell fusion protein KEYWORDS glycoprotein; membrane fusion; transmembrane protein FEATURE !$1-135 #domain signal sequence #status predicted #label SIG\ !$136-224 #product cell fusion glycoprotein F2 #status !8predicted #label F2P\ !$225-662 #product cell fusion glycoprotein F1 #status !8predicted #label F1P\ !$606-629 #domain transmembrane #status predicted #label MEM\ !$62,141,173,179,517 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 662 #molecular-weight 72970 #checksum 8624 SEQUENCE /// ENTRY VGNZPD #type complete TITLE cell fusion glycoprotein precursor - phocine distemper virus CONTAINS fusion protein F1; fusion protein F2 ORGANISM #formal_name phocine distemper virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 25-Oct-1996 ACCESSIONS JQ1368 REFERENCE JQ1368 !$#authors Koevamees, J.; Blixenkrone-Moeller, M.; Sharma, B.; Oervell, !1C.; Norrby, E. !$#journal J. Gen. Virol. (1991) 72:2959-2966 !$#title The nucleotide sequence and deduced amino acid composition !1of the haemagglutinin and fusion proteins of the !1morbillivirus phocid distemper virus. !$#cross-references MUID:92113538; PMID:1765768 !$#accession JQ1368 !'##molecule_type genomic RNA !'##residues 1-631 ##label KOV GENETICS !$#gene F CLASSIFICATION #superfamily parainfluenza virus cell fusion protein KEYWORDS glycoprotein; membrane fusion; transmembrane protein FEATURE !$1-188 #product cell fusion glycoprotein F2 #status !8predicted #label FP2\ !$89-106 #domain transmembrane #status predicted #label TM1\ !$189-193 #region cleavage processing #status predicted\ !$194-631 #product cell fusion glycoprotein F1 #status !8predicted #label FP1\ !$194-212 #domain transmembrane #status predicted #label TM2\ !$575-595 #domain transmembrane #status predicted #label TM3\ !$110,142,148,486 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 631 #molecular-weight 68873 #checksum 7841 SEQUENCE /// ENTRY A48346 #type complete TITLE cell fusion glycoprotein precursor - phocine distemper virus (strain Ulster/88) CONTAINS fusion protein F1; fusion protein F2 ORGANISM #formal_name phocine distemper virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 25-Oct-1996 ACCESSIONS A48346 REFERENCE A48346 !$#authors Curran, M.D.; Lu, Y.J.; Rima, B.K. !$#journal Arch. Virol. (1992) 126:159-169 !$#title The fusion protein gene of phocine distemper virus: !1nucleotide and deduced amino acid sequences and a comparison !1of morbillivirus fusion proteins. !$#cross-references MUID:92398437; PMID:1524494 !$#accession A48346 !'##molecule_type mRNA !'##residues 1-631 ##label CUR !'##note sequence extracted from NCBI backbone (NCBIN:113098, !1NCBIP:113099) GENETICS !$#gene F CLASSIFICATION #superfamily parainfluenza virus cell fusion protein KEYWORDS glycoprotein; membrane fusion; transmembrane protein FEATURE !$1-188 #product cell fusion glycoprotein F2 #status !8predicted #label FP2\ !$89-106 #domain transmembrane #status predicted #label TM1\ !$194-631 #product cell fusion glycoprotein F1 #status !8predicted #label FP1\ !$194-219 #domain transmembrane #status predicted #label TM2\ !$575-595 #domain transmembrane #status predicted #label TM3\ !$110,142 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 631 #molecular-weight 68859 #checksum 7919 SEQUENCE /// ENTRY VGNZNV #type complete TITLE cell fusion glycoprotein precursor - Newcastle disease virus (strains Beaudette C and BEA/45) CONTAINS fusion glycoprotein F1; fusion glycoprotein F2 ORGANISM #formal_name Newcastle disease virus DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jul-1999 ACCESSIONS A27008; F46329 REFERENCE A27008 !$#authors Chambers, P.; Millar, N.S.; Emmerson, P.T. !$#journal J. Gen. Virol. (1986) 67:2685-2694 !$#title Nucleotide sequence of the gene encoding the fusion !1glycoprotein of Newcastle disease virus. !$#cross-references MUID:87085486; PMID:3025345 !$#accession A27008 !'##molecule_type mRNA !'##residues 1-553 ##label CHA !'##cross-references GB:X04719; NID:g60933; PIDN:CAA28426.1; PID:g60934 !'##experimental_source strain Beaudette C REFERENCE A46329 !$#authors Toyoda, T.; Sakaguchi, T.; Hirota, H.; Gotoh, B.; Kuma, K.; !1Miyata, T.; Nagai, Y. !$#journal Virology (1989) 169:273-282 !$#title Newcastle disease virus evolution. II. Lack of gene !1recombination in generating virulent and avirulent strains. !$#cross-references MUID:89204898; PMID:2705298 !$#accession F46329 !'##molecule_type genomic RNA !'##residues 1-553 ##label TOY !'##cross-references GB:M24697; NID:g293929; PIDN:AAA46648.1; !1PID:g293930 !'##experimental_source strain BEA/45 GENETICS !$#gene F CLASSIFICATION #superfamily parainfluenza virus cell fusion protein KEYWORDS glycoprotein; membrane fusion; transmembrane protein FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-117 #product cell fusion glycoprotein F2 #status !8predicted #label FF2\ !$118-553 #product cell fusion glycoprotein F1 #status !8predicted #label FF1\ !$495-528 #domain transmembrane #status predicted #label TMN\ !$85,191,366,447,471 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 553 #molecular-weight 59041 #checksum 9131 SEQUENCE /// ENTRY VGNZGB #type complete TITLE cell fusion glycoprotein precursor - Newcastle disease virus (strain Texas G.B.) CONTAINS fusion glycoprotein F1; fusion glycoprotein F2 ORGANISM #formal_name Newcastle disease virus DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 25-Oct-1996 ACCESSIONS B29201 REFERENCE A94379 !$#authors Schaper, U.M.; Fuller, F.J.; Ward, M.D.W.; Mehrotra, Y.; !1Stone, H.O.; Stripp, B.R.; De Buysscher, E.V. !$#journal Virology (1988) 165:291-295 !$#title Nucleotide sequence of the envelope protein genes of a !1highly virulent, neurotropic strain of Newcastle disease !1virus. !$#cross-references MUID:88265873; PMID:3388773 !$#accession B29201 !'##molecule_type mRNA !'##residues 1-553 ##label SCH !'##experimental_source strain Texas G.B. GENETICS !$#gene F CLASSIFICATION #superfamily parainfluenza virus cell fusion protein KEYWORDS glycoprotein; membrane fusion; transmembrane protein FEATURE !$1-31 #domain signal sequence #status predicted #label SIG\ !$32-111 #product cell fusion glycoprotein F2 #status !8predicted #label FP2\ !$112-116 #region cleavage processing #status predicted\ !$117-553 #product cell fusion glycoprotein F1 #status !8predicted #label FP1\ !$9,85,191,366,447, !$471,541 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 553 #molecular-weight 58987 #checksum 9003 SEQUENCE /// ENTRY D46329 #type complete TITLE cell fusion glycoprotein precursor - Newcastle disease virus (strain BI/47) CONTAINS fusion glycoprotein F1; fusion glycoprotein F2 ORGANISM #formal_name Newcastle disease virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS D46329 REFERENCE A46329 !$#authors Toyoda, T.; Sakaguchi, T.; Hirota, H.; Gotoh, B.; Kuma, K.; !1Miyata, T.; Nagai, Y. !$#journal Virology (1989) 169:273-282 !$#title Newcastle disease virus evolution. II. Lack of gene !1recombination in generating virulent and avirulent strains. !$#cross-references MUID:89204898; PMID:2705298 !$#accession D46329 !'##molecule_type genomic RNA !'##residues 1-553 ##label TOY !'##cross-references GB:M24695; NID:g293925; PIDN:AAA46646.1; !1PID:g293926 GENETICS !$#gene F CLASSIFICATION #superfamily parainfluenza virus cell fusion protein KEYWORDS glycoprotein; membrane fusion; transmembrane protein FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-117 #product cell fusion glycoprotein F2 #status !8predicted #label FF2\ !$118-553 #product cell fusion glycoprotein F1 #status !8predicted #label FF1\ !$495-528 #domain transmembrane #status predicted #label TMN\ !$85,191,366,447,471 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 553 #molecular-weight 58909 #checksum 8285 SEQUENCE /// ENTRY E46329 #type complete TITLE cell fusion glycoprotein precursor - Newcastle disease virus (strain LAS/46) CONTAINS fusion glycoprotein F1; fusion glycoprotein F2 ORGANISM #formal_name Newcastle disease virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS E46329 REFERENCE A46329 !$#authors Toyoda, T.; Sakaguchi, T.; Hirota, H.; Gotoh, B.; Kuma, K.; !1Miyata, T.; Nagai, Y. !$#journal Virology (1989) 169:273-282 !$#title Newcastle disease virus evolution. II. Lack of gene !1recombination in generating virulent and avirulent strains. !$#cross-references MUID:89204898; PMID:2705298 !$#accession E46329 !'##molecule_type genomic RNA !'##residues 1-553 ##label TOY !'##cross-references GB:M24696; NID:g293927; PIDN:AAA46647.1; !1PID:g293928 GENETICS !$#gene F CLASSIFICATION #superfamily parainfluenza virus cell fusion protein KEYWORDS glycoprotein; membrane fusion; transmembrane protein FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-117 #product cell fusion glycoprotein F2 #status !8predicted #label FF2\ !$118-553 #product cell fusion glycoprotein F1 #status !8predicted #label FF1\ !$495-528 #domain transmembrane #status predicted #label TMN\ !$85,191,366,447,471 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 553 #molecular-weight 59047 #checksum 8769 SEQUENCE /// ENTRY G46329 #type complete TITLE cell fusion glycoprotein precursor - Newcastle disease virus (strain TEX/48) CONTAINS fusion glycoprotein F1; fusion glycoprotein F2 ORGANISM #formal_name Newcastle disease virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS G46329; S11266 REFERENCE A46329 !$#authors Toyoda, T.; Sakaguchi, T.; Hirota, H.; Gotoh, B.; Kuma, K.; !1Miyata, T.; Nagai, Y. !$#journal Virology (1989) 169:273-282 !$#title Newcastle disease virus evolution. II. Lack of gene !1recombination in generating virulent and avirulent strains. !$#cross-references MUID:89204898; PMID:2705298 !$#accession G46329 !'##molecule_type genomic RNA !'##residues 1-553 ##label TOY !'##cross-references GB:M24698; NID:g293931; PIDN:AAA46649.1; !1PID:g293932 REFERENCE S11266 !$#authors Richardson, C.D.; Scheid, A.; Choppin, P.W. !$#journal Virology (1980) 105:205-222 !$#title Specific inhibition of paramyxovirus and myxovirus !1replication by oligopeptides with amino acid sequences !1similar to those at the N-termini of the F1 or HA2 viral !1polypeptides. !$#cross-references MUID:81016739; PMID:7414950 !$#accession S11266 !'##molecule_type protein !'##residues 117-136 ##label RIC GENETICS !$#gene F CLASSIFICATION #superfamily parainfluenza virus cell fusion protein KEYWORDS glycoprotein; membrane fusion; transmembrane protein FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-117 #product cell fusion glycoprotein F2 #status !8predicted #label FF2\ !$118-553 #product cell fusion glycoprotein F1 #status !8predicted #label FF1\ !$495-528 #domain transmembrane #status predicted #label TMN\ !$85,191,366,447,471 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 553 #molecular-weight 59017 #checksum 9291 SEQUENCE /// ENTRY VGNZTE #type complete TITLE cell fusion glycoprotein precursor - Newcastle disease virus (strain Texas) CONTAINS fusion glycoprotein F1; fusion glycoprotein F2 ORGANISM #formal_name Newcastle disease virus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jul-1999 ACCESSIONS A34663 REFERENCE A34663 !$#authors Taylor, J.; Edbauer, C.; Rey-Senelonge, A.; Bouquet, J.F.; !1Norton, E.; Goebel, S.; Desmettre, P.; Paoletti, E. !$#journal J. Virol. (1990) 64:1441-1450 !$#title Newcastle disease virus fusion protein expressed in a !1fowlpox virus recombinant confers protection in chickens. !$#cross-references MUID:90204652; PMID:2157037 !$#accession A34663 !'##molecule_type genomic RNA !'##residues 1-553 ##label TAY !'##cross-references EMBL:M33855; NID:g332369; PIDN:AAA46675.1; !1PID:g332370 GENETICS !$#gene F CLASSIFICATION #superfamily parainfluenza virus cell fusion protein KEYWORDS glycoprotein; membrane fusion; transmembrane protein FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-116 #product cell fusion glycoprotein F2 #status !8predicted #label FF2\ !$112-116 #region cleavage processing #status predicted\ !$117-553 #product cell fusion glycoprotein F1 #status !8predicted #label FF1\ !$117-133 #domain transmembrane #status predicted #label TM1\ !$504-521 #domain transmembrane #status predicted #label TM2\ !$85,191,366,447,471, !$541 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 553 #molecular-weight 59042 #checksum 9848 SEQUENCE /// ENTRY A36830 #type complete TITLE cell fusion glycoprotein precursor - Newcastle disease virus (strain HER/33) CONTAINS fusion glycoprotein F1; fusion glycoprotein F2 ORGANISM #formal_name Newcastle disease virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS A36830 REFERENCE A46329 !$#authors Toyoda, T.; Sakaguchi, T.; Hirota, H.; Gotoh, B.; Kuma, K.; !1Miyata, T.; Nagai, Y. !$#journal Virology (1989) 169:273-282 !$#title Newcastle disease virus evolution. II. Lack of gene !1recombination in generating virulent and avirulent strains. !$#cross-references MUID:89204898; PMID:2705298 !$#accession A36830 !'##molecule_type genomic RNA !'##residues 1-553 ##label TOY !'##cross-references GB:M24702; NID:g293937; PIDN:AAA46652.1; !1PID:g293938 GENETICS !$#gene F CLASSIFICATION #superfamily parainfluenza virus cell fusion protein KEYWORDS glycoprotein; membrane fusion; transmembrane protein FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-117 #product cell fusion glycoprotein F2 #status !8predicted #label FF2\ !$118-553 #product cell fusion glycoprotein F1 #status !8predicted #label FF1\ !$495-528 #domain transmembrane #status predicted #label TMN\ !$85,191,366,447,471 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 553 #molecular-weight 59129 #checksum 739 SEQUENCE /// ENTRY B36830 #type complete TITLE cell fusion glycoprotein precursor - Newcastle disease virus (strain ITA/45) CONTAINS fusion glycoprotein F1; fusion glycoprotein F2 ORGANISM #formal_name Newcastle disease virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 07-May-1999 ACCESSIONS B36830 REFERENCE A46329 !$#authors Toyoda, T.; Sakaguchi, T.; Hirota, H.; Gotoh, B.; Kuma, K.; !1Miyata, T.; Nagai, Y. !$#journal Virology (1989) 169:273-282 !$#title Newcastle disease virus evolution. II. Lack of gene !1recombination in generating virulent and avirulent strains. !$#cross-references MUID:89204898; PMID:2705298 !$#accession B36830 !'##molecule_type genomic RNA !'##residues 1-553 ##label TOY !'##cross-references GB:M24703 GENETICS !$#gene F CLASSIFICATION #superfamily parainfluenza virus cell fusion protein KEYWORDS glycoprotein; membrane fusion; transmembrane protein FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-117 #product cell fusion glycoprotein F2 #status !8predicted #label FF2\ !$118-553 #product cell fusion glycoprotein F1 #status !8predicted #label FF1\ !$495-528 #domain transmembrane #status predicted #label TMN\ !$85,191,366,447,471 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 553 #molecular-weight 59244 #checksum 9880 SEQUENCE /// ENTRY VGNZND #type complete TITLE cell fusion glycoprotein precursor - Newcastle disease virus (strain Miyadera) ORGANISM #formal_name Newcastle disease virus DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 16-Jul-1999 ACCESSIONS A26185 REFERENCE A26185 !$#authors Toyoda, T.; Sakaguchi, T.; Imai, K.; Inocencio, N.M.; Gotoh, !1B.; Hamaguchi, M.; Nagai, Y. !$#journal Virology (1987) 158:242-247 !$#title Structural comparison of the cleavage-activation site of the !1fusion glycoprotein between virulent and avirulent strains !1of Newcastle disease virus. !$#cross-references MUID:87207668; PMID:3576973 !$#accession A26185 !'##molecule_type mRNA !'##residues 1-553 ##label TOY !'##cross-references GB:M18456; NID:g332318; PIDN:AAA46639.1; !1PID:g332319 GENETICS !$#gene F CLASSIFICATION #superfamily parainfluenza virus cell fusion protein KEYWORDS glycoprotein; membrane fusion; transmembrane protein FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-116 #product cell fusion glycoprotein F2 #status !8predicted #label FF2\ !$117-553 #product cell fusion glycoprotein F1 #status !8predicted #label FF1\ !$117-142 #domain fusion-inducing hydrophobic region #status !8predicted #label FIH\ !$499-526 #domain transmembrane #status predicted #label TMN\ !$85,191,192,366,447, !$471,497 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 553 #molecular-weight 59058 #checksum 9480 SEQUENCE /// ENTRY I46329 #type complete TITLE cell fusion glycoprotein precursor - Newcastle disease virus (strain MIY/51) CONTAINS fusion glycoprotein F1; fusion glycoprotein F2 ORGANISM #formal_name Newcastle disease virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 07-May-1999 ACCESSIONS I46329 REFERENCE A46329 !$#authors Toyoda, T.; Sakaguchi, T.; Hirota, H.; Gotoh, B.; Kuma, K.; !1Miyata, T.; Nagai, Y. !$#journal Virology (1989) 169:273-282 !$#title Newcastle disease virus evolution. II. Lack of gene !1recombination in generating virulent and avirulent strains. !$#cross-references MUID:89204898; PMID:2705298 !$#accession I46329 !'##molecule_type genomic RNA !'##residues 1-553 ##label TOY !'##cross-references GB:M24701 GENETICS !$#gene F CLASSIFICATION #superfamily parainfluenza virus cell fusion protein KEYWORDS glycoprotein; membrane fusion; transmembrane protein FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-117 #product cell fusion glycoprotein F2 #status !8predicted #label FF2\ !$118-553 #product cell fusion glycoprotein F1 #status !8predicted #label FF1\ !$497-528 #domain transmembrane #status predicted #label TMN\ !$85,191,192,366,447, !$471 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 553 #molecular-weight 59044 #checksum 9492 SEQUENCE /// ENTRY VGNZU1 #type complete TITLE cell fusion glycoprotein precursor - Newcastle disease virus (strains Ulster and ULS/67) CONTAINS fusion glycoprotein F1; fusion glycoprotein F2 ORGANISM #formal_name Newcastle disease virus DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jun-2000 ACCESSIONS A29823; C46329 REFERENCE A92799 !$#authors Millar, N.S.; Chambers, P.; Emmerson, P.T. !$#journal J. Gen. Virol. (1988) 69:613-620 !$#title Nucleotide sequence of the fusion and !1haemagglutinin-neuraminidase glycoprotein genes of Newcastle !1disease virus, strain Ulster: molecular basis for variations !1in pathogenicity between strains. !$#cross-references MUID:88171450; PMID:3351479 !$#accession A29823 !'##molecule_type mRNA !'##residues 1-553 ##label MIL !'##cross-references GB:D00243; NID:g222174; PIDN:BAA00173.1; !1PID:g222175 !'##experimental_source strain Ulster REFERENCE A46329 !$#authors Toyoda, T.; Sakaguchi, T.; Hirota, H.; Gotoh, B.; Kuma, K.; !1Miyata, T.; Nagai, Y. !$#journal Virology (1989) 169:273-282 !$#title Newcastle disease virus evolution. II. Lack of gene !1recombination in generating virulent and avirulent strains. !$#cross-references MUID:89204898; PMID:2705298 !$#accession C46329 !'##molecule_type genomic RNA !'##residues 1-553 ##label TOY !'##cross-references GB:M24694; NID:g293923; PIDN:AAA46645.1; !1PID:g293924 !'##experimental_source strain ULS/67 GENETICS !$#gene F CLASSIFICATION #superfamily parainfluenza virus cell fusion protein KEYWORDS glycoprotein; membrane fusion; transmembrane protein FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-117 #product cell fusion glycoprotein F2 #status !8predicted #label FF2\ !$118-553 #product cell fusion glycoprotein F1 #status !8predicted #label FF1\ !$495-528 #domain transmembrane #status predicted #label TMN\ !$85,191,366,447,471 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 553 #molecular-weight 58682 #checksum 9901 SEQUENCE /// ENTRY A46329 #type complete TITLE cell fusion glycoprotein precursor - Newcastle disease virus (strain D26/76) CONTAINS fusion glycoprotein F1; fusion glycoprotein F2 ORGANISM #formal_name Newcastle disease virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS A46329 REFERENCE A46329 !$#authors Toyoda, T.; Sakaguchi, T.; Hirota, H.; Gotoh, B.; Kuma, K.; !1Miyata, T.; Nagai, Y. !$#journal Virology (1989) 169:273-282 !$#title Newcastle disease virus evolution. II. Lack of gene !1recombination in generating virulent and avirulent strains. !$#cross-references MUID:89204898; PMID:2705298 !$#accession A46329 !'##molecule_type genomic RNA !'##residues 1-553 ##label TOY !'##cross-references GB:M24692; NID:g293919; PIDN:AAA46643.1; !1PID:g293920 GENETICS !$#gene F CLASSIFICATION #superfamily parainfluenza virus cell fusion protein KEYWORDS glycoprotein; membrane fusion; transmembrane protein FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-117 #product cell fusion glycoprotein F2 #status !8predicted #label FF2\ !$118-553 #product cell fusion glycoprotein F1 #status !8predicted #label FF1\ !$495-528 #domain transmembrane #status predicted #label TMN\ !$85,191,366,447,471 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 553 #molecular-weight 58891 #checksum 9009 SEQUENCE /// ENTRY B46329 #type complete TITLE cell fusion glycoprotein precursor - Newcastle disease virus (strain Que/66) CONTAINS fusion glycoprotein F1; fusion glycoprotein F2 ORGANISM #formal_name Newcastle disease virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS B46329 REFERENCE A46329 !$#authors Toyoda, T.; Sakaguchi, T.; Hirota, H.; Gotoh, B.; Kuma, K.; !1Miyata, T.; Nagai, Y. !$#journal Virology (1989) 169:273-282 !$#title Newcastle disease virus evolution. II. Lack of gene !1recombination in generating virulent and avirulent strains. !$#cross-references MUID:89204898; PMID:2705298 !$#accession B46329 !'##molecule_type genomic RNA !'##residues 1-553 ##label TOY !'##cross-references GB:M24693; NID:g293921; PIDN:AAA46644.1; !1PID:g293922 GENETICS !$#gene F CLASSIFICATION #superfamily parainfluenza virus cell fusion protein KEYWORDS glycoprotein; membrane fusion; transmembrane protein FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$26-117 #product cell fusion glycoprotein F2 #status !8predicted #label FF2\ !$118-553 #product cell fusion glycoprotein F1 #status !8predicted #label FF1\ !$495-528 #domain transmembrane #status predicted #label TMN\ !$85,191,366,447,471 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 553 #molecular-weight 58865 #checksum 141 SEQUENCE /// ENTRY H46329 #type complete TITLE cell fusion glycoprotein precursor - Newcastle disease virus CONTAINS fusion glycoprotein F1; fusion glycoprotein F2 ORGANISM #formal_name Newcastle disease virus DATE 31-Dec-1993 #sequence_revision 22-Oct-1999 #text_change 22-Oct-1999 ACCESSIONS S07422; H46329 REFERENCE S07422 !$#authors McGinnes, L.W.; Morrison, T.G. !$#journal Virus Res. (1986) 5:343-356 !$#title Nucleotide sequence of the gene encoding the Newcastle !1disease virus fusion protein and comparisons of !1paramyxovirus fusion protein sequences. !$#cross-references MUID:87044526; PMID:3776349 !$#accession S07422 !'##molecule_type mRNA !'##residues 1-553 ##label MCG !'##cross-references EMBL:M21881 !'##experimental_source strain Australia-Victoria REFERENCE A46329 !$#authors Toyoda, T.; Sakaguchi, T.; Hirota, H.; Gotoh, B.; Kuma, K.; !1Miyata, T.; Nagai, Y. !$#journal Virology (1989) 169:273-282 !$#title Newcastle disease virus evolution. II. Lack of gene !1recombination in generating virulent and avirulent strains. !$#cross-references MUID:89204898; PMID:2705298 !$#accession H46329 !'##molecule_type genomic RNA !'##residues 1-65,'H',67-553 ##label TOY !'##cross-references GB:M24700; NID:g293933; PIDN:AAA46650.1; !1PID:g293934 !'##experimental_source strain AUS/32 GENETICS !$#gene F CLASSIFICATION #superfamily parainfluenza virus cell fusion protein KEYWORDS glycoprotein; membrane fusion; transmembrane protein FEATURE !$1-25 #domain signal sequence #status predicted #label SIG\ !$25-116 #product cell fusion glycoprotein F2 #status !8predicted #label FF2\ !$112-116 #region cleavage processing #status predicted\ !$117-553 #product cell fusion glycoprotein F1 #status !8experimental #label FF1\ !$499-526 #domain transmembrane #status predicted #label TMM\ !$85,191,366,447,471 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$85,191,366,447,471, !$541 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 553 #molecular-weight 58998 #checksum 8234 SEQUENCE /// ENTRY VGNZMU #type complete TITLE cell fusion glycoprotein precursor - mumps virus (strain RW) CONTAINS fusion glycoprotein F1; fusion glycoprotein F2 ORGANISM #formal_name mumps virus DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jul-1999 ACCESSIONS A29124 REFERENCE A29124 !$#authors Waxham, M.N.; Server, A.C.; Goodman, H.M.; Wolinsky, J.S. !$#journal Virology (1987) 159:381-388 !$#title Cloning and sequencing of the mumps virus fusion protein !1gene. !$#cross-references MUID:87293896; PMID:3617503 !$#accession A29124 !'##molecule_type mRNA !'##residues 1-538 ##label WAX !'##cross-references GB:M17142; NID:g332273; PIDN:AAA46608.1; !1PID:g332274 GENETICS !$#gene F CLASSIFICATION #superfamily parainfluenza virus cell fusion protein KEYWORDS glycoprotein; membrane fusion; transmembrane protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-97 #product cell fusion glycoprotein F2 #status !8predicted #label FF2\ !$98-538 #product cell fusion glycoprotein F1 #status !8predicted #label FF1\ !$483-512 #domain transmembrane #status predicted #label TMN\ !$73,182,352,427,433, !$457 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 538 #molecular-weight 58760 #checksum 6572 SEQUENCE /// ENTRY VGNZMM #type complete TITLE cell fusion glycoprotein precursor - mumps virus (strain Miyahara) CONTAINS fusion glycoprotein F1; fusion glycoprotein F2 ORGANISM #formal_name mumps virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS A34062; S04879 REFERENCE A34062 !$#authors Takeuchi, K.; Tanabayashi, K.; Hishiyama, M.; Yamada, A.; !1Sugiura, A. !$#journal Nucleic Acids Res. (1989) 17:5839 !$#title Cloning and sequencing of the fusion protein gene of mumps !1virus (Miyahara strain). !$#cross-references MUID:89345174; PMID:2762156 !$#accession A34062 !'##molecule_type mRNA !'##residues 1-538 ##label TAK !'##cross-references GB:X15285; NID:g60580; PIDN:CAA33359.1; PID:g60581 GENETICS !$#gene F CLASSIFICATION #superfamily parainfluenza virus cell fusion protein KEYWORDS glycoprotein; membrane fusion; transmembrane protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-97 #product cell fusion glycoprotein F2 #status !8predicted #label GP2\ !$98-538 #product cell fusion glycoprotein F1 #status !8predicted #label GP1\ !$483-512 #domain transmembrane #status predicted #label TMN\ !$73,182,352,427,433, !$457 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 538 #molecular-weight 58711 #checksum 7733 SEQUENCE /// ENTRY VGNZMS #type complete TITLE cell fusion glycoprotein precursor - mumps virus (strain SBL-1) CONTAINS fusion glycoprotein F1; fusion glycoprotein F2 ORGANISM #formal_name mumps virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jun-2000 ACCESSIONS A31329 REFERENCE A31329 !$#authors Elango, N.; Varsanyi, T.M.; Koevamees, J.; Norrby, E. !$#journal J. Gen. Virol. (1989) 70:801-807 !$#title The mumps virus fusion protein mRNA sequence and homology !1among the paramyxoviridae proteins. !$#cross-references MUID:89279264; PMID:2732706 !$#accession A31329 !'##molecule_type mRNA !'##residues 1-538 ##label ELA !'##cross-references GB:D00426; NID:g222143; PIDN:BAA00330.1; !1PID:g222144 GENETICS !$#gene F CLASSIFICATION #superfamily parainfluenza virus cell fusion protein KEYWORDS glycoprotein; membrane fusion; transmembrane protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-97 #product cell fusion glycoprotein F2 #status !8predicted #label GP2\ !$98-538 #product cell fusion glycoprotein F1 #status !8predicted #label GP1\ !$483-512 #domain transmembrane #status predicted #label TMN\ !$73,89,182,352,427, !$433,457 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 538 #molecular-weight 58784 #checksum 8826 SEQUENCE /// ENTRY B60004 #type complete TITLE cell fusion glycoprotein precursor - mumps virus (strain SBL) CONTAINS fusion glycoprotein F1; fusion glycoprotein F2 ORGANISM #formal_name mumps virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jun-2000 ACCESSIONS B60004 REFERENCE A60004 !$#authors Elliott, G.D.; Afzal, M.A.; Martin, S.J.; Rima, B.K. !$#journal Virus Res. (1989) 12:61-75 !$#title Nucleotide sequence of the matrix, fusion and putative SH !1protein genes of mumps virus and their deduced amino acid !1sequences. !$#cross-references MUID:89243815; PMID:2718625 !$#accession B60004 !'##molecule_type mRNA !'##residues 1-538 ##label ELL !'##cross-references GB:D00663; NID:g222149; PIDN:BAA00561.1; !1PID:g222153 GENETICS !$#gene F CLASSIFICATION #superfamily parainfluenza virus cell fusion protein KEYWORDS glycoprotein; membrane fusion; transmembrane protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-97 #product cell fusion glycoprotein F2 #status !8predicted #label GP2\ !$98-538 #product cell fusion glycoprotein F1 #status !8predicted #label GP1\ !$483-512 #domain transmembrane #status predicted #label TMN\ !$73,89,182,352,427, !$433,457 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 538 #molecular-weight 58782 #checksum 9029 SEQUENCE /// ENTRY VGNZSP #type complete TITLE cell fusion glycoprotein precursor - simian paramyxovirus SV5 CONTAINS fusion glycoprotein F1; fusion glycoprotein F2 ORGANISM #formal_name simian paramyxovirus SV5 DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 13-Mar-1997 ACCESSIONS A21688; S11285 REFERENCE A21688 !$#authors Paterson, R.G.; Harris, T.J.R.; Lamb, R.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:6706-6710 !$#title Fusion protein of the paramyxovirus simian virus 5: !1nucleotide sequence of mRNA predicts a highly hydrophobic !1glycoprotein. !$#cross-references MUID:85038582; PMID:6093114 !$#accession A21688 !'##molecule_type mRNA !'##residues 1-529 ##label PAT REFERENCE S11266 !$#authors Richardson, C.D.; Scheid, A.; Choppin, P.W. !$#journal Virology (1980) 105:205-222 !$#title Specific inhibition of paramyxovirus and myxovirus !1replication by oligopeptides with amino acid sequences !1similar to those at the N-termini of the F1 or HA2 viral !1polypeptides. !$#cross-references MUID:81016739; PMID:7414950 !$#accession S11285 !'##molecule_type protein !'##residues 103-122 ##label RIC GENETICS !$#gene F CLASSIFICATION #superfamily parainfluenza virus cell fusion protein KEYWORDS glycoprotein; membrane fusion; transmembrane protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-97 #product cell fusion glycoprotein F2 #status !8predicted #label FUP\ !$103-529 #product cell fusion glycoprotein F1 #status !8predicted #label FUQ\ !$472-509 #domain transmembrane #status predicted #label TMM\ !$65,73,352,427,431, !$457 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 529 #molecular-weight 56596 #checksum 6878 SEQUENCE /// ENTRY VGNZ41 #type complete TITLE cell fusion glycoprotein precursor - simian paramyxovirus SV41 CONTAINS fusion glycoprotein F1; fusion glycoprotein F2 ORGANISM #formal_name simian paramyxovirus SV41 DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS B40563 REFERENCE A40563 !$#authors Tsurudome, M.; Bando, H.; Kawano, M.; Matsumura, H.; Komada, !1H.; Nishio, M.; Ito, Y. !$#journal Virology (1991) 184:93-100 !$#title Transcripts of simian virus 41 (SV41) matrix gene are !1exclusively dicistronic with the fusion gene which is also !1transcribed as a monocistron. !$#cross-references MUID:91335794; PMID:1651608 !$#accession B40563 !'##molecule_type genomic RNA !'##residues 1-561 ##label TSU !'##cross-references GB:S48627; NID:g233737; PIDN:AAB19494.1; !1PID:g233739 GENETICS !$#gene F CLASSIFICATION #superfamily parainfluenza virus cell fusion protein KEYWORDS glycoprotein; membrane fusion; transmembrane protein FEATURE !$1-28 #domain signal sequence #status predicted #label SIG\ !$29-109 #product cell fusion glycoprotein F2 #status !8predicted #label FG2\ !$110-561 #product cell fusion glycoprotein F1 #status !8predicted #label FG1\ !$110-126 #region hydrophobic\ !$226-243 #region hydrophobic\ !$491-507 #domain transmembrane #status predicted #label TM1\ !$72,80,359,434,440, !$464 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 561 #molecular-weight 59819 #checksum 8782 SEQUENCE /// ENTRY VGNZP2 #type complete TITLE cell fusion glycoprotein precursor - parainfluenza virus type 2 CONTAINS fusion glycoprotein F1; fusion glycoprotein F2 ORGANISM #formal_name parainfluenza virus type 2 DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jul-1999 ACCESSIONS A37078; A36423; S16662 REFERENCE A37078 !$#authors Kawano, M.; Bando, H.; Ohgimoto, S.; Kondo, K.; Tsurudome, !1M.; Nishio, M.; Ito, Y. !$#journal Virology (1990) 178:289-292 !$#title Sequence of the fusion protein gene of human parainfluenza !1type 2 virus and its 3' intergenic region: lack of small !1hydrophobic (SH) gene. !$#cross-references MUID:90357777; PMID:2167555 !$#accession A37078 !'##molecule_type genomic RNA !'##residues 1-551 ##label KAW1 !'##cross-references GB:M55698; NID:g332696; PIDN:AAA46842.1; !1PID:g332697 REFERENCE A36423 !$#authors Hu, X.; Compans, R.W.; Matsuoka, Y.; Ray, R. !$#journal Virology (1990) 179:915-920 !$#title Molecular cloning and sequence analysis of the fusion !1glycoprotein gene of human parainfluenza virus type 2. !$#cross-references MUID:91049467; PMID:2173268 !$#accession A36423 !'##molecule_type genomic RNA !'##residues 1-174,'H',176-247,'L',249-551 ##label HUX !'##cross-references GB:M60182; EMBL:M33816; NID:g332698; !1PIDN:AAA46843.1; PID:g332699 REFERENCE S16659 !$#authors Kawano, M.; Okamoto, K.; Bando, H.; Kondo, K.; Tsurudome, !1M.; Komada, H.; Nishio, M.; Ito, Y. !$#journal Nucleic Acids Res. (1991) 19:2739-2746 !$#title Characterizations of the human parainfluenza type 2 virus !1gene encoding the L protein and the intergenic sequences. !$#cross-references MUID:91252221; PMID:1645865 !$#accession S16662 !'##molecule_type genomic RNA !'##residues 1-551 ##label KAW2 !'##cross-references EMBL:X57559; NID:g61985; PIDN:CAA40786.1; !1PID:g61989 !'##experimental_source strain Toshiba !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1March 1991 GENETICS !$#gene F CLASSIFICATION #superfamily parainfluenza virus cell fusion protein KEYWORDS glycoprotein; membrane fusion; transmembrane protein FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-106 #product cell fusion glycoprotein F2 #status !8predicted #label FF2\ !$103-106 #region cleavage processing #status predicted\ !$107-551 #product cell fusion glycoprotein F1 #status !8predicted #label FF1\ !$107-132 #domain transmembrane #status predicted #label TM1\ !$492-513 #domain transmembrane #status predicted #label TM2\ !$65,69,77,90,431,461 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 551 #molecular-weight 59721 #checksum 8517 SEQUENCE /// ENTRY VGNZPG #type complete TITLE cell fusion glycoprotein precursor - parainfluenza virus type 2 (strain Greer) CONTAINS fusion glycoprotein F1; fusion glycoprotein F2 ORGANISM #formal_name parainfluenza virus type 2 DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 25-Oct-1996 ACCESSIONS A38509 REFERENCE A38509 !$#authors Varsanyi, T.M.; Koevamees, J.; Norrby, E. !$#journal J. Gen. Virol. (1991) 72:89-95 !$#title Molecular cloning and sequence analysis of human !1parainfluenza type 2 virus mRNA encoding the fusion !1glycoprotein. !$#cross-references MUID:91116325; PMID:1846648 !$#accession A38509 !'##molecule_type mRNA !'##residues 1-551 ##label VAR GENETICS !$#gene F CLASSIFICATION #superfamily parainfluenza virus cell fusion protein KEYWORDS glycoprotein; membrane fusion; transmembrane protein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-106 #product cell fusion glycoprotein F2 #status !8predicted #label FG2\ !$107-551 #product cell fusion glycoprotein F1 #status !8predicted #label FG1\ !$107-132 #domain transmembrane #status predicted #label TN1\ !$495-513 #domain transmembrane #status predicted #label TN2\ !$65,69,77,90,431,461 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 551 #molecular-weight 59623 #checksum 8444 SEQUENCE /// ENTRY MGNZ #type complete TITLE major surface glycoprotein G - human respiratory syncytial virus ORGANISM #formal_name human respiratory syncytial virus DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 24-Sep-1999 ACCESSIONS A94048; A93599; A04039 REFERENCE A94048 !$#authors Wertz, G.W.; Collins, P.L.; Huang, Y.; Gruber, C.; Levine, !1S.; Ball, L.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:4075-4079 !$#title Nucleotide sequence of the G protein gene of human !1respiratory syncytial virus reveals an unusual type of viral !1membrane protein. !$#cross-references MUID:85216636; PMID:3858865 !$#accession A94048 !'##molecule_type mRNA !'##residues 1-298 ##label WER !'##cross-references GB:M11486; GB:K01459; GB:K02719; GB:K03348; !1GB:K03349; GB:M11217; GB:M11244; GB:M11487; GB:M11505; !1GB:M11514; GB:M11631; GB:M12966; GB:X00001; GB:X02221; !1NID:g333925; PIDN:AAB59857.1; PID:g333932 !'##note residues 207-298 are identical with residues 376-467 of the !1nucleocapsid protein from this virus; these authors claim !1that the sequence reported for the nucleocapsid protein is !1incorrect !'##note this protein may carry 40-80 separate O-linked carbohydrate !1chains distributed among the 91 serine and threonine !1residues REFERENCE A93599 !$#authors Satake, M.; Coligan, J.E.; Elango, N.; Norrby, E.; !1Venkatesan, S. !$#journal Nucleic Acids Res. (1985) 13:7795-7812 !$#title Respiratory syncytial virus envelope glycoprotein (G) has a !1novel structure. !$#cross-references MUID:86067198; PMID:4069997 !$#accession A93599 !'##molecule_type mRNA !'##residues 1-298 ##label SAT !'##cross-references GB:X03149; NID:g60997; PIDN:CAA26928.1; PID:g60998 CLASSIFICATION #superfamily respiratory syncytial virus major surface !1glycoprotein G KEYWORDS glycoprotein; transmembrane protein FEATURE !$38-66 #domain transmembrane #status predicted #label TNM\ !$85,135,237,251 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 298 #molecular-weight 32586 #checksum 4914 SEQUENCE /// ENTRY MGNZRL #type complete TITLE major surface glycoprotein G - human respiratory syncytial virus (strain Long) ORGANISM #formal_name human respiratory syncytial virus DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Jul-1999 ACCESSIONS A32703; S12279 REFERENCE A32703 !$#authors Johnson, P.R.; Spriggs, M.K.; Olmsted, R.A.; Collins, P.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:5625-5629 !$#title The G glycoprotein of human respiratory syncytial viruses of !1subgroups A and B: extensive sequence divergence between !1antigenically related proteins. !$#cross-references MUID:87289657; PMID:2441388 !$#accession A32703 !'##molecule_type mRNA !'##residues 1-298 ##label JOH !'##cross-references GB:M17212; NID:g333940; PIDN:AAA47411.1; !1PID:g333941 REFERENCE S12279 !$#authors Garcia-Barreno, B.; Portela, A.; Delgado, T.; Lopez, J.A.; !1Melero, J.A. !$#journal EMBO J. (1990) 9:4181-4187 !$#title Frame shift mutations as a novel mechanism for the !1generation of neutralization resistant mutants of human !1respiratory syncytial virus. !$#cross-references MUID:91065351; PMID:2249671 !$#accession S12279 !'##molecule_type mRNA !'##residues 1-298 ##label GAR CLASSIFICATION #superfamily respiratory syncytial virus major surface !1glycoprotein G KEYWORDS glycoprotein; transmembrane protein FEATURE !$41-63 #domain transmembrane #status predicted #label TMN\ !$85,103,135,179,237, !$250,251,273,294 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 298 #molecular-weight 32781 #checksum 2959 SEQUENCE /// ENTRY MGNZ18 #type complete TITLE major surface glycoprotein G - human respiratory syncytial virus (strain 18537) ORGANISM #formal_name human respiratory syncytial virus DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Jul-1999 ACCESSIONS B32703 REFERENCE A32703 !$#authors Johnson, P.R.; Spriggs, M.K.; Olmsted, R.A.; Collins, P.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1987) 84:5625-5629 !$#title The G glycoprotein of human respiratory syncytial viruses of !1subgroups A and B: extensive sequence divergence between !1antigenically related proteins. !$#cross-references MUID:87289657; PMID:2441388 !$#accession B32703 !'##molecule_type mRNA !'##residues 1-292 ##label JOH !'##cross-references GB:M17213; NID:g333942; PIDN:AAA47412.1; !1PID:g333943 CLASSIFICATION #superfamily respiratory syncytial virus major surface !1glycoprotein G KEYWORDS glycoprotein; transmembrane protein FEATURE !$41-63 #domain transmembrane #status predicted #label TMN\ !$81,86,100 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 292 #molecular-weight 32306 #checksum 7174 SEQUENCE /// ENTRY MGNZ60 #type complete TITLE major surface glycoprotein G - human respiratory syncytial virus (strain 8/60) ALTERNATE_NAMES attachment glycoprotein G ORGANISM #formal_name human respiratory syncytial virus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jul-1999 ACCESSIONS A37077 REFERENCE A37077 !$#authors Sullender, W.M.; Anderson, K.; Wertz, G.W. !$#journal Virology (1990) 178:195-203 !$#title The respiratory syncytial virus subgroup B attachment !1glycoprotein: analysis of sequence, expression from a !1recombinant vector, and evaluation as an immunogen against !1homologous and heterologous subgroup virus challenge. !$#cross-references MUID:90357765; PMID:1697126 !$#accession A37077 !'##molecule_type mRNA !'##residues 1-292 ##label SUL !'##cross-references EMBL:M55633; NID:g333944; PIDN:AAA47413.1; !1PID:g333945 GENETICS !$#gene G CLASSIFICATION #superfamily respiratory syncytial virus major surface !1glycoprotein G KEYWORDS glycoprotein; transmembrane protein FEATURE !$45-63 #domain transmembrane #status predicted #label TMN\ !$81,86,100,230,290 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 292 #molecular-weight 32144 #checksum 7511 SEQUENCE /// ENTRY MGNZBR #type complete TITLE major surface glycoprotein G - bovine respiratory syncytial virus (strain 391-2) ALTERNATE_NAMES attachment glycoprotein G ORGANISM #formal_name bovine respiratory syncytial virus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jul-1999 ACCESSIONS A36408 REFERENCE A36408 !$#authors Lerch, R.A.; Anderson, K.; Wertz, G.W. !$#journal J. Virol. (1990) 64:5559-5569 !$#title Nucleotide sequence analysis and expression from recombinant !1vectors demonstrate that the attachment protein G of bovine !1respiratory syncytial virus is distinct from that of human !1respiratory syncytial virus. !$#cross-references MUID:91012801; PMID:2214024 !$#accession A36408 !'##molecule_type mRNA !'##residues 1-257 ##label LER !'##cross-references GB:M58307; NID:g210830; PIDN:AAA42810.1; !1PID:g210831 GENETICS !$#gene G CLASSIFICATION #superfamily respiratory syncytial virus major surface !1glycoprotein G KEYWORDS glycoprotein; transmembrane protein FEATURE !$45-62 #domain transmembrane #status predicted #label TMN\ !$3,85,127,149,233, !$251 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 257 #molecular-weight 28569 #checksum 686 SEQUENCE /// ENTRY MNNZC #type complete TITLE nonstructural protein C - measles virus ORGANISM #formal_name measles virus DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 16-Jul-1999 ACCESSIONS A04040 REFERENCE A93007 !$#authors Bellini, W.J.; Englund, G.; Rozenblatt, S.; Arnheiter, H.; !1Richardson, C.D. !$#journal J. Virol. (1985) 53:908-919 !$#title Measles virus P gene codes for two proteins. !$#cross-references MUID:85135038; PMID:3882996 !$#accession A04040 !'##molecule_type genomic RNA !'##residues 1-186 ##label BEL !'##cross-references GB:M10456; NID:g331803; PIDN:AAA46438.1; !1PID:g331805 !'##note the authors translated the codon AGG for residue 94 as Lys GENETICS !$#gene C CLASSIFICATION #superfamily measles virus nonstructural protein C KEYWORDS nonstructural protein SUMMARY #length 186 #molecular-weight 21037 #checksum 2080 SEQUENCE /// ENTRY C48556 #type complete TITLE nonstructural protein C - measles virus (strain AIK-C) ORGANISM #formal_name measles virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS C48556 REFERENCE A48556 !$#authors Mori, T.; Sasaki, K.; Hashimoto, H.; Makino, S. !$#journal Virus Genes (1993) 7:67-81 !$#title Molecular cloning and complete nucleotide sequence of !1genomic RNA of the AIK-C strain of attenuated measles virus. !$#cross-references MUID:93227570; PMID:8470368 !$#accession C48556 !'##molecule_type genomic RNA !'##residues 1-186 ##label MOR !'##cross-references GB:S58435; NID:g299460; PIDN:AAB26143.1; !1PID:g299463 !'##note sequence extracted from NCBI backbone (NCBIN:129264, !1NCBIP:129270) GENETICS !$#gene C CLASSIFICATION #superfamily measles virus nonstructural protein C KEYWORDS nonstructural protein SUMMARY #length 186 #molecular-weight 21113 #checksum 2200 SEQUENCE /// ENTRY B43387 #type complete TITLE nonstructural protein C - rinderpest virus (strain Kabete "O") ORGANISM #formal_name rinderpest virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS B43387 REFERENCE A43387 !$#authors Yamanaka, M.; Dale, B.; Crisp, T.; Cordell, B.; Grubman, M.; !1Yilma, T. !$#journal Virology (1992) 190:553-556 !$#title Sequence analysis and editing of the phosphoprotein (P) gene !1of rinderpest virus. !$#cross-references MUID:92410646; PMID:1529555 !$#accession B43387 !'##molecule_type mRNA !'##residues 1-177 ##label YAM !'##cross-references GB:S44819; NID:g255490; PIDN:AAB23269.1; !1PID:g255492 GENETICS !$#gene C CLASSIFICATION #superfamily measles virus nonstructural protein C KEYWORDS nonstructural protein SUMMARY #length 177 #molecular-weight 19926 #checksum 4600 SEQUENCE /// ENTRY MNNZCV #type complete TITLE nonstructural protein C - canine distemper virus ORGANISM #formal_name canine distemper virus DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 24-Sep-1999 ACCESSIONS A23778 REFERENCE A23778 !$#authors Barrett, T.; Shrimpton, S.B.; Russell, S.E.H. !$#journal Virus Res. (1985) 3:367-372 !$#title Nucleotide sequence of the entire protein coding region of !1canine distemper virus polymerase-associated (P) protein !1mRNA. !$#cross-references MUID:86072821; PMID:3000106 !$#accession A23778 !'##molecule_type mRNA !'##residues 1-174 ##label BAR !'##cross-references GB:M32418; NID:g323247; PIDN:AAA42881.1; !1PID:g323249 GENETICS !$#gene C CLASSIFICATION #superfamily measles virus nonstructural protein C KEYWORDS nonstructural protein SUMMARY #length 174 #molecular-weight 20264 #checksum 9469 SEQUENCE /// ENTRY JQ1564 #type complete TITLE nonstructural protein C - phocine distemper virus ORGANISM #formal_name phocine distemper virus DATE 31-Dec-1993 #sequence_revision 22-Oct-1999 #text_change 16-Jun-2000 ACCESSIONS JQ1611; JQ1564 REFERENCE JQ1608 !$#authors Blixenkrone-Moeller, M.; Sharma, B.; Varsanyi, T.M.; Hu, A.; !1Norrby, E.; Koevamees, J. !$#journal J. Gen. Virol. (1992) 73:885-893 !$#title Sequence analysis of the genes encoding the nucleocapsid !1protein and phosphoprotein (P) of phocid distemper virus, !1and editing of the P gene transcript. !$#cross-references MUID:92341068; PMID:1634877 !$#accession JQ1611 !'##molecule_type genomic RNA !'##residues 1-174 ##label BLI !'##cross-references GB:X75960; NID:g440570; PIDN:CAA53574.1; !1PID:g440572 !'##note the authors translated the codon GTA for residue 26 as Ala REFERENCE JQ1563 !$#authors Curran, M.D.; Rima, B.K. !$#journal J. Gen. Virol. (1992) 73:1587-1591 !$#title The genes encoding the phospho- and matrix proteins of !1phocine distemper virus. !$#cross-references MUID:92300361; PMID:1535099 !$#accession JQ1564 !'##molecule_type genomic RNA !'##residues 1-25,'A',27-174 ##label CUR !'##cross-references DDBJ:D10371; NID:g222246; PIDN:BAA01204.1; !1PID:g222249 !'##experimental_source strain Ulster/88 GENETICS !$#gene C CLASSIFICATION #superfamily measles virus nonstructural protein C KEYWORDS nonstructural protein SUMMARY #length 174 #molecular-weight 20349 #checksum 1123 SEQUENCE /// ENTRY QQBYTY #type complete TITLE TyA protein - yeast (Saccharomyces cerevisiae) retrotransposon Ty1-15 ORGANISM #formal_name Saccharomyces cerevisiae DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 16-Jul-1999 ACCESSIONS A21856 REFERENCE A21856 !$#authors Mellor, J.; Fulton, S.M.; Dobson, M.J.; Wilson, W.; !1Kingsman, S.M.; Kingsman, A.J. !$#journal Nature (1985) 313:243-246 !$#title A retrovirus-like strategy for expression of a fusion !1protein encoded by yeast transposon Ty1. !$#cross-references MUID:85111117; PMID:2982101 !$#accession A21856 !'##molecule_type DNA !'##residues 1-440 ##label MEL !'##cross-references GB:X01736; NID:g4708; PIDN:CAA25873.1; PID:g4709 GENETICS !$#mobile_element retrotransposon Ty1-15 CLASSIFICATION #superfamily TyA protein SUMMARY #length 440 #molecular-weight 49141 #checksum 4148 SEQUENCE /// ENTRY MNNZSV #type complete TITLE nonstructural protein - Sendai virus (strain Z) ORGANISM #formal_name Sendai virus DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 16-Jul-1999 ACCESSIONS A04041 REFERENCE A00726 !$#authors Shioda, T.; Hidaka, Y.; Kanda, T.; Shibuta, H.; Nomoto, A.; !1Iwasaki, K. !$#journal Nucleic Acids Res. (1983) 11:7317-7330 !$#title Sequence of 3,687 nucleotides from the 3' end of Sendai !1virus genome RNA and the predicted amino acid sequences of !1viral NP, P and C proteins. !$#cross-references MUID:84069769; PMID:6316257 !$#accession A04041 !'##molecule_type genomic RNA !'##residues 1-204 ##label SHI !'##cross-references GB:X00087; NID:g60928; PIDN:CAA24947.1; PID:g60931 GENETICS !$#gene C CLASSIFICATION #superfamily parainfluenza virus nonstructural protein KEYWORDS nonstructural protein SUMMARY #length 204 #molecular-weight 24015 #checksum 4299 SEQUENCE /// ENTRY MNNZHS #type complete TITLE nonstructural protein - Sendai virus (strain Harris) ORGANISM #formal_name Sendai virus DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 08-Apr-1994 ACCESSIONS B28985 REFERENCE A28985 !$#authors Giorgi, C.; Blumberg, B.M.; Kolakofsky, D. !$#journal Cell (1983) 35:829-836 !$#title Sendai virus contains overlapping genes expressed from a !1single mRNA. !$#cross-references MUID:84082108; PMID:6317203 !$#accession B28985 !'##molecule_type mRNA !'##residues 1-204 ##label GIO GENETICS !$#gene C CLASSIFICATION #superfamily parainfluenza virus nonstructural protein KEYWORDS nonstructural protein SUMMARY #length 204 #molecular-weight 24013 #checksum 4329 SEQUENCE /// ENTRY MNNZ39 #type complete TITLE nonstructural protein C - parainfluenza virus type 1 (strain C39) ORGANISM #formal_name parainfluenza virus type 1 DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS B39929 REFERENCE A39929 !$#authors Matsuoka, Y.; Curran, J.; Pelet, T.; Kolakofsky, D.; Ray, !1R.; Compans, R.W. !$#journal J. Virol. (1991) 65:3406-3410 !$#title The P gene of human parainfluenza virus type 1 encodes P and !1C proteins but not a cysteine-rich V protein. !$#cross-references MUID:91237868; PMID:1851888 !$#accession B39929 !'##molecule_type mRNA !'##residues 1-204 ##label MAT !'##cross-references GB:M37792; NID:g332741; PIDN:AAA46869.1; !1PID:g332743 CLASSIFICATION #superfamily parainfluenza virus nonstructural protein KEYWORDS nonstructural protein SUMMARY #length 204 #molecular-weight 24111 #checksum 8431 SEQUENCE /// ENTRY MNNZ35 #type complete TITLE nonstructural protein C - parainfluenza virus type 1 (strain C35) ORGANISM #formal_name parainfluenza virus type 1 DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 08-Apr-1994 ACCESSIONS B40234 REFERENCE A40234 !$#authors Power, U.F.; Ryan, K.W.; Portner, A. !$#journal Virology (1992) 189:340-343 !$#title The P genes of human parainfluenza virus type 1 clinical !1isolates are polycistronic and microheterogeneous. !$#cross-references MUID:92295573; PMID:1318610 !$#accession B40234 !'##molecule_type genomic RNA !'##residues 1-204 ##label POW !'##cross-references GB:M74080 CLASSIFICATION #superfamily parainfluenza virus nonstructural protein KEYWORDS nonstructural protein SUMMARY #length 204 #molecular-weight 24127 #checksum 8399 SEQUENCE /// ENTRY MNNZ73 #type complete TITLE nonstructural protein C - parainfluenza virus type 1 (strain CI-5/73) ORGANISM #formal_name parainfluenza virus type 1 DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 08-Apr-1994 ACCESSIONS D40234 REFERENCE A40234 !$#authors Power, U.F.; Ryan, K.W.; Portner, A. !$#journal Virology (1992) 189:340-343 !$#title The P genes of human parainfluenza virus type 1 clinical !1isolates are polycistronic and microheterogeneous. !$#cross-references MUID:92295573; PMID:1318610 !$#accession D40234 !'##molecule_type genomic RNA !'##residues 1-204 ##label POW !'##cross-references GB:M74082 CLASSIFICATION #superfamily parainfluenza virus nonstructural protein KEYWORDS nonstructural protein SUMMARY #length 204 #molecular-weight 24091 #checksum 8159 SEQUENCE /// ENTRY MNNZ83 #type complete TITLE nonstructural protein C - parainfluenza virus type 1 (strain CI-14/83) ORGANISM #formal_name parainfluenza virus type 1 DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS F40234 REFERENCE A40234 !$#authors Power, U.F.; Ryan, K.W.; Portner, A. !$#journal Virology (1992) 189:340-343 !$#title The P genes of human parainfluenza virus type 1 clinical !1isolates are polycistronic and microheterogeneous. !$#cross-references MUID:92295573; PMID:1318610 !$#accession F40234 !'##molecule_type genomic RNA !'##residues 1-204 ##label POW !'##cross-references GB:M74080; NID:g332679; PIDN:AAA46831.1; !1PID:g332682 CLASSIFICATION #superfamily parainfluenza virus nonstructural protein KEYWORDS nonstructural protein SUMMARY #length 204 #molecular-weight 24153 #checksum 7631 SEQUENCE /// ENTRY MNNZP3 #type complete TITLE nonstructural protein - parainfluenza virus type 3 (strain 47885) ORGANISM #formal_name parainfluenza virus type 3 #note host Homo sapiens (man) DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jul-1999 ACCESSIONS B27010 REFERENCE A92793 !$#authors Spriggs, M.K.; Collins, P.L. !$#journal J. Gen. Virol. (1986) 67:2705-2719 !$#title Sequence analysis of the P and C protein genes of human !1parainfluenza virus type 3: patterns of amino acid sequence !1homology among paramyxovirus proteins. !$#cross-references MUID:87085488; PMID:3025346 !$#accession B27010 !'##molecule_type mRNA !'##residues 1-199 ##label SPR !'##cross-references GB:X04721; NID:g60972; PIDN:CAA28430.1; PID:g60974 GENETICS !$#gene C CLASSIFICATION #superfamily parainfluenza virus nonstructural protein KEYWORDS nonstructural protein SUMMARY #length 199 #molecular-weight 23295 #checksum 5254 SEQUENCE /// ENTRY MNNZP4 #type complete TITLE nonstructural protein - parainfluenza virus type 3 ORGANISM #formal_name parainfluenza virus type 3 #note host Homo sapiens (man) DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jun-2000 ACCESSIONS B24189; B26896 REFERENCE A94343 !$#authors Luk, D.; Sanchez, A.; Banerjee, A.K. !$#journal Virology (1986) 153:318-325 !$#title Messenger RNA encoding the phosphoprotein (P) gene of human !1parainfluenza virus 3 is bicistronic. !$#cross-references MUID:86291173; PMID:3016995 !$#accession B24189 !'##molecule_type mRNA !'##residues 1-199 ##label LUK !'##cross-references GB:M14890; NID:g332738; PIDN:AAA46867.1; !1PID:g332740 REFERENCE A94348 !$#authors Galinski, M.S.; Mink, M.A.; Lambert, D.M.; Wechsler, S.L.; !1Pons, M.W. !$#journal Virology (1986) 155:46-60 !$#title Molecular cloning and sequence analysis of the human !1parainfluenza 3 virus mRNA encoding the P and C proteins. !$#cross-references MUID:87044104; PMID:3022477 !$#accession B26896 !'##molecule_type mRNA !'##residues 1-199 ##label GAL !'##cross-references GB:D00047; GB:N00047; NID:g222280; PIDN:BAA00032.1; !1PID:g222282 GENETICS !$#gene C CLASSIFICATION #superfamily parainfluenza virus nonstructural protein KEYWORDS nonstructural protein SUMMARY #length 199 #molecular-weight 23286 #checksum 5023 SEQUENCE /// ENTRY MNNZB3 #type complete TITLE nonstructural protein - parainfluenza virus type 3 ORGANISM #formal_name parainfluenza virus type 3 DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 16-Jul-1999 ACCESSIONS C27502 REFERENCE A93658 !$#authors Sakai, Y.; Suzu, S.; Shioda, T.; Shibuta, H. !$#journal Nucleic Acids Res. (1987) 15:2927-2944 !$#title Nucleotide sequence of the bovine parainfluenza 3 virus !1genome: its 3' end and the genes of NP, P, C and M proteins. !$#cross-references MUID:87174818; PMID:3031614 !$#accession C27502 !'##molecule_type genomic RNA !'##residues 1-201 ##label SAK !'##cross-references EMBL:Y00114; NID:g60891; PIDN:CAA68295.1; !1PID:g60894 GENETICS !$#gene C CLASSIFICATION #superfamily parainfluenza virus nonstructural protein KEYWORDS nonstructural protein SUMMARY #length 201 #molecular-weight 23509 #checksum 9027 SEQUENCE /// ENTRY MFNZS #type complete TITLE matrix protein - Sendai virus (strain Harris) ORGANISM #formal_name Sendai virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS A04042 REFERENCE A04042 !$#authors Blumberg, B.M.; Rose, K.; Simona, M.G.; Roux, L.; Giorgi, !1C.; Kolakofsky, D. !$#journal J. Virol. (1984) 52:656-663 !$#title Analysis of the Sendai virus M gene and protein. !$#cross-references MUID:85033911; PMID:6092688 !$#accession A04042 !'##molecule_type genomic RNA !'##residues 1-348 ##label BLU !'##cross-references GB:K02742; NID:g334935; PIDN:AAA47811.1; !1PID:g334936 CLASSIFICATION #superfamily parainfluenza virus matrix protein SUMMARY #length 348 #molecular-weight 38590 #checksum 3227 SEQUENCE /// ENTRY MFNZSV #type complete TITLE matrix protein - Sendai virus (strain Z) ORGANISM #formal_name Sendai virus DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 08-Apr-1994 ACCESSIONS A04043 REFERENCE A04043 !$#authors Hidaka, Y.; Kanda, T.; Iwasaki, K.; Nomoto, A.; Shioda, T.; !1Shibuta, H. !$#journal Nucleic Acids Res. (1984) 12:7965-7973 !$#title Nucleotide sequence of a Sendai virus genome region covering !1the entire M gene and the 3' proximal 1013 nucleotides of !1the F gene. !$#cross-references MUID:85062791; PMID:6095182 !$#accession A04043 !'##molecule_type genomic RNA !'##residues 1-348 ##label HID GENETICS !$#gene M CLASSIFICATION #superfamily parainfluenza virus matrix protein KEYWORDS matrix protein SUMMARY #length 348 #molecular-weight 38557 #checksum 3108 SEQUENCE /// ENTRY MFNZFU #type complete TITLE matrix protein - Sendai virus (strain Fushimi) ORGANISM #formal_name Sendai virus DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS S10330 REFERENCE S10330 !$#authors Willenbrink, W.; Neubert, W.J. !$#journal Nucleic Acids Res. (1990) 18:3993 !$#title Cloning and sequencing of the matrix protein gene (M) of !1Sendai virus (strain Fushimi). !$#cross-references MUID:90326529; PMID:2165255 !$#accession S10330 !'##molecule_type genomic RNA !'##residues 1-348 ##label WIL !'##cross-references GB:X53056; NID:g62017; PIDN:CAA37223.1; PID:g62018 !'##experimental_source ATCC VR-105 GENETICS !$#gene M CLASSIFICATION #superfamily parainfluenza virus matrix protein KEYWORDS matrix protein SUMMARY #length 348 #molecular-weight 38600 #checksum 3146 SEQUENCE /// ENTRY MFNZC3 #type complete TITLE matrix protein - parainfluenza virus type 1 (strain C35) ORGANISM #formal_name parainfluenza virus type 1 DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS A44218 REFERENCE A44218 !$#authors Power, U.F.; Ryan, K.W.; Portner, A. !$#journal Virology (1992) 191:947-952 !$#title Sequence characterization and expression of the matrix !1protein gene of human parainfluenza virus type 1. !$#cross-references MUID:93079897; PMID:1333129 !$#accession A44218 !'##molecule_type genomic RNA !'##residues 1-348 ##label POW !'##cross-references GB:M80818; NID:g332728; PIDN:AAA46861.1; !1PID:g332729 GENETICS !$#gene M CLASSIFICATION #superfamily parainfluenza virus matrix protein KEYWORDS matrix protein SUMMARY #length 348 #molecular-weight 38401 #checksum 729 SEQUENCE /// ENTRY B48341 #type complete TITLE matrix protein - parainfluenza virus type 1 (strains A1426, 86-315, 62M-753) ORGANISM #formal_name parainfluenza virus type 1 DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS B48341 REFERENCE A48341 !$#authors Miyahara, K.; Kitada, S.; Yoshimoto, M.; Matsumura, H.; !1Kawano, M.; Komada, H.; Tsurudome, M.; Kusagawa, S.; Nishio, !1M.; Ito, Y. !$#journal Arch. Virol. (1992) 124:255-268 !$#title Molecular evolution of human paramyxoviruses. Nucleotide !1sequence analyses of the human parainfluenza type 1 virus NP !1and M protein genes and construction of phylogenetic trees !1for all the human paramyxoviruses. !$#cross-references MUID:92296894; PMID:1605738 !$#accession B48341 !'##molecule_type genomic RNA !'##residues 1-348 ##label MIY !'##cross-references GB:S38067; NID:g250342; PIDN:AAB22344.1; !1PID:g250343 !'##note sequence extracted from NCBI backbone (NCBIN:106080, !1NCBIP:106081) GENETICS !$#gene M CLASSIFICATION #superfamily parainfluenza virus matrix protein KEYWORDS matrix protein SUMMARY #length 348 #molecular-weight 38445 #checksum 869 SEQUENCE /// ENTRY MFNZP3 #type complete TITLE matrix protein (version 1) - parainfluenza virus type 3 ORGANISM #formal_name parainfluenza virus type 3 #note host Homo sapiens (man) DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jul-1999 ACCESSIONS A27511; A26350 REFERENCE A94354 !$#authors Luk, D.; Masters, P.S.; Sanchez, A.; Banerjee, A.K. !$#journal Virology (1987) 156:189-192 !$#title Complete nucleotide sequence of the matrix protein mRNA and !1three intergenic junctions of human parainfluenza virus type !13. !$#cross-references MUID:87122153; PMID:3027966 !$#accession A27511 !'##molecule_type mRNA !'##residues 1-353 ##label LUK !'##cross-references GB:M16569; NID:g332726; PIDN:AAA46860.1; !1PID:g332727 REFERENCE A93662 !$#authors Prinoski, K.; Cote, M.J.; Kang, C.Y.; Dimock, K. !$#journal Nucleic Acids Res. (1987) 15:3182 !$#title Nucleotide sequence of the human parainfluenza virus 3 !1matrix protein gene. !$#cross-references MUID:87174839; PMID:3031622 !$#accession A26350 !'##molecule_type mRNA !'##residues 1-353 ##label PRI !'##cross-references GB:Y00119; NID:g60874; PIDN:CAA68302.1; PID:g60875 !'##experimental_source strain 47885 GENETICS !$#gene M CLASSIFICATION #superfamily parainfluenza virus matrix protein KEYWORDS matrix protein SUMMARY #length 353 #molecular-weight 39501 #checksum 4601 SEQUENCE /// ENTRY MFNZPT #type complete TITLE matrix protein (version 2) - parainfluenza virus type 3 ORGANISM #formal_name parainfluenza virus type 3 #note host Homo sapiens (man) DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 30-Jun-1993 ACCESSIONS A26349 REFERENCE A26349 !$#authors Galinski, M.S.; Mink, M.A.; Lambert, D.M.; Wechsler, S.L.; !1Pons, M.W. !$#journal Virology (1987) 157:24-30 !$#title Molecular cloning and sequence analysis of the human !1parainfluenza 3 virus gene encoding the matrix protein. !$#cross-references MUID:87151113; PMID:3029963 !$#accession A26349 !'##molecule_type DNA !'##residues 1-353 ##label GAL GENETICS !$#gene M CLASSIFICATION #superfamily parainfluenza virus matrix protein KEYWORDS matrix protein SUMMARY #length 353 #molecular-weight 39501 #checksum 5026 SEQUENCE /// ENTRY MFNZH3 #type complete TITLE matrix protein (version 3) - parainfluenza virus type 3 ORGANISM #formal_name parainfluenza virus type 3 #note host Homo sapiens (man) DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 16-Jun-2000 ACCESSIONS A29531 REFERENCE A29531 !$#authors Spriggs, M.K.; Johnson, P.R.; Collins, P.L. !$#journal J. Gen. Virol. (1987) 68:1491-1497 !$#title Sequence analysis of the matrix protein gene of human !1parainfluenza virus type 3: extensive sequence homology !1among paramyxoviruses. !$#cross-references MUID:87197247; PMID:2883252 !$#accession A29531 !'##molecule_type mRNA !'##residues 1-353 ##label SPR !'##cross-references GB:D00130; NID:g222273; PIDN:BAA00078.1; !1PID:g222274 GENETICS !$#gene M CLASSIFICATION #superfamily parainfluenza virus matrix protein KEYWORDS matrix protein SUMMARY #length 353 #molecular-weight 39528 #checksum 5850 SEQUENCE /// ENTRY MFNZB3 #type complete TITLE matrix protein - parainfluenza virus type 3 ORGANISM #formal_name parainfluenza virus type 3 DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 16-Jul-1999 ACCESSIONS D27502 REFERENCE A93658 !$#authors Sakai, Y.; Suzu, S.; Shioda, T.; Shibuta, H. !$#journal Nucleic Acids Res. (1987) 15:2927-2944 !$#title Nucleotide sequence of the bovine parainfluenza 3 virus !1genome: its 3' end and the genes of NP, P, C and M proteins. !$#cross-references MUID:87174818; PMID:3031614 !$#accession D27502 !'##molecule_type genomic RNA !'##residues 1-351 ##label SAK !'##cross-references EMBL:Y00114; NID:g60891; PIDN:CAA68296.1; !1PID:g60895 GENETICS !$#gene M CLASSIFICATION #superfamily parainfluenza virus matrix protein KEYWORDS matrix protein SUMMARY #length 351 #molecular-weight 39310 #checksum 3429 SEQUENCE /// ENTRY MFNZNC #type complete TITLE matrix protein - Newcastle disease virus (strain Beaudette C) ORGANISM #formal_name Newcastle disease virus DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 16-Jul-1999 ACCESSIONS A26111 REFERENCE A26111 !$#authors Chambers, P.; Millar, N.S.; Platt, S.G.; Emmerson, P.T. !$#journal Nucleic Acids Res. (1986) 14:9051-9061 !$#title Nucleotide sequence of the gene encoding the matrix protein !1of Newcastle disease virus. !$#cross-references MUID:87066775; PMID:3786143 !$#accession A26111 !'##molecule_type genomic RNA !'##residues 1-364 ##label CHA !'##cross-references GB:X04687; NID:g60940; PIDN:CAA28389.1; PID:g60941 GENETICS !$#gene M CLASSIFICATION #superfamily parainfluenza virus matrix protein KEYWORDS matrix protein SUMMARY #length 364 #molecular-weight 39604 #checksum 4208 SEQUENCE /// ENTRY MFNZNV #type complete TITLE matrix protein - Newcastle disease virus (strain Australia-Victoria) ALTERNATE_NAMES membrane protein ORGANISM #formal_name Newcastle disease virus DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 16-Jul-1999 ACCESSIONS A27530 REFERENCE A27530 !$#authors McGinnes, L.W.; Morrison, T.G. !$#journal Virology (1987) 156:221-228 !$#title The nucleotide sequence of the gene encoding the Newcastle !1disease virus membrane protein and comparisons of membrane !1protein sequences. !$#cross-references MUID:87122164; PMID:3027973 !$#accession A27530 !'##molecule_type genomic RNA !'##residues 1-364 ##label MCG !'##cross-references GB:M16622; NID:g332365; PIDN:AAA46673.1; !1PID:g332366 GENETICS !$#gene M CLASSIFICATION #superfamily parainfluenza virus matrix protein KEYWORDS matrix protein SUMMARY #length 364 #molecular-weight 39746 #checksum 3274 SEQUENCE /// ENTRY MFNZMS #type complete TITLE matrix protein - mumps virus ORGANISM #formal_name mumps virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 08-Apr-1994 ACCESSIONS A31295 REFERENCE A31295 !$#authors Elango, N. !$#journal Virology (1989) 168:426-428 !$#title Complete nucleotide sequence of the matrix protein mRNA of !1mumps virus. !$#cross-references MUID:89130960; PMID:2789521 !$#accession A31295 !'##molecule_type mRNA !'##residues 1-375 ##label ELA GENETICS !$#gene M CLASSIFICATION #superfamily parainfluenza virus matrix protein KEYWORDS matrix protein SUMMARY #length 375 #molecular-weight 41554 #checksum 7808 SEQUENCE /// ENTRY A60004 #type complete TITLE matrix protein - mumps virus (strain SBL) ORGANISM #formal_name mumps virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jun-2000 ACCESSIONS A60004 REFERENCE A60004 !$#authors Elliott, G.D.; Afzal, M.A.; Martin, S.J.; Rima, B.K. !$#journal Virus Res. (1989) 12:61-75 !$#title Nucleotide sequence of the matrix, fusion and putative SH !1protein genes of mumps virus and their deduced amino acid !1sequences. !$#cross-references MUID:89243815; PMID:2718625 !$#accession A60004 !'##molecule_type mRNA !'##residues 1-375 ##label ELL !'##cross-references GB:D00663; NID:g222149; PIDN:BAA00560.1; !1PID:g222152 GENETICS !$#gene M CLASSIFICATION #superfamily parainfluenza virus matrix protein KEYWORDS matrix protein SUMMARY #length 375 #molecular-weight 41584 #checksum 8496 SEQUENCE /// ENTRY JQ1290 #type complete TITLE matrix protein - parainfluenza virus type 4A (strain Toshiba) ORGANISM #formal_name parainfluenza virus type 4A DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jun-2000 ACCESSIONS JQ1290; JQ0933 REFERENCE JQ1290 !$#authors Kondo, K.; Fujii, M.; Nakamura, T.; Bando, H.; Kawano, M.; !1Tsurudome, M.; Komada, H.; Kusakawa, S.; Nishio, M.; Ito, Y. !$#journal J. Gen. Virol. (1991) 72:2283-2287 !$#title Sequence characterization of the matrix protein genes of !1parainfluenza virus types 4A and 4B. !$#cross-references MUID:91374032; PMID:1654379 !$#accession JQ1290 !'##molecule_type mRNA !'##residues 1-382 ##label KON !'##cross-references GB:D10241; NID:g222283; PIDN:BAA01086.1; !1PID:g222284 GENETICS !$#gene M CLASSIFICATION #superfamily parainfluenza virus matrix protein KEYWORDS matrix protein SUMMARY #length 382 #molecular-weight 43120 #checksum 6222 SEQUENCE /// ENTRY JQ1291 #type complete TITLE matrix protein - parainfluenza virus type 4B (strain 68-333) ORGANISM #formal_name parainfluenza virus type 4B DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jun-2000 ACCESSIONS JQ1291; JQ0934 REFERENCE JQ1290 !$#authors Kondo, K.; Fujii, M.; Nakamura, T.; Bando, H.; Kawano, M.; !1Tsurudome, M.; Komada, H.; Kusakawa, S.; Nishio, M.; Ito, Y. !$#journal J. Gen. Virol. (1991) 72:2283-2287 !$#title Sequence characterization of the matrix protein genes of !1parainfluenza virus types 4A and 4B. !$#cross-references MUID:91374032; PMID:1654379 !$#accession JQ1291 !'##molecule_type mRNA !'##residues 1-382 ##label KON !'##cross-references GB:D10242; NID:g222285; PIDN:BAA01087.1; !1PID:g222286 GENETICS !$#gene M CLASSIFICATION #superfamily parainfluenza virus matrix protein KEYWORDS matrix protein SUMMARY #length 382 #molecular-weight 43027 #checksum 7115 SEQUENCE /// ENTRY MFNZLA #type complete TITLE matrix protein - La Piedad-Michoacan-Mexico virus ORGANISM #formal_name La Piedad-Michoacan-Mexico virus, LPMV #note host Sus scrofa domestica (domestic pig) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 08-Apr-1994 ACCESSIONS A38707 REFERENCE A38707 !$#authors Berg, M.; Sundqvist, A.; Moreno-Lopez, J.; Linne, T. !$#journal J. Gen. Virol. (1991) 72:1045-1050 !$#title Identification of the porcine paramyxovirus LPMV matrix !1protein gene: comparative sequence analysis with other !1paramyxoviruses. !$#cross-references MUID:91237338; PMID:2033388 !$#accession A38707 !'##molecule_type genomic RNA !'##residues 1-369 ##label BER GENETICS !$#gene M CLASSIFICATION #superfamily parainfluenza virus matrix protein KEYWORDS matrix protein SUMMARY #length 369 #molecular-weight 41657 #checksum 2223 SEQUENCE /// ENTRY MFNZS5 #type complete TITLE matrix protein - simian paramyxovirus SV5 (strain W3) ORGANISM #formal_name simian paramyxovirus SV5 DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 08-Apr-1994 ACCESSIONS A34604 REFERENCE A34604 !$#authors Sheshberadaran, H.; Lamb, R.A. !$#journal Virology (1990) 176:234-243 !$#title Sequence characterization of the membrane protein gene of !1paramyxovirus simian virus 5. !$#cross-references MUID:90232733; PMID:2330672 !$#accession A34604 !'##molecule_type mRNA !'##residues 1-377 ##label SHE GENETICS !$#gene M CLASSIFICATION #superfamily parainfluenza virus matrix protein KEYWORDS matrix protein SUMMARY #length 377 #molecular-weight 42250 #checksum 8925 SEQUENCE /// ENTRY MFNZP2 #type complete TITLE matrix protein - parainfluenza virus type 2 ORGANISM #formal_name parainfluenza virus type 2 DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jul-1999 ACCESSIONS A36421; S16661 REFERENCE A36421 !$#authors Kawano, M.; Bando, H.; Ohgimoto, S.; Okamoto, K.; Kondo, K.; !1Tsurudome, M.; Nishio, M.; Ito, Y. !$#journal Virology (1990) 179:857-861 !$#title Complete nucleotide sequence of the matrix gene of human !1parainfluenza type 2 virus and expression of the M protein !1in bacteria. !$#cross-references MUID:91049454; PMID:2173264 !$#accession A36421 !'##molecule_type genomic RNA !'##residues 1-377 ##label KAW1 !'##cross-references GB:M62734; NID:g332730; PIDN:AAA46862.1; !1PID:g332731 REFERENCE S16659 !$#authors Kawano, M.; Okamoto, K.; Bando, H.; Kondo, K.; Tsurudome, !1M.; Komada, H.; Nishio, M.; Ito, Y. !$#journal Nucleic Acids Res. (1991) 19:2739-2746 !$#title Characterizations of the human parainfluenza type 2 virus !1gene encoding the L protein and the intergenic sequences. !$#cross-references MUID:91252221; PMID:1645865 !$#accession S16661 !'##molecule_type genomic RNA !'##residues 1-377 ##label KAW2 !'##cross-references EMBL:X57559; NID:g61985; PIDN:CAA40785.1; !1PID:g61988 !'##experimental_source strain Toshiba GENETICS !$#gene M CLASSIFICATION #superfamily parainfluenza virus matrix protein KEYWORDS matrix protein SUMMARY #length 377 #molecular-weight 42312 #checksum 5856 SEQUENCE /// ENTRY MFNZ41 #type complete TITLE matrix protein - simian paramyxovirus SV41 ORGANISM #formal_name simian paramyxovirus SV41 DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS A40563 REFERENCE A40563 !$#authors Tsurudome, M.; Bando, H.; Kawano, M.; Matsumura, H.; Komada, !1H.; Nishio, M.; Ito, Y. !$#journal Virology (1991) 184:93-100 !$#title Transcripts of simian virus 41 (SV41) matrix gene are !1exclusively dicistronic with the fusion gene which is also !1transcribed as a monocistron. !$#cross-references MUID:91335794; PMID:1651608 !$#accession A40563 !'##molecule_type genomic RNA !'##residues 1-382 ##label TSU !'##cross-references GB:S48627; NID:g233737; PIDN:AAB19493.1; !1PID:g233738 GENETICS !$#gene M CLASSIFICATION #superfamily parainfluenza virus matrix protein KEYWORDS matrix protein SUMMARY #length 382 #molecular-weight 42155 #checksum 1476 SEQUENCE /// ENTRY MFNZMV #type complete TITLE matrix protein - measles virus ORGANISM #formal_name measles virus DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Jul-1999 ACCESSIONS A93018; A25360 REFERENCE A93018 !$#authors Bellini, W.J.; Englund, G.; Richardson, C.D.; Rozenblatt, !1S.; Lazzarini, R.A. !$#journal J. Virol. (1986) 58:408-416 !$#title Matrix genes of measles virus andd canine distemper virus: !1cloning, nucleotide sequences, and deduced amino acid !1sequences. !$#cross-references MUID:86200383; PMID:3754588 !$#accession A93018 !'##molecule_type genomic RNA !'##residues 1-335 ##label BEL !'##cross-references GB:M12668; NID:g331778; PIDN:AAA66616.1; !1PID:g331779 GENETICS !$#gene M CLASSIFICATION #superfamily parainfluenza virus matrix protein KEYWORDS matrix protein SUMMARY #length 335 #molecular-weight 37714 #checksum 985 SEQUENCE /// ENTRY MFNZMH #type complete TITLE matrix protein - measles virus (strain Hu2) ORGANISM #formal_name measles virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jun-2000 ACCESSIONS A31039 REFERENCE A31039 !$#authors Curran, M.D.; Rima, B.K. !$#journal J. Gen. Virol. (1988) 69:2407-2411 !$#title Nucleotide sequence of the gene encoding the matrix protein !1of a recent measles virus isolate. !$#cross-references MUID:88316218; PMID:3411300 !$#accession A31039 !'##molecule_type genomic RNA !'##residues 1-335 ##label CUR !'##cross-references GB:D00338; NID:g222063; PIDN:BAA00242.1; !1PID:g222064 GENETICS !$#gene M CLASSIFICATION #superfamily parainfluenza virus matrix protein KEYWORDS matrix protein SUMMARY #length 335 #molecular-weight 37674 #checksum 677 SEQUENCE /// ENTRY D48556 #type complete TITLE matrix protein - measles virus (strain AIK-C) ORGANISM #formal_name measles virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS D48556 REFERENCE A48556 !$#authors Mori, T.; Sasaki, K.; Hashimoto, H.; Makino, S. !$#journal Virus Genes (1993) 7:67-81 !$#title Molecular cloning and complete nucleotide sequence of !1genomic RNA of the AIK-C strain of attenuated measles virus. !$#cross-references MUID:93227570; PMID:8470368 !$#accession D48556 !'##molecule_type genomic RNA !'##residues 1-335 ##label MOR !'##cross-references GB:S58435; NID:g299460; PIDN:AAB26144.1; !1PID:g299464 !'##note sequence extracted from NCBI backbone (NCBIN:129264, !1NCBIP:129271) GENETICS !$#gene M CLASSIFICATION #superfamily parainfluenza virus matrix protein KEYWORDS matrix protein SUMMARY #length 335 #molecular-weight 37681 #checksum 1547 SEQUENCE /// ENTRY MFNZBK #type complete TITLE matrix protein - measles virus (strain Biken) ORGANISM #formal_name measles virus DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Jun-2000 ACCESSIONS A33124 REFERENCE A33124 !$#authors Enami, M.; Sato, T.A.; Sugiura, A. !$#journal J. Gen. Virol. (1989) 70:2191-2196 !$#title Matrix protein of cell-associated subacute sclerosing !1panencephalitis viruses. !$#cross-references MUID:89361379; PMID:2769235 !$#accession A33124 !'##molecule_type genomic RNA !'##residues 1-343 ##label ENA !'##cross-references GB:D00495; NID:g222254; PIDN:BAA00381.1; !1PID:g222255 CLASSIFICATION #superfamily parainfluenza virus matrix protein KEYWORDS matrix protein SUMMARY #length 343 #molecular-weight 38173 #checksum 9895 SEQUENCE /// ENTRY B60285 #type complete TITLE matrix protein - subacute sclerosing panencephalitis virus (strain Yamagata-1) ORGANISM #formal_name subacute sclerosing panencephalitis virus, SSPEV DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 07-May-1999 ACCESSIONS B60285 REFERENCE A60285 !$#authors Yoshikawa, Y.; Tsuruoka, H.; Matsumoto, M.; Haga, T.; !1Shioda, T.; Shibuta, H.; Sato, T.A.; Yamanouchi, K. !$#journal Virus Genes (1990) 4:151-161 !$#title Molecular analysis of structural protein genes of the !1Yamagata-1 strain of defective subacute sclerosing !1panencephalitis virus. II. Nucleotide sequence of a cDNA !1corresponding to the P plus M dicistronic mRNA. !$#cross-references MUID:90385700; PMID:1698326 !$#accession B60285 !'##molecule_type mRNA !'##residues 1-300 ##label YOS GENETICS !$#gene M CLASSIFICATION #superfamily parainfluenza virus matrix protein KEYWORDS matrix protein SUMMARY #length 300 #molecular-weight 33126 #checksum 9746 SEQUENCE /// ENTRY MFNZCV #type complete TITLE matrix protein - canine distemper virus ORGANISM #formal_name canine distemper virus DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Jul-1999 ACCESSIONS B93018; A25360 REFERENCE A93018 !$#authors Bellini, W.J.; Englund, G.; Richardson, C.D.; Rozenblatt, !1S.; Lazzarini, R.A. !$#journal J. Virol. (1986) 58:408-416 !$#title Matrix genes of measles virus andd canine distemper virus: !1cloning, nucleotide sequences, and deduced amino acid !1sequences. !$#cross-references MUID:86200383; PMID:3754588 !$#accession B93018 !'##molecule_type genomic RNA !'##residues 1-335 ##label BEL !'##cross-references GB:M12669; NID:g323243; PIDN:AAA87372.1; !1PID:g323244 GENETICS !$#gene M CLASSIFICATION #superfamily parainfluenza virus matrix protein KEYWORDS matrix protein SUMMARY #length 335 #molecular-weight 37774 #checksum 9866 SEQUENCE /// ENTRY JQ1566 #type complete TITLE matrix protein - phocine distemper virus (strain Ulster/88) ALTERNATE_NAMES M protein ORGANISM #formal_name phocine distemper virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jun-2000 ACCESSIONS JQ1566; A45572 REFERENCE JQ1563 !$#authors Curran, M.D.; Rima, B.K. !$#journal J. Gen. Virol. (1992) 73:1587-1591 !$#title The genes encoding the phospho- and matrix proteins of !1phocine distemper virus. !$#cross-references MUID:92300361; PMID:1535099 !$#accession JQ1566 !'##molecule_type genomic RNA !'##residues 1-335 ##label CUR !'##cross-references DDBJ:D10371; NID:g222246; PIDN:BAA01205.1; !1PID:g222250 REFERENCE A45572 !$#authors Sharma, B.; Norrby, E.; Blixenkrone-Moller, M.; Kovamees, J. !$#journal Virus Res. (1992) 23:13-25 !$#title The nucleotide and deduced amino acid sequence of the M gene !1of phocid distemper virus (PDV). The most conserved protein !1of morbilliviruses shows a uniquely close relationship !1between PDV and canine distemper virus. !$#cross-references MUID:92295708; PMID:1604930 !$#accession A45572 !'##molecule_type DNA !'##residues 1-83,'T',85-177,'V',179-309,'H',311-330,'P',332,'Q',334-335 !1##label SHA !'##cross-references GB:S38237; NID:g250163; PIDN:AAB22302.1; !1PID:g250164 !'##note sequence extracted from NCBI backbone (NCBIN:106200, !1NCBIP:106202) GENETICS !$#gene M CLASSIFICATION #superfamily parainfluenza virus matrix protein KEYWORDS matrix protein SUMMARY #length 335 #molecular-weight 37867 #checksum 8470 SEQUENCE /// ENTRY MFNZRP #type complete TITLE matrix protein - rinderpest virus (strain Kabete-O) ORGANISM #formal_name rinderpest virus DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS A34684 REFERENCE A34684 !$#authors Limo, M.; Yilma, T. !$#journal Virology (1990) 175:323-327 !$#title Molecular cloning of the rinderpest virus matrix gene: !1comparative sequence analysis with other paramyxoviruses. !$#cross-references MUID:90177233; PMID:2309449 !$#accession A34684 !'##molecule_type mRNA !'##residues 1-335 ##label LIM !'##cross-references GB:M34018; NID:g333896; PIDN:AAA47398.1; !1PID:g333897 GENETICS !$#gene M CLASSIFICATION #superfamily parainfluenza virus matrix protein KEYWORDS matrix protein SUMMARY #length 335 #molecular-weight 38285 #checksum 1148 SEQUENCE /// ENTRY MFNZ #type complete TITLE matrix protein - human respiratory syncytial virus ORGANISM #formal_name human respiratory syncytial virus DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 16-Jul-1999 ACCESSIONS A04030 REFERENCE A04030 !$#authors Satake, M.; Venkatesan, S. !$#journal J. Virol. (1984) 50:92-99 !$#title Nucleotide sequence of the gene encoding respiratory !1syncytial virus matrix protein. !$#cross-references MUID:84138836; PMID:6699948 !$#accession A04030 !'##molecule_type genomic RNA !'##residues 1-256 ##label SAT !'##cross-references GB:M11486; GB:K01459; GB:K02719; GB:K03348; !1GB:K03349; GB:M11217; GB:M11244; GB:M11487; GB:M11505; !1GB:M11514; GB:M11631; GB:M12966; GB:X00001; GB:X02221; !1NID:g333925; PIDN:AAB59854.1; PID:g333930 CLASSIFICATION #superfamily respiratory syncytial virus matrix protein SUMMARY #length 256 #molecular-weight 28714 #checksum 7774 SEQUENCE /// ENTRY MFNZBR #type complete TITLE matrix protein - bovine respiratory syncytial virus (strain A51908) ORGANISM #formal_name bovine respiratory syncytial virus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jun-2000 ACCESSIONS JQ1178; JQ0952 REFERENCE JQ1178 !$#authors Samal, S.K.; Zamora, M. !$#journal J. Gen. Virol. (1991) 72:1715-1720 !$#title Nucleotide sequence analysis of a matrix and small !1hydrophobic protein dicistronic mRNA of bovine respiratory !1syncytial virus demonstrates extensive sequence divergence !1of the small hydrophobic protein from that of human !1respiratory syncytial virus. !$#cross-references MUID:91311427; PMID:1856698 !$#accession JQ1178 !'##molecule_type mRNA !'##residues 1-256 ##label SAM !'##cross-references GB:D01012; NID:g221063; PIDN:BAA00812.1; !1PID:g221064 !'##note the authors translated the codon GAG for residue 24 and GAA for !1residue 51 as Asp GENETICS !$#gene M CLASSIFICATION #superfamily respiratory syncytial virus matrix protein KEYWORDS matrix protein SUMMARY #length 256 #molecular-weight 28713 #checksum 5474 SEQUENCE /// ENTRY MFNZT3 #type complete TITLE matrix protein - turkey rhinotracheitis virus (strain 3BV) ORGANISM #formal_name turkey rhinotracheitis virus DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS A40817 REFERENCE A40817 !$#authors Yu, Q.; Davis, P.J.; Li, J.; Cavanagh, D. !$#journal Virology (1992) 186:426-434 !$#title Cloning and sequencing of the matrix protein (M) gene of !1turkey rhinotracheitis virus reveal a gene order different !1from that of respiratory syncytial virus. !$#cross-references MUID:92124715; PMID:1733097 !$#accession A40817 !'##molecule_type genomic RNA !'##residues 1-254 ##label YUQ !'##cross-references GB:X58639; NID:g62149; PIDN:CAA41496.1; PID:g62150 GENETICS !$#gene M CLASSIFICATION #superfamily respiratory syncytial virus matrix protein KEYWORDS matrix protein SUMMARY #length 254 #molecular-weight 27595 #checksum 1259 SEQUENCE /// ENTRY SHNZS5 #type complete TITLE small hydrophobic protein - simian paramyxovirus SV5 ORGANISM #formal_name simian paramyxovirus SV5 DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 16-Jul-1999 ACCESSIONS A25482 REFERENCE A25482 !$#authors Hiebert, S.W.; Paterson, R.G.; Lamb, R.A. !$#journal J. Virol. (1985) 55:744-751 !$#title Identification and predicted sequence of a previously !1unrecognized small hydrophobic protein, SH, of the !1paramyxovirus simian virus 5. !$#cross-references MUID:85265038; PMID:4020965 !$#accession A25482 !'##molecule_type mRNA !'##residues 1-44 ##label HIE !'##cross-references GB:M11785; NID:g335120; PIDN:AAA47883.1; !1PID:g335121 GENETICS !$#gene SH CLASSIFICATION #superfamily simian paramyxovirus small hydrophobic protein SUMMARY #length 44 #molecular-weight 5108 #checksum 5301 SEQUENCE /// ENTRY SHNZMV #type complete TITLE small hydrophobic protein - mumps virus (strains SBL-1 and SBL) ORGANISM #formal_name mumps virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jun-2000 ACCESSIONS A31884; S24823; C60004 REFERENCE A31884 !$#authors Elango, N.; Koevamees, J.; Varsanyi, T.M.; Norrby, E. !$#journal J. Virol. (1989) 63:1413-1415 !$#title mRNA sequence and deduced amino acid sequence of the mumps !1virus small hydrophobic protein gene. !$#cross-references MUID:89125739; PMID:2915385 !$#accession A31884 !'##molecule_type mRNA !'##residues 1-57 ##label ELA !'##cross-references GB:M25421; NID:g556278; PIDN:AAA50290.1; !1PID:g556279 !'##experimental_source strain SBL-1 REFERENCE S19866 !$#authors Yeo, R.P.; Afzal, M.A.; Forsey, T.; Rima, B.K. !$#submission submitted to the EMBL Data Library, January 1992 !$#description Nucleotide sequence analysis of the SH gene of mumps virus !1reveals several lineages of the virus. !$#accession S24823 !'##molecule_type DNA !'##residues 1-57 ##label YEO !'##cross-references EMBL:X63704; NID:g60586; PIDN:CAA45233.1; !1PID:g60587 !'##experimental_source strain SBL REFERENCE A60004 !$#authors Elliott, G.D.; Afzal, M.A.; Martin, S.J.; Rima, B.K. !$#journal Virus Res. (1989) 12:61-75 !$#title Nucleotide sequence of the matrix, fusion and putative SH !1protein genes of mumps virus and their deduced amino acid !1sequences. !$#cross-references MUID:89243815; PMID:2718625 !$#accession C60004 !'##molecule_type mRNA !'##residues 1-57 ##label ELL !'##cross-references GB:D00663; NID:g222149; PIDN:BAA00562.1; !1PID:g222154 !'##experimental_source strain SBL GENETICS !$#gene SH CLASSIFICATION #superfamily mumps virus small hydrophobic protein KEYWORDS transmembrane protein FEATURE !$8-32 #domain transmembrane #status predicted #label TMN SUMMARY #length 57 #molecular-weight 6718 #checksum 9075 SEQUENCE /// ENTRY SHNZME #type complete TITLE small hydrophobic protein - mumps virus (strain Enders) ORGANISM #formal_name mumps virus DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jun-2000 ACCESSIONS JU0305; S24824 REFERENCE JU0304 !$#authors Takeuchi, K. !$#submission submitted to JIPID, November 1990 !$#accession JU0305 !'##molecule_type mRNA !'##residues 1-57 ##label TAK !'##cross-references GB:D90231; NID:g222156; PIDN:BAA14279.1; !1PID:g222157 !'##experimental_source strain Enders REFERENCE S19866 !$#authors Yeo, R.P.; Afzal, M.A.; Forsey, T.; Rima, B.K. !$#submission submitted to the EMBL Data Library, January 1992 !$#description Nucleotide sequence analysis of the SH gene of mumps virus !1reveals several lineages of the virus. !$#accession S24824 !'##status preliminary !'##molecule_type DNA !'##residues 1-57 ##label YEO !'##cross-references EMBL:X63705; NID:g60588; PIDN:CAA45235.1; !1PID:g60589 GENETICS !$#gene SH CLASSIFICATION #superfamily mumps virus small hydrophobic protein KEYWORDS transmembrane protein FEATURE !$10-26 #domain transmembrane #status predicted #label TM1 SUMMARY #length 57 #molecular-weight 6717 #checksum 9055 SEQUENCE /// ENTRY SHNZMJ #type complete TITLE small hydrophobic protein - mumps virus ORGANISM #formal_name mumps virus DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jun-2000 ACCESSIONS JU0306; S24826 REFERENCE JU0304 !$#authors Takeuchi, K. !$#submission submitted to JIPID, November 1990 !$#accession JU0306 !'##molecule_type mRNA !'##residues 1-57 ##label TAK !'##cross-references GB:D90232; NID:g222158; PIDN:BAA14280.1; !1PID:g222159 !'##experimental_source strain Jeryl-Lynn REFERENCE S19866 !$#authors Yeo, R.P.; Afzal, M.A.; Forsey, T.; Rima, B.K. !$#submission submitted to the EMBL Data Library, January 1992 !$#description Nucleotide sequence analysis of the SH gene of mumps virus !1reveals several lineages of the virus. !$#accession S24826 !'##status preliminary !'##molecule_type DNA !'##residues 1-57 ##label YEO !'##cross-references EMBL:X63707; NID:g60592; PIDN:CAA45239.1; !1PID:g60593 GENETICS !$#gene SH CLASSIFICATION #superfamily mumps virus small hydrophobic protein KEYWORDS transmembrane protein FEATURE !$10-26 #domain transmembrane #status predicted #label TM1 SUMMARY #length 57 #molecular-weight 6735 #checksum 9480 SEQUENCE /// ENTRY SHNZMU #type complete TITLE small hydrophobic protein - mumps virus (strain Urabe Am9) ORGANISM #formal_name mumps virus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 07-May-1999 ACCESSIONS A38479; JU0308; JQ2366; S11637 REFERENCE A38479 !$#authors Turner, P.C.; Forsey, T.; Minor, P.D. !$#journal J. Gen. Virol. (1991) 72:435-437 !$#title Comparison of the nucleotide sequence of the SH gene and !1flanking regions of mumps vaccine virus (Urabe strain) grown !1on different substrates and isolated from vaccinees. !$#cross-references MUID:91132144; PMID:1993881 !$#accession A38479 !'##molecule_type mRNA !'##residues 1-57 ##label TUR REFERENCE JU0304 !$#authors Takeuchi, K. !$#submission submitted to JIPID, November 1990 !$#accession JU0308 !'##molecule_type mRNA !'##residues 1-57 ##label TAK REFERENCE JQ2366 !$#authors Afzal, M.A.; Pickford, A.R.; Forsey, T.; Heath, A.B.; Minor, !1P.D. !$#journal J. Gen. Virol. (1993) 74:917-920 !$#title The Jeryl Lynn vaccine strain of mumps virus is a mixture of !1two distinct isolates. !$#cross-references MUID:93260409; PMID:8492099 !$#accession JQ2366 !'##molecule_type mRNA !'##residues 1-57 ##label AFZ !'##experimental_source strain Urabe GENETICS !$#gene SH CLASSIFICATION #superfamily mumps virus small hydrophobic protein KEYWORDS transmembrane protein FEATURE !$8-28 #domain transmembrane #status predicted #label TMM SUMMARY #length 57 #molecular-weight 6755 #checksum 9678 SEQUENCE /// ENTRY SHNZMS #type complete TITLE small hydrophobic protein - mumps virus (strain Miyahara) ORGANISM #formal_name mumps virus DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jun-2000 ACCESSIONS JU0304 REFERENCE JU0304 !$#authors Takeuchi, K. !$#submission submitted to JIPID, November 1990 !$#accession JU0304 !'##molecule_type mRNA !'##residues 1-57 ##label TAK !'##cross-references GB:D90234; NID:g222162; PIDN:BAA14282.1; !1PID:g222163 CLASSIFICATION #superfamily mumps virus small hydrophobic protein KEYWORDS transmembrane protein FEATURE !$13-29 #domain transmembrane #status predicted #label TM1 SUMMARY #length 57 #molecular-weight 6621 #checksum 8822 SEQUENCE /// ENTRY SHNZMM #type complete TITLE small hydrophobic protein - mumps virus ORGANISM #formal_name mumps virus DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jun-2000 ACCESSIONS JU0307; S19870 REFERENCE JU0304 !$#authors Takeuchi, K. !$#submission submitted to JIPID, November 1990 !$#accession JU0307 !'##molecule_type mRNA !'##residues 1-57 ##label TAK !'##cross-references GB:D90233; NID:g222160; PIDN:BAA14281.1; !1PID:g222161 !'##experimental_source strain Matsuyama REFERENCE S19866 !$#authors Yeo, R.P.; Afzal, M.A.; Forsey, T.; Rima, B.K. !$#submission submitted to the EMBL Data Library, January 1992 !$#description Nucleotide sequence analysis of the SH gene of mumps virus !1reveals several lineages of the virus. !$#accession S19870 !'##molecule_type DNA !'##residues 1-6,'L',8-9,'L',11-18,'Y',20-27,'VV',30-41,'A',43-47,'LF', !150-52,'L',54-57 ##label YEO !'##cross-references EMBL:X63713; NID:g60604; PIDN:CAA45246.1; !1PID:g60605 !'##experimental_source strain Bristol1 GENETICS !$#gene SH CLASSIFICATION #superfamily mumps virus small hydrophobic protein KEYWORDS transmembrane protein FEATURE !$8-29 #domain transmembrane #status predicted #label TMM SUMMARY #length 57 #molecular-weight 6697 #checksum 8 SEQUENCE /// ENTRY SHNZMT #type complete TITLE small hydrophobic protein - mumps virus (strain Takahashi) ORGANISM #formal_name mumps virus DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jun-2000 ACCESSIONS JU0309 REFERENCE JU0304 !$#authors Takeuchi, K. !$#submission submitted to JIPID, November 1990 !$#accession JU0309 !'##molecule_type mRNA !'##residues 1-57 ##label TAK !'##cross-references GB:D90235; NID:g222164; PIDN:BAA14283.1; !1PID:g222165 CLASSIFICATION #superfamily mumps virus small hydrophobic protein KEYWORDS transmembrane protein FEATURE !$13-29 #domain transmembrane #status predicted #label TM1 SUMMARY #length 57 #molecular-weight 6745 #checksum 7727 SEQUENCE /// ENTRY SHNZBF #type complete TITLE small hydrophobic protein - mumps virus (strain Belfast) ORGANISM #formal_name mumps virus DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS S19866 REFERENCE S19866 !$#authors Yeo, R.P.; Afzal, M.A.; Forsey, T.; Rima, B.K. !$#submission submitted to the EMBL Data Library, January 1992 !$#description Nucleotide sequence analysis of the SH gene of mumps virus !1reveals several lineages of the virus. !$#accession S19866 !'##molecule_type DNA !'##residues 1-57 ##label YEO !'##cross-references EMBL:X63709; NID:g60596; PIDN:CAA45242.1; !1PID:g60597 GENETICS !$#gene SH CLASSIFICATION #superfamily mumps virus small hydrophobic protein KEYWORDS transmembrane protein FEATURE !$8-29 #domain transmembrane #status predicted #label TMM SUMMARY #length 57 #molecular-weight 6814 #checksum 9838 SEQUENCE /// ENTRY SHNZE4 #type complete TITLE small hydrophobic protein - mumps virus (strain Edingburgh4) ORGANISM #formal_name mumps virus DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS S19867 REFERENCE S19866 !$#authors Yeo, R.P.; Afzal, M.A.; Forsey, T.; Rima, B.K. !$#submission submitted to the EMBL Data Library, January 1992 !$#description Nucleotide sequence analysis of the SH gene of mumps virus !1reveals several lineages of the virus. !$#accession S19867 !'##molecule_type DNA !'##residues 1-57 ##label YEO !'##cross-references EMBL:X63710; NID:g60598; PIDN:CAA45243.1; !1PID:g60599 GENETICS !$#gene SH CLASSIFICATION #superfamily mumps virus small hydrophobic protein KEYWORDS transmembrane protein FEATURE !$8-29 #domain transmembrane #status predicted #label TMM SUMMARY #length 57 #molecular-weight 6852 #checksum 1510 SEQUENCE /// ENTRY SHNZE2 #type complete TITLE small hydrophobic protein - mumps virus (strains Edinburgh2 and Edinburgh6) ORGANISM #formal_name mumps virus DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS S19868; S19869 REFERENCE S19866 !$#authors Yeo, R.P.; Afzal, M.A.; Forsey, T.; Rima, B.K. !$#submission submitted to the EMBL Data Library, January 1992 !$#description Nucleotide sequence analysis of the SH gene of mumps virus !1reveals several lineages of the virus. !$#accession S19868 !'##molecule_type DNA !'##residues 1-57 ##label YEO !'##cross-references EMBL:X63711; NID:g60600; PIDN:CAA45244.1; !1PID:g60601 !'##experimental_source strain Edinburgh2 !$#accession S19869 !'##molecule_type DNA !'##residues 1-57 ##label YE2 !'##cross-references EMBL:X63712; NID:g60602; PIDN:CAA45245.1; !1PID:g60603 !'##experimental_source strain Edinburgh6 GENETICS !$#gene SH CLASSIFICATION #superfamily mumps virus small hydrophobic protein KEYWORDS transmembrane protein FEATURE !$8-29 #domain transmembrane #status predicted #label TMM SUMMARY #length 57 #molecular-weight 6894 #checksum 1543 SEQUENCE /// ENTRY JQ1625 #type complete TITLE small hydrophobic protein - turkey rhinotracheitis virus ORGANISM #formal_name turkey rhinotracheitis virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jul-1999 ACCESSIONS JQ1625 REFERENCE PQ0405 !$#authors Ling, R.; Easton, A.J.; Pringle, C.R. !$#journal J. Gen. Virol. (1992) 73:1709-1715 !$#title Sequence analysis of the 22K, SH and G genes of turkey !1rhinotracheitis virus and their intergenic regions reveals a !1gene order different from that of other pneumoviruses. !$#cross-references MUID:92333255; PMID:1629697 !$#accession JQ1625 !'##molecule_type mRNA !'##residues 1-174 ##label LIN !'##cross-references GB:S40185; NID:g251600; PIDN:AAB22546.1; !1PID:g251604 GENETICS !$#gene SH CLASSIFICATION #superfamily turkey rhinotracheitis virus small hydrophobic !1protein KEYWORDS glycoprotein FEATURE !$165 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 174 #molecular-weight 18796 #checksum 5800 SEQUENCE /// ENTRY P1NZAR #type complete TITLE small protein 1A - human respiratory syncytial virus ORGANISM #formal_name human respiratory syncytial virus DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 16-Jul-1999 ACCESSIONS A04031 REFERENCE A04031 !$#authors Collins, P.L.; Wertz, G.W. !$#journal Virology (1985) 141:283-291 !$#title The 1A protein gene of human respiratory syncytial virus: !1nucleotide sequence of the mRNA and a related polycistronic !1transcript. !$#cross-references MUID:86098645; PMID:3879976 !$#accession A04031 !'##molecule_type genomic RNA !'##residues 1-64 ##label COL !'##cross-references GB:M11486; GB:K01459; GB:K02719; GB:K03348; !1GB:K03349; GB:M11217; GB:M11244; GB:M11487; GB:M11505; !1GB:M11514; GB:M11631; GB:M12966; GB:X00001; GB:X02221; !1NID:g333925; PIDN:AAB59856.1; PID:g333931 GENETICS !$#gene 1A CLASSIFICATION #superfamily respiratory syncytial virus small protein 1A KEYWORDS transmembrane protein SUMMARY #length 64 #molecular-weight 7536 #checksum 7618 SEQUENCE /// ENTRY P1NZRS #type complete TITLE small protein 1A - human respiratory syncytial virus (strain 18537) ORGANISM #formal_name human respiratory syncytial virus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jun-2000 ACCESSIONS A35218 REFERENCE A35218 !$#authors Collins, P.L.; Olmsted, R.A.; Johnson, P.R. !$#journal J. Gen. Virol. (1990) 71:1571-1576 !$#title The small hydrophobic protein of human respiratory syncytial !1virus: comparison between antigenic subgroups A and B. !$#cross-references MUID:90324943; PMID:2374008 !$#accession A35218 !'##molecule_type DNA !'##residues 1-65 ##label COL !'##cross-references GB:D01042; NID:g222566; PIDN:BAA00849.1; !1PID:g222567 CLASSIFICATION #superfamily respiratory syncytial virus small protein 1A KEYWORDS glycoprotein; transmembrane protein FEATURE !$23-41 #domain transmembrane #status predicted #label TMN\ !$3,52 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 65 #molecular-weight 7535 #checksum 8039 SEQUENCE /// ENTRY P1NZB3 #type complete TITLE small protein 1A - human respiratory syncytial virus (strain 8/60) ORGANISM #formal_name human respiratory syncytial virus DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 07-May-1999 ACCESSIONS B44049 REFERENCE A44049 !$#authors Anderson, K.; King, A.M.Q.; Lerch, R.A.; Wertz, G.W. !$#journal Virology (1992) 191:417-430 !$#title Polylactosaminoglycan modification of the respiratory !1syncytial virus small hydrophobic (SH) protein: a conserved !1feature among human and bovine respiratory syncytial !1viruses. !$#cross-references MUID:93033134; PMID:1413513 !$#accession B44049 !'##molecule_type genomic RNA !'##residues 1-65 ##label AND !'##cross-references GB:M86651 GENETICS !$#gene 1A CLASSIFICATION #superfamily respiratory syncytial virus small protein 1A KEYWORDS glycoprotein; transmembrane protein FEATURE !$20-40 #domain transmembrane #status predicted #label TMN\ !$3 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 65 #molecular-weight 7551 #checksum 7931 SEQUENCE /// ENTRY P1NZBR #type complete TITLE small protein 1A - bovine respiratory syncytial virus (strain A51908) ORGANISM #formal_name bovine respiratory syncytial virus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jun-2000 ACCESSIONS JQ1179; JQ0953 REFERENCE JQ1178 !$#authors Samal, S.K.; Zamora, M. !$#journal J. Gen. Virol. (1991) 72:1715-1720 !$#title Nucleotide sequence analysis of a matrix and small !1hydrophobic protein dicistronic mRNA of bovine respiratory !1syncytial virus demonstrates extensive sequence divergence !1of the small hydrophobic protein from that of human !1respiratory syncytial virus. !$#cross-references MUID:91311427; PMID:1856698 !$#accession JQ1179 !'##molecule_type mRNA !'##residues 1-73 ##label SAM !'##cross-references GB:D01012; NID:g221063; PIDN:BAA00813.1; !1PID:g221065 CLASSIFICATION #superfamily respiratory syncytial virus small protein 1A KEYWORDS glycoprotein; transmembrane protein FEATURE !$23-41 #domain transmembrane #status predicted #label TMN\ !$2,3,63 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 73 #molecular-weight 8402 #checksum 4974 SEQUENCE /// ENTRY P1NZB2 #type complete TITLE small protein 1A - bovine respiratory syncytial virus (strain 391-2) ORGANISM #formal_name bovine respiratory syncytial virus DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS A44049 REFERENCE A44049 !$#authors Anderson, K.; King, A.M.Q.; Lerch, R.A.; Wertz, G.W. !$#journal Virology (1992) 191:417-430 !$#title Polylactosaminoglycan modification of the respiratory !1syncytial virus small hydrophobic (SH) protein: a conserved !1feature among human and bovine respiratory syncytial !1viruses. !$#cross-references MUID:93033134; PMID:1413513 !$#accession A44049 !'##molecule_type genomic RNA !'##residues 1-81 ##label AND !'##cross-references GB:M86652; NID:g210832; PIDN:AAA42811.1; !1PID:g210833 GENETICS !$#gene 1A CLASSIFICATION #superfamily respiratory syncytial virus small protein 1A KEYWORDS glycoprotein; transmembrane protein FEATURE !$20-40 #domain transmembrane #status predicted #label TMN\ !$2 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 81 #molecular-weight 9306 #checksum 7804 SEQUENCE /// ENTRY HMNZHA #type complete TITLE hemagglutinin - measles virus (strain Halle) ORGANISM #formal_name measles virus DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jul-1999 ACCESSIONS A27007 REFERENCE A27007 !$#authors Gerald, C.; Buckland, R.; Barker, R.; Freeman, G.; Wild, !1T.F. !$#journal J. Gen. Virol. (1986) 67:2695-2703 !$#title Measles virus haemagglutinin gene: cloning, complete !1nucleotide sequence analysis and expression in COS cells. !$#cross-references MUID:87085487; PMID:3794664 !$#accession A27007 !'##molecule_type mRNA !'##residues 1-617 ##label GER !'##cross-references GB:X04720; NID:g60923; PIDN:CAA28427.1; PID:g60924 GENETICS !$#gene HN CLASSIFICATION #superfamily measles virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; transmembrane protein FEATURE !$35-58 #domain transmembrane #status predicted #label TRM\ !$168,187,200,215,238 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 617 #molecular-weight 69077 #checksum 358 SEQUENCE /// ENTRY HMNZED #type complete TITLE hemagglutinin - measles virus (strain Edmonston) ORGANISM #formal_name measles virus DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jul-1999 ACCESSIONS A27006; PQ0389 REFERENCE A27006 !$#authors Alkhatib, G.; Briedis, D.J. !$#journal Virology (1986) 150:479-490 !$#title The predicted primary structure of the measles virus !1hemagglutinin. !$#cross-references MUID:86181590; PMID:3008420 !$#accession A27006 !'##molecule_type mRNA !'##residues 1-617 ##label ALK !'##cross-references GB:M14877; NID:g331764; PIDN:AAA46424.1; !1PID:g331765 REFERENCE PQ0374 !$#authors Schulz, T.F.; Hoad, J.G.; Whitby, D.; Tizard, E.J.; Dillon, !1M.J.; Weiss, R.A. !$#journal J. Gen. Virol. (1992) 73:1581-1586 !$#title A measles virus isolate from a child with Kawasaki disease: !1sequence comparison with contemporaneous isolates from !1'classical' cases. !$#cross-references MUID:92300360; PMID:1607874 !$#accession PQ0389 !'##molecule_type genomic RNA !'##residues 190-522 ##label SCH !'##experimental_source strain Schwarz vaccine GENETICS !$#gene HN CLASSIFICATION #superfamily measles virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; transmembrane protein FEATURE !$35-58 #domain transmembrane #status predicted #label TRM\ !$168,187,200,215,238 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 617 #molecular-weight 69249 #checksum 674 SEQUENCE /// ENTRY F48556 #type complete TITLE hemagglutinin - measles virus (strain AIK-C) ORGANISM #formal_name measles virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS F48556 REFERENCE A48556 !$#authors Mori, T.; Sasaki, K.; Hashimoto, H.; Makino, S. !$#journal Virus Genes (1993) 7:67-81 !$#title Molecular cloning and complete nucleotide sequence of !1genomic RNA of the AIK-C strain of attenuated measles virus. !$#cross-references MUID:93227570; PMID:8470368 !$#accession F48556 !'##molecule_type genomic RNA !'##residues 1-617 ##label MOR !'##cross-references GB:S58435; NID:g299460; PIDN:AAB26146.1; !1PID:g299466 !'##note sequence extracted from NCBI backbone (NCBIN:129264, !1NCBIP:129273) GENETICS !$#gene HN CLASSIFICATION #superfamily measles virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; transmembrane protein FEATURE !$37-55 #domain transmembrane #status predicted #label TMN\ !$168,187,200,215,238 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 617 #molecular-weight 69322 #checksum 1583 SEQUENCE /// ENTRY HMNZRP #type complete TITLE hemagglutinin - rinderpest virus ORGANISM #formal_name rinderpest virus DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 16-Jul-1999 ACCESSIONS A26799 REFERENCE A26799 !$#authors Tsukiyama, K.; Sugiyama, M.; Yoshikawa, Y.; Yamanouchi, K. !$#journal Virology (1987) 160:48-54 !$#title Molecular cloning and sequence analysis of the rinderpest !1virus mRNA encoding the hemagglutinin protein. !$#cross-references MUID:87321123; PMID:3629979 !$#accession A26799 !'##molecule_type mRNA !'##residues 1-609 ##label TSU !'##cross-references GB:M17434; NID:g333904; PIDN:AAA47402.1; !1PID:g333905 GENETICS !$#gene HN CLASSIFICATION #superfamily measles virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; transmembrane protein FEATURE !$35-58 #domain transmembrane #status predicted #label TMN\ !$168,200,215,395 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 609 #molecular-weight 67657 #checksum 175 SEQUENCE /// ENTRY HMNZKA #type complete TITLE hemagglutinin - rinderpest virus (strain Kabete O) ORGANISM #formal_name rinderpest virus DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jul-1999 ACCESSIONS A31053 REFERENCE A31053 !$#authors Yamanaka, M.; Hsu, D.; Crisp, T.; Dale, B.; Grubman, M.; !1Yilma, T. !$#journal Virology (1988) 166:251-253 !$#title Cloning and sequence analysis of the hemagglutinin gene of !1the virulent strain of rinderpest virus. !$#cross-references MUID:88322878; PMID:3413986 !$#accession A31053 !'##molecule_type genomic RNA !'##residues 1-609 ##label YAM !'##cross-references GB:M21513; NID:g333902; PIDN:AAA47401.1; !1PID:g333903 GENETICS !$#gene HA CLASSIFICATION #superfamily measles virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; transmembrane protein FEATURE !$35-58 #domain transmembrane #status predicted #label TMN\ !$168,187,200,215,395 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 609 #molecular-weight 67998 #checksum 9308 SEQUENCE /// ENTRY HMNZCD #type complete TITLE hemagglutinin - canine distemper virus ORGANISM #formal_name canine distemper virus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jun-2000 ACCESSIONS A38480 REFERENCE A38480 !$#authors Curran, M.D.; Clarke, D.K.; Rima, B.K. !$#journal J. Gen. Virol. (1991) 72:443-447 !$#title The nucleotide sequence of the gene encoding the attachment !1protein H of canine distemper virus. !$#cross-references MUID:91132146; PMID:1993883 !$#accession A38480 !'##molecule_type mRNA !'##residues 1-604 ##label CUR !'##cross-references GB:D00758; NID:g221113; PIDN:BAA00654.1; !1PID:g221114 GENETICS !$#gene H CLASSIFICATION #superfamily measles virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; transmembrane protein FEATURE !$35-58 #domain transmembrane #status predicted #label TMN\ !$19,149,422,587 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 604 #molecular-weight 67988 #checksum 3534 SEQUENCE /// ENTRY HMNZPD #type complete TITLE hemagglutinin - phocine distemper virus ORGANISM #formal_name phocine distemper virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS JQ1369 REFERENCE JQ1368 !$#authors Koevamees, J.; Blixenkrone-Moeller, M.; Sharma, B.; Oervell, !1C.; Norrby, E. !$#journal J. Gen. Virol. (1991) 72:2959-2966 !$#title The nucleotide sequence and deduced amino acid composition !1of the haemagglutinin and fusion proteins of the !1morbillivirus phocid distemper virus. !$#cross-references MUID:92113538; PMID:1765768 !$#accession JQ1369 !'##molecule_type genomic RNA !'##residues 1-607 ##label KOV !'##cross-references GB:Z36979; NID:g536790; PIDN:CAA85428.1; !1PID:g536791 GENETICS !$#gene H CLASSIFICATION #superfamily measles virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; transmembrane protein FEATURE !$39-55 #domain transmembrane #status predicted #label TMN\ !$19,149,276,391,422, !$456,587 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 607 #molecular-weight 68961 #checksum 3248 SEQUENCE /// ENTRY JQ1535 #type complete TITLE hemagglutinin - phocine distemper virus (strain Ulster/88) ALTERNATE_NAMES attachment protein ORGANISM #formal_name phocine distemper virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 09-Sep-1994 ACCESSIONS JQ1535 REFERENCE JQ1535 !$#authors Curran, M.D.; O'Loan, D.; Kennedy, S.; Rima, B.K. !$#journal J. Gen. Virol. (1992) 73:1189-1194 !$#title Molecular characterization of phocine distemper virus: Gene !1order and sequence of the gene encoding the attachment (H) !1protein. !$#cross-references MUID:92268877; PMID:1588321 !$#accession JQ1535 !'##molecule_type mRNA !'##residues 1-607 ##label CUR !'##cross-references GB:D10371 GENETICS !$#gene H CLASSIFICATION #superfamily measles virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; transmembrane protein FEATURE !$39-55 #domain transmembrane #status predicted #label TMN\ !$19,149,276,391,422, !$456,587 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 607 #molecular-weight 68969 #checksum 4542 SEQUENCE /// ENTRY HMIVV #type complete TITLE hemagglutinin precursor - influenza A virus (strain A/ Victoria/3/75) ORGANISM #formal_name influenza A virus DATE 28-Feb-1981 #sequence_revision 28-Feb-1981 #text_change 28-May-1999 ACCESSIONS A90794; A04050; A92790 REFERENCE A90794 !$#authors Min Jou, W.; Verhoeyen, M.; Devos, R.; Saman, E.; Fang, R.; !1Huylebroeck, D.; Fiers, W.; Threlfall, G.; Barber, C.; !1Carey, N.; Emtage, S. !$#journal Cell (1980) 19:683-696 !$#title Complete structure of the hemagglutinin gene from the human !1influenza A/Victoria/3/75 (H3N2) strain as determined from !1cloned DNA. !$#cross-references MUID:80155186; PMID:6153930 !$#accession A90794 !'##molecule_type genomic RNA !'##residues 1-567 ##label MIN !'##cross-references GB:V01098; GB:J02172; GB:M55060; NID:g60784; !1PIDN:CAA24281.1; PID:g60785 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS hemagglutinin; homotrimer; lipoprotein; thiolester bond FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-345 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$347-567 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$537-553 #domain transmembrane #status predicted #label TM1\ !$31-483,69-294, !$81-93,156-490, !$298-322 #disulfide_bonds #status predicted\ !$556,563,566 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 567 #molecular-weight 63422 #checksum 7034 SEQUENCE /// ENTRY HMIVH3 #type fragment TITLE hemagglutinin precursor - influenza A virus (strain A/ Memphis/1/71 [H3]) (fragment) ORGANISM #formal_name influenza A virus DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 15-Oct-1996 ACCESSIONS A04060 REFERENCE A93902 !$#authors Air, G.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:7639-7643 !$#title Sequence relationships among the hemagglutinin genes of 12 !1subtypes of influenza A virus. !$#cross-references MUID:82150925; PMID:6174976 !$#accession A04060 !'##molecule_type genomic RNA !'##residues 1-120 ##label AIR GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS hemagglutinin; homotrimer FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-120 #product hemagglutinin HA1 chain (fragment) #status !8predicted #label HA1 SUMMARY #length 120 #checksum 1533 SEQUENCE /// ENTRY HMIVH #type complete TITLE hemagglutinin precursor - influenza A virus ORGANISM #formal_name influenza A virus DATE 28-Feb-1981 #sequence_revision 28-Feb-1981 #text_change 22-Oct-1999 ACCESSIONS A93705; A93233; A04051; A93231; A94441 REFERENCE A93705 !$#authors Both, G.W.; Sleigh, M.J. !$#journal Nucleic Acids Res. (1980) 8:2561-2575 !$#title Complete nucleotide sequence of the haemagglutinin gene from !1a human influenza virus of the Hong Kong subtype. !$#cross-references MUID:81053698; PMID:6253883 !$#accession A93705 !'##molecule_type genomic RNA !'##residues 1-566 ##label BOT !'##cross-references GB:V01103 !'##experimental_source strain A/NT/60/68/29C !'##note human influenza strain A/NT/60/68/29C is a laboratory-isolated !1variant of A/NT/60/68, an early strain of the Hong Kong !1subtype REFERENCE A91276 !$#authors Dopheide, T.A.; Ward, C.W. !$#journal FEBS Lett. (1980) 110:181-183 !$#title The disulphide bonds of a Hong Kong influenza virus !1hemagglutinin. !$#cross-references MUID:80179105; PMID:6768586 !$#contents annotation; disulfide bonds REFERENCE A93233 !$#authors Gething, M.J.; Bye, J.; Skehel, J.; Waterfield, M. !$#journal Nature (1980) 287:301-306 !$#title Cloning and DNA sequence of double-stranded copies of !1haemagglutinin genes from H2 and H3 strains elucidates !1antigenic shift and drift in human influenza virus. !$#cross-references MUID:81030852; PMID:7421990 !$#accession A93233 !'##molecule_type genomic RNA !'##residues 1-24,'S',26,'D',28-159,'G',161-197,'I',199-241,'L',243-249 !1##label GET !'##experimental_source strain X-31[H3] CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS hemagglutinin; homotrimer; lipoprotein; thiolester bond FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-344 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$346-566 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$536-552 #domain transmembrane #status predicted #label TM1\ !$30-482,68-293, !$80-92,155-489, !$297-321 #disulfide_bonds #status experimental\ !$555,562,565 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 566 #molecular-weight 63487 #checksum 6880 SEQUENCE /// ENTRY HMIVHA #type complete TITLE hemagglutinin precursor - influenza A virus (strain A/Aichi/ 2/68) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 19-May-1994 #sequence_revision 19-May-1994 #text_change 16-Jul-1999 ACCESSIONS A93231; A04051 REFERENCE A93231 !$#authors Verhoeyen, M.; Fang, R.; Min Jou, W.; Devos, R.; !1Huylebroeck, D.; Saman, E.; Fiers, W. !$#journal Nature (1980) 286:771-776 !$#title Antigenic drift between the haemagglutinin of the Hong Kong !1influenza strains A/Aichi/2/68 and A/Victoria/3/75. !$#cross-references MUID:80254693; PMID:7402351 !$#accession A93231 !'##molecule_type genomic RNA !'##residues 1-566 ##label VER !'##cross-references GB:J02090; NID:g324131; PIDN:AAA43178.1; !1PID:g324132 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS hemagglutinin; homotrimer; lipoprotein; thiolester bond FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-344 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$346-566 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$555,562,565 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 566 #molecular-weight 63415 #checksum 6743 SEQUENCE /// ENTRY HMIVHM #type complete TITLE hemagglutinin precursor - influenza A virus (strain A/Mem/ 102/72) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 19-May-1994 #sequence_revision 19-May-1994 #text_change 31-Mar-2000 ACCESSIONS A94441; A04051 REFERENCE A94441 !$#authors Sleigh, M.J.; Both, G.W.; Brownlee, G.G.; Bender, V.J.; !1Moss, B.A. !$#book Structure and Variation in Influenza Virus, Laver, G., and !1Air, G., eds., pp.69-79, Elsevier North-Holland, New York, !11980 !$#title The haemagglutinin gene of influenza A virus: nucleotide !1sequence analysis of cloned DNA copies. !$#accession A94441 !'##molecule_type genomic RNA !'##residues 1-566 ##label SLE CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS hemagglutinin; homotrimer; lipoprotein; thiolester bond FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-344 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$346-566 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$555,562,565 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 566 #molecular-weight 63264 #checksum 5347 SEQUENCE /// ENTRY HMIVS2 #type fragment TITLE hemagglutinin precursor - influenza A virus (strain A/swine/ 126/82) (fragment) ORGANISM #formal_name influenza A virus DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 18-Sep-1998 ACCESSIONS A29971 REFERENCE A94370 !$#authors Kida, H.; Shortridge, K.F.; Webster, R.G. !$#journal Virology (1988) 162:160-166 !$#title Origin of the hemagglutinin gene of H3N2 influenza viruses !1from pigs in China. !$#cross-references MUID:88101364; PMID:3336940 !$#accession A29971 !'##molecule_type genomic RNA !'##residues 1-550 ##label KID !'##cross-references GB:M19056; NID:g324208 !'##note the sequence in GenBank entry FLAHAPA, release 106, !1(PID:g324209) differs from the sequence in Fig. 1 in !1omitting the nucleotides GCATTT before the final !1dinucleotide GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer; lipoprotein; !1thiolester bond FEATURE !$1-328 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$330-550 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$520-536 #domain transmembrane #status predicted #label TM1\ !$8,22,38,165,285,483 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$14-466,52-277, !$64-76,139-473, !$281-305 #disulfide_bonds #status predicted\ !$539,546,549 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 550 #checksum 4430 SEQUENCE /// ENTRY HMIVS3 #type fragment TITLE hemagglutinin precursor - influenza A virus (strain A/swine/ 81/78) (fragment) ORGANISM #formal_name influenza A virus DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 18-Sep-1998 ACCESSIONS B29971 REFERENCE A94370 !$#authors Kida, H.; Shortridge, K.F.; Webster, R.G. !$#journal Virology (1988) 162:160-166 !$#title Origin of the hemagglutinin gene of H3N2 influenza viruses !1from pigs in China. !$#cross-references MUID:88101364; PMID:3336940 !$#accession B29971 !'##molecule_type genomic RNA !'##residues 1-550 ##label KID !'##cross-references GB:M19057; NID:g324210 !'##note the sequence in GenBank entry FLAHAPB, release 106, !1(PID:g324211) differs from the sequence in Fig. 1 in !1omitting the nucleotides GCATTT before the final !1dinucleotide GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer; lipoprotein; !1thiolester bond FEATURE !$1-328 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$300-550 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$520-536 #domain transmembrane #status predicted #label TM1\ !$8,22,38,165,285,483 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$14-466,52-277, !$64-76,139-473, !$281-305 #disulfide_bonds #status predicted\ !$539,546,549 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 550 #checksum 3973 SEQUENCE /// ENTRY HMIV77 #type fragment TITLE hemagglutinin precursor - influenza A virus (strain A/duck/ Hokkaido/5/77) (fragment) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jul-1999 ACCESSIONS A27813 REFERENCE A94363 !$#authors Kida, H.; Kawaoka, Y.; Naeve, C.W.; Webster, R.G. !$#journal Virology (1987) 159:109-119 !$#title Antigenic and genetic conservation of H3 influenza virus in !1wild ducks. !$#cross-references MUID:87265458; PMID:2440178 !$#accession A27813 !'##molecule_type genomic RNA !'##residues 1-550 ##label KID !'##cross-references GB:M16737; NID:g324081; PIDN:AAA43143.1; !1PID:g324082 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer; lipoprotein; !1thiolester bond FEATURE !$1-328 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$330-550 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$520-536 #domain transmembrane #status predicted #label TM1\ !$8,22,38,165,285,483 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$14-466,52-277, !$64-76,139-473, !$281-305 #disulfide_bonds #status predicted\ !$539,546,549 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 550 #checksum 4839 SEQUENCE /// ENTRY HMIV80 #type fragment TITLE hemagglutinin precursor - influenza A virus (strain A/duck/ Hokkaido/8/80) (fragment) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 18-Sep-1998 ACCESSIONS B27813 REFERENCE A94363 !$#authors Kida, H.; Kawaoka, Y.; Naeve, C.W.; Webster, R.G. !$#journal Virology (1987) 159:109-119 !$#title Antigenic and genetic conservation of H3 influenza virus in !1wild ducks. !$#cross-references MUID:87265458; PMID:2440178 !$#accession B27813 !'##molecule_type genomic RNA !'##residues 1-550 ##label KID !'##cross-references GB:M16738; NID:g324083 !'##note the translation in Fig. 2 is inconsistent with the nucleotide !1sequence in Fig. 1 in having 137-Asn rather than Lys for !1codon AAG GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer; lipoprotein; !1thiolester bond FEATURE !$1-328 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$330-550 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$520-536 #domain transmembrane #status predicted #label TM1\ !$8,22,38,165,285,483 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$14-466,52-277, !$64-76,139-473, !$281-305 #disulfide_bonds #status predicted\ !$539,546,549 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 550 #checksum 4376 SEQUENCE /// ENTRY HMIV33 #type fragment TITLE hemagglutinin precursor - influenza A virus (strain A/duck/ Hokkaido/33/80) (fragment) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jul-1999 ACCESSIONS C27813 REFERENCE A94363 !$#authors Kida, H.; Kawaoka, Y.; Naeve, C.W.; Webster, R.G. !$#journal Virology (1987) 159:109-119 !$#title Antigenic and genetic conservation of H3 influenza virus in !1wild ducks. !$#cross-references MUID:87265458; PMID:2440178 !$#accession C27813 !'##molecule_type genomic RNA !'##residues 1-550 ##label KID !'##cross-references GB:M16739; NID:g324085; PIDN:AAA43145.1; !1PID:g324086 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer; lipoprotein; !1thiolester bond FEATURE !$1-328 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$330-550 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$520-536 #domain transmembrane #status predicted #label TM1\ !$8,22,38,165,285,483 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$14-466,52-277, !$64-76,139-473, !$281-305 #disulfide_bonds #status predicted\ !$539,546,549 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 550 #checksum 3746 SEQUENCE /// ENTRY HMIV89 #type fragment TITLE hemagglutinin precursor - influenza A virus (strain A/duck/ Hokkaido/7/82) (fragment) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jul-1999 ACCESSIONS D27813 REFERENCE A94363 !$#authors Kida, H.; Kawaoka, Y.; Naeve, C.W.; Webster, R.G. !$#journal Virology (1987) 159:109-119 !$#title Antigenic and genetic conservation of H3 influenza virus in !1wild ducks. !$#cross-references MUID:87265458; PMID:2440178 !$#accession D27813 !'##molecule_type genomic RNA !'##residues 1-550 ##label KID !'##cross-references GB:M16740; NID:g324087; PIDN:AAA43146.1; !1PID:g324088 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer; lipoprotein; !1thiolester bond FEATURE !$1-328 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$330-550 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$520-536 #domain transmembrane #status predicted #label TM1\ !$8,22,38,165,285,483 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$14-466,52-277, !$64-76,139-473, !$281-305 #disulfide_bonds #status predicted\ !$539,546,549 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 550 #checksum 5402 SEQUENCE /// ENTRY HMIV21 #type fragment TITLE hemagglutinin precursor - influenza A virus (strain A/duck/ Hokkaido/21/82) (fragment) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 18-Sep-1998 ACCESSIONS E27813 REFERENCE A94363 !$#authors Kida, H.; Kawaoka, Y.; Naeve, C.W.; Webster, R.G. !$#journal Virology (1987) 159:109-119 !$#title Antigenic and genetic conservation of H3 influenza virus in !1wild ducks. !$#cross-references MUID:87265458; PMID:2440178 !$#accession E27813 !'##molecule_type genomic RNA !'##residues 1-550 ##label KID !'##cross-references GB:M16741; NID:g324089 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer FEATURE !$1-328 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$330-550 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$520-536 #domain transmembrane #status predicted #label TM1\ !$7,8,22,38,165,285, !$483 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$14-466,52-277, !$64-76,139-473, !$281-305 #disulfide_bonds #status predicted SUMMARY #length 550 #checksum 6313 SEQUENCE /// ENTRY HMIV98 #type fragment TITLE hemagglutinin precursor - influenza A virus (strain A/duck/ Hokkaido/9/85) (fragment) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 18-Sep-1998 ACCESSIONS F27813 REFERENCE A94363 !$#authors Kida, H.; Kawaoka, Y.; Naeve, C.W.; Webster, R.G. !$#journal Virology (1987) 159:109-119 !$#title Antigenic and genetic conservation of H3 influenza virus in !1wild ducks. !$#cross-references MUID:87265458; PMID:2440178 !$#accession F27813 !'##molecule_type genomic RNA !'##residues 1-550 ##label KID !'##cross-references GB:M16742; NID:g324091 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer; lipoprotein; !1thiolester bond FEATURE !$1-328 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$330-550 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$520-536 #domain transmembrane #status predicted #label TM1\ !$8,22,38,165,285,483 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$14-466,52-277, !$64-76,139-473, !$281-305 #disulfide_bonds #status predicted\ !$539,546,549 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 550 #checksum 5355 SEQUENCE /// ENTRY HMIV15 #type fragment TITLE hemagglutinin precursor - influenza A virus (strain A/duck/ Hokkaido/10/85) (fragment) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jul-1999 ACCESSIONS G27813 REFERENCE A94363 !$#authors Kida, H.; Kawaoka, Y.; Naeve, C.W.; Webster, R.G. !$#journal Virology (1987) 159:109-119 !$#title Antigenic and genetic conservation of H3 influenza virus in !1wild ducks. !$#cross-references MUID:87265458; PMID:2440178 !$#accession G27813 !'##molecule_type genomic RNA !'##residues 1-550 ##label KID !'##cross-references GB:M16743; NID:g324093; PIDN:AAA43149.1; !1PID:g324094 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer; lipoprotein; !1thiolester bond FEATURE !$1-328 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$330-550 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$520-536 #domain transmembrane #status predicted #label TM1\ !$8,22,38,165,285,483 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$14-466,52-277, !$64-76,139-473, !$281-305 #disulfide_bonds #status predicted\ !$539,546,549 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 550 #checksum 5685 SEQUENCE /// ENTRY HMIV6 #type complete TITLE hemagglutinin precursor - influenza A virus (strain A/ England/321/77) ORGANISM #formal_name influenza A virus DATE 05-Apr-1983 #sequence_revision 14-Nov-1983 #text_change 22-Oct-1999 ACCESSIONS B92790; A92979; A04052 REFERENCE A92790 !$#authors Hauptmann, R.; Clarke, L.D.; Mountford, R.C.; Bachmayer, H.; !1Almond, J.W. !$#journal J. Gen. Virol. (1983) 64:215-220 !$#title Nucleotide sequence of the haemagglutinin gene of influenza !1virus A/England/321/77. !$#cross-references MUID:83110955; PMID:6822816 !$#accession B92790 !'##molecule_type genomic RNA !'##residues 1-566 ##label HAU !'##cross-references GB:X05907; NID:g60694; PIDN:CAA29337.1; PID:g60695 !'##note the authors translated the codon GUU for residue 14 as Asn, GCC !1for residue 16 as Pro, and GCA for residue 32 as Gly REFERENCE A92979 !$#authors Both, G.W.; Sleigh, M.J. !$#journal J. Virol. (1981) 39:663-672 !$#title Conservation and variation in the hemagglutinins of Hong !1Kong subtype influenza viruses during antigenic drift. !$#cross-references MUID:82033259; PMID:6169840 !$#accession A92979 !'##molecule_type genomic RNA !'##residues 17-31,'G',33-148,'S',150-158,'S',160-171,'E',173-175,'K', !1177-187,'G',189-208,'N',210-212,'R',214-232,'I',234-309,'X', !1311-362,'XX',365-524,'X',526-552,'XX',555-566 ##label BOT !'##cross-references GB:J02092; NID:g324139; PIDN:AAA43182.1; !1PID:g324140 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS hemagglutinin; homotrimer; lipoprotein; thiolester bond FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-344 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$346-566 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$536-552 #domain transmembrane #status predicted #label TM1\ !$30-482,68-293, !$80-92,155-489, !$297-321 #disulfide_bonds #status predicted\ !$555,562,565 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 566 #molecular-weight 63608 #checksum 5554 SEQUENCE /// ENTRY HMIV86 #type fragment TITLE hemagglutinin precursor - influenza A virus (strain A/Mem/6/ 86 [H3N2]) (fragment) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jul-1999 ACCESSIONS A29245 REFERENCE A29245 !$#authors Katz, J.M.; Webster, R.G. !$#journal Virology (1988) 165:446-456 !$#title Antigenic and structural characterization of multiple !1subpopulations of H3N2 influenza virus from an individual. !$#cross-references MUID:88306236; PMID:3407150 !$#accession A29245 !'##molecule_type genomic RNA !'##residues 1-550 ##label KAT !'##cross-references GB:M21648; NID:g324295; PIDN:AAA43275.1; !1PID:g324296 GENETICS !$#gene HA !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer; lipoprotein; !1thiolester bond FEATURE !$1-328 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$330-550 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$520-536 #domain transmembrane #status predicted #label TM1\ !$8,22,38,63,126,165, !$246,285,483 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$14-466,52-277, !$64-76,139-473, !$281-305 #disulfide_bonds #status predicted\ !$539,546,549 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 550 #checksum 3428 SEQUENCE /// ENTRY HMIVDU #type complete TITLE hemagglutinin precursor - influenza A virus (strain A/duck/ Ukraine/63) ORGANISM #formal_name influenza A virus DATE 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 28-May-1999 ACCESSIONS A04053 REFERENCE A04053 !$#authors Fang, R.; Min Jou, W.; Huylebroeck, D.; Devos, R.; Fiers, W. !$#journal Cell (1981) 25:315-323 !$#title Complete structure of A/duck/Ukraine/63 influenza !1hemagglutinin gene: animal virus as progenitor of human H3 !1Hong Kong 1968 influenza hemagglutinin. !$#cross-references MUID:82025542; PMID:6169439 !$#accession A04053 !'##molecule_type genomic RNA !'##residues 1-566 ##label FAN !'##cross-references GB:V01087; GB:J02109; NID:g60756; PIDN:CAA24271.1; !1PID:g60757 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS hemagglutinin; homotrimer; lipoprotein; thiolester bond FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-344 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$346-566 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$536-552 #domain transmembrane #status predicted #label TM1\ !$30-482,68-293, !$80-92,155-489, !$297-321 #disulfide_bonds #status predicted\ !$555,562,565 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 566 #molecular-weight 63529 #checksum 5712 SEQUENCE /// ENTRY HMIVE1 #type complete TITLE hemagglutinin precursor - influenza A virus (strain A/ equine/Uruguay/1/63[H3N8]) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS A34064 REFERENCE A34064 !$#authors Kawaoka, Y.; Bean, W.J.; Webster, R.G. !$#journal Virology (1989) 169:283-292 !$#title Evolution of the hemagglutinin of equine H3 influenza !1viruses. !$#cross-references MUID:89204899; PMID:2705299 !$#accession A34064 !'##molecule_type genomic RNA !'##residues 1-565 ##label KAW !'##cross-references GB:M24718; GB:J04336; NID:g324024; PIDN:AAA43114.1; !1PID:g324025 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer; lipoprotein; !1thiolester bond FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-344 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$345-565 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$535-551 #domain transmembrane #status predicted #label TM1\ !$29-481,67-292, !$79-91,154-488, !$296-320 #disulfide_bonds #status predicted\ !$37,53,78,180,300, !$498 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$554,561,564 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 565 #molecular-weight 63604 #checksum 4846 SEQUENCE /// ENTRY HMIVE2 #type complete TITLE hemagglutinin precursor - influenza A virus (strain A/ equine/Miami/1/63[H3N8]) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS B34064 REFERENCE A34064 !$#authors Kawaoka, Y.; Bean, W.J.; Webster, R.G. !$#journal Virology (1989) 169:283-292 !$#title Evolution of the hemagglutinin of equine H3 influenza !1viruses. !$#cross-references MUID:89204899; PMID:2705299 !$#accession B34064 !'##molecule_type genomic RNA !'##residues 1-565 ##label KAW !'##cross-references GB:M24719; GB:J04336; NID:g324006; PIDN:AAA43105.1; !1PID:g324007 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer; lipoprotein; !1thiolester bond FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-344 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$345-565 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$535-551 #domain transmembrane #status predicted #label TM1\ !$18,23,37,53,78,180, !$300,498 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$29-481,67-292, !$154-488,296-320 #disulfide_bonds #status predicted\ !$554,561,564 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 565 #molecular-weight 63729 #checksum 5628 SEQUENCE /// ENTRY HMIVE3 #type complete TITLE hemagglutinin precursor - influenza A virus (strain A/ equine/Tokyo/71[H3N8]) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS C34064 REFERENCE A34064 !$#authors Kawaoka, Y.; Bean, W.J.; Webster, R.G. !$#journal Virology (1989) 169:283-292 !$#title Evolution of the hemagglutinin of equine H3 influenza !1viruses. !$#cross-references MUID:89204899; PMID:2705299 !$#accession C34064 !'##molecule_type genomic RNA !'##residues 1-565 ##label KAW !'##cross-references GB:M24720; GB:J04336; NID:g324018; PIDN:AAA43111.1; !1PID:g324019 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer; lipoprotein; !1thiolester bond FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-344 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$345-565 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$535-551 #domain transmembrane #status predicted #label TM1\ !$23,37,53,68,78,180, !$300,498 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$29-481,67-292, !$79-91,154-488, !$296-320 #disulfide_bonds #status predicted\ !$554,561,564 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 565 #molecular-weight 63580 #checksum 3980 SEQUENCE /// ENTRY HMIVE4 #type complete TITLE hemagglutinin precursor - influenza A virus (strain A/ equine/Algiers/72[H3N8]) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS D34064 REFERENCE A34064 !$#authors Kawaoka, Y.; Bean, W.J.; Webster, R.G. !$#journal Virology (1989) 169:283-292 !$#title Evolution of the hemagglutinin of equine H3 influenza !1viruses. !$#cross-references MUID:89204899; PMID:2705299 !$#accession D34064 !'##molecule_type genomic RNA !'##residues 1-565 ##label KAW !'##cross-references GB:M24721; GB:J04336; NID:g323996; PIDN:AAA43100.1; !1PID:g323997 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer; lipoprotein; !1thiolester bond FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-344 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$345-565 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$535-551 #domain transmembrane #status predicted #label TM1\ !$23,37,53,78,180, !$300,498 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$29-481,67-292, !$79-91,154-488, !$296-320 #disulfide_bonds #status predicted\ !$554,561,564 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 565 #molecular-weight 63831 #checksum 4800 SEQUENCE /// ENTRY HMIVE5 #type complete TITLE hemagglutinin precursor - influenza A virus (strain A/ equine/New Market/76[H3N8]) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS E34064 REFERENCE A34064 !$#authors Kawaoka, Y.; Bean, W.J.; Webster, R.G. !$#journal Virology (1989) 169:283-292 !$#title Evolution of the hemagglutinin of equine H3 influenza !1viruses. !$#cross-references MUID:89204899; PMID:2705299 !$#accession E34064 !'##molecule_type genomic RNA !'##residues 1-565 ##label KAW !'##cross-references GB:M24722; GB:J04336; NID:g324010; PIDN:AAA43107.1; !1PID:g324011 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer; lipoprotein; !1thiolester bond FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-344 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$345-565 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$535-551 #domain transmembrane #status predicted #label TM1\ !$23,37,53,78,180, !$300,498 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$29-481,67-292, !$79-91,154-488, !$296-320 #disulfide_bonds #status predicted\ !$554,561,564 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 565 #molecular-weight 63749 #checksum 4207 SEQUENCE /// ENTRY HMIVE6 #type complete TITLE hemagglutinin precursor - influenza A virus (strain A/ equine/Fontainebleau/76[H3N8]) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS F34064 REFERENCE A34064 !$#authors Kawaoka, Y.; Bean, W.J.; Webster, R.G. !$#journal Virology (1989) 169:283-292 !$#title Evolution of the hemagglutinin of equine H3 influenza !1viruses. !$#cross-references MUID:89204899; PMID:2705299 !$#accession F34064 !'##molecule_type genomic RNA !'##residues 1-565 ##label KAW !'##cross-references GB:M24723; GB:J04336; NID:g323998; PIDN:AAA43101.1; !1PID:g323999 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer; lipoprotein; !1thiolester bond FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-344 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$345-565 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$535-551 #domain transmembrane #status predicted #label TM1\ !$18,23,37,53,78,180, !$300,498 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$29-481,67-292, !$79-91,154-488, !$296-320 #disulfide_bonds #status predicted\ !$554,561,564 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 565 #molecular-weight 63686 #checksum 4895 SEQUENCE /// ENTRY HMIVE7 #type complete TITLE hemagglutinin precursor - influenza A virus (strain A/ equine/Romania/80[H3N8]) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS G34064 REFERENCE A34064 !$#authors Kawaoka, Y.; Bean, W.J.; Webster, R.G. !$#journal Virology (1989) 169:283-292 !$#title Evolution of the hemagglutinin of equine H3 influenza !1viruses. !$#cross-references MUID:89204899; PMID:2705299 !$#accession G34064 !'##molecule_type genomic RNA !'##residues 1-565 ##label KAW !'##cross-references GB:M24724; GB:J04336; NID:g324014; PIDN:AAA43109.1; !1PID:g324015 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer; lipoprotein; !1thiolester bond FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-344 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$345-565 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$535-551 #domain transmembrane #status predicted #label TM1\ !$18,23,37,53,78,180, !$300,498 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$29-481,67-292, !$79-91,154-488, !$296-320 #disulfide_bonds #status predicted\ !$554,561,564 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 565 #molecular-weight 63660 #checksum 4278 SEQUENCE /// ENTRY HMIVE8 #type complete TITLE hemagglutinin precursor - influenza A virus (strain A/ equine/Santiago/1/85[H3N8]) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS H34064 REFERENCE A34064 !$#authors Kawaoka, Y.; Bean, W.J.; Webster, R.G. !$#journal Virology (1989) 169:283-292 !$#title Evolution of the hemagglutinin of equine H3 influenza !1viruses. !$#cross-references MUID:89204899; PMID:2705299 !$#accession H34064 !'##molecule_type genomic RNA !'##residues 1-565 ##label KAW !'##cross-references GB:M24725; GB:J04336; NID:g324016; PIDN:AAA43110.1; !1PID:g324017 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer; lipoprotein; !1thiolester bond FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-344 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$345-565 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$535-551 #domain transmembrane #status predicted #label TM1\ !$18,23,37,53,78,180, !$300,498 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$29-481,67-292, !$79-91,154-488, !$296-320 #disulfide_bonds #status predicted\ !$554,561,564 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 565 #molecular-weight 63665 #checksum 7024 SEQUENCE /// ENTRY HMIVE9 #type complete TITLE hemagglutinin precursor - influenza A virus (strain A/ equine/Tennessee/5/85[H3N8]) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS I34064 REFERENCE A34064 !$#authors Kawaoka, Y.; Bean, W.J.; Webster, R.G. !$#journal Virology (1989) 169:283-292 !$#title Evolution of the hemagglutinin of equine H3 influenza !1viruses. !$#cross-references MUID:89204899; PMID:2705299 !$#accession I34064 !'##molecule_type genomic RNA !'##residues 1-565 ##label KAW !'##cross-references GB:M24726; GB:J04336; NID:g324020; PIDN:AAA43112.1; !1PID:g324021 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer; lipoprotein; !1thiolester bond FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-344 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$345-565 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$535-551 #domain transmembrane #status predicted #label TM1\ !$18,23,37,53,68,78, !$180,300,498 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$29-481,67-292, !$79-91,154-488, !$296-320 #disulfide_bonds #status predicted\ !$554,561,564 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 565 #molecular-weight 63688 #checksum 5499 SEQUENCE /// ENTRY HMIVET #type complete TITLE hemagglutinin precursor - influenza A virus (strain A/ equine/Kentucky/2/86[H3N8]) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS A34065 REFERENCE A34064 !$#authors Kawaoka, Y.; Bean, W.J.; Webster, R.G. !$#journal Virology (1989) 169:283-292 !$#title Evolution of the hemagglutinin of equine H3 influenza !1viruses. !$#cross-references MUID:89204899; PMID:2705299 !$#accession A34065 !'##molecule_type genomic RNA !'##residues 1-565 ##label KAW !'##cross-references GB:M24727; GB:J04336; NID:g324000; PIDN:AAA43102.1; !1PID:g324001 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer; lipoprotein; !1thiolester bond FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-344 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$345-565 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$535-551 #domain transmembrane #status predicted #label TM1\ !$18,23,37,53,68,78, !$180,300,498 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$29-481,67-292, !$79-91,154-488, !$296-320 #disulfide_bonds #status predicted\ !$554,561,564 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 565 #molecular-weight 63610 #checksum 6051 SEQUENCE /// ENTRY HMIVEE #type complete TITLE hemagglutinin precursor - influenza A virus (strain A/ equine/Kentucky/1/87[H3N8]) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS B34065 REFERENCE A34064 !$#authors Kawaoka, Y.; Bean, W.J.; Webster, R.G. !$#journal Virology (1989) 169:283-292 !$#title Evolution of the hemagglutinin of equine H3 influenza !1viruses. !$#cross-references MUID:89204899; PMID:2705299 !$#accession B34065 !'##molecule_type genomic RNA !'##residues 1-565 ##label KAW !'##cross-references GB:M24728; GB:J04336; NID:g324002; PIDN:AAA43103.1; !1PID:g324003 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer; lipoprotein; !1thiolester bond FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-344 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$345-565 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$535-551 #domain transmembrane #status predicted #label TM1\ !$18,23,37,53,68,78, !$180,300,498 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$29-481,67-292, !$79-91,154-488, !$296-320 #disulfide_bonds #status predicted\ !$554,561,564 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 565 #molecular-weight 63702 #checksum 5766 SEQUENCE /// ENTRY A45591 #type complete TITLE hemagglutinin precursor - influenza A virus (strain A/ equine/Prague/56 [H7N7]) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 24-Feb-1994 #sequence_revision 24-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS A45591; S22019 REFERENCE A45591 !$#authors Gibson, C.A.; Daniels, R.S.; Oxford, J.S.; McCauley, J.W. !$#journal Virus Res. (1992) 22:93-106 !$#title Sequence analysis of the equine H7 influenza virus !1haemagglutinin gene. !$#cross-references MUID:92230399; PMID:1566601 !$#accession A45591 !'##molecule_type genomic RNA !'##residues 1-570 ##label GIB !'##cross-references GB:X62552; GB:S96523; NID:g59203; PIDN:CAA44429.1; !1PID:g59204 !'##note sequence extracted from NCBI backbone (NCBIN:96523, !1NCBIP:96524) GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer FEATURE !$1-12 #domain signal sequence #status predicted #label SIG\ !$13-349 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$350-570 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$30,46,167,249,431, !$503 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 570 #molecular-weight 64138 #checksum 8274 SEQUENCE /// ENTRY HMIVF1 #type complete TITLE hemagglutinin precursor - influenza A virus (strain A/duck/ Czeckoslovakia/56 [H4N6]) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jun-2000 ACCESSIONS A34214; D39987; A33157 REFERENCE A34214 !$#authors Donis, R.O.; Bean, W.J.; Kawaoka, Y.; Webster, R.G. !$#journal Virology (1989) 169:408-417 !$#title Distinct lineages of influenza virus H4 hemagglutinin genes !1in different regions of the world. !$#cross-references MUID:89204912; PMID:2705304 !$#accession A34214 !'##molecule_type genomic RNA !'##residues 1-564 ##label DON !'##cross-references GB:M25283; NID:g324218; PIDN:AAA43216.1; !1PID:g324219 REFERENCE A39987 !$#authors Nobusawa, E.; Aoyama, T.; Kato, H.; Suzuki, Y.; Tateno, Y.; !1Nakajima, K. !$#journal Virology (1991) 182:475-485 !$#title Comparison of complete amino acid sequences and !1receptor-binding properties among 13 serotypes of !1hemagglutinins of influenza A viruses. !$#cross-references MUID:91220697; PMID:2024485 !$#accession D39987 !'##molecule_type genomic RNA !'##residues 1-156,'D',158-200,'S',202-213,'R',215-228,'D',230-269,'H', !1271-424,'N',426-488,'N',490-564 ##label NOB !'##cross-references GB:D90302; NID:g221313; PIDN:BAA14332.1; !1PID:g221314 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer; lipoprotein; !1thiolester bond; transmembrane protein FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-343 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$344-564 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$534-550 #domain transmembrane #status predicted #label TM1\ !$18,34,178,310,497 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$26-480,64-291, !$76-88,151-487, !$295-319 #disulfide_bonds #status predicted\ !$553,560,563 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 564 #molecular-weight 63206 #checksum 6407 SEQUENCE /// ENTRY HMIVF2 #type complete TITLE hemagglutinin precursor - influenza A virus (strain A/grey teal/Australia/2/79 [H4N4]) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS B34214 REFERENCE A34214 !$#authors Donis, R.O.; Bean, W.J.; Kawaoka, Y.; Webster, R.G. !$#journal Virology (1989) 169:408-417 !$#title Distinct lineages of influenza virus H4 hemagglutinin genes !1in different regions of the world. !$#cross-references MUID:89204912; PMID:2705304 !$#accession B34214 !'##molecule_type genomic RNA !'##residues 1-564 ##label DON !'##cross-references GB:M25284; NID:g324220; PIDN:AAA43217.1; !1PID:g324221 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer; lipoprotein; !1thiolester bond FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-343 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$344-564 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$534-550 #domain transmembrane #status predicted #label TM1\ !$14,18,34,178,229, !$310,497 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$26-480,64-291, !$76-88,151-487, !$295-319 #disulfide_bonds #status predicted\ !$553,560,563 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 564 #molecular-weight 63237 #checksum 5514 SEQUENCE /// ENTRY HMIVF4 #type complete TITLE hemagglutinin precursor - influenza A virus (strain A/duck/ New Zealand/31/76 [H4N6]) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 18-Sep-1998 ACCESSIONS D34214 REFERENCE A34214 !$#authors Donis, R.O.; Bean, W.J.; Kawaoka, Y.; Webster, R.G. !$#journal Virology (1989) 169:408-417 !$#title Distinct lineages of influenza virus H4 hemagglutinin genes !1in different regions of the world. !$#cross-references MUID:89204912; PMID:2705304 !$#accession D34214 !'##molecule_type genomic RNA !'##residues 1-564 ##label DON GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer; lipoprotein; !1thiolester bond FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-343 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$344-564 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$534-550 #domain transmembrane #status predicted #label TM1\ !$18,34,178,497 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$26-480,64-291, !$76-88,151-487, !$295-319 #disulfide_bonds #status predicted\ !$553,560,563 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 564 #molecular-weight 63119 #checksum 3831 SEQUENCE /// ENTRY HMIVF5 #type complete TITLE hemagglutinin precursor - influenza A virus (strain A/duck/ Alberta/28/76 [H4N6]) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS E34214 REFERENCE A34214 !$#authors Donis, R.O.; Bean, W.J.; Kawaoka, Y.; Webster, R.G. !$#journal Virology (1989) 169:408-417 !$#title Distinct lineages of influenza virus H4 hemagglutinin genes !1in different regions of the world. !$#cross-references MUID:89204912; PMID:2705304 !$#accession E34214 !'##molecule_type genomic RNA !'##residues 1-564 ##label DON !'##cross-references GB:M25287; NID:g324226; PIDN:AAA43220.1; !1PID:g324227 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer; lipoprotein; !1thiolester bond FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-343 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$344-564 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$534-550 #domain transmembrane #status predicted #label TM1\ !$18,34,178,310,497 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$26-480,64-291, !$76-88,151-487, !$295-319 #disulfide_bonds #status predicted\ !$553,560,563 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 564 #molecular-weight 63381 #checksum 7529 SEQUENCE /// ENTRY HMIVF6 #type complete TITLE hemagglutinin precursor - influenza A virus (strain A/ chicken/Alabama/1/75 [H4N8]) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS F34214 REFERENCE A34214 !$#authors Donis, R.O.; Bean, W.J.; Kawaoka, Y.; Webster, R.G. !$#journal Virology (1989) 169:408-417 !$#title Distinct lineages of influenza virus H4 hemagglutinin genes !1in different regions of the world. !$#cross-references MUID:89204912; PMID:2705304 !$#accession F34214 !'##molecule_type genomic RNA !'##residues 1-564 ##label DON !'##cross-references GB:M25288; NID:g324228; PIDN:AAA43221.1; !1PID:g324229 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer; lipoprotein; !1thiolester bond FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-343 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$344-564 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$534-550 #domain transmembrane #status predicted #label TM1\ !$18,34,178,310,497 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$26-480,64-291, !$76-88,151-487, !$295-319 #disulfide_bonds #status predicted\ !$553,560,563 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 564 #molecular-weight 63264 #checksum 7366 SEQUENCE /// ENTRY HMIVF7 #type complete TITLE hemagglutinin precursor - influenza A virus (strain A/ruddy turnstone/NJ/47/85 [H4N6]) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 18-Sep-1998 ACCESSIONS G34214 REFERENCE A34214 !$#authors Donis, R.O.; Bean, W.J.; Kawaoka, Y.; Webster, R.G. !$#journal Virology (1989) 169:408-417 !$#title Distinct lineages of influenza virus H4 hemagglutinin genes !1in different regions of the world. !$#cross-references MUID:89204912; PMID:2705304 !$#accession G34214 !'##molecule_type genomic RNA !'##residues 1-564 ##label DON GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer; lipoprotein; !1thiolester bond FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-343 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$344-564 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$534-550 #domain transmembrane #status predicted #label TM1\ !$18,34,178,310,497 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$26-480,64-291, !$76-88,151-487, !$295-319 #disulfide_bonds #status predicted\ !$553,560,563 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 564 #molecular-weight 63271 #checksum 7890 SEQUENCE /// ENTRY HMIVF8 #type complete TITLE hemagglutinin precursor - influenza A virus (strain A/ turkey/Minnesota/833/80 [H4N2]) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS H34214 REFERENCE A34214 !$#authors Donis, R.O.; Bean, W.J.; Kawaoka, Y.; Webster, R.G. !$#journal Virology (1989) 169:408-417 !$#title Distinct lineages of influenza virus H4 hemagglutinin genes !1in different regions of the world. !$#cross-references MUID:89204912; PMID:2705304 !$#accession H34214 !'##molecule_type genomic RNA !'##residues 1-564 ##label DON !'##cross-references GB:M25290; NID:g456423; PIDN:AAA43223.1; !1PID:g456424 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer; lipoprotein; !1thiolester bond FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-343 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$344-564 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$534-550 #domain transmembrane #status predicted #label TM1\ !$18,34,178,310,497 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$26-480,64-291, !$76-88,151-487, !$295-319 #disulfide_bonds #status predicted\ !$553,560,563 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 564 #molecular-weight 63249 #checksum 8025 SEQUENCE /// ENTRY HMIVF9 #type complete TITLE hemagglutinin precursor - influenza A virus (strain A/seal/ Massachusetts/133/82 [H4N5]) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 18-Sep-1998 ACCESSIONS I34214 REFERENCE A34214 !$#authors Donis, R.O.; Bean, W.J.; Kawaoka, Y.; Webster, R.G. !$#journal Virology (1989) 169:408-417 !$#title Distinct lineages of influenza virus H4 hemagglutinin genes !1in different regions of the world. !$#cross-references MUID:89204912; PMID:2705304 !$#accession I34214 !'##molecule_type genomic RNA !'##residues 1-564 ##label DON GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer; lipoprotein; !1thiolester bond FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-343 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$344-564 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$534-550 #domain transmembrane #status predicted #label TM1\ !$18,34,178,310,497 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$26-480,64-291, !$76-88,151-487, !$295-319 #disulfide_bonds #status predicted\ !$553,560,563 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 564 #molecular-weight 63165 #checksum 7979 SEQUENCE /// ENTRY HMIVF3 #type complete TITLE hemagglutinin precursor - influenza A virus (strain A/ budgerigar/Hokkaido/1/77 [H4N6]) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS C34214 REFERENCE A34214 !$#authors Donis, R.O.; Bean, W.J.; Kawaoka, Y.; Webster, R.G. !$#journal Virology (1989) 169:408-417 !$#title Distinct lineages of influenza virus H4 hemagglutinin genes !1in different regions of the world. !$#cross-references MUID:89204912; PMID:2705304 !$#accession C34214 !'##molecule_type genomic RNA !'##residues 1-564 ##label DON !'##cross-references GB:M25285; NID:g324222; PIDN:AAA43218.1; !1PID:g324223 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer; lipoprotein; !1thiolester bond FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-343 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$344-564 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$534-550 #domain transmembrane #status predicted #label TM1\ !$14,34,178,310,497 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$26-480,64-291, !$76-88,151-487, !$295-319 #disulfide_bonds #status predicted\ !$553,560,563 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 564 #molecular-weight 63188 #checksum 9167 SEQUENCE /// ENTRY HMIVH4 #type fragment TITLE hemagglutinin precursor - influenza A virus (strain A/duck/ Alberta/28/76 [H4]) (fragment) ORGANISM #formal_name influenza A virus DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 16-Jul-1999 ACCESSIONS A04054 REFERENCE A93902 !$#authors Air, G.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:7639-7643 !$#title Sequence relationships among the hemagglutinin genes of 12 !1subtypes of influenza A virus. !$#cross-references MUID:82150925; PMID:6174976 !$#accession A04054 !'##molecule_type genomic RNA !'##residues 1-101 ##label AIR !'##cross-references GB:J02102; NID:g324133; PIDN:AAA43179.1; !1PID:g324134 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS hemagglutinin; homotrimer FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-101 #product hemagglutinin HA1 chain (fragment) #status !8predicted #label HA1 SUMMARY #length 101 #checksum 1288 SEQUENCE /// ENTRY A46339 #type complete TITLE hemagglutinin precursor - influenza A virus (strain A/ Mallard/Gurjev/263/82 [H14N5]) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 18-Sep-1998 ACCESSIONS A46339 REFERENCE A46339 !$#authors Kawaoka, Y.; Yamnikova, S.; Chambers, T.M.; Lvov, D.K.; !1Webster, R.G. !$#journal Virology (1990) 179:759-767 !$#title Molecular characterization of a new hemagglutinin, subtype !1H14, of influenza A virus. !$#cross-references MUID:91049442; PMID:2238469 !$#accession A46339 !'##molecule_type genomic RNA !'##residues 1-568 ##label KAW !'##cross-references GB:M35997 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer; lipoprotein; !1thiolester bond; transmembrane protein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-347 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$348-568 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$534-554 #domain transmembrane #status predicted #label TMN\ !$21,38,62,182,242, !$314,501 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$557,564,567 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 568 #molecular-weight 63149 #checksum 4880 SEQUENCE /// ENTRY HMIVH5 #type fragment TITLE hemagglutinin precursor - influenza A virus (strain A/ shearwater/Australia/75 [H5]) (fragment) ORGANISM #formal_name influenza A virus DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 16-Jul-1999 ACCESSIONS A04058 REFERENCE A93902 !$#authors Air, G.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:7639-7643 !$#title Sequence relationships among the hemagglutinin genes of 12 !1subtypes of influenza A virus. !$#cross-references MUID:82150925; PMID:6174976 !$#accession A04058 !'##molecule_type genomic RNA !'##residues 1-109 ##label AIR !'##cross-references GB:J02160; NID:g324176; PIDN:AAA43199.1; !1PID:g324177 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS hemagglutinin; homotrimer FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-109 #product hemagglutinin A1 chain (fragment) #status !8predicted #label HA1 SUMMARY #length 109 #checksum 1407 SEQUENCE /// ENTRY HMIVH6 #type fragment TITLE hemagglutinin precursor - influenza A virus (strain A/ shearwater/Australia/72 [H6]) (fragment) ORGANISM #formal_name influenza A virus DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 16-Jul-1999 ACCESSIONS A04059 REFERENCE A93902 !$#authors Air, G.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:7639-7643 !$#title Sequence relationships among the hemagglutinin genes of 12 !1subtypes of influenza A virus. !$#cross-references MUID:82150925; PMID:6174976 !$#accession A04059 !'##molecule_type genomic RNA !'##residues 1-97 ##label AIR !'##cross-references GB:J02158; NID:g324174; PIDN:AAA43198.1; !1PID:g324175 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS hemagglutinin; homotrimer FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-97 #product hemagglutinin HA1 chain (fragment) #status !8predicted #label HA1 SUMMARY #length 97 #checksum 9600 SEQUENCE /// ENTRY HMIVH2 #type fragment TITLE hemagglutinin precursor - influenza A virus (strain A/RI/5-/ 57 [H2]) (fragment) ORGANISM #formal_name influenza A virus DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 16-Jul-1999 ACCESSIONS A04061 REFERENCE A93902 !$#authors Air, G.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:7639-7643 !$#title Sequence relationships among the hemagglutinin genes of 12 !1subtypes of influenza A virus. !$#cross-references MUID:82150925; PMID:6174976 !$#accession A04061 !'##molecule_type genomic RNA !'##residues 1-108 ##label AIR !'##cross-references GB:J02154; NID:g324170; PIDN:AAA43196.1; !1PID:g324171 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS hemagglutinin; homotrimer FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-108 #product hemagglutinin HA1 chain (fragment) #status !8predicted #label HA1 SUMMARY #length 108 #checksum 5987 SEQUENCE /// ENTRY HMIV2 #type complete TITLE hemagglutinin precursor - influenza A virus (strain A/Japan/ 305/57[H2]) ORGANISM #formal_name influenza A virus #variety strain A/Japan/305/57[H2] DATE 28-Feb-1981 #sequence_revision 28-Feb-1981 #text_change 16-Jul-1999 ACCESSIONS A04062; S12270 REFERENCE A93233 !$#authors Gething, M.J.; Bye, J.; Skehel, J.; Waterfield, M. !$#journal Nature (1980) 287:301-306 !$#title Cloning and DNA sequence of double-stranded copies of !1haemagglutinin genes from H2 and H3 strains elucidates !1antigenic shift and drift in human influenza virus. !$#cross-references MUID:81030852; PMID:7421990 !$#accession A04062 !'##molecule_type mRNA !'##residues 1-562 ##label GET !'##cross-references GB:J02127; NID:g324145; PIDN:AAA43185.1; !1PID:g324146 !'##experimental_source strain A/Japan/305/57[H2] REFERENCE S12270 !$#authors Naeve, C.W.; Williams, D. !$#journal EMBO J. (1990) 9:3857-3866 !$#title Fatty acids on the A/Japan/305/57 influenza virus !1hemagglutinin have a role in membrane fusion. !$#cross-references MUID:91065313; PMID:2249653 !$#accession S12270 !'##molecule_type mRNA !'##residues 510-562 ##label NAE !'##experimental_source strain A/Japan/305/57 (H2N2) CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS hemagglutinin; homotrimer; lipoprotein; thiolester bond FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-339 #product hemagglutinin chain HA1 #status predicted !8#label HA1\ !$341-562 #product hemagglutinin chain HA2 #status predicted !8#label HA2\ !$551,558,561 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 562 #molecular-weight 63118 #checksum 2217 SEQUENCE /// ENTRY HMIV #type complete TITLE hemagglutinin precursor - influenza A virus (strain A/PR/8/ 34) ORGANISM #formal_name influenza A virus DATE 18-Dec-1981 #sequence_revision 18-Dec-1981 #text_change 28-May-1999 ACCESSIONS A93262; A90830; A04063 REFERENCE A93262 !$#authors Winter, G.; Fields, S.; Brownlee, G.G. !$#journal Nature (1981) 292:72-75 !$#title Nucleotide sequence of the haemagglutinin gene of a human !1influenza virus H1 subtype. !$#cross-references MUID:82013600; PMID:7278968 !$#accession A93262 !'##molecule_type genomic RNA !'##residues 1-566 ##label WIN !'##cross-references GB:V01088; GB:J02143; NID:g62290; PIDN:CAA24272.1; !1PID:g62291 REFERENCE A90830 !$#authors Caton, A.J.; Brownlee, G.G.; Yewdell, J.W.; Gerhard, W. !$#journal Cell (1982) 31:417-427 !$#title The antigenic structure of the influenza virus A/PR/8/34 !1hemagglutinin (H1 subtype). !$#cross-references MUID:83129356; PMID:6186384 !$#contents subtype H1 !$#accession A90830 !'##molecule_type genomic RNA !'##residues 18-145,'N',148-155,'E',157-199,'P',201-203,'E',205-207,'L', !1209-268,'M',270-308,'Y',310-343 ##label CAT GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS hemagglutinin; homotrimer; lipoprotein; thiolester bond FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-343 #product hemagglutinin HA1 chain #status predicted !8#label HA1\ !$345-566 #product hemagglutinin HA2 chain #status predicted !8#label HA2\ !$555,562,565 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 566 #molecular-weight 63380 #checksum 1931 SEQUENCE /// ENTRY HMIVUR #type complete TITLE hemagglutinin precursor - influenza A virus (strain A/USSR/ 90/77) ORGANISM #formal_name influenza A virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS A04064 REFERENCE A04064 !$#authors Concannon, P.; Cummings, I.W.; Salser, W.A. !$#journal J. Virol. (1984) 49:276-278 !$#title Nucleotide sequence of the influenza virus A/USSR/90/77 !1hemagglutinin gene. !$#cross-references MUID:84090410; PMID:6690716 !$#accession A04064 !'##molecule_type genomic RNA !'##residues 1-566 ##label CON !'##cross-references GB:K01330; NID:g324193; PIDN:AAA43206.1; !1PID:g554652 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS hemagglutinin; homotrimer; lipoprotein; thiolester bond FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-343 #product hemagglutinin HA1 chain #status predicted !8#label HA1\ !$345-566 #product hemagglutinin HA2 chain #status predicted !8#label HA2\ !$555,562,565 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 566 #molecular-weight 63460 #checksum 3121 SEQUENCE /// ENTRY HMIVTA #type complete TITLE hemagglutinin HA1 - influenza A virus (strain A/Taiwan/1/ 86[HA1]) ORGANISM #formal_name influenza A virus DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 08-Apr-1994 ACCESSIONS A26765 REFERENCE A26765 !$#authors Robertson, J.S. !$#journal J. Gen. Virol. (1987) 68:1205-1208 !$#title Sequence analysis of the haemagglutinin of A/Taiwan/1/86, a !1new variant of human influenza A(H1N1) virus. !$#cross-references MUID:87197215; PMID:3572359 !$#accession A26765 !'##molecule_type DNA !'##residues 1-343 ##label ROB GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer FEATURE !$27,28,40,71,104, !$142,172,177,286,304 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 343 #molecular-weight 38278 #checksum 5864 SEQUENCE /// ENTRY HMIV5 #type complete TITLE hemagglutinin precursor - influenza A virus (strain A/WSN/33 [H0N1]) ORGANISM #formal_name influenza A virus DATE 05-Apr-1983 #sequence_revision 05-Apr-1983 #text_change 16-Jul-1999 ACCESSIONS A04065 REFERENCE A04065 !$#authors Hiti, A.L.; Davis, A.R.; Nayak, D.P. !$#journal Virology (1981) 111:113-124 !$#title Complete sequence analysis shows that the hemagglutinins of !1the H0 and H2 subtypes of human influenza virus are closely !1related. !$#cross-references MUID:81202406; PMID:7233828 !$#accession A04065 !'##molecule_type genomic RNA !'##residues 1-565 ##label HIT !'##cross-references GB:J02176; GB:M25009; GB:M25010; GB:M38365; !1NID:g324199; PIDN:AAA43209.1; PID:g324200 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS hemagglutinin; homotrimer; lipoprotein; thiolester bond FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-342 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$344-565 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$21-480,59-291, !$72-84,152-487, !$295-319 #disulfide_bonds #status predicted\ !$554,561,564 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 565 #molecular-weight 63524 #checksum 448 SEQUENCE /// ENTRY HMIVN1 #type complete TITLE hemagglutinin precursor - influenza A virus (strain A/swine/ NJ/11/76[H1N1]) ORGANISM #formal_name influenza A virus DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS A04066 REFERENCE A04066 !$#authors Both, G.W.; Shi, C.H.; Kilbourne, E.D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:6996-7000 !$#title Hemagglutinin of swine influenza virus: a single amino acid !1change pleiotropically affects viral antigenicity and !1replication. !$#cross-references MUID:84070755; PMID:6580621 !$#accession A04066 !'##molecule_type genomic RNA !'##residues 1-566 ##label BOT !'##cross-references GB:K00992; GB:M57477; NID:g324158; PIDN:AAB39851.1; !1PID:g324159 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS hemagglutinin; homotrimer; lipoprotein; thiolester bond FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-343 #product hemagglutinin HA1 chain #status predicted !8#label HA1\ !$345-566 #product hemagglutinin HA2 chain #status predicted !8#label HA2\ !$555,562,565 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 566 #molecular-weight 63303 #checksum 3485 SEQUENCE /// ENTRY HMIV17 #type complete TITLE hemagglutinin precursor - influenza A virus (strain A/Swine/ Indiana/1726/88 [H1N1]) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 18-Sep-1998 ACCESSIONS A41807 REFERENCE A41807 !$#authors Luoh, S.M.; McGregor, M.W.; Hinshaw, V.S. !$#journal J. Virol. (1992) 66:1066-1073 !$#title Hemagglutinin mutations related to antigenic variation in H1 !1swine influenza viruses. !$#cross-references MUID:92114128; PMID:1731091 !$#accession A41807 !'##molecule_type genomic RNA !'##residues 1-566 ##label LUO !'##cross-references GB:M81707 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer; lipoprotein; !1thiolester bond; transmembrane protein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-344 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$345-566 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$530-546 #domain transmembrane #status predicted #label TM1\ !$27,28,40,104,293, !$304,498,505 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$555,562,565 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 566 #molecular-weight 63321 #checksum 3225 SEQUENCE /// ENTRY HMIVD1 #type complete TITLE hemagglutinin precursor - influenza A virus (strain A/duck/ Alberta/35/76 [H1N1]) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 18-Sep-1998 ACCESSIONS A36257 REFERENCE A36257 !$#authors Austin, F.J.; Kawaoka, Y.; Webster, R.G. !$#journal J. Gen. Virol. (1990) 71:2471-2474 !$#title Molecular analysis of the haemagglutinin gene of an avian !1H1N1 influenza virus. !$#cross-references MUID:91037983; PMID:2230742 !$#accession A36257 !'##molecule_type mRNA !'##residues 1-566 ##label AUS GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer; lipoprotein; !1thiolester bond FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-344 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$345-566 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$27,28,40,104,304, !$498,557 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$555,562,565 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 566 #molecular-weight 63026 #checksum 3419 SEQUENCE /// ENTRY HMIVGM #type complete TITLE hemagglutinin precursor - influenza A virus (strain A/gull/ Maryland/704/77 [H13N6]) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 09-Sep-1994 ACCESSIONS C39987 REFERENCE A39987 !$#authors Nobusawa, E.; Aoyama, T.; Kato, H.; Suzuki, Y.; Tateno, Y.; !1Nakajima, K. !$#journal Virology (1991) 182:475-485 !$#title Comparison of complete amino acid sequences and !1receptor-binding properties among 13 serotypes of !1hemagglutinins of influenza A viruses. !$#cross-references MUID:91220697; PMID:2024485 !$#accession C39987 !'##molecule_type genomic RNA !'##residues 1-565 ##label NOB !'##cross-references GB:D90308 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer; transmembrane !1protein FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-342 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$343-565 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$536-552 #domain transmembrane #status predicted #label TM1\ !$29,54,182,183,305, !$488,497 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 565 #molecular-weight 63207 #checksum 3020 SEQUENCE /// ENTRY HMIVT1 #type complete TITLE hemagglutinin precursor - influenza A virus (strain A/ ring-billed gull/Maryland/704/77 [H13N6]) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 22-Oct-1999 ACCESSIONS A32664; G33157 REFERENCE A32664 !$#authors Chambers, T.M.; Yamnikova, S.; Kawaoka, Y.; Lvov, D.K.; !1Webster, R.G. !$#journal Virology (1989) 172:180-188 !$#title Antigenic and molecular characterization of subtype H13 !1hemagglutinin of influenza virus. !$#cross-references MUID:89370299; PMID:2773315 !$#accession A32664 !'##molecule_type genomic RNA !'##residues 1-566 ##label CHA !'##cross-references GB:M26090; GB:J04370; NID:g324214; PIDN:AAA43214.1; !1PID:g324215 REFERENCE A33157 !$#authors Nobusawa, E.; Aoyama, T.; Kato, H.; Suzuki, Y.; Tateno, Y.; !1Nakajima, K. !$#submission submitted to the Protein Sequence Database, February 1991 !$#accession G33157 !'##status preliminary; not compared with conceptual translation !'##molecule_type genomic RNA !'##residues 1-79,'V',81-171,'T',173-566 ##label NOB GENETICS !$#gene HA !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-342 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$344-566 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$29,54,182,183,305, !$488,497 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 566 #molecular-weight 63265 #checksum 6993 SEQUENCE /// ENTRY HMIVT2 #type complete TITLE hemagglutinin precursor - influenza A virus (strain A/pilot whale/Maine/328 HN/84 [H13N2]) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS B32664 REFERENCE A32664 !$#authors Chambers, T.M.; Yamnikova, S.; Kawaoka, Y.; Lvov, D.K.; !1Webster, R.G. !$#journal Virology (1989) 172:180-188 !$#title Antigenic and molecular characterization of subtype H13 !1hemagglutinin of influenza virus. !$#cross-references MUID:89370299; PMID:2773315 !$#accession B32664 !'##molecule_type genomic RNA !'##residues 1-566 ##label CHA !'##cross-references GB:M26091; GB:J04370; NID:g324216; PIDN:AAA43215.1; !1PID:g324217 GENETICS !$#gene HA CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-342 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$344-566 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$29,54,182,183,305, !$488,497 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 566 #molecular-weight 63049 #checksum 8524 SEQUENCE /// ENTRY HMIVT3 #type complete TITLE hemagglutinin precursor - influenza A virus (strain A/ black-headed gull/Astrachan/227/84 [H13N6]) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 12-Apr-1996 ACCESSIONS C32664 REFERENCE A32664 !$#authors Chambers, T.M.; Yamnikova, S.; Kawaoka, Y.; Lvov, D.K.; !1Webster, R.G. !$#journal Virology (1989) 172:180-188 !$#title Antigenic and molecular characterization of subtype H13 !1hemagglutinin of influenza virus. !$#cross-references MUID:89370299; PMID:2773315 !$#accession C32664 !'##molecule_type genomic RNA !'##residues 1-565 ##label CHA GENETICS !$#gene HA CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-341 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$343-565 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$29,181,182,304,487, !$496,500 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 565 #molecular-weight 63011 #checksum 4704 SEQUENCE /// ENTRY HMIVTW #type complete TITLE hemagglutinin precursor - influenza A virus (strain A/ turkey/Wisconsin/66 [H9N2]) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jun-2000 ACCESSIONS G39987; A04068; D33157 REFERENCE A39987 !$#authors Nobusawa, E.; Aoyama, T.; Kato, H.; Suzuki, Y.; Tateno, Y.; !1Nakajima, K. !$#journal Virology (1991) 182:475-485 !$#title Comparison of complete amino acid sequences and !1receptor-binding properties among 13 serotypes of !1hemagglutinins of influenza A viruses. !$#cross-references MUID:91220697; PMID:2024485 !$#accession G39987 !'##molecule_type genomic RNA !'##residues 1-560 ##label NOB !'##cross-references GB:D90305; NID:g221319; PIDN:BAA14335.1; !1PID:g221320 REFERENCE A93902 !$#authors Air, G.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:7639-7643 !$#title Sequence relationships among the hemagglutinin genes of 12 !1subtypes of influenza A virus. !$#cross-references MUID:82150925; PMID:6174976 !$#accession A04068 !'##molecule_type genomic RNA !'##residues 1-99 ##label AIR !'##cross-references GB:J02166; NID:g324197; PIDN:AAA43208.1; !1PID:g324198 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer; transmembrane !1protein FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-338 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$339-560 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$530-546 #domain transmembrane #status predicted #label TM1\ !$29,141,218,298,305, !$492 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 560 #molecular-weight 62652 #checksum 7974 SEQUENCE /// ENTRY HMIVC2 #type complete TITLE hemagglutinin precursor - influenza A virus (strain chicken/ Scotland/59[H5N1]) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS S01276; S24588 REFERENCE S01276 !$#authors De, B.K.; Brownlee, G.G.; Kendal, A.P.; Shaw, M.W. !$#journal Nucleic Acids Res. (1988) 16:4181-4182 !$#title Complete sequence of a cDNA clone of the hemagglutinin gene !1of influenza A/Chicken/Scotland/59 (H5N1) virus: comparison !1with contemporary North American and European strains. !$#cross-references MUID:88234030; PMID:3375087 !$#accession S01276 !'##molecule_type mRNA !'##residues 1-564 ##label DE1 !'##cross-references EMBL:X07826; NID:g60702; PIDN:CAA30680.1; !1PID:g60703 !'##experimental_source strain chicken/Scotland/59[H5N1] !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1988 !'##note the authors translated the codon TGG for residues 76 and 138 as !1Tyr, CTG for residue 89 as Val, and GTC for residue 273 as !1Ala GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer; lipoprotein; !1thiolester bond; transmembrane protein FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-341 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$343-564 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$534-550 #domain transmembrane #status predicted #label TMN\ !$26,39,170,181,209, !$302,496,555 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$553,560,563 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 564 #molecular-weight 63860 #checksum 2110 SEQUENCE /// ENTRY HMIVTN #type complete TITLE hemagglutinin precursor - influenza A virus (strain A/ turkey/Ontario/6118/68) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jun-2000 ACCESSIONS F39987; A04067; C33157 REFERENCE A39987 !$#authors Nobusawa, E.; Aoyama, T.; Kato, H.; Suzuki, Y.; Tateno, Y.; !1Nakajima, K. !$#journal Virology (1991) 182:475-485 !$#title Comparison of complete amino acid sequences and !1receptor-binding properties among 13 serotypes of !1hemagglutinins of influenza A viruses. !$#cross-references MUID:91220697; PMID:2024485 !$#accession F39987 !'##molecule_type genomic RNA !'##residues 1-565 ##label NOB !'##cross-references GB:D90304; NID:g221317; PIDN:BAA14334.1; !1PID:g221318 !'##experimental_source strain A/turkey/Ontario/6118/68 [H8N4] REFERENCE A93902 !$#authors Air, G.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:7639-7643 !$#title Sequence relationships among the hemagglutinin genes of 12 !1subtypes of influenza A virus. !$#cross-references MUID:82150925; PMID:6174976 !$#accession A04067 !'##molecule_type genomic RNA !'##residues 1-8,'M',10,'L',11-35,'T',37-88,'VN',91-99 ##label AIR !'##cross-references GB:J02089; NID:g324129; PIDN:AAA43177.1; !1PID:g324130 !'##experimental_source strain A/turkey/Ontario/6118/68 [H8] !'##note the signal sequence and the amino end of the HA1 chain comprise !1residues 1-16 and 17-99, respectively GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer; transmembrane !1protein FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-343 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$344-565 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$536-552 #domain transmembrane #status predicted #label TM1\ !$26,27,139,150,222, !$303,310,497,524 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 565 #molecular-weight 63518 #checksum 9909 SEQUENCE /// ENTRY HMIVSA #type complete TITLE hemagglutinin precursor - influenza A virus (strain A/ shearwater/Australia/1/72 [H6N5]) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jun-2000 ACCESSIONS E39987; B33157 REFERENCE A39987 !$#authors Nobusawa, E.; Aoyama, T.; Kato, H.; Suzuki, Y.; Tateno, Y.; !1Nakajima, K. !$#journal Virology (1991) 182:475-485 !$#title Comparison of complete amino acid sequences and !1receptor-binding properties among 13 serotypes of !1hemagglutinins of influenza A viruses. !$#cross-references MUID:91220697; PMID:2024485 !$#accession E39987 !'##molecule_type genomic RNA !'##residues 1-566 ##label NOB !'##cross-references GB:D90303; NID:g221315; PIDN:BAA14333.1; !1PID:g221316 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer; lipoprotein; !1thiolester bond; transmembrane protein FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-344 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$345-566 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$539-555 #domain transmembrane #status predicted #label TM1\ !$26,27,39,182,306, !$498 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$555,562,565 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 566 #molecular-weight 63392 #checksum 4671 SEQUENCE /// ENTRY HMIVDE #type complete TITLE hemagglutinin precursor - influenza A virus (strain A/duck/ England/56 [H11N6]) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jun-2000 ACCESSIONS A39987; E33157 REFERENCE A39987 !$#authors Nobusawa, E.; Aoyama, T.; Kato, H.; Suzuki, Y.; Tateno, Y.; !1Nakajima, K. !$#journal Virology (1991) 182:475-485 !$#title Comparison of complete amino acid sequences and !1receptor-binding properties among 13 serotypes of !1hemagglutinins of influenza A viruses. !$#cross-references MUID:91220697; PMID:2024485 !$#accession A39987 !'##molecule_type genomic RNA !'##residues 1-565 ##label NOB !'##cross-references GB:D90306; NID:g221307; PIDN:BAA14336.1; !1PID:g221308 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer; lipoprotein; !1thiolester bond; transmembrane protein FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-342 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$343-565 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$535-551 #domain transmembrane #status predicted #label TM1\ !$26,27,39,181,304, !$496 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$554,561,564 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 565 #molecular-weight 63097 #checksum 1203 SEQUENCE /// ENTRY HMIVDA #type complete TITLE hemagglutinin precursor - influenza A virus CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jun-2000 ACCESSIONS B39987; A04057; F33157 REFERENCE A39987 !$#authors Nobusawa, E.; Aoyama, T.; Kato, H.; Suzuki, Y.; Tateno, Y.; !1Nakajima, K. !$#journal Virology (1991) 182:475-485 !$#title Comparison of complete amino acid sequences and !1receptor-binding properties among 13 serotypes of !1hemagglutinins of influenza A viruses. !$#cross-references MUID:91220697; PMID:2024485 !$#accession B39987 !'##molecule_type genomic RNA !'##residues 1-564 ##label NOB !'##cross-references GB:D90307; NID:g221309; PIDN:BAA14337.1; !1PID:g221310 !'##experimental_source strain A/duck/Alberta/60/76 [H12N5] REFERENCE A93902 !$#authors Air, G.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:7639-7643 !$#title Sequence relationships among the hemagglutinin genes of 12 !1subtypes of influenza A virus. !$#cross-references MUID:82150925; PMID:6174976 !$#accession A04057 !'##molecule_type genomic RNA !'##residues 1-38,'L',40-51,'G',53-101 ##label AIR !'##cross-references GB:J02104; NID:g324135; PIDN:AAA43180.1; !1PID:g324136 !'##experimental_source strain A/duck/Alberta/60/76 [H12] !'##note the signal sequence and the amino end of the HA1 chain comprise !1residues 1-17 and 18-101, respectively GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer; transmembrane !1protein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-342 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$343-564 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$535-551 #domain transmembrane #status predicted #label TM1\ !$27,28,140,151,152, !$222,302,309,496,523 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 564 #molecular-weight 63713 #checksum 2832 SEQUENCE /// ENTRY HMIVAT #type complete TITLE hemagglutinin precursor - influenza A virus (strain A/ Turkey/Ontario/7732/66 [H5N9]) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 18-Sep-1998 ACCESSIONS A34828 REFERENCE A34828 !$#authors Philpott, M.; Hioe, C.; Sheerar, M.; Hinshaw, V.S. !$#journal J. Virol. (1990) 64:2941-2947 !$#title Hemagglutinin mutations related to attenuation and altered !1cell tropism of virulent avian influenza A virus. !$#cross-references MUID:90244411; PMID:2335822 !$#accession A34828 !'##molecule_type mRNA !'##residues 1-566 ##label PHI GENETICS !$#gene HA !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer; lipoprotein; !1thiolester bond; transmembrane protein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-343 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$344-566 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$534-550 #domain transmembrane #status predicted #label TMN\ !$27,39,100,181,497 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$555,562,565 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 566 #molecular-weight 63914 #checksum 9407 SEQUENCE /// ENTRY HMIVT8 #type complete TITLE hemagglutinin precursor - influenza A virus (strain A/ turkey/Ireland/1378/83 [H5N8]) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 16-Jul-1999 ACCESSIONS A26184 REFERENCE A94359 !$#authors Kawaoka, Y.; Nestorowicz, A.; Alexander, D.J.; Webster, R.G. !$#journal Virology (1987) 158:218-227 !$#title Molecular analyses of the hemagglutinin genes of H5 !1influenza viruses: origin of a virulent turkey strain. !$#cross-references MUID:87207664; PMID:3576972 !$#accession A26184 !'##molecule_type genomic RNA !'##residues 1-566 ##label KAW !'##cross-references GB:M18451; NID:g323967; PIDN:AAA43083.1; !1PID:g323968 GENETICS !$#gene HA !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer; lipoprotein; !1thiolester bond FEATURE !$1-344 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$345-566 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$26,27,39,209,302, !$498,557 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$555,562,565 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 566 #molecular-weight 64020 #checksum 7976 SEQUENCE /// ENTRY HMIVD8 #type complete TITLE hemagglutinin precursor - influenza A virus (strain A/duck/ Ireland/113/83 [H5N8]) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 21-Jul-2000 ACCESSIONS B26184 REFERENCE A94359 !$#authors Kawaoka, Y.; Nestorowicz, A.; Alexander, D.J.; Webster, R.G. !$#journal Virology (1987) 158:218-227 !$#title Molecular analyses of the hemagglutinin genes of H5 !1influenza viruses: origin of a virulent turkey strain. !$#cross-references MUID:87207664; PMID:3576972 !$#accession B26184 !'##molecule_type genomic RNA !'##residues 1-566 ##label KAW GENETICS !$#gene HA !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer; lipoprotein; !1thiolester bond FEATURE !$1-344 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$345-566 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$26,27,39,181,209, !$302,498,557 #binding_site carbohydrate (Asn) (covalent) #status !8predicted\ !$555,562,565 #binding_site palmitate (Cys) (covalent) #status !8predicted SUMMARY #length 566 #molecular-weight 64044 #checksum 7391 SEQUENCE /// ENTRY HMIVF #type complete TITLE hemagglutinin precursor - influenza A virus ORGANISM #formal_name influenza A virus DATE 31-Jul-1980 #sequence_revision 31-Jul-1980 #text_change 15-Oct-1996 ACCESSIONS A04070 REFERENCE A04070 !$#authors Porter, A.G.; Barber, C.; Carey, N.H.; Hallewell, R.A.; !1Threlfall, G.; Emtage, J.S. !$#journal Nature (1979) 282:471-477 !$#title Complete nucleotide sequence of an influenza virus !1haemagglutinin gene from cloned DNA. !$#cross-references MUID:80054765; PMID:503226 !$#accession A04070 !'##molecule_type DNA !'##residues 1-563 ##label POR COMMENT Hemagglutinin is responsible for attaching the virus to cell !1receptors and for initiating infection. COMMENT Cleavage of hemagglutinin into two subunits, HA1 and HA2, !1usually takes place either on smooth internal membranes or !1at the plasma membrane; this step is essential for !1infectivity and probably also for pathogenicity. CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS hemagglutinin; homotrimer FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-337 #product hemagglutinin HA1 chain #status predicted !8#label HA1\ !$343-563 #product hemagglutinin HA2 chain #status predicted !8#label HA2 SUMMARY #length 563 #molecular-weight 62702 #checksum 1347 SEQUENCE /// ENTRY A45539 #type complete TITLE hemagglutinin precursor - influenza A virus (strain A/FPV/ Weybridge [H7N7]) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 24-Feb-1994 #sequence_revision 24-Feb-1994 #text_change 08-Apr-1994 ACCESSIONS A45539 REFERENCE A45539 !$#authors Klimov, A.; Prosch, S.; Schafer, J.; Bucher, D. !$#journal Arch. Virol. (1992) 122:143-161 !$#title Subtype H7 influenza viruses: comparative antigenic and !1molecular analysis of the HA-, M-, and NS-genes. !$#cross-references MUID:92109567; PMID:1530908 !$#accession A45539 !'##molecule_type genomic RNA !'##residues 1-563 ##label KLI !'##note sequence extracted from NCBI backbone (NCBIN:74239, !1NCBIP:74242) GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-342 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$343-563 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$30,46,141,249,424, !$496 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 563 #molecular-weight 62647 #checksum 1067 SEQUENCE /// ENTRY HMIVCV #type complete TITLE hemagglutinin precursor - influenza A virus (strain A/ chicken/Vic/1/85) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 16-Jul-1999 ACCESSIONS A27830 REFERENCE A94365 !$#authors Nestorowicz, A.; Kawaoka, Y.; Bean, W.J.; Webster, R.G. !$#journal Virology (1987) 160:411-418 !$#title Molecular analysis of the hemagglutinin genes of Australian !1H7N7 influenza viruses: role of passerine birds in !1maintenance or transmission? !$#cross-references MUID:88019190; PMID:3660587 !$#accession A27830 !'##molecule_type mRNA !'##residues 1-563 ##label NES !'##cross-references GB:M17735; NID:g324099; PIDN:AAA43152.1; !1PID:g324100 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-342 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$343-563 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$30,46,249,424,496 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 563 #molecular-weight 62726 #checksum 2442 SEQUENCE /// ENTRY HMIVSV #type complete TITLE hemagglutinin precursor - influenza A virus (strain A/ starling/Vic/5156/85) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 16-Jul-1999 ACCESSIONS B27830 REFERENCE A94365 !$#authors Nestorowicz, A.; Kawaoka, Y.; Bean, W.J.; Webster, R.G. !$#journal Virology (1987) 160:411-418 !$#title Molecular analysis of the hemagglutinin genes of Australian !1H7N7 influenza viruses: role of passerine birds in !1maintenance or transmission? !$#cross-references MUID:88019190; PMID:3660587 !$#accession B27830 !'##molecule_type mRNA !'##residues 1-563 ##label NES !'##cross-references GB:M17736; NID:g324101; PIDN:AAA43154.1; !1PID:g324102 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-342 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$343-563 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$30,46,249,424,496 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 563 #molecular-weight 62730 #checksum 3720 SEQUENCE /// ENTRY HMIVT7 #type complete TITLE hemagglutinin precursor - influenza A virus (strain A/ Turkey/Oregon/71 [H7N3]) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 12-Apr-1996 ACCESSIONS A34772 REFERENCE A34772 !$#authors Orlich, M.; Khatchikian, D.; Teigler, A.; Rott, R. !$#journal Virology (1990) 176:531-538 !$#title Structural variation occurring in the hemagglutinin of !1influenza virus A/Turkey/Oregon/71 during adaptation to !1different cell types. !$#cross-references MUID:90266469; PMID:2345964 !$#accession A34772 !'##molecule_type mRNA !'##residues 1-560 ##label ORL GENETICS !$#gene HA !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer; transmembrane !1protein FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-339 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$340-560 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$524-549 #domain transmembrane #status predicted #label TMN\ !$30,46,249,421,493 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 560 #molecular-weight 62108 #checksum 6895 SEQUENCE /// ENTRY HMIV49 #type complete TITLE hemagglutinin precursor - influenza A virus (strain A/chick/ Germany/N/49 [H10N7]) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jul-1999 ACCESSIONS A29244 REFERENCE A94382 !$#authors Feldmann, H.; Kretzschmar, E.; Klingeborn, B.; Rott, R.; !1Klenk, H.D.; Garten, W. !$#journal Virology (1988) 165:428-437 !$#title The structure of serotype H10 hemagglutinin of influenza A !1virus: comparison of an apathogenic avian and a mammalian !1strain pathogenic for mink. !$#cross-references MUID:88306234; PMID:3407149 !$#accession A29244 !'##molecule_type genomic RNA !'##residues 1-561 ##label FEL !'##cross-references GB:M21646; NID:g324037; PIDN:AAA79774.1; !1PID:g324038 GENETICS !$#gene HA !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer; transmembrane !1protein FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-339 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$341-561 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$525-550 #domain transmembrane #status predicted #label TMN\ !$29,45,252,306,422, !$494 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 561 #molecular-weight 62107 #checksum 7314 SEQUENCE /// ENTRY HMIV84 #type complete TITLE hemagglutinin precursor - influenza A virus (strain A/mink/ Sweden/84 [H10N4]) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza A virus DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 21-Jul-2000 ACCESSIONS B29244 REFERENCE A94382 !$#authors Feldmann, H.; Kretzschmar, E.; Klingeborn, B.; Rott, R.; !1Klenk, H.D.; Garten, W. !$#journal Virology (1988) 165:428-437 !$#title The structure of serotype H10 hemagglutinin of influenza A !1virus: comparison of an apathogenic avian and a mammalian !1strain pathogenic for mink. !$#cross-references MUID:88306234; PMID:3407149 !$#accession B29244 !'##molecule_type genomic RNA !'##residues 1-561 ##label FEL GENETICS !$#gene HA !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer; transmembrane !1protein FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-339 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$341-561 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$525-550 #domain transmembrane #status predicted #label TMN\ !$29,45,252,306,422, !$494 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 561 #molecular-weight 62306 #checksum 6368 SEQUENCE /// ENTRY HMIVB #type complete TITLE hemagglutinin precursor - influenza B virus (strain B/Lee/ 40) ORGANISM #formal_name influenza B virus DATE 14-Nov-1983 #sequence_revision 03-Aug-1984 #text_change 16-Jul-1999 ACCESSIONS C93986; A04071 REFERENCE A93986 !$#authors Krystal, M.; Young, J.F.; Palese, P.; Wilson, I.A.; Skehel, !1J.J.; Wiley, D.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:1261 !$#accession C93986 !'##molecule_type genomic RNA !'##residues 1-584 ##label KRY !'##cross-references GB:K00423; NID:g325175; PIDN:AAA43716.1; !1PID:g325176 !'##note this erratum corrects Fig. 1 of reference A93960; the corrected !1amino acid sequence is not given REFERENCE A93960 !$#authors Krystal, M.; Young, J.F.; Palese, P.; Wilson, I.A.; Skehel, !1J.J.; Wiley, D.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:4527-4531 !$#title Sequential mutations in hemagglutinins of influenza B virus !1isolates: definition of antigenic domains. !$#cross-references MUID:83273654; PMID:6192436 !$#contents annotation; sequence !$#note this sequence has been revised in reference A93986 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer; transmembrane !1protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-361 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$362-584 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$557-573 #domain transmembrane #status predicted #label TMN\ !$40,74,180,318,347, !$506,532,545,577 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 584 #molecular-weight 63275 #checksum 6543 SEQUENCE /// ENTRY HMIVBJ #type complete TITLE hemagglutinin precursor - influenza B virus (strain B/ Beijing/1/87) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza B virus #note host Homo sapiens (man) DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS S10312; PQ0512 REFERENCE S10312 !$#authors Dayan, S.; Ruigrok, R.W.H.; Daniels, R.S. !$#journal Nucleic Acids Res. (1990) 18:3633 !$#title Nucleotide sequence of the HA gene of influenza B/Beijing/1/ !187. !$#cross-references MUID:90301482; PMID:2362812 !$#accession S10312 !'##molecule_type mRNA !'##residues 1-585 ##label DAY !'##cross-references GB:X53098; NID:g60748; PIDN:CAA37262.1; PID:g60749 REFERENCE JQ1901 !$#authors Rota, P.A.; Hemphill, M.L.; Whistler, T.; Regnery, H.L.; !1Kendal, A.P. !$#journal J. Gen. Virol. (1992) 73:2737-2742 !$#title Antigenic and genetic characterization of the !1haemagglutinins of recent cocirculating strains of influenza !1B virus. !$#cross-references MUID:93019032; PMID:1402807 !$#accession PQ0512 !'##molecule_type genomic RNA !'##residues 363-585 ##label ROT !'##experimental_source strain B/AA/86 GENETICS !$#gene HA !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer; transmembrane !1protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-362 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$363-585 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$558-574 #domain transmembrane #status predicted #label TMN\ !$40,74,160,181,319, !$348,507,533,546,578 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 585 #molecular-weight 63166 #checksum 5054 SEQUENCE /// ENTRY HMIVBM #type fragment TITLE hemagglutinin precursor - influenza B virus (strain B/MD/59) (fragment) ORGANISM #formal_name influenza B virus DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 07-May-1999 ACCESSIONS A93986; PQ0513; A04072 REFERENCE A93986 !$#authors Krystal, M.; Young, J.F.; Palese, P.; Wilson, I.A.; Skehel, !1J.J.; Wiley, D.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:1261 !$#accession A93986 !'##molecule_type genomic RNA !'##residues 1-574 ##label KRY !'##cross-references GB:K00424 !'##note this erratum corrects Fig. 1 of reference A93960; the corrected !1amino acid sequence is not given REFERENCE A93960 !$#authors Krystal, M.; Young, J.F.; Palese, P.; Wilson, I.A.; Skehel, !1J.J.; Wiley, D.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:4527-4531 !$#title Sequential mutations in hemagglutinins of influenza B virus !1isolates: definition of antigenic domains. !$#cross-references MUID:83273654; PMID:6192436 !$#contents annotation; sequence !$#note this sequence has been revised in reference A93986 REFERENCE JQ1901 !$#authors Rota, P.A.; Hemphill, M.L.; Whistler, T.; Regnery, H.L.; !1Kendal, A.P. !$#journal J. Gen. Virol. (1992) 73:2737-2742 !$#title Antigenic and genetic characterization of the !1haemagglutinins of recent cocirculating strains of influenza !1B virus. !$#cross-references MUID:93019032; PMID:1402807 !$#accession PQ0513 !'##molecule_type genomic RNA !'##residues 352-574 ##label ROT !'##experimental_source strain B/VI/87 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer; transmembrane !1protein FEATURE !$1-9 #domain signal sequence #status predicted #label SIG\ !$10-351 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$352-574 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$547-563 #domain transmembrane #status predicted #label TMN\ !$30,64,150,170,237, !$308,337,496,522, !$535,567 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 574 #checksum 3461 SEQUENCE /// ENTRY HMIVBH #type fragment TITLE hemagglutinin precursor - influenza B virus (strain B/HK/8/ 73) (fragment) ORGANISM #formal_name influenza B virus DATE 03-Aug-1984 #sequence_revision 03-Aug-1984 #text_change 25-Oct-1996 ACCESSIONS B93986; A04073 REFERENCE A93986 !$#authors Krystal, M.; Young, J.F.; Palese, P.; Wilson, I.A.; Skehel, !1J.J.; Wiley, D.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:1261 !$#accession B93986 !'##molecule_type genomic RNA !'##residues 1-575 ##label KRY !'##cross-references GB:K00425 !'##note this erratum corrects Fig. 1 of reference A93960; the corrected !1amino acid sequence is not given REFERENCE A93960 !$#authors Krystal, M.; Young, J.F.; Palese, P.; Wilson, I.A.; Skehel, !1J.J.; Wiley, D.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:4527-4531 !$#title Sequential mutations in hemagglutinins of influenza B virus !1isolates: definition of antigenic domains. !$#cross-references MUID:83273654; PMID:6192436 !$#contents annotation; sequence !$#note this sequence has been revised in reference A93986 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer; transmembrane !1protein FEATURE !$1-12 #domain signal sequence #status predicted #label SIG\ !$13-352 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$353-575 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$548-564 #domain transmembrane #status predicted #label TMN\ !$33,67,131,153,171, !$309,338,497,523, !$536,568 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 575 #checksum 1650 SEQUENCE /// ENTRY HMIVBS #type complete TITLE hemagglutinin precursor - influenza B virus (strain B/ Singapore/222/79) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza B virus #note host Homo sapiens (man) DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 16-Jul-1999 ACCESSIONS A04074 REFERENCE A04074 !$#authors Verhoeyen, M.; Van Rompuy, L.; Min Jou, W.; Huylebroeck, D.; !1Fiers, W. !$#journal Nucleic Acids Res. (1983) 11:4703-4712 !$#title Complete nucleotide sequence of the influenza B/Singapore/ !1222/79 virus hemagglutinin gene and comparison with the B/ !1Lee/40 hemagglutinin. !$#cross-references MUID:83272925; PMID:6348701 !$#accession A04074 !'##molecule_type genomic RNA !'##residues 1-583 ##label VER !'##cross-references GB:X00897; GB:K00038; NID:g60779; PIDN:CAA25425.1; !1PID:g60780 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer; transmembrane !1protein FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-360 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$361-583 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$40,74,160,179,246, !$317,346,505,531, !$544,576 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 583 #molecular-weight 62929 #checksum 6421 SEQUENCE /// ENTRY HMIVHO #type complete TITLE hemagglutinin precursor - influenza B virus (strain B/ Oregon/5/80) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza B virus #note host Homo sapiens (man) DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 16-Jul-1999 ACCESSIONS A04075 REFERENCE A04075 !$#authors Berton, M.T.; Naeve, C.W.; Webster, R.G. !$#journal J. Virol. (1984) 52:919-927 !$#title Antigenic structure of the influenza B virus hemagglutinin: !1nucleotide sequence analysis of antigenic variants selected !1with monoclonal antibodies. !$#cross-references MUID:85033960; PMID:6208383 !$#accession A04075 !'##molecule_type genomic RNA !'##residues 1-583 ##label BER !'##cross-references GB:K02713; NID:g325146; PIDN:AAA43702.1; !1PID:g325147 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer; transmembrane !1protein FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-360 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$361-583 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$40,74,160,179,246, !$317,346,505,531, !$544,576 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 583 #molecular-weight 62912 #checksum 5408 SEQUENCE /// ENTRY HMIVBA #type fragment TITLE hemagglutinin precursor - influenza B virus (strain B/Ann Arbor/1/86) (fragment) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza B virus DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jul-1999 ACCESSIONS A31054 REFERENCE A31054 !$#authors Bootman, J.S.; Robertson, J.S. !$#journal Virology (1988) 166:271-274 !$#title Sequence analysis of the hemagglutinin of B/Ann Arbor/1/86, !1an epidemiologically significant variant of influenza B !1virus. !$#cross-references MUID:88322883; PMID:3267231 !$#accession A31054 !'##molecule_type genomic RNA !'##residues 1-353 ##label BOO !'##cross-references GB:M21874; NID:g325124; PIDN:AAA43696.1; !1PID:g325125 GENETICS !$#gene HA !$#map_position segment 4 CLASSIFICATION #superfamily influenza virus hemagglutinin KEYWORDS glycoprotein; hemagglutinin; homotrimer FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-344 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$346-353 #product hemagglutinin HA2 (fragment) #status !8predicted #label HA2\ !$32,66,152,173,311, !$340 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 353 #checksum 7762 SEQUENCE /// ENTRY HMIVC8 #type complete TITLE hemagglutinin precursor - influenza C virus (strain C/ California/78) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza C virus DATE 20-Sep-1984 #sequence_revision 20-Sep-1984 #text_change 16-Jul-1999 ACCESSIONS A04076 REFERENCE A04076 !$#authors Nakada, S.; Creager, R.S.; Krystal, M.; Aaronson, R.P.; !1Palese, P. !$#journal J. Virol. (1984) 50:118-124 !$#title Influenza C virus hemagglutinin: comparison with influenza A !1and B virus hemagglutinins. !$#cross-references MUID:84138802; PMID:6699942 !$#accession A04076 !'##molecule_type genomic RNA !'##residues 1-654 ##label NAK !'##cross-references GB:K01689; NID:g325323; PIDN:AAA43791.1; !1PID:g325324 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza C virus hemagglutinin; Berne virus !1hemagglutinin homolog homology KEYWORDS glycoprotein; hemagglutinin; homotrimer FEATURE !$1-14 #domain signal sequence #status predicted #label SIG\ !$15-444 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$323-413 #domain Berne virus hemagglutinin homolog homology !8#label BVH\ !$446-654 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$26,61,143,188,394, !$551,602 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 654 #molecular-weight 72085 #checksum 2960 SEQUENCE /// ENTRY HMIVEA #type fragment TITLE hemagglutinin precursor - influenza C virus (strain C/Kyoto/ 41/82) (fragment) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza C virus DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 12-Apr-1996 ACCESSIONS A32665 REFERENCE A32665 !$#authors Adachi, K.; Kitame, F.; Sugawara, K.; Nishimura, H.; !1Nakamura, K. !$#journal Virology (1989) 172:125-133 !$#title Antigenic and genetic characterization of three influenza C !1strains isolated in the Kinki district of Japan in !11982-1983. !$#cross-references MUID:89370294; PMID:2773313 !$#accession A32665 !'##molecule_type genomic RNA !'##residues 1-640 ##label ADA GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza C virus hemagglutinin; Berne virus !1hemagglutinin homolog homology KEYWORDS glycoprotein; hemagglutinin; homotrimer FEATURE !$1-431 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$309-399 #domain Berne virus hemagglutinin homolog homology !8#label BVH\ !$433-640 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$12,47,130,175,380, !$537,588 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 640 #checksum 8929 SEQUENCE /// ENTRY HMIVEC #type fragment TITLE hemagglutinin precursor - influenza C virus (strain C/Hyogo/ 1/83) (fragment) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza C virus DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 12-Apr-1996 ACCESSIONS C32665 REFERENCE A32665 !$#authors Adachi, K.; Kitame, F.; Sugawara, K.; Nishimura, H.; !1Nakamura, K. !$#journal Virology (1989) 172:125-133 !$#title Antigenic and genetic characterization of three influenza C !1strains isolated in the Kinki district of Japan in !11982-1983. !$#cross-references MUID:89370294; PMID:2773313 !$#accession C32665 !'##molecule_type genomic RNA !'##residues 1-640 ##label ADA GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza C virus hemagglutinin; Berne virus !1hemagglutinin homolog homology KEYWORDS glycoprotein; hemagglutinin; homotrimer FEATURE !$1-431 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$309-399 #domain Berne virus hemagglutinin homolog homology !8#label BVH\ !$433-640 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$12,47,130,175,380, !$537,588 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 640 #checksum 9961 SEQUENCE /// ENTRY HMIVEB #type fragment TITLE hemagglutinin precursor - influenza C virus (strain C/Nara/ 82) (fragment) CONTAINS hemagglutinin HA1; hemagglutinin HA2 ORGANISM #formal_name influenza C virus DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 12-Apr-1996 ACCESSIONS B32665 REFERENCE A32665 !$#authors Adachi, K.; Kitame, F.; Sugawara, K.; Nishimura, H.; !1Nakamura, K. !$#journal Virology (1989) 172:125-133 !$#title Antigenic and genetic characterization of three influenza C !1strains isolated in the Kinki district of Japan in !11982-1983. !$#cross-references MUID:89370294; PMID:2773313 !$#accession B32665 !'##molecule_type genomic RNA !'##residues 1-640 ##label ADA GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily influenza C virus hemagglutinin; Berne virus !1hemagglutinin homolog homology KEYWORDS glycoprotein; hemagglutinin; homotrimer FEATURE !$1-431 #product hemagglutinin HA1 #status predicted #label !8HA1\ !$309-399 #domain Berne virus hemagglutinin homolog homology !8#label BVH\ !$433-640 #product hemagglutinin HA2 #status predicted #label !8HA2\ !$12,47,130,175,380, !$537,588 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 640 #checksum 9625 SEQUENCE /// ENTRY HMIHMS #type complete TITLE hemagglutinin-esterase precursor - murine hepatitis virus (strain MHV-S) ORGANISM #formal_name murine hepatitis virus, MHV DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 07-May-1999 ACCESSIONS A40476 REFERENCE A40476 !$#authors Yokomori, K.; Banner, L.R.; Lai, M.M. !$#journal Virology (1991) 183:647-657 !$#title Heterogeneity of gene expression of the !1hemagglutinin-esterase (HE) protein of murine coronaviruses. !$#cross-references MUID:91306448; PMID:1649505 !$#accession A40476 !'##status translation not shown !'##molecule_type genomic RNA !'##residues 1-430 ##label YOK !'##cross-references GB:M64316 CLASSIFICATION #superfamily influenza C virus hemagglutinin; Berne virus !1hemagglutinin homolog homology KEYWORDS glycoprotein; hemagglutinin; transmembrane protein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-430 #product hemagglutinin-esterase #status predicted !8#label HEP\ !$297-385 #domain Berne virus hemagglutinin homolog homology !8#label BVH\ !$404-420 #domain transmembrane #status predicted #label TM1\ !$91,149,193,243,306, !$313,328,357,371 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 430 #molecular-weight 48255 #checksum 8456 SEQUENCE /// ENTRY HMIHMH #type complete TITLE hemagglutinin-esterase precursor - murine hepatitis virus (strain A59) ORGANISM #formal_name murine hepatitis virus, MHV DATE 30-Sep-1990 #sequence_revision 31-Mar-1993 #text_change 23-Mar-1995 ACCESSIONS B31165 REFERENCE A31165 !$#authors Luytjes, W.; Bredenbeek, P.J.; Noten, A.F.H.; Horzinek, !1M.C.; Spaan, W.J.M. !$#journal Virology (1988) 166:415-422 !$#title Sequence of mouse hepatitis virus A59 mRNA 2: indications !1for RNA recombination between coronaviruses and influenza C !1virus. !$#cross-references MUID:89020808; PMID:2845655 !$#accession B31165 !'##molecule_type genomic RNA !'##residues 1-427 ##label LUY !'##cross-references GB:M23256 !'##note readthrough of the terminator UGA may occur between the codons !1for 14-Ile and 15-Cys CLASSIFICATION #superfamily influenza C virus hemagglutinin; Berne virus !1hemagglutinin homolog homology KEYWORDS glycoprotein; hemagglutinin; transmembrane protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-427 #product hemagglutinin-esterase #status predicted !8#label HEP\ !$296-384 #domain Berne virus hemagglutinin homolog homology !8#label BVH\ !$403-419 #domain transmembrane #status predicted #label TM1\ !$90,148,192,242,312, !$327,331,356,370 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 427 #molecular-weight 47697 #checksum 4381 SEQUENCE /// ENTRY HMIHL9 #type complete TITLE hemagglutinin-esterase precursor - bovine coronavirus ALTERNATE_NAMES E3 glycoprotein; HE glycoprotein ORGANISM #formal_name bovine coronavirus DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 19-Oct-1995 ACCESSIONS A41702; A31684 REFERENCE A41702 !$#authors Zhang, X.; Kousoulas, K.G.; Storz, J. !$#journal Virology (1991) 185:847-852 !$#title The hemagglutinin/esterase glycoprotein of bovine !1coronaviruses: sequence and functional comparisons between !1virulent and avirulent strains. !$#cross-references MUID:92074250; PMID:1962455 !$#accession A41702 !'##molecule_type genomic RNA !'##residues 1-424 ##label ZHA !'##cross-references GB:M76372 !'##experimental_source strain L9, virulent REFERENCE A31684 !$#authors Parker, M.D.; Cox, G.J.; Deregt, D.; Fitzpatrick, D.R.; !1Babiuk, L.A. !$#journal J. Gen. Virol. (1989) 70:155-164 !$#title Cloning and in vitro expression of the gene for the E3 !1haemagglutinin glycoprotein of bovine coronavirus. !$#cross-references MUID:89279187; PMID:2732684 !$#accession A31684 !'##molecule_type genomic RNA !'##residues 1-424 ##label PAR !'##experimental_source strain Quebec CLASSIFICATION #superfamily influenza C virus hemagglutinin; Berne virus !1hemagglutinin homolog homology KEYWORDS glycoprotein; hemagglutinin; transmembrane protein FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-424 #product hemagglutinin-esterase #status predicted !8#label HGE\ !$285-372 #domain Berne virus hemagglutinin homolog homology !8#label BVH\ !$392-408 #domain transmembrane #status predicted #label TM1\ !$54,89,153,236,301, !$316,358 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 424 #molecular-weight 47709 #checksum 8162 SEQUENCE /// ENTRY HMIHLY #type complete TITLE hemagglutinin-esterase precursor - bovine coronavirus (strain LY138, virulent) ORGANISM #formal_name bovine coronavirus DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 23-Mar-1995 ACCESSIONS B41702 REFERENCE A41702 !$#authors Zhang, X.; Kousoulas, K.G.; Storz, J. !$#journal Virology (1991) 185:847-852 !$#title The hemagglutinin/esterase glycoprotein of bovine !1coronaviruses: sequence and functional comparisons between !1virulent and avirulent strains. !$#cross-references MUID:92074250; PMID:1962455 !$#accession B41702 !'##molecule_type genomic RNA !'##residues 1-424 ##label ZHA !'##cross-references GB:M76374 CLASSIFICATION #superfamily influenza C virus hemagglutinin; Berne virus !1hemagglutinin homolog homology KEYWORDS glycoprotein; hemagglutinin; transmembrane protein FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-424 #product hemagglutinin-esterase #status predicted !8#label HGE\ !$285-372 #domain Berne virus hemagglutinin homolog homology !8#label BVH\ !$392-408 #domain transmembrane #status predicted #label TM1\ !$54,89,153,236,301, !$316,358 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 424 #molecular-weight 47702 #checksum 8345 SEQUENCE /// ENTRY HMIHBC #type complete TITLE hemagglutinin-esterase precursor - bovine coronavirus (strain Mebus) ALTERNATE_NAMES E3 glycoprotein; HE glycoprotein ORGANISM #formal_name bovine coronavirus DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS A34666; A43571 REFERENCE A34666 !$#authors Kienzle, T.E.; Abraham, S.; Hogue, B.G.; Brian, D.A. !$#journal J. Virol. (1990) 64:1834-1838 !$#title Structure and orientation of expressed bovine coronavirus !1hemagglutinin-esterase protein. !$#cross-references MUID:90204700; PMID:2319653 !$#accession A34666 !'##molecule_type genomic RNA !'##residues 1-424 ##label KIE !'##cross-references GB:M30612; GB:M30613; GB:M30614; GB:M31052; !1NID:g323350; PIDN:AAA66393.1; PID:g323351 CLASSIFICATION #superfamily influenza C virus hemagglutinin; Berne virus !1hemagglutinin homolog homology KEYWORDS glycoprotein; hemagglutinin; transmembrane protein FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-424 #product hemagglutinin-esterase #status predicted !8#label HES\ !$285-372 #domain Berne virus hemagglutinin homolog homology !8#label BVH\ !$396-415 #domain transmembrane #status predicted #label TMN\ !$54,89,153,236,301, !$316,358 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 424 #molecular-weight 47695 #checksum 8622 SEQUENCE /// ENTRY A43566 #type complete TITLE hemagglutinin-esterase precursor - bovine coronavirus (strain F15) ORGANISM #formal_name bovine coronavirus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 23-Mar-1995 ACCESSIONS A43566 REFERENCE A43566 !$#authors Boireau, P.; Woloszyn, N.; Cruciere, C.; Savoysky, E.; !1Laporte, J. !$#journal Adv. Exp. Med. Biol. (1990) 276:81-88 !$#title Sequence analysis of the 3' end (8740 nucleotides) of BECV !1genome; comparison with homologous MHV nucleotide sequence. !$#cross-references MUID:91353423; PMID:1715665 !$#accession A43566 !'##molecule_type genomic RNA !'##residues 1-421 ##label BOI CLASSIFICATION #superfamily influenza C virus hemagglutinin; Berne virus !1hemagglutinin homolog homology KEYWORDS glycoprotein; hemagglutinin; transmembrane protein FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-421 #product hemagglutinin-esterase #status predicted !8#label HGE\ !$285-372 #domain Berne virus hemagglutinin homolog homology !8#label BVH\ !$392-408 #domain transmembrane #status predicted #label TM1\ !$54,89,153,236,301, !$316,358 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 421 #molecular-weight 47414 #checksum 3737 SEQUENCE /// ENTRY HMIHCC #type complete TITLE hemagglutinin-esterase precursor - human coronavirus (strain OC43) ORGANISM #formal_name human coronavirus #note host Homo sapiens (man) DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 23-Mar-1995 ACCESSIONS A39450 REFERENCE A39450 !$#authors Zhang, X.; Kousoulas, K.G.; Storz, J. !$#journal Virology (1992) 186:318-323 !$#title The hemagglutinin/esterase gene of human coronavirus strain !1OC43: phylogenetic relationships to bovine and murine !1coronaviruses and influenza C virus. !$#cross-references MUID:92087477; PMID:1727608 !$#accession A39450 !'##molecule_type genomic RNA !'##residues 1-424 ##label ZHA !'##cross-references GB:M76373 CLASSIFICATION #superfamily influenza C virus hemagglutinin; Berne virus !1hemagglutinin homolog homology KEYWORDS glycoprotein; hemagglutinin; transmembrane protein FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-424 #product hemagglutinin-esterase #status predicted !8#label HGE\ !$285-372 #domain Berne virus hemagglutinin homolog homology !8#label BVH\ !$392-408 #domain transmembrane #status predicted #label TM1\ !$54,89,114,153,236, !$301,316,358 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 424 #molecular-weight 47707 #checksum 6898 SEQUENCE /// ENTRY HMWJBV #type complete TITLE hemagglutinin homolog - Berne virus ORGANISM #formal_name Berne virus DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS A38524 REFERENCE A38524 !$#authors Snijder, E.J.; den Boon, J.A.; Horzinek, M.C.; Spaan, W.J.M. !$#journal Virology (1991) 180:448-452 !$#title Comparison of the genome organization of toro- and !1coronaviruses: evidence for two nonhomologous RNA !1recombination events during Berne virus evolution. !$#cross-references MUID:91082445; PMID:1984666 !$#accession A38524 !'##molecule_type mRNA !'##residues 1-142 ##label SNI !'##cross-references GB:X52375; NID:g58772; PIDN:CAA36602.1; PID:g58773 CLASSIFICATION #superfamily Berne virus hemagglutinin homolog; Berne virus !1hemagglutinin homolog homology KEYWORDS hemagglutinin FEATURE !$6-96 #domain Berne virus hemagglutinin homolog homology !8#label BVH SUMMARY #length 142 #molecular-weight 15571 #checksum 4760 SEQUENCE /// ENTRY HNVZVV #type complete TITLE hemagglutinin precursor - vaccinia virus ORGANISM #formal_name vaccinia virus DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jul-1999 ACCESSIONS A27789 REFERENCE A27789 !$#authors Shida, H. !$#journal Virology (1986) 150:451-462 !$#title Nucleotide sequence of the vaccinia virus hemagglutinin !1gene. !$#cross-references MUID:86181588; PMID:3008418 !$#accession A27789 !'##molecule_type DNA !'##residues 1-315 ##label SHI !'##cross-references GB:M14783; GB:M14130; NID:g335633; PIDN:AAA48251.1; !1PID:g335634 CLASSIFICATION #superfamily vaccinia virus hemagglutinin; immunoglobulin !1homology KEYWORDS glycoprotein; hemagglutinin; late protein; transmembrane !1protein FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-315 #product hemagglutinin #status predicted #label HNN\ !$27-105 #domain immunoglobulin homology #label IMM\ !$280-302 #domain transmembrane #status predicted #label TMM\ !$303-315 #domain intracellular #status predicted #label INT\ !$37,69,112,161,254 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 315 #molecular-weight 34834 #checksum 6271 SEQUENCE /// ENTRY HNVZVT #type complete TITLE hemagglutinin precursor - vaccinia virus (strain Tiantan) ORGANISM #formal_name vaccinia virus DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jul-1999 ACCESSIONS JL0108 REFERENCE JL0108 !$#authors Jin, D.; Li, Z.; Jin, Q.; Yuwen, H.; Hou, Y. !$#journal J. Exp. Med. (1989) 170:571-576 !$#title Vaccinia virus hemagglutinin. A novel member of the !1immunoglobulin superfamily. !$#cross-references MUID:89328331; PMID:2754392 !$#accession JL0108 !'##molecule_type mRNA !'##residues 1-315 ##label JIN !'##cross-references GB:X15709; GB:M57773; NID:g61313; PIDN:CAA33740.1; !1PID:g61314 CLASSIFICATION #superfamily vaccinia virus hemagglutinin; immunoglobulin !1homology KEYWORDS glycoprotein; hemagglutinin; late protein; transmembrane !1protein FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-315 #product hemagglutinin #status predicted #label MAT\ !$27-105 #domain immunoglobulin homology #label IMM\ !$280-302 #domain transmembrane #status predicted #label TMM\ !$303-315 #domain intracellular #status predicted #label INT\ !$37,69,112,161,254 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 315 #molecular-weight 34772 #checksum 6808 SEQUENCE /// ENTRY HNVZ4X #type complete TITLE hemagglutinin precursor - vaccinia virus (strain Copenhagen) ALTERNATE_NAMES A56R protein ORGANISM #formal_name vaccinia virus #note host Homo sapiens (man) DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Jul-1999 ACCESSIONS D42523 REFERENCE A42501 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:517-563 !$#title Appendix to "The complete DNA sequence of vaccinia virus". !$#accession D42523 !'##molecule_type DNA !'##residues 1-315 ##label GOE !'##cross-references GB:M35027; NID:g335317; PIDN:AAA48191.1; !1PID:g335539 !'##experimental_source strain Copenhagen REFERENCE A42531 !$#authors Goebel, S.J.; Johnson, G.P.; Perkus, M.E.; Davis, S.W.; !1Winslow, J.P.; Paoletti, E. !$#journal Virology (1990) 179:247-266 !$#title The complete DNA sequence of vaccinia virus. !$#cross-references MUID:91021027; PMID:2219722 !$#contents annotation; possible protein-coding frames !$#note neither amino acid nor nucleotide sequence is given CLASSIFICATION #superfamily vaccinia virus hemagglutinin; immunoglobulin !1homology KEYWORDS glycoprotein; hemagglutinin; late protein; transmembrane !1protein FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-315 #product hemagglutinin #status predicted #label HEG\ !$27-105 #domain immunoglobulin homology #label IMM\ !$280-302 #domain transmembrane #status predicted #label TMM\ !$303-315 #domain intracellular #status predicted #label INT\ !$37,69,112,161,254 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 315 #molecular-weight 34778 #checksum 7676 SEQUENCE /// ENTRY JQ1793 #type complete TITLE hemagglutinin precursor - vaccinia virus (strain WR) ALTERNATE_NAMES SalG1R protein ORGANISM #formal_name vaccinia virus #note host Homo sapiens (man) DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jun-2000 ACCESSIONS JQ1793 REFERENCE JQ1767 !$#authors Smith, G.L.; Chan, Y.S.; Howard, S.T. !$#journal J. Gen. Virol. (1991) 72:1349-1376 !$#title Nucleotide sequence of 42kbp of vaccinia virus strain WR !1from near the right inverted terminal repeat. !$#cross-references MUID:91259063; PMID:2045793 !$#accession JQ1793 !'##molecule_type DNA !'##residues 1-314 ##label SMI !'##cross-references DDBJ:D11079; NID:g222717; PIDN:BAA01829.1; !1PID:g222744 CLASSIFICATION #superfamily vaccinia virus hemagglutinin; immunoglobulin !1homology KEYWORDS glycoprotein; hemagglutinin; late protein; transmembrane !1protein FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-314 #product hemagglutinin #status predicted #label HEG\ !$27-105 #domain immunoglobulin homology #label IMM\ !$279-301 #domain transmembrane #status predicted #label TMM\ !$37,69,112,253 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 314 #molecular-weight 34678 #checksum 6304 SEQUENCE /// ENTRY HNVZVW #type complete TITLE hemagglutinin precursor - raccoonpox virus (strain WR) ORGANISM #formal_name raccoonpox virus DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS B43381 REFERENCE A43381 !$#authors Cavallaro, K.F.; Esposito, J.J. !$#journal Virology (1992) 190:434-439 !$#title Sequences of the raccoon poxvirus hemagglutinin protein. !$#cross-references MUID:92410621; PMID:1529542 !$#accession B43381 !'##molecule_type DNA !'##residues 1-314 ##label CAV !'##cross-references GB:M93956; NID:g335637; PIDN:AAA48252.1; !1PID:g335638 CLASSIFICATION #superfamily vaccinia virus hemagglutinin; immunoglobulin !1homology KEYWORDS glycoprotein; hemagglutinin; late protein; transmembrane !1protein FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-314 #product hemagglutinin #status predicted #label HEG\ !$27-105 #domain immunoglobulin homology #label IMM\ !$280-296 #domain transmembrane #status predicted #label TMM\ !$34-103 #disulfide_bonds #status predicted\ !$37,69,112,161,253 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 314 #molecular-weight 34678 #checksum 6304 SEQUENCE /// ENTRY HNVZRA #type complete TITLE hemagglutinin precursor - raccoonpox virus ORGANISM #formal_name raccoonpox virus DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS A43381 REFERENCE A43381 !$#authors Cavallaro, K.F.; Esposito, J.J. !$#journal Virology (1992) 190:434-439 !$#title Sequences of the raccoon poxvirus hemagglutinin protein. !$#cross-references MUID:92410621; PMID:1529542 !$#accession A43381 !'##molecule_type DNA !'##residues 1-310 ##label CAV !'##cross-references GB:M94169; NID:g333625; PIDN:AAA47231.1; !1PID:g333626 CLASSIFICATION #superfamily vaccinia virus hemagglutinin; immunoglobulin !1homology KEYWORDS glycoprotein; hemagglutinin; late protein; transmembrane !1protein FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-310 #product hemagglutinin #status predicted #label MAT\ !$29-107 #domain immunoglobulin homology #label IMM\ !$277-293 #domain transmembrane #status predicted #label TMM\ !$36-105 #disulfide_bonds #status predicted\ !$39,113,133,203 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 310 #molecular-weight 34189 #checksum 6391 SEQUENCE /// ENTRY VHIV34 #type complete TITLE nucleoprotein - influenza A virus (strain A/PR/8/34) ORGANISM #formal_name influenza A virus DATE 18-Aug-1982 #sequence_revision 17-Dec-1982 #text_change 24-Feb-1995 ACCESSIONS A94327; A94590; A04077 REFERENCE A94327 !$#authors Winter, G.; Fields, S. !$#journal Virology (1981) 114:423-428 !$#title The structure of the gene encoding the nucleoprotein of !1human influenza virus A/PR/8/34. !$#cross-references MUID:82041445; PMID:7292985 !$#accession A94327 !'##molecule_type genomic RNA !'##residues 1-498 ##label WIN REFERENCE A94590 !$#authors Van Rompuy, L.; Min Jou, W.; Huylebroeck, D.; Devos, R.; !1Fiers, W. !$#submission submitted to the Atlas, June 1982 !$#accession A94590 !'##molecule_type genomic RNA !'##residues 1-246,'N',248-352,'L',354-424,'I',426-429,'N',431-498 !1##label VAN !'##experimental_source substrain HON1 GENETICS !$#map_position segment 5 CLASSIFICATION #superfamily influenza virus nucleoprotein SUMMARY #length 498 #molecular-weight 56146 #checksum 9484 SEQUENCE /// ENTRY VHIVXL #type complete TITLE nucleoprotein - influenza A virus (strain X/Leningrad/54/1 [H1N1]) ORGANISM #formal_name influenza A virus #note host Homo sapiens (man) DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS JN0394 REFERENCE JN0394 !$#authors Beklemishev, A.B.; Blinov, V.M.; Vassilenko, S.K.; Golovin, !1S.Y.; Karginov, V.A.; Mamayev, L.V.; Mikriukov, N.N.; !1Netesov, S.V.; Petrenko, V.A.; Petrov, N.A.; Frolov, I.V. !$#journal Bioorg. Khim. (1985) 11:636-640 !$#title Synthesis, cloning and sequencing of a full-length DNA copy !1of NP gene of the influensa virus A. !$#cross-references MUID:85307106; PMID:4038349 !$#accession JN0394 !'##molecule_type genomic RNA !'##residues 1-498 ##label BEK !'##cross-references GB:M38279; NID:g324691; PIDN:AAA43459.1; !1PID:g324692 !'##note the authors translated the codon GUG for residue 67 as Ala GENETICS !$#gene NP !$#map_position segment 5 CLASSIFICATION #superfamily influenza virus nucleoprotein KEYWORDS nucleoprotein; phosphoprotein FEATURE !$176,345 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 498 #molecular-weight 56168 #checksum 9407 SEQUENCE /// ENTRY VHIV68 #type complete TITLE nucleoprotein - influenza A virus (strain A/NT/60/68) ORGANISM #formal_name influenza A virus DATE 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 16-Jul-1999 ACCESSIONS A04078; F36754 REFERENCE A04078 !$#authors Huddleston, J.A.; Brownlee, G.G. !$#journal Nucleic Acids Res. (1982) 10:1029-1038 !$#title The sequence of the nucleoprotein gene of human influenza A !1virus, strain A/NT/60/68. !$#cross-references MUID:82150233; PMID:6278431 !$#accession A04078 !'##molecule_type genomic RNA !'##residues 1-498 ##label HUD !'##cross-references GB:J02137; NID:g324703; PIDN:AAA43465.1; !1PID:g324704 !'##experimental_source strain A/NT/60/68 REFERENCE A36754 !$#authors Altmueller, A.; Fitch, W.M.; Scholtissek, C. !$#journal J. Gen. Virol. (1989) 70:2111-2119 !$#title Biological and genetic evolution of the nucleoprotein gene !1of human influenza A viruses. !$#cross-references MUID:89361370; PMID:2769232 !$#accession F36754 !'##status preliminary !'##molecule_type mRNA !'##residues 1-498 ##label ALT !'##experimental_source strain A/NT/60/68 [H3N2] GENETICS !$#gene NP !$#map_position segment 5 CLASSIFICATION #superfamily influenza virus nucleoprotein SUMMARY #length 498 #molecular-weight 55953 #checksum 6530 SEQUENCE /// ENTRY VHIV61 #type complete TITLE nucleoprotein - influenza A virus (strain A/Ann Arbor/6/60 [H2N2]) ALTERNATE_NAMES NP protein ORGANISM #formal_name influenza A virus DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 08-Apr-1994 ACCESSIONS D31831 REFERENCE A31831 !$#authors Cox, N.J.; Kitame, F.; Kendal, A.P.; Maassab, H.F.; Naeve, !1C. !$#journal Virology (1988) 167:554-567 !$#title Identification of sequence changes in the cold-adapted, live !1attenuated influenza vaccine strain, A/Ann Arbor/6/60 !1(H2N2). !$#cross-references MUID:89073759; PMID:2974219 !$#accession D31831 !'##molecule_type genomic RNA !'##residues 1-498 ##label COX GENETICS !$#map_position segment 5 CLASSIFICATION #superfamily influenza virus nucleoprotein KEYWORDS nucleoprotein SUMMARY #length 498 #molecular-weight 56008 #checksum 7144 SEQUENCE /// ENTRY VHIVA7 #type complete TITLE nucleoprotein - influenza A virus (strain A/Udorn/307/72) ORGANISM #formal_name influenza A virus #note host Homo sapiens (man) DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jul-1999 ACCESSIONS B25612; G36754 REFERENCE A94345 !$#authors Buckler-White, A.J.; Murphy, B.R. !$#journal Virology (1986) 155:345-355 !$#title Nucleotide sequence analysis of the nucleoprotein gene of an !1avian and a human influenza virus strain identifies two !1classes of nucleoproteins. !$#cross-references MUID:87071656; PMID:3788059 !$#accession B25612 !'##molecule_type mRNA !'##residues 1-498 ##label BUC !'##cross-references GB:M14922; NID:g325098; PIDN:AAA43686.1; !1PID:g325099 !'##experimental_source strain A/Udorn/307/72 REFERENCE A36754 !$#authors Altmueller, A.; Fitch, W.M.; Scholtissek, C. !$#journal J. Gen. Virol. (1989) 70:2111-2119 !$#title Biological and genetic evolution of the nucleoprotein gene !1of human influenza A viruses. !$#cross-references MUID:89361370; PMID:2769232 !$#accession G36754 !'##status preliminary !'##molecule_type mRNA !'##residues 1-498 ##label ALT !'##experimental_source strain A/Udorn/307/72 [H3N2] GENETICS !$#gene NP !$#map_position segment 5 CLASSIFICATION #superfamily influenza virus nucleoprotein KEYWORDS nucleoprotein SUMMARY #length 498 #molecular-weight 56182 #checksum 7970 SEQUENCE /// ENTRY VHIVAK #type complete TITLE nucleoprotein - influenza A virus (strain A/Kiev/59/79 [H1N1]) ORGANISM #formal_name influenza A virus #note host Homo sapiens (man) DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS JN0399; S09650 REFERENCE S09650 !$#authors Beklemishev, A.B.; Blynov, V.M.; Vassilenko, S.K.; Golovin, !1S.Y.; Karginov, V.A.; Mamayev, L.V.; Netesov, S.V.; Petrov, !1N.A.; Safronov, P.F. !$#journal Bioorg. Khim. (1986) 12:369-374 !$#title Nucleotide sequence of a full-length DNA copy of the !1influenza virus A/Kiev/59/79 (H1N1) nucleoprotein gene. !$#cross-references MUID:86186950; PMID:3964309 !$#accession JN0399 !'##molecule_type genomic RNA !'##residues 1-498 ##label BEK !'##cross-references EMBL:X51972; NID:g60820; PIDN:CAA36234.1; !1PID:g60821 GENETICS !$#gene NP !$#map_position segment 5 CLASSIFICATION #superfamily influenza virus nucleoprotein KEYWORDS nucleoprotein; phosphoprotein FEATURE !$176,345 #binding_site phosphate (Ser) (covalent) #status !8predicted SUMMARY #length 498 #molecular-weight 56323 #checksum 7965 SEQUENCE /// ENTRY VHIVN5 #type complete TITLE nucleoprotein - influenza A virus (strain A/Hong Kong/5/83 [H3N2]) ALTERNATE_NAMES NP protein ORGANISM #formal_name influenza A virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS E31470; B36755 REFERENCE A31470 !$#authors Gammelin, M.; Mandler, J.; Scholtissek, C. !$#journal Virology (1989) 170:71-80 !$#title Two subtypes of nucleoproteins (NP) of influenza A viruses. !$#cross-references MUID:89243210; PMID:2718389 !$#accession E31470 !'##molecule_type genomic RNA !'##residues 1-498 ##label GAM !'##cross-references GB:M22577; GB:J04339; NID:g324245; PIDN:AAA43241.1; !1PID:g324246 REFERENCE A36754 !$#authors Altmueller, A.; Fitch, W.M.; Scholtissek, C. !$#journal J. Gen. Virol. (1989) 70:2111-2119 !$#title Biological and genetic evolution of the nucleoprotein gene !1of human influenza A viruses. !$#cross-references MUID:89361370; PMID:2769232 !$#accession B36755 !'##status preliminary !'##molecule_type genomic RNA !'##residues 1-498 ##label ALT GENETICS !$#gene NP !$#map_position segment 5 CLASSIFICATION #superfamily influenza virus nucleoprotein KEYWORDS nucleoprotein SUMMARY #length 498 #molecular-weight 56264 #checksum 7908 SEQUENCE /// ENTRY VHIV8H #type complete TITLE nucleoprotein - influenza A virus (strain A/Hong Kong/1/68 [H3N2]) ORGANISM #formal_name influenza A virus DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Jul-1999 ACCESSIONS S05502 REFERENCE S05502 !$#authors Reinhardt, U.; Mandler, J.; Scholtissek, C. !$#journal Nucleic Acids Res. (1989) 17:6721 !$#title Sequence of the nucleoprotein (NP) gene of the influenza A !1virus reassortant 81/HO, carrying the NP originally derived !1from A/Hong Kong/1/68 (H3N2). !$#cross-references MUID:89385995; PMID:2780295 !$#accession S05502 !'##molecule_type DNA !'##residues 1-498 ##label REI !'##cross-references EMBL:X15890; NID:g60477; PIDN:CAA33899.1; !1PID:g60478 GENETICS !$#gene NP !$#map_position segment 5 CLASSIFICATION #superfamily influenza virus nucleoprotein KEYWORDS nucleoprotein SUMMARY #length 498 #molecular-weight 56034 #checksum 6182 SEQUENCE /// ENTRY VHIVN7 #type complete TITLE nucleoprotein - influenza A virus (strain A/swine/Hong Kong/ 6/76 [H3N2]) ALTERNATE_NAMES NP protein ORGANISM #formal_name influenza A virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS G31470 REFERENCE A31470 !$#authors Gammelin, M.; Mandler, J.; Scholtissek, C. !$#journal Virology (1989) 170:71-80 !$#title Two subtypes of nucleoproteins (NP) of influenza A viruses. !$#cross-references MUID:89243210; PMID:2718389 !$#accession G31470 !'##molecule_type genomic RNA !'##residues 1-498 ##label GAM !'##cross-references GB:M22571; GB:J04339; NID:g325058; PIDN:AAA43668.1; !1PID:g325059 GENETICS !$#gene NP !$#map_position segment 5 CLASSIFICATION #superfamily influenza virus nucleoprotein KEYWORDS nucleoprotein SUMMARY #length 498 #molecular-weight 56114 #checksum 8452 SEQUENCE /// ENTRY VHIVX2 #type complete TITLE nucleoprotein - influenza A virus (strain A/Fort Warren/1/50 [H1N1]) ALTERNATE_NAMES NP protein ORGANISM #formal_name influenza A virus #note host Homo sapiens (man) DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jun-2000 ACCESSIONS C36754 REFERENCE A36754 !$#authors Altmueller, A.; Fitch, W.M.; Scholtissek, C. !$#journal J. Gen. Virol. (1989) 70:2111-2119 !$#title Biological and genetic evolution of the nucleoprotein gene !1of human influenza A viruses. !$#cross-references MUID:89361370; PMID:2769232 !$#accession C36754 !'##molecule_type mRNA !'##residues 1-498 ##label ALT !'##cross-references GB:D00601; NID:g221287; PIDN:BAA00477.1; !1PID:g221288 GENETICS !$#gene NP !$#map_position segment 5 CLASSIFICATION #superfamily influenza virus nucleoprotein KEYWORDS nucleoprotein SUMMARY #length 498 #molecular-weight 56067 #checksum 7652 SEQUENCE /// ENTRY VHIVX3 #type complete TITLE nucleoprotein - influenza A virus (strain A/USSR/90/77 [H1N1]) ALTERNATE_NAMES NP protein ORGANISM #formal_name influenza A virus #note host Homo sapiens (man) DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 08-Apr-1994 ACCESSIONS D36754 REFERENCE A36754 !$#authors Altmueller, A.; Fitch, W.M.; Scholtissek, C. !$#journal J. Gen. Virol. (1989) 70:2111-2119 !$#title Biological and genetic evolution of the nucleoprotein gene !1of human influenza A viruses. !$#cross-references MUID:89361370; PMID:2769232 !$#accession D36754 !'##molecule_type mRNA !'##residues 1-498 ##label ALT GENETICS !$#gene NP !$#map_position segment 5 CLASSIFICATION #superfamily influenza virus nucleoprotein KEYWORDS nucleoprotein SUMMARY #length 498 #molecular-weight 56076 #checksum 7359 SEQUENCE /// ENTRY VHIVX4 #type complete TITLE nucleoprotein - influenza A virus (strain A/Brazil/11/78 [H1N1]) ALTERNATE_NAMES NP protein ORGANISM #formal_name influenza A virus #note host Homo sapiens (man) DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 08-Apr-1994 ACCESSIONS E36754 REFERENCE A36754 !$#authors Altmueller, A.; Fitch, W.M.; Scholtissek, C. !$#journal J. Gen. Virol. (1989) 70:2111-2119 !$#title Biological and genetic evolution of the nucleoprotein gene !1of human influenza A viruses. !$#cross-references MUID:89361370; PMID:2769232 !$#accession E36754 !'##molecule_type mRNA !'##residues 1-498 ##label ALT GENETICS !$#gene NP !$#map_position segment 5 CLASSIFICATION #superfamily influenza virus nucleoprotein KEYWORDS nucleoprotein SUMMARY #length 498 #molecular-weight 56064 #checksum 7776 SEQUENCE /// ENTRY VHIVX5 #type complete TITLE nucleoprotein - influenza A virus (strain A/Texas [H3N2]) ALTERNATE_NAMES NP protein ORGANISM #formal_name influenza A virus #note host Homo sapiens (man) DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jun-2000 ACCESSIONS H36754; PQ0411; PQ0423 REFERENCE A36754 !$#authors Altmueller, A.; Fitch, W.M.; Scholtissek, C. !$#journal J. Gen. Virol. (1989) 70:2111-2119 !$#title Biological and genetic evolution of the nucleoprotein gene !1of human influenza A viruses. !$#cross-references MUID:89361370; PMID:2769232 !$#accession H36754 !'##molecule_type mRNA !'##residues 1-498 ##label ALT !'##cross-references GB:D00602; NID:g221289; PIDN:BAA00478.1; !1PID:g221290 !'##experimental_source strain A/Texas [H3N2] REFERENCE PQ0408 !$#authors Li, X.S.; Zhao, C.Y.; Gao, H.M.; Zhang, Y.Q.; Ishida, M.; !1Kanegae, Y.; Endo, A.; Nerome, R.; Omoe, K.; Nerome, K. !$#journal J. Gen. Virol. (1992) 73:1329-1337 !$#title Origin and evolutionary characteristics of antigenic !1reassortant influenza A (H1N2) viruses isolated from man in !1China. !$#cross-references MUID:92300326; PMID:1607856 !$#accession PQ0411 !'##molecule_type genomic RNA !'##residues 23-55 ##label LIA1 !'##experimental_source strain A/Hebei/24/89 [H1N2] !$#accession PQ0423 !'##molecule_type genomic RNA !'##residues 23-55 ##label LIA2 !'##experimental_source strain A/Guizhou/54/89 [H3N2] GENETICS !$#gene NP !$#map_position segment 5 CLASSIFICATION #superfamily influenza virus nucleoprotein KEYWORDS nucleoprotein SUMMARY #length 498 #molecular-weight 56211 #checksum 8132 SEQUENCE /// ENTRY VHIVX6 #type complete TITLE nucleoprotein - influenza A virus (strain A/California [H1N1]) ALTERNATE_NAMES NP protein ORGANISM #formal_name influenza A virus #note host Homo sapiens (man) DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jun-2000 ACCESSIONS A36755 REFERENCE A36754 !$#authors Altmueller, A.; Fitch, W.M.; Scholtissek, C. !$#journal J. Gen. Virol. (1989) 70:2111-2119 !$#title Biological and genetic evolution of the nucleoprotein gene !1of human influenza A viruses. !$#cross-references MUID:89361370; PMID:2769232 !$#accession A36755 !'##molecule_type mRNA !'##residues 1-498 ##label ALT !'##cross-references GB:D00600; NID:g221285; PIDN:BAA00476.1; !1PID:g221286 GENETICS !$#gene NP !$#map_position segment 5 CLASSIFICATION #superfamily influenza virus nucleoprotein KEYWORDS nucleoprotein SUMMARY #length 498 #molecular-weight 56283 #checksum 7976 SEQUENCE /// ENTRY VHIVN9 #type complete TITLE nucleoprotein - influenza A virus (strain A/swine/Iowa/1976/ 31 [H1N1]) ALTERNATE_NAMES NP protein ORGANISM #formal_name influenza A virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS I31470 REFERENCE A31470 !$#authors Gammelin, M.; Mandler, J.; Scholtissek, C. !$#journal Virology (1989) 170:71-80 !$#title Two subtypes of nucleoproteins (NP) of influenza A viruses. !$#cross-references MUID:89243210; PMID:2718389 !$#accession I31470 !'##molecule_type genomic RNA !'##residues 1-498 ##label GAM !'##cross-references GB:M22578; GB:J04339; NID:g325071; PIDN:AAA43676.1; !1PID:g325072 GENETICS !$#gene NP !$#map_position segment 5 CLASSIFICATION #superfamily influenza virus nucleoprotein KEYWORDS nucleoprotein SUMMARY #length 498 #molecular-weight 56143 #checksum 7543 SEQUENCE /// ENTRY VHIVN6 #type complete TITLE nucleoprotein - influenza A virus (strain A/swine/Germany/2/ 81 [H1N1]) ALTERNATE_NAMES NP protein ORGANISM #formal_name influenza A virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS F31470 REFERENCE A31470 !$#authors Gammelin, M.; Mandler, J.; Scholtissek, C. !$#journal Virology (1989) 170:71-80 !$#title Two subtypes of nucleoproteins (NP) of influenza A viruses. !$#cross-references MUID:89243210; PMID:2718389 !$#accession F31470 !'##molecule_type genomic RNA !'##residues 1-498 ##label GAM !'##cross-references GB:M22579; GB:J04339; NID:g325056; PIDN:AAA43667.1; !1PID:g325057 GENETICS !$#gene NP !$#map_position segment 5 CLASSIFICATION #superfamily influenza virus nucleoprotein KEYWORDS nucleoprotein SUMMARY #length 498 #molecular-weight 56170 #checksum 9199 SEQUENCE /// ENTRY VHIVN3 #type complete TITLE nucleoprotein - influenza A virus (strain A/equi/Miami/1/63 [H3N8]) ALTERNATE_NAMES NP protein ORGANISM #formal_name influenza A virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS C31470 REFERENCE A31470 !$#authors Gammelin, M.; Mandler, J.; Scholtissek, C. !$#journal Virology (1989) 170:71-80 !$#title Two subtypes of nucleoproteins (NP) of influenza A viruses. !$#cross-references MUID:89243210; PMID:2718389 !$#accession C31470 !'##molecule_type genomic RNA !'##residues 1-498 ##label GAM !'##cross-references GB:M22575; GB:J04339; NID:g324008; PIDN:AAA43106.1; !1PID:g324009 GENETICS !$#gene NP !$#map_position segment 5 CLASSIFICATION #superfamily influenza virus nucleoprotein KEYWORDS nucleoprotein SUMMARY #length 498 #molecular-weight 56186 #checksum 8904 SEQUENCE /// ENTRY VHIVN2 #type complete TITLE nucleoprotein - influenza A virus (strain A/duck/Hong Kong/ 7/75 [H3N2]) ALTERNATE_NAMES NP protein ORGANISM #formal_name influenza A virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS B31470 REFERENCE A31470 !$#authors Gammelin, M.; Mandler, J.; Scholtissek, C. !$#journal Virology (1989) 170:71-80 !$#title Two subtypes of nucleoproteins (NP) of influenza A viruses. !$#cross-references MUID:89243210; PMID:2718389 !$#accession B31470 !'##molecule_type genomic RNA !'##residues 1-498 ##label GAM !'##cross-references GB:M22573; GB:J04339; NID:g323986; PIDN:AAA43097.1; !1PID:g323987 GENETICS !$#gene NP !$#map_position segment 5 CLASSIFICATION #superfamily influenza virus nucleoprotein KEYWORDS nucleoprotein SUMMARY #length 498 #molecular-weight 56239 #checksum 8529 SEQUENCE /// ENTRY VHIVN1 #type complete TITLE nucleoprotein - influenza A virus (strain A/duck/Bavaria/2/ 77 [H1N1]) ALTERNATE_NAMES NP protein ORGANISM #formal_name influenza A virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS A31470 REFERENCE A31470 !$#authors Gammelin, M.; Mandler, J.; Scholtissek, C. !$#journal Virology (1989) 170:71-80 !$#title Two subtypes of nucleoproteins (NP) of influenza A viruses. !$#cross-references MUID:89243210; PMID:2718389 !$#accession A31470 !'##molecule_type genomic RNA !'##residues 1-498 ##label GAM !'##cross-references GB:M22574; GB:J04339; NID:g323984; PIDN:AAA43095.1; !1PID:g323985 GENETICS !$#gene NP !$#map_position segment 5 CLASSIFICATION #superfamily influenza virus nucleoprotein KEYWORDS nucleoprotein SUMMARY #length 498 #molecular-weight 56283 #checksum 8411 SEQUENCE /// ENTRY VHIVC1 #type complete TITLE nucleoprotein - influenza A virus (strain A/chicken/Germany/ "N"/49 [H10N7]) ALTERNATE_NAMES NP protein ORGANISM #formal_name influenza A virus DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS A43494 REFERENCE A43494 !$#authors Reinhardt, U.; Scholtissek, C. !$#journal Arch. Virol. (1988) 103:139-145 !$#title Comparison of the nucleoprotein genes of a chicken and a !1mink influenza A H 10 virus. !$#cross-references MUID:89104698; PMID:3214270 !$#accession A43494 !'##molecule_type genomic RNA !'##residues 1-498 ##label REI !'##cross-references GB:M24453; NID:g324716; PIDN:AAA43470.1; !1PID:g324717 GENETICS !$#gene NP !$#map_position segment 5 CLASSIFICATION #superfamily influenza virus nucleoprotein KEYWORDS nucleoprotein SUMMARY #length 498 #molecular-weight 56235 #checksum 8871 SEQUENCE /// ENTRY VHIVM1 #type complete TITLE nucleoprotein - influenza A virus (strain A/mink/Sweden/84 [H10N4]) ALTERNATE_NAMES NP protein ORGANISM #formal_name influenza A virus DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS B43494 REFERENCE A43494 !$#authors Reinhardt, U.; Scholtissek, C. !$#journal Arch. Virol. (1988) 103:139-145 !$#title Comparison of the nucleoprotein genes of a chicken and a !1mink influenza A H 10 virus. !$#cross-references MUID:89104698; PMID:3214270 !$#accession B43494 !'##molecule_type genomic RNA !'##residues 1-498 ##label REI !'##cross-references GB:M24454; NID:g324681; PIDN:AAA43454.1; !1PID:g324682 GENETICS !$#gene NP !$#map_position segment 5 CLASSIFICATION #superfamily influenza virus nucleoprotein KEYWORDS nucleoprotein SUMMARY #length 498 #molecular-weight 56242 #checksum 5751 SEQUENCE /// ENTRY A60028 #type complete TITLE nucleoprotein - influenza A virus (strain A/Shearwater/Aust/ 1/72[H6N5]) ALTERNATE_NAMES NP protein ORGANISM #formal_name influenza A virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 26-Feb-1999 ACCESSIONS A60028 REFERENCE A60028 !$#authors Harley, V.R.; Hudson, P.J.; Coupar, B.E.H.; Selleck, P.W.; !1Westbury, H.; Boyle, D.B. !$#journal Arch. Virol. (1990) 113:133-141 !$#title Vaccinia virus expression and sequence of an avian influenza !1nucleoprotein gene: potential use in diagnosis. !$#cross-references MUID:90351274; PMID:2386434 !$#accession A60028 !'##molecule_type mRNA !'##residues 1-498 ##label HAR GENETICS !$#gene NP !$#map_position segment 5 CLASSIFICATION #superfamily influenza virus nucleoprotein KEYWORDS nucleoprotein SUMMARY #length 498 #molecular-weight 56325 #checksum 7538 SEQUENCE /// ENTRY VHIVA3 #type complete TITLE nucleoprotein - influenza A virus (strain A/parrot/Ulster/73 [H7N1]) ORGANISM #formal_name influenza A virus DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 16-Jul-1999 ACCESSIONS A23347 REFERENCE A23347 !$#authors Steuler, H.; Schroder, B.; Burger, H.; Scholtissek, C. !$#journal Virus Res. (1985) 3:35-40 !$#title Sequence of the nucleoprotein gene of influenza A/parrot/ !1Ulster/73. !$#cross-references MUID:85274879; PMID:4024728 !$#accession A23347 !'##molecule_type mRNA !'##residues 1-498 ##label STE !'##cross-references GB:M22344; NID:g325011; PIDN:AAA43663.1; !1PID:g325012 !'##experimental_source strain A/parrot/Ulster/73 [H7N1] GENETICS !$#map_position segment 5 CLASSIFICATION #superfamily influenza virus nucleoprotein KEYWORDS nucleoprotein SUMMARY #length 498 #molecular-weight 56241 #checksum 8371 SEQUENCE /// ENTRY VHIVA6 #type complete TITLE nucleoprotein - influenza A virus (strain A/mallard/New York/6750/78) ORGANISM #formal_name influenza A virus DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jul-1999 ACCESSIONS A25612 REFERENCE A94345 !$#authors Buckler-White, A.J.; Murphy, B.R. !$#journal Virology (1986) 155:345-355 !$#title Nucleotide sequence analysis of the nucleoprotein gene of an !1avian and a human influenza virus strain identifies two !1classes of nucleoproteins. !$#cross-references MUID:87071656; PMID:3788059 !$#accession A25612 !'##molecule_type mRNA !'##residues 1-498 ##label BUC !'##cross-references GB:M14921; NID:g324358; PIDN:AAA43310.1; !1PID:g324359 GENETICS !$#map_position segment 5 CLASSIFICATION #superfamily influenza virus nucleoprotein KEYWORDS nucleoprotein SUMMARY #length 498 #molecular-weight 56290 #checksum 9379 SEQUENCE /// ENTRY VHIVX1 #type complete TITLE nucleoprotein - influenza A virus (strain A/FPV/Rostock/34 [H7N1]) ALTERNATE_NAMES NP protein ORGANISM #formal_name influenza A virus #note host Homo sapiens (man) DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS S07416; A36754 REFERENCE S07416 !$#authors Tomley, F.M.; Roditi, I.J. !$#journal Virus Res. (1984) 1:625-630 !$#title Nucleotide sequence of RNA segment 5, encoding the !1nucleoprotein, of influenza A/FPV/Rostock/34. !$#accession S07416 !'##molecule_type genomic RNA !'##residues 1-498 ##label TOM !'##cross-references EMBL:M21937; NID:g324028; PIDN:AAA43116.1; !1PID:g324029 REFERENCE A36754 !$#authors Altmueller, A.; Fitch, W.M.; Scholtissek, C. !$#journal J. Gen. Virol. (1989) 70:2111-2119 !$#title Biological and genetic evolution of the nucleoprotein gene !1of human influenza A viruses. !$#cross-references MUID:89361370; PMID:2769232 !$#accession A36754 !'##molecule_type mRNA !'##residues 1-498 ##label ALT !'##cross-references GB:D00599 GENETICS !$#gene NP !$#map_position segment 5 CLASSIFICATION #superfamily influenza virus nucleoprotein KEYWORDS nucleoprotein SUMMARY #length 498 #molecular-weight 56296 #checksum 846 SEQUENCE /// ENTRY VHIVN8 #type complete TITLE nucleoprotein - influenza A virus (strain A/swine/Hong Kong/ 127/82 [H3N2]) ALTERNATE_NAMES NP protein ORGANISM #formal_name influenza A virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS H31470 REFERENCE A31470 !$#authors Gammelin, M.; Mandler, J.; Scholtissek, C. !$#journal Virology (1989) 170:71-80 !$#title Two subtypes of nucleoproteins (NP) of influenza A viruses. !$#cross-references MUID:89243210; PMID:2718389 !$#accession H31470 !'##molecule_type genomic RNA !'##residues 1-498 ##label GAM !'##cross-references GB:M22570; GB:J04339; NID:g325062; PIDN:AAA43670.1; !1PID:g325063 GENETICS !$#gene NP !$#map_position segment 5 CLASSIFICATION #superfamily influenza virus nucleoprotein KEYWORDS nucleoprotein SUMMARY #length 498 #molecular-weight 56149 #checksum 6128 SEQUENCE /// ENTRY VHIVN4 #type complete TITLE nucleoprotein - influenza A virus (strain A/equi/Prague/56 [H7N7]) ALTERNATE_NAMES NP protein ORGANISM #formal_name influenza A virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS D31470 REFERENCE A31470 !$#authors Gammelin, M.; Mandler, J.; Scholtissek, C. !$#journal Virology (1989) 170:71-80 !$#title Two subtypes of nucleoproteins (NP) of influenza A viruses. !$#cross-references MUID:89243210; PMID:2718389 !$#accession D31470 !'##molecule_type genomic RNA !'##residues 1-498 ##label GAM !'##cross-references GB:M22572; GB:J04339; NID:g324012; PIDN:AAA43108.1; !1PID:g324013 GENETICS !$#gene NP !$#map_position segment 5 CLASSIFICATION #superfamily influenza virus nucleoprotein KEYWORDS nucleoprotein SUMMARY #length 498 #molecular-weight 56262 #checksum 6307 SEQUENCE /// ENTRY VHIVBC #type complete TITLE nucleoprotein - influenza B virus (strain B/Ann Arbor/1/66 [cold-adapted]) ALTERNATE_NAMES NP protein ORGANISM #formal_name influenza B virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS G28604 REFERENCE A28604 !$#authors DeBorde, D.C.; Donabedian, A.M.; Herlocher, M.L.; Naeve, !1C.W.; Maassab, H.F. !$#journal Virology (1988) 163:429-443 !$#title Sequence comparison of wild-type and cold-adapted B/Ann !1Arbor/1/66 influenza virus genes. !$#cross-references MUID:88179548; PMID:3354202 !$#accession G28604 !'##molecule_type genomic RNA !'##residues 1-560 ##label DEB !'##cross-references GB:M20173; NID:g325242; PIDN:AAA66418.1; !1PID:g325243 GENETICS !$#map_position segment 5 CLASSIFICATION #superfamily influenza virus nucleoprotein KEYWORDS nucleoprotein SUMMARY #length 560 #molecular-weight 61593 #checksum 4748 SEQUENCE /// ENTRY VHIVBW #type complete TITLE nucleoprotein - influenza B virus (strain B/Ann Arbor/1/66 [wild-type]) ALTERNATE_NAMES NP protein ORGANISM #formal_name influenza B virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS H28604 REFERENCE A28604 !$#authors DeBorde, D.C.; Donabedian, A.M.; Herlocher, M.L.; Naeve, !1C.W.; Maassab, H.F. !$#journal Virology (1988) 163:429-443 !$#title Sequence comparison of wild-type and cold-adapted B/Ann !1Arbor/1/66 influenza virus genes. !$#cross-references MUID:88179548; PMID:3354202 !$#accession H28604 !'##molecule_type genomic RNA !'##residues 1-560 ##label DEB !'##cross-references GB:M20174; NID:g325246; PIDN:AAA66419.1; !1PID:g325247 GENETICS !$#map_position segment 5 CLASSIFICATION #superfamily influenza virus nucleoprotein KEYWORDS nucleoprotein SUMMARY #length 560 #molecular-weight 61580 #checksum 6429 SEQUENCE /// ENTRY VHIVBA #type complete TITLE nucleoprotein - influenza B virus (strain B/Ann Arbor/1/86) ALTERNATE_NAMES NP protein ORGANISM #formal_name influenza B virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS A34063 REFERENCE A34063 !$#authors Rota, P.A. !$#journal Nucleic Acids Res. (1989) 17:3595 !$#title Sequence of a cDNA clone of the nucleoprotein gene of !1influenza B/Ann Arbor/1/86. !$#cross-references MUID:89263806; PMID:2726497 !$#accession A34063 !'##molecule_type mRNA !'##residues 1-560 ##label ROT !'##cross-references GB:X14217; NID:g60475; PIDN:CAA32437.1; PID:g60476 GENETICS !$#gene NP !$#map_position segment 5 CLASSIFICATION #superfamily influenza virus nucleoprotein KEYWORDS nucleoprotein SUMMARY #length 560 #molecular-weight 61664 #checksum 6641 SEQUENCE /// ENTRY VHIVC8 #type complete TITLE nucleoprotein - influenza C virus (strain California/78) ORGANISM #formal_name influenza C virus DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jul-1999 ACCESSIONS S07413 REFERENCE S07413 !$#authors Nakada, S.; Creager, R.S.; Krystal, M.; Palese, P. !$#journal Virus Res. (1984) 1:433-441 !$#title Complete nucleotide sequence of the influenza C/California/ !178 virus nucleoprotein gene. !$#cross-references MUID:85170522; PMID:6532006 !$#accession S07413 !'##molecule_type genomic RNA !'##residues 1-565 ##label NAK !'##cross-references EMBL:M17700; NID:g325337; PIDN:AAA43798.1; !1PID:g325338 GENETICS !$#map_position segment 5 CLASSIFICATION #superfamily influenza virus nucleoprotein SUMMARY #length 565 #molecular-weight 63597 #checksum 9075 SEQUENCE /// ENTRY MFIV #type complete TITLE matrix protein M1 - influenza A virus (strain A/PR/8/34) ORGANISM #formal_name influenza A virus DATE 31-Aug-1980 #sequence_revision 31-Aug-1980 #text_change 16-Jul-1999 ACCESSIONS A04079; A92982 REFERENCE A93701 !$#authors Winter, G.; Fields, S. !$#journal Nucleic Acids Res. (1980) 8:1965-1974 !$#title Cloning of influenza cDNA into M13: the sequence of the RNA !1segment encoding the A/PR/8/34 matrix protein. !$#cross-references MUID:81053857; PMID:6927841 !$#accession A04079 !'##molecule_type genomic RNA !'##residues 1-252 ##label WIN !'##cross-references GB:V01099; NID:g60788; PIDN:CAA24282.1; PID:g60789 REFERENCE A92982 !$#authors Hall, R.M.; Air, G.M. !$#journal J. Virol. (1981) 38:1-7 !$#title Variation in nucleotide sequences coding for the N-terminal !1regions of the matrix and nonstructural proteins of !1influenza A viruses. !$#cross-references MUID:81218398; PMID:7241645 !$#accession A92982 !'##molecule_type genomic RNA !'##residues 1-106 ##label HAL !'##cross-references GB:J02145 GENETICS !$#map_position segment 7 CLASSIFICATION #superfamily influenza virus matrix protein M1 KEYWORDS matrix protein SUMMARY #length 252 #molecular-weight 27893 #checksum 8191 SEQUENCE /// ENTRY MFIVC #type complete TITLE matrix protein M1 - influenza A virus (strain A/Udorn/72 [H3N2]) ORGANISM #formal_name influenza A virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 31-Dec-1993 ACCESSIONS A94326; A04079 REFERENCE A94326 !$#authors Lamb, R.A.; Lai, C.J. !$#journal Virology (1981) 112:746-751 !$#title Conservation of the influenza virus membrane protein (M-1) !1amino acid sequence and an open reading frame of RNA segment !17 encoding a second protein (M-2) in H1N1 and H3N2 strains. !$#cross-references MUID:81251059; PMID:7257189 !$#accession A94326 !'##molecule_type genomic RNA !'##residues 1-252 ##label LAM !'##cross-references GB:J02167 GENETICS !$#map_position segment 7 CLASSIFICATION #superfamily influenza virus matrix protein M1 KEYWORDS matrix protein SUMMARY #length 252 #molecular-weight 27792 #checksum 5780 SEQUENCE /// ENTRY MFIV61 #type complete TITLE matrix protein M1 - influenza A virus (strain A/Ann Arbor/6/ 60 [H2N2]) ORGANISM #formal_name influenza A virus DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS E31831; PQ0412; PQ0424 REFERENCE A31831 !$#authors Cox, N.J.; Kitame, F.; Kendal, A.P.; Maassab, H.F.; Naeve, !1C. !$#journal Virology (1988) 167:554-567 !$#title Identification of sequence changes in the cold-adapted, live !1attenuated influenza vaccine strain, A/Ann Arbor/6/60 !1(H2N2). !$#cross-references MUID:89073759; PMID:2974219 !$#accession E31831 !'##molecule_type genomic RNA !'##residues 1-252 ##label COX !'##cross-references GB:M23978; GB:J04349; GB:M23979; NID:g324264; !1PIDN:AAA43256.1; PID:g324266 REFERENCE PQ0408 !$#authors Li, X.S.; Zhao, C.Y.; Gao, H.M.; Zhang, Y.Q.; Ishida, M.; !1Kanegae, Y.; Endo, A.; Nerome, R.; Omoe, K.; Nerome, K. !$#journal J. Gen. Virol. (1992) 73:1329-1337 !$#title Origin and evolutionary characteristics of antigenic !1reassortant influenza A (H1N2) viruses isolated from man in !1China. !$#cross-references MUID:92300326; PMID:1607856 !$#accession PQ0412 !'##molecule_type genomic RNA !'##residues 23-55 ##label LIA1 !'##experimental_source strain A/Hebei/24/89 [H1N2] !$#accession PQ0424 !'##molecule_type genomic RNA !'##residues 23-55 ##label LIA2 !'##experimental_source strain A/Guizhou/54/89 [H3N2] GENETICS !$#map_position segment 7 CLASSIFICATION #superfamily influenza virus matrix protein M1 KEYWORDS alternative splicing; matrix protein SUMMARY #length 252 #molecular-weight 27869 #checksum 8443 SEQUENCE /// ENTRY B45539 #type complete TITLE matrix protein M1 - influenza A virus (strain A/chicked/ Brescia/1902 [H7N7]) ORGANISM #formal_name influenza A virus DATE 24-Feb-1994 #sequence_revision 24-Feb-1994 #text_change 24-Feb-1994 ACCESSIONS B45539 REFERENCE A45539 !$#authors Klimov, A.; Prosch, S.; Schafer, J.; Bucher, D. !$#journal Arch. Virol. (1992) 122:143-161 !$#title Subtype H7 influenza viruses: comparative antigenic and !1molecular analysis of the HA-, M-, and NS-genes. !$#cross-references MUID:92109567; PMID:1530908 !$#accession B45539 !'##molecule_type genomic RNA !'##residues 1-252 ##label KLI !'##note sequence extracted from NCBI backbone (NCBIN:74244, !1NCBIP:74245) GENETICS !$#map_position segment 7 CLASSIFICATION #superfamily influenza virus matrix protein M1 KEYWORDS alternative splicing; matrix protein SUMMARY #length 252 #molecular-weight 27906 #checksum 8748 SEQUENCE /// ENTRY MFIVWS #type complete TITLE matrix protein M1 - influenza A virus (strain A/WSN/33) ORGANISM #formal_name influenza A virus #note host Homo sapiens (man) DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jul-1999 ACCESSIONS A28608 REFERENCE A28608 !$#authors Baylor, N.W.; Li, Y.; Ye, Z.; Wagner, R.R. !$#journal Virology (1988) 163:618-621 !$#title Transient expression and sequence of the matrix (M-1) gene !1of WSN influenza A virus in a vaccinia vector. !$#cross-references MUID:88179567; PMID:3354209 !$#accession A28608 !'##molecule_type mRNA !'##residues 1-252 ##label BAY !'##cross-references GB:M19374; NID:g324407; PIDN:AAA43352.1; !1PID:g324408 GENETICS !$#gene M1 !$#map_position segment 7 CLASSIFICATION #superfamily influenza virus matrix protein M1 KEYWORDS alternative splicing; matrix protein SUMMARY #length 252 #molecular-weight 27884 #checksum 8451 SEQUENCE /// ENTRY MFIV1K #type complete TITLE matrix protein M1 - influenza A virus (strain A/Bangkok/1/79 [H3N2]) ORGANISM #formal_name influenza A virus DATE 18-Apr-1984 #sequence_revision 18-Apr-1984 #text_change 16-Jul-1999 ACCESSIONS A04080 REFERENCE A91500 !$#authors Ortin, J.; Martinez, C.; del Rio, L.; Davila, M.; !1Lopez-Galindez, C.; Villanueva, N.; Domingo, E. !$#journal Gene (1983) 23:233-239 !$#title Evolution of the nucleotide sequence of influenza virus RNA !1segment 7 during drift of the H3N2 subtype. !$#cross-references MUID:84005895; PMID:6688599 !$#accession A04080 !'##molecule_type genomic RNA !'##residues 1-252 ##label ORT !'##cross-references GB:K01140; NID:g323976; PIDN:AAA43092.1; !1PID:g323978 GENETICS !$#map_position segment 7 CLASSIFICATION #superfamily influenza virus matrix protein M1 KEYWORDS alternative splicing SUMMARY #length 252 #molecular-weight 27810 #checksum 6226 SEQUENCE /// ENTRY MFIV1F #type complete TITLE matrix protein M1 - influenza A virus ORGANISM #formal_name influenza A virus DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 16-Jul-1999 ACCESSIONS A04081 REFERENCE A92788 !$#authors McCauley, J.W.; Mahy, B.W.J.; Inglis, S.C. !$#journal J. Gen. Virol. (1982) 58:211-215 !$#title Nucleotide sequence of fowl plague virus RNA segment 7. !$#cross-references MUID:83058699; PMID:6292344 !$#accession A04081 !'##molecule_type genomic RNA !'##residues 1-252 ##label MCC !'##cross-references GB:X05905; NID:g60720; PIDN:CAA29334.1; PID:g60721 !'##note the authors translated the codon ATG for residue 203 as Asn and !1AGG for residues 210 and 217 as Ser GENETICS !$#map_position segment 7 CLASSIFICATION #superfamily influenza virus matrix protein M1 KEYWORDS alternative splicing SUMMARY #length 252 #molecular-weight 27925 #checksum 8448 SEQUENCE /// ENTRY MFIV1M #type complete TITLE matrix protein M1 - influenza A virus (strain A/mallard/New York/6750/78) ORGANISM #formal_name influenza A virus DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jul-1999 ACCESSIONS A29511 REFERENCE A93016 !$#authors Buckler-White, A.J.; Naeve, C.W.; Murphy, B.R. !$#journal J. Virol. (1986) 57:697-700 !$#title Characterization of a gene coding for M proteins which is !1involved in host range restriction of an avian influenza A !1virus in monkeys. !$#cross-references MUID:86115422; PMID:3080604 !$#accession A29511 !'##molecule_type mRNA !'##residues 1-252 ##label BUC !'##cross-references GB:M12699; NID:g324362; PIDN:AAA43313.1; !1PID:g324364 GENETICS !$#map_position segment 7 CLASSIFICATION #superfamily influenza virus matrix protein M1 KEYWORDS alternative splicing; matrix protein SUMMARY #length 252 #molecular-weight 27926 #checksum 7836 SEQUENCE /// ENTRY JN0392 #type complete TITLE matrix protein M1 - influenza A virus (strain A/USSR/90/77 [H1N1]) ORGANISM #formal_name influenza A virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS JN0392 REFERENCE JN0392 !$#authors Samokhvalov, E.I.; Kongenov, V.A.; Chizhikov, V.E.; Blinov, !1V.M.; Yuferov, V.P.; Vasilenko, S.K.; Uryvaev, L.V.; !1Zhdanov, V.M. !$#journal Bioorg. Khim. (1985) 11:1080-1085 !$#title Primary structure of segment 7 RNA influenza virus A/USSR/ !190/77 (H1N1). !$#cross-references MUID:86050769; PMID:3877509 !$#accession JN0392 !'##molecule_type genomic RNA !'##residues 1-252 ##label SAM !'##cross-references GB:X53029; NID:g59292; PIDN:CAA37200.1; PID:g59293 GENETICS !$#map_position segment 7 CLASSIFICATION #superfamily influenza virus matrix protein M1 KEYWORDS matrix protein SUMMARY #length 252 #molecular-weight 27819 #checksum 5845 SEQUENCE /// ENTRY PN0083 #type complete TITLE matrix protein M1 - influenza A virus (strain A/FPV/ Weybridge [H7N7], remantadine-sensitive) ORGANISM #formal_name influenza A virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 30-Sep-1993 ACCESSIONS PN0083 REFERENCE PN0083 !$#authors Karginov, V.A.; Blinov, V.M.; Safronov, P.F.; Mamaev, L.V.; !1Golovin, S.Y.; Netesov, S.V.; Samokhvalov, E.I.; Sharova, !1N.K.; Yuferov, V.P.; Urivaev, L.V.; Bukrinskaya, A.G. !$#journal Bioorg. Khim. (1987) 13:1638-1643 !$#title Comparative analysis of the M-gene primary structures and !1corresponding amino acid sequences of remantadine-sensitive !1and remantadine-resistant strains of the influenza virus A/ !1FPV/Weybridge (H7N7). !$#cross-references MUID:88221675; PMID:3450279 !$#accession PN0083 !'##molecule_type genomic RNA !'##residues 1-252 ##label KAR !'##cross-references GB:M38299 !'##note the authors translated the codons GCA for residue 53 as Ser, !1ATA for residue 107 as Tyr, GCC for residue 202 as Tyr, GAG !1for residue 204 as Arg, GGG for residue 220 as Gln, and CAG !1for residue 247 as Ala GENETICS !$#map_position segment 7 CLASSIFICATION #superfamily influenza virus matrix protein M1 KEYWORDS matrix protein SUMMARY #length 252 #molecular-weight 27767 #checksum 6397 SEQUENCE /// ENTRY PN0086 #type complete TITLE matrix protein M1 - influenza A virus ORGANISM #formal_name influenza A virus DATE 30-Sep-1993 #sequence_revision 22-Oct-1999 #text_change 22-Oct-1999 ACCESSIONS S07945; PN0086 REFERENCE S07429 !$#authors Markushin, S.; Ghiasi, H.; Sokolov, N.; Shilov, A.; !1Sinitsin, B.; Brown, D.; Klimov, A.; Nayak, D. !$#journal Virus Res. (1988) 10:263-272 !$#title Nucleotide sequence of RNA segment 7 and the predicted amino !1sequence of M1 and M2 proteins of FPV/Weybridge (H7N7) and !1WSN (H1N1) influenza viruses. !$#cross-references MUID:88323193; PMID:3414185 !$#accession S07945 !'##molecule_type genomic RNA !'##residues 1-252 ##label MAR !'##cross-references EMBL:M23917; NID:g324257; PIDN:AAA43251.1; !1PID:g324258 !'##experimental_source strain A/FPV/Weybridge [H7N7] REFERENCE PN0083 !$#authors Karginov, V.A.; Blinov, V.M.; Safronov, P.F.; Mamaev, L.V.; !1Golovin, S.Y.; Netesov, S.V.; Samokhvalov, E.I.; Sharova, !1N.K.; Yuferov, V.P.; Urivaev, L.V.; Bukrinskaya, A.G. !$#journal Bioorg. Khim. (1987) 13:1638-1643 !$#title Comparative analysis of the M-gene primary structures and !1corresponding amino acid sequences of remantadine-sensitive !1and remantadine-resistant strains of the influenza virus A/ !1FPV/Weybridge (H7N7). !$#cross-references MUID:88221675; PMID:3450279 !$#accession PN0086 !'##molecule_type genomic RNA !'##residues 1-27,'I',29-40,'A',42-52,'A',54-94,'R',96-100,'K',102-108, !1'LH',111-143,'L',145-157,'H',159-180,'M',182-211,'IG', !1214-252 ##label KAR !'##cross-references GB:M38299 !'##experimental_source strain A/FPV/Weybridge [H7N7] !1remantadine-resistant !'##note the authors translated the codons GCA for residue 53 as Ser, !1ATA for residue 107 as Tyr, GCC for residue 202 as Tyr, GAG !1for residue 204 as Arg, GGG for residue 220 as Gln, and CAG !1for residue 247 as Ala GENETICS !$#map_position segment 7 CLASSIFICATION #superfamily influenza virus matrix protein M1 KEYWORDS alternative splicing; matrix protein SUMMARY #length 252 #molecular-weight 27904 #checksum 239 SEQUENCE /// ENTRY MFIV1 #type complete TITLE matrix protein M1 - influenza B virus (strain B/Lee/40) ORGANISM #formal_name influenza B virus DATE 05-Apr-1983 #sequence_revision 05-Apr-1983 #text_change 16-Jul-1999 ACCESSIONS A04082 REFERENCE A94328 !$#authors Briedis, D.J.; Lamb, R.A.; Choppin, P.W. !$#journal Virology (1982) 116:581-588 !$#title Sequence of RNA segment 7 of the influenza B virus genome: !1partial amino acid homology between the membrane proteins !1(M-1) of influenza A and B viruses and conservation of a !1second open reading frame. !$#cross-references MUID:82154757; PMID:6278729 !$#accession A04082 !'##molecule_type genomic RNA !'##residues 1-248 ##label BRI !'##cross-references GB:J02094; NID:g325201; PIDN:AAA43726.1; !1PID:g325202 GENETICS !$#map_position segment 7 CLASSIFICATION #superfamily influenza virus matrix protein M1 SUMMARY #length 248 #molecular-weight 27554 #checksum 2559 SEQUENCE /// ENTRY MFIVB1 #type complete TITLE matrix protein M1 - influenza B virus (strain B/Singapore/ 222/79) ORGANISM #formal_name influenza B virus #note host Homo sapiens (man) DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jul-1999 ACCESSIONS A25619 REFERENCE A94351 !$#authors Hiebert, S.W.; Williams, M.A.; Lamb, R.A. !$#journal Virology (1986) 155:747-751 !$#title Nucleotide sequence of RNA segment 7 of influenza B/ !1Singapore/222/79: maintenance of a second large open reading !1frame. !$#cross-references MUID:87071690; PMID:3788064 !$#accession A25619 !'##molecule_type mRNA !'##residues 1-248 ##label HIE !'##cross-references GB:M14909; GB:D00052; GB:N00052; NID:g325195; !1PIDN:AAA67100.1; PID:g325196 GENETICS !$#map_position segment 7 CLASSIFICATION #superfamily influenza virus matrix protein M1 KEYWORDS matrix protein SUMMARY #length 248 #molecular-weight 27474 #checksum 2871 SEQUENCE /// ENTRY MFIVBW #type complete TITLE matrix protein M1 - influenza B virus (strain B/Ann Arbor/1/ 66 [wild-type]) ORGANISM #formal_name influenza B virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS C30064 REFERENCE A28604 !$#authors DeBorde, D.C.; Donabedian, A.M.; Herlocher, M.L.; Naeve, !1C.W.; Maassab, H.F. !$#journal Virology (1988) 163:429-443 !$#title Sequence comparison of wild-type and cold-adapted B/Ann !1Arbor/1/66 influenza virus genes. !$#cross-references MUID:88179548; PMID:3354202 !$#accession C30064 !'##molecule_type genomic RNA !'##residues 1-248 ##label DEB !'##cross-references GB:M20176; NID:g325197; PIDN:AAA66416.1; !1PID:g325198 GENETICS !$#map_position segment 7 CLASSIFICATION #superfamily influenza virus matrix protein M1 KEYWORDS matrix protein SUMMARY #length 248 #molecular-weight 27415 #checksum 2829 SEQUENCE /// ENTRY MFIVBC #type complete TITLE matrix protein M1 - influenza B virus (strain B/Ann Arbor/1/ 66 [cold-adapted]) ORGANISM #formal_name influenza B virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS A30064 REFERENCE A28604 !$#authors DeBorde, D.C.; Donabedian, A.M.; Herlocher, M.L.; Naeve, !1C.W.; Maassab, H.F. !$#journal Virology (1988) 163:429-443 !$#title Sequence comparison of wild-type and cold-adapted B/Ann !1Arbor/1/66 influenza virus genes. !$#cross-references MUID:88179548; PMID:3354202 !$#accession A30064 !'##molecule_type genomic RNA !'##residues 1-248 ##label DEB !'##cross-references GB:M20175; NID:g325193; PIDN:AAA66414.1; !1PID:g325194 GENETICS !$#map_position segment 7 CLASSIFICATION #superfamily influenza virus matrix protein M1 KEYWORDS matrix protein SUMMARY #length 248 #molecular-weight 27374 #checksum 3342 SEQUENCE /// ENTRY MFIVCJ #type complete TITLE matrix protein M1 - influenza C virus (strain C/JJ/50) ORGANISM #formal_name influenza C virus DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jul-1999 ACCESSIONS A28878 REFERENCE A93036 !$#authors Yamashita, M.; Krystal, M.; Palese, P. !$#journal J. Virol. (1988) 62:3348-3355 !$#title Evidence that the matrix protein of influenza C virus is !1coded for by a spliced mRNA. !$#cross-references MUID:88300888; PMID:3404579 !$#accession A28878 !'##molecule_type mRNA !'##residues 1-242 ##label YAM !'##cross-references GB:M22038; NID:g325303; PIDN:AAA43781.1; !1PID:g325304 GENETICS !$#gene M !$#map_position segment 6 !$#introns 243/2 CLASSIFICATION #superfamily influenza C virus matrix protein M1 KEYWORDS matrix protein SUMMARY #length 242 #molecular-weight 26967 #checksum 7475 SEQUENCE /// ENTRY MMIV2 #type complete TITLE matrix protein M2 - influenza A virus ORGANISM #formal_name influenza A virus DATE 02-Apr-1982 #sequence_revision 02-Apr-1982 #text_change 16-Jul-1999 ACCESSIONS A93879; B94326; S04055; S04059; A04083 REFERENCE A93879 !$#authors Lamb, R.A.; Lai, C.J.; Choppin, P.W. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:4170-4174 !$#title Sequences of mRNAs derived from genome RNA segment 7 of !1influenza virus: colinear and interrupted mRNAs code for !1overlapping proteins. !$#cross-references MUID:82037801; PMID:6945577 !$#accession A93879 !'##molecule_type mRNA !'##residues 1-97 ##label LAM !'##cross-references GB:J02167; NID:g324335; PIDN:AAA43303.1; !1PID:g324336 !'##experimental_source strain A/Udorn/72 [H3N2] REFERENCE A94326 !$#authors Lamb, R.A.; Lai, C.J. !$#journal Virology (1981) 112:746-751 !$#title Conservation of the influenza virus membrane protein (M-1) !1amino acid sequence and an open reading frame of RNA segment !17 encoding a second protein (M-2) in H1N1 and H3N2 strains. !$#cross-references MUID:81251059; PMID:7257189 !$#accession B94326 !'##molecule_type genomic RNA !'##residues 1,'IF',4,'KICR',10-97 ##label LA2 !'##experimental_source strain A/Udorn/72 [H3N2] REFERENCE S04050 !$#authors Zebedee, S.L.; Lamb, R.A. !$#journal Nucleic Acids Res. (1989) 17:2870 !$#title Nucleotide sequences of influenza A virus RNA segment 7: a !1comparison of five isolates. !$#cross-references MUID:89240054; PMID:2701939 !$#accession S04055 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type genomic RNA !'##residues 1-97 ##label ZEB1 !'##cross-references EMBL:X08090; NID:g60463; PIDN:CAA30887.1; !1PID:g60465 !'##experimental_source strain Port Chalmers/1/73 mouse-adapted !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1988 !$#accession S04059 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type genomic RNA !'##residues 1-97 ##label ZEB2 !'##cross-references EMBL:X08092; NID:g60469; PIDN:CAA30891.1; !1PID:g60471 !'##experimental_source strain Port Chalmers/1/73 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1988 GENETICS !$#map_position segment 7 !$#introns 9/2 CLASSIFICATION #superfamily influenza virus matrix protein M2 KEYWORDS alternative splicing; transmembrane protein SUMMARY #length 97 #molecular-weight 11186 #checksum 5576 SEQUENCE /// ENTRY MFIV62 #type complete TITLE matrix protein M2 - influenza A virus (strain A/Ann Arbor/6/ 60 [H2N2]) ORGANISM #formal_name influenza A virus DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS F31831 REFERENCE A31831 !$#authors Cox, N.J.; Kitame, F.; Kendal, A.P.; Maassab, H.F.; Naeve, !1C. !$#journal Virology (1988) 167:554-567 !$#title Identification of sequence changes in the cold-adapted, live !1attenuated influenza vaccine strain, A/Ann Arbor/6/60 !1(H2N2). !$#cross-references MUID:89073759; PMID:2974219 !$#accession F31831 !'##molecule_type genomic RNA !'##residues 1-97 ##label COX !'##cross-references GB:M23978; GB:J04349; GB:M23979; NID:g324264; !1PIDN:AAA43255.1; PID:g324265 GENETICS !$#map_position segment 7 !$#introns 9/2 CLASSIFICATION #superfamily influenza virus matrix protein M2 KEYWORDS alternative splicing; matrix protein; transmembrane protein SUMMARY #length 97 #molecular-weight 11166 #checksum 5462 SEQUENCE /// ENTRY JN0393 #type complete TITLE matrix protein M2 - influenza A virus (strain A/USSR/90/77 [H1N1]) ORGANISM #formal_name influenza A virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jun-2000 ACCESSIONS JN0393 REFERENCE JN0392 !$#authors Samokhvalov, E.I.; Kongenov, V.A.; Chizhikov, V.E.; Blinov, !1V.M.; Yuferov, V.P.; Vasilenko, S.K.; Uryvaev, L.V.; !1Zhdanov, V.M. !$#journal Bioorg. Khim. (1985) 11:1080-1085 !$#title Primary structure of segment 7 RNA influenza virus A/USSR/ !190/77 (H1N1). !$#cross-references MUID:86050769; PMID:3877509 !$#accession JN0393 !'##molecule_type genomic RNA !'##residues 1-97 ##label SAM !'##cross-references GB:X53029; NID:g59292; PIDN:CAB38716.1; !1PID:g4490386 GENETICS !$#map_position segment 7 !$#introns 9/2 CLASSIFICATION #superfamily influenza virus matrix protein M2 KEYWORDS alternative splicing; matrix protein; transmembrane protein SUMMARY #length 97 #molecular-weight 11205 #checksum 5931 SEQUENCE /// ENTRY MFIV2K #type complete TITLE matrix protein M2 - influenza A virus (strain A/Bangkok/1/79 [H3N2]) ORGANISM #formal_name influenza A virus DATE 18-Apr-1984 #sequence_revision 18-Apr-1984 #text_change 16-Feb-1997 ACCESSIONS A04084 REFERENCE A91500 !$#authors Ortin, J.; Martinez, C.; del Rio, L.; Davila, M.; !1Lopez-Galindez, C.; Villanueva, N.; Domingo, E. !$#journal Gene (1983) 23:233-239 !$#title Evolution of the nucleotide sequence of influenza virus RNA !1segment 7 during drift of the H3N2 subtype. !$#cross-references MUID:84005895; PMID:6688599 !$#accession A04084 !'##molecule_type genomic RNA !'##residues 1-96 ##label ORT GENETICS !$#map_position segment 7 CLASSIFICATION #superfamily influenza virus matrix protein M2 KEYWORDS alternative splicing; transmembrane protein SUMMARY #length 96 #molecular-weight 11213 #checksum 2342 SEQUENCE /// ENTRY MFIVPR #type complete TITLE matrix protein M2 - influenza A virus (strain A/PR/8/34) ORGANISM #formal_name influenza A virus DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jul-1999 ACCESSIONS B04079 REFERENCE A93701 !$#authors Winter, G.; Fields, S. !$#journal Nucleic Acids Res. (1980) 8:1965-1974 !$#title Cloning of influenza cDNA into M13: the sequence of the RNA !1segment encoding the A/PR/8/34 matrix protein. !$#cross-references MUID:81053857; PMID:6927841 !$#accession B04079 !'##molecule_type genomic RNA !'##residues 1-96 ##label WIN !'##cross-references GB:V01099; GB:J02145; NID:g60788; PIDN:CAA24283.1; !1PID:g60790 GENETICS !$#map_position segment 7 CLASSIFICATION #superfamily influenza virus matrix protein M2 KEYWORDS alternative splicing; matrix protein; transmembrane protein SUMMARY #length 96 #molecular-weight 11046 #checksum 2730 SEQUENCE /// ENTRY MFIV2M #type complete TITLE matrix protein M2 - influenza A virus (strain A/mallard/New York/6750/78) ORGANISM #formal_name influenza A virus DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jul-1999 ACCESSIONS B29511 REFERENCE A93016 !$#authors Buckler-White, A.J.; Naeve, C.W.; Murphy, B.R. !$#journal J. Virol. (1986) 57:697-700 !$#title Characterization of a gene coding for M proteins which is !1involved in host range restriction of an avian influenza A !1virus in monkeys. !$#cross-references MUID:86115422; PMID:3080604 !$#accession B29511 !'##molecule_type mRNA !'##residues 1-97 ##label BUC !'##cross-references GB:M12699; NID:g324362; PIDN:AAA43312.1; !1PID:g324363 GENETICS !$#map_position segment 7 CLASSIFICATION #superfamily influenza virus matrix protein M2 KEYWORDS alternative splicing; matrix protein; transmembrane protein SUMMARY #length 97 #molecular-weight 11158 #checksum 7757 SEQUENCE /// ENTRY PN0084 #type complete TITLE matrix protein M2 - influenza A virus (strain A/FPV/ Weybridge [H7N7], remantadine-sensitive) ORGANISM #formal_name influenza A virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Feb-1997 ACCESSIONS PN0084 REFERENCE PN0083 !$#authors Karginov, V.A.; Blinov, V.M.; Safronov, P.F.; Mamaev, L.V.; !1Golovin, S.Y.; Netesov, S.V.; Samokhvalov, E.I.; Sharova, !1N.K.; Yuferov, V.P.; Urivaev, L.V.; Bukrinskaya, A.G. !$#journal Bioorg. Khim. (1987) 13:1638-1643 !$#title Comparative analysis of the M-gene primary structures and !1corresponding amino acid sequences of remantadine-sensitive !1and remantadine-resistant strains of the influenza virus A/ !1FPV/Weybridge (H7N7). !$#cross-references MUID:88221675; PMID:3450279 !$#accession PN0084 !'##molecule_type genomic RNA !'##residues 1-97 ##label KAR !'##cross-references GB:M38299 GENETICS !$#map_position segment 7 !$#introns 9/3 CLASSIFICATION #superfamily influenza virus matrix protein M2 KEYWORDS alternative splicing; matrix protein; transmembrane protein SUMMARY #length 97 #molecular-weight 11212 #checksum 7218 SEQUENCE /// ENTRY PN0087 #type complete TITLE matrix protein M2 - influenza A virus ORGANISM #formal_name influenza A virus DATE 30-Sep-1993 #sequence_revision 22-Oct-1999 #text_change 22-Oct-1999 ACCESSIONS S07946; PN0087 REFERENCE S07429 !$#authors Markushin, S.; Ghiasi, H.; Sokolov, N.; Shilov, A.; !1Sinitsin, B.; Brown, D.; Klimov, A.; Nayak, D. !$#journal Virus Res. (1988) 10:263-272 !$#title Nucleotide sequence of RNA segment 7 and the predicted amino !1sequence of M1 and M2 proteins of FPV/Weybridge (H7N7) and !1WSN (H1N1) influenza viruses. !$#cross-references MUID:88323193; PMID:3414185 !$#accession S07946 !'##molecule_type genomic RNA !'##residues 1-97 ##label MAR !'##cross-references EMBL:M23921; NID:g324291; PIDN:AAA43273.1; !1PID:g324292 !'##experimental_source strain A/FPV/Weybridge [H7N7] REFERENCE PN0083 !$#authors Karginov, V.A.; Blinov, V.M.; Safronov, P.F.; Mamaev, L.V.; !1Golovin, S.Y.; Netesov, S.V.; Samokhvalov, E.I.; Sharova, !1N.K.; Yuferov, V.P.; Urivaev, L.V.; Bukrinskaya, A.G. !$#journal Bioorg. Khim. (1987) 13:1638-1643 !$#title Comparative analysis of the M-gene primary structures and !1corresponding amino acid sequences of remantadine-sensitive !1and remantadine-resistant strains of the influenza virus A/ !1FPV/Weybridge (H7N7). !$#cross-references MUID:88221675; PMID:3450279 !$#accession PN0087 !'##molecule_type genomic RNA !'##residues 1-30,'N',32-54,'F',56-69,'E',71-97 ##label KAR !'##cross-references GB:M38299 !'##experimental_source strain A/FPV/Weybridge [H7N7] !1remantadine-resistant GENETICS !$#map_position segment 7 !$#introns 9/3 CLASSIFICATION #superfamily influenza virus matrix protein M2 KEYWORDS alternative splicing; matrix protein; transmembrane protein SUMMARY #length 97 #molecular-weight 11177 #checksum 7626 SEQUENCE /// ENTRY C45539 #type complete TITLE matrix protein M2 - influenza A virus (strain A/chicken/ Brescia/1902 [H7N7]) ORGANISM #formal_name influenza A virus DATE 24-Feb-1994 #sequence_revision 24-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS C45539 REFERENCE A45539 !$#authors Klimov, A.; Prosch, S.; Schafer, J.; Bucher, D. !$#journal Arch. Virol. (1992) 122:143-161 !$#title Subtype H7 influenza viruses: comparative antigenic and !1molecular analysis of the HA-, M-, and NS-genes. !$#cross-references MUID:92109567; PMID:1530908 !$#accession C45539 !'##molecule_type genomic RNA !'##residues 1-97 ##label KLI !'##cross-references GB:L37795; NID:g577464; PIDN:AAA56805.1; !1PID:g577466 !'##note sequence extracted from NCBI backbone (NCBIN:74244, !1NCBIP:74248) GENETICS !$#map_position segment 7 CLASSIFICATION #superfamily influenza virus matrix protein M2 KEYWORDS alternative splicing; matrix protein; transmembrane protein SUMMARY #length 97 #molecular-weight 11213 #checksum 7758 SEQUENCE /// ENTRY MFIV2F #type complete TITLE matrix protein M2 - influenza A virus ORGANISM #formal_name influenza A virus DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 16-Feb-1997 ACCESSIONS A04085 REFERENCE A92788 !$#authors McCauley, J.W.; Mahy, B.W.J.; Inglis, S.C. !$#journal J. Gen. Virol. (1982) 58:211-215 !$#title Nucleotide sequence of fowl plague virus RNA segment 7. !$#cross-references MUID:83058699; PMID:6292344 !$#accession A04085 !'##molecule_type genomic RNA !'##residues 1-96 ##label MCC !'##note the authors translated the codon CAC for residue 36 as Gln and !1GAA for residue 74 as Cys GENETICS !$#map_position segment 7 CLASSIFICATION #superfamily influenza virus matrix protein M2 KEYWORDS alternative splicing; transmembrane protein SUMMARY #length 96 #molecular-weight 11227 #checksum 4382 SEQUENCE /// ENTRY MFIV2 #type complete TITLE matrix protein M2 - influenza B virus (strain B/Lee/40) ORGANISM #formal_name influenza B virus DATE 05-Apr-1983 #sequence_revision 05-Apr-1983 #text_change 30-Sep-1993 ACCESSIONS A04086 REFERENCE A94328 !$#authors Briedis, D.J.; Lamb, R.A.; Choppin, P.W. !$#journal Virology (1982) 116:581-588 !$#title Sequence of RNA segment 7 of the influenza B virus genome: !1partial amino acid homology between the membrane proteins !1(M-1) of influenza A and B viruses and conservation of a !1second open reading frame. !$#cross-references MUID:82154757; PMID:6278729 !$#accession A04086 !'##molecule_type genomic RNA !'##residues 1-195 ##label BRI GENETICS !$#map_position segment 7 CLASSIFICATION #superfamily influenza virus matrix protein M2 SUMMARY #length 195 #molecular-weight 22578 #checksum 139 SEQUENCE /// ENTRY MFIVB2 #type complete TITLE matrix protein M2 - influenza B virus (strain B/Singapore/ 222/79) ORGANISM #formal_name influenza B virus DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 08-Apr-1994 ACCESSIONS B25619 REFERENCE A94351 !$#authors Hiebert, S.W.; Williams, M.A.; Lamb, R.A. !$#journal Virology (1986) 155:747-751 !$#title Nucleotide sequence of RNA segment 7 of influenza B/ !1Singapore/222/79: maintenance of a second large open reading !1frame. !$#cross-references MUID:87071690; PMID:3788064 !$#accession B25619 !'##molecule_type mRNA !'##residues 1-195 ##label HIE !'##note the authors translated the codon CAT for residue 195 as Gln COMMENT The RNA sequence was obtained from GenBank, release 52.0. GENETICS !$#map_position segment 7 CLASSIFICATION #superfamily influenza virus matrix protein M2 KEYWORDS matrix protein SUMMARY #length 195 #molecular-weight 22273 #checksum 7377 SEQUENCE /// ENTRY MFIV2C #type complete TITLE matrix protein M2 - influenza B virus (strain B/Ann Arbor/1/ 66 [cold-adapted]) ORGANISM #formal_name influenza B virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 08-Apr-1994 ACCESSIONS B30064 REFERENCE A28604 !$#authors DeBorde, D.C.; Donabedian, A.M.; Herlocher, M.L.; Naeve, !1C.W.; Maassab, H.F. !$#journal Virology (1988) 163:429-443 !$#title Sequence comparison of wild-type and cold-adapted B/Ann !1Arbor/1/66 influenza virus genes. !$#cross-references MUID:88179548; PMID:3354202 !$#accession B30064 !'##molecule_type genomic RNA !'##residues 1-195 ##label DEB COMMENT The RNA sequence was obtained from GenBank, release 58.0. GENETICS !$#map_position segment 7 CLASSIFICATION #superfamily influenza virus matrix protein M2 KEYWORDS matrix protein SUMMARY #length 195 #molecular-weight 22303 #checksum 7186 SEQUENCE /// ENTRY MFIV2W #type complete TITLE matrix protein M2 - influenza B virus (strain B/Ann Arbor/1/ 66 [wild-type]) ORGANISM #formal_name influenza B virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 08-Apr-1994 ACCESSIONS D30064 REFERENCE A28604 !$#authors DeBorde, D.C.; Donabedian, A.M.; Herlocher, M.L.; Naeve, !1C.W.; Maassab, H.F. !$#journal Virology (1988) 163:429-443 !$#title Sequence comparison of wild-type and cold-adapted B/Ann !1Arbor/1/66 influenza virus genes. !$#cross-references MUID:88179548; PMID:3354202 !$#accession D30064 !'##molecule_type genomic RNA !'##residues 1-195 ##label DEB COMMENT The RNA sequence was obtained from GenBank, release 58.0. GENETICS !$#map_position segment 7 CLASSIFICATION #superfamily influenza virus matrix protein M2 KEYWORDS matrix protein SUMMARY #length 195 #molecular-weight 22363 #checksum 7668 SEQUENCE /// ENTRY MFIV2J #type fragment TITLE matrix protein M2 - influenza C virus (strain C/JJ/50) (fragment) ORGANISM #formal_name influenza C virus DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 21-Nov-1997 ACCESSIONS B28878 REFERENCE A93036 !$#authors Yamashita, M.; Krystal, M.; Palese, P. !$#journal J. Virol. (1988) 62:3348-3355 !$#title Evidence that the matrix protein of influenza C virus is !1coded for by a spliced mRNA. !$#cross-references MUID:88300888; PMID:3404579 !$#accession B28878 !'##molecule_type mRNA !'##residues 1-132 ##label YAM !'##cross-references GB:M22038; NID:g325303 !'##note this ORF is not annotated in GenBank entry FLCCJJM GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily influenza C virus matrix protein M2 KEYWORDS matrix protein SUMMARY #length 132 #checksum 1563 SEQUENCE /// ENTRY PN0085 #type complete TITLE matrix protein M3 - influenza A virus (strain A/FPV/ Weybridge [H7N7], remantadine-sensitive) ORGANISM #formal_name influenza A virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 30-Sep-1993 ACCESSIONS PN0085 REFERENCE PN0083 !$#authors Karginov, V.A.; Blinov, V.M.; Safronov, P.F.; Mamaev, L.V.; !1Golovin, S.Y.; Netesov, S.V.; Samokhvalov, E.I.; Sharova, !1N.K.; Yuferov, V.P.; Urivaev, L.V.; Bukrinskaya, A.G. !$#journal Bioorg. Khim. (1987) 13:1638-1643 !$#title Comparative analysis of the M-gene primary structures and !1corresponding amino acid sequences of remantadine-sensitive !1and remantadine-resistant strains of the influenza virus A/ !1FPV/Weybridge (H7N7). !$#cross-references MUID:88221675; PMID:3450279 !$#accession PN0085 !'##molecule_type genomic RNA !'##residues 1-68 ##label KAR !'##cross-references GB:M38299 !'##note the authors translated the codon GTC for residue 4 as Tyr GENETICS !$#map_position segment 7 CLASSIFICATION #superfamily influenza A virus matrix protein M3 KEYWORDS matrix protein SUMMARY #length 68 #molecular-weight 8118 #checksum 3007 SEQUENCE /// ENTRY PN0088 #type complete TITLE matrix protein M3 - influenza A virus (strain A/FPV/ Weybridge [H7N7], remantadine-resistant) ORGANISM #formal_name influenza A virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 30-Sep-1993 ACCESSIONS PN0088 REFERENCE PN0083 !$#authors Karginov, V.A.; Blinov, V.M.; Safronov, P.F.; Mamaev, L.V.; !1Golovin, S.Y.; Netesov, S.V.; Samokhvalov, E.I.; Sharova, !1N.K.; Yuferov, V.P.; Urivaev, L.V.; Bukrinskaya, A.G. !$#journal Bioorg. Khim. (1987) 13:1638-1643 !$#title Comparative analysis of the M-gene primary structures and !1corresponding amino acid sequences of remantadine-sensitive !1and remantadine-resistant strains of the influenza virus A/ !1FPV/Weybridge (H7N7). !$#cross-references MUID:88221675; PMID:3450279 !$#accession PN0088 !'##molecule_type genomic RNA !'##residues 1-68 ##label KAR !'##cross-references GB:M38299 !'##note the authors translated the codon GTC for residue 4 as Tyr GENETICS !$#map_position segment 7 CLASSIFICATION #superfamily influenza A virus matrix protein M3 KEYWORDS matrix protein SUMMARY #length 68 #molecular-weight 8130 #checksum 2974 SEQUENCE /// ENTRY MNIV1K #type complete TITLE nonstructural protein NS1 - influenza A virus (strain A/ Alaska/6/77) ORGANISM #formal_name influenza A virus #note host Homo sapiens (man) DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 16-Jul-1999 ACCESSIONS A04087 REFERENCE A92994 !$#authors Buonagurio, D.A.; Krystal, M.; Palese, P.; DeBorde, D.C.; !1Maassab, H.F. !$#journal J. Virol. (1984) 49:418-425 !$#title Analysis of an influenza A virus mutant with a deletion in !1the NS segment. !$#cross-references MUID:84115066; PMID:6363726 !$#accession A04087 !'##molecule_type genomic RNA !'##residues 1-237 ##label BUO !'##cross-references GB:K01332; NID:g324795; PIDN:AAA43515.1; !1PID:g324797 GENETICS !$#map_position segment 8 CLASSIFICATION #superfamily influenza virus nonstructural protein NS1 KEYWORDS alternative splicing SUMMARY #length 237 #molecular-weight 26824 #checksum 6697 SEQUENCE /// ENTRY MNIV1A #type complete TITLE nonstructural protein NS1 - influenza A virus (strain A/ Udorn/72 [H3N2]) ORGANISM #formal_name influenza A virus DATE 31-Oct-1980 #sequence_revision 31-Oct-1980 #text_change 28-May-1999 ACCESSIONS A04088; S11297 REFERENCE A90801 !$#authors Lamb, R.A.; Lai, C.J. !$#journal Cell (1980) 21:475-485 !$#title Sequence of interrupted and uninterrupted mRNAs and cloned !1DNA coding for the two overlapping nonstructural proteins of !1influenza virus. !$#cross-references MUID:81001890; PMID:7407920 !$#accession A04088 !'##molecule_type mRNA !'##residues 1-237 ##label LAM !'##cross-references GB:V01102; GB:J02169; NID:g60797; PIDN:CAA24288.1; !1PID:g60798 !'##experimental_source strain A/Udorn/72 [H3N2] REFERENCE S11286 !$#authors Robertson, J.S. !$#journal Nucleic Acids Res. (1979) 6:3745-3757 !$#title 5' and 3' terminal nucleotide sequences of the RNA genome !1segments of influenza virus. !$#cross-references MUID:80034428; PMID:493121 !$#accession S11297 !'##molecule_type genomic RNA !'##residues 1-15 ##label ROB !'##cross-references GB:J02118 !'##experimental_source strain A/FPV/Rostock/34 [H7N1] !'##note the authors translated the codon CAG for residue 10 as Glu GENETICS !$#map_position segment 8 CLASSIFICATION #superfamily influenza virus nonstructural protein NS1 KEYWORDS alternative splicing SUMMARY #length 237 #molecular-weight 26846 #checksum 7549 SEQUENCE /// ENTRY MNIV1 #type complete TITLE nonstructural protein NS1 - influenza A virus (strain A/PR/ 8/34) ORGANISM #formal_name influenza A virus DATE 30-Apr-1981 #sequence_revision 30-Apr-1981 #text_change 30-Sep-1993 ACCESSIONS A04089 REFERENCE A93714 !$#authors Baez, M.; Taussig, R.; Zazra, J.J.; Young, J.F.; Palese, P.; !1Reisfeld, A.; Skalka, A.M. !$#journal Nucleic Acids Res. (1980) 8:5845-5858 !$#title Complete nucleotide sequence of the influenza A/PR/8/34 !1virus NS gene and comparison with the NS genes of the A/ !1Udorn/72 and A/FPV/Rostock/34 strains. !$#cross-references MUID:81124304; PMID:7465426 !$#accession A04089 !'##molecule_type genomic RNA !'##residues 1-230 ##label BAE GENETICS !$#map_position segment 8 CLASSIFICATION #superfamily influenza virus nonstructural protein NS1 KEYWORDS alternative splicing SUMMARY #length 230 #molecular-weight 25867 #checksum 4765 SEQUENCE /// ENTRY MNIV14 #type complete TITLE nonstructural protein NS1 - influenza A virus (strain A/FW/ 1/50 [H1N1]) ORGANISM #formal_name influenza A virus DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 16-Jul-1999 ACCESSIONS A92991; A04090; B92982 REFERENCE A92991 !$#authors Krystal, M.; Buonagurio, D.; Young, J.F.; Palese, P. !$#journal J. Virol. (1983) 45:547-554 !$#title Sequential mutations in the NS genes of influenza virus !1field strains. !$#cross-references MUID:83164298; PMID:6834468 !$#accession A92991 !'##molecule_type genomic RNA !'##residues 1-237 ##label KRY !'##cross-references GB:K00576; NID:g324813; PIDN:AAA43525.1; !1PID:g324815 GENETICS !$#map_position segment 8 CLASSIFICATION #superfamily influenza virus nonstructural protein NS1 KEYWORDS alternative splicing SUMMARY #length 237 #molecular-weight 26889 #checksum 9287 SEQUENCE /// ENTRY MNIV77 #type complete TITLE nonstructural protein NS1 - influenza A virus (strain A/ USSR/90/77 [H1N1]) ORGANISM #formal_name influenza A virus DATE 19-May-1994 #sequence_revision 19-May-1994 #text_change 16-Jul-1999 ACCESSIONS E92991; A04090 REFERENCE A92991 !$#authors Krystal, M.; Buonagurio, D.; Young, J.F.; Palese, P. !$#journal J. Virol. (1983) 45:547-554 !$#title Sequential mutations in the NS genes of influenza virus !1field strains. !$#cross-references MUID:83164298; PMID:6834468 !$#accession E92991 !'##molecule_type genomic RNA !'##residues 1-237 ##label KRY !'##cross-references GB:K00578; NID:g324839; PIDN:AAA43540.1; !1PID:g324841 GENETICS !$#map_position segment 8 CLASSIFICATION #superfamily influenza virus nonstructural protein NS1 KEYWORDS alternative splicing SUMMARY #length 237 #molecular-weight 26890 #checksum 8992 SEQUENCE /// ENTRY MNIV47 #type complete TITLE nonstructural protein NS1 - influenza A virus (strain A/FM/ 1/47 [H1N1]) ORGANISM #formal_name influenza A virus DATE 19-May-1994 #sequence_revision 19-May-1994 #text_change 16-Jul-1999 ACCESSIONS F92991; A04090 REFERENCE A92991 !$#authors Krystal, M.; Buonagurio, D.; Young, J.F.; Palese, P. !$#journal J. Virol. (1983) 45:547-554 !$#title Sequential mutations in the NS genes of influenza virus !1field strains. !$#cross-references MUID:83164298; PMID:6834468 !$#accession F92991 !'##molecule_type genomic RNA !'##residues 1-202 ##label KRY !'##cross-references GB:K00577; NID:g324808; PIDN:AAA43522.1; !1PID:g324810 GENETICS !$#map_position segment 8 CLASSIFICATION #superfamily influenza virus nonstructural protein NS1 KEYWORDS alternative splicing SUMMARY #length 202 #molecular-weight 22680 #checksum 4602 SEQUENCE /// ENTRY MNIV61 #type complete TITLE nonstructural protein NS1 - influenza A virus (strain A/Ann Arbor/6/60 [H2N2]) ORGANISM #formal_name influenza A virus DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS G31831 REFERENCE A31831 !$#authors Cox, N.J.; Kitame, F.; Kendal, A.P.; Maassab, H.F.; Naeve, !1C. !$#journal Virology (1988) 167:554-567 !$#title Identification of sequence changes in the cold-adapted, live !1attenuated influenza vaccine strain, A/Ann Arbor/6/60 !1(H2N2). !$#cross-references MUID:89073759; PMID:2974219 !$#accession G31831 !'##molecule_type genomic RNA !'##residues 1-217 ##label COX !'##cross-references GB:M23968; GB:J04349; GB:M23969; NID:g324860; !1PIDN:AAA43553.1; PID:g324862 GENETICS !$#map_position segment 8 CLASSIFICATION #superfamily influenza virus nonstructural protein NS1 KEYWORDS alternative splicing; nonstructural protein SUMMARY #length 217 #molecular-weight 24429 #checksum 478 SEQUENCE /// ENTRY MNIVC1 #type complete TITLE nonstructural protein NS1 - influenza A virus (strain A/ Chile/1/83 [H1N1]) ORGANISM #formal_name influenza A virus DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 07-Jun-1996 ACCESSIONS A34215; S04836 REFERENCE A34215 !$#authors Schreier, E.; Roeske, H.; Michel, S. !$#journal Nucleic Acids Res. (1989) 17:5381 !$#title Nucleotide sequence of the NS gene of influenza virus A/ !1Chile/1/83 (H1N1). !$#cross-references MUID:89345097; PMID:2762132 !$#accession A34215 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-237 ##label SCH !'##cross-references EMBL:X15282 GENETICS !$#map_position segment 8 CLASSIFICATION #superfamily influenza virus nonstructural protein NS1 KEYWORDS alternative splicing; nonstructural protein SUMMARY #length 237 #molecular-weight 26819 #checksum 7167 SEQUENCE /// ENTRY MNIV1F #type complete TITLE nonstructural protein NS1 - influenza A virus ORGANISM #formal_name influenza A virus DATE 31-Oct-1980 #sequence_revision 31-Oct-1980 #text_change 30-Sep-1993 ACCESSIONS A04091 REFERENCE A93858 !$#authors Porter, A.G.; Smith, J.C.; Emtage, J.S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1980) 77:5074-5078 !$#title Nucleotide sequence of influenza virus RNA segment 8 !1indicates that coding regions for NS-1 and NS-2 proteins !1overlap. !$#cross-references MUID:81054909; PMID:6254054 !$#accession A04091 !'##molecule_type mRNA !'##residues 1-230 ##label POR !'##experimental_source strain Rostock CLASSIFICATION #superfamily influenza virus nonstructural protein NS1 KEYWORDS alternative splicing SUMMARY #length 230 #molecular-weight 25923 #checksum 3791 SEQUENCE /// ENTRY MNIVX1 #type fragment TITLE nonstructural protein NS1 - influenza A virus (strain A/ Chicken/Japan/24 [H7N7]) (fragment) ORGANISM #formal_name influenza A virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS A27846 REFERENCE A94361 !$#authors Nakajima, K.; Nobusawa, E.; Ogawa, T.; Nakajima, S. !$#journal Virology (1987) 158:465-468 !$#title Genetic divergence of the NS genes of avian influenza !1viruses. !$#cross-references MUID:87236215; PMID:2954302 !$#accession A27846 !'##molecule_type genomic RNA !'##residues 1-227 ##label NAK !'##cross-references GB:M16561; NID:g324777; PIDN:AAA43504.1; !1PID:g324778 GENETICS !$#gene NS1 !$#map_position segment 8 CLASSIFICATION #superfamily influenza virus nonstructural protein NS1 KEYWORDS alternative splicing; nonstructural protein SUMMARY #length 227 #checksum 8526 SEQUENCE /// ENTRY MNIVX3 #type fragment TITLE nonstructural protein NS1 - influenza A virus (strain A/ Duck/England/56 [H11N6]) (fragment) ORGANISM #formal_name influenza A virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS C27846 REFERENCE A94361 !$#authors Nakajima, K.; Nobusawa, E.; Ogawa, T.; Nakajima, S. !$#journal Virology (1987) 158:465-468 !$#title Genetic divergence of the NS genes of avian influenza !1viruses. !$#cross-references MUID:87236215; PMID:2954302 !$#accession C27846 !'##molecule_type genomic RNA !'##residues 1-227 ##label NAK !'##cross-references GB:M16563; NID:g324786; PIDN:AAA43510.1; !1PID:g324787 GENETICS !$#gene NS1 !$#map_position segment 8 CLASSIFICATION #superfamily influenza virus nonstructural protein NS1 KEYWORDS alternative splicing; nonstructural protein SUMMARY #length 227 #checksum 9326 SEQUENCE /// ENTRY MNIVX5 #type fragment TITLE nonstructural protein NS1 - influenza A virus (strain A/ Tern/South Africa/61 [H5N3]) (fragment) ORGANISM #formal_name influenza A virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS E27846 REFERENCE A94361 !$#authors Nakajima, K.; Nobusawa, E.; Ogawa, T.; Nakajima, S. !$#journal Virology (1987) 158:465-468 !$#title Genetic divergence of the NS genes of avian influenza !1viruses. !$#cross-references MUID:87236215; PMID:2954302 !$#accession E27846 !'##molecule_type genomic RNA !'##residues 1-227 ##label NAK !'##cross-references GB:M16564; NID:g324875; PIDN:AAA43572.1; !1PID:g324876 GENETICS !$#gene NS1 !$#map_position segment 8 CLASSIFICATION #superfamily influenza virus nonstructural protein NS1 KEYWORDS alternative splicing; nonstructural protein SUMMARY #length 227 #checksum 8937 SEQUENCE /// ENTRY MNIVX9 #type fragment TITLE nonstructural protein NS1 - influenza A virus (strain A/ Mynah/Haneda-Thai/76 [H3N1]) (fragment) ORGANISM #formal_name influenza A virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS I27846 REFERENCE A94361 !$#authors Nakajima, K.; Nobusawa, E.; Ogawa, T.; Nakajima, S. !$#journal Virology (1987) 158:465-468 !$#title Genetic divergence of the NS genes of avian influenza !1viruses. !$#cross-references MUID:87236215; PMID:2954302 !$#accession I27846 !'##molecule_type genomic RNA !'##residues 1-227 ##label NAK !'##cross-references GB:M17070; NID:g324854; PIDN:AAA43548.1; !1PID:g324855 GENETICS !$#gene NS1 !$#map_position segment 8 CLASSIFICATION #superfamily influenza virus nonstructural protein NS1 KEYWORDS alternative splicing; nonstructural protein SUMMARY #length 227 #checksum 8286 SEQUENCE /// ENTRY MNIVA1 #type complete TITLE nonstructural protein NS1 - influenza A virus (strain A/ pintail/Alberta/268/78) ORGANISM #formal_name influenza A virus DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 08-Apr-1994 ACCESSIONS A32662 REFERENCE A32662 !$#authors Treanor, J.J.; Snyder, M.H.; London, W.T.; Murphy, B.R. !$#journal Virology (1989) 171:1-9 !$#title The B allele of the NS gene of avian influenza viruses, but !1not the A allele, attenuates a human influenza A virus for !1squirrel monkeys. !$#cross-references MUID:89299445; PMID:2525836 !$#accession A32662 !'##molecule_type genomic RNA !'##residues 1-230 ##label TRE GENETICS !$#gene NS1 !$#map_position segment 8 CLASSIFICATION #superfamily influenza virus nonstructural protein NS1 KEYWORDS alternative splicing; nonstructural protein SUMMARY #length 230 #molecular-weight 26058 #checksum 4478 SEQUENCE /// ENTRY MNIVA2 #type complete TITLE nonstructural protein NS1 - influenza A virus (strain A/ mallard/New York/6750/78) ORGANISM #formal_name influenza A virus DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 08-Apr-1994 ACCESSIONS C32662 REFERENCE A32662 !$#authors Treanor, J.J.; Snyder, M.H.; London, W.T.; Murphy, B.R. !$#journal Virology (1989) 171:1-9 !$#title The B allele of the NS gene of avian influenza viruses, but !1not the A allele, attenuates a human influenza A virus for !1squirrel monkeys. !$#cross-references MUID:89299445; PMID:2525836 !$#accession C32662 !'##molecule_type genomic RNA !'##residues 1-230 ##label TRE GENETICS !$#gene NS1 !$#map_position segment 8 CLASSIFICATION #superfamily influenza virus nonstructural protein NS1 KEYWORDS alternative splicing; nonstructural protein SUMMARY #length 230 #molecular-weight 26069 #checksum 3789 SEQUENCE /// ENTRY MNIVA3 #type complete TITLE nonstructural protein NS1 - influenza A virus (strain A/ mallard/New York/6874/78) ORGANISM #formal_name influenza A virus DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 08-Apr-1994 ACCESSIONS E32662 REFERENCE A32662 !$#authors Treanor, J.J.; Snyder, M.H.; London, W.T.; Murphy, B.R. !$#journal Virology (1989) 171:1-9 !$#title The B allele of the NS gene of avian influenza viruses, but !1not the A allele, attenuates a human influenza A virus for !1squirrel monkeys. !$#cross-references MUID:89299445; PMID:2525836 !$#accession E32662 !'##molecule_type genomic RNA !'##residues 1-230 ##label TRE GENETICS !$#gene NS1 !$#map_position segment 8 CLASSIFICATION #superfamily influenza virus nonstructural protein NS1 KEYWORDS alternative splicing; nonstructural protein SUMMARY #length 230 #molecular-weight 26069 #checksum 3307 SEQUENCE /// ENTRY MNIVA4 #type complete TITLE nonstructural protein NS1 - influenza A virus (strain A/ pintail/Alberta/119/79) ORGANISM #formal_name influenza A virus DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 08-Apr-1994 ACCESSIONS G32662 REFERENCE A32662 !$#authors Treanor, J.J.; Snyder, M.H.; London, W.T.; Murphy, B.R. !$#journal Virology (1989) 171:1-9 !$#title The B allele of the NS gene of avian influenza viruses, but !1not the A allele, attenuates a human influenza A virus for !1squirrel monkeys. !$#cross-references MUID:89299445; PMID:2525836 !$#accession G32662 !'##molecule_type genomic RNA !'##residues 1-230 ##label TRE GENETICS !$#gene NS1 !$#map_position segment 8 CLASSIFICATION #superfamily influenza virus nonstructural protein NS1 KEYWORDS alternative splicing; nonstructural protein SUMMARY #length 230 #molecular-weight 26186 #checksum 3622 SEQUENCE /// ENTRY MNIVX7 #type fragment TITLE nonstructural protein NS1 - influenza A virus (strain A/ Duck/Ukraine/63 [H3N8]) (fragment) ORGANISM #formal_name influenza A virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS G27846 REFERENCE A94361 !$#authors Nakajima, K.; Nobusawa, E.; Ogawa, T.; Nakajima, S. !$#journal Virology (1987) 158:465-468 !$#title Genetic divergence of the NS genes of avian influenza !1viruses. !$#cross-references MUID:87236215; PMID:2954302 !$#accession G27846 !'##molecule_type genomic RNA !'##residues 1-227 ##label NAK !'##cross-references GB:M16565; NID:g324789; PIDN:AAA43512.1; !1PID:g324790 GENETICS !$#gene NS1 !$#map_position segment 8 CLASSIFICATION #superfamily influenza virus nonstructural protein NS1 KEYWORDS alternative splicing; nonstructural protein SUMMARY #length 227 #checksum 7880 SEQUENCE /// ENTRY D45539 #type complete TITLE nonstructural protein NS1 - influenza A virus (strain A/ chicken/Brescia/1902 [H7N7]) ORGANISM #formal_name influenza A virus DATE 24-Feb-1994 #sequence_revision 24-Feb-1994 #text_change 24-Feb-1994 ACCESSIONS D45539 REFERENCE A45539 !$#authors Klimov, A.; Prosch, S.; Schafer, J.; Bucher, D. !$#journal Arch. Virol. (1992) 122:143-161 !$#title Subtype H7 influenza viruses: comparative antigenic and !1molecular analysis of the HA-, M-, and NS-genes. !$#cross-references MUID:92109567; PMID:1530908 !$#accession D45539 !'##molecule_type genomic RNA !'##residues 1-230 ##label KLI !'##note sequence extracted from NCBI backbone (NCBIN:74250, !1NCBIP:74252) GENETICS !$#gene NS1 !$#map_position segment 8 CLASSIFICATION #superfamily influenza virus nonstructural protein NS1 KEYWORDS alternative splicing; nonstructural protein SUMMARY #length 230 #molecular-weight 26156 #checksum 2172 SEQUENCE /// ENTRY MNIV16 #type complete TITLE nonstructural protein NS1 - influenza A virus (strain A/ duck/Alberta/60/76) ORGANISM #formal_name influenza A virus DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 16-Jul-1999 ACCESSIONS A04092 REFERENCE A04092 !$#authors Baez, M.; Zazra, J.J.; Elliott, R.M.; Young, J.F.; Palese, !1P. !$#journal Virology (1981) 113:397-402 !$#title Nucleotide sequence of the influenza A/duck/Alberta/60/76 !1virus NS RNA: conservation of the NS1/NS2 overlapping gene !1structure in a divergent influenza virus RNA segment. !$#cross-references MUID:81276929; PMID:6927848 !$#accession A04092 !'##molecule_type genomic RNA !'##residues 1-230 ##label BAE !'##cross-references GB:J02105; GB:M17071; NID:g324783; PIDN:AAA43509.1; !1PID:g324785 GENETICS !$#map_position segment 8 CLASSIFICATION #superfamily influenza virus nonstructural protein NS1 KEYWORDS alternative splicing SUMMARY #length 230 #molecular-weight 26049 #checksum 4412 SEQUENCE /// ENTRY MNIVA5 #type complete TITLE nonstructural protein NS1 - influenza A virus (strain A/ mallard/Alberta/88/76) ORGANISM #formal_name influenza A virus DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 08-Apr-1994 ACCESSIONS A32663 REFERENCE A32662 !$#authors Treanor, J.J.; Snyder, M.H.; London, W.T.; Murphy, B.R. !$#journal Virology (1989) 171:1-9 !$#title The B allele of the NS gene of avian influenza viruses, but !1not the A allele, attenuates a human influenza A virus for !1squirrel monkeys. !$#cross-references MUID:89299445; PMID:2525836 !$#accession A32663 !'##molecule_type genomic RNA !'##residues 1-230 ##label TRE GENETICS !$#gene NS1 !$#map_position segment 8 CLASSIFICATION #superfamily influenza virus nonstructural protein NS1 KEYWORDS alternative splicing; nonstructural protein SUMMARY #length 230 #molecular-weight 26008 #checksum 4393 SEQUENCE /// ENTRY MNIV71 #type complete TITLE nonstructural protein NS1 - influenza A virus (strain A/ turkey/Oregon/71 [H7N5]) ORGANISM #formal_name influenza A virus DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jul-1999 ACCESSIONS A27529 REFERENCE A27529 !$#authors Norton, G.P.; Tanaka, T.; Tobita, K.; Nakada, S.; !1Buonagurio, D.A.; Greenspan, D.; Krystal, M.; Palese, P. !$#journal Virology (1987) 156:204-213 !$#title Infectious influenza A and B virus variants with long !1carboxyl terminal deletions in the NS1 polypeptides. !$#cross-references MUID:87122162; PMID:3811235 !$#accession A27529 !'##molecule_type genomic RNA !'##residues 1-124 ##label NOR !'##cross-references GB:M16623; NID:g324857; PIDN:AAA43551.1; !1PID:g324859 GENETICS !$#map_position segment 8 CLASSIFICATION #superfamily influenza virus nonstructural protein NS1 KEYWORDS alternative splicing; nonstructural protein SUMMARY #length 124 #molecular-weight 14339 #checksum 6074 SEQUENCE /// ENTRY MNIVA6 #type complete TITLE nonstructural protein NS1 - influenza A virus (strain A/ mallard/Alberta/827/88) ORGANISM #formal_name influenza A virus DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 08-Apr-1994 ACCESSIONS C32663 REFERENCE A32662 !$#authors Treanor, J.J.; Snyder, M.H.; London, W.T.; Murphy, B.R. !$#journal Virology (1989) 171:1-9 !$#title The B allele of the NS gene of avian influenza viruses, but !1not the A allele, attenuates a human influenza A virus for !1squirrel monkeys. !$#cross-references MUID:89299445; PMID:2525836 !$#accession C32663 !'##molecule_type genomic RNA !'##residues 1-230 ##label TRE GENETICS !$#gene NS1 !$#map_position segment 8 CLASSIFICATION #superfamily influenza virus nonstructural protein NS1 KEYWORDS alternative splicing; nonstructural protein SUMMARY #length 230 #molecular-weight 26036 #checksum 4224 SEQUENCE /// ENTRY MNIVA7 #type complete TITLE nonstructural protein NS1 - influenza A virus (strain A/ pintail/Alberta/121/79) ORGANISM #formal_name influenza A virus DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 08-Apr-1994 ACCESSIONS E32663 REFERENCE A32662 !$#authors Treanor, J.J.; Snyder, M.H.; London, W.T.; Murphy, B.R. !$#journal Virology (1989) 171:1-9 !$#title The B allele of the NS gene of avian influenza viruses, but !1not the A allele, attenuates a human influenza A virus for !1squirrel monkeys. !$#cross-references MUID:89299445; PMID:2525836 !$#accession E32663 !'##molecule_type genomic RNA !'##residues 1-230 ##label TRE GENETICS !$#gene NS1 !$#map_position segment 8 CLASSIFICATION #superfamily influenza virus nonstructural protein NS1 KEYWORDS alternative splicing; nonstructural protein SUMMARY #length 230 #molecular-weight 26107 #checksum 3804 SEQUENCE /// ENTRY MNIVA8 #type complete TITLE nonstructural protein NS1 - influenza A virus (strain A/ pintail/Alberta/358/79) ORGANISM #formal_name influenza A virus DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 08-Apr-1994 ACCESSIONS G32663 REFERENCE A32662 !$#authors Treanor, J.J.; Snyder, M.H.; London, W.T.; Murphy, B.R. !$#journal Virology (1989) 171:1-9 !$#title The B allele of the NS gene of avian influenza viruses, but !1not the A allele, attenuates a human influenza A virus for !1squirrel monkeys. !$#cross-references MUID:89299445; PMID:2525836 !$#accession G32663 !'##molecule_type genomic RNA !'##residues 1-230 ##label TRE GENETICS !$#gene NS1 !$#map_position segment 8 CLASSIFICATION #superfamily influenza virus nonstructural protein NS1 KEYWORDS alternative splicing; nonstructural protein SUMMARY #length 230 #molecular-weight 26058 #checksum 4380 SEQUENCE /// ENTRY MNIVA #type complete TITLE nonstructural protein NS1 - influenza B virus (strain B/Lee/ 40) ORGANISM #formal_name influenza B virus DATE 05-Apr-1983 #sequence_revision 05-Apr-1983 #text_change 16-Jul-1999 ACCESSIONS A04093 REFERENCE A04093 !$#authors Briedis, D.J.; Lamb, R.A. !$#journal J. Virol. (1982) 42:186-193 !$#title Influenza B virus genome: sequences and structural !1organization of RNA segment 8 and the mRNAs coding for the !1NS-1 and NS-2 proteins. !$#cross-references MUID:82216985; PMID:6283137 !$#accession A04093 !'##molecule_type genomic RNA !'##residues 1-281 ##label BRI !'##cross-references GB:J02096; NID:g325254; PIDN:AAA43756.1; !1PID:g325256 GENETICS !$#map_position segment 8 CLASSIFICATION #superfamily influenza B virus nonstructural protein NS1 KEYWORDS alternative splicing SUMMARY #length 281 #molecular-weight 32067 #checksum 9608 SEQUENCE /// ENTRY MNIV73 #type complete TITLE nonstructural protein NS1 - influenza B virus (strain B/ Yamagata/1/73) ORGANISM #formal_name influenza B virus DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jul-1999 ACCESSIONS C27529 REFERENCE A27529 !$#authors Norton, G.P.; Tanaka, T.; Tobita, K.; Nakada, S.; !1Buonagurio, D.A.; Greenspan, D.; Krystal, M.; Palese, P. !$#journal Virology (1987) 156:204-213 !$#title Infectious influenza A and B virus variants with long !1carboxyl terminal deletions in the NS1 polypeptides. !$#cross-references MUID:87122162; PMID:3811235 !$#accession C27529 !'##molecule_type genomic RNA !'##residues 1-281 ##label NOR !'##cross-references GB:M16633; NID:g325262; PIDN:AAA43761.1; !1PID:g325264 GENETICS !$#map_position segment 8 CLASSIFICATION #superfamily influenza B virus nonstructural protein NS1 KEYWORDS alternative splicing; nonstructural protein SUMMARY #length 281 #molecular-weight 31943 #checksum 807 SEQUENCE /// ENTRY MNIV1B #type complete TITLE nonstructural protein NS1 - influenza B virus (strain B/Ann Arbor/1/66 [cold-adapted and wild-type]) ORGANISM #formal_name influenza B virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS E30064 REFERENCE A28604 !$#authors DeBorde, D.C.; Donabedian, A.M.; Herlocher, M.L.; Naeve, !1C.W.; Maassab, H.F. !$#journal Virology (1988) 163:429-443 !$#title Sequence comparison of wild-type and cold-adapted B/Ann !1Arbor/1/66 influenza virus genes. !$#cross-references MUID:88179548; PMID:3354202 !$#accession E30064 !'##molecule_type genomic RNA !'##residues 1-281 ##label DEB !'##cross-references GB:M20224; NID:g325251; PIDN:AAA43754.1; !1PID:g325253 GENETICS !$#map_position segment 8 CLASSIFICATION #superfamily influenza B virus nonstructural protein NS1 KEYWORDS alternative splicing; nonstructural protein SUMMARY #length 281 #molecular-weight 31854 #checksum 630 SEQUENCE /// ENTRY MNIV21 #type complete TITLE nonstructural protein NS1 - influenza B virus (strain B/ Yamagata/1/73/201) ORGANISM #formal_name influenza B virus DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jul-1999 ACCESSIONS D27529 REFERENCE A27529 !$#authors Norton, G.P.; Tanaka, T.; Tobita, K.; Nakada, S.; !1Buonagurio, D.A.; Greenspan, D.; Krystal, M.; Palese, P. !$#journal Virology (1987) 156:204-213 !$#title Infectious influenza A and B virus variants with long !1carboxyl terminal deletions in the NS1 polypeptides. !$#cross-references MUID:87122162; PMID:3811235 !$#accession D27529 !'##molecule_type genomic RNA !'##residues 1-127 ##label NOR !'##cross-references GB:M16634; NID:g325248; PIDN:AAA43752.1; !1PID:g325250 GENETICS !$#map_position segment 8 CLASSIFICATION #superfamily influenza B virus nonstructural protein NS1 KEYWORDS alternative splicing; nonstructural protein SUMMARY #length 127 #molecular-weight 14336 #checksum 8323 SEQUENCE /// ENTRY MNIVAW #type complete TITLE nonstructural protein NS1 - influenza B virus (strain B/ Yamagata [AWBY-234]) ORGANISM #formal_name influenza B virus #note host Homo sapiens (man) DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS A33778 REFERENCE A33778 !$#authors Tobita, K.; Tanaka, T.; Odagiri, T.; Tashiro, M.; Feng, S.Y. !$#journal Virology (1990) 174:314-319 !$#title Nucleotide sequence and some biological properties of the NS !1gene of a newly isolated influenza B virus mutant which has !1a long carboxyl terminal deletion in the NS1 protein. !$#cross-references MUID:90101391; PMID:2136779 !$#accession A33778 !'##molecule_type mRNA !'##residues 1-90 ##label TOB !'##cross-references GB:M32749; NID:g325257; PIDN:AAA43757.1; !1PID:g325258 !'##note the authors translated the codon CTT for residue 34 as Ile !'##note the carboxyl end of this protein is truncated, resulting from a !1heterotypic cross between influenza viruses A/WSN(H1N1) and !1B/Yamagata/1/73 GENETICS !$#gene NS1 !$#map_position segment 8 CLASSIFICATION #superfamily influenza B virus nonstructural protein NS1 KEYWORDS alternative splicing; nonstructural protein SUMMARY #length 90 #molecular-weight 10321 #checksum 9329 SEQUENCE /// ENTRY MNIV2K #type complete TITLE nonstructural protein NS2 - influenza A virus (strains A/ Alaska/6/77 and A/Udorn/72 [H3N2]) ORGANISM #formal_name influenza A virus #note host Homo sapiens (man) DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 16-Jul-1999 ACCESSIONS A04094; A90801; A04095 REFERENCE A92994 !$#authors Buonagurio, D.A.; Krystal, M.; Palese, P.; DeBorde, D.C.; !1Maassab, H.F. !$#journal J. Virol. (1984) 49:418-425 !$#title Analysis of an influenza A virus mutant with a deletion in !1the NS segment. !$#cross-references MUID:84115066; PMID:6363726 !$#accession A04094 !'##molecule_type genomic RNA !'##residues 1-121 ##label BUO !'##cross-references GB:K01332; NID:g324795; PIDN:AAA43514.1; !1PID:g324796 !'##experimental_source strain A/Alaska/6/77 REFERENCE A90801 !$#authors Lamb, R.A.; Lai, C.J. !$#journal Cell (1980) 21:475-485 !$#title Sequence of interrupted and uninterrupted mRNAs and cloned !1DNA coding for the two overlapping nonstructural proteins of !1influenza virus. !$#cross-references MUID:81001890; PMID:7407920 !$#accession A90801 !'##molecule_type genomic RNA !'##residues 1-121 ##label LAM !'##cross-references GB:V01102; GB:J02169; NID:g60797; PIDN:CAA24289.1; !1PID:g60799 !'##experimental_source strain A/Udorn/72 [H3N2] GENETICS !$#map_position segment 8 !$#introns 10/3 CLASSIFICATION #superfamily influenza virus nonstructural protein NS2 KEYWORDS alternative splicing SUMMARY #length 121 #molecular-weight 14365 #checksum 3413 SEQUENCE /// ENTRY MNIV62 #type complete TITLE nonstructural protein NS2 - influenza A virus (strain A/Ann Arbor/6/60 [H2N2]) ORGANISM #formal_name influenza A virus DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS H31831 REFERENCE A31831 !$#authors Cox, N.J.; Kitame, F.; Kendal, A.P.; Maassab, H.F.; Naeve, !1C. !$#journal Virology (1988) 167:554-567 !$#title Identification of sequence changes in the cold-adapted, live !1attenuated influenza vaccine strain, A/Ann Arbor/6/60 !1(H2N2). !$#cross-references MUID:89073759; PMID:2974219 !$#accession H31831 !'##molecule_type genomic RNA !'##residues 1-121 ##label COX !'##cross-references GB:M23968; GB:J04349; GB:M23969; NID:g324860; !1PIDN:AAA43552.1; PID:g324861 GENETICS !$#map_position segment 8 !$#introns 10/3 CLASSIFICATION #superfamily influenza virus nonstructural protein NS2 KEYWORDS alternative splicing; nonstructural protein SUMMARY #length 121 #molecular-weight 14351 #checksum 3262 SEQUENCE /// ENTRY MNIV2A #type complete TITLE nonstructural protein NS2 - influenza A virus (strain A/ USSR/90/77 [H1N1]) ORGANISM #formal_name influenza A virus DATE 31-Oct-1980 #sequence_revision 14-Nov-1983 #text_change 16-Jul-1999 ACCESSIONS B92991; A04095; A90801; C92991; D92991 REFERENCE A92991 !$#authors Krystal, M.; Buonagurio, D.; Young, J.F.; Palese, P. !$#journal J. Virol. (1983) 45:547-554 !$#title Sequential mutations in the NS genes of influenza virus !1field strains. !$#cross-references MUID:83164298; PMID:6834468 !$#accession B92991 !'##molecule_type genomic RNA !'##residues 1-121 ##label KRY !'##cross-references GB:K00578; NID:g324839; PIDN:AAA43539.1; !1PID:g324840 GENETICS !$#map_position segment 8 CLASSIFICATION #superfamily influenza virus nonstructural protein NS2 KEYWORDS alternative splicing SUMMARY #length 121 #molecular-weight 14379 #checksum 3465 SEQUENCE /// ENTRY MNIV2W #type complete TITLE nonstructural protein NS2 - influenza A virus (strain A/FW/ 1/50 [H1N1]) ORGANISM #formal_name influenza A virus DATE 19-May-1994 #sequence_revision 19-May-1994 #text_change 24-Sep-1999 ACCESSIONS C92991; A04095 REFERENCE A92991 !$#authors Krystal, M.; Buonagurio, D.; Young, J.F.; Palese, P. !$#journal J. Virol. (1983) 45:547-554 !$#title Sequential mutations in the NS genes of influenza virus !1field strains. !$#cross-references MUID:83164298; PMID:6834468 !$#accession C92991 !'##molecule_type genomic RNA !'##residues 1-121 ##label KRY !'##cross-references GB:K00577; NID:g324808; PIDN:AAA43521.1; !1PID:g324809 GENETICS !$#map_position segment 8 CLASSIFICATION #superfamily influenza virus nonstructural protein NS2 KEYWORDS alternative splicing SUMMARY #length 121 #molecular-weight 14433 #checksum 3615 SEQUENCE /// ENTRY MNIV2M #type complete TITLE nonstructural protein NS2 - influenza A virus (strain A/FM/ 1/47 [H1N1]) ORGANISM #formal_name influenza A virus DATE 19-May-1994 #sequence_revision 19-May-1994 #text_change 16-Jul-1999 ACCESSIONS D92991; A04095 REFERENCE A92991 !$#authors Krystal, M.; Buonagurio, D.; Young, J.F.; Palese, P. !$#journal J. Virol. (1983) 45:547-554 !$#title Sequential mutations in the NS genes of influenza virus !1field strains. !$#cross-references MUID:83164298; PMID:6834468 !$#accession D92991 !'##molecule_type genomic RNA !'##residues 1-121 ##label KRY !'##cross-references GB:K00576; NID:g324813; PIDN:AAA43524.1; !1PID:g324814 GENETICS !$#map_position segment 8 CLASSIFICATION #superfamily influenza virus nonstructural protein NS2 KEYWORDS alternative splicing SUMMARY #length 121 #molecular-weight 14300 #checksum 4024 SEQUENCE /// ENTRY MNIVC2 #type complete TITLE nonstructural protein NS2 - influenza A virus (strain A/ Chile/1/83 [H1N1]) ORGANISM #formal_name influenza A virus DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jul-1999 ACCESSIONS B34215; S04837 REFERENCE A34215 !$#authors Schreier, E.; Roeske, H.; Michel, S. !$#journal Nucleic Acids Res. (1989) 17:5381 !$#title Nucleotide sequence of the NS gene of influenza virus A/ !1Chile/1/83 (H1N1). !$#cross-references MUID:89345097; PMID:2762132 !$#accession B34215 !'##status translation not shown !'##molecule_type mRNA !'##residues 1-121 ##label SCH !'##cross-references EMBL:X15282; NID:g60479; PIDN:CAA33356.1; !1PID:g60481 GENETICS !$#map_position segment 8 !$#introns 10/3 CLASSIFICATION #superfamily influenza virus nonstructural protein NS2 KEYWORDS alternative splicing; nonstructural protein SUMMARY #length 121 #molecular-weight 14279 #checksum 3314 SEQUENCE /// ENTRY E45539 #type complete TITLE nonstructural protein NS2 - influenza A virus (strain A/ chicken/Brescia/1902 [H7N7]) ORGANISM #formal_name influenza A virus DATE 24-Feb-1994 #sequence_revision 24-Feb-1994 #text_change 26-May-1994 ACCESSIONS E45539 REFERENCE A45539 !$#authors Klimov, A.; Prosch, S.; Schafer, J.; Bucher, D. !$#journal Arch. Virol. (1992) 122:143-161 !$#title Subtype H7 influenza viruses: comparative antigenic and !1molecular analysis of the HA-, M-, and NS-genes. !$#cross-references MUID:92109567; PMID:1530908 !$#accession E45539 !'##molecule_type genomic RNA !'##residues 1-121 ##label KLI !'##note sequence extracted from NCBI backbone (NCBIN:74250, !1NCBIP:74255) GENETICS !$#map_position segment 8 CLASSIFICATION #superfamily influenza virus nonstructural protein NS2 KEYWORDS alternative splicing SUMMARY #length 121 #molecular-weight 14334 #checksum 3774 SEQUENCE /// ENTRY MNIVB1 #type complete TITLE nonstructural protein NS2 - influenza A virus (strains A/ pintail/Alberta/268/78 and A/mallard/New York/6750/78) ORGANISM #formal_name influenza A virus DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 19-Oct-1995 ACCESSIONS B32662; D32662 REFERENCE A32662 !$#authors Treanor, J.J.; Snyder, M.H.; London, W.T.; Murphy, B.R. !$#journal Virology (1989) 171:1-9 !$#title The B allele of the NS gene of avian influenza viruses, but !1not the A allele, attenuates a human influenza A virus for !1squirrel monkeys. !$#cross-references MUID:89299445; PMID:2525836 !$#accession B32662 !'##molecule_type genomic RNA !'##residues 1-121 ##label TRE !'##experimental_source strain A/pintail/Alberta/268/78 !$#accession D32662 !'##molecule_type genomic RNA !'##residues 1-121 ##label TR2 !'##experimental_source strain A/mallard/New York/6750/78 GENETICS !$#gene NS2 !$#map_position segment 8 !$#introns 10/3 CLASSIFICATION #superfamily influenza virus nonstructural protein NS2 KEYWORDS alternative splicing; nonstructural protein SUMMARY #length 121 #molecular-weight 14285 #checksum 3895 SEQUENCE /// ENTRY MNIVB3 #type complete TITLE nonstructural protein NS2 - influenza A virus (strain A/ mallard/New York/6874/78) ORGANISM #formal_name influenza A virus DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 08-Apr-1994 ACCESSIONS F32662 REFERENCE A32662 !$#authors Treanor, J.J.; Snyder, M.H.; London, W.T.; Murphy, B.R. !$#journal Virology (1989) 171:1-9 !$#title The B allele of the NS gene of avian influenza viruses, but !1not the A allele, attenuates a human influenza A virus for !1squirrel monkeys. !$#cross-references MUID:89299445; PMID:2525836 !$#accession F32662 !'##molecule_type genomic RNA !'##residues 1-121 ##label TRE GENETICS !$#gene NS2 !$#map_position segment 8 !$#introns 10/3 CLASSIFICATION #superfamily influenza virus nonstructural protein NS2 KEYWORDS alternative splicing; nonstructural protein SUMMARY #length 121 #molecular-weight 14253 #checksum 4363 SEQUENCE /// ENTRY MNIVB4 #type complete TITLE nonstructural protein NS2 - influenza A virus (strain A/ pintail/Alberta/119/79) ORGANISM #formal_name influenza A virus DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 08-Apr-1994 ACCESSIONS H32662 REFERENCE A32662 !$#authors Treanor, J.J.; Snyder, M.H.; London, W.T.; Murphy, B.R. !$#journal Virology (1989) 171:1-9 !$#title The B allele of the NS gene of avian influenza viruses, but !1not the A allele, attenuates a human influenza A virus for !1squirrel monkeys. !$#cross-references MUID:89299445; PMID:2525836 !$#accession H32662 !'##molecule_type genomic RNA !'##residues 1-121 ##label TRE GENETICS !$#gene NS2 !$#map_position segment 8 !$#introns 10/3 CLASSIFICATION #superfamily influenza virus nonstructural protein NS2 KEYWORDS alternative splicing; nonstructural protein SUMMARY #length 121 #molecular-weight 14294 #checksum 3672 SEQUENCE /// ENTRY MNIVX4 #type fragment TITLE nonstructural protein NS2 - influenza A virus (strain A/ Duck/England/56 [H11N6]) (fragment) ORGANISM #formal_name influenza A virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS D27846 REFERENCE A94361 !$#authors Nakajima, K.; Nobusawa, E.; Ogawa, T.; Nakajima, S. !$#journal Virology (1987) 158:465-468 !$#title Genetic divergence of the NS genes of avian influenza !1viruses. !$#cross-references MUID:87236215; PMID:2954302 !$#accession D27846 !'##molecule_type genomic RNA !'##residues 1-118 ##label NAK !'##cross-references GB:M16563; NID:g324786; PIDN:AAA43511.1; !1PID:g324788 GENETICS !$#gene NS2 !$#map_position segment 8 !$#introns 7/3 CLASSIFICATION #superfamily influenza virus nonstructural protein NS2 KEYWORDS alternative splicing; nonstructural protein SUMMARY #length 118 #checksum 4195 SEQUENCE /// ENTRY MNIVXX #type fragment TITLE nonstructural protein NS2 - influenza A virus (strain A/ Mynah/Haneda-Thai/76 [H3N1]) (fragment) ORGANISM #formal_name influenza A virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS A30086 REFERENCE A94361 !$#authors Nakajima, K.; Nobusawa, E.; Ogawa, T.; Nakajima, S. !$#journal Virology (1987) 158:465-468 !$#title Genetic divergence of the NS genes of avian influenza !1viruses. !$#cross-references MUID:87236215; PMID:2954302 !$#accession A30086 !'##molecule_type genomic RNA !'##residues 1-118 ##label NAK !'##cross-references GB:M17070; NID:g324854; PIDN:AAA43549.1; !1PID:g324856 GENETICS !$#gene NS2 !$#map_position segment 8 !$#introns 7/3 CLASSIFICATION #superfamily influenza virus nonstructural protein NS2 KEYWORDS alternative splicing; nonstructural protein SUMMARY #length 118 #checksum 3318 SEQUENCE /// ENTRY MNIVX8 #type fragment TITLE nonstructural protein NS2 - influenza A virus (strain A/ Duck/Ukraine/63 [H3N8]) (fragment) ORGANISM #formal_name influenza A virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS H27846 REFERENCE A94361 !$#authors Nakajima, K.; Nobusawa, E.; Ogawa, T.; Nakajima, S. !$#journal Virology (1987) 158:465-468 !$#title Genetic divergence of the NS genes of avian influenza !1viruses. !$#cross-references MUID:87236215; PMID:2954302 !$#accession H27846 !'##molecule_type genomic RNA !'##residues 1-118 ##label NAK !'##cross-references GB:M16565; NID:g324789; PIDN:AAA43513.1; !1PID:g324791 GENETICS !$#gene NS2 !$#map_position segment 8 !$#introns 7/3 CLASSIFICATION #superfamily influenza virus nonstructural protein NS2 KEYWORDS alternative splicing; nonstructural protein SUMMARY #length 118 #checksum 3555 SEQUENCE /// ENTRY MNIV2 #type complete TITLE nonstructural protein NS2 - influenza A virus (strain A/PR/ 8/34) ORGANISM #formal_name influenza A virus DATE 30-Apr-1981 #sequence_revision 30-Apr-1981 #text_change 16-Jul-1999 ACCESSIONS A04096 REFERENCE A93714 !$#authors Baez, M.; Taussig, R.; Zazra, J.J.; Young, J.F.; Palese, P.; !1Reisfeld, A.; Skalka, A.M. !$#journal Nucleic Acids Res. (1980) 8:5845-5858 !$#title Complete nucleotide sequence of the influenza A/PR/8/34 !1virus NS gene and comparison with the NS genes of the A/ !1Udorn/72 and A/FPV/Rostock/34 strains. !$#cross-references MUID:81124304; PMID:7465426 !$#accession A04096 !'##molecule_type genomic RNA !'##residues 1-121 ##label BAE !'##cross-references GB:V01104; NID:g60803; PIDN:CAA24293.1; PID:g60805 GENETICS !$#map_position segment 8 CLASSIFICATION #superfamily influenza virus nonstructural protein NS2 KEYWORDS alternative splicing SUMMARY #length 121 #molecular-weight 14380 #checksum 3121 SEQUENCE /// ENTRY MNIV2F #type complete TITLE nonstructural protein NS2 - influenza A virus ORGANISM #formal_name influenza A virus DATE 31-Oct-1980 #sequence_revision 31-Oct-1980 #text_change 16-Jul-1999 ACCESSIONS A04097 REFERENCE A93858 !$#authors Porter, A.G.; Smith, J.C.; Emtage, J.S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1980) 77:5074-5078 !$#title Nucleotide sequence of influenza virus RNA segment 8 !1indicates that coding regions for NS-1 and NS-2 proteins !1overlap. !$#cross-references MUID:81054909; PMID:6254054 !$#accession A04097 !'##molecule_type mRNA !'##residues 1-108 ##label POR !'##cross-references GB:V01100; NID:g60791; PIDN:CAA24285.1; PID:g60793 CLASSIFICATION #superfamily influenza virus nonstructural protein NS2 KEYWORDS alternative splicing SUMMARY #length 108 #molecular-weight 12884 #checksum 8588 SEQUENCE /// ENTRY MNIV26 #type complete TITLE nonstructural protein NS2 - influenza A virus (strains A/ duck/Alberta/60/76 and A/turkey/Oregon/71 [H7N5]) ORGANISM #formal_name influenza A virus DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 16-Jul-1999 ACCESSIONS A04098; B27529 REFERENCE A04092 !$#authors Baez, M.; Zazra, J.J.; Elliott, R.M.; Young, J.F.; Palese, !1P. !$#journal Virology (1981) 113:397-402 !$#title Nucleotide sequence of the influenza A/duck/Alberta/60/76 !1virus NS RNA: conservation of the NS1/NS2 overlapping gene !1structure in a divergent influenza virus RNA segment. !$#cross-references MUID:81276929; PMID:6927848 !$#accession A04098 !'##molecule_type genomic RNA !'##residues 1-121 ##label BAE !'##cross-references GB:J02105; GB:M17071; NID:g324783; PIDN:AAA43508.1; !1PID:g324784 !'##experimental_source strain A/duck/Alberta/60/76 REFERENCE A27529 !$#authors Norton, G.P.; Tanaka, T.; Tobita, K.; Nakada, S.; !1Buonagurio, D.A.; Greenspan, D.; Krystal, M.; Palese, P. !$#journal Virology (1987) 156:204-213 !$#title Infectious influenza A and B virus variants with long !1carboxyl terminal deletions in the NS1 polypeptides. !$#cross-references MUID:87122162; PMID:3811235 !$#accession B27529 !'##molecule_type genomic RNA !'##residues 1-121 ##label NOR !'##experimental_source strain A/turkey/Oregon/71 [H7N5] GENETICS !$#map_position segment 8 CLASSIFICATION #superfamily influenza virus nonstructural protein NS2 KEYWORDS alternative splicing; nonstructural protein SUMMARY #length 121 #molecular-weight 14287 #checksum 4655 SEQUENCE /// ENTRY MNIVB5 #type complete TITLE nonstructural protein NS2 - influenza A virus (strain A/ mallard/Alberta/88/76) ORGANISM #formal_name influenza A virus DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 08-Apr-1994 ACCESSIONS B32663 REFERENCE A32662 !$#authors Treanor, J.J.; Snyder, M.H.; London, W.T.; Murphy, B.R. !$#journal Virology (1989) 171:1-9 !$#title The B allele of the NS gene of avian influenza viruses, but !1not the A allele, attenuates a human influenza A virus for !1squirrel monkeys. !$#cross-references MUID:89299445; PMID:2525836 !$#accession B32663 !'##molecule_type genomic RNA !'##residues 1-121 ##label TRE GENETICS !$#gene NS2 !$#map_position segment 8 !$#introns 10/3 CLASSIFICATION #superfamily influenza virus nonstructural protein NS2 KEYWORDS alternative splicing; nonstructural protein SUMMARY #length 121 #molecular-weight 14261 #checksum 4575 SEQUENCE /// ENTRY MNIVB6 #type complete TITLE nonstructural protein NS2 - influenza A virus (strain A/ mallard/Alberta/827/78) ORGANISM #formal_name influenza A virus DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 08-Apr-1994 ACCESSIONS D32663 REFERENCE A32662 !$#authors Treanor, J.J.; Snyder, M.H.; London, W.T.; Murphy, B.R. !$#journal Virology (1989) 171:1-9 !$#title The B allele of the NS gene of avian influenza viruses, but !1not the A allele, attenuates a human influenza A virus for !1squirrel monkeys. !$#cross-references MUID:89299445; PMID:2525836 !$#accession D32663 !'##molecule_type genomic RNA !'##residues 1-121 ##label TRE GENETICS !$#gene NS2 !$#map_position segment 8 !$#introns 10/3 CLASSIFICATION #superfamily influenza virus nonstructural protein NS2 KEYWORDS alternative splicing; nonstructural protein SUMMARY #length 121 #molecular-weight 14303 #checksum 4536 SEQUENCE /// ENTRY MNIVB7 #type complete TITLE nonstructural protein NS2 - influenza A virus (strain A/ pintail/Alberta/121/79) ORGANISM #formal_name influenza A virus DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 08-Apr-1994 ACCESSIONS F32663 REFERENCE A32662 !$#authors Treanor, J.J.; Snyder, M.H.; London, W.T.; Murphy, B.R. !$#journal Virology (1989) 171:1-9 !$#title The B allele of the NS gene of avian influenza viruses, but !1not the A allele, attenuates a human influenza A virus for !1squirrel monkeys. !$#cross-references MUID:89299445; PMID:2525836 !$#accession F32663 !'##molecule_type genomic RNA !'##residues 1-121 ##label TRE GENETICS !$#gene NS2 !$#map_position segment 8 !$#introns 10/3 CLASSIFICATION #superfamily influenza virus nonstructural protein NS2 KEYWORDS alternative splicing; nonstructural protein SUMMARY #length 121 #molecular-weight 14260 #checksum 3926 SEQUENCE /// ENTRY MNIVB8 #type complete TITLE nonstructural protein NS2 - influenza A virus (strain A/ pintail/Alberta/358/79) ORGANISM #formal_name influenza A virus DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 08-Apr-1994 ACCESSIONS H32663 REFERENCE A32662 !$#authors Treanor, J.J.; Snyder, M.H.; London, W.T.; Murphy, B.R. !$#journal Virology (1989) 171:1-9 !$#title The B allele of the NS gene of avian influenza viruses, but !1not the A allele, attenuates a human influenza A virus for !1squirrel monkeys. !$#cross-references MUID:89299445; PMID:2525836 !$#accession H32663 !'##molecule_type genomic RNA !'##residues 1-121 ##label TRE GENETICS !$#gene NS2 !$#map_position segment 8 !$#introns 10/3 CLASSIFICATION #superfamily influenza virus nonstructural protein NS2 KEYWORDS alternative splicing; nonstructural protein SUMMARY #length 121 #molecular-weight 14233 #checksum 5267 SEQUENCE /// ENTRY MNIVX2 #type fragment TITLE nonstructural protein NS2 - influenza A virus (strain A/ Chicken/Japan/24 [H7N7]) (fragment) ORGANISM #formal_name influenza A virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS B27846 REFERENCE A94361 !$#authors Nakajima, K.; Nobusawa, E.; Ogawa, T.; Nakajima, S. !$#journal Virology (1987) 158:465-468 !$#title Genetic divergence of the NS genes of avian influenza !1viruses. !$#cross-references MUID:87236215; PMID:2954302 !$#accession B27846 !'##molecule_type genomic RNA !'##residues 1-118 ##label NAK !'##cross-references GB:M16561; NID:g324777; PIDN:AAA43505.1; !1PID:g324779 GENETICS !$#gene NS2 !$#map_position segment 8 !$#introns 7/3 CLASSIFICATION #superfamily influenza virus nonstructural protein NS2 KEYWORDS alternative splicing; nonstructural protein SUMMARY #length 118 #checksum 3996 SEQUENCE /// ENTRY MNIVX6 #type fragment TITLE nonstructural protein NS2 - influenza A virus (strain A/ Tern/South Africa/61 [H5N3]) (fragment) ORGANISM #formal_name influenza A virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS F27846 REFERENCE A94361 !$#authors Nakajima, K.; Nobusawa, E.; Ogawa, T.; Nakajima, S. !$#journal Virology (1987) 158:465-468 !$#title Genetic divergence of the NS genes of avian influenza !1viruses. !$#cross-references MUID:87236215; PMID:2954302 !$#accession F27846 !'##molecule_type genomic RNA !'##residues 1-118 ##label NAK !'##cross-references GB:M16564; NID:g324875; PIDN:AAA43573.1; !1PID:g324877 GENETICS !$#gene NS2 !$#map_position segment 8 !$#introns 7/3 CLASSIFICATION #superfamily influenza virus nonstructural protein NS2 KEYWORDS alternative splicing; nonstructural protein SUMMARY #length 118 #checksum 4209 SEQUENCE /// ENTRY MNIVB #type complete TITLE nonstructural protein NS2 - influenza B virus (strain B/Lee/ 40) ORGANISM #formal_name influenza B virus DATE 05-Apr-1983 #sequence_revision 05-Apr-1983 #text_change 16-Jul-1999 ACCESSIONS A04099 REFERENCE A04093 !$#authors Briedis, D.J.; Lamb, R.A. !$#journal J. Virol. (1982) 42:186-193 !$#title Influenza B virus genome: sequences and structural !1organization of RNA segment 8 and the mRNAs coding for the !1NS-1 and NS-2 proteins. !$#cross-references MUID:82216985; PMID:6283137 !$#accession A04099 !'##molecule_type genomic RNA !'##residues 1-122 ##label BRI !'##cross-references GB:J02096; NID:g325254; PIDN:AAA43755.1; !1PID:g325255 GENETICS !$#map_position segment 8 CLASSIFICATION #superfamily influenza virus nonstructural protein NS2 KEYWORDS alternative splicing SUMMARY #length 122 #molecular-weight 14238 #checksum 9440 SEQUENCE /// ENTRY MNIV23 #type complete TITLE nonstructural protein NS2 - influenza B virus (strains B/ Yamagata/1/73 and B/Ann Arbor/1/66) ORGANISM #formal_name influenza B virus DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 24-Sep-1999 ACCESSIONS E27529; F30064 REFERENCE A27529 !$#authors Norton, G.P.; Tanaka, T.; Tobita, K.; Nakada, S.; !1Buonagurio, D.A.; Greenspan, D.; Krystal, M.; Palese, P. !$#journal Virology (1987) 156:204-213 !$#title Infectious influenza A and B virus variants with long !1carboxyl terminal deletions in the NS1 polypeptides. !$#cross-references MUID:87122162; PMID:3811235 !$#accession E27529 !'##molecule_type genomic RNA !'##residues 1-122 ##label NOR !'##cross-references GB:M16634; NID:g325248; PIDN:AAA43751.1; !1PID:g325249 !'##experimental_source strain B/Yamagata/1/73 REFERENCE A28604 !$#authors DeBorde, D.C.; Donabedian, A.M.; Herlocher, M.L.; Naeve, !1C.W.; Maassab, H.F. !$#journal Virology (1988) 163:429-443 !$#title Sequence comparison of wild-type and cold-adapted B/Ann !1Arbor/1/66 influenza virus genes. !$#cross-references MUID:88179548; PMID:3354202 !$#accession F30064 !'##molecule_type genomic RNA !'##residues 1-122 ##label DEB !'##cross-references GB:M20224; NID:g325251; PIDN:AAA43753.1; !1PID:g325252 !'##experimental_source strain B/Ann Arbor/1/66 GENETICS !$#map_position segment 8 !$#introns 11/3 CLASSIFICATION #superfamily influenza virus nonstructural protein NS2 KEYWORDS alternative splicing; nonstructural protein SUMMARY #length 122 #molecular-weight 14321 #checksum 9528 SEQUENCE /// ENTRY VGIVL4 #type complete TITLE NB glycoprotein - influenza B virus (strain B/Lee/40) ORGANISM #formal_name influenza B virus DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Jul-1999 ACCESSIONS A26026 REFERENCE A26026 !$#authors Shaw, M.W.; Choppin, P.W.; Lamb, R.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:4879-4883 !$#title A previously unrecognized influenza B virus glycoprotein !1from a bicistronic mRNA that also encodes the viral !1neuraminidase. !$#cross-references MUID:83273716; PMID:6308656 !$#accession A26026 !'##molecule_type mRNA !'##residues 1-100 ##label SHA !'##cross-references GB:J02095; NID:g325235; PIDN:AAA43748.1; !1PID:g325236 GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily influenza B virus NB glycoprotein KEYWORDS glycoprotein; transmembrane protein FEATURE !$3,7,48,93 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 100 #molecular-weight 11024 #checksum 7767 SEQUENCE /// ENTRY VGIVB1 #type complete TITLE NB glycoprotein - influenza B virus (strain B/Beijing/1/87) ORGANISM #formal_name influenza B virus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS A38520 REFERENCE A38520 !$#authors Burmeister, W.P.; Daniels, R.S.; Dayan, S.; Gagnon, J.; !1Cusack, S.; Ruigrok, R.W.H. !$#journal Virology (1991) 180:266-272 !$#title Sequence and crystallization of influenza virus B/Beijing/1/ !187 neuraminidase. !$#cross-references MUID:91082418; PMID:1984652 !$#accession A38520 !'##molecule_type mRNA !'##residues 1-99 ##label BUR !'##cross-references GB:M54967; NID:g325211; PIDN:AAA43732.1; !1PID:g325212 GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily influenza B virus NB glycoprotein KEYWORDS glycoprotein; transmembrane protein FEATURE !$3,7,47,92 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 99 #molecular-weight 10892 #checksum 5399 SEQUENCE /// ENTRY A36825 #type complete TITLE NB glycoprotein - influenza B virus (strain B/Memphis/3/89) ORGANISM #formal_name influenza B virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS A36825 REFERENCE A46347 !$#authors Air, G.M.; Laver, W.G.; Luo, M.; Stray, S.J.; Legrone, G.; !1Webster, R.G. !$#journal Virology (1990) 177:578-587 !$#title Antigenic, sequence, and crystal variation in influenza B !1neuraminidase. !$#cross-references MUID:90320130; PMID:1695410 !$#accession A36825 !'##molecule_type genomic RNA !'##residues 1-99 ##label AIR !'##cross-references GB:M30635; NID:g325220; PIDN:AAA43738.1; !1PID:g325221 GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily influenza B virus NB glycoprotein KEYWORDS glycoprotein; transmembrane protein FEATURE !$3,7,47,92 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 99 #molecular-weight 10938 #checksum 5009 SEQUENCE /// ENTRY B36825 #type complete TITLE NB glycoprotein - influenza B virus (strain B/Memphis/6/86) ORGANISM #formal_name influenza B virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS B36825 REFERENCE A46347 !$#authors Air, G.M.; Laver, W.G.; Luo, M.; Stray, S.J.; Legrone, G.; !1Webster, R.G. !$#journal Virology (1990) 177:578-587 !$#title Antigenic, sequence, and crystal variation in influenza B !1neuraminidase. !$#cross-references MUID:90320130; PMID:1695410 !$#accession B36825 !'##molecule_type genomic RNA !'##residues 1-99 ##label AIR !'##cross-references GB:M30634; NID:g325217; PIDN:AAA43736.1; !1PID:g325218 GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily influenza B virus NB glycoprotein KEYWORDS glycoprotein; transmembrane protein FEATURE !$3,7,47,92 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 99 #molecular-weight 10914 #checksum 5823 SEQUENCE /// ENTRY C36825 #type complete TITLE NB glycoprotein - influenza B virus (strain B/Leningrad/179/ 86) ORGANISM #formal_name influenza B virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Feb-1997 ACCESSIONS C36825 REFERENCE A46347 !$#authors Air, G.M.; Laver, W.G.; Luo, M.; Stray, S.J.; Legrone, G.; !1Webster, R.G. !$#journal Virology (1990) 177:578-587 !$#title Antigenic, sequence, and crystal variation in influenza B !1neuraminidase. !$#cross-references MUID:90320130; PMID:1695410 !$#accession C36825 !'##molecule_type genomic RNA !'##residues 1-99 ##label AIR !'##cross-references GB:M30632 GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily influenza B virus NB glycoprotein KEYWORDS glycoprotein; transmembrane protein FEATURE !$3,7,47 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 99 #molecular-weight 10910 #checksum 6262 SEQUENCE /// ENTRY D36825 #type complete TITLE NB glycoprotein - influenza B virus (strain B/Victoria/3/85) ORGANISM #formal_name influenza B virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS D36825 REFERENCE A46347 !$#authors Air, G.M.; Laver, W.G.; Luo, M.; Stray, S.J.; Legrone, G.; !1Webster, R.G. !$#journal Virology (1990) 177:578-587 !$#title Antigenic, sequence, and crystal variation in influenza B !1neuraminidase. !$#cross-references MUID:90320130; PMID:1695410 !$#accession D36825 !'##molecule_type genomic RNA !'##residues 1-99 ##label AIR !'##cross-references GB:M30639; NID:g325232; PIDN:AAA43746.1; !1PID:g325233 GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily influenza B virus NB glycoprotein KEYWORDS glycoprotein; transmembrane protein FEATURE !$3,7,47,92 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 99 #molecular-weight 10895 #checksum 5263 SEQUENCE /// ENTRY E36825 #type complete TITLE NB glycoprotein - influenza B virus (strain B/USSR/100/83) ORGANISM #formal_name influenza B virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS E36825 REFERENCE A46347 !$#authors Air, G.M.; Laver, W.G.; Luo, M.; Stray, S.J.; Legrone, G.; !1Webster, R.G. !$#journal Virology (1990) 177:578-587 !$#title Antigenic, sequence, and crystal variation in influenza B !1neuraminidase. !$#cross-references MUID:90320130; PMID:1695410 !$#accession E36825 !'##molecule_type genomic RNA !'##residues 1-100 ##label AIR !'##cross-references GB:M30638; NID:g325229; PIDN:AAA43744.1; !1PID:g325230 GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily influenza B virus NB glycoprotein KEYWORDS glycoprotein; transmembrane protein FEATURE !$3,7,48,93 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 100 #molecular-weight 11001 #checksum 252 SEQUENCE /// ENTRY F36825 #type complete TITLE NB glycoprotein - influenza B virus (strain B/Oregon/5/80) ORGANISM #formal_name influenza B virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS F36825 REFERENCE A46347 !$#authors Air, G.M.; Laver, W.G.; Luo, M.; Stray, S.J.; Legrone, G.; !1Webster, R.G. !$#journal Virology (1990) 177:578-587 !$#title Antigenic, sequence, and crystal variation in influenza B !1neuraminidase. !$#cross-references MUID:90320130; PMID:1695410 !$#accession F36825 !'##molecule_type genomic RNA !'##residues 1-100 ##label AIR !'##cross-references GB:M30636; NID:g325223; PIDN:AAA43740.1; !1PID:g325224 GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily influenza B virus NB glycoprotein KEYWORDS glycoprotein; transmembrane protein FEATURE !$3,7,48,93 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 100 #molecular-weight 11005 #checksum 485 SEQUENCE /// ENTRY G36825 #type complete TITLE NB glycoprotein - influenza B virus (strain B/Singapore/222/ 79) ORGANISM #formal_name influenza B virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS G36825 REFERENCE A46347 !$#authors Air, G.M.; Laver, W.G.; Luo, M.; Stray, S.J.; Legrone, G.; !1Webster, R.G. !$#journal Virology (1990) 177:578-587 !$#title Antigenic, sequence, and crystal variation in influenza B !1neuraminidase. !$#cross-references MUID:90320130; PMID:1695410 !$#accession G36825 !'##molecule_type genomic RNA !'##residues 1-100 ##label AIR !'##cross-references GB:M30637; NID:g325226; PIDN:AAA43742.1; !1PID:g325227 GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily influenza B virus NB glycoprotein KEYWORDS glycoprotein; transmembrane protein FEATURE !$3,7,48,93 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 100 #molecular-weight 11027 #checksum 388 SEQUENCE /// ENTRY H36825 #type complete TITLE NB glycoprotein - influenza B virus (strain B/Hong Kong/8/ 73) ORGANISM #formal_name influenza B virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS H36825 REFERENCE A46347 !$#authors Air, G.M.; Laver, W.G.; Luo, M.; Stray, S.J.; Legrone, G.; !1Webster, R.G. !$#journal Virology (1990) 177:578-587 !$#title Antigenic, sequence, and crystal variation in influenza B !1neuraminidase. !$#cross-references MUID:90320130; PMID:1695410 !$#accession H36825 !'##molecule_type genomic RNA !'##residues 1-100 ##label AIR !'##cross-references GB:M30631; NID:g325205; PIDN:AAA43728.1; !1PID:g325206 GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily influenza B virus NB glycoprotein KEYWORDS glycoprotein; transmembrane protein FEATURE !$3,7,48,93 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 100 #molecular-weight 10981 #checksum 9026 SEQUENCE /// ENTRY I36825 #type complete TITLE NB glycoprotein - influenza B virus (strain B/Maryland/59) ORGANISM #formal_name influenza B virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Feb-1997 ACCESSIONS I36825 REFERENCE A46347 !$#authors Air, G.M.; Laver, W.G.; Luo, M.; Stray, S.J.; Legrone, G.; !1Webster, R.G. !$#journal Virology (1990) 177:578-587 !$#title Antigenic, sequence, and crystal variation in influenza B !1neuraminidase. !$#cross-references MUID:90320130; PMID:1695410 !$#accession I36825 !'##molecule_type genomic RNA !'##residues 1-100 ##label AIR !'##cross-references GB:M30633 GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily influenza B virus NB glycoprotein KEYWORDS glycoprotein; transmembrane protein FEATURE !$3,7,48,93 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 100 #molecular-weight 11098 #checksum 201 SEQUENCE /// ENTRY MNIVC7 #type complete TITLE nonstructural protein NS1 - influenza C virus (strain C/ California/78) ORGANISM #formal_name influenza C virus DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Jul-1999 ACCESSIONS A25320 REFERENCE A25320 !$#authors Nakada, S.; Graves, P.N.; Desselberger, U.; Creager, R.S.; !1Krystal, M.; Palese, P. !$#journal J. Virol. (1985) 56:221-226 !$#title Influenza C virus RNA 7 codes for a nonstructural protein. !$#cross-references MUID:85293225; PMID:4032535 !$#accession A25320 !'##molecule_type genomic RNA !'##residues 1-286 ##label NAK !'##cross-references EMBL:M10087; NID:g325301; PIDN:AAA43780.1; !1PID:g325302 GENETICS !$#gene NS !$#map_position segment 7 CLASSIFICATION #superfamily influenza C virus nonstructural protein NS1; !1influenza C virus nonstructural protein NS1/NS2 homology KEYWORDS alternative splicing; nonstructural protein FEATURE !$1-62 #domain influenza C virus nonstructural protein NS1/ !8NS2 homology #label NS1 SUMMARY #length 286 #molecular-weight 32486 #checksum 2908 SEQUENCE /// ENTRY S28883 #type complete TITLE nonstructural protein NS2 - influenza C virus (strain C/ California/78) ORGANISM #formal_name influenza C virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 18-Nov-1994 ACCESSIONS S28883 REFERENCE A25320 !$#authors Nakada, S.; Graves, P.N.; Desselberger, U.; Creager, R.S.; !1Krystal, M.; Palese, P. !$#journal J. Virol. (1985) 56:221-226 !$#title Influenza C virus RNA 7 codes for a nonstructural protein. !$#cross-references MUID:85293225; PMID:4032535 !$#accession S28883 !'##status translation not shown !'##molecule_type genomic RNA !'##residues 1-121 ##label NAK !'##cross-references EMBL:M10087 REFERENCE S07420 !$#authors Nakada, S.; Graves, P.N.; Palese, P. !$#journal Virus Res. (1986) 4:263-273 !$#title The influenza C virus NS gene: evidence for a spliced mRNA !1and a second NS gene product (NS2 protein). !$#cross-references MUID:86291553; PMID:2943090 !$#contents annotation; identification of NS2 GENETICS !$#introns 63/1 CLASSIFICATION #superfamily influenza C virus nonstructural protein NS2; !1influenza C virus nonstructural protein NS1/NS2 homology KEYWORDS alternative splicing; nonstructural protein FEATURE !$1-62 #domain influenza C virus nonstructural protein NS1/ !8NS2 homology #label NS1 SUMMARY #length 121 #molecular-weight 13829 #checksum 8663 SEQUENCE /// ENTRY QQIVE1 #type complete TITLE hypothetical 18K protein - influenza A virus (strain A/PR/8/ 34) ORGANISM #formal_name influenza A virus DATE 24-Sep-1981 #sequence_revision 24-Sep-1981 #text_change 17-Jul-1998 ACCESSIONS A04100 REFERENCE A93714 !$#authors Baez, M.; Taussig, R.; Zazra, J.J.; Young, J.F.; Palese, P.; !1Reisfeld, A.; Skalka, A.M. !$#journal Nucleic Acids Res. (1980) 8:5845-5858 !$#title Complete nucleotide sequence of the influenza A/PR/8/34 !1virus NS gene and comparison with the NS genes of the A/ !1Udorn/72 and A/FPV/Rostock/34 strains. !$#cross-references MUID:81124304; PMID:7465426 !$#accession A04100 !'##molecule_type genomic RNA !'##residues 1-167 ##label BAE !'##note this protein is coded by the negative strand (residues 793-293) !1of the NS gene CLASSIFICATION #superfamily influenza virus hypothetical 18K protein SUMMARY #length 167 #molecular-weight 18082 #checksum 5238 SEQUENCE /// ENTRY GNVUBW #type complete TITLE M polyprotein precursor - bunyamwera virus CONTAINS glycoprotein G1; glycoprotein G2; nonstructural protein ORGANISM #formal_name bunyamwera virus DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 16-Jul-1999 ACCESSIONS A04101 REFERENCE A04101 !$#authors Lees, J.F.; Pringle, C.R.; Elliott, R.M. !$#journal Virology (1986) 148:1-14 !$#title Nucleotide sequence of the Bunyamwera virus M RNA segment: !1conservation of structural features in the bunyavirus !1glycoprotein gene product. !$#cross-references MUID:86098655; PMID:3753629 !$#accession A04101 !'##molecule_type genomic RNA !'##residues 1-1433 ##label LEE !'##cross-references GB:M11852; NID:g210743; PIDN:AAA42777.1; !1PID:g210744 COMMENT Specific enzymatic cleavages in vivo yield mature proteins !1including nonstructural protein NS-M, glycoprotein G1, and !1glycoprotein G2. However, exact cleavage sites are !1undetermined. GENETICS !$#map_position segment M CLASSIFICATION #superfamily bunyavirus M polyprotein KEYWORDS glycoprotein; nonstructural protein; polyprotein; !1transmembrane protein FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-1433 #product M polyprotein #status predicted #label MPP\ !$60,248,624,1169 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1433 #molecular-weight 162077 #checksum 1114 SEQUENCE /// ENTRY GNVUSV #type complete TITLE M polyprotein precursor - snowshoe hare virus CONTAINS glycoprotein G1; glycoprotein G2; nonstructural protein ORGANISM #formal_name snowshoe hare virus DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 16-Jul-1999 ACCESSIONS A04102; A31826 REFERENCE A04102 !$#authors Eshita, Y.; Bishop, D.H.L. !$#journal Virology (1984) 137:227-240 !$#title The complete sequence of the M RNA of snowshoe hare !1bunyavirus reveals the presence of internal hydrophobic !1domains in the viral glycoprotein. !$#cross-references MUID:85018241; PMID:6091326 !$#accession A04102 !'##molecule_type genomic RNA !'##residues 1-1441 ##label ESH !'##cross-references GB:K02539; NID:g335025; PIDN:AAA47827.1; !1PID:g335026 REFERENCE A31826 !$#authors Fazakerley, J.K.; Gonzalez-Scarano, F.; Strickler, J.; !1Dietzschold, B.; Karush, F.; Nathanson, N. !$#journal Virology (1988) 167:422-432 !$#title Organization of the middle RNA segment of snowshoe hare !1bunyavirus. !$#cross-references MUID:89073745; PMID:2974218 !$#accession A31826 !'##molecule_type protein !'##residues 'X',15-19,'X',21-23;295-299;474,'XX',477-478,'XXX',482-483, !1'DX',486-488;'XL',764-771 ##label FAZ !'##note boundaries of the mature proteins were determined GENETICS !$#map_position segment M CLASSIFICATION #superfamily bunyavirus M polyprotein KEYWORDS glycoprotein; nonstructural protein; polyprotein FEATURE !$1-13 #domain signal sequence #status predicted #label SIG\ !$14-299 #product glycoprotein G2 #status experimental #label !8GG2\ !$300-473 #product nonstructural protein NS-M #status predicted !8#label NSM\ !$474-1441 #product glycoprotein G1 #status experimental #label !8GG1\ !$30,57,245,490,1177 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1441 #molecular-weight 162389 #checksum 6040 SEQUENCE /// ENTRY GNVULC #type complete TITLE M polyprotein precursor - La Crosse virus (isolate 74-32813) CONTAINS glycoprotein G1; glycoprotein G2; nonstructural protein NS-M ORGANISM #formal_name La Crosse virus DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 05-Jan-1996 ACCESSIONS A29377 REFERENCE A29377 !$#authors Grady, L.J.; Sanders, M.L.; Campbell, W.P. !$#journal J. Gen. Virol. (1987) 68:3057-3071 !$#title The sequence of the M RNA of an isolate of La Crosse virus. !$#cross-references MUID:88089508; PMID:3694177 !$#accession A29377 !'##molecule_type mRNA !'##residues 1-1441 ##label GRA !'##note the authors translated the codon GCC for residue 164 as Gly COMMENT Specific enzymatic cleavages in vivo yield mature proteins !1including nonstructural protein NS-M, glycoprotein G1, and !1glycoprotein G2. However, exact cleavage sites are !1undetermined. GENETICS !$#map_position segment M CLASSIFICATION #superfamily bunyavirus M polyprotein KEYWORDS glycoprotein; nonstructural protein; polyprotein FEATURE !$1-13 #domain signal sequence #status predicted #label SIG\ !$14-1441 #product M polyprotein #status predicted #label MPP\ !$30,57,245,490,1177 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1441 #molecular-weight 162540 #checksum 6648 SEQUENCE /// ENTRY GNVUHV #type complete TITLE M polyprotein - Hantaan virus CONTAINS glycoprotein G1; glycoprotein G2 ORGANISM #formal_name Hantaan virus DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 22-Oct-1999 ACCESSIONS A26348; JS0245 REFERENCE A26348 !$#authors Schmaljohn, C.S.; Schmaljohn, A.L.; Dalrymple, J.M. !$#journal Virology (1987) 157:31-39 !$#title Hantaan virus M RNA: coding strategy, nucleotide sequence, !1and gene order. !$#cross-references MUID:87151118; PMID:3103329 !$#accession A26348 !'##molecule_type mRNA !'##residues 1-1135 ##label SCH !'##cross-references GB:M14627; NID:g325412; PIDN:AAA43836.1; !1PID:g325413 REFERENCE JS0245 !$#authors Schmaljohn, C.S.; Arikawa, J.; Hasty, S.E.; Rasmussen, L.; !1Lee, H.W.; Lee, P.W.; Dalrymple, J.M. !$#journal J. Gen. Virol. (1988) 69:1949-1955 !$#title Conservation of antigenic properties and sequence encoding !1the envelope proteins of prototype Hantaan virus and two !1virus isolates from Korean haemorrhagic fever patients. !$#cross-references MUID:88299956; PMID:2900289 !$#accession JS0245 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type mRNA !'##residues 1-48,'M',50-56,'L',58-63,'S',65-125,'I',127-172,'T', !1174-288,'T',290,'T',292-315,'F',317-353,'G',355-358,'M', !1360-365,'V',367,'R',369-370,'DGI',374-375,'F',377-428,'V', !1430-500,'V',502-506,'AI',509-666,'I',668-696,698-785,'R', !1787-862,'R',864-1043,'K',1045-1052,'PN',1055-1076,'E', !11078-1135 ##label SC2 !'##experimental_source isolate Hojo !'##note only a list of differences from sequence A26348 is shown in !1this paper COMMENT The genome consists of three linear, negative, !1single-stranded RNA segments designated large (L), medium !1(M), and small (S) RNA. This protein is coded by M RNA. GENETICS !$#map_position segment M CLASSIFICATION #superfamily Hantaan virus M polyprotein KEYWORDS glycoprotein; polyprotein FEATURE !$18-648 #product glycoprotein G1 #status predicted #label !8GP1\ !$649-1135 #product glycoprotein G2 #status predicted #label !8GP2\ !$134,235,347,399, !$609,766,928 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1135 #molecular-weight 126420 #checksum 9914 SEQUENCE /// ENTRY GNVUH7 #type complete TITLE M polyprotein - Hantaan virus (strain 76-118) CONTAINS glycoprotein G1; glycoprotein G2 ORGANISM #formal_name Hantaan virus DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 16-Jul-1999 ACCESSIONS A29382 REFERENCE A29382 !$#authors Yoo, D.; Kang, C.Y. !$#journal Nucleic Acids Res. (1987) 15:6299-6300 !$#title Nucleotide sequence of the M segment of the genomic RNA of !1Hantaan virus 76-118. !$#cross-references MUID:87316891; PMID:3114716 !$#accession A29382 !'##molecule_type mRNA !'##residues 1-1135 ##label YOO !'##cross-references GB:Y00386; NID:g58763; PIDN:CAA68456.1; PID:g58764 !'##note the authors translated the codon ATT for residue 501 as Leu GENETICS !$#map_position segment M CLASSIFICATION #superfamily Hantaan virus M polyprotein KEYWORDS glycoprotein; polyprotein FEATURE !$18-648 #product glycoprotein G1 #status predicted #label !8GG1\ !$649-1135 #product glycoprotein G2 #status predicted #label !8GG2\ !$134,235,347,399, !$609,766,928 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1135 #molecular-weight 126335 #checksum 25 SEQUENCE /// ENTRY GNVUSR #type complete TITLE M polyprotein precursor - Sapporo rat virus (strain SR-11) CONTAINS glycoprotein G1; glycoprotein G2 ORGANISM #formal_name Sapporo rat virus DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS B34601 REFERENCE A34601 !$#authors Arikawa, J.; Lapenotiere, H.F.; Iacono-Connors, L.; Wang, !1M.; Schmaljohn, C.S. !$#journal Virology (1990) 176:114-125 !$#title Coding properties of the S and the M genome segments of !1Sapporo rat virus: comparison to other causative agents of !1hemorrhagic fever with renal syndrome. !$#cross-references MUID:90232720; PMID:1970443 !$#accession B34601 !'##molecule_type genomic RNA !'##residues 1-1133 ##label ARI !'##cross-references GB:M34882; NID:g335017; PIDN:AAA47825.1; !1PID:g335018 GENETICS !$#map_position segment M CLASSIFICATION #superfamily Hantaan virus M polyprotein KEYWORDS glycoprotein; polyprotein; transmembrane protein FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-646 #product glycoprotein G1 #status predicted #label !8GG1\ !$647-1133 #product glycoprotein G2 #status predicted #label !8GG2\ !$132,233,345,397, !$560,926 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1133 #molecular-weight 125591 #checksum 1101 SEQUENCE /// ENTRY GNVU22 #type complete TITLE M polyprotein precursor - Seoul virus (strain R22) CONTAINS glycoprotein G1; glycoprotein G2 ORGANISM #formal_name Seoul virus #note host Homo sapiens (man) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 09-Sep-1994 ACCESSIONS JC1006 REFERENCE JC1006 !$#authors Shi, L.C.; Hang, C.S.; Li, D.X.; Yuan, J.S.; Jin, D.Y.; !1Song, G. !$#journal Chinese J. Virol. (1991) 7:295-302 !$#title Moleculal cloning and sequencing of the M genome segment of !1epidemic hemorrhagic fever virus R22 strain. !$#accession JC1006 !'##molecule_type genomic RNA !'##residues 1-1134 ##label SHI !'##note the source was designated as epidemic hemorrhagic fever virus GENETICS !$#map_position segment M CLASSIFICATION #superfamily Hantaan virus M polyprotein KEYWORDS glycoprotein; polyprotein; transmembrane protein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-647 #product glycoprotein G1 #status predicted #label !8G1P\ !$445-464 #domain transmembrane #status predicted #label TM1\ !$489-507 #domain transmembrane #status predicted #label TM2\ !$625-641 #domain transmembrane #status predicted #label TM3\ !$648-1134 #product glycoprotein G2 #status predicted #label !8G2P\ !$1106-1122 #domain transmembrane #status predicted #label TM4\ !$132,233,345,397, !$560,927 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1134 #molecular-weight 126319 #checksum 4238 SEQUENCE /// ENTRY A43964 #type complete TITLE M polyprotein precursor - Seoul virus (strain 80-39) CONTAINS glycoprotein G1; glycoprotein G2 ORGANISM #formal_name Seoul virus #note host Homo sapiens (man) DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jul-1999 ACCESSIONS A43964 REFERENCE A43964 !$#authors Antic, D.; Lim, B.U.; Kang, C.Y. !$#journal Virus Res. (1991) 19:47-58 !$#title Molecular characterization of the M genomic segment of the !1Seoul 80-39 virus; nucleotide and amino acid sequence !1comparisons with other hantaviruses reveal the evolutionary !1pathway. !$#cross-references MUID:91327730; PMID:1867009 !$#accession A43964 !'##molecule_type genomic RNA !'##residues 1-1133 ##label ANT !'##cross-references GB:S47716; NID:g1679997; PIDN:AAB19434.1; !1PID:g233373 !'##note sequence extracted from NCBI backbone (NCBIN:47716, !1NCBIP:47735) GENETICS !$#map_position segment M CLASSIFICATION #superfamily Hantaan virus M polyprotein KEYWORDS glycoprotein; polyprotein; transmembrane protein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-646 #product glycoprotein G1 #status predicted #label !8G1P\ !$444-461 #domain transmembrane #status predicted #label TM1\ !$485-504 #domain transmembrane #status predicted #label TM2\ !$625-646 #domain transmembrane #status predicted #label TM3\ !$647-1133 #product glycoprotein G2 #status predicted #label !8G2P\ !$1105-1121 #domain transmembrane #status predicted #label TM4\ !$132,233,345,397, !$560,926 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1133 #molecular-weight 125775 #checksum 2639 SEQUENCE /// ENTRY A43960 #type complete TITLE M polyprotein precursor - Hantaan virus (strain R22) CONTAINS glycoprotein G1; glycoprotein G2 ORGANISM #formal_name Hantaan virus #note host Rattus norvegicus (Norway rat) DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jul-1999 ACCESSIONS A43960 REFERENCE A43960 !$#authors Xu, X.A.; Ruo, S.L.; Tang, Y.W.; Fisher-Hoch, S.P.; !1McCormick, J.B. !$#journal Virus Res. (1991) 21:35-52 !$#title Molecular characterization and expression of glycoprotein !1gene of Hantavirus R22 strain isolated from Rattus !1norvegicus in China. !$#cross-references MUID:92074322; PMID:1962503 !$#accession A43960 !'##molecule_type genomic RNA !'##residues 1-1134 ##label XU1 !'##cross-references GB:S68035; NID:g239786; PIDN:AAB20470.1; !1PID:g239787 !'##note sequence extracted from NCBI backbone (NCBIN:68035, !1NCBIP:68036) GENETICS !$#map_position segment M CLASSIFICATION #superfamily Hantaan virus M polyprotein KEYWORDS glycoprotein; polyprotein; transmembrane protein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-646 #product glycoprotein G1 #status predicted #label !8G1P\ !$444-461 #domain transmembrane #status predicted #label TM1\ !$485-504 #domain transmembrane #status predicted #label TM2\ !$626-646 #domain transmembrane #status predicted #label TM3\ !$647-1134 #product glycoprotein G2 #status predicted #label !8G2P\ !$1106-1122 #domain transmembrane #status predicted #label TM4\ !$132,233,345,397, !$560,927 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1134 #molecular-weight 126367 #checksum 4238 SEQUENCE /// ENTRY GNVUNE #type complete TITLE M polyprotein precursor - Puumala virus (strain Hallnas B1) CONTAINS glycoprotein G1; glycoprotein G2 ORGANISM #formal_name Puumala virus DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 10-Sep-1999 ACCESSIONS A33077; A43963 REFERENCE A33077 !$#authors Giebel, L.B.; Stohwasser, R.; Zoeller, L.; Bautz, E.K.F.; !1Darai, G. !$#journal Virology (1989) 172:498-505 !$#title Determination of the coding capacity of the M genome segment !1of nephropathia epidemica virus strain Haellnaes B1 by !1molecular cloning and nucleotide sequence analysis. !$#cross-references MUID:90021180; PMID:2508317 !$#accession A33077 !'##molecule_type genomic RNA !'##residues 1-1148 ##label GIE !'##cross-references GB:M29979; NID:g333364 !'##note this translation is not annotated in GenBank entry PUUMSEG, !1release 111.0 REFERENCE A43963 !$#authors Antic, D.; Kang, C.Y.; Spik, K.; Schmaljohn, C.; Vapalahti, !1O.; Vaheri, A. !$#journal Virus Res. (1992) 24:35-46 !$#title Comparison of the deduced gene products of the L, M and S !1genome segments of hantaviruses. !$#cross-references MUID:92327838; PMID:1626424 !$#accession A43963 !'##status not compared with conceptual translation !'##molecule_type genomic RNA; protein !'##residues 1-538,'V',540-543,'K',545-590,'P',592-801,'KV',804-1148 !1##label ANT !'##cross-references PIDN:AAB22506.1; PID:g215348 !'##experimental_source Hallnas strain !'##note sequence extracted from NCBI backbone (NCBIP:108388) GENETICS !$#map_position segment M CLASSIFICATION #superfamily Hantaan virus M polyprotein KEYWORDS glycoprotein; polyprotein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-658 #product glycoprotein G1 #status predicted #label !8GG1\ !$659-1148 #product glycoprotein G2 #status predicted #label !8GG2\ !$142,357,409,585, !$898,937 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1148 #molecular-weight 126982 #checksum 4688 SEQUENCE /// ENTRY JQ1604 #type complete TITLE M polyprotein precursor - Puumala virus (strain Sotkamo) CONTAINS glycoprotein G1; glycoprotein G2 ORGANISM #formal_name Puumala virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jul-1999 ACCESSIONS JQ1604; S15718 REFERENCE JQ1604 !$#authors Vapalahti, O.; Kallio-Kokko, H.; Salonen, E.M.; !1Brummer-Korvenkontio, M.; Vaheri, A. !$#journal J. Gen. Virol. (1992) 73:829-838 !$#title Cloning and sequencing of Puumala virus Sotkamo strain S and !1M RNA segments: Evidence for strain variation in !1hantaviruses and expression of the nucleocapsid protein. !$#cross-references MUID:92341063; PMID:1353107 !$#accession JQ1604 !'##status nucleic acid sequence not shown !'##molecule_type genomic RNA !'##residues 1-1148 ##label VAP !'##cross-references EMBL:X61034; NID:g61383; PIDN:CAA43369.1; !1PID:g61384 !'##note the authors translated the codon ATG for residue 472 as Leu GENETICS !$#map_position segment M CLASSIFICATION #superfamily Hantaan virus M polyprotein KEYWORDS glycoprotein; polyprotein; transmembrane protein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-658 #product glycoprotein G1 #status predicted #label !8G1P\ !$456-473 #domain transmembrane #status predicted #label TM1\ !$497-516 #domain transmembrane #status predicted #label TM2\ !$637-658 #domain transmembrane #status predicted #label TM3\ !$659-1148 #product glycoprotein G2 #status predicted #label !8G2P\ !$1116-1132 #domain transmembrane #status predicted #label TM4\ !$142,357,409,898,937 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1148 #molecular-weight 126293 #checksum 286 SEQUENCE /// ENTRY GNVUPH #type complete TITLE M polyprotein precursor - Prospect Hill virus CONTAINS glycoprotein G1; glycoprotein G2 ORGANISM #formal_name Prospect Hill virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS JQ1380 REFERENCE JQ1380 !$#authors Parrington, M.A.; Lee, P.W.; Kang, Y. !$#journal J. Gen. Virol. (1991) 72:1845-1854 !$#title Molecular characterization of the Prospect Hill virus M RNA !1segment: a comparison with the M RNA segments of other !1hantaviruses. !$#cross-references MUID:91341470; PMID:1840609 !$#accession JQ1380 !'##molecule_type genomic RNA !'##residues 1-1142 ##label PAR !'##cross-references GB:X55129; NID:g61029; PIDN:CAA38922.1; PID:g61030 GENETICS !$#map_position segment M CLASSIFICATION #superfamily Hantaan virus M polyprotein KEYWORDS glycoprotein; polyprotein; transmembrane protein FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-654 #product glycoprotein G1 #status predicted #label !8GG1\ !$488-517 #domain transmembrane #status predicted #label TM1\ !$655-1142 #product glycoprotein G2 #status predicted #label !8GG2\ !$1111-1128 #domain transmembrane #status predicted #label TM2\ !$139,353,405,527, !$581,933 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1142 #molecular-weight 125685 #checksum 2612 SEQUENCE /// ENTRY GNVUUK #type complete TITLE glycoprotein precursor - Uukuniemi virus CONTAINS glycoprotein G1; glycoprotein G2 ORGANISM #formal_name Uukuniemi virus DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jul-1999 ACCESSIONS A28502 REFERENCE A28502 !$#authors Roennholm, R.; Pettersson, R.F. !$#journal Virology (1987) 160:191-202 !$#title Complete nucleotide sequence of the M RNA segment of !1Uukuniemi virus encoding the membrane glycoproteins G1 and !1G2. !$#cross-references MUID:87321102; PMID:3629974 !$#accession A28502 !'##molecule_type mRNA !'##residues 1-1008 ##label ROE !'##cross-references GB:M17417; NID:g335293; PIDN:AAA79512.1; !1PID:g335294 GENETICS !$#map_position segment M CLASSIFICATION #superfamily Uukuvirus glycoprotein KEYWORDS glycoprotein; polyprotein; transmembrane protein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-513 #product glycoprotein G1 #status predicted #label !8GG1\ !$397-415 #domain transmembrane #status predicted #label TM1\ !$497-513 #domain transmembrane #status predicted #label TM2\ !$514-1008 #product glycoprotein G2 #status predicted #label !8GG2\ !$977-1008 #domain transmembrane #status predicted #label TM3\ !$34,70,108,208,493, !$691,696,912,949 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1008 #molecular-weight 113571 #checksum 3134 SEQUENCE /// ENTRY VHVUNH #type complete TITLE nucleoprotein N - snowshoe hare virus ORGANISM #formal_name snowshoe hare virus DATE 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 30-Sep-1993 ACCESSIONS A04103 REFERENCE A93429 !$#authors Bishop, D.H.L.; Gould, K.G.; Akashi, H.; Clerx-van Haaster, !1C.M. !$#journal Nucleic Acids Res. (1982) 10:3703-3713 !$#title The complete sequence and coding content of snowshoe hare !1bunyavirus small (S) viral RNA species. !$#cross-references MUID:82274210; PMID:7050911 !$#accession A04103 !'##molecule_type genomic RNA !'##residues 1-235 ##label BIS !'##note this virus is a member of the California encephalitis serogroup !1of mosquito-transmitted viruses (genus Bunyavirus, family !1Bunyaviridae) COMMENT The genome consists of a large (L) RNA, a medium (M) RNA, !1and a small (S) RNA with polarities opposite to mRNA. This !1protein is encoded by the S RNA. CLASSIFICATION #superfamily bunyavirus nucleoprotein N SUMMARY #length 235 #molecular-weight 26770 #checksum 5346 SEQUENCE /// ENTRY VHVULV #type complete TITLE nucleoprotein N - La Crosse virus ORGANISM #formal_name La Crosse virus DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 16-Jul-1999 ACCESSIONS A04104 REFERENCE A92989 !$#authors Akashi, H.; Bishop, D.H.L. !$#journal J. Virol. (1983) 45:1155-1158 !$#title Comparison of the sequences and coding of La Crosse and !1snowshoe hare bunyavirus S RNA species. !$#cross-references MUID:83164355; PMID:6834480 !$#accession A04104 !'##molecule_type genomic RNA !'##residues 1-235 ##label AKA !'##cross-references GB:K00610; NID:g210760; PIDN:AAA42782.1; !1PID:g210761 GENETICS !$#map_position segment S CLASSIFICATION #superfamily bunyavirus nucleoprotein N KEYWORDS nucleoprotein SUMMARY #length 235 #molecular-weight 26530 #checksum 2640 SEQUENCE /// ENTRY VHVUMB #type complete TITLE nucleoprotein N - Maguari virus ALTERNATE_NAMES nucleocapsid protein N ORGANISM #formal_name Maguari virus DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jun-2000 ACCESSIONS A33076; JT0424 REFERENCE A33076 !$#authors Elliott, R.M.; McGregor, A. !$#journal Virology (1989) 171:516-524 !$#title Nucleotide sequence and expression of the small (S) RNA !1segment of Maguari bunyavirus. !$#cross-references MUID:89348010; PMID:2527439 !$#accession A33076 !'##molecule_type genomic RNA !'##residues 1-233 ##label ELL !'##cross-references GB:M28380; GB:D00380; NID:g601857; PIDN:AAA57147.1; !1PID:g601858 REFERENCE JT0421 !$#authors Elliott, R.M. !$#submission submitted to the EMBL Data Library, January 1989 !$#accession JT0424 !'##molecule_type genomic RNA !'##residues 1-233 ##label EL2 !'##cross-references GB:D13783; NID:g222091; PIDN:BAA02926.1; !1PID:g222092 GENETICS !$#map_position segment S CLASSIFICATION #superfamily bunyavirus nucleoprotein N KEYWORDS nucleocapsid; nucleoprotein SUMMARY #length 233 #molecular-weight 26427 #checksum 7283 SEQUENCE /// ENTRY VHVUBV #type complete TITLE nucleoprotein N - bunyamwera virus ALTERNATE_NAMES nucleocapsid protein N ORGANISM #formal_name bunyamwera virus DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jun-2000 ACCESSIONS A31365; JT0421 REFERENCE A31365 !$#authors Elliott, R.M. !$#journal J. Gen. Virol. (1989) 70:1281-1285 !$#title Nucleotide sequence analysis of the small (S) RNA segment of !1bunyamwera virus, the prototype of the family Bunyaviridae. !$#cross-references MUID:89279304; PMID:2732714 !$#accession A31365 !'##molecule_type genomic RNA !'##residues 1-233 ##label ELL !'##cross-references GB:D00353; NID:g221048; PIDN:BAA00261.1; !1PID:g221049 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1989 GENETICS !$#map_position segment S CLASSIFICATION #superfamily bunyavirus nucleoprotein N KEYWORDS nucleocapsid; nucleoprotein SUMMARY #length 233 #molecular-weight 26664 #checksum 7943 SEQUENCE /// ENTRY VHVUAV #type complete TITLE nucleoprotein N - aino virus ORGANISM #formal_name aino virus DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jul-1999 ACCESSIONS S07414 REFERENCE S07414 !$#authors Akashi, H.; Gay, M.; Ihara, T.; Bishop, D.H.L. !$#journal Virus Res. (1984) 1:51-63 !$#title Localized conserved regions of the S RNA gene products of !1bunyaviruses are revealed by sequence analyses of the Simbu !1serogroup Aino virus. !$#cross-references MUID:85170502; PMID:6532000 !$#accession S07414 !'##molecule_type genomic RNA !'##residues 1-233 ##label AKA !'##cross-references EMBL:M22011; NID:g210064; PIDN:AAA42543.1; !1PID:g210065 GENETICS !$#gene N !$#map_position segment S CLASSIFICATION #superfamily bunyavirus nucleoprotein N KEYWORDS nucleoprotein SUMMARY #length 233 #molecular-weight 26279 #checksum 2471 SEQUENCE /// ENTRY VHVUW1 #type complete TITLE nucleoprotein N - tomato spotted wilt virus (strain L3) ORGANISM #formal_name tomato spotted wilt virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 03-Feb-1994 ACCESSIONS JQ0955 REFERENCE JQ0954 !$#authors Maiss, E.; Ivanova, L.; Breyel, E.; Adam, G. !$#submission submitted to JIPID, January 1991 !$#description Cloning and sequencing of the S RNA from a Bulganan isolate !1of tomato spotted wilt virus. !$#accession JQ0955 !'##molecule_type mRNA !'##residues 1-258 ##label MAI GENETICS !$#gene N !$#map_position segment S CLASSIFICATION #superfamily tomato spotted wilt virus nucleoprotein N KEYWORDS nucleoprotein; RNA binding SUMMARY #length 258 #molecular-weight 28902 #checksum 6693 SEQUENCE /// ENTRY VHVUWC #type complete TITLE nucleoprotein N - tomato spotted wilt virus (isolate CPNH1) ALTERNATE_NAMES nucleocapsid protein N ORGANISM #formal_name tomato spotted wilt virus DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jun-2000 ACCESSIONS JQ0548 REFERENCE JQ0547 !$#authors de Haan, P.; Wagemakers, L.; Peters, D.; Goldbach, R. !$#journal J. Gen. Virol. (1990) 71:1001-1007 !$#title The S RNA segment of tomato spotted wilt virus has an !1ambisense character. !$#cross-references MUID:90264829; PMID:1693160 !$#accession JQ0548 !'##molecule_type genomic RNA !'##residues 1-258 ##label DEH !'##cross-references DDBJ:D00645; NID:g222685; PIDN:BAA00541.1; !1PID:g222687 GENETICS !$#gene N !$#map_position segment S CLASSIFICATION #superfamily tomato spotted wilt virus nucleoprotein N KEYWORDS nucleocapsid; nucleoprotein SUMMARY #length 258 #molecular-weight 28844 #checksum 6266 SEQUENCE /// ENTRY JQ1876 #type complete TITLE nucleoprotein N - tomato spotted wilt virus (strain SA-05) ALTERNATE_NAMES nucleocapsid protein N ORGANISM #formal_name tomato spotted wilt virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 07-May-1999 ACCESSIONS JQ1876 REFERENCE JQ1876 !$#authors de Avila, A.C.; de Haan, P.; Kormelink, R.; Resende, R.O.; !1Goldbach, R.W.; Peters, D. !$#journal J. Gen. Virol. (1993) 74:153-159 !$#title Classification of tospoviruses based on phylogeny of !1nucleoprotein gene sequences. !$#cross-references MUID:93155639; PMID:8429298 !$#accession JQ1876 !'##molecule_type genomic RNA !'##residues 1-258 ##label DEA GENETICS !$#gene N !$#map_position segment S CLASSIFICATION #superfamily tomato spotted wilt virus nucleoprotein N KEYWORDS nucleocapsid; nucleoprotein SUMMARY #length 258 #molecular-weight 28852 #checksum 5187 SEQUENCE /// ENTRY JQ1877 #type complete TITLE nucleoprotein N - tomato spotted wilt virus (strain BR-03) ALTERNATE_NAMES nucleocapsid protein N ORGANISM #formal_name tomato spotted wilt virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 07-May-1999 ACCESSIONS JQ1877 REFERENCE JQ1876 !$#authors de Avila, A.C.; de Haan, P.; Kormelink, R.; Resende, R.O.; !1Goldbach, R.W.; Peters, D. !$#journal J. Gen. Virol. (1993) 74:153-159 !$#title Classification of tospoviruses based on phylogeny of !1nucleoprotein gene sequences. !$#cross-references MUID:93155639; PMID:8429298 !$#accession JQ1877 !'##molecule_type genomic RNA !'##residues 1-258 ##label DEA GENETICS !$#gene N !$#map_position segment S CLASSIFICATION #superfamily tomato spotted wilt virus nucleoprotein N KEYWORDS nucleocapsid; nucleoprotein SUMMARY #length 258 #molecular-weight 28677 #checksum 3076 SEQUENCE /// ENTRY VHVUW2 #type complete TITLE nucleoprotein N - Impatiens necrotic spot virus ORGANISM #formal_name Impatiens necrotic spot virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jun-2000 ACCESSIONS JQ1333 REFERENCE JQ1333 !$#authors Law, M.D.; Speck, J.; Moyer, J.W. !$#journal J. Gen. Virol. (1991) 72:2597-2601 !$#title Nucleotide sequence of the 3' non-coding region and N gene !1of the S RNA of a serologically distinct tospovirus. !$#cross-references MUID:92013985; PMID:1840613 !$#accession JQ1333 !'##molecule_type genomic RNA !'##residues 1-262 ##label LAW !'##cross-references GB:D00914; NID:g221908; PIDN:BAA00760.1; !1PID:g221909 GENETICS !$#gene N !$#map_position segment S CLASSIFICATION #superfamily tomato spotted wilt virus nucleoprotein N KEYWORDS nucleoprotein SUMMARY #length 262 #molecular-weight 28777 #checksum 7966 SEQUENCE /// ENTRY VHVUHV #type complete TITLE nucleocapsid protein - Hantaan virus ORGANISM #formal_name Hantaan virus DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 16-Jul-1999 ACCESSIONS A25617 REFERENCE A25617 !$#authors Schmaljohn, C.S.; Jennings, G.B.; Hay, J.; Dalrymple, J.M. !$#journal Virology (1986) 155:633-643 !$#title Coding strategy of the S genome segment of Hantaan virus. !$#cross-references MUID:87071678; PMID:3024404 !$#accession A25617 !'##molecule_type mRNA !'##residues 1-429 ##label SCH !'##cross-references GB:M14626; NID:g325415; PIDN:AAA43837.1; !1PID:g325416 COMMENT The genome consists of three linear, negative, !1single-stranded RNA segments designated large (L), medium !1(M), and small (S) RNA. This protein is coded by S RNA. GENETICS !$#map_position segment S CLASSIFICATION #superfamily Hantaan virus nucleocapsid protein KEYWORDS nucleocapsid SUMMARY #length 429 #molecular-weight 48142 #checksum 4253 SEQUENCE /// ENTRY VHVUSR #type complete TITLE nucleocapsid protein N - Sapporo rat virus (strain SR-11) ALTERNATE_NAMES nucleoprotein N ORGANISM #formal_name Sapporo rat virus DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 24-Jul-1997 ACCESSIONS A34601 REFERENCE A34601 !$#authors Arikawa, J.; Lapenotiere, H.F.; Iacono-Connors, L.; Wang, !1M.; Schmaljohn, C.S. !$#journal Virology (1990) 176:114-125 !$#title Coding properties of the S and the M genome segments of !1Sapporo rat virus: comparison to other causative agents of !1hemorrhagic fever with renal syndrome. !$#cross-references MUID:90232720; PMID:1970443 !$#accession A34601 !'##molecule_type genomic RNA !'##residues 1-429 ##label ARI GENETICS !$#gene N !$#map_position segment S CLASSIFICATION #superfamily Hantaan virus nucleocapsid protein KEYWORDS nucleocapsid; nucleoprotein SUMMARY #length 429 #molecular-weight 48078 #checksum 3333 SEQUENCE /// ENTRY VHVUNE #type complete TITLE nucleocapsid protein - Puumala virus (strain Hallnas B1) ORGANISM #formal_name Puumala virus DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Jul-1999 ACCESSIONS A33773 REFERENCE A33773 !$#authors Stohwasser, R.; Giebel, L.B.; Zoeller, L.; Bautz, E.K.F.; !1Darai, G. !$#journal Virology (1990) 174:79-86 !$#title Molecular characterization of the RNA S segment of !1nephropathia epidemica virus strain Haellnaes B1. !$#cross-references MUID:90101400; PMID:2104684 !$#accession A33773 !'##molecule_type genomic RNA !'##residues 1-433 ##label STO !'##cross-references GB:M32750; NID:g333365; PIDN:AAA47116.1; !1PID:g333366 GENETICS !$#map_position segment S CLASSIFICATION #superfamily Hantaan virus nucleocapsid protein KEYWORDS nucleocapsid SUMMARY #length 433 #molecular-weight 49470 #checksum 6244 SEQUENCE /// ENTRY JQ1605 #type complete TITLE nucleocapsid protein - Puumala virus (strain Sotkamo) ORGANISM #formal_name Puumala virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jul-1999 ACCESSIONS JQ1605; S15719 REFERENCE JQ1604 !$#authors Vapalahti, O.; Kallio-Kokko, H.; Salonen, E.M.; !1Brummer-Korvenkontio, M.; Vaheri, A. !$#journal J. Gen. Virol. (1992) 73:829-838 !$#title Cloning and sequencing of Puumala virus Sotkamo strain S and !1M RNA segments: Evidence for strain variation in !1hantaviruses and expression of the nucleocapsid protein. !$#cross-references MUID:92341063; PMID:1353107 !$#accession JQ1605 !'##status nucleic acid sequence not shown !'##molecule_type genomic RNA !'##residues 1-433 ##label VAP !'##cross-references EMBL:X61035; NID:g61385; PIDN:CAA43370.1; !1PID:g61386 !'##experimental_source strain Sotkamo !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1991 GENETICS !$#map_position segment S CLASSIFICATION #superfamily Hantaan virus nucleocapsid protein KEYWORDS nucleocapsid SUMMARY #length 433 #molecular-weight 49451 #checksum 3396 SEQUENCE /// ENTRY VHVUPH #type complete TITLE nucleocapsid protein N - Prospect Hill virus (strain PHV-1) ALTERNATE_NAMES nucleoprotein N ORGANISM #formal_name Prospect Hill virus DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 24-Jul-1997 ACCESSIONS A34681 REFERENCE A34681 !$#authors Parrington, M.A.; Kang, C.Y. !$#journal Virology (1990) 175:167-175 !$#title Nucleotide sequence analysis of the S genomic segment of !1Prospect Hill virus: comparison with the prototype !1Hantavirus. !$#cross-references MUID:90177212; PMID:2309440 !$#accession A34681 !'##molecule_type genomic RNA !'##residues 1-433 ##label PAR GENETICS !$#gene N !$#map_position segment S CLASSIFICATION #superfamily Hantaan virus nucleocapsid protein KEYWORDS nucleocapsid; nucleoprotein SUMMARY #length 433 #molecular-weight 49005 #checksum 2420 SEQUENCE /// ENTRY VHVUDU #type complete TITLE nucleocapsid protein N - Dugbe virus (isolate ArD 44313) ALTERNATE_NAMES nucleoprotein N ORGANISM #formal_name Dugbe virus DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS A34748 REFERENCE A34748 !$#authors Ward, V.K.; Marriott, A.C.; El-Ghorr, A.A.; Nuttall, P.A. !$#journal Virology (1990) 175:518-524 !$#title Coding strategy of the S RNA segment of Dugbe virus !1(Nairovirus; Bunyaviridae). !$#cross-references MUID:90223997; PMID:2327076 !$#accession A34748 !'##molecule_type genomic RNA !'##residues 1-441 ##label WAR !'##cross-references GB:M25150; NID:g323682; PIDN:AAA42975.1; !1PID:g323683 GENETICS !$#gene N !$#map_position segment S CLASSIFICATION #superfamily Nairovirus nucleocapsid protein KEYWORDS nucleocapsid; nucleoprotein SUMMARY #length 441 #molecular-weight 49436 #checksum 5749 SEQUENCE /// ENTRY VHVUHJ #type complete TITLE nucleoprotein - Hazara virus (strain JC280) ALTERNATE_NAMES nucleoprotein N ORGANISM #formal_name Hazara virus DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS A42990 REFERENCE A42990 !$#authors Marriott, A.C.; Nuttall, P.A. !$#journal Virology (1992) 189:795-799 !$#title Comparison of the S RNA segments and nucleoprotein sequences !1of Crimean-Congo hemorrhagic fever, Hazara, and Dugbe !1viruses. !$#cross-references MUID:92351584; PMID:1641991 !$#accession A42990 !'##molecule_type genomic RNA !'##residues 1-485 ##label MAR !'##cross-references GB:M86624; NID:g325423; PIDN:AAA43842.1; !1PID:g325424 GENETICS !$#map_position segment S CLASSIFICATION #superfamily Nairovirus nucleocapsid protein KEYWORDS nucleocapsid; nucleoprotein SUMMARY #length 485 #molecular-weight 54185 #checksum 4954 SEQUENCE /// ENTRY VHVUCH #type complete TITLE nucleocapsid protein N - Crimean-Congo hemorrhagic virus (strain C68031) ALTERNATE_NAMES nucleoprotein N ORGANISM #formal_name Crimean-Congo hemorrhagic virus, CCHFV DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS B42990 REFERENCE A42990 !$#authors Marriott, A.C.; Nuttall, P.A. !$#journal Virology (1992) 189:795-799 !$#title Comparison of the S RNA segments and nucleoprotein sequences !1of Crimean-Congo hemorrhagic fever, Hazara, and Dugbe !1viruses. !$#cross-references MUID:92351584; PMID:1641991 !$#accession B42990 !'##molecule_type genomic RNA !'##residues 1-482 ##label MAR !'##cross-references GB:M86625; NID:g323278; PIDN:AAA42888.1; !1PID:g323279 GENETICS !$#map_position segment S CLASSIFICATION #superfamily Nairovirus nucleocapsid protein KEYWORDS nucleocapsid; nucleoprotein SUMMARY #length 482 #molecular-weight 53965 #checksum 9885 SEQUENCE /// ENTRY VHVUDH #type complete TITLE nucleoprotein - Dhori virus (strain Dhori/Indian/1313/61) ORGANISM #formal_name Dhori virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS A26800 REFERENCE A26800 !$#authors Fuller, F.J.; Freedman-Faulstich, E.Z.; Barnes, J.A. !$#journal Virology (1987) 160:81-87 !$#title Complete nucleotide sequence of the tick-borne, !1orthomyxo-like Dhori/Indian/1313/61 virus nucleoprotein !1gene. !$#cross-references MUID:87321128; PMID:2442888 !$#accession A26800 !'##molecule_type genomic RNA !'##residues 1-477 ##label FUL !'##cross-references GB:M17435; NID:g323666; PIDN:AAA42967.1; !1PID:g323667 GENETICS !$#map_position segment 5 CLASSIFICATION #superfamily Dhori virus nucleoprotein KEYWORDS nucleoprotein SUMMARY #length 477 #molecular-weight 53968 #checksum 1809 SEQUENCE /// ENTRY QQVUMB #type complete TITLE hypothetical 9.3K protein - Maguari virus ORGANISM #formal_name Maguari virus DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jun-2000 ACCESSIONS C33076; JT0426 REFERENCE A33076 !$#authors Elliott, R.M.; McGregor, A. !$#journal Virology (1989) 171:516-524 !$#title Nucleotide sequence and expression of the small (S) RNA !1segment of Maguari bunyavirus. !$#cross-references MUID:89348010; PMID:2527439 !$#accession C33076 !'##molecule_type genomic RNA !'##residues 1-75 ##label ELL !'##cross-references GB:M28380; GB:D00380; NID:g601857; PIDN:AAA57149.1; !1PID:g601860 REFERENCE JT0421 !$#authors Elliott, R.M. !$#submission submitted to the EMBL Data Library, January 1989 !$#accession JT0426 !'##molecule_type genomic RNA !'##residues 1-75 ##label EL2 !'##cross-references GB:D13783; NID:g222091; PIDN:BAA02928.1; !1PID:g222094 GENETICS !$#map_position segment S CLASSIFICATION #superfamily bunyavirus hypothetical 9.3K protein SUMMARY #length 75 #molecular-weight 9257 #checksum 2262 SEQUENCE /// ENTRY VHVUPT #type complete TITLE nucleocapsid protein N - Punta Toro virus ORGANISM #formal_name Punta Toro virus #note host (mosquito); Homo sapiens (man) DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 16-Jul-1999 ACCESSIONS A04107 REFERENCE A94334 !$#authors Ihara, T.; Akashi, H.; Bishop, D.H.L. !$#journal Virology (1984) 136:293-306 !$#title Novel coding strategy (ambisense genomic RNA) revealed by !1sequence analyses of Punta Toro phlebovirus S RNA. !$#cross-references MUID:84276006; PMID:6087547 !$#accession A04107 !'##molecule_type genomic RNA !'##residues 1-243 ##label IHA !'##cross-references GB:K02736; NID:g333348; PIDN:AAA47114.1; !1PID:g333349 CLASSIFICATION #superfamily Punta Toro virus nucleocapsid protein N KEYWORDS nucleocapsid SUMMARY #length 243 #molecular-weight 26911 #checksum 9627 SEQUENCE /// ENTRY VHVUTV #type complete TITLE nucleocapsid protein N - Toscana virus ORGANISM #formal_name Toscana virus #note host (mosquito); Homo sapiens (man) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS B38552 REFERENCE A38552 !$#authors Giorgi, C.; Accardi, L.; Nicoletti, L.; Gro, M.C.; Takehara, !1K.; Hilditch, C.; Morikawa, S.; Bishop, D.H.L. !$#journal Virology (1991) 180:738-753 !$#title Sequences and coding strategies of the S RNAs of Toscana and !1Rift Valley fever viruses compared to those of Punta Toro, !1Sicilian Sandfly fever, and Uukuniemi viruses. !$#cross-references MUID:91111992; PMID:1846496 !$#accession B38552 !'##molecule_type genomic RNA !'##residues 1-253 ##label GIO !'##cross-references GB:X53794; NID:g62201; PIDN:CAA37803.1; PID:g62203 GENETICS !$#map_position segment S CLASSIFICATION #superfamily Punta Toro virus nucleocapsid protein N KEYWORDS nucleocapsid SUMMARY #length 253 #molecular-weight 27704 #checksum 5369 SEQUENCE /// ENTRY VHVURV #type complete TITLE nucleocapsid protein N - Rift Valley fever virus ORGANISM #formal_name Rift Valley fever virus #note host (mosquito); Homo sapiens (man) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS D38552; S11744 REFERENCE A38552 !$#authors Giorgi, C.; Accardi, L.; Nicoletti, L.; Gro, M.C.; Takehara, !1K.; Hilditch, C.; Morikawa, S.; Bishop, D.H.L. !$#journal Virology (1991) 180:738-753 !$#title Sequences and coding strategies of the S RNAs of Toscana and !1Rift Valley fever viruses compared to those of Punta Toro, !1Sicilian Sandfly fever, and Uukuniemi viruses. !$#cross-references MUID:91111992; PMID:1846496 !$#accession D38552 !'##molecule_type genomic RNA !'##residues 1-245 ##label GIO !'##cross-references GB:X53771; NID:g61928; PIDN:CAA37789.1; PID:g61930 GENETICS !$#map_position segment S CLASSIFICATION #superfamily Punta Toro virus nucleocapsid protein N KEYWORDS nucleocapsid SUMMARY #length 245 #molecular-weight 27430 #checksum 89 SEQUENCE /// ENTRY VHVUUU #type complete TITLE nucleocapsid protein N - Uukuniemi virus (strain S23) ALTERNATE_NAMES nucleoprotein N ORGANISM #formal_name Uukuniemi virus DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS A33559 REFERENCE A33559 !$#authors Simons, J.F.; Hellman, U.; Pettersson, R.F. !$#journal J. Virol. (1990) 64:247-255 !$#title Uukuniemi virus S RNA segment: ambisense coding strategy, !1packaging of complementary strands into virions, and !1homology to members of the genus Phlebovirus. !$#cross-references MUID:90080128; PMID:2136709 !$#accession A33559 !'##molecule_type genomic RNA !'##residues 1-254 ##label SIM !'##cross-references GB:M33551; NID:g335295; PIDN:AAA47958.1; !1PID:g335296 GENETICS !$#gene N !$#map_position segment S CLASSIFICATION #superfamily Punta Toro virus nucleocapsid protein N KEYWORDS nucleocapsid; nucleoprotein SUMMARY #length 254 #molecular-weight 28508 #checksum 3156 SEQUENCE /// ENTRY VHVUSS #type complete TITLE nucleocapsid protein N - sandfly fever virus ALTERNATE_NAMES nucleoprotein N ORGANISM #formal_name sandfly fever virus DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 24-Jul-1997 ACCESSIONS A30180 REFERENCE A30180 !$#authors Marriott, A.C.; Ward, V.K.; Nuttall, P.A. !$#journal Virology (1989) 169:341-345 !$#title The S RNA segment of sandfly fever Sicilian virus: evidence !1for an ambisense genome. !$#cross-references MUID:89204905; PMID:2705301 !$#accession A30180 !'##molecule_type genomic RNA !'##residues 1-218 ##label MAR GENETICS !$#map_position segment S CLASSIFICATION #superfamily Punta Toro virus nucleocapsid protein N KEYWORDS nucleocapsid; nucleoprotein SUMMARY #length 218 #molecular-weight 24790 #checksum 2244 SEQUENCE /// ENTRY MNVUSH #type complete TITLE nonstructural protein NS - snowshoe hare virus ORGANISM #formal_name snowshoe hare virus DATE 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 30-Sep-1993 ACCESSIONS A04105 REFERENCE A93429 !$#authors Bishop, D.H.L.; Gould, K.G.; Akashi, H.; Clerx-van Haaster, !1C.M. !$#journal Nucleic Acids Res. (1982) 10:3703-3713 !$#title The complete sequence and coding content of snowshoe hare !1bunyavirus small (S) viral RNA species. !$#cross-references MUID:82274210; PMID:7050911 !$#accession A04105 !'##molecule_type genomic RNA !'##residues 1-92 ##label BIS !'##note this virus is a member of the California encephalitis serogroup !1of mosquito-transmitted viruses (genus Bunyavirus, family !1Bunyaviridae) COMMENT The genome consists of a large (L) RNA, a medium (M) RNA, !1and a small (S) RNA with polarities opposite to mRNA. This !1protein is encoded by the S RNA. CLASSIFICATION #superfamily bunyavirus nonstructural protein SUMMARY #length 92 #molecular-weight 10490 #checksum 8792 SEQUENCE /// ENTRY MNVULV #type complete TITLE nonstructural protein NS - La Crosse virus ORGANISM #formal_name La Crosse virus DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 16-Jul-1999 ACCESSIONS A04106 REFERENCE A92989 !$#authors Akashi, H.; Bishop, D.H.L. !$#journal J. Virol. (1983) 45:1155-1158 !$#title Comparison of the sequences and coding of La Crosse and !1snowshoe hare bunyavirus S RNA species. !$#cross-references MUID:83164355; PMID:6834480 !$#accession A04106 !'##molecule_type genomic RNA !'##residues 1-92 ##label AKA !'##cross-references GB:K00610; NID:g210760; PIDN:AAA42783.1; !1PID:g210762 GENETICS !$#map_position segment S CLASSIFICATION #superfamily bunyavirus nonstructural protein KEYWORDS nonstructural protein SUMMARY #length 92 #molecular-weight 10441 #checksum 731 SEQUENCE /// ENTRY MNVUMB #type complete TITLE nonstructural protein NS - Maguari virus ORGANISM #formal_name Maguari virus DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jun-2000 ACCESSIONS B33076; JT0425 REFERENCE A33076 !$#authors Elliott, R.M.; McGregor, A. !$#journal Virology (1989) 171:516-524 !$#title Nucleotide sequence and expression of the small (S) RNA !1segment of Maguari bunyavirus. !$#cross-references MUID:89348010; PMID:2527439 !$#accession B33076 !'##molecule_type genomic RNA !'##residues 1-101 ##label ELL !'##cross-references GB:M28380; GB:D00380; NID:g601857; PIDN:AAA57148.1; !1PID:g601859 REFERENCE JT0421 !$#authors Elliott, R.M. !$#submission submitted to the EMBL Data Library, January 1989 !$#accession JT0425 !'##molecule_type genomic RNA !'##residues 1-101 ##label EL2 !'##cross-references GB:D13783; NID:g222091; PIDN:BAA02927.1; !1PID:g222093 GENETICS !$#map_position segment S CLASSIFICATION #superfamily bunyavirus nonstructural protein KEYWORDS nonstructural protein SUMMARY #length 101 #molecular-weight 11099 #checksum 6939 SEQUENCE /// ENTRY MNVUBV #type complete TITLE nonstructural protein NS - bunyamwera virus ORGANISM #formal_name bunyamwera virus DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jun-2000 ACCESSIONS B31365; JT0422 REFERENCE A31365 !$#authors Elliott, R.M. !$#journal J. Gen. Virol. (1989) 70:1281-1285 !$#title Nucleotide sequence analysis of the small (S) RNA segment of !1bunyamwera virus, the prototype of the family Bunyaviridae. !$#cross-references MUID:89279304; PMID:2732714 !$#accession B31365 !'##molecule_type genomic RNA !'##residues 1-101 ##label ELL !'##cross-references GB:D00353; NID:g221048; PIDN:BAA00262.1; !1PID:g221050 REFERENCE JT0421 !$#authors Elliott, R.M. !$#submission submitted to the EMBL Data Library, January 1989 !$#accession JT0422 !'##molecule_type mRNA !'##residues 1-101 ##label EL2 GENETICS !$#map_position segment S CLASSIFICATION #superfamily bunyavirus nonstructural protein KEYWORDS nonstructural protein SUMMARY #length 101 #molecular-weight 11024 #checksum 6376 SEQUENCE /// ENTRY MNVUAV #type complete TITLE nonstructural protein NS-S - aino virus ORGANISM #formal_name aino virus DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jul-1999 ACCESSIONS S07943 REFERENCE S07414 !$#authors Akashi, H.; Gay, M.; Ihara, T.; Bishop, D.H.L. !$#journal Virus Res. (1984) 1:51-63 !$#title Localized conserved regions of the S RNA gene products of !1bunyaviruses are revealed by sequence analyses of the Simbu !1serogroup Aino virus. !$#cross-references MUID:85170502; PMID:6532000 !$#accession S07943 !'##molecule_type genomic RNA !'##residues 1-91 ##label AKA !'##cross-references EMBL:M22011; NID:g210064; PIDN:AAA42544.1; !1PID:g210066 GENETICS !$#map_position segment S CLASSIFICATION #superfamily bunyavirus nonstructural protein KEYWORDS nonstructural protein SUMMARY #length 91 #molecular-weight 10503 #checksum 7435 SEQUENCE /// ENTRY MNVUUU #type complete TITLE nonstructural protein NS-S - Uukuniemi virus (strain S23) ORGANISM #formal_name Uukuniemi virus DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS B33559 REFERENCE A33559 !$#authors Simons, J.F.; Hellman, U.; Pettersson, R.F. !$#journal J. Virol. (1990) 64:247-255 !$#title Uukuniemi virus S RNA segment: ambisense coding strategy, !1packaging of complementary strands into virions, and !1homology to members of the genus Phlebovirus. !$#cross-references MUID:90080128; PMID:2136709 !$#accession B33559 !'##molecule_type genomic RNA !'##residues 1-273 ##label SIM !'##cross-references GB:M33551; NID:g335295; PIDN:AAA47959.1; !1PID:g335297 GENETICS !$#gene NS-S !$#map_position segment S CLASSIFICATION #superfamily Uukuvirus nonstructural protein NS-S KEYWORDS nonstructural protein SUMMARY #length 273 #molecular-weight 32019 #checksum 8313 SEQUENCE /// ENTRY MNVUPT #type complete TITLE nonstructural protein NS - Punta Toro virus ORGANISM #formal_name Punta Toro virus #note host (mosquito); Homo sapiens (man) DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 16-Jul-1999 ACCESSIONS A04108 REFERENCE A94334 !$#authors Ihara, T.; Akashi, H.; Bishop, D.H.L. !$#journal Virology (1984) 136:293-306 !$#title Novel coding strategy (ambisense genomic RNA) revealed by !1sequence analyses of Punta Toro phlebovirus S RNA. !$#cross-references MUID:84276006; PMID:6087547 !$#accession A04108 !'##molecule_type genomic RNA !'##residues 1-250 ##label IHA !'##cross-references GB:K02736; NID:g333348; PIDN:AAA47115.1; !1PID:g333350 COMMENT This protein may be a transcriptase component. CLASSIFICATION #superfamily Punta Toro virus nonstructural protein NS KEYWORDS nonstructural protein SUMMARY #length 250 #molecular-weight 29097 #checksum 2788 SEQUENCE /// ENTRY MNVUSS #type complete TITLE nonstructural protein NS - sandfly fever virus ORGANISM #formal_name sandfly fever virus DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS B30180 REFERENCE A30180 !$#authors Marriott, A.C.; Ward, V.K.; Nuttall, P.A. !$#journal Virology (1989) 169:341-345 !$#title The S RNA segment of sandfly fever Sicilian virus: evidence !1for an ambisense genome. !$#cross-references MUID:89204905; PMID:2705301 !$#accession B30180 !'##molecule_type genomic RNA !'##residues 1-267 ##label MAR !'##cross-references GB:J04418; NID:g334033; PIDN:AAA47459.1; !1PID:g334035 GENETICS !$#map_position segment S CLASSIFICATION #superfamily Punta Toro virus nonstructural protein NS KEYWORDS nonstructural protein SUMMARY #length 267 #molecular-weight 30379 #checksum 5420 SEQUENCE /// ENTRY MNVURV #type complete TITLE nonstructural protein NS - Rift Valley fever virus ORGANISM #formal_name Rift Valley fever virus #note host (mosquito); Homo sapiens (man) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS C38552; S11743 REFERENCE A38552 !$#authors Giorgi, C.; Accardi, L.; Nicoletti, L.; Gro, M.C.; Takehara, !1K.; Hilditch, C.; Morikawa, S.; Bishop, D.H.L. !$#journal Virology (1991) 180:738-753 !$#title Sequences and coding strategies of the S RNAs of Toscana and !1Rift Valley fever viruses compared to those of Punta Toro, !1Sicilian Sandfly fever, and Uukuniemi viruses. !$#cross-references MUID:91111992; PMID:1846496 !$#accession C38552 !'##molecule_type genomic RNA !'##residues 1-265 ##label GIO !'##cross-references GB:X53771; NID:g61928; PIDN:CAA37788.1; PID:g61929 GENETICS !$#map_position segment S CLASSIFICATION #superfamily Punta Toro virus nonstructural protein NS KEYWORDS nonstructural protein SUMMARY #length 265 #molecular-weight 29903 #checksum 6063 SEQUENCE /// ENTRY MNVUTV #type complete TITLE nonstructural protein NS - Toscana virus ORGANISM #formal_name Toscana virus #note host (mosquito); Homo sapiens (man) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS A38552 REFERENCE A38552 !$#authors Giorgi, C.; Accardi, L.; Nicoletti, L.; Gro, M.C.; Takehara, !1K.; Hilditch, C.; Morikawa, S.; Bishop, D.H.L. !$#journal Virology (1991) 180:738-753 !$#title Sequences and coding strategies of the S RNAs of Toscana and !1Rift Valley fever viruses compared to those of Punta Toro, !1Sicilian Sandfly fever, and Uukuniemi viruses. !$#cross-references MUID:91111992; PMID:1846496 !$#accession A38552 !'##molecule_type genomic RNA !'##residues 1-316 ##label GIO !'##cross-references GB:X53794; NID:g62201; PIDN:CAA37802.1; PID:g62202 GENETICS !$#map_position segment S CLASSIFICATION #superfamily Toscana virus nonstructural protein NS KEYWORDS nonstructural protein SUMMARY #length 316 #molecular-weight 36677 #checksum 3287 SEQUENCE /// ENTRY MNVUW1 #type complete TITLE nonstructural protein NS - tomato spotted wilt virus (strain L3) ORGANISM #formal_name tomato spotted wilt virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 03-Feb-1994 ACCESSIONS JQ0954 REFERENCE JQ0954 !$#authors Maiss, E.; Ivanova, L.; Breyel, E.; Adam, G. !$#submission submitted to JIPID, January 1991 !$#description Cloning and sequencing of the S RNA from a Bulganan isolate !1of tomato spotted wilt virus. !$#accession JQ0954 !'##molecule_type mRNA !'##residues 1-467 ##label MAI GENETICS !$#gene NS !$#map_position segment S CLASSIFICATION #superfamily tomato spotted wilt virus nonstructural protein !1NS KEYWORDS nonstructural protein SUMMARY #length 467 #molecular-weight 52413 #checksum 4214 SEQUENCE /// ENTRY MNVUWC #type complete TITLE nonstructural protein NS - tomato spotted wilt virus (strain CPNH1) ORGANISM #formal_name tomato spotted wilt virus DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jun-2000 ACCESSIONS JQ0547 REFERENCE JQ0547 !$#authors de Haan, P.; Wagemakers, L.; Peters, D.; Goldbach, R. !$#journal J. Gen. Virol. (1990) 71:1001-1007 !$#title The S RNA segment of tomato spotted wilt virus has an !1ambisense character. !$#cross-references MUID:90264829; PMID:1693160 !$#accession JQ0547 !'##molecule_type genomic RNA !'##residues 1-464 ##label DEH !'##cross-references DDBJ:D00645; NID:g222685; PIDN:BAA00540.1; !1PID:g222686 GENETICS !$#gene NS !$#map_position segment S CLASSIFICATION #superfamily tomato spotted wilt virus nonstructural protein !1NS KEYWORDS glycoprotein; nonstructural protein FEATURE !$132,210,270,291,381 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 464 #molecular-weight 52448 #checksum 2559 SEQUENCE /// ENTRY A42544 #type complete TITLE nonstructural protein - Impatiens necrotic spot virus ORGANISM #formal_name Impatiens necrotic spot virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jul-1999 ACCESSIONS A42544 REFERENCE A42544 !$#authors Law, M.D.; Speck, J.; Moyer, J.W. !$#journal Virology (1992) 188:732-741 !$#title The M RNA of Impatiens necrotic spot Tospovirus !1(Bunyaviridae) has an ambisense genomic organization. !$#cross-references MUID:92263777; PMID:1585644 !$#accession A42544 !'##molecule_type genomic RNA !'##residues 1-303 ##label LAW !'##cross-references GB:M74904; NID:g331308; PIDN:AAA46241.1; !1PID:g331309 GENETICS !$#map_position segment M CLASSIFICATION #superfamily Impatiens necrotic spot virus nonstructural !1protein KEYWORDS nonstructural protein SUMMARY #length 303 #molecular-weight 34104 #checksum 3783 SEQUENCE /// ENTRY JQ1927 #type complete TITLE nonstructural protein - tomato spotted wilt virus (strain BR-01) ORGANISM #formal_name tomato spotted wilt virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 07-May-1999 ACCESSIONS JQ1927 REFERENCE JQ1927 !$#authors Kormelink, R.; de Haan, P.; Meurs, C.; Peters, D.; Goldbach, !1R. !$#journal J. Gen. Virol. (1992) 73:2795-2804 !$#title The nucleotide sequence of the M RNA segment of tomato !1spotted wilt virus, a bunyavirus with two ambisense RNA !1segments. !$#cross-references MUID:93057351; PMID:1431808 !$#accession JQ1927 !'##molecule_type genomic RNA !'##residues 1-301 ##label KOR !'##cross-references GB:S48091 GENETICS !$#map_position segment M CLASSIFICATION #superfamily Impatiens necrotic spot virus nonstructural !1protein KEYWORDS glycoprotein; nonstructural protein FEATURE !$28,182 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 301 #molecular-weight 33563 #checksum 2054 SEQUENCE /// ENTRY B42544 #type complete TITLE G2-G1 polyprotein - Impatiens necrotic spot virus CONTAINS glycoprotein G1; glycoprotein G2 ORGANISM #formal_name Impatiens necrotic spot virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jul-1999 ACCESSIONS B42544 REFERENCE A42544 !$#authors Law, M.D.; Speck, J.; Moyer, J.W. !$#journal Virology (1992) 188:732-741 !$#title The M RNA of Impatiens necrotic spot Tospovirus !1(Bunyaviridae) has an ambisense genomic organization. !$#cross-references MUID:92263777; PMID:1585644 !$#accession B42544 !'##molecule_type genomic RNA !'##residues 1-1110 ##label LAW !'##cross-references GB:M74904; NID:g331308; PIDN:AAA46242.1; !1PID:g331310 !'##note the cleavage site between the G2 glycoprotein and G1 !1glycoprotein is not determined GENETICS !$#map_position segment M CLASSIFICATION #superfamily Impatiens necrotic spot virus G2-G1 polyprotein KEYWORDS glycoprotein; polyprotein; transmembrane protein FEATURE !$291-307 #region hydrophobic\ !$328-344 #region hydrophobic\ !$414-430 #region hydrophobic\ !$1046-1062 #region hydrophobic\ !$46,92,186,294,316, !$566,582,957,1072 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1110 #molecular-weight 124867 #checksum 2949 SEQUENCE /// ENTRY JQ1928 #type complete TITLE G2-G1 polyprotein precursor - tomato spotted wilt virus (strain BR-01) CONTAINS glycoprotein G1; glycoprotein G2 ORGANISM #formal_name tomato spotted wilt virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS JQ1928 REFERENCE JQ1927 !$#authors Kormelink, R.; de Haan, P.; Meurs, C.; Peters, D.; Goldbach, !1R. !$#journal J. Gen. Virol. (1992) 73:2795-2804 !$#title The nucleotide sequence of the M RNA segment of tomato !1spotted wilt virus, a bunyavirus with two ambisense RNA !1segments. !$#cross-references MUID:93057351; PMID:1431808 !$#accession JQ1928 !'##molecule_type genomic RNA !'##residues 1-1135 ##label KOR !'##cross-references GB:S48091; NID:g259518; PIDN:AAB24089.1; !1PID:g259520 !'##note the cleavage site between the G2 glycoprotein and G1 !1glycoprotein is not determined GENETICS !$#map_position segment M CLASSIFICATION #superfamily Impatiens necrotic spot virus G2-G1 polyprotein KEYWORDS glycoprotein; polyprotein; transmembrane protein FEATURE !$1-35 #domain signal sequence #status predicted #label SIG\ !$36-1135 #product G2-G1 polyprotein #status predicted #label !8GGP\ !$315-335 #region hydrophobic\ !$352-368 #region hydrophobic\ !$448-483 #region hydrophobic\ !$1068-1089 #region hydrophobic\ !$116,210,318,340, !$395,605,980,1095 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1135 #molecular-weight 127317 #checksum 1360 SEQUENCE /// ENTRY VGVUPT #type complete TITLE M polyprotein - Punta Toro virus CONTAINS glycoprotein G1; glycoprotein G2; nonstructural protein NS-M ORGANISM #formal_name Punta Toro virus #note host (mosquito); Homo sapiens (man) DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 16-Jul-1999 ACCESSIONS A04109 REFERENCE A04109 !$#authors Ihara, T.; Smith, J.; Dalrymple, J.M.; Bishop, D.H.L. !$#journal Virology (1985) 144:246-259 !$#title Complete sequences of the glycoproteins and M RNA of Punta !1Toro phlebovirus compared to those of Rift valley fever !1virus. !$#cross-references MUID:86045944; PMID:2998043 !$#accession A04109 !'##molecule_type genomic RNA !'##residues 1-1313 ##label IHA !'##cross-references GB:M11156; NID:g333337; PIDN:AAA47110.1; !1PID:g333338 GENETICS !$#map_position segment M CLASSIFICATION #superfamily phlebovirus M polyprotein KEYWORDS glycoprotein; nonstructural protein; polyprotein FEATURE !$1-270 #product nonstructural protein NS-M #status predicted !8#label NSM\ !$271-809 #product glycoprotein G1 #status predicted #label !8GG1\ !$810-1313 #product glycoprotein G2 #status predicted #label !8GG2\ !$36,76,102,496,948, !$1154,1243,1253 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1313 #molecular-weight 146374 #checksum 4967 SEQUENCE /// ENTRY VGVURV #type complete TITLE M polyprotein - Rift Valley fever virus (strain ZH-501) CONTAINS glycoprotein G1; glycoprotein G2; nonstructural protein NS-M ORGANISM #formal_name Rift Valley fever virus #note host (mosquito); Homo sapiens (man) DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 12-Apr-1996 ACCESSIONS A04110 REFERENCE A04110 !$#authors Collett, M.S.; Purchio, A.F.; Keegan, K.; Frazier, S.; Hays, !1W.; Anderson, D.K.; Parker, M.D.; Schmaljohn, C.; Schmidt, !1J.; Dalrymple, J.M. !$#journal Virology (1985) 144:228-245 !$#title Complete nucleotide sequence of the M RNA segment of Rift !1valley fever virus. !$#cross-references MUID:86045943; PMID:2998042 !$#accession A04110 !'##molecule_type genomic RNA !'##residues 1-1206 ##label COL GENETICS !$#map_position segment M CLASSIFICATION #superfamily phlebovirus M polyprotein KEYWORDS glycoprotein; nonstructural protein; polyprotein FEATURE !$1-153 #product nonstructural protein NS-M #status predicted !8#label NSM\ !$154-690 #product glycoprotein G1 #status predicted #label !8GG1\ !$691-1206 #product glycoprotein G2 #status predicted #label !8GG2\ !$88,794,1035,1077 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1206 #molecular-weight 132030 #checksum 8546 SEQUENCE /// ENTRY VGVURF #type complete TITLE M polyprotein - Rift Valley fever virus (strain ZH-548M12) CONTAINS glycoprotein G1; glycoprotein G2; nonstructural protein NS-M ORGANISM #formal_name Rift Valley fever virus #note host (mosquito); Homo sapiens (man) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS A30183 REFERENCE A30183 !$#authors Takehara, K.; Min, M.K.; Battles, J.K.; Sugiyama, K.; Emery, !1V.C.; Dalrymple, J.M.; Bishop, D.H.L. !$#journal Virology (1989) 169:452-457 !$#title Identification of mutations in the M RNA of a candidate !1vaccine strain of Rift Valley fever virus. !$#cross-references MUID:89204917; PMID:2705307 !$#accession A30183 !'##molecule_type genomic RNA !'##residues 1-1197 ##label TAK !'##cross-references GB:M25276; NID:g538444; PIDN:AAA47449.1; !1PID:g538445 GENETICS !$#map_position segment M CLASSIFICATION #superfamily phlebovirus M polyprotein KEYWORDS glycoprotein; nonstructural protein; polyprotein FEATURE !$1-153 #product nonstructural protein NS-M #status predicted !8#label NSM\ !$154-690 #product glycoprotein G1 #status predicted #label !8GG1\ !$691-1197 #product glycoprotein G2 #status predicted #label !8GG2\ !$88,438,794,829, !$1035,1077 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1197 #molecular-weight 130804 #checksum 2113 SEQUENCE /// ENTRY A43364 #type complete TITLE M polyprotein precursor - Dugbe virus (strain ArD 44313) CONTAINS glycoprotein G1; glycoprotein G2 ORGANISM #formal_name Dugbe virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jul-1999 ACCESSIONS A43364; B43364 REFERENCE A43364 !$#authors Marriott, A.C.; El-Ghorr, A.A.; Nuttall, P.A. !$#journal Virology (1992) 190:606-615 !$#title Dugbe nairovirus M RNA: nucleotide sequence and coding !1strategy. !$#cross-references MUID:92391077; PMID:1387749 !$#accession A43364 !'##molecule_type genomic RNA !'##residues 1-1551 ##label MA1 !'##cross-references GB:M94133; NID:g323680; PIDN:AAA42974.1; !1PID:g323681 !$#accession B43364 !'##molecule_type protein !'##residues 897-905 ##label MA2 GENETICS !$#map_position segment M CLASSIFICATION #superfamily Nairovirus M polyprotein KEYWORDS glycoprotein; polyprotein; transmembrane protein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-896 #product glycoprotein G1 #status predicted #label !8GP1\ !$831-847 #domain transmembrane #status predicted #label TM1\ !$897-1551 #product glycoprotin G2 #status predicted #label GP2\ !$1452-1468 #domain transmembrane #status predicted #label TM2\ !$25,30,80,142,413, !$827,848,1201,1258, !$1420 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1551 #molecular-weight 173353 #checksum 7674 SEQUENCE /// ENTRY MFVN #type complete TITLE matrix protein - vesicular stomatitis Indiana virus (strain San Juan) ORGANISM #formal_name vesicular stomatitis Indiana virus DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 16-Jul-1999 ACCESSIONS A04111 REFERENCE A92983 !$#authors Rose, J.K.; Gallione, C.J. !$#journal J. Virol. (1981) 39:519-528 !$#title Nucleotide sequences of the mRNA's encoding the vesicular !1stomatitis virus G and M proteins determined from cDNA !1clones containing the complete coding regions. !$#cross-references MUID:82010868; PMID:6268840 !$#accession A04111 !'##molecule_type genomic RNA !'##residues 1-229 ##label ROS !'##cross-references GB:J02428; GB:J02430; GB:J02431; GB:J02432; !1GB:J02434; GB:J02435; GB:J02436; GB:J02437; GB:J02438; !1GB:K00519; GB:K00520; GB:K00625; GB:K01068; GB:K01069; !1GB:K01070; GB:K01638; GB:K01639; NID:g335873; !1PIDN:AAA48369.1; PID:g335876 CLASSIFICATION #superfamily rhabdovirus matrix protein SUMMARY #length 229 #molecular-weight 26094 #checksum 2803 SEQUENCE /// ENTRY MFVNGG #type complete TITLE matrix protein - vesicular stomatitis Indiana virus (strain Glasgow) ORGANISM #formal_name vesicular stomatitis Indiana virus DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 16-Jul-1999 ACCESSIONS A04112 REFERENCE A04112 !$#authors Gopalakrishna, Y.; Lenard, J. !$#journal J. Virol. (1985) 56:655-659 !$#title Sequence alterations in temperature-sensitive M-protein !1mutants (complementation group III) of vesicular stomatitis !1virus. !$#cross-references MUID:86062892; PMID:2999421 !$#accession A04112 !'##molecule_type mRNA !'##residues 1-229 ##label GOP !'##cross-references GB:M11754; NID:g336033; PIDN:AAA48444.1; !1PID:g336034 GENETICS !$#gene M CLASSIFICATION #superfamily rhabdovirus matrix protein KEYWORDS matrix protein SUMMARY #length 229 #molecular-weight 26121 #checksum 1753 SEQUENCE /// ENTRY MFVNVJ #type complete TITLE matrix protein - vesicular stomatitis New Jersey virus ORGANISM #formal_name vesicular stomatitis New Jersey virus DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jul-1999 ACCESSIONS A27254 REFERENCE A27254 !$#authors Gill, D.S.; Banerjee, A.K. !$#journal Virology (1986) 150:308-312 !$#title Complete nucleotide sequence of the matrix protein mRNA of !1vesicular stomatitis virus (New Jersey serotype). !$#cross-references MUID:86153622; PMID:3006343 !$#accession A27254 !'##molecule_type mRNA !'##residues 1-229 ##label GIL !'##cross-references GB:M14553; NID:g336031; PIDN:AAA48443.1; !1PID:g336032 GENETICS !$#gene M CLASSIFICATION #superfamily rhabdovirus matrix protein KEYWORDS matrix protein SUMMARY #length 229 #molecular-weight 26229 #checksum 7412 SEQUENCE /// ENTRY MFVNSV #type complete TITLE matrix protein - spring viremia of carp virus ORGANISM #formal_name spring viremia of carp virus DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 16-Jul-1999 ACCESSIONS A04113 REFERENCE A04113 !$#authors Kiuchi, A.; Roy, P. !$#journal Virology (1984) 134:238-243 !$#title Comparison of the primary sequence of spring viremia of carp !1virus M protein with that of vesicular stomatitis virus. !$#cross-references MUID:84174091; PMID:6324471 !$#accession A04113 !'##molecule_type mRNA !'##residues 1-223 ##label KIU !'##cross-references GB:K02123; NID:g335123; PIDN:AAA47884.1; !1PID:g335124 !'##note the authors translated the codon UGG for residues 200 and 204 !1as Met GENETICS !$#gene M CLASSIFICATION #superfamily rhabdovirus matrix protein KEYWORDS matrix protein SUMMARY #length 223 #molecular-weight 25628 #checksum 7559 SEQUENCE /// ENTRY MFVNRV #type complete TITLE matrix protein - rabies virus ORGANISM #formal_name rabies virus DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Jul-1999 ACCESSIONS A26275; C24887 REFERENCE A94100 !$#authors Tordo, N.; Poch, O.; Ermine, A.; Keith, G.; Rougeon, F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:3914-3918 !$#title Walking along the rabies genome: is the large G-L intergenic !1region a remnant gene? !$#cross-references MUID:86233343; PMID:3459163 !$#accession A26275 !'##molecule_type genomic RNA !'##residues 1-202 ##label TOR !'##cross-references GB:M13215; GB:M21634; NID:g333585; PIDN:AAA47217.1; !1PID:g333588 GENETICS !$#gene M; M2 CLASSIFICATION #superfamily rabies virus matrix protein KEYWORDS matrix protein; phosphoprotein SUMMARY #length 202 #molecular-weight 23157 #checksum 8468 SEQUENCE /// ENTRY MFVNSB #type complete TITLE matrix protein - rabies virus (strain SAD B19) ORGANISM #formal_name rabies virus DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS C34746 REFERENCE A34746 !$#authors Conzelmann, K.K.; Cox, J.H.; Schneider, L.G.; Thiel, H.J. !$#journal Virology (1990) 175:485-499 !$#title Molecular cloning and complete nucleotide sequence of the !1attenuated rabies virus SAD B19. !$#cross-references MUID:90223994; PMID:2139267 !$#accession C34746 !'##molecule_type genomic RNA !'##residues 1-202 ##label CON !'##cross-references GB:M31046; NID:g333556; PIDN:AAA47201.1; !1PID:g333559 GENETICS !$#gene M; M2 CLASSIFICATION #superfamily rabies virus matrix protein KEYWORDS matrix protein; phosphoprotein SUMMARY #length 202 #molecular-weight 23341 #checksum 7627 SEQUENCE /// ENTRY MFVNAV #type complete TITLE matrix protein - rabies virus (strain AVO1) ORGANISM #formal_name rabies virus DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS S07816 REFERENCE S07813 !$#authors Poch, O.; Tordo, N.; Keith, G. !$#journal Biochimie (1988) 70:1019-1029 !$#title Sequence of the 3386 3' nucleotides of the genome of the !1AVO1 strain rabies virus: structural similarities in the !1protein regions involved in transcription. !$#cross-references MUID:89150295; PMID:3147698 !$#accession S07816 !'##molecule_type genomic RNA !'##residues 1-202 ##label POC !'##cross-references EMBL:X13357; NID:g61809; PIDN:CAA31736.1; !1PID:g61813 GENETICS !$#gene M; M2 CLASSIFICATION #superfamily rabies virus matrix protein KEYWORDS matrix protein; phosphoprotein SUMMARY #length 202 #molecular-weight 23231 #checksum 9397 SEQUENCE /// ENTRY MFVNCV #type complete TITLE matrix protein - rabies virus (strain CVS) ALTERNATE_NAMES M2 phosphoprotein ORGANISM #formal_name rabies virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 10-Oct-1997 ACCESSIONS JQ1112; C58460 REFERENCE JQ1112 !$#authors Hiramatsu, K.; Takita, Y.; Mannen, K.; Mifune, K. !$#submission submitted to JIPID, July 1991 !$#accession JQ1112 !'##molecule_type genomic RNA !'##residues 1-202 ##label HIR !'##experimental_source strain CVS REFERENCE A58460 !$#authors Bai, X.; Gu, L.; Wang, S. !$#journal Chinese J. Microbiol. Immunol. (1996) 16:121-124 !$#title Nucleotide sequences of the N, NS, and M genes of Chinese !1vaccine strain (aG) of rabies virus. !$#accession C58460 !'##molecule_type mRNA !'##residues 1-202 ##label BAI !'##experimental_source Chinese vaccine strain aG GENETICS !$#gene M CLASSIFICATION #superfamily rabies virus matrix protein KEYWORDS matrix protein; phosphoprotein SUMMARY #length 202 #molecular-weight 23132 #checksum 9177 SEQUENCE /// ENTRY MFVNNA #type complete TITLE matrix protein - rabies virus (strain Nishigahara RCEH) ORGANISM #formal_name rabies virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jun-2000 ACCESSIONS JQ1113; A48557 REFERENCE JQ1112 !$#authors Hiramatsu, K.; Takita, Y.; Mannen, K.; Mifune, K. !$#submission submitted to JIPID, July 1991 !$#accession JQ1113 !'##molecule_type genomic RNA !'##residues 1-202 ##label HI1 REFERENCE A48557 !$#authors Hiramatsu, K.; Mannen, K.; Mifune, K.; Nishizono, A.; !1Takita-Sonoda, Y. !$#journal Virus Genes (1993) 7:83-88 !$#title Comparative sequence analysis of the M gene among rabies !1virus strains and its expression by recombinant vaccinia !1virus. !$#cross-references MUID:93227571; PMID:8470369 !$#accession A48557 !'##molecule_type genomic RNA !'##residues 1-202 ##label HI2 !'##cross-references GB:D10482; GB:D90451; NID:g222468; PIDN:BAA01285.1; !1PID:g222469 !'##note sequence extracted from NCBI backbone (NCBIN:129325, !1NCBIP:129326) GENETICS !$#gene M CLASSIFICATION #superfamily rabies virus matrix protein KEYWORDS matrix protein; phosphoprotein SUMMARY #length 202 #molecular-weight 23320 #checksum 6400 SEQUENCE /// ENTRY MFVNSY #type complete TITLE matrix protein - Sonchus yellow net virus ALTERNATE_NAMES M2 protein ORGANISM #formal_name Sonchus yellow net virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 24-Sep-1999 ACCESSIONS A27031 REFERENCE A27031 !$#authors Heaton, L.A.; Zuidema, D.; Jackson, A.O. !$#journal Virology (1987) 161:234-241 !$#title Structure of the M2 protein gene of Sonchus yellow net !1virus. !$#cross-references MUID:88044498; PMID:3672930 !$#accession A27031 !'##molecule_type genomic RNA !'##residues 1-345 ##label HEA !'##cross-references GB:L32603; NID:g484030; PIDN:AAA50381.1; !1PID:g484032 !'##note the authors translated the codon GUG for residue 19 as Asn CLASSIFICATION #superfamily plant rhabdovirus matrix protein KEYWORDS matrix protein SUMMARY #length 345 #molecular-weight 38326 #checksum 5945 SEQUENCE /// ENTRY A45350 #type complete TITLE matrix protein M1 - Sonchus yellow net virus ALTERNATE_NAMES M1 protein ORGANISM #formal_name Sonchus yellow net virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jul-1999 ACCESSIONS A45350 REFERENCE A45350 !$#authors Hillman, B.I.; Heaton, L.A.; Hunter, B.G.; Modrell, B.; !1Jackson, A.O. !$#journal Virology (1990) 179:201-207 !$#title Structure of the gene encoding the M1 protein of Sonchus !1yellow net virus. !$#cross-references MUID:91021022; PMID:2219720 !$#accession A45350 !'##molecule_type genomic RNA !'##residues 1-286 ##label HIL !'##cross-references GB:M35689; NID:g335141; PIDN:AAA47897.1; !1PID:g335142 CLASSIFICATION #superfamily plant rhabdovirus M1 protein KEYWORDS matrix protein SUMMARY #length 286 #molecular-weight 31775 #checksum 8358 SEQUENCE /// ENTRY MNVN #type complete TITLE nonstructural protein - vesicular stomatitis Indiana virus (strain San Juan) ORGANISM #formal_name vesicular stomatitis Indiana virus DATE 19-Feb-1984 #sequence_revision 25-Feb-1985 #text_change 27-Jan-1995 ACCESSIONS A92984; A04114 REFERENCE A92984 !$#authors Gallione, C.J.; Greene, J.R.; Iverson, L.E.; Rose, J.K. !$#journal J. Virol. (1981) 39:529-535 !$#title Nucleotide sequences of the mRNA's encoding the vesicular !1stomatitis virus N and NS proteins. !$#cross-references MUID:82010869; PMID:6268841 !$#accession A92984 !'##molecule_type genomic RNA !'##residues 1-265 ##label GAL !'##note an extra U in the codon for residue 189 was erroneously !1reported. Deletion of the U changes the reading frame and !1produces the correct sequence as shown above REFERENCE A94454 !$#authors Schubert, M. !$#submission submitted to the Protein Sequence Database, May 1984 !$#contents annotation; revision to residues 189-265 !$#note deletion of U from codon 189 changes the reading frame !1between residues 189-265, giving the correct sequence as !1shown above COMMENT The L protein and the NS protein are considered to be the !1subunits of the polymerase complex, because they are !1individually inactive. CLASSIFICATION #superfamily vesicular stomatitis virus nonstructural !1protein SUMMARY #length 265 #molecular-weight 29942 #checksum 8193 SEQUENCE /// ENTRY MNVNIM #type complete TITLE nonstructural protein - vesicular stomatitis Indiana virus (strain Mudd-Summers) ORGANISM #formal_name vesicular stomatitis Indiana virus DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jul-1999 ACCESSIONS A29144 REFERENCE A29144 !$#authors Hudson, L.D.; Condra, C.; Lazzarini, R.A. !$#journal J. Gen. Virol. (1986) 67:1571-1579 !$#title Cloning and expression of a viral phosphoprotein: structure !1suggests vesicular stomatitis virus NS may function by !1mimicking an RNA template. !$#cross-references MUID:86280368; PMID:3016152 !$#accession A29144 !'##molecule_type mRNA !'##residues 1-265 ##label HUD !'##cross-references GB:X04196; NID:g61843; PIDN:CAA27788.1; PID:g61844 GENETICS !$#gene NS CLASSIFICATION #superfamily vesicular stomatitis virus nonstructural !1protein KEYWORDS nonstructural protein SUMMARY #length 265 #molecular-weight 30035 #checksum 8303 SEQUENCE /// ENTRY MNVNV4 #type complete TITLE nonstructural protein - vesicular stomatitis Indiana virus (strain Glasgow) ORGANISM #formal_name vesicular stomatitis Indiana virus DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 16-Jul-1999 ACCESSIONS A26794 REFERENCE A93029 !$#authors DePolo, N.J.; Giachetti, C.; Holland, J.J. !$#journal J. Virol. (1987) 61:454-464 !$#title Continuing coevolution of virus and defective interfering !1particles and of viral genome sequences during undiluted !1passages: virus mutants exhibiting nearly complete !1resistance to formerly dominant defective interfering !1particles. !$#cross-references MUID:87112941; PMID:3027375 !$#accession A26794 !'##molecule_type genomic RNA !'##residues 1-265 ##label DEP !'##cross-references GB:M15121; NID:g335892; PIDN:AAA48375.1; !1PID:g335893 GENETICS !$#gene NS CLASSIFICATION #superfamily vesicular stomatitis virus nonstructural !1protein KEYWORDS nonstructural protein SUMMARY #length 265 #molecular-weight 29905 #checksum 8960 SEQUENCE /// ENTRY MNVNVJ #type complete TITLE polymerase-associated phosphoprotein P - vesicular stomatitis New Jersey virus ORGANISM #formal_name vesicular stomatitis New Jersey virus DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 29-Oct-1999 ACCESSIONS A04115; A45692 REFERENCE A04115 !$#authors Gill, D.S.; Banerjee, A.K. !$#journal J. Virol. (1985) 55:60-66 !$#title Vesicular stomatitis virus NS proteins: structural !1similarity without extensive sequence homology. !$#cross-references MUID:85237710; PMID:2989560 !$#accession A04115 !'##molecule_type mRNA !'##residues 1-274 ##label GIL !'##cross-references GB:K03387; NID:g336047; PIDN:AAA48453.1; !1PID:g336048 REFERENCE A45692 !$#authors Spiropoulou, C.F.; Nichol, S.T. !$#journal J. Virol. (1993) 67:3103-3110 !$#title A small highly basic protein is encoded in overlapping frame !1within the P gene of vesicular stomatitis virus. !$#cross-references MUID:93267755; PMID:8388490 !$#accession A45692 !'##status preliminary !'##molecule_type genomic RNA !'##residues 1-87 ##label SPI !'##cross-references GB:S61075; NID:g300483; PIDN:AAB26735.1; !1PID:g300484 !'##experimental_source (strain Ogden) !'##note sequence extracted from NCBI backbone (NCBIN:132387, !1NCBIP:132388) GENETICS !$#gene NS; M1 CLASSIFICATION #superfamily vesicular stomatitis virus nonstructural !1protein KEYWORDS nonstructural protein; phosphoprotein SUMMARY #length 274 #molecular-weight 31406 #checksum 8492 SEQUENCE /// ENTRY MNVNVM #type complete TITLE nonstructural protein - vesicular stomatitis New Jersey virus (strain Missouri) ORGANISM #formal_name vesicular stomatitis New Jersey virus DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jul-1999 ACCESSIONS A29143 REFERENCE A29143 !$#authors Rae, B.P.; Elliott, R.M. !$#journal J. Gen. Virol. (1986) 67:1351-1360 !$#title Conservation of potential phosphorylation sites in the NS !1proteins of the New Jersey and Indiana serotypes of !1vesicular stomatitis virus. !$#cross-references MUID:86253157; PMID:3014048 !$#accession A29143 !'##molecule_type mRNA !'##residues 1-274 ##label RAE !'##cross-references EMBL:X04063; NID:g61848; PIDN:CAA27695.1; !1PID:g61849 GENETICS !$#gene NS CLASSIFICATION #superfamily vesicular stomatitis virus nonstructural !1protein KEYWORDS nonstructural protein SUMMARY #length 274 #molecular-weight 31300 #checksum 6939 SEQUENCE /// ENTRY B44502 #type complete TITLE nonstructural protein - Chandipura virus (strain I653514) ORGANISM #formal_name Chandipura virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jul-1999 ACCESSIONS B44502 REFERENCE A44502 !$#authors Masters, P.S.; Banerjee, A.K. !$#journal Virology (1987) 157:298-306 !$#title Sequences of Chandipura virus N and NS genes: evidence for !1high mutability of the NS gene within vesiculoviruses. !$#cross-references MUID:87151129; PMID:3029973 !$#accession B44502 !'##molecule_type mRNA !'##residues 1-293 ##label MAS !'##cross-references GB:M16608; NID:g336043; PIDN:AAA48451.1; !1PID:g336045 GENETICS !$#gene NS CLASSIFICATION #superfamily vesicular stomatitis virus nonstructural !1protein KEYWORDS nonstructural protein SUMMARY #length 293 #molecular-weight 32523 #checksum 312 SEQUENCE /// ENTRY MNVNRV #type complete TITLE nonstructural protein - rabies virus ORGANISM #formal_name rabies virus DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Jul-1999 ACCESSIONS B26275; B24887 REFERENCE A94100 !$#authors Tordo, N.; Poch, O.; Ermine, A.; Keith, G.; Rougeon, F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:3914-3918 !$#title Walking along the rabies genome: is the large G-L intergenic !1region a remnant gene? !$#cross-references MUID:86233343; PMID:3459163 !$#accession B26275 !'##molecule_type genomic RNA !'##residues 1-297 ##label TOR !'##cross-references GB:M13215; GB:M21634; NID:g333585; PIDN:AAA47216.1; !1PID:g333587 GENETICS !$#gene NS; M1 CLASSIFICATION #superfamily rabies virus nonstructural protein KEYWORDS nonstructural protein SUMMARY #length 297 #molecular-weight 33166 #checksum 7377 SEQUENCE /// ENTRY MNVNSB #type complete TITLE nonstructural protein - rabies virus (strain SAD B19) ORGANISM #formal_name rabies virus DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS B34746 REFERENCE A34746 !$#authors Conzelmann, K.K.; Cox, J.H.; Schneider, L.G.; Thiel, H.J. !$#journal Virology (1990) 175:485-499 !$#title Molecular cloning and complete nucleotide sequence of the !1attenuated rabies virus SAD B19. !$#cross-references MUID:90223994; PMID:2139267 !$#accession B34746 !'##molecule_type genomic RNA !'##residues 1-297 ##label CON !'##cross-references GB:M31046; NID:g333556; PIDN:AAA47200.1; !1PID:g333558 GENETICS !$#gene NS; M1 CLASSIFICATION #superfamily rabies virus nonstructural protein KEYWORDS nonstructural protein SUMMARY #length 297 #molecular-weight 33248 #checksum 6462 SEQUENCE /// ENTRY MNVNAV #type complete TITLE nonstructural protein - rabies virus (strain AVO1) ORGANISM #formal_name rabies virus DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS S07814 REFERENCE S07813 !$#authors Poch, O.; Tordo, N.; Keith, G. !$#journal Biochimie (1988) 70:1019-1029 !$#title Sequence of the 3386 3' nucleotides of the genome of the !1AVO1 strain rabies virus: structural similarities in the !1protein regions involved in transcription. !$#cross-references MUID:89150295; PMID:3147698 !$#accession S07814 !'##molecule_type genomic RNA !'##residues 1-297 ##label POC !'##cross-references EMBL:X13357; NID:g61809; PIDN:CAA31734.1; !1PID:g61811 GENETICS !$#gene NS; M1 CLASSIFICATION #superfamily rabies virus nonstructural protein KEYWORDS nonstructural protein SUMMARY #length 297 #molecular-weight 33603 #checksum 4986 SEQUENCE /// ENTRY WMVNAV #type complete TITLE C protein - rabies virus (strain AVO1) ORGANISM #formal_name rabies virus DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS S07815 REFERENCE S07813 !$#authors Poch, O.; Tordo, N.; Keith, G. !$#journal Biochimie (1988) 70:1019-1029 !$#title Sequence of the 3386 3' nucleotides of the genome of the !1AVO1 strain rabies virus: structural similarities in the !1protein regions involved in transcription. !$#cross-references MUID:89150295; PMID:3147698 !$#accession S07815 !'##molecule_type genomic RNA !'##residues 1-69 ##label POC !'##cross-references EMBL:X13357; NID:g61809; PIDN:CAA31735.1; !1PID:g61812 GENETICS !$#gene C CLASSIFICATION #superfamily rabies virus C protein SUMMARY #length 69 #molecular-weight 8255 #checksum 5035 SEQUENCE /// ENTRY VHVNN #type complete TITLE nucleoprotein - vesicular stomatitis Indiana virus (strain San Juan) ORGANISM #formal_name vesicular stomatitis Indiana virus DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 16-Jul-1999 ACCESSIONS A04116 REFERENCE A92984 !$#authors Gallione, C.J.; Greene, J.R.; Iverson, L.E.; Rose, J.K. !$#journal J. Virol. (1981) 39:529-535 !$#title Nucleotide sequences of the mRNA's encoding the vesicular !1stomatitis virus N and NS proteins. !$#cross-references MUID:82010869; PMID:6268841 !$#accession A04116 !'##molecule_type genomic RNA !'##residues 1-422 ##label GAL !'##cross-references GB:J02428; GB:J02430; GB:J02431; GB:J02432; !1GB:J02434; GB:J02435; GB:J02436; GB:J02437; GB:J02438; !1GB:K00519; GB:K00520; GB:K00625; GB:K01068; GB:K01069; !1GB:K01070; GB:K01638; GB:K01639; NID:g335873; !1PIDN:AAA48367.1; PID:g335874 GENETICS !$#gene N CLASSIFICATION #superfamily vesicular stomatitis virus nucleoprotein KEYWORDS nucleoprotein SUMMARY #length 422 #molecular-weight 47409 #checksum 5119 SEQUENCE /// ENTRY VHVNV4 #type complete TITLE nucleoprotein - vesicular stomatitis Indiana virus (strain Glasgow) ORGANISM #formal_name vesicular stomatitis Indiana virus DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 16-Jul-1999 ACCESSIONS B26794 REFERENCE A93029 !$#authors DePolo, N.J.; Giachetti, C.; Holland, J.J. !$#journal J. Virol. (1987) 61:454-464 !$#title Continuing coevolution of virus and defective interfering !1particles and of viral genome sequences during undiluted !1passages: virus mutants exhibiting nearly complete !1resistance to formerly dominant defective interfering !1particles. !$#cross-references MUID:87112941; PMID:3027375 !$#accession B26794 !'##molecule_type genomic RNA !'##residues 1-422 ##label DEP !'##cross-references GB:M15213; NID:g335894; PIDN:AAA48376.1; !1PID:g335895 GENETICS !$#gene N CLASSIFICATION #superfamily vesicular stomatitis virus nucleoprotein KEYWORDS nucleoprotein SUMMARY #length 422 #molecular-weight 47437 #checksum 5490 SEQUENCE /// ENTRY VHVNPV #type complete TITLE nucleoprotein - Piry virus ORGANISM #formal_name Piry virus #note host Didelphis virginiana (opossum) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 30-Jun-1993 ACCESSIONS A36643 REFERENCE A36643 !$#authors Crysler, J.G.; Lee, P.; Reinders, M.; Prevec, L. !$#journal J. Gen. Virol. (1990) 71:2191-2194 !$#title The sequence of the nucleocapsid protein (N) gene of Piry !1virus: possible domains in the N protein of vesiculoviruses. !$#cross-references MUID:91011370; PMID:1698928 !$#accession A36643 !'##molecule_type mRNA !'##residues 1-427 ##label CRY GENETICS !$#gene N CLASSIFICATION #superfamily vesicular stomatitis virus nucleoprotein KEYWORDS nucleoprotein SUMMARY #length 427 #molecular-weight 48435 #checksum 2725 SEQUENCE /// ENTRY A44502 #type complete TITLE nucleoprotein - Chandipura virus (strain I653514) ALTERNATE_NAMES nucleocapsid protein ORGANISM #formal_name Chandipura virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jul-1999 ACCESSIONS A44502 REFERENCE A44502 !$#authors Masters, P.S.; Banerjee, A.K. !$#journal Virology (1987) 157:298-306 !$#title Sequences of Chandipura virus N and NS genes: evidence for !1high mutability of the NS gene within vesiculoviruses. !$#cross-references MUID:87151129; PMID:3029973 !$#accession A44502 !'##molecule_type mRNA !'##residues 1-422 ##label MAS !'##cross-references GB:M16608; NID:g336043; PIDN:AAA48450.1; !1PID:g336044 GENETICS !$#gene N CLASSIFICATION #superfamily vesicular stomatitis virus nucleoprotein KEYWORDS nucleocapsid; nucleoprotein SUMMARY #length 422 #molecular-weight 47943 #checksum 2285 SEQUENCE /// ENTRY VHVNRV #type complete TITLE nucleoprotein - rabies virus ORGANISM #formal_name rabies virus DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Jul-1999 ACCESSIONS D26275; A24887 REFERENCE A94100 !$#authors Tordo, N.; Poch, O.; Ermine, A.; Keith, G.; Rougeon, F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:3914-3918 !$#title Walking along the rabies genome: is the large G-L intergenic !1region a remnant gene? !$#cross-references MUID:86233343; PMID:3459163 !$#accession D26275 !'##molecule_type genomic RNA !'##residues 1-450 ##label TOR !'##cross-references GB:M13215; GB:M21634; NID:g333585; PIDN:AAA47215.1; !1PID:g333586 GENETICS !$#gene N CLASSIFICATION #superfamily rabies virus nucleoprotein KEYWORDS nucleoprotein SUMMARY #length 450 #molecular-weight 50605 #checksum 4089 SEQUENCE /// ENTRY VHVNSB #type complete TITLE nucleoprotein - rabies virus (strain SAD B19) ORGANISM #formal_name rabies virus DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS A34746 REFERENCE A34746 !$#authors Conzelmann, K.K.; Cox, J.H.; Schneider, L.G.; Thiel, H.J. !$#journal Virology (1990) 175:485-499 !$#title Molecular cloning and complete nucleotide sequence of the !1attenuated rabies virus SAD B19. !$#cross-references MUID:90223994; PMID:2139267 !$#accession A34746 !'##molecule_type genomic RNA !'##residues 1-450 ##label CON !'##cross-references GB:M31046; NID:g333556; PIDN:AAA47199.1; !1PID:g333557 GENETICS !$#gene N CLASSIFICATION #superfamily rabies virus nucleoprotein KEYWORDS nucleoprotein SUMMARY #length 450 #molecular-weight 50603 #checksum 4016 SEQUENCE /// ENTRY VHVNAV #type complete TITLE nucleoprotein - rabies virus (strain AVO1) ORGANISM #formal_name rabies virus DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS S07813 REFERENCE S07813 !$#authors Poch, O.; Tordo, N.; Keith, G. !$#journal Biochimie (1988) 70:1019-1029 !$#title Sequence of the 3386 3' nucleotides of the genome of the !1AVO1 strain rabies virus: structural similarities in the !1protein regions involved in transcription. !$#cross-references MUID:89150295; PMID:3147698 !$#accession S07813 !'##molecule_type genomic RNA !'##residues 1-450 ##label POC !'##cross-references EMBL:X13357; NID:g61809; PIDN:CAA31733.1; !1PID:g61810 GENETICS !$#gene N CLASSIFICATION #superfamily rabies virus nucleoprotein KEYWORDS nucleoprotein SUMMARY #length 450 #molecular-weight 50733 #checksum 3967 SEQUENCE /// ENTRY VHVNSY #type complete TITLE nucleoprotein - Sonchus yellow net virus ORGANISM #formal_name Sonchus yellow net virus #note host Nicotiana sp. (tobacco) DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 16-Jul-1999 ACCESSIONS A29123 REFERENCE A29123 !$#authors Zuidema, D.; Heaton, L.A.; Jackson, A.O. !$#journal Virology (1987) 159:373-380 !$#title Structure of the nucleocapsid protein gene of Sonchus yellow !1net virus. !$#accession A29123 !'##molecule_type mRNA !'##residues 1-475 ##label ZUI !'##cross-references GB:M17210; NID:g335135; PIDN:AAA47895.1; !1PID:g335136 GENETICS !$#gene N CLASSIFICATION #superfamily plant rhabdovirus nucleoprotein KEYWORDS nucleoprotein SUMMARY #length 475 #molecular-weight 53635 #checksum 8066 SEQUENCE /// ENTRY VHVNIH #type complete TITLE nucleoprotein - infectious hematopoietic necrosis virus ALTERNATE_NAMES nucleocapsid protein ORGANISM #formal_name infectious hematopoietic necrosis virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS A31834 REFERENCE A31834 !$#authors Gilmore Jr., R.D.; Leong, J.C. !$#journal Virology (1988) 167:644-648 !$#title The nucleocapsid gene of infectious hematopoietic necrosis !1virus, a fish rhabdovirus. !$#cross-references MUID:89073771; PMID:3201758 !$#accession A31834 !'##molecule_type mRNA !'##residues 1-413 ##label GIL !'##cross-references GB:J04321; NID:g331304; PIDN:AAA46240.1; !1PID:g331305 CLASSIFICATION #superfamily infectious hematopoietic necrosis virus !1nucleoprotein KEYWORDS nucleocapsid; nucleoprotein SUMMARY #length 413 #molecular-weight 45700 #checksum 2727 SEQUENCE /// ENTRY VHVNHS #type complete TITLE nucleoprotein - hemorrhagic septicemia virus ALTERNATE_NAMES nucleocapsid protein ORGANISM #formal_name hemorrhagic septicemia virus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jun-2000 ACCESSIONS A36651 REFERENCE A36651 !$#authors Bernard, J.; Lecocq-Xhonneux, F.; Rossius, M.; Thiry, M.E.; !1de Kinkelin, P. !$#journal J. Gen. Virol. (1990) 71:1669-1674 !$#title Cloning and sequencing the messenger RNA of the N gene of !1viral haemorrhagic septicaemia virus. !$#cross-references MUID:90362052; PMID:2202782 !$#accession A36651 !'##molecule_type mRNA !'##residues 1-404 ##label BER !'##cross-references GB:D00687; NID:g222771; PIDN:BAA00591.1; !1PID:g222772 GENETICS !$#gene N CLASSIFICATION #superfamily infectious hematopoietic necrosis virus !1nucleoprotein KEYWORDS nucleocapsid; nucleoprotein SUMMARY #length 404 #molecular-weight 44369 #checksum 9647 SEQUENCE /// ENTRY JQ1531 #type complete TITLE nucleoprotein - hemorrhagic septicemia virus (strain Makah) ALTERNATE_NAMES nucleocapsid protein ORGANISM #formal_name hemorrhagic septicemia virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS JQ1531; S21836 REFERENCE JQ1531 !$#authors Bernard, J.; Bremont, M.; Winton, J. !$#journal J. Gen. Virol. (1992) 73:1011-1014 !$#title Nucleocapsid gene sequence of a North American isolate of !1viral haemorrhagic septicaemia virus, a fish rhabdovirus. !$#cross-references MUID:92341050; PMID:1634868 !$#accession JQ1531 !'##molecule_type mRNA !'##residues 1-404 ##label BER !'##cross-references EMBL:X59241; NID:g60410; PIDN:CAA41930.1; !1PID:g60411 GENETICS !$#gene N CLASSIFICATION #superfamily infectious hematopoietic necrosis virus !1nucleoprotein KEYWORDS nucleocapsid; nucleoprotein SUMMARY #length 404 #molecular-weight 44066 #checksum 7775 SEQUENCE /// ENTRY VGVN #type complete TITLE spike glycoprotein G precursor - vesicular stomatitis Indiana virus (strain San Juan) ORGANISM #formal_name vesicular stomatitis Indiana virus DATE 31-Mar-1981 #sequence_revision 19-Feb-1984 #text_change 16-Jul-1999 ACCESSIONS A04117 REFERENCE A92983 !$#authors Rose, J.K.; Gallione, C.J. !$#journal J. Virol. (1981) 39:519-528 !$#title Nucleotide sequences of the mRNA's encoding the vesicular !1stomatitis virus G and M proteins determined from cDNA !1clones containing the complete coding regions. !$#cross-references MUID:82010868; PMID:6268840 !$#accession A04117 !'##molecule_type mRNA !'##residues 1-511 ##label ROS !'##cross-references GB:J02428; NID:g335873; PIDN:AAA48370.1; !1PID:g335877 GENETICS !$#gene G CLASSIFICATION #superfamily rhabdovirus spike glycoprotein G KEYWORDS glycoprotein; spike protein; transmembrane protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-511 #product spike glycoprotein G #status predicted !8#label SGG\ !$465-481 #domain transmembrane #status predicted #label TMN\ !$179,336 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 511 #molecular-weight 57481 #checksum 9374 SEQUENCE /// ENTRY VGVNVJ #type complete TITLE spike glycoprotein G precursor - vesicular stomatitis New Jersey virus ORGANISM #formal_name vesicular stomatitis New Jersey virus DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 16-Jul-1999 ACCESSIONS A04118 REFERENCE A04118 !$#authors Gallione, C.J.; Rose, J.K. !$#journal J. Virol. (1983) 46:162-169 !$#title Nucleotide sequence of a cDNA clone encoding the entire !1glycoprotein from the New Jersey serotype of vesicular !1stomatitis virus. !$#cross-references MUID:83138980; PMID:6298453 !$#accession A04118 !'##molecule_type mRNA !'##residues 1-517 ##label GAL !'##cross-references GB:V01214; NID:g61839; PIDN:CAA24525.1; PID:g61840 GENETICS !$#gene G CLASSIFICATION #superfamily rhabdovirus spike glycoprotein G KEYWORDS glycoprotein; spike protein; transmembrane protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-517 #product spike glycoprotein G #status predicted !8#label SGG\ !$473-489 #domain transmembrane #status predicted #label TMN\ !$179,340 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 517 #molecular-weight 58229 #checksum 2066 SEQUENCE /// ENTRY VGVNFR #type complete TITLE spike glycoprotein G precursor - infectious hematopoietic necrosis virus (strain Round Butte) ORGANISM #formal_name infectious hematopoietic necrosis virus #note host Oncorhynchus tschawytscha (chinook salmon) DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 09-Sep-1994 ACCESSIONS A29532 REFERENCE A29532 !$#authors Koener, J.F.; Passavant, C.W.; Kurath, G.; Leong, J. !$#journal J. Virol. (1987) 61:1342-1349 !$#title Nucleotide sequence of a cDNA clone carrying the !1glycoprotein gene of infectious hematopoietic necrosis !1virus, a fish Rhabdovirus. !$#cross-references MUID:87198856; PMID:3033264 !$#accession A29532 !'##molecule_type mRNA !'##residues 1-508 ##label KOE !'##cross-references GB:M16023 GENETICS !$#gene G CLASSIFICATION #superfamily rhabdovirus spike glycoprotein G KEYWORDS glycoprotein; spike protein; transmembrane protein FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-508 #product spike glycoprotein G #status predicted !8#label SGG\ !$469-485 #domain transmembrane #status predicted #label TMN\ !$56,400,401,438 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 508 #molecular-weight 56785 #checksum 4253 SEQUENCE /// ENTRY VGVNCV #type complete TITLE spike glycoprotein G precursor - Chandipura virus ORGANISM #formal_name Chandipura virus DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS A32443 REFERENCE A32443 !$#authors Masters, P.S.; Bella, R.S.; Butcher, M.; Patel, B.; Ghosh, !1H.P.; Banerjee, A.K. !$#journal Virology (1989) 171:285-290 !$#title Structure and expression of the glycoprotein gene of !1Chandipura virus. !$#cross-references MUID:89299473; PMID:2741347 !$#accession A32443 !'##molecule_type mRNA !'##residues 1-524 ##label MAS !'##cross-references GB:J04350; NID:g323376; PIDN:AAA42916.1; !1PID:g323377 GENETICS !$#gene G CLASSIFICATION #superfamily rhabdovirus spike glycoprotein G KEYWORDS glycoprotein; spike protein; transmembrane protein FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-524 #product spike glycoprotein G #status predicted !8#label SGG\ !$472-491 #domain transmembrane #status predicted #label TMN\ !$184,344 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 524 #molecular-weight 58826 #checksum 2589 SEQUENCE /// ENTRY VGVNSG #type complete TITLE spike glycoprotein G precursor - sigma virus ORGANISM #formal_name sigma virus #note host Drosophila melanogaster DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jul-1999 ACCESSIONS A27150 REFERENCE A27150 !$#authors Teninges, D.; Bras-Herreng, F. !$#journal J. Gen. Virol. (1987) 68:2625-2638 !$#title Rhabdovirus sigma, the hereditary CO-2 sensitivity agent of !1Drosophila: nucleotide sequence of a cDNA clone encoding the !1glycoprotein. !$#cross-references MUID:88034947; PMID:2822842 !$#accession A27150 !'##molecule_type genomic RNA !'##residues 1-526 ##label TEN !'##cross-references GB:X06171; NID:g61818; PIDN:CAA29536.1; PID:g61819 GENETICS !$#gene G !'##cross-references FlyBase:FBgn0015809 CLASSIFICATION #superfamily rhabdovirus spike glycoprotein G KEYWORDS glycoprotein; spike protein; transmembrane protein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-526 #product spike glycoprotein G #status predicted !8#label SGG\ !$499-515 #domain transmembrane #status predicted #label TMN\ !$32,445,459 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 526 #molecular-weight 59010 #checksum 8550 SEQUENCE /// ENTRY VGVNBE #type complete TITLE spike glycoprotein G precursor - bovine ephemeral fever virus ORGANISM #formal_name bovine ephemeral fever virus DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS A44060; C44060 REFERENCE A44060 !$#authors Walker, P.J.; Byrne, K.A.; Riding, G.A.; Cowley, J.A.; Wang, !1Y.; McWilliam, S. !$#journal Virology (1992) 191:49-61 !$#title The genome of bovine ephemeral fever rhabdovirus contains !1two related glycoprotein genes. !$#cross-references MUID:93033149; PMID:1413521 !$#accession A44060 !'##molecule_type genomic RNA !'##residues 1-623 ##label WA1 !'##cross-references GB:M94266; NID:g210703; PIDN:AAA42760.1; !1PID:g210704 !$#accession C44060 !'##molecule_type protein !'##residues 17-28;90-99;210-220;349-367 ##label WA2 GENETICS !$#gene G CLASSIFICATION #superfamily rhabdovirus spike glycoprotein G KEYWORDS glycoprotein; spike protein; transmembrane protein FEATURE !$1-12 #domain signal sequence #status predicted #label SIG\ !$13-623 #product spike glycoprotein G #status predicted !8#label SGG\ !$540-554 #domain transmembrane #status predicted #label TMN\ !$175,264,416,438,507 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 623 #molecular-weight 72284 #checksum 3483 SEQUENCE /// ENTRY VGVNBF #type complete TITLE nonstructural glycoprotein Gns precursor - bovine ephemeral fever virus ORGANISM #formal_name bovine ephemeral fever virus DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS B44060 REFERENCE A44060 !$#authors Walker, P.J.; Byrne, K.A.; Riding, G.A.; Cowley, J.A.; Wang, !1Y.; McWilliam, S. !$#journal Virology (1992) 191:49-61 !$#title The genome of bovine ephemeral fever rhabdovirus contains !1two related glycoprotein genes. !$#cross-references MUID:93033149; PMID:1413521 !$#accession B44060 !'##molecule_type genomic RNA !'##residues 1-586 ##label WAL !'##cross-references GB:M94266; NID:g210703; PIDN:AAA42761.1; !1PID:g210705 CLASSIFICATION #superfamily rhabdovirus spike glycoprotein G KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-14 #domain signal sequence #status predicted #label SIG\ !$15-586 #product nonstructural glycoprotein Gns #status !8predicted #label NGG\ !$546-562 #domain transmembrane #status predicted #label TMN\ !$27,68,274,350,383, !$476,501,521 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 586 #molecular-weight 68811 #checksum 5493 SEQUENCE /// ENTRY VGVNG #type complete TITLE spike glycoprotein precursor - rabies virus (strain ERA) ORGANISM #formal_name rabies virus DATE 02-Apr-1982 #sequence_revision 02-Apr-1982 #text_change 23-Aug-1997 ACCESSIONS A04121 REFERENCE A04121 !$#authors Anilionis, A.; Wunner, W.H.; Curtis, P.J. !$#journal Nature (1981) 294:275-278 !$#title Structure of the glycoprotein gene in rabies virus. !$#cross-references MUID:82058119; PMID:6272128 !$#accession A04121 !'##molecule_type mRNA !'##residues 1-524 ##label ANI GENETICS !$#gene G CLASSIFICATION #superfamily rabies virus spike glycoprotein KEYWORDS glycoprotein; spike protein; transmembrane protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-524 #product spike glycoprotein #status predicted #label !8SGP\ !$56,266,338,484 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 524 #molecular-weight 58658 #checksum 9404 SEQUENCE /// ENTRY VGVNRV #type complete TITLE spike glycoprotein precursor - rabies virus ORGANISM #formal_name rabies virus DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Jul-1999 ACCESSIONS C26275; D24887 REFERENCE A94100 !$#authors Tordo, N.; Poch, O.; Ermine, A.; Keith, G.; Rougeon, F. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:3914-3918 !$#title Walking along the rabies genome: is the large G-L intergenic !1region a remnant gene? !$#cross-references MUID:86233343; PMID:3459163 !$#accession C26275 !'##molecule_type genomic RNA !'##residues 1-524 ##label TOR !'##cross-references GB:M13215; GB:M21634; NID:g333585; PIDN:AAA47218.1; !1PID:g333589 GENETICS !$#gene G CLASSIFICATION #superfamily rabies virus spike glycoprotein KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-524 #product spike glycoprotein #status predicted #label !8SGP\ !$56,266,338,484 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 524 #molecular-weight 58535 #checksum 9076 SEQUENCE /// ENTRY VGVNSB #type complete TITLE spike glycoprotein precursor - rabies virus (strain SAD B19) ORGANISM #formal_name rabies virus DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS D34746 REFERENCE A34746 !$#authors Conzelmann, K.K.; Cox, J.H.; Schneider, L.G.; Thiel, H.J. !$#journal Virology (1990) 175:485-499 !$#title Molecular cloning and complete nucleotide sequence of the !1attenuated rabies virus SAD B19. !$#cross-references MUID:90223994; PMID:2139267 !$#accession D34746 !'##molecule_type genomic RNA !'##residues 1-524 ##label CON !'##cross-references GB:M31046; NID:g333556; PIDN:AAA47202.1; !1PID:g333560 GENETICS !$#gene G CLASSIFICATION #superfamily rabies virus spike glycoprotein KEYWORDS glycoprotein; spike protein; transmembrane protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-524 #product spike glycoprotein #status predicted #label !8SGP\ !$56,266,338,484 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 524 #molecular-weight 58626 #checksum 9986 SEQUENCE /// ENTRY VGVNRB #type complete TITLE spike glycoprotein precursor - rabies virus (strain HEP-Flury) ORGANISM #formal_name rabies virus DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Jul-1999 ACCESSIONS A33745 REFERENCE A33745 !$#authors Morimoto, K.; Ohkubo, A.; Kawai, A. !$#journal Virology (1989) 173:465-477 !$#title Structure and transcription of the glycoprotein gene of !1attenuated HEP-Flury strain of rabies virus. !$#cross-references MUID:90085795; PMID:2596027 !$#accession A33745 !'##molecule_type mRNA !'##residues 1-524 ##label MOR !'##cross-references GB:M32751; NID:g333581; PIDN:AAA47213.1; !1PID:g333582 GENETICS !$#gene G CLASSIFICATION #superfamily rabies virus spike glycoprotein KEYWORDS glycoprotein; spike protein; transmembrane protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-524 #product spike glycoprotein #status predicted #label !8SGP\ !$56,177,338,499 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 524 #molecular-weight 58583 #checksum 9879 SEQUENCE /// ENTRY VGVNDB #type complete TITLE spike glycoprotein precursor - rabies virus (strain street) ORGANISM #formal_name rabies virus DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 09-Sep-1994 ACCESSIONS A42189 REFERENCE A42189 !$#authors Benmansour, A.; Brahimi, M.; Tuffereau, C.; Coulon, P.; !1Lafay, F.; Flamand, A. !$#journal Virology (1992) 187:33-45 !$#title Rapid sequence evolution of street rabies glycoprotein is !1related to the highly heterogeneous nature of the viral !1population. !$#cross-references MUID:92142521; PMID:1736537 !$#accession A42189 !'##molecule_type genomic RNA !'##residues 1-524 ##label BEN !'##cross-references GB:M81059 CLASSIFICATION #superfamily rabies virus spike glycoprotein KEYWORDS glycoprotein; spike protein; transmembrane protein FEATURE !$1-19 #domain signal sequence #status predicted #label SIG\ !$20-524 #product spike glycoprotein #status predicted #label !8SGP\ !$460-476 #domain transmembrane #status predicted #label TMN\ !$56,177,338 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 524 #molecular-weight 58692 #checksum 9051 SEQUENCE /// ENTRY VGVNSY #type complete TITLE surface glycoprotein G precursor - Sonchus yellow net virus ORGANISM #formal_name Sonchus yellow net virus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS A40776 REFERENCE A40776 !$#authors Goldberg, K.B.; Modrell, B.; Hillman, B.I.; Heaton, L.A.; !1Choi, T.J.; Jackson, A.O. !$#journal Virology (1991) 185:32-38 !$#title Structure of the glycoprotein gene of Sonchus yellow net !1virus, a plant rhabdovirus. !$#cross-references MUID:92024089; PMID:1926779 !$#accession A40776 !'##molecule_type genomic RNA !'##residues 1-632 ##label GOL !'##cross-references GB:M73626; NID:g335143; PIDN:AAA47898.1; !1PID:g335144 CLASSIFICATION #superfamily plant rhabdovirus surface glycoprotein G KEYWORDS glycoprotein; transmembrane protein FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-632 #product surface glycoprotein G #status predicted !8#label SGG\ !$560-578 #domain transmembrane #status predicted #label TMN\ !$39,93,385,501,512, !$541 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 632 #molecular-weight 71093 #checksum 3963 SEQUENCE /// ENTRY MWXR31 #type complete TITLE lambda 3 protein - reovirus type 1 (strain Lang) ALTERNATE_NAMES minor core protein ORGANISM #formal_name reovirus type 1 DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 12-Feb-1999 ACCESSIONS A30121 REFERENCE A94390 !$#authors Wiener, J.R.; Joklik, W.K. !$#journal Virology (1989) 169:194-203 !$#title The sequences of the reovirus serotype 1, 2, and 3 L1 genome !1segments and analysis of the mode of divergence of the !1reovirus serotypes. !$#cross-references MUID:89163254; PMID:2922925 !$#accession A30121 !'##molecule_type genomic RNA !'##residues 1-1267 ##label WIE !'##cross-references GB:M24734; NID:g499863 !'##note this sequence, which matches the sequence attributed to type 1 !1in Fig. 2, matched the original sequence attributed to type !11 in GenBank entry REO1LAM3P before it was corrected in June !11994; the translations in entries REO1LAM3P and REO3LAM3P !1now differ only by the sequence correction apparently made !1to the wrong entry COMMENT See also PIR:MWXR33. GENETICS !$#map_position segment L1 CLASSIFICATION #superfamily reovirus lambda 3 protein KEYWORDS core protein SUMMARY #length 1267 #molecular-weight 142354 #checksum 3511 SEQUENCE /// ENTRY MWXR33 #type complete TITLE lambda 3 protein - reovirus type 3 (strain Dearing) ALTERNATE_NAMES minor core protein ORGANISM #formal_name reovirus type 3 DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS C30121 REFERENCE A94390 !$#authors Wiener, J.R.; Joklik, W.K. !$#journal Virology (1989) 169:194-203 !$#title The sequences of the reovirus serotype 1, 2, and 3 L1 genome !1segments and analysis of the mode of divergence of the !1reovirus serotypes. !$#cross-references MUID:89163254; PMID:2922925 !$#accession C30121 !'##molecule_type genomic RNA !'##residues 1-1267 ##label WIE !'##cross-references GB:M31058; NID:g499867; GB:M24734; NID:g499863; !1PIDN:AAA47234.1; PID:g499864 !'##note this sequence, which matches the sequence attributed to type 3 !1in Fig. 2, matches the sequence attributed to type 1 in !1GenBank entry REO1LAM3P as corrected in June 1994; the !1translations in entries REO1LAM3P and REO3LAM3P now differ !1only by the sequence correction apparently made to the wrong !1entry COMMENT See also PIR:MWXR31. GENETICS !$#map_position segment L1 CLASSIFICATION #superfamily reovirus lambda 3 protein KEYWORDS core protein SUMMARY #length 1267 #molecular-weight 142269 #checksum 3075 SEQUENCE /// ENTRY MWXR32 #type complete TITLE lambda 3 protein - reovirus type 2 (strain D5/Jones) ALTERNATE_NAMES minor core protein ORGANISM #formal_name reovirus type 2 #note host Homo sapiens (man) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS B30121 REFERENCE A94390 !$#authors Wiener, J.R.; Joklik, W.K. !$#journal Virology (1989) 169:194-203 !$#title The sequences of the reovirus serotype 1, 2, and 3 L1 genome !1segments and analysis of the mode of divergence of the !1reovirus serotypes. !$#cross-references MUID:89163254; PMID:2922925 !$#accession B30121 !'##molecule_type genomic RNA !'##residues 1-1267 ##label WIE !'##cross-references GB:M31057; NID:g499865; PIDN:AAA47245.1; !1PID:g499866 GENETICS !$#map_position segment L1 CLASSIFICATION #superfamily reovirus lambda 3 protein KEYWORDS core protein SUMMARY #length 1267 #molecular-weight 142287 #checksum 7880 SEQUENCE /// ENTRY HMXRL1 #type complete TITLE sigma 1 protein - reovirus type 1 (strain Lang) ALTERNATE_NAMES hemagglutinin; minor outer capsid protein ORGANISM #formal_name reovirus type 1 #note host Homo sapiens (man) DATE 30-Jun-1988 #sequence_revision 22-Oct-1999 #text_change 22-Oct-1999 ACCESSIONS A34829; A26436 REFERENCE A34829 !$#authors Nibert, M.L.; Dermody, T.S.; Fields, B.N. !$#journal J. Virol. (1990) 64:2976-2989 !$#title Structure of the reovirus cell-attachment protein: a model !1for the domain organization of sigma1. !$#cross-references MUID:90244415; PMID:2335823 !$#accession A34829 !'##status preliminary !'##molecule_type genomic RNA !'##residues 1-470 ##label NIB REFERENCE A90128 !$#authors Munemitsu, S.M.; Atwater, J.A.; Samuel, C.E. !$#journal Biochem. Biophys. Res. Commun. (1986) 140:508-514 !$#title Biosynthesis of reovirus-specified polypeptides: molecular !1cDNA cloning and nucleotide sequence of the reovirus !1serotype 1 Lang strain bicistronic s1 mRNA which encodes the !1minor capsid polypeptide sigma-1a and the nonstructural !1polypeptide sigma-1bNS. !$#cross-references MUID:87048799; PMID:2430568 !$#accession A26436 !'##molecule_type mRNA !'##residues 1-90,'G',92-383,'L',385-409,'LRHLPRSN',418 ##label MUN !'##cross-references GB:M14779; NID:g333744; PIDN:AAA47276.1; !1PID:g333745 !'##note the authors translated the codon CAA for residue 86 as Glu GENETICS !$#map_position segment S1 CLASSIFICATION #superfamily reovirus sigma 1 protein KEYWORDS glycoprotein; hemagglutinin; outer capsid protein FEATURE !$21,121,205,353 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 470 #molecular-weight 51403 #checksum 3616 SEQUENCE /// ENTRY HMXRH1 #type complete TITLE sigma 1 protein - reovirus type 1 ALTERNATE_NAMES hemagglutinin ORGANISM #formal_name reovirus type 1 #note host Homo sapiens (man) DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 16-Jul-1999 ACCESSIONS A04122 REFERENCE A94035 !$#authors Cashdollar, L.W.; Chmelo, R.A.; Wiener, J.R.; Joklik, W.K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:24-28 !$#title Sequences of the S1 genes of the three serotypes of !1reovirus. !$#cross-references MUID:85113159; PMID:3855545 !$#accession A04122 !'##molecule_type genomic RNA !'##residues 1-418 ##label CAS !'##cross-references GB:M10260; NID:g808811; PIDN:AAA66877.1; !1PID:g333739 !'##note the authors translated the codon TTC for residue 169 as Ser, !1AAA for residue 189 as Leu, and TGG for residue 203 as Thr GENETICS !$#gene S1; sigma 1 CLASSIFICATION #superfamily reovirus sigma 1 protein KEYWORDS glycoprotein; hemagglutinin FEATURE !$21,121,205,353 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 418 #molecular-weight 45554 #checksum 1346 SEQUENCE /// ENTRY HMXRH2 #type complete TITLE sigma 1 protein - reovirus type 2 ALTERNATE_NAMES hemagglutinin ORGANISM #formal_name reovirus type 2 #note host Homo sapiens (man) DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 16-Jul-1999 ACCESSIONS A04123 REFERENCE A94035 !$#authors Cashdollar, L.W.; Chmelo, R.A.; Wiener, J.R.; Joklik, W.K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:24-28 !$#title Sequences of the S1 genes of the three serotypes of !1reovirus. !$#cross-references MUID:85113159; PMID:3855545 !$#accession A04123 !'##molecule_type genomic RNA !'##residues 1-399 ##label CAS !'##cross-references GB:M10261; NID:g808813; PIDN:AAA66879.1; !1PID:g333741 GENETICS !$#gene S1; sigma 1 CLASSIFICATION #superfamily reovirus sigma 1 protein KEYWORDS glycoprotein; hemagglutinin FEATURE !$237,243,297 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 399 #molecular-weight 44304 #checksum 3097 SEQUENCE /// ENTRY HMXRS3 #type complete TITLE sigma 1 protein precursor - reovirus type 3 ALTERNATE_NAMES hemagglutinin S1 ORGANISM #formal_name reovirus type 3 #note host Homo sapiens (man) DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 16-Jul-1999 ACCESSIONS A93360; A93545; A94035; A21900; A04124; A23880 REFERENCE A93360 !$#authors Bassel-Duby, R.; Jayasuriya, A.; Chatterjee, D.; Sonenberg, !1N.; Maizel Jr., J.V.; Fields, B.N. !$#journal Nature (1985) 315:421-423 !$#title Sequence of reovirus haemagglutinin predicts a coiled-coil !1structure. !$#cross-references MUID:85213868; PMID:4000269 !$#accession A93360 !'##molecule_type genomic RNA !'##residues 1-455 ##label BAS REFERENCE A93545 !$#authors Nagata, L.; Masri, S.A.; Mah, D.C.W.; Lee, P.W.K. !$#journal Nucleic Acids Res. (1984) 12:8699-8710 !$#title Molecular cloning and sequencing of the reovirus (serotype !13) S1 gene which encodes the viral cell attachment protein !1sigma 1. !$#cross-references MUID:85062842; PMID:6095208 !$#accession A93545 !'##molecule_type genomic RNA !'##residues 1-21,'A',23-117,'DV',120-407,'A',409-455 ##label NAG !'##cross-references GB:M32094; GB:X01161; NID:g333696; PID:g333697 REFERENCE A94035 !$#authors Cashdollar, L.W.; Chmelo, R.A.; Wiener, J.R.; Joklik, W.K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:24-28 !$#title Sequences of the S1 genes of the three serotypes of !1reovirus. !$#cross-references MUID:85113159; PMID:3855545 !$#accession A94035 !'##molecule_type genomic RNA !'##residues 1-21,'A',23-162,'T',164-407,'A',409-455 ##label CAS !'##cross-references GB:M10262; NID:g333742; PIDN:AAA47275.1; !1PID:g333743 REFERENCE A21900 !$#authors Ernst, H.; Shatkin, A.J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:48-52 !$#cross-references MUID:85113169; PMID:3855548 !$#accession A21900 !'##molecule_type mRNA !'##residues 1-26 ##label ERN GENETICS !$#gene S1; sigma 1 CLASSIFICATION #superfamily reovirus sigma 1 protein KEYWORDS glycoprotein; hemagglutinin FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-455 #product sigma 1 protein #status predicted #label !8SIP\ !$27-160 #domain helical #status predicted #label HLX\ !$231,264,282 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 455 #molecular-weight 49153 #checksum 9851 SEQUENCE /// ENTRY FOXRL2 #type complete TITLE sigma 2 protein - reovirus type 1 (strain Lang) ALTERNATE_NAMES core protein ORGANISM #formal_name reovirus type 1 #note host Homo sapiens (man) DATE 31-Mar-1989 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS A41306; A29708 REFERENCE A41306 !$#authors Dermody, T.S.; Schiff, L.A.; Nibert, M.L.; Coombs, K.M.; !1Fields, B.N. !$#journal J. Virol. (1991) 65:5721-5731 !$#title The S2 gene nucleotide sequences of prototype strains of the !1three reovirus serotypes: characterization of reovirus core !1protein sigma2. !$#cross-references MUID:92015462; PMID:1920614 !$#accession A41306 !'##molecule_type genomic RNA !'##residues 1-418 ##label DER !'##cross-references GB:S59098 REFERENCE A29708 !$#authors George, C.X.; Crowe, A.; Munemitsu, S.M.; Atwater, J.A.; !1Samuel, C.E. !$#journal Biochem. Biophys. Res. Commun. (1987) 147:1153-1161 !$#title Biosynthesis of reovirus-specified polypeptides. Molecular !1cDNA cloning and nucleotide sequence of the reovirus !1serotype 1 Lang strain s2 mRNA which encodes the virion core !1polypeptide sigma-2. !$#cross-references MUID:88024195; PMID:3663211 !$#accession A29708 !'##molecule_type genomic RNA !'##residues 1-88,'V',90-204,'Y',206-322,'VATSCMVSKCDEW' ##label GEO !'##cross-references GB:M17598; NID:g333748; PIDN:AAA47278.1; !1PID:g333749 GENETICS !$#map_position segment S2 CLASSIFICATION #superfamily reovirus sigma 2 protein KEYWORDS core protein SUMMARY #length 418 #molecular-weight 47110 #checksum 6814 SEQUENCE /// ENTRY FOXR3D #type complete TITLE sigma 2 protein - reovirus type 3 (strain Dearing) ALTERNATE_NAMES core protein ORGANISM #formal_name reovirus type 3 #note host Homo sapiens (man) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS A31475; C41306; A04125 REFERENCE A31475 !$#authors Wiener, J.R.; McLaughlin, T.; Joklik, W.K. !$#journal Virology (1989) 170:340-341 !$#title The sequences of the S2 genome segments of reovirus serotype !13 and of the dsRNA-negative mutant ts447. !$#cross-references MUID:89243203; PMID:2718385 !$#accession A31475 !'##molecule_type genomic RNA !'##residues 1-418 ##label WIE !'##cross-references GB:M25780; NID:g333750; PIDN:AAA47279.1; !1PID:g333751 !'##note the sequence from the mutant ts447 differs from that shown in !1having 188-Val, 323-Val, and 383-Asp REFERENCE A41306 !$#authors Dermody, T.S.; Schiff, L.A.; Nibert, M.L.; Coombs, K.M.; !1Fields, B.N. !$#journal J. Virol. (1991) 65:5721-5731 !$#title The S2 gene nucleotide sequences of prototype strains of the !1three reovirus serotypes: characterization of reovirus core !1protein sigma2. !$#cross-references MUID:92015462; PMID:1920614 !$#accession C41306 !'##molecule_type genomic RNA !'##residues 1-204,'H',206-356,'I',358-418 ##label DER !'##cross-references GB:S59098 REFERENCE A04125 !$#authors Cashdollar, L.W.; Esparza, J.; Hudson, G.R.; Chmelo, R.; !1Lee, P.W.K.; Joklik, W.K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:7644-7648 !$#title Cloning the double-stranded RNA genes of reovirus: sequences !1of the cloned S2 gene. !$#cross-references MUID:83117734; PMID:6961439 !$#accession A04125 !'##molecule_type genomic RNA !'##residues 1-258,'Y',260-309,'LQCRVTSMAGLVELVTNCMGSR' ##label CAS !'##cross-references GB:J02327 GENETICS !$#map_position segment S2 CLASSIFICATION #superfamily reovirus sigma 2 protein KEYWORDS core protein SUMMARY #length 418 #molecular-weight 47161 #checksum 8516 SEQUENCE /// ENTRY FOXRJS #type complete TITLE sigma 2 protein - reovirus type 2 (strain Jones) ALTERNATE_NAMES core protein ORGANISM #formal_name reovirus type 2 #note host Homo sapiens (man) DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 07-May-1999 ACCESSIONS B41306 REFERENCE A41306 !$#authors Dermody, T.S.; Schiff, L.A.; Nibert, M.L.; Coombs, K.M.; !1Fields, B.N. !$#journal J. Virol. (1991) 65:5721-5731 !$#title The S2 gene nucleotide sequences of prototype strains of the !1three reovirus serotypes: characterization of reovirus core !1protein sigma2. !$#cross-references MUID:92015462; PMID:1920614 !$#accession B41306 !'##molecule_type genomic RNA !'##residues 1-418 ##label DER !'##cross-references GB:S59098 GENETICS !$#map_position segment S2 CLASSIFICATION #superfamily reovirus sigma 2 protein KEYWORDS core protein SUMMARY #length 418 #molecular-weight 47045 #checksum 5426 SEQUENCE /// ENTRY MNXRSD #type complete TITLE sigma NS protein - reovirus type 3 (strain Dearing) ALTERNATE_NAMES core protein; RNA-binding protein ORGANISM #formal_name reovirus type 3 #note host Homo sapiens (man) DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 16-Jul-1999 ACCESSIONS A04126 REFERENCE A04126 !$#authors Richardson, M.A.; Furuichi, Y. !$#journal Nucleic Acids Res. (1983) 11:6399-6408 !$#title Nucleotide sequence of reovirus genome segment S3, encoding !1non-structural protein sigma NS. !$#cross-references MUID:84015379; PMID:6312421 !$#accession A04126 !'##molecule_type genomic RNA !'##residues 1-366 ##label RIC !'##cross-references GB:X01627; NID:g61560; PIDN:CAA25768.1; PID:g61561 COMMENT This genome consists of 10 segments of linear, !1double-stranded RNA. COMMENT This protein comprises 36% alpha-helix, 31% beta-sheet, and !133% coiled regions. COMMENT This protein has a poly(C)-dependent poly(G) polymerase !1activity, and binds single-stranded, but not !1double-stranded, RNA. GENETICS !$#map_position segment 3 CLASSIFICATION #superfamily reovirus sigma NS protein KEYWORDS core protein; RNA binding SUMMARY #length 366 #molecular-weight 41056 #checksum 5712 SEQUENCE /// ENTRY MNXRST #type complete TITLE sigma NS protein - reovirus type 1 (strain Lang) ALTERNATE_NAMES nonstructural RNA-binding protein ORGANISM #formal_name reovirus type 1 #note host Homo sapiens (man) DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 16-Jul-1999 ACCESSIONS A25068; A27401 REFERENCE A90127 !$#authors George, C.X.; Atwater, J.A.; Samuel, C.E. !$#journal Biochem. Biophys. Res. Commun. (1986) 139:845-851 !$#title Biosynthesis of reovirus-specified polypeptides: molecular !1cDNA cloning and nucleotide sequence of the reovirus !1serotype 1 Lang strain s3 mRNA which encodes the !1nonstructural RNA-binding protein sigma NS. !$#cross-references MUID:87025802; PMID:3767989 !$#accession A25068 !'##molecule_type mRNA !'##residues 1-366 ##label GEO !'##cross-references GB:M14325; NID:g333734; PIDN:AAA47273.1; !1PID:g333735 REFERENCE A27401 !$#authors Wiener, J.R.; Joklik, W.K. !$#journal Virology (1987) 161:332-339 !$#title Comparison of the reovirus serotype 1, 2, and 3 S3 genome !1segments encoding the nonstructural protein sigma-NS. !$#cross-references MUID:88072071; PMID:3686825 !$#accession A27401 !'##molecule_type genomic RNA !'##residues 1-366 ##label WIE !'##cross-references GB:M18389 !'##note the authors translated the codon UUG for residue 359 as Ile GENETICS !$#map_position segment S3 CLASSIFICATION #superfamily reovirus sigma NS protein KEYWORDS core protein; nonstructural protein; RNA binding SUMMARY #length 366 #molecular-weight 41188 #checksum 6487 SEQUENCE /// ENTRY MNXRT2 #type complete TITLE sigma NS protein - reovirus type 2 (strain D5/Jones) ALTERNATE_NAMES nonstructural RNA-binding protein ORGANISM #formal_name reovirus type 2 #note host Homo sapiens (man) DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 08-Apr-1994 ACCESSIONS B27401 REFERENCE A27401 !$#authors Wiener, J.R.; Joklik, W.K. !$#journal Virology (1987) 161:332-339 !$#title Comparison of the reovirus serotype 1, 2, and 3 S3 genome !1segments encoding the nonstructural protein sigma-NS. !$#cross-references MUID:88072071; PMID:3686825 !$#accession B27401 !'##molecule_type genomic RNA !'##residues 1-366 ##label WIE !'##note the authors translated the codon CUC for residue 359 as Ile GENETICS !$#map_position segment S3 CLASSIFICATION #superfamily reovirus sigma NS protein KEYWORDS core protein; nonstructural protein; RNA binding SUMMARY #length 366 #molecular-weight 41305 #checksum 4649 SEQUENCE /// ENTRY MNXR1B #type complete TITLE sigma 1bNS protein - reovirus type 1 (strain Lang) ALTERNATE_NAMES nonstructural protein ORGANISM #formal_name reovirus type 1 #note host Homo sapiens (man) DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 16-Jul-1999 ACCESSIONS B26436 REFERENCE A90128 !$#authors Munemitsu, S.M.; Atwater, J.A.; Samuel, C.E. !$#journal Biochem. Biophys. Res. Commun. (1986) 140:508-514 !$#title Biosynthesis of reovirus-specified polypeptides: molecular !1cDNA cloning and nucleotide sequence of the reovirus !1serotype 1 Lang strain bicistronic s1 mRNA which encodes the !1minor capsid polypeptide sigma-1a and the nonstructural !1polypeptide sigma-1bNS. !$#cross-references MUID:87048799; PMID:2430568 !$#accession B26436 !'##molecule_type mRNA !'##residues 1-119 ##label MUN !'##cross-references GB:M14779; NID:g333744; PIDN:AAA47277.1; !1PID:g333746 !'##note the authors translated the codon CAA for residue 5 as Glu GENETICS !$#map_position segment S1 CLASSIFICATION #superfamily reovirus sigma 1bNS protein KEYWORDS nonstructural protein SUMMARY #length 119 #molecular-weight 13989 #checksum 8404 SEQUENCE /// ENTRY MNXRS4 #type complete TITLE sigma 3 protein - reovirus type 1 (strain Lang) ALTERNATE_NAMES major capsid surface protein ORGANISM #formal_name reovirus type 1 DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 01-Dec-2000 ACCESSIONS A24245; A42192; S17372 REFERENCE A24245 !$#authors Atwater, J.A.; Munemitsu, S.M.; Samuel, C.E. !$#journal Biochem. Biophys. Res. Commun. (1986) 136:183-192 !$#title Biosynthesis of reovirus-specified polypeptides: molecular !1cDNA cloning and nucleotide sequence of the reovirus !1serotype 1 Lang strain s4 mRNA which encodes the major !1capsid surface polypeptide sigma-3. !$#cross-references MUID:86215171; PMID:3518713 !$#accession A24245 !'##molecule_type mRNA !'##residues 1-365 ##label ATW !'##cross-references GB:M13139; NID:g333719; PIDN:AAA47272.1; !1PID:g333720 !'##experimental_source strain Lang REFERENCE A42192 !$#authors Seliger, L.S.; Giantini, M.; Shatkin, A.J. !$#journal Virology (1992) 187:202-210 !$#title Translational effects and sequence comparisons of the three !1serotypes of the reovirus S4 gene. !$#cross-references MUID:92142506; PMID:1736524 !$#accession A42192 !'##molecule_type genomic RNA !'##residues 1-324,'N',326-365 ##label SEL !'##cross-references EMBL:X61586; NID:g61947; PIDN:CAA43783.1; !1PID:g61948 !'##experimental_source strain Lang !'##note submitted to the EMBL Data Library, September 1991 GENETICS !$#map_position segment S4 CLASSIFICATION #superfamily reovirus sigma 3 protein KEYWORDS capsid protein; coat protein SUMMARY #length 365 #molecular-weight 41156 #checksum 3880 SEQUENCE /// ENTRY MNXRS3 #type complete TITLE sigma 3 protein - reovirus type 3 ALTERNATE_NAMES major outer capsid protein ORGANISM #formal_name reovirus type 3 #note host Homo sapiens (man) DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 16-Jul-1999 ACCESSIONS A04127 REFERENCE A04127 !$#authors Giantini, M.; Seliger, L.S.; Furuichi, Y.; Shatkin, A.J. !$#journal J. Virol. (1984) 52:984-987 !$#title Reovirus type 3 genome segment S4: nucleotide sequence of !1the gene encoding a major virion surface protein. !$#cross-references MUID:85033971; PMID:6492267 !$#accession A04127 !'##molecule_type genomic RNA !'##residues 1-365 ##label GIA !'##cross-references GB:K02739; NID:g333759; PIDN:AAA47283.1; !1PID:g333760 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily reovirus sigma 3 protein KEYWORDS coat protein SUMMARY #length 365 #molecular-weight 41160 #checksum 4014 SEQUENCE /// ENTRY MNXRSJ #type complete TITLE sigma 3 protein - reovirus type 2 (strain Jones) ALTERNATE_NAMES major capsid surface protein ORGANISM #formal_name reovirus type 2 #note host Homo sapiens (man) DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS B42192 REFERENCE A42192 !$#authors Seliger, L.S.; Giantini, M.; Shatkin, A.J. !$#journal Virology (1992) 187:202-210 !$#title Translational effects and sequence comparisons of the three !1serotypes of the reovirus S4 gene. !$#cross-references MUID:92142506; PMID:1736524 !$#accession B42192 !'##molecule_type genomic RNA !'##residues 1-365 ##label SEL !'##cross-references EMBL:X60066; NID:g62268; PIDN:CAA42670.1; !1PID:g62269 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily reovirus sigma 3 protein KEYWORDS capsid protein; coat protein SUMMARY #length 365 #molecular-weight 41226 #checksum 4590 SEQUENCE /// ENTRY P3XRD3 #type complete TITLE major core protein lambda 1 - reovirus type 3 (strain Dearing) ORGANISM #formal_name reovirus type 3 DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 17-Mar-2000 ACCESSIONS A31286 REFERENCE A31286 !$#authors Bartlett, J.A.; Joklik, W.K. !$#journal Virology (1988) 167:31-37 !$#title The sequence of the reovirus serotype 3 L3 genome segment !1which encodes the major core protein lambda-1. !$#cross-references MUID:89045662; PMID:3267236 !$#accession A31286 !'##molecule_type genomic RNA !'##residues 1-1233 ##label BAR !'##cross-references GB:M23747; NID:g333717; PIDN:AAA47271.1; !1PID:g333718 GENETICS !$#map_position segment L3 CLASSIFICATION #superfamily reovirus major core protein lambda 1 KEYWORDS core protein; zinc finger FEATURE !$8-14 #region nucleotide binding #status predicted\ !$183-206 #region zinc finger CCHH motif SUMMARY #length 1233 #molecular-weight 137353 #checksum 6055 SEQUENCE /// ENTRY WMXRGB #type complete TITLE probable core protein - human rotavirus B ORGANISM #formal_name human rotavirus B #note host Homo sapiens (man) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS A33093; S06927 REFERENCE S06927 !$#authors Sato, S.; Yolken, R.H.; Eiden, J.J. !$#journal Nucleic Acids Res. (1989) 17:10113 !$#title The complete nucleic acid sequence of gene segment 3 of the !1IDIR strain of group B rotavirus. !$#cross-references MUID:90098788; PMID:2557579 !$#accession A33093 !'##status translation not shown !'##molecule_type genomic RNA !'##residues 1-751 ##label SAT !'##cross-references EMBL:X16949; NID:g61931; PIDN:CAA34823.1; !1PID:g61932 GENETICS !$#map_position segment 3 CLASSIFICATION #superfamily rotavirus core protein KEYWORDS core protein SUMMARY #length 751 #molecular-weight 85557 #checksum 8864 SEQUENCE /// ENTRY M2XR1L #type complete TITLE structural protein u1 (version 1) - reovirus type 1 (strain Lang) CONTAINS structural protein u1C ORGANISM #formal_name reovirus type 1 #note host Homo sapiens (man) DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jul-1999 ACCESSIONS A28612 REFERENCE A94375 !$#authors Tarlow, O.; McCorquodale, J.G.; McCrae, M.A. !$#journal Virology (1988) 164:141-146 !$#title Molecular cloning and sequencing of the gene (M2) encoding !1the major virion structural protein (mu1-mu1C) of serotypes !11 and 3 of mammalian reovirus. !$#cross-references MUID:88206057; PMID:3363862 !$#accession A28612 !'##molecule_type genomic RNA !'##residues 1-708 ##label TAR !'##cross-references GB:M19407; NID:g333638; PIDN:AAA47237.1; !1PID:g333639 GENETICS !$#map_position segment M2 CLASSIFICATION #superfamily reovirus structural protein u1 KEYWORDS glycoprotein; structural protein FEATURE !$43-708 #product structural protein u1C #status predicted !8#label M1C\ !$12,81,110,458,482, !$528,659 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 708 #molecular-weight 76307 #checksum 5319 SEQUENCE /// ENTRY M2XR2L #type complete TITLE structural protein u1 (version 2) - reovirus type 1 (strain Lang) CONTAINS structural protein u1C ORGANISM #formal_name reovirus type 1 #note host Homo sapiens (man) DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jul-1999 ACCESSIONS A28607 REFERENCE A94374 !$#authors Wiener, J.R.; Joklik, W.K. !$#journal Virology (1988) 163:603-613 !$#title Evolution of reovirus genes: a comparison of serotype 1, 2, !1and 3 M2 genome segments, which encode the major structural !1capsid protein mu1C. !$#cross-references MUID:88179565; PMID:3354208 !$#accession A28607 !'##molecule_type genomic RNA !'##residues 1-708 ##label WIE !'##cross-references GB:M19345; NID:g333636; PIDN:AAA47236.1; !1PID:g333637 COMMENT The RNA sequence was obtained from Genbank, release 57.0. GENETICS !$#map_position segment M2 CLASSIFICATION #superfamily reovirus structural protein u1 KEYWORDS glycoprotein; structural protein FEATURE !$43-708 #product structural protein u1C #status predicted !8#label M1C\ !$3,12,81,110,458, !$482,528,659 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 708 #molecular-weight 76276 #checksum 5671 SEQUENCE /// ENTRY M2XR3D #type complete TITLE structural protein u1 (version 1) - reovirus type 3 (strain Dearing) CONTAINS structural protein u1C ORGANISM #formal_name reovirus type 3 #note host Homo sapiens (man) DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jul-1999 ACCESSIONS B28612 REFERENCE A94375 !$#authors Tarlow, O.; McCorquodale, J.G.; McCrae, M.A. !$#journal Virology (1988) 164:141-146 !$#title Molecular cloning and sequencing of the gene (M2) encoding !1the major virion structural protein (mu1-mu1C) of serotypes !11 and 3 of mammalian reovirus. !$#cross-references MUID:88206057; PMID:3363862 !$#accession B28612 !'##molecule_type genomic RNA !'##residues 1-709 ##label TAR !'##cross-references GB:M19408; NID:g333684; PIDN:AAA47258.1; !1PID:g333685 GENETICS !$#map_position segment M2 CLASSIFICATION #superfamily reovirus structural protein u1 KEYWORDS glycoprotein; structural protein FEATURE !$43-709 #product structural protein u1C #status predicted !8#label M1C\ !$3,12,81,110,459, !$483,529,660 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 709 #molecular-weight 76485 #checksum 9318 SEQUENCE /// ENTRY M2XR4D #type complete TITLE structural protein u1 (version 2) - reovirus type 3 (strain Dearing) CONTAINS structural protein u1C ORGANISM #formal_name reovirus type 3 #note host Homo sapiens (man) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS A28606 REFERENCE A28606 !$#authors Jayasuriya, A.K.; Nibert, M.L.; Fields, B.N. !$#journal Virology (1988) 163:591-602 !$#title Complete nucleotide sequence of the M2 gene segment of !1reovirus type 3 Dearing and analysis of its protein product !1mu-1. !$#cross-references MUID:88179564; PMID:3354207 !$#accession A28606 !'##molecule_type genomic RNA !'##residues 1-708 ##label JAY !'##cross-references GB:M20161; NID:g703264; PIDN:AAA63507.1; !1PID:g703265 !'##note the authors translated the codon ACG for residue 227 as Ser GENETICS !$#map_position segment M2 CLASSIFICATION #superfamily reovirus structural protein u1 KEYWORDS glycoprotein; structural protein FEATURE !$43-708 #product structural protein u1C #status predicted !8#label M1C\ !$3,12,81,110,458, !$482,528,659 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 708 #molecular-weight 76284 #checksum 6731 SEQUENCE /// ENTRY M2XR2J #type complete TITLE structural protein u1 - reovirus type 2 (strain D5/Jones) CONTAINS structural protein u1C ORGANISM #formal_name reovirus type 2 #note host Homo sapiens (man) DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jul-1999 ACCESSIONS B28607 REFERENCE A94374 !$#authors Wiener, J.R.; Joklik, W.K. !$#journal Virology (1988) 163:603-613 !$#title Evolution of reovirus genes: a comparison of serotype 1, 2, !1and 3 M2 genome segments, which encode the major structural !1capsid protein mu1C. !$#cross-references MUID:88179565; PMID:3354208 !$#accession B28607 !'##molecule_type genomic RNA !'##residues 1-708 ##label WIE !'##cross-references GB:M19355; NID:g333659; PIDN:AAA47246.1; !1PID:g333660 COMMENT The RNA sequence was obtained from Genbank, release 57.0. GENETICS !$#map_position segment M2 CLASSIFICATION #superfamily reovirus structural protein u1 KEYWORDS glycoprotein; structural protein FEATURE !$43-708 #product structural protein u1C #status predicted !8#label M1C\ !$3,12,81,110,458, !$482,528 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 708 #molecular-weight 76145 #checksum 5897 SEQUENCE /// ENTRY M4XR3D #type complete TITLE structural protein u2 - reovirus type 3 (strain Dearing) ORGANISM #formal_name reovirus type 3 DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jul-1999 ACCESSIONS A30179 REFERENCE A30179 !$#authors Wiener, J.R.; Bartlett, J.A.; Joklik, W.K. !$#journal Virology (1989) 169:293-304 !$#title The sequences of reovirus serotype 3 genome segments M1 and !1M3 encoding the minor protein mu-2 and the major !1nonstructural protein mu-NS, respectively. !$#cross-references MUID:89204900; PMID:2523177 !$#accession A30179 !'##molecule_type genomic RNA !'##residues 1-736 ##label WIE !'##cross-references GB:M27261; NID:g333679; PIDN:AAA47256.1; !1PID:g333680 CLASSIFICATION #superfamily reovirus structural protein u2 KEYWORDS structural protein SUMMARY #length 736 #molecular-weight 83276 #checksum 1331 SEQUENCE /// ENTRY MWXRWV #type complete TITLE structural protein P8 - wound tumor virus ORGANISM #formal_name wound tumor virus, WTV DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS A30231 REFERENCE A30231 !$#authors Xu, Z.; Anzola, J.V.; Nalin, C.M.; Nuss, D.L. !$#journal Virology (1989) 170:511-522 !$#title The 3'-terminal sequence of a wound tumor virus transcript !1can influence conformational and functional properties !1associated with the 5'-terminus. !$#cross-references MUID:89268473; PMID:2543127 !$#accession A30231 !'##molecule_type genomic RNA !'##residues 1-427 ##label XUZ !'##cross-references GB:J04344; NID:g336177; PIDN:AAA48503.1; !1PID:g336178 GENETICS !$#map_position segment S8 CLASSIFICATION #superfamily wound tumor virus structural protein P8 KEYWORDS glycoprotein; structural protein FEATURE !$45,63,121,282,363 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 427 #molecular-weight 48064 #checksum 3809 SEQUENCE /// ENTRY MWXRRD #type complete TITLE structural protein P8 - rice dwarf virus (strain O) ALTERNATE_NAMES outer capsid protein ORGANISM #formal_name rice dwarf virus DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jun-2000 ACCESSIONS JQ0105 REFERENCE JQ0105 !$#authors Omura, T.; Ishikawa, K.; Hirano, H.; Ugaki, M.; Minobe, Y.; !1Tsuchizaki, T.; Kato, H. !$#journal J. Gen. Virol. (1989) 70:2759-2764 !$#title The outer capsid protein of rice dwarf virus is encoded by !1genome segment S8. !$#cross-references MUID:90010981; PMID:2794978 !$#accession JQ0105 !'##molecule_type mRNA !'##residues 1-420 ##label OMU !'##cross-references GB:D00536; NID:g222492; PIDN:BAA00424.1; !1PID:g222493 GENETICS !$#map_position segment S8 CLASSIFICATION #superfamily wound tumor virus structural protein P8 KEYWORDS capsid protein; structural protein SUMMARY #length 420 #molecular-weight 46424 #checksum 9011 SEQUENCE /// ENTRY MWXRRG #type complete TITLE structural protein P8 - rice gall dwarf virus ALTERNATE_NAMES outer capsid protein ORGANISM #formal_name rice gall dwarf virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jun-2000 ACCESSIONS JQ1308; PQ0244 REFERENCE JQ1308 !$#authors Noda, H.; Ishikawa, K.; Hibino, H.; Kato, H.; Omura, T. !$#journal J. Gen. Virol. (1991) 72:2837-2847 !$#title Nucleotide sequences of genome segments S8, encoding a !1capsid protein, and S10, encoding a 36K protein, of rice !1gall dwarf virus. !$#cross-references MUID:92044463; PMID:1940872 !$#accession JQ1308 !'##molecule_type genomic RNA !'##residues 1-426 ##label NOD !'##cross-references GB:D13410; NID:g222506; PIDN:BAA02676.1; !1PID:g222507 !$#accession PQ0244 !'##molecule_type protein !'##residues 85-95;143-148;160-166;363-375;404-407 ##label NO2 GENETICS !$#map_position segment S8 CLASSIFICATION #superfamily wound tumor virus structural protein P8 KEYWORDS capsid protein; structural protein SUMMARY #length 426 #molecular-weight 47422 #checksum 6112 SEQUENCE /// ENTRY A45341 #type complete TITLE major structural core protein - rice dwarf virus ORGANISM #formal_name rice dwarf virus #note host Oryza sativa (rice) DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jun-2000 ACCESSIONS A45341; S12826; S12621 REFERENCE A45341 !$#authors Suzuki, N.; Watanabe, Y.; Kusano, T.; Kitagawa, Y. !$#journal Virology (1990) 179:455-459 !$#title Sequence analysis of the rice dwarf phytoreovirus segment S3 !1transcript encoding for the major structural core protein of !1114 kDa. !$#cross-references MUID:91021050; PMID:2219733 !$#accession A45341 !'##molecule_type mRNA !'##residues 1-1019 ##label SUZ !'##cross-references GB:X54620; NID:g61467; PIDN:CAA38440.1; PID:g61468 REFERENCE S12826 !$#authors Yamada, N.; Uyeda, I.; Kudo, H.; Shikata, E. !$#journal Nucleic Acids Res. (1990) 18:6419 !$#title Nucleotide sequence of rice dwarf virus genome segment 3. !$#cross-references MUID:91057125; PMID:2243784 !$#accession S12826 !'##molecule_type genomic RNA !'##residues 1-303,'S',305-1019 ##label YAM !'##cross-references EMBL:D00607; NID:g222500; PIDN:BAA00482.1; !1PID:g222501 REFERENCE S12621 !$#authors Kano, H.; Koizumi, M.; Noda, H.; Mizuno, H.; Tsukihara, T.; !1Ishikawa, K.; Hibino, H.; Omura, T. !$#journal Nucleic Acids Res. (1990) 18:6700 !$#title Nucleotide sequence of rice dwarf virus (RDV) genome segment !1S3 coding for 114 K major core protein. !$#cross-references MUID:91067474; PMID:2251136 !$#accession S12621 !'##molecule_type genomic RNA !'##residues 1-18,'Y',20-182,'HG',185-246,'Y',248-422,'N',424-658,'Y', !1660-809,'N',811-909,'N',911-1005,'M',1007-1019 ##label KAN !'##cross-references GB:D00693 GENETICS !$#map_position segment 3 CLASSIFICATION #superfamily rice dwarf virus major structural core protein KEYWORDS core protein SUMMARY #length 1019 #molecular-weight 114290 #checksum 2402 SEQUENCE /// ENTRY QMXRWT #type complete TITLE capsomere protein P9 - wound tumor virus ORGANISM #formal_name wound tumor virus, WTV DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS S04139 REFERENCE S04139 !$#authors Dall, D.J.; Anzola, J.V.; Xu, Z.; Nuss, D.L. !$#journal Nucleic Acids Res. (1989) 17:3599 !$#title Complete nucleotide sequence of wound tumor virus genomic !1segment S11. !$#cross-references MUID:89263810; PMID:2726499 !$#accession S04139 !'##molecule_type genomic RNA !'##residues 1-313 ##label DAL !'##cross-references GB:X14219; NID:g62264; PIDN:CAA32439.1; PID:g62265 GENETICS !$#map_position segment 11 CLASSIFICATION #superfamily phytoreovirus nonstructural protein Pns9 SUMMARY #length 313 #molecular-weight 35606 #checksum 6945 SEQUENCE /// ENTRY QMXRWN #type complete TITLE nonstructural protein Pns11 - wound tumor virus (strain NJ) ALTERNATE_NAMES segment 11 protein ORGANISM #formal_name wound tumor virus, WTV DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS C41705 REFERENCE A41705 !$#authors Hillman, B.I.; Anzola, J.V.; Halpern, B.T.; Cavileer, T.D.; !1Nuss, D.L. !$#journal Virology (1991) 185:896-900 !$#title First field isolation of wound tumor virus from a plant !1host: minimal sequence divergence from the type strain !1isolated from an insect vector. !$#cross-references MUID:92074261; PMID:1962460 !$#accession C41705 !'##molecule_type genomic RNA !'##residues 1-313 ##label HIL !'##cross-references GB:M77020; NID:g336172; PIDN:AAA48500.1; !1PID:g336173 GENETICS !$#map_position segment 11 CLASSIFICATION #superfamily phytoreovirus nonstructural protein Pns9 KEYWORDS nonstructural protein SUMMARY #length 313 #molecular-weight 35551 #checksum 6712 SEQUENCE /// ENTRY MNXRRW #type complete TITLE nonstructural protein Pns9 - rice dwarf virus ORGANISM #formal_name rice dwarf virus #note host Oryza sativa (rice) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jun-2000 ACCESSIONS JA0113 REFERENCE JA0113 !$#authors Uyeda, I.; Kudo, H.; Takahashi, T.; Sano, T.; Ohshima, K.; !1Matsumura, T.; Shikata, E. !$#journal J. Gen. Virol. (1989) 70:1297-1300 !$#title Nucleotide sequence of rice dwarf virus genome segment 9. !$#cross-references MUID:89279307; PMID:2732716 !$#accession JA0113 !'##molecule_type genomic RNA !'##residues 1-351 ##label UYE !'##cross-references GB:D00465; NID:g222504; PIDN:BAA00360.1; !1PID:g222505 !'##note the translation of residues 293-312 is not shown COMMENT The genome consists of 12 double-stranded RNA segments. !1Segment 9 has a single open reading frame. GENETICS !$#map_position segment 9 CLASSIFICATION #superfamily phytoreovirus nonstructural protein Pns9 KEYWORDS nonstructural protein SUMMARY #length 351 #molecular-weight 38729 #checksum 5696 SEQUENCE /// ENTRY MNXRRG #type complete TITLE nonstructural protein Pns10 - rice gall dwarf virus ORGANISM #formal_name rice gall dwarf virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jun-2000 ACCESSIONS JQ1309 REFERENCE JQ1308 !$#authors Noda, H.; Ishikawa, K.; Hibino, H.; Kato, H.; Omura, T. !$#journal J. Gen. Virol. (1991) 72:2837-2847 !$#title Nucleotide sequences of genome segments S8, encoding a !1capsid protein, and S10, encoding a 36K protein, of rice !1gall dwarf virus. !$#cross-references MUID:92044463; PMID:1940872 !$#accession JQ1309 !'##molecule_type genomic RNA !'##residues 1-320 ##label NOD !'##cross-references GB:D13411; NID:g222508; PIDN:BAA02677.1; !1PID:g222509 GENETICS !$#map_position segment S10 CLASSIFICATION #superfamily phytoreovirus nonstructural protein Pns9 KEYWORDS nonstructural protein SUMMARY #length 320 #molecular-weight 36096 #checksum 6953 SEQUENCE /// ENTRY MWXRR5 #type complete TITLE RNA 5 protein - rice dwarf virus ORGANISM #formal_name rice dwarf virus DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 21-Jul-2000 ACCESSIONS S06751; B45342 REFERENCE S06751 !$#authors Suzuki, N.; Watanabe, Y.; Kusano, T.; Kitagawa, Y. !$#journal Nucleic Acids Res. (1989) 17:8858 !$#title Nucleotide sequence of rice dwarf virus segment 5. !$#cross-references MUID:90067853; PMID:2587221 !$#accession S06751 !'##molecule_type genomic RNA !'##residues 1-801 ##label SUZ !'##cross-references EMBL:X16017; NID:g222478; PIDN:BAA14081.1; !1PID:g222479 GENETICS !$#map_position segment 5 CLASSIFICATION #superfamily rice dwarf virus RNA 5 protein SUMMARY #length 801 #molecular-weight 90533 #checksum 4330 SEQUENCE /// ENTRY MWXRRT #type complete TITLE RNA 10 protein - rice black streaked dwarf virus ORGANISM #formal_name rice black streaked dwarf virus DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jun-2000 ACCESSIONS JQ0409 REFERENCE JQ0409 !$#authors Uyeda, I.; Azuhata, F.; Shikata, E. !$#journal Proc. Jpn. Acad. B Phys. Biol. Sci. (1990) 66:37-40 !$#title Nucleotide sequence of rice black-streaked dwarf virus !1genome segment 10. !$#accession JQ0409 !'##molecule_type mRNA !'##residues 1-558 ##label UYE !'##cross-references EMBL:D00606; NID:g222470; PIDN:BAA00481.1; !1PID:g222471 GENETICS !$#map_position segment S10 CLASSIFICATION #superfamily rice black streaked dwarf virus RNA 10 protein SUMMARY #length 558 #molecular-weight 63266 #checksum 2141 SEQUENCE /// ENTRY QQXRS3 #type complete TITLE nonstructural protein sigma 1s - reovirus type 3 ORGANISM #formal_name reovirus type 3 #note host Homo sapiens (man) DATE 27-Nov-1985 #sequence_revision 27-Nov-1985 #text_change 16-Jul-1999 ACCESSIONS A04128; B23880 REFERENCE A93360 !$#authors Bassel-Duby, R.; Jayasuriya, A.; Chatterjee, D.; Sonenberg, !1N.; Maizel Jr., J.V.; Fields, B.N. !$#journal Nature (1985) 315:421-423 !$#title Sequence of reovirus haemagglutinin predicts a coiled-coil !1structure. !$#cross-references MUID:85213868; PMID:4000269 !$#accession A04128 !'##molecule_type genomic RNA !'##residues 1-120 ##label BAS REFERENCE A93545 !$#authors Nagata, L.; Masri, S.A.; Mah, D.C.W.; Lee, P.W.K. !$#journal Nucleic Acids Res. (1984) 12:8699-8710 !$#title Molecular cloning and sequencing of the reovirus (serotype !13) S1 gene which encodes the viral cell attachment protein !1sigma 1. !$#cross-references MUID:85062842; PMID:6095208 !$#accession B23880 !'##molecule_type genomic RNA !'##residues 1-2,'H',4-98,'T',100-120 ##label NAG !'##cross-references GB:X01161; NID:g61780; PIDN:CAA25606.1; PID:g61783 GENETICS !$#gene S1; sigma 1 !$#note this coding region is an internal ORF of the sigma 1 protein !1gene CLASSIFICATION #superfamily reovirus nonstructural protein sigma 1s KEYWORDS nonstructural protein SUMMARY #length 120 #molecular-weight 14017 #checksum 1663 SEQUENCE /// ENTRY VPXRWA #type complete TITLE outer capsid protein VP8 - human rotavirus A (serotype 1 strain WA) ORGANISM #formal_name human rotavirus A DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 30-Sep-1993 ACCESSIONS D25904 REFERENCE A94126 !$#authors Gorziglia, M.; Hoshino, Y.; Buckler-White, A.; Blumentals, !1I.; Glass, R.; Flores, J.; Kapikian, A.Z.; Chanock, R.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:7039-7043 !$#title Conservation of amino acid sequence of VP8 and cleavage !1region of 84-kDa outer capsid protein among rotaviruses !1recovered from asymptomatic neonatal infection. !$#cross-references MUID:86313706; PMID:3018754 !$#accession D25904 !'##molecule_type genomic RNA !'##residues 1-280 ##label GOR COMMENT VP8 is one of two trypsin cleavage products of VP3; the !1other product is VP5. GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily rotavirus outer layer protein VP3 KEYWORDS glycoprotein; outer capsid protein FEATURE !$32,36,56,97,129, !$132,195 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 280 #molecular-weight 32153 #checksum 8648 SEQUENCE /// ENTRY VPXRRP #type complete TITLE outer capsid protein VP8 - human rotavirus A (serotype 3 strain P) ORGANISM #formal_name human rotavirus A DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 30-Sep-1993 ACCESSIONS B25904 REFERENCE A94126 !$#authors Gorziglia, M.; Hoshino, Y.; Buckler-White, A.; Blumentals, !1I.; Glass, R.; Flores, J.; Kapikian, A.Z.; Chanock, R.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:7039-7043 !$#title Conservation of amino acid sequence of VP8 and cleavage !1region of 84-kDa outer capsid protein among rotaviruses !1recovered from asymptomatic neonatal infection. !$#cross-references MUID:86313706; PMID:3018754 !$#accession B25904 !'##molecule_type genomic RNA !'##residues 1-279 ##label GOR COMMENT VP8 is one of two trypsin cleavage products of VP3; the !1other product is VP5. GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily rotavirus outer layer protein VP3 KEYWORDS glycoprotein; outer capsid protein FEATURE !$32,56,97,129,132, !$194 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 279 #molecular-weight 31896 #checksum 4915 SEQUENCE /// ENTRY VPXRDS #type complete TITLE outer capsid protein VP8 - human rotavirus A (serotype 2 strain DS1) ORGANISM #formal_name human rotavirus A DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 30-Sep-1993 ACCESSIONS C25904 REFERENCE A94126 !$#authors Gorziglia, M.; Hoshino, Y.; Buckler-White, A.; Blumentals, !1I.; Glass, R.; Flores, J.; Kapikian, A.Z.; Chanock, R.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:7039-7043 !$#title Conservation of amino acid sequence of VP8 and cleavage !1region of 84-kDa outer capsid protein among rotaviruses !1recovered from asymptomatic neonatal infection. !$#cross-references MUID:86313706; PMID:3018754 !$#accession C25904 !'##molecule_type genomic RNA !'##residues 1-280 ##label GOR COMMENT VP8 is one of two trypsin cleavage products of VP3; the !1other product is VP5. GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily rotavirus outer layer protein VP3 KEYWORDS glycoprotein; outer capsid protein FEATURE !$56,132,150,195 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 280 #molecular-weight 32010 #checksum 1604 SEQUENCE /// ENTRY JQ1638 #type complete TITLE outer layer protein VP4 - human rotavirus A (serotype G3, strain AU-1) ALTERNATE_NAMES hemagglutinin; outer capsid protein VP4 CONTAINS outer layer protein VP5; outer layer protein VP8 ORGANISM #formal_name human rotavirus A DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jun-2000 ACCESSIONS JQ1638 REFERENCE JQ1638 !$#authors Isegawa, Y.; Nakagomi, O.; Nakagomi, T.; Ueda, S. !$#journal J. Gen. Virol. (1992) 73:1939-1946 !$#title A VP4 sequence highly conserved in human rotavirus strain !1AU-1 and feline rotavirus strain FRV-1. !$#cross-references MUID:92356070; PMID:1322955 !$#accession JQ1638 !'##molecule_type genomic RNA !'##residues 1-775 ##label ISE !'##cross-references GB:D10970; NID:g222542; PIDN:BAA01747.1; !1PID:g222543 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily rotavirus outer layer protein VP3 KEYWORDS glycoprotein; hemagglutinin; outer capsid protein FEATURE !$1-241 #product outer layer protein VP8 #status predicted !8#label VP8\ !$242-247 #region cleavage processing #status predicted\ !$248-775 #product outer layer protein VP5 #status predicted !8#label VP5\ !$17,32,97,132,183, !$198,237,567,613 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 775 #molecular-weight 87092 #checksum 6461 SEQUENCE /// ENTRY JQ1639 #type complete TITLE outer layer protein VP4 - feline rotavirus A (serotype G3, strain FRV-1) ALTERNATE_NAMES hemagglutinin; outer capsid protein VP4 CONTAINS outer layer protein VP5; outer layer protein VP8 ORGANISM #formal_name feline rotavirus A DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jun-2000 ACCESSIONS JQ1639 REFERENCE JQ1638 !$#authors Isegawa, Y.; Nakagomi, O.; Nakagomi, T.; Ueda, S. !$#journal J. Gen. Virol. (1992) 73:1939-1946 !$#title A VP4 sequence highly conserved in human rotavirus strain !1AU-1 and feline rotavirus strain FRV-1. !$#cross-references MUID:92356070; PMID:1322955 !$#accession JQ1639 !'##molecule_type genomic RNA !'##residues 1-775 ##label ISE !'##cross-references DDBJ:D10971; NID:g222536; PIDN:BAA01748.1; !1PID:g222537 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily rotavirus outer layer protein VP3 KEYWORDS glycoprotein; hemagglutinin; outer capsid protein FEATURE !$1-241 #product outer layer protein VP8 #status predicted !8#label VP8\ !$242-247 #region cleavage processing #status predicted\ !$248-775 #product outer layer protein VP5 #status predicted !8#label VP5\ !$17,32,97,132,183, !$198,567,613 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 775 #molecular-weight 87138 #checksum 7222 SEQUENCE /// ENTRY VPXRRH #type complete TITLE outer layer protein VP3 - rhesus rotavirus ALTERNATE_NAMES glycoprotein VP3; hemagglutinin; outer capsid protein VP3 CONTAINS outer capsid protein VP5; outer capsid protein VP8 ORGANISM #formal_name rhesus rotavirus DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jul-1999 ACCESSIONS A31078 REFERENCE A31078 !$#authors Mackow, E.R.; Shaw, R.D.; Matsui, S.M.; Vo, P.T.; Dang, !1M.N.; Greenberg, H.B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1988) 85:645-649 !$#title The rhesus rotavirus gene encoding protein VP3: location of !1amino acids involved in homologous and heterologous !1rotavirus neutralization and identification of a putative !1fusion region. !$#cross-references MUID:88124898; PMID:2829198 !$#accession A31078 !'##molecule_type genomic RNA !'##residues 1-776 ##label MAC !'##cross-references GB:M18736; GB:J03567; NID:g333868; PIDN:AAA47345.1; !1PID:g333869 COMMENT This protein can be cleaved with trypsin to form outer !1capsid protein VP8 and outer capsid protein VP5. GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily rotavirus outer layer protein VP3 KEYWORDS glycoprotein; hemagglutinin; outer capsid protein FEATURE !$1-241 #product outer capsid protein VP8 #status predicted !8#label VP8\ !$242-247 #region cleavage processing #status predicted\ !$248-776 #product outer capsid protein VP5 #status predicted !8#label VP5\ !$32,56,97,111,149, !$183,198 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 776 #molecular-weight 86602 #checksum 673 SEQUENCE /// ENTRY VPXR4S #type fragment TITLE outer layer protein VP3 - simian rotavirus SA11 (fragment) ORGANISM #formal_name simian rotavirus SA11 #note host (monkey) DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 29-Oct-1999 ACCESSIONS A04129 REFERENCE A04129 !$#authors Lopez, S.; Arias, C.F.; Bell, J.R.; Strauss, J.H.; Espejo, !1R.T. !$#journal Virology (1985) 144:11-19 !$#title Primary structure of the cleavage site associated with !1trypsin enhancement of rotavirus SA11 infectivity. !$#cross-references MUID:86045932; PMID:2998038 !$#accession A04129 !'##status translated from GB/EMBL/DDBJ !'##molecule_type genomic RNA !'##residues 1-747 ##label LOP !'##cross-references GB:M11158; NID:g61868 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily rotavirus outer layer protein VP3 SUMMARY #length 747 #checksum 2482 SEQUENCE /// ENTRY VPXRT1 #type complete TITLE outer layer protein VP3 - simian rotavirus SA11 (strain SA11-FEM) ALTERNATE_NAMES glycoprotein VP3; hemagglutinin; outer capsid protein VP3 CONTAINS outer layer protein VP5; outer layer protein VP8 ORGANISM #formal_name simian rotavirus SA11 #note host (monkey) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 12-Apr-1996 ACCESSIONS B31159 REFERENCE A94694 !$#authors Nishikawa, K.; Taniguchi, K.; Torres, A.; Hoshino, Y.; !1Green, K.; Kapikian, A.Z.; Chanock, R.M.; Gorziglia, M. !$#journal J. Virol. (1988) 62:4022-4026 !$#title Comparative analysis of the VP3 gene of divergent strains of !1the rotaviruses simian SA11 and bovine Nebraska calf !1diarrhea virus. !$#cross-references MUID:89012172; PMID:2845121 !$#accession B31159 !'##molecule_type genomic RNA !'##residues 1-776 ##label NIS GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily rotavirus outer layer protein VP3 KEYWORDS glycoprotein; hemagglutinin; outer capsid protein FEATURE !$1-241 #product outer layer protein VP8 #status predicted !8#label VP8\ !$248-776 #product outer layer protein VP5 #status predicted !8#label VP5\ !$32,56,97,132,151, !$198,456,507,602 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 776 #molecular-weight 86692 #checksum 960 SEQUENCE /// ENTRY VPXRT2 #type complete TITLE outer layer protein VP3 - Nebraska calf diarrhea virus (strain NCDV-Lincoln) ALTERNATE_NAMES glycoprotein VP3; hemagglutinin; outer capsid protein VP3 CONTAINS outer layer protein VP5; outer layer protein VP8 ORGANISM #formal_name Nebraska calf diarrhea virus DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 12-Apr-1996 ACCESSIONS C31159 REFERENCE A94694 !$#authors Nishikawa, K.; Taniguchi, K.; Torres, A.; Hoshino, Y.; !1Green, K.; Kapikian, A.Z.; Chanock, R.M.; Gorziglia, M. !$#journal J. Virol. (1988) 62:4022-4026 !$#title Comparative analysis of the VP3 gene of divergent strains of !1the rotaviruses simian SA11 and bovine Nebraska calf !1diarrhea virus. !$#cross-references MUID:89012172; PMID:2845121 !$#accession C31159 !'##molecule_type genomic RNA !'##residues 1-775 ##label NIS GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily rotavirus outer layer protein VP3 KEYWORDS glycoprotein; hemagglutinin; outer capsid protein FEATURE !$1-241 #product outer layer protein VP8 #status predicted !8#label VP8\ !$248-775 #product outer layer protein VP5 #status predicted !8#label VP5\ !$56,97,132,151,183, !$198,456,507,596,602 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 775 #molecular-weight 86548 #checksum 9392 SEQUENCE /// ENTRY VPXRB3 #type complete TITLE outer layer protein VP3 - bovine rotavirus A (strain C486) ALTERNATE_NAMES hemagglutinin ORGANISM #formal_name bovine rotavirus A DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 16-Jul-1999 ACCESSIONS A29529 REFERENCE A29529 !$#authors Potter, A.A.; Cox, G.; Parker, M.; Babiuk, L.A. !$#journal Nucleic Acids Res. (1987) 15:4361 !$#title The complete nucleotide sequence of bovine rotavirus C486 !1gene 4 cDNA. !$#cross-references MUID:87231020; PMID:3035492 !$#accession A29529 !'##molecule_type genomic RNA !'##residues 1-776 ##label POT !'##cross-references GB:Y00127; NID:g61854; PIDN:CAA68325.1; PID:g61855 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily rotavirus outer layer protein VP3 KEYWORDS glycoprotein; hemagglutinin FEATURE !$32,56,97,132,151, !$183,198,456,507, !$596,602 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 776 #molecular-weight 86768 #checksum 1702 SEQUENCE /// ENTRY JQ2022 #type complete TITLE outer layer protein VP4 - bovine rotavirus A (serotype 5) ALTERNATE_NAMES hemagglutinin; outer capsid protein VP4 CONTAINS outer layer protein VP5; outer layer protein VP8 ORGANISM #formal_name bovine rotavirus A DATE 24-Feb-1994 #sequence_revision 24-Feb-1994 #text_change 02-Jun-2000 ACCESSIONS JQ2022 REFERENCE JQ2022 !$#authors Taniguchi, K.; Urasawa, T.; Urasawa, S. !$#journal J. Gen. Virol. (1993) 74:1215-1221 !$#title Independent segregation of the VP4 and the VP7 genes in !1bovine rotaviruses as confirmed by VP4 sequence analysis of !1G8 and G10 bovine rotavirus strains. !$#cross-references MUID:93286580; PMID:8389807 !$#accession JQ2022 !'##molecule_type genomic RNA !'##residues 1-776 ##label TAN !'##cross-references GB:D13395; NID:g393327 !'##note this translation is not annotated in GenBank entry ROBA5VP4, !1release 113.0 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily rotavirus outer layer protein VP3 KEYWORDS glycoprotein; hemagglutinin; outer capsid protein FEATURE !$1-241 #product outer layer protein VP8 #status predicted !8#label VP8\ !$242-247 #region cleavage processing #status predicted\ !$248-776 #product outer layer protein VP5 #status predicted !8#label VP5\ !$56,97,132,151,198, !$456,507,670 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 776 #molecular-weight 86590 #checksum 8060 SEQUENCE /// ENTRY VPXRSU #type complete TITLE outer layer protein VP3 - porcine rotavirus C (strain OSU) ORGANISM #formal_name porcine rotavirus C DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS A33384 REFERENCE A33384 !$#authors Nishikawa, K.; Gorziglia, M. !$#journal Nucleic Acids Res. (1988) 16:11847 !$#title The nucleotide sequence of the VP3 gene of porcine rotavirus !1OSU. !$#cross-references MUID:89098360; PMID:2850544 !$#accession A33384 !'##molecule_type genomic RNA !'##residues 1-776 ##label NIS !'##cross-references GB:X13190; NID:g61688; PIDN:CAA31581.1; PID:g61689 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily rotavirus outer layer protein VP3 KEYWORDS capsid protein; coat protein SUMMARY #length 776 #molecular-weight 86741 #checksum 8119 SEQUENCE /// ENTRY VPXRYM #type complete TITLE outer layer protein VP3 - porcine rotavirus C (strain YM) ALTERNATE_NAMES hemagglutinin; VP4 protein CONTAINS outer layer protein VP5; outer layer protein VP8 ORGANISM #formal_name porcine rotavirus C DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS A40342 REFERENCE A40342 !$#authors Lopez, S.; Lopez, I.; Romero, P.; Mendez, E.; Soberon, X.; !1Arias, C.F. !$#journal J. Virol. (1991) 65:3738-3745 !$#title Rotavirus YM gene 4: analysis of its deduced amino acid !1sequence and prediction of the secondary structure of the !1VP4 protein. !$#cross-references MUID:91251227; PMID:1645789 !$#accession A40342 !'##molecule_type genomic RNA !'##residues 1-776 ##label LOP !'##cross-references GB:M63231; NID:g333323; PIDN:AAA47100.1; !1PID:g333324 CLASSIFICATION #superfamily rotavirus outer layer protein VP3 KEYWORDS capsid protein; coat protein; glycoprotein; hemagglutinin FEATURE !$1-241 #product outer layer protein VP8 #status predicted !8#label VP8\ !$242-247 #region cleavage processing #status predicted\ !$248-776 #product outer layer protein VP5 #status predicted !8#label VP5\ !$17,32,56,97,116, !$132,151,178,183, !$198,325,670 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 776 #molecular-weight 86772 #checksum 9159 SEQUENCE /// ENTRY VPXRS1 #type complete TITLE outer layer protein VP3 - simian rotavirus SA11 (strain SA11-SEM) ALTERNATE_NAMES glycoprotein VP3; hemagglutinin; outer capsid protein VP3 CONTAINS outer layer protein VP5; outer layer protein VP8 ORGANISM #formal_name simian rotavirus SA11 #note host (monkey) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS A31159 REFERENCE A94694 !$#authors Nishikawa, K.; Taniguchi, K.; Torres, A.; Hoshino, Y.; !1Green, K.; Kapikian, A.Z.; Chanock, R.M.; Gorziglia, M. !$#journal J. Virol. (1988) 62:4022-4026 !$#title Comparative analysis of the VP3 gene of divergent strains of !1the rotaviruses simian SA11 and bovine Nebraska calf !1diarrhea virus. !$#cross-references MUID:89012172; PMID:2845121 !$#accession A31159 !'##molecule_type genomic RNA !'##residues 1-776 ##label NIS !'##cross-references GB:M23188; NID:g515742; PIDN:AAA47355.1; !1PID:g515743 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily rotavirus outer layer protein VP3 KEYWORDS glycoprotein; hemagglutinin; outer capsid protein FEATURE !$1-241 #product outer layer protein VP8 #status predicted !8#label VP8\ !$248-776 #product outer layer protein VP5 #status predicted !8#label VP5\ !$32,56,97,116,132, !$149,198,386 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 776 #molecular-weight 86770 #checksum 4359 SEQUENCE /// ENTRY A45395 #type complete TITLE outer layer protein VP4 - equine rotavirus A (serotype G3, strain H-2) ALTERNATE_NAMES hemagglutinin; outer capsid protein VP4 CONTAINS outer layer protein VP5; outer layer protein VP8 ORGANISM #formal_name equine rotavirus A DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS A45395 REFERENCE A45395 !$#authors Hardy, M.E.; Gorziglia, M.; Woode, G.N. !$#journal Virology (1993) 193:492-497 !$#title The outer capsid protein VP4 of equine rotavirus strain H-2 !1represents a unique VP4 type by amino acid sequence !1analysis. !$#cross-references MUID:93174966; PMID:8382410 !$#accession A45395 !'##molecule_type genomic RNA !'##residues 1-776 ##label HAR !'##cross-references GB:L04638; NID:g294727; PIDN:AAA70383.1; !1PID:g294728 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily rotavirus outer layer protein VP3 KEYWORDS glycoprotein; hemagglutinin; outer capsid protein FEATURE !$1-241 #product outer layer protein VP8 #status predicted !8#label VP8\ !$242-247 #region cleavage processing #status predicted\ !$248-776 #product outer layer protein VP5 #status predicted !8#label VP5\ !$32,56,132,133,151, !$183,578 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 776 #molecular-weight 86690 #checksum 28 SEQUENCE /// ENTRY VPXRBU #type complete TITLE outer layer protein VP3 - bovine rotavirus A (strain UK) ALTERNATE_NAMES glycoprotein VP3; hemagglutinin; outer capsid protein VP3 CONTAINS outer capsid protein VP5; outer capsid protein VP8 ORGANISM #formal_name bovine rotavirus A DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jul-1999 ACCESSIONS A31164 REFERENCE A31164 !$#authors Kantharidis, P.; Dyall-Smith, M.L.; Tregear, G.W.; Holmes, !1I.H. !$#journal Virology (1988) 166:308-315 !$#title Nucleotide sequence of UK bovine rotavirus segment 4: !1possible host restriction of VP3 genes. !$#cross-references MUID:89020797; PMID:2845645 !$#accession A31164 !'##molecule_type mRNA !'##residues 1-776 ##label KAN !'##cross-references GB:M22306; NID:g333819; PIDN:AAA47318.1; !1PID:g333820 COMMENT This protein can be cleaved with trypsin to form outer !1capsid protein VP8 and outer capsid protein VP5. GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily rotavirus outer layer protein VP3 KEYWORDS glycoprotein; hemagglutinin; outer capsid protein FEATURE !$1-240 #product outer capsid protein VP8 #status predicted !8#label VP8\ !$241-247 #region cleavage processing #status predicted\ !$248-776 #product outer capsid protein VP5 #status predicted !8#label VP5\ !$17,56,132,183,507, !$593 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 776 #molecular-weight 86465 #checksum 1658 SEQUENCE /// ENTRY JQ2023 #type complete TITLE outer layer protein VP4 - bovine rotavirus A (serotype 61) ALTERNATE_NAMES hemagglutinin; outer capsid protein VP4 CONTAINS outer layer protein VP5; outer layer protein VP8 ORGANISM #formal_name bovine rotavirus A DATE 24-Feb-1994 #sequence_revision 24-Feb-1994 #text_change 02-Jun-2000 ACCESSIONS JQ2023 REFERENCE JQ2022 !$#authors Taniguchi, K.; Urasawa, T.; Urasawa, S. !$#journal J. Gen. Virol. (1993) 74:1215-1221 !$#title Independent segregation of the VP4 and the VP7 genes in !1bovine rotaviruses as confirmed by VP4 sequence analysis of !1G8 and G10 bovine rotavirus strains. !$#cross-references MUID:93286580; PMID:8389807 !$#accession JQ2023 !'##molecule_type genomic RNA !'##residues 1-776 ##label TAN !'##cross-references GB:D13396; NID:g393325 !'##note this translation is not annotated in GenBank entry ROB61AVP4, !1release 113.0 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily rotavirus outer layer protein VP3 KEYWORDS glycoprotein; hemagglutinin; outer capsid protein FEATURE !$1-241 #product outer layer protein VP8 #status predicted !8#label VP8\ !$242-247 #region cleavage processing #status predicted\ !$248-776 #product outer layer protein VP5 #status predicted !8#label VP5\ !$132,183,507,593 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 776 #molecular-weight 86336 #checksum 648 SEQUENCE /// ENTRY VPXRB6 #type complete TITLE outer layer protein VP3 - bovine rotavirus A (serotype 6 strain B641) ALTERNATE_NAMES hemagglutinin; VP4 protein CONTAINS outer layer protein VP5; outer layer protein VP8 ORGANISM #formal_name bovine rotavirus A DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 01-Mar-1996 ACCESSIONS B40508 REFERENCE A40508 !$#authors Hardy, M.E.; Woode, G.N.; Xu, Z.; Gorziglia, M. !$#journal J. Virol. (1991) 65:5535-5538 !$#title Comparative amino acid sequence analysis of VP4 for VP7 !1serotype 6 bovine rotavirus strains NCDV, B641, and UK. !$#cross-references MUID:91374610; PMID:1654450 !$#accession B40508 !'##molecule_type genomic RNA !'##residues 1-776 ##label HAR !'##cross-references GB:M63267 CLASSIFICATION #superfamily rotavirus outer layer protein VP3 KEYWORDS capsid protein; coat protein; glycoprotein; hemagglutinin FEATURE !$1-241 #product outer layer protein VP8 #status predicted !8#label VP8\ !$242-247 #region cleavage processing #status predicted\ !$248-776 #product outer layer protein VP5 #status predicted !8#label VP5\ !$56,132,183,193,507, !$593 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 776 #molecular-weight 86406 #checksum 329 SEQUENCE /// ENTRY A44052 #type complete TITLE outer layer protein VP4 - bovine rotavirus A (serotype 10, strain B223) ALTERNATE_NAMES hemagglutinin; outer capsid protein VP4; outer layer protein VP3 CONTAINS outer layer protein VP5; outer layer protein VP8 ORGANISM #formal_name bovine rotavirus A DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 01-Mar-1996 ACCESSIONS A44052 REFERENCE A44052 !$#authors Hardy, M.E.; Gorziglia, M.; Woode, G.N. !$#journal Virology (1992) 191:291-300 !$#title Amino acid sequence analysis of bovine rotavirus B223 !1reveals a unique outer capsid protein VP4 and confirms a !1third bovine VP4 type. !$#cross-references MUID:93033121; PMID:1329320 !$#accession A44052 !'##molecule_type genomic RNA !'##residues 1-772 ##label HAR !'##cross-references GB:M92986 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily rotavirus outer layer protein VP3 KEYWORDS glycoprotein; hemagglutinin; outer capsid protein FEATURE !$1-242 #product outer layer protein VP8 #status predicted !8#label VP8\ !$243-248 #region cleavage processing #status predicted\ !$249-772 #product outer layer protein VP5 #status predicted !8#label VP5\ !$32,98,116,123,127, !$173 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 772 #molecular-weight 86577 #checksum 3607 SEQUENCE /// ENTRY JQ2024 #type complete TITLE outer layer protein VP4 - bovine rotavirus A (serotype 44) ALTERNATE_NAMES hemagglutinin; outer capsid protein VP4 CONTAINS outer layer protein VP5; outer layer protein VP8 ORGANISM #formal_name bovine rotavirus A DATE 24-Feb-1994 #sequence_revision 24-Feb-1994 #text_change 02-Jun-2000 ACCESSIONS JQ2024 REFERENCE JQ2022 !$#authors Taniguchi, K.; Urasawa, T.; Urasawa, S. !$#journal J. Gen. Virol. (1993) 74:1215-1221 !$#title Independent segregation of the VP4 and the VP7 genes in !1bovine rotaviruses as confirmed by VP4 sequence analysis of !1G8 and G10 bovine rotavirus strains. !$#cross-references MUID:93286580; PMID:8389807 !$#accession JQ2024 !'##molecule_type genomic RNA !'##residues 1-772 ##label TAN !'##cross-references GB:D13392; NID:g393326 !'##note this translation is not annotated in GenBank entry ROBA44VP4, !1release 113.0 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily rotavirus outer layer protein VP3 KEYWORDS glycoprotein; hemagglutinin; outer capsid protein FEATURE !$1-242 #product outer layer protein VP8 #status predicted !8#label VP8\ !$243-248 #region cleavage processing #status predicted\ !$249-772 #product outer layer protein VP5 #status predicted !8#label VP5\ !$32,98,116,123,127, !$173 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 772 #molecular-weight 86618 #checksum 3280 SEQUENCE /// ENTRY JQ2025 #type complete TITLE outer layer protein VP4 - bovine rotavirus B (serotype 223) ALTERNATE_NAMES hemagglutinin; outer capsid protein VP4 CONTAINS outer layer protein VP5; outer layer protein VP8 ORGANISM #formal_name bovine rotavirus B DATE 24-Feb-1994 #sequence_revision 24-Feb-1994 #text_change 02-Jun-2000 ACCESSIONS JQ2025 REFERENCE JQ2022 !$#authors Taniguchi, K.; Urasawa, T.; Urasawa, S. !$#journal J. Gen. Virol. (1993) 74:1215-1221 !$#title Independent segregation of the VP4 and the VP7 genes in !1bovine rotaviruses as confirmed by VP4 sequence analysis of !1G8 and G10 bovine rotavirus strains. !$#cross-references MUID:93286580; PMID:8389807 !$#accession JQ2025 !'##molecule_type genomic RNA !'##residues 1-772 ##label TAN !'##cross-references GB:D13394; NID:g393328 !'##note this translation is not annotated in GenBank entry ROBB223VP4, !1release 113.0 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily rotavirus outer layer protein VP3 KEYWORDS glycoprotein; hemagglutinin; outer capsid protein FEATURE !$1-242 #product outer layer protein VP8 #status predicted !8#label VP8\ !$243-248 #region cleavage processing #status predicted\ !$249-772 #product outer layer protein VP5 #status predicted !8#label VP5\ !$32,98,116,123,127, !$173 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 772 #molecular-weight 86491 #checksum 2038 SEQUENCE /// ENTRY JQ2026 #type complete TITLE outer layer protein VP4 - bovine rotavirus (strain KK3) ALTERNATE_NAMES hemagglutinin; outer capsid protein VP4 CONTAINS outer layer protein VP5; outer layer protein VP8 ORGANISM #formal_name bovine rotavirus DATE 24-Feb-1994 #sequence_revision 24-Feb-1994 #text_change 02-Jun-2000 ACCESSIONS JQ2026 REFERENCE JQ2022 !$#authors Taniguchi, K.; Urasawa, T.; Urasawa, S. !$#journal J. Gen. Virol. (1993) 74:1215-1221 !$#title Independent segregation of the VP4 and the VP7 genes in !1bovine rotaviruses as confirmed by VP4 sequence analysis of !1G8 and G10 bovine rotavirus strains. !$#cross-references MUID:93286580; PMID:8389807 !$#accession JQ2026 !'##molecule_type genomic RNA !'##residues 1-772 ##label TAN !'##cross-references GB:D13393; NID:g393329 !'##note this translation is not annotated in GenBank entry ROBKK33, !1release 113.0 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily rotavirus outer layer protein VP3 KEYWORDS glycoprotein; hemagglutinin; outer capsid protein FEATURE !$1-242 #product outer layer protein VP8 #status predicted !8#label VP8\ !$243-248 #region cleavage processing #status predicted\ !$249-772 #product outer layer protein VP5 #status predicted !8#label VP5\ !$32,98,116,123,127, !$173 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 772 #molecular-weight 86572 #checksum 2531 SEQUENCE /// ENTRY VPXRHK #type complete TITLE outer layer protein VP3 - human rotavirus A (strain KU) ALTERNATE_NAMES glycoprotein VP3; hemagglutinin; outer capsid protein VP3 ORGANISM #formal_name human rotavirus A DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS A28844 REFERENCE A28844 !$#authors Taniguchi, K.; Maloy, W.L.; Nishikawa, K.; Green, K.Y.; !1Hoshino, Y.; Urasawa, S.; Kapikian, A.Z.; Chanock, R.M.; !1Gorziglia, M. !$#journal J. Virol. (1988) 62:2421-2426 !$#title Identification of cross-reactive and serotype 2-specific !1neutralization epitopes on VP3 of human rotavirus. !$#cross-references MUID:88230603; PMID:2453680 !$#accession A28844 !'##molecule_type mRNA !'##residues 1-775 ##label TAN !'##cross-references GB:M21014; NID:g333852; PIDN:AAA47334.1; !1PID:g333853 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily rotavirus outer layer protein VP3 KEYWORDS glycoprotein; hemagglutinin; outer capsid protein FEATURE !$32,56,97,132,324, !$583,589,592,599 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 775 #molecular-weight 87538 #checksum 4552 SEQUENCE /// ENTRY VPXRW3 #type complete TITLE outer layer protein VP3 - human rotavirus A (serotype 1 strain WA) ALTERNATE_NAMES hemagglutinin CONTAINS outer capsid protein VP5; outer capsid protein VP8 ORGANISM #formal_name human rotavirus A DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 01-Mar-1996 ACCESSIONS A28839 REFERENCE A28839 !$#authors Gorziglia, M.; Green, K.; Nishikawa, K.; Taniguchi, K.; !1Jones, R.; Kapikian, A.Z.; Chanock, R.M. !$#journal J. Virol. (1988) 62:2978-2984 !$#title Sequence of the fourth gene of human rotaviruses recovered !1from asymptomatic or symptomatic infections. !$#cross-references MUID:88275070; PMID:2839714 !$#accession A28839 !'##molecule_type genomic RNA !'##residues 1-775 ##label GOR GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily rotavirus outer layer protein VP3 KEYWORDS capsid protein; coat protein; glycoprotein; hemagglutinin FEATURE !$1-240 #product outer capsid protein VP8 #status predicted !8#label VP8\ !$241-246 #region cleavage processing #status predicted\ !$247-775 #product outer capsid protein VP5 #status predicted !8#label VP5\ !$32,36,56,97,129, !$132,195,324,385, !$577,583,589,592,599 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 775 #molecular-weight 87739 #checksum 5937 SEQUENCE /// ENTRY VPXRW4 #type complete TITLE outer layer protein VP3 - human rotavirus A (serotype 2 strain DS1) ALTERNATE_NAMES hemagglutinin CONTAINS outer capsid protein VP5; outer capsid protein VP8 ORGANISM #formal_name human rotavirus A DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 01-Mar-1996 ACCESSIONS B28839 REFERENCE A28839 !$#authors Gorziglia, M.; Green, K.; Nishikawa, K.; Taniguchi, K.; !1Jones, R.; Kapikian, A.Z.; Chanock, R.M. !$#journal J. Virol. (1988) 62:2978-2984 !$#title Sequence of the fourth gene of human rotaviruses recovered !1from asymptomatic or symptomatic infections. !$#cross-references MUID:88275070; PMID:2839714 !$#accession B28839 !'##molecule_type genomic RNA !'##residues 1-775 ##label GOR GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily rotavirus outer layer protein VP3 KEYWORDS capsid protein; coat protein; glycoprotein; hemagglutinin FEATURE !$1-240 #product outer capsid protein VP8 #status predicted !8#label VP8\ !$241-246 #region cleavage processing #status predicted\ !$247-775 #product outer capsid protein VP5 #status predicted !8#label VP5\ !$56,132,150,195,324, !$583,589,592,599 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 775 #molecular-weight 87592 #checksum 6001 SEQUENCE /// ENTRY VPXRWF #type complete TITLE outer layer protein VP3 - human rotavirus A (serotype 2 strain RV5) ALTERNATE_NAMES hemagglutinin CONTAINS outer capsid protein VP5; outer capsid protein VP8 ORGANISM #formal_name human rotavirus A DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS A43760 REFERENCE A43760 !$#authors Kantharidis, P.; Dyall-Smith, M.L.; Holmes, I.H. !$#journal Arch. Virol. (1987) 93:111-121 !$#title Marked sequence variation between segment 4 genes of human !1RV-5 and simian SA11 rotaviruses. !$#cross-references MUID:87127560; PMID:3028337 !$#accession A43760 !'##molecule_type genomic RNA !'##residues 1-775 ##label KAN !'##cross-references GB:M32559; NID:g333850; PIDN:AAA47333.1; !1PID:g333851 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily rotavirus outer layer protein VP3 KEYWORDS capsid protein; coat protein; glycoprotein; hemagglutinin FEATURE !$1-240 #product outer capsid protein VP8 #status predicted !8#label VP8\ !$241-246 #region cleavage processing #status predicted\ !$247-775 #product outer capsid protein VP5 #status predicted !8#label VP5\ !$56,132,195,324,583, !$589,592,599 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 775 #molecular-weight 87593 #checksum 4719 SEQUENCE /// ENTRY VPXRWL #type complete TITLE outer layer protein VP3 - human rotavirus A (strain L26) ALTERNATE_NAMES VP4 protein CONTAINS outer capsid protein VP5; outer capsid protein VP8 ORGANISM #formal_name human rotavirus A DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jul-1999 ACCESSIONS A36410 REFERENCE A36410 !$#authors Taniguchi, K.; Urasawa, T.; Kobayashi, N.; Gorziglia, M.; !1Urasawa, S. !$#journal J. Virol. (1990) 64:5640-5644 !$#title Nucleotide sequence of VP4 and VP7 genes of human !1rotaviruses with subgroup I specificity and long RNA !1pattern: implication for new G serotype specificity. !$#cross-references MUID:91012813; PMID:2170690 !$#accession A36410 !'##molecule_type genomic RNA !'##residues 1-775 ##label TAN !'##cross-references EMBL:M58292; NID:g333854; PIDN:AAA47335.1; !1PID:g333855 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily rotavirus outer layer protein VP3 KEYWORDS capsid protein; glycoprotein FEATURE !$1-240 #product outer capsid protein VP8 #status predicted !8#label VP8\ !$241-246 #region cleavage processing #status predicted\ !$247-775 #product outer capsid protein VP5 #status predicted !8#label VP5\ !$32,56,97,132,150, !$195,324,583,589,599 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 775 #molecular-weight 87650 #checksum 6192 SEQUENCE /// ENTRY VPXRWM #type complete TITLE outer layer protein VP3 - human rotavirus A (strain L27) ALTERNATE_NAMES VP4 protein CONTAINS outer capsid protein VP5; outer capsid protein VP8 ORGANISM #formal_name human rotavirus A DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 01-Mar-1996 ACCESSIONS C36410 REFERENCE A36410 !$#authors Taniguchi, K.; Urasawa, T.; Kobayashi, N.; Gorziglia, M.; !1Urasawa, S. !$#journal J. Virol. (1990) 64:5640-5644 !$#title Nucleotide sequence of VP4 and VP7 genes of human !1rotaviruses with subgroup I specificity and long RNA !1pattern: implication for new G serotype specificity. !$#cross-references MUID:91012813; PMID:2170690 !$#accession C36410 !'##molecule_type genomic RNA !'##residues 1-775 ##label TAN !'##cross-references EMBL:M58292 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily rotavirus outer layer protein VP3 KEYWORDS capsid protein; glycoprotein FEATURE !$1-240 #product outer capsid protein VP8 #status predicted !8#label VP8\ !$241-246 #region cleavage processing #status predicted\ !$247-775 #product outer capsid protein VP5 #status predicted !8#label VP5\ !$32,56,97,132,150, !$195,324,583,589,599 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 775 #molecular-weight 87506 #checksum 5913 SEQUENCE /// ENTRY VPXRW5 #type complete TITLE outer layer protein VP3 - human rotavirus A (serotype 3 strain P) ALTERNATE_NAMES hemagglutinin CONTAINS outer capsid protein VP5; outer capsid protein VP8 ORGANISM #formal_name human rotavirus A DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 01-Mar-1996 ACCESSIONS C28839 REFERENCE A28839 !$#authors Gorziglia, M.; Green, K.; Nishikawa, K.; Taniguchi, K.; !1Jones, R.; Kapikian, A.Z.; Chanock, R.M. !$#journal J. Virol. (1988) 62:2978-2984 !$#title Sequence of the fourth gene of human rotaviruses recovered !1from asymptomatic or symptomatic infections. !$#cross-references MUID:88275070; PMID:2839714 !$#accession C28839 !'##molecule_type genomic RNA !'##residues 1-775 ##label GOR GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily rotavirus outer layer protein VP3 KEYWORDS capsid protein; coat protein; glycoprotein; hemagglutinin FEATURE !$1-240 #product outer capsid protein VP8 #status predicted !8#label VP8\ !$241-246 #region cleavage processing #status predicted\ !$247-775 #product outer capsid protein VP5 #status predicted !8#label VP5\ !$32,56,97,129,132, !$195,324,583,589, !$592,599 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 775 #molecular-weight 87687 #checksum 7244 SEQUENCE /// ENTRY VPXRW6 #type complete TITLE outer layer protein VP3 - human rotavirus A (serotype 4 strain VA70) ALTERNATE_NAMES hemagglutinin CONTAINS outer capsid protein VP5; outer capsid protein VP8 ORGANISM #formal_name human rotavirus A DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 04-Dec-1994 ACCESSIONS D28839; A25904 REFERENCE A28839 !$#authors Gorziglia, M.; Green, K.; Nishikawa, K.; Taniguchi, K.; !1Jones, R.; Kapikian, A.Z.; Chanock, R.M. !$#journal J. Virol. (1988) 62:2978-2984 !$#title Sequence of the fourth gene of human rotaviruses recovered !1from asymptomatic or symptomatic infections. !$#cross-references MUID:88275070; PMID:2839714 !$#accession D28839 !'##molecule_type genomic RNA !'##residues 1-775 ##label GOR !'##cross-references GB:M88480 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily rotavirus outer layer protein VP3 KEYWORDS capsid protein; coat protein; glycoprotein; hemagglutinin FEATURE !$1-240 #product outer capsid protein VP8 #status predicted !8#label VP8\ !$247-775 #product outer capsid protein VP5 #status predicted !8#label VP5\ !$32,56,97,129,132, !$195,324,577,583, !$589,592 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 775 #molecular-weight 87609 #checksum 3991 SEQUENCE /// ENTRY VPXR16 #type complete TITLE outer capsid protein VP8 - human rotavirus A (serotype 2 strain 1076) ORGANISM #formal_name human rotavirus A DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 30-Sep-1993 ACCESSIONS F25904 REFERENCE A94126 !$#authors Gorziglia, M.; Hoshino, Y.; Buckler-White, A.; Blumentals, !1I.; Glass, R.; Flores, J.; Kapikian, A.Z.; Chanock, R.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:7039-7043 !$#title Conservation of amino acid sequence of VP8 and cleavage !1region of 84-kDa outer capsid protein among rotaviruses !1recovered from asymptomatic neonatal infection. !$#cross-references MUID:86313706; PMID:3018754 !$#accession F25904 !'##molecule_type genomic RNA !'##residues 1-280 ##label GOR COMMENT VP8 is one of two trypsin cleavage products of VP3; the !1other product is VP5. GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily rotavirus outer layer protein VP3 KEYWORDS glycoprotein; outer capsid protein FEATURE !$32,56,85,97,111, !$114,132,192,277 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 280 #molecular-weight 32132 #checksum 9878 SEQUENCE /// ENTRY VPXRMN #type complete TITLE outer capsid protein VP8 - human rotavirus A (strain McN) ORGANISM #formal_name human rotavirus A DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 30-Sep-1993 ACCESSIONS G25904 REFERENCE A94126 !$#authors Gorziglia, M.; Hoshino, Y.; Buckler-White, A.; Blumentals, !1I.; Glass, R.; Flores, J.; Kapikian, A.Z.; Chanock, R.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:7039-7043 !$#title Conservation of amino acid sequence of VP8 and cleavage !1region of 84-kDa outer capsid protein among rotaviruses !1recovered from asymptomatic neonatal infection. !$#cross-references MUID:86313706; PMID:3018754 !$#accession G25904 !'##molecule_type genomic RNA !'##residues 1-280 ##label GOR COMMENT VP8 is one of two trypsin cleavage products of VP3; the !1other product is VP5. GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily rotavirus outer layer protein VP3 KEYWORDS glycoprotein; outer capsid protein FEATURE !$32,56,85,97,111, !$114,132,192,277 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 280 #molecular-weight 32095 #checksum 544 SEQUENCE /// ENTRY VPXRW7 #type complete TITLE outer layer protein VP3 - human rotavirus A (serotype 1 strain M37) ALTERNATE_NAMES hemagglutinin CONTAINS outer capsid protein VP5; outer capsid protein VP8 ORGANISM #formal_name human rotavirus A DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 04-Dec-1994 ACCESSIONS E28839; E25904 REFERENCE A28839 !$#authors Gorziglia, M.; Green, K.; Nishikawa, K.; Taniguchi, K.; !1Jones, R.; Kapikian, A.Z.; Chanock, R.M. !$#journal J. Virol. (1988) 62:2978-2984 !$#title Sequence of the fourth gene of human rotaviruses recovered !1from asymptomatic or symptomatic infections. !$#cross-references MUID:88275070; PMID:2839714 !$#accession E28839 !'##molecule_type genomic RNA !'##residues 1-775 ##label GOR !'##cross-references GB:M88480 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily rotavirus outer layer protein VP3 KEYWORDS capsid protein; coat protein; glycoprotein; hemagglutinin FEATURE !$1-240 #product outer capsid protein VP8 #status predicted !8#label VP8\ !$247-775 #product outer capsid protein VP5 #status predicted !8#label VP5\ !$32,56,97,111,114, !$132,146,192,277, !$324,583,606 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 775 #molecular-weight 87402 #checksum 5667 SEQUENCE /// ENTRY VPXRW8 #type complete TITLE outer layer protein VP3 - human rotavirus A (serotype 2 strain 1076) ALTERNATE_NAMES hemagglutinin CONTAINS outer capsid protein VP5; outer capsid protein VP8 ORGANISM #formal_name human rotavirus A DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 01-Mar-1996 ACCESSIONS F28839 REFERENCE A28839 !$#authors Gorziglia, M.; Green, K.; Nishikawa, K.; Taniguchi, K.; !1Jones, R.; Kapikian, A.Z.; Chanock, R.M. !$#journal J. Virol. (1988) 62:2978-2984 !$#title Sequence of the fourth gene of human rotaviruses recovered !1from asymptomatic or symptomatic infections. !$#cross-references MUID:88275070; PMID:2839714 !$#accession F28839 !'##molecule_type genomic RNA !'##residues 1-775 ##label GOR GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily rotavirus outer layer protein VP3 KEYWORDS capsid protein; coat protein; glycoprotein; hemagglutinin FEATURE !$1-240 #product outer capsid protein VP8 #status predicted !8#label VP8\ !$241-246 #region cleavage processing #status predicted\ !$247-775 #product outer capsid protein VP5 #status predicted !8#label VP5\ !$32,56,85,97,111, !$114,132,192,277, !$324,583,606 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 775 #molecular-weight 87697 #checksum 7493 SEQUENCE /// ENTRY VPXRW9 #type complete TITLE outer layer protein VP3 - human rotavirus A (serotype 3 strain McN13) ALTERNATE_NAMES hemagglutinin CONTAINS outer capsid protein VP5; outer capsid protein VP8 ORGANISM #formal_name human rotavirus A DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 01-Mar-1996 ACCESSIONS G28839 REFERENCE A28839 !$#authors Gorziglia, M.; Green, K.; Nishikawa, K.; Taniguchi, K.; !1Jones, R.; Kapikian, A.Z.; Chanock, R.M. !$#journal J. Virol. (1988) 62:2978-2984 !$#title Sequence of the fourth gene of human rotaviruses recovered !1from asymptomatic or symptomatic infections. !$#cross-references MUID:88275070; PMID:2839714 !$#accession G28839 !'##molecule_type genomic RNA !'##residues 1-776 ##label GOR GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily rotavirus outer layer protein VP3 KEYWORDS capsid protein; coat protein; glycoprotein; hemagglutinin FEATURE !$1-241 #product outer capsid protein VP8 #status predicted !8#label VP8\ !$242-246 #region cleavage processing #status predicted\ !$247-776 #product outer capsid protein VP5 #status predicted !8#label VP5\ !$32,56,85,97,111, !$114,132,193,278, !$325,584,607 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 776 #molecular-weight 87793 #checksum 4092 SEQUENCE /// ENTRY VPXRWT #type complete TITLE outer layer protein VP3 - human rotavirus A (serotype 4 strain ST3) ALTERNATE_NAMES hemagglutinin CONTAINS outer capsid protein VP5; outer capsid protein VP8 ORGANISM #formal_name human rotavirus A DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 04-Dec-1994 ACCESSIONS H28839; H25904 REFERENCE A28839 !$#authors Gorziglia, M.; Green, K.; Nishikawa, K.; Taniguchi, K.; !1Jones, R.; Kapikian, A.Z.; Chanock, R.M. !$#journal J. Virol. (1988) 62:2978-2984 !$#title Sequence of the fourth gene of human rotaviruses recovered !1from asymptomatic or symptomatic infections. !$#cross-references MUID:88275070; PMID:2839714 !$#accession H28839 !'##molecule_type genomic RNA !'##residues 1-774 ##label GOR !'##cross-references GB:M88480 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily rotavirus outer layer protein VP3 KEYWORDS capsid protein; coat protein; glycoprotein; hemagglutinin FEATURE !$1-240 #product outer capsid protein VP8 #status predicted !8#label VP8\ !$247-774 #product outer capsid protein VP5 #status predicted !8#label VP5\ !$32,56,97,111,114, !$132,192,277,324, !$583,606 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 774 #molecular-weight 87455 #checksum 4293 SEQUENCE /// ENTRY VPXRPG #type complete TITLE outer layer protein VP4 - porcine rotavirus C (type 4, strain Gottfried) ALTERNATE_NAMES outer capsid protein VP4 CONTAINS outer capsid protein VP5; outer capsid protein VP8 ORGANISM #formal_name porcine rotavirus C DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS A33563 REFERENCE A33563 !$#authors Gorziglia, M.; Nishikawa, K.; Hoshino, Y.; Taniguchi, K. !$#journal J. Virol. (1990) 64:414-418 !$#title Similarity of the outer capsid protein VP4 of the Gottfried !1strain of porcine rotavirus to that of asymptomatic human !1rotavirus strains. !$#cross-references MUID:90080150; PMID:2152826 !$#accession A33563 !'##molecule_type genomic RNA !'##residues 1-775 ##label GOR !'##cross-references GB:M33516; NID:g333315; PIDN:AAA47095.1; !1PID:g333316 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily rotavirus outer layer protein VP3 KEYWORDS glycoprotein; outer capsid protein FEATURE !$1-240 #product outer capsid protein VP8 #status predicted !8#label VP8\ !$241-246 #region cleavage processing #status predicted\ !$247-775 #product outer capsid protein VP5 #status predicted !8#label VP5\ !$32,56,97,132,324, !$583 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 775 #molecular-weight 87098 #checksum 4192 SEQUENCE /// ENTRY VPXRRR #type complete TITLE outer capsid protein VP8 - human rotavirus A (strain RRV) ORGANISM #formal_name human rotavirus A DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 30-Sep-1993 ACCESSIONS I25904 REFERENCE A94126 !$#authors Gorziglia, M.; Hoshino, Y.; Buckler-White, A.; Blumentals, !1I.; Glass, R.; Flores, J.; Kapikian, A.Z.; Chanock, R.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1986) 83:7039-7043 !$#title Conservation of amino acid sequence of VP8 and cleavage !1region of 84-kDa outer capsid protein among rotaviruses !1recovered from asymptomatic neonatal infection. !$#cross-references MUID:86313706; PMID:3018754 !$#accession I25904 !'##molecule_type genomic RNA !'##residues 1-281 ##label GOR COMMENT VP8 is one of two trypsin cleavage products of VP3; the !1other product is VP5. GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily rotavirus outer layer protein VP3 KEYWORDS glycoprotein; outer capsid protein FEATURE !$32,56,97,111,132, !$149,183,198,242 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 281 #molecular-weight 31468 #checksum 5744 SEQUENCE /// ENTRY VPXRPC #type complete TITLE outer layer protein VP4 - porcine rotavirus C (strain Cowden) ALTERNATE_NAMES hemagglutinin; outer capsid protein VP4 CONTAINS outer capsid protein VP5; outer capsid protein VP8 ORGANISM #formal_name porcine rotavirus C DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS D40822 REFERENCE A40822 !$#authors Bremont, M.; Juste-Lesage, P.; Chabanne-Vautherot, D.; !1Charpilienne, A.; Cohen, J. !$#journal Virology (1992) 186:684-692 !$#title Sequences of the four larger proteins of a porcine group C !1rotavirus and comparison with the equivalent group A !1rotavirus proteins. !$#cross-references MUID:92124743; PMID:1310192 !$#accession D40822 !'##molecule_type genomic RNA !'##residues 1-736 ##label BRE !'##cross-references GB:M74218; NID:g333317; PIDN:AAB00802.1; !1PID:g333318 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily rotavirus outer layer protein VP3 KEYWORDS glycoprotein; hemagglutinin; outer capsid protein FEATURE !$1-243 #product outer capsid protein VP8 #status predicted !8#label VP8\ !$244-250 #region cleavage processing #status predicted\ !$251-736 #product outer capsid protein VP5 #status predicted !8#label VP5\ !$39,61,64,93,162, !$191,237,251,304, !$471,631 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 736 #molecular-weight 83231 #checksum 2438 SEQUENCE /// ENTRY VPXR6H #type complete TITLE inner capsid protein VP6 - human rotavirus A ORGANISM #formal_name human rotavirus A DATE 20-Sep-1984 #sequence_revision 20-Sep-1984 #text_change 16-Jul-1999 ACCESSIONS A04130 REFERENCE A93002 !$#authors Both, G.W.; Siegman, L.J.; Bellamy, A.R.; Ikegami, N.; !1Shatkin, A.J.; Furuichi, Y. !$#journal J. Virol. (1984) 51:97-101 !$#title Comparative sequence analysis of rotavirus genomic segment !16- the gene specifying viral subgroups 1 and 2. !$#cross-references MUID:84216525; PMID:6328048 !$#accession A04130 !'##molecule_type genomic RNA !'##residues 1-397 ##label BOT !'##cross-references GB:K02086; NID:g333802; PIDN:AAA47311.1; !1PID:g333803 !'##experimental_source strain Wa COMMENT The genome consists of 11 segments of double-stranded RNA. GENETICS !$#map_position segment 11 CLASSIFICATION #superfamily rotavirus VP6 protein KEYWORDS capsid protein SUMMARY #length 397 #molecular-weight 44937 #checksum 7975 SEQUENCE /// ENTRY VPXRS2 #type complete TITLE inner capsid protein VP6 - human rotavirus A (serotype 2 strain S2) ALTERNATE_NAMES inner shell protein VP6 ORGANISM #formal_name human rotavirus A DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 16-Jul-1999 ACCESSIONS A26849 REFERENCE A26849 !$#authors Hofer, J.M.I.; Sato, F.; Street, J.E.; Bellamy, A.R. !$#journal Nucleic Acids Res. (1987) 15:7175 !$#title Nucleotide sequence for gene 6 of rotavirus strain S2. !$#cross-references MUID:88015552; PMID:2821494 !$#accession A26849 !'##molecule_type genomic RNA !'##residues 1-397 ##label HOF !'##cross-references EMBL:Y00437; NID:g61887; PIDN:CAA68495.1; !1PID:g61888 GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily rotavirus VP6 protein KEYWORDS capsid protein SUMMARY #length 397 #molecular-weight 44906 #checksum 543 SEQUENCE /// ENTRY VPXR6S #type complete TITLE inner capsid protein VP6 - simian rotavirus SA11 ALTERNATE_NAMES major inner capsid protein ORGANISM #formal_name simian rotavirus SA11 #note host (monkey) DATE 20-Sep-1984 #sequence_revision 20-Sep-1984 #text_change 16-Jul-1999 ACCESSIONS A93002; A93505; A04131 REFERENCE A93002 !$#authors Both, G.W.; Siegman, L.J.; Bellamy, A.R.; Ikegami, N.; !1Shatkin, A.J.; Furuichi, Y. !$#journal J. Virol. (1984) 51:97-101 !$#title Comparative sequence analysis of rotavirus genomic segment !16- the gene specifying viral subgroups 1 and 2. !$#cross-references MUID:84216525; PMID:6328048 !$#accession A93002 !'##molecule_type genomic RNA !'##residues 1-397 ##label BOT REFERENCE A93505 !$#authors Estes, M.K.; Mason, B.B.; Crawford, S.; Cohen, J. !$#journal Nucleic Acids Res. (1984) 12:1875-1887 !$#title Cloning and nucleotide sequence of the simian rotavirus gene !16 that codes for the major inner capsid protein. !$#cross-references MUID:84144075; PMID:6322125 !$#accession A93505 !'##molecule_type genomic RNA !'##residues 1-163,'F',165-384,'V',386-397 ##label EST !'##cross-references GB:X00421; NID:g61878; PIDN:CAA25122.1; PID:g61879 COMMENT The genome consists of 11 segments of double-stranded RNA. GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily rotavirus VP6 protein KEYWORDS coat protein SUMMARY #length 397 #molecular-weight 44903 #checksum 306 SEQUENCE /// ENTRY VPXR11 #type complete TITLE inner capsid protein VP6 - simian rotavirus SA11 ORGANISM #formal_name simian rotavirus SA11 DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jul-1999 ACCESSIONS JQ0019 REFERENCE JQ0019 !$#authors Smith, R.E.; Kister, S.E.; Carozzi, N.B. !$#journal Gene (1989) 79:239-248 !$#title Cloning and expression of the major inner capsid protein of !1SA-11 simian rotavirus in Escherichia coli. !$#cross-references MUID:90006753; PMID:2551775 !$#accession JQ0019 !'##molecule_type mRNA !'##residues 1-397 ##label SMI !'##cross-references GB:M27824; NID:g333894; PIDN:AAA47397.1; !1PID:g333895 GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily rotavirus VP6 protein KEYWORDS capsid protein; coat protein SUMMARY #length 397 #molecular-weight 44873 #checksum 9915 SEQUENCE /// ENTRY VPXRBR #type complete TITLE inner capsid protein VP6 - bovine rotavirus A (strain RF) ALTERNATE_NAMES major capsid protein; major internal structural protein ORGANISM #formal_name bovine rotavirus A #note host Bos sp. (cattle) DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 12-Dec-1997 ACCESSIONS A04132 REFERENCE A04132 !$#authors Cohen, J.; Lefevre, F.; Estes, M.K.; Bremont, M. !$#journal Virology (1984) 138:178-182 !$#title Cloning of bovine rotavirus (RF strain): nucleotide sequence !1of the gene coding for the major capsid protein. !$#cross-references MUID:85042067; PMID:6093360 !$#accession A04132 !'##molecule_type genomic RNA !'##residues 1-397 ##label COH !'##cross-references GB:K02254; NID:g333813; PID:g333814 !'##note the authors translated the codon CCA for residue 142 as Gln GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily rotavirus VP6 protein KEYWORDS capsid protein SUMMARY #length 397 #molecular-weight 44811 #checksum 9914 SEQUENCE /// ENTRY VPXR14 #type complete TITLE inner capsid protein VP6 - equine rotavirus A (strain FI-14) ORGANISM #formal_name equine rotavirus A DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jun-2000 ACCESSIONS JS0246 REFERENCE JS0246 !$#authors Gorziglia, M.; Hoshino, Y.; Nishikawa, K.; Maloy, W.L.; !1Jones, R.W.; Kapikian, A.Z.; Chanock, R.M. !$#journal J. Gen. Virol. (1988) 69:1659-1669 !$#title Comparative sequence analysis of the genomic segment 6 of !1four rotaviruses each with a different subgroup specificity. !$#cross-references MUID:88274335; PMID:2455770 !$#accession JS0246 !'##molecule_type mRNA !'##residues 1-397 ##label GOR !'##cross-references DDBJ:D00323; NID:g222521; PIDN:BAA00235.1; !1PID:g222522 GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily rotavirus VP6 protein KEYWORDS capsid protein; coat protein SUMMARY #length 397 #molecular-weight 44935 #checksum 9416 SEQUENCE /// ENTRY VPXR15 #type complete TITLE inner capsid protein VP6 - equine rotavirus A (strain H-2) ORGANISM #formal_name equine rotavirus A DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jun-2000 ACCESSIONS JS0247 REFERENCE JS0246 !$#authors Gorziglia, M.; Hoshino, Y.; Nishikawa, K.; Maloy, W.L.; !1Jones, R.W.; Kapikian, A.Z.; Chanock, R.M. !$#journal J. Gen. Virol. (1988) 69:1659-1669 !$#title Comparative sequence analysis of the genomic segment 6 of !1four rotaviruses each with a different subgroup specificity. !$#cross-references MUID:88274335; PMID:2455770 !$#accession JS0247 !'##molecule_type mRNA !'##residues 1-399 ##label GOR !'##cross-references DDBJ:D00324; NID:g222523; PIDN:BAA00236.1; !1PID:g222524 GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily rotavirus VP6 protein KEYWORDS capsid protein; coat protein SUMMARY #length 399 #molecular-weight 45197 #checksum 7216 SEQUENCE /// ENTRY VPXR76 #type complete TITLE inner capsid protein VP6 - human rotavirus A (serotype 2 strain 1076) ORGANISM #formal_name human rotavirus A DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jun-2000 ACCESSIONS JS0248 REFERENCE JS0246 !$#authors Gorziglia, M.; Hoshino, Y.; Nishikawa, K.; Maloy, W.L.; !1Jones, R.W.; Kapikian, A.Z.; Chanock, R.M. !$#journal J. Gen. Virol. (1988) 69:1659-1669 !$#title Comparative sequence analysis of the genomic segment 6 of !1four rotaviruses each with a different subgroup specificity. !$#cross-references MUID:88274335; PMID:2455770 !$#accession JS0248 !'##molecule_type mRNA !'##residues 1-397 ##label GOR !'##cross-references DDBJ:D00325; NID:g222515; PIDN:BAA00237.1; !1PID:g222516 GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily rotavirus VP6 protein KEYWORDS capsid protein; coat protein SUMMARY #length 397 #molecular-weight 44929 #checksum 9972 SEQUENCE /// ENTRY VPXRGT #type complete TITLE inner capsid protein VP6 - porcine rotavirus C (strain Gottfried) ORGANISM #formal_name porcine rotavirus C DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jun-2000 ACCESSIONS JS0249 REFERENCE JS0246 !$#authors Gorziglia, M.; Hoshino, Y.; Nishikawa, K.; Maloy, W.L.; !1Jones, R.W.; Kapikian, A.Z.; Chanock, R.M. !$#journal J. Gen. Virol. (1988) 69:1659-1669 !$#title Comparative sequence analysis of the genomic segment 6 of !1four rotaviruses each with a different subgroup specificity. !$#cross-references MUID:88274335; PMID:2455770 !$#accession JS0249 !'##molecule_type mRNA !'##residues 1-397 ##label GOR !'##cross-references DDBJ:D00326; NID:g222517; PIDN:BAA00238.1; !1PID:g222518 GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily rotavirus VP6 protein KEYWORDS capsid protein; coat protein SUMMARY #length 397 #molecular-weight 44965 #checksum 7810 SEQUENCE /// ENTRY VPXRPR #type complete TITLE inner capsid protein VP6 - porcine rotavirus C (strain Cowden) ALTERNATE_NAMES major inner capsid protein ORGANISM #formal_name porcine rotavirus C DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jul-1999 ACCESSIONS A36216; A43385 REFERENCE A36216 !$#authors Bremont, M.; Chabanne-Vautherot, D.; Vannier, P.; McCrae, !1M.A.; Cohen, J. !$#journal Virology (1990) 178:579-583 !$#title Sequence analysis of the gene (6) encoding the major capsid !1protein (VP6) of group C rotavirus: higher than expected !1homology to the corresponding protein from group A virus. !$#cross-references MUID:91020998; PMID:2171196 !$#accession A36216 !'##molecule_type genomic RNA !'##residues 1-394 ##label BRE !'##cross-references EMBL:M29287; NID:g333319; PIDN:AAA47096.1; !1PID:g333320 REFERENCE A43385 !$#authors Cooke, S.J.; Clarke, I.N.; Freitas, R.B.; Gabbay, Y.B.; !1Lambden, P.R. !$#journal Virology (1992) 190:531-537 !$#title The correct sequence of the porcine group C/Cowden rotavirus !1major inner capsid protein shows close homology with human !1isolates from Brazil and the U.K. !$#cross-references MUID:92410641; PMID:1326817 !$#accession A43385 !'##molecule_type genomic RNA !'##residues 1-143,'RRENPVYEYK',153-346,'V',348-394 ##label COO !'##cross-references GB:M94157; NID:g333321; PIDN:AAA47097.1; !1PID:g333322 GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily rotavirus VP6 protein KEYWORDS capsid protein SUMMARY #length 394 #molecular-weight 44475 #checksum 4800 SEQUENCE /// ENTRY VPXRCR #type complete TITLE inner capsid protein VP6 - human rotavirus C ALTERNATE_NAMES major inner capsid protein ORGANISM #formal_name human rotavirus C DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS A41041; B43385 REFERENCE A41041 !$#authors Cooke, S.J.; Lambden, P.R.; Caul, E.O.; Clarke, I.N. !$#journal Virology (1991) 184:781-785 !$#title Molecular cloning, sequence analysis and coding assignment !1of the major inner capsid protein gene of human group C !1rotavirus. !$#cross-references MUID:91361573; PMID:1653500 !$#accession A41041 !'##molecule_type genomic RNA !'##residues 1-395 ##label COO !'##cross-references EMBL:X59843; NID:g297570; PIDN:CAA42504.1; !1PID:g297571 !'##experimental_source strain Bristol REFERENCE A43385 !$#authors Cooke, S.J.; Clarke, I.N.; Freitas, R.B.; Gabbay, Y.B.; !1Lambden, P.R. !$#journal Virology (1992) 190:531-537 !$#title The correct sequence of the porcine group C/Cowden rotavirus !1major inner capsid protein shows close homology with human !1isolates from Brazil and the U.K. !$#cross-references MUID:92410641; PMID:1326817 !$#accession B43385 !'##molecule_type genomic RNA !'##residues 1-395 ##label CO2 !'##cross-references GB:M94155; NID:g294735; PIDN:AAA47339.1; !1PID:g294736 !'##experimental_source strain Belem GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily rotavirus VP6 protein KEYWORDS capsid protein; coat protein SUMMARY #length 395 #molecular-weight 44720 #checksum 7698 SEQUENCE /// ENTRY A43386 #type complete TITLE inner capsid protein VP6 - bovine rotavirus C (strain Shintoku) ALTERNATE_NAMES major inner capsid protein ORGANISM #formal_name bovine rotavirus C DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS A43386 REFERENCE A43386 !$#authors Jiang, B.; Tsunemitsu, H.; Gentsch, J.R.; Glass, R.I.; !1Green, K.Y.; Qian, Y.; Saif, L.J. !$#journal Virology (1992) 190:542-547 !$#title Nucleotide sequence of gene 5 encoding the inner capsid !1protein (VP6) of bovine group C rotavirus: comparison with !1corresponding genes of group C, A, and B rotaviruses. !$#cross-references MUID:92410643; PMID:1326819 !$#accession A43386 !'##molecule_type genomic RNA !'##residues 1-395 ##label JIA !'##cross-references GB:M88768; NID:g333883; PIDN:AAA03235.1; !1PID:g333884 GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily rotavirus VP6 protein KEYWORDS capsid protein; coat protein SUMMARY #length 395 #molecular-weight 44534 #checksum 9178 SEQUENCE /// ENTRY VPXRC3 #type complete TITLE minor inner core protein VP6 - bluetongue virus (serotype 10, American isolate) ALTERNATE_NAMES inner capsid protein VP6; VP6 protein ORGANISM #formal_name bluetongue virus DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 10-Nov-1995 ACCESSIONS B32400; S10542 REFERENCE A32400 !$#authors Fukusho, A.; Yu, Y.; Yamaguchi, S.; Roy, P. !$#journal J. Gen. Virol. (1989) 70:1677-1689 !$#title Completion of the sequence of bluetongue virus serotype 10 !1by the characterization of a structural protein, VP6, and a !1non-structural protein, NS2. !$#cross-references MUID:89293076; PMID:2544660 !$#accession B32400 !'##molecule_type genomic RNA !'##residues 1-328 ##label FUK REFERENCE S10534 !$#authors Roy, P.; Marshall, J.J.A.; French, T.J. !$#journal Curr. Top. Microbiol. Immunol. (1990) 162:43-87 !$#title Structure of the bluetongue virus genome and its encoded !1proteins. !$#cross-references MUID:90345726; PMID:2166648 !$#accession S10542 !'##status preliminary !'##molecule_type genomic RNA !'##residues 1-328 ##label CUR GENETICS !$#map_position segment 9 CLASSIFICATION #superfamily bluetongue virus VP6 protein KEYWORDS capsid protein SUMMARY #length 328 #molecular-weight 35749 #checksum 5072 SEQUENCE /// ENTRY JQ1875 #type complete TITLE inner capsid protein VP6 - bluetongue virus (serotype 1, strain South Africa) ALTERNATE_NAMES VP6 protein ORGANISM #formal_name bluetongue virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jun-2000 ACCESSIONS JQ1875 REFERENCE JQ1875 !$#authors Wade-Evans, A.M.; Mertens, P.P.C.; Belsham, G.J. !$#journal J. Gen. Virol. (1992) 73:3023-3026 !$#title Sequence of genome segment 9 of bluetongue virus (serotype !11, South Africa) and expression analysis demonstrating that !1different forms of VP6 are derived from initiation of !1protein synthesis at two distinct sites. !$#cross-references MUID:93057380; PMID:1331303 !$#accession JQ1875 !'##molecule_type genomic RNA !'##residues 1-328 ##label WAD !'##cross-references GB:D10905; NID:g221080; PIDN:BAA01713.1; !1PID:g221081 GENETICS !$#map_position segment 9 CLASSIFICATION #superfamily bluetongue virus VP6 protein KEYWORDS capsid protein SUMMARY #length 328 #molecular-weight 35928 #checksum 4514 SEQUENCE /// ENTRY A48561 #type complete TITLE inner capsid protein VP6 - bluetongue virus (serotype 11, strain USA) ORGANISM #formal_name bluetongue virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 17-Feb-1994 ACCESSIONS A48561 REFERENCE A48561 !$#authors Hwang, G.Y.; Chiou, J.F.; Yang, Y.Y.; Li, J.K. !$#journal Virus Res. (1992) 24:315-323 !$#title Comparative sequence analyses of the cognate structural !1protein VP6 genes of five US bluetongue viruses. !$#cross-references MUID:93033709; PMID:1329371 !$#accession A48561 !'##molecule_type genomic RNA !'##residues 1-325 ##label HWA !'##note sequence extracted from NCBI backbone (NCBIN:115442, !1NCBIP:115444) GENETICS !$#map_position segment 9 CLASSIFICATION #superfamily bluetongue virus VP6 protein KEYWORDS capsid protein SUMMARY #length 325 #molecular-weight 35354 #checksum 2927 SEQUENCE /// ENTRY B48561 #type complete TITLE inner capsid protein VP6 - bluetongue virus (serotype 10, strain USA) ORGANISM #formal_name bluetongue virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS B48561 REFERENCE A48561 !$#authors Hwang, G.Y.; Chiou, J.F.; Yang, Y.Y.; Li, J.K. !$#journal Virus Res. (1992) 24:315-323 !$#title Comparative sequence analyses of the cognate structural !1protein VP6 genes of five US bluetongue viruses. !$#cross-references MUID:93033709; PMID:1329371 !$#accession B48561 !'##molecule_type genomic RNA !'##residues 1-325 ##label HWA !'##cross-references GB:L08669; NID:g210842; PIDN:AAA42818.1; !1PID:g210843 !'##note sequence extracted from NCBI backbone (NCBIP:115445) GENETICS !$#map_position segment 9 CLASSIFICATION #superfamily bluetongue virus VP6 protein KEYWORDS capsid protein SUMMARY #length 325 #molecular-weight 35163 #checksum 4288 SEQUENCE /// ENTRY VPXRHB #type complete TITLE major inner capsid protein - human rotavirus B ORGANISM #formal_name human rotavirus B #note host Homo sapiens (man) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS A39993 REFERENCE A39993 !$#authors Chen, G.M.; Werner-Eckert, R.; Tao, H.; Mackow, E.R. !$#journal Virology (1991) 182:820-829 !$#title Expression of the major inner capsid protein of the group B !1rotavirus ADRV: primary characterization of genome segment !15. !$#cross-references MUID:91220732; PMID:1850929 !$#accession A39993 !'##molecule_type genomic RNA !'##residues 1-391 ##label CHE !'##cross-references GB:M55982; NID:g333876; PIDN:AAA47353.1; !1PID:g333877 !'##experimental_source Chinese adult diarrheal rotavirus strain GENETICS !$#map_position segment 5 CLASSIFICATION #superfamily human rotavirus B major inner capsid protein KEYWORDS capsid protein SUMMARY #length 391 #molecular-weight 43671 #checksum 9735 SEQUENCE /// ENTRY VPXRIB #type complete TITLE major inner capsid protein - human rotavirus B (strain IDIR, infectious diarrhea of infant rats) ORGANISM #formal_name human rotavirus B #note host Homo sapiens (man) DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS A42540 REFERENCE A42540 !$#authors Eiden, J.J.; Nataro, J.; Vonderfecht, S.; Petric, M. !$#journal Virology (1992) 188:580-589 !$#title Molecular cloning, sequence analysis, in vitro expression, !1and immunoprecipitation of the major inner capsid protein of !1the IDIR strain of group B rotavirus (GBR). !$#cross-references MUID:92263761; PMID:1316675 !$#accession A42540 !'##molecule_type genomic RNA !'##residues 1-391 ##label EID !'##cross-references GB:M84456; NID:g333872; PIDN:AAA47348.1; !1PID:g333873 GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily human rotavirus B major inner capsid protein KEYWORDS capsid protein SUMMARY #length 391 #molecular-weight 43646 #checksum 9445 SEQUENCE /// ENTRY VGXR1S #type complete TITLE glycoprotein VP7 precursor - simian rotavirus SA11 ORGANISM #formal_name simian rotavirus SA11 DATE 18-Apr-1984 #sequence_revision 18-Apr-1984 #text_change 16-Jul-1999 ACCESSIONS A04135; A92999 REFERENCE A93949 !$#authors Both, G.W.; Mattick, J.S.; Bellamy, A.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:3091-3095 !$#title Serotype-specific glycoprotein of simian 11 retovirus: !1coding assignment and gene sequence. !$#cross-references MUID:83221547; PMID:6304692 !$#accession A04135 !'##molecule_type genomic RNA !'##residues 1-326 ##label BOT !'##cross-references GB:V01190; NID:g61682; PIDN:CAA24510.1; PID:g61683 REFERENCE A92999 !$#authors Arias, C.F.; Lopez, S.; Bell, J.R.; Strauss, J.H. !$#journal J. Virol. (1984) 50:657-661 !$#title Primary structure of the neutralization antigen of simian !1rotavirus SA11 as deduced from cDNA sequence. !$#cross-references MUID:84165100; PMID:6323768 !$#accession A92999 !'##molecule_type genomic RNA !'##residues 1-15,'T',17-31,'F',33-36,'F',38-59,'A',61-74,'P',76-113, !1'E',115-218,'P',220-326 ##label ARI !'##cross-references GB:K02028; NID:g333791; PIDN:AAA47307.1; !1PID:g333792 GENETICS !$#map_position segment 9 CLASSIFICATION #superfamily rotavirus glycoprotein VP7 KEYWORDS coat protein; glycoprotein; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-326 #product glycoprotein VP7 #status predicted #label !8GVP\ !$32-48 #region hydrophobic #status predicted\ !$69 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 326 #molecular-weight 37119 #checksum 886 SEQUENCE /// ENTRY VGXRRH #type complete TITLE glycoprotein VP7 precursor - rhesus rotavirus ALTERNATE_NAMES outer shell glycoprotein ORGANISM #formal_name rhesus rotavirus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS A29247 REFERENCE A29247 !$#authors Mackow, E.R.; Shaw, R.D.; Matsui, S.M.; Vo, P.T.; Benfield, !1D.A.; Greenberg, H.B. !$#journal Virology (1988) 165:511-517 !$#title Characterization of homotypic and heterotypic VP7 !1neutralization sites of rhesus rotavirus. !$#cross-references MUID:88306243; PMID:2457279 !$#accession A29247 !'##molecule_type genomic RNA !'##residues 1-326 ##label MAC !'##cross-references GB:M21650; NID:g333870; PIDN:AAA47346.1; !1PID:g333871 GENETICS !$#map_position segment 9 CLASSIFICATION #superfamily rotavirus glycoprotein VP7 KEYWORDS coat protein; glycoprotein; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-326 #product glycoprotein VP7 #status predicted #label !8GVP\ !$32-48 #region hydrophobic #status predicted\ !$69 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 326 #molecular-weight 36988 #checksum 9352 SEQUENCE /// ENTRY VGXRPR #type complete TITLE glycoprotein VP7 precursor - porcine rotavirus C (serotype 5, strain OSU) ALTERNATE_NAMES outer shell glycoprotein ORGANISM #formal_name porcine rotavirus C DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jul-1999 ACCESSIONS A29151 REFERENCE A29151 !$#authors Gorziglia, M.; Aguirre, Y.; Hoshino, Y.; Esparza, J.; !1Blumentals, I.; Askaa, J.; Thompson, M.; Glass, R.I.; !1Kapikian, A.Z.; Chanock, R.M. !$#journal J. Gen. Virol. (1986) 67:2445-2454 !$#title VP7 serotype-specific glycoprotein of OSU porcine rotavirus: !1coding assignment and gene sequence. !$#cross-references MUID:87059767; PMID:3023532 !$#accession A29151 !'##molecule_type genomic RNA !'##residues 1-326 ##label GOR !'##cross-references GB:X04613; NID:g61856; PIDN:CAA28283.1; PID:g61857 GENETICS !$#map_position segment 9 CLASSIFICATION #superfamily rotavirus glycoprotein VP7 KEYWORDS coat protein; glycoprotein; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-326 #product glycoprotein VP7 #status predicted #label !8GVP\ !$32-48 #region hydrophobic #status predicted\ !$69 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 326 #molecular-weight 36976 #checksum 1489 SEQUENCE /// ENTRY VGXRT1 #type complete TITLE glycoprotein VP7 precursor - porcine rotavirus A (serotype G5 strain TFR-41) ORGANISM #formal_name porcine rotavirus A DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 07-May-1999 ACCESSIONS D60075 REFERENCE A60075 !$#authors Huang, J.; Nagesha, H.S.; Dyall-Smith, M.L.; Holmes, I.H. !$#journal Arch. Virol. (1989) 109:173-183 !$#title Comparative sequence analysis of VP7 genes from five !1Australian porcine rotaviruses. !$#cross-references MUID:90120966; PMID:2558633 !$#accession D60075 !'##molecule_type DNA !'##residues 1-326 ##label HUA GENETICS !$#map_position segment 9 CLASSIFICATION #superfamily rotavirus glycoprotein VP7 KEYWORDS coat protein; glycoprotein; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-326 #product glycoprotein VP7 #status predicted #label !8VP7\ !$32-48 #region hydrophobic #status predicted\ !$69 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 326 #molecular-weight 36991 #checksum 2572 SEQUENCE /// ENTRY VGXRPY #type complete TITLE glycoprotein VP7 precursor - porcine rotavirus C (strain YM) ALTERNATE_NAMES major outer layer glycoprotein VP7 ORGANISM #formal_name porcine rotavirus C DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jul-1999 ACCESSIONS A31160 REFERENCE A31160 !$#authors Ruiz, A.M.; Lopez, I.V.; Lopez, S.; Espejo, R.T.; Arias, !1C.F. !$#journal J. Virol. (1988) 62:4331-4336 !$#title Molecular and antigenic characterization of porcine !1rotavirus YM, a possible new rotavirus serotype. !$#cross-references MUID:89012209; PMID:2845146 !$#accession A31160 !'##molecule_type genomic RNA !'##residues 1-326 ##label RUI !'##cross-references GB:M23194; NID:g516630; PIDN:AAA47099.1; !1PID:g516631 GENETICS !$#map_position segment 9 CLASSIFICATION #superfamily rotavirus glycoprotein VP7 KEYWORDS coat protein; glycoprotein; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-326 #product glycoprotein VP7 #status predicted #label !8GPV\ !$32-48 #region hydrophobic #status predicted\ !$69 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 326 #molecular-weight 37238 #checksum 2368 SEQUENCE /// ENTRY JN0307 #type complete TITLE glycoprotein VP7 precursor - human rotavirus A (serotype G strain RK9) ALTERNATE_NAMES VP7 antigen ORGANISM #formal_name human rotavirus A DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Feb-1997 ACCESSIONS JN0307 REFERENCE JN0307 !$#authors Bessarab, I.N.; Novikova, P.A.; Borodin, A.M. !$#journal Bioorg. Khim. (1990) 16:1689-1691 !$#title Utilization of polymerase chain reaction for rotavirus !1analysis; nucleotide sequence of gene coding basic and novel !1G-serum type of human rotavirus antigen VP7. !$#cross-references MUID:91214432; PMID:1965285 !$#accession JN0307 !'##molecule_type genomic RNA !'##residues 1-326 ##label BES CLASSIFICATION #superfamily rotavirus glycoprotein VP7 KEYWORDS coat protein; glycoprotein; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-326 #product glycoprotein VP7 #status predicted #label !8VP7\ !$69 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 326 #molecular-weight 37323 #checksum 6606 SEQUENCE /// ENTRY VGXRDB #type complete TITLE glycoprotein VP7 precursor - bovine rotavirus A (strain NCDV) ALTERNATE_NAMES outer shell glycoprotein ORGANISM #formal_name bovine rotavirus A #note host Bos sp. (cattle) DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 16-Jul-1999 ACCESSIONS A04136 REFERENCE A04136 !$#authors Glass, R.I.; Keith, J.; Nakagomi, O.; Nakagomi, T.; Askaa, !1J.; Kapikian, A.Z.; Chanock, R.M.; Flores, J. !$#journal Virology (1985) 141:292-298 !$#title Nucleotide sequence of the structural glycoprotein VP7 gene !1of Nebraska calf diarrhea virus rotavirus: comparison with !1homologous genes from four strains of human and animal !1rotaviruses. !$#cross-references MUID:86098646; PMID:2417410 !$#accession A04136 !'##molecule_type genomic RNA !'##residues 1-326 ##label GLA !'##cross-references GB:M12394; NID:g333835; PIDN:AAA47325.1; !1PID:g333836 GENETICS !$#map_position segment 8 CLASSIFICATION #superfamily rotavirus glycoprotein VP7 KEYWORDS coat protein; glycoprotein; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-326 #product glycoprotein VP7 #status predicted #label !8GPV\ !$32-48 #region hydrophobic #status predicted\ !$238,318 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 326 #molecular-weight 37086 #checksum 5160 SEQUENCE /// ENTRY VGXRCB #type complete TITLE glycoprotein VP7 precursor - bovine rotavirus A (strain UK) ALTERNATE_NAMES outer shell glycoprotein ORGANISM #formal_name bovine rotavirus A #note host Bos sp. (cattle) DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 16-Jul-1999 ACCESSIONS A04138 REFERENCE A04138 !$#authors Elleman, T.C.; Hoyne, P.A.; Dyall-Smith, M.L.; Holmes, I.H.; !1Azad, A.A. !$#journal Nucleic Acids Res. (1983) 11:4689-4701 !$#title Nucleotide sequence of the gene encoding the !1serotype-specific glycoprotein of UK bovine rotavirus. !$#cross-references MUID:83272924; PMID:6308556 !$#accession A04138 !'##molecule_type genomic RNA !'##residues 1-326 ##label ELL !'##cross-references GB:X00896; NID:g61686; PIDN:CAA25424.1; PID:g61687 GENETICS !$#map_position segment 8 CLASSIFICATION #superfamily rotavirus glycoprotein VP7 KEYWORDS coat protein; glycoprotein; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-326 #product glycoprotein VP7 #status predicted #label !8GPV\ !$32-48 #region hydrophobic #status predicted\ !$69,238,318 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 326 #molecular-weight 37119 #checksum 4911 SEQUENCE /// ENTRY VGXRB6 #type complete TITLE glycoprotein VP7 precursor - bovine rotavirus A (serotype 6 strain B641) ALTERNATE_NAMES outer shell glycoprotein ORGANISM #formal_name bovine rotavirus A DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS A40508 REFERENCE A40508 !$#authors Hardy, M.E.; Woode, G.N.; Xu, Z.; Gorziglia, M. !$#journal J. Virol. (1991) 65:5535-5538 !$#title Comparative amino acid sequence analysis of VP4 for VP7 !1serotype 6 bovine rotavirus strains NCDV, B641, and UK. !$#cross-references MUID:91374610; PMID:1654450 !$#accession A40508 !'##molecule_type genomic RNA !'##residues 1-326 ##label HAR !'##cross-references GB:M63266; NID:g333833; PIDN:AAA47324.1; !1PID:g333834 GENETICS !$#map_position segment 8 CLASSIFICATION #superfamily rotavirus glycoprotein VP7 KEYWORDS coat protein; glycoprotein; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-326 #product glycoprotein VP7 #status predicted #label !8GPV\ !$32-48 #region hydrophobic #status predicted\ !$20,69,238,318 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 326 #molecular-weight 37140 #checksum 4916 SEQUENCE /// ENTRY VGXRK4 #type complete TITLE glycoprotein VP7 precursor - bovine rotavirus A (strain KN-4) ALTERNATE_NAMES outer shell glycoprotein ORGANISM #formal_name bovine rotavirus A DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jun-2000 ACCESSIONS JS0720 REFERENCE JS0720 !$#authors Matsuda, Y.; Isegawa, Y.; Woode, G.N.; Zheng, S.; Kaga, E.; !1Nakagomi, T.; Ueda, S.; Nakagomi, O. !$#submission submitted to JIPID, July 1992 !$#accession JS0720 !'##molecule_type genomic RNA !'##residues 1-326 ##label MAT !'##cross-references DDBJ:D12710; NID:g222534; PIDN:BAA02206.1; !1PID:g222535 GENETICS !$#map_position segment 8 CLASSIFICATION #superfamily rotavirus glycoprotein VP7 KEYWORDS coat protein; glycoprotein; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-326 #product glycoprotein VP7 #status predicted #label !8GPV\ !$33-49 #region hydrophobic #status predicted\ !$69 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 326 #molecular-weight 37060 #checksum 3508 SEQUENCE /// ENTRY VGXR7H #type complete TITLE glycoprotein VP7 precursor - human rotavirus A (strain Wa) ORGANISM #formal_name human rotavirus A DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Feb-1997 ACCESSIONS A04137 REFERENCE A04137 !$#authors Richardson, M.A.; Iwamoto, A.; Ikegami, N.; Nomoto, A.; !1Furuichi, Y. !$#journal J. Virol. (1984) 51:860-862 !$#title Nucleotide sequence of the gene encoding the !1serotype-specific antigen of human (Wa) rotavirus: !1comparison with the homologous genes from simian SA11 and UK !1bovine rotaviruses. !$#cross-references MUID:84292467; PMID:6088808 !$#accession A04137 !'##molecule_type genomic RNA !'##residues 1-326 ##label RIC !'##cross-references GB:K02033 GENETICS !$#map_position segment 9 CLASSIFICATION #superfamily rotavirus glycoprotein VP7 KEYWORDS coat protein; glycoprotein; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-326 #product glycoprotein VP7 #status predicted #label !8GPV\ !$32-48 #region hydrophobic #status predicted\ !$69,238 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 326 #molecular-weight 37341 #checksum 3968 SEQUENCE /// ENTRY VGXRMD #type complete TITLE glycoprotein VP7 precursor - human rotavirus A (serotype 1 strains D and MO) ALTERNATE_NAMES outer capsid protein VP7 ORGANISM #formal_name human rotavirus A DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Feb-1997 ACCESSIONS A27620 REFERENCE A27620 !$#authors Green, K.Y.; Midthun, K.; Gorziglia, M.; Hoshino, Y.; !1Kapikian, A.Z.; Chanock, R.M.; Flores, J. !$#journal Virology (1987) 161:153-159 !$#title Comparison of the amino acid sequences of the major !1neutralization protein of four human rotavirus serotypes. !$#cross-references MUID:88044489; PMID:2823458 !$#accession A27620 !'##molecule_type genomic RNA !'##residues 1-326 ##label GRE GENETICS !$#map_position segment 9 CLASSIFICATION #superfamily rotavirus glycoprotein VP7 KEYWORDS coat protein; glycoprotein; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-326 #product glycoprotein VP7 #status predicted #label !8GPV\ !$32-48 #region hydrophobic #status predicted\ !$69,238 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 326 #molecular-weight 37314 #checksum 4013 SEQUENCE /// ENTRY VGXR37 #type complete TITLE glycoprotein VP7 precursor - human rotavirus A (serotype 1 strain M37) ALTERNATE_NAMES outer capsid protein VP7 ORGANISM #formal_name human rotavirus A DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Feb-1997 ACCESSIONS C27620 REFERENCE A27620 !$#authors Green, K.Y.; Midthun, K.; Gorziglia, M.; Hoshino, Y.; !1Kapikian, A.Z.; Chanock, R.M.; Flores, J. !$#journal Virology (1987) 161:153-159 !$#title Comparison of the amino acid sequences of the major !1neutralization protein of four human rotavirus serotypes. !$#cross-references MUID:88044489; PMID:2823458 !$#accession C27620 !'##molecule_type genomic RNA !'##residues 1-326 ##label GRE GENETICS !$#map_position segment 9 CLASSIFICATION #superfamily rotavirus glycoprotein VP7 KEYWORDS coat protein; glycoprotein; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-326 #product glycoprotein VP7 #status predicted #label !8GPV\ !$32-48 #region hydrophobic #status predicted\ !$69,238 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 326 #molecular-weight 37294 #checksum 4365 SEQUENCE /// ENTRY VGXRWA #type complete TITLE glycoprotein VP7 precursor - human rotavirus A (serotype 1 strain WA) ALTERNATE_NAMES outer capsid protein VP7 ORGANISM #formal_name human rotavirus A DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Feb-1997 ACCESSIONS D27620 REFERENCE A27620 !$#authors Green, K.Y.; Midthun, K.; Gorziglia, M.; Hoshino, Y.; !1Kapikian, A.Z.; Chanock, R.M.; Flores, J. !$#journal Virology (1987) 161:153-159 !$#title Comparison of the amino acid sequences of the major !1neutralization protein of four human rotavirus serotypes. !$#cross-references MUID:88044489; PMID:2823458 !$#accession D27620 !'##molecule_type genomic RNA !'##residues 1-326 ##label GRE GENETICS !$#map_position segment 9 CLASSIFICATION #superfamily rotavirus glycoprotein VP7 KEYWORDS coat protein; glycoprotein; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-326 #product glycoprotein VP7 #status predicted #label !8GPV\ !$32-48 #region hydrophobic #status predicted\ !$69,238 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 326 #molecular-weight 37324 #checksum 4014 SEQUENCE /// ENTRY VGXRH4 #type complete TITLE glycoprotein VP7 precursor - human rotavirus A (serotype 4) ALTERNATE_NAMES outer capsid protein VP7 ORGANISM #formal_name human rotavirus A DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Feb-1997 ACCESSIONS A41310 REFERENCE A41310 !$#authors Coulson, B.S.; Kirkwood, C. !$#journal J. Virol. (1991) 65:5968-5974 !$#title Relation of VP7 amino acid sequence to monoclonal antibody !1neutralization of rotavirus and rotavirus monotype. !$#cross-references MUID:92015491; PMID:1656083 !$#accession A41310 !'##molecule_type genomic RNA !'##residues 1-326 ##label COU !'##cross-references GB:M64666 GENETICS !$#map_position segment 9 CLASSIFICATION #superfamily rotavirus glycoprotein VP7 KEYWORDS coat protein; glycoprotein; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-326 #product glycoprotein VP7 #status predicted #label !8GVP\ !$32-48 #region hydrophobic #status predicted\ !$69,238 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 326 #molecular-weight 37291 #checksum 3238 SEQUENCE /// ENTRY VGXRP #type complete TITLE glycoprotein VP7 precursor - human rotavirus A (serotype 3 strain P) ALTERNATE_NAMES outer capsid protein VP7 ORGANISM #formal_name human rotavirus A DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Feb-1997 ACCESSIONS I27620 REFERENCE A27620 !$#authors Green, K.Y.; Midthun, K.; Gorziglia, M.; Hoshino, Y.; !1Kapikian, A.Z.; Chanock, R.M.; Flores, J. !$#journal Virology (1987) 161:153-159 !$#title Comparison of the amino acid sequences of the major !1neutralization protein of four human rotavirus serotypes. !$#cross-references MUID:88044489; PMID:2823458 !$#accession I27620 !'##molecule_type genomic RNA !'##residues 1-326 ##label GRE GENETICS !$#map_position segment 9 CLASSIFICATION #superfamily rotavirus glycoprotein VP7 KEYWORDS coat protein; glycoprotein; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-326 #product glycoprotein VP7 #status predicted #label !8GPV\ !$32-48 #region hydrophobic #status predicted\ !$69,238 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 326 #molecular-weight 37249 #checksum 3522 SEQUENCE /// ENTRY VGXRW8 #type complete TITLE glycoprotein VP7 precursor - porcine rotavirus A (serotype G3 strain CRW-8) ORGANISM #formal_name porcine rotavirus A DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 07-May-1999 ACCESSIONS A60075 REFERENCE A60075 !$#authors Huang, J.; Nagesha, H.S.; Dyall-Smith, M.L.; Holmes, I.H. !$#journal Arch. Virol. (1989) 109:173-183 !$#title Comparative sequence analysis of VP7 genes from five !1Australian porcine rotaviruses. !$#cross-references MUID:90120966; PMID:2558633 !$#accession A60075 !'##molecule_type DNA !'##residues 1-326 ##label HUA GENETICS !$#map_position segment 9 CLASSIFICATION #superfamily rotavirus glycoprotein VP7 KEYWORDS coat protein; glycoprotein; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-326 #product glycoprotein VP7 #status predicted #label !8VP7\ !$32-48 #region hydrophobic #status predicted\ !$69 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 326 #molecular-weight 37092 #checksum 1017 SEQUENCE /// ENTRY VGXRT6 #type complete TITLE glycoprotein VP7 precursor - porcine rotavirus A (serotype G3 strain AT/76) ORGANISM #formal_name porcine rotavirus A DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 07-May-1999 ACCESSIONS E60075 REFERENCE A60075 !$#authors Huang, J.; Nagesha, H.S.; Dyall-Smith, M.L.; Holmes, I.H. !$#journal Arch. Virol. (1989) 109:173-183 !$#title Comparative sequence analysis of VP7 genes from five !1Australian porcine rotaviruses. !$#cross-references MUID:90120966; PMID:2558633 !$#accession E60075 !'##molecule_type DNA !'##residues 1-326 ##label HUA GENETICS !$#map_position segment 9 CLASSIFICATION #superfamily rotavirus glycoprotein VP7 KEYWORDS coat protein; glycoprotein; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-326 #product glycoprotein VP7 #status predicted #label !8VP7\ !$32-48 #region hydrophobic #status predicted\ !$69 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 326 #molecular-weight 37246 #checksum 772 SEQUENCE /// ENTRY VGXRRR #type complete TITLE glycoprotein VP7 precursor - rhesus rotavirus (serotype 3, strain RRV) ALTERNATE_NAMES outer capsid protein VP7 ORGANISM #formal_name rhesus rotavirus DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Feb-1997 ACCESSIONS A27621 REFERENCE A27620 !$#authors Green, K.Y.; Midthun, K.; Gorziglia, M.; Hoshino, Y.; !1Kapikian, A.Z.; Chanock, R.M.; Flores, J. !$#journal Virology (1987) 161:153-159 !$#title Comparison of the amino acid sequences of the major !1neutralization protein of four human rotavirus serotypes. !$#cross-references MUID:88044489; PMID:2823458 !$#accession A27621 !'##molecule_type genomic RNA !'##residues 1-326 ##label GRE GENETICS !$#map_position segment 9 CLASSIFICATION #superfamily rotavirus glycoprotein VP7 KEYWORDS coat protein; glycoprotein; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-326 #product glycoprotein VP7 #status predicted #label !8GPV\ !$32-48 #region hydrophobic #status predicted\ !$69 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 326 #molecular-weight 37111 #checksum 960 SEQUENCE /// ENTRY VGXRER #type complete TITLE glycoprotein VP7 precursor - equine rotavirus A (strain L338) ORGANISM #formal_name equine rotavirus A DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jun-2000 ACCESSIONS A38708 REFERENCE A38708 !$#authors Browning, G.F.; Chalmers, R.M.; Fitzgerald, T.A.; Snodgrass, !1D.R. !$#journal J. Gen. Virol. (1991) 72:1059-1064 !$#title Serological and genomic characterization of L338, a novel !1equine group A rotavirus G serotype. !$#cross-references MUID:91237340; PMID:1851806 !$#accession A38708 !'##molecule_type genomic RNA !'##residues 1-326 ##label BRO !'##cross-references GB:D13549; GB:D00843; NID:g222519; PIDN:BAA02748.1; !1PID:g222520 GENETICS !$#map_position segment 9 CLASSIFICATION #superfamily rotavirus glycoprotein VP7 KEYWORDS coat protein; glycoprotein; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-326 #product glycoprotein VP7 #status predicted #label !8GPV\ !$32-48 #region hydrophobic #status predicted\ !$69,238 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 326 #molecular-weight 37409 #checksum 6217 SEQUENCE /// ENTRY VGXRAB #type complete TITLE glycoprotein VP7 precursor - bovine rotavirus A (strain 61A) ALTERNATE_NAMES outer capsid protein VP7 ORGANISM #formal_name bovine rotavirus A DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jul-1999 ACCESSIONS S10977 REFERENCE S10977 !$#authors Taniguchi, K.; Pongsuwanna, Y.; Choonthanom, M.; Urasawa, S. !$#journal Nucleic Acids Res. (1990) 18:4613 !$#title Nucleotide sequence of the VP7 gene of a bovine rotavirus !1(strain 61A) with different serotype specificity from !1serotype 6. !$#cross-references MUID:90356420; PMID:1697069 !$#accession S10977 !'##molecule_type genomic RNA !'##residues 1-326 ##label TAN !'##cross-references EMBL:X53403; NID:g61514; PIDN:CAA37478.1; !1PID:g61515 GENETICS !$#map_position segment 9 CLASSIFICATION #superfamily rotavirus glycoprotein VP7 KEYWORDS coat protein; glycoprotein; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-326 #product glycoprotein VP7 #status predicted #label !8GPV\ !$32-48 #region hydrophobic #status predicted\ !$69,145 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 326 #molecular-weight 37310 #checksum 4386 SEQUENCE /// ENTRY VGXRBB #type complete TITLE glycoprotein VP7 precursor - bovine rotavirus A (serotype 10 strain B223) ORGANISM #formal_name bovine rotavirus A DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jul-1999 ACCESSIONS A38510 REFERENCE A38510 !$#authors Xu, L.; Harbour, D.; McCrae, M.A. !$#journal J. Gen. Virol. (1991) 72:177-180 !$#title Sequence of the gene encoding the major neutralization !1antigen (VP7) of serotype 10 rotavirus. !$#cross-references MUID:91116309; PMID:1703560 !$#accession A38510 !'##molecule_type genomic RNA !'##residues 1-326 ##label XUL !'##cross-references EMBL:X52650; NID:g61512; PIDN:CAA36875.1; !1PID:g61513 GENETICS !$#map_position segment 9 CLASSIFICATION #superfamily rotavirus glycoprotein VP7 KEYWORDS coat protein; glycoprotein; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-326 #product glycoprotein VP7 #status predicted #label !8GPV\ !$32-48 #region hydrophobic #status predicted\ !$69,145 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 326 #molecular-weight 37310 #checksum 6510 SEQUENCE /// ENTRY JQ1442 #type complete TITLE glycoprotein VP7 precursor - bovine rotavirus A (serotype 10, strain A44) ALTERNATE_NAMES outer capsid protein VP7 ORGANISM #formal_name bovine rotavirus A DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jun-2000 ACCESSIONS JQ1442 REFERENCE JQ1442 !$#authors Taniguchi, K.; Urasawa, T.; Pongsuwanna, Y.; Choonthanom, !1M.; Jayavasu, C.; Urasawa, S. !$#journal J. Gen. Virol. (1991) 72:2929-2937 !$#title Molecular and antigenic analyses of serotypes 8 and 10 of !1bovine rotaviruses in Thailand. !$#cross-references MUID:92113534; PMID:1662688 !$#accession JQ1442 !'##molecule_type genomic RNA !'##residues 1-326 ##label TAN !'##cross-references GB:D01055; NID:g222525; PIDN:BAA00857.1; !1PID:g222526 !'##note translation of the nucleotide sequence is not complete GENETICS !$#map_position segment 9 CLASSIFICATION #superfamily rotavirus glycoprotein VP7 KEYWORDS capsid protein; coat protein; glycoprotein; transmembrane !1protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-326 #product glycoprotein VP7 #status predicted #label !8GPV\ !$37-55 #domain transmembrane #status predicted #label TMN\ !$69,145,270 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 326 #molecular-weight 37200 #checksum 3467 SEQUENCE /// ENTRY JQ1443 #type complete TITLE glycoprotein VP7 precursor - bovine rotavirus A (serotype 10, strain KK3) ALTERNATE_NAMES outer capsid protein VP7 ORGANISM #formal_name bovine rotavirus A DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jun-2000 ACCESSIONS JQ1443 REFERENCE JQ1442 !$#authors Taniguchi, K.; Urasawa, T.; Pongsuwanna, Y.; Choonthanom, !1M.; Jayavasu, C.; Urasawa, S. !$#journal J. Gen. Virol. (1991) 72:2929-2937 !$#title Molecular and antigenic analyses of serotypes 8 and 10 of !1bovine rotaviruses in Thailand. !$#cross-references MUID:92113534; PMID:1662688 !$#accession JQ1443 !'##molecule_type genomic RNA !'##residues 1-326 ##label TAN !'##cross-references GB:D01056; NID:g222531; PIDN:BAA00858.1; !1PID:g222532 !'##note translation of the nucleotide sequence is not complete GENETICS !$#map_position segment 9 CLASSIFICATION #superfamily rotavirus glycoprotein VP7 KEYWORDS capsid protein; coat protein; glycoprotein; transmembrane !1protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-326 #product glycoprotein VP7 #status predicted #label !8GPV\ !$37-55 #domain transmembrane #status predicted #label TMN\ !$69 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 326 #molecular-weight 37423 #checksum 6093 SEQUENCE /// ENTRY VGXR49 #type complete TITLE glycoprotein VP7 precursor - bovine rotavirus A (serotype 1 strain T449) ALTERNATE_NAMES outer capsid protein VP7 ORGANISM #formal_name bovine rotavirus A DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Feb-1997 ACCESSIONS A42989 REFERENCE A42989 !$#authors Blackhall, J.; Bellinzoni, R.; Mattion, N.; Estes, M.K.; La !1Torre, J.L.; Magnusson, G. !$#journal Virology (1992) 189:833-837 !$#title A bovine rotavirus serotype 1: serologic characterization of !1the virus and nucleotide sequence determination of the !1structural glycoprotein VP7 gene. !$#cross-references MUID:92351592; PMID:1322609 !$#accession A42989 !'##molecule_type genomic RNA !'##residues 1-326 ##label BLA !'##cross-references GB:M92651 GENETICS !$#map_position segment 8 CLASSIFICATION #superfamily rotavirus glycoprotein VP7 KEYWORDS coat protein; glycoprotein; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-326 #product glycoprotein VP7 #status predicted #label !8GVP\ !$32-48 #region hydrophobic #status predicted\ !$69,238 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 326 #molecular-weight 37346 #checksum 1891 SEQUENCE /// ENTRY A44891 #type complete TITLE glycoprotein VP7 precursor - equine rotavirus A (serotype G, isolate FI23) ALTERNATE_NAMES outer capsid protein VP7 ORGANISM #formal_name equine rotavirus A DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 22-May-1998 ACCESSIONS A44891 REFERENCE A44891 !$#authors Browning, G.F.; Fitzgerald, T.A.; Chalmers, R.M.; Snodgrass, !1D.R. !$#journal J. Clin. Microbiol. (1991) 29:2043-2046 !$#title A novel group A rotavirus G serotype: serological and !1genomic characterization of equine isolate FI23. !$#cross-references MUID:92129619; PMID:1663521 !$#accession A44891 !'##molecule_type DNA !'##residues 1-326 ##label BRO !'##note sequence extracted from NCBI backbone (NCBIN:78190, !1NCBIP:78192) CLASSIFICATION #superfamily rotavirus glycoprotein VP7 KEYWORDS coat protein; glycoprotein; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-326 #product glycoprotein VP7 #status predicted #label !8GPV\ !$32-48 #region hydrophobic #status predicted\ !$69 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 326 #molecular-weight 37234 #checksum 7854 SEQUENCE /// ENTRY VGXRC2 #type complete TITLE glycoprotein VP7 precursor - chicken rotavirus A (serotype 7, strain Ch2) ORGANISM #formal_name chicken rotavirus A DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jul-1999 ACCESSIONS A41703 REFERENCE A41703 !$#authors Nishikawa, K.; Hoshino, Y.; Gorziglia, M. !$#journal Virology (1991) 185:853-856 !$#title Sequence of the VP7 gene of chicken rotavirus Ch2 strain of !1serotype 7 rotavirus. !$#cross-references MUID:92074251; PMID:1660203 !$#accession A41703 !'##molecule_type genomic RNA !'##residues 1-329 ##label NIS !'##cross-references EMBL:X56784; NID:g58735; PIDN:CAA40104.1; !1PID:g58736 GENETICS !$#map_position segment 9 CLASSIFICATION #superfamily rotavirus glycoprotein VP7 KEYWORDS coat protein; glycoprotein; transmembrane protein FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-329 #product glycoprotein VP7 #status predicted #label !8GPV\ !$33-49 #region hydrophobic #status predicted\ !$72,193 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 329 #molecular-weight 37616 #checksum 4045 SEQUENCE /// ENTRY A48351 #type complete TITLE glycoprotein VP7 precursor - chicken rotavirus A (serotype 7, strain Ty-1) ORGANISM #formal_name chicken rotavirus A DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS A48351 REFERENCE A48351 !$#authors Kool, D.A.; Holmes, I.H. !$#journal Arch. Virol. (1993) 129:227-234 !$#title The avian rotavirus Ty-1 Vp7 nucleotide and deduced amino !1acid sequences differ significantly from those of Ch-2 !1rotavirus. !$#cross-references MUID:93228444; PMID:8385915 !$#accession A48351 !'##molecule_type genomic RNA !'##residues 1-329 ##label KOO !'##cross-references GB:S58166; NID:g299084; PIDN:AAB26094.1; !1PID:g299085 !'##note sequence extracted from NCBI backbone (NCBIN:129072, !1NCBIP:129073) GENETICS !$#map_position segment 9 CLASSIFICATION #superfamily rotavirus glycoprotein VP7 KEYWORDS coat protein; glycoprotein; transmembrane protein FEATURE !$1-27 #domain signal sequence #status predicted #label SIG\ !$28-329 #product glycoprotein VP7 #status predicted #label !8GPV\ !$35-51 #region hydrophobic\ !$72,150,241,321 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 329 #molecular-weight 37287 #checksum 1467 SEQUENCE /// ENTRY VGXRWL #type complete TITLE glycoprotein VP7 precursor - human rotavirus A (strain L26) ORGANISM #formal_name human rotavirus A DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Feb-1997 ACCESSIONS B36410 REFERENCE A36410 !$#authors Taniguchi, K.; Urasawa, T.; Kobayashi, N.; Gorziglia, M.; !1Urasawa, S. !$#journal J. Virol. (1990) 64:5640-5644 !$#title Nucleotide sequence of VP4 and VP7 genes of human !1rotaviruses with subgroup I specificity and long RNA !1pattern: implication for new G serotype specificity. !$#cross-references MUID:91012813; PMID:2170690 !$#accession B36410 !'##molecule_type genomic RNA !'##residues 1-326 ##label TAN !'##cross-references EMBL:M58292 !'##note the authors translated the codon ATC for residue 43 as Leu, ATG !1for residue 77 as Tyr, and ACT for residue 78 as Ala GENETICS !$#map_position segment 9 CLASSIFICATION #superfamily rotavirus glycoprotein VP7 KEYWORDS coat protein; glycoprotein; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-326 #product glycoprotein VP7 #status predicted #label !8MAT\ !$32-48 #region hydrophobic #status predicted\ !$69,238 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 326 #molecular-weight 37176 #checksum 4474 SEQUENCE /// ENTRY VGXRB7 #type complete TITLE glycoprotein VP7 precursor - human rotavirus A (serotype G strain B37) ORGANISM #formal_name human rotavirus A #note host Homo sapiens (man) DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 16-Jul-1999 ACCESSIONS A31469 REFERENCE A31469 !$#authors Hum, C.P.; Dyall-Smith, M.L.; Holmes, I.H. !$#journal Virology (1989) 170:55-61 !$#title The VP7 gene of a new G serotype of human rotavirus (B37) is !1similar to G3 proteins in the antigenic C region. !$#cross-references MUID:89243208; PMID:2541556 !$#accession A31469 !'##molecule_type genomic RNA !'##residues 1-326 ##label HUM !'##cross-references GB:J04334; NID:g333866; PIDN:AAA47344.1; !1PID:g333867 GENETICS !$#map_position segment 9 CLASSIFICATION #superfamily rotavirus glycoprotein VP7 KEYWORDS coat protein; glycoprotein; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-326 #product glycoprotein VP7 #status predicted #label !8GPV\ !$32-48 #region hydrophobic #status predicted\ !$69,238 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 326 #molecular-weight 37356 #checksum 3750 SEQUENCE /// ENTRY JQ1444 #type complete TITLE glycoprotein VP7 precursor - bovine rotavirus A (serotype 8, strain A5) ALTERNATE_NAMES outer capsid protein VP7 ORGANISM #formal_name bovine rotavirus A DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jun-2000 ACCESSIONS JQ1444 REFERENCE JQ1442 !$#authors Taniguchi, K.; Urasawa, T.; Pongsuwanna, Y.; Choonthanom, !1M.; Jayavasu, C.; Urasawa, S. !$#journal J. Gen. Virol. (1991) 72:2929-2937 !$#title Molecular and antigenic analyses of serotypes 8 and 10 of !1bovine rotaviruses in Thailand. !$#cross-references MUID:92113534; PMID:1662688 !$#accession JQ1444 !'##molecule_type genomic RNA !'##residues 1-326 ##label TAN !'##cross-references GB:D01054; NID:g222527; PIDN:BAA00856.1; !1PID:g222528 !'##note translation of the nucleotide sequence is not complete GENETICS !$#map_position segment 9 CLASSIFICATION #superfamily rotavirus glycoprotein VP7 KEYWORDS capsid protein; coat protein; glycoprotein; transmembrane !1protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-326 #product glycoprotein VP7 #status predicted #label !8GPV\ !$37-55 #domain transmembrane #status predicted #label TMN\ !$69,238 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 326 #molecular-weight 37164 #checksum 1427 SEQUENCE /// ENTRY VGXRDS #type complete TITLE glycoprotein VP7 precursor - human rotavirus A (serotype 2 strain DS1) ALTERNATE_NAMES outer capsid protein VP7 ORGANISM #formal_name human rotavirus A DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Feb-1997 ACCESSIONS E27620 REFERENCE A27620 !$#authors Green, K.Y.; Midthun, K.; Gorziglia, M.; Hoshino, Y.; !1Kapikian, A.Z.; Chanock, R.M.; Flores, J. !$#journal Virology (1987) 161:153-159 !$#title Comparison of the amino acid sequences of the major !1neutralization protein of four human rotavirus serotypes. !$#cross-references MUID:88044489; PMID:2823458 !$#accession E27620 !'##molecule_type genomic RNA !'##residues 1-326 ##label GRE GENETICS !$#map_position segment 9 CLASSIFICATION #superfamily rotavirus glycoprotein VP7 KEYWORDS coat protein; glycoprotein; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-326 #product glycoprotein VP7 #status predicted #label !8GPV\ !$32-48 #region hydrophobic #status predicted\ !$69,146,238 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 326 #molecular-weight 37216 #checksum 3035 SEQUENCE /// ENTRY VGXRHN #type complete TITLE glycoprotein VP7 precursor - human rotavirus A (serotype 2 strain HN126) ALTERNATE_NAMES outer capsid protein VP7 ORGANISM #formal_name human rotavirus A DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Feb-1997 ACCESSIONS F27620 REFERENCE A27620 !$#authors Green, K.Y.; Midthun, K.; Gorziglia, M.; Hoshino, Y.; !1Kapikian, A.Z.; Chanock, R.M.; Flores, J. !$#journal Virology (1987) 161:153-159 !$#title Comparison of the amino acid sequences of the major !1neutralization protein of four human rotavirus serotypes. !$#cross-references MUID:88044489; PMID:2823458 !$#accession F27620 !'##molecule_type genomic RNA !'##residues 1-326 ##label GRE GENETICS !$#map_position segment 9 CLASSIFICATION #superfamily rotavirus glycoprotein VP7 KEYWORDS coat protein; glycoprotein; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-326 #product glycoprotein VP7 #status predicted #label !8GPV\ !$32-48 #region hydrophobic #status predicted\ !$69,146,238 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 326 #molecular-weight 37246 #checksum 3605 SEQUENCE /// ENTRY VGXRHU #type complete TITLE glycoprotein VP7 precursor - human rotavirus A ALTERNATE_NAMES outer capsid protein VP7 ORGANISM #formal_name human rotavirus A DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jul-1999 ACCESSIONS G27620; A93520; A04134 REFERENCE A27620 !$#authors Green, K.Y.; Midthun, K.; Gorziglia, M.; Hoshino, Y.; !1Kapikian, A.Z.; Chanock, R.M.; Flores, J. !$#journal Virology (1987) 161:153-159 !$#title Comparison of the amino acid sequences of the major !1neutralization protein of four human rotavirus serotypes. !$#cross-references MUID:88044489; PMID:2823458 !$#accession G27620 !'##molecule_type genomic RNA !'##residues 1-326 ##label GRE !'##experimental_source serotype 2 strain HU5 REFERENCE A93520 !$#authors Dyall-Smith, M.L.; Holmes, I.H. !$#journal Nucleic Acids Res. (1984) 12:3973-3982 !$#title Sequence homology between human and animal rotavirus !1serotype-specific glycoproteins. !$#cross-references MUID:84221410; PMID:6328448 !$#accession A93520 !'##molecule_type DNA !'##residues 1-326 ##label DYA !'##cross-references GB:X00572; NID:g61680; PIDN:CAA25236.1; PID:g61681 !'##experimental_source serotype 2 strain Hu/Australia/5/7 GENETICS !$#map_position segment 9 CLASSIFICATION #superfamily rotavirus glycoprotein VP7 KEYWORDS coat protein; glycoprotein; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-326 #product glycoprotein VP7 #status predicted #label !8GPV\ !$32-48 #region hydrophobic #status predicted\ !$69,146,238 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 326 #molecular-weight 37202 #checksum 3059 SEQUENCE /// ENTRY VGXR2S #type complete TITLE glycoprotein VP7 precursor - human rotavirus A (serotype 2 strain S2) ALTERNATE_NAMES outer capsid protein VP7; outer shell glycoprotein ORGANISM #formal_name human rotavirus A DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Feb-1997 ACCESSIONS H27620; A04133 REFERENCE A27620 !$#authors Green, K.Y.; Midthun, K.; Gorziglia, M.; Hoshino, Y.; !1Kapikian, A.Z.; Chanock, R.M.; Flores, J. !$#journal Virology (1987) 161:153-159 !$#title Comparison of the amino acid sequences of the major !1neutralization protein of four human rotavirus serotypes. !$#cross-references MUID:88044489; PMID:2823458 !$#accession H27620 !'##molecule_type genomic RNA !'##residues 1-326 ##label GRE GENETICS !$#map_position segment 9 CLASSIFICATION #superfamily rotavirus glycoprotein VP7 KEYWORDS coat protein; glycoprotein; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-326 #product glycoprotein VP7 #status predicted #label !8GPV\ !$32-48 #region hydrophobic #status predicted\ !$69,146,238 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 326 #molecular-weight 37284 #checksum 4030 SEQUENCE /// ENTRY VGXR3S #type complete TITLE glycoprotein VP7 precursor - human rotavirus A (serotype 2) ALTERNATE_NAMES outer capsid protein VP7; outer shell glycoprotein ORGANISM #formal_name human rotavirus A DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS A04133 REFERENCE A04133 !$#authors Both, G.W. !$#submission submitted to GenBank, March 1985 !$#accession A04133 !'##molecule_type DNA !'##residues 1-326 ##label BOT !'##cross-references GB:M11164; NID:g333804; PIDN:AAA47312.1; !1PID:g333805 GENETICS !$#map_position segment 9 CLASSIFICATION #superfamily rotavirus glycoprotein VP7 KEYWORDS coat protein; glycoprotein; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-326 #product glycoprotein VP7 #status predicted #label !8GPV\ !$32-48 #region hydrophobic #status predicted\ !$69,146,238 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 326 #molecular-weight 37272 #checksum 4448 SEQUENCE /// ENTRY VGXRST #type complete TITLE glycoprotein VP7 precursor - human rotavirus A (serotype 4 strain ST3) ALTERNATE_NAMES outer capsid protein VP7 ORGANISM #formal_name human rotavirus A DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Feb-1997 ACCESSIONS C27621 REFERENCE A27620 !$#authors Green, K.Y.; Midthun, K.; Gorziglia, M.; Hoshino, Y.; !1Kapikian, A.Z.; Chanock, R.M.; Flores, J. !$#journal Virology (1987) 161:153-159 !$#title Comparison of the amino acid sequences of the major !1neutralization protein of four human rotavirus serotypes. !$#cross-references MUID:88044489; PMID:2823458 !$#accession C27621 !'##molecule_type genomic RNA !'##residues 1-326 ##label GRE GENETICS !$#map_position segment 9 CLASSIFICATION #superfamily rotavirus glycoprotein VP7 KEYWORDS coat protein; glycoprotein; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-326 #product glycoprotein VP7 #status predicted #label !8GPV\ !$32-48 #region hydrophobic #status predicted\ !$69,238 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 326 #molecular-weight 37068 #checksum 5193 SEQUENCE /// ENTRY VGXRTH #type complete TITLE glycoprotein VP7 precursor - human rotavirus A (serotype 4 strain St. Thomas 3) ALTERNATE_NAMES outer capsid protein VP7 ORGANISM #formal_name human rotavirus A DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS S02211 REFERENCE S02211 !$#authors Reddy, D.A.; Greenberg, H.B.; Bellamy, A.R. !$#journal Nucleic Acids Res. (1989) 17:449 !$#title Rotavirus serotype IV: nucleotide sequence of genomic !1segment nine of the St Thomas 3 strain. !$#cross-references MUID:89098407; PMID:2536151 !$#accession S02211 !'##molecule_type genomic RNA !'##residues 1-326 ##label RED !'##cross-references EMBL:X13603; NID:g61880; PIDN:CAA31938.1; !1PID:g61881 GENETICS !$#map_position segment 9 CLASSIFICATION #superfamily rotavirus glycoprotein VP7 KEYWORDS coat protein; glycoprotein; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-326 #product glycoprotein VP7 #status predicted #label !8GPV\ !$32-48 #region hydrophobic #status predicted\ !$69,238 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 326 #molecular-weight 37206 #checksum 5163 SEQUENCE /// ENTRY VGXR4G #type complete TITLE glycoprotein VP7 precursor - porcine rotavirus C (serotype 4, strain Gottfried) ORGANISM #formal_name porcine rotavirus C DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS S01748 REFERENCE S01748 !$#authors Gorziglia, M.; Nishikawa, K.; Green, K.; Taniguchi, K. !$#journal Nucleic Acids Res. (1988) 16:775 !$#title Gene sequence of the VP7 serotype specific glycoprotein of !1Gottfried porcine rotavirus. !$#cross-references MUID:88124278; PMID:2829137 !$#accession S01748 !'##status translation not shown !'##molecule_type genomic RNA !'##residues 1-326 ##label GOR !'##cross-references EMBL:X06759; NID:g61859; PIDN:CAA29933.1; !1PID:g61860 GENETICS !$#map_position segment 9 CLASSIFICATION #superfamily rotavirus glycoprotein VP7 KEYWORDS coat protein; glycoprotein; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-326 #product glycoprotein VP7 #status predicted #label !8GPV\ !$32-48 #region hydrophobic #status predicted\ !$69 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 326 #molecular-weight 37076 #checksum 5136 SEQUENCE /// ENTRY VGXRN1 #type complete TITLE glycoprotein VP7 precursor - porcine rotavirus A (serotype G4 strain BEN-144) ORGANISM #formal_name porcine rotavirus A DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 07-May-1999 ACCESSIONS B60075 REFERENCE A60075 !$#authors Huang, J.; Nagesha, H.S.; Dyall-Smith, M.L.; Holmes, I.H. !$#journal Arch. Virol. (1989) 109:173-183 !$#title Comparative sequence analysis of VP7 genes from five !1Australian porcine rotaviruses. !$#cross-references MUID:90120966; PMID:2558633 !$#accession B60075 !'##molecule_type DNA !'##residues 1-326 ##label HUA GENETICS !$#map_position segment 9 CLASSIFICATION #superfamily rotavirus glycoprotein VP7 KEYWORDS coat protein; glycoprotein; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-326 #product glycoprotein VP7 #status predicted #label !8GPV\ !$32-48 #region hydrophobic #status predicted\ !$69 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 326 #molecular-weight 37295 #checksum 5838 SEQUENCE /// ENTRY VGXRM1 #type complete TITLE glycoprotein VP7 precursor - porcine rotavirus A (serotype G4 strain BMI-1) ORGANISM #formal_name porcine rotavirus A DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 07-May-1999 ACCESSIONS C60075 REFERENCE A60075 !$#authors Huang, J.; Nagesha, H.S.; Dyall-Smith, M.L.; Holmes, I.H. !$#journal Arch. Virol. (1989) 109:173-183 !$#title Comparative sequence analysis of VP7 genes from five !1Australian porcine rotaviruses. !$#cross-references MUID:90120966; PMID:2558633 !$#accession C60075 !'##molecule_type DNA !'##residues 1-326 ##label HUA GENETICS !$#map_position segment 9 CLASSIFICATION #superfamily rotavirus glycoprotein VP7 KEYWORDS coat protein; glycoprotein; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-326 #product glycoprotein VP7 #status predicted #label !8VP7\ !$29-45 #region hydrophobic #status predicted\ !$69 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 326 #molecular-weight 37191 #checksum 4563 SEQUENCE /// ENTRY A48554 #type complete TITLE glycoprotein VP7 precursor - porcine rotavirus A (strain K) ALTERNATE_NAMES outer capsid protein VP7 ORGANISM #formal_name porcine rotavirus A DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 01-Dec-2000 ACCESSIONS A48554; S14839; S36948 REFERENCE A48554 !$#authors Akopian, T.A.; Lunin, V.G.; Kruglyak, V.A.; Ruchadze, G.G.; !1Bakhutashvili, V.I.; Naroditsky, B.S.; Tichonenko, T.I. !$#journal Virus Genes (1992) 6:393-396 !$#title Nucleotide sequence of the cDNA for porcine rotavirus VP7 !1gene (strain K). !$#cross-references MUID:93118248; PMID:1335631 !$#accession A48554 !'##molecule_type genomic RNA !'##residues 1-326 ##label AKO !'##cross-references EMBL:X58439; NID:g61356; PIDN:CAA41345.1; !1PID:g61357 !'##note submitted to the EMBL Data Library, March 1991 !'##note sequence extracted from NCBI backbone (NCBIN:121643, !1NCBIP:121644) GENETICS !$#map_position segment 9 CLASSIFICATION #superfamily rotavirus glycoprotein VP7 KEYWORDS coat protein; glycoprotein; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-326 #product glycoprotein VP7 #status predicted #label !8GPV\ !$32-47 #region hydrophobic\ !$69,211 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 326 #molecular-weight 37191 #checksum 5195 SEQUENCE /// ENTRY VGXRVA #type complete TITLE glycoprotein VP7 precursor - human rotavirus A (serotype 4 strain VA70) ALTERNATE_NAMES outer capsid protein VP7 ORGANISM #formal_name human rotavirus A DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Feb-1997 ACCESSIONS D27621 REFERENCE A27620 !$#authors Green, K.Y.; Midthun, K.; Gorziglia, M.; Hoshino, Y.; !1Kapikian, A.Z.; Chanock, R.M.; Flores, J. !$#journal Virology (1987) 161:153-159 !$#title Comparison of the amino acid sequences of the major !1neutralization protein of four human rotavirus serotypes. !$#cross-references MUID:88044489; PMID:2823458 !$#accession D27621 !'##molecule_type genomic RNA !'##residues 1-326 ##label GRE GENETICS !$#map_position segment 9 CLASSIFICATION #superfamily rotavirus glycoprotein VP7 KEYWORDS coat protein; glycoprotein; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-326 #product glycoprotein VP7 #status predicted #label !8GPV\ !$32-48 #region hydrophobic #status predicted\ !$69 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 326 #molecular-weight 37079 #checksum 3216 SEQUENCE /// ENTRY VGXRCN #type complete TITLE glycoprotein VP7 precursor - porcine rotavirus C (strain Cowden) ORGANISM #formal_name porcine rotavirus C DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS A39988 REFERENCE A39988 !$#authors Qian, Y.; Jiang, B.; Saif, L.J.; Kang, S.Y.; Ishimaru, Y.; !1Yamashita, Y.; Oseto, M.; Green, K.Y. !$#journal Virology (1991) 182:562-569 !$#title Sequence conservation of gene 8 between human and porcine !1group C rotaviruses and its relationship to the VP7 gene of !1group A rotaviruses. !$#cross-references MUID:91220706; PMID:1850919 !$#accession A39988 !'##molecule_type genomic RNA !'##residues 1-332 ##label QIA !'##cross-references GB:M61100; GB:M61101; NID:g294325; PIDN:AAA47351.1; !1PID:g294326 GENETICS !$#map_position segment 9 CLASSIFICATION #superfamily rotavirus glycoprotein VP7 KEYWORDS coat protein; glycoprotein; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-332 #product glycoprotein VP7 #status predicted #label !8GPV\ !$28-44 #region hydrophobic #status predicted\ !$67,225 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 332 #molecular-weight 37347 #checksum 8326 SEQUENCE /// ENTRY VGXR88 #type complete TITLE glycoprotein VP7 precursor - human rotavirus C (strain 88-220) ORGANISM #formal_name human rotavirus C DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jul-1999 ACCESSIONS B39988 REFERENCE A39988 !$#authors Qian, Y.; Jiang, B.; Saif, L.J.; Kang, S.Y.; Ishimaru, Y.; !1Yamashita, Y.; Oseto, M.; Green, K.Y. !$#journal Virology (1991) 182:562-569 !$#title Sequence conservation of gene 8 between human and porcine !1group C rotaviruses and its relationship to the VP7 gene of !1group A rotaviruses. !$#cross-references MUID:91220706; PMID:1850919 !$#accession B39988 !'##molecule_type genomic RNA !'##residues 1-332 ##label QIA !'##cross-references GB:M61100; NID:g294733; PIDN:AAA47352.1; !1PID:g294734; GB:M61101 GENETICS !$#map_position segment 9 CLASSIFICATION #superfamily rotavirus glycoprotein VP7 KEYWORDS coat protein; glycoprotein; transmembrane protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-332 #product glycoprotein VP7 #status predicted #label !8GPV\ !$28-44 #region hydrophobic #status predicted\ !$67,152,225 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 332 #molecular-weight 37499 #checksum 359 SEQUENCE /// ENTRY VGXRHB #type complete TITLE glycoprotein VP7 precursor - human rotavirus B ORGANISM #formal_name human rotavirus B DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jul-1999 ACCESSIONS A37080 REFERENCE A37080 !$#authors Chen, G.M.; Hung, T.; Mackow, E.R. !$#journal Virology (1990) 178:311-315 !$#title Identification of the gene encoding the group B rotavirus !1VP7 equivalent: primary characterization of the ADRV segment !19 RNA. !$#cross-references MUID:90357782; PMID:2167559 !$#accession A37080 !'##molecule_type genomic RNA !'##residues 1-249 ##label CHE !'##cross-references EMBL:M33872; NID:g210569; PIDN:AAA42675.1; !1PID:g210570 !'##note the authors translated the codon GAT for residue 88 as Val and !1GTA for residue 89 as Asp GENETICS !$#map_position segment 9 CLASSIFICATION #superfamily rotavirus B glycoprotein VP7 KEYWORDS capsid protein; glycoprotein FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-249 #product glycoprotein VP7 #status predicted #label !8VP7\ !$45,91,105 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 249 #molecular-weight 28459 #checksum 6071 SEQUENCE /// ENTRY VGXRNH #type complete TITLE glycoprotein NCVP5 - human rotavirus A ORGANISM #formal_name human rotavirus A DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS A04139 REFERENCE A04139 !$#authors Okada, Y.; Richardson, M.A.; Ikegami, N.; Nomoto, A.; !1Furuichi, Y. !$#journal J. Virol. (1984) 51:856-859 !$#title Nucleotide sequence of human rotavirus genome segment 10, an !1RNA encoding a glycosylated virus protein. !$#cross-references MUID:84292466; PMID:6088807 !$#accession A04139 !'##molecule_type genomic RNA !'##residues 1-175 ##label OKA !'##cross-references GB:K02032; NID:g333797; PIDN:AAA47309.1; !1PID:g333798 !'##experimental_source strain Wa COMMENT The genome consists of 11 segments of double-stranded RNA. GENETICS !$#map_position segment 10 CLASSIFICATION #superfamily rotavirus glycoprotein NCVP5 KEYWORDS glycoprotein; transmembrane protein FEATURE !$8,18 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 175 #molecular-weight 20236 #checksum 624 SEQUENCE /// ENTRY VGXRA2 #type complete TITLE glycoprotein NCVP5 - human rotavirus A (strain A28) ORGANISM #formal_name human rotavirus A #note host Homo sapiens (man) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jun-2000 ACCESSIONS JQ1449 REFERENCE JQ1449 !$#authors Ballard, A.; McCrae, M.A.; Desselberger, U. !$#journal J. Gen. Virol. (1992) 73:633-638 !$#title Nucleotide sequences of normal and rearranged RNA segments !110 of human rotaviruses. !$#cross-references MUID:92185474; PMID:1312123 !$#accession JQ1449 !'##molecule_type genomic RNA !'##residues 1-175 ##label BAL !'##cross-references GB:D10771; DDBJ:D01145; NID:g222538; !1PIDN:BAA01602.1; PID:g222539 GENETICS !$#map_position segment 10 CLASSIFICATION #superfamily rotavirus glycoprotein NCVP5 KEYWORDS glycoprotein; transmembrane protein FEATURE !$8,18 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 175 #molecular-weight 20354 #checksum 859 SEQUENCE /// ENTRY VGXR66 #type complete TITLE glycoprotein NCVP5 (clone 6) - human rotavirus A (strain A64) ORGANISM #formal_name human rotavirus A #note host Homo sapiens (man) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Feb-1997 ACCESSIONS JQ1450 REFERENCE JQ1449 !$#authors Ballard, A.; McCrae, M.A.; Desselberger, U. !$#journal J. Gen. Virol. (1992) 73:633-638 !$#title Nucleotide sequences of normal and rearranged RNA segments !110 of human rotaviruses. !$#cross-references MUID:92185474; PMID:1312123 !$#accession JQ1450 !'##status translation not shown !'##molecule_type genomic RNA !'##residues 1-175 ##label BAL !'##cross-references DDBJ:D01146 GENETICS !$#map_position segment 10 CLASSIFICATION #superfamily rotavirus glycoprotein NCVP5 KEYWORDS glycoprotein; transmembrane protein FEATURE !$8,18 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 175 #molecular-weight 20320 #checksum 505 SEQUENCE /// ENTRY VGXR62 #type complete TITLE glycoprotein NCVP5 (clone 2) - human rotavirus A (strain A64) ORGANISM #formal_name human rotavirus A #note host Homo sapiens (man) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Feb-1997 ACCESSIONS JS0679 REFERENCE JQ1449 !$#authors Ballard, A.; McCrae, M.A.; Desselberger, U. !$#journal J. Gen. Virol. (1992) 73:633-638 !$#title Nucleotide sequences of normal and rearranged RNA segments !110 of human rotaviruses. !$#cross-references MUID:92185474; PMID:1312123 !$#accession JS0679 !'##molecule_type genomic RNA !'##residues 1-175 ##label BAL !'##cross-references DDBJ:D01145 !'##note only the residues that differ from human rotavirus (strain 64, !1clone 6) are shown GENETICS !$#map_position segment 10 CLASSIFICATION #superfamily rotavirus glycoprotein NCVP5 KEYWORDS glycoprotein; transmembrane protein FEATURE !$8,18 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 175 #molecular-weight 20360 #checksum 244 SEQUENCE /// ENTRY VGXRTS #type complete TITLE glycoprotein NCVP5 - simian rotavirus SA11 ORGANISM #formal_name simian rotavirus SA11 #note host (monkey) DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 16-Jul-1999 ACCESSIONS A04140 REFERENCE A04140 !$#authors Both, G.W.; Siegman, L.J.; Bellamy, A.R.; Atkinson, P.H. !$#journal J. Virol. (1983) 48:335-339 !$#title Coding assignment and nucleotide sequence of simian !1rotavirus SA11 gene segment 10: location of glycosylation !1sites suggests that the signal peptide is not cleaved. !$#cross-references MUID:84011028; PMID:6312090 !$#accession A04140 !'##molecule_type genomic RNA !'##residues 1-175 ##label BOT !'##cross-references GB:K01138; NID:g333782; PIDN:AAA47291.1; !1PID:g333783 GENETICS !$#map_position segment 10 CLASSIFICATION #superfamily rotavirus glycoprotein NCVP5 KEYWORDS glycoprotein; transmembrane protein FEATURE !$8,18 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 175 #molecular-weight 20309 #checksum 1166 SEQUENCE /// ENTRY VGXRBR #type complete TITLE glycoprotein NCVP5 - bovine rotavirus A (strain UK) ALTERNATE_NAMES glycoprotein VP10; glycoprotein VP10c; protein VP12 ORGANISM #formal_name bovine rotavirus A DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 16-Jul-1999 ACCESSIONS A04141; S07415 REFERENCE A94337 !$#authors Ward, C.W.; Azad, A.A.; Dyall-Smith, M.L. !$#journal Virology (1985) 144:328-336 !$#title Structural homologies between RNA gene segments 10 and 11 !1from UK simian SA11, and human Wa rotaviruses. !$#cross-references MUID:86045957; PMID:2998051 !$#accession A04141 !'##molecule_type genomic RNA !'##residues 1-175 ##label WAR !'##cross-references EMBL:K03384; NID:g333776; PIDN:AAA47288.1; !1PID:g333777 REFERENCE S07415 !$#authors Baybutt, H.N.; McCrae, M.A. !$#journal Virus Res. (1984) 1:533-541 !$#title The molecular biology of rotaviruses VII. Detailed !1structural analysis of gene 10 of bovine rotavirus. !$#cross-references MUID:85194810; PMID:6099939 !$#accession S07415 !'##molecule_type genomic RNA !'##residues 1-18,'S',20-36,'V',38-130,'H',132-135,'I',137,'TVD', !1141-160,'N',162,'R',164-175 ##label BAY !'##cross-references EMBL:M21885; NID:g333806; PIDN:AAA47313.1; !1PID:g333807 GENETICS !$#map_position segment 10 CLASSIFICATION #superfamily rotavirus glycoprotein NCVP5 KEYWORDS glycoprotein; transmembrane protein FEATURE !$8,18 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 175 #molecular-weight 20378 #checksum 1206 SEQUENCE /// ENTRY VGXRP5 #type complete TITLE glycoprotein NCVP5 - Nebraska calf diarrhea virus ORGANISM #formal_name Nebraska calf diarrhea virus #note host Bos sp. (cattle) DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS S01888 REFERENCE S01888 !$#authors Powell, K.F.H.; Gunn, P.R.; Bellamy, A.R. !$#journal Nucleic Acids Res. (1988) 16:763 !$#title Nucleotide sequence of bovine rotavirus genomic segment 10: !1an RNA encoding the viral non-structural glycoprotein. !$#cross-references MUID:88124266; PMID:2829135 !$#accession S01888 !'##molecule_type DNA !'##residues 1-175 ##label POW !'##cross-references EMBL:X06806; NID:g61852; PIDN:CAA29959.1; !1PID:g61853 GENETICS !$#map_position segment 10 CLASSIFICATION #superfamily rotavirus glycoprotein NCVP5 KEYWORDS glycoprotein; transmembrane protein FEATURE !$8,18 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 175 #molecular-weight 20380 #checksum 108 SEQUENCE /// ENTRY MNXR3D #type complete TITLE nonstructural protein uNS - reovirus type 3 (strain Dearing) ORGANISM #formal_name reovirus type 3 DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jul-1999 ACCESSIONS B30179 REFERENCE A30179 !$#authors Wiener, J.R.; Bartlett, J.A.; Joklik, W.K. !$#journal Virology (1989) 169:293-304 !$#title The sequences of reovirus serotype 3 genome segments M1 and !1M3 encoding the minor protein mu-2 and the major !1nonstructural protein mu-NS, respectively. !$#cross-references MUID:89204900; PMID:2523177 !$#accession B30179 !'##molecule_type genomic RNA !'##residues 1-719 ##label WIE !'##cross-references GB:M27262; NID:g333689; PIDN:AAA47260.1; !1PID:g333690 CLASSIFICATION #superfamily reovirus nonstructural protein uNS KEYWORDS nonstructural protein SUMMARY #length 719 #molecular-weight 79959 #checksum 8551 SEQUENCE /// ENTRY MNXR4S #type complete TITLE nonstructural protein NCVP4 - simian rotavirus SA11 ORGANISM #formal_name simian rotavirus SA11 DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS A04142 REFERENCE A04142 !$#authors Both, G.W.; Bellamy, A.R.; Siegman, L.J. !$#journal Nucleic Acids Res. (1984) 12:1621-1626 !$#title Nucleotide sequence of the dsRNA genomic segment 7 of simian !111 rotavirus. !$#cross-references MUID:84144056; PMID:6322111 !$#accession A04142 !'##molecule_type genomic RNA !'##residues 1-315 ##label BOT !'##cross-references GB:X00355; NID:g61863; PIDN:CAA25102.1; PID:g61864 COMMENT The genome consists of 11 segments of double-stranded RNA. GENETICS !$#map_position segment 7 CLASSIFICATION #superfamily rotavirus nonstructural protein KEYWORDS nonstructural protein SUMMARY #length 315 #molecular-weight 36444 #checksum 2842 SEQUENCE /// ENTRY MNXRBR #type complete TITLE nonstructural protein NS2/VP9 - bovine rotavirus A (strain UK) ORGANISM #formal_name bovine rotavirus A #note host Bos sp. (cattle) DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 21-Nov-1997 ACCESSIONS A04143 REFERENCE A04143 !$#authors Ward, C.W.; Elleman, T.C.; Azad, A.A.; Dyall-Smith, M.L. !$#journal Virology (1984) 134:249-253 !$#title Nucleotide sequence of gene segment 9 encoding a !1nonstructural protein of UK bovine rotavirus. !$#cross-references MUID:84174093; PMID:6324473 !$#accession A04143 !'##molecule_type genomic RNA !'##residues 1-313 ##label WAR !'##cross-references GB:K02170; NID:g333817 GENETICS !$#map_position segment 9 CLASSIFICATION #superfamily rotavirus nonstructural protein KEYWORDS nonstructural protein SUMMARY #length 313 #molecular-weight 36153 #checksum 5484 SEQUENCE /// ENTRY MNXRPC #type complete TITLE nonstructural protein NS34 - porcine rotavirus C (strain Cowden) ORGANISM #formal_name porcine rotavirus C DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS A41040 REFERENCE A41040 !$#authors Qian, Y.; Jiang, B.; Saif, L.J.; Kang, S.Y.; Ojeh, C.K.; !1Green, K.Y. !$#journal Virology (1991) 184:752-757 !$#title Molecular analysis of the gene 6 from a porcine group C !1rotavirus that encodes the NS34 equivalent of group A !1rotaviruses. !$#cross-references MUID:91361567; PMID:1653496 !$#accession A41040 !'##molecule_type genomic RNA !'##residues 1-402 ##label QIA !'##cross-references GB:M69115; NID:g333307; PIDN:AAA47087.1; !1PID:g333308 GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily rotavirus nonstructural protein KEYWORDS nonstructural protein SUMMARY #length 402 #molecular-weight 45125 #checksum 2457 SEQUENCE /// ENTRY MNXRBF #type complete TITLE nonstructural protein NCVP2 - bovine rotavirus A (strain RF) ORGANISM #formal_name bovine rotavirus A DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jul-1999 ACCESSIONS A27030 REFERENCE A27030 !$#authors Bremont, M.; Charpilienne, A.; Chabanne, D.; Cohen, J. !$#journal Virology (1987) 161:138-144 !$#title Nucleotide sequence and expression in Escherichia coli of !1the gene encoding the nonstructural protein NCVP2 of bovine !1rotavirus. !$#cross-references MUID:88044487; PMID:2823457 !$#accession A27030 !'##molecule_type genomic RNA !'##residues 1-491 ##label BRE !'##cross-references GB:M22308; NID:g333815; PIDN:AAA47316.1; !1PID:g333816 GENETICS !$#map_position segment 5 CLASSIFICATION #superfamily bovine rotavirus nonstructural protein NCVP2 KEYWORDS glycoprotein; nonstructural protein; zinc finger FEATURE !$50,168,277,404,438 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 491 #molecular-weight 58729 #checksum 4955 SEQUENCE /// ENTRY MNXRSA #type complete TITLE nonstructural protein NCVP2 - simian rotavirus SA11 ALTERNATE_NAMES nonstructural protein NS53 ORGANISM #formal_name simian rotavirus SA11 DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS S08215 REFERENCE S08215 !$#authors Mitchell, D.B.; Both, G.W. !$#journal Virology (1990) 174:618-621 !$#title Conservation of a potential metal binding motif despite !1extensive sequence diversity in the rotavirus nonstructural !1protein NS53. !$#cross-references MUID:90163231; PMID:2154894 !$#accession S08215 !'##molecule_type genomic RNA !'##residues 1-495 ##label MIT !'##cross-references EMBL:X14914; NID:g61889; PIDN:CAA33039.1; !1PID:g61890 GENETICS !$#map_position segment 5 CLASSIFICATION #superfamily bovine rotavirus nonstructural protein NCVP2 KEYWORDS nonstructural protein; zinc finger SUMMARY #length 495 #molecular-weight 58483 #checksum 1476 SEQUENCE /// ENTRY MNXRAD #type complete TITLE nonstructural protein - human rotavirus A (strain ADRV) ORGANISM #formal_name human rotavirus A #note host Homo sapiens (man) DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS A34750 REFERENCE A34750 !$#authors Chen, G.M.; Hung, T.; Mackow, E.R. !$#journal Virology (1990) 175:605-609 !$#title cDNA cloning of each genomic segment of the group B !1rotavirus ADRV: molecular characterization of the 11th RNA !1segment. !$#cross-references MUID:90224011; PMID:2158190 !$#accession A34750 !'##molecule_type genomic RNA !'##residues 1-170 ##label CHE !'##cross-references GB:M34380; GB:M33873; NID:g210567; PIDN:AAA42674.1; !1PID:g210568 CLASSIFICATION #superfamily group B rotavirus nonstructural protein KEYWORDS nonstructural protein SUMMARY #length 170 #molecular-weight 19938 #checksum 6453 SEQUENCE /// ENTRY A48357 #type complete TITLE nonstructural protein NS53 - porcine rotavirus C (strain Cowden) ORGANISM #formal_name porcine rotavirus C DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jul-1999 ACCESSIONS A48357; S16051 REFERENCE A48357 !$#authors Bremont, M.; Chabanne-Vautherot, D.; Cohen, J. !$#journal Arch. Virol. (1993) 130:85-92 !$#title Sequence analysis of three non structural proteins of a !1porcine group C (Cowden strain) rotavirus. !$#cross-references MUID:93277387; PMID:8389118 !$#accession A48357 !'##molecule_type genomic RNA !'##residues 1-393 ##label BRE !'##cross-references GB:X60546; NID:g61348; PIDN:CAA43036.1; PID:g61349 !'##experimental_source strain Cowden !'##note sequence extracted from NCBI backbone (NCBIN:132688, !1NCBIP:132689) REFERENCE S16051 !$#authors Bremont, M.; Brottier, P.; Chabanne-Vautherot, D.; Cohen, J. !$#submission submitted to the EMBL Data Library, July 1991 !$#description "Zinc finger" motif conservation in a group C Rotavirus !1genome. !$#accession S16051 !'##status preliminary !'##molecule_type mRNA !'##residues 1-393 ##label BRM !'##cross-references EMBL:X60546; NID:g61348; PIDN:CAA43036.1; !1PID:g61349 GENETICS !$#map_position segment 7 CLASSIFICATION #superfamily porcine rotavirus C nonstructural protein NS53 KEYWORDS glycoprotein; nonstructural protein; zinc finger FEATURE !$39-68 #region zinc finger\ !$290 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 393 #molecular-weight 46438 #checksum 4724 SEQUENCE /// ENTRY WMXR3S #type complete TITLE 34K protein - simian rotavirus SA11 ORGANISM #formal_name simian rotavirus SA11 DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 16-Jul-1999 ACCESSIONS A04144 REFERENCE A04144 !$#authors Both, G.W.; Bellamy, A.R.; Street, J.E.; Siegman, L.J. !$#journal Nucleic Acids Res. (1982) 10:7075-7088 !$#title A general strategy for cloning double-stranded RNA: !1nucleotide sequence of the simian-11 rotavirus gene 8. !$#cross-references MUID:83116940; PMID:6296764 !$#accession A04144 !'##molecule_type genomic RNA !'##residues 1-317 ##label BOT !'##cross-references GB:J02353; NID:g333786; PIDN:AAA47293.1; !1PID:g333787 COMMENT The genome consists of 11 segments of double-stranded RNA. GENETICS !$#map_position segment 8 CLASSIFICATION #superfamily rotavirus 34K protein SUMMARY #length 317 #molecular-weight 36628 #checksum 2005 SEQUENCE /// ENTRY WMXR3B #type complete TITLE 33K protein - bovine rotavirus A ORGANISM #formal_name bovine rotavirus A DATE 25-Feb-1985 #sequence_revision 25-Feb-1985 #text_change 31-Dec-1993 ACCESSIONS A04145 REFERENCE A04145 !$#authors Dyall-Smith, M.L.; Elleman, T.C.; Hoyne, P.A.; Holmes, I.H.; !1Azad, A.A. !$#journal Nucleic Acids Res. (1983) 11:3351-3362 !$#title Cloning and sequence of UK bovine rotavirus gene segment 7: !1marked sequence homology with simian rotavirus gene segment !18. !$#cross-references MUID:83220747; PMID:6304629 !$#accession A04145 !'##molecule_type genomic RNA !'##residues 1-317 ##label DYA COMMENT The genome consists of 11 segments of double-stranded RNA. GENETICS !$#map_position segment 7 CLASSIFICATION #superfamily rotavirus 34K protein SUMMARY #length 317 #molecular-weight 36691 #checksum 3706 SEQUENCE /// ENTRY WMXR5U #type complete TITLE 34K protein - porcine rotavirus C (serotype 5, strain OSU) ORGANISM #formal_name porcine rotavirus C DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS S01747 REFERENCE S01747 !$#authors Rushlow, K.; McNab, A.; Olson, K.; Maxwell, F.; Maxwell, I.; !1Stiegler, G. !$#journal Nucleic Acids Res. (1988) 16:367-368 !$#title Nucleotide sequence of porcine rotavirus (OSU strain) gene !1segments 7, 8, and 9. !$#cross-references MUID:88124224; PMID:2829124 !$#accession S01747 !'##status translation not shown !'##molecule_type genomic RNA !'##residues 1-317 ##label RUS !'##cross-references EMBL:X06722; NID:g61861; PIDN:CAA29902.1; !1PID:g61862 COMMENT The segment number may be 7, 8, or 9. CLASSIFICATION #superfamily rotavirus 34K protein SUMMARY #length 317 #molecular-weight 36456 #checksum 3989 SEQUENCE /// ENTRY VHXRBR #type complete TITLE minor outer capsid protein - bovine rotavirus A (strain UK) ORGANISM #formal_name bovine rotavirus A #note host Bos sp. (cattle) DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 16-Jul-1999 ACCESSIONS A04146 REFERENCE A94337 !$#authors Ward, C.W.; Azad, A.A.; Dyall-Smith, M.L. !$#journal Virology (1985) 144:328-336 !$#title Structural homologies between RNA gene segments 10 and 11 !1from UK simian SA11, and human Wa rotaviruses. !$#cross-references MUID:86045957; PMID:2998051 !$#accession A04146 !'##molecule_type genomic RNA !'##residues 1-198 ##label WAR !'##cross-references GB:K03385; NID:g333778; PIDN:AAA47289.1; !1PID:g333779 GENETICS !$#map_position segment 11 CLASSIFICATION #superfamily rotavirus minor outer capsid protein KEYWORDS capsid protein; coat protein; glycoprotein FEATURE !$20 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 198 #molecular-weight 21705 #checksum 131 SEQUENCE /// ENTRY MNXRVM #type complete TITLE minor outer capsid protein - bovine rotavirus A (strain VMRI) ORGANISM #formal_name bovine rotavirus A DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS C33557 REFERENCE A33557 !$#authors Matsui, S.M.; Mackow, E.R.; Matsuno, S.; Paul, P.S.; !1Greenberg, H.B. !$#journal J. Virol. (1990) 64:120-124 !$#title Sequence analysis of gene 11 equivalents from "short" and !1"super short" strains of rotavirus. !$#cross-references MUID:90080112; PMID:2152809 !$#accession C33557 !'##molecule_type genomic RNA !'##residues 1-198 ##label MAT !'##cross-references GB:M33606; NID:g333808; PIDN:AAA47314.1; !1PID:g333809 GENETICS !$#map_position segment 11 CLASSIFICATION #superfamily rotavirus minor outer capsid protein KEYWORDS capsid protein; coat protein SUMMARY #length 198 #molecular-weight 21679 #checksum 9131 SEQUENCE /// ENTRY MNXRSE #type complete TITLE minor outer capsid protein - simian rotavirus SA11 ORGANISM #formal_name simian rotavirus SA11 DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS S01246 REFERENCE S01246 !$#authors Mitchell, D.B.; Both, G.W. !$#journal Nucleic Acids Res. (1988) 16:6244 !$#title Simian rotavirus SA11 segment 11 contains overlapping !1reading frames. !$#cross-references MUID:88289384; PMID:2840642 !$#accession S01246 !'##molecule_type DNA !'##residues 1-198 ##label MIT !'##cross-references EMBL:X07831; NID:g61865; PIDN:CAA30683.1; !1PID:g61866 GENETICS !$#map_position segment 11 CLASSIFICATION #superfamily rotavirus minor outer capsid protein KEYWORDS capsid protein; coat protein SUMMARY #length 198 #molecular-weight 21722 #checksum 8527 SEQUENCE /// ENTRY MNXRRA #type complete TITLE minor outer capsid protein - rabbit rotavirus A (strain Alabama) ORGANISM #formal_name rabbit rotavirus A DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS A30233 REFERENCE A30233 !$#authors Gorziglia, M.; Nishikawa, K.; Fukuhara, N. !$#journal Virology (1989) 170:587-590 !$#title Evidence of duplication and deletion in super short segment !111 of rabbit rotavirus Alabama strain. !$#cross-references MUID:89268483; PMID:2543133 !$#accession A30233 !'##molecule_type genomic RNA !'##residues 1-198 ##label GOR !'##cross-references GB:J04361; NID:g333620; PIDN:AAA66883.1; !1PID:g333621 GENETICS !$#map_position segment 11 CLASSIFICATION #superfamily rotavirus minor outer capsid protein KEYWORDS capsid protein; coat protein SUMMARY #length 198 #molecular-weight 21810 #checksum 6700 SEQUENCE /// ENTRY MNXRB3 #type complete TITLE minor outer capsid protein - human rotavirus A (serotype G strain B37) ALTERNATE_NAMES nonstructural protein VP9 ORGANISM #formal_name human rotavirus A DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 08-Apr-1994 ACCESSIONS A34007 REFERENCE A34007 !$#authors Nuttall, S.D.; Hum, C.P.; Holmes, I.H.; Dyall-Smith, M.L. !$#journal Virology (1989) 171:453-457 !$#title Sequences of VP9 genes from short and supershort rotavirus !1strains. !$#cross-references MUID:89348003; PMID:2548328 !$#accession A34007 !'##molecule_type genomic RNA !'##residues 1-198 ##label NUT GENETICS !$#map_position segment 10 CLASSIFICATION #superfamily rotavirus minor outer capsid protein KEYWORDS capsid protein; coat protein SUMMARY #length 198 #molecular-weight 21797 #checksum 8698 SEQUENCE /// ENTRY MNXR69 #type complete TITLE minor outer capsid protein - human rotavirus A (strain 69M) ORGANISM #formal_name human rotavirus A #note host Homo sapiens (man) DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 08-Apr-1994 ACCESSIONS B33557 REFERENCE A33557 !$#authors Matsui, S.M.; Mackow, E.R.; Matsuno, S.; Paul, P.S.; !1Greenberg, H.B. !$#journal J. Virol. (1990) 64:120-124 !$#title Sequence analysis of gene 11 equivalents from "short" and !1"super short" strains of rotavirus. !$#cross-references MUID:90080112; PMID:2152809 !$#accession B33557 !'##molecule_type genomic RNA !'##residues 1-198 ##label MAT GENETICS !$#map_position segment 11 CLASSIFICATION #superfamily rotavirus minor outer capsid protein KEYWORDS capsid protein; coat protein SUMMARY #length 198 #molecular-weight 21731 #checksum 8061 SEQUENCE /// ENTRY MNXRB5 #type complete TITLE minor outer capsid protein - human rotavirus A (strain RV5) ALTERNATE_NAMES nonstructural protein VP9 ORGANISM #formal_name human rotavirus A DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 08-Apr-1994 ACCESSIONS B34007 REFERENCE A34007 !$#authors Nuttall, S.D.; Hum, C.P.; Holmes, I.H.; Dyall-Smith, M.L. !$#journal Virology (1989) 171:453-457 !$#title Sequences of VP9 genes from short and supershort rotavirus !1strains. !$#cross-references MUID:89348003; PMID:2548328 !$#accession B34007 !'##molecule_type genomic RNA !'##residues 1-200 ##label NUT CLASSIFICATION #superfamily rotavirus minor outer capsid protein KEYWORDS capsid protein; coat protein SUMMARY #length 200 #molecular-weight 21970 #checksum 2539 SEQUENCE /// ENTRY MNXRDS #type complete TITLE minor outer capsid protein - human rotavirus A (strain DS-1) ORGANISM #formal_name human rotavirus A #note host Homo sapiens (man) DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 08-Apr-1994 ACCESSIONS A33557 REFERENCE A33557 !$#authors Matsui, S.M.; Mackow, E.R.; Matsuno, S.; Paul, P.S.; !1Greenberg, H.B. !$#journal J. Virol. (1990) 64:120-124 !$#title Sequence analysis of gene 11 equivalents from "short" and !1"super short" strains of rotavirus. !$#cross-references MUID:90080112; PMID:2152809 !$#accession A33557 !'##molecule_type genomic RNA !'##residues 1-198 ##label MAT GENETICS !$#map_position segment 11 CLASSIFICATION #superfamily rotavirus minor outer capsid protein KEYWORDS capsid protein; coat protein SUMMARY #length 198 #molecular-weight 21699 #checksum 7505 SEQUENCE /// ENTRY VHXREH #type complete TITLE minor outer capsid protein - human rotavirus A (serotype 1 strain WA) ORGANISM #formal_name human rotavirus A #note host Homo sapiens (man) DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 16-Jul-1999 ACCESSIONS A04147 REFERENCE A04147 !$#authors Imai, M.; Richardson, M.A.; Ikegami, N.; Shatkin, A.J.; !1Furuichi, Y. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1983) 80:373-377 !$#title Molecular cloning of double-stranded RNA virus genomes. !$#cross-references MUID:83169661; PMID:6300836 !$#accession A04147 !'##molecule_type genomic RNA !'##residues 1-197 ##label IMA !'##cross-references GB:V01191; GB:J02440; NID:g61684; PIDN:CAA24511.1; !1PID:g61685 GENETICS !$#map_position segment 11 CLASSIFICATION #superfamily rotavirus minor outer capsid protein KEYWORDS capsid protein; coat protein; glycoprotein FEATURE !$20,117 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 197 #molecular-weight 21857 #checksum 7773 SEQUENCE /// ENTRY VHXRPU #type complete TITLE minor outer capsid protein - porcine rotavirus C (strain OSU) ORGANISM #formal_name porcine rotavirus C DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 16-Jul-1999 ACCESSIONS A34009 REFERENCE A34009 !$#authors Gonzalez, S.A.; Burrone, O.R. !$#journal Nucleic Acids Res. (1989) 17:6402 !$#title Porcine OSU rotavirus segment II sequence shows common !1features with the viral gene of human origin. !$#cross-references MUID:89366681; PMID:2549514 !$#accession A34009 !'##molecule_type genomic RNA !'##residues 1-197 ##label GON !'##cross-references GB:X15519; NID:g61882; PIDN:CAA33540.1; PID:g61883 GENETICS !$#map_position segment 11 CLASSIFICATION #superfamily rotavirus minor outer capsid protein KEYWORDS capsid protein; coat protein SUMMARY #length 197 #molecular-weight 21458 #checksum 6791 SEQUENCE /// ENTRY B48357 #type complete TITLE minor outer capsid protein - porcine rotavirus C (strain Cowden) ALTERNATE_NAMES nonstructural protein NS26 ORGANISM #formal_name porcine rotavirus C DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 17-Feb-1994 ACCESSIONS B48357 REFERENCE A48357 !$#authors Bremont, M.; Chabanne-Vautherot, D.; Cohen, J. !$#journal Arch. Virol. (1993) 130:85-92 !$#title Sequence analysis of three non structural proteins of a !1porcine group C (Cowden strain) rotavirus. !$#cross-references MUID:93277387; PMID:8389118 !$#accession B48357 !'##molecule_type genomic RNA !'##residues 1-210 ##label BRE !'##note sequence extracted from NCBI backbone (NCBIN:132693, !1NCBIP:132694) GENETICS !$#map_position segment 10 CLASSIFICATION #superfamily rotavirus minor outer capsid protein KEYWORDS capsid protein; coat protein; glycoprotein FEATURE !$30,120 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 210 #molecular-weight 23393 #checksum 621 SEQUENCE /// ENTRY MNXRB1 #type complete TITLE minor outer capsid protein - human rotavirus C (strain Bristol) ALTERNATE_NAMES nonstructural protein NS26 ORGANISM #formal_name human rotavirus C #note host Homo sapiens (man) DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS A42188 REFERENCE A42188 !$#authors Lambden, P.R.; Cooke, S.J.; Caul, E.O.; Clarke, I.N. !$#journal J. Virol. (1992) 66:1817-1822 !$#title Cloning of noncultivatable human rotavirus by single primer !1amplification. !$#cross-references MUID:92148978; PMID:1371174 !$#accession A42188 !'##molecule_type genomic RNA !'##residues 1-212 ##label LAM !'##cross-references GB:M81488; NID:g333878; PIDN:AAA47354.1; !1PID:g333879 GENETICS !$#map_position segment 10 CLASSIFICATION #superfamily rotavirus minor outer capsid protein KEYWORDS capsid protein; coat protein; glycoprotein FEATURE !$30,120,147,163 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 212 #molecular-weight 23792 #checksum 5927 SEQUENCE /// ENTRY P2XRWA #type complete TITLE RNA-binding protein - human rotavirus A (serotype 1 strain WA) ORGANISM #formal_name human rotavirus A DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jul-1999 ACCESSIONS A34008 REFERENCE A34008 !$#authors Ernst, H.; Duhl, J.A. !$#journal Nucleic Acids Res. (1989) 17:4382 !$#title Nucleotide sequence of genomic segment of the human !1rotavirus Wa. !$#cross-references MUID:89296494; PMID:2544861 !$#accession A34008 !'##molecule_type mRNA !'##residues 1-890 ##label ERN !'##cross-references GB:X14942; NID:g60310; PIDN:CAA33074.1; PID:g60311 GENETICS !$#map_position segment 2 CLASSIFICATION #superfamily rotavirus RNA-binding protein KEYWORDS RNA binding SUMMARY #length 890 #molecular-weight 103750 #checksum 2331 SEQUENCE /// ENTRY P2XRSR #type complete TITLE RNA-binding protein - simian rotavirus SA11 ALTERNATE_NAMES core protein VP2 ORGANISM #formal_name simian rotavirus SA11 DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jul-1999 ACCESSIONS B35321 REFERENCE A35321 !$#authors Mitchell, D.B.; Both, G.W. !$#journal Virology (1990) 177:324-331 !$#title Completion of the genomic sequence of the simian rotavirus !1SA11: nucleotide sequences of segments 1, 2, and 3. !$#cross-references MUID:90281597; PMID:2162107 !$#accession B35321 !'##molecule_type genomic RNA !'##residues 1-881 ##label MIT !'##cross-references EMBL:X16831; NID:g61874; PIDN:CAA34733.1; !1PID:g61875 GENETICS !$#map_position segment 2 CLASSIFICATION #superfamily rotavirus RNA-binding protein KEYWORDS core protein; leucine zipper; RNA binding FEATURE !$536-558 #region leucine zipper motif\ !$666-687 #region leucine zipper motif SUMMARY #length 881 #molecular-weight 102696 #checksum 228 SEQUENCE /// ENTRY P2XRUK #type complete TITLE RNA-binding protein - bovine rotavirus A (strain UK) ORGANISM #formal_name bovine rotavirus A #note host Bos sp. (cattle) DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS S10252 REFERENCE S10252 !$#authors Tian, Y.; Tarlow, O.; McCrae, M.A. !$#journal Nucleic Acids Res. (1990) 18:4015 !$#title Nucleotide sequence of gene 2 of the UK tissue culture !1adapted strain of the bovine rotavirus. !$#cross-references MUID:90326551; PMID:2165258 !$#accession S10252 !'##molecule_type genomic RNA !'##residues 1-881 ##label TIA !'##cross-references GB:X52589; NID:g61516; PIDN:CAA36825.1; PID:g61517 GENETICS !$#map_position segment 2 CLASSIFICATION #superfamily rotavirus RNA-binding protein KEYWORDS RNA binding SUMMARY #length 881 #molecular-weight 102487 #checksum 1498 SEQUENCE /// ENTRY P2XRCW #type complete TITLE RNA-binding protein - porcine rotavirus C (strain Cowden) ALTERNATE_NAMES core protein VP2; major internal core protein VP2 ORGANISM #formal_name porcine rotavirus C DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jul-1999 ACCESSIONS B40822 REFERENCE A40822 !$#authors Bremont, M.; Juste-Lesage, P.; Chabanne-Vautherot, D.; !1Charpilienne, A.; Cohen, J. !$#journal Virology (1992) 186:684-692 !$#title Sequences of the four larger proteins of a porcine group C !1rotavirus and comparison with the equivalent group A !1rotavirus proteins. !$#cross-references MUID:92124743; PMID:1310192 !$#accession B40822 !'##molecule_type genomic RNA !'##residues 1-872 ##label BRE !'##cross-references GB:M74217; NID:g333311; PIDN:AAA19561.1; !1PID:g333312 GENETICS !$#map_position segment 2 CLASSIFICATION #superfamily rotavirus RNA-binding protein KEYWORDS core protein; leucine zipper; RNA binding FEATURE !$527-551 #region leucine zipper motif\ !$657-682 #region leucine zipper motif SUMMARY #length 872 #molecular-weight 101018 #checksum 3851 SEQUENCE /// ENTRY F36841 #type complete TITLE E3L protein - variola virus (strain India-1967) ORGANISM #formal_name variola virus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 23-Mar-2001 ACCESSIONS F36841 REFERENCE A36859 !$#authors Blinov, V.M. !$#submission submitted to GenBank, November 1992 !$#accession F36841 !'##status preliminary !'##molecule_type DNA !'##residues 1-190 ##label BLI !'##cross-references GB:X69198; NID:g456758; PID:g297225 CLASSIFICATION #superfamily E3L protein; double-stranded RNA-binding repeat !1homology FEATURE !$114-185 #domain double-stranded RNA-binding repeat homology !8#label DSR SUMMARY #length 190 #molecular-weight 21663 #checksum 23 SEQUENCE /// ENTRY P2XR10 #type complete TITLE major outer capsid protein VP2 - bluetongue virus (serotype 10, American isolate) ALTERNATE_NAMES BTV hemagglutinin protein; principal serotype-determining antigen ORGANISM #formal_name bluetongue virus DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 16-Jul-1999 ACCESSIONS A25484; S10535 REFERENCE A25484 !$#authors Purdy, M.A.; Ghiasi, H.; Rao, C.D.; Roy, P. !$#journal J. Virol. (1985) 55:826-830 !$#title Complete sequence of bluetongue virus L2 RNA that codes for !1the antigen recognized by neutralizing antibodies. !$#cross-references MUID:85265048; PMID:2991598 !$#accession A25484 !'##molecule_type genomic RNA !'##residues 1-956 ##label PUR !'##cross-references GB:M11787; GB:M16566; NID:g210854; PIDN:AAA42828.1; !1PID:g210855 REFERENCE S10534 !$#authors Roy, P.; Marshall, J.J.A.; French, T.J. !$#journal Curr. Top. Microbiol. Immunol. (1990) 162:43-87 !$#title Structure of the bluetongue virus genome and its encoded !1proteins. !$#cross-references MUID:90345726; PMID:2166648 !$#accession S10535 !'##status preliminary !'##molecule_type genomic RNA !'##residues 1-956 ##label ROY GENETICS !$#map_position segment 2 CLASSIFICATION #superfamily bluetongue virus VP2 protein KEYWORDS capsid protein; hemagglutinin SUMMARY #length 956 #molecular-weight 111021 #checksum 4561 SEQUENCE /// ENTRY P2XR13 #type complete TITLE outer capsid protein VP2 - bluetongue virus (serotype 13) ORGANISM #formal_name bluetongue virus DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 16-Jun-2000 ACCESSIONS A27495 REFERENCE A27495 !$#authors Fukusho, A.; Ritter, G.D.; Roy, P. !$#journal J. Gen. Virol. (1987) 68:2967-2973 !$#title Variation in the bluetongue virus neutralization protein !1VP2. !$#cross-references MUID:88061222; PMID:2824673 !$#accession A27495 !'##molecule_type genomic RNA !'##residues 1-959 ##label FUK !'##cross-references GB:D00153; NID:g221072; PIDN:BAA00108.1; !1PID:g221073 GENETICS !$#map_position segment 2 CLASSIFICATION #superfamily bluetongue virus VP2 protein KEYWORDS capsid protein SUMMARY #length 959 #molecular-weight 112563 #checksum 9232 SEQUENCE /// ENTRY B60017 #type complete TITLE outer capsid protein VP2 - bluetongue virus (serotype 3, strain South Africa-VACC) ORGANISM #formal_name bluetongue virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS B60017 REFERENCE A60017 !$#authors Gould, A.R.; Pritchard, L.I. !$#journal Virus Res. (1990) 17:31-52 !$#title Relationships amongst bluetongue viruses revealed by !1comparisons of capsid and outer coat protein nucleotide !1sequences. !$#cross-references MUID:91021485; PMID:2171239 !$#accession B60017 !'##molecule_type genomic RNA !'##residues 1-959 ##label GOU !'##cross-references GB:X55801; NID:g297130; PIDN:CAA39323.1; !1PID:g297131 GENETICS !$#map_position segment 2 CLASSIFICATION #superfamily bluetongue virus VP2 protein KEYWORDS capsid protein; glycoprotein FEATURE !$749,910 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 959 #molecular-weight 112163 #checksum 4588 SEQUENCE /// ENTRY P2XRAU #type complete TITLE outer capsid protein VP2 - bluetongue virus (serotype 1, strain Australia) ORGANISM #formal_name bluetongue virus DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jul-1999 ACCESSIONS S03654; JS0322 REFERENCE S03654 !$#authors Yamaguchi, S.; Fukusho, A.; Roy, P. !$#journal Nucleic Acids Res. (1988) 16:2725 !$#title Complete sequence of VP2 gene of the bluetongue virus !1serotype 1 (BTV-1). !$#cross-references MUID:88203217; PMID:2834696 !$#accession S03654 !'##molecule_type genomic RNA !'##residues 1-961 ##label YAM REFERENCE JS0322 !$#authors Gould, A.R. !$#journal Virus Res. (1988) 9:145-158 !$#title Conserved and non-conserved regions of the outer coat !1protein, VP2, of the Australian bluetongue serotype 1 virus, !1revealed by sequence comparison to the VP2 of North American !1BTV serotype 10. !$#cross-references MUID:88180013; PMID:2833046 !$#accession JS0322 !'##molecule_type genomic RNA !'##residues 1-12,'V',14-71,'V',73-185,'LTL',189-199,'D',201-350,'F', !1352-556,'D',558-749,'N',751-961 ##label GOU !'##cross-references GB:M21844; NID:g323187; PIDN:AAA42844.1; !1PID:g323188 GENETICS !$#map_position segment 2 CLASSIFICATION #superfamily bluetongue virus VP2 protein KEYWORDS capsid protein SUMMARY #length 961 #molecular-weight 112095 #checksum 8398 SEQUENCE /// ENTRY P2XRSA #type complete TITLE outer capsid protein VP2 - bluetongue virus (serotype 1, strain South Africa) ORGANISM #formal_name bluetongue virus DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 07-May-1999 ACCESSIONS A60014; B60014 REFERENCE A60014 !$#authors Wade-Evans, A.M.; Mertens, P.P.C. !$#journal Virus Res. (1990) 15:213-230 !$#title Expression of the outer capsid protein, VP2, from a full !1length cDNA clone of genome segment 2 of bluetongue serotype !11 from South Africa, using both Sp6 and vaccinia expression !1systems and a comparison of the nucleic acid sequence of !1this segment with those of other serotypes. !$#cross-references MUID:90261331; PMID:2160764 !$#accession A60014 !'##molecule_type mRNA !'##residues 1-961 ##label WA1 !$#accession B60014 !'##molecule_type protein !'##residues 322-346;492-503 ##label WA2 GENETICS !$#map_position segment 2 CLASSIFICATION #superfamily bluetongue virus VP2 protein KEYWORDS capsid protein; glycoprotein; transmembrane protein FEATURE !$666-682 #domain transmembrane #status predicted #label TMN\ !$303,432 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 961 #molecular-weight 111937 #checksum 9142 SEQUENCE /// ENTRY A60017 #type complete TITLE outer capsid protein VP2 - bluetongue virus (serotype 1, strain South Africa-VACC) ORGANISM #formal_name bluetongue virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jul-1999 ACCESSIONS A60017 REFERENCE A60017 !$#authors Gould, A.R.; Pritchard, L.I. !$#journal Virus Res. (1990) 17:31-52 !$#title Relationships amongst bluetongue viruses revealed by !1comparisons of capsid and outer coat protein nucleotide !1sequences. !$#cross-references MUID:91021485; PMID:2171239 !$#accession A60017 !'##molecule_type genomic RNA !'##residues 1-961 ##label GOU !'##cross-references GB:X55800; NID:g297132; PIDN:CAA39322.1; !1PID:g297133 GENETICS !$#map_position segment 2 CLASSIFICATION #superfamily bluetongue virus VP2 protein KEYWORDS capsid protein; glycoprotein; membrane protein FEATURE !$303,432 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 961 #molecular-weight 111755 #checksum 9904 SEQUENCE /// ENTRY JQ1634 #type complete TITLE outer capsid protein VP2 - epizootic hemorrhagic disease virus (type 1) ORGANISM #formal_name epizootic hemorrhagic disease virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 07-May-1999 ACCESSIONS JQ1634 REFERENCE JQ1634 !$#authors Iwata, H.; Chuma, T.; Roy, P. !$#journal J. Gen. Virol. (1992) 73:915-924 !$#title Characterization of the genes encoding two of the major !1capsid proteins of epizootic haemorrhagic disease virus !1indicates a close genetic relationship to bluetongue virus. !$#cross-references MUID:92341072; PMID:1321879 !$#accession JQ1634 !'##molecule_type mRNA !'##residues 1-971 ##label IWA !'##cross-references DDBJ:D01139 GENETICS !$#map_position segment L2 CLASSIFICATION #superfamily bluetongue virus VP2 protein KEYWORDS capsid protein; glycoprotein FEATURE !$5,32,83,146,422 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 971 #molecular-weight 113247 #checksum 1130 SEQUENCE /// ENTRY P2XRA4 #type complete TITLE outer capsid protein VP2 - African horse sickness virus (serotype 4) ORGANISM #formal_name African horse sickness virus DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jul-1999 ACCESSIONS A36820 REFERENCE A36820 !$#authors Iwata, H.; Rowley, A.; Yamagawa, M.; Roy, P. !$#submission submitted to GenBank, May 1992 !$#description Evolutionary relationships among the gnat-transmitted !1orbiviruses that cause African horse sickness, bluetongue, !1and epizootic hemorrhagic disease as evidenced by their !1capsid protein sequences. !$#accession A36820 !'##molecule_type genomic RNA !'##residues 1-1060 ##label IWA !'##cross-references GB:M94680; NID:g210052; PIDN:AAA42537.1; !1PID:g210053 REFERENCE A44053 !$#authors Iwata, H.; Yamagawa, M.; Roy, P. !$#journal Virology (1992) 191:251-261 !$#title Evolutionary relationships among the gnat-transmitted !1orbiviruses that cause African horse sickness, bluetongue, !1and epizootic hemorrhagic disease as evidenced by their !1capsid protein sequences. !$#cross-references MUID:93033117; PMID:1329319 !$#contents annotation !$#note neither amino acid nor nucleotide sequence is given CLASSIFICATION #superfamily African horse sickness virus VP2 protein KEYWORDS capsid protein; glycoprotein FEATURE !$292,301,498,624, !$1016 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1060 #molecular-weight 124057 #checksum 8504 SEQUENCE /// ENTRY P3XR17 #type complete TITLE core protein VP3 - bluetongue virus ORGANISM #formal_name bluetongue virus DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 16-Jul-1999 ACCESSIONS A04148 REFERENCE A04148 !$#authors Purdy, M.; Petre, J.; Roy, P. !$#journal J. Virol. (1984) 51:754-759 !$#title Cloning of the bluetongue virus L3 gene. !$#cross-references MUID:84292453; PMID:6206235 !$#accession A04148 !'##molecule_type genomic RNA !'##residues 1-901 ##label PUR !'##cross-references GB:K02369; NID:g210860; PIDN:AAA42831.1; !1PID:g210861 GENETICS !$#map_position segment 3 CLASSIFICATION #superfamily bluetongue virus core protein VP3 KEYWORDS core protein SUMMARY #length 901 #molecular-weight 103414 #checksum 9051 SEQUENCE /// ENTRY P3XREH #type complete TITLE core protein VP3 - epizootic hemorrhagic disease virus (type 1) ORGANISM #formal_name epizootic hemorrhagic disease virus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jul-1999 ACCESSIONS A40900; A43971; S18107 REFERENCE A40900 !$#authors Le Blois, H.; Fayard, B.; Urakawa, T.; Roy, P. !$#journal J. Virol. (1991) 65:4821-4831 !$#title Synthesis and characterization of chimeric particles between !1epizootic hemorrhagic disease virus and bluetongue virus: !1functional domains are conserved on the VP3 protein. !$#cross-references MUID:91333025; PMID:1870203 !$#accession A40900 !'##molecule_type genomic RNA !'##residues 1-899 ##label LEB !'##cross-references GB:M76616; NID:g323735; PIDN:AAA43002.1; !1PID:g323736 REFERENCE A43971 !$#authors Wilson, W.C. !$#journal Virus Res. (1991) 21:225-236 !$#title Molecular comparison of VP3 from bluetongue and epizootic !1hemorrhagic disease viruses. !$#cross-references MUID:92116637; PMID:1662848 !$#accession A43971 !'##molecule_type genomic RNA !'##residues 1-231,'AA',234-298,'EYVS',303-748,'LQ',751-767,'G',769-786, !1'L',788-884,'T',886-899 ##label WIL !'##cross-references GB:S76272 !'##note sequence extracted from NCBI backbone (NCBIN:76272, !1NCBIP:76274) GENETICS !$#map_position segment 3 CLASSIFICATION #superfamily bluetongue virus core protein VP3 KEYWORDS core protein SUMMARY #length 899 #molecular-weight 103495 #checksum 6349 SEQUENCE /// ENTRY A43969 #type complete TITLE core protein VP3 - epizootic hemorrhagic disease virus (type 2, strain Australia) ORGANISM #formal_name epizootic hemorrhagic disease virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jul-1999 ACCESSIONS A43969 REFERENCE A43969 !$#authors Gould, A.R.; Pritchard, L.I. !$#journal Virus Res. (1991) 21:1-18 !$#title Phylogenetic analyses of the complete nucleotide sequence of !1the capsid protein (VP3) of Australian epizootic !1haemorrhagic disease of deer virus (serotype 2) and cognate !1genes from other orbiviruses. !$#cross-references MUID:92074320; PMID:1962502 !$#accession A43969 !'##molecule_type genomic RNA !'##residues 1-899 ##label GOU !'##cross-references GB:S68010; NID:g239784; PIDN:AAB20469.1; !1PID:g239785 !'##note sequence extracted from NCBI backbone (NCBIN:68010, !1NCBIP:68012) GENETICS !$#map_position segment 3 CLASSIFICATION #superfamily bluetongue virus core protein VP3 KEYWORDS core protein SUMMARY #length 899 #molecular-weight 103150 #checksum 4924 SEQUENCE /// ENTRY P3XRA4 #type complete TITLE inner capsid protein VP3 - African horse sickness virus (serotype 4) ORGANISM #formal_name African horse sickness virus DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 07-May-1999 ACCESSIONS B44053 REFERENCE A44053 !$#authors Iwata, H.; Yamagawa, M.; Roy, P. !$#journal Virology (1992) 191:251-261 !$#title Evolutionary relationships among the gnat-transmitted !1orbiviruses that cause African horse sickness, bluetongue, !1and epizootic hemorrhagic disease as evidenced by their !1capsid protein sequences. !$#cross-references MUID:93033117; PMID:1329319 !$#accession B44053 !'##molecule_type genomic RNA !'##residues 1-905 ##label IWA !'##cross-references GB:M94681 CLASSIFICATION #superfamily bluetongue virus core protein VP3 KEYWORDS capsid protein SUMMARY #length 905 #molecular-weight 102824 #checksum 9679 SEQUENCE /// ENTRY JQ1938 #type complete TITLE structural core protein VP2 - Broadhaven virus ORGANISM #formal_name Broadhaven virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 07-May-1999 ACCESSIONS JQ1938 REFERENCE JQ1938 !$#authors Moss, S.R.; Jones, L.D.; Nuttall, P.A. !$#journal J. Gen. Virol. (1992) 73:2585-2590 !$#title Comparison of the major structural core proteins of !1tick-borne and Culicoides-borne orbiviruses. !$#cross-references MUID:93019012; PMID:1328474 !$#accession JQ1938 !'##molecule_type genomic RNA !'##residues 1-908 ##label MOS !'##cross-references GB:M87875 !'##note the authors translated the codon ACG for residue 266 as Tyr GENETICS !$#map_position segment 2 CLASSIFICATION #superfamily bluetongue virus core protein VP3 KEYWORDS core protein SUMMARY #length 908 #molecular-weight 102894 #checksum 6517 SEQUENCE /// ENTRY P5XR10 #type complete TITLE outer capsid protein VP5 - bluetongue virus (serotype 10, American isolate) ORGANISM #formal_name bluetongue virus DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 16-Jun-2000 ACCESSIONS A25419; S10538 REFERENCE A25419 !$#authors Purdy, M.A.; Ritter, G.D.; Roy, P. !$#journal J. Gen. Virol. (1986) 67:957-962 !$#title Nucleotide sequence of cDNA clones encoding the outer capsid !1protein, VP5, of bluetongue virus serotype 10. !$#cross-references MUID:86198636; PMID:3009695 !$#accession A25419 !'##molecule_type genomic RNA !'##residues 1-526 ##label PUR !'##cross-references GB:D12532; GB:D01183; NID:g221078; PIDN:BAA02095.1; !1PID:g221079 REFERENCE S10534 !$#authors Roy, P.; Marshall, J.J.A.; French, T.J. !$#journal Curr. Top. Microbiol. Immunol. (1990) 162:43-87 !$#title Structure of the bluetongue virus genome and its encoded !1proteins. !$#cross-references MUID:90345726; PMID:2166648 !$#accession S10538 !'##status preliminary !'##molecule_type genomic RNA !'##residues 1-526 ##label ROY GENETICS !$#map_position segment 5 CLASSIFICATION #superfamily bluetongue virus outer capsid protein VP5 KEYWORDS capsid protein SUMMARY #length 526 #molecular-weight 59162 #checksum 3004 SEQUENCE /// ENTRY A43968 #type complete TITLE outer capsid protein VP5 - bluetongue virus ORGANISM #formal_name bluetongue virus DATE 30-Sep-1993 #sequence_revision 22-Oct-1999 #text_change 22-Oct-1999 ACCESSIONS S23619; A43968 REFERENCE S23619 !$#authors Yang, Y.Y.; Li, J.K.K. !$#journal Virus Res. (1992) 23:163-171 !$#title Complete genomic sequences of the GP5 protein gene of !1bluetongue virus serotype 11 and 17. !$#cross-references MUID:92295711; PMID:1318625 !$#accession S23619 !'##status preliminary !'##molecule_type genomic RNA !'##residues 1-533 ##label YAN !'##cross-references EMBL:X55359; NID:g58779; PIDN:CAA39042.1; !1PID:g58780 !'##note the authors did not translate the codons for residues 1-7 !'##note it is uncertain whether Met-1 or Met-8 is the initiator REFERENCE A43968 !$#authors Dunn, S.J.; Hsu, D.; Zee, Y.C.; Stott, J.L. !$#journal Virus Res. (1991) 21:155-162 !$#title Complete nucleotide and deduced amino acid sequence of !1genome segment 5 encoding the outer capsid protein, VP5, of !1a U.S. isolate of bluetongue virus serotype 11. !$#cross-references MUID:92101623; PMID:1661982 !$#accession A43968 !'##molecule_type genomic RNA !'##residues 8-533 ##label DUN !'##cross-references GB:M73715; NID:g210852; PIDN:AAA42823.1; !1PID:g210853 !'##experimental_source serotype 11, strain USA !'##note sequence extracted from NCBI backbone (NCBIN:72955, !1NCBIP:72957) GENETICS !$#map_position segment 5 CLASSIFICATION #superfamily bluetongue virus outer capsid protein VP5 KEYWORDS capsid protein; coat protein; glycoprotein FEATURE !$395,441 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 533 #molecular-weight 60150 #checksum 2802 SEQUENCE /// ENTRY P5XRBT #type complete TITLE outer capsid protein VP5 - bluetongue virus (serotype 13, strain USA) ORGANISM #formal_name bluetongue virus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jul-1999 ACCESSIONS A38481 REFERENCE A38481 !$#authors Oldfield, S.; Hirasawa, T.; Roy, P. !$#journal J. Gen. Virol. (1991) 72:449-451 !$#title Sequence conservation of the outer capsid protein, VP5, of !1bluetongue virus, a contrasting feature to the outer capsid !1protein VP2. !$#cross-references MUID:91132147; PMID:1847179 !$#accession A38481 !'##molecule_type genomic RNA !'##residues 1-526 ##label OLD !'##cross-references GB:X54308; NID:g60704; PIDN:CAA38205.1; PID:g60705 GENETICS !$#map_position segment 5 CLASSIFICATION #superfamily bluetongue virus outer capsid protein VP5 KEYWORDS capsid protein; coat protein SUMMARY #length 526 #molecular-weight 59194 #checksum 5874 SEQUENCE /// ENTRY S18762 #type complete TITLE outer capsid protein VP5 - epizootic hemorrhagic disease virus (serotype 1, strain USA) ORGANISM #formal_name epizootic hemorrhagic disease virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jul-1999 ACCESSIONS S18762; S26752 REFERENCE S18762 !$#authors Iwata, H.; Hirasawa, T.; Roy, P. !$#journal Virus Res. (1991) 20:273-281 !$#title Complete nucleotide sequence of segment 5 of epizootic !1haemorrhagic disease virus; the outer capsid protein VP5 is !1homologous to the VP5 protein of bluetongue virus. !$#cross-references MUID:92116632; PMID:1662845 !$#accession S18762 !'##molecule_type genomic RNA !'##residues 1-527 ##label IWA !'##cross-references EMBL:X55782 REFERENCE S26752 !$#authors Roy, P. !$#submission submitted to the EMBL Data Library, November 1990 !$#accession S26752 !'##molecule_type genomic RNA !'##residues 1-392,'S',394-527 ##label ROY !'##cross-references EMBL:X55782; NID:g59227; PIDN:CAA39303.1; !1PID:g59228 GENETICS !$#map_position segment 5 CLASSIFICATION #superfamily bluetongue virus outer capsid protein VP5 KEYWORDS capsid protein; coat protein; glycoprotein FEATURE !$390,484 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 527 #molecular-weight 59179 #checksum 1761 SEQUENCE /// ENTRY P5XR15 #type complete TITLE outer capsid protein VP5 - bluetongue virus (serotype 1, strain Australia) ORGANISM #formal_name bluetongue virus DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 23-Jul-1999 ACCESSIONS JS0323 REFERENCE JS0323 !$#authors Gould, A.R.; Pritchard, L.I. !$#journal Virus Res. (1988) 9:285-292 !$#title The complete nucleotide sequence of the outer coat protein, !1VP5, of the Australian bluetongue virus (BTV) serotype 1 !1reveals conserved and non-conserved sequences. !$#cross-references MUID:88237575; PMID:2837015 !$#accession JS0323 !'##molecule_type genomic RNA !'##residues 1-526 ##label GOU !'##cross-references GB:M21845; NID:g323193; PIDN:AAA42849.1; !1PID:g323194 GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily bluetongue virus outer capsid protein VP5 KEYWORDS capsid protein SUMMARY #length 526 #molecular-weight 59243 #checksum 6851 SEQUENCE /// ENTRY P5XRBU #type complete TITLE outer capsid protein VP5 - bluetongue virus (serotype 2, strain USA) ORGANISM #formal_name bluetongue virus DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 23-Jul-1999 ACCESSIONS A43486; S26852 REFERENCE A43486 !$#authors Hirasawa, T.; Roy, P. !$#journal Virus Res. (1990) 15:107-112 !$#title The complete nucleotide sequence of VP5 of a strain of !1bluetongue virus of serotype 2 isolated in the USA reveals !1its close relationship with a virus of serotype 1 isolated !1in Australia. !$#cross-references MUID:90209358; PMID:2157314 !$#accession A43486 !'##molecule_type genomic RNA !'##residues 1-526 ##label HIR !'##cross-references GB:X62283; NID:g60708; PIDN:CAA44172.1; PID:g60709 !'##experimental_source serotype 2, strain USA REFERENCE S26852 !$#authors Blachere, C. !$#submission submitted to the EMBL Data Library, September 1991 !$#accession S26852 !'##status preliminary !'##molecule_type DNA !'##residues 1-526 ##label BLA !'##cross-references EMBL:X62283; NID:g60708; PIDN:CAA44172.1; !1PID:g60709 GENETICS !$#map_position segment 5 CLASSIFICATION #superfamily bluetongue virus outer capsid protein VP5 KEYWORDS capsid protein; coat protein; glycoprotein FEATURE !$388 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 526 #molecular-weight 58953 #checksum 6927 SEQUENCE /// ENTRY A45185 #type complete TITLE outer capsid protein VP5 - bluetongue virus (serotype 1, strain South Africa) ORGANISM #formal_name bluetongue virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 23-Jul-1999 ACCESSIONS A45185 REFERENCE A45185 !$#authors Wade-Evans, A.M.; Pan, Z.Q.; Mertens, P.P.C. !$#journal Virus Res. (1988) 11:227-240 !$#title Sequence analysis and in vitro expression of a cDNA clone of !1genome segment 5 from bluetongue virus, serotype 1 from !1South Africa. !$#cross-references MUID:89059564; PMID:2848383 !$#accession A45185 !'##molecule_type genomic RNA !'##residues 1-526 ##label WAD !'##cross-references GB:M36713; NID:g323191; PIDN:AAA42848.1; !1PID:g323192 GENETICS !$#map_position segment 5 CLASSIFICATION #superfamily bluetongue virus outer capsid protein VP5 KEYWORDS capsid protein; coat protein; glycoprotein FEATURE !$388 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 526 #molecular-weight 59421 #checksum 6901 SEQUENCE /// ENTRY P5XRA4 #type complete TITLE outer capsid protein VP5 - African horse sickness virus (serotype 4) ORGANISM #formal_name African horse sickness virus DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 23-Jul-1999 ACCESSIONS A44053 REFERENCE A44053 !$#authors Iwata, H.; Yamagawa, M.; Roy, P. !$#journal Virology (1992) 191:251-261 !$#title Evolutionary relationships among the gnat-transmitted !1orbiviruses that cause African horse sickness, bluetongue, !1and epizootic hemorrhagic disease as evidenced by their !1capsid protein sequences. !$#cross-references MUID:93033117; PMID:1329319 !$#accession A44053 !'##molecule_type genomic RNA !'##residues 1-505 ##label IWA !'##cross-references GB:M94682; NID:g210056; PIDN:AAA42539.1; !1PID:g210057 CLASSIFICATION #superfamily bluetongue virus outer capsid protein VP5 KEYWORDS capsid protein; coat protein; glycoprotein FEATURE !$13 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 505 #molecular-weight 56780 #checksum 1926 SEQUENCE /// ENTRY A45339 #type complete TITLE outer capsid protein VP5 - Broadhaven virus ORGANISM #formal_name Broadhaven virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 23-Jul-1999 ACCESSIONS A45339 REFERENCE A45339 !$#authors Moss, S.R.; Fukusho, A.; Nuttall, P.A. !$#journal Virology (1990) 179:482-484 !$#title RNA segment 5 of Broadhaven virus, a tick-borne orbivirus, !1shows sequence homology with segment 5 of bluetongue virus. !$#cross-references MUID:91021056; PMID:2171220 !$#accession A45339 !'##molecule_type genomic RNA !'##residues 1-480 ##label MOS !'##cross-references GB:M58030; NID:g210813; PIDN:AAA42802.1; !1PID:g210814 GENETICS !$#map_position segment 5 CLASSIFICATION #superfamily bluetongue virus outer capsid protein VP5 KEYWORDS capsid protein; coat protein; glycoprotein FEATURE !$122,201 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 480 #molecular-weight 52522 #checksum 1741 SEQUENCE /// ENTRY P7XRB1 #type complete TITLE core protein VP7 - bluetongue virus (serotype 1, strain Australia) ORGANISM #formal_name bluetongue virus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 23-Jul-1999 ACCESSIONS A38551 REFERENCE A38551 !$#authors Eaton, B.T.; Gould, A.R.; Hyatt, A.D.; Coupar, B.E.H.; !1Martyn, J.C.; White, J.R. !$#journal Virology (1991) 180:687-696 !$#title A bluetongue serogroup-reactive epitope in the amino !1terminal half of the major core protein VP7 is accessible on !1the surface of bluetongue virus particles. !$#cross-references MUID:91111987; PMID:1703371 !$#accession A38551 !'##molecule_type genomic RNA !'##residues 1-349 ##label EAT !'##cross-references EMBL:M63417; NID:g323195; PIDN:AAA42850.1; !1PID:g323196 GENETICS !$#map_position segment 7 CLASSIFICATION #superfamily bluetongue virus core protein VP7 KEYWORDS core protein SUMMARY #length 349 #molecular-weight 38531 #checksum 1166 SEQUENCE /// ENTRY P7XRB2 #type complete TITLE core protein VP7 - bluetongue virus (serotype 2, strain USA) ORGANISM #formal_name bluetongue virus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 23-Jul-1999 ACCESSIONS A37950 REFERENCE A37950 !$#authors Kowalik, T.F.; Li, J.K.K. !$#journal Virology (1991) 181:749-755 !$#title Bluetongue virus evolution: sequence analyses of the genomic !1S1 segments and major core protein VP7. !$#cross-references MUID:91196269; PMID:1849684 !$#accession A37950 !'##molecule_type genomic RNA !'##residues 1-349 ##label KOW !'##cross-references GB:M64997; EMBL:M38172; NID:g323201; !1PIDN:AAA42852.1; PID:g323202 GENETICS !$#map_position segment 7 CLASSIFICATION #superfamily bluetongue virus core protein VP7 KEYWORDS core protein SUMMARY #length 349 #molecular-weight 38517 #checksum 99 SEQUENCE /// ENTRY P7XR10 #type complete TITLE core protein VP7 - bluetongue virus (serotypes 10 and 11) ORGANISM #formal_name bluetongue virus DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 23-Jul-1999 ACCESSIONS A28537; A35527; S10540 REFERENCE A28537 !$#authors Yu, Y.; Fukusho, A.; Ritter, D.G.; Roy, P. !$#journal Nucleic Acids Res. (1988) 16:1620 !$#title Complete nucleotide sequence of the group-reactive antigen !1VP7 gene of bluetongue virus. !$#cross-references MUID:88157722; PMID:2831505 !$#accession A28537 !'##molecule_type genomic RNA !'##residues 1-349 ##label YUY !'##cross-references GB:X06463; NID:g58755; PIDN:CAA29771.1; PID:g58756 !'##experimental_source serotype 10 REFERENCE A35527 !$#authors Kowalik, T.F.; Yang, Y.Y.; Li, J.K.K. !$#journal Virology (1990) 177:820-823 !$#title Molecular cloning and comparative sequence analyses of !1bluetongue virus S1 segments by selective synthesis of !1specific full-length DNA copies of dsRNA genes. !$#cross-references MUID:90320164; PMID:2164738 !$#accession A35527 !'##molecule_type genomic RNA !'##residues 1-349 ##label KOW !'##cross-references GB:M32102; NID:g323203; PIDN:AAA42853.1; !1PID:g323204 !'##experimental_source serotype 11 REFERENCE S10534 !$#authors Roy, P.; Marshall, J.J.A.; French, T.J. !$#journal Curr. Top. Microbiol. Immunol. (1990) 162:43-87 !$#title Structure of the bluetongue virus genome and its encoded !1proteins. !$#cross-references MUID:90345726; PMID:2166648 !$#accession S10540 !'##status preliminary !'##molecule_type genomic RNA !'##residues 1-349 ##label ROY !'##experimental_source serotype 10, American isolate GENETICS !$#map_position segment 7 CLASSIFICATION #superfamily bluetongue virus core protein VP7 KEYWORDS core protein SUMMARY #length 349 #molecular-weight 38547 #checksum 783 SEQUENCE /// ENTRY P7XR13 #type complete TITLE core protein VP7 - bluetongue virus (serotype 13) ORGANISM #formal_name bluetongue virus DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 23-Jul-1999 ACCESSIONS A33385 REFERENCE A33385 !$#authors Kowalik, T.F.; Li, J.K.K. !$#journal Virology (1989) 172:189-195 !$#title Sequence analyses and structural predictions of !1double-stranded RNA segment S1 and VP7 from United States !1prototype bluetongue virus serotypes 13 and 10. !$#cross-references MUID:89370300; PMID:2549709 !$#accession A33385 !'##molecule_type genomic RNA !'##residues 1-349 ##label KOW !'##cross-references GB:J04365; NID:g210864; PIDN:AAA42833.1; !1PID:g210865 GENETICS !$#map_position segment 7 CLASSIFICATION #superfamily bluetongue virus core protein VP7 KEYWORDS core protein SUMMARY #length 349 #molecular-weight 38615 #checksum 4894 SEQUENCE /// ENTRY JQ1635 #type complete TITLE core protein VP7 - epizootic hemorrhagic disease virus (type 1) ORGANISM #formal_name epizootic hemorrhagic disease virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 07-May-1999 ACCESSIONS JQ1635 REFERENCE JQ1634 !$#authors Iwata, H.; Chuma, T.; Roy, P. !$#journal J. Gen. Virol. (1992) 73:915-924 !$#title Characterization of the genes encoding two of the major !1capsid proteins of epizootic haemorrhagic disease virus !1indicates a close genetic relationship to bluetongue virus. !$#cross-references MUID:92341072; PMID:1321879 !$#accession JQ1635 !'##molecule_type mRNA !'##residues 1-349 ##label IWA !'##cross-references DDBJ:D01140 GENETICS !$#map_position segment 7 CLASSIFICATION #superfamily bluetongue virus core protein VP7 KEYWORDS core protein SUMMARY #length 349 #molecular-weight 38296 #checksum 4536 SEQUENCE /// ENTRY JQ1939 #type complete TITLE core protein VP7 - Broadhaven virus ORGANISM #formal_name Broadhaven virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 07-May-1999 ACCESSIONS JQ1939 REFERENCE JQ1938 !$#authors Moss, S.R.; Jones, L.D.; Nuttall, P.A. !$#journal J. Gen. Virol. (1992) 73:2585-2590 !$#title Comparison of the major structural core proteins of !1tick-borne and Culicoides-borne orbiviruses. !$#cross-references MUID:93019012; PMID:1328474 !$#accession JQ1939 !'##molecule_type genomic RNA !'##residues 1-356 ##label MOS !'##cross-references GB:M87876 GENETICS !$#map_position segment 7 CLASSIFICATION #superfamily bluetongue virus core protein VP7 KEYWORDS core protein SUMMARY #length 356 #molecular-weight 40197 #checksum 5652 SEQUENCE /// ENTRY JQ1946 #type complete TITLE core protein VP7 - African horse sickness virus (serotype 4, strain Spane) ORGANISM #formal_name African horse sickness virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jun-2000 ACCESSIONS JQ1946 REFERENCE JQ1946 !$#authors Roy, P.; Hirasawa, T.; Fernandez, M.; Blinov, V.M.; !1Sanchez-Vixcain Rodrique, J.M. !$#journal J. Gen. Virol. (1991) 72:1237-1241 !$#title The complete sequence of the group-specific antigen, VP7, of !1African horsesickness disease virus serotype 4 reveals a !1close relationship to bluetongue virus. !$#cross-references MUID:91259049; PMID:1646273 !$#accession JQ1946 !'##molecule_type genomic RNA !'##residues 1-353 ##label ROY !'##cross-references GB:D12533; NID:g221010; PIDN:BAA02096.1; !1PID:g221011 GENETICS !$#map_position segment 7 CLASSIFICATION #superfamily bluetongue virus core protein VP7 KEYWORDS core protein SUMMARY #length 353 #molecular-weight 38166 #checksum 8110 SEQUENCE /// ENTRY P1XRBR #type complete TITLE inner layer protein VP1 - bovine rotavirus A (strain RF) ALTERNATE_NAMES core protein VP1 ORGANISM #formal_name bovine rotavirus A DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 23-Jul-1999 ACCESSIONS A32439 REFERENCE A32439 !$#authors Cohen, J.; Charpilienne, A.; Chilmonczyk, S.; Estes, M.K. !$#journal Virology (1989) 171:131-140 !$#title Nucleotide sequence of bovine rotavirus gene 1 and !1expression of the gene product in baculovirus. !$#cross-references MUID:89299450; PMID:2545026 !$#accession A32439 !'##molecule_type genomic RNA !'##residues 1-1088 ##label COH !'##cross-references GB:J04346; NID:g333821; PIDN:AAA47319.1; !1PID:g333822 GENETICS !$#map_position segment 1 CLASSIFICATION #superfamily rotavirus inner layer protein VP1 KEYWORDS core protein; glycoprotein FEATURE !$68,208,236,258,512, !$547,760,1048,1072 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1088 #molecular-weight 124989 #checksum 3852 SEQUENCE /// ENTRY P1XRSR #type complete TITLE inner layer protein VP1 - simian rotavirus SA11 ALTERNATE_NAMES core protein VP1 ORGANISM #formal_name simian rotavirus SA11 DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 23-Jul-1999 ACCESSIONS A35321 REFERENCE A35321 !$#authors Mitchell, D.B.; Both, G.W. !$#journal Virology (1990) 177:324-331 !$#title Completion of the genomic sequence of the simian rotavirus !1SA11: nucleotide sequences of segments 1, 2, and 3. !$#cross-references MUID:90281597; PMID:2162107 !$#accession A35321 !'##molecule_type genomic RNA !'##residues 1-1088 ##label MIT !'##cross-references EMBL:X16830; NID:g61872; PIDN:CAA34732.1; !1PID:g61873 COMMENT This protein may be associated with RNA polymerase activity. GENETICS !$#map_position segment 1 CLASSIFICATION #superfamily rotavirus inner layer protein VP1 KEYWORDS core protein SUMMARY #length 1088 #molecular-weight 125126 #checksum 3685 SEQUENCE /// ENTRY P1XRPR #type complete TITLE inner layer protein VP1 - porcine rotavirus C (strain Gottfried) ALTERNATE_NAMES core protein VP1 ORGANISM #formal_name porcine rotavirus C DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 08-Apr-1994 ACCESSIONS A33749 REFERENCE A33749 !$#authors Fukuhara, N.; Nishikawa, K.; Gorziglia, M.; Kapikian, A.Z. !$#journal Virology (1989) 173:743-749 !$#title Nucleotide sequence of gene segment 1 of a porcine rotavirus !1strain. !$#cross-references MUID:90085826; PMID:2556853 !$#accession A33749 !'##molecule_type genomic RNA !'##residues 1-1088 ##label FUK GENETICS !$#map_position segment 1 CLASSIFICATION #superfamily rotavirus inner layer protein VP1 KEYWORDS core protein; glycoprotein FEATURE !$68,236,258,547,760, !$1048,1072 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1088 #molecular-weight 124952 #checksum 9327 SEQUENCE /// ENTRY P1XRPC #type complete TITLE inner layer protein VP1 - porcine rotavirus C (strain Cowden) ALTERNATE_NAMES core protein VP1; minor internal core protein VP1 ORGANISM #formal_name porcine rotavirus C DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 23-Jul-1999 ACCESSIONS A40822 REFERENCE A40822 !$#authors Bremont, M.; Juste-Lesage, P.; Chabanne-Vautherot, D.; !1Charpilienne, A.; Cohen, J. !$#journal Virology (1992) 186:684-692 !$#title Sequences of the four larger proteins of a porcine group C !1rotavirus and comparison with the equivalent group A !1rotavirus proteins. !$#cross-references MUID:92124743; PMID:1310192 !$#accession A40822 !'##molecule_type genomic RNA !'##residues 1-1082 ##label BRE !'##cross-references GB:M74216; NID:g333309; PIDN:AAB00801.1; !1PID:g333310 COMMENT This protein may have RNA polymerase activity. GENETICS !$#map_position segment 1 CLASSIFICATION #superfamily rotavirus inner layer protein VP1 KEYWORDS core protein; glycoprotein FEATURE !$136,160,206,234, !$753,808,855,881, !$891,946,1053 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1082 #molecular-weight 125081 #checksum 9580 SEQUENCE /// ENTRY A44280 #type complete TITLE inner layer protein VP1 - human rotavirus B (strain IDIR) ALTERNATE_NAMES core protein VP1 ORGANISM #formal_name human rotavirus B DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 31-Dec-1993 ACCESSIONS A44280 REFERENCE A44280 !$#authors Eiden, J.J.; Hirshon, C. !$#journal Virology (1993) 192:154-160 !$#title Sequence analysis of group B rotavirus gene 1 and definition !1of a rotavirus-specific sequence motif within the RNA !1polymerase gene. !$#cross-references MUID:93297100; PMID:8390749 !$#accession A44280 !'##molecule_type genomic RNA !'##residues 1-1159 ##label EID !'##cross-references GB:M97203 GENETICS !$#gene 1 !$#map_position segment 1 CLASSIFICATION #superfamily rotavirus inner layer protein VP1 KEYWORDS core protein; glycoprotein FEATURE !$310,343,356,443, !$694,914 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1159 #molecular-weight 131649 #checksum 9033 SEQUENCE /// ENTRY P3XRSR #type complete TITLE minor inner core protein VP3 - simian rotavirus SA11 ORGANISM #formal_name simian rotavirus SA11 DATE 31-Mar-1992 #sequence_revision 22-Oct-1999 #text_change 22-Oct-1999 ACCESSIONS S06085; C35321 REFERENCE S06085 !$#authors Liu, M.; Estes, M.K. !$#journal Nucleic Acids Res. (1989) 17:7991 !$#title Nucleotide sequence of the simian rotavirus SA11 genome !1segment 3. !$#cross-references MUID:90016887; PMID:2552420 !$#accession S06085 !'##status translation not shown !'##molecule_type genomic RNA !'##residues 1-835 ##label LIU !'##cross-references EMBL:X16062; NID:g61901; PIDN:CAA34198.1; !1PID:g61902 REFERENCE A35321 !$#authors Mitchell, D.B.; Both, G.W. !$#journal Virology (1990) 177:324-331 !$#title Completion of the genomic sequence of the simian rotavirus !1SA11: nucleotide sequences of segments 1, 2, and 3. !$#cross-references MUID:90281597; PMID:2162107 !$#accession C35321 !'##molecule_type genomic RNA !'##residues 1-24,'I',26-135,'G',137-387,'H',389-612,'I',614-835 ##label !1MIT !'##cross-references EMBL:X16387; NID:g61876; PIDN:CAA34423.1; !1PID:g61877 COMMENT This protein may be associated with RNA polymerase activity. GENETICS !$#map_position segment 3 CLASSIFICATION #superfamily rotavirus inner layer protein VP3 KEYWORDS core protein SUMMARY #length 835 #molecular-weight 98106 #checksum 6903 SEQUENCE /// ENTRY P3XRPC #type complete TITLE inner layer protein VP3 - porcine rotavirus C (strain Cowden) ALTERNATE_NAMES minor internal core protein VP3 ORGANISM #formal_name porcine rotavirus C DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 23-Jul-1999 ACCESSIONS C40822 REFERENCE A40822 !$#authors Bremont, M.; Juste-Lesage, P.; Chabanne-Vautherot, D.; !1Charpilienne, A.; Cohen, J. !$#journal Virology (1992) 186:684-692 !$#title Sequences of the four larger proteins of a porcine group C !1rotavirus and comparison with the equivalent group A !1rotavirus proteins. !$#cross-references MUID:92124743; PMID:1310192 !$#accession C40822 !'##molecule_type genomic RNA !'##residues 1-692 ##label BRE !'##cross-references GB:M74219; NID:g333313; PIDN:AAA99239.1; !1PID:g333314 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily rotavirus inner layer protein VP3 KEYWORDS core protein SUMMARY #length 692 #molecular-weight 81377 #checksum 3486 SEQUENCE /// ENTRY P4XRBV #type complete TITLE minor inner core protein VP4 - bluetongue virus (serotype 10, American isolate) ORGANISM #formal_name bluetongue virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 10-Nov-1995 ACCESSIONS A26862; S10537 REFERENCE A26862 !$#authors Yu, Y.; Fukusho, A.; Roy, P. !$#journal Nucleic Acids Res. (1987) 15:7206 !$#title Nucleotide sequence of the VP4 core protein gene (M4 RNA) of !1US bluetongue virus serotype 10. !$#cross-references MUID:88015582; PMID:2821504 !$#accession A26862 !'##molecule_type genomic RNA !'##residues 1-654 ##label YUY REFERENCE S10534 !$#authors Roy, P.; Marshall, J.J.A.; French, T.J. !$#journal Curr. Top. Microbiol. Immunol. (1990) 162:43-87 !$#title Structure of the bluetongue virus genome and its encoded !1proteins. !$#cross-references MUID:90345726; PMID:2166648 !$#accession S10537 !'##status preliminary !'##molecule_type genomic RNA !'##residues 1-654 ##label ROY GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily bluetongue virus core protein VP4 KEYWORDS core protein SUMMARY #length 654 #molecular-weight 76432 #checksum 8272 SEQUENCE /// ENTRY P8XR10 #type complete TITLE nonstructural protein NS3 - bluetongue virus (serotype 10) ALTERNATE_NAMES nonstructural protein P8; nonstructural protein VP8 CONTAINS nonstructural protein NS3a ORGANISM #formal_name bluetongue virus DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 23-Jul-1999 ACCESSIONS A29153; S10543 REFERENCE A29153 !$#authors Lee, J.W.; Roy, P. !$#journal J. Gen. Virol. (1986) 67:2833-2837 !$#title Nucleotide sequence of a cDNA clone of RNA segment 10 of !1bluetongue virus (serotype 10). !$#cross-references MUID:87085500; PMID:3025349 !$#accession A29153 !'##molecule_type genomic RNA !'##residues 1-229 ##label LEE !'##cross-references GB:M28981; NID:g323172; PIDN:AAA42840.1; !1PID:g323173 REFERENCE S10534 !$#authors Roy, P.; Marshall, J.J.A.; French, T.J. !$#journal Curr. Top. Microbiol. Immunol. (1990) 162:43-87 !$#title Structure of the bluetongue virus genome and its encoded !1proteins. !$#cross-references MUID:90345726; PMID:2166648 !$#contents annotation GENETICS !$#map_position segment 10 CLASSIFICATION #superfamily bluetongue virus nonstructural protein P8 KEYWORDS alternative initiators; nonstructural protein FEATURE !$1-229 #product nonstructural protein NS3 #status predicted !8#label MAT1\ !$14-229 #product nonstructural protein NS3a #status predicted !8#label MAT2 SUMMARY #length 229 #molecular-weight 25602 #checksum 7834 SEQUENCE /// ENTRY P8XRAU #type complete TITLE nonstructural protein P8 - bluetongue virus (serotype 1, strain Australia) ORGANISM #formal_name bluetongue virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 16-Jun-2000 ACCESSIONS A28600 REFERENCE A28600 !$#authors Gould, A.R. !$#journal J. Gen. Virol. (1988) 69:945-949 !$#title Nucleotide sequence of the Australian bluetongue virus !1serotype 1 RNA segment 10. !$#cross-references MUID:88187687; PMID:2833571 !$#accession A28600 !'##molecule_type genomic RNA !'##residues 1-229 ##label GOU !'##cross-references GB:D00253; NID:g221069; PIDN:BAA00184.1; !1PID:g221070 GENETICS !$#map_position segment 10 CLASSIFICATION #superfamily bluetongue virus nonstructural protein P8 KEYWORDS nonstructural protein SUMMARY #length 229 #molecular-weight 25501 #checksum 6767 SEQUENCE /// ENTRY P8XRBH #type complete TITLE nonstructural protein NS3 - Broadhaven virus ORGANISM #formal_name Broadhaven virus DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 08-Apr-1994 ACCESSIONS A42457 REFERENCE A42457 !$#authors Moss, S.R.; Jones, L.D.; Nuttall, P.A. !$#journal Virology (1992) 187:841-844 !$#title Comparison of the nonstructural protein, NS3, of tick-borne !1and insect-borne orbiviruses. !$#cross-references MUID:92188563; PMID:1312282 !$#accession A42457 !'##molecule_type genomic RNA !'##residues 1-205 ##label MOS !'##cross-references GB:M83197 GENETICS !$#map_position segment 10 CLASSIFICATION #superfamily bluetongue virus nonstructural protein P8 KEYWORDS nonstructural protein SUMMARY #length 205 #molecular-weight 22043 #checksum 6105 SEQUENCE /// ENTRY MNXRS1 #type complete TITLE nonstructural protein NS1 - bluetongue virus (serotype 10, American isolate) ORGANISM #formal_name bluetongue virus DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 23-Jul-1999 ACCESSIONS A26863; S10539 REFERENCE A26863 !$#authors Lee, J.; Roy, P. !$#journal Nucleic Acids Res. (1987) 15:7207 !$#title Complete sequence of the NS1 gene (M6 RNA) of US bluetongue !1virus serotype 10. !$#cross-references MUID:88015583; PMID:2821505 !$#accession A26863 !'##molecule_type genomic RNA !'##residues 1-552 ##label LEE !'##cross-references GB:Y00422; NID:g58753; PIDN:CAA68484.1; PID:g58754 REFERENCE S10534 !$#authors Roy, P.; Marshall, J.J.A.; French, T.J. !$#journal Curr. Top. Microbiol. Immunol. (1990) 162:43-87 !$#title Structure of the bluetongue virus genome and its encoded !1proteins. !$#cross-references MUID:90345726; PMID:2166648 !$#accession S10539 !'##status preliminary !'##molecule_type genomic RNA !'##residues 1-552 ##label ROY GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily bluetongue virus nonstructural protein NS1 KEYWORDS nonstructural protein SUMMARY #length 552 #molecular-weight 64444 #checksum 3589 SEQUENCE /// ENTRY A44277 #type complete TITLE nonstructural protein NS1 - bluetongue virus (serotype 2) ORGANISM #formal_name bluetongue virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 26-Feb-1999 ACCESSIONS A44277 REFERENCE A44277 !$#authors Hwang, G.Y.; Chiou, J.F.; Yang, Y.Y.; Li, J.K.K. !$#journal Virology (1993) 192:321-327 !$#title High-sequence conservation among the United States !1bluetongue viruses cognate M2 genes which encode the !1nonstructural NS1 tubule protein. !$#cross-references MUID:93297121; PMID:8390758 !$#accession A44277 !'##molecule_type genomic RNA !'##residues 1-552 ##label HWA !'##cross-references GB:M97680 GENETICS !$#map_position segment 5 CLASSIFICATION #superfamily bluetongue virus nonstructural protein NS1 KEYWORDS nonstructural protein SUMMARY #length 552 #molecular-weight 64545 #checksum 4602 SEQUENCE /// ENTRY B44277 #type complete TITLE nonstructural protein NS1 - bluetongue virus (serotype 11) ORGANISM #formal_name bluetongue virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 26-Feb-1999 ACCESSIONS B44277 REFERENCE A44277 !$#authors Hwang, G.Y.; Chiou, J.F.; Yang, Y.Y.; Li, J.K.K. !$#journal Virology (1993) 192:321-327 !$#title High-sequence conservation among the United States !1bluetongue viruses cognate M2 genes which encode the !1nonstructural NS1 tubule protein. !$#cross-references MUID:93297121; PMID:8390758 !$#accession B44277 !'##molecule_type genomic RNA !'##residues 1-552 ##label HWA !'##cross-references GB:M97681 GENETICS !$#map_position segment 5 CLASSIFICATION #superfamily bluetongue virus nonstructural protein NS1 KEYWORDS nonstructural protein SUMMARY #length 552 #molecular-weight 64580 #checksum 4442 SEQUENCE /// ENTRY C44277 #type complete TITLE nonstructural protein NS1 - bluetongue virus (serotype 13) ORGANISM #formal_name bluetongue virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 23-Jul-1999 ACCESSIONS C44277 REFERENCE A44277 !$#authors Hwang, G.Y.; Chiou, J.F.; Yang, Y.Y.; Li, J.K.K. !$#journal Virology (1993) 192:321-327 !$#title High-sequence conservation among the United States !1bluetongue viruses cognate M2 genes which encode the !1nonstructural NS1 tubule protein. !$#cross-references MUID:93297121; PMID:8390758 !$#accession C44277 !'##molecule_type genomic RNA !'##residues 1-552 ##label HWA !'##cross-references GB:M97762; NID:g210866; PIDN:AAA02484.1; !1PID:g210867 GENETICS !$#map_position segment 5 CLASSIFICATION #superfamily bluetongue virus nonstructural protein NS1 KEYWORDS nonstructural protein SUMMARY #length 552 #molecular-weight 64517 #checksum 4188 SEQUENCE /// ENTRY B60000 #type complete TITLE nonstructural protein NS1 - bluetongue virus (serotype 1, strain South Africa) ORGANISM #formal_name bluetongue virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 30-Sep-1993 ACCESSIONS B60000 REFERENCE A60000 !$#authors Gould, A.R.; Pritchard, L.I.; Tavaria, M.D. !$#journal Virus Res. (1988) 11:97-107 !$#title Nucleotide and deduced amino acid sequences of the !1non-structural protein, NS1, of Australian and South African !1bluetongue virus serotype 1. !$#cross-references MUID:89073916; PMID:2849255 !$#accession B60000 !'##molecule_type genomic RNA !'##residues 1-552 ##label GOU GENETICS !$#map_position segment 5 CLASSIFICATION #superfamily bluetongue virus nonstructural protein NS1 KEYWORDS nonstructural protein SUMMARY #length 552 #molecular-weight 64507 #checksum 7398 SEQUENCE /// ENTRY A60000 #type complete TITLE nonstructural protein NS1 - bluetongue virus (serotype 1, strain Australia) ORGANISM #formal_name bluetongue virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 30-Sep-1993 ACCESSIONS A60000 REFERENCE A60000 !$#authors Gould, A.R.; Pritchard, L.I.; Tavaria, M.D. !$#journal Virus Res. (1988) 11:97-107 !$#title Nucleotide and deduced amino acid sequences of the !1non-structural protein, NS1, of Australian and South African !1bluetongue virus serotype 1. !$#cross-references MUID:89073916; PMID:2849255 !$#accession A60000 !'##molecule_type genomic RNA !'##residues 1-552 ##label GOU GENETICS !$#map_position segment 5 CLASSIFICATION #superfamily bluetongue virus nonstructural protein NS1 KEYWORDS nonstructural protein SUMMARY #length 552 #molecular-weight 64593 #checksum 3918 SEQUENCE /// ENTRY A48553 #type complete TITLE nonstructural protein NS1 - bluetongue virus (serotype 20, strain Australis) ORGANISM #formal_name bluetongue virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 23-Jul-1999 ACCESSIONS A48553; S25105 REFERENCE A48553 !$#authors Cowley, J.A. !$#journal Virus Genes (1992) 6:387-392 !$#title Nucleotide sequence of the genome segment encoding !1nonstructural protein NS1 of bluetongue virus serotype 20 !1from Australia. !$#cross-references MUID:93118247; PMID:1335630 !$#accession A48553 !'##molecule_type genomic RNA !'##residues 1-552 ##label COW !'##cross-references EMBL:X56735; NID:g58757; PIDN:CAA40059.1; !1PID:g58758 !'##note submitted to the EMBL Data Library, November 1990 !'##note sequence extracted from NCBI backbone (NCBIP:121635) GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily bluetongue virus nonstructural protein NS1 KEYWORDS nonstructural protein SUMMARY #length 552 #molecular-weight 64511 #checksum 4292 SEQUENCE /// ENTRY JQ1640 #type complete TITLE nonstructural protein NS1 - African horse sickness virus (serotype 4) ORGANISM #formal_name African horse sickness virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jun-2000 ACCESSIONS JQ1640 REFERENCE JQ1640 !$#authors Mizukoshi, N.; Sakamoto, K.; Iwata, A.; Tsuchiya, T.; Ueda, !1S.; Watanabe, T.; Kamada, M.; Fukusho, A. !$#journal J. Gen. Virol. (1992) 73:2425-2428 !$#title The complete sequence of African horsesickness virus !1serotype 4 (vaccine strain) RNA segment 5 and its predicted !1polypeptide compared with NS1 of bluetongue virus. !$#cross-references MUID:93019068; PMID:1328499 !$#accession JQ1640 !'##molecule_type genomic RNA !'##residues 1-548 ##label MIZ !'##cross-references GB:D11390; NID:g221008; PIDN:BAA01986.1; !1PID:g221009 GENETICS !$#map_position segment 5 CLASSIFICATION #superfamily bluetongue virus nonstructural protein NS1 KEYWORDS nonstructural protein SUMMARY #length 548 #molecular-weight 63122 #checksum 1801 SEQUENCE /// ENTRY MNXRS2 #type complete TITLE nonstructural protein NS2 (version 1) - bluetongue virus (serotype 10) ORGANISM #formal_name bluetongue virus DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 23-Jul-1999 ACCESSIONS S02112 REFERENCE S02112 !$#authors Hall, S.J.; van Dijk, A.A.; Huismans, H. !$#journal Nucleic Acids Res. (1989) 17:457 !$#title Complete nucleotide sequence of gene segment 8 encoding !1non-structural protein NS2 of SA bluetongue virus serotype !110. !$#cross-references MUID:89098415; PMID:2536152 !$#accession S02112 !'##status translation not shown !'##molecule_type genomic RNA !'##residues 1-357 ##label HAL !'##cross-references EMBL:X13374; NID:g58743; PIDN:CAA31749.1; !1PID:g58744 GENETICS !$#map_position segment 8 CLASSIFICATION #superfamily bluetongue virus nonstructural protein NS2 KEYWORDS nonstructural protein; phosphoprotein SUMMARY #length 357 #molecular-weight 41149 #checksum 5367 SEQUENCE /// ENTRY JC1256 #type complete TITLE nonstructural protein NS2 - bluetongue virus (serotype 1, strain South Africa) ORGANISM #formal_name bluetongue virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 23-Jul-1999 ACCESSIONS JC1256; S26659 REFERENCE JC1256 !$#authors Wade-Evans, A.M. !$#journal Gene (1992) 118:295-296 !$#title The complete sequence of genome segment 8 of bluetongue !1virus, serotype 1, which encodes the nonstructural protein, !1NS2. !$#cross-references MUID:92380519; PMID:1324875 !$#accession JC1256 !'##molecule_type mRNA !'##residues 1-357 ##label WAD !'##cross-references EMBL:X58064; NID:g58770; PIDN:CAA41095.1; !1PID:g58771 COMMENT This protein binds single-stranded RNA. GENETICS !$#map_position segment 8 CLASSIFICATION #superfamily bluetongue virus nonstructural protein NS2 KEYWORDS nonstructural protein; RNA binding SUMMARY #length 357 #molecular-weight 41289 #checksum 5875 SEQUENCE /// ENTRY MNXRC3 #type complete TITLE nonstructural protein NS2 (version 2) - bluetongue virus (serotype 10) ORGANISM #formal_name bluetongue virus DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 10-Nov-1995 ACCESSIONS A32400; S10541 REFERENCE A32400 !$#authors Fukusho, A.; Yu, Y.; Yamaguchi, S.; Roy, P. !$#journal J. Gen. Virol. (1989) 70:1677-1689 !$#title Completion of the sequence of bluetongue virus serotype 10 !1by the characterization of a structural protein, VP6, and a !1non-structural protein, NS2. !$#cross-references MUID:89293076; PMID:2544660 !$#accession A32400 !'##molecule_type genomic RNA !'##residues 1-357 ##label FUK REFERENCE S10534 !$#authors Roy, P.; Marshall, J.J.A.; French, T.J. !$#journal Curr. Top. Microbiol. Immunol. (1990) 162:43-87 !$#title Structure of the bluetongue virus genome and its encoded !1proteins. !$#cross-references MUID:90345726; PMID:2166648 !$#accession S10541 !'##status preliminary !'##molecule_type genomic RNA !'##residues 1-357 ##label ROY GENETICS !$#map_position segment 8 CLASSIFICATION #superfamily bluetongue virus nonstructural protein NS2 KEYWORDS nonstructural protein; phosphoprotein SUMMARY #length 357 #molecular-weight 40998 #checksum 6680 SEQUENCE /// ENTRY A60015 #type complete TITLE nonstructural protein NS2 - bluetongue virus (serotype 17, strain North America) ORGANISM #formal_name bluetongue virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 30-Sep-1993 ACCESSIONS A60015 REFERENCE A60015 !$#authors Grubman, M.J.; Zellner, M.; Samal, S. !$#journal Virus Res. (1990) 15:243-250 !$#title Nucleotide and deduced amino acid sequence of the !1nonstructural phosphoprotein, NS2, of bluetongue virus !1serotype 17: comparison to two isolates of serotype 10. !$#cross-references MUID:90261334; PMID:2160765 !$#accession A60015 !'##molecule_type DNA !'##residues 1-354 ##label GRU GENETICS !$#map_position segment 8 CLASSIFICATION #superfamily bluetongue virus nonstructural protein NS2 KEYWORDS nonstructural protein SUMMARY #length 354 #molecular-weight 40584 #checksum 4305 SEQUENCE /// ENTRY MNXRAH #type complete TITLE nonstructural protein NS2 - African horse sickness virus (serotype 9) ORGANISM #formal_name African horse sickness virus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 23-Jul-1999 ACCESSIONS A40788 REFERENCE A40788 !$#authors van Staden, V.; Theron, J.; Greyling, B.J.; Huismans, H.; !1Nel, L.H. !$#journal Virology (1991) 185:500-504 !$#title A comparison of the nucleotide sequences of cognate NS2 !1genes of three different orbiviruses. !$#cross-references MUID:92024120; PMID:1656603 !$#accession A40788 !'##molecule_type genomic RNA !'##residues 1-365 ##label VAN !'##cross-references GB:M69090; NID:g210058; PIDN:AAA42540.1; !1PID:g210059 GENETICS !$#map_position segment 8 CLASSIFICATION #superfamily bluetongue virus nonstructural protein NS2 KEYWORDS nonstructural protein; RNA binding SUMMARY #length 365 #molecular-weight 41193 #checksum 8178 SEQUENCE /// ENTRY MNXREH #type complete TITLE nonstructural protein NS2 - epizootic hemorrhagic disease virus (serotype 2, strain Alberta) ORGANISM #formal_name epizootic hemorrhagic disease virus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 23-Jul-1999 ACCESSIONS B40788 REFERENCE A40788 !$#authors van Staden, V.; Theron, J.; Greyling, B.J.; Huismans, H.; !1Nel, L.H. !$#journal Virology (1991) 185:500-504 !$#title A comparison of the nucleotide sequences of cognate NS2 !1genes of three different orbiviruses. !$#cross-references MUID:92024120; PMID:1656603 !$#accession B40788 !'##molecule_type genomic RNA !'##residues 1-376 ##label VAN !'##cross-references GB:M69091; NID:g323733; PIDN:AAA43001.1; !1PID:g323734 GENETICS !$#map_position segment 8 CLASSIFICATION #superfamily bluetongue virus nonstructural protein NS2 KEYWORDS nonstructural protein; RNA binding SUMMARY #length 376 #molecular-weight 43615 #checksum 9491 SEQUENCE /// ENTRY MNXRW4 #type complete TITLE nonstructural protein Pns4 - wound tumor virus ORGANISM #formal_name wound tumor virus, WTV DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 23-Jul-1999 ACCESSIONS A32442 REFERENCE A94397 !$#authors Anzola, J.V.; Dall, D.J.; Xu, Z.; Nuss, D.L. !$#journal Virology (1989) 171:222-228 !$#title Complete nucleotide sequence of wound tumor virus genomic !1segments encoding nonstructural polypeptides. !$#cross-references MUID:89299461; PMID:2525838 !$#accession A32442 !'##molecule_type genomic RNA !'##residues 1-732 ##label ANZ !'##cross-references GB:M24117; GB:J04352; NID:g336183; PIDN:AAA48506.1; !1PID:g336184 GENETICS !$#map_position segment S4 CLASSIFICATION #superfamily wound tumor virus nonstructural protein Pns4 KEYWORDS glycoprotein; nonstructural protein FEATURE !$90,94,124,537,546 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 732 #molecular-weight 81129 #checksum 1553 SEQUENCE /// ENTRY A45342 #type complete TITLE nonstructural protein Pns4 - rice dwarf virus ORGANISM #formal_name rice dwarf virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 23-Jul-1999 ACCESSIONS A45342 REFERENCE A45342 !$#authors Suzuki, N.; Watanabe, Y.; Kusano, T.; Kitagawa, Y. !$#journal Virology (1990) 179:446-454 !$#title Sequence analysis of rice dwarf phytoreovirus genome !1segments S4, S5, and S6: comparison with the equivalent !1wound tumor virus segments. !$#cross-references MUID:91021049; PMID:2219732 !$#accession A45342 !'##molecule_type genomic RNA !'##residues 1-727 ##label SUZ !'##cross-references GB:X54622; NID:g61469; PIDN:CAA38442.1; PID:g61470 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily wound tumor virus nonstructural protein Pns4 KEYWORDS glycoprotein; nonstructural protein FEATURE !$2,94,138,161,176, !$283,402,537,600,644 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 727 #molecular-weight 79836 #checksum 5336 SEQUENCE /// ENTRY MNXRW7 #type complete TITLE nonstructural protein Pns7 - wound tumor virus ORGANISM #formal_name wound tumor virus, WTV DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 23-Jul-1999 ACCESSIONS B32442 REFERENCE A94397 !$#authors Anzola, J.V.; Dall, D.J.; Xu, Z.; Nuss, D.L. !$#journal Virology (1989) 171:222-228 !$#title Complete nucleotide sequence of wound tumor virus genomic !1segments encoding nonstructural polypeptides. !$#cross-references MUID:89299461; PMID:2525838 !$#accession B32442 !'##molecule_type genomic RNA !'##residues 1-520 ##label ANZ !'##cross-references GB:M24116; GB:J04352; NID:g336185; PIDN:AAA48507.1; !1PID:g336186 GENETICS !$#map_position segment S6 CLASSIFICATION #superfamily wound tumor virus nonstructural protein Pns7 KEYWORDS glycoprotein; nonstructural protein FEATURE !$63,104,119,225,312, !$469 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 520 #molecular-weight 58748 #checksum 1594 SEQUENCE /// ENTRY C45342 #type complete TITLE nonstructural protein Pns7 - rice dwarf virus ORGANISM #formal_name rice dwarf virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 08-Apr-1994 ACCESSIONS C45342 REFERENCE A45342 !$#authors Suzuki, N.; Watanabe, Y.; Kusano, T.; Kitagawa, Y. !$#journal Virology (1990) 179:446-454 !$#title Sequence analysis of rice dwarf phytoreovirus genome !1segments S4, S5, and S6: comparison with the equivalent !1wound tumor virus segments. !$#cross-references MUID:91021049; PMID:2219732 !$#accession C45342 !'##molecule_type genomic RNA !'##residues 1-509 ##label SUZ !'##cross-references GB:X54622 GENETICS !$#map_position segment 6 CLASSIFICATION #superfamily wound tumor virus nonstructural protein Pns7 KEYWORDS glycoprotein; nonstructural protein FEATURE !$341,475,492 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 509 #molecular-weight 57402 #checksum 4354 SEQUENCE /// ENTRY MNXRWT #type complete TITLE nonstructural protein Pns10 - wound tumor virus ORGANISM #formal_name wound tumor virus, WTV DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 23-Jul-1999 ACCESSIONS C32442 REFERENCE A94397 !$#authors Anzola, J.V.; Dall, D.J.; Xu, Z.; Nuss, D.L. !$#journal Virology (1989) 171:222-228 !$#title Complete nucleotide sequence of wound tumor virus genomic !1segments encoding nonstructural polypeptides. !$#cross-references MUID:89299461; PMID:2525838 !$#accession C32442 !'##molecule_type genomic RNA !'##residues 1-345 ##label ANZ !'##cross-references GB:M24115; GB:J04352; NID:g336179; PIDN:AAA48504.1; !1PID:g336180 GENETICS !$#map_position segment S9 CLASSIFICATION #superfamily wound tumor virus nonstructural protein Pns10 KEYWORDS glycoprotein; nonstructural protein FEATURE !$67,114,232 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 345 #molecular-weight 38610 #checksum 4593 SEQUENCE /// ENTRY MNXRWE #type complete TITLE nonstructural protein Pns11 - wound tumor virus ORGANISM #formal_name wound tumor virus, WTV DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 23-Jul-1999 ACCESSIONS D32442 REFERENCE A94397 !$#authors Anzola, J.V.; Dall, D.J.; Xu, Z.; Nuss, D.L. !$#journal Virology (1989) 171:222-228 !$#title Complete nucleotide sequence of wound tumor virus genomic !1segments encoding nonstructural polypeptides. !$#cross-references MUID:89299461; PMID:2525838 !$#accession D32442 !'##molecule_type genomic RNA !'##residues 1-347 ##label ANZ !'##cross-references GB:M24114; GB:J04352; NID:g336181; PIDN:AAA48505.1; !1PID:g336182 GENETICS !$#map_position segment S10 CLASSIFICATION #superfamily wound tumor virus nonstructural protein Pns11 KEYWORDS glycoprotein; nonstructural protein FEATURE !$35,44 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 347 #molecular-weight 38966 #checksum 1581 SEQUENCE /// ENTRY MNXRWW #type complete TITLE nonstructural protein Pns12 - wound tumor virus ORGANISM #formal_name wound tumor virus, WTV DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 23-Jul-1999 ACCESSIONS A33387 REFERENCE A33387 !$#authors Asamizu, T.; Summers, D.; Motika, M.B.; Anzola, J.V.; Nuss, !1D.L. !$#journal Virology (1985) 144:398-409 !$#title Molecular cloning and characterization of the genome of !1wound tumor virus: a tumor-inducing plant reovirus. !$#cross-references MUID:86045962; PMID:3840622 !$#accession A33387 !'##molecule_type genomic RNA !'##residues 1-178 ##label ASA !'##cross-references GB:M11133; NID:g336187; PIDN:AAA48508.1; !1PID:g336188 GENETICS !$#map_position segment S12 CLASSIFICATION #superfamily wound tumor virus nonstructural protein Pns12 KEYWORDS glycoprotein; nonstructural protein FEATURE !$128,129,132,166 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 178 #molecular-weight 19196 #checksum 2529 SEQUENCE /// ENTRY MNXR12 #type complete TITLE nonstructural protein Pns12 - wound tumor virus (strain NJ) ALTERNATE_NAMES segment 12 protein A ORGANISM #formal_name wound tumor virus, WTV DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 23-Jul-1999 ACCESSIONS A41705 REFERENCE A41705 !$#authors Hillman, B.I.; Anzola, J.V.; Halpern, B.T.; Cavileer, T.D.; !1Nuss, D.L. !$#journal Virology (1991) 185:896-900 !$#title First field isolation of wound tumor virus from a plant !1host: minimal sequence divergence from the type strain !1isolated from an insect vector. !$#cross-references MUID:92074261; PMID:1962460 !$#accession A41705 !'##molecule_type genomic RNA !'##residues 1-178 ##label HIL !'##cross-references GB:M77021; NID:g336174; PIDN:AAA48501.1; !1PID:g336175 GENETICS !$#map_position segment 12 CLASSIFICATION #superfamily wound tumor virus nonstructural protein Pns12 KEYWORDS glycoprotein; nonstructural protein FEATURE !$87,128,129,132,166 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 178 #molecular-weight 19284 #checksum 2847 SEQUENCE /// ENTRY MNXRRD #type complete TITLE nonstructural protein P11 - rice dwarf virus ORGANISM #formal_name rice dwarf virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jun-2000 ACCESSIONS JQ1364 REFERENCE JQ1364 !$#authors Suzuki, N.; Harada, M.; Kusano, T. !$#journal J. Gen. Virol. (1991) 72:2233-2237 !$#title Molecular analysis of rice dwarf phytoreovirus segment S11 !1corresponding to wound tumour phytoreovirus segment S12. !$#cross-references MUID:91374022; PMID:1840611 !$#accession JQ1364 !'##molecule_type genomic RNA !'##residues 1-181 ##label SUZ !'##cross-references GB:D10249; GB:D90199; NID:g222484; PIDN:BAA01094.1; !1PID:g222485 GENETICS !$#map_position segment S11 CLASSIFICATION #superfamily wound tumor virus nonstructural protein Pns12 KEYWORDS nonstructural protein SUMMARY #length 181 #molecular-weight 19988 #checksum 6121 SEQUENCE /// ENTRY WMXRWT #type complete TITLE core protein P6 - wound tumor virus ORGANISM #formal_name wound tumor virus, WTV DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 23-Jul-1999 ACCESSIONS A34010 REFERENCE A34010 !$#authors Anzola, J.V.; Xu, Z.; Nuss, D.L. !$#journal Nucleic Acids Res. (1989) 17:3300 !$#title Complete nucleotide sequence of wound tumor virus genomic !1segment S7. !$#cross-references MUID:89263744; PMID:2726467 !$#accession A34010 !'##molecule_type genomic RNA !'##residues 1-519 ##label ANZ !'##cross-references GB:X14218; NID:g62266; PIDN:CAA32438.1; PID:g62267 GENETICS !$#map_position segment 7 CLASSIFICATION #superfamily wound tumor virus core protein P6 KEYWORDS core protein SUMMARY #length 519 #molecular-weight 57630 #checksum 9562 SEQUENCE /// ENTRY WMXRWN #type complete TITLE core protein P6 - wound tumor virus (strain NJ) ALTERNATE_NAMES segment 7 protein ORGANISM #formal_name wound tumor virus, WTV DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 08-Apr-1994 ACCESSIONS D41705 REFERENCE A41705 !$#authors Hillman, B.I.; Anzola, J.V.; Halpern, B.T.; Cavileer, T.D.; !1Nuss, D.L. !$#journal Virology (1991) 185:896-900 !$#title First field isolation of wound tumor virus from a plant !1host: minimal sequence divergence from the type strain !1isolated from an insect vector. !$#cross-references MUID:92074261; PMID:1962460 !$#accession D41705 !'##molecule_type genomic RNA !'##residues 1-519 ##label HIL !'##cross-references GB:M77019 GENETICS !$#map_position segment 7 CLASSIFICATION #superfamily wound tumor virus core protein P6 KEYWORDS core protein SUMMARY #length 519 #molecular-weight 57600 #checksum 7995 SEQUENCE /// ENTRY VPXSN1 #type complete TITLE VP5 protein - infectious pancreatic necrosis virus (strain N1) ORGANISM #formal_name infectious pancreatic necrosis virus DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jun-2000 ACCESSIONS A34148 REFERENCE A34148 !$#authors Havarstein, L.S.; Kalland, K.H.; Christie, K.E.; Endresen, !1C. !$#journal J. Gen. Virol. (1990) 71:299-308 !$#title Sequence of the large double-stranded RNA segment of the N1 !1strain of infectious pancreatic necrosis virus: a comparison !1with other Birnaviridae. !$#cross-references MUID:90171914; PMID:2307963 !$#accession A34148 !'##molecule_type genomic RNA !'##residues 1-148 ##label HAV !'##cross-references EMBL:D00701; NID:g221910; PIDN:BAA00608.1; !1PID:g221911 GENETICS !$#map_position segment A CLASSIFICATION #superfamily birnavirus VP5 protein SUMMARY #length 148 #molecular-weight 17033 #checksum 8008 SEQUENCE /// ENTRY GNXSAU #type complete TITLE genome polyprotein - infectious bursal disease virus (strain 002-73) CONTAINS major structural protein VP2; minor structural protein VP3; nonstructural protein VP4 ORGANISM #formal_name infectious bursal disease virus DATE 31-Mar-1988 #sequence_revision 30-Jun-1991 #text_change 12-Apr-1996 ACCESSIONS A24382; A24860 REFERENCE A24382 !$#authors Hudson, P.J.; McKern, N.M.; Power, B.E.; Azad, A.A. !$#journal Nucleic Acids Res. (1986) 14:5001-5012 !$#title Genomic structure of the large RNA segment of infectious !1bursal disease virus. !$#cross-references MUID:86259073; PMID:3014441 !$#accession A24382 !'##molecule_type genomic RNA !'##residues 1-1012 ##label HUD GENETICS !$#map_position segment A CLASSIFICATION #superfamily birnavirus segment A genome polyprotein KEYWORDS nonstructural protein; polyprotein; structural protein FEATURE !$1-588 #product major structural protein VP2 #status !8predicted #label VP2\ !$589-760 #product nonstructural protein VP4 #status predicted !8#label VP4\ !$761-1012 #product minor structural protein VP3 #status !8predicted #label VP3 SUMMARY #length 1012 #molecular-weight 109502 #checksum 2194 SEQUENCE /// ENTRY GNXSIR #type complete TITLE genome polyprotein - infectious bursal disease virus (strain STC) CONTAINS major structural protein VP2; minor structural protein VP3; nonstructural protein VP4 ORGANISM #formal_name infectious bursal disease virus DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jun-2000 ACCESSIONS JS0360 REFERENCE JS0359 !$#authors Kibenge, F.S.B.; Jackwood, D.J.; Mercado, C.C. !$#journal J. Gen. Virol. (1990) 71:569-577 !$#title Nucleotide sequence analysis of genome segment A of !1infectious bursal disease virus. !$#cross-references MUID:90188302; PMID:2155995 !$#accession JS0360 !'##molecule_type genomic RNA !'##residues 1-1012 ##label KIB !'##cross-references GB:D00499; NID:g221891; PIDN:BAA00391.1; !1PID:g221893 GENETICS !$#map_position segment A CLASSIFICATION #superfamily birnavirus segment A genome polyprotein KEYWORDS nonstructural protein; polyprotein; structural protein FEATURE !$2-588 #product major structural protein VP2 #status !8predicted #label VP2\ !$589-760 #product nonstructural protein VP4 #status predicted !8#label VP4\ !$761-1012 #product minor structural protein VP3 #status !8predicted #label VP3 SUMMARY #length 1012 #molecular-weight 109500 #checksum 9883 SEQUENCE /// ENTRY GNXS52 #type complete TITLE genome polyprotein - infectious bursal disease virus (strain 52/70) CONTAINS major structural protein VP2; minor structural protein VP3; nonstructural protein VP4 ORGANISM #formal_name infectious bursal disease virus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 08-Apr-1994 ACCESSIONS JQ0941 REFERENCE JQ0941 !$#authors Bayliss, C.D.; Spies, U.; Shaw, K.; Peters, R.W.; !1Papageorgiou, A.; Mueller, H.; Boursnell, M.E.G. !$#journal J. Gen. Virol. (1990) 71:1303-1312 !$#title A comparison of the sequences of segment A of four !1infectious bursal disease virus strains and identification !1of a variable region in VP2. !$#cross-references MUID:90278420; PMID:2161902 !$#accession JQ0941 !'##molecule_type genomic RNA !'##residues 1-1012 ##label BAY !'##cross-references GB:D00867 GENETICS !$#map_position segment A CLASSIFICATION #superfamily birnavirus segment A genome polyprotein KEYWORDS nonstructural protein; polyprotein; structural protein FEATURE !$1-452 #product major structural protein VP2 #status !8predicted #label VP2\ !$453-722 #product nonstructural protein VP4 #status predicted !8#label VP4\ !$723-1012 #product minor structural protein VP3 #status !8predicted #label VP3 SUMMARY #length 1012 #molecular-weight 109567 #checksum 152 SEQUENCE /// ENTRY GNXS98 #type complete TITLE genome polyprotein - infectious bursal disease virus (strain PBG98) CONTAINS major structural protein VP2; minor structural protein VP3; nonstructural protein VP4 ORGANISM #formal_name infectious bursal disease virus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 08-Apr-1994 ACCESSIONS JQ0944 REFERENCE JQ0941 !$#authors Bayliss, C.D.; Spies, U.; Shaw, K.; Peters, R.W.; !1Papageorgiou, A.; Mueller, H.; Boursnell, M.E.G. !$#journal J. Gen. Virol. (1990) 71:1303-1312 !$#title A comparison of the sequences of segment A of four !1infectious bursal disease virus strains and identification !1of a variable region in VP2. !$#cross-references MUID:90278420; PMID:2161902 !$#accession JQ0944 !'##molecule_type genomic RNA !'##residues 1-993 ##label BAY !'##cross-references GB:D00867 GENETICS !$#map_position segment A CLASSIFICATION #superfamily birnavirus segment A genome polyprotein KEYWORDS nonstructural protein; polyprotein; structural protein FEATURE !$1-433 #product major structural protein VP2 #status !8predicted #label VP2\ !$434-703 #product nonstructural protein VP4 #status predicted !8#label VP4\ !$704-993 #product minor structural protein VP3 #status !8predicted #label VP3 SUMMARY #length 993 #molecular-weight 107531 #checksum 1621 SEQUENCE /// ENTRY GNXSCU #type complete TITLE genome polyprotein - infectious bursal disease virus (strain Cu-1) CONTAINS major structural protein VP2; minor structural protein VP3; nonstructural protein VP4 ORGANISM #formal_name infectious bursal disease virus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jun-2000 ACCESSIONS A35353; S06091 REFERENCE JQ0941 !$#authors Bayliss, C.D.; Spies, U.; Shaw, K.; Peters, R.W.; !1Papageorgiou, A.; Mueller, H.; Boursnell, M.E.G. !$#journal J. Gen. Virol. (1990) 71:1303-1312 !$#title A comparison of the sequences of segment A of four !1infectious bursal disease virus strains and identification !1of a variable region in VP2. !$#cross-references MUID:90278420; PMID:2161902 !$#accession A35353 !'##molecule_type genomic RNA !'##residues 1-1012 ##label BAY !'##cross-references GB:D00867; NID:g221894; PIDN:BAA00740.1; !1PID:g221895 REFERENCE S06090 !$#authors Spies, U.; Mueller, H.; Becht, H. !$#journal Nucleic Acids Res. (1989) 17:7982 !$#title Nucleotide sequence of infectious bursal disease virus !1genome segment A delineates two major open reading frames. !$#cross-references MUID:90016880; PMID:2552417 !$#accession S06091 !'##status translation not shown !'##molecule_type genomic RNA !'##residues 1-1012 ##label SPI !'##cross-references EMBL:X16107; NID:g60444; PIDN:CAA34234.1; !1PID:g60446 GENETICS !$#map_position segment A CLASSIFICATION #superfamily birnavirus segment A genome polyprotein KEYWORDS nonstructural protein; polyprotein; structural protein FEATURE !$1-452 #product major structural protein VP2 #status !8predicted #label VP2\ !$453-722 #product nonstructural protein VP4 #status predicted !8#label VP4\ !$723-1012 #product minor structural protein VP3 #status !8predicted #label VP3 SUMMARY #length 1012 #molecular-weight 109680 #checksum 1381 SEQUENCE /// ENTRY GNXSIE #type fragment TITLE genome polyprotein - infectious bursal disease virus (strain E) (fragment) CONTAINS major structural protein VP2; nonstructural protein VP4 ORGANISM #formal_name infectious bursal disease virus #note host Gallus gallus (chicken) DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jun-2000 ACCESSIONS PQ0283 REFERENCE PQ0283 !$#authors Heine, H.G.; Haritou, M.; Failla, P.; Fahey, K.; Azad, A. !$#journal J. Gen. Virol. (1991) 72:1835-1843 !$#title Sequence analysis and expression of the host-protective !1immunogen VP2 of a variant strain of infectious bursal !1disease virus which can circumvent vaccination with standard !1type I strains. !$#cross-references MUID:91341469; PMID:1651980 !$#accession PQ0283 !'##molecule_type genomic RNA !'##residues 1-496 ##label HEI !'##cross-references GB:D10065; NID:g221889; PIDN:BAA00954.1; !1PID:g221890 COMMENT This virus is responsible for a severe immunodepressive !1disease in young chickens. GENETICS !$#map_position segment A CLASSIFICATION #superfamily birnavirus segment A genome polyprotein KEYWORDS nonstructural protein; polyprotein; structural protein FEATURE !$1-452 #product structural protein VP2 #status predicted !8#label VP2\ !$453-496 #product nonstructural protein VP4 (fragment) #status !8predicted #label VP4 SUMMARY #length 496 #checksum 439 SEQUENCE /// ENTRY GNXSOH #type complete TITLE genome polyprotein - infectious bursal disease virus (strain OH) CONTAINS major structural protein VP2; minor structural protein VP3; nonstructural protein VP4 ORGANISM #formal_name infectious bursal disease virus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 23-Jul-1999 ACCESSIONS A40569 REFERENCE A40569 !$#authors Kibenge, F.S.; McKenna, P.K.; Dybing, J.K. !$#journal Virology (1991) 184:437-440 !$#title Genome cloning and analysis of the large RNA segment !1(segment A) of a naturally avirulent serotype 2 infectious !1bursal disease virus. !$#cross-references MUID:91335781; PMID:1651602 !$#accession A40569 !'##status translation not shown !'##molecule_type genomic RNA !'##residues 1-1012 ##label KIB !'##cross-references GB:M66722; NID:g331203; PIDN:AAA46239.1; !1PID:g331204 GENETICS !$#map_position segment A CLASSIFICATION #superfamily birnavirus segment A genome polyprotein KEYWORDS nonstructural protein; polyprotein; structural protein FEATURE !$1-453 #product major structural protein VP2 #status !8predicted #label VP2\ !$454-722 #product nonstructural protein VP4 #status predicted !8#label VP4\ !$723-1012 #product minor structural protein VP3 #status !8predicted #label VP3 SUMMARY #length 1012 #molecular-weight 109865 #checksum 3953 SEQUENCE /// ENTRY GNXSIV #type complete TITLE genome polyprotein - infectious pancreatic necrosis virus (strain Jasper) ORGANISM #formal_name infectious pancreatic necrosis virus DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 31-Dec-1996 ACCESSIONS A23599 REFERENCE A23599 !$#authors Duncan, R.; Dobos, P. !$#journal Nucleic Acids Res. (1986) 14:5934 !$#title The nucleotide sequence of infectious pancreatic necrosis !1virus (IPNV) dsRNA segment A reveals one large ORF encoding !1a precursor polyprotein. !$#cross-references MUID:86286599; PMID:3737418 !$#accession A23599 !'##molecule_type genomic RNA !'##residues 1-972 ##label DUN GENETICS !$#map_position segment A CLASSIFICATION #superfamily birnavirus segment A genome polyprotein KEYWORDS polyprotein FEATURE !$2-570 #product major structural protein VP2 #status !8predicted #label VP2\ !$571-739 #product nonstructural protein VP4 #status predicted !8#label VP4\ !$740-972 #product minor structural protein VP3 #status !8predicted #label VP3 SUMMARY #length 972 #molecular-weight 106623 #checksum 8317 SEQUENCE /// ENTRY GNXSN1 #type complete TITLE genome polyprotein - infectious pancreatic necrosis virus (strain N1) CONTAINS major structural protein VP2; minor structural protein VP3; nonstructural protein NS ORGANISM #formal_name infectious pancreatic necrosis virus DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 16-Jun-2000 ACCESSIONS B34148 REFERENCE A34148 !$#authors Havarstein, L.S.; Kalland, K.H.; Christie, K.E.; Endresen, !1C. !$#journal J. Gen. Virol. (1990) 71:299-308 !$#title Sequence of the large double-stranded RNA segment of the N1 !1strain of infectious pancreatic necrosis virus: a comparison !1with other Birnaviridae. !$#cross-references MUID:90171914; PMID:2307963 !$#accession B34148 !'##molecule_type genomic RNA !'##residues 1-972 ##label HAV !'##cross-references EMBL:D00701; NID:g221910; PIDN:BAA00609.1; !1PID:g221912 !'##note the precise cleavage sites were not determined GENETICS !$#map_position segment A CLASSIFICATION #superfamily birnavirus segment A genome polyprotein KEYWORDS polyprotein FEATURE !$2-570 #product major structural protein VP2 #status !8predicted #label VP2\ !$571-739 #product nonstructural protein VP4 #status predicted !8#label VP4\ !$740-972 #product minor structural protein VP3 #status !8predicted #label VP3 SUMMARY #length 972 #molecular-weight 106669 #checksum 7283 SEQUENCE /// ENTRY QQXPGP #type complete TITLE surface glycoprotein polyprotein - Pichinde virus ORGANISM #formal_name Pichinde virus DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 23-Jul-1999 ACCESSIONS A04149 REFERENCE A93005 !$#authors Auperin, D.D.; Romanowski, V.; Galinski, M.; Bishop, D.H.L. !$#journal J. Virol. (1984) 52:897-904 !$#title Sequencing studies of Pichinde arenavirus S RNA indicate a !1novel coding strategy, and ambisense viral S RNA. !$#cross-references MUID:85033957; PMID:6492264 !$#accession A04149 !'##molecule_type genomic RNA !'##residues 1-503 ##label AUP !'##cross-references GB:K02734; NID:g332643; PIDN:AAA46824.1; !1PID:g332644 COMMENT The genome consists of two species of RNA, designated S !1(small) RNA and L (large) RNA. This protein is coded by S !1RNA. COMMENT Specific enzymatic cleavage may yield mature glycoproteins !1G1 and G2. However, the exact cleavage site is undetermined. CLASSIFICATION #superfamily arenavirus surface glycoprotein KEYWORDS glycoprotein FEATURE !$67,74,89,100,111, !$116,121,132,181, !$241,379,387,404, !$409,499 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 503 #molecular-weight 57278 #checksum 1944 SEQUENCE /// ENTRY VGXPJV #type complete TITLE surface glycoprotein polyprotein - Junin virus (strain MC2) CONTAINS glycoprotein G1; glycoprotein G2 ORGANISM #formal_name Junin virus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jun-2000 ACCESSIONS JT0978 REFERENCE JT0978 !$#authors Ghiringhelli, P.D.; Rivera-Pomar, R.V.; Lozano, M.E.; Grau, !1O.; Romanowski, V. !$#journal J. Gen. Virol. (1991) 72:2129-2141 !$#title Molecular organization of Junin virus S RNA: complete !1nucleotide sequence, relationship with other members of the !1Arenaviridae and unusual secondary structures. !$#cross-references MUID:91374010; PMID:1654373 !$#accession JT0978 !'##molecule_type genomic RNA !'##residues 1-481 ##label GHI !'##cross-references GB:D10072; NID:g221963; PIDN:BAA00964.1; !1PID:g221964 GENETICS !$#map_position segment S CLASSIFICATION #superfamily arenavirus surface glycoprotein KEYWORDS glycoprotein; polyprotein FEATURE !$1-243 #product glycoprotein G1 #status predicted #label !8GG1\ !$244-481 #product glycoprotein G2 #status predicted #label !8GG2\ !$91,101,162,174,353, !$361,378,383 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 481 #molecular-weight 55118 #checksum 9654 SEQUENCE /// ENTRY VGXPTV #type complete TITLE surface glycoprotein polyprotein - Tacaribe virus CONTAINS surface glycoprotein G1; surface glycoprotein G2 ORGANISM #formal_name Tacaribe virus DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 08-Apr-1994 ACCESSIONS JQ1453 REFERENCE JQ1453 !$#authors Allison, L.M.C.; Salter, M.W.A.P.; Kiguwa, S.; Howard, C.R. !$#journal J. Gen. Virol. (1991) 72:2025-2029 !$#title Analysis of the glycoprotein gene of Tacaribe virus and !1neutralization-resistant variants. !$#cross-references MUID:91341495; PMID:1875197 !$#accession JQ1453 !'##molecule_type genomic RNA !'##residues 1-483 ##label ALL GENETICS !$#map_position segment S CLASSIFICATION #superfamily arenavirus surface glycoprotein KEYWORDS glycoprotein; membrane protein; polyprotein FEATURE !$1-245 #product surface glycoprotein G1 #status predicted !8#label GG1\ !$20-36 #region hydrophobic\ !$38-54 #region hydrophobic\ !$246-483 #product surface glycoprotein G2 #status predicted !8#label GG2\ !$83,95,164,176,355, !$363,380,385 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 483 #molecular-weight 55602 #checksum 4216 SEQUENCE /// ENTRY VGXPT5 #type complete TITLE surface glycoprotein polyprotein - Tacaribe virus (strain V5) CONTAINS surface glycoprotein G1; surface glycoprotein G2 ORGANISM #formal_name Tacaribe virus DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 08-Apr-1994 ACCESSIONS JQ1454 REFERENCE JQ1453 !$#authors Allison, L.M.C.; Salter, M.W.A.P.; Kiguwa, S.; Howard, C.R. !$#journal J. Gen. Virol. (1991) 72:2025-2029 !$#title Analysis of the glycoprotein gene of Tacaribe virus and !1neutralization-resistant variants. !$#cross-references MUID:91341495; PMID:1875197 !$#accession JQ1454 !'##molecule_type genomic RNA !'##residues 1-483 ##label ALL GENETICS !$#map_position segment S CLASSIFICATION #superfamily arenavirus surface glycoprotein KEYWORDS glycoprotein; membrane protein; polyprotein FEATURE !$1-245 #product surface glycoprotein G1 #status predicted !8#label GG1\ !$20-36 #region hydrophobic\ !$38-54 #region hydrophobic\ !$246-483 #product surface glycoprotein G2 #status predicted !8#label GG2\ !$83,95,164,176,355, !$363,380,385 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 483 #molecular-weight 55598 #checksum 5351 SEQUENCE /// ENTRY VGXPT7 #type complete TITLE surface glycoprotein polyprotein - Tacaribe virus (strain V7) CONTAINS surface glycoprotein G1; surface glycoprotein G2 ORGANISM #formal_name Tacaribe virus DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 08-Apr-1994 ACCESSIONS JQ1455 REFERENCE JQ1453 !$#authors Allison, L.M.C.; Salter, M.W.A.P.; Kiguwa, S.; Howard, C.R. !$#journal J. Gen. Virol. (1991) 72:2025-2029 !$#title Analysis of the glycoprotein gene of Tacaribe virus and !1neutralization-resistant variants. !$#cross-references MUID:91341495; PMID:1875197 !$#accession JQ1455 !'##molecule_type genomic RNA !'##residues 1-482 ##label ALL !'##note the authors translated the codon AUU for residue 431 as Thr GENETICS !$#map_position segment S CLASSIFICATION #superfamily arenavirus surface glycoprotein KEYWORDS glycoprotein; membrane protein; polyprotein FEATURE !$1-245 #product surface glycoprotein G1 #status predicted !8#label GG1\ !$20-36 #region hydrophobic\ !$38-54 #region hydrophobic\ !$246-482 #product surface glycoprotein G2 #status predicted !8#label GG2\ !$83,95,164,176,354, !$362,379,384 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 482 #molecular-weight 55607 #checksum 2278 SEQUENCE /// ENTRY VGXPLV #type complete TITLE surface glycoprotein polyprotein - Lassa virus (strain Josiah) CONTAINS glycoprotein G1; glycoprotein G2 ORGANISM #formal_name Lassa virus #note host Mastomys natalensis (multimammate rat) DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 23-Jul-1999 ACCESSIONS A24296; B31294 REFERENCE A24296 !$#authors Auperin, D.D.; Sasso, D.R.; McCormick, J.B. !$#journal Virology (1986) 154:155-167 !$#title Nucleotide sequence of the glycoprotein gene and intergenic !1region of the Lassa virus S genome RNA. !$#cross-references MUID:86317709; PMID:3750844 !$#accession A24296 !'##molecule_type genomic RNA !'##residues 1-491 ##label AUP !'##cross-references GB:M15076; NID:g331410; PIDN:AAA46283.1; !1PID:g331411 REFERENCE A31294 !$#authors Auperin, D.D.; McCormick, J.B. !$#journal Virology (1989) 168:421-425 !$#title Nucleotide sequence of the Lassa virus (Josiah strain) S !1genome RNA and amino acid sequence comparison of the N and !1GPC proteins to other arenaviruses. !$#cross-references MUID:89130959; PMID:2916333 !$#accession B31294 !'##status preliminary !'##molecule_type genomic RNA !'##residues 1-491 ##label AU2 !'##cross-references GB:J04324; NID:g331414; PIDN:AAA46286.1; !1PID:g331416 COMMENT The genome consists of two species of RNA, designated as S !1(small) RNA and L (large) RNA. This protein is coded by S !1RNA. COMMENT Specific enzymatic cleavage may yield mature glycoproteins !1G1 and G2; however, the exact cleavage site is undetermined. GENETICS !$#map_position segment S RNA CLASSIFICATION #superfamily arenavirus surface glycoprotein KEYWORDS glycoprotein FEATURE !$79,89,99,109,119, !$167,224,365,373, !$390,395 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 491 #molecular-weight 55813 #checksum 7584 SEQUENCE /// ENTRY A43492 #type complete TITLE surface glycoprotein polyprotein - Lassa virus (strain GA391, Nigeria) CONTAINS surface glycoprotein G1; surface glycoprotein G2 ORGANISM #formal_name Lassa virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 23-Jul-1999 ACCESSIONS A43492; S10904 REFERENCE A43492 !$#authors Clegg, J.C.S.; Wilson, S.M.; Oram, J.D. !$#journal Virus Res. (1990) 18:151-164 !$#title Nucleotide sequence of the S RNA of Lassa virus (Nigerian !1strain) and comparative analysis of arenavirus gene !1products. !$#accession A43492 !'##molecule_type genomic RNA !'##residues 1-490 ##label CLE !'##cross-references GB:X52400; GB:M36544; NID:g58641; PIDN:CAA36645.1; !1PID:g58642 GENETICS !$#map_position segment S CLASSIFICATION #superfamily arenavirus surface glycoprotein KEYWORDS glycoprotein; polyprotein; transmembrane protein FEATURE !$1-255 #product surface glycoprotein G1 #status predicted !8#label SG1\ !$256-490 #product surface glycoprotein G2 #status predicted !8#label SG2\ !$433-449 #domain transmembrane #status predicted #label TMN\ !$78,88,98,108,118, !$166,223,364,372, !$389,394 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 490 #molecular-weight 55839 #checksum 4565 SEQUENCE /// ENTRY VGXPMV #type complete TITLE surface glycoprotein polyprotein - Mopeia virus (strain 800150) CONTAINS glycoprotein G1; glycoprotein G2 ORGANISM #formal_name Mopeia virus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 23-Jul-1999 ACCESSIONS A38546 REFERENCE A38546 !$#authors Wilson, S.M.; Clegg, J.C.S. !$#journal Virology (1991) 180:543-552 !$#title Sequence analysis of the S RNA of the African arenavirus !1Mopeia: an unusual secondary structure feature in the !1intergenic region. !$#cross-references MUID:91111973; PMID:1989384 !$#accession A38546 !'##molecule_type genomic RNA !'##residues 1-489 ##label WIL !'##cross-references GB:M33879; NID:g332155; PIDN:AAC08700.1; !1PID:g332156 GENETICS !$#map_position segment S CLASSIFICATION #superfamily arenavirus surface glycoprotein KEYWORDS glycoprotein; polyprotein FEATURE !$1-254 #product glycoprotein G1 #status predicted #label !8GG1\ !$255-489 #product glycoprotein G2 #status predicted #label !8GG2\ !$78,88,98,108,118, !$166,222,363,371, !$388,393 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 489 #molecular-weight 55987 #checksum 953 SEQUENCE /// ENTRY VGXPLC #type complete TITLE surface glycoprotein polyprotein - lymphocytic choriomeningitis virus CONTAINS glycoprotein G1; glycoprotein G2 ORGANISM #formal_name lymphocytic choriomeningitis virus DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 23-Jul-1999 ACCESSIONS A23481 REFERENCE A94399 !$#authors Romanowski, V.; Matsuura, Y.; Bishop, D.H.L. !$#journal Virus Res. (1985) 3:101-114 !$#title Complete sequence of the S RNA of lymphocytic !1choriomeningitis virus (WE strain) compared to that of !1pichinde arenavirus. !$#cross-references MUID:86046554; PMID:4060885 !$#accession A23481 !'##molecule_type genomic RNA !'##residues 1-498 ##label ROM !'##cross-references GB:M22138; NID:g331379; PIDN:AAA46265.1; !1PID:g331380 !'##experimental_source strain WE COMMENT The genome consists of two species of RNA, designated S !1(small) RNA and L (large) RNA. This protein is coded by S !1RNA. COMMENT Specific enzymatic cleavage may yield mature glycoproteins !1G1 and G2; however, the exact cleavage site is undetermined. GENETICS !$#map_position segment S CLASSIFICATION #superfamily arenavirus surface glycoprotein KEYWORDS glycoprotein FEATURE !$85,95,114,124,171, !$232,371,396,401 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 498 #molecular-weight 56280 #checksum 6272 SEQUENCE /// ENTRY VGXPLM #type complete TITLE surface glycoprotein polyprotein - lymphocytic choriomeningitis virus (strain Armstrong) CONTAINS glycoprotein G1; glycoprotein G2 ORGANISM #formal_name lymphocytic choriomeningitis virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 12-Apr-1996 ACCESSIONS B26345 REFERENCE A94356 !$#authors Southern, P.J.; Singh, M.K.; Riviere, Y.; Jacoby, D.R.; !1Buchmeier, M.J.; Oldstone, M.B.A. !$#journal Virology (1987) 157:145-155 !$#title Molecular characterization of the genomic S RNA segment from !1lymphocytic choriomeningitis virus. !$#cross-references MUID:87151103; PMID:3824905 !$#accession B26345 !'##molecule_type genomic RNA !'##residues 1-498 ##label SOU COMMENT The genome consists of two species of RNA, designated S !1(small) RNA and L (large) RNA. This protein is coded by S !1RNA. GENETICS !$#map_position segment S CLASSIFICATION #superfamily arenavirus surface glycoprotein KEYWORDS glycoprotein FEATURE !$1-262 #product glycoprotein G1 #status predicted #label !8GP1\ !$263-498 #product glycoprotein G2 #status predicted #label !8GP2\ !$85,95,114,124,171, !$232,371,396,401 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 498 #molecular-weight 56130 #checksum 4604 SEQUENCE /// ENTRY VGXPLA #type complete TITLE surface glycoprotein polyprotein - lymphocytic choriomeningitis virus (strain Armstrong 53b, CTL positive) CONTAINS glycoprotein G1; glycoprotein G2 ORGANISM #formal_name lymphocytic choriomeningitis virus DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 23-Jul-1999 ACCESSIONS A28920 REFERENCE A28920 !$#authors Salvato, M.; Shimomaye, E.; Southern, P.; Oldstone, M.B.A. !$#journal Virology (1988) 164:517-522 !$#title Virus-lymphocyte interactions. IV. Molecular !1characterization of LCMV Armstrong (CTL+) small genomic !1segment and that of its variant, clone 13 (CTL-). !$#cross-references MUID:88219540; PMID:3259346 !$#accession A28920 !'##molecule_type genomic RNA !'##residues 1-498 ##label SAL !'##cross-references GB:M20869; NID:g331358; PIDN:AAA46256.1; !1PID:g331359 !'##note the CTL negative clone 13 differs from that shown in having !1260-Leu COMMENT The genome consists of two segments of RNA, small (S) and !1large (L). This protein is coded by S RNA. GENETICS !$#map_position segment S CLASSIFICATION #superfamily arenavirus surface glycoprotein KEYWORDS glycoprotein; polyprotein FEATURE !$1-262 #product glycoprotein G1 #status predicted #label !8GG1\ !$263-498 #product glycoprotein G2 #status predicted #label !8GG2\ !$85,95,114,124,171, !$232,371,396,401 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 498 #molecular-weight 56215 #checksum 4706 SEQUENCE /// ENTRY VHXPNP #type complete TITLE major structural nucleoprotein N - Pichinde virus ORGANISM #formal_name Pichinde virus DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 23-Jul-1999 ACCESSIONS A04150 REFERENCE A93005 !$#authors Auperin, D.D.; Romanowski, V.; Galinski, M.; Bishop, D.H.L. !$#journal J. Virol. (1984) 52:897-904 !$#title Sequencing studies of Pichinde arenavirus S RNA indicate a !1novel coding strategy, and ambisense viral S RNA. !$#cross-references MUID:85033957; PMID:6492264 !$#accession A04150 !'##molecule_type genomic RNA !'##residues 1-561 ##label AUP !'##cross-references GB:K02734; NID:g332643; PIDN:AAA46825.1; !1PID:g332645 COMMENT The genome consists of two species of RNA, designated S !1(small) RNA and L (large) RNA. This protein is coded by S !1RNA. CLASSIFICATION #superfamily arenavirus major nucleoprotein KEYWORDS nucleoprotein SUMMARY #length 561 #molecular-weight 62983 #checksum 8193 SEQUENCE /// ENTRY VHXPLC #type complete TITLE major structural nucleoprotein N - lymphocytic choriomeningitis virus ORGANISM #formal_name lymphocytic choriomeningitis virus DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 08-Apr-1994 ACCESSIONS B23481 REFERENCE A94399 !$#authors Romanowski, V.; Matsuura, Y.; Bishop, D.H.L. !$#journal Virus Res. (1985) 3:101-114 !$#title Complete sequence of the S RNA of lymphocytic !1choriomeningitis virus (WE strain) compared to that of !1pichinde arenavirus. !$#cross-references MUID:86046554; PMID:4060885 !$#accession B23481 !'##molecule_type genomic RNA !'##residues 1-558 ##label ROM !'##experimental_source strain WE COMMENT The genome consists of two species of RNA, designated S !1(small) RNA and L (large) RNA. This protein is coded by S !1RNA. GENETICS !$#map_position segment S CLASSIFICATION #superfamily arenavirus major nucleoprotein KEYWORDS nucleoprotein SUMMARY #length 558 #molecular-weight 62152 #checksum 5372 SEQUENCE /// ENTRY VHXPLM #type complete TITLE major structural nucleoprotein N - lymphocytic choriomeningitis virus (strain Armstrong) ORGANISM #formal_name lymphocytic choriomeningitis virus DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 23-Jul-1999 ACCESSIONS A26345; B28920 REFERENCE A94356 !$#authors Southern, P.J.; Singh, M.K.; Riviere, Y.; Jacoby, D.R.; !1Buchmeier, M.J.; Oldstone, M.B.A. !$#journal Virology (1987) 157:145-155 !$#title Molecular characterization of the genomic S RNA segment from !1lymphocytic choriomeningitis virus. !$#cross-references MUID:87151103; PMID:3824905 !$#accession A26345 !'##molecule_type genomic RNA !'##residues 1-558 ##label SOU !'##cross-references GB:M20869; NID:g331358; PIDN:AAA46257.1; !1PID:g331360 REFERENCE A28920 !$#authors Salvato, M.; Shimomaye, E.; Southern, P.; Oldstone, M.B.A. !$#journal Virology (1988) 164:517-522 !$#title Virus-lymphocyte interactions. IV. Molecular !1characterization of LCMV Armstrong (CTL+) small genomic !1segment and that of its variant, clone 13 (CTL-). !$#cross-references MUID:88219540; PMID:3259346 !$#contents annotation COMMENT The genome consists of two species of RNA, designated S !1(small) RNA and L (large) RNA. This protein is coded by S !1RNA. GENETICS !$#map_position segment S CLASSIFICATION #superfamily arenavirus major nucleoprotein KEYWORDS nucleoprotein SUMMARY #length 558 #molecular-weight 62177 #checksum 5257 SEQUENCE /// ENTRY VHXPLJ #type complete TITLE major structural nucleoprotein N - Lassa virus (strain Josiah) ORGANISM #formal_name Lassa virus DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 23-Jul-1999 ACCESSIONS A31294 REFERENCE A31294 !$#authors Auperin, D.D.; McCormick, J.B. !$#journal Virology (1989) 168:421-425 !$#title Nucleotide sequence of the Lassa virus (Josiah strain) S !1genome RNA and amino acid sequence comparison of the N and !1GPC proteins to other arenaviruses. !$#cross-references MUID:89130959; PMID:2916333 !$#accession A31294 !'##molecule_type genomic RNA !'##residues 1-569 ##label AUP !'##cross-references GB:J04324; NID:g331414; PIDN:AAA46285.1; !1PID:g331415 GENETICS !$#map_position segment S CLASSIFICATION #superfamily arenavirus major nucleoprotein KEYWORDS nucleoprotein SUMMARY #length 569 #molecular-weight 62998 #checksum 756 SEQUENCE /// ENTRY VHXPL2 #type complete TITLE major structural nucleoprotein N - Lassa virus (strain GA391, Nigeria) ALTERNATE_NAMES nucleocapsid protein ORGANISM #formal_name Lassa virus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 24-Jul-1997 ACCESSIONS B43492; S10905 REFERENCE A43492 !$#authors Clegg, J.C.S.; Wilson, S.M.; Oram, J.D. !$#journal Virus Res. (1990) 18:151-164 !$#title Nucleotide sequence of the S RNA of Lassa virus (Nigerian !1strain) and comparative analysis of arenavirus gene !1products. !$#accession B43492 !'##molecule_type genomic RNA !'##residues 1-570 ##label CLE !'##cross-references GB:M36544 GENETICS !$#map_position segment S CLASSIFICATION #superfamily arenavirus major nucleoprotein KEYWORDS nucleocapsid; nucleoprotein SUMMARY #length 570 #molecular-weight 62913 #checksum 3635 SEQUENCE /// ENTRY VHXPMV #type complete TITLE major structural nucleoprotein - Machupo virus ALTERNATE_NAMES nucleocapsid protein ORGANISM #formal_name Machupo virus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 23-Jul-1999 ACCESSIONS S18042 REFERENCE S18042 !$#authors Griffiths, C.; Wilson, S.M.; Clegg, J.C.S. !$#submission submitted to the EMBL Data Library, October 1991 !$#description Sequence of the nucleocapsid gene of Machupo virus: close !1relationship with another South American pathogenic !1arenavirus, Junin. !$#accession S18042 !'##molecule_type genomic RNA !'##residues 1-564 ##label GRI !'##cross-references EMBL:X62616; NID:g60621; PIDN:CAA44486.1; !1PID:g60622 GENETICS !$#map_position segment S CLASSIFICATION #superfamily arenavirus major nucleoprotein KEYWORDS nucleocapsid; nucleoprotein SUMMARY #length 564 #molecular-weight 63299 #checksum 9818 SEQUENCE /// ENTRY VHXPJV #type complete TITLE major structural nucleoprotein N - Junin virus (strain MC2) ORGANISM #formal_name Junin virus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 08-Apr-1994 ACCESSIONS JQ1268 REFERENCE JT0978 !$#authors Ghiringhelli, P.D.; Rivera-Pomar, R.V.; Lozano, M.E.; Grau, !1O.; Romanowski, V. !$#journal J. Gen. Virol. (1991) 72:2129-2141 !$#title Molecular organization of Junin virus S RNA: complete !1nucleotide sequence, relationship with other members of the !1Arenaviridae and unusual secondary structures. !$#cross-references MUID:91374010; PMID:1654373 !$#accession JQ1268 !'##molecule_type genomic RNA !'##residues 1-564 ##label GHI GENETICS !$#map_position segment S CLASSIFICATION #superfamily arenavirus major nucleoprotein KEYWORDS nucleoprotein SUMMARY #length 564 #molecular-weight 63013 #checksum 2877 SEQUENCE /// ENTRY B38546 #type complete TITLE major structural nucleoprotein N - Mopeia virus (strain 800150) ORGANISM #formal_name Mopeia virus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 23-Jul-1999 ACCESSIONS B38546 REFERENCE A38546 !$#authors Wilson, S.M.; Clegg, J.C.S. !$#journal Virology (1991) 180:543-552 !$#title Sequence analysis of the S RNA of the African arenavirus !1Mopeia: an unusual secondary structure feature in the !1intergenic region. !$#cross-references MUID:91111973; PMID:1989384 !$#accession B38546 !'##molecule_type genomic RNA !'##residues 1-570 ##label WIL !'##cross-references GB:M33879; NID:g332155; PIDN:AAC08701.1; !1PID:g332157 GENETICS !$#map_position segment S CLASSIFICATION #superfamily arenavirus major nucleoprotein KEYWORDS nucleoprotein SUMMARY #length 570 #molecular-weight 63434 #checksum 2909 SEQUENCE /// ENTRY ZNXPLC #type complete TITLE zinc finger protein - lymphocytic choriomeningitis virus (strain Armstrong 53b) ORGANISM #formal_name lymphocytic choriomeningitis virus DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 23-Jul-1999 ACCESSIONS A32592 REFERENCE A32592 !$#authors Salvato, M.S.; Shimomaye, E.M. !$#journal Virology (1989) 173:1-10 !$#title The completed sequence of lymphocytic choriomeningitis virus !1reveals a unique RNA structure and a gene for a zinc finger !1protein. !$#cross-references MUID:90051057; PMID:2510401 !$#accession A32592 !'##molecule_type genomic RNA !'##residues 1-90 ##label SAL !'##cross-references GB:M27693; NID:g331385; PIDN:AAA46268.1; !1PID:g331386 COMMENT This protein may act as an RNA-binding protein. GENETICS !$#map_position segment L CLASSIFICATION #superfamily arenavirus zinc finger protein KEYWORDS RNA binding; zinc finger FEATURE !$32-54 #region zinc finger CCCC motif SUMMARY #length 90 #molecular-weight 10184 #checksum 9608 SEQUENCE /// ENTRY A46313 #type complete TITLE zinc finger protein - Tacaribe virus ALTERNATE_NAMES P11 protein ORGANISM #formal_name Tacaribe virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 23-Jul-1999 ACCESSIONS A46313 REFERENCE A46313 !$#authors Iapalucci, S.; Lopez, N.; Rey, O.; Zakin, M.M.; Cohen, G.N.; !1Franze-Fernandez, M.T. !$#journal Virology (1989) 173:357-361 !$#title The 5' region of Tacaribe virus L RNA encodes a protein with !1a potential metal binding domain. !$#cross-references MUID:90051092; PMID:2510403 !$#accession A46313 !'##molecule_type genomic RNA !'##residues 1-95 ##label IAP !'##cross-references GB:J04340; GB:M33513; NID:g335147; PIDN:AAA47900.1; !1PID:g335148 COMMENT This protein may act as an RNA-binding protein. GENETICS !$#map_position segment L CLASSIFICATION #superfamily arenavirus zinc finger protein KEYWORDS RNA binding; zinc finger FEATURE !$40-76 #region zinc finger SUMMARY #length 95 #molecular-weight 10850 #checksum 1752 SEQUENCE /// ENTRY MNWWHE #type complete TITLE genome polyprotein - hepatitis E virus (strain Burma) CONTAINS RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name hepatitis E virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 23-Jul-1999 ACCESSIONS A40778; A48547 REFERENCE A40778 !$#authors Tam, A.W.; Smith, M.M.; Guerra, M.E.; Huang, C.C.; Bradley, !1D.W.; Fry, K.E.; Reyes, G.R. !$#journal Virology (1991) 185:120-131 !$#title Hepatitis E virus (HEV): molecular cloning and sequencing of !1the full-length viral genome. !$#cross-references MUID:92024067; PMID:1926770 !$#accession A40778 !'##molecule_type genomic RNA !'##residues 1-1693 ##label TAM !'##cross-references GB:M73218; NID:g330023; PIDN:AAA45734.1; !1PID:g330024 REFERENCE A48547 !$#authors Fry, K.E.; Tam, A.W.; Smith, M.M.; Kim, J.P.; Luk, K.C.; !1Young, L.M.; Piatak, M.; Feldman, R.A.; Yun, K.Y.; Purdy, !1M.A.; McCaustland, K.A.; Bradley, D.W.; Reyes, G.R. !$#journal Virus Genes (1992) 6:173-185 !$#title Hepatitis E virus (HEV): strain variation in the !1nonstructural gene region encoding consensus motifs for an !1RNA-dependent RNA polymerase and an ATP/GTP binding site. !$#cross-references MUID:92271462; PMID:1589964 !$#accession A48547 !'##molecule_type genomic RNA !'##residues 967-1693 ##label FRY !'##cross-references GB:M32400; NID:g330021; PIDN:AAA03206.1; !1PID:g330022 !'##note sequence extracted from NCBI backbone (NCBIN:104572, !1NCBIP:104573) CLASSIFICATION #superfamily hepatitis E virus nonstructural protein KEYWORDS ATP; nonstructural protein; nucleotidyltransferase SUMMARY #length 1693 #molecular-weight 185190 #checksum 6520 SEQUENCE /// ENTRY A44212 #type complete TITLE genome polyprotein - hepatitis E virus (strain Mexico) CONTAINS RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name hepatitis E virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 19-Jan-2001 ACCESSIONS A44212; B48547 REFERENCE A44212 !$#authors Huang, C.C.; Nguyen, D.; Fernandez, J.; Yun, K.Y.; Fry, !1K.E.; Bradley, D.W.; Tam, A.W.; Reyes, G.R. !$#journal Virology (1992) 191:550-558 !$#title Molecular cloning and sequencing of the Mexico isolate of !1hepatitis E virus (HEV). !$#cross-references MUID:93079857; PMID:1448913 !$#accession A44212 !'##molecule_type genomic RNA !'##residues 1-1691 ##label HUA !'##cross-references GB:M74506; NID:g330017; PIDN:AAA45730.1; !1PID:g330018 REFERENCE A48547 !$#authors Fry, K.E.; Tam, A.W.; Smith, M.M.; Kim, J.P.; Luk, K.C.; !1Young, L.M.; Piatak, M.; Feldman, R.A.; Yun, K.Y.; Purdy, !1M.A.; McCaustland, K.A.; Bradley, D.W.; Reyes, G.R. !$#journal Virus Genes (1992) 6:173-185 !$#title Hepatitis E virus (HEV): strain variation in the !1nonstructural gene region encoding consensus motifs for an !1RNA-dependent RNA polymerase and an ATP/GTP binding site. !$#cross-references MUID:92271462; PMID:1589964 !$#accession B48547 !'##molecule_type genomic RNA !'##residues 965-1691 ##label FRY !'##note sequence extracted from NCBI backbone (NCBIN:104576, !1NCBIP:104578) CLASSIFICATION #superfamily hepatitis E virus nonstructural protein KEYWORDS ATP; GTP binding; nonstructural protein; nucleotide binding; !1nucleotidyltransferase; P-loop FEATURE !$973-980 #region nucleotide-binding motif A (P-loop)\ !$979 #binding_site ATP/GTP (Lys) #status predicted SUMMARY #length 1691 #molecular-weight 185223 #checksum 835 SEQUENCE /// ENTRY VHWWHE #type complete TITLE structural protein 1 - hepatitis E virus (strain Burma) ORGANISM #formal_name hepatitis E virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 23-Jul-1999 ACCESSIONS B40778; A40236 REFERENCE A40778 !$#authors Tam, A.W.; Smith, M.M.; Guerra, M.E.; Huang, C.C.; Bradley, !1D.W.; Fry, K.E.; Reyes, G.R. !$#journal Virology (1991) 185:120-131 !$#title Hepatitis E virus (HEV): molecular cloning and sequencing of !1the full-length viral genome. !$#cross-references MUID:92024067; PMID:1926770 !$#accession B40778 !'##molecule_type genomic RNA !'##residues 1-123 ##label TAM !'##cross-references GB:M73218; NID:g330023; PIDN:AAA45735.1; !1PID:g330025 REFERENCE A40236 !$#authors Ray, R.; Jameel, S.; Manivel, V.; Ray, R. !$#journal Virology (1992) 189:359-362 !$#title Indian hepatitis E virus shows a major deletion in the small !1open reading frame. !$#cross-references MUID:92295577; PMID:1534953 !$#accession A40236 !'##molecule_type genomic RNA !'##residues 1-57,'P',59-102,'P',104-123 ##label RAY CLASSIFICATION #superfamily hepatitis E virus structural protein 1 KEYWORDS structural protein SUMMARY #length 123 #molecular-weight 12676 #checksum 7070 SEQUENCE /// ENTRY C44212 #type complete TITLE structural protein 1 - hepatitis E virus (strain Mexico) ORGANISM #formal_name hepatitis E virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 23-Jul-1999 ACCESSIONS C44212 REFERENCE A44212 !$#authors Huang, C.C.; Nguyen, D.; Fernandez, J.; Yun, K.Y.; Fry, !1K.E.; Bradley, D.W.; Tam, A.W.; Reyes, G.R. !$#journal Virology (1992) 191:550-558 !$#title Molecular cloning and sequencing of the Mexico isolate of !1hepatitis E virus (HEV). !$#cross-references MUID:93079857; PMID:1448913 !$#accession C44212 !'##molecule_type genomic RNA !'##residues 1-123 ##label HUA !'##cross-references GB:M74506; NID:g330017; PIDN:AAA45731.1; !1PID:g330019 CLASSIFICATION #superfamily hepatitis E virus structural protein 1 KEYWORDS structural protein SUMMARY #length 123 #molecular-weight 12714 #checksum 4107 SEQUENCE /// ENTRY B40236 #type complete TITLE structural protein 1 - hepatitis E virus (strain Indian) ORGANISM #formal_name hepatitis E virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 07-May-1999 ACCESSIONS B40236 REFERENCE A40236 !$#authors Ray, R.; Jameel, S.; Manivel, V.; Ray, R. !$#journal Virology (1992) 189:359-362 !$#title Indian hepatitis E virus shows a major deletion in the small !1open reading frame. !$#cross-references MUID:92295577; PMID:1534953 !$#accession B40236 !'##molecule_type genomic RNA !'##residues 1-41 ##label RAY CLASSIFICATION #superfamily hepatitis E virus structural protein 1 KEYWORDS structural protein SUMMARY #length 41 #molecular-weight 4428 #checksum 5460 SEQUENCE /// ENTRY VHWWH2 #type complete TITLE structural protein 2 precursor - hepatitis E virus (strain Burma) ORGANISM #formal_name hepatitis E virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 23-Jul-1999 ACCESSIONS C40778 REFERENCE A40778 !$#authors Tam, A.W.; Smith, M.M.; Guerra, M.E.; Huang, C.C.; Bradley, !1D.W.; Fry, K.E.; Reyes, G.R. !$#journal Virology (1991) 185:120-131 !$#title Hepatitis E virus (HEV): molecular cloning and sequencing of !1the full-length viral genome. !$#cross-references MUID:92024067; PMID:1926770 !$#accession C40778 !'##molecule_type genomic RNA !'##residues 1-660 ##label TAM !'##cross-references GB:M73218; NID:g330023; PIDN:AAA45736.1; !1PID:g330026 !'##note the authors translated the codon CGC for residue 2 as Ala CLASSIFICATION #superfamily hepatitis E virus structural protein 2 KEYWORDS structural protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-660 #product structural protein 2 #status predicted !8#label SP2 SUMMARY #length 660 #molecular-weight 70977 #checksum 3679 SEQUENCE /// ENTRY B44212 #type complete TITLE structural protein 2 precursor - hepatitis E virus (strain Mexico) ORGANISM #formal_name hepatitis E virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 23-Jul-1999 ACCESSIONS B44212 REFERENCE A44212 !$#authors Huang, C.C.; Nguyen, D.; Fernandez, J.; Yun, K.Y.; Fry, !1K.E.; Bradley, D.W.; Tam, A.W.; Reyes, G.R. !$#journal Virology (1992) 191:550-558 !$#title Molecular cloning and sequencing of the Mexico isolate of !1hepatitis E virus (HEV). !$#cross-references MUID:93079857; PMID:1448913 !$#accession B44212 !'##molecule_type genomic RNA !'##residues 1-659 ##label HUA !'##cross-references GB:M74506; NID:g330017; PIDN:AAA45732.1; !1PID:g330020 CLASSIFICATION #superfamily hepatitis E virus structural protein 2 KEYWORDS structural protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-659 #product structural protein 2 #status predicted !8#label SP2 SUMMARY #length 659 #molecular-weight 70640 #checksum 8511 SEQUENCE /// ENTRY VCWWFC #type complete TITLE coat protein - feline calicivirus (strain Japanese F4) ALTERNATE_NAMES capsid protein ORGANISM #formal_name feline calicivirus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jun-2000 ACCESSIONS B40481 REFERENCE A40481 !$#authors Tohya, Y.; Taniguchi, Y.; Takahashi, E.; Utagawa, E.; !1Takeda, N.; Miyamura, K.; Yamazaki, S.; Mikami, T. !$#journal Virology (1991) 183:810-814 !$#title Sequence analysis of the 3'-end of feline calicivirus !1genome. !$#cross-references MUID:91306470; PMID:1853578 !$#accession B40481 !'##molecule_type genomic RNA !'##residues 1-668 ##label TOH !'##cross-references GB:D90357; NID:g221264; PIDN:BAA14371.1; !1PID:g221266 CLASSIFICATION #superfamily feline calicivirus coat protein KEYWORDS capsid protein; coat protein; glycoprotein FEATURE !$177,301,304,399, !$459,615 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 668 #molecular-weight 73589 #checksum 3239 SEQUENCE /// ENTRY VCWWFF #type complete TITLE coat protein - feline calicivirus (strain CFI/68 FIV) ALTERNATE_NAMES capsid protein ORGANISM #formal_name feline calicivirus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 20-Aug-1999 ACCESSIONS A40507; B40507; T09246 REFERENCE A40507 !$#authors Neill, J.D.; Reardon, I.M.; Heinrikson, R.L. !$#journal J. Virol. (1991) 65:5440-5447 !$#title Nucleotide sequence and expression of the capsid protein !1gene of feline calicivirus. !$#cross-references MUID:91374597; PMID:1716692 !$#accession A40507 !'##molecule_type genomic RNA !'##residues 1-668 ##label NEI !'##cross-references GB:M32819; NID:g323874; PIDN:AAA42925.1; !1PID:g323875 !$#accession B40507 !'##molecule_type protein !'##residues 373-379;403-419;481-489;560-566 ##label NE2 REFERENCE Z16626 !$#authors Neill, J.D. !$#submission submitted to the EMBL Data Library, April 1998 !$#description Complete nucleotide sequence of feline calicivirus strain !1CFI/68. !$#accession T09246 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type genomic RNA !'##residues 1-668 ##label NE3 !'##cross-references EMBL:U13992; NID:g3056875; PIDN:AAC13993.1; !1PID:g537256 !'##experimental_source strain CFI/68 FIV CLASSIFICATION #superfamily feline calicivirus coat protein KEYWORDS capsid protein; coat protein; glycoprotein FEATURE !$177,301,304,439, !$459,615 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 668 #molecular-weight 73550 #checksum 2441 SEQUENCE /// ENTRY VCWWF9 #type complete TITLE coat protein - feline calicivirus (strain F9) ALTERNATE_NAMES capsid protein ORGANISM #formal_name feline calicivirus DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 28-Jul-2000 ACCESSIONS B43382; C45538; PQ0407; S23702 REFERENCE A43382 !$#authors Carter, M.J.; Milton, I.D.; Meanger, J.; Bennett, M.; !1Gaskell, R.M.; Turner, P.C. !$#journal Virology (1992) 190:443-448 !$#title The complete nucleotide sequence of a feline calicivirus. !$#cross-references MUID:92410623; PMID:1529544 !$#accession B43382 !'##molecule_type genomic RNA !'##residues 1-671 ##label CAR1 !'##cross-references GB:M86379; NID:g323877; PIDN:AAA79327.1; !1PID:g323879 REFERENCE A45538 !$#authors Carter, M.J.; Milton, I.D.; Turner, P.C.; Meanger, J.; !1Bennett, M.; Gaskell, R.M. !$#journal Arch. Virol. (1992) 122:223-235 !$#title Identification and sequence determination of the capsid !1protein gene of feline calicivirus. !$#cross-references MUID:92117861; PMID:1731695 !$#accession C45538 !'##molecule_type genomic RNA; protein !'##residues 1-671 ##label CAR2 !'##cross-references GB:M86379; NID:g323877; PIDN:AAA79327.1; !1PID:g323879 !'##experimental_source strain F9 !'##note sequence extracted from NCBI backbone (NCBIN:77457, !1NCBIP:77462) REFERENCE PQ0407 !$#authors Guiver, M.; Littler, E.; Caul, E.O.; Fox, A.J. !$#journal J. Gen. Virol. (1992) 73:2429-2433 !$#title The cloning, sequencing and expression of a major antigenic !1region from the feline calicivirus capsid protein. !$#cross-references MUID:93019069; PMID:1402818 !$#accession PQ0407 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 217-266,'SI',269-336,'V',338-395,'S',397-412,'A',414-521, !1'EV',524-671 ##label GUI !'##cross-references PIDN:AAB23553.1; PID:g257083 CLASSIFICATION #superfamily feline calicivirus coat protein KEYWORDS capsid protein; coat protein; glycoprotein FEATURE !$177,304,439,459,618 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 671 #molecular-weight 73441 #checksum 4147 SEQUENCE /// ENTRY A48562 #type complete TITLE coat protein - San Miguel sea lion virus (serotype 1) ALTERNATE_NAMES capsid protein ORGANISM #formal_name San Miguel sea lion virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 23-Jul-1999 ACCESSIONS A48562 REFERENCE A48562 !$#authors Neill, J.D. !$#journal Virus Res. (1992) 24:211-222 !$#title Nucleotide sequence of the capsid protein gene of two !1serotypes of San Miguel sea lion virus: identification of !1conserved and non-conserved amino acid sequences among !1calicivirus capsid proteins. !$#cross-references MUID:92410750; PMID:1529644 !$#accession A48562 !'##molecule_type genomic RNA !'##residues 1-702 ##label NEI !'##cross-references GB:M87481; NID:g334882; PIDN:AAA16217.1; !1PID:g334884 !'##note sequence extracted from NCBI backbone (NCBIN:113564, !1NCBIP:113565) CLASSIFICATION #superfamily feline calicivirus coat protein KEYWORDS capsid protein; coat protein; glycoprotein FEATURE !$208,481,493,545 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 702 #molecular-weight 77850 #checksum 1551 SEQUENCE /// ENTRY C48562 #type complete TITLE coat protein - San Miguel sea lion virus (serotype 4) ALTERNATE_NAMES capsid protein ORGANISM #formal_name San Miguel sea lion virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 23-Jul-1999 ACCESSIONS C48562 REFERENCE A48562 !$#authors Neill, J.D. !$#journal Virus Res. (1992) 24:211-222 !$#title Nucleotide sequence of the capsid protein gene of two !1serotypes of San Miguel sea lion virus: identification of !1conserved and non-conserved amino acid sequences among !1calicivirus capsid proteins. !$#cross-references MUID:92410750; PMID:1529644 !$#accession C48562 !'##molecule_type genomic RNA !'##residues 1-703 ##label NEI !'##cross-references GB:M87482; NID:g334886; PIDN:AAA16220.1; !1PID:g334888 !'##note sequence extracted from NCBI backbone (NCBIP:113567) CLASSIFICATION #superfamily feline calicivirus coat protein KEYWORDS capsid protein; coat protein; glycoprotein FEATURE !$89,208,329,463,482 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 703 #molecular-weight 77721 #checksum 3549 SEQUENCE /// ENTRY VCWWRH #type complete TITLE coat protein - rabbit hemorrhagic disease virus ALTERNATE_NAMES capsid protein ORGANISM #formal_name rabbit hemorrhagic disease virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 23-Jul-1999 ACCESSIONS B41039 REFERENCE A41039 !$#authors Meyers, G.; Wirblich, C.; Thiel, H.J. !$#journal Virology (1991) 184:664-676 !$#title Rabbit hemorrhagic disease virus--molecular cloning and !1nucleotide sequencing of a calicivirus genome. !$#cross-references MUID:91361557; PMID:1840711 !$#accession B41039 !'##molecule_type genomic RNA !'##residues 1-117 ##label MEY !'##cross-references GB:M67473; NID:g333765; PIDN:AAA47286.1; !1PID:g333767 CLASSIFICATION #superfamily rabbit calicivirus coat protein KEYWORDS capsid protein; coat protein; glycoprotein FEATURE !$103,110 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 117 #molecular-weight 12670 #checksum 4589 SEQUENCE /// ENTRY VCBB2G #type complete TITLE coat protein precursor - black beetle virus CONTAINS coat protein alpha; coat protein beta; coat protein gamma ORGANISM #formal_name black beetle virus #note host Drosophila melanogaster DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 23-Jul-1999 ACCESSIONS A04151; S11036 REFERENCE A93535 !$#authors Dasgupta, R.; Ghosh, A.; Dasmahapatra, B.; Guarino, L.A.; !1Kaesberg, P. !$#journal Nucleic Acids Res. (1984) 12:7215-7223 !$#title Primary and secondary structure of black beetle virus RNA2, !1the genomic messenger for BBV coat protein precursor. !$#cross-references MUID:85014162; PMID:6548308 !$#accession A04151 !'##molecule_type mRNA !'##residues 1-407 ##label DAS !'##cross-references GB:X00956; NID:g60681; PIDN:CAA25468.1; PID:g60682 REFERENCE S11036 !$#authors Kaesberg, P.; Dasgupta, R.; Sgro, J.Y.; Wery, J.P.; Selling, !1B.H.; Hosur, M.V.; Johnson, J.E. !$#journal J. Mol. Biol. (1990) 214:423-435 !$#title Structural homology among four nodaviruses as deduced by !1sequencing and X-ray crystallography. !$#cross-references MUID:90339486; PMID:2116525 !$#contents annotation COMMENT Of the 180 copies of the alpha chain in the mature virion, !1about eighty per cent are enzymatically cleaved into coat !1proteins beta and gamma. GENETICS !$#map_position segment 2 !$#note the genome consists of two linear, single-stranded RNAs with !1the same polarity as the mRNA CLASSIFICATION #superfamily black beetle virus coat protein KEYWORDS coat protein; RNA binding FEATURE !$1-407 #product coat protein alpha #status experimental !8#label ALP\ !$1-363 #product coat protein beta #status experimental !8#label BET\ !$35-49 #region arginine-rich RNA-binding pattern\ !$364-407 #product coat protein gamma #status experimental !8#label GAM\ !$363-364 #cleavage_site Asn-Ala (autolytic) (partial) #status !8experimental SUMMARY #length 407 #molecular-weight 43838 #checksum 8555 SEQUENCE /// ENTRY VCBBFH #type complete TITLE coat protein precursor - flock house virus CONTAINS coat protein alpha; coat protein beta; coat protein gamma ORGANISM #formal_name flock house virus DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 23-Jul-1999 ACCESSIONS B34011; S11037 REFERENCE A34011 !$#authors Dasgupta, R.; Sgro, J.Y. !$#journal Nucleic Acids Res. (1989) 17:7525-7526 !$#title Nucleotide sequences of three nodavirus RNA2's: the !1messenger for their coat protein precursors. !$#cross-references MUID:90016821; PMID:2798110 !$#accession B34011 !'##molecule_type genomic RNA !'##residues 1-407 ##label DAS !'##cross-references EMBL:X15959; NID:g59265; PIDN:CAA34081.1; !1PID:g59266 REFERENCE S11036 !$#authors Kaesberg, P.; Dasgupta, R.; Sgro, J.Y.; Wery, J.P.; Selling, !1B.H.; Hosur, M.V.; Johnson, J.E. !$#journal J. Mol. Biol. (1990) 214:423-435 !$#title Structural homology among four nodaviruses as deduced by !1sequencing and X-ray crystallography. !$#cross-references MUID:90339486; PMID:2116525 !$#contents annotation GENETICS !$#map_position segment 2 CLASSIFICATION #superfamily black beetle virus coat protein KEYWORDS coat protein; RNA binding FEATURE !$1-407 #product coat protein alpha #status predicted #label !8ALP\ !$1-363 #product coat protein beta #status predicted #label !8BET\ !$35-49 #region arginine-rich RNA-binding pattern\ !$364-407 #product coat protein gamma #status predicted #label !8GAM\ !$363-364 #cleavage_site Asn-Ala (autolytic) #status predicted SUMMARY #length 407 #molecular-weight 43709 #checksum 4034 SEQUENCE /// ENTRY VCBBBL #type complete TITLE coat protein precursor - boolarra virus CONTAINS coat protein alpha; coat protein beta; coat protein gamma ORGANISM #formal_name boolarra virus DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 23-Jul-1999 ACCESSIONS A34011; S11038 REFERENCE A34011 !$#authors Dasgupta, R.; Sgro, J.Y. !$#journal Nucleic Acids Res. (1989) 17:7525-7526 !$#title Nucleotide sequences of three nodavirus RNA2's: the !1messenger for their coat protein precursors. !$#cross-references MUID:90016821; PMID:2798110 !$#accession A34011 !'##molecule_type genomic RNA !'##residues 1-403 ##label DAS !'##cross-references EMBL:X15960; NID:g58723; PIDN:CAA34082.1; !1PID:g58724 REFERENCE S11036 !$#authors Kaesberg, P.; Dasgupta, R.; Sgro, J.Y.; Wery, J.P.; Selling, !1B.H.; Hosur, M.V.; Johnson, J.E. !$#journal J. Mol. Biol. (1990) 214:423-435 !$#title Structural homology among four nodaviruses as deduced by !1sequencing and X-ray crystallography. !$#cross-references MUID:90339486; PMID:2116525 !$#contents annotation GENETICS !$#map_position segment 2 CLASSIFICATION #superfamily black beetle virus coat protein KEYWORDS coat protein; RNA binding FEATURE !$1-403 #product coat protein alpha #status predicted #label !8ALP\ !$1-359 #product coat protein beta #status predicted #label !8BET\ !$25-34 #region arginine-rich RNA-binding pattern\ !$360-403 #product coat protein gamma #status predicted #label !8GAM\ !$359-360 #cleavage_site Asn-Ala (autolytic) #status predicted SUMMARY #length 403 #molecular-weight 43357 #checksum 2263 SEQUENCE /// ENTRY VCBBND #type complete TITLE coat protein precursor - Nodamura virus CONTAINS coat protein alpha; coat protein beta; coat protein gamma ORGANISM #formal_name Nodamura virus DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 23-Jul-1999 ACCESSIONS C34011; S11039 REFERENCE A34011 !$#authors Dasgupta, R.; Sgro, J.Y. !$#journal Nucleic Acids Res. (1989) 17:7525-7526 !$#title Nucleotide sequences of three nodavirus RNA2's: the !1messenger for their coat protein precursors. !$#cross-references MUID:90016821; PMID:2798110 !$#accession C34011 !'##molecule_type genomic RNA !'##residues 1-399 ##label DAS !'##cross-references EMBL:X15961; NID:g60685; PIDN:CAA34083.1; !1PID:g60686 REFERENCE S11036 !$#authors Kaesberg, P.; Dasgupta, R.; Sgro, J.Y.; Wery, J.P.; Selling, !1B.H.; Hosur, M.V.; Johnson, J.E. !$#journal J. Mol. Biol. (1990) 214:423-435 !$#title Structural homology among four nodaviruses as deduced by !1sequencing and X-ray crystallography. !$#cross-references MUID:90339486; PMID:2116525 !$#contents annotation GENETICS !$#map_position segment 2 CLASSIFICATION #superfamily black beetle virus coat protein KEYWORDS coat protein; RNA binding FEATURE !$1-399 #product coat protein alpha #status predicted #label !8ALP\ !$1-355 #product coat protein beta #status predicted #label !8BET\ !$29-41 #region arginine-rich RNA-binding pattern\ !$356-399 #product coat protein gamma #status predicted #label !8GAM\ !$355-356 #cleavage_site Asn-Ala (autolytic) #status predicted SUMMARY #length 399 #molecular-weight 43067 #checksum 4555 SEQUENCE /// ENTRY QQBBB1 #type complete TITLE B1 protein - black beetle virus ORGANISM #formal_name black beetle virus DATE 30-Sep-1992 #sequence_revision 22-Oct-1999 #text_change 22-Oct-1999 ACCESSIONS S78471; S28728; S28729; A23243 REFERENCE S78471 !$#authors Dasgupta, R. !$#submission submitted to the EMBL Data Library, July 1986 !$#accession S78471 !'##molecule_type genomic RNA !'##residues 1-998 ##label DAS !'##cross-references EMBL:X02396; NID:g60679; PIDN:CAA26238.1; !1PID:g60680 REFERENCE S28728 !$#authors Dasmahapatra, B.; Dasgupta, R.; Ghosh, A.; Kaesberg, P. !$#journal J. Mol. Biol. (1985) 182:183-189 !$#title Structure of the black beetle virus genome and its !1functional implications. !$#cross-references MUID:85210903; PMID:3839022 !$#accession S28728 !'##molecule_type genomic RNA !'##residues 1-883,'AALRRTPWTNRYQC' ##label DAW !'##cross-references EMBL:X02396 !$#accession S28729 !'##molecule_type genomic RNA !'##residues 897-998 ##label DA2 !'##cross-references EMBL:X02396 REFERENCE A23243 !$#authors Guarino, L.A.; Ghosh, A.; Dasmahapatra, B.; Dasgupta, R.; !1Kaesberg, P. !$#journal Virology (1984) 139:199-203 !$#title Sequence of the black beetle virus subgenomic RNA and its !1location in the viral genome. !$#cross-references MUID:85042104; PMID:6495657 !$#accession A23243 !'##molecule_type genomic RNA !'##residues 897-998 ##label GUA !'##cross-references GB:M33065; NID:g210673; PIDN:AAA42745.1; !1PID:g210674 CLASSIFICATION #superfamily black beetle virus B1 protein KEYWORDS RNA biosynthesis SUMMARY #length 998 #molecular-weight 112196 #checksum 4131 SEQUENCE /// ENTRY QQBBB2 #type complete TITLE B2 protein - black beetle virus ORGANISM #formal_name black beetle virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 23-Jul-1999 ACCESSIONS B23243; S28730 REFERENCE A23243 !$#authors Guarino, L.A.; Ghosh, A.; Dasmahapatra, B.; Dasgupta, R.; !1Kaesberg, P. !$#journal Virology (1984) 139:199-203 !$#title Sequence of the black beetle virus subgenomic RNA and its !1location in the viral genome. !$#cross-references MUID:85042104; PMID:6495657 !$#accession B23243 !'##molecule_type mRNA !'##residues 1-106 ##label GUA !'##cross-references GB:M33065; NID:g210673; PIDN:AAA42746.1; !1PID:g210675 REFERENCE S28728 !$#authors Dasmahapatra, B.; Dasgupta, R.; Ghosh, A.; Kaesberg, P. !$#journal J. Mol. Biol. (1985) 182:183-189 !$#title Structure of the black beetle virus genome and its !1functional implications. !$#cross-references MUID:85210903; PMID:3839022 !$#accession S28730 !'##molecule_type genomic RNA !'##residues 1-13,'R',15-106 ##label DAS !'##cross-references EMBL:X02396 CLASSIFICATION #superfamily black beetle virus B2 protein SUMMARY #length 106 #molecular-weight 11587 #checksum 162 SEQUENCE /// ENTRY QQBB2G #type complete TITLE hypothetical protein - black beetle virus ORGANISM #formal_name black beetle virus #note host Drosophila melanogaster DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 10-Sep-1999 ACCESSIONS A04152 REFERENCE A93535 !$#authors Dasgupta, R.; Ghosh, A.; Dasmahapatra, B.; Guarino, L.A.; !1Kaesberg, P. !$#journal Nucleic Acids Res. (1984) 12:7215-7223 !$#title Primary and secondary structure of black beetle virus RNA2, !1the genomic messenger for BBV coat protein precursor. !$#cross-references MUID:85014162; PMID:6548308 !$#accession A04152 !'##molecule_type mRNA !'##residues 1-72 ##label DAS !'##cross-references GB:X00956; NID:g60681; PIDN:CAA25469.1; PID:g60683 COMMENT The genome consists of two linear, single-stranded RNAs with !1the same polarity as the mRNA. GENETICS !$#map_position segment 2 CLASSIFICATION #superfamily black beetle virus hypothetical 8K protein SUMMARY #length 72 #molecular-weight 7973 #checksum 295 SEQUENCE /// ENTRY VCCV #type complete TITLE coat protein - cauliflower mosaic virus (strain Strasbourg) ORGANISM #formal_name cauliflower mosaic virus DATE 31-Oct-1980 #sequence_revision 31-Oct-1980 #text_change 23-Jul-1999 ACCESSIONS A04153 REFERENCE A90799 !$#authors Franck, A.; Guilley, H.; Jonard, G.; Richards, K.; Hirth, L. !$#journal Cell (1980) 21:285-294 !$#title Nucleotide sequence of cauliflower mosaic virus DNA. !$#cross-references MUID:81001865; PMID:7407912 !$#accession A04153 !'##molecule_type DNA !'##residues 1-489 ##label FRA !'##cross-references GB:V00141; GB:J02048; NID:g58821; PIDN:CAA23459.1; !1PID:g58825 !'##note the identification of this protein was based on the high lysine !1content of the coat protein and the lysine-rich character of !1this open coding region !'##note this sequence is 3.9% different from that of cauliflower mosaic !1virus strain CM1841 CLASSIFICATION #superfamily cauliflower mosaic virus coat protein KEYWORDS zinc finger SUMMARY #length 489 #molecular-weight 56663 #checksum 777 SEQUENCE /// ENTRY VCCV4C #type complete TITLE coat protein - cauliflower mosaic virus (strain CM1841) ORGANISM #formal_name cauliflower mosaic virus DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 23-Jul-1999 ACCESSIONS A04154 REFERENCE A93729 !$#authors Gardner, R.C.; Howarth, A.J.; Hahn, P.; Brown-Luedi, M.; !1Shepherd, R.J.; Messing, J. !$#journal Nucleic Acids Res. (1981) 9:2871-2888 !$#title The complete nucleotide sequence of an infectious clone of !1cauliflower mosaic virus by M13mp7 shotgun sequencing. !$#cross-references MUID:82014878; PMID:6269062 !$#accession A04154 !'##molecule_type DNA !'##residues 1-488 ##label GAR !'##cross-references GB:V00140; GB:J02046; NID:g58815; PIDN:CAA23455.1; !1PID:g58819 !'##note this sequence is 3.9% different from that of cauliflower mosaic !1virus strain Strasbourg CLASSIFICATION #superfamily cauliflower mosaic virus coat protein KEYWORDS zinc finger SUMMARY #length 488 #molecular-weight 56686 #checksum 711 SEQUENCE /// ENTRY VCCV3 #type complete TITLE coat protein - cauliflower mosaic virus (strain D/H) ORGANISM #formal_name cauliflower mosaic virus DATE 05-Apr-1983 #sequence_revision 05-Apr-1983 #text_change 30-Jun-1993 ACCESSIONS A04155 REFERENCE A94613 !$#authors Guilley, H. !$#submission submitted to the Nucleic Acid Sequence Database, October !11982 !$#accession A04155 !'##molecule_type DNA !'##residues 1-490 ##label GUI CLASSIFICATION #superfamily cauliflower mosaic virus coat protein KEYWORDS zinc finger SUMMARY #length 490 #molecular-weight 56821 #checksum 3301 SEQUENCE /// ENTRY VCCVCE #type complete TITLE coat protein - carnation etched ring virus ORGANISM #formal_name carnation etched ring virus DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 23-Jul-1999 ACCESSIONS S00853 REFERENCE S00850 !$#authors Hull, R.; Sadler, J.; Longstaff, M. !$#journal EMBO J. (1986) 5:3083-3090 !$#title The sequence of carnation etched ring virus DNA: comparison !1with cauliflower mosaic virus and retroviruses. !$#accession S00853 !'##molecule_type DNA !'##residues 1-494 ##label HUL !'##cross-references EMBL:X04658; NID:g58858; PIDN:CAA28359.1; !1PID:g58862 CLASSIFICATION #superfamily cauliflower mosaic virus coat protein KEYWORDS coat protein; zinc finger SUMMARY #length 494 #molecular-weight 56886 #checksum 3876 SEQUENCE /// ENTRY VCCVFM #type complete TITLE coat protein - figwort mosaic virus ORGANISM #formal_name figwort mosaic virus DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 23-Jul-1999 ACCESSIONS S01282 REFERENCE S01279 !$#authors Richins, R.D.; Scholthof, H.B.; Shepherd, R.J. !$#journal Nucleic Acids Res. (1987) 15:8451-8466 !$#title Sequence of figwort mosaic virus DNA (caulimovirus group). !$#cross-references MUID:88040466; PMID:3671088 !$#accession S01282 !'##status translation not shown !'##molecule_type DNA !'##residues 1-489 ##label RIC !'##cross-references EMBL:X06166; NID:g58808; PIDN:CAA29526.1; !1PID:g58812 CLASSIFICATION #superfamily cauliflower mosaic virus coat protein KEYWORDS coat protein; zinc finger SUMMARY #length 489 #molecular-weight 57419 #checksum 6160 SEQUENCE /// ENTRY QQCV1 #type complete TITLE movement protein - cauliflower mosaic virus ALTERNATE_NAMES cell-to-cell transport protein; ORF I; ORF1 protein ORGANISM #formal_name cauliflower mosaic virus DATE 31-Oct-1980 #sequence_revision 31-Oct-1980 #text_change 23-Jul-1999 ACCESSIONS B90799; B93729; B94613; JN0493; A04156 REFERENCE A90799 !$#authors Franck, A.; Guilley, H.; Jonard, G.; Richards, K.; Hirth, L. !$#journal Cell (1980) 21:285-294 !$#title Nucleotide sequence of cauliflower mosaic virus DNA. !$#cross-references MUID:81001865; PMID:7407912 !$#accession B90799 !'##molecule_type DNA !'##residues 1-327 ##label FRA !'##cross-references GB:V00141; GB:J02048; NID:g58821; PIDN:CAA23456.1; !1PID:g58822 !'##experimental_source strain Strasbourg REFERENCE A93729 !$#authors Gardner, R.C.; Howarth, A.J.; Hahn, P.; Brown-Luedi, M.; !1Shepherd, R.J.; Messing, J. !$#journal Nucleic Acids Res. (1981) 9:2871-2888 !$#title The complete nucleotide sequence of an infectious clone of !1cauliflower mosaic virus by M13mp7 shotgun sequencing. !$#cross-references MUID:82014878; PMID:6269062 !$#accession B93729 !'##molecule_type DNA !'##residues 1-105,'R',107-122,'I',124-221,'I',223-257,'D',259-284,'QS', !1287-290,'S',292-327 ##label GAR !'##cross-references GB:V00140; GB:J02046; NID:g58815; PIDN:CAA23452.1; !1PID:g58816 !'##experimental_source strain CM1841 REFERENCE A94613 !$#authors Guilley, H. !$#submission submitted to the Nucleic Acid Sequence Database, October !11982 !$#accession B94613 !'##molecule_type DNA !'##residues 1-27,'T',29-36,'K',38-121,'R',123-221,'I',223-253,'I', !1255-290,'S',292-296,'I',298-301,'S',303-327 ##label GUI !'##experimental_source strain D/H REFERENCE JN0493 !$#authors Chenault, K.D.; Melcher, U. !$#journal Gene (1993) 123:255-257 !$#title The complete nucleotide sequence of cauliflower mosaic virus !1isolate BBC. !$#cross-references MUID:93154593; PMID:8428667 !$#accession JN0493 !'##molecule_type DNA !'##residues 1-14,'H',16-70,'R',72-105,'R',107-221,'M',223-254,'HE',257, !1'D',259-285,'S',287-327 ##label CHE !'##experimental_source isolate BBC CLASSIFICATION #superfamily cauliflower mosaic virus movement protein KEYWORDS DNA binding SUMMARY #length 327 #molecular-weight 36873 #checksum 5272 SEQUENCE /// ENTRY QQCV2 #type complete TITLE aphid transmission protein - cauliflower mosaic virus ALTERNATE_NAMES ORF II; ORF2 protein ORGANISM #formal_name cauliflower mosaic virus DATE 31-Oct-1980 #sequence_revision 31-Oct-1980 #text_change 23-Jul-1999 ACCESSIONS A90799; JA0010; A93729; A94613; JN0494; A04157 REFERENCE A90799 !$#authors Franck, A.; Guilley, H.; Jonard, G.; Richards, K.; Hirth, L. !$#journal Cell (1980) 21:285-294 !$#title Nucleotide sequence of cauliflower mosaic virus DNA. !$#cross-references MUID:81001865; PMID:7407912 !$#accession A90799 !'##molecule_type DNA !'##residues 1-159 ##label FRA !'##cross-references GB:V00141; GB:J02048; NID:g58821; PIDN:CAA23457.1; !1PID:g58823 !'##experimental_source strain Strasbourg REFERENCE A91334 !$#authors Modjtahedi, N.; Volovitch, M.; Mazzolini, L.; Yot, P. !$#journal FEBS Lett. (1985) 181:223-228 !$#title Comparison of the predicted secondary structure of aphid !1transmission factor for transmissible and non-transmissible !1cauliflower mosaic virus strains. !$#accession JA0010 !'##molecule_type DNA !'##residues 1-159 ##label MOD !'##experimental_source strain PV14 REFERENCE A93729 !$#authors Gardner, R.C.; Howarth, A.J.; Hahn, P.; Brown-Luedi, M.; !1Shepherd, R.J.; Messing, J. !$#journal Nucleic Acids Res. (1981) 9:2871-2888 !$#title The complete nucleotide sequence of an infectious clone of !1cauliflower mosaic virus by M13mp7 shotgun sequencing. !$#cross-references MUID:82014878; PMID:6269062 !$#accession A93729 !'##molecule_type DNA !'##residues 1-88,'N',90-93,'R',95-104,'V',106-117,'N',119-120,'N', !1123-126,'D',128-159 ##label GAR !'##experimental_source strain CM1841 REFERENCE A94613 !$#authors Guilley, H. !$#submission submitted to the Nucleic Acid Sequence Database, October !11982 !$#accession A94613 !'##molecule_type DNA !'##residues 1-50,'K',52-101,'P',103-126,'DE',129-159 ##label GUI !'##experimental_source strain D/H REFERENCE JN0493 !$#authors Chenault, K.D.; Melcher, U. !$#journal Gene (1993) 123:255-257 !$#title The complete nucleotide sequence of cauliflower mosaic virus !1isolate BBC. !$#cross-references MUID:93154593; PMID:8428667 !$#accession JN0494 !'##molecule_type DNA !'##residues 1,'R',3-117,'N',119-126,'D',128-137,'K',139-159 ##label CHE !'##cross-references GB:M90542; NID:g678542; PIDN:AAA62372.1; !1PID:g293182 !'##experimental_source isolate BBC CLASSIFICATION #superfamily cauliflower mosaic virus aphid transmission !1protein SUMMARY #length 159 #molecular-weight 17803 #checksum 3030 SEQUENCE /// ENTRY QQCV3 #type complete TITLE DNA-binding protein - cauliflower mosaic virus ALTERNATE_NAMES ORF III; ORF3 protein ORGANISM #formal_name cauliflower mosaic virus DATE 31-Oct-1980 #sequence_revision 31-Oct-1980 #text_change 23-Jul-1999 ACCESSIONS C90799; C93729; C94613; JN0495; A04158 REFERENCE A90799 !$#authors Franck, A.; Guilley, H.; Jonard, G.; Richards, K.; Hirth, L. !$#journal Cell (1980) 21:285-294 !$#title Nucleotide sequence of cauliflower mosaic virus DNA. !$#cross-references MUID:81001865; PMID:7407912 !$#accession C90799 !'##molecule_type DNA !'##residues 1-129 ##label FRA !'##cross-references GB:V00141; GB:J02048; NID:g58821; PIDN:CAA23458.1; !1PID:g58824 !'##experimental_source strain Strasbourg REFERENCE A93729 !$#authors Gardner, R.C.; Howarth, A.J.; Hahn, P.; Brown-Luedi, M.; !1Shepherd, R.J.; Messing, J. !$#journal Nucleic Acids Res. (1981) 9:2871-2888 !$#title The complete nucleotide sequence of an infectious clone of !1cauliflower mosaic virus by M13mp7 shotgun sequencing. !$#cross-references MUID:82014878; PMID:6269062 !$#accession C93729 !'##molecule_type DNA !'##residues 1-23,'S',25-37,'T',39-43,'A',45-71,'N',73-94,'T',96-129 !1##label GAR !'##experimental_source strain CM1841 REFERENCE A94613 !$#authors Guilley, H. !$#submission submitted to the Nucleic Acid Sequence Database, October !11982 !$#accession C94613 !'##molecule_type DNA !'##residues 1-71,'N',73-79,'G',81-128,'Y' ##label GUI !'##experimental_source strain D/H REFERENCE JN0493 !$#authors Chenault, K.D.; Melcher, U. !$#journal Gene (1993) 123:255-257 !$#title The complete nucleotide sequence of cauliflower mosaic virus !1isolate BBC. !$#cross-references MUID:93154593; PMID:8428667 !$#accession JN0495 !'##molecule_type DNA !'##residues 1-22,'S',24-37,'T',39-43,'A',45-71,'N',73-129 ##label CHE !'##cross-references GB:M90542; NID:g678542; PIDN:AAA62373.1; !1PID:g293183 !'##experimental_source isolate BBC CLASSIFICATION #superfamily cauliflower mosaic virus DNA-binding protein KEYWORDS DNA binding SUMMARY #length 129 #molecular-weight 14153 #checksum 9843 SEQUENCE /// ENTRY QQCV5 #type complete TITLE trifunctional enzyme - cauliflower mosaic virus ALTERNATE_NAMES ORF5 protein CONTAINS aspartic proteinase (EC 3.4.23.-); endonuclease; RNA-directed DNA polymerase ORGANISM #formal_name cauliflower mosaic virus DATE 31-Oct-1980 #sequence_revision 31-Oct-1980 #text_change 23-Jul-1999 ACCESSIONS D90799; D93729; D94613; JN0497; A04159 REFERENCE A90799 !$#authors Franck, A.; Guilley, H.; Jonard, G.; Richards, K.; Hirth, L. !$#journal Cell (1980) 21:285-294 !$#title Nucleotide sequence of cauliflower mosaic virus DNA. !$#cross-references MUID:81001865; PMID:7407912 !$#accession D90799 !'##molecule_type DNA !'##residues 1-679 ##label FRA !'##cross-references GB:V00141; GB:J02048; NID:g58821; PIDN:CAA23460.1; !1PID:g58826 !'##experimental_source strain Strasbourg REFERENCE A93729 !$#authors Gardner, R.C.; Howarth, A.J.; Hahn, P.; Brown-Luedi, M.; !1Shepherd, R.J.; Messing, J. !$#journal Nucleic Acids Res. (1981) 9:2871-2888 !$#title The complete nucleotide sequence of an infectious clone of !1cauliflower mosaic virus by M13mp7 shotgun sequencing. !$#cross-references MUID:82014878; PMID:6269062 !$#accession D93729 !'##molecule_type DNA !'##residues 1,'N',3-11,'I',13-98,'K',100-144,'T',146-154,'I',156-313, !1'I',315-514,'K',516-587,'R',589-679 ##label GAR !'##experimental_source strain CM1841 REFERENCE A94613 !$#authors Guilley, H. !$#submission submitted to the Nucleic Acid Sequence Database, October !11982 !$#accession D94613 !'##molecule_type DNA !'##residues 1-5,'Q',7-9,'I',11,'NQ',12-17,'I',19-63,'I',65-82,'N', !184-86,'R',88-98,'H',100-136,'DRT',140-181,189-319,'P', !1321-514,'K',516-675,'R',677-679 ##label GUI !'##experimental_source strain D/H REFERENCE JN0493 !$#authors Chenault, K.D.; Melcher, U. !$#journal Gene (1993) 123:255-257 !$#title The complete nucleotide sequence of cauliflower mosaic virus !1isolate BBC. !$#cross-references MUID:93154593; PMID:8428667 !$#accession JN0497 !'##molecule_type DNA !'##residues 1-56,'L',58-94,'R',96-98,'K',100-185,'K',187-313,'I', !1315-514,'K',516-587,'R',589-679 ##label CHE !'##experimental_source isolate BBC !'##note the authors translated the codon CTC for residue 57 as Val CLASSIFICATION #superfamily cauliflower mosaic virus trifunctional enzyme KEYWORDS aspartic proteinase; endonuclease; hydrolase; !1multifunctional enzyme; nucleotidyltransferase SUMMARY #length 679 #molecular-weight 78628 #checksum 2168 SEQUENCE /// ENTRY WMCVFM #type complete TITLE inclusion body matrix protein - figwort mosaic virus ORGANISM #formal_name figwort mosaic virus DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 23-Jul-1999 ACCESSIONS S01284 REFERENCE S01279 !$#authors Richins, R.D.; Scholthof, H.B.; Shepherd, R.J. !$#journal Nucleic Acids Res. (1987) 15:8451-8466 !$#title Sequence of figwort mosaic virus DNA (caulimovirus group). !$#cross-references MUID:88040466; PMID:3671088 !$#accession S01284 !'##status translation not shown !'##molecule_type DNA !'##residues 1-512 ##label RIC !'##cross-references EMBL:X06166; NID:g58808; PIDN:CAA29528.1; !1PID:g58814 CLASSIFICATION #superfamily caulimovirus inclusion body matrix protein KEYWORDS matrix protein SUMMARY #length 512 #molecular-weight 58207 #checksum 1605 SEQUENCE /// ENTRY QQCV6 #type complete TITLE hypothetical protein 6 - cauliflower mosaic virus (strain D/ H) ORGANISM #formal_name cauliflower mosaic virus DATE 31-Oct-1980 #sequence_revision 05-Apr-1983 #text_change 30-Jun-1993 ACCESSIONS A04160 REFERENCE A94613 !$#authors Guilley, H. !$#submission submitted to the Nucleic Acid Sequence Database, October !11982 !$#accession A04160 !'##molecule_type DNA !'##residues 1-522 ##label GUI CLASSIFICATION #superfamily caulimovirus inclusion body matrix protein SUMMARY #length 522 #molecular-weight 58292 #checksum 4016 SEQUENCE /// ENTRY QQCV6C #type complete TITLE hypothetical protein 6 - cauliflower mosaic virus (strain CM1841) ORGANISM #formal_name cauliflower mosaic virus DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 30-Sep-1993 ACCESSIONS A04161 REFERENCE A93729 !$#authors Gardner, R.C.; Howarth, A.J.; Hahn, P.; Brown-Luedi, M.; !1Shepherd, R.J.; Messing, J. !$#journal Nucleic Acids Res. (1981) 9:2871-2888 !$#title The complete nucleotide sequence of an infectious clone of !1cauliflower mosaic virus by M13mp7 shotgun sequencing. !$#cross-references MUID:82014878; PMID:6269062 !$#accession A04161 !'##molecule_type DNA !'##residues 1-520 ##label GAR !'##note the authors assume this protein is the inclusion body protein, !1a protein found in the cytoplasmic inclusion bodies; the !1inclusion bodies are the site of virus accumulation in the !1infected cell !'##note this sequence is 5.2% different from that of cauliflower mosaic !1virus strain Strasbourg CLASSIFICATION #superfamily caulimovirus inclusion body matrix protein SUMMARY #length 520 #molecular-weight 57907 #checksum 719 SEQUENCE /// ENTRY QQCV6S #type complete TITLE hypothetical protein 6 - cauliflower mosaic virus (strain Strasbourg) ORGANISM #formal_name cauliflower mosaic virus DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 23-Jul-1999 ACCESSIONS A04162 REFERENCE A90799 !$#authors Franck, A.; Guilley, H.; Jonard, G.; Richards, K.; Hirth, L. !$#journal Cell (1980) 21:285-294 !$#title Nucleotide sequence of cauliflower mosaic virus DNA. !$#cross-references MUID:81001865; PMID:7407912 !$#accession A04162 !'##molecule_type DNA !'##residues 1-520 ##label FRA !'##cross-references GB:V00141; GB:J02048; NID:g58821; PIDN:CAA23461.1; !1PID:g58827 CLASSIFICATION #superfamily caulimovirus inclusion body matrix protein SUMMARY #length 520 #molecular-weight 57992 #checksum 318 SEQUENCE /// ENTRY QQCVR1 #type complete TITLE coat protein - tomato golden mosaic virus ORGANISM #formal_name tomato golden mosaic virus DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 08-Apr-1994 ACCESSIONS A04163 REFERENCE A04163 !$#authors Hamilton, W.D.O.; Stein, V.E.; Coutts, R.H.A.; Buck, K.W. !$#journal EMBO J. (1984) 3:2197-2205 !$#title Complete nucleotide sequence of the infectious cloned DNA !1components of tomato golden mosaic virus: potential coding !1regions and regulatory sequences. !$#accession A04163 !'##molecule_type DNA !'##residues 1-247 ##label HAM GENETICS !$#map_position segment DNA1 CLASSIFICATION #superfamily cassava latent virus coat protein KEYWORDS coat protein SUMMARY #length 247 #molecular-weight 28684 #checksum 6493 SEQUENCE /// ENTRY QQCVW2 #type complete TITLE coat protein - abutilon mosaic virus (isolate West India) ORGANISM #formal_name abutilon mosaic virus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 23-Jul-1999 ACCESSIONS B36214 REFERENCE A36214 !$#authors Frischmuth, T.; Zimmat, G.; Jeske, H. !$#journal Virology (1990) 178:461-468 !$#title The nucleotide sequence of the abutilon mosaic virus reveals !1prokaryotic as well as eukaryotic features. !$#cross-references MUID:91020984; PMID:2219703 !$#accession B36214 !'##status translation not shown !'##molecule_type DNA !'##residues 1-241 ##label FRI !'##cross-references EMBL:X15983; NID:g59349; PIDN:CAA34110.1; !1PID:g59350 GENETICS !$#map_position segment A CLASSIFICATION #superfamily cassava latent virus coat protein KEYWORDS coat protein SUMMARY #length 241 #molecular-weight 28084 #checksum 7122 SEQUENCE /// ENTRY QQCVP2 #type complete TITLE coat protein - potato yellow mosaic virus (isolate Venezuela) ORGANISM #formal_name potato yellow mosaic virus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jun-2000 ACCESSIONS JU0367 REFERENCE JU0362 !$#authors Coutts, R.H.A.; Coffin, R.S.; Roberts, E.J.F.; Hamilton, !1W.D.O. !$#journal J. Gen. Virol. (1991) 72:1515-1520 !$#title The nucleotide sequence of the infectious cloned DNA !1components of potato yellow mosaic virus. !$#cross-references MUID:91311403; PMID:1856690 !$#accession JU0367 !'##molecule_type DNA !'##residues 1-251 ##label COU !'##cross-references GB:D00940; NID:g222458; PIDN:BAA00779.1; !1PID:g222460 GENETICS !$#map_position segment A CLASSIFICATION #superfamily cassava latent virus coat protein KEYWORDS coat protein SUMMARY #length 251 #molecular-weight 29266 #checksum 3568 SEQUENCE /// ENTRY QQCVS2 #type complete TITLE coat protein - squash leaf curl virus ORGANISM #formal_name squash leaf curl virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 23-Jul-1999 ACCESSIONS D36785 REFERENCE A36785 !$#authors Lazarowitz, S.G.; Lazdins, I.B. !$#journal Virology (1991) 180:58-69 !$#title Infectivity and complete nucleotide sequence of the cloned !1genomic components of a bipartite squash leaf curl !1geminivirus with a broad host range phenotype. !$#cross-references MUID:91082449; PMID:1984668 !$#accession D36785 !'##status translation not shown !'##molecule_type DNA !'##residues 1-251 ##label LAZ !'##cross-references GB:M38183; NID:g335003; PIDN:AAC32411.1; !1PID:g335005 GENETICS !$#map_position segment A CLASSIFICATION #superfamily cassava latent virus coat protein KEYWORDS coat protein SUMMARY #length 251 #molecular-weight 29228 #checksum 1692 SEQUENCE /// ENTRY JQ1869 #type complete TITLE coat protein - tomato mottle virus (isolate Florida) ALTERNATE_NAMES AR1 protein ORGANISM #formal_name tomato mottle virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 23-Jul-1999 ACCESSIONS JQ1869 REFERENCE JQ1869 !$#authors Abouzid, A.M.; Polston, J.E.; Hiebert, E. !$#journal J. Gen. Virol. (1992) 73:3225-3229 !$#title The nucleotide sequence of tomato mottle virus, a new !1geminivirus isolated from tomatoes in Florida. !$#cross-references MUID:93107858; PMID:1469361 !$#accession JQ1869 !'##status translation not shown !'##molecule_type DNA !'##residues 1-251 ##label ABO !'##cross-references GB:L14460; NID:g295320; PIDN:AAC32415.1; !1PID:g295322 GENETICS !$#map_position segment A CLASSIFICATION #superfamily cassava latent virus coat protein KEYWORDS coat protein SUMMARY #length 251 #molecular-weight 29265 #checksum 4322 SEQUENCE /// ENTRY QQOMC1 #type complete TITLE coat protein - cassava latent virus (West Kenyan isolate 844) ORGANISM #formal_name cassava latent virus DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 08-Apr-1994 ACCESSIONS A04164 REFERENCE A04164 !$#authors Stanley, J.; Gay, M.R. !$#journal Nature (1983) 301:260-262 !$#title Nucleotide sequence of cassava latent virus DNA. !$#accession A04164 !'##molecule_type DNA !'##residues 1-258 ##label STA GENETICS !$#map_position segment DNA1 CLASSIFICATION #superfamily cassava latent virus coat protein KEYWORDS coat protein SUMMARY #length 258 #molecular-weight 30129 #checksum 6022 SEQUENCE /// ENTRY VCOMCN #type complete TITLE coat protein - cassava latent virus (strain Nigeria) ORGANISM #formal_name cassava latent virus DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 23-Jul-1999 ACCESSIONS S07591 REFERENCE S07590 !$#authors Morris, B.; Coates, L.; Lowe, S.; Richardson, K.; Eddy, P. !$#journal Nucleic Acids Res. (1990) 18:197-198 !$#title Nucleotide sequence of the infectious cloned DNA components !1of African cassava mosaic virus (Nigerian strain). !$#cross-references MUID:90174930; PMID:2308831 !$#accession S07591 !'##status translation not shown !'##molecule_type DNA !'##residues 1-258 ##label MOR !'##cross-references EMBL:X17095; NID:g59371; PIDN:CAA34950.1; !1PID:g59373 GENETICS !$#map_position segment DNA1 CLASSIFICATION #superfamily cassava latent virus coat protein KEYWORDS coat protein SUMMARY #length 258 #molecular-weight 30210 #checksum 5228 SEQUENCE /// ENTRY QQCVCL #type complete TITLE coat protein - tomato yellow leaf curl virus ORGANISM #formal_name tomato yellow leaf curl virus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 23-Jul-1999 ACCESSIONS A40779 REFERENCE A40779 !$#authors Navot, N.; Pichersky, E.; Zeidan, M.; Zamir, D.; Czosnek, H. !$#journal Virology (1991) 185:151-161 !$#title Tomato yellow leaf curl virus: a whitefly-transmitted !1geminivirus with a single genomic component. !$#cross-references MUID:92024070; PMID:1926771 !$#accession A40779 !'##status translation not shown !'##molecule_type DNA !'##residues 1-260 ##label NAV !'##cross-references GB:X15656; NID:g62204; PIDN:CAA33686.1; PID:g62205 CLASSIFICATION #superfamily cassava latent virus coat protein KEYWORDS coat protein SUMMARY #length 260 #molecular-weight 30320 #checksum 3499 SEQUENCE /// ENTRY JQ1886 #type complete TITLE coat protein - tomato yellow leaf curl virus (strain Australia) ORGANISM #formal_name tomato yellow leaf curl virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 07-May-1999 ACCESSIONS JQ1886 REFERENCE JQ1885 !$#authors Dry, I.B.; Rigden, J.E.; Krake, L.R.; Mullineaux, P.M.; !1Rezaian, M.A. !$#journal J. Gen. Virol. (1993) 74:147-151 !$#title Nucleotide sequence and genome organization of tomato leaf !1curl geminivirus. !$#cross-references MUID:93139778; PMID:8423446 !$#accession JQ1886 !'##status translation not shown !'##molecule_type DNA !'##residues 1-256 ##label DRY !'##cross-references GB:S53251 CLASSIFICATION #superfamily cassava latent virus coat protein KEYWORDS coat protein SUMMARY #length 256 #molecular-weight 29713 #checksum 4185 SEQUENCE /// ENTRY QQCVL2 #type complete TITLE AL2 protein - tomato golden mosaic virus ORGANISM #formal_name tomato golden mosaic virus #note host Nicotiana sp. (tobacco) DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 08-Apr-1994 ACCESSIONS A04165 REFERENCE A04163 !$#authors Hamilton, W.D.O.; Stein, V.E.; Coutts, R.H.A.; Buck, K.W. !$#journal EMBO J. (1984) 3:2197-2205 !$#title Complete nucleotide sequence of the infectious cloned DNA !1components of tomato golden mosaic virus: potential coding !1regions and regulatory sequences. !$#accession A04165 !'##molecule_type DNA !'##residues 1-129 ##label HAM COMMENT The genome consists of two circular, single-stranded DNA !1components, DNA A and DNA B. There are six potential coding !1regions, four in DNA A and two in DNA B. This protein is !1coded by DNA A. GENETICS !$#map_position segment A CLASSIFICATION #superfamily tomato golden mosaic virus AL2 protein SUMMARY #length 129 #molecular-weight 14887 #checksum 1777 SEQUENCE /// ENTRY QQCVW4 #type complete TITLE AC2 protein - abutilon mosaic virus (isolate West India) ORGANISM #formal_name abutilon mosaic virus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 18-Nov-1994 ACCESSIONS D36214 REFERENCE A36214 !$#authors Frischmuth, T.; Zimmat, G.; Jeske, H. !$#journal Virology (1990) 178:461-468 !$#title The nucleotide sequence of the abutilon mosaic virus reveals !1prokaryotic as well as eukaryotic features. !$#cross-references MUID:91020984; PMID:2219703 !$#accession D36214 !'##status translation not shown !'##molecule_type DNA !'##residues 1-129 ##label FRI !'##cross-references EMBL:X15983 GENETICS !$#map_position segment A CLASSIFICATION #superfamily tomato golden mosaic virus AL2 protein SUMMARY #length 129 #molecular-weight 14425 #checksum 234 SEQUENCE /// ENTRY QQCVP4 #type complete TITLE AL2 protein - potato yellow mosaic virus (isolate Venezuela) ORGANISM #formal_name potato yellow mosaic virus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jun-2000 ACCESSIONS JU0365 REFERENCE JU0362 !$#authors Coutts, R.H.A.; Coffin, R.S.; Roberts, E.J.F.; Hamilton, !1W.D.O. !$#journal J. Gen. Virol. (1991) 72:1515-1520 !$#title The nucleotide sequence of the infectious cloned DNA !1components of potato yellow mosaic virus. !$#cross-references MUID:91311403; PMID:1856690 !$#accession JU0365 !'##status translation not shown !'##molecule_type DNA !'##residues 1-129 ##label COU !'##cross-references GB:D00940; NID:g222458; PIDN:BAA00781.1; !1PID:g222462 GENETICS !$#map_position segment A CLASSIFICATION #superfamily tomato golden mosaic virus AL2 protein SUMMARY #length 129 #molecular-weight 14735 #checksum 8931 SEQUENCE /// ENTRY QQCVC4 #type complete TITLE AL2 protein - tomato yellow leaf curl virus ALTERNATE_NAMES C2 protein ORGANISM #formal_name tomato yellow leaf curl virus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 23-Jul-1999 ACCESSIONS C40779 REFERENCE A40779 !$#authors Navot, N.; Pichersky, E.; Zeidan, M.; Zamir, D.; Czosnek, H. !$#journal Virology (1991) 185:151-161 !$#title Tomato yellow leaf curl virus: a whitefly-transmitted !1geminivirus with a single genomic component. !$#cross-references MUID:92024070; PMID:1926771 !$#accession C40779 !'##status translation not shown !'##molecule_type DNA !'##residues 1-135 ##label NAV !'##cross-references GB:X15656; NID:g62204; PIDN:CAA33689.1; PID:g62208 CLASSIFICATION #superfamily tomato golden mosaic virus AL2 protein SUMMARY #length 135 #molecular-weight 15611 #checksum 9404 SEQUENCE /// ENTRY QQCVS4 #type complete TITLE AL2 protein - squash leaf curl virus ORGANISM #formal_name squash leaf curl virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 23-Jul-1999 ACCESSIONS F36785 REFERENCE A36785 !$#authors Lazarowitz, S.G.; Lazdins, I.B. !$#journal Virology (1991) 180:58-69 !$#title Infectivity and complete nucleotide sequence of the cloned !1genomic components of a bipartite squash leaf curl !1geminivirus with a broad host range phenotype. !$#cross-references MUID:91082449; PMID:1984668 !$#accession F36785 !'##status translation not shown !'##molecule_type DNA !'##residues 1-131 ##label LAZ !'##cross-references GB:M38183; NID:g335003; PIDN:AAC32413.1; !1PID:g335007 GENETICS !$#map_position segment A CLASSIFICATION #superfamily tomato golden mosaic virus AL2 protein SUMMARY #length 131 #molecular-weight 14582 #checksum 3331 SEQUENCE /// ENTRY JQ1888 #type complete TITLE AL2 protein - tomato yellow leaf curl virus (strain Australia) ALTERNATE_NAMES C2 protein ORGANISM #formal_name tomato yellow leaf curl virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 07-May-1999 ACCESSIONS JQ1888 REFERENCE JQ1885 !$#authors Dry, I.B.; Rigden, J.E.; Krake, L.R.; Mullineaux, P.M.; !1Rezaian, M.A. !$#journal J. Gen. Virol. (1993) 74:147-151 !$#title Nucleotide sequence and genome organization of tomato leaf !1curl geminivirus. !$#cross-references MUID:93139778; PMID:8423446 !$#accession JQ1888 !'##status translation not shown !'##molecule_type DNA !'##residues 1-135 ##label DRY !'##cross-references GB:S53251 CLASSIFICATION #superfamily tomato golden mosaic virus AL2 protein SUMMARY #length 135 #molecular-weight 15304 #checksum 1503 SEQUENCE /// ENTRY JQ1871 #type complete TITLE AL2 protein - tomato mottle virus (isolate Florida) ORGANISM #formal_name tomato mottle virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 23-Jul-1999 ACCESSIONS JQ1871 REFERENCE JQ1869 !$#authors Abouzid, A.M.; Polston, J.E.; Hiebert, E. !$#journal J. Gen. Virol. (1992) 73:3225-3229 !$#title The nucleotide sequence of tomato mottle virus, a new !1geminivirus isolated from tomatoes in Florida. !$#cross-references MUID:93107858; PMID:1469361 !$#accession JQ1871 !'##status translation not shown !'##molecule_type DNA !'##residues 1-129 ##label ABO !'##cross-references GB:L14460; NID:g295320; PIDN:AAC32417.1; !1PID:g295324 GENETICS !$#map_position segment A CLASSIFICATION #superfamily tomato golden mosaic virus AL2 protein SUMMARY #length 129 #molecular-weight 14503 #checksum 2634 SEQUENCE /// ENTRY QQCVL3 #type complete TITLE AL3 protein - tomato golden mosaic virus ORGANISM #formal_name tomato golden mosaic virus #note host Nicotiana sp. (tobacco) DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 08-Apr-1994 ACCESSIONS A04166 REFERENCE A04163 !$#authors Hamilton, W.D.O.; Stein, V.E.; Coutts, R.H.A.; Buck, K.W. !$#journal EMBO J. (1984) 3:2197-2205 !$#title Complete nucleotide sequence of the infectious cloned DNA !1components of tomato golden mosaic virus: potential coding !1regions and regulatory sequences. !$#accession A04166 !'##molecule_type DNA !'##residues 1-132 ##label HAM COMMENT The genome consists of two circular, single-stranded DNA !1components, DNA A and DNA B. There are six potential coding !1regions, four in DNA A and two in DNA B. This protein is !1coded by DNA A. GENETICS !$#map_position segment A CLASSIFICATION #superfamily tomato golden mosaic virus AL3 protein SUMMARY #length 132 #molecular-weight 15695 #checksum 185 SEQUENCE /// ENTRY QQCVW3 #type complete TITLE AC3 protein - abutilon mosaic virus (isolate West India) ORGANISM #formal_name abutilon mosaic virus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 23-Jul-1999 ACCESSIONS C36214 REFERENCE A36214 !$#authors Frischmuth, T.; Zimmat, G.; Jeske, H. !$#journal Virology (1990) 178:461-468 !$#title The nucleotide sequence of the abutilon mosaic virus reveals !1prokaryotic as well as eukaryotic features. !$#cross-references MUID:91020984; PMID:2219703 !$#accession C36214 !'##status translation not shown !'##molecule_type DNA !'##residues 1-132 ##label FRI !'##cross-references EMBL:X15983; NID:g59349; PIDN:CAA34113.1; !1PID:g59352 GENETICS !$#map_position segment A CLASSIFICATION #superfamily tomato golden mosaic virus AL3 protein SUMMARY #length 132 #molecular-weight 15899 #checksum 1528 SEQUENCE /// ENTRY JQ1872 #type complete TITLE AL3 protein - tomato mottle virus (isolate Florida) ORGANISM #formal_name tomato mottle virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 23-Jul-1999 ACCESSIONS JQ1872 REFERENCE JQ1869 !$#authors Abouzid, A.M.; Polston, J.E.; Hiebert, E. !$#journal J. Gen. Virol. (1992) 73:3225-3229 !$#title The nucleotide sequence of tomato mottle virus, a new !1geminivirus isolated from tomatoes in Florida. !$#cross-references MUID:93107858; PMID:1469361 !$#accession JQ1872 !'##status translation not shown !'##molecule_type DNA !'##residues 1-132 ##label ABO !'##cross-references GB:L14460; NID:g295320; PIDN:AAC32416.1; !1PID:g295323 GENETICS !$#map_position segment A CLASSIFICATION #superfamily tomato golden mosaic virus AL3 protein SUMMARY #length 132 #molecular-weight 15777 #checksum 1618 SEQUENCE /// ENTRY QQCVP3 #type complete TITLE AL3 protein - potato yellow mosaic virus (isolate Venezuela) ORGANISM #formal_name potato yellow mosaic virus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jun-2000 ACCESSIONS JU0366 REFERENCE JU0362 !$#authors Coutts, R.H.A.; Coffin, R.S.; Roberts, E.J.F.; Hamilton, !1W.D.O. !$#journal J. Gen. Virol. (1991) 72:1515-1520 !$#title The nucleotide sequence of the infectious cloned DNA !1components of potato yellow mosaic virus. !$#cross-references MUID:91311403; PMID:1856690 !$#accession JU0366 !'##status translation not shown !'##molecule_type DNA !'##residues 1-132 ##label COU !'##cross-references GB:D00940; NID:g222458; PIDN:BAA00780.1; !1PID:g222461 GENETICS !$#map_position segment A CLASSIFICATION #superfamily tomato golden mosaic virus AL3 protein SUMMARY #length 132 #molecular-weight 15784 #checksum 1767 SEQUENCE /// ENTRY QQCVC3 #type complete TITLE AL3 protein - tomato yellow leaf curl virus ALTERNATE_NAMES C3 protein ORGANISM #formal_name tomato yellow leaf curl virus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 23-Jul-1999 ACCESSIONS B40779 REFERENCE A40779 !$#authors Navot, N.; Pichersky, E.; Zeidan, M.; Zamir, D.; Czosnek, H. !$#journal Virology (1991) 185:151-161 !$#title Tomato yellow leaf curl virus: a whitefly-transmitted !1geminivirus with a single genomic component. !$#cross-references MUID:92024070; PMID:1926771 !$#accession B40779 !'##status translation not shown !'##molecule_type DNA !'##residues 1-134 ##label NAV !'##cross-references GB:X15656; NID:g62204; PIDN:CAA33690.1; PID:g62209 CLASSIFICATION #superfamily tomato golden mosaic virus AL3 protein SUMMARY #length 134 #molecular-weight 15939 #checksum 1080 SEQUENCE /// ENTRY QQCVS3 #type complete TITLE AL3 protein - squash leaf curl virus ORGANISM #formal_name squash leaf curl virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 23-Jul-1999 ACCESSIONS E36785 REFERENCE A36785 !$#authors Lazarowitz, S.G.; Lazdins, I.B. !$#journal Virology (1991) 180:58-69 !$#title Infectivity and complete nucleotide sequence of the cloned !1genomic components of a bipartite squash leaf curl !1geminivirus with a broad host range phenotype. !$#cross-references MUID:91082449; PMID:1984668 !$#accession E36785 !'##status translation not shown !'##molecule_type DNA !'##residues 1-134 ##label LAZ !'##cross-references GB:M38183; NID:g335003; PIDN:AAC32412.1; !1PID:g335006 GENETICS !$#map_position segment A CLASSIFICATION #superfamily tomato golden mosaic virus AL3 protein SUMMARY #length 134 #molecular-weight 16231 #checksum 3560 SEQUENCE /// ENTRY JQ1889 #type complete TITLE AL3 protein - tomato yellow leaf curl virus (strain Australia) ALTERNATE_NAMES C3 protein ORGANISM #formal_name tomato yellow leaf curl virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 07-May-1999 ACCESSIONS JQ1889 REFERENCE JQ1885 !$#authors Dry, I.B.; Rigden, J.E.; Krake, L.R.; Mullineaux, P.M.; !1Rezaian, M.A. !$#journal J. Gen. Virol. (1993) 74:147-151 !$#title Nucleotide sequence and genome organization of tomato leaf !1curl geminivirus. !$#cross-references MUID:93139778; PMID:8423446 !$#accession JQ1889 !'##status translation not shown !'##molecule_type DNA !'##residues 1-134 ##label DRY !'##cross-references GB:S53251 CLASSIFICATION #superfamily tomato golden mosaic virus AL3 protein SUMMARY #length 134 #molecular-weight 16114 #checksum 2916 SEQUENCE /// ENTRY QQCVRG #type complete TITLE BR1 protein - tomato golden mosaic virus ORGANISM #formal_name tomato golden mosaic virus #note host Nicotiana sp. (tobacco) DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 08-Apr-1994 ACCESSIONS A04167 REFERENCE A04163 !$#authors Hamilton, W.D.O.; Stein, V.E.; Coutts, R.H.A.; Buck, K.W. !$#journal EMBO J. (1984) 3:2197-2205 !$#title Complete nucleotide sequence of the infectious cloned DNA !1components of tomato golden mosaic virus: potential coding !1regions and regulatory sequences. !$#accession A04167 !'##molecule_type DNA !'##residues 1-256 ##label HAM COMMENT The genome consists of two circular, single-stranded DNA !1components, DNA A and DNA B. There are six potential coding !1regions, four in DNA A and two in DNA B. This protein is !1coded by DNA B. GENETICS !$#map_position segment B CLASSIFICATION #superfamily tomato golden mosaic virus BR1 protein SUMMARY #length 256 #molecular-weight 29374 #checksum 8329 SEQUENCE /// ENTRY QQCVW5 #type complete TITLE BV1 protein - abutilon mosaic virus (isolate West India) ORGANISM #formal_name abutilon mosaic virus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 23-Jul-1999 ACCESSIONS E36214 REFERENCE A36214 !$#authors Frischmuth, T.; Zimmat, G.; Jeske, H. !$#journal Virology (1990) 178:461-468 !$#title The nucleotide sequence of the abutilon mosaic virus reveals !1prokaryotic as well as eukaryotic features. !$#cross-references MUID:91020984; PMID:2219703 !$#accession E36214 !'##status translation not shown !'##molecule_type DNA !'##residues 1-257 ##label FRI !'##cross-references EMBL:X15984; NID:g59353; PIDN:CAA34114.1; !1PID:g59354 GENETICS !$#map_position segment B CLASSIFICATION #superfamily tomato golden mosaic virus BR1 protein SUMMARY #length 257 #molecular-weight 29807 #checksum 2472 SEQUENCE /// ENTRY QQCVPP #type complete TITLE BR1 protein - potato yellow mosaic virus (isolate Venezuela) ORGANISM #formal_name potato yellow mosaic virus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jun-2000 ACCESSIONS JU0363 REFERENCE JU0362 !$#authors Coutts, R.H.A.; Coffin, R.S.; Roberts, E.J.F.; Hamilton, !1W.D.O. !$#journal J. Gen. Virol. (1991) 72:1515-1520 !$#title The nucleotide sequence of the infectious cloned DNA !1components of potato yellow mosaic virus. !$#cross-references MUID:91311403; PMID:1856690 !$#accession JU0363 !'##status translation not shown !'##molecule_type DNA !'##residues 1-256 ##label COU !'##cross-references GB:D00941; NID:g222463; PIDN:BAA00783.1; !1PID:g222464 GENETICS !$#map_position segment B CLASSIFICATION #superfamily tomato golden mosaic virus BR1 protein SUMMARY #length 256 #molecular-weight 29499 #checksum 9895 SEQUENCE /// ENTRY QQCVSV #type complete TITLE BR1 protein - squash leaf curl virus ORGANISM #formal_name squash leaf curl virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 23-Jul-1999 ACCESSIONS A36785 REFERENCE A36785 !$#authors Lazarowitz, S.G.; Lazdins, I.B. !$#journal Virology (1991) 180:58-69 !$#title Infectivity and complete nucleotide sequence of the cloned !1genomic components of a bipartite squash leaf curl !1geminivirus with a broad host range phenotype. !$#cross-references MUID:91082449; PMID:1984668 !$#accession A36785 !'##status translation not shown !'##molecule_type DNA !'##residues 1-283 ##label LAZ !'##cross-references GB:M38182; NID:g335000; PIDN:AAC32408.1; !1PID:g335001 GENETICS !$#map_position segment B CLASSIFICATION #superfamily tomato golden mosaic virus BR1 protein SUMMARY #length 283 #molecular-weight 32302 #checksum 8541 SEQUENCE /// ENTRY JQ1873 #type complete TITLE BR1 protein - tomato mottle virus (isolate Florida) ORGANISM #formal_name tomato mottle virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 23-Jul-1999 ACCESSIONS JQ1873 REFERENCE JQ1869 !$#authors Abouzid, A.M.; Polston, J.E.; Hiebert, E. !$#journal J. Gen. Virol. (1992) 73:3225-3229 !$#title The nucleotide sequence of tomato mottle virus, a new !1geminivirus isolated from tomatoes in Florida. !$#cross-references MUID:93107858; PMID:1469361 !$#accession JQ1873 !'##status translation not shown !'##molecule_type DNA !'##residues 1-257 ##label ABO !'##cross-references GB:L14461; NID:g1200530; PIDN:AAC32418.1; !1PID:g295328 GENETICS !$#map_position segment B CLASSIFICATION #superfamily tomato golden mosaic virus BR1 protein SUMMARY #length 257 #molecular-weight 29508 #checksum 2069 SEQUENCE /// ENTRY QQOMC2 #type complete TITLE B256 protein - cassava latent virus (West Kenyan isolate 844) ORGANISM #formal_name cassava latent virus DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 08-Apr-1994 ACCESSIONS A04168 REFERENCE A04164 !$#authors Stanley, J.; Gay, M.R. !$#journal Nature (1983) 301:260-262 !$#title Nucleotide sequence of cassava latent virus DNA. !$#accession A04168 !'##molecule_type DNA !'##residues 1-256 ##label STA COMMENT The genome consists of two circular, single-stranded DNA !1components, DNA A and DNA B. GENETICS !$#map_position segment B CLASSIFICATION #superfamily tomato golden mosaic virus BR1 protein SUMMARY #length 256 #molecular-weight 29305 #checksum 3458 SEQUENCE /// ENTRY QQCVB1 #type complete TITLE V2 protein - tomato yellow leaf curl virus ORGANISM #formal_name tomato yellow leaf curl virus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 23-Jul-1999 ACCESSIONS E40779 REFERENCE A40779 !$#authors Navot, N.; Pichersky, E.; Zeidan, M.; Zamir, D.; Czosnek, H. !$#journal Virology (1991) 185:151-161 !$#title Tomato yellow leaf curl virus: a whitefly-transmitted !1geminivirus with a single genomic component. !$#cross-references MUID:92024070; PMID:1926771 !$#accession E40779 !'##status translation not shown !'##molecule_type DNA !'##residues 1-116 ##label NAV !'##cross-references GB:X15656; NID:g62204; PIDN:CAA33687.1; PID:g62206 CLASSIFICATION #superfamily tomato yellow leaf curl virus V2 protein SUMMARY #length 116 #molecular-weight 13459 #checksum 3144 SEQUENCE /// ENTRY JQ1885 #type complete TITLE V2 protein - tomato yellow leaf curl virus (strain Australia) ORGANISM #formal_name tomato yellow leaf curl virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 07-May-1999 ACCESSIONS JQ1885 REFERENCE JQ1885 !$#authors Dry, I.B.; Rigden, J.E.; Krake, L.R.; Mullineaux, P.M.; !1Rezaian, M.A. !$#journal J. Gen. Virol. (1993) 74:147-151 !$#title Nucleotide sequence and genome organization of tomato leaf !1curl geminivirus. !$#cross-references MUID:93139778; PMID:8423446 !$#accession JQ1885 !'##status translation not shown !'##molecule_type DNA !'##residues 1-115 ##label DRY !'##cross-references GB:S53251 CLASSIFICATION #superfamily tomato yellow leaf curl virus V2 protein SUMMARY #length 115 #molecular-weight 13250 #checksum 1008 SEQUENCE /// ENTRY QQCVLG #type complete TITLE BL1 protein - tomato golden mosaic virus ORGANISM #formal_name tomato golden mosaic virus #note host Nicotiana sp. (tobacco) DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 08-Apr-1994 ACCESSIONS A04169 REFERENCE A04163 !$#authors Hamilton, W.D.O.; Stein, V.E.; Coutts, R.H.A.; Buck, K.W. !$#journal EMBO J. (1984) 3:2197-2205 !$#title Complete nucleotide sequence of the infectious cloned DNA !1components of tomato golden mosaic virus: potential coding !1regions and regulatory sequences. !$#accession A04169 !'##molecule_type DNA !'##residues 1-184 ##label HAM COMMENT The genome consists of two circular, single-stranded DNA !1components, DNA A and DNA B. There are six potential coding !1regions, four in DNA A and two in DNA B. This protein is !1coded by DNA B. GENETICS !$#map_position segment B CLASSIFICATION #superfamily tomato golden mosaic virus BL1 protein SUMMARY #length 184 #molecular-weight 21122 #checksum 6350 SEQUENCE /// ENTRY JQ1874 #type complete TITLE BL1 protein - tomato mottle virus (isolate Florida) ORGANISM #formal_name tomato mottle virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 07-May-1999 ACCESSIONS JQ1874 REFERENCE JQ1869 !$#authors Abouzid, A.M.; Polston, J.E.; Hiebert, E. !$#journal J. Gen. Virol. (1992) 73:3225-3229 !$#title The nucleotide sequence of tomato mottle virus, a new !1geminivirus isolated from tomatoes in Florida. !$#cross-references MUID:93107858; PMID:1469361 !$#accession JQ1874 !'##status translation not shown !'##molecule_type DNA !'##residues 1-280 ##label ABO !'##cross-references GB:L14461 GENETICS !$#map_position segment B CLASSIFICATION #superfamily tomato golden mosaic virus BL1 protein SUMMARY #length 280 #molecular-weight 31872 #checksum 7747 SEQUENCE /// ENTRY QQCVW6 #type complete TITLE BC1 protein - abutilon mosaic virus (isolate West India) ORGANISM #formal_name abutilon mosaic virus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 23-Jul-1999 ACCESSIONS F36214 REFERENCE A36214 !$#authors Frischmuth, T.; Zimmat, G.; Jeske, H. !$#journal Virology (1990) 178:461-468 !$#title The nucleotide sequence of the abutilon mosaic virus reveals !1prokaryotic as well as eukaryotic features. !$#cross-references MUID:91020984; PMID:2219703 !$#accession F36214 !'##status translation not shown !'##molecule_type DNA !'##residues 1-292 ##label FRI !'##cross-references EMBL:X15984; NID:g59353; PIDN:CAA34115.1; !1PID:g59355 GENETICS !$#map_position segment B CLASSIFICATION #superfamily tomato golden mosaic virus BL1 protein SUMMARY #length 292 #molecular-weight 32939 #checksum 1874 SEQUENCE /// ENTRY QQCVPY #type complete TITLE BL1 protein - potato yellow mosaic virus (isolate Venezuela) ORGANISM #formal_name potato yellow mosaic virus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jun-2000 ACCESSIONS JU0362 REFERENCE JU0362 !$#authors Coutts, R.H.A.; Coffin, R.S.; Roberts, E.J.F.; Hamilton, !1W.D.O. !$#journal J. Gen. Virol. (1991) 72:1515-1520 !$#title The nucleotide sequence of the infectious cloned DNA !1components of potato yellow mosaic virus. !$#cross-references MUID:91311403; PMID:1856690 !$#accession JU0362 !'##status translation not shown !'##molecule_type DNA !'##residues 1-293 ##label COU !'##cross-references GB:D00941; NID:g222463; PIDN:BAA00784.1; !1PID:g222465 GENETICS !$#map_position segment B CLASSIFICATION #superfamily tomato golden mosaic virus BL1 protein SUMMARY #length 293 #molecular-weight 33279 #checksum 3711 SEQUENCE /// ENTRY QQCVBV #type complete TITLE BL1 protein - squash leaf curl virus ORGANISM #formal_name squash leaf curl virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 23-Jul-1999 ACCESSIONS B36785 REFERENCE A36785 !$#authors Lazarowitz, S.G.; Lazdins, I.B. !$#journal Virology (1991) 180:58-69 !$#title Infectivity and complete nucleotide sequence of the cloned !1genomic components of a bipartite squash leaf curl !1geminivirus with a broad host range phenotype. !$#cross-references MUID:91082449; PMID:1984668 !$#accession B36785 !'##status translation not shown !'##molecule_type DNA !'##residues 1-293 ##label LAZ !'##cross-references GB:M38182; NID:g335000; PIDN:AAC32409.1; !1PID:g335002 GENETICS !$#map_position segment B CLASSIFICATION #superfamily tomato golden mosaic virus BL1 protein SUMMARY #length 293 #molecular-weight 33178 #checksum 2643 SEQUENCE /// ENTRY QQCVB2 #type complete TITLE C4 protein - tomato yellow leaf curl virus ORGANISM #formal_name tomato yellow leaf curl virus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 18-Nov-1994 ACCESSIONS F40779 REFERENCE A40779 !$#authors Navot, N.; Pichersky, E.; Zeidan, M.; Zamir, D.; Czosnek, H. !$#journal Virology (1991) 185:151-161 !$#title Tomato yellow leaf curl virus: a whitefly-transmitted !1geminivirus with a single genomic component. !$#cross-references MUID:92024070; PMID:1926771 !$#accession F40779 !'##status translation not shown !'##molecule_type DNA !'##residues 1-96 ##label NAV !'##cross-references GB:X15656 CLASSIFICATION #superfamily tomato yellow leaf curl virus C4 protein SUMMARY #length 96 #molecular-weight 10935 #checksum 1890 SEQUENCE /// ENTRY JQ1890 #type complete TITLE C4 protein - tomato yellow leaf curl virus (strain Australia) ORGANISM #formal_name tomato yellow leaf curl virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 07-May-1999 ACCESSIONS JQ1890 REFERENCE JQ1885 !$#authors Dry, I.B.; Rigden, J.E.; Krake, L.R.; Mullineaux, P.M.; !1Rezaian, M.A. !$#journal J. Gen. Virol. (1993) 74:147-151 !$#title Nucleotide sequence and genome organization of tomato leaf !1curl geminivirus. !$#cross-references MUID:93139778; PMID:8423446 !$#accession JQ1890 !'##status translation not shown !'##molecule_type DNA !'##residues 1-102 ##label DRY !'##cross-references GB:S53251 CLASSIFICATION #superfamily tomato yellow leaf curl virus C4 protein SUMMARY #length 102 #molecular-weight 11410 #checksum 1606 SEQUENCE /// ENTRY QQCVL1 #type complete TITLE AL1 protein - tomato golden mosaic virus ORGANISM #formal_name tomato golden mosaic virus #note host Nicotiana sp. (tobacco) DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 08-Apr-1994 ACCESSIONS A04170 REFERENCE A04163 !$#authors Hamilton, W.D.O.; Stein, V.E.; Coutts, R.H.A.; Buck, K.W. !$#journal EMBO J. (1984) 3:2197-2205 !$#title Complete nucleotide sequence of the infectious cloned DNA !1components of tomato golden mosaic virus: potential coding !1regions and regulatory sequences. !$#accession A04170 !'##molecule_type DNA !'##residues 1-352 ##label HAM COMMENT The genome consists of two circular, single-stranded DNA !1components, DNA A and DNA B. There are six potential coding !1regions, four in DNA A and two in DNA B. This protein is !1coded by DNA A. GENETICS !$#map_position segment A CLASSIFICATION #superfamily tomato golden mosaic virus AL1 protein SUMMARY #length 352 #molecular-weight 40332 #checksum 755 SEQUENCE /// ENTRY QQCVW1 #type complete TITLE AV1 protein - abutilon mosaic virus (isolate West India) ORGANISM #formal_name abutilon mosaic virus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 08-Apr-1994 ACCESSIONS A36214 REFERENCE A36214 !$#authors Frischmuth, T.; Zimmat, G.; Jeske, H. !$#journal Virology (1990) 178:461-468 !$#title The nucleotide sequence of the abutilon mosaic virus reveals !1prokaryotic as well as eukaryotic features. !$#cross-references MUID:91020984; PMID:2219703 !$#accession A36214 !'##molecule_type DNA !'##residues 1-355 ##label FRI !'##cross-references EMBL:X15983 GENETICS !$#map_position segment A CLASSIFICATION #superfamily tomato golden mosaic virus AL1 protein SUMMARY #length 355 #molecular-weight 40257 #checksum 4263 SEQUENCE /// ENTRY QQCVPT #type complete TITLE AL1 protein - potato yellow mosaic virus (isolate Venezuela) ORGANISM #formal_name potato yellow mosaic virus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jun-2000 ACCESSIONS JU0364 REFERENCE JU0362 !$#authors Coutts, R.H.A.; Coffin, R.S.; Roberts, E.J.F.; Hamilton, !1W.D.O. !$#journal J. Gen. Virol. (1991) 72:1515-1520 !$#title The nucleotide sequence of the infectious cloned DNA !1components of potato yellow mosaic virus. !$#cross-references MUID:91311403; PMID:1856690 !$#accession JU0364 !'##status translation not shown !'##molecule_type DNA !'##residues 1-361 ##label COU !'##cross-references GB:D00940; NID:g222458; PIDN:BAA00782.1; !1PID:g222459 GENETICS !$#map_position segment A CLASSIFICATION #superfamily tomato golden mosaic virus AL1 protein SUMMARY #length 361 #molecular-weight 40850 #checksum 7479 SEQUENCE /// ENTRY QQCVC1 #type complete TITLE AL1 protein - tomato yellow leaf curl virus ALTERNATE_NAMES C1 protein ORGANISM #formal_name tomato yellow leaf curl virus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 23-Jul-1999 ACCESSIONS D40779 REFERENCE A40779 !$#authors Navot, N.; Pichersky, E.; Zeidan, M.; Zamir, D.; Czosnek, H. !$#journal Virology (1991) 185:151-161 !$#title Tomato yellow leaf curl virus: a whitefly-transmitted !1geminivirus with a single genomic component. !$#cross-references MUID:92024070; PMID:1926771 !$#accession D40779 !'##status translation not shown !'##molecule_type DNA !'##residues 1-357 ##label NAV !'##cross-references GB:X15656; NID:g62204; PIDN:CAA33688.1; PID:g62207 CLASSIFICATION #superfamily tomato golden mosaic virus AL1 protein SUMMARY #length 357 #molecular-weight 40678 #checksum 7160 SEQUENCE /// ENTRY JQ1887 #type complete TITLE AL1 protein - tomato yellow leaf curl virus (strain Australia) ALTERNATE_NAMES C1 protein ORGANISM #formal_name tomato yellow leaf curl virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 07-May-1999 ACCESSIONS JQ1887 REFERENCE JQ1885 !$#authors Dry, I.B.; Rigden, J.E.; Krake, L.R.; Mullineaux, P.M.; !1Rezaian, M.A. !$#journal J. Gen. Virol. (1993) 74:147-151 !$#title Nucleotide sequence and genome organization of tomato leaf !1curl geminivirus. !$#cross-references MUID:93139778; PMID:8423446 !$#accession JQ1887 !'##status translation not shown !'##molecule_type DNA !'##residues 1-362 ##label DRY !'##cross-references GB:S53251 CLASSIFICATION #superfamily tomato golden mosaic virus AL1 protein SUMMARY #length 362 #molecular-weight 41197 #checksum 2220 SEQUENCE /// ENTRY QQCVS1 #type complete TITLE AL1 protein - squash leaf curl virus ORGANISM #formal_name squash leaf curl virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 18-Nov-1994 ACCESSIONS C36785 REFERENCE A36785 !$#authors Lazarowitz, S.G.; Lazdins, I.B. !$#journal Virology (1991) 180:58-69 !$#title Infectivity and complete nucleotide sequence of the cloned !1genomic components of a bipartite squash leaf curl !1geminivirus with a broad host range phenotype. !$#cross-references MUID:91082449; PMID:1984668 !$#accession C36785 !'##status translation not shown !'##molecule_type DNA !'##residues 1-347 ##label LAZ !'##cross-references GB:M38183 GENETICS !$#map_position segment A !$#introns 10/1 CLASSIFICATION #superfamily tomato golden mosaic virus AL1 protein SUMMARY #length 347 #molecular-weight 39110 #checksum 4581 SEQUENCE /// ENTRY JQ1870 #type complete TITLE AL1 protein - tomato mottle virus (isolate Florida) ORGANISM #formal_name tomato mottle virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 07-May-1999 ACCESSIONS JQ1870 REFERENCE JQ1869 !$#authors Abouzid, A.M.; Polston, J.E.; Hiebert, E. !$#journal J. Gen. Virol. (1992) 73:3225-3229 !$#title The nucleotide sequence of tomato mottle virus, a new !1geminivirus isolated from tomatoes in Florida. !$#cross-references MUID:93107858; PMID:1469361 !$#accession JQ1870 !'##status translation not shown !'##molecule_type DNA !'##residues 1-358 ##label ABO !'##cross-references GB:L14460 GENETICS !$#map_position segment A CLASSIFICATION #superfamily tomato golden mosaic virus AL1 protein SUMMARY #length 358 #molecular-weight 40191 #checksum 4511 SEQUENCE /// ENTRY QQCVPZ #type complete TITLE P1 polyprotein - maize streak virus (Kenyan isolate) CONTAINS P1a protein; P1b protein ORGANISM #formal_name maize streak virus #note host Zea mays (maize) DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 04-Oct-1996 ACCESSIONS A04171 REFERENCE A93538 !$#authors Howell, S.H. !$#journal Nucleic Acids Res. (1984) 12:7359-7375 !$#title Physical structure and genetic organisation of the genome of !1maize streak virus (Kenyan isolate). !$#cross-references MUID:85037917; PMID:6493977 !$#accession A04171 !'##molecule_type DNA !'##residues 1-411 ##label HOW CLASSIFICATION #superfamily tomato golden mosaic virus AL1 protein KEYWORDS polyprotein FEATURE !$1-272 #product P1a protein #status predicted #label HPA\ !$273-411 #product P1b protein #status predicted #label HPB SUMMARY #length 411 #molecular-weight 47150 #checksum 8765 SEQUENCE /// ENTRY VCCVZ #type complete TITLE coat protein - maize streak virus (Kenyan isolate) ORGANISM #formal_name maize streak virus #note host Zea mays (maize) DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 16-Jun-2000 ACCESSIONS A04172 REFERENCE A93538 !$#authors Howell, S.H. !$#journal Nucleic Acids Res. (1984) 12:7359-7375 !$#title Physical structure and genetic organisation of the genome of !1maize streak virus (Kenyan isolate). !$#cross-references MUID:85037917; PMID:6493977 !$#accession A04172 !'##molecule_type DNA !'##residues 1-244 ##label HOW !'##cross-references GB:X01089; NID:g59364; PIDN:CAB37352.1; !1PID:g4456135 CLASSIFICATION #superfamily maize streak virus coat protein KEYWORDS coat protein SUMMARY #length 244 #molecular-weight 26879 #checksum 9521 SEQUENCE /// ENTRY VCCVSV #type complete TITLE coat protein - maize streak virus (Nigerian isolate) ORGANISM #formal_name maize streak virus DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 23-Jul-1999 ACCESSIONS A04173 REFERENCE A90997 !$#authors Mullineaux, P.M.; Donson, J.; Morris-Krsinich, B.A.M.; !1Boulton, M.I.; Davies, J.W. !$#journal EMBO J. (1984) 3:3063-3068 !$#title The nucleotide sequence of maize streak virus DNA. !$#cross-references MUID:85126910; PMID:6526009 !$#accession A04173 !'##molecule_type DNA !'##residues 1-244 ##label MUL !'##cross-references GB:X01633; GB:K02026; NID:g59357; PIDN:CAA25788.1; !1PID:g59358 CLASSIFICATION #superfamily maize streak virus coat protein KEYWORDS coat protein SUMMARY #length 244 #molecular-weight 26968 #checksum 9420 SEQUENCE /// ENTRY JQ1550 #type complete TITLE coat protein - Panicum streak virus (Kenyan isolate) ORGANISM #formal_name Panicum streak virus #note host Panicum maximum (guinea grass) DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 23-Jul-1999 ACCESSIONS JQ1550 REFERENCE JQ1549 !$#authors Briddon, R.W.; Lunness, P.; Chamberlin, L.C.L.; Pinner, !1M.S.; Brundish, H.; Markham, P.G. !$#journal J. Gen. Virol. (1992) 73:1041-1047 !$#title The nucleotide sequence of an infections !1insect-transmissible clone of the geminivirus Panicum streak !1virus. !$#cross-references MUID:92268861; PMID:1588314 !$#accession JQ1550 !'##molecule_type DNA !'##residues 1-247 ##label BRI !'##cross-references EMBL:X60168; NID:g61358; PIDN:CAA42734.1; !1PID:g61360 !'##note the authors translated the codons CTC for residue 138 as His !1and GTT for residue 244 as Asn CLASSIFICATION #superfamily maize streak virus coat protein KEYWORDS coat protein SUMMARY #length 247 #molecular-weight 27183 #checksum 659 SEQUENCE /// ENTRY VCCVWV #type complete TITLE coat protein - wheat dwarf virus ORGANISM #formal_name wheat dwarf virus DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 08-Apr-1994 ACCESSIONS A25005; A24356 REFERENCE A91012 !$#authors MacDowell, S.W.; Macdonald, H.; Hamilton, W.D.O.; Coutts, !1R.H.A.; Buck, K.W. !$#journal EMBO J. (1985) 4:2173-2180 !$#title The nucleotide sequence of cloned wheat dwarf virus DNA. !$#accession A25005 !'##molecule_type DNA !'##residues 1-260 ##label MAC !'##note the authors translated the codon AAG for residue 5 as Arg CLASSIFICATION #superfamily maize streak virus coat protein KEYWORDS coat protein SUMMARY #length 260 #molecular-weight 29408 #checksum 2085 SEQUENCE /// ENTRY VCCVMS #type complete TITLE coat protein - Miscanthus streak virus ORGANISM #formal_name Miscanthus streak virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jun-2000 ACCESSIONS JQ1357; JQ0920 REFERENCE JQ1355 !$#authors Chatani, M.; Matsumoto, Y.; Mizuta, H.; Ikegami, M.; !1Boulton, M.I.; Davies, J.W. !$#journal J. Gen. Virol. (1991) 72:2325-2331 !$#title The nucleotide sequence and genome structure of the !1geminivirus miscanthus streak virus. !$#cross-references MUID:92013947; PMID:1919519 !$#accession JQ1357 !'##status translation not shown !'##molecule_type DNA !'##residues 1-255 ##label CHA !'##cross-references DDBJ:D01030; NID:g222128; PIDN:BAA00833.1; !1PID:g222131 CLASSIFICATION #superfamily maize streak virus coat protein KEYWORDS coat protein SUMMARY #length 255 #molecular-weight 28176 #checksum 3631 SEQUENCE /// ENTRY VCCVTY #type complete TITLE coat protein - tobacco yellow dwarf virus (strain Australia) ORGANISM #formal_name tobacco yellow dwarf virus DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 23-Jul-1999 ACCESSIONS B42452 REFERENCE A42452 !$#authors Morris, B.A.M.; Richardson, K.A.; Haley, A.; Zhan, X.; !1Thomas, J.E. !$#journal Virology (1992) 187:633-642 !$#title The nucleotide sequence of the infectious cloned DNA !1component of tobacco yellow dwarf virus reveals features of !1geminiviruses infecting monocotyledonous plants. !$#cross-references MUID:92188538; PMID:1546458 !$#accession B42452 !'##status translation not shown !'##molecule_type DNA !'##residues 1-254 ##label MOR !'##cross-references GB:M81103; NID:g335283; PIDN:AAA47948.1; !1PID:g335285 CLASSIFICATION #superfamily maize streak virus coat protein KEYWORDS coat protein SUMMARY #length 254 #molecular-weight 28583 #checksum 2493 SEQUENCE /// ENTRY WMWGP4 #type complete TITLE 8K protein - potato virus X (strain X3) ORGANISM #formal_name potato virus X, PVX #note host Nicotiana tabacum cv. Samsun (tobacco) DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jun-2000 ACCESSIONS JA0105 REFERENCE JA0102 !$#authors Huisman, M.J.; Linthorst, H.J.M.; Bol, J.F.; Cornelissen, !1B.J.C. !$#journal J. Gen. Virol. (1988) 69:1789-1798 !$#title The complete nucleotide sequence of potato virus X and its !1homologies at the amino acid level with various !1plus-stranded RNA viruses. !$#cross-references MUID:88299944; PMID:3404114 !$#accession JA0105 !'##molecule_type mRNA !'##residues 1-70 ##label HUI !'##cross-references DDBJ:D00344; NID:g222441; PIDN:BAA00252.1; !1PID:g222445 CLASSIFICATION #superfamily potato virus 7.5K protein SUMMARY #length 70 #molecular-weight 7595 #checksum 1211 SEQUENCE /// ENTRY VCTMVU #type complete TITLE coat protein - tobacco mosaic virus (strains Vulgare and NC 82) ORGANISM #formal_name tobacco mosaic virus, TMV DATE 12-Aug-1981 #sequence_revision 18-Mar-1997 #text_change 31-Mar-2000 ACCESSIONS S26360; A04174; B04174; C04174; D04174 REFERENCE S26358 !$#authors Koh, H.K.; Song, E.K.; Lee, S.Y.; Park, Y.I.; Park, W.M. !$#journal Nucleic Acids Res. (1992) 20:5474 !$#title Nucleotide sequence of cDNA of the tobacco mosaic virus RNA !1isolated in Korea. !$#cross-references MUID:93065219; PMID:1437566 !$#accession S26360 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type mRNA !'##residues 1-159 ##label KOH !'##cross-references EMBL:X68110 !'##experimental_source strain NC 82 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1992 REFERENCE A93926 !$#authors Goelet, P.; Lomonossoff, G.P.; Butler, P.J.G.; Akam, M.E.; !1Gait, M.J.; Karn, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:5818-5822 !$#title Nucleotide sequence of tobacco mosaic virus RNA. !$#cross-references MUID:83299880; PMID:6964389 !$#accession A04174 !'##molecule_type genomic RNA !'##residues 2-159 ##label GOE !'##cross-references GB:J02415; NID:g332233; PID:g332239 REFERENCE A93691 !$#authors Guilley, H.; Jonard, G.; Kukla, B.; Richards, K.E. !$#journal Nucleic Acids Res. (1979) 6:1287-1308 !$#title Sequence of 1000 nucleotides at the 3' end of tobacco mosaic !1virus RNA. !$#cross-references MUID:79201054; PMID:109810 !$#accession B04174 !'##molecule_type genomic RNA !'##residues 2-159 ##label GUI !'##cross-references GB:V01406; NID:g62119; PIDN:CAA24685.1; PID:g62120 !'##experimental_source strain Vulgare REFERENCE A90044 !$#authors Funatsu, G.; Tsugita, A.; Fraenkel-Conrat, H. !$#journal Arch. Biochem. Biophys. (1964) 105:25-41 !$#title Studies on the amino acid sequence of tobacco mosaic virus !1protein. V. Amino acid sequences of two peptides from !1tryptic digests and location of amide group. !$#accession C04174 !'##molecule_type protein !'##residues 2-42;94-113 ##label FUN REFERENCE A94401 !$#authors Anderer, F.A.; Handschuh, D. !$#journal Z. Naturforsch. B (1962) 17:536-543 !$#title Die reihenfolge der aminosauren im protein des !1tabakmosaikvirus. !$#accession D04174 !'##molecule_type protein !'##residues 2-44,'QV',47-50,'Q',52-97,'Q',99-106,'Q',108-125,'DI', !1128-159 ##label AND CLASSIFICATION #superfamily tobacco mosaic virus coat protein KEYWORDS acetylated amino end; coat protein FEATURE !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental SUMMARY #length 159 #molecular-weight 17624 #checksum 6791 SEQUENCE /// ENTRY VCTMOM #type complete TITLE coat protein - tobacco mosaic virus (strain OM) ORGANISM #formal_name tobacco mosaic virus, TMV DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 05-Aug-1994 ACCESSIONS A91925 REFERENCE A91925 !$#authors Nozu, Y.; Ohno, T.; Okada, Y. !$#journal J. Biochem. (1970) 68:39-52 !$#title Amino acid sequences of some common Japanese strains of !1tobacco mosaic virus. !$#cross-references MUID:70269749; PMID:5452764 !$#accession A91925 !'##molecule_type protein !'##residues 1-158 ##label NOZ CLASSIFICATION #superfamily tobacco mosaic virus coat protein KEYWORDS acetylated amino end; coat protein FEATURE !$1 #modified_site acetylated amino end (Ser) #status !8experimental SUMMARY #length 158 #molecular-weight 17491 #checksum 3941 SEQUENCE /// ENTRY VCTMKO #type complete TITLE coat protein - tobacco mosaic virus (strains Kokubu and O) ORGANISM #formal_name tobacco mosaic virus, TMV DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 18-Jun-1999 ACCESSIONS C91925; B91925 REFERENCE A91925 !$#authors Nozu, Y.; Ohno, T.; Okada, Y. !$#journal J. Biochem. (1970) 68:39-52 !$#title Amino acid sequences of some common Japanese strains of !1tobacco mosaic virus. !$#cross-references MUID:70269749; PMID:5452764 !$#accession C91925 !'##molecule_type protein !'##residues 1-158 ##label NOZ !'##experimental_source strain Kokubu !$#accession B91925 !'##molecule_type protein !'##residues 1-158 ##label NO2 !'##experimental_source strain O CLASSIFICATION #superfamily tobacco mosaic virus coat protein KEYWORDS acetylated amino end; coat protein FEATURE !$1 #modified_site acetylated amino end (Ser) #status !8experimental SUMMARY #length 158 #molecular-weight 17478 #checksum 4175 SEQUENCE /// ENTRY VCTMDA #type complete TITLE coat protein - tobacco mosaic virus (strain dahlemense) ORGANISM #formal_name tobacco mosaic virus, TMV DATE 12-Aug-1981 #sequence_revision 12-Aug-1981 #text_change 31-Mar-2000 ACCESSIONS A04175; A94402 REFERENCE A94407 !$#authors Wittmann-Liebold, B.; Wittmann, H.G. !$#journal Z. Vererbungsl. (1963) 94:427-435 !$#title Die primare proteinstruktur von stammen des !1tabakmosaikvirus. !$#accession A04175 !'##molecule_type protein !'##residues 1-158 ##label WIT REFERENCE A94402 !$#authors Anderer, F.A.; Wittmann-Liebold, B.; Wittmann, H.G. !$#journal Z. Naturforsch. B (1965) 20:1203-1213 !$#title Weitere Untersuchungen zur aminosauresequenz des proteins im !1tabakmosaikvirus. !$#cross-references MUID:67124537; PMID:4381389 !$#contents revisions !$#accession A94402 !'##molecule_type protein !'##residues 44-48;123-134 ##label AND CLASSIFICATION #superfamily tobacco mosaic virus coat protein KEYWORDS acetylated amino end; coat protein FEATURE !$1 #modified_site acetylated amino end (Ser) #status !8experimental SUMMARY #length 158 #molecular-weight 17618 #checksum 5410 SEQUENCE /// ENTRY VCTMTO #type complete TITLE coat protein - tomato mosaic virus (strain L) ORGANISM #formal_name tomato mosaic virus #note host (tomato) DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 03-Dec-1999 ACCESSIONS A04176 REFERENCE A91984 !$#authors Ohno, T.; Aoyagi, M.; Yamanashi, Y.; Saito, H.; Ikawa, S.; !1Meshi, T.; Okada, Y. !$#journal J. Biochem. (1984) 96:1915-1923 !$#title Nucleotide sequence of the tobacco mosaic virus (tomato !1strain) genome and comparison with the common strain genome. !$#cross-references MUID:85157522; PMID:6549393 !$#accession A04176 !'##molecule_type genomic RNA !'##residues 1-159 ##label OHN !'##cross-references GB:X02144; NID:g62128; PIDN:CAA26084.1; PID:g62131 CLASSIFICATION #superfamily tobacco mosaic virus coat protein KEYWORDS acetylated amino end; coat protein FEATURE !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status predicted SUMMARY #length 159 #molecular-weight 17746 #checksum 7583 SEQUENCE /// ENTRY VCTMDB #type complete TITLE coat protein - tobacco mosaic virus (strain tomato) ORGANISM #formal_name tobacco mosaic virus, TMV DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 03-Dec-1999 ACCESSIONS B04175; A04175 REFERENCE A93473 !$#authors Takamatsu, N.; Ohno, T.; Meshi, T.; Okada, Y. !$#journal Nucleic Acids Res. (1983) 11:3767-3778 !$#title Molecular cloning and nucleotide sequence of the 30k and the !1coat protein cistron of tmv (tomato strain) genome. !$#cross-references MUID:83220776; PMID:6304642 !$#accession B04175 !'##molecule_type genomic RNA !'##residues 1-158 ##label TAK !'##cross-references GB:X02144 CLASSIFICATION #superfamily tobacco mosaic virus coat protein KEYWORDS acetylated amino end; coat protein FEATURE !$1 #modified_site acetylated amino end (Ser) #status !8predicted SUMMARY #length 158 #molecular-weight 17615 #checksum 4709 SEQUENCE /// ENTRY VCTMOR #type complete TITLE coat protein - tobacco mosaic virus (strain ORS) (tentative sequence) ORGANISM #formal_name tobacco mosaic virus, TMV DATE 12-Aug-1981 #sequence_revision 12-Aug-1981 #text_change 31-Mar-2000 ACCESSIONS A94453; A94557; A04177 REFERENCE A94453 !$#authors Hennig, B. !$#citation Ph.D. thesis, University of Tubingen, 1970 !$#accession A94453 !'##molecule_type protein !'##residues 1-157 ##label HEN REFERENCE A94557 !$#authors Hennig, B. !$#submission submitted to the Atlas, August 1970 !$#accession A94557 !'##molecule_type protein !'##residues 1-157 ##label HE2 !'##experimental_source Odontoglossum ringspot strain CLASSIFICATION #superfamily tobacco mosaic virus coat protein KEYWORDS acetylated amino end FEATURE !$1 #modified_site acetylated amino end (Ser) #status !8experimental SUMMARY #length 157 #molecular-weight 17597 #checksum 3994 SEQUENCE /// ENTRY VCTMU2 #type complete TITLE coat protein - tobacco mosaic virus (strain U2) (tentative sequence) ORGANISM #formal_name tobacco mosaic virus, TMV DATE 12-Aug-1981 #sequence_revision 12-Aug-1981 #text_change 31-Mar-2000 ACCESSIONS A94403; A93116; A04178 REFERENCE A94403 !$#authors Wittmann, H.G. !$#journal Z. Naturforsch. B (1965) 20:1213-1223 !$#title Die primaere Proteinstruktur von Staemmen des !1Tabakmosaikvirus. !$#cross-references MUID:67124538; PMID:4381390 !$#accession A94403 !'##molecule_type protein !'##residues 1-61;135-158 ##label WIT REFERENCE A93116 !$#authors Rentschler, L. !$#journal Mol. Gen. Genet. (1967) 100:84-95 !$#title Aminosaeuresequenzen und Physikochemisches Verhalten des !1Hullproteins eines Wildstammes des Tabakmosaikvirus. !$#cross-references MUID:68236437; PMID:5586539 !$#accession A93116 !'##molecule_type protein !'##residues 62-134 ##label REN CLASSIFICATION #superfamily tobacco mosaic virus coat protein SUMMARY #length 158 #molecular-weight 17460 #checksum 4155 SEQUENCE /// ENTRY VCTMUT #type complete TITLE coat protein - tobacco mild green mosaic virus (strain U2-TMV) ORGANISM #formal_name tobacco mild green mosaic virus #note host Nicotiana tabacum cv. Samsun (tobacco) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 23-Jul-1999 ACCESSIONS C35520 REFERENCE A35520 !$#authors Solis, I.; Garcia-Arenal, F. !$#journal Virology (1990) 177:553-558 !$#title The complete nucleotide sequence of the genomic RNA of the !1tobamovirus tobacco mild green mosaic virus. !$#cross-references MUID:90320127; PMID:2371769 !$#accession C35520 !'##molecule_type genomic RNA !'##residues 1-159 ##label SOL !'##cross-references EMBL:M34077; NID:g335243; PIDN:AAA47937.1; !1PID:g335247 CLASSIFICATION #superfamily tobacco mosaic virus coat protein KEYWORDS coat protein SUMMARY #length 159 #molecular-weight 17590 #checksum 6010 SEQUENCE /// ENTRY VCTMPV #type complete TITLE coat protein - pepper mild mottle virus (strain Spain) ORGANISM #formal_name pepper mild mottle virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 03-Dec-1999 ACCESSIONS JQ1315 REFERENCE JQ1312 !$#authors Alonso, E.; Garcia-Luque, I.; de la Cruz, A.; Wicke, B.; !1Avila-Rincon, M.J.; Serra, M.T.; Castresana, C.; Diaz-Ruiz, !1J.R. !$#journal J. Gen. Virol. (1991) 72:2875-2884 !$#title Nucleotide sequence of the genomic RNA of pepper mild mottle !1virus, a resistance-breaking tobamovirus in pepper. !$#cross-references MUID:92113528; PMID:1765765 !$#accession JQ1315 !'##molecule_type genomic RNA !'##residues 1-157 ##label ALO !'##cross-references GB:M81413; NID:g333293; PIDN:AAB02337.1; !1PID:g333297 !'##note the authors translated the codon AAT for residue 26 as Ala, CAA !1for residue 46 as Gly, and GAG for residue 146 as Gly CLASSIFICATION #superfamily tobacco mosaic virus coat protein KEYWORDS acetylated amino end; coat protein FEATURE !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status predicted SUMMARY #length 157 #molecular-weight 17241 #checksum 9298 SEQUENCE /// ENTRY VCTMHR #type complete TITLE coat protein - tobacco mosaic virus (strain HR) ORGANISM #formal_name tobacco mosaic virus, TMV DATE 12-Aug-1981 #sequence_revision 12-Aug-1981 #text_change 05-Aug-1994 ACCESSIONS A94404; A94405; A90039; A04179 REFERENCE A94404 !$#authors Jauregui-Adell, J.; Hindennach, I.; Wittmann, H.G. !$#journal Z. Naturforsch. B (1969) 24:870-877 !$#title Sequence of amino acids (1-61) within the protein of the !1strain Holmes rib grass of tobacco mosaic virus. !$#cross-references MUID:69279982; PMID:4390042 !$#accession A94404 !'##molecule_type protein !'##residues 1-61 ##label JAU !'##experimental_source strain Holmes ribgrass REFERENCE A94405 !$#authors Wittmann, H.G.; Hindennach, I.; Wittmann-Liebold, B. !$#journal Z. Naturforsch. B (1969) 24:877-885 !$#title Teil VI: Aminosaeurensequenz (Positionen 62-156) des !1Proteins des Tabakmosaikvirusstammes Holmes Rib Grass. !$#cross-references MUID:69279983; PMID:4390043 !$#accession A94405 !'##molecule_type protein !'##residues 62-156 ##label WIT REFERENCE A90039 !$#authors Funatsu, G.; Funatsu, M. !$#journal Ann. Phytopathol. Soc. Jpn. (1968) 43:1-9 !$#title Chemical studies on proteins from two tobacco mosaic virus !1strains. !$#accession A90039 !'##molecule_type protein !'##residues 1-94,'E',96-98,'E',100-108,'D',110-139,'D',141-142,'Q', !1144-156 ##label FUN CLASSIFICATION #superfamily tobacco mosaic virus coat protein KEYWORDS acetylated amino end FEATURE !$1 #modified_site acetylated amino end (Ser) #status !8experimental SUMMARY #length 156 #molecular-weight 17510 #checksum 5794 SEQUENCE /// ENTRY VCTMCP #type complete TITLE coat protein - sunnhemp mosaic virus ORGANISM #formal_name sunnhemp mosaic virus DATE 12-Aug-1981 #sequence_revision 12-Aug-1981 #text_change 05-Aug-1994 ACCESSIONS A04180 REFERENCE A90602 !$#authors Rees, M.W.; Short, M.N. !$#journal Biochim. Biophys. Acta (1975) 393:15-23 !$#title The amino acid sequence of the cowpea strain of tobacco !1mosaic virus protein. !$#cross-references MUID:75184103; PMID:1138919 !$#accession A04180 !'##molecule_type protein !'##residues 1-161 ##label REE CLASSIFICATION #superfamily tobacco mosaic virus coat protein KEYWORDS acetylated amino end FEATURE !$1 #modified_site acetylated amino end (Ala) #status !8experimental SUMMARY #length 161 #molecular-weight 18017 #checksum 7655 SEQUENCE /// ENTRY VCTMSH #type complete TITLE coat protein - cucumber green mottle mosaic virus ORGANISM #formal_name cucumber green mottle mosaic virus DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jun-2000 ACCESSIONS JQ1160; PS0051; S42525; JT0685 REFERENCE JQ1157 !$#authors Ugaki, M.; Tomiyama, M.; Kakutani, T.; Hidaka, S.; Kiguchi, !1T.; Nagata, R.; Sato, T.; Motoyoshi, F.; Nishiguchi, M. !$#journal J. Gen. Virol. (1991) 72:1487-1495 !$#title The complete nucleotide sequence of cucumber green mottle !1mosaic virus (SH strain) genomic RNA. !$#cross-references MUID:91311400; PMID:1856687 !$#accession JQ1160 !'##molecule_type genomic RNA !'##residues 1-161 ##label UGA !'##cross-references GB:D12505; NID:g1902985; PIDN:BAA02071.1; !1PID:g222017 !'##experimental_source strain SH REFERENCE JS0261 !$#authors Saito, T.; Imai, Y.; Meshi, T.; Okada, Y. !$#journal Virology (1988) 167:653-656 !$#title Interviral homologies of the 30K proteins of tobamoviruses. !$#cross-references MUID:89073773; PMID:3201760 !$#accession PS0051 !'##molecule_type genomic RNA !'##residues 1-44 ##label SAI !'##cross-references GB:J04322; NID:g331644; PIDN:AAA46384.1; !1PID:g555241 !'##experimental_source strain watermelon REFERENCE S42525 !$#authors Meshi, T.; Kiyama, R.; Ohno, T.; Okada, Y. !$#journal Virology (1983) 127:54-64 !$#title Nucleotide sequence of the coat protein cistron and the 3' !1noncoding region of cucumber green mottle mosaic virus !1(watermelon strain) RNA. !$#accession S42525 !'##status preliminary !'##molecule_type mRNA !'##residues 1-161 ##label MES !'##cross-references GB:V01551; GB:J02054; NID:g62063; PIDN:CAA24792.1; !1PID:g62064 !'##experimental_source strain watermelon !'##note the authors did not translate the codon for residue 1 REFERENCE JT0685 !$#authors Nozu, Y.; Tsugita, A. !$#journal Plant Sci. (1986) 44:47-51 !$#title The amino acid sequence of cucumber green mottle mosaic !1virus (watermelon strain) protein. !$#accession JT0685 !'##molecule_type protein !'##residues 2-161 ##label NOZ !'##experimental_source strain watermelon CLASSIFICATION #superfamily tobacco mosaic virus coat protein KEYWORDS acetylated amino end; coat protein FEATURE !$2-161 #product coat protein #status experimental #label !8MAT\ !$2 #modified_site acetylated amino end (Ala) (in mature !8form) #status experimental SUMMARY #length 161 #molecular-weight 17394 #checksum 2805 SEQUENCE /// ENTRY VCTMST #type complete TITLE coat protein - tobacco mosaic satellite virus ORGANISM #formal_name tobacco mosaic satellite virus #note host Nicotiana tabacum (tobacco) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 23-Jul-1999 ACCESSIONS JA0135 REFERENCE A94393 !$#authors Mirkov, T.E.; Mathews, D.M.; Du Plessis, D.H.; Dodds, J.A. !$#journal Virology (1989) 170:139-146 !$#title Nucleotide sequence and translation of satellite tobacco !1mosaic virus RNA. !$#cross-references MUID:89243170; PMID:2718378 !$#accession JA0135 !'##molecule_type genomic RNA !'##residues 1-159 ##label MIR !'##cross-references GB:M25782; NID:g530201; PIDN:AAA47785.1; !1PID:g530203 COMMENT The genome is a single-stranded, positive-sense RNA. It !1codes for a 6.8K protein and a 17.5K protein. COMMENT This virus depends on tobacco mosaic virus for its !1replication. CLASSIFICATION #superfamily tobacco mosaic satellite virus coat protein KEYWORDS coat protein SUMMARY #length 159 #molecular-weight 17514 #checksum 6774 SEQUENCE /// ENTRY WMTM68 #type complete TITLE 6.8K protein - tobacco mosaic satellite virus ORGANISM #formal_name tobacco mosaic satellite virus #note host Nicotiana tabacum (tobacco) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 23-Jul-1999 ACCESSIONS JA0134 REFERENCE A94393 !$#authors Mirkov, T.E.; Mathews, D.M.; Du Plessis, D.H.; Dodds, J.A. !$#journal Virology (1989) 170:139-146 !$#title Nucleotide sequence and translation of satellite tobacco !1mosaic virus RNA. !$#cross-references MUID:89243170; PMID:2718378 !$#accession JA0134 !'##molecule_type mRNA !'##residues 1-58 ##label MIR !'##cross-references GB:M25782; NID:g530201; PIDN:AAA47784.1; !1PID:g530202 COMMENT The genome is a single-stranded, positive-sense RNA. It !1codes for a 6.8K protein and a 17.5K protein. COMMENT This virus depends on tobacco mosaic virus for its !1replication. CLASSIFICATION #superfamily tobacco mosaic satellite virus 6.8K protein SUMMARY #length 58 #molecular-weight 6750 #checksum 8990 SEQUENCE /// ENTRY WMTM30 #type complete TITLE 30K protein - tobacco mosaic virus ORGANISM #formal_name tobacco mosaic virus, TMV DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 23-Jul-1999 ACCESSIONS A91965; A93926; A04181 REFERENCE A91965 !$#authors Meshi, T.; Ohno, T.; Okada, Y. !$#journal J. Biochem. (1982) 91:1441-1444 !$#title Nucleotide sequence and its character of cistron coding for !1the 30 K protein of tobacco mosaic virus (OM strain). !$#cross-references MUID:82239259; PMID:7096297 !$#accession A91965 !'##molecule_type genomic RNA !'##residues 1-268 ##label MES !'##cross-references GB:V01407; NID:g62121; PIDN:CAA24686.1; PID:g62122 !'##experimental_source strain OM REFERENCE A93926 !$#authors Goelet, P.; Lomonossoff, G.P.; Butler, P.J.G.; Akam, M.E.; !1Gait, M.J.; Karn, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:5818-5822 !$#title Nucleotide sequence of tobacco mosaic virus RNA. !$#cross-references MUID:83299880; PMID:6964389 !$#accession A93926 !'##molecule_type genomic RNA !'##residues 1-179,'N',181-224,'N',226-227,'N',229-231,'V',233-259,'A', !1261-268 ##label GOE !'##cross-references GB:V01409; NID:g62125; PIDN:CAA24689.1; PID:g663265 !'##experimental_source strain Vulgare !'##note the sequence contains proteins 27.9K (residues 20-268), 25.3K !1(43-268), and 19.5K (97-268) CLASSIFICATION #superfamily tobravirus 30K protein KEYWORDS DNA binding SUMMARY #length 268 #molecular-weight 29951 #checksum 9976 SEQUENCE /// ENTRY WMBVT3 #type complete TITLE 30K protein - tomato mosaic virus (strain L) ORGANISM #formal_name tomato mosaic virus #note host (tomato) DATE 18-Apr-1984 #sequence_revision 18-Apr-1984 #text_change 16-Feb-1997 ACCESSIONS A04182 REFERENCE A93473 !$#authors Takamatsu, N.; Ohno, T.; Meshi, T.; Okada, Y. !$#journal Nucleic Acids Res. (1983) 11:3767-3778 !$#title Molecular cloning and nucleotide sequence of the 30k and the !1coat protein cistron of tmv (tomato strain) genome. !$#cross-references MUID:83220776; PMID:6304642 !$#accession A04182 !'##molecule_type genomic RNA !'##residues 1-264 ##label TAK CLASSIFICATION #superfamily tobravirus 30K protein KEYWORDS DNA binding SUMMARY #length 264 #molecular-weight 29291 #checksum 8439 SEQUENCE /// ENTRY WMBVL1 #type complete TITLE 30K protein - tomato mosaic virus (strain LIIA) ALTERNATE_NAMES transport protein ORGANISM #formal_name tomato mosaic virus DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Feb-1997 ACCESSIONS JQ1456 REFERENCE JQ1456 !$#authors Calder, V.L.; Palukaitis, P. !$#journal J. Gen. Virol. (1992) 73:165-168 !$#title Nucleotide sequence analysis of the movement genes of !1resistance breaking strains of tomato mosaic virus. !$#cross-references MUID:92113565; PMID:1730937 !$#accession JQ1456 !'##molecule_type genomic RNA !'##residues 1-264 ##label CAL !'##note the authors translated the codons TGG for residue 68 as Cys, !1AGT for residue 238 as Arg, and GTT for residue 239 as Phe COMMENT This protein is involved in cell-to-cell transport of the !1virus. CLASSIFICATION #superfamily tobravirus 30K protein KEYWORDS DNA binding; transport protein SUMMARY #length 264 #molecular-weight 29354 #checksum 8673 SEQUENCE /// ENTRY WMBVL2 #type complete TITLE 30K protein - tomato mosaic virus (strain LII) ALTERNATE_NAMES transport protein ORGANISM #formal_name tomato mosaic virus DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Feb-1997 ACCESSIONS JQ1457 REFERENCE JQ1456 !$#authors Calder, V.L.; Palukaitis, P. !$#journal J. Gen. Virol. (1992) 73:165-168 !$#title Nucleotide sequence analysis of the movement genes of !1resistance breaking strains of tomato mosaic virus. !$#cross-references MUID:92113565; PMID:1730937 !$#accession JQ1457 !'##molecule_type genomic RNA !'##residues 1-264 ##label CAL !'##note the authors translated the codon TGG for residue 68 as Cys COMMENT This protein is involved in cell-to-cell transport of the !1virus. CLASSIFICATION #superfamily tobravirus 30K protein KEYWORDS DNA binding; transport protein SUMMARY #length 264 #molecular-weight 29396 #checksum 8887 SEQUENCE /// ENTRY WMTMU2 #type complete TITLE 28.5K transport protein - tobacco mild green mosaic virus (strain U2-TMV) ALTERNATE_NAMES 28.5K movement protein ORGANISM #formal_name tobacco mild green mosaic virus #note host Nicotiana tabacum cv. Samsun (tobacco) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 23-Jul-1999 ACCESSIONS B35520 REFERENCE A35520 !$#authors Solis, I.; Garcia-Arenal, F. !$#journal Virology (1990) 177:553-558 !$#title The complete nucleotide sequence of the genomic RNA of the !1tobamovirus tobacco mild green mosaic virus. !$#cross-references MUID:90320127; PMID:2371769 !$#accession B35520 !'##molecule_type genomic RNA !'##residues 1-256 ##label SOL !'##cross-references EMBL:M34077; NID:g335243; PIDN:AAA47936.1; !1PID:g335246 COMMENT This protein may play a role in cell-to-cell transport. CLASSIFICATION #superfamily tobravirus 30K protein KEYWORDS DNA binding; transport protein SUMMARY #length 256 #molecular-weight 28441 #checksum 5800 SEQUENCE /// ENTRY WMTMP3 #type complete TITLE 30K protein - pepper mild mottle virus (strain Spain) ALTERNATE_NAMES movement protein; transport protein ORGANISM #formal_name pepper mild mottle virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 23-Jul-1999 ACCESSIONS JQ1314 REFERENCE JQ1312 !$#authors Alonso, E.; Garcia-Luque, I.; de la Cruz, A.; Wicke, B.; !1Avila-Rincon, M.J.; Serra, M.T.; Castresana, C.; Diaz-Ruiz, !1J.R. !$#journal J. Gen. Virol. (1991) 72:2875-2884 !$#title Nucleotide sequence of the genomic RNA of pepper mild mottle !1virus, a resistance-breaking tobamovirus in pepper. !$#cross-references MUID:92113528; PMID:1765765 !$#accession JQ1314 !'##molecule_type genomic RNA !'##residues 1-257 ##label ALO !'##cross-references GB:M81413; NID:g333293; PIDN:AAB02336.1; !1PID:g333296 COMMENT This protein participates in the cell-to-cell spread of the !1viral infection. CLASSIFICATION #superfamily tobravirus 30K protein KEYWORDS DNA binding; transport protein SUMMARY #length 257 #molecular-weight 28345 #checksum 9 SEQUENCE /// ENTRY WMTMCV #type complete TITLE 30K protein - cucumber green mottle mosaic virus (strain watermelon) ALTERNATE_NAMES movement protein; transport protein ORGANISM #formal_name cucumber green mottle mosaic virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 23-Jul-1999 ACCESSIONS JS0261 REFERENCE JS0261 !$#authors Saito, T.; Imai, Y.; Meshi, T.; Okada, Y. !$#journal Virology (1988) 167:653-656 !$#title Interviral homologies of the 30K proteins of tobamoviruses. !$#cross-references MUID:89073773; PMID:3201760 !$#accession JS0261 !'##molecule_type mRNA !'##residues 1-264 ##label SAI !'##cross-references GB:J04322; NID:g331644; PIDN:AAA46383.1; !1PID:g331646 !'##note the authors translated the codon GAA for residue 85 as Gly COMMENT This protein participates in the cell-to-cell spread of the !1viral infection. CLASSIFICATION #superfamily tobravirus 30K protein KEYWORDS DNA binding; transport protein SUMMARY #length 264 #molecular-weight 28881 #checksum 3982 SEQUENCE /// ENTRY WMTMSH #type complete TITLE 29K protein - cucumber green mottle mosaic virus (strain SH) ALTERNATE_NAMES movement protein; transport protein ORGANISM #formal_name cucumber green mottle mosaic virus DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 16-Jun-2000 ACCESSIONS JQ1159 REFERENCE JQ1157 !$#authors Ugaki, M.; Tomiyama, M.; Kakutani, T.; Hidaka, S.; Kiguchi, !1T.; Nagata, R.; Sato, T.; Motoyoshi, F.; Nishiguchi, M. !$#journal J. Gen. Virol. (1991) 72:1487-1495 !$#title The complete nucleotide sequence of cucumber green mottle !1mosaic virus (SH strain) genomic RNA. !$#cross-references MUID:91311400; PMID:1856687 !$#accession JQ1159 !'##molecule_type genomic RNA !'##residues 1-264 ##label UGA !'##cross-references GB:D12505; NID:g1902985; PIDN:BAA02070.1; !1PID:g222016 COMMENT This protein participates in the cell-to-cell spread of the !1viral infection. CLASSIFICATION #superfamily tobravirus 30K protein KEYWORDS DNA binding; transport protein SUMMARY #length 264 #molecular-weight 28875 #checksum 3953 SEQUENCE /// ENTRY WMTM3C #type complete TITLE 30K protein - tobacco mosaic virus (strain cowpea) ORGANISM #formal_name tobacco mosaic virus, TMV DATE 05-Apr-1983 #sequence_revision 05-Apr-1983 #text_change 23-Jul-1999 ACCESSIONS A04183 REFERENCE A04183 !$#authors Meshi, T.; Ohno, T.; Okada, Y. !$#journal Nucleic Acids Res. (1982) 10:6111-6117 !$#title Nucleotide sequence of the 30K protein cistron of cowpea !1strain of tobacco mosaic virus. !$#cross-references MUID:83064542; PMID:6292867 !$#accession A04183 !'##molecule_type genomic RNA !'##residues 1-283 ##label MES !'##cross-references GB:J02413; NID:g332223; PIDN:AAA46586.1; !1PID:g332225 CLASSIFICATION #superfamily tobravirus 30K protein KEYWORDS DNA binding SUMMARY #length 283 #molecular-weight 30965 #checksum 1964 SEQUENCE /// ENTRY WMBV2P #type complete TITLE 29K protein - tobacco rattle virus ORGANISM #formal_name tobacco rattle virus, TRV DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 23-Jul-1999 ACCESSIONS A04184; S02359 REFERENCE A93608 !$#authors Cornelissen, B.J.C.; Linthorst, H.J.M.; Brederode, F.T.; !1Bol, J.F. !$#journal Nucleic Acids Res. (1986) 14:2157-2169 !$#title Analysis of the genome structure of tobacco rattle virus !1strain PSG. !$#cross-references MUID:86176720; PMID:3960718 !$#accession A04184 !'##molecule_type genomic RNA !'##residues 1-252 ##label COR !'##cross-references GB:X03685; NID:g62136; PIDN:CAA27320.1; PID:g62137 !'##experimental_source strain PSG REFERENCE S01865 !$#authors Hamilton, W.D.O.; Boccara, M.; Robinson, D.J.; Baulcombe, !1D.C. !$#journal J. Gen. Virol. (1987) 68:2563-2575 !$#title The complete nucleotide sequence of tobacco rattle virus !1RNA-1. !$#cross-references MUID:88034943; PMID:3668507 !$#accession S02359 !'##molecule_type genomic RNA !'##residues 1-252 ##label HAM !'##cross-references EMBL:X06172; NID:g62132; PIDN:CAA29538.1; !1PID:g62134 !'##experimental_source strain SYM COMMENT The genome of this virus consists of two linear, positive, !1single-stranded RNAs encapsidated in separate virions. They !1are designated RNA-1 and RNA-2. COMMENT This protein was translated from the RNA-1. CLASSIFICATION #superfamily tobravirus 30K protein SUMMARY #length 252 #molecular-weight 28826 #checksum 871 SEQUENCE /// ENTRY WMBV2T #type complete TITLE 29K protein - tobacco rattle virus (strain TCM) ORGANISM #formal_name tobacco rattle virus, TRV DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 23-Jul-1999 ACCESSIONS A04185 REFERENCE A93628 !$#authors Angenent, G.C.; Linthorst, H.J.M.; van Belkum, A.F.; !1Cornelissen, B.J.C.; Bol, J.F. !$#journal Nucleic Acids Res. (1986) 14:4673-4682 !$#title RNA 2 of tobacco rattle virus strain TCM encodes an !1unexpected gene. !$#cross-references MUID:86232599; PMID:3714489 !$#accession A04185 !'##molecule_type genomic RNA !'##residues 1-255 ##label ANG !'##cross-references GB:X03955; NID:g62141; PIDN:CAA27585.1; PID:g62143 COMMENT The genome of this virus consists of two linear, positive, !1single-stranded RNAs encapsidated in separate virions. They !1are designated RNA-1 and RNA-2. COMMENT This protein was translated from the RNA-2. CLASSIFICATION #superfamily tobacco rattle virus 29K protein SUMMARY #length 255 #molecular-weight 29018 #checksum 9080 SEQUENCE /// ENTRY WMBV6P #type complete TITLE 16K protein - tobacco rattle virus (strain PSG) ORGANISM #formal_name tobacco rattle virus, TRV DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 23-Jul-1999 ACCESSIONS A04186 REFERENCE A93608 !$#authors Cornelissen, B.J.C.; Linthorst, H.J.M.; Brederode, F.T.; !1Bol, J.F. !$#journal Nucleic Acids Res. (1986) 14:2157-2169 !$#title Analysis of the genome structure of tobacco rattle virus !1strain PSG. !$#cross-references MUID:86176720; PMID:3960718 !$#accession A04186 !'##molecule_type genomic RNA !'##residues 1-141 ##label COR !'##cross-references GB:X03685; NID:g62136; PIDN:CAA27321.1; PID:g62138 COMMENT The genome of this virus consists of two linear, positive, !1single-stranded RNAs encapsidated in separate virions. They !1are designated RNA-1 and RNA-2. COMMENT This protein was translated from the RNA-1. CLASSIFICATION #superfamily tobacco rattle virus 16K protein SUMMARY #length 141 #molecular-weight 16297 #checksum 9773 SEQUENCE /// ENTRY WMBV6T #type complete TITLE 16K protein - tobacco rattle virus (strain TCM) ORGANISM #formal_name tobacco rattle virus, TRV DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 23-Jul-1999 ACCESSIONS A04187 REFERENCE A93628 !$#authors Angenent, G.C.; Linthorst, H.J.M.; van Belkum, A.F.; !1Cornelissen, B.J.C.; Bol, J.F. !$#journal Nucleic Acids Res. (1986) 14:4673-4682 !$#title RNA 2 of tobacco rattle virus strain TCM encodes an !1unexpected gene. !$#cross-references MUID:86232599; PMID:3714489 !$#accession A04187 !'##molecule_type genomic RNA !'##residues 1-141 ##label ANG !'##cross-references GB:X03955; NID:g62141; PIDN:CAA27587.1; PID:g62145 COMMENT The genome of this virus consists of two linear, positive, !1single-stranded RNAs encapsidated in separate virions. They !1are designated RNA-1 and RNA-2. COMMENT This protein was translated from the RNA-2. CLASSIFICATION #superfamily tobacco rattle virus 16K protein SUMMARY #length 141 #molecular-weight 16298 #checksum 9633 SEQUENCE /// ENTRY B46322 #type complete TITLE 16K protein - tobacco rattle virus (strain PLB) ORGANISM #formal_name tobacco rattle virus, TRV DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 23-Jul-1999 ACCESSIONS B46322 REFERENCE A46322 !$#authors Angenent, G.C.; Posthumus, E.; Brederode, F.T.; Bol, J.F. !$#journal Virology (1989) 171:271-274 !$#title Genome structure of tobacco rattle virus strain PLB: further !1evidence on the occurrence of RNA recombination among !1tobraviruses. !$#cross-references MUID:89299469; PMID:2741345 !$#accession B46322 !'##molecule_type genomic RNA !'##residues 1-141 ##label ANG !'##cross-references GB:J04347; NID:g332219; PIDN:AAA47079.1; !1PID:g332221 CLASSIFICATION #superfamily tobacco rattle virus 16K protein SUMMARY #length 141 #molecular-weight 16331 #checksum 139 SEQUENCE /// ENTRY VCBVCP #type complete TITLE coat protein - tobacco rattle virus ALTERNATE_NAMES capsid protein ORGANISM #formal_name tobacco rattle virus, TRV DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 23-Jul-1999 ACCESSIONS A04188; A46322 REFERENCE A93608 !$#authors Cornelissen, B.J.C.; Linthorst, H.J.M.; Brederode, F.T.; !1Bol, J.F. !$#journal Nucleic Acids Res. (1986) 14:2157-2169 !$#title Analysis of the genome structure of tobacco rattle virus !1strain PSG. !$#cross-references MUID:86176720; PMID:3960718 !$#accession A04188 !'##molecule_type genomic RNA !'##residues 1-209 ##label COR !'##cross-references GB:X03686; NID:g62139; PIDN:CAA27322.1; PID:g62140 !'##experimental_source strain PSG REFERENCE A46322 !$#authors Angenent, G.C.; Posthumus, E.; Brederode, F.T.; Bol, J.F. !$#journal Virology (1989) 171:271-274 !$#title Genome structure of tobacco rattle virus strain PLB: further !1evidence on the occurrence of RNA recombination among !1tobraviruses. !$#cross-references MUID:89299469; PMID:2741345 !$#accession A46322 !'##molecule_type genomic RNA !'##residues 1-209 ##label ANG !'##cross-references GB:J04347; NID:g332219; PIDN:AAA47078.1; !1PID:g332220 !'##experimental_source strain PLB COMMENT The genome of this virus consists of two linear, positive, !1single-stranded RNAs encapsidated in separate virions. They !1are designated RNA-1 and RNA-2. COMMENT This protein was translated from the RNA-2. CLASSIFICATION #superfamily tobacco rattle virus coat protein KEYWORDS capsid protein; coat protein SUMMARY #length 209 #molecular-weight 22879 #checksum 6772 SEQUENCE /// ENTRY VCBVCT #type complete TITLE coat protein - tobacco rattle virus (strain TCM) ALTERNATE_NAMES capsid protein ORGANISM #formal_name tobacco rattle virus, TRV DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 23-Jul-1999 ACCESSIONS A04189 REFERENCE A93628 !$#authors Angenent, G.C.; Linthorst, H.J.M.; van Belkum, A.F.; !1Cornelissen, B.J.C.; Bol, J.F. !$#journal Nucleic Acids Res. (1986) 14:4673-4682 !$#title RNA 2 of tobacco rattle virus strain TCM encodes an !1unexpected gene. !$#cross-references MUID:86232599; PMID:3714489 !$#accession A04189 !'##molecule_type genomic RNA !'##residues 1-205 ##label ANG !'##cross-references GB:X03955; NID:g62141; PIDN:CAA27584.1; PID:g62142 COMMENT The genome of this virus consists of two linear, positive, !1single-stranded RNAs encapsidated in separate virions. They !1are designated RNA-1 and RNA-2. COMMENT This protein was translated from the RNA-2. CLASSIFICATION #superfamily tobacco rattle virus coat protein KEYWORDS capsid protein; coat protein SUMMARY #length 205 #molecular-weight 22394 #checksum 1907 SEQUENCE /// ENTRY VCBVCA #type complete TITLE coat protein - tobacco rattle virus (strain CAM) ORGANISM #formal_name tobacco rattle virus, TRV DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 23-Jul-1999 ACCESSIONS A26027 REFERENCE A26027 !$#authors Bergh, S.T.; Koziel, M.G.; Huang, S.C.; Thomas, R.A.; !1Gilley, D.P.; Siegel, A. !$#journal Nucleic Acids Res. (1985) 13:8507-8518 !$#title The nucleotide sequence of tobacco rattle virus RNA-2 (CAM !1strain). !$#cross-references MUID:86093657; PMID:3841203 !$#accession A26027 !'##molecule_type genomic RNA !'##residues 1-223 ##label BER !'##cross-references GB:X03241; NID:g62057; PIDN:CAA26998.1; PID:g62058 !'##note the authors translated the codon GAG for residue 178 as Gly GENETICS !$#map_position segment 2 CLASSIFICATION #superfamily tobacco rattle virus coat protein KEYWORDS coat protein SUMMARY #length 223 #molecular-weight 23683 #checksum 3725 SEQUENCE /// ENTRY VCBVBV #type complete TITLE coat protein - barley stripe mosaic virus ALTERNATE_NAMES capsid protein ORGANISM #formal_name barley stripe mosaic virus, BSMV DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 23-Jul-1999 ACCESSIONS A04190 REFERENCE A93623 !$#authors Gustafson, G.; Armour, S.L. !$#journal Nucleic Acids Res. (1986) 14:3895-3909 !$#title The complete nucleotide sequence of RNAbeta from the type !1strain of barley stripe mosaic virus. !$#cross-references MUID:86232627; PMID:3754962 !$#accession A04190 !'##molecule_type genomic RNA !'##residues 1-198 ##label GUS !'##cross-references GB:X03854; NID:g60265; PIDN:CAA27484.1; PID:g60266 !'##experimental_source ATCC PV43 COMMENT The genome of this virus consists of three linear, positive, !1single-stranded RNAs encapsidated in separate virions. They !1are designated RNA-alpha, RNA-beta, and RNA-gamma. COMMENT This protein was translated from the RNA-beta. CLASSIFICATION #superfamily tobacco rattle virus coat protein KEYWORDS capsid protein; coat protein SUMMARY #length 198 #molecular-weight 22527 #checksum 8400 SEQUENCE /// ENTRY WMBV8B #type complete TITLE 58K protein - barley stripe mosaic virus ORGANISM #formal_name barley stripe mosaic virus, BSMV DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 23-Jul-1999 ACCESSIONS A04191 REFERENCE A93623 !$#authors Gustafson, G.; Armour, S.L. !$#journal Nucleic Acids Res. (1986) 14:3895-3909 !$#title The complete nucleotide sequence of RNAbeta from the type !1strain of barley stripe mosaic virus. !$#cross-references MUID:86232627; PMID:3754962 !$#accession A04191 !'##molecule_type genomic RNA !'##residues 1-528 ##label GUS !'##cross-references GB:X03854; NID:g60265; PIDN:CAA27485.1; PID:g60267 !'##experimental_source ATCC PV43 COMMENT The genome of this virus consists of three linear, positive, !1single-stranded RNAs encapsidated in separate virions. They !1are designated RNA-alpha, RNA-beta, and RNA-gamma. COMMENT This protein was translated from the RNA-beta. CLASSIFICATION #superfamily barley stripe mosaic virus 58K protein KEYWORDS duplication; tandem repeat FEATURE !$52-103 #region 26-residue repeats SUMMARY #length 528 #molecular-weight 58095 #checksum 5679 SEQUENCE /// ENTRY WMBV4B #type complete TITLE 14K protein - barley stripe mosaic virus ORGANISM #formal_name barley stripe mosaic virus, BSMV DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 23-Jul-1999 ACCESSIONS A04192 REFERENCE A93623 !$#authors Gustafson, G.; Armour, S.L. !$#journal Nucleic Acids Res. (1986) 14:3895-3909 !$#title The complete nucleotide sequence of RNAbeta from the type !1strain of barley stripe mosaic virus. !$#cross-references MUID:86232627; PMID:3754962 !$#accession A04192 !'##molecule_type genomic RNA !'##residues 1-131 ##label GUS !'##cross-references GB:X03854; NID:g60265; PIDN:CAA27486.1; PID:g60268 !'##experimental_source ATCC PV43 !'##note the authors translated the codon CAU for residue 121 as Asn COMMENT The genome of this virus consists of three linear, positive, !1single-stranded RNAs encapsidated in separate virions. They !1are designated RNA-alpha, RNA-beta, and RNA-gamma. COMMENT This protein was translated from the RNA-beta. CLASSIFICATION #superfamily barley stripe mosaic virus 14K protein SUMMARY #length 131 #molecular-weight 14119 #checksum 2660 SEQUENCE /// ENTRY WMWGP3 #type complete TITLE 12K protein - potato virus X (strain X3) ORGANISM #formal_name potato virus X, PVX #note host Nicotiana tabacum cv. Samsun (tobacco) DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jun-2000 ACCESSIONS JA0104 REFERENCE JA0102 !$#authors Huisman, M.J.; Linthorst, H.J.M.; Bol, J.F.; Cornelissen, !1B.J.C. !$#journal J. Gen. Virol. (1988) 69:1789-1798 !$#title The complete nucleotide sequence of potato virus X and its !1homologies at the amino acid level with various !1plus-stranded RNA viruses. !$#cross-references MUID:88299944; PMID:3404114 !$#accession JA0104 !'##molecule_type mRNA !'##residues 1-115 ##label HUI !'##cross-references DDBJ:D00344; NID:g222441; PIDN:BAA00251.1; !1PID:g222444 CLASSIFICATION #superfamily barley stripe mosaic virus 14K protein KEYWORDS transmembrane protein SUMMARY #length 115 #molecular-weight 12338 #checksum 2989 SEQUENCE /// ENTRY WMVYP2 #type complete TITLE 12K protein - potato virus M (strain Russian) ORGANISM #formal_name potato virus M #note host Lycopersicon esculentum (tomato) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jun-2000 ACCESSIONS PN0003; C54333; S21603 REFERENCE A92800 !$#authors Rupasov, V.V.; Morozov, S.Y.; Kanyuka, K.V.; Zavriev, S.K. !$#journal J. Gen. Virol. (1989) 70:1861-1869 !$#title Partial nucleotide sequence of potato virus M RNA shows !1similarities to potexviruses in gene arrangement and the !1encoded amino acid sequences. !$#cross-references MUID:89293091; PMID:2738581 !$#accession PN0003 !'##molecule_type mRNA !'##residues 1-109 ##label RUP !'##cross-references GB:D14449; GB:D00515; GB:X53062; NID:g222424; !1PIDN:BAA03341.1; PID:g222427 REFERENCE A54333 !$#authors Zavriev, S.K.; Kanyuka, K.V.; Levay, K.E. !$#journal J. Gen. Virol. (1991) 72:9-14 !$#title The genome organization of potato virus M RNA. !$#cross-references MUID:91116326; PMID:1990070 !$#accession C54333 !'##molecule_type genomic RNA !'##residues 1-109 ##label ZAV !'##cross-references EMBL:X53062; NID:g61291; PIDN:CAA37234.1; !1PID:g61294 COMMENT The genome is a single-stranded, positive-sense RNA. CLASSIFICATION #superfamily barley stripe mosaic virus 14K protein KEYWORDS transmembrane protein SUMMARY #length 109 #molecular-weight 11907 #checksum 3415 SEQUENCE /// ENTRY WMWGN2 #type complete TITLE 14K protein - narcissus mosaic virus ORGANISM #formal_name narcissus mosaic virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jun-2000 ACCESSIONS JT0472 REFERENCE JT0470 !$#authors Zuidema, D.; Linthorst, H.J.M.; Huisman, M.J.; Asjes, C.J.; !1Bol, J.F. !$#journal J. Gen. Virol. (1989) 70:267-276 !$#title Nucleotide sequence of narcissus mosaic virus RNA. !$#cross-references MUID:89279206; PMID:2732689 !$#accession JT0472 !'##molecule_type genomic RNA !'##residues 1-130 ##label ZUI !'##cross-references GB:D13747; GB:D00405; NID:g222107; PIDN:BAA02893.1; !1PID:g222110 CLASSIFICATION #superfamily barley stripe mosaic virus 14K protein KEYWORDS transmembrane protein SUMMARY #length 130 #molecular-weight 13998 #checksum 3361 SEQUENCE /// ENTRY WMWG14 #type complete TITLE 14K protein - Cymbidium mosaic virus ORGANISM #formal_name Cymbidium mosaic virus DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 23-Jul-1999 ACCESSIONS S20928 REFERENCE S20927 !$#authors Neo, K.K.; Wong, S.M.; Wu, M. !$#journal Plant Mol. Biol. (1992) 18:1027-1029 !$#title Nucleotide sequences of the two ORFs upstream to the coat !1protein gene of cymbidium mosaic virus. !$#cross-references MUID:92256805; PMID:1581564 !$#accession S20928 !'##molecule_type genomic RNA !'##residues 1-112 ##label NEO !'##cross-references EMBL:X62664; NID:g58891; PIDN:CAA44531.1; !1PID:g58892 CLASSIFICATION #superfamily barley stripe mosaic virus 14K protein SUMMARY #length 112 #molecular-weight 12474 #checksum 4017 SEQUENCE /// ENTRY WMWG10 #type complete TITLE 10K protein - Cymbidium mosaic virus ORGANISM #formal_name Cymbidium mosaic virus DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 23-Jul-1999 ACCESSIONS S20927 REFERENCE S20927 !$#authors Neo, K.K.; Wong, S.M.; Wu, M. !$#journal Plant Mol. Biol. (1992) 18:1027-1029 !$#title Nucleotide sequences of the two ORFs upstream to the coat !1protein gene of cymbidium mosaic virus. !$#cross-references MUID:92256805; PMID:1581564 !$#accession S20927 !'##molecule_type genomic RNA !'##residues 1-91 ##label NEO !'##cross-references EMBL:X62663; NID:g58889; PIDN:CAA44530.1; !1PID:g58890 CLASSIFICATION #superfamily narcissus mosaic virus 11K protein KEYWORDS transmembrane protein SUMMARY #length 91 #molecular-weight 9666 #checksum 9890 SEQUENCE /// ENTRY WMWGN3 #type complete TITLE 11K protein - narcissus mosaic virus ORGANISM #formal_name narcissus mosaic virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jun-2000 ACCESSIONS JT0473 REFERENCE JT0470 !$#authors Zuidema, D.; Linthorst, H.J.M.; Huisman, M.J.; Asjes, C.J.; !1Bol, J.F. !$#journal J. Gen. Virol. (1989) 70:267-276 !$#title Nucleotide sequence of narcissus mosaic virus RNA. !$#cross-references MUID:89279206; PMID:2732689 !$#accession JT0473 !'##molecule_type genomic RNA !'##residues 1-100 ##label ZUI !'##cross-references GB:D13747; GB:D00405; NID:g222107; PIDN:BAA02894.1; !1PID:g222111 CLASSIFICATION #superfamily narcissus mosaic virus 11K protein SUMMARY #length 100 #molecular-weight 11059 #checksum 1040 SEQUENCE /// ENTRY WMWGN5 #type complete TITLE 10K protein - narcissus mosaic virus ORGANISM #formal_name narcissus mosaic virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jun-2000 ACCESSIONS JT0475 REFERENCE JT0470 !$#authors Zuidema, D.; Linthorst, H.J.M.; Huisman, M.J.; Asjes, C.J.; !1Bol, J.F. !$#journal J. Gen. Virol. (1989) 70:267-276 !$#title Nucleotide sequence of narcissus mosaic virus RNA. !$#cross-references MUID:89279206; PMID:2732689 !$#accession JT0475 !'##molecule_type genomic RNA !'##residues 1-94 ##label ZUI !'##cross-references GB:D13747; GB:D00405; NID:g222107; PIDN:BAA02896.1; !1PID:g222113 CLASSIFICATION #superfamily narcissus mosaic virus 10K protein SUMMARY #length 94 #molecular-weight 10419 #checksum 4101 SEQUENCE /// ENTRY WMBV7B #type complete TITLE 17K protein - barley stripe mosaic virus ORGANISM #formal_name barley stripe mosaic virus, BSMV DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 23-Jul-1999 ACCESSIONS A04193 REFERENCE A93623 !$#authors Gustafson, G.; Armour, S.L. !$#journal Nucleic Acids Res. (1986) 14:3895-3909 !$#title The complete nucleotide sequence of RNAbeta from the type !1strain of barley stripe mosaic virus. !$#cross-references MUID:86232627; PMID:3754962 !$#accession A04193 !'##molecule_type genomic RNA !'##residues 1-155 ##label GUS !'##cross-references GB:X03854; NID:g60265; PIDN:CAA27487.1; PID:g60269 !'##experimental_source ATCC PV43 COMMENT The genome of this virus consists of three linear, positive, !1single-stranded RNAs encapsidated in separate virions. They !1are designated RNA-alpha, RNA-beta, and RNA-gamma. COMMENT This protein was translated from the RNA-beta. CLASSIFICATION #superfamily barley stripe mosaic virus 17K protein SUMMARY #length 155 #molecular-weight 17377 #checksum 8643 SEQUENCE /// ENTRY PAVBBS #type complete TITLE alpha-a protein - barley stripe mosaic virus ORGANISM #formal_name barley stripe mosaic virus, BSMV #note host Hordeum vulgare (barley) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 23-Jul-1999 ACCESSIONS JA0109; PN0104 REFERENCE JA0109 !$#authors Gustafson, G.; Armour, S.L.; Gamboa, G.C.; Burgett, S.G.; !1Shepherd, J.W. !$#journal Virology (1989) 170:370-377 !$#title Nucleotide sequence of barley stripe mosaic virus RNA alpha: !1RNA alpha encodes a single polypeptide with homology to !1corresponding proteins from other viruses. !$#cross-references MUID:89268457; PMID:2728343 !$#accession JA0109 !'##molecule_type genomic RNA !'##residues 1-1139 ##label GUS !'##cross-references GB:J04342; NID:g331510; PIDN:AAA46336.1; !1PID:g331511 REFERENCE PN0102 !$#authors Kozlov, Y.V.; Afanasiev, B.N.; Rupasov, V.V.; Golova, Y.B.; !1Kulaeva, O.I.; Dolja, V.V.; Atabekov, J.G.; Bayev, A.A. !$#journal Mol. Biol. (Mosk.) (1989) 23:1080-1090 !$#title The complete nucleotide sequence of barley stripe mosaic !1virus RNA 3 and its variability. !$#cross-references MUID:90066400; PMID:2586501 !$#accession PN0104 !'##molecule_type genomic RNA !'##residues 935-941,'E',943-976,'R',978-997,'L',999-1006,'F',1008-1056, !1'L',1058-1129,'L',1131-1139 ##label KOZ !'##note the authors translated the codon GAA for residue 942 as Gln and !1CCC for residue 1081 as Arg GENETICS !$#map_position segment 1 CLASSIFICATION #superfamily barley stripe mosaic virus alpha-a protein SUMMARY #length 1139 #molecular-weight 129627 #checksum 6065 SEQUENCE /// ENTRY WMTM18 #type complete TITLE 183.3K protein - tobacco mosaic virus ORGANISM #formal_name tobacco mosaic virus, TMV DATE 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 15-Oct-1994 ACCESSIONS A04194 REFERENCE A93926 !$#authors Goelet, P.; Lomonossoff, G.P.; Butler, P.J.G.; Akam, M.E.; !1Gait, M.J.; Karn, J. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:5818-5822 !$#title Nucleotide sequence of tobacco mosaic virus RNA. !$#cross-references MUID:83299880; PMID:6964389 !$#accession A04194 !'##molecule_type genomic RNA !'##residues 1-1615 ##label GOE !'##note the authors translated the codon AUU for residue 1302 as Tyr !'##note this sequence contains proteins 125.9K (residues 1-1116), 87.4K !1(336-1116), 83.5K (369-1116), 48.4K (681-1116), 34.6K !1(806-1116), and 46.2K (1218-1615) !'##note readthrough of the terminator codon UAG between codons for !1Gln-1116 and Gln-1117 occurs !'##note variant forms are found with 9-Ser, 14-Glu, 21-Thr, 37-Asp, and !1683-Ala CLASSIFICATION #superfamily cucumber mosaic virus RNA 1 protein SUMMARY #length 1615 #molecular-weight 183355 #checksum 198 SEQUENCE /// ENTRY WMTM8T #type complete TITLE 180K protein - tomato mosaic virus (strain L) CONTAINS 130K protein ORGANISM #formal_name tomato mosaic virus DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 30-Sep-1993 ACCESSIONS A04195 REFERENCE A91984 !$#authors Ohno, T.; Aoyagi, M.; Yamanashi, Y.; Saito, H.; Ikawa, S.; !1Meshi, T.; Okada, Y. !$#journal J. Biochem. (1984) 96:1915-1923 !$#title Nucleotide sequence of the tobacco mosaic virus (tomato !1strain) genome and comparison with the common strain genome. !$#cross-references MUID:85157522; PMID:6549393 !$#accession A04195 !'##molecule_type genomic RNA !'##residues 1-1615 ##label OHN !'##note readthrough of the terminator UAG between codons for Gln-1116 !1and Gln-1117 occurs CLASSIFICATION #superfamily cucumber mosaic virus RNA 1 protein SUMMARY #length 1615 #molecular-weight 183454 #checksum 276 SEQUENCE /// ENTRY WMTMGM #type complete TITLE 183K protein - tobacco mild green mosaic virus (strain U2-TMV) CONTAINS 126K protein ORGANISM #formal_name tobacco mild green mosaic virus #note host Nicotiana tabacum cv. Samsun (tobacco) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 23-Jul-1999 ACCESSIONS A35520 REFERENCE A35520 !$#authors Solis, I.; Garcia-Arenal, F. !$#journal Virology (1990) 177:553-558 !$#title The complete nucleotide sequence of the genomic RNA of the !1tobamovirus tobacco mild green mosaic virus. !$#cross-references MUID:90320127; PMID:2371769 !$#accession A35520 !'##molecule_type genomic RNA !'##residues 1-1608 ##label SOL !'##cross-references EMBL:M34077; NID:g335243; PIDN:AAA47934.1; !1PID:g335244 COMMENT This protein may have RNA polymerase activity. CLASSIFICATION #superfamily cucumber mosaic virus RNA 1 protein FEATURE !$1-1111 #product 126K protein #status predicted #label KPP SUMMARY #length 1608 #molecular-weight 182689 #checksum 1084 SEQUENCE /// ENTRY WMTMPV #type complete TITLE 183K protein - pepper mild mottle virus (strain Spain) CONTAINS 126K protein ORGANISM #formal_name pepper mild mottle virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 08-Apr-1994 ACCESSIONS JQ1312 REFERENCE JQ1312 !$#authors Alonso, E.; Garcia-Luque, I.; de la Cruz, A.; Wicke, B.; !1Avila-Rincon, M.J.; Serra, M.T.; Castresana, C.; Diaz-Ruiz, !1J.R. !$#journal J. Gen. Virol. (1991) 72:2875-2884 !$#title Nucleotide sequence of the genomic RNA of pepper mild mottle !1virus, a resistance-breaking tobamovirus in pepper. !$#cross-references MUID:92113528; PMID:1765765 !$#accession JQ1312 !'##molecule_type genomic RNA !'##residues 1-1611 ##label ALO !'##cross-references GB:M81413 !'##note readthrough of the terminator UAG occurs between the codons CAA !1for 1117-Gln and CAA for 1118-Gln COMMENT This protein may have RNA polymerase activity. CLASSIFICATION #superfamily cucumber mosaic virus RNA 1 protein FEATURE !$1-1117 #product 126K protein #status predicted #label PRO SUMMARY #length 1611 #molecular-weight 183155 #checksum 9283 SEQUENCE /// ENTRY JQ2144 #type complete TITLE 183K protein - tomato mosaic virus (strain Ob) CONTAINS 126K protein ORGANISM #formal_name tomato mosaic virus DATE 03-May-1994 #sequence_revision 03-May-1994 #text_change 16-Jun-2000 ACCESSIONS JQ2144; JQ2143; JQ2158; JQ2157 REFERENCE JQ2143 !$#authors Padgett, H.S.; Beachy, R.N. !$#journal Plant Cell (1993) 5:577-586 !$#title Analysis of a tobacco mosaic virus strain capable of !1overcoming N gene-mediated resistance. !$#cross-references MUID:93299124; PMID:8518557 !$#accession JQ2144 !'##molecule_type mRNA !'##residues 1-1616 ##label PAD !'##cross-references GB:L11665 !'##note this form is translated based on a read-through of the codon !1TAG for residue 1116 as Trp !$#accession JQ2143 !'##molecule_type mRNA !'##residues 1-1115 ##label PA2 !'##cross-references GB:L11665 !'##note this form is translated based on the interpretation of the TAG !1at position 1116 as a terminator REFERENCE JQ2157 !$#authors Ikeda, R.; Watanabe, E.; Watanabe, Y.; Okada, Y. !$#journal J. Gen. Virol. (1993) 74:1939-1944 !$#title Nucleotide sequence of tobamovirus Ob which can spread !1systemically in N gene tobacco. !$#cross-references MUID:93389450; PMID:8376970 !$#accession JQ2158 !'##molecule_type genomic RNA !'##residues 1-152,'K',154-872,'N',874-1616 ##label IKE !'##cross-references GB:D13438; NID:g436229; PIDN:BAA02700.1; !1PID:g436231 !'##note the codon TAG for residue 1116 is translated to Trp !$#accession JQ2157 !'##molecule_type genomic RNA !'##residues 1-152,'K',154-872,'N',874-1115 ##label IK2 !'##cross-references DDBJ:D13438; NID:g436229; PIDN:BAA02701.1; !1PID:g436230 COMMENT This protein is involved in replication of the RNA genome. CLASSIFICATION #superfamily cucumber mosaic virus RNA 1 protein FEATURE !$1-1616 #product 183K protein #status predicted #label MAT1\ !$1-1115 #product 126K protein #status predicted #label MAT2 SUMMARY #length 1616 #molecular-weight 183073 #checksum 8911 SEQUENCE /// ENTRY WMTMS2 #type complete TITLE 186K protein - cucumber green mottle mosaic virus (strain SH) ORGANISM #formal_name cucumber green mottle mosaic virus DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 08-Apr-1994 ACCESSIONS JQ1157 REFERENCE JQ1157 !$#authors Ugaki, M.; Tomiyama, M.; Kakutani, T.; Hidaka, S.; Kiguchi, !1T.; Nagata, R.; Sato, T.; Motoyoshi, F.; Nishiguchi, M. !$#journal J. Gen. Virol. (1991) 72:1487-1495 !$#title The complete nucleotide sequence of cucumber green mottle !1mosaic virus (SH strain) genomic RNA. !$#cross-references MUID:91311400; PMID:1856687 !$#accession JQ1157 !'##molecule_type genomic RNA !'##residues 1-1646 ##label UGA !'##cross-references GB:D12505 CLASSIFICATION #superfamily cucumber mosaic virus RNA 1 protein SUMMARY #length 1646 #molecular-weight 186453 #checksum 4871 SEQUENCE /// ENTRY P1BVA #type complete TITLE RNA 1a protein - brome mosaic virus CONTAINS ATP-dependent helicase (EC 3.6.1.-); mRNA (guanine-N7-)-methyltransferase (EC 2.1.1.56) ORGANISM #formal_name brome mosaic virus, BMV DATE 20-Sep-1984 #sequence_revision 20-Sep-1984 #text_change 19-Jan-2001 ACCESSIONS A04196 REFERENCE A92908 !$#authors Ahlquist, P.; Dasgupta, R.; Kaesberg, P. !$#journal J. Mol. Biol. (1984) 172:369-383 !$#title Nucleotide sequence of the brome mosaic virus genome and its !1implications for viral replication. !$#cross-references MUID:84114904; PMID:6694215 !$#accession A04196 !'##molecule_type genomic RNA !'##residues 1-961 ##label AHL !'##cross-references GB:X02380; GB:K02706; NID:g58728; PIDN:CAA26228.1; !1PID:g58729 CLASSIFICATION #superfamily cucumber mosaic virus RNA 1 protein KEYWORDS hydrolase; methyltransferase; mRNA capping; nucleotide !1binding; P-loop; S-adenosylmethionine FEATURE !$80-168 #domain methyltransferase #status predicted #label !8MTF\ !$683-939 #domain helicase #status predicted #label HHG\ !$685-692 #region nucleotide-binding motif A (P-loop) SUMMARY #length 961 #molecular-weight 109209 #checksum 4622 SEQUENCE /// ENTRY P1BVBB #type complete TITLE RNA 1a protein - broad bean mottle virus (strain Bawden) CONTAINS ATP-dependent helicase (EC 3.6.1.-); mRNA (guanine-N7-)-methyltransferase (EC 2.1.1.56) ORGANISM #formal_name broad bean mottle virus DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 19-Jan-2001 ACCESSIONS A41699 REFERENCE A41699 !$#authors Dzianott, A.M.; Bujarski, J.J. !$#journal Virology (1991) 185:553-562 !$#title The nucleotide sequence and genome organization of the RNA-1 !1segment in two bromoviruses: broad bean mottle virus and !1cowpea chlorotic mottle virus. !$#cross-references MUID:92074218; PMID:1962437 !$#accession A41699 !'##molecule_type genomic RNA !'##residues 1-966 ##label DZI !'##cross-references GB:M65138; NID:g210662; PIDN:AAA42740.1; !1PID:g210663 CLASSIFICATION #superfamily cucumber mosaic virus RNA 1 protein KEYWORDS hydrolase; methyltransferase; mRNA capping; nucleotide !1binding; P-loop; S-adenosylmethionine FEATURE !$80-168 #domain methyltransferase #status predicted #label !8MTF\ !$688-944 #domain helicase #status predicted #label HHG\ !$690-697 #region nucleotide-binding motif A (P-loop) SUMMARY #length 966 #molecular-weight 109621 #checksum 6077 SEQUENCE /// ENTRY P1BVCC #type complete TITLE 1a protein - cowpea chlorotic mottle virus ORGANISM #formal_name cowpea chlorotic mottle virus #note host Vigna unquiculata (cowpea) DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 08-Apr-1994 ACCESSIONS B41699 REFERENCE A41699 !$#authors Dzianott, A.M.; Bujarski, J.J. !$#journal Virology (1991) 185:553-562 !$#title The nucleotide sequence and genome organization of the RNA-1 !1segment in two bromoviruses: broad bean mottle virus and !1cowpea chlorotic mottle virus. !$#cross-references MUID:92074218; PMID:1962437 !$#accession B41699 !'##molecule_type genomic RNA !'##residues 1-958 ##label DZI !'##cross-references GB:M65138 CLASSIFICATION #superfamily cucumber mosaic virus RNA 1 protein SUMMARY #length 958 #molecular-weight 109137 #checksum 51 SEQUENCE /// ENTRY P1BVCV #type complete TITLE RNA 1 protein - cucumber mosaic virus (strain Q) CONTAINS ATP-dependent helicase (EC 3.6.1.-); mRNA (guanine-N7-)-methyltransferase (EC 2.1.1.56) ORGANISM #formal_name cucumber mosaic virus, CMV DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 19-Jan-2001 ACCESSIONS A25480 REFERENCE A25480 !$#authors Rezaian, M.A.; Williams, R.H.V.; Symons, R.H. !$#journal Eur. J. Biochem. (1985) 150:331-339 !$#title Nucleotide sequence of cucumber mosaic virus RNA 1. Presence !1of a sequence complementary to part of the viral satellite !1RNA and homologies with other viral RNAs. !$#cross-references MUID:85257660; PMID:4018086 !$#accession A25480 !'##molecule_type genomic RNA !'##residues 1-991 ##label REZ !'##cross-references EMBL:X02733; NID:g59037; PIDN:CAA26515.1; !1PID:g59038 GENETICS !$#map_position segment 1 CLASSIFICATION #superfamily cucumber mosaic virus RNA 1 protein KEYWORDS hydrolase; methyltransferase; mRNA capping; nucleotide !1binding; P-loop; S-adenosylmethionine FEATURE !$80-168 #domain methyltransferase #status predicted #label !8MTF\ !$697-954 #domain helicase #status predicted #label HHG\ !$713-720 #region nucleotide-binding motif A (P-loop) SUMMARY #length 991 #molecular-weight 110917 #checksum 2857 SEQUENCE /// ENTRY P1VXCM #type complete TITLE RNA 1 protein - cucumber mosaic virus (strain O) CONTAINS ATP-dependent helicase (EC 3.6.1.-); mRNA (guanine-N7-)-methyltransferase (EC 2.1.1.56) ORGANISM #formal_name cucumber mosaic virus, CMV DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 19-Jan-2001 ACCESSIONS JQ0379 REFERENCE JQ0379 !$#authors Hayakawa, T.; Mizukami, M.; Nakamura, I.; Suzuki, M. !$#journal Gene (1989) 85:533-540 !$#title Cloning and sequencing of RNA-1 cDNA from cucumber mosaic !1virus strain O. !$#cross-references MUID:90185229; PMID:2628183 !$#accession JQ0379 !'##molecule_type mRNA !'##residues 1-993 ##label HAY GENETICS !$#map_position segment 1 CLASSIFICATION #superfamily cucumber mosaic virus RNA 1 protein KEYWORDS hydrolase; methyltransferase; mRNA capping; nucleotide !1binding; P-loop; S-adenosylmethionine FEATURE !$81-174 #domain methyltransferase #status predicted #label !8MTF\ !$714-721 #region nucleotide-binding motif A (P-loop)\ !$721-979 #domain helicase #status predicted #label HHG SUMMARY #length 993 #molecular-weight 111265 #checksum 4751 SEQUENCE /// ENTRY P1VXPJ #type complete TITLE RNA 1 protein - peanut stunt virus (strain J) CONTAINS ATP-dependent helicase (EC 3.6.1.-); mRNA (guanine-N7-)-methyltransferase (EC 2.1.1.56) ORGANISM #formal_name peanut stunt virus DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 19-Jan-2001 ACCESSIONS JQ1451 REFERENCE JQ1451 !$#authors Karasawa, A.; Nakaho, K.; Kakutani, T.; Minobe, Y.; Ehara, !1Y. !$#journal J. Gen. Virol. (1992) 73:701-707 !$#title Nucleotide sequence analyses of peanut stunt cucumovirus !1RNAs 1 and 2. !$#cross-references MUID:92185483; PMID:1545224 !$#accession JQ1451 !'##molecule_type genomic RNA !'##residues 1-1005 ##label KAR !'##cross-references DDBJ:D11126; DDBJ:D01123; NID:g222417; !1PIDN:BAA01900.1; PID:g222418 GENETICS !$#map_position segment 1 CLASSIFICATION #superfamily cucumber mosaic virus RNA 1 protein KEYWORDS hydrolase; methyltransferase; mRNA capping; nucleotide !1binding; P-loop; S-adenosylmethionine FEATURE !$81-174 #domain methyltransferase #status predicted #label !8MTF\ !$720-977 #domain helicase #status predicted #label HHG\ !$722-729 #region nucleotide-binding motif A (P-loop) SUMMARY #length 1005 #molecular-weight 112017 #checksum 6917 SEQUENCE /// ENTRY P1VXTA #type complete TITLE RNA 1 protein - tomato aspermy virus (strain V) CONTAINS ATP-dependent helicase (EC 3.6.1.-); mRNA (guanine-N7-)-methyltransferase (EC 2.1.1.56) ORGANISM #formal_name tomato aspermy virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 19-Jan-2001 ACCESSIONS JQ1370 REFERENCE JQ1370 !$#authors Bernal, J.J.; Moriones, E.; Garcia-Arenal, F. !$#journal J. Gen. Virol. (1991) 72:2191-2195 !$#title Evolutionary relationships in the cucumoviruses: nucleotide !1sequence of tomato aspermy virus RNA 1. !$#cross-references MUID:91374017; PMID:1895056 !$#accession JQ1370 !'##molecule_type genomic RNA !'##residues 1-993 ##label BER !'##cross-references DDBJ:D01101 GENETICS !$#map_position segment 1 CLASSIFICATION #superfamily cucumber mosaic virus RNA 1 protein KEYWORDS hydrolase; methyltransferase; mRNA capping; nucleotide !1binding; P-loop; S-adenosylmethionine FEATURE !$81-174 #domain methyltransferase #status predicted #label !8MTF\ !$714-721 #region nucleotide-binding motif A (P-loop)\ !$721-979 #domain helicase #status predicted #label HHG SUMMARY #length 993 #molecular-weight 112035 #checksum 5227 SEQUENCE /// ENTRY WMFM12 #type complete TITLE 125K protein - alfalfa mosaic virus CONTAINS ATP-dependent helicase (EC 3.6.1.-); mRNA (guanine-N7-)-methyltransferase (EC 2.1.1.56) ORGANISM #formal_name alfalfa mosaic virus, AMV DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 19-Jan-2001 ACCESSIONS A04197 REFERENCE A04197 !$#authors Cornelissen, B.J.C.; Brederode, F.T.; Moormann, R.J.M.; Bol, !1J.F. !$#journal Nucleic Acids Res. (1983) 11:1253-1265 !$#title Complete nucleotide sequence of alfalfa mosaic virus RNA 1. !$#cross-references MUID:83143345; PMID:6298738 !$#accession A04197 !'##molecule_type mRNA !'##residues 1-1126 ##label COR !'##cross-references GB:L00163; GB:J02000; NID:g331424; PIDN:AAA46289.1; !1PID:g331425 GENETICS !$#map_position segment 1 CLASSIFICATION #superfamily cucumber mosaic virus RNA 1 protein KEYWORDS hydrolase; methyltransferase; mRNA capping; nucleotide !1binding; P-loop; S-adenosylmethionine FEATURE !$99-188 #domain methyltransferase #status predicted #label !8MTF\ !$838-845 #region nucleotide-binding motif A (P-loop)\ !$845-1096 #domain helicase #status predicted #label HHG SUMMARY #length 1126 #molecular-weight 125827 #checksum 1419 SEQUENCE /// ENTRY VCFMS #type complete TITLE coat protein - alfalfa mosaic virus (strain S) ORGANISM #formal_name alfalfa mosaic virus, AMV DATE 12-Aug-1981 #sequence_revision 12-Aug-1981 #text_change 05-Aug-1994 ACCESSIONS A90622; A90621; A04198 REFERENCE A90622 !$#authors Collot, D.; Peter, R.; Das, B.; Wolff, B.; Duranton, H. !$#journal Biochim. Biophys. Acta (1977) 492:267-283 !$#title Determination de la structure primaire de la proteine du !1virus de la mosaique de la luzerne (souche S). II. Sequence !1complete de la proteine. !$#cross-references MUID:77222094; PMID:884129 !$#accession A90622 !'##molecule_type protein !'##residues 1-217 ##label COL REFERENCE A90621 !$#authors Collot, D.; Dupin, A.; Duranton, H. !$#journal Biochim. Biophys. Acta (1977) 492:260-266 !$#title Determination de la structure primaire de la proteine du !1virus de la mosaique de la luzerne (souche S). I. !1Determination du poids moleculaire de la proteine, de sa !1composition en acides amines, et etude de ses extremites !1N-et-C-terminales. !$#cross-references MUID:77222093; PMID:884128 !$#accession A90621 !'##molecule_type DNA !'##residues 1-217 ##label COL2 CLASSIFICATION #superfamily alfalfa mosaic virus coat protein KEYWORDS acetylated amino end FEATURE !$1 #modified_site acetylated amino end (Ser) #status !8experimental SUMMARY #length 217 #molecular-weight 23617 #checksum 7862 SEQUENCE /// ENTRY VCFM42 #type complete TITLE coat protein - alfalfa mosaic virus ORGANISM #formal_name alfalfa mosaic virus, AMV DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 24-Sep-1999 ACCESSIONS A93466; A93703; A91245; A04199 REFERENCE A93466 !$#authors Barker, R.F.; Jarvis, N.P.; Thompson, D.V.; Loesch-Fries, !1L.S.; Hall, T.C. !$#journal Nucleic Acids Res. (1983) 11:2881-2891 !$#title Complete nucleotide sequence of alfalfa mosaic virus RNA3. !$#cross-references MUID:83220826; PMID:6856479 !$#accession A93466 !'##molecule_type genomic RNA !'##residues 1-221 ##label BAR !'##cross-references GB:K02703; NID:g331428; PIDN:AAA46292.1; !1PID:g331430 REFERENCE A93703 !$#authors Brederode, F.T.; Koper-Zwarthoff, E.C.; Bol, J.F. !$#journal Nucleic Acids Res. (1980) 8:2213-2223 !$#title Complete nucleotide sequence of alfalfa mosaic virus RNA 4. !$#cross-references MUID:81053689; PMID:7433090 !$#accession A93703 !'##molecule_type genomic RNA !'##residues 1-71,'A',73-82,'V',84-103,'H',105-184,'F',186-211,'F', !1213-221 ##label BRE !'##cross-references GB:V00048; NID:g58584; PIDN:CAA23418.1; PID:g58585 REFERENCE A91245 !$#authors van Beynum, G.M.A.; de Graff, J.M.; Castel, A.; Kraal, B.; !1Bosch, L. !$#journal Eur. J. Biochem. (1977) 72:63-78 !$#title Structural studies on the coat protein of alfalfa mosaic !1virus. The complete primary structure. !$#cross-references MUID:77091134; PMID:836394 !$#accession A91245 !'##molecule_type protein !'##residues 2-71,'A',73-82,'V',84-103,'H',105-184,'F',186-211,'F', !1213-215,'N',217-221 ##label VAN GENETICS !$#map_position segment 3 CLASSIFICATION #superfamily alfalfa mosaic virus coat protein KEYWORDS acetylated amino end FEATURE !$2 #modified_site acetylated amino end (Ser) (in mature !8form) #status experimental SUMMARY #length 221 #molecular-weight 24378 #checksum 4910 SEQUENCE /// ENTRY VCBV2S #type complete TITLE coat protein - alfalfa mosaic virus (strain Strasbourg) ALTERNATE_NAMES P4 protein ORGANISM #formal_name alfalfa mosaic virus, AMV #note host Nicotiana tabacum cv. Xanthi (tobacco) DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 23-Jul-1999 ACCESSIONS A04200 REFERENCE A90677 !$#authors Ravelonandro, M.; Pinck, M.; Pinck, L. !$#journal Biochimie (1984) 66:395-402 !$#title Complete nucleotide sequence of RNA 3 from alfalfa mosaic !1virus, strain S. !$#cross-references MUID:84281125; PMID:6205697 !$#accession A04200 !'##molecule_type genomic RNA !'##residues 1-218 ##label RAV !'##cross-references GB:X00819; NID:g58606; PIDN:CAA25393.1; PID:g58608 GENETICS !$#map_position segment 3 CLASSIFICATION #superfamily alfalfa mosaic virus coat protein SUMMARY #length 218 #molecular-weight 23945 #checksum 2862 SEQUENCE /// ENTRY VCFMYS #type complete TITLE coat protein - alfalfa mosaic virus (strain YSMV) ALTERNATE_NAMES P4 protein ORGANISM #formal_name alfalfa mosaic virus, AMV #note host Nicotiana tabacum cv. Samsun NN (tobacco) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 23-Jul-1999 ACCESSIONS B37948 REFERENCE A37948 !$#authors Neeleman, L.; Van Der Kuyl, A.C.; Bol, J.F. !$#journal Virology (1991) 181:687-693 !$#title Role of alfalfa mosaic virus coat protein gene in symptom !1formation. !$#cross-references MUID:91196260; PMID:2014643 !$#accession B37948 !'##molecule_type genomic RNA !'##residues 1-221 ##label NEE !'##cross-references EMBL:M59241; NID:g331421; PIDN:AAA46288.1; !1PID:g331423 GENETICS !$#map_position segment 3 CLASSIFICATION #superfamily alfalfa mosaic virus coat protein KEYWORDS coat protein SUMMARY #length 221 #molecular-weight 24352 #checksum 3279 SEQUENCE /// ENTRY WMFM9 #type complete TITLE 90K protein - alfalfa mosaic virus ORGANISM #formal_name alfalfa mosaic virus, AMV DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 12-Dec-1997 ACCESSIONS A04201 REFERENCE A04201 !$#authors Cornelissen, B.J.C.; Brederode, F.T.; Veeneman, G.H.; van !1Boom, J.H.; Bol, J.F. !$#journal Nucleic Acids Res. (1983) 11:3019-3025 !$#title Complete nucleotide sequence of alfalfa mosaic virus RNA 2. !$#cross-references MUID:83220723; PMID:6304618 !$#accession A04201 !'##molecule_type genomic RNA !'##residues 1-790 ##label COR GENETICS !$#map_position segment 2 CLASSIFICATION #superfamily alfalfa mosaic virus 90K protein KEYWORDS nonstructural protein; RNA replication SUMMARY #length 790 #molecular-weight 89879 #checksum 8373 SEQUENCE /// ENTRY P2BVA #type complete TITLE 2a protein - brome mosaic virus ORGANISM #formal_name brome mosaic virus, BMV DATE 20-Sep-1984 #sequence_revision 20-Sep-1984 #text_change 23-Jul-1999 ACCESSIONS A04202 REFERENCE A92908 !$#authors Ahlquist, P.; Dasgupta, R.; Kaesberg, P. !$#journal J. Mol. Biol. (1984) 172:369-383 !$#title Nucleotide sequence of the brome mosaic virus genome and its !1implications for viral replication. !$#cross-references MUID:84114904; PMID:6694215 !$#accession A04202 !'##molecule_type genomic RNA !'##residues 1-822 ##label AHL !'##cross-references GB:X01678; GB:K02707; NID:g58730; PIDN:CAA25834.1; !1PID:g58731 CLASSIFICATION #superfamily alfalfa mosaic virus 90K protein KEYWORDS nonstructural protein; RNA replication SUMMARY #length 822 #molecular-weight 93926 #checksum 2701 SEQUENCE /// ENTRY P2WMCC #type complete TITLE 2a protein - cowpea chlorotic mottle virus ORGANISM #formal_name cowpea chlorotic mottle virus DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 23-Jul-1999 ACCESSIONS JU0117 REFERENCE JU0117 !$#authors Allison, R.F.; Janda, M.; Ahlquist, P. !$#journal Virology (1989) 172:321-330 !$#title Sequence of cowpea chlorotic mottle virus RNAs 2 and 3 and !1evidence of a recombination event during bromovirus !1evolution. !$#cross-references MUID:89370316; PMID:2773323 !$#accession JU0117 !'##molecule_type genomic RNA !'##residues 1-808 ##label ALL !'##cross-references GB:M28817; NID:g331605; PIDN:AAA46371.1; !1PID:g331606 COMMENT This protein is a trans-acting factor in viral RNA !1replication. GENETICS !$#map_position segment 2 CLASSIFICATION #superfamily alfalfa mosaic virus 90K protein KEYWORDS nonstructural protein; RNA replication SUMMARY #length 808 #molecular-weight 92936 #checksum 2372 SEQUENCE /// ENTRY P2WMBB #type complete TITLE 2a protein - broad bean mottle virus ORGANISM #formal_name broad bean mottle virus DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 23-Jul-1999 ACCESSIONS A42453 REFERENCE A42453 !$#authors Romero, J.; Dzianott, A.M.; Bujarski, J.J. !$#journal Virology (1992) 187:671-681 !$#title The nucleotide sequence and genome organization of the RNA2 !1and RNA3 segments in broad bean mottle virus. !$#cross-references MUID:92188542; PMID:1546462 !$#accession A42453 !'##molecule_type genomic RNA !'##residues 1-810 ##label ROM !'##cross-references GB:M64713; NID:g210666; PIDN:AAA42741.1; !1PID:g210667 COMMENT This protein is a trans-acting factor in viral RNA !1replication. GENETICS !$#map_position segment 2 CLASSIFICATION #superfamily alfalfa mosaic virus 90K protein KEYWORDS nonstructural protein; RNA replication SUMMARY #length 810 #molecular-weight 92992 #checksum 4864 SEQUENCE /// ENTRY WMVXCU #type complete TITLE genome RNA2 protein - cucumber mosaic virus (strain Fny subgroup I) ORGANISM #formal_name cucumber mosaic virus, CMV DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jun-2000 ACCESSIONS JQ0015 REFERENCE JQ0015 !$#authors Rizzo, T.M.; Palukaitis, P. !$#journal J. Gen. Virol. (1988) 69:1777-1787 !$#title Nucleotide sequence and evolutionary relationships of !1cucumber mosaic virus (CMV) strains: CMV RNA2. !$#cross-references MUID:88299943; PMID:3404113 !$#accession JQ0015 !'##molecule_type genomic RNA !'##residues 1-857 ##label RIZ !'##cross-references DDBJ:D00355; NID:g222035; PIDN:BAA00263.1; !1PID:g222036 COMMENT The genome consists of three species of single-stranded, !1positive-sense RNA, called RNA1, RNA2, and RNA3. This !1protein is encoded by the RNA2. GENETICS !$#map_position segment 2 CLASSIFICATION #superfamily alfalfa mosaic virus 90K protein KEYWORDS nonstructural protein; RNA replication SUMMARY #length 857 #molecular-weight 96709 #checksum 6040 SEQUENCE /// ENTRY WMVXPJ #type complete TITLE RNA replicase 2 (EC 2.7.7.-) - peanut stunt virus (strain J) ORGANISM #formal_name peanut stunt virus DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 16-Jun-2000 ACCESSIONS JQ1452 REFERENCE JQ1451 !$#authors Karasawa, A.; Nakaho, K.; Kakutani, T.; Minobe, Y.; Ehara, !1Y. !$#journal J. Gen. Virol. (1992) 73:701-707 !$#title Nucleotide sequence analyses of peanut stunt cucumovirus !1RNAs 1 and 2. !$#cross-references MUID:92185483; PMID:1545224 !$#accession JQ1452 !'##molecule_type genomic RNA !'##residues 1-834 ##label KAR !'##cross-references GB:D11127; GB:D01124; NID:g222419; PIDN:BAA01901.1; !1PID:g222420 GENETICS !$#map_position segment 2 CLASSIFICATION #superfamily alfalfa mosaic virus 90K protein KEYWORDS nucleotidyltransferase SUMMARY #length 834 #molecular-weight 93520 #checksum 8257 SEQUENCE /// ENTRY WMVYPM #type complete TITLE 25K protein - potato virus M (strain Russian) ORGANISM #formal_name potato virus M #note host Lycopersicon esculentum (tomato) DATE 31-Mar-1990 #sequence_revision 17-Feb-1994 #text_change 29-Oct-1999 ACCESSIONS PN0094; B54333; PN0002; S21602 REFERENCE PN0093 !$#authors Zavriev, S.K.; Kanyka, K.V.; Levay, K.E. !$#journal Mol. Biol. (Mosk.) (1991) 25:761-769 !$#title The complete nucleotide sequence of potato virus M genomic !1RNA. !$#cross-references MUID:92049299; PMID:1944258 !$#accession PN0094 !'##molecule_type genomic RNA !'##residues 1-229 ##label ZAV !'##cross-references GB:X53062; NID:g61291; PIDN:CAA37233.1; PID:g61293 REFERENCE A54333 !$#authors Zavriev, S.K.; Kanyuka, K.V.; Levay, K.E. !$#journal J. Gen. Virol. (1991) 72:9-14 !$#title The genome organization of potato virus M RNA. !$#cross-references MUID:91116326; PMID:1990070 !$#accession B54333 !'##molecule_type genomic RNA !'##residues 1-229 ##label ZA2 !'##cross-references EMBL:X53062; NID:g61291; PIDN:CAA37233.1; !1PID:g61293 REFERENCE A92800 !$#authors Rupasov, V.V.; Morozov, S.Y.; Kanyuka, K.V.; Zavriev, S.K. !$#journal J. Gen. Virol. (1989) 70:1861-1869 !$#title Partial nucleotide sequence of potato virus M RNA shows !1similarities to potexviruses in gene arrangement and the !1encoded amino acid sequences. !$#cross-references MUID:89293091; PMID:2738581 !$#accession PN0002 !'##molecule_type mRNA !'##residues 1-214,'RLCTSVS' ##label RUP REFERENCE S21601 !$#authors Zavriev, S.K. !$#submission submitted to the EMBL Data Library, May 1990 !$#accession S21602 !'##status preliminary !'##molecule_type genomic RNA !'##residues 1-214,'RLCTSVS' ##label ZA3 !'##cross-references EMBL:X53062 !'##experimental_source Russian wild type CLASSIFICATION #superfamily potato virus 25K protein SUMMARY #length 229 #molecular-weight 25439 #checksum 5117 SEQUENCE /// ENTRY WMWGP2 #type complete TITLE 25K protein - potato virus X (strain X3) ORGANISM #formal_name potato virus X, PVX #note host Nicotiana tabacum cv. Samsun (tobacco) DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jun-2000 ACCESSIONS JA0103 REFERENCE JA0102 !$#authors Huisman, M.J.; Linthorst, H.J.M.; Bol, J.F.; Cornelissen, !1B.J.C. !$#journal J. Gen. Virol. (1988) 69:1789-1798 !$#title The complete nucleotide sequence of potato virus X and its !1homologies at the amino acid level with various !1plus-stranded RNA viruses. !$#cross-references MUID:88299944; PMID:3404114 !$#accession JA0103 !'##molecule_type mRNA !'##residues 1-226 ##label HUI !'##cross-references DDBJ:D00344; NID:g222441; PIDN:BAA00250.1; !1PID:g222443 CLASSIFICATION #superfamily potato virus 25K protein SUMMARY #length 226 #molecular-weight 24596 #checksum 5651 SEQUENCE /// ENTRY WMWGN1 #type complete TITLE 25K protein - narcissus mosaic virus ORGANISM #formal_name narcissus mosaic virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jun-2000 ACCESSIONS JT0471 REFERENCE JT0470 !$#authors Zuidema, D.; Linthorst, H.J.M.; Huisman, M.J.; Asjes, C.J.; !1Bol, J.F. !$#journal J. Gen. Virol. (1989) 70:267-276 !$#title Nucleotide sequence of narcissus mosaic virus RNA. !$#cross-references MUID:89279206; PMID:2732689 !$#accession JT0471 !'##molecule_type genomic RNA !'##residues 1-233 ##label ZUI !'##cross-references GB:D13747; GB:D00405; NID:g222107; PIDN:BAA02892.1; !1PID:g222109 CLASSIFICATION #superfamily potato virus 25K protein SUMMARY #length 233 #molecular-weight 25845 #checksum 4909 SEQUENCE /// ENTRY B46350 #type complete TITLE 25K protein - white clover mosaic virus (strain O) ORGANISM #formal_name white clover mosaic virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 07-May-1999 ACCESSIONS B46350 REFERENCE A46350 !$#authors Beck, D.L.; Forster, R.L.S.; Bevan, M.W.; Boxen, K.A.; Lowe, !1S.C. !$#journal Virology (1990) 177:152-158 !$#title Infectious transcripts and nucleotide sequence of cloned !1cDNA of the potexvirus white clover mosaic virus. !$#cross-references MUID:90281578; PMID:2353451 !$#accession B46350 !'##status translation not shown !'##molecule_type genomic RNA !'##residues 1-235 ##label BEC !'##cross-references GB:X16636 CLASSIFICATION #superfamily potato virus 25K protein SUMMARY #length 235 #molecular-weight 26354 #checksum 6147 SEQUENCE /// ENTRY WMVYP3 #type complete TITLE 7K protein - potato virus M (strain Russian) ORGANISM #formal_name potato virus M #note host Lycopersicon esculentum (tomato) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jun-2000 ACCESSIONS PN0004; D54333; S21604 REFERENCE A92800 !$#authors Rupasov, V.V.; Morozov, S.Y.; Kanyuka, K.V.; Zavriev, S.K. !$#journal J. Gen. Virol. (1989) 70:1861-1869 !$#title Partial nucleotide sequence of potato virus M RNA shows !1similarities to potexviruses in gene arrangement and the !1encoded amino acid sequences. !$#cross-references MUID:89293091; PMID:2738581 !$#accession PN0004 !'##molecule_type mRNA !'##residues 1-63 ##label RUP !'##cross-references GB:D14449; GB:D00515; GB:X53062; NID:g222424; !1PIDN:BAA03342.1; PID:g222428 REFERENCE A54333 !$#authors Zavriev, S.K.; Kanyuka, K.V.; Levay, K.E. !$#journal J. Gen. Virol. (1991) 72:9-14 !$#title The genome organization of potato virus M RNA. !$#cross-references MUID:91116326; PMID:1990070 !$#accession D54333 !'##molecule_type mRNA !'##residues 1-63 ##label ZAV !'##cross-references EMBL:X53062; NID:g61291; PIDN:CAA37235.1; !1PID:g61295 COMMENT The genome is a single-stranded, positive-sense RNA. CLASSIFICATION #superfamily potato virus 7K protein SUMMARY #length 63 #molecular-weight 6747 #checksum 7979 SEQUENCE /// ENTRY VCVYPM #type complete TITLE coat protein - potato virus M (strain Russian) ORGANISM #formal_name potato virus M #note host Lycopersicon esculentum (tomato) DATE 31-Mar-1990 #sequence_revision 23-Mar-1995 #text_change 23-Jul-1999 ACCESSIONS E54333; PN0005; S21605 REFERENCE A54333 !$#authors Zavriev, S.K.; Kanyuka, K.V.; Levay, K.E. !$#journal J. Gen. Virol. (1991) 72:9-14 !$#title The genome organization of potato virus M RNA. !$#cross-references MUID:91116326; PMID:1990070 !$#accession E54333 !'##molecule_type genomic RNA !'##residues 1-304 ##label ZAV !'##cross-references EMBL:X53062; NID:g61291; PIDN:CAA37236.1; !1PID:g61296 REFERENCE A92800 !$#authors Rupasov, V.V.; Morozov, S.Y.; Kanyuka, K.V.; Zavriev, S.K. !$#journal J. Gen. Virol. (1989) 70:1861-1869 !$#title Partial nucleotide sequence of potato virus M RNA shows !1similarities to potexviruses in gene arrangement and the !1encoded amino acid sequences. !$#cross-references MUID:89293091; PMID:2738581 !$#accession PN0005 !'##molecule_type mRNA !'##residues 1-268,'L',270-304 ##label RUP COMMENT The genome is a single-stranded, positive-sense RNA. CLASSIFICATION #superfamily potato virus coat protein KEYWORDS coat protein SUMMARY #length 304 #molecular-weight 33930 #checksum 3103 SEQUENCE /// ENTRY A48549 #type complete TITLE coat protein - potato virus S ORGANISM #formal_name potato virus S DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 23-Jul-1999 ACCESSIONS A48549 REFERENCE A48549 !$#authors Foster, G.D.; Mills, P.R. !$#journal Virus Genes (1992) 6:213-220 !$#title The 3'-nucleotide sequence of an ordinary strain of potato !1virus S. !$#cross-references MUID:93033173; PMID:1413539 !$#accession A48549 !'##molecule_type genomic RNA !'##residues 1-297 ##label FOS !'##cross-references GB:S45593; NID:g256417; PIDN:AAB23461.1; !1PID:g256418 !'##note sequence extracted from NCBI backbone (NCBIN:114637, !1NCBIP:114638) CLASSIFICATION #superfamily potato virus coat protein KEYWORDS coat protein; glycoprotein FEATURE !$62 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 297 #molecular-weight 32881 #checksum 6175 SEQUENCE /// ENTRY VCVYPV #type complete TITLE coat protein - potato virus S (strain Andean) ORGANISM #formal_name potato virus S DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jun-2000 ACCESSIONS JA0127 REFERENCE JA0123 !$#authors MacKenzie, D.J.; Tremaine, J.H.; Stace-Smith, R. !$#journal J. Gen. Virol. (1989) 70:1053-1063 !$#title Organization and interviral homologies of the 3'-terminal !1portion of potato virus S RNA. !$#cross-references MUID:89279283; PMID:2732711 !$#accession JA0127 !'##molecule_type genomic RNA !'##residues 1-293 ##label MAC !'##cross-references EMBL:D00461; NID:g222438; PIDN:BAA00355.1; !1PID:g2160372 CLASSIFICATION #superfamily potato virus coat protein KEYWORDS coat protein; glycoprotein FEATURE !$61,66 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 293 #molecular-weight 32408 #checksum 3923 SEQUENCE /// ENTRY VCWGPV #type complete TITLE coat protein - potato virus X ORGANISM #formal_name potato virus X, PVX #note host Nicotiana tabacum cv. Samsun (tobacco) DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 16-Jun-2000 ACCESSIONS JA0106; S47079; S57503; S57504 REFERENCE JA0102 !$#authors Huisman, M.J.; Linthorst, H.J.M.; Bol, J.F.; Cornelissen, !1B.J.C. !$#journal J. Gen. Virol. (1988) 69:1789-1798 !$#title The complete nucleotide sequence of potato virus X and its !1homologies at the amino acid level with various !1plus-stranded RNA viruses. !$#cross-references MUID:88299944; PMID:3404114 !$#accession JA0106 !'##molecule_type mRNA !'##residues 1-237 ##label HUI !'##cross-references DDBJ:D00344; NID:g222441; PIDN:BAA00253.1; !1PID:g222446 !'##experimental_source strain X3 REFERENCE S47079 !$#authors Feigelstock, D.; Tozzini, A.C.; Hopp, H.E. !$#submission submitted to the EMBL Data Library, May 1994 !$#description The coat protein sequence of a resistance-breaking strain of !1potato virus X. !$#accession S47079 !'##status preliminary !'##molecule_type DNA !'##residues 1-237 ##label FEI !'##cross-references EMBL:Z34261; NID:g498700; PIDN:CAA84016.1; !1PID:g498701 !'##experimental_source strain X3 REFERENCE S57501 !$#authors Santa Cruz, S.; Baulcombe, D.C. !$#submission submitted to the EMBL Data Library, June 1995 !$#description Analysis of potato virus X coat protein genes in relation to !1resistance conferred by the genes Nx, Nb and Rx1 of potato. !$#accession S57503 !'##status preliminary !'##molecule_type DNA !'##residues 1-237 ##label SAN !'##cross-references EMBL:X88783; NID:g872283; PIDN:CAA61262.1; !1PID:g872284 !$#accession S57504 !'##status preliminary !'##molecule_type DNA !'##residues 1-237 ##label SA2 !'##cross-references EMBL:X88784; NID:g872285; PIDN:CAA61263.1; !1PID:g872286 CLASSIFICATION #superfamily potato virus coat protein KEYWORDS coat protein SUMMARY #length 237 #molecular-weight 25081 #checksum 3601 SEQUENCE /// ENTRY VCWGPX #type complete TITLE coat protein - potato virus X (strain PVX-UK3) ORGANISM #formal_name potato virus X, PVX DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 08-Apr-1994 ACCESSIONS A42993 REFERENCE A42993 !$#authors Kavanagh, T.; Goulden, M.; Santa Cruz, S.; Chapman, S.; !1Barker, I.; Baulcombe, D. !$#journal Virology (1992) 189:609-617 !$#title Molecular analysis of a resistance-breaking strain of potato !1virus X. !$#cross-references MUID:92351559; PMID:1641981 !$#accession A42993 !'##molecule_type genomic RNA !'##residues 1-237 ##label KAV !'##cross-references GB:S41268 CLASSIFICATION #superfamily potato virus coat protein KEYWORDS coat protein SUMMARY #length 237 #molecular-weight 25119 #checksum 3630 SEQUENCE /// ENTRY VCWGWC #type complete TITLE coat protein - white clover mosaic virus ORGANISM #formal_name white clover mosaic virus DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 23-Jul-1999 ACCESSIONS S01089; D34002 REFERENCE S01085 !$#authors Forster, R.L.S.; Bevan, M.W.; Harbison, S.A.; Gardner, R.C. !$#journal Nucleic Acids Res. (1988) 16:291-303 !$#title The complete nucleotide sequence of the potexvirus white !1clover mosaic virus. !$#cross-references MUID:88124202; PMID:3340527 !$#accession S01089 !'##molecule_type mRNA !'##residues 1-190 ##label FOR !'##cross-references GB:X06728; NID:g61317; PIDN:CAA29908.1; PID:g61322 REFERENCE A34002 !$#authors Harbison, S.A.; Forster, R.L.S.; Guilford, P.J.; Gardner, !1R.C. !$#journal Virology (1988) 162:459-465 !$#title Organization and interviral homologies of the coat protein !1gene of white clover mosaic virus. !$#cross-references MUID:88128564; PMID:3341118 !$#accession D34002 !'##molecule_type genomic RNA !'##residues 1-190 ##label HAR !'##cross-references GB:M18920; NID:g336125; PIDN:AAA69638.1; !1PID:g893349 !'##experimental_source isolate M CLASSIFICATION #superfamily potato virus coat protein KEYWORDS coat protein SUMMARY #length 190 #molecular-weight 20684 #checksum 6660 SEQUENCE /// ENTRY E46350 #type complete TITLE coat protein - white clover mosaic virus ORGANISM #formal_name white clover mosaic virus DATE 31-Dec-1993 #sequence_revision 13-Mar-1997 #text_change 23-Jul-1999 ACCESSIONS S35114; E46350 REFERENCE A46350 !$#authors Beck, D.L.; Forster, R.L.S.; Bevan, M.W.; Boxen, K.A.; Lowe, !1S.C. !$#journal Virology (1990) 177:152-158 !$#title Infectious transcripts and nucleotide sequence of cloned !1cDNA of the potexvirus white clover mosaic virus. !$#cross-references MUID:90281578; PMID:2353451 !$#accession S35114 !'##status preliminary; translation not shown !'##molecule_type genomic RNA !'##residues 1-208 ##label BEC !'##cross-references EMBL:X16636; NID:g61323; PIDN:CAA34632.1; !1PID:g61328 !$#accession E46350 !'##status translation not shown !'##molecule_type genomic RNA !'##residues 1-207 ##label BE2 !'##cross-references GB:X16636 !'##experimental_source strain O CLASSIFICATION #superfamily potato virus coat protein KEYWORDS coat protein SUMMARY #length 208 #molecular-weight 22467 #checksum 8283 SEQUENCE /// ENTRY VCWGN4 #type complete TITLE coat protein - narcissus mosaic virus ORGANISM #formal_name narcissus mosaic virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jun-2000 ACCESSIONS JT0474 REFERENCE JT0470 !$#authors Zuidema, D.; Linthorst, H.J.M.; Huisman, M.J.; Asjes, C.J.; !1Bol, J.F. !$#journal J. Gen. Virol. (1989) 70:267-276 !$#title Nucleotide sequence of narcissus mosaic virus RNA. !$#cross-references MUID:89279206; PMID:2732689 !$#accession JT0474 !'##molecule_type genomic RNA !'##residues 1-240 ##label ZUI !'##cross-references GB:D13747; GB:D00405; NID:g222107; PIDN:BAA02895.1; !1PID:g222112 CLASSIFICATION #superfamily potato virus coat protein KEYWORDS coat protein SUMMARY #length 240 #molecular-weight 26097 #checksum 8500 SEQUENCE /// ENTRY VCWGPM #type complete TITLE coat protein - papaya mosaic virus ORGANISM #formal_name papaya mosaic virus DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jun-2000 ACCESSIONS JQ0100; A37015; A47609 REFERENCE JQ0096 !$#authors Sit, T.L.; Abouhaidar, M.G.; Holy, S. !$#journal J. Gen. Virol. (1989) 70:2325-2331 !$#title Nucleotide sequence of papaya mosaic virus RNA. !$#cross-references MUID:89381685; PMID:2778435 !$#accession JQ0100 !'##molecule_type genomic RNA !'##residues 1-215 ##label SIT !'##cross-references GB:D13957; GB:D00580; NID:g222330; PIDN:BAA03054.1; !1PID:g222335 REFERENCE A37015 !$#authors Verde, C.; Malorni, A.; Parente, A. !$#journal J. Protein Chem. (1989) 8:795-805 !$#title The primary structure of papaya mosaic virus coat protein: a !1revision. !$#cross-references MUID:90166218; PMID:2624687 !$#accession A37015 !'##molecule_type protein !'##residues 2-10,'T',12-30,'Q',31-184,'E',186-189,'A',191-215 ##label !1VER REFERENCE A47609 !$#authors Short, M.N.; Turner, D.S.; March, J.F.; Pappin, D.J.C.; !1Parente, A.; Davies, J.W. !$#journal Virology (1986) 152:280-283 !$#title The primary structure of papaya mosaic coat protein. !$#accession A47609 !'##molecule_type protein !'##residues 6-10,'T',12-30,'Q',31-184,'E',186-189,'A',191-214,'Q' !1##label SHO CLASSIFICATION #superfamily potato virus coat protein KEYWORDS coat protein SUMMARY #length 215 #molecular-weight 23045 #checksum 5227 SEQUENCE /// ENTRY VCWGSM #type complete TITLE coat protein - strawberry mild yellow edge-associated virus ORGANISM #formal_name strawberry mild yellow edge-associated virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jun-2000 ACCESSIONS JQ1430 REFERENCE JQ1426 !$#authors Jelkmann, W.; Maiss, E.; Martin, R.R. !$#journal J. Gen. Virol. (1992) 73:475-479 !$#title The nucleotide sequence and genome organization of !1strawberry mild yellow edge-associated potexvirus. !$#cross-references MUID:92166762; PMID:1339469 !$#accession JQ1430 !'##molecule_type genomic RNA !'##residues 1-242 ##label JEL !'##cross-references GB:D12517; DDBJ:D01227; NID:g222631; !1PIDN:BAA02086.1; PID:g222636 CLASSIFICATION #superfamily potato virus coat protein KEYWORDS coat protein SUMMARY #length 242 #molecular-weight 25743 #checksum 2247 SEQUENCE /// ENTRY JQ1645 #type complete TITLE coat protein - poplar mosaic virus ORGANISM #formal_name poplar mosaic virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 23-Jul-1999 ACCESSIONS JQ1645; PQ0426; S23875 REFERENCE JQ1645 !$#authors Henderson, J.; Gibbs, M.J.; Edwards, M.L.; Clarke, V.A.; !1Gardner, K.A.; Cooper, J.I. !$#journal J. Gen. Virol. (1992) 73:1887-1890 !$#title Partial nucleotide sequence of poplar mosaic virus RNA !1confirms its classification as a carlavirus. !$#cross-references MUID:92333281; PMID:1629709 !$#accession JQ1645 !'##molecule_type genomic RNA !'##residues 1-322 ##label HEN1 !'##cross-references EMBL:X65102; GB:S40191; NID:g61205; !1PIDN:CAA46226.1; PID:g61206 !$#accession PQ0426 !'##molecule_type protein !'##residues 59-69;80-89;270-279;294-304 ##label HEN2 CLASSIFICATION #superfamily potato virus coat protein KEYWORDS coat protein; glycoprotein FEATURE !$277 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 322 #molecular-weight 35819 #checksum 3880 SEQUENCE /// ENTRY JQ1738 #type complete TITLE coat protein - shallot virus X ORGANISM #formal_name shallot virus X DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 23-Jul-1999 ACCESSIONS JQ1738 REFERENCE JQ1734 !$#authors Kanyuka, K.V.; Vishnichenko, V.K.; Levay, K.E.; Kondrikov, !1D.Y.; Ryabov, E.V.; Zavriev, S.K. !$#journal J. Gen. Virol. (1992) 73:2553-2560 !$#title Nucleotide sequence of shallot virus X RNA reveals a !15'-proximal cistron closely related to those of potexviruses !1and a unique arrangement of the 3'-proximal cistrons. !$#cross-references MUID:93019008; PMID:1339468 !$#accession JQ1738 !'##molecule_type genomic RNA !'##residues 1-262 ##label KAN !'##cross-references GB:M97264; NID:g295078; PIDN:AAA47791.1; !1PID:g295083 CLASSIFICATION #superfamily potato virus coat protein KEYWORDS coat protein; glycoprotein FEATURE !$10,105,121,176 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 262 #molecular-weight 28487 #checksum 307 SEQUENCE /// ENTRY C45353 #type complete TITLE coat protein - apple chlorotic leaf spot virus (strain P863) ORGANISM #formal_name apple chlorotic leaf spot virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 17-Sep-1997 ACCESSIONS C45353; D45353 REFERENCE A45353 !$#authors German, S.; Candresse, T.; Lanneau, M.; Huet, J.C.; !1Pernollet, J.C.; Dunez, J. !$#journal Virology (1990) 179:104-112 !$#title Nucleotide sequence and genomic organization of apple !1chlorotic leaf spot closterovirus. !$#cross-references MUID:91021011; PMID:2219716 !$#accession C45353 !'##molecule_type genomic RNA !'##residues 1-250 ##label GE1 !'##cross-references GB:M58152; GB:M31714; NID:g210293 !'##note the sequence of PID:g210296 differs from the authors' !1translation !$#accession D45353 !'##molecule_type protein !'##residues 120-127 ##label GE2 !'##note the amino end of the mature protein is blocked CLASSIFICATION #superfamily apple chlorotic leaf spot virus coat protein KEYWORDS blocked amino end; coat protein; glycoprotein FEATURE !$46 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 250 #molecular-weight 28377 #checksum 2833 SEQUENCE /// ENTRY WMVYP5 #type complete TITLE nucleic acid-binding protein - potato virus M (strain Russian) ORGANISM #formal_name potato virus M #note host Lycopersicon esculentum (tomato) DATE 31-Mar-1990 #sequence_revision 23-Mar-1995 #text_change 29-Oct-1999 ACCESSIONS F54333; PN0006; PN0095; S21606 REFERENCE A54333 !$#authors Zavriev, S.K.; Kanyuka, K.V.; Levay, K.E. !$#journal J. Gen. Virol. (1991) 72:9-14 !$#title The genome organization of potato virus M RNA. !$#cross-references MUID:91116326; PMID:1990070 !$#accession F54333 !'##molecule_type genomic RNA !'##residues 1-108 ##label ZAV !'##cross-references EMBL:X53062; NID:g61291; PIDN:CAA37237.1; !1PID:g61297 REFERENCE A92800 !$#authors Rupasov, V.V.; Morozov, S.Y.; Kanyuka, K.V.; Zavriev, S.K. !$#journal J. Gen. Virol. (1989) 70:1861-1869 !$#title Partial nucleotide sequence of potato virus M RNA shows !1similarities to potexviruses in gene arrangement and the !1encoded amino acid sequences. !$#cross-references MUID:89293091; PMID:2738581 !$#accession PN0006 !'##molecule_type mRNA !'##residues 1-79,'LVSLTMCAWRNLLMKE' ##label RUP !'##note this sequence has been corrected REFERENCE PN0093 !$#authors Zavriev, S.K.; Kanyka, K.V.; Levay, K.E. !$#journal Mol. Biol. (Mosk.) (1991) 25:761-769 !$#title The complete nucleotide sequence of potato virus M genomic !1RNA. !$#cross-references MUID:92049299; PMID:1944258 !$#accession PN0095 !'##molecule_type genomic RNA !'##residues 1-108 ##label ZA2 !'##cross-references GB:X53062; NID:g61291; PIDN:CAA37237.1; PID:g61297 !'##note this is a revision to the sequence from reference A92800 REFERENCE S21601 !$#authors Zavriev, S.K. !$#submission submitted to the EMBL Data Library, May 1990 !$#accession S21606 !'##status preliminary !'##molecule_type genomic RNA !'##residues 1-79,'LVSLTMCAWRNLLMKE' ##label ZA3 !'##cross-references EMBL:X53062 !'##experimental_source Russian wild type CLASSIFICATION #superfamily potato virus nucleic acid-binding protein KEYWORDS DNA binding; metal binding; nucleotide binding; zinc finger FEATURE !$57-78 #region zinc finger SUMMARY #length 108 #molecular-weight 12183 #checksum 8275 SEQUENCE /// ENTRY JQ1646 #type complete TITLE nucleic acid-binding protein - poplar mosaic virus ORGANISM #formal_name poplar mosaic virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 23-Jul-1999 ACCESSIONS JQ1646; S23876 REFERENCE JQ1645 !$#authors Henderson, J.; Gibbs, M.J.; Edwards, M.L.; Clarke, V.A.; !1Gardner, K.A.; Cooper, J.I. !$#journal J. Gen. Virol. (1992) 73:1887-1890 !$#title Partial nucleotide sequence of poplar mosaic virus RNA !1confirms its classification as a carlavirus. !$#cross-references MUID:92333281; PMID:1629709 !$#accession JQ1646 !'##molecule_type genomic RNA !'##residues 1-121 ##label HEN !'##cross-references EMBL:X65102; NID:g61205; PIDN:CAA46227.1; !1PID:g61207 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1March 1992 CLASSIFICATION #superfamily potato virus nucleic acid-binding protein KEYWORDS DNA binding; zinc finger FEATURE !$62-83 #region zinc finger CCCC motif SUMMARY #length 121 #molecular-weight 14451 #checksum 6543 SEQUENCE /// ENTRY B48549 #type complete TITLE nucleic acid-binding protein - potato virus S ORGANISM #formal_name potato virus S DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 23-Jul-1999 ACCESSIONS B48549 REFERENCE A48549 !$#authors Foster, G.D.; Mills, P.R. !$#journal Virus Genes (1992) 6:213-220 !$#title The 3'-nucleotide sequence of an ordinary strain of potato !1virus S. !$#cross-references MUID:93033173; PMID:1413539 !$#accession B48549 !'##molecule_type genomic RNA !'##residues 1-94 ##label FOS !'##cross-references GB:S45593; NID:g256417; PIDN:AAB23462.1; !1PID:g256419 !'##note sequence extracted from NCBI backbone (NCBIN:114637, !1NCBIP:114639) CLASSIFICATION #superfamily potato virus nucleic acid-binding protein KEYWORDS DNA binding; zinc finger FEATURE !$55-75 #region zinc finger SUMMARY #length 94 #molecular-weight 10680 #checksum 4113 SEQUENCE /// ENTRY WMFM32 #type complete TITLE 32.4K protein - alfalfa mosaic virus ORGANISM #formal_name alfalfa mosaic virus, AMV DATE 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 23-Jul-1999 ACCESSIONS A04203 REFERENCE A93466 !$#authors Barker, R.F.; Jarvis, N.P.; Thompson, D.V.; Loesch-Fries, !1L.S.; Hall, T.C. !$#journal Nucleic Acids Res. (1983) 11:2881-2891 !$#title Complete nucleotide sequence of alfalfa mosaic virus RNA3. !$#cross-references MUID:83220826; PMID:6856479 !$#accession A04203 !'##molecule_type genomic RNA !'##residues 1-300 ##label BAR !'##cross-references GB:K02703; NID:g331428; PIDN:AAA46291.1; !1PID:g331429 GENETICS !$#map_position segment 3 CLASSIFICATION #superfamily alfalfa mosaic virus 32.4K protein SUMMARY #length 300 #molecular-weight 32398 #checksum 1285 SEQUENCE /// ENTRY WMBV3S #type complete TITLE 32.4K protein - alfalfa mosaic virus (strain Strasbourg) ALTERNATE_NAMES P3 protein ORGANISM #formal_name alfalfa mosaic virus, AMV #note host Nicotiana tabacum cv. Xanthi (tobacco) DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 23-Jul-1999 ACCESSIONS A04204 REFERENCE A90677 !$#authors Ravelonandro, M.; Pinck, M.; Pinck, L. !$#journal Biochimie (1984) 66:395-402 !$#title Complete nucleotide sequence of RNA 3 from alfalfa mosaic !1virus, strain S. !$#cross-references MUID:84281125; PMID:6205697 !$#accession A04204 !'##molecule_type genomic RNA !'##residues 1-300 ##label RAV !'##cross-references GB:X00819; NID:g58606; PIDN:CAA25392.1; PID:g58607 !'##note the authors translated the codon UCA for residue 38 as Leu, CAU !1for residue 128 as Thr, and UAC for residue 175 as Ile GENETICS !$#map_position segment 3 CLASSIFICATION #superfamily alfalfa mosaic virus 32.4K protein SUMMARY #length 300 #molecular-weight 32479 #checksum 1158 SEQUENCE /// ENTRY WMFMYS #type complete TITLE 32.4K transport protein - alfalfa mosaic virus (strain YSMV) ALTERNATE_NAMES 32.4K movement protein; P3 protein ORGANISM #formal_name alfalfa mosaic virus, AMV #note host Nicotiana tabacum cv. Samsun NN (tobacco) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 23-Jul-1999 ACCESSIONS A37948 REFERENCE A37948 !$#authors Neeleman, L.; Van Der Kuyl, A.C.; Bol, J.F. !$#journal Virology (1991) 181:687-693 !$#title Role of alfalfa mosaic virus coat protein gene in symptom !1formation. !$#cross-references MUID:91196260; PMID:2014643 !$#accession A37948 !'##molecule_type genomic RNA !'##residues 1-300 ##label NEE !'##cross-references EMBL:M59241; NID:g331421; PIDN:AAA46287.1; !1PID:g331422 COMMENT This protein may play a role in cell-to-cell transport. GENETICS !$#map_position segment 3 CLASSIFICATION #superfamily alfalfa mosaic virus 32.4K protein KEYWORDS transport protein SUMMARY #length 300 #molecular-weight 32395 #checksum 1271 SEQUENCE /// ENTRY WMBV3T #type complete TITLE 31.7K protein - tobacco streak virus (strain WC) ALTERNATE_NAMES P3 protein ORGANISM #formal_name tobacco streak virus, TSV #note host Nicotiana glutinosa x N. clevelandii (tobacco) DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 23-Jul-1999 ACCESSIONS A04205 REFERENCE A93507 !$#authors Cornelissen, B.J.C.; Janssen, H.; Zuidema, D.; Bol, J.F. !$#journal Nucleic Acids Res. (1984) 12:2427-2437 !$#title Complete nucleotide sequence of tobacco streak virus RNA 3. !$#cross-references MUID:84169544; PMID:6546793 !$#accession A04205 !'##molecule_type genomic RNA !'##residues 1-289 ##label COR !'##cross-references GB:X00435; NID:g62146; PIDN:CAA25132.1; PID:g62147 GENETICS !$#map_position segment 3 CLASSIFICATION #superfamily alfalfa mosaic virus 32.4K protein SUMMARY #length 289 #molecular-weight 31674 #checksum 8119 SEQUENCE /// ENTRY VCBVWC #type complete TITLE coat protein - tobacco streak virus (strain WC) ALTERNATE_NAMES P4 protein ORGANISM #formal_name tobacco streak virus, TSV #note host Nicotiana glutinosa x N. clevelandii (tobacco) DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 23-Jul-1999 ACCESSIONS A04206 REFERENCE A93507 !$#authors Cornelissen, B.J.C.; Janssen, H.; Zuidema, D.; Bol, J.F. !$#journal Nucleic Acids Res. (1984) 12:2427-2437 !$#title Complete nucleotide sequence of tobacco streak virus RNA 3. !$#cross-references MUID:84169544; PMID:6546793 !$#accession A04206 !'##molecule_type genomic RNA !'##residues 1-237 ##label COR !'##cross-references GB:X00435; NID:g62146; PIDN:CAA25133.1; PID:g62148 GENETICS !$#map_position segment 3 CLASSIFICATION #superfamily tobacco streak virus coat protein SUMMARY #length 237 #molecular-weight 26237 #checksum 3595 SEQUENCE /// ENTRY GNBVEV #type complete TITLE genome polyprotein - tobacco etch virus CONTAINS 49K proteinase; coat protein; nuclear inclusion protein; probable RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name tobacco etch virus, TEV #note host Nicotiana tabacum (tobacco) DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 19-Jan-2001 ACCESSIONS A04207; S02595 REFERENCE A04207 !$#authors Allison, R.; Johnston, R.E.; Dougherty, W.G. !$#journal Virology (1986) 154:9-20 !$#title The nucleotide sequence of the coding region of tobacco etch !1virus genomic RNA: evidence for the synthesis of a single !1polyprotein. !$#accession A04207 !'##molecule_type genomic RNA !'##residues 1-3054 ##label ALL REFERENCE S02595 !$#authors Dougherty, W.G.; Carrington, J.C.; Cary, S.M.; Parks, T.D. !$#journal EMBO J. (1988) 7:1281-1287 !$#title Biochemical and mutational analysis of a plant virus !1polyprotein cleavage site. !$#cross-references MUID:88312575; PMID:3409865 !$#accession S02595 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 2784-2797 ##label DOU CLASSIFICATION #superfamily tobacco etch virus genome polyprotein KEYWORDS ATP; coat protein; genome-linked protein; nucleotide !1binding; nucleotidyltransferase; P-loop; phosphoprotein; !1polyprotein FEATURE !$1-1796 #product 70K protein #status predicted #label M70K\ !$1247-1254 #region nucleotide-binding motif A (P-loop)\ !$1332-1337 #region nucleotide-binding motif B\ !$1336-1339 #region DEXH motif\ !$1797-1849 #product 6K protein #status predicted #label M6K\ !$1850-2279 #product 49K proteinase (49K nuclear inclusion !8protein) #status predicted #label M49K\ !$2280-2791 #product 54K nuclear inclusion protein #status !8predicted #label M54K\ !$2792-3054 #product coat protein #status predicted #label CPT\ !$1163-1164 #cleavage_site Gln-Ser (49K proteinase) #status !8predicted\ !$1796-1797 #cleavage_site Gln-Ser (49K proteinase) #status !8predicted\ !$1849-1850 #cleavage_site Gln-Gly (49K proteinase) #status !8predicted\ !$1911 #binding_site phosphoryl-RNA (Tyr) (covalent) #status !8predicted\ !$2279-2280 #cleavage_site Gln-Gly (49K proteinase) #status !8predicted\ !$2791-2792 #cleavage_site Gln-Ser (49K proteinase) #status !8experimental SUMMARY #length 3054 #molecular-weight 346162 #checksum 6554 SEQUENCE /// ENTRY GNVSTV #type complete TITLE genome polyprotein - tobacco vein mottling virus CONTAINS 29K protein; 34K protein; coat protein; cylindrical inclusion protein; helper component protein; nuclear inclusion protein a; nuclear inclusion protein b ORGANISM #formal_name tobacco vein mottling virus, TVMV DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 19-Jan-2001 ACCESSIONS A23647 REFERENCE A23647 !$#authors Domier, L.L.; Franklin, K.M.; Shahabuddin, M.; Hellmann, !1G.M.; Overmeyer, J.H.; Hiremath, S.T.; Siaw, M.F.E.; !1Lomonossoff, G.P.; Shaw, J.G.; Rhoads, R.E. !$#journal Nucleic Acids Res. (1986) 14:5417-5430 !$#title The nucleotide sequence of tobacco vein mottling virus RNA. !$#cross-references MUID:86286553; PMID:3737407 !$#accession A23647 !'##molecule_type genomic RNA !'##residues 1-3005 ##label DOM !'##cross-references EMBL:X04083; NID:g61306; PID:g61307 REFERENCE A30631 !$#authors Murphy, J.F.; Rychlik, W.; Rhoads, R.E.; Hunt, A.G.; Shaw, !1J.G. !$#journal J. Virol. (1991) 65:511-513 !$#title A tyrosine residue in the small nuclear inclusion protein of !1tobacco vein mottling virus links the VPg to the viral RNA. !$#cross-references MUID:91087329; PMID:1702164 !$#contents annotation; identification of tyrosine RNA attachment site CLASSIFICATION #superfamily tobacco etch virus genome polyprotein KEYWORDS ATP; coat protein; cylindrical inclusion protein; !1genome-linked protein; inclusion protein; nucleotide !1binding; nucleus; P-loop; phosphoprotein; polyprotein FEATURE !$1-247 #product 34K protein #status predicted #label KPT\ !$248-731 #product helper component protein #status predicted !8#label HCP\ !$732-1112 #product 29K protein #status predicted #label KPR\ !$1113-1747 #product cylindrical inclusion protein #status !8predicted #label CIP\ !$1197-1204 #region nucleotide-binding motif A (P-loop)\ !$1282-1287 #region nucleotide-binding motif B\ !$1286-1289 #region DEXH motif\ !$1748-2224 #product nuclear inclusion protein a #status !8predicted #label NIA\ !$2225-2740 #product nuclear inclusion protein b #status !8predicted #label NIB\ !$2741-3005 #product coat protein #status predicted #label CPT\ !$1860 #binding_site phosphoryl-RNA (Tyr) (covalent) #status !8experimental SUMMARY #length 3005 #molecular-weight 340263 #checksum 2726 SEQUENCE /// ENTRY A44062 #type complete TITLE genome polyprotein - pepper mottle virus (strain California) CONTAINS 29K protein; 34K protein; coat protein; cylindrical inclusion protein; helper component protein; nuclear inclusion protein a; nuclear inclusion protein b ORGANISM #formal_name pepper mottle virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 19-Jan-2001 ACCESSIONS A44062 REFERENCE A44062 !$#authors Vance, V.B.; Moore, D.; Turpen, T.H.; Bracker, A.; !1Hollowell, V.C. !$#journal Virology (1992) 191:19-30 !$#title The complete nucleotide sequence of pepper mottle virus !1genomic RNA: comparison of the encoded polyprotein with !1those of other sequenced potyviruses. !$#cross-references MUID:93033110; PMID:1413501 !$#accession A44062 !'##molecule_type genomic RNA !'##residues 1-3068 ##label VAN !'##cross-references GB:M96425; NID:g332869; PIDN:AAA46903.1; !1PID:g332870 CLASSIFICATION #superfamily tobacco etch virus genome polyprotein KEYWORDS ATP; coat protein; cylindrical inclusion protein; !1genome-linked protein; inclusion protein; nucleotide !1binding; nucleus; P-loop; phosphoprotein; polyprotein FEATURE !$1-287 #product 34K protein #status predicted #label KPT\ !$288-743 #product helper component protein #status predicted !8#label HCP\ !$744-1156 #product 29K protein #status predicted #label KPR\ !$1157-1790 #product cylindrical inclusion protein #status !8predicted #label CIP\ !$1241-1248 #region nucleotide-binding motif A (P-loop)\ !$1326-1331 #region nucleotide-binding motif B\ !$1330-1333 #region DEXH motif\ !$1791-2276 #product nuclear inclusion protein a #status !8predicted #label NIA\ !$2277-2799 #product nuclear inclusion protein b #status !8predicted #label NIB\ !$2800-3068 #product coat protein #status predicted #label CPT\ !$1906 #binding_site phosphoryl-RNA (Tyr) (covalent) #status !8predicted SUMMARY #length 3068 #molecular-weight 348653 #checksum 2964 SEQUENCE /// ENTRY JN0545 #type complete TITLE genome polyprotein - potato virus Y (isolate Hungary) CONTAINS 29K protein; 34K protein; coat protein; cylindrical inclusion protein; helper component protein; nuclear inclusion protein a; nuclear inclusion protein b ORGANISM #formal_name potato virus Y, PVY DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 19-Jan-2001 ACCESSIONS JN0545 REFERENCE JN0545 !$#authors Thole, V.; Dalmay, T.; Burgyan, J.; Balazs, E. !$#journal Gene (1993) 123:149-156 !$#title Cloning and sequencing of potato virus Y (Hungarian isolate) !1genomic RNA. !$#cross-references MUID:93154578; PMID:8428653 !$#accession JN0545 !'##molecule_type genomic RNA !'##residues 1-3061 ##label THO !'##cross-references GB:M95491; NID:g294438; PIDN:AAB59762.1; !1PID:g294439 CLASSIFICATION #superfamily tobacco etch virus genome polyprotein KEYWORDS ATP; coat protein; cylindrical inclusion protein; !1genome-linked protein; inclusion protein; nucleotide !1binding; nucleus; P-loop; phosphoprotein; polyprotein FEATURE !$1-275 #product 34K protein #status predicted #label KPT\ !$276-740 #product helper component protein #status predicted !8#label HCP\ !$741-1157 #product 29K protein #status predicted #label KPR\ !$1158-1791 #product cylindrical inclusion protein #status !8predicted #label CIP\ !$1242-1249 #region nucleotide-binding motif A (P-loop)\ !$1327-1332 #region nucleotide-binding motif B\ !$1331-1334 #region DEXH motif\ !$1792-2275 #product nuclear inclusion protein a #status !8predicted #label NIA\ !$2276-2794 #product nuclear inclusion protein b #status !8predicted #label NIB\ !$2795-3061 #product coat protein #status predicted #label CPT\ !$1907 #binding_site phosphoryl-RNA (Tyr) (covalent) #status !8predicted SUMMARY #length 3061 #molecular-weight 347328 #checksum 1805 SEQUENCE /// ENTRY GNVSPP #type complete TITLE genome polyprotein - plum pox virus (strain NAT) CONTAINS 29K protein; 34K protein; coat protein; cylindrical inclusion protein; helper component protein; nuclear inclusion protein a; nuclear inclusion protein b ORGANISM #formal_name plum pox virus, PPV #note host Nicotiana clevelandii (tobacco) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 19-Jan-2001 ACCESSIONS JQ0003; JU0089 REFERENCE A92802 !$#authors Maiss, E.; Timpe, U.; Brisske, A.; Jelkmann, W.; Casper, R.; !1Himmler, G.; Mattanovich, D.; Katinger, H.W.D. !$#journal J. Gen. Virol. (1989) 70:513-524 !$#title The complete nucleotide sequence of plum pox virus RNA. !$#cross-references MUID:89279232; PMID:2732699 !$#accession JQ0003 !'##molecule_type genomic RNA !'##residues 1-3125 ##label MAI !'##cross-references GB:D13751; GB:D00424; NID:g222408; PIDN:BAA02898.1; !1PID:g222409 CLASSIFICATION #superfamily tobacco etch virus genome polyprotein KEYWORDS ATP; coat protein; cylindrical inclusion protein; !1genome-linked protein; inclusion protein; nucleotide !1binding; nucleus; P-loop; phosphoprotein; polyprotein FEATURE !$1-301 #product 34K protein #status predicted #label PRO\ !$302-914 #product helper component protein #status predicted !8#label HCP\ !$915-1168 #product 29K protein #status predicted #label PRT\ !$1169-1856 #product cylindrical inclusion protein #status !8predicted #label CIP\ !$1253-1260 #region nucleotide-binding motif A (P-loop)\ !$1338-1343 #region nucleotide-binding motif B\ !$1342-1345 #region DEXH motif\ !$1857-2292 #product nuclear inclusion protein a #status !8predicted #label NIA\ !$2293-2810 #product nuclear inclusion protein b #status !8predicted #label NIB\ !$2811-3125 #product coat protein #status predicted #label COP\ !$1919 #binding_site phosphoryl-RNA (Tyr) (covalent) #status !8predicted SUMMARY #length 3125 #molecular-weight 354263 #checksum 5925 SEQUENCE /// ENTRY GNVSPD #type complete TITLE genome polyprotein - plum pox virus (strain D) CONTAINS 29K protein; 34K protein; coat protein (capsid protein); cylindrical inclusion protein; helper component protein; nuclear inclusion protein a; nuclear inclusion protein b ORGANISM #formal_name plum pox virus, PPV DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 19-Jan-2001 ACCESSIONS S06929; JA0078 REFERENCE S06929 !$#authors Teycheney, P.Y.; Tavert, G.; Delbos, R.; Ravelonandro, M.; !1Dunez, J. !$#journal Nucleic Acids Res. (1989) 17:10115-10116 !$#title The complete nucleotide sequence of plum pox virus RNA !1(strain D). !$#cross-references MUID:90098790; PMID:2602121 !$#accession S06929 !'##status translation not shown !'##molecule_type genomic RNA !'##residues 1-3141 ##label TEY !'##cross-references EMBL:X16415 REFERENCE JA0078 !$#authors Ravelonandro, M.; Varveri, C.; Delbos, R.; Dunez, J. !$#journal J. Gen. Virol. (1988) 69:1509-1516 !$#title Nucleotide sequence of the capsid protein gene of plum pox !1potyvirus. !$#accession JA0078 !'##molecule_type genomic RNA !'##residues 2709,'QT',2712,'L',2714,2810-3141 ##label RAV !'##cross-references GB:D00298; NID:g222410; PIDN:BAA00210.1; !1PID:g222411 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing CLASSIFICATION #superfamily tobacco etch virus genome polyprotein KEYWORDS ATP; coat protein; cylindrical inclusion protein; !1genome-linked protein; inclusion protein; nucleotide !1binding; nucleus; P-loop; phosphoprotein; polyprotein FEATURE !$1-301 #product 34K protein #status predicted #label PRO\ !$302-915 #product helper component protein #status predicted !8#label HCP\ !$916-1169 #product 29K protein #status predicted #label PRT\ !$1170-1857 #product cylindrical inclusion protein #status !8predicted #label CIP\ !$1254-1261 #region nucleotide-binding motif A (P-loop)\ !$1339-1344 #region nucleotide-binding motif B\ !$1343-1346 #region DEXH motif\ !$1858-2293 #product nuclear inclusion protein a #status !8predicted #label NIA\ !$2294-2811 #product nuclear inclusion protein b #status !8predicted #label NIB\ !$2812-3141 #product coat protein #status predicted #label COP\ !$1920 #binding_site phosphoryl-RNA (Tyr) (covalent) #status !8predicted SUMMARY #length 3141 #molecular-weight 355551 #checksum 3143 SEQUENCE /// ENTRY GNVSRA #type complete TITLE genome polyprotein - plum pox virus (strain Rankovic) CONTAINS 29K protein; 34K protein; coat protein; cylindrical inclusion protein; helper component protein; nuclear inclusion protein a; nuclear inclusion protein b ORGANISM #formal_name plum pox virus, PPV #note host Nicotiana clevelandii (tobacco) DATE 30-Jun-1993 #sequence_revision 30-Sep-1993 #text_change 19-Jan-2001 ACCESSIONS A60009; A42761; B42761; JA0138 REFERENCE A60009 !$#authors Lain, S.; Riechmann, J.L.; Garcia, J.A. !$#journal Virus Res. (1989) 13:157-172 !$#title The complete nucleotide sequence of plum pox potyvirus RNA. !$#cross-references MUID:89370814; PMID:2773595 !$#accession A60009 !'##molecule_type genomic RNA !'##residues 1-3140 ##label LAI REFERENCE A42761 !$#authors Lain, S.; Riechmann, J.L.; Mendez, E.; Garcia, J.A. !$#journal Virus Res. (1988) 10:325-342 !$#title Nucleotide sequence of the 3' terminal region of plum pox !1potyvirus RNA. !$#accession A42761 !'##molecule_type genomic RNA !'##residues 2263-2874,'G',2876-3140 ##label LA1 !'##cross-references GB:M21847; NID:g333301; PIDN:AAA85458.1; !1PID:g333302 !$#accession B42761 !'##molecule_type protein !'##residues 2811-2815;2881-2893 ##label LA2 CLASSIFICATION #superfamily tobacco etch virus genome polyprotein KEYWORDS ATP; coat protein; cylindrical inclusion protein; !1genome-linked protein; inclusion protein; nucleotide !1binding; nucleus; P-loop; phosphoprotein; polyprotein FEATURE !$1-301 #product 34K protein #status predicted #label PRO\ !$302-914 #product helper component protein #status predicted !8#label HCP\ !$915-1168 #product 29K protein #status predicted #label PRT\ !$1169-1856 #product cylindrical inclusion protein #status !8predicted #label CIP\ !$1253-1260 #region nucleotide-binding motif A (P-loop)\ !$1338-1343 #region nucleotide-binding motif B\ !$1342-1345 #region DEXH motif\ !$1857-2292 #product nuclear inclusion protein a #status !8predicted #label NIA\ !$2293-2810 #product nuclear inclusion protein b #status !8predicted #label NIB\ !$2811-3140 #product coat protein #status predicted #label COP\ !$1919 #binding_site phosphoryl-RNA (Tyr) (covalent) #status !8predicted SUMMARY #length 3140 #molecular-weight 355579 #checksum 7922 SEQUENCE /// ENTRY JQ1895 #type complete TITLE genome polyprotein - turnip mosaic virus CONTAINS coat protein; cytoplasmic inclusion protein; helper component protein; nuclear inclusion a protein; nuclear inclusion b protein; P1 protein; P3 protein; p6K1 protein; p6K2 protein; VPg protein ORGANISM #formal_name turnip mosaic virus, TuMV DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 19-Jan-2001 ACCESSIONS JQ1895; JQ1168; PQ0217 REFERENCE JQ1895 !$#authors Nicolas, O.; Laliberte, J.F. !$#journal J. Gen. Virol. (1992) 73:2785-2793 !$#title The complete nucleotide sequence of turnip mosaic potyvirus !1RNA. !$#cross-references MUID:93057350; PMID:1431807 !$#accession JQ1895 !'##molecule_type mRNA !'##residues 1-3163 ##label NIC !'##cross-references DDBJ:D10927; NID:g222660; PIDN:BAA01725.1; !1PID:g222661 !'##experimental_source strain Quebec REFERENCE JQ1168 !$#authors Tremblay, M.F.; Nicolas, O.; Sinha, R.C.; Lazure, C.; !1Laliberte, J.F. !$#journal J. Gen. Virol. (1990) 71:2769-2772 !$#title Sequence of the 3'-terminal region of turnip mosaic virus !1RNA and the capsid protein gene. !$#cross-references MUID:91073142; PMID:2254757 !$#accession JQ1168 !'##molecule_type genomic RNA !'##residues 1534-2861,'G',2863-3163 ##label TRE !'##cross-references GB:D10601; GB:D01090; NID:g222658; PIDN:BAA01452.1; !1PID:g222659 !$#accession PQ0217 !'##molecule_type protein !'##residues 2876-2892;2929-2941;3118-3141 ##label TR2 CLASSIFICATION #superfamily tobacco etch virus genome polyprotein KEYWORDS ATP; coat protein; genome-linked protein; inclusion protein; !1nucleotide binding; nucleus; P-loop; phosphoprotein; !1polyprotein FEATURE !$1-362 #product P1 protein #status predicted #label P1P\ !$363-820 #product helper component protein #status predicted !8#label HCP\ !$821-1175 #product P3 protein #status predicted #label P3P\ !$1176-1227 #product p6K1 protein #status predicted #label P6P\ !$1228-1870 #product cytoplasmic inclusion protein #status !8predicted #label CIP\ !$1313-1320 #region nucleotide-binding motif A (P-loop)\ !$1398-1403 #region nucleotide-binding motif B\ !$1402-1405 #region DEXH motif\ !$1871-1923 #product p6K2 protein #status predicted #label PKP\ !$1924-2115 #product VPg protein #status predicted #label VPG\ !$2116-2358 #product nuclear inclusion a protein #status !8predicted #label NIA\ !$2359-2875 #product nuclear inclusion b protein #status !8predicted #label NIB\ !$2876-3163 #product coat (capsid) protein #status experimental !8#label CAP\ !$1986 #binding_site phosphoryl-RNA (Tyr) (covalent) #status !8predicted SUMMARY #length 3163 #molecular-weight 357819 #checksum 4441 SEQUENCE /// ENTRY GNVSPV #type complete TITLE genome polyprotein - pea seed-borne mosaic virus (strain DPD1) CONTAINS 47K protein; 49K proteinase (EC 3.4.22.-), nuclear inclusion protein a; 6K protein; coat protein; cytoplasmic inclusion protein; helper component-proteinase (EC 3.4.22.-); RNA-directed RNA polymerase (EC 2.7.7.48), nuclear inclusion protein b ORGANISM #formal_name pea seed-borne mosaic virus, PSbMV DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 19-Jan-2001 ACCESSIONS JQ1331 REFERENCE JQ1331 !$#authors Johansen, E.; Rasmussen, O.F.; Heide, M.; Borkhardt, B. !$#journal J. Gen. Virol. (1991) 72:2625-2632 !$#title The complete nucleotide sequence of pea seed-borne mosaic !1virus RNA. !$#cross-references MUID:92044431; PMID:1940858 !$#accession JQ1331 !'##molecule_type genomic RNA !'##residues 1-3206 ##label JOH !'##cross-references GB:D10930; GB:D01152; NID:g220995; PIDN:BAA01726.1; !1PID:g286190 COMMENT Helper component-proteinase is required for aphid !1transmission and also has proteolytic activity. COMMENT Cytoplasmic inclusion protein has helicase activity. COMMENT Nuclear inclusion protein a is covalently linked to the !1genomic RNA and also has proteolytic activity. COMMENT Nuclear inclusion protein b has RNA polymerase activity. CLASSIFICATION #superfamily tobacco etch virus genome polyprotein KEYWORDS ATP; coat protein; cysteine proteinase; genome-linked !1protein; hydrolase; inclusion protein; nucleotide binding; !1nucleotidyltransferase; P-loop; phosphoprotein; polyprotein FEATURE !$1-856 #product helper component-proteinase #status !8predicted #label NTE\ !$857-1266 #product 47K protein #status predicted #label 47P\ !$1267-1902 #product cytoplasmic inclusion protein #status !8predicted #label CYT\ !$1351-1358 #region nucleotide-binding motif A (P-loop)\ !$1436-1441 #region nucleotide-binding motif B\ !$1440-1443 #region DEXH motif\ !$1903-1955 #product 6K protein #status predicted #label 6KP\ !$1956-2395 #product nuclear inclusion protein a #status !8predicted #label NIA\ !$2396-2915 #product nuclear inclusion protein b #status !8predicted #label NIB\ !$2916-3206 #product coat protein #status predicted #label COA\ !$2016 #binding_site phosphoryl-RNA (Tyr) (covalent) #status !8predicted SUMMARY #length 3206 #molecular-weight 364273 #checksum 1325 SEQUENCE /// ENTRY JQ1661 #type complete TITLE genome polyprotein - soybean mosaic virus (strain G2) CONTAINS 27K protein; 35K protein; 42K protein; 6K protein; coat protein; cylindrical inclusion protein; helper component-protein; RNA-directed RNA polymerase (EC 2.7.7.48); VPg protein ORGANISM #formal_name soybean mosaic virus, SbMV DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 19-Jan-2001 ACCESSIONS JQ1661 REFERENCE JQ1661 !$#authors Jayaram, C.; Hill, J.H.; Miller, W.A. !$#journal J. Gen. Virol. (1992) 73:2067-2077 !$#title Complete nucleotide sequences of two soybean mosaic virus !1strains differentiated by response of soybean containing the !1Rsv resistance gene. !$#cross-references MUID:92356085; PMID:1645142 !$#accession JQ1661 !'##molecule_type genomic RNA !'##residues 1-3066 ##label JAY !'##cross-references GB:S42280; NID:g253297; PIDN:AAB22819.2; !1PID:g5705963 CLASSIFICATION #superfamily tobacco etch virus genome polyprotein KEYWORDS ATP; coat protein; cylindrical inclusion protein; !1genome-linked protein; nucleotide binding; !1nucleotidyltransferase; P-loop; phosphoprotein; polyprotein FEATURE !$1-308 #product 35K protein #status predicted #label PT1\ !$309-765 #product helper component-protein #status predicted !8#label HCP\ !$766-1164 #product 42K protein #status predicted #label PT2\ !$1165-1798 #product cylindrical inclusion protein #status !8predicted #label CIP\ !$1249-1256 #region nucleotide-binding motif A (P-loop)\ !$1334-1339 #region nucleotide-binding motif B\ !$1338-1341 #region DEXH motif\ !$1799-1852 #product 6K protein #status predicted #label PT3\ !$1853-2041 #product VPg protein #status predicted #label VPG\ !$2042-2284 #product 27K protein #status predicted #label PT4\ !$2285-2801 #product RNA-directed RNA polymerase #status !8predicted #label POL\ !$2802-3066 #product coat protein #status predicted #label COP\ !$1915 #binding_site phosphoryl-RNA (Tyr) (covalent) #status !8predicted SUMMARY #length 3066 #molecular-weight 349541 #checksum 9472 SEQUENCE /// ENTRY JQ1662 #type complete TITLE genome polyprotein - soybean mosaic virus (strain G7) CONTAINS 27K protein; 35K protein; 42K protein; 6K protein; coat protein; cylindrical inclusion protein; helper component-protein; RNA-directed RNA polymerase (EC 2.7.7.48); VPg protein ORGANISM #formal_name soybean mosaic virus, SbMV DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 19-Jan-2001 ACCESSIONS JQ1662 REFERENCE JQ1661 !$#authors Jayaram, C.; Hill, J.H.; Miller, W.A. !$#journal J. Gen. Virol. (1992) 73:2067-2077 !$#title Complete nucleotide sequences of two soybean mosaic virus !1strains differentiated by response of soybean containing the !1Rsv resistance gene. !$#cross-references MUID:92356085; PMID:1645142 !$#accession JQ1662 !'##molecule_type genomic RNA !'##residues 1-3066 ##label JAY !'##cross-references GB:S42280 !'##note the authors translated the codon TTG for residue 2358 as Phe CLASSIFICATION #superfamily tobacco etch virus genome polyprotein KEYWORDS ATP; coat protein; cylindrical inclusion protein; !1genome-linked protein; nucleotide binding; !1nucleotidyltransferase; P-loop; phosphoprotein; polyprotein FEATURE !$1-308 #product 35K protein #status predicted #label PT1\ !$309-765 #product helper component-protein #status predicted !8#label HCP\ !$766-1164 #product 42K protein #status predicted #label PT2\ !$1165-1798 #product cylindrical inclusion protein #status !8predicted #label CIP\ !$1249-1256 #region nucleotide-binding motif A (P-loop)\ !$1334-1339 #region nucleotide-binding motif B\ !$1338-1341 #region DEXH motif\ !$1799-1852 #product 6K protein #status predicted #label PT3\ !$1853-2041 #product VPg protein #status predicted #label VPG\ !$2042-2284 #product 27K protein #status predicted #label PT4\ !$2285-2801 #product RNA-directed RNA polymerase #status !8predicted #label POL\ !$2802-3066 #product coat protein #status predicted #label COP\ !$1915 #binding_site phosphoryl-RNA (Tyr) (covalent) #status !8predicted SUMMARY #length 3066 #molecular-weight 349705 #checksum 1346 SEQUENCE /// ENTRY GNVSSC #type fragment TITLE genome polyprotein - sugarcane mosaic virus (strain SC) (fragment) CONTAINS carboxyl end of nuclear inclusion protein b; coat protein ORGANISM #formal_name sugarcane mosaic virus, SCMV DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 17-Nov-2000 ACCESSIONS PH0207 REFERENCE PH0207 !$#authors Frenkel, M.J.; Jilka, J.M.; McKern, N.M.; Strike, P.M.; !1Clark Jr., J.M.; Shukla, D.D.; Ward, C.W. !$#journal J. Gen. Virol. (1991) 72:237-242 !$#title Unexpected sequence diversity in the amino-terminal ends of !1the coat proteins of strains of sugarcane mosaic virus. !$#cross-references MUID:91132116; PMID:1993866 !$#accession PH0207 !'##molecule_type genomic RNA !'##residues 1-365 ##label FRE !'##cross-references GB:D00948; NID:g222123; PIDN:BAA00796.1; !1PID:g222124 CLASSIFICATION #superfamily tobacco etch virus genome polyprotein KEYWORDS coat protein; inclusion protein FEATURE !$1-52 #product nuclear inclusion protein b (fragment) !8#status predicted #label IPB\ !$53-365 #product coat protein #status predicted #label COA SUMMARY #length 365 #checksum 4869 SEQUENCE /// ENTRY GNVSMB #type fragment TITLE genome polyprotein - maize dwarf mosaic virus (strain B) (fragment) CONTAINS carboxyl end of nuclear inclusion protein b; coat protein ORGANISM #formal_name maize dwarf mosaic virus, MDMV DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 17-Nov-2000 ACCESSIONS PH0208 REFERENCE PH0207 !$#authors Frenkel, M.J.; Jilka, J.M.; McKern, N.M.; Strike, P.M.; !1Clark Jr., J.M.; Shukla, D.D.; Ward, C.W. !$#journal J. Gen. Virol. (1991) 72:237-242 !$#title Unexpected sequence diversity in the amino-terminal ends of !1the coat proteins of strains of sugarcane mosaic virus. !$#cross-references MUID:91132116; PMID:1993866 !$#accession PH0208 !'##molecule_type genomic RNA !'##residues 1-380 ##label FRE !'##cross-references GB:D00949; NID:g222059; PIDN:BAA00797.1; !1PID:g222060 CLASSIFICATION #superfamily tobacco etch virus genome polyprotein KEYWORDS coat protein; inclusion protein FEATURE !$1-52 #product nuclear inclusion protein b (fragment) !8#status predicted #label NIP\ !$53-380 #product coat protein #status predicted #label COA SUMMARY #length 380 #checksum 1190 SEQUENCE /// ENTRY VCVZWT #type fragment TITLE coat protein - passionfruit woodiness virus (strain Tip Bright) (fragment) ORGANISM #formal_name passionfruit woodiness virus, PWV #note host Passiflora edulis DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 17-Nov-2000 ACCESSIONS A60078 REFERENCE A60078 !$#authors Shukla, D.D.; McKern, N.M.; Ward, C.W. !$#journal Arch. Virol. (1988) 102:221-232 !$#title Coat protein of potyviruses: symptomatology, serology, and !1coat protein sequences of three strains of passionfruit !1woodiness virus. !$#cross-references MUID:89075954; PMID:3202695 !$#accession A60078 !'##molecule_type protein !'##residues 1-269 ##label SHU COMMENT This protein is expressed as a genome polyprotein. CLASSIFICATION #superfamily tobacco etch virus genome polyprotein KEYWORDS coat protein; polyprotein SUMMARY #length 269 #checksum 5462 SEQUENCE /// ENTRY VCVSWS #type fragment TITLE coat protein - passionfruit woodiness virus (strain severe) (fragment) ORGANISM #formal_name passionfruit woodiness virus, PWV #note host Passiflora edulis DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 17-Nov-2000 ACCESSIONS B60078 REFERENCE A60078 !$#authors Shukla, D.D.; McKern, N.M.; Ward, C.W. !$#journal Arch. Virol. (1988) 102:221-232 !$#title Coat protein of potyviruses: symptomatology, serology, and !1coat protein sequences of three strains of passionfruit !1woodiness virus. !$#cross-references MUID:89075954; PMID:3202695 !$#accession B60078 !'##molecule_type protein !'##residues 1-269 ##label SHU COMMENT This protein is expressed as a genome polyprotein. CLASSIFICATION #superfamily tobacco etch virus genome polyprotein KEYWORDS coat protein; polyprotein SUMMARY #length 269 #checksum 5233 SEQUENCE /// ENTRY VCVSWM #type fragment TITLE coat protein - passionfruit woodiness virus (strain mild) (fragment) ORGANISM #formal_name passionfruit woodiness virus, PWV #note host Passiflora edulis DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 17-Nov-2000 ACCESSIONS C60078 REFERENCE A60078 !$#authors Shukla, D.D.; McKern, N.M.; Ward, C.W. !$#journal Arch. Virol. (1988) 102:221-232 !$#title Coat protein of potyviruses: symptomatology, serology, and !1coat protein sequences of three strains of passionfruit !1woodiness virus. !$#cross-references MUID:89075954; PMID:3202695 !$#accession C60078 !'##molecule_type protein !'##residues 1-269 ##label SHU COMMENT This protein is expressed as a genome polyprotein. CLASSIFICATION #superfamily tobacco etch virus genome polyprotein KEYWORDS coat protein; polyprotein SUMMARY #length 269 #checksum 4218 SEQUENCE /// ENTRY JQ1537 #type complete TITLE genome polyprotein 1 - barley yellow mosaic virus (isolate German) CONTAINS coat protein; probable RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name barley yellow mosaic virus, BaYMV DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 19-Jan-2001 ACCESSIONS JQ1537 REFERENCE JQ1537 !$#authors Peerenboom, E.; Proels, M.; Schell, J.; Steinbiss, H.H.; !1Davidson, A.D. !$#journal J. Gen. Virol. (1992) 73:1303-1308 !$#title The complete nucleotide sequence of RNA 1 of a German !1isolate of barley yellow mosaic virus and its comparison !1with a Japanese isolate. !$#cross-references MUID:92268893; PMID:1588327 !$#accession JQ1537 !'##molecule_type genomic RNA !'##residues 1-2412 ##label PEE !'##cross-references GB:X69757; NID:g58678; PIDN:CAA49412.1; PID:g58679 GENETICS !$#map_position segment 1 CLASSIFICATION #superfamily tobacco etch virus genome polyprotein KEYWORDS ATP; coat protein; nucleotide binding; !1nucleotidyltransferase; P-loop; polyprotein FEATURE !$1-2115 #product probable RNA-directed RNA polymerase #status !8predicted #label RRP\ !$487-494 #region nucleotide-binding motif A (P-loop)\ !$579-584 #region nucleotide-binding motif B\ !$583-586 #region DEAH motif\ !$2116-2412 #product coat protein #status predicted #label CPR SUMMARY #length 2412 #molecular-weight 270874 #checksum 6215 SEQUENCE /// ENTRY JQ1948 #type complete TITLE genome polyprotein 1 - barley yellow mosaic virus (strain II-1) CONTAINS coat protein; RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name barley yellow mosaic virus, BaYMV DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 19-Jan-2001 ACCESSIONS JQ1948 REFERENCE JQ1948 !$#authors Kashiwazaki, S.; Minobe, Y.; Omura, T.; Hibino, H. !$#journal J. Gen. Virol. (1990) 71:2781-2790 !$#title Nucleotide sequence of barley yellow mosaic virus RNA 1: a !1close evolutionary relationship with potyviruses. !$#cross-references MUID:91108371; PMID:2273381 !$#accession JQ1948 !'##molecule_type genomic RNA !'##residues 1-2410 ##label KAS !'##cross-references DDBJ:D01091; NID:g221109; PIDN:BAA00875.1; !1PID:g221110 GENETICS !$#map_position segment 1 CLASSIFICATION #superfamily tobacco etch virus genome polyprotein KEYWORDS ATP; coat protein; nucleotide binding; !1nucleotidyltransferase; P-loop; polyprotein FEATURE !$1-2115 #product RNA-directed RNA polymerase #status !8predicted #label RRP\ !$487-494 #region nucleotide-binding motif A (P-loop)\ !$579-584 #region nucleotide-binding motif B\ !$583-586 #region DEAH motif\ !$2116-2410 #product coat protein #status predicted #label CPR SUMMARY #length 2410 #molecular-weight 270768 #checksum 9443 SEQUENCE /// ENTRY JQ1947 #type complete TITLE genome polyprotein 2 - barley yellow mosaic virus (isolate German) CONTAINS 70K protein; proteinase (EC 3.4.-.-) ORGANISM #formal_name barley yellow mosaic virus, BaYMV DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jun-2000 ACCESSIONS JQ1947 REFERENCE JQ1947 !$#authors Davidson, A.D.; Proels, M.; Schell, J.; Steinbiss, H.H. !$#journal J. Gen. Virol. (1991) 72:989-993 !$#title The nucleotide sequence of RNA 2 of barley yellow mosaic !1virus. !$#cross-references MUID:91202139; PMID:2016598 !$#accession JQ1947 !'##molecule_type genomic RNA !'##residues 1-890 ##label DAV !'##cross-references GB:D01099; NID:g221107; PIDN:BAA00884.1; !1PID:g221108 GENETICS !$#map_position segment 2 CLASSIFICATION #superfamily barley yellow mosaic virus genome polyprotein 2 KEYWORDS hydrolase; polyprotein; proteinase FEATURE !$1-255 #product proteinase #status predicted #label PRO\ !$256-890 #product 70K protein #status predicted #label PR2 SUMMARY #length 890 #molecular-weight 98202 #checksum 3547 SEQUENCE /// ENTRY VCVECV #type complete TITLE coat protein - carnation mottle virus ORGANISM #formal_name carnation mottle virus, CarMV DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 28-Jul-2000 ACCESSIONS A04209 REFERENCE A93590 !$#authors Guilley, H.; Carrington, J.C.; Balazs, E.; Jonard, G.; !1Richards, K.; Morris, T.J. !$#journal Nucleic Acids Res. (1985) 13:6663-6677 !$#title Nucleotide sequence and genome organization of carnation !1mottle virus RNA. !$#cross-references MUID:86041863; PMID:3840587 !$#accession A04209 !'##molecule_type genomic RNA !'##residues 1-348 ##label GUI !'##cross-references GB:X02986; NID:g62271; PIDN:CAA26728.1; !1PID:g4469341 CLASSIFICATION #superfamily carnation mottle virus coat protein KEYWORDS coat protein SUMMARY #length 348 #molecular-weight 37787 #checksum 5006 SEQUENCE /// ENTRY VCVGTB #type complete TITLE coat protein - tomato bushy stunt virus (strain cherry) ORGANISM #formal_name tomato bushy stunt virus, TBSV #note host Nicotiana clevelandii DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 23-Jul-1999 ACCESSIONS JA0114; A30826; B35315 REFERENCE A94392 !$#authors Hillman, B.I.; Hearne, P.; Rochon, D.; Morris, T.J. !$#journal Virology (1989) 169:42-50 !$#title Organization of tomato bushy stunt virus genome: !1characterization of the coat protein gene and the 3' !1terminus. !$#cross-references MUID:89163266; PMID:2922927 !$#accession JA0114 !'##molecule_type mRNA !'##residues 1-388 ##label HIL !'##cross-references GB:M21958; NID:g335172; PIDN:AAB02536.1; !1PID:g335175 CLASSIFICATION #superfamily carnation mottle virus coat protein KEYWORDS coat protein SUMMARY #length 388 #molecular-weight 41151 #checksum 180 SEQUENCE /// ENTRY VCVGAC #type complete TITLE coat protein - artichoke mottled crinkle virus ORGANISM #formal_name artichoke mottled crinkle virus DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 29-Oct-1999 ACCESSIONS S08428; S07548 REFERENCE S08428 !$#authors Grieco, P.; Gallitelli, D. !$#journal Nucleic Acids Res. (1990) 18:1300 !$#title Nucleotide sequence of the 3'-terminal region of artichoke !1mottled crinkle tombusvirus RNA. !$#cross-references MUID:90206806; PMID:2320427 !$#accession S08428 !'##status translation not shown !'##molecule_type genomic RNA !'##residues 1-388 ##label GRI !'##cross-references EMBL:X51456; NID:g59016; PIDN:CAA35821.1; !1PID:g59017 REFERENCE S07548 !$#authors Tavazza, M.; Lucioli, A.; Ancora, G.; Benvenuto, E. !$#journal Plant Mol. Biol. (1989) 13:685-692 !$#title cDNA cloning of artichoke mottled crinkle virus RNA and !1localization and sequencing of the coat protein gene. !$#cross-references MUID:91370852; PMID:2491684 !$#accession S07548 !'##molecule_type genomic RNA !'##residues 1-16,'T',18-81,83-148,'A',150-272,'L',274-279,'L',281-305, !1'FR',308-378,'R',380-384,'V',386-388 ##label TAV !'##cross-references EMBL:X16060 CLASSIFICATION #superfamily carnation mottle virus coat protein KEYWORDS coat protein SUMMARY #length 388 #molecular-weight 41206 #checksum 2198 SEQUENCE /// ENTRY A48355 #type complete TITLE coat protein - pelargonium leaf curl virus ORGANISM #formal_name pelargonium leaf curl virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 23-Jul-1999 ACCESSIONS A48355 REFERENCE A48355 !$#authors Li, Y.; Bachmann, S.; Maiss, E.; Commandeur, U.; Breyel, E.; !1Timpe, U.; Koenig, R. !$#journal Arch. Virol. (1993) 129:349-356 !$#title Nucleotide sequence of the coat protein gene of pelargonium !1leaf curl virus and comparison of the deduced coat protein !1amino acid sequence with those of other tombusviruses. !$#cross-references MUID:93228459; PMID:8470957 !$#accession A48355 !'##molecule_type genomic RNA !'##residues 1-389 ##label LI1 !'##cross-references GB:S58174; NID:g299096; PIDN:AAB26100.1; !1PID:g299097 !'##note sequence extracted from NCBI backbone (NCBIN:129117, !1NCBIP:129118) CLASSIFICATION #superfamily carnation mottle virus coat protein KEYWORDS coat protein; glycoprotein FEATURE !$8,9,117,118,139,353 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 389 #molecular-weight 41194 #checksum 4396 SEQUENCE /// ENTRY VCVGCN #type complete TITLE coat protein - cucumber necrosis virus ORGANISM #formal_name cucumber necrosis virus #note host Cucumis sativus (cucumber) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 23-Jul-1999 ACCESSIONS JA0131 REFERENCE A94391 !$#authors Rochon, D.M.; Tremaine, J.H. !$#journal Virology (1989) 169:251-259 !$#title Complete nucleotide sequence of the cucumber necrosis virus !1genome. !$#cross-references MUID:89204896; PMID:2705296 !$#accession JA0131 !'##molecule_type genomic RNA !'##residues 1-380 ##label ROC !'##cross-references GB:M25270; NID:g323338; PIDN:AAA42904.1; !1PID:g323341 COMMENT The genome is a single-stranded, positive-sense RNA. It !1codes for 33K, 92K, 40K, 21K, and 20K proteins. The 92K !1protein is a viral replicase, the 40K is a coat protein, and !1the 21K and 20K are core proteins. CLASSIFICATION #superfamily carnation mottle virus coat protein KEYWORDS coat protein SUMMARY #length 380 #molecular-weight 40878 #checksum 4508 SEQUENCE /// ENTRY VCVGCR #type complete TITLE coat protein - Cymbidium ringspot virus ORGANISM #formal_name Cymbidium ringspot virus DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 08-Apr-1994 ACCESSIONS JS0269 REFERENCE A92801 !$#authors Grieco, F.; Burgyan, J.; Russo, M. !$#journal J. Gen. Virol. (1989) 70:2533-2538 !$#title Nucleotide sequence of the 3'-terminal region of Cymbidium !1ringspot virus RNA. !$#cross-references MUID:89381709; PMID:2778443 !$#accession JS0269 !'##molecule_type genomic RNA !'##residues 1-380 ##label GRI COMMENT The genome is a single-stranded, positive-sense RNA. CLASSIFICATION #superfamily carnation mottle virus coat protein KEYWORDS coat protein SUMMARY #length 380 #molecular-weight 40580 #checksum 4759 SEQUENCE /// ENTRY VCVETC #type complete TITLE coat protein - turnip crinkle virus ORGANISM #formal_name turnip crinkle virus #note host Brassica rapa (turnip) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 23-Jul-1999 ACCESSIONS JA0111; S07285 REFERENCE A94394 !$#authors Carrington, J.C.; Heaton, L.A.; Zuidema, D.; Hillman, B.I.; !1Morris, T.J. !$#journal Virology (1989) 170:219-226 !$#title The genome structure of turnip crinkle virus. !$#cross-references MUID:89243179; PMID:2718381 !$#accession JA0111 !'##molecule_type genomic RNA !'##residues 1-351 ##label CAR1 REFERENCE S07285 !$#authors Carrington, J.C.; Morris, T.J.; Stockley, P.G.; Harrison, !1S.C. !$#journal J. Mol. Biol. (1987) 194:265-276 !$#title Structure and assembly of turnip crinkle virus. IV. Analysis !1of the coat protein gene and implications of the subunit !1primary structure. !$#cross-references MUID:87283926; PMID:3612806 !$#accession S07285 !'##molecule_type genomic RNA !'##residues 1-351 ##label CAR2 !'##cross-references EMBL:X05193; NID:g62114; PIDN:CAA28823.1; !1PID:g62115 !'##note the authors translated the codon TTG for residue 346 as Trp COMMENT The genome is a single-stranded, positive-sense RNA. CLASSIFICATION #superfamily carnation mottle virus coat protein KEYWORDS coat protein FEATURE !$1-56 #domain R #label DOR\ !$62-246 #domain S #label DOS\ !$249-351 #domain P #label DOP SUMMARY #length 351 #molecular-weight 38052 #checksum 1818 SEQUENCE /// ENTRY VCVEMN #type complete TITLE coat protein - melon necrotic spot virus ORGANISM #formal_name melon necrotic spot virus DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 21-Jul-2000 ACCESSIONS JQ0169 REFERENCE JQ0169 !$#authors Riviere, C.J.; Pot, J.; Tremaine, J.H.; Rochon, D.M. !$#journal J. Gen. Virol. (1989) 70:3033-3042 !$#title Coat protein of melon necrotic spot carmovirus is more !1similar to those of tombusviruses than those of !1carmoviruses. !$#cross-references MUID:90063551; PMID:2584953 !$#accession JQ0169 !'##molecule_type mRNA !'##residues 1-390 ##label RIV !'##cross-references GB:D00562; NID:g332140; PIDN:AAB02435.1; !1PID:g332146 CLASSIFICATION #superfamily carnation mottle virus coat protein KEYWORDS coat protein SUMMARY #length 390 #molecular-weight 41852 #checksum 821 SEQUENCE /// ENTRY C43684 #type complete TITLE capsid protein 37K - red clover necrotic mosaic virus (strain Australia) ORGANISM #formal_name red clover necrotic mosaic virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 20-Aug-1999 ACCESSIONS C43684; T10782 REFERENCE A43684 !$#authors Xiong, Z.; Lommel, S.A. !$#journal Virology (1989) 171:543-554 !$#title The complete nucleotide sequence and genome organization of !1red clover necrotic mosaic virus RNA-1. !$#cross-references MUID:89348013; PMID:2763465 !$#accession C43684 !'##molecule_type genomic RNA !'##residues 1-339 ##label XIO !'##cross-references GB:J04357; GB:M24621; NID:g333772; PIDN:AAB02542.1; !1PID:g333775 REFERENCE Z17138 !$#authors Xiong, Z.; Kim, K.H.; Kendall, T.L.; Lommel, S.A. !$#journal Virology (1993) 193:213-221 !$#title Synthesis of the putative red clover necrotic mosaic virus !1RNA polymerase by ribosomal frameshifting in vitro. !$#cross-references MUID:93174929; PMID:8438566 !$#accession T10782 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type genomic RNA !'##residues 1-339 ##label XI2 !'##cross-references EMBL:J04357; NID:g333772; PIDN:AAB02542.1; !1PID:g333775 GENETICS !$#map_position segment 1 CLASSIFICATION #superfamily carnation mottle virus coat protein KEYWORDS coat protein; glycoprotein FEATURE !$21,170,278 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 339 #molecular-weight 36582 #checksum 7292 SEQUENCE /// ENTRY WMVETC #type complete TITLE 8K protein - turnip crinkle virus ORGANISM #formal_name turnip crinkle virus #note host Brassica rapa (turnip) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 23-Jul-1999 ACCESSIONS JA0112 REFERENCE A94394 !$#authors Carrington, J.C.; Heaton, L.A.; Zuidema, D.; Hillman, B.I.; !1Morris, T.J. !$#journal Virology (1989) 170:219-226 !$#title The genome structure of turnip crinkle virus. !$#cross-references MUID:89243179; PMID:2718381 !$#accession JA0112 !'##molecule_type mRNA !'##residues 1-72 ##label CAR !'##cross-references GB:M22445; NID:g335192; PIDN:AAA96970.1; !1PID:g335195 COMMENT The genome is a single-stranded, positive-sense RNA. CLASSIFICATION #superfamily turnip crinkle virus 8K protein SUMMARY #length 72 #molecular-weight 7774 #checksum 4828 SEQUENCE /// ENTRY NKVGTB #type complete TITLE core protein p22 - tomato bushy stunt virus (strain cherry) ORGANISM #formal_name tomato bushy stunt virus, TBSV #note host Nicotiana clevelandii DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 23-Jul-1999 ACCESSIONS JA0115; C30826; C35315 REFERENCE A94392 !$#authors Hillman, B.I.; Hearne, P.; Rochon, D.; Morris, T.J. !$#journal Virology (1989) 169:42-50 !$#title Organization of tomato bushy stunt virus genome: !1characterization of the coat protein gene and the 3' !1terminus. !$#cross-references MUID:89163266; PMID:2922927 !$#accession JA0115 !'##molecule_type mRNA !'##residues 1-189 ##label HIL !'##cross-references GB:M21958; NID:g335172; PIDN:AAB02537.1; !1PID:g335176 CLASSIFICATION #superfamily tombusvirus core protein p22 KEYWORDS core protein SUMMARY #length 189 #molecular-weight 21608 #checksum 6866 SEQUENCE /// ENTRY NKVGAC #type complete TITLE core protein p21 - artichoke mottled crinkle virus ORGANISM #formal_name artichoke mottled crinkle virus DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 23-Jul-1999 ACCESSIONS S08429 REFERENCE S08428 !$#authors Grieco, P.; Gallitelli, D. !$#journal Nucleic Acids Res. (1990) 18:1300 !$#title Nucleotide sequence of the 3'-terminal region of artichoke !1mottled crinkle tombusvirus RNA. !$#cross-references MUID:90206806; PMID:2320427 !$#accession S08429 !'##status translation not shown !'##molecule_type genomic RNA !'##residues 1-189 ##label GRI !'##cross-references EMBL:X51456; NID:g59016; PIDN:CAA35822.1; !1PID:g59018 CLASSIFICATION #superfamily tombusvirus core protein p22 KEYWORDS core protein SUMMARY #length 189 #molecular-weight 21647 #checksum 6625 SEQUENCE /// ENTRY NKVGCN #type complete TITLE core protein p21 - cucumber necrosis virus ORGANISM #formal_name cucumber necrosis virus #note host Cucumis sativus (cucumber) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 23-Jul-1999 ACCESSIONS JA0132 REFERENCE A94391 !$#authors Rochon, D.M.; Tremaine, J.H. !$#journal Virology (1989) 169:251-259 !$#title Complete nucleotide sequence of the cucumber necrosis virus !1genome. !$#cross-references MUID:89204896; PMID:2705296 !$#accession JA0132 !'##molecule_type genomic RNA !'##residues 1-190 ##label ROC !'##cross-references GB:M25270; NID:g323338; PIDN:AAA42905.1; !1PID:g323342 COMMENT The genome is a single-stranded, positive-sense RNA. It !1codes for 33K, 92K, 40K, 21K, and 20K proteins. The 92K !1protein is a viral replicase, the 40K is a coat protein, and !1the 21K and 20K are core proteins. CLASSIFICATION #superfamily tombusvirus core protein p22 KEYWORDS core protein SUMMARY #length 190 #molecular-weight 21470 #checksum 7290 SEQUENCE /// ENTRY NKVGCR #type complete TITLE core protein p21 - Cymbidium ringspot virus ORGANISM #formal_name Cymbidium ringspot virus DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 08-Apr-1994 ACCESSIONS JS0270 REFERENCE A92801 !$#authors Grieco, F.; Burgyan, J.; Russo, M. !$#journal J. Gen. Virol. (1989) 70:2533-2538 !$#title Nucleotide sequence of the 3'-terminal region of Cymbidium !1ringspot virus RNA. !$#cross-references MUID:89381709; PMID:2778443 !$#accession JS0270 !'##molecule_type genomic RNA !'##residues 1-189 ##label GRI COMMENT The genome is a single-stranded, positive-sense RNA. CLASSIFICATION #superfamily tombusvirus core protein p22 KEYWORDS core protein SUMMARY #length 189 #molecular-weight 21309 #checksum 5568 SEQUENCE /// ENTRY NKVGD2 #type complete TITLE core protein p19 - Cymbidium ringspot virus ORGANISM #formal_name Cymbidium ringspot virus DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 21-Jul-2000 ACCESSIONS JS0271; S05459 REFERENCE A92801 !$#authors Grieco, F.; Burgyan, J.; Russo, M. !$#journal J. Gen. Virol. (1989) 70:2533-2538 !$#title Nucleotide sequence of the 3'-terminal region of Cymbidium !1ringspot virus RNA. !$#cross-references MUID:89381709; PMID:2778443 !$#accession JS0271 !'##molecule_type genomic RNA !'##residues 1-172 ##label GR1 REFERENCE JS0268 !$#authors Grieco, F.; Burgyan, J.; Russo, M. !$#journal Nucleic Acids Res. (1989) 17:6383 !$#title The nucleotide sequence of Cymbidium ringspot virus RNA. !$#cross-references MUID:89366663; PMID:2771646 !$#accession S05459 !'##status preliminary; translation not shown !'##molecule_type genomic RNA !'##residues 1-172 ##label GR2 !'##cross-references EMBL:X15511; NID:g59020; PIDN:CAA33535.1; !1PID:g4469164 COMMENT The genome is a single-stranded, positive-sense RNA. CLASSIFICATION #superfamily tombusvirus core protein p19 KEYWORDS core protein SUMMARY #length 172 #molecular-weight 19385 #checksum 8393 SEQUENCE /// ENTRY NKVGCU #type complete TITLE core protein p20 - cucumber necrosis virus ORGANISM #formal_name cucumber necrosis virus #note host Cucumis sativus (cucumber) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 23-Jul-1999 ACCESSIONS JA0133 REFERENCE A94391 !$#authors Rochon, D.M.; Tremaine, J.H. !$#journal Virology (1989) 169:251-259 !$#title Complete nucleotide sequence of the cucumber necrosis virus !1genome. !$#cross-references MUID:89204896; PMID:2705296 !$#accession JA0133 !'##molecule_type genomic RNA !'##residues 1-173 ##label ROC !'##cross-references GB:M25270; NID:g323338; PIDN:AAA42906.1; !1PID:g323343 COMMENT The genome is a single-stranded, positive-sense RNA. It !1codes for 33K, 92K, 40K, 21K, and 20K proteins. The 92K !1protein is a viral replicase, the 40K is a coat protein, and !1the 21K and 20K are core proteins. CLASSIFICATION #superfamily tombusvirus core protein p19 KEYWORDS core protein SUMMARY #length 173 #molecular-weight 19808 #checksum 9846 SEQUENCE /// ENTRY NKVGTD #type complete TITLE core protein p19 - tomato bushy stunt virus (strain cherry) ORGANISM #formal_name tomato bushy stunt virus, TBSV #note host Nicotiana clevelandii DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 23-Jul-1999 ACCESSIONS JA0116; B30826; D35315 REFERENCE A94392 !$#authors Hillman, B.I.; Hearne, P.; Rochon, D.; Morris, T.J. !$#journal Virology (1989) 169:42-50 !$#title Organization of tomato bushy stunt virus genome: !1characterization of the coat protein gene and the 3' !1terminus. !$#cross-references MUID:89163266; PMID:2922927 !$#accession JA0116 !'##molecule_type mRNA !'##residues 1-172 ##label HIL !'##cross-references GB:M21958; NID:g335172; PIDN:AAB02538.1; !1PID:g335177 CLASSIFICATION #superfamily tombusvirus core protein p19 KEYWORDS core protein SUMMARY #length 172 #molecular-weight 19395 #checksum 9943 SEQUENCE /// ENTRY NKVGBC #type complete TITLE core protein p19 - artichoke mottled crinkle virus ORGANISM #formal_name artichoke mottled crinkle virus DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 23-Jul-1999 ACCESSIONS S08430 REFERENCE S08428 !$#authors Grieco, P.; Gallitelli, D. !$#journal Nucleic Acids Res. (1990) 18:1300 !$#title Nucleotide sequence of the 3'-terminal region of artichoke !1mottled crinkle tombusvirus RNA. !$#cross-references MUID:90206806; PMID:2320427 !$#accession S08430 !'##status translation not shown !'##molecule_type genomic RNA !'##residues 1-172 ##label GRI !'##cross-references EMBL:X51456; NID:g59016; PIDN:CAA35823.1; !1PID:g59019 CLASSIFICATION #superfamily tombusvirus core protein p19 KEYWORDS core protein SUMMARY #length 172 #molecular-weight 19280 #checksum 9745 SEQUENCE /// ENTRY GNWEC #type complete TITLE genome polyprotein M - cowpea aphid-borne mosaic virus CONTAINS coat protein VP23; coat protein VP37 ORGANISM #formal_name cowpea aphid-borne mosaic virus, CABMV DATE 18-Apr-1984 #sequence_revision 18-Apr-1984 #text_change 23-Jul-1999 ACCESSIONS A04210 REFERENCE A04210 !$#authors van Wezenbeek, P.; Verver, J.; Harmsen, J.; Vos, P.; van !1Kammen, A. !$#journal EMBO J. (1983) 2:941-946 !$#title Primary structure and gene organization of the !1middle-component RNA of cowpea mosaic virus. !$#cross-references MUID:84057775; PMID:6641721 !$#accession A04210 !'##molecule_type genomic RNA !'##residues 1-1046 ##label VAN !'##cross-references GB:X00729; NID:g58910; PIDN:CAA25314.1; PID:g58911 CLASSIFICATION #superfamily cowpea aphid-borne mosaic virus genome !1polyprotein M KEYWORDS polyprotein FEATURE !$460-833 #product coat protein VP37 #status predicted #label !8P37\ !$834-1046 #product coat protein VP23 #status predicted #label !8P23 SUMMARY #length 1046 #molecular-weight 116217 #checksum 3998 SEQUENCE /// ENTRY GNWXG7 #type complete TITLE genome polyprotein M - bean pod mottle virus (strain Kentucky G7) CONTAINS coat protein VP23; coat protein VP37 ORGANISM #formal_name bean pod mottle virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 23-Jul-1999 ACCESSIONS A40321 REFERENCE A40321 !$#authors MacFarlane, S.A.; Shanks, M.; Davies, J.W.; Zlotnick, A.; !1Lomonossoff, G.P. !$#journal Virology (1991) 183:405-409 !$#title Analysis of the nucleotide sequence of bean pod mottle virus !1middle component RNA. !$#cross-references MUID:91272504; PMID:2053290 !$#accession A40321 !'##molecule_type genomic RNA !'##residues 1-1018 ##label MAC !'##cross-references GB:M62738; NID:g210811; PIDN:AAA42801.1; !1PID:g210812 COMMENT The genomic RNA is present in the M particle. CLASSIFICATION #superfamily cowpea aphid-borne mosaic virus genome !1polyprotein M KEYWORDS coat protein; glycoprotein; polyprotein FEATURE !$447-820 #product coat protein VP37 #status predicted #label !8VP1\ !$821-1018 #product coat protein VP23 #status predicted #label !8VP2\ !$70,182,374,539,919, !$961 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1018 #molecular-weight 113351 #checksum 8882 SEQUENCE /// ENTRY GNWXCS #type complete TITLE genome polyprotein M - cowpea severe mosaic virus (strain DG) CONTAINS coat protein VP23; coat protein VP37 ORGANISM #formal_name cowpea severe mosaic virus #note host Vigna unquiculata (cowpea) DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 08-Apr-1994 ACCESSIONS A42454; B42454 REFERENCE A42454 !$#authors Chen, X.; Bruening, G. !$#journal Virology (1992) 187:682-692 !$#title Nucleotide sequence and genetic map of cowpea severe mosaic !1virus RNA 2 and comparisons with RNA 2 of other comoviruses. !$#cross-references MUID:92188543; PMID:1546463 !$#accession A42454 !'##molecule_type genomic RNA !'##residues 1-1002 ##label CH1 !'##cross-references GB:M83309 !$#accession B42454 !'##molecule_type protein !'##residues 434-449 ##label CH2 GENETICS !$#map_position segment 2 CLASSIFICATION #superfamily cowpea aphid-borne mosaic virus genome !1polyprotein M KEYWORDS coat protein; glycoprotein; membrane protein; polyprotein FEATURE !$70-86 #region hydrophobic\ !$434-807 #product coat protein VP37 #status predicted #label !8CP1\ !$808-1002 #product coat protein VP23 #status predicted #label !8CP2\ !$125,692,945 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1002 #molecular-weight 112108 #checksum 1899 SEQUENCE /// ENTRY A48356 #type complete TITLE genome polyprotein M - squash mosaic virus (strain melon) CONTAINS 22K coat protein; 42K coat protein ORGANISM #formal_name squash mosaic virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 10-Mar-1994 ACCESSIONS A48356; B48356 REFERENCE A48356 !$#authors Hu, J.S.; Pang, S.Z.; Nagpala, P.G.; Siemieniak, D.R.; !1Slightom, J.L.; Gonsalves, D. !$#journal Arch. Virol. (1993) 130:17-31 !$#title The coat protein genes of squash mosaic virus: cloning, !1sequence analysis, and expression in tobacco protoplasts. !$#cross-references MUID:93277375; PMID:8503782 !$#accession A48356 !'##molecule_type genomic RNA !'##residues 1-790 ##label HU1 !'##note sequence extracted from NCBI backbone (NCBIN:132678, !1NCBIP:132679) !$#accession B48356 !'##molecule_type protein !'##residues 357-381;606-616 ##label HU2 GENETICS !$#map_position segment 2 CLASSIFICATION #superfamily cowpea aphid-borne mosaic virus genome !1polyprotein M KEYWORDS coat protein; glycoprotein; polyprotein FEATURE !$233-606 #product 42K coat protein #status predicted #label !8CP1\ !$607-790 #product 22K coat protein #status predicted #label !8CP2\ !$183,187,205,655, !$704,742 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 790 #molecular-weight 86938 #checksum 998 SEQUENCE /// ENTRY GNWE2C #type complete TITLE genome polyprotein B - cowpea aphid-borne mosaic virus CONTAINS 24K viral proteinase (EC 3.4.22.-); 32K proteinase cofactor; 58K membrane-binding protein; genome-linked protein VPg; RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name cowpea aphid-borne mosaic virus, CABMV DATE 18-Apr-1984 #sequence_revision 18-Apr-1984 #text_change 31-Mar-2000 ACCESSIONS A04211 REFERENCE A04211 !$#authors Lomonossoff, G.P.; Shanks, M. !$#journal EMBO J. (1983) 2:2253-2258 !$#title The nucleotide sequence of cowpea mosaic virus B RNA. !$#accession A04211 !'##molecule_type genomic RNA !'##residues 1-1866 ##label LOM !'##note the polyprotein is cleaved to give at least eight mature !1proteins; however, the exact cleavage sites are unknown !'##note the authors translated the codon AAU for residue 630 as Asp, !1GAG for 844 as Gly, and CAA for 857 as Asn CLASSIFICATION #superfamily cowpea aphid-borne mosaic virus genome !1polyprotein B KEYWORDS cysteine proteinase; genome-linked protein; hydrolase; !1membrane protein; nucleotidyltransferase; polyprotein FEATURE !$2-326 #product 32K proteinase cofactor #status predicted !8#label PCF\ !$327-919 #product 58K membrane-binding protein #status !8predicted #label MBP\ !$920-947 #product genome-linked protein VPg #status predicted !8#label VPG\ !$948-1155 #product 24K viral proteinase #status predicted !8#label VPT\ !$1156-1866 #product RNA-directed RNA polymerase #status !8predicted #label RRP SUMMARY #length 1866 #molecular-weight 209809 #checksum 2223 SEQUENCE /// ENTRY JQ1657 #type complete TITLE genome polyprotein B - red clover mottle virus (strain S) CONTAINS 24K viral proteinase; 32K proteinase cofactor; 58K membrane-binding protein; RNA-directed RNA polymerase (EC 2.7.7.48); VPg protein ORGANISM #formal_name red clover mottle virus DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jun-2000 ACCESSIONS JQ1657; JQ0572; S19926 REFERENCE JQ1657 !$#authors Shanks, M.; Lomonossoff, G.P. !$#journal J. Gen. Virol. (1992) 73:2473-2477 !$#title The nucleotide sequence of red clover mottle virus bottom !1component RNA. !$#cross-references MUID:93019077; PMID:1402822 !$#accession JQ1657 !'##molecule_type genomic RNA !'##residues 1-1864 ##label SHA !'##cross-references EMBL:X64886; NID:g61463; PIDN:CAA46104.1; !1PID:g61464 REFERENCE JQ0572 !$#authors Shanks, M.; Lomonossoff, G.P. !$#journal J. Gen. Virol. (1990) 71:735-738 !$#title The primary structure of the 24K protease from red clover !1mottle virus: implications for the mode of action of !1comovirus proteases. !$#cross-references MUID:90188322; PMID:2179468 !$#accession JQ0572 !'##molecule_type genomic RNA !'##residues 912-1167 ##label SH2 !'##cross-references GB:D00657; NID:g222473; PIDN:BAA00547.1; !1PID:g222474 GENETICS !$#map_position segment B CLASSIFICATION #superfamily cowpea aphid-borne mosaic virus genome !1polyprotein B KEYWORDS genome-linked protein; hydrolase; membrane protein; !1nucleotidyltransferase; polyprotein; proteinase FEATURE !$2-315 #product 32K proteinase cofactor #status predicted !8#label PCF\ !$316-915 #product 58K membrane-binding protein #status !8predicted #label MBP\ !$916-943 #product genome-linked protein VPg #status predicted !8#label VPG\ !$944-1151 #product 24K viral proteinase #status predicted !8#label VPT\ !$1152-1864 #product RNA-directed RNA polymerase #status !8predicted #label RRP SUMMARY #length 1864 #molecular-weight 210254 #checksum 268 SEQUENCE /// ENTRY GNVVTB #type complete TITLE genome polyprotein 1 - tomato black ring virus (strain S) CONTAINS 2.3K genome-linked protein; 23 K proteinase (EC 3.4.-.-); 63K protein; 72K protein; RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name tomato black ring virus #note host Nicotiana clevelandii (tobacco) DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 26-Apr-1996 ACCESSIONS JQ0009 REFERENCE JQ0009 !$#authors Greif, C.; Hemmer, O.; Fritsch, C. !$#journal J. Gen. Virol. (1988) 69:1517-1529 !$#title Nucleotide sequence of tomato black ring virus RNA-1. !$#accession JQ0009 !'##molecule_type mRNA !'##residues 1-2264 ##label GRE COMMENT The genome consists of two single-stranded RNAs, called !1RNA-1 and RNA-2. CLASSIFICATION #superfamily cowpea aphid-borne mosaic virus genome !1polyprotein B KEYWORDS genome-linked protein; hydrolase; membrane protein; !1nucleotidyltransferase; polyprotein; proteinase FEATURE !$1-565 #product 63K protein #status predicted #label PRH\ !$566-1212 #product 72K protein #status predicted #label ATP\ !$1213-1232 #product 2.3K genome-linked protein #status predicted !8#label GLP\ !$1233-1440 #product 23K proteinase #status predicted #label PTH\ !$1441-2264 #product RNA-directed RNA polymerase #status !8predicted #label POH SUMMARY #length 2264 #molecular-weight 253676 #checksum 5425 SEQUENCE /// ENTRY GNVVGV #type complete TITLE genome polyprotein - grapevine fanleaf virus CONTAINS 63K protein; 72K protein; genome-linked protein; proteinase (EC 3.4.-.-); RNA-directed RNA polymerase (EC 2.7.7.48) ORGANISM #formal_name grapevine fanleaf virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jun-2000 ACCESSIONS JQ1373; S15873 REFERENCE JQ1373 !$#authors Ritzenthaler, C.; Viry, M.; Pinck, M.; Margis, R.; Fuchs, !1M.; Pinck, L. !$#journal J. Gen. Virol. (1991) 72:2357-2365 !$#title Complete nucleotide sequence and genetic organization of !1grapevine fanleaf nepovirus RNA1. !$#cross-references MUID:92013951; PMID:1655953 !$#accession JQ1373 !'##molecule_type genomic RNA !'##residues 1-2284 ##label RIT !'##cross-references DDBJ:D00915; NID:g221421; PIDN:BAA00761.1; !1PID:g221422 REFERENCE S15873 !$#authors Pinck, M.; Reinbolt, J.; Loudes, A.M.; le Ret, M.; Pinck, L. !$#journal FEBS Lett. (1991) 284:117-119 !$#title Primary structure and location of the genome-linked protein !1(VPg) of grapevine fanleaf nepovirus. !$#cross-references MUID:91285092; PMID:2060618 !$#accession S15873 !'##molecule_type protein !'##residues 1218-1241 ##label PIN GENETICS !$#map_position segment 1 CLASSIFICATION #superfamily cowpea aphid-borne mosaic virus genome !1polyprotein B KEYWORDS genome-linked protein; hydrolase; membrane protein; !1nucleotidyltransferase; phosphoprotein; polyprotein; !1proteinase FEATURE !$1-568 #product 63K protein #status predicted #label STK\ !$569-1217 #product 72K protein #status predicted #label SKP\ !$1218-1241 #product genome-linked protein #status experimental !8#label GLP\ !$1242-1460 #product proteinase #status predicted #label TKP\ !$1461-2284 #product RNA-directed RNA polymerase #status !8predicted #label RRP\ !$1218 #binding_site phosphoryl-RNA (Ser) (covalent) #status !8experimental SUMMARY #length 2284 #molecular-weight 252930 #checksum 8511 SEQUENCE /// ENTRY A44214 #type complete TITLE genome polyprotein 1 - cowpea severe mosaic virus CONTAINS 24K protein; 32K protein; 58K membrane-binding protein; RNA-directed RNA polymerase (EC 2.7.7.48); VPg protein ORGANISM #formal_name cowpea severe mosaic virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 31-Dec-1996 ACCESSIONS A44214 REFERENCE A44214 !$#authors Chen, X.; Bruening, G. !$#journal Virology (1992) 191:607-618 !$#title Cloned DNA copies of cowpea severe mosaic virus genomic !1RNAs: infectious transcripts and complete nucleotide !1sequence of RNA 1. !$#cross-references MUID:93079863; PMID:1448917 !$#accession A44214 !'##molecule_type genomic RNA !'##residues 1-1858 ##label CHE !'##cross-references GB:M83830 GENETICS !$#map_position segment 1 CLASSIFICATION #superfamily cowpea aphid-borne mosaic virus genome !1polyprotein B KEYWORDS genome-linked protein; glycoprotein; hydrolase; !1nucleotidyltransferase; polyprotein; proteinase; !1transmembrane protein FEATURE !$2-313 #product 32K proteinase cofactor #status predicted !8#label PCF\ !$218-235 #region hydrophobic\ !$314-908 #product 58K membrane-binding protein #status !8predicted #label MBP\ !$891-907 #domain transmembrane #status predicted #label TMN\ !$909-936 #product genome-linked protein VPg #status predicted !8#label VPG\ !$937-1146 #product 24K viral proteinase #status predicted !8#label VPT\ !$1147-1858 #product RNA-directed RNA polymerase #status !8predicted #label RRP\ !$1811-1826 #region hydrophobic\ !$326,958,1744,1758 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1858 #molecular-weight 208861 #checksum 3636 SEQUENCE /// ENTRY A46112 #type complete TITLE genome polyprotein - rice tungro spherical virus (strain Los Banos) ORGANISM #formal_name rice tungro spherical virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 31-Dec-1996 ACCESSIONS A46112 REFERENCE A46112 !$#authors Shen, P.; Kaniewska, M.; Smith, C.; Beachy, R.N. !$#journal Virology (1993) 193:621-630 !$#title Nucleotide sequence and genomic organization of rice tungro !1spherical virus. !$#cross-references MUID:93212494; PMID:8460478 !$#accession A46112 !'##molecule_type genomic RNA !'##residues 1-3473 ##label SHE !'##cross-references GB:S57835 CLASSIFICATION #superfamily rice tungro spherical virus genome polyprotein KEYWORDS glycoprotein; polyprotein FEATURE !$106,367,903,1018, !$1274,1311,1385, !$1665,1755,2291,2779 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 3473 #molecular-weight 390260 #checksum 8842 SEQUENCE /// ENTRY GNVVTR #type complete TITLE genome polyprotein 2 - tomato ringspot virus (strain raspberry) CONTAINS coat protein ORGANISM #formal_name tomato ringspot virus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jun-2000 ACCESSIONS JQ1093 REFERENCE JQ1093 !$#authors Rott, M.E.; Tremaine, J.H.; Rochon, D.M. !$#journal J. Gen. Virol. (1991) 72:1505-1514 !$#title Nucleotide sequence of tomato ringspot virus RNA-2. !$#cross-references MUID:91311402; PMID:1856689 !$#accession JQ1093 !'##molecule_type genomic RNA !'##residues 1-1882 ##label ROT !'##cross-references GB:D12477; GB:D01129; NID:g222674; PIDN:BAA02043.1; !1PID:g222675 !'##note it is uncertain whether Met-1 or Met-122 is the initiator GENETICS !$#map_position segment 2 CLASSIFICATION #superfamily tomato ringspot virus genome polyprotein KEYWORDS coat protein; glycoprotein; polyprotein FEATURE !$1321-1882 #product coat protein #status predicted #label MAT\ !$269,295,1183,1316, !$1543,1561,1735 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1882 #molecular-weight 206801 #checksum 3855 SEQUENCE /// ENTRY GNVVSR #type fragment TITLE genome polyprotein 1 - tomato ringspot virus (strain raspberry) (fragment) ORGANISM #formal_name tomato ringspot virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 23-Jul-1999 ACCESSIONS A40787 REFERENCE A40787 !$#authors Rott, M.E.; Tremaine, J.H.; Rochon, D.M. !$#journal Virology (1991) 185:468-472 !$#title Comparison of the 5' and 3' termini of tomato ringspot virus !1RNA1 and RNA2: evidence for RNA recombination. !$#cross-references MUID:92024112; PMID:1926788 !$#accession A40787 !'##molecule_type genomic RNA !'##residues 1-354 ##label ROT !'##cross-references GB:M73822; NID:g335267; PIDN:AAA47941.1; !1PID:g555406 GENETICS !$#map_position segment 1 CLASSIFICATION #superfamily tomato ringspot virus genome polyprotein KEYWORDS glycoprotein; polyprotein FEATURE !$270 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 354 #checksum 9843 SEQUENCE /// ENTRY JQ1658 #type complete TITLE genome polyprotein 2 - raspberry ringspot virus (strain S) CONTAINS 66K protein; coat protein ORGANISM #formal_name raspberry ringspot virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 23-Jul-1999 ACCESSIONS JQ1658; PQ0439 REFERENCE JQ1658 !$#authors Blok, V.C.; Wardell, J.; Jolly, C.A.; Manoukian, A.; !1Robinson, D.J.; Edwards, M.L.; Mayo, M.A. !$#journal J. Gen. Virol. (1992) 73:2189-2194 !$#title The nucleotide sequence of RNA-2 of raspberry ringspot !1nepovirus. !$#cross-references MUID:93019039; PMID:1402811 !$#accession JQ1658 !'##molecule_type genomic RNA !'##residues 1-1107 ##label BL1 !'##cross-references GB:S46011; NID:g257077; PIDN:AAB23551.1; !1PID:g257078 !$#accession PQ0439 !'##molecule_type protein !'##residues 594-604 ##label BL2 GENETICS !$#map_position segment 2 CLASSIFICATION #superfamily raspberry ringspot virus genome polyprotein KEYWORDS coat protein; polyprotein FEATURE !$1-593 #product 66K protein #status predicted #label MA1\ !$594-1107 #product coat protein #status predicted #label MA2 SUMMARY #length 1107 #molecular-weight 123508 #checksum 6822 SEQUENCE /// ENTRY SAVVTL #type complete TITLE satellite RNA-encoded 48K protein - tomato black ring virus (strain L) ORGANISM #formal_name tomato black ring virus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 08-Apr-1994 ACCESSIONS A27169 REFERENCE A27169 !$#authors Hemmer, O.; Meyer, M.; Greif, C.; Fritsch, C. !$#journal J. Gen. Virol. (1987) 68:1823-1833 !$#title Comparison of the nucleotide sequences of five tomato black !1ring virus satellite RNAs. !$#accession A27169 !'##molecule_type genomic RNA !'##residues 1-425 ##label HEM !'##cross-references EMBL:X05687 GENETICS !$#map_position segment RNA3 CLASSIFICATION #superfamily tomato black ring virus satellite RNA-encoded !148K protein SUMMARY #length 425 #molecular-weight 47907 #checksum 6317 SEQUENCE /// ENTRY SAVVTE #type complete TITLE satellite RNA-encoded 48K protein - tomato black ring virus (strain E) ORGANISM #formal_name tomato black ring virus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 08-Apr-1994 ACCESSIONS B27169 REFERENCE A27169 !$#authors Hemmer, O.; Meyer, M.; Greif, C.; Fritsch, C. !$#journal J. Gen. Virol. (1987) 68:1823-1833 !$#title Comparison of the nucleotide sequences of five tomato black !1ring virus satellite RNAs. !$#accession B27169 !'##molecule_type genomic RNA !'##residues 1-420 ##label HEM !'##cross-references EMBL:X05687 GENETICS !$#map_position segment RNA3 CLASSIFICATION #superfamily tomato black ring virus satellite RNA-encoded !148K protein SUMMARY #length 420 #molecular-weight 47955 #checksum 2980 SEQUENCE /// ENTRY SAVVTC #type complete TITLE satellite RNA-encoded 48K protein - tomato black ring virus (strain C) ORGANISM #formal_name tomato black ring virus DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 08-Apr-1994 ACCESSIONS C27169 REFERENCE A27169 !$#authors Hemmer, O.; Meyer, M.; Greif, C.; Fritsch, C. !$#journal J. Gen. Virol. (1987) 68:1823-1833 !$#title Comparison of the nucleotide sequences of five tomato black !1ring virus satellite RNAs. !$#accession C27169 !'##molecule_type genomic RNA !'##residues 1-421 ##label HEM !'##cross-references EMBL:X05687 GENETICS !$#map_position segment RNA3 CLASSIFICATION #superfamily tomato black ring virus satellite RNA-encoded !148K protein SUMMARY #length 421 #molecular-weight 47990 #checksum 6919 SEQUENCE /// ENTRY VCBVC #type complete TITLE coat protein - cowpea chlorotic mottle virus ORGANISM #formal_name cowpea chlorotic mottle virus DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 23-Jul-1999 ACCESSIONS A04212; JU0119 REFERENCE A04212 !$#authors Dasgupta, R.; Kaesberg, P. !$#journal Nucleic Acids Res. (1982) 10:703-713 !$#title Complete nucleotide sequences of the coat protein messenger !1RNAs of brome mosaic virus and cowpea chlorotic mottle !1virus. !$#cross-references MUID:82150226; PMID:6895941 !$#accession A04212 !'##molecule_type genomic RNA !'##residues 1-190 ##label DAS !'##cross-references GB:J02052; NID:g331602; PIDN:AAA46370.1; !1PID:g331603 REFERENCE JU0117 !$#authors Allison, R.F.; Janda, M.; Ahlquist, P. !$#journal Virology (1989) 172:321-330 !$#title Sequence of cowpea chlorotic mottle virus RNAs 2 and 3 and !1evidence of a recombination event during bromovirus !1evolution. !$#cross-references MUID:89370316; PMID:2773323 !$#accession JU0119 !'##molecule_type genomic RNA !'##residues 1-150,'T',152-190 ##label ALL !'##cross-references GB:M28818; NID:g331607; PIDN:AAA46373.1; !1PID:g331609 GENETICS !$#map_position segment 3 CLASSIFICATION #superfamily brome mosaic virus coat protein KEYWORDS coat protein; RNA binding FEATURE !$10-23 #region arginine-rich RNA-binding pattern SUMMARY #length 190 #molecular-weight 20313 #checksum 8914 SEQUENCE /// ENTRY VCBVM #type complete TITLE coat protein - brome mosaic virus ORGANISM #formal_name brome mosaic virus, BMV DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 24-Sep-1999 ACCESSIONS A04213 REFERENCE A92875 !$#authors Ahlquist, P.; Luckow, V.; Kaesberg, P. !$#journal J. Mol. Biol. (1981) 153:23-38 !$#title Complete nucleotide sequence of brome mosaic virus RNA3. !$#cross-references MUID:82170464; PMID:7338913 !$#accession A04213 !'##molecule_type mRNA !'##residues 1-189 ##label AHL !'##cross-references GB:V00099; GB:J02042; GB:J02043; NID:g58732; !1PIDN:CAA23435.1; PID:g58734 CLASSIFICATION #superfamily brome mosaic virus coat protein KEYWORDS RNA binding FEATURE !$10-23 #region arginine-rich RNA-binding pattern SUMMARY #length 189 #molecular-weight 20384 #checksum 9337 SEQUENCE /// ENTRY VCWMBB #type complete TITLE coat protein - broad bean mottle virus ORGANISM #formal_name broad bean mottle virus DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 08-Apr-1994 ACCESSIONS C42453 REFERENCE A42453 !$#authors Romero, J.; Dzianott, A.M.; Bujarski, J.J. !$#journal Virology (1992) 187:671-681 !$#title The nucleotide sequence and genome organization of the RNA2 !1and RNA3 segments in broad bean mottle virus. !$#cross-references MUID:92188542; PMID:1546462 !$#accession C42453 !'##molecule_type genomic RNA !'##residues 1-188 ##label ROM !'##cross-references GB:M64713 GENETICS !$#map_position segment 3 CLASSIFICATION #superfamily brome mosaic virus coat protein KEYWORDS coat protein SUMMARY #length 188 #molecular-weight 20526 #checksum 2304 SEQUENCE /// ENTRY P3BVAM #type complete TITLE 3a protein - brome mosaic virus ORGANISM #formal_name brome mosaic virus, BMV DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 24-Sep-1999 ACCESSIONS A04214 REFERENCE A92875 !$#authors Ahlquist, P.; Luckow, V.; Kaesberg, P. !$#journal J. Mol. Biol. (1981) 153:23-38 !$#title Complete nucleotide sequence of brome mosaic virus RNA3. !$#cross-references MUID:82170464; PMID:7338913 !$#accession A04214 !'##molecule_type mRNA !'##residues 1-303 ##label AHL !'##cross-references GB:V00099; GB:J02042; GB:J02043; NID:g58732; !1PIDN:CAA23434.1; PID:g58733 !'##note this protein is coded by a portion of the viral genomic RNA 3 CLASSIFICATION #superfamily brome mosaic virus 3a protein SUMMARY #length 303 #molecular-weight 32482 #checksum 4656 SEQUENCE /// ENTRY P3WMCC #type complete TITLE 3a protein - cowpea chlorotic mottle virus ORGANISM #formal_name cowpea chlorotic mottle virus DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 23-Jul-1999 ACCESSIONS JU0118 REFERENCE JU0117 !$#authors Allison, R.F.; Janda, M.; Ahlquist, P. !$#journal Virology (1989) 172:321-330 !$#title Sequence of cowpea chlorotic mottle virus RNAs 2 and 3 and !1evidence of a recombination event during bromovirus !1evolution. !$#cross-references MUID:89370316; PMID:2773323 !$#accession JU0118 !'##molecule_type genomic RNA !'##residues 1-302 ##label ALL !'##cross-references GB:M28818; NID:g331607; PIDN:AAA46372.1; !1PID:g331608 GENETICS !$#map_position segment 3 CLASSIFICATION #superfamily brome mosaic virus 3a protein KEYWORDS nonstructural protein SUMMARY #length 302 #molecular-weight 33363 #checksum 237 SEQUENCE /// ENTRY P3WMBB #type complete TITLE 3a protein - broad bean mottle virus ORGANISM #formal_name broad bean mottle virus DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 08-Apr-1994 ACCESSIONS B42453 REFERENCE A42453 !$#authors Romero, J.; Dzianott, A.M.; Bujarski, J.J. !$#journal Virology (1992) 187:671-681 !$#title The nucleotide sequence and genome organization of the RNA2 !1and RNA3 segments in broad bean mottle virus. !$#cross-references MUID:92188542; PMID:1546462 !$#accession B42453 !'##molecule_type genomic RNA !'##residues 1-295 ##label ROM !'##cross-references GB:M64713 GENETICS !$#map_position segment 3 CLASSIFICATION #superfamily brome mosaic virus 3a protein KEYWORDS nonstructural protein SUMMARY #length 295 #molecular-weight 32597 #checksum 9327 SEQUENCE /// ENTRY P3VXUV #type complete TITLE 3a protein - cucumber mosaic virus (strain Q) ORGANISM #formal_name cucumber mosaic virus, CMV #note host Cucumis sativus (cucumber) DATE 05-Apr-1983 #sequence_revision 30-Jun-1990 #text_change 23-Jul-1999 ACCESSIONS JA0107; A04215 REFERENCE JA0107 !$#authors Davies, C.; Symons, R.H. !$#journal Virology (1988) 165:216-224 !$#title Further implications for the evolutionary relationships !1between tripartite plant viruses based on cucumber mosaic !1virus RNA 3. !$#cross-references MUID:88265861; PMID:3388769 !$#accession JA0107 !'##molecule_type mRNA !'##residues 1-279 ##label DAV !'##cross-references GB:M21464; NID:g331707; PIDN:AAA46415.1; !1PID:g331708 COMMENT The genome consists of three single-stranded, positive RNAs, !1designated RNA1, RNA2, and RNA3. GENETICS !$#map_position segment RNA3 CLASSIFICATION #superfamily brome mosaic virus 3a protein SUMMARY #length 279 #molecular-weight 30348 #checksum 8651 SEQUENCE /// ENTRY A46111 #type complete TITLE 3a protein - cucumber mosaic virus ORGANISM #formal_name cucumber mosaic virus, CMV #note host Cucumis sativus (cucumber) DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 23-Jul-1999 ACCESSIONS A46111; S22094 REFERENCE A46111 !$#authors Boccard, F.; Baulcombe, D. !$#journal Virology (1993) 193:563-578 !$#title Mutational analysis of Cis-acting sequences and gene !1function in RNA3 of cucumber mosaic virus. !$#cross-references MUID:93212489; PMID:8460476 !$#accession A46111 !'##molecule_type genomic RNA !'##residues 1-279 ##label BOC !'##cross-references GB:Z12818; GB:S57834; NID:g58893; PIDN:CAA78278.1; !1PID:g58894 !'##experimental_source strain Kin REFERENCE S22094 !$#authors Baulcombe, D. !$#submission submitted to the EMBL Data Library, June 1992 !$#description Mutational analysis of CMV RNA3: Effects on RNA3 !1accumulation, RNA4 synthesis and plant infection. !$#accession S22094 !'##status preliminary !'##molecule_type DNA !'##residues 1-279 ##label BAU !'##cross-references EMBL:Z12818; NID:g58893; PIDN:CAA78278.1; !1PID:g58894 GENETICS !$#map_position segment RNA3 CLASSIFICATION #superfamily brome mosaic virus 3a protein SUMMARY #length 279 #molecular-weight 30288 #checksum 8450 SEQUENCE /// ENTRY P3VXY1 #type complete TITLE 3a protein - cucumber mosaic virus (strain Y) ORGANISM #formal_name cucumber mosaic virus, CMV #note host Nicotiana tabacum cv. Xanthi nc (tobacco) DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 08-Apr-1994 ACCESSIONS JA0096 REFERENCE JA0096 !$#authors Nitta, N.; Masuta, C.; Kuwata, S.; Takanami, Y. !$#journal Ann. Phytopathol. Soc. Jpn. (1989) 54:516-522 !$#title Comparative studies on the nucleotide sequence of cucumber !1mosaic virus RNA3 between Y strain and Q strain. !$#accession JA0096 !'##molecule_type mRNA !'##residues 1-279 ##label NIT COMMENT The genome consists of three single-stranded, positive RNAs, !1designated RNA1, RNA2, and RNA3. GENETICS !$#map_position segment RNA3 CLASSIFICATION #superfamily brome mosaic virus 3a protein SUMMARY #length 279 #molecular-weight 30475 #checksum 8109 SEQUENCE /// ENTRY P3VXPS #type complete TITLE 3a protein - peanut stunt virus (strain J) ORGANISM #formal_name peanut stunt virus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jun-2000 ACCESSIONS A40786; JQ0604 REFERENCE A40786 !$#authors Karasawa, A.; Nakaho, K.; Kakutani, T.; Minobe, Y.; Ehara, !1Y. !$#journal Virology (1991) 185:464-467 !$#title Nucleotide sequence of RNA 3 of peanut stunt cucumovirus. !$#cross-references MUID:92024111; PMID:1926787 !$#accession A40786 !'##molecule_type genomic RNA !'##residues 1-288 ##label KAR !'##cross-references GB:D00668; NID:g222421; PIDN:BAA00571.1; !1PID:g222422 GENETICS !$#map_position segment 3 CLASSIFICATION #superfamily brome mosaic virus 3a protein KEYWORDS nonstructural protein SUMMARY #length 288 #molecular-weight 31418 #checksum 4910 SEQUENCE /// ENTRY VCVXUV #type complete TITLE coat protein - cucumber mosaic virus (strain Q) ORGANISM #formal_name cucumber mosaic virus, CMV #note host Cucumis sativus (cucumber) DATE 05-Apr-1983 #sequence_revision 30-Jun-1990 #text_change 23-Jul-1999 ACCESSIONS JA0108; A04216 REFERENCE JA0107 !$#authors Davies, C.; Symons, R.H. !$#journal Virology (1988) 165:216-224 !$#title Further implications for the evolutionary relationships !1between tripartite plant viruses based on cucumber mosaic !1virus RNA 3. !$#cross-references MUID:88265861; PMID:3388769 !$#accession JA0108 !'##molecule_type mRNA !'##residues 1-218 ##label DAV !'##cross-references GB:M21464; NID:g331707; PIDN:AAA46416.1; !1PID:g331709 REFERENCE A61297 !$#authors Tsunasawa, S.; Narita, K. !$#journal J. Biochem. (1982) 92:607-613 !$#title Micro-identification of amino-terminal acetylamino acids in !1proteins. !$#cross-references MUID:83056735; PMID:6754709 !$#contents annotation; acetylation COMMENT The genome consists of three single-stranded, positive RNAs, !1designated RNA1, RNA2, and RNA3. GENETICS !$#map_position segment RNA3 CLASSIFICATION #superfamily cucumber mosaic virus coat protein KEYWORDS acetylated amino end; coat protein FEATURE !$1 #modified_site acetylated amino end (Met) #status !8experimental SUMMARY #length 218 #molecular-weight 24243 #checksum 1039 SEQUENCE /// ENTRY VCVXWL #type complete TITLE coat protein - cucumber mosaic virus (strain WL) ORGANISM #formal_name cucumber mosaic virus, CMV #note host Lycopersicon esculentum (tomato) DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Jun-2000 ACCESSIONS JA0137; JU0087 REFERENCE JU0087 !$#authors Quemada, H.; Kearney, C.; Gonsalves, D.; Slightom, J.L. !$#journal J. Gen. Virol. (1989) 70:1065-1073 !$#title Nucleotide sequences of the coat protein genes and flanking !1regions of cucumber mosaic virus strains C and WL RNA 3. !$#cross-references MUID:89279284; PMID:2732712 !$#accession JA0137 !'##molecule_type genomic RNA !'##residues 1-218 ##label QUE !'##cross-references EMBL:D00463; NID:g222043; PIDN:BAA00358.1; !1PID:g222044 REFERENCE A61297 !$#authors Tsunasawa, S.; Narita, K. !$#journal J. Biochem. (1982) 92:607-613 !$#title Micro-identification of amino-terminal acetylamino acids in !1proteins. !$#cross-references MUID:83056735; PMID:6754709 !$#contents annotation; acetylation GENETICS !$#map_position segment RNA3 CLASSIFICATION #superfamily cucumber mosaic virus coat protein KEYWORDS acetylated amino end; coat protein FEATURE !$1 #modified_site acetylated amino end (Met) #status !8experimental SUMMARY #length 218 #molecular-weight 24201 #checksum 1153 SEQUENCE /// ENTRY B46111 #type complete TITLE coat protein - cucumber mosaic virus (strain Kin) ORGANISM #formal_name cucumber mosaic virus, CMV #note host Cucumis sativus (cucumber) DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 23-Jul-1999 ACCESSIONS B46111; S22095 REFERENCE A46111 !$#authors Boccard, F.; Baulcombe, D. !$#journal Virology (1993) 193:563-578 !$#title Mutational analysis of Cis-acting sequences and gene !1function in RNA3 of cucumber mosaic virus. !$#cross-references MUID:93212489; PMID:8460476 !$#accession B46111 !'##molecule_type genomic RNA !'##residues 1-218 ##label BOC !'##cross-references GB:S57834; EMBL:Z12818; NID:g58893; !1PIDN:CAA78279.1; PID:g58895 REFERENCE A61297 !$#authors Tsunasawa, S.; Narita, K. !$#journal J. Biochem. (1982) 92:607-613 !$#title Micro-identification of amino-terminal acetylamino acids in !1proteins. !$#cross-references MUID:83056735; PMID:6754709 !$#contents annotation; acetylation GENETICS !$#map_position segment RNA3 CLASSIFICATION #superfamily cucumber mosaic virus coat protein KEYWORDS acetylated amino end; coat protein; glycoprotein FEATURE !$1 #modified_site acetylated amino end (Met) #status !8experimental\ !$8,43 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 218 #molecular-weight 24201 #checksum 818 SEQUENCE /// ENTRY VCVXY1 #type complete TITLE coat protein - cucumber mosaic virus (strain Y) ORGANISM #formal_name cucumber mosaic virus, CMV #note host Nicotiana tabacum cv. Xanthi nc (tobacco) DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 07-May-1999 ACCESSIONS JA0097 REFERENCE JA0096 !$#authors Nitta, N.; Masuta, C.; Kuwata, S.; Takanami, Y. !$#journal Ann. Phytopathol. Soc. Jpn. (1989) 54:516-522 !$#title Comparative studies on the nucleotide sequence of cucumber !1mosaic virus RNA3 between Y strain and Q strain. !$#accession JA0097 !'##molecule_type mRNA !'##residues 1-218 ##label NIT REFERENCE A61297 !$#authors Tsunasawa, S.; Narita, K. !$#journal J. Biochem. (1982) 92:607-613 !$#title Micro-identification of amino-terminal acetylamino acids in !1proteins. !$#cross-references MUID:83056735; PMID:6754709 !$#contents annotation; acetylation COMMENT The genome consists of three single-stranded, positive RNAs, !1designated RNA1, RNA2, and RNA3. GENETICS !$#map_position segment RNA3 CLASSIFICATION #superfamily cucumber mosaic virus coat protein KEYWORDS acetylated amino end; coat protein FEATURE !$1 #modified_site acetylated amino end (Met) #status !8experimental SUMMARY #length 218 #molecular-weight 24110 #checksum 2923 SEQUENCE /// ENTRY JA0136 #type complete TITLE coat protein - cucumber mosaic virus (strain C) ORGANISM #formal_name cucumber mosaic virus, CMV DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 16-Jun-2000 ACCESSIONS JA0136 REFERENCE JU0087 !$#authors Quemada, H.; Kearney, C.; Gonsalves, D.; Slightom, J.L. !$#journal J. Gen. Virol. (1989) 70:1065-1073 !$#title Nucleotide sequences of the coat protein genes and flanking !1regions of cucumber mosaic virus strains C and WL RNA 3. !$#cross-references MUID:89279284; PMID:2732712 !$#accession JA0136 !'##molecule_type genomic RNA !'##residues 1-218 ##label QUE !'##cross-references GB:D00462; NID:g222041; PIDN:BAA00357.1; !1PID:g222042 REFERENCE A61297 !$#authors Tsunasawa, S.; Narita, K. !$#journal J. Biochem. (1982) 92:607-613 !$#title Micro-identification of amino-terminal acetylamino acids in !1proteins. !$#cross-references MUID:83056735; PMID:6754709 !$#contents annotation; acetylation GENETICS !$#map_position segment RNA3 CLASSIFICATION #superfamily cucumber mosaic virus coat protein KEYWORDS acetylated amino end; coat protein; glycoprotein FEATURE !$1 #modified_site acetylated amino end (Met) #status !8experimental\ !$43 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 218 #molecular-weight 24177 #checksum 773 SEQUENCE /// ENTRY JQ1253 #type complete TITLE coat protein - cucumber mosaic virus (strain FC) ORGANISM #formal_name cucumber mosaic virus, CMV DATE 31-Mar-1992 #sequence_revision 05-Aug-1994 #text_change 16-Jun-2000 ACCESSIONS JQ1253 REFERENCE JQ1253 !$#authors Shintaku, M. !$#journal J. Gen. Virol. (1991) 72:2587-2589 !$#title Coat protein gene sequences of two cucumber mosaic virus !1strains reveal a single amino acid change correlating with !1chlorosis induction. !$#cross-references MUID:92013983; PMID:1919534 !$#accession JQ1253 !'##molecule_type genomic RNA !'##residues 1-218 ##label SHI !'##cross-references GB:D10544; NID:g222024; PIDN:BAA01403.1; !1PID:g222025 !'##note comparison of the amino acid sequence of this protein to that !1of strain P6 shows 97% identity REFERENCE A61297 !$#authors Tsunasawa, S.; Narita, K. !$#journal J. Biochem. (1982) 92:607-613 !$#title Micro-identification of amino-terminal acetylamino acids in !1proteins. !$#cross-references MUID:83056735; PMID:6754709 !$#contents annotation; acetylation COMMENT This cucumber mosaic virus strain induces a yellow !1chlorosis. CLASSIFICATION #superfamily cucumber mosaic virus coat protein KEYWORDS acetylated amino end; coat protein FEATURE !$1 #modified_site acetylated amino end (Met) #status !8experimental SUMMARY #length 218 #molecular-weight 24130 #checksum 2026 SEQUENCE /// ENTRY JQ1254 #type complete TITLE coat protein - cucumber mosaic virus (strain P6) ORGANISM #formal_name cucumber mosaic virus, CMV DATE 31-Mar-1992 #sequence_revision 05-Aug-1994 #text_change 16-Jun-2000 ACCESSIONS JQ1254 REFERENCE JQ1253 !$#authors Shintaku, M. !$#journal J. Gen. Virol. (1991) 72:2587-2589 !$#title Coat protein gene sequences of two cucumber mosaic virus !1strains reveal a single amino acid change correlating with !1chlorosis induction. !$#cross-references MUID:92013983; PMID:1919534 !$#accession JQ1254 !'##molecule_type genomic RNA !'##residues 1-218 ##label SHI !'##cross-references GB:D10545; NID:g222026; PIDN:BAA01404.1; !1PID:g222027 !'##note comparison of the amino acid sequence of this protein to that !1of strain FC shows 97% identity REFERENCE A61297 !$#authors Tsunasawa, S.; Narita, K. !$#journal J. Biochem. (1982) 92:607-613 !$#title Micro-identification of amino-terminal acetylamino acids in !1proteins. !$#cross-references MUID:83056735; PMID:6754709 !$#contents annotation; acetylation COMMENT This cucumber mosaic virus strain induces a yellow !1chlorosis. CLASSIFICATION #superfamily cucumber mosaic virus coat protein KEYWORDS acetylated amino end; coat protein FEATURE !$1 #modified_site acetylated amino end (Met) #status !8experimental SUMMARY #length 218 #molecular-weight 24160 #checksum 1814 SEQUENCE /// ENTRY JS0090 #type complete TITLE coat protein - cucumber mosaic virus (strain O) ORGANISM #formal_name cucumber mosaic virus, CMV DATE 31-Mar-1992 #sequence_revision 05-Aug-1994 #text_change 16-Jun-2000 ACCESSIONS JS0090; PS0314 REFERENCE JS0089 !$#authors Hayakawa, T.; Mizukami, M.; Nakajima, M.; Suzuki, M. !$#journal J. Gen. Virol. (1989) 70:499-504 !$#title Complete nucleotide sequence of RNA 3 from cucumber mosaic !1virus (CMV) strain O: comparative study of nucleotide !1sequences and amino acid sequences among CMV strains O, Q, D !1and Y. !$#cross-references MUID:89279231; PMID:2732698 !$#accession JS0090 !'##molecule_type mRNA !'##residues 1-218 ##label HAY !'##cross-references GB:D00385; NID:g222030; PIDN:BAA00297.1; !1PID:g222032 !$#accession PS0314 !'##molecule_type protein !'##residues 216-218 ##label HA2 REFERENCE A61297 !$#authors Tsunasawa, S.; Narita, K. !$#journal J. Biochem. (1982) 92:607-613 !$#title Micro-identification of amino-terminal acetylamino acids in !1proteins. !$#cross-references MUID:83056735; PMID:6754709 !$#contents annotation; acetylation GENETICS !$#map_position segment 3 CLASSIFICATION #superfamily cucumber mosaic virus coat protein KEYWORDS acetylated amino end; coat protein FEATURE !$1 #modified_site acetylated amino end (Met) #status !8experimental SUMMARY #length 218 #molecular-weight 24272 #checksum 1826 SEQUENCE /// ENTRY VCVXPS #type complete TITLE coat protein - peanut stunt virus (strain J) ORGANISM #formal_name peanut stunt virus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jun-2000 ACCESSIONS B40786; A40786; JQ0605 REFERENCE A40786 !$#authors Karasawa, A.; Nakaho, K.; Kakutani, T.; Minobe, Y.; Ehara, !1Y. !$#journal Virology (1991) 185:464-467 !$#title Nucleotide sequence of RNA 3 of peanut stunt cucumovirus. !$#cross-references MUID:92024111; PMID:1926787 !$#accession B40786 !'##molecule_type genomic RNA !'##residues 1-217 ##label KAR !'##cross-references GB:D00668; NID:g222421; PIDN:BAA00572.1; !1PID:g222423 GENETICS !$#map_position segment 3 CLASSIFICATION #superfamily cucumber mosaic virus coat protein KEYWORDS coat protein SUMMARY #length 217 #molecular-weight 24179 #checksum 5054 SEQUENCE /// ENTRY VCTNS #type complete TITLE coat protein - tobacco necrosis satellite virus ORGANISM #formal_name tobacco necrosis satellite virus DATE 31-Mar-1981 #sequence_revision 31-Mar-1981 #text_change 23-Jul-1999 ACCESSIONS A04217 REFERENCE A04217 !$#authors Ysebaert, M.; van Emmelo, J.; Fiers, W. !$#journal J. Mol. Biol. (1980) 143:273-287 !$#title Total nucleotide sequence of a nearly full-size DNA copy of !1satellite tobacco necrosis virus RNA. !$#cross-references MUID:81170584; PMID:6260960 !$#accession A04217 !'##molecule_type genomic RNA !'##residues 1-196 ##label YSE !'##cross-references GB:J02399; NID:g335254; PIDN:AAA69583.1; !1PID:g335255 CLASSIFICATION #superfamily satellite tobacco necrosis virus coat protein KEYWORDS coat protein SUMMARY #length 196 #molecular-weight 21715 #checksum 4307 SEQUENCE /// ENTRY VCWZMW #type complete TITLE coat protein - maize white line mosaic satellite virus ORGANISM #formal_name maize white line mosaic satellite virus DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 23-Jul-1999 ACCESSIONS A38543 REFERENCE A38543 !$#authors Zhang, L.; Zitter, T.A.; Palukaitis, P. !$#journal Virology (1991) 180:467-473 !$#title Helper virus-dependent replication, nucleotide sequence and !1genome organization of the satellite virus of maize white !1line mosaic virus. !$#cross-references MUID:91111965; PMID:1989380 !$#accession A38543 !'##molecule_type genomic RNA !'##residues 1-218 ##label ZHA !'##cross-references EMBL:M55012; NID:g335126; PIDN:AAA47885.1; !1PID:g335127 COMMENT This virus has not been classified. CLASSIFICATION #superfamily satellite tobacco necrosis virus coat protein KEYWORDS coat protein SUMMARY #length 218 #molecular-weight 23959 #checksum 1209 SEQUENCE /// ENTRY VCBW #type complete TITLE coat protein - southern bean mosaic virus ORGANISM #formal_name southern bean mosaic virus, SBMV DATE 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 03-Feb-1994 ACCESSIONS A04218 REFERENCE A94329 !$#authors Hermodson, M.A.; Abad-Zapatero, C.; Abdel-Meguid, S.S.; !1Pundak, S.; Rossmann, M.G.; Tremaine, J.H. !$#journal Virology (1982) 119:133-149 !$#title Amino acid sequence of southern bean mosaic virus coat !1protein and its relation to the three-dimensional structure !1of the virus. !$#accession A04218 !'##molecule_type protein !'##residues 1-260 ##label HER REFERENCE A93227 !$#authors Abad-Zapatero, C.; Abdel-Meguid, S.S.; Johnson, J.E.; !1Leslie, A.G.W.; Rayment, I.; Rossmann, M.G.; Suck, D.; !1Tsukihara, T. !$#journal Nature (1980) 286:33-39 !$#title Structure of southern bean mosaic virus at 2.8 angstrom !1resolution. !$#contents annotation; X-ray crystallography, 2.8 angstroms CLASSIFICATION #superfamily southern bean mosaic virus coat protein SUMMARY #length 260 #molecular-weight 28231 #checksum 3364 SEQUENCE /// ENTRY VCBWSC #type complete TITLE coat protein - southern bean mosaic virus (strain cowpea) ALTERNATE_NAMES capsid protein ORGANISM #formal_name southern bean mosaic virus, SBMV DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 23-Jul-1999 ACCESSIONS D33739 REFERENCE A33739 !$#authors Wu, S.; Rinehart, C.A.; Kaesberg, P. !$#journal Virology (1987) 161:73-80 !$#title Sequence and organization of southern bean mosaic virus !1genomic RNA. !$#cross-references MUID:88044510; PMID:2823471 !$#accession D33739 !'##molecule_type genomic RNA !'##residues 1-279 ##label WUS !'##cross-references GB:M23021; NID:g511859; PIDN:AAA46567.1; !1PID:g511863 CLASSIFICATION #superfamily southern bean mosaic virus coat protein KEYWORDS capsid protein; coat protein SUMMARY #length 279 #molecular-weight 30555 #checksum 3796 SEQUENCE /// ENTRY VCWQTN #type complete TITLE coat protein - tobacco necrosis virus (strain A) ORGANISM #formal_name tobacco necrosis virus, TNV #note host Phaseolus vulgaris (kidney bean) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 23-Jul-1999 ACCESSIONS D35523 REFERENCE A35523 !$#authors Meulewaeter, F.; Seurinck, J.; van Emmelo, J. !$#journal Virology (1990) 177:699-709 !$#title Genome structure of tobacco necrosis virus strain A. !$#cross-references MUID:90320143; PMID:2371773 !$#accession D35523 !'##molecule_type genomic RNA !'##residues 1-276 ##label MEU !'##cross-references EMBL:M33002; NID:g1172549; PIDN:AAA86437.1; !1PID:g310918 CLASSIFICATION #superfamily southern bean mosaic virus coat protein KEYWORDS coat protein SUMMARY #length 276 #molecular-weight 29784 #checksum 4684 SEQUENCE /// ENTRY VCWQTD #type complete TITLE coat protein - tobacco necrosis virus (strain D) ORGANISM #formal_name tobacco necrosis virus, TNV DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jun-2000 ACCESSIONS JU0371 REFERENCE JU0368 !$#authors Coutts, R.H.A.; Rigden, J.E.; Slabas, A.R.; Lomonossoff, !1G.P.; Wise, P.J. !$#journal J. Gen. Virol. (1991) 72:1521-1529 !$#title The complete sequence of tobacco necrosis virus strain D. !$#cross-references MUID:91311404; PMID:1856691 !$#accession JU0371 !'##molecule_type genomic RNA !'##residues 1-268 ##label COU !'##cross-references GB:D00942; NID:g1638813; PIDN:BAA00790.1; !1PID:g222666 CLASSIFICATION #superfamily southern bean mosaic virus coat protein KEYWORDS coat protein SUMMARY #length 268 #molecular-weight 29031 #checksum 3914 SEQUENCE /// ENTRY WMWQTD #type complete TITLE p7a protein - tobacco necrosis virus (strain D) ORGANISM #formal_name tobacco necrosis virus, TNV DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 08-Apr-1994 ACCESSIONS JU0369 REFERENCE JU0368 !$#authors Coutts, R.H.A.; Rigden, J.E.; Slabas, A.R.; Lomonossoff, !1G.P.; Wise, P.J. !$#journal J. Gen. Virol. (1991) 72:1521-1529 !$#title The complete sequence of tobacco necrosis virus strain D. !$#cross-references MUID:91311404; PMID:1856691 !$#accession JU0369 !'##molecule_type genomic RNA !'##residues 1-64 ##label COU !'##cross-references GB:D00942 CLASSIFICATION #superfamily tobacco necrosis virus p7a protein SUMMARY #length 64 #molecular-weight 7292 #checksum 282 SEQUENCE /// ENTRY WMWQTT #type complete TITLE p7b protein - tobacco necrosis virus (strain D) ORGANISM #formal_name tobacco necrosis virus, TNV DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jun-2000 ACCESSIONS JU0370 REFERENCE JU0368 !$#authors Coutts, R.H.A.; Rigden, J.E.; Slabas, A.R.; Lomonossoff, !1G.P.; Wise, P.J. !$#journal J. Gen. Virol. (1991) 72:1521-1529 !$#title The complete sequence of tobacco necrosis virus strain D. !$#cross-references MUID:91311404; PMID:1856691 !$#accession JU0370 !'##molecule_type genomic RNA !'##residues 1-66 ##label COU !'##cross-references GB:D00942; NID:g1638813; PIDN:BAA00789.1; !1PID:g222665 CLASSIFICATION #superfamily tobacco necrosis virus p7b protein SUMMARY #length 66 #molecular-weight 7373 #checksum 1255 SEQUENCE /// ENTRY WMBWSC #type complete TITLE P4 protein - southern bean mosaic virus (strain cowpea) ORGANISM #formal_name southern bean mosaic virus, SBMV DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 23-Jul-1999 ACCESSIONS A33739 REFERENCE A33739 !$#authors Wu, S.; Rinehart, C.A.; Kaesberg, P. !$#journal Virology (1987) 161:73-80 !$#title Sequence and organization of southern bean mosaic virus !1genomic RNA. !$#cross-references MUID:88044510; PMID:2823471 !$#accession A33739 !'##molecule_type genomic RNA !'##residues 1-185 ##label WUS !'##cross-references GB:M23021; NID:g511859; PIDN:AAA46564.1; !1PID:g511860 CLASSIFICATION #superfamily southern bean mosaic virus P4 protein SUMMARY #length 185 #molecular-weight 20983 #checksum 2569 SEQUENCE /// ENTRY VCTY #type complete TITLE coat protein - turnip yellow mosaic virus ORGANISM #formal_name turnip yellow mosaic virus, TYMV DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 28-Jul-2000 ACCESSIONS S19153; A90586; A90779; S02247; A04219 REFERENCE S19150 !$#authors Dreher, T.W.; Bransom, K.L. !$#journal Plant Mol. Biol. (1992) 18:403-406 !$#title Genomic RNA sequence of turnip yellow mosaic virus isolate !1TYMC, a cDNA-based clone with verified infectivity. !$#cross-references MUID:92119261; PMID:1731998 !$#accession S19153 !'##molecule_type genomic RNA !'##residues 1-189 ##label DRE !'##cross-references EMBL:X16378; NID:g62218; PIDN:CAA34416.1; !1PID:g62221 REFERENCE A90586 !$#authors Stehelin, D.; Peter, R.; Duranton, H. !$#journal Biochim. Biophys. Acta (1973) 317:253-265 !$#title Etude de la structure primaire de la proteine du virus de la !1mosaique jaune du navet. III. Sequence des peptides !1chymotrypsiques de la proteine aminoethylee et enchainement !1des peptides trypsiques. !$#accession A90586 !'##molecule_type protein !'##residues 1-189 ##label STE REFERENCE A90779 !$#authors Guilley, H.; Briand, J.P. !$#journal Cell (1978) 15:113-122 !$#title Nucleotide sequence of turnip yellow mosaic virus coat !1protein mRNA. !$#cross-references MUID:79023049; PMID:699035 !$#accession A90779 !'##molecule_type mRNA !'##residues 1-189 ##label GUI !'##cross-references GB:K00602; NID:g332241; PIDN:AAA46590.1; !1PID:g332243 REFERENCE S01955 !$#authors Morch, M.D.; Boyer, J.C.; Haenni, A.L. !$#journal Nucleic Acids Res. (1988) 16:6157-6173 !$#title Overlapping open reading frames revealed by complete !1nucleotide sequencing of turnip yellow mosaic virus genomic !1RNA. !$#cross-references MUID:88289359; PMID:3399388 !$#accession S02247 !'##status preliminary !'##molecule_type genomic RNA !'##residues 1-85,'A',87-189 ##label MOR !'##cross-references EMBL:X07441; NID:g62222; PIDN:CAA30323.1; !1PID:g62225 CLASSIFICATION #superfamily turnip yellow mosaic virus coat protein KEYWORDS acetylated amino end FEATURE !$1 #modified_site acetylated amino end (Met) #status !8experimental SUMMARY #length 189 #molecular-weight 20088 #checksum 4931 SEQUENCE /// ENTRY VCWPTM #type complete TITLE coat protein - turnip yellow mosaic virus (strain Australia) ORGANISM #formal_name turnip yellow mosaic virus, TYMV DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 23-Jul-1999 ACCESSIONS JQ0111 REFERENCE JQ0109 !$#authors Keese, P.; Mackenzie, A.; Gibbs, A. !$#journal Virology (1989) 172:536-546 !$#title Nucleotide sequence of the genome of an Australian isolate !1of turnip yellow mosaic tymovirus. !$#cross-references MUID:90021184; PMID:2800335 !$#accession JQ0111 !'##molecule_type genomic RNA !'##residues 1-189 ##label KEE !'##cross-references EMBL:J04373; NID:g332244; PIDN:AAA46593.1; !1PID:g332247 CLASSIFICATION #superfamily turnip yellow mosaic virus coat protein KEYWORDS coat protein SUMMARY #length 189 #molecular-weight 20152 #checksum 5536 SEQUENCE /// ENTRY JQ0534 #type complete TITLE coat protein - Kennedya yellow mosaic virus (strain Jervis Bay) ORGANISM #formal_name Kennedya yellow mosaic virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 16-Jun-2000 ACCESSIONS JQ0534 REFERENCE JQ0532 !$#authors Ding, S.; Keese, P.; Gibbs, A. !$#journal J. Gen. Virol. (1990) 71:925-931 !$#title The nucleotide sequence of the genomic RNA of kennedya !1yellow mosaic tymovirus-Jervis Bay isolate: relationships !1with potex- and carlaviruses. !$#cross-references MUID:90218040; PMID:2324710 !$#accession JQ0534 !'##molecule_type genomic RNA !'##residues 1-188 ##label DIN !'##cross-references GB:D00637; NID:g221969; PIDN:BAA00533.1; !1PID:g221972 CLASSIFICATION #superfamily turnip yellow mosaic virus coat protein KEYWORDS coat protein; glycoprotein FEATURE !$99,133 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 188 #molecular-weight 19601 #checksum 5251 SEQUENCE /// ENTRY VCWPEM #type complete TITLE coat protein - eggplant mosaic virus ORGANISM #formal_name eggplant mosaic virus DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 11-May-2000 ACCESSIONS JQ0104; S41852 REFERENCE JQ0102 !$#authors Osorio-Keese, M.E.; Keese, P.; Gibbs, A. !$#journal Virology (1989) 172:547-554 !$#title Nucleotide sequence of the genome of eggplant mosaic !1tymovirus. !$#cross-references MUID:90021185; PMID:2800336 !$#accession JQ0104 !'##molecule_type genomic RNA !'##residues 1-188 ##label OSO !'##cross-references EMBL:J04374; NID:g323865; PIDN:AAA43040.1; !1PID:g323868 REFERENCE S41850 !$#authors Peter, R.; Peter, C.; Dupin, A.; Witz, J. !$#journal C. R. Acad. Sci. III (1989) 309:599-604 !$#title A problem of tymovirus taxonomy: comparison of the coat !1proteins of two Belladonna mottle viruses. !$#cross-references MUID:90058208; PMID:2510912 !$#accession S41852 !'##molecule_type protein !'##residues 108-188 ##label PET CLASSIFICATION #superfamily turnip yellow mosaic virus coat protein KEYWORDS coat protein SUMMARY #length 188 #molecular-weight 19769 #checksum 1010 SEQUENCE /// ENTRY B45540 #type complete TITLE coat protein - Physalis mottle virus ORGANISM #formal_name Physalis mottle virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 23-Jul-1999 ACCESSIONS B45540; A46115 REFERENCE A45540 !$#authors Jacob, A.N.K.; Murthy, M.R.; Savithri, H.S. !$#journal Arch. Virol. (1992) 123:367-377 !$#title Nucleotide sequence of the 3' terminal region of belladonna !1mottle virus-Iowa (renamed Physalis mottle virus) RNA and an !1analysis of the relationships of tymoviral coat proteins. !$#cross-references MUID:92222369; PMID:1562236 !$#accession B45540 !'##molecule_type genomic RNA !'##residues 1-188 ##label JAC !'##cross-references GB:S97776; NID:g248382; PIDN:AAB21997.1; !1PID:g248384 !'##note sequence extracted from NCBI backbone (NCBIN:97776, !1NCBIP:97780) !'##note in Genbank entry S97776, release 109.0, the source is !1designated as Belladonna mottle virus REFERENCE A46115 !$#authors Kekuda, R.; Karande, A.A.; Jacob, A.N.K.; Savithri, H.S. !$#journal Virology (1993) 193:959-966 !$#title Architecture of Physalis mottle tymovirus as probed by !1monoclonal antibodies and cross-linking studies. !$#cross-references MUID:93212529; PMID:8460497 !$#accession A46115 !'##molecule_type protein !'##residues 1-188 ##label KEK CLASSIFICATION #superfamily turnip yellow mosaic virus coat protein KEYWORDS coat protein SUMMARY #length 188 #molecular-weight 19974 #checksum 5801 SEQUENCE /// ENTRY VCWPYM #type complete TITLE coat protein - Ononis yellow mosaic virus ORGANISM #formal_name Ononis yellow mosaic virus DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 23-Jul-1999 ACCESSIONS JQ0108 REFERENCE JQ0106 !$#authors Ding, S.W.; Keese, P.; Gibbs, A. !$#journal Virology (1989) 172:555-563 !$#title Nucleotide sequence of the ononis yellow mosaic tymovirus !1genome. !$#cross-references MUID:90021186; PMID:2800337 !$#accession JQ0108 !'##molecule_type genomic RNA !'##residues 1-192 ##label DIN !'##cross-references EMBL:J04375; NID:g332572; PIDN:AAA46797.1; !1PID:g332575 CLASSIFICATION #superfamily turnip yellow mosaic virus coat protein KEYWORDS coat protein SUMMARY #length 192 #molecular-weight 20466 #checksum 5468 SEQUENCE /// ENTRY JQ1556 #type complete TITLE coat protein - Erysimum latent virus ORGANISM #formal_name Erysimum latent virus, CLV DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 28-May-1999 ACCESSIONS JQ1556 REFERENCE JQ1554 !$#authors Srifah, P.; Keese, P.; Weiller, G.; Gibbs, A. !$#journal J. Gen. Virol. (1992) 73:1437-1447 !$#title Comparisons of the genomic sequences of erysimum latent !1virus and other tymoviruses: A search for the molecular !1basis of their host specificities. !$#cross-references MUID:92300338; PMID:1607861 !$#accession JQ1556 !'##molecule_type genomic RNA !'##residues 1-202 ##label SRI !'##cross-references GB:AF098523; NID:g3892230; PIDN:AAC80556.1; !1PID:g3892233 CLASSIFICATION #superfamily turnip yellow mosaic virus coat protein KEYWORDS coat protein; glycoprotein FEATURE !$28 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 202 #molecular-weight 21482 #checksum 6149 SEQUENCE /// ENTRY WMVQ28 #type complete TITLE 28K protein - potato leaf roll virus (strain 1) ORGANISM #formal_name potato leaf roll virus #note host Solanum tuberosum (potato) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 21-Jul-2000 ACCESSIONS JA0117; S24590 REFERENCE JA0119 !$#authors Mayo, M.A.; Robinson, D.J.; Jolly, C.A.; Hyman, L. !$#journal J. Gen. Virol. (1989) 70:1037-1051 !$#title Nucleotide sequence of potato leafroll luteovirus RNA. !$#cross-references MUID:89279282; PMID:2732710 !$#accession JA0117 !'##molecule_type genomic RNA !'##residues 1-247 ##label MAY !'##cross-references EMBL:X14600; NID:g222293; PIDN:BAA00416.1; !1PID:g222296 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1March 1989 COMMENT The genome is a single-stranded, positive-sense RNA. CLASSIFICATION #superfamily potato leaf roll virus 28K protein SUMMARY #length 247 #molecular-weight 28130 #checksum 7917 SEQUENCE /// ENTRY WMVQ70 #type complete TITLE 70K protein - potato leaf roll virus (strain 1) ORGANISM #formal_name potato leaf roll virus #note host Solanum tuberosum (potato) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 21-Jul-2000 ACCESSIONS JA0118; S24591 REFERENCE JA0119 !$#authors Mayo, M.A.; Robinson, D.J.; Jolly, C.A.; Hyman, L. !$#journal J. Gen. Virol. (1989) 70:1037-1051 !$#title Nucleotide sequence of potato leafroll luteovirus RNA. !$#cross-references MUID:89279282; PMID:2732710 !$#accession JA0118 !'##molecule_type genomic RNA !'##residues 1-639 ##label MAY !'##cross-references EMBL:X14600; NID:g222293; PIDN:BAA00417.1; !1PID:g222297 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1March 1989 COMMENT The genome is a single-stranded, positive-sense RNA. CLASSIFICATION #superfamily potato leaf roll virus 70K protein SUMMARY #length 639 #molecular-weight 69629 #checksum 1964 SEQUENCE /// ENTRY VCVQWA #type complete TITLE coat protein - potato leaf roll virus (strain Wageningen) ORGANISM #formal_name potato leaf roll virus DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 23-Jul-1999 ACCESSIONS S03549 REFERENCE S03546 !$#authors van der Wilk, F.; Huisman, M.J.; Cornelissen, B.J.C.; !1Huttinga, H.; Goldbach, R. !$#journal FEBS Lett. (1989) 245:51-56 !$#title Nucleotide sequence and organization of potato leafroll !1virus genomic RNA. !$#cross-references MUID:89171329; PMID:2466700 !$#accession S03549 !'##molecule_type genomic RNA !'##residues 1-208 ##label VAN !'##cross-references EMBL:Y07496; NID:g61198; PIDN:CAA68797.1; !1PID:g61202 CLASSIFICATION #superfamily potato leaf roll virus coat protein; potato !1leaf roll virus coat protein homology KEYWORDS coat protein FEATURE !$21-208 #domain potato leaf roll virus coat protein homology !8#label COP SUMMARY #length 208 #molecular-weight 23234 #checksum 109 SEQUENCE /// ENTRY VCVQL2 #type complete TITLE coat protein - potato leaf roll virus ORGANISM #formal_name potato leaf roll virus #note host Solanum tuberosum (potato) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jun-2000 ACCESSIONS JQ0001; A60080 REFERENCE A92803 !$#authors Kawchuk, L.M.; Martin, R.R.; Rochon, D.M.; McPherson, J. !$#journal J. Gen. Virol. (1989) 70:783-788 !$#title Identification and characterization of the potato leafroll !1virus putative coat protein gene. !$#cross-references MUID:89279259; PMID:2732704 !$#accession JQ0001 !'##molecule_type mRNA !'##residues 1-208 ##label KAW !'##cross-references GB:D13753; NID:g222290; PIDN:BAA02900.1; !1PID:g222291 REFERENCE A60080 !$#authors Tacke, E.; Sarkar, S.; Salamini, F.; Rohde, W. !$#journal Arch. Virol. (1989) 105:153-163 !$#title Cloning of the gene for the capsid protein of potato !1leafroll virus. !$#cross-references MUID:89321807; PMID:2751428 !$#accession A60080 !'##molecule_type mRNA !'##residues 1-40,'S',42-79,'M',81-191,'T',193-208 ##label TAC CLASSIFICATION #superfamily potato leaf roll virus coat protein; potato !1leaf roll virus coat protein homology KEYWORDS coat protein FEATURE !$1-208 #domain potato leaf roll virus coat protein homology !8#label COP SUMMARY #length 208 #molecular-weight 23202 #checksum 9930 SEQUENCE /// ENTRY VCVQGB #type fragment TITLE coat protein - beet western yellows virus (isolate GB1) (fragment) ORGANISM #formal_name beet western yellows virus #variety isolate GB1 (from sugar beet) DATE 30-Sep-1991 #sequence_revision 17-Apr-1998 #text_change 23-Jul-1999 ACCESSIONS S01935 REFERENCE S01935 !$#authors Veidt, I.; Lot, H.; Leiser, M.; Scheidecker, D.; Guilley, !1H.; Richards, K.; Jonard, G. !$#journal Nucleic Acids Res. (1988) 16:9917-9932 !$#title Nucleotide sequence of beet western yellows virus RNA. !$#cross-references MUID:89057523; PMID:3194229 !$#accession S01935 !'##molecule_type genomic RNA !'##residues 1-201 ##label VEI !'##cross-references EMBL:X13062; NID:g58782; PIDN:CAA31459.1; !1PID:g809537 CLASSIFICATION #superfamily potato leaf roll virus coat protein; potato !1leaf roll virus coat protein homology KEYWORDS coat protein FEATURE !$1-201 #domain potato leaf roll virus coat protein homology !8(fragment) #label COP SUMMARY #length 201 #checksum 8415 SEQUENCE /// ENTRY VCVQFL #type complete TITLE coat protein - beet western yellows virus (isolate FL1) ORGANISM #formal_name beet western yellows virus DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 23-Jul-1999 ACCESSIONS S01941 REFERENCE S01935 !$#authors Veidt, I.; Lot, H.; Leiser, M.; Scheidecker, D.; Guilley, !1H.; Richards, K.; Jonard, G. !$#journal Nucleic Acids Res. (1988) 16:9917-9932 !$#title Nucleotide sequence of beet western yellows virus RNA. !$#cross-references MUID:89057523; PMID:3194229 !$#accession S01941 !'##molecule_type genomic RNA !'##residues 1-202 ##label VEI !'##cross-references EMBL:X13063; NID:g62294; PIDN:CAA31465.1; !1PID:g62298 CLASSIFICATION #superfamily potato leaf roll virus coat protein; potato !1leaf roll virus coat protein homology KEYWORDS coat protein FEATURE !$1-202 #domain potato leaf roll virus coat protein homology !8#label COP SUMMARY #length 202 #molecular-weight 22484 #checksum 1170 SEQUENCE /// ENTRY VCXBPM #type complete TITLE coat protein - pea enation mosaic virus ORGANISM #formal_name pea enation mosaic virus, PEMV DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 23-Jul-1999 ACCESSIONS JQ1385 REFERENCE JQ1382 !$#authors Demler, S.A.; de Zoeten, G.A. !$#journal J. Gen. Virol. (1991) 72:1819-1834 !$#title The nucleotide sequence and luteovirus-like nature of RNA 1 !1of an aphid non-transmissible strain of pea enation mosaic !1virus. !$#cross-references MUID:91341468; PMID:1875194 !$#accession JQ1385 !'##molecule_type genomic RNA !'##residues 1-189 ##label DEM !'##cross-references GB:L04573; NID:g294105; PIDN:AAA72301.1; !1PID:g294110 GENETICS !$#map_position segment 1 CLASSIFICATION #superfamily potato leaf roll virus coat protein; potato !1leaf roll virus coat protein homology KEYWORDS coat protein FEATURE !$4-188 #domain potato leaf roll virus coat protein homology !8#label COP SUMMARY #length 189 #molecular-weight 21128 #checksum 5119 SEQUENCE /// ENTRY VCVQBY #type complete TITLE coat protein - barley yellow dwarf virus ORGANISM #formal_name barley yellow dwarf virus, BYDV #note host Avena sativa (oat) DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 23-Jul-1999 ACCESSIONS JA0101; S00948 REFERENCE JA0101 !$#authors Miller, W.A.; Waterhouse, P.M.; Kortt, A.A.; Gerlach, W.L. !$#journal Virology (1988) 165:306-309 !$#title Sequence and identification of the barley yellow dwarf virus !1coat protein gene. !$#cross-references MUID:88265877; PMID:3388774 !$#accession JA0101 !'##molecule_type mRNA !'##residues 1-200 ##label MIL1 !'##cross-references GB:M21347; NID:g323234; PIDN:AAA87366.1; !1PID:g323235 REFERENCE S00946 !$#authors Miller, W.A.; Waterhouse, P.M.; Gerlach, W.L. !$#journal Nucleic Acids Res. (1988) 16:6097-6111 !$#title Sequence and organization of barley yellow dwarf virus !1genomic RNA. !$#cross-references MUID:88289355; PMID:3399386 !$#accession S00948 !'##molecule_type genomic RNA !'##residues 1-200 ##label MIL2 !'##cross-references EMBL:X07653; NID:g58798; PIDN:CAA30493.1; !1PID:g58800 CLASSIFICATION #superfamily potato leaf roll virus coat protein; potato !1leaf roll virus coat protein homology KEYWORDS coat protein FEATURE !$13-200 #domain potato leaf roll virus coat protein homology !8#label COP SUMMARY #length 200 #molecular-weight 22047 #checksum 4567 SEQUENCE /// ENTRY VCVQB3 #type complete TITLE coat protein - barley yellow dwarf virus (strain MAV-PS1) ORGANISM #formal_name barley yellow dwarf virus, BYDV DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jun-2000 ACCESSIONS JQ1411 REFERENCE JQ1409 !$#authors Ueng, P.P.; Vincent, J.R.; Kawata, E.E.; Lei, C.H.; Lister, !1R.M.; Larkins, B.A. !$#journal J. Gen. Virol. (1992) 73:487-492 !$#title Nucleotide sequence analysis of the genomes of the MAV-PS1 !1and P-PAV isolates of barley yellow dwarf virus. !$#cross-references MUID:92166764; PMID:1538199 !$#accession JQ1411 !'##molecule_type genomic RNA !'##residues 1-199 ##label UEN !'##cross-references GB:D11028; DDBJ:D01213; NID:g221084; !1PIDN:BAA01781.1; PID:g221087 CLASSIFICATION #superfamily potato leaf roll virus coat protein; potato !1leaf roll virus coat protein homology KEYWORDS coat protein FEATURE !$1-199 #domain potato leaf roll virus coat protein homology !8#label COP SUMMARY #length 199 #molecular-weight 21932 #checksum 3009 SEQUENCE /// ENTRY VCVQC3 #type complete TITLE coat protein - barley yellow dwarf virus (strain P-PAV) ORGANISM #formal_name barley yellow dwarf virus, BYDV DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jun-2000 ACCESSIONS JQ1417 REFERENCE JQ1409 !$#authors Ueng, P.P.; Vincent, J.R.; Kawata, E.E.; Lei, C.H.; Lister, !1R.M.; Larkins, B.A. !$#journal J. Gen. Virol. (1992) 73:487-492 !$#title Nucleotide sequence analysis of the genomes of the MAV-PS1 !1and P-PAV isolates of barley yellow dwarf virus. !$#cross-references MUID:92166764; PMID:1538199 !$#accession JQ1417 !'##molecule_type genomic RNA !'##residues 1-200 ##label UEN !'##cross-references GB:D11032; DDBJ:D01214; NID:g221098; !1PIDN:BAA01787.1; PID:g221101 !'##note 124-Leu was also found !'##note the authors translated the codon UUG for residue 196 as Met and !1AUG for residue 197 as Leu CLASSIFICATION #superfamily potato leaf roll virus coat protein; potato !1leaf roll virus coat protein homology KEYWORDS coat protein FEATURE !$1-200 #domain potato leaf roll virus coat protein homology !8#label COP SUMMARY #length 200 #molecular-weight 21978 #checksum 4042 SEQUENCE /// ENTRY VCWURB #type complete TITLE coat protein - raspberry bushy dwarf virus (strain R15) ORGANISM #formal_name raspberry bushy dwarf virus DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 16-Jun-2000 ACCESSIONS JQ0936 REFERENCE JQ0936 !$#authors Mayo, M.A.; Jolly, C.A.; Murant, A.F.; Raschke, J.H. !$#journal J. Gen. Virol. (1991) 72:469-472 !$#title Nucleotide sequence of raspberry bushy dwarf virus RNA-3. !$#cross-references MUID:91132152; PMID:1993886 !$#accession JQ0936 !'##molecule_type genomic RNA !'##residues 1-274 ##label MAY !'##cross-references GB:D01052; NID:g222580; PIDN:BAA00855.1; !1PID:g222581 GENETICS !$#map_position segment 3 CLASSIFICATION #superfamily raspberry bushy dwarf virus coat protein KEYWORDS coat protein SUMMARY #length 274 #molecular-weight 30509 #checksum 2729 SEQUENCE /// ENTRY WMVQ53 #type complete TITLE 80K protein - potato leaf roll virus (strain 1) CONTAINS 53K protein; coat protein ORGANISM #formal_name potato leaf roll virus #note host Solanum tuberosum (potato) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 30-Apr-1999 ACCESSIONS JA0122; JA0120 REFERENCE JA0119 !$#authors Mayo, M.A.; Robinson, D.J.; Jolly, C.A.; Hyman, L. !$#journal J. Gen. Virol. (1989) 70:1037-1051 !$#title Nucleotide sequence of potato leafroll luteovirus RNA. !$#cross-references MUID:89279282; PMID:2732710 !$#accession JA0122 !'##molecule_type genomic RNA !'##residues 1-716 ##label MAY !'##note readthrough of the terminator UAG occurs between codons AAA for !1208-Lys and GUA for 209-Val CLASSIFICATION #superfamily potato leaf roll virus 80K protein; potato leaf !1roll virus coat protein homology KEYWORDS coat protein FEATURE !$21-208 #domain potato leaf roll virus coat protein homology !8#label COP\ !$209-716 #product 53K protein #status predicted #label FFP SUMMARY #length 716 #molecular-weight 79696 #checksum 3080 SEQUENCE /// ENTRY WMWRMS #type complete TITLE nonstructural protein NS3 - maize stripe virus ORGANISM #formal_name maize stripe virus #note host Zea mays (maize) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 23-Jul-1999 ACCESSIONS A39146 REFERENCE A39146 !$#authors Huiet, L.; Klaassen, V.; Tsai, J.H.; Falk, B.W. !$#journal Virology (1991) 182:47-53 !$#title Nucleotide sequence and RNA hybridization analyses reveal an !1ambisense coding strategy for maize stripe virus RNA3. !$#cross-references MUID:91220684; PMID:2024478 !$#accession A39146 !'##molecule_type genomic RNA !'##residues 1-197 ##label HUI !'##cross-references EMBL:M57426; NID:g293916; PIDN:AAA46636.1; !1PID:g293917 GENETICS !$#map_position segment 3 CLASSIFICATION #superfamily maize stripe virus nonstructural protein NS3 KEYWORDS nonstructural protein SUMMARY #length 197 #molecular-weight 22732 #checksum 9036 SEQUENCE /// ENTRY JQ1637 #type complete TITLE nonstructural protein NS4 - maize stripe virus ORGANISM #formal_name maize stripe virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 21-Jul-2000 ACCESSIONS JQ1637 REFERENCE JQ1636 !$#authors Huiet, L.; Tsai, J.H.; Falk, B.W. !$#journal J. Gen. Virol. (1992) 73:1603-1607 !$#title Complete sequence of maize stripe virus RNA4 and mapping of !1its subgenomic RNAs. !$#cross-references MUID:92333241; PMID:1629690 !$#accession JQ1637 !'##molecule_type mRNA !'##residues 1-283 ##label HUI !'##cross-references GB:S40180; NID:g251580; PIDN:AAB22542.2; !1PID:g5705954 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily maize stripe virus nonstructural protein NS4 KEYWORDS nonstructural protein SUMMARY #length 283 #molecular-weight 31924 #checksum 1150 SEQUENCE /// ENTRY JQ1963 #type complete TITLE nonstructural protein NS5 - maize stripe virus ORGANISM #formal_name maize stripe virus DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 28-May-1999 ACCESSIONS JQ1963 REFERENCE JQ1963 !$#authors Huiet, L.; Tsai, J.H.; Falk, B.W. !$#journal J. Gen. Virol. (1993) 74:549-554 !$#title Maize stripe virus RNA5 is of negative polarity and encodes !1a highly basic protein. !$#cross-references MUID:93224875; PMID:8468548 !$#accession JQ1963 !'##molecule_type genomic RNA !'##residues 1-375 ##label HUI !'##cross-references GB:S58504; NID:g299098; PIDN:AAB26111.1; !1PID:g299099 GENETICS !$#map_position segment 5 CLASSIFICATION #superfamily maize stripe virus nonstructural protein NS5 KEYWORDS nonstructural protein SUMMARY #length 375 #molecular-weight 44281 #checksum 8911 SEQUENCE /// ENTRY VNWRMS #type complete TITLE nucleocapsid protein N - maize stripe virus ORGANISM #formal_name maize stripe virus #note host Zea mays (maize) DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 23-Jul-1999 ACCESSIONS B39146 REFERENCE A39146 !$#authors Huiet, L.; Klaassen, V.; Tsai, J.H.; Falk, B.W. !$#journal Virology (1991) 182:47-53 !$#title Nucleotide sequence and RNA hybridization analyses reveal an !1ambisense coding strategy for maize stripe virus RNA3. !$#cross-references MUID:91220684; PMID:2024478 !$#accession B39146 !'##molecule_type genomic RNA !'##residues 1-316 ##label HUI !'##cross-references EMBL:M57426; NID:g293916; PIDN:AAA46637.1; !1PID:g293918 GENETICS !$#map_position segment 3 CLASSIFICATION #superfamily maize stripe virus nucleocapsid protein N KEYWORDS nucleocapsid SUMMARY #length 316 #molecular-weight 34597 #checksum 6663 SEQUENCE /// ENTRY JQ1636 #type complete TITLE major noncapsid protein - maize stripe virus ORGANISM #formal_name maize stripe virus DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 23-Jul-1999 ACCESSIONS JQ1636; A46340; B46340 REFERENCE JQ1636 !$#authors Huiet, L.; Tsai, J.H.; Falk, B.W. !$#journal J. Gen. Virol. (1992) 73:1603-1607 !$#title Complete sequence of maize stripe virus RNA4 and mapping of !1its subgenomic RNAs. !$#cross-references MUID:92333241; PMID:1629690 !$#accession JQ1636 !'##molecule_type mRNA !'##residues 1-176 ##label HUI !'##cross-references GB:S40180; NID:g251580; PIDN:AAB22541.1; !1PID:g251581 REFERENCE A46340 !$#authors Huiet, L.; Klaassen, V.; Tsai, J.H.; Falk, B.W. !$#journal Virology (1990) 179:862-866 !$#title Identification and sequence analysis of the maize stripe !1virus major noncapsid protein gene. !$#cross-references MUID:91049455; PMID:2238475 !$#accession A46340 !'##molecule_type genomic RNA !'##residues 1-176 ##label HU1 !'##cross-references GB:M60181; NID:g332313; PIDN:AAA46634.1; !1PID:g332314 !$#accession B46340 !'##molecule_type protein !'##residues 68-79 ##label HU2 GENETICS !$#map_position segment 4 CLASSIFICATION #superfamily maize stripe virus major noncapsid protein KEYWORDS noncapsid protein SUMMARY #length 176 #molecular-weight 19959 #checksum 8637 SEQUENCE /// ENTRY GNVQLL #type complete TITLE genome-linked protein - potato leaf roll virus (strain 1) ORGANISM #formal_name potato leaf roll virus #note host Solanum tuberosum (potato) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 21-Jul-2000 ACCESSIONS JA0121; S36689 REFERENCE JA0119 !$#authors Mayo, M.A.; Robinson, D.J.; Jolly, C.A.; Hyman, L. !$#journal J. Gen. Virol. (1989) 70:1037-1051 !$#title Nucleotide sequence of potato leafroll luteovirus RNA. !$#cross-references MUID:89279282; PMID:2732710 !$#accession JA0121 !'##molecule_type genomic RNA !'##residues 1-156 ##label MAY !'##cross-references EMBL:X14600; NID:g222293; PIDN:BAA00420.1; !1PID:g222299 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1March 1989 CLASSIFICATION #superfamily potato leaf roll virus genome-linked protein KEYWORDS genome-linked protein SUMMARY #length 156 #molecular-weight 17427 #checksum 2437 SEQUENCE /// ENTRY GNVQL2 #type complete TITLE genome-linked protein - potato leaf roll virus ORGANISM #formal_name potato leaf roll virus #note host Solanum tuberosum (potato) DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jun-2000 ACCESSIONS JQ0002; B60080 REFERENCE A92803 !$#authors Kawchuk, L.M.; Martin, R.R.; Rochon, D.M.; McPherson, J. !$#journal J. Gen. Virol. (1989) 70:783-788 !$#title Identification and characterization of the potato leafroll !1virus putative coat protein gene. !$#cross-references MUID:89279259; PMID:2732704 !$#accession JQ0002 !'##molecule_type mRNA !'##residues 1-156 ##label KAW !'##cross-references GB:D13753; NID:g222290; PIDN:BAA02901.1; !1PID:g222292 REFERENCE A60080 !$#authors Tacke, E.; Sarkar, S.; Salamini, F.; Rohde, W. !$#journal Arch. Virol. (1989) 105:153-163 !$#title Cloning of the gene for the capsid protein of potato !1leafroll virus. !$#cross-references MUID:89321807; PMID:2751428 !$#accession B60080 !'##molecule_type mRNA !'##residues 1-9,'G',11-40,'V',42-120,'A',122-156 ##label TAC CLASSIFICATION #superfamily potato leaf roll virus genome-linked protein KEYWORDS genome-linked protein SUMMARY #length 156 #molecular-weight 17381 #checksum 2481 SEQUENCE /// ENTRY GNVQWA #type complete TITLE genome-linked protein - potato leaf roll virus (strain Wageningen) ALTERNATE_NAMES VPg protein ORGANISM #formal_name potato leaf roll virus #note host Solanum tuberosum (potato) DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 23-Jul-1999 ACCESSIONS S03550 REFERENCE S03546 !$#authors van der Wilk, F.; Huisman, M.J.; Cornelissen, B.J.C.; !1Huttinga, H.; Goldbach, R. !$#journal FEBS Lett. (1989) 245:51-56 !$#title Nucleotide sequence and organization of potato leafroll !1virus genomic RNA. !$#cross-references MUID:89171329; PMID:2466700 !$#accession S03550 !'##molecule_type genomic RNA !'##residues 1-156 ##label VAN !'##cross-references EMBL:Y07496; NID:g61198; PIDN:CAA68798.1; !1PID:g61203 CLASSIFICATION #superfamily potato leaf roll virus genome-linked protein KEYWORDS genome-linked protein SUMMARY #length 156 #molecular-weight 17344 #checksum 2019 SEQUENCE /// ENTRY GNVQGB #type complete TITLE genome-linked protein - beet western yellows virus (strain GB1) ORGANISM #formal_name beet western yellows virus DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 23-Jul-1999 ACCESSIONS S01936 REFERENCE S01935 !$#authors Veidt, I.; Lot, H.; Leiser, M.; Scheidecker, D.; Guilley, !1H.; Richards, K.; Jonard, G. !$#journal Nucleic Acids Res. (1988) 16:9917-9932 !$#title Nucleotide sequence of beet western yellows virus RNA. !$#cross-references MUID:89057523; PMID:3194229 !$#accession S01936 !'##molecule_type genomic RNA !'##residues 1-175 ##label VEI !'##cross-references EMBL:X13062; NID:g58782; PIDN:CAA31460.1; !1PID:g58783 !'##note the authors translated the codon GAC for residue 70 as Glu CLASSIFICATION #superfamily potato leaf roll virus genome-linked protein KEYWORDS genome-linked protein SUMMARY #length 175 #molecular-weight 19689 #checksum 6550 SEQUENCE /// ENTRY GNVQFL #type complete TITLE genome-linked protein - beet western yellows virus (strain FL1) ORGANISM #formal_name beet western yellows virus DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 23-Jul-1999 ACCESSIONS S01942 REFERENCE S01935 !$#authors Veidt, I.; Lot, H.; Leiser, M.; Scheidecker, D.; Guilley, !1H.; Richards, K.; Jonard, G. !$#journal Nucleic Acids Res. (1988) 16:9917-9932 !$#title Nucleotide sequence of beet western yellows virus RNA. !$#cross-references MUID:89057523; PMID:3194229 !$#accession S01942 !'##molecule_type genomic RNA !'##residues 1-175 ##label VEI !'##cross-references EMBL:X13063; NID:g62294; PIDN:CAA31466.1; !1PID:g62299 CLASSIFICATION #superfamily potato leaf roll virus genome-linked protein KEYWORDS genome-linked protein SUMMARY #length 175 #molecular-weight 19567 #checksum 6464 SEQUENCE /// ENTRY WMVQBY #type complete TITLE genome-linked protein - barley yellow dwarf virus ALTERNATE_NAMES probable RNA terminal protein ORGANISM #formal_name barley yellow dwarf virus, BYDV #note host Avena sativa (oat) DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 23-Jul-1999 ACCESSIONS JU0040; S00949 REFERENCE JA0101 !$#authors Miller, W.A.; Waterhouse, P.M.; Kortt, A.A.; Gerlach, W.L. !$#journal Virology (1988) 165:306-309 !$#title Sequence and identification of the barley yellow dwarf virus !1coat protein gene. !$#cross-references MUID:88265877; PMID:3388774 !$#accession JU0040 !'##molecule_type mRNA !'##residues 1-153 ##label MIL !'##cross-references GB:M21347; NID:g323234; PIDN:AAA87367.1; !1PID:g807587 REFERENCE S00946 !$#authors Miller, W.A.; Waterhouse, P.M.; Gerlach, W.L. !$#journal Nucleic Acids Res. (1988) 16:6097-6111 !$#title Sequence and organization of barley yellow dwarf virus !1genomic RNA. !$#cross-references MUID:88289355; PMID:3399386 !$#accession S00949 !'##molecule_type genomic RNA !'##residues 1-153 ##label MI2 !'##cross-references EMBL:X07653; NID:g58798; PIDN:CAA30494.1; !1PID:g58801 CLASSIFICATION #superfamily potato leaf roll virus genome-linked protein KEYWORDS genome-linked protein SUMMARY #length 153 #molecular-weight 17147 #checksum 936 SEQUENCE /// ENTRY GNVQB4 #type complete TITLE genome-linked protein - barley yellow dwarf virus (strain MAV-PS1) ALTERNATE_NAMES VPg protein ORGANISM #formal_name barley yellow dwarf virus, BYDV DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jun-2000 ACCESSIONS JQ1412 REFERENCE JQ1409 !$#authors Ueng, P.P.; Vincent, J.R.; Kawata, E.E.; Lei, C.H.; Lister, !1R.M.; Larkins, B.A. !$#journal J. Gen. Virol. (1992) 73:487-492 !$#title Nucleotide sequence analysis of the genomes of the MAV-PS1 !1and P-PAV isolates of barley yellow dwarf virus. !$#cross-references MUID:92166764; PMID:1538199 !$#accession JQ1412 !'##molecule_type genomic RNA !'##residues 1-154 ##label UEN !'##cross-references GB:D11028; DDBJ:D01213; NID:g221084; !1PIDN:BAA01782.1; PID:g221088 CLASSIFICATION #superfamily potato leaf roll virus genome-linked protein KEYWORDS genome-linked protein SUMMARY #length 154 #molecular-weight 17180 #checksum 4150 SEQUENCE /// ENTRY GNVQC4 #type complete TITLE genome-linked protein - barley yellow dwarf virus (strain P-PAV) ALTERNATE_NAMES VPg protein ORGANISM #formal_name barley yellow dwarf virus, BYDV DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Jun-2000 ACCESSIONS JQ1418 REFERENCE JQ1409 !$#authors Ueng, P.P.; Vincent, J.R.; Kawata, E.E.; Lei, C.H.; Lister, !1R.M.; Larkins, B.A. !$#journal J. Gen. Virol. (1992) 73:487-492 !$#title Nucleotide sequence analysis of the genomes of the MAV-PS1 !1and P-PAV isolates of barley yellow dwarf virus. !$#cross-references MUID:92166764; PMID:1538199 !$#accession JQ1418 !'##molecule_type genomic RNA !'##residues 1-153 ##label UEN !'##cross-references GB:D11032; DDBJ:D01214; NID:g221098; !1PIDN:BAA01788.1; PID:g221102 !'##note 61-Leu was also found !'##note the authors translated the codon UCC for residue 93 as Gln CLASSIFICATION #superfamily potato leaf roll virus genome-linked protein KEYWORDS genome-linked protein SUMMARY #length 153 #molecular-weight 17123 #checksum 1802 SEQUENCE /// ENTRY P3VVGF #type complete TITLE P3 protein - grapevine fanleaf virus ORGANISM #formal_name grapevine fanleaf virus DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Jun-2000 ACCESSIONS A92804; JE0069; JU0023 REFERENCE A92804 !$#authors Fuchs, M.; Pinck, M.; Serghini, M.A.; Ravelonandro, M.; !1Walter, B.; Pinck, L. !$#journal J. Gen. Virol. (1989) 70:955-962 !$#title The nucleotide sequence of satellite RNA in grapevine !1fanleaf virus, strain F13. !$#cross-references MUID:89279276; PMID:2471799 !$#accession A92804 !'##molecule_type genomic RNA !'##residues 1-341 ##label FUC !'##cross-references GB:D00442; NID:g221423; PIDN:BAA00343.1; !1PID:g221424 !'##experimental_source strain F13 COMMENT The genome consists of two species of single-stranded, !1positive-sense RNA, called RNA1 and RNA2, which are !1separately encapsidated. In addition, this virus also !1contains a satellite RNA, called RNA3. COMMENT This protein is encoded by the RNA3. CLASSIFICATION #superfamily grapevine fanleaf virus P3 protein SUMMARY #length 341 #molecular-weight 37276 #checksum 9785 SEQUENCE /// ENTRY P3VVAM #type complete TITLE P3 protein - arabis mosaic virus (strain lilac) ORGANISM #formal_name arabis mosaic virus DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 16-Jun-2000 ACCESSIONS JQ0579 REFERENCE JQ0579 !$#authors Liu, Y.Y.; Hellen, C.U.T.; Cooper, J.I.; Bertioli, D.J.; !1Coates, D.; Bauer, G. !$#journal J. Gen. Virol. (1990) 71:1259-1263 !$#title The nucleotide sequence of a satellite RNA associated with !1arabis mosaic nepovirus. !$#cross-references MUID:90278415; PMID:1693660 !$#accession JQ0579 !'##molecule_type genomic RNA !'##residues 1-360 ##label LIU !'##cross-references DDBJ:D00664; NID:g221019; PIDN:BAA00564.1; !1PID:g221020; GB:D00664 CLASSIFICATION #superfamily grapevine fanleaf virus P3 protein SUMMARY #length 360 #molecular-weight 38849 #checksum 6580 SEQUENCE /// ENTRY VCXDS1 #type complete TITLE structural protein VP1 - Sulfolobus particle SSV1 (strain B12) ORGANISM #formal_name Sulfolobus particle SSV1 #note host Sulfolobus shibatae DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Feb-1997 ACCESSIONS A40782; S03235 REFERENCE A40782 !$#authors Palm, P.; Schleper, C.; Grampp, B.; Yeats, S.; McWilliams, !1P.; Reiter, W.D.; Zillig, W. !$#journal Virology (1991) 185:242-250 !$#title Complete nucleotide sequence of the virus SSV1 of the !1archaebacterium Sulfolobus shibatae. !$#cross-references MUID:92024080; PMID:1926776 !$#accession A40782 !'##status translation not shown !'##molecule_type DNA !'##residues 1-144 ##label PAL !'##cross-references EMBL:X07234 CLASSIFICATION #superfamily Sulfolobus particle SSV1 structural protein VP1 KEYWORDS structural protein; transmembrane protein SUMMARY #length 144 #molecular-weight 16076 #checksum 2182 SEQUENCE /// ENTRY VCXDS3 #type complete TITLE structural protein VP3 - Sulfolobus particle SSV1 (strain B12) ORGANISM #formal_name Sulfolobus particle SSV1 #note host Sulfolobus shibatae DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 23-Jul-1999 ACCESSIONS C40782; S03236 REFERENCE A40782 !$#authors Palm, P.; Schleper, C.; Grampp, B.; Yeats, S.; McWilliams, !1P.; Reiter, W.D.; Zillig, W. !$#journal Virology (1991) 185:242-250 !$#title Complete nucleotide sequence of the virus SSV1 of the !1archaebacterium Sulfolobus shibatae. !$#cross-references MUID:92024080; PMID:1926776 !$#accession C40782 !'##status translation not shown !'##molecule_type DNA !'##residues 1-92 ##label PAL !'##cross-references EMBL:X07234; NID:g46703; PIDN:CAA30203.1; !1PID:g46729 CLASSIFICATION #superfamily Sulfolobus particle SSV1 structural protein VP1 KEYWORDS structural protein; transmembrane protein SUMMARY #length 92 #molecular-weight 9868 #checksum 1741 SEQUENCE /// ENTRY VCXDS2 #type complete TITLE structural protein VP2 - Sulfolobus particle SSV1 (strain B12) ORGANISM #formal_name Sulfolobus particle SSV1 #note host Sulfolobus shibatae DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 23-Jul-1999 ACCESSIONS B40782; S03237 REFERENCE A40782 !$#authors Palm, P.; Schleper, C.; Grampp, B.; Yeats, S.; McWilliams, !1P.; Reiter, W.D.; Zillig, W. !$#journal Virology (1991) 185:242-250 !$#title Complete nucleotide sequence of the virus SSV1 of the !1archaebacterium Sulfolobus shibatae. !$#cross-references MUID:92024080; PMID:1926776 !$#accession B40782 !'##status translation not shown !'##molecule_type DNA !'##residues 1-74 ##label PAL !'##cross-references EMBL:X07234; NID:g46703; PIDN:CAA30204.1; !1PID:g46730 CLASSIFICATION #superfamily Sulfolobus particle SSV1 structural protein VP2 KEYWORDS DNA binding; structural protein SUMMARY #length 74 #molecular-weight 8827 #checksum 6431 SEQUENCE /// ENTRY YVBPMS #type complete TITLE lysis protein - phage MS2 ALTERNATE_NAMES gene L protein ORGANISM #formal_name phage MS2 DATE 30-Nov-1980 #sequence_revision 30-Nov-1980 #text_change 23-Jul-1999 ACCESSIONS A90787; A93163; A93179; A04220 REFERENCE A90787 !$#authors Atkins, J.F.; Steitz, J.A.; Anderson, C.W.; Model, P. !$#journal Cell (1979) 18:247-256 !$#title Binding of mammalian ribosomes to MS2 phage RNA reveals an !1overlapping gene encoding a lysis function. !$#cross-references MUID:80045008; PMID:498271 !$#contents identification of protein coding region !$#accession A90787 !'##molecule_type genomic RNA; protein !'##residues 1-75 ##label ATK !'##cross-references GB:V00642; GB:J02467; NID:g15081; PIDN:CAA23990.1; !1PID:g15084; GB:M24961; NID:g215232; PID:g215235 !'##note the translation was prepared from earlier nucleic acid sequence !1determinations; the translation origin was demonstrated by !1ribosome binding; radiolabled protein sequencing confirmed !1the amino-terminus REFERENCE A93163 !$#authors Min Jou, W.; Haegeman, G.; Ysebaert, M.; Fiers, W. !$#journal Nature (1972) 237:82-88 !$#title Nucleotide sequence of the gene coding for the bacteriophage !1MS2 coat protein. !$#cross-references MUID:72195690; PMID:4555447 !$#accession A93163 !'##status translation not shown !'##molecule_type genomic RNA !'##residues 1-34 ##label MIN !'##cross-references GB:V00642; GB:J02467; NID:g15081; GB:M24961; !1NID:g215232 REFERENCE A93179 !$#authors Fiers, W.; Contreras, R.; Duerinck, F.; Haegeman, G.; !1Iserentant, D.; Merregaert, J.; Min Jou, W.; Molemans, F.; !1Raeymaekers, A.; van den Berghe, A.; Volckaert, G.; !1Ysebaert, M. !$#journal Nature (1976) 260:500-507 !$#title Complete nucleotide sequence of bacteriophage MS2 RNA: !1primary and secondary structure of the replicase gene. !$#cross-references MUID:76174431; PMID:1264203 !$#accession A93179 !'##status translation not shown !'##molecule_type genomic RNA !'##residues 29-75 ##label FIE !'##cross-references GB:V00642; GB:J02467; NID:g15081; GB:M24961; !1NID:g215232 CLASSIFICATION #superfamily phage GA lysis protein KEYWORDS host cell lysis SUMMARY #length 75 #molecular-weight 8870 #checksum 1882 SEQUENCE /// ENTRY YVBPGA #type complete TITLE lysis protein - phage GA ORGANISM #formal_name phage GA #note host Escherichia coli DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 23-Jul-1999 ACCESSIONS B29178 REFERENCE A92000 !$#authors Inokuchi, Y.; Takahashi, R.; Hirose, T.; Inayama, S.; !1Jacobson, A.B.; Hirashima, A. !$#journal J. Biochem. (1986) 99:1169-1180 !$#title The complete nucleotide sequence of the group II RNA !1coliphage GA. !$#cross-references MUID:86223910; PMID:3711059 !$#accession B29178 !'##molecule_type genomic RNA !'##residues 1-63 ##label INO !'##cross-references GB:X03869; NID:g15076; PIDN:CAA27498.1; PID:g15079 CLASSIFICATION #superfamily phage GA lysis protein KEYWORDS host cell lysis SUMMARY #length 63 #molecular-weight 7358 #checksum 9337 SEQUENCE /// ENTRY B46324 #type complete TITLE lysis protein - phage JP34 ORGANISM #formal_name phage JP34 #note host Escherichia coli DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 23-Jul-1999 ACCESSIONS B46324 REFERENCE A46324 !$#authors Adhin, M.R.; Hirashima, A.; Van Duin, J. !$#journal Virology (1989) 170:238-242 !$#title Nucleotide sequence from the ssRNA bacteriophage JP34 !1resolves the discrepancy between serological and biophysical !1classification. !$#cross-references MUID:89243181; PMID:2718383 !$#accession B46324 !'##molecule_type genomic RNA !'##residues 1-63 ##label ADH !'##cross-references GB:J04343; NID:g215076; PIDN:AAA72211.1; !1PID:g215078 CLASSIFICATION #superfamily phage GA lysis protein KEYWORDS host cell lysis SUMMARY #length 63 #molecular-weight 7335 #checksum 8796 SEQUENCE /// ENTRY ACBPMS #type complete TITLE maturation protein - phage MS2 ALTERNATE_NAMES assembly protein; gene A protein ORGANISM #formal_name phage MS2 DATE 24-Sep-1981 #sequence_revision 24-Sep-1981 #text_change 23-Jul-1999 ACCESSIONS A93176; A92214; A04221 REFERENCE A93176 !$#authors Fiers, W.; Contreras, R.; Duerinck, F.; Haegeman, G.; !1Merregaert, J.; Min Jou, W.; Raeymakers, A.; Volckaert, G.; !1Ysebaert, M.; Vandekerckhove, J.; Nolf, F.; van Montagu, M. !$#journal Nature (1975) 256:273-278 !$#title A-protein gene of bacteriophage MS2. !$#cross-references MUID:75194432; PMID:806810 !$#accession A93176 !'##molecule_type genomic RNA !'##residues 1-393 ##label FIE !'##cross-references GB:V00642; GB:J02467; NID:g15081; PIDN:CAA23988.1; !1PID:g579114; GB:M24961; NID:g215232; PID:g215233 REFERENCE A93179 !$#authors Fiers, W.; Contreras, R.; Duerinck, F.; Haegeman, G.; !1Iserentant, D.; Merregaert, J.; Min Jou, W.; Molemans, F.; !1Raeymaekers, A.; van den Berghe, A.; Volckaert, G.; !1Ysebaert, M. !$#journal Nature (1976) 260:500-507 !$#title Complete nucleotide sequence of bacteriophage MS2 RNA: !1primary and secondary structure of the replicase gene. !$#cross-references MUID:76174431; PMID:1264203 !$#contents annotation; sequence of complete genome reported REFERENCE A92214 !$#authors Vandekerckhove, J.S.; Van Montagu, M.C. !$#journal J. Biol. Chem. (1977) 252:7773-7782 !$#title Sequence of the A-protein of coliphage MS2. III. Isolation !1and sequence determination of thermolytic peptides and !1soluble cyanogen bromide fragments: alignment of 363 amino !1acid residues of a total of 393. !$#cross-references MUID:78026528; PMID:914838 !$#accession A92214 !'##molecule_type protein !'##residues 1-393 ##label VAN REFERENCE A92213 !$#authors Vandekerckhove, J.S.; Gielen, J.G.; Van Montagu, M.C. !$#journal J. Biol. Chem. (1977) 252:7761-7772 !$#title Sequence of the A-protein of coliphage MS2. II. Isolation !1and sequence determination of chymotryptic peptides. !$#cross-references MUID:78026527; PMID:914837 !$#contents annotation; sequences of chymotryptic peptides REFERENCE A92212 !$#authors Nolf, F.A.; Vandekerckhove, J.S.; Lenaerts, A.K.; Van !1Montagu, M.C. !$#journal J. Biol. Chem. (1977) 252:7752-7760 !$#title Sequence of the A-protein of coliphage MS2. I. Isolation of !1A-protein, determination of the NH-2 and COOH-terminal !1sequences, isolation and amino acid sequence of the tryptic !1peptides. !$#cross-references MUID:78026526; PMID:914836 !$#contents annotation; sequences of amino-terminal, carboxyl-terminal, !1and tryptic peptides GENETICS !$#map_position 3.64-36.65 !$#start_codon GUG CLASSIFICATION #superfamily phage maturation protein KEYWORDS phage maturation FEATURE !$1 #modified_site N-formylmethionine (partial) #status !8experimental SUMMARY #length 393 #molecular-weight 43983 #checksum 8923 SEQUENCE /// ENTRY ACBPMG #type complete TITLE maturation protein - phage GA ALTERNATE_NAMES assembly protein ORGANISM #formal_name phage GA #note host Escherichia coli DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 16-Jun-2000 ACCESSIONS JS0009 REFERENCE A92000 !$#authors Inokuchi, Y.; Takahashi, R.; Hirose, T.; Inayama, S.; !1Jacobson, A.B.; Hirashima, A. !$#journal J. Biochem. (1986) 99:1169-1180 !$#title The complete nucleotide sequence of the group II RNA !1coliphage GA. !$#cross-references MUID:86223910; PMID:3711059 !$#accession JS0009 !'##molecule_type genomic RNA !'##residues 1-390 ##label INO !'##cross-references GB:D10027; GB:D00046; GB:X03869; NID:g217784; !1PIDN:BAA00917.1; PID:g217785; NID:g15076; PID:g15077 COMMENT Bacteriophage GA is a group II RNA coliphage. CLASSIFICATION #superfamily phage maturation protein KEYWORDS phage maturation SUMMARY #length 390 #molecular-weight 44384 #checksum 4330 SEQUENCE /// ENTRY VCBPF2 #type complete TITLE coat protein - phage f2 ORGANISM #formal_name phage f2 DATE 29-Jul-1981 #sequence_revision 29-Jul-1981 #text_change 30-Sep-1993 ACCESSIONS A04222 REFERENCE A92031 !$#authors Weber, K.; Konigsberg, W. !$#journal J. Biol. Chem. (1967) 242:3563-3578 !$#title Amino acid sequence of the f-2 coat protein. !$#accession A04222 !'##molecule_type protein !'##residues 1-129 ##label WEB CLASSIFICATION #superfamily phage GA coat protein KEYWORDS coat protein SUMMARY #length 129 #molecular-weight 13709 #checksum 4020 SEQUENCE /// ENTRY VCBPM2 #type complete TITLE coat protein [validated] - phage MS2 ORGANISM #formal_name phage MS2 DATE 31-Dec-1991 #sequence_revision 23-Oct-1998 #text_change 19-Jan-2001 ACCESSIONS B04222; A04222 REFERENCE A93163 !$#authors Min Jou, W.; Haegeman, G.; Ysebaert, M.; Fiers, W. !$#journal Nature (1972) 237:82-88 !$#title Nucleotide sequence of the gene coding for the bacteriophage !1MS2 coat protein. !$#cross-references MUID:72195690; PMID:4555447 !$#accession B04222 !'##molecule_type mRNA !'##residues 1-130 ##label MIN !'##cross-references GB:V00642; GB:J02467; NID:g15081; PIDN:CAA23989.1; !1PID:g15083; GB:M24961; NID:g215232; PIDN:AAA32260.1; !1PID:g215234 !'##note translation of initiator Met is not shown REFERENCE A93179 !$#authors Fiers, W.; Contreras, R.; Duerinck, F.; Haegeman, G.; !1Iserentant, D.; Merregaert, J.; Min Jou, W.; Molemans, F.; !1Raeymaekers, A.; van den Berghe, A.; Volckaert, G.; !1Ysebaert, M. !$#journal Nature (1976) 260:500-507 !$#title Complete nucleotide sequence of bacteriophage MS2 RNA: !1primary and secondary structure of the replicase gene. !$#cross-references MUID:76174431; PMID:1264203 !$#contents annotation; sequence of complete genome reported REFERENCE A51875 !$#authors Valegard, K.; Liljas, L. !$#submission submitted to the Brookhaven Protein Data Bank, May 1991 !$#cross-references PDB:1MS2 !$#contents annotation; X-ray crystallography, 3.3 angstroms, residues !12-130 REFERENCE A30641 !$#authors Valegard, K.; Liljas, L.; Fridborg, K.; Unge, T. !$#journal Nature (1990) 345:36-41 !$#title The three-dimensional structure of the bacterial virus MS2. !$#cross-references MUID:90231453; PMID:2330049 !$#contents annotation; X-ray crystallography, 3.3 angstroms REFERENCE A67225 !$#authors Valegard, K.; Liljas, L. !$#submission submitted to the Brookhaven Protein Data Bank, August 1994 !$#cross-references PDB:2MS2 !$#contents annotation; X-ray crystallography, 2.8 angstroms, residues !12-130 REFERENCE A67370 !$#authors Valegard, K.; Vandenworm, S.; Liljas, L. !$#submission submitted to the Brookhaven Protein Data Bank, September !11996 !$#cross-references PDB:1ZDH !$#contents annotation; X-ray crystallography, 2.7 angstroms, residues !12-130, with RNA REFERENCE A67379 !$#authors Valegard, K.; Vandenworm, S.; Liljas, L. !$#submission submitted to the Brookhaven Protein Data Bank, September !11996 !$#cross-references PDB:1ZDI !$#contents annotation; X-ray crystallography, 2.7 angstroms, residues !12-130 REFERENCE A30642 !$#authors Valegard, K.; Murray, J.B.; Stockley, P.G.; Stonehouse, !1N.J.; Liljas, L. !$#journal Nature (1994) 371:623-626 !$#title Crystal structure of an RNA bacteriophage coat !1protein-operator complex. !$#cross-references MUID:95021717; PMID:7523953 !$#contents annotation; X-ray crystallography, 3.0 angstroms REFERENCE A30643 !$#authors Golmohammadi, R.; Valegard, K.; Fridborg, K.; Liljas, L. !$#journal J. Mol. Biol. (1993) 234:620-639 !$#title The refined structure of bacteriophage MS2 at 2.8 Angstroms !1resolution. !$#cross-references MUID:94076340; PMID:8254664 !$#contents annotation; X-ray crystallography, 2.8 angstroms CLASSIFICATION #superfamily phage GA coat protein KEYWORDS coat protein; RNA binding FEATURE !$2-130 #product coat protein #status experimental #label MAT SUMMARY #length 130 #molecular-weight 13860 #checksum 5760 SEQUENCE /// ENTRY VCBPR7 #type complete TITLE coat protein - phage R17 ALTERNATE_NAMES RNA-protein ORGANISM #formal_name phage R17 DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 19-Apr-1996 ACCESSIONS C04222; S50819; A04222 REFERENCE A90551 !$#authors Weber, K. !$#journal Biochemistry (1967) 6:3144-3154 !$#title Amino acid sequence studies on the tryptic peptides of the !1coat protein of the bacteriophage R17. !$#cross-references MUID:68042042; PMID:6056980 !$#accession C04222 !'##molecule_type protein !'##residues 1-129 ##label WEB REFERENCE S50819 !$#authors Willis, M.C.; LeCuyer, K.A.; Meisenheimer, K.M.; Uhlenbeck, !1O.C.; Koch, T.H. !$#journal Nucleic Acids Res. (1994) 22:4947-4952 !$#title An RNA-protein contact determined by 5-bromouridine !1substitution, photocrosslinking and sequencing. !$#cross-references MUID:95098610; PMID:7800485 !$#accession S50819 !'##status preliminary !'##molecule_type protein !'##residues 84-113 ##label WIL CLASSIFICATION #superfamily phage GA coat protein KEYWORDS coat protein SUMMARY #length 129 #molecular-weight 13727 #checksum 4051 SEQUENCE /// ENTRY VCBPZR #type complete TITLE coat protein - phage ZR ORGANISM #formal_name phage ZR DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 30-Sep-1993 ACCESSIONS D04222; A04222 REFERENCE A91924 !$#authors Nishihara, T.; Nozu, Y.; Okada, Y. !$#journal J. Biochem. (1970) 67:403-413 !$#title Amino acid sequence of the coat protein of the RNA phage ZR. !$#cross-references MUID:70216643; PMID:4912732 !$#accession D04222 !'##molecule_type protein !'##residues 1-129 ##label NIS CLASSIFICATION #superfamily phage GA coat protein KEYWORDS coat protein SUMMARY #length 129 #molecular-weight 13727 #checksum 4051 SEQUENCE /// ENTRY VCBPFR #type complete TITLE coat protein - phage fr ORGANISM #formal_name phage fr DATE 24-Apr-1984 #sequence_revision 13-Mar-1997 #text_change 23-Jul-1999 ACCESSIONS S08018; S13143; A04223; A93115; A90722; JN0375; JT0015 REFERENCE S08017 !$#authors Adhin, M.R.; Avots, A.; Berzin, V.; Overbeek, G.P.; van !1Duin, J. !$#submission submitted to the EMBL Data Library, April 1989 !$#description Complete nucleotide sequence of RNA bacteriophage fr. !$#accession S08018 !'##molecule_type genomic RNA !'##residues 1-130 ##label ADH !'##cross-references EMBL:X15031; NID:g15071; PIDN:CAA33136.1; !1PID:g15073 REFERENCE S13075 !$#authors Adhin, M.R.; Avots, A.; Berzin, V.; Overbeek, G.P.; van !1Duin, J. !$#journal Biochim. Biophys. Acta (1990) 1050:104-109 !$#title Complete nucleotide sequence of the group I RNA !1bacteriophage fr. !$#cross-references MUID:91002624; PMID:2207135 !$#accession S13143 !'##molecule_type genomic RNA !'##residues 2-130 ##label ADW !'##cross-references GB:X15031; NID:g15071; PIDN:CAA33136.1; PID:g15073 REFERENCE A93115 !$#authors Wittmann-Liebold, B.; Wittmann, H.G. !$#journal Mol. Gen. Genet. (1967) 100:358-363 !$#title Coat proteins of strains of two RNA viruses: comparison of !1their amino acid sequences. !$#cross-references MUID:68199043; PMID:5584177 !$#accession A04223 !'##molecule_type protein !'##residues 2-11,'ND',14-98,'B',100-116,'IAPN',121-130 ##label WIT !$#accession A93115 !'##molecule_type protein !'##residues 2-98,'B',100-130 ##label WI2 REFERENCE A90722 !$#authors Berzin, V.M.; Avots, A.J.; Jansone, I.V.; Tsimanis, A.J. !$#journal Bioorg. Khim. (1986) 12:149-152 !$#title The primary structure of a fragment of the phage fr cDNA. !$#cross-references MUID:86130773; PMID:3753874 !$#accession A90722 !'##molecule_type mRNA !'##residues 2-98,'B',100-130 ##label BER REFERENCE JN0375 !$#authors Berzin, B.M.; Gribanov, B.A.; Tsielens, I.A.; Yansone, H.B.; !1Gren, A.Y. !$#journal Bioorg. Khim. (1981) 7:306-307 !$#title Structure of regulator part of phage fr replicase gene. !$#accession JN0375 !'##molecule_type genomic RNA !'##residues 126-130 ##label BE2 GENETICS !$#gene BO CLASSIFICATION #superfamily phage GA coat protein KEYWORDS coat protein SUMMARY #length 130 #molecular-weight 13867 #checksum 4923 SEQUENCE /// ENTRY VCBPGA #type complete TITLE coat protein - phage GA ORGANISM #formal_name phage GA #note host Escherichia coli DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 16-Jun-2000 ACCESSIONS A29178 REFERENCE A92000 !$#authors Inokuchi, Y.; Takahashi, R.; Hirose, T.; Inayama, S.; !1Jacobson, A.B.; Hirashima, A. !$#journal J. Biochem. (1986) 99:1169-1180 !$#title The complete nucleotide sequence of the group II RNA !1coliphage GA. !$#cross-references MUID:86223910; PMID:3711059 !$#accession A29178 !'##molecule_type genomic RNA !'##residues 1-130 ##label INO !'##cross-references GB:D10027; GB:D00046; GB:X03869; NID:g217784; !1PIDN:BAA00918.1; PID:g217786; NID:g15076; PID:g15078 CLASSIFICATION #superfamily phage GA coat protein KEYWORDS coat protein SUMMARY #length 130 #molecular-weight 13682 #checksum 4751 SEQUENCE /// ENTRY A46324 #type complete TITLE coat protein - phage JP34 ORGANISM #formal_name phage JP34 #note host Escherichia coli DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 23-Jul-1999 ACCESSIONS A46324 REFERENCE A46324 !$#authors Adhin, M.R.; Hirashima, A.; Van Duin, J. !$#journal Virology (1989) 170:238-242 !$#title Nucleotide sequence from the ssRNA bacteriophage JP34 !1resolves the discrepancy between serological and biophysical !1classification. !$#cross-references MUID:89243181; PMID:2718383 !$#accession A46324 !'##molecule_type genomic RNA !'##residues 1-130 ##label ADH !'##cross-references GB:J04343; NID:g215076; PIDN:AAA72210.1; !1PID:g215077 CLASSIFICATION #superfamily phage GA coat protein KEYWORDS coat protein SUMMARY #length 130 #molecular-weight 13741 #checksum 4943 SEQUENCE /// ENTRY VCBPQB #type complete TITLE coat protein - phage Q-beta ORGANISM #formal_name phage Q-beta DATE 29-Jul-1981 #sequence_revision 24-Sep-1981 #text_change 31-Dec-1993 ACCESSIONS A92240; A92221; A92088; A04224 REFERENCE A92240 !$#authors Escarmis, C.; Sastry, P.A.; Billeter, M.A. !$#journal J. Biol. Chem. (1978) 253:8390-8399 !$#title Determination of the first half of the coat protein cistron !1of bacteriophage Qbeta as an application of a mapping !1procedure for RNA fragments. !$#cross-references MUID:79048469; PMID:361741 !$#accession A92240 !'##molecule_type mRNA !'##residues 1-80 ##label ESC REFERENCE A92221 !$#authors Stoll, E.; Wilson, K.J.; Reiser, J.; Weissmann, C. !$#journal J. Biol. Chem. (1977) 252:990-993 !$#title Revised amino acid sequence of Qbeta coat protein between !1positions 1 and 60. !$#cross-references MUID:77118576; PMID:838709 !$#accession A92221 !'##molecule_type protein !'##residues 1-60 ##label STO REFERENCE A92088 !$#authors Maita, T.; Konigsberg, W. !$#journal J. Biol. Chem. (1971) 246:5003-5024 !$#title The amino acid sequence of the Qbeta coat protein. !$#cross-references MUID:71288580; PMID:5570434 !$#accession A92088 !'##molecule_type protein !'##residues 1-21,'D',23-55,57-132 ##label MAI CLASSIFICATION #superfamily phage GA coat protein SUMMARY #length 132 #molecular-weight 14123 #checksum 9083 SEQUENCE /// ENTRY VCBPP1 #type complete TITLE coat protein - phage PRR1 ORGANISM #formal_name phage PRR1 DATE 30-Nov-1979 #sequence_revision 30-Nov-1979 #text_change 31-Dec-1993 ACCESSIONS A04225 REFERENCE A04225 !$#authors Dhaese, P.; Vandekerckhove, J.S.; Van Montagu, M.C. !$#journal Eur. J. Biochem. (1979) 94:375-386 !$#title The primary structure of the coat protein of the !1broad-host-range RNA bacteriophage PRR1. !$#cross-references MUID:79148387; PMID:107028 !$#accession A04225 !'##molecule_type protein !'##residues 1-131 ##label DHA CLASSIFICATION #superfamily phage GA coat protein SUMMARY #length 131 #molecular-weight 14535 #checksum 9091 SEQUENCE /// ENTRY VCBPFD #type complete TITLE coat protein B precursor - phage fd ORGANISM #formal_name phage fd DATE 18-Dec-1981 #sequence_revision 18-Dec-1981 #text_change 23-Jul-1999 ACCESSIONS A04226; B04226; C04226 REFERENCE A93690 !$#authors Beck, E.; Sommer, R.; Auerswald, E.A.; Kurz, C.; Zink, B.; !1Osterburg, G.; Schaller, H.; Sugimoto, K.; Sugisaki, H.; !1Okamoto, T.; Takanami, M. !$#journal Nucleic Acids Res. (1978) 5:4495-4503 !$#title Nucleotide sequence of bacteriophage fd DNA. !$#cross-references MUID:79136480; PMID:745987 !$#accession A04226 !'##molecule_type DNA !'##residues 1-73 ##label BEC !'##cross-references GB:V00602; GB:J02451; GB:M10731; GB:M10767; !1GB:M21666; GB:M21667; GB:M21668; GB:M21669; GB:M21670; !1GB:M25198; NID:g14931; PIDN:CAA23850.1; PID:g14937 !'##experimental_source strain 478, Heidelberg REFERENCE A91643 !$#authors Asbeck, F.; Beyreuther, K.; Kohler, H.; von Wettstein, G.; !1Braunitzer, G. !$#journal Hoppe-Seyler's Z. Physiol. Chem. (1969) 350:1047-1066 !$#title Die Konstitution des Huellproteins des Phagen fd. !$#cross-references MUID:70028989; PMID:5349375 !$#accession B04226 !'##molecule_type DNA !'##residues 24-49,'X',51-73 ##label ASB !'##experimental_source strain 478, Heidelberg REFERENCE A92951 !$#authors Nakashima, Y.; Konigsberg, W. !$#journal J. Mol. Biol. (1974) 88:598-600 !$#title Reinvestigation of a region of the fd bacteriophage coat !1protein sequence. !$#cross-references MUID:75097503; PMID:4449122 !$#accession C04226 !'##molecule_type DNA !'##residues 24-73 ##label NAK COMMENT Coat protein B is the major coat protein of the virion. GENETICS !$#gene VIII CLASSIFICATION #superfamily filamentous phage coat protein B KEYWORDS coat protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-73 #product coat protein B #status predicted #label CPB SUMMARY #length 73 #molecular-weight 7626 #checksum 5504 SEQUENCE /// ENTRY VCBPM3 #type complete TITLE coat protein B precursor - phage M13 ORGANISM #formal_name phage M13 DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 23-Jul-1999 ACCESSIONS D04226; A04226 REFERENCE A91470 !$#authors van Wezenbeek, P.M.G.F.; Hulsebos, T.J.M.; Schoenmakers, !1J.G.G. !$#journal Gene (1980) 11:129-148 !$#title Nucleotide sequence of the filamentous bacteriophage M13 DNA !1genome: comparison with phage fd. !$#cross-references MUID:81067903; PMID:6254849 !$#accession D04226 !'##molecule_type DNA !'##residues 1-73 ##label VAN !'##cross-references GB:V00604; GB:J02461; GB:M10377; NID:g14959; !1PIDN:CAA23861.1; PID:g14965 COMMENT Coat protein B is the major coat protein of the virion. !1There are about 2,700 copies of this protein in the coat of !1bacteriophage M13. They are arranged in a helix around the !1DNA. GENETICS !$#gene VIII CLASSIFICATION #superfamily filamentous phage coat protein B KEYWORDS coat protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-73 #product coat protein B #status predicted #label CPB SUMMARY #length 73 #molecular-weight 7625 #checksum 5854 SEQUENCE /// ENTRY VCBPF1 #type complete TITLE coat protein B precursor - phage f1 ORGANISM #formal_name phage f1 DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 23-Jul-1999 ACCESSIONS E04226; F04226; G04226; A04226 REFERENCE A91490 !$#authors Beck, E.; Zink, B. !$#journal Gene (1981) 16:35-58 !$#title Nucleotide sequence and genome organisation of filamentous !1bacteriophages f1 and fd. !$#cross-references MUID:82211801; PMID:6282703 !$#accession E04226 !'##molecule_type DNA !'##residues 1-73 ##label BEC !'##cross-references GB:V00606; GB:J02449; GB:M10881; NID:g14974; !1PIDN:CAA23871.1; PID:g14979 REFERENCE A92980 !$#authors Hill, D.F.; Petersen, G.B. !$#journal J. Virol. (1980) 34:40-50 !$#title Nucleotide sequences in bacteriophage f1 DNA: nucleotide !1sequence of genes V, VII, and VIII. !$#cross-references MUID:80185134; PMID:7373712 !$#accession F04226 !'##molecule_type DNA !'##residues 1-73 ##label HIL !'##cross-references GB:J02450; NID:g166212; PIDN:AAA32220.1; !1PID:g166214 REFERENCE A92201 !$#authors Bailey, G.S.; Gillett, D.; Hill, D.F.; Petersen, G.B. !$#journal J. Biol. Chem. (1977) 252:2218-2225 !$#title Automated sequencing of insoluble peptides using detergent. !1Bacteriophage fl coat protein. !$#cross-references MUID:77140968; PMID:321454 !$#accession G04226 !'##molecule_type protein !'##residues 24-73 ##label BAI COMMENT Coat protein B is the major coat protein of the virion. GENETICS !$#gene VIII CLASSIFICATION #superfamily filamentous phage coat protein B KEYWORDS coat protein FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-73 #product coat protein B #status experimental #label !8CPB SUMMARY #length 73 #molecular-weight 7626 #checksum 5504 SEQUENCE /// ENTRY VCBPZ2 #type complete TITLE coat protein B - phage ZJ-2 ORGANISM #formal_name phage ZJ-2 DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 31-Dec-1993 ACCESSIONS H04226; A04226 REFERENCE A90260 !$#authors Snell, D.T.; Offord, R.E. !$#journal Biochem. J. (1972) 127:167-178 !$#title The amino acid sequence of the B-protein of bacteriophage !1ZJ-2. !$#cross-references MUID:73009813; PMID:5073740 !$#accession H04226 !'##molecule_type DNA !'##residues 1-50 ##label SNE COMMENT Coat protein B is the major coat protein of the virion. GENETICS !$#gene VIII CLASSIFICATION #superfamily filamentous phage coat protein B KEYWORDS coat protein SUMMARY #length 50 #molecular-weight 5209 #checksum 6001 SEQUENCE /// ENTRY VCBPIF #type complete TITLE coat protein - phage If1 ORGANISM #formal_name phage If1 DATE 29-Jul-1981 #sequence_revision 29-Jul-1981 #text_change 30-Sep-1993 ACCESSIONS A04227 REFERENCE A92326 !$#authors Nakashima, Y.; Frangione, B.; Wiseman, R.L.; Konigsberg, !1W.H. !$#journal J. Biol. Chem. (1981) 256:5792-5797 !$#title Primary structure of the major coat protein of the !1filamentous bacterial viruses, If1 and Ike. !$#cross-references MUID:81215498; PMID:7240173 !$#accession A04227 !'##molecule_type protein !'##residues 1-51 ##label NAK CLASSIFICATION #superfamily filamentous phage coat protein B SUMMARY #length 51 #molecular-weight 5293 #checksum 1631 SEQUENCE /// ENTRY VCBPIK #type complete TITLE coat protein B precursor - phage IKe ALTERNATE_NAMES gene VIII protein ORGANISM #formal_name phage IKe #note host Escherichia coli DATE 29-Jul-1981 #sequence_revision 28-May-1986 #text_change 28-Jul-2000 ACCESSIONS A92912; A92326; A04228 REFERENCE A92912 !$#authors Peeters, B.P.H.; Peters, R.M.; Schoenmakers, J.G.G.; !1Konings, R.N.H. !$#journal J. Mol. Biol. (1985) 181:27-39 !$#title Nucleotide sequence and genetic organization of the genome !1of the N-specific filamentous bacteriophage IKe. Comparison !1with the genome of the F-specific filamentous phages M13, fd !1and f1. !$#cross-references MUID:85160831; PMID:3981635 !$#accession A92912 !'##molecule_type DNA !'##residues 1-82 ##label PEE !'##cross-references GB:K02750; NID:g14942; PIDN:CAA26072.1; PID:g14948 REFERENCE A92326 !$#authors Nakashima, Y.; Frangione, B.; Wiseman, R.L.; Konigsberg, !1W.H. !$#journal J. Biol. Chem. (1981) 256:5792-5797 !$#title Primary structure of the major coat protein of the !1filamentous bacterial viruses, If1 and Ike. !$#cross-references MUID:81215498; PMID:7240173 !$#accession A92326 !'##molecule_type protein !'##residues 30-82 ##label NAK !'##note coat protein B is the major coat protein of the virion GENETICS !$#gene VIII CLASSIFICATION #superfamily filamentous phage coat protein B KEYWORDS capsid protein FEATURE !$1-29 #domain signal sequence #status predicted #label SIG\ !$30-82 #product coat protein B #status experimental #label !8CPB SUMMARY #length 82 #molecular-weight 8570 #checksum 9241 SEQUENCE /// ENTRY VCBPPF #type complete TITLE coat protein - phage Pf1 ORGANISM #formal_name phage Pf1 DATE 24-Sep-1981 #sequence_revision 24-Sep-1981 #text_change 31-Dec-1993 ACCESSIONS A04229 REFERENCE A04229 !$#authors Nakashima, Y.; Wiseman, R.L.; Konigsberg, W.; Marvin, D.A. !$#journal Nature (1975) 253:68-71 !$#title Primary structure and sidechain interactions of PFL !1filamentous bacterial virus coat protein. !$#cross-references MUID:75082355; PMID:1110754 !$#accession A04229 !'##molecule_type protein !'##residues 1-46 ##label NAK COMMENT Pf1 is a filamentous bacteriophage with single-stranded DNA. CLASSIFICATION #superfamily filamentous phage coat protein B SUMMARY #length 46 #molecular-weight 4608 #checksum 1520 SEQUENCE /// ENTRY VCBPXF #type complete TITLE coat protein - phage Xf ORGANISM #formal_name phage Xf DATE 31-May-1979 #sequence_revision 23-Oct-1981 #text_change 15-Nov-1996 ACCESSIONS A04230 REFERENCE A04230 !$#authors Frangione, B.; Nakashima, Y.; Konigsberg, W.; Wiseman, R.L. !$#journal FEBS Lett. (1978) 96:381-384 !$#title The amino acid sequence of the major coat protein subunit of !1the filamentous virus Xf. !$#cross-references MUID:79086258; PMID:729805 !$#accession A04230 !'##molecule_type protein !'##residues 1-44 ##label FRA COMMENT Xf differs from other filamentous bacteriophages in that its !1host is Xanthomonas oryzae. CLASSIFICATION #superfamily filamentous phage coat protein B KEYWORDS acetylated amino end FEATURE !$1 #modified_site acetylated amino end (Ser) #status !8experimental SUMMARY #length 44 #molecular-weight 4342 #checksum 6148 SEQUENCE /// ENTRY VCBPP3 #type complete TITLE major coat protein - phage Pf3 ORGANISM #formal_name phage Pf3 #note host Pseudomonas aeruginosa DATE 15-Nov-1984 #sequence_revision 15-Nov-1984 #text_change 24-Sep-1999 ACCESSIONS A04231 REFERENCE A94693 !$#authors Luiten, R.G.M.; Putterman, D.G.; Schoenmakers, J.G.G.; !1Konings, R.N.H.; Day, L.A. !$#journal J. Virol. (1985) 56:268-276 !$#title Nucleotide sequence of the genome of Pf3, an IncP-1 !1plasmid-specific filamentous bacteriophage of Pseudomonas !1aeruginosa. !$#cross-references MUID:85293231; PMID:3928901 !$#accession A04231 !'##molecule_type DNA !'##residues 1-44 ##label LUI !'##cross-references GB:M11912; NID:g215371; PIDN:AAA88378.1; !1PID:g215373 !'##note most of this sequence was confirmed by amino acid analysis COMMENT Bacteriophage Pf3 is a class II filamentous phage. COMMENT The host is strain O harboring IncP1 plasmids. GENETICS !$#gene 44 CLASSIFICATION #superfamily filamentous phage coat protein B KEYWORDS capsid protein SUMMARY #length 44 #molecular-weight 4630 #checksum 4527 SEQUENCE /// ENTRY VCBPI3 #type complete TITLE minor coat protein - phage Pf3 ORGANISM #formal_name phage Pf3 #note host Pseudomonas aeruginosa DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 23-Jul-1999 ACCESSIONS A04232 REFERENCE A94693 !$#authors Luiten, R.G.M.; Putterman, D.G.; Schoenmakers, J.G.G.; !1Konings, R.N.H.; Day, L.A. !$#journal J. Virol. (1985) 56:268-276 !$#title Nucleotide sequence of the genome of Pf3, an IncP-1 !1plasmid-specific filamentous bacteriophage of Pseudomonas !1aeruginosa. !$#cross-references MUID:85293231; PMID:3928901 !$#accession A04232 !'##molecule_type DNA !'##residues 1-483 ##label LUI !'##cross-references GB:M11912; NID:g215371; PIDN:AAA88379.1; !1PID:g215374 COMMENT Bacteriophage Pf3 is a class II filamentous phage. COMMENT The host is strain O harboring IncP1 plasmids. GENETICS !$#gene 483 CLASSIFICATION #superfamily class II filamentous phage minor coat protein KEYWORDS capsid protein SUMMARY #length 483 #molecular-weight 52196 #checksum 2873 SEQUENCE /// ENTRY S07502 #type complete TITLE gene 5.9 protein - phage T3 ORGANISM #formal_name phage T3 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS S07502 REFERENCE S07500 !$#authors Beck, P.J.; Gonzalez, S.; Ward, C.L.; Molineux, I.J. !$#journal J. Mol. Biol. (1989) 210:687-701 !$#title Sequence of bacteriophage T3 DNA from gene 2.5 through gene !19. !$#cross-references MUID:90133923; PMID:2614843 !$#accession S07502 !'##molecule_type DNA !'##residues 1-52 ##label BEC !'##cross-references EMBL:X17255; NID:g15682; PIDN:CAA35146.1; !1PID:g15708 GENETICS !$#gene 5.9 CLASSIFICATION #superfamily gene 5.9 protein SUMMARY #length 52 #molecular-weight 6063 #checksum 4117 SEQUENCE /// ENTRY S42315 #type complete TITLE gene 5.9 protein - phage T7 ORGANISM #formal_name phage T7 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S42315; A00780; S43608 REFERENCE S42315 !$#authors Dunn, J.J. !$#submission submitted to the EMBL Data Library, October 1993 !$#accession S42315 !'##molecule_type DNA !'##residues 1-52 ##label DUN !'##cross-references EMBL:V01146; NID:g431187; PID:g431191 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession A00780 !'##status significant sequence differences !'##molecule_type DNA !'##note due to a frameshift error genes 5.9 and 6 were concatenated !1into a single reading frame REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S43608 !'##status significant sequence differences !'##molecule_type DNA !'##cross-references EMBL:V01146 !'##note the authors did not translate the codon for residue 1 !'##note due to a frameshift error genes 5.9 and 6 were concatenated !1into a single reading frame GENETICS !$#gene 5.9 !$#map_position 43.47-46.08 CLASSIFICATION #superfamily gene 5.9 protein SUMMARY #length 52 #molecular-weight 6045 #checksum 4053 SEQUENCE /// ENTRY Z9BP33 #type complete TITLE gene 93 protein - phage Pf3 ORGANISM #formal_name phage Pf3 #note host Pseudomonas aeruginosa DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 24-Sep-1999 ACCESSIONS A04233 REFERENCE A94693 !$#authors Luiten, R.G.M.; Putterman, D.G.; Schoenmakers, J.G.G.; !1Konings, R.N.H.; Day, L.A. !$#journal J. Virol. (1985) 56:268-276 !$#title Nucleotide sequence of the genome of Pf3, an IncP-1 !1plasmid-specific filamentous bacteriophage of Pseudomonas !1aeruginosa. !$#cross-references MUID:85293231; PMID:3928901 !$#accession A04233 !'##molecule_type DNA !'##residues 1-93 ##label LUI !'##cross-references GB:M11912; NID:g215371; PIDN:AAA88380.1; !1PID:g1196711 COMMENT Bacteriophage Pf3 is a class II filamentous phage. COMMENT The host is strain O harboring IncP1 plasmids. GENETICS !$#gene 93 CLASSIFICATION #superfamily class II filamentous phage gene 93 protein SUMMARY #length 93 #molecular-weight 9640 #checksum 8709 SEQUENCE /// ENTRY Z3BP13 #type complete TITLE gene 301 protein - phage Pf3 ORGANISM #formal_name phage Pf3 #note host Pseudomonas aeruginosa DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 23-Jul-1999 ACCESSIONS A04234 REFERENCE A94693 !$#authors Luiten, R.G.M.; Putterman, D.G.; Schoenmakers, J.G.G.; !1Konings, R.N.H.; Day, L.A. !$#journal J. Virol. (1985) 56:268-276 !$#title Nucleotide sequence of the genome of Pf3, an IncP-1 !1plasmid-specific filamentous bacteriophage of Pseudomonas !1aeruginosa. !$#cross-references MUID:85293231; PMID:3928901 !$#accession A04234 !'##molecule_type DNA !'##residues 1-301 ##label LUI !'##cross-references GB:M11912; NID:g215371; PIDN:AAA88382.1; !1PID:g215376 COMMENT Bacteriophage Pf3 is a class II filamentous phage. COMMENT The host is strain O harboring IncP1 plasmids. GENETICS !$#gene 301 CLASSIFICATION #superfamily class II filamentous phage gene 301 protein SUMMARY #length 301 #molecular-weight 32731 #checksum 5471 SEQUENCE /// ENTRY Z2BP73 #type complete TITLE gene 278 protein - phage Pf3 ORGANISM #formal_name phage Pf3 #note host Pseudomonas aeruginosa DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 23-Jul-1999 ACCESSIONS A04235 REFERENCE A94693 !$#authors Luiten, R.G.M.; Putterman, D.G.; Schoenmakers, J.G.G.; !1Konings, R.N.H.; Day, L.A. !$#journal J. Virol. (1985) 56:268-276 !$#title Nucleotide sequence of the genome of Pf3, an IncP-1 !1plasmid-specific filamentous bacteriophage of Pseudomonas !1aeruginosa. !$#cross-references MUID:85293231; PMID:3928901 !$#accession A04235 !'##molecule_type DNA !'##residues 1-278 ##label LUI !'##cross-references GB:M11912; NID:g215371; PIDN:AAA88383.1; !1PID:g215377 COMMENT Bacteriophage Pf3 is a class II filamentous phage. COMMENT The host is strain O harboring IncP1 plasmids. GENETICS !$#gene 278 CLASSIFICATION #superfamily class II filamentous phage gene 278 protein SUMMARY #length 278 #molecular-weight 32134 #checksum 3794 SEQUENCE /// ENTRY Z7BP13 #type complete TITLE gene 71 protein - phage Pf3 ORGANISM #formal_name phage Pf3 #note host Pseudomonas aeruginosa DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 23-Jul-1999 ACCESSIONS A04236 REFERENCE A94693 !$#authors Luiten, R.G.M.; Putterman, D.G.; Schoenmakers, J.G.G.; !1Konings, R.N.H.; Day, L.A. !$#journal J. Virol. (1985) 56:268-276 !$#title Nucleotide sequence of the genome of Pf3, an IncP-1 !1plasmid-specific filamentous bacteriophage of Pseudomonas !1aeruginosa. !$#cross-references MUID:85293231; PMID:3928901 !$#accession A04236 !'##molecule_type DNA !'##residues 1-71 ##label LUI !'##cross-references GB:M11912; NID:g215371; PIDN:AAA88384.1; !1PID:g215378 COMMENT Bacteriophage Pf3 is a class II filamentous phage. COMMENT The host is strain O harboring IncP1 plasmids. GENETICS !$#gene 71 CLASSIFICATION #superfamily class II filamentous phage gene 71 protein SUMMARY #length 71 #molecular-weight 7974 #checksum 2923 SEQUENCE /// ENTRY Z5BP83 #type complete TITLE gene 58 protein - phage Pf3 ORGANISM #formal_name phage Pf3 #note host Pseudomonas aeruginosa DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 24-Sep-1999 ACCESSIONS A04237 REFERENCE A94693 !$#authors Luiten, R.G.M.; Putterman, D.G.; Schoenmakers, J.G.G.; !1Konings, R.N.H.; Day, L.A. !$#journal J. Virol. (1985) 56:268-276 !$#title Nucleotide sequence of the genome of Pf3, an IncP-1 !1plasmid-specific filamentous bacteriophage of Pseudomonas !1aeruginosa. !$#cross-references MUID:85293231; PMID:3928901 !$#accession A04237 !'##molecule_type DNA !'##residues 1-58 ##label LUI !'##cross-references GB:M11912; NID:g215371; PIDN:AAA88377.1; !1PID:g215372 COMMENT Bacteriophage Pf3 is a class II filamentous phage. COMMENT The host is strain O harboring IncP1 plasmids. GENETICS !$#gene 58 CLASSIFICATION #superfamily class II filamentous phage gene 58 protein SUMMARY #length 58 #molecular-weight 6446 #checksum 5476 SEQUENCE /// ENTRY VCBPP7 #type complete TITLE coat protein - phage PP7 ORGANISM #formal_name phage PP7 DATE 30-Sep-1980 #sequence_revision 30-Sep-1980 #text_change 31-Dec-1993 ACCESSIONS A04238 REFERENCE A04238 !$#authors Dhaese, P.; Lenaerts, A.; Gielen, J.; Van Montagu, M. !$#journal Biochem. Biophys. Res. Commun. (1980) 94:1394-1400 !$#title Complete amino acid sequence of the coat protein of the !1Pseudomonas aeruginosa RNA bacteriophage PP7. !$#cross-references MUID:80242064; PMID:6772187 !$#accession A04238 !'##molecule_type protein !'##residues 1-127 ##label DHA COMMENT Bacteriophage PP7 infects Pseudomonas aeruginosa PA01. CLASSIFICATION #superfamily phage PP7 coat protein SUMMARY #length 127 #molecular-weight 13890 #checksum 5157 SEQUENCE /// ENTRY VHBPF6 #type complete TITLE major nucleocapsid protein - phage phi-6 ALTERNATE_NAMES P8 protein ORGANISM #formal_name phage phi-6 #note host Pseudomonas phaseolicola DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 23-Jul-1999 ACCESSIONS A23368 REFERENCE A93017 !$#authors McGraw, T.; Mindich, L.; Frangione, B. !$#journal J. Virol. (1986) 58:142-151 !$#title Nucleotide sequence of the small double-stranded RNA segment !1of bacteriophage phi6: novel mechanism of natural !1translational control. !$#cross-references MUID:86144085; PMID:3754015 !$#accession A23368 !'##molecule_type genomic RNA !'##residues 1-149 ##label MCG !'##cross-references GB:M12921; NID:g215492; PIDN:AAA32358.1; !1PID:g215493 GENETICS !$#gene P8 !$#map_position segment S CLASSIFICATION #superfamily phage phi-6 nucleocapsid protein KEYWORDS nucleocapsid SUMMARY #length 149 #molecular-weight 16004 #checksum 6252 SEQUENCE /// ENTRY YHBPF6 #type complete TITLE morphogenetic protein - phage phi-6 ALTERNATE_NAMES P12 protein ORGANISM #formal_name phage phi-6 #note host Pseudomonas phaseolicola DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 23-Jul-1999 ACCESSIONS B23368 REFERENCE A93017 !$#authors McGraw, T.; Mindich, L.; Frangione, B. !$#journal J. Virol. (1986) 58:142-151 !$#title Nucleotide sequence of the small double-stranded RNA segment !1of bacteriophage phi6: novel mechanism of natural !1translational control. !$#cross-references MUID:86144085; PMID:3754015 !$#accession B23368 !'##molecule_type genomic RNA !'##residues 1-195 ##label MCG !'##cross-references GB:M12921; NID:g215492; PIDN:AAA32359.1; !1PID:g215494 GENETICS !$#gene P12 !$#map_position segment S CLASSIFICATION #superfamily phage phi-6 morphogenetic protein SUMMARY #length 195 #molecular-weight 20293 #checksum 9211 SEQUENCE /// ENTRY MNBPF6 #type complete TITLE major membrane protein - phage phi-6 ALTERNATE_NAMES P9 protein ORGANISM #formal_name phage phi-6 #note host Pseudomonas phaseolicola DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 23-Jul-1999 ACCESSIONS C23368 REFERENCE A93017 !$#authors McGraw, T.; Mindich, L.; Frangione, B. !$#journal J. Virol. (1986) 58:142-151 !$#title Nucleotide sequence of the small double-stranded RNA segment !1of bacteriophage phi6: novel mechanism of natural !1translational control. !$#cross-references MUID:86144085; PMID:3754015 !$#accession C23368 !'##molecule_type genomic RNA !'##residues 1-90 ##label MCG !'##cross-references GB:M12921; NID:g215492; PIDN:AAA32360.1; !1PID:g215495 GENETICS !$#gene P9 !$#map_position segment S CLASSIFICATION #superfamily phage phi-6 membrane protein KEYWORDS membrane protein SUMMARY #length 90 #molecular-weight 9613 #checksum 7695 SEQUENCE /// ENTRY YVBPF6 #type complete TITLE phage lysis protein - phage phi-6 ALTERNATE_NAMES P5 protein ORGANISM #formal_name phage phi-6 #note host Pseudomonas phaseolicola DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 30-Jun-1993 ACCESSIONS D23368 REFERENCE A93017 !$#authors McGraw, T.; Mindich, L.; Frangione, B. !$#journal J. Virol. (1986) 58:142-151 !$#title Nucleotide sequence of the small double-stranded RNA segment !1of bacteriophage phi6: novel mechanism of natural !1translational control. !$#cross-references MUID:86144085; PMID:3754015 !$#accession D23368 !'##molecule_type genomic RNA !'##residues 1-220 ##label MCG GENETICS !$#gene P5 !$#map_position segment S CLASSIFICATION #superfamily phage phi-6 lysis protein SUMMARY #length 220 #molecular-weight 24117 #checksum 9312 SEQUENCE /// ENTRY P7BPF6 #type complete TITLE P7 protein - phage phi-6 ORGANISM #formal_name phage phi-6 #note host Pseudomonas phaseolicola DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 23-Jul-1999 ACCESSIONS A29885 REFERENCE A93032 !$#authors Mindich, L.; Nemhauser, I.; Gottlieb, P.; Romantschuk, M.; !1Carton, J.; Frucht, S.; Strassman, J.; Bamford, D.H.; !1Kalkkinen, N. !$#journal J. Virol. (1988) 62:1180-1185 !$#title Nucleotide sequence of the large double-stranded RNA segment !1of bacteriophage phi-6: genes specifying the viral replicase !1and transcriptase. !$#cross-references MUID:88155752; PMID:3346944 !$#accession A29885 !'##molecule_type genomic RNA !'##residues 1-161 ##label MIN !'##cross-references GB:M17461; NID:g215480; PIDN:AAA32354.1; !1PID:g215481 COMMENT The genome of this phage consists of three segments of !1double-stranded RNA; this protein is coded by the largest !1segment (L). GENETICS !$#gene 7 !$#map_position segment L CLASSIFICATION #superfamily phage phi-6 P7 protein KEYWORDS early protein SUMMARY #length 161 #molecular-weight 17300 #checksum 3968 SEQUENCE /// ENTRY P2BPF6 #type complete TITLE P2 protein - phage phi-6 ORGANISM #formal_name phage phi-6 #note host Pseudomonas phaseolicola DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 23-Jul-1999 ACCESSIONS B29885 REFERENCE A93032 !$#authors Mindich, L.; Nemhauser, I.; Gottlieb, P.; Romantschuk, M.; !1Carton, J.; Frucht, S.; Strassman, J.; Bamford, D.H.; !1Kalkkinen, N. !$#journal J. Virol. (1988) 62:1180-1185 !$#title Nucleotide sequence of the large double-stranded RNA segment !1of bacteriophage phi-6: genes specifying the viral replicase !1and transcriptase. !$#cross-references MUID:88155752; PMID:3346944 !$#accession B29885 !'##molecule_type genomic RNA !'##residues 1-665 ##label MIN !'##cross-references GB:M17461; NID:g215480; PIDN:AAA32355.1; !1PID:g215482 COMMENT The genome of this phage consists of three segments of !1double-stranded RNA; this protein is coded by the largest !1segment RNA (L). GENETICS !$#gene 2 !$#map_position segment L CLASSIFICATION #superfamily phage phi-6 P2 protein KEYWORDS early protein SUMMARY #length 665 #molecular-weight 74922 #checksum 7144 SEQUENCE /// ENTRY P4BPF6 #type complete TITLE P4 protein - phage phi-6 ORGANISM #formal_name phage phi-6 #note host Pseudomonas phaseolicola DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 23-Jul-1999 ACCESSIONS C29885 REFERENCE A93032 !$#authors Mindich, L.; Nemhauser, I.; Gottlieb, P.; Romantschuk, M.; !1Carton, J.; Frucht, S.; Strassman, J.; Bamford, D.H.; !1Kalkkinen, N. !$#journal J. Virol. (1988) 62:1180-1185 !$#title Nucleotide sequence of the large double-stranded RNA segment !1of bacteriophage phi-6: genes specifying the viral replicase !1and transcriptase. !$#cross-references MUID:88155752; PMID:3346944 !$#accession C29885 !'##molecule_type genomic RNA !'##residues 1-332 ##label MIN !'##cross-references GB:M17461; NID:g215480; PIDN:AAA32356.1; !1PID:g215483 COMMENT The genome of this phage consists of three segments of !1double-stranded RNA; this protein is coded by the largest !1segment (L). GENETICS !$#gene 4 !$#map_position segment L CLASSIFICATION #superfamily phage phi-6 P4 protein KEYWORDS early protein SUMMARY #length 332 #molecular-weight 35163 #checksum 6416 SEQUENCE /// ENTRY P1BPF6 #type complete TITLE P1 protein - phage phi-6 ORGANISM #formal_name phage phi-6 #note host Pseudomonas phaseolicola DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 23-Jul-1999 ACCESSIONS D29885 REFERENCE A93032 !$#authors Mindich, L.; Nemhauser, I.; Gottlieb, P.; Romantschuk, M.; !1Carton, J.; Frucht, S.; Strassman, J.; Bamford, D.H.; !1Kalkkinen, N. !$#journal J. Virol. (1988) 62:1180-1185 !$#title Nucleotide sequence of the large double-stranded RNA segment !1of bacteriophage phi-6: genes specifying the viral replicase !1and transcriptase. !$#cross-references MUID:88155752; PMID:3346944 !$#accession D29885 !'##molecule_type genomic RNA !'##residues 1-769 ##label MIN !'##cross-references GB:M17461; NID:g215480; PIDN:AAA32357.1; !1PID:g215484 COMMENT The genome of this phage consists of three segments of !1double-stranded RNA; this protein is coded by the largest !1segment (L). GENETICS !$#gene 1 !$#map_position segment L CLASSIFICATION #superfamily phage phi-6 P1 protein KEYWORDS early protein SUMMARY #length 769 #molecular-weight 84986 #checksum 4775 SEQUENCE /// ENTRY PTBPF6 #type complete TITLE P10 protein - phage phi-6 ORGANISM #formal_name phage phi-6 #note host Pseudomonas phaseolicola DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 23-Jul-1999 ACCESSIONS A28648 REFERENCE A94372 !$#authors Gottlieb, P.; Metzger, S.; Romantschuk, M.; Carton, J.; !1Strassman, J.; Bamford, D.H.; Kalkkinen, N.; Mindich, L. !$#journal Virology (1988) 163:183-190 !$#title Nucleotide sequence of the middle dsRNA segment of !1bacteriophage phi-6: placement of the genes of !1membrane-associated proteins. !$#cross-references MUID:88160044; PMID:3347997 !$#accession A28648 !'##molecule_type genomic RNA !'##residues 1-42 ##label GOT !'##cross-references GB:M17462; NID:g862621; PIDN:AAA68483.1; !1PID:g215488 COMMENT The genome of this phage consists of three segments of !1double-stranded RNA; this protein is coded by the !1middle-sized segment (M). COMMENT The function of this protein is related to cell lysis and !1perhaps to membrane assembly. GENETICS !$#gene 10 !$#map_position segment M CLASSIFICATION #superfamily phage phi-6 P10 protein KEYWORDS late protein SUMMARY #length 42 #molecular-weight 4272 #checksum 8415 SEQUENCE /// ENTRY P6BPF6 #type complete TITLE P6 protein - phage phi-6 ORGANISM #formal_name phage phi-6 #note host Pseudomonas phaseolicola DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 31-Mar-1993 ACCESSIONS B28648 REFERENCE A94372 !$#authors Gottlieb, P.; Metzger, S.; Romantschuk, M.; Carton, J.; !1Strassman, J.; Bamford, D.H.; Kalkkinen, N.; Mindich, L. !$#journal Virology (1988) 163:183-190 !$#title Nucleotide sequence of the middle dsRNA segment of !1bacteriophage phi-6: placement of the genes of !1membrane-associated proteins. !$#cross-references MUID:88160044; PMID:3347997 !$#accession B28648 !'##molecule_type genomic RNA !'##residues 1-168 ##label GOT COMMENT The RNA sequence was obtained from GenBank, release 58.0. COMMENT The genome of this phage consists of three segments of !1double-stranded RNA; this protein is coded by the !1middle-sized segment (M). COMMENT This protein is required for adsorption onto host cells. GENETICS !$#gene 6 !$#map_position segment M CLASSIFICATION #superfamily phage phi-6 P6 protein KEYWORDS late protein SUMMARY #length 168 #molecular-weight 17328 #checksum 2252 SEQUENCE /// ENTRY P3BPF6 #type complete TITLE P3 protein - phage phi-6 ORGANISM #formal_name phage phi-6 #note host Pseudomonas phaseolicola DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 23-Jul-1999 ACCESSIONS C28648 REFERENCE A94372 !$#authors Gottlieb, P.; Metzger, S.; Romantschuk, M.; Carton, J.; !1Strassman, J.; Bamford, D.H.; Kalkkinen, N.; Mindich, L. !$#journal Virology (1988) 163:183-190 !$#title Nucleotide sequence of the middle dsRNA segment of !1bacteriophage phi-6: placement of the genes of !1membrane-associated proteins. !$#cross-references MUID:88160044; PMID:3347997 !$#accession C28648 !'##molecule_type genomic RNA !'##residues 1-648 ##label GOT !'##cross-references GB:M17462; NID:g862621; PIDN:AAA68485.1; !1PID:g215490 COMMENT The genome of this phage consists of three segments of !1double-stranded RNA; this protein is coded by the !1middle-sized segment (M). COMMENT This protein is required for adsorption onto host cells. GENETICS !$#gene 3 !$#map_position segment M CLASSIFICATION #superfamily phage phi-6 P3 protein KEYWORDS late protein SUMMARY #length 648 #molecular-weight 69178 #checksum 5429 SEQUENCE /// ENTRY PNBPF6 #type complete TITLE P13 protein - phage phi-6 ORGANISM #formal_name phage phi-6 #note host Pseudomonas phaseolicola DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 23-Jul-1999 ACCESSIONS D28648 REFERENCE A94372 !$#authors Gottlieb, P.; Metzger, S.; Romantschuk, M.; Carton, J.; !1Strassman, J.; Bamford, D.H.; Kalkkinen, N.; Mindich, L. !$#journal Virology (1988) 163:183-190 !$#title Nucleotide sequence of the middle dsRNA segment of !1bacteriophage phi-6: placement of the genes of !1membrane-associated proteins. !$#cross-references MUID:88160044; PMID:3347997 !$#accession D28648 !'##molecule_type genomic RNA !'##residues 1-72 ##label GOT !'##cross-references GB:M17462; NID:g862621; PIDN:AAA68486.1; !1PID:g215491 COMMENT The genome of this phage consists of three segments of !1double-stranded RNA; this protein is coded by the !1middle-sized segment (M). GENETICS !$#gene 13 !$#map_position segment M CLASSIFICATION #superfamily phage phi-6 P13 protein KEYWORDS late protein SUMMARY #length 72 #molecular-weight 7649 #checksum 6397 SEQUENCE /// ENTRY G8BPSV #type complete TITLE gene 8 protein - spiroplasma virus 4 ORGANISM #formal_name spiroplasma virus 4, SpV4 #note host Spiroplasma melliferum DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 07-Dec-1999 ACCESSIONS A29825 REFERENCE A91845 !$#authors Renaudin, J.; Pascarel, M.C.; Bove, J.M. !$#journal J. Bacteriol. (1987) 169:4950-4961 !$#title Spiroplasma virus 4: nucleotide sequence of the viral DNA, !1regulatory signals, and proposed genome organization. !$#cross-references MUID:88032809; PMID:2822658 !$#accession A29825 !'##molecule_type DNA !'##residues 1-38 ##label REN !'##cross-references GB:M17988; NID:g334998 !'##note this ORF is not annotated in GenBank entry SPVDNA COMMENT This virus is a procaryote DNA virus. GENETICS !$#gene 8 !$#genetic_code SGC3 !$#start_codon GTG CLASSIFICATION #superfamily spiroplasma virus 4 gene 8 protein SUMMARY #length 38 #molecular-weight 4629 #checksum 7361 SEQUENCE /// ENTRY G9BPSV #type complete TITLE gene 9 protein - spiroplasma virus 4 ORGANISM #formal_name spiroplasma virus 4, SpV4 #note host Spiroplasma melliferum DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 07-Dec-1999 ACCESSIONS B29825 REFERENCE A91845 !$#authors Renaudin, J.; Pascarel, M.C.; Bove, J.M. !$#journal J. Bacteriol. (1987) 169:4950-4961 !$#title Spiroplasma virus 4: nucleotide sequence of the viral DNA, !1regulatory signals, and proposed genome organization. !$#cross-references MUID:88032809; PMID:2822658 !$#accession B29825 !'##molecule_type DNA !'##residues 1-28 ##label REN !'##cross-references GB:M17988; NID:g334998 !'##note this ORF is not annotated in GenBank entry SPVDNA COMMENT This virus is a procaryote DNA virus. GENETICS !$#gene 9 !$#genetic_code SGC3 CLASSIFICATION #superfamily spiroplasma virus 4 gene 9 protein SUMMARY #length 28 #molecular-weight 3776 #checksum 2767 SEQUENCE /// ENTRY G6BPSV #type complete TITLE gene 6 protein - spiroplasma virus 4 ORGANISM #formal_name spiroplasma virus 4, SpV4 #note host Spiroplasma melliferum DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 07-Dec-1999 ACCESSIONS C29825 REFERENCE A91845 !$#authors Renaudin, J.; Pascarel, M.C.; Bove, J.M. !$#journal J. Bacteriol. (1987) 169:4950-4961 !$#title Spiroplasma virus 4: nucleotide sequence of the viral DNA, !1regulatory signals, and proposed genome organization. !$#cross-references MUID:88032809; PMID:2822658 !$#accession C29825 !'##molecule_type DNA !'##residues 1-71 ##label REN !'##cross-references GB:M17988; NID:g334998 !'##note this ORF is not annotated in GenBank entry SPVDNA COMMENT This virus is a procaryote DNA virus. GENETICS !$#gene 6 !$#genetic_code SGC3 CLASSIFICATION #superfamily spiroplasma virus 4 gene 6 protein SUMMARY #length 71 #molecular-weight 8520 #checksum 4261 SEQUENCE /// ENTRY G5BPSV #type complete TITLE gene 5 protein - spiroplasma virus 4 ORGANISM #formal_name spiroplasma virus 4, SpV4 #note host Spiroplasma melliferum DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 07-Dec-1999 ACCESSIONS D29825 REFERENCE A91845 !$#authors Renaudin, J.; Pascarel, M.C.; Bove, J.M. !$#journal J. Bacteriol. (1987) 169:4950-4961 !$#title Spiroplasma virus 4: nucleotide sequence of the viral DNA, !1regulatory signals, and proposed genome organization. !$#cross-references MUID:88032809; PMID:2822658 !$#accession D29825 !'##molecule_type DNA !'##residues 1-83 ##label REN !'##cross-references GB:M17988; NID:g334998 !'##note this ORF is not annotated in GenBank entry SPVDNA COMMENT This virus is a procaryote DNA virus. GENETICS !$#gene 5 !$#genetic_code SGC3 CLASSIFICATION #superfamily spiroplasma virus 4 gene 5 protein SUMMARY #length 83 #molecular-weight 9494 #checksum 4266 SEQUENCE /// ENTRY G3BPSV #type complete TITLE gene 3 protein - spiroplasma virus 4 ORGANISM #formal_name spiroplasma virus 4, SpV4 #note host Spiroplasma melliferum DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 07-Dec-1999 ACCESSIONS E29825 REFERENCE A91845 !$#authors Renaudin, J.; Pascarel, M.C.; Bove, J.M. !$#journal J. Bacteriol. (1987) 169:4950-4961 !$#title Spiroplasma virus 4: nucleotide sequence of the viral DNA, !1regulatory signals, and proposed genome organization. !$#cross-references MUID:88032809; PMID:2822658 !$#accession E29825 !'##molecule_type DNA !'##residues 1-149 ##label REN !'##cross-references GB:M17988; NID:g334998 !'##note this ORF is not annotated in GenBank entry SPVDNA COMMENT This virus is a procaryote DNA virus. GENETICS !$#gene 3 !$#genetic_code SGC3 CLASSIFICATION #superfamily spiroplasma virus 4 gene 3 protein SUMMARY #length 149 #molecular-weight 17314 #checksum 8459 SEQUENCE /// ENTRY G1BPSV #type complete TITLE gene 1 protein - spiroplasma virus 4 ALTERNATE_NAMES capsid protein ORGANISM #formal_name spiroplasma virus 4, SpV4 #note host Spiroplasma melliferum DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 07-Dec-1999 ACCESSIONS F29825 REFERENCE A91845 !$#authors Renaudin, J.; Pascarel, M.C.; Bove, J.M. !$#journal J. Bacteriol. (1987) 169:4950-4961 !$#title Spiroplasma virus 4: nucleotide sequence of the viral DNA, !1regulatory signals, and proposed genome organization. !$#cross-references MUID:88032809; PMID:2822658 !$#accession F29825 !'##molecule_type DNA !'##residues 1-553 ##label REN !'##cross-references GB:M17988; NID:g334998; PIDN:AAA72621.1; !1PID:g334999 COMMENT This virus is a procaryote DNA virus. GENETICS !$#gene 1 !$#genetic_code SGC3 CLASSIFICATION #superfamily spiroplasma virus 4 gene 1 protein KEYWORDS capsid protein SUMMARY #length 553 #molecular-weight 62219 #checksum 45 SEQUENCE /// ENTRY JU0345 #type complete TITLE major capsid protein VP1 - Chlamydophila psittaci phage Chp1 ORGANISM #formal_name Chlamydophila psittaci phage Chp1, Chlamydia psittaci phage Chp1 #note host Chlamydia psittaci DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jun-2000 ACCESSIONS JU0345; A36822 REFERENCE JU0345 !$#authors Storey, C.C.; Lusher, M.; Richmond, S.J. !$#journal J. Gen. Virol. (1989) 70:3381-3390 !$#title Analysis of the complete nucleotide sequence of Chp1, a !1phage which infects avian Chlamydia psittaci. !$#cross-references MUID:90111716; PMID:2607341 !$#accession JU0345 !'##molecule_type DNA !'##residues 1-596 ##label ST1 !'##cross-references DDBJ:D00624; NID:g217761; PIDN:BAA00515.1; !1PID:g217762 !'##note the authors translated codon AAA for residue 144 as Leu, and !1codon CAA for residue 151 as Gly !$#accession A36822 !'##molecule_type protein !'##residues 2-21 ##label ST2 CLASSIFICATION #superfamily spiroplasma virus 4 gene 1 protein KEYWORDS capsid protein FEATURE !$2-596 #product major capsid protein VP1 #status predicted !8#label MAT SUMMARY #length 596 #molecular-weight 66981 #checksum 7842 SEQUENCE /// ENTRY JU0346 #type complete TITLE capsid protein VP2 - Chlamydophila psittaci phage Chp1 ORGANISM #formal_name Chlamydophila psittaci phage Chp1, Chlamydia psittaci phage Chp1 #note host Chlamydia psittaci DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jun-2000 ACCESSIONS JU0346; B36822 REFERENCE JU0345 !$#authors Storey, C.C.; Lusher, M.; Richmond, S.J. !$#journal J. Gen. Virol. (1989) 70:3381-3390 !$#title Analysis of the complete nucleotide sequence of Chp1, a !1phage which infects avian Chlamydia psittaci. !$#cross-references MUID:90111716; PMID:2607341 !$#accession JU0346 !'##molecule_type DNA !'##residues 1-263 ##label ST1 !'##cross-references DDBJ:D00624; NID:g217761; PIDN:BAA00505.1; !1PID:g217764 !$#accession B36822 !'##molecule_type protein !'##residues 'X',3-16,'X',18-19 ##label ST2 CLASSIFICATION #superfamily Chlamydia psittaci phage Chp1 capsid protein !1VP2 KEYWORDS capsid protein FEATURE !$2-263 #product capsid protein VP2 #status predicted #label !8MAT SUMMARY #length 263 #molecular-weight 28548 #checksum 5179 SEQUENCE /// ENTRY JU0347 #type complete TITLE capsid protein VP3 - Chlamydophila psittaci phage Chp1 ORGANISM #formal_name Chlamydophila psittaci phage Chp1, Chlamydia psittaci phage Chp1 #note host Chlamydia psittaci DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jun-2000 ACCESSIONS JU0347; C36822 REFERENCE JU0345 !$#authors Storey, C.C.; Lusher, M.; Richmond, S.J. !$#journal J. Gen. Virol. (1989) 70:3381-3390 !$#title Analysis of the complete nucleotide sequence of Chp1, a !1phage which infects avian Chlamydia psittaci. !$#cross-references MUID:90111716; PMID:2607341 !$#accession JU0347 !'##molecule_type DNA !'##residues 1-145 ##label ST1 !'##cross-references DDBJ:D00624; NID:g217761; PIDN:BAA00509.1; !1PID:g217768 !$#accession C36822 !'##molecule_type protein !'##residues 1-17,'X',19-21 ##label ST2 CLASSIFICATION #superfamily Chlamydia psittaci phage Chp1 capsid protein !1VP3 KEYWORDS capsid protein FEATURE !$1-145 #product capsid protein VP3 #status predicted #label !8MAT SUMMARY #length 145 #molecular-weight 16681 #checksum 8447 SEQUENCE /// ENTRY G4BPSV #type complete TITLE gene 4 protein - spiroplasma virus 4 ORGANISM #formal_name spiroplasma virus 4, SpV4 #note host Spiroplasma melliferum DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 07-Dec-1999 ACCESSIONS G29825 REFERENCE A91845 !$#authors Renaudin, J.; Pascarel, M.C.; Bove, J.M. !$#journal J. Bacteriol. (1987) 169:4950-4961 !$#title Spiroplasma virus 4: nucleotide sequence of the viral DNA, !1regulatory signals, and proposed genome organization. !$#cross-references MUID:88032809; PMID:2822658 !$#accession G29825 !'##molecule_type DNA !'##residues 1-133 ##label REN !'##cross-references GB:M17988; NID:g334998 !'##note this ORF is not annotated in GenBank entry SPVDNA COMMENT This virus is a procaryote DNA virus. GENETICS !$#gene 4 !$#genetic_code SGC3 CLASSIFICATION #superfamily spiroplasma virus 4 gene 4 protein SUMMARY #length 133 #molecular-weight 14048 #checksum 5572 SEQUENCE /// ENTRY G2BPSV #type complete TITLE gene 2 protein - spiroplasma virus 4 ORGANISM #formal_name spiroplasma virus 4, SpV4 #note host Spiroplasma melliferum DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 07-Dec-1999 ACCESSIONS H29825 REFERENCE A91845 !$#authors Renaudin, J.; Pascarel, M.C.; Bove, J.M. !$#journal J. Bacteriol. (1987) 169:4950-4961 !$#title Spiroplasma virus 4: nucleotide sequence of the viral DNA, !1regulatory signals, and proposed genome organization. !$#cross-references MUID:88032809; PMID:2822658 !$#accession H29825 !'##molecule_type DNA !'##residues 1-320 ##label REN !'##cross-references GB:M17988; NID:g334998 !'##note this ORF is not annotated in GenBank entry SPVDNA COMMENT This virus is a procaryote DNA virus. GENETICS !$#gene 2 !$#genetic_code SGC3 CLASSIFICATION #superfamily spiroplasma virus 4 gene 2 protein SUMMARY #length 320 #molecular-weight 38090 #checksum 4322 SEQUENCE /// ENTRY JU0348 #type complete TITLE 47.6K protein - Chlamydophila psittaci phage Chp1 ORGANISM #formal_name Chlamydophila psittaci phage Chp1, Chlamydia psittaci phage Chp1 #note host Chlamydia psittaci DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jun-2000 ACCESSIONS JU0348 REFERENCE JU0345 !$#authors Storey, C.C.; Lusher, M.; Richmond, S.J. !$#journal J. Gen. Virol. (1989) 70:3381-3390 !$#title Analysis of the complete nucleotide sequence of Chp1, a !1phage which infects avian Chlamydia psittaci. !$#cross-references MUID:90111716; PMID:2607341 !$#accession JU0348 !'##molecule_type DNA !'##residues 1-399 ##label STO !'##cross-references GB:D00624; NID:g217761; PIDN:BAA00511.1; !1PID:g217770 CLASSIFICATION #superfamily spiroplasma virus 4 gene 2 protein SUMMARY #length 399 #molecular-weight 47560 #checksum 5121 SEQUENCE /// ENTRY JU0349 #type complete TITLE 11.5K protein - Chlamydophila psittaci phage Chp1 ORGANISM #formal_name Chlamydophila psittaci phage Chp1, Chlamydia psittaci phage Chp1 #note host Chlamydia psittaci DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jun-2000 ACCESSIONS JU0349 REFERENCE JU0345 !$#authors Storey, C.C.; Lusher, M.; Richmond, S.J. !$#journal J. Gen. Virol. (1989) 70:3381-3390 !$#title Analysis of the complete nucleotide sequence of Chp1, a !1phage which infects avian Chlamydia psittaci. !$#cross-references MUID:90111716; PMID:2607341 !$#accession JU0349 !'##molecule_type DNA !'##residues 1-96 ##label STO !'##cross-references GB:D00624; NID:g217761; PIDN:BAA00513.1; !1PID:g217772 CLASSIFICATION #superfamily Chlamydia psittaci phage Chp1 11.5K protein SUMMARY #length 96 #molecular-weight 11469 #checksum 3094 SEQUENCE /// ENTRY JU0350 #type complete TITLE 9.4K protein - Chlamydophila psittaci phage Chp1 ORGANISM #formal_name Chlamydophila psittaci phage Chp1, Chlamydia psittaci phage Chp1 #note host Chlamydia psittaci DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jun-2000 ACCESSIONS JU0350 REFERENCE JU0345 !$#authors Storey, C.C.; Lusher, M.; Richmond, S.J. !$#journal J. Gen. Virol. (1989) 70:3381-3390 !$#title Analysis of the complete nucleotide sequence of Chp1, a !1phage which infects avian Chlamydia psittaci. !$#cross-references MUID:90111716; PMID:2607341 !$#accession JU0350 !'##molecule_type DNA !'##residues 1-82 ##label STO !'##cross-references GB:D00624; NID:g217761; PIDN:BAA00508.1; !1PID:g217767 CLASSIFICATION #superfamily Chlamydia psittaci phage Chp1 9.4K protein SUMMARY #length 82 #molecular-weight 9426 #checksum 238 SEQUENCE /// ENTRY JU0351 #type complete TITLE 3.6K protein - Chlamydophila psittaci phage Chp1 ORGANISM #formal_name Chlamydophila psittaci phage Chp1, Chlamydia psittaci phage Chp1 #note host Chlamydia psittaci DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jun-2000 ACCESSIONS JU0351 REFERENCE JU0345 !$#authors Storey, C.C.; Lusher, M.; Richmond, S.J. !$#journal J. Gen. Virol. (1989) 70:3381-3390 !$#title Analysis of the complete nucleotide sequence of Chp1, a !1phage which infects avian Chlamydia psittaci. !$#cross-references MUID:90111716; PMID:2607341 !$#accession JU0351 !'##molecule_type DNA !'##residues 1-31 ##label STO !'##cross-references GB:D00624; NID:g217761; PIDN:BAA00504.1; !1PID:g217763 CLASSIFICATION #superfamily Chlamydia psittaci phage Chp1 3.6K protein SUMMARY #length 31 #molecular-weight 3575 #checksum 8918 SEQUENCE /// ENTRY JU0352 #type complete TITLE 4.6K protein - Chlamydophila psittaci phage Chp1 ORGANISM #formal_name Chlamydophila psittaci phage Chp1, Chlamydia psittaci phage Chp1 #note host Chlamydia psittaci DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 16-Jun-2000 ACCESSIONS JU0352 REFERENCE JU0345 !$#authors Storey, C.C.; Lusher, M.; Richmond, S.J. !$#journal J. Gen. Virol. (1989) 70:3381-3390 !$#title Analysis of the complete nucleotide sequence of Chp1, a !1phage which infects avian Chlamydia psittaci. !$#cross-references MUID:90111716; PMID:2607341 !$#accession JU0352 !'##molecule_type DNA !'##residues 1-36 ##label STO !'##cross-references GB:D00624; NID:g217761; PIDN:BAA00510.1; !1PID:g217769 CLASSIFICATION #superfamily Chlamydia psittaci phage Chp1 4.6K protein SUMMARY #length 36 #molecular-weight 4670 #checksum 1964 SEQUENCE /// ENTRY G7BPSV #type complete TITLE gene 7 protein - spiroplasma virus 4 ORGANISM #formal_name spiroplasma virus 4, SpV4 #note host Spiroplasma melliferum DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 07-Dec-1999 ACCESSIONS I29825 REFERENCE A91845 !$#authors Renaudin, J.; Pascarel, M.C.; Bove, J.M. !$#journal J. Bacteriol. (1987) 169:4950-4961 !$#title Spiroplasma virus 4: nucleotide sequence of the viral DNA, !1regulatory signals, and proposed genome organization. !$#cross-references MUID:88032809; PMID:2822658 !$#accession I29825 !'##molecule_type DNA !'##residues 1-48 ##label REN !'##cross-references GB:M17988; NID:g334998 !'##note this ORF is not annotated in GenBank entry SPVDNA COMMENT This virus is a procaryote DNA virus. GENETICS !$#gene 7 !$#genetic_code SGC3 CLASSIFICATION #superfamily spiroplasma virus 4 gene 7 protein SUMMARY #length 48 #molecular-weight 5588 #checksum 1253 SEQUENCE /// ENTRY ZABPF4 #type complete TITLE replication initiation gene A protein [similarity] - phage phi-X174 CONTAINS DNA ligase (EC 6.5.1.-); DNA lyase (EC 4.2.99.-); gene A* protein ORGANISM #formal_name phage phi-X174 DATE 30-Apr-1980 #sequence_revision 30-Apr-1980 #text_change 28-Jul-2000 ACCESSIONS A04239; B94690; B92262 REFERENCE A93185 !$#authors Sanger, F.; Air, G.M.; Barrell, B.G.; Brown, N.L.; Coulson, !1A.R.; Fiddes, J.C.; Hutchison III, C.A.; Slocombe, P.M.; !1Smith, M. !$#journal Nature (1977) 265:687-695 !$#title Nucleotide sequence of bacteriophage phiX174 DNA. !$#cross-references MUID:77171175; PMID:870828 !$#accession A04239 !'##molecule_type DNA !'##residues 1-513 ##label SAN !'##cross-references GB:J02482; GB:M10348; GB:M10379; GB:M10714; !1GB:M10749; GB:M10750; GB:M10866; GB:M10867; GB:M24859; !1NID:g15535; PIDN:CAA24351.1; PID:g1667374 REFERENCE A94690 !$#authors Sanger, F.; Coulson, A.R.; Friedmann, T.; Air, G.M.; !1Barrell, B.G.; Brown, N.L.; Fiddes, J.C.; Hutchison III, !1C.A.; Slocombe, P.M.; Smith, M. !$#journal J. Mol. Biol. (1978) 125:225-246 !$#title The nucleotide sequence of bacteriophage phiX174. !$#cross-references MUID:79091185; PMID:731693 !$#accession B94690 !'##molecule_type DNA !'##residues 1-513 ##label SA2 !'##cross-references GB:V01128; GB:J02482; GB:M10348; GB:M10379; !1GB:M10714; GB:M10749; GB:M10750; GB:M10866; GB:M10867; !1GB:M24859; NID:g15535; PIDN:CAA24351.1; PID:g1667374 REFERENCE A92262 !$#authors Ikeda, J.; Yudelevich, A.; Shimamoto, N.; Hurwitz, J. !$#journal J. Biol. Chem. (1979) 254:9416-9428 !$#title Role of polymeric forms of the bacteriophage phiX174 coded !1gene A protein in phiXRFI DNA cleavage. !$#cross-references MUID:80027245; PMID:158588 !$#accession B92262 !'##molecule_type DNA !'##residues 1-513 ##label IKE COMMENT Gene A* protein is formed from a natural initiation site !1within the A gene. COMMENT Gene A protein is a specific endonuclease that cleaves the !1viral strand of supertwisted, closed circular phi-X174 DNA !1at a unique site in the A gene. COMMENT Gene A protein also causes relaxation of supertwisted !1phi-X174 DNA and forms a complex with phi-X DNA that has a !1discontinuity in gene A of the viral strand. COMMENT Gene A* protein binds to all double-stranded DNA !1preparations tested and prevents their hydrolysis by !1nucleases. COMMENT The internal initiation site for gene A* protein was !1identified by homology with the sequence from phage G4 as !1Met-173. CLASSIFICATION #superfamily phage phi-X174 gene A protein KEYWORDS alternative initiators; carbon-oxygen lyase; DNA binding; !1DNA replication initiation; ligase; zinc finger FEATURE !$1-513 #product gene A protein #status predicted #label GP1\ !$173-513 #product gene A* protein #status predicted #label !8GP2\ !$343,347 #active_site Tyr (covalent DNA-binding) #status !8predicted SUMMARY #length 513 #molecular-weight 58718 #checksum 200 SEQUENCE /// ENTRY ZABPG4 #type complete TITLE replication initiation gene A protein [similarity] - phage G4 CONTAINS DNA ligase (EC 6.5.1.-); DNA lyase (EC 4.2.99.-); gene A* protein ORGANISM #formal_name phage G4 DATE 30-Nov-1979 #sequence_revision 30-Nov-1979 #text_change 20-Apr-2000 ACCESSIONS A04240 REFERENCE A93200 !$#authors Godson, G.N.; Barrell, B.G.; Staden, R.; Fiddes, J.C. !$#journal Nature (1978) 276:236-247 !$#title Nucleotide sequence of bacteriophage G4 DNA. !$#cross-references MUID:79053264; PMID:714153 !$#accession A04240 !'##molecule_type DNA !'##residues 1-554 ##label GOD !'##cross-references GB:J02454; GB:M10724; GB:M11404; GB:V00657; !1NID:g215415; PIDN:AAA32315.1; PID:g215416 COMMENT Gene A and A* proteins are involved in viral DNA replication !1and phage assembly. CLASSIFICATION #superfamily phage phi-X174 gene A protein KEYWORDS alternative initiators; carbon-oxygen lyase; DNA binding; !1DNA replication initiation; ligase; zinc finger FEATURE !$1-554 #product gene A protein #status predicted #label GP1\ !$214-554 #product gene A* protein #status predicted #label !8GP2\ !$384,388 #active_site Tyr (covalent DNA-binding) #status !8predicted SUMMARY #length 554 #molecular-weight 63381 #checksum 8018 SEQUENCE /// ENTRY ZBBPF4 #type complete TITLE gene B protein - phage phi-X174 ORGANISM #formal_name phage phi-X174 DATE 24-Sep-1981 #sequence_revision 24-Sep-1981 #text_change 28-Jul-2000 ACCESSIONS A04241 REFERENCE A93185 !$#authors Sanger, F.; Air, G.M.; Barrell, B.G.; Brown, N.L.; Coulson, !1A.R.; Fiddes, J.C.; Hutchison III, C.A.; Slocombe, P.M.; !1Smith, M. !$#journal Nature (1977) 265:687-695 !$#title Nucleotide sequence of bacteriophage phiX174 DNA. !$#cross-references MUID:77171175; PMID:870828 !$#accession A04241 !'##molecule_type DNA !'##residues 1-120 ##label SAN !'##cross-references GB:J02482; GB:M10348; GB:M10379; GB:M10714; !1GB:M10749; GB:M10750; GB:M10866; GB:M10867; GB:M24859; !1NID:g15535; PIDN:CAA24352.1; PID:g1667375 !'##note the region of DNA coding for gene B protein is contained within !1the region coding for gene A protein, in a different reading !1frame COMMENT Gene B protein is involved in the production of viral !1single-stranded DNA. COMMENT Bacteriophage phi-X174 has a circular, single-stranded DNA !1genome. CLASSIFICATION #superfamily phage phi-X174 gene B protein SUMMARY #length 120 #molecular-weight 13843 #checksum 1516 SEQUENCE /// ENTRY ZBBPG4 #type complete TITLE gene B protein - phage G4 ORGANISM #formal_name phage G4 DATE 30-Nov-1979 #sequence_revision 30-Nov-1979 #text_change 28-Jul-2000 ACCESSIONS A04242 REFERENCE A93200 !$#authors Godson, G.N.; Barrell, B.G.; Staden, R.; Fiddes, J.C. !$#journal Nature (1978) 276:236-247 !$#title Nucleotide sequence of bacteriophage G4 DNA. !$#cross-references MUID:79053264; PMID:714153 !$#accession A04242 !'##molecule_type DNA !'##residues 1-120 ##label GOD !'##cross-references GB:J02454; GB:M10724; GB:M11404; GB:V00657; !1NID:g15831; PIDN:CAA24013.1; PID:g15834 COMMENT Gene B protein is involved in the production of viral !1single-stranded DNA. CLASSIFICATION #superfamily phage phi-X174 gene B protein SUMMARY #length 120 #molecular-weight 13784 #checksum 4715 SEQUENCE /// ENTRY ZCBPF4 #type complete TITLE gene C protein - phage phi-X174 ORGANISM #formal_name phage phi-X174 DATE 30-Apr-1980 #sequence_revision 30-Apr-1980 #text_change 28-Jul-2000 ACCESSIONS A93185; A04243 REFERENCE A93185 !$#authors Sanger, F.; Air, G.M.; Barrell, B.G.; Brown, N.L.; Coulson, !1A.R.; Fiddes, J.C.; Hutchison III, C.A.; Slocombe, P.M.; !1Smith, M. !$#journal Nature (1977) 265:687-695 !$#title Nucleotide sequence of bacteriophage phiX174 DNA. !$#cross-references MUID:77171175; PMID:870828 !$#accession A93185 !'##molecule_type DNA !'##residues 1-86 ##label SAN !'##cross-references GB:J02482; GB:M10348; GB:M10379; GB:M10714; !1GB:M10749; GB:M10750; GB:M10866; GB:M10867; GB:M24859; !1NID:g15535; PIDN:CAA24354.1; PID:g15538 REFERENCE A94690 !$#authors Sanger, F.; Coulson, A.R.; Friedmann, T.; Air, G.M.; !1Barrell, B.G.; Brown, N.L.; Fiddes, J.C.; Hutchison III, !1C.A.; Slocombe, P.M.; Smith, M. !$#journal J. Mol. Biol. (1978) 125:225-246 !$#title The nucleotide sequence of bacteriophage phiX174. !$#cross-references MUID:79091185; PMID:731693 !$#contents annotation; 30 revisions to the nucleotide sequence of the !1genome COMMENT Gene C protein is one of the proteins involved in the !1production and packaging of viral single-stranded DNA. CLASSIFICATION #superfamily phage phi-X174 gene C protein SUMMARY #length 86 #molecular-weight 10080 #checksum 9805 SEQUENCE /// ENTRY ZCBPG4 #type complete TITLE gene C protein - phage G4 ORGANISM #formal_name phage G4 DATE 30-Nov-1979 #sequence_revision 30-Nov-1979 #text_change 28-Jul-2000 ACCESSIONS A04244 REFERENCE A93200 !$#authors Godson, G.N.; Barrell, B.G.; Staden, R.; Fiddes, J.C. !$#journal Nature (1978) 276:236-247 !$#title Nucleotide sequence of bacteriophage G4 DNA. !$#cross-references MUID:79053264; PMID:714153 !$#accession A04244 !'##molecule_type DNA !'##residues 1-84 ##label GOD !'##cross-references GB:J02454; GB:M10724; GB:M11404; GB:V00657; !1NID:g15831; PIDN:CAA24015.1; PID:g15836 COMMENT Gene C protein is one of the proteins involved in the !1production and packaging of viral single-stranded DNA. CLASSIFICATION #superfamily phage phi-X174 gene C protein SUMMARY #length 84 #molecular-weight 9873 #checksum 3593 SEQUENCE /// ENTRY ZDBPF4 #type complete TITLE gene D protein - phage phi-X174 ORGANISM #formal_name phage phi-X174 DATE 24-Apr-1984 #sequence_revision 31-Dec-1991 #text_change 23-Jul-1999 ACCESSIONS A04245; B04245; S02329 REFERENCE A93183 !$#authors Barrell, B.G.; Air, G.M.; Hutchison III, C.A. !$#journal Nature (1976) 264:34-41 !$#title Overlapping genes in bacteriophage phi-X174. !$#cross-references MUID:77077164; PMID:1004533 !$#accession A04245 !'##molecule_type DNA !'##residues 1-152 ##label BAR !'##cross-references GB:J02482; GB:M10348; GB:M10379; GB:M10714; !1GB:M10749; GB:M10750; GB:M10866; GB:M10867; GB:M24859; !1NID:g216019; PIDN:AAA32575.1; PID:g216025 !$#accession B04245 !'##molecule_type protein !'##residues 2-57,'XX',60-92,'X',94-122,'X',124-152 ##label BAR2 REFERENCE S02329 !$#authors Buckley, K.J.; Hayashi, M. !$#journal J. Mol. Biol. (1987) 198:599-607 !$#title Role of premature translational termination in the !1regulation of expression of the phi-X174 lysis gene. !$#cross-references MUID:88118956; PMID:2963134 !$#accession S02329 !'##status translation not shown !'##molecule_type DNA !'##residues 1-69 ##label BUC !'##cross-references EMBL:X07809; NID:g15094; PIDN:CAA30667.1; !1PID:g15095 COMMENT Gene D protein is involved in the production of viral !1single-stranded DNA. COMMENT Bacteriophage phi-X174 has single-stranded DNA. GENETICS !$#gene D CLASSIFICATION #superfamily phage phi-X174 gene D protein FEATURE !$2-152 #product gene D protein #status experimental #label !8MAT SUMMARY #length 152 #molecular-weight 16937 #checksum 6132 SEQUENCE /// ENTRY ZDBPG4 #type complete TITLE gene D protein - phage G4 ORGANISM #formal_name phage G4 DATE 30-Nov-1979 #sequence_revision 30-Nov-1979 #text_change 28-Jul-2000 ACCESSIONS A04246 REFERENCE A93200 !$#authors Godson, G.N.; Barrell, B.G.; Staden, R.; Fiddes, J.C. !$#journal Nature (1978) 276:236-247 !$#title Nucleotide sequence of bacteriophage G4 DNA. !$#cross-references MUID:79053264; PMID:714153 !$#accession A04246 !'##molecule_type DNA !'##residues 1-152 ##label GOD !'##cross-references GB:J02454; GB:M10724; GB:M11404; GB:V00657; !1NID:g15831; PIDN:CAA24016.1; PID:g15837 COMMENT Gene D protein is involved in the production of viral !1single-stranded DNA. CLASSIFICATION #superfamily phage phi-X174 gene D protein SUMMARY #length 152 #molecular-weight 16872 #checksum 5914 SEQUENCE /// ENTRY ZEBPF4 #type complete TITLE gene E protein - phage phi-X174 ORGANISM #formal_name phage phi-X174 DATE 24-Sep-1981 #sequence_revision 24-Sep-1981 #text_change 23-Jul-1999 ACCESSIONS A04247 REFERENCE A93183 !$#authors Barrell, B.G.; Air, G.M.; Hutchison III, C.A. !$#journal Nature (1976) 264:34-41 !$#title Overlapping genes in bacteriophage phi-X174. !$#cross-references MUID:77077164; PMID:1004533 !$#accession A04247 !'##molecule_type DNA !'##residues 1-90 ##label BAR !'##cross-references GB:J02482; GB:M10348; GB:M10379; GB:M10714; !1GB:M10749; GB:M10750; GB:M10866; GB:M10867; GB:M24859; !1NID:g216019; PIDN:AAA32576.1; PID:g216026 !'##note gene E and gene D proteins are coded by the same region of DNA !1but in different reading frames COMMENT Gene E protein is responsible for host cell lysis. CLASSIFICATION #superfamily phage phi-X174 gene E protein SUMMARY #length 90 #molecular-weight 10471 #checksum 2965 SEQUENCE /// ENTRY ZEBPG4 #type complete TITLE gene E protein - phage G4 ORGANISM #formal_name phage G4 DATE 30-Nov-1979 #sequence_revision 30-Nov-1979 #text_change 28-Jul-2000 ACCESSIONS A04248 REFERENCE A93200 !$#authors Godson, G.N.; Barrell, B.G.; Staden, R.; Fiddes, J.C. !$#journal Nature (1978) 276:236-247 !$#title Nucleotide sequence of bacteriophage G4 DNA. !$#cross-references MUID:79053264; PMID:714153 !$#accession A04248 !'##molecule_type DNA !'##residues 1-96 ##label GOD !'##cross-references GB:J02454; GB:M10724; GB:M11404; GB:V00657; !1NID:g15831; PIDN:CAA24017.1; PID:g15838 COMMENT Gene E protein is responsible for host cell lysis. CLASSIFICATION #superfamily phage phi-X174 gene E protein SUMMARY #length 96 #molecular-weight 10531 #checksum 408 SEQUENCE /// ENTRY ZFBPF4 #type complete TITLE gene F protein - phage phi-X174 ORGANISM #formal_name phage phi-X174 DATE 30-Apr-1980 #sequence_revision 29-Jun-1981 #text_change 28-Jul-2000 ACCESSIONS B93185; A92841; A92854; A04249 REFERENCE A93185 !$#authors Sanger, F.; Air, G.M.; Barrell, B.G.; Brown, N.L.; Coulson, !1A.R.; Fiddes, J.C.; Hutchison III, C.A.; Slocombe, P.M.; !1Smith, M. !$#journal Nature (1977) 265:687-695 !$#title Nucleotide sequence of bacteriophage phiX174 DNA. !$#cross-references MUID:77171175; PMID:870828 !$#accession B93185 !'##molecule_type DNA !'##residues 1-426 ##label SAN !'##cross-references GB:J02482; GB:M10348; GB:M10379; GB:M10714; !1GB:M10749; GB:M10750; GB:M10866; GB:M10867; GB:M24859; !1NID:g15535; PIDN:CAA24358.1; PID:g15542 REFERENCE A94690 !$#authors Sanger, F.; Coulson, A.R.; Friedmann, T.; Air, G.M.; !1Barrell, B.G.; Brown, N.L.; Fiddes, J.C.; Hutchison III, !1C.A.; Slocombe, P.M.; Smith, M. !$#journal J. Mol. Biol. (1978) 125:225-246 !$#title The nucleotide sequence of bacteriophage phiX174. !$#cross-references MUID:79091185; PMID:731693 !$#contents annotation; 30 revisions to the nucleotide sequence of the !1genome !$#note the sequence shown is from this reference REFERENCE A92841 !$#authors Air, G.M. !$#journal J. Mol. Biol. (1976) 107:433-443 !$#title Amino acid sequences from the gene F(capsid) protein of !1bacteriophage phiX174. !$#cross-references MUID:77074162; PMID:794486 !$#accession A92841 !'##molecule_type protein !'##residues 1-94 ##label AIR1 REFERENCE A92854 !$#authors Air, G.M.; Coulson, A.R.; Fiddes, J.C.; Friedmann, T.; !1Hutchison III, C.A.; Sanger, F.; Slocombe, P.M.; Smith, !1A.J.H. !$#journal J. Mol. Biol. (1978) 125:247-254 !$#title Nucleotide sequence of the F protein coding region of !1bacteriophage phiX174 and the amino acid sequence of its !1product. !$#cross-references MUID:79091186; PMID:731694 !$#accession A92854 !'##molecule_type protein !'##residues 85-426 ##label AIR2 COMMENT Gene F protein is the major capsid component. CLASSIFICATION #superfamily phage phi-X174 gene F protein SUMMARY #length 426 #molecular-weight 48351 #checksum 7825 SEQUENCE /// ENTRY ZFBPG4 #type complete TITLE gene F protein - phage G4 ORGANISM #formal_name phage G4 DATE 30-Nov-1979 #sequence_revision 30-Nov-1979 #text_change 28-Jul-2000 ACCESSIONS A04250 REFERENCE A93200 !$#authors Godson, G.N.; Barrell, B.G.; Staden, R.; Fiddes, J.C. !$#journal Nature (1978) 276:236-247 !$#title Nucleotide sequence of bacteriophage G4 DNA. !$#cross-references MUID:79053264; PMID:714153 !$#accession A04250 !'##molecule_type DNA !'##residues 1-427 ##label GOD !'##cross-references GB:J02454; GB:M10724; GB:M11404; GB:V00657; !1NID:g15831; PIDN:CAA24019.1; PID:g15840 COMMENT Gene F protein is the major capsid component. CLASSIFICATION #superfamily phage phi-X174 gene F protein SUMMARY #length 427 #molecular-weight 48728 #checksum 2729 SEQUENCE /// ENTRY ZGBPF4 #type complete TITLE gene G protein - phage phi-X174 ORGANISM #formal_name phage phi-X174 DATE 24-Sep-1981 #sequence_revision 24-Sep-1981 #text_change 28-Jul-2000 ACCESSIONS C93185; A92952; B92952; A92842; B92842; A04251 REFERENCE A93185 !$#authors Sanger, F.; Air, G.M.; Barrell, B.G.; Brown, N.L.; Coulson, !1A.R.; Fiddes, J.C.; Hutchison III, C.A.; Slocombe, P.M.; !1Smith, M. !$#journal Nature (1977) 265:687-695 !$#title Nucleotide sequence of bacteriophage phiX174 DNA. !$#cross-references MUID:77171175; PMID:870828 !$#accession C93185 !'##molecule_type DNA !'##residues 1-175 ##label SAN !'##cross-references GB:J02482; GB:M10348; GB:M10379; GB:M10714; !1GB:M10749; GB:M10750; GB:M10866; GB:M10867; GB:M24859; !1NID:g15535; PIDN:CAA24359.1; PID:g15543 REFERENCE A94604 !$#authors Sanger, F.; Coulson, A.R.; Friedmann, T. !$#submission submitted to the Atlas, October 1977 !$#contents annotation; revision from the nucleotide sequence !$#note the residue at position 113 is Asn REFERENCE A92952 !$#authors Air, G.M.; Blackburn, E.H.; Sanger, F.; Coulson, A.R. !$#journal J. Mol. Biol. (1975) 96:703-719 !$#title The nucleotide and amino acid sequences of the N (5') !1terminal region of gene G of bacteriophage phiX174. !$#cross-references MUID:76072037; PMID:1081600 !$#accession A92952 !'##molecule_type DNA !'##residues 1-67 ##label AI1 !$#accession B92952 !'##molecule_type protein !'##residues 1-67 ##label AI2 REFERENCE A92842 !$#authors Air, G.M.; Sanger, F.; Coulson, A.R. !$#journal J. Mol. Biol. (1976) 108:519-533 !$#title Nucleotide and amino acid sequences of gene G of phiX174. !$#cross-references MUID:77121207; PMID:1088827 !$#accession A92842 !'##molecule_type DNA !'##residues 63-175 ##label AI3 !$#accession B92842 !'##molecule_type protein !'##residues 63-175 ##label AI4 COMMENT The order of some peptides, amidation states of eight !1residues, and identities of some doubtful residues were !1confirmed by the nucleotide sequence. COMMENT Gene G protein is one of the structural components of the !1bacteriophage capsid. CLASSIFICATION #superfamily phage phi-X174 gene G protein SUMMARY #length 175 #molecular-weight 19047 #checksum 3724 SEQUENCE /// ENTRY ZGBPG4 #type complete TITLE gene G protein - phage G4 ORGANISM #formal_name phage G4 DATE 30-Nov-1979 #sequence_revision 30-Nov-1979 #text_change 28-Jul-2000 ACCESSIONS A04252 REFERENCE A93200 !$#authors Godson, G.N.; Barrell, B.G.; Staden, R.; Fiddes, J.C. !$#journal Nature (1978) 276:236-247 !$#title Nucleotide sequence of bacteriophage G4 DNA. !$#cross-references MUID:79053264; PMID:714153 !$#accession A04252 !'##molecule_type DNA !'##residues 1-177 ##label GOD !'##cross-references GB:J02454; GB:M10724; GB:M11404; GB:V00657; !1NID:g15831; PIDN:CAA24020.1; PID:g15841 COMMENT Gene G protein is one of the structural components of the !1bacteriophage capsid. CLASSIFICATION #superfamily phage phi-X174 gene G protein SUMMARY #length 177 #molecular-weight 18820 #checksum 4484 SEQUENCE /// ENTRY ZGBPS1 #type fragment TITLE gene G protein - phage St-1 (fragment) ORGANISM #formal_name phage St-1 DATE 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 30-Sep-1993 ACCESSIONS A04253 REFERENCE A92247 !$#authors Sims, J.; Capon, D.; Dressler, D. !$#journal J. Biol. Chem. (1979) 254:12615-12628 !$#title dnaG (primase)-dependent origins of DNA replication. !1Nucleotide sequences of the negative strand initiation sites !1of bacteriophages St-1, phiK, and alpha3. !$#cross-references MUID:80049950; PMID:387790 !$#accession A04253 !'##molecule_type DNA !'##residues 1-103 ##label SIM COMMENT This protein is one of the structural components of the !1bacteriophage capsid. GENETICS !$#gene G CLASSIFICATION #superfamily phage phi-X174 gene G protein KEYWORDS capsid protein SUMMARY #length 103 #checksum 334 SEQUENCE /// ENTRY ZHBPF4 #type complete TITLE gene H protein - phage phi-X174 ORGANISM #formal_name phage phi-X174 DATE 30-Apr-1980 #sequence_revision 30-Apr-1980 #text_change 28-Jul-2000 ACCESSIONS D93185; A04254 REFERENCE A93185 !$#authors Sanger, F.; Air, G.M.; Barrell, B.G.; Brown, N.L.; Coulson, !1A.R.; Fiddes, J.C.; Hutchison III, C.A.; Slocombe, P.M.; !1Smith, M. !$#journal Nature (1977) 265:687-695 !$#title Nucleotide sequence of bacteriophage phiX174 DNA. !$#cross-references MUID:77171175; PMID:870828 !$#accession D93185 !'##molecule_type DNA !'##residues 1-328 ##label SAN !'##cross-references GB:J02482; GB:M10348; GB:M10379; GB:M10714; !1GB:M10749; GB:M10750; GB:M10866; GB:M10867; GB:M24859; !1NID:g15535; PIDN:CAA24360.1; PID:g15544 REFERENCE A94690 !$#authors Sanger, F.; Coulson, A.R.; Friedmann, T.; Air, G.M.; !1Barrell, B.G.; Brown, N.L.; Fiddes, J.C.; Hutchison III, !1C.A.; Slocombe, P.M.; Smith, M. !$#journal J. Mol. Biol. (1978) 125:225-246 !$#title The nucleotide sequence of bacteriophage phiX174. !$#cross-references MUID:79091185; PMID:731693 !$#contents annotation; 30 revisions to the nucleotide sequence of the !1genome COMMENT Gene H protein is the minor spike component of the viral !1shell. CLASSIFICATION #superfamily phage phi-X174 gene H protein SUMMARY #length 328 #molecular-weight 34419 #checksum 3614 SEQUENCE /// ENTRY ZHBPG4 #type complete TITLE gene H protein - phage G4 ORGANISM #formal_name phage G4 DATE 30-Nov-1979 #sequence_revision 30-Nov-1979 #text_change 28-Jul-2000 ACCESSIONS A04255 REFERENCE A93200 !$#authors Godson, G.N.; Barrell, B.G.; Staden, R.; Fiddes, J.C. !$#journal Nature (1978) 276:236-247 !$#title Nucleotide sequence of bacteriophage G4 DNA. !$#cross-references MUID:79053264; PMID:714153 !$#accession A04255 !'##molecule_type DNA !'##residues 1-337 ##label GOD !'##cross-references GB:J02454; GB:M10724; GB:M11404; GB:V00657; !1NID:g15831; PIDN:CAA24021.1; PID:g15842 COMMENT Gene H protein is the minor spike component of the viral !1shell. CLASSIFICATION #superfamily phage phi-X174 gene H protein SUMMARY #length 337 #molecular-weight 35706 #checksum 3264 SEQUENCE /// ENTRY ZHBPA3 #type complete TITLE gene H protein - phage alpha-3 ORGANISM #formal_name phage alpha-3 DATE 17-Dec-1982 #sequence_revision 19-Apr-1996 #text_change 23-Jul-1999 ACCESSIONS A21537; S22332; A04257 REFERENCE A21537 !$#authors Kodaira, K.I.; Nakano, K.; Taketo, A. !$#journal Biochim. Biophys. Acta (1985) 825:255-260 !$#title Function and structure of microvirid phage alpha3 genome. !1DNA sequence of H gene and properties of missense H mutant. !$#cross-references MUID:85226468; PMID:2988629 !$#accession A21537 !'##status preliminary !'##molecule_type DNA !'##residues 1-330 ##label KOD !'##cross-references GB:M25640; NID:g166101; PIDN:AAA32174.1; !1PID:g166102 REFERENCE S22324 !$#authors Kodaira, K.I.; Nakano, K.; Okada, S.; Taketo, A. !$#journal Biochim. Biophys. Acta (1992) 1130:277-288 !$#title Nucleotide sequence of the genome of the bacteriophage !1alpha3: interrelationship of the genome structure and the !1gene products with those of the phages, phiX174, G4 and !1phiK. !$#cross-references MUID:92223109; PMID:1532908 !$#accession S22332 !'##molecule_type DNA !'##residues 1-330 ##label KO2 !'##cross-references EMBL:X60322; NID:g14775; PIDN:CAA42883.1; !1PID:g14785 REFERENCE A92247 !$#authors Sims, J.; Capon, D.; Dressler, D. !$#journal J. Biol. Chem. (1979) 254:12615-12628 !$#title dnaG (primase)-dependent origins of DNA replication. !1Nucleotide sequences of the negative strand initiation sites !1of bacteriophages St-1, phiK, and alpha3. !$#cross-references MUID:80049950; PMID:387790 !$#accession A04257 !'##molecule_type DNA !'##residues 1-70 ##label SIM !'##cross-references GB:J02444; GB:M10725; NID:g166103; PIDN:AAA32176.1; !1PID:g166105 GENETICS !$#gene H FUNCTION !$#description gene H protein is a minor spike component of the viral shell CLASSIFICATION #superfamily phage phi-X174 gene H protein SUMMARY #length 330 #molecular-weight 34844 #checksum 6269 SEQUENCE /// ENTRY ZHBPS1 #type fragment TITLE gene H protein - phage St-1 (fragment) ORGANISM #formal_name phage St-1 DATE 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 30-Sep-1993 ACCESSIONS A04256 REFERENCE A92247 !$#authors Sims, J.; Capon, D.; Dressler, D. !$#journal J. Biol. Chem. (1979) 254:12615-12628 !$#title dnaG (primase)-dependent origins of DNA replication. !1Nucleotide sequences of the negative strand initiation sites !1of bacteriophages St-1, phiK, and alpha3. !$#cross-references MUID:80049950; PMID:387790 !$#accession A04256 !'##molecule_type DNA !'##residues 1-103 ##label SIM COMMENT This protein is a minor spike component of the viral shell. GENETICS !$#gene H CLASSIFICATION #superfamily phage phi-X174 gene H protein KEYWORDS spike protein SUMMARY #length 103 #checksum 4061 SEQUENCE /// ENTRY ZJBPF4 #type complete TITLE gene J protein - phage phi-X174 ALTERNATE_NAMES small core protein ORGANISM #formal_name phage phi-X174 DATE 24-Sep-1981 #sequence_revision 24-Sep-1981 #text_change 28-Jul-2000 ACCESSIONS E93185; A90405; A04258 REFERENCE A93185 !$#authors Sanger, F.; Air, G.M.; Barrell, B.G.; Brown, N.L.; Coulson, !1A.R.; Fiddes, J.C.; Hutchison III, C.A.; Slocombe, P.M.; !1Smith, M. !$#journal Nature (1977) 265:687-695 !$#title Nucleotide sequence of bacteriophage phiX174 DNA. !$#cross-references MUID:77171175; PMID:870828 !$#accession E93185 !'##molecule_type DNA !'##residues 1-37 ##label SAN !'##cross-references GB:J02482; GB:M10348; GB:M10379; GB:M10714; !1GB:M10749; GB:M10750; GB:M10866; GB:M10867; GB:M24859; !1NID:g15535; PIDN:CAA24357.1; PID:g15541 REFERENCE A90405 !$#authors Freymeyer II, D.K.; Shank, P.R.; Edgell, M.H.; Hutchison !1III, C.A.; Vanaman, T.C. !$#journal Biochemistry (1977) 16:4550-4556 !$#title Amino acid sequence of the small core protein from !1bacteriophage 0X174. !$#cross-references MUID:78020823; PMID:911774 !$#accession A90405 !'##molecule_type protein !'##residues 1-37 ##label FRE COMMENT Gene J protein is one of the structural components of the !1bacteriophage coat. CLASSIFICATION #superfamily phage phi-X174 gene J protein KEYWORDS DNA binding SUMMARY #length 37 #molecular-weight 4096 #checksum 4402 SEQUENCE /// ENTRY ZJBPG4 #type complete TITLE gene J protein - phage G4 ORGANISM #formal_name phage G4 DATE 30-Nov-1979 #sequence_revision 30-Nov-1979 #text_change 28-Jul-2000 ACCESSIONS A04259 REFERENCE A93200 !$#authors Godson, G.N.; Barrell, B.G.; Staden, R.; Fiddes, J.C. !$#journal Nature (1978) 276:236-247 !$#title Nucleotide sequence of bacteriophage G4 DNA. !$#cross-references MUID:79053264; PMID:714153 !$#accession A04259 !'##molecule_type DNA !'##residues 1-25 ##label GOD !'##cross-references GB:J02454; GB:M10724; GB:M11404; GB:V00657; !1NID:g15831; PIDN:CAA24018.1; PID:g15839 COMMENT Gene J protein is one of the structural components of the !1bacteriophage coat. CLASSIFICATION #superfamily phage phi-X174 gene J protein KEYWORDS DNA binding SUMMARY #length 25 #molecular-weight 2815 #checksum 5728 SEQUENCE /// ENTRY ZKBPF4 #type complete TITLE gene K protein - phage phi-X174 ORGANISM #formal_name phage phi-X174 DATE 30-Apr-1980 #sequence_revision 08-Oct-1981 #text_change 28-Jul-2000 ACCESSIONS F93185; A93196; A04260 REFERENCE A93185 !$#authors Sanger, F.; Air, G.M.; Barrell, B.G.; Brown, N.L.; Coulson, !1A.R.; Fiddes, J.C.; Hutchison III, C.A.; Slocombe, P.M.; !1Smith, M. !$#journal Nature (1977) 265:687-695 !$#title Nucleotide sequence of bacteriophage phiX174 DNA. !$#cross-references MUID:77171175; PMID:870828 !$#accession F93185 !'##molecule_type DNA !'##residues 1-56 ##label SAN !'##cross-references GB:J02482; GB:M10348; GB:M10379; GB:M10714; !1GB:M10749; GB:M10750; GB:M10866; GB:M10867; GB:M24859; !1NID:g15535; PIDN:CAA24353.1; PID:g15537 REFERENCE A94690 !$#authors Sanger, F.; Coulson, A.R.; Friedmann, T.; Air, G.M.; !1Barrell, B.G.; Brown, N.L.; Fiddes, J.C.; Hutchison III, !1C.A.; Slocombe, P.M.; Smith, M. !$#journal J. Mol. Biol. (1978) 125:225-246 !$#title The nucleotide sequence of bacteriophage phiX174. !$#cross-references MUID:79091185; PMID:731693 !$#contents annotation; 30 revisions to the nucleotide sequence of the !1genome REFERENCE A93196 !$#authors Shaw, D.C.; Walker, J.E.; Northrop, F.D.; Barrell, B.G.; !1Godson, G.N.; Fiddes, J.C. !$#journal Nature (1978) 272:510-515 !$#title Gene K, a new overlapping gene in bacteriophage G4. !$#cross-references MUID:79010545; PMID:692656 !$#accession A93196 !'##molecule_type DNA !'##residues 1-56 ##label SHA !'##note the sequence of gene K and its protein from bacteriophage G4 !1were determined and comparison suggests a potential new !1protein from the corresponding gene in bacteriophage !1phi-X174; this potential gene K overlaps genes B, A, and C !1and is the third example of an overlapping gene in the !1isometric phages !'##note no function has yet been ascribed to gene K protein CLASSIFICATION #superfamily phage phi-X174 gene K protein SUMMARY #length 56 #molecular-weight 6392 #checksum 1807 SEQUENCE /// ENTRY ZKBPG4 #type complete TITLE gene K protein - phage G4 ORGANISM #formal_name phage G4 DATE 30-Nov-1979 #sequence_revision 30-Nov-1979 #text_change 28-Jul-2000 ACCESSIONS A93200; B93196; A04261 REFERENCE A93200 !$#authors Godson, G.N.; Barrell, B.G.; Staden, R.; Fiddes, J.C. !$#journal Nature (1978) 276:236-247 !$#title Nucleotide sequence of bacteriophage G4 DNA. !$#cross-references MUID:79053264; PMID:714153 !$#accession A93200 !'##molecule_type DNA !'##residues 1-56 ##label GOD !'##cross-references GB:J02454; GB:M10724; GB:M11404; GB:V00657; !1NID:g15831; PIDN:CAA24014.1; PID:g15835 REFERENCE A93196 !$#authors Shaw, D.C.; Walker, J.E.; Northrop, F.D.; Barrell, B.G.; !1Godson, G.N.; Fiddes, J.C. !$#journal Nature (1978) 272:510-515 !$#title Gene K, a new overlapping gene in bacteriophage G4. !$#cross-references MUID:79010545; PMID:692656 !$#accession B93196 !'##molecule_type DNA !'##residues 1-56 ##label SHA !'##cross-references GB:V00656; NID:g15829; PIDN:CAA24010.1; PID:g15830 !'##note no function has yet been ascribed to gene K protein CLASSIFICATION #superfamily phage phi-X174 gene K protein SUMMARY #length 56 #molecular-weight 6338 #checksum 3117 SEQUENCE /// ENTRY ZNBPFE #type complete TITLE gene N protein - phage phi-80 ORGANISM #formal_name phage phi-80 #note host Escherichia coli DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 23-Jul-1999 ACCESSIONS A24523; S04825 REFERENCE A24523 !$#authors Tanaka, S.; Matsushiro, A. !$#journal Gene (1985) 38:119-129 !$#title Characterization and sequencing of the region containing !1gene N, the nutL site and t-L1 terminator of bacteriophage !1phi-80. !$#cross-references MUID:86056968; PMID:4065570 !$#accession A24523 !'##molecule_type DNA !'##residues 1-98 ##label TAN !'##cross-references GB:M11919; NID:g215358; PIDN:AAA32296.1; !1PID:g215359 !'##note the authors translated the codon GAA for residue 30 as Gln, AAG !1for residue 43 as Leu, and GAG for residue 68 as Gln REFERENCE S01776 !$#authors Ogawa, T.; Ogawa, H.; Tomizawa, J.I. !$#journal J. Mol. Biol. (1988) 202:537-550 !$#title Organization of the early region of bacteriophage phi-80. !1Genes and proteins. !$#cross-references MUID:89011978; PMID:3172225 !$#accession S04825 !'##status preliminary !'##molecule_type DNA !'##residues 1-98 ##label OGA !'##cross-references EMBL:X13065; NID:g14800; PIDN:CAA31468.1; !1PID:g14801 GENETICS !$#gene N CLASSIFICATION #superfamily phage phi-80 gene N protein KEYWORDS transcription regulation SUMMARY #length 98 #molecular-weight 11682 #checksum 9119 SEQUENCE /// ENTRY Z1BPFD #type complete TITLE gene I protein - phage fd (strain 478, Heidelberg) ORGANISM #formal_name phage fd DATE 30-Sep-1980 #sequence_revision 30-Sep-1980 #text_change 23-Jul-1999 ACCESSIONS A04262 REFERENCE A93690 !$#authors Beck, E.; Sommer, R.; Auerswald, E.A.; Kurz, C.; Zink, B.; !1Osterburg, G.; Schaller, H.; Sugimoto, K.; Sugisaki, H.; !1Okamoto, T.; Takanami, M. !$#journal Nucleic Acids Res. (1978) 5:4495-4503 !$#title Nucleotide sequence of bacteriophage fd DNA. !$#cross-references MUID:79136480; PMID:745987 !$#accession A04262 !'##molecule_type DNA !'##residues 1-348 ##label BEC !'##cross-references GB:V00602; GB:J02451; GB:M10731; GB:M10767; !1GB:M21666; GB:M21667; GB:M21668; GB:M21669; GB:M21670; !1GB:M25198; NID:g14931; PIDN:CAA23853.1; PID:g14940 COMMENT The exact function of this protein is not known although it !1may be involved in phage assembly. GENETICS !$#gene I CLASSIFICATION #superfamily filamentous phage gene I protein KEYWORDS phage maturation SUMMARY #length 348 #molecular-weight 39536 #checksum 2767 SEQUENCE /// ENTRY Z1BPM3 #type complete TITLE gene I protein - phage M13 ORGANISM #formal_name phage M13 DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 23-Jul-1999 ACCESSIONS B04262; A04262 REFERENCE A91470 !$#authors van Wezenbeek, P.M.G.F.; Hulsebos, T.J.M.; Schoenmakers, !1J.G.G. !$#journal Gene (1980) 11:129-148 !$#title Nucleotide sequence of the filamentous bacteriophage M13 DNA !1genome: comparison with phage fd. !$#cross-references MUID:81067903; PMID:6254849 !$#accession B04262 !'##molecule_type DNA !'##residues 1-348 ##label VAN !'##cross-references GB:V00604; GB:J02461; GB:M10377; NID:g14959; !1PIDN:CAA23864.1; PID:g14968 COMMENT The exact function of this protein is not known although it !1may be involved in phage assembly. GENETICS !$#gene I CLASSIFICATION #superfamily filamentous phage gene I protein KEYWORDS phage maturation SUMMARY #length 348 #molecular-weight 39550 #checksum 2240 SEQUENCE /// ENTRY Z1BPF1 #type complete TITLE gene I protein - phage f1 ORGANISM #formal_name phage f1 DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 23-Jul-1999 ACCESSIONS C04262; A04262 REFERENCE A91490 !$#authors Beck, E.; Zink, B. !$#journal Gene (1981) 16:35-58 !$#title Nucleotide sequence and genome organisation of filamentous !1bacteriophages f1 and fd. !$#cross-references MUID:82211801; PMID:6282703 !$#accession C04262 !'##molecule_type DNA !'##residues 1-348 ##label BEC !'##cross-references GB:V00606; GB:J02449; GB:M10881; NID:g14974; !1PIDN:CAA23874.1; PID:g14982 COMMENT The exact function of this protein is not known although it !1may be involved in phage assembly. GENETICS !$#gene I CLASSIFICATION #superfamily filamentous phage gene I protein KEYWORDS phage maturation SUMMARY #length 348 #molecular-weight 39527 #checksum 2408 SEQUENCE /// ENTRY Z1BPIK #type complete TITLE gene I protein - phage IKe ORGANISM #formal_name phage IKe #note host Escherichia coli DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 28-Jul-2000 ACCESSIONS A04263 REFERENCE A92912 !$#authors Peeters, B.P.H.; Peters, R.M.; Schoenmakers, J.G.G.; !1Konings, R.N.H. !$#journal J. Mol. Biol. (1985) 181:27-39 !$#title Nucleotide sequence and genetic organization of the genome !1of the N-specific filamentous bacteriophage IKe. Comparison !1with the genome of the F-specific filamentous phages M13, fd !1and f1. !$#cross-references MUID:85160831; PMID:3981635 !$#accession A04263 !'##molecule_type DNA !'##residues 1-365 ##label PEE !'##cross-references GB:K02750; NID:g14942; PIDN:CAA26075.1; PID:g14955 COMMENT The exact function of this protein is not known, although it !1may be involved in phage assembly. GENETICS !$#gene I CLASSIFICATION #superfamily filamentous phage gene I protein KEYWORDS phage maturation SUMMARY #length 365 #molecular-weight 41305 #checksum 4570 SEQUENCE /// ENTRY Z2BPFD #type complete TITLE gene II protein - phage fd (strain 478, Heidelberg) CONTAINS gene X protein ORGANISM #formal_name phage fd DATE 30-Nov-1980 #sequence_revision 30-Nov-1980 #text_change 23-Jul-1999 ACCESSIONS A04264 REFERENCE A93690 !$#authors Beck, E.; Sommer, R.; Auerswald, E.A.; Kurz, C.; Zink, B.; !1Osterburg, G.; Schaller, H.; Sugimoto, K.; Sugisaki, H.; !1Okamoto, T.; Takanami, M. !$#journal Nucleic Acids Res. (1978) 5:4495-4503 !$#title Nucleotide sequence of bacteriophage fd DNA. !$#cross-references MUID:79136480; PMID:745987 !$#accession A04264 !'##molecule_type DNA !'##residues 1-410 ##label BEC !'##cross-references GB:V00602; GB:J02451; GB:M10731; GB:M10767; !1GB:M21666; GB:M21667; GB:M21668; GB:M21669; GB:M21670; !1GB:M25198; NID:g14931; PIDN:CAA23845.1; PID:g14932 COMMENT The gene II protein is required for DNA replication. One of !1its major functions is the site-specific cleavage of the !1viral strand of the double-stranded, replicative form of the !1phage DNA. GENETICS !$#gene II; X CLASSIFICATION #superfamily class I filamentous phage gene II protein KEYWORDS alternative initiators; DNA replication FEATURE !$1-410 #product gene II protein #status predicted #label !8GIIP\ !$300-410 #product gene X protein #status predicted #label GXP\ !$300 #modified_site N-formylmethionine (in mature form) !8#link GXP #status predicted SUMMARY #length 410 #molecular-weight 46236 #checksum 4568 SEQUENCE /// ENTRY Z2BPM3 #type complete TITLE gene II protein - phage M13 CONTAINS gene X protein ORGANISM #formal_name phage M13 DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 23-Jul-1999 ACCESSIONS B04264; A04264 REFERENCE A91470 !$#authors van Wezenbeek, P.M.G.F.; Hulsebos, T.J.M.; Schoenmakers, !1J.G.G. !$#journal Gene (1980) 11:129-148 !$#title Nucleotide sequence of the filamentous bacteriophage M13 DNA !1genome: comparison with phage fd. !$#cross-references MUID:81067903; PMID:6254849 !$#accession B04264 !'##molecule_type DNA !'##residues 1-410 ##label VAN !'##cross-references GB:V00604; GB:J02461; GB:M10377; NID:g14959; !1PIDN:CAA23856.1; PID:g14960 COMMENT The gene II protein is required for DNA replication. One of !1its major functions is the site-specific cleavage of the !1viral strand of the double-stranded, replicative form of the !1phage DNA. GENETICS !$#gene II CLASSIFICATION #superfamily class I filamentous phage gene II protein KEYWORDS DNA replication FEATURE !$300-410 #product gene X protein #status predicted #label GXP SUMMARY #length 410 #molecular-weight 46166 #checksum 4740 SEQUENCE /// ENTRY Z2BPF1 #type complete TITLE gene II protein - phage f1 CONTAINS gene X protein ORGANISM #formal_name phage f1 DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 23-Jul-1999 ACCESSIONS C04264; D04264; A04264; D04262 REFERENCE A91490 !$#authors Beck, E.; Zink, B. !$#journal Gene (1981) 16:35-58 !$#title Nucleotide sequence and genome organisation of filamentous !1bacteriophages f1 and fd. !$#cross-references MUID:82211801; PMID:6282703 !$#accession C04264 !'##molecule_type DNA !'##residues 1-410 ##label BEC !'##cross-references GB:V00606; GB:J02449; GB:M10881; NID:g14974; !1PIDN:CAA23876.1; PID:g603850 REFERENCE A92294 !$#authors Yen, T.S.B.; Webster, R.E. !$#journal J. Biol. Chem. (1981) 256:11259-11265 !$#title Bacteriophage f1 gene II and X proteins. Isolation and !1characterization of the products of two overlapping genes. !$#cross-references MUID:82030944; PMID:7026565 !$#accession D04264 !'##molecule_type protein !'##residues 1-410 ##label YEN !'##note the initiator methionine of the gene II protein is !1deformylated, whereas in the mature gene X protein it is not !1deformylated COMMENT The gene II protein is required for DNA replication. One of !1its major functions is the site-specific cleavage of the !1viral strand of the double-stranded, replicative form of the !1phage DNA. GENETICS !$#gene II; X CLASSIFICATION #superfamily class I filamentous phage gene II protein KEYWORDS alternative initiators; DNA replication FEATURE !$1-410 #product gene II protein #status experimental #label !8GIIP\ !$300-410 #product gene X protein #status experimental #label !8GXP\ !$1 #modified_site N-formylmethionine #link GIIP #status !8absent\ !$300 #modified_site N-formylmethionine (in mature form) !8#link GXP #status experimental SUMMARY #length 410 #molecular-weight 46167 #checksum 4614 SEQUENCE /// ENTRY Z2BPIK #type complete TITLE gene II protein - phage IKe CONTAINS gene X protein ORGANISM #formal_name phage IKe #note host Escherichia coli DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 28-Jul-2000 ACCESSIONS A04265 REFERENCE A92912 !$#authors Peeters, B.P.H.; Peters, R.M.; Schoenmakers, J.G.G.; !1Konings, R.N.H. !$#journal J. Mol. Biol. (1985) 181:27-39 !$#title Nucleotide sequence and genetic organization of the genome !1of the N-specific filamentous bacteriophage IKe. Comparison !1with the genome of the F-specific filamentous phages M13, fd !1and f1. !$#cross-references MUID:85160831; PMID:3981635 !$#accession A04265 !'##molecule_type DNA !'##residues 1-421 ##label PEE !'##cross-references GB:K02750; NID:g14942; PIDN:CAA26067.1; PID:g14943 COMMENT The gene II protein is required for DNA replication. GENETICS !$#gene II CLASSIFICATION #superfamily class I filamentous phage gene II protein KEYWORDS DNA replication FEATURE !$301-421 #product gene X protein #status predicted #label PXP SUMMARY #length 421 #molecular-weight 47594 #checksum 6235 SEQUENCE /// ENTRY Z3BPFD #type complete TITLE coat protein A precursor - phage fd ORGANISM #formal_name phage fd DATE 30-Sep-1980 #sequence_revision 18-Aug-1982 #text_change 23-Jul-1999 ACCESSIONS A04266; B04266 REFERENCE A93690 !$#authors Beck, E.; Sommer, R.; Auerswald, E.A.; Kurz, C.; Zink, B.; !1Osterburg, G.; Schaller, H.; Sugimoto, K.; Sugisaki, H.; !1Okamoto, T.; Takanami, M. !$#journal Nucleic Acids Res. (1978) 5:4495-4503 !$#title Nucleotide sequence of bacteriophage fd DNA. !$#cross-references MUID:79136480; PMID:745987 !$#accession A04266 !'##molecule_type DNA !'##residues 1-424 ##label BEC !'##cross-references GB:V00602; GB:J02451; GB:M10731; GB:M10767; !1GB:M21666; GB:M21667; GB:M21668; GB:M21669; GB:M21670; !1GB:M25198; NID:g14931; PIDN:CAA23851.1; PID:g579097 !'##experimental_source strain 478, Heidelberg REFERENCE A90402 !$#authors Goldsmith, M.E.; Konigsberg, W.H. !$#journal Biochemistry (1977) 16:2686-2694 !$#title Adsorption protein of the bacteriophage fd: isolation, !1molecular properties, and location in the virus. !$#cross-references MUID:77242231; PMID:329863 !$#accession B04266 !'##molecule_type protein !'##residues 1-24,'P',26,'P' ##label GOL COMMENT Coat protein A is necessary for adsorption of the virion !1onto the F-pilus of the host cell. There are about five !1copies of this protein per mature phage. They are located at !1the adsorption end of the phage particle. COMMENT Bacteriophages fd, M13, and f1 are male-specific filamentous !1coliphages. GENETICS !$#gene III CLASSIFICATION #superfamily class I filamentous phage coat protein A KEYWORDS coat protein FEATURE !$19-424 #product coat protein A #status predicted #label CPA SUMMARY #length 424 #molecular-weight 44637 #checksum 9808 SEQUENCE /// ENTRY Z3BPM3 #type complete TITLE coat protein A precursor - phage M13 ORGANISM #formal_name phage M13 DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 23-Jul-1999 ACCESSIONS C04266; A04266 REFERENCE A91470 !$#authors van Wezenbeek, P.M.G.F.; Hulsebos, T.J.M.; Schoenmakers, !1J.G.G. !$#journal Gene (1980) 11:129-148 !$#title Nucleotide sequence of the filamentous bacteriophage M13 DNA !1genome: comparison with phage fd. !$#cross-references MUID:81067903; PMID:6254849 !$#accession C04266 !'##molecule_type DNA !'##residues 1-424 ##label VAN !'##cross-references GB:V00604; GB:J02461; GB:M10377; NID:g14959; !1PIDN:CAA23862.1; PID:g579102 COMMENT Coat protein A is necessary for adsorption of the virion !1onto the F-pilus of the host cell. There are about five !1copies of this protein per mature phage. They are located at !1the adsorption end of the phage particle. COMMENT Bacteriophages fd, M13, and f1 are male-specific filamentous !1coliphages. GENETICS !$#gene III CLASSIFICATION #superfamily class I filamentous phage coat protein A KEYWORDS coat protein FEATURE !$19-424 #product coat protein A #status predicted #label CPA SUMMARY #length 424 #molecular-weight 44651 #checksum 9613 SEQUENCE /// ENTRY Z3BPF1 #type complete TITLE coat protein A precursor - phage f1 ORGANISM #formal_name phage f1 DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 31-Dec-1993 ACCESSIONS D04266; A04266 REFERENCE A91490 !$#authors Beck, E.; Zink, B. !$#journal Gene (1981) 16:35-58 !$#title Nucleotide sequence and genome organisation of filamentous !1bacteriophages f1 and fd. !$#cross-references MUID:82211801; PMID:6282703 !$#accession D04266 !'##molecule_type DNA !'##residues 1-424 ##label BEC COMMENT Coat protein A is necessary for adsorption of the virion !1onto the F-pilus of the host cell. There are about five !1copies of this protein per mature phage. They are located at !1the adsorption end of the phage particle. COMMENT Bacteriophage f1 is a male-specific filamentous coliphage. GENETICS !$#gene III CLASSIFICATION #superfamily class I filamentous phage coat protein A KEYWORDS coat protein FEATURE !$19-424 #product coat protein A #status predicted #label CPA SUMMARY #length 424 #molecular-weight 44721 #checksum 9577 SEQUENCE /// ENTRY Z3BPIK #type complete TITLE coat protein A - phage IKe ALTERNATE_NAMES gene III protein ORGANISM #formal_name phage IKe #note host Escherichia coli DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 28-Jul-2000 ACCESSIONS A04267 REFERENCE A92912 !$#authors Peeters, B.P.H.; Peters, R.M.; Schoenmakers, J.G.G.; !1Konings, R.N.H. !$#journal J. Mol. Biol. (1985) 181:27-39 !$#title Nucleotide sequence and genetic organization of the genome !1of the N-specific filamentous bacteriophage IKe. Comparison !1with the genome of the F-specific filamentous phages M13, fd !1and f1. !$#cross-references MUID:85160831; PMID:3981635 !$#accession A04267 !'##molecule_type DNA !'##residues 1-434 ##label PEE !'##cross-references GB:K02750; NID:g14942; PIDN:CAA26073.1; PID:g579099 COMMENT Coat protein A is necessary for adsorption of the virion !1onto the F-pilus of the host cell. GENETICS !$#gene III !$#start_codon GTG CLASSIFICATION #superfamily phage IKe coat protein A KEYWORDS adsorption; capsid protein SUMMARY #length 434 #molecular-weight 45574 #checksum 9885 SEQUENCE /// ENTRY Z4BPFD #type complete TITLE gene IV protein - phage fd (strain 478, Heidelberg) ORGANISM #formal_name phage fd DATE 30-Sep-1980 #sequence_revision 30-Sep-1980 #text_change 23-Jul-1999 ACCESSIONS A04268 REFERENCE A93690 !$#authors Beck, E.; Sommer, R.; Auerswald, E.A.; Kurz, C.; Zink, B.; !1Osterburg, G.; Schaller, H.; Sugimoto, K.; Sugisaki, H.; !1Okamoto, T.; Takanami, M. !$#journal Nucleic Acids Res. (1978) 5:4495-4503 !$#title Nucleotide sequence of bacteriophage fd DNA. !$#cross-references MUID:79136480; PMID:745987 !$#accession A04268 !'##molecule_type DNA !'##residues 1-426 ##label BEC !'##cross-references GB:V00602; GB:J02451; GB:M10731; GB:M10767; !1GB:M21666; GB:M21667; GB:M21668; GB:M21669; GB:M21670; !1GB:M25198; NID:g14931; PIDN:CAA23854.1; PID:g14941 COMMENT The exact function of this protein is unknown although it !1may be involved in phage assembly. GENETICS !$#gene IV CLASSIFICATION #superfamily filamentous phage gene IV protein KEYWORDS phage maturation SUMMARY #length 426 #molecular-weight 45822 #checksum 2670 SEQUENCE /// ENTRY Z4BPM3 #type complete TITLE gene IV protein - phage M13 ORGANISM #formal_name phage M13 DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 11-Nov-1996 ACCESSIONS B04268; A04268 REFERENCE A91470 !$#authors van Wezenbeek, P.M.G.F.; Hulsebos, T.J.M.; Schoenmakers, !1J.G.G. !$#journal Gene (1980) 11:129-148 !$#title Nucleotide sequence of the filamentous bacteriophage M13 DNA !1genome: comparison with phage fd. !$#cross-references MUID:81067903; PMID:6254849 !$#accession B04268 !'##molecule_type DNA !'##residues 1-426 ##label VAN COMMENT The exact function of this protein is unknown although it !1may be involved in phage assembly. GENETICS !$#gene IV CLASSIFICATION #superfamily filamentous phage gene IV protein KEYWORDS phage maturation SUMMARY #length 426 #molecular-weight 45860 #checksum 2783 SEQUENCE /// ENTRY Z4BPF1 #type complete TITLE gene IV protein - phage f1 ORGANISM #formal_name phage f1 DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 23-Jul-1999 ACCESSIONS C04268; A04268 REFERENCE A91490 !$#authors Beck, E.; Zink, B. !$#journal Gene (1981) 16:35-58 !$#title Nucleotide sequence and genome organisation of filamentous !1bacteriophages f1 and fd. !$#cross-references MUID:82211801; PMID:6282703 !$#accession C04268 !'##molecule_type DNA !'##residues 1-426 ##label BEC !'##cross-references GB:V00606; GB:J02449; GB:M10881; NID:g14974; !1PIDN:CAA23875.1; PID:g14983 COMMENT The exact function of this protein is unknown although it !1may be involved in phage assembly. GENETICS !$#gene IV CLASSIFICATION #superfamily filamentous phage gene IV protein KEYWORDS phage maturation SUMMARY #length 426 #molecular-weight 45841 #checksum 2690 SEQUENCE /// ENTRY Z4BPIK #type complete TITLE gene IV protein - phage IKe ORGANISM #formal_name phage IKe #note host Escherichia coli DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 28-Jul-2000 ACCESSIONS A04269 REFERENCE A92912 !$#authors Peeters, B.P.H.; Peters, R.M.; Schoenmakers, J.G.G.; !1Konings, R.N.H. !$#journal J. Mol. Biol. (1985) 181:27-39 !$#title Nucleotide sequence and genetic organization of the genome !1of the N-specific filamentous bacteriophage IKe. Comparison !1with the genome of the F-specific filamentous phages M13, fd !1and f1. !$#cross-references MUID:85160831; PMID:3981635 !$#accession A04269 !'##molecule_type DNA !'##residues 1-437 ##label PEE !'##cross-references GB:K02750; NID:g14942; PIDN:CAA26076.1; PID:g14956 COMMENT The exact function of this protein is not known, although it !1may be involved in phage assembly. GENETICS !$#gene IV CLASSIFICATION #superfamily filamentous phage gene IV protein KEYWORDS phage maturation SUMMARY #length 437 #molecular-weight 46485 #checksum 9846 SEQUENCE /// ENTRY Z4BP33 #type complete TITLE gene 430 protein - phage Pf3 ORGANISM #formal_name phage Pf3 #note host Pseudomonas aeruginosa DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 24-Sep-1999 ACCESSIONS A04270 REFERENCE A94693 !$#authors Luiten, R.G.M.; Putterman, D.G.; Schoenmakers, J.G.G.; !1Konings, R.N.H.; Day, L.A. !$#journal J. Virol. (1985) 56:268-276 !$#title Nucleotide sequence of the genome of Pf3, an IncP-1 !1plasmid-specific filamentous bacteriophage of Pseudomonas !1aeruginosa. !$#cross-references MUID:85293231; PMID:3928901 !$#accession A04270 !'##molecule_type DNA !'##residues 1-430 ##label LUI !'##cross-references GB:M11912; NID:g215371; PIDN:AAA88381.1; !1PID:g215375 COMMENT Bacteriophage Pf3 is a class II filamentous phage. COMMENT The host is strain O harboring IncP1 plasmids. GENETICS !$#gene 430 CLASSIFICATION #superfamily filamentous phage gene IV protein KEYWORDS phage maturation SUMMARY #length 430 #molecular-weight 46490 #checksum 5887 SEQUENCE /// ENTRY DDBPFD #type complete TITLE helix-destabilizing protein [validated] - phage fd ORGANISM #formal_name phage fd DATE 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 15-Sep-2000 ACCESSIONS A04271; B04271 REFERENCE A93690 !$#authors Beck, E.; Sommer, R.; Auerswald, E.A.; Kurz, C.; Zink, B.; !1Osterburg, G.; Schaller, H.; Sugimoto, K.; Sugisaki, H.; !1Okamoto, T.; Takanami, M. !$#journal Nucleic Acids Res. (1978) 5:4495-4503 !$#title Nucleotide sequence of bacteriophage fd DNA. !$#cross-references MUID:79136480; PMID:745987 !$#accession A04271 !'##molecule_type DNA !'##residues 1-87 ##label BEC !'##cross-references GB:V00602; GB:J02451; GB:M10731; GB:M10767; !1GB:M21666; GB:M21667; GB:M21668; GB:M21669; GB:M21670; !1GB:M25198; NID:g14931; PIDN:CAA23847.1; PID:g14934 !'##experimental_source strain 478, Heidelberg REFERENCE A91404 !$#authors Nakashima, Y.; Dunker, A.K.; Marvin, D.A.; Konigsberg, W. !$#journal FEBS Lett. (1974) 40:290-292 !$#title The amino acid sequence of a DNA binding protein, the gene 5 !1product of fd filamentous bacteriophage. !$#cross-references MUID:74308150; PMID:4605211 !$#accession B04271 !'##molecule_type protein !'##residues 1-87 ##label NAK REFERENCE A90728 !$#authors McPherson, A.; Jurnak, F.; Wang, A.; Kolpak, F.; Rich, A.; !1Molineux, I.; Fitzgerald, P. !$#journal Biophys. J. (1980) 32:155-173 !$#title The structure of a DNA unwinding protein and its complexes !1with oligo-deoxynucleotides by x-ray diffraction. !$#cross-references MUID:81233192; PMID:6264986 !$#contents annotation; X-ray crystallography, 2.3 angstroms REFERENCE A50452 !$#authors Brayer, G.D.; McPherson, A. !$#submission submitted to the Brookhaven Protein Data Bank, January 1986 !$#cross-references PDB:2GN5 !$#contents annotation; X-ray crystallography, 2.3 angstroms, residues !11-87 REFERENCE A58702 !$#authors Brayer, G.D.; McPherson, A. !$#journal J. Mol. Biol. (1983) 169:565-596 !$#title Refined structure of the gene 5 DNA binding protein from !1bacteriophage fd. !$#cross-references MUID:84010877; PMID:6684697 !$#contents annotation; X-ray crystallography, 2.3 angstroms COMMENT The helix-destabilizing protein is displaced by the coat !1protein (on the inner bacterial membrane) during phage !1assembly. GENETICS !$#gene V COMPLEX monomer; homodimer associated with DNA FUNCTION !$#description monomers bind to single-stranded, progeny viral DNA, !1dimerize and both prevent the conversion of the DNA to a !1double-stranded replicative form and protect it from !1nuclease attack CLASSIFICATION #superfamily class I filamentous phage helix-destabilizing !1protein KEYWORDS DNA binding; helix-destabilization; homodimer FEATURE !$41 #binding_site DNA (Tyr) #status predicted SUMMARY #length 87 #molecular-weight 9688 #checksum 3268 SEQUENCE /// ENTRY DDBPM3 #type complete TITLE helix-destabilizing protein [validated] - phage M13 ORGANISM #formal_name phage M13 DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 15-Sep-2000 ACCESSIONS C04271; D04271; S08796; A04271; S08797 REFERENCE A91470 !$#authors van Wezenbeek, P.M.G.F.; Hulsebos, T.J.M.; Schoenmakers, !1J.G.G. !$#journal Gene (1980) 11:129-148 !$#title Nucleotide sequence of the filamentous bacteriophage M13 DNA !1genome: comparison with phage fd. !$#cross-references MUID:81067903; PMID:6254849 !$#accession C04271 !'##molecule_type DNA !'##residues 1-87 ##label VAW !'##cross-references GB:V00604; GB:J02461; GB:M10377; NID:g14959; !1PIDN:CAA23858.1; PID:g14962 REFERENCE A90192 !$#authors Cuypers, T.; van der Ouderaa, F.J.; de Jong, W.W. !$#journal Biochem. Biophys. Res. Commun. (1974) 59:557-563 !$#title The amino acid sequence of gene 5 protein of bacteriophage M !113. !$#cross-references MUID:74308151; PMID:4605212 !$#accession D04271 !'##molecule_type protein !'##residues 1-19;87 ##label CUY REFERENCE S08795 !$#authors van Duynhoven, J.P.M.; Folkers, P.J.M.; Stassen, A.P.M.; !1Harmsen, B.J.M.; Konings, R.N.H.; Hilbers, C.W. !$#journal FEBS Lett. (1990) 261:1-4 !$#title Structure of the DNA binding wing of the gene-V encoded !1single-stranded DNA binding protein of the filamentous !1bacteriophage M13. !$#cross-references MUID:90169094; PMID:2307226 !$#accession S08796 !'##molecule_type protein !'##residues 13-31 ##label VAD REFERENCE A67931 !$#authors Folkers, P.J.M.; Nilges, M.; Folmer, R.H.A.; Prompers, J.J.; !1Konings, R.N.H.; Hilbers, C.W. !$#submission submitted to the Brookhaven Protein Data Bank, July 1995 !$#cross-references PDB:2GVA !$#contents annotation; conformation by (1)H-NMR, residues 1-40,'H', !142-87 REFERENCE A58704 !$#authors Folkers, P.J.M.; Nilges, M.; Folmer, R.H.A.; Konings, !1R.N.H.; Hilbers, C.W. !$#journal J. Mol. Biol. (1994) 236:229-246 !$#title The solution structure of the Tyr41-->His mutant of the !1single-stranded DNA binding protein encoded by gene V of the !1filamentous bacteriophage M13. !$#cross-references MUID:94149718; PMID:8107108 !$#contents annotation; conformation by (1)H-NMR COMMENT The helix-destabilizing protein is displaced by the coat !1protein (on the inner bacterial membrane) during phage !1assembly. GENETICS !$#gene V COMPLEX monomer; homodimer associated with DNA FUNCTION !$#description monomers bind to single-stranded, progeny viral DNA, !1dimerize and both prevent the conversion of the DNA to a !1double-stranded replicative form and protect it from !1nuclease attack CLASSIFICATION #superfamily class I filamentous phage helix-destabilizing !1protein KEYWORDS DNA binding; helix-destabilization; homodimer FEATURE !$41 #binding_site DNA (Tyr) #status predicted SUMMARY #length 87 #molecular-weight 9688 #checksum 3268 SEQUENCE /// ENTRY DDBPF1 #type complete TITLE helix-destabilizing protein [validated] - phage f1 ORGANISM #formal_name phage f1 DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 15-Sep-2000 ACCESSIONS E04271; F04271; A04271 REFERENCE A91490 !$#authors Beck, E.; Zink, B. !$#journal Gene (1981) 16:35-58 !$#title Nucleotide sequence and genome organisation of filamentous !1bacteriophages f1 and fd. !$#cross-references MUID:82211801; PMID:6282703 !$#accession E04271 !'##molecule_type DNA !'##residues 1-87 ##label BEC !'##cross-references GB:V00606; GB:J02449; GB:M10881; NID:g14974; !1PIDN:CAA23868.1; PID:g14976 REFERENCE A92980 !$#authors Hill, D.F.; Petersen, G.B. !$#journal J. Virol. (1980) 34:40-50 !$#title Nucleotide sequences in bacteriophage f1 DNA: nucleotide !1sequence of genes V, VII, and VIII. !$#cross-references MUID:80185134; PMID:7373712 !$#accession F04271 !'##molecule_type DNA !'##residues 1-87 ##label HIL !'##cross-references GB:J02450; NID:g166212 !'##note the codon given for 28-Leu (GTG) is inconsistent with the !1authors' translation and with the given anti-codon !'##note the authors translated the codon CAA for residue 40 as Glu REFERENCE A51052 !$#authors Skinner, M.M.; Zhang, H.; Leschnitzer, D.H.; Guan, Y.; !1Bellamy, H.; Sweet, R.M.; Gray, C.W.; Konings, R.N.H.; Wang, !1A.H.J.; Terwilliger, T.C. !$#submission submitted to the Brookhaven Protein Data Bank, August 1993 !$#cross-references PDB:1BGH !$#contents annotation; X-ray crystallography, 1.8 angstroms, residues !12-86 REFERENCE A52991 !$#authors Guan, Y.; Zhang, H.; Wang, A.H.J. !$#submission submitted to the Brookhaven Protein Data Bank, November 1994 !$#cross-references PDB:1GPV !$#contents annotation; conformation by theoretical model, residues 1-87 REFERENCE A54207 !$#authors Guan, Y.; Zhang, H.; Konings, R.N.H.; Hilbers, C.W.; !1Terwilliger, T.C.; Wang, A.H.J. !$#journal Biochemistry (1994) 33:7768-7778 !$#title Crystal structures of Y41H and Y41F mutants of gene V !1protein from Ff phage suggest possible protein-protein !1interactions in the GVP-ssDNA complex. !$#cross-references MUID:94281208; PMID:8011642 !$#contents annotation; X-ray crystallography, 1.8 angstroms REFERENCE A66881 !$#authors Skinner, M.M.; Zhang, H.; Leschnitzer, D.H.; Guan, Y.; !1Bellamy, H.; Sweet, R.M.; Gray, C.W.; Konings, R.N.H.; Wang, !1A.H.J.; Terwilliger, T.C. !$#submission submitted to the Brookhaven Protein Data Bank, August 1996 !$#cross-references PDB:1VQB !$#contents annotation; X-ray crystallography, 1.8 angstroms COMMENT The helix-destabilizing protein is displaced by the coat !1protein (on the inner bacterial membrane) during phage !1assembly. GENETICS !$#gene V COMPLEX monomer; homodimer associated with DNA FUNCTION !$#description monomers bind to single-stranded, progeny viral DNA, !1dimerize and both prevent the conversion of the DNA to a !1double-stranded replicative form and protect it from !1nuclease attack CLASSIFICATION #superfamily class I filamentous phage helix-destabilizing !1protein KEYWORDS DNA binding; helix-destabilization; homodimer FEATURE !$41 #binding_site DNA (Tyr) #status predicted SUMMARY #length 87 #molecular-weight 9688 #checksum 3268 SEQUENCE /// ENTRY DDBPIK #type complete TITLE helix-destabilizing protein - phage IKe ALTERNATE_NAMES single-stranded DNA binding protein ORGANISM #formal_name phage IKe #note host Escherichia coli DATE 18-Apr-1984 #sequence_revision 18-Apr-1984 #text_change 28-Jul-2000 ACCESSIONS A04272; S08795 REFERENCE A92912 !$#authors Peeters, B.P.H.; Peters, R.M.; Schoenmakers, J.G.G.; !1Konings, R.N.H. !$#journal J. Mol. Biol. (1985) 181:27-39 !$#title Nucleotide sequence and genetic organization of the genome !1of the N-specific filamentous bacteriophage IKe. Comparison !1with the genome of the F-specific filamentous phages M13, fd !1and f1. !$#cross-references MUID:85160831; PMID:3981635 !$#accession A04272 !'##molecule_type DNA !'##residues 1-88 ##label PEE !'##cross-references GB:K02750; GB:X02139; NID:g14942; PIDN:CAA26069.1; !1PID:g14945 !'##note the reading frame was confirmed by determination of the amino !1acid composition and the sequence of residues 1-13 REFERENCE S08795 !$#authors van Duynhoven, J.P.M.; Folkers, P.J.M.; Stassen, A.P.M.; !1Harmsen, B.J.M.; Konings, R.N.H.; Hilbers, C.W. !$#journal FEBS Lett. (1990) 261:1-4 !$#title Structure of the DNA binding wing of the gene-V encoded !1single-stranded DNA binding protein of the filamentous !1bacteriophage M13. !$#cross-references MUID:90169094; PMID:2307226 !$#accession S08795 !'##status preliminary !'##molecule_type protein !'##residues 13-32 ##label VAN GENETICS !$#gene V CLASSIFICATION #superfamily class I filamentous phage helix-destabilizing !1protein KEYWORDS DNA binding; helix-destabilization FEATURE !$42 #binding_site DNA (Tyr) #status predicted SUMMARY #length 88 #molecular-weight 9813 #checksum 5243 SEQUENCE /// ENTRY DDBPPF #type complete TITLE helix-destabilizing protein - phage Pf1 ALTERNATE_NAMES gene 5 protein; single-stranded DNA-binding protein ORGANISM #formal_name phage Pf1 DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 23-Jul-1999 ACCESSIONS A04273; B04273; S20696; S15140 REFERENCE A04273 !$#authors Maeda, K.; Kneale, G.G.; Tsugita, A.; Short, N.J.; Perham, !1R.N.; Hill, D.F.; Petersen, G.B. !$#journal EMBO J. (1982) 1:255-261 !$#title The DNA-binding protein of Pf1 filamentous bacteriophage: !1amino-acid sequence and structure of the gene. !$#accession A04273 !'##molecule_type DNA !'##residues 1-144 ##label MAE1 !$#accession B04273 !'##molecule_type protein !'##residues 1-10,12-144 ##label MAE2 !'##note the discrepancy between the DNA and protein sequences may be !1the result of an unusual resistance of the Val-Val bond, at !1positions 10 and 11, to acid hydrolysis !'##note the mature protein generally starts with Met-1 but occasionally !1starts with Asn-2 REFERENCE S20696 !$#authors Hill, D.F.; Short, N.J.; Perham, R.N.; Petersen, G.B. !$#submission submitted to the EMBL Data Library, March 1990 !$#description The DNA sequence of the filamentous bacteriophage pf1. !$#accession S20696 !'##status preliminary !'##molecule_type DNA !'##residues 1-144 ##label HIL !'##cross-references EMBL:X52107; NID:g14829; PIDN:CAA36328.1; !1PID:g14830 REFERENCE S15140 !$#authors Hill, D.F.; Short, N.J.; Perham, R.N.; Petersen, G.B. !$#journal J. Mol. Biol. (1991) 218:349-364 !$#title DNA sequence of the filamentous bacteriophage Pf1. !$#cross-references MUID:91186399; PMID:2010913 !$#accession S15140 !'##molecule_type DNA !'##residues 1-144 ##label JMO !'##cross-references EMBL:X52107; NID:g14829; PIDN:CAA36328.1; !1PID:g14830 !'##experimental_source ATCC 25102-B1 GENETICS !$#gene 5 CLASSIFICATION #superfamily phage Pf1 helix-destabilizing protein KEYWORDS single-stranded DNA binding SUMMARY #length 144 #molecular-weight 15428 #checksum 6724 SEQUENCE /// ENTRY DNBPP3 #type complete TITLE helix-destabilizing protein - phage Pf3 ORGANISM #formal_name phage Pf3 #note host Pseudomonas aeruginosa DATE 15-Nov-1984 #sequence_revision 15-Nov-1984 #text_change 24-Sep-1999 ACCESSIONS A04274 REFERENCE A94693 !$#authors Luiten, R.G.M.; Putterman, D.G.; Schoenmakers, J.G.G.; !1Konings, R.N.H.; Day, L.A. !$#journal J. Virol. (1985) 56:268-276 !$#title Nucleotide sequence of the genome of Pf3, an IncP-1 !1plasmid-specific filamentous bacteriophage of Pseudomonas !1aeruginosa. !$#cross-references MUID:85293231; PMID:3928901 !$#accession A04274 !'##molecule_type DNA !'##residues 1-78 ##label LUI !'##cross-references GB:M11912; NID:g215371; PIDN:AAA88385.1; !1PID:g215379 COMMENT Bacteriophage Pf3 is a class II filamentous phage. COMMENT The host is strain O harboring IncP1 plasmids. GENETICS !$#gene 78 CLASSIFICATION #superfamily class II filamentous phage helix-destabilizing !1protein KEYWORDS DNA binding; replication SUMMARY #length 78 #molecular-weight 8903 #checksum 4734 SEQUENCE /// ENTRY Z6BPFD #type complete TITLE coat protein D - phage fd ORGANISM #formal_name phage fd DATE 30-Sep-1980 #sequence_revision 29-Jun-1981 #text_change 23-Jul-1999 ACCESSIONS A04275 REFERENCE A93690 !$#authors Beck, E.; Sommer, R.; Auerswald, E.A.; Kurz, C.; Zink, B.; !1Osterburg, G.; Schaller, H.; Sugimoto, K.; Sugisaki, H.; !1Okamoto, T.; Takanami, M. !$#journal Nucleic Acids Res. (1978) 5:4495-4503 !$#title Nucleotide sequence of bacteriophage fd DNA. !$#cross-references MUID:79136480; PMID:745987 !$#accession A04275 !'##molecule_type DNA !'##residues 1-112 ##label BEC !'##cross-references GB:V00602; GB:J02451; GB:M10731; GB:M10767; !1GB:M21666; GB:M21667; GB:M21668; GB:M21669; GB:M21670; !1GB:M25198; NID:g14931; PIDN:CAA23852.1; PID:g14939 !'##experimental_source strain 478, Heidelberg REFERENCE A92264 !$#authors Lin, T.C.; Webster, R.E.; Konigsberg, W. !$#journal J. Biol. Chem. (1980) 255:10331-10337 !$#title Isolation and characterization of the C and D proteins coded !1by gene IX and gene VI in the filamentous bacteriophage fl !1and fd. !$#cross-references MUID:81046866; PMID:7000776 !$#contents annotation !$#note the protein was isolated from the mature phages and !1identified as the gene VI product on the basis of !1composition. Met was determined to be the amino-terminal !1residue COMMENT There are about five copies of coat protein D in the mature !1phage particle. They are believed to be located at the same !1end of the filamentous particle as coat protein A. GENETICS !$#gene VI CLASSIFICATION #superfamily filamentous phage coat protein D KEYWORDS coat protein SUMMARY #length 112 #molecular-weight 12350 #checksum 2292 SEQUENCE /// ENTRY Z6BPM3 #type complete TITLE coat protein D - phage M13 ORGANISM #formal_name phage M13 DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 23-Jul-1999 ACCESSIONS B04275; A04275 REFERENCE A91470 !$#authors van Wezenbeek, P.M.G.F.; Hulsebos, T.J.M.; Schoenmakers, !1J.G.G. !$#journal Gene (1980) 11:129-148 !$#title Nucleotide sequence of the filamentous bacteriophage M13 DNA !1genome: comparison with phage fd. !$#cross-references MUID:81067903; PMID:6254849 !$#accession B04275 !'##molecule_type DNA !'##residues 1-112 ##label VAN !'##cross-references GB:V00604; GB:J02461; GB:M10377; NID:g14959; !1PIDN:CAA23863.1; PID:g14967 COMMENT There are about five copies of coat protein D in the mature !1phage particle. They are believed to be located at the same !1end of the filamentous particle as coat protein A. GENETICS !$#gene VI CLASSIFICATION #superfamily filamentous phage coat protein D KEYWORDS coat protein SUMMARY #length 112 #molecular-weight 12350 #checksum 2292 SEQUENCE /// ENTRY Z6BPF1 #type complete TITLE coat protein D - phage f1 ORGANISM #formal_name phage f1 DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 23-Jul-1999 ACCESSIONS C04275; A04275 REFERENCE A91490 !$#authors Beck, E.; Zink, B. !$#journal Gene (1981) 16:35-58 !$#title Nucleotide sequence and genome organisation of filamentous !1bacteriophages f1 and fd. !$#cross-references MUID:82211801; PMID:6282703 !$#accession C04275 !'##molecule_type DNA !'##residues 1-112 ##label BEC !'##cross-references GB:V00606; GB:J02449; GB:M10881; NID:g14974; !1PIDN:CAA23873.1; PID:g14981 REFERENCE A92264 !$#authors Lin, T.C.; Webster, R.E.; Konigsberg, W. !$#journal J. Biol. Chem. (1980) 255:10331-10337 !$#title Isolation and characterization of the C and D proteins coded !1by gene IX and gene VI in the filamentous bacteriophage fl !1and fd. !$#cross-references MUID:81046866; PMID:7000776 !$#contents annotation !$#note the protein was isolated from the mature phages and !1identified as the gene VI product on the basis of !1composition. Met was determined to be the amino-terminal !1residue COMMENT There are about five copies of coat protein D in the mature !1phage particle. They are believed to be located at the same !1end of the filamentous particle as coat protein A. GENETICS !$#gene VI CLASSIFICATION #superfamily filamentous phage coat protein D KEYWORDS coat protein SUMMARY #length 112 #molecular-weight 12350 #checksum 2292 SEQUENCE /// ENTRY Z6BPIK #type complete TITLE coat protein D - phage IKe ALTERNATE_NAMES gene VI protein ORGANISM #formal_name phage IKe #note host Escherichia coli DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 28-Jul-2000 ACCESSIONS A04276 REFERENCE A92912 !$#authors Peeters, B.P.H.; Peters, R.M.; Schoenmakers, J.G.G.; !1Konings, R.N.H. !$#journal J. Mol. Biol. (1985) 181:27-39 !$#title Nucleotide sequence and genetic organization of the genome !1of the N-specific filamentous bacteriophage IKe. Comparison !1with the genome of the F-specific filamentous phages M13, fd !1and f1. !$#cross-references MUID:85160831; PMID:3981635 !$#accession A04276 !'##molecule_type DNA !'##residues 1-116 ##label PEE !'##cross-references GB:K02750; NID:g14942; PIDN:CAA26074.1; PID:g14954 GENETICS !$#gene VI CLASSIFICATION #superfamily filamentous phage coat protein D KEYWORDS capsid protein SUMMARY #length 116 #molecular-weight 12117 #checksum 630 SEQUENCE /// ENTRY Z7BPFD #type complete TITLE coat protein C chain I - phage fd (strain 478, Heidelberg) ORGANISM #formal_name phage fd DATE 30-Sep-1980 #sequence_revision 30-Sep-1980 #text_change 23-Jul-1999 ACCESSIONS A04277 REFERENCE A93690 !$#authors Beck, E.; Sommer, R.; Auerswald, E.A.; Kurz, C.; Zink, B.; !1Osterburg, G.; Schaller, H.; Sugimoto, K.; Sugisaki, H.; !1Okamoto, T.; Takanami, M. !$#journal Nucleic Acids Res. (1978) 5:4495-4503 !$#title Nucleotide sequence of bacteriophage fd DNA. !$#cross-references MUID:79136480; PMID:745987 !$#accession A04277 !'##molecule_type DNA !'##residues 1-33 ##label BEC !'##cross-references GB:V00602; GB:J02451; GB:M10731; GB:M10767; !1GB:M21666; GB:M21667; GB:M21668; GB:M21669; GB:M21670; !1GB:M25198; NID:g14931; PIDN:CAA23848.1; PID:g14935 GENETICS !$#gene VII CLASSIFICATION #superfamily class I filamentous phage coat protein C chain !1I KEYWORDS coat protein; heterodimer SUMMARY #length 33 #molecular-weight 3602 #checksum 1924 SEQUENCE /// ENTRY Z7BPM3 #type complete TITLE coat protein C chain I - phage M13 ORGANISM #formal_name phage M13 DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 23-Jul-1999 ACCESSIONS B04277; A04277 REFERENCE A91470 !$#authors van Wezenbeek, P.M.G.F.; Hulsebos, T.J.M.; Schoenmakers, !1J.G.G. !$#journal Gene (1980) 11:129-148 !$#title Nucleotide sequence of the filamentous bacteriophage M13 DNA !1genome: comparison with phage fd. !$#cross-references MUID:81067903; PMID:6254849 !$#accession B04277 !'##molecule_type DNA !'##residues 1-33 ##label VAN !'##cross-references GB:V00604; GB:J02461; GB:M10377; NID:g14959; !1PIDN:CAA23859.1; PID:g14963 REFERENCE A93880 !$#authors Simons, G.F.M.; Konings, R.N.H.; Schoenmakers, J.G.G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:4194-4198 !$#title Genes VI, VII, and IX of phage M13 code for minor capsid !1proteins of the virion. !$#cross-references MUID:82037805; PMID:6945579 !$#contents annotation !$#note identification of the gene VII product as a subunit of coat !1protein C !$#note there are three or four copies of this protein in the mature !1phage particle; the are located at the opposite end of the !1filamentous particle from coat proteins A and D GENETICS !$#gene VII CLASSIFICATION #superfamily class I filamentous phage coat protein C chain !1I KEYWORDS coat protein; heterodimer SUMMARY #length 33 #molecular-weight 3602 #checksum 1924 SEQUENCE /// ENTRY Z7BPF1 #type complete TITLE coat protein C chain I - phage f1 ORGANISM #formal_name phage f1 DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 23-Jul-1999 ACCESSIONS C04277; D04277; A04277 REFERENCE A91490 !$#authors Beck, E.; Zink, B. !$#journal Gene (1981) 16:35-58 !$#title Nucleotide sequence and genome organisation of filamentous !1bacteriophages f1 and fd. !$#cross-references MUID:82211801; PMID:6282703 !$#accession C04277 !'##molecule_type DNA !'##residues 1-33 ##label BEC !'##cross-references GB:V00606; GB:J02449; GB:M10881; NID:g14974; !1PIDN:CAA23869.1; PID:g14977 REFERENCE A92980 !$#authors Hill, D.F.; Petersen, G.B. !$#journal J. Virol. (1980) 34:40-50 !$#title Nucleotide sequences in bacteriophage f1 DNA: nucleotide !1sequence of genes V, VII, and VIII. !$#cross-references MUID:80185134; PMID:7373712 !$#accession D04277 !'##molecule_type DNA !'##residues 1-33 ##label HIL GENETICS !$#gene VII CLASSIFICATION #superfamily class I filamentous phage coat protein C chain !1I KEYWORDS coat protein; heterodimer SUMMARY #length 33 #molecular-weight 3602 #checksum 1924 SEQUENCE /// ENTRY Z7BPIK #type complete TITLE coat protein C chain I - phage IKe ALTERNATE_NAMES gene VII protein ORGANISM #formal_name phage IKe #note host Escherichia coli DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 28-Jul-2000 ACCESSIONS A04278 REFERENCE A92912 !$#authors Peeters, B.P.H.; Peters, R.M.; Schoenmakers, J.G.G.; !1Konings, R.N.H. !$#journal J. Mol. Biol. (1985) 181:27-39 !$#title Nucleotide sequence and genetic organization of the genome !1of the N-specific filamentous bacteriophage IKe. Comparison !1with the genome of the F-specific filamentous phages M13, fd !1and f1. !$#cross-references MUID:85160831; PMID:3981635 !$#accession A04278 !'##molecule_type DNA !'##residues 1-32 ##label PEE !'##cross-references GB:K02750; NID:g14942; PIDN:CAA26070.1; PID:g14946 GENETICS !$#gene VII CLASSIFICATION #superfamily class I filamentous phage coat protein C chain !1I KEYWORDS capsid protein; heterodimer SUMMARY #length 32 #molecular-weight 3351 #checksum 9976 SEQUENCE /// ENTRY Z9BPFD #type complete TITLE coat protein C chain II - phage fd (strain 478, Heidelberg) ORGANISM #formal_name phage fd DATE 30-Sep-1980 #sequence_revision 30-Sep-1980 #text_change 23-Jul-1999 ACCESSIONS A04279 REFERENCE A93690 !$#authors Beck, E.; Sommer, R.; Auerswald, E.A.; Kurz, C.; Zink, B.; !1Osterburg, G.; Schaller, H.; Sugimoto, K.; Sugisaki, H.; !1Okamoto, T.; Takanami, M. !$#journal Nucleic Acids Res. (1978) 5:4495-4503 !$#title Nucleotide sequence of bacteriophage fd DNA. !$#cross-references MUID:79136480; PMID:745987 !$#accession A04279 !'##molecule_type DNA !'##residues 1-32 ##label BEC !'##cross-references GB:V00602; GB:J02451; GB:M10731; GB:M10767; !1GB:M21666; GB:M21667; GB:M21668; GB:M21669; GB:M21670; !1GB:M25198; NID:g14931; PIDN:CAA23849.1; PID:g14936 GENETICS !$#gene IX CLASSIFICATION #superfamily class I filamentous phage coat protein C chain !1II KEYWORDS coat protein; heterodimer SUMMARY #length 32 #molecular-weight 3653 #checksum 1549 SEQUENCE /// ENTRY Z9BPM3 #type complete TITLE coat protein C chain II - phage M13 ORGANISM #formal_name phage M13 DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 23-Jul-1999 ACCESSIONS B04279; A04279 REFERENCE A91470 !$#authors van Wezenbeek, P.M.G.F.; Hulsebos, T.J.M.; Schoenmakers, !1J.G.G. !$#journal Gene (1980) 11:129-148 !$#title Nucleotide sequence of the filamentous bacteriophage M13 DNA !1genome: comparison with phage fd. !$#cross-references MUID:81067903; PMID:6254849 !$#accession B04279 !'##molecule_type DNA !'##residues 1-32 ##label VAN !'##cross-references GB:V00604; GB:J02461; GB:M10377; NID:g14959; !1PIDN:CAA23860.1; PID:g14964 REFERENCE A93880 !$#authors Simons, G.F.M.; Konings, R.N.H.; Schoenmakers, J.G.G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:4194-4198 !$#title Genes VI, VII, and IX of phage M13 code for minor capsid !1proteins of the virion. !$#cross-references MUID:82037805; PMID:6945579 !$#contents annotation !$#note identification of the gene IX product as a subunit of coat !1protein C !$#note there are three or four copies of this protein in the mature !1phage particle; the are located at the opposite end of the !1filamentous particle from coat proteins A and D GENETICS !$#gene IX CLASSIFICATION #superfamily class I filamentous phage coat protein C chain !1II KEYWORDS coat protein; heterodimer SUMMARY #length 32 #molecular-weight 3653 #checksum 1549 SEQUENCE /// ENTRY Z9BPF1 #type complete TITLE coat protein C chain II - phage f1 ORGANISM #formal_name phage f1 DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 23-Jul-1999 ACCESSIONS C04279; D04279; A04279 REFERENCE A91490 !$#authors Beck, E.; Zink, B. !$#journal Gene (1981) 16:35-58 !$#title Nucleotide sequence and genome organisation of filamentous !1bacteriophages f1 and fd. !$#cross-references MUID:82211801; PMID:6282703 !$#accession C04279 !'##molecule_type DNA !'##residues 1-32 ##label BEC !'##cross-references GB:V00606; GB:J02449; GB:M10881; NID:g14974; !1PIDN:CAA23870.1; PID:g14978 REFERENCE A92980 !$#authors Hill, D.F.; Petersen, G.B. !$#journal J. Virol. (1980) 34:40-50 !$#title Nucleotide sequences in bacteriophage f1 DNA: nucleotide !1sequence of genes V, VII, and VIII. !$#cross-references MUID:80185134; PMID:7373712 !$#accession D04279 !'##molecule_type DNA !'##residues 1-32 ##label HIL GENETICS !$#gene IX CLASSIFICATION #superfamily class I filamentous phage coat protein C chain !1II KEYWORDS coat protein; heterodimer SUMMARY #length 32 #molecular-weight 3653 #checksum 1549 SEQUENCE /// ENTRY Z9BPIK #type complete TITLE coat protein C chain II - phage IKe ALTERNATE_NAMES gene IX protein ORGANISM #formal_name phage IKe #note host Escherichia coli DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 28-Jul-2000 ACCESSIONS A04280 REFERENCE A92912 !$#authors Peeters, B.P.H.; Peters, R.M.; Schoenmakers, J.G.G.; !1Konings, R.N.H. !$#journal J. Mol. Biol. (1985) 181:27-39 !$#title Nucleotide sequence and genetic organization of the genome !1of the N-specific filamentous bacteriophage IKe. Comparison !1with the genome of the F-specific filamentous phages M13, fd !1and f1. !$#cross-references MUID:85160831; PMID:3981635 !$#accession A04280 !'##molecule_type DNA !'##residues 1-33 ##label PEE !'##cross-references GB:K02750; NID:g14942; PIDN:CAA26071.1; PID:g14947 GENETICS !$#gene IX CLASSIFICATION #superfamily class I filamentous phage coat protein C chain !1II KEYWORDS capsid protein; heterodimer SUMMARY #length 33 #molecular-weight 3728 #checksum 2128 SEQUENCE /// ENTRY ERBP1A #type complete TITLE gene 1A protein - phage PZA ORGANISM #formal_name phage PZA #note host Bacillus subtilis DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 23-Jul-1999 ACCESSIONS A24528 REFERENCE A91538 !$#authors Paces, V.; Vlcek, C.; Urbanek, P.; Hostomsky, Z. !$#journal Gene (1985) 38:45-56 !$#title Nucleotide sequence of the major early region of Bacillus !1subtilis phage PZA, a close relative of phi29. !$#cross-references MUID:86056991; PMID:3934048 !$#accession A24528 !'##molecule_type DNA !'##residues 1-59 ##label PAC !'##cross-references GB:M11813; GB:M13904; GB:M13905; NID:g216046; !1PIDN:AAA88481.1; PID:g216054 GENETICS !$#gene 1A CLASSIFICATION #superfamily phage PZA gene 1A protein KEYWORDS early protein SUMMARY #length 59 #molecular-weight 6865 #checksum 6451 SEQUENCE /// ENTRY ERBP1B #type complete TITLE gene 1B protein - phage PZA ORGANISM #formal_name phage PZA #note host Bacillus subtilis DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 23-Jul-1999 ACCESSIONS B24528 REFERENCE A91538 !$#authors Paces, V.; Vlcek, C.; Urbanek, P.; Hostomsky, Z. !$#journal Gene (1985) 38:45-56 !$#title Nucleotide sequence of the major early region of Bacillus !1subtilis phage PZA, a close relative of phi29. !$#cross-references MUID:86056991; PMID:3934048 !$#accession B24528 !'##molecule_type DNA !'##residues 1-56 ##label PAC !'##cross-references GB:M11813; GB:M13904; GB:M13905; NID:g216046; !1PIDN:AAA88480.1; PID:g216053 GENETICS !$#gene 1B CLASSIFICATION #superfamily phage PZA gene 1B protein KEYWORDS early protein SUMMARY #length 56 #molecular-weight 6580 #checksum 2704 SEQUENCE /// ENTRY ERBP19 #type complete TITLE probable early protein gp1 - phage phi-29 ORGANISM #formal_name phage phi-29 #note host Bacillus subtilis DATE 15-Nov-1984 #sequence_revision 15-Nov-1984 #text_change 23-Jul-1999 ACCESSIONS A04281 REFERENCE A91493 !$#authors Yoshikawa, H.; Ito, J. !$#journal Gene (1982) 17:323-335 !$#title Nucleotide sequence of the major early region of !1bacteriophage phi29. !$#cross-references MUID:82262795; PMID:6809534 !$#accession A04281 !'##status translation not shown !'##molecule_type DNA !'##residues 1-89 ##label YOS !'##cross-references GB:V01155; GB:J02478; NID:g15659; PIDN:CAA24479.1; !1PID:g15666 !'##note the authors report the amino acid composition of the translated !1protein GENETICS !$#gene 1 !$#map_position 6-4 CLASSIFICATION #superfamily phage PZA gene 1C protein KEYWORDS early protein SUMMARY #length 89 #molecular-weight 10270 #checksum 3208 SEQUENCE /// ENTRY ERBP1Z #type complete TITLE gene 1C protein - phage PZA ORGANISM #formal_name phage PZA #note host Bacillus subtilis DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 23-Jul-1999 ACCESSIONS C24528 REFERENCE A91538 !$#authors Paces, V.; Vlcek, C.; Urbanek, P.; Hostomsky, Z. !$#journal Gene (1985) 38:45-56 !$#title Nucleotide sequence of the major early region of Bacillus !1subtilis phage PZA, a close relative of phi29. !$#cross-references MUID:86056991; PMID:3934048 !$#accession C24528 !'##molecule_type DNA !'##residues 1-97 ##label PAC !'##cross-references GB:M11813; GB:M13904; GB:M13905; NID:g216046; !1PIDN:AAA88479.1; PID:g216052 GENETICS !$#gene 1C CLASSIFICATION #superfamily phage PZA gene 1C protein KEYWORDS early protein SUMMARY #length 97 #molecular-weight 11159 #checksum 6186 SEQUENCE /// ENTRY ERBP29 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - phage phi-29 ALTERNATE_NAMES early protein gp2 ORGANISM #formal_name phage phi-29 #note host Bacillus subtilis DATE 15-Nov-1984 #sequence_revision 15-Nov-1984 #text_change 23-Jul-1999 ACCESSIONS A04282; B93439; S11668; S11669 REFERENCE A91493 !$#authors Yoshikawa, H.; Ito, J. !$#journal Gene (1982) 17:323-335 !$#title Nucleotide sequence of the major early region of !1bacteriophage phi29. !$#cross-references MUID:82262795; PMID:6809534 !$#accession A04282 !'##status translation not shown !'##molecule_type DNA !'##residues 1-575 ##label YOS !'##cross-references GB:V01155; GB:J02478; NID:g15659; PIDN:CAA24480.1; !1PID:g15667 !'##note the authors report the amino acid composition of the translated !1protein; the reported composition differs from that of the !1sequence shown in having 37 residues each of Thr and Tyr REFERENCE A93439 !$#authors Escarmis, C.; Salas, M. !$#journal Nucleic Acids Res. (1982) 10:5785-5798 !$#title Nucleotide sequence of the early genes 3 and 4 of !1bacteriophage psi29. !$#cross-references MUID:83064518; PMID:6292852 !$#accession B93439 !'##molecule_type DNA !'##residues 1-85 ##label ESC GENETICS !$#gene 2 !$#map_position 16-6 CLASSIFICATION #superfamily phage PZA DNA-directed DNA polymerase KEYWORDS DNA binding; DNA replication; early protein; !1nucleotidyltransferase SUMMARY #length 575 #molecular-weight 66714 #checksum 4529 SEQUENCE /// ENTRY ERBP2Z #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) - phage PZA ALTERNATE_NAMES gene 2 protein (gp2) ORGANISM #formal_name phage PZA #note host Bacillus subtilis DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 23-Jul-1999 ACCESSIONS D24528 REFERENCE A91538 !$#authors Paces, V.; Vlcek, C.; Urbanek, P.; Hostomsky, Z. !$#journal Gene (1985) 38:45-56 !$#title Nucleotide sequence of the major early region of Bacillus !1subtilis phage PZA, a close relative of phi29. !$#cross-references MUID:86056991; PMID:3934048 !$#accession D24528 !'##molecule_type DNA !'##residues 1-572 ##label PAC !'##cross-references GB:M11813; GB:M13904; GB:M13905; NID:g216046; !1PIDN:AAA88478.1; PID:g216051 GENETICS !$#gene 2 CLASSIFICATION #superfamily phage PZA DNA-directed DNA polymerase KEYWORDS DNA binding; early protein; nucleotidyltransferase SUMMARY #length 572 #molecular-weight 66262 #checksum 3385 SEQUENCE /// ENTRY ERBP39 #type complete TITLE terminal protein - phage phi-29 ALTERNATE_NAMES gene 3 protein (gp3) ORGANISM #formal_name phage phi-29 #note host Bacillus subtilis DATE 15-Nov-1984 #sequence_revision 15-Nov-1984 #text_change 23-Jul-1999 ACCESSIONS A93439; A04283 REFERENCE A93439 !$#authors Escarmis, C.; Salas, M. !$#journal Nucleic Acids Res. (1982) 10:5785-5798 !$#title Nucleotide sequence of the early genes 3 and 4 of !1bacteriophage psi29. !$#cross-references MUID:83064518; PMID:6292852 !$#accession A93439 !'##molecule_type DNA !'##residues 1-266 ##label ESC !'##cross-references GB:V01155; NID:g15659; PIDN:CAA24481.1; PID:g15668 !'##note the DNA sequence of ochre-suppressible mutant sus3(91) contains !1the termination codon TAA rather than the CAA codon at the !1position corresponding to Gln-124 of the wild type REFERENCE A91493 !$#authors Yoshikawa, H.; Ito, J. !$#journal Gene (1982) 17:323-335 !$#title Nucleotide sequence of the major early region of !1bacteriophage phi29. !$#cross-references MUID:82262795; PMID:6809534 !$#accession A04283 !'##status translation not shown !'##molecule_type DNA !'##residues 1-266 ##label YOS !'##cross-references GB:V01155; GB:J02478; NID:g15659; PIDN:CAA24481.1; !1PID:g15668 !'##note the authors report the amino acid composition of the translated !1protein REFERENCE A93862 !$#authors Hermoso, J.M.; Salas, M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1980) 77:6425-6428 !$#title Protein pe is linked to the DNA of phage phi29 through a !1phosphoester bond between serine and 5'-dAMP. !$#cross-references MUID:81101064; PMID:6779279 !$#contents annotation; characterization of the terminal protein-DNA !1linkage REFERENCE A30635 !$#authors Hermoso, J.M.; Mendez, E.; Soriano, F.; Salas, M. !$#journal Nucleic Acids Res. (1985) 13:7715-7728 !$#title Location of the serine residue involved in the linkage !1between the terminal protein and the DNA of phage phi29. !$#cross-references MUID:86067193; PMID:3934646 !$#contents annotation; identification of the terminal protein-DNA !1linkage site COMMENT Terminal protein is linked to the 5' ends of both strands of !1the genome through a phosphodiester bond between the !1beta-hydroxyl group of a serine residue and the 5'-phosphate !1of the terminal deoxyadenylate. This protein is essential !1for DNA replication and is believed to be involved in the !1priming of DNA elongation. GENETICS !$#gene 3 !$#map_position 21-16 CLASSIFICATION #superfamily phage PZA terminal protein KEYWORDS DNA replication initiation; early protein; genome-linked !1protein; phosphoprotein FEATURE !$232 #binding_site phosphoryl-DNA (Ser) (covalent) #status !8experimental SUMMARY #length 266 #molecular-weight 31049 #checksum 5346 SEQUENCE /// ENTRY ERBP3Z #type complete TITLE terminal protein - phage PZA ALTERNATE_NAMES gene 3 protein (gp3) ORGANISM #formal_name phage PZA #note host Bacillus subtilis DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 23-Jul-1999 ACCESSIONS E24528 REFERENCE A91538 !$#authors Paces, V.; Vlcek, C.; Urbanek, P.; Hostomsky, Z. !$#journal Gene (1985) 38:45-56 !$#title Nucleotide sequence of the major early region of Bacillus !1subtilis phage PZA, a close relative of phi29. !$#cross-references MUID:86056991; PMID:3934048 !$#accession E24528 !'##molecule_type DNA !'##residues 1-266 ##label PAC !'##cross-references GB:M11813; GB:M13904; GB:M13905; NID:g216046; !1PIDN:AAA88477.1; PID:g216050 GENETICS !$#gene 3 CLASSIFICATION #superfamily phage PZA terminal protein KEYWORDS DNA replication initiation; early protein; genome-linked !1protein; phosphoprotein FEATURE !$232 #binding_site phosphoryl-DNA (Ser) (covalent) #status !8predicted SUMMARY #length 266 #molecular-weight 31067 #checksum 6315 SEQUENCE /// ENTRY ERBPNP #type complete TITLE terminal protein - phage NF ORGANISM #formal_name phage NF #note host Bacillus amyloliquefaciens DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 23-Jul-1999 ACCESSIONS A27856 REFERENCE A27856 !$#authors Leavitt, M.C.; Ito, J. !$#journal Nucleic Acids Res. (1987) 15:5251-5259 !$#title Nucleotide sequence of Bacillus phage Nf terminal protein !1gene. !$#cross-references MUID:87259998; PMID:3601672 !$#accession A27856 !'##molecule_type DNA !'##residues 1-266 ##label LEA !'##cross-references EMBL:Y00363; NID:g15451; PIDN:CAA68440.1; !1PID:g579177 GENETICS !$#gene E !$#start_codon GTG CLASSIFICATION #superfamily phage PZA terminal protein KEYWORDS DNA replication initiation; early protein; genome-linked !1protein; phosphoprotein FEATURE !$232 #binding_site phosphoryl-DNA (Ser) (covalent) #status !8predicted SUMMARY #length 266 #molecular-weight 31211 #checksum 4772 SEQUENCE /// ENTRY TPBPPR #type complete TITLE terminal protein - phage PRD1 ALTERNATE_NAMES P8 protein ORGANISM #formal_name phage PRD1 #note host Salmonella typhimurium; Escherichia coli DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 23-Jul-1999 ACCESSIONS S01613; A27328; A40477 REFERENCE S01613 !$#authors Hsieh, J.C.; Jung, G.; Leavitt, M.C.; Ito, J. !$#journal Nucleic Acids Res. (1987) 15:8999-9009 !$#title Primary structure of the DNA terminal protein of !1bacteriophage PRD1. !$#cross-references MUID:88067710; PMID:3684578 !$#accession S01613 !'##molecule_type DNA !'##residues 1-259 ##label HSI !'##cross-references EMBL:X06321; NID:g15800; PIDN:CAA29636.1; !1PID:g15801 REFERENCE A27328 !$#authors Savilahti, H.; Bamford, D.H. !$#journal Gene (1987) 57:121-130 !$#title The complete nucleotide sequence of the left very early !1region of Escherichia coli bacteriophage PRD1 coding for the !1terminal protein and the DNA polymerase. !$#cross-references MUID:88112855; PMID:3322943 !$#accession A27328 !'##molecule_type DNA !'##residues 1-259 ##label SAV !'##cross-references GB:M22161; NID:g215750; PIDN:AAA32449.1; !1PID:g215751 REFERENCE A40477 !$#authors Bamford, J.K.H.; Haenninen, A.L.; Pakula, T.M.; Ojala, P.M.; !1Kalkkinen, N.; Frilander, M.; Bamford, D.H. !$#journal Virology (1991) 183:658-676 !$#title Genome organization of membrane-containing bacteriophage !1PRD1. !$#cross-references MUID:91306449; PMID:1853567 !$#accession A40477 !'##status translation not shown !'##molecule_type DNA !'##residues 1-259 ##label BAM !'##cross-references GB:M69077; NID:g215765; PIDN:AAA32455.1; !1PID:g215766 REFERENCE A58835 !$#authors Shiue, S.Y.; Hsieh, J.C.; Ito, J. !$#journal Nucleic Acids Res. (1991) 19:3805-3810 !$#title Mapping of the DNA linking tyrosine residue of the PRD1 !1terminal protein. !$#cross-references MUID:91319535; PMID:1861973 !$#contents annotation; linkage site by site-directed mutagenesis GENETICS !$#gene 8 CLASSIFICATION #superfamily phage PRD1 terminal protein KEYWORDS DNA replication initiation; early protein; genome-linked !1protein; phosphoprotein FEATURE !$190 #binding_site phosphoryl-DNA (Tyr) (covalent) #status !8experimental SUMMARY #length 259 #molecular-weight 29514 #checksum 5217 SEQUENCE /// ENTRY A46345 #type complete TITLE gene III protein - phage PRD1 ALTERNATE_NAMES major capsid protein III ORGANISM #formal_name phage PRD1 DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 23-Jul-1999 ACCESSIONS A46345; C46345 REFERENCE A46345 !$#authors Bamford, J.K.H.; Bamford, D.H. !$#journal Virology (1990) 177:445-451 !$#title Capsomer proteins of bacteriophage PRD1, a bacterial virus !1with a membrane. !$#cross-references MUID:90320115; PMID:2196741 !$#accession A46345 !'##molecule_type DNA !'##residues 1-395 ##label BAM !'##cross-references GB:M55567; NID:g215743; PIDN:AAA32445.1; !1PID:g215744 !$#accession C46345 !'##molecule_type protein !'##residues 2-10 ##label BA2 GENETICS !$#gene III CLASSIFICATION #superfamily phage PRD1 gene III protein KEYWORDS capsid protein SUMMARY #length 395 #molecular-weight 43447 #checksum 2757 SEQUENCE /// ENTRY B46345 #type complete TITLE gene V protein - phage PRD1 ALTERNATE_NAMES minor capsid protein V ORGANISM #formal_name phage PRD1 DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 23-Jul-1999 ACCESSIONS B46345; D46345 REFERENCE A46345 !$#authors Bamford, J.K.H.; Bamford, D.H. !$#journal Virology (1990) 177:445-451 !$#title Capsomer proteins of bacteriophage PRD1, a bacterial virus !1with a membrane. !$#cross-references MUID:90320115; PMID:2196741 !$#accession B46345 !'##molecule_type DNA !'##residues 1-340 ##label BAM !'##cross-references GB:M55568; NID:g215745; PIDN:AAA32446.1; !1PID:g215746 !$#accession D46345 !'##molecule_type protein !'##residues 2-6 ##label BA2 GENETICS !$#gene V CLASSIFICATION #superfamily phage PRD1 gene V protein KEYWORDS capsid protein SUMMARY #length 340 #molecular-weight 34449 #checksum 9549 SEQUENCE /// ENTRY WMBPQ2 #type complete TITLE gene P2 protein - phage PRD1 ORGANISM #formal_name phage PRD1 #note host Escherichia coli DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 23-Jul-1999 ACCESSIONS D40477; A36784 REFERENCE A40477 !$#authors Bamford, J.K.H.; Haenninen, A.L.; Pakula, T.M.; Ojala, P.M.; !1Kalkkinen, N.; Frilander, M.; Bamford, D.H. !$#journal Virology (1991) 183:658-676 !$#title Genome organization of membrane-containing bacteriophage !1PRD1. !$#cross-references MUID:91306449; PMID:1853567 !$#accession D40477 !'##molecule_type DNA !'##residues 1-591 ##label BAM !'##cross-references GB:M69077; NID:g215765; PIDN:AAA32458.1; !1PID:g215769 !$#accession A36784 !'##molecule_type protein !'##residues 2-10 ##label BA2 COMMENT This protein adsorbs to surface receptors of the host when !1the life cycle of the phage begins. GENETICS !$#gene P2 CLASSIFICATION #superfamily phage PRD1 gene P2 protein KEYWORDS adsorption SUMMARY #length 591 #molecular-weight 63821 #checksum 4528 SEQUENCE /// ENTRY WMBPQC #type complete TITLE gene c protein - phage PRD1 ORGANISM #formal_name phage PRD1 #note host Escherichia coli DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 23-Jul-1999 ACCESSIONS E40477; B36784 REFERENCE A40477 !$#authors Bamford, J.K.H.; Haenninen, A.L.; Pakula, T.M.; Ojala, P.M.; !1Kalkkinen, N.; Frilander, M.; Bamford, D.H. !$#journal Virology (1991) 183:658-676 !$#title Genome organization of membrane-containing bacteriophage !1PRD1. !$#cross-references MUID:91306449; PMID:1853567 !$#accession E40477 !'##molecule_type DNA !'##residues 1-126 ##label BAM !'##cross-references GB:M69077; NID:g215765; PIDN:AAA32459.1; !1PID:g215770 !$#accession B36784 !'##molecule_type protein !'##residues 28-40 ##label BM2 GENETICS !$#gene c CLASSIFICATION #superfamily phage PRD1 gene c protein SUMMARY #length 126 #molecular-weight 13746 #checksum 8478 SEQUENCE /// ENTRY WMBP77 #type complete TITLE gene 17 protein - phage PRD1 ORGANISM #formal_name phage PRD1 #note host Escherichia coli DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 23-Jul-1999 ACCESSIONS G40477 REFERENCE A40477 !$#authors Bamford, J.K.H.; Haenninen, A.L.; Pakula, T.M.; Ojala, P.M.; !1Kalkkinen, N.; Frilander, M.; Bamford, D.H. !$#journal Virology (1991) 183:658-676 !$#title Genome organization of membrane-containing bacteriophage !1PRD1. !$#cross-references MUID:91306449; PMID:1853567 !$#accession G40477 !'##molecule_type DNA !'##residues 1-86 ##label BAM !'##cross-references GB:M69077; NID:g215765; PIDN:AAA32461.1; !1PID:g215772 COMMENT This protein is involved in phage assembly. GENETICS !$#gene 17 CLASSIFICATION #superfamily phage PRD1 gene 17 protein KEYWORDS phage maturation SUMMARY #length 86 #molecular-weight 9538 #checksum 8423 SEQUENCE /// ENTRY WMBPP6 #type complete TITLE gene 6 protein - phage PRD1 ORGANISM #formal_name phage PRD1 #note host Escherichia coli DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 23-Jul-1999 ACCESSIONS H40477; C36784 REFERENCE A40477 !$#authors Bamford, J.K.H.; Haenninen, A.L.; Pakula, T.M.; Ojala, P.M.; !1Kalkkinen, N.; Frilander, M.; Bamford, D.H. !$#journal Virology (1991) 183:658-676 !$#title Genome organization of membrane-containing bacteriophage !1PRD1. !$#cross-references MUID:91306449; PMID:1853567 !$#accession H40477 !'##molecule_type DNA !'##residues 1-166 ##label BAM !'##cross-references GB:M69077; NID:g215765; PIDN:AAA32462.1; !1PID:g215773 !$#accession C36784 !'##molecule_type protein !'##residues 1-6 ##label BA2 GENETICS !$#gene 6 CLASSIFICATION #superfamily phage PRD1 gene 6 protein SUMMARY #length 166 #molecular-weight 17573 #checksum 9959 SEQUENCE /// ENTRY WMBPQ9 #type complete TITLE gene 9 protein - phage PRD1 ORGANISM #formal_name phage PRD1 #note host Escherichia coli DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 23-Jul-1999 ACCESSIONS I40477; D36784 REFERENCE A40477 !$#authors Bamford, J.K.H.; Haenninen, A.L.; Pakula, T.M.; Ojala, P.M.; !1Kalkkinen, N.; Frilander, M.; Bamford, D.H. !$#journal Virology (1991) 183:658-676 !$#title Genome organization of membrane-containing bacteriophage !1PRD1. !$#cross-references MUID:91306449; PMID:1853567 !$#accession I40477 !'##molecule_type DNA !'##residues 1-227 ##label BAM !'##cross-references GB:M69077; NID:g215765; PIDN:AAA32463.1; !1PID:g215774 !$#accession D36784 !'##molecule_type protein !'##residues 2-7 ##label BA2 COMMENT This protein is involved in phage DNA packaging. GENETICS !$#gene 9 CLASSIFICATION #superfamily phage PRD1 gene 9 protein KEYWORDS DNA packaging SUMMARY #length 227 #molecular-weight 25787 #checksum 7983 SEQUENCE /// ENTRY WMBPPI #type complete TITLE gene i protein - phage PRD1 ORGANISM #formal_name phage PRD1 #note host Escherichia coli DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 23-Jul-1999 ACCESSIONS A36776 REFERENCE A40477 !$#authors Bamford, J.K.H.; Haenninen, A.L.; Pakula, T.M.; Ojala, P.M.; !1Kalkkinen, N.; Frilander, M.; Bamford, D.H. !$#journal Virology (1991) 183:658-676 !$#title Genome organization of membrane-containing bacteriophage !1PRD1. !$#cross-references MUID:91306449; PMID:1853567 !$#accession A36776 !'##molecule_type DNA !'##residues 1-42 ##label BAM !'##cross-references GB:M69077; NID:g215765; PIDN:AAA32464.1; !1PID:g215775 GENETICS !$#gene i CLASSIFICATION #superfamily phage PRD1 gene i protein SUMMARY #length 42 #molecular-weight 4541 #checksum 7788 SEQUENCE /// ENTRY WMBPPJ #type complete TITLE gene j protein - phage PRD1 ORGANISM #formal_name phage PRD1 #note host Escherichia coli DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 23-Jul-1999 ACCESSIONS B36776 REFERENCE A40477 !$#authors Bamford, J.K.H.; Haenninen, A.L.; Pakula, T.M.; Ojala, P.M.; !1Kalkkinen, N.; Frilander, M.; Bamford, D.H. !$#journal Virology (1991) 183:658-676 !$#title Genome organization of membrane-containing bacteriophage !1PRD1. !$#cross-references MUID:91306449; PMID:1853567 !$#accession B36776 !'##molecule_type DNA !'##residues 1-42 ##label BAM !'##cross-references GB:M69077; NID:g215765; PIDN:AAA32465.1; !1PID:g215776 GENETICS !$#gene j CLASSIFICATION #superfamily phage PRD1 gene j protein SUMMARY #length 42 #molecular-weight 4671 #checksum 8223 SEQUENCE /// ENTRY WMBPBH #type complete TITLE gene h protein - phage PRD1 ORGANISM #formal_name phage PRD1 #note host Escherichia coli DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 23-Jul-1999 ACCESSIONS D36776 REFERENCE A40477 !$#authors Bamford, J.K.H.; Haenninen, A.L.; Pakula, T.M.; Ojala, P.M.; !1Kalkkinen, N.; Frilander, M.; Bamford, D.H. !$#journal Virology (1991) 183:658-676 !$#title Genome organization of membrane-containing bacteriophage !1PRD1. !$#cross-references MUID:91306449; PMID:1853567 !$#accession D36776 !'##molecule_type DNA !'##residues 1-84 ##label BAM !'##cross-references GB:M69077; NID:g215765; PIDN:AAA32467.1; !1PID:g215778 GENETICS !$#gene h CLASSIFICATION #superfamily phage PRD1 gene h protein SUMMARY #length 84 #molecular-weight 9295 #checksum 6152 SEQUENCE /// ENTRY WMBPKB #type complete TITLE gene k protein - phage PRD1 ORGANISM #formal_name phage PRD1 #note host Escherichia coli DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 23-Jul-1999 ACCESSIONS E36776; E36784 REFERENCE A40477 !$#authors Bamford, J.K.H.; Haenninen, A.L.; Pakula, T.M.; Ojala, P.M.; !1Kalkkinen, N.; Frilander, M.; Bamford, D.H. !$#journal Virology (1991) 183:658-676 !$#title Genome organization of membrane-containing bacteriophage !1PRD1. !$#cross-references MUID:91306449; PMID:1853567 !$#accession E36776 !'##molecule_type DNA !'##residues 1-47 ##label BAM !'##cross-references GB:M69077; NID:g215765; PIDN:AAA32468.1; !1PID:g215779 !$#accession E36784 !'##molecule_type protein !'##residues 1-9 ##label BA2 GENETICS !$#gene k CLASSIFICATION #superfamily phage PRD1 gene k protein SUMMARY #length 47 #molecular-weight 5493 #checksum 5500 SEQUENCE /// ENTRY WMBPMB #type complete TITLE gene m protein - phage PRD1 ORGANISM #formal_name phage PRD1 #note host Escherichia coli DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 16-Feb-1997 ACCESSIONS F36776 REFERENCE A40477 !$#authors Bamford, J.K.H.; Haenninen, A.L.; Pakula, T.M.; Ojala, P.M.; !1Kalkkinen, N.; Frilander, M.; Bamford, D.H. !$#journal Virology (1991) 183:658-676 !$#title Genome organization of membrane-containing bacteriophage !1PRD1. !$#cross-references MUID:91306449; PMID:1853567 !$#accession F36776 !'##molecule_type DNA !'##residues 1-90 ##label BAM !'##cross-references GB:M69077 GENETICS !$#gene m CLASSIFICATION #superfamily phage PRD1 gene m protein KEYWORDS transmembrane protein SUMMARY #length 90 #molecular-weight 9777 #checksum 6623 SEQUENCE /// ENTRY WMBPUB #type complete TITLE gene o protein - phage PRD1 ORGANISM #formal_name phage PRD1 #note host Escherichia coli DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 23-Jul-1999 ACCESSIONS G36776; F36784 REFERENCE A40477 !$#authors Bamford, J.K.H.; Haenninen, A.L.; Pakula, T.M.; Ojala, P.M.; !1Kalkkinen, N.; Frilander, M.; Bamford, D.H. !$#journal Virology (1991) 183:658-676 !$#title Genome organization of membrane-containing bacteriophage !1PRD1. !$#cross-references MUID:91306449; PMID:1853567 !$#accession G36776 !'##molecule_type DNA !'##residues 1-68 ##label BAM !'##cross-references GB:M69077; NID:g215765; PIDN:AAA32470.1; !1PID:g215781 !$#accession F36784 !'##molecule_type protein !'##residues 61-68 ##label BA2 GENETICS !$#gene o CLASSIFICATION #superfamily phage PRD1 gene o protein SUMMARY #length 68 #molecular-weight 6695 #checksum 2201 SEQUENCE /// ENTRY WMBPWB #type complete TITLE gene p protein - phage PRD1 ORGANISM #formal_name phage PRD1 #note host Escherichia coli DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 23-Jul-1999 ACCESSIONS H36776; G36784 REFERENCE A40477 !$#authors Bamford, J.K.H.; Haenninen, A.L.; Pakula, T.M.; Ojala, P.M.; !1Kalkkinen, N.; Frilander, M.; Bamford, D.H. !$#journal Virology (1991) 183:658-676 !$#title Genome organization of membrane-containing bacteriophage !1PRD1. !$#cross-references MUID:91306449; PMID:1853567 !$#accession H36776 !'##molecule_type DNA !'##residues 1-84 ##label BAM !'##cross-references GB:M69077; NID:g215765; PIDN:AAA32471.1; !1PID:g215782 !$#accession G36784 !'##molecule_type protein !'##residues 2-10 ##label BA2 GENETICS !$#gene p CLASSIFICATION #superfamily phage PRD1 gene p protein SUMMARY #length 84 #molecular-weight 9187 #checksum 4684 SEQUENCE /// ENTRY WMBPXB #type complete TITLE gene 11 protein - phage PRD1 ORGANISM #formal_name phage PRD1 #note host Escherichia coli DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 23-Jul-1999 ACCESSIONS I36776; H36784 REFERENCE A40477 !$#authors Bamford, J.K.H.; Haenninen, A.L.; Pakula, T.M.; Ojala, P.M.; !1Kalkkinen, N.; Frilander, M.; Bamford, D.H. !$#journal Virology (1991) 183:658-676 !$#title Genome organization of membrane-containing bacteriophage !1PRD1. !$#cross-references MUID:91306449; PMID:1853567 !$#accession I36776 !'##molecule_type DNA !'##residues 1-166 ##label BAM !'##cross-references GB:M69077; NID:g215765; PIDN:AAA32472.1; !1PID:g215783 !$#accession H36784 !'##molecule_type protein !'##residues 83-92;105-129;148-163 ##label BA2 GENETICS !$#gene 11 CLASSIFICATION #superfamily phage PRD1 gene 11 protein SUMMARY #length 166 #molecular-weight 18215 #checksum 6279 SEQUENCE /// ENTRY WMBPSB #type complete TITLE gene s protein - phage PRD1 ORGANISM #formal_name phage PRD1 #note host Escherichia coli DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 23-Jul-1999 ACCESSIONS A36777; I36784 REFERENCE A40477 !$#authors Bamford, J.K.H.; Haenninen, A.L.; Pakula, T.M.; Ojala, P.M.; !1Kalkkinen, N.; Frilander, M.; Bamford, D.H. !$#journal Virology (1991) 183:658-676 !$#title Genome organization of membrane-containing bacteriophage !1PRD1. !$#cross-references MUID:91306449; PMID:1853567 !$#accession A36777 !'##molecule_type DNA !'##residues 1-117 ##label BAM !'##cross-references GB:M69077; NID:g215765; PIDN:AAA32473.1; !1PID:g215784 !$#accession I36784 !'##molecule_type protein !'##residues 71-85;92-110 ##label BA2 GENETICS !$#gene s CLASSIFICATION #superfamily phage PRD1 gene s protein SUMMARY #length 117 #molecular-weight 12551 #checksum 6020 SEQUENCE /// ENTRY WMBPG7 #type complete TITLE gene 7 protein - phage PRD1 ORGANISM #formal_name phage PRD1 #note host Escherichia coli DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 23-Jul-1999 ACCESSIONS B36777; A36783 REFERENCE A40477 !$#authors Bamford, J.K.H.; Haenninen, A.L.; Pakula, T.M.; Ojala, P.M.; !1Kalkkinen, N.; Frilander, M.; Bamford, D.H. !$#journal Virology (1991) 183:658-676 !$#title Genome organization of membrane-containing bacteriophage !1PRD1. !$#cross-references MUID:91306449; PMID:1853567 !$#accession B36777 !'##molecule_type DNA !'##residues 1-265 ##label BAM !'##cross-references GB:M69077; NID:g215765; PIDN:AAA32474.1; !1PID:g215785 !$#accession A36783 !'##molecule_type protein !'##residues 2-7;24-35;85-98;118-129 ##label BA2 GENETICS !$#gene 7 CLASSIFICATION #superfamily phage PRD1 gene 7 protein SUMMARY #length 265 #molecular-weight 27073 #checksum 3414 SEQUENCE /// ENTRY WMBPTB #type complete TITLE gene 10 protein - phage PRD1 ORGANISM #formal_name phage PRD1 #note host Escherichia coli DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 30-Jun-1993 ACCESSIONS E36777 REFERENCE A40477 !$#authors Bamford, J.K.H.; Haenninen, A.L.; Pakula, T.M.; Ojala, P.M.; !1Kalkkinen, N.; Frilander, M.; Bamford, D.H. !$#journal Virology (1991) 183:658-676 !$#title Genome organization of membrane-containing bacteriophage !1PRD1. !$#cross-references MUID:91306449; PMID:1853567 !$#accession E36777 !'##molecule_type DNA !'##residues 1-203 ##label BAM !'##cross-references GB:M69077 GENETICS !$#gene 10 CLASSIFICATION #superfamily phage PRD1 gene 10 protein SUMMARY #length 203 #molecular-weight 20688 #checksum 60 SEQUENCE /// ENTRY ERBP49 #type complete TITLE early protein gp4 - phage phi-29 ALTERNATE_NAMES transcription activator p4 ORGANISM #formal_name phage phi-29 #note host Bacillus subtilis DATE 15-Nov-1984 #sequence_revision 15-Nov-1984 #text_change 23-Jul-1999 ACCESSIONS C93439; A04284; S09124 REFERENCE A93439 !$#authors Escarmis, C.; Salas, M. !$#journal Nucleic Acids Res. (1982) 10:5785-5798 !$#title Nucleotide sequence of the early genes 3 and 4 of !1bacteriophage psi29. !$#cross-references MUID:83064518; PMID:6292852 !$#accession C93439 !'##molecule_type DNA !'##residues 1-125 ##label ESC !'##note the DNA sequence of ochre-suppressible mutant sus4(56) contains !1the termination codon TAA rather than the CAA codon at the !1position corresponding to Gln-42 of the wild type REFERENCE A91493 !$#authors Yoshikawa, H.; Ito, J. !$#journal Gene (1982) 17:323-335 !$#title Nucleotide sequence of the major early region of !1bacteriophage phi29. !$#cross-references MUID:82262795; PMID:6809534 !$#accession A04284 !'##status translation not shown !'##molecule_type DNA !'##residues 1-125 ##label YOS !'##cross-references GB:V01155; GB:J02478; NID:g15659; PIDN:CAA24482.1; !1PID:g15669 !'##note the authors assign the gene 4 protein to a different open !1reading frame; the sequence shown corresponds to ORF 9 of !1the authors; with the exception of the initiator Met, the !1reported composition based on the translated sequence agrees !1with that of the sequence shown REFERENCE S09124 !$#authors Rojo, F.; Zaballos, A.; Salas, M. !$#journal J. Mol. Biol. (1990) 211:713-725 !$#title Bend induced by the phage phi29 transcriptional activator in !1the viral late promoter is required for activation. !$#cross-references MUID:90189140; PMID:2107318 !$#accession S09124 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 110-125 ##label ROJ GENETICS !$#gene 4 !$#map_position 22-20 FUNCTION !$#description early protein gp4 is believed to be a positive regulator of !1late transcription; it may function as a sigma-like !1component of the Bacillus RNA polymerase CLASSIFICATION #superfamily phage PZA gene 4 protein KEYWORDS early protein; sigma factor; transcription SUMMARY #length 125 #molecular-weight 15133 #checksum 457 SEQUENCE /// ENTRY ERBP4Z #type complete TITLE gene 4 protein - phage PZA ORGANISM #formal_name phage PZA #note host Bacillus subtilis DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 23-Jul-1999 ACCESSIONS F24528 REFERENCE A91538 !$#authors Paces, V.; Vlcek, C.; Urbanek, P.; Hostomsky, Z. !$#journal Gene (1985) 38:45-56 !$#title Nucleotide sequence of the major early region of Bacillus !1subtilis phage PZA, a close relative of phi29. !$#cross-references MUID:86056991; PMID:3934048 !$#accession F24528 !'##molecule_type DNA !'##residues 1-125 ##label PAC !'##cross-references GB:M11813; GB:M13904; GB:M13905; NID:g216046; !1PIDN:AAA88476.1; PID:g216049 GENETICS !$#gene 4 CLASSIFICATION #superfamily phage PZA gene 4 protein KEYWORDS early protein; transcription regulation SUMMARY #length 125 #molecular-weight 15090 #checksum 647 SEQUENCE /// ENTRY ERBPNF #type complete TITLE gene F protein - phage NF ORGANISM #formal_name phage NF #note host Bacillus sp. DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 23-Jul-1999 ACCESSIONS A25643 REFERENCE A25643 !$#authors Mizukami, Y.; Sekiya, T.; Hirokawa, H. !$#journal Gene (1986) 42:231-235 !$#title Nucleotide sequence of gene F of Bacillus phage Nf. !$#cross-references MUID:86275998; PMID:3015737 !$#accession A25643 !'##molecule_type DNA !'##residues 1-125 ##label MIZ !'##cross-references GB:M13664; NID:g166146; PIDN:AAA32195.1; !1PID:g166147 !'##note the authors translated the codon CAA for residue 34 as Leu GENETICS !$#gene F CLASSIFICATION #superfamily phage PZA gene 4 protein KEYWORDS early protein; transcription regulation SUMMARY #length 125 #molecular-weight 15019 #checksum 67 SEQUENCE /// ENTRY ERBP5A #type complete TITLE gene 5A protein - phage PZA ORGANISM #formal_name phage PZA #note host Bacillus subtilis DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 23-Jul-1999 ACCESSIONS G24528 REFERENCE A91538 !$#authors Paces, V.; Vlcek, C.; Urbanek, P.; Hostomsky, Z. !$#journal Gene (1985) 38:45-56 !$#title Nucleotide sequence of the major early region of Bacillus !1subtilis phage PZA, a close relative of phi29. !$#cross-references MUID:86056991; PMID:3934048 !$#accession G24528 !'##molecule_type DNA !'##residues 1-124 ##label PAC !'##cross-references GB:M11813; GB:M13904; GB:M13905; NID:g216046; !1PIDN:AAA88475.1; PID:g216048 GENETICS !$#gene 5A CLASSIFICATION #superfamily phage PZA gene 5A protein KEYWORDS early protein SUMMARY #length 124 #molecular-weight 13330 #checksum 7445 SEQUENCE /// ENTRY ERBP5Z #type complete TITLE gene 5B protein - phage PZA ORGANISM #formal_name phage PZA #note host Bacillus subtilis DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 23-Jul-1999 ACCESSIONS H24528 REFERENCE A91538 !$#authors Paces, V.; Vlcek, C.; Urbanek, P.; Hostomsky, Z. !$#journal Gene (1985) 38:45-56 !$#title Nucleotide sequence of the major early region of Bacillus !1subtilis phage PZA, a close relative of phi29. !$#cross-references MUID:86056991; PMID:3934048 !$#accession H24528 !'##molecule_type DNA !'##residues 1-65 ##label PAC !'##cross-references GB:M11813; GB:M13904; GB:M13905; NID:g216046; !1PIDN:AAA88474.1; PID:g1196802 GENETICS !$#gene 5B CLASSIFICATION #superfamily phage PZA gene 5B protein KEYWORDS early protein SUMMARY #length 65 #molecular-weight 7266 #checksum 137 SEQUENCE /// ENTRY ERBP59 #type complete TITLE early protein gp5 (version 1) - phage phi-29 ORGANISM #formal_name phage phi-29 #note host Bacillus subtilis DATE 18-Aug-1982 #sequence_revision 15-Nov-1984 #text_change 23-Jul-1999 ACCESSIONS A92343; A04285 REFERENCE A92343 !$#authors Murray, C.L.; Rabinowitz, J.C. !$#journal J. Biol. Chem. (1982) 257:1053-1062 !$#title Nucleotide sequences of transcription and translation !1initiation regions in Bacillus phage 029 early genes. !$#cross-references MUID:82098089; PMID:6274853 !$#accession A92343 !'##molecule_type DNA !'##residues 1-36 ##label MUR !'##cross-references GB:V01154; GB:J02480; NID:g15656; PIDN:CAA24472.1; !1PID:g15658 !'##note the authors do not include Met-1 in their translation REFERENCE A91493 !$#authors Yoshikawa, H.; Ito, J. !$#journal Gene (1982) 17:323-335 !$#title Nucleotide sequence of the major early region of !1bacteriophage phi29. !$#cross-references MUID:82262795; PMID:6809534 !$#accession A04285 !'##status translation not shown !'##molecule_type DNA !'##residues 1-66 ##label YOS !'##note the authors assign the gene 5 protein to a different open !1reading frame; the sequence shown corresponds to ORF 12 of !1the authors; however, the DNA sequence reported by the !1authors for this ORF differs from that of the sequence shown !1and results in the translated sequence having 28-Asp !'##note the composition based on the translated sequence was reported !1and agrees with that of the sequence shown except for the !1discrepancy at position 28 and the absence of the initiator !1Met COMMENT The function of early protein gp5 is unknown; however, !1mutants in gene 5 are defective in DNA replication. COMMENT This sequence was translated from one of two possible open !1reading frames for the gene 5 protein; see PIR:EABP59 for !1the alternative version. GENETICS !$#gene 5 !$#map_position 26-25 CLASSIFICATION #superfamily phage PZA gene 5B protein KEYWORDS early protein; replication SUMMARY #length 66 #molecular-weight 7421 #checksum 9934 SEQUENCE /// ENTRY EABP59 #type complete TITLE early protein gp5 (version 2) - phage phi-29 ORGANISM #formal_name phage phi-29 #note host Bacillus subtilis DATE 15-Nov-1984 #sequence_revision 15-Nov-1984 #text_change 23-Jul-1999 ACCESSIONS A04286 REFERENCE A91493 !$#authors Yoshikawa, H.; Ito, J. !$#journal Gene (1982) 17:323-335 !$#title Nucleotide sequence of the major early region of !1bacteriophage phi29. !$#cross-references MUID:82262795; PMID:6809534 !$#accession A04286 !'##status translation not shown !'##molecule_type DNA !'##residues 1-45 ##label YOS !'##cross-references GB:V01155; GB:J02478; NID:g15659; PIDN:CAA24484.1; !1PID:g15671 !'##note the authors report the amino acid composition of the translated !1protein COMMENT This sequence was translated from one of two possible open !1reading frames for the gene 5 protein; see PIR:ERBP59 for !1the alternative version. COMMENT The function of early protein gp5 is unknown; however, !1mutants in gene 5 are defective in DNA replication. GENETICS !$#gene 5 !$#map_position 25-24 CLASSIFICATION #superfamily phage phi-29 early protein gp5 KEYWORDS early protein; replication SUMMARY #length 45 #molecular-weight 5320 #checksum 217 SEQUENCE /// ENTRY ERBP69 #type complete TITLE early protein gp6 - phage phi-29 ORGANISM #formal_name phage phi-29 #note host Bacillus subtilis DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 23-Jul-1999 ACCESSIONS B92343; A04287 REFERENCE A92343 !$#authors Murray, C.L.; Rabinowitz, J.C. !$#journal J. Biol. Chem. (1982) 257:1053-1062 !$#title Nucleotide sequences of transcription and translation !1initiation regions in Bacillus phage 029 early genes. !$#cross-references MUID:82098089; PMID:6274853 !$#accession B92343 !'##molecule_type DNA !'##residues 1-104 ##label MUR !'##cross-references GB:V01154; GB:J02480; NID:g15656; PIDN:CAA24471.1; !1PID:g15657 !'##note the reading frame for gene 6 was determined by analysis of the !1amino end of the protein REFERENCE A91493 !$#authors Yoshikawa, H.; Ito, J. !$#journal Gene (1982) 17:323-335 !$#title Nucleotide sequence of the major early region of !1bacteriophage phi29. !$#cross-references MUID:82262795; PMID:6809534 !$#accession A04287 !'##molecule_type DNA !'##residues 1-104 ##label YOS !'##cross-references GB:V01155; GB:J02478; NID:g15659; PIDN:CAA24486.1; !1PID:g15673 !'##note the authors report the amino acid composition of the translated !1protein COMMENT The function of early protein gp6 is unknown; however, !1mutants in gene 6 are defective in DNA replication. GENETICS !$#gene 6 !$#map_position 27-26 CLASSIFICATION #superfamily phage PZA gene 6 protein KEYWORDS early protein; replication SUMMARY #length 104 #molecular-weight 12005 #checksum 2995 SEQUENCE /// ENTRY ERBP6Z #type complete TITLE gene 6 protein - phage PZA ORGANISM #formal_name phage PZA #note host Bacillus subtilis DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 23-Jul-1999 ACCESSIONS I24528; J24528 REFERENCE A91538 !$#authors Paces, V.; Vlcek, C.; Urbanek, P.; Hostomsky, Z. !$#journal Gene (1985) 38:45-56 !$#title Nucleotide sequence of the major early region of Bacillus !1subtilis phage PZA, a close relative of phi29. !$#cross-references MUID:86056991; PMID:3934048 !$#accession I24528 !'##molecule_type DNA !'##residues 1-96 ##label PAC !'##cross-references GB:M11813; GB:M13904; GB:M13905; NID:g216046; !1PIDN:AAA88473.1; PID:g216047 GENETICS !$#gene 6 CLASSIFICATION #superfamily phage PZA gene 6 protein KEYWORDS early protein SUMMARY #length 96 #molecular-weight 11050 #checksum 7523 SEQUENCE /// ENTRY WMBP7Z #type complete TITLE gene 7 protein - phage PZA ORGANISM #formal_name phage PZA #note host Bacillus subtilis DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 23-Jul-1999 ACCESSIONS A24831 REFERENCE A91550 !$#authors Paces, V.; Vlcek, C.; Urbanek, P. !$#journal Gene (1986) 44:107-114 !$#title Nucleotide sequence of the late region of Bacillus subtilis !1phage PZA, a close relative of phi-29. !$#cross-references MUID:87031573; PMID:3095188 !$#accession A24831 !'##molecule_type DNA !'##residues 1-98 ##label PAC !'##cross-references GB:M11813; GB:M13904; GB:M13905; NID:g216046; !1PIDN:AAA88483.1; PID:g216055 GENETICS !$#gene 7 CLASSIFICATION #superfamily phage PZA gene 7 protein KEYWORDS late protein SUMMARY #length 98 #molecular-weight 11281 #checksum 9567 SEQUENCE /// ENTRY WMBPF9 #type complete TITLE gene 7 protein - phage phi-29 ALTERNATE_NAMES head morphogenesis protein ORGANISM #formal_name phage phi-29 #note host Bacillus subtilis DATE 30-Sep-1989 #sequence_revision 30-Sep-1989 #text_change 23-Jul-1999 ACCESSIONS A28923; A25816 REFERENCE A28923 !$#authors Innis, C.A.; Garvey, K.J.; Ito, J. !$#journal Nucleic Acids Res. (1986) 14:7129 !$#title Nucleotide sequence of phage phi-29 gene 7: structure of !1intergenic spacer between the major early and late genes. !$#cross-references MUID:87016351; PMID:3763399 !$#accession A28923 !'##molecule_type DNA !'##residues 1-98 ##label INN !'##cross-references GB:X04386; NID:g15522; PIDN:CAA27974.1; PID:g15524 REFERENCE A25816 !$#authors Vlcek, C.; Paces, V. !$#journal Gene (1986) 46:215-225 !$#title Nucleotide sequence of the late region of Bacillus phage !1phi-29 completes the 19285-bp sequence of phi-29 genome. !1Comparison with the homologous sequence of phage PZA. !$#cross-references MUID:87106857; PMID:3803926 !$#accession A25816 !'##molecule_type DNA !'##residues 1-98 ##label VLC !'##cross-references GB:M14782; NID:g215323; PIDN:AAA32279.1; !1PID:g215324 GENETICS !$#gene 7 CLASSIFICATION #superfamily phage PZA gene 7 protein KEYWORDS head protein; late protein SUMMARY #length 98 #molecular-weight 11266 #checksum 8579 SEQUENCE /// ENTRY WMBP8Z #type complete TITLE gene 8 protein - phage PZA ORGANISM #formal_name phage PZA #note host Bacillus subtilis DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 23-Jul-1999 ACCESSIONS B24831 REFERENCE A91550 !$#authors Paces, V.; Vlcek, C.; Urbanek, P. !$#journal Gene (1986) 44:107-114 !$#title Nucleotide sequence of the late region of Bacillus subtilis !1phage PZA, a close relative of phi-29. !$#cross-references MUID:87031573; PMID:3095188 !$#accession B24831 !'##molecule_type DNA !'##residues 1-448 ##label PAC !'##cross-references GB:M11813; GB:M13904; GB:M13905; NID:g216046; !1PIDN:AAA88484.1; PID:g216056 GENETICS !$#gene 8 CLASSIFICATION #superfamily phage PZA gene 8 protein KEYWORDS late protein SUMMARY #length 448 #molecular-weight 49754 #checksum 1098 SEQUENCE /// ENTRY WMBP89 #type complete TITLE gene 8 protein - phage phi-29 ALTERNATE_NAMES major head protein ORGANISM #formal_name phage phi-29 #note host Bacillus subtilis DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 23-Jul-1999 ACCESSIONS B25816 REFERENCE A25816 !$#authors Vlcek, C.; Paces, V. !$#journal Gene (1986) 46:215-225 !$#title Nucleotide sequence of the late region of Bacillus phage !1phi-29 completes the 19285-bp sequence of phi-29 genome. !1Comparison with the homologous sequence of phage PZA. !$#cross-references MUID:87106857; PMID:3803926 !$#accession B25816 !'##molecule_type DNA !'##residues 1-448 ##label VLC !'##cross-references GB:M14782; NID:g215323; PIDN:AAA32280.1; !1PID:g215325 GENETICS !$#gene 8 CLASSIFICATION #superfamily phage PZA gene 8 protein KEYWORDS head protein; late protein SUMMARY #length 448 #molecular-weight 49844 #checksum 924 SEQUENCE /// ENTRY WMBP8H #type complete TITLE gene 8.5 protein - phage PZA ORGANISM #formal_name phage PZA #note host Bacillus subtilis DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 23-Jul-1999 ACCESSIONS C24831 REFERENCE A91550 !$#authors Paces, V.; Vlcek, C.; Urbanek, P. !$#journal Gene (1986) 44:107-114 !$#title Nucleotide sequence of the late region of Bacillus subtilis !1phage PZA, a close relative of phi-29. !$#cross-references MUID:87031573; PMID:3095188 !$#accession C24831 !'##molecule_type DNA !'##residues 1-280 ##label PAC !'##cross-references GB:M11813; GB:M13904; GB:M13905; NID:g216046; !1PIDN:AAA88485.1; PID:g216057 !'##note the authors translated the codon CTT for residue 207 as Pro, !1GGG for residue 208 as Trp, TTA for residue 209 as Val, TTA !1for residue 210 as Ile, TCT for residue 211 as Ile, GGT for !1residue 212 as Val, and GCG for residue 213 as Ser GENETICS !$#gene 8.5 CLASSIFICATION #superfamily phage Nf assembly protein KEYWORDS capsid assembly; late protein SUMMARY #length 280 #molecular-weight 29457 #checksum 7245 SEQUENCE /// ENTRY WMBPHF #type complete TITLE gene 8.5 protein - phage phi-29 ALTERNATE_NAMES assembly protein; head fiber protein ORGANISM #formal_name phage phi-29 #note host Bacillus subtilis DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 23-Jul-1999 ACCESSIONS C25816 REFERENCE A25816 !$#authors Vlcek, C.; Paces, V. !$#journal Gene (1986) 46:215-225 !$#title Nucleotide sequence of the late region of Bacillus phage !1phi-29 completes the 19285-bp sequence of phi-29 genome. !1Comparison with the homologous sequence of phage PZA. !$#cross-references MUID:87106857; PMID:3803926 !$#accession C25816 !'##molecule_type DNA !'##residues 1-280 ##label VLC !'##cross-references GB:M14782; NID:g215323; PIDN:AAA32281.1; !1PID:g215326 GENETICS !$#gene 8.5 CLASSIFICATION #superfamily phage Nf assembly protein KEYWORDS capsid assembly; head protein; late protein SUMMARY #length 280 #molecular-weight 29489 #checksum 8530 SEQUENCE /// ENTRY ACBPNF #type complete TITLE probable assembly protein - phage NF ORGANISM #formal_name phage NF #note host Bacillus sp. DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 07-Nov-1997 ACCESSIONS A23632 REFERENCE A23632 !$#authors Mizukami, Y.; Sekiya, T.; Hirokawa, H. !$#journal FEBS Lett. (1986) 197:311-314 !$#title The nucleotide sequences of the heterologous region between !1the genomes of Bacillus phages M2 and Nf that indicate the !1two phages are originally identical. !$#cross-references MUID:86136589; PMID:3949018 !$#accession A23632 !'##molecule_type DNA !'##residues 1-127 ##label MIZ !'##cross-references GB:X03643; NID:g15820 !'##note Ser-3 is missing from the authors' translation !'##note the GenBank entry XXNFHB PID:g861166 differs from the published !1sequence in translating three codons, Ala-Ser-Val, before !1the initiator codon CLASSIFICATION #superfamily phage Nf assembly protein KEYWORDS capsid assembly SUMMARY #length 127 #molecular-weight 13989 #checksum 83 SEQUENCE /// ENTRY WMBP9Z #type complete TITLE gene 9 protein - phage PZA ORGANISM #formal_name phage PZA #note host Bacillus subtilis DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 23-Jul-1999 ACCESSIONS D24831 REFERENCE A91550 !$#authors Paces, V.; Vlcek, C.; Urbanek, P. !$#journal Gene (1986) 44:107-114 !$#title Nucleotide sequence of the late region of Bacillus subtilis !1phage PZA, a close relative of phi-29. !$#cross-references MUID:87031573; PMID:3095188 !$#accession D24831 !'##molecule_type DNA !'##residues 1-599 ##label PAC !'##cross-references GB:M11813; GB:M13904; GB:M13905; NID:g216046; !1PIDN:AAA88486.1; PID:g216058 GENETICS !$#gene 9 CLASSIFICATION #superfamily phage PZA gene 9 protein KEYWORDS late protein SUMMARY #length 599 #molecular-weight 67668 #checksum 1920 SEQUENCE /// ENTRY WMBPT9 #type complete TITLE gene 9 protein - phage phi-29 ALTERNATE_NAMES tail protein ORGANISM #formal_name phage phi-29 #note host Bacillus subtilis DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 23-Jul-1999 ACCESSIONS D25816; A04289 REFERENCE A25816 !$#authors Vlcek, C.; Paces, V. !$#journal Gene (1986) 46:215-225 !$#title Nucleotide sequence of the late region of Bacillus phage !1phi-29 completes the 19285-bp sequence of phi-29 genome. !1Comparison with the homologous sequence of phage PZA. !$#cross-references MUID:87106857; PMID:3803926 !$#accession D25816 !'##molecule_type DNA !'##residues 1-599 ##label VLC !'##cross-references GB:M14782; NID:g215323; PIDN:AAA32282.1; !1PID:g215327 REFERENCE A04289 !$#authors Garcia, J.A.; Mendez, E.; Salas, M. !$#journal Gene (1984) 30:87-98 !$#title Cloning, nucleotide sequence and high level expression of !1the gene coding for the connector protein of Bacillus !1subtilis phage phi-29. !$#cross-references MUID:85077631; PMID:6096227 !$#accession A04289 !'##molecule_type DNA !'##residues 265-599 ##label GAR !'##cross-references GB:M12456; NID:g215338; PIDN:AAA32291.1; !1PID:g215339 GENETICS !$#gene 9 CLASSIFICATION #superfamily phage PZA gene 9 protein KEYWORDS late protein; tail protein SUMMARY #length 599 #molecular-weight 67590 #checksum 7987 SEQUENCE /// ENTRY WMBP10 #type complete TITLE gene 10 protein - phage PZA ORGANISM #formal_name phage PZA #note host Bacillus subtilis DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 23-Jul-1999 ACCESSIONS E24831 REFERENCE A91550 !$#authors Paces, V.; Vlcek, C.; Urbanek, P. !$#journal Gene (1986) 44:107-114 !$#title Nucleotide sequence of the late region of Bacillus subtilis !1phage PZA, a close relative of phi-29. !$#cross-references MUID:87031573; PMID:3095188 !$#accession E24831 !'##molecule_type DNA !'##residues 1-309 ##label PAC !'##cross-references GB:M11813; GB:M13904; GB:M13905; NID:g216046; !1PIDN:AAA88487.1; PID:g216059 GENETICS !$#gene 10 CLASSIFICATION #superfamily phage PZA gene 10 protein KEYWORDS late protein SUMMARY #length 309 #molecular-weight 35865 #checksum 7526 SEQUENCE /// ENTRY WMBPC9 #type complete TITLE gene 10 protein - phage phi-29 ALTERNATE_NAMES connector protein; upper collar protein ORGANISM #formal_name phage phi-29 #note host Bacillus subtilis DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 23-Jul-1999 ACCESSIONS E25816; A04290 REFERENCE A25816 !$#authors Vlcek, C.; Paces, V. !$#journal Gene (1986) 46:215-225 !$#title Nucleotide sequence of the late region of Bacillus phage !1phi-29 completes the 19285-bp sequence of phi-29 genome. !1Comparison with the homologous sequence of phage PZA. !$#cross-references MUID:87106857; PMID:3803926 !$#accession E25816 !'##molecule_type DNA !'##residues 1-309 ##label VLC !'##cross-references GB:M14782; NID:g215323; PIDN:AAA32283.1; !1PID:g215328 REFERENCE A04289 !$#authors Garcia, J.A.; Mendez, E.; Salas, M. !$#journal Gene (1984) 30:87-98 !$#title Cloning, nucleotide sequence and high level expression of !1the gene coding for the connector protein of Bacillus !1subtilis phage phi-29. !$#cross-references MUID:85077631; PMID:6096227 !$#accession A04290 !'##molecule_type DNA !'##residues 1-309 ##label GAR !'##cross-references GB:M12456; NID:g215338; PIDN:AAA32292.1; !1PID:g215340 GENETICS !$#gene 10 CLASSIFICATION #superfamily phage PZA gene 10 protein KEYWORDS late protein SUMMARY #length 309 #molecular-weight 35878 #checksum 6769 SEQUENCE /// ENTRY WMBP11 #type complete TITLE gene 11 protein - phage PZA ORGANISM #formal_name phage PZA #note host Bacillus subtilis DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 23-Jul-1999 ACCESSIONS F24831 REFERENCE A91550 !$#authors Paces, V.; Vlcek, C.; Urbanek, P. !$#journal Gene (1986) 44:107-114 !$#title Nucleotide sequence of the late region of Bacillus subtilis !1phage PZA, a close relative of phi-29. !$#cross-references MUID:87031573; PMID:3095188 !$#accession F24831 !'##molecule_type DNA !'##residues 1-293 ##label PAC !'##cross-references GB:M11813; GB:M13904; GB:M13905; NID:g216046; !1PIDN:AAA88488.1; PID:g216060 GENETICS !$#gene 11 CLASSIFICATION #superfamily phage PZA gene 11 protein KEYWORDS late protein SUMMARY #length 293 #molecular-weight 33799 #checksum 7572 SEQUENCE /// ENTRY WMBPL9 #type complete TITLE gene 11 protein - phage phi-29 ALTERNATE_NAMES lower collar protein ORGANISM #formal_name phage phi-29 #note host Bacillus subtilis DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 23-Jul-1999 ACCESSIONS F25816; A04291 REFERENCE A25816 !$#authors Vlcek, C.; Paces, V. !$#journal Gene (1986) 46:215-225 !$#title Nucleotide sequence of the late region of Bacillus phage !1phi-29 completes the 19285-bp sequence of phi-29 genome. !1Comparison with the homologous sequence of phage PZA. !$#cross-references MUID:87106857; PMID:3803926 !$#accession F25816 !'##molecule_type DNA !'##residues 1-293 ##label VLC !'##cross-references GB:M14782; NID:g215323; PIDN:AAA32284.1; !1PID:g215329 REFERENCE A04289 !$#authors Garcia, J.A.; Mendez, E.; Salas, M. !$#journal Gene (1984) 30:87-98 !$#title Cloning, nucleotide sequence and high level expression of !1the gene coding for the connector protein of Bacillus !1subtilis phage phi-29. !$#cross-references MUID:85077631; PMID:6096227 !$#accession A04291 !'##molecule_type DNA !'##residues 1-89 ##label GAR GENETICS !$#gene 11 CLASSIFICATION #superfamily phage PZA gene 11 protein KEYWORDS late protein SUMMARY #length 293 #molecular-weight 33799 #checksum 7572 SEQUENCE /// ENTRY WMBP12 #type complete TITLE gene 12 protein - phage PZA ORGANISM #formal_name phage PZA #note host Bacillus subtilis DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 23-Jul-1999 ACCESSIONS G24831 REFERENCE A91550 !$#authors Paces, V.; Vlcek, C.; Urbanek, P. !$#journal Gene (1986) 44:107-114 !$#title Nucleotide sequence of the late region of Bacillus subtilis !1phage PZA, a close relative of phi-29. !$#cross-references MUID:87031573; PMID:3095188 !$#accession G24831 !'##molecule_type DNA !'##residues 1-854 ##label PAC !'##cross-references GB:M11813; GB:M13904; GB:M13905; NID:g216046; !1PIDN:AAA88489.1; PID:g216061 GENETICS !$#gene 12 CLASSIFICATION #superfamily phage PZA gene 12 protein KEYWORDS late protein SUMMARY #length 854 #molecular-weight 92072 #checksum 7500 SEQUENCE /// ENTRY WMBP22 #type complete TITLE gene 12 protein - phage phi-29 ALTERNATE_NAMES pre-neck appendage protein ORGANISM #formal_name phage phi-29 #note host Bacillus subtilis DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 23-Jul-1999 ACCESSIONS G25816 REFERENCE A25816 !$#authors Vlcek, C.; Paces, V. !$#journal Gene (1986) 46:215-225 !$#title Nucleotide sequence of the late region of Bacillus phage !1phi-29 completes the 19285-bp sequence of phi-29 genome. !1Comparison with the homologous sequence of phage PZA. !$#cross-references MUID:87106857; PMID:3803926 !$#accession G25816 !'##molecule_type DNA !'##residues 1-854 ##label VLC !'##cross-references GB:M14782; NID:g215323; PIDN:AAA32285.1; !1PID:g215330 GENETICS !$#gene 12 CLASSIFICATION #superfamily phage PZA gene 12 protein KEYWORDS late protein SUMMARY #length 854 #molecular-weight 92102 #checksum 7978 SEQUENCE /// ENTRY WMBP13 #type complete TITLE gene 13 protein - phage PZA ORGANISM #formal_name phage PZA #note host Bacillus subtilis DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 23-Jul-1999 ACCESSIONS H24831 REFERENCE A91550 !$#authors Paces, V.; Vlcek, C.; Urbanek, P. !$#journal Gene (1986) 44:107-114 !$#title Nucleotide sequence of the late region of Bacillus subtilis !1phage PZA, a close relative of phi-29. !$#cross-references MUID:87031573; PMID:3095188 !$#accession H24831 !'##molecule_type DNA !'##residues 1-365 ##label PAC !'##cross-references GB:M11813; GB:M13904; GB:M13905; NID:g216046; !1PIDN:AAA88490.1; PID:g216062 GENETICS !$#gene 13 CLASSIFICATION #superfamily phage PZA gene 13 protein KEYWORDS late protein SUMMARY #length 365 #molecular-weight 40919 #checksum 6890 SEQUENCE /// ENTRY WMBP23 #type complete TITLE gene 13 protein - phage phi-29 ALTERNATE_NAMES morphogenesis protein 1 ORGANISM #formal_name phage phi-29 #note host Bacillus subtilis DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 23-Jul-1999 ACCESSIONS H25816 REFERENCE A25816 !$#authors Vlcek, C.; Paces, V. !$#journal Gene (1986) 46:215-225 !$#title Nucleotide sequence of the late region of Bacillus phage !1phi-29 completes the 19285-bp sequence of phi-29 genome. !1Comparison with the homologous sequence of phage PZA. !$#cross-references MUID:87106857; PMID:3803926 !$#accession H25816 !'##molecule_type DNA !'##residues 1-365 ##label VLC !'##cross-references GB:M14782; NID:g215323; PIDN:AAA32286.1; !1PID:g215331 GENETICS !$#gene 13 CLASSIFICATION #superfamily phage PZA gene 13 protein KEYWORDS late protein SUMMARY #length 365 #molecular-weight 40925 #checksum 5940 SEQUENCE /// ENTRY WMBP14 #type complete TITLE gene 14 protein - phage PZA ORGANISM #formal_name phage PZA #note host Bacillus subtilis DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 23-Jul-1999 ACCESSIONS I24831 REFERENCE A91550 !$#authors Paces, V.; Vlcek, C.; Urbanek, P. !$#journal Gene (1986) 44:107-114 !$#title Nucleotide sequence of the late region of Bacillus subtilis !1phage PZA, a close relative of phi-29. !$#cross-references MUID:87031573; PMID:3095188 !$#accession I24831 !'##molecule_type DNA !'##residues 1-131 ##label PAC !'##cross-references GB:M11813; GB:M13904; GB:M13905; NID:g216046; !1PIDN:AAA88491.1; PID:g216063 GENETICS !$#gene 14 CLASSIFICATION #superfamily phage PZA gene 14 protein KEYWORDS late protein SUMMARY #length 131 #molecular-weight 14977 #checksum 4167 SEQUENCE /// ENTRY WMBP29 #type complete TITLE gene 14 protein - phage phi-29 ALTERNATE_NAMES lysis protein ORGANISM #formal_name phage phi-29 #note host Bacillus amyloliquefaciens DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 23-Jul-1999 ACCESSIONS A24721; I25816 REFERENCE A24721 !$#authors Garvey, K.J.; Saedi, M.S.; Ito, J. !$#journal Nucleic Acids Res. (1986) 14:10001-10008 !$#title Nucleotide sequence of Bacillus phage phi-29 genes 14 and !115: homology of gene 15 with other phage lysozymes. !$#cross-references MUID:87117505; PMID:3027653 !$#accession A24721 !'##molecule_type DNA !'##residues 1-131 ##label GAR !'##cross-references GB:X04962; NID:g15676; PIDN:CAA28631.1; PID:g15678 REFERENCE A25816 !$#authors Vlcek, C.; Paces, V. !$#journal Gene (1986) 46:215-225 !$#title Nucleotide sequence of the late region of Bacillus phage !1phi-29 completes the 19285-bp sequence of phi-29 genome. !1Comparison with the homologous sequence of phage PZA. !$#cross-references MUID:87106857; PMID:3803926 !$#accession I25816 !'##molecule_type DNA !'##residues 1-131 ##label VLC GENETICS !$#gene 14 CLASSIFICATION #superfamily phage PZA gene 14 protein KEYWORDS host cell lysis; late protein SUMMARY #length 131 #molecular-weight 15032 #checksum 3983 SEQUENCE /// ENTRY WMBP16 #type complete TITLE gene 16 protein - phage PZA ORGANISM #formal_name phage PZA #note host Bacillus subtilis DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 23-Jul-1999 ACCESSIONS B26215; K24831 REFERENCE A91550 !$#authors Paces, V.; Vlcek, C.; Urbanek, P. !$#journal Gene (1986) 44:107-114 !$#title Nucleotide sequence of the late region of Bacillus subtilis !1phage PZA, a close relative of phi-29. !$#cross-references MUID:87031573; PMID:3095188 !$#accession B26215 !'##molecule_type DNA !'##residues 1-332 ##label PAC !'##cross-references GB:M11813; GB:M13904; GB:M13905; NID:g216046; !1PIDN:AAA88493.1; PID:g216065 GENETICS !$#gene 16 CLASSIFICATION #superfamily phage PZA gene 16 protein KEYWORDS late protein SUMMARY #length 332 #molecular-weight 38959 #checksum 5552 SEQUENCE /// ENTRY WMBP26 #type complete TITLE gene 16 protein - phage phi-29 ALTERNATE_NAMES encapsidation protein ORGANISM #formal_name phage phi-29 #note host Bacillus subtilis DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 23-Jul-1999 ACCESSIONS B33078; JQ0168 REFERENCE A25816 !$#authors Vlcek, C.; Paces, V. !$#journal Gene (1986) 46:215-225 !$#title Nucleotide sequence of the late region of Bacillus phage !1phi-29 completes the 19285-bp sequence of phi-29 genome. !1Comparison with the homologous sequence of phage PZA. !$#cross-references MUID:87106857; PMID:3803926 !$#accession B33078 !'##molecule_type DNA !'##residues 1-332 ##label VLC !'##cross-references GB:M14782; NID:g215323; PIDN:AAA32289.1; !1PID:g215334 REFERENCE JQ0168 !$#authors Garvey, K.J.; Saedi, M.S.; Ito, J. !$#journal Gene (1985) 40:311-316 !$#title The complete sequence of Bacillus phage phi-29 gene 16: a !1protein required for the genome encapsidation reaction. !$#cross-references MUID:86165873; PMID:3879485 !$#accession JQ0168 !'##molecule_type DNA !'##residues 1-332 ##label GAR !'##cross-references GB:M14431; NID:g215319; PIDN:AAA88348.1; !1PID:g215320 COMMENT This protein catalyzes the in vivo and in vitro !1genome-encapsidation reaction. GENETICS !$#gene 16 CLASSIFICATION #superfamily phage PZA gene 16 protein KEYWORDS late protein SUMMARY #length 332 #molecular-weight 38964 #checksum 5597 SEQUENCE /// ENTRY WRBP65 #type complete TITLE early protein gp5 - phage PZA ORGANISM #formal_name phage PZA #note host Bacillus subtilis DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 23-Jul-1999 ACCESSIONS A29004 REFERENCE A91551 !$#authors Paces, V.; Vlcek, C.; Urbanek, P.; Hostomsky, Z. !$#journal Gene (1986) 44:115-120 !$#title Nucleotide sequence of the right early region of Bacillus !1subtilis phage PZA completes the 19366-bp sequence of PZA !1genome. Comparison with the homologous sequence of phage !1phi-29. !$#cross-references MUID:87031575; PMID:3095189 !$#accession A29004 !'##molecule_type DNA !'##residues 1-37 ##label PAC !'##cross-references GB:M11813; GB:M13904; GB:M13905; NID:g216046; !1PIDN:AAA88494.1; PID:g455338 GENETICS !$#gene 16.5 CLASSIFICATION #superfamily phage PZA early protein gp5 KEYWORDS early protein SUMMARY #length 37 #molecular-weight 4657 #checksum 4683 SEQUENCE /// ENTRY WRBPF7 #type complete TITLE early protein gp5 - phage phi-15 ORGANISM #formal_name phage phi-15 #note host Bacillus subtilis DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 23-Jul-1999 ACCESSIONS JS0197 REFERENCE JS0192 !$#authors Benes, V.; Arnold, L.; Smrt, J.; Paces, V. !$#journal Gene (1989) 75:341-347 !$#title Nucleotide sequence of the right early region of Bacillus !1phage phi-15 and comparison with related phages: !1reorganization of gene 17 during evolution. !$#cross-references MUID:89232766; PMID:2497055 !$#accession JS0197 !'##molecule_type DNA !'##residues 1-37 ##label BEN !'##cross-references GB:M28830; NID:g215438; PIDN:AAA32334.1; !1PID:g215444 GENETICS !$#gene 16.5 CLASSIFICATION #superfamily phage PZA early protein gp5 KEYWORDS early protein SUMMARY #length 37 #molecular-weight 4657 #checksum 4683 SEQUENCE /// ENTRY WRBP66 #type complete TITLE early protein gp6 - phage PZA ORGANISM #formal_name phage PZA #note host Bacillus subtilis DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 23-Jul-1999 ACCESSIONS B29004 REFERENCE A91551 !$#authors Paces, V.; Vlcek, C.; Urbanek, P.; Hostomsky, Z. !$#journal Gene (1986) 44:115-120 !$#title Nucleotide sequence of the right early region of Bacillus !1subtilis phage PZA completes the 19366-bp sequence of PZA !1genome. Comparison with the homologous sequence of phage !1phi-29. !$#cross-references MUID:87031575; PMID:3095189 !$#accession B29004 !'##molecule_type DNA !'##residues 1-54 ##label PAC !'##cross-references GB:M11813; GB:M13904; GB:M13905; NID:g216046; !1PIDN:AAA88495.1; PID:g455339 GENETICS !$#gene 16.6 CLASSIFICATION #superfamily phage PZA early protein gp6 KEYWORDS early protein SUMMARY #length 54 #molecular-weight 6114 #checksum 1816 SEQUENCE /// ENTRY WRBPF6 #type complete TITLE early protein gp6 - phage phi-15 ORGANISM #formal_name phage phi-15 #note host Bacillus subtilis DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 23-Jul-1999 ACCESSIONS JS0196 REFERENCE JS0192 !$#authors Benes, V.; Arnold, L.; Smrt, J.; Paces, V. !$#journal Gene (1989) 75:341-347 !$#title Nucleotide sequence of the right early region of Bacillus !1phage phi-15 and comparison with related phages: !1reorganization of gene 17 during evolution. !$#cross-references MUID:89232766; PMID:2497055 !$#accession JS0196 !'##molecule_type DNA !'##residues 1-54 ##label BEN !'##cross-references GB:M28830; NID:g215438; PIDN:AAA32333.1; !1PID:g215443 GENETICS !$#gene 16.6 CLASSIFICATION #superfamily phage PZA early protein gp6 KEYWORDS early protein SUMMARY #length 54 #molecular-weight 6128 #checksum 1894 SEQUENCE /// ENTRY WRBP67 #type complete TITLE early protein gp15 - phage PZA ORGANISM #formal_name phage PZA #note host Bacillus subtilis DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 23-Jul-1999 ACCESSIONS C29004 REFERENCE A91551 !$#authors Paces, V.; Vlcek, C.; Urbanek, P.; Hostomsky, Z. !$#journal Gene (1986) 44:115-120 !$#title Nucleotide sequence of the right early region of Bacillus !1subtilis phage PZA completes the 19366-bp sequence of PZA !1genome. Comparison with the homologous sequence of phage !1phi-29. !$#cross-references MUID:87031575; PMID:3095189 !$#accession C29004 !'##molecule_type DNA !'##residues 1-130 ##label PAC !'##cross-references GB:M11813; GB:M13904; GB:M13905; NID:g216046; !1PIDN:AAA88496.1; PID:g1196804 GENETICS !$#gene 16.7 CLASSIFICATION #superfamily phage PZA early protein gp15 KEYWORDS early protein SUMMARY #length 130 #molecular-weight 15222 #checksum 4667 SEQUENCE /// ENTRY WRBPF5 #type complete TITLE early protein gp15 - phage phi-15 ORGANISM #formal_name phage phi-15 #note host Bacillus subtilis DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 23-Jul-1999 ACCESSIONS JS0195 REFERENCE JS0192 !$#authors Benes, V.; Arnold, L.; Smrt, J.; Paces, V. !$#journal Gene (1989) 75:341-347 !$#title Nucleotide sequence of the right early region of Bacillus !1phage phi-15 and comparison with related phages: !1reorganization of gene 17 during evolution. !$#cross-references MUID:89232766; PMID:2497055 !$#accession JS0195 !'##molecule_type DNA !'##residues 1-130 ##label BEN !'##cross-references GB:M28830; NID:g215438; PIDN:AAA32332.1; !1PID:g215442 GENETICS !$#gene 16.7 CLASSIFICATION #superfamily phage PZA early protein gp15 KEYWORDS early protein SUMMARY #length 130 #molecular-weight 15293 #checksum 5831 SEQUENCE /// ENTRY WRBP68 #type complete TITLE early protein gp12 - phage PZA ORGANISM #formal_name phage PZA #note host Bacillus subtilis DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 23-Jul-1999 ACCESSIONS D29004 REFERENCE A91551 !$#authors Paces, V.; Vlcek, C.; Urbanek, P.; Hostomsky, Z. !$#journal Gene (1986) 44:115-120 !$#title Nucleotide sequence of the right early region of Bacillus !1subtilis phage PZA completes the 19366-bp sequence of PZA !1genome. Comparison with the homologous sequence of phage !1phi-29. !$#cross-references MUID:87031575; PMID:3095189 !$#accession D29004 !'##molecule_type DNA !'##residues 1-105 ##label PAC !'##cross-references GB:M11813; GB:M13904; GB:M13905; NID:g216046; !1PIDN:AAA88497.1; PID:g1196805 GENETICS !$#gene 16.8 CLASSIFICATION #superfamily phage PZA early protein gp12 KEYWORDS early protein SUMMARY #length 105 #molecular-weight 12444 #checksum 7560 SEQUENCE /// ENTRY WRBP12 #type complete TITLE early protein gp12 - phage phi-15 ORGANISM #formal_name phage phi-15 #note host Bacillus subtilis DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 23-Jul-1999 ACCESSIONS JS0194 REFERENCE JS0192 !$#authors Benes, V.; Arnold, L.; Smrt, J.; Paces, V. !$#journal Gene (1989) 75:341-347 !$#title Nucleotide sequence of the right early region of Bacillus !1phage phi-15 and comparison with related phages: !1reorganization of gene 17 during evolution. !$#cross-references MUID:89232766; PMID:2497055 !$#accession JS0194 !'##molecule_type DNA !'##residues 1-105 ##label BEN !'##cross-references GB:M28830; NID:g215438; PIDN:AAA32331.1; !1PID:g215441 GENETICS !$#gene 16.8 CLASSIFICATION #superfamily phage PZA early protein gp12 SUMMARY #length 105 #molecular-weight 12444 #checksum 7560 SEQUENCE /// ENTRY WRBP69 #type complete TITLE early protein gp13 - phage PZA ORGANISM #formal_name phage PZA #note host Bacillus subtilis DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 23-Jul-1999 ACCESSIONS E29004 REFERENCE A91551 !$#authors Paces, V.; Vlcek, C.; Urbanek, P.; Hostomsky, Z. !$#journal Gene (1986) 44:115-120 !$#title Nucleotide sequence of the right early region of Bacillus !1subtilis phage PZA completes the 19366-bp sequence of PZA !1genome. Comparison with the homologous sequence of phage !1phi-29. !$#cross-references MUID:87031575; PMID:3095189 !$#accession E29004 !'##molecule_type DNA !'##residues 1-108 ##label PAC !'##cross-references GB:M11813; GB:M13904; GB:M13905; NID:g216046; !1PIDN:AAA88498.1; PID:g455340 GENETICS !$#gene 16.9 CLASSIFICATION #superfamily phage PZA early protein gp13 KEYWORDS early protein SUMMARY #length 108 #molecular-weight 12648 #checksum 8323 SEQUENCE /// ENTRY WRBP13 #type complete TITLE early protein gp13 - phage phi-15 ORGANISM #formal_name phage phi-15 #note host Bacillus subtilis DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 23-Jul-1999 ACCESSIONS JS0193 REFERENCE JS0192 !$#authors Benes, V.; Arnold, L.; Smrt, J.; Paces, V. !$#journal Gene (1989) 75:341-347 !$#title Nucleotide sequence of the right early region of Bacillus !1phage phi-15 and comparison with related phages: !1reorganization of gene 17 during evolution. !$#cross-references MUID:89232766; PMID:2497055 !$#accession JS0193 !'##molecule_type DNA !'##residues 1-108 ##label BEN !'##cross-references GB:M28830; NID:g215438; PIDN:AAA32330.1; !1PID:g215440 GENETICS !$#gene 16.9 CLASSIFICATION #superfamily phage PZA early protein gp13 KEYWORDS early protein SUMMARY #length 108 #molecular-weight 12648 #checksum 8323 SEQUENCE /// ENTRY WRBP70 #type complete TITLE early protein gp17 - phage PZA ORGANISM #formal_name phage PZA #note host Bacillus subtilis DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 23-Jul-1999 ACCESSIONS F29004 REFERENCE A91551 !$#authors Paces, V.; Vlcek, C.; Urbanek, P.; Hostomsky, Z. !$#journal Gene (1986) 44:115-120 !$#title Nucleotide sequence of the right early region of Bacillus !1subtilis phage PZA completes the 19366-bp sequence of PZA !1genome. Comparison with the homologous sequence of phage !1phi-29. !$#cross-references MUID:87031575; PMID:3095189 !$#accession F29004 !'##molecule_type DNA !'##residues 1-174 ##label PAC !'##cross-references GB:M11813; GB:M13904; GB:M13905; NID:g216046; !1PIDN:AAA88499.1; PID:g455341 GENETICS !$#gene 17 CLASSIFICATION #superfamily phage PZA early protein gp17 KEYWORDS early protein SUMMARY #length 174 #molecular-weight 20022 #checksum 3530 SEQUENCE /// ENTRY WRBP15 #type complete TITLE early protein gp17 - phage phi-15 ORGANISM #formal_name phage phi-15 #note host Bacillus subtilis DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 23-Jul-1999 ACCESSIONS JS0192 REFERENCE JS0192 !$#authors Benes, V.; Arnold, L.; Smrt, J.; Paces, V. !$#journal Gene (1989) 75:341-347 !$#title Nucleotide sequence of the right early region of Bacillus !1phage phi-15 and comparison with related phages: !1reorganization of gene 17 during evolution. !$#cross-references MUID:89232766; PMID:2497055 !$#accession JS0192 !'##molecule_type DNA !'##residues 1-153 ##label BEN !'##cross-references GB:M28830; NID:g215438; PIDN:AAA32329.1; !1PID:g215439 COMMENT This protein is involved in the replication of phage DNA. GENETICS !$#gene 17 CLASSIFICATION #superfamily phage PZA early protein gp17 KEYWORDS early protein SUMMARY #length 153 #molecular-weight 17590 #checksum 6983 SEQUENCE /// ENTRY WMBP2P #type complete TITLE ogr protein - phage P2 ORGANISM #formal_name phage P2 DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 23-Jul-1999 ACCESSIONS A24826 REFERENCE A24826 !$#authors Birkeland, N.K.; Lindqvist, B.H. !$#journal J. Mol. Biol. (1986) 188:487-490 !$#title Coliphage P2 late control gene ogr DNA sequence and product !1identification. !$#cross-references MUID:86281704; PMID:3735430 !$#accession A24826 !'##molecule_type DNA !'##residues 1-72 ##label BIR !'##cross-references GB:X03782; NID:g15148; PIDN:CAA27414.1; PID:g15149 GENETICS !$#gene ogr CLASSIFICATION #superfamily phage P2 ogr protein KEYWORDS late protein; transcription regulation; zinc finger FEATURE !$4-35 #region zinc finger CCCC motif SUMMARY #length 72 #molecular-weight 8342 #checksum 6780 SEQUENCE /// ENTRY WMBPP4 #type complete TITLE transactivation protein - satellite phage P4 ORGANISM #formal_name satellite phage P4 DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 08-Dec-2000 ACCESSIONS B23878 REFERENCE A93544 !$#authors Lin, C.S. !$#journal Nucleic Acids Res. (1984) 12:8667-8684 !$#title Nucleotide sequence of the essential region of bacteriophage !1P4. !$#cross-references MUID:85062840; PMID:6095206 !$#accession B23878 !'##molecule_type DNA !'##residues 1-155 ##label LIN !'##cross-references GB:X02534 GENETICS !$#gene delta CLASSIFICATION #superfamily phage P2 ogr protein KEYWORDS DNA binding; late protein; transcription regulation; zinc !1finger FEATURE !$4-35 #region zinc finger CCCC motif SUMMARY #length 155 #molecular-weight 17719 #checksum 72 SEQUENCE /// ENTRY WPBPP2 #type complete TITLE repressor protein C - phage P2 ORGANISM #formal_name phage P2 DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Feb-1997 ACCESSIONS A05127 REFERENCE A05127 !$#authors Ljungquist, E.; Kockum, K.; Bertani, L.E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:3988-3992 !$#title DNA sequences of the repressor gene and operator region of !1bacteriophage P2. !$#cross-references MUID:84248044; PMID:6330728 !$#accession A05127 !'##molecule_type DNA !'##residues 1-99 ##label LJU CLASSIFICATION #superfamily phage P2 repressor protein C KEYWORDS DNA binding; repressor; transcription regulation SUMMARY #length 99 #molecular-weight 11077 #checksum 9520 SEQUENCE /// ENTRY RBBP22 #type complete TITLE abc1 protein - phage P22 ORGANISM #formal_name phage P22 #note host Salmonella typhimurium DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 23-Jul-1999 ACCESSIONS A27841 REFERENCE A94366 !$#authors Murphy, K.C.; Fenton, A.C.; Poteete, A.R. !$#journal Virology (1987) 160:456-464 !$#title Sequence of the bacteriophage P22 anti-recBCD (abc) genes !1and properties of P22 abc region deletion mutants. !$#cross-references MUID:88019195; PMID:3660589 !$#accession A27841 !'##molecule_type DNA !'##residues 1-94 ##label MUR !'##cross-references GB:J02471; GB:M17737; NID:g215277; PIDN:AAA88344.1; !1PID:g215279 !'##note the authors translated the codon TTA for residues 4 and 91 as !1Lys, ACG for residues 45 and 62 as Tyr, and CTA for residue !188 as Lys GENETICS !$#gene abc1 CLASSIFICATION #superfamily phage P22 abc1 protein SUMMARY #length 94 #molecular-weight 10895 #checksum 9384 SEQUENCE /// ENTRY RCBP22 #type complete TITLE abc2 protein - phage P22 ORGANISM #formal_name phage P22 #note host Salmonella typhimurium DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 23-Jul-1999 ACCESSIONS B27841 REFERENCE A94366 !$#authors Murphy, K.C.; Fenton, A.C.; Poteete, A.R. !$#journal Virology (1987) 160:456-464 !$#title Sequence of the bacteriophage P22 anti-recBCD (abc) genes !1and properties of P22 abc region deletion mutants. !$#cross-references MUID:88019195; PMID:3660589 !$#accession B27841 !'##molecule_type DNA !'##residues 1-97 ##label MUR !'##cross-references GB:J02471; GB:M17737; NID:g215277; PIDN:AAA88345.1; !1PID:g215280 !'##note the authors translated the codon TTG for residue 5 as Lys, ACG !1for residue 40 as Tyr, and TAC for residue 91 as Thr GENETICS !$#gene abc2 CLASSIFICATION #superfamily phage P22 abc2 protein SUMMARY #length 97 #molecular-weight 11620 #checksum 7122 SEQUENCE /// ENTRY RDBP22 #type complete TITLE orf-56 protein - phage P22 ALTERNATE_NAMES hypothetical protein 56 (eaE 5' region) ORGANISM #formal_name phage P22 #note host Salmonella typhimurium DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 23-Jul-1999 ACCESSIONS C27841; S35288; S36951 REFERENCE A94366 !$#authors Murphy, K.C.; Fenton, A.C.; Poteete, A.R. !$#journal Virology (1987) 160:456-464 !$#title Sequence of the bacteriophage P22 anti-recBCD (abc) genes !1and properties of P22 abc region deletion mutants. !$#cross-references MUID:88019195; PMID:3660589 !$#accession C27841 !'##molecule_type DNA !'##residues 1-56 ##label MUR !'##cross-references GB:J02471; GB:M17737; NID:g215277; PIDN:AAA88346.1; !1PID:g1196686 !'##note the authors translated the codon ACA for residue 26 as Tyr and !1CCT for residue 37 as Phe REFERENCE S35280 !$#authors Wulff, D.L.; Ho, Y.S.; Powers, S.; Rosenberg, M. !$#journal Mol. Microbiol. (1993) 9:261-271 !$#title The int genes of bacteriophages P22 and lambda are regulated !1by different mechanisms. !$#cross-references MUID:94018622; PMID:8412679 !$#accession S35288 !'##status preliminary !'##molecule_type DNA !'##residues 47-56 ##label WU2 !'##cross-references EMBL:L06296 CLASSIFICATION #superfamily phage P22 orf-56 protein SUMMARY #length 56 #molecular-weight 6634 #checksum 1412 SEQUENCE /// ENTRY QQBP22 #type complete TITLE orf-201 protein - phage P22 ORGANISM #formal_name phage P22 #note host Salmonella typhimurium DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 23-Jul-1999 ACCESSIONS B33080 REFERENCE A33080 !$#authors Casjens, S.; Eppler, K.; Parr, R.; Poteete, A.R. !$#journal Virology (1989) 171:588-598 !$#title Nucleotide sequence of the bacteriophage P22 gene 19 to 3 !1region: identification of a new gene required for lysis. !$#cross-references MUID:89348017; PMID:2763468 !$#accession B33080 !'##molecule_type DNA !'##residues 1-201 ##label CAS !'##cross-references GB:J04356; NID:g215265; PIDN:AAA88342.1; !1PID:g1196685 CLASSIFICATION #superfamily phage P22 orf-201 protein SUMMARY #length 201 #molecular-weight 22762 #checksum 9118 SEQUENCE /// ENTRY Z1BP22 #type complete TITLE gene 1 protein - phage P22 ORGANISM #formal_name phage P22 #note host Salmonella typhimurium DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 23-Jul-1999 ACCESSIONS C40474 REFERENCE A40474 !$#authors Eppler, K.; Wyckoff, E.; Goates, J.; Parr, R.; Casjens, S. !$#journal Virology (1991) 183:519-538 !$#title Nucleotide sequence of the bacteriophage P22 genes required !1for DNA packaging. !$#cross-references MUID:91306435; PMID:1853558 !$#accession C40474 !'##molecule_type DNA !'##residues 1-725 ##label EPP !'##cross-references GB:M59749; NID:g215302; PIDN:AAA72961.1; !1PID:g553006 GENETICS !$#gene 1 CLASSIFICATION #superfamily phage P22 gene 1 protein SUMMARY #length 725 #molecular-weight 82742 #checksum 9976 SEQUENCE /// ENTRY Z2BP22 #type complete TITLE gene 2 protein - phage P22 ORGANISM #formal_name phage P22 #note host Salmonella typhimurium DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 23-Jul-1999 ACCESSIONS B40474 REFERENCE A40474 !$#authors Eppler, K.; Wyckoff, E.; Goates, J.; Parr, R.; Casjens, S. !$#journal Virology (1991) 183:519-538 !$#title Nucleotide sequence of the bacteriophage P22 genes required !1for DNA packaging. !$#cross-references MUID:91306435; PMID:1853558 !$#accession B40474 !'##molecule_type DNA !'##residues 1-499 ##label EPP !'##cross-references GB:M59749; NID:g215302; PIDN:AAA72959.1; !1PID:g553005 GENETICS !$#gene 2 CLASSIFICATION #superfamily phage P22 gene 2 protein KEYWORDS DNA packaging SUMMARY #length 499 #molecular-weight 57591 #checksum 3962 SEQUENCE /// ENTRY Z2BPL7 #type fragment TITLE gene 2 protein - phage LP-7 (fragment) ORGANISM #formal_name phage LP-7 DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 23-Jul-1999 ACCESSIONS PQ0094 REFERENCE PQ0093 !$#authors Petri, J.B.; Schmieger, H. !$#journal Gene (1990) 88:47-55 !$#title Isolation of fragments with pac function for phage P22 from !1phage LP7 DNA and comparison of packaging gene 3 sequences. !$#cross-references MUID:90255967; PMID:2341038 !$#accession PQ0094 !'##molecule_type DNA !'##residues 1-475 ##label PET !'##cross-references GB:M32403; NID:g215205; PIDN:AAA88220.1; !1PID:g553003 !'##note the authors translated the codon TGG for residue 148 as Thr, !1CAG for residues 246 and 263 as Asn, and CAA for residue 266 !1as Asp COMMENT This protein is involved in the initiation of phage DNA !1packaging. GENETICS !$#gene 2 CLASSIFICATION #superfamily phage P22 gene 2 protein KEYWORDS DNA packaging SUMMARY #length 475 #checksum 1949 SEQUENCE /// ENTRY Z3BP22 #type complete TITLE gene 3 protein - phage P22 ORGANISM #formal_name phage P22 #note host Salmonella typhimurium DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 23-Jul-1999 ACCESSIONS A04292; A40474 REFERENCE A04292 !$#authors Backhaus, H. !$#journal J. Virol. (1985) 55:458-465 !$#title DNA packaging initiation of Salmonella bacteriophage P22: !1determination of cut sites within the DNA sequence coding !1for gene 3. !$#cross-references MUID:85264998; PMID:2991569 !$#accession A04292 !'##molecule_type DNA !'##residues 1-162 ##label BAC !'##cross-references GB:M10075; NID:g215300; PIDN:AAA32272.1; !1PID:g215301 REFERENCE A40474 !$#authors Eppler, K.; Wyckoff, E.; Goates, J.; Parr, R.; Casjens, S. !$#journal Virology (1991) 183:519-538 !$#title Nucleotide sequence of the bacteriophage P22 genes required !1for DNA packaging. !$#cross-references MUID:91306435; PMID:1853558 !$#accession A40474 !'##molecule_type DNA !'##residues 1-162 ##label EPP !'##cross-references GB:M59749; NID:g215302; PIDN:AAA72958.1; !1PID:g215303 COMMENT This protein is involved in the initiation of phage DNA !1packaging. GENETICS !$#gene 3 CLASSIFICATION #superfamily phage P22 gene 3 protein KEYWORDS DNA packaging SUMMARY #length 162 #molecular-weight 18650 #checksum 265 SEQUENCE /// ENTRY Z3BPL7 #type complete TITLE gene 3 protein - phage LP-7 ORGANISM #formal_name phage LP-7 DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 23-Jul-1999 ACCESSIONS JQ0531 REFERENCE PQ0093 !$#authors Petri, J.B.; Schmieger, H. !$#journal Gene (1990) 88:47-55 !$#title Isolation of fragments with pac function for phage P22 from !1phage LP7 DNA and comparison of packaging gene 3 sequences. !$#cross-references MUID:90255967; PMID:2341038 !$#accession JQ0531 !'##molecule_type DNA !'##residues 1-162 ##label PET !'##cross-references GB:M32403; NID:g215205; PIDN:AAA88219.1; !1PID:g215206 COMMENT This protein is involved in the initiation of phage DNA !1packaging. GENETICS !$#gene 3 CLASSIFICATION #superfamily phage P22 gene 3 protein KEYWORDS DNA packaging SUMMARY #length 162 #molecular-weight 18757 #checksum 454 SEQUENCE /// ENTRY Z4BP22 #type complete TITLE gene 4 protein - phage P22 ORGANISM #formal_name phage P22 #note host Salmonella typhimurium DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 23-Jul-1999 ACCESSIONS F40474 REFERENCE A40474 !$#authors Eppler, K.; Wyckoff, E.; Goates, J.; Parr, R.; Casjens, S. !$#journal Virology (1991) 183:519-538 !$#title Nucleotide sequence of the bacteriophage P22 genes required !1for DNA packaging. !$#cross-references MUID:91306435; PMID:1853558 !$#accession F40474 !'##molecule_type DNA !'##residues 1-166 ##label EPP !'##cross-references GB:M59749; NID:g215302; PIDN:AAA72964.1; !1PID:g553009 GENETICS !$#gene 4 CLASSIFICATION #superfamily phage P22 gene 4 protein SUMMARY #length 166 #molecular-weight 18025 #checksum 761 SEQUENCE /// ENTRY Z5BP22 #type complete TITLE coat protein - phage P22 ORGANISM #formal_name phage P22 #note host Salmonella typhimurium DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 23-Jul-1999 ACCESSIONS E40474 REFERENCE A40474 !$#authors Eppler, K.; Wyckoff, E.; Goates, J.; Parr, R.; Casjens, S. !$#journal Virology (1991) 183:519-538 !$#title Nucleotide sequence of the bacteriophage P22 genes required !1for DNA packaging. !$#cross-references MUID:91306435; PMID:1853558 !$#accession E40474 !'##molecule_type DNA !'##residues 1-430 ##label EPP !'##cross-references GB:M59749; NID:g215302; PIDN:AAA72963.1; !1PID:g553008 GENETICS !$#gene 5 CLASSIFICATION #superfamily phage P22 coat protein KEYWORDS coat protein SUMMARY #length 430 #molecular-weight 46751 #checksum 7835 SEQUENCE /// ENTRY Z8BP22 #type complete TITLE gene 8 protein - phage P22 ORGANISM #formal_name phage P22 #note host Salmonella typhimurium DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 23-Jul-1999 ACCESSIONS D40474 REFERENCE A40474 !$#authors Eppler, K.; Wyckoff, E.; Goates, J.; Parr, R.; Casjens, S. !$#journal Virology (1991) 183:519-538 !$#title Nucleotide sequence of the bacteriophage P22 genes required !1for DNA packaging. !$#cross-references MUID:91306435; PMID:1853558 !$#accession D40474 !'##molecule_type DNA !'##residues 1-303 ##label EPP !'##cross-references GB:M59749; NID:g215302; PIDN:AAA72962.1; !1PID:g553007 GENETICS !$#gene 8 CLASSIFICATION #superfamily phage P22 gene 8 protein SUMMARY #length 303 #molecular-weight 33564 #checksum 2121 SEQUENCE /// ENTRY A42537 #type complete TITLE gene 16 protein - phage P22 ORGANISM #formal_name phage P22 #note host Salmonella typhimurium DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 23-Jul-1999 ACCESSIONS A42537 REFERENCE A42537 !$#authors Umlauf, B.; Dreiseikelmann, B. !$#journal Virology (1992) 188:495-501 !$#title Cloning, sequencing, and overexpression of gene 16 of !1Salmonella bacteriophage P22. !$#cross-references MUID:92263752; PMID:1585633 !$#accession A42537 !'##molecule_type DNA !'##residues 1-609 ##label UML !'##cross-references GB:M74136; NID:g215281; PIDN:AAA79250.1; !1PID:g215282 GENETICS !$#gene 16 CLASSIFICATION #superfamily phage 22 gene 16 protein SUMMARY #length 609 #molecular-weight 64357 #checksum 906 SEQUENCE /// ENTRY Z8BPC2 #type complete TITLE gene 18 protein - phage P22 ALTERNATE_NAMES replication protein ORGANISM #formal_name phage P22 #note host Salmonella typhimurium DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 23-Jul-1999 ACCESSIONS A04293 REFERENCE A91518 !$#authors Backhaus, H.; Petri, J.B. !$#journal Gene (1984) 32:289-303 !$#title Sequence analysis of a region from the early right operon in !1phage P22 including the replication genes 18 and 12. !$#cross-references MUID:85155495; PMID:6241581 !$#accession A04293 !'##molecule_type DNA !'##residues 1-271 ##label BAC !'##cross-references GB:M10074; NID:g215307; PIDN:AAA32275.1; !1PID:g215310 COMMENT This protein is related to the replication protein O of !1bacteriophage lambda. GENETICS !$#gene 18 CLASSIFICATION #superfamily phage P22 gene 18 protein KEYWORDS replication SUMMARY #length 271 #molecular-weight 30557 #checksum 9559 SEQUENCE /// ENTRY ORBPL #type complete TITLE replication protein O - phage lambda ORGANISM #formal_name phage lambda DATE 31-Mar-1980 #sequence_revision 29-Jun-1981 #text_change 17-Jul-1998 ACCESSIONS F94614; H92891; A93689; A93195; A04294 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession F94614 !'##molecule_type DNA !'##residues 1-333 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession H92891 !'##molecule_type DNA !'##residues 1-333 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104 REFERENCE A93689 !$#authors Scherer, G. !$#journal Nucleic Acids Res. (1978) 5:3141-3156 !$#title Nucleotide sequence of the O gene and of the origin of !1replication in bacteriophage lambda DNA. !$#cross-references MUID:79033241; PMID:704348 !$#contents lambda-dvh93, residues 44-333; lambda, residues 1-43 !$#accession A93689 !'##molecule_type DNA !'##residues 1-43;44-133 ##label SCHE !'##note lambda-dvh93 is a bacteriophage lambda-derived E. coli plasmid !'##note the amino end of replication protein O may be as shown or may !1begin at residue 22; there is a UGA terminator after residue !1299. In vitro, this terminator codon is skipped and !1read-through occurs; it is not known whether read-through !1occurs in vivo REFERENCE A93195 !$#authors Schwarz, E.; Scherer, G.; Hobom, G.; Kossel, H. !$#journal Nature (1978) 272:410-414 !$#title Nucleotide sequence of cro, cII and part of the O gene in !1phage lambda DNA. !$#cross-references MUID:78135462; PMID:264238 !$#accession A93195 !'##molecule_type DNA !'##residues 1-99 ##label SCHW COMMENT Replication protein O is necessary for the bidirectional !1replication of lambda DNA. It interacts with the ori (origin !1of replication) region of the genome during the initiation !1of replication. GENETICS !$#gene O !$#map_position 79.76-81.83 CLASSIFICATION #superfamily phage P22 gene 18 protein KEYWORDS DNA binding SUMMARY #length 333 #molecular-weight 37772 #checksum 3192 SEQUENCE /// ENTRY ORBP15 #type complete TITLE replication protein 15 - phage phi-80 ORGANISM #formal_name phage phi-80 #note host Escherichia coli DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 23-Jul-1999 ACCESSIONS S01776 REFERENCE S01776 !$#authors Ogawa, T.; Ogawa, H.; Tomizawa, J.I. !$#journal J. Mol. Biol. (1988) 202:537-550 !$#title Organization of the early region of bacteriophage phi-80. !1Genes and proteins. !$#cross-references MUID:89011978; PMID:3172225 !$#accession S01776 !'##molecule_type DNA !'##residues 1-302 ##label OGA !'##cross-references EMBL:X13065; NID:g14800; PIDN:CAA31474.1; !1PID:g14807 GENETICS !$#gene 15 CLASSIFICATION #superfamily phage P22 gene 18 protein KEYWORDS DNA binding SUMMARY #length 302 #molecular-weight 34333 #checksum 7767 SEQUENCE /// ENTRY PQBPL #type complete TITLE replication protein P - phage lambda ORGANISM #formal_name phage lambda DATE 31-Mar-1981 #sequence_revision 31-Mar-1981 #text_change 23-Jul-1999 ACCESSIONS G94614; I92891; A90234; A04295 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession G94614 !'##molecule_type DNA !'##residues 1-233 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession I92891 !'##molecule_type DNA !'##residues 1-233 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96585.1; PID:g215151 REFERENCE A90234 !$#authors Schwarz, E.; Scherer, G.; Hobom, G.; Kossel, H. !$#journal Biochem. Int. (1980) 1:386-394 !$#title The primary structure of the phage lambda P gene completes !1the nucleotide sequence of the plasmid lambda dvh93. !$#contents lambda-dvo21 !$#accession A90234 !'##molecule_type DNA !'##residues 1-233 ##label SCH !'##note lambda-dvo21 is a bacteriophage lambda-derived E. coli plasmid COMMENT Replication protein P is necessary for the bidirectional !1replication of lambda DNA. It interacts with the ori (origin !1of replication) region of the genome during the initiation !1of replication. GENETICS !$#gene P !$#map_position 81.61-83.05 CLASSIFICATION #superfamily phage lambda replication protein P SUMMARY #length 233 #molecular-weight 26518 #checksum 4779 SEQUENCE /// ENTRY PQBP14 #type complete TITLE replication protein 14 - phage phi-80 ORGANISM #formal_name phage phi-80 #note host Escherichia coli DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 30-Jun-1993 ACCESSIONS S01777 REFERENCE S01776 !$#authors Ogawa, T.; Ogawa, H.; Tomizawa, J.I. !$#journal J. Mol. Biol. (1988) 202:537-550 !$#title Organization of the early region of bacteriophage phi-80. !1Genes and proteins. !$#cross-references MUID:89011978; PMID:3172225 !$#accession S01777 !'##molecule_type DNA !'##residues 1-229 ##label OGA !'##cross-references EMBL:X13065 !'##note the authors translated the codon GCC for residue 88 as Gly and !1GGC for residue 89 as Ala GENETICS !$#gene 14 CLASSIFICATION #superfamily phage lambda replication protein P SUMMARY #length 229 #molecular-weight 26492 #checksum 5818 SEQUENCE /// ENTRY S41182 #type complete TITLE phage-related replication protein - phage SPP1 ORGANISM #formal_name phage SPP1 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS S43808; S41182 REFERENCE S43798 !$#authors Pedre, X.; Weise, F.; Chai, S.; Lueder, G.; Alonso, J.C. !$#journal J. Mol. Biol. (1994) 236:1324-1340 !$#title Analysis of cis and trans acting elements required for the !1initiation of DNA replication in the Bacillus subtilis !1bacteriophage SPP1. !$#cross-references MUID:94172631; PMID:8126723 !$#accession S43808 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-197 ##label PE2 !'##cross-references EMBL:X67865; NID:g472886; PIDN:CAA48058.1; !1PID:g439639 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1992 CLASSIFICATION #superfamily phage-related replication protein SUMMARY #length 197 #molecular-weight 22336 #checksum 8728 SEQUENCE /// ENTRY C69890 #type complete TITLE phage-related replication protein homolog yndL - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69890 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69890 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-252 ##label KUN !'##cross-references GB:Z99113; GB:AL009126; NID:g2634090; !1PIDN:CAB13666.1; PID:g2634166 !'##experimental_source strain 168 GENETICS !$#gene yndL CLASSIFICATION #superfamily phage-related replication protein SUMMARY #length 252 #molecular-weight 28218 #checksum 7844 SEQUENCE /// ENTRY E69883 #type complete TITLE phage-related replication protein homolog ymaC - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69883 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69883 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-235 ##label KUN !'##cross-references GB:Z99113; GB:AL009126; NID:g2634090; !1PIDN:CAB13611.1; PID:g2634111 !'##experimental_source strain 168 GENETICS !$#gene ymaC CLASSIFICATION #superfamily phage-related replication protein SUMMARY #length 235 #molecular-weight 26871 #checksum 8700 SEQUENCE /// ENTRY B69854 #type complete TITLE phage-related replication protein homolog yjqB - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69854 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69854 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-200 ##label KUN !'##cross-references GB:Z99110; GB:AL009126; NID:g2633472; !1PIDN:CAB13105.1; PID:g2633602 !'##experimental_source strain 168 GENETICS !$#gene yjqB CLASSIFICATION #superfamily phage-related replication protein SUMMARY #length 200 #molecular-weight 22851 #checksum 9072 SEQUENCE /// ENTRY RPBPP4 #type complete TITLE DNA primase - satellite phage P4 ALTERNATE_NAMES gp alpha ORGANISM #formal_name satellite phage P4 #note host Escherichia coli DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 23-Jul-1999 ACCESSIONS A26869; JW0024 REFERENCE A92939 !$#authors Flensburg, J.; Calendar, R. !$#journal J. Mol. Biol. (1987) 195:439-445 !$#title Bacteriophage P4 DNA replication. Nucleotide sequence of the !1P4 replication gene and the cis replication region. !$#cross-references MUID:88011258; PMID:3309336 !$#accession A26869 !'##molecule_type DNA !'##residues 1-777 ##label FLE !'##cross-references EMBL:X05623; NID:g15150; PIDN:CAA29111.1; !1PID:g15152 REFERENCE JW0020 !$#authors Halling, C.; Calendar, R.; Christie, G.E.; Dale, E.C.; Deho, !1G.; Finkel, S.; Flensburg, J.; Ghisotti, D.; Kahn, M.L.; !1Lane, K.B.; Lin, C.S.; Lindqvist, B.H.; Pierson III, L.S.; !1Six, E.W.; Sunshine, M.G.; Ziermann, R. !$#journal Nucleic Acids Res. (1990) 18:1649 !$#title DNA sequence of satellite bacteriophage P4. !$#cross-references MUID:90221913; PMID:2183201 !$#accession JW0024 !'##molecule_type DNA !'##residues 1-777 ##label HAL !'##cross-references EMBL:X51522; NID:g450916; PIDN:CAA35898.1; !1PID:g15158 GENETICS !$#gene alpha CLASSIFICATION #superfamily phage P4 DNA primase KEYWORDS DNA binding; DNA replication SUMMARY #length 777 #molecular-weight 84919 #checksum 6882 SEQUENCE /// ENTRY QQBPP4 #type complete TITLE orf-106 protein - satellite phage P4 ALTERNATE_NAMES hypothetical 11.8K protein; orf106 protein ORGANISM #formal_name satellite phage P4 #note host Escherichia coli DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 23-Jul-1999 ACCESSIONS A92939; A93544; JW0025; B26869; F23878 REFERENCE A92939 !$#authors Flensburg, J.; Calendar, R. !$#journal J. Mol. Biol. (1987) 195:439-445 !$#title Bacteriophage P4 DNA replication. Nucleotide sequence of the !1P4 replication gene and the cis replication region. !$#cross-references MUID:88011258; PMID:3309336 !$#accession A92939 !'##molecule_type DNA !'##residues 1-106 ##label FLE !'##cross-references EMBL:X05623; NID:g15150; PIDN:CAA29110.1; !1PID:g15151 REFERENCE A93544 !$#authors Lin, C.S. !$#journal Nucleic Acids Res. (1984) 12:8667-8684 !$#title Nucleotide sequence of the essential region of bacteriophage !1P4. !$#cross-references MUID:85062840; PMID:6095206 !$#accession A93544 !'##molecule_type DNA !'##residues 1-18 ##label LIN !'##cross-references EMBL:X02534; NID:g15167; PIDN:CAA26381.1; !1PID:g579157 REFERENCE JW0020 !$#authors Halling, C.; Calendar, R.; Christie, G.E.; Dale, E.C.; Deho, !1G.; Finkel, S.; Flensburg, J.; Ghisotti, D.; Kahn, M.L.; !1Lane, K.B.; Lin, C.S.; Lindqvist, B.H.; Pierson III, L.S.; !1Six, E.W.; Sunshine, M.G.; Ziermann, R. !$#journal Nucleic Acids Res. (1990) 18:1649 !$#title DNA sequence of satellite bacteriophage P4. !$#cross-references MUID:90221913; PMID:2183201 !$#accession JW0025 !'##molecule_type DNA !'##residues 1-106 ##label HAL !'##cross-references GB:X51522; NID:g450916; PIDN:CAA35899.1; PID:g15159 CLASSIFICATION #superfamily phage P4 orf-106 protein SUMMARY #length 106 #molecular-weight 11802 #checksum 5343 SEQUENCE /// ENTRY GSBPP4 #type complete TITLE head size determination protein sid - satellite phage P4 ALTERNATE_NAMES capsid size-determining protein ORGANISM #formal_name satellite phage P4 DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 23-Jul-1999 ACCESSIONS C23878; JW0030; S57826 REFERENCE A93544 !$#authors Lin, C.S. !$#journal Nucleic Acids Res. (1984) 12:8667-8684 !$#title Nucleotide sequence of the essential region of bacteriophage !1P4. !$#cross-references MUID:85062840; PMID:6095206 !$#accession C23878 !'##molecule_type DNA !'##residues 1-244 ##label LIN !'##cross-references EMBL:X02534; GB:M11913; GB:M11914; NID:g15167; !1PIDN:CAA26376.1; PID:g15170 REFERENCE JW0020 !$#authors Halling, C.; Calendar, R.; Christie, G.E.; Dale, E.C.; Deho, !1G.; Finkel, S.; Flensburg, J.; Ghisotti, D.; Kahn, M.L.; !1Lane, K.B.; Lin, C.S.; Lindqvist, B.H.; Pierson III, L.S.; !1Six, E.W.; Sunshine, M.G.; Ziermann, R. !$#journal Nucleic Acids Res. (1990) 18:1649 !$#title DNA sequence of satellite bacteriophage P4. !$#cross-references MUID:90221913; PMID:2183201 !$#accession JW0030 !'##molecule_type DNA !'##residues 1-197,'V',199-244 ##label HAL !'##cross-references GB:X51522; NID:g450916; PIDN:CAA35904.1; PID:g15164 REFERENCE S57826 !$#authors Marvik, O.J.; Dokland, T.; Nokling, R.H.; Jacobsen, E.; !1Larsen, T.; Lindqvist, B.H. !$#journal J. Mol. Biol. (1995) 251:59-75 !$#title The capsid size-determining protein sid forms an external !1scaffold on phage P4 procapsids. !$#cross-references MUID:95371113; PMID:7643390 !$#contents annotation GENETICS !$#gene sid FUNCTION !$#description auxiliary protein for capsid assembly; forms a transient !1external scaffold with icosahedral symmetry on procapsids !$#note absent from mature virus particels CLASSIFICATION #superfamily head size determination protein sid KEYWORDS capsid assembly SUMMARY #length 244 #molecular-weight 27345 #checksum 8157 SEQUENCE /// ENTRY GABPP4 #type complete TITLE ash protein - satellite phage P4 ALTERNATE_NAMES cI protein ORGANISM #formal_name satellite phage P4 #note host Escherichia coli DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 23-Jul-1999 ACCESSIONS D23878; JW0028 REFERENCE A93544 !$#authors Lin, C.S. !$#journal Nucleic Acids Res. (1984) 12:8667-8684 !$#title Nucleotide sequence of the essential region of bacteriophage !1P4. !$#cross-references MUID:85062840; PMID:6095206 !$#accession D23878 !'##molecule_type DNA !'##residues 1-137 ##label LIN !'##cross-references GB:X02534; NID:g15167; PIDN:CAA26378.1; PID:g15172 REFERENCE JW0020 !$#authors Halling, C.; Calendar, R.; Christie, G.E.; Dale, E.C.; Deho, !1G.; Finkel, S.; Flensburg, J.; Ghisotti, D.; Kahn, M.L.; !1Lane, K.B.; Lin, C.S.; Lindqvist, B.H.; Pierson III, L.S.; !1Six, E.W.; Sunshine, M.G.; Ziermann, R. !$#journal Nucleic Acids Res. (1990) 18:1649 !$#title DNA sequence of satellite bacteriophage P4. !$#cross-references MUID:90221913; PMID:2183201 !$#accession JW0028 !'##molecule_type DNA !'##residues 1-137 ##label HAL !'##cross-references GB:X51522; NID:g450916; PIDN:CAA35902.1; !1PID:g1262833 GENETICS !$#gene ash; cI CLASSIFICATION #superfamily phage P4 ash protein SUMMARY #length 137 #molecular-weight 14850 #checksum 1034 SEQUENCE /// ENTRY PUBPP4 #type complete TITLE amber mutation-suppressing protein - satellite phage P4 ORGANISM #formal_name satellite phage P4 DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 17-Nov-2000 ACCESSIONS S06887; JW0032; A23878 REFERENCE S06887 !$#authors Dale, E.C.; Christie, G.E.; Calendar, R. !$#journal J. Mol. Biol. (1986) 192:793-803 !$#title Organization and expression of the satellite bacteriophage !1P4 late gene cluster. !$#cross-references MUID:87226170; PMID:3295254 !$#accession S06887 !'##molecule_type DNA !'##residues 1-190 ##label DAL !'##cross-references GB:X16283; GB:M29650; NID:g15453; PIDN:CAA34359.1; !1PID:g15454 !'##note the authors translated the codon GCA for residue 18 as Thr and !1AAT for residue 141 as Asp REFERENCE JW0020 !$#authors Halling, C.; Calendar, R.; Christie, G.E.; Dale, E.C.; Deho, !1G.; Finkel, S.; Flensburg, J.; Ghisotti, D.; Kahn, M.L.; !1Lane, K.B.; Lin, C.S.; Lindqvist, B.H.; Pierson III, L.S.; !1Six, E.W.; Sunshine, M.G.; Ziermann, R. !$#journal Nucleic Acids Res. (1990) 18:1649 !$#title DNA sequence of satellite bacteriophage P4. !$#cross-references MUID:90221913; PMID:2183201 !$#accession JW0032 !'##molecule_type DNA !'##residues 1-190 ##label HAL !'##cross-references GB:X51522; NID:g450916 REFERENCE A93544 !$#authors Lin, C.S. !$#journal Nucleic Acids Res. (1984) 12:8667-8684 !$#title Nucleotide sequence of the essential region of bacteriophage !1P4. !$#cross-references MUID:85062840; PMID:6095206 !$#accession A23878 !'##molecule_type DNA !'##residues 1-17,'T',19-61 ##label LIN !'##cross-references GB:X02534; NID:g15167; PIDN:CAA26374.1; PID:g15168 GENETICS !$#gene psu CLASSIFICATION #superfamily phage P4 amber mutation-suppressing protein KEYWORDS late protein SUMMARY #length 190 #molecular-weight 21306 #checksum 9561 SEQUENCE /// ENTRY DEBPP4 #type complete TITLE derepression protein - satellite phage P4 ORGANISM #formal_name satellite phage P4 DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 31-Oct-1997 ACCESSIONS E23878 REFERENCE A93544 !$#authors Lin, C.S. !$#journal Nucleic Acids Res. (1984) 12:8667-8684 !$#title Nucleotide sequence of the essential region of bacteriophage !1P4. !$#cross-references MUID:85062840; PMID:6095206 !$#accession E23878 !'##molecule_type DNA !'##residues 1-95 ##label LIN !'##cross-references GB:X02534 GENETICS !$#gene epsilon CLASSIFICATION #superfamily satellite phage P4 derepression protein SUMMARY #length 95 #molecular-weight 10932 #checksum 1161 SEQUENCE /// ENTRY GPBPP4 #type complete TITLE gop protein - satellite phage P4 ORGANISM #formal_name satellite phage P4 #note host Escherichia coli DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 23-Jul-1999 ACCESSIONS A33556; JW0020 REFERENCE A33556 !$#authors Ghisotti, D.; Finkel, S.; Halling, C.; Deho, G.; Sironi, G.; !1Calendar, R. !$#journal J. Virol. (1990) 64:24-36 !$#title Nonessential region of bacteriophage P4: DNA sequence, !1transcription, gene products, and functions. !$#cross-references MUID:90080127; PMID:2403440 !$#accession A33556 !'##molecule_type DNA !'##residues 1-133 ##label GHI !'##cross-references GB:M27748; NID:g215691; PIDN:AAA32427.1; !1PID:g215692 REFERENCE JW0020 !$#authors Halling, C.; Calendar, R.; Christie, G.E.; Dale, E.C.; Deho, !1G.; Finkel, S.; Flensburg, J.; Ghisotti, D.; Kahn, M.L.; !1Lane, K.B.; Lin, C.S.; Lindqvist, B.H.; Pierson III, L.S.; !1Six, E.W.; Sunshine, M.G.; Ziermann, R. !$#journal Nucleic Acids Res. (1990) 18:1649 !$#title DNA sequence of satellite bacteriophage P4. !$#cross-references MUID:90221913; PMID:2183201 !$#accession JW0020 !'##molecule_type DNA !'##residues 1-133 ##label HAL !'##cross-references GB:X51522; NID:g450916; PIDN:CAA35894.1; PID:g15154 GENETICS !$#gene gop CLASSIFICATION #superfamily satellite phage P4 gop protein SUMMARY #length 133 #molecular-weight 14891 #checksum 5928 SEQUENCE /// ENTRY GBBPP4 #type complete TITLE beta protein - satellite phage P4 ORGANISM #formal_name satellite phage P4 #note host Escherichia coli DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 23-Jul-1999 ACCESSIONS JW0021; B33556 REFERENCE JW0020 !$#authors Halling, C.; Calendar, R.; Christie, G.E.; Dale, E.C.; Deho, !1G.; Finkel, S.; Flensburg, J.; Ghisotti, D.; Kahn, M.L.; !1Lane, K.B.; Lin, C.S.; Lindqvist, B.H.; Pierson III, L.S.; !1Six, E.W.; Sunshine, M.G.; Ziermann, R. !$#journal Nucleic Acids Res. (1990) 18:1649 !$#title DNA sequence of satellite bacteriophage P4. !$#cross-references MUID:90221913; PMID:2183201 !$#accession JW0021 !'##molecule_type DNA !'##residues 1-355 ##label HAL !'##cross-references GB:X51522; NID:g450916; PIDN:CAA35895.1; PID:g15155 REFERENCE A33556 !$#authors Ghisotti, D.; Finkel, S.; Halling, C.; Deho, G.; Sironi, G.; !1Calendar, R. !$#journal J. Virol. (1990) 64:24-36 !$#title Nonessential region of bacteriophage P4: DNA sequence, !1transcription, gene products, and functions. !$#cross-references MUID:90080127; PMID:2403440 !$#accession B33556 !'##molecule_type DNA !'##residues 1-355 ##label GHI !'##cross-references GB:M27748; NID:g215691; PIDN:AAA32428.1; !1PID:g215693 GENETICS !$#gene beta CLASSIFICATION #superfamily satellite phage P4 beta protein SUMMARY #length 355 #molecular-weight 39909 #checksum 1620 SEQUENCE /// ENTRY GCBPP4 #type complete TITLE cII protein - satellite phage P4 ORGANISM #formal_name satellite phage P4 #note host Escherichia coli DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 30-Jun-1993 ACCESSIONS C33556 REFERENCE A33556 !$#authors Ghisotti, D.; Finkel, S.; Halling, C.; Deho, G.; Sironi, G.; !1Calendar, R. !$#journal J. Virol. (1990) 64:24-36 !$#title Nonessential region of bacteriophage P4: DNA sequence, !1transcription, gene products, and functions. !$#cross-references MUID:90080127; PMID:2403440 !$#accession C33556 !'##molecule_type DNA !'##residues 1-264 ##label GHI GENETICS !$#gene cII CLASSIFICATION #superfamily satellite phage P4 cII protein SUMMARY #length 264 #molecular-weight 30185 #checksum 5056 SEQUENCE /// ENTRY Q1BPP4 #type complete TITLE hypothetical protein ORF1 - satellite phage P4 ORGANISM #formal_name satellite phage P4 DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 10-Sep-1999 ACCESSIONS G23878 REFERENCE A93544 !$#authors Lin, C.S. !$#journal Nucleic Acids Res. (1984) 12:8667-8684 !$#title Nucleotide sequence of the essential region of bacteriophage !1P4. !$#cross-references MUID:85062840; PMID:6095206 !$#accession G23878 !'##molecule_type DNA !'##residues 1-109 ##label LIN !'##cross-references GB:X02534 CLASSIFICATION #superfamily Escherichia coli prophage cp4-57 regulatory !1protein alpA SUMMARY #length 109 #molecular-weight 12118 #checksum 961 SEQUENCE /// ENTRY Q2BPP4 #type complete TITLE hypothetical protein ORF2 - satellite phage P4 ALTERNATE_NAMES hypothetical 17.7K protein; ORF151 protein ORGANISM #formal_name satellite phage P4 #note host Escherichia coli DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 10-Sep-1999 ACCESSIONS H23878; JW0026 REFERENCE A93544 !$#authors Lin, C.S. !$#journal Nucleic Acids Res. (1984) 12:8667-8684 !$#title Nucleotide sequence of the essential region of bacteriophage !1P4. !$#cross-references MUID:85062840; PMID:6095206 !$#accession H23878 !'##molecule_type DNA !'##residues 1-151 ##label LIN !'##cross-references GB:X02534; NID:g15167; PIDN:CAA26380.1; PID:g15174 REFERENCE JW0020 !$#authors Halling, C.; Calendar, R.; Christie, G.E.; Dale, E.C.; Deho, !1G.; Finkel, S.; Flensburg, J.; Ghisotti, D.; Kahn, M.L.; !1Lane, K.B.; Lin, C.S.; Lindqvist, B.H.; Pierson III, L.S.; !1Six, E.W.; Sunshine, M.G.; Ziermann, R. !$#journal Nucleic Acids Res. (1990) 18:1649 !$#title DNA sequence of satellite bacteriophage P4. !$#cross-references MUID:90221913; PMID:2183201 !$#accession JW0026 !'##molecule_type DNA !'##residues 1-151 ##label HAL !'##cross-references GB:X51522; NID:g450916; PIDN:CAA35900.1; PID:g15160 CLASSIFICATION #superfamily satellite phage P4 hypothetical 17.7K protein SUMMARY #length 151 #molecular-weight 17726 #checksum 9539 SEQUENCE /// ENTRY NDBPT4 #type complete TITLE ndd protein - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 30-Jun-1993 ACCESSIONS S01868 REFERENCE S01711 !$#authors Chapman, D.; Morad, I.; Kaufmann, G.; Gait, M.J.; Jorissen, !1L.; Snyder, L. !$#journal J. Mol. Biol. (1988) 199:373-377 !$#title Nucleotide and deduced amino acid sequence of stp: the !1bacteriophage T4 anticodon nuclease gene. !$#cross-references MUID:88172481; PMID:3280805 !$#accession S01868 !'##molecule_type DNA !'##residues 1-97 ##label CHA GENETICS !$#gene ndd !$#map_position 162-164 CLASSIFICATION #superfamily phage T4 ndd protein SUMMARY #length 97 #molecular-weight 11159 #checksum 2212 SEQUENCE /// ENTRY ZMBPT4 #type complete TITLE late transcription regulation protein - phage T4 ALTERNATE_NAMES gp mrh ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 01-Dec-1995 ACCESSIONS JH0136 REFERENCE JH0136 !$#authors Frazier, M.W.; Mosig, G. !$#journal Gene (1990) 88:7-14 !$#title The bacteriophage T4 gene mrh whose product inhibits late T4 !1gene expression in an Escherichia coli rpoH (sigma(32)) !1mutant. !$#cross-references MUID:90255970; PMID:1692800 !$#accession JH0136 !'##molecule_type DNA !'##residues 1-116 ##label FRA !'##cross-references EMBL:M30001 COMMENT This protein contains an ATPase motif. COMMENT This protein is responsible for the inhibition of the late !1transcription in the rpoH mutant host. GENETICS !$#gene mrh !$#map_position 14.199-14.681 CLASSIFICATION #superfamily phage T4 mrh protein KEYWORDS transcription regulation SUMMARY #length 116 #molecular-weight 13434 #checksum 4321 SEQUENCE /// ENTRY ZKBPT4 #type complete TITLE transcription regulator motA - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 23-Jul-1999 ACCESSIONS JV0101 REFERENCE JV0101 !$#authors Uzan, M.; Brody, E.; Favre, R. !$#journal Mol. Microbiol. (1990) 4:1487-1496 !$#title Nucleotide sequence and control of transcription of the !1bacteriophage T4 motA regulatory gene. !$#cross-references MUID:91141300; PMID:2287273 !$#accession JV0101 !'##molecule_type DNA !'##residues 1-211 ##label UZA !'##cross-references GB:Z48569; NID:g695449; PIDN:CAA88453.1; !1PID:g695450 GENETICS !$#gene motA !$#map_position 160 CLASSIFICATION #superfamily phage T4 transcription regulator motA KEYWORDS DNA binding; transcription SUMMARY #length 211 #molecular-weight 23574 #checksum 5601 SEQUENCE /// ENTRY STBPT4 #type complete TITLE stp protein - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 30-Sep-1990 #sequence_revision 18-Jul-1997 #text_change 23-Jul-1999 ACCESSIONS S55796; S01869; S49926 REFERENCE S55796 !$#authors Penner, M.; Morad, I.; Snyder, L.; Kaufmann, G. !$#journal J. Mol. Biol. (1995) 249:857-868 !$#title Phage T4-coded Stp: double-edged effector of coupled DNA and !1tRNA-restriction systems. !$#cross-references MUID:95311310; PMID:7791212 !$#accession S55796 !'##molecule_type DNA !'##residues 1-26 ##label PEN !'##cross-references EMBL:Z46874; NID:g599667; PIDN:CAA86954.1; !1PID:g599668 !'##note this is a revision to the sequence from reference S01711 REFERENCE S01711 !$#authors Chapman, D.; Morad, I.; Kaufmann, G.; Gait, M.J.; Jorissen, !1L.; Snyder, L. !$#journal J. Mol. Biol. (1988) 199:373-377 !$#title Nucleotide and deduced amino acid sequence of stp: the !1bacteriophage T4 anticodon nuclease gene. !$#cross-references MUID:88172481; PMID:3280805 !$#accession S01869 !'##molecule_type DNA !'##residues 1-20,'RLRTPVRKI' ##label CHA !'##note this sequence has been revised in reference S55796 GENETICS !$#gene stp !$#map_position 162-164 CLASSIFICATION #superfamily phage T4 stp protein SUMMARY #length 26 #molecular-weight 3184 #checksum 7233 SEQUENCE /// ENTRY ACBPT4 #type complete TITLE gene ac protein - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 30-Jun-1993 ACCESSIONS S01871 REFERENCE S01711 !$#authors Chapman, D.; Morad, I.; Kaufmann, G.; Gait, M.J.; Jorissen, !1L.; Snyder, L. !$#journal J. Mol. Biol. (1988) 199:373-377 !$#title Nucleotide and deduced amino acid sequence of stp: the !1bacteriophage T4 anticodon nuclease gene. !$#cross-references MUID:88172481; PMID:3280805 !$#accession S01871 !'##molecule_type DNA !'##residues 1-46 ##label CHA GENETICS !$#gene ac !$#map_position 162-164 CLASSIFICATION #superfamily phage T4 ac protein SUMMARY #length 46 #molecular-weight 5098 #checksum 3484 SEQUENCE /// ENTRY Z8BPT4 #type complete TITLE DNA-priming protein - phage T4 ALTERNATE_NAMES gp 61 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 11-May-2000 ACCESSIONS A94456; A04296; A90996 REFERENCE A94456 !$#authors Nakanishi, M.; Alberts, B. !$#citation unpublished results 1985, cited by GenBank !$#accession A94456 !'##molecule_type DNA !'##residues 1-211 ##label NAK !'##cross-references GB:K03113; NID:g215964 REFERENCE A45681 !$#authors Selick, H.E.; Stormo, G.D.; Dyson, R.L.; Alberts, B.M. !$#journal J. Virol. (1993) 67:2305-2316 !$#title Analysis of five presumptive protein-coding sequences !1clustered between the primosome genes, 41 and 61, of !1bacteriophages T4, T2, and T6. !$#cross-references MUID:93188183; PMID:8383243 !$#accession A04296 !'##molecule_type DNA !'##residues 1-211 ##label SEL !'##cross-references GB:S57514; NID:g298518 REFERENCE A90996 !$#authors Macdonald, P.M.; Mosig, G. !$#journal EMBO J. (1984) 3:2863-2871 !$#title Regulation of a new bacteriophage T4 gene, 69, that spans an !1origin of DNA replication. !$#cross-references MUID:85126881; PMID:6098451 !$#accession A90996 !'##molecule_type DNA !'##residues 212-342 ##label MAC !'##cross-references GB:X01416; NID:g15329; PIDN:CAA25659.1; PID:g836603 GENETICS !$#gene 61; 58 !$#map_position 17.942-18.968 CLASSIFICATION #superfamily phage T4 DNA priming protein KEYWORDS early protein SUMMARY #length 342 #molecular-weight 39778 #checksum 8618 SEQUENCE /// ENTRY NCBPX4 #type complete TITLE exonuclease 47 (EC 3.1.11.-) chain 1 - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 23-Jul-1999 ACCESSIONS A04297; T10159 REFERENCE A91016 !$#authors Gram, H.; Ruger, W. !$#journal EMBO J. (1985) 4:257-264 !$#title Genes 55, alpha-gt, 47 and 46 of bacteriophage T4: the !1genomic organization as deduced by sequence analysis. !$#cross-references MUID:85257446; PMID:4018026 !$#accession A04297 !'##molecule_type DNA !'##residues 1-339 ##label GRA !'##cross-references GB:X01804; NID:g15229; PIDN:CAA25942.1; PID:g15238 GENETICS !$#gene 47 CLASSIFICATION #superfamily phage T4 exonuclease 47; phosphoesterase core !1homology KEYWORDS exonuclease; hydrolase FEATURE !$2-86 #domain phosphoesterase core homology #label PEC SUMMARY #length 339 #molecular-weight 39166 #checksum 5995 SEQUENCE /// ENTRY NCBPX6 #type complete TITLE exonuclease 46 (EC 3.1.11.-) chain 2 - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 17-Mar-1987 #sequence_revision 21-Nov-1997 #text_change 19-Jan-2001 ACCESSIONS A04298; T10162 REFERENCE A91016 !$#authors Gram, H.; Ruger, W. !$#journal EMBO J. (1985) 4:257-264 !$#title Genes 55, alpha-gt, 47 and 46 of bacteriophage T4: the !1genomic organization as deduced by sequence analysis. !$#cross-references MUID:85257446; PMID:4018026 !$#accession A04298 !'##molecule_type DNA !'##residues 1-560 ##label GRA !'##cross-references GB:X01804; NID:g15229; PIDN:CAA25945.1; PID:g577852 !'##note the authors translated the initiation codon GUG for residue 1 !1as Val GENETICS !$#gene 46 !$#start_codon GUG CLASSIFICATION #superfamily phage T4 exonuclease 46 KEYWORDS exonuclease; hydrolase; nucleotide binding; P-loop FEATURE !$36-43 #region nucleotide-binding motif A (P-loop) SUMMARY #length 560 #molecular-weight 63613 #checksum 6279 SEQUENCE /// ENTRY Z9BPT4 #type complete TITLE DNA replication protein - phage T4 ALTERNATE_NAMES gp56; gp69 CONTAINS small gene 69 protein, gp69* ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 24-Sep-1999 ACCESSIONS A04299; JS0574 REFERENCE A90996 !$#authors Macdonald, P.M.; Mosig, G. !$#journal EMBO J. (1984) 3:2863-2871 !$#title Regulation of a new bacteriophage T4 gene, 69, that spans an !1origin of DNA replication. !$#cross-references MUID:85126881; PMID:6098451 !$#accession A04299 !'##molecule_type DNA !'##residues 1-392 ##label MAC !'##cross-references GB:X01416; NID:g15329; PIDN:CAA25661.1; PID:g15331 !$#accession JS0574 !'##molecule_type DNA !'##residues 1-174 ##label MA2 GENETICS !$#gene 69; 56 !$#map_position 15.613-16.285; 16.277-16.790 FUNCTION !$#description the gene 69 produces two proteins, gp69 and gp69* (the !1carboxyl-terminal part of gp 69) which are regulated by two !1different promotors; the proteins span an origin of !1replication; defective DNA replication in an amber mutant !1shows that at least the larger protein is required for T4 !1DNA replication CLASSIFICATION #superfamily phage T4 DNA replication protein KEYWORDS DNA replication FEATURE !$169-392 #product small gene 69 protein #status predicted !8#label S69 SUMMARY #length 392 #molecular-weight 46239 #checksum 4371 SEQUENCE /// ENTRY Z1BPT9 #type complete TITLE gene 49.3 protein - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 23-Jul-1999 ACCESSIONS A29284 REFERENCE A30291 !$#authors Tomaschewski, J.; Rueger, W. !$#journal Nucleic Acids Res. (1987) 15:3632-3633 !$#title Nucleotide sequence and primary structures of gene products !1coded for by the T4 genome between map positions 48.266 kb !1and 39.166 kb. !$#cross-references MUID:87203398; PMID:3575111 !$#accession A29284 !'##molecule_type DNA !'##residues 1-102 ##label TOM !'##cross-references GB:Y00122; NID:g15346; PIDN:CAA68304.1; PID:g15347 GENETICS !$#gene 49.3 CLASSIFICATION #superfamily phage T4 gene 49.3 protein SUMMARY #length 102 #molecular-weight 11938 #checksum 5445 SEQUENCE /// ENTRY Z2BPT9 #type complete TITLE gene 49.2 protein - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 23-Jul-1999 ACCESSIONS B29284 REFERENCE A30291 !$#authors Tomaschewski, J.; Rueger, W. !$#journal Nucleic Acids Res. (1987) 15:3632-3633 !$#title Nucleotide sequence and primary structures of gene products !1coded for by the T4 genome between map positions 48.266 kb !1and 39.166 kb. !$#cross-references MUID:87203398; PMID:3575111 !$#accession B29284 !'##molecule_type DNA !'##residues 1-106 ##label TOM !'##cross-references GB:Y00122; NID:g15346; PIDN:CAA68305.1; PID:g15348 GENETICS !$#gene 49.2 CLASSIFICATION #superfamily phage T4 gene 49.2 protein SUMMARY #length 106 #molecular-weight 12579 #checksum 3359 SEQUENCE /// ENTRY Z3BPT9 #type complete TITLE gene 49.1 protein - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 23-Jul-1999 ACCESSIONS I30292 REFERENCE A30291 !$#authors Tomaschewski, J.; Rueger, W. !$#journal Nucleic Acids Res. (1987) 15:3632-3633 !$#title Nucleotide sequence and primary structures of gene products !1coded for by the T4 genome between map positions 48.266 kb !1and 39.166 kb. !$#cross-references MUID:87203398; PMID:3575111 !$#accession I30292 !'##molecule_type DNA !'##residues 1-161 ##label TOM !'##cross-references GB:Y00122; NID:g15346; PIDN:CAA68306.1; PID:g15349 GENETICS !$#gene 49.1 CLASSIFICATION #superfamily phage T4 gene 49.1 protein SUMMARY #length 161 #molecular-weight 18816 #checksum 5976 SEQUENCE /// ENTRY ZNBPT9 #type complete TITLE recombination endonuclease VII (EC 3.1.-.-) - phage T4 ALTERNATE_NAMES gene 49 protein (gp49) ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 16-Jun-2000 ACCESSIONS S01906; A30291; S13861 REFERENCE S01906 !$#authors Barth, K.A.; Powell, D.; Trupin, M.; Mosig, G. !$#journal Genetics (1988) 120:329-343 !$#title Regulation of two nested proteins from gene 49 !1(recombination endonuclease VII) and of a lambda RexA-like !1protein of bacteriophage T4. !$#cross-references MUID:89065345; PMID:2974005 !$#accession S01906 !'##molecule_type DNA !'##residues 1-157 ##label BAR !'##cross-references GB:X12629; NID:g15314; PIDN:CAA31148.1; PID:g15315 REFERENCE A30291 !$#authors Tomaschewski, J.; Rueger, W. !$#journal Nucleic Acids Res. (1987) 15:3632-3633 !$#title Nucleotide sequence and primary structures of gene products !1coded for by the T4 genome between map positions 48.266 kb !1and 39.166 kb. !$#cross-references MUID:87203398; PMID:3575111 !$#accession A30291 !'##molecule_type DNA !'##residues 1-157 ##label TOM !'##cross-references GB:Y00122; NID:g15346; PIDN:CAA68307.1; !1PID:g1177560 REFERENCE S13861 !$#authors Kosak, H.G.; Kemper, B.W. !$#journal Eur. J. Biochem. (1990) 194:779-784 !$#title Large-scale preparation of T4 endonuclease VII from !1over-expressing bacteria. !$#cross-references MUID:91099358; PMID:2269300 !$#accession S13861 !'##status preliminary !'##molecule_type DNA !'##residues 1-15 ##label KOS GENETICS !$#gene 49 CLASSIFICATION #superfamily phage T4 gene 49 protein KEYWORDS endonuclease; hydrolase SUMMARY #length 157 #molecular-weight 18144 #checksum 2977 SEQUENCE /// ENTRY GPBP84 #type complete TITLE baseplate protein gp53 - phage T4 ALTERNATE_NAMES gene 50.1 protein; gene 53 protein ORGANISM #formal_name phage T4 DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 23-Jul-1999 ACCESSIONS S25239; S04608; JF0062; S10107 REFERENCE S25239 !$#authors Mosig, G.; Lin, G.W.; Franklin, J.; Fan, W.H. !$#journal New Biol. (1989) 1:171-179 !$#title Functional relationships and structural determinants of two !1bacteriophage T4 lysozymes: a soluble (gene e) and a !1baseplate-associated (gene 5) protein. !$#cross-references MUID:91190815; PMID:2488704 !$#accession S25239 !'##molecule_type DNA !'##residues 1-196 ##label MOS !'##cross-references GB:X15728; NID:g15224; PIDN:CAA33748.1; PID:g15226 REFERENCE S04608 !$#authors Koch, T.; Lamm, N.; Rueger, W. !$#journal Nucleic Acids Res. (1989) 17:4392 !$#title Sequencing, cloning and overexpression of genes of !1bacteriophage T4 between map positions 74.325 and 77.184. !$#cross-references MUID:89296504; PMID:2740234 !$#accession S04608 !'##status translation not shown !'##molecule_type DNA !'##residues 1-196 ##label KOC !'##cross-references EMBL:X14845; NID:g15218; PIDN:CAA32949.1; !1PID:g15219 GENETICS !$#gene 53; 50.1 !$#map_position 76.4-77.0 CLASSIFICATION #superfamily phage T4 gene 53 protein KEYWORDS baseplate; late protein SUMMARY #length 196 #molecular-weight 22966 #checksum 6922 SEQUENCE /// ENTRY Z4BPT9 #type complete TITLE ribonucleoside-triphosphate reductase (EC 1.17.4.2) anaerobic - phage T4 ALTERNATE_NAMES gene 55.13 protein; ribonucleoside-triphosphate reductase, class III; ribonucleoside-triphosphate reductase, oxygen-sensitive ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 24-Sep-1999 ACCESSIONS S01907; C29284 REFERENCE S01906 !$#authors Barth, K.A.; Powell, D.; Trupin, M.; Mosig, G. !$#journal Genetics (1988) 120:329-343 !$#title Regulation of two nested proteins from gene 49 !1(recombination endonuclease VII) and of a lambda RexA-like !1protein of bacteriophage T4. !$#cross-references MUID:89065345; PMID:2974005 !$#accession S01907 !'##molecule_type DNA !'##residues 1-181 ##label BAR !'##cross-references GB:X12629; NID:g15314; PIDN:CAA31150.1; PID:g15317 REFERENCE A30291 !$#authors Tomaschewski, J.; Rueger, W. !$#journal Nucleic Acids Res. (1987) 15:3632-3633 !$#title Nucleotide sequence and primary structures of gene products !1coded for by the T4 genome between map positions 48.266 kb !1and 39.166 kb. !$#cross-references MUID:87203398; PMID:3575111 !$#accession C29284 !'##molecule_type DNA !'##residues 1-181 ##label TOM !'##cross-references GB:Y00122; NID:g15346; PIDN:CAA68308.1; PID:g15350 GENETICS !$#gene 55.13 CLASSIFICATION #superfamily phage T4 anaerobic ribonucleoside-triphosphate !1reductase; oxygen-sensitive ribonucleoside-triphosphate !1reductase middle homology KEYWORDS oxidoreductase FEATURE !$1-181 #domain oxygen-sensitive ribonucleoside-triphosphate !8reductase middle homology #label ARRM SUMMARY #length 181 #molecular-weight 20144 #checksum 8462 SEQUENCE /// ENTRY Z5BPT9 #type complete TITLE gene 55.12 protein - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 23-Jul-1999 ACCESSIONS D29284 REFERENCE A30291 !$#authors Tomaschewski, J.; Rueger, W. !$#journal Nucleic Acids Res. (1987) 15:3632-3633 !$#title Nucleotide sequence and primary structures of gene products !1coded for by the T4 genome between map positions 48.266 kb !1and 39.166 kb. !$#cross-references MUID:87203398; PMID:3575111 !$#accession D29284 !'##molecule_type DNA !'##residues 1-258 ##label TOM !'##cross-references GB:Y00122; NID:g15346; PIDN:CAA68309.1; PID:g15351 GENETICS !$#gene 55.12 CLASSIFICATION #superfamily phage T4 gene 55.12 protein SUMMARY #length 258 #molecular-weight 30367 #checksum 1322 SEQUENCE /// ENTRY Z7BPT9 #type complete TITLE gene 55.10 protein - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 23-Jul-1999 ACCESSIONS F29284 REFERENCE A30291 !$#authors Tomaschewski, J.; Rueger, W. !$#journal Nucleic Acids Res. (1987) 15:3632-3633 !$#title Nucleotide sequence and primary structures of gene products !1coded for by the T4 genome between map positions 48.266 kb !1and 39.166 kb. !$#cross-references MUID:87203398; PMID:3575111 !$#accession F29284 !'##molecule_type DNA !'##residues 1-210 ##label TOM !'##cross-references GB:Y00122; NID:g15346; PIDN:CAA68311.1; PID:g15353 GENETICS !$#gene 55.10 CLASSIFICATION #superfamily phage T4 gene 55.10 protein SUMMARY #length 210 #molecular-weight 23975 #checksum 443 SEQUENCE /// ENTRY Z9BPT9 #type complete TITLE gene 55.8 protein - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 23-Jul-1999 ACCESSIONS H29284 REFERENCE A30291 !$#authors Tomaschewski, J.; Rueger, W. !$#journal Nucleic Acids Res. (1987) 15:3632-3633 !$#title Nucleotide sequence and primary structures of gene products !1coded for by the T4 genome between map positions 48.266 kb !1and 39.166 kb. !$#cross-references MUID:87203398; PMID:3575111 !$#accession H29284 !'##molecule_type DNA !'##residues 1-70 ##label TOM !'##cross-references GB:Y00122; NID:g15346; PIDN:CAA68313.1; PID:g15355 GENETICS !$#gene 55.8 CLASSIFICATION #superfamily phage T4 gene 55.8 protein SUMMARY #length 70 #molecular-weight 7912 #checksum 758 SEQUENCE /// ENTRY ZABPT9 #type complete TITLE gene 55.7 protein - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 23-Jul-1999 ACCESSIONS I29284 REFERENCE A30291 !$#authors Tomaschewski, J.; Rueger, W. !$#journal Nucleic Acids Res. (1987) 15:3632-3633 !$#title Nucleotide sequence and primary structures of gene products !1coded for by the T4 genome between map positions 48.266 kb !1and 39.166 kb. !$#cross-references MUID:87203398; PMID:3575111 !$#accession I29284 !'##molecule_type DNA !'##residues 1-102 ##label TOM !'##cross-references GB:Y00122; NID:g15346; PIDN:CAA68314.1; PID:g579165 GENETICS !$#gene 55.7 CLASSIFICATION #superfamily phage T4 gene 55.7 protein SUMMARY #length 102 #molecular-weight 11752 #checksum 5569 SEQUENCE /// ENTRY ZBBPT9 #type complete TITLE gene 55.6 protein - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 23-Jul-1999 ACCESSIONS A30292 REFERENCE A30291 !$#authors Tomaschewski, J.; Rueger, W. !$#journal Nucleic Acids Res. (1987) 15:3632-3633 !$#title Nucleotide sequence and primary structures of gene products !1coded for by the T4 genome between map positions 48.266 kb !1and 39.166 kb. !$#cross-references MUID:87203398; PMID:3575111 !$#accession A30292 !'##molecule_type DNA !'##residues 1-60 ##label TOM !'##cross-references GB:Y00122; NID:g15346; PIDN:CAA68315.1; PID:g15357 GENETICS !$#gene 55.6 CLASSIFICATION #superfamily phage T4 gene 55.6 protein SUMMARY #length 60 #molecular-weight 6962 #checksum 7706 SEQUENCE /// ENTRY ZCBPT9 #type complete TITLE gene 55.5 protein - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 23-Jul-1999 ACCESSIONS B30292 REFERENCE A30291 !$#authors Tomaschewski, J.; Rueger, W. !$#journal Nucleic Acids Res. (1987) 15:3632-3633 !$#title Nucleotide sequence and primary structures of gene products !1coded for by the T4 genome between map positions 48.266 kb !1and 39.166 kb. !$#cross-references MUID:87203398; PMID:3575111 !$#accession B30292 !'##molecule_type DNA !'##residues 1-97 ##label TOM !'##cross-references GB:Y00122; NID:g15346; PIDN:CAA68316.1; PID:g15358 GENETICS !$#gene 55.5 CLASSIFICATION #superfamily phage T4 gene 55.5 protein SUMMARY #length 97 #molecular-weight 11808 #checksum 9852 SEQUENCE /// ENTRY ZDBPT9 #type complete TITLE gene 55.4 protein - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 23-Jul-1999 ACCESSIONS C30292 REFERENCE A30291 !$#authors Tomaschewski, J.; Rueger, W. !$#journal Nucleic Acids Res. (1987) 15:3632-3633 !$#title Nucleotide sequence and primary structures of gene products !1coded for by the T4 genome between map positions 48.266 kb !1and 39.166 kb. !$#cross-references MUID:87203398; PMID:3575111 !$#accession C30292 !'##molecule_type DNA !'##residues 1-43 ##label TOM !'##cross-references GB:Y00122; NID:g15346; PIDN:CAA68317.1; PID:g15359 GENETICS !$#gene 55.4 CLASSIFICATION #superfamily phage T4 gene 55.4 protein SUMMARY #length 43 #molecular-weight 5146 #checksum 2533 SEQUENCE /// ENTRY ZEBPT9 #type complete TITLE gene 55.3 protein - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 23-Jul-1999 ACCESSIONS D30292 REFERENCE A30291 !$#authors Tomaschewski, J.; Rueger, W. !$#journal Nucleic Acids Res. (1987) 15:3632-3633 !$#title Nucleotide sequence and primary structures of gene products !1coded for by the T4 genome between map positions 48.266 kb !1and 39.166 kb. !$#cross-references MUID:87203398; PMID:3575111 !$#accession D30292 !'##molecule_type DNA !'##residues 1-79 ##label TOM !'##cross-references GB:Y00122; NID:g15346; PIDN:CAA68318.1; PID:g15360 GENETICS !$#gene 55.3 CLASSIFICATION #superfamily phage T4 gene 55.3 protein SUMMARY #length 79 #molecular-weight 9152 #checksum 3412 SEQUENCE /// ENTRY ZFBPT9 #type complete TITLE gene 55.2 protein - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 23-Jul-1999 ACCESSIONS E30292 REFERENCE A30291 !$#authors Tomaschewski, J.; Rueger, W. !$#journal Nucleic Acids Res. (1987) 15:3632-3633 !$#title Nucleotide sequence and primary structures of gene products !1coded for by the T4 genome between map positions 48.266 kb !1and 39.166 kb. !$#cross-references MUID:87203398; PMID:3575111 !$#accession E30292 !'##molecule_type DNA !'##residues 1-108 ##label TOM !'##cross-references GB:Y00122; NID:g15346; PIDN:CAA68319.1; PID:g15361 GENETICS !$#gene 55.2 CLASSIFICATION #superfamily phage T4 gene 55.2 protein SUMMARY #length 108 #molecular-weight 12727 #checksum 8103 SEQUENCE /// ENTRY ZGBPT9 #type complete TITLE gene 55.1 protein - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 23-Jul-1999 ACCESSIONS F30292 REFERENCE A30291 !$#authors Tomaschewski, J.; Rueger, W. !$#journal Nucleic Acids Res. (1987) 15:3632-3633 !$#title Nucleotide sequence and primary structures of gene products !1coded for by the T4 genome between map positions 48.266 kb !1and 39.166 kb. !$#cross-references MUID:87203398; PMID:3575111 !$#accession F30292 !'##molecule_type DNA !'##residues 1-87 ##label TOM !'##cross-references GB:Y00122; NID:g15346; PIDN:CAA68320.1; PID:g15362 GENETICS !$#gene 55.1 CLASSIFICATION #superfamily phage T4 gene 55.1 protein SUMMARY #length 87 #molecular-weight 9845 #checksum 433 SEQUENCE /// ENTRY Z5BPT4 #type complete TITLE gene 55 protein - phage T4 ORGANISM #formal_name phage T4 DATE 17-Mar-1987 #sequence_revision 23-Oct-1998 #text_change 16-Jun-2000 ACCESSIONS B30291; A04300 REFERENCE A30291 !$#authors Tomaschewski, J.; Rueger, W. !$#journal Nucleic Acids Res. (1987) 15:3632-3633 !$#title Nucleotide sequence and primary structures of gene products !1coded for by the T4 genome between map positions 48.266 kb !1and 39.166 kb. !$#cross-references MUID:87203398; PMID:3575111 !$#accession B30291 !'##status preliminary !'##molecule_type DNA !'##residues 1-185 ##label TOM !'##cross-references GB:Y00122; NID:g15346; PIDN:CAA68321.1; !1PID:g1177561 REFERENCE A91016 !$#authors Gram, H.; Ruger, W. !$#journal EMBO J. (1985) 4:257-264 !$#title Genes 55, alpha-gt, 47 and 46 of bacteriophage T4: the !1genomic organization as deduced by sequence analysis. !$#cross-references MUID:85257446; PMID:4018026 !$#accession A04300 !'##molecule_type DNA !'##residues 1-174,'P',176-185 ##label GRA !'##cross-references GB:X01804; NID:g15229; PIDN:CAA25934.1; PID:g15230 COMMENT This protein associates with the modified host RNA !1polymerase and is necessary for late RNA transcription. GENETICS !$#gene 55 CLASSIFICATION #superfamily phage T4 gene 55 protein KEYWORDS DNA binding; transcription regulation SUMMARY #length 185 #molecular-weight 21526 #checksum 5294 SEQUENCE /// ENTRY IDBP44 #type complete TITLE DNA polymerase accessory protein 45 - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 23-Jul-1999 ACCESSIONS A04301 REFERENCE A04301 !$#authors Spicer, E.K.; Noble, J.A.; Nossal, N.G.; Konigsberg, W.H.; !1Williams, K.R. !$#journal J. Biol. Chem. (1982) 257:8972-8979 !$#title Bacteriophage T4 gene 45. Sequences of the structural gene !1and its protein product. !$#cross-references MUID:82239387; PMID:6284751 !$#accession A04301 !'##molecule_type DNA !'##residues 1-227 ##label SPI !'##cross-references GB:V01535; NID:g15216; PIDN:CAA24777.1; PID:g15217 GENETICS !$#gene 45 CLASSIFICATION #superfamily phage T4 DNA polymerase accessory protein 45 KEYWORDS DNA replication SUMMARY #length 227 #molecular-weight 24832 #checksum 5827 SEQUENCE /// ENTRY IDBPA4 #type complete TITLE DNA polymerase accessory protein 44 - phage T4 ALTERNATE_NAMES gp 44 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 23-Jul-1999 ACCESSIONS A04302; PS0460; JS0784 REFERENCE A04302 !$#authors Spicer, E.K.; Nossal, N.G.; Williams, K.R. !$#journal J. Biol. Chem. (1984) 259:15425-15432 !$#title Bacteriophage T4 gene 44 DNA polymerase accessory protein. !1Sequences of gene 44 and its protein product. !$#cross-references MUID:85080036; PMID:6096371 !$#accession A04302 !'##molecule_type DNA !'##residues 1-319 ##label SPI !'##cross-references GB:M10160; GB:J02510; GB:X00769; NID:g2947028; !1PIDN:AAC05394.1; PID:g215905 !$#accession PS0460 !'##molecule_type protein !'##residues 1-22 ##label SP3 COMMENT This is one of the DNA polymerase accessory proteins which !1play essential roles in replication of T4 DNA. The gp44-gp62 !1complex has a DNA-dependent nucleotidase activity which is !1specific for ATP or dATP and stimulated by gp 45. COMMENT The accessory proteins are required for nick translation. COMMENT The gp44-gp62 complex utilize ATP hydrolysis to form a !1specific protein complex with gp 43, which facilitates the !1movement of polymerase along the template and increases the !1processivity. COMMENT This complex plays a role in unwinding the helix and !1enhances the action of gp 32 in strand separation. COMMENT The formation of the accessory protein-polymerase complex !1increases the fidelity of DNA replication since the addition !1of accessory proteins to T4 polymerase increases its 3'-5' !1exonuclease degradation ratio. GENETICS !$#gene 44 !$#map_position 30.911-31.868 CLASSIFICATION #superfamily phage T4 DNA polymerase accessory protein 44 KEYWORDS DNA replication SUMMARY #length 319 #molecular-weight 35786 #checksum 2979 SEQUENCE /// ENTRY IDBPT4 #type complete TITLE DNA polymerase accessory protein 62 - phage T4 ALTERNATE_NAMES gp 62 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 01-Dec-1995 ACCESSIONS A04303; JF0009 REFERENCE A04303 !$#authors Spicer, E.K.; Konigsberg, W.H. !$#book Bacteriophage T4, Mathews, C.K., Kutter, E.M., Mosig, G., !1and Berget, P.B., eds., pp.291-301, American Society for !1Microbiology, Washington, 1983 !$#title Organization and structure of four T4 genes coding for DNA !1replication proteins. !$#accession A04303 !'##molecule_type DNA !'##residues 1-187 ##label SPI COMMENT This protein is one of the DNA polymerase accessory proteins !1which play essential roles in replication of T4 DNA. The !1gp44-gp62 complex has a DNA-dependent nucleotidase activity !1which is specific for ATP and dATP and the activity is !1stimulated by gp 45. COMMENT The accessory proteins are required for nick translation. COMMENT The gp44-gp62 complex utilize ATP hydrolysis to form a !1specific protein complex with gp 43, which facilitates the !1movement of polymerase along the template and increases the !1processivity. This complex plays a role in unwinding the !1helix and enhances the action of gp 32 in strand separtion. COMMENT The formation of the accessory protein-polymerase complex !1increases the fidelity of DNA replication since the addition !1of accessory proteins to T4 polymerase increases its 3' to !15' exonuclease degradation ratio. GENETICS !$#gene 62 !$#map_position 30.346-30.907 CLASSIFICATION #superfamily phage T4 DNA polymerase accessory protein 62 KEYWORDS DNA replication SUMMARY #length 187 #molecular-weight 21363 #checksum 4741 SEQUENCE /// ENTRY Z2BPA4 #type complete TITLE rapid lysis protein IIA - phage T4 ALTERNATE_NAMES gp rIIA; rIIA protein ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 19-Feb-1984 #sequence_revision 03-Oct-1995 #text_change 16-Jun-2000 ACCESSIONS JU0400; A92909; A92868; S52613; A04304; PS0468; PS0469 REFERENCE PS0194 !$#authors Daegelen, P.; Brody, E. !$#journal Genetics (1990) 125:237-248 !$#title The rIIA gene of bacteriophage T4. I. Its DNA sequence and !1discovery of a new open reading frame between genes 60 and !1rIIA. !$#cross-references MUID:90337270; PMID:2379817 !$#accession JU0400 !'##molecule_type DNA !'##residues 1-725 ##label DAE !'##cross-references GB:X52686; GB:X00905; NID:g15177; PIDN:CAA36911.1; !1PID:g15179 REFERENCE A92909 !$#authors Sugino, A.; Drake, J.W. !$#journal J. Mol. Biol. (1984) 176:239-249 !$#title Modulation of mutation rates in bacteriophage T4 by a !1base-pair change a dozen nucleotides removed. !$#cross-references MUID:84267841; PMID:6748077 !$#accession A92909 !'##molecule_type DNA !'##residues 476-725 ##label HER !'##note the authors translated the codon ACA for residue 517 as Lys REFERENCE A92868 !$#authors Pribnow, D.; Sigurdson, D.C.; Gold, L.; Singer, B.S.; !1Napoli, C.; Brosius, J.; Dull, T.J.; Noller, H.F. !$#journal J. Mol. Biol. (1981) 149:337-376 !$#title rII cistrons of bacteriophage T4. DNA sequence around the !1intercistronic divide and positions of genetic landmarks. !$#cross-references MUID:82078066; PMID:6273585 !$#accession A92868 !'##molecule_type DNA !'##residues 587-615,'D',617-725 ##label PRI !'##note the authors translated the codon GCT for residue 595 as Ser REFERENCE S52613 !$#authors Kumagai, M.; Yamashita, T.; Honda, M.; Ikeda, H. !$#journal Genetics (1993) 135:255-264 !$#title Effects of uvsX, uvsY and DNA topoisomerase on the formation !1of tandem duplications of the rII gene in bacteriophage T4. !$#cross-references MUID:94063467; PMID:7916730 !$#accession S52613 !'##status preliminary; translation not shown !'##molecule_type DNA !'##residues 244-725 ##label KUM !'##cross-references EMBL:D16359; NID:g303761; PIDN:BAA23634.1; !1PID:g2648161 COMMENT This protein is found on the inner membrane of the host !1shortly after infection; it forms part of the replication !1complex and has DNA-binding properties. COMMENT The rIIA gene is one of two rII genes, loss of which gives !1rise to large, sharp edged plaques on E. coli strain B. GENETICS !$#gene rIIA !$#map_position 0.014-2.189 CLASSIFICATION #superfamily phage T4 rIIA protein KEYWORDS DNA binding; membrane protein SUMMARY #length 725 #molecular-weight 82893 #checksum 253 SEQUENCE /// ENTRY Z2BPB4 #type complete TITLE rIIB protein - phage T4 ORGANISM #formal_name phage T4 DATE 19-Feb-1984 #sequence_revision 19-Apr-1996 #text_change 16-Jun-2000 ACCESSIONS S52614; A04305; PS0195; A24705 REFERENCE S52613 !$#authors Kumagai, M.; Yamashita, T.; Honda, M.; Ikeda, H. !$#journal Genetics (1993) 135:255-264 !$#title Effects of uvsX, uvsY and DNA topoisomerase on the formation !1of tandem duplications of the rII gene in bacteriophage T4. !$#cross-references MUID:94063467; PMID:7916730 !$#accession S52614 !'##status preliminary; translation not shown !'##molecule_type DNA !'##residues 1-312 ##label KUM !'##cross-references EMBL:D16359; NID:g303761; PIDN:BAA23635.1; !1PID:g2648162 REFERENCE A92868 !$#authors Pribnow, D.; Sigurdson, D.C.; Gold, L.; Singer, B.S.; !1Napoli, C.; Brosius, J.; Dull, T.J.; Noller, H.F. !$#journal J. Mol. Biol. (1981) 149:337-376 !$#title rII cistrons of bacteriophage T4. DNA sequence around the !1intercistronic divide and positions of genetic landmarks. !$#cross-references MUID:82078066; PMID:6273585 !$#accession A04305 !'##molecule_type DNA !'##residues 1-146 ##label PRI REFERENCE PS0194 !$#authors Daegelen, P.; Brody, E. !$#journal Genetics (1990) 125:237-248 !$#title The rIIA gene of bacteriophage T4. I. Its DNA sequence and !1discovery of a new open reading frame between genes 60 and !1rIIA. !$#cross-references MUID:90337270; PMID:2379817 !$#accession PS0195 !'##status preliminary !'##molecule_type DNA !'##residues 1-33 ##label DAE REFERENCE A24705 !$#authors Huang, W.M. !$#journal Nucleic Acids Res. (1986) 14:7379-7390 !$#title The 52-protein subunit of T4 DNA topoisomerase is homologous !1to the gyrA-protein of gyrase. !$#cross-references MUID:87016377; PMID:3020513 !$#accession A24705 !'##status preliminary !'##molecule_type DNA !'##residues 146-312 ##label HUA !'##cross-references GB:X04376; NID:g728618; PIDN:CAA27958.1; !1PID:g728619 GENETICS !$#gene rIIB !$#map_position 0 CLASSIFICATION #superfamily phage T4 gene rIIB protein KEYWORDS DNA binding SUMMARY #length 312 #molecular-weight 35541 #checksum 7136 SEQUENCE /// ENTRY RGBPT4 #type complete TITLE translation repressor - phage T4 ALTERNATE_NAMES gp regA ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 24-Sep-1999 ACCESSIONS A93530; A94029; PS0465; A45083; A04306 REFERENCE A93530 !$#authors Trojanowska, M.; Miller, E.S.; Karam, J.; Stormo, G.; Gold, !1L. !$#journal Nucleic Acids Res. (1984) 12:5979-5993 !$#title The bacteriophage T4 regA gene: primary sequence of a !1translational repressor. !$#cross-references MUID:84297207; PMID:6473098 !$#accession A93530 !'##molecule_type DNA !'##residues 1-122 ##label TRO !'##cross-references GB:X00769; NID:g15377; PIDN:CAA25343.1; PID:g15381 REFERENCE A94029 !$#authors Adari, H.Y.; Rose, K.; Williams, K.R.; Konigsberg, W.H.; !1Lin, T.C.; Spicer, E.K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:1901-1905 !$#title Cloning, nucleotide sequence, and overexpression of the !1bacteriophage T4 regA gene. !$#cross-references MUID:85166240; PMID:3872458 !$#accession A94029 !'##molecule_type DNA !'##residues 1-122 ##label ADA !'##cross-references GB:M10160; GB:J02510; GB:X00769; NID:g2947028; !1PIDN:AAC05396.1; PID:g215907 !$#accession PS0465 !'##molecule_type protein !'##residues 1-31 ##label AD1 REFERENCE A45083 !$#authors Webster, K.R.; Keill, S.; Konigsberg, W.; Williams, K.R.; !1Spicer, E.K. !$#journal J. Biol. Chem. (1992) 267:26097-26103 !$#title Identification of amino acid residues at the interface of a !1bacteriophage T4 regA protein-nucleic acid complex. !$#cross-references MUID:93100336; PMID:1464621 !$#accession A45083 !'##status preliminary !'##molecule_type protein !'##residues 1-122 ##label WEB !'##note sequence extracted from NCBI backbone (NCBIP:120914) COMMENT This protein is an autogenously controlled translational !1regulatory protein that plays a role in differential !1inhibition (translational repression) of a subpopulation of !1T4-encoded early mRNA. COMMENT Mutations in the regA gene result in overproduction of phage !1DNA replication proteins and rIIA/B proteins as well as of !1the defective regA peptides. GENETICS !$#gene regA !$#map_position 29.976-30.342 CLASSIFICATION #superfamily phage T4 translation repressor KEYWORDS RNA binding; translation repressor SUMMARY #length 122 #molecular-weight 14619 #checksum 5571 SEQUENCE /// ENTRY RRBPT4 #type complete TITLE recombination/repair protein precursor - phage T4 ALTERNATE_NAMES gp uvsX precursor ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 23-Jul-1999 ACCESSIONS A04307; PS0466; A44782 REFERENCE A04307 !$#authors Fujisawa, H.; Yonesaki, T.; Minagawa, T. !$#journal Nucleic Acids Res. (1985) 13:7473-7481 !$#title Sequence of the T4 recombination gene, uvsX, and its !1comparison with that of the recA gene of Escherichia coli. !$#cross-references MUID:86041927; PMID:2932679 !$#accession A04307 !'##molecule_type DNA !'##residues 1-390 ##label FUJ !'##cross-references GB:K03113; NID:g215964; PIDN:AAA32552.1; !1PID:g215965 !$#accession PS0466 !'##molecule_type protein !'##residues 2-7 ##label FU2 REFERENCE A44782 !$#authors Hinton, D.M. !$#journal J. Biol. Chem. (1989) 264:14440-14446 !$#title Altered expression of the bacteriophage T4 gene 41 !1(primase-helicase) in an Escherichia coli rho mutant. !$#cross-references MUID:89340565; PMID:2668290 !$#accession A44782 !'##status preliminary !'##molecule_type DNA !'##residues 361-390 ##label HIN !'##cross-references GB:J04978; NID:g215913; PIDN:AAA32523.1; !1PID:g215914 GENETICS !$#gene uvsX !$#map_position 22.393-23.563 CLASSIFICATION #superfamily phage T4 recombination and repair protein KEYWORDS DNA recombination; DNA repair FEATURE !$2-390 #product uvsX protein #status predicted #label MAT\ !$76-99 #region tyrosine-rich\ !$374-390 #region acidic SUMMARY #length 390 #molecular-weight 43909 #checksum 2750 SEQUENCE /// ENTRY GUBPT4 #type complete TITLE proximal tail fiber protein gp34 - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 30-Sep-1991 #sequence_revision 17-Feb-1994 #text_change 28-Jul-2000 ACCESSIONS JT0576; S05555 REFERENCE JT0576 !$#authors Mesyanzhinov, V.V. !$#submission submitted to JIPID, April 1991 !$#accession JT0576 !'##molecule_type DNA !'##residues 1-1289 ##label MES REFERENCE S05555 !$#authors Hahn, S.; Rueger, W. !$#journal Nucleic Acids Res. (1989) 17:6729 !$#title Organization of the bacteriophage T4 genome between map !1positions 150.745 and 145.824. !$#cross-references MUID:89386003; PMID:2674900 !$#accession S05555 !'##status translation not shown !'##molecule_type DNA !'##residues 1-694 ##label HAH !'##cross-references EMBL:X15818; NID:g4490552; PIDN:CAA33811.2; !1PID:g4490553 GENETICS !$#gene 34 CLASSIFICATION #superfamily phage T4 gene 34 protein KEYWORDS tail fiber SUMMARY #length 1289 #molecular-weight 140403 #checksum 1450 SEQUENCE /// ENTRY GWBPT4 #type complete TITLE gene 33 protein - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 05-Sep-1997 ACCESSIONS S05558 REFERENCE S05555 !$#authors Hahn, S.; Rueger, W. !$#journal Nucleic Acids Res. (1989) 17:6729 !$#title Organization of the bacteriophage T4 genome between map !1positions 150.745 and 145.824. !$#cross-references MUID:89386003; PMID:2674900 !$#accession S05558 !'##status translation not shown !'##molecule_type DNA !'##residues 1-112 ##label HAH !'##cross-references EMBL:X15818; NID:g15210; PID:g15213 GENETICS !$#gene 33 CLASSIFICATION #superfamily phage T4 gene 33 protein SUMMARY #length 112 #molecular-weight 12830 #checksum 9958 SEQUENCE /// ENTRY GRBPT4 #type complete TITLE RNA polymerase-binding protein - phage T4 ALTERNATE_NAMES rpbA protein ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 23-Jul-1999 ACCESSIONS JF0029; NT0063 REFERENCE JF0029 !$#authors Hsu, T.; Wei, R.; Dawson, M.; Karam, J.D. !$#journal J. Virol. (1987) 61:366-374 !$#title Identification of two new bacteriophage T4 genes that may !1have roles in transcription and DNA replication. !$#cross-references MUID:87112930; PMID:3543399 !$#accession JF0029 !'##molecule_type DNA !'##residues 1-100 ##label HSU !'##cross-references GB:M15080; NID:g215894; PIDN:AAA32518.1; !1PID:g215897 !$#accession NT0063 !'##molecule_type protein !'##residues 1-23 ##label HS2 !'##note two open reading frames between genes 45 and 46 were designated !1as genes 45.1 and 45.2 COMMENT Genes 45.1 and 45.2 are cotranscribed with gene 45 and have !1roles in controlling phage-induced transcription and !1replication. COMMENT The gene coding for an RNA polymerase-binding 15K protein !1maps to the location of the 45.1 cistron. GENETICS !$#gene rpbA !$#map_position 32.417-32.717 CLASSIFICATION #superfamily phage T4 RNA polymerase-binding protein SUMMARY #length 100 #molecular-weight 11391 #checksum 7786 SEQUENCE /// ENTRY Z4BPT4 #type complete TITLE helicase (EC 3.6.1.-) primase chain - phage T4 ALTERNATE_NAMES gp 41 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 19-Jan-2001 ACCESSIONS A04308 REFERENCE A94456 !$#authors Nakanishi, M.; Alberts, B. !$#citation unpublished results 1985, cited by GenBank !$#accession A04308 !'##molecule_type DNA !'##residues 1-475 ##label NAK !'##cross-references GB:K03113; NID:g215964; PIDN:AAA32553.1; !1PID:g215966 REFERENCE A58645 !$#authors Young, M.C.; Schultz, D.E.; Ring, D.; von Hippel, P.H. !$#journal J. Mol. Biol. (1994) 235:1447-1458 !$#title Kinetic parameters of the translocation of bacteriophage T4 !1gene 41 protein helicase on single-stranded DNA. !$#cross-references MUID:94149695; PMID:8107085 !$#contents annotation; enzyme activity COMMENT This protein has GTPase, dGTPase and dATPase activities, and !1it is a helicase-primase subunit. GENETICS !$#gene 41 !$#map_position 20.619-22.044 !$#start_codon GUG CLASSIFICATION #superfamily phage T4 gene 41 protein KEYWORDS DNA binding; DNA repair; DNA replication; hydrolase; !1nucleotide binding; P-loop FEATURE !$197-204 #region nucleotide-binding motif A (P-loop) SUMMARY #length 475 #molecular-weight 53601 #checksum 3450 SEQUENCE /// ENTRY ZABPT4 #type complete TITLE gene 57A protein - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 28-Jul-2000 ACCESSIONS B92919; A93414; A04310 REFERENCE A92919 !$#authors Broida, J.; Abelson, J. !$#journal J. Mol. Biol. (1985) 185:545-563 !$#title Sequence organization and control of transcription in the !1bacteriophage T4 tRNA region. !$#cross-references MUID:86037230; PMID:4057254 !$#accession B92919 !'##molecule_type DNA !'##residues 1-80 ##label BRO !'##cross-references GB:X03016; GB:J02511; GB:J02516; GB:J02517; !1GB:V00861; GB:V00862; NID:g15386; PIDN:CAA26801.1; !1PID:g15388 REFERENCE A93414 !$#authors Herrmann, R. !$#journal Nucleic Acids Res. (1982) 10:1105-1112 !$#title Nucleotide sequence of the bacteriophge T4 gene 57 and a !1deduced amino acid sequence. !$#cross-references MUID:82150240; PMID:7063418 !$#accession A93414 !'##molecule_type DNA !'##residues 1-80 ##label HER !'##cross-references GB:X03016; GB:J02516; NID:g15386; PIDN:CAA26801.1; !1PID:g15388 GENETICS !$#gene 57A CLASSIFICATION #superfamily phage T4 gene 57A protein KEYWORDS DNA binding SUMMARY #length 80 #molecular-weight 8731 #checksum 3707 SEQUENCE /// ENTRY ZBBPT4 #type complete TITLE gene 57B protein - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 23-Jul-1999 ACCESSIONS A04311 REFERENCE A92919 !$#authors Broida, J.; Abelson, J. !$#journal J. Mol. Biol. (1985) 185:545-563 !$#title Sequence organization and control of transcription in the !1bacteriophage T4 tRNA region. !$#cross-references MUID:86037230; PMID:4057254 !$#accession A04311 !'##molecule_type DNA !'##residues 1-152 ##label BRO !'##cross-references GB:X03016; GB:J02511; GB:J02516; GB:J02517; !1GB:V00861; GB:V00862; NID:g15386; PIDN:CAA26802.1; !1PID:g15389 GENETICS !$#gene 57B CLASSIFICATION #superfamily phage T4 gene 57B protein SUMMARY #length 152 #molecular-weight 17244 #checksum 2170 SEQUENCE /// ENTRY Z2BPT4 #type complete TITLE major prohead scaffolding core protein gp22 - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 17-Mar-1987 #sequence_revision 30-Sep-1990 #text_change 23-Jul-1999 ACCESSIONS S06066; A04312; C04348; A04348; JS0358 REFERENCE S06066 !$#authors Marusich, E.I.; Mesyanzhinov, V.V. !$#journal Nucleic Acids Res. (1989) 17:8865 !$#title Nucleotide and deduced amino acid sequences of bacteriophage !1T4 gene 22. !$#cross-references MUID:90067860; PMID:2587226 !$#accession S06066 !'##molecule_type DNA !'##residues 1-269 ##label MAR !'##cross-references GB:X16492; NID:g15298; PIDN:CAA34509.1; PID:g15299 REFERENCE A94505 !$#authors Christensen, A.C.; Parker, M.L. !$#submission submitted to GenBank, August 1981 !$#accession A04312 !'##molecule_type DNA !'##residues 86-88,'S',90-269 ##label CHR REFERENCE A92849 !$#authors van Eerd, J.P.; Champe, S.P.; Yager, L.; Kubota, I.; !1Tsugita, A. !$#journal J. Mol. Biol. (1977) 117:521-524 !$#title Primary structure of internal peptide VII of T-even !1bacteriophages. !$#cross-references MUID:78111436; PMID:604510 !$#accession C04348 !'##molecule_type protein !'##residues 62-76,'E',78-84 ##label VAN COMMENT Mutations in gene 22 affect the head width. GENETICS !$#gene 22 CLASSIFICATION #superfamily phage T4 gene 22 protein KEYWORDS core protein FEATURE !$62-84 #product internal peptide VII #status experimental !8#label IA8 SUMMARY #length 269 #molecular-weight 29904 #checksum 9798 SEQUENCE /// ENTRY ZTBPT9 #type fragment TITLE gene 50 protein - phage T4 (fragment) ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 23-Jul-1999 ACCESSIONS A32254 REFERENCE A91899 !$#authors Lipinska, B.; Rao, A.S.M.K.; Bolten, B.M.; Balakrishnan, R.; !1Goldberg, E.B. !$#journal J. Bacteriol. (1989) 171:488-497 !$#title Cloning and identification of bacteriophage T4 gene 2 !1product gp2 and action of gp2 on infecting DNA in vivo. !$#cross-references MUID:89123061; PMID:2644202 !$#accession A32254 !'##molecule_type DNA !'##residues 1-125 ##label LIP !'##cross-references GB:M23012; NID:g340786; PIDN:AAA50417.1; !1PID:g557581 GENETICS !$#gene 50 CLASSIFICATION #superfamily phage T4 gene 50 protein SUMMARY #length 125 #checksum 4860 SEQUENCE /// ENTRY ZHBPT9 #type complete TITLE head protein gp2 - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 23-Jul-1999 ACCESSIONS B32254 REFERENCE A91899 !$#authors Lipinska, B.; Rao, A.S.M.K.; Bolten, B.M.; Balakrishnan, R.; !1Goldberg, E.B. !$#journal J. Bacteriol. (1989) 171:488-497 !$#title Cloning and identification of bacteriophage T4 gene 2 !1product gp2 and action of gp2 on infecting DNA in vivo. !$#cross-references MUID:89123061; PMID:2644202 !$#accession B32254 !'##molecule_type DNA !'##residues 1-234 ##label LIP !'##cross-references GB:M23012; NID:g340786; PIDN:AAA50418.1; !1PID:g557582 GENETICS !$#gene 2 CLASSIFICATION #superfamily phage T4 head protein gp2 KEYWORDS head protein SUMMARY #length 234 #molecular-weight 27104 #checksum 8685 SEQUENCE /// ENTRY ZRBPT9 #type complete TITLE gene 3 protein - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 23-Jul-1999 ACCESSIONS C32254; S04611 REFERENCE A91899 !$#authors Lipinska, B.; Rao, A.S.M.K.; Bolten, B.M.; Balakrishnan, R.; !1Goldberg, E.B. !$#journal J. Bacteriol. (1989) 171:488-497 !$#title Cloning and identification of bacteriophage T4 gene 2 !1product gp2 and action of gp2 on infecting DNA in vivo. !$#cross-references MUID:89123061; PMID:2644202 !$#accession C32254 !'##molecule_type DNA !'##residues 1-184 ##label LIP !'##cross-references GB:M23012; NID:g340786; PIDN:AAA50419.1; !1PID:g557583 REFERENCE S04608 !$#authors Koch, T.; Lamm, N.; Rueger, W. !$#journal Nucleic Acids Res. (1989) 17:4392 !$#title Sequencing, cloning and overexpression of genes of !1bacteriophage T4 between map positions 74.325 and 77.184. !$#cross-references MUID:89296504; PMID:2740234 !$#accession S04611 !'##status translation not shown !'##molecule_type DNA !'##residues 1-176 ##label KOC !'##cross-references EMBL:X14845; NID:g15218; PIDN:CAA32952.1; !1PID:g15222 GENETICS !$#gene 3 CLASSIFICATION #superfamily phage T4 gene 3 protein SUMMARY #length 184 #molecular-weight 20660 #checksum 941 SEQUENCE /// ENTRY VHBPT4 #type complete TITLE major capsid protein - phage T4 ALTERNATE_NAMES major head protein; major head protein gP23* ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 23-Jul-1999 ACCESSIONS A92911; A92998; S10634; S03363; A04313 REFERENCE A92911 !$#authors Parker, M.L.; Christensen, A.C.; Boosman, A.; Stockard, J.; !1Young, E.T.; Doermann, A.H. !$#journal J. Mol. Biol. (1984) 180:399-416 !$#title Nucleotide sequence of bacteriophage T4 gene 23 and the !1amino acid sequence of its product. !$#cross-references MUID:85134863; PMID:6335532 !$#accession A92911 !'##molecule_type DNA !'##residues 1-521 ##label PAR !'##cross-references GB:K01765; GB:J02506; GB:J02507; NID:g215870; !1PIDN:AAA32503.1; PID:g215872 REFERENCE A92998 !$#authors Champness, W.C.; Snyder, L. !$#journal J. Virol. (1984) 50:555-562 !$#title Bacteriophage T4 gol site: sequence analysis and effects of !1the site on plasmid transformation. !$#cross-references MUID:84165083; PMID:6323755 !$#accession A92998 !'##molecule_type DNA !'##residues 48-138 ##label CHA !'##cross-references GB:K01765 REFERENCE S10634 !$#authors Bergsland, K.J.; Kao, C.; Yu, Y.T.N.; Gulati, R.; Snyder, L. !$#journal J. Mol. Biol. (1990) 213:477-494 !$#title A site in the T4 bacteriophage major head protein gene that !1can promote the inhibition of all translation in Escherichia !1coli. !$#cross-references MUID:90278957; PMID:2191141 !$#accession S10634 !'##status preliminary !'##molecule_type DNA !'##residues 93-132 ##label BER REFERENCE S03363 !$#authors Tsugita, A.; van den Broek, R. !$#journal Protein Seq. Data Anal. (1987) 1:99-102 !$#title The amino acid sequence of crystalline sheets: a proteolytic !1fragment of the major head protein (gP23*) of bacteriophage !1T4. !$#cross-references MUID:88190060; PMID:3447164 !$#accession S03363 !'##molecule_type protein !'##residues 295-304;313-381;395-449 ##label TSU !'##experimental_source strain D GENETICS !$#gene 23 CLASSIFICATION #superfamily phage T4 major capsid protein KEYWORDS capsid protein; coat protein SUMMARY #length 521 #molecular-weight 56048 #checksum 9886 SEQUENCE /// ENTRY FIBPT4 #type complete TITLE fibritin - phage T4 ALTERNATE_NAMES collar protein; whisker protein ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 19-Apr-1996 ACCESSIONS S01917; JT0578 REFERENCE S01917 !$#authors Prilipov, A.G.; Selivanov, N.A.; Nikolaeva, L.I.; !1Mesyanzhinov, V.V. !$#journal Nucleic Acids Res. (1988) 16:10361 !$#title Nucleotide and deduced amino acid sequence of bacteriophage !1T4 gene wac. !$#cross-references MUID:89057475; PMID:3194206 !$#accession S01917 !'##molecule_type DNA !'##residues 1-487 ##label PRI REFERENCE JT0578 !$#authors Mesyanzhinov, V.V.; Efimov, V.P.; Sobolev, B.N.; !1Zurabishvili, T.G.; Bukovsky, A.A.; Miyatake, N.; Tsugita, !1A. !$#submission submitted to JIPID, July 1990 !$#accession JT0578 !'##status preliminary !'##molecule_type protein !'##residues 2-35 ##label MES GENETICS !$#gene wac !$#map_position 91.450-92.800 CLASSIFICATION #superfamily phage T4 fibritin FEATURE !$2-487 #product fibritin #status predicted #label MAT SUMMARY #length 487 #molecular-weight 51881 #checksum 4565 SEQUENCE /// ENTRY G6BPT4 #type complete TITLE baseplate protein gp6 - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 23-Jul-1999 ACCESSIONS JQ0656 REFERENCE JQ0656 !$#authors Efimov, V.P.; Prilipov, A.G.; Mesyanzhinov, V.V. !$#journal Nucleic Acids Res. (1990) 18:5313 !$#title Nucleotide sequences of bacteriophage T4 genes 6, 7 and 8. !$#cross-references MUID:90384864; PMID:2402473 !$#accession JQ0656 !'##molecule_type DNA !'##residues 1-660 ##label EFI !'##cross-references EMBL:X15907; NID:g15321; PIDN:CAA34021.1; !1PID:g15322 GENETICS !$#gene 6 CLASSIFICATION #superfamily phage T4 baseplate protein gp6 KEYWORDS baseplate; late protein SUMMARY #length 660 #molecular-weight 74428 #checksum 5756 SEQUENCE /// ENTRY G7BPT4 #type complete TITLE baseplate protein gp7 - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 23-Jul-1999 ACCESSIONS JQ0657 REFERENCE JQ0656 !$#authors Efimov, V.P.; Prilipov, A.G.; Mesyanzhinov, V.V. !$#journal Nucleic Acids Res. (1990) 18:5313 !$#title Nucleotide sequences of bacteriophage T4 genes 6, 7 and 8. !$#cross-references MUID:90384864; PMID:2402473 !$#accession JQ0657 !'##molecule_type DNA !'##residues 1-1032 ##label EFI !'##cross-references EMBL:X15907; NID:g15321; PIDN:CAA34022.1; !1PID:g15323 GENETICS !$#gene 7 CLASSIFICATION #superfamily phage T4 baseplate protein gp7 KEYWORDS baseplate; late protein SUMMARY #length 1032 #molecular-weight 119214 #checksum 3351 SEQUENCE /// ENTRY G8BPT4 #type complete TITLE baseplate protein gp8 - phage T4 ALTERNATE_NAMES baseplate wedge protein ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 23-Jul-1999 ACCESSIONS JQ0658; JF0058 REFERENCE JQ0656 !$#authors Efimov, V.P.; Prilipov, A.G.; Mesyanzhinov, V.V. !$#journal Nucleic Acids Res. (1990) 18:5313 !$#title Nucleotide sequences of bacteriophage T4 genes 6, 7 and 8. !$#cross-references MUID:90384864; PMID:2402473 !$#accession JQ0658 !'##molecule_type DNA !'##residues 1-334 ##label EFI !'##cross-references EMBL:X15907; NID:g15321; PIDN:CAA34023.1; !1PID:g15324 REFERENCE JF0058 !$#authors Mesyanzhinov, V.V. !$#submission submitted to JIPID, December 1989 !$#accession JF0058 !'##molecule_type DNA !'##residues 1-334 ##label MES COMMENT The order of association in the morphogenesis pathway is !1strictly determined except for gp 11 which can be added at !1any stage of the pathway. Gp 8 associates to the precursor !1structure after gp 7 binding and before gp 6 binding. GENETICS !$#gene gp8 !$#map_position 85.20-86.20 !$#note gene 8 is directed clockwise in the T4 map; the 5'-end of !1gene 8 overlaps with the 3'-end of gene 7 CLASSIFICATION #superfamily phage T4 baseplate protein gp8 KEYWORDS baseplate; late protein SUMMARY #length 334 #molecular-weight 38007 #checksum 5888 SEQUENCE /// ENTRY GNBPT4 #type complete TITLE gene 9 protein - phage T4 ALTERNATE_NAMES baseplate protein gp9 ORGANISM #formal_name phage T4 DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 23-Jul-1999 ACCESSIONS S04082; PT0033 REFERENCE S04082 !$#authors Prilipov, A.G.; Selivanov, N.A.; Efimov, V.P.; Marusich, !1E.I.; Mesyanzhinov, V.V. !$#journal Nucleic Acids Res. (1989) 17:3303 !$#title Nucleotide sequences of bacteriophage T4 genes 9, 10 and 11. !$#cross-references MUID:89263746; PMID:2726468 !$#accession S04082 !'##status translation not shown !'##molecule_type DNA !'##residues 1-288 ##label PRI !'##cross-references EMBL:X14192; NID:g15242; PIDN:CAA32395.1; !1PID:g15243 REFERENCE PT0033 !$#authors Miyatake, N.; Zurbishivili, T.G.; Efimov, V.P.; Prilipov, !1A.G.; Mesyanzhinov, V.V.; Tsugita, A. !$#submission submitted to JIPID, June 1990 !$#accession PT0033 !'##status preliminary !'##molecule_type protein !'##residues 1-25 ##label MIY GENETICS !$#gene 9 CLASSIFICATION #superfamily phage T4 gene 9 protein KEYWORDS baseplate SUMMARY #length 288 #molecular-weight 30997 #checksum 2706 SEQUENCE /// ENTRY GEBPT4 #type complete TITLE gene 10 protein - phage T4 ORGANISM #formal_name phage T4 DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 23-Jul-1999 ACCESSIONS S04083; A32479 REFERENCE S04082 !$#authors Prilipov, A.G.; Selivanov, N.A.; Efimov, V.P.; Marusich, !1E.I.; Mesyanzhinov, V.V. !$#journal Nucleic Acids Res. (1989) 17:3303 !$#title Nucleotide sequences of bacteriophage T4 genes 9, 10 and 11. !$#cross-references MUID:89263746; PMID:2726468 !$#accession S04083 !'##status translation not shown !'##molecule_type DNA !'##residues 1-602 ##label PRI !'##cross-references EMBL:X14192; NID:g15242; PIDN:CAA32396.1; !1PID:g15244 REFERENCE A32479 !$#authors Barrett, B.K.; Berget, P.B. !$#journal DNA (1989) 8:287-295 !$#title Laboratory methods: using transposon Tn5 insertions to !1sequence bacteriophage T4 gene 11. !$#cross-references MUID:89356257; PMID:2548819 !$#accession A32479 !'##status preliminary !'##molecule_type DNA !'##residues 535-602 ##label BAR !'##cross-references GB:M26253; NID:g215856; PIDN:AAA32493.1; !1PID:g215857 GENETICS !$#gene 10 CLASSIFICATION #superfamily phage T4 gene 10 protein SUMMARY #length 602 #molecular-weight 66232 #checksum 6935 SEQUENCE /// ENTRY GLBPT4 #type complete TITLE baseplate protein gp11 - phage T4 ALTERNATE_NAMES gene 11 protein ORGANISM #formal_name phage T4 DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 23-Jul-1999 ACCESSIONS S04084; B32479; PT0035 REFERENCE S04082 !$#authors Prilipov, A.G.; Selivanov, N.A.; Efimov, V.P.; Marusich, !1E.I.; Mesyanzhinov, V.V. !$#journal Nucleic Acids Res. (1989) 17:3303 !$#title Nucleotide sequences of bacteriophage T4 genes 9, 10 and 11. !$#cross-references MUID:89263746; PMID:2726468 !$#accession S04084 !'##status translation not shown !'##molecule_type DNA !'##residues 1-219 ##label PRI !'##cross-references EMBL:X14192; NID:g15242; PIDN:CAA32397.1; !1PID:g15245 REFERENCE A32479 !$#authors Barrett, B.K.; Berget, P.B. !$#journal DNA (1989) 8:287-295 !$#title Laboratory methods: using transposon Tn5 insertions to !1sequence bacteriophage T4 gene 11. !$#cross-references MUID:89356257; PMID:2548819 !$#accession B32479 !'##molecule_type DNA !'##residues 1-219 ##label BAR !'##cross-references GB:M26253; NID:g215856; PIDN:AAA32494.1; !1PID:g215858 REFERENCE PT0033 !$#authors Miyatake, N.; Zurbishivili, T.G.; Efimov, V.P.; Prilipov, !1A.G.; Mesyanzhinov, V.V.; Tsugita, A. !$#submission submitted to JIPID, June 1990 !$#accession PT0035 !'##status preliminary !'##molecule_type protein !'##residues 9-17;31-40;121-130;153-162 ##label MIY GENETICS !$#gene 11 CLASSIFICATION #superfamily phage T4 gene 11 protein KEYWORDS baseplate SUMMARY #length 219 #molecular-weight 23706 #checksum 5298 SEQUENCE /// ENTRY GIBPT4 #type complete TITLE gene 12 protein - phage T4 ALTERNATE_NAMES tail fiber protein ORGANISM #formal_name phage T4 DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 30-Jun-1993 ACCESSIONS S01889 REFERENCE S01889 !$#authors Selivanov, N.A.; Prilipov, A.G.; Mesyanzhinov, V.V. !$#journal Nucleic Acids Res. (1988) 16:2334 !$#title Nucleotide and deduced amino acid sequence of bacteriophage !1T4 gene 12. !$#cross-references MUID:88189824; PMID:3357780 !$#accession S01889 !'##molecule_type DNA !'##residues 1-517 ##label SEL !'##cross-references EMBL:X06792 !'##note the authors translated the codon CAG for residue 279 as His GENETICS !$#gene 12 CLASSIFICATION #superfamily phage T4 gene 12 protein KEYWORDS tail fiber SUMMARY #length 517 #molecular-weight 55270 #checksum 9816 SEQUENCE /// ENTRY GTBPT4 #type complete TITLE gene 13 protein - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 23-Jul-1999 ACCESSIONS JF0052; S04096 REFERENCE JF0046 !$#authors Selivanov, N.A.; Prilipov, A.G.; Mesyanzhinov, V.V. !$#journal Nucleic Acids Res. (1989) 17:3583 !$#title Nucleotide sequences of bacteriophage T4 genes 13, 14 and !115. !$#cross-references MUID:89263795; PMID:2657662 !$#accession JF0052 !'##status translation not shown !'##molecule_type DNA !'##residues 1-309 ##label SEL !'##cross-references EMBL:X14868; NID:g15294; PIDN:CAA33007.1; !1PID:g15295 COMMENT Gene 13 protein is a component of the phage neck. GENETICS !$#gene 13 !$#map_position 92.80-93.55 CLASSIFICATION #superfamily phage T4 gene 13 protein SUMMARY #length 309 #molecular-weight 34741 #checksum 4387 SEQUENCE /// ENTRY GFBPT4 #type complete TITLE gene 14 protein - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 23-Jul-1999 ACCESSIONS JF0053; S04097 REFERENCE JF0046 !$#authors Selivanov, N.A.; Prilipov, A.G.; Mesyanzhinov, V.V. !$#journal Nucleic Acids Res. (1989) 17:3583 !$#title Nucleotide sequences of bacteriophage T4 genes 13, 14 and !115. !$#cross-references MUID:89263795; PMID:2657662 !$#accession JF0053 !'##status translation not shown !'##molecule_type DNA !'##residues 1-256 ##label SEL !'##cross-references EMBL:X14868; NID:g15294; PIDN:CAA33008.1; !1PID:g15296 COMMENT Gene 14 protein is a component of the phage neck. GENETICS !$#gene 14 !$#map_position 93.55-94.25 CLASSIFICATION #superfamily phage T4 gene 14 protein SUMMARY #length 256 #molecular-weight 29573 #checksum 2607 SEQUENCE /// ENTRY GHBPT4 #type complete TITLE gene 15 protein - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 23-Jul-1999 ACCESSIONS JF0046; S04098 REFERENCE JF0046 !$#authors Selivanov, N.A.; Prilipov, A.G.; Mesyanzhinov, V.V. !$#journal Nucleic Acids Res. (1989) 17:3583 !$#title Nucleotide sequences of bacteriophage T4 genes 13, 14 and !115. !$#cross-references MUID:89263795; PMID:2657662 !$#accession JF0046 !'##status translation not shown !'##molecule_type DNA !'##residues 1-272 ##label SEL !'##cross-references EMBL:X14868; NID:g15294; PIDN:CAA33009.1; !1PID:g15297 COMMENT Gene 15 protein is a component of the phage tail. GENETICS !$#gene 15 !$#map_position 94.25-95.00 CLASSIFICATION #superfamily phage T4 gene 15 protein KEYWORDS tail protein SUMMARY #length 272 #molecular-weight 31429 #checksum 5146 SEQUENCE /// ENTRY GSBPT4 #type complete TITLE gene 16 protein - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 23-Jul-1999 ACCESSIONS JU0286 REFERENCE JU0286 !$#authors Powell, D.; Franklin, J.; Arisaka, F.; Mosig, G. !$#journal Nucleic Acids Res. (1990) 18:4005 !$#title Bacteriophage T4 DNA packaging genes 16 and 17. !$#cross-references MUID:90326541; PMID:2374730 !$#accession JU0286 !'##molecule_type DNA !'##residues 1-164 ##label POW !'##cross-references EMBL:X52394; NID:g15199; PIDN:CAA36640.1; !1PID:g15200 COMMENT This protein is required to translocate phage T4 DNA into !1the head. GENETICS !$#gene 16 CLASSIFICATION #superfamily phage T4 gene 16 protein KEYWORDS DNA binding SUMMARY #length 164 #molecular-weight 18388 #checksum 8796 SEQUENCE /// ENTRY GVBPT4 #type complete TITLE gene 17 protein - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 23-Jul-1999 ACCESSIONS JU0287 REFERENCE JU0286 !$#authors Powell, D.; Franklin, J.; Arisaka, F.; Mosig, G. !$#journal Nucleic Acids Res. (1990) 18:4005 !$#title Bacteriophage T4 DNA packaging genes 16 and 17. !$#cross-references MUID:90326541; PMID:2374730 !$#accession JU0287 !'##molecule_type DNA !'##residues 1-610 ##label POW !'##cross-references EMBL:X52394; NID:g15199; PIDN:CAA36641.1; !1PID:g15201 COMMENT This protein is required to translocate phage T4 DNA into !1the head. GENETICS !$#gene 17 CLASSIFICATION #superfamily phage T4 gene 17 protein KEYWORDS DNA binding SUMMARY #length 610 #molecular-weight 69756 #checksum 7920 SEQUENCE /// ENTRY GPBPT4 #type complete TITLE prohead proteinase (EC 3.4.99.-) precursor - phage T4 ALTERNATE_NAMES gene 21 protein (gp21) ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 23-Jul-1999 ACCESSIONS JF0025 REFERENCE JF0025 !$#authors Keller, B.; Bickle, T.A. !$#journal Gene (1986) 49:245-251 !$#title The nucleotide sequence of gene 21 of bacteriophage T4 !1coding for the prohead protease. !$#cross-references MUID:87192014; PMID:3552886 !$#accession JF0025 !'##molecule_type DNA !'##residues 1-212 ##label KEL !'##cross-references EMBL:M15359; NID:g215866; PIDN:AAA32501.1; !1PID:g215868 GENETICS !$#gene 21 !$#map_position 102.28-102.9 FUNCTION !$#description proteolytic cleavage, generally between glutamic acid and !1alanine residues in helical peptides; necessary for !1maturation of prohead proteins !$#note may also function as a structural protein of the prohead !1core CLASSIFICATION #superfamily phage T4 prohead proteinase KEYWORDS core protein; hydrolase; proteinase FEATURE !$121 #active_site His #status predicted\ !$206-207 #cleavage_site Glu-Ala (autolytic) #status predicted SUMMARY #length 212 #molecular-weight 23250 #checksum 1628 SEQUENCE /// ENTRY IMBPT4 #type complete TITLE immunity protein - phage T4 ALTERNATE_NAMES gp imm; imm protein; ORF 42.1 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 23-Jul-1999 ACCESSIONS JF0072 REFERENCE JF0071 !$#authors Lamm, N.; Wang, Y.; Mathews, C.K.; Rueger, W. !$#journal Eur. J. Biochem. (1988) 172:553-563 !$#title Deoxycytidylate hydroxymethylase gene of bacteriophage T4: !1nucleotide sequence determination and over-expression of the !1gene. !$#cross-references MUID:88166734; PMID:3350013 !$#accession JF0072 !'##molecule_type DNA !'##residues 1-83 ##label LAM !'##cross-references GB:M37159; GB:M28192; NID:g215839; PIDN:AAA21708.1; !1PID:g215842 REFERENCE JS0785 !$#authors Lu, M.; Henning, U. !$#journal J. Virol. (1989) 63:3472-3478 !$#title Immunity (imm) gene of Escherichia coli bacteriophage T4. !$#cross-references MUID:89311640; PMID:2746737 !$#contents annotation COMMENT This protein is located in the plasma membrane. GENETICS !$#gene imm !$#map_position 26.377-26.626 CLASSIFICATION #superfamily phage T4 immunity region protein SUMMARY #length 83 #molecular-weight 9342 #checksum 2779 SEQUENCE /// ENTRY G2BPT4 #type complete TITLE hypothetical 14.1 protein (gene imm.1 protein) - phage T4 ALTERNATE_NAMES gp imm.1; gp42.2 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 23-Jul-1999 ACCESSIONS JU0098 REFERENCE JF0071 !$#authors Lamm, N.; Wang, Y.; Mathews, C.K.; Rueger, W. !$#journal Eur. J. Biochem. (1988) 172:553-563 !$#title Deoxycytidylate hydroxymethylase gene of bacteriophage T4: !1nucleotide sequence determination and over-expression of the !1gene. !$#cross-references MUID:88166734; PMID:3350013 !$#accession JU0098 !'##molecule_type DNA !'##residues 1-125 ##label LAM !'##cross-references GB:M37159; GB:M28192; NID:g215839; PIDN:AAA21707.1; !1PID:g215841 GENETICS !$#gene imm.1; 42.2 !$#map_position 26.640-27.015 CLASSIFICATION #superfamily phage T4 gene 42.2 protein SUMMARY #length 125 #molecular-weight 14074 #checksum 1357 SEQUENCE /// ENTRY YDBPA7 #type complete TITLE DNA primase - phage T7 CONTAINS DNA primase chain A; DNA primase chain B ORGANISM #formal_name phage T7 DATE 01-Sep-1981 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS A04314; B92866; S42304; S42306 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession A04314 !'##molecule_type DNA !'##residues 1-566 ##label DUN REFERENCE A92866 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1981) 148:303-330 !$#title Nucleotide sequence from the genetic left end of !1bacteriophage T7 DNA to the beginning of gene 4. !$#cross-references MUID:82078034; PMID:7310871 !$#accession B92866 !'##molecule_type DNA !'##residues 1-179 ##label DU2 !'##cross-references GB:V01127; NID:g15498; PIDN:CAA24348.1; PID:g408135 !'##note this late gene protein consists of two subunits, chains A and !1B. Both chains are the products of gene 4 and result from !1useage of alternative initiators REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42304 !'##molecule_type DNA !'##residues 1-566 ##label DUW !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24405.1; !1PID:g15584 !'##note chain A !$#accession S42306 !'##status translation not shown !'##molecule_type DNA !'##residues 64-566 ##label DUF !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24407.1; !1PID:g15586 !'##note chain B COMMENT DNA primase synthesizes RNA primers necessary for !1replication by T7 DNA polymerase. It also functions as an !1ATP-dependent unwinding protein. GENETICS !$#gene 4 !$#map_position 28.91-33.21 CLASSIFICATION #superfamily phage T7 DNA primase KEYWORDS alternative initiators FEATURE !$1-566 #product DNA primase chain A #status predicted #label !8DCA\ !$64-566 #product DNA primase chain B #status predicted #label !8DCB SUMMARY #length 566 #molecular-weight 62655 #checksum 4729 SEQUENCE /// ENTRY JVBPT3 #type complete TITLE DNA maturase A - phage T3 ALTERNATE_NAMES DNA packaging protein A ORGANISM #formal_name phage T3 #note host Escherichia coli DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 23-Jul-1999 ACCESSIONS C23476 REFERENCE A94339 !$#authors Yamada, M.; Fujisawa, H.; Kato, H.; Hamada, K.; Minagawa, T. !$#journal Virology (1986) 151:350-361 !$#title Cloning and sequencing of the genetic right end of !1bacteriophage T3 DNA. !$#cross-references MUID:86209997; PMID:3010556 !$#accession C23476 !'##molecule_type DNA !'##residues 1-89 ##label YAM !'##cross-references GB:M14784; NID:g215810; PIDN:AAA92525.1; !1PID:g215813 REFERENCE A94344 !$#authors Yamada, M.; Fujisawa, H.; Kato, H.; Hamada, K.; Minagawa, T. !$#journal Virology (1986) 154:246 !$#contents annotation; erratum; corrections to coding regions GENETICS !$#gene 18 CLASSIFICATION #superfamily phage T7 DNA maturase A KEYWORDS DNA packaging SUMMARY #length 89 #molecular-weight 10033 #checksum 3928 SEQUENCE /// ENTRY JVBPA7 #type complete TITLE DNA maturase A - phage T7 ORGANISM #formal_name phage T7 DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS A04315; S42335 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession A04315 !'##molecule_type DNA !'##residues 1-89 ##label DUN REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42335 !'##molecule_type DNA !'##residues 1-89 ##label DUW !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24437.1; !1PID:g15613 GENETICS !$#gene 18 !$#map_position 91.53-92.19 CLASSIFICATION #superfamily phage T7 DNA maturase A SUMMARY #length 89 #molecular-weight 10145 #checksum 4572 SEQUENCE /// ENTRY JVBPB3 #type complete TITLE DNA maturase B - phage T3 ALTERNATE_NAMES DNA packaging protein B; DNA packaging protein gp19 ORGANISM #formal_name phage T3 #note host Escherichia coli DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 23-Jul-1999 ACCESSIONS F23476; S53785 REFERENCE A94339 !$#authors Yamada, M.; Fujisawa, H.; Kato, H.; Hamada, K.; Minagawa, T. !$#journal Virology (1986) 151:350-361 !$#title Cloning and sequencing of the genetic right end of !1bacteriophage T3 DNA. !$#cross-references MUID:86209997; PMID:3010556 !$#accession F23476 !'##molecule_type DNA !'##residues 1-586 ##label YAM !'##cross-references GB:M14784; NID:g215810; PIDN:AAA92528.1; !1PID:g215814 REFERENCE A94344 !$#authors Yamada, M.; Fujisawa, H.; Kato, H.; Hamada, K.; Minagawa, T. !$#journal Virology (1986) 154:246 !$#contents annotation; erratum; corrections to coding regions REFERENCE S53785 !$#authors Morita, M.; Tasaka, M.; Fujisawa, H. !$#journal J. Mol. Biol. (1995) 245:635-644 !$#title Structural and functional domains of the large subunit of !1the bacteriophage T3 DNA packaging enzyme: importance of the !1C-terminal region in prohead binding. !$#cross-references MUID:95147284; PMID:7844832 !$#accession S53785 !'##molecule_type protein !'##residues 2-12;281-285;288-297 ##label MOR GENETICS !$#gene 19 !$#start_codon GTG CLASSIFICATION #superfamily phage T7 DNA maturase B KEYWORDS DNA packaging SUMMARY #length 586 #molecular-weight 66672 #checksum 1039 SEQUENCE /// ENTRY JVBPB7 #type complete TITLE DNA maturase B - phage T7 ALTERNATE_NAMES gene 19 protein ORGANISM #formal_name phage T7 DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS S42338; A04316 REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42338 !'##molecule_type DNA !'##residues 1-586 ##label DUN !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24440.1; !1PID:g579206 !'##note the authors did not translate the codon for residue 1 GENETICS !$#gene 19 !$#map_position 93.57-97.97 !$#start_codon GTG CLASSIFICATION #superfamily phage T7 DNA maturase B SUMMARY #length 586 #molecular-weight 66260 #checksum 3995 SEQUENCE /// ENTRY DDBP32 #type fragment TITLE helix-destabilizing protein - phage T2 (fragment) ALTERNATE_NAMES gene 32 protein; single-stranded DNA-binding protein ORGANISM #formal_name phage T2 DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 23-Jul-1999 ACCESSIONS S01437 REFERENCE S01437 !$#authors McPheeters, D.S.; Gosch, G.; Gold, L. !$#journal Nucleic Acids Res. (1988) 16:9341 !$#title Nucleotide sequences of the bacteriophage T2 and T6 gene 32 !1mRNAs. !$#cross-references MUID:89016637; PMID:3262868 !$#accession S01437 !'##molecule_type mRNA !'##residues 1-293 ##label MCP !'##cross-references EMBL:X12460; NID:g15192; PIDN:CAA31000.1; !1PID:g15193 GENETICS !$#gene 32 CLASSIFICATION #superfamily phage T4 helix-destabilizing protein KEYWORDS DNA binding; zinc finger FEATURE !$3-7 #region LAST motif\ !$111-115 #region LAST motif SUMMARY #length 293 #checksum 6760 SEQUENCE /// ENTRY DDBP34 #type complete TITLE helix-destabilizing protein - phage T4 ALTERNATE_NAMES gene 32 protein ORGANISM #formal_name phage T4 DATE 29-Jul-1981 #sequence_revision 17-Dec-1982 #text_change 26-Feb-1999 ACCESSIONS A93924; A92302; A04317 REFERENCE A93924 !$#authors Krisch, H.M.; Allet, B. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:4937-4941 !$#title Nucleotide sequences involved in bacteriophage T4 gene 32 !1translational self-regulation. !$#cross-references MUID:83015007; PMID:6289325 !$#contents amber mutant 32amA453 !$#accession A93924 !'##molecule_type DNA !'##residues 1-115;117-301 ##label KRI !'##note mutant 32amA453 contains the amber termination codon UAG at the !1position corresponding to 116-Trp. In agreement with the !1sequence elucidated by amino acid analysis, mutant 32amA453 !1may have been derived by a point mutation of the Trp codon !1UGG to UAG REFERENCE A92302 !$#authors Williams, K.R.; LoPresti, M.B.; Setoguchi, M. !$#journal J. Biol. Chem. (1981) 256:1754-1762 !$#title Primary structure of the bacteriophge T4 DNA !1helix-destabilizing protein. !$#cross-references MUID:81117259; PMID:6257686 !$#accession A92302 !'##molecule_type protein !'##residues 1-85,'A',87-90,'E',92-123,'N',125-155,'Q',157-193,'E', !1195-201,'N',203-211,'E',213-222,'N',224-275,'NN',278-301 !1##label WIL REFERENCE A38187 !$#authors Casas-Finet, J.R.; Fischer, K.R.; Karpel, R.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:1050-1054 !$#title Structural basis for the nucleic acid binding cooperativity !1of bacteriophage T4 gene 32 protein: the (Lys/Arg)-3(Ser/ !1Thr)-2(LAST) motif. !$#cross-references MUID:92141200; PMID:1736285 !$#contents annotation; LAST motif COMMENT The helix-destabilizing protein binds preferentially to !1single-stranded DNA and, therefore, destabilizes !1double-stranded DNA. This protein is involved in T4 DNA !1replication, repair, and recombination. GENETICS !$#gene 32 !$#map_position 87.1-88.0 CLASSIFICATION #superfamily phage T4 helix-destabilizing protein KEYWORDS DNA binding; zinc finger FEATURE !$3-7 #region LAST motif\ !$110-114 #region LAST motif SUMMARY #length 301 #molecular-weight 33506 #checksum 5466 SEQUENCE /// ENTRY DDBP36 #type fragment TITLE helix-destabilizing protein - phage T6 (fragment) ALTERNATE_NAMES gene 32 protein; single-stranded DNA-binding protein ORGANISM #formal_name phage T6 DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 23-Mar-1995 ACCESSIONS S02263 REFERENCE S01437 !$#authors McPheeters, D.S.; Gosch, G.; Gold, L. !$#journal Nucleic Acids Res. (1988) 16:9341 !$#title Nucleotide sequences of the bacteriophage T2 and T6 gene 32 !1mRNAs. !$#cross-references MUID:89016637; PMID:3262868 !$#accession S02263 !'##molecule_type mRNA !'##residues 1-293 ##label MCP !'##cross-references EMBL:X12460 GENETICS !$#gene 32 CLASSIFICATION #superfamily phage T4 helix-destabilizing protein KEYWORDS DNA binding; zinc finger FEATURE !$3-7 #region LAST motif\ !$111-115 #region LAST motif SUMMARY #length 293 #checksum 7492 SEQUENCE /// ENTRY DDBPT7 #type complete TITLE helix-destabilizing protein - phage T7 ORGANISM #formal_name phage T7 DATE 01-Sep-1981 #sequence_revision 01-Sep-1981 #text_change 23-Jul-1999 ACCESSIONS F94615; G92866; S42299; A04318 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession F94615 !'##molecule_type DNA !'##residues 1-232 ##label DU1 REFERENCE A92866 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1981) 148:303-330 !$#title Nucleotide sequence from the genetic left end of !1bacteriophage T7 DNA to the beginning of gene 4. !$#cross-references MUID:82078034; PMID:7310871 !$#accession G92866 !'##molecule_type DNA !'##residues 1-232 ##label DU2 !'##cross-references GB:V01127; NID:g15498; PIDN:CAA24343.1; PID:g15515 REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42299 !'##molecule_type DNA !'##residues 1-232 ##label DUN !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24400.1; !1PID:g15579 !'##note the authors did not translate the codon for residue 1 COMMENT Helix-destabilizing protein, which is expressed in the late !1stage of lytic development, binds preferentially to !1single-stranded DNA. GENETICS !$#gene 2.5 !$#map_position 22.90-24.64 CLASSIFICATION #superfamily phage T7 helix-destabilizing protein KEYWORDS DNA binding SUMMARY #length 232 #molecular-weight 25693 #checksum 329 SEQUENCE /// ENTRY NDBPXL #type complete TITLE exonuclease (EC 3.1.-.-) - phage lambda ORGANISM #formal_name phage lambda DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS H94614; A43012; A04319 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession H94614 !'##molecule_type DNA !'##residues 1-226 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession A43012 !'##molecule_type DNA !'##residues 1-226 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96569.1; PID:g215137 COMMENT Exonuclease functions in general recombination and the late, !1rolling-circle mode of lambda DNA replication. GENETICS !$#gene exo; red-X; red-alpha !$#map_position 66.03-64.64 CLASSIFICATION #superfamily phage lambda exonuclease KEYWORDS exonuclease; hydrolase SUMMARY #length 226 #molecular-weight 25908 #checksum 7665 SEQUENCE /// ENTRY QBBPL #type complete TITLE recombination protein bet - phage lambda ORGANISM #formal_name phage lambda DATE 02-Apr-1982 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS B94164; B43012; C93737; A04320 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession B94164 !'##molecule_type DNA !'##residues 1-261 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession B43012 !'##molecule_type DNA !'##residues 1-261 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96570.1; PID:g215138 REFERENCE A93737 !$#authors Ineichen, K.; Shepherd, J.C.W.; Bickle, T.A. !$#journal Nucleic Acids Res. (1981) 9:4639-4653 !$#title The DNA sequence of the phage lambda genome between P-L and !1the gene bet. !$#cross-references MUID:82059489; PMID:6458018 !$#accession C93737 !'##molecule_type DNA !'##residues 1-102 ##label INE COMMENT Gene bet protein functions in general recombination and in !1the late, rolling-circle mode of lambda DNA replication. GENETICS !$#gene bet; beta; red-beta !$#map_position 67.65-66.03 CLASSIFICATION #superfamily phage lambda recombination protein bet KEYWORDS DNA binding SUMMARY #length 261 #molecular-weight 29688 #checksum 9417 SEQUENCE /// ENTRY RGBPP1 #type complete TITLE recombinase - phage P1 ORGANISM #formal_name phage P1 #note host Escherichia coli DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 23-Jul-1999 ACCESSIONS B24836 REFERENCE A92923 !$#authors Sternberg, N.; Sauer, B.; Hoess, R.; Abremski, K. !$#journal J. Mol. Biol. (1986) 187:197-212 !$#title Bacteriophage P1 cre gene and its regulatory region. !1Evidence for multiple promoters and for regulation by DNA !1methylation. !$#cross-references MUID:86200206; PMID:3486297 !$#accession B24836 !'##molecule_type DNA !'##residues 1-343 ##label STE !'##cross-references GB:X03453; NID:g15135; PIDN:CAA27178.1; PID:g15137 GENETICS !$#gene cre CLASSIFICATION #superfamily phage P1 recombinase KEYWORDS DNA recombination SUMMARY #length 343 #molecular-weight 38540 #checksum 8677 SEQUENCE /// ENTRY C4BPP1 #type complete TITLE gene c4 protein - phage P1 ALTERNATE_NAMES repressor protein c4 ORGANISM #formal_name phage P1 #note host Escherichia coli DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 23-Jul-1999 ACCESSIONS A27528; S04260 REFERENCE A27528 !$#authors Baumstark, B.R.; Scott, J.R. !$#journal Virology (1987) 156:197-203 !$#title The c4 gene of phage P1. !$#cross-references MUID:87122161; PMID:3811234 !$#accession A27528 !'##molecule_type DNA !'##residues 1-66 ##label BAU !'##cross-references GB:M16568; NID:g215603; PIDN:AAA32417.1; !1PID:g215604 REFERENCE S04260 !$#authors Hansen, E.B. !$#journal J. Mol. Biol. (1989) 207:135-149 !$#title Structure and regulation of the lytic replicon of phage P1. !$#cross-references MUID:89293847; PMID:2661831 !$#accession S04260 !'##molecule_type DNA !'##residues 1-66 ##label HAN !'##cross-references GB:X15639; NID:g15739; PIDN:CAA33658.1; PID:g15740 GENETICS !$#gene c4 CLASSIFICATION #superfamily phage P1 gene c4 protein KEYWORDS DNA binding; repressor; transcription regulation SUMMARY #length 66 #molecular-weight 7312 #checksum 1376 SEQUENCE /// ENTRY CSBPP1 #type fragment TITLE gene 16 protein - phage P1 (fragment) ORGANISM #formal_name phage P1 DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 23-Jul-1999 ACCESSIONS PS0109 REFERENCE PS0109 !$#authors Guidolin, A.; Zingg, J.M.; Arber, W. !$#journal Gene (1989) 76:239-243 !$#title Organization of the bacteriophage P1 tail-fibre operon. !$#cross-references MUID:89326122; PMID:2526777 !$#accession PS0109 !'##molecule_type DNA !'##residues 1-166 ##label GUI !'##cross-references GB:M25470; NID:g341349; PIDN:AAA58776.1; !1PID:g538420 GENETICS !$#gene 16 CLASSIFICATION #superfamily phage P1 gene 16 protein SUMMARY #length 166 #checksum 6269 SEQUENCE /// ENTRY TPBPP1 #type complete TITLE tail fiber protein R - phage P1 ORGANISM #formal_name phage P1 DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 23-Jul-1999 ACCESSIONS JS0460 REFERENCE PS0109 !$#authors Guidolin, A.; Zingg, J.M.; Arber, W. !$#journal Gene (1989) 76:239-243 !$#title Organization of the bacteriophage P1 tail-fibre operon. !$#cross-references MUID:89326122; PMID:2526777 !$#accession JS0460 !'##molecule_type DNA !'##residues 1-144 ##label GUI !'##cross-references GB:M25470; NID:g341349; PIDN:AAA58777.1; !1PID:g538421 GENETICS !$#gene R CLASSIFICATION #superfamily phage P1 tail fiber protein R KEYWORDS tail fiber SUMMARY #length 144 #molecular-weight 15974 #checksum 1200 SEQUENCE /// ENTRY MFBPP1 #type fragment TITLE major tail fiber protein S - phage P1 (fragment) ORGANISM #formal_name phage P1 DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 30-Jun-1993 ACCESSIONS PS0110 REFERENCE PS0109 !$#authors Guidolin, A.; Zingg, J.M.; Arber, W. !$#journal Gene (1989) 76:239-243 !$#title Organization of the bacteriophage P1 tail-fibre operon. !$#cross-references MUID:89326122; PMID:2526777 !$#accession PS0110 !'##molecule_type DNA !'##residues 1-247 ##label GUI !'##cross-references GB:M25470 GENETICS !$#gene S CLASSIFICATION #superfamily phage P1 major tail fiber protein S KEYWORDS tail fiber SUMMARY #length 247 #checksum 436 SEQUENCE /// ENTRY ATBPP1 #type complete TITLE antirepressor protein 1 - phage P1 ALTERNATE_NAMES rebA protein; rebB protein CONTAINS antirepressor protein 1; antirepressor protein 2 ORGANISM #formal_name phage P1 DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 23-Jul-1999 ACCESSIONS S04261 REFERENCE S04260 !$#authors Hansen, E.B. !$#journal J. Mol. Biol. (1989) 207:135-149 !$#title Structure and regulation of the lytic replicon of phage P1. !$#cross-references MUID:89293847; PMID:2661831 !$#accession S04261 !'##molecule_type DNA !'##residues 1-322 ##label HAN !'##cross-references EMBL:X15639; NID:g15739; PIDN:CAA33659.1; !1PID:g15741 GENETICS !$#gene ant1; rebB; ant2; rebA !$#map_position 53 map units CLASSIFICATION #superfamily phage P1 ant1 protein KEYWORDS alternative initiators; DNA binding FEATURE !$1-322 #product antirepressor protein 1 #status predicted !8#label MAT1\ !$84-322 #product antirepressor protein 2 #status predicted !8#label MAT2 SUMMARY #length 322 #molecular-weight 35994 #checksum 8035 SEQUENCE /// ENTRY KIBPP1 #type complete TITLE kilA protein - phage P1 ORGANISM #formal_name phage P1 DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 23-Jul-1999 ACCESSIONS S04262; S04258; S06803 REFERENCE S04260 !$#authors Hansen, E.B. !$#journal J. Mol. Biol. (1989) 207:135-149 !$#title Structure and regulation of the lytic replicon of phage P1. !$#cross-references MUID:89293847; PMID:2661831 !$#accession S04262 !'##molecule_type DNA !'##residues 1-266 ##label HAN !'##cross-references EMBL:X15639; NID:g15739; PIDN:CAA33661.1; !1PID:g15743 REFERENCE S04258 !$#authors Sternberg, N.; Cohen, G. !$#journal J. Mol. Biol. (1989) 207:111-133 !$#title Genetic analysis of the lytic replicon of bacteriophage P1. !1II. Organization of replicon elements. !$#cross-references MUID:89293846; PMID:2661830 !$#accession S04258 !'##molecule_type DNA !'##residues 1-266 ##label STE !'##cross-references EMBL:X15638; NID:g15735; PIDN:CAA33655.1; !1PID:g15736 REFERENCE S06803 !$#authors Heisig, A.; Riedel, H.D.; Dobrinski, B.; Lurz, R.; Schuster, !1H. !$#journal J. Mol. Biol. (1989) 209:525-538 !$#title Organization of the immunity region immI of bacteriophage P1 !1and synthesis of the P1 antirepressor. !$#cross-references MUID:90064513; PMID:2585500 !$#accession S06803 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 6-164 ##label HEI GENETICS !$#gene kilA; ant1 !$#map_position 53 map units CLASSIFICATION #superfamily phage P1 kilA protein KEYWORDS DNA binding SUMMARY #length 266 #molecular-weight 29576 #checksum 7364 SEQUENCE /// ENTRY A60478 #type complete TITLE ref protein - phage P1 ORGANISM #formal_name phage P1 #note host Escherichia coli DATE 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 23-Jul-1999 ACCESSIONS A60478 REFERENCE A60478 !$#authors Lu, S.D.; Lu, D.; Gottesman, M. !$#journal J. Bacteriol. (1989) 171:3427-3432 !$#title Stimulation of IS1 excision by bacteriophage P1 ref !1function. !$#cross-references MUID:89255114; PMID:2542224 !$#accession A60478 !'##molecule_type DNA !'##residues 1-186 ##label LUS !'##cross-references GB:M27041; NID:g215650; PIDN:AAA32422.1; !1PID:g215651 GENETICS !$#gene ref CLASSIFICATION #superfamily phage P1 ref protein SUMMARY #length 186 #molecular-weight 21329 #checksum 5333 SEQUENCE /// ENTRY RLBPP1 #type complete TITLE repL protein - phage P1 ORGANISM #formal_name phage P1 DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 23-Jul-1999 ACCESSIONS S04263; S04259 REFERENCE S04260 !$#authors Hansen, E.B. !$#journal J. Mol. Biol. (1989) 207:135-149 !$#title Structure and regulation of the lytic replicon of phage P1. !$#cross-references MUID:89293847; PMID:2661831 !$#accession S04263 !'##molecule_type DNA !'##residues 1-281 ##label HAN !'##cross-references EMBL:X15639; NID:g15739; PIDN:CAA33662.1; !1PID:g15744 REFERENCE S04258 !$#authors Sternberg, N.; Cohen, G. !$#journal J. Mol. Biol. (1989) 207:111-133 !$#title Genetic analysis of the lytic replicon of bacteriophage P1. !1II. Organization of replicon elements. !$#cross-references MUID:89293846; PMID:2661830 !$#accession S04259 !'##molecule_type DNA !'##residues 1-281 ##label STE !'##cross-references EMBL:X15638; NID:g15735; PIDN:CAA33656.1; !1PID:g15737 !'##note it is uncertain whether Met-1 or Met-13 is the initiator GENETICS !$#gene repL !$#map_position 53 map units CLASSIFICATION #superfamily phage P1 repL protein SUMMARY #length 281 #molecular-weight 30857 #checksum 6596 SEQUENCE /// ENTRY XSSOP5 #type complete TITLE excisionase - Streptococcus pneumoniae transposon Tn1545 ORGANISM #formal_name Streptococcus pneumoniae DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 23-Jul-1999 ACCESSIONS S05385 REFERENCE S05385 !$#authors Poyart-Salmeron, C.; Trieu-Cuot, P.; Carlier, C.; Courvalin, !1P. !$#journal EMBO J. (1989) 8:2425-2433 !$#title Molecular characterization of two proteins involved in the !1excision of the conjugative transposon Tn1545: homologies !1with other site-specific recombinases. !$#cross-references MUID:90005451; PMID:2551683 !$#accession S05385 !'##molecule_type DNA !'##residues 1-67 ##label POY !'##cross-references EMBL:X61025; NID:g47461; PIDN:CAA43359.1; !1PID:g47462 GENETICS !$#gene xis CLASSIFICATION #superfamily transposon Tn1545 excisionase KEYWORDS DNA excision SUMMARY #length 67 #molecular-weight 8110 #checksum 9590 SEQUENCE /// ENTRY RSBPXL #type complete TITLE excisionase - phage lambda ORGANISM #formal_name phage lambda DATE 31-Oct-1980 #sequence_revision 23-Oct-1981 #text_change 23-Jul-1999 ACCESSIONS C94164; C43012; A93699; A93844; A04321 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession C94164 !'##molecule_type DNA !'##residues 1-72 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession C43012 !'##molecule_type DNA !'##residues 1-72 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96563.1; PID:g215134 REFERENCE A93699 !$#authors Davies, R.W. !$#journal Nucleic Acids Res. (1980) 8:1765-1782 !$#title DNA sequence of the int-xis P--I region of the bacteriophage !1lambda; overlap of the int xis genes. !$#cross-references MUID:81053845; PMID:6253947 !$#accession A93699 !'##molecule_type DNA !'##residues 1-72 ##label DAV !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96563.1; PID:g215134 REFERENCE A93844 !$#authors Hoess, R.H.; Foeller, C.; Bidwell, K.; Landy, A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1980) 77:2482-2486 !$#title Site-specific recombination functions of bacteriophage !1lambda: DNA sequence of regulatory regions and overlapping !1structural genes for Int and Xis. !$#cross-references MUID:80234646; PMID:6446713 !$#accession A93844 !'##molecule_type DNA !'##residues 1-72 ##label HOE !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96563.1; PID:g215134 COMMENT Excisionase and lambda integrase are necessary for the !1excision of prophage lambda from the host genome by !1site-specific recombination at the att site. GENETICS !$#gene xis !$#map_position 59.95-59.51 CLASSIFICATION #superfamily phage lambda excisionase KEYWORDS DNA binding SUMMARY #length 72 #molecular-weight 8605 #checksum 7873 SEQUENCE /// ENTRY RSBPX8 #type complete TITLE excisionase - phage phi-80 ORGANISM #formal_name phage phi-80 #note host Escherichia coli DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 23-Jul-1999 ACCESSIONS B24253 REFERENCE A92928 !$#authors Leong, J.M.; Nunes-Duby, S.E.; Oser, A.B.; Lesser, C.F.; !1Youderian, P.; Susskind, M.M.; Landy, A. !$#journal J. Mol. Biol. (1986) 189:603-616 !$#title Structural and regulatory divergence among site-specific !1recombination genes of lambdoid phage. !$#cross-references MUID:87060955; PMID:3491212 !$#accession B24253 !'##molecule_type DNA !'##residues 1-65 ##label LEO !'##cross-references GB:X04051; NID:g15770; PIDN:CAA27684.1; PID:g15772 GENETICS !$#gene xis CLASSIFICATION #superfamily phage phi-80 excisionase KEYWORDS DNA binding; DNA excision SUMMARY #length 65 #molecular-weight 7740 #checksum 1556 SEQUENCE /// ENTRY RSBPXP #type complete TITLE excisionase - phage P22 ORGANISM #formal_name phage P22 #note host Salmonella typhimurium DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 23-Jul-1999 ACCESSIONS D24253 REFERENCE A92928 !$#authors Leong, J.M.; Nunes-Duby, S.E.; Oser, A.B.; Lesser, C.F.; !1Youderian, P.; Susskind, M.M.; Landy, A. !$#journal J. Mol. Biol. (1986) 189:603-616 !$#title Structural and regulatory divergence among site-specific !1recombination genes of lambdoid phage. !$#cross-references MUID:87060955; PMID:3491212 !$#accession D24253 !'##molecule_type DNA !'##residues 1-116 ##label LEO !'##cross-references GB:X04052; NID:g15641; PIDN:CAA27686.1; PID:g15643 GENETICS !$#gene xis CLASSIFICATION #superfamily phage P22 excisionase KEYWORDS DNA binding; DNA excision SUMMARY #length 116 #molecular-weight 12754 #checksum 4535 SEQUENCE /// ENTRY JC4118 #type complete TITLE probable site-specific integrase - phage Cf1t ALTERNATE_NAMES ORF344 ORGANISM #formal_name phage Cf1t DATE 26-Jul-1995 #sequence_revision 07-Jun-1996 #text_change 23-Jul-1999 ACCESSIONS JC4118 REFERENCE JC4118 !$#authors Shieh, G.J.; Lin, C.H.; Kuo, J.L.; Kuo, T.T. !$#journal Gene (1995) 158:73-76 !$#title Characterization of an open reading frame involved in !1site-specific integration of filamentous phage Cf1t from !1Xanthomonas campestris pv. citri. !$#cross-references MUID:95309728; PMID:7789813 !$#accession JC4118 !'##molecule_type DNA !'##residues 1-344 ##label SHI !'##cross-references GB:U08370; NID:g483848; PIDN:AAA83412.1; !1PID:g483849 COMMENT This gene was shown by site-directed mutagenesis to be !1required for integration activity. The lack of apparent !1homology to other know integrases suggests a novel !1mechanism. COMMENT This phage was isolated from Xanthomonas campestris pv. !1citri, a pathogenic bacterium that causes citrus canker !1disease in orange. GENETICS !$#start_codon GTG CLASSIFICATION #superfamily phage Cf1t integrase KEYWORDS site-specific integration SUMMARY #length 344 #molecular-weight 38790 #checksum 8326 SEQUENCE /// ENTRY RSBPIL #type complete TITLE integrase - phage lambda ORGANISM #formal_name phage lambda DATE 31-Oct-1980 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS A04322; B04322; C04322; D04322 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession A04322 !'##molecule_type DNA !'##residues 1-356 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession B04322 !'##molecule_type DNA !'##residues 1-356 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96562.1; PID:g215133 REFERENCE A93844 !$#authors Hoess, R.H.; Foeller, C.; Bidwell, K.; Landy, A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1980) 77:2482-2486 !$#title Site-specific recombination functions of bacteriophage !1lambda: DNA sequence of regulatory regions and overlapping !1structural genes for Int and Xis. !$#cross-references MUID:80234646; PMID:6446713 !$#accession C04322 !'##molecule_type DNA !'##residues 1-356 ##label HOE !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96562.1; PID:g215133 REFERENCE A93699 !$#authors Davies, R.W. !$#journal Nucleic Acids Res. (1980) 8:1765-1782 !$#title DNA sequence of the int-xis P--I region of the bacteriophage !1lambda; overlap of the int xis genes. !$#cross-references MUID:81053845; PMID:6253947 !$#accession D04322 !'##molecule_type DNA !'##residues 1-117,'V',119-356 ##label DAV COMMENT Integrase is necessary for integration of lambda into the !1host genome by site-specific recombination at the att site. !1In conjunction with lambda excisionase, integrase is also !1necessary for excision of prophage lambda from the host !1genome. GENETICS !$#gene int !$#map_position 59.55-57.35 (Lambda) CLASSIFICATION #superfamily phage lambda integrase SUMMARY #length 356 #molecular-weight 40304 #checksum 8190 SEQUENCE /// ENTRY RSBPI8 #type complete TITLE probable integrase - phage phi-80 ORGANISM #formal_name phage phi-80 #note host Escherichia coli DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 30-Sep-1993 ACCESSIONS A24253 REFERENCE A92928 !$#authors Leong, J.M.; Nunes-Duby, S.E.; Oser, A.B.; Lesser, C.F.; !1Youderian, P.; Susskind, M.M.; Landy, A. !$#journal J. Mol. Biol. (1986) 189:603-616 !$#title Structural and regulatory divergence among site-specific !1recombination genes of lambdoid phage. !$#cross-references MUID:87060955; PMID:3491212 !$#accession A24253 !'##molecule_type DNA !'##residues 1-402 ##label LEO GENETICS !$#gene int CLASSIFICATION #superfamily phage phi-80 integrase KEYWORDS DNA integration SUMMARY #length 402 #molecular-weight 46745 #checksum 7352 SEQUENCE /// ENTRY IMBPSB #type complete TITLE immunity protein - phage SP-beta ORGANISM #formal_name phage SP-beta #note host Bacillus subtilis DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 31-Oct-1997 ACCESSIONS A24499 REFERENCE A24499 !$#authors McLaughlin, J.R.; Wong, H.C.; Ting, Y.E.; Van Arsdell, J.N.; !1Chang, S. !$#journal J. Bacteriol. (1986) 167:952-959 !$#title Control of lysogeny and immunity of Bacillus subtilis !1temperate bacteriophage SP-beta by its d gene. !$#cross-references MUID:86304188; PMID:3091583 !$#accession A24499 !'##molecule_type DNA !'##residues 1-201 ##label MCL !'##cross-references GB:M13821 GENETICS !$#gene d CLASSIFICATION #superfamily phage SP-beta immunity protein KEYWORDS immunity protein SUMMARY #length 201 #molecular-weight 22118 #checksum 9651 SEQUENCE /// ENTRY RPBPF5 #type complete TITLE immunity repressor protein - Bacillus phage phi-105 ORGANISM #formal_name Bacillus phage phi-105 #note host Bacillus subtilis DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 16-Jun-2000 ACCESSIONS A93579; A91535; S02459; T13543; A24339; A24521 REFERENCE A93579 !$#authors Dhaese, P.; Seurinck, J.; De Smet, B.; Van Montagu, M. !$#journal Nucleic Acids Res. (1985) 13:5441-5455 !$#title Nucleotide sequence and mutational analysis of an immunity !1repressor gene from Bacillus subtilis temperate phage !1phi-105. !$#cross-references MUID:85297750; PMID:2993999 !$#accession A93579 !'##molecule_type DNA !'##residues 1-147 ##label DHA !'##cross-references GB:X02799; NID:g15455; PIDN:CAA26567.1; PID:g579178 REFERENCE A91535 !$#authors Cully, D.F.; Garro, A.J. !$#journal Gene (1985) 38:153-164 !$#title Nucleotide sequence of the immunity region of Bacillus !1subtilis bacteriophage phi-105: identification of the !1repressor gene and its mRNA and protein products. !$#cross-references MUID:86056972; PMID:3934047 !$#accession A91535 !'##molecule_type DNA !'##residues 1-147 ##label CUL REFERENCE S02459 !$#authors van Kaer, L.; Gansemans, Y.; van Montagu, M.; Dhaese, P. !$#journal EMBO J. (1988) 7:859-866 !$#title Interaction of the Bacillus subtilis phage phi105 repressor !1with operator DNA: a genetic analysis. !$#cross-references MUID:88283656; PMID:3135184 !$#accession S02459 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 4-147 ##label VAN !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing REFERENCE Z17688 !$#authors Kobayashi, K.; Okamura, K.; Inoue, T.; Sato, T.; Kobayashi, !1Y. !$#submission submitted to the EMBL Data Library, July 1998 !$#description Complete nucleotide sequence of Bacillus subtilis phage !1phi-105. !$#accession T13543 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 4-147 ##label KOB !'##cross-references EMBL:AB016282; PIDN:BAA36660.1 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily phage phi-105 immunity repressor protein KEYWORDS DNA binding; early protein; repressor; transcription !1regulation SUMMARY #length 147 #molecular-weight 16877 #checksum 2117 SEQUENCE /// ENTRY IMBP2 #type complete TITLE immunity region protein 2 - Bacillus phage phi-105 ORGANISM #formal_name Bacillus phage phi-105 #note host Bacillus subtilis DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 16-Jun-2000 ACCESSIONS B24521; B24339; T13542 REFERENCE A91535 !$#authors Cully, D.F.; Garro, A.J. !$#journal Gene (1985) 38:153-164 !$#title Nucleotide sequence of the immunity region of Bacillus !1subtilis bacteriophage phi-105: identification of the !1repressor gene and its mRNA and protein products. !$#cross-references MUID:86056972; PMID:3934047 !$#accession B24521 !'##molecule_type DNA !'##residues 1-158 ##label CUL !'##cross-references GB:M11920 REFERENCE A93579 !$#authors Dhaese, P.; Seurinck, J.; De Smet, B.; Van Montagu, M. !$#journal Nucleic Acids Res. (1985) 13:5441-5455 !$#title Nucleotide sequence and mutational analysis of an immunity !1repressor gene from Bacillus subtilis temperate phage !1phi-105. !$#cross-references MUID:85297750; PMID:2993999 !$#accession B24339 !'##molecule_type DNA !'##residues 1-158 ##label DHA !'##cross-references GB:X02799; NID:g15455; PIDN:CAA26568.1; PID:g15457 REFERENCE Z17688 !$#authors Kobayashi, K.; Okamura, K.; Inoue, T.; Sato, T.; Kobayashi, !1Y. !$#submission submitted to the EMBL Data Library, July 1998 !$#description Complete nucleotide sequence of Bacillus subtilis phage !1phi-105. !$#accession T13542 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 'M',12-158 ##label KOB !'##cross-references EMBL:AB016282; PIDN:BAA36659.1 CLASSIFICATION #superfamily phage phi-105 immunity region protein 2 KEYWORDS early protein SUMMARY #length 158 #molecular-weight 18406 #checksum 7695 SEQUENCE /// ENTRY IMBP4 #type complete TITLE site-specific recombinase for integration and excision - Bacillus phage phi-105 ALTERNATE_NAMES immunity region protein 3, 4, 5, 6 ORGANISM #formal_name Bacillus phage phi-105 DATE 31-Dec-1988 #sequence_revision 22-Oct-1999 #text_change 16-Jun-2000 ACCESSIONS T13541; C24521; D24521; E24521; F24521 REFERENCE Z17688 !$#authors Kobayashi, K.; Okamura, K.; Inoue, T.; Sato, T.; Kobayashi, !1Y. !$#submission submitted to the EMBL Data Library, July 1998 !$#description Complete nucleotide sequence of Bacillus subtilis phage !1phi-105. !$#accession T13541 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-474 ##label KOB !'##cross-references EMBL:AB016282; PIDN:BAA36658.1 REFERENCE A91535 !$#authors Cully, D.F.; Garro, A.J. !$#journal Gene (1985) 38:153-164 !$#title Nucleotide sequence of the immunity region of Bacillus !1subtilis bacteriophage phi-105: identification of the !1repressor gene and its mRNA and protein products. !$#cross-references MUID:86056972; PMID:3934047 !$#accession C24521 !'##molecule_type DNA !'##residues 1-78,'MTHC' ##label CUL !'##cross-references GB:M11920; NID:g215477; PIDN:AAA88399.1; !1PID:g1196717 !$#accession D24521 !'##molecule_type DNA !'##residues 149-160,'AR',163,'H','HSDSQRRVR',381-383,'RIQRRARS',392 !1##label CU2 !'##cross-references GB:M11920; NID:g215477; PIDN:AAA88401.1; !1PID:g1196719 !$#accession E24521 !'##molecule_type DNA !'##residues 189-318,'HAP' ##label CU3 !'##cross-references GB:M11920 !$#accession F24521 !'##molecule_type DNA !'##residues 'MP',319-376,'RNTK',381,'PGPWS' ##label CU4 !'##cross-references GB:M11920 CLASSIFICATION #superfamily phage phi-105 site-specific recombinase KEYWORDS early protein SUMMARY #length 474 #molecular-weight 55472 #checksum 4887 SEQUENCE /// ENTRY RSSOP5 #type complete TITLE integrase - Streptococcus pneumoniae transposon Tn1545 ORGANISM #formal_name Streptococcus pneumoniae DATE 30-Jun-1992 #sequence_revision 30-Jun-1992 #text_change 23-Jul-1999 ACCESSIONS S05386 REFERENCE S05385 !$#authors Poyart-Salmeron, C.; Trieu-Cuot, P.; Carlier, C.; Courvalin, !1P. !$#journal EMBO J. (1989) 8:2425-2433 !$#title Molecular characterization of two proteins involved in the !1excision of the conjugative transposon Tn1545: homologies !1with other site-specific recombinases. !$#cross-references MUID:90005451; PMID:2551683 !$#accession S05386 !'##molecule_type DNA !'##residues 1-405 ##label POY !'##cross-references EMBL:X61025; NID:g47461; PIDN:CAA43360.1; !1PID:g47463 GENETICS !$#gene int CLASSIFICATION #superfamily transposon Tn1545 integrase KEYWORDS DNA integration SUMMARY #length 405 #molecular-weight 47022 #checksum 5712 SEQUENCE /// ENTRY H70799 #type complete TITLE integrase-related protein - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H70799 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession H70799 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-71 ##label COL !'##cross-references GB:AL022121; GB:AL123456; NID:g3261559; !1PIDN:CAA18073.1; PID:g2960175 !'##experimental_source strain H37Rv GENETICS !$#gene Rv3751 CLASSIFICATION #superfamily Mycobacterium tuberculosis integrase-related !1protein SUMMARY #length 71 #molecular-weight 7584 #checksum 1481 SEQUENCE /// ENTRY RSBPP4 #type complete TITLE integrase - satellite phage P4 ORGANISM #formal_name satellite phage P4 #note host Escherichia coli DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 23-Jul-1999 ACCESSIONS JW0023; S00577 REFERENCE JW0020 !$#authors Halling, C.; Calendar, R.; Christie, G.E.; Dale, E.C.; Deho, !1G.; Finkel, S.; Flensburg, J.; Ghisotti, D.; Kahn, M.L.; !1Lane, K.B.; Lin, C.S.; Lindqvist, B.H.; Pierson III, L.S.; !1Six, E.W.; Sunshine, M.G.; Ziermann, R. !$#journal Nucleic Acids Res. (1990) 18:1649 !$#title DNA sequence of satellite bacteriophage P4. !$#cross-references MUID:90221913; PMID:2183201 !$#accession JW0023 !'##molecule_type DNA !'##residues 1-440 ##label HAL !'##cross-references GB:X51522 REFERENCE S00576 !$#authors Pierson, L.S.; Kahn, M.L. !$#journal J. Mol. Biol. (1987) 196:487-496 !$#title Integration of satellite bacteriophage P4 in Escherichia !1coli. DNA sequences of the phage and host regions involved !1in site-specific recombination. !$#cross-references MUID:88062688; PMID:3119856 !$#accession S00577 !'##molecule_type DNA !'##residues 1-440 ##label PIE !'##cross-references EMBL:X05947; NID:g15175; PIDN:CAA29379.1; !1PID:g15176 !'##note the authors translated the codon CAG for residue 11 as Asn, AAA !1for residue 18 as Leu, and AAA for residue 428 as Tyr GENETICS !$#gene int CLASSIFICATION #superfamily satellite phage P4 integrase KEYWORDS DNA integration SUMMARY #length 440 #molecular-weight 50970 #checksum 8978 SEQUENCE /// ENTRY RSBPIP #type complete TITLE integrase - phage P22 ORGANISM #formal_name phage P22 #note host Salmonella typhimurium DATE 30-Sep-1987 #sequence_revision 30-Sep-1987 #text_change 23-Jul-1999 ACCESSIONS C24253 REFERENCE A92928 !$#authors Leong, J.M.; Nunes-Duby, S.E.; Oser, A.B.; Lesser, C.F.; !1Youderian, P.; Susskind, M.M.; Landy, A. !$#journal J. Mol. Biol. (1986) 189:603-616 !$#title Structural and regulatory divergence among site-specific !1recombination genes of lambdoid phage. !$#cross-references MUID:87060955; PMID:3491212 !$#accession C24253 !'##molecule_type DNA !'##residues 1-387 ##label LEO !'##cross-references GB:X04052; NID:g15641; PIDN:CAA27685.1; PID:g15642 GENETICS !$#gene int CLASSIFICATION #superfamily phage P22 integrase KEYWORDS DNA integration SUMMARY #length 387 #molecular-weight 44782 #checksum 4500 SEQUENCE /// ENTRY RSBPHP #type complete TITLE integrase - phage HP1 ORGANISM #formal_name phage HP1 #note host Haemophilus influenzae DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 23-Jul-1999 ACCESSIONS A33857; S69503; S72329 REFERENCE A33857 !$#authors Goodman, S.D.; Scocca, J.J. !$#journal J. Bacteriol. (1989) 171:4232-4240 !$#title Nucleotide sequence and expression of the gene for the !1site-specific integration protein from bacteriophage HP1 of !1Haemophilus influenzae. !$#cross-references MUID:89327135; PMID:2546915 !$#accession A33857 !'##molecule_type DNA !'##residues 1-337 ##label GOO !'##cross-references GB:U24159; GB:U06847; GB:M28366; GB:M12911; !1GB:M22941; GB:M12910; GB:M15313; NID:g1046235; !1PIDN:AAB09182.1; PID:g459175 REFERENCE S69503 !$#authors Esposito, D.; Fitzmaurice, W.P.; Benjamin, R.C.; Goodman, !1S.D.; Waldman, A.S.; Scocca, J.J. !$#journal Nucleic Acids Res. (1996) 24:2360-2368 !$#title The complete nucleotide sequence of bacteriophage HP1 DNA. !$#cross-references MUID:96279738; PMID:8710508 !$#accession S69503 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-337 ##label ESP !'##cross-references EMBL:U24159; NID:g1046235; PIDN:AAB09182.1; !1PID:g459175 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1995 REFERENCE S72329 !$#authors Esposito, D.; Scocca, J.J. !$#journal Mol. Microbiol. (1994) 13:685-695 !$#title Identification of an HP1 phage protein required for !1site-specific excision. !$#cross-references MUID:95089704; PMID:7997180 !$#accession S72329 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-337 ##label ES2 !'##cross-references GB:U24159; EMBL:U06847; NID:g1046235; !1PIDN:AAB09182.1; PID:g459175 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1February 1994 GENETICS !$#gene int CLASSIFICATION #superfamily phage P22 integrase KEYWORDS DNA integration SUMMARY #length 337 #molecular-weight 38598 #checksum 6966 SEQUENCE /// ENTRY RSBPL5 #type complete TITLE integrase - Staphylococcus phage L54a ORGANISM #formal_name Staphylococcus phage L54a #note host Staphylococcus aureus DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 23-Jul-1999 ACCESSIONS A33855 REFERENCE A33855 !$#authors Ye, Z.H.; Lee, C.Y. !$#journal J. Bacteriol. (1989) 171:4146-4153 !$#title Nucleotide sequence and genetic characterization of !1staphylococcal bacteriophage L54a int and xis genes. !$#cross-references MUID:89327124; PMID:2526804 !$#accession A33855 !'##molecule_type DNA !'##residues 1-59 ##label YEZ !'##cross-references GB:M27965; NID:g215096; PIDN:AAA98160.1; !1PID:g455285 GENETICS !$#gene int CLASSIFICATION #superfamily phage L54a integrase KEYWORDS DNA binding; DNA integration SUMMARY #length 59 #molecular-weight 7199 #checksum 6529 SEQUENCE /// ENTRY RSXFF3 #type complete TITLE integrase homolog - frog virus 3 ORGANISM #formal_name frog virus 3, FV3 #note host Rana pipiens (northern leopard frog) DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 23-Jul-1999 ACCESSIONS A40823 REFERENCE A40823 !$#authors Rohozinski, J.; Goorha, R. !$#journal Virology (1992) 186:693-700 !$#title A frog virus 3 gene codes for a protein containing the motif !1characteristic of the INT family of integrases. !$#cross-references MUID:92124744; PMID:1733108 !$#accession A40823 !'##molecule_type DNA !'##residues 1-275 ##label ROH !'##cross-references GB:M80548; NID:g325389; PIDN:AAA73142.1; !1PID:g325390 CLASSIFICATION #superfamily frog virus 3 integrase KEYWORDS DNA integration SUMMARY #length 275 #molecular-weight 29943 #checksum 6051 SEQUENCE /// ENTRY XSBPL5 #type complete TITLE excisionase - Staphylococcus phage L54a ORGANISM #formal_name Staphylococcus phage L54a #note host Staphylococcus aureus DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 23-Jul-1999 ACCESSIONS B33855 REFERENCE A33855 !$#authors Ye, Z.H.; Lee, C.Y. !$#journal J. Bacteriol. (1989) 171:4146-4153 !$#title Nucleotide sequence and genetic characterization of !1staphylococcal bacteriophage L54a int and xis genes. !$#cross-references MUID:89327124; PMID:2526804 !$#accession B33855 !'##molecule_type DNA !'##residues 1-354 ##label YEZ !'##cross-references GB:M27965; NID:g215096; PIDN:AAA98161.1; !1PID:g215098 GENETICS !$#gene xis CLASSIFICATION #superfamily phage L54a excisionase KEYWORDS DNA excision SUMMARY #length 354 #molecular-weight 41018 #checksum 4900 SEQUENCE /// ENTRY MMBPL #type complete TITLE membrane protein lom - phage lambda ORGANISM #formal_name phage lambda DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS E94164; D43012; A04323 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession E94164 !'##molecule_type DNA !'##residues 1-206 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession D43012 !'##molecule_type DNA !'##residues 1-206 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96554.1; PID:g215126 COMMENT Gene lom protein is incorporated into the outer membrane of !1the host during infection. GENETICS !$#gene lom !$#map_position 39.10-40.37 CLASSIFICATION #superfamily phage lambda membrane protein lom SUMMARY #length 206 #molecular-weight 21856 #checksum 921 SEQUENCE /// ENTRY QGBPL #type complete TITLE host-nuclease inhibitor protein gam - phage lambda ORGANISM #formal_name phage lambda DATE 02-Apr-1982 #sequence_revision 02-Apr-1982 #text_change 23-Jul-1999 ACCESSIONS D93737; F94164; E43012; JC1433; A04324 REFERENCE A93737 !$#authors Ineichen, K.; Shepherd, J.C.W.; Bickle, T.A. !$#journal Nucleic Acids Res. (1981) 9:4639-4653 !$#title The DNA sequence of the phage lambda genome between P-L and !1the gene bet. !$#cross-references MUID:82059489; PMID:6458018 !$#accession D93737 !'##molecule_type DNA !'##residues 1-138 ##label INE !'##cross-references GB:V00638; NID:g15060; PIDN:CAA23978.1; PID:g15061 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession F94164 !'##molecule_type DNA !'##residues 1-138 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession E43012 !'##molecule_type DNA !'##residues 1-138 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96571.1; PID:g215139 REFERENCE JC1433 !$#authors Maruyama, I.N.; Brenner, S. !$#journal Gene (1992) 120:135-141 !$#title A selective lambda phage cloning vector with automatic !1excision of the insert in a plasmid. !$#cross-references MUID:93013027; PMID:1327972 !$#accession JC1433 !'##molecule_type DNA !'##residues 1-138 ##label MAR !'##cross-references GB:S46756 COMMENT gam protein inhibits the host recBC-coded nuclease and thus !1promotes the late, rolling-circle mode of lambda DNA !1replication. GENETICS !$#gene gam; gamma !$#map_position 68.52-67.67 CLASSIFICATION #superfamily phage lambda host-nuclease inhibitor protein !1gam SUMMARY #length 138 #molecular-weight 16346 #checksum 2418 SEQUENCE /// ENTRY QABPL #type complete TITLE restriction inhibitor protein ral - phage lambda ORGANISM #formal_name phage lambda DATE 02-Apr-1982 #sequence_revision 02-Apr-1982 #text_change 24-Sep-1999 ACCESSIONS G94164; F43012; E93737; A04325 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession G94164 !'##molecule_type DNA !'##residues 1-66 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession F43012 !'##molecule_type DNA !'##residues 1-66 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96575.1; PID:g215143 REFERENCE A93737 !$#authors Ineichen, K.; Shepherd, J.C.W.; Bickle, T.A. !$#journal Nucleic Acids Res. (1981) 9:4639-4653 !$#title The DNA sequence of the phage lambda genome between P-L and !1the gene bet. !$#cross-references MUID:82059489; PMID:6458018 !$#accession E93737 !'##molecule_type DNA !'##residues 1-66 ##label INE !'##cross-references GB:V00638; NID:g15060; PIDN:CAA23981.1; PID:g15064 COMMENT The ral gene product interferes with the cleavage of lambda !1DNA by E. coli K12 and E. coli B restriction endonucleases. GENETICS !$#gene ral !$#map_position 70.69-70.29 CLASSIFICATION #superfamily phage lambda restriction inhibitor protein ral SUMMARY #length 66 #molecular-weight 7604 #checksum 8102 SEQUENCE /// ENTRY QABP22 #type complete TITLE restriction inhibitor protein ral - phage P22 ORGANISM #formal_name phage P22 #note host Salmonella typhimurium DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 23-Jul-1999 ACCESSIONS S04245 REFERENCE S04245 !$#authors Semerjian, A.V.; Malloy, D.C.; Poteete, A.R. !$#journal J. Mol. Biol. (1989) 207:1-13 !$#title Genetic structure of the bacteriophage P22 P(L) operon. !$#cross-references MUID:89293845; PMID:2738922 !$#accession S04245 !'##molecule_type DNA !'##residues 1-64 ##label SEM !'##cross-references GB:X15637; NID:g15646; PIDN:CAA33647.1; PID:g15647 GENETICS !$#gene ral CLASSIFICATION #superfamily phage lambda restriction inhibitor protein ral SUMMARY #length 64 #molecular-weight 7407 #checksum 5765 SEQUENCE /// ENTRY W1BP22 #type complete TITLE gene 17 protein - phage P22 ORGANISM #formal_name phage P22 DATE 31-Mar-1991 #sequence_revision 30-Sep-1991 #text_change 23-Jul-1999 ACCESSIONS S04246 REFERENCE S04245 !$#authors Semerjian, A.V.; Malloy, D.C.; Poteete, A.R. !$#journal J. Mol. Biol. (1989) 207:1-13 !$#title Genetic structure of the bacteriophage P22 P(L) operon. !$#cross-references MUID:89293845; PMID:2738922 !$#accession S04246 !'##molecule_type DNA !'##residues 1-103 ##label SEM !'##cross-references EMBL:X15637; NID:g15646; PIDN:CAA33650.1; !1PID:g15650 !'##note the authors translated the codon GGT for residue 26 as Gln GENETICS !$#gene 17 CLASSIFICATION #superfamily phage P22 gene 17 protein SUMMARY #length 103 #molecular-weight 12184 #checksum 6135 SEQUENCE /// ENTRY JRBP27 #type complete TITLE bacterial RNA polymerase inhibitor - phage T7 ORGANISM #formal_name phage T7 DATE 01-Sep-1981 #sequence_revision 01-Sep-1981 #text_change 23-Jul-1999 ACCESSIONS G94615; H92866; S42298; A04326 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession G94615 !'##molecule_type DNA !'##residues 1-64 ##label DU1 REFERENCE A92866 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1981) 148:303-330 !$#title Nucleotide sequence from the genetic left end of !1bacteriophage T7 DNA to the beginning of gene 4. !$#cross-references MUID:82078034; PMID:7310871 !$#accession H92866 !'##molecule_type DNA !'##residues 1-64 ##label DU2 !'##cross-references GB:V01127; NID:g15498; PIDN:CAA24342.1; PID:g15514 REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42298 !'##molecule_type DNA !'##residues 1-64 ##label DUN !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24399.1; !1PID:g15578 !'##note the authors did not translate the codon for residue 1 COMMENT Bacterial RNA polymerase inhibitor, which is expressed in !1the late stage of lytic development, is also essential for !1continuous synthesis of T7 DNA and functions in the !1packaging of the viral genome into the mature phage !1particle. GENETICS !$#gene 2 !$#map_position 22.25-22.73 CLASSIFICATION #superfamily bacterial RNA polymerase inhibitor SUMMARY #length 64 #molecular-weight 7175 #checksum 8698 SEQUENCE /// ENTRY QIBPS2 #type complete TITLE uracil-DNA glycosylase inhibitor - phage PBS2 ORGANISM #formal_name phage PBS2 #note host Bacillus subtilis DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 23-Jul-1999 ACCESSIONS A32206 REFERENCE A32206 !$#authors Wang, Z.; Mosbaugh, D.W. !$#journal J. Biol. Chem. (1989) 264:1163-1171 !$#title Uracil-DNA glycosylase inhibitor gene of bacteriophage PBS2 !1encodes a binding protein specific for uracil-DNA !1glycosylase. !$#cross-references MUID:89093103; PMID:2492016 !$#accession A32206 !'##molecule_type DNA !'##residues 1-84 ##label WAN !'##cross-references GB:J04434; NID:g215788; PIDN:AAA91582.1; !1PID:g215789 GENETICS !$#gene ugi CLASSIFICATION #superfamily phage PBS2 uracil-DNA glycosylase inhibitor SUMMARY #length 84 #molecular-weight 9476 #checksum 4450 SEQUENCE /// ENTRY YVBPL #type complete TITLE lysis protein S - phage lambda ORGANISM #formal_name phage lambda DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS H94164; G43012; A04327 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession H94164 !'##molecule_type DNA !'##residues 1-107 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession G43012 !'##molecule_type DNA !'##residues 1-107 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96597.1; PID:g215163 !'##note the lambda DNA sequence is from the standard strain !1lambda-cIindlts857Sam7; this strain contains an amber !1mutation in gene S; the codon TGG for 56-Trp is replaced by !1the termination codon TAG GENETICS !$#gene S !$#map_position 93.16-93.82 CLASSIFICATION #superfamily phage lambda lysis protein S KEYWORDS host cell lysis SUMMARY #length 107 #molecular-weight 11520 #checksum 7803 SEQUENCE /// ENTRY YVBPS2 #type complete TITLE lysis protein S - phage P22 ALTERNATE_NAMES gene 13 protein ORGANISM #formal_name phage P22 DATE 31-Dec-1992 #sequence_revision 31-Dec-1992 #text_change 23-Jul-1999 ACCESSIONS S22903 REFERENCE S22903 !$#authors Rennell, D.; Poteete, A.R. !$#journal Virology (1985) 143:280-289 !$#title Phage P22 lysis genes: nucleotide sequences and functional !1relationships with T4 and lambda genes. !$#cross-references MUID:86045883; PMID:2998005 !$#accession S22903 !'##molecule_type DNA !'##residues 1-108 ##label REN !'##cross-references EMBL:M10997; NID:g215262; PIDN:AAA32265.1; !1PID:g215263 GENETICS !$#gene 13 CLASSIFICATION #superfamily phage lambda lysis protein S KEYWORDS host cell lysis SUMMARY #length 108 #molecular-weight 11682 #checksum 674 SEQUENCE /// ENTRY EYBPL #type complete TITLE endolysin - phage lambda ORGANISM #formal_name phage lambda DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS B04333; H43012; A93400; A04328 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession B04333 !'##molecule_type DNA !'##residues 1-158 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession H43012 !'##molecule_type DNA !'##residues 1-158 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96598.1; PID:g215164 REFERENCE A93400 !$#authors Imada, M.; Tsugita, A. !$#journal Nature New Biol. (1971) 233:230-231 !$#title Amino-acid sequence of lambda phage endolysin. !$#accession A93400 !'##molecule_type protein !'##residues 1-73,75-158 ##label IMA COMMENT Lambda endolysin is necessary for host cell lysis. It !1probably functions as a transglycosylase. GENETICS !$#gene R !$#map_position 93.80-94.77 CLASSIFICATION #superfamily phage lambda endolysin SUMMARY #length 158 #molecular-weight 17825 #checksum 5919 SEQUENCE /// ENTRY JVBPNL #type complete TITLE DNA-packaging protein Nu1 - phage lambda ORGANISM #formal_name phage lambda DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS C04333; I43012; A04329 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession C04333 !'##molecule_type DNA !'##residues 1-181 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession I43012 !'##molecule_type DNA !'##residues 1-181 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96533.1; PID:g215105 !'##note there are two possible initiation sites for gene Nu1 !1translation, the codon for 1-Met as shown and that for !127-Met COMMENT Gene Nu1 protein is involved in the initiation of lambda DNA !1packaging into the prohead. In conjunction with gene A !1protein, it processes replicating concatemeric DNA into !1pieces of unit length with cohesive ends. GENETICS !$#gene Nu1 !$#map_position 0.39-1.51 CLASSIFICATION #superfamily phage lambda DNA packaging protein Nu1 SUMMARY #length 181 #molecular-weight 20441 #checksum 4110 SEQUENCE /// ENTRY JVBPAL #type complete TITLE DNA-packaging protein A - phage lambda ORGANISM #formal_name phage lambda DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS D04333; A92891; A04330 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession D04333 !'##molecule_type DNA !'##residues 1-641 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession A92891 !'##molecule_type DNA !'##residues 1-641 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96534.1; PID:g215106 !'##note there are five possible initiation sites for gene A !1translation, the GTG codon for 1-Met as shown, the ATG !1codons for 61-Met and 64-Met, and the GTG codons !1corresponding to 74-Val and 75-Val COMMENT Gene A protein is involved in the initiation of lambda DNA !1packaging into the prohead. In conjunction with gene Nu1 !1protein, it processes replicating concatemeric DNA into !1pieces of unit length with cohesive ends. GENETICS !$#gene A !$#map_position 1.47-5.43 !$#start_codon GTG CLASSIFICATION #superfamily phage lambda DNA packaging protein A SUMMARY #length 641 #molecular-weight 73301 #checksum 6241 SEQUENCE /// ENTRY JVBPFL #type complete TITLE DNA-packaging protein FI - phage lambda ORGANISM #formal_name phage lambda DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS E04333; A43013; A04331 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession E04333 !'##molecule_type DNA !'##residues 1-132 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession A43013 !'##molecule_type DNA !'##residues 1-132 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96541.1; PID:g215113 !'##note the translation initiation site corresponding to 1-Met is the !1most probable of two possible sites COMMENT Gene FI protein is involved in lambda DNA packaging and !1prohead enlargement during packaging. GENETICS !$#gene FI !$#map_position 14.85-15.66 CLASSIFICATION #superfamily phage lambda DNA packaging protein FI SUMMARY #length 132 #molecular-weight 14308 #checksum 2653 SEQUENCE /// ENTRY VHBPBL #type complete TITLE minor capsid protein B - phage lambda ORGANISM #formal_name phage lambda DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS F04333; B43013; A04332 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession F04333 !'##molecule_type DNA !'##residues 1-533 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession B43013 !'##molecule_type DNA !'##residues 1-533 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96536.1; PID:g215108 !'##note there are two possible initiation sites for gene B translation, !1the codon for 1-Met as shown and that for 15-Met; the amino !1end of protein B* has been determined by partial sequence !1analysis and corresponds to 23-Gly COMMENT Together with its cleavage product, protein B*, gene B !1protein is a minor capsid component located in the head-tail !1connector region. These proteins form the site at which DNA !1packaging proteins Nu1 and A react with concatemeric DNA. !1There are approximately 3 copies of protein B and 10-12 !1copies of protein B* per mature phage. GENETICS !$#gene B !$#map_position 5.85-9.14 CLASSIFICATION #superfamily phage lambda minor capsid protein B SUMMARY #length 533 #molecular-weight 59465 #checksum 8166 SEQUENCE /// ENTRY JN0538 #type complete TITLE head protein gp4 - phage 21 ORGANISM #formal_name phage 21 DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 23-Jul-1999 ACCESSIONS JN0538 REFERENCE JN0537 !$#authors Smith, M.P.; Feiss, M. !$#journal Gene (1993) 126:1-7 !$#title Sequence analysis of the phage 21 genes for prohead assembly !1and head completion. !$#cross-references MUID:93231520; PMID:8472949 !$#accession JN0538 !'##molecule_type DNA !'##residues 1-530 ##label SMI !'##cross-references GB:M81255; NID:g215454; PIDN:AAA32342.1; !1PID:g215458 GENETICS !$#gene 4 CLASSIFICATION #superfamily phage lambda minor capsid protein B KEYWORDS capsid protein; head protein FEATURE !$356-375 #region helix-turn-helix motif SUMMARY #length 530 #molecular-weight 59728 #checksum 3682 SEQUENCE /// ENTRY VHBPCL #type complete TITLE minor capsid protein precursor C - phage lambda CONTAINS capsid assembly protein Nu3 ORGANISM #formal_name phage lambda DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS A04333; B92891 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession A04333 !'##molecule_type DNA !'##residues 1-439 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession B92891 !'##molecule_type DNA !'##residues 1-439 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96537.1; PID:g215109 !'##note there are five alternative initiation sites for gene C !1translation; the codon corresponding to 1-Met is the most !1probable site !'##note gene Nu3 is believed to be coded within gene C, in the same !1reading frame; there are two possible start sites for gene !1Nu3, the GTG codon corresponding to 260-Val and the codon !1for 309-Met COMMENT During head assembly, the gene C protein is covalently !1linked with an equimolar amount of protein E and cleaved to !1yield the minor capsid proteins X1 and X2. COMMENT In conjunction with host protein groE, gene C protein !1specifically cleaves scaffold protein Nu3 during its removal !1from the maturing prohead. COMMENT Gene Nu3 protein forms the scaffold for capsid assembly and !1is required for binding of the B and C protein products. It !1is subsequently lost from the head during maturation. GENETICS !$#gene C !$#map_position 9.11-11.82 CLASSIFICATION #superfamily phage lambda minor capsid protein C FEATURE !$260-439 #product capsid assembly protein Nu3 (version 1) !8#status predicted #label CA1\ !$309-439 #product capsid assembly protein Nu3 (version 2) !8#status predicted #label CA2 SUMMARY #length 439 #molecular-weight 45939 #checksum 7816 SEQUENCE /// ENTRY JN0539 #type complete TITLE head protein gp5 - phage 21 CONTAINS head protein gp6 ORGANISM #formal_name phage 21 DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 23-Jul-1999 ACCESSIONS JN0539; JN0540 REFERENCE JN0537 !$#authors Smith, M.P.; Feiss, M. !$#journal Gene (1993) 126:1-7 !$#title Sequence analysis of the phage 21 genes for prohead assembly !1and head completion. !$#cross-references MUID:93231520; PMID:8472949 !$#accession JN0539 !'##molecule_type DNA !'##residues 1-501 ##label SMI !'##cross-references GB:M81255; NID:g215454; PIDN:AAA32343.1; !1PID:g215459 GENETICS !$#gene 5 !$#start_codon GTG CLASSIFICATION #superfamily phage lambda minor capsid protein C KEYWORDS capsid protein; head protein FEATURE !$302-501 #product head protein gp6 #status predicted #label !8GP6 SUMMARY #length 501 #molecular-weight 52440 #checksum 3291 SEQUENCE /// ENTRY VHBPLL #type complete TITLE major capsid protein - Lactococcus lactis phage F4-1 ORGANISM #formal_name Lactococcus lactis phage F4-1 DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 23-Jul-1999 ACCESSIONS JE0412 REFERENCE JE0412 !$#authors Chung, D.K.; Kim, J.H.; Batt, C.A. !$#journal Gene (1991) 101:121-125 !$#title Cloning and nucleotide sequence of the major capsid protein !1from Lactococcus lactis ssp. cremoris bacteriophage F4-1. !$#cross-references MUID:91285421; PMID:1905665 !$#accession JE0412 !'##molecule_type DNA !'##residues 1-301 ##label CHU !'##cross-references GB:M37979; NID:g215505; PIDN:AAA66055.1; !1PID:g215506 GENETICS !$#gene mcp CLASSIFICATION #superfamily phage F4-1 major coat protein KEYWORDS coat protein SUMMARY #length 301 #molecular-weight 32389 #checksum 4688 SEQUENCE /// ENTRY VHBPDL #type complete TITLE major capsid protein D - phage lambda ALTERNATE_NAMES head protein D ORGANISM #formal_name phage lambda DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS G04333; C43013; A04334; A23206 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession G04333 !'##molecule_type DNA !'##residues 1-110 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession C43013 !'##molecule_type DNA !'##residues 1-110 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96539.1; PID:g215111 REFERENCE A23206 !$#authors Witkiewicz, H.; Schweiger, M. !$#journal EMBO J. (1982) 1:1559-1564 !$#cross-references MUID:84207913; PMID:6233140 !$#contents annotation; physicochemical properties COMMENT Gene D protein is a major component of the phage head and !1serves to stabilize the head during DNA packaging. There are !1approximately 420 copies of protein D per mature phage. GENETICS !$#gene D !$#map_position 11.85-12.53 CLASSIFICATION #superfamily phage lambda major capsid protein D KEYWORDS DNA packaging SUMMARY #length 110 #molecular-weight 11572 #checksum 3863 SEQUENCE /// ENTRY JN0541 #type complete TITLE head protein gpshp - phage 21 ORGANISM #formal_name phage 21 DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 23-Jul-1999 ACCESSIONS JN0541 REFERENCE JN0537 !$#authors Smith, M.P.; Feiss, M. !$#journal Gene (1993) 126:1-7 !$#title Sequence analysis of the phage 21 genes for prohead assembly !1and head completion. !$#cross-references MUID:93231520; PMID:8472949 !$#accession JN0541 !'##molecule_type DNA !'##residues 1-115 ##label SMI !'##cross-references GB:M81255; NID:g215454; PIDN:AAA32345.1; !1PID:g215461 GENETICS !$#gene shp CLASSIFICATION #superfamily phage lambda major capsid protein D KEYWORDS capsid protein; head protein SUMMARY #length 115 #molecular-weight 11976 #checksum 8666 SEQUENCE /// ENTRY VHBPEL #type complete TITLE major capsid protein E - phage lambda ORGANISM #formal_name phage lambda DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS H04333; D43013; A04335 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession H04333 !'##molecule_type DNA !'##residues 1-341 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession D43013 !'##molecule_type DNA !'##residues 1-341 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96540.1; PID:g215112 COMMENT Gene E protein is a major component of the phage head. There !1are about 420 copies of protein E per mature phage. Some of !1the E protein is covalently linked with an equimolar amount !1of protein C and cleaved to yield minor capsid proteins X1 !1and X2. GENETICS !$#gene E !$#map_position 12.65-14.76 CLASSIFICATION #superfamily phage lambda major capsid protein E KEYWORDS capsid protein SUMMARY #length 341 #molecular-weight 38188 #checksum 9211 SEQUENCE /// ENTRY VHBP80 #type complete TITLE major capsid protein - phage phi-80 ORGANISM #formal_name phage phi-80 #note host Escherichia coli DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 23-Jul-1999 ACCESSIONS S03314 REFERENCE S03314 !$#authors Kitao, S.; Nakano, E. !$#journal Nucleic Acids Res. (1988) 16:764 !$#title Nucleotide sequence from bacteriophage phi-80 with high !1homology to the major coat protein gene of lambda. !$#cross-references MUID:88124267; PMID:3267214 !$#accession S03314 !'##molecule_type DNA !'##residues 1-341 ##label KIT !'##cross-references GB:X06751; NID:g15768; PIDN:CAA29926.1; PID:g15769 CLASSIFICATION #superfamily phage lambda major capsid protein E KEYWORDS capsid protein SUMMARY #length 341 #molecular-weight 38054 #checksum 8940 SEQUENCE /// ENTRY JN0542 #type complete TITLE head protein gp7 - phage 21 ORGANISM #formal_name phage 21 DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 23-Jul-1999 ACCESSIONS JN0542 REFERENCE JN0537 !$#authors Smith, M.P.; Feiss, M. !$#journal Gene (1993) 126:1-7 !$#title Sequence analysis of the phage 21 genes for prohead assembly !1and head completion. !$#cross-references MUID:93231520; PMID:8472949 !$#accession JN0542 !'##molecule_type DNA !'##residues 1-342 ##label SMI !'##cross-references GB:M81255; NID:g215454; PIDN:AAA32346.1; !1PID:g215462 GENETICS !$#gene 7 CLASSIFICATION #superfamily phage lambda major capsid protein E KEYWORDS capsid protein; head protein SUMMARY #length 342 #molecular-weight 38569 #checksum 926 SEQUENCE /// ENTRY VHBPFL #type complete TITLE minor capsid protein FII - phage lambda ORGANISM #formal_name phage lambda DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS I94614; E43013; A04336 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession I94614 !'##molecule_type DNA !'##residues 1-117 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession E43013 !'##molecule_type DNA !'##residues 1-117 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96542.1; PID:g215114 !'##note the translation initiation site corresponding to 1-Met is the !1most probable of two possible sites COMMENT Gene FII protein is incorporated into the base vertex of !1DNA-filled heads to facilitate head-tail joining and may !1determine the specificity of tail attachment. There are 5-6 !1copies of protein FII per mature phage. GENETICS !$#gene FII !$#map_position 15.69-16.42 !$#start_codon GTG CLASSIFICATION #superfamily phage lambda minor capsid protein FII SUMMARY #length 117 #molecular-weight 12761 #checksum 3281 SEQUENCE /// ENTRY ZXBPAL #type complete TITLE alc protein - phage T4 ORGANISM #formal_name phage T4 DATE 30-Jun-1987 #sequence_revision 30-Jun-1987 #text_change 23-Jul-1999 ACCESSIONS A04337 REFERENCE A04337 !$#authors Kutter, E.; Drivdahl, R.; Rand, K. !$#journal Genetics (1984) 108:291-304 !$#title Identification and characterization of the alc gene product !1of bacteriophage T4. !$#cross-references MUID:85052459; PMID:6389256 !$#accession A04337 !'##molecule_type DNA !'##residues 1-167 ##label KUT !'##cross-references GB:X03193; GB:X01132; NID:g15246; PIDN:CAA26950.1; !1PID:g15247 GENETICS !$#gene alc CLASSIFICATION #superfamily phage T4 alc protein KEYWORDS DNA binding SUMMARY #length 167 #molecular-weight 19021 #checksum 3152 SEQUENCE /// ENTRY ZNBPT4 #type complete TITLE denA protein - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 23-Jul-1999 ACCESSIONS S08603; JF0024 REFERENCE S07190 !$#authors Sjoeberg, B.M.; Hahne, S.; Mathews, C.Z.; Mathews, C.K.; !1Rand, K.N.; Gait, M.J. !$#journal EMBO J. (1986) 5:2031-2036 !$#title The bacteriophage T4 gene for the small subunit of !1ribonucleotide reductase contains an intron. !$#cross-references MUID:87004574; PMID:3530746 !$#accession S08603 !'##molecule_type DNA !'##residues 1-136 ##label SJO !'##cross-references EMBL:X04140; NID:g15341; PIDN:CAA27759.1; !1PID:g15344 COMMENT This protein is probably an endonuclease II. GENETICS !$#gene denA !$#map_position 135.649-136.056 CLASSIFICATION #superfamily phage T4 denA protein KEYWORDS early protein; endonuclease SUMMARY #length 136 #molecular-weight 15802 #checksum 2165 SEQUENCE /// ENTRY ZXBPB4 #type complete TITLE exonuclease (EC 3.1.-.-) A - phage T4 ALTERNATE_NAMES gp dexA ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 23-Jul-1999 ACCESSIONS B32338; A04338; A32338 REFERENCE A32338 !$#authors Gauss, P.; Gayle, M.; Winter, R.B.; Gold, L. !$#journal Mol. Gen. Genet. (1987) 206:24-34 !$#title The bacteriophage T4 dexA gene: sequence and analysis of a !1gene conditionally required for DNA replication. !$#cross-references MUID:87201086; PMID:3553862 !$#accession B32338 !'##molecule_type DNA !'##residues 1-227 ##label GAU !'##cross-references GB:X04834; NID:g15253; PIDN:CAA28536.1; PID:g15255 GENETICS !$#gene dexA !$#map_position 8.231-8.912 FUNCTION !$#description 3' to 5' exonuclease CLASSIFICATION #superfamily phage T4 dexA protein KEYWORDS exonuclease; hydrolase SUMMARY #length 227 #molecular-weight 25963 #checksum 4628 SEQUENCE /// ENTRY ZXBPH4 #type complete TITLE hoc protein - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 23-Jul-1999 ACCESSIONS JQ0566 REFERENCE JQ0564 !$#authors Kaliman, A.V.; Khasanova, M.A.; Kryukov, V.M.; Tanyashin, !1V.I.; Bayev, A.A. !$#journal Nucleic Acids Res. (1990) 18:4277 !$#title The nucleotide sequence of the region of bacteriophage T4 !1inh(lip)-hoc genes. !$#cross-references MUID:90332449; PMID:2377482 !$#accession JQ0566 !'##status translation not shown !'##molecule_type DNA !'##residues 1-376 ##label KAL !'##cross-references EMBL:X14869; NID:g14789; PIDN:CAA33010.1; !1PID:g14790 COMMENT This protein is a component of T4 capsid. GENETICS !$#gene hoc CLASSIFICATION #superfamily phage T4 hoc protein KEYWORDS capsid protein SUMMARY #length 376 #molecular-weight 40387 #checksum 8885 SEQUENCE /// ENTRY GPBP23 #type complete TITLE gene 23.1 protein - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 30-Jun-1993 ACCESSIONS JF0079 REFERENCE JF0074 !$#authors Yasuda, G.K.; Churchill, G.A.; Parker, M.L.; Mooney, D.T. !$#submission submitted to JIPID, January 1990 !$#accession JF0079 !'##molecule_type DNA !'##residues 1-155 ##label YAS GENETICS !$#gene 23.1 !$#map_position 105.368-105.787 CLASSIFICATION #superfamily phage T4 gene 23.1 protein SUMMARY #length 155 #molecular-weight 17728 #checksum 7992 SEQUENCE /// ENTRY ZXBPT4 #type complete TITLE uvsY protein - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 17-Mar-1987 #sequence_revision 30-Sep-1991 #text_change 23-Jul-1999 ACCESSIONS JS0136; A45963; A04339 REFERENCE JS0136 !$#authors Kobayashi, M.; Saito, H.; Takahashi, H. !$#journal Nucleic Acids Res. (1988) 16:7729 !$#title Confirmation of the reading frame of bacteriophage T4 uvsY !1gene. !$#cross-references MUID:88319967; PMID:3412904 !$#accession JS0136 !'##molecule_type DNA !'##residues 1-137 ##label KOB REFERENCE A45963 !$#authors Gruidl, M.E.; Mosig, G. !$#journal Genetics (1986) 114:1061-1079 !$#title Sequence and transcripts of the bacteriophage T4 DNA repair !1gene uvsY. !$#cross-references MUID:87106763; PMID:3026891 !$#accession A45963 !'##status preliminary !'##molecule_type DNA !'##residues 1-137 ##label GRU !'##cross-references GB:X04856; NID:g15399; PIDN:CAA28549.1; PID:g15402 COMMENT This protein is involved in the DNA synthesis and !1recombination process. GENETICS !$#gene uvsY CLASSIFICATION #superfamily phage T4 uvsY protein KEYWORDS DNA biosynthesis; DNA recombination; DNA repair SUMMARY #length 137 #molecular-weight 15839 #checksum 1346 SEQUENCE /// ENTRY GHBP24 #type complete TITLE gene 24 protein - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 13-Sep-1997 ACCESSIONS JF0074 REFERENCE JF0074 !$#authors Yasuda, G.K.; Churchill, G.A.; Parker, M.L.; Mooney, D.T. !$#submission submitted to JIPID, January 1990 !$#accession JF0074 !'##molecule_type DNA !'##residues 1-427 ##label YAS !'##note the authors translated the codon AAT for residue 425 as Ile COMMENT This protein is a component of the phage head vertex. GENETICS !$#gene 24 !$#map_position 106.081-107.362 CLASSIFICATION #superfamily phage T4 gene 24 protein KEYWORDS head protein; late protein SUMMARY #length 427 #molecular-weight 46994 #checksum 2861 SEQUENCE /// ENTRY GYBPT4 #type complete TITLE gene 25 protein - phage T4 ALTERNATE_NAMES baseplate protein 25 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 16-Jun-2000 ACCESSIONS JF0054; D45963; S01692 REFERENCE JF0054 !$#authors Gruidl, M.E.; Canan, N.C.; Mosig, G. !$#journal Nucleic Acids Res. (1988) 16:9862 !$#title Bacteriophage T4 gene 25. !$#cross-references MUID:89041577; PMID:3186452 !$#accession JF0054 !'##molecule_type DNA !'##residues 1-132 ##label GRU !'##cross-references EMBL:X12628; NID:g15303; PIDN:CAA31147.1; !1PID:g15304 REFERENCE A45963 !$#authors Gruidl, M.E.; Mosig, G. !$#journal Genetics (1986) 114:1061-1079 !$#title Sequence and transcripts of the bacteriophage T4 DNA repair !1gene uvsY. !$#cross-references MUID:87106763; PMID:3026891 !$#accession D45963 !'##status preliminary !'##molecule_type DNA !'##residues 6-132 ##label GR2 !'##cross-references GB:X04856; NID:g15399; PIDN:CAA28547.1; !1PID:g1364178 GENETICS !$#gene 25 FUNCTION !$#description an acidic structural component of the outer wedges of the !1phage baseplate and has lysozyme activity CLASSIFICATION #superfamily phage T4 gene 25 protein KEYWORDS baseplate; late protein SUMMARY #length 132 #molecular-weight 15095 #checksum 6448 SEQUENCE /// ENTRY GXBPT4 #type complete TITLE baseplate protein gp26 - phage T4 ALTERNATE_NAMES gene 26 protein ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 23-Jul-1999 ACCESSIONS JQ0441; PS0092 REFERENCE JQ0441 !$#authors Nivinskas, R.; Raudonikiene, A.; Vaiskunaite, R. !$#journal Nucleic Acids Res. (1990) 18:1913 !$#title Bacteriophage T4 gene 26. !$#cross-references MUID:90245607; PMID:2186370 !$#accession JQ0441 !'##molecule_type DNA !'##residues 1-208 ##label NIV !'##cross-references EMBL:X17685; NID:g14787; PIDN:CAA35676.1; !1PID:g14788 REFERENCE JF0082 !$#authors Scarlato, V.; Storlazzi, A.; Gargano, S.; Cascino, A. !$#journal Virology (1989) 171:475-483 !$#title Bacteriophage T4 late gene expression: overlapping promoters !1direct divergent transcription of the base plate gene !1cluster. !$#cross-references MUID:89348006; PMID:2763463 !$#accession PS0092 !'##molecule_type DNA !'##residues 1-26 ##label SCA !'##cross-references GB:J04354; NID:g215826; PIDN:AAA88464.1; !1PID:g1196769 GENETICS !$#gene 26 !$#map_position 115.166-115.913 FUNCTION !$#description this protein is a structural component of the central hub of !1the phage baseplate CLASSIFICATION #superfamily phage T4 baseplate protein gp26 KEYWORDS baseplate; late protein SUMMARY #length 208 #molecular-weight 23881 #checksum 6222 SEQUENCE /// ENTRY GZBPT4 #type complete TITLE baseplate protein gp27 - phage T4 ALTERNATE_NAMES gene 27 protein ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 23-Jul-1999 ACCESSIONS JU0285; PS0093 REFERENCE JU0285 !$#authors Bova, R.; Cascino, A.; Cipollaro, M.; Grau, O.; Micheli, !1M.R.; Santoro, M.; Storlazzi, A.; Scarlato, V.; Gargano, S. !$#journal Nucleic Acids Res. (1990) 18:3046 !$#title Bacteriophage T4 gene 27. !$#cross-references MUID:90272413; PMID:2349100 !$#accession JU0285 !'##molecule_type DNA !'##residues 1-391 ##label BOV !'##cross-references EMBL:X52236; NID:g15202; PIDN:CAA36481.1; !1PID:g15203 REFERENCE JF0082 !$#authors Scarlato, V.; Storlazzi, A.; Gargano, S.; Cascino, A. !$#journal Virology (1989) 171:475-483 !$#title Bacteriophage T4 late gene expression: overlapping promoters !1direct divergent transcription of the base plate gene !1cluster. !$#cross-references MUID:89348006; PMID:2763463 !$#accession PS0093 !'##molecule_type DNA !'##residues 1-53 ##label SCA !'##cross-references GB:J04354; NID:g215826; PIDN:AAA88466.1; !1PID:g215828 GENETICS !$#gene 27 !$#map_position 116.0-117.2 FUNCTION !$#description a structural component of the central hub of the phage !1baseplate CLASSIFICATION #superfamily phage T4 baseplate protein gp27 KEYWORDS baseplate; late protein SUMMARY #length 391 #molecular-weight 44422 #checksum 8810 SEQUENCE /// ENTRY GBBPT4 #type complete TITLE baseplate protein gp29 - phage T4 ALTERNATE_NAMES probable tetrahydrofolylpolyglutamate synthase (EC 6.3.2.17); tail length regulator ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 02-Jun-2000 ACCESSIONS JF0035 REFERENCE JF0035 !$#authors Ishimoto, L.K.; Ishimoto, K.S.; Cascino, A.; Cipollaro, M.; !1Eiserling, F.A. !$#journal Virology (1988) 164:81-90 !$#title The structure of three bacteriophage T4 genes required for !1tail-tube assembly. !$#cross-references MUID:88206086; PMID:3363870 !$#accession JF0035 !'##molecule_type DNA !'##residues 1-590 ##label ISH !'##cross-references GB:M20298; NID:g215944; PIDN:AAA32538.1; !1PID:g215946 !'##note the initiation codon of gene 29 and the termination codon of !1gene 28 overlap (ATGA) COMMENT gp29 is a component of the phage baseplate initiating !1assembly of the baseplate central hub. GENETICS !$#gene 29 !$#map_position 117.515-119.285 CLASSIFICATION #superfamily phage T4 baseplate protein gp29 KEYWORDS baseplate; ligase; tail protein SUMMARY #length 590 #molecular-weight 64410 #checksum 5445 SEQUENCE /// ENTRY GCBPT4 #type complete TITLE baseplate protein gp48 precursor - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 23-Jul-1999 ACCESSIONS JF0036; PU0011 REFERENCE JF0035 !$#authors Ishimoto, L.K.; Ishimoto, K.S.; Cascino, A.; Cipollaro, M.; !1Eiserling, F.A. !$#journal Virology (1988) 164:81-90 !$#title The structure of three bacteriophage T4 genes required for !1tail-tube assembly. !$#cross-references MUID:88206086; PMID:3363870 !$#accession JF0036 !'##molecule_type DNA !'##residues 1-364 ##label ISH !'##cross-references GB:M20298; NID:g215944; PIDN:AAA32539.1; !1PID:g215947 !$#accession PU0011 !'##molecule_type protein !'##residues 2-13 ##label IS2 !'##note the initiation codon for gene 54 overlaps with the termination !1codon of gene 48 COMMENT Morphogenesis of baseplates is completed by association of !1gp48 and gp54, and the baseplate is then able to initiate !1tail-tube polymerization. GENETICS !$#gene 48 !$#map_position 119.296-120.388 CLASSIFICATION #superfamily phage T4 baseplate protein gp48 KEYWORDS baseplate FEATURE !$2-364 #product baseplate protein gp48 #status predicted !8#label MAT SUMMARY #length 364 #molecular-weight 39733 #checksum 4459 SEQUENCE /// ENTRY GDBPT4 #type complete TITLE baseplate protein gp54 - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 23-Jul-1999 ACCESSIONS JF0037 REFERENCE JF0035 !$#authors Ishimoto, L.K.; Ishimoto, K.S.; Cascino, A.; Cipollaro, M.; !1Eiserling, F.A. !$#journal Virology (1988) 164:81-90 !$#title The structure of three bacteriophage T4 genes required for !1tail-tube assembly. !$#cross-references MUID:88206086; PMID:3363870 !$#accession JF0037 !'##molecule_type DNA !'##residues 1-320 ##label ISH !'##cross-references GB:M20298; NID:g215944; PIDN:AAA32540.1; !1PID:g215948 !'##note the initiation codon for gene 54 overlaps with the termination !1codon of gene 48 COMMENT Morphogenesis of baseplates is completed by association of !1gp48 and gp54, and the baseplate then initiates tail-tube !1polymerization. GENETICS !$#gene 54 !$#map_position 120.390-121.350 CLASSIFICATION #superfamily phage T4 baseplate protein gp54 KEYWORDS baseplate; tail protein SUMMARY #length 320 #molecular-weight 34977 #checksum 6234 SEQUENCE /// ENTRY GMBPT4 #type complete TITLE gene 59 protein - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 05-Sep-1997 ACCESSIONS S05559 REFERENCE S05555 !$#authors Hahn, S.; Rueger, W. !$#journal Nucleic Acids Res. (1989) 17:6729 !$#title Organization of the bacteriophage T4 genome between map !1positions 150.745 and 145.824. !$#cross-references MUID:89386003; PMID:2674900 !$#accession S05559 !'##status translation not shown !'##molecule_type DNA !'##residues 1-217 ##label HAH !'##cross-references EMBL:X15818; NID:g15210; PID:g15214 GENETICS !$#gene 59 CLASSIFICATION #superfamily phage T4 gene 59 protein KEYWORDS DNA binding SUMMARY #length 217 #molecular-weight 25997 #checksum 1520 SEQUENCE /// ENTRY GKBPT4 #type complete TITLE gene 18 protein - phage T4 ALTERNATE_NAMES tail sheath protein gp18 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 23-Jul-1999 ACCESSIONS JF0021 REFERENCE JF0021 !$#authors Arisaka, F.; Nakako, T.; Takahashi, H.; Ishii, S. !$#journal J. Virol. (1988) 62:1186-1193 !$#title Nucleotide sequence of the tail sheath gene of bacteriophage !1T4 and amino acid sequence of its product. !$#cross-references MUID:88155753; PMID:2964531 !$#accession JF0021 !'##molecule_type DNA !'##residues 1-659 ##label ARI !'##cross-references GB:M19085; EMBL:M36959; NID:g215949; !1PIDN:AAA32541.1; PID:g215950 GENETICS !$#gene 18 !$#map_position 97.352-99.328 CLASSIFICATION #superfamily phage T4 gene 18 protein SUMMARY #length 659 #molecular-weight 71288 #checksum 1763 SEQUENCE /// ENTRY ZYBPT4 #type complete TITLE tail protein gp51 - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 23-Jul-1999 ACCESSIONS JF0082; S20451 REFERENCE JF0082 !$#authors Scarlato, V.; Storlazzi, A.; Gargano, S.; Cascino, A. !$#journal Virology (1989) 171:475-483 !$#title Bacteriophage T4 late gene expression: overlapping promoters !1direct divergent transcription of the base plate gene !1cluster. !$#cross-references MUID:89348006; PMID:2763463 !$#accession JF0082 !'##molecule_type DNA !'##residues 1-249 ##label SCA !'##cross-references GB:J04354; NID:g215826; PIDN:AAA88465.1; !1PID:g215827 REFERENCE S20451 !$#authors Nivinskas, R.; Vaiskunaite, R.; Raudonikiene, A. !$#journal Mol. Gen. Genet. (1992) 232:257-261 !$#title An internal AUU codon initiates a smaller peptide encoded by !1bacteriophage T4 baseplate gene 26. !$#cross-references MUID:92212289; PMID:1557032 !$#accession S20451 !'##status translation not shown !'##molecule_type DNA !'##residues 1-78,'VP',81-104,'EP',107-229,'M',231-249 ##label NIV !'##cross-references EMBL:X55132; NID:g14878; PIDN:CAA38925.1; !1PID:g14879 COMMENT This protein is essential for the formation of the central !1hub of the phage baseplate. GENETICS !$#gene 51 !$#map_position 115.166-115.913 CLASSIFICATION #superfamily phage T4 tail protein gp51 KEYWORDS late protein; tail protein SUMMARY #length 249 #molecular-weight 29339 #checksum 2098 SEQUENCE /// ENTRY HIBPX4 #type complete TITLE prohead core protein precursor - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 23-Jul-1999 ACCESSIONS A04340 REFERENCE A04340 !$#authors Keller, B.; Sengstag, C.; Kellenberger, E.; Bickle, T.A. !$#journal J. Mol. Biol. (1984) 179:415-430 !$#title Gene 68, a new bacteriophage T4 gene which codes for the 17K !1prohead core protein is involved in head size determination. !$#cross-references MUID:85083058; PMID:6512858 !$#accession A04340 !'##molecule_type DNA !'##residues 1-141 ##label KEL !'##cross-references GB:X01414; NID:g15325; PIDN:CAA25656.1; PID:g15327 GENETICS !$#gene 68 CLASSIFICATION #superfamily phage T4 prohead core protein FEATURE !$22-141 #product prohead core protein #status predicted !8#label MAT SUMMARY #length 141 #molecular-weight 15873 #checksum 7477 SEQUENCE /// ENTRY VHBPC4 #type complete TITLE small outer capsid protein - phage T4 ALTERNATE_NAMES gp soc ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 24-Sep-1999 ACCESSIONS A04342; JS0789; T10134; A04341 REFERENCE A90996 !$#authors Macdonald, P.M.; Mosig, G. !$#journal EMBO J. (1984) 3:2863-2871 !$#title Regulation of a new bacteriophage T4 gene, 69, that spans an !1origin of DNA replication. !$#cross-references MUID:85126881; PMID:6098451 !$#accession A04342 !'##molecule_type DNA !'##residues 1-80 ##label MAC !'##cross-references GB:X01416; NID:g15329; PIDN:CAA25663.1; PID:g15333 REFERENCE A04341 !$#authors Bijlenga, R.K.L.; Ishii, T.; Tsugita, A. !$#journal J. Mol. Biol. (1978) 120:249-263 !$#title Complete primary structure of the small outer capsid (soc) !1protein of bacteriophage T4. !$#cross-references MUID:78153769; PMID:642009 !$#accession JS0789 !'##molecule_type protein !'##residues 2-39,'EGKEFH',40-44,'T',46-77,'GVT' ##label BIJ REFERENCE JH0136 !$#authors Frazier, M.W.; Mosig, G. !$#journal Gene (1990) 88:7-14 !$#title The bacteriophage T4 gene mrh whose product inhibits late T4 !1gene expression in an Escherichia coli rpoH (sigma(32)) !1mutant. !$#cross-references MUID:90255970; PMID:1692800 !$#accession T10134 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-80 ##label FRA !'##cross-references EMBL:M30001; NID:g1532074; PIDN:AAB07793.1; !1PID:g1532077 !'##experimental_source strain GT7 COMMENT This protein is nonessential but one of the major capsid !1protein. Itplays a role of resistance to osmosis. Soc !1protein and hoc protein cocrystallize on the surface of !1capsid with essential protein, gp 23 in the capsomer !1morphology of 6:1:6. GENETICS !$#gene soc CLASSIFICATION #superfamily phage T4 small outer capsid protein KEYWORDS capsid protein FEATURE !$2-80 #product small outer capsid protein #status predicted !8#label MAT SUMMARY #length 80 #molecular-weight 9117 #checksum 6971 SEQUENCE /// ENTRY VHBP20 #type complete TITLE capsid protein 20 - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 23-Jul-1999 ACCESSIONS JU0161; S05997 REFERENCE JU0161 !$#authors Marusich, E.I.; Mesyanzhinov, V.V. !$#journal Nucleic Acids Res. (1989) 17:7514 !$#title Nucleotide and deduced amino acid sequences of bacteriophage !1T4 gene 20. !$#cross-references MUID:90016810; PMID:2798102 !$#accession JU0161 !'##molecule_type DNA !'##residues 1-524 ##label MAR !'##cross-references GB:X16055; NID:g15334; PIDN:CAA34190.1; PID:g15335 COMMENT This protein is responsible for initiation of head assembly, !1DNA packaging, and binding with tail connector. GENETICS !$#gene 20 CLASSIFICATION #superfamily phage T4 capsid protein 20 KEYWORDS capsid protein SUMMARY #length 524 #molecular-weight 60986 #checksum 3053 SEQUENCE /// ENTRY VHBPP4 #type complete TITLE capsid assembly protein gp31 - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 23-Jul-1999 ACCESSIONS JT0488; A38822; S12715; S26170; JS0555 REFERENCE JT0488 !$#authors Nivinskas, R.; Black, L.W. !$#journal Gene (1988) 73:251-257 !$#title Cloning, sequence, and expression of the !1temperature-dependent phage T4 capsid assembly gene 31. !$#cross-references MUID:89211957; PMID:3072258 !$#accession JT0488 !'##molecule_type DNA !'##residues 1-111 ##label NIV !'##cross-references GB:M37882; NID:g215873; PIDN:AAA32506.1; !1PID:g215876 REFERENCE JQ0524 !$#authors Prilipov, A.G.; Mesyanzhinov, V.V.; Aebi, U.; Kellenberger, !1E. !$#journal Nucleic Acids Res. (1990) 18:3635 !$#title Cloning and sequencing of bacteriophage T4 genes between map !1positions 128.3-130.3. !$#cross-references MUID:90301484; PMID:2362813 !$#accession A38822 !'##status translation not shown !'##molecule_type DNA !'##residues 1-111 ##label PRI !'##cross-references EMBL:X17657; NID:g15204; PIDN:CAA35651.1; !1PID:g15207 REFERENCE JU0290 !$#authors Raudonikiene, A.; Nivinskas, R. !$#journal Nucleic Acids Res. (1990) 18:4280 !$#title Nucleotide sequence of bacteriophage T4 gene 31 region. !$#cross-references MUID:90332452; PMID:2377483 !$#accession S12715 !'##status translation not shown !'##molecule_type DNA !'##residues 1-111 ##label RAU !'##cross-references EMBL:M37882; NID:g215873; PIDN:AAA32506.1; !1PID:g215876 REFERENCE S26167 !$#authors Raudonikiene, A.; Nivinskas, R. !$#journal Gene (1992) 114:85-90 !$#title Gene rIII is the nearest downstream neighbour of !1bacteriophage T4 gene 31. !$#cross-references MUID:92267389; PMID:1587487 !$#accession S26170 !'##status preliminary !'##molecule_type DNA !'##residues 1-111 ##label RA2 !'##cross-references EMBL:X54536; NID:g15789; PIDN:CAA38405.1; !1PID:g15792 COMMENT This protein is an initiator and organizer of head assembly, !1but the gene product is not found in the mature phage. It is !1a membrane protein and appears to interact with the host !1Escherichia coli groEL protein. GENETICS !$#gene 31 !$#map_position 129.247-129.580 CLASSIFICATION #superfamily phage T4 capsid assembly protein gp31 KEYWORDS capsid assembly SUMMARY #length 111 #molecular-weight 12079 #checksum 9714 SEQUENCE /// ENTRY ACBPT7 #type complete TITLE capsid assembly protein - phage T7 ORGANISM #formal_name phage T7 DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS A04343; S42324 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession A04343 !'##molecule_type DNA !'##residues 1-307 ##label DUN REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42324 !'##molecule_type DNA !'##residues 1-307 ##label DUW !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24426.1; !1PID:g15603 !'##note the authors did not translate the codon for residue 1 GENETICS !$#gene 9 !$#map_position 54.96-57.26 CLASSIFICATION #superfamily phage T7 capsid assembly protein KEYWORDS capsid assembly SUMMARY #length 307 #molecular-weight 33897 #checksum 8163 SEQUENCE /// ENTRY VABPA7 #type complete TITLE major capsid protein 10A - phage T7 ORGANISM #formal_name phage T7 #note host Escherichia coli DATE 13-Jun-1983 #sequence_revision 30-Sep-1990 #text_change 23-Jul-1999 ACCESSIONS A04344; S42325 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession A04344 !'##molecule_type DNA !'##residues 1-345 ##label DUN REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42325 !'##molecule_type DNA !'##residues 1-345 ##label DUW !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24427.1; !1PID:g15604 !'##note the authors did not translate the codon for residue 1 GENETICS !$#gene 10A !$#map_position 57.51-60.49 CLASSIFICATION #superfamily phage T7 major capsid protein 10A KEYWORDS capsid protein SUMMARY #length 345 #molecular-weight 36545 #checksum 8044 SEQUENCE /// ENTRY VBBPA7 #type complete TITLE minor capsid protein 10B - phage T7 ORGANISM #formal_name phage T7 #note host Escherichia coli DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 23-Jul-1999 ACCESSIONS B04344; S42326 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession B04344 !'##molecule_type DNA !'##residues 1-398 ##label DUN REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42326 !'##status preliminary; translation not shown !'##molecule_type DNA !'##residues 1-398 ##label DU2 !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24428.1; !1PID:g431193 GENETICS !$#gene 10B !$#map_position 57.51-60.49 !$#note translation of the nucleotide sequence involves a -1 !1frameshift within codon 341 CLASSIFICATION #superfamily phage T7 major capsid protein 10A KEYWORDS capsid protein SUMMARY #length 398 #molecular-weight 41830 #checksum 5020 SEQUENCE /// ENTRY VABPA3 #type complete TITLE major capsid protein 10A - phage T3 ORGANISM #formal_name phage T3 #note host Escherichia coli DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 23-Jul-1999 ACCESSIONS S04618 REFERENCE S04618 !$#authors Condreay, J.P.; Wright, S.E.; Molineux, I.J. !$#journal J. Mol. Biol. (1989) 207:555-561 !$#title Nucleotide sequence and complementation studies of the gene !110 region of bacteriophage T3. !$#cross-references MUID:89342440; PMID:2760923 !$#accession S04618 !'##molecule_type DNA !'##residues 1-347 ##label CON !'##cross-references GB:X17255; NID:g15682; PIDN:CAA35154.1; PID:g15716 GENETICS !$#gene 10A CLASSIFICATION #superfamily phage T7 major capsid protein 10A KEYWORDS capsid protein SUMMARY #length 347 #molecular-weight 36882 #checksum 9272 SEQUENCE /// ENTRY VBBPA3 #type complete TITLE minor capsid protein 10B - phage T3 ORGANISM #formal_name phage T3 #note host Escherichia coli DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 30-Jun-1993 ACCESSIONS A33079 REFERENCE S04618 !$#authors Condreay, J.P.; Wright, S.E.; Molineux, I.J. !$#journal J. Mol. Biol. (1989) 207:555-561 !$#title Nucleotide sequence and complementation studies of the gene !110 region of bacteriophage T3. !$#cross-references MUID:89342440; PMID:2760923 !$#accession A33079 !'##molecule_type DNA !'##residues 1-433 ##label CON GENETICS !$#gene 10B CLASSIFICATION #superfamily phage T7 major capsid protein 10A KEYWORDS capsid protein SUMMARY #length 433 #molecular-weight 45356 #checksum 1194 SEQUENCE /// ENTRY HIBP14 #type complete TITLE internal protein I precursor - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 24-Apr-1984 #sequence_revision 17-Mar-1987 #text_change 23-Jul-1999 ACCESSIONS A92919; A92843; A04345 REFERENCE A92919 !$#authors Broida, J.; Abelson, J. !$#journal J. Mol. Biol. (1985) 185:545-563 !$#title Sequence organization and control of transcription in the !1bacteriophage T4 tRNA region. !$#cross-references MUID:86037230; PMID:4057254 !$#accession A92919 !'##molecule_type DNA !'##residues 1-95 ##label BRO !'##cross-references GB:X03016; GB:J02511; GB:J02516; GB:J02517; !1GB:V00861; GB:V00862; NID:g15386; PIDN:CAA26803.1; !1PID:g15390 REFERENCE A92843 !$#authors Isobe, T.; Black, L.W.; Tsugita, A. !$#journal J. Mol. Biol. (1977) 110:165-177 !$#title Complete amino acid sequence of bacteriophage T4 internal !1protein I and its cleavage site on virus maturation. !$#cross-references MUID:77144072; PMID:845944 !$#accession A92843 !'##molecule_type protein !'##residues 16-95 ##label ISO !'##note this sequence differs from that shown in the transposition of !1several groups of nearby residues and one peptide COMMENT Internal protein I is one of four proteins in a complex that !1functions in bacteriophage head maturation. A segment is !1cleaved from each protein during this process by the head !1assembly proteinase. GENETICS !$#gene ipI CLASSIFICATION #superfamily phage T4 internal protein I KEYWORDS head protein FEATURE !$1-15 #domain signal sequence #status predicted #label SIG\ !$16-19 #domain propeptide #status experimental #label PRO\ !$19-95 #product internal protein I #status experimental !8#label MAT\ !$19-20 #cleavage_site Glu-Ala (prohead proteinase) #status !8experimental SUMMARY #length 95 #molecular-weight 10177 #checksum 521 SEQUENCE /// ENTRY HIBP24 #type complete TITLE internal protein II precursor - phage T4 ALTERNATE_NAMES Ip2 protein; ipII protein ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 24-Apr-1984 #sequence_revision 03-May-1996 #text_change 23-Jul-1999 ACCESSIONS B36780; S48007; A04346 REFERENCE JF0016 !$#authors Valerie, K.; Stevens, J.; Lynch, M.; Henderson, E.E.; de !1Riel, J.K. !$#journal Nucleic Acids Res. (1986) 14:8637-8654 !$#title Nucleotide sequence and analysis of the 58.3 to 65.5-kb !1early region of bacteriophage T4. !$#cross-references MUID:87066735; PMID:3024113 !$#accession B36780 !'##molecule_type DNA !'##residues 1-100 ##label VAL !'##cross-references GB:X04567; NID:g15260; PIDN:CAA28214.1; PID:g15265 REFERENCE S48006 !$#authors Repoila, F.; Tetart, F.; Bouet, J.Y.; Krisch, H.M. !$#journal EMBO J. (1994) 13:4181-4192 !$#title Genomic polymorphism in the T-even bacteriophages. !$#cross-references MUID:94357192; PMID:8076614 !$#accession S48007 !'##molecule_type DNA !'##residues 1-100 ##label REP REFERENCE A04346 !$#authors Isobe, T.; Black, L.W.; Tsugita, A. !$#journal J. Mol. Biol. (1976) 102:349-365 !$#title Primary structure of bacteriophage T4 internal protein II !1and characterization of the cleavage upon phage maturation. !$#cross-references MUID:76193777; PMID:1271467 !$#accession A04346 !'##molecule_type protein !'##residues 'ZPALK',1-39,'K',40-62,'PK',65-72,'ND',75-83,'N',85-88, !191-94,'AA',95-100 ##label ISO !'##note the amino end of the precursor protein is blocked COMMENT Internal protein II, which has a histone-like character, !1weakly binds to other components of the assembly core during !1an early stage of bacteriophage head morphogenesis. CLASSIFICATION #superfamily phage T4 internal protein II KEYWORDS head protein FEATURE !$1-10 #domain propeptide #status predicted #label PRO\ !$11-100 #product internal protein II #status predicted #label !8MAT\ !$10-11 #cleavage_site Glu-Ala (prohead proteinase) #status !8experimental SUMMARY #length 100 #molecular-weight 11086 #checksum 1909 SEQUENCE /// ENTRY HIBPA4 #type complete TITLE internal protein III precursor - phage T4 ALTERNATE_NAMES IPIII protein ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 23-Jul-1999 ACCESSIONS A36780; JF0027; S48008 REFERENCE JF0016 !$#authors Valerie, K.; Stevens, J.; Lynch, M.; Henderson, E.E.; de !1Riel, J.K. !$#journal Nucleic Acids Res. (1986) 14:8637-8654 !$#title Nucleotide sequence and analysis of the 58.3 to 65.5-kb !1early region of bacteriophage T4. !$#cross-references MUID:87066735; PMID:3024113 !$#accession A36780 !'##molecule_type DNA !'##residues 1-193 ##label VAL !'##cross-references GB:X04567; NID:g15260; PIDN:CAA28213.1; PID:g15262 REFERENCE JF0027 !$#authors Isobe, T.; Black, L.W.; Tsugita, A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1976) 73:4205-4209 !$#title Protein cleavage during virus assembly: a novel specificity !1of assembly dependent cleavage in bacteriophage T4. !$#cross-references MUID:77058095; PMID:1069310 !$#accession JF0027 !'##molecule_type protein !'##residues 1-2,'V',4-11,'T',13-20 ##label ISO REFERENCE S48006 !$#authors Repoila, F.; Tetart, F.; Bouet, J.Y.; Krisch, H.M. !$#journal EMBO J. (1994) 13:4181-4192 !$#title Genomic polymorphism in the T-even bacteriophages. !$#cross-references MUID:94357192; PMID:8076614 !$#accession S48008 !'##status preliminary !'##molecule_type DNA !'##residues 1-193 ##label REP COMMENT Internal protein III is part of a protein complex that !1functions in phage head assembly. A segment is cleaved from !1the precursor protein during head maturation by prohead !1proteinase (gp21). GENETICS !$#gene IPIII !$#map_position 64.970-65.549 CLASSIFICATION #superfamily phage T4 internal protein III KEYWORDS head protein FEATURE !$1-10 #domain propeptide #status experimental #label PRO\ !$11-193 #product internal protein III #status predicted !8#label MAT\ !$10-11 #cleavage_site Glu-Ala (prohead proteinase) #status !8predicted SUMMARY #length 193 #molecular-weight 21687 #checksum 9479 SEQUENCE /// ENTRY HIBPT4 #type complete TITLE prehead core component PIP - phage T4 ORGANISM #formal_name phage T4 DATE 15-Nov-1984 #sequence_revision 15-Nov-1984 #text_change 23-Jul-1999 ACCESSIONS A04347 REFERENCE A04347 !$#authors Volker, T.A.; Gafner, J.; Bickle, T.A.; Showe, M.K. !$#journal J. Mol. Biol. (1982) 161:479-489 !$#title Gene 67, a new, essential bacteriophage T4 head gene codes !1for a prehead core component, PIP. I. Genetic mapping and !1DNA sequence. !$#cross-references MUID:83111965; PMID:7154087 !$#accession A04347 !'##molecule_type DNA !'##residues 1-80 ##label VOL !'##cross-references GB:J02512; GB:J02505; NID:g215909; PIDN:AAA32520.1; !1PID:g215910 COMMENT The production of one phage particle requires 250 copies of !1PIP. During head maturation, PIP is cleaved to form the !1stable head constituent, internal peptide II; the remaining !1amino end of PIP is degraded. GENETICS !$#map_position 61.8 CLASSIFICATION #superfamily phage T4 prehead core component PIP KEYWORDS capsid assembly FEATURE !$1-46 #domain propeptide #status predicted #label PRO\ !$47-80 #product internal peptide II #status predicted #label !8MAT SUMMARY #length 80 #molecular-weight 9105 #checksum 7813 SEQUENCE /// ENTRY NIBPA7 #type complete TITLE internal virion protein A - phage T7 ORGANISM #formal_name phage T7 DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS A04349; S42329 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession A04349 !'##molecule_type DNA !'##residues 1-138 ##label DUN REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42329 !'##molecule_type DNA !'##residues 1-138 ##label DUW !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24431.1; !1PID:g15607 GENETICS !$#gene 13 !$#map_position 68.37-69.41 CLASSIFICATION #superfamily phage T7 internal virion protein A SUMMARY #length 138 #molecular-weight 15852 #checksum 4444 SEQUENCE /// ENTRY NIBPB7 #type complete TITLE internal virion protein B - phage T7 ORGANISM #formal_name phage T7 DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS A04350; S42330 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession A04350 !'##molecule_type DNA !'##residues 1-196 ##label DUN REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42330 !'##molecule_type DNA !'##residues 1-196 ##label DUW !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24432.1; !1PID:g15608 !'##note the authors did not translate the codon for residue 1 GENETICS !$#gene 14 !$#map_position 69.43-70.90 CLASSIFICATION #superfamily phage T7 internal virion protein B SUMMARY #length 196 #molecular-weight 20968 #checksum 157 SEQUENCE /// ENTRY HIBPC7 #type complete TITLE internal virion protein C - phage T7 ORGANISM #formal_name phage T7 DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS A04351; S42331 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession A04351 !'##molecule_type DNA !'##residues 1-747 ##label DUN REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42331 !'##molecule_type DNA !'##residues 1-747 ##label DUW !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24433.1; !1PID:g15609 !'##note the authors did not translate the codon for residue 1 GENETICS !$#gene 15 !$#map_position 70.92-76.53 CLASSIFICATION #superfamily phage T7 internal virion protein C SUMMARY #length 747 #molecular-weight 84340 #checksum 5513 SEQUENCE /// ENTRY HIBPD7 #type complete TITLE internal virion protein D - phage T7 ORGANISM #formal_name phage T7 DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS A04352; S42332 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession A04352 !'##molecule_type DNA !'##residues 1-1318 ##label DUN REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42332 !'##molecule_type DNA !'##residues 1-1318 ##label DUW !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24434.1; !1PID:g15610 GENETICS !$#gene 16 !$#map_position 76.61-86.51 CLASSIFICATION #superfamily phage T7 internal virion protein D SUMMARY #length 1318 #molecular-weight 143837 #checksum 272 SEQUENCE /// ENTRY JQBPL #type complete TITLE head-to-tail joining protein W - phage lambda ORGANISM #formal_name phage lambda DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS H43008; F43013; A04353 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession H43008 !'##molecule_type DNA !'##residues 1-68 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession F43013 !'##molecule_type DNA !'##residues 1-68 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96535.1; PID:g215107 !'##note the reading frame for gene W was established on the basis of !1the nucleotide sequence of a strain of lambda with an amber !1mutation in this gene; the sequence of this strain contains !1the amber codon, TAG, at the position corresponding to the !1codon CAG, for Gln-4, of the wild type COMMENT Gene W protein functions in the final maturation of !1DNA-filled heads that is necessary for the joining of the !1head to the tail. It may be present in the mature phage. GENETICS !$#gene W !$#map_position 5.43-5.85 CLASSIFICATION #superfamily phage lambda head-to-tail joining protein W SUMMARY #length 68 #molecular-weight 7613 #checksum 2050 SEQUENCE /// ENTRY JN0537 #type complete TITLE head protein gp3 - phage 21 ORGANISM #formal_name phage 21 DATE 17-Feb-1994 #sequence_revision 17-Feb-1994 #text_change 23-Jul-1999 ACCESSIONS JN0537; C49849 REFERENCE JN0537 !$#authors Smith, M.P.; Feiss, M. !$#journal Gene (1993) 126:1-7 !$#title Sequence analysis of the phage 21 genes for prohead assembly !1and head completion. !$#cross-references MUID:93231520; PMID:8472949 !$#accession JN0537 !'##molecule_type DNA !'##residues 1-68 ##label SMI !'##cross-references GB:M81255; NID:g215454; PIDN:AAA32341.1; !1PID:g215457 REFERENCE A49849 !$#authors Smith, M.P.; Feiss, M. !$#journal J. Bacteriol. (1993) 175:2393-2399 !$#title Sites and gene products involved in lambdoid phage DNA !1packaging. !$#cross-references MUID:93224462; PMID:8468297 !$#accession C49849 !'##status preliminary !'##molecule_type DNA !'##residues 1-27 ##label SM2 !'##note sequence extracted from NCBI backbone (NCBIN:129221, !1NCBIP:129224) GENETICS !$#gene 3 CLASSIFICATION #superfamily phage lambda head-to-tail joining protein W KEYWORDS head protein SUMMARY #length 68 #molecular-weight 7621 #checksum 1140 SEQUENCE /// ENTRY JQBPT7 #type complete TITLE head-to-tail joining protein - phage T7 ORGANISM #formal_name phage T7 DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS A04354; S42323 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession A04354 !'##molecule_type DNA !'##residues 1-536 ##label DUN REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42323 !'##molecule_type DNA !'##residues 1-536 ##label DUW !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24425.1; !1PID:g15602 !'##note the authors did not translate the codon for residue 1 GENETICS !$#gene 8 !$#map_position 50.68-54.70 CLASSIFICATION #superfamily phage T7 head-to-tail joining protein SUMMARY #length 536 #molecular-weight 59120 #checksum 3485 SEQUENCE /// ENTRY TJBPKL #type complete TITLE tail assembly protein K - phage lambda ORGANISM #formal_name phage lambda DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS H43009; G43013; A04355 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession H43009 !'##molecule_type DNA !'##residues 1-199 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession G43013 !'##molecule_type DNA !'##residues 1-199 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96551.1; PID:g215123 !'##note there are two possible initiation sites for gene K translation, !1the codon for 1-Met and that for 11-Met COMMENT Gene K protein is involved in the assembly of the initiator !1complex for tail polymerization. It has not been found in !1the mature phage. GENETICS !$#gene K !$#map_position 29.43-30.66 CLASSIFICATION #superfamily phage lambda tail assembly protein K SUMMARY #length 199 #molecular-weight 23011 #checksum 9747 SEQUENCE /// ENTRY TJBPIL #type complete TITLE tail assembly protein I - phage lambda ORGANISM #formal_name phage lambda DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS A43008; H43013; A04356 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession A43008 !'##molecule_type DNA !'##residues 1-223 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession H43013 !'##molecule_type DNA !'##residues 1-223 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96552.1; PID:g215124 !'##note there are three possible initiation sites for gene I !1translation, the ATG codons corresponding to 1-Met and !114-Met and the GTG codon corresponding to 34-Val COMMENT Gene I protein is involved in the assembly of the initiator !1complex for tail polymerization. It has not been found in !1the mature phage. GENETICS !$#gene I !$#map_position 30.46-31.84 CLASSIFICATION #superfamily phage lambda tail assembly protein I SUMMARY #length 223 #molecular-weight 23123 #checksum 9074 SEQUENCE /// ENTRY TLBPZL #type complete TITLE minor tail protein Z - phage lambda ORGANISM #formal_name phage lambda DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS B43008; I43013; A04357 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession B43008 !'##molecule_type DNA !'##residues 1-192 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession I43013 !'##molecule_type DNA !'##residues 1-192 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96543.1; PID:g215115 !'##note the codon corresponding to 1-Met is the most probable of three !1possible translational start sites COMMENT Gene Z protein is a minor tail component, located at the !1proximal end; in conjunction with protein U, it is involved !1in the termination of tail-tube polymerization. GENETICS !$#gene Z !$#map_position 16.45-17.63 CLASSIFICATION #superfamily phage lambda minor tail protein Z SUMMARY #length 192 #molecular-weight 21560 #checksum 2254 SEQUENCE /// ENTRY TLBPUL #type complete TITLE minor tail protein U - phage lambda ORGANISM #formal_name phage lambda DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS C43008; A43014; A04358 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession C43008 !'##molecule_type DNA !'##residues 1-131 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession A43014 !'##molecule_type DNA !'##residues 1-131 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96544.1; PID:g215116 COMMENT Gene U protein is a minor tail component, located at the !1proximal end; in conjunction with protein Z, it is involved !1in the termination of tail-tube polymerization. GENETICS !$#gene U !$#map_position 17.63-18.44 CLASSIFICATION #superfamily phage lambda minor tail protein U SUMMARY #length 131 #molecular-weight 14649 #checksum 1848 SEQUENCE /// ENTRY TLBPVL #type complete TITLE major tail protein V - phage lambda ORGANISM #formal_name phage lambda DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS D43008; B43014; A04359 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession D43008 !'##molecule_type DNA !'##residues 1-246 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession B43014 !'##molecule_type DNA !'##residues 1-246 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96545.1; PID:g215117 COMMENT Gene V protein is the major component of the tail. It makes !1up the tubular portion of the tail, which is composed of !1about 32 hexameric discs. There are 135-212 copies of gene V !1protein per mature phage. GENETICS !$#gene V !$#map_position 18.46-19.98 CLASSIFICATION #superfamily phage lambda major tail protein V SUMMARY #length 246 #molecular-weight 25810 #checksum 2405 SEQUENCE /// ENTRY TLBPGL #type complete TITLE minor tail protein G - phage lambda ORGANISM #formal_name phage lambda DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS E43008; C43014; A04360 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession E43008 !'##molecule_type DNA !'##residues 1-140 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession C43014 !'##molecule_type DNA !'##residues 1-140 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96546.1; PID:g215118 !'##note there are only two possible initiation sites for gene G !1translation, the codon for 1-Met and the GTG codon !1corresponding to 13-Val REFERENCE S38947 !$#authors Levin, M.E.; Hendrix, R.W.; Casjens, S.R. !$#journal J. Mol. Biol. (1993) 234:124-139 !$#title A programmed translational frameshift is required for the !1synthesis of a bacteriophage lambda tail assembly protein. !$#cross-references MUID:94047055; PMID:8230192 !$#contents annotation !$#note confirmed initiation site, nature of longer gene product COMMENT Gene G protein is a minor tail protein, located at the !1distal end. It is involved in the assembly of the initiator !1complex for tail polymerization. COMMENT For the longer G-T protein, see PIR:TLBPTL. GENETICS !$#gene G !$#map_position 20.02-20.89 CLASSIFICATION #superfamily phage lambda minor tail protein G KEYWORDS tail protein SUMMARY #length 140 #molecular-weight 15607 #checksum 9688 SEQUENCE /// ENTRY TLBPTL #type complete TITLE minor tail protein G-T - phage lambda ALTERNATE_NAMES gene G-T protein; minor tail protein T [misidentification] ORGANISM #formal_name phage lambda DATE 13-Jun-1983 #sequence_revision 23-Oct-1998 #text_change 04-Feb-2000 ACCESSIONS C43014; D43014; E43008; F43008; S38947; A04360; A04361 REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession C43014 !'##molecule_type DNA !'##residues 1-135,'CSTVS' ##label SAN1 !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96546.1; PID:g215118 !'##note there are only two possible initiation sites for gene G !1translation, the codon for 1-Met and the GTG codon !1corresponding to 13-Val; however, the protein identified as !1the gene G product has a molecular weight of about 33K, !1which is more than double that of the proteins produced from !1either start site !$#accession D43014 !'##molecule_type DNA !'##residues 'M',137-279 ##label SAN2 !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96547.1; PID:g215119 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession E43008 !'##molecule_type DNA !'##residues 1-135,'CSTVS' ##label DAN1 !$#accession F43008 !'##molecule_type DNA !'##residues 'M',137-279 ##label DAN2 REFERENCE S38947 !$#authors Levin, M.E.; Hendrix, R.W.; Casjens, S.R. !$#journal J. Mol. Biol. (1993) 234:124-139 !$#title A programmed translational frameshift is required for the !1synthesis of a bacteriophage lambda tail assembly protein. !$#cross-references MUID:94047055; PMID:8230192 !$#accession S38947 !'##molecule_type protein !'##residues 1-6,'X',8-16 ##label LEV !'##note confirms initiation site of G protein, translational frameshift !1for the G-T protein COMMENT Gene G-T protein is a minor protein required for tail !1assembly. It is a 31.2 kDa protein produced at a 4% !1expression rate for the G gene by a minus-one translational !1frameshift believed to occur at a slippage heptamer GGGAAAG !1encoding residues Gly-Lys at 134-135. The sequence !1previously reported for the T gene is now thought not to be !1expressed. For the minor tail protein G, see PIR:TLBPGL. GENETICS !$#gene G-T !$#map_position 20.02-21.74 CLASSIFICATION #superfamily phage lambda minor tail protein G-T KEYWORDS translational frameshift FEATURE !$134-135 #region minus-one translational frameshift SUMMARY #length 279 #molecular-weight 31171 #checksum 1991 SEQUENCE /// ENTRY TLBPHL #type complete TITLE minor tail protein precursor H - phage lambda ORGANISM #formal_name phage lambda DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS G43008; E43014; A04362 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession G43008 !'##molecule_type DNA !'##residues 1-853 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession E43014 !'##molecule_type DNA !'##residues 1-853 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96548.1; PID:g215120 !'##note the amino end of protein H* was determined by partial sequence !1analysis to correspond to 1-Met; thus maturation of the H !1protein does not involve cleavage at the amino end COMMENT Gene H protein is cleaved to form minor tail protein H*, !1located at the distal end. There are 6-7 copies of protein !1H* per mature phage. This protein is believed to function in !1the injection of lambda DNA into the host cell during early !1infection. COMMENT Gene H protein functions in the assembly of the tail !1polymerization initiator complex and is postulated to act as !1a template to determine the tail length. GENETICS !$#gene H !$#map_position 21.74-27.01 CLASSIFICATION #superfamily phage lambda minor tail protein H SUMMARY #length 853 #molecular-weight 92280 #checksum 2824 SEQUENCE /// ENTRY TLBPML #type complete TITLE minor tail protein M - phage lambda ORGANISM #formal_name phage lambda DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS I43008; F43014; A04363 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession I43008 !'##molecule_type DNA !'##residues 1-109 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession F43014 !'##molecule_type DNA !'##residues 1-109 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96549.1; PID:g215121 !'##note the codon corresponding to 1-Met is the most probable of five !1possible translational start sites for gene M COMMENT Gene M protein is a minor tail protein, located at the !1distal end, and is involved in the assembly of the initiator !1complex for tail polymerization. It acts to stabilize the !1complex. GENETICS !$#gene M !$#map_position 27.01-27.68 CLASSIFICATION #superfamily phage lambda minor tail protein M SUMMARY #length 109 #molecular-weight 12530 #checksum 6572 SEQUENCE /// ENTRY TLBPLL #type complete TITLE minor tail protein L - phage lambda ORGANISM #formal_name phage lambda DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS A43009; G43014; A04364 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession A43009 !'##molecule_type DNA !'##residues 1-232 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession G43014 !'##molecule_type DNA !'##residues 1-232 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96550.1; PID:g215122 COMMENT Gene L protein is a minor tail protein, located at the !1distal end. It is involved in the assembly of the initiator !1complex for tail polymerization. GENETICS !$#gene L !$#map_position 27.69-29.12 CLASSIFICATION #superfamily phage lambda minor tail protein L SUMMARY #length 232 #molecular-weight 25709 #checksum 8452 SEQUENCE /// ENTRY TLBP22 #type complete TITLE tail protein - phage P22 ORGANISM #formal_name phage P22 #note host Salmonella typhimurium DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 07-Nov-1997 ACCESSIONS A18750 REFERENCE A18750 !$#authors Sauer, R.T.; Krovatin, W.; Poteete, A.R.; Berget, P.B. !$#journal Biochemistry (1982) 21:5811-5815 !$#title Phage P22 tail protein: gene and amino acid sequence. !$#cross-references MUID:83101218; PMID:6295443 !$#accession A18750 !'##molecule_type DNA !'##residues 1-667 ##label SAU !'##cross-references GB:J02473; NID:g215314 GENETICS !$#gene 9 CLASSIFICATION #superfamily phage P22 tail protein KEYWORDS tail protein SUMMARY #length 667 #molecular-weight 71856 #checksum 1932 SEQUENCE /// ENTRY TLBP84 #type complete TITLE tail fiber assembly protein gp38 - phage T4 ORGANISM #formal_name phage T4 DATE 06-Jul-1982 #sequence_revision 31-Mar-1990 #text_change 24-Sep-1999 ACCESSIONS A94692; A92877; A04365; A94612; JS0288; JS0367 REFERENCE A94692 !$#authors Montag, D.; Riede, I.; Eschbach, M.L.; Degen, M.; Henning, !1U. !$#journal J. Mol. Biol. (1987) 196:165-174 !$#title Receptor-recognizing proteins of T-even type bacteriophages. !1Constant and hypervariable regions and an unusual case of !1evolution. !$#cross-references MUID:88011316; PMID:2958637 !$#accession A94692 !'##molecule_type DNA !'##residues 1-183 ##label MON !'##cross-references GB:X05677; NID:g15306; PIDN:CAA29163.1; PID:g15307 REFERENCE A92877 !$#authors Oliver, D.B.; Crowther, R.A. !$#journal J. Mol. Biol. (1981) 153:545-568 !$#title DNA sequence of the tail fibre genes 36 and 37 of !1bacteriophge T4. !$#cross-references MUID:82170495; PMID:7338921 !$#accession A92877 !'##molecule_type DNA !'##residues 1-132 ##label OLI !'##cross-references GB:V00863; GB:J02508; GB:J02509; NID:g15371; !1PIDN:CAA24229.1; PID:g15375 REFERENCE A94612 !$#authors Crowther, R.A. !$#submission submitted to the Nucleic Acid Sequence Database, June 1982 !$#contents annotation; revision to residue 72 COMMENT The gene gp38 product is involved in the assembly of the !1distal-half tail fiber of bacteriophage T4. It is necessary !1for the maturation of protein gp37 to the dimeric structural !1subunit P37. See the entries for tail fiber proteins gp35 !1(PIR:TLBP54), gp36 (PIR:TLBP64), and gp37 (PIR:TLBP74). GENETICS !$#gene 38 !$#map_position 157.410-158.160 CLASSIFICATION #superfamily phage T4 tail fiber assembly protein gp38 SUMMARY #length 183 #molecular-weight 22310 #checksum 2560 SEQUENCE /// ENTRY QXBP3L #type complete TITLE hypothetical protein A-194 - phage lambda ORGANISM #formal_name phage lambda DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS B43009; H43014; A04366 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession B43009 !'##molecule_type DNA !'##residues 1-194 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession H43014 !'##molecule_type DNA !'##residues 1-194 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96558.1; PID:g215129 GENETICS !$#map_position 45.30-46.50 CLASSIFICATION #superfamily phage T4 tail fiber assembly protein gp38 SUMMARY #length 194 #molecular-weight 21602 #checksum 6014 SEQUENCE /// ENTRY TLBP54 #type complete TITLE tail fiber protein gp35 - phage T4 ORGANISM #formal_name phage T4 DATE 06-Jul-1982 #sequence_revision 19-Apr-1996 #text_change 24-Sep-1999 ACCESSIONS JT0577; A04367 REFERENCE JT0576 !$#authors Mesyanzhinov, V.V. !$#submission submitted to JIPID, April 1991 !$#accession JT0577 !'##status preliminary !'##molecule_type protein !'##residues 1-275 ##label MES REFERENCE A92877 !$#authors Oliver, D.B.; Crowther, R.A. !$#journal J. Mol. Biol. (1981) 153:545-568 !$#title DNA sequence of the tail fibre genes 36 and 37 of !1bacteriophge T4. !$#cross-references MUID:82170495; PMID:7338921 !$#accession A04367 !'##molecule_type DNA !'##residues 218-275 ##label OLI !'##cross-references GB:V00863; GB:J02508; GB:J02509; NID:g15371; !1PIDN:CAA24226.1; PID:g836604 !'##note the gene gp35 product was identified on the basis of its map !1position GENETICS !$#gene gp35 !$#map_position 91.6-92.3 COMPLEX the distal half-fiber contains two molecules each of gp36 !1(PIR:TLBP64) and gp37 (PIR:TLBP74), and one molecule of gp35 CLASSIFICATION #superfamily phage T4 tail fiber protein gp35 KEYWORDS structural protein; tail fiber SUMMARY #length 275 #molecular-weight 30237 #checksum 7602 SEQUENCE /// ENTRY TLBP64 #type complete TITLE tail fiber protein gp36 - phage T4 ORGANISM #formal_name phage T4 DATE 06-Jul-1982 #sequence_revision 06-Jul-1982 #text_change 24-Sep-1999 ACCESSIONS A04368 REFERENCE A92877 !$#authors Oliver, D.B.; Crowther, R.A. !$#journal J. Mol. Biol. (1981) 153:545-568 !$#title DNA sequence of the tail fibre genes 36 and 37 of !1bacteriophge T4. !$#cross-references MUID:82170495; PMID:7338921 !$#accession A04368 !'##molecule_type DNA !'##residues 1-221 ##label OLI !'##cross-references GB:V00863; GB:J02508; GB:J02509; NID:g15371; !1PIDN:CAA24227.1; PID:g15373 !'##note the gene gp36 product was identified by the genetic mapping of !1two gene gp36 mutants within the coding region; the !1calculated molecular weight of this sequence agrees with the !1reported molecular weight of 24,000 for this protein GENETICS !$#gene gp36 !$#map_position 92.3-92.6 COMPLEX the distal half-fiber contains two molecules each of gp36 !1and gp37 (PIR:TLBP74), and one molecule of gp35 (PIR:TLBP54) CLASSIFICATION #superfamily phage T4 tail fiber protein gp36 KEYWORDS structural protein; tail fiber SUMMARY #length 221 #molecular-weight 23342 #checksum 4319 SEQUENCE /// ENTRY TLBPT2 #type complete TITLE tail fiber protein gp36 - phage T2 ORGANISM #formal_name phage T2 #note host Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 23-Jul-1999 ACCESSIONS A23056 REFERENCE A93582 !$#authors Riede, I.; Drexler, K.; Eschbach, M.L. !$#journal Nucleic Acids Res. (1985) 13:605-616 !$#title The nucleotide sequences of the tail fiber gene 36 of !1bacteriophage T2 and of genes 36 of the T-even type !1Escherichia coli phages K3 and Ox2. !$#cross-references MUID:85215500; PMID:4000929 !$#accession A23056 !'##molecule_type DNA !'##residues 1-219 ##label RIE !'##cross-references GB:X01755; NID:g15189; PIDN:CAA25897.1; PID:g15191 GENETICS !$#gene 36 CLASSIFICATION #superfamily phage T4 tail fiber protein gp36 KEYWORDS tail fiber SUMMARY #length 219 #molecular-weight 23488 #checksum 8273 SEQUENCE /// ENTRY TLBPK3 #type complete TITLE tail fiber protein gp36 - phage K3 ORGANISM #formal_name phage K3 #note host Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 23-Jul-1999 ACCESSIONS B23056 REFERENCE A93582 !$#authors Riede, I.; Drexler, K.; Eschbach, M.L. !$#journal Nucleic Acids Res. (1985) 13:605-616 !$#title The nucleotide sequences of the tail fiber gene 36 of !1bacteriophage T2 and of genes 36 of the T-even type !1Escherichia coli phages K3 and Ox2. !$#cross-references MUID:85215500; PMID:4000929 !$#accession B23056 !'##molecule_type DNA !'##residues 1-230 ##label RIE !'##cross-references GB:X01754; NID:g15108; PIDN:CAA25894.1; PID:g15109 GENETICS !$#gene 36 CLASSIFICATION #superfamily phage T4 tail fiber protein gp36 KEYWORDS tail fiber SUMMARY #length 230 #molecular-weight 24747 #checksum 5943 SEQUENCE /// ENTRY TLBPX2 #type complete TITLE tail fiber protein gp36 - phage Ox2 ORGANISM #formal_name phage Ox2 #note host Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 23-Jul-1999 ACCESSIONS C23056 REFERENCE A93582 !$#authors Riede, I.; Drexler, K.; Eschbach, M.L. !$#journal Nucleic Acids Res. (1985) 13:605-616 !$#title The nucleotide sequences of the tail fiber gene 36 of !1bacteriophage T2 and of genes 36 of the T-even type !1Escherichia coli phages K3 and Ox2. !$#cross-references MUID:85215500; PMID:4000929 !$#accession C23056 !'##molecule_type DNA !'##residues 1-216 ##label RIE !'##cross-references GB:X01753; NID:g15122; PIDN:CAA25891.1; PID:g15123 GENETICS !$#gene 36 CLASSIFICATION #superfamily phage T4 tail fiber protein gp36 KEYWORDS tail fiber SUMMARY #length 216 #molecular-weight 22713 #checksum 2082 SEQUENCE /// ENTRY TLBP74 #type complete TITLE tail fiber protein gp37 - phage T4 ORGANISM #formal_name phage T4 DATE 06-Jul-1982 #sequence_revision 06-Jul-1982 #text_change 24-Sep-1999 ACCESSIONS A04369 REFERENCE A92877 !$#authors Oliver, D.B.; Crowther, R.A. !$#journal J. Mol. Biol. (1981) 153:545-568 !$#title DNA sequence of the tail fibre genes 36 and 37 of !1bacteriophge T4. !$#cross-references MUID:82170495; PMID:7338921 !$#accession A04369 !'##molecule_type DNA !'##residues 1-1026 ##label OLI !'##cross-references GB:V00863; GB:J02508; GB:J02509; NID:g15371; !1PIDN:CAA24228.1; PID:g15374 !'##note the gene gp37 protein was identified on the basis of its !1composition and the genetic mapping of four gene gp37 !1mutants within the coding region COMMENT The tail fiber of bacteriophage T4 is about 1600 angstroms !1long with a kink in the middle that divides the fiber into !1proximal and distal halves. The thin tip of the distal !1half-fiber interacts with the bacterial lipopolysaccharide !1receptor and specifies the host range of the phage. COMMENT The two gp37 protein chains run in parallel, the length of !1the distal half-fiber, with the amino end near the center !1kink of the fiber and the carboxyl end at the distal tip. !1The other polypeptides are distributed uniformly along the !1length of the distal half-fiber. GENETICS !$#gene gp37 !$#map_position 92.6-94.5 COMPLEX the distal half-fiber contains two molecules each of gp36 !1(PIR:TLBP64) and gp37, and one molecule of gp35 (PIR:TLBP54) CLASSIFICATION #superfamily phage T4 tail fiber protein gp37 KEYWORDS structural protein; tail fiber SUMMARY #length 1026 #molecular-weight 109224 #checksum 7271 SEQUENCE /// ENTRY QXBP2L #type complete TITLE hypothetical protein B-314 - phage lambda ORGANISM #formal_name phage lambda DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS C43009; I43014; A04370 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession C43009 !'##molecule_type DNA !'##residues 1-314 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession I43014 !'##molecule_type DNA !'##residues 1-314 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96557.1; PID:g215128 GENETICS !$#map_position 43.39-45.30 CLASSIFICATION #superfamily phage T4 tail fiber protein gp37 SUMMARY #length 314 #molecular-weight 32019 #checksum 3780 SEQUENCE /// ENTRY TLBP2X #type complete TITLE tail fiber protein gp38 - phage Ox2 ALTERNATE_NAMES receptor recognition protein gp38 ORGANISM #formal_name phage Ox2 DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 23-Jul-1999 ACCESSIONS JS0286 REFERENCE A94692 !$#authors Montag, D.; Riede, I.; Eschbach, M.L.; Degen, M.; Henning, !1U. !$#journal J. Mol. Biol. (1987) 196:165-174 !$#title Receptor-recognizing proteins of T-even type bacteriophages. !1Constant and hypervariable regions and an unusual case of !1evolution. !$#cross-references MUID:88011316; PMID:2958637 !$#accession JS0286 !'##molecule_type DNA !'##residues 1-266 ##label MON !'##cross-references GB:X05675; NID:g15124; PIDN:CAA29158.1; PID:g15126 GENETICS !$#gene 38 CLASSIFICATION #superfamily phage Ox2 tail fiber protein gp38 KEYWORDS tail fiber SUMMARY #length 266 #molecular-weight 27036 #checksum 6577 SEQUENCE /// ENTRY TLBPM1 #type complete TITLE tail fiber protein gp38 - phage M1 ALTERNATE_NAMES receptor recognition protein gp38 ORGANISM #formal_name phage M1 DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 23-Jul-1999 ACCESSIONS JS0287 REFERENCE A94692 !$#authors Montag, D.; Riede, I.; Eschbach, M.L.; Degen, M.; Henning, !1U. !$#journal J. Mol. Biol. (1987) 196:165-174 !$#title Receptor-recognizing proteins of T-even type bacteriophages. !1Constant and hypervariable regions and an unusual case of !1evolution. !$#cross-references MUID:88011316; PMID:2958637 !$#accession JS0287 !'##molecule_type DNA !'##residues 1-262 ##label MON !'##cross-references GB:X05676; NID:g15114; PIDN:CAA29161.1; PID:g15116 GENETICS !$#gene 38 CLASSIFICATION #superfamily phage Ox2 tail fiber protein gp38 KEYWORDS tail fiber SUMMARY #length 262 #molecular-weight 26291 #checksum 8286 SEQUENCE /// ENTRY TLBP3X #type fragment TITLE tail fiber protein gp37 - phage Ox2 (fragment) ORGANISM #formal_name phage Ox2 DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 23-Jul-1999 ACCESSIONS PS0062 REFERENCE A94692 !$#authors Montag, D.; Riede, I.; Eschbach, M.L.; Degen, M.; Henning, !1U. !$#journal J. Mol. Biol. (1987) 196:165-174 !$#title Receptor-recognizing proteins of T-even type bacteriophages. !1Constant and hypervariable regions and an unusual case of !1evolution. !$#cross-references MUID:88011316; PMID:2958637 !$#accession PS0062 !'##molecule_type DNA !'##residues 1-251 ##label MON !'##cross-references GB:X05675; NID:g15124; PIDN:CAA29157.1; PID:g15125 !'##note the authors translated the codon CAA for residue 95 as Asn GENETICS !$#gene 38 CLASSIFICATION #superfamily phage Ox2 tail fiber protein gp37 KEYWORDS tail fiber SUMMARY #length 251 #checksum 5856 SEQUENCE /// ENTRY TLBP1M #type fragment TITLE tail fiber protein gp37 - phage M1 (fragment) ORGANISM #formal_name phage M1 DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 23-Jul-1999 ACCESSIONS PS0064 REFERENCE A94692 !$#authors Montag, D.; Riede, I.; Eschbach, M.L.; Degen, M.; Henning, !1U. !$#journal J. Mol. Biol. (1987) 196:165-174 !$#title Receptor-recognizing proteins of T-even type bacteriophages. !1Constant and hypervariable regions and an unusual case of !1evolution. !$#cross-references MUID:88011316; PMID:2958637 !$#accession PS0064 !'##molecule_type DNA !'##residues 1-251 ##label MON !'##cross-references GB:X05676; NID:g15114; PIDN:CAA29160.1; PID:g15115 GENETICS !$#gene 38 CLASSIFICATION #superfamily phage Ox2 tail fiber protein gp37 KEYWORDS tail fiber SUMMARY #length 251 #checksum 4929 SEQUENCE /// ENTRY TLBPA7 #type complete TITLE tail tubular protein A - phage T7 ALTERNATE_NAMES gene 11 protein ORGANISM #formal_name phage T7 DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS A04371; S42327 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession A04371 !'##molecule_type DNA !'##residues 1-196 ##label DUN REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42327 !'##molecule_type DNA !'##residues 1-196 ##label DU2 !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24429.1; !1PID:g15605 GENETICS !$#gene 11 !$#map_position 60.66-62.13 CLASSIFICATION #superfamily phage T7 tail tubular protein A KEYWORDS tail protein SUMMARY #length 196 #molecular-weight 22289 #checksum 3868 SEQUENCE /// ENTRY TLBPB7 #type complete TITLE tail tubular protein B - phage T7 ORGANISM #formal_name phage T7 DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS A04372; S42328 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession A04372 !'##molecule_type DNA !'##residues 1-794 ##label DUN REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42328 !'##molecule_type DNA !'##residues 1-794 ##label DUW !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24430.1; !1PID:g15606 !'##note the authors did not translate the codon for residue 1 GENETICS !$#gene 12 !$#map_position 62.20-68.16 CLASSIFICATION #superfamily phage T7 tail tubular protein B SUMMARY #length 794 #molecular-weight 89395 #checksum 8457 SEQUENCE /// ENTRY TLBPF7 #type complete TITLE tail fiber protein - phage T7 ORGANISM #formal_name phage T7 DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS A04373; S42333 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession A04373 !'##molecule_type DNA !'##residues 1-553 ##label DUN REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42333 !'##molecule_type DNA !'##residues 1-553 ##label DUW !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24435.1; !1PID:g15611 !'##note the authors did not translate the codon for residue 1 GENETICS !$#gene 17 !$#map_position 86.70-90.85 CLASSIFICATION #superfamily phage T7 tail fiber protein KEYWORDS tail fiber SUMMARY #length 553 #molecular-weight 61572 #checksum 1138 SEQUENCE /// ENTRY TLBPT3 #type complete TITLE tail fiber protein - phage T3 ORGANISM #formal_name phage T3 #note host Escherichia coli DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 23-Jul-1999 ACCESSIONS A23476 REFERENCE A94339 !$#authors Yamada, M.; Fujisawa, H.; Kato, H.; Hamada, K.; Minagawa, T. !$#journal Virology (1986) 151:350-361 !$#title Cloning and sequencing of the genetic right end of !1bacteriophage T3 DNA. !$#cross-references MUID:86209997; PMID:3010556 !$#accession A23476 !'##molecule_type DNA !'##residues 1-557 ##label YAM !'##cross-references GB:M14784; NID:g215810; PIDN:AAA92523.1; !1PID:g215811 REFERENCE A94344 !$#authors Yamada, M.; Fujisawa, H.; Kato, H.; Hamada, K.; Minagawa, T. !$#journal Virology (1986) 154:246 !$#contents annotation; erratum; corrections to coding regions GENETICS !$#gene 17 CLASSIFICATION #superfamily phage T7 tail fiber protein KEYWORDS tail fiber SUMMARY #length 557 #molecular-weight 61801 #checksum 9639 SEQUENCE /// ENTRY ZYBPT5 #type complete TITLE tail protein pb5 - phage T5 ORGANISM #formal_name phage T5 #note host Escherichia coli DATE 31-Mar-1993 #sequence_revision 31-Mar-1993 #text_change 23-Jul-1999 ACCESSIONS A38181; S44990 REFERENCE A38181 !$#authors Krauel, V.; Heller, K.J. !$#journal J. Bacteriol. (1991) 173:1287-1297 !$#title Cloning, sequencing, and recombinational analysis with !1bacteriophage BF23 of the bacteriophage T5 oad gene encoding !1the receptor-binding protein. !$#cross-references MUID:91123205; PMID:1825083 !$#accession A38181 !'##molecule_type DNA !'##residues 1-640 ##label KRA !'##cross-references GB:M62847; NID:g215973; PIDN:AAA32559.1; !1PID:g215974 REFERENCE S44984 !$#authors Decker, K.; Krauel, V.; Meesmann, A.; Heller, K.J. !$#journal Mol. Microbiol. (1994) 12:321-332 !$#title Lytic conversion of Escherichia coli by bacteriophage T5: !1blocking of the FhuA receptor protein by a lipoprotein !1expressed early during infection. !$#cross-references MUID:94335651; PMID:8057856 !$#accession S44990 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-20 ##label DEC !'##cross-references EMBL:X75922 !'##experimental_source strain T5st(H) !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1993 GENETICS !$#gene oad CLASSIFICATION #superfamily phage T5 tail protein pb5 KEYWORDS tail protein SUMMARY #length 640 #molecular-weight 68756 #checksum 3407 SEQUENCE /// ENTRY QSBPL #type complete TITLE host specificity protein J - phage lambda ORGANISM #formal_name phage lambda DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS D43009; A43015; A04374 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession D43009 !'##molecule_type DNA !'##residues 1-1132 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession A43015 !'##molecule_type DNA !'##residues 1-1132 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96553.1; PID:g215125 COMMENT Gene J protein makes up the distal fiber of the phage tail. !1It is responsible for adsorption to the host during !1infection and determines host specificity. It specifically !1binds to the lambda receptor protein of E. coli K12. This !1receptor protein encoded by E. coli gene lamB is an outer !1membrane protein that functions in the transport of maltose !1and maltodextrins. COMMENT Under the action of the gene G, T, H, M, L, K, and I !1proteins, gene J protein serves as the initiator of tail !1polymerization. There are 2-4 copies of protein J per mature !1phage. GENETICS !$#gene J !$#map_position 31.97-38.97 CLASSIFICATION #superfamily phage lambda host specificity protein J SUMMARY #length 1132 #molecular-weight 124421 #checksum 1868 SEQUENCE /// ENTRY QSBPA7 #type complete TITLE host specificity protein A - phage T7 ORGANISM #formal_name phage T7 DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS A04375; S42320 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession A04375 !'##molecule_type DNA !'##residues 1-133 ##label DUN REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42320 !'##molecule_type DNA !'##residues 1-133 ##label DUW !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24422.1; !1PID:g15599 !'##note the authors did not translate the codon for residue 1 GENETICS !$#gene 7 !$#map_position 47.90-48.90 CLASSIFICATION #superfamily phage T7 host specificity protein A SUMMARY #length 133 #molecular-weight 15435 #checksum 3514 SEQUENCE /// ENTRY QSBPB7 #type complete TITLE host specificity protein B - phage T7 ORGANISM #formal_name phage T7 DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS A04376; S42321 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession A04376 !'##molecule_type DNA !'##residues 1-99 ##label DUN REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42321 !'##molecule_type DNA !'##residues 1-99 ##label DUW !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24423.1; !1PID:g15600 !'##note the authors did not translate the codon for residue 1 GENETICS !$#gene 7.3 !$#map_position 48.91-49.65 CLASSIFICATION #superfamily phage T7 host specificity protein B SUMMARY #length 99 #molecular-weight 10069 #checksum 2650 SEQUENCE /// ENTRY PQBP82 #type complete TITLE antiterminator Q - phage 82 ALTERNATE_NAMES regulatory protein Q ORGANISM #formal_name phage 82 DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 23-Jul-1999 ACCESSIONS A29791; S66585 REFERENCE A29791 !$#authors Goliger, J.A.; Roberts, J.W. !$#journal J. Biol. Chem. (1987) 262:11721-11725 !$#title Bacteriophage 82 gene Q and Q protein: sequence, !1overproduction, and activity as a transcription !1antiterminator in vitro. !$#cross-references MUID:87308148; PMID:3624233 !$#accession A29791 !'##molecule_type DNA !'##residues 1-229 ##label GOL !'##cross-references GB:J02803; NID:g215364; PIDN:AAA32298.1; !1PID:g215365 !'##note the authors translated the codon ACT for residue 188 as Phe and !1GAA for residue 189 as Thr REFERENCE S66579 !$#authors Mahdi, A.A.; Sharples, G.J.; Mandal, T.N.; Lloyd, R.G. !$#journal J. Mol. Biol. (1996) 257:561-573 !$#title Holliday junction resolvases encoded by homologous rusA !1genes in Escherichia coli K-12 and phage 82. !$#cross-references MUID:96196428; PMID:8648624 !$#accession S66585 !'##molecule_type DNA !'##residues 1-229 ##label MAH !'##cross-references EMBL:X92588; NID:g1051111; PIDN:CAA63332.1; !1PID:g1051118 GENETICS !$#gene Q CLASSIFICATION #superfamily phage 82 regulatory protein Q KEYWORDS DNA binding; late protein; transcription regulation SUMMARY #length 229 #molecular-weight 26400 #checksum 9335 SEQUENCE /// ENTRY S66580 #type complete TITLE hypothetical protein ybcN - phage 82 ORGANISM #formal_name phage 82 DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 15-Oct-1999 ACCESSIONS S66580 REFERENCE S66579 !$#authors Mahdi, A.A.; Sharples, G.J.; Mandal, T.N.; Lloyd, R.G. !$#journal J. Mol. Biol. (1996) 257:561-573 !$#title Holliday junction resolvases encoded by homologous rusA !1genes in Escherichia coli K-12 and phage 82. !$#cross-references MUID:96196428; PMID:8648624 !$#accession S66580 !'##molecule_type DNA !'##residues 1-151 ##label MAH !'##cross-references EMBL:X92588; NID:g1051111; PIDN:CAA63327.1; !1PID:g1051113 !'##note the authors translated the codon CGC for residue 40 as Ala GENETICS !$#start_codon GTG CLASSIFICATION #superfamily phage 82 hypothetical protein ybcN SUMMARY #length 151 #molecular-weight 17463 #checksum 8416 SEQUENCE /// ENTRY S66587 #type complete TITLE hypothetical protein ybcN - Escherichia coli (strain K-12) cryptic lambdoid prophage DLP12 ALTERNATE_NAMES protein 151 ORGANISM #formal_name Escherichia coli DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 01-Mar-2002 ACCESSIONS S66587; A64787 REFERENCE S66579 !$#authors Mahdi, A.A.; Sharples, G.J.; Mandal, T.N.; Lloyd, R.G. !$#journal J. Mol. Biol. (1996) 257:561-573 !$#title Holliday junction resolvases encoded by homologous rusA !1genes in Escherichia coli K-12 and phage 82. !$#cross-references MUID:96196428; PMID:8648624 !$#accession S66587 !'##molecule_type DNA !'##residues 1-151 ##label MAH !'##cross-references EMBL:X92587; NID:g1051136; PIDN:CAA63318.1; !1PID:g1051138 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64787 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-151 ##label BLAT !'##cross-references GB:AE000160; GB:U00096; NID:g1786751; !1PIDN:AAC73648.1; PID:g1786759; UWGP:b0547 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ybcN !$#map_position 12 min !$#genome prophage !$#start_codon GTG CLASSIFICATION #superfamily phage 82 hypothetical protein ybcN SUMMARY #length 151 #molecular-weight 17433 #checksum 8236 SEQUENCE /// ENTRY S66581 #type complete TITLE ninE protein - phage 82 ORGANISM #formal_name phage 82 DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 15-Oct-1999 ACCESSIONS S66581 REFERENCE S66579 !$#authors Mahdi, A.A.; Sharples, G.J.; Mandal, T.N.; Lloyd, R.G. !$#journal J. Mol. Biol. (1996) 257:561-573 !$#title Holliday junction resolvases encoded by homologous rusA !1genes in Escherichia coli K-12 and phage 82. !$#cross-references MUID:96196428; PMID:8648624 !$#accession S66581 !'##molecule_type DNA !'##residues 1-56 ##label MAH !'##cross-references EMBL:X92588; NID:g1051111; PIDN:CAA63328.1; !1PID:g1051114 CLASSIFICATION #superfamily phage 82 ninE protein SUMMARY #length 56 #molecular-weight 6493 #checksum 2721 SEQUENCE /// ENTRY S66588 #type complete TITLE ninE protein - Escherichia coli (strain K-12) cryptic lambdoid prophage DLP12 ALTERNATE_NAMES protein 56 ORGANISM #formal_name Escherichia coli DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 01-Mar-2002 ACCESSIONS S66588; B64787 REFERENCE S66579 !$#authors Mahdi, A.A.; Sharples, G.J.; Mandal, T.N.; Lloyd, R.G. !$#journal J. Mol. Biol. (1996) 257:561-573 !$#title Holliday junction resolvases encoded by homologous rusA !1genes in Escherichia coli K-12 and phage 82. !$#cross-references MUID:96196428; PMID:8648624 !$#accession S66588 !'##molecule_type DNA !'##residues 1-56 ##label MAH !'##cross-references EMBL:X92587; NID:g1051136; PIDN:CAA63319.1; !1PID:g1051139 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64787 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-56 ##label BLAT !'##cross-references GB:AE000160; GB:U00096; NID:g1786751; !1PIDN:AAC73649.1; PID:g1786760; UWGP:b0548 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ninE !$#map_position 12 min !$#genome prophage CLASSIFICATION #superfamily phage 82 ninE protein SUMMARY #length 56 #molecular-weight 6494 #checksum 3096 SEQUENCE /// ENTRY S66584 #type complete TITLE hypothetical protein 45 - phage 82 ORGANISM #formal_name phage 82 DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 15-Oct-1999 ACCESSIONS S66584 REFERENCE S66579 !$#authors Mahdi, A.A.; Sharples, G.J.; Mandal, T.N.; Lloyd, R.G. !$#journal J. Mol. Biol. (1996) 257:561-573 !$#title Holliday junction resolvases encoded by homologous rusA !1genes in Escherichia coli K-12 and phage 82. !$#cross-references MUID:96196428; PMID:8648624 !$#accession S66584 !'##molecule_type DNA !'##residues 1-46 ##label MAH !'##cross-references EMBL:X92588; NID:g1051111; PIDN:CAA63331.1; !1PID:g1051117 CLASSIFICATION #superfamily phage 82 hypothetical protein 45 SUMMARY #length 46 #molecular-weight 5556 #checksum 2239 SEQUENCE /// ENTRY S66591 #type complete TITLE hypothetical protein 45 - Escherichia coli cryptic lambdoid prophage DLP12 ORGANISM #formal_name Escherichia coli DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 15-Oct-1999 ACCESSIONS S66591 REFERENCE S66579 !$#authors Mahdi, A.A.; Sharples, G.J.; Mandal, T.N.; Lloyd, R.G. !$#journal J. Mol. Biol. (1996) 257:561-573 !$#title Holliday junction resolvases encoded by homologous rusA !1genes in Escherichia coli K-12 and phage 82. !$#cross-references MUID:96196428; PMID:8648624 !$#accession S66591 !'##molecule_type DNA !'##residues 1-46 ##label MAH !'##cross-references EMBL:X92587; NID:g1051136; PIDN:CAA63322.1; !1PID:g1051142 GENETICS !$#map_position 12 min !$#genome prophage CLASSIFICATION #superfamily phage 82 hypothetical protein 45 SUMMARY #length 46 #molecular-weight 5493 #checksum 3787 SEQUENCE /// ENTRY S66579 #type complete TITLE hypothetical protein 33 - phage 82 ORGANISM #formal_name phage 82 DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 15-Oct-1999 ACCESSIONS S66579 REFERENCE S66579 !$#authors Mahdi, A.A.; Sharples, G.J.; Mandal, T.N.; Lloyd, R.G. !$#journal J. Mol. Biol. (1996) 257:561-573 !$#title Holliday junction resolvases encoded by homologous rusA !1genes in Escherichia coli K-12 and phage 82. !$#cross-references MUID:96196428; PMID:8648624 !$#accession S66579 !'##molecule_type DNA !'##residues 1-33 ##label MAH !'##cross-references EMBL:X92588; NID:g1051111; PIDN:CAA63326.1; !1PID:g1051112 CLASSIFICATION #superfamily phage 82 hypothetical protein 33 SUMMARY #length 33 #molecular-weight 3673 #checksum 1193 SEQUENCE /// ENTRY S66586 #type complete TITLE hypothetical protein 33 - Escherichia coli cryptic lambdoid prophage DLP12 ORGANISM #formal_name Escherichia coli DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 15-Oct-1999 ACCESSIONS S66586 REFERENCE S66579 !$#authors Mahdi, A.A.; Sharples, G.J.; Mandal, T.N.; Lloyd, R.G. !$#journal J. Mol. Biol. (1996) 257:561-573 !$#title Holliday junction resolvases encoded by homologous rusA !1genes in Escherichia coli K-12 and phage 82. !$#cross-references MUID:96196428; PMID:8648624 !$#accession S66586 !'##molecule_type DNA !'##residues 1-33 ##label MAH !'##cross-references EMBL:X92587; NID:g1051136; PIDN:CAA63317.1; !1PID:g1051137 GENETICS !$#map_position 12 min !$#genome prophage CLASSIFICATION #superfamily phage 82 hypothetical protein 33 SUMMARY #length 33 #molecular-weight 3644 #checksum 1210 SEQUENCE /// ENTRY RPBP16 #type complete TITLE repressor protein C - phage 16-3 ORGANISM #formal_name phage 16-3 #note host Rhizobium meliloti DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 23-Jul-1999 ACCESSIONS S01612 REFERENCE S01612 !$#authors Dallmann, G.; Papp, P.; Orosz, L. !$#journal Nature (1987) 330:398-401 !$#title Related repressor specificity of unrelated phages. !$#accession S01612 !'##molecule_type DNA !'##residues 1-197 ##label DAL !'##cross-references EMBL:X06420; NID:g15429; PIDN:CAA29729.1; !1PID:g15430 GENETICS !$#gene c CLASSIFICATION #superfamily phage 16-3 repressor protein C KEYWORDS DNA binding; repressor; transcription regulation SUMMARY #length 197 #molecular-weight 22242 #checksum 7692 SEQUENCE /// ENTRY ZEBP4L #type complete TITLE Ea47 protein - phage lambda ORGANISM #formal_name phage lambda DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS E43009; B43015; A04377 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession E43009 !'##molecule_type DNA !'##residues 1-410 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession B43015 !'##molecule_type DNA !'##residues 1-410 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96559.1; PID:g508992 GENETICS !$#gene Ea47 !$#map_position 49.31-46.78 CLASSIFICATION #superfamily phage lambda Ea47 protein SUMMARY #length 410 #molecular-weight 48096 #checksum 9012 SEQUENCE /// ENTRY ZEBP3L #type complete TITLE Ea31 protein - phage lambda ORGANISM #formal_name phage lambda DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS F43009; C43015; A04378 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession F43009 !'##molecule_type DNA !'##residues 1-296 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession C43015 !'##molecule_type DNA !'##residues 1-296 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96560.1; PID:g215131 GENETICS !$#gene Ea31 !$#map_position 52.37-50.54 CLASSIFICATION #superfamily phage lambda Ea31 protein SUMMARY #length 296 #molecular-weight 34583 #checksum 6023 SEQUENCE /// ENTRY ZEBP5L #type complete TITLE Ea59 protein - phage lambda ORGANISM #formal_name phage lambda DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS G43009; D43015; A04379 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession G43009 !'##molecule_type DNA !'##residues 1-525 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession D43015 !'##molecule_type DNA !'##residues 1-525 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96561.1; PID:g215132 GENETICS !$#gene Ea59 !$#map_position 55.61-52.37 CLASSIFICATION #superfamily phage lambda Ea59 protein SUMMARY #length 525 #molecular-weight 59484 #checksum 9577 SEQUENCE /// ENTRY ZEBP8L #type complete TITLE Ea8.5 protein - phage lambda ORGANISM #formal_name phage lambda DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS I43009; E43015; A04380 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession I43009 !'##molecule_type DNA !'##residues 1-93 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession E43015 !'##molecule_type DNA !'##residues 1-93 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96564.1; PID:g215135 GENETICS !$#gene Ea8.5 !$#map_position 61.14-60.57 CLASSIFICATION #superfamily phage lambda Ea8.5 protein SUMMARY #length 93 #molecular-weight 10750 #checksum 7373 SEQUENCE /// ENTRY ZEBP2L #type complete TITLE Ea22 protein - phage lambda ORGANISM #formal_name phage lambda DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS A43010; F43015; A04381 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession A43010 !'##molecule_type DNA !'##residues 1-182 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession F43015 !'##molecule_type DNA !'##residues 1-182 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96565.1; PID:g215136 GENETICS !$#gene Ea22 !$#map_position 62.67-61.54 !$#start_codon GTG CLASSIFICATION #superfamily phage lambda Ea22 protein SUMMARY #length 182 #molecular-weight 20968 #checksum 2726 SEQUENCE /// ENTRY QEBPL #type complete TITLE Ea10 protein - phage lambda ORGANISM #formal_name phage lambda DATE 02-Apr-1982 #sequence_revision 02-Apr-1982 #text_change 24-Sep-1999 ACCESSIONS B43010; G43015; F93737; A04382 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession B43010 !'##molecule_type DNA !'##residues 1-122 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession G43015 !'##molecule_type DNA !'##residues 1-122 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96574.1; PID:g215142 REFERENCE A93737 !$#authors Ineichen, K.; Shepherd, J.C.W.; Bickle, T.A. !$#journal Nucleic Acids Res. (1981) 9:4639-4653 !$#title The DNA sequence of the phage lambda genome between P-L and !1the gene bet. !$#cross-references MUID:82059489; PMID:6458018 !$#accession F93737 !'##molecule_type DNA !'##residues 1-122 ##label INE !'##cross-references GB:V00638; NID:g15060; PIDN:CAA23980.1; PID:g15063 COMMENT The Ea10 protein is believed to be involved in the !1production of the Tro phenotype. This phenotype is expressed !1when phages that possess a mutant cro gene and a !1thermolabile cI repressor gene are unable to propagate at !1restrictive temperatures. This inability is correlated with !1the shutoff of host macromolecular synthesis. GENETICS !$#gene Ea10; ssb !$#map_position 69.90-69.15 CLASSIFICATION #superfamily phage lambda Ea10 protein SUMMARY #length 122 #molecular-weight 13780 #checksum 2978 SEQUENCE /// ENTRY VDBPL #type complete TITLE kil protein - phage lambda ORGANISM #formal_name phage lambda DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS C43010; H43015; G93737; A04383 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession C43010 !'##molecule_type DNA !'##residues 1-89 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession H43015 !'##molecule_type DNA !'##residues 1-89 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104 REFERENCE A93737 !$#authors Ineichen, K.; Shepherd, J.C.W.; Bickle, T.A. !$#journal Nucleic Acids Res. (1981) 9:4639-4653 !$#title The DNA sequence of the phage lambda genome between P-L and !1the gene bet. !$#cross-references MUID:82059489; PMID:6458018 !$#accession G93737 !'##molecule_type DNA !'##residues 1-89 ##label INE !'##cross-references GB:V00638; NID:g15060; PIDN:CAA23979.1; PID:g15062 !'##note these authors have assigned the sequence shown to regulatory !1protein cIII. See the entry for the gam protein for their !1assignment of the kil protein COMMENT Residues 43-89 of the sequence shown correspond to the kil !1protein. COMMENT Gene kil kills the host upon prophage induction. GENETICS !$#gene kil !$#map_position 68.72-68.43 CLASSIFICATION #superfamily phage lambda kil protein SUMMARY #length 89 #molecular-weight 10066 #checksum 7908 SEQUENCE /// ENTRY VDBPHK #type complete TITLE kil protein - phage HK022 ORGANISM #formal_name phage HK022 #note host Escherichia coli DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 23-Jul-1999 ACCESSIONS S04989 REFERENCE S04989 !$#authors Oberto, J.; Weisberg, R.A.; Gottesman, M.E. !$#journal J. Mol. Biol. (1989) 207:675-693 !$#title Structure and function of the nun gene and the immunity !1region of the lambdoid phage HK022. !$#cross-references MUID:89342456; PMID:2760929 !$#accession S04989 !'##molecule_type DNA !'##residues 1-50 ##label OBE !'##cross-references GB:X16093; NID:g435309; PIDN:CAA34219.1; PID:g15763 GENETICS !$#gene kil CLASSIFICATION #superfamily phage lambda kil protein SUMMARY #length 50 #molecular-weight 5886 #checksum 7121 SEQUENCE /// ENTRY VDBP22 #type complete TITLE kil protein - phage P22 ORGANISM #formal_name phage P22 #note host Salmonella typhimurium DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 16-Jun-2000 ACCESSIONS S04248 REFERENCE S04245 !$#authors Semerjian, A.V.; Malloy, D.C.; Poteete, A.R. !$#journal J. Mol. Biol. (1989) 207:1-13 !$#title Genetic structure of the bacteriophage P22 P(L) operon. !$#cross-references MUID:89293845; PMID:2738922 !$#accession S04248 !'##molecule_type DNA !'##residues 1-62 ##label SEM !'##cross-references GB:X15637; NID:g15646; PIDN:CAA33654.1; !1PID:g4379359 GENETICS !$#gene kil CLASSIFICATION #superfamily phage P22 kil protein SUMMARY #length 62 #molecular-weight 6950 #checksum 4897 SEQUENCE /// ENTRY W2BP22 #type complete TITLE arf protein - phage P22 ORGANISM #formal_name phage P22 #note host Salmonella typhimurium DATE 31-Mar-1991 #sequence_revision 31-Mar-1991 #text_change 23-Jul-1999 ACCESSIONS S04249 REFERENCE S04245 !$#authors Semerjian, A.V.; Malloy, D.C.; Poteete, A.R. !$#journal J. Mol. Biol. (1989) 207:1-13 !$#title Genetic structure of the bacteriophage P22 P(L) operon. !$#cross-references MUID:89293845; PMID:2738922 !$#accession S04249 !'##molecule_type DNA !'##residues 1-47 ##label SEM !'##cross-references GB:X15637; NID:g15646; PIDN:CAA33652.1; PID:g15653 GENETICS !$#gene arf CLASSIFICATION #superfamily phage P22 arf protein SUMMARY #length 47 #molecular-weight 5517 #checksum 4804 SEQUENCE /// ENTRY IMBPBL #type complete TITLE rexB protein - phage lambda ORGANISM #formal_name phage lambda DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS D43010; I43015; A04384 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession D43010 !'##molecule_type DNA !'##residues 1-144 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession I43015 !'##molecule_type DNA !'##residues 1-144 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96579.1; PID:g215145 !'##note there are two possible initiation sites for gene rexB !1translation, the codons for 1-Met and 6-Met COMMENT The rex gene inhibits the growth of unrelated coliphages, !1including T4rII, T5lr, T1, and some mutants of T7, P22, !1phi-80, and lambda. It controls the activity of gene S and !1may inhibit the establishment of lysogeny by the repressor !1protein. GENETICS !$#gene rexB !$#map_position 74.76-73.87 CLASSIFICATION #superfamily phage lambda rexB protein SUMMARY #length 144 #molecular-weight 15967 #checksum 8555 SEQUENCE /// ENTRY IMBPAL #type complete TITLE rexA protein - phage lambda ORGANISM #formal_name phage lambda DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS E43010; A43016; A04385 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession E43010 !'##molecule_type DNA !'##residues 1-279 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession A43016 !'##molecule_type DNA !'##residues 1-279 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96580.1; PID:g215146 COMMENT The rex gene inhibits the growth of unrelated coliphages, !1including T4rII, T5lr, T1, and some mutants of T7, P22, !1phi-80, and lambda. It controls the activity of gene S and !1may inhibit the establishment of lysogeny by the repressor !1protein. GENETICS !$#gene rexA !$#map_position 76.52-74.80 CLASSIFICATION #superfamily phage lambda rexA protein SUMMARY #length 279 #molecular-weight 31255 #checksum 9390 SEQUENCE /// ENTRY ZRBPL #type complete TITLE ren protein - phage lambda ORGANISM #formal_name phage lambda DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS F43010; B43016; A04386 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession F43010 !'##molecule_type DNA !'##residues 1-96 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession B43016 !'##molecule_type DNA !'##residues 1-96 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96586.1; PID:g215152 GENETICS !$#gene ren !$#map_position 83.05-83.64 CLASSIFICATION #superfamily phage lambda ren protein SUMMARY #length 96 #molecular-weight 10611 #checksum 6749 SEQUENCE /// ENTRY QQBPGL #type complete TITLE git protein - phage lambda ORGANISM #formal_name phage lambda DATE 02-Apr-1982 #sequence_revision 02-Apr-1982 #text_change 17-Jul-1998 ACCESSIONS I43010; C43016; H93737; A04387 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession I43010 !'##molecule_type DNA !'##residues 1-183 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession C43016 !'##molecule_type DNA !'##residues 1-183 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104 REFERENCE A93737 !$#authors Ineichen, K.; Shepherd, J.C.W.; Bickle, T.A. !$#journal Nucleic Acids Res. (1981) 9:4639-4653 !$#title The DNA sequence of the phage lambda genome between P-L and !1the gene bet. !$#cross-references MUID:82059489; PMID:6458018 !$#accession H93737 !'##molecule_type DNA !'##residues 1-183 ##label INE !'##cross-references GB:V00638; NID:g15060 !'##note there is no known gene that maps in this region. As this region !1is not overlapped by any other genes and it contains a large !1open reading frame, the authors suggest that it represents a !1previously unidentified gene, which they named git; the !1propose that, in conjunction with the Ea10 protein, the git !1gene product is involved in production of the Tro phenotype !'##note this phenotype is expressed when phages that possess a mutant !1cro gene and a thermolabile cI repressor gene are unable to !1propagate at restrictive temperatures; this inability is !1correlated with the shutoff of host macromolecular synthesis !'##note the authors chose Met-5 as the initial residue because it is !1preceded by a Shine-Dalgarno sequence GENETICS !$#gene git !$#map_position 71.10-72.23 CLASSIFICATION #superfamily phage lambda git protein KEYWORDS transmembrane protein SUMMARY #length 183 #molecular-weight 21426 #checksum 89 SEQUENCE /// ENTRY ZBBPU2 #type complete TITLE gene B protein - phage Mu ORGANISM #formal_name phage Mu #note host Escherichia coli DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 23-Jul-1999 ACCESSIONS A04388 REFERENCE A04388 !$#authors Miller, J.L.; Anderson, S.K.; Fujita, D.J.; Chaconas, G.; !1Baldwin, D.L.; Harshey, R.M. !$#journal Nucleic Acids Res. (1984) 12:8627-8638 !$#title The nucleotide sequence of the B gene of bacteriophage mu. !$#cross-references MUID:85062837; PMID:6095204 !$#accession A04388 !'##molecule_type DNA !'##residues 1-312 ##label MIL !'##cross-references GB:X01149; GB:K03390; NID:g15447; PIDN:CAA25599.1; !1PID:g15448 COMMENT This protein is an essential gene product that is involved !1in bacteriophage integration and replication. CLASSIFICATION #superfamily phage Mu gene B protein KEYWORDS DNA binding; DNA replication FEATURE !$19-40 #region DNA binding #status predicted SUMMARY #length 312 #molecular-weight 35106 #checksum 9712 SEQUENCE /// ENTRY TQBPU #type complete TITLE transposase - phage Mu ORGANISM #formal_name phage Mu DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 23-Jul-1999 ACCESSIONS A24746; S09550; S06975; S57318 REFERENCE A24746 !$#authors Harshey, R.M.; Getzoff, E.D.; Baldwin, D.L.; Miller, J.L.; !1Chaconas, G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1985) 82:7676-7680 !$#title Primary structure of phage mu transposase: homology to mu !1repressor. !$#cross-references MUID:86067968; PMID:2999776 !$#accession A24746 !'##molecule_type DNA !'##residues 1-662 ##label HAR !'##cross-references GB:M11195 REFERENCE S57318 !$#authors Wu, Z.; Chaconas, G. !$#journal EMBO J. (1995) 14:3835-3843 !$#title A novel DNA binding and nuclease activity in domain III of !1Mu transposase: evidence for a catalytic region involved in !1donor cleavage. !$#cross-references MUID:95369255; PMID:7641701 !$#contents annotation REFERENCE S07291 !$#authors Priess, H.; Kamp, D.; Kahmann, R.; Braeuer, B.; Delius, H. !$#journal Mol. Gen. Genet. (1982) 186:315-321 !$#title Nucleotide sequence of the immunity region of bacteriophage !1Mu. !$#cross-references MUID:83012203; PMID:6214696 !$#accession S09550 !'##molecule_type DNA !'##residues 1-88 ##label PRI !'##cross-references EMBL:V01464; NID:g15807; PIDN:CAA24713.1; !1PID:g15810 GENETICS !$#gene A FUNCTION !$#description it is essential for integration, replication-transposition, !1and excision of Mu DNA CLASSIFICATION #superfamily phage Mu transposase KEYWORDS DNA binding; DNA replication SUMMARY #length 662 #molecular-weight 74888 #checksum 1944 SEQUENCE /// ENTRY ZCBPU2 #type complete TITLE gene C protein - phage Mu ORGANISM #formal_name phage Mu #note host Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 23-Jul-1999 ACCESSIONS A91549; A93629; A24379; A24399 REFERENCE A91549 !$#authors Heisig, P.; Kahmann, R. !$#journal Gene (1986) 43:59-67 !$#title The sequence and mom-transactivation function of the C gene !1of bacteriophage mu. !$#cross-references MUID:87005950; PMID:3019838 !$#accession A91549 !'##molecule_type DNA !'##residues 1-140 ##label HEI !'##cross-references GB:M13657; NID:g215520; PIDN:AAA32372.1; !1PID:g215521 REFERENCE A93629 !$#authors Margolin, W.; Howe, M.M. !$#journal Nucleic Acids Res. (1986) 14:4881-4897 !$#title Localization and DNA sequence analysis of the C gene of !1bacteriophage mu, the positive regulator of mu late !1transcription. !$#cross-references MUID:86259065; PMID:3014438 !$#accession A93629 !'##molecule_type DNA !'##residues 1-140 ##label MAR !'##cross-references GB:X03992; NID:g15811; PIDN:CAA27628.1; PID:g15812 COMMENT This protein may act as a positive regulator of the p-mom !1promoter and is required for transcription of the phage late !1genes. GENETICS !$#gene C CLASSIFICATION #superfamily phage Mu gene C protein KEYWORDS DNA binding; transcription regulation SUMMARY #length 140 #molecular-weight 16514 #checksum 1865 SEQUENCE /// ENTRY ZNBPMU #type complete TITLE gene N protein - phage Mu ORGANISM #formal_name phage Mu #note host Escherichia coli DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 23-Jul-1999 ACCESSIONS S01890; A27347 REFERENCE S01890 !$#authors Gloor, G.; Chaconas, G. !$#journal Nucleic Acids Res. (1988) 16:5211-5212 !$#title Sequence of bacteriophage Mu N and P genes. !$#cross-references MUID:88262526; PMID:2968539 !$#accession S01890 !'##molecule_type DNA !'##residues 1-491 ##label GLO !'##cross-references EMBL:X06796; NID:g15104; PIDN:CAA29955.1; !1PID:g15105 COMMENT This protein is bound to the ends of the Mu DNA. GENETICS !$#gene N CLASSIFICATION #superfamily phage Mu gene N protein KEYWORDS DNA binding SUMMARY #length 491 #molecular-weight 51575 #checksum 2852 SEQUENCE /// ENTRY ZPBPMU #type complete TITLE gene P protein - phage Mu ORGANISM #formal_name phage Mu #note host Escherichia coli DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 23-Jul-1999 ACCESSIONS S01891 REFERENCE S01890 !$#authors Gloor, G.; Chaconas, G. !$#journal Nucleic Acids Res. (1988) 16:5211-5212 !$#title Sequence of bacteriophage Mu N and P genes. !$#cross-references MUID:88262526; PMID:2968539 !$#accession S01891 !'##molecule_type DNA !'##residues 1-379 ##label GLO !'##cross-references EMBL:X06796; NID:g15104; PIDN:CAA29956.1; !1PID:g15106 COMMENT This protein is a component of the phage tail. GENETICS !$#gene P CLASSIFICATION #superfamily phage Mu gene P protein KEYWORDS DNA binding; tail protein SUMMARY #length 379 #molecular-weight 41785 #checksum 5214 SEQUENCE /// ENTRY ZQBPMU #type complete TITLE mom protein - phage Mu ORGANISM #formal_name phage Mu #note host Escherichia coli K12 DATE 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 23-Jul-1999 ACCESSIONS B21135 REFERENCE A21135 !$#authors Plasterk, R.H.A.; Vollering, M.; Brinkman, A.; van de Putte, !1P. !$#journal Cell (1984) 36:189-196 !$#title Analysis of the methylation-regulated Mu mom transcript. !$#cross-references MUID:84106815; PMID:6229339 !$#accession B21135 !'##molecule_type DNA !'##residues 1-241 ##label PLA !'##cross-references GB:V01463; NID:g15804; PIDN:CAA24710.1; PID:g15806 GENETICS !$#gene mom CLASSIFICATION #superfamily phage Mu gene mom protein SUMMARY #length 241 #molecular-weight 28277 #checksum 8096 SEQUENCE /// ENTRY QXBP1L #type complete TITLE hypothetical protein 401 - phage lambda ALTERNATE_NAMES orf-401; orf401 ORGANISM #formal_name phage lambda DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS G43010; D43016; A04389 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession G43010 !'##molecule_type DNA !'##residues 1-401 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession D43016 !'##molecule_type DNA !'##residues 1-401 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96555.1; PID:g215127 GENETICS !$#map_position 40.51-42.99 CLASSIFICATION #superfamily phage lambda hypothetical protein 401 SUMMARY #length 401 #molecular-weight 39883 #checksum 2402 SEQUENCE /// ENTRY QXBP4L #type complete TITLE hypothetical protein C-146 (nin region) - phage lambda ORGANISM #formal_name phage lambda DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 10-Sep-1999 ACCESSIONS H43010; E43016; A04390 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession H43010 !'##molecule_type DNA !'##residues 1-146 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession E43016 !'##molecule_type DNA !'##residues 1-146 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96587.1; PID:g215153 GENETICS !$#map_position 83.80-84.70 CLASSIFICATION #superfamily phage lambda hypothetical 16.6K protein (nin !1region) SUMMARY #length 146 #molecular-weight 16648 #checksum 2241 SEQUENCE /// ENTRY QXBP5L #type complete TITLE hypothetical nin region protein B-290 (nin region) - phage lambda ORGANISM #formal_name phage lambda DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 10-Sep-1999 ACCESSIONS A43011; F43016; A04391 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession A43011 !'##molecule_type DNA !'##residues 1-290 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession F43016 !'##molecule_type DNA !'##residues 1-290 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96588.1; PID:g215154 GENETICS !$#map_position 84.70-86.49 CLASSIFICATION #superfamily phage lambda hypothetical 33.6K protein (nin !1region) SUMMARY #length 290 #molecular-weight 33561 #checksum 8721 SEQUENCE /// ENTRY QXBP6L #type complete TITLE hypothetical protein A-57 (nin region) - phage lambda ORGANISM #formal_name phage lambda DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 10-Sep-1999 ACCESSIONS B43011; G43016; A04392 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession B43011 !'##molecule_type DNA !'##residues 1-57 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession G43016 !'##molecule_type DNA !'##residues 1-9,'C',11-57 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96589.1; PID:g215155 GENETICS !$#map_position 86.49-86.84 CLASSIFICATION #superfamily phage lambda hypothetical 7K protein (nin !1region) SUMMARY #length 57 #molecular-weight 6963 #checksum 8935 SEQUENCE /// ENTRY QXBP7L #type complete TITLE hypothetical protein C-60 (nin region) - phage lambda ORGANISM #formal_name phage lambda DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 10-Sep-1999 ACCESSIONS C43011; H43016; A04393 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession C43011 !'##molecule_type DNA !'##residues 1-60 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession H43016 !'##molecule_type DNA !'##residues 1-60 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96590.1; PID:g215156 GENETICS !$#map_position 86.78-87.15 !$#start_codon GTG CLASSIFICATION #superfamily phage lambda hypothetical 7.4K protein (nin !1region) SUMMARY #length 60 #molecular-weight 7415 #checksum 8948 SEQUENCE /// ENTRY QXBP8L #type complete TITLE hypothetical protein B-56 (nin region) - phage lambda ORGANISM #formal_name phage lambda DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 10-Sep-1999 ACCESSIONS D43011; I43016; A04394 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession D43011 !'##molecule_type DNA !'##residues 1-56 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession I43016 !'##molecule_type DNA !'##residues 1-56 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96591.1; PID:g215157 GENETICS !$#map_position 87.15-87.49 !$#start_codon GTG CLASSIFICATION #superfamily phage lambda hypothetical 6.4K protein (nin !1region) SUMMARY #length 56 #molecular-weight 6352 #checksum 7931 SEQUENCE /// ENTRY JN0728 #type complete TITLE hypothetical protein nin204 - Escherichia coli ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JN0728 REFERENCE JN0725 !$#authors Paton, A.W.; Paton, J.C.; Goldwater, P.N.; Heuzenroeder, !1M.W.; Manning, P.A. !$#journal Gene (1993) 129:87-92 !$#title Sequence of a variant Shiga-like toxin type-I operon of !1Escherichia coli O111:H-. !$#cross-references MUID:93328129; PMID:8335264 !$#accession JN0728 !'##molecule_type DNA !'##residues 1-193 ##label PAT !'##cross-references GB:L04539 !'##experimental_source serotype O111:H GENETICS !$#gene SLT-1 CLASSIFICATION #superfamily hypothetical protein nin204 SUMMARY #length 193 #molecular-weight 22616 #checksum 3355 SEQUENCE /// ENTRY QXBP9L #type complete TITLE hypothetical protein C-204 (nin region) - phage lambda ORGANISM #formal_name phage lambda DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS E43011; A43017; A04395 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession E43011 !'##molecule_type DNA !'##residues 1-204 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession A43017 !'##molecule_type DNA !'##residues 1-204 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96592.1; PID:g215158 GENETICS !$#map_position 87.48-88.74 CLASSIFICATION #superfamily hypothetical protein nin204 SUMMARY #length 204 #molecular-weight 24115 #checksum 6511 SEQUENCE /// ENTRY Q1BP0L #type complete TITLE hypothetical protein B-68 (nin region) - phage lambda ORGANISM #formal_name phage lambda DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 10-Sep-1999 ACCESSIONS F43011; B43017; A04396 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession F43011 !'##molecule_type DNA !'##residues 1-68 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession B43017 !'##molecule_type DNA !'##residues 1-68 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104 GENETICS !$#map_position 88.74-89.16 CLASSIFICATION #superfamily phage lambda hypothetical 7.9K protein (nin !1region) SUMMARY #length 68 #molecular-weight 7881 #checksum 2016 SEQUENCE /// ENTRY Q1BP2L #type complete TITLE hypothetical protein B-64 - phage lambda ORGANISM #formal_name phage lambda DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 10-Sep-1999 ACCESSIONS H43011; D43017; A04398 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession H43011 !'##molecule_type DNA !'##residues 1-64 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession D43017 !'##molecule_type DNA !'##residues 1-64 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96596.1; PID:g215162 GENETICS !$#map_position 92.00-92.39 CLASSIFICATION #superfamily phage lambda hypothetical 7.1K protein (nin !1region) SUMMARY #length 64 #molecular-weight 7083 #checksum 9670 SEQUENCE /// ENTRY QDBP4L #type complete TITLE hypothetical protein D-206 - phage lambda ORGANISM #formal_name phage lambda DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 10-Sep-1999 ACCESSIONS I43011; E43017; A04399 REFERENCE A94614 !$#authors Daniels, D. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession I43011 !'##molecule_type DNA !'##residues 1-206 ##label DAN REFERENCE A92891 !$#authors Sanger, F.; Coulson, A.R.; Hong, G.F.; Hill, D.F.; Petersen, !1G.B. !$#journal J. Mol. Biol. (1982) 162:729-773 !$#title Nucleotide sequence of bacteriophage lambda DNA. !$#cross-references MUID:83189071; PMID:6221115 !$#accession E43017 !'##molecule_type DNA !'##residues 1-206 ##label SAN !'##cross-references GB:J02459; GB:M17233; GB:M24325; GB:V00636; !1GB:X00906; NID:g215104; PIDN:AAA96556.1; PID:g508991 GENETICS !$#map_position 42.82-41.55 !$#start_codon GTG CLASSIFICATION #superfamily phage lambda hypothetical 20.2K protein SUMMARY #length 206 #molecular-weight 20215 #checksum 1070 SEQUENCE /// ENTRY WXBPT5 #type complete TITLE gene A2 protein - phage T5 ORGANISM #formal_name phage T5 #note host Escherichia coli DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 16-Feb-1997 ACCESSIONS JQ1034 REFERENCE JQ1034 !$#authors Snyder Jr., C.E. !$#journal Biochem. Biophys. Res. Commun. (1991) 177:1240-1246 !$#title Amino acid sequence of the bacteriophage T5 gene A2 protein. !$#cross-references MUID:91282771; PMID:2059212 !$#accession JQ1034 !'##molecule_type protein !'##residues 1-134 ##label SNY GENETICS !$#gene A2 CLASSIFICATION #superfamily phage T5 gene A2 protein KEYWORDS DNA binding SUMMARY #length 134 #molecular-weight 14200 #checksum 3352 SEQUENCE /// ENTRY WABPT5 #type complete TITLE gene D10 protein - phage T5 ORGANISM #formal_name phage T5 #note host Escherichia coli DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 23-Jul-1999 ACCESSIONS S01931 REFERENCE S01931 !$#authors Kaliman, A.V.; Kryukov, V.M.; Bayev, A.A. !$#journal Nucleic Acids Res. (1988) 16:10353-10354 !$#title The nucleotide sequence of the region of bacteriophage T5 !1early genes D10-D15. !$#cross-references MUID:89057468; PMID:3057441 !$#accession S01931 !'##status translation not shown !'##molecule_type DNA !'##residues 1-450 ##label KAL !'##cross-references EMBL:X12930; NID:g15407; PIDN:CAA31398.1; !1PID:g15409 GENETICS !$#gene D10 CLASSIFICATION #superfamily phage T5 gene D10 protein KEYWORDS DNA binding; early protein SUMMARY #length 450 #molecular-weight 50365 #checksum 5364 SEQUENCE /// ENTRY WBBPT5 #type complete TITLE gene D11 protein - phage T5 ORGANISM #formal_name phage T5 #note host Escherichia coli DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 27-Jan-1995 ACCESSIONS S10131 REFERENCE S01931 !$#authors Kaliman, A.V.; Kryukov, V.M.; Bayev, A.A. !$#journal Nucleic Acids Res. (1988) 16:10353-10354 !$#title The nucleotide sequence of the region of bacteriophage T5 !1early genes D10-D15. !$#cross-references MUID:89057468; PMID:3057441 !$#accession S10131 !'##status translation not shown !'##molecule_type DNA !'##residues 1-257 ##label KAL !'##cross-references EMBL:X12930 GENETICS !$#gene D11 CLASSIFICATION #superfamily phage T5 gene D11 protein KEYWORDS early protein SUMMARY #length 257 #molecular-weight 28909 #checksum 3598 SEQUENCE /// ENTRY WCBPT5 #type complete TITLE gene D12 protein - phage T5 ORGANISM #formal_name phage T5 #note host Escherichia coli DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 23-Jul-1999 ACCESSIONS S01932 REFERENCE S01931 !$#authors Kaliman, A.V.; Kryukov, V.M.; Bayev, A.A. !$#journal Nucleic Acids Res. (1988) 16:10353-10354 !$#title The nucleotide sequence of the region of bacteriophage T5 !1early genes D10-D15. !$#cross-references MUID:89057468; PMID:3057441 !$#accession S01932 !'##status translation not shown !'##molecule_type DNA !'##residues 1-297 ##label KAL !'##cross-references EMBL:X12930; NID:g15407; PIDN:CAA31399.1; !1PID:g15410 GENETICS !$#gene D12 CLASSIFICATION #superfamily phage T5 gene D12 protein KEYWORDS early protein SUMMARY #length 297 #molecular-weight 33850 #checksum 6939 SEQUENCE /// ENTRY WDBPT5 #type complete TITLE gene D13 protein - phage T5 ORGANISM #formal_name phage T5 #note host Escherichia coli DATE 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 23-Jul-1999 ACCESSIONS S01933 REFERENCE S01931 !$#authors Kaliman, A.V.; Kryukov, V.M.; Bayev, A.A. !$#journal Nucleic Acids Res. (1988) 16:10353-10354 !$#title The nucleotide sequence of the region of bacteriophage T5 !1early genes D10-D15. !$#cross-references MUID:89057468; PMID:3057441 !$#accession S01933 !'##status translation not shown !'##molecule_type DNA !'##residues 1-612 ##label KAL !'##cross-references EMBL:X12930; NID:g15407; PIDN:CAA31400.1; !1PID:g15411 GENETICS !$#gene D13 CLASSIFICATION #superfamily phage T5 gene D13 protein KEYWORDS early protein SUMMARY #length 612 #molecular-weight 68673 #checksum 546 SEQUENCE /// ENTRY W0BP37 #type complete TITLE gene 0.3 protein - phage T7 ORGANISM #formal_name phage T7 DATE 01-Sep-1981 #sequence_revision 01-Sep-1981 #text_change 23-Jul-1999 ACCESSIONS A43002; A43004; A90727; A90726; A92312; S42283; A04400 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession A43002 !'##molecule_type DNA !'##residues 1-117 ##label DUN REFERENCE A92866 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1981) 148:303-330 !$#title Nucleotide sequence from the genetic left end of !1bacteriophage T7 DNA to the beginning of gene 4. !$#cross-references MUID:82078034; PMID:7310871 !$#accession A43004 !'##molecule_type DNA !'##residues 1-117 ##label DU2 !'##cross-references GB:V01127; NID:g15498; PIDN:CAA24327.1; PID:g15499 REFERENCE A90727 !$#authors Korobko, V.G.; Chuvpilo, S.A.; Kolosov, M.N. !$#journal Bioorg. Khim. (1980) 6:1272-1274 !$#title Nucleotide sequence of gene 0.3 of bacteriophage T7. !$#accession A90727 !'##molecule_type DNA !'##residues 1-42,'S',44-117 ##label KOR !'##note the authors translated the codon CGT for residue 24 as Leu, ATC !1for residue 53 as His, and TTT for residue 54 as Leu REFERENCE A90726 !$#authors Korobko, V.G.; Chuvpilo, S.A.; Kolosov, M.N. !$#journal Bioorg. Khim. (1980) 6:1114-1116 !$#title Nucleotide sequence of gene 0.4 of bacteriophage T7. !$#accession A90726 !'##molecule_type DNA !'##residues 85-117 ##label KO2 REFERENCE A92312 !$#authors Dunn, J.J.; Elzinga, M.; Mark, K.K.; Studier, F.W. !$#journal J. Biol. Chem. (1981) 256:2579-2585 !$#title Amino acid sequence of the gene 0.3 protein of bacteriophage !1T7 and nucleotide sequence of its mRNA. !$#cross-references MUID:81117390; PMID:7007389 !$#accession A92312 !'##molecule_type mRNA !'##residues 1-117 ##label DU3 REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42283 !'##molecule_type DNA !'##residues 1-117 ##label DUW !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24384.1; !1PID:g15564 !'##note the authors did not translate the codon for residue 1 COMMENT This early gene protein is responsible for protecting the !1viral genome against degradation by the host restriction !1endonucleases. GENETICS !$#gene 0.3 !$#map_position 2.31-3.19 CLASSIFICATION #superfamily phage T7 gene 0.3 protein SUMMARY #length 117 #molecular-weight 13809 #checksum 7705 SEQUENCE /// ENTRY W0BP47 #type complete TITLE gene 0.4 protein - phage T7 ORGANISM #formal_name phage T7 DATE 01-Sep-1981 #sequence_revision 01-Sep-1981 #text_change 23-Jul-1999 ACCESSIONS B43002; B43004; B90726; B92312; S42284; A04401 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession B43002 !'##molecule_type DNA !'##residues 1-51 ##label DUN REFERENCE A92866 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1981) 148:303-330 !$#title Nucleotide sequence from the genetic left end of !1bacteriophage T7 DNA to the beginning of gene 4. !$#cross-references MUID:82078034; PMID:7310871 !$#accession B43004 !'##molecule_type DNA !'##residues 1-51 ##label DU2 !'##cross-references GB:V01127; NID:g15498; PIDN:CAA24328.1; PID:g15500 REFERENCE A90726 !$#authors Korobko, V.G.; Chuvpilo, S.A.; Kolosov, M.N. !$#journal Bioorg. Khim. (1980) 6:1114-1116 !$#title Nucleotide sequence of gene 0.4 of bacteriophage T7. !$#accession B90726 !'##molecule_type DNA !'##residues 1-51 ##label KOR REFERENCE A92312 !$#authors Dunn, J.J.; Elzinga, M.; Mark, K.K.; Studier, F.W. !$#journal J. Biol. Chem. (1981) 256:2579-2585 !$#title Amino acid sequence of the gene 0.3 protein of bacteriophage !1T7 and nucleotide sequence of its mRNA. !$#cross-references MUID:81117390; PMID:7007389 !$#accession B92312 !'##molecule_type mRNA !'##residues 1-51 ##label DU3 REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42284 !'##molecule_type DNA !'##residues 1-51 ##label DUW !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24385.1; !1PID:g15565 !'##note the authors did not translate the codon for residue 1 COMMENT The function of this early gene protein is unknown. GENETICS !$#gene 0.4 !$#map_position 3.20-3.58 CLASSIFICATION #superfamily phage T7 gene 0.4 protein SUMMARY #length 51 #molecular-weight 5752 #checksum 9374 SEQUENCE /// ENTRY W0BP57 #type complete TITLE gene 0.5 protein - phage T7 ORGANISM #formal_name phage T7 DATE 01-Sep-1981 #sequence_revision 01-Sep-1981 #text_change 23-Jul-1999 ACCESSIONS C43002; C43004; S42285; A04402 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession C43002 !'##molecule_type DNA !'##residues 1-47 ##label DUN REFERENCE A92866 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1981) 148:303-330 !$#title Nucleotide sequence from the genetic left end of !1bacteriophage T7 DNA to the beginning of gene 4. !$#cross-references MUID:82078034; PMID:7310871 !$#accession C43004 !'##molecule_type DNA !'##residues 1-47 ##label DU2 !'##cross-references GB:V01127; NID:g15498; PIDN:CAA24329.1; PID:g15501 REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42285 !'##molecule_type DNA !'##residues 1-47 ##label DUW !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24386.1; !1PID:g15566 COMMENT The function of this early gene protein is unknown. GENETICS !$#gene 0.5 !$#map_position 3.74-4.09 CLASSIFICATION #superfamily phage T7 gene 0.5 protein SUMMARY #length 47 #molecular-weight 4745 #checksum 3670 SEQUENCE /// ENTRY W0BP67 #type complete TITLE gene 0.6B protein - phage T7 ORGANISM #formal_name phage T7 DATE 01-Sep-1981 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS D43002; D43004; S42287; A04403 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession D43002 !'##molecule_type DNA !'##residues 1-111 ##label DUN !'##note it is assumed that gene 0.6 codes for two proteins; the first !1codes for a protein corresponding to residues 1-45 of the !1sequence shown, with an additional GSGYDRTH at the carboxyl !1end; the other is assumed to be produced by a +1 frameshift !1during translation, yielding the sequence shown !'##note this frameshift may occur anywhere within the region !1corresponding to residues 46-52 of the sequence shown; thus !1a portion of these residues may be replaced by a portion of !1the segment GSGYDRT in the actual protein REFERENCE A92866 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1981) 148:303-330 !$#title Nucleotide sequence from the genetic left end of !1bacteriophage T7 DNA to the beginning of gene 4. !$#cross-references MUID:82078034; PMID:7310871 !$#accession D43004 !'##molecule_type DNA !'##residues 1-111 ##label DU2 REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42287 !'##status translation not shown !'##molecule_type DNA !'##residues 1-45,'GSGYDRTH',54-111 ##label DUW !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24388.1; !1PID:g431188 !'##note biosynthesis of this protein probably involves a +1 frameshift !1between the codons 53 and 54; the exact position of the !1frameshift is unknown COMMENT The function of this early gene protein is unknown. GENETICS !$#gene 0.6B !$#map_position 4.09-4.92 CLASSIFICATION #superfamily phage T7 gene 0.6 protein SUMMARY #length 111 #molecular-weight 13247 #checksum 441 SEQUENCE /// ENTRY W1BP17 #type complete TITLE gene 1.1 protein - phage T7 ORGANISM #formal_name phage T7 DATE 28-Feb-1981 #sequence_revision 01-Sep-1981 #text_change 23-Jul-1999 ACCESSIONS E43002; E43004; A93851; S42290; A04404 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession E43002 !'##molecule_type DNA !'##residues 1-42 ##label DUN REFERENCE A92866 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1981) 148:303-330 !$#title Nucleotide sequence from the genetic left end of !1bacteriophage T7 DNA to the beginning of gene 4. !$#cross-references MUID:82078034; PMID:7310871 !$#accession E43004 !'##molecule_type DNA !'##residues 1-42 ##label DU2 !'##cross-references GB:V01127; NID:g15498; PIDN:CAA24334.1; PID:g15506 REFERENCE A93851 !$#authors Saito, H.; Tabor, S.; Tamanoi, F.; Richardson, C.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1980) 77:3917-3921 !$#title Nucleotide sequence of the primary origin of bacteriophage !1T7 DNA replication: relationship to adjacent genes and !1regulatory elements. !$#cross-references MUID:81054683; PMID:6254001 !$#accession A93851 !'##molecule_type DNA !'##residues 1-42 ##label SAI !'##cross-references GB:V01126; NID:g15495; PIDN:CAA24324.1; PID:g15496 REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42290 !'##molecule_type DNA !'##residues 1-42 ##label DUW !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24391.1; !1PID:g15570 COMMENT The function of this early gene protein is unknown. GENETICS !$#gene 1.1 !$#map_position 15.02-15.33 CLASSIFICATION #superfamily phage T7 gene 1.1 protein SUMMARY #length 42 #molecular-weight 5181 #checksum 9455 SEQUENCE /// ENTRY W1BP27 #type complete TITLE gene 1.2 protein - phage T7 ORGANISM #formal_name phage T7 DATE 28-Feb-1981 #sequence_revision 01-Sep-1981 #text_change 23-Jul-1999 ACCESSIONS F43002; F43004; B93851; S42291; A04405 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession F43002 !'##molecule_type DNA !'##residues 1-85 ##label DUN REFERENCE A92866 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1981) 148:303-330 !$#title Nucleotide sequence from the genetic left end of !1bacteriophage T7 DNA to the beginning of gene 4. !$#cross-references MUID:82078034; PMID:7310871 !$#accession F43004 !'##molecule_type DNA !'##residues 1-85 ##label DU2 !'##cross-references GB:V01127; NID:g15498; PIDN:CAA24335.1; PID:g15507 REFERENCE A93851 !$#authors Saito, H.; Tabor, S.; Tamanoi, F.; Richardson, C.C. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1980) 77:3917-3921 !$#title Nucleotide sequence of the primary origin of bacteriophage !1T7 DNA replication: relationship to adjacent genes and !1regulatory elements. !$#cross-references MUID:81054683; PMID:6254001 !$#accession B93851 !'##molecule_type DNA !'##residues 1-85 ##label SAI !'##cross-references GB:V01126; NID:g15495; PIDN:CAA24325.1; PID:g15497 REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42291 !'##molecule_type DNA !'##residues 1-85 ##label DUW !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24392.1; !1PID:g15571 !'##note the authors did not translate the codon for residue 1 COMMENT This early gene protein has been implicated in T7 DNA !1replication. GENETICS !$#gene 1.2 !$#map_position 15.34-15.98 CLASSIFICATION #superfamily phage T7 gene 1.2 protein SUMMARY #length 85 #molecular-weight 10190 #checksum 6988 SEQUENCE /// ENTRY W1BP77 #type complete TITLE gene 1.7 protein - phage T7 ORGANISM #formal_name phage T7 DATE 01-Sep-1981 #sequence_revision 01-Sep-1981 #text_change 23-Jul-1999 ACCESSIONS G43002; G43004; S42296; A04406 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession G43002 !'##molecule_type DNA !'##residues 1-196 ##label DUN REFERENCE A92866 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1981) 148:303-330 !$#title Nucleotide sequence from the genetic left end of !1bacteriophage T7 DNA to the beginning of gene 4. !$#cross-references MUID:82078034; PMID:7310871 !$#accession G43004 !'##molecule_type DNA !'##residues 1-196 ##label DU2 !'##cross-references GB:V01127; NID:g15498; PIDN:CAA24340.1; PID:g15512 REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42296 !'##molecule_type DNA !'##residues 1-196 ##label DUW !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24397.1; !1PID:g15576 !'##note the authors did not translate the codon for residue 1 COMMENT The function of this late gene protein is unknown. GENETICS !$#gene 1.7 !$#map_position 20.42-21.89 CLASSIFICATION #superfamily phage T7 gene 1.7 protein SUMMARY #length 196 #molecular-weight 22184 #checksum 6863 SEQUENCE /// ENTRY W4BP17 #type complete TITLE gene 4.1 protein - phage T7 ORGANISM #formal_name phage T7 DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS A04407; S42305 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession A04407 !'##molecule_type DNA !'##residues 1-40 ##label DUN REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42305 !'##molecule_type DNA !'##residues 1-40 ##label DUW !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24406.1; !1PID:g15585 !'##note the authors did not translate the codon for residue 1 GENETICS !$#gene 4.1 !$#map_position 29.13-29.43 CLASSIFICATION #superfamily phage T7 gene 4.1 protein SUMMARY #length 40 #molecular-weight 4397 #checksum 3955 SEQUENCE /// ENTRY W4BP27 #type complete TITLE gene 4.2 protein - phage T7 ORGANISM #formal_name phage T7 DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS A04408; S42307 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession A04408 !'##molecule_type DNA !'##residues 1-112 ##label DUN REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42307 !'##molecule_type DNA !'##residues 1-112 ##label DUW !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24408.1; !1PID:g15587 GENETICS !$#gene 4.2 !$#map_position 32.52-33.36 CLASSIFICATION #superfamily phage T7 gene 4.2 protein SUMMARY #length 112 #molecular-weight 12654 #checksum 6361 SEQUENCE /// ENTRY W4BP37 #type complete TITLE gene 4.3 protein - phage T7 ORGANISM #formal_name phage T7 DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS A04409; S42308 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession A04409 !'##molecule_type DNA !'##residues 1-70 ##label DUN REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42308 !'##molecule_type DNA !'##residues 1-70 ##label DUW !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24409.1; !1PID:g15588 GENETICS !$#gene 4.3 !$#map_position 33.43-33.96 CLASSIFICATION #superfamily phage T7 gene 4.3 protein SUMMARY #length 70 #molecular-weight 7927 #checksum 1286 SEQUENCE /// ENTRY W4BP57 #type complete TITLE gene 4.5 protein - phage T7 ORGANISM #formal_name phage T7 DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS A04410; S42309 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession A04410 !'##molecule_type DNA !'##residues 1-89 ##label DUN REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42309 !'##molecule_type DNA !'##residues 1-89 ##label DUW !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24410.1; !1PID:g15589 !'##note the authors did not translate the codon for residue 1 GENETICS !$#gene 4.5 !$#map_position 34.01-34.68 CLASSIFICATION #superfamily phage T7 gene 4.5 protein SUMMARY #length 89 #molecular-weight 10091 #checksum 7318 SEQUENCE /// ENTRY W4BP77 #type complete TITLE gene 4.7 protein - phage T7 ORGANISM #formal_name phage T7 DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS A04411; S42310 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession A04411 !'##molecule_type DNA !'##residues 1-135 ##label DUN REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42310 !'##molecule_type DNA !'##residues 1-135 ##label DUW !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24411.1; !1PID:g15590 GENETICS !$#gene 4.7 !$#map_position 34.87-35.88 CLASSIFICATION #superfamily phage T7 gene 4.7 protein SUMMARY #length 135 #molecular-weight 15209 #checksum 5554 SEQUENCE /// ENTRY W5BP57 #type complete TITLE gene 5.5 protein - phage T7 ORGANISM #formal_name phage T7 DATE 13-Jun-1983 #sequence_revision 31-Mar-1992 #text_change 16-Jun-2000 ACCESSIONS A04412; S42313 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession A04412 !'##molecule_type DNA !'##residues 1-99 ##label DUN REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42313 !'##molecule_type DNA !'##residues 1-99 ##label DUW !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24414.1; !1PID:g15593 !'##note the authors did not translate the codon for residue 1 GENETICS !$#gene 5.5 !$#map_position 42.20-43.46 CLASSIFICATION #superfamily phage T7 gene 5.5 protein SUMMARY #length 99 #molecular-weight 11206 #checksum 4190 SEQUENCE /// ENTRY W8BPG7 #type complete TITLE gene 18.7 protein - phage T7 ORGANISM #formal_name phage T7 DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS A04413; S42337 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession A04413 !'##molecule_type DNA !'##residues 1-83 ##label DUN REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42337 !'##molecule_type DNA !'##residues 1-83 ##label DUW !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24439.1; !1PID:g15615 !'##note the authors did not translate the codon for residue 1 GENETICS !$#gene 18.7 !$#map_position 92.73-93.35 CLASSIFICATION #superfamily phage T7 gene 18.7 protein SUMMARY #length 83 #molecular-weight 9326 #checksum 2479 SEQUENCE /// ENTRY W8BPT3 #type complete TITLE gene 18.7 protein - phage T3 ORGANISM #formal_name phage T3 #note host Escherichia coli DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 23-Jul-1999 ACCESSIONS E23476 REFERENCE A94339 !$#authors Yamada, M.; Fujisawa, H.; Kato, H.; Hamada, K.; Minagawa, T. !$#journal Virology (1986) 151:350-361 !$#title Cloning and sequencing of the genetic right end of !1bacteriophage T3 DNA. !$#cross-references MUID:86209997; PMID:3010556 !$#accession E23476 !'##molecule_type DNA !'##residues 1-83 ##label YAM !'##cross-references GB:M14784; NID:g215810; PIDN:AAA92527.1; !1PID:g1196765 REFERENCE A94344 !$#authors Yamada, M.; Fujisawa, H.; Kato, H.; Hamada, K.; Minagawa, T. !$#journal Virology (1986) 154:246 !$#contents annotation; erratum; corrections to coding regions GENETICS !$#gene 18.7 CLASSIFICATION #superfamily phage T7 gene 18.7 protein SUMMARY #length 83 #molecular-weight 9393 #checksum 4304 SEQUENCE /// ENTRY W9BPB7 #type complete TITLE gene 19.2 protein - phage T7 ORGANISM #formal_name phage T7 DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS S42339; A04414 REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42339 !'##status preliminary !'##molecule_type DNA !'##residues 1-85 ##label DU2 !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24441.1; !1PID:g579207 !'##note the authors did not translate the codon for residue 1 GENETICS !$#map_position 95.19-95.83 !$#start_codon GTG CLASSIFICATION #superfamily phage T7 gene 19.2 protein SUMMARY #length 85 #molecular-weight 9395 #checksum 365 SEQUENCE /// ENTRY W9BPT3 #type complete TITLE gene 19.2 protein - phage T3 ORGANISM #formal_name phage T3 #note host Escherichia coli DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 23-Jul-1999 ACCESSIONS G23476 REFERENCE A94339 !$#authors Yamada, M.; Fujisawa, H.; Kato, H.; Hamada, K.; Minagawa, T. !$#journal Virology (1986) 151:350-361 !$#title Cloning and sequencing of the genetic right end of !1bacteriophage T3 DNA. !$#cross-references MUID:86209997; PMID:3010556 !$#accession G23476 !'##molecule_type DNA !'##residues 1-146 ##label YAM !'##cross-references GB:M14784; NID:g215810; PIDN:AAA92529.1; !1PID:g1196766 REFERENCE A94344 !$#authors Yamada, M.; Fujisawa, H.; Kato, H.; Hamada, K.; Minagawa, T. !$#journal Virology (1986) 154:246 !$#contents annotation; erratum; corrections to coding regions GENETICS !$#gene 19.2 !$#start_codon GTG CLASSIFICATION #superfamily phage T7 gene 19.2 protein SUMMARY #length 146 #molecular-weight 15987 #checksum 1392 SEQUENCE /// ENTRY W9BPC7 #type complete TITLE gene 19.3 protein - phage T7 ORGANISM #formal_name phage T7 DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS A04415; S42340 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession A04415 !'##molecule_type DNA !'##residues 1-57 ##label DUN REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42340 !'##molecule_type DNA !'##residues 1-57 ##label DUW !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24442.1; !1PID:g15618 !'##note the authors did not translate the codon for residue 1 GENETICS !$#gene 19.3 !$#map_position 96.53-96.96 CLASSIFICATION #superfamily phage T7 gene 19.3 protein SUMMARY #length 57 #molecular-weight 6561 #checksum 4641 SEQUENCE /// ENTRY W9BPB3 #type complete TITLE gene 19.3 protein - phage T3 ORGANISM #formal_name phage T3 #note host Escherichia coli DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 23-Jul-1999 ACCESSIONS H23476 REFERENCE A94339 !$#authors Yamada, M.; Fujisawa, H.; Kato, H.; Hamada, K.; Minagawa, T. !$#journal Virology (1986) 151:350-361 !$#title Cloning and sequencing of the genetic right end of !1bacteriophage T3 DNA. !$#cross-references MUID:86209997; PMID:3010556 !$#accession H23476 !'##molecule_type DNA !'##residues 1-57 ##label YAM !'##cross-references GB:M14784; NID:g215810; PIDN:AAA92530.1; !1PID:g1196767 REFERENCE A94344 !$#authors Yamada, M.; Fujisawa, H.; Kato, H.; Hamada, K.; Minagawa, T. !$#journal Virology (1986) 154:246 !$#contents annotation; erratum; corrections to coding regions GENETICS !$#gene 19.3 CLASSIFICATION #superfamily phage T7 gene 19.3 protein SUMMARY #length 57 #molecular-weight 6641 #checksum 1720 SEQUENCE /// ENTRY Q1BP47 #type complete TITLE gene 1.4 protein - phage T7 ORGANISM #formal_name phage T7 DATE 01-Sep-1981 #sequence_revision 01-Sep-1981 #text_change 23-Jul-1999 ACCESSIONS H43002; H43004; S42293; A04416 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession H43002 !'##molecule_type DNA !'##residues 1-51 ##label DUN REFERENCE A92866 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1981) 148:303-330 !$#title Nucleotide sequence from the genetic left end of !1bacteriophage T7 DNA to the beginning of gene 4. !$#cross-references MUID:82078034; PMID:7310871 !$#accession H43004 !'##molecule_type DNA !'##residues 1-51 ##label DU2 !'##cross-references GB:V01127; NID:g15498; PIDN:CAA24337.1; PID:g15509 REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42293 !'##molecule_type DNA !'##residues 1-51 ##label DUW !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24394.1; !1PID:g15573 GENETICS !$#gene 1.4 !$#map_position 19.02-19.40 CLASSIFICATION #superfamily phage T7 gene 1.4 protein SUMMARY #length 51 #molecular-weight 5447 #checksum 1934 SEQUENCE /// ENTRY Q1BP57 #type complete TITLE gene 1.5 protein - phage T7 ORGANISM #formal_name phage T7 DATE 01-Sep-1981 #sequence_revision 01-Sep-1981 #text_change 23-Jul-1999 ACCESSIONS I43002; I43004; S42294; A04417 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession I43002 !'##molecule_type DNA !'##residues 1-29 ##label DUN REFERENCE A92866 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1981) 148:303-330 !$#title Nucleotide sequence from the genetic left end of !1bacteriophage T7 DNA to the beginning of gene 4. !$#cross-references MUID:82078034; PMID:7310871 !$#accession I43004 !'##molecule_type DNA !'##residues 1-29 ##label DU2 !'##cross-references GB:V01127; NID:g15498; PIDN:CAA24338.1; PID:g15510 REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42294 !'##molecule_type DNA !'##residues 1-29 ##label DUW !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24395.1; !1PID:g15574 GENETICS !$#gene 1.5 !$#map_position 19.48-19.69 CLASSIFICATION #superfamily phage T7 gene 1.5 protein SUMMARY #length 29 #molecular-weight 3175 #checksum 1643 SEQUENCE /// ENTRY Q1BP67 #type complete TITLE gene 1.6 protein - phage T7 ORGANISM #formal_name phage T7 DATE 01-Sep-1981 #sequence_revision 01-Sep-1981 #text_change 23-Jul-1999 ACCESSIONS A43003; A43005; S42295; A04418 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession A43003 !'##molecule_type DNA !'##residues 1-86 ##label DUN REFERENCE A92866 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1981) 148:303-330 !$#title Nucleotide sequence from the genetic left end of !1bacteriophage T7 DNA to the beginning of gene 4. !$#cross-references MUID:82078034; PMID:7310871 !$#accession A43005 !'##molecule_type DNA !'##residues 1-86 ##label DU2 !'##cross-references GB:V01127; NID:g15498; PIDN:CAA24339.1; PID:g15511 REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42295 !'##molecule_type DNA !'##residues 1-86 ##label DUW !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24396.1; !1PID:g15575 GENETICS !$#gene 1.6 !$#map_position 19.77-20.41 CLASSIFICATION #superfamily phage T7 gene 1.6 protein SUMMARY #length 86 #molecular-weight 9946 #checksum 8593 SEQUENCE /// ENTRY Q1BP87 #type complete TITLE gene 1.8 protein - phage T7 ORGANISM #formal_name phage T7 DATE 01-Sep-1981 #sequence_revision 01-Sep-1981 #text_change 23-Jul-1999 ACCESSIONS B43003; B43005; S42297; A04419 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession B43003 !'##molecule_type DNA !'##residues 1-48 ##label DUN REFERENCE A92866 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1981) 148:303-330 !$#title Nucleotide sequence from the genetic left end of !1bacteriophage T7 DNA to the beginning of gene 4. !$#cross-references MUID:82078034; PMID:7310871 !$#accession B43005 !'##molecule_type DNA !'##residues 1-48 ##label DU2 !'##cross-references GB:V01127; NID:g15498; PIDN:CAA24341.1; PID:g15513 REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42297 !'##molecule_type DNA !'##residues 1-48 ##label DUW !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24398.1; !1PID:g15577 GENETICS !$#gene 1.8 !$#map_position 21.87-22.23 CLASSIFICATION #superfamily phage T7 gene 1.8 protein SUMMARY #length 48 #molecular-weight 5781 #checksum 31 SEQUENCE /// ENTRY Q2BP87 #type complete TITLE gene 2.8 protein - phage T7 ORGANISM #formal_name phage T7 DATE 01-Sep-1981 #sequence_revision 19-Oct-1995 #text_change 23-Jul-1999 ACCESSIONS C43003; C43005; S42300; A04420 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession C43003 !'##molecule_type DNA !'##residues 1-139 ##label DUN REFERENCE A92866 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1981) 148:303-330 !$#title Nucleotide sequence from the genetic left end of !1bacteriophage T7 DNA to the beginning of gene 4. !$#cross-references MUID:82078034; PMID:7310871 !$#accession C43005 !'##molecule_type DNA !'##residues 1-139 ##label DU2 !'##cross-references GB:V01127; NID:g15498; PIDN:CAA24344.1; PID:g579181 REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42300 !'##molecule_type DNA !'##residues 1-139 ##label DUW !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24401.1; !1PID:g579202 GENETICS !$#gene 2.8 !$#map_position 24.64-25.69 !$#start_codon GTG CLASSIFICATION #superfamily phage T7 gene 2.8 protein SUMMARY #length 139 #molecular-weight 15618 #checksum 1959 SEQUENCE /// ENTRY Q7BP77 #type complete TITLE gene 7.7 protein - phage T7 ORGANISM #formal_name phage T7 DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS A04421; S42322 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession A04421 !'##molecule_type DNA !'##residues 1-130 ##label DUN1 REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42322 !'##molecule_type DNA !'##residues 1-130 ##label DUN2 !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24424.1; !1PID:g579204 GENETICS !$#gene 7.7 !$#map_position 49.70-50.67 !$#start_codon GTG CLASSIFICATION #superfamily phage T7 gene 2.8 protein SUMMARY #length 130 #molecular-weight 14737 #checksum 7231 SEQUENCE /// ENTRY Q3BP87 #type complete TITLE gene 3.8 protein - phage T7 ORGANISM #formal_name phage T7 DATE 01-Sep-1981 #sequence_revision 01-Sep-1981 #text_change 23-Jul-1999 ACCESSIONS D43003; D43005; S42303; A04422 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession D43003 !'##molecule_type DNA !'##residues 1-121 ##label DUN REFERENCE A92866 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1981) 148:303-330 !$#title Nucleotide sequence from the genetic left end of !1bacteriophage T7 DNA to the beginning of gene 4. !$#cross-references MUID:82078034; PMID:7310871 !$#accession D43005 !'##molecule_type DNA !'##residues 1-121 ##label DU2 !'##cross-references GB:V01127; NID:g15498; PIDN:CAA24347.1; PID:g15519 REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42303 !'##molecule_type DNA !'##residues 1-121 ##label DUW !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24404.1; !1PID:g15583 GENETICS !$#gene 3.8 !$#map_position 28.06-28.97 CLASSIFICATION #superfamily phage T7 gene 3.8 protein SUMMARY #length 121 #molecular-weight 14329 #checksum 5688 SEQUENCE /// ENTRY Q5BP37 #type complete TITLE gene 5.3 protein - phage T7 ORGANISM #formal_name phage T7 DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 16-Jun-2000 ACCESSIONS A04423; S42312 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession A04423 !'##molecule_type DNA !'##residues 1-118 ##label DUN REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42312 !'##molecule_type DNA !'##residues 1-118 ##label DUW !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24413.1; !1PID:g15592 GENETICS !$#gene 5.3 !$#map_position 41.27-42.16 CLASSIFICATION #superfamily phage T7 gene 5.3 protein SUMMARY #length 118 #molecular-weight 13067 #checksum 5789 SEQUENCE /// ENTRY Q6BP37 #type complete TITLE gene 6.3 protein - phage T7 ORGANISM #formal_name phage T7 DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS A04424; S42317 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession A04424 !'##molecule_type DNA !'##residues 1-37 ##label DUN REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42317 !'##molecule_type DNA !'##residues 1-37 ##label DUW !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24419.1; !1PID:g579203 GENETICS !$#gene 6.3 !$#map_position 46.06-46.33 !$#start_codon GTG CLASSIFICATION #superfamily phage T7 gene 6.3 protein SUMMARY #length 37 #molecular-weight 4089 #checksum 3335 SEQUENCE /// ENTRY Q6BP57 #type complete TITLE gene 6.5 protein - phage T7 ORGANISM #formal_name phage T7 DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS A04425; S42318 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession A04425 !'##molecule_type DNA !'##residues 1-84 ##label DUN REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42318 !'##molecule_type DNA !'##residues 1-84 ##label DUW !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24420.1; !1PID:g15597 GENETICS !$#gene 6.5 !$#map_position 46.58-47.21 CLASSIFICATION #superfamily phage T7 gene 6.5 protein SUMMARY #length 84 #molecular-weight 9475 #checksum 1151 SEQUENCE /// ENTRY Q6BP77 #type complete TITLE gene 6.7 protein - phage T7 ORGANISM #formal_name phage T7 DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS A04426; S42319 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession A04426 !'##molecule_type DNA !'##residues 1-88 ##label DUN REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42319 !'##molecule_type DNA !'##residues 1-88 ##label DUW !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24421.1; !1PID:g15598 !'##note the authors did not translate the codon for residue 1 GENETICS !$#gene 6.7 !$#map_position 47.23-47.89 CLASSIFICATION #superfamily phage T7 gene 6.7 protein SUMMARY #length 88 #molecular-weight 9338 #checksum 3829 SEQUENCE /// ENTRY Q7BPE7 #type complete TITLE gene 17.5 protein - phage T7 ORGANISM #formal_name phage T7 DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS A04427; S42334 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession A04427 !'##molecule_type DNA !'##residues 1-67 ##label DUN REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42334 !'##molecule_type DNA !'##residues 1-67 ##label DUW !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24436.1; !1PID:g579205 GENETICS !$#gene 17.5 !$#map_position 91.0-91.50 !$#start_codon GTG CLASSIFICATION #superfamily phage T3 lysis protein SUMMARY #length 67 #molecular-weight 7392 #checksum 265 SEQUENCE /// ENTRY Q7BPT3 #type complete TITLE lysis protein - phage T3 ORGANISM #formal_name phage T3 #note host Escherichia coli DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 31-Dec-1996 ACCESSIONS B23476 REFERENCE A94339 !$#authors Yamada, M.; Fujisawa, H.; Kato, H.; Hamada, K.; Minagawa, T. !$#journal Virology (1986) 151:350-361 !$#title Cloning and sequencing of the genetic right end of !1bacteriophage T3 DNA. !$#cross-references MUID:86209997; PMID:3010556 !$#accession B23476 !'##molecule_type DNA !'##residues 1-67 ##label YAM REFERENCE A94344 !$#authors Yamada, M.; Fujisawa, H.; Kato, H.; Hamada, K.; Minagawa, T. !$#journal Virology (1986) 154:246 !$#contents annotation; erratum; corrections to coding regions GENETICS !$#gene 17.5 CLASSIFICATION #superfamily phage T3 lysis protein KEYWORDS host cell lysis SUMMARY #length 67 #molecular-weight 7471 #checksum 1534 SEQUENCE /// ENTRY YVBPK3 #type complete TITLE lysis protein t - phage K3 ORGANISM #formal_name phage K3 #note host Escherichia coli DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 23-Jul-1999 ACCESSIONS A27083 REFERENCE A27083 !$#authors Riede, I. !$#journal J. Bacteriol. (1987) 169:2956-2961 !$#title Lysis gene t of T-even bacteriophages: evidence that !1colicins and bacteriophage genes have common ancestors. !$#cross-references MUID:87250254; PMID:3597316 !$#accession A27083 !'##molecule_type DNA !'##residues 1-218 ##label RIE !'##cross-references GB:M16812; NID:g215503; PIDN:AAA88415.1; !1PID:g215504 !'##note the author translated the codon CAA for residue 85 as Ile and !1CAG for residue 209 as Asn GENETICS !$#gene t CLASSIFICATION #superfamily phage T4 lysis protein t KEYWORDS host cell lysis SUMMARY #length 218 #molecular-weight 25222 #checksum 7363 SEQUENCE /// ENTRY YVBPT4 #type complete TITLE lysis protein t - phage T4 ORGANISM #formal_name phage T4 #note host Escherichia coli DATE 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 23-Jul-1999 ACCESSIONS JF0028; S07395 REFERENCE S07395 !$#authors Montag, D.; Degen, M.; Henning, U. !$#journal Nucleic Acids Res. (1987) 15:6736 !$#title Nucleotide sequence of gene t (lysis gene) of the E. coli !1phage T4. !$#cross-references MUID:87316934; PMID:3628006 !$#accession JF0028 !'##molecule_type DNA !'##residues 1-218 ##label MON !'##cross-references GB:Y00408; NID:g15368; PIDN:CAA68470.1; PID:g15369 !'##note the sequence is almost identical with that of the E.coli phage !1K3 COMMENT At the end of the growth cycle, phage T4 expresses two genes !1with lysis function, e and t. Gene e codes for a lysozyme !1whose structure and function are well characterized. Nothing !1is known about the gene product of t, although it has been !1suggested that it acts as a phospholipase. GENETICS !$#gene t !$#map_position 157.985-158.639 CLASSIFICATION #superfamily phage T4 lysis protein t KEYWORDS host cell lysis; transmembrane protein FEATURE !$35-49 #domain transmembrane #status predicted #label TMN SUMMARY #length 218 #molecular-weight 25175 #checksum 6633 SEQUENCE /// ENTRY Q8BPE7 #type complete TITLE gene 18.5 protein - phage T7 ORGANISM #formal_name phage T7 DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS A04428; S42336 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession A04428 !'##molecule_type DNA !'##residues 1-143 ##label DUN REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42336 !'##molecule_type DNA !'##residues 1-143 ##label DUW !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24438.1; !1PID:g15614 GENETICS !$#gene 18.5 !$#map_position 92.44-93.51 CLASSIFICATION #superfamily phage T7 gene 18.5 protein SUMMARY #length 143 #molecular-weight 16243 #checksum 2450 SEQUENCE /// ENTRY Q8BPT3 #type complete TITLE gene 18.5 protein - phage T3 ORGANISM #formal_name phage T3 #note host Escherichia coli DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 23-Jul-1999 ACCESSIONS D23476 REFERENCE A94339 !$#authors Yamada, M.; Fujisawa, H.; Kato, H.; Hamada, K.; Minagawa, T. !$#journal Virology (1986) 151:350-361 !$#title Cloning and sequencing of the genetic right end of !1bacteriophage T3 DNA. !$#cross-references MUID:86209997; PMID:3010556 !$#accession D23476 !'##molecule_type DNA !'##residues 1-147 ##label YAM !'##cross-references GB:M14784; NID:g215810; PIDN:AAA92526.1; !1PID:g1196764 REFERENCE A94344 !$#authors Yamada, M.; Fujisawa, H.; Kato, H.; Hamada, K.; Minagawa, T. !$#journal Virology (1986) 154:246 !$#contents annotation; erratum; corrections to coding regions GENETICS !$#gene 18.5 CLASSIFICATION #superfamily phage T7 gene 18.5 protein SUMMARY #length 147 #molecular-weight 16911 #checksum 2850 SEQUENCE /// ENTRY QQECFT #type complete TITLE yabC protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 01-Mar-2002 ACCESSIONS JH0092; S40593; B64730 REFERENCE JH0092 !$#authors Gomez, M.J.; Fluoret, B.; van Heijenoort, J.; Ayala, J.A. !$#journal Nucleic Acids Res. (1990) 18:2813 !$#title Nucleotide sequence of the regulatory region of the gene !1pbpB of Escherichia coli. !$#cross-references MUID:90251464; PMID:2187182 !$#accession JH0092 !'##molecule_type DNA !'##residues 1-346 ##label GOM !'##cross-references EMBL:X52063; NID:g42317; PIDN:CAA36283.1; !1PID:g42318 !'##experimental_source strain K-12, substrain W3110 REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40593 !'##molecule_type DNA !'##residues 1-346 ##label YUR !'##cross-references EMBL:D10483; NID:g216434; PIDN:BAA01348.1; !1PID:g216497 !'##experimental_source strain K-12 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64730 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 34-346 ##label BLAT !'##cross-references GB:AE000118; GB:U00096; NID:g1786262; !1PIDN:AAC73193.1; PID:g1786270; UWGP:b0082 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yabC !$#map_position 2 min CLASSIFICATION #superfamily Escherichia coli yabC protein SUMMARY #length 346 #molecular-weight 38794 #checksum 858 SEQUENCE /// ENTRY Q9BPE7 #type complete TITLE gene 19.5 protein - phage T7 ORGANISM #formal_name phage T7 DATE 13-Jun-1983 #sequence_revision 13-Jun-1983 #text_change 23-Jul-1999 ACCESSIONS A04429; S42341 REFERENCE A94615 !$#authors Dunn, J.J.; Thompson, K. !$#submission submitted to the Nucleic Acid Sequence Database, September !11982 !$#accession A04429 !'##molecule_type DNA !'##residues 1-49 ##label DUN REFERENCE S42283 !$#authors Dunn, J.J.; Studier, F.W. !$#journal J. Mol. Biol. (1983) 166:477-535 !$#title Complete nucleotide sequence of bacteriophage T7 DNA and the !1locations of T7 genetic elements. !$#cross-references MUID:83241725; PMID:6864790 !$#accession S42341 !'##molecule_type DNA !'##residues 1-49 ##label DUW !'##cross-references EMBL:V01146; NID:g431187; PIDN:CAA24443.1; !1PID:g15619 GENETICS !$#gene 19.5 !$#map_position 98.63-98.99 CLASSIFICATION #superfamily phage T7 gene 19.5 protein SUMMARY #length 49 #molecular-weight 5434 #checksum 4249 SEQUENCE /// ENTRY Q9BPT3 #type complete TITLE gene 19.5 protein - phage T3 ORGANISM #formal_name phage T3 #note host Escherichia coli DATE 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 23-Jul-1999 ACCESSIONS I23476 REFERENCE A94339 !$#authors Yamada, M.; Fujisawa, H.; Kato, H.; Hamada, K.; Minagawa, T. !$#journal Virology (1986) 151:350-361 !$#title Cloning and sequencing of the genetic right end of !1bacteriophage T3 DNA. !$#cross-references MUID:86209997; PMID:3010556 !$#accession I23476 !'##molecule_type DNA !'##residues 1-49 ##label YAM !'##cross-references GB:M14784; NID:g215810; PIDN:AAA92531.1; !1PID:g1196768 !'##note the authors translated the codon TGT for residue 47 as Val REFERENCE A94344 !$#authors Yamada, M.; Fujisawa, H.; Kato, H.; Hamada, K.; Minagawa, T. !$#journal Virology (1986) 154:246 !$#contents annotation; erratum; corrections to coding regions GENETICS !$#gene 19.5 CLASSIFICATION #superfamily phage T7 gene 19.5 protein SUMMARY #length 49 #molecular-weight 5484 #checksum 1771 SEQUENCE /// ENTRY Q9EC15 #type complete TITLE ribosome-binding factor rbfA - Escherichia coli (strain K-12) ALTERNATE_NAMES protein P15B ORGANISM #formal_name Escherichia coli DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 01-Mar-2002 ACCESSIONS S01915; A56159; C65107; A05050 REFERENCE S01915 !$#authors Sands, J.F.; Regnier, P.; Cummings, H.S.; Grunberg-Manago, !1M.; Hershey, J.W.B. !$#journal Nucleic Acids Res. (1988) 16:10803-10816 !$#title The existence of two genes between infB and rpsO in the !1Escherichia coli genome: DNA sequencing and S1 nuclease !1mapping. !$#cross-references MUID:89083498; PMID:2849753 !$#accession S01915 !'##molecule_type DNA !'##residues 1-133 ##label SAN !'##cross-references EMBL:X13270; NID:g42221; PIDN:CAA31634.1; !1PID:g42222 REFERENCE A56159 !$#authors Dammel, C.S.; Noller, H.F. !$#journal Genes Dev. (1995) 9:626-637 !$#title Suppression of a cold-sensitive mutation in 16S rRNA by !1overexpression of a novel ribosome-binding factor, RbfA. !$#cross-references MUID:95212911; PMID:7535280 !$#accession A56159 !'##status preliminary; nucleic acid sequence not shown; not compared !1with conceptual translation !'##molecule_type DNA !'##residues 1-133 ##label DAM REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65107 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-133 ##label BLAT !'##cross-references GB:AE000397; GB:U00096; NID:g2367199; !1PIDN:AAC76201.1; PID:g1789558; UWGP:b3167 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene rbfA !$#map_position 69 min CLASSIFICATION #superfamily Escherichia coli protein P15B SUMMARY #length 133 #molecular-weight 15154 #checksum 9498 SEQUENCE /// ENTRY Q9EC35 #type complete TITLE tRNA-pseudouridine synthase (EC 5.4.99.-) truB [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES p35 protein; tRNA pseudouridine-55 synthase ORGANISM #formal_name Escherichia coli DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 01-Mar-2002 ACCESSIONS S01916; B65107 REFERENCE S01915 !$#authors Sands, J.F.; Regnier, P.; Cummings, H.S.; Grunberg-Manago, !1M.; Hershey, J.W.B. !$#journal Nucleic Acids Res. (1988) 16:10803-10816 !$#title The existence of two genes between infB and rpsO in the !1Escherichia coli genome: DNA sequencing and S1 nuclease !1mapping. !$#cross-references MUID:89083498; PMID:2849753 !$#accession S01916 !'##molecule_type DNA !'##residues 1-314 ##label SAN !'##cross-references EMBL:X13270; NID:g42221; PIDN:CAA31635.1; !1PID:g42223 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65107 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-314 ##label BLAT !'##cross-references GB:AE000397; GB:U00096; NID:g2367199; !1PIDN:AAC76200.1; PID:g2367200; UWGP:b3166 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene truB !$#map_position 69 min FUNCTION !$#description EC 5.4.99.-; tRNA-pseudouridine synthase [validated, !1MUID:99459256]; catalyzes the isomerization of uridine to !1pseudouridine in RNA molecules CLASSIFICATION #superfamily Escherichia coli protein P35 KEYWORDS intramolecular transferase; isomerase; tRNA modification SUMMARY #length 314 #molecular-weight 35087 #checksum 3742 SEQUENCE /// ENTRY B64170 #type complete TITLE tRNA-pseudouridine synthase (EC 5.4.99.-) HI1289 - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES tRNA pseudouridine 55 synthase ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS B64170; T09418 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession B64170 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-312 ##label TIGR !'##cross-references GB:U32809; GB:L42023; NID:g3212217; !1PIDN:AAC22938.1; PID:g1574748; TIGR:HI1289 REFERENCE Z16667 !$#authors White, O.; Clayton, R.A.; Kerlavage, A.R.; Fleischmann, !1R.D.; Peterson, J.; Hickey, E.; Dodson, R.; Gwinn, M. !$#submission submitted to the EMBL Data Library, May 1998 !$#accession T09418 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-312 ##label WHI !'##cross-references EMBL:U32809; NID:g3212217; PID:g1574748 GENETICS !$#gene HI1289 CLASSIFICATION #superfamily Escherichia coli protein P35 KEYWORDS intramolecular transferase; isomerase; tRNA modification SUMMARY #length 312 #molecular-weight 35085 #checksum 5638 SEQUENCE /// ENTRY QQECX #type complete TITLE membrane protein ydaA - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 17-Dec-1982 #sequence_revision 13-Feb-1998 #text_change 01-Mar-2002 ACCESSIONS H64882; A04432 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64882 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-316 ##label BLAT !'##cross-references GB:AE000231; GB:U00096; NID:g1787588; !1PIDN:AAC74415.1; PID:g1787594; UWGP:b1333 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A93444 !$#authors Shaw, D.J.; Guest, J.R. !$#journal Nucleic Acids Res. (1982) 10:6119-6130 !$#title Nucleotide sequence of the fnr gene and primary structure of !1the Fnr protein of Escherichia coli. !$#cross-references MUID:83064543; PMID:6292868 !$#accession A04432 !'##molecule_type DNA !'##residues 1-54,'ERTYRYASGRHQPAYSLDP' ##label SHA !'##cross-references GB:J01608; NID:g146960; PIDN:AAA87982.1; !1PID:g146962 !'##experimental_source strain K-12 GENETICS !$#gene ydaA CLASSIFICATION #superfamily ydaA protein KEYWORDS transmembrane protein FEATURE !$265-281 #domain transmembrane #status predicted #label TM01 SUMMARY #length 316 #molecular-weight 35707 #checksum 4656 SEQUENCE /// ENTRY QQECIL #type complete TITLE probable regulator ribF [similarity] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS A64723; A22609; S40548 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64723 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-313 ##label BLAT !'##cross-references GB:AE000113; GB:U00096; NID:g2367095; !1PIDN:AAC73136.1; PID:g1786208; UWGP:b0025 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A22609 !$#authors Kamio, Y.; Lin, C.K.; Regue, M.; Wu, H.C. !$#journal J. Biol. Chem. (1985) 260:5616-5620 !$#title Characterization of the ileS-lsp operon in Escherichia coli. !1Identification of an open reading frame upstream of the ileS !1gene and potential promoter(s) for the ileS-lsp operon. !$#cross-references MUID:85182715; PMID:2985604 !$#accession A22609 !'##molecule_type DNA !'##residues 1-107,'V',109-127,'PLALVVKAISCYYR',142,'LAWNTASISPVRKL', !1157,'A',159,'VACA',165,'AARL',170-213,'P',215-313 ##label !1KAM !'##cross-references GB:D10483; GB:J01597; GB:J01683; GB:J01706; !1GB:K01298; GB:K01990; GB:M10420; GB:M10611; GB:M12544; !1GB:V00259; GB:X04711; GB:X54847; GB:X54945; GB:X55034; !1GB:X56742; NID:g216434; PIDN:BAA01303.1; PID:g216452 !'##note the authors translated the codon GGT for residue 31 as Glu REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40548 !'##status preliminary !'##molecule_type DNA !'##residues 1-107,'V',109-127,'PLALVVKAISCYYR',142,'LAWNTASISPVRKL', !1157,'A',159,'VACA',165,'AARL',170-213,'P',215-313 ##label !1YUR !'##cross-references EMBL:D10483; NID:g216434; PIDN:BAA01303.1; !1PID:g216452 GENETICS !$#gene yaaC !$#map_position 0.5 min CLASSIFICATION #superfamily conserved hypothetical protein HI0963 SUMMARY #length 313 #molecular-weight 34734 #checksum 2500 SEQUENCE /// ENTRY QQECRD #type complete TITLE glutathione-regulated potassium efflux system protein kefC [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 05-Apr-1983 #sequence_revision 01-Mar-1996 #text_change 01-Mar-2002 ACCESSIONS S40568; S15165; A04444; G64725 REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40568 !'##status preliminary !'##molecule_type DNA !'##residues 1-620 ##label YUR !'##cross-references EMBL:D10483; NID:g216434; PIDN:BAA01323.1; !1PID:g216472 REFERENCE S15165 !$#authors Munro, A.W.; Ritchie, G.Y.; Lamb, A.J.; Douglas, R.M.; !1Booth, I.R. !$#journal Mol. Microbiol. (1991) 5:607-616 !$#title The cloning and DNA sequence of the gene for the !1glutathione-regulated potassium-efflux system KefC of !1Escherichia coli. !$#cross-references MUID:91260444; PMID:2046548 !$#accession S15165 !'##molecule_type DNA !'##residues 1-620 ##label MUN !'##cross-references EMBL:X56742; NID:g41874; PIDN:CAA40066.1; !1PID:g41875 !'##experimental_source strain CS520 REFERENCE A93704 !$#authors Smith, D.R.; Calvo, J.M. !$#journal Nucleic Acids Res. (1980) 8:2255-2274 !$#title Nucleotide sequence of the Escherichia coli gene coding for !1dihydrofolate reductase. !$#cross-references MUID:81053692; PMID:6159575 !$#accession A04444 !'##molecule_type DNA !'##residues 500-620 ##label SMI !'##experimental_source strain K12 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64725 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-620 ##label BLAT !'##cross-references GB:AE000115; GB:U00096; NID:g1786230; !1PIDN:AAC73158.1; PID:g1786232; UWGP:b0047 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene kefC !$#map_position 1 min FUNCTION !$#description glutathione-gated potassium(+)-efflux system, which plays a !1role in the protection of cells from the toxic effects of !1electrophilic reagents, such as N-ethylmaleimide (NEM) !1[validated, MUID:94290548] CLASSIFICATION #superfamily glutathione-regulated potassium efflux system !1protein kefC KEYWORDS potassium transport; transmembrane protein FEATURE !$6-22 #domain transmembrane #status predicted #label TM1\ !$26-42 #domain transmembrane #status predicted #label TM2\ !$55-71 #domain transmembrane #status predicted #label TM3\ !$94-110 #domain transmembrane #status predicted #label TM4\ !$150-166 #domain transmembrane #status predicted #label TM5\ !$182-198 #domain transmembrane #status predicted #label TM6\ !$218-234 #domain transmembrane #status predicted #label TM7\ !$237-253 #domain transmembrane #status predicted #label TM8\ !$270-286 #domain transmembrane #status predicted #label TM9\ !$296-312 #domain transmembrane #status predicted #label TM10\ !$362-378 #domain transmembrane #status predicted #label TM11 SUMMARY #length 620 #molecular-weight 67795 #checksum 3086 SEQUENCE /// ENTRY QQEC49 #type complete TITLE yafA protein, 49K - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 04-Dec-1986 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS H64748; A04451 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64748 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-414 ##label BLAT !'##cross-references GB:AE000132; GB:U00096; NID:g2367098; !1PIDN:AAC73343.1; PID:g1786434; UWGP:b0239 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A91517 !$#authors Nuesch, J.; Schumperli, D. !$#journal Gene (1984) 32:243-249 !$#title Structural and functional organization of the gpt gene !1region of Escherichia coli. !$#cross-references MUID:85155481; PMID:6397401 !$#accession A04451 !'##molecule_type DNA !'##residues 1-241,'S',243-276,'TL',279-396,'KILTKVFRKSPTGS',411,'NA', !1414,'VKNLLNFANLVKQLHHNRR' ##label NUE !'##cross-references GB:M13422; NID:g146255; PIDN:AAA23929.1; !1PID:g146257 COMMENT The gene coding for this protein is located between the gpt !1and phoE genes. GENETICS !$#gene yafA !$#map_position 6 min CLASSIFICATION #superfamily yafA protein SUMMARY #length 414 #molecular-weight 47008 #checksum 3907 SEQUENCE /// ENTRY QQECLM #type complete TITLE yaiA protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 01-Mar-2002 ACCESSIONS B25197; E64767 REFERENCE A91812 !$#authors DeFeyter, R.C.; Davidson, B.E.; Pittard, J. !$#journal J. Bacteriol. (1986) 165:233-239 !$#title Nucleotide sequence of the transcription unit containing the !1aroL and aroM genes from Escherichia coli K-12. !$#cross-references MUID:86085676; PMID:3001025 !$#accession B25197 !'##molecule_type DNA !'##residues 1-63 ##label DEF !'##cross-references GB:M13045; NID:g145381; PIDN:AAA83834.1; !1PID:g1128942 !'##experimental_source strain K12 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64767 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-63 ##label BLAT !'##cross-references GB:AE000145; GB:U00096; NID:g1786580; !1PIDN:AAC73492.1; PID:g1786588; UWGP:b0389 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yaiA CLASSIFICATION #superfamily Escherichia coli yaiA protein SUMMARY #length 63 #molecular-weight 7281 #checksum 7562 SEQUENCE /// ENTRY Q3ECFS #type complete TITLE hypothetical 8K protein (fes 3' region) - Escherichia coli ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 26-Aug-1999 ACCESSIONS B31958; A38408 REFERENCE A31958 !$#authors Pettis, G.S.; Brickman, T.J.; McIntosh, M.A. !$#journal J. Biol. Chem. (1988) 263:18857-18863 !$#title Transcriptional mapping and nucleotide sequence of the !1Escherichia coli fepA-fes enterobactin region. !1Identification of a unique iron-regulated bidirectional !1promoter. !$#cross-references MUID:89066678; PMID:2974033 !$#accession B31958 !'##molecule_type DNA !'##residues 1-72 ##label PET !'##cross-references GB:J04216; NID:g145916; PIDN:AAA23758.1; !1PID:g145919 REFERENCE A38408 !$#authors Rusnak, F.; Sakaitani, M.; Drueckhammer, D.; Reichert, J.; !1Walsh, C.T. !$#journal Biochemistry (1991) 30:2916-2927 !$#title Biosynthesis of the Escherichia coli siderophore !1enterobactin: sequence of the entF gene, expression and !1purification of EntF, and analysis of covalent !1phosphopantetheine. !$#cross-references MUID:91175738; PMID:1826089 !$#accession A38408 !'##molecule_type DNA !'##residues 1-72 ##label RUS !'##cross-references GB:J05325 GENETICS !$#map_position 14 min CLASSIFICATION #superfamily Escherichia coli hypothetical 8K protein (fes !13' region) SUMMARY #length 72 #molecular-weight 8271 #checksum 6070 SEQUENCE /// ENTRY H70587 #type complete TITLE probable mbtH protein - Mycobacterium tuberculosis (strain H37RV) ALTERNATE_NAMES hypothetical protein Rv2377c ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS H70587 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession H70587 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-71 ##label COL !'##cross-references GB:Z95208; GB:AL123456; NID:g3261747; !1PIDN:CAB08480.1; PID:g3261748 !'##experimental_source strain H37Rv GENETICS !$#gene mbtH CLASSIFICATION #superfamily Escherichia coli hypothetical 8K protein (fes !13' region) SUMMARY #length 71 #molecular-weight 8082 #checksum 3385 SEQUENCE /// ENTRY QQECP7 #type complete TITLE ybeB protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 01-Mar-2002 ACCESSIONS A24995; C64798 REFERENCE A91176 !$#authors Asoh, S.; Matsuzawa, H.; Ishino, F.; Strominger, J.L.; !1Matsuhashi, M.; Ohta, T. !$#journal Eur. J. Biochem. (1986) 160:231-238 !$#title Nucleotide sequence of the pbpA gene and characteristics of !1the deduced amino acid sequence of penicillin-binding !1protein 2 of Escherichia coli K12. !$#cross-references MUID:87030266; PMID:3533535 !$#accession A24995 !'##molecule_type DNA !'##residues 1-69 ##label ASO !'##cross-references GB:X04516; GB:D00001; GB:N00001; NID:g42313; !1PIDN:CAA28199.1; PID:g42314 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64798 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-69 ##label BLAT !'##cross-references GB:AE000168; GB:U00096; NID:g1786849; !1PIDN:AAC73738.1; PID:g1786856; UWGP:b0637 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ybeB !$#map_position 15 min CLASSIFICATION #superfamily Escherichia coli ybeB protein SUMMARY #length 69 #molecular-weight 7678 #checksum 1801 SEQUENCE /// ENTRY Q3ECBA #type complete TITLE conserved hypothetical protein ybhB - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS E64813; B32025 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64813 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-158 ##label BLAT !'##cross-references GB:AE000180; GB:U00096; NID:g1786988; !1PIDN:AAC73860.1; PID:g1786990; UWGP:b0773 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A32025 !$#authors Otsuka, A.J.; Buoncristiani, M.R.; Howard, P.K.; Flamm, J.; !1Johnson, C.; Yamamoto, R.; Uchida, K.; Cook, C.; Ruppert, !1J.; Matsuzaki, J. !$#journal J. Biol. Chem. (1988) 263:19577-19585 !$#title The Escherichia coli biotin biosynthetic enzyme sequences !1predicted from the nucleotide sequence of the bio operon. !$#cross-references MUID:89066784; PMID:3058702 !$#accession B32025 !'##molecule_type DNA !'##residues 1-135,'A',137-158 ##label OTS !'##cross-references GB:J04423; NID:g145422; PIDN:AAA23513.1; !1PID:g455168 GENETICS !$#gene ybhB !$#map_position 17 min CLASSIFICATION #superfamily conserved hypothetical protein ybhB SUMMARY #length 158 #molecular-weight 17085 #checksum 5214 SEQUENCE /// ENTRY QQECP5 #type complete TITLE yceB protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Sep-1988 #sequence_revision 30-Sep-1988 #text_change 01-Mar-2002 ACCESSIONS B25008; D64849 REFERENCE A91177 !$#authors Backstrom, D.; Sjoberg, R.M.; Lundberg, L.G. !$#journal Eur. J. Biochem. (1986) 160:77-82 !$#title Nucleotide sequence of the structural gene for !1dihydroorotase of Escherichia coli K12. !$#cross-references MUID:87030260; PMID:2876892 !$#accession B25008 !'##molecule_type DNA !'##residues 1-186 ##label BAC !'##cross-references GB:X04469; GB:D00002; GB:N00002; NID:g42605; !1PIDN:CAA28156.1; PID:g42606 !'##experimental_source strain K-12 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64849 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-186 ##label BLAT !'##cross-references GB:AE000207; GB:U00096; NID:g1787293; !1PIDN:AAC74147.1; PID:g1787302; UWGP:b1063 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yceB !$#map_position 23 min CLASSIFICATION #superfamily Escherichia coli yceB protein SUMMARY #length 186 #molecular-weight 20500 #checksum 2401 SEQUENCE /// ENTRY S31245 #type complete TITLE translation initiation factor SUI1 [validated] - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein N0905; protein YNL244c ORGANISM #formal_name Saccharomyces cerevisiae DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 28-Jul-2000 ACCESSIONS S31245; S63212; S63216 REFERENCE S31245 !$#authors Yoon, H.; Donahue, T.F. !$#journal Mol. Cell. Biol. (1992) 12:248-260 !$#title The sui1 suppressor locus in Saccharomyces cerevisiae !1encodes a translation factor that functions during tRNA(Met) !1(i) recognition of the start codon. !$#cross-references MUID:92107175; PMID:1729602 !$#accession S31245 !'##molecule_type DNA !'##residues 1-108 ##label YOO !'##cross-references EMBL:M77514; NID:g172786; PID:g172787 !'##experimental_source strain TD28 REFERENCE S62997 !$#authors Poehlmann, R.; Philippsen, P. !$#submission submitted to the Protein Sequence Database, April 1996 !$#accession S63212 !'##molecule_type DNA !'##residues 1-108 ##label POE !'##cross-references EMBL:Z71520; NID:g1302281; PID:g1302282; !1GSPDB:GN00014; MIPS:YNL244c !'##experimental_source strain S288C REFERENCE S63216 !$#authors Sen-Gupta, M.; Hegemann, J.H. !$#submission submitted to the Protein Sequence Database, April 1996 !$#accession S63216 !'##molecule_type DNA !'##residues 1-108 ##label SEN !'##cross-references EMBL:Z71520; NID:g1302281; PID:g1302282; !1GSPDB:GN00014; MIPS:YNL244c !'##experimental_source strain S288C GENETICS !$#gene SGD:SUI1; RFR1; MIPS:YNL244c !'##cross-references SGD:S0005188; MIPS:YNL244c !$#map_position 14L FUNCTION !$#description involved in the translation initiation process [validated, !1MUID:92107175]; probably required in addition to elongation !1facter eIF-2 to establish ribosomal recognition of an ATG !1initiation codon CLASSIFICATION #superfamily translation initiation factor SUI SUMMARY #length 108 #molecular-weight 12312 #checksum 7002 SEQUENCE /// ENTRY Q3ECPF #type complete TITLE translation initiation factor SUI [similarity] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1988 #sequence_revision 14-Nov-1997 #text_change 01-Mar-2002 ACCESSIONS E64876; B28440 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64876 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-109 ##label BLAT !'##cross-references GB:AE000226; GB:U00096; NID:g2367115; !1PIDN:AAC74364.1; PID:g1787538; UWGP:b1282 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A92598 !$#authors Turnbough Jr., C.L.; Kerr, K.H.; Funderburg, W.R.; Donahue, !1J.P.; Powell, F.E. !$#journal J. Biol. Chem. (1987) 262:10239-10245 !$#title Nucleotide sequence and characterization of the pyrF operon !1of Escherichia coli K12. !$#cross-references MUID:87280048; PMID:2956254 !$#accession B28440 !'##molecule_type DNA !'##residues 2-109 ##label TUR !'##cross-references GB:J02768; NID:g147474; PIDN:AAA24484.1; !1PID:g147476 GENETICS !$#gene yciH !$#map_position 28 min CLASSIFICATION #superfamily translation initiation factor SUI KEYWORDS translation regulation SUMMARY #length 109 #molecular-weight 11527 #checksum 8290 SEQUENCE /// ENTRY Q3ECEA #type complete TITLE ybdB protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 01-Mar-2002 ACCESSIONS B91904; C91903; C64793; C32046; D32047 REFERENCE A91904 !$#authors Liu, J.; Duncan, K.; Walsh, C.T. !$#journal J. Bacteriol. (1989) 171:791-798 !$#title Nucleotide sequence of a cluster of Escherichia coli !1enterobactin biosynthesis genes: identification of entA and !1purification of its product 2,3-dihydro-2, !13-dihydroxybenzoate dehydrogenase. !$#cross-references MUID:89123155; PMID:2521622 !$#accession B91904 !'##molecule_type DNA !'##residues 1-137 ##label LIU !'##cross-references GB:M24148; NID:g304949; PIDN:AAA16104.1; !1PID:g450383 REFERENCE A91903 !$#authors Nahlik, M.S.; Brickman, T.J.; Ozenberger, B.A.; McIntosh, !1M.A. !$#journal J. Bacteriol. (1989) 171:784-790 !$#title Nucleotide sequence and transcriptional organization of the !1Escherichia coli enterobactin biosynthesis cistrons entB and !1entA. !$#cross-references MUID:89123154; PMID:2521621 !$#accession C91903 !'##molecule_type DNA !'##residues 1-137 ##label NAH !'##cross-references GB:M24143; NID:g341118; PIDN:AAA76837.1; !1PID:g522184 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64793 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-137 ##label BLAT !'##cross-references GB:AE000165; GB:U00096; NID:g1786808; !1PIDN:AAC73698.1; PID:g1786813; UWGP:b0597 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ybdB !$#map_position 13 min CLASSIFICATION #superfamily Escherichia coli ybdB protein SUMMARY #length 137 #molecular-weight 14970 #checksum 3735 SEQUENCE /// ENTRY Q0ECNA #type complete TITLE carbon starvation protein A - Escherichia coli (strain K-12) ALTERNATE_NAMES protein b0598 ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 07-Nov-1997 #text_change 01-Mar-2002 ACCESSIONS D64793; S14411; S14412; E32047 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64793 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-701 ##label BLAT !'##cross-references GB:AE000165; GB:U00096; NID:g1786808; !1PIDN:AAC73699.1; PID:g1786814; UWGP:b0598 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S14411 !$#authors Schultz, J.E.; Matin, A. !$#journal J. Mol. Biol. (1991) 218:129-140 !$#title Molecular and functional characterization of a carbon !1starvation gene of Escherichia coli. !$#cross-references MUID:91162636; PMID:1848300 !$#accession S14411 !'##molecule_type DNA !'##residues 1-128,'G',130-542,'ALTLCGRCLVLPTRCWQGWR' ##label SCH !'##cross-references EMBL:X52904; NID:g41080; PIDN:CAA37086.1; !1PID:g41081 !$#accession S14412 !'##molecule_type DNA !'##residues 564-701 ##label SC2 !'##cross-references EMBL:X52904; NID:g41080; PIDN:CAA37087.1; !1PID:g41082 REFERENCE A91904 !$#authors Liu, J.; Duncan, K.; Walsh, C.T. !$#journal J. Bacteriol. (1989) 171:791-798 !$#title Nucleotide sequence of a cluster of Escherichia coli !1enterobactin biosynthesis genes: identification of entA and !1purification of its product 2,3-dihydro-2, !13-dihydroxybenzoate dehydrogenase. !$#cross-references MUID:89123155; PMID:2521622 !$#accession E32047 !'##molecule_type DNA !'##residues 1-200 ##label LIU GENETICS !$#gene cstA !$#map_position 13 min CLASSIFICATION #superfamily carbon starvation protein KEYWORDS transmembrane protein FEATURE !$8-24 #domain transmembrane #status predicted #label TM1\ !$32-48 #domain transmembrane #status predicted #label TM2\ !$93-109 #domain transmembrane #status predicted #label TM3\ !$114-130 #domain transmembrane #status predicted #label TM4\ !$167-183 #domain transmembrane #status predicted #label TM5\ !$194-210 #domain transmembrane #status predicted #label TM6\ !$218-234 #domain transmembrane #status predicted #label TM7\ !$260-276 #domain transmembrane #status predicted #label TM8\ !$285-301 #domain transmembrane #status predicted #label TM9\ !$325-341 #domain transmembrane #status predicted #label TM10\ !$369-385 #domain transmembrane #status predicted #label TM11\ !$468-484 #domain transmembrane #status predicted #label TM12\ !$517-533 #domain transmembrane #status predicted #label TM13\ !$557-573 #domain transmembrane #status predicted #label TM14\ !$581-597 #domain transmembrane #status predicted #label TM15\ !$648-664 #domain transmembrane #status predicted #label TM16 SUMMARY #length 701 #molecular-weight 75105 #checksum 6365 SEQUENCE /// ENTRY QQECHE #type complete TITLE hydrogenase 1 formation factor hyaE - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 01-Mar-2002 ACCESSIONS JV0076; F64838 REFERENCE JV0072 !$#authors Menon, N.K.; Robbins, J.; Peck Jr., H.D.; Chatelus, C.Y.; !1Choi, E.S.; Przybyla, A.E. !$#journal J. Bacteriol. (1990) 172:1969-1977 !$#title Cloning and sequencing of a putative Escherichia coli [NiFe] !1hydrogenase-1 operon containing six open reading frames. !$#cross-references MUID:90202716; PMID:2180913 !$#accession JV0076 !'##molecule_type DNA !'##residues 1-132 ##label MEN !'##cross-references GB:M34825; NID:g146419; PIDN:AAA24001.1; !1PID:g146424 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64838 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-132 ##label BLAT !'##cross-references GB:AE000199; GB:U00096; NID:g1787202; !1PIDN:AAC74061.1; PID:g1787210; UWGP:b0976 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene hyaE !$#map_position 21 min CLASSIFICATION #superfamily hydrogenase-1 operon protein hyaE SUMMARY #length 132 #molecular-weight 14890 #checksum 8061 SEQUENCE /// ENTRY QQECHF #type complete TITLE hydrogenase-1 cofactor biosynthesis protein hyaF - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 01-Mar-2002 ACCESSIONS JV0077; G64838 REFERENCE JV0072 !$#authors Menon, N.K.; Robbins, J.; Peck Jr., H.D.; Chatelus, C.Y.; !1Choi, E.S.; Przybyla, A.E. !$#journal J. Bacteriol. (1990) 172:1969-1977 !$#title Cloning and sequencing of a putative Escherichia coli [NiFe] !1hydrogenase-1 operon containing six open reading frames. !$#cross-references MUID:90202716; PMID:2180913 !$#accession JV0077 !'##molecule_type DNA !'##residues 1-285 ##label MEN !'##cross-references GB:M34825; NID:g146419; PIDN:AAA24002.1; !1PID:g146425 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64838 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-285 ##label BLAT !'##cross-references GB:AE000199; GB:U00096; NID:g1787202; !1PIDN:AAC74062.1; PID:g1787211; UWGP:b0977 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene hyaF !$#map_position 21 min CLASSIFICATION #superfamily hydrogenase-1 operon protein hyaF SUMMARY #length 285 #molecular-weight 31430 #checksum 3262 SEQUENCE /// ENTRY H43255 #type complete TITLE hydrogenase-1 cofactor biosynthesis protein hoxQ - Alcaligenes eutrophus ORGANISM #formal_name Alcaligenes eutrophus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-May-2000 ACCESSIONS H43255 REFERENCE A43255 !$#authors Kortluke, C.; Horstmann, K.; Schwartz, E.; Rohde, M.; !1Binsack, R.; Friedrich, B. !$#journal J. Bacteriol. (1992) 174:6277-6289 !$#title A gene complex coding for the membrane-bound hydrogenase of !1Alcaligenes eutrophus H16. !$#cross-references MUID:93015670; PMID:1383192 !$#contents H16, megaplasmid pHG1 !$#accession H43255 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-282 ##label KOR !'##cross-references GB:M96433; NID:g141932; PID:g141940 !'##note sequence extracted from NCBI backbone (NCBIP:115463) CLASSIFICATION #superfamily hydrogenase-1 operon protein hyaF SUMMARY #length 282 #molecular-weight 30994 #checksum 9049 SEQUENCE /// ENTRY S53660 #type complete TITLE hydrogenase-1 cofactor biosynthesis protein hoxQ - Azotobacter chroococcum ORGANISM #formal_name Azotobacter chroococcum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S53660 REFERENCE S53655 !$#authors Du, L.; Tibelius, K.H.; Souza, E.M.; Garg, R.P.; Yates, M.G. !$#journal J. Mol. Biol. (1994) 243:549-557 !$#title Sequences, organization and analysis of the hupZMNOQRTV !1genes from the Azotobacter chroococcum hydrogenase gene !1cluster. !$#cross-references MUID:95055698; PMID:7966281 !$#accession S53660 !'##status preliminary !'##molecule_type DNA !'##residues 1-284 ##label DUL !'##cross-references EMBL:L25315; NID:g408900; PIDN:AAA64451.1; !1PID:g408906 CLASSIFICATION #superfamily hydrogenase-1 operon protein hyaF SUMMARY #length 284 #molecular-weight 31298 #checksum 9516 SEQUENCE /// ENTRY S25689 #type complete TITLE hydrogenase-1 cofactor biosynthesis protein hupH [similarity] - Rhodobacter capsulatus ORGANISM #formal_name Rhodobacter capsulatus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-May-2000 ACCESSIONS S25689 REFERENCE S25686 !$#authors Toussaint, B. !$#submission submitted to the EMBL Data Library, September 1992 !$#accession S25689 !'##molecule_type DNA !'##residues 1-182 ##label TOU !'##cross-references EMBL:Z15089 GENETICS !$#gene hupH CLASSIFICATION #superfamily hydrogenase-1 operon protein hyaF SUMMARY #length 182 #molecular-weight 18976 #checksum 7107 SEQUENCE /// ENTRY D44915 #type complete TITLE hydrogenase-1 cofactor biosynthesis protein hoxQ - Azotobacter vinelandii ORGANISM #formal_name Azotobacter vinelandii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D44915 REFERENCE A44915 !$#authors Menon, A.L.; Mortenson, L.E.; Robson, R.L. !$#journal J. Bacteriol. (1992) 174:4549-4557 !$#title Nucleotide sequences and genetic analysis of hydrogen !1oxidation (hox) genes in Azotobacter vinelandii. !$#cross-references MUID:92325046; PMID:1624446 !$#accession D44915 !'##status preliminary !'##molecule_type DNA !'##residues 1-283 ##label MEN !'##cross-references GB:M80522; NID:g142313; PIDN:AAA22129.1; !1PID:g142317 !'##note sequence extracted from NCBI backbone (NCBIN:108128, !1NCBIP:108132) CLASSIFICATION #superfamily hydrogenase-1 operon protein hyaF SUMMARY #length 283 #molecular-weight 31015 #checksum 5173 SEQUENCE /// ENTRY S27342 #type complete TITLE hydrogenase-1 cofactor biosynthesis protein hupH - Rhizobium leguminosarum ORGANISM #formal_name Rhizobium leguminosarum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S27342 REFERENCE S27340 !$#authors Rey, L.; Hidalgo, E.; Palacios, J.; Ruiz-Argueeso, T. !$#journal J. Mol. Biol. (1992) 228:998-1002 !$#title Nucleotide sequence and organization of an H(2)-uptake gene !1cluster from Rhizobium leguminosarum bv. viciae containing a !1rubredoxin-like gene and four additional open reading !1frames. !$#cross-references MUID:93108466; PMID:1469733 !$#accession S27342 !'##status preliminary !'##molecule_type DNA !'##residues 1-282 ##label REY !'##cross-references EMBL:X52974; NID:g1167855; PIDN:CAA37155.1; !1PID:g48728 CLASSIFICATION #superfamily hydrogenase-1 operon protein hyaF SUMMARY #length 282 #molecular-weight 30507 #checksum 783 SEQUENCE /// ENTRY QQECP1 #type complete TITLE ybeA protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 01-Mar-2002 ACCESSIONS B24995; B64798 REFERENCE A91176 !$#authors Asoh, S.; Matsuzawa, H.; Ishino, F.; Strominger, J.L.; !1Matsuhashi, M.; Ohta, T. !$#journal Eur. J. Biochem. (1986) 160:231-238 !$#title Nucleotide sequence of the pbpA gene and characteristics of !1the deduced amino acid sequence of penicillin-binding !1protein 2 of Escherichia coli K12. !$#cross-references MUID:87030266; PMID:3533535 !$#accession B24995 !'##molecule_type DNA !'##residues 1-155 ##label ASO !'##cross-references GB:X04516; GB:D00001; GB:N00001; NID:g42313; !1PIDN:CAA28200.1; PID:g581174 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64798 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-155 ##label BLAT !'##cross-references GB:AE000168; GB:U00096; NID:g1786849; !1PIDN:AAC73737.1; PID:g1786855; UWGP:b0636 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ybeA !$#map_position 15 min !$#start_codon GTG CLASSIFICATION #superfamily conserved hypothetical protein HI0033 SUMMARY #length 155 #molecular-weight 17341 #checksum 4122 SEQUENCE /// ENTRY QQECA5 #type complete TITLE hypothetical 23.4K protein (ansA 3' region) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS H64936; JU0048 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64936 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-219 ##label BLAT !'##cross-references GB:AE000271; GB:U00096; NID:g1788058; !1PIDN:AAC74838.1; PID:g1788066; UWGP:b1768 !'##experimental_source strain K-12, substrain MG1655 REFERENCE JU0047 !$#authors Jerlstroem, P.G.; Bezjak, D.A.; Jennings, M.P.; Beacham, !1I.R. !$#journal Gene (1989) 78:37-46 !$#title Structure and expression in Escherichia coli K-12 of the !1L-asparaginase I-encoding ansA gene and its flanking !1regions. !$#cross-references MUID:89357501; PMID:2670682 !$#accession JU0048 !'##molecule_type DNA !'##residues 7-219 ##label JER !'##cross-references GB:M26934; NID:g145278; PIDN:AAA23447.1; !1PID:g145280 GENETICS !$#gene ydjB !$#map_position 39 min CLASSIFICATION #superfamily Escherichia coli hypothetical 23.4K protein !1(ansA 3' region) SUMMARY #length 219 #molecular-weight 24064 #checksum 2172 SEQUENCE /// ENTRY QQEC32 #type complete TITLE hypothetical protein D-143 - Escherichia coli ORGANISM #formal_name Escherichia coli DATE 05-Apr-1983 #sequence_revision 05-Apr-1983 #text_change 10-Sep-1999 ACCESSIONS A04449 REFERENCE A04448 !$#authors Schnier, J.; Isono, K. !$#journal Nucleic Acids Res. (1982) 10:1857-1865 !$#title The DNA sequence of the gene rspA of Escherichia coli coding !1for ribosomal protein S1. !$#cross-references MUID:82196866; PMID:6281725 !$#accession A04449 !'##molecule_type DNA !'##residues 1-143 ##label SCH GENETICS !$#map_position 20 min CLASSIFICATION #superfamily Escherichia coli hypothetical 15.8K protein SUMMARY #length 143 #molecular-weight 15811 #checksum 5475 SEQUENCE /// ENTRY QQECR1 #type complete TITLE relE protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 01-Mar-2002 ACCESSIONS B22830; F64911 REFERENCE A22830 !$#authors Bech, F.W.; Jorgensen, S.T.; Diderichsen, B.; Karlstrom, !1O.H. !$#journal EMBO J. (1985) 4:1059-1066 !$#title Sequence of the relB transcription unit from Escherichia !1coli and identification of the relB gene. !$#cross-references MUID:85257499; PMID:2990907 !$#accession B22830 !'##molecule_type DNA !'##residues 1-95 ##label BEC !'##cross-references GB:X02405; NID:g42699; PIDN:CAA26251.1; PID:g42701 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64911 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-95 ##label BLAT !'##cross-references GB:AE000253; GB:U00096; NID:g1787841; !1PIDN:AAC74636.1; PID:g1787846; UWGP:b1563 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene relE !$#map_position 34 min CLASSIFICATION #superfamily Escherichia coli relE protein SUMMARY #length 95 #molecular-weight 11225 #checksum 4451 SEQUENCE /// ENTRY QQECR9 #type complete TITLE rem protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 01-Mar-2002 ACCESSIONS D22830; D64911 REFERENCE A22830 !$#authors Bech, F.W.; Jorgensen, S.T.; Diderichsen, B.; Karlstrom, !1O.H. !$#journal EMBO J. (1985) 4:1059-1066 !$#title Sequence of the relB transcription unit from Escherichia !1coli and identification of the relB gene. !$#cross-references MUID:85257499; PMID:2990907 !$#accession D22830 !'##molecule_type DNA !'##residues 1-83 ##label BEC !'##cross-references GB:X02405; NID:g42699; PIDN:CAA26253.1; PID:g42703 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64911 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-83 ##label BLAT !'##cross-references GB:AE000253; GB:U00096; NID:g1787841; !1PIDN:AAC74634.1; PID:g1787844; UWGP:b1561 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene rem !$#map_position 34 min CLASSIFICATION #superfamily Escherichia coli rem protein SUMMARY #length 83 #molecular-weight 9235 #checksum 141 SEQUENCE /// ENTRY QQECAD #type complete TITLE probable membrane protein ydiA - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 05-Apr-1983 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS G64928; A04447; PQ0197 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64928 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-277 ##label BLAT !'##cross-references GB:AE000265; GB:U00096; NID:g2367122; !1PIDN:AAC74773.1; PID:g1787995; UWGP:b1703 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A01107 !$#authors Zurawski, G.; Gunsalus, R.P.; Brown, K.D.; Yanofsky, C. !$#journal J. Mol. Biol. (1981) 145:47-73 !$#title Structure and regulation of aroH, the structural gene for !1the tryptophan-repressible 3-deoxy-D-arabino-heptulosonic !1acid-7-phosphate synthetase of Escherichia coli. !$#cross-references MUID:81267314; PMID:6167722 !$#accession A04447 !'##molecule_type DNA !'##residues 'M',154-199,'V',201-277 ##label ZUR REFERENCE JQ1131 !$#authors Hudson, G.S.; Rellos, P.; Davidson, B.E. !$#journal Gene (1991) 102:87-91 !$#title Two promoters control the aroH gene of Escherichia coli. !$#cross-references MUID:91323737; PMID:1677907 !$#accession PQ0197 !'##molecule_type DNA !'##residues 107-277 ##label HUD !'##cross-references GB:M38266; NID:g145376; PIDN:AAA23496.1; !1PID:g145377 GENETICS !$#gene ydiA !$#map_position 37 min CLASSIFICATION #superfamily ydiA protein KEYWORDS nucleotide binding; P-loop FEATURE !$67-83 #domain transmembrane #status predicted #label TM01\ !$157-164 #region nucleotide-binding motif A (P-loop) SUMMARY #length 277 #molecular-weight 31211 #checksum 7560 SEQUENCE /// ENTRY QQECW7 #type complete TITLE yecA protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS D64954; A25071 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64954 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-221 ##label BLAT !'##cross-references GB:AE000284; GB:U00096; NID:g1788214; !1PIDN:AAC74978.1; PID:g1788219; UWGP:b1908 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A25071 !$#authors Tucker, S.D.; Murgola, E.J. !$#journal Biochimie (1985) 67:1053-1057 !$#title Sequence analysis of the glyW region in Escherichia coli. !$#cross-references MUID:86104468; PMID:3002500 !$#accession A25071 !'##molecule_type DNA !'##residues 1-74,'AL' ##label TUC !'##cross-references GB:X03239; GB:M14391; NID:g41604; PIDN:CAA26984.1; !1PID:g41605 COMMENT This protein is coded by a gene immediately downstream of !1glyW, a duplicated gene for glycine tRNA (glycine tRNA3). GENETICS !$#gene yecA !$#map_position 42 min CLASSIFICATION #superfamily yecA protein SUMMARY #length 221 #molecular-weight 25039 #checksum 8046 SEQUENCE /// ENTRY QQEC2K #type complete TITLE hypothetical 21.1K protein (ssr-serA intergenic region) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 01-Mar-2002 ACCESSIONS A21894; G65075 REFERENCE A21894 !$#authors Hsu, L.M.; Zagorski, J.; Wang, Z.; Fournier, M.J. !$#journal J. Bacteriol. (1985) 161:1162-1170 !$#title Escherichia coli 6S RNA gene is part of a dual-function !1transcription unit. !$#cross-references MUID:85130798; PMID:2579060 !$#accession A21894 !'##molecule_type DNA !'##residues 1-182 ##label HSU !'##cross-references GB:M12965; NID:g147873; PIDN:AAA24651.1; !1PID:g147874 !'##experimental_source strain K12 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65075 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-182 ##label BLAT !'##cross-references GB:AE000374; GB:U00096; NID:g1789270; !1PIDN:AAC75949.1; PID:g1789278; UWGP:b2912 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ygfA CLASSIFICATION #superfamily conserved hypothetical protein HI0858 SUMMARY #length 182 #molecular-weight 21105 #checksum 7210 SEQUENCE /// ENTRY Q4ECD8 #type complete TITLE ydfC protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 01-Mar-2002 ACCESSIONS D30383; H64912 REFERENCE A30383 !$#authors Cam, K.; Bejar, S.; Gil, D.; Bouche, J.P. !$#journal Nucleic Acids Res. (1988) 16:6327-6338 !$#title Identification and sequence of gene dicB: translation of the !1division inhibitor from an in-phase internal start. !$#cross-references MUID:88289404; PMID:3041373 !$#accession D30383 !'##molecule_type DNA !'##residues 1-72 ##label CAM REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64912 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-72 ##label BLAT !'##cross-references GB:AE000253; GB:U00096; NID:g1787841; !1PIDN:AAC74646.1; PID:g1787856; UWGP:b1573 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ydfC !$#map_position 35 min CLASSIFICATION #superfamily Escherichia coli ydfC protein SUMMARY #length 72 #molecular-weight 8350 #checksum 2556 SEQUENCE /// ENTRY Q3ECD7 #type complete TITLE ydfD protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 26-Sep-1997 #text_change 01-Mar-2002 ACCESSIONS B64913; S03697; E30383 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64913 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-63 ##label BLAT !'##cross-references GB:AE000253; GB:U00096; NID:g1787841; !1PIDN:AAC74648.1; PID:g1787858; UWGP:b1576 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S03697 !$#authors Barcellini-Couget, S.; Galucci, P.; Bouche, J.P. !$#journal Nucleic Acids Res. (1988) 16:10388 !$#title Escherichia coli dicB operon includes a truncated IS2 !1element. !$#cross-references MUID:89057500; PMID:2848223 !$#accession S03697 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 35-63 ##label BAR !'##cross-references EMBL:X07465 REFERENCE A30383 !$#authors Cam, K.; Bejar, S.; Gil, D.; Bouche, J.P. !$#journal Nucleic Acids Res. (1988) 16:6327-6338 !$#title Identification and sequence of gene dicB: translation of the !1division inhibitor from an in-phase internal start. !$#cross-references MUID:88289404; PMID:3041373 !$#accession E30383 !'##molecule_type DNA !'##residues 1-61,'VFKTVP' ##label CAM GENETICS !$#gene ydfD !$#map_position 35 min CLASSIFICATION #superfamily Escherichia coli ydfD protein SUMMARY #length 63 #molecular-weight 6842 #checksum 7770 SEQUENCE /// ENTRY QQECXQ #type complete TITLE hypothetical protein B-113 - Escherichia coli ORGANISM #formal_name Escherichia coli DATE 05-Apr-1983 #sequence_revision 05-Apr-1983 #text_change 10-Sep-1999 ACCESSIONS A04445 REFERENCE A92366 !$#authors Tso, J.Y.; Zalkin, H.; van Cleemput, M.; Yanofsky, C.; !1Smith, J.M. !$#journal J. Biol. Chem. (1982) 257:3525-3531 !$#title Nucleotide sequence of Escherichia coli purF and deduced !1amino acid sequence of glutamine phosphoribosylpyrophosphate !1amidotransferase. !$#cross-references MUID:82142516; PMID:6277938 !$#accession A04445 !'##molecule_type DNA !'##residues 1-113 ##label TSO GENETICS !$#map_position 49 min !$#start_codon GTG CLASSIFICATION #superfamily Escherichia coli hypothetical 13.3K protein SUMMARY #length 113 #molecular-weight 13327 #checksum 9299 SEQUENCE /// ENTRY QQECXP #type complete TITLE hypothetical protein F-92 - Escherichia coli ORGANISM #formal_name Escherichia coli DATE 05-Apr-1983 #sequence_revision 05-Apr-1983 #text_change 10-Sep-1999 ACCESSIONS A04446 REFERENCE A92366 !$#authors Tso, J.Y.; Zalkin, H.; van Cleemput, M.; Yanofsky, C.; !1Smith, J.M. !$#journal J. Biol. Chem. (1982) 257:3525-3531 !$#title Nucleotide sequence of Escherichia coli purF and deduced !1amino acid sequence of glutamine phosphoribosylpyrophosphate !1amidotransferase. !$#cross-references MUID:82142516; PMID:6277938 !$#accession A04446 !'##molecule_type DNA !'##residues 1-92 ##label TSO GENETICS !$#map_position 49 min CLASSIFICATION #superfamily Escherichia coli hypothetical 10.2K protein SUMMARY #length 92 #molecular-weight 10156 #checksum 8082 SEQUENCE /// ENTRY QQECE5 #type complete TITLE hypothetical 73.3K protein (mreB-accB intergenic region) - Escherichia coli (strain K-12) ALTERNATE_NAMES hypothetical protein 102 (envB 5' region) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1990 #sequence_revision 30-Sep-1997 #text_change 01-Mar-2002 ACCESSIONS F65117; B31843; PS0032 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65117 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-646 ##label BLAT !'##cross-references GB:AE000404; GB:U00096; NID:g2367207; !1PIDN:AAC76284.1; PID:g1789650; UWGP:b3252 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A91887 !$#authors Doi, M.; Wachi, M.; Ishino, F.; Tomioka, S.; Ito, M.; !1Sakagami, Y.; Suzuki, A.; Matsuhashi, M. !$#journal J. Bacteriol. (1988) 170:4619-4624 !$#title Determinations of the DNA sequence of the mreB gene and of !1the gene products of the mre region that function in !1formation of the rod shape of Escherichia coli cells. !$#cross-references MUID:89008079; PMID:3049542 !$#accession B31843 !'##molecule_type DNA !'##residues 545-646 ##label DOI !'##cross-references GB:M22055; NID:g146887; PIDN:AAA83890.1; !1PID:g1128966 !'##experimental_source strain K12 GENETICS !$#gene yhdA !$#map_position 71 min CLASSIFICATION #superfamily Escherichia coli hypothetical 73.3K protein !1(mreB-accB intergenic region) SUMMARY #length 646 #molecular-weight 73339 #checksum 2428 SEQUENCE /// ENTRY Q4ECAD #type complete TITLE damX protein (aroB-dam intergenic region) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1990 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS G65133; A93129; S31743; A30921; JS0141 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65133 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-428 ##label BLAT !'##cross-references GB:AE000414; GB:U00096; NID:g1789783; !1PIDN:AAC76413.1; PID:g1789790; UWGP:b3388 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A93129 !$#authors Jonczyk, P.; Hines, R.; Smith, D.W. !$#journal Mol. Gen. Genet. (1989) 217:85-96 !$#title The Escherichia coli dam gene is expressed as a distal gene !1of a new operon. !$#cross-references MUID:89364696; PMID:2549371 !$#accession A93129 !'##molecule_type DNA !'##residues 1-5,'T',7-30,'P',32-85,'L','V',89,'VS',92-309,'V',311-381, !1'V',383-428 ##label JON !'##cross-references GB:X15162; NID:g43273; PIDN:CAA33253.1; PID:g43274 !'##experimental_source strain K12 REFERENCE S31739 !$#authors Lyngstadaas, A.; Boye, E. !$#submission submitted to the EMBL Data Library, January 1993 !$#description dam operon. !$#accession S31743 !'##molecule_type DNA !'##residues 1-5,'T',7-30,'P',32-85,'L','V',89,'VS',92-232,'L',234-309, !1'V',311-365,'N',367-381,'V',383-428 ##label LYN !'##cross-references EMBL:Z19601; NID:g41221; PIDN:CAA79667.1; !1PID:g41226 COMMENT The gene that codes for this protein is part of an operon !1that includes the dam gene and possibly the aroB gene. GENETICS !$#gene damX !$#map_position 74.3 min CLASSIFICATION #superfamily damX protein SUMMARY #length 428 #molecular-weight 46162 #checksum 4482 SEQUENCE /// ENTRY QQEC13 #type complete TITLE hypothetical 13.5K protein (ppdC-ppdB intergenic region) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 01-Mar-2002 ACCESSIONS D24137; A65065 REFERENCE A93625 !$#authors Finch, P.W.; Wilson, R.E.; Brown, K.; Hickson, I.D.; !1Tomkinson, A.E.; Emmerson, P.T. !$#journal Nucleic Acids Res. (1986) 14:4437-4451 !$#title Complete nucleotide sequence of the Escherichia coli recC !1gene and of the thyA-recC intergenic region. !$#cross-references MUID:86232583; PMID:3520484 !$#accession D24137 !'##molecule_type DNA !'##residues 1-121 ##label FIN !'##cross-references GB:X03966; NID:g42684; PIDN:CAA27602.1; PID:g42687 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65065 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-121 ##label BLAT !'##cross-references GB:AE000366; GB:U00096; NID:g1789185; !1PIDN:AAC75863.1; PID:g1789188; UWGP:b2824 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ygdB !$#map_position 61 min CLASSIFICATION #superfamily Escherichia coli hypothetical 13.5K protein !1(ppdC-ppdB intergenic region) SUMMARY #length 121 #molecular-weight 13474 #checksum 5261 SEQUENCE /// ENTRY QQECB7 #type complete TITLE yheA protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Sep-1990 #sequence_revision 30-Sep-1990 #text_change 01-Mar-2002 ACCESSIONS JV0033; D65127 REFERENCE JV0032 !$#authors Andrews, S.C.; Harrison, P.M.; Guest, J.R. !$#journal J. Bacteriol. (1989) 171:3940-3947 !$#title Cloning, sequencing, and mapping of the bacterioferritin !1gene (bfr) of Escherichia coli K-12. !$#cross-references MUID:89291745; PMID:2661540 !$#accession JV0033 !'##molecule_type DNA !'##residues 1-64 ##label AND !'##cross-references GB:M27176; NID:g145406; PIDN:AAC13986.1; !1PID:g145408 !'##experimental_source strain K12 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65127 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-64 ##label BLAT !'##cross-references GB:AE000410; GB:U00096; NID:g1789734; !1PIDN:AAC76362.1; PID:g1789735; UWGP:b3337 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yheA !$#map_position 73 min CLASSIFICATION #superfamily yheA protein SUMMARY #length 64 #molecular-weight 7363 #checksum 6796 SEQUENCE /// ENTRY QQEC17 #type complete TITLE hypothetical 17.7K protein (secB region) - Escherichia coli ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 26-Aug-1999 ACCESSIONS JS0125 REFERENCE A91601 !$#authors Kumamoto, C.A.; Nault, A.K. !$#journal Gene (1989) 75:167-175 !$#title Characterization of the Escherichia coli protein-export gene !1secB. !$#cross-references MUID:89252913; PMID:2656409 !$#accession JS0125 !'##molecule_type DNA !'##residues 1-150 ##label KUM !'##cross-references GB:M24489; GB:M24490; NID:g147796; PIDN:AAA83908.1; !1PID:g1128972 !'##experimental_source strain K12 COMMENT This protein is encoded by the opposite strand of the secB !1gene. CLASSIFICATION #superfamily Escherichia coli hypothetical 17.7K protein !1(secB region) SUMMARY #length 150 #molecular-weight 17665 #checksum 3322 SEQUENCE /// ENTRY Q4ECKR #type complete TITLE fucose operon U protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS H65062; JS0187 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65062 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-140 ##label BLAT !'##cross-references GB:AE000364; GB:U00096; NID:g2367162; !1PIDN:AAC75846.1; PID:g1789169; UWGP:b2804 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S04702 !$#authors Lu, Z.; Lin, E.C.C. !$#journal Nucleic Acids Res. (1989) 17:4883-4884 !$#title The nucleotide sequence of Escherichia coli genes for !1L-fucose dissimilation. !$#cross-references MUID:89315234; PMID:2664711 !$#accession JS0187 !'##molecule_type DNA !'##residues 1-105,'IVLR',110,'MNGRK',116,'PLRSLSQANERST',130,'IFF' !1##label LUZ !'##cross-references GB:X15025; NID:g41501; PIDN:CAA33129.1; PID:g41507 GENETICS !$#gene fucU !$#map_position 60 min CLASSIFICATION #superfamily fucose operon U protein SUMMARY #length 140 #molecular-weight 15473 #checksum 4820 SEQUENCE /// ENTRY S01828 #type complete TITLE probable high-affinity transport protein P37 precursor - Mycoplasma hyorhinis ALTERNATE_NAMES 37K protein ORGANISM #formal_name Mycoplasma hyorhinis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 07-Dec-1999 ACCESSIONS S01828 REFERENCE S01828 !$#authors Dudler, R.; Schmidhauser, C.; Parish, R.W.; Wettenhall, !1R.E.H.; Schmidt, T. !$#journal EMBO J. (1988) 7:3963-3970 !$#title A mycoplasma high-affinity transport system and the in vitro !1invasiveness of mouse sarcoma cells. !$#cross-references MUID:89091146; PMID:3208756 !$#accession S01828 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-403 ##label DUD !'##cross-references GB:X14140; NID:g288402; PIDN:CAA32357.1; !1PID:g577661 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing GENETICS !$#genetic_code SGC3 !$#start_codon TTG CLASSIFICATION #superfamily Mycoplasma hyorhinis high affinity transport !1system protein P37 FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-403 #product probable high-affinity transport protein !8#status experimental #label MAT SUMMARY #length 403 #molecular-weight 46118 #checksum 3770 SEQUENCE /// ENTRY I64231 #type complete TITLE high affinity transport system protein P37 homolog - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS I64231 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession I64231 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-368 ##label TIGR !'##cross-references GB:U39709; GB:L43967; NID:g3844870; !1PIDN:AAC71510.1; PID:g1045986; TIGR:MG289 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 !$#start_codon GTG CLASSIFICATION #superfamily Mycoplasma hyorhinis high affinity transport !1system protein P37 SUMMARY #length 368 #molecular-weight 42258 #checksum 2867 SEQUENCE /// ENTRY S73751 #type complete TITLE high affinity transport system protein P37 - Mycoplasma pneumoniae (strain ATCC 29342) ALTERNATE_NAMES hypothetical protein A05_orf380V ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Dec-1999 ACCESSIONS S73751 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73751 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-380 ##label HIM !'##cross-references EMBL:AE000041; GB:U00089; NID:g1674104; !1PIDN:AAB96073.1; PID:g1674110 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#gene P37 !$#genetic_code SGC3 !$#start_codon GTG CLASSIFICATION #superfamily Mycoplasma hyorhinis high affinity transport !1system protein P37 SUMMARY #length 380 #molecular-weight 43495 #checksum 9892 SEQUENCE /// ENTRY QQEC30 #type complete TITLE prepilin peptidase dependent protein B precursor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS B65065; C24137 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65065 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-187 ##label BLAT !'##cross-references GB:AE000366; GB:U00096; NID:g1789185; !1PIDN:AAC75864.1; PID:g1789189; UWGP:b2825 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A93625 !$#authors Finch, P.W.; Wilson, R.E.; Brown, K.; Hickson, I.D.; !1Tomkinson, A.E.; Emmerson, P.T. !$#journal Nucleic Acids Res. (1986) 14:4437-4451 !$#title Complete nucleotide sequence of the Escherichia coli recC !1gene and of the thyA-recC intergenic region. !$#cross-references MUID:86232583; PMID:3520484 !$#accession C24137 !'##molecule_type DNA !'##residues !1'MVPCEFRCWGQYLSWQFTIGLCATLARSRNERPDTFACFLWPAQYRMGRAYSLQKLNGR !1VVAGGFAVGKTPALSARRNRR',1-187 ##label FIN !'##cross-references GB:X03966; NID:g42684; PIDN:CAA27601.1; PID:g42686 GENETICS !$#gene ppdB !$#map_position 61 min CLASSIFICATION #superfamily prepilin peptidase dependent protein B !1precursor SUMMARY #length 187 #molecular-weight 20519 #checksum 9433 SEQUENCE /// ENTRY QQEC12 #type complete TITLE prepilin peptidase dependent protein C precursor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 01-Mar-2002 ACCESSIONS E24137; H65064 REFERENCE A93625 !$#authors Finch, P.W.; Wilson, R.E.; Brown, K.; Hickson, I.D.; !1Tomkinson, A.E.; Emmerson, P.T. !$#journal Nucleic Acids Res. (1986) 14:4437-4451 !$#title Complete nucleotide sequence of the Escherichia coli recC !1gene and of the thyA-recC intergenic region. !$#cross-references MUID:86232583; PMID:3520484 !$#accession E24137 !'##molecule_type DNA !'##residues 1-107 ##label FIN !'##cross-references GB:X03966; NID:g42684; PIDN:CAA27603.1; PID:g42688 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65064 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-107 ##label BLAT !'##cross-references GB:AE000366; GB:U00096; NID:g1789185; !1PIDN:AAC75862.1; PID:g1789187; UWGP:b2823 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ppdC !$#map_position 61 min CLASSIFICATION #superfamily prepilin peptidase dependent protein C !1precursor SUMMARY #length 107 #molecular-weight 12004 #checksum 9287 SEQUENCE /// ENTRY QQECK #type complete TITLE hypothetical 25.2K (lysR-araE intergenic region) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 01-Mar-2002 ACCESSIONS A04438; A65067 REFERENCE A92901 !$#authors Stragier, P.; Patte, J.C. !$#journal J. Mol. Biol. (1983) 168:333-350 !$#title Regulation of diaminopimelate decarboxylase synthesis in !1Escherichia coli. III. Nucleotide sequence and regulation of !1the lysR gene. !$#cross-references MUID:83294517; PMID:6350602 !$#accession A04438 !'##molecule_type DNA !'##residues 1-230 ##label STR !'##cross-references GB:J01614; NID:g146067; PIDN:AAA83863.1; !1PID:g1128956 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65067 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-230 ##label BLAT !'##cross-references GB:AE000367; GB:U00096; NID:g1789195; !1PIDN:AAC75879.1; PID:g1789205; UWGP:b2840 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ygeA !$#map_position 61 min CLASSIFICATION #superfamily Escherichia coli hypothetical 25.2K (lysR-araE !1intergenic region) SUMMARY #length 230 #molecular-weight 25248 #checksum 3101 SEQUENCE /// ENTRY QQEC2B #type complete TITLE hypothetical protein (gapB-cmtA intergenic region) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS H65077; S04730 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65077 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-169 ##label BLAT !'##cross-references GB:AE000376; GB:U00096; NID:g2367176; !1PIDN:AAC75966.1; PID:g1789297; UWGP:b2929 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S04730 !$#authors Alefounder, P.R.; Perham, R.N. !$#journal Mol. Microbiol. (1989) 3:723-732 !$#title Identification, molecular cloning and sequence analysis of a !1gene cluster encoding the class II fructose 1,6-bisphosphate !1aldolase, 3-phosphoglycerate kinase and a putative second !1glyceraldehyde 3-phosphate dehydrogenase of Escherichia !1coli. !$#cross-references MUID:89313302; PMID:2546007 !$#accession S04730 !'##molecule_type DNA !'##residues 23-155 ##label ALE !'##cross-references EMBL:X14436; NID:g41417; PIDN:CAA32601.1; !1PID:g41419 GENETICS !$#gene yggD !$#map_position 63 min CLASSIFICATION #superfamily Escherichia coli hypothetical protein !1(gapB-cmtA intergenic region) SUMMARY #length 169 #molecular-weight 19272 #checksum 8408 SEQUENCE /// ENTRY QQEC3B #type complete TITLE hypothetical 27.1K protein (gapB-cmtA intergenic region) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS G65077; S04731 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65077 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-237 ##label BLAT !'##cross-references GB:AE000376; GB:U00096; NID:g2367176; !1PIDN:AAC75965.1; PID:g1789296; UWGP:b2928 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S04730 !$#authors Alefounder, P.R.; Perham, R.N. !$#journal Mol. Microbiol. (1989) 3:723-732 !$#title Identification, molecular cloning and sequence analysis of a !1gene cluster encoding the class II fructose 1,6-bisphosphate !1aldolase, 3-phosphoglycerate kinase and a putative second !1glyceraldehyde 3-phosphate dehydrogenase of Escherichia !1coli. !$#cross-references MUID:89313302; PMID:2546007 !$#accession S04731 !'##molecule_type DNA !'##residues 81-237 ##label ALE !'##cross-references EMBL:X14436; NID:g41417; PIDN:CAA32602.1; !1PID:g41420 GENETICS !$#gene yggC !$#map_position 63 min CLASSIFICATION #superfamily Escherichia coli hypothetical 27.1K protein !1(gapB-cmtA intergenic region) SUMMARY #length 237 #molecular-weight 27132 #checksum 6541 SEQUENCE /// ENTRY QQEC4A #type complete TITLE hypothetical 30.9K protein (sbm-fba intergenic region) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 01-Mar-2002 ACCESSIONS S04735; C65077 REFERENCE S04730 !$#authors Alefounder, P.R.; Perham, R.N. !$#journal Mol. Microbiol. (1989) 3:723-732 !$#title Identification, molecular cloning and sequence analysis of a !1gene cluster encoding the class II fructose 1,6-bisphosphate !1aldolase, 3-phosphoglycerate kinase and a putative second !1glyceraldehyde 3-phosphate dehydrogenase of Escherichia !1coli. !$#cross-references MUID:89313302; PMID:2546007 !$#accession S04735 !'##molecule_type DNA !'##residues 1-286 ##label ALE !'##cross-references EMBL:X14436; NID:g41417; PIDN:CAA32606.1; !1PID:g41424 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65077 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-286 ##label BLAT !'##cross-references GB:AE000375; GB:U00096; NID:g1789282; !1PIDN:AAC75961.1; PID:g1789291; UWGP:b2924 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yggB !$#map_position 63 min CLASSIFICATION #superfamily Escherichia coli hypothetical 30.9K protein !1(sbm-fba intergenic region) SUMMARY #length 286 #molecular-weight 30896 #checksum 7523 SEQUENCE /// ENTRY QQEC5A #type complete TITLE hypothetical 23K protein (sbm-fba intergenic region) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS B65077; S04736 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65077 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-211 ##label BLAT !'##cross-references GB:AE000375; GB:U00096; NID:g1789282; !1PIDN:AAC75960.1; PID:g1789290; UWGP:b2923 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S04730 !$#authors Alefounder, P.R.; Perham, R.N. !$#journal Mol. Microbiol. (1989) 3:723-732 !$#title Identification, molecular cloning and sequence analysis of a !1gene cluster encoding the class II fructose 1,6-bisphosphate !1aldolase, 3-phosphoglycerate kinase and a putative second !1glyceraldehyde 3-phosphate dehydrogenase of Escherichia !1coli. !$#cross-references MUID:89313302; PMID:2546007 !$#accession S04736 !'##molecule_type DNA !'##residues 15-211 ##label ALE !'##cross-references EMBL:X14436; NID:g41417; PIDN:CAA32607.1; !1PID:g41425 GENETICS !$#gene yggA !$#map_position 63 min CLASSIFICATION #superfamily Escherichia coli hypothetical 23K protein !1(sbm-fba intergenic region) SUMMARY #length 211 #molecular-weight 23175 #checksum 2783 SEQUENCE /// ENTRY QQEC15 #type complete TITLE hypothetical 34K protein (gapB-cmtA intergenic region) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS A65078; S04738 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65078 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-321 ##label BLAT !'##cross-references GB:AE000376; GB:U00096; NID:g2367176; !1PIDN:AAC75967.1; PID:g1789298; UWGP:b2930 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S04730 !$#authors Alefounder, P.R.; Perham, R.N. !$#journal Mol. Microbiol. (1989) 3:723-732 !$#title Identification, molecular cloning and sequence analysis of a !1gene cluster encoding the class II fructose 1,6-bisphosphate !1aldolase, 3-phosphoglycerate kinase and a putative second !1glyceraldehyde 3-phosphate dehydrogenase of Escherichia !1coli. !$#cross-references MUID:89313302; PMID:2546007 !$#accession S04738 !'##molecule_type DNA !'##residues 227-321 ##label ALE !'##cross-references EMBL:X14436; NID:g41417; PIDN:CAA32600.1; !1PID:g41418 GENETICS !$#gene yggF !$#map_position 63 min CLASSIFICATION #superfamily Escherichia coli hypothetical 34K protein !1(gapB-cmtA intergenic region) SUMMARY #length 321 #molecular-weight 34323 #checksum 2737 SEQUENCE /// ENTRY QQEC89 #type complete TITLE hypothetical protein (aroF-rplS intergenic region) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1989 #sequence_revision 30-Sep-1997 #text_change 01-Mar-2002 ACCESSIONS E65038; A30262 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65038 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-134 ##label BLAT !'##cross-references GB:AE000346; GB:U00096; NID:g2367141; !1PIDN:AAC75651.1; PID:g1788954; UWGP:b2602 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A92910 !$#authors Hudson, G.S.; Davidson, B.E. !$#journal J. Mol. Biol. (1984) 180:1023-1051 !$#title Nucleotide sequence and transcription of the phenylalanine !1and tyrosine operons of Escherichia coli K12. !$#cross-references MUID:85134883; PMID:6396419 !$#accession A30262 !'##molecule_type DNA !'##residues 14-102 ##label HUD !'##cross-references GB:M10431; EMBL:X02137 GENETICS !$#gene yfiL !$#map_position 57 min CLASSIFICATION #superfamily Escherichia coli hypothetical protein !1(aroF-rplS intergenic region) SUMMARY #length 134 #molecular-weight 14824 #checksum 6965 SEQUENCE /// ENTRY QQEC3R #type complete TITLE transcription activator nhaR - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1991 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS D64722; S07928; S40542; JN0325 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64722 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-301 ##label BLAT !'##cross-references GB:AE000112; GB:U00096; NID:g1786192; !1PIDN:AAC73131.1; PID:g1786202; UWGP:b0020 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S07374 !$#authors Mackie, G.A. !$#journal Nucleic Acids Res. (1986) 14:6965-6981 !$#title Structure of the DNA distal to the gene for ribosomal !1protein S20 in Escherichia coli K12: presence of a strong !1terminator and an IS1 element. !$#cross-references MUID:87016337; PMID:2429258 !$#accession S07928 !'##status translation not shown !'##molecule_type DNA !'##residues 1-45,'DA',48-49,'A',51-57,'TWSRTQRA',66-145,'E',147-232, !1'W','LQVLLVAMQM',280,'SSLP',285-286,'FMHMTFMPIKLS' ##label !1MAC !'##cross-references GB:J01683; EMBL:X04382; NID:g42864; !1PIDN:CAA27969.1; PID:g42866 REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40542 !'##molecule_type DNA !'##residues 1-45,'DA',48-49,'A',51-57,'TWSRTQRA',66-145,'E',147-232, !1'W','LQVLLVAMQM',280,'SSLP',285-286,'FMHMTFMPIKLS' ##label !1YUR !'##cross-references EMBL:D10483; NID:g216434; PIDN:BAA01297.1; !1PID:g216446 REFERENCE JN0325 !$#authors Rahav-Manor, O.; Carmel, O.; Karpel, R.; Taglicht, D.; !1Glaser, G.; Schuldiner, S.; Padan, E. !$#journal J. Biol. Chem. (1992) 267:10433-10438 !$#title NhaR, a protein homologous to a family of bacterial !1regulatory proteins (LysR), regulates nhaA, the sodium !1proton antiporter gene in Escherichia coli. !$#cross-references MUID:92268083; PMID:1316901 !$#accession JN0325 !'##molecule_type DNA !'##residues 220-301 ##label RAH !'##cross-references GB:S36154; NID:g249598; PIDN:AAB22211.1; !1PID:g249599 COMMENT This protein is a positive regulator for the nhaA gene. GENETICS !$#gene nhaR !$#map_position 0 min CLASSIFICATION #superfamily regulatory protein nhaR KEYWORDS DNA binding; transcription regulation FEATURE !$23-42 #region helix-turn-helix motif SUMMARY #length 301 #molecular-weight 34284 #checksum 6990 SEQUENCE /// ENTRY S37312 #type complete TITLE transcription activator hlyT NhaR VC0677 [similarity] - Vibrio cholerae (strain N16961 serogroup O1) ORGANISM #formal_name Vibrio cholerae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 02-Feb-2001 ACCESSIONS S37312; G82292 REFERENCE S37312 !$#authors Williams, S.G.; Attridge, S.R.; Manning, P.A. !$#journal Mol. Microbiol. (1993) 9:751-760 !$#title The transcriptional activator HlyU of Vibrio cholerae: !1nucleotide sequence and role in virulence gene expression. !$#cross-references MUID:94049116; PMID:8231807 !$#accession S37312 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-296 ##label WIL !'##cross-references EMBL:X66866; NID:g403330; PID:g403331 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1992 REFERENCE A82035 !$#authors Heidelberg, J.F.; Eisen, J.A.; Nelson, W.C.; Clayton, R.A.; !1Gwinn, M.L.; Dodson, R.J.; Haft, D.H.; Hickey, E.K.; !1Peterson, J.D.; Umayam, L.A.; Gill, S.R.; Nelson, K.E.; !1Read, T.D.; Tettelin, H.; Richardson, D.; Ermolaeva, M.D.; !1Vamathevan, J.; Bass, S.; Qin, H.; Dragoi, I.; Sellers, P.; !1McDonald, L.; Utterback, T.; Fleishmann, R.D.; Nierman, !1W.C.; White, O.; Salzberg, S.L.; Smith, H.O.; Colwell, R.R.; !1Mekalanos, J.J.; Venter, J.C.; Fraser, C.M. !$#journal Nature (2000) 406:477-483 !$#title DNA Sequence of both chromosomes of the cholera pathogen !1Vibrio cholerae. !$#cross-references MUID:20406833; PMID:10952301 !$#accession G82292 !'##status preliminary !'##molecule_type DNA !'##residues 1-296 ##label HEI !'##cross-references GB:AE004154; GB:AE003852; NID:g9655115; !1PIDN:AAF93842.1; GSPDB:GN00126; TIGR:VC0677 !'##experimental_source serogroup O1; strain N16961; biotype El Tor GENETICS !$#gene hlyT; VC0677 !$#map_position 1 CLASSIFICATION #superfamily regulatory protein nhaR KEYWORDS DNA binding; transcription regulation FEATURE !$21-40 #region helix-turn-helix motif SUMMARY #length 296 #molecular-weight 33559 #checksum 5219 SEQUENCE /// ENTRY QQECR6 #type complete TITLE O-sialoglycoprotein endopeptidase (EC 3.4.24.57) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS F65094; D29049 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65094 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-337 ##label BLAT !'##cross-references GB:AE000388; GB:U00096; NID:g1789441; !1PIDN:AAC76100.1; PID:g1789445; UWGP:b3064 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A91573 !$#authors Nesin, M.; Lupski, J.R.; Svec, P.; Godson, G.N. !$#journal Gene (1987) 51:149-161 !$#title Possible new genes as revealed by molecular analysis of a !15-kb Escherichia coli chromosomal region 5' to the !1rpsU-dnaG-rpoD macromolecular-synthesis operon. !$#cross-references MUID:87248073; PMID:3297921 !$#accession D29049 !'##molecule_type DNA !'##residues 1-135,'C',137-337 ##label NES !'##cross-references GB:M16194; GB:X00773; NID:g147764; PIDN:AAA72575.1; !1PID:g551834 GENETICS !$#gene ygjD !$#map_position 67 min CLASSIFICATION #superfamily O-sialoglycoprotein endopeptidase KEYWORDS hydrolase; metalloproteinase; zinc FEATURE !$111,115 #binding_site zinc (His) #status predicted SUMMARY #length 337 #molecular-weight 36008 #checksum 5464 SEQUENCE /// ENTRY QQECU1 #type complete TITLE probable transcription regulator sdiA - Escherichia coli (strain K-12) ALTERNATE_NAMES trans-acting factor sdiA ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS A64955; A24964 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64955 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-240 ##label BLAT !'##cross-references GB:AE000284; GB:U00096; NID:g1788214; !1PIDN:AAC74983.1; PID:g1788224; UWGP:b1916 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A93609 !$#authors Sharma, S.; Stark, T.F.; Beattie, W.G.; Moses, R.E. !$#journal Nucleic Acids Res. (1986) 14:2301-2318 !$#title Multiple control elements for the uvrC gene unit of !1Escherichia coli. !$#cross-references MUID:86176730; PMID:3515318 !$#accession A24964 !'##molecule_type DNA !'##residues 1-119,'HSVFNAAQTG',129-139,'R',141-240 ##label SHA !'##cross-references GB:X03691; GB:X00189; GB:X00638; NID:g43287; !1PIDN:CAA27327.1; PID:g43288 REFERENCE S17790 !$#authors Wang, X.; de Boer, P.A.J.; Rothfield, L.I. !$#journal EMBO J. (1991) 10:3363-3372 !$#title A factor that positively regulates cell division by !1activating transcription of the major cluster of essential !1cell division genes of Escherichia coli. !$#cross-references MUID:92007787; PMID:1915297 !$#contents annotation GENETICS !$#gene sdiA !$#map_position 68 min FUNCTION !$#description suppresses cell division inhibitors !$#note increases specifically transcription of the ftsQAZ gene !1cluster, resulting in an increase in cellular concentration !1of the fTsZ protein CLASSIFICATION #superfamily sdiA regulatory protein KEYWORDS DNA binding; transcription regulation SUMMARY #length 240 #molecular-weight 28117 #checksum 60 SEQUENCE /// ENTRY QQEC94 #type complete TITLE dicarboxylate membrane-transporter protein A - Escherichia coli (strain K-12) ALTERNATE_NAMES anaerobic c4-dicarboxylate transporter dcua; aspartase membrane transport protein genA ORGANISM #formal_name Escherichia coli DATE 17-Mar-1987 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS S56366; S57340; H65223; A04471; S08589 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56366 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-433 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97037.1; !1PID:g536982 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE S57340 !$#authors Six, S.; Andrews, S.C.; Unden, G.; Guest, J.R. !$#journal J. Bacteriol. (1994) 176:6470-6478 !$#title Escherichia coli possesses two homologous anaerobic C !1(4)-dicarboxylate membrane transporters (DcuA and DcuB) !1distinct from the aerobic dicarboxylate transport system !1(Dct). !$#cross-references MUID:95050204; PMID:7961398 !$#accession S57340 !'##molecule_type DNA !'##residues 1-433 ##label SIX !'##cross-references EMBL:X79887; NID:g510887; PIDN:CAA56259.1; !1PID:g510888 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65223 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-433 ##label BLAT !'##cross-references GB:AE000486; GB:U00096; NID:g1790574; !1PIDN:AAC77098.1; PID:g1790580; UWGP:b4138 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A93560 !$#authors Takagi, J.S.; Ida, N.; Tokushige, M.; Sakamoto, H.; Shimura, !1Y. !$#journal Nucleic Acids Res. (1985) 13:2063-2074 !$#title Cloning and nucleotide sequence of the aspartase gene of !1Escherichia coli W. !$#cross-references MUID:85215599; PMID:2987841 !$#accession A04471 !'##molecule_type DNA !'##residues 1-354,'IA',357-364,'R' ##label TAK !'##cross-references GB:X02307; NID:g41001; PIDN:CAA26176.1; PID:g41004 !'##experimental_source strain W REFERENCE S07138 !$#authors Woods, S.A.; Miles, J.S.; Roberts, R.E.; Guest, J.R. !$#journal Biochem. J. (1986) 237:547-557 !$#title Structural and functional relationships between fumarase and !1aspartase. Nucleotide sequences of the fumarase (fumC) and !1aspartase (aspA) genes of Escherichia coli K12. !$#cross-references MUID:87099873; PMID:3541901 !$#accession S08589 !'##molecule_type DNA !'##residues 1-264 ##label WOO !'##cross-references EMBL:X04066; NID:g41006; PIDN:CAA27702.1; !1PID:g41009 !'##experimental_source strain K12 GENETICS !$#gene dcuA; genA !$#map_position 94 min CLASSIFICATION #superfamily dicarboxylate membrane-transporter protein A KEYWORDS transmembrane protein SUMMARY #length 433 #molecular-weight 45750 #checksum 8668 SEQUENCE /// ENTRY QQECR3 #type complete TITLE hypothetical protein E-116 - Escherichia coli ORGANISM #formal_name Escherichia coli DATE 05-Apr-1983 #sequence_revision 05-Apr-1983 #text_change 10-Sep-1999 ACCESSIONS A04439 REFERENCE A04439 !$#authors Post, L.E.; Arfsten, A.E.; Davis, G.R.; Nomura, M. !$#journal J. Biol. Chem. (1980) 255:4653-4659 !$#title DNA sequence of the promoter region for the alpha ribosomal !1protein operon in Escherichia coli. !$#cross-references MUID:80182128; PMID:6154696 !$#accession A04439 !'##molecule_type DNA !'##residues 1-116 ##label POS GENETICS !$#map_position 72 min CLASSIFICATION #superfamily Escherichia coli hypothetical 13.6K protein SUMMARY #length 116 #molecular-weight 13603 #checksum 3925 SEQUENCE /// ENTRY QQECRP #type complete TITLE pino protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 05-Apr-1983 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS E65125; A04450 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65125 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-139 ##label BLAT !'##cross-references GB:AE000409; GB:U00096; NID:g1789718; !1PIDN:AAC76347.1; PID:g1789719; UWGP:b3322 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A02720 !$#authors Olins, P.O.; Nomura, M. !$#journal Cell (1981) 26:205-211 !$#title Regulation of the S10 ribosomal protein operon in E. coli: !1nucleotide sequence at the start of the operon. !$#cross-references MUID:82137054; PMID:7037196 !$#accession A04450 !'##molecule_type DNA !'##residues 'MTDLPVVCRNGAGWWVCQAAMG',8,'LDS',12,'SRS',16,'L',67-139 !1##label OLI GENETICS !$#gene pinO !$#map_position 72 min CLASSIFICATION #superfamily pinO protein SUMMARY #length 139 #molecular-weight 15876 #checksum 6665 SEQUENCE /// ENTRY QQEC16 #type complete TITLE mioC protein - Escherichia coli (strain K-12) ALTERNATE_NAMES hypothetical protein b2790 ORGANISM #formal_name Escherichia coli DATE 02-Apr-1982 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS G65177; A04442; A30410 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65177 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-147 ##label BLAT !'##cross-references GB:AE000451; GB:U00096; NID:g2367272; !1PIDN:AAC76765.1; PID:g1790181; UWGP:b3742 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A04442 !$#authors Sugimoto, K.; Oka, A.; Sugisaki, H.; Takanami, M.; !1Nishimura, A.; Yasuda, Y.; Hirota, Y. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1979) 76:575-579 !$#title Nucleotide sequence of Escherichia coli K-12 replication !1origin. !$#cross-references MUID:79137155; PMID:370832 !$#accession A04442 !'##molecule_type DNA !'##residues 1-55,'PTVPEIFRTTFLLSMKHCRNRS',78,'IFLQSALAQSVLAVVNMTP',98, !1'V',100-147 ##label SUG !'##cross-references GB:J01657; GB:X02820; NID:g147023; PIDN:AAA24247.1; !1PID:g455177 !'##experimental_source strain K12 REFERENCE A30410 !$#authors Hirota, Y.; Yamada, M.; Nishimura, A.; Oka, A.; Sugimoto, !1K.; Asada, K.; Takanami, M. !$#journal Prog. Nucleic Acid Res. Mol. Biol. (1981) 26:33-48 !$#title The DNA replication origin (ori) of Escherichia coli: !1structure and function of the ori-containing DNA fragment. !$#cross-references MUID:82016299; PMID:6169112 !$#accession A30410 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-55,'PTVPEIFRTTFLLSMKHCRNRS',78,'IFLQSALAQSVLAVVNMTP',98, !1'V',100-147 ##label HIR GENETICS !$#gene mioC !$#map_position 83 min CLASSIFICATION #superfamily mioC protein; flavodoxin homology KEYWORDS flavoprotein FEATURE !$6-147 #domain flavodoxin homology #label FLX SUMMARY #length 147 #molecular-weight 15807 #checksum 9316 SEQUENCE /// ENTRY C64085 #type complete TITLE hypothetical protein HI0669 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS C64085 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession C64085 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-146 ##label TIGR !'##cross-references GB:U32750; GB:L42023; NID:g1573668; !1PIDN:AAC22329.1; PID:g1573670; TIGR:HI0669 CLASSIFICATION #superfamily mioC protein; flavodoxin homology KEYWORDS flavoprotein FEATURE !$5-141 #domain flavodoxin homology #label FLX SUMMARY #length 146 #molecular-weight 16030 #checksum 1443 SEQUENCE /// ENTRY S45108 #type complete TITLE hypothetical protein 2 - Erwinia carotovora ORGANISM #formal_name Erwinia carotovora DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 15-Oct-1999 ACCESSIONS S45108 REFERENCE S45107 !$#authors Golby, P.; Jones, S.E.; Stephens, S.; Reeves, P.J.; Bycroft, !1B.; Stewart, G.; Williams, P.; Salmond, G.P.C. !$#submission submitted to the EMBL Data Library, May 1994 !$#description Global regulation of Erwinia carotovora exoenzyme virulence !1factors: multicopy suppression of rex mutants and evidence !1for a global repression regulon. !$#accession S45108 !'##status preliminary !'##molecule_type DNA !'##residues 1-151 ##label GOL !'##cross-references EMBL:X79474; NID:g496597; PID:g496599 CLASSIFICATION #superfamily mioC protein; flavodoxin homology KEYWORDS flavoprotein FEATURE !$6-144 #domain flavodoxin homology #label FLX SUMMARY #length 151 #molecular-weight 16417 #checksum 4151 SEQUENCE /// ENTRY B65061 #type complete TITLE hypothetical protein b2790 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS B65061 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65061 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-149 ##label BLAT !'##cross-references GB:AE000363; GB:U00096; NID:g1789153; !1PIDN:AAC75832.1; PID:g1789154; UWGP:b2790 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily mioC protein; flavodoxin homology KEYWORDS flavoprotein FEATURE !$6-144 #domain flavodoxin homology #label FLX SUMMARY #length 149 #molecular-weight 16274 #checksum 2034 SEQUENCE /// ENTRY QQECG1 #type complete TITLE hypothetical 13.7K protein (gyrB 3' region) - Escherichia coli (strain K-12) ALTERNATE_NAMES hypothetical protein b3698 ORGANISM #formal_name Escherichia coli DATE 30-Sep-1988 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS C65172; B26444 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65172 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-135 ##label BLAT !'##cross-references GB:AE000447; GB:U00096; NID:g2367266; !1PIDN:AAC76721.1; PID:g1790133; UWGP:b3698 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A93674 !$#authors Adachi, T.; Mizuuchi, M.; Robinson, E.A.; Appella, E.; !1O'Dea, M.H.; Gellert, M.; Mizuuchi, K. !$#journal Nucleic Acids Res. (1987) 15:771-784 !$#title DNA sequence of the E. coli gyrB gene: application of a new !1sequencing strategy. !$#cross-references MUID:87146392; PMID:3029692 !$#accession B26444 !'##molecule_type DNA !'##residues 4-135 ##label ADA !'##cross-references GB:X04341; GB:X00870; NID:g41643; PIDN:CAA27872.1; !1PID:g41647 GENETICS !$#map_position 83 min CLASSIFICATION #superfamily Escherichia coli hypothetical 13.7K protein !1(gyrB 3' region) SUMMARY #length 135 #molecular-weight 14144 #checksum 9367 SEQUENCE /// ENTRY B70075 #type complete TITLE conserved hypothetical protein yxeH - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B70075 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B70075 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-270 ##label KUN !'##cross-references GB:Z99124; GB:AL009126; NID:g2636442; !1PIDN:CAB15991.1; PID:g2636501 !'##experimental_source strain 168 GENETICS !$#gene yxeH CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum conserved !1hypothetical protein MTH1071 SUMMARY #length 270 #molecular-weight 30223 #checksum 9698 SEQUENCE /// ENTRY C69009 #type complete TITLE conserved hypothetical protein MTH1071 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69009 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession C69009 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-221 ##label MTH !'##cross-references GB:AE000877; GB:AE000666; NID:g2622157; !1PIDN:AAB85560.1; PID:g2622169 !'##experimental_source strain Delta H GENETICS !$#gene MTH1071 CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum conserved !1hypothetical protein MTH1071 SUMMARY #length 221 #molecular-weight 23785 #checksum 9844 SEQUENCE /// ENTRY D69305 #type complete TITLE conserved hypothetical protein AF0444 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69305 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession D69305 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-223 ##label KLE !'##cross-references GB:AE001074; GB:AE000782; NID:g2689397; !1PIDN:AAB90791.1; PID:g2650184; TIGR:AF0444 CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum conserved !1hypothetical protein MTH1071 SUMMARY #length 223 #molecular-weight 24481 #checksum 4435 SEQUENCE /// ENTRY G71015 #type complete TITLE hypothetical protein PH1421 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G71015 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession G71015 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-231 ##label KAW !'##cross-references GB:AP000006; NID:g3236133; PIDN:BAA30527.1; !1PID:g3257844 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1421 CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum conserved !1hypothetical protein MTH1071 SUMMARY #length 231 #molecular-weight 25605 #checksum 8024 SEQUENCE /// ENTRY Q4ECGG #type complete TITLE hypothetical 10.7K protein in glpD-glgP intergenic region - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS F65138; JT0477 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65138 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-97 ##label BLAT !'##cross-references GB:AE000419; GB:U00096; NID:g2367227; !1PIDN:AAC76452.1; PID:g1789834; UWGP:b3427 !'##experimental_source strain K-12, substrain MG1655 REFERENCE JT0476 !$#authors Choi, Y.L.; Kawase, S.; Kawamukai, M.; Utsumi, R.; Sakai, !1H.; Komano, T. !$#journal Agric. Biol. Chem. (1989) 53:1135-1143 !$#title Nucleotide sequence of the glycerol-3-phosphate !1dehydrogenase gene of Escherichia coli and regulation by the !1cAMP-CRP complex. !$#accession JT0477 !'##molecule_type DNA !'##residues 5-67,'R',69-97 ##label CHO GENETICS !$#gene yzgL !$#map_position 75 min CLASSIFICATION #superfamily Escherichia coli hypothetical 10.7K protein !1(glpD-glgP intergenic region) SUMMARY #length 97 #molecular-weight 10659 #checksum 8020 SEQUENCE /// ENTRY Q3ECTR #type complete TITLE hypothetical 20.6K protein (tdcR-rnpB intergenic region) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS E65101; JU0025; S05360 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65101 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-186 ##label BLAT !'##cross-references GB:AE000393; GB:U00096; NID:g1789499; !1PIDN:AAC76155.1; PID:g1789508; UWGP:b3120 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A93688 !$#authors Schweizer, H.P.; Datta, P. !$#journal Nucleic Acids Res. (1989) 17:3994 !$#title The complete nucleotide sequence of the tdc region of !1Escherichia coli. !$#cross-references MUID:89282418; PMID:2660107 !$#accession JU0025 !'##molecule_type DNA !'##residues 8-186 ##label SCH1 !'##cross-references GB:X14430; NID:g43038; PIDN:CAA32590.1; PID:g43040 REFERENCE S05359 !$#authors Schweizer, H.P.; Datta, P. !$#journal Mol. Gen. Genet. (1989) 218:516-522 !$#title Identification and DNA sequence of tdcR, a positive !1regulatory gene of the tdc operon of Escherichia coli. !$#cross-references MUID:90066355; PMID:2573820 !$#accession S05360 !'##molecule_type DNA !'##residues 8-186 ##label SCH2 !'##cross-references EMBL:X16445; NID:g43034; PIDN:CAA34465.1; !1PID:g43036 GENETICS !$#gene yhaB !$#map_position 67 min CLASSIFICATION #superfamily Escherichia coli hypothetical 20.6K protein !1(tdcR-rnpB intergenic region) SUMMARY #length 186 #molecular-weight 21382 #checksum 9267 SEQUENCE /// ENTRY QQECO3 #type complete TITLE hypothetical 49.6K protein (asnA 3' region) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 17-May-1985 #sequence_revision 30-Sep-1997 #text_change 01-Mar-2002 ACCESSIONS B65178; A04443 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65178 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-427 ##label BLAT !'##cross-references GB:AE000451; GB:U00096; NID:g2367272; !1PIDN:AAC76768.1; PID:g2367274; UWGP:b3745 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A91504 !$#authors Buhk, H.J.; Messer, W. !$#journal Gene (1983) 24:265-279 !$#title The replication origin region of Escherichia coli: !1nucleotide sequence and functional units. !$#cross-references MUID:84059088; PMID:6357950 !$#accession A04443 !'##molecule_type DNA !'##residues 128-427 ##label BUH GENETICS !$#map_position 84 min CLASSIFICATION #superfamily Escherichia coli hypothetical 49.6K protein !1(asnA 3' region) SUMMARY #length 427 #molecular-weight 49625 #checksum 4786 SEQUENCE /// ENTRY BVECCT #type complete TITLE inner membrane protein creD - Escherichia coli (strain K-12) ALTERNATE_NAMES creD protein ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 01-Mar-2002 ACCESSIONS D25038; S03765; A92515; S56624; G65255; B22277 REFERENCE A25038 !$#authors Amemura, M.; Makino, K.; Shinagawa, H.; Nakata, A. !$#journal J. Bacteriol. (1986) 168:294-302 !$#title Nucleotide sequence of the phoM region of Escherichia coli: !1four open reading frames may constitute an operon. !$#cross-references MUID:87008393; PMID:3531171 !$#accession D25038 !'##molecule_type DNA !'##residues 1-450 ##label AME !'##cross-references EMBL:M13608; NID:g147248; PIDN:AAA24376.1; !1PID:g147252 REFERENCE S03764 !$#authors Drury, L.S.; Buxton, R.S. !$#journal Mol. Microbiol. (1988) 2:109-119 !$#title Identification and sequencing of the Escherichia coli cet !1gene which codes for an inner membrane protein, mutation of !1which causes tolerance to colicin E2. !$#cross-references MUID:88216172; PMID:2835585 !$#accession S03765 !'##molecule_type DNA !'##residues 1-450 ##label DRU !'##cross-references EMBL:Y00538; NID:g41102; PIDN:CAA68602.1; !1PID:g41104 REFERENCE A92515 !$#authors Drury, L.S.; Buxton, R.S. !$#journal J. Biol. Chem. (1985) 260:4236-4242 !$#title DNA sequence analysis of the dye gene of Escherichia coli !1reveals amino acid homology between the dye and ompR !1proteins. !$#cross-references MUID:85157583; PMID:2984198 !$#accession A92515 !'##molecule_type DNA !'##residues 254-450 ##label DR2 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56624 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-450 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97296.1; !1PID:g537240 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65255 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-450 ##label BLAT !'##cross-references GB:AE000510; GB:U00096; NID:g1790858; !1PIDN:AAC77353.1; PID:g1790862; UWGP:b4400 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene creD; cet !$#map_position 100 min CLASSIFICATION #superfamily cet protein KEYWORDS membrane protein SUMMARY #length 450 #molecular-weight 49829 #checksum 9859 SEQUENCE /// ENTRY WMECN5 #type complete TITLE nus operon 15K protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 17-May-1985 #sequence_revision 14-Nov-1997 #text_change 01-Mar-2002 ACCESSIONS F65107; A04472 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65107 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-152 ##label BLAT !'##cross-references GB:AE000397; GB:U00096; NID:g2367199; !1PIDN:AAC76204.1; PID:g1789561; UWGP:b3170 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A93514 !$#authors Ishii, S.; Ihara, M.; Maekawa, T.; Nakamura, Y.; Uchida, H.; !1Imamoto, F. !$#journal Nucleic Acids Res. (1984) 12:3333-3342 !$#title The nucleotide sequence of the cloned nusA gene and its !1flanking region of Escherichia coli. !$#cross-references MUID:84193200; PMID:6326058 !$#accession A04472 !'##molecule_type DNA !'##residues 13-152 ##label ISH !'##cross-references GB:X00513; GB:K01175; NID:g42142; PIDN:CAA25199.1; !1PID:g42143 GENETICS !$#gene yhbC !$#map_position 69 min CLASSIFICATION #superfamily nus operon 15K protein SUMMARY #length 152 #molecular-weight 16821 #checksum 8251 SEQUENCE /// ENTRY Q5ECRS #type complete TITLE hypothetical 6K protein (rts 5' region) - Escherichia coli ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 26-Aug-1999 ACCESSIONS JV0017 REFERENCE A91599 !$#authors Flamm, J.A.; Friesen, J.D.; Otsuka, A.J. !$#journal Gene (1988) 74:555-558 !$#title The nucleotide sequence of the Escherichia coli rts gene. !$#cross-references MUID:89232747; PMID:3073109 !$#accession JV0017 !'##molecule_type DNA !'##residues 1-53 ##label FLA GENETICS !$#map_position 88.5 min !$#start_codon GTG CLASSIFICATION #superfamily Escherichia coli hypothetical 6K protein (rts !15' region) SUMMARY #length 53 #molecular-weight 6190 #checksum 466 SEQUENCE /// ENTRY Q3ECE4 #type complete TITLE hypothetical 14.4K protein (rrfE-metA intergenic region) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 01-Mar-2002 ACCESSIONS A24340; B65208 REFERENCE A93580 !$#authors Liebke, H.; Hatfull, G. !$#journal Nucleic Acids Res. (1985) 13:5515-5525 !$#title The sequence of the distal end of the E. coli ribosomal RNA !1rrnE operon indicates conserved features are shared by rrn !1operons. !$#cross-references MUID:85297755; PMID:2412207 !$#accession A24340 !'##molecule_type DNA !'##residues 1-127 ##label LIE !'##cross-references GB:X02800; NID:g42882; PIDN:CAA26569.1; PID:g42883 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65208 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-127 ##label BLAT !'##cross-references GB:AE000474; GB:U00096; NID:g1790440; !1PIDN:AAC76981.1; PID:g1790441; UWGP:b4011 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yjaA !$#map_position 90 min CLASSIFICATION #superfamily Escherichia coli hypothetical 14.4K protein !1(rrfE-metA intergenic region) SUMMARY #length 127 #molecular-weight 14447 #checksum 8429 SEQUENCE /// ENTRY Q3ECE6 #type complete TITLE hypothetical 16.4K protein rrfE-metA intergenic region - Escherichia coli (strain K-12) ALTERNATE_NAMES hypothetical protein witA 5'-region; hypothetical protein yjaB ORGANISM #formal_name Escherichia coli DATE 30-Jun-1989 #sequence_revision 30-Jun-1989 #text_change 01-Mar-2002 ACCESSIONS B24340; C65208; S15705 REFERENCE A93580 !$#authors Liebke, H.; Hatfull, G. !$#journal Nucleic Acids Res. (1985) 13:5515-5525 !$#title The sequence of the distal end of the E. coli ribosomal RNA !1rrnE operon indicates conserved features are shared by rrn !1operons. !$#cross-references MUID:85297755; PMID:2412207 !$#accession B24340 !'##molecule_type DNA !'##residues 1-147 ##label LBK !'##cross-references GB:X02800; NID:g42882; PIDN:CAA26570.1; PID:g42884 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65208 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-147 ##label BLAT !'##cross-references GB:AE000474; GB:U00096; NID:g1790440; !1PIDN:AAC76982.1; PID:g1790442; UWGP:b4012 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S15705 !$#authors Albrechtsen, B.; Ross, B.M.; Squires, C.; Squires, C.L. !$#journal Nucleic Acids Res. (1991) 19:1845-1852 !$#title Transcriptional termination sequence at the end of the !1Escherichia coli ribosomal RNA G operon: complex terminators !1and antitermination. !$#cross-references MUID:91232952; PMID:1709493 !$#accession S15705 !'##molecule_type DNA !'##residues 'M',129-130,'GK',133-146,'V' ##label ALB !'##cross-references EMBL:X56780; NID:g42887; PIDN:CAA40098.1; !1PID:g42888 GENETICS !$#gene yjaB !$#map_position 90 min CLASSIFICATION #superfamily Escherichia coli hypothetical 16.4K protein !1(rrfE-metA intergenic region) SUMMARY #length 147 #molecular-weight 16447 #checksum 5144 SEQUENCE /// ENTRY QQECX3 #type complete TITLE Putative methylase yhhF (EC 2.1.1.-) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 01-Mar-2002 ACCESSIONS S03129; S47684; D65143 REFERENCE S03129 !$#authors Gill, D.R.; Hatfull, G.F.; Salmond, G.P.C. !$#journal Mol. Gen. Genet. (1986) 205:134-145 !$#title A new cell division operon in Escherichia coli. !$#cross-references MUID:87089083; PMID:3025556 !$#accession S03129 !'##molecule_type DNA !'##residues 1-198 ##label GIL !'##cross-references EMBL:X04398; NID:g41496; PIDN:CAA27983.1; !1PID:g41497 REFERENCE S47666 !$#authors Plunkett, G. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S47684 !'##molecule_type DNA !'##residues 1-198 ##label PLU !'##cross-references EMBL:U00039; NID:g466582; PIDN:AAB18440.1; !1PID:g466601 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65143 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-198 ##label BLAT !'##cross-references GB:AE000422; GB:U00096; NID:g1789868; !1PIDN:AAC76490.1; PID:g1789875; UWGP:b3465 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yhhF !$#map_position 76 min CLASSIFICATION #superfamily Escherichia coli hypothetical 21.7K protein !1(ftsY-nikA intergenic region) KEYWORDS methyltransferase SUMMARY #length 198 #molecular-weight 21677 #checksum 7157 SEQUENCE /// ENTRY Q3ECS7 #type complete TITLE hypothetical 77K protein (spoT 3' region) - Escherichia coli ORGANISM #formal_name Escherichia coli DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 26-Aug-1999 ACCESSIONS A30374; Q90796 REFERENCE A30374 !$#authors Sarubbi, E.; Rudd, K.E.; Xiao, H.; Ikehara, K.; Kalman, M.; !1Cashel, M. !$#journal J. Biol. Chem. (1989) 264:15074-15082 !$#title Characterization of the spoT gene of Escherichia coli. !$#cross-references MUID:89359321; PMID:2549050 !$#accession A30374 !'##molecule_type DNA !'##residues 1-685 ##label SAR GENETICS !$#map_position 82 min CLASSIFICATION #superfamily Escherichia coli hypothetical 77K protein (spoT !13' region) SUMMARY #length 685 #molecular-weight 77226 #checksum 3704 SEQUENCE /// ENTRY QQECZG #type complete TITLE ybaB protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 01-Mar-2002 ACCESSIONS A30371; C25549; F64777; Q00815 REFERENCE A30371 !$#authors Mahdi, A.A.; Lloyd, R.G. !$#journal Nucleic Acids Res. (1989) 17:6781-6794 !$#title The recR locus of Escherichia coli K-12: molecular cloning, !1DNA sequencing and identification of the gene product. !$#cross-references MUID:89386036; PMID:2674903 !$#accession A30371 !'##molecule_type DNA !'##residues 1-109 ##label MAH !'##cross-references GB:M38777; NID:g145295; PIDN:AAA23458.1; !1PID:g145298 REFERENCE A25549 !$#authors Flower, A.M.; McHenry, C.S. !$#journal Nucleic Acids Res. (1986) 14:8091-8101 !$#title The adjacent dnaZ and dnaX genes of Escherichia coli are !1contained within one continuous open reading frame. !$#cross-references MUID:87040775; PMID:3534795 !$#accession C25549 !'##molecule_type DNA !'##residues 1-75 ##label FLO !'##cross-references GB:X04487; NID:g43319; PIDN:CAA28176.1; PID:g43322 !'##experimental_source strain K-12, substrain JM109 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64777 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-109 ##label BLAT !'##cross-references GB:AE000153; GB:U00096; NID:g1786671; !1PIDN:AAC73573.1; PID:g1786677; UWGP:b0471 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ybaB !$#map_position 11 min CLASSIFICATION #superfamily Escherichia coli ybaB protein SUMMARY #length 109 #molecular-weight 12015 #checksum 8633 SEQUENCE /// ENTRY IEECC7 #type complete TITLE hypothetical protein, 8K - Escherichia coli insertion sequence IS1 ORGANISM #formal_name Escherichia coli DATE 24-Sep-1981 #sequence_revision 15-Oct-1982 #text_change 16-Jun-2000 ACCESSIONS A93826; A93117; S40546; A04452 REFERENCE A93826 !$#authors Ohtsubo, H.; Ohtsubo, E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1978) 75:615-619 !$#title Nucleotide sequence of an insertion element, IS1. !$#cross-references MUID:78137003; PMID:273224 !$#accession A93826 !'##molecule_type DNA !'##residues 1-70 ##label OHT !'##cross-references GB:D10483; GB:J01597; GB:J01683; GB:J01706; !1GB:K01298; GB:K01990; GB:M10420; GB:M10611; GB:M12544; !1NID:g216434; PIDN:BAA01301.1; PID:g285762 !'##experimental_source strain K-12 REFERENCE A93117 !$#authors Johnsrud, L. !$#journal Mol. Gen. Genet. (1979) 169:213-218 !$#title DNA sequence of the transposable element IS1. !$#cross-references MUID:79177885; PMID:375010 !$#accession A93117 !'##molecule_type DNA !'##residues 1-70 ##label JOH !'##cross-references GB:D10483; GB:J01597; GB:J01683; GB:J01706; !1GB:K01298; GB:K01990; GB:M10420; GB:M10611; GB:M12544; !1NID:g216434; PIDN:BAA01301.1; PID:g285762 !'##experimental_source strain K-12 REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40546 !'##molecule_type DNA !'##residues 'V',2-70 ##label YUR !'##cross-references EMBL:D10483 !'##experimental_source strain K-12 GENETICS !$#mobile_element insertion sequence IS1 !$#start_codon GTG CLASSIFICATION #superfamily Escherichia coli insertion sequence IS1 !1hypothetical 7.6K protein SUMMARY #length 70 #molecular-weight 7633 #checksum 3823 SEQUENCE /// ENTRY QQECSY #type complete TITLE preprotein translocase secY [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 01-Mar-2002 ACCESSIONS A04473; G65122 REFERENCE A02714 !$#authors Cerretti, D.P.; Dean, D.; Davis, G.R.; Bedwell, D.M.; !1Nomura, M. !$#journal Nucleic Acids Res. (1983) 11:2599-2616 !$#title The spc ribosomal protein operon of Escherichia coli: !1sequence and cotranscription of the ribosomal protein genes !1and a protein export gene. !$#cross-references MUID:83220807; PMID:6222285 !$#accession A04473 !'##molecule_type DNA !'##residues 1-443 ##label CER !'##cross-references GB:X01563; NID:g42977; PIDN:CAA25725.1; PID:g42989 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65122 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-443 ##label BLAT !'##cross-references GB:AE000408; GB:U00096; NID:g1789694; !1PIDN:AAC76325.1; PID:g1789696; UWGP:b3300 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene secY; prlA !$#map_position 73 min FUNCTION !$#description essential for preprotein translocation across the !1cytoplasmic membrane [validated, MUID:84182537] CLASSIFICATION #superfamily preprotein translocase secY KEYWORDS protein transport; transmembrane protein FEATURE !$1-21 #domain intracellular #status predicted #label INT1\ !$22-43 #domain transmembrane #status predicted #label TM01\ !$44-77 #domain extracellular #status predicted #label EXT1\ !$78-98 #domain transmembrane #status predicted #label TM02\ !$99-120 #domain intracellular #status predicted #label INT2\ !$121-138 #domain transmembrane #status predicted #label TM03\ !$139-157 #domain extracellular #status predicted #label EXT2\ !$158-175 #domain transmembrane #status predicted #label TM04\ !$176-183 #domain intracellular #status predicted #label INT3\ !$184-205 #domain transmembrane #status predicted #label TM05\ !$206-214 #domain extracellular #status predicted #label EXT3\ !$215-238 #domain transmembrane #status predicted #label TM06\ !$239-270 #domain intracellular #status predicted #label INT4\ !$271-292 #domain transmembrane #status predicted #label TM07\ !$293-314 #domain extracellular #status predicted #label EXT4\ !$315-336 #domain transmembrane #status predicted #label TM08\ !$337-371 #domain intracellular #status predicted #label INT5\ !$372-391 #domain transmembrane #status predicted #label TM09\ !$392-395 #domain extracellular #status predicted #label EXT5\ !$396-419 #domain transmembrane #status predicted #label TM10\ !$420-443 #domain intracellular #status predicted #label INT6 SUMMARY #length 443 #molecular-weight 48511 #checksum 6428 SEQUENCE /// ENTRY BWBSSY #type complete TITLE preprotein translocase secY - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 16-Jun-2000 ACCESSIONS S08629; JX0114; S12683; S15062; A69705 REFERENCE S08628 !$#authors Suh, J.W.; Boylan, S.A.; Thomas, S.M.; Dolan, K.M.; Oliver, !1D.B.; Price, C.W. !$#journal Mol. Microbiol. (1990) 4:305-314 !$#title Isolation of a secY homologue from Bacillus subtilis: !1evidence for a common protein export pathway in eubacteria. !$#cross-references MUID:90251170; PMID:2110998 !$#accession S08629 !'##molecule_type DNA !'##residues 1-431 ##label SUH !'##cross-references EMBL:X51329; NID:g40132; PIDN:CAA35712.1; !1PID:g580926 REFERENCE JS0490 !$#authors Nakamura, K.; Nakamura, A.; Takamatsu, H.; Yoshikawa, H.; !1Yamane, K. !$#journal J. Biochem. (1990) 107:603-607 !$#title Cloning and characterization of a Bacillus subtilis gene !1homologous to E. coli secY. !$#cross-references MUID:90292990; PMID:2113521 !$#accession JX0114 !'##molecule_type DNA !'##residues 9-431 ##label NAK !'##cross-references GB:D00619; NID:g216336; PIDN:BAA00495.1; !1PID:g216339 REFERENCE S12680 !$#authors Yoshikawa, H.; Doi, R.H. !$#journal Nucleic Acids Res. (1990) 18:1647 !$#title Sequence of the Bacillus subtilis spectinomycin resistance !1gene region. !$#cross-references MUID:90221911; PMID:2139212 !$#accession S12683 !'##molecule_type DNA !'##residues 1-431 ##label YOS !'##cross-references EMBL:M31102; NID:g1184272; PIDN:AAB59118.1; !1PID:g1184273 !'##note the authors translated the initiation codon TTG for residue 1 !1as Leu REFERENCE S15062 !$#authors Yoshikawa, H.; Doi, R.H. !$#submission submitted to the EMBL Data Library, January 1990 !$#description The nucleotide sequence of the Bacillus subtilis !1spectinomycin resistance gene region. !$#accession S15062 !'##molecule_type DNA !'##residues 1-235,'R',257-431 ##label EMB !'##cross-references EMBL:M31102 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69705 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-431 ##label KUN !'##cross-references GB:Z99104; GB:AL009126; NID:g2632267; !1PIDN:CAB11912.1; PID:g2632403 !'##experimental_source strain 168 COMMENT This protein is involved in protein export. GENETICS !$#gene secY !$#start_codon TTG CLASSIFICATION #superfamily preprotein translocase secY KEYWORDS protein transport; transmembrane protein FEATURE !$1-17 #domain intracellular #status predicted #label INT1\ !$18-39 #domain transmembrane #status predicted #label TM01\ !$59-80 #domain transmembrane #status predicted #label TM02\ !$115-132 #domain transmembrane #status predicted #label TM03\ !$149-167 #domain transmembrane #status predicted #label TM04\ !$174-192 #domain transmembrane #status predicted #label TM05\ !$217-234 #domain transmembrane #status predicted #label TM06\ !$268-284 #domain transmembrane #status predicted #label TM07\ !$310-326 #domain transmembrane #status predicted #label TM08\ !$367-385 #domain transmembrane #status predicted #label TM09\ !$388-410 #domain transmembrane #status predicted #label TM10\ !$411-431 #domain intracellular #status predicted #label INT2 SUMMARY #length 431 #molecular-weight 47243 #checksum 3098 SEQUENCE /// ENTRY S17985 #type complete TITLE preprotein translocase secY - Lactococcus lactis subsp. lactis ORGANISM #formal_name Lactococcus lactis subsp. lactis #variety strain MG1614 DATE 30-Jun-1993 #sequence_revision 30-Jun-1993 #text_change 23-Jul-1999 ACCESSIONS S17985; A44812 REFERENCE S17985 !$#authors Koivula, T.; Palva, I.; Hemilae, H. !$#journal FEBS Lett. (1991) 288:114-118 !$#title Nucleotide sequence of the secY gene from Lactococcus lactis !1and identification of conserved regions by comparison of !1four SecY proteins. !$#cross-references MUID:91348245; PMID:1908794 !$#accession S17985 !'##molecule_type DNA !'##residues 1-439 ##label KOI !'##cross-references EMBL:X59250; NID:g44071; PIDN:CAA41939.1; !1PID:g44073 REFERENCE A44812 !$#authors Koivula, T.; Hemila, H. !$#journal J. Gen. Microbiol. (1991) 137:2595-2600 !$#title Nucleotide sequence of a Lactococcus lactis gene cluster !1encoding adenylate kinase, initiation factor 1 and ribosomal !1proteins. !$#cross-references MUID:92148378; PMID:1783905 !$#accession A44812 !'##molecule_type DNA !'##residues 422-439 ##label KO2 !'##note sequence extracted from NCBI backbone (NCBIN:81088, !1NCBIP:81089) GENETICS !$#gene secY FUNCTION !$#description involved in protein export CLASSIFICATION #superfamily preprotein translocase secY KEYWORDS protein transport; transmembrane protein FEATURE !$1-18 #domain intracellular #status predicted #label INT1\ !$19-40 #domain transmembrane #status predicted #label TM01\ !$60-81 #domain transmembrane #status predicted #label TM02\ !$116-133 #domain transmembrane #status predicted #label TM03\ !$150-168 #domain transmembrane #status predicted #label TM04\ !$175-193 #domain transmembrane #status predicted #label TM05\ !$219-236 #domain transmembrane #status predicted #label TM06\ !$266-289 #domain transmembrane #status predicted #label TM07\ !$312-332 #domain transmembrane #status predicted #label TM08\ !$370-388 #domain transmembrane #status predicted #label TM09\ !$391-413 #domain transmembrane #status predicted #label TM10\ !$414-439 #domain intracellular #status predicted #label INT2 SUMMARY #length 439 #molecular-weight 48438 #checksum 4841 SEQUENCE /// ENTRY BWYMSY #type complete TITLE preprotein translocase secY - Mycoplasma capricolum ORGANISM #formal_name Mycoplasma capricolum DATE 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 07-Dec-1999 ACCESSIONS S02850 REFERENCE S02830 !$#authors Ohkubo, S.; Muto, A.; Kawauchi, Y.; Yamao, F.; Osawa, S. !$#journal Mol. Gen. Genet. (1987) 210:314-322 !$#title The ribosomal protein gene cluster of Mycoplasma capricolum. !$#cross-references MUID:88142549; PMID:3481422 !$#accession S02850 !'##molecule_type DNA !'##residues 1-482 ##label OHK !'##cross-references EMBL:X06414; NID:g44207; PIDN:CAA29723.1; !1PID:g44228 COMMENT This protein is involved in protein export. GENETICS !$#gene secY !$#genetic_code SGC3 CLASSIFICATION #superfamily preprotein translocase secY KEYWORDS protein transport; transmembrane protein FEATURE !$1-40 #domain intracellular #status predicted #label INT1\ !$41-64 #domain transmembrane #status predicted #label TM01\ !$92-112 #domain transmembrane #status predicted #label TM02\ !$140-157 #domain transmembrane #status predicted #label TM03\ !$179-198 #domain transmembrane #status predicted #label TM04\ !$205-223 #domain transmembrane #status predicted #label TM05\ !$248-265 #domain transmembrane #status predicted #label TM06\ !$301-319 #domain transmembrane #status predicted #label TM07\ !$346-362 #domain transmembrane #status predicted #label TM08\ !$403-421 #domain transmembrane #status predicted #label TM09\ !$427-446 #domain transmembrane #status predicted #label TM10\ !$450-482 #domain intracellular #status predicted #label INT2 SUMMARY #length 482 #molecular-weight 53300 #checksum 755 SEQUENCE /// ENTRY IEECB9 #type complete TITLE insA protein - Escherichia coli (strain K-12) insertion sequence IS1 ORGANISM #formal_name Escherichia coli DATE 24-Sep-1981 #sequence_revision 15-Oct-1982 #text_change 01-Mar-2002 ACCESSIONS B93826; B93117; JN0136; JN0138; I41088; I41307; I56386; !1A64752; C64753; S40545; A04453; S10441; S10442 REFERENCE A93826 !$#authors Ohtsubo, H.; Ohtsubo, E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1978) 75:615-619 !$#title Nucleotide sequence of an insertion element, IS1. !$#cross-references MUID:78137003; PMID:273224 !$#accession B93826 !'##molecule_type DNA !'##residues 1-91 ##label OHT !'##cross-references GB:J01730; NID:g151742; PIDN:AAA92258.1; !1PID:g294459 !'##experimental_source insertion sequence IS1 REFERENCE A93117 !$#authors Johnsrud, L. !$#journal Mol. Gen. Genet. (1979) 169:213-218 !$#title DNA sequence of the transposable element IS1. !$#cross-references MUID:79177885; PMID:375010 !$#accession B93117 !'##molecule_type DNA !'##residues 1-80,'L',82-91 ##label JOH !'##cross-references GB:D10483; GB:J01597; GB:J01683; GB:J01706; !1GB:K01298; GB:K01990; GB:M10420; GB:M10611; GB:M12544; !1GB:V00259; GB:X04711; GB:X54847; GB:X54945; GB:X55034; !1GB:X56742; NID:g216434; PIDN:BAA01300.1; PID:g285761 !'##experimental_source insertion sequence IS1 REFERENCE JN0134 !$#authors Umeda, M.; Ohtsubo, E. !$#journal Gene (1991) 98:1-5 !$#title Four types of IS1 with differences in nucleotide sequence !1reside in the Escherichia coli K-12 chromosome. !$#cross-references MUID:91192599; PMID:1849492 !$#accession JN0136 !'##molecule_type DNA !'##residues 1-91 ##label UME1 !'##cross-references EMBL:X52535; NID:g41818; PIDN:CAA36771.1; !1PID:g581114 !'##experimental_source strain K12, substrain W3110, insertion sequence !1IS1C !'##note the authors translated the initiation codon GTG for residue 1 !1as Val !'##note this protein is coded by insertion sequence IS1C !$#accession JN0138 !'##molecule_type DNA !'##residues 1-91 ##label UME2 !'##cross-references EMBL:X52536; NID:g41820; PIDN:CAA36772.1; !1PID:g581115 !'##experimental_source strain K12, substrain W3110, insertion sequence !1IS1D !'##note the authors translated the initiation codon GTG for residue 1 !1as Val !'##note this protein is coded by insertion sequence IS1D REFERENCE I41088 !$#authors Umeda, M.; Ohtsubo, E. !$#journal Mol. Gen. Genet. (1990) 222:317-322 !$#title Mapping of insertion element IS30 in the Escherichia coli !1K12 chromosome. !$#cross-references MUID:91109718; PMID:1980336 !$#accession I41088 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-91 ##label RES !'##cross-references EMBL:X17345; NID:g41814; PIDN:CAA35227.1; !1PID:g581113 !'##experimental_source strain K12, substrain W3110; insertion sequence !1IS1B REFERENCE I41306 !$#authors Volkert, M.R.; Loewen, P.C.; Switala, J.; Crowley, D.; !1Conley, M. !$#journal J. Bacteriol. (1994) 176:1297-1302 !$#title The delta (argF-lacZ)205(U169) deletion greatly enhances !1resistance to hydrogen peroxide in stationary-phase !1Escherichia coli. !$#cross-references MUID:94156832; PMID:8113168 !$#accession I41307 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-91 ##label RE2 !'##cross-references GB:L20943; NID:g304899; PIDN:AAA69642.1; !1PID:g304901 !'##experimental_source insertion sequence IS1B REFERENCE I56386 !$#authors Machida, Y.; Machida, C.; Ohtsubo, E. !$#journal J. Mol. Biol. (1984) 177:229-245 !$#title Insertion element IS1 encodes two structural genes required !1for its transposition. !$#cross-references MUID:84267874; PMID:6086942 !$#accession I56386 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 41-91 ##label RE3 !'##cross-references GB:M28607; NID:g294460; PIDN:AAA26062.1; !1PID:g294461 !'##experimental_source insertion sequence IS1 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64752 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-91 ##label BLAT !'##cross-references GB:AE000134; GB:U00096; NID:g1786454; !1PIDN:AAC73368.1; PID:g1786460; UWGP:b0265 !'##experimental_source strain K-12, substrain MG1655, insertion !1sequence IS1 !'##genetics IA2 !$#accession C64753 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-91 ##label BLA2 !'##cross-references GB:AE000135; GB:U00096; NID:g1786465; !1PIDN:AAC73378.1; PID:g1786471; UWGP:b0275 !'##experimental_source strain K-12, substrain MG1655, insertion !1sequence IS1 !'##genetics IA3 REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40545 !'##status preliminary !'##molecule_type DNA !'##residues 1-80,'L',82-91 ##label YUR !'##cross-references EMBL:D10483; NID:g216434; PIDN:BAA01300.1; !1PID:g285761 !'##experimental_source strain K-12; insertion sequence IS1 GENETICS IA2 !$#gene insA_2 !$#mobile_element insertion sequence IS1 GENETICS IA3 !$#gene insA_3 !$#mobile_element insertion sequence IS1 !$#start_codon GTG FUNCTION !$#description required for transposition of insertion sequence IS1 CLASSIFICATION #superfamily insA protein KEYWORDS nucleotide binding; P-loop FEATURE !$16-23 #region nucleotide-binding motif A (P-loop) SUMMARY #length 91 #molecular-weight 9902 #checksum 4217 SEQUENCE /// ENTRY IEEBB1 #type complete TITLE insA protein homolog B-91 - Shigella dysenteriae insertion sequence IS1-D ORGANISM #formal_name Shigella dysenteriae DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 28-May-1999 ACCESSIONS B04602; A04453 REFERENCE A04602 !$#authors Ohtsubo, H.; Nyman, K.; Doroszkiewicz, W.; Ohtsubo, E. !$#journal Nature (1981) 292:640-643 !$#title Multiple copies of iso-insertion sequences of IS1 in !1Shigella dysenteriae chromosome. !$#cross-references MUID:81245267; PMID:6265806 !$#accession B04602 !'##molecule_type DNA !'##residues 1-91 ##label OHT !'##cross-references GB:J01731; NID:g149065; PIDN:AAA96230.1; !1PID:g149066 COMMENT This protein is coded by IS1-D, an iso-insertion sequence of !1IS1. GENETICS !$#mobile_element insertion sequence IS1-D !$#start_codon GTG CLASSIFICATION #superfamily insA protein KEYWORDS nucleotide binding; P-loop FEATURE !$16-23 #region nucleotide-binding motif A (P-loop) SUMMARY #length 91 #molecular-weight 9898 #checksum 4589 SEQUENCE /// ENTRY IEEBB9 #type complete TITLE insA protein - Shigella dysenteriae insertion sequence IS1-N ORGANISM #formal_name Shigella dysenteriae DATE 02-Apr-1982 #sequence_revision 02-Apr-1982 #text_change 28-May-1999 ACCESSIONS A04454 REFERENCE A04602 !$#authors Ohtsubo, H.; Nyman, K.; Doroszkiewicz, W.; Ohtsubo, E. !$#journal Nature (1981) 292:640-643 !$#title Multiple copies of iso-insertion sequences of IS1 in !1Shigella dysenteriae chromosome. !$#cross-references MUID:81245267; PMID:6265806 !$#accession A04454 !'##molecule_type DNA !'##residues 1-90 ##label OHT !'##cross-references GB:J01737; NID:g149062; PIDN:AAA25031.1; !1PID:g149063 COMMENT This protein is coded by IS1-N, an iso-insertion sequence of !1IS1. GENETICS !$#gene insA !$#mobile_element insertion sequence IS1-N CLASSIFICATION #superfamily insA protein SUMMARY #length 90 #molecular-weight 10348 #checksum 9829 SEQUENCE /// ENTRY IEECA1 #type complete TITLE insB protein - Escherichia coli (strain K-12) insertion sequence IS1 CONTAINS insB protein ORGANISM #formal_name Escherichia coli DATE 24-Sep-1981 #sequence_revision 30-Jan-1998 #text_change 01-Mar-2002 ACCESSIONS JN0137; JN0139; I41308; B64753; H64751; B64840; C93826; !1I73451; A04455 REFERENCE JN0134 !$#authors Umeda, M.; Ohtsubo, E. !$#journal Gene (1991) 98:1-5 !$#title Four types of IS1 with differences in nucleotide sequence !1reside in the Escherichia coli K-12 chromosome. !$#cross-references MUID:91192599; PMID:1849492 !$#accession JN0137 !'##molecule_type DNA !'##residues 1-167 ##label UME !'##cross-references EMBL:X52535; NID:g41818 !'##experimental_source strain K-12, subatrain W3110, insersion sequence !1IS1 !$#accession JN0139 !'##molecule_type DNA !'##residues 1-4,'S',6-127,'Y',129-151,'L',153-167 ##label UM2 !'##cross-references EMBL:X52536; NID:g41820 !'##experimental_source strain K-12, substrain W3110, insertion sequence !1IS1D !'##genetics IS1D REFERENCE I41306 !$#authors Volkert, M.R.; Loewen, P.C.; Switala, J.; Crowley, D.; !1Conley, M. !$#journal J. Bacteriol. (1994) 176:1297-1302 !$#title The delta (argF-lacZ)205(U169) deletion greatly enhances !1resistance to hydrogen peroxide in stationary-phase !1Escherichia coli. !$#cross-references MUID:94156832; PMID:8113168 !$#accession I41308 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-167 ##label RES !'##cross-references GB:L20943; NID:g304899; PIDN:AAA69643.1; !1PID:g304902 !'##experimental_source insertion sequence IS1B REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64753 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-167 ##label BLAT !'##cross-references GB:AE000135; GB:U00096; NID:g1786465; !1PIDN:AAC73377.1; PID:g1786470; UWGP:b0274 !'##experimental_source strain K-12, substrain MG1655, insertion !1sequence IS1 !'##genetics INS3 !$#accession H64751 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-167 ##label BLA2 !'##cross-references GB:AE000134; GB:U00096; NID:g1786454; !1PIDN:AAC73367.1; PID:g1786459; UWGP:b0264 !'##experimental_source strain K-12, substrain MG1655, insertion !1sequence IS1 !'##genetics INS2 !$#accession B64840 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-4,'S',6-127,'Y',129-151,'L',153-167 ##label BLA3 !'##cross-references GB:AE000200; GB:U00096; NID:g2367111; !1PIDN:AAC74073.1; PID:g1787223; UWGP:b0988 !'##experimental_source strain K-12, substrain MG1655, insertion !1sequence IS1D !'##genetics INS4 REFERENCE A93826 !$#authors Ohtsubo, H.; Ohtsubo, E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1978) 75:615-619 !$#title Nucleotide sequence of an insertion element, IS1. !$#cross-references MUID:78137003; PMID:273224 !$#accession C93826 !'##molecule_type DNA !'##residues 1-151,'L',153-167 ##label OHT !'##cross-references GB:V00609; NID:g43698; PIDN:CAA23879.1; PID:g673426 !'##experimental_source K-12 REFERENCE I56386 !$#authors Machida, Y.; Machida, C.; Ohtsubo, E. !$#journal J. Mol. Biol. (1984) 177:229-245 !$#title Insertion element IS1 encodes two structural genes required !1for its transposition. !$#cross-references MUID:84267874; PMID:6086942 !$#accession I73451 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 43-85,'V',87-151,'L',153-156 ##label RE2 !'##cross-references GB:M28607; NID:g294460; PIDN:AAA26063.1; !1PID:g294462 !'##experimental_source insertion sequence IS1 COMMENT This protein is coded by the insertion sequence IS1. GENETICS IN1D !$#gene insB_1D !$#mobile_element insersion sequence IS1D GENETICS INS3 !$#gene insB_3 !$#mobile_element insersion sequence IS1 GENETICS INS2 !$#gene insB_2 !$#mobile_element insersion sequence IS1 GENETICS INS4 !$#gene insB_4 !$#mobile_element insersion sequence IS1D FUNCTION !$#description required for transposition of insertion sequence IS1 CLASSIFICATION #superfamily insB protein KEYWORDS DNA recombination; transposition SUMMARY #length 167 #molecular-weight 19758 #checksum 7065 SEQUENCE /// ENTRY IEEB1D #type complete TITLE insB protein A-125 - Shigella dysenteriae insertion sequence IS1-D ORGANISM #formal_name Shigella dysenteriae DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 28-May-1999 ACCESSIONS A04602; A04455 REFERENCE A04602 !$#authors Ohtsubo, H.; Nyman, K.; Doroszkiewicz, W.; Ohtsubo, E. !$#journal Nature (1981) 292:640-643 !$#title Multiple copies of iso-insertion sequences of IS1 in !1Shigella dysenteriae chromosome. !$#cross-references MUID:81245267; PMID:6265806 !$#accession A04602 !'##molecule_type DNA !'##residues 1-125 ##label OHT !'##cross-references GB:J01731; NID:g149065; PIDN:AAA96231.1; !1PID:g149067 COMMENT This protein is coded by IS1-D, an iso-insertion sequence of !1IS1. GENETICS !$#gene insB !$#mobile_element insertion sequence IS1-D CLASSIFICATION #superfamily insB protein KEYWORDS DNA recombination; transposition SUMMARY #length 125 #molecular-weight 14999 #checksum 1588 SEQUENCE /// ENTRY IEEBC1 #type complete TITLE insB protein homolog C-131 - Shigella dysenteriae insertion sequence IS1-N ORGANISM #formal_name Shigella dysenteriae DATE 02-Apr-1982 #sequence_revision 15-Oct-1982 #text_change 28-May-1999 ACCESSIONS A04456 REFERENCE A04602 !$#authors Ohtsubo, H.; Nyman, K.; Doroszkiewicz, W.; Ohtsubo, E. !$#journal Nature (1981) 292:640-643 !$#title Multiple copies of iso-insertion sequences of IS1 in !1Shigella dysenteriae chromosome. !$#cross-references MUID:81245267; PMID:6265806 !$#accession A04456 !'##molecule_type DNA !'##residues 1-131 ##label OHT !'##cross-references GB:J01737; NID:g149062; PIDN:AAA25032.1; !1PID:g149064 !'##note this protein is coded by IS1-N, an iso-insertion sequence of !1IS1 GENETICS !$#mobile_element insertion sequence IS1-N !$#start_codon GTG CLASSIFICATION #superfamily insB protein KEYWORDS DNA recombination; transposition SUMMARY #length 131 #molecular-weight 15364 #checksum 6487 SEQUENCE /// ENTRY IEECE9 #type complete TITLE hypothetical protein, 11K - Escherichia coli insertion sequence IS1 ORGANISM #formal_name Escherichia coli DATE 24-Sep-1981 #sequence_revision 24-Sep-1981 #text_change 16-Jun-2000 ACCESSIONS D93826; D93117; S40544; A04462 REFERENCE A93826 !$#authors Ohtsubo, H.; Ohtsubo, E. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1978) 75:615-619 !$#title Nucleotide sequence of an insertion element, IS1. !$#cross-references MUID:78137003; PMID:273224 !$#accession D93826 !'##molecule_type DNA !'##residues 1-96 ##label OHT REFERENCE A93117 !$#authors Johnsrud, L. !$#journal Mol. Gen. Genet. (1979) 169:213-218 !$#title DNA sequence of the transposable element IS1. !$#cross-references MUID:79177885; PMID:375010 !$#accession D93117 !'##molecule_type DNA !'##residues 1-91,'R',93-96 ##label JOH !'##cross-references GB:D10483; GB:J01597; GB:J01683; GB:J01706; !1GB:K01298; GB:K01990; GB:M10420; GB:M10611; GB:M12544; !1NID:g216434; PIDN:BAA01299.1; PID:g216448 !'##experimental_source strain K-12 REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40544 !'##molecule_type DNA !'##residues 1-91,'R',93-96 ##label YUR !'##cross-references EMBL:D10483; NID:g216434; PIDN:BAA01299.1; !1PID:g216448 !'##experimental_source strain K-12 GENETICS !$#mobile_element insertion sequence IS1 CLASSIFICATION #superfamily Escherichia coli insertion sequence IS1 !1hypothetical 11K protein SUMMARY #length 96 #molecular-weight 10965 #checksum 9786 SEQUENCE /// ENTRY IEEC41 #type complete TITLE Transposase insG for insertion sequence element IS4 - Escherichia coli (strain K-12) insertion sequence IS4 ALTERNATE_NAMES hypothetical protein f442 ORGANISM #formal_name Escherichia coli DATE 29-Jul-1981 #sequence_revision 29-Jul-1981 #text_change 01-Mar-2002 ACCESSIONS A04463; S56503; H65240 REFERENCE A93121 !$#authors Klaer, R.; Kuhn, S.; Tillmann, E.; Fritz, H.J.; Starlinger, !1P. !$#journal Mol. Gen. Genet. (1981) 181:169-175 !$#title The sequence of IS4. !$#cross-references MUID:82012962; PMID:6268937 !$#accession A04463 !'##molecule_type DNA !'##residues 1-442 ##label KLA !'##experimental_source strain K12 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56503 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-442 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97174.1; !1PID:g537119 !'##experimental_source strain K-12 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65240 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-442 ##label BLAT !'##cross-references GB:AE000498; GB:U00096; NID:g2367368; !1PIDN:AAC77234.1; PID:g1790729; UWGP:b4278 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yi41 !$#mobile_element insertion sequence IS4 CLASSIFICATION #superfamily Escherichia coli insertion sequence IS4 !1hypothetical protein yi41 SUMMARY #length 442 #molecular-weight 50385 #checksum 4161 SEQUENCE /// ENTRY IEEC42 #type complete TITLE hypothetical protein 2 - Escherichia coli insertion sequence IS4 ORGANISM #formal_name Escherichia coli DATE 29-Jul-1981 #sequence_revision 29-Jul-1981 #text_change 10-Sep-1999 ACCESSIONS A04464 REFERENCE A93121 !$#authors Klaer, R.; Kuhn, S.; Tillmann, E.; Fritz, H.J.; Starlinger, !1P. !$#journal Mol. Gen. Genet. (1981) 181:169-175 !$#title The sequence of IS4. !$#cross-references MUID:82012962; PMID:6268937 !$#accession A04464 !'##molecule_type DNA !'##residues 1-131 ##label KLA !'##experimental_source strain K12 GENETICS !$#mobile_element insertion sequence IS4 CLASSIFICATION #superfamily Escherichia coli insertion sequence IS4 !1hypothetical 14.4K protein SUMMARY #length 131 #molecular-weight 14446 #checksum 49 SEQUENCE /// ENTRY IEEC5D #type complete TITLE probable transposase, 39K - Escherichia coli (strain K-12) insertion sequence IS5 ALTERNATE_NAMES hypothetical protein f338 ORGANISM #formal_name Escherichia coli DATE 18-Dec-1981 #sequence_revision 05-Apr-1983 #text_change 01-Mar-2002 ACCESSIONS A91483; B03582; S47725; C64751; F64787; F64800; F64882; !1E64968; F64988; D65084; D65113; D65148; A04465 REFERENCE A91483 !$#authors Schoner, B.; Kahn, M. !$#journal Gene (1981) 14:165-174 !$#title The nucleotide sequence of IS5 from Escherichia coli. !$#cross-references MUID:82028653; PMID:6269959 !$#accession A91483 !'##molecule_type DNA !'##residues 1-338 ##label SCH !'##cross-references GB:J01734; NID:g149079 !'##note this ORF is not annotated in GenBank entry ECOIS5, release !1109.0 REFERENCE A03582 !$#authors Engler, J.A.; van Bree, M.P. !$#journal Gene (1981) 14:155-163 !$#title The nucleotide sequence and protein-coding capability of the !1transposable element IS5. !$#cross-references MUID:82028652; PMID:6269958 !$#accession B03582 !'##molecule_type DNA !'##residues 1-338 ##label ENG !'##cross-references GB:J01736; NID:g149083 !'##note this ORF is not annotated in GenBank entry INS5MUBCM, release !1109.0 REFERENCE S47666 !$#authors Plunkett, G. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S47725 !'##molecule_type DNA !'##residues 1-338 ##label PLU !'##cross-references EMBL:U00039; NID:g466582; PIDN:AAB18481.1; !1PID:g466642 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64751 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-338 ##label BLAT !'##cross-references GB:AE000133; GB:U00096; NID:g2367099; !1PIDN:AAC73362.1; PID:g1786453; UWGP:b0259 !'##experimental_source strain K-12, substrain MG1655 !'##genetics YI1 !$#accession F64787 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-338 ##label BLA2 !'##cross-references GB:AE000160; GB:U00096; NID:g1786751; !1PIDN:AAC73653.1; PID:g1786764; UWGP:b0552 !'##experimental_source strain K-12, substrain MG1655 !'##genetics YI2 !$#accession F64800 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-338 ##label BLA3 !'##cross-references GB:AE000170; GB:U00096; NID:g1786875; !1PIDN:AAC73757.1; PID:g1786877; UWGP:b0656 !'##experimental_source strain K-12, substrain MG1655 !'##genetics YI3 !$#accession F64882 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-338 ##label BLA4 !'##cross-references GB:AE000231; GB:U00096; NID:g1787588; !1PIDN:AAC74413.1; PID:g1787592; UWGP:b1331 !'##experimental_source strain K-12, substrain MG1655 !'##genetics YI4 !$#accession E64968 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-338 ##label BLA5 !'##cross-references GB:AE000294; GB:U00096; NID:g1788338; !1PIDN:AAC75091.1; PID:g1788342; UWGP:b2030 !'##experimental_source strain K-12, substrain MG1655 !'##genetics YI7 !$#accession F64988 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-338 ##label BLA6 !'##cross-references GB:AE000308; GB:U00096; NID:g1788508; !1PIDN:AAC75252.1; PID:g1788518; UWGP:b2192 !'##experimental_source strain K-12, substrain MG1655 !'##genetics YI8 !$#accession D65084 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-338 ##label BLA7 !'##cross-references GB:AE000381; GB:U00096; NID:g2367181; !1PIDN:AAC76018.1; PID:g1789355; UWGP:b2982 !'##experimental_source strain K-12, substrain MG1655 !'##genetics YI9 !$#accession D65113 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-338 ##label BLA8 !'##cross-references GB:AE000401; GB:U00096; NID:g1789607; !1PIDN:AAC76250.1; PID:g1789612; UWGP:b3218 !'##experimental_source strain K-12, substrain MG1655 !'##genetics Y10 !$#accession D65148 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-338 ##label BLA9 !'##cross-references GB:AE000427; GB:U00096; NID:g1789919; !1PIDN:AAC76530.1; PID:g1789921; UWGP:b3505 !'##experimental_source strain K-12, substrain MG1655 !'##genetics Y11 GENETICS YI1 !$#gene yi52_1 !$#mobile_element insertion sequence IS5 GENETICS YI2 !$#gene yi52_2 !$#mobile_element insertion sequence IS5 GENETICS YI3 !$#gene yi52_3 !$#mobile_element insertion sequence IS5 GENETICS YI4 !$#gene yi52_4 !$#mobile_element insertion sequence IS5 GENETICS YI7 !$#gene yi52_7 !$#mobile_element insertion sequence IS5 GENETICS YI8 !$#gene yi52_8 !$#mobile_element insertion sequence IS5 GENETICS YI9 !$#gene yi52_9 !$#mobile_element insertion sequence IS5 GENETICS Y10 !$#gene yi52_10 !$#mobile_element insertion sequence IS5 GENETICS Y11 !$#gene yi52_11 !$#mobile_element insertion sequence IS5 CLASSIFICATION #superfamily transposase IS5 SUMMARY #length 338 #molecular-weight 39327 #checksum 6809 SEQUENCE /// ENTRY IEEC5B #type complete TITLE hypothetical protein, 12K - Escherichia coli insertion sequence IS5 ORGANISM #formal_name Escherichia coli DATE 18-Dec-1981 #sequence_revision 18-Dec-1981 #text_change 10-Sep-1999 ACCESSIONS B91483; C03582; A04466 REFERENCE A91483 !$#authors Schoner, B.; Kahn, M. !$#journal Gene (1981) 14:165-174 !$#title The nucleotide sequence of IS5 from Escherichia coli. !$#cross-references MUID:82028653; PMID:6269959 !$#accession B91483 !'##molecule_type DNA !'##residues 1-118 ##label SCH REFERENCE A03582 !$#authors Engler, J.A.; van Bree, M.P. !$#journal Gene (1981) 14:155-163 !$#title The nucleotide sequence and protein-coding capability of the !1transposable element IS5. !$#cross-references MUID:82028652; PMID:6269958 !$#accession C03582 !'##molecule_type DNA !'##residues 1-118 ##label ENG GENETICS !$#mobile_element insertion sequence IS5 CLASSIFICATION #superfamily Escherichia coli hypothetical protein o263 SUMMARY #length 118 #molecular-weight 12270 #checksum 7134 SEQUENCE /// ENTRY QQECT9 #type complete TITLE hypothetical protein IR903 - Escherichia coli transposon Tn903 ORGANISM #formal_name Escherichia coli DATE 29-Jul-1981 #sequence_revision 29-Jul-1981 #text_change 23-Jul-1999 ACCESSIONS B92864; B93868; A04467 REFERENCE A92864 !$#authors Oka, A.; Sugisaki, H.; Takanami, M. !$#journal J. Mol. Biol. (1981) 147:217-226 !$#title Nucleotide sequence of the kanamycin resistance transposon !1Tn903. !$#cross-references MUID:82033200; PMID:6270337 !$#accession B92864 !'##molecule_type DNA !'##residues 1-114 ##label OKA !'##cross-references GB:V00359; GB:J01839; NID:g43025; PIDN:CAA23655.1; !1PID:g43026 !'##note this protein may be associated with transposition functions of !1transposon Tn903 REFERENCE A93868 !$#authors Grindley, N.D.F.; Joyce, C.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1980) 77:7176-7180 !$#title Genetic and DNA sequence analysis of the kanamycin !1resistance transposon Tn903. !$#cross-references MUID:81175113; PMID:6261245 !$#accession B93868 !'##molecule_type DNA !'##residues 1-114 ##label GRI !'##cross-references GB:V00621; GB:J01840; NID:g43762; PIDN:CAA23896.1; !1PID:g43763 GENETICS !$#mobile_element transposon Tn903 CLASSIFICATION #superfamily hypothetical protein IR903 SUMMARY #length 114 #molecular-weight 12758 #checksum 8690 SEQUENCE /// ENTRY QQEC47 #type complete TITLE probable transposase T31 - Escherichia coli (strain K-12) insertion sequence IS186 ALTERNATE_NAMES protein b2394 ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 13-Feb-1998 #text_change 01-Mar-2002 ACCESSIONS G65013; D64791; H64721; S40538; A25031; A24221 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65013 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-372 ##label BLAT !'##cross-references GB:AE000327; GB:U00096; NID:g1788731; !1PIDN:AAC75453.1; PID:g1788738; UWGP:b2394 !'##experimental_source strain K-12, substrain MG1655 !$#accession D64791 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 3-372 ##label BLA3 !'##cross-references GB:AE000163; GB:U00096; NID:g1786790; !1PIDN:AAC73683.1; PID:g1786796; UWGP:b0582 !'##experimental_source strain K-12, substrain MG1655, insertion !1sequence IS186 !'##genetics YI2 !$#accession H64721 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 3-372 ##label BLA2 !'##cross-references GB:AE000112; GB:U00096; NID:g1786192; !1PIDN:AAC73127.1; PID:g1786198; UWGP:b0016 !'##experimental_source strain K-12, substrain MG1655, insertion !1sequence IS186 !'##genetics YI1 REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40538 !'##status preliminary !'##molecule_type DNA !'##residues 3-372 ##label YUR !'##cross-references EMBL:D10483; NID:g216434; PIDN:BAA01293.1; !1PID:g216442 REFERENCE A25031 !$#authors Kothary, R.K.; Jones, D.; Candido, E.P.M. !$#journal J. Bacteriol. (1985) 164:957-959 !$#title IS186: an Escherichia coli insertion element isolated from a !1cDNA library. !$#cross-references MUID:86033672; PMID:2997142 !$#accession A25031 !'##molecule_type mRNA !'##residues 3-122,'G',124-127,'T',129-355,'SHRWIS',362-363, !1'EVRIRKEELTRCGE' ##label KOT !'##cross-references GB:M11300; NID:g149057; PIDN:AAA25030.1; !1PID:g149058 !'##experimental_source insertion sequence IS186 REFERENCE A24221 !$#authors Chong, P.; Hui, I.; Loo, T.; Gillam, S. !$#journal FEBS Lett. (1985) 192:47-52 !$#title Structural analysis of a new GC-specific insertion element !1IS186. !$#cross-references MUID:86030702; PMID:2996940 !$#accession A24221 !'##molecule_type mRNA !'##residues 3-355,'SHRWIS',362-363, !1'EVPDPKRRTNSLWRITKMVIWSLQVAIRGTVSLTAYKTQLKNARHRLNEAPRRRILQMV !1QPLS' ##label CHO !'##cross-references GB:X03123; NID:g43689; PIDN:CAA26900.1; PID:g43690 !'##experimental_source insertion sequence IS186 COMMENT This protein is encoded by an insertion sequence isolated !1from a cDNA library of Oncorhynchus mykiss (rainbow trout) !1and maintained in Escherichia coli RR1. The genetic source !1must be Escherichia coli. GENETICS YI2 !$#gene yi81_2 !$#mobile_element insertion sequence IS186 GENETICS YI1 !$#gene yi81_1 !$#mobile_element insertion sequence IS186 CLASSIFICATION #superfamily IS186 probable transposase T31 KEYWORDS transmembrane protein FEATURE !$337-353 #domain transmembrane #status predicted #label TMM SUMMARY #length 372 #molecular-weight 41137 #checksum 8120 SEQUENCE /// ENTRY QQECD7 #type complete TITLE tnsE protein - Escherichia coli transposon Tn7 ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 21-Jul-2000 ACCESSIONS A25543; S12641; S06770 REFERENCE A93644 !$#authors Smith, G.M.; Jones, P. !$#journal Nucleic Acids Res. (1986) 14:7915-7927 !$#title Tn7 transposition: a multigene process. Identification of a !1regulatory gene product. !$#cross-references MUID:87040763; PMID:3022239 !$#accession A25543 !'##molecule_type DNA !'##residues 1-538 ##label SMI !'##cross-references GB:X04534; NID:g43752; PIDN:CAB56509.1; !1PID:g5921493 REFERENCE S12637 !$#authors Flores, C.; Qadri, M.I.; Lichtenstein, C. !$#journal Nucleic Acids Res. (1990) 18:901-911 !$#title DNA sequence analysis of five genes; tnsA, B, C, D and E, !1required for Tn7 transposition. !$#cross-references MUID:90192166; PMID:2156235 !$#accession S12641 !'##molecule_type DNA !'##residues 1-538 ##label FLO !'##cross-references EMBL:X17693; NID:g43755; PIDN:CAA35687.1; !1PID:g581281 !'##note the authors translated the initiation codon GTG for residue 1 !1as Val GENETICS !$#gene tnsE !$#start_codon GTG FUNCTION !$#description required for the transposition of transposon Tn7 CLASSIFICATION #superfamily tnsE protein KEYWORDS DNA binding; transposition SUMMARY #length 538 #molecular-weight 61211 #checksum 2543 SEQUENCE /// ENTRY D38530 #type complete TITLE preprotein translocase chain yajC - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS D38530; JQ0695; S12300; G64769 REFERENCE A38530 !$#authors Reuter, K.; Slany, R.; Ullrich, F.; Kersten, H. !$#journal J. Bacteriol. (1991) 173:2256-2264 !$#title Structure and organization of Escherichia coli genes !1involved in biosynthesis of the deazaguanine derivative !1queuine, a nutrient factor for eukaryotes. !$#cross-references MUID:91177815; PMID:1706703 !$#accession D38530 !'##molecule_type DNA !'##residues 1-110 ##label REU !'##cross-references EMBL:M37702; NID:g147482 !'##experimental_source strain K-12 REFERENCE JQ0693 !$#authors Gardel, C.; Johnson, K.; Jacq, A.; Beckwith, J. !$#journal EMBO J. (1990) 9:3209-3216 !$#title The secD locus of E.coli codes for two membrane proteins !1required for protein export. !$#cross-references MUID:91006014; PMID:2170107 !$#accession JQ0695 !'##molecule_type DNA !'##residues 1-81,'R',83-110 ##label GAR !'##cross-references GB:X56175; NID:g42929; PIDN:CAA39633.1; PID:g42932 !'##experimental_source strain K-12 REFERENCE S12298 !$#authors Gardel, C.; Johnson, K.; Jacq, A.; Beckwith, J. !$#journal EMBO J. (1990) 9:4205-4206 !$#cross-references MUID:91065354; PMID:2249673 !$#contents erratum !$#accession S12300 !'##molecule_type DNA !'##residues 1-81,'R',83-110 ##label GA2 !'##cross-references EMBL:X56175; NID:g42929; PID:g42932 REFERENCE A36969 !$#authors Pogliano, K.J.; Beckwith, J. !$#journal J. Bacteriol. (1994) 176:804-814 !$#title Genetic and molecular characterization of the Escherichia !1coli secD operon and its products. !$#cross-references MUID:94131960; PMID:7507921 !$#contents annotation; functional study of yajC REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64769 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-110 ##label BLAT !'##cross-references GB:AE000147; GB:U00096; NID:g1786603; !1PIDN:AAC73510.1; PID:g1786608; UWGP:b0407 !'##experimental_source strain K-12, substrain MG1655 COMMENT Preprotein translocase contains a membrane-embedded trimeric !1complex of SecY, SecE and SecG and the peripheral SecA !1protein. The proteins SecD, SecF and YajC also form an !1integral membrane heterotrimeric complex. These two trimeric !1complexes are associated to form SecYEGDFyajC, the hexameric !1integral membrane domain of the pre- protein translocase !1'holoenzyme'. GENETICS !$#gene yajC !$#map_position 9 min COMPLEX heterohexamer; chains secY, secE, secG, secD, secF, and yajC CLASSIFICATION #superfamily yajC protein KEYWORDS protein export; transmembrane protein FEATURE !$23-39 #domain transmembrane #status predicted #label TMM SUMMARY #length 110 #molecular-weight 11887 #checksum 3892 SEQUENCE /// ENTRY A64146 #type complete TITLE yajC protein homolog HI0241 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS A64146 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession A64146 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-97 ##label TIGR !'##cross-references GB:U32710; GB:L42023; NID:g1573200; !1PIDN:AAC21909.1; PID:g1573206; TIGR:HI0241 CLASSIFICATION #superfamily yajC protein KEYWORDS transmembrane protein FEATURE !$8-24 #domain transmembrane #status predicted #label TMM SUMMARY #length 97 #molecular-weight 10754 #checksum 8866 SEQUENCE /// ENTRY G64713 #type complete TITLE conserved hypothetical secreted protein HP1551 - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS G64713 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession G64713 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-127 ##label TOM !'##cross-references GB:AE000653; GB:AE000511; NID:g2314733; !1PIDN:AAD08591.1; PID:g2314734; TIGR:HP1551 CLASSIFICATION #superfamily yajC protein SUMMARY #length 127 #molecular-weight 14392 #checksum 8282 SEQUENCE /// ENTRY WMEC5R #type complete TITLE replication control protein repA2 - Escherichia coli plasmid R1drd-19 ORGANISM #formal_name Escherichia coli DATE 29-Jul-1981 #sequence_revision 29-Jul-1981 #text_change 16-Feb-1997 ACCESSIONS A04484 REFERENCE A93120 !$#authors Stougaard, P.; Molin, S.; Nordstrom, K.; Hansen, F.G. !$#journal Mol. Gen. Genet. (1981) 181:116-122 !$#title The nucleotide sequence of the replication control region of !1the resistance plasmid R1drd-19. !$#cross-references MUID:81172236; PMID:6261081 !$#accession A04484 !'##molecule_type DNA !'##residues 1-86 ##label STO !'##note this protein is involved in the determination of copy number in !1gene replication GENETICS !$#genome plasmid CLASSIFICATION #superfamily repA2 protein KEYWORDS DNA binding; plasmid copy control; plasmid replication; !1transcription regulation SUMMARY #length 86 #molecular-weight 10038 #checksum 9371 SEQUENCE /// ENTRY QQECAR #type complete TITLE replication control protein repA2 - Escherichia coli plasmids ALTERNATE_NAMES replication control protein copB ORGANISM #formal_name Escherichia coli DATE 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 23-Jul-1999 ACCESSIONS A04476; B04476; A28378; A44820; S21510; I41106; I58974 REFERENCE A93119 !$#authors Rosen, J.; Ryder, T.; Inokuchi, H.; Ohtsubo, H.; Ohtsubo, E. !$#journal Mol. Gen. Genet. (1980) 179:527-537 !$#title Genes and sites involved in replication and incompatibility !1of an R100 plasmid derivative based on nucleotide sequence !1analysis. !$#cross-references MUID:81074309; PMID:7003300 !$#accession A04476 !'##molecule_type DNA !'##residues 1-103 ##label RO1 !'##cross-references GB:J01762; GB:J01761; GB:J01767; GB:J01768; !1NID:g151740; PIDN:AAA92255.1; PID:g151744 REFERENCE A93253 !$#authors Rosen, J.; Ryder, T.; Ohtsubo, H.; Ohtsubo, E. !$#journal Nature (1981) 290:794-797 !$#title Role of RNA transcripts in replication incompatibility and !1copy number control in antibiotic resistance plasmid !1derivatives. !$#cross-references MUID:81173118; PMID:6163994 !$#accession B04476 !'##status preliminary !'##molecule_type DNA !'##residues 81-103 ##label ROS REFERENCE A28378 !$#authors Dong, X.; Womble, D.D.; Rownd, R.H. !$#journal J. Bacteriol. (1987) 169:5353-5363 !$#title Transcriptional pausing in a region important for plasmid !1NR1 replication control. !$#cross-references MUID:88058738; PMID:2445727 !$#accession A28378 !'##molecule_type DNA !'##residues 1-80,'KRCM' ##label DON !'##cross-references GB:M18273; NID:g150397; PIDN:AAA88332.1; !1PID:g1196669 !'##experimental_source plasmid NR1 REFERENCE A44820 !$#authors Lopez, J.; Delgado, D.; Andres, I.; Ortiz, J.M.; Rodriguez, !1J.C. !$#journal J. Gen. Microbiol. (1991) 137:1093-1099 !$#title Isolation and evolutionary analysis of a RepFVIB replicon of !1the plasmid pSU212. !$#cross-references MUID:91324851; PMID:1865183 !$#contents replicon RepFVIB !$#accession A44820 !'##molecule_type DNA !'##residues 1-80,'KRCM' ##label LOP !'##experimental_source plasmid pSU212 !'##note sequence extracted from NCBI backbone (NCBIN:45962, !1NCBIP:45965) REFERENCE S21510 !$#authors Andres, L.; Rodriquez, O. !$#submission submitted to the EMBL Data Library, September 1990 !$#accession S21510 !'##status preliminary !'##molecule_type DNA !'##residues 1-80,'KRCM' ##label AND !'##cross-references EMBL:X55895; NID:g42544; PIDN:CAA39380.1; !1PID:g42545 REFERENCE I41106 !$#authors Womble, D.D.; Sampathkumar, P.; Easton, A.M.; Luckow, V.A.; !1Rownd, R.H. !$#journal J. Mol. Biol. (1985) 181:395-410 !$#title Transcription of the replication control region of the !1IncFII R-plasmid NR1 in vitro and in vivo. !$#cross-references MUID:85160860; PMID:2580099 !$#accession I41106 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-80,'KRCM' ##label RES !'##cross-references EMBL:X02302; NID:g42132; PIDN:CAA26165.1; !1PID:g42133 REFERENCE I58974 !$#authors Danbara, H.; Brady, G.; Timmis, J.K.; Timmis, K.N. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:4699-4703 !$#title Regulation of DNA replication: 'target' determinant of the !1replication control elements of plasmid R6-5 lies within a !1control element gene. !$#cross-references MUID:82060121; PMID:7029525 !$#accession I58974 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-80,'KRCM' ##label RE2 !'##cross-references EMBL:V00318; NID:g42485; PIDN:CAA23608.1; !1PID:g42486 GENETICS !$#gene copB; repA2 !$#genome plasmid CLASSIFICATION #superfamily repA2 protein KEYWORDS DNA binding; plasmid copy control; plasmid replication; !1transcription regulation SUMMARY #length 103 #molecular-weight 11393 #checksum 7761 SEQUENCE /// ENTRY QQECAP #type complete TITLE replication control protein repA2 - Escherichia coli plasmid P307 ORGANISM #formal_name Escherichia coli DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 24-Sep-1999 ACCESSIONS A26870; S15224 REFERENCE A91829 !$#authors Saadi, S.; Maas, W.K.; Hill, D.F.; Bergquist, P.L. !$#journal J. Bacteriol. (1987) 169:1836-1846 !$#title Nucleotide sequence analysis of RepFIC, a basic replicon !1present in IncFI plasmids P307 and F, and its relation to !1the RepA replicon of IncFII plasmids. !$#cross-references MUID:87194554; PMID:3032897 !$#accession A26870 !'##molecule_type DNA !'##residues 1-85 ##label SAA !'##cross-references GB:M16167; NID:g1621020; PIDN:AAB17110.1; !1PID:g150461 REFERENCE S15224 !$#authors Maas, R.; Oppenheim, J.; Saadi, S.; Fuchs, T.; Maas, W.K. !$#journal Mol. Microbiol. (1991) 5:927-932 !$#title Isolation and properties of the RepA1 protein of the IncFII !1replicon, RepFIC. !$#cross-references MUID:91312131; PMID:1857211 !$#accession S15224 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-85 ##label MAA !'##cross-references EMBL:M16167; NID:g1621020; PIDN:AAB17110.1; !1PID:g150461 !'##note this sequence was submitted to the EMBL Data Library, June 1991 GENETICS !$#gene copB; repA2 !$#genome plasmid CLASSIFICATION #superfamily repA2 protein KEYWORDS DNA binding; plasmid copy control; plasmid replication; !1transcription regulation SUMMARY #length 85 #molecular-weight 9604 #checksum 6865 SEQUENCE /// ENTRY QQECAA #type complete TITLE yacA protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1988 #sequence_revision 14-Nov-1997 #text_change 01-Mar-2002 ACCESSIONS A64732; B28381; B31088; S40607 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64732 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-195 ##label BLAT !'##cross-references GB:AE000119; GB:U00096; NID:g1786283; !1PIDN:AAC73208.1; PID:g1786286; UWGP:b0097 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A91852 !$#authors Beall, B.; Lutkenhaus, J. !$#journal J. Bacteriol. (1987) 169:5408-5415 !$#title Sequence analysis, transcriptional organization, and !1insertional mutagenesis of the envA gene of Escherichia !1coli. !$#cross-references MUID:88058745; PMID:2824434 !$#accession B28381 !'##molecule_type DNA !'##residues 49-195 ##label BEA !'##cross-references GB:X55034; GB:M10429; NID:g40841; PIDN:CAA38874.1; !1PID:g40865 REFERENCE A31088 !$#authors Schmidt, M.G.; Rollo, E.E.; Grodberg, J.; Oliver, D.B. !$#journal J. Bacteriol. (1988) 170:3404-3414 !$#title Nucleotide sequence of the secA gene and secA(Ts) mutations !1preventing protein export in Escherichia coli. !$#cross-references MUID:88298644; PMID:2841285 !$#accession B31088 !'##molecule_type DNA !'##residues 49-195 ##label SCH !'##cross-references GB:X55034; GB:M10429; NID:g40841; PIDN:CAA38874.1; !1PID:g40865 REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40607 !'##status preliminary !'##molecule_type DNA !'##residues 49-195 ##label YUR !'##cross-references EMBL:D10483; NID:g216434; PIDN:BAA01362.1; !1PID:g216511 GENETICS !$#gene yacA !$#map_position 2 min CLASSIFICATION #superfamily Escherichia coli yacA protein SUMMARY #length 195 #molecular-weight 21738 #checksum 4273 SEQUENCE /// ENTRY QQEC45 #type complete TITLE hypothetical protein 1 - Escherichia coli plasmid pAO2 ORGANISM #formal_name Escherichia coli DATE 31-Oct-1980 #sequence_revision 08-Oct-1981 #text_change 10-Sep-1999 ACCESSIONS C93118; A04474 REFERENCE A93118 !$#authors Oka, A.; Nomura, N.; Morita, M.; Sugisaki, H.; Sugimoto, K.; !1Takanami, M. !$#journal Mol. Gen. Genet. (1979) 172:151-159 !$#title Nucleotide sequence of small CoIE1 derivitives: structure of !1the regions essential for autonomous replication and colicin !1E1 immunity. !$#cross-references MUID:80010893; PMID:384144 !$#accession C93118 !'##molecule_type DNA !'##residues 1-42 ##label OKA REFERENCE A93697 !$#authors Stuitje, A.R.; Veltkamp, E.; Maat, J.; Heyneker, H.L. !$#journal Nucleic Acids Res. (1980) 8:1459-1473 !$#title The nucleotide sequence surrounding the replication origin !1of the cop3 mutant of the bacteriocinogenic plasmid Clo !1DF13. !$#cross-references MUID:81053824; PMID:6253936 !$#contents annotation; identification of hypothetical protein coding !1region GENETICS !$#genome plasmid CLASSIFICATION #superfamily Escherichia coli plasmid pAO2 hypothetical !1protein 1 SUMMARY #length 42 #molecular-weight 4862 #checksum 288 SEQUENCE /// ENTRY QQECP3 #type complete TITLE hypothetical protein 1 - Escherichia coli plasmid CloDF13 ORGANISM #formal_name Escherichia coli DATE 29-Jul-1981 #sequence_revision 29-Jul-1981 #text_change 10-Sep-1999 ACCESSIONS B93250; A93697; A04475 REFERENCE A93250 !$#authors Stuitje, A.R.; Spelt, C.E.; Veltkamp, E.; Nijkamp, H.J.J. !$#journal Nature (1981) 290:264-267 !$#title Identification of mutations affecting replication control of !1plasmid Clo DF13. !$#cross-references MUID:81148852; PMID:6163089 !$#accession B93250 !'##molecule_type DNA !'##residues 1-47 ##label ST1 REFERENCE A93697 !$#authors Stuitje, A.R.; Veltkamp, E.; Maat, J.; Heyneker, H.L. !$#journal Nucleic Acids Res. (1980) 8:1459-1473 !$#title The nucleotide sequence surrounding the replication origin !1of the cop3 mutant of the bacteriocinogenic plasmid Clo !1DF13. !$#cross-references MUID:81053824; PMID:6253936 !$#contents mutant cop3 !$#accession A93697 !'##molecule_type DNA !'##residues 1-47 ##label ST2 COMMENT Plasmid Clo DF13 originates from Enterobacter cloacae but is !1stably maintained in and studied mostly from E. coli. GENETICS !$#genome plasmid CLASSIFICATION #superfamily Escherichia coli plasmid pAO2 hypothetical !1protein 1 SUMMARY #length 47 #molecular-weight 5433 #checksum 9624 SEQUENCE /// ENTRY QQECBR #type complete TITLE replication-associated protein A4 - Escherichia coli plasmids ORGANISM #formal_name Escherichia coli DATE 18-Dec-1981 #sequence_revision 18-Dec-1981 #text_change 23-Jul-1999 ACCESSIONS A04477; A93253; B48662; I64781 REFERENCE A93253 !$#authors Rosen, J.; Ryder, T.; Ohtsubo, H.; Ohtsubo, E. !$#journal Nature (1981) 290:794-797 !$#title Role of RNA transcripts in replication incompatibility and !1copy number control in antibiotic resistance plasmid !1derivatives. !$#cross-references MUID:81173118; PMID:6163994 !$#accession A04477 !'##molecule_type DNA !'##residues 1-128 ##label ROS1 !'##experimental_source plasmid R100 !$#accession A93253 !'##molecule_type DNA !'##residues 1-128 ##label ROS2 !'##experimental_source plasmid R1 REFERENCE A48662 !$#authors Jiang, T.; Min, Y.N.; Liu, W.; Womble, D.D.; Rownd, R.H. !$#journal J. Bacteriol. (1993) 175:5350-5358 !$#title Insertion and deletion mutations in the repA4 region of the !1IncFII plasmid NR1 cause unstable inheritance. !$#cross-references MUID:93374828; PMID:8396115 !$#accession B48662 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-128 ##label JIA !'##experimental_source plasmid NR1 REFERENCE I51821 !$#authors Ohtsubo, H.; Ryder, T.B.; Maeda, Y.; Armstrong, K.A.; !1Ohtsubo, E. !$#journal Adv. Biophys. (1986) 21:115-133 !$#title DNA replication of the resistance plasmid R100 and its !1control. !$#cross-references MUID:86319522; PMID:3019092 !$#accession I64781 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-128 ##label RES !'##cross-references GB:M26840; NID:g151770; PIDN:AAA26068.1; !1PID:g151774 GENETICS !$#gene repA4 !$#genome plasmid CLASSIFICATION #superfamily replication-associated protein A4 SUMMARY #length 128 #molecular-weight 14230 #checksum 7005 SEQUENCE /// ENTRY QQEC6K #type complete TITLE hypothetical 6.8K protein - plasmid RK2 ORGANISM #formal_name plasmid RK2 DATE 29-Jul-1981 #sequence_revision 29-Jul-1981 #text_change 26-Aug-1999 ACCESSIONS A04478 REFERENCE A04478 !$#authors Stalker, D.M.; Thomas, C.M.; Helinski, D.R. !$#journal Mol. Gen. Genet. (1981) 181:8-12 !$#title Nucleotide sequence of the region of the origin of !1replication of the broad host range plasmid RK2. !$#cross-references MUID:81172248; PMID:6261086 !$#accession A04478 !'##molecule_type DNA !'##residues 1-62 ##label STA GENETICS !$#genome plasmid CLASSIFICATION #superfamily plasmid RK2 hypothetical 6.8K protein SUMMARY #length 62 #molecular-weight 6805 #checksum 8674 SEQUENCE /// ENTRY QQEC2 #type complete TITLE hypothetical protein A-87 - Escherichia coli plasmid pBR322 ORGANISM #formal_name Escherichia coli DATE 31-Dec-1980 #sequence_revision 15-Oct-1982 #text_change 10-Sep-1999 ACCESSIONS A04479 REFERENCE A90923 !$#authors Sutcliffe, J.G. !$#journal Cold Spring Harb. Symp. Quant. Biol. (1979) 43:77-90 !$#title Complete nucleotide sequence of the Escherichia coli plasmid !1pBR322. !$#cross-references MUID:80002802; PMID:383387 !$#accession A04479 !'##molecule_type DNA !'##residues 1-87 ##label SUT GENETICS !$#genome plasmid !$#start_codon GTG CLASSIFICATION #superfamily Escherichia coli plasmid pBR322 hypothetical !110K protein SUMMARY #length 87 #molecular-weight 10035 #checksum 3775 SEQUENCE /// ENTRY QQEC7 #type complete TITLE hypothetical protein C-84 - Escherichia coli plasmid pBR322 ORGANISM #formal_name Escherichia coli DATE 31-Dec-1980 #sequence_revision 15-Oct-1982 #text_change 10-Sep-1999 ACCESSIONS A04480 REFERENCE A90923 !$#authors Sutcliffe, J.G. !$#journal Cold Spring Harb. Symp. Quant. Biol. (1979) 43:77-90 !$#title Complete nucleotide sequence of the Escherichia coli plasmid !1pBR322. !$#cross-references MUID:80002802; PMID:383387 !$#accession A04480 !'##molecule_type DNA !'##residues 1-84 ##label SUT COMMENT The author translated the codon TTG for the residue at !1position 52 as Phe. GENETICS !$#genome plasmid !$#start_codon GTG CLASSIFICATION #superfamily Escherichia coli plasmid pBR322 hypothetical !19.4K protein SUMMARY #length 84 #molecular-weight 9364 #checksum 6584 SEQUENCE /// ENTRY QQEC8 #type complete TITLE hypothetical protein D-132 - Escherichia coli plasmid pBR322 ORGANISM #formal_name Escherichia coli DATE 31-Dec-1980 #sequence_revision 31-Dec-1980 #text_change 10-Sep-1999 ACCESSIONS A04481 REFERENCE A90923 !$#authors Sutcliffe, J.G. !$#journal Cold Spring Harb. Symp. Quant. Biol. (1979) 43:77-90 !$#title Complete nucleotide sequence of the Escherichia coli plasmid !1pBR322. !$#cross-references MUID:80002802; PMID:383387 !$#accession A04481 !'##molecule_type DNA !'##residues 1-132 ##label SUT GENETICS !$#genome plasmid CLASSIFICATION #superfamily Escherichia coli plasmid pBR322 hypothetical !115.3K protein SUMMARY #length 132 #molecular-weight 15322 #checksum 7480 SEQUENCE /// ENTRY QQECC8 #type complete TITLE hypothetical protein C-88 - Escherichia coli plasmid pBR322 ORGANISM #formal_name Escherichia coli DATE 08-Aug-1983 #sequence_revision 08-Aug-1983 #text_change 10-Sep-1999 ACCESSIONS A04482 REFERENCE A90923 !$#authors Sutcliffe, J.G. !$#journal Cold Spring Harb. Symp. Quant. Biol. (1979) 43:77-90 !$#title Complete nucleotide sequence of the Escherichia coli plasmid !1pBR322. !$#cross-references MUID:80002802; PMID:383387 !$#accession A04482 !'##molecule_type DNA !'##residues 1-88 ##label SUT GENETICS !$#genome plasmid CLASSIFICATION #superfamily Escherichia coli plasmid pBR322 hypothetical !19.2K protein SUMMARY #length 88 #molecular-weight 9213 #checksum 7429 SEQUENCE /// ENTRY A36141 #type complete TITLE cop protein - Staphylococcus aureus plasmid pE194 ORGANISM #formal_name Staphylococcus aureus DATE 30-Nov-1990 #sequence_revision 08-Dec-1995 #text_change 23-Jul-1999 ACCESSIONS A36141 REFERENCE A36141 !$#authors Byeon, W.H.; Weisblum, B. !$#journal J. Bacteriol. (1990) 172:5892-5900 !$#title Replication genes of plasmid pE194-cop and repF: transcripts !1and encoded proteins. !$#cross-references MUID:91008965; PMID:2120193 !$#accession A36141 !'##molecule_type DNA !'##residues 1-55 ##label BYE !'##cross-references GB:M59209; NID:g150652; PIDN:AAA25602.1; !1PID:g150653 GENETICS !$#gene cop !$#genome plasmid CLASSIFICATION #superfamily Staphylococcus aureus plasmid cop protein KEYWORDS DNA binding; plasmid copy control SUMMARY #length 55 #molecular-weight 6405 #checksum 5650 SEQUENCE /// ENTRY QQEC71 #type complete TITLE probable cop protein - Escherichia coli plasmids ORGANISM #formal_name Escherichia coli DATE 31-Dec-1991 #sequence_revision 31-Dec-1991 #text_change 23-Jul-1999 ACCESSIONS B93253; A04483; I64779; A93120; I41108; I54849; I79323 REFERENCE A93253 !$#authors Rosen, J.; Ryder, T.; Ohtsubo, H.; Ohtsubo, E. !$#journal Nature (1981) 290:794-797 !$#title Role of RNA transcripts in replication incompatibility and !1copy number control in antibiotic resistance plasmid !1derivatives. !$#cross-references MUID:81173118; PMID:6163994 !$#accession B93253 !'##molecule_type DNA !'##residues 1-61 ##label ROS1 !'##cross-references GB:J01762; GB:J01761; GB:J01767; GB:J01768; !1NID:g151740; PIDN:AAA92256.1; PID:g151745 !'##experimental_source plasmid R1 !$#accession A04483 !'##molecule_type DNA !'##residues 1-61 ##label ROS2 !'##cross-references GB:J01762; GB:J01761; GB:J01767; GB:J01768; !1NID:g151740; PIDN:AAA92256.1; PID:g151745 !'##experimental_source plasmid R100 REFERENCE I51821 !$#authors Ohtsubo, H.; Ryder, T.B.; Maeda, Y.; Armstrong, K.A.; !1Ohtsubo, E. !$#journal Adv. Biophys. (1986) 21:115-133 !$#title DNA replication of the resistance plasmid R100 and its !1control. !$#cross-references MUID:86319522; PMID:3019092 !$#accession I64779 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-61 ##label RES !'##cross-references GB:M26840; NID:g151770; PIDN:AAA26066.1; !1PID:g151772 REFERENCE A93120 !$#authors Stougaard, P.; Molin, S.; Nordstrom, K.; Hansen, F.G. !$#journal Mol. Gen. Genet. (1981) 181:116-122 !$#title The nucleotide sequence of the replication control region of !1the resistance plasmid R1drd-19. !$#cross-references MUID:81172236; PMID:6261081 !$#accession A93120 !'##molecule_type DNA !'##residues 1-18,'W',20-61 ##label STO !'##cross-references GB:V00326; GB:J01772; NID:g42636; PIDN:CAA23617.1; !1PID:g671862 !'##note this protein is most likely the cop gene protein, which !1controls the copy number in gene replication REFERENCE I41106 !$#authors Womble, D.D.; Sampathkumar, P.; Easton, A.M.; Luckow, V.A.; !1Rownd, R.H. !$#journal J. Mol. Biol. (1985) 181:395-410 !$#title Transcription of the replication control region of the !1IncFII R-plasmid NR1 in vitro and in vivo. !$#cross-references MUID:85160860; PMID:2580099 !$#accession I41108 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-18,'W',20-61 ##label RE4 !'##cross-references EMBL:X02302; NID:g42132; PIDN:CAA26167.1; !1PID:g42134 REFERENCE I54849 !$#authors Brady, G.; Frey, J.; Danbara, H.; Timmis, K.N. !$#journal J. Bacteriol. (1983) 154:429-436 !$#title Replication control mutations of plasmid R6-5 and their !1effects on interactions of the RNA-I control element with !1its target. !$#cross-references MUID:83160806; PMID:6187730 !$#accession I54849 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-18,'W',20-61 ##label RE2 !'##cross-references EMBL:V00319; NID:g42488; PIDN:CAA23610.1; !1PID:g42489 REFERENCE I58974 !$#authors Danbara, H.; Brady, G.; Timmis, J.K.; Timmis, K.N. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1981) 78:4699-4703 !$#title Regulation of DNA replication: 'target' determinant of the !1replication control elements of plasmid R6-5 lies within a !1control element gene. !$#cross-references MUID:82060121; PMID:7029525 !$#accession I79323 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-18,'W',20-61 ##label RE3 !'##cross-references EMBL:V00318; NID:g42485; PIDN:CAA23609.1; !1PID:g42487 GENETICS !$#genome plasmid COMPLEX homodimer FUNCTION !$#description controls the copy number in gene replication CLASSIFICATION #superfamily cop protein KEYWORDS plasmid copy control SUMMARY #length 61 #molecular-weight 7179 #checksum 7942 SEQUENCE /// ENTRY IDECRK #type complete TITLE replication initiation protein - Escherichia coli plasmid R6K ORGANISM #formal_name Escherichia coli DATE 13-Jun-1983 #sequence_revision 30-Sep-1993 #text_change 08-Mar-1996 ACCESSIONS S02261; A03603; S12034 REFERENCE S02261 !$#authors Inuzuka, M.; Wada, Y. !$#journal EMBO J. (1985) 4:2301-2307 !$#title A single amino acid alteration in the initiation protein is !1responsible for the DNA overproduction phenotype of copy !1number mutants of plasmid R6K. !$#cross-references MUID:86081740; PMID:3000771 !$#accession S02261 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-305 ##label INU !'##cross-references EMBL:Y00768 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1February 1988 REFERENCE A03603 !$#authors Germino, J.; Bastia, D. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:5475-5479 !$#title Primary structure of the replication initiation protein of !1plasmid R6K. !$#cross-references MUID:83039393; PMID:6291046 !$#accession A03603 !'##molecule_type DNA !'##residues 1-305 ##label GER !'##note the authors translated the codon AAG for residue 258 as Asn REFERENCE S12034 !$#authors Greener, A.; Filutowicz, M.S.; McEachern, M.J.; Helinski, !1D.R. !$#journal Mol. Gen. Genet. (1990) 224:24-32 !$#title N-terminal truncated forms of the bifunctional pi initiation !1protein express negative activity on plasmid R6K !1replication. !$#cross-references MUID:91117173; PMID:2277631 !$#accession S12034 !'##status preliminary !'##molecule_type DNA !'##residues 75-117 ##label GRE GENETICS !$#gene pir !$#genome plasmid CLASSIFICATION #superfamily replication initiation protein KEYWORDS plasmid copy control; replication SUMMARY #length 305 #molecular-weight 34959 #checksum 1075 SEQUENCE /// ENTRY QQEC27 #type complete TITLE 27K replication protein - Escherichia coli plasmid pCU1 ORGANISM #formal_name Escherichia coli DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 23-Jul-1999 ACCESSIONS JQ0682; JQ0045; JQ0046; I57778 REFERENCE JQ0682 !$#authors Krishnan, B.R.; Fobert, P.R.; Seitzer, U.; Iyer, V.N. !$#journal Gene (1990) 91:1-7 !$#title Mutations within the replicon of the IncN plasmid pCU1 that !1affect its Escherichia coli polA-independence but not its !1autonomous replication ability. !$#cross-references MUID:90382682; PMID:2205534 !$#contents plasmid pCU1 !$#accession JQ0682 !'##molecule_type DNA !'##residues 1-239 ##label KRI !'##cross-references GB:M18262; GB:X52972; NID:g146869; PIDN:AAA98068.1; !1PID:g146871 REFERENCE JQ0045 !$#authors Kozlowski, M.; Thatte, V.; Lau, P.C.K.; Visentin, L.P.; !1Iyer, V.N. !$#journal Gene (1987) 58:217-228 !$#title Isolation and structure of the replicon of the promiscuous !1plasmid pCU1. !$#cross-references MUID:88112872; PMID:2828186 !$#accession JQ0045 !'##molecule_type DNA !'##residues 1-43,'FSKRR' ##label KOZ !$#accession JQ0046 !'##molecule_type DNA !'##residues 'MQ',164-208,'R',210-218 ##label KO2 REFERENCE I57778 !$#authors Gigliani, F.; Ciotta, C.; Del Grosso, M.F.; Battaglia, P.A. !$#journal Mol. Gen. Genet. (1993) 238:333-338 !$#title pR plasmid replication provides evidence that !1single-stranded DNA induces the SOS system in vivo. !$#cross-references MUID:93261415; PMID:8492801 !$#accession I57778 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-239 ##label RES !'##cross-references GB:S61747; NID:g404337 GENETICS !$#genome plasmid CLASSIFICATION #superfamily 27K replication protein KEYWORDS plasmid copy control; replication SUMMARY #length 239 #molecular-weight 27591 #checksum 9739 SEQUENCE /// ENTRY QQECR7 #type complete TITLE gene E protein - Escherichia coli plasmid R27 ORGANISM #formal_name Escherichia coli DATE 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 23-Jul-1999 ACCESSIONS S03768 REFERENCE S03768 !$#authors Saul, D.; Lane, D.; Bergquist, P.L. !$#journal Mol. Microbiol. (1988) 2:219-225 !$#title A replication region of the IncHI plasmid, R27, is highly !1homologous with the RepFIA replicon of F. !$#cross-references MUID:88246049; PMID:3288833 !$#accession S03768 !'##molecule_type DNA !'##residues 1-251 ##label SAU !'##cross-references EMBL:Y00547; NID:g45794; PIDN:CAA68616.1; !1PID:g671612 GENETICS !$#gene E !$#genome plasmid CLASSIFICATION #superfamily 27K replication protein KEYWORDS plasmid copy control; replication SUMMARY #length 251 #molecular-weight 29377 #checksum 8547 SEQUENCE /// ENTRY QQECF #type complete TITLE Replication initiation protein (REP protein) (Protein E) (F4 protein) - Escherichia coli plasmid F ORGANISM #formal_name Escherichia coli DATE 02-Apr-1982 #sequence_revision 02-Apr-1982 #text_change 27-Nov-2001 ACCESSIONS A91487; A90811; D25783; I41086; A04485 REFERENCE A91487 !$#authors Murotsu, T.; Matsubara, K.; Sugisaki, H.; Takanami, M. !$#journal Gene (1981) 15:257-271 !$#title Nine unique repeating sequences in a region essential for !1replication and incompatibility of the mini-F plasmid. !$#cross-references MUID:82051318; PMID:7028572 !$#accession A91487 !'##molecule_type DNA !'##residues 1-251 ##label MUR !'##cross-references GB:J01724; GB:X00959; NID:g148595; PIDN:AAA91062.1; !1PID:g148596 REFERENCE A90811 !$#authors Tolun, A.; Helinski, D.R. !$#journal Cell (1981) 24:687-694 !$#title Direct repeats of the F plasmid incC region express F !1incompatibility. !$#cross-references MUID:81234554; PMID:7018695 !$#accession A90811 !'##molecule_type DNA !'##residues 211-251 ##label TOL REFERENCE A92934 !$#authors Mori, H.; Kondo, A.; Ohshima, A.; Ogura, T.; Hiraga, S. !$#journal J. Mol. Biol. (1986) 192:1-15 !$#title Structure and function of the F plasmid genes essential for !1partitioning. !$#cross-references MUID:87141188; PMID:3029390 !$#accession D25783 !'##molecule_type DNA !'##residues 209-251 ##label MOR !'##cross-references GB:X04619; NID:g42429; PIDN:CAA28294.1; PID:g42430 REFERENCE I41085 !$#authors Disque-Kochem, C.; Seidel, U.; Helsberg, M.; Eichenlaub, R. !$#journal Mol. Gen. Genet. (1986) 202:132-135 !$#title The repeated sequences (incB) preceding the protein E gene !1of plasmid mini-F are essential for replication. !$#cross-references MUID:86174346; PMID:3007930 !$#accession I41086 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-17 ##label RES !'##cross-references EMBL:X03410; NID:g41804; PIDN:CAA27146.1; !1PID:g41805 COMMENT This protein is essential for replication from ori-2. GENETICS !$#gene rep !$#map_position 44.1-46.4 !$#genome plasmid CLASSIFICATION #superfamily 27K replication protein KEYWORDS plasmid copy control; replication SUMMARY #length 251 #molecular-weight 29358 #checksum 9658 SEQUENCE /// ENTRY QQECU2 #type complete TITLE hypothetical 21.9K protein - Escherichia coli plasmid pCU1 ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 30-Jun-1990 #text_change 26-Aug-1999 ACCESSIONS JQ0047 REFERENCE JQ0045 !$#authors Kozlowski, M.; Thatte, V.; Lau, P.C.K.; Visentin, L.P.; !1Iyer, V.N. !$#journal Gene (1987) 58:217-228 !$#title Isolation and structure of the replicon of the promiscuous !1plasmid pCU1. !$#cross-references MUID:88112872; PMID:2828186 !$#accession JQ0047 !'##molecule_type DNA !'##residues 1-207 ##label KOZ GENETICS !$#genome plasmid CLASSIFICATION #superfamily Escherichia coli plasmid pCU1 hypothetical !121.9K protein SUMMARY #length 207 #molecular-weight 21885 #checksum 6199 SEQUENCE /// ENTRY QQEC4W #type complete TITLE Citrate utilization protein B - Escherichia coli plasmid pWR60 ORGANISM #formal_name Escherichia coli DATE 30-Jun-1988 #sequence_revision 30-Jun-1988 #text_change 27-Nov-2001 ACCESSIONS A23104 REFERENCE A91810 !$#authors Sasatsu, M.; Misra, T.K.; Chu, L.; Laddaga, R.; Silver, S. !$#journal J. Bacteriol. (1985) 164:983-993 !$#title Cloning and DNA sequence of a plasmid-determined citrate !1utilization system in Escherichia coli. !$#cross-references MUID:86059247; PMID:2999088 !$#accession A23104 !'##molecule_type DNA !'##residues 1-379 ##label SAS !'##cross-references GB:M11559; NID:g151715; PIDN:AAA88471.1; !1PID:g1196800 GENETICS !$#genome plasmid CLASSIFICATION #superfamily Escherichia coli plasmid pWR60 hypothetical 42K !1protein SUMMARY #length 379 #molecular-weight 41797 #checksum 7393 SEQUENCE /// ENTRY QQEC25 #type complete TITLE hypothetical 12.5K protein (trbB-trbF intergenic region) - Escherichia coli plasmid F ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 26-Aug-1999 ACCESSIONS F32238 REFERENCE A32238 !$#authors Wu, J.H.; Ippen-Ihler, K. !$#journal J. Bacteriol. (1989) 171:213-221 !$#title Nucleotide sequence of traQ and adjacent loci in the !1Escherichia coli K-12 F-plasmid transfer operon. !$#cross-references MUID:89123020; PMID:2536655 !$#accession F32238 !'##molecule_type DNA !'##residues 1-113 ##label WU1 !'##cross-references GB:M20787; NID:g148622; PIDN:AAC63068.1; !1PID:g1181551 !'##experimental_source strain K12 GENETICS !$#genome plasmid CLASSIFICATION #superfamily Escherichia coli plasmid F hypothetical 12.5K !1protein (trbB-trbF intergenic region) SUMMARY #length 113 #molecular-weight 12587 #checksum 1549 SEQUENCE /// ENTRY Q4ECTD #type complete TITLE hypothetical 26.3K protein (traD-traI intergenic region) - Escherichia coli plasmid F ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 26-Aug-1999 ACCESSIONS JS0294 REFERENCE JS0293 !$#authors Jalajakumari, M.B.; Manning, P.A. !$#journal Gene (1989) 81:195-202 !$#title Nucleotide sequence of the traD region in the Escherichia !1coli F sex factor. !$#cross-references MUID:90034191; PMID:2680768 !$#accession JS0294 !'##molecule_type DNA !'##residues 1-239 ##label JAL !'##cross-references GB:M29254; NID:g148618; PIDN:AAA83929.1; !1PID:g1128984 !'##experimental_source strain K12 !'##note this may be a cytoplasmic membrane protein GENETICS !$#genome plasmid CLASSIFICATION #superfamily Escherichia coli plasmid F hypothetical 26.3K !1protein (traD-traI intergenic region) KEYWORDS transmembrane protein SUMMARY #length 239 #molecular-weight 26259 #checksum 9969 SEQUENCE /// ENTRY Q4ECTI #type complete TITLE hypothetical 8.5K protein (traD-traI intergenic region) - Escherichia coli plasmid F ORGANISM #formal_name Escherichia coli DATE 30-Jun-1990 #sequence_revision 30-Jun-1990 #text_change 26-Aug-1999 ACCESSIONS JS0295 REFERENCE JS0293 !$#authors Jalajakumari, M.B.; Manning, P.A. !$#journal Gene (1989) 81:195-202 !$#title Nucleotide sequence of the traD region in the Escherichia !1coli F sex factor. !$#cross-references MUID:90034191; PMID:2680768 !$#accession JS0295 !'##molecule_type DNA !'##residues 1-75 ##label JAL !'##experimental_source strain K12 GENETICS !$#genome plasmid CLASSIFICATION #superfamily Escherichia coli plasmid F hypothetical 8.5K !1protein (traD-traI intergenic region) SUMMARY #length 75 #molecular-weight 8512 #checksum 399 SEQUENCE /// ENTRY C64162 #type complete TITLE hypothetical protein HI0948 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 08-Oct-1999 ACCESSIONS C64162 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession C64162 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-77 ##label TIGR !'##cross-references GB:U32776; GB:L42023; NID:g1573969; !1PIDN:AAC22609.1; PID:g1573973; TIGR:HI0948 !'##note best homolog was a hypothetical protein from Escherichia coli CLASSIFICATION #superfamily Escherichia coli plasmid F hypothetical 8.5K !1protein (traD-traI intergenic region) SUMMARY #length 77 #molecular-weight 8881 #checksum 2519 SEQUENCE /// ENTRY QQPSHT #type complete TITLE hypothetical protein merT - Pseudomonas aeruginosa transposon Tn501 ORGANISM #formal_name Pseudomonas aeruginosa DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 24-Sep-1999 ACCESSIONS A04457 REFERENCE A03556 !$#authors Misra, T.K.; Brown, N.L.; Fritzinger, D.C.; Pridmore, R.D.; !1Barnes, W.M.; Haberstroh, L.; Silver, S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:5975-5979 !$#title Mercuric ion-resistance operons of plasmid R100 and !1transposon Tn501: the beginning of the operon including the !1regulatory region and the first two structural genes. !$#cross-references MUID:85014891; PMID:6091128 !$#accession A04457 !'##molecule_type DNA !'##residues 1-116 ##label MIS !'##cross-references GB:Z00027; GB:K00031; GB:K01725; GB:X01297; !1GB:X03406; NID:g43714; PIDN:CAA77321.1; PID:g43716 GENETICS !$#gene merT CLASSIFICATION #superfamily merT protein KEYWORDS transmembrane protein SUMMARY #length 116 #molecular-weight 12498 #checksum 732 SEQUENCE /// ENTRY QQEBHT #type complete TITLE hypothetical protein merT - Shigella flexneri plasmid R100 ORGANISM #formal_name Shigella flexneri DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 22-Oct-1999 ACCESSIONS A04458 REFERENCE A03556 !$#authors Misra, T.K.; Brown, N.L.; Fritzinger, D.C.; Pridmore, R.D.; !1Barnes, W.M.; Haberstroh, L.; Silver, S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:5975-5979 !$#title Mercuric ion-resistance operons of plasmid R100 and !1transposon Tn501: the beginning of the operon including the !1regulatory region and the first two structural genes. !$#cross-references MUID:85014891; PMID:6091128 !$#accession A04458 !'##molecule_type DNA !'##residues 1-116 ##label MIS !'##cross-references GB:J01730; NID:g151742; PIDN:AAA92261.1; !1PID:g151750 GENETICS !$#gene merT !$#genome plasmid CLASSIFICATION #superfamily merT protein SUMMARY #length 116 #molecular-weight 12521 #checksum 3070 SEQUENCE /// ENTRY QQPSHC #type complete TITLE hypothetical protein merC - Pseudomonas aeruginosa transposon Tn501 ORGANISM #formal_name Pseudomonas aeruginosa DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 28-May-1999 ACCESSIONS A04459 REFERENCE A03556 !$#authors Misra, T.K.; Brown, N.L.; Fritzinger, D.C.; Pridmore, R.D.; !1Barnes, W.M.; Haberstroh, L.; Silver, S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:5975-5979 !$#title Mercuric ion-resistance operons of plasmid R100 and !1transposon Tn501: the beginning of the operon including the !1regulatory region and the first two structural genes. !$#cross-references MUID:85014891; PMID:6091128 !$#accession A04459 !'##molecule_type DNA !'##residues 1-60 ##label MIS !'##cross-references GB:K02503; NID:g154897; PIDN:AAA27432.1; !1PID:g154898 GENETICS !$#gene merC CLASSIFICATION #superfamily merC protein SUMMARY #length 60 #molecular-weight 6575 #checksum 1800 SEQUENCE /// ENTRY QQEBHC #type complete TITLE hypothetical protein merC - Shigella flexneri plasmid R100 ORGANISM #formal_name Shigella flexneri DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 28-May-1999 ACCESSIONS A04460 REFERENCE A03556 !$#authors Misra, T.K.; Brown, N.L.; Fritzinger, D.C.; Pridmore, R.D.; !1Barnes, W.M.; Haberstroh, L.; Silver, S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1984) 81:5975-5979 !$#title Mercuric ion-resistance operons of plasmid R100 and !1transposon Tn501: the beginning of the operon including the !1regulatory region and the first two structural genes. !$#cross-references MUID:85014891; PMID:6091128 !$#accession A04460 !'##molecule_type DNA !'##residues 1-60 ##label MIS !'##cross-references GB:J01730; NID:g151742; PIDN:AAA92260.1; !1PID:g151749 GENETICS !$#gene merC !$#genome plasmid CLASSIFICATION #superfamily merC protein SUMMARY #length 60 #molecular-weight 6456 #checksum 232 SEQUENCE /// ENTRY QQSABE #type complete TITLE hypothetical protein B-111 - Staphylococcus aureus plasmid pE194 ORGANISM #formal_name Staphylococcus aureus DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 10-Sep-1999 ACCESSIONS A04487 REFERENCE A91790 !$#authors Horinouchi, S.; Weisblum, B. !$#journal J. Bacteriol. (1982) 150:804-814 !$#title Nucleotide sequence and functional map of pE194, a plasmid !1that specifies inducible resistance to macrolide, !1lincosamide, and streptogramin type B antibiotics. !$#cross-references MUID:82167187; PMID:6279574 !$#accession A04487 !'##molecule_type DNA !'##residues 1-111 ##label HOR GENETICS !$#genome plasmid CLASSIFICATION #superfamily Staphylococcus aureus plasmid pE194 !1hypothetical 13.3K protein SUMMARY #length 111 #molecular-weight 13305 #checksum 8755 SEQUENCE /// ENTRY QQSACE #type complete TITLE hypothetical protein C-102 - Staphylococcus aureus plasmid pE194 ORGANISM #formal_name Staphylococcus aureus DATE 18-Aug-1982 #sequence_revision 15-Oct-1982 #text_change 10-Sep-1999 ACCESSIONS A04488 REFERENCE A91790 !$#authors Horinouchi, S.; Weisblum, B. !$#journal J. Bacteriol. (1982) 150:804-814 !$#title Nucleotide sequence and functional map of pE194, a plasmid !1that specifies inducible resistance to macrolide, !1lincosamide, and streptogramin type B antibiotics. !$#cross-references MUID:82167187; PMID:6279574 !$#accession A04488 !'##molecule_type DNA !'##residues 1-102 ##label HOR GENETICS !$#genome plasmid !$#start_codon GTG CLASSIFICATION #superfamily Staphylococcus aureus plasmid pE194 !1hypothetical 12.4K protein SUMMARY #length 102 #molecular-weight 12362 #checksum 4873 SEQUENCE /// ENTRY QQSA7C #type complete TITLE hypothetical protein E-74 - Staphylococcus aureus plasmid pC194 ORGANISM #formal_name Staphylococcus aureus DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 10-Sep-1999 ACCESSIONS A04489 REFERENCE A91791 !$#authors Horinouchi, S.; Weisblum, B. !$#journal J. Bacteriol. (1982) 150:815-825 !$#title Nucleotide sequence and functional map of pC194, a plasmid !1that specifies inducible chloramphenicol resistance. !$#cross-references MUID:82167188; PMID:6950931 !$#accession A04489 !'##molecule_type DNA !'##residues 1-74 ##label HOR GENETICS !$#genome plasmid CLASSIFICATION #superfamily Staphylococcus aureus plasmid pC194 !1hypothetical 8.7K protein SUMMARY #length 74 #molecular-weight 8667 #checksum 7505 SEQUENCE /// ENTRY QQSACC #type complete TITLE hypothetical protein C-120 - Staphylococcus aureus plasmid pC194 ORGANISM #formal_name Staphylococcus aureus DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 10-Sep-1999 ACCESSIONS A04490 REFERENCE A91791 !$#authors Horinouchi, S.; Weisblum, B. !$#journal J. Bacteriol. (1982) 150:815-825 !$#title Nucleotide sequence and functional map of pC194, a plasmid !1that specifies inducible chloramphenicol resistance. !$#cross-references MUID:82167188; PMID:6950931 !$#accession A04490 !'##molecule_type DNA !'##residues 1-120 ##label HOR GENETICS !$#genome plasmid CLASSIFICATION #superfamily Staphylococcus aureus plasmid pC194 !1hypothetical 14.6K protein SUMMARY #length 120 #molecular-weight 14619 #checksum 5067 SEQUENCE /// ENTRY QQSAEC #type complete TITLE replication initiation protein E-229 - Staphylococcus aureus plasmid pC194 CONTAINS DNA ligase (EC 6.5.1.-); DNA lyase (EC 4.2.99.-) ORGANISM #formal_name Staphylococcus aureus DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 20-Apr-2000 ACCESSIONS A04491 REFERENCE A91791 !$#authors Horinouchi, S.; Weisblum, B. !$#journal J. Bacteriol. (1982) 150:815-825 !$#title Nucleotide sequence and functional map of pC194, a plasmid !1that specifies inducible chloramphenicol resistance. !$#cross-references MUID:82167188; PMID:6950931 !$#accession A04491 !'##molecule_type DNA !'##residues 1-229 ##label HOR GENETICS !$#genome plasmid CLASSIFICATION #superfamily Staphylococcus aureus plasmid pC194 !1hypothetical 27.5K protein KEYWORDS carbon-oxygen lyase; ligase FEATURE !$214 #active_site Tyr (covalent DNA-binding) #status !8predicted SUMMARY #length 229 #molecular-weight 27546 #checksum 6751 SEQUENCE /// ENTRY QQSA8T #type complete TITLE hypothetical protein B-189 - Staphylococcus aureus plasmid pT181 ORGANISM #formal_name Staphylococcus aureus DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 10-Sep-1999 ACCESSIONS A04493 REFERENCE A03510 !$#authors Khan, S.A.; Novick, R.P. !$#journal Plasmid (1983) 10:251-259 !$#title Complete nucleotide sequence of pT181, a !1tetracycline-resistance plasmid from Staphylococcus aureus. !$#cross-references MUID:84095990; PMID:6657777 !$#accession A04493 !'##molecule_type DNA !'##residues 1-189 ##label KHA GENETICS !$#genome plasmid CLASSIFICATION #superfamily Staphylococcus aureus plasmid pT181 !1hypothetical 22K protein SUMMARY #length 189 #molecular-weight 21985 #checksum 5283 SEQUENCE /// ENTRY QQSAA2 #type complete TITLE rlx protein - Staphylococcus aureus plasmid pC221 ALTERNATE_NAMES hypothetical protein A ORGANISM #formal_name Staphylococcus aureus DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 23-Jul-1999 ACCESSIONS A04494; S40421 REFERENCE A91033 !$#authors Brenner, D.G.; Shaw, W.V. !$#journal EMBO J. (1985) 4:561-568 !$#title The use of synthetic oligonucleotides with universal !1templates for rapid DNA sequencing: results with !1staphylococcal replicon pC21. !$#cross-references MUID:85257490; PMID:3860383 !$#accession A04494 !'##molecule_type DNA !'##residues 1-315 ##label BRE !'##cross-references GB:X02166; NID:g46545; PIDN:CAA26106.1; PID:g46549 !'##note the authors translated the codon TAT for residue 209 as Trp REFERENCE S40418 !$#authors Projan, S.J.; Kornblum, J.; Moghazeh, S.L.; Edelman, I.; !1Gennaro, M.L.; Novick, R.P. !$#journal Mol. Gen. Genet. (1985) 199:452-464 !$#title Comparative sequence and functional analysis of pT181 and !1pC221, cognate plasmid replicons from Staphylococcus aureus. !$#cross-references MUID:85295465; PMID:2993795 !$#accession S40421 !'##molecule_type DNA !'##residues 1-218,'PWTNTRLAI' ##label PRO !'##cross-references EMBL:X02529 GENETICS !$#gene rlx !$#genome plasmid CLASSIFICATION #superfamily rlx protein SUMMARY #length 315 #molecular-weight 36445 #checksum 3520 SEQUENCE /// ENTRY QQSAC2 #type complete TITLE hypothetical protein C - Staphylococcus aureus plasmid pC221 ORGANISM #formal_name Staphylococcus aureus DATE 28-May-1986 #sequence_revision 28-May-1986 #text_change 10-Sep-1999 ACCESSIONS A04495; S40422; S40418 REFERENCE A91033 !$#authors Brenner, D.G.; Shaw, W.V. !$#journal EMBO J. (1985) 4:561-568 !$#title The use of synthetic oligonucleotides with universal !1templates for rapid DNA sequencing: results with !1staphylococcal replicon pC21. !$#cross-references MUID:85257490; PMID:3860383 !$#accession A04495 !'##molecule_type DNA !'##residues 1-230 ##label BRE REFERENCE S40418 !$#authors Projan, S.J.; Kornblum, J.; Moghazeh, S.L.; Edelman, I.; !1Gennaro, M.L.; Novick, R.P. !$#journal Mol. Gen. Genet. (1985) 199:452-464 !$#title Comparative sequence and functional analysis of pT181 and !1pC221, cognate plasmid replicons from Staphylococcus aureus. !$#cross-references MUID:85295465; PMID:2993795 !$#accession S40422 !'##molecule_type DNA !'##residues 1-90 ##label PRW !'##cross-references EMBL:X02529 !$#accession S40418 !'##molecule_type DNA !'##residues 91-230 ##label PRO !'##cross-references EMBL:X02529; NID:g46630; PIDN:CAA26365.1; !1PID:g809754 GENETICS !$#genome plasmid CLASSIFICATION #superfamily Staphylococcus aureus plasmid pC221 !1hypothetical protein C SUMMARY #length 230 #molecular-weight 26839 #checksum 4269 SEQUENCE /// ENTRY QQMX3 #type complete TITLE hypothetical protein 3 - Methanococcus vannielii ORGANISM #formal_name Methanococcus vannielii DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 10-Sep-1999 ACCESSIONS S06626 REFERENCE S06620 !$#authors Lechner, K.; Heller, G.; Boeck, A. !$#journal J. Mol. Evol. (1989) 29:20-27 !$#title Organization and nucleotide sequence of a transcriptional !1unit of Methanococcus vannielii comprising genes for protein !1synthesis elongation factors and ribosomal proteins. !$#cross-references MUID:89362493; PMID:2475640 !$#accession S06626 !'##molecule_type DNA !'##residues 1-132 ##label LEC !'##cross-references EMBL:X15972; NID:g44787; PIDN:CAA34094.1; !1PID:g44789 CLASSIFICATION #superfamily Methanococcus vannielii hypothetical 15.3K !1protein SUMMARY #length 132 #molecular-weight 15288 #checksum 3163 SEQUENCE /// ENTRY QQHSNB #type complete TITLE hypothetical protein NAB - Halobacterium salinarum (strain cutirubrum) ORGANISM #formal_name Halobacterium salinarum #variety strain cutirubrum DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 20-Oct-2000 ACCESSIONS S04117 REFERENCE S04116 !$#authors Shimmin, L.C.; Dennis, P.P. !$#journal EMBO J. (1989) 8:1225-1235 !$#title Characterization of the L11, L1, L10 and L12 equivalent !1ribosomal protein gene cluster of the halophilic !1archaebacterium Halobacterium cutirubrum. !$#cross-references MUID:89305527; PMID:2743981 !$#accession S04117 !'##molecule_type DNA !'##residues 1-68 ##label SHI !'##cross-references EMBL:X15078; NID:g43449; PIDN:CAA33177.1; !1PID:g43451 !'##note the source is designated as Halobacterium cutirubrum CLASSIFICATION #superfamily hypothetical protein NAB SUMMARY #length 68 #molecular-weight 7539 #checksum 2249 SEQUENCE /// ENTRY QQMX4 #type complete TITLE hypothetical protein 4 - Methanococcus vannielii ORGANISM #formal_name Methanococcus vannielii DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 10-Sep-1999 ACCESSIONS S06627 REFERENCE S06620 !$#authors Lechner, K.; Heller, G.; Boeck, A. !$#journal J. Mol. Evol. (1989) 29:20-27 !$#title Organization and nucleotide sequence of a transcriptional !1unit of Methanococcus vannielii comprising genes for protein !1synthesis elongation factors and ribosomal proteins. !$#cross-references MUID:89362493; PMID:2475640 !$#accession S06627 !'##molecule_type DNA !'##residues 1-97 ##label LEC !'##cross-references EMBL:X15972; NID:g44787; PIDN:CAA34095.1; !1PID:g44790 CLASSIFICATION #superfamily Methanococcus vannielii hypothetical 10.9K !1protein SUMMARY #length 97 #molecular-weight 10893 #checksum 9398 SEQUENCE /// ENTRY H64316 #type complete TITLE conserved hypothetical protein MJ0136 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 17-Jul-1998 #sequence_revision 17-Jul-1998 #text_change 21-Jul-2000 ACCESSIONS H64316 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession H64316 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-361 ##label BUL !'##cross-references GB:U67470; GB:L77117; NID:g2826247; !1PIDN:AAB98117.1; PID:g1498904; TIGR:MJ0136 GENETICS !$#map_position FOR131469-132554 CLASSIFICATION #superfamily conserved hypothetical protein MJ0136 SUMMARY #length 361 #molecular-weight 40824 #checksum 8604 SEQUENCE /// ENTRY D69027 #type complete TITLE conserved hypothetical protein MTH1201 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 17-Jul-1998 #sequence_revision 17-Jul-1998 #text_change 23-Jul-1999 ACCESSIONS D69027 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession D69027 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-377 ##label MTH !'##cross-references GB:AE000888; GB:AE000666; NID:g2622304; !1PIDN:AAB85690.1; PID:g2622310 !'##experimental_source strain Delta H GENETICS !$#gene MTH1201 CLASSIFICATION #superfamily conserved hypothetical protein MJ0136 SUMMARY #length 377 #molecular-weight 42984 #checksum 9738 SEQUENCE /// ENTRY A69264 #type complete TITLE conserved hypothetical protein AF0113 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 17-Jul-1998 #sequence_revision 17-Jul-1998 #text_change 23-Jul-1999 ACCESSIONS A69264 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession A69264 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-359 ##label KLE !'##cross-references GB:AE001098; GB:AE000782; NID:g2689421; !1PIDN:AAB91114.1; PID:g2650530; TIGR:AF0113 CLASSIFICATION #superfamily conserved hypothetical protein MJ0136 SUMMARY #length 359 #molecular-weight 40559 #checksum 5892 SEQUENCE /// ENTRY H69281 #type complete TITLE conserved hypothetical protein AF0256 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 17-Jul-1998 #sequence_revision 17-Jul-1998 #text_change 23-Jul-1999 ACCESSIONS H69281 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession H69281 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-373 ##label KLE !'##cross-references GB:AE001088; GB:AE000782; NID:g2689411; !1PIDN:AAB90975.1; PID:g2650382; TIGR:AF0256 CLASSIFICATION #superfamily conserved hypothetical protein MJ0136 SUMMARY #length 373 #molecular-weight 43043 #checksum 9851 SEQUENCE /// ENTRY QQQYAW #type complete TITLE hypothetical protein A - Pyrococcus woesei ORGANISM #formal_name Pyrococcus woesei DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 10-Sep-1999 ACCESSIONS S10652 REFERENCE S10650 !$#authors Zwickl, P.; Fabry, S.; Bogedain, C.; Haas, A.; Hensel, R. !$#journal J. Bacteriol. (1990) 172:4329-4338 !$#title Glyceraldehyde-3-phosphate dehydrogenase from the !1hyperthermophilic archaebacterium Pyrococcus woesei: !1characterization of the enzyme, cloning and sequencing of !1the gene, and expression in Escherichia coli. !$#cross-references MUID:90330536; PMID:2165475 !$#accession S10652 !'##molecule_type DNA !'##residues 1-222 ##label ZWI CLASSIFICATION #superfamily Pyrococcus woesei hypothetical 24.8K protein SUMMARY #length 222 #molecular-weight 24755 #checksum 5694 SEQUENCE /// ENTRY QQQYBW #type complete TITLE hypothetical protein B - Pyrococcus woesei ORGANISM #formal_name Pyrococcus woesei DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 10-Sep-1999 ACCESSIONS S10654 REFERENCE S10650 !$#authors Zwickl, P.; Fabry, S.; Bogedain, C.; Haas, A.; Hensel, R. !$#journal J. Bacteriol. (1990) 172:4329-4338 !$#title Glyceraldehyde-3-phosphate dehydrogenase from the !1hyperthermophilic archaebacterium Pyrococcus woesei: !1characterization of the enzyme, cloning and sequencing of !1the gene, and expression in Escherichia coli. !$#cross-references MUID:90330536; PMID:2165475 !$#accession S10654 !'##molecule_type DNA !'##residues 1-99 ##label ZWI CLASSIFICATION #superfamily Pyrococcus horikoshii hypothetical protein !1PHS036 SUMMARY #length 99 #molecular-weight 11386 #checksum 1350 SEQUENCE /// ENTRY QQAG1T #type complete TITLE hypothetical protein 1 - Agrobacterium tumefaciens plasmid pTiAch5 ORGANISM #formal_name Agrobacterium tumefaciens DATE 13-Aug-1986 #sequence_revision 13-Aug-1986 #text_change 10-Sep-1999 ACCESSIONS A04496 REFERENCE A91001 !$#authors Gielen, J.; De Beuckeleer, M.; Seurinck, J.; Deboeck, F.; De !1Greve, H.; Lemmers, M.; Van Montagu, M.; Schell, J. !$#journal EMBO J. (1984) 3:835-846 !$#title The complete nucleotide sequence of the TL-DNA of the !1Agrobacterium tumefaciens plasmid pTiAch5. !$#cross-references MUID:84207942; PMID:6327292 !$#accession A04496 !'##molecule_type DNA !'##residues 1-226 ##label GIE GENETICS !$#genome plasmid CLASSIFICATION #superfamily Agrobacterium tumefaciens plasmid pTiAch5 !1hypothetical protein 1 SUMMARY #length 226 #molecular-weight 25766 #checksum 2839 SEQUENCE /// ENTRY Q7AGOT #type complete TITLE hypothetical protein 7 - Agrobacterium tumefaciens plasmids ORGANISM #formal_name Agrobacterium tumefaciens DATE 20-Sep-1984 #sequence_revision 20-Sep-1984 #text_change 10-Sep-1999 ACCESSIONS A93506; A90978; S28685; A04500 REFERENCE A93506 !$#authors McPherson, J.C. !$#journal Nucleic Acids Res. (1984) 12:2317-2325 !$#title DNA sequence analysis of crown gall tumor T-DNA encoding the !10.7kb transcript. !$#cross-references MUID:84169535; PMID:6324113 !$#accession A93506 !'##molecule_type DNA !'##residues 1-126 ##label MCP !'##cross-references GB:X00431; NID:g39150; PIDN:CAA25129.1; PID:g39151 !'##experimental_source plasmid pTiA6 A6S/2 tumor line REFERENCE A90978 !$#authors Dhaese, P.; De Greve, H.; Gielen, J.; Seurinck, J.; Van !1Montagu, M.; Schell, J. !$#journal EMBO J. (1983) 2:419-426 !$#title Identification of sequences involved in the polyadenylation !1of higher plant nuclear transcripts using Agrobacterium !1T-DNA genes as models. !$#contents Ach5 !$#accession A90978 !'##molecule_type DNA !'##residues 1-126 ##label DHA !'##experimental_source plasmid pTiA5 REFERENCE S28683 !$#authors Barker, R.F.; Idler, K.B.; Thompson, D.V.; Kemp, J.D. !$#journal Plant Mol. Biol. (1983) 2:335-350 !$#title Nucleotide sequence of the T-DNA region from the !1Agrobacterium tumefaciens octopine Ti plasmid pTi15955. !$#accession S28685 !'##status translation not shown !'##molecule_type DNA !'##residues 1-126 ##label BAR !'##cross-references EMBL:X00493; NID:g39062; PIDN:CAA25165.1; !1PID:g39065 !'##experimental_source plasmid pTi15955 GENETICS !$#genome plasmid CLASSIFICATION #superfamily Agrobacterium tumefaciens plasmids hypothetical !1protein 7 SUMMARY #length 126 #molecular-weight 14350 #checksum 9434 SEQUENCE /// ENTRY QQBYPT #type complete TITLE hypothetical protein YER152c - yeast (Saccharomyces cerevisiae) ORGANISM #formal_name Saccharomyces cerevisiae DATE 30-Jun-1991 #sequence_revision 12-May-1995 #text_change 19-Apr-2002 ACCESSIONS S50655; C36328; S05725; S12290 REFERENCE S50430 !$#authors Dietrich, F.S. !$#submission submitted to the EMBL Data Library, December 1994 !$#description The sequence of S. cerevisiae cosmids 8229, 9115, 9132, !19981, and lambda clones 7990 and 6134. !$#accession S50655 !'##molecule_type DNA !'##residues 1-443 ##label DIE !'##cross-references EMBL:U18917; NID:g603377; PIDN:AAB64679.1; !1PID:g603392; GSPDB:GN00005; MIPS:YER152c REFERENCE A36328 !$#authors Ohmen, J.D.; Burke, K.A.; McEwen, J.E. !$#journal Mol. Cell. Biol. (1990) 10:3027-3035 !$#title Divergent overlapping transcripts at the PET122 locus in !1Saccharomyces cerevisiae. !$#cross-references MUID:90258894; PMID:2160592 !$#accession C36328 !'##molecule_type DNA !'##residues 1-230 ##label OHM !'##cross-references GB:X07558; NID:g4127; PIDN:CAA30440.1; PID:g4129 REFERENCE S05724 !$#authors Ohmen, J.D.; Kloeckener-Gruissem, B.; McEwen, J.E. !$#journal Nucleic Acids Res. (1988) 16:10783-10802 !$#title Molecular cloning and nucleotide sequence of the nuclear !1PET122 gene required for expression of the mitochondrial !1COX3 gene in S. cerevisae. !$#cross-references MUID:89083497; PMID:2849752 !$#accession S05725 !'##molecule_type DNA !'##residues 1-56,'CGA',60-61,63-66,'V',68-72,'T',74-76,'R',78-86,'V', !188-122,'SDQQ',128-132,'DSRENDRHQRA',145,'PRLD',150-152,'YV', !1155-230 ##label OH2 !'##cross-references EMBL:X07558 !'##note this sequence has been revised in reference A36328 GENETICS !$#gene MIPS:YER152c !'##cross-references SGD:S0000954 !$#map_position 5R CLASSIFICATION #superfamily yeast hypothetical protein YER152c SUMMARY #length 443 #molecular-weight 49490 #checksum 8378 SEQUENCE /// ENTRY PDBYB #type complete TITLE REP1 protein - yeast (Saccharomyces cerevisiae) (strain A364A D5) 2-mu plasmid ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Oct-1980 #sequence_revision 23-Oct-1981 #text_change 21-Jul-2000 ACCESSIONS A04503; B93695 REFERENCE A93232 !$#authors Hartley, J.L.; Donelson, J.E. !$#journal Nature (1980) 286:860-864 !$#title Nucleotide sequence of the yeast plasmid. !$#cross-references MUID:81012161; PMID:6251374 !$#accession A04503 !'##molecule_type DNA !'##residues 1-373 ##label HAR !'##cross-references GB:J01347; NID:g4182; PIDN:CAA24632.1; PID:g4183 !'##experimental_source strain A364A D5 REFERENCE A93695 !$#authors Hindley, J.; Phear, G.A. !$#journal Nucleic Acids Res. (1979) 7:361-375 !$#title Sequence of 1019 nucleotides encompassing one of the !1inverted repeats from the yeast 2 mu plasmid. !$#cross-references MUID:80034481; PMID:386282 !$#accession B93695 !'##molecule_type DNA !'##residues 330-373 ##label HIN GENETICS !$#gene REP1 !$#genome 2-mu plasmid CLASSIFICATION #superfamily yeast REP1 protein KEYWORDS plasmid partition SUMMARY #length 373 #molecular-weight 43231 #checksum 2037 SEQUENCE /// ENTRY PDBYC #type complete TITLE REP2 protein - yeast (Saccharomyces cerevisiae) plasmid ALTERNATE_NAMES hypothetical protein C ORGANISM #formal_name Saccharomyces cerevisiae DATE 31-Oct-1980 #sequence_revision 23-Oct-1981 #text_change 21-Jul-2000 ACCESSIONS A04504 REFERENCE A93232 !$#authors Hartley, J.L.; Donelson, J.E. !$#journal Nature (1980) 286:860-864 !$#title Nucleotide sequence of the yeast plasmid. !$#cross-references MUID:81012161; PMID:6251374 !$#accession A04504 !'##molecule_type DNA !'##residues 1-296 ##label HAR !'##cross-references GB:J01347; NID:g4182; PIDN:CAA24633.1; PID:g4184 !'##experimental_source strain A364A D5 GENETICS !$#genome plasmid CLASSIFICATION #superfamily yeast REP2 protein KEYWORDS plasmid partition SUMMARY #length 296 #molecular-weight 33196 #checksum 6596 SEQUENCE /// ENTRY COSJS #type complete TITLE 1G2 protein - bracket fungus (Schizophyllum commune) ORGANISM #formal_name Schizophyllum commune DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 31-Dec-1993 ACCESSIONS A04506 REFERENCE A04506 !$#authors Dons, J.J.M.; Mulder, G.H.; Rouwendal, G.J.A.; Springer, J.; !1Bremer, W.; Wessels, J.G.H. !$#journal EMBO J. (1984) 3:2101-2106 !$#title Sequence analysis of a split gene involved in fruiting from !1the fungus Schizophyllum commune. !$#accession A04506 !'##molecule_type DNA !'##residues 1-94 ##label DON COMMENT This protein is encoded by one of the genes that are !1abundantly expressed during formation of fruiting bodies. !1The exact function of the protein in the fruiting process is !1not yet known. GENETICS !$#introns 40/3; 65/2 CLASSIFICATION #superfamily 1G2 protein SUMMARY #length 94 #molecular-weight 9853 #checksum 9635 SEQUENCE /// ENTRY BWBY #type complete TITLE CBP2 protein - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YHL038c ORGANISM #formal_name Saccharomyces cerevisiae DATE 18-Apr-1984 #sequence_revision 02-Dec-1994 #text_change 12-Nov-1999 ACCESSIONS S48930; A04507 REFERENCE S46794 !$#authors Favello, T. !$#submission submitted to the EMBL Data Library, June 1994 !$#description The sequence of S. cerevisiae cosmid 9196. !$#accession S48930 !'##molecule_type DNA !'##residues 1-630 ##label FAV !'##cross-references EMBL:U11583; NID:g2289854; PIDN:AAB65050.1; !1PID:g2289867; GSPDB:GN00008; MIPS:YHL038c REFERENCE A04507 !$#authors McGraw, P.; Tzagoloff, A. !$#journal J. Biol. Chem. (1983) 258:9459-9468 !$#title Assembly of the mitochondrial membrane system. !1Characterization of a yeast nuclear gene involved in the !1processing of the cytochrome b pre-mRNA. !$#cross-references MUID:83265749; PMID:6348045 !$#accession A04507 !'##molecule_type DNA !'##residues 1-45,'D',47-64,'N',66-489,'S',491-630 ##label MCG !'##cross-references EMBL:K00138 GENETICS !$#gene SGD:CBP2; MIPS:YHL038c !'##cross-references SGD:S0001030; MIPS:YHL038c !$#map_position 8L FUNCTION !$#description required for the splicing of the terminal intron of the !1cytochrome b pre-mRNA CLASSIFICATION #superfamily CBP2 protein KEYWORDS pre-mRNA splicing SUMMARY #length 630 #molecular-weight 73860 #checksum 9838 SEQUENCE /// ENTRY A8BYD #type complete TITLE ADE8 protein - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YDR408c ORGANISM #formal_name Saccharomyces cerevisiae DATE 28-Dec-1987 #sequence_revision 28-Dec-1987 #text_change 21-Jul-2000 ACCESSIONS A22316; S69690; A05011 REFERENCE A93359 !$#authors White, J.H.; Lusnak, K.; Fogel, S. !$#journal Nature (1985) 315:350-352 !$#title Mismatch-specific post-meiotic segregation frequency in !1yeast suggests a heteroduplex recombination intermediate. !$#cross-references MUID:85213852; PMID:3889658 !$#accession A22316 !'##molecule_type DNA !'##residues 1-214 ##label WHI !'##cross-references EMBL:M36585; NID:g171014; PIDN:AAA34406.1; !1PID:g171015 REFERENCE S69665 !$#authors Dietrich, F.S. !$#submission submitted to the EMBL Data Library, July 1995 !$#description The sequence of S. cerevisiae cosmids 9481, 9509, 9926, !19461, and lambda 3641. !$#accession S69690 !'##molecule_type DNA !'##residues 1-214 ##label DIE !'##cross-references EMBL:U32274; NID:g927313; PIDN:AAB64848.1; !1PID:g927339; GSPDB:GN00004; MIPS:YDR408c GENETICS !$#gene SGD:ADE8; MIPS:YDR408c !'##cross-references SGD:S0002816; MIPS:YDR408c !$#map_position 4R CLASSIFICATION #superfamily ade8 protein; phosphoribosylglycinamide !1formyltransferase homology FEATURE !$4-214 #domain phosphoribosylglycinamide formyltransferase !8homology #label PRGF SUMMARY #length 214 #molecular-weight 23540 #checksum 5328 SEQUENCE /// ENTRY MRBY #type complete TITLE mRNA maturase bI3 - yeast (Saccharomyces cerevisiae) mitochondrion ALTERNATE_NAMES cytochrome b mRNA maturase 3 ORGANISM #formal_name mitochondrion Saccharomyces cerevisiae DATE 31-Mar-1981 #sequence_revision 19-Feb-1984 #text_change 07-Dec-1999 ACCESSIONS A04505; B38011 REFERENCE A00159 !$#authors Nobrega, F.G.; Tzagoloff, A. !$#journal J. Biol. Chem. (1980) 255:9828-9837 !$#title Assembly of the mitochondrial membrane system. DNA sequence !1and organization of the cytochrome b gene in Saccharomyces !1cerevisiae D273-10B. !$#cross-references MUID:81046788; PMID:6253454 !$#accession A04505 !'##molecule_type DNA !'##residues 1-19 ##label NOB !'##cross-references EMBL:V00696 !'##experimental_source strain D273-10B/A21 REFERENCE A38011 !$#authors Lazowska, J.; Jacq, C.; Slonimski, P.P. !$#journal Cell (1980) 22:333-348 !$#title Sequence of introns and flanking exons in wild-type and box3 !1mutants of cytochrome b reveals an interlaced splicing !1protein coded by an intron. !$#cross-references MUID:81088336; PMID:7004642 !$#accession B38011 !'##molecule_type DNA !'##residues 20-423 ##label LAZ !'##cross-references EMBL:V00686; NID:g13513; PIDN:CAA24057.1; !1PID:g13515 !'##experimental_source strain 777-3A !'##note the authors translated the codon ATA which occurs 24 times in !1the coding region according to the standard code GENETICS !$#genome mitochondrion !$#genetic_code SGC2 !$#introns 120/1 CLASSIFICATION #superfamily mRNA maturase bI3; cytochrome b homology; !1cytochrome b6 homology KEYWORDS mitochondrion FEATURE !$10-143 #domain cytochrome b homology #status atypical #label !8CBH\ !$10-143 #domain cytochrome b6 homology #status atypical !8#label CB6 SUMMARY #length 423 #molecular-weight 49332 #checksum 1834 SEQUENCE /// ENTRY QXASBI #type complete TITLE mRNA maturase bi1 - Emericella nidulans mitochondrion ALTERNATE_NAMES cobA intron protein ORGANISM #formal_name mitochondrion Emericella nidulans, Aspergillus nidulans DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 07-Dec-1999 ACCESSIONS A04513; A37516 REFERENCE A00157 !$#authors Waring, R.B.; Davies, R.W.; Lee, S.; Grisi, E.; Berks, M.M.; !1Scazzocchio, C. !$#journal Cell (1981) 27:4-11 !$#title The mosaic organization of the apocytochrome b gene of !1Aspergillus nidulans revealed by DNA sequencing. !$#cross-references MUID:82115341; PMID:7034966 !$#accession A04513 !'##molecule_type DNA !'##residues 1-237 ##label WA1 !'##cross-references GB:J01388; GB:J01389; GB:V00651; GB:V00652; !1NID:g336901 !'##experimental_source imperfect stage !'##note this ORF is not annotated in GenBank entry EMEMTCYB2, release !1106.0 REFERENCE A37516 !$#authors Waring, R.B.; Davies, R.W.; Scazzocchio, C.; Brown, T.A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1982) 79:6332-6336 !$#title Internal structure of a mitochondrial intron of Aspergillus !1nidulans. !$#cross-references MUID:83065170; PMID:6755468 !$#accession A37516 !'##molecule_type DNA !'##residues 161-488 ##label WA2 !'##cross-references GB:J01387; NID:g336899 !'##experimental_source imperfect stage !'##note this ORF is not annotated in GenBank entry EMEMTCOBA, release !1106.0 GENETICS !$#genome mitochondrion !$#genetic_code SGC3 CLASSIFICATION #superfamily Emericella mRNA maturase bI1; cytochrome b !1homology; cytochrome b6 homology KEYWORDS mitochondrion FEATURE !$1-168 #region cytochrome b exon encoded\ !$10-168 #domain cytochrome b homology (fragment) #label CBH\ !$10-168 #domain cytochrome b6 homology (fragment) #label CB6\ !$169-488 #region cytochrome b intron encoded SUMMARY #length 488 #molecular-weight 55394 #checksum 9690 SEQUENCE /// ENTRY QQBY2M #type complete TITLE mRNA maturase bI4 - yeast (Saccharomyces cerevisiae) mitochondrion ALTERNATE_NAMES gene cob intron 4 protein; intron-encoded protein bI4 ORGANISM #formal_name mitochondrion Saccharomyces cerevisiae DATE 31-Dec-1980 #sequence_revision 29-Jan-1999 #text_change 19-Apr-2002 ACCESSIONS S78666; S78667; S72691; A04512; S26761; B30101 REFERENCE S78634 !$#authors Foury, F.; Roganti, T.; Lecrenier, N.; Purnelle, B. !$#submission submitted to the Protein Sequence Database, December 1998 !$#accession S78666 !'##molecule_type DNA !'##residues 1-638 ##label FOU1 !'##cross-references EMBL:AJ011856; MIPS:Q0120 !'##experimental_source strain FY1679, isogenic derivative of strain !1S288C REFERENCE Z13743 !$#authors Foury, F.; Roganti, T.; Lecrenier, N.; Purnelle, B. !$#journal FEBS Lett. (1998) 440:325-331 !$#title The complete sequence of the mitochondrial genome of !1Saccharomyces cerevisiae. !$#cross-references MUID:99087401; PMID:9872396 !$#accession S78667 !'##molecule_type DNA !'##residues 1-638 ##label FOU2 !'##cross-references EMBL:AJ011856; NID:g4160362; PIDN:CAA09837.1; !1PID:g4160379 !'##experimental_source strain FY1679, isogenic derivative of strain !1S288C REFERENCE S72681 !$#authors de Zamaroczy, M.; Bernardi, G. !$#journal Gene (1986) 47:155-177 !$#title The primary structure of the mitochondrial genome of !1Saccharomyces cerevisiae - a review. !$#cross-references MUID:87163488; PMID:3549452 !$#accession S72691 !'##status translation not shown !'##molecule_type DNA !'##residues 'MCNY',165,'NIKS',170-369,'E',371-458,'T',460-638 ##label !1DEZ !'##cross-references EMBL:L36899; PIDN:AAA67535.1 !'##note this is not the original publication REFERENCE A00159 !$#authors Nobrega, F.G.; Tzagoloff, A. !$#journal J. Biol. Chem. (1980) 255:9828-9837 !$#title Assembly of the mitochondrial membrane system. DNA sequence !1and organization of the cytochrome b gene in Saccharomyces !1cerevisiae D273-10B. !$#cross-references MUID:81046788; PMID:6253454 !$#accession A04512 !'##molecule_type DNA !'##residues 255-369,'E',371-458,'T',460-638 ##label NOB !'##cross-references GB:J01476; GB:V00696; NID:g13534; PIDN:CAB43023.1; !1PID:g4837716 !'##experimental_source strain D273-10B !'##note the authors translated the codon ATA for residues 158, 184, !1222, 225, 310, and 355 according to the standard code REFERENCE S26761 !$#authors Goguel, V.; Delahodde, A.; Jacq, C. !$#journal Mol. Cell. Biol. (1992) 12:696-705 !$#title Connections between RNA splicing and DNA intron mobility in !1yeast mitochondria: RNA maturase and DNA endonuclease !1switching experiments. !$#cross-references MUID:92123194; PMID:1310149 !$#accession S26761 !'##molecule_type DNA !'##residues 385-432,'K',434-464,'K',466-638 ##label GOG !'##cross-references GB:S76640; NID:g243422; PIDN:AAB21125.1; !1PID:g243423 REFERENCE A30101 !$#authors Delahodde, A.; Goguel, V.; Becam, A.M.; Creusot, F.; Perea, !1J.; Banroques, J.; Jacq, C. !$#journal Cell (1989) 56:431-441 !$#title Site-specific DNA endonuclease and RNA maturase activities !1of two homologous intron-encoded proteins from yeast !1mitochondria. !$#cross-references MUID:89119565; PMID:2536593 !$#accession B30101 !'##molecule_type DNA !'##residues 385-432,'K',434-464,'K',466-511,'S',513-514,'V',516-585, !1'L',587-638 ##label DEL GENETICS !$#gene SGD:BI4; SCBI4 !'##cross-references SGD:S0007273 !$#map_position 72.7-74.3 !$#genome mitochondrion !$#genetic_code SGC2 CLASSIFICATION #superfamily yeast mRNA maturase bI4; COI intron 9 protein !1homology; cytochrome b6 homology KEYWORDS mitochondrion FEATURE !$10-210 #domain cytochrome b6 homology #label CB6\ !$407-635 #domain COI intron 9 protein homology #label CI9 SUMMARY #length 638 #molecular-weight 74580 #checksum 7401 SEQUENCE /// ENTRY QXBY31 #type complete TITLE gene cox1 intron 1 protein - yeast (Saccharomyces cerevisiae) mitochondrion (strain D273-10B) ALTERNATE_NAMES gene oxi3 intron 1 protein ORGANISM #formal_name mitochondrion Saccharomyces cerevisiae #variety strain D273-10B DATE 15-Nov-1984 #sequence_revision 15-Nov-1984 #text_change 08-Sep-2000 ACCESSIONS A04508 REFERENCE A92267 !$#authors Bonitz, S.G.; Coruzzi, G.; Thalenfeld, B.E.; Tzagoloff, A.; !1Macino, G. !$#journal J. Biol. Chem. (1980) 255:11927-11941 !$#title Assembly of the mitochondrial membrane system. Structure and !1nucleotide sequence of the gene coding for subunit 1 of !1yeast cytochrome oxidase. !$#cross-references MUID:81069885; PMID:6254986 !$#accession A04508 !'##molecule_type DNA !'##residues 1-834 ##label BON !'##cross-references EMBL:V00694 !'##experimental_source strain D273-10B !'##note the authors translated the codon ATA for residue 834 according !1to the standard code GENETICS !$#map_position 43.7-47.2 !$#genome mitochondrion !$#genetic_code SGC2 CLASSIFICATION #superfamily yeast mitochondrion oxi3 intron 1 protein KEYWORDS mitochondrion FEATURE !$1-56 #region cox1 exon 1 encoded\ !$57-834 #region cox1 intron encoded SUMMARY #length 834 #molecular-weight 96045 #checksum 7921 SEQUENCE /// ENTRY QXBY32 #type complete TITLE gene cox1 intron 2 protein - yeast (Saccharomyces cerevisiae) mitochondrion (strain D273-10B) ALTERNATE_NAMES gene oxi3 intron 2 protein ORGANISM #formal_name mitochondrion Saccharomyces cerevisiae #variety strain D273-10B DATE 15-Nov-1984 #sequence_revision 15-Nov-1984 #text_change 08-Sep-2000 ACCESSIONS A04509 REFERENCE A92267 !$#authors Bonitz, S.G.; Coruzzi, G.; Thalenfeld, B.E.; Tzagoloff, A.; !1Macino, G. !$#journal J. Biol. Chem. (1980) 255:11927-11941 !$#title Assembly of the mitochondrial membrane system. Structure and !1nucleotide sequence of the gene coding for subunit 1 of !1yeast cytochrome oxidase. !$#cross-references MUID:81069885; PMID:6254986 !$#accession A04509 !'##molecule_type DNA !'##residues 1-789 ##label BON !'##cross-references EMBL:V00694 !'##experimental_source strain D273-10B !'##note we have reassigned the boundaries of intron 1 by homology with !1other cytochrome-c oxidase chain I sequences. As a result, !1the authors' translation differs from the sequence shown in !1lacking 57-Val GENETICS !$#map_position 43.7-50.7 !$#genome mitochondrion !$#genetic_code SGC2 !$#introns 57/1 CLASSIFICATION #superfamily yeast mitochondrion oxi3 intron 1 protein KEYWORDS mitochondrion FEATURE !$1-68 #region cox1 exon 1 and 2 encoded\ !$69-789 #region cox1 intron 2 encoded SUMMARY #length 789 #molecular-weight 90815 #checksum 9531 SEQUENCE /// ENTRY QXBY33 #type complete TITLE oxi3 intron 3 protein - yeast (Saccharomyces cerevisiae) mitochondrion ORGANISM #formal_name mitochondrion Saccharomyces cerevisiae DATE 15-Nov-1984 #sequence_revision 15-Nov-1984 #text_change 07-Dec-1999 ACCESSIONS A04510 REFERENCE A92267 !$#authors Bonitz, S.G.; Coruzzi, G.; Thalenfeld, B.E.; Tzagoloff, A.; !1Macino, G. !$#journal J. Biol. Chem. (1980) 255:11927-11941 !$#title Assembly of the mitochondrial membrane system. Structure and !1nucleotide sequence of the gene coding for subunit 1 of !1yeast cytochrome oxidase. !$#cross-references MUID:81069885; PMID:6254986 !$#accession A04510 !'##molecule_type DNA !'##residues 1-378 ##label BON !'##cross-references EMBL:V00694 !'##experimental_source strain D273-10B !'##note we have reassigned the boundaries of introns 1, 2 by homology !1with other cytochrome-c oxidase chain I sequences; the !1authors' translation differs from the sequence shown in !1lacking 57-Val, in having 69-Cys, and in having an !1additional Thr after 69-Cys GENETICS !$#map_position 43.7-52.4 !$#genome mitochondrion !$#genetic_code SGC2 !$#introns 57/1; 69/1 CLASSIFICATION #superfamily yeast mitochondrion oxi3 intron 3 protein KEYWORDS mitochondrion FEATURE !$1-81 #domain cytochrome-c oxidase chain I (exons 1 to 3) !8#label EXN SUMMARY #length 378 #molecular-weight 44226 #checksum 7707 SEQUENCE /// ENTRY QXBY34 #type complete TITLE DNA endonuclease I-SceII - yeast (Saccharomyces cerevisiae) mitochondrion ALTERNATE_NAMES DNA endonuclease aI4; gene oxi3 intron 4 protein; intron-encoded protein aI4; protein Q0065 ORGANISM #formal_name mitochondrion Saccharomyces cerevisiae DATE 15-Nov-1984 #sequence_revision 24-Mar-1999 #text_change 30-Jun-2001 ACCESSIONS S78649; A04511; S72688; S26763; C30101; A30101; S26762; !1S78648 REFERENCE Z13743 !$#authors Foury, F.; Roganti, T.; Lecrenier, N.; Purnelle, B. !$#journal FEBS Lett. (1998) 440:325-331 !$#title The complete sequence of the mitochondrial genome of !1Saccharomyces cerevisiae. !$#cross-references MUID:99087401; PMID:9872396 !$#accession S78649 !'##molecule_type DNA !'##residues 1-556 ##label FOU !'##cross-references EMBL:AJ011856; NID:g4160362; PIDN:CAA09828.1; !1PID:g4160370; MIPS:Q0065 !'##experimental_source strain FY1679, isogenic derivative of strain !1S288C REFERENCE A92267 !$#authors Bonitz, S.G.; Coruzzi, G.; Thalenfeld, B.E.; Tzagoloff, A.; !1Macino, G. !$#journal J. Biol. Chem. (1980) 255:11927-11941 !$#title Assembly of the mitochondrial membrane system. Structure and !1nucleotide sequence of the gene coding for subunit 1 of !1yeast cytochrome oxidase. !$#cross-references MUID:81069885; PMID:6254986 !$#accession A04511 !'##molecule_type DNA !'##residues 82-223,'A',225-456,'KT',459-556 ##label BON !'##cross-references EMBL:V00694; NID:g13523 !'##experimental_source strain D273-10B !'##note we have reassigned the boundaries of introns 1, 2 by homology !1with other cytochrome-c oxidase chain I sequences; the !1authors' translation differs from the sequence shown in !1lacking 57-Val, in having 69-Cys, and in having an !1additional Thr after 69-Cys !'##note the authors translated the codon ATA for residue 87 according !1to the standard code REFERENCE S72681 !$#authors de Zamaroczy, M.; Bernardi, G. !$#journal Gene (1986) 47:155-177 !$#title The primary structure of the mitochondrial genome of !1Saccharomyces cerevisiae - a review. !$#cross-references MUID:87163488; PMID:3549452 !$#accession S72688 !'##status translation not shown !'##molecule_type DNA !'##residues 241-456,'KT',459-556 ##label DEZ !'##cross-references EMBL:L36897; NID:g559273; PIDN:AAA67532.1 !'##note this is not the original publication REFERENCE S26761 !$#authors Goguel, V.; Delahodde, A.; Jacq, C. !$#journal Mol. Cell. Biol. (1992) 12:696-705 !$#title Connections between RNA splicing and DNA intron mobility in !1yeast mitochondria: RNA maturase and DNA endonuclease !1switching experiments. !$#cross-references MUID:92123194; PMID:1310149 !$#accession S26763 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 299-556 ##label GOG !'##cross-references GB:S76641; NID:g243424 !'##experimental_source strain 777-3A !'##note the translated sequence in GenBank entry S76641, release 114, !1(PIDN:AAB21126.1) differs from the published sequence !'##note the sequence from Fig. 2 shows 315-Ile and 320-Ile, which !1results from the transfer of the mitochondrial gene to the !1cytosol without modification of the corresponding codons REFERENCE A30101 !$#authors Delahodde, A.; Goguel, V.; Becam, A.M.; Creusot, F.; Perea, !1J.; Banroques, J.; Jacq, C. !$#journal Cell (1989) 56:431-441 !$#title Site-specific DNA endonuclease and RNA maturase activities !1of two homologous intron-encoded proteins from yeast !1mitochondria. !$#cross-references MUID:89119565; PMID:2536593 !$#accession C30101 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type DNA !'##residues 299-314,'I',316-319,'I',321-556 ##label DEL !'##experimental_source strain 777-3A GENETICS !$#gene mim2 !$#map_position 43.7-55.1 !$#genome mitochondrion !$#genetic_code SGC2 !$#introns 138/1; 150/1; 162/3 !$#note MIPS:Q0065 CLASSIFICATION #superfamily DNA endonuclease I-SceII; COI intron 9 protein !1homology; cytochrome-c oxidase chain I homology KEYWORDS endonuclease; mitochondrion FEATURE !$82-240 #region cox1 exons 1 to 4 encoded\ !$241-556 #region cox 1 intron encoded\ !$327-553 #domain COI intron 9 protein homology #label CI9 SUMMARY #length 556 #molecular-weight 63311 #checksum 220 SEQUENCE /// ENTRY QQBY3M #type complete TITLE hypothetical protein (oxiI 3' region) - yeast (Saccharomyces cerevisiae) mitochondrion ORGANISM #formal_name mitochondrion Saccharomyces cerevisiae DATE 18-Aug-1982 #sequence_revision 19-Feb-1984 #text_change 07-Dec-1999 ACCESSIONS A04514 REFERENCE A04514 !$#authors Coruzzi, G.; Bonitz, S.G.; Thalenfeld, B.E.; Tzagoloff, A. !$#journal J. Biol. Chem. (1981) 256:12780-12787 !$#title Assembly of the mitochondrial membrane system. Analysis of !1the nucleotide sequence and the transcripts in the oxi1 !1region of yeast mitochondrial DNA. !$#cross-references MUID:82075797; PMID:7031051 !$#accession A04514 !'##molecule_type DNA !'##residues 1-386 ##label COR !'##cross-references EMBL:J01485 !'##experimental_source strain D273-10B/A21 !'##note the nucleotides coding for residues 4, 295, and 296 are !1uncertain; the nucleotide sequence coding for residues 295 !1and 296 may contain one or two extra nucleotides; thus, the !1sequence after residue 294 may have been translated in the !1wrong reading frame !'##note the authors translated the codon GAA for residue 39 as Gly !'##note the authors translated the codon ATA for residues 30, 44, 47, !159, 94, 96, 103, 123, 133, 222, 253, 257, 312, 324, 334, !1357, and 379 according to the standard code GENETICS !$#map_position 15.7-17.4 !$#genome mitochondrion !$#genetic_code SGC2 CLASSIFICATION #superfamily yeast mitochondrion oxiI 3' region hypothetical !1protein KEYWORDS mitochondrion SUMMARY #length 386 #molecular-weight 45607 #checksum 3962 SEQUENCE /// ENTRY QQBY1M #type complete TITLE mRNA maturase-related protein (21S rRNA intron) - yeast (Saccharomyces cerevisiae) mitochondrion ALTERNATE_NAMES 21S rRNA intron protein; protein Q0160 CONTAINS endonuclease ORGANISM #formal_name mitochondrion Saccharomyces cerevisiae DATE 31-Dec-1980 #sequence_revision 19-Feb-1984 #text_change 21-Jul-2000 ACCESSIONS A23170; A04515; S25392; S78678; S78679 REFERENCE A23170 !$#authors Jacquier, A.; Dujon, B. !$#journal Cell (1985) 41:383-394 !$#title An intron-encoded protein is active in a gene conversion !1process that spreads an intron into a mitochondrial gene. !$#cross-references MUID:85176962; PMID:3886163 !$#accession A23170 !'##molecule_type DNA !'##residues 1-235 ##label JAC !'##cross-references EMBL:X00149 REFERENCE A04515 !$#authors Dujon, B. !$#journal Cell (1980) 20:185-197 !$#title Sequence of the intron and flanking exons of the !1mitochondrial 21S rRNA gene of yeast strains having !1different alleles at the omega and rib-1 loci. !$#cross-references MUID:80222854; PMID:6156002 !$#accession A04515 !'##molecule_type DNA !'##residues 1-235 ##label DUJ !'##cross-references GB:V00684; NID:g13509; PIDN:CAA24055.1; PID:g13510 !'##note the authors translated the codon CTT for residues 123 and 156 !1as Leu, CTA for residue 55 as Leu, and ATA for residues 10, !1136, 143, 203, and 221 as Ile REFERENCE S25392 !$#authors Colleaux, L.; d'Auriol, L.; Betermier, M.; Cottarel, G.; !1Jacquier, A.; Galibert, F.; Dujon, B. !$#journal Cell (1986) 44:521-533 !$#title Universal code equivalent of a yeast mitochondrial intron !1reading frame is expressed into E. coli as a specific double !1strand endonuclease. !$#cross-references MUID:86133545; PMID:3004738 !$#accession S25392 !'##molecule_type DNA !'##residues 1-122,'L',124-155,'L',157-235 ##label COL !'##cross-references EMBL:M12278 REFERENCE S78634 !$#authors Foury, F.; Roganti, T.; Lecrenier, N.; Purnelle, B. !$#submission submitted to the Protein Sequence Database, December 1998 !$#accession S78678 !'##molecule_type DNA !'##residues 1-235 ##label FOU1 !'##cross-references EMBL:AJ011856; MIPS:Q0160 !'##experimental_source strain FY1679, isogenic derivative of strain !1S288C REFERENCE Z13743 !$#authors Foury, F.; Roganti, T.; Lecrenier, N.; Purnelle, B. !$#journal FEBS Lett. (1998) 440:325-331 !$#title The complete sequence of the mitochondrial genome of !1Saccharomyces cerevisiae. !$#cross-references MUID:99087401; PMID:9872396 !$#accession S78679 !'##molecule_type DNA !'##residues 1-235 ##label FOU2 !'##cross-references EMBL:AJ011856; NID:g4160362; PIDN:CAA09843.1; !1PID:g4160385 !'##experimental_source strain FY1679, isogenic derivative of strain !1S288C GENETICS !$#genome mitochondrion !$#genetic_code SGC2 CLASSIFICATION #superfamily yeast 21S rRNA intron mRNA maturase-related !1protein KEYWORDS mitochondrion SUMMARY #length 235 #molecular-weight 27683 #checksum 9651 SEQUENCE /// ENTRY QXASD #type complete TITLE hypothetical protein D - Emericella nidulans mitochondrion ORGANISM #formal_name mitochondrion Emericella nidulans, Aspergillus nidulans DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 07-Dec-1999 ACCESSIONS F93436; D94593; A04517 REFERENCE A93436 !$#authors Netzker, R.; Kochel, H.G.; Basak, N.; Kuntzel, H. !$#journal Nucleic Acids Res. (1982) 10:4783-4794 !$#title Nucleotide sequence of Aspergillus nidulans mitochondrial !1genes coding for ATPase subunit 6, cytochrome oxidase !1subunit 3, seven unidentified proteins, four tRNAs and !1L-rRNA. !$#cross-references MUID:83038633; PMID:6290989 !$#accession F93436 !'##molecule_type DNA !'##residues 1-14,'Q',16-27 ##label NET !'##experimental_source imperfect stage !'##note this sequence has been revised in reference A94593 REFERENCE A94593 !$#authors Lazarus, C.M.; Kuntzel, H. !$#submission submitted to the Atlas, March 1984 !$#accession D94593 !'##molecule_type DNA !'##residues 1-27 ##label LAZ GENETICS !$#genome mitochondrion !$#genetic_code SGC3 CLASSIFICATION #superfamily Emericella mitochondrion hypothetical protein D KEYWORDS mitochondrion SUMMARY #length 27 #molecular-weight 3514 #checksum 8686 SEQUENCE /// ENTRY QXASF #type complete TITLE hypothetical protein F - Emericella nidulans mitochondrion ORGANISM #formal_name mitochondrion Emericella nidulans, Aspergillus nidulans DATE 14-Nov-1983 #sequence_revision 14-Nov-1983 #text_change 07-Dec-1999 ACCESSIONS A04518 REFERENCE A93436 !$#authors Netzker, R.; Kochel, H.G.; Basak, N.; Kuntzel, H. !$#journal Nucleic Acids Res. (1982) 10:4783-4794 !$#title Nucleotide sequence of Aspergillus nidulans mitochondrial !1genes coding for ATPase subunit 6, cytochrome oxidase !1subunit 3, seven unidentified proteins, four tRNAs and !1L-rRNA. !$#cross-references MUID:83038633; PMID:6290989 !$#accession A04518 !'##molecule_type DNA !'##residues 1-48 ##label NET !'##cross-references GB:J01390; NID:g336905; PIDN:AAA99211.1; !1PID:g472825 !'##experimental_source imperfect stage GENETICS !$#genome mitochondrion !$#genetic_code SGC3 CLASSIFICATION #superfamily Emericella mitochondrion hypothetical protein F KEYWORDS mitochondrion SUMMARY #length 48 #molecular-weight 5628 #checksum 515 SEQUENCE /// ENTRY Q3YCRQ #type fragment TITLE hypothetical protein (recA 3' region) - Synechococcus sp. (strain PCC 7002) (fragment) ORGANISM #formal_name Synechococcus sp. DATE 30-Sep-1990 #sequence_revision 30-Jun-1991 #text_change 23-Jul-1999 ACCESSIONS B35120 REFERENCE A35120 !$#authors Murphy, R.C.; Gasparich, G.E.; Bryant, D.A.; Porter, R.D. !$#journal J. Bacteriol. (1990) 172:967-976 !$#title Nucleotide sequence and further characterization of the !1Synechococcus sp. strain PCC 7002 recA gene: complementation !1of a cyanobacterial recA mutation by the Escherichia coli !1recA gene. !$#cross-references MUID:90130334; PMID:2105307 !$#accession B35120 !'##molecule_type DNA !'##residues 1-256 ##label MUR !'##cross-references GB:M29495; NID:g154601; PIDN:AAA88637.1; !1PID:g1196960 CLASSIFICATION #superfamily Synechococcus recA 3' region hypothetical !1protein; tetratricopeptide repeat homology FEATURE !$43-76 #domain tetratricopeptide repeat homology #label TT1\ !$77-110 #domain tetratricopeptide repeat homology #label TT2\ !$111-144 #domain tetratricopeptide repeat homology #label TT3\ !$145-178 #domain tetratricopeptide repeat homology #label TT4\ !$179-212 #domain tetratricopeptide repeat homology #label TT5 SUMMARY #length 256 #checksum 4262 SEQUENCE /// ENTRY QQKWTA #type complete TITLE hypothetical 32K protein - Caenorhabditis elegans transposon Tc1 ORGANISM #formal_name Caenorhabditis elegans DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 05-Nov-1999 ACCESSIONS A04520; T32084 REFERENCE A93476 !$#authors Rosenzweig, B.; Liao, L.W.; Hirsh, D. !$#journal Nucleic Acids Res. (1983) 11:4201-4209 !$#title Sequence of the Caenorhabditis elegans transposable element !1Tc1. !$#cross-references MUID:83246543; PMID:6306578 !$#accession A04520 !'##molecule_type DNA !'##residues 1-273 ##label ROS !'##cross-references GB:X01005; NID:g6887; PIDN:CAA25498.1; PID:g6888 REFERENCE Z21121 !$#authors Lamar, B.; Wamsley, P.; Twyman, B. !$#submission submitted to the EMBL Data Library, July 1997 !$#description The sequence of C. elegans cosmid T07D3. !$#accession T32084 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-273 ##label LAM !'##cross-references EMBL:AF016682; PIDN:AAB66191.1; GSPDB:GN00020; !1CESP:T07D3.8 !'##experimental_source strain Bristol N2; clone T07D3 GENETICS !$#gene CESP:T07D3.8 !$#map_position 2 CLASSIFICATION #superfamily Caenorhabditis transposon Tc1 hypothetical 32K !1protein SUMMARY #length 273 #molecular-weight 31820 #checksum 1430 SEQUENCE /// ENTRY QQKWTB #type complete TITLE hypothetical 12K protein - Caenorhabditis elegans transposon Tc1 ORGANISM #formal_name Caenorhabditis elegans DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 23-Jul-1999 ACCESSIONS A04521 REFERENCE A93476 !$#authors Rosenzweig, B.; Liao, L.W.; Hirsh, D. !$#journal Nucleic Acids Res. (1983) 11:4201-4209 !$#title Sequence of the Caenorhabditis elegans transposable element !1Tc1. !$#cross-references MUID:83246543; PMID:6306578 !$#accession A04521 !'##molecule_type DNA !'##residues 1-112 ##label ROS !'##cross-references GB:X01005; NID:g6887; PIDN:CAA25499.1; PID:g6889 CLASSIFICATION #superfamily Caenorhabditis transposon Tc1 hypothetical 12K !1protein SUMMARY #length 112 #molecular-weight 12249 #checksum 5771 SEQUENCE /// ENTRY QQZMCA #type complete TITLE hypothetical protein Ac9 - maize transposon Ac9 ORGANISM #formal_name Zea mays #common_name maize DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 23-Aug-1997 ACCESSIONS A04522 REFERENCE A90848 !$#authors Pohlman, R.F.; Fedoroff, N.V.; Messing, J. !$#journal Cell (1984) 37:635-643 !$#title The nucleotide sequence of the maize controlling element !1activator. !$#cross-references MUID:84205699; PMID:6327080 !$#accession A04522 !'##molecule_type DNA !'##residues 1-210 ##label POH CLASSIFICATION #superfamily maize transposon Ac9 23K protein SUMMARY #length 210 #molecular-weight 23009 #checksum 566 SEQUENCE /// ENTRY QIZMI #type complete TITLE hypothetical protein C-123 - maize chloroplast ORGANISM #formal_name chloroplast Zea mays #common_name maize DATE 18-Aug-1982 #sequence_revision 18-Aug-1982 #text_change 23-Aug-1997 ACCESSIONS A04524 REFERENCE A04524 !$#authors Koch, W.; Edwards, K.; Kossel, H. !$#journal Cell (1981) 25:203-213 !$#title Sequencing of the 16S-23S spacer in a ribosomal RNA operon !1of Zea mays chloroplast DNA reveals two split tRNA genes. !$#cross-references MUID:82002211; PMID:7023695 !$#accession A04524 !'##molecule_type DNA !'##residues 1-123 ##label KOC !'##note this protein is coded by a portion of the tRNA-Ile intron GENETICS !$#genome chloroplast CLASSIFICATION #superfamily maize trnI intron hypothetical protein KEYWORDS chloroplast SUMMARY #length 123 #molecular-weight 13992 #checksum 8773 SEQUENCE /// ENTRY QQEGC4 #type complete TITLE psbC intron protein - Euglena gracilis chloroplast ALTERNATE_NAMES hypothetical protein 458 (psbC 3' region) ORGANISM #formal_name chloroplast Euglena gracilis DATE 31-Mar-1989 #sequence_revision 31-Mar-1989 #text_change 23-Jul-1999 ACCESSIONS JT0170; S34869; S34502 REFERENCE JT0170 !$#authors Montandon, P.E.; Vasserot, A.; Stutz, E. !$#journal Curr. Genet. (1986) 11:35-39 !$#title Euglena gracilis chloroplast DNA: analysis of a 1.6 kb !1intron of the psb C gene containing an open reading frame of !1458 codons. !$#cross-references MUID:88194657; PMID:3129199 !$#accession JT0170 !'##molecule_type DNA !'##residues 1-458 ##label MON !'##cross-references GB:X04509; NID:g18017; PIDN:CAA28194.1; PID:g18019 REFERENCE S34862 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.R.; !1Monfort, A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#journal Nucleic Acids Res. (1993) 21:3537-3544 !$#title Complete sequence of Euglena gracilis chloroplast DNA. !$#cross-references MUID:93347989; PMID:8346031 !$#accession S34869 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-458 ##label HAL2 !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50081.1; !1PID:g415737 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1993 GENETICS !$#genome chloroplast CLASSIFICATION #superfamily Euglena psbC intron protein KEYWORDS chloroplast SUMMARY #length 458 #molecular-weight 54385 #checksum 4020 SEQUENCE /// ENTRY QQFB #type complete TITLE hypothetical basic polypeptide - kidney bean ORGANISM #formal_name Phaseolus vulgaris #common_name kidney bean DATE 28-Aug-1985 #sequence_revision 28-Aug-1985 #text_change 23-Aug-1997 ACCESSIONS A04525; B27350 REFERENCE A03365 !$#authors Hoffman, L.M. !$#journal J. Mol. Appl. Genet. (1984) 2:447-453 !$#title Structure of a chromosomal Phaseolus vulgaris lectin gene !1and its transcript. !$#cross-references MUID:85008540; PMID:6090563 !$#accession A04525 !'##molecule_type DNA !'##residues 1-58 ##label HOF1 !'##experimental_source cv. Tendergreen REFERENCE A27350 !$#authors Hoffman, L.M.; Ma, Y.; Barker, R.F. !$#journal Nucleic Acids Res. (1982) 10:7819-7828 !$#title Molecular cloning of Phaseolus vulgaris lectin mRNA and use !1of cDNA as a probe to estimate lectin transcript levels in !1various tissues. !$#cross-references MUID:83116994; PMID:6897567 !$#accession B27350 !'##status preliminary !'##molecule_type mRNA !'##residues 1-58 ##label HOF2 !'##cross-references GB:J01261 !'##experimental_source cv. Tendergreen CLASSIFICATION #superfamily Phaseolus hypothetical basic polypeptide SUMMARY #length 58 #molecular-weight 6859 #checksum 9836 SEQUENCE /// ENTRY QXFF71 #type complete TITLE hypothetical 51K protein - fruit fly (Drosophila melanogaster) transposon 17.6 ORGANISM #formal_name Drosophila melanogaster DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 23-Jul-1999 ACCESSIONS A03325 REFERENCE A93349 !$#authors Saigo, K.; Kugimiya, W.; Matsuo, Y.; Inouye, S.; Yoshioka, !1K.; Yuki, S. !$#journal Nature (1984) 312:659-661 !$#title Identification of the coding sequence for a reverse !1transcriptase-like enzyme in a transposable genetic element !1in Drosophila melanogaster. !$#cross-references MUID:85061628; PMID:6209583 !$#accession A03325 !'##molecule_type DNA !'##residues 1-439 ##label SAI !'##cross-references GB:X01472; GB:J01060; GB:J01061; NID:g8142; !1PIDN:CAA25701.1; PID:g8143 GENETICS !$#gene FlyBase:17.6 !'##cross-references FlyBase:FBgn0000004 CLASSIFICATION #superfamily Drosophila transposon 17.6 51K protein SUMMARY #length 439 #molecular-weight 51586 #checksum 6987 SEQUENCE /// ENTRY QXFF73 #type complete TITLE hypothetical 53K protein - fruit fly (Drosophila melanogaster) transposon 17.6 ORGANISM #formal_name Drosophila melanogaster DATE 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 23-Aug-1997 ACCESSIONS A03326 REFERENCE A93349 !$#authors Saigo, K.; Kugimiya, W.; Matsuo, Y.; Inouye, S.; Yoshioka, !1K.; Yuki, S. !$#journal Nature (1984) 312:659-661 !$#title Identification of the coding sequence for a reverse !1transcriptase-like enzyme in a transposable genetic element !1in Drosophila melanogaster. !$#cross-references MUID:85061628; PMID:6209583 !$#accession A03326 !'##molecule_type DNA !'##residues 1-456 ##label SAI GENETICS !$#gene FlyBase:17.6 !'##cross-references FlyBase:FBgn0000004 CLASSIFICATION #superfamily Drosophila transposon 17.6 53K protein SUMMARY #length 456 #molecular-weight 53419 #checksum 6327 SEQUENCE /// ENTRY S06119 #type complete TITLE membrane protein patched - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 21-Jul-2000 ACCESSIONS S06119; A33468 REFERENCE S06119 !$#authors Nakano, Y.; Guerrero, I.; Hidalgo, A.; Taylor, A.; Whittle, !1J.R.S.; Ingham, P.W. !$#journal Nature (1989) 341:508-513 !$#title A protein with several possible membrane-spanning domains !1encoded by the Drosophila segment polarity gene patched. !$#cross-references MUID:90015164; PMID:2797178 !$#accession S06119 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-1299 ##label NAK !'##cross-references GB:X17558; NID:g8389; PIDN:CAA35591.1; PID:g8390 REFERENCE A33468 !$#authors Hooper, J.E.; Scott, M.P. !$#journal Cell (1989) 59:751-765 !$#title The Drosophila patched gene encodes a putative membrane !1protein required for segmental patterning. !$#cross-references MUID:90058658; PMID:2582494 !$#accession A33468 !'##status preliminary; nucleic acid sequence not shown; not compared !1with conceptual translation !'##molecule_type mRNA !'##residues 1-110,'R',112-273,'G',275-331,'R',333-635,'P',637-861, !1'DVF',878,'Y',880-1299 ##label HOO !'##cross-references GB:M28418; GB:M28999; NID:g552097; PID:g552099 GENETICS !$#gene FlyBase:ptc !'##cross-references FlyBase:FBgn0003892 !$#map_position 2 44D3-D4 CLASSIFICATION #superfamily Drosophila membrane protein patched KEYWORDS glycoprotein; transmembrane protein FEATURE !$74-92 #domain transmembrane #status predicted #label TM01\ !$427-448 #domain transmembrane #status predicted #label TM02\ !$456-503 #domain transmembrane #status predicted #label TM03\ !$529-555 #domain transmembrane #status predicted #label TM04\ !$557-585 #domain transmembrane #status predicted #label TM05\ !$677-699 #domain transmembrane #status predicted #label TM06\ !$967-1017 #domain transmembrane #status predicted #label TM07\ !$1019-1047 #domain transmembrane #status predicted #label TM08\ !$1061-1086 #domain transmembrane #status predicted #label TM09\ !$1093-1121 #domain transmembrane #status predicted #label TM10\ !$142,298,335,388, !$807,861,1194,1271 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 1299 #molecular-weight 144091 #checksum 7740 SEQUENCE /// ENTRY F64559 #type complete TITLE conserved hypothetical protein HP0318 - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS F64559 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession F64559 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-251 ##label TOM !'##cross-references GB:AE000550; GB:AE000511; NID:g2313417; !1PIDN:AAD07387.1; PID:g2313418; TIGR:HP0318 CLASSIFICATION #superfamily conserved hypothetical protein HP0318 SUMMARY #length 251 #molecular-weight 28507 #checksum 8065 SEQUENCE /// ENTRY G64014 #type complete TITLE hypothetical protein HI0854 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS G64014 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession G64014 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-253 ##label TIGR !'##cross-references GB:U32767; GB:L42023; NID:g1573868; !1PIDN:AAC22513.1; PID:g1573877; TIGR:HI0854 CLASSIFICATION #superfamily conserved hypothetical protein HP0318 SUMMARY #length 253 #molecular-weight 28840 #checksum 3721 SEQUENCE /// ENTRY E64606 #type complete TITLE conserved hypothetical integral membrane protein HP0693 - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS E64606 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession E64606 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-454 ##label TOM !'##cross-references GB:AE000582; GB:AE000511; NID:g2313812; !1PIDN:AAD07745.1; PID:g2313817; TIGR:HP0693 CLASSIFICATION #superfamily conserved hypothetical integral membrane !1protein HP0693 SUMMARY #length 454 #molecular-weight 49215 #checksum 827 SEQUENCE /// ENTRY F64013 #type complete TITLE hypothetical protein HI0772 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS F64013 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession F64013 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-447 ##label TIGR !'##cross-references GB:U32761; GB:L42023; NID:g1573780; !1PIDN:AAC22431.1; PID:g1573782; TIGR:HI0772 CLASSIFICATION #superfamily conserved hypothetical integral membrane !1protein HP0693 SUMMARY #length 447 #molecular-weight 48443 #checksum 5707 SEQUENCE /// ENTRY S28734 #type complete TITLE hypothetical protein 4 - Halobacterium salinarum phage phi-H insertion sequence ISH1.8 ORGANISM #formal_name Halobacterium salinarium phage phi-H DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 18-Jul-2001 ACCESSIONS S28734 REFERENCE S28732 !$#authors Schnabel, H.; Palm, P.; Dick, K.; Grampp, B. !$#journal EMBO J. (1984) 3:1717-1722 !$#title Sequence analysis of the insertion element ISH1.8 and of !1associated structural changes in the genome of phage Phi-H !1of the archaebacterium Halobacterium halobium. !$#accession S28734 !'##status translation not shown !'##molecule_type DNA !'##residues 1-130 ##label SCH !'##cross-references EMBL:X00805; NID:g15525; PID:g15527 !'##note the source is designated as phage Phi-H of the archaebacterium !1Halobacterium halobium GENETICS !$#mobile_element insertion sequence ISH1.8 CLASSIFICATION #superfamily conserved hypothetical protein 4 (insertion !1sequence ISH1.8) SUMMARY #length 130 #molecular-weight 14978 #checksum 703 SEQUENCE /// ENTRY F64571 #type complete TITLE hypothetical protein SARA17 - Helicobacter pylori insertion sequence IS200 ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS F64571; H64645 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession F64571 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-138 ##label TOM !'##cross-references GB:AE000557; GB:AE000511; NID:g2313514; !1PIDN:AAD07480.1; PID:g2313518; TIGR:HP0414; GB:AE000609; !1NID:g2314150; PIDN:AAD08053.1; PID:g2314152; TIGR:HP1008 !'##experimental_source strain 26695 GENETICS !$#mobile_element insertion sequence IS200 CLASSIFICATION #superfamily conserved hypothetical protein 4 (insertion !1sequence ISH1.8) SUMMARY #length 138 #molecular-weight 15965 #checksum 7702 SEQUENCE /// ENTRY B64657 #type complete TITLE conserved hypothetical secreted protein HP1098 - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS B64657 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession B64657 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-290 ##label TOM !'##cross-references GB:AE000616; GB:AE000511; NID:g2314242; !1PIDN:AAD08141.1; PID:g2314247; TIGR:HP1098 CLASSIFICATION #superfamily conserved hypothetical secreted protein HP1098 SUMMARY #length 290 #molecular-weight 31594 #checksum 5252 SEQUENCE /// ENTRY H64539 #type complete TITLE conserved hypothetical secreted protein HP0160 - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS H64539 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession H64539 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-306 ##label TOM !'##cross-references GB:AE000537; GB:AE000511; NID:g2313247; !1PIDN:AAD07230.1; PID:g2313248; TIGR:HP0160 CLASSIFICATION #superfamily conserved hypothetical secreted protein HP1098 SUMMARY #length 306 #molecular-weight 34097 #checksum 5277 SEQUENCE /// ENTRY JN0256 #type complete TITLE Sec-independent protein translocase ybeC [similarity] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS JN0256; A64797 REFERENCE JN0256 !$#authors Hayden, M.A.; Huand, I.; Bussiere, D.E.; Ashley, G.W. !$#journal J. Biol. Chem. (1992) 267:9512-9515 !$#title The biosynthesis of lipoic acid; cloning of lip, a lipoate !1biosynthetic locus of Escherichia coli. !$#cross-references MUID:92250596; PMID:1577793 !$#accession JN0256 !'##molecule_type DNA !'##residues 1-67 ##label HAY !'##cross-references GB:M82805 !'##note the authors translated the codon CAG for residue 59 as Asn REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64797 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-67 ##label BLAT !'##cross-references GB:AE000167; GB:U00096; NID:g1786836; !1PIDN:AAC73728.1; PID:g1786845; UWGP:b0627 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ybeC CLASSIFICATION #superfamily conserved hypothetical secreted protein HP0320 SUMMARY #length 67 #molecular-weight 7024 #checksum 3785 SEQUENCE /// ENTRY H64559 #type complete TITLE conserved hypothetical secreted protein HP0320 - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS H64559 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession H64559 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-79 ##label TOM !'##cross-references GB:AE000550; GB:AE000511; NID:g2313417; !1PIDN:AAD07397.1; PID:g2313428; TIGR:HP0320 CLASSIFICATION #superfamily conserved hypothetical secreted protein HP0320 SUMMARY #length 79 #molecular-weight 8722 #checksum 1943 SEQUENCE /// ENTRY S72850 #type complete TITLE hypothetical protein B2126_C1_182 - Mycobacterium leprae ORGANISM #formal_name Mycobacterium leprae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 23-Mar-2001 ACCESSIONS S72850 REFERENCE S72585 !$#authors Smith, D.R.; Robison, K. !$#submission submitted to the EMBL Data Library, November 1993 !$#description Mycobacterium leprae cosmid B2126. !$#accession S72850 !'##status preliminary !'##molecule_type DNA !'##residues 1-88 ##label SMI !'##cross-references EMBL:U00017; NID:g466994; PID:g467005 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily conserved hypothetical secreted protein HP0320 SUMMARY #length 88 #molecular-weight 9824 #checksum 3978 SEQUENCE /// ENTRY D64705 #type complete TITLE conserved hypothetical integral membrane protein HP1484 - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS D64705 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession D64705 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-148 ##label TOM !'##cross-references GB:AE000647; GB:AE000511; NID:g2314645; !1PIDN:AAD08519.1; PID:g2314656; TIGR:HP1484 CLASSIFICATION #superfamily conserved hypothetical integral membrane !1protein HP1484 SUMMARY #length 148 #molecular-weight 17159 #checksum 6934 SEQUENCE /// ENTRY S74656 #type complete TITLE hypothetical protein slr1790 - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S74656 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74656 !'##status preliminary !'##molecule_type DNA !'##residues 1-210 ##label KAN !'##cross-references EMBL:D90900; GB:AB001339; NID:g1651768; !1PIDN:BAA16808.1; PID:g1651881 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily conserved hypothetical integral membrane !1protein HP1484 SUMMARY #length 210 #molecular-weight 24063 #checksum 6811 SEQUENCE /// ENTRY D64706 #type complete TITLE conserved hypothetical nifU-like protein - Helicobacter pylori ORGANISM #formal_name Helicobacter pylori #variety strains J99, 26695 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS D64706; B71812 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession D64706 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-89 ##label TOM !'##cross-references GB:AE000648; GB:AE000511; NID:g2314670; !1PIDN:AAD08534.1; PID:g2314672; TIGR:HP1492 !'##experimental_source strain 26695 REFERENCE A71800 !$#authors Alm, R.A.; Ling, L.S.L.; Moir, D.T.; King, B.L.; Brown, !1E.D.; Doig, P.C.; Smith, D.R.; Noonan, B.; Guild, B.C.; !1deJonge, B.L.; Carmel, G.; Tummino, P.J.; Caruso, A.; !1Uria-Nickelsen, M.; Mills, D.M.; Ives, C.; Gibson, R.; !1Merberg, D.; Mills, S.D.; Jiang, Q.; Taylor, D.E.; Vovis, !1G.F.; Trust, T.J. !$#journal Nature (1999) 397:176-180 !$#title Genomic sequence comparison of two unrelated isolates of the !1human gastric pathogen Helicobacter pylori. !$#cross-references MUID:99120557; PMID:9923682 !$#accession B71812 !'##molecule_type DNA !'##residues 1-89 ##label ARN !'##cross-references GB:AE001561; GB:AE001439; NID:g4156000; !1PIDN:AAD06966.1; PID:g4156005 !'##experimental_source strain J99 GENETICS !$#gene HP1492; jhp1385 CLASSIFICATION #superfamily conserved hypothetical nifU-like protein HP1492 SUMMARY #length 89 #molecular-weight 10121 #checksum 4841 SEQUENCE /// ENTRY S76753 #type complete TITLE hypothetical protein - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S76753 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76753 !'##status preliminary !'##molecule_type DNA !'##residues 1-76 ##label KAN !'##cross-references EMBL:D90916; GB:AB001339; NID:g1653715; !1PIDN:BAA18665.1; PID:g1653754 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily conserved hypothetical nifU-like protein HP1492 SUMMARY #length 76 #molecular-weight 8374 #checksum 1161 SEQUENCE /// ENTRY S23058 #type complete TITLE gcpE protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS S23058; B65028 REFERENCE S23057 !$#authors Baker, J.; Franklin, D.B.; Parker, J. !$#journal FEMS Microbiol. Lett. (1992) 94:175-180 !$#title Sequence and characterization of the gcpE gene of !1Escherichia coli. !$#accession S23058 !'##molecule_type DNA !'##residues 1-372 ##label BAK !'##cross-references EMBL:X64451; NID:g41540; PID:g41542 !'##experimental_source strain K-12 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65028 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-372 ##label BLAT !'##cross-references GB:AE000338; GB:U00096; NID:g1788862; !1PIDN:AAC75568.1; PID:g1788863; UWGP:b2515 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene gcpE CLASSIFICATION #superfamily gcpE protein SUMMARY #length 372 #molecular-weight 40683 #checksum 6592 SEQUENCE /// ENTRY H64063 #type complete TITLE gcpE protein - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS H64063 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession H64063 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-368 ##label TIGR !'##cross-references GB:U32721; GB:L42023; NID:g1573334; !1PIDN:AAC22026.1; PID:g1573337; TIGR:HI0368 GENETICS !$#gene gcpE CLASSIFICATION #superfamily gcpE protein SUMMARY #length 368 #molecular-weight 40116 #checksum 6795 SEQUENCE /// ENTRY A64598 #type complete TITLE protein E - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS A64598 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession A64598 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-359 ##label TOM !'##cross-references GB:AE000577; GB:AE000511; NID:g2313747; !1PIDN:AAD07695.1; PID:g2313753; TIGR:HP0625 CLASSIFICATION #superfamily gcpE protein SUMMARY #length 359 #molecular-weight 39278 #checksum 3634 SEQUENCE /// ENTRY A64634 #type complete TITLE outer membrane protein (omp21) - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS A64634 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession A64634 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-529 ##label TOM !'##cross-references GB:AE000600; GB:AE000511; NID:g2314042; !1PIDN:AAD07957.1; PID:g2314047; TIGR:HP0913 CLASSIFICATION #superfamily Helicobacter pylori outer membrane protein !1omp20 SUMMARY #length 529 #molecular-weight 57062 #checksum 8368 SEQUENCE /// ENTRY H64633 #type complete TITLE outer membrane protein (omp20) - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS H64633 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession H64633 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-515 ##label TOM !'##cross-references GB:AE000600; GB:AE000511; NID:g2314042; !1PIDN:AAD07960.1; PID:g2314050; TIGR:HP0912 CLASSIFICATION #superfamily Helicobacter pylori outer membrane protein !1omp20 SUMMARY #length 515 #molecular-weight 55931 #checksum 248 SEQUENCE /// ENTRY B64664 #type complete TITLE hypothetical protein HP1154 - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS B64664 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession B64664 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-135 ##label TOM !'##cross-references GB:AE000621; GB:AE000511; NID:g2314301; !1PIDN:AAD08203.1; PID:g2314314; TIGR:HP1154 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily hypothetical protein HP1154 SUMMARY #length 135 #molecular-weight 15604 #checksum 1521 SEQUENCE /// ENTRY A64692 #type complete TITLE hypothetical protein HP1377 - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS A64692 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession A64692 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-146 ##label TOM !'##cross-references GB:AE000638; GB:AE000511; NID:g2314547; !1PIDN:AAD08427.1; PID:g2314555; TIGR:HP1377 CLASSIFICATION #superfamily hypothetical protein HP1154 SUMMARY #length 146 #molecular-weight 16873 #checksum 4711 SEQUENCE /// ENTRY D64523 #type complete TITLE conserved hypothetical secreted protein HP0028 - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS D64523 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession D64523 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-177 ##label TOM !'##cross-references GB:AE000525; GB:AE000511; NID:g2313102; !1PIDN:AAD07099.1; PID:g2313105; TIGR:HP0028 CLASSIFICATION #superfamily conserved hypothetical protein HI0453 SUMMARY #length 177 #molecular-weight 20649 #checksum 2283 SEQUENCE /// ENTRY H64007 #type complete TITLE hypothetical protein HI0453 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS H64007 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession H64007 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-174 ##label TIGR !'##cross-references GB:U32728; GB:L42023; NID:g1573425; !1PIDN:AAC22111.1; PID:g1573438; TIGR:HI0453 CLASSIFICATION #superfamily conserved hypothetical protein HI0453 SUMMARY #length 174 #molecular-weight 20416 #checksum 40 SEQUENCE /// ENTRY S73919 #type complete TITLE pet112 protein homolog - Mycoplasma pneumoniae (strain ATCC 29342) ALTERNATE_NAMES hypothetical protein G07_orf478o ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S73919 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73919 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-478 ##label HIM !'##cross-references EMBL:AE000058; GB:U00089; NID:g1674291; !1PIDN:AAB96241.1; PID:g1674295 !'##experimental_source ATCC 29342 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#gene pet112 !$#genetic_code SGC3 CLASSIFICATION #superfamily PET112 protein KEYWORDS transmembrane protein FEATURE !$53-69 #domain transmembrane #status predicted #label TMM SUMMARY #length 478 #molecular-weight 54562 #checksum 1920 SEQUENCE /// ENTRY A64211 #type complete TITLE PET112 protein homolog - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 07-Dec-1999 ACCESSIONS A64211 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession A64211 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-477 ##label TIGR !'##cross-references GB:U39689; GB:L43967; NID:g1045773; PID:g1045778; !1TIGR:MG100 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily PET112 protein KEYWORDS transmembrane protein FEATURE !$52-68 #domain transmembrane #status predicted #label TMM SUMMARY #length 477 #molecular-weight 54695 #checksum 5081 SEQUENCE /// ENTRY B64602 #type complete TITLE PET112-like protein - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS B64602 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession B64602 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-475 ##label TOM !'##cross-references GB:AE000579; GB:AE000511; NID:g2313778; !1PIDN:AAD07723.1; PID:g2313783; TIGR:HP0658 CLASSIFICATION #superfamily PET112 protein KEYWORDS transmembrane protein FEATURE !$51-67 #domain transmembrane #status predicted #label TMM SUMMARY #length 475 #molecular-weight 53288 #checksum 3460 SEQUENCE /// ENTRY S75850 #type complete TITLE pet112 protein - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein sll1435 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S75850 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75850 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-519 ##label KAN !'##cross-references EMBL:D90913; GB:AB001339; NID:g1653348; !1PIDN:BAA18309.1; PID:g1653395 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene pet112 !$#start_codon GTG CLASSIFICATION #superfamily PET112 protein KEYWORDS transmembrane protein FEATURE !$81-97 #domain transmembrane #status predicted #label TMM SUMMARY #length 519 #molecular-weight 57605 #checksum 5786 SEQUENCE /// ENTRY S45428 #type complete TITLE PET112 protein - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YBL0724; protein YBL080c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S45428; S45821; S41997; S59225; S41792 REFERENCE S45387 !$#authors Obermaier, B.; Gassenhuber, J.; Piravandi, E.; Domdey, H. !$#submission submitted to the EMBL Data Library, May 1994 !$#description Sequence analysis of a 78,6 kb segment of the left end of !1Saccaromyces cerevisiae chromosome II. !$#accession S45428 !'##molecule_type DNA !'##residues 1-541 ##label OBE !'##cross-references EMBL:X79489; NID:g496661; PID:g496701 REFERENCE S45816 !$#authors Domdey, H.; Gassenhuber, H.; Obermaier, B.; Piravandi, E. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S45821 !'##molecule_type DNA !'##residues 1-541 ##label DOM !'##cross-references EMBL:Z35841; NID:g536128; PID:g536129; !1GSPDB:GN00002; MIPS:YBL080c REFERENCE S41997 !$#authors Mulero, J.J.; Rosenthal, J.K.; Fox, T.D. !$#journal Curr. Genet. (1994) 25:299-304 !$#title PET112, a Saccharomyces cerevisiae nuclear gene required to !1maintain rho(+) mitochondrial DNA. !$#cross-references MUID:94363744; PMID:8082172 !$#accession S41997 !'##molecule_type DNA !'##residues 1-414,'P',416-541 ##label MUL !'##cross-references EMBL:L22072; NID:g347492; PIDN:AAC37508.1; !1PID:g347493 REFERENCE S59184 !$#authors Obermaier, B.; Gassenhuber, J.; Piravandi, E.; Domdey, H. !$#journal Yeast (1995) 11:1103-1112 !$#title Sequence analysis of a 78.6 kb segment of the left end of !1Saccharomyces cerevisiae chromosome II. !$#cross-references MUID:96076635; PMID:7502586 !$#accession S59225 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-541 ##label OBW !'##cross-references EMBL:X79489; NID:g496661; PIDN:CAA56028.1; !1PID:g496701 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1May 1994 GENETICS !$#gene SGD:PET112; MIPS:YBL080c !'##cross-references SGD:S0000176; MIPS:YBL080c !$#map_position 2L FUNCTION !$#description involved in mitochondrial gene expression, probably in !1translation CLASSIFICATION #superfamily PET112 protein KEYWORDS mitochondrion; transmembrane protein FEATURE !$77-93 #domain transmembrane #status predicted #label TMM SUMMARY #length 541 #molecular-weight 61842 #checksum 7244 SEQUENCE /// ENTRY B64623 #type complete TITLE lipopolysaccharide biosynthesis-associated protein lex2B - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS B64623 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession B64623 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-273 ##label TOM !'##cross-references GB:AE000594; GB:AE000511; NID:g2313957; !1PIDN:AAD07876.1; PID:g2313960; TIGR:HP0826 GENETICS !$#start_codon TTG CLASSIFICATION #superfamily lipopolysaccharide biosynthesis-associated !1protein SUMMARY #length 273 #molecular-weight 31557 #checksum 3174 SEQUENCE /// ENTRY E64620 #type complete TITLE lipopolysaccharide 5G8 epitope biosynthesis-associated protein - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS E64620 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession E64620 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-284 ##label TOM !'##cross-references GB:AE000592; GB:AE000511; NID:g2313929; !1PIDN:AAD07853.1; PID:g2313935; TIGR:HP0805 CLASSIFICATION #superfamily lipopolysaccharide biosynthesis-associated !1protein SUMMARY #length 284 #molecular-weight 32972 #checksum 5727 SEQUENCE /// ENTRY A64077 #type complete TITLE lipopolysaccharide biosynthesis protein lic2A - Haemophilus influenzae ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS A64077; S15282; S39576 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession A64077 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-302 ##label TIGR !'##cross-references GB:U32736; GB:L42023; NID:g1573519; !1PIDN:AAC22208.1; PID:g1573535; TIGR:HI0550 !'##experimental_source strain Rd KW20 REFERENCE S15282 !$#authors Cope, L.D.; Yogev, R.; Mertsola, J.; Latimer, J.L.; Hanson, !1M.S.; McCracken Jr., G.H.; Hansen, E.J. !$#journal Mol. Microbiol. (1991) 5:1113-1124 !$#title Molecular cloning of a gene involved in lipooligosaccharide !1biosynthesis and virulence expression by Haemophilus !1influenzae type B. !$#cross-references MUID:92065807; PMID:1956289 !$#accession S15282 !'##molecule_type DNA !'##residues 1-28,'N',30-40,45-105,'L',107-150,'R',152-302 ##label COP !'##cross-references EMBL:X56903; NID:g48811; PIDN:CAA40221.1; !1PID:g48812 !'##experimental_source strain DL42 !'##note it is uncertain whether Met-1 or Met-11 is the initiator REFERENCE S39576 !$#authors High, N.J.; Deadman, M.E.; Moxon, E.R. !$#journal Mol. Microbiol. (1993) 9:1275-1282 !$#title The role of a repetitive DNA motif (5'-CAAT-3') in the !1variable expression of the Haemophilus influenzae !1lipopolysaccharide epitope alpha-Gal(1-4)beta-Gal. !$#cross-references MUID:95020659; PMID:7523834 !$#accession S39576 !'##molecule_type DNA !'##residues 1-28,'N',30-40,49-105,'L',107-150,'R',152-255,'P',257-273, !1'D',275-302 ##label HIG !'##cross-references EMBL:L19441; NID:g305379; PIDN:AAA65534.1; !1PID:g305380 !'##experimental_source strain RM7004 GENETICS !$#gene lic2A FUNCTION !$#description involved in lipooligosaccharide biosynthesis and virulence !1expression CLASSIFICATION #superfamily lipopolysaccharide biosynthesis-associated !1protein SUMMARY #length 302 #molecular-weight 35490 #checksum 5218 SEQUENCE /// ENTRY B40608 #type complete TITLE glycogen biosynthesis inhibitor csrA - Escherichia coli (strain K-12) ALTERNATE_NAMES carbon storage regulator (csrA) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS B40608; D65049 REFERENCE A40608 !$#authors Romeo, T.; Gong, M.; Liu, M.Y.; Brun-Zinkernagel, A.M. !$#journal J. Bacteriol. (1993) 175:4744-4755 !$#title Identification and molecular characterization of csrA, a !1pleiotropic gene from Escherichia coli that affects glycogen !1biosynthesis, gluconeogenesis, cell size, and surface !1properties. !$#cross-references MUID:93328679; PMID:8393005 !$#accession B40608 !'##status preliminary !'##molecule_type DNA !'##residues 1-61 ##label ROM !'##cross-references GB:L07596; NID:g304880; PIDN:AAA71919.1; !1PID:g304882 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65049 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-61 ##label BLAT !'##cross-references GB:AE000353; GB:U00096; NID:g1789037; !1PIDN:AAC75738.1; PID:g1789047; UWGP:b2696 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene csrA CLASSIFICATION #superfamily glycogen biosynthesis inhibitor SUMMARY #length 61 #molecular-weight 6856 #checksum 8816 SEQUENCE /// ENTRY H64095 #type complete TITLE carbon storage regulator (csrA) homolog - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS H64095 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession H64095 !'##status preliminary !'##molecule_type DNA !'##residues 1-63 ##label TIGR !'##cross-references GB:U32763; GB:L42023; NID:g1573817; !1PIDN:AAC22472.1; PID:g1573825; TIGR:HI0813 CLASSIFICATION #superfamily glycogen biosynthesis inhibitor SUMMARY #length 63 #molecular-weight 7024 #checksum 9020 SEQUENCE /// ENTRY B64700 #type complete TITLE carbon storage regulator - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS B64700 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession B64700 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-76 ##label TOM !'##cross-references GB:AE000644; GB:AE000511; NID:g2314609; !1PIDN:AAD08480.1; PID:g2314614; TIGR:HP1442 CLASSIFICATION #superfamily glycogen biosynthesis inhibitor SUMMARY #length 76 #molecular-weight 8440 #checksum 9061 SEQUENCE /// ENTRY C64572 #type complete TITLE conserved hypothetical protein HP0419 - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS C64572 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession C64572 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-261 ##label TOM !'##cross-references GB:AE000557; GB:AE000511; NID:g2313514; !1PIDN:AAD07484.1; PID:g2313522; TIGR:HP0419 CLASSIFICATION #superfamily conserved hypothetical protein HP0419; bioC !1homology FEATURE !$56-161 #domain bioC homology #label BIOC SUMMARY #length 261 #molecular-weight 29920 #checksum 3589 SEQUENCE /// ENTRY E64026 #type complete TITLE probable S-adenosylmethionine-dependent methyltransferase HI1351 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS E64026 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession E64026 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-321 ##label TIGR !'##cross-references GB:U32814; GB:L42023; NID:g1574809; !1PIDN:AAC22998.1; PID:g1574813; TIGR:HI1351 CLASSIFICATION #superfamily conserved hypothetical protein HP0419; bioC !1homology FEATURE !$122-225 #domain bioC homology #label BIOC SUMMARY #length 321 #molecular-weight 36854 #checksum 2999 SEQUENCE /// ENTRY A60340 #type complete TITLE hypothetical protein a - Mycobacterium bovis insertion sequence IS987 ORGANISM #formal_name Mycobacterium bovis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A60340; S26366 REFERENCE A60340 !$#authors Hermans, P.W.M.; van Soolingen, D.; Bik, E.M.; de Haas, !1P.E.W.; Dale, J.W.; van Embden, J.D.A. !$#journal Infect. Immun. (1991) 59:2695-2705 !$#title Insertion element IS987 from Mycobacterium bovis BCG is !1located in a hot-spot integration region for insertion !1elements in Mycobacterium tuberculosis complex strains. !$#cross-references MUID:91310322; PMID:1649798 !$#accession A60340 !'##molecule_type DNA !'##residues 1-108 ##label HER !'##cross-references GB:X57835 !'##experimental_source strain 44 (RIVM), substrain BCG GENETICS !$#mobile_element insertion sequence IS987 CLASSIFICATION #superfamily insertion sequence IS1203 SUMMARY #length 108 #molecular-weight 12004 #checksum 4003 SEQUENCE /// ENTRY JC5304 #type complete TITLE probable transposase, 11.8K - Streptomyces lividans insertion sequence IS1372 ORGANISM #formal_name Streptomyces lividans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JC5304 REFERENCE JC5304 !$#authors Fischer, J.; Maier, H.; Viell, P.; Altenbuchner, J. !$#journal Gene (1996) 180:81-89 !$#title The use of an improved transposon mutagenesis system for DNA !1sequencing leads to the characterization of a new insertion !1sequence of Streptomyces lividans 66. !$#cross-references MUID:97128810; PMID:8973350 !$#accession JC5304 !'##molecule_type DNA !'##residues 1-103 ##label FIS !'##cross-references GB:U50076; NID:g1236634; PID:g1236635 !'##experimental_source strain 66; strain ZX7 GENETICS !$#mobile_element insertion sequence IS1372 !$#start_codon GTG CLASSIFICATION #superfamily insertion sequence IS1203 SUMMARY #length 103 #molecular-weight 11849 #checksum 3900 SEQUENCE /// ENTRY I53893 #type complete TITLE 12.7K protein - Escherichia coli insertion sequence IS1203 ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS I53893 REFERENCE I53893 !$#authors Paton, A.W.; Paton, J.C. !$#journal Gene (1994) 150:67-70 !$#title Characterization of IS1203, an insertion sequence of !1Escherichia coli O111:H(-). !$#cross-references MUID:95047551; PMID:7959065 !$#accession I53893 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-108 ##label RES !'##cross-references EMBL:U06468; NID:g459153; PIDN:AAA60328.1; !1PID:g459154 !'##experimental_source strain O111:H(-) GENETICS !$#mobile_element insertion sequence IS1203 CLASSIFICATION #superfamily insertion sequence IS1203 SUMMARY #length 108 #molecular-weight 12711 #checksum 7325 SEQUENCE /// ENTRY S03413 #type complete TITLE hypothetical protein A - Shigella sonnei insertion sequence IS629 ORGANISM #formal_name Shigella sonnei DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S03413; S09260 REFERENCE S03411 !$#authors Matsutani, S.; Ohtsubo, H.; Maeda, Y.; Ohtsubo, E. !$#journal J. Mol. Biol. (1987) 196:445-455 !$#title Isolation and characterization of IS elements repeated in !1the bacterial chromosome. !$#cross-references MUID:88062685; PMID:2824781 !$#accession S03413 !'##molecule_type DNA !'##residues 1-108 ##label MAT1 !'##cross-references GB:X51586; EMBL:X05953; NID:g47538; PID:g47539 REFERENCE S09260 !$#authors Matsutani, S.; Ohtsubo, E. !$#journal Nucleic Acids Res. (1990) 18:1899 !$#title Complete sequence of IS629. !$#cross-references MUID:90245593; PMID:2159625 !$#accession S09260 !'##molecule_type DNA !'##residues 1-108 ##label MAT2 !'##cross-references EMBL:X51586; NID:g47538; PID:g47539 GENETICS !$#mobile_element insertion sequence IS629 CLASSIFICATION #superfamily insertion sequence IS1203 SUMMARY #length 108 #molecular-weight 12583 #checksum 7300 SEQUENCE /// ENTRY JC5051 #type complete TITLE hypothetical protein, 12.5K - Shigella flexneri insertion sequence IS629 ORGANISM #formal_name Shigella flexneri DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS JC5051 REFERENCE JC5050 !$#authors Venkatesan, M.M.; Alexander, W.A.; Fernandez-Prada, C. !$#journal Gene (1996) 175:23-27 !$#title A Shigella flexneri invasion plasmid gene, ipgH, with !1homology to IS629 and sequences encoding bacterial sugar !1phosphate transport proteins. !$#cross-references MUID:97074644; PMID:8917071 !$#accession JC5051 !'##molecule_type DNA !'##residues 1-108 ##label VEN !'##cross-references GB:U28354; NID:g1016674; PIDN:AAC44574.1; !1PID:g1016675 !'##experimental_source strain M9OT-W; plasmid pWR100; insertion !1sequence IS629 GENETICS !$#mobile_element insertion sequence IS629 CLASSIFICATION #superfamily insertion sequence IS1203 SUMMARY #length 108 #molecular-weight 12539 #checksum 6996 SEQUENCE /// ENTRY S21331 #type complete TITLE hypothetical protein 1 - Agrobacterium tumefaciens insertion sequence IS868 ORGANISM #formal_name Agrobacterium tumefaciens DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S21331 REFERENCE S21331 !$#authors Paulus, F.; Canaday, J.; Otten, L. !$#submission submitted to the EMBL Data Library, October 1990 !$#description Limited host range Ti plasmids; recent origin from wide host !1range Ti plasmids & involvement of a novel IS element IS868. !$#accession S21331 !'##molecule_type DNA !'##residues 1-108 ##label PAU !'##cross-references EMBL:X55075; NID:g39138; PID:g39139 !'##experimental_source plasmid Ti, insertion sequence IS868 GENETICS !$#mobile_element insertion sequence IS868 CLASSIFICATION #superfamily insertion sequence IS1203 SUMMARY #length 108 #molecular-weight 12264 #checksum 4507 SEQUENCE /// ENTRY B65110 #type complete TITLE hypothetical 24.0 kD protein in murZ-rpoN intergenic region - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS B65110 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65110 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-211 ##label BLAT !'##cross-references GB:AE000399; GB:U00096; NID:g2367201; !1PIDN:AAC76224.1; PID:g1789583; UWGP:b3192 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yrbC CLASSIFICATION #superfamily hypothetical protein HI1084 SUMMARY #length 211 #molecular-weight 23962 #checksum 983 SEQUENCE /// ENTRY B64166 #type complete TITLE hypothetical protein HI1084 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS B64166 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession B64166 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-214 ##label TIGR !'##cross-references GB:U32788; GB:L42023; NID:g1574629; !1PIDN:AAC22740.1; PID:g1574638; TIGR:HI1084 !'##note best homolog was a hypothetical protein from Escherichia coli CLASSIFICATION #superfamily hypothetical protein HI1084 SUMMARY #length 214 #molecular-weight 24510 #checksum 1216 SEQUENCE /// ENTRY S36695 #type complete TITLE hypothetical protein 312 - Autographa californica nuclear polyhedrosis virus ORGANISM #formal_name Autographa californica nuclear polyhedrosis virus, AcMNPV DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S36695 REFERENCE S36690 !$#authors Kool, M.; Broer, R.; Zuidema, D.; Goldbach, R.W.; Vlak, J.M. !$#submission submitted to the EMBL Data Library, April 1993 !$#description Nucleotide sequence of an Autographa californica nuclear !1polyhedrosis virus 7.3 Kbp region (47 to 52.5 map units) of !1EcoRI-C. !$#accession S36695 !'##status preliminary !'##molecule_type DNA !'##residues 1-104 ##label KOO !'##cross-references EMBL:X71415; NID:g525306; PID:g296326 CLASSIFICATION #superfamily hypothetical protein 312 SUMMARY #length 104 #molecular-weight 12213 #checksum 3542 SEQUENCE /// ENTRY G65105 #type complete TITLE hypothetical 11.3 kD protein in sohA-mtr intergenic region - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS G65105 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65105 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-100 ##label BLAT !'##cross-references GB:AE000396; GB:U00096; NID:g1789536; !1PIDN:AAC76189.1; PID:g1789545; UWGP:b3155 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yhbQ CLASSIFICATION #superfamily hypothetical protein 312 SUMMARY #length 100 #molecular-weight 11270 #checksum 7768 SEQUENCE /// ENTRY S32865 #type complete TITLE outK protein - Erwinia carotovora ORGANISM #formal_name Erwinia carotovora DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S32865; S31754 REFERENCE S32857 !$#authors Reeves, P.J.; Whitcombe, D.; Wharam, S.; Gibson, M.; !1Allison, G.; Bunce, N.; Barallon, R.; Douglas, P.; !1Mulholland, V.; Stevens, S.; Walker, D.; Salmond, G.P.C. !$#journal Mol. Microbiol. (1993) 8:443-456 !$#title Molecular cloning and characterization of 13 out genes from !1Erwinia carotovora subspecies carotovora: genes encoding !1members of a general secretion pathway (GSP) widespread in !1gram-negative bacteria. !$#cross-references MUID:93316842; PMID:8326859 !$#accession S32865 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-328 ##label REE !'##cross-references EMBL:X70049; NID:g42184; PIDN:CAA49652.1; !1PID:g42193 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1/./ GENETICS !$#gene outK CLASSIFICATION #superfamily outK protein KEYWORDS transmembrane protein SUMMARY #length 328 #molecular-weight 36569 #checksum 5004 SEQUENCE /// ENTRY G65126 #type complete TITLE probable general secretion pathway protein k - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS G65126 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65126 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-327 ##label BLAT !'##cross-references GB:AE000409; GB:U00096; NID:g1789718; !1PIDN:AAC76357.1; PID:g1789729; UWGP:b3332 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yheJ CLASSIFICATION #superfamily outK protein KEYWORDS transmembrane protein SUMMARY #length 327 #molecular-weight 37646 #checksum 2433 SEQUENCE /// ENTRY S11921 #type complete TITLE pulK protein - Klebsiella oxytoca ORGANISM #formal_name Klebsiella oxytoca DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S11921 REFERENCE S11917 !$#authors Reyss, I.; Pugsley, A.P. !$#journal Mol. Gen. Genet. (1990) 222:176-184 !$#title Five additional genes in the pulC-O operon of the !1gram-negative bacterium Klebsiella oxytoca UNF5023 which are !1required for pullulanase secretion. !$#cross-references MUID:91109698; PMID:2129543 !$#accession S11921 !'##status preliminary !'##molecule_type DNA !'##residues 1-326 ##label REY CLASSIFICATION #superfamily outK protein KEYWORDS transmembrane protein SUMMARY #length 326 #molecular-weight 36153 #checksum 3690 SEQUENCE /// ENTRY S56477 #type complete TITLE hypothetical 17.3K protein (pyrL-argI intergenic region) - Escherichia coli (strain K-12) ALTERNATE_NAMES hypothetical protein o153b ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS S56477; G65237 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56477 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-153 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97148.1; !1PID:g537093 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65237 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-153 ##label BLAT !'##cross-references GB:AE000496; GB:U00096; NID:g2367366; !1PIDN:AAC77209.1; PID:g1790701; UWGP:b4252 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yjgK !$#start_codon GTG CLASSIFICATION #superfamily hypothetical protein HI0227 SUMMARY #length 153 #molecular-weight 17254 #checksum 6449 SEQUENCE /// ENTRY S47797 #type complete TITLE hypothetical 17.5K protein (avtA-selB intergenic region) - Escherichia coli (strain K-12) ALTERNATE_NAMES hypothetical protein o155 ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS S47797; B65157 REFERENCE S47666 !$#authors Plunkett, G. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S47797 !'##status preliminary !'##molecule_type DNA !'##residues 1-155 ##label PLU !'##cross-references EMBL:U00039; NID:g466582; PID:g466714 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65157 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-155 ##label BLAT !'##cross-references GB:AE000435; GB:U00096; NID:g2367244; !1PIDN:AAC76600.1; PID:g1790001; UWGP:b3576 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yiaL CLASSIFICATION #superfamily hypothetical protein HI0227 SUMMARY #length 155 #molecular-weight 17549 #checksum 4058 SEQUENCE /// ENTRY G65113 #type complete TITLE hypothetical protein b3221 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS G65113 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65113 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-154 ##label BLAT !'##cross-references GB:AE000401; GB:U00096; NID:g1789607; !1PIDN:AAC76253.1; PID:g1789615; UWGP:b3221 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily hypothetical protein HI0227 SUMMARY #length 154 #molecular-weight 17038 #checksum 65 SEQUENCE /// ENTRY F64145 #type complete TITLE hypothetical protein HI0227 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS F64145 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession F64145 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-155 ##label TIGR !'##cross-references GB:U32709; GB:L42023; NID:g1573190; !1PIDN:AAC21897.1; PID:g1573192; TIGR:HI0227 !'##note best homolog was a hypothetical protein from Escherichia coli CLASSIFICATION #superfamily hypothetical protein HI0227 SUMMARY #length 155 #molecular-weight 17670 #checksum 6408 SEQUENCE /// ENTRY F65241 #type complete TITLE transposase - Escherichia coli (strain K-12) insertion sequence IS30 ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS F65241; G64891; H64750; S56509; S28740 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65241 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-383 ##label BLAT !'##cross-references GB:AE000499; GB:U00096; NID:g1790732; PID:g1790736; !1UWGP:b4284 !'##experimental_source insertion sequence IS30; strain K-12, substrain !1MG1655 !'##genetics TRA3 !$#accession G64891 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-383 ##label BLA2 !'##cross-references GB:AE000237; GB:U00096; NID:g1787665; !1PIDN:AAC74486.1; PID:g1787671; UWGP:b1404 !'##experimental_source insertion sequence IS30; strain K-12, substrain !1MG1655 !'##genetics TRA2 !$#accession H64750 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-260,'V',262-383 ##label BLA3 !'##cross-references GB:U00096; NID:g2367099; PIDN:AAC73359.1; !1PID:g1786450; UWGP:b0256 !'##experimental_source insertion sequence IS30; strain K-12, substrain !1MG1655 !'##genetics TRA1 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56509 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-383 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97180.1; !1PID:g537125 !'##experimental_source insertion sequence IS30; strain K12 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE S28740 !$#authors Dalrymple, B.; Caspers, P.; Arber, W. !$#journal EMBO J. (1984) 3:2145-2149 !$#title Nucleotide sequence of the prokaryotic mobile genetic !1element IS30. !$#cross-references MUID:85027168; PMID:6092059 !$#accession S28740 !'##status translation not shown !'##molecule_type DNA !'##residues 1-4,'I',6-26,'T',28-383 ##label DAL !'##cross-references EMBL:X00792 !'##experimental_source insertion sequence IS30; strain K-12 GENETICS TRA3 !$#gene tra8_3 !$#mobile_element insertion sequence IS30 GENETICS TRA1 !$#gene tra8_1 !$#mobile_element insertion sequence IS30 GENETICS TRA2 !$#gene tra8_2 !$#mobile_element insertion sequence IS30 CLASSIFICATION #superfamily insertion sequence element IS30 transposase KEYWORDS DNA binding SUMMARY #length 383 #molecular-weight 44281 #checksum 856 SEQUENCE /// ENTRY A47049 #type complete TITLE probable transposase - Alcaligenes eutrophus ORGANISM #formal_name Alcaligenes eutrophus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A47049 REFERENCE A47049 !$#authors Dong, Q.; Sadouk, A.; van der Lelie, D.; Taghavi, S.; !1Ferhat, A.; Nuyten, J.M.; Borremans, B.; Mergeay, M.; !1Toussaint, A. !$#journal J. Bacteriol. (1992) 174:8133-8138 !$#title Cloning and sequencing of IS1086, an Alcaligenes eutrophus !1insertion element related to IS30 and IS4351. !$#cross-references MUID:93094145; PMID:1334071 !$#contents CH34, IS1086 !$#accession A47049 !'##status preliminary !'##molecule_type DNA !'##residues 1-339 ##label DON !'##cross-references GB:X58441; GB:S51074; NID:g48875; PID:g48876 !'##experimental_source strain ATCC 43123; substrain CH34 !'##note sequence extracted from NCBI backbone (NCBIN:120028, !1NCBIP:120029) CLASSIFICATION #superfamily insertion sequence element IS30 transposase KEYWORDS DNA binding SUMMARY #length 339 #molecular-weight 38086 #checksum 7355 SEQUENCE /// ENTRY G65106 #type complete TITLE lipoprotein precursor [imported] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS G65106 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65106 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-294 ##label BLAT !'##cross-references GB:AE000397; GB:U00096; NID:g2367199; !1PIDN:AAC76197.1; PID:g1789554; UWGP:b3163 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yhbM CLASSIFICATION #superfamily hypothetical protein HI0230; tetratricopeptide !1repeat homology FEATURE !$62-95 #domain tetratricopeptide repeat homology #label TT1\ !$96-129 #domain tetratricopeptide repeat homology #label TT2 SUMMARY #length 294 #molecular-weight 33620 #checksum 1878 SEQUENCE /// ENTRY G64145 #type complete TITLE hypothetical protein HI0230 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS G64145 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession G64145 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-314 ##label TIGR !'##cross-references GB:U32709; GB:L42023; NID:g1573190; !1PIDN:AAC21899.1; PID:g1573194; TIGR:HI0230 !'##note best homolog was a hypothetical protein from Escherichia coli CLASSIFICATION #superfamily hypothetical protein HI0230; tetratricopeptide !1repeat homology FEATURE !$74-107 #domain tetratricopeptide repeat homology #label TT1\ !$108-141 #domain tetratricopeptide repeat homology #label TT2\ !$142-175 #domain tetratricopeptide repeat homology #label TT3 SUMMARY #length 314 #molecular-weight 36433 #checksum 6982 SEQUENCE /// ENTRY S01832 #type complete TITLE regulatory protein gutR - Escherichia coli (strain K-12) ALTERNATE_NAMES glucitol operon protein R; srlR protein ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS S01832; G65050 REFERENCE S01831 !$#authors Yamada, M.; Saier Jr., M.H. !$#journal J. Mol. Biol. (1988) 203:569-583 !$#title Positive and negative regulators for glucitol (gut) operon !1expression in Escherichia coli. !$#cross-references MUID:89094828; PMID:3062173 !$#accession S01832 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-257 ##label YAM !'##cross-references GB:X13463; NID:g41628; PIDN:CAA31820.1; PID:g41630 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65050 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-257 ##label BLAT !'##cross-references GB:AE000354; GB:U00096; NID:g2367149; !1PIDN:AAC75749.1; PID:g1789059; UWGP:b2707 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene srlR; gutR CLASSIFICATION #superfamily regulatory protein gutR KEYWORDS DNA binding; transcription regulation SUMMARY #length 257 #molecular-weight 28236 #checksum 4398 SEQUENCE /// ENTRY G65102 #type complete TITLE probable transcription repressor of aga operon - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS G65102 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65102 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-269 ##label BLAT !'##cross-references GB:AE000394; GB:U00096; NID:g2367197; !1PIDN:AAC76165.1; PID:g1789519; UWGP:b3131 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene agaR CLASSIFICATION #superfamily regulatory protein gutR KEYWORDS DNA binding; transcription regulation SUMMARY #length 269 #molecular-weight 29572 #checksum 9399 SEQUENCE /// ENTRY B69627 #type complete TITLE transcription repressor of fructose operon fruR - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69627 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69627 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-251 ##label KUN !'##cross-references GB:Z99111; GB:AL009126; NID:g2633699; !1PIDN:CAB13311.1; PID:g2633809 !'##experimental_source strain 168 GENETICS !$#gene fruR CLASSIFICATION #superfamily regulatory protein gutR SUMMARY #length 251 #molecular-weight 27817 #checksum 4925 SEQUENCE /// ENTRY D70014 #type complete TITLE transcription regulator DeoR family homolog yulB - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS D70014 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D70014 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-258 ##label KUN !'##cross-references GB:Z99119; GB:Z99120; GB:AL009126; NID:g2635613; !1PID:g2635617; NID:g2635411; PID:g2635605 !'##experimental_source strain 168 GENETICS !$#gene yulB CLASSIFICATION #superfamily regulatory protein gutR SUMMARY #length 258 #molecular-weight 28855 #checksum 8962 SEQUENCE /// ENTRY C65054 #type complete TITLE hypothetical protein b2735 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS C65054 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65054 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-265 ##label BLAT !'##cross-references GB:AE000357; GB:U00096; NID:g2367155; !1PIDN:AAC75777.1; PID:g1789091; UWGP:b2735 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily regulatory protein gutR SUMMARY #length 265 #molecular-weight 28561 #checksum 7291 SEQUENCE /// ENTRY S70466 #type complete TITLE transcription regulator scgR - Bacillus subtilis ALTERNATE_NAMES transcription regulator tnrA ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S70466; F69724 REFERENCE S70466 !$#authors Kontinen, V.P.; Helander, I.M.; Tokuda, H. !$#journal FEBS Lett. (1996) 389:281-284 !$#title The secG deletion mutation of Escherichia coli is suppressed !1by expression of a novel regulatory gene of Bacillus !1subtilis. !$#cross-references MUID:96335610; PMID:8766716 !$#accession S70466 !'##molecule_type DNA !'##residues 1-110 ##label KON !'##cross-references EMBL:X98512; NID:g1405479; PIDN:CAA67135.1; !1PID:g1405480 !'##experimental_source strain 168 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69724 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-110 ##label KUN !'##cross-references GB:Z99110; GB:AL009126; NID:g2633472; PID:g2633685; !1GB:Z99111; NID:g2633699; PID:g2633702 !'##experimental_source strain 168 GENETICS !$#gene tnrA; scgR CLASSIFICATION #superfamily transcription repressor glnR KEYWORDS DNA binding; transcription regulation FEATURE !$16-36 #region helix-turn-helix motif SUMMARY #length 110 #molecular-weight 13126 #checksum 8554 SEQUENCE /// ENTRY JT0393 #type complete TITLE glutamine synthetase transcription repressor glnR [validated] - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 18-Aug-2000 ACCESSIONS JT0393; S06830; H69633 REFERENCE JT0392 !$#authors Strauch, M.A.; Aronson, A.I.; Brown, S.W.; Schreier, H.J.; !1Sonenshein, A.L. !$#journal Gene (1988) 71:257-265 !$#title Sequence of the Bacillus subtilis glutamine synthetase gene !1region. !$#cross-references MUID:89138001; PMID:2906311 !$#accession JT0393 !'##molecule_type DNA !'##residues 1-135 ##label STR !'##cross-references GB:M22811; NID:g142985; PIDN:AAA83375.1; !1PID:g1119204 REFERENCE S06830 !$#authors Schreier, H.J.; Brown, S.W.; Hirschi, K.D.; Nomellini, J.F.; !1Sonenshein, A.L. !$#journal J. Mol. Biol. (1989) 210:51-63 !$#title Regulation of Bacillus subtilis glutamine synthetase gene !1expression by the product of the glnR gene. !$#cross-references MUID:90064556; PMID:2573733 !$#accession S06830 !'##molecule_type DNA !'##residues 1-28,'L',30-50,'G',52-82 ##label SCH !'##note the authors have confirmed that the sequence in reference !1JT0392 is correct REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69633 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-135 ##label KUN !'##cross-references GB:Z99113; GB:AL009126; NID:g2634090; !1PIDN:CAB13629.1; PID:g2634129 !'##experimental_source strain 168 GENETICS !$#gene glnR FUNCTION !$#description involved in transcription regulation of glutamine synthetase !1(glnA, PIR:AJBSQS) [validated, MUID:90064556] CLASSIFICATION #superfamily transcription repressor glnR KEYWORDS DNA binding; transcription regulation FEATURE !$59-83 #domain DNA binding #status predicted #label DNB SUMMARY #length 135 #molecular-weight 15832 #checksum 6687 SEQUENCE /// ENTRY A69334 #type complete TITLE mercuric resistance operon regulatory protein (merR) homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A69334 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession A69334 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-130 ##label KLE !'##cross-references GB:AE001058; GB:AE000782; NID:g2689381; !1PIDN:AAB90568.1; PID:g2649944; TIGR:AF0673 CLASSIFICATION #superfamily transcription repressor glnR SUMMARY #length 130 #molecular-weight 15673 #checksum 9823 SEQUENCE /// ENTRY I64059 #type complete TITLE mercuric resistance operon regulatory protein homolog HI0293 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS I64059 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession I64059 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-128 ##label TIGR !'##cross-references GB:U32715; GB:L42023; NID:g1573254; !1PIDN:AAC21957.1; PID:g1573261; TIGR:HI0293 CLASSIFICATION #superfamily transcription repressor glnR SUMMARY #length 128 #molecular-weight 14589 #checksum 1858 SEQUENCE /// ENTRY B65093 #type complete TITLE ADP-heptose synthase homolog - Escherichia coli (strain K-12) ALTERNATE_NAMES hypothetical protein b3052 ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS B65093 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65093 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-477 ##label BLAT !'##cross-references GB:AE000387; GB:U00096; NID:g1789431; !1PIDN:AAC76088.1; PID:g1789432; UWGP:b3052 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily hypothetical protein b3052 SUMMARY #length 477 #molecular-weight 51050 #checksum 188 SEQUENCE /// ENTRY C64127 #type complete TITLE ADP-heptose synthase homolog - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS C64127 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession C64127 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-476 ##label TIGR !'##cross-references GB:U32828; GB:L42023; NID:g1574362; !1PIDN:AAC23172.1; PID:g1574367; TIGR:HI1526 CLASSIFICATION #superfamily hypothetical protein b3052 SUMMARY #length 476 #molecular-weight 51945 #checksum 3533 SEQUENCE /// ENTRY B64627 #type complete TITLE ADP-heptose synthase - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS B64627 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession B64627 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-461 ##label TOM !'##cross-references GB:AE000596; GB:AE000511; NID:g2313982; !1PIDN:AAD07904.1; PID:g2313990; TIGR:HP0858 CLASSIFICATION #superfamily hypothetical protein b3052 SUMMARY #length 461 #molecular-weight 50688 #checksum 6300 SEQUENCE /// ENTRY D65106 #type complete TITLE hypothetical 37.1 kD protein in sohA-mtr intergenic region - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS D65106 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65106 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-335 ##label BLAT !'##cross-references GB:AE000397; GB:U00096; NID:g2367199; !1PIDN:AAC76194.1; PID:g1789551; UWGP:b3160 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yhbW CLASSIFICATION #superfamily ynbW protein SUMMARY #length 335 #molecular-weight 37129 #checksum 5008 SEQUENCE /// ENTRY S39699 #type complete TITLE monooxygenase homolog ywcH - Bacillus subtilis ALTERNATE_NAMES protein ipa-44d ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S39699; C70053 REFERENCE S39655 !$#authors Glaser, P.; Kunst, F.; Arnaud, M.; Coudart, M.P.; Gonzales, !1W.; Hullo, M.F.; Ionescu, M.; Lubochinsky, B.; Marcelino, !1L.; Moszer, I.; Presecan, E.; Santana, M.; Schneider, E.; !1Schweizer, J.; Vertes, A.; Rapoport, G.; Danchin, A. !$#journal Mol. Microbiol. (1993) 10:371-384 !$#title Bacillus subtilis genome project: cloning and sequencing of !1the 97 kb region from 325 degrees to 333 degrees. !$#cross-references MUID:95020537; PMID:7934828 !$#accession S39699 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-333 ##label GLA !'##cross-references EMBL:X73124; NID:g413923; PIDN:CAA51600.1; !1PID:g413968 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1993 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C70053 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-333 ##label KUN !'##cross-references GB:Z99123; GB:AL009126; NID:g2636240; !1PIDN:CAB15836.1; PID:g2636345 !'##experimental_source strain 168 GENETICS !$#gene ywcH CLASSIFICATION #superfamily ynbW protein SUMMARY #length 333 #molecular-weight 36557 #checksum 7405 SEQUENCE /// ENTRY B64706 #type complete TITLE hemolysin - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS B64706 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession B64706 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-449 ##label TOM !'##cross-references GB:AE000647; GB:AE000511; NID:g2314645; !1PIDN:AAD08525.1; PID:g2314662; TIGR:HP1490 CLASSIFICATION #superfamily hypothetical protein HI0107 SUMMARY #length 449 #molecular-weight 50433 #checksum 8893 SEQUENCE /// ENTRY S56443 #type complete TITLE hypothetical 49.8K protein (cysq-msra intergenic region) - Escherichia coli (strain K-12) ALTERNATE_NAMES hypothetical protein f447 ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS S56443; E65233 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56443 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-447 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97114.1; !1PID:g537059 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65233 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-447 ##label BLAT !'##cross-references GB:AE000493; GB:U00096; NID:g2367360; !1PIDN:AAC77175.1; PID:g1790664; UWGP:b4218 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ytfL CLASSIFICATION #superfamily hypothetical protein HI0107 SUMMARY #length 447 #molecular-weight 49762 #checksum 9085 SEQUENCE /// ENTRY H64142 #type complete TITLE hypothetical protein HI0107 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS H64142 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession H64142 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-403 ##label TIGR !'##cross-references GB:U32696; GB:L42023; NID:g1573057; !1PIDN:AAC21785.1; PID:g1573060; TIGR:HI0107 !'##note best homolog was a hypothetical protein from Escherichia coli GENETICS !$#start_codon GTG CLASSIFICATION #superfamily hypothetical protein HI0107 SUMMARY #length 403 #molecular-weight 45104 #checksum 6403 SEQUENCE /// ENTRY S75595 #type complete TITLE hemolysin, 38K - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein sll1254 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S75595 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75595 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-346 ##label KAN !'##cross-references EMBL:D90912; GB:AB001339; NID:g1653228; !1PIDN:BAA18156.1; PID:g1653241 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily hypothetical protein HI0107 SUMMARY #length 346 #molecular-weight 38343 #checksum 3675 SEQUENCE /// ENTRY S76248 #type complete TITLE hemolysin, 49K - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein sll0260 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S76248 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76248 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-448 ##label KAN !'##cross-references EMBL:D90914; GB:AB001339; NID:g1653477; !1PIDN:BAA18507.1; PID:g1653594 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily hypothetical protein HI0107 SUMMARY #length 448 #molecular-weight 49227 #checksum 9157 SEQUENCE /// ENTRY B64216 #type complete TITLE hemolysin tlyC homolog - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 07-Dec-1999 ACCESSIONS B64216 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession B64216 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-424 ##label TIGR !'##cross-references GB:U39694; GB:L43967; NID:g1045822; PID:g1045829; !1TIGR:MG146 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily hemolysin homolog tlyC SUMMARY #length 424 #molecular-weight 48720 #checksum 7217 SEQUENCE /// ENTRY B70125 #type complete TITLE hemolysin homolog - Lyme disease spirochete ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 15-Oct-1999 ACCESSIONS B70125 REFERENCE A70100 !$#authors Fraser, C.M.; Casjens, S.; Huang, W.M.; Sutton, G.G.; !1Clayton, R.; Lathigra, R.; White, O.; Ketchum, K.A.; Dodson, !1R.; Hickey, E.K.; Gwinn, M.; Dougherty, B.; Tomb, J.F.; !1Fleischmann, R.D.; Richardson, D.; Peterson, J.; Kerlavage, !1A.R.; Quackenbush, J.; Salzberg, S.; Hanson, M.; Vugt, R.V.; !1Palmer, N.; Adams, M.D.; Gocayne, J.; Weidman, J.; !1Utterback, T.; Watthey, L.; McDonald, L.; Artiach, P.; !1Bowman, C.; Garland, S.; Fujii, C.; Cotton, M.D.; Horst, K.; !1Roberts, K.; Hatch, B.; Smith, H.O.; Venter, J.C. !$#journal Nature (1997) 390:580-586 !$#title Genomic sequence of a Lyme disease spirochaete, Borrelia !1burgdorferi. !$#cross-references MUID:98065943; PMID:9403685 !$#accession B70125 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-412 ##label KLE !'##cross-references GB:AE001130; GB:AE000783; NID:g2688088; !1PIDN:AAC66587.1; PID:g2688091; TIGR:BB0202 !'##experimental_source strain B31 CLASSIFICATION #superfamily hemolysin homolog tlyC SUMMARY #length 412 #molecular-weight 46390 #checksum 66 SEQUENCE /// ENTRY S73998 #type complete TITLE hemolysin hlyC homolog VXpSPT7_orf424 - Mycoplasma pneumoniae (strain ATCC 29342) ALTERNATE_NAMES hypothetical protein VXpSPT7_orf424 ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 10-Dec-1999 ACCESSIONS S73998 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73998 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-424 ##label HIM !'##cross-references EMBL:AE000062; GB:U00089; NID:g1674373; !1PIDN:AAB96320.1; PID:g1674378 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#gene hlyC !$#genetic_code SGC3 CLASSIFICATION #superfamily hemolysin homolog tlyC SUMMARY #length 424 #molecular-weight 48527 #checksum 5397 SEQUENCE /// ENTRY H64800 #type complete TITLE ybeX protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS H64800 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64800 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-292 ##label BLAT !'##cross-references GB:AE000170; GB:U00096; NID:g1786875; !1PIDN:AAC73759.1; PID:g1786879; UWGP:b0658 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ybeX CLASSIFICATION #superfamily hypothetical protein b0658 SUMMARY #length 292 #molecular-weight 33298 #checksum 3815 SEQUENCE /// ENTRY G64060 #type complete TITLE conserved hypothetical protein HI0301 - Haemophilus influenzae ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS G64060 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession G64060 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-299 ##label TIGR !'##cross-references GB:U32716; GB:L42023; NID:g1573268; !1PIDN:AAC21966.1; PID:g1573270; TIGR:HI0301 !'##experimental_source strain Rd KW20 CLASSIFICATION #superfamily hypothetical protein b0658 SUMMARY #length 299 #molecular-weight 34583 #checksum 3734 SEQUENCE /// ENTRY H65039 #type complete TITLE hypothetical protein in grpE 3' region - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS H65039 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65039 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-227 ##label BLAT !'##cross-references GB:AE000347; GB:U00096; NID:g2367142; !1PIDN:AAC75662.1; PID:g1788966; UWGP:b2613 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yfjD CLASSIFICATION #superfamily yfjD protein SUMMARY #length 227 #molecular-weight 25693 #checksum 877 SEQUENCE /// ENTRY B64896 #type complete TITLE hypothetical protein b1439 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS B64896 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64896 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-468 ##label BLAT !'##cross-references GB:AE000241; GB:U00096; NID:g1787706; !1PIDN:AAC74521.1; PID:g1787710; UWGP:b1439 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily hypothetical protein b1439 SUMMARY #length 468 #molecular-weight 52792 #checksum 6396 SEQUENCE /// ENTRY S56565 #type complete TITLE hypothetical 53K protein (iadA-mcrD intergenic region) - Escherichia coli (strain K-12) ALTERNATE_NAMES hypothetical protein f470 ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS S56565; F65248 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56565 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-470 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97236.1; !1PID:g537181 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65248 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-470 ##label BLAT !'##cross-references GB:AE000504; GB:U00096; NID:g1790789; !1PIDN:AAC77296.1; PID:g1790797; UWGP:b4340 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yjiR CLASSIFICATION #superfamily hypothetical protein b1439 SUMMARY #length 470 #molecular-weight 53046 #checksum 4826 SEQUENCE /// ENTRY I40492 #type complete TITLE gntR-type transcription regulator homolog ycxD - Bacillus subtilis ALTERNATE_NAMES hypothetical protein 8 (srfA operon) ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS I40492; F69766; S34990 REFERENCE I40485 !$#authors Cosmina, P.; Rodriguez, F.; de Ferra, F.; Grandi, G.; !1Perego, M.; Venema, G.; van Sinderen, D. !$#journal Mol. Microbiol. (1993) 8:821-831 !$#title Sequence and analysis of the genetic locus responsible for !1surfactin synthesis in Bacillus subtilis. !$#cross-references MUID:93360813; PMID:8355609 !$#accession I40492 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-444 ##label RES !'##cross-references EMBL:X70356; NID:g396480; PIDN:CAA49821.1; !1PID:g396486 !'##experimental_source ATCC 21332 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69766 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-444 ##label KUN !'##cross-references GB:Z99105; GB:Z99106; GB:AL009126; NID:g2632653; !1PID:g2632657; NID:g2632457; PID:g2632642 !'##experimental_source strain 168 GENETICS !$#gene ycxD CLASSIFICATION #superfamily hypothetical protein b1439 SUMMARY #length 444 #molecular-weight 50755 #checksum 165 SEQUENCE /// ENTRY S51574 #type complete TITLE mocR protein - Rhizobium meliloti ORGANISM #formal_name Rhizobium meliloti DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S51574; S43169 REFERENCE S51569 !$#authors Rossbach, S.; Kulpa, D.A.; Rossbach, U.; de Bruijn, F.J. !$#journal Mol. Gen. Genet. (1994) 245:11-24 !$#title Molecular and genetic characterization of the rhizopine !1catabolism (mocABRC) genes of Rhizobium meliloti L5-30. !$#cross-references MUID:95147842; PMID:7845353 !$#accession S51574 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-493 ##label ROS !'##cross-references EMBL:X78503; NID:g468758; PID:g468764 GENETICS !$#gene mocR CLASSIFICATION #superfamily hypothetical protein b1439 SUMMARY #length 493 #molecular-weight 55128 #checksum 9790 SEQUENCE /// ENTRY S47793 #type complete TITLE valine-pyruvate transaminase (EC 2.6.1.66) avtA [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES protein o417; transaminase C; valine-pyruvate aminotransferase ORGANISM #formal_name Escherichia coli DATE 19-May-2000 #sequence_revision 19-May-2000 #text_change 03-Jun-2002 ACCESSIONS S47793; F65156; B27279 REFERENCE S47666 !$#authors Plunkett, G. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S47793 !'##molecule_type DNA !'##residues 1-417 ##label PLU !'##cross-references EMBL:U00039; NID:g466582; PIDN:AAB18549.1; !1PID:g466710 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65156 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-417 ##label BLAT !'##cross-references GB:AE000434; GB:U00096; NID:g1789989; !1PIDN:AAC76596.1; PID:g1789996; UWGP:b3572 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A27279 !$#authors Liu, L.; Whalen, W.; Das, A.; Berg, C.M. !$#journal Nucleic Acids Res. (1987) 15:9461-9469 !$#title Rapid sequencing of cloned DNA using a transposon for !1bidirectional priming: sequence of the Escherichia coli K-12 !1avtA gene. !$#cross-references MUID:88067768; PMID:2825136 !$#accession B27279 !'##molecule_type DNA !'##residues 1-169,'G',171 ##label LIU !'##cross-references GB:Y00490; NID:g41040 !'##note this translation is made from the reverse complement of !1nucleotides 1460 to 944 in GenBank entry ECAVT, release !1113.0 !'##note the enzyme activity of the gene product was deduced from the !1differential valine requirements of low-copy versus !1high-copy plasmids carrying the gene in isoleucine-requiring !1ilvE strains GENETICS !$#gene avtA !$#map_position 84 min FUNCTION !$#description catalyzes the reversible transamination of valine and !1pyruvate to 3-methyl-2-oxobutanoate and alanine CLASSIFICATION #superfamily Escherichia coli valine-pyruvate transaminase KEYWORDS aminotransferase; phosphoprotein; pyridoxal phosphate FEATURE !$249 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 417 #molecular-weight 46697 #checksum 7790 SEQUENCE /// ENTRY S75385 #type complete TITLE probable valine-pyruvate transaminase (EC 2.6.1.66) c04018 [similarity] - Sulfolobus solfataricus ALTERNATE_NAMES transaminase C ORGANISM #formal_name Sulfolobus solfataricus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S75385 REFERENCE S73076 !$#authors Sensen, C.W.; Klenk, H.P.; Singh, R.K.; Allard, G.; Chan, !1C.C.Y.; Liu, Q.Y.; Penny, S.L.; Young, F.; Schenk, M.E.; !1Gaasterland, T.; Doolittle, W.F.; Ragan, M.A.; Charlebois, !1R.L. !$#journal Mol. Microbiol. (1996) 22:175-191 !$#title Organizational characteristics and information content of an !1archaeal genome: 156 kb of sequence from Sulfolobus !1solfataricus P2. !$#cross-references MUID:97055432; PMID:8899719 !$#accession S75385 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-401 ##label SEN !'##cross-references EMBL:Y08257; NID:g1707772; PID:g1707790 !'##experimental_source strain P2 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1September 1996 FUNCTION !$#description catalyzes the reversible transamination of valine and !1pyruvate to 3-methyl-2-oxobutanoate and alanine CLASSIFICATION #superfamily Escherichia coli valine-pyruvate transaminase KEYWORDS aminotransferase; phosphoprotein; pyridoxal phosphate FEATURE !$242 #binding_site pyridoxal phosphate (Lys) (covalent) !8#status predicted SUMMARY #length 401 #molecular-weight 45571 #checksum 4316 SEQUENCE /// ENTRY S73506 #type complete TITLE pilB homolog K05_orf151 - Mycoplasma pneumoniae (strain ATCC 29342) ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S73506 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73506 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-151 ##label HIM !'##cross-references EMBL:AE000019; GB:U00089; NID:g1673839; !1PIDN:AAB95828.1; PID:g1673843 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#gene pilB !$#genetic_code SGC3 CLASSIFICATION #superfamily hypothetical protein YCL033c SUMMARY #length 151 #molecular-weight 17279 #checksum 5467 SEQUENCE /// ENTRY E64249 #type complete TITLE pilin repressor pilB homolog MG448 - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E64249 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession E64249 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-150 ##label TIGR !'##cross-references GB:U39731; GB:L43967; NID:g3845031; !1PIDN:AAC72468.1; PID:g3845041; TIGR:MG448 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily hypothetical protein YCL033c SUMMARY #length 150 #molecular-weight 17289 #checksum 1228 SEQUENCE /// ENTRY S44820 #type complete TITLE F44E2.6 protein - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 20-Apr-2000 ACCESSIONS S44820 REFERENCE S44816 !$#authors Anderson, K. !$#submission submitted to the EMBL Data Library, September 1993 !$#description Sequence of the C. elegans cosmid F44E2. !$#accession S44820 !'##status preliminary !'##molecule_type DNA !'##residues 1-152 ##label AND !'##cross-references EMBL:L23646; NID:g388595; PID:g388600 GENETICS !$#introns 46/1; 75/2; 118/3 CLASSIFICATION #superfamily hypothetical protein YCL033c SUMMARY #length 152 #molecular-weight 17212 #checksum 8393 SEQUENCE /// ENTRY B64938 #type complete TITLE hypothetical protein b1778 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS B64938 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64938 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-137 ##label BLAT !'##cross-references GB:AE000272; GB:U00096; NID:g1788067; !1PIDN:AAC74848.1; PID:g1788077; UWGP:b1778 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily hypothetical protein YCL033c SUMMARY #length 137 #molecular-weight 15451 #checksum 89 SEQUENCE /// ENTRY S74642 #type complete TITLE hypothetical protein sll1680 - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S74642 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74642 !'##status preliminary !'##molecule_type DNA !'##residues 1-176 ##label KAN !'##cross-references EMBL:D90900; GB:AB001339; NID:g1651768; !1PIDN:BAA16794.1; PID:g1651867 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily hypothetical protein YCL033c SUMMARY #length 176 #molecular-weight 19661 #checksum 140 SEQUENCE /// ENTRY S19361 #type complete TITLE hypothetical protein YCL033c - yeast (Saccharomyces cerevisiae) ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S19361 REFERENCE S19350 !$#authors Hollenberg, C.P.; Kleinhans, U.; Lutzenkirchen, K.; Ramezani !1Rad, M.; Xu, G. !$#submission submitted to the Protein Sequence Database, March 1992 !$#accession S19361 !'##molecule_type DNA !'##residues 1-168 ##label HOL !'##cross-references EMBL:X59720; NID:g1907116; PID:g5331; !1GSPDB:GN00003; MIPS:YCL033c GENETICS !$#gene MIPS:YCL033c !'##cross-references SGD:S0000538 !$#map_position 3L CLASSIFICATION #superfamily hypothetical protein YCL033c SUMMARY #length 168 #molecular-weight 19279 #checksum 6412 SEQUENCE /// ENTRY F64835 #type complete TITLE paraquat-inducible protein pqiB - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS F64835; B57146; S52912 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64835 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-546 ##label BLAT !'##cross-references GB:AE000197; GB:U00096; NID:g1787180; !1PIDN:AAC74037.1; PID:g1787184; UWGP:b0951 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A57146 !$#authors Koh, Y.S.; Roe, J.H. !$#journal J. Bacteriol. (1995) 177:2673-2678 !$#title Isolation of a novel paraquat-inducible (pqi) gene regulated !1by the soxRS locus in Escherichia coli. !$#cross-references MUID:95270582; PMID:7751275 !$#accession B57146 !'##status preliminary !'##molecule_type DNA !'##residues 1-91 ##label KOH !'##cross-references EMBL:X81561 !'##experimental_source strain K-12, substrain W3110 COMMENT Residues 1-282 appear to be homologous to PIR:B64945 and !1other members of that superfamily. GENETICS !$#gene pqiB; pqi5B CLASSIFICATION #superfamily pqiB protein KEYWORDS transmembrane protein FEATURE !$19-35 #domain transmembrane #status predicted #label TMM SUMMARY #length 546 #molecular-weight 60520 #checksum 3624 SEQUENCE /// ENTRY B64945 #type complete TITLE probable membrane protein b1834 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS B64945 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64945 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-879 ##label BLAT !'##cross-references GB:AE000277; GB:U00096; NID:g1788129; !1PIDN:AAC74904.1; PID:g1788138; UWGP:b1834 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily hypothetical protein b1834 KEYWORDS transmembrane protein FEATURE !$25-41 #domain transmembrane #status predicted #label TMM SUMMARY #length 879 #molecular-weight 95238 #checksum 5981 SEQUENCE /// ENTRY A64040 #type complete TITLE hypothetical protein HI1672 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS A64040 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession A64040 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-881 ##label TIGR !'##cross-references GB:U32840; GB:L42023; NID:g1574518; !1PIDN:AAC23317.1; PID:g1574522; TIGR:HI1672 CLASSIFICATION #superfamily hypothetical protein b1834 SUMMARY #length 881 #molecular-weight 96677 #checksum 466 SEQUENCE /// ENTRY I40398 #type complete TITLE flagellar protein fliS - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS I40398; E69625 REFERENCE I40396 !$#authors Chen, L.; Helmann, J.D. !$#journal J. Bacteriol. (1994) 176:3093-3101 !$#title The Bacillus subtilis sigma D-dependent operon encoding the !1flagellar proteins FliD, FliS, and FliT. !$#cross-references MUID:94252974; PMID:8195064 !$#accession I40398 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-133 ##label RES !'##cross-references EMBL:Z31376; NID:g499379; PIDN:CAA83249.1; !1PID:g499382 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69625 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-133 ##label KUN !'##cross-references GB:Z99122; GB:AL009126; NID:g2636029; !1PIDN:CAB15550.1; PID:g2636059 !'##experimental_source strain 168 GENETICS !$#gene fliS CLASSIFICATION #superfamily flagellar protein fliS SUMMARY #length 133 #molecular-weight 15131 #checksum 2756 SEQUENCE /// ENTRY A64614 #type complete TITLE flagellar protein - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS A64614 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession A64614 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-126 ##label TOM !'##cross-references GB:AE000588; GB:AE000511; NID:g2313880; !1PIDN:AAD07803.1; PID:g2313881; TIGR:HP0753 CLASSIFICATION #superfamily flagellar protein fliS SUMMARY #length 126 #molecular-weight 14542 #checksum 8463 SEQUENCE /// ENTRY B64956 #type complete TITLE flagellar protein fliS - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS B64956 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64956 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-136 ##label BLAT !'##cross-references GB:AE000285; GB:U00096; NID:g1788229; !1PIDN:AAC74992.1; PID:g1788234; UWGP:b1925 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene fliS CLASSIFICATION #superfamily flagellar protein fliS KEYWORDS flagellum SUMMARY #length 136 #molecular-weight 14950 #checksum 3465 SEQUENCE /// ENTRY S71028 #type complete TITLE flagellar protein flaJ - Vibrio parahaemolyticus ALTERNATE_NAMES fliS protein homolog ORGANISM #formal_name Vibrio parahaemolyticus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S71028 REFERENCE S71027 !$#authors Stewart, B.J.; McCarter, L.L. !$#journal Mol. Microbiol. (1996) 20:137-149 !$#title Vibrio parahaemolyticus FlaJ, a homologue of FliS, is !1required for production of a flagellin. !$#cross-references MUID:97014377; PMID:8861212 !$#accession S71028 !'##molecule_type DNA !'##residues 1-136 ##label STE !'##cross-references EMBL:U12816; NID:g6806922; PIDN:AAC27805.1; !1PID:g1254205 GENETICS !$#gene flaJ CLASSIFICATION #superfamily flagellar protein fliS SUMMARY #length 136 #molecular-weight 14716 #checksum 5038 SEQUENCE /// ENTRY D41886 #type complete TITLE probable export protein fliQ precursor - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 07-Aug-1998 #sequence_revision 07-Aug-1998 #text_change 16-Jun-2000 ACCESSIONS D41886; C69625 REFERENCE A41886 !$#authors Bischoff, D.S.; Weinreich, M.D.; Ordal, G.W. !$#journal J. Bacteriol. (1992) 174:4017-4025 !$#title Nucleotide sequences of Bacillus subtilis flagellar !1biosynthetic genes fliP and fliQ and identification of a !1novel flagellar gene, fliZ. !$#cross-references MUID:92283757; PMID:1597417 !$#accession D41886 !'##molecule_type DNA !'##residues 'V',2-89 ##label BIS !'##cross-references GB:M87005; NID:g142928; PIDN:AAA22454.1; !1PID:g142932 !'##note the authors translated the initiation codon GTG for residue 1 !1as Val !'##note sequence extracted from NCBI backbone (NCBIN:106465, !1NCBIP:106469) REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69625 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-89 ##label KUN !'##cross-references GB:Z99112; GB:AL009126; NID:g2633902; !1PIDN:CAB13509.1; PID:g2634008 !'##experimental_source strain 168 GENETICS !$#gene fliQ !$#start_codon GTG FUNCTION !$#description required for assembly of the flagellum rivet; may be !1involved in export of flagellar protein !$#pathway flagellum assembly CLASSIFICATION #superfamily flagellar biosynthesis-specific protein KEYWORDS flagellum; transmembrane protein FEATURE !$1-36 #domain signal sequence #status predicted #label SIG\ !$37-89 #product probable export protein fliQ #status !8predicted #label MAT\ !$49-65 #domain transmembrane #status predicted #label TRM SUMMARY #length 89 #molecular-weight 9713 #checksum 5763 SEQUENCE /// ENTRY C36869 #type complete TITLE probable export protein fliQ - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS C36869; B64959 REFERENCE A36869 !$#authors Malakooti, J.; Ely, B.; Matsumura, P. !$#journal J. Bacteriol. (1994) 176:189-197 !$#title Molecular characterization, nucleotide sequence, and !1expression of the fliO, fliP, fliQ, and fliR genes of !1Escherichia coli. !$#cross-references MUID:94110225; PMID:8282695 !$#accession C36869 !'##status preliminary !'##molecule_type DNA !'##residues 1-89 ##label MAL !'##cross-references GB:L22182; NID:g347241; PIDN:AAC36860.1; !1PID:g347244 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64959 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-89 ##label BLAT !'##cross-references GB:AE000287; GB:U00096; NID:g1788257; !1PIDN:AAC75016.1; PID:g1788260; UWGP:b1949 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene fliQ FUNCTION !$#description required for assembly of the flagellum rivet; may be !1involved in export of flagellar protein CLASSIFICATION #superfamily flagellar biosynthesis-specific protein KEYWORDS flagellum; transmembrane protein FEATURE !$22-38 #domain transmembrane #status predicted #label TM1\ !$49-65 #domain transmembrane #status predicted #label TM2 SUMMARY #length 89 #molecular-weight 9632 #checksum 5179 SEQUENCE /// ENTRY JC4508 #type complete TITLE flagellar biosynthesis-specific protein FliQ precursor - syphilis spirochete ORGANISM #formal_name Treponema pallidum subsp. pallidum #common_name syphilis spirochete DATE 07-Aug-1998 #sequence_revision 07-Aug-1998 #text_change 23-Jul-1999 ACCESSIONS JC4508; A71291 REFERENCE PC4114 !$#authors Hardham, J.M.; Frye, J.G.; Stamm, L.V. !$#journal Gene (1995) 166:57-64 !$#title Identification and sequences of the Treponema pallidum !1fliM', fliY, fliP, fliQ, fliR and flhB' genes. !$#cross-references MUID:96105201; PMID:8529894 !$#accession JC4508 !'##molecule_type DNA !'##residues 'V',2-94 ##label HAR !'##cross-references GB:U26453 !'##note the authors are uncertain whether Val-1 (GTG) or Met-2 (ATG) is !1the initiator REFERENCE A71250 !$#authors Fraser, C.M.; Norris, S.J.; Weinstock, G.M.; White, O.; !1Sutton, G.G.; Dodson, R.; Gwinn, M.; Hickey, E.K.; Clayton, !1R.; Ketchum, K.A.; Sodergren, E.; Hardham, J.M.; McLeod, !1M.P.; Salzberg, S.; Peterson, J.; Khalak, H.; Richardson, !1D.; Howell, J.K.; Chidambaram, M.; Utterback, T.; McDonald, !1L.; Artiach, P.; Bowman, C.; Cotton, M.D.; Fujii, C.; !1Garland, S.; Hatch, B.; Horst, K.; Roberts, K.; Watthey, L.; !1Weidman, J.; Smith, H.O.; Venter, J.C. !$#journal Science (1998) 281:375-388 !$#title Complete genome sequence of Treponema pallidum, the syphilis !1spirochete. !$#cross-references MUID:98332770; PMID:9665876 !$#accession A71291 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-94 ##label COL !'##cross-references GB:AE001244; GB:AE000520; NID:g3323005; !1PIDN:AAC65683.1; PID:g3323019 !'##experimental_source strain Nichols GENETICS !$#gene fliQ; TP0717 !$#start_codon GTG FUNCTION !$#description required for assembly of the flagellum rivet !$#pathway flagellum assembly CLASSIFICATION #superfamily flagellar biosynthesis-specific protein KEYWORDS flagellum; transmembrane protein FEATURE !$1-37 #domain signal sequence #status predicted #label SIG\ !$38-94 #product flagellar biosynthesis-specific protein FliQ !8#status predicted #label MAT\ !$50-66 #domain transmembrane #status predicted #label TRM SUMMARY #length 94 #molecular-weight 10185 #checksum 3246 SEQUENCE /// ENTRY I40670 #type complete TITLE flagellar biosynthesis-specific protein fliQ - Caulobacter crescentus ORGANISM #formal_name Caulobacter crescentus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 18-Jul-2001 ACCESSIONS I40670; G87382 REFERENCE I40669 !$#authors Zhuang, W.Y.; Shapiro, L. !$#journal J. Bacteriol. (1995) 177:343-356 !$#title Caulobacter FliQ and FliR membrane proteins, required for !1flagellar biogenesis and cell division, belong to a family !1of virulence factor export proteins. !$#cross-references MUID:95113771; PMID:7814323 !$#accession I40670 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-87 ##label RES !'##cross-references EMBL:U13663; NID:g535421; PIDN:AAA66206.1; !1PID:g535423 REFERENCE A87249 !$#authors Nierman, W.C.; Feldblyum, T.V.; Paulsen, I.T.; Nelson, K.E.; !1Eisen, J.; Heidelberg, J.F.; Alley, M.; Ohta, N.; Maddock, !1J.R.; Potocka, I.; Nelson, W.C.; Newton, A.; Stephens, C.; !1Phadke, N.D.; Ely, B.; Laub, M.T.; DeBoy, R.T.; Dodson, !1R.J.; Durkin, A.S.; Gwinn, M.L.; Haft, D.H.; Kolonay, J.F.; !1Smit, J.; Craven, M.; Khouri, H.; Shetty, J.; Berry, K.; !1Utterback, T.; Tran, K.; Wolf, A.; Vamathevan, J.; !1Ermolaeva, M.; White, O.; Salzberg, S.L.; Shapiro, L.; !1Venter, J.C.; Fraser, C.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (2001) 98:4136-4141 !$#title Complete Genome Sequence of Caulobacter crescentus. !$#cross-references MUID:21173698; PMID:11259647 !$#accession G87382 !'##status preliminary !'##molecule_type DNA !'##residues 1-87 ##label STO !'##cross-references GB:AE005673; NID:g13422377; PIDN:AAK23059.1; !1GSPDB:GN00148 GENETICS !$#gene fliQ; CC1075 CLASSIFICATION #superfamily flagellar biosynthesis-specific protein SUMMARY #length 87 #molecular-weight 9286 #checksum 938 SEQUENCE /// ENTRY C36955 #type complete TITLE flagellar biosynthesis-specific protein fliQ - Yersinia pestis plasmid pCD1 ORGANISM #formal_name Yersinia pestis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C36955 REFERENCE A36955 !$#authors Fields, K.A.; Plano, G.V.; Straley, S.C. !$#journal J. Bacteriol. (1994) 176:569-579 !$#title A low-Ca(2+) response (LCR) secretion (ysc) locus lies !1within the lcrB region of the LCR plasmid in Yersinia !1pestis. !$#cross-references MUID:94131934; PMID:8300512 !$#accession C36955 !'##status preliminary !'##molecule_type DNA !'##residues 1-79 ##label FIE !'##cross-references GB:L22495; NID:g2465655; PIDN:AAB72202.1; !1PID:g2465660 GENETICS !$#gene yscS !$#genome plasmid CLASSIFICATION #superfamily flagellar biosynthesis-specific protein SUMMARY #length 79 #molecular-weight 8531 #checksum 7118 SEQUENCE /// ENTRY B65058 #type complete TITLE fixC protein homolog b2766 - Escherichia coli (strain K-12) CONTAINS probable quinone reductase (EC 1.6.5.-) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS B65058 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65058 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-433 ##label BLAT !'##cross-references GB:AE000360; GB:U00096; NID:g2367157; !1PIDN:AAC75808.1; PID:g1789125; UWGP:b2766 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily fixC protein KEYWORDS oxidoreductase SUMMARY #length 433 #molecular-weight 47470 #checksum 669 SEQUENCE /// ENTRY C26952 #type complete TITLE fixC protein - Rhizobium meliloti CONTAINS probable quinone reductase (EC 1.6.5.-) ORGANISM #formal_name Rhizobium meliloti DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C26952 REFERENCE A26952 !$#authors Earl, C.D.; Ronson, C.W.; Ausubel, F.M. !$#journal J. Bacteriol. (1987) 169:1127-1136 !$#title Genetic and structural analysis of the Rhizobium meliloti !1fixA, fixB, fixC, and fixX genes. !$#cross-references MUID:87137267; PMID:3029021 !$#accession C26952 !'##molecule_type DNA !'##residues 1-435 ##label EAR !'##cross-references GB:M15546; NID:g340664; PID:g551200 CLASSIFICATION #superfamily fixC protein KEYWORDS oxidoreductase SUMMARY #length 435 #molecular-weight 47288 #checksum 5796 SEQUENCE /// ENTRY S14072 #type complete TITLE fixC protein - Azorhizobium caulinodans CONTAINS probable quinone reductase (EC 1.6.5.-) ORGANISM #formal_name Azorhizobium caulinodans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S14072 REFERENCE S14070 !$#authors Arigoni, F.; Kaminski, P.A.; Hennecke, H.; Elmerich, C. !$#journal Mol. Gen. Genet. (1991) 225:514-520 !$#title Nucleotide sequence of the fixABC region of Azorhizobium !1caulinodans ORS571: similarity of the fixB product with !1eukaryotic flavoproteins, characterization of fixX, and !1identification of nifW. !$#cross-references MUID:91203829; PMID:1850088 !$#accession S14072 !'##status preliminary !'##molecule_type DNA !'##residues 1-435 ##label ARI !'##cross-references EMBL:X55450; NID:g38695; PIDN:CAA39093.1; !1PID:g38698 CLASSIFICATION #superfamily fixC protein KEYWORDS oxidoreductase SUMMARY #length 435 #molecular-weight 48578 #checksum 8378 SEQUENCE /// ENTRY S49189 #type complete TITLE FixC protein - Azotobacter vinelandii CONTAINS probable quinone reductase (EC 1.6.5.-) ORGANISM #formal_name Azotobacter vinelandii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S49189 REFERENCE S49186 !$#authors Wientjens, R.; van Dongen, W.; Haaker, H. !$#submission submitted to the EMBL Data Library, April 1992 !$#description Molecular cloning of fixA, fixB, fixC and fixX genes of !1Azotobacter vinelandii. !$#accession S49189 !'##status preliminary !'##molecule_type DNA !'##residues 1-427 ##label WIE !'##cross-references EMBL:X65515; NID:g510483; PID:g510487 CLASSIFICATION #superfamily fixC protein KEYWORDS oxidoreductase SUMMARY #length 427 #molecular-weight 47730 #checksum 9537 SEQUENCE /// ENTRY C64927 #type complete TITLE probable membrane protein b1691 precursor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS C64927 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64927 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-423 ##label BLAT !'##cross-references GB:AE000264; GB:U00096; NID:g1787978; !1PIDN:AAC74761.1; PID:g1787982; UWGP:b1691 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily hypothetical protein b1691 FEATURE !$1-35 #domain signal sequence #status predicted #label SIG\ !$36-423 #product probable membrane protein b1691 #status !8predicted #label MAT\ !$56-72 #domain transmembrane #status predicted #label TM01\ !$81-97 #domain transmembrane #status predicted #label TM02\ !$103-119 #domain transmembrane #status predicted #label TM03\ !$171-187 #domain transmembrane #status predicted #label TM04\ !$220-236 #domain transmembrane #status predicted #label TM05\ !$259-275 #domain transmembrane #status predicted #label TM06\ !$286-302 #domain transmembrane #status predicted #label TM07\ !$312-328 #domain transmembrane #status predicted #label TM08\ !$345-361 #domain transmembrane #status predicted #label TM09\ !$372-388 #domain transmembrane #status predicted #label TM10 SUMMARY #length 423 #molecular-weight 46339 #checksum 6795 SEQUENCE /// ENTRY B64927 #type complete TITLE probable sugar transport protein b1690 - Escherichia coli (strain K-12) ALTERNATE_NAMES probable membrane protein b1690 ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS B64927 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64927 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-404 ##label BLAT !'##cross-references GB:AE000264; GB:U00096; NID:g1787978; !1PIDN:AAC74760.1; PID:g1787981; UWGP:b1690 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily hypothetical protein b1691 FEATURE !$46-62 #domain transmembrane #status predicted #label TM01\ !$62-78 #region sugar transporter protein signature\ !$74-90 #domain transmembrane #status predicted #label TM02\ !$95-111 #domain transmembrane #status predicted #label TM03\ !$144-178 #domain transmembrane #status predicted #label TM04\ !$249-265 #domain transmembrane #status predicted #label TM05\ !$275-308 #domain transmembrane #status predicted #label TM06 SUMMARY #length 404 #molecular-weight 44608 #checksum 5395 SEQUENCE /// ENTRY E64112 #type complete TITLE bicyclomycin resistance protein homolog - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS E64112 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession E64112 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-398 ##label TIGR !'##cross-references GB:U32804; GB:L42023; NID:g1574170; !1PIDN:AAC22894.1; PID:g1574174; TIGR:HI1242 CLASSIFICATION #superfamily bicyclomycin resistance protein SUMMARY #length 398 #molecular-weight 43458 #checksum 5846 SEQUENCE /// ENTRY E64987 #type complete TITLE bicyclomycin resistance protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS E64987; JN0659 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64987 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-396 ##label BLAT !'##cross-references GB:AE000308; GB:U00096; NID:g1788508; !1PIDN:AAC75243.1; PID:g1788509; UWGP:b2182 !'##experimental_source strain K-12, substrain MG1655 REFERENCE JN0659 !$#authors Bentley, J.; Hyatt, L.S.; Ainley, K.; Parish, J.H.; Herbert, !1R.B.; White, G.R. !$#journal Gene (1993) 127:117-120 !$#title Cloning and sequence analysis of an Escherichia coli gene !1conferring bicyclomycin resistance. !$#cross-references MUID:93252267; PMID:8486276 !$#accession JN0659 !'##molecule_type DNA !'##residues 20-98,'V',100-245,'I',247-396 ##label BEN !'##cross-references EMBL:X63703; NID:g41064; PIDN:CAA45230.1; !1PID:g41065 GENETICS !$#gene bcr CLASSIFICATION #superfamily bicyclomycin resistance protein KEYWORDS antibiotic resistance SUMMARY #length 396 #molecular-weight 43352 #checksum 5671 SEQUENCE /// ENTRY S44207 #type complete TITLE hypothetical protein 337 - Coxiella burnetii ORGANISM #formal_name Coxiella burnetii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S44207 REFERENCE S44206 !$#authors Willems, H.; Thiele, D.; Oswald, W.; Krauss, H. !$#submission submitted to the EMBL Data Library, April 1994 !$#accession S44207 !'##status preliminary !'##molecule_type DNA !'##residues 1-338 ##label WIL !'##cross-references EMBL:X78969 CLASSIFICATION #superfamily bicyclomycin resistance protein SUMMARY #length 338 #molecular-weight 36914 #checksum 8401 SEQUENCE /// ENTRY B65169 #type complete TITLE multidrug resistance protein d - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS B65169 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65169 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-396 ##label BLAT !'##cross-references GB:AE000445; GB:U00096; NID:g1790105; !1PIDN:AAC76696.1; PID:g1790107; UWGP:b3673 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene emrD CLASSIFICATION #superfamily bicyclomycin resistance protein SUMMARY #length 396 #molecular-weight 42460 #checksum 8572 SEQUENCE /// ENTRY E64794 #type complete TITLE ybdQ protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS E64794 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64794 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-142 ##label BLAT !'##cross-references GB:AE000166; GB:U00096; NID:g1786819; !1PIDN:AAC73708.1; PID:g1786824; UWGP:b0607 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ybdQ CLASSIFICATION #superfamily Escherichia coli ybdQ protein SUMMARY #length 142 #molecular-weight 15935 #checksum 2509 SEQUENCE /// ENTRY C64888 #type complete TITLE conserved hypothetical protein b1376 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS C64888 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64888 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-168 ##label BLAT !'##cross-references GB:AE000234; GB:U00096; NID:g1787633; !1PIDN:AAC74458.1; PID:g1787640; UWGP:b1376 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily Escherichia coli ybdQ protein SUMMARY #length 168 #molecular-weight 18503 #checksum 3273 SEQUENCE /// ENTRY A64372 #type complete TITLE hypothetical protein homolog MJ0577 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A64372 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession A64372 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-162 ##label BUL !'##cross-references GB:U67506; GB:L77117; NID:g1591274; !1PIDN:AAB98568.1; PID:g1591284; TIGR:MJ0577 GENETICS !$#map_position FOR512975-513463 !$#start_codon GTG CLASSIFICATION #superfamily Escherichia coli ybdQ protein SUMMARY #length 162 #molecular-weight 18338 #checksum 9028 SEQUENCE /// ENTRY E64833 #type complete TITLE nitrate transport protein nrtB homolog ycbM - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS E64833 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64833 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-278 ##label BLAT !'##cross-references GB:AE000195; GB:U00096; NID:g1787156; !1PIDN:AAC74020.1; PID:g1787165; UWGP:b0934 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ycbM CLASSIFICATION #superfamily Synechococcus nitrate transport protein nrtB KEYWORDS transmembrane protein; transport protein FEATURE !$23-39 #domain transmembrane #status predicted #label TM1\ !$85-101 #domain transmembrane #status predicted #label TM2\ !$121-137 #domain transmembrane #status predicted #label TM3\ !$140-156 #domain transmembrane #status predicted #label TM4\ !$177-193 #domain transmembrane #status predicted #label TM5\ !$196-212 #domain transmembrane #status predicted #label TM6\ !$233-249 #domain transmembrane #status predicted #label TM7 SUMMARY #length 278 #molecular-weight 30636 #checksum 5322 SEQUENCE /// ENTRY I39928 #type complete TITLE nitrate transport protein nrtB homolog ygaM - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS I39928; H69816 REFERENCE I39839 !$#authors Quirk, P.G.; Guffanti, A.A.; Clejan, S.; Cheng, J.; !1Krulwich, T.A. !$#journal Biochim. Biophys. Acta (1994) 1186:27-34 !$#title Isolation of Tn917 insertional mutants of Bacillus subtilis !1that are resistant to the protonophore carbonyl cyanide !1m-chlorophenylhydrazone. !$#cross-references MUID:94281248; PMID:8011666 !$#accession I39928 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-276 ##label RES !'##cross-references GB:L16808; NID:g438471; PIDN:AAA64349.1; !1PID:g438473 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69816 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-276 ##label KUN !'##cross-references GB:Z99108; GB:AL009126; NID:g2633055; !1PIDN:CAB12713.1; PID:g2633208 !'##experimental_source strain 168 GENETICS !$#gene ygaM CLASSIFICATION #superfamily Synechococcus nitrate transport protein nrtB SUMMARY #length 276 #molecular-weight 30240 #checksum 3341 SEQUENCE /// ENTRY E64351 #type complete TITLE nitrate transport protein nrtB homolog - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E64351 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession E64351 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-267 ##label BUL !'##cross-references GB:U67493; GB:L77117; NID:g2826279; !1PIDN:AAB98402.1; PID:g1591119; TIGR:MJ0413 GENETICS !$#map_position REV373335-372532 !$#start_codon GTG CLASSIFICATION #superfamily Synechococcus nitrate transport protein nrtB SUMMARY #length 267 #molecular-weight 29043 #checksum 5314 SEQUENCE /// ENTRY S77447 #type complete TITLE nitrate transport protein nrtB homolog - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein sll1081 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S77447 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S77447 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-280 ##label KAN !'##cross-references EMBL:D90905; GB:AB001339; NID:g1652360; !1PIDN:BAA17294.1; PID:g1652372 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily Synechococcus nitrate transport protein nrtB SUMMARY #length 280 #molecular-weight 30980 #checksum 5180 SEQUENCE /// ENTRY S30892 #type complete TITLE nitrate transport protein nrtB - Synechococcus sp. (strain PCC 7942) ORGANISM #formal_name Synechococcus sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S30892 REFERENCE S30891 !$#authors Omata, T.; Andriesse, X.; Hirano, A. !$#journal Mol. Gen. Genet. (1993) 236:193-202 !$#title Identification and characterization of a gene cluster !1involved in nitrate transport in the cyanobacterium !1Synechococcus sp. PCC7942. !$#cross-references MUID:93173091; PMID:8437564 !$#accession S30892 !'##molecule_type DNA !'##residues 1-279 ##label OMA !'##cross-references EMBL:X61625; NID:g48968; PID:g48970 GENETICS !$#gene nrtB CLASSIFICATION #superfamily Synechococcus nitrate transport protein nrtB KEYWORDS transmembrane protein SUMMARY #length 279 #molecular-weight 30207 #checksum 6745 SEQUENCE /// ENTRY S56642 #type complete TITLE nitrate transport protein nrtB [similarity] - Phormidium laminosum ORGANISM #formal_name Phormidium laminosum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 20-Oct-2000 ACCESSIONS S56642; S58739 REFERENCE S56640 !$#authors Merchan, F.; Prieto, R.; Kindle, K.L.; Llama, M.J.; Serra, !1J.L.; Fernandez, E. !$#journal Plant Mol. Biol. (1995) 27:1037-1042 !$#title Isolation, sequence and expression in Escherichia coli of !1the nitrite reductase gene from the filamentous, !1thermophilic cyanobacterium Phormidium laminosum. !$#cross-references MUID:95284340; PMID:7766873 !$#accession S56642 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-279 ##label MER1 !'##cross-references EMBL:Z19598; NID:g1154890; PID:g887567; !1PIDN:CAA79657.1 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1993 REFERENCE S58738 !$#authors Merchan, F.; Kindle, K.L.; Llama, M.J.; Serra, J.L.; !1Fernandez, E. !$#journal Plant Mol. Biol. (1995) 28:759-766 !$#title Cloning and sequencing of the nitrate transport system from !1the thermophilic, filamentous cyanobacterium Phormidium !1laminosum: comparative analysis with the homologous system !1from Synechococcus sp. PCC 7942. !$#cross-references MUID:95375238; PMID:7647306 !$#accession S58739 !'##status preliminary !'##molecule_type DNA !'##residues 1-279 ##label MER2 !'##cross-references EMBL:Z19598; NID:g1154890; PID:g887567; !1PIDN:CAA79657.1 GENETICS !$#gene nrtB CLASSIFICATION #superfamily Synechococcus nitrate transport protein nrtB KEYWORDS transmembrane protein SUMMARY #length 279 #molecular-weight 30204 #checksum 1540 SEQUENCE /// ENTRY F64149 #type complete TITLE nitrate transport protein nrtB homolog HI0355 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS F64149 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession F64149 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-260 ##label TIGR !'##cross-references GB:L42023; TIGR:HI0355 !'##note best homolog was a hypothetical protein from Bacillus subtilis CLASSIFICATION #superfamily Synechococcus nitrate transport protein nrtB SUMMARY #length 260 #molecular-weight 28624 #checksum 8059 SEQUENCE /// ENTRY JC6192 #type complete TITLE nitrate transport protein nrtB homolog - Mycobacterium smegmatis ORGANISM #formal_name Mycobacterium smegmatis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS JC6192; S77668 REFERENCE JC6190 !$#authors Barsom, E.K.; Hatfull, G.F. !$#journal Gene (1997) 185:127-132 !$#title A putative ABC-transport operon of Mycobacterium smegmatis. !$#cross-references MUID:97186707; PMID:9034323 !$#accession JC6192 !'##molecule_type DNA !'##residues 1-233 ##label BAR !'##cross-references GB:U50335; NID:g1477566; PID:g1477571 REFERENCE S77663 !$#authors Barsom, E.K.; Hatfull, G.F. !$#journal Mol. Microbiol. (1996) 21:159-170 !$#title Characterization of a Mycobacterium smegmatis gene that !1confers resistance to phages L5 and D29 when overexpressed. !$#cross-references MUID:97000357; PMID:8843442 !$#accession S77668 !'##status preliminary !'##molecule_type DNA !'##residues 1-233 ##label BA2 !'##cross-references EMBL:U50335; NID:g1477566; PIDN:AAB41655.1; !1PID:g1477571 COMMENT This protein is a member of subroup of integral membrane !1components, and it functions as a permease. CLASSIFICATION #superfamily Synechococcus nitrate transport protein nrtB SUMMARY #length 233 #molecular-weight 25502 #checksum 5987 SEQUENCE /// ENTRY S78606 #type complete TITLE probable transport system integral membrane component tauC - Escherichia coli (strain K-12) ALTERNATE_NAMES sulfate starvation-induced protein ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS S78606; G64764; S78614 REFERENCE S78604 !$#authors van der Ploeg, J.R.; Weiss, M.A.; Saller, E.; Nashimoto, H.; !1Saito, N.; Kertesz, M.A.; Leisinger, T. !$#journal J. Bacteriol. (1996) 178:5438-5446 !$#title Identification of sulfate starvation-regulated genes in !1Escherichia coli: a gene cluster involved in the utilization !1of taurine as a sulfur source. !$#cross-references MUID:96404792; PMID:8808933 !$#accession S78606 !'##molecule_type DNA !'##residues 1-275 ##label VAN !'##cross-references EMBL:D85613; EMBL:D64043; NID:g1384055; !1PIDN:BAA12840.1; PID:g1384060 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64764 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-73,'A',75-275 ##label BLAT !'##cross-references GB:AE000143; GB:U00096; NID:g1786554; !1PIDN:AAC73470.1; PID:g1786564; UWGP:b0367 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene tauC FUNCTION !$#description required for the utilization of taurine as a sulfur source CLASSIFICATION #superfamily Synechococcus nitrate transport protein nrtB KEYWORDS inner membrane; transmembrane protein; transport system FEATURE !$31-47 #domain transmembrane #status predicted #label TM1\ !$87-103 #domain transmembrane #status predicted #label TM2\ !$125-141 #domain transmembrane #status predicted #label TM3\ !$146-162 #domain transmembrane #status predicted #label TM4\ !$186-202 #domain transmembrane #status predicted #label TM5\ !$205-221 #domain transmembrane #status predicted #label TM6\ !$240-256 #domain transmembrane #status predicted #label TM7 SUMMARY #length 275 #molecular-weight 29897 #checksum 2906 SEQUENCE /// ENTRY E64982 #type complete TITLE yohK protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS E64982 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64982 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-231 ##label BLAT !'##cross-references GB:AE000303; GB:U00096; NID:g1788456; !1PIDN:AAC75203.1; PID:g1788464; UWGP:b2142 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yohK CLASSIFICATION #superfamily yohK protein SUMMARY #length 231 #molecular-weight 24469 #checksum 1831 SEQUENCE /// ENTRY D64170 #type complete TITLE hypothetical protein HI1298 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS D64170; T09426 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession D64170 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-231 ##label TIGR !'##cross-references GB:U32809; GB:L42023; NID:g3212217; !1PIDN:AAC22944.1; PID:g1574756; TIGR:HI1298 !'##note best homolog was a hypothetical protein from Escherichia coli REFERENCE Z16667 !$#authors White, O.; Clayton, R.A.; Kerlavage, A.R.; Fleischmann, !1R.D.; Peterson, J.; Hickey, E.; Dodson, R.; Gwinn, M. !$#submission submitted to the EMBL Data Library, May 1998 !$#accession T09426 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-231 ##label WHI !'##cross-references EMBL:U32809; NID:g3212217; PID:g1574756 GENETICS !$#gene HI1298 CLASSIFICATION #superfamily yohK protein SUMMARY #length 231 #molecular-weight 24886 #checksum 7110 SEQUENCE /// ENTRY S39677 #type complete TITLE conserved hypothetical protein ywbG - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S39677; E70051 REFERENCE S39655 !$#authors Glaser, P.; Kunst, F.; Arnaud, M.; Coudart, M.P.; Gonzales, !1W.; Hullo, M.F.; Ionescu, M.; Lubochinsky, B.; Marcelino, !1L.; Moszer, I.; Presecan, E.; Santana, M.; Schneider, E.; !1Schweizer, J.; Vertes, A.; Rapoport, G.; Danchin, A. !$#journal Mol. Microbiol. (1993) 10:371-384 !$#title Bacillus subtilis genome project: cloning and sequencing of !1the 97 kb region from 325 degrees to 333 degrees. !$#cross-references MUID:95020537; PMID:7934828 !$#accession S39677 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-241 ##label GLA !'##cross-references EMBL:X73124; NID:g413923; PIDN:CAA51578.1; !1PID:g580868 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1993 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E70051 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-241 ##label KUN !'##cross-references GB:Z99123; GB:AL009126; NID:g2636240; !1PIDN:CAB15859.1; PID:g2636368 !'##experimental_source strain 168 GENETICS !$#gene ywbG !$#start_codon GTG CLASSIFICATION #superfamily yohK protein SUMMARY #length 241 #molecular-weight 25813 #checksum 5527 SEQUENCE /// ENTRY E64990 #type complete TITLE NapD protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Dec-2002 ACCESSIONS E64990 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64990 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-87 ##label BLAT !'##cross-references GB:AE000309; GB:U00096; NID:g1788520; !1PIDN:AAC75267.1; PID:g1788535; UWGP:b2207 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yojF CLASSIFICATION #superfamily NapD protein SUMMARY #length 87 #molecular-weight 9468 #checksum 1400 SEQUENCE /// ENTRY I64148 #type complete TITLE hypothetical protein HI0343 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Dec-2002 ACCESSIONS I64148 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession I64148 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-93 ##label TIGR !'##cross-references GB:U32719; GB:L42023; NID:g1573310; !1PIDN:AAC22005.1; PID:g1573314; TIGR:HI0343 !'##note best homolog was a hypothetical protein from Escherichia coli CLASSIFICATION #superfamily NapD protein SUMMARY #length 93 #molecular-weight 10516 #checksum 6701 SEQUENCE /// ENTRY E65001 #type complete TITLE hypothetical protein b2295 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS E65001 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65001 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-151 ##label BLAT !'##cross-references GB:AE000318; GB:U00096; NID:g1788623; !1PIDN:AAC75355.1; PID:g1788632; UWGP:b2295 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily hypothetical protein HI1205 SUMMARY #length 151 #molecular-weight 17213 #checksum 8258 SEQUENCE /// ENTRY A64022 #type complete TITLE hypothetical protein HI1205 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS A64022 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession A64022 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-147 ##label TIGR !'##cross-references GB:U32800; GB:L42023; NID:g1574133; !1PIDN:AAC22859.1; PID:g1574135; TIGR:HI1205 CLASSIFICATION #superfamily hypothetical protein HI1205 SUMMARY #length 147 #molecular-weight 17270 #checksum 3472 SEQUENCE /// ENTRY C64151 #type complete TITLE C4-dicarboxylate transport protein homolog HI0400 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS C64151 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession C64151 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-95 ##label TIGR !'##cross-references GB:U32723; GB:L42023; NID:g1573363; !1PIDN:AAC22059.1; PID:g1573371; TIGR:HI0400 !'##note best homolog was a hypothetical protein from Escherichia coli CLASSIFICATION #superfamily C4-dicarboxylate carrier protein SUMMARY #length 95 #molecular-weight 10342 #checksum 480 SEQUENCE /// ENTRY E65007 #type complete TITLE C4-dicarboxylate transport protein homolog b2343 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS E65007 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65007 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-102 ##label BLAT !'##cross-references GB:AE000323; GB:U00096; NID:g1788684; !1PIDN:AAC75403.1; PID:g1788685; UWGP:b2343 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily C4-dicarboxylate carrier protein SUMMARY #length 102 #molecular-weight 11300 #checksum 533 SEQUENCE /// ENTRY I64010 #type complete TITLE C4-dicarboxylate transport protein homolog HI0636 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS I64010 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession I64010 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-96 ##label TIGR !'##cross-references GB:U32746; GB:L42023; NID:g1573626; !1PIDN:AAC22295.1; PID:g1573632; TIGR:HI0636 CLASSIFICATION #superfamily C4-dicarboxylate carrier protein SUMMARY #length 96 #molecular-weight 10966 #checksum 1426 SEQUENCE /// ENTRY S40865 #type complete TITLE C4-dicarboxylate transport protein homolog (tpia-fpr intergenic region) - Escherichia coli (strain K-12) ALTERNATE_NAMES hypothetical protein o99 ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS S40865; E65198 REFERENCE S40802 !$#authors Plunkett III, G.; Burland, V.; Daniels, D.L.; Blattner, F.R. !$#journal Nucleic Acids Res. (1993) 21:3391-3398 !$#title Analysis of the Escherichia coli genome. III. DNA sequence !1of the region from 87.2 to 89.2 minutes. !$#cross-references MUID:93347969; PMID:8346018 !$#accession S40865 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-99 ##label PLU !'##cross-references EMBL:L19201; NID:g304961; PIDN:AAB03054.1; !1PID:g305025 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1993 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65198 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-99 ##label BLAT !'##cross-references GB:AE000467; GB:U00096; NID:g1790356; !1PIDN:AAC76904.1; PID:g1790357; UWGP:b3922 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yiiS CLASSIFICATION #superfamily C4-dicarboxylate carrier protein SUMMARY #length 99 #molecular-weight 10776 #checksum 9767 SEQUENCE /// ENTRY S49042 #type complete TITLE global stress protein gspA - Legionella pneumophila ORGANISM #formal_name Legionella pneumophila DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S49042 REFERENCE S49039 !$#authors Abu Kwaik, Y.; Engleberg, N.C. !$#journal Mol. Microbiol. (1994) 13:243-251 !$#title Cloning and molecular characterization of a Legionella !1pneumophila gene induced by intracellular infection and by !1various in vitro stress conditions. !$#cross-references MUID:95075310; PMID:7984104 !$#accession S49042 !'##molecule_type DNA !'##residues 1-166 ##label ABU !'##cross-references EMBL:Z46737 GENETICS !$#gene gspA CLASSIFICATION #superfamily heat shock protein ibpA KEYWORDS stress-induced protein SUMMARY #length 166 #molecular-weight 19023 #checksum 6568 SEQUENCE /// ENTRY G65206 #type complete TITLE NADH pyrophosphatase (EC 3.6.1.-) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS G65206 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65206 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-257 ##label BLAT !'##cross-references GB:AE000473; GB:U00096; NID:g2367336; !1PIDN:AAC76970.1; PID:g1790429; UWGP:b3996 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yjaD CLASSIFICATION #superfamily hypothetical protein HI0432; mutT domain !1homology KEYWORDS hydrolase FEATURE !$154-186 #domain mutT domain homology #label MUTT SUMMARY #length 257 #molecular-weight 29774 #checksum 9848 SEQUENCE /// ENTRY F64152 #type complete TITLE hypothetical protein HI0432 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS F64152 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession F64152 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-264 ##label TIGR !'##cross-references GB:U32726; GB:L42023; NID:g1573399; !1PIDN:AAC22091.1; PID:g1573407; TIGR:HI0432 CLASSIFICATION #superfamily hypothetical protein HI0432; mutT domain !1homology FEATURE !$158-190 #domain mutT domain homology #label MUT SUMMARY #length 264 #molecular-weight 30163 #checksum 9965 SEQUENCE /// ENTRY G65213 #type complete TITLE hypothetical 15.7 kD protein in tyrB-uvrA intergenic region - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Dec-2002 ACCESSIONS G65213 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65213 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-138 ##label BLAT !'##cross-references GB:AE000479; GB:U00096; NID:g2367340; !1PIDN:AAC77026.1; PID:g1790491; UWGP:b4056 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yjbQ CLASSIFICATION #superfamily uncharacterized conserved protein SUMMARY #length 138 #molecular-weight 15656 #checksum 6353 SEQUENCE /// ENTRY S75650 #type complete TITLE hypothetical protein sll1880 - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Dec-2002 ACCESSIONS S75650 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75650 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-147 ##label KAN !'##cross-references EMBL:D90912; GB:AB001339; NID:g1653228; !1PIDN:BAA18211.1; PID:g1653296 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily uncharacterized conserved protein SUMMARY #length 147 #molecular-weight 16436 #checksum 7510 SEQUENCE /// ENTRY H64434 #type complete TITLE hypothetical protein homolog MJ1081 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Dec-2002 ACCESSIONS H64434 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession H64434 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-138 ##label BUL !'##cross-references GB:U67551; GB:L77117; NID:g1591728; !1PIDN:AAB99083.1; PID:g1591729; TIGR:MJ1081 GENETICS !$#map_position FOR1021224-1021640 !$#start_codon TTG CLASSIFICATION #superfamily uncharacterized conserved protein SUMMARY #length 138 #molecular-weight 15613 #checksum 4949 SEQUENCE /// ENTRY H64744 #type complete TITLE yaeD protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS H64744 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64744 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-191 ##label BLAT !'##cross-references GB:AE000129; GB:U00096; NID:g1786395; !1PIDN:AAC73311.1; PID:g1786399; UWGP:b0200 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yaeD CLASSIFICATION #superfamily lmbK protein SUMMARY #length 191 #molecular-weight 21294 #checksum 716 SEQUENCE /// ENTRY D64627 #type complete TITLE conserved hypothetical protein HP0860 - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS D64627 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession D64627 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-173 ##label TOM !'##cross-references GB:AE000596; GB:AE000511; NID:g2313982; !1PIDN:AAD07906.1; PID:g2313992; TIGR:HP0860 CLASSIFICATION #superfamily lmbK protein SUMMARY #length 173 #molecular-weight 19994 #checksum 2019 SEQUENCE /// ENTRY S76604 #type complete TITLE hypothetical protein - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S76604 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76604 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-161 ##label KAN !'##cross-references EMBL:D64004; GB:AB001339; NID:g1001701; !1PID:g1001711 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily lmbK protein SUMMARY #length 161 #molecular-weight 17385 #checksum 2961 SEQUENCE /// ENTRY S44958 #type complete TITLE lmbK protein - Streptomyces lincolnensis ORGANISM #formal_name Streptomyces lincolnensis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S69820; S44958 REFERENCE S69805 !$#authors Peschke, U.; Schmidt, H.; Zhang, H.Z.; Piepersberg, W. !$#journal Mol. Microbiol. (1995) 16:1137-1156 !$#title Molecular characterization of the lincomycin-production gene !1cluster of Streptomyces lincolnensis 78-11. !$#cross-references MUID:96020646; PMID:8577249 !$#accession S69820 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-190 ##label PE2 !'##cross-references EMBL:X79146; NID:g499194; PID:g487701 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1May 1994 GENETICS !$#gene lmbK CLASSIFICATION #superfamily lmbK protein SUMMARY #length 190 #molecular-weight 20298 #checksum 7947 SEQUENCE /// ENTRY H64746 #type complete TITLE yafJ protein - Escherichia coli (strain K-12) ALTERNATE_NAMES protein b0223 ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS H64746 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64746 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-255 ##label BLAT !'##cross-references GB:AE000131; GB:U00096; NID:g1786415; !1PIDN:AAC73327.1; PID:g1786417; UWGP:b0223 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yafJ CLASSIFICATION #superfamily hypothetical protein HI1037 SUMMARY #length 255 #molecular-weight 28635 #checksum 7116 SEQUENCE /// ENTRY H64018 #type complete TITLE hypothetical protein HI1037 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS H64018 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession H64018 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-294 ##label TIGR !'##cross-references GB:U32784; GB:L42023; NID:g3212210; !1PIDN:AAC22697.1; PID:g1574070; TIGR:HI1037 CLASSIFICATION #superfamily hypothetical protein HI1037 SUMMARY #length 294 #molecular-weight 33182 #checksum 1199 SEQUENCE /// ENTRY B64489 #type complete TITLE hypothetical protein MJ1515 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B64489 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession B64489 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-355 ##label BUL !'##cross-references GB:U67592; GB:L77117; NID:g2826425; !1PIDN:AAB99533.1; PID:g1592147; TIGR:MJ1515 COMMENT Residues 1-200 appear to be homologous to PIR:H64746 and !1other members of that superfamily. GENETICS !$#map_position FOR1490086-1491153 CLASSIFICATION #superfamily hypothetical protein MJ1515 SUMMARY #length 355 #molecular-weight 41888 #checksum 6765 SEQUENCE /// ENTRY H64810 #type complete TITLE ybgR protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS H64810 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64810 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-313 ##label BLAT !'##cross-references GB:AE000177; GB:U00096; NID:g1786955; !1PIDN:AAC73839.1; PID:g1786966; UWGP:b0752 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ybgR CLASSIFICATION #superfamily zinc transporter ZnT-2 KEYWORDS transmembrane protein FEATURE !$21-37 #domain transmembrane #status predicted #label TM1\ !$54-70 #domain transmembrane #status predicted #label TM2\ !$90-106 #domain transmembrane #status predicted #label TM3\ !$126-142 #domain transmembrane #status predicted #label TM4\ !$164-180 #domain transmembrane #status predicted #label TM5\ !$188-204 #domain transmembrane #status predicted #label TM6 SUMMARY #length 313 #molecular-weight 34678 #checksum 4741 SEQUENCE /// ENTRY JC4701 #type complete TITLE cadmium, zinc, cobalt divalent cation resistant determinant D - Alcaligenes sp. ORGANISM #formal_name Alcaligenes sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JC4701 REFERENCE JC4698 !$#authors Kunito, T.; Kusano, T.; Oyaizu, H.; Senoo, K.; Kanazawa, S.; !1Matsumoto, S. !$#journal Biosci. Biotechnol. Biochem. (1996) 60:699-704 !$#title Cloning and sequence analysis of czc genes in Alcaligenes !1sp. strain CT14. !$#cross-references MUID:96219090; PMID:8829543 !$#accession JC4701 !'##molecule_type DNA !'##residues 1-316 ##label KUN !'##cross-references DDBJ:D67024 GENETICS !$#gene czcD CLASSIFICATION #superfamily zinc transporter ZnT-2 SUMMARY #length 316 #molecular-weight 33741 #checksum 4808 SEQUENCE /// ENTRY S70632 #type complete TITLE zinc transporter ZnT-2 - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S70632 REFERENCE S70632 !$#authors Palmiter, R.D.; Cole, T.B.; Findley, S.D. !$#journal EMBO J. (1996) 15:1784-1791 !$#title ZnT-2, a mammalian protein that confers resistance to zinc !1by facilitating vesicular sequestration. !$#cross-references MUID:96203098; PMID:8617223 !$#accession S70632 !'##status preliminary !'##molecule_type mRNA !'##residues 1-359 ##label PAL !'##cross-references EMBL:U50927; NID:g1256377; PIDN:AAB02775.1; !1PID:g1256378 GENETICS !$#gene ZnT-2 !$#start_codon CTG CLASSIFICATION #superfamily zinc transporter ZnT-2 SUMMARY #length 359 #molecular-weight 39276 #checksum 2497 SEQUENCE /// ENTRY S75583 #type complete TITLE hypothetical protein sll1263 - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S75583 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75583 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-310 ##label KAN !'##cross-references EMBL:D90912; GB:AB001339; NID:g1653228; !1PIDN:BAA18144.1; PID:g1653229 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily zinc transporter ZnT-2 SUMMARY #length 310 #molecular-weight 33324 #checksum 4772 SEQUENCE /// ENTRY D33830 #type complete TITLE cation efflux system membrane protein czcD - Alcaligenes eutrophus ORGANISM #formal_name Alcaligenes eutrophus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 29-Oct-1999 ACCESSIONS D33830 REFERENCE A33830 !$#authors Nies, D.H.; Nies, A.; Chu, L.; Silver, S. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1989) 86:7351-7355 !$#title Expression and nucleotide sequence of a plasmid-determined !1divalent cation efflux system from Alcaligenes eutrophus. !$#cross-references MUID:90017477; PMID:2678100 !$#accession D33830 !'##status preliminary !'##molecule_type DNA !'##residues 1-199 ##label NIE !'##cross-references GB:M26073 COMMENT This sequence appears to be homologous to PIR:H64810 and !1other members of that superfamily. CLASSIFICATION #superfamily membrane protein czcD KEYWORDS membrane protein SUMMARY #length 199 #molecular-weight 21256 #checksum 8057 SEQUENCE /// ENTRY F69831 #type complete TITLE iron(III) dicitrate-binding protein homolog yhfQ - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F69831 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69831 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-348 ##label KUN !'##cross-references GB:Z99109; GB:AL009126; NID:g2633260; !1PIDN:CAB12873.1; PID:g2633369 !'##experimental_source strain 168 GENETICS !$#gene yhfQ CLASSIFICATION #superfamily iron(III) dicitrate transport protein SUMMARY #length 348 #molecular-weight 38551 #checksum 7818 SEQUENCE /// ENTRY C69805 #type complete TITLE iron(III) dicitrate transport permease homolog yfiY - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69805 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69805 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-325 ##label KUN !'##cross-references GB:Z99108; GB:AL009126; NID:g2633055; !1PIDN:CAB12673.1; PID:g2633168 !'##experimental_source strain 168 GENETICS !$#gene yfiY CLASSIFICATION #superfamily iron(III) dicitrate transport protein SUMMARY #length 325 #molecular-weight 36304 #checksum 4007 SEQUENCE /// ENTRY S74441 #type complete TITLE iron(III) dicitrate transport system permease protein fecB - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein slr1319 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S74441 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74441 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-315 ##label KAN !'##cross-references EMBL:D90899; GB:AB001339; NID:g1651650; !1PIDN:BAA16593.1; PID:g1651665 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene fecB CLASSIFICATION #superfamily iron(III) dicitrate transport protein KEYWORDS iron transport SUMMARY #length 315 #molecular-weight 34868 #checksum 7094 SEQUENCE /// ENTRY S54820 #type complete TITLE CbrA protein - Erwinia chrysanthemi ORGANISM #formal_name Erwinia chrysanthemi DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S54820 REFERENCE S54820 !$#authors Mahe, B.; Masclaux, C.; Rauscher, L.; Enard, C.; Expert, D. !$#submission submitted to the EMBL Data Library, May 1995 !$#description Differential expression of two siderophore-dependent-iron !1acquisition pathways in Erwinia chrysanthemi 3937: !1characterization of a novel ferrisiderophore permease of the !1ABC transporter family. !$#accession S54820 !'##status preliminary !'##molecule_type DNA !'##residues 1-305 ##label MAH !'##cross-references EMBL:X87208; NID:g809540; PID:g809541 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily iron(III) dicitrate transport protein SUMMARY #length 305 #molecular-weight 34011 #checksum 3538 SEQUENCE /// ENTRY B69812 #type complete TITLE ferrichrome ABC transporter (binding prote) homolog yfmC - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69812 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69812 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-315 ##label KUN !'##cross-references GB:Z99108; GB:AL009126; NID:g2633055; !1PIDN:CAB12581.1; PID:g2633076 !'##experimental_source strain 168 GENETICS !$#gene yfmC CLASSIFICATION #superfamily iron(III) dicitrate transport protein SUMMARY #length 315 #molecular-weight 35020 #checksum 7136 SEQUENCE /// ENTRY E69763 #type complete TITLE probable ferrichrome ABC transporter yclQ - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69763 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69763 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-317 ##label KUN !'##cross-references GB:Z99106; GB:AL009126; NID:g2632653; !1PIDN:CAB12191.1; PID:g2632684 !'##experimental_source strain 168 GENETICS !$#gene yclQ CLASSIFICATION #superfamily iron(III) dicitrate transport protein SUMMARY #length 317 #molecular-weight 34791 #checksum 7282 SEQUENCE /// ENTRY A29928 #type complete TITLE membrane-associated 40K protein precursor - Vibrio anguillarum plasmid pJM1 ORGANISM #formal_name Vibrio anguillarum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 18-Aug-2000 ACCESSIONS A29928; C41671 REFERENCE A92707 !$#authors Actis, L.A.; Tolmasky, M.E.; Farrell, D.H.; Crosa, J.H. !$#journal J. Biol. Chem. (1988) 263:2853-2860 !$#title Genetic and molecular characterization of essential !1components of the Vibrio anguillarum plasmid-mediated !1iron-transport system. !$#cross-references MUID:88139336; PMID:2830268 !$#accession A29928 !'##molecule_type DNA !'##residues 1-322 ##label ACT !'##cross-references GB:J03529; NID:g150755; PIDN:AAA91580.1; !1PID:g150756 REFERENCE A41671 !$#authors Koester, W.L.; Actis, L.A.; Waldbeser, L.S.; Tolmasky, M.E.; !1Crosa, J.H. !$#journal J. Biol. Chem. (1991) 266:23829-23833 !$#title Molecular characterization of the iron transport system !1mediated by the pJM1 plasmid in Vibrio anguillarum 775. !$#cross-references MUID:92084677; PMID:1748657 !$#accession C41671 !'##status preliminary !'##molecule_type DNA !'##residues 1-154 ##label KOE !'##cross-references GB:M74068 CLASSIFICATION #superfamily iron(III) dicitrate transport protein KEYWORDS membrane protein FEATURE !$1-22 #domain signal sequence #status predicted #label SIG\ !$23-322 #product membrane-associated 40K protein #status !8predicted #label MAT SUMMARY #length 322 #molecular-weight 35635 #checksum 3447 SEQUENCE /// ENTRY E64821 #type complete TITLE yliI protein precursor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS E64821 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64821 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-371 ##label BLAT !'##cross-references GB:AE000186; GB:U00096; NID:g1787058; !1PIDN:AAC73924.1; PID:g1787060; UWGP:b0837 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yliI CLASSIFICATION #superfamily hypothetical protein b0837 FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-371 #product yliI protein #status predicted #label MAT SUMMARY #length 371 #molecular-weight 41054 #checksum 7481 SEQUENCE /// ENTRY S74981 #type complete TITLE glucose dehydrogenase-B - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein slr1608 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S74981 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74981 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-412 ##label KAN !'##cross-references EMBL:D90902; GB:AB001339; NID:g1652027; !1PIDN:BAA17021.1; PID:g1652096 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene gdhB CLASSIFICATION #superfamily hypothetical protein b0837 SUMMARY #length 412 #molecular-weight 45119 #checksum 3690 SEQUENCE /// ENTRY C64157 #type complete TITLE hypothetical protein HI0719 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS C64157 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession C64157 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-130 ##label TIGR !'##cross-references GB:U32754; GB:L42023; NID:g1573711; !1PIDN:AAC22376.1; PID:g1573721; TIGR:HI0719 !'##note best homolog was a hypothetical protein from Escherichia coli CLASSIFICATION #superfamily hypothetical protein HI0719 SUMMARY #length 130 #molecular-weight 14024 #checksum 441 SEQUENCE /// ENTRY S56682 #type complete TITLE hypothetical protein 2 - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S56682; S77063 REFERENCE S56682 !$#authors Chavez, S.; Reyes, J.C.; Chauvat, F.; Florencio, F.J.; !1Candau, P. !$#journal Plant Mol. Biol. (1995) 28:173-188 !$#title The NADP-glutamate dehydrogenase of the cyanobacterium !1Synechocystis 6803: cloning, transcriptional analysis and !1disruption of the gdhA gene. !$#cross-references MUID:95306786; PMID:7787182 !$#accession S56682 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-130 ##label CHA !'##cross-references EMBL:X77454; NID:g1006749; PID:g1006750 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1994 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S77063 !'##status preliminary !'##molecule_type DNA !'##residues 1-130 ##label KAN !'##cross-references EMBL:D64005; GB:AB001339; NID:g1001779; !1PID:g1006602 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily hypothetical protein HI0719 SUMMARY #length 130 #molecular-weight 13834 #checksum 252 SEQUENCE /// ENTRY S66077 #type complete TITLE conserved hypothetical protein yabJ - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S66077; B69739 REFERENCE S65967 !$#authors Ogasawara, N.; Nakai, S.; Yoshikawa, H. !$#journal DNA Res. (1994) 1:1-14 !$#title Systematic sequencing of the 180 kilobase region of the !1Bacillus subtilis chromosome containing the replication !1origin. !$#cross-references MUID:96051385; PMID:7584024 !$#accession S66077 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-125 ##label OGA !'##cross-references EMBL:D26185; NID:g467326; PIDN:BAA05283.1; !1PID:g467437 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1993 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69739 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-125 ##label KUN !'##cross-references GB:Z99104; GB:AL009126; NID:g2632267; !1PIDN:CAB11824.1; PID:g2632315 !'##experimental_source strain 168 GENETICS !$#gene yabJ CLASSIFICATION #superfamily hypothetical protein HI0719 SUMMARY #length 125 #molecular-weight 13654 #checksum 7336 SEQUENCE /// ENTRY B44514 #type complete TITLE hypothetical protein 1 (vnfA 5' region) - Azotobacter vinelandii ORGANISM #formal_name Azotobacter vinelandii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B44514 REFERENCE A44514 !$#authors Joerger, R.D.; Jacobson, M.R.; Bishop, P.E. !$#journal J. Bacteriol. (1989) 171:3258-3267 !$#title Two nifA-like genes required for expression of alternative !1nitrogenases by Azotobacter vinelandii. !$#cross-references MUID:89255091; PMID:2722750 !$#accession B44514 !'##status preliminary !'##molecule_type DNA !'##residues 1-127 ##label JOE !'##cross-references EMBL:M26752 CLASSIFICATION #superfamily hypothetical protein HI0719 SUMMARY #length 127 #molecular-weight 13463 #checksum 5923 SEQUENCE /// ENTRY S30349 #type complete TITLE perchloric acid-soluble protein, 23K - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S30349 REFERENCE S30349 !$#authors Levy-Favatier, F.; Cuisset, L.; Nedelec, B.; Tichonicky, L.; !1Kruh, J.; Delpech, M. !$#journal Eur. J. Biochem. (1993) 212:665-673 !$#title Characterization, purification and cDNA cloning of a rat !1perchloric-acid-soluble 23-kDa protein present only in liver !1and kidney. !$#cross-references MUID:93215643; PMID:8385007 !$#accession S30349 !'##status preliminary !'##molecule_type mRNA !'##residues 1-99 ##label LEV !'##cross-references EMBL:X70825; NID:g56601; PIDN:CAB36976.1; !1PID:g4456766 CLASSIFICATION #superfamily hypothetical protein HI0719 SUMMARY #length 99 #molecular-weight 10355 #checksum 1939 SEQUENCE /// ENTRY H64637 #type complete TITLE probable translation initiation inhibitor - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS H64637 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession H64637 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-125 ##label TOM !'##cross-references GB:AE000603; GB:AE000511; NID:g2314075; !1PIDN:AAD07989.1; PID:g2314082; TIGR:HP0944 CLASSIFICATION #superfamily hypothetical protein HI0719 SUMMARY #length 125 #molecular-weight 13373 #checksum 7173 SEQUENCE /// ENTRY H64842 #type complete TITLE probable translation initiation regulator b1010 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS H64842 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64842 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-128 ##label BLAT !'##cross-references GB:AE000202; GB:U00096; NID:g1787233; !1PIDN:AAC74095.1; PID:g1787245; UWGP:b1010 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily hypothetical protein HI0719 SUMMARY #length 128 #molecular-weight 13763 #checksum 6264 SEQUENCE /// ENTRY H64845 #type complete TITLE ycdY protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS H64845 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64845 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-184 ##label BLAT !'##cross-references GB:AE000205; GB:U00096; NID:g1787265; !1PIDN:AAC74119.1; PID:g1787272; UWGP:b1035 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ycdY CLASSIFICATION #superfamily Escherichia coli ycdY protein SUMMARY #length 184 #molecular-weight 20724 #checksum 896 SEQUENCE /// ENTRY F64035 #type complete TITLE ycdY protein homolog HI1543 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS F64035 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession F64035 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-184 ##label TIGR !'##cross-references GB:U32829; GB:L42023; NID:g1574375; !1PIDN:AAC23193.1; PID:g1574385; TIGR:HI1543 CLASSIFICATION #superfamily Escherichia coli ycdY protein SUMMARY #length 184 #molecular-weight 21059 #checksum 2367 SEQUENCE /// ENTRY A64915 #type complete TITLE ycdY protein homolog b1591 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS A64915 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64915 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-207 ##label BLAT !'##cross-references GB:AE000254; GB:U00096; NID:g1787862; !1PIDN:AAC74663.1; PID:g1787874; UWGP:b1591 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily Escherichia coli ycdY protein SUMMARY #length 207 #molecular-weight 23646 #checksum 9900 SEQUENCE /// ENTRY H64863 #type complete TITLE ycgL protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS H64863 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64863 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-108 ##label BLAT !'##cross-references GB:AE000216; GB:U00096; NID:g1787417; !1PIDN:AAC74263.1; PID:g1787427; UWGP:b1179 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ycgL CLASSIFICATION #superfamily hypothetical protein b1179 SUMMARY #length 108 #molecular-weight 12414 #checksum 8428 SEQUENCE /// ENTRY A64030 #type complete TITLE hypothetical protein HI1446 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS A64030 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession A64030 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-107 ##label TIGR !'##cross-references GB:U32823; GB:L42023; NID:g1574281; !1PIDN:AAC23096.1; PID:g1574295; TIGR:HI1446 CLASSIFICATION #superfamily hypothetical protein b1179 SUMMARY #length 107 #molecular-weight 12282 #checksum 2637 SEQUENCE /// ENTRY H65050 #type complete TITLE probable ATP-binding protein gutQ - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS H65050; A48429; S10373 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65050 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-308 ##label BLAT !'##cross-references GB:AE000354; GB:U00096; NID:g2367149; !1PIDN:AAC75750.1; PID:g1789060; UWGP:b2708 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A48429 !$#authors Yamada, M.; Yamada, Y.; Saier Jr., M.H. !$#journal DNA Seq. (1990) 1:141-145 !$#title Nucleotide sequence and expression of the gutQ gene within !1the glucitol operon of Escherichia coli. !$#cross-references MUID:92190542; PMID:2134185 !$#accession A48429 !'##status preliminary !'##molecule_type DNA !'##residues 1-200,'VN','R',228,'RD',231,'CDAGTQPH',240,'SGA',244-246, !1'M' ##label YAM !'##cross-references EMBL:X51361; NID:g41631; PIDN:CAA35745.1; !1PID:g41632 !'##note sequence extracted from NCBI backbone (NCBIN:89668, !1NCBIP:89670) GENETICS !$#gene gutQ !$#map_position 58 min CLASSIFICATION #superfamily probable ATP-binding protein gutQ; CBS homology KEYWORDS ATP SUMMARY #length 308 #molecular-weight 32646 #checksum 1994 SEQUENCE /// ENTRY G65110 #type complete TITLE hypothetical 35.2 kD protein in murZ-rpoN intergenic region - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS G65110 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65110 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-328 ##label BLAT !'##cross-references GB:AE000399; GB:U00096; NID:g2367201; !1PIDN:AAC76229.1; PID:g1789588; UWGP:b3197 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yrbH CLASSIFICATION #superfamily probable ATP-binding protein gutQ; CBS homology SUMMARY #length 328 #molecular-weight 35196 #checksum 7386 SEQUENCE /// ENTRY B70434 #type complete TITLE polysialic acid capsule expression protein - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 29-Sep-1999 ACCESSIONS B70434 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession B70434 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-322 ##label AQF !'##cross-references GB:AE000745; NID:g2983907; PIDN:AAC07460.1; !1PID:g2983910; GB:AE000657 !'##experimental_source strain VF5 GENETICS !$#gene kpsF CLASSIFICATION #superfamily probable ATP-binding protein gutQ; CBS homology FEATURE !$208-256 #domain CBS homology #label CBS1\ !$273-321 #domain CBS homology #label CBS2 SUMMARY #length 322 #molecular-weight 35114 #checksum 6980 SEQUENCE /// ENTRY A49915 #type complete TITLE GutQ homolog - Escherichia coli ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A49915 REFERENCE A49915 !$#authors Cieslewicz, M.J.; Steenbergen, S.M.; Vimr, E.R. !$#journal J. Bacteriol. (1993) 175:8018-8023 !$#title Cloning, sequencing, expression, and complementation !1analysis of the Escherichia coli K1 kps region 1 gene, kpsE, !1and identification of an upstream open reading frame !1encoding a protein with homology to GutQ. !$#cross-references MUID:94075243; PMID:8253690 !$#contents K1 !$#accession A49915 !'##status preliminary !'##molecule_type DNA !'##residues 1-317 ##label CIE !'##note sequence inconsistent with nucleotide translation !'##note sequence extracted from NCBI backbone (NCBIN:140654, !1NCBIP:140655) CLASSIFICATION #superfamily probable ATP-binding protein gutQ; CBS homology SUMMARY #length 317 #molecular-weight 34434 #checksum 5610 SEQUENCE /// ENTRY C64136 #type complete TITLE kpsF protein homolog - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 29-Sep-1999 ACCESSIONS C64136 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession C64136 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-337 ##label TIGR !'##cross-references GB:U32841; GB:L42023; NID:g1574529; !1PIDN:AAC23324.1; PID:g1574530; TIGR:HI1678 CLASSIFICATION #superfamily probable ATP-binding protein gutQ; CBS homology SUMMARY #length 337 #molecular-weight 36655 #checksum 231 SEQUENCE /// ENTRY C71654 #type complete TITLE kpsF protein (kpsF) RP505 - Rickettsia prowazekii ORGANISM #formal_name Rickettsia prowazekii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Nov-2000 ACCESSIONS C71654 REFERENCE A71630 !$#authors Andersson, S.G.E.; Zomorodipour, A.; Andersson, J.O.; !1Sicheritz-Ponten, T.; Alsmark, U.C.M.; Podowski, R.M.; !1Naeslund, A.K.; Eriksson, A.S.; Winkler, H.H.; Kurland, C.G. !$#journal Nature (1998) 396:133-140 !$#title The genome sequence of Rickettsia prowazekii and the origin !1of mitochondria. !$#cross-references MUID:99039499; PMID:9823893 !$#accession C71654 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-319 ##label AND !'##cross-references GB:AJ235272; GB:AJ235269; NID:g3861033; !1PIDN:CAA14957.1; PID:g3861057; GSPDB:GN00081 !'##experimental_source strain Madrid E GENETICS !$#gene kpsF; RP505 CLASSIFICATION #superfamily probable ATP-binding protein gutQ; CBS homology FEATURE !$208-256 #domain CBS homology #label CBS SUMMARY #length 319 #molecular-weight 35296 #checksum 1842 SEQUENCE /// ENTRY B71519 #type complete TITLE probable gutQ/kpsF sugar-phosphate isomerase - Chlamydia trachomatis (serotype D, strain UW3/Cx) ORGANISM #formal_name Chlamydia trachomatis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 08-Oct-1999 ACCESSIONS B71519 REFERENCE A71570 !$#authors Stephens, R.S.; Kalman, S.; Lammel, C.J.; Fan, J.; Marathe, !1R.; Aravind, L.; Mitchell, W.P.; Olinger, L.; Tatusov, R.L.; !1Zhao, Q.; Koonin, E.V.; Davis, R.W. !$#journal Science (1998) 282:754-759 !$#title Genome sequence of an obligate intracellular pathogen of !1humans: Chlamydia trachomatis. !$#cross-references MUID:99000809; PMID:9784136 !$#accession B71519 !'##status preliminary !'##molecule_type DNA !'##residues 1-328 ##label ARN !'##cross-references GB:AE001313; GB:AE001273; NID:g3328823; !1PIDN:AAC67996.1; PID:g3328826 !'##experimental_source serotype D, strain UW-3/Cx GENETICS !$#gene yrbH CLASSIFICATION #superfamily probable ATP-binding protein gutQ; CBS homology SUMMARY #length 328 #molecular-weight 36020 #checksum 1481 SEQUENCE /// ENTRY E72068 #type complete TITLE carbohydrate isomerase CP0226 [similarity] - Chlamydophila pneumoniae (strains CWL029 and AR39) ORGANISM #formal_name Chlamydophila pneumoniae, Chlamydia pneumoniae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 11-May-2000 ACCESSIONS E72068; G81600 REFERENCE A72000 !$#authors Kalman, S.; Mitchell, W.; Marathe, R.; Lammel, C.; Fan, J.; !1Olinger, L.; Grimwood, J.; Davis, R.W.; Stephens, R.S. !$#journal Nature Genet. (1999) 21:385-389 !$#title Comparative genomes of Clamydia pneumoniae and C. !1trachomatis. !$#cross-references MUID:99206606; PMID:10192388 !$#accession E72068 !'##molecule_type DNA !'##residues 1-329 ##label ARN !'##cross-references GB:AE001637; GB:AE001363; NID:g4376807; !1PID:g4376815 !'##experimental_source strain CWL029 REFERENCE A81500 !$#authors Read, T.D.; Brunham, R.C.; Shen, C.; Gill, S.R.; Heidelberg, !1J.F.; White, O.; Hickey, E.K.; Peterson, J.; Utterback, T.; !1Berry, K.; Bass, S.; Linher, K.; Weidman, J.; Khouri, H.; !1Craven, B.; Bowman, C.; Dodson, R.; Gwinn, M.; Nelson, W.; !1DeBoy, R.; Kolonay, J.; McClarty, G.; Salzberg, S.L.; Eisen, !1J.; Fraser, C.M. !$#journal Nucleic Acids Res. (2000) 28:1397-1406 !$#title Genome sequences of Chlamydia trachomatis MoPn and Chlamydia !1pneumoniae AR39. !$#cross-references MUID:20150255; PMID:10684935 !$#accession G81600 !'##molecule_type DNA !'##residues 1-329 ##label REA !'##cross-references GB:AE002183; GB:AE002161; NID:g7189146; !1PIDN:AAF38092.1; PID:g7189153; GSPDB:GN00122; TIGR:CP0226 !'##experimental_source strain AR39, HL cells GENETICS !$#gene kpsF; CP0226 CLASSIFICATION #superfamily probable ATP-binding protein gutQ; CBS homology SUMMARY #length 329 #molecular-weight 35650 #checksum 1483 SEQUENCE /// ENTRY H64452 #type complete TITLE conserved hypothetical protein MJ1225 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H64452 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession H64452 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-280 ##label BUL !'##cross-references GB:U67563; GB:L77117; NID:g2826379; !1PIDN:AAB99228.1; PID:g1591856; TIGR:MJ1225 GENETICS !$#map_position FOR1167099-1167941 CLASSIFICATION #superfamily conserved hypothetical protein MJ1225; CBS !1homology FEATURE !$157-204 #domain CBS homology #label CBS SUMMARY #length 280 #molecular-weight 31719 #checksum 6755 SEQUENCE /// ENTRY E69030 #type complete TITLE conserved hypothetical protein MJ1225 homolog - Methanobacterium thermoautotrophicum (strain Delta H) ALTERNATE_NAMES inosine-monophosphate dehydrogenase related protein III [misnomer] ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69030 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession E69030 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-313 ##label MTH !'##cross-references GB:AE000890; GB:AE000666; NID:g2622331; !1PIDN:AAB85713.1; PID:g2622335 !'##experimental_source strain Delta H GENETICS !$#gene MTH1224 CLASSIFICATION #superfamily conserved hypothetical protein MJ1225; CBS !1homology KEYWORDS duplication FEATURE !$38-87 #domain CBS homology #label CBS1\ !$118-166 #domain CBS homology #label CBS2\ !$181-237 #domain CBS homology #label CBS3\ !$265-312 #domain CBS homology #label CBS4 SUMMARY #length 313 #molecular-weight 34258 #checksum 5758 SEQUENCE /// ENTRY H69355 #type complete TITLE conserved hypothetical protein MJ1225 homolog - Archaeoglobus fulgidus ALTERNATE_NAMES conserved hypothetical protein AF0848 ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H69355 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession H69355 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-284 ##label KLE !'##cross-references GB:AE001045; GB:AE000782; NID:g2689368; !1PIDN:AAB90389.1; PID:g2649753; TIGR:AF0848 CLASSIFICATION #superfamily conserved hypothetical protein MJ1225; CBS !1homology KEYWORDS duplication FEATURE !$88-140 #domain CBS homology #label CBS SUMMARY #length 284 #molecular-weight 31515 #checksum 3361 SEQUENCE /// ENTRY D69030 #type complete TITLE MJ1225-related protein MTH1223 - Methanobacterium thermoautotrophicum (strain Delta H) ALTERNATE_NAMES inosine-5'-monophosphate dehydrogenase related protein II [misnomer] ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69030 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession D69030 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-281 ##label MTH !'##cross-references GB:AE000890; GB:AE000666; NID:g2622331; !1PIDN:AAB85712.1; PID:g2622334 !'##experimental_source strain Delta H GENETICS !$#gene MTH1223 !$#start_codon GTG CLASSIFICATION #superfamily conserved hypothetical protein MJ1225; CBS !1homology KEYWORDS duplication FEATURE !$234-281 #domain CBS homology #label CBS SUMMARY #length 281 #molecular-weight 31133 #checksum 7479 SEQUENCE /// ENTRY C69030 #type complete TITLE MJ1225 protein homolog MTH1222 - Methanobacterium thermoautotrophicum (strain Delta H) ALTERNATE_NAMES inosine-5'-monophosphate dehydrogenase related protein I [misnomer] ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69030 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession C69030 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-275 ##label MTH !'##cross-references GB:AE000890; GB:AE000666; NID:g2622331; !1PIDN:AAB85711.1; PID:g2622333 !'##experimental_source strain Delta H GENETICS !$#gene MTH1222 !$#start_codon GTG CLASSIFICATION #superfamily conserved hypothetical protein MJ1225; CBS !1homology KEYWORDS duplication FEATURE !$13-65 #domain CBS homology #label CBS1\ !$86-133 #domain CBS homology #label CBS2\ !$149-196 #domain CBS homology #label CBS3\ !$223-269 #domain CBS homology #label CBS4 SUMMARY #length 275 #molecular-weight 30589 #checksum 9681 SEQUENCE /// ENTRY S08244 #type complete TITLE conserved hypothetical protein MJ1225 homolog - Thermofilum pendens ALTERNATE_NAMES hypothetical protein 1 ORGANISM #formal_name Thermofilum pendens DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S08244 REFERENCE S08244 !$#authors Kjems, J.; Leffers, H.; Olesen, T.; Ingelore, H.; Garrett, !1R.A. !$#submission submitted to the EMBL Data Library, March 1989 !$#accession S08244 !'##molecule_type DNA !'##residues 1-300 ##label KJE !'##cross-references EMBL:X14835; NID:g48225; PID:g48226 CLASSIFICATION #superfamily conserved hypothetical protein MJ1225; CBS !1homology KEYWORDS duplication FEATURE !$13-61 #domain CBS homology #label CBS1\ !$92-140 #domain CBS homology #label CBS2\ !$155-202 #domain CBS homology #label CBS3\ !$230-277 #domain CBS homology #label CBS4 SUMMARY #length 300 #molecular-weight 33437 #checksum 1549 SEQUENCE /// ENTRY F69030 #type complete TITLE MJ1225 protein homolog MTH1225 - Methanobacterium thermoautotrophicum (strain Delta H) ALTERNATE_NAMES inosine-5'-monophosphate dehydrogenase related protein IV [misnomer] ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F69030 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession F69030 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-272 ##label MTH !'##cross-references GB:AE000890; GB:AE000666; NID:g2622331; !1PIDN:AAB85714.1; PID:g2622336 !'##experimental_source strain Delta H GENETICS !$#gene MTH1225 !$#start_codon GTG CLASSIFICATION #superfamily conserved hypothetical protein MJ1225; CBS !1homology KEYWORDS duplication FEATURE !$13-60 #domain CBS homology #label CBS1\ !$81-124 #domain CBS homology #label CBS2\ !$137-189 #domain CBS homology #label CBS3 SUMMARY #length 272 #molecular-weight 29954 #checksum 9489 SEQUENCE /// ENTRY C71188 #type complete TITLE conserved hypothetical protein MJ1225 homolog - Pyrococcus horikoshii ALTERNATE_NAMES hypothetical protein PH1780 ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C71188 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession C71188 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-285 ##label KAW !'##cross-references GB:AP000007; NID:g3236134; PIDN:BAA30898.1; !1PID:g3258215 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1780 CLASSIFICATION #superfamily conserved hypothetical protein MJ1225; CBS !1homology KEYWORDS duplication FEATURE !$73-120 #domain CBS homology #label CBS SUMMARY #length 285 #molecular-weight 32305 #checksum 3497 SEQUENCE /// ENTRY H69232 #type complete TITLE MJ1225-related protein MTH992 - Methanobacterium thermoautotrophicum (strain Delta H) ALTERNATE_NAMES inosine-5'-monophosphate dehydrogenase related protein IX [misnomer] ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H69232 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession H69232 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-284 ##label MTH !'##cross-references GB:AE000872; GB:AE000666; NID:g2622082; !1PIDN:AAB85489.1; PID:g2622093 !'##experimental_source strain Delta H GENETICS !$#gene MTH992 !$#start_codon GTG CLASSIFICATION #superfamily conserved hypothetical protein MJ1225; CBS !1homology KEYWORDS duplication FEATURE !$73-120 #domain CBS homology #label CBS SUMMARY #length 284 #molecular-weight 31804 #checksum 1620 SEQUENCE /// ENTRY F69257 #type complete TITLE MJ1225-related protein AF0062 - Archaeoglobus fulgidus ALTERNATE_NAMES conserved hypothetical protein AF0062 ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F69257 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession F69257 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-296 ##label KLE !'##cross-references GB:AE001102; GB:AE000782; NID:g2689425; !1PIDN:AAB91162.1; PID:g2650583; TIGR:AF0062 CLASSIFICATION #superfamily conserved hypothetical protein MJ1225; CBS !1homology KEYWORDS duplication FEATURE !$85-132 #domain CBS homology #label CBS SUMMARY #length 296 #molecular-weight 33782 #checksum 7728 SEQUENCE /// ENTRY B69824 #type complete TITLE conserved hypothetical protein yhcV - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 04-Jun-1999 #sequence_revision 04-Jun-1999 #text_change 16-Jun-2000 ACCESSIONS B69824 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69824 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-140 ##label KUN !'##cross-references GB:Z99108; GB:AL009126; NID:g2633055; !1PIDN:CAB12751.1; PID:g2633246 !'##experimental_source strain 168 GENETICS !$#gene yhcV CLASSIFICATION #superfamily conserved hypothetical protein yhcV; CBS !1homology KEYWORDS duplication FEATURE !$11-58 #domain CBS homology #label CBS1\ !$75-122 #domain CBS homology #label CBS2 SUMMARY #length 140 #molecular-weight 14916 #checksum 532 SEQUENCE /// ENTRY G69873 #type complete TITLE yhcV-related protein ylbB - Bacillus subtilis ALTERNATE_NAMES inosine-monophosphate dehydrogenase homolog [misnomer] ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69873 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69873 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-150 ##label KUN !'##cross-references GB:Z99111; GB:AL009126; NID:g2633699; !1PIDN:CAB13368.1; PID:g2633866 !'##experimental_source strain 168 GENETICS !$#gene ylbB CLASSIFICATION #superfamily conserved hypothetical protein yhcV; CBS !1homology FEATURE !$11-60 #domain CBS homology #label CBS1\ !$77-124 #domain CBS homology #label CBS2 SUMMARY #length 150 #molecular-weight 16357 #checksum 2501 SEQUENCE /// ENTRY B69077 #type complete TITLE yhcV homolog 2 - Methanobacterium thermoautotrophicum (strain Delta H) ALTERNATE_NAMES inosine-monophosphate dehydrogenase related protein X [misnomer] ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69077 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession B69077 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-133 ##label MTH !'##cross-references GB:AE000917; GB:AE000666; NID:g2622689; !1PIDN:AAB86048.1; PID:g2622697 !'##experimental_source strain Delta H GENETICS !$#gene MTH1575 CLASSIFICATION #superfamily conserved hypothetical protein yhcV; CBS !1homology FEATURE !$22-69 #domain CBS homology #label CBS1\ !$83-130 #domain CBS homology #label CBS2 SUMMARY #length 133 #molecular-weight 14751 #checksum 7412 SEQUENCE /// ENTRY F69514 #type complete TITLE yhcV homolog 2 - Archaeoglobus fulgidus ALTERNATE_NAMES inosine-monophosphate dehydrogenase (guaB-2) homolog [misnomer] ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F69514 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession F69514 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-183 ##label KLE !'##cross-references GB:AE000958; GB:AE000782; NID:g2689281; !1PIDN:AAB89133.1; PID:g2648410; TIGR:AF2118 CLASSIFICATION #superfamily conserved hypothetical protein yhcV; CBS !1homology FEATURE !$72-119 #domain CBS homology #label CBS SUMMARY #length 183 #molecular-weight 20269 #checksum 5938 SEQUENCE /// ENTRY S76072 #type complete TITLE yhcV homolog - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S76072 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76072 !'##status preliminary !'##molecule_type DNA !'##residues 1-155 ##label KAN !'##cross-references EMBL:D63999; GB:AB001339; NID:g1001396; !1PID:g1001427 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily conserved hypothetical protein yhcV; CBS !1homology FEATURE !$39-85 #domain CBS homology #label CBS1\ !$102-151 #domain CBS homology #label CBS2 SUMMARY #length 155 #molecular-weight 17270 #checksum 8815 SEQUENCE /// ENTRY A64478 #type complete TITLE hypothetical protein homolog MJ1426 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A64478 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession A64478 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-168 ##label BUL !'##cross-references GB:U67583; GB:L77117; NID:g2826409; !1PIDN:AAB99437.1; PID:g1592076; TIGR:MJ1426 GENETICS !$#map_position FOR1396048-1396554 !$#start_codon TTG CLASSIFICATION #superfamily conserved hypothetical protein yhcV; CBS !1homology FEATURE !$120-168 #domain CBS homology #label CBS SUMMARY #length 168 #molecular-weight 18873 #checksum 901 SEQUENCE /// ENTRY F69185 #type complete TITLE yhcV homolog MTH644 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F69185 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession F69185 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-157 ##label MTH !'##cross-references GB:AE000844; GB:AE000666; NID:g2621707; !1PIDN:AAB85149.1; PID:g2621725 !'##experimental_source strain Delta H GENETICS !$#gene MTH644 CLASSIFICATION #superfamily conserved hypothetical protein yhcV; CBS !1homology FEATURE !$108-156 #domain CBS homology #label CBS SUMMARY #length 157 #molecular-weight 17387 #checksum 2825 SEQUENCE /// ENTRY B64356 #type complete TITLE hypothetical protein MJ0450 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B64356 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession B64356 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-186 ##label BUL !'##cross-references GB:U67496; GB:L77117; NID:g2826283; !1PIDN:AAB98439.1; PID:g1591154; TIGR:MJ0450 GENETICS !$#map_position FOR403277-403837 CLASSIFICATION #superfamily hypothetical protein MJ0450; CBS homology KEYWORDS duplication FEATURE !$13-63 #domain CBS homology #label CBS1\ !$81-128 #domain CBS homology #label CBS2 SUMMARY #length 186 #molecular-weight 20791 #checksum 5594 SEQUENCE /// ENTRY E64381 #type complete TITLE conserved hypothetical protein MJ0653 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E64381 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession E64381 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-194 ##label BUL !'##cross-references GB:U67513; GB:L77117; NID:g1591365; !1PIDN:AAB98648.1; PID:g1592300; TIGR:MJ0653 GENETICS !$#map_position FOR581423-582007 CLASSIFICATION #superfamily conserved hypothetical protein MJ0653; CBS !1homology KEYWORDS duplication FEATURE !$16-63 #domain CBS homology #label CBS1\ !$81-128 #domain CBS homology #label CBS2 SUMMARY #length 194 #molecular-weight 21723 #checksum 4958 SEQUENCE /// ENTRY G69355 #type complete TITLE MJ0653 homolog AF0847 - Archaeoglobus fulgidus ALTERNATE_NAMES inosine-monophosphate dehydrogenase (guaB-1) homolog [misnomer] ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69355 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession G69355 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-189 ##label KLE !'##cross-references GB:AE001045; GB:AE000782; NID:g2689368; !1PIDN:AAB90390.1; PID:g2649754; TIGR:AF0847 CLASSIFICATION #superfamily conserved hypothetical protein MJ0653; CBS !1homology KEYWORDS duplication FEATURE !$79-127 #domain CBS homology #label CBS SUMMARY #length 189 #molecular-weight 20623 #checksum 314 SEQUENCE /// ENTRY G69030 #type complete TITLE MJ0653 homolog MTH1226 - Methanobacterium thermoautotrophicum (strain Delta H) ALTERNATE_NAMES inosine-monophosphate dehydrogenase related protein V [misnomer] ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69030 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession G69030 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-187 ##label MTH !'##cross-references GB:AE000890; GB:AE000666; NID:g2622331; !1PIDN:AAB85715.1; PID:g2622337 !'##experimental_source strain Delta H GENETICS !$#gene MTH1226 CLASSIFICATION #superfamily conserved hypothetical protein MJ0653; CBS !1homology KEYWORDS duplication FEATURE !$16-63 #domain CBS homology #label CBS1\ !$81-128 #domain CBS homology #label CBS2 SUMMARY #length 187 #molecular-weight 20659 #checksum 6369 SEQUENCE /// ENTRY S22196 #type complete TITLE MJ0653 homolog - Desulfurolobus ambivalens ALTERNATE_NAMES hypothetical protein 3 ORGANISM #formal_name Desulfurolobus ambivalens DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 29-Oct-1999 ACCESSIONS S22196 REFERENCE S22194 !$#authors Kletzin, A. !$#submission submitted to the EMBL Data Library, January 1992 !$#accession S22196 !'##molecule_type DNA !'##residues 1-164 ##label KLE !'##cross-references EMBL:X64202; NID:g40780; PID:g40783 !'##experimental_source DSM 3772 CLASSIFICATION #superfamily conserved hypothetical protein MJ0653; CBS !1homology KEYWORDS duplication FEATURE !$12-60 #domain CBS homology #label CBS1\ !$75-123 #domain CBS homology #label CBS2 SUMMARY #length 164 #molecular-weight 17731 #checksum 9079 SEQUENCE /// ENTRY I39734 #type complete TITLE CBS domain-containing protein - Anabaena variabilis ALTERNATE_NAMES hypothetical protein 3 ORGANISM #formal_name Anabaena variabilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S68184; I39734 REFERENCE I39730 !$#authors Schmitz, O.; Boison, G.; Hilscher, R.; Hundeshagen, B.; !1Zimmer, W.; Lottspeich, F.; Bothe, H. !$#journal Eur. J. Biochem. (1995) 233:266-276 !$#title Molecular biological analysis of a bidirectional hydrogenase !1from cyanobacteria. !$#cross-references MUID:96061958; PMID:7588754 !$#accession S68184 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-199 ##label SCH !'##cross-references EMBL:X79285; NID:g1032475; PIDN:CAA55877.1; !1PID:g1032480 !'##experimental_source ATCC 29413 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1May 1994 CLASSIFICATION #superfamily Anabaena CBS domain-containing protein; CBS !1homology KEYWORDS duplication FEATURE !$11-60 #domain CBS homology #label CBS1\ !$78-124 #domain CBS homology #label CBS2 SUMMARY #length 199 #molecular-weight 22491 #checksum 3175 SEQUENCE /// ENTRY D64312 #type complete TITLE conserved hypothetical protein MJ0100 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 14-May-1999 #sequence_revision 14-May-1999 #text_change 21-Jul-2000 ACCESSIONS D64312 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession D64312 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-509 ##label BUL !'##cross-references GB:U67467; GB:L77117; NID:g2826242; !1PIDN:AAB98080.1; PID:g1498865; TIGR:MJ0100 GENETICS !$#map_position REV94823-93294 CLASSIFICATION #superfamily conserved hypothetical protein MJ0100; CBS !1homology KEYWORDS duplication FEATURE !$397-445 #domain CBS homology #label CBS1\ !$458-506 #domain CBS homology #label CBS2 SUMMARY #length 509 #molecular-weight 56457 #checksum 6497 SEQUENCE /// ENTRY B69214 #type complete TITLE MJ0100 protein homolog MTH855 - Methanobacterium thermoautotrophicum (strain Delta H) ALTERNATE_NAMES inosine-5'-monophosphate dehydrogenase related protein VIII [misnomer] ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 14-May-1999 #sequence_revision 14-May-1999 #text_change 04-Feb-2000 ACCESSIONS B69214 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession B69214 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-514 ##label MTH !'##cross-references GB:AE000862; GB:AE000666; NID:g2621943; !1PIDN:AAB85353.1; PID:g2621947 !'##experimental_source strain Delta H GENETICS !$#gene MTH855 !$#start_codon TTG CLASSIFICATION #superfamily conserved hypothetical protein MJ0100; CBS !1homology KEYWORDS duplication FEATURE !$396-444 #domain CBS homology #label CBS1\ !$457-505 #domain CBS homology #label CBS2 SUMMARY #length 514 #molecular-weight 56350 #checksum 8622 SEQUENCE /// ENTRY A69398 #type complete TITLE MJ0100 protein homolog AF1186 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 14-May-1999 #sequence_revision 14-May-1999 #text_change 23-Jul-1999 ACCESSIONS A69398 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession A69398 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-491 ##label KLE !'##cross-references GB:AE001022; GB:AE000782; NID:g2689345; !1PIDN:AAB90057.1; PID:g2649397; TIGR:AF1186 CLASSIFICATION #superfamily conserved hypothetical protein MJ0100; CBS !1homology KEYWORDS duplication FEATURE !$381-428 #domain CBS homology #label CBS1\ !$442-490 #domain CBS homology #label CBS2 SUMMARY #length 491 #molecular-weight 54340 #checksum 6671 SEQUENCE /// ENTRY B69407 #type complete TITLE MJ0188 homolog - Archaeoglobus fulgidus ALTERNATE_NAMES inosine monophosphate dehydrogenase homolog [misnomer] ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69407 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession B69407 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-259 ##label KLE !'##cross-references GB:AE001017; GB:AE000782; NID:g2689340; !1PIDN:AAB89984.1; PID:g2649320; TIGR:AF1259 CLASSIFICATION #superfamily conserved hypothetical protein MJ0188; CBS !1homology FEATURE !$12-60 #domain CBS homology #label CBS1\ !$71-119 #domain CBS homology #label CBS2 SUMMARY #length 259 #molecular-weight 29545 #checksum 1216 SEQUENCE /// ENTRY E64323 #type complete TITLE conserved hypothetical protein MJ0188 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E64323 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession E64323 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-265 ##label BUL !'##cross-references GB:U67475; GB:L77117; NID:g1590930; !1PIDN:AAB98168.1; PID:g1498962; TIGR:MJ0188 GENETICS !$#map_position REV186674-185877 CLASSIFICATION #superfamily conserved hypothetical protein MJ0188; CBS !1homology FEATURE !$12-59 #domain CBS homology #label CBS1\ !$72-120 #domain CBS homology #label CBS2 SUMMARY #length 265 #molecular-weight 29851 #checksum 150 SEQUENCE /// ENTRY F69037 #type complete TITLE MJ0188 homolog - Methanobacterium thermoautotrophicum (strain Delta H) ALTERNATE_NAMES inosine-monophosphate dehydrogenase related protein VI [misnomer] ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F69037 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession F69037 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-269 ##label MTH !'##cross-references GB:AE000893; GB:AE000666; NID:g2622375; !1PIDN:AAB85764.1; PID:g2622389 !'##experimental_source strain Delta H GENETICS !$#gene MTH1282 CLASSIFICATION #superfamily conserved hypothetical protein MJ0188; CBS !1homology FEATURE !$14-61 #domain CBS homology #label CBS1\ !$72-120 #domain CBS homology #label CBS2 SUMMARY #length 269 #molecular-weight 30294 #checksum 9826 SEQUENCE /// ENTRY S54581 #type complete TITLE probable membrane protein YMR119w - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein YM8564.01; hypothetical protein YM9718.18 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 12-Nov-1999 ACCESSIONS S54581; S54488 REFERENCE S54510 !$#authors Hunt, S.; Bowman, S. !$#submission submitted to the EMBL Data Library, May 1995 !$#accession S54581 !'##molecule_type DNA !'##residues 1-431 ##label HUN !'##cross-references EMBL:Z49702; NID:g817859; PID:g1326013; !1GSPDB:GN00013; MIPS:YMR119w !'##experimental_source strain AB972 REFERENCE S54014 !$#authors Lye, G.; Churcher, C.M. !$#submission submitted to the EMBL Data Library, May 1995 !$#accession S54488 !'##molecule_type DNA !'##residues 345-624 ##label LYE !'##cross-references EMBL:Z49273; NID:g809577; PID:g809578; !1GSPDB:GN00013; MIPS:YMR119w GENETICS !$#gene MIPS:YMR119w !$#map_position 13R CLASSIFICATION #superfamily probable membrane protein YMR119w KEYWORDS transmembrane protein FEATURE !$82-98 #domain transmembrane #status predicted #label TM1\ !$120-136 #domain transmembrane #status predicted #label TM2\ !$211-227 #domain transmembrane #status predicted #label TM3\ !$237-253 #domain transmembrane #status predicted #label TM4\ !$278-294 #domain transmembrane #status predicted #label TM5 SUMMARY #length 624 #molecular-weight 71443 #checksum 3923 SEQUENCE /// ENTRY S62919 #type complete TITLE probable membrane protein YNL008c - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein N2874 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S62919; S62920 REFERENCE S62916 !$#authors Doignon, F.; Crouzet, M. !$#submission submitted to the Protein Sequence Database, April 1996 !$#accession S62919 !'##molecule_type DNA !'##residues 1-370 ##label DOI !'##cross-references EMBL:Z71284; GSPDB:GN00014; MIPS:YNL008c !'##experimental_source strain S288C REFERENCE S62920 !$#authors Andre, B.; Iraqui Houssaini, I.; Urrestarazu, L.A.; Vissers, !1S. !$#submission submitted to the Protein Sequence Database, April 1996 !$#accession S62920 !'##molecule_type DNA !'##residues 103-669 ##label AND !'##cross-references EMBL:Z71284; GSPDB:GN00014; MIPS:YNL008c !'##experimental_source strain S288C GENETICS !$#gene SGD:ASI3; MIPS:YNL008c !'##cross-references SGD:S0004953 !$#map_position 14L CLASSIFICATION #superfamily probable membrane protein YMR119w KEYWORDS transmembrane protein FEATURE !$82-98 #domain transmembrane #status predicted #label TM1\ !$117-133 #domain transmembrane #status predicted #label TM2\ !$153-169 #domain transmembrane #status predicted #label TM3\ !$211-227 #domain transmembrane #status predicted #label TM4\ !$275-291 #domain transmembrane #status predicted #label TM5 SUMMARY #length 669 #molecular-weight 76740 #checksum 9538 SEQUENCE /// ENTRY BVECA #type complete TITLE pyruvate dehydrogenase complex repressor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Mar-1989 #sequence_revision 05-Dec-1997 #text_change 01-Mar-2002 ACCESSIONS A64734; A30263; S45192; I53482 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64734 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-254 ##label BLAT !'##cross-references GB:AE000120; GB:U00096; NID:g1786298; !1PIDN:AAC73224.1; PID:g1786303; UWGP:b0113 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A91130 !$#authors Stephens, P.E.; Darlison, M.G.; Lewis, H.M.; Guest, J.R. !$#journal Eur. J. Biochem. (1983) 133:155-162 !$#title The pyruvate dehydrogenase complex of Escherichia coli K12. !1Nucleotide sequence encoding the pyruvate dehydrogenase !1component. !$#cross-references MUID:83209630; PMID:6343085 !$#accession A30263 !'##molecule_type DNA !'##residues 1-229,'DFARQK',236 ##label STE !'##cross-references EMBL:V01498 !'##note the gene for this protein, called gene A by the authors, is !1situated upstream of the pyruvate dehydrogenase complex; it !1is a weakly expressed product of unknown function REFERENCE S45181 !$#authors Fujita, N. !$#submission submitted to the EMBL Data Library, January 1994 !$#accession S45192 !'##molecule_type DNA !'##residues 1-229,'DFARQK',236 ##label FUJ !'##cross-references EMBL:D26562; NID:g473770; PIDN:BAA05571.1; !1PID:g473782 !'##experimental_source strain K-12 substrain W3110 REFERENCE I53482 !$#authors Haydon, D.J.; Quail, M.A.; Guest, J.R. !$#journal FEBS Lett. (1993) 336:43-47 !$#title A mutation causing constitutive synthesis of the pyruvate !1dehydrogenase complex in Escherichia coli is located within !1the pdhR gene. !$#cross-references MUID:94085588; PMID:8262214 !$#accession I53482 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-117,'C',119-254 ##label RES !'##cross-references GB:S67363; NID:g455921; PIDN:AAB29356.1; !1PID:g455922 GENETICS !$#gene pdhR !$#map_position 3 min CLASSIFICATION #superfamily pyruvate dehydrogenase complex repressor KEYWORDS DNA binding; transcription regulation SUMMARY #length 254 #molecular-weight 29425 #checksum 7524 SEQUENCE /// ENTRY S14473 #type complete TITLE regulatory protein mprA - Escherichia coli (strain K-12) ALTERNATE_NAMES emrR protein ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS S14473; PC1160; A39444; E65048; I55139 REFERENCE S14473 !$#authors Moreno, F. !$#submission submitted to the EMBL Data Library, July 1990 !$#description Nucleotide sequence of sbmA, the gene encoding the putative !1receptor of the peptide MccB17. Identification of the gene !1product. !$#accession S14473 !'##molecule_type DNA !'##residues 1-176 ##label MOR !'##cross-references EMBL:X54151; NID:g42013; PID:g42014 REFERENCE JC1344 !$#authors Lomovskaya, O.; Lewis, K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1992) 89:8938-8942 !$#title emr, an Escherichia coli locus for multidrug resistance. !$#cross-references MUID:93028382; PMID:1409590 !$#accession PC1160 !'##molecule_type DNA !'##residues 152-176 ##label LOM !'##cross-references GB:M86657 REFERENCE A39444 !$#authors del Castillo, I.; Gonzalez-Pastor, J.E.; San Millan, J.L.; !1Moreno, F. !$#journal J. Bacteriol. (1991) 173:3924-3929 !$#title Nucleotide sequence of the Escherichia coli regulatory gene !1mprA and construction and characterization of mprA-deficient !1mutants. !$#cross-references MUID:91267965; PMID:1840583 !$#accession A39444 !'##status preliminary !'##molecule_type DNA !'##residues 1-176 ##label DEL !'##cross-references GB:X54151; NID:g42013; PIDN:CAA38090.1; PID:g42014 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65048 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-176 ##label BLAT !'##cross-references GB:AE000353; GB:U00096; NID:g1789037; !1PIDN:AAC75731.1; PID:g1789040; UWGP:b2684 REFERENCE I55139 !$#authors Lomovskaya, O.; Lewis, K.; Matin, A. !$#journal J. Bacteriol. (1995) 177:2328-2334 !$#title EmrR is a negative regulator of the Escherichia coli !1multidrug resistance pump EmrAB. !$#cross-references MUID:95247664; PMID:7730261 !$#accession I55139 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-5 ##label RES !'##cross-references EMBL:U19993; NID:g643480 GENETICS !$#gene emrR; mprA !$#map_position 58 min CLASSIFICATION #superfamily regulatory protein mprA KEYWORDS DNA binding; transcription regulation SUMMARY #length 176 #molecular-weight 20563 #checksum 8688 SEQUENCE /// ENTRY S25225 #type complete TITLE papX protein - Escherichia coli ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Nov-2001 ACCESSIONS S25225; S16409; S16404 REFERENCE S25205 !$#authors Marklund, B.I.; Tennent, J.M.; Garcia, E.; Hamers, A.; Baga, !1M.; Lindberg, F.; Gaastra, W.; Normark, S. !$#journal Mol. Microbiol. (1992) 6:2225-2242 !$#title Horizontal gene transfer of the Escherichia coli pap and prs !1pili operons as a mechanism for the development of !1tissue-specific adhesive properties. !$#cross-references MUID:93023852; PMID:1357526 !$#accession S25225 !'##molecule_type DNA !'##residues 1-164 ##label MAR !'##cross-references EMBL:X61239; NID:g42290; PIDN:CAA43571.1; !1PID:g42302 !'##experimental_source strain J96 REFERENCE S16393 !$#authors Marklund, B.I.H. !$#submission submitted to the EMBL Data Library, August 1991 !$#accession S16409 !'##status preliminary !'##molecule_type DNA !'##residues 1-5,'T',7-14,'K',16-34,'T',36-37,'RM',40,'DNI',44-46,'L', !148-55,'A',57-60,'TT',63,'FAA',67,'N',69-99,'V',101-110,'A', !1112-131,'SM',134-137,'I',139,'DY',142-143,'H',145-146,'Q', !1148,'L',150-153,'N',155-163,'ASS' ##label MA2 !'##cross-references EMBL:X61238; NID:g42526; PID:g42530 CLASSIFICATION #superfamily regulatory protein mprA SUMMARY #length 164 #molecular-weight 19303 #checksum 9319 SEQUENCE /// ENTRY D69783 #type complete TITLE transcription regulator MarR family homolog ydgJ - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69783 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D69783 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-164 ##label KUN !'##cross-references GB:Z99107; GB:AL009126; NID:g2632866; !1PIDN:CAB12386.1; PID:g2632880 !'##experimental_source strain 168 GENETICS !$#gene ydgJ CLASSIFICATION #superfamily regulatory protein mprA SUMMARY #length 164 #molecular-weight 18809 #checksum 128 SEQUENCE /// ENTRY S35973 #type complete TITLE regulatory protein pecS - Erwinia chrysanthemi ORGANISM #formal_name Erwinia chrysanthemi DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S35973 REFERENCE S35972 !$#authors Reverchon, S.; Nasser, W.; Robert-Baudouy, J. !$#submission submitted to the EMBL Data Library, August 1993 !$#description pecS: a locus controlling pectinase, cellulase and blue !1pigment production in Erwinia chrysanthemi. !$#accession S35973 !'##status preliminary !'##molecule_type DNA !'##residues 1-166 ##label REV !'##cross-references EMBL:X74409; NID:g396456; PID:g396458 GENETICS !$#gene pecS CLASSIFICATION #superfamily regulatory protein mprA KEYWORDS DNA binding; transcription regulation SUMMARY #length 166 #molecular-weight 19285 #checksum 44 SEQUENCE /// ENTRY G69867 #type complete TITLE transcription regulator MarR family homolog ykvE - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69867 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69867 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-145 ##label KUN !'##cross-references GB:Z99111; GB:AL009126; NID:g2633699; !1PIDN:CAB13240.1; PID:g2633738 !'##experimental_source strain 168 GENETICS !$#gene ykvE CLASSIFICATION #superfamily regulatory protein mprA SUMMARY #length 145 #molecular-weight 16567 #checksum 4479 SEQUENCE /// ENTRY A69860 #type complete TITLE transcription regulator MarR family homolog ykoM - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A69860 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69860 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-154 ##label KUN !'##cross-references GB:Z99110; GB:Z99111; GB:AL009126; NID:g2633699; !1PID:g2633705; NID:g2633472; PID:g2633688 !'##experimental_source strain 168 GENETICS !$#gene ykoM CLASSIFICATION #superfamily regulatory protein mprA SUMMARY #length 154 #molecular-weight 17858 #checksum 4165 SEQUENCE /// ENTRY B69986 #type complete TITLE transcription regulator MarR family homolog ysmB - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69986 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69986 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-146 ##label KUN !'##cross-references GB:Z99118; GB:AL009126; NID:g2635200; !1PIDN:CAB14800.1; PID:g2635305 !'##experimental_source strain 168 GENETICS !$#gene ysmB CLASSIFICATION #superfamily regulatory protein mprA SUMMARY #length 146 #molecular-weight 17144 #checksum 2111 SEQUENCE /// ENTRY H64868 #type complete TITLE ychN protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS H64868 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64868 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-117 ##label BLAT !'##cross-references GB:AE000220; GB:U00096; NID:g1787467; !1PIDN:AAC74303.1; PID:g1787471; UWGP:b1219 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ychN CLASSIFICATION #superfamily Escherichia coli ychN protein SUMMARY #length 117 #molecular-weight 12693 #checksum 1401 SEQUENCE /// ENTRY E64423 #type complete TITLE ychN protein homolog MJ0989 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E64423 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession E64423 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-114 ##label BUL !'##cross-references GB:U67541; GB:L77117; NID:g2826353; !1PIDN:AAB98991.1; PID:g1591651; TIGR:MJ0989 GENETICS !$#map_position REV919693-919349 CLASSIFICATION #superfamily Escherichia coli ychN protein SUMMARY #length 114 #molecular-weight 12577 #checksum 9225 SEQUENCE /// ENTRY H64900 #type complete TITLE hypothetical protein b1477 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS H64900 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64900 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-120 ##label BLAT !'##cross-references GB:AE000244; GB:U00096; NID:g1787742; !1PIDN:AAD13441.1; PID:g1787751; UWGP:b1477 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily hypothetical protein b1477 SUMMARY #length 120 #molecular-weight 13268 #checksum 4386 SEQUENCE /// ENTRY JC4694 #type complete TITLE proteic killer active protein hig B - plasmid Rts1 ORGANISM #formal_name plasmid Rts1 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS JC4694 REFERENCE JC4693 !$#authors Tian, Q.B.; Ohnishi, M.; Tabuchi, A.; Terawaki, Y. !$#journal Biochem. Biophys. Res. Commun. (1996) 220:280-284 !$#title A new plasmid-encoded proteic killer gene system: Cloning, !1sequencing, and alalyzing hig locus of plasmid Rts1. !$#cross-references MUID:96184644; PMID:8645296 !$#accession JC4694 !'##molecule_type DNA !'##residues 1-104 ##label TIA !'##cross-references GB:U43847; NID:g1262203; PIDN:AAC43983.1; !1PID:g1262205 GENETICS !$#gene higB !$#genome plasmid CLASSIFICATION #superfamily hypothetical protein b1477 SUMMARY #length 104 #molecular-weight 11537 #checksum 2758 SEQUENCE /// ENTRY H64913 #type complete TITLE probable membrane protein b1582 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS H64913 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64913 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-108 ##label BLAT !'##cross-references GB:AE000254; GB:U00096; NID:g1787862; !1PIDN:AAC74654.1; PID:g1787865; UWGP:b1582 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily hypothetical protein b1582 KEYWORDS transmembrane protein FEATURE !$5-21 #domain transmembrane #status predicted #label TM1\ !$32-48 #domain transmembrane #status predicted #label TM2\ !$90-106 #domain transmembrane #status predicted #label TM3 SUMMARY #length 108 #molecular-weight 11919 #checksum 6335 SEQUENCE /// ENTRY S77013 #type complete TITLE hypothetical protein sll0793 - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S77013 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S77013 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-108 ##label KAN !'##cross-references EMBL:D64005; GB:AB001339; NID:g1001779; !1PID:g1001824 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily hypothetical protein b1582 SUMMARY #length 108 #molecular-weight 11998 #checksum 8727 SEQUENCE /// ENTRY H65004 #type complete TITLE hypothetical protein b2322 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS H65004 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65004 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-392 ##label BLAT !'##cross-references GB:AE000321; GB:U00096; NID:g1788659; !1PIDN:AAC75382.1; PID:g1788662; UWGP:b2322 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily hypothetical protein b2322 SUMMARY #length 392 #molecular-weight 40465 #checksum 9841 SEQUENCE /// ENTRY S47692 #type complete TITLE hypothetical 43.8K protein (ftsY-nikA intergenic region) - Escherichia coli (strain K-12) ALTERNATE_NAMES hypothetical protein f419 ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS S47692; D65144 REFERENCE S47666 !$#authors Plunkett, G. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S47692 !'##status preliminary !'##molecule_type DNA !'##residues 1-419 ##label PLU !'##cross-references EMBL:U00039; NID:g466582; PID:g912459 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65144 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-419 ##label BLAT !'##cross-references GB:AE000423; GB:U00096; NID:g1789880; !1PIDN:AAC76498.1; PID:g1789884; UWGP:b3473 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yhhS !$#start_codon GTG CLASSIFICATION #superfamily hypothetical protein b2322 SUMMARY #length 419 #molecular-weight 43783 #checksum 4573 SEQUENCE /// ENTRY A65012 #type complete TITLE probable sensor protein b2380 [similarity] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS A65012 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65012 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-565 ##label BLAT !'##cross-references GB:AE000326; GB:U00096; NID:g1788718; !1PIDN:AAC75439.1; PID:g1788723; UWGP:b2380 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily hypothetical protein b2380 SUMMARY #length 565 #molecular-weight 62657 #checksum 3817 SEQUENCE /// ENTRY E64980 #type complete TITLE hypothetical 62.1 kD protein in molR-bglX intergenic region - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS E64980 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64980 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-561 ##label BLAT !'##cross-references GB:AE000301; GB:U00096; NID:g2367129; !1PIDN:AAC75187.1; PID:g1788446; UWGP:b2126 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yehU CLASSIFICATION #superfamily hypothetical protein b2380 SUMMARY #length 561 #molecular-weight 62092 #checksum 2172 SEQUENCE /// ENTRY A69655 #type complete TITLE two-component sensor histidine kinase lytS-involved - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A69655 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69655 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-593 ##label KUN !'##cross-references GB:Z99118; GB:AL009126; NID:g2635200; !1PIDN:CAB14853.1; PID:g2635358 !'##experimental_source strain 168 GENETICS !$#gene lytS CLASSIFICATION #superfamily hypothetical protein b2380 SUMMARY #length 593 #molecular-weight 64854 #checksum 63 SEQUENCE /// ENTRY A69811 #type complete TITLE conserved hypothetical protein yflK - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A69811 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69811 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-221 ##label KUN !'##cross-references GB:Z99108; GB:AL009126; NID:g2633055; !1PIDN:CAB12594.1; PID:g2633089 !'##experimental_source strain 168 GENETICS !$#gene yflK CLASSIFICATION #superfamily hypothetical protein HI0278 SUMMARY #length 221 #molecular-weight 24834 #checksum 1796 SEQUENCE /// ENTRY S40854 #type complete TITLE hypothetical 26.6K protein (kdgt-cpxa intergenic region) - Escherichia coli (strain K-12) ALTERNATE_NAMES hypothetical protein o234 ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS S40854; A65197 REFERENCE S40802 !$#authors Plunkett III, G.; Burland, V.; Daniels, D.L.; Blattner, F.R. !$#journal Nucleic Acids Res. (1993) 21:3391-3398 !$#title Analysis of the Escherichia coli genome. III. DNA sequence !1of the region from 87.2 to 89.2 minutes. !$#cross-references MUID:93347969; PMID:8346018 !$#accession S40854 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-234 ##label PLU !'##cross-references EMBL:L19201; NID:g304961; PIDN:AAB03043.1; !1PID:g305014 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1993 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65197 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-234 ##label BLAT !'##cross-references GB:AE000466; GB:U00096; NID:g2367328; !1PIDN:AAC76892.1; PID:g1790345; UWGP:b3910 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yiiM CLASSIFICATION #superfamily hypothetical protein HI0278 SUMMARY #length 234 #molecular-weight 26561 #checksum 2138 SEQUENCE /// ENTRY C64005 #type complete TITLE hypothetical protein HI0278 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS C64005 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession C64005 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-138 ##label TIGR !'##cross-references GB:U32714; GB:L42023; NID:g1573241; !1PIDN:AAC21950.1; PID:g1573244; TIGR:HI0278 CLASSIFICATION #superfamily hypothetical protein HI0278 SUMMARY #length 138 #molecular-weight 15747 #checksum 5435 SEQUENCE /// ENTRY A69892 #type complete TITLE conserved hypothetical protein yneS - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A69892 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69892 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-193 ##label KUN !'##cross-references GB:Z99113; GB:AL009126; NID:g2634090; !1PIDN:CAB13690.1; PID:g2634190 !'##experimental_source strain 168 GENETICS !$#gene yneS CLASSIFICATION #superfamily Escherichia coli ygiH protein SUMMARY #length 193 #molecular-weight 20966 #checksum 8045 SEQUENCE /// ENTRY S75137 #type complete TITLE hypothetical protein sll1973 - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S75137 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75137 !'##status preliminary !'##molecule_type DNA !'##residues 1-222 ##label KAN !'##cross-references EMBL:D90910; GB:AB001339; NID:g1652956; !1PIDN:BAA17999.1; PID:g1653082 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily Escherichia coli ygiH protein SUMMARY #length 222 #molecular-weight 23534 #checksum 8710 SEQUENCE /// ENTRY A65094 #type complete TITLE ygiH protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS A65094 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65094 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-205 ##label BLAT !'##cross-references GB:AE000387; GB:U00096; NID:g1789431; !1PIDN:AAC76095.1; PID:g1789439; UWGP:b3059 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ygiH CLASSIFICATION #superfamily Escherichia coli ygiH protein SUMMARY #length 205 #molecular-weight 22193 #checksum 367 SEQUENCE /// ENTRY E64708 #type complete TITLE conserved hypothetical integral membrane protein HP1509 - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS E64708 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession E64708 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-262 ##label TOM !'##cross-references GB:AE000649; GB:AE000511; NID:g2314687; !1PIDN:AAD08551.1; PID:g2314690; TIGR:HP1509 CLASSIFICATION #superfamily Escherichia coli ygiH protein SUMMARY #length 262 #molecular-weight 28835 #checksum 768 SEQUENCE /// ENTRY C64227 #type complete TITLE hypothetical protein homolog MG247 - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C64227 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession C64227 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-239 ##label TIGR !'##cross-references GB:U39703; GB:L43967; NID:g3844835; !1PIDN:AAC71467.1; PID:g1045938; TIGR:MG247 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily Escherichia coli ygiH protein SUMMARY #length 239 #molecular-weight 27489 #checksum 2205 SEQUENCE /// ENTRY A69894 #type complete TITLE hypothetical protein yngL - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A69894 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69894 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-130 ##label KUN !'##cross-references GB:Z99113; GB:AL009126; NID:g2634090; !1PIDN:CAB13712.1; PID:g2634212 !'##experimental_source strain 168 GENETICS !$#gene yngL CLASSIFICATION #superfamily hypothetical protein yngL SUMMARY #length 130 #molecular-weight 14670 #checksum 9789 SEQUENCE /// ENTRY A69846 #type complete TITLE conserved hypothetical protein yjcA - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A69846 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69846 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-118 ##label KUN !'##cross-references GB:Z99110; GB:AL009126; NID:g2633472; !1PIDN:CAB13036.1; PID:g2633533 !'##experimental_source strain 168 GENETICS !$#gene yjcA CLASSIFICATION #superfamily hypothetical protein yngL SUMMARY #length 118 #molecular-weight 13035 #checksum 8484 SEQUENCE /// ENTRY A69967 #type complete TITLE conserved hypothetical protein yqkG - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A69967 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69967 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-185 ##label KUN !'##cross-references GB:Z99116; GB:AL009126; NID:g2634723; !1PIDN:CAB14293.1; PID:g2634796 !'##experimental_source strain 168 GENETICS !$#gene yqkG CLASSIFICATION #superfamily yffH protein; mutT domain homology FEATURE !$72-106 #domain mutT domain homology #label MUTT SUMMARY #length 185 #molecular-weight 20980 #checksum 2702 SEQUENCE /// ENTRY S74496 #type complete TITLE hypothetical protein sll1054 - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S74496 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74496 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-187 ##label KAN !'##cross-references EMBL:D90899; GB:AB001339; NID:g1651650; !1PIDN:BAA16648.1; PID:g1651720 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily yffH protein; mutT domain homology FEATURE !$80-114 #domain mutT domain homology #label MUTT SUMMARY #length 187 #molecular-weight 21030 #checksum 5397 SEQUENCE /// ENTRY B65022 #type complete TITLE yffH protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS B65022 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65022 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-191 ##label BLAT !'##cross-references GB:AE000333; GB:U00096; NID:g1788805; !1PIDN:AAC75520.1; PID:g1788810; UWGP:b2467 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yffH CLASSIFICATION #superfamily yffH protein; mutT domain homology SUMMARY #length 191 #molecular-weight 21749 #checksum 586 SEQUENCE /// ENTRY S48276 #type complete TITLE YSA1 protein - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YBR0907; protein YBR111c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S48276; S45979; S25364; S44691 REFERENCE S48255 !$#authors Mannhaupt, G.; Stucka, R.; Ehnle, S.; Vetter, I.; Feldmann, !1H. !$#journal Yeast (1994) 10:1363-1381 !$#title Analysis of a 70 kb region on the right arm of yeast !1chromosome II. !$#cross-references MUID:95208357; PMID:7900426 !$#accession S48276 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-231 ##label MAN !'##cross-references EMBL:X78993; NID:g476045; PIDN:CAA55614.1; !1PID:g476067 REFERENCE S45927 !$#authors Feldmann, H.; Mannhaupt, G.; Schwarzlose, C.; Vetter, I. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S45979 !'##molecule_type DNA !'##residues 1-231 ##label FE2 !'##cross-references EMBL:Z35980; NID:g536465; PID:g536466; !1GSPDB:GN00002; MIPS:YBR111c REFERENCE S25364 !$#authors Mannhaupt, G.; Stucka, R.; Ehnle, S.; Vetter, I.; Feldmann, !1H. !$#journal Yeast (1992) 8:397-408 !$#title Molecular analysis of yeast chromosome II between CMD1 and !1LYS2: the excision repair gene RAD16 located in this region !1belongs to a novel group of double-finger proteins. !$#cross-references MUID:92327848; PMID:1626431 !$#accession S25364 !'##molecule_type DNA !'##residues 1-47 ##label MAW !'##cross-references EMBL:X66247; NID:g3548; PIDN:CAA46972.1; PID:g3549 GENETICS !$#gene SGD:YSA1; MIPS:YBR111c !'##cross-references SGD:S0000315; MIPS:YBR111c !$#map_position 2R CLASSIFICATION #superfamily yffH protein; mutT domain homology FEATURE !$111-145 #domain mutT domain homology #label MUTT SUMMARY #length 231 #molecular-weight 26087 #checksum 4809 SEQUENCE /// ENTRY D64757 #type complete TITLE ykgG protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS D64757 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64757 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-282 ##label BLAT !'##cross-references GB:AE000137; GB:U00096; NID:g2367108; !1PIDN:AAC73411.1; PID:g1786499; UWGP:b0308 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ykgG CLASSIFICATION #superfamily ykgG protein SUMMARY #length 282 #molecular-weight 31132 #checksum 5854 SEQUENCE /// ENTRY A70031 #type complete TITLE conserved hypothetical protein yvbY - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A70031 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A70031 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-240 ##label KUN !'##cross-references GB:Z99121; GB:AL009126; NID:g2635827; !1PIDN:CAB15408.1; PID:g2635916 !'##experimental_source strain 168 GENETICS !$#gene yvbY CLASSIFICATION #superfamily ykgG protein SUMMARY #length 240 #molecular-weight 26277 #checksum 5615 SEQUENCE /// ENTRY D64814 #type complete TITLE ybhK protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS D64814 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64814 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-302 ##label BLAT !'##cross-references GB:AE000180; GB:U00096; NID:g1786988; !1PIDN:AAC73867.1; PID:g1786997; UWGP:b0780 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ybhK CLASSIFICATION #superfamily Escherichia coli ybhK protein SUMMARY #length 302 #molecular-weight 32788 #checksum 3710 SEQUENCE /// ENTRY S76100 #type complete TITLE hypothetical protein - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S76100 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76100 !'##status preliminary !'##molecule_type DNA !'##residues 1-462 ##label KAN !'##cross-references EMBL:D63999; GB:AB001339; NID:g1001396; !1PID:g1001453 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily Escherichia coli ybhK protein SUMMARY #length 462 #molecular-weight 51007 #checksum 2981 SEQUENCE /// ENTRY A70032 #type complete TITLE conserved hypothetical protein yvcK - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A70032 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A70032 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-331 ##label KUN !'##cross-references GB:Z99121; GB:AL009126; NID:g2635827; !1PIDN:CAB15481.1; PID:g2635989 !'##experimental_source strain 168 GENETICS !$#gene yvcK CLASSIFICATION #superfamily Escherichia coli ybhK protein SUMMARY #length 331 #molecular-weight 36201 #checksum 7757 SEQUENCE /// ENTRY S60035 #type complete TITLE senescence marker protein 30 - human ALTERNATE_NAMES regucalcin ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S60035; I52491 REFERENCE I52491 !$#authors Fujita, T.; Mandel, J.L.; Shirasawa, T.; Hino, O.; Shirai, !1T.; Maruyama, N. !$#journal Biochim. Biophys. Acta (1995) 1263:249-252 !$#title Isolation of cDNA clone encoding human homologue of !1senescence marker protein-30 (SMP30) and its location on the !1X chromosome. !$#cross-references MUID:96004897; PMID:7548213 !$#accession S60035 !'##molecule_type mRNA !'##residues 1-299 ##label FUJ !'##cross-references EMBL:D31815; NID:g1072311; PIDN:BAA06602.1; !1PID:g1072312 GENETICS !$#gene GDB:RGN; RC; SMP30 !'##cross-references GDB:9955055 !$#map_position Xp11.3-Xp11.2 CLASSIFICATION #superfamily senescence marker protein-30 KEYWORDS calcium binding SUMMARY #length 299 #molecular-weight 33253 #checksum 7020 SEQUENCE /// ENTRY A70047 #type complete TITLE RNA polymerase homolog yvrE - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A70047 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A70047 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-292 ##label KUN !'##cross-references GB:Z99120; GB:Z99121; GB:AL009126; NID:g2635827; !1PID:g2635833; NID:g2635613; PID:g2635817 !'##experimental_source strain 168 GENETICS !$#gene yvrE CLASSIFICATION #superfamily senescence marker protein-30 SUMMARY #length 292 #molecular-weight 33204 #checksum 3347 SEQUENCE /// ENTRY A70049 #type complete TITLE conserved hypothetical protein yvyE - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A70049; A30191 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A70049 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-217 ##label KUN !'##cross-references GB:Z99122; GB:AL009126; NID:g2636029; !1PIDN:CAB15568.1; PID:g2636077 !'##experimental_source strain 168 REFERENCE A30191 !$#authors Henner, D.J.; Yang, M.; Ferrari, E. !$#journal J. Bacteriol. (1988) 170:5102-5109 !$#title Localization of Bacillus subtilis sacU(Hy) mutations to two !1linked genes with similarities to the conserved procaryotic !1family of two-component signalling systems. !$#cross-references MUID:89033891; PMID:3141378 !$#accession A30191 !'##molecule_type DNA !'##residues 1-164,'LIQKMLN' ##label HEN GENETICS !$#gene yvyE CLASSIFICATION #superfamily hypothetical protein HI0722 SUMMARY #length 217 #molecular-weight 24838 #checksum 7849 SEQUENCE /// ENTRY I64088 #type complete TITLE conserved hypothetical protein HI0722 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS I64088 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession I64088 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-206 ##label TIGR !'##cross-references GB:U32755; GB:L42023; NID:g3212203; !1PIDN:AAC22380.1; PID:g1573725; TIGR:HI0722 CLASSIFICATION #superfamily hypothetical protein HI0722 SUMMARY #length 206 #molecular-weight 22710 #checksum 3466 SEQUENCE /// ENTRY E64705 #type complete TITLE conserved hypothetical protein - Helicobacter pylori (strain 26695) ALTERNATE_NAMES proline dipeptidase ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS E64705 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession E64705 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-190 ##label TOM !'##cross-references GB:AE000647; GB:AE000511; NID:g2314645; !1PIDN:AAD08520.1; PID:g2314657; TIGR:HP1485 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily hypothetical protein HI0722 SUMMARY #length 190 #molecular-weight 21467 #checksum 1376 SEQUENCE /// ENTRY B64802 #type complete TITLE nagD protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS B64802; D37018; S06991 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64802 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-250 ##label BLAT !'##cross-references GB:AE000171; GB:U00096; NID:g1786888; !1PIDN:AAC73769.1; PID:g1786890; UWGP:b0675 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A37018 !$#authors Peri, K.G.; Goldie, H.; Waygood, E.B. !$#journal Biochem. Cell Biol. (1990) 68:123-137 !$#title Cloning and characterization of the N-acetylglucosamine !1operon of Escherichia coli. !$#cross-references MUID:90274974; PMID:2190615 !$#accession D37018 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-96,'Y',98-250 ##label PER !'##cross-references GB:AF052007; NID:g3005593; PIDN:AAC09327.1; !1PID:g3005597 REFERENCE S06989 !$#authors Plumbridge, J.A. !$#journal Mol. Microbiol. (1989) 3:505-515 !$#title Sequence of the nagBACD operon in Escherichia coli K12 and !1pattern of transcription within the nag regulon. !$#cross-references MUID:89343637; PMID:2668691 !$#accession S06991 !'##molecule_type DNA !'##residues 1-250 ##label PLU !'##cross-references EMBL:X14135; NID:g42078; PIDN:CAA32355.1; !1PID:g42081 GENETICS !$#gene nagD !$#map_position 15 min CLASSIFICATION #superfamily nagD protein SUMMARY #length 250 #molecular-weight 27163 #checksum 7705 SEQUENCE /// ENTRY G69587 #type complete TITLE L-arabinose operon araL - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69587 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69587 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-272 ##label KUN !'##cross-references GB:Z99118; GB:AL009126; NID:g2635200; !1PIDN:CAB14837.1; PID:g2635342 !'##experimental_source strain 168 GENETICS !$#gene araL CLASSIFICATION #superfamily nagD protein SUMMARY #length 272 #molecular-weight 29314 #checksum 9010 SEQUENCE /// ENTRY F69296 #type complete TITLE p-nitrophenyl phosphatase (pho2) homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F69296 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession F69296 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-265 ##label KLE !'##cross-references GB:AE001078; GB:AE000782; NID:g2689401; !1PIDN:AAB90861.1; PID:g2650258; TIGR:AF0374 CLASSIFICATION #superfamily nagD protein SUMMARY #length 265 #molecular-weight 29077 #checksum 330 SEQUENCE /// ENTRY H70023 #type complete TITLE N-acetyl-glucosamine catabolism homolog yutF - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H70023 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H70023 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-256 ##label KUN !'##cross-references GB:Z99120; GB:AL009126; NID:g2635613; !1PIDN:CAB15219.1; PID:g2635726 !'##experimental_source strain 168 GENETICS !$#gene yutF CLASSIFICATION #superfamily nagD protein SUMMARY #length 256 #molecular-weight 27957 #checksum 3941 SEQUENCE /// ENTRY B69757 #type complete TITLE toxic anion resistance protein homolog yceH - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69757 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69757 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-363 ##label KUN !'##cross-references GB:Z99105; GB:AL009126; NID:g2632457; !1PIDN:CAB12088.1; PID:g2632580 !'##experimental_source strain 168 GENETICS !$#gene yceH CLASSIFICATION #superfamily telA protein SUMMARY #length 363 #molecular-weight 41673 #checksum 3494 SEQUENCE /// ENTRY S66056 #type complete TITLE yaaN protein - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S66056; S27527; E69737 REFERENCE S65967 !$#authors Ogasawara, N.; Nakai, S.; Yoshikawa, H. !$#journal DNA Res. (1994) 1:1-14 !$#title Systematic sequencing of the 180 kilobase region of the !1Bacillus subtilis chromosome containing the replication !1origin. !$#cross-references MUID:96051385; PMID:7584024 !$#accession S66056 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-386 ##label OGA !'##cross-references EMBL:D26185; NID:g467326; PIDN:BAA05262.1; !1PID:g467416 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1993 REFERENCE S27525 !$#authors Bookstein, C.; Edwards, C.W.; Hulett, F.M. !$#submission submitted to the EMBL Data Library, June 1992 !$#description Characterization of the Bacillus subtilis xpaC gene, which !1in double copy causes aberrant cell morphology, !1filamentation and inhibits sporulation. !$#accession S27527 !'##status preliminary !'##molecule_type DNA !'##residues 1-190,'M' ##label BOO !'##cross-references EMBL:M96156; NID:g143828; PID:g551736 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69737 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-386 ##label KUN !'##cross-references GB:Z99104; GB:AL009126; NID:g2632267; !1PIDN:CAB11802.1; PID:g2632293 !'##experimental_source strain 168 GENETICS !$#gene yaaN CLASSIFICATION #superfamily telA protein SUMMARY #length 386 #molecular-weight 43830 #checksum 5320 SEQUENCE /// ENTRY B38178 #type complete TITLE telA protein - plasmid RK2 ALTERNATE_NAMES klaB protein ORGANISM #formal_name plasmid RK2 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 18-Aug-2000 ACCESSIONS B38178; B42362 REFERENCE A38178 !$#authors Walter, E.G.; Thomas, C.M.; Ibbotson, J.P.; Taylor, D.E. !$#journal J. Bacteriol. (1991) 173:1111-1119 !$#title Transcriptional analysis, translational analysis, and !1sequence of the kilA-tellurite resistance region of plasmid !1RK2Te(r). !$#cross-references MUID:91123183; PMID:1846856 !$#accession B38178 !'##molecule_type DNA !'##residues 1-378 ##label WAL !'##cross-references GB:M62846; GB:M38697; NID:g149152; PIDN:AAA98154.1; !1PID:g149154 REFERENCE A42362 !$#authors Goncharoff, P.; Saadi, S.; Chang, C.H.; Saltman, L.H.; !1Figurski, D.H. !$#journal J. Bacteriol. (1991) 173:3463-3477 !$#title Structural, molecular, and genetic analysis of the kilA !1operon of broad-host-range plasmid RK2. !$#cross-references MUID:91258329; PMID:2045366 !$#accession B42362 !'##molecule_type DNA !'##residues 1-378 ##label GON !'##cross-references GB:M62426; NID:g152517; PIDN:AAA26402.1; !1PID:g152519 COMMENT The RK2 plasmid is a member of the P-alpha incompatibility !1group of plasmids, which replicate and are maintained stably !1in a wide variety of gram-negative bacteria. GENETICS !$#genome plasmid CLASSIFICATION #superfamily telA protein SUMMARY #length 378 #molecular-weight 42156 #checksum 4185 SEQUENCE /// ENTRY B69892 #type complete TITLE conserved hypothetical protein yneT - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69892 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69892 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-135 ##label KUN !'##cross-references GB:Z99113; GB:AL009126; NID:g2634090; !1PIDN:CAB13691.1; PID:g2634191 !'##experimental_source strain 168 GENETICS !$#gene yneT CLASSIFICATION #superfamily hypothetical protein yneT SUMMARY #length 135 #molecular-weight 14989 #checksum 8392 SEQUENCE /// ENTRY D64837 #type complete TITLE hypothetical protein b0965 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS D64837 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64837 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-164 ##label BLAT !'##cross-references GB:AE000198; GB:U00096; NID:g1787189; !1PIDN:AAC74051.1; PID:g1787199; UWGP:b0965 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily hypothetical protein yneT SUMMARY #length 164 #molecular-weight 17706 #checksum 7438 SEQUENCE /// ENTRY B69906 #type complete TITLE rarD protein homolog yojE - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69906 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69906 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-263 ##label KUN !'##cross-references GB:Z99114; GB:AL009126; NID:g2634230; !1PIDN:CAB13840.1; PID:g2634341 !'##experimental_source strain 168 GENETICS !$#gene yojE CLASSIFICATION #superfamily Escherichia coli rarD protein SUMMARY #length 263 #molecular-weight 29277 #checksum 398 SEQUENCE /// ENTRY S30709 #type complete TITLE rarD protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS S30709; D65186 REFERENCE S30660 !$#authors Daniels, D.L.; Plunkett III, G.; Burland, V.; Blattner, F.R. !$#journal Science (1992) 257:771-778 !$#title Analysis of the Escherichia coli genome: DNA sequence of the !1region from 84.5 to 86.5 minutes. !$#cross-references MUID:92358234; PMID:1379743 !$#accession S30709 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-300 ##label DAN !'##cross-references EMBL:M87049; NID:g836656; PIDN:AAA67615.1; !1PID:g148218 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1992 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65186 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-300 ##label BLAT !'##cross-references GB:AE000457; GB:U00096; NID:g2367294; !1PIDN:AAC76822.1; PID:g1790252; UWGP:b3819 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene rarD CLASSIFICATION #superfamily Escherichia coli rarD protein SUMMARY #length 300 #molecular-weight 33703 #checksum 9949 SEQUENCE /// ENTRY I64085 #type complete TITLE rarD protein homolog HI0680 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS I64085 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession I64085 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-298 ##label TIGR !'##cross-references GB:U32750; GB:L42023; NID:g1573668; !1PIDN:AAC22339.1; PID:g1573680; TIGR:HI0680 CLASSIFICATION #superfamily Escherichia coli rarD protein SUMMARY #length 298 #molecular-weight 33463 #checksum 1380 SEQUENCE /// ENTRY S03778 #type complete TITLE uviB protein - Clostridium perfringens plasmid pIP404 ORGANISM #formal_name Clostridium perfringens DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 18-Aug-2000 ACCESSIONS S03778; JT0354 REFERENCE S03777 !$#authors Garnier, T.; Cole, S.T. !$#journal Mol. Microbiol. (1988) 2:607-614 !$#title Studies of UV-inducible promoters from Clostridium !1perfringens in vivo and in vitro. !$#cross-references MUID:89039249; PMID:2460717 !$#accession S03778 !'##molecule_type DNA !'##residues 1-64 ##label GAR !'##cross-references EMBL:M32882; NID:g150738; PIDN:AAA98258.1; !1PID:g150748 GENETICS !$#gene uviB !$#genome plasmid CLASSIFICATION #superfamily uviB protein SUMMARY #length 64 #molecular-weight 7616 #checksum 6364 SEQUENCE /// ENTRY B69954 #type complete TITLE penicillin tolerance homolog yqfP - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69954 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69954 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-314 ##label KUN !'##cross-references GB:Z99116; GB:AL009126; NID:g2634723; !1PIDN:CAB14446.1; PID:g2634949 !'##experimental_source strain 168 GENETICS !$#gene yqfP CLASSIFICATION #superfamily penicillin tolerance protein SUMMARY #length 314 #molecular-weight 34924 #checksum 2122 SEQUENCE /// ENTRY A64164 #type complete TITLE lytB protein homolog HI1007 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A64164 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession A64164 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-318 ##label TIGR !'##cross-references GB:L42023; TIGR:HI1007 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily penicillin tolerance protein SUMMARY #length 318 #molecular-weight 34972 #checksum 245 SEQUENCE /// ENTRY H64569 #type complete TITLE lysis tolerance protein - Helicobacter pylori ALTERNATE_NAMES penicillin tolerance protein ORGANISM #formal_name Helicobacter pylori #variety strains J99, 26695 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS H64569; H71863 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession H64569 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-274 ##label TOM !'##cross-references GB:AE000556; GB:AE000511; NID:g2313505; !1PIDN:AAD07469.1; PID:g2313506; TIGR:HP0400 !'##experimental_source strain 26695 REFERENCE A71800 !$#authors Alm, R.A.; Ling, L.S.L.; Moir, D.T.; King, B.L.; Brown, !1E.D.; Doig, P.C.; Smith, D.R.; Noonan, B.; Guild, B.C.; !1deJonge, B.L.; Carmel, G.; Tummino, P.J.; Caruso, A.; !1Uria-Nickelsen, M.; Mills, D.M.; Ives, C.; Gibson, R.; !1Merberg, D.; Mills, S.D.; Jiang, Q.; Taylor, D.E.; Vovis, !1G.F.; Trust, T.J. !$#journal Nature (1999) 397:176-180 !$#title Genomic sequence comparison of two unrelated isolates of the !1human gastric pathogen Helicobacter pylori. !$#cross-references MUID:99120557; PMID:9923682 !$#accession H71863 !'##molecule_type DNA !'##residues 1-274 ##label ARN !'##cross-references GB:AE001527; GB:AE001439; NID:g4155558; !1PIDN:AAD06556.1; PID:g4155562 !'##experimental_source strain J99 GENETICS !$#gene lytB; HP0400 CLASSIFICATION #superfamily penicillin tolerance protein SUMMARY #length 274 #molecular-weight 30917 #checksum 8783 SEQUENCE /// ENTRY B69997 #type complete TITLE conserved hypothetical protein ytmQ - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69997 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69997 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-213 ##label KUN !'##cross-references GB:Z99119; GB:AL009126; NID:g2635411; !1PIDN:CAB14968.1; PID:g2635474 !'##experimental_source strain 168 GENETICS !$#gene ytmQ CLASSIFICATION #superfamily hypothetical protein HI0340 SUMMARY #length 213 #molecular-weight 24504 #checksum 6622 SEQUENCE /// ENTRY D64238 #type complete TITLE hypothetical protein homolog MG347 - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 07-Dec-1999 ACCESSIONS D64238 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession D64238 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-210 ##label TIGR !'##cross-references GB:U39718; GB:L43967; NID:g1046047; PID:g1046053; !1TIGR:MG347 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 !$#start_codon GTG CLASSIFICATION #superfamily hypothetical protein HI0340 SUMMARY #length 210 #molecular-weight 24929 #checksum 2806 SEQUENCE /// ENTRY F64148 #type complete TITLE hypothetical protein HI0340 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS F64148 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession F64148 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-246 ##label TIGR !'##cross-references GB:U32719; GB:L42023; NID:g1573310; !1PIDN:AAC22002.1; PID:g1573311; TIGR:HI0340 !'##note best homolog was a hypothetical protein from Escherichia coli CLASSIFICATION #superfamily hypothetical protein HI0340 SUMMARY #length 246 #molecular-weight 28053 #checksum 6797 SEQUENCE /// ENTRY S75273 #type complete TITLE hypothetical protein sll1300 - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S75273 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75273 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-192 ##label KAN !'##cross-references EMBL:D90904; GB:AB001339; NID:g1652225; !1PIDN:BAA17187.1; PID:g1652264 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily hypothetical protein HI0340 SUMMARY #length 192 #molecular-weight 22084 #checksum 6171 SEQUENCE /// ENTRY B70071 #type complete TITLE conserved hypothetical protein yxaB - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B70071 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B70071 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-317 ##label KUN !'##cross-references GB:Z99124; GB:AL009126; NID:g2636442; !1PIDN:CAB16040.1; PID:g2636550 !'##experimental_source strain 168 GENETICS !$#gene yxaB CLASSIFICATION #superfamily hypothetical protein yxaB SUMMARY #length 317 #molecular-weight 36550 #checksum 7211 SEQUENCE /// ENTRY H70036 #type complete TITLE conserved hypothetical protein yveS - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H70036 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H70036 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-358 ##label KUN !'##cross-references GB:Z99121; GB:AL009126; NID:g2635827; !1PIDN:CAB15434.1; PID:g2635942 !'##experimental_source strain 168 GENETICS !$#gene yveS CLASSIFICATION #superfamily hypothetical protein yxaB SUMMARY #length 358 #molecular-weight 41508 #checksum 2348 SEQUENCE /// ENTRY G70037 #type complete TITLE conserved hypothetical protein yvfF - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G70037 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G70037 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-322 ##label KUN !'##cross-references GB:Z99121; GB:AL009126; NID:g2635827; !1PIDN:CAB15427.1; PID:g2635935 !'##experimental_source strain 168 GENETICS !$#gene yvfF CLASSIFICATION #superfamily hypothetical protein yxaB SUMMARY #length 322 #molecular-weight 37274 #checksum 5253 SEQUENCE /// ENTRY C69661 #type complete TITLE transcription activator of multidrug-efflux transporter genes mta - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69661 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69661 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-257 ##label KUN !'##cross-references GB:Z99122; GB:AL009126; NID:g2636029; !1PIDN:CAB15677.1; PID:g2636185 !'##experimental_source strain 168 GENETICS !$#gene mta CLASSIFICATION #superfamily tipA protein SUMMARY #length 257 #molecular-weight 29935 #checksum 217 SEQUENCE /// ENTRY S35354 #type complete TITLE tipA protein - Streptomyces lividans ORGANISM #formal_name Streptomyces lividans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S35354; A45923 REFERENCE S35354 !$#authors Holmes, D.J.; Caso, J.L.; Thompson, C.J. !$#journal EMBO J. (1993) 12:3183-3191 !$#title Autogenous transcriptional activation of a !1thiostrepton-induced gene in Streptomyces lividans. !$#cross-references MUID:93345463; PMID:7688297 !$#accession S35354 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-253 ##label HOL !'##cross-references GB:S64314; NID:g408222; PIDN:AAB27737.1; !1PID:g408223 !'##note part of this sequence was confirmed by protein sequencing REFERENCE A45923 !$#authors Murakami, T.; Holt, T.G.; Thompson, C.J. !$#journal J. Bacteriol. (1989) 171:1459-1466 !$#title Thiostrepton-induced gene expression in Streptomyces !1lividans. !$#cross-references MUID:89155448; PMID:2537819 !$#accession A45923 !'##status preliminary !'##molecule_type DNA !'##residues 110-253 ##label MUR !'##cross-references GB:M24524; NID:g341187; PIDN:AAC13653.1; !1PID:g530217 GENETICS !$#gene tipA !$#start_codon GTG CLASSIFICATION #superfamily tipA protein KEYWORDS alternative initiators; DNA binding; transcription !1regulation FEATURE !$1-253 #product tipA protein long form #status predicted !8#label MAT1\ !$110-253 #product tipA protein short form #status predicted !8#label MAT2 SUMMARY #length 253 #molecular-weight 28711 #checksum 3466 SEQUENCE /// ENTRY A39017 #type complete TITLE nodulation control protein nolA - Bradyrhizobium japonicum ORGANISM #formal_name Bradyrhizobium japonicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A39017 REFERENCE A39017 !$#authors Sadowsky, M.J.; Cregan, P.B.; Gottfert, M.; Sharma, A.; !1Gerhold, D.; Rodriguez-Quinones, F.; Keyser, H.H.; Hennecke, !1H.; Stacey, G. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1991) 88:637-641 !$#title The Bradyrhizobium japonicum nolA gene and its involvement !1in the genotype-specific nodulation of soybeans. !$#cross-references MUID:91110583; PMID:1988958 !$#accession A39017 !'##status preliminary !'##molecule_type DNA !'##residues 1-237 ##label SAD !'##cross-references GB:M58360; NID:g152127; PIDN:AAA26237.1; !1PID:g152128 CLASSIFICATION #superfamily tipA protein KEYWORDS DNA binding SUMMARY #length 237 #molecular-weight 26871 #checksum 6246 SEQUENCE /// ENTRY A69677 #type complete TITLE phosphatase (RapC) regulator / competence and sporulation stimu phrC - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A69677 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69677 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-40 ##label KUN !'##cross-references GB:Z99106; GB:AL009126; NID:g2632653; !1PIDN:CAB12186.1; PID:g2632679 !'##experimental_source strain 168 GENETICS !$#gene phrC CLASSIFICATION #superfamily phosphatase regulator SUMMARY #length 40 #molecular-weight 4198 #checksum 601 SEQUENCE /// ENTRY C69677 #type complete TITLE phosphatase (RapF) regulator phrF - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69677 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69677 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-39 ##label KUN !'##cross-references GB:Z99123; GB:AL009126; NID:g2636240; !1PIDN:CAB15774.1; PID:g2636283 !'##experimental_source strain 168 GENETICS !$#gene phrF CLASSIFICATION #superfamily phosphatase regulator SUMMARY #length 39 #molecular-weight 4199 #checksum 9304 SEQUENCE /// ENTRY C69744 #type complete TITLE conserved hypothetical protein ybbH - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69744 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69744 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-283 ##label KUN !'##cross-references GB:Z99104; GB:AL009126; NID:g2632267; !1PIDN:CAB11945.1; PID:g2632436 !'##experimental_source strain 168 GENETICS !$#gene ybbH CLASSIFICATION #superfamily hypothetical protein ybbH SUMMARY #length 283 #molecular-weight 30709 #checksum 7408 SEQUENCE /// ENTRY E64947 #type complete TITLE yebK protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS E64947 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64947 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-289 ##label BLAT !'##cross-references GB:AE000279; GB:U00096; NID:g1788154; !1PIDN:AAC74923.1; PID:g1788159; UWGP:b1853 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yebK CLASSIFICATION #superfamily hypothetical protein ybbH SUMMARY #length 289 #molecular-weight 31975 #checksum 8273 SEQUENCE /// ENTRY G64143 #type complete TITLE hypothetical protein HI0143 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS G64143 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession G64143 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-299 ##label TIGR !'##cross-references GB:L42023; TIGR:HI0143 !'##note best homolog was a hypothetical protein from Clostridium !1perfringens CLASSIFICATION #superfamily hypothetical protein ybbH SUMMARY #length 299 #molecular-weight 32939 #checksum 3159 SEQUENCE /// ENTRY S43902 #type complete TITLE hypothetical protein B - Clostridium perfringens ORGANISM #formal_name Clostridium perfringens DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S43902; S27538 REFERENCE S43901 !$#authors Canard, B.; Garnier, T.; Saint-Joanis, B.; Cole, S.T. !$#journal Mol. Gen. Genet. (1994) 243:215-224 !$#title Molecular genetic analysis of the nagH gene encoding a !1hyaluronidase of Clostridium perfringens. !$#cross-references MUID:94232189; PMID:8177218 !$#accession S43902 !'##status preliminary !'##molecule_type DNA !'##residues 1-279 ##label CAN !'##cross-references EMBL:M81878; NID:g144857; PIDN:AAA23257.1; !1PID:g144859 CLASSIFICATION #superfamily hypothetical protein ybbH SUMMARY #length 279 #molecular-weight 31254 #checksum 8667 SEQUENCE /// ENTRY H65033 #type complete TITLE hypothetical protein in purL-dpj intergenic region - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS H65033 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65033 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-306 ##label BLAT !'##cross-references GB:AE000342; GB:U00096; NID:g1788907; !1PIDN:AAC75614.1; PID:g1788913; UWGP:b2561 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yfhH CLASSIFICATION #superfamily hypothetical protein ybbH SUMMARY #length 306 #molecular-weight 33654 #checksum 2620 SEQUENCE /// ENTRY I40661 #type complete TITLE mutL protein - Clostridium cochlearium ALTERNATE_NAMES glmL protein; methylaspartate mutase component L [misnomer] ORGANISM #formal_name Clostridium cochlearium DATE 18-Feb-2000 #sequence_revision 18-Feb-2000 #text_change 18-Feb-2000 ACCESSIONS I40661; S47463 REFERENCE I40659 !$#authors Zelder, O.; Beatrix, B.; Leutbecher, U.; Buckel, W. !$#journal Eur. J. Biochem. (1994) 226:577-585 !$#title Characterization of the coenzyme-B12-dependent glutamate !1mutase from Clostridium cochlearium produced in Escherichia !1coli. !$#cross-references MUID:95094816; PMID:7880251 !$#accession I40661 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-463 ##label RES !'##cross-references EMBL:X80997; NID:g530005; PIDN:CAA56922.1; !1PID:g580977 COMMENT The function of this protein, whose gene is located between !1those of mutE (glmE) and mutS (glmS), is unknown. GENETICS !$#gene mutL; glmL !$#start_codon GTG CLASSIFICATION #superfamily Clostridium mutL protein SUMMARY #length 463 #molecular-weight 50357 #checksum 9882 SEQUENCE /// ENTRY S29503 #type complete TITLE mutL protein - Clostridium tetanomorphum (strain NCIMB 11547) ALTERNATE_NAMES glmL protein ORGANISM #formal_name Clostridium tetanomorphum DATE 18-Feb-2000 #sequence_revision 18-Feb-2000 #text_change 18-Feb-2000 ACCESSIONS S29503 REFERENCE S29501 !$#authors Holloway, D.E.; Marsh, E.N.G. !$#journal FEBS Lett. (1993) 317:44-48 !$#title Cloning and sequencing of glutamate mutase component E from !1Clostridium tetanomorphum. Organization of the mut genes. !$#cross-references MUID:93154518; PMID:8428631 !$#accession S29503 !'##molecule_type DNA !'##residues 1-462 ##label HOL !'##cross-references EMBL:X70499; NID:g49238; PIDN:CAA49909.1; !1PID:g581010 COMMENT The function of this protein, whose gene is located between !1those of mutE (glmE) and mutS (glmS), is unknown. GENETICS !$#gene mutL !$#start_codon GTG CLASSIFICATION #superfamily Clostridium mutL protein SUMMARY #length 462 #molecular-weight 50203 #checksum 9955 SEQUENCE /// ENTRY C69750 #type complete TITLE yceA protein homolog ybfQ - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69750 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69750 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-322 ##label KUN !'##cross-references GB:Z99105; GB:AL009126; NID:g2632457; !1PIDN:CAB12027.1; PID:g2632519 !'##experimental_source strain 168 GENETICS !$#gene ybfQ CLASSIFICATION #superfamily Escherichia coli yceA protein SUMMARY #length 322 #molecular-weight 37265 #checksum 7897 SEQUENCE /// ENTRY S76272 #type complete TITLE yceA protein homolog - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S76272 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76272 !'##status preliminary !'##molecule_type DNA !'##residues 1-278 ##label KAN !'##cross-references EMBL:D64000; GB:AB001339; NID:g1001484; !1PID:g1001499 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily Escherichia coli yceA protein SUMMARY #length 278 #molecular-weight 31166 #checksum 9615 SEQUENCE /// ENTRY D64848 #type complete TITLE yceA protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS D64848; S16889 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64848 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-350 ##label BLAT !'##cross-references GB:AE000207; GB:U00096; NID:g1787293; !1PIDN:AAC74139.1; PID:g1787294; UWGP:b1055 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S16888 !$#authors Karow, M.; Georgopoulos, C. !$#journal Mol. Microbiol. (1991) 5:2285-2292 !$#title Sequencing, mutational analysis, and transcriptional !1regulation of the Escherichia coli htrB gene. !$#cross-references MUID:92114808; PMID:1840644 !$#accession S16889 !'##status translation not shown !'##molecule_type DNA !'##residues 1-81,'HV',84-311,'R',313-350 ##label KAR !'##cross-references EMBL:X61000; NID:g48956; PIDN:CAA43318.1; !1PID:g48958 !'##experimental_source strain K-12 GENETICS !$#gene yceA CLASSIFICATION #superfamily Escherichia coli yceA protein KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$98-105 #region nucleotide-binding motif A (P-loop) SUMMARY #length 350 #molecular-weight 39781 #checksum 6323 SEQUENCE /// ENTRY C69762 #type complete TITLE di-tripeptide ABC transporter (membrane pr) homolog yclF - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69762 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69762 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-492 ##label KUN !'##cross-references GB:Z99106; GB:AL009126; NID:g2632653; !1PIDN:CAB12175.1; PID:g2632668 !'##experimental_source strain 168 GENETICS !$#gene yclF CLASSIFICATION #superfamily peptide transporter protein SUMMARY #length 492 #molecular-weight 53275 #checksum 9486 SEQUENCE /// ENTRY A53620 #type complete TITLE peptide transport protein DtpT - Lactococcus lactis ORGANISM #formal_name Lactococcus lactis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A53620 REFERENCE A53620 !$#authors Hagting, A.; Kunji, E.R.S.; Leenhouts, K.J.; Poolman, B.; !1Konings, W.N. !$#journal J. Biol. Chem. (1994) 269:11391-11399 !$#title The Di- and tripeptide transport protein of Lactococcus !1lactis. A new type of bacterial peptide transporter. !$#cross-references MUID:94209318; PMID:8157671 !$#accession A53620 !'##status preliminary !'##molecule_type DNA !'##residues 1-463 ##label HAG !'##cross-references GB:U05215; NID:g451071; PIDN:AAA20660.1; !1PID:g451072 GENETICS !$#gene dtpT CLASSIFICATION #superfamily peptide transporter protein KEYWORDS transmembrane protein SUMMARY #length 463 #molecular-weight 50630 #checksum 664 SEQUENCE /// ENTRY D64806 #type complete TITLE probable proton/oligopeptide symporter ybgH - Escherichia coli (strain K-12) ALTERNATE_NAMES protein f485 ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS D64806; T48921 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64806 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-493 ##label BLAT !'##cross-references GB:AE000174; GB:U00096; NID:g1786920; !1PIDN:AAC73803.1; PID:g1786927; UWGP:b0709 !'##experimental_source strain K-12, substrain MG1655 REFERENCE Z25006 !$#authors Oshima, T.; Aiba, H.; Baba, T.; Fujita, K.; Hayashi, K.; !1Honjo, A.; Ikemoto, K.; Inada, T.; Itoh, T.; Kajihara, M.; !1Kanai, K.; Kashimoto, K.; Kimura, S.; Kitagawa, M.; Makino, !1K.; Masuda, S.; Miki, T.; Mizobuchi, K.; Mori, H.; Motomura, !1K.; Nakamura, Y.; Nashimoto, H.; Nishio, Y.; Saito, N.; !1Sampei, G.; Seki, Y.; Tagami, H.; Takemoto, K.; Wada, C.; !1Yamamoto, Y.; Yano, M.; Horiuchi, T. !$#journal DNA Res. (1996) 3:137-155 !$#title A 718-kb DNA Sequence of Escherichia coli K-12 Genome !1Corresponding to the 12.7-28.0 min Region on the Linkage !1Map. !$#cross-references MUID:97061202; PMID:8905232 !$#accession T48921 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 179-493 ##label OSH !'##cross-references EMBL:D90709; GB:AB001340; NID:g1651305; !1PIDN:BAA35368.1; PID:g4062301 !'##experimental_source strain K12; Kohara clone 174 GENETICS !$#gene ybgH !$#map_position 15.7-16.0 FUNCTION !$#description probably involved in the intake of small peptides with the !1concomitant uptake of a proton CLASSIFICATION #superfamily peptide transporter protein KEYWORDS transmembrane protein; transport protein FEATURE !$77-93 #domain transmembrane #status predicted #label TM01\ !$101-117 #domain transmembrane #status predicted #label TM02\ !$171-187 #domain transmembrane #status predicted #label TM03\ !$215-231 #domain transmembrane #status predicted #label TM04\ !$236-252 #domain transmembrane #status predicted #label TM05\ !$267-283 #domain transmembrane #status predicted #label TM06\ !$316-332 #domain transmembrane #status predicted #label TM07\ !$348-364 #domain transmembrane #status predicted #label TM08\ !$378-394 #domain transmembrane #status predicted #label TM09\ !$410-426 #domain transmembrane #status predicted #label TM10\ !$462-478 #domain transmembrane #status predicted #label TM11 SUMMARY #length 493 #molecular-weight 54158 #checksum 9839 SEQUENCE /// ENTRY D64920 #type complete TITLE probable membrane protein b1634 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS D64920 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64920 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-500 ##label BLAT !'##cross-references GB:AE000259; GB:U00096; NID:g1787921; !1PIDN:AAC74706.1; PID:g1787922; UWGP:b1634 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily peptide transporter protein FEATURE !$60-76 #domain transmembrane #status predicted #label TM01\ !$90-106 #domain transmembrane #status predicted #label TM02\ !$181-197 #domain transmembrane #status predicted #label TM03\ !$221-237 #domain transmembrane #status predicted #label TM04\ !$244-260 #domain transmembrane #status predicted #label TM05\ !$275-291 #domain transmembrane #status predicted #label TM06\ !$323-339 #domain transmembrane #status predicted #label TM07\ !$353-369 #domain transmembrane #status predicted #label TM08\ !$460-476 #domain transmembrane #status predicted #label TM09 SUMMARY #length 500 #molecular-weight 53991 #checksum 6777 SEQUENCE /// ENTRY C69797 #type complete TITLE conserved hypothetical protein yesT - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69797 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69797 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-232 ##label KUN !'##cross-references GB:Z99107; GB:AL009126; NID:g2632866; !1PIDN:CAB12521.1; PID:g2633015 !'##experimental_source strain 168 GENETICS !$#gene yesT CLASSIFICATION #superfamily hypothetical protein yesT SUMMARY #length 232 #molecular-weight 25944 #checksum 9853 SEQUENCE /// ENTRY H69797 #type complete TITLE rhamnogalacturonan acetylesterase homolog yesY - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H69797 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69797 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-217 ##label KUN !'##cross-references GB:Z99107; GB:AL009126; NID:g2632866; !1PIDN:CAB12526.1; PID:g2633020 !'##experimental_source strain 168 GENETICS !$#gene yesY CLASSIFICATION #superfamily hypothetical protein yesT SUMMARY #length 217 #molecular-weight 24594 #checksum 7517 SEQUENCE /// ENTRY A70078 #type complete TITLE conserved hypothetical protein yxiM - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A70078 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A70078 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-382 ##label KUN !'##cross-references GB:Z99124; GB:AL009126; NID:g2636442; !1PIDN:CAB15948.1; PID:g2636458 !'##experimental_source strain 168 GENETICS !$#gene yxiM CLASSIFICATION #superfamily hypothetical protein yxiM SUMMARY #length 382 #molecular-weight 41836 #checksum 6590 SEQUENCE /// ENTRY C69798 #type complete TITLE probable membrane protein yetF - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69798 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69798 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-231 ##label KUN !'##cross-references GB:Z99107; GB:AL009126; NID:g2632866; !1PIDN:CAB12533.1; PID:g2633027 !'##experimental_source strain 168 GENETICS !$#gene yetF CLASSIFICATION #superfamily probable membrane protein ycaP SUMMARY #length 231 #molecular-weight 26310 #checksum 6267 SEQUENCE /// ENTRY A69782 #type complete TITLE probable membrane protein ydfS - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A69782 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69782 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-235 ##label KUN !'##cross-references GB:Z99106; GB:Z99107; GB:AL009126; NID:g2632866; !1PID:g2632867; NID:g2632653; PID:g2632854 !'##experimental_source strain 168 GENETICS !$#gene ydfS CLASSIFICATION #superfamily probable membrane protein ycaP KEYWORDS transmembrane protein SUMMARY #length 235 #molecular-weight 27104 #checksum 6356 SEQUENCE /// ENTRY F69856 #type complete TITLE probable membrane protein ykjA - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F69856 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69856 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-243 ##label KUN !'##cross-references GB:Z99110; GB:AL009126; NID:g2633472; !1PIDN:CAB13163.1; PID:g2633660 !'##experimental_source strain 168 GENETICS !$#gene ykjA CLASSIFICATION #superfamily probable membrane protein ycaP KEYWORDS transmembrane protein SUMMARY #length 243 #molecular-weight 27707 #checksum 3511 SEQUENCE /// ENTRY H69781 #type complete TITLE probable membrane protein ydfR - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H69781 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69781 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-225 ##label KUN !'##cross-references GB:Z99106; GB:AL009126; NID:g2632653; !1PIDN:CAB12360.1; PID:g2632853 !'##experimental_source strain 168 GENETICS !$#gene ydfR CLASSIFICATION #superfamily probable membrane protein ycaP KEYWORDS transmembrane protein SUMMARY #length 225 #molecular-weight 25164 #checksum 967 SEQUENCE /// ENTRY A64830 #type complete TITLE probable membrane protein ycaP - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS A64830 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64830 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-230 ##label BLAT !'##cross-references GB:AE000193; GB:U00096; NID:g1787134; !1PIDN:AAC73992.1; PID:g1787135; UWGP:b0906 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ycaP CLASSIFICATION #superfamily probable membrane protein ycaP KEYWORDS transmembrane protein FEATURE !$21-37 #domain transmembrane #status predicted #label TM1\ !$48-64 #domain transmembrane #status predicted #label TM2\ !$72-88 #domain transmembrane #status predicted #label TM3 SUMMARY #length 230 #molecular-weight 26282 #checksum 3470 SEQUENCE /// ENTRY C69825 #type complete TITLE conserved hypothetical protein yhdE - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69825 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69825 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-146 ##label KUN !'##cross-references GB:Z99109; GB:AL009126; NID:g2633260; !1PIDN:CAB12777.1; PID:g2633273 !'##experimental_source strain 168 GENETICS !$#gene yhdE CLASSIFICATION #superfamily hypothetical protein b2531 SUMMARY #length 146 #molecular-weight 16609 #checksum 2066 SEQUENCE /// ENTRY S56403 #type complete TITLE hypothetical 15.6K protein (purA-vacB intergenic region) - Escherichia coli (strain K-12) ALTERNATE_NAMES hypothetical protein o141 ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS S56403; E65228; B31965 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56403 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-141 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97074.1; !1PID:g537019 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65228 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-141 ##label BLAT !'##cross-references GB:AE000490; GB:U00096; NID:g2367356; !1PIDN:AAC77135.1; PID:g1790621; UWGP:b4178 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A31965 !$#authors Wolfe, S.A.; Smith, J.M. !$#journal J. Biol. Chem. (1988) 263:19147-19153 !$#title Nucleotide sequence and analysis of the purA gene encoding !1adenylosuccinate synthetase of Escherichia coli K12. !$#cross-references MUID:89066719; PMID:3058695 !$#accession B31965 !'##molecule_type DNA !'##residues 'V',2-141 ##label WOL !'##cross-references GB:J04199 !'##experimental_source strain K12 GENETICS !$#gene yjeB !$#map_position 95 min !$#start_codon GTG CLASSIFICATION #superfamily hypothetical protein b2531 SUMMARY #length 141 #molecular-weight 15593 #checksum 3829 SEQUENCE /// ENTRY H40605 #type complete TITLE hypothetical protein rrf2 - Desulfovibrio vulgaris ORGANISM #formal_name Desulfovibrio vulgaris DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H40605 REFERENCE A40605 !$#authors Rossi, M.; Pollock, W.B.R.; Reij, M.W.; Keon, R.G.; Fu, R.; !1Voordouw, G. !$#journal J. Bacteriol. (1993) 175:4699-4711 !$#title The hmc operon of Desulfovibrio vulgaris subsp. vulgaris !1Hildenborough encodes a potential transmembrane redox !1protein complex. !$#cross-references MUID:93328674; PMID:8335628 !$#accession H40605 !'##status preliminary !'##molecule_type DNA !'##residues 1-150 ##label ROS !'##cross-references GB:L16784; NID:g290377; PIDN:AAA72001.1; !1PID:g290384 !'##experimental_source subsp. vulgaris GENETICS !$#gene rrf2 CLASSIFICATION #superfamily hypothetical protein b2531 SUMMARY #length 150 #molecular-weight 16681 #checksum 1056 SEQUENCE /// ENTRY S75800 #type complete TITLE hypothetical protein slr0846 - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S75800 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75800 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-157 ##label KAN !'##cross-references EMBL:D64003; GB:AB001339; NID:g1001200; !1PID:g1673323 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily hypothetical protein b2531 SUMMARY #length 157 #molecular-weight 17495 #checksum 2259 SEQUENCE /// ENTRY B65030 #type complete TITLE hypothetical protein b2531 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS B65030 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65030 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-162 ##label BLAT !'##cross-references GB:AE000339; GB:U00096; NID:g1788870; !1PIDN:AAC75584.1; PID:g1788880; UWGP:b2531 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily hypothetical protein b2531 SUMMARY #length 162 #molecular-weight 17336 #checksum 1525 SEQUENCE /// ENTRY C69838 #type complete TITLE nuclease inhibitor homolog yisT - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69838 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69838 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-171 ##label KUN !'##cross-references GB:Z99109; GB:AL009126; NID:g2633260; !1PIDN:CAB12925.1; PID:g2633421 !'##experimental_source strain 168 GENETICS !$#gene yisT CLASSIFICATION #superfamily nuclease inhibitor dinB SUMMARY #length 171 #molecular-weight 19732 #checksum 1619 SEQUENCE /// ENTRY F69615 #type complete TITLE nuclease inhibitor dinB - Bacillus subtilis ALTERNATE_NAMES hypothetical protein (DNA damage-inducible B7 promoter region) ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F69615; C37317 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69615 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-172 ##label KUN !'##cross-references GB:Z99106; GB:Z99107; GB:AL009126; NID:g2632866; !1PID:g2632876; NID:g2632653; PID:g2632863 !'##experimental_source strain 168 REFERENCE A37317 !$#authors Cheo, D.L.; Bayles, K.W.; Yasbin, R.E. !$#journal J. Bacteriol. (1991) 173:1696-1703 !$#title Cloning and characterization of DNA damage-inducible !1promoter regions from Bacillus subtilis. !$#cross-references MUID:91154125; PMID:1847907 !$#accession C37317 !'##status preliminary !'##molecule_type DNA !'##residues 1-28 ##label CHE !'##cross-references GB:M64049; NID:g142844; PIDN:AAA22390.1; !1PID:g142845 GENETICS !$#gene dinB CLASSIFICATION #superfamily nuclease inhibitor dinB SUMMARY #length 172 #molecular-weight 19904 #checksum 964 SEQUENCE /// ENTRY C69888 #type complete TITLE conserved hypothetical protein ynbB - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69888 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69888 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-421 ##label KUN !'##cross-references GB:Z99113; GB:AL009126; NID:g2634090; !1PIDN:CAB13628.1; PID:g2634128 !'##experimental_source strain 168 GENETICS !$#gene ynbB CLASSIFICATION #superfamily hypothetical protein ynbB SUMMARY #length 421 #molecular-weight 46074 #checksum 3540 SEQUENCE /// ENTRY B48947 #type complete TITLE orf306 - Lactobacillus delbrueckii ORGANISM #formal_name Lactobacillus delbrueckii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B48947 REFERENCE A48947 !$#authors Ishino, Y.; Morgenthaler, P.; Hottinger, H.; Soll, D. !$#journal Appl. Environ. Microbiol. (1992) 58:3165-3169 !$#title Organization and nucleotide sequence of the glutamine !1synthetase (glnA) gene from Lactobacillus delbrueckii subsp. !1bulgaricus. !$#cross-references MUID:93073924; PMID:1359838 !$#contents L. d. bulgaricus !$#accession B48947 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-306 ##label ISH !'##experimental_source ATCC 11842 !'##note sequence extracted from NCBI backbone (NCBIP:117806) CLASSIFICATION #superfamily hypothetical protein ynbB SUMMARY #length 306 #molecular-weight 33861 #checksum 3969 SEQUENCE /// ENTRY S75766 #type complete TITLE hypothetical protein slr0580 - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S75766 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75766 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-415 ##label KAN !'##cross-references EMBL:D64003; GB:AB001339; NID:g1001200; !1PID:g1001257 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily hypothetical protein ynbB SUMMARY #length 415 #molecular-weight 44669 #checksum 7076 SEQUENCE /// ENTRY C69895 #type complete TITLE conserved hypothetical protein yoaA - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69895 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69895 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-165 ##label KUN !'##cross-references GB:Z99114; GB:AL009126; NID:g2634230; !1PIDN:CAB13746.1; PID:g2634247 !'##experimental_source strain 168 GENETICS !$#gene yoaA CLASSIFICATION #superfamily Escherichia coli ribosomal-protein-alanine !1N-acetyltransferase rimJ SUMMARY #length 165 #molecular-weight 19037 #checksum 767 SEQUENCE /// ENTRY S00875 #type complete TITLE hypothetical protein P20 - Bacillus licheniformis ORGANISM #formal_name Bacillus licheniformis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S00875 REFERENCE S00875 !$#authors Zhu, Y.F.; Kobayashi, T.; Lampen, J.O. !$#journal Nucleic Acids Res. (1988) 16:5691 !$#title A hypothetical protein (P20), homologous to Tn3 repressor is !1encoded downstream from the bla regulatory region in !1Bacillus licheniformis 749. !$#cross-references MUID:88262575; PMID:2838827 !$#accession S00875 !'##molecule_type mRNA !'##residues 1-178 ##label ZHU !'##cross-references EMBL:X07542; NID:g39572; PIDN:CAA30415.1; !1PID:g39573 CLASSIFICATION #superfamily Escherichia coli ribosomal-protein-alanine !1N-acetyltransferase rimJ SUMMARY #length 178 #molecular-weight 20469 #checksum 9256 SEQUENCE /// ENTRY C69847 #type complete TITLE ribosomal-protein-alanine N-acetyltransfer homolog yjcK - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69847 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69847 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-181 ##label KUN !'##cross-references GB:Z99110; GB:AL009126; NID:g2633472; !1PIDN:CAB13046.1; PID:g2633543 !'##experimental_source strain 168 GENETICS !$#gene yjcK CLASSIFICATION #superfamily Escherichia coli ribosomal-protein-alanine !1N-acetyltransferase rimJ SUMMARY #length 181 #molecular-weight 20925 #checksum 9360 SEQUENCE /// ENTRY H69856 #type complete TITLE N-acetyltransferase homolog ykkB - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H69856 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69856 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-172 ##label KUN !'##cross-references GB:Z99110; GB:AL009126; NID:g2633472; !1PIDN:CAB13165.1; PID:g2633662 !'##experimental_source strain 168 GENETICS !$#gene ykkB CLASSIFICATION #superfamily Escherichia coli ribosomal-protein-alanine !1N-acetyltransferase rimJ SUMMARY #length 172 #molecular-weight 20088 #checksum 1690 SEQUENCE /// ENTRY A69854 #type complete TITLE hypothetical protein yjqA - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A69854 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69854 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-125 ##label KUN !'##cross-references GB:Z99110; GB:AL009126; NID:g2633472; !1PIDN:CAB13104.1; PID:g2633601 !'##experimental_source strain 168 GENETICS !$#gene yjqA CLASSIFICATION #superfamily hypothetical protein yozO SUMMARY #length 125 #molecular-weight 13824 #checksum 4527 SEQUENCE /// ENTRY C69932 #type complete TITLE hypothetical protein yozO - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69932 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69932 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-114 ##label KUN !'##cross-references GB:Z99114; GB:AL009126; NID:g2634230; !1PIDN:CAB13821.1; PID:g2634322 !'##experimental_source strain 168 GENETICS !$#gene yozO CLASSIFICATION #superfamily hypothetical protein yozO SUMMARY #length 114 #molecular-weight 13138 #checksum 344 SEQUENCE /// ENTRY C70009 #type complete TITLE ABC transporter (lipoprotein) homolog yufN - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C70009 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C70009 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-350 ##label KUN !'##cross-references GB:Z99120; GB:AL009126; NID:g2635613; !1PIDN:CAB15143.1; PID:g2635650 !'##experimental_source strain 168 GENETICS !$#gene yufN CLASSIFICATION #superfamily ABC transporter yufN SUMMARY #length 350 #molecular-weight 37349 #checksum 3817 SEQUENCE /// ENTRY H71340 #type complete TITLE membrane lipoprotein TmpC precursor - syphilis spirochete ORGANISM #formal_name Treponema pallidum subsp. pallidum #common_name syphilis spirochete DATE 07-Aug-1998 #sequence_revision 07-Aug-1998 #text_change 23-Jul-1999 ACCESSIONS H71340; A43595; S29561 REFERENCE A71250 !$#authors Fraser, C.M.; Norris, S.J.; Weinstock, G.M.; White, O.; !1Sutton, G.G.; Dodson, R.; Gwinn, M.; Hickey, E.K.; Clayton, !1R.; Ketchum, K.A.; Sodergren, E.; Hardham, J.M.; McLeod, !1M.P.; Salzberg, S.; Peterson, J.; Khalak, H.; Richardson, !1D.; Howell, J.K.; Chidambaram, M.; Utterback, T.; McDonald, !1L.; Artiach, P.; Bowman, C.; Cotton, M.D.; Fujii, C.; !1Garland, S.; Hatch, B.; Horst, K.; Roberts, K.; Watthey, L.; !1Weidman, J.; Smith, H.O.; Venter, J.C. !$#journal Science (1998) 281:375-388 !$#title Complete genome sequence of Treponema pallidum, the syphilis !1spirochete. !$#cross-references MUID:98332770; PMID:9665876 !$#accession H71340 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-353 ##label COL !'##cross-references GB:AE001211; GB:AE000520; NID:g3322582; !1PIDN:AAC65302.1; PID:g3322590 !'##experimental_source strain Nichols REFERENCE A43595 !$#authors Schouls, L.M.; van der Heide, H.G.J.; van Embden, J.D.A. !$#journal Infect. Immun. (1991) 59:3536-3546 !$#title Characterization of the 35-kilodalton Treponema pallidum !1subsp. pallidum recombinant lipoprotein TmpC and antibody !1response to lipidated and nonlipidated Treponema pallidum !1antigens. !$#cross-references MUID:91372962; PMID:1894360 !$#accession A43595 !'##molecule_type DNA !'##residues 1-10,'A',12-158,'R',160-353 ##label SCH !'##cross-references GB:X57836; NID:g48838; PIDN:CAA40968.1; PID:g581809 !'##note this protein is shown to incorporate palmitic acid GENETICS !$#gene tmpC; TP0319 !$#start_codon GTG CLASSIFICATION #superfamily ABC transporter yufN KEYWORDS blocked amino end; lipoprotein; membrane protein; thiolester !1bond FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-353 #product membrane lipoprotein tmpC #status predicted !8#label MAT\ !$21 #modified_site fatty acylated amino end (Cys) (in !8mature form) #status predicted\ !$21 #binding_site sn-2,3-diacylglycerol (Cys) (covalent) !8#status predicted SUMMARY #length 353 #molecular-weight 37769 #checksum 3863 SEQUENCE /// ENTRY C70066 #type complete TITLE conserved hypothetical protein ywpJ - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C70066 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C70066 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-285 ##label KUN !'##cross-references GB:Z99122; GB:AL009126; NID:g2636029; !1PIDN:CAB15646.1; PID:g2636154 !'##experimental_source strain 168 GENETICS !$#gene ywpJ CLASSIFICATION #superfamily hypothetical protein ywpJ SUMMARY #length 285 #molecular-weight 31955 #checksum 5235 SEQUENCE /// ENTRY C70070 #type complete TITLE conserved hypothetical protein ywtE - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C70070 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C70070 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-286 ##label KUN !'##cross-references GB:Z99122; GB:AL009126; NID:g2636029; !1PIDN:CAB15602.1; PID:g2636110 !'##experimental_source strain 168 GENETICS !$#gene ywtE CLASSIFICATION #superfamily hypothetical protein ywpJ SUMMARY #length 286 #molecular-weight 31588 #checksum 9818 SEQUENCE /// ENTRY QQECGB #type complete TITLE hypothetical 29.7K protein, ibpA-gyrB intergenic region - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 30-Sep-1988 #sequence_revision 30-Sep-1997 #text_change 02-Aug-2002 ACCESSIONS B65172; C26444 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65172 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-270 ##label BLAT !'##cross-references GB:AE000446; GB:U00096; NID:g2367261; !1PIDN:AAC76720.1; PID:g2367265; UWGP:b3697 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A93674 !$#authors Adachi, T.; Mizuuchi, M.; Robinson, E.A.; Appella, E.; !1O'Dea, M.H.; Gellert, M.; Mizuuchi, K. !$#journal Nucleic Acids Res. (1987) 15:771-784 !$#title DNA sequence of the E. coli gyrB gene: application of a new !1sequencing strategy. !$#cross-references MUID:87146392; PMID:3029692 !$#accession C26444 !'##molecule_type DNA !'##residues 1-195 ##label ADA !'##cross-references GB:X04341; GB:X00870; NID:g41643; PIDN:CAA27873.1; !1PID:g41648 GENETICS !$#gene yidA !$#map_position 83 min CLASSIFICATION #superfamily hypothetical protein ywpJ SUMMARY #length 270 #molecular-weight 29721 #checksum 7355 SEQUENCE /// ENTRY C36905 #type complete TITLE transcription termination-antitermination factor nusA - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C36905; B69668; S31991 REFERENCE A36905 !$#authors Shazand, K.; Tucker, J.; Grunberg-Manago, M.; Rabinowitz, !1J.C.; Leighton, T. !$#journal J. Bacteriol. (1993) 175:2880-2887 !$#title Similar organization of the nusA-infB operon in Bacillus !1subtilis and Escherichia coli. !$#cross-references MUID:93259931; PMID:8491709 !$#accession C36905 !'##molecule_type DNA !'##residues 1-371 ##label SHA !'##cross-references EMBL:Z18631; NID:g49314; PID:g49316 !'##experimental_source strain 168 !'##note sequence extracted from NCBI backbone (NCBIN:131760, !1NCBIP:131766) REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69668 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-110,'KQ',113-371 ##label KUN !'##cross-references GB:Z99112; GB:AL009126; NID:g2633902; !1PIDN:CAB13533.1; PID:g2634032 !'##experimental_source strain 168 GENETICS !$#gene nusA CLASSIFICATION #superfamily Bacillus transcription termination factor nusA; !1transcription termination factor nusA homology KEYWORDS transcription termination FEATURE !$64-338 #domain transcription termination factor nusA !8homology #label TTN SUMMARY #length 371 #molecular-weight 41712 #checksum 7760 SEQUENCE /// ENTRY S52274 #type complete TITLE transcription termination-antitermination factor nusA - Thermus aquaticus ORGANISM #formal_name Thermus aquaticus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 15-Oct-1999 ACCESSIONS S52274 REFERENCE S52273 !$#authors Vornlocher, H.; Sprinzl, M. !$#submission submitted to the EMBL Data Library, January 1995 !$#description Molecular cloning of the Thermus thermophilus nusA/infB !1operon. !$#accession S52274 !'##status preliminary !'##molecule_type DNA !'##residues 1-387 ##label VOR !'##cross-references EMBL:Z48001; NID:g642362; PID:g642364 !'##note the source is designated as Thermus thermophilus CLASSIFICATION #superfamily Bacillus transcription termination factor nusA; !1transcription termination factor nusA homology KEYWORDS transcription termination FEATURE !$74-349 #domain transcription termination factor nusA !8homology #label TTN SUMMARY #length 387 #molecular-weight 43939 #checksum 6179 SEQUENCE /// ENTRY A69144 #type complete TITLE succinoglycan biosynthesis transport protein - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A69144 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession A69144 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-477 ##label MTH !'##cross-references GB:AE000819; GB:AE000666; NID:g2621396; !1PIDN:AAB84848.1; PID:g2621399 !'##experimental_source strain Delta H GENETICS !$#gene MTH342 CLASSIFICATION #superfamily succinoglycan biosynthesis transport protein SUMMARY #length 477 #molecular-weight 52663 #checksum 3576 SEQUENCE /// ENTRY A69149 #type complete TITLE O-antigen transporter related protein - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A69149 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession A69149 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-475 ##label MTH !'##cross-references GB:AE000823; GB:AE000666; NID:g2621432; !1PIDN:AAB84885.1; PID:g2621440 !'##experimental_source strain Delta H GENETICS !$#gene MTH379 !$#start_codon GTG CLASSIFICATION #superfamily succinoglycan biosynthesis transport protein SUMMARY #length 475 #molecular-weight 51904 #checksum 4296 SEQUENCE /// ENTRY I40487 #type complete TITLE surfactin synthetase / competence protein srfAC - Bacillus subtilis ALTERNATE_NAMES surfactin synthetase srfA3 ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Nov-2000 ACCESSIONS I40487; S46969; D69718; S34987 REFERENCE I40485 !$#authors Cosmina, P.; Rodriguez, F.; de Ferra, F.; Grandi, G.; !1Perego, M.; Venema, G.; van Sinderen, D. !$#journal Mol. Microbiol. (1993) 8:821-831 !$#title Sequence and analysis of the genetic locus responsible for !1surfactin synthesis in Bacillus subtilis. !$#cross-references MUID:93360813; PMID:8355609 !$#accession I40487 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-1274 ##label RES !'##cross-references EMBL:X70356; NID:g396480; PIDN:CAA49818.1; !1PID:g396483 !'##experimental_source ATCC 21332 REFERENCE S46967 !$#authors Fabret, C.; Quentin, Y.; Guiseppi, A.; Busuttil, J.; Haiech, !1J.; Denizot, F. !$#submission submitted to the EMBL Data Library, March 1993 !$#accession S46969 !'##molecule_type DNA !'##residues 1-25,'A',27-32,'S',34-646 ##label FAB !'##cross-references EMBL:X72672; NID:g516358; PID:g516361 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D69718 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-1274 ##label KUN !'##cross-references GB:Z99105; GB:AL009126; NID:g2632457; !1PIDN:CAB12145.1; PID:g2632637 !'##experimental_source strain 168 GENETICS !$#gene srfAC; srfA3 CLASSIFICATION #superfamily peptide synthetase ppsE; acetate-CoA ligase !1homology; acyl carrier protein homology KEYWORDS antibiotic biosynthesis; carrier protein; !1phosphopantetheine; phosphoprotein FEATURE !$510-954 #domain acetate-CoA ligase homology #label ACL1\ !$971-1038 #domain acyl carrier protein homology #label ACP1\ !$1003 #binding_site phosphopantetheine (Ser) (covalent) !8#status predicted SUMMARY #length 1274 #molecular-weight 143816 #checksum 5763 SEQUENCE /// ENTRY E69681 #type complete TITLE peptide synthetase ppsE - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Nov-2000 ACCESSIONS E69681 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69681 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-1279 ##label KUN !'##cross-references GB:Z99113; GB:AL009126; NID:g2634090; !1PIDN:CAB13713.1; PID:g2634213 !'##experimental_source strain 168 GENETICS !$#gene ppsE CLASSIFICATION #superfamily peptide synthetase ppsE; acetate-CoA ligase !1homology; acyl carrier protein homology KEYWORDS carrier protein; phosphopantetheine; phosphoprotein FEATURE !$522-960 #domain acetate-CoA ligase homology #label ACL\ !$978-1046 #domain acyl carrier protein homology #label ACP\ !$1010 #binding_site phosphopantetheine (Ser) (covalent) !8#status predicted SUMMARY #length 1279 #molecular-weight 144618 #checksum 9590 SEQUENCE /// ENTRY D69681 #type complete TITLE peptide synthetase ppsD - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Nov-2000 ACCESSIONS D69681 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D69681 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-3603 ##label KUN !'##cross-references GB:Z99113; GB:AL009126; NID:g2634090; !1PIDN:CAB13714.1; PID:g2634214 !'##experimental_source strain 168 GENETICS !$#gene ppsD CLASSIFICATION #superfamily surfactin synthetase; acetate-CoA ligase !1homology; acyl carrier protein homology KEYWORDS carrier protein; phosphopantetheine; phosphoprotein FEATURE !$509-952 #domain acetate-CoA ligase homology #label ACL1\ !$969-1037 #domain acyl carrier protein homology #label ACP1\ !$1540-1983 #domain acetate-CoA ligase homology #label ACL2\ !$2000-2068 #domain acyl carrier protein homology #label ACP2\ !$2579-3019 #domain acetate-CoA ligase homology #label ACL3\ !$3037-3104 #domain acyl carrier protein homology #label ACP3\ !$1001,2032,3069 #binding_site phosphopantetheine (Ser) (covalent) !8#status predicted SUMMARY #length 3603 #molecular-weight 406807 #checksum 1084 SEQUENCE /// ENTRY D69840 #type complete TITLE conserved hypothetical protein yitK - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69840 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D69840 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-163 ##label KUN !'##cross-references GB:Z99109; GB:AL009126; NID:g2633260; !1PIDN:CAB12942.1; PID:g2633438 !'##experimental_source strain 168 GENETICS !$#gene yitK CLASSIFICATION #superfamily hypothetical protein b0426 SUMMARY #length 163 #molecular-weight 18202 #checksum 3578 SEQUENCE /// ENTRY B64772 #type complete TITLE yajQ protein - Escherichia coli (strain K-12) ALTERNATE_NAMES protein b0426 ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS B64772 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64772 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-169 ##label BLAT !'##cross-references GB:AE000149; GB:U00096; NID:g1786628; !1PIDN:AAC73529.1; PID:g1786629; UWGP:b0426 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yajQ CLASSIFICATION #superfamily hypothetical protein b0426 SUMMARY #length 169 #molecular-weight 19047 #checksum 6695 SEQUENCE /// ENTRY B64330 #type complete TITLE hypothetical protein MJ0241 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B64330 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession B64330 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-145 ##label BUL !'##cross-references GB:U67479; GB:L77117; NID:g1590965; !1PIDN:AAB98229.1; PID:g1499019; TIGR:MJ0241 GENETICS !$#map_position REV232062-231625 CLASSIFICATION #superfamily hypothetical protein MJ0241 SUMMARY #length 145 #molecular-weight 16280 #checksum 9338 SEQUENCE /// ENTRY A64619 #type complete TITLE polypeptide deformylase - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS A64619 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession A64619 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-174 ##label TOM !'##cross-references GB:AE000591; GB:AE000511; NID:g2313918; !1PIDN:AAD07841.1; PID:g2313922; TIGR:HP0793 CLASSIFICATION #superfamily polypeptide deformylase SUMMARY #length 174 #molecular-weight 20057 #checksum 3976 SEQUENCE /// ENTRY D64082 #type complete TITLE N-formylmethionylaminoacyl-tRNA deformylase (EC 3.5.1.27) - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS D64082 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession D64082 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-169 ##label TIGR !'##cross-references GB:U32745; GB:L42023; NID:g1573617; !1PIDN:AAC22282.1; PID:g1573618; TIGR:HI0622 CLASSIFICATION #superfamily polypeptide deformylase KEYWORDS hydrolase SUMMARY #length 169 #molecular-weight 19057 #checksum 7063 SEQUENCE /// ENTRY F69613 #type complete TITLE polypeptide deformylase def - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F69613 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69613 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-160 ##label KUN !'##cross-references GB:Z99112; GB:AL009126; NID:g2633902; !1PIDN:CAB13445.1; PID:g2633944 !'##experimental_source strain 168 GENETICS !$#gene def CLASSIFICATION #superfamily polypeptide deformylase SUMMARY #length 160 #molecular-weight 17775 #checksum 2267 SEQUENCE /// ENTRY S77378 #type complete TITLE polypeptide deformylase def - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein slr1549 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S77378 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S77378 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-187 ##label KAN !'##cross-references EMBL:D90906; GB:AB001339; NID:g1652492; !1PIDN:BAA17481.1; PID:g1652560 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene def CLASSIFICATION #superfamily polypeptide deformylase SUMMARY #length 187 #molecular-weight 21026 #checksum 8228 SEQUENCE /// ENTRY D69862 #type complete TITLE formylmethionine deformylase homolog ykrB - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69862 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D69862 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-184 ##label KUN !'##cross-references GB:Z99111; GB:AL009126; NID:g2633699; !1PIDN:CAB13329.1; PID:g2633827 !'##experimental_source strain 168 GENETICS !$#gene ykrB CLASSIFICATION #superfamily polypeptide deformylase SUMMARY #length 184 #molecular-weight 20655 #checksum 2114 SEQUENCE /// ENTRY G64211 #type complete TITLE formylmethionine deformylase homolog - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 07-Dec-1999 ACCESSIONS G64211 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession G64211 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-226 ##label TIGR !'##cross-references GB:U39690; GB:L43967; NID:g1045782; PID:g1045785; !1TIGR:MG106 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 !$#start_codon GTG CLASSIFICATION #superfamily polypeptide deformylase SUMMARY #length 226 #molecular-weight 26190 #checksum 6241 SEQUENCE /// ENTRY D69868 #type complete TITLE conserved hypothetical protein ykvM - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69868 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D69868 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-165 ##label KUN !'##cross-references GB:Z99111; GB:AL009126; NID:g2633699; !1PIDN:CAB13248.1; PID:g2633746 !'##experimental_source strain 168 GENETICS !$#gene ykvM CLASSIFICATION #superfamily hypothetical protein ykvM SUMMARY #length 165 #molecular-weight 19375 #checksum 1953 SEQUENCE /// ENTRY E64696 #type complete TITLE conserved hypothetical protein HP1413 - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS E64696 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession E64696 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-148 ##label TOM !'##cross-references GB:AE000642; GB:AE000511; NID:g2314587; !1PIDN:AAD08456.1; PID:g2314588; TIGR:HP1413 CLASSIFICATION #superfamily hypothetical protein ykvM SUMMARY #length 148 #molecular-weight 17092 #checksum 8572 SEQUENCE /// ENTRY S77065 #type complete TITLE hypothetical protein slr0711 - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S77065 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S77065 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-137 ##label KAN !'##cross-references EMBL:D64005; GB:AB001339; NID:g1001779; !1PID:g1006604 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily hypothetical protein ykvM SUMMARY #length 137 #molecular-weight 15940 #checksum 4262 SEQUENCE /// ENTRY F65061 #type complete TITLE hypothetical protein b2794 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS F65061 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65061 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-282 ##label BLAT !'##cross-references GB:AE000363; GB:U00096; NID:g1789153; !1PIDN:AAC75836.1; PID:g1789158; UWGP:b2794 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily hypothetical protein ykvM SUMMARY #length 282 #molecular-weight 32587 #checksum 4578 SEQUENCE /// ENTRY S39747 #type complete TITLE ywfN protein - Bacillus subtilis ALTERNATE_NAMES hypothetical protein ipa-92r ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S39747; F70056 REFERENCE S39655 !$#authors Glaser, P.; Kunst, F.; Arnaud, M.; Coudart, M.P.; Gonzales, !1W.; Hullo, M.F.; Ionescu, M.; Lubochinsky, B.; Marcelino, !1L.; Moszer, I.; Presecan, E.; Santana, M.; Schneider, E.; !1Schweizer, J.; Vertes, A.; Rapoport, G.; Danchin, A. !$#journal Mol. Microbiol. (1993) 10:371-384 !$#title Bacillus subtilis genome project: cloning and sequencing of !1the 97 kb region from 325 degrees to 333 degrees. !$#cross-references MUID:95020537; PMID:7934828 !$#accession S39747 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-258 ##label GLA !'##cross-references EMBL:X73124; NID:g413923; PIDN:CAA51648.1; !1PID:g414016 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1993 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F70056 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-258 ##label KUN !'##cross-references GB:Z99123; GB:AL009126; NID:g2636240; !1PIDN:CAB15789.1; PID:g2636298 !'##experimental_source strain 168 GENETICS !$#gene ywfN CLASSIFICATION #superfamily hypothetical protein ylbO SUMMARY #length 258 #molecular-weight 29728 #checksum 7220 SEQUENCE /// ENTRY D69875 #type complete TITLE conserved hypothetical protein ylbO - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69875 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D69875 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-193 ##label KUN !'##cross-references GB:Z99111; GB:AL009126; NID:g2633699; !1PIDN:CAB13382.1; PID:g2633880 !'##experimental_source strain 168 GENETICS !$#gene ylbO CLASSIFICATION #superfamily hypothetical protein ylbO SUMMARY #length 193 #molecular-weight 22366 #checksum 5905 SEQUENCE /// ENTRY E69839 #type complete TITLE conserved hypothetical protein yitD - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-Jan-2003 ACCESSIONS E69839 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69839 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-252 ##label KUN !'##cross-references GB:Z99109; GB:AL009126; NID:g2633260; !1PIDN:CAB12935.1; PID:g2633431 !'##experimental_source strain 168 GENETICS !$#gene yitD CLASSIFICATION #superfamily uncharacterized conserved protein SUMMARY #length 252 #molecular-weight 28357 #checksum 2225 SEQUENCE /// ENTRY G69090 #type complete TITLE conserved hypothetical protein MTH1674 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-Jan-2003 ACCESSIONS G69090 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession G69090 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-258 ##label MTH !'##cross-references GB:AE000925; GB:AE000666; NID:g2622791; !1PIDN:AAB86146.1; PID:g2622803 !'##experimental_source strain Delta H GENETICS !$#gene MTH1674 CLASSIFICATION #superfamily uncharacterized conserved protein SUMMARY #length 258 #molecular-weight 29409 #checksum 7628 SEQUENCE /// ENTRY H64331 #type complete TITLE hypothetical protein MJ0255 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-Jan-2003 ACCESSIONS H64331 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession H64331 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-251 ##label BUL !'##cross-references GB:U67480; GB:L77117; NID:g2826265; !1PIDN:AAB98242.1; PID:g1499034; TIGR:MJ0255 GENETICS !$#map_position REV241359-240604 CLASSIFICATION #superfamily uncharacterized conserved protein SUMMARY #length 251 #molecular-weight 28368 #checksum 8080 SEQUENCE /// ENTRY F64155 #type complete TITLE hypothetical protein HI0624 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS F64155 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession F64155 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-451 ##label TIGR !'##cross-references GB:U32745; GB:L42023; NID:g1573617; !1PIDN:AAC22284.1; PID:g1573620; TIGR:HI0624 !'##note best homolog was a hypothetical protein from Escherichia coli CLASSIFICATION #superfamily hypothetical protein HI0624 SUMMARY #length 451 #molecular-weight 50597 #checksum 361 SEQUENCE /// ENTRY I40649 #type complete TITLE hypothetical protein 265 - Coxiella burnetii ORGANISM #formal_name Coxiella burnetii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS I40649 REFERENCE I40647 !$#authors Suhan, M.; Chen, S.Y.; Thompson, H.A.; Hoover, T.A.; Hill, !1A.; Williams, J.C. !$#journal J. Bacteriol. (1994) 176:5233-5243 !$#title Cloning and characterization of an autonomous replication !1sequence from Coxiella burnetii. !$#cross-references MUID:94350801; PMID:8071197 !$#accession I40649 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-265 ##label RES !'##cross-references EMBL:U10529; NID:g511451; PIDN:AAA56914.1; !1PID:g511454 CLASSIFICATION #superfamily hypothetical protein HI0624 SUMMARY #length 265 #molecular-weight 29863 #checksum 5535 SEQUENCE /// ENTRY E69878 #type complete TITLE RNA-binding Sun protein homolog yloM - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69878 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69878 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-447 ##label KUN !'##cross-references GB:Z99112; GB:AL009126; NID:g2633902; !1PIDN:CAB13447.1; PID:g2633946 !'##experimental_source strain 168 GENETICS !$#gene yloM CLASSIFICATION #superfamily hypothetical protein HI0624 SUMMARY #length 447 #molecular-weight 50274 #checksum 6704 SEQUENCE /// ENTRY S74920 #type complete TITLE fmu protein - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein slr0679 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S74920 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74920 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-446 ##label KAN !'##cross-references EMBL:D90902; GB:AB001339; NID:g1652027; !1PIDN:BAA16960.1; PID:g1652035 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene fmu; fmv CLASSIFICATION #superfamily hypothetical protein HI0624 SUMMARY #length 446 #molecular-weight 49729 #checksum 5821 SEQUENCE /// ENTRY B64303 #type complete TITLE 120K proliferating-cell nucleolar antigen homolog - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B64303 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession B64303 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-274 ##label BUL !'##cross-references GB:U67461; GB:L77117; NID:g1590827; !1PIDN:AAB98007.1; PID:g1592257; TIGR:MJ0026 GENETICS !$#map_position REV27958-27134 !$#start_codon TTG CLASSIFICATION #superfamily hypothetical protein HI0624 SUMMARY #length 274 #molecular-weight 31490 #checksum 2157 SEQUENCE /// ENTRY A69895 #type complete TITLE hypothetical protein ynzG - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A69895 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69895 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-83 ##label KUN !'##cross-references GB:Z99113; GB:AL009126; NID:g2634090; !1PIDN:CAB13633.1; PID:g2634133 !'##experimental_source strain 168 GENETICS !$#gene ynzG CLASSIFICATION #superfamily hypothetical protein yolF SUMMARY #length 83 #molecular-weight 9343 #checksum 3341 SEQUENCE /// ENTRY E69957 #type complete TITLE gamma-D-glutamyl-L-diamino acid endopeptid homolog yqgT - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69957 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69957 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-376 ##label KUN !'##cross-references GB:Z99116; GB:AL009126; NID:g2634723; !1PIDN:CAB14414.1; PID:g2634917 !'##experimental_source strain 168 GENETICS !$#gene yqgT CLASSIFICATION #superfamily endopeptidase I SUMMARY #length 376 #molecular-weight 43439 #checksum 7889 SEQUENCE /// ENTRY S33310 #type complete TITLE endopeptidase I - Bacillus sphaericus ORGANISM #formal_name Bacillus sphaericus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S33310; S31620; S28585 REFERENCE S33310 !$#authors Hourdou, M.L.; Guinand, M.; Vacheron, M.J.; Michel, G.; !1Denoroy, L.; Duez, C.; Englebert, S.; Joris, B.; Weber, G.; !1Ghuysen, J.M. !$#journal Biochem. J. (1993) 292:563-570 !$#title Characterization of the sporulation-related !1gamma-D-glutamyl-(L)meso-diaminopimelic-acid-hydrolysing !1peptidase I of Bacillus sphaericus NCTC 9602 as a member of !1the metallo(zinc) carboxypeptidase A family. Modular design !1of the protein. !$#cross-references MUID:93277526; PMID:8503890 !$#accession S33310 !'##status preliminary !'##molecule_type DNA !'##residues 1-396 ##label HOU !'##cross-references EMBL:X69507; NID:g39895; PIDN:CAA49259.1; !1PID:g580856 REFERENCE S31619 !$#authors Hourdou, M.L.; Joris, B.; Duez, C.; Vacheron, M.J.; Guinand, !1M.; Ghuysen, J.M. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Nucleotide sequence of a Bacillus sphaericus NTCC 9602 gene !1X that encodes a 109 amino acid residue protein having !1similarity with the ribosomal protein S14 of the Euglena !1gracilis chloroplasts. !$#accession S31620 !'##status preliminary !'##molecule_type DNA !'##residues 375-396 ##label HO2 !'##cross-references EMBL:X69895; NID:g40066; PID:g40068 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily endopeptidase I SUMMARY #length 396 #molecular-weight 44724 #checksum 2152 SEQUENCE /// ENTRY E69978 #type complete TITLE conserved hypothetical protein yrpE - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69978 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69978 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-251 ##label KUN !'##cross-references GB:Z99117; GB:AL009126; NID:g2634966; !1PIDN:CAB14624.1; PID:g2635128 !'##experimental_source strain 168 GENETICS !$#gene yrpE CLASSIFICATION #superfamily hypothetical protein yrpE SUMMARY #length 251 #molecular-weight 28869 #checksum 9304 SEQUENCE /// ENTRY A64962 #type complete TITLE conserved hypothetical protein b1973 precursor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS A64962 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64962 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-216 ##label BLAT !'##cross-references GB:AE000288; GB:U00096; NID:g2367124; !1PIDN:AAC75039.1; PID:g1788284; UWGP:b1973 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#start_codon TTG CLASSIFICATION #superfamily hypothetical protein yrpE FEATURE !$1-21 #domain signal sequence #status predicted #label SIG\ !$22-216 #product conserved hypothetical protein b1973 #status !8predicted #label MAT SUMMARY #length 216 #molecular-weight 24762 #checksum 3800 SEQUENCE /// ENTRY E70012 #type complete TITLE conserved hypothetical protein yuiD - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E70012 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E70012 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-158 ##label KUN !'##cross-references GB:Z99120; GB:AL009126; NID:g2635613; !1PIDN:CAB15196.1; PID:g2635703 !'##experimental_source strain 168 GENETICS !$#gene yuiD CLASSIFICATION #superfamily hypothetical protein yuiD SUMMARY #length 158 #molecular-weight 17182 #checksum 6897 SEQUENCE /// ENTRY S75297 #type complete TITLE hypothetical protein slr1394 - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S75297 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75297 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-151 ##label KAN !'##cross-references EMBL:D90904; GB:AB001339; NID:g1652225; !1PIDN:BAA17211.1; PID:g1652288 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily hypothetical protein yuiD SUMMARY #length 151 #molecular-weight 15997 #checksum 9416 SEQUENCE /// ENTRY E70034 #type complete TITLE beta-phosphoglucomutase homolog yvdM - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E70034 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E70034 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-226 ##label KUN !'##cross-references GB:Z99121; GB:AL009126; NID:g2635827; !1PIDN:CAB15460.1; PID:g2635968 !'##experimental_source strain 168 GENETICS !$#gene yvdM CLASSIFICATION #superfamily hypothetical protein b2690 SUMMARY #length 226 #molecular-weight 25101 #checksum 5776 SEQUENCE /// ENTRY H64880 #type complete TITLE probable beta-phosphoglucomutase (EC 5.4.2.6) ycjU - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS H64880 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64880 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-219 ##label BLAT !'##cross-references GB:AE000229; GB:U00096; NID:g1787566; !1PIDN:AAC74399.1; PID:g1787576; UWGP:b1317 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ycjU FUNCTION !$#description isomerase; intramolecular transferase; may catalyze !1reversible isomerization of glucose-6-phosphate and beta !1glucose-1-phosphate !$#pathway starch and sucrose metabolism CLASSIFICATION #superfamily hypothetical protein b2690 KEYWORDS intramolecular transferase; isomerase; transmembrane protein FEATURE !$112-128 #domain transmembrane #status predicted #label TM01\ !$152-168 #domain transmembrane #status predicted #label TM02 SUMMARY #length 219 #molecular-weight 23565 #checksum 3392 SEQUENCE /// ENTRY C65049 #type complete TITLE hypothetical protein b2690 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS C65049 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65049 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-188 ##label BLAT !'##cross-references GB:AE000353; GB:U00096; NID:g1789037; !1PIDN:AAC75737.1; PID:g1789046; UWGP:b2690 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily hypothetical protein b2690 SUMMARY #length 188 #molecular-weight 20780 #checksum 7752 SEQUENCE /// ENTRY D64008 #type complete TITLE hypothetical protein HI0488 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS D64008 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession D64008 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-200 ##label TIGR !'##cross-references GB:U32731; GB:L42023; NID:g3212193; !1PIDN:AAC22147.1; PID:g1573468; TIGR:HI0488 CLASSIFICATION #superfamily hypothetical protein b2690 SUMMARY #length 200 #molecular-weight 22522 #checksum 7962 SEQUENCE /// ENTRY C69824 #type complete TITLE phosphoglycolate phosphatase homolog yhcW - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69824 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69824 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-220 ##label KUN !'##cross-references GB:Z99108; GB:AL009126; NID:g2633055; !1PIDN:CAB12752.1; PID:g2633247 !'##experimental_source strain 168 GENETICS !$#gene yhcW CLASSIFICATION #superfamily hypothetical protein b2690 SUMMARY #length 220 #molecular-weight 24675 #checksum 5867 SEQUENCE /// ENTRY E70044 #type complete TITLE Hpr kinase (EC 2.7.1.-) [validated] - Bacillus subtilis ALTERNATE_NAMES histidine-containing protein kinase; serine protein kinase hprK ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS E70044 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E70044 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-310 ##label KUN !'##cross-references GB:Z99121; GB:AL009126; NID:g2635827; !1PIDN:CAB15505.1; PID:g2636013 !'##experimental_source strain 168 GENETICS !$#gene hprK; yvoB FUNCTION !$#description catalyzes the ATP-dependent phosphorylation of HPr !1(histidine-containing protein ptsH; PIR:WQBSPH) and crh !1(catabolite repression protein crh; PIR:D69607) [validated, !1MUID:98132676] !$#note fructose-1,6-bisphosphate (FBP) was found to be an !1allosteric activator of the hprK catalyzed phosphorylation; !1inorganic phosphate acts as an inhibitor CLASSIFICATION #superfamily hypothetical protein yvoB KEYWORDS ATP; phosphotransferase; serine/threonine-specific protein !1kinase SUMMARY #length 310 #molecular-weight 34702 #checksum 4650 SEQUENCE /// ENTRY S73934 #type complete TITLE MG085 homolog G07_orf312 - Mycoplasma pneumoniae (strain ATCC 29342) ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S73934 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73934 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-312 ##label HIM !'##cross-references EMBL:AE000058; GB:U00089; NID:g1674291; !1PIDN:AAB96256.1; PID:g1674310 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily hypothetical protein yvoB SUMMARY #length 312 #molecular-weight 35234 #checksum 904 SEQUENCE /// ENTRY E70040 #type complete TITLE conserved hypothetical protein yvgP - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E70040 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E70040 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-670 ##label KUN !'##cross-references GB:Z99121; GB:AL009126; NID:g2635827; !1PIDN:CAB15347.1; PID:g2635855 !'##experimental_source strain 168 GENETICS !$#gene yvgP CLASSIFICATION #superfamily hypothetical protein yvgP SUMMARY #length 670 #molecular-weight 75227 #checksum 7758 SEQUENCE /// ENTRY H65214 #type complete TITLE probable Na+/H+ exchanger yjcE - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS H65214 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65214 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-549 ##label BLAT !'##cross-references GB:AE000480; GB:U00096; NID:g2367344; !1PIDN:AAC77035.1; PID:g1790501; UWGP:b4065 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yjcE CLASSIFICATION #superfamily hypothetical protein yvgP SUMMARY #length 549 #molecular-weight 60522 #checksum 9601 SEQUENCE /// ENTRY F69355 #type complete TITLE Na+/H+ antiporter (nhe2) homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F69355 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession F69355 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-494 ##label KLE !'##cross-references GB:AE001046; GB:AE000782; NID:g2689369; !1PIDN:AAB90396.1; PID:g2649761; TIGR:AF0846 CLASSIFICATION #superfamily hypothetical protein yvgP SUMMARY #length 494 #molecular-weight 53710 #checksum 914 SEQUENCE /// ENTRY S75063 #type complete TITLE Na+/H+-exchanging protein slr1727 - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES Na+/H+ exchanger ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S75063 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75063 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-527 ##label KAN !'##cross-references EMBL:D90910; GB:AB001339; NID:g1652956; !1PIDN:BAA17925.1; PID:g1653008 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily hypothetical protein yvgP KEYWORDS ion transport SUMMARY #length 527 #molecular-weight 57538 #checksum 5338 SEQUENCE /// ENTRY S76231 #type complete TITLE Na+/H+-exchanging protein sll0273 - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES Na+/H+ exchanger; protein sll0273 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S76231 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76231 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-540 ##label KAN !'##cross-references EMBL:D90914; GB:AB001339; NID:g1653477; !1PIDN:BAA18490.1; PID:g1653577 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily hypothetical protein yvgP KEYWORDS ion transport SUMMARY #length 540 #molecular-weight 58116 #checksum 8237 SEQUENCE /// ENTRY F55516 #type complete TITLE hydrogenase-2 operon protein hybF - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS F55516; E65085 REFERENCE A55516 !$#authors Menon, N.K.; Chatelus, C.Y.; Dervartanian, M.; Wendt, J.C.; !1Shanmugam, K.T.; Peck Jr., H.D.; Przybyla, A.E. !$#journal J. Bacteriol. (1994) 176:4416-4423 !$#title Cloning, sequencing, and mutational analysis of the hyb !1operon encoding Escherichia coli hydrogenase 2. !$#cross-references MUID:94292472; PMID:8021226 !$#accession F55516 !'##status preliminary !'##molecule_type DNA !'##residues 1-113 ##label MEN !'##cross-references GB:U09177 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65085 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-113 ##label BLAT !'##cross-references GB:AE000382; GB:U00096; NID:g2367182; !1PIDN:AAC76027.1; PID:g1789365; UWGP:b2991 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene hybF; hybE CLASSIFICATION #superfamily hydrogenase accessory protein SUMMARY #length 113 #molecular-weight 12697 #checksum 5936 SEQUENCE /// ENTRY S15197 #type complete TITLE hypA protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS S15197; B65053 REFERENCE S15197 !$#authors Lutz, S.; Jacobi, A.; Schlensog, V.; Boehm, R.; Sawers, G.; !1Boeck, A. !$#journal Mol. Microbiol. (1991) 5:123-135 !$#title Molecular characterization of an operon (hyp) necessary for !1the activity of the three hydrogenase isoenzymes in !1Escherichia coli. !$#cross-references MUID:91194542; PMID:1849603 !$#accession S15197 !'##status preliminary !'##molecule_type DNA !'##residues 1-116 ##label LUT !'##cross-references EMBL:X54543; NID:g41774; PIDN:CAA38412.1; !1PID:g41775 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65053 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-116 ##label BLAT !'##cross-references GB:AE000356; GB:U00096; NID:g2367153; !1PIDN:AAC75768.1; PID:g1789081; UWGP:b2726 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene hypA CLASSIFICATION #superfamily hydrogenase accessory protein SUMMARY #length 116 #molecular-weight 13168 #checksum 9227 SEQUENCE /// ENTRY S32873 #type complete TITLE hypA protein - Rhizobium leguminosarum bv. viciae ORGANISM #formal_name Rhizobium leguminosarum bv. viciae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS S32873 REFERENCE S32873 !$#authors Rey, L.; Murillo, J.; Hernando, Y.; Hidalgo, E.; Cabrera, !1E.; Imperial, J.; Ruiz-Argueeso, T. !$#journal Mol. Microbiol. (1993) 8:471-481 !$#title Molecular analysis of a microaerobically induced operon !1required for hydrogenase synthesis in Rhizobium !1leguminosarum biovar viciae. !$#cross-references MUID:93316844; PMID:8326860 !$#accession S32873 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-113 ##label REY !'##cross-references EMBL:X52974; NID:g1167855; PIDN:CAA37159.1; !1PID:g48732 GENETICS !$#gene hypA CLASSIFICATION #superfamily hydrogenase accessory protein SUMMARY #length 113 #molecular-weight 12447 #checksum 4867 SEQUENCE /// ENTRY C38532 #type complete TITLE hypA protein - Rhodobacter capsulatus ORGANISM #formal_name Rhodobacter capsulatus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C38532; S32949; S21902; S59983 REFERENCE A38532 !$#authors Xu, H.W.; Wall, J.D. !$#journal J. Bacteriol. (1991) 173:2401-2405 !$#title Clustering of genes necessary for hydrogen oxidation in !1Rhodobacter capsulatus. !$#cross-references MUID:91177833; PMID:2007559 !$#accession C38532 !'##status preliminary !'##molecule_type DNA !'##residues 1-113 ##label XUA !'##cross-references EMBL:X61007; NID:g46051; PID:g46052 REFERENCE S32941 !$#authors Colbeau, A.; Richaud, P.; Toussaint, B.; Caballero, F.J.; !1Elster, C.; Delphin, C.; Smith, R.L.; Chabert, J.; Vignais, !1P.M. !$#journal Mol. Microbiol. (1993) 8:15-29 !$#title Organization of the genes necessary for hydrogenase !1expression in Rhodobacter capsulatus. Sequence analysis and !1identification of two hyp regulatory mutants. !$#cross-references MUID:93268090; PMID:8497190 !$#accession S32949 !'##status preliminary !'##molecule_type DNA !'##residues 1-21 ##label COL !'##cross-references EMBL:X61007 GENETICS !$#gene hypA CLASSIFICATION #superfamily hydrogenase accessory protein SUMMARY #length 113 #molecular-weight 12194 #checksum 1747 SEQUENCE /// ENTRY G64326 #type complete TITLE hydrogenase accessory protein - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G64326 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession G64326 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-124 ##label BUL !'##cross-references GB:U67477; GB:L77117; NID:g1590949; !1PIDN:AAB98198.1; PID:g1590952; TIGR:MJ0214 GENETICS !$#map_position FOR204676-205050 CLASSIFICATION #superfamily hydrogenase accessory protein SUMMARY #length 124 #molecular-weight 14058 #checksum 78 SEQUENCE /// ENTRY H64601 #type complete TITLE conserved hypothetical protein HP0656 - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS H64601 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession H64601 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-383 ##label TOM !'##cross-references GB:AE000579; GB:AE000511; NID:g2313778; !1PIDN:AAD07721.1; PID:g2313781; TIGR:HP0656 CLASSIFICATION #superfamily hypothetical protein AF0390 SUMMARY #length 383 #molecular-weight 43423 #checksum 7559 SEQUENCE /// ENTRY F64601 #type complete TITLE conserved hypothetical protein HP0654 - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS F64601 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession F64601 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-360 ##label TOM !'##cross-references GB:AE000579; GB:AE000511; NID:g2313778; !1PIDN:AAD07719.1; PID:g2313779; TIGR:HP0654 CLASSIFICATION #superfamily hypothetical protein AF0390 SUMMARY #length 360 #molecular-weight 41395 #checksum 4323 SEQUENCE /// ENTRY F69209 #type complete TITLE conserved hypothetical protein MTH820 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F69209 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession F69209 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-403 ##label MTH !'##cross-references GB:AE000859; GB:AE000666; NID:g2621902; !1PIDN:AAB85320.1; PID:g2621911 !'##experimental_source strain Delta H GENETICS !$#gene MTH820 !$#start_codon GTG CLASSIFICATION #superfamily hypothetical protein AF0390 SUMMARY #length 403 #molecular-weight 44976 #checksum 665 SEQUENCE /// ENTRY S74675 #type complete TITLE hypothetical protein sll1659 - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S74675 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74675 !'##status preliminary !'##molecule_type DNA !'##residues 1-392 ##label KAN !'##cross-references EMBL:D90901; GB:AB001339; NID:g1651897; !1PIDN:BAA16826.1; PID:g1651900 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily hypothetical protein AF0390 SUMMARY #length 392 #molecular-weight 43331 #checksum 1681 SEQUENCE /// ENTRY F69777 #type complete TITLE conserved hypothetical protein ydeD - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F69777 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69777 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-319 ##label KUN !'##cross-references GB:Z99106; GB:AL009126; NID:g2632653; !1PIDN:CAB12323.1; PID:g2632816 !'##experimental_source strain 168 GENETICS !$#gene ydeD CLASSIFICATION #superfamily hypothetical protein ydeD SUMMARY #length 319 #molecular-weight 35311 #checksum 9135 SEQUENCE /// ENTRY E65167 #type complete TITLE hypothetical 33.1 kD protein in nlpA 5' region - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS E65167 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65167 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-307 ##label BLAT !'##cross-references GB:AE000443; GB:U00096; NID:g2367255; !1PIDN:AAC76683.1; PID:g1790092; UWGP:b3660 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yicL CLASSIFICATION #superfamily hypothetical protein ydeD SUMMARY #length 307 #molecular-weight 33112 #checksum 1495 SEQUENCE /// ENTRY H69798 #type complete TITLE conserved hypothetical protein yetK - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H69798 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69798 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-330 ##label KUN !'##cross-references GB:Z99107; GB:AL009126; NID:g2632866; !1PIDN:CAB12540.1; PID:g2633034 !'##experimental_source strain 168 GENETICS !$#gene yetK CLASSIFICATION #superfamily hypothetical protein ydeD SUMMARY #length 330 #molecular-weight 35758 #checksum 7739 SEQUENCE /// ENTRY F69810 #type complete TITLE conserved hypothetical protein yflH - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F69810 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69810 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-104 ##label KUN !'##cross-references GB:Z99108; GB:AL009126; NID:g2633055; !1PIDN:CAB12597.1; PID:g2633092 !'##experimental_source strain 168 GENETICS !$#gene yflH CLASSIFICATION #superfamily hypothetical protein yflH SUMMARY #length 104 #molecular-weight 12023 #checksum 8221 SEQUENCE /// ENTRY A69886 #type complete TITLE conserved hypothetical protein ymfJ - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A69886 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69886 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-85 ##label KUN !'##cross-references GB:Z99112; GB:AL009126; NID:g2633902; !1PIDN:CAB13561.1; PID:g2634060 !'##experimental_source strain 168 GENETICS !$#gene ymfJ CLASSIFICATION #superfamily hypothetical protein yflH SUMMARY #length 85 #molecular-weight 9648 #checksum 6272 SEQUENCE /// ENTRY F69814 #type complete TITLE fosmidmycin resistance protein homolog yfnC - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS F69814 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69814 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-409 ##label KUN !'##cross-references GB:Z99107; GB:Z99108; GB:AL009126; NID:g2633055; !1PID:g2633056; NID:g2632866; PID:g2633045 !'##experimental_source strain 168 GENETICS !$#gene yfnC CLASSIFICATION #superfamily fosmidmycin resistance protein SUMMARY #length 409 #molecular-weight 43488 #checksum 5270 SEQUENCE /// ENTRY JC5041 #type complete TITLE fosmidomycin resistance protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS JC5041; F64778 REFERENCE JC5041 !$#authors Fujisaki, S.; Ohnuma, S.; Horiuchi, T.; Takahashi, I.; !1Tsukui, S.; Nishimura, Y.; Nishino, T.; Kitabatake, M.; !1Inokuchi, H. !$#journal Gene (1996) 175:83-87 !$#title Cloning of a gene from Escherichia coli that confers !1resistance to fosmidomycin as a consequence of !1amplification. !$#cross-references MUID:97074653; PMID:8917080 !$#accession JC5041 !'##molecule_type DNA !'##residues 1-406 ##label FUJ !'##cross-references DDBJ:D73370; NID:g1019359; PIDN:BAA11120.1; !1PID:g1019360 !'##experimental_source strain DH5alpha REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64778 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-406 ##label BLAT !'##cross-references GB:AE000154; GB:U00096; NID:g1786683; !1PIDN:AAC73581.1; PID:g1786686; UWGP:b0479 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene fsr FUNCTION !$#description confers resistance to fosmidomycin CLASSIFICATION #superfamily fosmidmycin resistance protein KEYWORDS antibiotic resistance; transmembrane protein FEATURE !$104-120 #domain transmembrane #status predicted #label TM1\ !$181-197 #domain transmembrane #status predicted #label TM2\ !$225-241 #domain transmembrane #status predicted #label TM3\ !$267-283 #domain transmembrane #status predicted #label TM4\ !$294-310 #domain transmembrane #status predicted #label TM5\ !$320-336 #domain transmembrane #status predicted #label TM6\ !$358-374 #domain transmembrane #status predicted #label TM7\ !$381-397 #domain transmembrane #status predicted #label TM8 SUMMARY #length 406 #molecular-weight 43305 #checksum 450 SEQUENCE /// ENTRY G70064 #type complete TITLE transporter homolog ywoD - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G70064 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G70064 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-452 ##label KUN !'##cross-references GB:Z99122; GB:AL009126; NID:g2636029; !1PIDN:CAB15665.1; PID:g2636173 !'##experimental_source strain 168 GENETICS !$#gene ywoD CLASSIFICATION #superfamily fosmidmycin resistance protein SUMMARY #length 452 #molecular-weight 48654 #checksum 7655 SEQUENCE /// ENTRY F69846 #type complete TITLE conserved hypothetical protein yjcF - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F69846 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69846 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-140 ##label KUN !'##cross-references GB:Z99110; GB:AL009126; NID:g2633472; !1PIDN:CAB13041.1; PID:g2633538 !'##experimental_source strain 168 GENETICS !$#gene yjcF CLASSIFICATION #superfamily hypothetical protein yjcF SUMMARY #length 140 #molecular-weight 15668 #checksum 2830 SEQUENCE /// ENTRY S65997 #type complete TITLE conserved hypothetical protein yyaT - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S65997; C70086 REFERENCE S65967 !$#authors Ogasawara, N.; Nakai, S.; Yoshikawa, H. !$#journal DNA Res. (1994) 1:1-14 !$#title Systematic sequencing of the 180 kilobase region of the !1Bacillus subtilis chromosome containing the replication !1origin. !$#cross-references MUID:96051385; PMID:7584024 !$#accession S65997 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-148 ##label OGA !'##cross-references EMBL:D26185; NID:g467326; PIDN:BAA05203.1; !1PID:g467357 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1993 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C70086 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-148 ##label KUN !'##cross-references GB:Z99124; GB:AL009126; NID:g2636442; !1PIDN:CAB16109.1; PID:g2636619 !'##experimental_source strain 168 GENETICS !$#gene yyaT CLASSIFICATION #superfamily hypothetical protein yjcF SUMMARY #length 148 #molecular-weight 17003 #checksum 5825 SEQUENCE /// ENTRY F65033 #type complete TITLE hypothetical 20.0 kD protein in purL-dpj intergenic region - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS F65033; S20974 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65033 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-178 ##label BLAT !'##cross-references GB:AE000342; GB:U00096; NID:g1788907; !1PIDN:AAC75612.1; PID:g1788911; UWGP:b2559 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S20973 !$#authors Poulsen, L.K.; Larsen, N.W.; Molin, S.; Andersson, P. !$#journal Mol. Microbiol. (1992) 6:895-905 !$#title Analysis of an Escherichia coli mutant strain resistant to !1the cell-killing function encoded by the gef gene family. !$#cross-references MUID:92292954; PMID:1602968 !$#accession S20974 !'##molecule_type DNA !'##residues 1-165,'G',167-178 ##label POU GENETICS !$#gene yfhC CLASSIFICATION #superfamily hypothetical protein Yaaj SUMMARY #length 178 #molecular-weight 20026 #checksum 8002 SEQUENCE /// ENTRY S11690 #type complete TITLE conserved hypothetical protein yaaJ - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S11690; S66048; B69737 REFERENCE S11690 !$#authors Struck, J.C.R.; Kretschmer-Kazemi Far, R.; Schroeder, W.; !1Hucho, F.; Toschka, H.Y.; Erdmann, V.A. !$#journal Biochim. Biophys. Acta (1990) 1050:80-83 !$#title Characterization of a 17 kDa protein gene upstream from the !1small cytoplasmic RNA gene of Bacillus subtilis. !$#cross-references MUID:91002681; PMID:1698458 !$#accession S11690 !'##status preliminary !'##molecule_type DNA !'##residues 1-161 ##label STR !'##cross-references EMBL:X52144; NID:g40010; PIDN:CAA36389.1; !1PID:g40011 REFERENCE S65967 !$#authors Ogasawara, N.; Nakai, S.; Yoshikawa, H. !$#journal DNA Res. (1994) 1:1-14 !$#title Systematic sequencing of the 180 kilobase region of the !1Bacillus subtilis chromosome containing the replication !1origin. !$#cross-references MUID:96051385; PMID:7584024 !$#accession S66048 !'##status preliminary !'##molecule_type DNA !'##residues 1-161 ##label OGA !'##cross-references EMBL:D26185; NID:g467326; PIDN:BAA05254.1; !1PID:g467408 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69737 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-161 ##label KUN !'##cross-references GB:Z99104; GB:AL009126; NID:g2632267; !1PIDN:CAB11794.1; PID:g2632285 !'##experimental_source strain 168 GENETICS !$#gene yaaJ CLASSIFICATION #superfamily hypothetical protein Yaaj SUMMARY #length 161 #molecular-weight 17751 #checksum 1447 SEQUENCE /// ENTRY S74803 #type complete TITLE hypothetical protein sll1631 - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S74803 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74803 !'##status preliminary !'##molecule_type DNA !'##residues 1-164 ##label KAN !'##cross-references EMBL:D90909; GB:AB001339; NID:g1652844; !1PIDN:BAA17764.1; PID:g1652846 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily hypothetical protein Yaaj SUMMARY #length 164 #molecular-weight 17985 #checksum 9782 SEQUENCE /// ENTRY F69857 #type complete TITLE conserved hypothetical protein yknA - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F69857 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69857 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-156 ##label KUN !'##cross-references GB:Z99110; GB:AL009126; NID:g2633472; !1PIDN:CAB13174.1; PID:g2633671 !'##experimental_source strain 168 GENETICS !$#gene yknA CLASSIFICATION #superfamily hypothetical protein Yaaj SUMMARY #length 156 #molecular-weight 17156 #checksum 4078 SEQUENCE /// ENTRY S74382 #type complete TITLE hypothetical protein sll0051 - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S74382 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74382 !'##status preliminary !'##molecule_type DNA !'##residues 1-159 ##label KAN !'##cross-references EMBL:D64001; GB:AB001339; NID:g1001102; !1PID:g1001158 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily hypothetical protein Yaaj SUMMARY #length 159 #molecular-weight 17799 #checksum 8640 SEQUENCE /// ENTRY B64250 #type complete TITLE osmotically inducible protein osmC homolog - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B64250 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession B64250 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-155 ##label TIGR !'##cross-references GB:U39732; GB:L43967; NID:g3845044; !1PIDN:AAC72474.1; PID:g3845048; TIGR:MG454 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily hypothetical protein yklA SUMMARY #length 155 #molecular-weight 17376 #checksum 8910 SEQUENCE /// ENTRY E64901 #type complete TITLE protein C, osmotically inducible - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS E64901; S17652 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64901 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-143 ##label BLAT !'##cross-references GB:AE000245; GB:U00096; NID:g1787752; !1PIDN:AAC74555.1; PID:g1787757; UWGP:b1482 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S17652 !$#authors Gutierrez, C.; Devedjian, J.C. !$#journal J. Mol. Biol. (1991) 220:959-973 !$#title Osmotic induction of gene osmC expression in Escherichia !1coli K12. !$#cross-references MUID:91350191; PMID:1715407 !$#accession S17652 !'##molecule_type DNA !'##residues 1-138 ##label GUT !'##cross-references EMBL:X57433; NID:g42180; PIDN:CAA40680.1; !1PID:g42181 GENETICS !$#gene osmC CLASSIFICATION #superfamily hypothetical protein yklA SUMMARY #length 143 #molecular-weight 15088 #checksum 402 SEQUENCE /// ENTRY H64614 #type complete TITLE conserved hypothetical protein HP0760 - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS H64614 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession H64614 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-462 ##label TOM !'##cross-references GB:AE000588; GB:AE000511; NID:g2313880; !1PIDN:AAD07808.1; PID:g2313886; TIGR:HP0760 CLASSIFICATION #superfamily hypothetical protein ymdA SUMMARY #length 462 #molecular-weight 52582 #checksum 6288 SEQUENCE /// ENTRY F69884 #type complete TITLE conserved hypothetical protein ymdA - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F69884 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69884 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-520 ##label KUN !'##cross-references GB:Z99112; GB:AL009126; NID:g2633902; !1PIDN:CAB13569.1; PID:g2634068 !'##experimental_source strain 168 GENETICS !$#gene ymdA CLASSIFICATION #superfamily hypothetical protein ymdA SUMMARY #length 520 #molecular-weight 58919 #checksum 9128 SEQUENCE /// ENTRY F70002 #type complete TITLE conserved hypothetical protein ytwI - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F70002 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F70002 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-154 ##label KUN !'##cross-references GB:Z99118; GB:AL009126; NID:g2635200; !1PIDN:CAB14875.1; PID:g2635380 !'##experimental_source strain 168 GENETICS !$#gene ytwI CLASSIFICATION #superfamily hypothetical protein ytwI SUMMARY #length 154 #molecular-weight 16066 #checksum 2085 SEQUENCE /// ENTRY B64020 #type complete TITLE hypothetical protein HI1074 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS B64020 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession B64020 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-150 ##label TIGR !'##cross-references GB:U32787; GB:L42023; NID:g1574619; !1PIDN:AAC22730.1; PID:g1574625; TIGR:HI1074 CLASSIFICATION #superfamily hypothetical protein ytwI SUMMARY #length 150 #molecular-weight 15479 #checksum 2854 SEQUENCE /// ENTRY F70043 #type complete TITLE hypothetical protein yvlD - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS F70043 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F70043 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-119 ##label KUN !'##cross-references GB:Z99121; GB:Z99122; GB:AL009126; NID:g2636029; !1PID:g2636036; NID:g2635827; PID:g2636023 !'##experimental_source strain 168 GENETICS !$#gene yvlD CLASSIFICATION #superfamily hypothetical protein yvlD SUMMARY #length 119 #molecular-weight 12904 #checksum 804 SEQUENCE /// ENTRY S76245 #type complete TITLE hypothetical protein - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S76245 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76245 !'##status preliminary !'##molecule_type DNA !'##residues 1-116 ##label KAN !'##cross-references EMBL:D90914; GB:AB001339; NID:g1653477; !1PIDN:BAA18504.1; PID:g1653591 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily hypothetical protein yvlD SUMMARY #length 116 #molecular-weight 12648 #checksum 1376 SEQUENCE /// ENTRY F70063 #type complete TITLE conserved hypothetical protein ywnC - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F70063 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F70063 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-127 ##label KUN !'##cross-references GB:Z99122; GB:AL009126; NID:g2636029; !1PIDN:CAB15678.1; PID:g2636186 !'##experimental_source strain 168 GENETICS !$#gene ywnC CLASSIFICATION #superfamily hypothetical protein ywnC SUMMARY #length 127 #molecular-weight 13799 #checksum 4347 SEQUENCE /// ENTRY A70064 #type complete TITLE conserved hypothetical protein ywnG - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A70064 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A70064 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-172 ##label KUN !'##cross-references GB:Z99122; GB:AL009126; NID:g2636029; !1PIDN:CAB15674.1; PID:g2636182 !'##experimental_source strain 168 GENETICS !$#gene ywnG CLASSIFICATION #superfamily hypothetical protein ywnC SUMMARY #length 172 #molecular-weight 18464 #checksum 6203 SEQUENCE /// ENTRY F70064 #type complete TITLE isochorismatase homolog ywoC - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F70064 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F70064 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-189 ##label KUN !'##cross-references GB:Z99122; GB:AL009126; NID:g2636029; !1PIDN:CAB15666.1; PID:g2636174 !'##experimental_source strain 168 GENETICS !$#gene ywoC CLASSIFICATION #superfamily hypothetical protein b1011 SUMMARY #length 189 #molecular-weight 21116 #checksum 6664 SEQUENCE /// ENTRY C64949 #type complete TITLE yecD protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS C64949 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64949 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-199 ##label BLAT !'##cross-references GB:AE000280; GB:U00096; NID:g1788163; !1PIDN:AAC74937.1; PID:g1788174; UWGP:b1867 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yecD CLASSIFICATION #superfamily hypothetical protein b1011 SUMMARY #length 199 #molecular-weight 21742 #checksum 1244 SEQUENCE /// ENTRY G69518 #type complete TITLE isochorismatase (entB) homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69518 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession G69518 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-175 ##label KLE !'##cross-references GB:AE000956; GB:AE000782; NID:g2689279; !1PIDN:AAB89104.1; PID:g2648379; TIGR:AF2151 CLASSIFICATION #superfamily hypothetical protein b1011 SUMMARY #length 175 #molecular-weight 20188 #checksum 7039 SEQUENCE /// ENTRY C70008 #type complete TITLE pyrazinamidase/nicotinamidase homolog yueJ - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C70008 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C70008 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-183 ##label KUN !'##cross-references GB:Z99120; GB:AL009126; NID:g2635613; !1PIDN:CAB15164.1; PID:g2635671 !'##experimental_source strain 168 GENETICS !$#gene yueJ CLASSIFICATION #superfamily hypothetical protein b1011 SUMMARY #length 183 #molecular-weight 20523 #checksum 1356 SEQUENCE /// ENTRY A64843 #type complete TITLE hypothetical protein b1011 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS A64843 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64843 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-244 ##label BLAT !'##cross-references GB:AE000202; GB:U00096; NID:g1787233; !1PIDN:AAC74096.1; PID:g1787246; UWGP:b1011 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily hypothetical protein b1011 SUMMARY #length 244 #molecular-weight 26557 #checksum 2773 SEQUENCE /// ENTRY G69592 #type complete TITLE branched-chain amino acid transport azlC - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69592; T44777 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69592 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-254 ##label KUN !'##cross-references GB:Z99117; GB:AL009126; NID:g2634966; !1PIDN:CAB14612.1; PID:g2635116 !'##experimental_source strain 168 REFERENCE Z22837 !$#authors Belitsky, B.R.; Gustafsson, M.C.U.; Sonenshein, A.L.; von !1Wachenfeldt, C. !$#journal J. Bacteriol. (1997) 179:5448-5457 !$#title An lrp-like gene of Bacillus subtilis involved in !1branched-chain amino acid transport. !$#cross-references MUID:97431495; PMID:9287000 !$#accession T44777 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-254 ##label BEL !'##cross-references EMBL:Y11043; NID:g1926275; PIDN:CAA71940.1; !1PID:g1926281 !'##experimental_source strain 1A1 GENETICS !$#gene azlC CLASSIFICATION #superfamily hypothetical protein b2682 SUMMARY #length 254 #molecular-weight 28365 #checksum 5140 SEQUENCE /// ENTRY F64041 #type complete TITLE hypothetical protein HI1738 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS F64041 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession F64041 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-244 ##label TIGR !'##cross-references GB:U32846; GB:L42023; NID:g3212237; !1PIDN:AAC23382.1; PID:g1574596; TIGR:HI1738 CLASSIFICATION #superfamily hypothetical protein b2682 SUMMARY #length 244 #molecular-weight 27360 #checksum 3165 SEQUENCE /// ENTRY C64686 #type complete TITLE conserved hypothetical integral membrane protein HP1331 - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS C64686 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession C64686 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-228 ##label TOM !'##cross-references GB:AE000634; GB:AE000511; NID:g2314489; !1PIDN:AAD08372.1; PID:g2314496; TIGR:HP1331 CLASSIFICATION #superfamily hypothetical protein b2682 SUMMARY #length 228 #molecular-weight 25854 #checksum 2560 SEQUENCE /// ENTRY B69469 #type complete TITLE conserved hypothetical protein AF1755 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69469 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession B69469 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-219 ##label KLE !'##cross-references GB:AE000982; GB:AE000782; NID:g2689305; !1PIDN:AAB89495.1; PID:g2648796; TIGR:AF1755 CLASSIFICATION #superfamily hypothetical protein b2682 SUMMARY #length 219 #molecular-weight 23337 #checksum 2666 SEQUENCE /// ENTRY C65048 #type complete TITLE hypothetical protein b2682 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS C65048 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65048 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-245 ##label BLAT !'##cross-references GB:AE000353; GB:U00096; NID:g1789037; !1PIDN:AAC75729.1; PID:g1789038; UWGP:b2682 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily hypothetical protein b2682 SUMMARY #length 245 #molecular-weight 26107 #checksum 5557 SEQUENCE /// ENTRY G69833 #type complete TITLE conserved hypothetical protein yhjH - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69833 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69833 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-175 ##label KUN !'##cross-references GB:Z99109; GB:AL009126; NID:g2633260; !1PIDN:CAB12891.1; PID:g2633387 !'##experimental_source strain 168 GENETICS !$#gene yhjH CLASSIFICATION #superfamily hypothetical protein yhjH SUMMARY #length 175 #molecular-weight 20423 #checksum 9058 SEQUENCE /// ENTRY S47218 #type complete TITLE conserved hypothetical protein yvmB - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S47218; H70043 REFERENCE S47218 !$#authors Walther, T.; Hofemeister, J. !$#submission submitted to the EMBL Data Library, August 1994 !$#description Transposon Tn917 mutants of Bacillus subtilis involved in !1protein secretion. !$#accession S47218 !'##molecule_type DNA !'##residues 1-169 ##label WAL !'##cross-references EMBL:Z36881; NID:g535051; PID:g535052 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H70043 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-169 ##label KUN !'##cross-references GB:Z99121; GB:Z99122; GB:AL009126; NID:g2636029; !1PID:g2636034; NID:g2635827; PID:g2636021 !'##experimental_source strain 168 GENETICS !$#gene yvmB CLASSIFICATION #superfamily hypothetical protein yhjH SUMMARY #length 169 #molecular-weight 19681 #checksum 7763 SEQUENCE /// ENTRY B70044 #type complete TITLE conserved hypothetical protein yvnA - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS B70044 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B70044 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-157 ##label KUN !'##cross-references GB:Z99121; GB:Z99122; GB:AL009126; NID:g2636029; !1PID:g2636031; NID:g2635827; PID:g2636018 !'##experimental_source strain 168 GENETICS !$#gene yvnA CLASSIFICATION #superfamily hypothetical protein yhjH SUMMARY #length 157 #molecular-weight 18244 #checksum 5757 SEQUENCE /// ENTRY H69804 #type complete TITLE transcription regulator MarR family homolog yfiV - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H69804 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69804 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-160 ##label KUN !'##cross-references GB:Z99108; GB:AL009126; NID:g2633055; !1PIDN:CAB12670.1; PID:g2633165 !'##experimental_source strain 168 GENETICS !$#gene yfiV CLASSIFICATION #superfamily transcription regulator yfiV SUMMARY #length 160 #molecular-weight 18211 #checksum 6771 SEQUENCE /// ENTRY H70021 #type complete TITLE transcription regulator MarR family homolog yusO - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H70021 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H70021 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-155 ##label KUN !'##cross-references GB:Z99120; GB:AL009126; NID:g2635613; !1PIDN:CAB15276.1; PID:g2635783 !'##experimental_source strain 168 GENETICS !$#gene yusO CLASSIFICATION #superfamily transcription regulator yfiV SUMMARY #length 155 #molecular-weight 17400 #checksum 3206 SEQUENCE /// ENTRY D69843 #type complete TITLE conserved hypothetical protein yjbD - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69843 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D69843 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-131 ##label KUN !'##cross-references GB:Z99110; GB:AL009126; NID:g2633472; !1PIDN:CAB13007.1; PID:g2633504 !'##experimental_source strain 168 GENETICS !$#gene yjbD CLASSIFICATION #superfamily hypothetical protein yjbD SUMMARY #length 131 #molecular-weight 15529 #checksum 1591 SEQUENCE /// ENTRY C69958 #type complete TITLE conserved hypothetical protein yqgZ - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69958 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69958 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-126 ##label KUN !'##cross-references GB:Z99116; GB:AL009126; NID:g2634723; !1PIDN:CAB14408.1; PID:g2634911 !'##experimental_source strain 168 GENETICS !$#gene yqgZ CLASSIFICATION #superfamily hypothetical protein yjbD SUMMARY #length 126 #molecular-weight 14824 #checksum 8624 SEQUENCE /// ENTRY A64214 #type complete TITLE hypothetical protein homolog MG127 - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 07-Dec-1999 ACCESSIONS A64214 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession A64214 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-145 ##label TIGR !'##cross-references GB:U39691; GB:L43967; NID:g1045794; PID:g1045807; !1TIGR:MG127 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily hypothetical protein yjbD SUMMARY #length 145 #molecular-weight 16565 #checksum 2477 SEQUENCE /// ENTRY B70021 #type complete TITLE arsenate reductase homolog yusI - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B70021 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B70021 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-118 ##label KUN !'##cross-references GB:Z99120; GB:AL009126; NID:g2635613; !1PIDN:CAB15270.1; PID:g2635777 !'##experimental_source strain 168 GENETICS !$#gene yusI CLASSIFICATION #superfamily hypothetical protein yjbD SUMMARY #length 118 #molecular-weight 13909 #checksum 8011 SEQUENCE /// ENTRY B42959 #type complete TITLE 14K hypothetical protein (5' of dapE) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS B42959; F65022; S26998 REFERENCE A42959 !$#authors Bouvier, J.; Richaud, C.; Higgins, W.; Bogler, O.; Stragier, !1P. !$#journal J. Bacteriol. (1992) 174:5265-5271 !$#title Cloning, characterization, and expression of the dapE gene !1of Escherichia coli. !$#cross-references MUID:92355499; PMID:1644752 !$#accession B42959 !'##status preliminary !'##molecule_type DNA !'##residues 1-118 ##label BOU !'##cross-references EMBL:X57403; NID:g41231; PIDN:CAA40664.1; !1PID:g41233 !'##note sequence extracted from NCBI backbone (NCBIN:110333, !1NCBIP:110335) REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65022 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-118 ##label BLAT !'##cross-references GB:AE000334; GB:U00096; NID:g1788813; !1PIDN:AAC75524.1; PID:g1788815; UWGP:b2471 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yffB !$#map_position 53 min CLASSIFICATION #superfamily hypothetical protein yjbD SUMMARY #length 118 #molecular-weight 13600 #checksum 1171 SEQUENCE /// ENTRY G69843 #type complete TITLE oligoendopeptidase homolog yjbG - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69843 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69843 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-609 ##label KUN !'##cross-references GB:Z99110; GB:AL009126; NID:g2633472; !1PIDN:CAB13011.1; PID:g2633508 !'##experimental_source strain 168 GENETICS !$#gene yjbG CLASSIFICATION #superfamily oligoendopeptidase F SUMMARY #length 609 #molecular-weight 70143 #checksum 3453 SEQUENCE /// ENTRY A55485 #type complete TITLE oligopeptidase (EC 3.4.24.-) pepF [validated] - Lactococcus lactis ALTERNATE_NAMES metalloendopeptidase ORGANISM #formal_name Lactococcus lactis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 18-Aug-2000 ACCESSIONS A55485; S49150 REFERENCE A55485 !$#authors Monnet, V.; Nardi, M.; Chopin, A.; Chopin, M.C.; Gripon, !1J.C. !$#journal J. Biol. Chem. (1994) 269:32070-32076 !$#title Biochemical and genetic characterization of PepF, an !1oligopeptidase from Lactococcus lactis. !$#cross-references MUID:95096044; PMID:7798200 !$#accession A55485 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-601 ##label RES !'##cross-references EMBL:Z32522; NID:g510139; PIDN:CAA83534.1; !1PID:g510140 GENETICS !$#gene pepF FUNCTION !$#description EC 3.4.24.-; oligopeptidase [validated, MUID:95096044]; !1hydrolyzes peptides containing between 7 and 17 amino acids CLASSIFICATION #superfamily oligoendopeptidase F KEYWORDS hydrolase; metalloproteinase SUMMARY #length 601 #molecular-weight 69674 #checksum 3333 SEQUENCE /// ENTRY S62811 #type complete TITLE oligoendopeptidase F - Mycoplasma pneumoniae (strain ATCC 29342) ALTERNATE_NAMES hypothetical protein GT9_orf611 ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S62811; S73960 REFERENCE S62797 !$#authors Hilbert, H.; Himmelreich, R.; Plagens, H.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:628-639 !$#title Sequence analysis of 56 kb from the genome of the bacterium !1Mycoplasma pneumoniae comprising the dnaA region, the atp !1operon and a cluster of ribosomal protein genes. !$#cross-references MUID:96177562; PMID:8604303 !$#accession S62811 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-611 ##label HIL !'##cross-references EMBL:U34795; NID:g1215683; PIDN:AAC43684.1; !1PID:g1215691 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1995 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73960 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-611 ##label HIM !'##cross-references EMBL:AE000061; GB:U00089; NID:g1674336; !1PIDN:AAB96282.1; PID:g1674339 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#gene pepF !$#genetic_code SGC3 CLASSIFICATION #superfamily oligoendopeptidase F SUMMARY #length 611 #molecular-weight 70959 #checksum 6435 SEQUENCE /// ENTRY F64578 #type complete TITLE oligoendopeptidase F - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS F64578 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession F64578 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-578 ##label TOM !'##cross-references GB:AE000561; GB:AE000511; NID:g2313564; !1PIDN:AAD07532.1; PID:g2313574; TIGR:HP0470 CLASSIFICATION #superfamily oligoendopeptidase F SUMMARY #length 578 #molecular-weight 67705 #checksum 261 SEQUENCE /// ENTRY G69847 #type complete TITLE conserved hypothetical protein yjcO - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69847 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69847 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-153 ##label KUN !'##cross-references GB:Z99110; GB:AL009126; NID:g2633472; !1PIDN:CAB13050.1; PID:g2633547 !'##experimental_source strain 168 GENETICS !$#gene yjcO CLASSIFICATION #superfamily hypothetical protein yjcO SUMMARY #length 153 #molecular-weight 18052 #checksum 9476 SEQUENCE /// ENTRY H69945 #type complete TITLE conserved hypothetical protein yqaQ - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H69945 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69945 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-151 ##label KUN !'##cross-references GB:Z99117; GB:AL009126; NID:g2634966; !1PIDN:CAB14563.1; PID:g2635067 !'##experimental_source strain 168 GENETICS !$#gene yqaQ CLASSIFICATION #superfamily hypothetical protein yjcO SUMMARY #length 151 #molecular-weight 17932 #checksum 8063 SEQUENCE /// ENTRY D69727 #type complete TITLE biosynthesis of teichuronic acid tuaB - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69727 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D69727 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-483 ##label KUN !'##cross-references GB:Z99122; GB:AL009126; NID:g2636029; !1PIDN:CAB15577.1; PID:g2636086 !'##experimental_source strain 168 GENETICS !$#gene tuaB CLASSIFICATION #superfamily hypothetical protein b2046 SUMMARY #length 483 #molecular-weight 53720 #checksum 790 SEQUENCE /// ENTRY E64970 #type complete TITLE Lipopolysaccharide biosynthesis protein wzxC - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS E64970 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64970 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-492 ##label BLAT !'##cross-references GB:AE000295; GB:U00096; NID:g1788354; !1PIDN:AAC75107.1; PID:g1788359; UWGP:b2046 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily hypothetical protein b2046 SUMMARY #length 492 #molecular-weight 53692 #checksum 3294 SEQUENCE /// ENTRY S67859 #type complete TITLE GumJ protein - Xanthomonas campestris ORGANISM #formal_name Xanthomonas campestris DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S67859 REFERENCE S67859 !$#authors Pollock, T.J. !$#submission submitted to the EMBL Data Library, March 1995 !$#accession S67859 !'##status preliminary !'##molecule_type DNA !'##residues 1-498 ##label POL !'##cross-references EMBL:U22511; NID:g1172090; PID:g733151 GENETICS !$#gene gumJ !$#start_codon GTG CLASSIFICATION #superfamily hypothetical protein b2046 SUMMARY #length 498 #molecular-weight 53689 #checksum 1102 SEQUENCE /// ENTRY D69782 #type complete TITLE conserved hypothetical protein ydgB - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS D69782 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D69782 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-90 ##label KUN !'##cross-references GB:Z99106; GB:Z99107; GB:AL009126; NID:g2632866; !1PID:g2632870; NID:g2632653; PID:g2632857 !'##experimental_source strain 168 GENETICS !$#gene ydgB CLASSIFICATION #superfamily hypothetical protein ydgB SUMMARY #length 90 #molecular-weight 9462 #checksum 1496 SEQUENCE /// ENTRY C69782 #type complete TITLE conserved hypothetical protein ydgA - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS C69782 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69782 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-80 ##label KUN !'##cross-references GB:Z99106; GB:Z99107; GB:AL009126; NID:g2632866; !1PID:g2632869; NID:g2632653; PID:g2632856 !'##experimental_source strain 168 GENETICS !$#gene ydgA CLASSIFICATION #superfamily hypothetical protein ydgB SUMMARY #length 80 #molecular-weight 8414 #checksum 8709 SEQUENCE /// ENTRY S52149 #type complete TITLE pore protein amsL - Erwinia amylovora ORGANISM #formal_name Erwinia amylovora DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S61902; S52149 REFERENCE S61891 !$#authors Bugert, P.; Geider, K. !$#journal Mol. Microbiol. (1995) 15:917-933 !$#title Molecular analysis of the ams operon required for !1exopolysaccharide synthesis of Erwinia amylovora. !$#cross-references MUID:95319333; PMID:7596293 !$#accession S61902 !'##status preliminary !'##molecule_type DNA !'##residues 1-388 ##label BU2 !'##cross-references EMBL:X77921; NID:g600426; PIDN:CAA54890.1; !1PID:g600439 CLASSIFICATION #superfamily pore protein amsL SUMMARY #length 388 #molecular-weight 43740 #checksum 8146 SEQUENCE /// ENTRY G69773 #type complete TITLE conserved hypothetical protein ydcI - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69773 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69773 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-777 ##label KUN !'##cross-references GB:Z99106; GB:AL009126; NID:g2632653; !1PIDN:CAB12285.1; PID:g2632778 !'##experimental_source strain 168 GENETICS !$#gene ydcI CLASSIFICATION #superfamily hypothetical protein ydcI SUMMARY #length 777 #molecular-weight 88167 #checksum 1168 SEQUENCE /// ENTRY B65136 #type complete TITLE yhgF protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS B65136 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65136 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-740 ##label BLAT !'##cross-references GB:AE000416; GB:U00096; NID:g2367219; !1PIDN:AAC76432.1; PID:g1789811; UWGP:b3407 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yhgF CLASSIFICATION #superfamily hypothetical protein ydcI SUMMARY #length 740 #molecular-weight 81505 #checksum 2034 SEQUENCE /// ENTRY G69776 #type complete TITLE conserved hypothetical protein yddQ - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69776 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69776 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-180 ##label KUN !'##cross-references GB:Z99106; GB:AL009126; NID:g2632653; !1PIDN:CAB12314.1; PID:g2632807 !'##experimental_source strain 168 GENETICS !$#gene yddQ CLASSIFICATION #superfamily hypothetical protein yddQ SUMMARY #length 180 #molecular-weight 19921 #checksum 8329 SEQUENCE /// ENTRY A69973 #type complete TITLE hypothetical protein yrdC - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A69973 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69973 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-187 ##label KUN !'##cross-references GB:Z99117; GB:AL009126; NID:g2634966; !1PIDN:CAB14617.1; PID:g2635121 !'##experimental_source strain 168 GENETICS !$#gene yrdC CLASSIFICATION #superfamily hypothetical protein yddQ SUMMARY #length 187 #molecular-weight 21250 #checksum 7451 SEQUENCE /// ENTRY G69814 #type complete TITLE conserved hypothetical protein yfnD - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69814 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69814 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-311 ##label KUN !'##cross-references GB:Z99107; GB:AL009126; NID:g2632866; !1PIDN:CAB12550.1; PID:g2633044 !'##experimental_source strain 168 GENETICS !$#gene yfnD CLASSIFICATION #superfamily hypothetical protein yfnD SUMMARY #length 311 #molecular-weight 37128 #checksum 6580 SEQUENCE /// ENTRY A69815 #type complete TITLE conserved hypothetical protein yfnF - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A69815 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69815 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-303 ##label KUN !'##cross-references GB:Z99107; GB:AL009126; NID:g2632866; !1PIDN:CAB12548.1; PID:g2633042 !'##experimental_source strain 168 GENETICS !$#gene yfnF CLASSIFICATION #superfamily hypothetical protein yfnD SUMMARY #length 303 #molecular-weight 35026 #checksum 2486 SEQUENCE /// ENTRY G69884 #type complete TITLE conserved hypothetical protein ymdB - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69884 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69884 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-264 ##label KUN !'##cross-references GB:Z99112; GB:AL009126; NID:g2633902; !1PIDN:CAB13570.1; PID:g2634069 !'##experimental_source strain 168 GENETICS !$#gene ymdB CLASSIFICATION #superfamily hypothetical protein ymdB SUMMARY #length 264 #molecular-weight 29288 #checksum 388 SEQUENCE /// ENTRY B64227 #type complete TITLE hypothetical protein MG246 - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B64227 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession B64227 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-281 ##label TIGR !'##cross-references GB:U39703; GB:L43967; NID:g3844835; !1PIDN:AAC71466.1; PID:g1045937; TIGR:MG246 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily hypothetical protein ymdB SUMMARY #length 281 #molecular-weight 31595 #checksum 2281 SEQUENCE /// ENTRY S73813 #type complete TITLE MG246 homolog H91_orf281 - Mycoplasma pneumoniae (strain ATCC 29342) ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S73813 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73813 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-281 ##label HIM !'##cross-references EMBL:AE000047; GB:U00089; NID:g1674162; !1PIDN:AAB96135.1; PID:g1674178 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily hypothetical protein ymdB SUMMARY #length 281 #molecular-weight 31431 #checksum 7572 SEQUENCE /// ENTRY G69951 #type complete TITLE conserved hypothetical protein yqeK - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69951 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69951 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-186 ##label KUN !'##cross-references GB:Z99117; GB:AL009126; NID:g2634966; !1PIDN:CAB14505.1; PID:g2635009 !'##experimental_source strain 168 GENETICS !$#gene yqeK CLASSIFICATION #superfamily hypothetical protein yqeK SUMMARY #length 186 #molecular-weight 21282 #checksum 3970 SEQUENCE /// ENTRY S77144 #type complete TITLE hypothetical protein slr1885 - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S77144 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S77144 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-192 ##label KAN !'##cross-references EMBL:D90908; GB:AB001339; NID:g1652725; !1PIDN:BAA17702.1; PID:g1652783 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily hypothetical protein yqeK SUMMARY #length 192 #molecular-weight 21607 #checksum 1025 SEQUENCE /// ENTRY E64226 #type complete TITLE hypothetical protein homolog MG240 - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 07-Dec-1999 ACCESSIONS E64226 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession E64226 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-292 ##label TIGR !'##cross-references GB:U39702; GB:L43967; NID:g1045928; PID:g1045930; !1TIGR:MG240 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily hypothetical protein yqeK SUMMARY #length 292 #molecular-weight 33550 #checksum 1376 SEQUENCE /// ENTRY S77216 #type complete TITLE hypothetical protein sll1358 - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S77216 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S77216 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-394 ##label KAN !'##cross-references EMBL:D90907; GB:AB001339; NID:g1652618; !1PIDN:BAA17550.1; PID:g1652630 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily conserved hypothetical protein yoaN SUMMARY #length 394 #molecular-weight 43151 #checksum 6019 SEQUENCE /// ENTRY G70062 #type complete TITLE conserved hypothetical protein ywmC - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G70062 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G70062 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-227 ##label KUN !'##cross-references GB:Z99122; GB:AL009126; NID:g2636029; !1PIDN:CAB15691.1; PID:g2636199 !'##experimental_source strain 168 GENETICS !$#gene ywmC CLASSIFICATION #superfamily hypothetical protein ywmC SUMMARY #length 227 #molecular-weight 24542 #checksum 6021 SEQUENCE /// ENTRY H70062 #type complete TITLE conserved hypothetical protein ywmD - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H70062 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H70062 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-224 ##label KUN !'##cross-references GB:Z99122; GB:AL009126; NID:g2636029; !1PIDN:CAB15690.1; PID:g2636198 !'##experimental_source strain 168 GENETICS !$#gene ywmD CLASSIFICATION #superfamily hypothetical protein ywmC SUMMARY #length 224 #molecular-weight 23965 #checksum 7162 SEQUENCE /// ENTRY H69744 #type complete TITLE conserved hypothetical protein ybbP - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS H69744 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69744 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-273 ##label KUN !'##cross-references GB:Z99104; GB:Z99105; GB:AL009126; NID:g2632457; !1PID:g2632460; NID:g2632267; PID:g2632442 !'##experimental_source strain 168 GENETICS !$#gene ybbP CLASSIFICATION #superfamily hypothetical protein ybbP SUMMARY #length 273 #molecular-weight 30574 #checksum 6549 SEQUENCE /// ENTRY S75983 #type complete TITLE hypothetical protein - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S75983 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75983 !'##status preliminary !'##molecule_type DNA !'##residues 1-303 ##label KAN !'##cross-references EMBL:D64006; GB:AB001339; NID:g1001291; !1PID:g1001343 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily hypothetical protein ybbP SUMMARY #length 303 #molecular-weight 33599 #checksum 9908 SEQUENCE /// ENTRY S73914 #type complete TITLE MG105 homolog K04_orf202 - Mycoplasma pneumoniae (strain ATCC 29342) ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S73914 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73914 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-202 ##label HIM !'##cross-references EMBL:AE000057; GB:U00089; NID:g1674279; !1PIDN:AAB96236.1; PID:g1674289 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily hypothetical protein ybbP SUMMARY #length 202 #molecular-weight 22733 #checksum 2918 SEQUENCE /// ENTRY F64211 #type complete TITLE hypothetical protein MG105 - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 07-Dec-1999 ACCESSIONS F64211 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession F64211 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-200 ##label TIGR !'##cross-references GB:U39690; GB:L43967; NID:g1045782; PID:g1045784; !1TIGR:MG105 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily hypothetical protein ybbP SUMMARY #length 200 #molecular-weight 22668 #checksum 7449 SEQUENCE /// ENTRY H69756 #type complete TITLE tellurium resistance protein homolog yceF - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H69756 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69756 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-257 ##label KUN !'##cross-references GB:Z99105; GB:AL009126; NID:g2632457; !1PIDN:CAB12086.1; PID:g2632578 !'##experimental_source strain 168 GENETICS !$#gene yceF CLASSIFICATION #superfamily hypothetical protein sll1022 SUMMARY #length 257 #molecular-weight 29167 #checksum 3438 SEQUENCE /// ENTRY C69861 #type complete TITLE toxic anion resistance protein homolog ykoY - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS C69861 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69861 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-324 ##label KUN !'##cross-references GB:Z99110; GB:Z99111; GB:AL009126; NID:g2633699; !1PID:g2633715; NID:g2633472; PID:g2633698 !'##experimental_source strain 168 GENETICS !$#gene ykoY CLASSIFICATION #superfamily hypothetical protein sll1022 SUMMARY #length 324 #molecular-weight 35532 #checksum 2408 SEQUENCE /// ENTRY S74794 #type complete TITLE hypothetical protein sll1022 - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S74794 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74794 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-242 ##label KAN !'##cross-references EMBL:D90901; GB:AB001339; NID:g1651897; !1PIDN:BAA16945.1; PID:g1652019 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily hypothetical protein sll1022 SUMMARY #length 242 #molecular-weight 26782 #checksum 7526 SEQUENCE /// ENTRY H69772 #type complete TITLE holo-[acyl-carrier-protein] synthase (EC 2.7.8.7) - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H69772 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69772 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-121 ##label KUN !'##cross-references GB:Z99106; GB:AL009126; NID:g2632653; !1PIDN:CAB12269.1; PID:g2632762 !'##experimental_source strain 168 GENETICS !$#gene ydcB CLASSIFICATION #superfamily holo-ACP synthase KEYWORDS coenzyme A; transferase SUMMARY #length 121 #molecular-weight 13718 #checksum 1560 SEQUENCE /// ENTRY B42294 #type complete TITLE holo-[acyl-carrier-protein] synthase (EC 2.7.8.7) - Escherichia coli (strain K-12) ALTERNATE_NAMES dpj protein ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS B42294; B42293; B65034 REFERENCE A42294 !$#authors Lam, H.M.; Tancula, E.; Dempsey, W.B.; Winkler, M.E. !$#journal J. Bacteriol. (1992) 174:1554-1567 !$#title Suppression of insertions in the complex pdxJ operon of !1Escherichia coli K-12 by lon and other mutations. !$#cross-references MUID:92165730; PMID:1537800 !$#accession B42294 !'##status preliminary !'##molecule_type DNA !'##residues 1-126 ##label LAM !'##cross-references GB:M74526; NID:g147136; PIDN:AAA24316.1; !1PID:g147138 REFERENCE A42293 !$#authors Takiff, H.E.; Baker, T.; Copeland, T.; Chen, S.M.; Court, !1D.L. !$#journal J. Bacteriol. (1992) 174:1544-1553 !$#title Locating essential Escherichia coli genes by using mini-Tn10 !1transposons: the pdxJ operon. !$#cross-references MUID:92165729; PMID:1537799 !$#accession B42293 !'##status preliminary !'##molecule_type DNA !'##residues 1-126 ##label TAK !'##cross-references GB:M76470; NID:g147553; PIDN:AAA21846.1; !1PID:g147556 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65034 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-126 ##label BLAT !'##cross-references GB:AE000343; GB:U00096; NID:g2367139; !1PIDN:AAC75616.1; PID:g1788916; UWGP:b2563 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene acpS CLASSIFICATION #superfamily holo-ACP synthase KEYWORDS coenzyme A; transferase SUMMARY #length 126 #molecular-weight 14052 #checksum 4410 SEQUENCE /// ENTRY H64620 #type complete TITLE holo-[acyl-carrier-protein] synthase (EC 2.7.8.7) - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS H64620 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession H64620 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-119 ##label TOM !'##cross-references GB:AE000592; GB:AE000511; NID:g2313929; !1PIDN:AAD07855.1; PID:g2313937; TIGR:HP0808 CLASSIFICATION #superfamily holo-ACP synthase KEYWORDS coenzyme A; transferase SUMMARY #length 119 #molecular-weight 13004 #checksum 8913 SEQUENCE /// ENTRY S73864 #type complete TITLE hypothetical protein H10_orf119 - Mycoplasma pneumoniae (strain ATCC 29342) ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S73864 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73864 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-119 ##label HIM !'##cross-references EMBL:AE000052; GB:U00089; NID:g1674223; !1PIDN:AAB96186.1; PID:g1674234 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily holo-ACP synthase SUMMARY #length 119 #molecular-weight 13774 #checksum 4610 SEQUENCE /// ENTRY G69878 #type complete TITLE conserved hypothetical protein yloO - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69878 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69878 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-254 ##label KUN !'##cross-references GB:Z99112; GB:AL009126; NID:g2633902; !1PIDN:CAB13449.1; PID:g2633948 !'##experimental_source strain 168 GENETICS !$#gene yloO CLASSIFICATION #superfamily conserved hypothetical protein yloO; conserved !1hypothetical protein yloO homology FEATURE !$33-248 #domain conserved hypothetical protein yloO homology !8#label YLOO SUMMARY #length 254 #molecular-weight 27674 #checksum 2164 SEQUENCE /// ENTRY S77113 #type complete TITLE hypothetical protein sll1771 - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S77113 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S77113 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-254 ##label KAN !'##cross-references EMBL:D90908; GB:AB001339; NID:g1652725; !1PIDN:BAA17671.1; PID:g1652752 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily conserved hypothetical protein yloO; conserved !1hypothetical protein yloO homology FEATURE !$40-252 #domain conserved hypothetical protein yloO homology !8#label YLOO SUMMARY #length 254 #molecular-weight 28472 #checksum 4749 SEQUENCE /// ENTRY I64211 #type complete TITLE protein phosphatase 2C homolog - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 07-Dec-1999 ACCESSIONS I64211 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession I64211 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-260 ##label TIGR !'##cross-references GB:U39690; GB:L43967; NID:g1045782; PID:g1045787; !1TIGR:MG108 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily conserved hypothetical protein yloO; conserved !1hypothetical protein yloO homology FEATURE !$38-259 #domain conserved hypothetical protein yloO homology !8#label YLOO SUMMARY #length 260 #molecular-weight 29960 #checksum 4807 SEQUENCE /// ENTRY S74619 #type complete TITLE hypothetical protein sll1033 - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S74619 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74619 !'##status preliminary !'##molecule_type DNA !'##residues 1-668 ##label KAN !'##cross-references EMBL:D90900; GB:AB001339; NID:g1651768; !1PIDN:BAA16771.1; PID:g1651844 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily hypothetical protein sll1033; conserved !1hypothetical protein yloO homology FEATURE !$441-662 #domain conserved hypothetical protein yloO homology !8#label YLOO SUMMARY #length 668 #molecular-weight 73712 #checksum 6656 SEQUENCE /// ENTRY S76521 #type complete TITLE hypothetical protein - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S76521 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76521 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-691 ##label KAN !'##cross-references EMBL:D64002; GB:AB001339; NID:g1001612; !1PID:g1001636 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily conserved hypothetical protein sll1033; !1conserved hypothetical protein yloO homology FEATURE !$297-525 #domain conserved hypothetical protein yloO homology !8#label YLOO SUMMARY #length 691 #molecular-weight 77764 #checksum 774 SEQUENCE /// ENTRY F64226 #type complete TITLE hypothetical protein MG241 - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 07-Dec-1999 ACCESSIONS F64226 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession F64226 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-620 ##label TIGR !'##cross-references GB:U39702; GB:L43967; NID:g1045928; PID:g1045931; !1TIGR:MG241 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily Mycoplasma genitalium hypothetical protein !1MG241 SUMMARY #length 620 #molecular-weight 72875 #checksum 3709 SEQUENCE /// ENTRY S73825 #type complete TITLE hypothetical protein MG241 homolog - Mycoplasma pneumoniae (strain ATCC 29342) ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S73825 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73825 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-621 ##label HIM !'##cross-references EMBL:AE000049; GB:U00089; NID:g1674188; !1PIDN:AAB96147.1; PID:g1674192 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily Mycoplasma genitalium hypothetical protein !1MG241 SUMMARY #length 621 #molecular-weight 72813 #checksum 8324 SEQUENCE /// ENTRY G64226 #type complete TITLE hypothetical protein MG242 - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 07-Dec-1999 ACCESSIONS G64226 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession G64226 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-630 ##label TIGR !'##cross-references GB:U39702; GB:L43967; NID:g1045928; PID:g1045932; !1TIGR:MG242 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily Mycoplasma genitalium hypothetical protein !1MG241 SUMMARY #length 630 #molecular-weight 74234 #checksum 8041 SEQUENCE /// ENTRY S73824 #type complete TITLE hypothetical protein MG242 homolog - Mycoplasma pneumoniae (strain ATCC 29342) ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S73824 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73824 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-632 ##label HIM !'##cross-references EMBL:AE000049; GB:U00089; NID:g1674188; !1PIDN:AAB96146.1; PID:g1674191 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily Mycoplasma genitalium hypothetical protein !1MG241 SUMMARY #length 632 #molecular-weight 74334 #checksum 6670 SEQUENCE /// ENTRY A64224 #type complete TITLE hypothetical protein MG218 - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 07-Dec-1999 ACCESSIONS A64224 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession A64224 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1805 ##label TIGR !'##cross-references GB:U39699; GB:L43967; NID:g1045903; PID:g1045905; !1TIGR:MG218 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily Mycoplasma genitalium hypothetical protein !1MG218 SUMMARY #length 1805 #molecular-weight 216251 #checksum 7540 SEQUENCE /// ENTRY S73852 #type complete TITLE hypothetical protein MG218 homolog F10_orf1818 - Mycoplasma pneumoniae (strain ATCC 29342) ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S73852 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73852 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1818 ##label HIM !'##cross-references EMBL:AE000051; GB:U00089; NID:g1674211; !1PIDN:AAB96174.1; PID:g1674221 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily Mycoplasma genitalium hypothetical protein !1MG218 SUMMARY #length 1818 #molecular-weight 215621 #checksum 9441 SEQUENCE /// ENTRY E64240 #type complete TITLE hypothetical protein MG366 - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 07-Dec-1999 ACCESSIONS E64240 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession E64240 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-667 ##label TIGR !'##cross-references GB:U39721; GB:L43967; NID:g1046072; PID:g1046075; !1TIGR:MG366 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily Mycoplasma genitalium hypothetical protein !1MG366 SUMMARY #length 667 #molecular-weight 78117 #checksum 1383 SEQUENCE /// ENTRY S73624 #type complete TITLE hypothetical protein MG366 homolog G12_orf664 - Mycoplasma pneumoniae (strain ATCC 29342) ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S73624 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73624 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-664 ##label HIM !'##cross-references EMBL:AE000027; GB:U00089; NID:g1673941; !1PIDN:AAB95946.1; PID:g1673969 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily Mycoplasma genitalium hypothetical protein !1MG366 SUMMARY #length 664 #molecular-weight 76769 #checksum 452 SEQUENCE /// ENTRY I64243 #type complete TITLE hypothetical protein MG397 - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 07-Dec-1999 ACCESSIONS I64243 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession I64243 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-566 ##label TIGR !'##cross-references GB:U39725; GB:L43967; NID:g1046106; PID:g1046110; !1TIGR:MG397 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily Mycoplasma genitalium hypothetical protein !1MG397 SUMMARY #length 566 #molecular-weight 67223 #checksum 6446 SEQUENCE /// ENTRY S62851 #type complete TITLE hypothetical protein MG397 homolog D02_orf569 - Mycoplasma pneumoniae (strain ATCC 29342) ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S62851; S73572 REFERENCE S62797 !$#authors Hilbert, H.; Himmelreich, R.; Plagens, H.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:628-639 !$#title Sequence analysis of 56 kb from the genome of the bacterium !1Mycoplasma pneumoniae comprising the dnaA region, the atp !1operon and a cluster of ribosomal protein genes. !$#cross-references MUID:96177562; PMID:8604303 !$#accession S62851 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-569 ##label HIL !'##cross-references EMBL:U43738; NID:g1209757; PIDN:AAC43661.1; !1PID:g1209768 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1995 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73572 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-569 ##label HIM !'##cross-references EMBL:AE000024; GB:U00089; NID:g1673904; !1PIDN:AAB95894.1; PID:g1673914 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily Mycoplasma genitalium hypothetical protein !1MG397 SUMMARY #length 569 #molecular-weight 66339 #checksum 7596 SEQUENCE /// ENTRY D64215 #type complete TITLE conserved hypothetical protein MG139 - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 07-Dec-1999 ACCESSIONS D64215 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession D64215 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-569 ##label TIGR !'##cross-references GB:U39693; GB:L43967; NID:g1045820; PID:g1045821; !1TIGR:MG139 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily conserved hypothetical protein MG139 SUMMARY #length 569 #molecular-weight 64201 #checksum 3233 SEQUENCE /// ENTRY S73881 #type complete TITLE conserved hypothetical protein MG139 homolog A65_orf569 - Mycoplasma pneumoniae (strain ATCC 29342) ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S73881 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73881 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-569 ##label HIM !'##cross-references EMBL:AE000054; GB:U00089; NID:g1674247; !1PIDN:AAB96203.1; PID:g1674253 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily conserved hypothetical protein MG139 SUMMARY #length 569 #molecular-weight 64086 #checksum 6937 SEQUENCE /// ENTRY B69862 #type complete TITLE conserved hypothetical protein ykqC - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69862 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69862 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-555 ##label KUN !'##cross-references GB:Z99111; GB:AL009126; NID:g2633699; !1PIDN:CAB13326.1; PID:g2633824 !'##experimental_source strain 168 GENETICS !$#gene ykqC CLASSIFICATION #superfamily conserved hypothetical protein MG139 SUMMARY #length 555 #molecular-weight 61516 #checksum 6618 SEQUENCE /// ENTRY H69884 #type complete TITLE conserved hypothetical protein ymfA - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H69884 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69884 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-515 ##label KUN !'##cross-references GB:Z99112; GB:AL009126; NID:g2633902; !1PIDN:CAB13551.1; PID:g2634050 !'##experimental_source strain 168 GENETICS !$#gene ymfA CLASSIFICATION #superfamily conserved hypothetical protein MG139 SUMMARY #length 515 #molecular-weight 56840 #checksum 5733 SEQUENCE /// ENTRY S76024 #type complete TITLE conserved hypothetical protein slr0551 - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S76024 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76024 !'##molecule_type DNA !'##residues 1-640 ##label KAN !'##cross-references EMBL:D64006; GB:AB001339; NID:g1001291; !1PID:g1001381 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily conserved hypothetical protein MG139 SUMMARY #length 640 #molecular-weight 70427 #checksum 4335 SEQUENCE /// ENTRY G64246 #type complete TITLE conserved hypothetical protein MG423 - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 07-Dec-1999 ACCESSIONS G64246; T09752; S18693; S18701 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession G64246 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-561 ##label TIGR !'##cross-references GB:U39728; GB:L43967; NID:g1046134; PID:g1046138; !1TIGR:MG423 !'##experimental_source strain G-37 REFERENCE Z16818 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.L.; Nguyen, !1D.T.; Utterback, T.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Venter, J.C. !$#submission submitted to the EMBL Data Library, October 1998 !$#accession T09752 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-561 ##label FRA !'##cross-references EMBL:U39724; NID:g3845008; PID:g3845013 !'##experimental_source strain G37 GENETICS !$#gene MG423 !$#genetic_code SGC3 CLASSIFICATION #superfamily conserved hypothetical protein MG139 SUMMARY #length 561 #molecular-weight 63396 #checksum 1259 SEQUENCE /// ENTRY S73547 #type complete TITLE hypothetical protein MG423 homolog C12_orf561 - Mycoplasma pneumoniae (strain ATCC 29342) ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S73547 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73547 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-561 ##label HIM !'##cross-references EMBL:AE000022; GB:U00089; NID:g1673882; !1PIDN:AAB95869.1; PID:g1673887 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily conserved hypothetical protein MG139 SUMMARY #length 561 #molecular-weight 63358 #checksum 3756 SEQUENCE /// ENTRY H64240 #type complete TITLE hypothetical protein MG369 - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 07-Dec-1999 ACCESSIONS H64240 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession H64240 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-557 ##label TIGR !'##cross-references GB:U39721; GB:L43967; NID:g1046072; PID:g1046078; !1TIGR:MG369 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily Mycoplasma genitalium hypothetical protein !1MG369 SUMMARY #length 557 #molecular-weight 62665 #checksum 8442 SEQUENCE /// ENTRY S73621 #type complete TITLE hypothetical protein MG369 homolog G12_orf558 - Mycoplasma pneumoniae (strain ATCC 29342) ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S73621 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73621 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-558 ##label HIM !'##cross-references EMBL:AE000027; GB:U00089; NID:g1673941; !1PIDN:AAB95943.1; PID:g1673966 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily Mycoplasma genitalium hypothetical protein !1MG369 SUMMARY #length 558 #molecular-weight 62438 #checksum 1222 SEQUENCE /// ENTRY E69879 #type complete TITLE conserved hypothetical protein yloV - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69879 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69879 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-553 ##label KUN !'##cross-references GB:Z99112; GB:AL009126; NID:g2633902; !1PIDN:CAB13457.1; PID:g2633956 !'##experimental_source strain 168 GENETICS !$#gene yloV CLASSIFICATION #superfamily Mycoplasma genitalium hypothetical protein !1MG369 SUMMARY #length 553 #molecular-weight 59497 #checksum 5186 SEQUENCE /// ENTRY A64231 #type complete TITLE hypothetical protein MG281 - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A64231 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession A64231 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-556 ##label TIGR !'##cross-references GB:U39708; GB:L43967; NID:g3844869; !1PIDN:AAC71503.1; PID:g1045977; TIGR:MG281 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily Mycoplasma genitalium hypothetical protein !1MG281 SUMMARY #length 556 #molecular-weight 62163 #checksum 5665 SEQUENCE /// ENTRY S73764 #type complete TITLE hypothetical protein MG281 homolog F11_orf582 - Mycoplasma pneumoniae (strain ATCC 29342) ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S73764 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73764 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-582 ##label HIM !'##cross-references EMBL:AE000043; GB:U00089; NID:g1674122; !1PIDN:AAB96086.1; PID:g1674125 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily Mycoplasma genitalium hypothetical protein !1MG281 SUMMARY #length 582 #molecular-weight 65977 #checksum 233 SEQUENCE /// ENTRY D64249 #type complete TITLE hypothetical protein MG447 - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D64249 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession D64249 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-547 ##label TIGR !'##cross-references GB:U39731; GB:L43967; NID:g3845031; !1PIDN:AAC72467.1; PID:g3845040; TIGR:MG447 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 !$#start_codon GTG CLASSIFICATION #superfamily Mycoplasma genitalium hypothetical protein !1MG447 SUMMARY #length 547 #molecular-weight 62052 #checksum 5269 SEQUENCE /// ENTRY S73507 #type complete TITLE hypothetical protein MG447 homolog K05_orf499 - Mycoplasma pneumoniae (strain ATCC 29342) ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S73507 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73507 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-499 ##label HIM !'##cross-references EMBL:AE000019; GB:U00089; NID:g1673839; !1PIDN:AAB95829.1; PID:g1673844 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily Mycoplasma genitalium hypothetical protein !1MG447 SUMMARY #length 499 #molecular-weight 55777 #checksum 4766 SEQUENCE /// ENTRY C69020 #type complete TITLE ABC transporter Ycf24 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69020 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession C69020 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-410 ##label MTH !'##cross-references GB:AE000884; GB:AE000666; NID:g2622242; !1PIDN:AAB85639.1; PID:g2622255 !'##experimental_source strain Delta H GENETICS !$#gene MTH1150 CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum ABC !1transporter Ycf24 SUMMARY #length 410 #molecular-weight 45250 #checksum 3720 SEQUENCE /// ENTRY E69545 #type complete TITLE conserved hypothetical protein AF2365 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69545 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession E69545 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-369 ##label KLE !'##cross-references GB:AE001113; GB:AE000782; NID:g2689436; !1PIDN:AAB91300.1; PID:g2650732; TIGR:AF2365 CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum ABC !1transporter Ycf24 SUMMARY #length 369 #molecular-weight 41110 #checksum 6659 SEQUENCE /// ENTRY D70019 #type complete TITLE conserved hypothetical protein yurU - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D70019 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D70019 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-465 ##label KUN !'##cross-references GB:Z99120; GB:AL009126; NID:g2635613; !1PIDN:CAB15256.1; PID:g2635763 !'##experimental_source strain 168 GENETICS !$#gene yurU CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum ABC !1transporter Ycf24 SUMMARY #length 465 #molecular-weight 52729 #checksum 8618 SEQUENCE /// ENTRY A71303 #type complete TITLE conserved hypothetical protein TP0612 - syphilis spirochete ORGANISM #formal_name Treponema pallidum subsp. pallidum #common_name syphilis spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS A71303 REFERENCE A71250 !$#authors Fraser, C.M.; Norris, S.J.; Weinstock, G.M.; White, O.; !1Sutton, G.G.; Dodson, R.; Gwinn, M.; Hickey, E.K.; Clayton, !1R.; Ketchum, K.A.; Sodergren, E.; Hardham, J.M.; McLeod, !1M.P.; Salzberg, S.; Peterson, J.; Khalak, H.; Richardson, !1D.; Howell, J.K.; Chidambaram, M.; Utterback, T.; McDonald, !1L.; Artiach, P.; Bowman, C.; Cotton, M.D.; Fujii, C.; !1Garland, S.; Hatch, B.; Horst, K.; Roberts, K.; Watthey, L.; !1Weidman, J.; Smith, H.O.; Venter, J.C. !$#journal Science (1998) 281:375-388 !$#title Complete genome sequence of Treponema pallidum, the syphilis !1spirochete. !$#cross-references MUID:98332770; PMID:9665876 !$#accession A71303 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-479 ##label COL !'##cross-references GB:AE001236; GB:AE000520; NID:g3322906; !1PIDN:AAC65588.1; PID:g3322910 !'##experimental_source strain Nichols GENETICS !$#gene TP0612 CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum ABC !1transporter Ycf24 SUMMARY #length 479 #molecular-weight 54106 #checksum 3686 SEQUENCE /// ENTRY C71011 #type complete TITLE hypothetical protein PH1385 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C71011 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession C71011 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-446 ##label KAW !'##cross-references GB:AP000006; NID:g3236133; PIDN:BAA30491.1; !1PID:g3257808 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1385 CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum ABC !1transporter Ycf24 SUMMARY #length 446 #molecular-weight 50164 #checksum 8263 SEQUENCE /// ENTRY C64484 #type complete TITLE hypothetical protein HI0380 homolog - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C64484 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession C64484 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-230 ##label BUL !'##cross-references GB:U67588; GB:L77117; NID:g2826411; !1PIDN:AAB99481.1; PID:g1592115; TIGR:MJ1476 GENETICS !$#map_position FOR1446823-1447515 !$#start_codon GTG CLASSIFICATION #superfamily conserved hypothetical protein MTH1849 SUMMARY #length 230 #molecular-weight 26279 #checksum 9064 SEQUENCE /// ENTRY C69114 #type complete TITLE conserved hypothetical protein MTH1849 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69114 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession C69114 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-240 ##label MTH !'##cross-references GB:AE000937; GB:AE000666; NID:g2622974; !1PIDN:AAB86315.1; PID:g2622984 !'##experimental_source strain Delta H GENETICS !$#gene MTH1849 CLASSIFICATION #superfamily conserved hypothetical protein MTH1849 SUMMARY #length 240 #molecular-weight 26881 #checksum 5355 SEQUENCE /// ENTRY H69474 #type complete TITLE conserved hypothetical protein AF1801 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H69474 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession H69474 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-226 ##label KLE !'##cross-references GB:AE000978; GB:AE000782; NID:g2689301; !1PIDN:AAB89450.1; PID:g2648747; TIGR:AF1801 CLASSIFICATION #superfamily conserved hypothetical protein MTH1849 SUMMARY #length 226 #molecular-weight 26123 #checksum 6592 SEQUENCE /// ENTRY S76714 #type complete TITLE hypothetical protein - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S76714 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76714 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-240 ##label KAN !'##cross-references EMBL:D64004; GB:AB001339; NID:g1001701; !1PID:g1208490 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily conserved hypothetical protein MTH1849 SUMMARY #length 240 #molecular-weight 26916 #checksum 9723 SEQUENCE /// ENTRY C65030 #type complete TITLE hypothetical protein b2532 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS C65030 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65030 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-246 ##label BLAT !'##cross-references GB:AE000339; GB:U00096; NID:g1788870; !1PIDN:AAC75585.1; PID:g1788881; UWGP:b2532 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily conserved hypothetical protein MTH1849 SUMMARY #length 246 #molecular-weight 27048 #checksum 5778 SEQUENCE /// ENTRY G64150 #type complete TITLE hypothetical protein HI0380 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS G64150 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession G64150 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-241 ##label TIGR !'##cross-references GB:U32722; GB:L42023; NID:g1573348; !1PIDN:AAC22038.1; PID:g1573350; TIGR:HI0380 !'##note best homolog was a hypothetical protein from Escherichia coli CLASSIFICATION #superfamily conserved hypothetical protein MTH1849 SUMMARY #length 241 #molecular-weight 27251 #checksum 1738 SEQUENCE /// ENTRY S56627 #type complete TITLE hypothetical protein o228b - Escherichia coli (strain K-12) ALTERNATE_NAMES hypothetical protein lasT ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS S56627; B65256 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56627 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-228 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97299.1; !1PID:g537243 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65256 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-228 ##label BLAT !'##cross-references GB:AE000510; GB:U00096; NID:g1790858; !1PIDN:AAC77356.1; PID:g1790865; UWGP:b4403 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene lasT CLASSIFICATION #superfamily conserved hypothetical protein MTH1849 SUMMARY #length 228 #molecular-weight 25259 #checksum 1840 SEQUENCE /// ENTRY G69024 #type complete TITLE pheromone shutdown protein TraB - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69024 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession G69024 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-234 ##label MTH !'##cross-references GB:AE000887; GB:AE000666; NID:g2622289; !1PIDN:AAB85672.1; PID:g2622291 !'##experimental_source strain Delta H GENETICS !$#gene MTH1183 !$#start_codon TTG CLASSIFICATION #superfamily pheromone shutdown protein SUMMARY #length 234 #molecular-weight 26751 #checksum 7916 SEQUENCE /// ENTRY G71261 #type complete TITLE probable pheromone shutdown protein (traB) - syphilis spirochete ORGANISM #formal_name Treponema pallidum subsp. pallidum #common_name syphilis spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS G71261 REFERENCE A71250 !$#authors Fraser, C.M.; Norris, S.J.; Weinstock, G.M.; White, O.; !1Sutton, G.G.; Dodson, R.; Gwinn, M.; Hickey, E.K.; Clayton, !1R.; Ketchum, K.A.; Sodergren, E.; Hardham, J.M.; McLeod, !1M.P.; Salzberg, S.; Peterson, J.; Khalak, H.; Richardson, !1D.; Howell, J.K.; Chidambaram, M.; Utterback, T.; McDonald, !1L.; Artiach, P.; Bowman, C.; Cotton, M.D.; Fujii, C.; !1Garland, S.; Hatch, B.; Horst, K.; Roberts, K.; Watthey, L.; !1Weidman, J.; Smith, H.O.; Venter, J.C. !$#journal Science (1998) 281:375-388 !$#title Complete genome sequence of Treponema pallidum, the syphilis !1spirochete. !$#cross-references MUID:98332770; PMID:9665876 !$#accession G71261 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-396 ##label COL !'##cross-references GB:AE001263; GB:AE000520; NID:g3323266; !1PIDN:AAC65908.1; PID:g3323273 !'##experimental_source strain Nichols GENETICS !$#gene TP0953 CLASSIFICATION #superfamily pheromone shutdown protein SUMMARY #length 396 #molecular-weight 43075 #checksum 9517 SEQUENCE /// ENTRY C53309 #type complete TITLE prgY protein - Enterococcus faecalis plasmid pCF10 ALTERNATE_NAMES pheromone responsive gene Y protein ORGANISM #formal_name Enterococcus faecalis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 18-Aug-2000 ACCESSIONS C53309 REFERENCE A53309 !$#authors Ruhfel, R.E.; Manias, D.A.; Dunny, G.M. !$#journal J. Bacteriol. (1993) 175:5253-5259 !$#title Cloning and characterization of a region of the Enterococcus !1faecalis conjugative plasmid, pCF10, encoding a sex !1pheromone-binding function. !$#cross-references MUID:93352432; PMID:8349565 !$#accession C53309 !'##status preliminary !'##molecule_type DNA !'##residues 1-383 ##label RUH !'##cross-references GB:L14285; NID:g309660; PIDN:AAA25555.1; !1PID:g309663 GENETICS !$#gene prgY !$#genome plasmid CLASSIFICATION #superfamily pheromone shutdown protein SUMMARY #length 383 #molecular-weight 43337 #checksum 8633 SEQUENCE /// ENTRY G70151 #type complete TITLE pheromone shutdown protein (traB) homolog - Lyme disease spirochete ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G70151 REFERENCE A70100 !$#authors Fraser, C.M.; Casjens, S.; Huang, W.M.; Sutton, G.G.; !1Clayton, R.; Lathigra, R.; White, O.; Ketchum, K.A.; Dodson, !1R.; Hickey, E.K.; Gwinn, M.; Dougherty, B.; Tomb, J.F.; !1Fleischmann, R.D.; Richardson, D.; Peterson, J.; Kerlavage, !1A.R.; Quackenbush, J.; Salzberg, S.; Hanson, M.; Vugt, R.V.; !1Palmer, N.; Adams, M.D.; Gocayne, J.; Weidman, J.; !1Utterback, T.; Watthey, L.; McDonald, L.; Artiach, P.; !1Bowman, C.; Garland, S.; Fujii, C.; Cotton, M.D.; Horst, K.; !1Roberts, K.; Hatch, B.; Smith, H.O.; Venter, J.C. !$#journal Nature (1997) 390:580-586 !$#title Genomic sequence of a Lyme disease spirochaete, Borrelia !1burgdorferi. !$#cross-references MUID:98065943; PMID:9403685 !$#accession G70151 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-404 ##label KLE !'##cross-references GB:AE001146; GB:AE000783; NID:g2688312; !1PIDN:AAC66783.1; PID:g2688316; TIGR:BB0416 !'##experimental_source strain B31 CLASSIFICATION #superfamily pheromone shutdown protein SUMMARY #length 404 #molecular-weight 45677 #checksum 4647 SEQUENCE /// ENTRY D64470 #type complete TITLE probable pheromone shutdown protein - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D64470 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession D64470 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-397 ##label BUL !'##cross-references GB:U67576; GB:L77117; NID:g2826398; !1PIDN:AAB99373.1; PID:g1592009; TIGR:MJ1365 GENETICS !$#map_position FOR1314715-1315908 CLASSIFICATION #superfamily pheromone shutdown protein SUMMARY #length 397 #molecular-weight 44777 #checksum 5030 SEQUENCE /// ENTRY C69291 #type complete TITLE pheromone shutdown protein (traB) homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69291 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession C69291 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-396 ##label KLE !'##cross-references GB:AE001082; GB:AE000782; NID:g2689405; !1PIDN:AAB90915.1; PID:g2650316; TIGR:AF0331 CLASSIFICATION #superfamily pheromone shutdown protein SUMMARY #length 396 #molecular-weight 44188 #checksum 4349 SEQUENCE /// ENTRY B35177 #type complete TITLE chromate resistance protein A - Alcaligenes eutrophus plasmid pMOL28 ORGANISM #formal_name Alcaligenes eutrophus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B35177 REFERENCE A35177 !$#authors Nies, A.; Nies, D.H.; Silver, S. !$#journal J. Biol. Chem. (1990) 265:5648-5653 !$#title Nucleotide sequence and expression of a plasmid-encoded !1chromate resistance determinant from Alcaligenes eutrophus. !$#cross-references MUID:90202806; PMID:2180932 !$#accession B35177 !'##status preliminary !'##molecule_type DNA !'##residues 1-401 ##label NIE !'##cross-references GB:J05278; NID:g141911; PID:g141913 GENETICS !$#genome plasmid CLASSIFICATION #superfamily chromate resistance protein A SUMMARY #length 401 #molecular-weight 42641 #checksum 2518 SEQUENCE /// ENTRY C56274 #type complete TITLE ChrA homolog SrpC, sulfur-regulated - Synechococcus sp. (strain PCC 7942) plasmid pANL ORGANISM #formal_name Synechococcus sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C56274 REFERENCE A56274 !$#authors Nicholson, M.L.; Laudenbach, D.E. !$#journal J. Bacteriol. (1995) 177:2143-2150 !$#title Genes encoded on a cyanobacterial plasmid are !1transcriptionally regulated by sulfur availability and cysR. !$#cross-references MUID:95238287; PMID:7536734 !$#accession C56274 !'##status preliminary !'##molecule_type DNA !'##residues 1-393 ##label NIC !'##cross-references GB:U20224; NID:g687686; PID:g687689 GENETICS !$#gene srpC !$#genome plasmid CLASSIFICATION #superfamily chromate resistance protein A SUMMARY #length 393 #molecular-weight 41976 #checksum 8456 SEQUENCE /// ENTRY S76745 #type complete TITLE hypothetical protein - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S76745 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76745 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-399 ##label KAN !'##cross-references EMBL:D90916; GB:AB001339; NID:g1653715; !1PIDN:BAA18657.1; PID:g1653746 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily chromate resistance protein A SUMMARY #length 399 #molecular-weight 42916 #checksum 858 SEQUENCE /// ENTRY F64389 #type complete TITLE chromate resistance protein A homolog - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F64389 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession F64389 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-402 ##label BUL !'##cross-references GB:U67518; GB:L77117; NID:g2826312; !1PIDN:AAB98712.1; PID:g1591434; TIGR:MJ0718 GENETICS !$#map_position REV652045-650837 CLASSIFICATION #superfamily chromate resistance protein A SUMMARY #length 402 #molecular-weight 45131 #checksum 984 SEQUENCE /// ENTRY C64423 #type complete TITLE conserved hypothetical protein MJ0987 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C64423 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession C64423 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-116 ##label BUL !'##cross-references GB:U67541; GB:L77117; NID:g2826353; !1PIDN:AAB98989.1; PID:g1591649; TIGR:MJ0987 GENETICS !$#map_position FOR917902-918252 !$#start_codon GTG CLASSIFICATION #superfamily Archaeoglobus fulgidus probable erpK protein SUMMARY #length 116 #molecular-weight 13698 #checksum 2684 SEQUENCE /// ENTRY E69393 #type complete TITLE probable erpK protein - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69393 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession E69393 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-116 ##label KLE !'##cross-references GB:AE001024; GB:AE000782; NID:g2689347; !1PIDN:AAB90093.1; PID:g2649436; TIGR:AF1150 CLASSIFICATION #superfamily Archaeoglobus fulgidus probable erpK protein SUMMARY #length 116 #molecular-weight 13464 #checksum 3986 SEQUENCE /// ENTRY H71166 #type complete TITLE hypothetical protein PH0532 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H71166 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession H71166 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-117 ##label KAW !'##cross-references GB:AP000002; NID:g3236129; PIDN:BAA29621.1; !1PID:g3256938 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0532 CLASSIFICATION #superfamily Archaeoglobus fulgidus probable erpK protein SUMMARY #length 117 #molecular-weight 13316 #checksum 716 SEQUENCE /// ENTRY C69190 #type complete TITLE conserved hypothetical protein MTH678 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69190 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession C69190 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-121 ##label MTH !'##cross-references GB:AE000848; GB:AE000666; NID:g2621761; !1PIDN:AAB85183.1; PID:g2621763 !'##experimental_source strain Delta H GENETICS !$#gene MTH678 CLASSIFICATION #superfamily Archaeoglobus fulgidus probable erpK protein SUMMARY #length 121 #molecular-weight 13863 #checksum 1917 SEQUENCE /// ENTRY S48552 #type complete TITLE hypothetical protein YLR200w - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein L8167.8 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 22-Oct-1999 ACCESSIONS S48552 REFERENCE S48545 !$#authors Pauley, A. !$#submission submitted to the EMBL Data Library, September 1994 !$#description The sequence of S. cerevisiae cosmid 8167. !$#accession S48552 !'##molecule_type DNA !'##residues 1-114 ##label PAU !'##cross-references EMBL:U14913; NID:g544497; PID:g544505; !1GSPDB:GN00012; MIPS:YLR200w GENETICS !$#gene SGD:YKE2; MIPS:YLR200w !'##cross-references SGD:S0004190; MIPS:YLR200w !$#map_position 12R CLASSIFICATION #superfamily Archaeoglobus fulgidus probable erpK protein SUMMARY #length 114 #molecular-weight 13284 #checksum 1406 SEQUENCE /// ENTRY I53651 #type complete TITLE hydrophilic protein - mouse ALTERNATE_NAMES KE2 protein ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS I53651; I67749; JQ1433 REFERENCE JQ1433 !$#authors Ha, H.; Abe, K.; Artzt, K. !$#journal Gene (1991) 107:345-346 !$#title Primary structure of the embryo-expressed gene KE2 from the !1mouse H-2K region. !$#cross-references MUID:92084131; PMID:1748305 !$#accession I53651 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-127 ##label RES !'##cross-references GB:M65255; NID:g198573; PIDN:AAA39368.1; !1PID:g198574 !$#accession I67749 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-127 ##label RE2 !'##cross-references GB:M65256; NID:g198575; PID:g198576 !$#accession JQ1433 !'##molecule_type mRNA !'##residues 1-127 ##label HAH !'##cross-references GB:M65255; NID:g198573; PIDN:AAA39368.1; !1PID:g198574 !'##experimental_source embryo COMMENT This protein is encoded by H-2K region of the major !1histocompatibility complex and is expressed in embryo. GENETICS !$#gene KE2 !$#introns 22/1; 46/1; 87/2 CLASSIFICATION #superfamily Archaeoglobus fulgidus probable erpK protein SUMMARY #length 127 #molecular-weight 14454 #checksum 9281 SEQUENCE /// ENTRY A69000 #type complete TITLE conserved hypothetical protein MTH1 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A69000 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession A69000 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-268 ##label MTH !'##cross-references GB:AE000795; GB:AE000666; NID:g2621036; !1PIDN:AAB84510.1; PID:g2621037 !'##experimental_source strain Delta H GENETICS !$#gene MTH1 CLASSIFICATION #superfamily conserved hypothetical protein MTH1 SUMMARY #length 268 #molecular-weight 30191 #checksum 6508 SEQUENCE /// ENTRY E69490 #type complete TITLE conserved hypothetical protein AF1926 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69490 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession E69490 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-256 ##label KLE !'##cross-references GB:AE000971; GB:AE000782; NID:g2689294; !1PIDN:AAB89330.1; PID:g2648620; TIGR:AF1926 CLASSIFICATION #superfamily conserved hypothetical protein MTH1 SUMMARY #length 256 #molecular-weight 29009 #checksum 3527 SEQUENCE /// ENTRY B71188 #type complete TITLE hypothetical protein PH1779 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B71188 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession B71188 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-258 ##label KAW !'##cross-references GB:AP000007; NID:g3236134; PIDN:BAA30897.1; !1PID:g3258214 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1779 CLASSIFICATION #superfamily conserved hypothetical protein MTH1 SUMMARY #length 258 #molecular-weight 29305 #checksum 7000 SEQUENCE /// ENTRY G69458 #type complete TITLE acetolactate synthase, small subunit homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69458 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession G69458 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-137 ##label KLE !'##cross-references GB:AE000988; GB:AE000782; NID:g2689311; !1PIDN:AAB89585.1; PID:g2648892; TIGR:AF1672 CLASSIFICATION #superfamily conserved hypothetical protein MTH1854 SUMMARY #length 137 #molecular-weight 15201 #checksum 7443 SEQUENCE /// ENTRY A69137 #type complete TITLE hypothetical protein MTH291 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A69137 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession A69137 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-148 ##label MTH !'##cross-references GB:AE000814; GB:AE000666; NID:g2621334; !1PIDN:AAB84797.1; PID:g2621343 !'##experimental_source strain Delta H GENETICS !$#gene MTH291 CLASSIFICATION #superfamily hypothetical protein MTH291 SUMMARY #length 148 #molecular-weight 16982 #checksum 7719 SEQUENCE /// ENTRY H69136 #type complete TITLE hypothetical protein MTH290 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H69136 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession H69136 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-169 ##label MTH !'##cross-references GB:AE000814; GB:AE000666; NID:g2621334; !1PIDN:AAB84796.1; PID:g2621342 !'##experimental_source strain Delta H GENETICS !$#gene MTH290 CLASSIFICATION #superfamily hypothetical protein MTH291 SUMMARY #length 169 #molecular-weight 18481 #checksum 8616 SEQUENCE /// ENTRY S39876 #type complete TITLE gufA protein - Myxococcus xanthus ALTERNATE_NAMES hypothetical protein X ORGANISM #formal_name Myxococcus xanthus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S39876; S33148; S35738 REFERENCE S39875 !$#authors McGowan, S.J.; Gorham, H.C.; Hodgson, D.A. !$#journal Mol. Microbiol. (1993) 10:713-735 !$#title Light-induced carotenogenesis in Myxococcus xanthus: DNA !1sequence analysis of the carR region. !$#cross-references MUID:95020544; PMID:7934835 !$#accession S39876 !'##molecule_type DNA !'##residues 1-254 ##label MCG !'##cross-references EMBL:X71062; NID:g49252; PIDN:CAA50385.1; !1PID:g49253 GENETICS !$#gene gufA CLASSIFICATION #superfamily gufA protein KEYWORDS transmembrane protein SUMMARY #length 254 #molecular-weight 25890 #checksum 3879 SEQUENCE /// ENTRY D70456 #type complete TITLE gufA protein homolog aq_1814 - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D70456 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession D70456 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-243 ##label AQF !'##cross-references GB:AE000757; GB:AE000657; NID:g2984092; !1PIDN:AAC07647.1; PID:g2984109 !'##experimental_source strain VF5 GENETICS !$#gene aq_1814 CLASSIFICATION #superfamily gufA protein SUMMARY #length 243 #molecular-weight 26211 #checksum 1373 SEQUENCE /// ENTRY S22363 #type complete TITLE gufA protein homolog - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS S22363; F65091 REFERENCE S22360 !$#authors Yang, T.P.; Depew, R.E. !$#journal Biochim. Biophys. Acta (1992) 1130:227-228 !$#title Nucleotide sequence of a region duplicated in Escherichia !1coli toc mutants. !$#cross-references MUID:92223101; PMID:1314093 !$#accession S22363 !'##status translation not shown !'##molecule_type DNA !'##residues 1-257 ##label YAN !'##cross-references EMBL:M77129; NID:g146676; PIDN:AAA71878.1; !1PID:g146680 !'##experimental_source strain RED44 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65091 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-257 ##label BLAT !'##cross-references GB:AE000386; GB:U00096; NID:g2367187; !1PIDN:AAC76076.1; PID:g1789419; UWGP:b3040 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ygiE CLASSIFICATION #superfamily gufA protein SUMMARY #length 257 #molecular-weight 26484 #checksum 9360 SEQUENCE /// ENTRY H71107 #type complete TITLE gufA protein homolog - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H71107 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession H71107 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-269 ##label KAW !'##cross-references GB:AP000003; NID:g3236130; PIDN:BAA29722.1; !1PID:g3257039 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0632 CLASSIFICATION #superfamily gufA protein SUMMARY #length 269 #molecular-weight 28994 #checksum 1527 SEQUENCE /// ENTRY C70127 #type complete TITLE gufA protein homolog - Lyme disease spirochete ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C70127 REFERENCE A70100 !$#authors Fraser, C.M.; Casjens, S.; Huang, W.M.; Sutton, G.G.; !1Clayton, R.; Lathigra, R.; White, O.; Ketchum, K.A.; Dodson, !1R.; Hickey, E.K.; Gwinn, M.; Dougherty, B.; Tomb, J.F.; !1Fleischmann, R.D.; Richardson, D.; Peterson, J.; Kerlavage, !1A.R.; Quackenbush, J.; Salzberg, S.; Hanson, M.; Vugt, R.V.; !1Palmer, N.; Adams, M.D.; Gocayne, J.; Weidman, J.; !1Utterback, T.; Watthey, L.; McDonald, L.; Artiach, P.; !1Bowman, C.; Garland, S.; Fujii, C.; Cotton, M.D.; Horst, K.; !1Roberts, K.; Hatch, B.; Smith, H.O.; Venter, J.C. !$#journal Nature (1997) 390:580-586 !$#title Genomic sequence of a Lyme disease spirochaete, Borrelia !1burgdorferi. !$#cross-references MUID:98065943; PMID:9403685 !$#accession C70127 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-273 ##label KLE !'##cross-references GB:AE001132; GB:AE000783; NID:g2688107; !1PIDN:AAC66605.1; PID:g2688111; TIGR:BB0219 !'##experimental_source strain B31 CLASSIFICATION #superfamily gufA protein SUMMARY #length 273 #molecular-weight 29549 #checksum 4812 SEQUENCE /// ENTRY A69162 #type complete TITLE gufA protein homolog MTH473 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A69162 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession A69162 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-259 ##label MTH !'##cross-references GB:AE000831; GB:AE000666; NID:g2621533; !1PIDN:AAB84979.1; PID:g2621542 !'##experimental_source strain Delta H GENETICS !$#gene MTH473 CLASSIFICATION #superfamily gufA protein SUMMARY #length 259 #molecular-weight 26747 #checksum 1665 SEQUENCE /// ENTRY A69169 #type complete TITLE hypothetical protein MTH523 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A69169 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession A69169 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-185 ##label MTH !'##cross-references GB:AE000835; GB:AE000666; NID:g2621586; !1PIDN:AAB85029.1; PID:g2621596 !'##experimental_source strain Delta H GENETICS !$#gene MTH523 !$#start_codon TTG CLASSIFICATION #superfamily hypothetical protein MTH523 SUMMARY #length 185 #molecular-weight 20574 #checksum 4888 SEQUENCE /// ENTRY E69138 #type complete TITLE hypothetical protein MTH301 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69138 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession E69138 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-172 ##label MTH !'##cross-references GB:AE000815; GB:AE000666; NID:g2621345; !1PIDN:AAB84807.1; PID:g2621354 !'##experimental_source strain Delta H GENETICS !$#gene MTH301 CLASSIFICATION #superfamily hypothetical protein MTH523 SUMMARY #length 172 #molecular-weight 18862 #checksum 3275 SEQUENCE /// ENTRY A69204 #type complete TITLE hypothetical protein MTH778 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A69204 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession A69204 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-372 ##label MTH !'##cross-references GB:AE000856; GB:AE000666; NID:g2621862; !1PIDN:AAB85281.1; PID:g2621869 !'##experimental_source strain Delta H GENETICS !$#gene MTH778 CLASSIFICATION #superfamily hypothetical protein MTH778 SUMMARY #length 372 #molecular-weight 41254 #checksum 2797 SEQUENCE /// ENTRY D69005 #type complete TITLE hypothetical protein MTH1037 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69005 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession D69005 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-361 ##label MTH !'##cross-references GB:AE000876; GB:AE000666; NID:g2622140; !1PIDN:AAB85533.1; PID:g2622141 !'##experimental_source strain Delta H GENETICS !$#gene MTH1037 CLASSIFICATION #superfamily hypothetical protein MTH778 SUMMARY #length 361 #molecular-weight 39939 #checksum 7792 SEQUENCE /// ENTRY F69524 #type complete TITLE conserved hypothetical protein AF2198 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F69524 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession F69524 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-121 ##label KLE !'##cross-references GB:AE000954; GB:AE000782; NID:g2689277; !1PIDN:AAB89058.1; PID:g2648331; TIGR:AF2198 CLASSIFICATION #superfamily hypothetical protein MTH971 SUMMARY #length 121 #molecular-weight 13617 #checksum 3938 SEQUENCE /// ENTRY D71156 #type complete TITLE hypothetical protein PH0451 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D71156 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession D71156 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-122 ##label KAW !'##cross-references GB:AP000002; NID:g3236129; PIDN:BAA29537.1; !1PID:g3256854 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0451 CLASSIFICATION #superfamily hypothetical protein MTH971 SUMMARY #length 122 #molecular-weight 14031 #checksum 1187 SEQUENCE /// ENTRY A69230 #type complete TITLE hypothetical protein MTH971 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A69230 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession A69230 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-144 ##label MTH !'##cross-references GB:AE000871; GB:AE000666; NID:g2622069; !1PIDN:AAB85467.1; PID:g2622070 !'##experimental_source strain Delta H GENETICS !$#gene MTH971 !$#start_codon GTG CLASSIFICATION #superfamily hypothetical protein MTH971 SUMMARY #length 144 #molecular-weight 15747 #checksum 5076 SEQUENCE /// ENTRY F65230 #type complete TITLE probable PTS system enzyme IIA component [imported] - Escherichia coli (strain K-12) ALTERNATE_NAMES hypothetical protein o158 ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS F65230; S56420 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65230 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-154 ##label BLAT !'##cross-references GB:AE000491; GB:U00096; NID:g2367357; !1PIDN:AAC77152.1; PID:g2367359; UWGP:b4195 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56420 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-152,'GSLRRN' ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97091.1; !1PID:g537036 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 GENETICS !$#gene ptxA CLASSIFICATION #superfamily probable phosphotransferase protein yjfU; !1phosphotransferase system mannitol-specific enzyme II factor !1III homology FEATURE !$21-148 #domain phosphotransferase system mannitol-specific !8enzyme II factor III homology #label PT3M SUMMARY #length 154 #molecular-weight 17237 #checksum 916 SEQUENCE /// ENTRY H65243 #type complete TITLE yjhL protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS H65243; S56527 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65243 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-143 ##label BLAT !'##cross-references GB:AE000500; GB:U00096; NID:g2367369; !1PIDN:AAC77258.1; PID:g1790755; UWGP:b4302 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56527 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-69,'GKL' ##label BUR !'##cross-references EMBL:U14003 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 GENETICS !$#gene yjhL CLASSIFICATION #superfamily probable phosphotransferase protein yjfU; !1phosphotransferase system mannitol-specific enzyme II factor !1III homology FEATURE !$16-142 #domain phosphotransferase system mannitol-specific !8enzyme II factor III homology #label PT3M SUMMARY #length 143 #molecular-weight 15638 #checksum 5893 SEQUENCE /// ENTRY S36122 #type complete TITLE phosphotransferase system enzyme II (EC 2.7.1.69) factor III, mannitol-specific - Escherichia coli (strain K-12) ALTERNATE_NAMES protein-Npi-phosphohistidine-sugar phosphotransferase ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS S36122; E65078; S34369 REFERENCE S36122 !$#authors Sprenger, G.A. !$#journal Biochim. Biophys. Acta (1993) 1158:103-106 !$#title Two open reading frames adjacent to the Escherichia coli !1K-12 transketolase (tkt) gene show high similarity to the !1mannitol phosphotransferase system enzymes from Escherichia !1coli and various Gram-positive bacteria. !$#cross-references MUID:93357262; PMID:8353127 !$#accession S36122 !'##status preliminary !'##molecule_type DNA !'##residues 1-147 ##label SPR !'##cross-references EMBL:X72677; NID:g312761; PIDN:CAA51228.1; !1PID:g312762 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65078 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-147 ##label BLAT !'##cross-references GB:AE000376; GB:U00096; NID:g2367176; !1PIDN:AAC75971.1; PID:g1789302; UWGP:b2934 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene cmtB CLASSIFICATION #superfamily probable phosphotransferase protein yjfU; !1phosphotransferase system mannitol-specific enzyme II factor !1III homology KEYWORDS phosphoprotein; phosphotransferase; sugar transport system FEATURE !$20-145 #domain phosphotransferase system mannitol-specific !8enzyme II factor III homology #label PT3M SUMMARY #length 147 #molecular-weight 16046 #checksum 1663 SEQUENCE /// ENTRY S73674 #type complete TITLE probable phosphotransferase protein yjfU - Mycoplasma pneumoniae (strain ATCC 29342) ALTERNATE_NAMES hypothetical protein P02_orf159 ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S73674 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73674 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-159 ##label HIM !'##cross-references EMBL:AE000033; GB:U00089; NID:g1674022; !1PIDN:AAB95996.1; PID:g1674025 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#gene yjfU !$#genetic_code SGC3 CLASSIFICATION #superfamily probable phosphotransferase protein yjfU; !1phosphotransferase system mannitol-specific enzyme II factor !1III homology FEATURE !$24-150 #domain phosphotransferase system mannitol-specific !8enzyme II factor III homology #label PT3M SUMMARY #length 159 #molecular-weight 17807 #checksum 9855 SEQUENCE /// ENTRY C70124 #type complete TITLE conserved hypothetical protein BB0195 - Lyme disease spirochete ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C70124 REFERENCE A70100 !$#authors Fraser, C.M.; Casjens, S.; Huang, W.M.; Sutton, G.G.; !1Clayton, R.; Lathigra, R.; White, O.; Ketchum, K.A.; Dodson, !1R.; Hickey, E.K.; Gwinn, M.; Dougherty, B.; Tomb, J.F.; !1Fleischmann, R.D.; Richardson, D.; Peterson, J.; Kerlavage, !1A.R.; Quackenbush, J.; Salzberg, S.; Hanson, M.; Vugt, R.V.; !1Palmer, N.; Adams, M.D.; Gocayne, J.; Weidman, J.; !1Utterback, T.; Watthey, L.; McDonald, L.; Artiach, P.; !1Bowman, C.; Garland, S.; Fujii, C.; Cotton, M.D.; Horst, K.; !1Roberts, K.; Hatch, B.; Smith, H.O.; Venter, J.C. !$#journal Nature (1997) 390:580-586 !$#title Genomic sequence of a Lyme disease spirochaete, Borrelia !1burgdorferi. !$#cross-references MUID:98065943; PMID:9403685 !$#accession C70124 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-379 ##label KLE !'##cross-references GB:AE001129; GB:AE000783; NID:g2688071; !1PIDN:AAC66569.1; PID:g2688072; TIGR:BB0195 !'##experimental_source strain B31 CLASSIFICATION #superfamily transformation sensitive protein; !1tetratricopeptide repeat homology FEATURE !$24-57 #domain tetratricopeptide repeat homology #label TT1\ !$58-91 #domain tetratricopeptide repeat homology #label TT2\ !$92-125 #domain tetratricopeptide repeat homology #label TT3\ !$196-229 #domain tetratricopeptide repeat homology #label TT4\ !$230-263 #domain tetratricopeptide repeat homology #label TT5 SUMMARY #length 379 #molecular-weight 44123 #checksum 9678 SEQUENCE /// ENTRY C71371 #type complete TITLE conserved hypothetical protein TP0067 - syphilis spirochete ORGANISM #formal_name Treponema pallidum subsp. pallidum #common_name syphilis spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS C71371 REFERENCE A71250 !$#authors Fraser, C.M.; Norris, S.J.; Weinstock, G.M.; White, O.; !1Sutton, G.G.; Dodson, R.; Gwinn, M.; Hickey, E.K.; Clayton, !1R.; Ketchum, K.A.; Sodergren, E.; Hardham, J.M.; McLeod, !1M.P.; Salzberg, S.; Peterson, J.; Khalak, H.; Richardson, !1D.; Howell, J.K.; Chidambaram, M.; Utterback, T.; McDonald, !1L.; Artiach, P.; Bowman, C.; Cotton, M.D.; Fujii, C.; !1Garland, S.; Hatch, B.; Horst, K.; Roberts, K.; Watthey, L.; !1Weidman, J.; Smith, H.O.; Venter, J.C. !$#journal Science (1998) 281:375-388 !$#title Complete genome sequence of Treponema pallidum, the syphilis !1spirochete. !$#cross-references MUID:98332770; PMID:9665876 !$#accession C71371 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-393 ##label COL !'##cross-references GB:AE001191; GB:AE000520; NID:g3322316; !1PIDN:AAC65060.1; PID:g3322323 !'##experimental_source strain Nichols GENETICS !$#gene TP0067 CLASSIFICATION #superfamily transformation sensitive protein; !1tetratricopeptide repeat homology FEATURE !$211-244 #domain tetratricopeptide repeat homology #label TTR SUMMARY #length 393 #molecular-weight 45769 #checksum 0 SEQUENCE /// ENTRY E64417 #type complete TITLE transcription initiation factor IIIC homolog - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 15-Oct-1999 ACCESSIONS E64417 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession E64417 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-338 ##label BUL !'##cross-references GB:U67537; GB:L77117; NID:g1591605; PID:g1591609; !1TIGR:MJ0941; PID:g1510980 GENETICS !$#map_position FOR870427-871443 !$#start_codon TTG CLASSIFICATION #superfamily transformation sensitive protein; !1tetratricopeptide repeat homology KEYWORDS transcription initiation FEATURE !$29-62 #domain tetratricopeptide repeat homology #label TT1\ !$63-96 #domain tetratricopeptide repeat homology #label TT2\ !$165-198 #domain tetratricopeptide repeat homology #label TT3\ !$199-232 #domain tetratricopeptide repeat homology #label TT4\ !$268-301 #domain tetratricopeptide repeat homology #label TT5 SUMMARY #length 338 #molecular-weight 39485 #checksum 2966 SEQUENCE /// ENTRY D64417 #type complete TITLE transformation sensitive protein homolog - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D64417 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession D64417 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-318 ##label BUL !'##cross-references GB:U67537; GB:L77117; NID:g2826351; !1PIDN:AAB98944.1; PID:g1591608; TIGR:MJ0940 GENETICS !$#map_position FOR869481-870437 CLASSIFICATION #superfamily transformation sensitive protein; !1tetratricopeptide repeat homology FEATURE !$17-50 #domain tetratricopeptide repeat homology #label TT1\ !$51-83 #domain tetratricopeptide repeat homology #status !8atypical #label TT2\ !$84-117 #domain tetratricopeptide repeat homology #label TT3\ !$118-151 #domain tetratricopeptide repeat homology #label TT4\ !$152-185 #domain tetratricopeptide repeat homology #label TT5\ !$186-219 #domain tetratricopeptide repeat homology #label TT6\ !$255-288 #domain tetratricopeptide repeat homology #label TT7 SUMMARY #length 318 #molecular-weight 36860 #checksum 3163 SEQUENCE /// ENTRY D64117 #type complete TITLE ftsH protein homolog HI1335 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS D64117 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession D64117 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-31 ##label TIGR !'##cross-references GB:L42023; TIGR:HI1335 CLASSIFICATION #superfamily transformation sensitive protein; !1tetratricopeptide repeat homology SUMMARY #length 31 #molecular-weight 3570 #checksum 9255 SEQUENCE /// ENTRY H70166 #type complete TITLE conserved hypothetical protein BB0537 - Lyme disease spirochete ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H70166 REFERENCE A70100 !$#authors Fraser, C.M.; Casjens, S.; Huang, W.M.; Sutton, G.G.; !1Clayton, R.; Lathigra, R.; White, O.; Ketchum, K.A.; Dodson, !1R.; Hickey, E.K.; Gwinn, M.; Dougherty, B.; Tomb, J.F.; !1Fleischmann, R.D.; Richardson, D.; Peterson, J.; Kerlavage, !1A.R.; Quackenbush, J.; Salzberg, S.; Hanson, M.; Vugt, R.V.; !1Palmer, N.; Adams, M.D.; Gocayne, J.; Weidman, J.; !1Utterback, T.; Watthey, L.; McDonald, L.; Artiach, P.; !1Bowman, C.; Garland, S.; Fujii, C.; Cotton, M.D.; Horst, K.; !1Roberts, K.; Hatch, B.; Smith, H.O.; Venter, J.C. !$#journal Nature (1997) 390:580-586 !$#title Genomic sequence of a Lyme disease spirochaete, Borrelia !1burgdorferi. !$#cross-references MUID:98065943; PMID:9403685 !$#accession H70166 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-214 ##label KLE !'##cross-references GB:AE001155; GB:AE000783; NID:g2688448; !1PIDN:AAC66900.1; PID:g2688452; TIGR:BB0537 !'##experimental_source strain B31 CLASSIFICATION #superfamily hypothetical protein BB0537; tetratricopeptide !1repeat homology FEATURE !$93-126 #domain tetratricopeptide repeat homology #label TT1\ !$130-163 #domain tetratricopeptide repeat homology #label TT2\ !$164-197 #domain tetratricopeptide repeat homology #label TT3 SUMMARY #length 214 #molecular-weight 24699 #checksum 3100 SEQUENCE /// ENTRY B70107 #type complete TITLE hypothetical protein BB0058 - Lyme disease spirochete ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B70107 REFERENCE A70100 !$#authors Fraser, C.M.; Casjens, S.; Huang, W.M.; Sutton, G.G.; !1Clayton, R.; Lathigra, R.; White, O.; Ketchum, K.A.; Dodson, !1R.; Hickey, E.K.; Gwinn, M.; Dougherty, B.; Tomb, J.F.; !1Fleischmann, R.D.; Richardson, D.; Peterson, J.; Kerlavage, !1A.R.; Quackenbush, J.; Salzberg, S.; Hanson, M.; Vugt, R.V.; !1Palmer, N.; Adams, M.D.; Gocayne, J.; Weidman, J.; !1Utterback, T.; Watthey, L.; McDonald, L.; Artiach, P.; !1Bowman, C.; Garland, S.; Fujii, C.; Cotton, M.D.; Horst, K.; !1Roberts, K.; Hatch, B.; Smith, H.O.; Venter, J.C. !$#journal Nature (1997) 390:580-586 !$#title Genomic sequence of a Lyme disease spirochaete, Borrelia !1burgdorferi. !$#cross-references MUID:98065943; PMID:9403685 !$#accession B70107 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-656 ##label KLE !'##cross-references GB:AE001119; GB:AE000783; NID:g2687936; !1PIDN:AAC66456.1; PID:g2687949; TIGR:BB0058 !'##experimental_source strain B31 CLASSIFICATION #superfamily hypothetical protein BB0058; tetratricopeptide !1repeat homology FEATURE !$24-57 #domain tetratricopeptide repeat homology #label TT1\ !$58-91 #domain tetratricopeptide repeat homology #label TT2\ !$92-125 #domain tetratricopeptide repeat homology #label TT3\ !$126-159 #domain tetratricopeptide repeat homology #label TT4\ !$234-267 #domain tetratricopeptide repeat homology #label TT5\ !$268-301 #domain tetratricopeptide repeat homology #label TT6 SUMMARY #length 656 #molecular-weight 76394 #checksum 2139 SEQUENCE /// ENTRY G71299 #type complete TITLE conserved hypothetical protein TP0648 - syphilis spirochete ORGANISM #formal_name Treponema pallidum subsp. pallidum #common_name syphilis spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS G71299 REFERENCE A71250 !$#authors Fraser, C.M.; Norris, S.J.; Weinstock, G.M.; White, O.; !1Sutton, G.G.; Dodson, R.; Gwinn, M.; Hickey, E.K.; Clayton, !1R.; Ketchum, K.A.; Sodergren, E.; Hardham, J.M.; McLeod, !1M.P.; Salzberg, S.; Peterson, J.; Khalak, H.; Richardson, !1D.; Howell, J.K.; Chidambaram, M.; Utterback, T.; McDonald, !1L.; Artiach, P.; Bowman, C.; Cotton, M.D.; Fujii, C.; !1Garland, S.; Hatch, B.; Horst, K.; Roberts, K.; Watthey, L.; !1Weidman, J.; Smith, H.O.; Venter, J.C. !$#journal Science (1998) 281:375-388 !$#title Complete genome sequence of Treponema pallidum, the syphilis !1spirochete. !$#cross-references MUID:98332770; PMID:9665876 !$#accession G71299 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-682 ##label COL !'##cross-references GB:AE001239; GB:AE000520; NID:g3322937; !1PIDN:AAC65621.1; PID:g3322946 !'##experimental_source strain Nichols GENETICS !$#gene TP0648 CLASSIFICATION #superfamily hypothetical protein TP0648 SUMMARY #length 682 #molecular-weight 77635 #checksum 763 SEQUENCE /// ENTRY F70115 #type complete TITLE hypothetical protein BB0126 - Lyme disease spirochete ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F70115 REFERENCE A70100 !$#authors Fraser, C.M.; Casjens, S.; Huang, W.M.; Sutton, G.G.; !1Clayton, R.; Lathigra, R.; White, O.; Ketchum, K.A.; Dodson, !1R.; Hickey, E.K.; Gwinn, M.; Dougherty, B.; Tomb, J.F.; !1Fleischmann, R.D.; Richardson, D.; Peterson, J.; Kerlavage, !1A.R.; Quackenbush, J.; Salzberg, S.; Hanson, M.; Vugt, R.V.; !1Palmer, N.; Adams, M.D.; Gocayne, J.; Weidman, J.; !1Utterback, T.; Watthey, L.; McDonald, L.; Artiach, P.; !1Bowman, C.; Garland, S.; Fujii, C.; Cotton, M.D.; Horst, K.; !1Roberts, K.; Hatch, B.; Smith, H.O.; Venter, J.C. !$#journal Nature (1997) 390:580-586 !$#title Genomic sequence of a Lyme disease spirochaete, Borrelia !1burgdorferi. !$#cross-references MUID:98065943; PMID:9403685 !$#accession F70115 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-203 ##label KLE !'##cross-references GB:AE001124; GB:AE000783; NID:g2688003; !1PIDN:AAC66520.1; PID:g2688018; TIGR:BB0126 !'##experimental_source strain B31 CLASSIFICATION #superfamily hypothetical protein BB0126; tetratricopeptide !1repeat homology FEATURE !$82-115 #domain tetratricopeptide repeat homology #label TT1 SUMMARY #length 203 #molecular-weight 23595 #checksum 2166 SEQUENCE /// ENTRY D71263 #type complete TITLE conserved hypothetical protein TP0944 - syphilis spirochete ORGANISM #formal_name Treponema pallidum subsp. pallidum #common_name syphilis spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS D71263 REFERENCE A71250 !$#authors Fraser, C.M.; Norris, S.J.; Weinstock, G.M.; White, O.; !1Sutton, G.G.; Dodson, R.; Gwinn, M.; Hickey, E.K.; Clayton, !1R.; Ketchum, K.A.; Sodergren, E.; Hardham, J.M.; McLeod, !1M.P.; Salzberg, S.; Peterson, J.; Khalak, H.; Richardson, !1D.; Howell, J.K.; Chidambaram, M.; Utterback, T.; McDonald, !1L.; Artiach, P.; Bowman, C.; Cotton, M.D.; Fujii, C.; !1Garland, S.; Hatch, B.; Horst, K.; Roberts, K.; Watthey, L.; !1Weidman, J.; Smith, H.O.; Venter, J.C. !$#journal Science (1998) 281:375-388 !$#title Complete genome sequence of Treponema pallidum, the syphilis !1spirochete. !$#cross-references MUID:98332770; PMID:9665876 !$#accession D71263 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-390 ##label COL !'##cross-references GB:AE001262; GB:AE000520; NID:g3323254; !1PIDN:AAC65897.1; PID:g3323261 !'##experimental_source strain Nichols GENETICS !$#gene TP0944 CLASSIFICATION #superfamily hypothetical protein TP0944; tetratricopeptide !1repeat homology SUMMARY #length 390 #molecular-weight 43479 #checksum 8731 SEQUENCE /// ENTRY F70116 #type complete TITLE hypothetical protein BB0134 - Lyme disease spirochete ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F70116 REFERENCE A70100 !$#authors Fraser, C.M.; Casjens, S.; Huang, W.M.; Sutton, G.G.; !1Clayton, R.; Lathigra, R.; White, O.; Ketchum, K.A.; Dodson, !1R.; Hickey, E.K.; Gwinn, M.; Dougherty, B.; Tomb, J.F.; !1Fleischmann, R.D.; Richardson, D.; Peterson, J.; Kerlavage, !1A.R.; Quackenbush, J.; Salzberg, S.; Hanson, M.; Vugt, R.V.; !1Palmer, N.; Adams, M.D.; Gocayne, J.; Weidman, J.; !1Utterback, T.; Watthey, L.; McDonald, L.; Artiach, P.; !1Bowman, C.; Garland, S.; Fujii, C.; Cotton, M.D.; Horst, K.; !1Roberts, K.; Hatch, B.; Smith, H.O.; Venter, J.C. !$#journal Nature (1997) 390:580-586 !$#title Genomic sequence of a Lyme disease spirochaete, Borrelia !1burgdorferi. !$#cross-references MUID:98065943; PMID:9403685 !$#accession F70116 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-382 ##label KLE !'##cross-references GB:AE001125; GB:AE000783; NID:g2688021; !1PIDN:AAC66535.1; PID:g2688034; TIGR:BB0134 !'##experimental_source strain B31 CLASSIFICATION #superfamily hypothetical protein TP0944; tetratricopeptide !1repeat homology FEATURE !$10-43 #domain tetratricopeptide repeat homology #label TT1\ !$44-77 #domain tetratricopeptide repeat homology #label TT2 SUMMARY #length 382 #molecular-weight 44325 #checksum 7918 SEQUENCE /// ENTRY A70126 #type complete TITLE hypothetical protein BB0209 - Lyme disease spirochete ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A70126 REFERENCE A70100 !$#authors Fraser, C.M.; Casjens, S.; Huang, W.M.; Sutton, G.G.; !1Clayton, R.; Lathigra, R.; White, O.; Ketchum, K.A.; Dodson, !1R.; Hickey, E.K.; Gwinn, M.; Dougherty, B.; Tomb, J.F.; !1Fleischmann, R.D.; Richardson, D.; Peterson, J.; Kerlavage, !1A.R.; Quackenbush, J.; Salzberg, S.; Hanson, M.; Vugt, R.V.; !1Palmer, N.; Adams, M.D.; Gocayne, J.; Weidman, J.; !1Utterback, T.; Watthey, L.; McDonald, L.; Artiach, P.; !1Bowman, C.; Garland, S.; Fujii, C.; Cotton, M.D.; Horst, K.; !1Roberts, K.; Hatch, B.; Smith, H.O.; Venter, J.C. !$#journal Nature (1997) 390:580-586 !$#title Genomic sequence of a Lyme disease spirochaete, Borrelia !1burgdorferi. !$#cross-references MUID:98065943; PMID:9403685 !$#accession A70126 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-255 ##label KLE !'##cross-references GB:AE001131; GB:AE000783; NID:g2688098; !1PIDN:AAC66599.1; PID:g2688104; TIGR:BB0209 !'##experimental_source strain B31 CLASSIFICATION #superfamily hypothetical protein BB0209; tetratricopeptide !1repeat homology FEATURE !$29-62 #domain tetratricopeptide repeat homology #label TT1\ !$63-96 #domain tetratricopeptide repeat homology #label TT2 SUMMARY #length 255 #molecular-weight 30055 #checksum 9610 SEQUENCE /// ENTRY E70132 #type complete TITLE hypothetical protein BB0261 - Lyme disease spirochete ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E70132 REFERENCE A70100 !$#authors Fraser, C.M.; Casjens, S.; Huang, W.M.; Sutton, G.G.; !1Clayton, R.; Lathigra, R.; White, O.; Ketchum, K.A.; Dodson, !1R.; Hickey, E.K.; Gwinn, M.; Dougherty, B.; Tomb, J.F.; !1Fleischmann, R.D.; Richardson, D.; Peterson, J.; Kerlavage, !1A.R.; Quackenbush, J.; Salzberg, S.; Hanson, M.; Vugt, R.V.; !1Palmer, N.; Adams, M.D.; Gocayne, J.; Weidman, J.; !1Utterback, T.; Watthey, L.; McDonald, L.; Artiach, P.; !1Bowman, C.; Garland, S.; Fujii, C.; Cotton, M.D.; Horst, K.; !1Roberts, K.; Hatch, B.; Smith, H.O.; Venter, J.C. !$#journal Nature (1997) 390:580-586 !$#title Genomic sequence of a Lyme disease spirochaete, Borrelia !1burgdorferi. !$#cross-references MUID:98065943; PMID:9403685 !$#accession E70132 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-460 ##label KLE !'##cross-references GB:AE001137; GB:AE000783; NID:g2688160; !1PIDN:AAC66691.1; PID:g2688209; TIGR:BB0261 !'##experimental_source strain B31 CLASSIFICATION #superfamily hypothetical protein BB0261; tetratricopeptide !1repeat homology FEATURE !$103-136 #domain tetratricopeptide repeat homology #label TT1\ !$137-170 #domain tetratricopeptide repeat homology #label TT2\ !$205-238 #domain tetratricopeptide repeat homology #label TT3\ !$239-272 #domain tetratricopeptide repeat homology #label TT4\ !$278-310 #domain tetratricopeptide repeat homology #status !8atypical #label TT5\ !$311-344 #domain tetratricopeptide repeat homology #label TT6 SUMMARY #length 460 #molecular-weight 54024 #checksum 9100 SEQUENCE /// ENTRY H71264 #type complete TITLE conserved hypothetical protein TP0915 - syphilis spirochete ORGANISM #formal_name Treponema pallidum subsp. pallidum #common_name syphilis spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS H71264 REFERENCE A71250 !$#authors Fraser, C.M.; Norris, S.J.; Weinstock, G.M.; White, O.; !1Sutton, G.G.; Dodson, R.; Gwinn, M.; Hickey, E.K.; Clayton, !1R.; Ketchum, K.A.; Sodergren, E.; Hardham, J.M.; McLeod, !1M.P.; Salzberg, S.; Peterson, J.; Khalak, H.; Richardson, !1D.; Howell, J.K.; Chidambaram, M.; Utterback, T.; McDonald, !1L.; Artiach, P.; Bowman, C.; Cotton, M.D.; Fujii, C.; !1Garland, S.; Hatch, B.; Horst, K.; Roberts, K.; Watthey, L.; !1Weidman, J.; Smith, H.O.; Venter, J.C. !$#journal Science (1998) 281:375-388 !$#title Complete genome sequence of Treponema pallidum, the syphilis !1spirochete. !$#cross-references MUID:98332770; PMID:9665876 !$#accession H71264 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-444 ##label COL !'##cross-references GB:AE001260; GB:AE000520; NID:g3323232; !1PIDN:AAC65872.1; PID:g3323234 !'##experimental_source strain Nichols GENETICS !$#gene TP0915 CLASSIFICATION #superfamily hypothetical protein BB0261; tetratricopeptide !1repeat homology SUMMARY #length 444 #molecular-weight 50768 #checksum 1454 SEQUENCE /// ENTRY JC5394 #type complete TITLE DJ-1 protein - human ORGANISM #formal_name Homo sapiens #common_name man DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 16-Jun-2000 ACCESSIONS JC5394 REFERENCE JC5394 !$#authors Nagakubo, D.; Taira, T.; Kitaura, H.; Ikeda, M.; Tamai, K.; !1Iguchi-Ariga, S.M.M.; Ariga, H. !$#journal Biochem. Biophys. Res. Commun. (1997) 231:509-513 !$#title DJ-1, a novel oncogene which transforms mouse NIH3T3 cells !1in cooperation with ras. !$#cross-references MUID:97223489; PMID:9070310 !$#accession JC5394 !'##molecule_type mRNA !'##residues 1-189 ##label NAG !'##cross-references DDBJ:D61380; NID:g914937; PIDN:BAA09603.1; !1PID:g1780755 COMMENT This protein is involved in a Ras-related signal !1transduction pathway. GENETICS !$#gene GDB:DJ1 !'##cross-references GDB:175839; OMIM:602533 CLASSIFICATION #superfamily signal transduction protein DJ-1 SUMMARY #length 189 #molecular-weight 19847 #checksum 4343 SEQUENCE /// ENTRY JE0344 #type complete TITLE contraception associated protein 1 - rat ALTERNATE_NAMES CAP1 ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 16-Jun-2000 ACCESSIONS JE0344 REFERENCE JE0344 !$#authors Wagenfeld, A.; Gromoll, J.; Cooper, T.G. !$#journal Biochem. Biophys. Res. Commun. (1998) 251:545-549 !$#title Molecular cloning and expression of rat contraception !1associated protein 1 (CAP1), a protein putatively involved !1in fertilization. !$#cross-references MUID:99011415; PMID:9792810 !$#accession JE0344 !'##status preliminary !'##molecule_type mRNA !'##residues 1-189 ##label WAG !'##cross-references GB:AJ007291; NID:g3250915; PIDN:CAA07434.1; !1PID:g3250916 CLASSIFICATION #superfamily signal transduction protein DJ-1 SUMMARY #length 189 #molecular-weight 19974 #checksum 5939 SEQUENCE /// ENTRY H64771 #type complete TITLE hydroxymethylpyrimidine kinase (EC 2.7.1.49) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 01-Mar-2002 ACCESSIONS H64771 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64771 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-198 ##label BLAT !'##cross-references GB:AE000148; GB:U00096; NID:g1786614; !1PIDN:AAC73527.1; PID:g1786626; UWGP:b0424 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene thiJ FUNCTION !$#description catalyzes phosphorylation of hydroxymethylpyrimidine to !1hydroxymethylpyrimidine monophosphate !$#pathway thiamine biosynthesis CLASSIFICATION #superfamily signal transduction protein DJ-1 KEYWORDS phosphotransferase SUMMARY #length 198 #molecular-weight 21022 #checksum 3952 SEQUENCE /// ENTRY T03871 #type complete TITLE hypothetical protein C49G7.11 - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 15-Oct-1999 ACCESSIONS T03871 REFERENCE Z16068 !$#authors Bradshaw, H.; Graves, T.; Fronick, W. !$#submission submitted to the EMBL Data Library, July 1997 !$#description The sequence of C. elegans cosmid C49G7. !$#accession T03871 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-186 ##label WIL !'##cross-references EMBL:AF016418; NID:g2291147; PIDN:AAB65292.1; !1PID:g2291156 GENETICS !$#map_position V !$#introns 44/3; 135/1 !$#note C49G7.11 CLASSIFICATION #superfamily signal transduction protein DJ-1 SUMMARY #length 186 #molecular-weight 19556 #checksum 3552 SEQUENCE /// ENTRY B64203 #type complete TITLE hypothetical protein homolog MG029 - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 07-Dec-1999 ACCESSIONS B64203 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession B64203 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-186 ##label TIGR !'##cross-references GB:U39681; GB:L43967; NID:g1045694; PID:g1045699; !1TIGR:MG029 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily signal transduction protein DJ-1 SUMMARY #length 186 #molecular-weight 20884 #checksum 8342 SEQUENCE /// ENTRY S73448 #type complete TITLE hypothetical protein B01_orf108 - Mycoplasma pneumoniae (strain ATCC 29342) ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 10-Dec-1999 ACCESSIONS S73448 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73448 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-108 ##label HIM !'##cross-references EMBL:AE000015; GB:U00089; NID:g1673779; !1PIDN:AAB95770.1; PID:g1673781 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily signal transduction protein DJ-1 SUMMARY #length 108 #molecular-weight 12200 #checksum 1256 SEQUENCE /// ENTRY D70177 #type complete TITLE 4-methyl-5(b-hydroxyethyl)-thiazole monophosphate biosynthesis protein (thiJ) homolog - Lyme disease spirochete ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 15-Oct-1999 ACCESSIONS D70177 REFERENCE A70100 !$#authors Fraser, C.M.; Casjens, S.; Huang, W.M.; Sutton, G.G.; !1Clayton, R.; Lathigra, R.; White, O.; Ketchum, K.A.; Dodson, !1R.; Hickey, E.K.; Gwinn, M.; Dougherty, B.; Tomb, J.F.; !1Fleischmann, R.D.; Richardson, D.; Peterson, J.; Kerlavage, !1A.R.; Quackenbush, J.; Salzberg, S.; Hanson, M.; Vugt, R.V.; !1Palmer, N.; Adams, M.D.; Gocayne, J.; Weidman, J.; !1Utterback, T.; Watthey, L.; McDonald, L.; Artiach, P.; !1Bowman, C.; Garland, S.; Fujii, C.; Cotton, M.D.; Horst, K.; !1Roberts, K.; Hatch, B.; Smith, H.O.; Venter, J.C. !$#journal Nature (1997) 390:580-586 !$#title Genomic sequence of a Lyme disease spirochaete, Borrelia !1burgdorferi. !$#cross-references MUID:98065943; PMID:9403685 !$#accession D70177 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-184 ##label KLE !'##cross-references GB:AE001163; GB:AE000783; NID:g2688541; !1PIDN:AAC66975.1; PID:g2688544; TIGR:BB0621 !'##experimental_source strain B31 CLASSIFICATION #superfamily signal transduction protein DJ-1 SUMMARY #length 184 #molecular-weight 19884 #checksum 1398 SEQUENCE /// ENTRY E71324 #type complete TITLE probable 4-methyl-5(b-hydroxyethyl)-thiazole monophosphate biosynthesis enzyme (thiJ) - syphilis spirochete ORGANISM #formal_name Treponema pallidum subsp. pallidum #common_name syphilis spirochete DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 28-Jul-2000 ACCESSIONS E71324 REFERENCE A71250 !$#authors Fraser, C.M.; Norris, S.J.; Weinstock, G.M.; White, O.; !1Sutton, G.G.; Dodson, R.; Gwinn, M.; Hickey, E.K.; Clayton, !1R.; Ketchum, K.A.; Sodergren, E.; Hardham, J.M.; McLeod, !1M.P.; Salzberg, S.; Peterson, J.; Khalak, H.; Richardson, !1D.; Howell, J.K.; Chidambaram, M.; Utterback, T.; McDonald, !1L.; Artiach, P.; Bowman, C.; Cotton, M.D.; Fujii, C.; !1Garland, S.; Hatch, B.; Horst, K.; Roberts, K.; Watthey, L.; !1Weidman, J.; Smith, H.O.; Venter, J.C. !$#journal Science (1998) 281:375-388 !$#title Complete genome sequence of Treponema pallidum, the syphilis !1spirochete. !$#cross-references MUID:98332770; PMID:9665876 !$#accession E71324 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-209 ##label COL !'##cross-references GB:AE001221; GB:AE000520; NID:g3322720; !1PIDN:AAC65432.1; PID:g3322730 !'##experimental_source strain Nichols GENETICS !$#gene TP0445 CLASSIFICATION #superfamily signal transduction protein DJ-1 SUMMARY #length 209 #molecular-weight 22045 #checksum 9673 SEQUENCE /// ENTRY A70189 #type complete TITLE hypothetical protein BB0714 - Lyme disease spirochete ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A70189 REFERENCE A70100 !$#authors Fraser, C.M.; Casjens, S.; Huang, W.M.; Sutton, G.G.; !1Clayton, R.; Lathigra, R.; White, O.; Ketchum, K.A.; Dodson, !1R.; Hickey, E.K.; Gwinn, M.; Dougherty, B.; Tomb, J.F.; !1Fleischmann, R.D.; Richardson, D.; Peterson, J.; Kerlavage, !1A.R.; Quackenbush, J.; Salzberg, S.; Hanson, M.; Vugt, R.V.; !1Palmer, N.; Adams, M.D.; Gocayne, J.; Weidman, J.; !1Utterback, T.; Watthey, L.; McDonald, L.; Artiach, P.; !1Bowman, C.; Garland, S.; Fujii, C.; Cotton, M.D.; Horst, K.; !1Roberts, K.; Hatch, B.; Smith, H.O.; Venter, J.C. !$#journal Nature (1997) 390:580-586 !$#title Genomic sequence of a Lyme disease spirochaete, Borrelia !1burgdorferi. !$#cross-references MUID:98065943; PMID:9403685 !$#accession A70189 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-322 ##label KLE !'##cross-references GB:AE001171; GB:AE000783; NID:g2688640; !1PIDN:AAC67064.1; PID:g2688650; TIGR:BB0714 !'##experimental_source strain B31 CLASSIFICATION #superfamily hypothetical protein BB0714; tetratricopeptide !1repeat homology FEATURE !$122-155 #domain tetratricopeptide repeat homology #label TT1\ !$161-193 #domain tetratricopeptide repeat homology #status !8atypical #label TT2\ !$194-227 #domain tetratricopeptide repeat homology #label TT3\ !$240-273 #domain tetratricopeptide repeat homology #label TT4 SUMMARY #length 322 #molecular-weight 38625 #checksum 4804 SEQUENCE /// ENTRY D71316 #type complete TITLE conserved hypothetical protein TP0496 - syphilis spirochete ORGANISM #formal_name Treponema pallidum subsp. pallidum #common_name syphilis spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS D71316 REFERENCE A71250 !$#authors Fraser, C.M.; Norris, S.J.; Weinstock, G.M.; White, O.; !1Sutton, G.G.; Dodson, R.; Gwinn, M.; Hickey, E.K.; Clayton, !1R.; Ketchum, K.A.; Sodergren, E.; Hardham, J.M.; McLeod, !1M.P.; Salzberg, S.; Peterson, J.; Khalak, H.; Richardson, !1D.; Howell, J.K.; Chidambaram, M.; Utterback, T.; McDonald, !1L.; Artiach, P.; Bowman, C.; Cotton, M.D.; Fujii, C.; !1Garland, S.; Hatch, B.; Horst, K.; Roberts, K.; Watthey, L.; !1Weidman, J.; Smith, H.O.; Venter, J.C. !$#journal Science (1998) 281:375-388 !$#title Complete genome sequence of Treponema pallidum, the syphilis !1spirochete. !$#cross-references MUID:98332770; PMID:9665876 !$#accession D71316 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-329 ##label COL !'##cross-references GB:AE001226; GB:AE000520; NID:g3322785; !1PIDN:AAC65483.1; PID:g3322786 !'##experimental_source strain Nichols GENETICS !$#gene TP0496 CLASSIFICATION #superfamily hypothetical protein BB0714; tetratricopeptide !1repeat homology SUMMARY #length 329 #molecular-weight 37761 #checksum 7074 SEQUENCE /// ENTRY F64006 #type complete TITLE hypothetical protein HI0366 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS F64006 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession F64006 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-179 ##label TIGR !'##cross-references GB:U32721; GB:L42023; NID:g1573334; !1PIDN:AAC22024.1; PID:g1573335; TIGR:HI0366 CLASSIFICATION #superfamily hypothetical protein HI0366; tetratricopeptide !1repeat homology FEATURE !$34-67 #domain tetratricopeptide repeat homology #label TT1\ !$68-101 #domain tetratricopeptide repeat homology #label TT2\ !$102-135 #domain tetratricopeptide repeat homology #label TT3 SUMMARY #length 179 #molecular-weight 20598 #checksum 403 SEQUENCE /// ENTRY JC5302 #type complete TITLE PilF protein - Pseudomonas aeruginosa ORGANISM #formal_name Pseudomonas aeruginosa DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS JC5302 REFERENCE JC5302 !$#authors Watson, A.A.; Alm, R.A.; Mattick, J.S. !$#journal Gene (1996) 180:49-56 !$#title Identification of a gene, pilF, required for type 4 fimbrial !1biogenesis and twitching motility in Pseudomonas aeruginosa. !$#cross-references MUID:97128806; PMID:8973346 !$#accession JC5302 !'##molecule_type DNA !'##residues 1-198 ##label WAT !'##cross-references GB:L49434; NID:g1162958; PIDN:AAB40949.1; !1PID:g1162960 COMMENT This protein is an outer membrane-associated lipoprotein and !1involved in the fimbrial biogenesis and twitching motility. GENETICS !$#gene pilF CLASSIFICATION #superfamily hypothetical protein HI0366; tetratricopeptide !1repeat homology FEATURE !$37-70 #domain tetratricopeptide repeat homology #label TT1\ !$71-104 #domain tetratricopeptide repeat homology #label TT2\ !$141-174 #domain tetratricopeptide repeat homology #label TT3 SUMMARY #length 198 #molecular-weight 22416 #checksum 5637 SEQUENCE /// ENTRY C43735 #type complete TITLE bcsC protein - Acetobacter pasteurianus ORGANISM #formal_name Acetobacter pasteurianus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C43735 REFERENCE A43735 !$#authors Wong, H.C.; Fear, A.L.; Calhoon, R.D.; Eichinger, G.H.; !1Mayer, R.; Amikam, D.; Benziman, M.; Gelfand, D.H.; Meade, !1J.H.; Emerick, A.W.; Bruner, R.; Ben-Bassat, A.; Tal, R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:8130-8134 !$#title Genetic organization of the cellulose synthase operon in !1Acetobacter xylinum. !$#cross-references MUID:91045951; PMID:2146681 !$#accession C43735 !'##status preliminary; translation not shown !'##molecule_type DNA !'##residues 1-1319 ##label WON !'##cross-references EMBL:M37202; NID:g141731; PID:g141734 !'##note the source is designated as Acetobacter xylinum CLASSIFICATION #superfamily Acetobacter pasteurianus bcsC protein; !1tetratricopeptide repeat homology FEATURE !$291-324 #domain tetratricopeptide repeat homology #label TT1\ !$325-358 #domain tetratricopeptide repeat homology #label TT2\ !$701-734 #domain tetratricopeptide repeat homology #label TT3\ !$735-768 #domain tetratricopeptide repeat homology #label TT4 SUMMARY #length 1319 #molecular-weight 141430 #checksum 9345 SEQUENCE /// ENTRY E65151 #type complete TITLE hypothetical 126K protein (dctA-dppF intergenic region) - Escherichia coli (strain K-12) ALTERNATE_NAMES hypothetical protein f1165 ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS E65151; S47751 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65151 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-1166 ##label BLAT !'##cross-references GB:AE000430; GB:U00096; NID:g2367238; !1PIDN:AAC76555.1; PID:g2367239; UWGP:b3530 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S47666 !$#authors Plunkett, G. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S47751 !'##status preliminary !'##molecule_type DNA !'##residues 1-602,'V',605-1166 ##label PLU !'##cross-references EMBL:U00039; NID:g466582; PID:g912469 GENETICS !$#gene yhjL !$#start_codon GTG CLASSIFICATION #superfamily hypothetical protein f1165; tetratricopeptide !1repeat homology FEATURE !$252-285 #domain tetratricopeptide repeat homology #label TT1\ !$286-319 #domain tetratricopeptide repeat homology #label TT2 SUMMARY #length 1166 #molecular-weight 128654 #checksum 4040 SEQUENCE /// ENTRY H70421 #type complete TITLE hypothetical protein aq_1402 - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H70421 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession H70421 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-670 ##label AQF !'##cross-references GB:AE000738; GB:AE000657; NID:g2983801; !1PIDN:AAC07363.1; PID:g2983806 !'##experimental_source strain VF5 GENETICS !$#gene aq_1402 CLASSIFICATION #superfamily Aquifex aeolicus hypothetical protein aq_1402; !1tetratricopeptide repeat homology FEATURE !$226-255 #domain tetratricopeptide repeat homology #label TT1\ !$256-289 #domain tetratricopeptide repeat homology #label TT2\ !$290-323 #domain tetratricopeptide repeat homology #label TT3\ !$402-439 #domain tetratricopeptide repeat homology #label TT4\ !$440-475 #domain tetratricopeptide repeat homology #label TT5 SUMMARY #length 670 #molecular-weight 78190 #checksum 8320 SEQUENCE /// ENTRY JC6009 #type complete TITLE surface-located membrane protein lmp3 precursor - Mycoplasma hominis ORGANISM #formal_name Mycoplasma hominis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS JC6009 REFERENCE JC6009 !$#authors Ladefoged, S.A.; Jensen, L.T.; Brock, B.; Birkelund, S.; !1Christiansen, G. !$#journal J. Bacteriol. (1996) 178:2775-2784 !$#title Analysis of 0.5-kilobase-pair repeats in the Mycoplasma !1hominis lmp gene system and identification of gene products. !$#cross-references MUID:96213016; PMID:8631664 !$#accession JC6009 !'##molecule_type DNA !'##residues 1-1302 ##label LAD !'##cross-references EMBL:X95601; NID:g1197335; PIDN:CAA64858.1; !1PID:g1197336 GENETICS !$#gene lmp3 !$#genetic_code SGC3 CLASSIFICATION #superfamily surface-located membrane protein lmp3; !1tetratricopeptide repeat homology KEYWORDS duplication; membrane protein FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-1302 #product surface-located membrane protein Lmp3 !8#status predicted #label MAT\ !$957-992 #domain tetratricopeptide repeat homology #label TT1\ !$993-1026 #domain tetratricopeptide repeat homology #label TT2\ !$1089-1120 #domain tetratricopeptide repeat homology #label TT3\ !$1154-1190 #domain tetratricopeptide repeat homology #label TT4 SUMMARY #length 1302 #molecular-weight 145798 #checksum 8932 SEQUENCE /// ENTRY E65006 #type complete TITLE hypothetical protein b2335 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS E65006 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65006 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-170 ##label BLAT !'##cross-references GB:AE000322; GB:U00096; NID:g1788672; !1PIDN:AAC75395.1; PID:g1788676; UWGP:b2335 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily fimbrial protein smfE SUMMARY #length 170 #molecular-weight 17890 #checksum 5960 SEQUENCE /// ENTRY B39415 #type complete TITLE fimbrial protein smfE - Serratia marcescens ORGANISM #formal_name Serratia marcescens DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B39415 REFERENCE A39415 !$#authors Mizunoe, Y.; Matsumoto, T.; Amako, K.; Sekiguchi, M.; !1Kumazawa, J. !$#journal J. Bacteriol. (1991) 173:3257-3260 !$#title Identification and nucleotide sequence of the gene !1determining the adhesion capacity of Serratia marcescens. !$#cross-references MUID:91217004; PMID:2022623 !$#accession B39415 !'##status preliminary !'##molecule_type DNA !'##residues 1-163 ##label MIZ !'##cross-references GB:M68877; NID:g152865; PID:g152866 CLASSIFICATION #superfamily fimbrial protein smfE SUMMARY #length 163 #molecular-weight 17690 #checksum 3240 SEQUENCE /// ENTRY D65006 #type complete TITLE hypothetical protein b2334 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS D65006 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65006 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-162 ##label BLAT !'##cross-references GB:AE000322; GB:U00096; NID:g1788672; !1PIDN:AAC75394.1; PID:g1788675; UWGP:b2334 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily fimbrial protein smfE SUMMARY #length 162 #molecular-weight 17890 #checksum 9169 SEQUENCE /// ENTRY B32048 #type complete TITLE gliding motility protein - Myxococcus xanthus ORGANISM #formal_name Myxococcus xanthus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B32048 REFERENCE A32048 !$#authors Stephens, K.; Hartzell, P.; Kaiser, D. !$#journal J. Bacteriol. (1989) 171:819-830 !$#title Gliding motility in Myxococcus xanthus: mgl locus, RNA, and !1predicted protein products. !$#cross-references MUID:89123159; PMID:2464581 !$#accession B32048 !'##status preliminary !'##molecule_type DNA !'##residues 1-195 ##label STE !'##cross-references GB:M24147; NID:g150076; PIDN:AAA25389.1; !1PID:g150078 CLASSIFICATION #superfamily gliding motility protein SUMMARY #length 195 #molecular-weight 22015 #checksum 2336 SEQUENCE /// ENTRY C70435 #type complete TITLE gliding motility protein - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C70435 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession C70435 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-190 ##label AQF !'##cross-references GB:AE000745; GB:AE000657; NID:g2983907; !1PIDN:AAC07468.1; PID:g2983918 !'##experimental_source strain VF5 GENETICS !$#gene mglA1 CLASSIFICATION #superfamily gliding motility protein SUMMARY #length 190 #molecular-weight 21696 #checksum 2399 SEQUENCE /// ENTRY B70457 #type complete TITLE gliding motility protein MglA - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B70457 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession B70457 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-141 ##label AQF !'##cross-references GB:AE000757; GB:AE000657; NID:g2984092; !1PIDN:AAC07638.1; PID:g2984100 !'##experimental_source strain VF5 GENETICS !$#gene mglA2 CLASSIFICATION #superfamily gliding motility protein SUMMARY #length 141 #molecular-weight 16206 #checksum 1284 SEQUENCE /// ENTRY B47679 #type complete TITLE major autolysin (lytC) secretion protein lytA precursor - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B47679; C69654 REFERENCE A47679 !$#authors Lazarevic, V.; Margot, P.; Soldo, B.; Karamata, D. !$#journal J. Gen. Microbiol. (1992) 138:1949-1961 !$#title Sequencing and analysis of the Bacillus subtilis lytRABC !1divergon: a regulatory unit encompassing the structural !1genes of the N-acetylmuramoyl-L-alanine amidase and its !1modifier. !$#cross-references MUID:93018998; PMID:1357079 !$#accession B47679 !'##molecule_type DNA !'##residues 1-102 ##label LAZ !'##cross-references GB:M87645; NID:g143155; PIDN:AAA22579.1; !1PID:g143157 !'##experimental_source strain 168 !'##note sequence extracted from NCBI backbone (NCBIN:116645, !1NCBIP:116647) REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69654 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-102 ##label KUN !'##cross-references GB:Z99122; GB:AL009126; NID:g2636029; !1PIDN:CAB15581.1; PID:g2636090 !'##experimental_source strain 168 GENETICS !$#gene lytA CLASSIFICATION #superfamily Bacillus subtilis major autolysin secretion !1protein lytA KEYWORDS blocked amino end; lipoprotein FEATURE !$1-16 #domain signal sequence #status predicted #label SIG\ !$17-102 #product lytA #status predicted #label MAT\ !$17 #binding_site sn-2,3-diacylglycerol (Cys) (covalent) !8#status predicted\ !$17 #modified_site fatty acylated amino end (Cys) (in !8mature form) #status predicted SUMMARY #length 102 #molecular-weight 11228 #checksum 4645 SEQUENCE /// ENTRY D69961 #type complete TITLE lipoprotein homolog yqiH - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69961; I40005 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D69961 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-97 ##label KUN !'##cross-references GB:Z99116; GB:AL009126; NID:g2634723; !1PIDN:CAB14351.1; PID:g2634854 !'##experimental_source strain 168 REFERENCE I39994 !$#authors Smith, H.; de Jong, A.; Bron, S.; Venema, G. !$#journal Gene (1988) 70:351-361 !$#title Characterization of signal-sequence-coding regions selected !1from the Bacillus subtilis chromosome. !$#cross-references MUID:89108019; PMID:3145906 !$#accession I40005 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-41,93,'ES',96,'AQA' ##label RES !'##cross-references GB:M22911; NID:g143691; PIDN:AAA22827.1; !1PID:g143692 GENETICS !$#gene yqiH !$#start_codon GTG CLASSIFICATION #superfamily Bacillus subtilis major autolysin secretion !1protein lytA SUMMARY #length 97 #molecular-weight 10743 #checksum 9082 SEQUENCE /// ENTRY B49939 #type complete TITLE ebsB protein - Enterococcus faecalis ORGANISM #formal_name Enterococcus faecalis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B49939 REFERENCE A49939 !$#authors Bensing, B.A.; Dunny, G.M. !$#journal J. Bacteriol. (1993) 175:7421-7429 !$#title Cloning and molecular analysis of genes affecting expression !1of binding substance, the recipient-encoded receptor(s) !1mediating mating aggregate formation in Enterococcus !1faecalis. !$#cross-references MUID:94042918; PMID:8226689 !$#accession B49939 !'##status preliminary !'##molecule_type DNA !'##residues 1-135 ##label BEN !'##cross-references GB:L23802; NID:g388106; PIDN:AAC36852.1; !1PID:g388108 CLASSIFICATION #superfamily Enterococcus faecalis ebsB protein SUMMARY #length 135 #molecular-weight 15369 #checksum 9819 SEQUENCE /// ENTRY D69934 #type complete TITLE cell wall enzyme homolog ypdQ - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69934 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D69934 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-132 ##label KUN !'##cross-references GB:Z99115; GB:AL009126; NID:g2634478; !1PIDN:CAB14117.1; PID:g2634619 !'##experimental_source strain 168 GENETICS !$#gene ypdQ CLASSIFICATION #superfamily Enterococcus faecalis ebsB protein SUMMARY #length 132 #molecular-weight 14670 #checksum 8850 SEQUENCE /// ENTRY B64021 #type complete TITLE hypothetical protein HI1173 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS B64021 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession B64021 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-156 ##label TIGR !'##cross-references GB:U32797; GB:L42023; NID:g1574095; !1PIDN:AAC22826.1; PID:g1574100; TIGR:HI1173 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily hypothetical protein HI1173 SUMMARY #length 156 #molecular-weight 18684 #checksum 8139 SEQUENCE /// ENTRY G65079 #type complete TITLE protein sprT - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS G65079 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65079 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-165 ##label BLAT !'##cross-references GB:AE000377; GB:U00096; NID:g2367178; !1PIDN:AAC75981.1; PID:g1789313; UWGP:b2944 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene sprT CLASSIFICATION #superfamily hypothetical protein HI1173 SUMMARY #length 165 #molecular-weight 19348 #checksum 6999 SEQUENCE /// ENTRY H69773 #type complete TITLE conserved hypothetical protein ydcK - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H69773 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69773 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-150 ##label KUN !'##cross-references GB:Z99106; GB:AL009126; NID:g2632653; !1PIDN:CAB12286.1; PID:g2632779 !'##experimental_source strain 168 GENETICS !$#gene ydcK CLASSIFICATION #superfamily hypothetical protein HI1173 SUMMARY #length 150 #molecular-weight 18067 #checksum 2650 SEQUENCE /// ENTRY B64040 #type complete TITLE hypothetical protein HI1680 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS B64040 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession B64040 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-718 ##label TIGR !'##cross-references GB:U32841; GB:L42023; NID:g1574529; !1PIDN:AAC23326.1; PID:g1574532; TIGR:HI1680 CLASSIFICATION #superfamily hypothetical protein HI1680 SUMMARY #length 718 #molecular-weight 82373 #checksum 9730 SEQUENCE /// ENTRY G64836 #type complete TITLE probable membrane protein yccS - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS G64836 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64836 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-720 ##label BLAT !'##cross-references GB:AE000198; GB:U00096; NID:g1787189; !1PIDN:AAC74046.1; PID:g1787194; UWGP:b0960 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yccS CLASSIFICATION #superfamily hypothetical protein HI1680 KEYWORDS transmembrane protein FEATURE !$41-57 #domain transmembrane #status predicted #label TM1\ !$70-86 #domain transmembrane #status predicted #label TM2\ !$93-109 #domain transmembrane #status predicted #label TM3\ !$116-132 #domain transmembrane #status predicted #label TM4\ !$397-413 #domain transmembrane #status predicted #label TM5\ !$445-461 #domain transmembrane #status predicted #label TM6\ !$469-485 #domain transmembrane #status predicted #label TM7\ !$490-506 #domain transmembrane #status predicted #label TM8\ !$517-533 #domain transmembrane #status predicted #label TM9\ !$687-703 #domain transmembrane #status predicted #label TM10 SUMMARY #length 720 #molecular-weight 82016 #checksum 781 SEQUENCE /// ENTRY S74695 #type complete TITLE hypothetical protein slr1298 - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S74695 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74695 !'##status preliminary !'##molecule_type DNA !'##residues 1-755 ##label KAN !'##cross-references EMBL:D90901; GB:AB001339; NID:g1651897; !1PIDN:BAA16846.1; PID:g1651920 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily hypothetical protein HI1680 SUMMARY #length 755 #molecular-weight 84275 #checksum 2716 SEQUENCE /// ENTRY B64041 #type complete TITLE hypothetical protein HI1730 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS B64041 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession B64041 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-309 ##label TIGR !'##cross-references GB:U32845; GB:L42023; NID:g3212236; !1PIDN:AAC23376.1; PID:g1574586; TIGR:HI1730 CLASSIFICATION #superfamily hypothetical protein HI1730 SUMMARY #length 309 #molecular-weight 34562 #checksum 8223 SEQUENCE /// ENTRY G64806 #type complete TITLE ybgK protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS G64806 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64806 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-310 ##label BLAT !'##cross-references GB:AE000174; GB:U00096; NID:g1786920; !1PIDN:AAC73806.1; PID:g1786930; UWGP:b0712 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ybgK CLASSIFICATION #superfamily hypothetical protein HI1730 SUMMARY #length 310 #molecular-weight 34386 #checksum 3144 SEQUENCE /// ENTRY G71090 #type complete TITLE hypothetical protein PH0988 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G71090 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession G71090 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-331 ##label KAW !'##cross-references GB:AP000004; NID:g3236131; PIDN:BAA30085.1; !1PID:g3257402 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0988 CLASSIFICATION #superfamily hypothetical protein HI1730 SUMMARY #length 331 #molecular-weight 36515 #checksum 9504 SEQUENCE /// ENTRY B70627 #type complete TITLE hypothetical protein Rv0263c - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B70627 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession B70627 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-300 ##label COL !'##cross-references GB:Z86089; GB:AL123456; NID:g3261711; !1PIDN:CAB06690.1; PID:g1850108 !'##experimental_source strain H37Rv GENETICS !$#gene Rv0263c CLASSIFICATION #superfamily hypothetical protein HI1730 SUMMARY #length 300 #molecular-weight 32203 #checksum 3216 SEQUENCE /// ENTRY C69516 #type complete TITLE hypothetical protein AF2131 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69516 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession C69516 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-329 ##label KLE !'##cross-references GB:AE000957; GB:AE000782; NID:g2689280; !1PIDN:AAB89128.1; PID:g2648404; TIGR:AF2131 CLASSIFICATION #superfamily hypothetical protein AF2131 SUMMARY #length 329 #molecular-weight 37066 #checksum 8687 SEQUENCE /// ENTRY B64047 #type complete TITLE acyl-CoA thiolesterase (EC 3.1.2.-) II - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS B64047 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession B64047 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-286 ##label TIGR !'##cross-references GB:U32693; GB:L42023; NID:g1573021; !1PIDN:AAC21752.1; PID:g1573025; TIGR:HI0076 GENETICS !$#gene tesB FUNCTION !$#description hydrolyzes a broad range of acyl-CoA thioesters CLASSIFICATION #superfamily acyl-CoA thiolesterase II KEYWORDS thiolester hydrolase FEATURE !$58 #active_site His #status predicted SUMMARY #length 286 #molecular-weight 32406 #checksum 3830 SEQUENCE /// ENTRY D64775 #type complete TITLE acyl-CoA thiolesterase (EC 3.1.2.-) II - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 09-Apr-1999 #sequence_revision 09-Apr-1999 #text_change 01-Mar-2002 ACCESSIONS D64775; JH0411; PS0216 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64775 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-286 ##label BLAT !'##cross-references GB:AE000151; GB:U00096; NID:g1786649; !1PIDN:AAC73555.1; PID:g1786657; UWGP:b0452 !'##experimental_source strain K-12, substrain MG1655 REFERENCE JH0411 !$#authors Naggert, J.; Narasimhan, M.L.; De Veaux, L.; Cho, H.; !1Randhawa, Z.I.; Cronan Jr., J.E.; Green, B.N.; Smith, S. !$#journal J. Biol. Chem. (1991) 266:11044-11050 !$#title Cloning, sequencing, and characterization of Escherichia !1coli thioesterase II. !$#cross-references MUID:91250410; PMID:1645722 !$#accession JH0411 !'##molecule_type DNA !'##residues 1-11,'QALYAAKETV',12-41,52-286 ##label NAG1 !'##cross-references GB:M63308; NID:g147931 !'##note the sequence in GenBank entry ECOTESB, release 109.0, !1(PID:g147932) does not have the transposed segment 42-51 !1shown in the published Fig. 2 !$#accession PS0216 !'##molecule_type protein !'##residues 2-7;56-63 ##label NAG2 GENETICS !$#gene tesB COMPLEX homotetramer FUNCTION !$#description hydrolyzes a broad range of acyl-CoA thioesters CLASSIFICATION #superfamily acyl-CoA thiolesterase II KEYWORDS homotetramer; thiolester hydrolase FEATURE !$2-286 #product thiolesterase II #status experimental #label !8MAT\ !$58 #active_site His #status experimental SUMMARY #length 286 #molecular-weight 31966 #checksum 9349 SEQUENCE /// ENTRY JC5644 #type complete TITLE acyl-CoA thiolesterase (EC 3.1.2.-) III, peroxisomal - human ALTERNATE_NAMES HIV Nef-binding protein CONTAINS palmitoyl-CoA hydrolase (EC 3.1.2.2) ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-May-2000 ACCESSIONS JC5644 REFERENCE JC5644 !$#authors Watanabe, H.; Shiratori, T.; Shoji, H.; Miyatake, S.; !1Okazaki, Y.; Ikuta, K.; Sato, T.; Saito, T. !$#journal Biochem. Biophys. Res. Commun. (1997) 238:234-239 !$#title A novel acyl-CoA thioesterase enhances its enzymatic !1activity by direct binding with HIV Nef. !$#cross-references MUID:97445158; PMID:9299485 !$#accession JC5644 !'##molecule_type mRNA !'##residues 1-319 ##label WAT !'##cross-references DDBJ:AF014404; NID:g2318124; PIDN:AAB71665.1; !1PID:g2318125 COMMENT This enzyme regulates membrane sorting and subcellular !1morphology. GENETICS !$#gene GDB:PTE1 !'##cross-references GDB:9954875 CLASSIFICATION #superfamily acyl-CoA thiolesterase II KEYWORDS coenzyme A; peroxisome; thiolester hydrolase FEATURE !$317-319 #region peroxisome/glyoxysome location signal !8(S-[RKH]-L) motif\ !$78 #active_site His #status predicted SUMMARY #length 319 #molecular-weight 35914 #checksum 9763 SEQUENCE /// ENTRY D70570 #type complete TITLE probable acyl-CoA thiolesterase II - Mycobacterium tuberculosis (strain H37RV) ALTERNATE_NAMES tesB2 protein ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D70570 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession D70570 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-281 ##label COL !'##cross-references GB:Z95387; GB:AL123456; NID:g3261763; !1PIDN:CAB08615.1; PID:g2104308 !'##experimental_source strain H37Rv GENETICS !$#gene tesB2 CLASSIFICATION #superfamily acyl-CoA thiolesterase II SUMMARY #length 281 #molecular-weight 31569 #checksum 8077 SEQUENCE /// ENTRY H70557 #type complete TITLE probable acyl-CoA thiolesterase (EC 3.1.2.-) II - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H70557 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession H70557 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-300 ##label COL !'##cross-references GB:Z95554; GB:AL123456; NID:g3261771; !1PIDN:CAB08895.1; PID:g2113902 !'##experimental_source strain H37Rv GENETICS !$#gene tesB1 CLASSIFICATION #superfamily acyl-CoA thiolesterase II KEYWORDS thiolester hydrolase SUMMARY #length 300 #molecular-weight 33172 #checksum 4858 SEQUENCE /// ENTRY S52763 #type complete TITLE hypothetical protein YJR019c - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein J1456 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S52763; S55209; S57034; S65928 REFERENCE S52762 !$#authors Hani, J.; Stumpf, G.; Domdey, H. !$#submission submitted to the EMBL Data Library, March 1995 !$#description PFT1 encodes an essential protein in Saccharomyces !1cerevisiae, which shows strong homology with a new putative !1family of PPIases. !$#accession S52763 !'##molecule_type DNA !'##residues 1-349 ##label HAN !'##cross-references EMBL:X85972; NID:g758283; PID:g758285 REFERENCE S55183 !$#authors de Haan, M.; Smits, P.H.M.; Grivell, L.A. !$#submission submitted to the EMBL Data Library, May 1995 !$#accession S55209 !'##molecule_type DNA !'##residues 1-349 ##label DEH !'##cross-references EMBL:X87611; NID:g854567; PID:g854594 REFERENCE S56771 !$#authors de Haan, M.; Grivell, L.A.; Smits, P.H.M. !$#submission submitted to the Protein Sequence Database, September 1995 !$#accession S57034 !'##molecule_type DNA !'##residues 1-349 ##label ZAG !'##cross-references EMBL:Z49519; NID:g1015654; PID:g1015655; !1GSPDB:GN00010; MIPS:YJR019c REFERENCE S65927 !$#authors Hani, J.; Stumpf, G.; Domdey, H. !$#journal FEBS Lett. (1995) 365:198-202 !$#title PTF1 encodes an essential protein in Saccharomyces !1cerevisiae, which shows strong homology with a new putative !1family of PPIases. !$#cross-references MUID:95300974; PMID:7781779 !$#accession S65928 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-349 ##label HAW !'##cross-references EMBL:X85972; NID:g758283; PIDN:CAA59960.1; !1PID:g758285 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1March 1995 GENETICS !$#gene SGD:TES1; MIPS:YJR019c !'##cross-references SGD:S0003780; MIPS:YJR019c !$#map_position 10R CLASSIFICATION #superfamily acyl-CoA thiolesterase II SUMMARY #length 349 #molecular-weight 40259 #checksum 9438 SEQUENCE /// ENTRY C70588 #type complete TITLE probable mbtE protein - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Nov-2000 ACCESSIONS C70588 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession C70588 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-1682 ##label COL !'##cross-references GB:Z95208; GB:AL123456; NID:g3261747; !1PIDN:CAB08481.1; PID:g3261749 !'##experimental_source strain H37Rv GENETICS !$#gene mbtE CLASSIFICATION #superfamily Mycobacterium tuberculosis mbtE protein; !1acetate-CoA ligase homology; acyl carrier protein homology KEYWORDS carrier protein; phosphopantetheine; phosphoprotein FEATURE !$485-923 #domain acetate-CoA ligase homology #label ACL\ !$939-1007 #domain acyl carrier protein homology #label ACP1\ !$1576-1643 #domain acyl carrier protein homology #label ACP2\ !$971,1608 #binding_site phosphopantetheine (Ser) (covalent) !8#status predicted SUMMARY #length 1682 #molecular-weight 183280 #checksum 3108 SEQUENCE /// ENTRY D69664 #type complete TITLE molybdenum cofactor biosynthesis protein narA - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 20-Oct-2000 ACCESSIONS D69664 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D69664 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-341 ##label KUN !'##cross-references GB:Z99122; GB:AL009126; NID:g2636029; !1PIDN:CAB15687.1; PID:g2636195 !'##experimental_source strain 168 GENETICS !$#gene narA CLASSIFICATION #superfamily Escherichia coli molybdopterin biosynthesis !1protein moaA SUMMARY #length 341 #molecular-weight 38549 #checksum 5564 SEQUENCE /// ENTRY E70487 #type complete TITLE molybdenum cofactor biosynthesis protein A - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 20-Oct-2000 ACCESSIONS E70487 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession E70487 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-320 ##label AQF !'##cross-references GB:AE000776; GB:AE000657; NID:g2984355; !1PIDN:AAC07877.1; PID:g2984358 !'##experimental_source strain VF5 GENETICS !$#gene moaA CLASSIFICATION #superfamily Escherichia coli molybdopterin biosynthesis !1protein moaA SUMMARY #length 320 #molecular-weight 37124 #checksum 2062 SEQUENCE /// ENTRY E70816 #type complete TITLE probable moaA2 protein - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 20-Oct-2000 ACCESSIONS E70816 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession E70816 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-360 ##label COL !'##cross-references GB:AL022004; GB:AL123456; NID:g3261550; !1PIDN:CAA17675.1; PID:g2916928 !'##experimental_source strain H37Rv GENETICS !$#gene moaA2 CLASSIFICATION #superfamily Escherichia coli molybdopterin biosynthesis !1protein moaA SUMMARY #length 360 #molecular-weight 38985 #checksum 2645 SEQUENCE /// ENTRY S75716 #type complete TITLE molybdenum cofactor biosynthesis protein A - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein slr0901 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 20-Oct-2000 ACCESSIONS S75716 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75716 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-327 ##label KAN !'##cross-references EMBL:D64003; GB:AB001339; NID:g1001200; !1PID:g1001211 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene moaA CLASSIFICATION #superfamily Escherichia coli molybdopterin biosynthesis !1protein moaA SUMMARY #length 327 #molecular-weight 37365 #checksum 7430 SEQUENCE /// ENTRY D70920 #type complete TITLE probable moaA protein - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 20-Oct-2000 ACCESSIONS D70920 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession D70920 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-359 ##label COL !'##cross-references GB:Z95150; GB:AL123456; NID:g3250708; !1PIDN:CAB08366.1; PID:g2076684 !'##experimental_source strain H37Rv GENETICS !$#gene moaA CLASSIFICATION #superfamily Escherichia coli molybdopterin biosynthesis !1protein moaA SUMMARY #length 359 #molecular-weight 39959 #checksum 3141 SEQUENCE /// ENTRY H64615 #type complete TITLE molybdenum cofactor biosynthesis protein A - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 20-Oct-2000 ACCESSIONS H64615 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession H64615 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-321 ##label TOM !'##cross-references GB:AE000589; GB:AE000511; NID:g2313895; !1PIDN:AAD07817.1; PID:g2313896; TIGR:HP0768 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily Escherichia coli molybdopterin biosynthesis !1protein moaA SUMMARY #length 321 #molecular-weight 36657 #checksum 793 SEQUENCE /// ENTRY B64136 #type complete TITLE molybdenum cofactor biosynthesis protein A - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 20-Oct-2000 ACCESSIONS B64136 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession B64136 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-337 ##label TIGR !'##cross-references GB:U32840; GB:L42023; NID:g1574518; !1PIDN:AAC23321.1; PID:g1574526; TIGR:HI1676 CLASSIFICATION #superfamily Escherichia coli molybdopterin biosynthesis !1protein moaA SUMMARY #length 337 #molecular-weight 38305 #checksum 603 SEQUENCE /// ENTRY S31879 #type complete TITLE molybdenum cofactor biosynthesis protein A - Escherichia coli (strain K-12) ALTERNATE_NAMES moaA protein ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS S31879; S34998; E64814 REFERENCE S31879 !$#authors Rivers, S.L.; McNairn, E.; Blasco, F.; Giordano, G.; Boxer, !1D.H. !$#submission submitted to the EMBL Data Library, February 1993 !$#description Molecular genetic analysis of the MOA operon of E. coli K12 !1required for molybdenum cofactor biosynthesis. !$#accession S31879 !'##molecule_type DNA !'##residues 1-329 ##label RIV !'##cross-references EMBL:X70420; NID:g42007; PID:g42008 !'##experimental_source strain K-12 REFERENCE S34998 !$#authors Rivers, S.L.; McNairn, E.; Blasco, F.; Giordano, G.; Boxer, !1D.H. !$#journal Mol. Microbiol. (1993) 8:1071-1081 !$#title Molecular genetic analysis of the moa operon of Escherichia !1coli K-12 required for molybdenum cofactor biosynthesis. !$#cross-references MUID:93368423; PMID:8361352 !$#accession S34998 !'##status preliminary !'##molecule_type DNA !'##residues 1-329 ##label RI2 !'##cross-references EMBL:X70420; NID:g42007; PIDN:CAA49861.1; !1PID:g42008 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64814 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-329 ##label BLAT !'##cross-references GB:AE000181; GB:U00096; NID:g1786998; !1PIDN:AAC73868.1; PID:g1786999; UWGP:b0781 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene moaA !$#map_position 18 min CLASSIFICATION #superfamily Escherichia coli molybdopterin biosynthesis !1protein moaA SUMMARY #length 329 #molecular-weight 37346 #checksum 5529 SEQUENCE /// ENTRY B64127 #type complete TITLE molybdenum transport protein molB homolog HI1525 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS B64127 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession B64127 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-245 ##label TIGR !'##cross-references GB:U32828; GB:L42023; NID:g1574362; !1PIDN:AAC23171.1; PID:g1574366; TIGR:HI1525 CLASSIFICATION #superfamily molybdate-binding periplasmic protein SUMMARY #length 245 #molecular-weight 26765 #checksum 6208 SEQUENCE /// ENTRY C64812 #type complete TITLE molybdate-binding periplasmic protein precursor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS C64812 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64812 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-257 ##label BLAT !'##cross-references GB:AE000179; GB:U00096; NID:g1786978; !1PIDN:AAC73850.1; PID:g1786979; UWGP:b0763 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene modA FUNCTION !$#description involved in transport of molybdenum into the cell CLASSIFICATION #superfamily molybdate-binding periplasmic protein FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-257 #product molybdate-binding periplasmic protein !8#status predicted #label MAT SUMMARY #length 257 #molecular-weight 27364 #checksum 3359 SEQUENCE /// ENTRY A64175 #type complete TITLE molybdate-binding periplasmic protein - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES protein HI1693 ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS A64175 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession A64175 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-254 ##label TIGR !'##cross-references GB:U32842; GB:L42023; NID:g1574541; !1PIDN:AAC23339.1; PID:g1574546; TIGR:HI1693 !'##experimental_source strain Rd KW20 GENETICS !$#gene modA FUNCTION !$#description involved in transport of molybdenum into the cell CLASSIFICATION #superfamily molybdate-binding periplasmic protein SUMMARY #length 254 #molecular-weight 27302 #checksum 245 SEQUENCE /// ENTRY S31044 #type complete TITLE molybdenum transport protein molB - Azotobacter vinelandii ORGANISM #formal_name Azotobacter vinelandii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S31044; S28075 REFERENCE S30947 !$#authors Luque, F.; Mitchenall, L.A.; Chapman, M.; Christine, R.; !1Pau, R.N. !$#journal Mol. Microbiol. (1993) 7:447-459 !$#title Characterization of genes involved in molybdenum transport !1in Azotobacter vinelandii. !$#cross-references MUID:93211287; PMID:8384683 !$#accession S31044 !'##molecule_type DNA !'##residues 1-252 ##label LUQ !'##cross-references EMBL:X69077; NID:g49177; PIDN:CAA48820.1; !1PID:g49179 GENETICS !$#gene molB; modB FUNCTION !$#description involved in molybdenum transport CLASSIFICATION #superfamily molybdate-binding periplasmic protein SUMMARY #length 252 #molecular-weight 26284 #checksum 421 SEQUENCE /// ENTRY E36914 #type complete TITLE molybdate-binding protein homolog ModA - Rhodobacter capsulatus ORGANISM #formal_name Rhodobacter capsulatus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E36914 REFERENCE A36914 !$#authors Wang, G.; Angermuller, S.; Klipp, W. !$#journal J. Bacteriol. (1993) 175:3031-3042 !$#title Characterization of Rhodobacter capsulatus genes encoding a !1molybdenum transport system and putative !1molybdenum-pterin-binding proteins. !$#cross-references MUID:93259949; PMID:8491722 !$#accession E36914 !'##status preliminary !'##molecule_type DNA !'##residues 1-252 ##label WAN !'##cross-references GB:L06254; NID:g310272; PIDN:AAA71911.1; !1PID:g310276 !'##note sequence extracted from NCBI backbone (NCBIN:131915, !1NCBIP:131920) CLASSIFICATION #superfamily molybdate-binding periplasmic protein SUMMARY #length 252 #molecular-weight 26620 #checksum 1612 SEQUENCE /// ENTRY S77085 #type complete TITLE molybdate-binding periplasmic protein modA - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein sll0738 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S77085 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S77085 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-270 ##label KAN !'##cross-references EMBL:D64005; GB:AB001339; NID:g1001779; !1PID:g1006621 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene modA CLASSIFICATION #superfamily molybdate-binding periplasmic protein SUMMARY #length 270 #molecular-weight 29156 #checksum 1676 SEQUENCE /// ENTRY A64579 #type complete TITLE molybdenum ABC transporter, periplasmic molybdate-binding protein - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS A64579 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession A64579 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-246 ##label TOM !'##cross-references GB:AE000562; GB:AE000511; NID:g2313581; !1PIDN:AAD07541.1; PID:g2313584; TIGR:HP0473 CLASSIFICATION #superfamily molybdate-binding periplasmic protein SUMMARY #length 246 #molecular-weight 27594 #checksum 2217 SEQUENCE /// ENTRY A70040 #type complete TITLE molybdate-binding protein homolog yvgL - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A70040 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A70040 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-260 ##label KUN !'##cross-references GB:Z99121; GB:AL009126; NID:g2635827; !1PIDN:CAB15343.1; PID:g2635851 !'##experimental_source strain 168 GENETICS !$#gene yvgL CLASSIFICATION #superfamily molybdate-binding periplasmic protein SUMMARY #length 260 #molecular-weight 28355 #checksum 9355 SEQUENCE /// ENTRY G69223 #type complete TITLE molybdate-binding periplasmic protein - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69223 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession G69223 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-260 ##label MTH !'##cross-references GB:AE000867; GB:AE000666; NID:g2622009; !1PIDN:AAB85422.1; PID:g2622021 !'##experimental_source strain Delta H GENETICS !$#gene MTH924 CLASSIFICATION #superfamily molybdate-binding periplasmic protein SUMMARY #length 260 #molecular-weight 28359 #checksum 2282 SEQUENCE /// ENTRY B70439 #type complete TITLE molybdate periplasmic binding protein - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B70439 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession B70439 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-240 ##label AQF !'##cross-references GB:AE000747; GB:AE000657; NID:g2983944; !1PIDN:AAC07501.1; PID:g2983953 !'##experimental_source strain VF5 GENETICS !$#gene modA CLASSIFICATION #superfamily molybdate-binding periplasmic protein SUMMARY #length 240 #molecular-weight 26889 #checksum 2365 SEQUENCE /// ENTRY JC6038 #type complete TITLE probable molybdenum transport protein modF - Escherichia coli (strain K-12) ALTERNATE_NAMES photorepair protein phrA ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS JC6038; H64811; I60601; S32737 REFERENCE JC6037 !$#authors Grunden, A.M.; Ray, R.M.; Rosentel, J.K.; Healy, F.G.; !1Shanmugam, K.T. !$#journal J. Bacteriol. (1996) 178:735-744 !$#title Repression of the Escherichia coli modABCD (molybdate !1transport) operon by ModE. !$#cross-references MUID:96146523; PMID:8550508 !$#accession JC6038 !'##molecule_type DNA !'##residues 1-490 ##label GRU !'##cross-references GB:U27192; NID:g973213; PID:g973219 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64811 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-490 ##label BLAT !'##cross-references GB:AE000178; GB:U00096; NID:g1786967; !1PIDN:AAC73847.1; PID:g1786975; UWGP:b0760 !'##experimental_source strain K-12, substrain MG1655 REFERENCE I60601 !$#authors Dorrell, N.; Ahmed, A.H.; Moss, S.H. !$#journal Photochem. Photobiol. (1993) 58:831-835 !$#title Photoreactivation in a phrB mutant of Escherichia coli K-12: !1evidence for the role of a second protein in photorepair. !$#cross-references MUID:94143420; PMID:8310005 !$#accession I60601 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 151-319,'A',321,'R',323-324,'A',326-490 ##label RES !'##cross-references EMBL:X69182; NID:g296234; PIDN:CAA48926.1; !1PID:g296235 !'##experimental_source K-12 strain C600; cell line JM83/pND01 GENETICS !$#gene modF; phrA !$#map_position 17 min CLASSIFICATION #superfamily Escherichia coli probable molybdenum transport !1protein modF; ATP-binding cassette homology KEYWORDS ATP; DNA repair; GTP binding; nucleotide binding; P-loop; !1transport protein FEATURE !$19-211 #domain ATP-binding cassette homology #label ABC1\ !$36-43 #region nucleotide-binding motif A (P-loop)\ !$276-479 #domain ATP-binding cassette homology #label ABC2\ !$293-300 #region nucleotide-binding motif A (P-loop) SUMMARY #length 490 #molecular-weight 54535 #checksum 2387 SEQUENCE /// ENTRY C70325 #type complete TITLE conserved hypothetical protein aq_274 - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C70325 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession C70325 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-228 ##label AQF !'##cross-references GB:AE000681; GB:AE000657; NID:g2982963; !1PIDN:AAC06592.1; PID:g2982978 !'##experimental_source strain VF5 GENETICS !$#gene aq_274 CLASSIFICATION #superfamily conserved hypothetical protein HI0090 SUMMARY #length 228 #molecular-weight 26339 #checksum 1978 SEQUENCE /// ENTRY E69876 #type complete TITLE conserved hypothetical protein ylmE - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69876 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69876 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-230 ##label KUN !'##cross-references GB:Z99112; GB:AL009126; NID:g2633902; !1PIDN:CAB13412.1; PID:g2633911 !'##experimental_source strain 168 GENETICS !$#gene ylmE CLASSIFICATION #superfamily conserved hypothetical protein HI0090 SUMMARY #length 230 #molecular-weight 25704 #checksum 1665 SEQUENCE /// ENTRY B64142 #type complete TITLE hypothetical protein HI0090 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS B64142 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession B64142 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-237 ##label TIGR !'##cross-references GB:U32694; GB:L42023; NID:g1573035; !1PIDN:AAC21768.1; PID:g1573041; TIGR:HI0090 !'##note best homolog was a hypothetical protein from Pseudomonas !1aeruginosa CLASSIFICATION #superfamily conserved hypothetical protein HI0090 SUMMARY #length 237 #molecular-weight 26766 #checksum 2881 SEQUENCE /// ENTRY JN0060 #type complete TITLE hypothetical 24.5K protein (pilT region) - Pseudomonas aeruginosa ORGANISM #formal_name Pseudomonas aeruginosa DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 31-Dec-2000 ACCESSIONS JN0060; PQ0052; A83598 REFERENCE JN0055 !$#authors Whitchurch, C.B.; Hobbs, M.; Livingston, S.P.; !1Krishnapillai, V.; Mattick, J.S. !$#journal Gene (1991) 101:33-44 !$#title Characterisation of a Pseudomonas aeruginosa twitching !1motility gene and evidence for a specialised protein export !1system widespread in eubacteria. !$#cross-references MUID:91285432; PMID:1676385 !$#accession JN0060 !'##molecule_type DNA !'##residues 1-230 ##label WHI !'##cross-references GB:M55524; NID:g151483; PIDN:AAA25959.1; !1PID:g454838 REFERENCE JQ0418 !$#authors Savioz, A.; Jeenes, D.J.; Kocher, H.P.; Haas, D. !$#journal Gene (1990) 86:107-111 !$#title Comparison of proC and other housekeeping genes of !1Pseudomonas aeruginosa with their counterparts in !1Escherichia coli. !$#cross-references MUID:90185238; PMID:2107123 !$#accession PQ0052 !'##molecule_type DNA !'##residues 202-230 ##label SAV REFERENCE A82950 !$#authors Stover, C.K.; Pham, X.Q.; Erwin, A.L.; Mizoguchi, S.D.; !1Warrener, P.; Hickey, M.J.; Brinkman, F.S.L.; Hufnagle, !1W.O.; Kowalik, D.J.; Lagrou, M.; Garber, R.L.; Goltry, L.; !1Tolentino, E.; Westbrook-Wadman, S.; Yuan, Y.; Brody, L.L.; !1Coulter, S.N.; Folger, K.R.; Kas, A.; Larbig, K.; Lim, R.M.; !1Smith, K.A.; Spencer, D.H.; Wong, G.K.S.; Wu, Z.; Paulsen, !1I.T.; Reizer, J.; Saier, M.H.; Hancock, R.E.W.; Lory, S.; !1Olson, M.V. !$#journal Nature (2000) 406:959-964 !$#title Complete genome sequence of Pseudomonas aeruginosa PA01, an !1opportunistic pathogen. !$#cross-references MUID:20437337; PMID:10984043 !$#accession A83598 !'##status preliminary !'##molecule_type DNA !'##residues 1-230 ##label STO !'##cross-references GB:AE004476; GB:AE004091; NID:g9946234; !1PIDN:AAG03783.1; GSPDB:GN00131; PASP:PA0394 !'##experimental_source strain PAO1 GENETICS !$#gene PA0394 CLASSIFICATION #superfamily conserved hypothetical protein HI0090 SUMMARY #length 230 #molecular-weight 24505 #checksum 4648 SEQUENCE /// ENTRY F65080 #type complete TITLE hypothetical protein b2951 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS F65080 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65080 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-234 ##label BLAT !'##cross-references GB:AE000378; GB:U00096; NID:g1789319; !1PIDN:AAC75988.1; PID:g1789321; UWGP:b2951 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily conserved hypothetical protein HI0090 SUMMARY #length 234 #molecular-weight 25787 #checksum 5065 SEQUENCE /// ENTRY C64569 #type complete TITLE conserved hypothetical protein HP0395 - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS C64569 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession C64569 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-222 ##label TOM !'##cross-references GB:AE000555; GB:AE000511; NID:g2313485; !1PIDN:AAD07459.1; PID:g2313495; TIGR:HP0395 CLASSIFICATION #superfamily conserved hypothetical protein HI0090 SUMMARY #length 222 #molecular-weight 25011 #checksum 15 SEQUENCE /// ENTRY S76030 #type complete TITLE hypothetical protein - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S76030 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76030 !'##status preliminary !'##molecule_type DNA !'##residues 1-218 ##label KAN !'##cross-references EMBL:D64006; GB:AB001339; NID:g1001291; !1PID:g1001387 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily conserved hypothetical protein HI0090 SUMMARY #length 218 #molecular-weight 24038 #checksum 5886 SEQUENCE /// ENTRY S50294 #type complete TITLE hypothetical protein YBL036c - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein YBL0413 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S50294; S45770; S42508 REFERENCE S50284 !$#authors de Wergifosse, P.; Jacques, B.; Jonniaux, J.L.; Purnelle, !1B.; Skala, J.; Goffeau, A. !$#journal Yeast (1994) 10:1489-1496 !$#title The sequence of a 22.4 kb DNA fragment from the left arm of !1yeast chromosome II reveals homologues to bacterial proline !1synthetase and murine alpha-adaptin, as well as a new !1permease and a DNA-binding protein. !$#cross-references MUID:95176707; PMID:7871888 !$#accession S50294 !'##molecule_type DNA !'##residues 1-257 ##label DEW !'##cross-references EMBL:X78214; NID:g463261; PIDN:CAA55058.1; !1PID:g463272 REFERENCE S45745 !$#authors Goffeau, A.; Jonniaux, J.L.; Purnelle, B.; Skala, J.; de !1Wergifosse, P.; van Dyck, L. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S45770 !'##molecule_type DNA !'##residues 1-257 ##label GOF !'##cross-references EMBL:Z35797; NID:g536046; PID:g536047; !1GSPDB:GN00002; MIPS:YBL036c GENETICS !$#gene MIPS:YBL036c !'##cross-references SGD:S0000132 !$#map_position 2L CLASSIFICATION #superfamily conserved hypothetical protein HI0090 SUMMARY #length 257 #molecular-weight 29123 #checksum 2439 SEQUENCE /// ENTRY B64921 #type complete TITLE conserved hypothetical protein b1640 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS B64921 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64921 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-369 ##label BLAT !'##cross-references GB:AE000259; GB:U00096; NID:g1787921; !1PIDN:AAC74712.1; PID:g1787928; UWGP:b1640 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily hypothetical protein HI0753 SUMMARY #length 369 #molecular-weight 39496 #checksum 2437 SEQUENCE /// ENTRY B64158 #type complete TITLE hypothetical protein HI0753 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS B64158 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession B64158 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-382 ##label TIGR !'##cross-references GB:U32759; GB:L42023; NID:g1573756; !1PIDN:AAC22412.1; PID:g1573761; TIGR:HI0753 !'##note best homolog was a hypothetical protein from Yersinia !1enterocolitica CLASSIFICATION #superfamily hypothetical protein HI0753 SUMMARY #length 382 #molecular-weight 42026 #checksum 6423 SEQUENCE /// ENTRY S76913 #type complete TITLE hypothetical protein - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S76913 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76913 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-376 ##label KAN !'##cross-references EMBL:D90917; GB:AB001339; NID:g1653836; !1PIDN:BAA18825.1; PID:g1653915 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily hypothetical protein HI0753 SUMMARY #length 376 #molecular-weight 41357 #checksum 8797 SEQUENCE /// ENTRY B64176 #type complete TITLE hypothetical protein HI1714 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS B64176 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession B64176 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-346 ##label TIGR !'##cross-references GB:U32844; GB:L42023; NID:g1574563; !1PIDN:AAC23359.1; PID:g1574569; TIGR:HI1714 !'##note best homolog was a hypothetical protein from Escherichia coli CLASSIFICATION #superfamily conserved hypothetical protein HI1714 SUMMARY #length 346 #molecular-weight 38886 #checksum 256 SEQUENCE /// ENTRY S56389 #type complete TITLE hypothetical 37.7K protein (psd-amiB intergenic region) - Escherichia coli (strain K-12) ALTERNATE_NAMES hypothetical protein f337 ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS S56389; G65226 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56389 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-337 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97060.1; !1PID:g537005 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65226 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-337 ##label BLAT !'##cross-references GB:AE000488; GB:U00096; NID:g2367354; !1PIDN:AAC77121.1; PID:g1790605; UWGP:b4161 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yjeQ !$#start_codon GTG CLASSIFICATION #superfamily conserved hypothetical protein HI1714 SUMMARY #length 337 #molecular-weight 37682 #checksum 7306 SEQUENCE /// ENTRY A69879 #type complete TITLE conserved hypothetical protein yloQ - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A69879 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69879 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-298 ##label KUN !'##cross-references GB:Z99112; GB:AL009126; NID:g2633902; !1PIDN:CAB13451.1; PID:g2633950 !'##experimental_source strain 168 GENETICS !$#gene yloQ CLASSIFICATION #superfamily conserved hypothetical protein HI1714 SUMMARY #length 298 #molecular-weight 33797 #checksum 6283 SEQUENCE /// ENTRY C70112 #type complete TITLE conserved hypothetical protein BB0099 - Lyme disease spirochete ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C70112 REFERENCE A70100 !$#authors Fraser, C.M.; Casjens, S.; Huang, W.M.; Sutton, G.G.; !1Clayton, R.; Lathigra, R.; White, O.; Ketchum, K.A.; Dodson, !1R.; Hickey, E.K.; Gwinn, M.; Dougherty, B.; Tomb, J.F.; !1Fleischmann, R.D.; Richardson, D.; Peterson, J.; Kerlavage, !1A.R.; Quackenbush, J.; Salzberg, S.; Hanson, M.; Vugt, R.V.; !1Palmer, N.; Adams, M.D.; Gocayne, J.; Weidman, J.; !1Utterback, T.; Watthey, L.; McDonald, L.; Artiach, P.; !1Bowman, C.; Garland, S.; Fujii, C.; Cotton, M.D.; Horst, K.; !1Roberts, K.; Hatch, B.; Smith, H.O.; Venter, J.C. !$#journal Nature (1997) 390:580-586 !$#title Genomic sequence of a Lyme disease spirochaete, Borrelia !1burgdorferi. !$#cross-references MUID:98065943; PMID:9403685 !$#accession C70112 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-307 ##label KLE !'##cross-references GB:AE001122; GB:AE000783; NID:g2687974; !1PIDN:AAC66480.1; PID:g2687976; TIGR:BB0099 !'##experimental_source strain B31 CLASSIFICATION #superfamily conserved hypothetical protein HI1714 SUMMARY #length 307 #molecular-weight 35256 #checksum 6898 SEQUENCE /// ENTRY S76011 #type complete TITLE hypothetical protein - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S76011 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76011 !'##status preliminary !'##molecule_type DNA !'##residues 1-369 ##label KAN !'##cross-references EMBL:D64006; GB:AB001339; NID:g1001291; !1PID:g1001369 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily conserved hypothetical protein HI1714 SUMMARY #length 369 #molecular-weight 41890 #checksum 7973 SEQUENCE /// ENTRY F70590 #type complete TITLE hypothetical protein Rv3228 - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F70590 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession F70590 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-330 ##label COL !'##cross-references GB:Z95121; GB:AL123456; NID:g3261742; !1PIDN:CAB08329.1; PID:g2072695 !'##experimental_source strain H37Rv GENETICS !$#gene Rv3228 CLASSIFICATION #superfamily conserved hypothetical protein HI1714 SUMMARY #length 330 #molecular-weight 34875 #checksum 5196 SEQUENCE /// ENTRY S73909 #type complete TITLE hypothetical protein yjeQ homolog K04_orf278L - Mycoplasma pneumoniae (strain ATCC 29342) ALTERNATE_NAMES hypothetical protein K04_orf278L ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 10-Dec-1999 ACCESSIONS S73909 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73909 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-278 ##label HIM !'##cross-references EMBL:AE000057; GB:U00089; NID:g1674279; !1PIDN:AAB96231.1; PID:g1674284 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#gene yjeQ !$#genetic_code SGC3 !$#start_codon TTG CLASSIFICATION #superfamily conserved hypothetical protein HI1714 SUMMARY #length 278 #molecular-weight 31567 #checksum 5220 SEQUENCE /// ENTRY B64212 #type complete TITLE hypothetical protein MG110 - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 07-Dec-1999 ACCESSIONS B64212; S18698 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession B64212 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-236 ##label TIGR !'##cross-references GB:U39690; GB:L43967; NID:g1045782; PID:g1045789; !1TIGR:MG110 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily conserved hypothetical protein HI1714 SUMMARY #length 236 #molecular-weight 27196 #checksum 2871 SEQUENCE /// ENTRY I69653 #type complete TITLE UDPgalactopyranose mutase (EC 5.4.99.9) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS I69653; I69643; C64969 REFERENCE I55054 !$#authors Stevenson, G.; Neal, B.; Liu, D.; Hobbs, M.; Packer, N.H.; !1Batley, M.; Redmond, J.W.; Lindquist, L.; Reeves, P. !$#journal J. Bacteriol. (1994) 176:4144-4156 !$#title Structure of the O antigen of Escherichia coli K-12 and the !1sequence of its rfb gene cluster. !$#cross-references MUID:94292435; PMID:7517391 !$#accession I69653 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-367 ##label RES !'##cross-references EMBL:U09876; NID:g2665488; PIDN:AAB88403.1; !1PID:g508242 REFERENCE I55053 !$#authors Yao, Z.; Valvano, M.A. !$#journal J. Bacteriol. (1994) 176:4133-4143 !$#title Genetic analysis of the O-specific lipopolysaccharide !1biosynthesis region (rfb) of Escherichia coli K-12 W3110: !1identification of genes that confer group 6 specificity to !1Shigella flexneri serotypes Y and 4a. !$#cross-references MUID:94292434; PMID:7517390 !$#accession I69643 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-367 ##label RE2 !'##cross-references EMBL:U03041; NID:g501028; PIDN:AAC31632.1; !1PID:g510253 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64969 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-367 ##label BLAT !'##cross-references GB:AE000294; GB:U00096; NID:g1788338; !1PIDN:AAC75097.1; PID:g1788348; UWGP:b2036 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yefE !$#map_position 45 min CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum !1UDP-galactopyranose mutase KEYWORDS intramolecular transferase; isomerase SUMMARY #length 367 #molecular-weight 42966 #checksum 3495 SEQUENCE /// ENTRY E70888 #type complete TITLE probable glf protein - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E70888 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession E70888 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-399 ##label COL !'##cross-references GB:AL022076; GB:AL123456; NID:g3256026; !1PIDN:CAA17873.1; PID:g2950428 !'##experimental_source strain H37Rv GENETICS !$#gene glf CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum !1UDP-galactopyranose mutase SUMMARY #length 399 #molecular-weight 45814 #checksum 1412 SEQUENCE /// ENTRY C69144 #type complete TITLE UDP-galactopyranose mutase - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69144 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession C69144 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-380 ##label MTH !'##cross-references GB:AE000819; GB:AE000666; NID:g2621396; !1PIDN:AAB84850.1; PID:g2621401 !'##experimental_source strain Delta H GENETICS !$#gene MTH344 CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum !1UDP-galactopyranose mutase SUMMARY #length 380 #molecular-weight 44660 #checksum 5865 SEQUENCE /// ENTRY B64215 #type complete TITLE probable dTDP-4-dehydrorhamnose reductase - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 07-Dec-1999 ACCESSIONS B64215 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession B64215 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-404 ##label TIGR !'##cross-references GB:U39692; GB:L43967; NID:g1045812; PID:g1045818; !1TIGR:MG137 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 !$#start_codon GTG CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum !1UDP-galactopyranose mutase SUMMARY #length 404 #molecular-weight 46661 #checksum 4704 SEQUENCE /// ENTRY S73883 #type complete TITLE yefE protein homolog A65_orf399V - Mycoplasma pneumoniae (strain ATCC 29342) ALTERNATE_NAMES hypothetical protein A65_orf399V ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S73883 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73883 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-399 ##label HIM !'##cross-references EMBL:AE000055; GB:U00089; NID:g1674254; !1PIDN:AAB96205.1; PID:g1674256 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#genetic_code SGC3 !$#start_codon GTG CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum !1UDP-galactopyranose mutase SUMMARY #length 399 #molecular-weight 45910 #checksum 4973 SEQUENCE /// ENTRY B70477 #type complete TITLE conserved hypothetical protein aq_2066 - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B70477 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession B70477 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-156 ##label AQF !'##cross-references GB:AE000771; GB:AE000657; NID:g2984286; !1PIDN:AAC07821.1; PID:g2984297 !'##experimental_source strain VF5 GENETICS !$#gene aq_2066 CLASSIFICATION #superfamily conserved hypothetical protein MJ0201 SUMMARY #length 156 #molecular-weight 17088 #checksum 5425 SEQUENCE /// ENTRY B64325 #type complete TITLE hypothetical protein MJ0201 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B64325 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession B64325 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-160 ##label BUL !'##cross-references GB:U67476; GB:L77117; NID:g1590942; !1PIDN:AAB98185.1; PID:g1498976; TIGR:MJ0201 GENETICS !$#map_position REV193486-193004 CLASSIFICATION #superfamily conserved hypothetical protein MJ0201 SUMMARY #length 160 #molecular-weight 18626 #checksum 1615 SEQUENCE /// ENTRY E64087 #type complete TITLE lipoprotein B - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS E64087; T09408 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession E64087 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-192 ##label TIGR !'##cross-references GB:U32753; GB:L42023; NID:g1573701; !1PIDN:AAC22362.1; PID:g1573705; TIGR:HI0703 GENETICS !$#gene HI0703 CLASSIFICATION #superfamily conserved hypothetical protein MJ0201 SUMMARY #length 192 #molecular-weight 21688 #checksum 5017 SEQUENCE /// ENTRY B64326 #type complete TITLE hypothetical protein MJ0209 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Dec-2002 ACCESSIONS B64326 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession B64326 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-266 ##label BUL !'##cross-references GB:U67476; GB:L77117; NID:g1590942; !1PIDN:AAB98192.1; PID:g1498984; TIGR:MJ0209 GENETICS !$#map_position REV200956-200156 CLASSIFICATION #superfamily uncharacterized conserved protein SUMMARY #length 266 #molecular-weight 29853 #checksum 2981 SEQUENCE /// ENTRY A71022 #type complete TITLE hypothetical protein PH1470 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Dec-2002 ACCESSIONS A71022 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession A71022 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-280 ##label KAW !'##cross-references GB:AP000006; NID:g3236133; PIDN:BAA30577.1; !1PID:g3257894 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1470 CLASSIFICATION #superfamily uncharacterized conserved protein SUMMARY #length 280 #molecular-weight 32106 #checksum 6140 SEQUENCE /// ENTRY G69156 #type complete TITLE conserved hypothetical protein MTH435 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Dec-2002 ACCESSIONS G69156 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession G69156 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-248 ##label MTH !'##cross-references GB:AE000827; GB:AE000666; NID:g2621489; !1PIDN:AAB84941.1; PID:g2621500 !'##experimental_source strain Delta H GENETICS !$#gene MTH435 CLASSIFICATION #superfamily uncharacterized conserved protein SUMMARY #length 248 #molecular-weight 27462 #checksum 1112 SEQUENCE /// ENTRY G69365 #type complete TITLE conserved hypothetical protein AF0927 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Dec-2002 ACCESSIONS G69365 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession G69365 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-188 ##label KLE !'##cross-references GB:AE001040; GB:AE000782; NID:g2689363; !1PIDN:AAB90316.1; PID:g2649675; TIGR:AF0927 CLASSIFICATION #superfamily uncharacterized conserved protein SUMMARY #length 188 #molecular-weight 21187 #checksum 6470 SEQUENCE /// ENTRY B64328 #type complete TITLE conserved hypothetical protein MJ0225 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B64328 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession B64328 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-263 ##label BUL !'##cross-references GB:U67478; GB:L77117; NID:g1590958; !1PIDN:AAB98210.1; PID:g1590962; TIGR:MJ0225 GENETICS !$#map_position FOR215452-216243 !$#start_codon GTG CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0225 SUMMARY #length 263 #molecular-weight 30984 #checksum 2936 SEQUENCE /// ENTRY F71233 #type complete TITLE hypothetical protein PH0128 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F71233 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession F71233 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-253 ##label KAW !'##cross-references GB:AP000001; NID:g3236128; PIDN:BAA29197.1; !1PID:g3256514 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0128 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0225 SUMMARY #length 253 #molecular-weight 29057 #checksum 4941 SEQUENCE /// ENTRY G69109 #type complete TITLE conserved hypothetical protein MTH1816 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69109 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession G69109 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-253 ##label MTH !'##cross-references GB:AE000935; GB:AE000666; NID:g2622945; !1PIDN:AAB86282.1; PID:g2622949 !'##experimental_source strain Delta H GENETICS !$#gene MTH1816 !$#start_codon GTG CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0225 SUMMARY #length 253 #molecular-weight 28975 #checksum 3714 SEQUENCE /// ENTRY A64451 #type complete TITLE probable 3-isopropylmalate dehydratase - Methanococcus jannaschii ALTERNATE_NAMES hypothetical protein MJ1210 ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A64451 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession A64451 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-258 ##label BUL !'##cross-references GB:U67562; GB:L77117; NID:g2826374; !1PIDN:AAB99213.1; PID:g1591839; TIGR:MJ1210 GENETICS !$#map_position REV1154923-1154147 !$#start_codon GTG CLASSIFICATION #superfamily 3-isopropylmalate dehydratase leuD chain SUMMARY #length 258 #molecular-weight 28707 #checksum 4804 SEQUENCE /// ENTRY E69040 #type complete TITLE probable 3-isopropylmalate dehydratase - Methanobacterium thermoautotrophicum (strain Delta H) ALTERNATE_NAMES conserved hypothetical protein MTH1306 ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69040 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession E69040 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-189 ##label MTH !'##cross-references GB:AE000895; GB:AE000666; NID:g2622403; !1PIDN:AAB85784.1; PID:g2622411 !'##experimental_source strain Delta H GENETICS !$#gene MTH1306 CLASSIFICATION #superfamily 3-isopropylmalate dehydratase leuD chain SUMMARY #length 189 #molecular-weight 20939 #checksum 3477 SEQUENCE /// ENTRY E69315 #type complete TITLE probable 3-isopropylmalate dehydratase - Archaeoglobus fulgidus ALTERNATE_NAMES conserved hypothetical protein AF0525 ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69315 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession E69315 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-259 ##label KLE !'##cross-references GB:AE001068; GB:AE000782; NID:g2689391; !1PIDN:AAB90711.1; PID:g2650098; TIGR:AF0525 CLASSIFICATION #superfamily 3-isopropylmalate dehydratase leuD chain SUMMARY #length 259 #molecular-weight 28470 #checksum 9031 SEQUENCE /// ENTRY B64313 #type complete TITLE probable 3-isopropylmalate dehydratase - Methanococcus jannaschii ALTERNATE_NAMES conserved hypothetical protein MJ0106 ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B64313 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession B64313 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-238 ##label BUL !'##cross-references GB:U67468; GB:L77117; NID:g1590882; !1PIDN:AAB98088.1; PID:g1590883; TIGR:MJ0106 GENETICS !$#map_position REV102553-101837 !$#start_codon TTG CLASSIFICATION #superfamily 3-isopropylmalate dehydratase leuD chain SUMMARY #length 238 #molecular-weight 26473 #checksum 7921 SEQUENCE /// ENTRY C69040 #type complete TITLE probable 3-isopropylmalate dehydratase - Methanobacterium thermoautotrophicum (strain Delta H) ALTERNATE_NAMES conserved hypothetical protein MTH1302 ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69040 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession C69040 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-237 ##label MTH !'##cross-references GB:AE000895; GB:AE000666; NID:g2622403; !1PIDN:AAB85782.1; PID:g2622409 !'##experimental_source strain Delta H GENETICS !$#gene MTH1302 CLASSIFICATION #superfamily 3-isopropylmalate dehydratase leuD chain SUMMARY #length 237 #molecular-weight 25962 #checksum 7837 SEQUENCE /// ENTRY B69406 #type complete TITLE probable 3-isopropylmalate dehydratase - Archaeoglobus fulgidus ALTERNATE_NAMES conserved hypothetical protein AF1251 ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69406 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession B69406 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-239 ##label KLE !'##cross-references GB:AE001018; GB:AE000782; NID:g2689341; !1PIDN:AAB89995.1; PID:g2649332; TIGR:AF1251 CLASSIFICATION #superfamily 3-isopropylmalate dehydratase leuD chain SUMMARY #length 239 #molecular-weight 26217 #checksum 3591 SEQUENCE /// ENTRY D71233 #type complete TITLE probable 3-isopropylmalate dehydratase - Pyrococcus horikoshii ALTERNATE_NAMES hypothetical protein PH0126 ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D71233 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession D71233 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-241 ##label KAW !'##cross-references GB:AP000001; NID:g3236128; PIDN:BAA29195.1; !1PID:g3256512 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0126 CLASSIFICATION #superfamily 3-isopropylmalate dehydratase leuD chain SUMMARY #length 241 #molecular-weight 27003 #checksum 7549 SEQUENCE /// ENTRY B64347 #type complete TITLE hypothetical protein MJ0378 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B64347 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession B64347 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-322 ##label BUL !'##cross-references GB:U67490; GB:L77117; NID:g2826276; !1PIDN:AAB98367.1; PID:g1499166; TIGR:MJ0378 GENETICS !$#map_position FOR343921-344889 CLASSIFICATION #superfamily conserved hypothetical protein MJ0378 SUMMARY #length 322 #molecular-weight 38147 #checksum 6481 SEQUENCE /// ENTRY D69554 #type complete TITLE conserved hypothetical protein AF2435 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69554 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession D69554 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-322 ##label KLE !'##cross-references GB:AE001107; GB:AE000782; NID:g2689430; !1PIDN:AAB91228.1; PID:g2650654; TIGR:AF2435 CLASSIFICATION #superfamily conserved hypothetical protein MJ0378 SUMMARY #length 322 #molecular-weight 37261 #checksum 9125 SEQUENCE /// ENTRY A69011 #type complete TITLE conserved hypothetical protein MTH1084 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A69011 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession A69011 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-334 ##label MTH !'##cross-references GB:AE000879; GB:AE000666; NID:g2622175; !1PIDN:AAB85573.1; PID:g2622184 !'##experimental_source strain Delta H GENETICS !$#gene MTH1084 !$#start_codon TTG CLASSIFICATION #superfamily conserved hypothetical protein MJ0378 SUMMARY #length 334 #molecular-weight 38817 #checksum 9533 SEQUENCE /// ENTRY G71068 #type complete TITLE hypothetical protein PH1245 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G71068 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession G71068 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-322 ##label KAW !'##cross-references GB:AP000005; NID:g3236132; PIDN:BAA30345.1; !1PID:g3257662 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1245 CLASSIFICATION #superfamily conserved hypothetical protein MJ0378 SUMMARY #length 322 #molecular-weight 37754 #checksum 5130 SEQUENCE /// ENTRY H70332 #type complete TITLE conserved hypothetical protein aq_369 - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H70332 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession H70332 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-316 ##label AQF !'##cross-references GB:AE000686; GB:AE000657; NID:g2983038; !1PIDN:AAC06657.1; PID:g2983048 !'##experimental_source strain VF5 GENETICS !$#gene aq_369 CLASSIFICATION #superfamily conserved hypothetical protein MJ0378 SUMMARY #length 316 #molecular-weight 36886 #checksum 2274 SEQUENCE /// ENTRY C71239 #type complete TITLE hypothetical protein PH0173 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C71239 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession C71239 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-317 ##label KAW !'##cross-references GB:AP000001; NID:g3236128; PIDN:BAA29242.1; !1PID:g3256559 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0173 CLASSIFICATION #superfamily conserved hypothetical protein MJ0378 SUMMARY #length 317 #molecular-weight 36898 #checksum 9501 SEQUENCE /// ENTRY B64357 #type complete TITLE hypothetical protein homolog MJ0458 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B64357 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession B64357 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-216 ##label BUL !'##cross-references GB:U67496; GB:L77117; NID:g2826283; !1PIDN:AAB98446.1; PID:g1499252; TIGR:MJ0458 GENETICS !$#map_position FOR409196-409846 CLASSIFICATION #superfamily hypothetical protein MJ0458 SUMMARY #length 216 #molecular-weight 24080 #checksum 946 SEQUENCE /// ENTRY A69094 #type complete TITLE delta 1-pyrroline-5-carboxylate synthetase - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A69094 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession A69094 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-228 ##label MTH !'##cross-references GB:AE000927; GB:AE000666; NID:g2622822; !1PIDN:AAB86170.1; PID:g2622829 !'##experimental_source strain Delta H GENETICS !$#gene MTH1698 !$#start_codon GTG CLASSIFICATION #superfamily hypothetical protein MJ0458 SUMMARY #length 228 #molecular-weight 24749 #checksum 125 SEQUENCE /// ENTRY D69321 #type complete TITLE conserved hypothetical protein AF0572 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69321 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession D69321 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-202 ##label KLE !'##cross-references GB:AE001065; GB:AE000782; NID:g2689388; !1PIDN:AAB90667.1; PID:g2650051; TIGR:AF0572 CLASSIFICATION #superfamily hypothetical protein MJ0458 SUMMARY #length 202 #molecular-weight 22471 #checksum 8325 SEQUENCE /// ENTRY S64534 #type complete TITLE hypothetical protein YGR211w - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein G7801 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S64534; S64533; S61949; S61950 REFERENCE S64071 !$#authors Rieger, M.; Mueller-Auer, S.; Brueckner, M.; Schaefer, M. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64534 !'##molecule_type DNA !'##residues 1-486 ##label RIE !'##cross-references EMBL:Z72996; NID:g1323378; PID:g1323379; !1GSPDB:GN00007; MIPS:YGR211w !'##experimental_source strain S288C REFERENCE S64517 !$#authors Guerreiro, P.; Barreiros, T.; Cyrne, L.; Soares, H.; Maia e !1Silva, A.; Rodrigues-Pousada, C. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64533 !'##molecule_type DNA !'##residues 1-93 ##label GUE !'##cross-references EMBL:Z72996; GSPDB:GN00007; MIPS:YGR211w !'##experimental_source strain S288C REFERENCE S61947 !$#authors Song, J.M.; Cheung, E.; Rabinowitz, J.C. !$#submission submitted to the EMBL Data Library, November 1995 !$#description Analysis of the 15.6-kb fragment encompassing the ADE3 gene. !$#accession S61949 !'##molecule_type DNA !'##residues 1-170,'VSLQEDR' ##label SON !'##cross-references EMBL:U40843; NID:g1165213; PID:g1165216 !'##experimental_source strain GRF88 !$#accession S61950 !'##molecule_type DNA !'##residues 306-419,'AG' ##label SOW !'##cross-references EMBL:U40843; NID:g1165213; PID:g1165217 !'##experimental_source strain GRF88 !'##note Region 290-* of this protein is homologous to thioredoxin-2 !1proteins, Acc A71066 GENETICS !$#gene SGD:ZPR1; MIPS:YGR211w !'##cross-references SGD:S0003443 !$#map_position 7R CLASSIFICATION #superfamily hypothetical protein YGR211w SUMMARY #length 486 #molecular-weight 55072 #checksum 7588 SEQUENCE /// ENTRY S78078 #type complete TITLE IMP dehydrogenase-related protein YAR075w - yeast (Saccharomyces cerevisiae) ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S78078; S70312 REFERENCE S78078 !$#authors Zhong, W.; Louis, E.J.; Bussey, H. !$#submission submitted to the EMBL Data Library, August 1996 !$#description Saccharomyces cerevisiae chromosome I right arm. !$#accession S78078 !'##molecule_type DNA !'##residues 1-157 ##label ZHO !'##cross-references EMBL:L28920; NID:g2911244; PID:g2911246; !1GSPDB:GN00001; MIPS:YAR075w !'##note this is a revision to the sequence from reference S53458 REFERENCE S53458 !$#authors Bussey, H.; Keng, T.; Storms, R.K.; Vo, D.; Zhong, W.; !1Fortin, N.; Barton, A.B.; Kaback, D.B.; Clark, M.W. !$#submission submitted to the EMBL Data Library, February 1994 !$#description Sequencing of chromosome I of Saccharomyces cerevisiae: !1analysis of the 52Kbp CDC15- FLO1-PHO11-YAR074 region. !$#accession S70312 !'##molecule_type DNA !'##residues 1-134 ##label BUS !'##cross-references EMBL:L28920; GSPDB:GN00001; MIPS:YAR075w !'##note this sequence has been revised in reference S78078 COMMENT This sequence is highly similar to the carboxyl 30% of IMP !1dehydrogenase (see PIR:S59402 and PIR:S48997) but lacks the !1active site region. GENETICS !$#gene MIPS:YAR075w !'##cross-references SGD:S0002145 !$#map_position 1R CLASSIFICATION #superfamily hypothetical IMP dehydrogenase-related protein !1YAR075w; IMP dehydrogenase catalytic homology FEATURE !$1-157 #domain IMP dehydrogenase catalytic homology #status !8atypical #label IDHC SUMMARY #length 157 #molecular-weight 17003 #checksum 4414 SEQUENCE /// ENTRY B64366 #type complete TITLE thioredoxin-2 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B64366 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession B64366 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-198 ##label BUL !'##cross-references GB:U67502; GB:L77117; NID:g2826293; !1PIDN:AAB98521.1; PID:g1591233; TIGR:MJ0530 GENETICS !$#map_position FOR466350-466946 CLASSIFICATION #superfamily Methanococcus jannaschii thioredoxin-2 SUMMARY #length 198 #molecular-weight 22591 #checksum 1933 SEQUENCE /// ENTRY A71066 #type complete TITLE hypothetical protein PH1223 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A71066 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession A71066 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-223 ##label KAW !'##cross-references GB:AP000005; NID:g3236132; PIDN:BAA30323.1; !1PID:g3257640 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1223 CLASSIFICATION #superfamily Methanococcus jannaschii thioredoxin-2 SUMMARY #length 223 #molecular-weight 25465 #checksum 8344 SEQUENCE /// ENTRY C69112 #type complete TITLE hypothetical protein MTH1834 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69112 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession C69112 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-196 ##label MTH !'##cross-references GB:AE000936; GB:AE000666; NID:g2622959; !1PIDN:AAB86300.1; PID:g2622968 !'##experimental_source strain Delta H GENETICS !$#gene MTH1834 !$#start_codon GTG CLASSIFICATION #superfamily Methanococcus jannaschii thioredoxin-2 SUMMARY #length 196 #molecular-weight 22017 #checksum 9495 SEQUENCE /// ENTRY G69347 #type complete TITLE conserved hypothetical protein AF0783 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69347 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession G69347 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-193 ##label KLE !'##cross-references GB:AE001050; GB:AE000782; NID:g2689373; !1PIDN:AAB90454.1; PID:g2649823; TIGR:AF0783 CLASSIFICATION #superfamily Methanococcus jannaschii thioredoxin-2 SUMMARY #length 193 #molecular-weight 21695 #checksum 5344 SEQUENCE /// ENTRY A70409 #type complete TITLE hypothetical protein aq_1259 - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A70409 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession A70409 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-436 ##label AQF !'##cross-references GB:AE000731; GB:AE000657; NID:g2983691; !1PIDN:AAC07262.1; PID:g2983698 !'##experimental_source strain VF5 GENETICS !$#gene aq_1259 CLASSIFICATION #superfamily Aquifex aeolicus hypothetical protein aq_1259 SUMMARY #length 436 #molecular-weight 49421 #checksum 2683 SEQUENCE /// ENTRY F71328 #type complete TITLE probable flagellar basal-body M ring protein (fliF) - syphilis spirochete ORGANISM #formal_name Treponema pallidum subsp. pallidum #common_name syphilis spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS F71328 REFERENCE A71250 !$#authors Fraser, C.M.; Norris, S.J.; Weinstock, G.M.; White, O.; !1Sutton, G.G.; Dodson, R.; Gwinn, M.; Hickey, E.K.; Clayton, !1R.; Ketchum, K.A.; Sodergren, E.; Hardham, J.M.; McLeod, !1M.P.; Salzberg, S.; Peterson, J.; Khalak, H.; Richardson, !1D.; Howell, J.K.; Chidambaram, M.; Utterback, T.; McDonald, !1L.; Artiach, P.; Bowman, C.; Cotton, M.D.; Fujii, C.; !1Garland, S.; Hatch, B.; Horst, K.; Roberts, K.; Watthey, L.; !1Weidman, J.; Smith, H.O.; Venter, J.C. !$#journal Science (1998) 281:375-388 !$#title Complete genome sequence of Treponema pallidum, the syphilis !1spirochete. !$#cross-references MUID:98332770; PMID:9665876 !$#accession F71328 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-567 ##label COL !'##cross-references GB:AE001218; GB:AE000520; NID:g3322678; !1PIDN:AAC65387.1; PID:g3322682 !'##experimental_source strain Nichols GENETICS !$#gene TP0399 CLASSIFICATION #superfamily probable flagellar basal-body M ring protein SUMMARY #length 567 #molecular-weight 64638 #checksum 4347 SEQUENCE /// ENTRY F64346 #type complete TITLE hypothetical protein MJ0374 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F64346 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession F64346 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-330 ##label BUL !'##cross-references GB:U67490; GB:L77117; NID:g2826276; !1PIDN:AAB98363.1; PID:g1591081; TIGR:MJ0374 !'##note Region 1-160 of this protein is homologous to Acc B70477; !1B64325 GENETICS !$#map_position REV339873-338881 CLASSIFICATION #superfamily hypothetical protein MJ0374; !1glucose-6-phosphatase catalytic domain homology FEATURE !$206-315 #domain glucose-6-phosphatase catalytic domain !8homology #label GPH SUMMARY #length 330 #molecular-weight 37018 #checksum 1179 SEQUENCE /// ENTRY B64373 #type complete TITLE hypothetical protein MJ0586 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B64373 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession B64373 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-170 ##label BUL !'##cross-references GB:U67507; GB:L77117; NID:g1591288; !1PIDN:AAB98578.1; PID:g1591294; TIGR:MJ0586 GENETICS !$#map_position FOR518550-519062 !$#start_codon TTG CLASSIFICATION #superfamily conserved hypothetical protein MJ0586 SUMMARY #length 170 #molecular-weight 19671 #checksum 8532 SEQUENCE /// ENTRY D69197 #type complete TITLE conserved hypothetical protein MTH729 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69197 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession D69197 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-155 ##label MTH !'##cross-references GB:AE000852; GB:AE000666; NID:g2621812; !1PIDN:AAB85234.1; PID:g2621818 !'##experimental_source strain Delta H GENETICS !$#gene MTH729 CLASSIFICATION #superfamily conserved hypothetical protein MJ0586 SUMMARY #length 155 #molecular-weight 18153 #checksum 6671 SEQUENCE /// ENTRY H69496 #type complete TITLE conserved hypothetical protein AF1977 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H69496 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession H69496 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-159 ##label KLE !'##cross-references GB:AE000966; GB:AE000782; NID:g2689289; !1PIDN:AAB89276.1; PID:g2648561; TIGR:AF1977 CLASSIFICATION #superfamily conserved hypothetical protein MJ0586 SUMMARY #length 159 #molecular-weight 18248 #checksum 1581 SEQUENCE /// ENTRY A71127 #type complete TITLE hypothetical protein PH0783 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A71127 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession A71127 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-200 ##label KAW !'##cross-references GB:AP000003; NID:g3236130; PIDN:BAA29875.1; !1PID:g3257192 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0783 CLASSIFICATION #superfamily conserved hypothetical protein MJ0586 SUMMARY #length 200 #molecular-weight 23127 #checksum 7590 SEQUENCE /// ENTRY G69184 #type complete TITLE conserved hypothetical protein MTH637 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69184 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession G69184 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-104 ##label MTH !'##cross-references GB:AE000844; GB:AE000666; NID:g2621707; !1PIDN:AAB85143.1; PID:g2621719 !'##experimental_source strain Delta H GENETICS !$#gene MTH637 !$#start_codon GTG CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0618 SUMMARY #length 104 #molecular-weight 11862 #checksum 1485 SEQUENCE /// ENTRY G69508 #type complete TITLE conserved hypothetical protein AF2072 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69508 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession G69508 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-78 ##label KLE !'##cross-references GB:AE000960; GB:AE000782; NID:g2689283; !1PIDN:AAB89177.1; PID:g2648454; TIGR:AF2072 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0618 SUMMARY #length 78 #molecular-weight 8816 #checksum 3060 SEQUENCE /// ENTRY B64377 #type complete TITLE conserved hypothetical protein MJ0618 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B64377 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession B64377 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-98 ##label BUL !'##cross-references GB:U67510; GB:L77117; NID:g1591325; !1PIDN:AAB98613.1; PID:g1591329; TIGR:MJ0618 GENETICS !$#map_position REV547879-547583 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0618 SUMMARY #length 98 #molecular-weight 11289 #checksum 8605 SEQUENCE /// ENTRY B64378 #type complete TITLE conserved hypothetical protein MJ0626 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B64378 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession B64378 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-209 ##label BUL !'##cross-references GB:U67510; GB:L77117; NID:g1591325; !1PIDN:AAB98620.1; PID:g1591337; TIGR:MJ0626 GENETICS !$#map_position FOR554711-555340 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0626 SUMMARY #length 209 #molecular-weight 23718 #checksum 7572 SEQUENCE /// ENTRY B69003 #type complete TITLE conserved hypothetical protein MTH1020 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69003 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession B69003 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-202 ##label MTH !'##cross-references GB:AE000874; GB:AE000666; NID:g2622110; !1PIDN:AAB85516.1; PID:g2622122 !'##experimental_source strain Delta H GENETICS !$#gene MTH1020 !$#start_codon TTG CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0626 SUMMARY #length 202 #molecular-weight 21839 #checksum 3355 SEQUENCE /// ENTRY F64410 #type complete TITLE molybdenum cofactor biosynthesis protein moeA homolog - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F64410 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession F64410 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-620 ##label BUL !'##cross-references GB:U67532; GB:L77117; NID:g2826344; !1PIDN:AAB98890.1; PID:g1591564; TIGR:MJ0886 GENETICS !$#map_position REV818205-816343 CLASSIFICATION #superfamily molybdenum cofactor biosynthesis protein moeA-1 SUMMARY #length 620 #molecular-weight 68896 #checksum 6614 SEQUENCE /// ENTRY C69366 #type complete TITLE molybdenum cofactor biosynthesis protein (moeA-1) homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69366 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession C69366 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-654 ##label KLE !'##cross-references GB:AE001039; GB:AE000782; NID:g2689362; !1PIDN:AAB90307.1; PID:g2649665; TIGR:AF0931 CLASSIFICATION #superfamily molybdenum cofactor biosynthesis protein moeA-1 SUMMARY #length 654 #molecular-weight 71189 #checksum 6416 SEQUENCE /// ENTRY B64384 #type complete TITLE hypothetical protein homolog MJ0674 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B64384 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession B64384 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-338 ##label BUL !'##cross-references GB:U67514; GB:L77117; NID:g2826304; !1PIDN:AAB98668.1; PID:g1591388; TIGR:MJ0674 GENETICS !$#map_position FOR599727-600743 CLASSIFICATION #superfamily conserved hypothetical protein MJ0674 SUMMARY #length 338 #molecular-weight 40020 #checksum 2846 SEQUENCE /// ENTRY H69008 #type complete TITLE conserved hypothetical protein MTH1069 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H69008 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession H69008 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-332 ##label MTH !'##cross-references GB:AE000877; GB:AE000666; NID:g2622157; !1PIDN:AAB85558.1; PID:g2622167 !'##experimental_source strain Delta H GENETICS !$#gene MTH1069 CLASSIFICATION #superfamily conserved hypothetical protein MJ0674 SUMMARY #length 332 #molecular-weight 37538 #checksum 9790 SEQUENCE /// ENTRY B71052 #type complete TITLE hypothetical protein PH1113 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B71052 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession B71052 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-337 ##label KAW !'##cross-references GB:AP000005; NID:g3236132; PIDN:BAA30212.1; !1PID:g3257529 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1113 CLASSIFICATION #superfamily conserved hypothetical protein MJ0674 SUMMARY #length 337 #molecular-weight 39482 #checksum 8611 SEQUENCE /// ENTRY A70364 #type complete TITLE conserved hypothetical protein aq_729 - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A70364 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession A70364 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-337 ##label AQF !'##cross-references GB:AE000705; GB:AE000657; NID:g2983310; !1PIDN:AAC06914.1; PID:g2983324 !'##experimental_source strain VF5 GENETICS !$#gene aq_729 CLASSIFICATION #superfamily conserved hypothetical protein MJ0674 SUMMARY #length 337 #molecular-weight 39099 #checksum 8149 SEQUENCE /// ENTRY H64400 #type complete TITLE hypothetical protein MJ0808 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H64400 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession H64400 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-333 ##label BUL !'##cross-references GB:U67525; GB:L77117; NID:g2826325; !1PIDN:AAB98808.1; PID:g1499631; TIGR:MJ0808 GENETICS !$#map_position FOR730808-731809 CLASSIFICATION #superfamily conserved hypothetical protein MJ0808 SUMMARY #length 333 #molecular-weight 38337 #checksum 8005 SEQUENCE /// ENTRY A71012 #type complete TITLE hypothetical protein PH1391 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A71012 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession A71012 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-348 ##label KAW !'##cross-references GB:AP000006; NID:g3236133; PIDN:BAA30497.1; !1PID:g3257814 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1391 CLASSIFICATION #superfamily conserved hypothetical protein MJ0808 SUMMARY #length 348 #molecular-weight 40165 #checksum 3380 SEQUENCE /// ENTRY G70460 #type complete TITLE conserved hypothetical protein aq_1861 - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G70460 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession G70460 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-342 ##label AQF !'##cross-references GB:AE000760; GB:AE000657; NID:g2984138; !1PIDN:AAC07683.1; PID:g2984148 !'##experimental_source strain VF5 GENETICS !$#gene aq_1861 CLASSIFICATION #superfamily conserved hypothetical protein MJ0808 SUMMARY #length 342 #molecular-weight 39014 #checksum 4952 SEQUENCE /// ENTRY C70646 #type complete TITLE probable pflA protein - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C70646 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession C70646 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-362 ##label COL !'##cross-references GB:Z83867; GB:AL123456; NID:g3261695; !1PIDN:CAB06292.1; PID:g3261696 !'##experimental_source strain H37Rv GENETICS !$#gene pflA CLASSIFICATION #superfamily conserved hypothetical protein MJ0808 SUMMARY #length 362 #molecular-weight 40432 #checksum 9987 SEQUENCE /// ENTRY A69416 #type complete TITLE pyruvate formate-lyase activating enzyme (act-3) homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A69416 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession A69416 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-336 ##label KLE !'##cross-references GB:AE001012; GB:AE000782; NID:g2689335; !1PIDN:AAB89917.1; PID:g2649248; TIGR:AF1330 CLASSIFICATION #superfamily conserved hypothetical protein MJ0808 SUMMARY #length 336 #molecular-weight 38729 #checksum 155 SEQUENCE /// ENTRY F69052 #type complete TITLE pyruvate formate-lyase activating enzyme related protein - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F69052 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession F69052 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-335 ##label MTH !'##cross-references GB:AE000902; GB:AE000666; NID:g2622500; !1PIDN:AAB85872.1; PID:g2622506 !'##experimental_source strain Delta H GENETICS !$#gene MTH1395 CLASSIFICATION #superfamily conserved hypothetical protein MJ0808 SUMMARY #length 335 #molecular-weight 37644 #checksum 400 SEQUENCE /// ENTRY F69534 #type complete TITLE pyruvate formate-lyase activating enzyme (act-4) homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F69534 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession F69534 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-330 ##label KLE !'##cross-references GB:AE000947; GB:AE000782; NID:g2689270; !1PIDN:AAB88976.1; PID:g2648242; TIGR:AF2278 CLASSIFICATION #superfamily conserved hypothetical protein MJ0808 SUMMARY #length 330 #molecular-weight 37713 #checksum 960 SEQUENCE /// ENTRY B64383 #type complete TITLE molybdenum cofactor biosynthesis protein moeA homolog - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B64383 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession B64383 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-398 ##label BUL !'##cross-references GB:U67514; GB:L77117; NID:g2826304; !1PIDN:AAB98661.1; PID:g1591380; TIGR:MJ0666 GENETICS !$#map_position REV592613-591417 CLASSIFICATION #superfamily molybdenum cofactor biosynthesis protein moeA-2 SUMMARY #length 398 #molecular-weight 44418 #checksum 2925 SEQUENCE /// ENTRY A69049 #type complete TITLE molybdenum cofactor biosynthesis MoeA - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A69049 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession A69049 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-404 ##label MTH !'##cross-references GB:AE000899; GB:AE000666; NID:g2622468; !1PIDN:AAB85846.1; PID:g2622477 !'##experimental_source strain Delta H GENETICS !$#gene MTH1369 CLASSIFICATION #superfamily molybdenum cofactor biosynthesis protein moeA-2 SUMMARY #length 404 #molecular-weight 43544 #checksum 6748 SEQUENCE /// ENTRY G69000 #type complete TITLE molybdenum cofactor biosynthesis protein MoeA - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69000 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession G69000 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-409 ##label MTH !'##cross-references GB:AE000873; GB:AE000666; NID:g2622101; !1PIDN:AAB85499.1; PID:g2622104 !'##experimental_source strain Delta H GENETICS !$#gene MTH1003 !$#start_codon TTG CLASSIFICATION #superfamily molybdenum cofactor biosynthesis protein moeA-2 SUMMARY #length 409 #molecular-weight 43410 #checksum 7972 SEQUENCE /// ENTRY B69366 #type complete TITLE molybdenum cofactor biosynthesis protein (moeA-2) homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69366 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession B69366 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-414 ##label KLE !'##cross-references GB:AE001039; GB:AE000782; NID:g2689362; !1PIDN:AAB90308.1; PID:g2649666; TIGR:AF0930 CLASSIFICATION #superfamily molybdenum cofactor biosynthesis protein moeA-2 SUMMARY #length 414 #molecular-weight 45033 #checksum 6227 SEQUENCE /// ENTRY E69659 #type complete TITLE molybdopterin biosynthesis protein moeA - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69659 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69659 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-430 ##label KUN !'##cross-references GB:Z99111; GB:AL009126; NID:g2633699; !1PIDN:CAB13301.1; PID:g2633799 !'##experimental_source strain 168 GENETICS !$#gene moeA CLASSIFICATION #superfamily molybdenum cofactor biosynthesis protein moeA-2 SUMMARY #length 430 #molecular-weight 46619 #checksum 2964 SEQUENCE /// ENTRY E70302 #type complete TITLE molybdenum cofactor biosynthesis protein A - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E70302 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession E70302 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-402 ##label AQF !'##cross-references GB:AE000670; GB:AE000657; NID:g2982779; !1PIDN:AAC06407.1; PID:g2982782 !'##experimental_source strain VF5 GENETICS !$#gene moeA1 CLASSIFICATION #superfamily molybdenum cofactor biosynthesis protein moeA-2 SUMMARY #length 402 #molecular-weight 45037 #checksum 4909 SEQUENCE /// ENTRY B71173 #type complete TITLE probable molybdopterin biosynthesis moea protein - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B71173 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession B71173 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-402 ##label KAW !'##cross-references GB:AP000002; NID:g3236129; PIDN:BAA29671.1; !1PID:g3256988 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0582 CLASSIFICATION #superfamily molybdenum cofactor biosynthesis protein moeA-2 SUMMARY #length 402 #molecular-weight 42800 #checksum 246 SEQUENCE /// ENTRY C69166 #type complete TITLE conserved hypothetical protein MTH503 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69166 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession C69166 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-107 ##label MTH !'##cross-references GB:AE000834; GB:AE000666; NID:g2621574; !1PIDN:AAB85009.1; PID:g2621575 !'##experimental_source strain Delta H GENETICS !$#gene MTH503 !$#start_codon TTG CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0714 SUMMARY #length 107 #molecular-weight 11370 #checksum 8958 SEQUENCE /// ENTRY H69178 #type complete TITLE conserved hypothetical protein MTH595 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H69178 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession H69178 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-126 ##label MTH !'##cross-references GB:AE000841; GB:AE000666; NID:g2621665; !1PIDN:AAB85101.1; PID:g2621674 !'##experimental_source strain Delta H GENETICS !$#gene MTH595 !$#start_codon TTG CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0714 SUMMARY #length 126 #molecular-weight 13497 #checksum 2600 SEQUENCE /// ENTRY C69437 #type complete TITLE conserved hypothetical protein AF1500 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69437 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession C69437 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-114 ##label KLE !'##cross-references GB:AE000999; GB:AE000782; NID:g2689322; !1PIDN:AAB89744.1; PID:g2649062; TIGR:AF1500 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0714 SUMMARY #length 114 #molecular-weight 12341 #checksum 5642 SEQUENCE /// ENTRY B70459 #type complete TITLE conserved hypothetical protein aq_1847 - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B70459 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession B70459 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-117 ##label AQF !'##cross-references GB:AE000759; GB:AE000657; NID:g2984125; !1PIDN:AAC07671.1; PID:g2984135 !'##experimental_source strain VF5 GENETICS !$#gene aq_1847 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0714 SUMMARY #length 117 #molecular-weight 12457 #checksum 8342 SEQUENCE /// ENTRY JC5016 #type complete TITLE hyaluronan receptor - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 29-Sep-1999 ACCESSIONS JC5016 REFERENCE JC5016 !$#authors Wang, C.; Entwistle, J.; Hou, G.; Li, Q.; Turley, E.A. !$#journal Gene (1996) 174:299-306 !$#title The characterization of a human RHAMM cDNA: Conservation of !1the hyaluronan-binding domains. !$#cross-references MUID:97045829; PMID:8890751 !$#contents breast !$#accession JC5016 !'##molecule_type mRNA !'##residues 1-725 ##label WAN !'##cross-references GB:U29343 !'##note it is uncertain whether Met-1 or Met-196 is the initiator COMMENT This receptor regulates focal adhesion turnover, and !1regulates human breast cancer cell motility and invasion. GENETICS !$#gene GDB:HMMR; RHAMM !'##cross-references GDB:683209; OMIM:600936 !$#map_position 5q33.2-5qter CLASSIFICATION #superfamily hyaluronan receptor SUMMARY #length 725 #molecular-weight 84209 #checksum 4502 SEQUENCE /// ENTRY B64414 #type complete TITLE hypothetical protein MJ0914 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B64414 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession B64414 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-136 ##label BUL !'##cross-references GB:U67535; GB:L77117; NID:g2826348; !1PIDN:AAB98919.1; PID:g1591588; TIGR:MJ0914 GENETICS !$#map_position REV846192-845782 !$#start_codon GTG CLASSIFICATION #superfamily hypothetical protein MJ0914 SUMMARY #length 136 #molecular-weight 16210 #checksum 6690 SEQUENCE /// ENTRY S73090 #type complete TITLE hypothetical protein c0623 - Sulfolobus solfataricus ORGANISM #formal_name Sulfolobus solfataricus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S73090 REFERENCE S73076 !$#authors Sensen, C.W.; Klenk, H.P.; Singh, R.K.; Allard, G.; Chan, !1C.C.Y.; Liu, Q.Y.; Penny, S.L.; Young, F.; Schenk, M.E.; !1Gaasterland, T.; Doolittle, W.F.; Ragan, M.A.; Charlebois, !1R.L. !$#journal Mol. Microbiol. (1996) 22:175-191 !$#title Organizational characteristics and information content of an !1archaeal genome: 156 kb of sequence from Sulfolobus !1solfataricus P2. !$#cross-references MUID:97055432; PMID:8899719 !$#accession S73090 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-123 ##label SEN !'##cross-references EMBL:Y08256; NID:g1707679; PID:g1707702 !'##experimental_source strain P2 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1September 1996 GENETICS !$#start_codon TTG CLASSIFICATION #superfamily hypothetical protein MJ0914 SUMMARY #length 123 #molecular-weight 14371 #checksum 302 SEQUENCE /// ENTRY D69340 #type complete TITLE cobalamin biosynthesis precorrin-3 methylase (cbiH) homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69340 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession D69340 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-446 ##label KLE !'##cross-references GB:AE001055; GB:AE000782; NID:g2689378; !1PIDN:AAB90518.1; PID:g2649892; TIGR:AF0724 !'##note Region (350-*) is homologous to other bacterial precorrin !1isomerases; Acc B69128 CLASSIFICATION #superfamily probable cobalamin biosynthesis precorrin-3 !1methylase SUMMARY #length 446 #molecular-weight 48678 #checksum 6007 SEQUENCE /// ENTRY B64416 #type complete TITLE probable precorrin isomerase - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B64416 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession B64416 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-210 ##label BUL !'##cross-references GB:U67536; GB:L77117; NID:g1591596; !1PIDN:AAB98932.1; PID:g1591601; TIGR:MJ0930 GENETICS !$#map_position FOR860304-860936 CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum precorrin !1isomerase SUMMARY #length 210 #molecular-weight 22974 #checksum 3393 SEQUENCE /// ENTRY B69128 #type complete TITLE precorrin isomerase - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69128 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession B69128 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-206 ##label MTH !'##cross-references GB:AE000809; GB:AE000666; NID:g2621265; !1PIDN:AAB84733.1; PID:g2621274 !'##experimental_source strain Delta H GENETICS !$#gene MTH227 !$#start_codon TTG CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum precorrin !1isomerase SUMMARY #length 206 #molecular-weight 21904 #checksum 9667 SEQUENCE /// ENTRY S76139 #type complete TITLE hypothetical protein - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S76139 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76139 !'##status preliminary !'##molecule_type DNA !'##residues 1-217 ##label KAN !'##cross-references EMBL:D90914; GB:AB001339; NID:g1653477; !1PIDN:BAA18398.1; PID:g1653485 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum precorrin !1isomerase SUMMARY #length 217 #molecular-weight 23363 #checksum 5614 SEQUENCE /// ENTRY S75678 #type complete TITLE hypothetical protein slr1467 - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S75678 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75678 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-222 ##label KAN !'##cross-references EMBL:D90912; GB:AB001339; NID:g1653228; !1PIDN:BAA18239.1; PID:g1653324 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum precorrin !1isomerase SUMMARY #length 222 #molecular-weight 24620 #checksum 8734 SEQUENCE /// ENTRY C36145 #type complete TITLE hydrogenobyrinic acid synthase, hydrogenobyrinic acid-binding protein, CobH - Pseudomonas sp. ORGANISM #formal_name Pseudomonas sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS C36145; A44925 REFERENCE A36145 !$#authors Crouzet, J.; Cameron, B.; Cauchois, L.; Rigault, S.; Rouyez, !1M.C.; Blanche, F.; Thibaut, D.; Debussche, L. !$#journal J. Bacteriol. (1990) 172:5980-5990 !$#title Genetic and sequence analysis of an 8.7-kilobase Pseudomonas !1denitrificans fragment carrying eight genes involved in !1transformation of precorrin-2 to cobyrinic acid. !$#cross-references MUID:91008976; PMID:2211521 !$#accession C36145 !'##status preliminary !'##molecule_type DNA !'##residues 1-210 ##label CRO !'##cross-references GB:M59301; GB:M32224; NID:g151170; PID:g151173 !'##note the source is designated as Pseudomonas denitrificans REFERENCE A44925 !$#authors Thibaut, D.; Couder, M.; Famechon, A.; Debussche, L.; !1Cameron, B.; Crouzet, J.; Blanche, F. !$#journal J. Bacteriol. (1992) 174:1043-1049 !$#title The final step in the biosynthesis of hydrogenobyrinic acid !1is catalyzed by the cobH gene product with precorrin-8x as !1the substrate. !$#cross-references MUID:92121091; PMID:1732194 !$#accession A44925 !'##status preliminary !'##molecule_type protein !'##residues 2-18 ##label THI !'##note sequence extracted from NCBI backbone (NCBIP:77817) GENETICS !$#gene cobH CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum precorrin !1isomerase SUMMARY #length 210 #molecular-weight 22064 #checksum 7302 SEQUENCE /// ENTRY D70764 #type complete TITLE probable cobH - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D70764 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession D70764 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-208 ##label COL !'##cross-references GB:Z73966; GB:AL123456; NID:g3261577; !1PIDN:CAA98213.1; PID:g1370231 !'##experimental_source strain H37Rv GENETICS !$#gene cobH CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum precorrin !1isomerase SUMMARY #length 208 #molecular-weight 21613 #checksum 6643 SEQUENCE /// ENTRY B64421 #type complete TITLE conserved hypothetical protein MJ0970 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B64421 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession B64421 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-143 ##label BUL !'##cross-references GB:U67540; GB:L77117; NID:g1591631; !1PIDN:AAB98975.1; PID:g1591633; TIGR:MJ0970 GENETICS !$#map_position REV904629-904198 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0970 SUMMARY #length 143 #molecular-weight 16519 #checksum 7673 SEQUENCE /// ENTRY H69052 #type complete TITLE conserved hypothetical protein MTH1397 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H69052 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession H69052 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-128 ##label MTH !'##cross-references GB:AE000902; GB:AE000666; NID:g2622500; !1PIDN:AAB85874.1; PID:g2622508 !'##experimental_source strain Delta H GENETICS !$#gene MTH1397 !$#start_codon GTG CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0970 SUMMARY #length 128 #molecular-weight 14232 #checksum 1897 SEQUENCE /// ENTRY A69340 #type complete TITLE conserved hypothetical protein AF0721 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A69340 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession A69340 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-132 ##label KLE !'##cross-references GB:AE001055; GB:AE000782; NID:g2689378; !1PIDN:AAB90530.1; PID:g2649904; TIGR:AF0721 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0970 SUMMARY #length 132 #molecular-weight 15109 #checksum 9898 SEQUENCE /// ENTRY E69877 #type complete TITLE conserved hypothetical protein ylnE - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69877 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69877 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-261 ##label KUN !'##cross-references GB:Z99112; GB:AL009126; NID:g2633902; !1PIDN:CAB13436.1; PID:g2633935 !'##experimental_source strain 168 GENETICS !$#gene ylnE CLASSIFICATION #superfamily conserved hypothetical protein ylnE SUMMARY #length 261 #molecular-weight 28835 #checksum 4950 SEQUENCE /// ENTRY S75947 #type complete TITLE hypothetical protein - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S75947 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75947 !'##status preliminary !'##molecule_type DNA !'##residues 1-336 ##label KAN !'##cross-references EMBL:D64006; GB:AB001339; NID:g1001291; !1PID:g1001307 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily conserved hypothetical protein ylnE SUMMARY #length 336 #molecular-weight 38339 #checksum 5133 SEQUENCE /// ENTRY B64420 #type complete TITLE conserved hypothetical protein MJ0962 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B64420 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession B64420 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-128 ##label BUL !'##cross-references GB:U67539; GB:L77117; NID:g1591619; !1PIDN:AAB98964.1; PID:g1591626; TIGR:MJ0962 GENETICS !$#map_position FOR894939-895325 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0962 SUMMARY #length 128 #molecular-weight 15567 #checksum 131 SEQUENCE /// ENTRY A71039 #type complete TITLE hypothetical protein PH1601 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A71039 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession A71039 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-120 ##label KAW !'##cross-references GB:AP000006; NID:g3236133; PIDN:BAA30713.1; !1PID:g3258030 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1601 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0962 SUMMARY #length 120 #molecular-weight 14588 #checksum 6181 SEQUENCE /// ENTRY B69083 #type complete TITLE conserved hypothetical protein MTH1618 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69083 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession B69083 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-140 ##label MTH !'##cross-references GB:AE000920; GB:AE000666; NID:g2622729; !1PIDN:AAB86091.1; PID:g2622743 !'##experimental_source strain Delta H GENETICS !$#gene MTH1618 !$#start_codon TTG CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0962 SUMMARY #length 140 #molecular-weight 16953 #checksum 8123 SEQUENCE /// ENTRY E69263 #type complete TITLE conserved hypothetical protein AF0109 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69263 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession E69263 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-107 ##label KLE !'##cross-references GB:AE001099; GB:AE000782; NID:g2689422; !1PIDN:AAB91122.1; PID:g2650539; TIGR:AF0109 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0962 SUMMARY #length 107 #molecular-weight 13307 #checksum 6760 SEQUENCE /// ENTRY B64440 #type complete TITLE hypothetical protein MJ1123 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B64440 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession B64440 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-205 ##label BUL !'##cross-references GB:U67555; GB:L77117; NID:g1591760; !1PIDN:AAB99125.1; PID:g1499975; TIGR:MJ1123 GENETICS !$#map_position FOR1061811-1062428 CLASSIFICATION #superfamily conserved hypothetical protein MJ1123; bioC !1homology FEATURE !$35-126 #domain bioC homology #label BIOC SUMMARY #length 205 #molecular-weight 23560 #checksum 1373 SEQUENCE /// ENTRY F69348 #type complete TITLE conserved hypothetical protein AF0790 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F69348 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession F69348 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-184 ##label KLE !'##cross-references GB:AE001050; GB:AE000782; NID:g2689373; !1PIDN:AAB90450.1; PID:g2649819; TIGR:AF0790 CLASSIFICATION #superfamily conserved hypothetical protein MJ1123; bioC !1homology FEATURE !$33-123 #domain bioC homology #label BIOC SUMMARY #length 184 #molecular-weight 20960 #checksum 2379 SEQUENCE /// ENTRY H70409 #type complete TITLE conserved hypothetical protein aq_1270 - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H70409 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession H70409 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-200 ##label AQF !'##cross-references GB:AE000732; GB:AE000657; NID:g2983704; !1PIDN:AAC07281.1; PID:g2983718 !'##experimental_source strain VF5 GENETICS !$#gene aq_1270 CLASSIFICATION #superfamily conserved hypothetical protein MJ1123; bioC !1homology FEATURE !$24-116 #domain bioC homology #label BIOC SUMMARY #length 200 #molecular-weight 23113 #checksum 9193 SEQUENCE /// ENTRY F64379 #type complete TITLE hypothetical protein MJ0638 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F64379 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession F64379 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-225 ##label BUL !'##cross-references GB:U67511; GB:L77117; NID:g2826300; !1PIDN:AAB98634.1; PID:g1499447; TIGR:MJ0638 GENETICS !$#map_position REV568588-567911 CLASSIFICATION #superfamily conserved hypothetical protein MJ1123; bioC !1homology FEATURE !$47-138 #domain bioC homology #label BIOC SUMMARY #length 225 #molecular-weight 26694 #checksum 298 SEQUENCE /// ENTRY B64456 #type complete TITLE bioC protein homolog - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B64456 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession B64456 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-251 ##label BUL !'##cross-references GB:U67565; GB:L77117; NID:g1591874; !1PIDN:AAB99255.1; PID:g1591885; TIGR:MJ1252 GENETICS !$#map_position REV1194506-1193751 CLASSIFICATION #superfamily conserved hypothetical protein MJ1123; bioC !1homology FEATURE !$56-148 #domain bioC homology #label BIOC SUMMARY #length 251 #molecular-weight 29161 #checksum 1074 SEQUENCE /// ENTRY A70759 #type complete TITLE hypothetical protein Rv2003c - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A70759 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession A70759 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-285 ##label COL !'##cross-references GB:Z74025; GB:AL123456; NID:g3261586; !1PIDN:CAA98385.1; PID:g1403450 !'##experimental_source strain H37Rv GENETICS !$#gene Rv2003c CLASSIFICATION #superfamily conserved hypothetical protein MJ1123; bioC !1homology SUMMARY #length 285 #molecular-weight 31049 #checksum 295 SEQUENCE /// ENTRY F71129 #type complete TITLE hypothetical protein PH0803 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F71129 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession F71129 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-110 ##label KAW !'##cross-references GB:AP000003; NID:g3236130; PIDN:BAA29896.1; !1PID:g3257213 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0803 CLASSIFICATION #superfamily hypothetical protein MJ1243 SUMMARY #length 110 #molecular-weight 12763 #checksum 5955 SEQUENCE /// ENTRY B69333 #type complete TITLE conserved hypothetical protein AF0666 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69333 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession B69333 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-105 ##label KLE !'##cross-references GB:AE001059; GB:AE000782; NID:g2689382; !1PIDN:AAB90575.1; PID:g2649953; TIGR:AF0666 CLASSIFICATION #superfamily hypothetical protein MJ1243 SUMMARY #length 105 #molecular-weight 11691 #checksum 1492 SEQUENCE /// ENTRY A69024 #type complete TITLE conserved hypothetical protein MTH1178 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A69024 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession A69024 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-189 ##label MTH !'##cross-references GB:AE000886; GB:AE000666; NID:g2622276; !1PIDN:AAB85667.1; PID:g2622285 !'##experimental_source strain Delta H GENETICS !$#gene MTH1178 CLASSIFICATION #superfamily hypothetical protein MJ1243 SUMMARY #length 189 #molecular-weight 21050 #checksum 3758 SEQUENCE /// ENTRY B64455 #type complete TITLE hypothetical protein MJ1243 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B64455 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession B64455 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-123 ##label BUL !'##cross-references GB:U67565; GB:L77117; NID:g1591874; !1PIDN:AAB99248.1; PID:g1591876; TIGR:MJ1243 GENETICS !$#map_position REV1187994-1187623 CLASSIFICATION #superfamily hypothetical protein MJ1243 SUMMARY #length 123 #molecular-weight 14391 #checksum 2286 SEQUENCE /// ENTRY B64457 #type complete TITLE uridylate kinase homolog - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B64457 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession B64457 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-240 ##label BUL !'##cross-references GB:U67566; GB:L77117; NID:g1591887; !1PIDN:AAB99262.1; PID:g1591893; TIGR:MJ1259 GENETICS !$#map_position FOR1201101-1201823 !$#start_codon TTG CLASSIFICATION #superfamily probable uridylate kinase MTH879 SUMMARY #length 240 #molecular-weight 25611 #checksum 2770 SEQUENCE /// ENTRY B71014 #type complete TITLE hypothetical protein PH1408 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B71014 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession B71014 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-226 ##label KAW !'##cross-references GB:AP000006; NID:g3236133; PIDN:BAA30514.1; !1PID:g3257831 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1408 CLASSIFICATION #superfamily probable uridylate kinase MTH879 SUMMARY #length 226 #molecular-weight 24691 #checksum 407 SEQUENCE /// ENTRY A69505 #type complete TITLE uridylate kinase (pyrH) homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A69505 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession A69505 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-219 ##label KLE !'##cross-references GB:AE000962; GB:AE000782; NID:g2689285; !1PIDN:AAB89213.1; PID:g2648494; TIGR:AF2042 CLASSIFICATION #superfamily probable uridylate kinase MTH879 SUMMARY #length 219 #molecular-weight 23398 #checksum 8995 SEQUENCE /// ENTRY D69217 #type complete TITLE hypothetical protein MTH879 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69217 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession D69217 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-224 ##label MTH !'##cross-references GB:AE000864; GB:AE000666; NID:g2621970; !1PIDN:AAB85377.1; PID:g2621973 !'##experimental_source strain Delta H GENETICS !$#gene MTH879 CLASSIFICATION #superfamily probable uridylate kinase MTH879 SUMMARY #length 224 #molecular-weight 24438 #checksum 2487 SEQUENCE /// ENTRY B70171 #type complete TITLE uridylate kinase (smbA) homolog - Lyme disease spirochete ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B70171 REFERENCE A70100 !$#authors Fraser, C.M.; Casjens, S.; Huang, W.M.; Sutton, G.G.; !1Clayton, R.; Lathigra, R.; White, O.; Ketchum, K.A.; Dodson, !1R.; Hickey, E.K.; Gwinn, M.; Dougherty, B.; Tomb, J.F.; !1Fleischmann, R.D.; Richardson, D.; Peterson, J.; Kerlavage, !1A.R.; Quackenbush, J.; Salzberg, S.; Hanson, M.; Vugt, R.V.; !1Palmer, N.; Adams, M.D.; Gocayne, J.; Weidman, J.; !1Utterback, T.; Watthey, L.; McDonald, L.; Artiach, P.; !1Bowman, C.; Garland, S.; Fujii, C.; Cotton, M.D.; Horst, K.; !1Roberts, K.; Hatch, B.; Smith, H.O.; Venter, J.C. !$#journal Nature (1997) 390:580-586 !$#title Genomic sequence of a Lyme disease spirochaete, Borrelia !1burgdorferi. !$#cross-references MUID:98065943; PMID:9403685 !$#accession B70171 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-229 ##label KLE !'##cross-references GB:AE001158; GB:AE000783; NID:g2688483; !1PIDN:AAC66932.1; PID:g2688487; TIGR:BB0571 !'##experimental_source strain B31 CLASSIFICATION #superfamily probable uridylate kinase MTH879 SUMMARY #length 229 #molecular-weight 26212 #checksum 516 SEQUENCE /// ENTRY G71366 #type complete TITLE probable uridylate kinase (smbA) - syphilis spirochete ORGANISM #formal_name Treponema pallidum subsp. pallidum #common_name syphilis spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS G71366 REFERENCE A71250 !$#authors Fraser, C.M.; Norris, S.J.; Weinstock, G.M.; White, O.; !1Sutton, G.G.; Dodson, R.; Gwinn, M.; Hickey, E.K.; Clayton, !1R.; Ketchum, K.A.; Sodergren, E.; Hardham, J.M.; McLeod, !1M.P.; Salzberg, S.; Peterson, J.; Khalak, H.; Richardson, !1D.; Howell, J.K.; Chidambaram, M.; Utterback, T.; McDonald, !1L.; Artiach, P.; Bowman, C.; Cotton, M.D.; Fujii, C.; !1Garland, S.; Hatch, B.; Horst, K.; Roberts, K.; Watthey, L.; !1Weidman, J.; Smith, H.O.; Venter, J.C. !$#journal Science (1998) 281:375-388 !$#title Complete genome sequence of Treponema pallidum, the syphilis !1spirochete. !$#cross-references MUID:98332770; PMID:9665876 !$#accession G71366 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-251 ##label COL !'##cross-references GB:AE001194; GB:AE000520; NID:g3322355; !1PIDN:AAC65094.1; PID:g3322360 !'##experimental_source strain Nichols GENETICS !$#gene TP0099 CLASSIFICATION #superfamily probable uridylate kinase MTH879 SUMMARY #length 251 #molecular-weight 27299 #checksum 4611 SEQUENCE /// ENTRY B64467 #type complete TITLE conserved hypothetical protein MJ1339 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS B64467 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession B64467 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-154 ##label BUL !'##cross-references GB:U67574; GB:L77117; NID:g1591978; !1PIDN:AAB99349.1; PID:g1591981; TIGR:MJ1339 GENETICS !$#map_position FOR1287391-1287855 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ1339; translation elongation factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop FEATURE !$6-114 #domain translation elongation factor Tu homology !8#label ETU\ !$12-19 #region nucleotide-binding motif A (P-loop)\ !$111-114 #region GTP-binding NKXD motif SUMMARY #length 154 #molecular-weight 17196 #checksum 9694 SEQUENCE /// ENTRY C69202 #type complete TITLE conserved hypothetical protein MTH765 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS C69202 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession C69202 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-152 ##label MTH !'##cross-references GB:AE000855; GB:AE000666; NID:g2621852; !1PIDN:AAB85268.1; PID:g2621855 !'##experimental_source strain Delta H GENETICS !$#gene MTH765 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ1339; translation elongation factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop FEATURE !$7-115 #domain translation elongation factor Tu homology !8#label ETU\ !$13-20 #region nucleotide-binding motif A (P-loop)\ !$112-115 #region GTP-binding NKXD motif SUMMARY #length 152 #molecular-weight 16878 #checksum 6271 SEQUENCE /// ENTRY H71054 #type complete TITLE hypothetical protein PH1134 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H71054 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession H71054 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-310 ##label KAW !'##cross-references GB:AP000005; NID:g3236132; PIDN:BAA30234.1; !1PID:g3257551 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1134 CLASSIFICATION #superfamily hypothetical protein PH1134; bioC homology FEATURE !$43-134 #domain bioC homology #label BIOC SUMMARY #length 310 #molecular-weight 35754 #checksum 7380 SEQUENCE /// ENTRY H69510 #type complete TITLE conserved hypothetical protein AF2089 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H69510 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession H69510 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-313 ##label KLE !'##cross-references GB:AE000960; GB:AE000782; NID:g2689283; !1PIDN:AAB89167.1; PID:g2648456; TIGR:AF2089 CLASSIFICATION #superfamily conserved hypothetical protein MJ1427 SUMMARY #length 313 #molecular-weight 34075 #checksum 2984 SEQUENCE /// ENTRY G69210 #type complete TITLE conserved hypothetical protein MTH830 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69210 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession G69210 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-329 ##label MTH !'##cross-references GB:AE000860; GB:AE000666; NID:g2621915; !1PIDN:AAB85328.1; PID:g2621920 !'##experimental_source strain Delta H GENETICS !$#gene MTH830 !$#start_codon GTG CLASSIFICATION #superfamily conserved hypothetical protein MJ1427 SUMMARY #length 329 #molecular-weight 35602 #checksum 8229 SEQUENCE /// ENTRY B64478 #type complete TITLE hypothetical protein MJ1427 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B64478 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession B64478 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-328 ##label BUL !'##cross-references GB:U67584; GB:L77117; NID:g1592077; !1PIDN:AAB99449.1; PID:g1592332; TIGR:MJ1427 GENETICS !$#map_position FOR1396652-1397638 !$#start_codon TTG CLASSIFICATION #superfamily conserved hypothetical protein MJ1427 SUMMARY #length 328 #molecular-weight 36198 #checksum 1179 SEQUENCE /// ENTRY F71066 #type complete TITLE hypothetical protein PH1228 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F71066 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession F71066 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-325 ##label KAW !'##cross-references GB:AP000005; NID:g3236132; PIDN:BAA30328.1; !1PID:g3257645 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1228 CLASSIFICATION #superfamily conserved hypothetical protein MJ1427 SUMMARY #length 325 #molecular-weight 36135 #checksum 141 SEQUENCE /// ENTRY D71246 #type complete TITLE hypothetical protein PH0227 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D71246 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession D71246 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-316 ##label KAW !'##cross-references GB:AP000001; NID:g3236128; PIDN:BAA29299.1; !1PID:g3256616 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0227 CLASSIFICATION #superfamily conserved hypothetical protein MJ1427 SUMMARY #length 316 #molecular-weight 35845 #checksum 1031 SEQUENCE /// ENTRY B64490 #type complete TITLE hypothetical protein homolog MJ1523 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B64490 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession B64490 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-124 ##label BUL !'##cross-references GB:U67593; GB:L77117; NID:g2826427; !1PIDN:AAB99542.1; PID:g1592153; TIGR:MJ1523 GENETICS !$#map_position FOR1501023-1501397 CLASSIFICATION #superfamily hypothetical protein MJ1523 SUMMARY #length 124 #molecular-weight 13534 #checksum 4894 SEQUENCE /// ENTRY A64673 #type complete TITLE conserved hypothetical integral membrane protein HP1225 - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS A64673 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession A64673 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-130 ##label TOM !'##cross-references GB:AE000628; GB:AE000511; NID:g2314386; !1PIDN:AAD08270.1; PID:g2314388; TIGR:HP1225 CLASSIFICATION #superfamily hypothetical protein MJ1523 SUMMARY #length 130 #molecular-weight 14093 #checksum 1864 SEQUENCE /// ENTRY A70341 #type complete TITLE conserved hypothetical protein aq_449 - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A70341 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession A70341 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-124 ##label AQF !'##cross-references GB:AE000690; GB:AE000657; NID:g2983100; !1PIDN:AAC06721.1; PID:g2983116 !'##experimental_source strain VF5 GENETICS !$#gene aq_449 CLASSIFICATION #superfamily hypothetical protein MJ1523 SUMMARY #length 124 #molecular-weight 13362 #checksum 5241 SEQUENCE /// ENTRY F64796 #type complete TITLE crcB protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS F64796 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64796 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-127 ##label BLAT !'##cross-references GB:AE000167; GB:U00096; NID:g1786836; !1PIDN:AAC73725.1; PID:g1786842; UWGP:b0624 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene crcB; ybeI CLASSIFICATION #superfamily hypothetical protein MJ1523 KEYWORDS transmembrane protein FEATURE !$1-17 #domain transmembrane #status predicted #label TM1\ !$37-53 #domain transmembrane #status predicted #label TM2\ !$100-116 #domain transmembrane #status predicted #label TM3 SUMMARY #length 127 #molecular-weight 13777 #checksum 6931 SEQUENCE /// ENTRY G70650 #type complete TITLE hypothetical protein Rv3070 - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G70650 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession G70650 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-126 ##label COL !'##cross-references GB:Z83866; GB:AL123456; NID:g3261691; !1PIDN:CAB06253.1; PID:g1781143 !'##experimental_source strain H37Rv GENETICS !$#gene Rv3070 CLASSIFICATION #superfamily hypothetical protein MJ1523 SUMMARY #length 126 #molecular-weight 13166 #checksum 726 SEQUENCE /// ENTRY D69827 #type complete TITLE hypothetical protein yhdV - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69827 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D69827 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-131 ##label KUN !'##cross-references GB:Z99109; GB:AL009126; NID:g2633260; !1PIDN:CAB12800.1; PID:g2633296 !'##experimental_source strain 168 GENETICS !$#gene yhdV CLASSIFICATION #superfamily hypothetical protein MJ1523 SUMMARY #length 131 #molecular-weight 13905 #checksum 9258 SEQUENCE /// ENTRY B71026 #type complete TITLE hypothetical protein PH1502 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B71026 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession B71026 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-123 ##label KAW !'##cross-references GB:AP000006; NID:g3236133; PIDN:BAA30610.1; !1PID:g3257927 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1502 CLASSIFICATION #superfamily hypothetical protein MJ1523 SUMMARY #length 123 #molecular-weight 13552 #checksum 7307 SEQUENCE /// ENTRY B64537 #type complete TITLE probable iron-sulfur protein HP0138 [similarity] - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B64537 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession B64537 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-481 ##label TOM !'##cross-references GB:AE000535; GB:AE000511; NID:g2313217; !1PIDN:AAD07206.1; PID:g2313222; TIGR:HP0138 CLASSIFICATION #superfamily conserved hypothetical iron-sulfur protein !1HP0138; ferredoxin 2[4Fe-4S] homology KEYWORDS 4Fe-4S; iron-sulfur protein; metalloprotein FEATURE !$314,317,320,374 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$324,364,367,370 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 481 #molecular-weight 54236 #checksum 1429 SEQUENCE /// ENTRY F70039 #type complete TITLE probable iron-sulfur protein yvfW [similarity] - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F70039 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F70039 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-479 ##label KUN !'##cross-references GB:Z99121; GB:AL009126; NID:g2635827; !1PIDN:CAB15409.1; PID:g2635917 !'##experimental_source strain 168 GENETICS !$#gene yvfW CLASSIFICATION #superfamily conserved hypothetical iron-sulfur protein !1HP0138; ferredoxin 2[4Fe-4S] homology KEYWORDS 4Fe-4S; iron-sulfur protein; metalloprotein FEATURE !$303-381 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$313,316,319,373 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$323,363,366,369 #binding_site 4Fe-4S cluster (Cys, Ser, Cys, Cys) !8(covalent) #status predicted SUMMARY #length 479 #molecular-weight 53474 #checksum 4241 SEQUENCE /// ENTRY C69351 #type complete TITLE probable iron-sulfur protein AF0811 [similarity] - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69351 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession C69351 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-364 ##label KLE !'##cross-references GB:AE001048; GB:AE000782; NID:g2689371; !1PIDN:AAB90430.1; PID:g2649796; TIGR:AF0811 CLASSIFICATION #superfamily conserved hypothetical iron-sulfur protein !1HP0138; ferredoxin 2[4Fe-4S] homology KEYWORDS 4Fe-4S; iron-sulfur protein; metalloprotein FEATURE !$286,289,292,343 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$296,333,336,339 #binding_site 4Fe-4S cluster (Cys, Ser, Cys, Cys) !8(covalent) #status predicted SUMMARY #length 364 #molecular-weight 41158 #checksum 1066 SEQUENCE /// ENTRY D69053 #type complete TITLE probable iron-sulfur protein MTH140 [similarity] - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69053 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession D69053 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-396 ##label MTH !'##cross-references GB:AE000803; GB:AE000666; NID:g2621179; !1PIDN:AAB84646.1; PID:g2621181 !'##experimental_source strain Delta H GENETICS !$#gene MTH140 !$#start_codon TTG CLASSIFICATION #superfamily conserved hypothetical iron-sulfur protein !1HP0138; ferredoxin 2[4Fe-4S] homology KEYWORDS 4Fe-4S; iron-sulfur protein; metalloprotein FEATURE !$287-363 #domain ferredoxin 2[4Fe-4S] homology #label FER\ !$294,297,300,355 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$304,345,348,351 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted SUMMARY #length 396 #molecular-weight 42840 #checksum 1550 SEQUENCE /// ENTRY B64498 #type complete TITLE conserved hypothetical protein MJ1587 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B64498 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession B64498 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-171 ##label BUL !'##cross-references GB:U67599; GB:L77117; NID:g2826435; !1PIDN:AAB99616.1; PID:g1500483; TIGR:MJ1587 GENETICS !$#map_position FOR1560754-1561269 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ1587 SUMMARY #length 171 #molecular-weight 19198 #checksum 2039 SEQUENCE /// ENTRY H69063 #type complete TITLE conserved hypothetical protein MTH1478 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H69063 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession H69063 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-154 ##label MTH !'##cross-references GB:AE000908; GB:AE000666; NID:g2622579; !1PIDN:AAB85953.1; PID:g2622593 !'##experimental_source strain Delta H GENETICS !$#gene MTH1478 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ1587 SUMMARY #length 154 #molecular-weight 16618 #checksum 3368 SEQUENCE /// ENTRY A69313 #type complete TITLE conserved hypothetical protein AF0505 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A69313 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession A69313 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-208 ##label KLE !'##cross-references GB:AE001069; GB:AE000782; NID:g2689392; !1PIDN:AAB90733.1; PID:g2650121; TIGR:AF0505 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ1587 SUMMARY #length 208 #molecular-weight 23438 #checksum 3611 SEQUENCE /// ENTRY B64815 #type complete TITLE ybhL protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS B64815 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64815 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-234 ##label BLAT !'##cross-references GB:AE000181; GB:U00096; NID:g1786998; !1PIDN:AAC73873.1; PID:g1787004; UWGP:b0786 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ybhL CLASSIFICATION #superfamily Escherichia coli ybhL protein KEYWORDS transmembrane protein FEATURE !$24-40 #domain transmembrane #status predicted #label TM1\ !$57-73 #domain transmembrane #status predicted #label TM2\ !$103-119 #domain transmembrane #status predicted #label TM3\ !$143-159 #domain transmembrane #status predicted #label TM4\ !$165-181 #domain transmembrane #status predicted #label TM5\ !$209-225 #domain transmembrane #status predicted #label TM6 SUMMARY #length 234 #molecular-weight 25902 #checksum 9438 SEQUENCE /// ENTRY B70167 #type complete TITLE conserved hypothetical integral membrane protein BB0539 - Lyme disease spirochete ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B70167 REFERENCE A70100 !$#authors Fraser, C.M.; Casjens, S.; Huang, W.M.; Sutton, G.G.; !1Clayton, R.; Lathigra, R.; White, O.; Ketchum, K.A.; Dodson, !1R.; Hickey, E.K.; Gwinn, M.; Dougherty, B.; Tomb, J.F.; !1Fleischmann, R.D.; Richardson, D.; Peterson, J.; Kerlavage, !1A.R.; Quackenbush, J.; Salzberg, S.; Hanson, M.; Vugt, R.V.; !1Palmer, N.; Adams, M.D.; Gocayne, J.; Weidman, J.; !1Utterback, T.; Watthey, L.; McDonald, L.; Artiach, P.; !1Bowman, C.; Garland, S.; Fujii, C.; Cotton, M.D.; Horst, K.; !1Roberts, K.; Hatch, B.; Smith, H.O.; Venter, J.C. !$#journal Nature (1997) 390:580-586 !$#title Genomic sequence of a Lyme disease spirochaete, Borrelia !1burgdorferi. !$#cross-references MUID:98065943; PMID:9403685 !$#accession B70167 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-232 ##label KLE !'##cross-references GB:AE001155; GB:AE000783; NID:g2688448; !1PIDN:AAC66898.1; PID:g2688450; TIGR:BB0539 !'##experimental_source strain B31 CLASSIFICATION #superfamily Escherichia coli ybhL protein SUMMARY #length 232 #molecular-weight 25708 #checksum 6705 SEQUENCE /// ENTRY H64634 #type complete TITLE conserved hypothetical integral membrane protein HP0920 - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS H64634 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession H64634 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-230 ##label TOM !'##cross-references GB:AE000601; GB:AE000511; NID:g2314051; !1PIDN:AAD07964.1; PID:g2314055; TIGR:HP0920 CLASSIFICATION #superfamily Escherichia coli ybhL protein SUMMARY #length 230 #molecular-weight 25141 #checksum 2086 SEQUENCE /// ENTRY G69798 #type complete TITLE hypothetical protein yetJ - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 02-Aug-2002 ACCESSIONS G69798 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69798 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-214 ##label KUN !'##cross-references GB:Z99107; GB:AL009126; NID:g2632866; !1PIDN:CAB12539.1; PID:g2633033 !'##experimental_source strain 168 GENETICS !$#gene yetJ CLASSIFICATION #superfamily Escherichia coli ybhL protein SUMMARY #length 214 #molecular-weight 23828 #checksum 9157 SEQUENCE /// ENTRY S44904 #type complete TITLE ZK652.9 protein - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 23-Mar-2001 ACCESSIONS S44904 REFERENCE S44618 !$#authors Du, Z. !$#submission submitted to the EMBL Data Library, May 1993 !$#description Sequence of the C. elegans cosmid ZK652. !$#accession S44904 !'##status preliminary !'##molecule_type DNA !'##residues 1-568 ##label DUZ !'##cross-references EMBL:L14429; NID:g289765; PID:g289770 GENETICS !$#introns 57/1; 144/3; 236/1; 259/2; 285/3; 314/2; 365/2; 529/2 CLASSIFICATION #superfamily ZK652.9 protein; bioC homology FEATURE !$96-203 #domain bioC homology #label BIOC SUMMARY #length 568 #molecular-weight 64529 #checksum 8046 SEQUENCE /// ENTRY B65188 #type complete TITLE Ubiquinone/menaquinone biosynthesis methyltransferase yigO (EC 2.1.1.-) - Escherichia coli (strain K-12) ALTERNATE_NAMES hypothetical protein o251 ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS B65188; S30722 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65188 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-251 ##label BLAT !'##cross-references GB:AE000459; GB:U00096; NID:g2367306; !1PIDN:AAC76836.1; PID:g2367307; UWGP:b3833 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S30660 !$#authors Daniels, D.L.; Plunkett III, G.; Burland, V.; Blattner, F.R. !$#journal Science (1992) 257:771-778 !$#title Analysis of the Escherichia coli genome: DNA sequence of the !1region from 84.5 to 86.5 minutes. !$#cross-references MUID:92358234; PMID:1379743 !$#accession S30722 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-100,'L',102-122,'XX',125-189,'XX',192-251 ##label DAN !'##cross-references EMBL:M87049 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1992 GENETICS !$#gene yigO CLASSIFICATION #superfamily spore germination protein C2; bioC homology KEYWORDS methyltransferase FEATURE !$64-170 #domain bioC homology #label BIOC SUMMARY #length 251 #molecular-weight 28057 #checksum 3932 SEQUENCE /// ENTRY B48583 #type complete TITLE spore germination protein homolog - Leishmania donovani ORGANISM #formal_name Leishmania donovani DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B48583 REFERENCE A48583 !$#authors Joshi, M.; Dwyer, D.M.; Nakhasi, H.L. !$#journal Mol. Biochem. Parasitol. (1993) 58:345-354 !$#title Cloning and characterization of differentially expressed !1genes from in vitro-grown 'amastigotes' of Leishmania !1donovani. !$#cross-references MUID:93241226; PMID:8479459 !$#accession B48583 !'##status preliminary; not compared with conceptual translation !'##molecule_type mRNA !'##residues 1-288 ##label JOS !'##experimental_source amastigote !'##note sequence extracted from NCBI backbone (NCBIP:130078) CLASSIFICATION #superfamily spore germination protein C2; bioC homology FEATURE !$58-176 #domain bioC homology #status atypical #label BIOC SUMMARY #length 288 #molecular-weight 31974 #checksum 9320 SEQUENCE /// ENTRY A70549 #type complete TITLE probable methyltransferase - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A70549 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession A70549 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-234 ##label COL !'##cross-references GB:Z95558; GB:AL123456; NID:g3261781; !1PIDN:CAB08969.1; PID:g2114020 !'##experimental_source strain H37Rv GENETICS !$#gene ubiE CLASSIFICATION #superfamily spore germination protein C2; bioC homology FEATURE !$52-147 #domain bioC homology #label BIOC SUMMARY #length 234 #molecular-weight 25299 #checksum 5812 SEQUENCE /// ENTRY S53962 #type complete TITLE hypothetical protein YML110c - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein YM8339.09c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 22-Oct-1999 ACCESSIONS S53962 REFERENCE S53954 !$#authors Skelton, J.; Churcher, C.M. !$#submission submitted to the EMBL Data Library, May 1995 !$#accession S53962 !'##molecule_type DNA !'##residues 1-307 ##label SKE !'##cross-references EMBL:Z49210; NID:g798881; PID:g798890; !1GSPDB:GN00013; MIPS:YML110c !'##experimental_source strain AB972 GENETICS !$#gene SGD:DBI56; MIPS:YML110c !'##cross-references SGD:S0004578; MIPS:YML110c !$#map_position 13L CLASSIFICATION #superfamily spore germination protein C2; bioC homology FEATURE !$112-227 #domain bioC homology #label BIOC SUMMARY #length 307 #molecular-weight 34684 #checksum 6613 SEQUENCE /// ENTRY B48653 #type complete TITLE hypothetical protein 2 (pip 3' region) - Lactococcus lactis subsp. lactis (strain C2) ORGANISM #formal_name Lactococcus lactis subsp. lactis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B48653 REFERENCE A48653 !$#authors Geller, B.L.; Ivey, R.G.; Trempy, J.E.; Hettinger-Smith, B. !$#journal J. Bacteriol. (1993) 175:5510-5519 !$#title Cloning of a chromosomal gene required for phage infection !1of Lactococcus lactis subsp. lactis C2. !$#cross-references MUID:93374846; PMID:8366036 !$#accession B48653 !'##status preliminary !'##molecule_type DNA !'##residues 1-252 ##label GEL !'##cross-references GB:L14679 CLASSIFICATION #superfamily spore germination protein C2; bioC homology FEATURE !$54-159 #domain bioC homology #label BIOC SUMMARY #length 252 #molecular-weight 28431 #checksum 2794 SEQUENCE /// ENTRY D69630 #type complete TITLE menaquinone biosynthesis methyltransferase gerCB - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69630 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D69630 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-233 ##label KUN !'##cross-references GB:Z99115; GB:AL009126; NID:g2634478; !1PIDN:CAB14191.1; PID:g2634693 !'##experimental_source strain 168 GENETICS !$#gene gerCB CLASSIFICATION #superfamily spore germination protein C2; bioC homology FEATURE !$48-153 #domain bioC homology #label BIOC SUMMARY #length 233 #molecular-weight 26576 #checksum 40 SEQUENCE /// ENTRY S74682 #type complete TITLE spore germination protein c2 - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein sll1653 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S74682 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74682 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-238 ##label KAN !'##cross-references EMBL:D90901; GB:AB001339; NID:g1651897; !1PIDN:BAA16833.1; PID:g1651907 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene gerCb CLASSIFICATION #superfamily spore germination protein C2; bioC homology FEATURE !$53-159 #domain bioC homology #label BIOC SUMMARY #length 238 #molecular-weight 26072 #checksum 2671 SEQUENCE /// ENTRY C64705 #type complete TITLE gerC2 protein - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS C64705 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession C64705 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-246 ##label TOM !'##cross-references GB:AE000647; GB:AE000511; NID:g2314645; !1PIDN:AAD08518.1; PID:g2314655; TIGR:HP1483 CLASSIFICATION #superfamily spore germination protein C2; bioC homology FEATURE !$55-164 #domain bioC homology #label BIOC SUMMARY #length 246 #molecular-weight 27871 #checksum 8177 SEQUENCE /// ENTRY H71222 #type complete TITLE hypothetical protein PH0043 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H71222 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession H71222 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-200 ##label KAW !'##cross-references GB:AP000001; NID:g3236128; PIDN:BAA29111.1; !1PID:g3256428 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0043 CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum conserved !1hypothetical protein MTH1318 SUMMARY #length 200 #molecular-weight 22277 #checksum 380 SEQUENCE /// ENTRY F69275 #type complete TITLE hypothetical protein AF0206 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F69275 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession F69275 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-179 ##label KLE !'##cross-references GB:AE001092; GB:AE000782; NID:g2689415; !1PIDN:AAB91036.1; PID:g2650447; TIGR:AF0206 CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum conserved !1hypothetical protein MTH1318 SUMMARY #length 179 #molecular-weight 19596 #checksum 8482 SEQUENCE /// ENTRY B69042 #type complete TITLE conserved hypothetical protein MTH1318 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69042 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession B69042 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-189 ##label MTH !'##cross-references GB:AE000895; GB:AE000666; NID:g2622403; !1PIDN:AAB85796.1; PID:g2622423 !'##experimental_source strain Delta H GENETICS !$#gene MTH1318 CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum conserved !1hypothetical protein MTH1318 SUMMARY #length 189 #molecular-weight 20995 #checksum 3365 SEQUENCE /// ENTRY B71233 #type complete TITLE hypothetical protein PH0124 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B71233 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession B71233 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-437 ##label KAW !'##cross-references GB:AP000001; NID:g3236128; PIDN:BAA29193.1; !1PID:g3256510 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0124 CLASSIFICATION #superfamily Archaeoglobus fulgidus probable cell division !1control protein 6 SUMMARY #length 437 #molecular-weight 50039 #checksum 3471 SEQUENCE /// ENTRY D69280 #type complete TITLE cell division control protein 6 homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69280 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession D69280 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-409 ##label KLE !'##cross-references GB:AE001089; GB:AE000782; NID:g2689412; !1PIDN:AAB90989.1; PID:g2650397; TIGR:AF0244 CLASSIFICATION #superfamily Archaeoglobus fulgidus probable cell division !1control protein 6 SUMMARY #length 409 #molecular-weight 46413 #checksum 4697 SEQUENCE /// ENTRY B69055 #type complete TITLE probable cell division control protein 6 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69055 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession B69055 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-382 ##label MTH !'##cross-references GB:AE000903; GB:AE000666; NID:g2622514; !1PIDN:AAB85889.1; PID:g2622524 !'##experimental_source strain Delta H GENETICS !$#gene MTH1412 CLASSIFICATION #superfamily Archaeoglobus fulgidus probable cell division !1control protein 6 SUMMARY #length 382 #molecular-weight 43875 #checksum 5482 SEQUENCE /// ENTRY G69336 #type complete TITLE conserved hypothetical protein AF0695 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69336 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession G69336 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-376 ##label KLE !'##cross-references GB:AE001057; GB:AE000782; NID:g2689380; !1PIDN:AAB90547.1; PID:g2649923; TIGR:AF0695 CLASSIFICATION #superfamily Archaeoglobus fulgidus probable cell division !1control protein 6 SUMMARY #length 376 #molecular-weight 42977 #checksum 1658 SEQUENCE /// ENTRY D69080 #type complete TITLE Cdc6 related protein - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69080 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession D69080 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-379 ##label MTH !'##cross-references GB:AE000919; GB:AE000666; NID:g2622717; !1PIDN:AAB86072.1; PID:g2622723 !'##experimental_source strain Delta H GENETICS !$#gene MTH1599 CLASSIFICATION #superfamily Archaeoglobus fulgidus probable cell division !1control protein 6 SUMMARY #length 379 #molecular-weight 43301 #checksum 7413 SEQUENCE /// ENTRY D69228 #type complete TITLE conserved hypothetical protein MTH96 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69228 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession D69228 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-189 ##label MTH !'##cross-references GB:AE000800; GB:AE000666; NID:g2621130; !1PIDN:AAB84609.1; PID:g2621141 !'##experimental_source strain Delta H GENETICS !$#gene MTH96 CLASSIFICATION #superfamily conserved hypothetical protein MTH1332 SUMMARY #length 189 #molecular-weight 21672 #checksum 5946 SEQUENCE /// ENTRY B69060 #type complete TITLE hypothetical protein MTH1450 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69060 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession B69060 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-205 ##label MTH !'##cross-references GB:AE000906; GB:AE000666; NID:g2622557; !1PIDN:AAB85925.1; PID:g2622563 !'##experimental_source strain Delta H GENETICS !$#gene MTH1450 !$#start_codon GTG CLASSIFICATION #superfamily hypothetical protein MTH1450 SUMMARY #length 205 #molecular-weight 22595 #checksum 952 SEQUENCE /// ENTRY F70457 #type complete TITLE hypothetical protein aq_1829 - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F70457 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession F70457 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-141 ##label AQF !'##cross-references GB:AE000758; GB:AE000657; NID:g2984111; !1PIDN:AAC07659.1; PID:g2984122 !'##experimental_source strain VF5 GENETICS !$#gene aq_1829 CLASSIFICATION #superfamily hypothetical protein MTH1450 SUMMARY #length 141 #molecular-weight 15895 #checksum 9361 SEQUENCE /// ENTRY B69066 #type complete TITLE conserved hypothetical protein MTH1494 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69066 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession B69066 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-208 ##label MTH !'##cross-references GB:AE000910; GB:AE000666; NID:g2622610; !1PIDN:AAB85969.1; PID:g2622611 !'##experimental_source strain Delta H GENETICS !$#gene MTH1494 CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum conserved !1hypothetical protein MTH1494 SUMMARY #length 208 #molecular-weight 22283 #checksum 1018 SEQUENCE /// ENTRY F69462 #type complete TITLE hypothetical protein AF1703 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F69462 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession F69462 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-208 ##label KLE !'##cross-references GB:AE000986; GB:AE000782; NID:g2689309; !1PIDN:AAB89558.1; PID:g2648863; TIGR:AF1703 CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum conserved !1hypothetical protein MTH1494 SUMMARY #length 208 #molecular-weight 21841 #checksum 7965 SEQUENCE /// ENTRY B69088 #type complete TITLE conserved hypothetical protein MTH1654 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69088 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession B69088 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-175 ##label MTH !'##cross-references GB:AE000924; GB:AE000666; NID:g2622777; !1PIDN:AAB86126.1; PID:g2622782 !'##experimental_source strain Delta H GENETICS !$#gene MTH1654 CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum conserved !1hypothetical protein MTH1654 SUMMARY #length 175 #molecular-weight 19455 #checksum 478 SEQUENCE /// ENTRY D69377 #type complete TITLE hypothetical protein AF1020 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69377 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession D69377 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-165 ##label KLE !'##cross-references GB:AE001033; GB:AE000782; NID:g2689356; !1PIDN:AAB90227.1; PID:g2649579; TIGR:AF1020 CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum conserved !1hypothetical protein MTH1654 SUMMARY #length 165 #molecular-weight 17739 #checksum 2123 SEQUENCE /// ENTRY B71033 #type complete TITLE hypothetical protein PH1554 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B71033 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession B71033 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-166 ##label KAW !'##cross-references GB:AP000006; NID:g3236133; PIDN:BAA30666.1; !1PID:g3257983 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1554 CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum conserved !1hypothetical protein MTH1654 SUMMARY #length 166 #molecular-weight 18954 #checksum 7342 SEQUENCE /// ENTRY D71206 #type complete TITLE hypothetical protein PH1918 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D71206 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession D71206 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-162 ##label KAW !'##cross-references GB:AP000007; NID:g3236134; PIDN:BAA31043.1; !1PID:g3258360 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1918 CLASSIFICATION #superfamily hypothetical protein MTH699 SUMMARY #length 162 #molecular-weight 17641 #checksum 6715 SEQUENCE /// ENTRY G69552 #type complete TITLE hypothetical protein AF2422 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69552 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession G69552 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-162 ##label KLE !'##cross-references GB:AE001108; GB:AE000782; NID:g2689431; !1PIDN:AAB91249.1; PID:g2650677; TIGR:AF2422 CLASSIFICATION #superfamily hypothetical protein MTH699 SUMMARY #length 162 #molecular-weight 17705 #checksum 8561 SEQUENCE /// ENTRY B69193 #type complete TITLE hypothetical protein MTH699 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69193 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession B69193 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-168 ##label MTH !'##cross-references GB:AE000849; GB:AE000666; NID:g2621780; !1PIDN:AAB85204.1; PID:g2621785 !'##experimental_source strain Delta H GENETICS !$#gene MTH699 CLASSIFICATION #superfamily hypothetical protein MTH699 SUMMARY #length 168 #molecular-weight 18614 #checksum 8359 SEQUENCE /// ENTRY H70797 #type complete TITLE hypothetical protein Rv3735 - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H70797 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession H70797 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-162 ##label COL !'##cross-references GB:AL022121; GB:AL123456; NID:g3261559; !1PIDN:CAA18057.1; PID:g2960159 !'##experimental_source strain H37Rv GENETICS !$#gene Rv3735 CLASSIFICATION #superfamily hypothetical protein MTH699 SUMMARY #length 162 #molecular-weight 17293 #checksum 8231 SEQUENCE /// ENTRY B69350 #type complete TITLE hypothetical protein AF0802 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69350 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession B69350 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-214 ##label KLE !'##cross-references GB:AE001049; GB:AE000782; NID:g2689372; !1PIDN:AAB90445.1; PID:g2649813; TIGR:AF0802 CLASSIFICATION #superfamily hypothetical protein AF0802 SUMMARY #length 214 #molecular-weight 24469 #checksum 8914 SEQUENCE /// ENTRY G70428 #type complete TITLE hypothetical protein aq_1481 - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G70428 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession G70428 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-161 ##label AQF !'##cross-references GB:AE000742; GB:AE000657; NID:g2983858; !1PIDN:AAC07424.1; PID:g2983871 !'##experimental_source strain VF5 GENETICS !$#gene aq_1481 CLASSIFICATION #superfamily hypothetical protein AF0802 SUMMARY #length 161 #molecular-weight 18843 #checksum 7714 SEQUENCE /// ENTRY B69374 #type complete TITLE conserved hypothetical protein AF0994 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69374 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession B69374 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-185 ##label KLE !'##cross-references GB:AE001035; GB:AE000782; NID:g2689358; !1PIDN:AAB90247.1; PID:g2649601; TIGR:AF0994 CLASSIFICATION #superfamily conserved hypothetical protein AF0994 SUMMARY #length 185 #molecular-weight 21203 #checksum 4155 SEQUENCE /// ENTRY F71208 #type complete TITLE hypothetical protein PH1934 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F71208 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession F71208 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-206 ##label KAW !'##cross-references GB:AP000007; NID:g3236134; PIDN:BAA31061.1; !1PID:g3258378 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1934 CLASSIFICATION #superfamily conserved hypothetical protein AF0994 SUMMARY #length 206 #molecular-weight 23550 #checksum 4917 SEQUENCE /// ENTRY E69935 #type complete TITLE conserved hypothetical protein ypgQ - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69935 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69935 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-205 ##label KUN !'##cross-references GB:Z99115; GB:AL009126; NID:g2634478; !1PIDN:CAB14107.1; PID:g2634609 !'##experimental_source strain 168 GENETICS !$#gene ypgQ CLASSIFICATION #superfamily conserved hypothetical protein AF0994 SUMMARY #length 205 #molecular-weight 23122 #checksum 5807 SEQUENCE /// ENTRY F64960 #type complete TITLE membrane protein yedJ - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS F64960 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64960 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-231 ##label BLAT !'##cross-references GB:AE000288; GB:U00096; NID:g2367124; !1PIDN:AAC75028.1; PID:g1788273; UWGP:b1962 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yedJ CLASSIFICATION #superfamily conserved hypothetical protein AF0994 KEYWORDS transmembrane protein FEATURE !$48-64 #domain transmembrane #status predicted #label TM1\ !$135-151 #domain transmembrane #status predicted #label TM2 SUMMARY #length 231 #molecular-weight 25904 #checksum 8997 SEQUENCE /// ENTRY B69375 #type complete TITLE phosphohistidine phosphatase (EC3.1.3.-) sixA-related [similarity] - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 14-Dec-2001 ACCESSIONS B69375 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession B69375 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-151 ##label KLE !'##cross-references GB:AE001035; GB:AE000782; NID:g2689358; !1PIDN:AAB90241.1; PID:g2649595; TIGR:AF1002 CLASSIFICATION #superfamily Escherichia coli phosphohistidine phosphatase !1sixA SUMMARY #length 151 #molecular-weight 17134 #checksum 4004 SEQUENCE /// ENTRY G70400 #type complete TITLE phosphohistidine phosphatase (EC3.1.3.-) sixA-related [similarity] - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 14-Dec-2001 ACCESSIONS G70400 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession G70400 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-149 ##label AQF !'##cross-references GB:AE000727; GB:AE000657; NID:g2983623; !1PIDN:AAC07207.1; PID:g2983639 !'##experimental_source strain VF5 GENETICS !$#gene aq_1173 CLASSIFICATION #superfamily Escherichia coli phosphohistidine phosphatase !1sixA SUMMARY #length 149 #molecular-weight 17008 #checksum 636 SEQUENCE /// ENTRY S74345 #type complete TITLE phosphohistidine phosphatase (EC 3.1.3.-) sixA-related [similarity] - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 31-Dec-2001 ACCESSIONS S74345 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74345 !'##status preliminary !'##molecule_type DNA !'##residues 1-164 ##label KAN !'##cross-references EMBL:D64001; GB:AB001339; NID:g1001102; !1PID:g1001123 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily Escherichia coli phosphohistidine phosphatase !1sixA KEYWORDS phosphoric monoester hydrolase SUMMARY #length 164 #molecular-weight 18270 #checksum 9686 SEQUENCE /// ENTRY B69413 #type complete TITLE conserved hypothetical protein AF1307 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69413 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession B69413 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-264 ##label KLE !'##cross-references GB:AE001013; GB:AE000782; NID:g2689336; !1PIDN:AAB89937.1; PID:g2649269; TIGR:AF1307 CLASSIFICATION #superfamily hypothetical protein AF1307 SUMMARY #length 264 #molecular-weight 29786 #checksum 5210 SEQUENCE /// ENTRY D69513 #type complete TITLE conserved hypothetical protein AF2108 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69513 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession D69513 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-280 ##label KLE !'##cross-references GB:AE000958; GB:AE000782; NID:g2689281; !1PIDN:AAB89140.1; PID:g2648417; TIGR:AF2108 CLASSIFICATION #superfamily hypothetical protein AF1307 SUMMARY #length 280 #molecular-weight 31661 #checksum 9976 SEQUENCE /// ENTRY E64394 #type complete TITLE hypothetical protein MJ0757 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E64394 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession E64394 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-260 ##label BUL !'##cross-references GB:U67521; GB:L77117; NID:g1591463; !1PIDN:AAB98749.1; PID:g1591468; TIGR:MJ0757 GENETICS !$#map_position REV682205-681423 !$#start_codon TTG CLASSIFICATION #superfamily hypothetical protein AF1307 SUMMARY #length 260 #molecular-weight 30434 #checksum 5020 SEQUENCE /// ENTRY B69419 #type complete TITLE hypothetical protein AF1355 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69419 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession B69419 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-315 ##label KLE !'##cross-references GB:AE001010; GB:AE000782; NID:g2689333; !1PIDN:AAB89895.1; PID:g2649224; TIGR:AF1355 CLASSIFICATION #superfamily Archaeoglobus fulgidus conserved hypothetical !1protein AF0472 SUMMARY #length 315 #molecular-weight 36136 #checksum 3827 SEQUENCE /// ENTRY D69474 #type complete TITLE phosphate regulatory protein homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69474 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession D69474 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-321 ##label KLE !'##cross-references GB:AE000979; GB:AE000782; NID:g2689302; !1PIDN:AAB89454.1; PID:g2648752; TIGR:AF1797 CLASSIFICATION #superfamily Archaeoglobus fulgidus conserved hypothetical !1protein AF0472 SUMMARY #length 321 #molecular-weight 36659 #checksum 1270 SEQUENCE /// ENTRY H71246 #type complete TITLE hypothetical protein PH0231 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H71246 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession H71246 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-303 ##label KAW !'##cross-references GB:AP000001; NID:g3236128; PIDN:BAA29303.1; !1PID:g3256620 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0231 CLASSIFICATION #superfamily Archaeoglobus fulgidus conserved hypothetical !1protein AF0472 SUMMARY #length 303 #molecular-weight 35053 #checksum 9678 SEQUENCE /// ENTRY B69349 #type complete TITLE conserved hypothetical protein AF0794 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69349 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession B69349 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-335 ##label KLE !'##cross-references GB:AE001050; GB:AE000782; NID:g2689373; !1PIDN:AAB90455.1; PID:g2649824; TIGR:AF0794 CLASSIFICATION #superfamily Archaeoglobus fulgidus conserved hypothetical !1protein AF0472 SUMMARY #length 335 #molecular-weight 38858 #checksum 4521 SEQUENCE /// ENTRY H69308 #type complete TITLE conserved hypothetical protein AF0472 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H69308 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession H69308 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-320 ##label KLE !'##cross-references GB:AE001071; GB:AE000782; NID:g2689394; !1PIDN:AAB90766.1; PID:g2650156; TIGR:AF0472 CLASSIFICATION #superfamily Archaeoglobus fulgidus conserved hypothetical !1protein AF0472 SUMMARY #length 320 #molecular-weight 37377 #checksum 9403 SEQUENCE /// ENTRY B69510 #type complete TITLE conserved hypothetical protein AF2083 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69510 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession B69510 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-83 ##label KLE !'##cross-references GB:AE000960; GB:AE000782; NID:g2689283; !1PIDN:AAB89173.1; PID:g2648450; TIGR:AF2083 CLASSIFICATION #superfamily hypothetical protein AF2083 SUMMARY #length 83 #molecular-weight 9511 #checksum 2320 SEQUENCE /// ENTRY F69457 #type complete TITLE conserved hypothetical protein AF1663 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F69457 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession F69457 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-96 ##label KLE !'##cross-references GB:AE000989; GB:AE000782; NID:g2689312; !1PIDN:AAB89587.1; PID:g2648895; TIGR:AF1663 CLASSIFICATION #superfamily hypothetical protein AF2083 SUMMARY #length 96 #molecular-weight 11049 #checksum 5048 SEQUENCE /// ENTRY B69526 #type complete TITLE conserved hypothetical protein AF2210 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69526 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession B69526 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-78 ##label KLE !'##cross-references GB:AE000953; GB:AE000782; NID:g2689276; !1PIDN:AAB89053.1; PID:g2648327; TIGR:AF2210 CLASSIFICATION #superfamily hypothetical protein AF2210 SUMMARY #length 78 #molecular-weight 8730 #checksum 5761 SEQUENCE /// ENTRY D69550 #type complete TITLE hypothetical protein AF2403 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69550 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession D69550 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-72 ##label KLE !'##cross-references GB:AE001110; GB:AE000782; NID:g2689433; !1PIDN:AAB91269.1; PID:g2650698; TIGR:AF2403 CLASSIFICATION #superfamily hypothetical protein AF2210 SUMMARY #length 72 #molecular-weight 8252 #checksum 7839 SEQUENCE /// ENTRY B69735 #type complete TITLE PBSX prophage ORF xtrA - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69735 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69735 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-68 ##label KUN !'##cross-references GB:Z99110; GB:AL009126; NID:g2633472; !1PIDN:CAB13112.1; PID:g2633609 !'##experimental_source strain 168 GENETICS !$#gene xtrA CLASSIFICATION #superfamily hypothetical protein yqaO SUMMARY #length 68 #molecular-weight 7750 #checksum 9174 SEQUENCE /// ENTRY F69945 #type complete TITLE phage-related protein homolog yqaO - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F69945 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69945 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-68 ##label KUN !'##cross-references GB:Z99117; GB:AL009126; NID:g2634966; !1PIDN:CAB14565.1; PID:g2635069 !'##experimental_source strain 168 GENETICS !$#gene yqaO CLASSIFICATION #superfamily hypothetical protein yqaO SUMMARY #length 68 #molecular-weight 7613 #checksum 233 SEQUENCE /// ENTRY B69754 #type complete TITLE conserved hypothetical protein ycbP - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69754 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69754 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-128 ##label KUN !'##cross-references GB:Z99105; GB:AL009126; NID:g2632457; !1PIDN:CAB12053.1; PID:g2632545 !'##experimental_source strain 168 GENETICS !$#gene ycbP CLASSIFICATION #superfamily hypothetical protein ycbP SUMMARY #length 128 #molecular-weight 14054 #checksum 9721 SEQUENCE /// ENTRY D69890 #type complete TITLE conserved hypothetical protein yndM - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69890 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D69890 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-179 ##label KUN !'##cross-references GB:Z99113; GB:AL009126; NID:g2634090; !1PIDN:CAB13667.1; PID:g2634167 !'##experimental_source strain 168 GENETICS !$#gene yndM CLASSIFICATION #superfamily hypothetical protein ycbP SUMMARY #length 179 #molecular-weight 20452 #checksum 1245 SEQUENCE /// ENTRY B69838 #type complete TITLE myo-inositol 2-dehydrogenase homolog yisS - Bacillus subtilis ALTERNATE_NAMES degA 3'-region hypothetical protein ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69838; C36940 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69838 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-342 ##label KUN !'##cross-references GB:Z99109; GB:AL009126; NID:g2633260; !1PIDN:CAB12924.1; PID:g2633420 !'##experimental_source strain 168 REFERENCE A36940 !$#authors Bussey, L.B.; Switzer, R.L. !$#journal J. Bacteriol. (1993) 175:6348-6353 !$#title The degA gene product accelerates degradation of Bacillus !1subtilis phosphoribosylpyrophosphate amidotransferase in !1Escherichia coli. !$#cross-references MUID:94012500; PMID:8407808 !$#accession C36940 !'##status preliminary !'##molecule_type DNA !'##residues 1-92 ##label BUS !'##cross-references GB:L08822 GENETICS !$#gene yisS CLASSIFICATION #superfamily Streptomyces griseus strI protein SUMMARY #length 342 #molecular-weight 37483 #checksum 7629 SEQUENCE /// ENTRY D69972 #type complete TITLE opine catabolism homolog yrbE - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69972 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D69972 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-341 ##label KUN !'##cross-references GB:Z99118; GB:AL009126; NID:g2635200; !1PIDN:CAB14737.1; PID:g2635242 !'##experimental_source strain 168 GENETICS !$#gene yrbE CLASSIFICATION #superfamily Streptomyces griseus strI protein SUMMARY #length 341 #molecular-weight 37788 #checksum 2692 SEQUENCE /// ENTRY S17779 #type complete TITLE strI protein - Streptomyces griseus ORGANISM #formal_name Streptomyces griseus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S17779 REFERENCE S17775 !$#authors Mansouri, K.; Piepersberg, W. !$#journal Mol. Gen. Genet. (1991) 228:459-469 !$#title Genetics of streptomycin production in Streptomyces griseus: !1nucleotide sequence of five genes, strFGHIK, including a !1phosphatase gene. !$#cross-references MUID:91375432; PMID:1654502 !$#accession S17779 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-348 ##label MAN !'##cross-references GB:Y00459; GB:S55493; NID:g1621271; PID:g49268 GENETICS !$#gene strI CLASSIFICATION #superfamily Streptomyces griseus strI protein SUMMARY #length 348 #molecular-weight 36709 #checksum 878 SEQUENCE /// ENTRY H69216 #type complete TITLE 3-chlorobenzoate-3,4-dioxygenase dyhydrogenase related protein - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H69216 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession H69216 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-318 ##label MTH !'##cross-references GB:AE000863; GB:AE000666; NID:g2621956; !1PIDN:AAB85373.1; PID:g2621968 !'##experimental_source strain Delta H GENETICS !$#gene MTH875 !$#start_codon TTG CLASSIFICATION #superfamily Streptomyces griseus strI protein SUMMARY #length 318 #molecular-weight 35653 #checksum 1419 SEQUENCE /// ENTRY D71201 #type complete TITLE hypothetical protein PH1881 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D71201 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession D71201 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-371 ##label KAW !'##cross-references GB:AP000007; NID:g3236134; PIDN:BAA31003.1; !1PID:g3258320 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1881 CLASSIFICATION #superfamily Streptomyces griseus strI protein SUMMARY #length 371 #molecular-weight 42125 #checksum 6856 SEQUENCE /// ENTRY C69689 #type complete TITLE response regulator aspartate phosphatase rapH - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69689; I40009 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69689 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-431 ##label KUN !'##cross-references GB:Z99107; GB:AL009126; NID:g2632866; !1PIDN:CAB12503.1; PID:g2632997 !'##experimental_source strain 168 REFERENCE I39994 !$#authors Smith, H.; de Jong, A.; Bron, S.; Venema, G. !$#journal Gene (1988) 70:351-361 !$#title Characterization of signal-sequence-coding regions selected !1from the Bacillus subtilis chromosome. !$#cross-references MUID:89108019; PMID:3145906 !$#accession I40009 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 'MPIK',379-410,'PLESTAAA' ##label RES !'##cross-references GB:M22915; NID:g143699; PID:g143700 GENETICS !$#gene rapH CLASSIFICATION #superfamily response regulator aspartate phosphatase rapA SUMMARY #length 431 #molecular-weight 50119 #checksum 3871 SEQUENCE /// ENTRY H69688 #type complete TITLE response regulator aspartate phosphatase rapE - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H69688 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69688 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-375 ##label KUN !'##cross-references GB:Z99117; GB:AL009126; NID:g2634966; !1PIDN:CAB14524.1; PID:g2635028 !'##experimental_source strain 168 GENETICS !$#gene rapE CLASSIFICATION #superfamily response regulator aspartate phosphatase rapA SUMMARY #length 375 #molecular-weight 44564 #checksum 1606 SEQUENCE /// ENTRY D69689 #type complete TITLE response regulator aspartate phosphatase rapI - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69689 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D69689 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-391 ##label KUN !'##cross-references GB:Z99106; GB:AL009126; NID:g2632653; !1PIDN:CAB12308.1; PID:g2632801 !'##experimental_source strain 168 GENETICS !$#gene rapI CLASSIFICATION #superfamily response regulator aspartate phosphatase rapA SUMMARY #length 391 #molecular-weight 46566 #checksum 5681 SEQUENCE /// ENTRY E69689 #type complete TITLE response regulator aspartate phosphatase rapJ - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69689 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69689 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-373 ##label KUN !'##cross-references GB:Z99105; GB:AL009126; NID:g2632457; !1PIDN:CAB12076.1; PID:g2632568 !'##experimental_source strain 168 GENETICS !$#gene rapJ CLASSIFICATION #superfamily response regulator aspartate phosphatase rapA SUMMARY #length 373 #molecular-weight 44414 #checksum 4341 SEQUENCE /// ENTRY B69689 #type complete TITLE response regulator aspartate phosphatase rapG - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69689 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69689 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-365 ##label KUN !'##cross-references GB:Z99124; GB:AL009126; NID:g2636442; !1PIDN:CAB16067.1; PID:g2636577 !'##experimental_source strain 168 GENETICS !$#gene rapG CLASSIFICATION #superfamily response regulator aspartate phosphatase rapA SUMMARY #length 365 #molecular-weight 42842 #checksum 7813 SEQUENCE /// ENTRY F69689 #type complete TITLE response regulator aspartate phosphatase rapK - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F69689 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69689 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-371 ##label KUN !'##cross-references GB:Z99114; GB:AL009126; NID:g2634230; !1PIDN:CAB13783.1; PID:g2634284 !'##experimental_source strain 168 GENETICS !$#gene rapK CLASSIFICATION #superfamily response regulator aspartate phosphatase rapA SUMMARY #length 371 #molecular-weight 43844 #checksum 4402 SEQUENCE /// ENTRY S58437 #type complete TITLE probable phosphatase - Bacillus subtilis plasmid pLS20 ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S58437 REFERENCE S58436 !$#authors Meijer, W.J.J.; de Boer, A.J.; van Tongeren, S.; Venema, G.; !1Bron, S. !$#journal Nucleic Acids Res. (1995) 23:3214-3223 !$#title Characterization of the replication region of the Bacillus !1subtilis plasmid pLS20: a novel type of replicon. !$#cross-references MUID:95396582; PMID:7667098 !$#accession S58437 !'##status preliminary !'##molecule_type DNA !'##residues 1-368 ##label MEI !'##cross-references EMBL:U26059; NID:g833836; PIDN:AAA84441.1; !1PID:g833837 GENETICS !$#genome plasmid pLS20 CLASSIFICATION #superfamily response regulator aspartate phosphatase rapA SUMMARY #length 368 #molecular-weight 43367 #checksum 1499 SEQUENCE /// ENTRY B69903 #type complete TITLE aromatic metabolite ABC transporter yodE - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69903 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69903 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-303 ##label KUN !'##cross-references GB:Z99114; GB:AL009126; NID:g2634230; !1PIDN:CAB13848.1; PID:g2634349 !'##experimental_source strain 168 GENETICS !$#gene yodE CLASSIFICATION #superfamily Bacillus subtilis probable ABC transporter ydfO SUMMARY #length 303 #molecular-weight 33851 #checksum 2146 SEQUENCE /// ENTRY E69781 #type complete TITLE ABC transporter homolog ydfO - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69781 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69781 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-312 ##label KUN !'##cross-references GB:Z99106; GB:AL009126; NID:g2632653; !1PIDN:CAB12356.1; PID:g2632849 !'##experimental_source strain 168 GENETICS !$#gene ydfO CLASSIFICATION #superfamily Bacillus subtilis probable ABC transporter ydfO SUMMARY #length 312 #molecular-weight 35056 #checksum 1154 SEQUENCE /// ENTRY C69855 #type complete TITLE ABC transporter homolog ykcA - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69855 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69855 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-316 ##label KUN !'##cross-references GB:Z99110; GB:AL009126; NID:g2633472; !1PIDN:CAB13144.1; PID:g2633641 !'##experimental_source strain 168 GENETICS !$#gene ykcA CLASSIFICATION #superfamily Bacillus subtilis probable ABC transporter ydfO SUMMARY #length 316 #molecular-weight 35387 #checksum 6228 SEQUENCE /// ENTRY B69904 #type complete TITLE conserved hypothetical protein yodO - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69904 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69904 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-471 ##label KUN !'##cross-references GB:Z99114; GB:AL009126; NID:g2634230; !1PIDN:CAB13860.1; PID:g2634361 !'##experimental_source strain 168 GENETICS !$#gene yodO CLASSIFICATION #superfamily conserved hypothetical protein yodO SUMMARY #length 471 #molecular-weight 54073 #checksum 4632 SEQUENCE /// ENTRY E70341 #type complete TITLE conserved hypothetical protein aq_454 - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E70341 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession E70341 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-370 ##label AQF !'##cross-references GB:AE000690; GB:AE000657; NID:g2983100; !1PIDN:AAC06722.1; PID:g2983117 !'##experimental_source strain VF5 GENETICS !$#gene aq_454 CLASSIFICATION #superfamily conserved hypothetical protein yodO SUMMARY #length 370 #molecular-weight 43494 #checksum 818 SEQUENCE /// ENTRY H71363 #type complete TITLE conserved hypothetical protein TP0121 - syphilis spirochete ORGANISM #formal_name Treponema pallidum subsp. pallidum #common_name syphilis spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS H71363 REFERENCE A71250 !$#authors Fraser, C.M.; Norris, S.J.; Weinstock, G.M.; White, O.; !1Sutton, G.G.; Dodson, R.; Gwinn, M.; Hickey, E.K.; Clayton, !1R.; Ketchum, K.A.; Sodergren, E.; Hardham, J.M.; McLeod, !1M.P.; Salzberg, S.; Peterson, J.; Khalak, H.; Richardson, !1D.; Howell, J.K.; Chidambaram, M.; Utterback, T.; McDonald, !1L.; Artiach, P.; Bowman, C.; Cotton, M.D.; Fujii, C.; !1Garland, S.; Hatch, B.; Horst, K.; Roberts, K.; Watthey, L.; !1Weidman, J.; Smith, H.O.; Venter, J.C. !$#journal Science (1998) 281:375-388 !$#title Complete genome sequence of Treponema pallidum, the syphilis !1spirochete. !$#cross-references MUID:98332770; PMID:9665876 !$#accession H71363 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-355 ##label COL !'##cross-references GB:AE001197; GB:AE000520; NID:g3322382; !1PIDN:AAC65111.1; PID:g3322385 !'##experimental_source strain Nichols GENETICS !$#gene TP0121 CLASSIFICATION #superfamily conserved hypothetical protein yodO SUMMARY #length 355 #molecular-weight 39102 #checksum 7800 SEQUENCE /// ENTRY S56374 #type complete TITLE hypothetical 38.7K protein (mopa-efp intergenic region) - Escherichia coli (strain K-12) ALTERNATE_NAMES hypothetical protein f342 ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS S56374; H65224 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56374 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-342 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97045.1; !1PID:g536990 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65224 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-342 ##label BLAT !'##cross-references GB:AE000487; GB:U00096; NID:g1790582; !1PIDN:AAC77106.1; PID:g1790589; UWGP:b4146 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yjeK CLASSIFICATION #superfamily conserved hypothetical protein yodO SUMMARY #length 342 #molecular-weight 38749 #checksum 4245 SEQUENCE /// ENTRY H70440 #type complete TITLE conserved hypothetical protein aq_1632 - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H70440 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession H70440 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-374 ##label AQF !'##cross-references GB:AE000748; GB:AE000657; NID:g2983960; !1PIDN:AAC07521.1; PID:g2983974 !'##experimental_source strain VF5 GENETICS !$#gene aq_1632 CLASSIFICATION #superfamily conserved hypothetical protein yodO SUMMARY #length 374 #molecular-weight 43370 #checksum 5198 SEQUENCE /// ENTRY B70022 #type complete TITLE acyloate catabolism homolog yusQ - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B70022 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B70022 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-127 ##label KUN !'##cross-references GB:Z99120; GB:AL009126; NID:g2635613; !1PIDN:CAB15278.1; PID:g2635785 !'##experimental_source strain 168 GENETICS !$#gene yusQ CLASSIFICATION #superfamily hypothetical protein yrdN SUMMARY #length 127 #molecular-weight 15253 #checksum 9361 SEQUENCE /// ENTRY E69973 #type complete TITLE hypothetical protein yrdN - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69973 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69973 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-129 ##label KUN !'##cross-references GB:Z99117; GB:AL009126; NID:g2634966; !1PIDN:CAB14607.1; PID:g2635111 !'##experimental_source strain 168 GENETICS !$#gene yrdN CLASSIFICATION #superfamily hypothetical protein yrdN SUMMARY #length 129 #molecular-weight 14682 #checksum 8825 SEQUENCE /// ENTRY B70058 #type complete TITLE conserved hypothetical protein ywhK - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B70058 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B70058 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-451 ##label KUN !'##cross-references GB:Z99123; GB:AL009126; NID:g2636240; !1PIDN:CAB15772.1; PID:g2636281 !'##experimental_source strain 168 GENETICS !$#gene ywhK CLASSIFICATION #superfamily hypothetical protein ywhK SUMMARY #length 451 #molecular-weight 49367 #checksum 9538 SEQUENCE /// ENTRY C70058 #type complete TITLE conserved hypothetical protein ywhL - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C70058 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C70058 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-458 ##label KUN !'##cross-references GB:Z99123; GB:AL009126; NID:g2636240; !1PIDN:CAB15771.1; PID:g2636280 !'##experimental_source strain 168 GENETICS !$#gene ywhL CLASSIFICATION #superfamily hypothetical protein ywhK SUMMARY #length 458 #molecular-weight 49580 #checksum 9767 SEQUENCE /// ENTRY E69216 #type complete TITLE conserved hypothetical protein MTH872 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69216 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession E69216 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-283 ##label MTH !'##cross-references GB:AE000863; GB:AE000666; NID:g2621956; !1PIDN:AAB85370.1; PID:g2621965 !'##experimental_source strain Delta H GENETICS !$#gene MTH872 CLASSIFICATION #superfamily conserved hypothetical protein HI0072 SUMMARY #length 283 #molecular-weight 31603 #checksum 6760 SEQUENCE /// ENTRY B65040 #type complete TITLE yfjB protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS B65040 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65040 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-292 ##label BLAT !'##cross-references GB:AE000347; GB:U00096; NID:g2367142; !1PIDN:AAC75664.1; PID:g1788968; UWGP:b2615 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yfjB CLASSIFICATION #superfamily conserved hypothetical protein HI0072 SUMMARY #length 292 #molecular-weight 32566 #checksum 3133 SEQUENCE /// ENTRY I64141 #type complete TITLE hypothetical protein HI0072 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS I64141 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession I64141 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-285 ##label TIGR !'##cross-references GB:L42023; TIGR:HI0072 !'##note best homolog was a hypothetical protein from Escherichia coli CLASSIFICATION #superfamily conserved hypothetical protein HI0072 SUMMARY #length 285 #molecular-weight 31827 #checksum 7693 SEQUENCE /// ENTRY G71101 #type complete TITLE hypothetical protein PH1074 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G71101 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession G71101 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-277 ##label KAW !'##cross-references GB:AP000004; NID:g3236131; PIDN:BAA30173.1; !1PID:g3257490 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1074 CLASSIFICATION #superfamily conserved hypothetical protein HI0072 SUMMARY #length 277 #molecular-weight 31414 #checksum 6268 SEQUENCE /// ENTRY D70378 #type complete TITLE conserved hypothetical protein aq_909 - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D70378 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession D70378 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-274 ##label AQF !'##cross-references GB:AE000713; GB:AE000657; NID:g2983424; !1PIDN:AAC07026.1; PID:g2983444 !'##experimental_source strain VF5 GENETICS !$#gene aq_909 CLASSIFICATION #superfamily conserved hypothetical protein HI0072 SUMMARY #length 274 #molecular-weight 31327 #checksum 8202 SEQUENCE /// ENTRY B69990 #type complete TITLE conserved hypothetical protein ytdI - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69990 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69990 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-267 ##label KUN !'##cross-references GB:Z99119; GB:AL009126; NID:g2635411; !1PIDN:CAB14932.1; PID:g2635438 !'##experimental_source strain 168 GENETICS !$#gene ytdI CLASSIFICATION #superfamily conserved hypothetical protein HI0072 SUMMARY #length 267 #molecular-weight 30253 #checksum 4836 SEQUENCE /// ENTRY F69844 #type complete TITLE conserved hypothetical protein yjbN - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F69844 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69844 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-266 ##label KUN !'##cross-references GB:Z99110; GB:AL009126; NID:g2633472; !1PIDN:CAB13018.1; PID:g2633515 !'##experimental_source strain 168 GENETICS !$#gene yjbN CLASSIFICATION #superfamily conserved hypothetical protein HI0072 SUMMARY #length 266 #molecular-weight 30012 #checksum 9264 SEQUENCE /// ENTRY B64214 #type complete TITLE hypothetical protein homolog MG128 - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 07-Dec-1999 ACCESSIONS B64214 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession B64214 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-259 ##label TIGR !'##cross-references GB:U39691; GB:L43967; NID:g1045794; PID:g1045808; !1TIGR:MG128 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily conserved hypothetical protein HI0072 SUMMARY #length 259 #molecular-weight 29199 #checksum 9625 SEQUENCE /// ENTRY S73892 #type complete TITLE hypothetical protein HI0072 homolog A65_orf259 - Mycoplasma pneumoniae (strain ATCC 29342) ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S73892 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73892 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-259 ##label HIM !'##cross-references EMBL:AE000056; GB:U00089; NID:g1674263; !1PIDN:AAB96214.1; PID:g1674266 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily conserved hypothetical protein HI0072 SUMMARY #length 259 #molecular-weight 29033 #checksum 9283 SEQUENCE /// ENTRY C69796 #type complete TITLE conserved hypothetical protein yesL - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69796 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69796 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-209 ##label KUN !'##cross-references GB:Z99107; GB:AL009126; NID:g2632866; !1PIDN:CAB12513.1; PID:g2633007 !'##experimental_source strain 168 GENETICS !$#gene yesL CLASSIFICATION #superfamily Bacillus subtilis conserved hypothetical !1protein yesL SUMMARY #length 209 #molecular-weight 23436 #checksum 2220 SEQUENCE /// ENTRY D69991 #type complete TITLE conserved hypothetical protein yteU - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69991 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D69991 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-222 ##label KUN !'##cross-references GB:Z99119; GB:AL009126; NID:g2635411; !1PIDN:CAB14987.1; PID:g2635493 !'##experimental_source strain 168 GENETICS !$#gene yteU CLASSIFICATION #superfamily Bacillus subtilis conserved hypothetical !1protein yesL SUMMARY #length 222 #molecular-weight 25933 #checksum 8892 SEQUENCE /// ENTRY E69797 #type complete TITLE conserved hypothetical protein yesV - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69797 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69797 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-208 ##label KUN !'##cross-references GB:Z99107; GB:AL009126; NID:g2632866; !1PIDN:CAB12523.1; PID:g2633017 !'##experimental_source strain 168 GENETICS !$#gene yesV CLASSIFICATION #superfamily Bacillus subtilis conserved hypothetical !1protein yesL SUMMARY #length 208 #molecular-weight 23166 #checksum 1841 SEQUENCE /// ENTRY B64030 #type complete TITLE hypothetical protein HI1450 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Dec-2002 ACCESSIONS B64030 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession B64030 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-107 ##label TIGR !'##cross-references GB:U32823; GB:L42023; NID:g1574281; !1PIDN:AAC23100.1; PID:g1574289; TIGR:HI1450 CLASSIFICATION #superfamily uncharacterized conserved protein SUMMARY #length 107 #molecular-weight 12525 #checksum 7206 SEQUENCE /// ENTRY C64872 #type complete TITLE hypothetical protein b1248 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Dec-2002 ACCESSIONS C64872 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64872 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-135 ##label BLAT !'##cross-references GB:AE000223; GB:U00096; NID:g1787496; !1PIDN:AAC74330.1; PID:g1787501; UWGP:b1248 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily uncharacterized conserved protein SUMMARY #length 135 #molecular-weight 15490 #checksum 2069 SEQUENCE /// ENTRY H64404 #type complete TITLE hypothetical protein MJ0840 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H64404 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession H64404 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-330 ##label BUL !'##cross-references GB:U67528; GB:L77117; NID:g2826335; !1PIDN:AAB98845.1; PID:g1591527; TIGR:MJ0840 GENETICS !$#map_position FOR765985-766977 !$#start_codon GTG CLASSIFICATION #superfamily conserved hypothetical protein MJ0840 SUMMARY #length 330 #molecular-weight 37376 #checksum 4870 SEQUENCE /// ENTRY C69211 #type complete TITLE conserved hypothetical protein MTH834 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69211 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession C69211 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-343 ##label MTH !'##cross-references GB:AE000860; GB:AE000666; NID:g2621915; !1PIDN:AAB85332.1; PID:g2621924 !'##experimental_source strain Delta H GENETICS !$#gene MTH834 CLASSIFICATION #superfamily conserved hypothetical protein MJ0840 SUMMARY #length 343 #molecular-weight 37020 #checksum 6827 SEQUENCE /// ENTRY G69309 #type complete TITLE conserved hypothetical protein AF0479 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69309 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession G69309 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-355 ##label KLE !'##cross-references GB:AE001071; GB:AE000782; NID:g2689394; !1PIDN:AAB90759.1; PID:g2650148; TIGR:AF0479 CLASSIFICATION #superfamily conserved hypothetical protein MJ0840 SUMMARY #length 355 #molecular-weight 39883 #checksum 7748 SEQUENCE /// ENTRY G64313 #type complete TITLE protein-export membrane protein - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G64313 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession G64313 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-396 ##label BUL !'##cross-references GB:U67468; GB:L77117; NID:g1590882; !1PIDN:AAB98092.1; PID:g1590887; TIGR:MJ0111 GENETICS !$#map_position FOR106958-108148 CLASSIFICATION #superfamily Methanococcus jannaschii protein-export !1membrane protein SUMMARY #length 396 #molecular-weight 43052 #checksum 3868 SEQUENCE /// ENTRY C69213 #type complete TITLE protein-export membrane protein, SecD - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69213 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession C69213 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-403 ##label MTH !'##cross-references GB:AE000861; GB:AE000666; NID:g2621930; !1PIDN:AAB85347.1; PID:g2621940 !'##experimental_source strain Delta H GENETICS !$#gene MTH849 CLASSIFICATION #superfamily Methanococcus jannaschii protein-export !1membrane protein SUMMARY #length 403 #molecular-weight 42862 #checksum 4329 SEQUENCE /// ENTRY F65116 #type complete TITLE tldD protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 29-Jan-1999 #sequence_revision 29-Jan-1999 #text_change 01-Mar-2002 ACCESSIONS F65116 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65116 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-481 ##label BLAT !'##cross-references GB:AE000403; GB:U00096; NID:g2367205; !1PIDN:AAC76276.1; PID:g1789640; UWGP:b3244 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene tldD CLASSIFICATION #superfamily Escherichia coli tldD protein SUMMARY #length 481 #molecular-weight 51364 #checksum 9754 SEQUENCE /// ENTRY G70473 #type complete TITLE tldD homolog - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 29-Jan-1999 #sequence_revision 29-Jan-1999 #text_change 23-Jul-1999 ACCESSIONS G70473 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession G70473 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-404 ##label AQF !'##cross-references GB:AE000768; NID:g2984249; PIDN:AAC07784.1; !1PID:g2984257; GB:AE000657 !'##experimental_source strain VF5 GENETICS !$#gene tldD CLASSIFICATION #superfamily Escherichia coli tldD protein SUMMARY #length 404 #molecular-weight 44580 #checksum 4808 SEQUENCE /// ENTRY D64424 #type complete TITLE tldD homolog MJ0996 - Methanococcus jannaschii ALTERNATE_NAMES zinc metalloproteinase homolog ORGANISM #formal_name Methanococcus jannaschii DATE 29-Jan-1999 #sequence_revision 29-Jan-1999 #text_change 01-Feb-1999 ACCESSIONS D64424 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession D64424 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-451 ##label BUL !'##cross-references GB:U67542; GB:L77117; NID:g1591655; PID:g1499836; !1TIGR:MJ0996 GENETICS !$#gene MJ0996 !$#map_position FOR924376-925731 CLASSIFICATION #superfamily Escherichia coli tldD protein SUMMARY #length 451 #molecular-weight 49810 #checksum 1082 SEQUENCE /// ENTRY S70839 #type fragment TITLE tldD homolog - Bradyrhizobium japonicum (fragment) ORGANISM #formal_name Bradyrhizobium japonicum DATE 29-Jan-1999 #sequence_revision 29-Jan-1999 #text_change 23-Jul-1999 ACCESSIONS S70839 REFERENCE S70839 !$#authors Mueller, P.; Ahrens, K.; Keller, T.; Klaucke, A. !$#journal Mol. Microbiol. (1995) 18:831-840 !$#title A TnphoA insertion within the Bradyrhizobium japonicum sipS !1gene, homologous to prokaryotic signal peptidases, results !1in extensive changes in the expression of PBM-specific !1nodulins of infected soybean (Glycine max) cells. !$#cross-references MUID:96422470; PMID:8825087 !$#accession S70839 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-313 ##label MUE !'##cross-references EMBL:U33883; NID:g1200339; PIDN:AAC43985.1; !1PID:g1200340 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1995 CLASSIFICATION #superfamily Escherichia coli tldD protein SUMMARY #length 313 #checksum 8324 SEQUENCE /// ENTRY C69214 #type complete TITLE zinc metalloproteinase - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 29-Jan-1999 #sequence_revision 29-Jan-1999 #text_change 23-Jul-1999 ACCESSIONS C69214 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession C69214 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-454 ##label MTH !'##cross-references GB:AE000862; GB:AE000666; NID:g2621943; !1PIDN:AAB85354.1; PID:g2621948 !'##experimental_source strain Delta H GENETICS !$#gene MTH856 CLASSIFICATION #superfamily Escherichia coli tldD protein SUMMARY #length 454 #molecular-weight 48154 #checksum 4866 SEQUENCE /// ENTRY G71248 #type complete TITLE tldD homolog PH0246 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 29-Jan-1999 #sequence_revision 29-Jan-1999 #text_change 21-Jul-2000 ACCESSIONS G71248 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession G71248 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-504 ##label KAW !'##cross-references GB:AP000001; NID:g3236128; PIDN:BAA29318.1; !1PID:g3256635 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0246 CLASSIFICATION #superfamily Escherichia coli tldD protein SUMMARY #length 504 #molecular-weight 55950 #checksum 6137 SEQUENCE /// ENTRY G69331 #type complete TITLE conserved hypothetical protein AF0655 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 29-Jan-1999 #sequence_revision 29-Jan-1999 #text_change 23-Jul-1999 ACCESSIONS G69331 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession G69331 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-425 ##label KLE !'##cross-references GB:AE001059; GB:AE000782; NID:g2689382; !1PIDN:AAB90585.1; PID:g2649963; TIGR:AF0655 CLASSIFICATION #superfamily Escherichia coli tldD protein SUMMARY #length 425 #molecular-weight 47187 #checksum 5308 SEQUENCE /// ENTRY D71135 #type complete TITLE tldD-related protein PH0848 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 29-Jan-1999 #sequence_revision 29-Jan-1999 #text_change 16-Jun-2000 ACCESSIONS D71135 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession D71135 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-481 ##label KAW !'##cross-references GB:AP000003; NID:g3236130; PIDN:BAA29942.1; !1PID:g3257259 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0848 CLASSIFICATION #superfamily Escherichia coli tldD protein SUMMARY #length 481 #molecular-weight 54442 #checksum 5941 SEQUENCE /// ENTRY E71033 #type complete TITLE tldD-related protein PH1557 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 29-Jan-1999 #sequence_revision 29-Jan-1999 #text_change 21-Jul-2000 ACCESSIONS E71033 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession E71033 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-458 ##label KAW !'##cross-references GB:AP000006; NID:g3236133; PIDN:BAA30669.1; !1PID:g3257986 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1557 CLASSIFICATION #superfamily Escherichia coli tldD protein SUMMARY #length 458 #molecular-weight 51662 #checksum 1163 SEQUENCE /// ENTRY S74845 #type complete TITLE tldD homolog slr0863 - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 29-Jan-1999 #sequence_revision 29-Jan-1999 #text_change 16-Jun-2000 ACCESSIONS S74845 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74845 !'##molecule_type DNA !'##residues 1-463 ##label KAN !'##cross-references EMBL:D90909; GB:AB001339; NID:g1652844; !1PIDN:BAA17806.1; PID:g1652888 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily Escherichia coli tldD protein SUMMARY #length 463 #molecular-weight 50369 #checksum 5364 SEQUENCE /// ENTRY D70703 #type complete TITLE tldD homolog Rv2315c - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 29-Jan-1999 #sequence_revision 29-Jan-1999 #text_change 16-Jun-2000 ACCESSIONS D70703 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession D70703 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-505 ##label COL !'##cross-references GB:Z79702; GB:AL123456; NID:g3261642; !1PIDN:CAB02052.1; PID:g1524285 !'##experimental_source strain H37Rv GENETICS !$#gene Rv2315c CLASSIFICATION #superfamily Escherichia coli tldD protein SUMMARY #length 505 #molecular-weight 54578 #checksum 3909 SEQUENCE /// ENTRY S75512 #type complete TITLE hypothetical protein slr1322 - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S75512 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75512 !'##status preliminary !'##molecule_type DNA !'##residues 1-489 ##label KAN !'##cross-references EMBL:D90911; GB:AB001339; NID:g1653083; !1PIDN:BAA18073.1; PID:g1653157 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily Escherichia coli tldD protein SUMMARY #length 489 #molecular-weight 53129 #checksum 6920 SEQUENCE /// ENTRY S13730 #type complete TITLE pmbA protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 29-Jan-1999 #sequence_revision 29-Jan-1999 #text_change 01-Mar-2002 ACCESSIONS S13730; S56461; F65235 REFERENCE S13730 !$#authors Rodriguez-Sainz, M.C.; Hernandez-Chico, C.; Moreno, F. !$#journal Mol. Microbiol. (1990) 4:1921-1932 !$#title Molecular characterization of pmbA, an Escherichia coli !1chromosomal gene required for the production of the !1antibiotic peptide MccB17. !$#cross-references MUID:91186828; PMID:2082149 !$#accession S13730 !'##molecule_type DNA !'##residues 1-450 ##label ROD !'##cross-references EMBL:X54152; NID:g42439; PIDN:CAA38091.1; !1PID:g42440 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56461 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-450 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97132.1; !1PID:g537077 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65235 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-450 ##label BLAT !'##cross-references GB:AE000494; GB:U00096; NID:g1790670; !1PIDN:AAC77192.1; PID:g1790682; UWGP:b4235 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene pmbA !$#map_position 96 min CLASSIFICATION #superfamily Escherichia coli pmbA protein SUMMARY #length 450 #molecular-weight 48369 #checksum 1212 SEQUENCE /// ENTRY C64186 #type complete TITLE pmbA protein - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 29-Jan-1999 #sequence_revision 29-Jan-1999 #text_change 23-Jul-1999 ACCESSIONS C64186 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession C64186 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-451 ##label TIGR !'##cross-references GB:U32795; GB:L42023; NID:g1574708; !1PIDN:AAC22807.1; PID:g1574709; TIGR:HI1152 GENETICS !$#gene pmbA CLASSIFICATION #superfamily Escherichia coli pmbA protein SUMMARY #length 451 #molecular-weight 48497 #checksum 5177 SEQUENCE /// ENTRY E70461 #type complete TITLE pmbA protein - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 29-Jan-1999 #sequence_revision 29-Jan-1999 #text_change 23-Jul-1999 ACCESSIONS E70461 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession E70461 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-441 ##label AQF !'##cross-references GB:AE000761; NID:g2984149; PIDN:AAC07693.1; !1PID:g2984159; GB:AE000657 !'##experimental_source strain VF5 GENETICS !$#gene pmbA CLASSIFICATION #superfamily Escherichia coli pmbA protein SUMMARY #length 441 #molecular-weight 49573 #checksum 9768 SEQUENCE /// ENTRY B69009 #type complete TITLE conserved hypothetical protein MTH1070 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 29-Jan-1999 #sequence_revision 29-Jan-1999 #text_change 23-Jul-1999 ACCESSIONS B69009 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession B69009 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-430 ##label MTH !'##cross-references GB:AE000877; GB:AE000666; NID:g2622157; !1PIDN:AAB85559.1; PID:g2622168 !'##experimental_source strain Delta H GENETICS !$#gene MTH1070 CLASSIFICATION #superfamily conserved hypothetical protein MTH1070 SUMMARY #length 430 #molecular-weight 46062 #checksum 1394 SEQUENCE /// ENTRY H64328 #type complete TITLE hypothetical protein MJ0231 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 29-Jan-1999 #sequence_revision 29-Jan-1999 #text_change 21-Jul-2000 ACCESSIONS H64328 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession H64328 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-416 ##label BUL !'##cross-references GB:U67479; GB:L77117; NID:g1590965; !1PIDN:AAB98219.1; PID:g1590966; TIGR:MJ0231 GENETICS !$#map_position REV222794-221544 CLASSIFICATION #superfamily conserved hypothetical protein MTH1070 SUMMARY #length 416 #molecular-weight 46660 #checksum 3538 SEQUENCE /// ENTRY H69331 #type complete TITLE hypothetical protein AF0656 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 29-Jan-1999 #sequence_revision 29-Jan-1999 #text_change 23-Jul-1999 ACCESSIONS H69331 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession H69331 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-391 ##label KLE !'##cross-references GB:AE001059; GB:AE000782; NID:g2689382; !1PIDN:AAB90584.1; PID:g2649962; TIGR:AF0656 CLASSIFICATION #superfamily conserved hypothetical protein MTH1070 SUMMARY #length 391 #molecular-weight 42906 #checksum 7679 SEQUENCE /// ENTRY B71249 #type complete TITLE hypothetical protein PH0249 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 29-Jan-1999 #sequence_revision 29-Jan-1999 #text_change 21-Jul-2000 ACCESSIONS B71249 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession B71249 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-426 ##label KAW !'##cross-references GB:AP000001; NID:g3236128; PIDN:BAA29321.1; !1PID:g3256638 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0249 CLASSIFICATION #superfamily conserved hypothetical protein MTH1070 SUMMARY #length 426 #molecular-weight 47253 #checksum 3146 SEQUENCE /// ENTRY F71033 #type complete TITLE hypothetical protein PH1558 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 29-Jan-1999 #sequence_revision 29-Jan-1999 #text_change 21-Jul-2000 ACCESSIONS F71033 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession F71033 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-445 ##label KAW !'##cross-references GB:AP000006; NID:g3236133; PIDN:BAA30670.1; !1PID:g3257987 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1558 CLASSIFICATION #superfamily conserved hypothetical protein MTH1070 SUMMARY #length 445 #molecular-weight 49409 #checksum 968 SEQUENCE /// ENTRY G69282 #type complete TITLE hypothetical protein AF0263 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69282 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession G69282 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-490 ##label KLE !'##cross-references GB:AE001087; GB:AE000782; NID:g2689410; !1PIDN:AAB90972.1; PID:g2650378; TIGR:AF0263 CLASSIFICATION #superfamily Aquifex aeolicus glucose-1-phosphate !1thymidylyltransferase SUMMARY #length 490 #molecular-weight 54559 #checksum 9695 SEQUENCE /// ENTRY E71065 #type complete TITLE hypothetical protein PH1219 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E71065 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession E71065 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-423 ##label KAW !'##cross-references GB:AP000005; NID:g3236132; PIDN:BAA30319.1; !1PID:g3257636 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1219 CLASSIFICATION #superfamily Aquifex aeolicus glucose-1-phosphate !1thymidylyltransferase SUMMARY #length 423 #molecular-weight 48147 #checksum 5155 SEQUENCE /// ENTRY H70418 #type complete TITLE glucose-1-phosphate thymidylyltransferase - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H70418 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession H70418 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-428 ##label AQF !'##cross-references GB:AE000737; GB:AE000657; NID:g2983782; !1PIDN:AAC07344.1; PID:g2983786 !'##experimental_source strain VF5 GENETICS !$#gene spsI CLASSIFICATION #superfamily Aquifex aeolicus glucose-1-phosphate !1thymidylyltransferase SUMMARY #length 428 #molecular-weight 48500 #checksum 2649 SEQUENCE /// ENTRY S70213 #type complete TITLE hypothetical protein 4 - Photobacterium sp. ORGANISM #formal_name Photobacterium sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S70213 REFERENCE S70210 !$#authors Chi, E.; Bartlett, D.H. !$#journal Mol. Microbiol. (1995) 17:713-726 !$#title An rpoE-like locus controls outer membrane protein synthesis !1and growth at cold temperatures and high pressures in the !1deep-sea bacterium Photobacterium SS9. !$#cross-references MUID:96111491; PMID:8801425 !$#accession S70213 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-165 ##label CHI !'##cross-references EMBL:L41667; NID:g777746; PID:g777750 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1995 CLASSIFICATION #superfamily Escherichia coli sigma-E factor regulatory !1protein rseC SUMMARY #length 165 #molecular-weight 17450 #checksum 3809 SEQUENCE /// ENTRY I83299 #type complete TITLE sigma-E factor regulatory protein rseC - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS I83299; A65035 REFERENCE I60227 !$#authors Raina, S.; Missiakas, D.; Georgopoulos, C. !$#journal EMBO J. (1995) 14:1043-1055 !$#title The rpoE gene encoding the sigma E (sigma 24) heat shock !1sigma factor of Escherichia coli. !$#cross-references MUID:95196748; PMID:7889935 !$#accession I83299 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-159 ##label RES !'##cross-references EMBL:U37089; NID:g1045627; PIDN:AAC45317.1; !1PID:g1045631 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65035 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-159 ##label BLAT !'##cross-references GB:AE000343; GB:U00096; NID:g2367139; !1PIDN:AAC75623.1; PID:g1788923; UWGP:b2570 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene rseC CLASSIFICATION #superfamily Escherichia coli sigma-E factor regulatory !1protein rseC SUMMARY #length 159 #molecular-weight 16639 #checksum 8348 SEQUENCE /// ENTRY A70330 #type complete TITLE CysQ protein - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A70330 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession A70330 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-268 ##label AQF !'##cross-references GB:AE000684; GB:AE000657; NID:g2983009; !1PIDN:AAC06626.1; PID:g2983015 !'##experimental_source strain VF5 GENETICS !$#gene cysQ CLASSIFICATION #superfamily Aquifex aeolicus cysQ protein SUMMARY #length 268 #molecular-weight 30602 #checksum 1925 SEQUENCE /// ENTRY S56439 #type complete TITLE ammonium transport system structural protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS S56439; A65233; A49759; A41962 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56439 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-246 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97110.1; !1PID:g537055 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65233 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-246 ##label BLAT !'##cross-references GB:AE000492; GB:U00096; NID:g1790649; !1PIDN:AAC77171.1; PID:g1790659; UWGP:b4214 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A49759 !$#authors Fabiny, J.M.; Jayakumar, A.; Chinault, A.C.; Barnes Jr., !1E.M. !$#journal J. Gen. Microbiol. (1991) 137:983-989 !$#title Ammonium transport in Escherichia coli: localization and !1nucleotide sequence of the amtA gene. !$#cross-references MUID:91311397; PMID:1856684 !$#accession A49759 !'##status preliminary !'##molecule_type DNA !'##residues 1-192,'HV',195-246 ##label FAB !'##cross-references GB:M55170; NID:g145274; PIDN:AAA23444.1; !1PID:g145275 REFERENCE A41962 !$#authors Neuwald, A.F.; Krishnan, B.R.; Brikun, I.; Kulakauskas, S.; !1Suziedelis, K.; Tomcsanyi, T.; Leyh, T.S.; Berg, D.E. !$#journal J. Bacteriol. (1992) 174:415-425 !$#title cysQ, a gene needed for cysteine synthesis in Escherichia !1coli K-12 only during aerobic growth. !$#cross-references MUID:92105007; PMID:1729235 !$#accession A41962 !'##status preliminary !'##molecule_type DNA !'##residues 1-140,'E',142-192,'HV',195-246 ##label NEU !'##experimental_source strain K-12 !'##note sequence inconsistent with the nucleotide translation !'##note sequence extracted from NCBI backbone (NCBIN:75603, !1NCBIP:75607) GENETICS !$#gene cysQ; amtA CLASSIFICATION #superfamily Aquifex aeolicus cysQ protein KEYWORDS ammonium transport SUMMARY #length 246 #molecular-weight 27176 #checksum 3493 SEQUENCE /// ENTRY F64077 #type complete TITLE cysQ protein homolog - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS F64077 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession F64077 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-228 ##label TIGR !'##cross-references GB:U32737; GB:L42023; NID:g1573536; !1PIDN:AAC22214.1; PID:g1573544; TIGR:HI0559 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily Aquifex aeolicus cysQ protein SUMMARY #length 228 #molecular-weight 25910 #checksum 7932 SEQUENCE /// ENTRY S76015 #type complete TITLE hypothetical protein - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S76015 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76015 !'##status preliminary !'##molecule_type DNA !'##residues 1-291 ##label KAN !'##cross-references EMBL:D64006; GB:AB001339; NID:g1001291; !1PID:g1001372 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily Aquifex aeolicus cysQ protein SUMMARY #length 291 #molecular-weight 32197 #checksum 8139 SEQUENCE /// ENTRY G70576 #type complete TITLE probable cysQ protein - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G70576 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession G70576 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-267 ##label COL !'##cross-references GB:Z95388; GB:AL123456; NID:g3261759; !1PIDN:CAB08639.1; PID:g2104347 !'##experimental_source strain H37Rv GENETICS !$#gene cysQ CLASSIFICATION #superfamily Aquifex aeolicus cysQ protein SUMMARY #length 267 #molecular-weight 28447 #checksum 5068 SEQUENCE /// ENTRY S72862 #type complete TITLE cysQ homolog - Mycobacterium leprae ALTERNATE_NAMES B2126_C3_229 protein ORGANISM #formal_name Mycobacterium leprae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 23-Mar-2001 ACCESSIONS S72862 REFERENCE S72585 !$#authors Smith, D.R.; Robison, K. !$#submission submitted to the EMBL Data Library, November 1993 !$#description Mycobacterium leprae cosmid B2126. !$#accession S72862 !'##status preliminary !'##molecule_type DNA !'##residues 1-289 ##label SMI !'##cross-references EMBL:U00017; NID:g466994; PID:g467017 CLASSIFICATION #superfamily Aquifex aeolicus cysQ protein SUMMARY #length 289 #molecular-weight 30923 #checksum 931 SEQUENCE /// ENTRY S76736 #type complete TITLE hypothetical protein - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S76736 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76736 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-287 ##label KAN !'##cross-references EMBL:D90916; GB:AB001339; NID:g1653715; !1PIDN:BAA18648.1; PID:g1653737 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily Aquifex aeolicus cysQ protein SUMMARY #length 287 #molecular-weight 31555 #checksum 6005 SEQUENCE /// ENTRY S39676 #type complete TITLE sugar permease homolog ywbF - Bacillus subtilis ALTERNATE_NAMES protein ipa-21r ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S39676; D70051 REFERENCE S39655 !$#authors Glaser, P.; Kunst, F.; Arnaud, M.; Coudart, M.P.; Gonzales, !1W.; Hullo, M.F.; Ionescu, M.; Lubochinsky, B.; Marcelino, !1L.; Moszer, I.; Presecan, E.; Santana, M.; Schneider, E.; !1Schweizer, J.; Vertes, A.; Rapoport, G.; Danchin, A. !$#journal Mol. Microbiol. (1993) 10:371-384 !$#title Bacillus subtilis genome project: cloning and sequencing of !1the 97 kb region from 325 degrees to 333 degrees. !$#cross-references MUID:95020537; PMID:7934828 !$#accession S39676 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-399 ##label GLA !'##cross-references EMBL:X73124; NID:g413923; PIDN:CAA51577.1; !1PID:g413945 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1993 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D70051 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-399 ##label KUN !'##cross-references GB:Z99123; GB:AL009126; NID:g2636240; !1PIDN:CAB15860.1; PID:g2636369 !'##experimental_source strain 168 GENETICS !$#gene ywbF CLASSIFICATION #superfamily maltose permease KEYWORDS transmembrane protein SUMMARY #length 399 #molecular-weight 44009 #checksum 6567 SEQUENCE /// ENTRY S43915 #type complete TITLE maltose permease - Bacillus stearothermophilus ORGANISM #formal_name Bacillus stearothermophilus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S43915 REFERENCE S43914 !$#authors Liong, E.C.; Ferenci, T. !$#journal Mol. Gen. Genet. (1994) 243:343-352 !$#title Molecular cloning of a maltose transport gene from Bacillus !1stearothermophilus and its expression in Escherichia coli !1K-12. !$#cross-references MUID:94247374; PMID:8190087 !$#accession S43915 !'##status preliminary !'##molecule_type DNA !'##residues 1-394 ##label LIO !'##cross-references EMBL:L13418; NID:g436964; PIDN:AAA71980.1; !1PID:g436966 CLASSIFICATION #superfamily maltose permease SUMMARY #length 394 #molecular-weight 42326 #checksum 4074 SEQUENCE /// ENTRY F64147 #type complete TITLE hypothetical protein HI0308 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS F64147 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession F64147 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-388 ##label TIGR !'##cross-references GB:U32716; GB:L42023; NID:g1573268; !1PIDN:AAC21973.1; PID:g1573277; TIGR:HI0308 !'##note best homolog was a hypothetical protein from Escherichia coli CLASSIFICATION #superfamily maltose permease SUMMARY #length 388 #molecular-weight 43030 #checksum 9733 SEQUENCE /// ENTRY G65030 #type complete TITLE Probable 3-phenylpropionic acid transporter - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS G65030 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65030 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-379 ##label BLAT !'##cross-references GB:AE000340; GB:U00096; NID:g1788883; !1PIDN:AAC75589.1; PID:g1788886; UWGP:b2536 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily maltose permease SUMMARY #length 379 #molecular-weight 41592 #checksum 231 SEQUENCE /// ENTRY F64249 #type complete TITLE hypothetical protein MG449 - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F64249 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession F64249 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-144 ##label TIGR !'##cross-references GB:U39731; GB:L43967; NID:g3845031; !1PIDN:AAC72469.1; PID:g3845042; TIGR:MG449 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily Mycoplasma genitalium hypothetical protein !1MG449 SUMMARY #length 144 #molecular-weight 15815 #checksum 7813 SEQUENCE /// ENTRY S73505 #type complete TITLE MG449 homolog K05_orf234 - Mycoplasma pneumoniae (strain ATCC 29342) ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S73505 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73505 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-234 ##label HIM !'##cross-references EMBL:AE000019; GB:U00089; NID:g1673839; !1PIDN:AAB95827.1; PID:g1673842 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily Mycoplasma genitalium hypothetical protein !1MG449 SUMMARY #length 234 #molecular-weight 26154 #checksum 6422 SEQUENCE /// ENTRY A69999 #type complete TITLE phenylalanyl-tRNA synthetase (beta subunit) homolog ytpR - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A69999 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69999 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-201 ##label KUN !'##cross-references GB:Z99119; GB:AL009126; NID:g2635411; !1PIDN:CAB14960.1; PID:g2635466 !'##experimental_source strain 168 GENETICS !$#gene ytpR CLASSIFICATION #superfamily Mycoplasma genitalium hypothetical protein !1MG449 SUMMARY #length 201 #molecular-weight 21696 #checksum 3769 SEQUENCE /// ENTRY F64302 #type complete TITLE cobalamin biosynthesis protein D homolog - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F64302 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession F64302 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-362 ##label BUL !'##cross-references GB:U67461; GB:L77117; NID:g1590827; !1PIDN:AAB98004.1; PID:g1592256; TIGR:MJ0022 GENETICS !$#map_position FOR24003-25091 CLASSIFICATION #superfamily Methanobacterium cobalamin biosynthesis protein !1D SUMMARY #length 362 #molecular-weight 39950 #checksum 3295 SEQUENCE /// ENTRY H69207 #type complete TITLE cobalamin biosynthesis protein D - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H69207 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession H69207 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-364 ##label MTH !'##cross-references GB:AE000858; GB:AE000666; NID:g2621885; !1PIDN:AAB85308.1; PID:g2621898 !'##experimental_source strain Delta H GENETICS !$#gene MTH808 CLASSIFICATION #superfamily Methanobacterium cobalamin biosynthesis protein !1D SUMMARY #length 364 #molecular-weight 39808 #checksum 6324 SEQUENCE /// ENTRY S77360 #type complete TITLE cbiD protein - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein slr1538 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S77360 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S77360 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-364 ##label KAN !'##cross-references EMBL:D90906; GB:AB001339; NID:g1652492; !1PIDN:BAA17463.1; PID:g1652542 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene cbiD !$#start_codon GTG CLASSIFICATION #superfamily Methanobacterium cobalamin biosynthesis protein !1D SUMMARY #length 364 #molecular-weight 39379 #checksum 882 SEQUENCE /// ENTRY F64304 #type complete TITLE conserved hypothetical protein MJ0038 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F64304 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession F64304 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-217 ##label BUL !'##cross-references GB:U67462; GB:L77117; NID:g1590835; !1PIDN:AAB98019.1; PID:g1498798; TIGR:MJ0038 GENETICS !$#map_position REV39443-38790 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0038 SUMMARY #length 217 #molecular-weight 26274 #checksum 9575 SEQUENCE /// ENTRY F71193 #type complete TITLE hypothetical protein PH1822 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F71193 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession F71193 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-205 ##label KAW !'##cross-references GB:AP000007; NID:g3236134; PIDN:BAA30941.1; !1PID:g3258258 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1822 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0038 SUMMARY #length 205 #molecular-weight 24398 #checksum 9642 SEQUENCE /// ENTRY B69043 #type complete TITLE conserved hypothetical protein MTH1325 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69043 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession B69043 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-193 ##label MTH !'##cross-references GB:AE000896; GB:AE000666; NID:g2622424; !1PIDN:AAB85803.1; PID:g2622431 !'##experimental_source strain Delta H GENETICS !$#gene MTH1325 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0038 SUMMARY #length 193 #molecular-weight 22588 #checksum 7353 SEQUENCE /// ENTRY B69441 #type complete TITLE conserved hypothetical protein AF1531 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69441 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession B69441 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-195 ##label KLE !'##cross-references GB:AE000997; GB:AE000782; NID:g2689320; !1PIDN:AAB89717.1; PID:g2649033; TIGR:AF1531 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0038 SUMMARY #length 195 #molecular-weight 23194 #checksum 978 SEQUENCE /// ENTRY F64306 #type complete TITLE hypothetical protein MJ0054 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F64306 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession F64306 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-281 ##label BUL !'##cross-references GB:U67463; GB:L77117; NID:g1590846; !1PIDN:AAB98034.1; PID:g1498815; TIGR:MJ0054 GENETICS !$#map_position REV55001-54156 CLASSIFICATION #superfamily hypothetical protein MJ0054 SUMMARY #length 281 #molecular-weight 31168 #checksum 5409 SEQUENCE /// ENTRY A69077 #type complete TITLE conserved hypothetical protein MTH1574 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A69077 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession A69077 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-276 ##label MTH !'##cross-references GB:AE000917; GB:AE000666; NID:g2622689; !1PIDN:AAB86047.1; PID:g2622696 !'##experimental_source strain Delta H GENETICS !$#gene MTH1574 !$#start_codon GTG CLASSIFICATION #superfamily hypothetical protein MJ0054 SUMMARY #length 276 #molecular-weight 30124 #checksum 362 SEQUENCE /// ENTRY I40476 #type complete TITLE conserved hypothetical protein ywlC - Bacillus subtilis ALTERNATE_NAMES SUA5 homolog ipc-29d ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Feb-2003 ACCESSIONS I40476; H70061; S49358 REFERENCE I40473 !$#authors Martinussen, J.; Glaser, P.; Andersen, P.S.; Saxild, H.H. !$#journal J. Bacteriol. (1995) 177:271-274 !$#title Two genes encoding uracil phosphoribosyltransferase are !1present in Bacillus subtilis. !$#cross-references MUID:95095982; PMID:7798145 !$#accession I40476 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-346 ##label RES !'##cross-references EMBL:Z38002; NID:g556877; PIDN:CAA86105.1; !1PID:g556881 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H70061 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-346 ##label KUN !'##cross-references GB:Z99122; GB:AL009126; NID:g2636029; !1PIDN:CAB15712.1; PID:g2636220 !'##experimental_source strain 168 GENETICS !$#gene ywlC; ipc-29d CLASSIFICATION #superfamily Probable translation factor, SUA5-type SUMMARY #length 346 #molecular-weight 37007 #checksum 6137 SEQUENCE /// ENTRY D71154 #type complete TITLE hypothetical protein PH0435 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Feb-2003 ACCESSIONS D71154 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession D71154 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-340 ##label KAW !'##cross-references GB:AP000002; NID:g3236129; PIDN:BAA29521.1; !1PID:g3256838 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0435 CLASSIFICATION #superfamily Probable translation factor, SUA5-type SUMMARY #length 340 #molecular-weight 37087 #checksum 1323 SEQUENCE /// ENTRY E70191 #type complete TITLE conserved hypothetical protein BB0734 - Lyme disease spirochete ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Feb-2003 ACCESSIONS E70191 REFERENCE A70100 !$#authors Fraser, C.M.; Casjens, S.; Huang, W.M.; Sutton, G.G.; !1Clayton, R.; Lathigra, R.; White, O.; Ketchum, K.A.; Dodson, !1R.; Hickey, E.K.; Gwinn, M.; Dougherty, B.; Tomb, J.F.; !1Fleischmann, R.D.; Richardson, D.; Peterson, J.; Kerlavage, !1A.R.; Quackenbush, J.; Salzberg, S.; Hanson, M.; Vugt, R.V.; !1Palmer, N.; Adams, M.D.; Gocayne, J.; Weidman, J.; !1Utterback, T.; Watthey, L.; McDonald, L.; Artiach, P.; !1Bowman, C.; Garland, S.; Fujii, C.; Cotton, M.D.; Horst, K.; !1Roberts, K.; Hatch, B.; Smith, H.O.; Venter, J.C. !$#journal Nature (1997) 390:580-586 !$#title Genomic sequence of a Lyme disease spirochaete, Borrelia !1burgdorferi. !$#cross-references MUID:98065943; PMID:9403685 !$#accession E70191 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-337 ##label KLE !'##cross-references GB:AE001173; GB:AE000783; NID:g2688665; !1PIDN:AAC67081.1; PID:g2688669; TIGR:BB0734 !'##experimental_source strain B31 CLASSIFICATION #superfamily Probable translation factor, SUA5-type SUMMARY #length 337 #molecular-weight 38280 #checksum 8273 SEQUENCE /// ENTRY E69347 #type complete TITLE conserved hypothetical protein AF0781 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Feb-2003 ACCESSIONS E69347 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession E69347 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-309 ##label KLE !'##cross-references GB:AE001051; GB:AE000782; NID:g2689374; !1PIDN:AAB90461.1; PID:g2649831; TIGR:AF0781 CLASSIFICATION #superfamily Probable translation factor, SUA5-type SUMMARY #length 309 #molecular-weight 34379 #checksum 5609 SEQUENCE /// ENTRY F64307 #type complete TITLE conserved hypothetical protein MJ0062 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F64307 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession F64307 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-207 ##label BUL !'##cross-references GB:U67464; GB:L77117; NID:g1590852; !1PIDN:AAB98044.1; PID:g1498824; TIGR:MJ0062 GENETICS !$#map_position FOR60618-61241 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0062 SUMMARY #length 207 #molecular-weight 23496 #checksum 5474 SEQUENCE /// ENTRY C69093 #type complete TITLE conserved hypothetical protein MTH1692 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69093 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession C69093 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-208 ##label MTH !'##cross-references GB:AE000927; GB:AE000666; NID:g2622822; !1PIDN:AAB86164.1; PID:g2622823 !'##experimental_source strain Delta H GENETICS !$#gene MTH1692 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0062 SUMMARY #length 208 #molecular-weight 22614 #checksum 403 SEQUENCE /// ENTRY S74580 #type complete TITLE hypothetical protein sll0216 - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S74580 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74580 !'##status preliminary !'##molecule_type DNA !'##residues 1-210 ##label KAN !'##cross-references EMBL:D90900; GB:AB001339; NID:g1651768; !1PIDN:BAA16732.1; PID:g1651805 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0062 SUMMARY #length 210 #molecular-weight 23860 #checksum 7753 SEQUENCE /// ENTRY I64168 #type complete TITLE probable translation factor HI1198 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS I64168 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession I64168 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-207 ##label TIGR !'##cross-references GB:U32799; GB:L42023; NID:g1574122; !1PIDN:AAC22852.1; PID:g1574127; TIGR:HI1198 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0062 SUMMARY #length 207 #molecular-weight 23092 #checksum 9897 SEQUENCE /// ENTRY F64321 #type complete TITLE conserved hypothetical protein MJ0173 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 23-Dec-2002 ACCESSIONS F64321 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession F64321 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-157 ##label BUL !'##cross-references GB:U67474; GB:L77117; NID:g1590921; !1PIDN:AAB98158.1; PID:g1498946; TIGR:MJ0173 GENETICS !$#map_position FOR175871-176344 CLASSIFICATION #superfamily helix-turn-helix protein SUMMARY #length 157 #molecular-weight 18190 #checksum 163 SEQUENCE /// ENTRY D71124 #type complete TITLE hypothetical protein PH0763 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 23-Dec-2002 ACCESSIONS D71124 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession D71124 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-167 ##label KAW !'##cross-references GB:AP000003; NID:g3236130; PIDN:BAA29854.1; !1PID:g3257171 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0763 CLASSIFICATION #superfamily helix-turn-helix protein SUMMARY #length 167 #molecular-weight 19141 #checksum 6296 SEQUENCE /// ENTRY F69222 #type complete TITLE conserved hypothetical protein MTH916 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 23-Dec-2002 ACCESSIONS F69222 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession F69222 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-122 ##label MTH !'##cross-references GB:AE000867; GB:AE000666; NID:g2622009; !1PIDN:AAB85414.1; PID:g2622013 !'##experimental_source strain Delta H GENETICS !$#gene MTH916 CLASSIFICATION #superfamily helix-turn-helix protein SUMMARY #length 122 #molecular-weight 14161 #checksum 5353 SEQUENCE /// ENTRY F64351 #type complete TITLE hypothetical protein MJ0414 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F64351 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession F64351 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-395 ##label BUL !'##cross-references GB:U67493; GB:L77117; NID:g2826279; !1PIDN:AAB98403.1; PID:g1499205; TIGR:MJ0414 GENETICS !$#map_position REV374603-373416 CLASSIFICATION #superfamily hypothetical protein MJ0414 SUMMARY #length 395 #molecular-weight 46417 #checksum 8120 SEQUENCE /// ENTRY B69030 #type complete TITLE conserved hypothetical protein MTH1221 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69030 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession B69030 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-381 ##label MTH !'##cross-references GB:AE000890; GB:AE000666; NID:g2622331; !1PIDN:AAB85710.1; PID:g2622332 !'##experimental_source strain Delta H GENETICS !$#gene MTH1221 !$#start_codon GTG CLASSIFICATION #superfamily hypothetical protein MJ0414 SUMMARY #length 381 #molecular-weight 43146 #checksum 8807 SEQUENCE /// ENTRY A69356 #type complete TITLE conserved hypothetical protein AF0849 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A69356 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession A69356 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-378 ##label KLE !'##cross-references GB:AE001045; GB:AE000782; NID:g2689368; !1PIDN:AAB90388.1; PID:g2649752; TIGR:AF0849 CLASSIFICATION #superfamily hypothetical protein MJ0414 SUMMARY #length 378 #molecular-weight 44226 #checksum 235 SEQUENCE /// ENTRY E71162 #type complete TITLE hypothetical protein PH0498 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E71162 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession E71162 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-379 ##label KAW !'##cross-references GB:AP000002; NID:g3236129; PIDN:BAA29586.1; !1PID:g3256903 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0498 CLASSIFICATION #superfamily hypothetical protein MJ0414 SUMMARY #length 379 #molecular-weight 43959 #checksum 7182 SEQUENCE /// ENTRY D70395 #type complete TITLE conserved hypothetical protein aq_1106 - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D70395 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession D70395 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-367 ##label AQF !'##cross-references GB:AE000723; GB:AE000657; NID:g2983569; !1PIDN:AAC07155.1; PID:g2983583 !'##experimental_source strain VF5 GENETICS !$#gene aq_1106 CLASSIFICATION #superfamily hypothetical protein MJ0414 SUMMARY #length 367 #molecular-weight 43272 #checksum 4309 SEQUENCE /// ENTRY F64355 #type complete TITLE conserved hypothetical protein MJ0446 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F64355 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession F64355 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-361 ##label BUL !'##cross-references GB:U67496; GB:L77117; NID:g2826283; !1PIDN:AAB98436.1; PID:g1591150; TIGR:MJ0446 GENETICS !$#map_position FOR399495-400580 !$#start_codon GTG CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0446 SUMMARY #length 361 #molecular-weight 41984 #checksum 6502 SEQUENCE /// ENTRY S75303 #type complete TITLE hypothetical protein sll1285 - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S75303 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75303 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-313 ##label KAN !'##cross-references EMBL:D90904; GB:AB001339; NID:g1652225; !1PIDN:BAA17217.1; PID:g1652294 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0446 SUMMARY #length 313 #molecular-weight 35288 #checksum 2013 SEQUENCE /// ENTRY E69349 #type complete TITLE conserved hypothetical protein AF0797 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69349 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession E69349 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-324 ##label KLE !'##cross-references GB:AE001049; GB:AE000782; NID:g2689372; !1PIDN:AAB90441.1; PID:g2649809; TIGR:AF0797 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0446 SUMMARY #length 324 #molecular-weight 36799 #checksum 1097 SEQUENCE /// ENTRY G69026 #type complete TITLE conserved hypothetical protein MTH1198 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69026 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession G69026 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-359 ##label MTH !'##cross-references GB:AE000888; GB:AE000666; NID:g2622304; !1PIDN:AAB85687.1; PID:g2622307 !'##experimental_source strain Delta H GENETICS !$#gene MTH1198 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0446 SUMMARY #length 359 #molecular-weight 40875 #checksum 2684 SEQUENCE /// ENTRY C64416 #type complete TITLE conserved hypothetical MG372 related protein - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C64416 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession C64416 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-381 ##label BUL !'##cross-references GB:U67536; GB:L77117; NID:g1591596; !1PIDN:AAB98933.1; PID:g1591602; TIGR:MJ0931 GENETICS !$#map_position FOR860923-862068 CLASSIFICATION #superfamily Mycoplasma genitalium hypothetical protein !1MG372 SUMMARY #length 381 #molecular-weight 43436 #checksum 7754 SEQUENCE /// ENTRY B64241 #type complete TITLE hypothetical protein MG372 - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 07-Dec-1999 ACCESSIONS B64241 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession B64241 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-385 ##label TIGR !'##cross-references GB:U39722; GB:L43967; NID:g1046079; PID:g1046082; !1TIGR:MG372 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily Mycoplasma genitalium hypothetical protein !1MG372 SUMMARY #length 385 #molecular-weight 44176 #checksum 1136 SEQUENCE /// ENTRY C69092 #type complete TITLE conserved hypothetical protein MTH1685 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69092 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession C69092 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-389 ##label MTH !'##cross-references GB:AE000926; GB:AE000666; NID:g2622806; !1PIDN:AAB86157.1; PID:g2622815 !'##experimental_source strain Delta H GENETICS !$#gene MTH1685 CLASSIFICATION #superfamily Mycoplasma genitalium hypothetical protein !1MG372 SUMMARY #length 389 #molecular-weight 42472 #checksum 528 SEQUENCE /// ENTRY G69359 #type complete TITLE conserved hypothetical protein AF0879 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69359 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession G69359 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-374 ##label KLE !'##cross-references GB:AE001043; GB:AE000782; NID:g2689366; !1PIDN:AAB90361.1; PID:g2649723; TIGR:AF0879 CLASSIFICATION #superfamily Mycoplasma genitalium hypothetical protein !1MG372 SUMMARY #length 374 #molecular-weight 42272 #checksum 8141 SEQUENCE /// ENTRY C71310 #type complete TITLE conserved hypothetical protein TP0559 - syphilis spirochete ORGANISM #formal_name Treponema pallidum subsp. pallidum #common_name syphilis spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS C71310 REFERENCE A71250 !$#authors Fraser, C.M.; Norris, S.J.; Weinstock, G.M.; White, O.; !1Sutton, G.G.; Dodson, R.; Gwinn, M.; Hickey, E.K.; Clayton, !1R.; Ketchum, K.A.; Sodergren, E.; Hardham, J.M.; McLeod, !1M.P.; Salzberg, S.; Peterson, J.; Khalak, H.; Richardson, !1D.; Howell, J.K.; Chidambaram, M.; Utterback, T.; McDonald, !1L.; Artiach, P.; Bowman, C.; Cotton, M.D.; Fujii, C.; !1Garland, S.; Hatch, B.; Horst, K.; Roberts, K.; Watthey, L.; !1Weidman, J.; Smith, H.O.; Venter, J.C. !$#journal Science (1998) 281:375-388 !$#title Complete genome sequence of Treponema pallidum, the syphilis !1spirochete. !$#cross-references MUID:98332770; PMID:9665876 !$#accession C71310 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-401 ##label COL !'##cross-references GB:AE001231; GB:AE000520; NID:g3322846; !1PIDN:AAC26563.1; PID:g3322853 !'##experimental_source strain Nichols GENETICS !$#gene TP0559 CLASSIFICATION #superfamily Mycoplasma genitalium hypothetical protein !1MG372 SUMMARY #length 401 #molecular-weight 44639 #checksum 2595 SEQUENCE /// ENTRY E69988 #type complete TITLE conserved hypothetical protein ytbJ - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69988 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69988 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-358 ##label KUN !'##cross-references GB:Z99119; GB:AL009126; NID:g2635411; !1PIDN:CAB14936.1; PID:g2635442 !'##experimental_source strain 168 GENETICS !$#gene ytbJ CLASSIFICATION #superfamily Mycoplasma genitalium hypothetical protein !1MG372 SUMMARY #length 358 #molecular-weight 40323 #checksum 3503 SEQUENCE /// ENTRY S73618 #type complete TITLE MG372 homolog G12_orf387 - Mycoplasma pneumoniae (strain ATCC 29342) ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S73618 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73618 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-387 ##label HIM !'##cross-references EMBL:AE000027; GB:U00089; NID:g1673941; !1PIDN:AAB95940.1; PID:g1673963 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily Mycoplasma genitalium hypothetical protein !1MG372 SUMMARY #length 387 #molecular-weight 43341 #checksum 2044 SEQUENCE /// ENTRY D64140 #type complete TITLE conserved hypothetical protein HI0019 - Haemophilus influenzae ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS D64140 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession D64140 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-474 ##label TIGR !'##cross-references GB:U32687; GB:L42023; NID:g1572955; !1PIDN:AAC21697.1; PID:g1572963; TIGR:HI0019 !'##experimental_source strain Rd KW20 CLASSIFICATION #superfamily conserved hypothetical protein b0835 SUMMARY #length 474 #molecular-weight 53640 #checksum 542 SEQUENCE /// ENTRY S57900 #type complete TITLE conserved hypothetical protein 2 (hemL 3' region) - Pseudomonas aeruginosa ORGANISM #formal_name Pseudomonas aeruginosa DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S57900; S49379 REFERENCE S57898 !$#authors Hungerer, C.; Troup, B.; Roemling, U.; Jahn, D. !$#journal Mol. Gen. Genet. (1995) 248:375-380 !$#title Cloning, mapping and characterization of the Pseudomonas !1aeruginosa hemL gene. !$#cross-references MUID:96004705; PMID:7565600 !$#accession S57900 !'##molecule_type DNA !'##residues 1-446 ##label HUN !'##cross-references EMBL:X82072; NID:g557261; PIDN:CAA57577.1; !1PID:g557263 CLASSIFICATION #superfamily conserved hypothetical protein b0835 SUMMARY #length 446 #molecular-weight 49962 #checksum 6304 SEQUENCE /// ENTRY C64801 #type complete TITLE yleA protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS C64801 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64801 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-474 ##label BLAT !'##cross-references GB:AE000170; GB:U00096; NID:g1786875; !1PIDN:AAC73762.1; PID:g1786882; UWGP:b0661 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yleA CLASSIFICATION #superfamily conserved hypothetical protein b0835 SUMMARY #length 474 #molecular-weight 53662 #checksum 1944 SEQUENCE /// ENTRY S72937 #type complete TITLE hypothetical protein B2235_C2_195 - Mycobacterium leprae ORGANISM #formal_name Mycobacterium leprae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 23-Mar-2001 ACCESSIONS S72937 REFERENCE S72587 !$#authors Smith, D.R.; Robison, K. !$#submission submitted to the EMBL Data Library, November 1993 !$#description Mycobacterium leprae cosmid B2235. !$#accession S72937 !'##status preliminary !'##molecule_type DNA !'##residues 1-516 ##label SMI !'##cross-references EMBL:U00019; NID:g467079; PID:g467090 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily conserved hypothetical protein b0835 SUMMARY #length 516 #molecular-weight 56023 #checksum 8769 SEQUENCE /// ENTRY D70506 #type complete TITLE hypothetical protein Rv2733c - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D70506 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession D70506 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-512 ##label COL !'##cross-references GB:Z98209; GB:AL123456; NID:g3261838; !1PIDN:CAB10909.1; PID:g2292967 !'##experimental_source strain H37Rv GENETICS !$#gene Rv2733c CLASSIFICATION #superfamily conserved hypothetical protein b0835 SUMMARY #length 512 #molecular-weight 55085 #checksum 4717 SEQUENCE /// ENTRY S75239 #type complete TITLE hypothetical protein - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S75239 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75239 !'##status preliminary !'##molecule_type DNA !'##residues 1-451 ##label KAN !'##cross-references EMBL:D90904; GB:AB001339; NID:g1652225; !1PIDN:BAA17153.1; PID:g1652230 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily conserved hypothetical protein b0835 SUMMARY #length 451 #molecular-weight 50956 #checksum 6371 SEQUENCE /// ENTRY S76611 #type complete TITLE hypothetical protein slr0082 - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S76611 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76611 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-443 ##label KAN !'##cross-references EMBL:D64004; GB:AB001339; NID:g1001701; !1PID:g1001718 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily conserved hypothetical protein b0835 SUMMARY #length 443 #molecular-weight 49362 #checksum 1518 SEQUENCE /// ENTRY E64553 #type complete TITLE conserved hypothetical ATP-binding protein HP0269 - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS E64553 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession E64553 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-437 ##label TOM !'##cross-references GB:AE000546; GB:AE000511; NID:g2313363; !1PIDN:AAD07337.1; PID:g2313364; TIGR:HP0269 GENETICS !$#start_codon TTG CLASSIFICATION #superfamily conserved hypothetical protein b0835 SUMMARY #length 437 #molecular-weight 49423 #checksum 4716 SEQUENCE /// ENTRY F64611 #type complete TITLE conserved hypothetical protein HP0734 - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS F64611 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession F64611 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-439 ##label TOM !'##cross-references GB:AE000586; GB:AE000511; NID:g2313854; !1PIDN:AAD07780.1; PID:g2313856; TIGR:HP0734 CLASSIFICATION #superfamily conserved hypothetical protein b0835 SUMMARY #length 439 #molecular-weight 49633 #checksum 1711 SEQUENCE /// ENTRY C64821 #type complete TITLE conserved hypothetical protein b0835 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS C64821 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64821 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-441 ##label BLAT !'##cross-references GB:AE000185; GB:U00096; NID:g1787047; !1PIDN:AAC73922.1; PID:g1787057; UWGP:b0835 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily conserved hypothetical protein b0835 SUMMARY #length 441 #molecular-weight 49581 #checksum 1198 SEQUENCE /// ENTRY E69952 #type complete TITLE conserved hypothetical protein yqeV - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69952 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69952 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-451 ##label KUN !'##cross-references GB:Z99117; GB:AL009126; NID:g2634966; !1PIDN:CAB14485.1; PID:g2634989 !'##experimental_source strain 168 GENETICS !$#gene yqeV CLASSIFICATION #superfamily conserved hypothetical protein b0835 SUMMARY #length 451 #molecular-weight 51657 #checksum 7503 SEQUENCE /// ENTRY D69884 #type complete TITLE conserved hypothetical protein ymcB - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69884 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D69884 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-509 ##label KUN !'##cross-references GB:Z99112; GB:AL009126; NID:g2633902; !1PIDN:CAB13574.1; PID:g2634073 !'##experimental_source strain 168 GENETICS !$#gene ymcB CLASSIFICATION #superfamily conserved hypothetical protein b0835 SUMMARY #length 509 #molecular-weight 58169 #checksum 2054 SEQUENCE /// ENTRY H70342 #type complete TITLE conserved hypothetical protein aq_474 - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H70342 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession H70342 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-410 ##label AQF !'##cross-references GB:AE000691; GB:AE000657; NID:g2983118; !1PIDN:AAC06733.1; PID:g2983129 !'##experimental_source strain VF5 GENETICS !$#gene aq_474 CLASSIFICATION #superfamily conserved hypothetical protein b0835 SUMMARY #length 410 #molecular-weight 47833 #checksum 2996 SEQUENCE /// ENTRY B70326 #type complete TITLE conserved hypothetical protein aq_284 - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B70326 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession B70326 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-440 ##label AQF !'##cross-references GB:AE000682; GB:AE000657; NID:g2982979; !1PIDN:AAC06605.1; PID:g2982992 !'##experimental_source strain VF5 GENETICS !$#gene aq_284 CLASSIFICATION #superfamily conserved hypothetical protein b0835 SUMMARY #length 440 #molecular-weight 50321 #checksum 4160 SEQUENCE /// ENTRY E70373 #type complete TITLE conserved hypothetical protein aq_849 - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E70373 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession E70373 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-432 ##label AQF !'##cross-references GB:AE000710; GB:AE000657; NID:g2983385; !1PIDN:AAC06982.1; PID:g2983397 !'##experimental_source strain VF5 GENETICS !$#gene aq_849 CLASSIFICATION #superfamily conserved hypothetical protein b0835 SUMMARY #length 432 #molecular-weight 49574 #checksum 6922 SEQUENCE /// ENTRY F71200 #type complete TITLE hypothetical protein PH1875 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F71200 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession F71200 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-432 ##label KAW !'##cross-references GB:AP000007; NID:g3236134; PIDN:BAA30997.1; !1PID:g3258314 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1875 CLASSIFICATION #superfamily conserved hypothetical protein b0835 SUMMARY #length 432 #molecular-weight 49494 #checksum 2648 SEQUENCE /// ENTRY C64408 #type complete TITLE hypothetical protein HI0019 homolog - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C64408 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession C64408 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-427 ##label BUL !'##cross-references GB:U67530; GB:L77117; NID:g2826340; !1PIDN:AAB98872.1; PID:g1591550; TIGR:MJ0867 GENETICS !$#map_position REV791272-789989 CLASSIFICATION #superfamily conserved hypothetical protein b0835 SUMMARY #length 427 #molecular-weight 49090 #checksum 1269 SEQUENCE /// ENTRY F69405 #type complete TITLE conserved hypothetical protein AF1247 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F69405 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession F69405 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-405 ##label KLE !'##cross-references GB:AE001018; GB:AE000782; NID:g2689341; !1PIDN:AAB89997.1; PID:g2649334; TIGR:AF1247 CLASSIFICATION #superfamily conserved hypothetical protein b0835 SUMMARY #length 405 #molecular-weight 46056 #checksum 9581 SEQUENCE /// ENTRY B69210 #type complete TITLE conserved hypothetical protein MTH826 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69210 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession B69210 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-424 ##label MTH !'##cross-references GB:AE000860; GB:AE000666; NID:g2621915; !1PIDN:AAB85324.1; PID:g2621916 !'##experimental_source strain Delta H GENETICS !$#gene MTH826 CLASSIFICATION #superfamily conserved hypothetical protein b0835 SUMMARY #length 424 #molecular-weight 47315 #checksum 6866 SEQUENCE /// ENTRY G71345 #type complete TITLE conserved hypothetical protein TP0269 - syphilis spirochete ORGANISM #formal_name Treponema pallidum subsp. pallidum #common_name syphilis spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS G71345 REFERENCE A71250 !$#authors Fraser, C.M.; Norris, S.J.; Weinstock, G.M.; White, O.; !1Sutton, G.G.; Dodson, R.; Gwinn, M.; Hickey, E.K.; Clayton, !1R.; Ketchum, K.A.; Sodergren, E.; Hardham, J.M.; McLeod, !1M.P.; Salzberg, S.; Peterson, J.; Khalak, H.; Richardson, !1D.; Howell, J.K.; Chidambaram, M.; Utterback, T.; McDonald, !1L.; Artiach, P.; Bowman, C.; Cotton, M.D.; Fujii, C.; !1Garland, S.; Hatch, B.; Horst, K.; Roberts, K.; Watthey, L.; !1Weidman, J.; Smith, H.O.; Venter, J.C. !$#journal Science (1998) 281:375-388 !$#title Complete genome sequence of Treponema pallidum, the syphilis !1spirochete. !$#cross-references MUID:98332770; PMID:9665876 !$#accession G71345 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-482 ##label COL !'##cross-references GB:AE001208; GB:AE000520; NID:g3322538; !1PIDN:AAC65257.1; PID:g3322542 !'##experimental_source strain Nichols GENETICS !$#gene TP0269 CLASSIFICATION #superfamily conserved hypothetical protein b0835 SUMMARY #length 482 #molecular-weight 53173 #checksum 4049 SEQUENCE /// ENTRY E71284 #type complete TITLE conserved hypothetical protein TP0754 - syphilis spirochete ORGANISM #formal_name Treponema pallidum subsp. pallidum #common_name syphilis spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS E71284 REFERENCE A71250 !$#authors Fraser, C.M.; Norris, S.J.; Weinstock, G.M.; White, O.; !1Sutton, G.G.; Dodson, R.; Gwinn, M.; Hickey, E.K.; Clayton, !1R.; Ketchum, K.A.; Sodergren, E.; Hardham, J.M.; McLeod, !1M.P.; Salzberg, S.; Peterson, J.; Khalak, H.; Richardson, !1D.; Howell, J.K.; Chidambaram, M.; Utterback, T.; McDonald, !1L.; Artiach, P.; Bowman, C.; Cotton, M.D.; Fujii, C.; !1Garland, S.; Hatch, B.; Horst, K.; Roberts, K.; Watthey, L.; !1Weidman, J.; Smith, H.O.; Venter, J.C. !$#journal Science (1998) 281:375-388 !$#title Complete genome sequence of Treponema pallidum, the syphilis !1spirochete. !$#cross-references MUID:98332770; PMID:9665876 !$#accession E71284 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-456 ##label COL !'##cross-references GB:AE001247; GB:AE000520; NID:g3323059; !1PIDN:AAC65721.1; PID:g3323060 !'##experimental_source strain Nichols GENETICS !$#gene TP0754 CLASSIFICATION #superfamily conserved hypothetical protein b0835 SUMMARY #length 456 #molecular-weight 52572 #checksum 55 SEQUENCE /// ENTRY E64555 #type complete TITLE conserved hypothetical protein HP0285 - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS E64555 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession E64555 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-418 ##label TOM !'##cross-references GB:AE000547; GB:AE000511; NID:g2313377; !1PIDN:AAD07353.1; PID:g2313381; TIGR:HP0285 CLASSIFICATION #superfamily conserved hypothetical protein b0835 SUMMARY #length 418 #molecular-weight 47823 #checksum 7758 SEQUENCE /// ENTRY G71699 #type complete TITLE hypothetical protein RP416 - Rickettsia prowazekii ORGANISM #formal_name Rickettsia prowazekii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Nov-2000 ACCESSIONS G71699 REFERENCE A71630 !$#authors Andersson, S.G.E.; Zomorodipour, A.; Andersson, J.O.; !1Sicheritz-Ponten, T.; Alsmark, U.C.M.; Podowski, R.M.; !1Naeslund, A.K.; Eriksson, A.S.; Winkler, H.H.; Kurland, C.G. !$#journal Nature (1998) 396:133-140 !$#title The genome sequence of Rickettsia prowazekii and the origin !1of mitochondria. !$#cross-references MUID:99039499; PMID:9823893 !$#accession G71699 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-421 ##label AND !'##cross-references GB:AJ235271; GB:AJ235269; NID:g3868717; !1PIDN:CAA14873.1; PID:g3860973; GSPDB:GN00081 !'##experimental_source strain Madrid E GENETICS !$#gene RP416 CLASSIFICATION #superfamily conserved hypothetical protein b0835 SUMMARY #length 421 #molecular-weight 47922 #checksum 1016 SEQUENCE /// ENTRY S20857 #type complete TITLE hypothetical protein rps16 3'-region [imported] - red alga (Cyanidium caldarium) chloroplast ORGANISM #formal_name chloroplast Cyanidium caldarium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Sep-2000 ACCESSIONS S20857 REFERENCE S20854 !$#authors Kessler, U.; Maid, U.; Zetsche, K. !$#journal Plant Mol. Biol. (1992) 18:777-780 !$#title An equivalent to bacterial ompR genes is encoded on the !1plastid genome of red algae. !$#cross-references MUID:92216053; PMID:1558950 !$#accession S20857 !'##status translation not shown !'##molecule_type DNA !'##residues 1-98 ##label KES !'##cross-references EMBL:X62578; NID:g11278; PIDN:CAA44461.1; !1PID:g11282 GENETICS !$#genome chloroplast CLASSIFICATION #superfamily conserved hypothetical protein ssr2142 KEYWORDS chloroplast SUMMARY #length 98 #molecular-weight 11562 #checksum 4850 SEQUENCE /// ENTRY S73274 #type complete TITLE hypothetical protein 19 rps16 3'-region [imported] - red alga (Porphyra purpurea) chloroplast ORGANISM #formal_name chloroplast Porphyra purpurea DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Sep-2000 ACCESSIONS S73274 REFERENCE S73108 !$#authors Reith, M.; Munholland, J. !$#journal Plant Mol. Biol. Rep. (1995) 13:333-335 !$#title Complete nucleotide sequence of the Porphyra purpurea !1chloroplast genome. !$#accession S73274 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-95 ##label REI !'##cross-references EMBL:U38804; NID:g1276652; PIDN:AAC08239.1; !1PID:g1276819 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1995 GENETICS !$#gene ycf19 !$#genome chloroplast CLASSIFICATION #superfamily conserved hypothetical protein ssr2142 KEYWORDS chloroplast SUMMARY #length 95 #molecular-weight 10832 #checksum 4315 SEQUENCE /// ENTRY S74690 #type complete TITLE conserved hypothetical protein ssr2142 [imported] - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Sep-2000 ACCESSIONS S74690 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74690 !'##status preliminary !'##molecule_type DNA !'##residues 1-90 ##label KAN !'##cross-references EMBL:D90901; GB:AB001339; NID:g1651897; !1PIDN:BAA16841.1; PID:g1651915 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily conserved hypothetical protein ssr2142 SUMMARY #length 90 #molecular-weight 10003 #checksum 9606 SEQUENCE /// ENTRY G69876 #type complete TITLE conserved hypothetical protein ylmG [imported] - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Sep-2000 ACCESSIONS G69876 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69876 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-90 ##label KUN !'##cross-references GB:Z99112; GB:AL009126; NID:g2633902; !1PIDN:CAB13414.1; PID:g2633913 !'##experimental_source strain 168 GENETICS !$#gene ylmG CLASSIFICATION #superfamily conserved hypothetical protein ssr2142 SUMMARY #length 90 #molecular-weight 10307 #checksum 9410 SEQUENCE /// ENTRY B72038 #type complete TITLE conserved hypothetical protein CP1105 [imported] - Chlamydophila pneumoniae (strains CWL029 and AR39) ALTERNATE_NAMES ct645 hypothetical protein ORGANISM #formal_name Chlamydophila pneumoniae, Chlamydia pneumoniae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 11-May-2000 ACCESSIONS B72038; E81503 REFERENCE A72000 !$#authors Kalman, S.; Mitchell, W.; Marathe, R.; Lammel, C.; Fan, J.; !1Olinger, L.; Grimwood, J.; Davis, R.W.; Stephens, R.S. !$#journal Nature Genet. (1999) 21:385-389 !$#title Comparative genomes of Clamydia pneumoniae and C. !1trachomatis. !$#cross-references MUID:99206606; PMID:10192388 !$#accession B72038 !'##molecule_type DNA !'##residues 1-98 ##label ARN !'##cross-references GB:AE001658; GB:AE001363; NID:g4377069; !1PID:g4377075 !'##experimental_source strain CWL029 REFERENCE A81500 !$#authors Read, T.D.; Brunham, R.C.; Shen, C.; Gill, S.R.; Heidelberg, !1J.F.; White, O.; Hickey, E.K.; Peterson, J.; Utterback, T.; !1Berry, K.; Bass, S.; Linher, K.; Weidman, J.; Khouri, H.; !1Craven, B.; Bowman, C.; Dodson, R.; Gwinn, M.; Nelson, W.; !1DeBoy, R.; Kolonay, J.; McClarty, G.; Salzberg, S.L.; Eisen, !1J.; Fraser, C.M. !$#journal Nucleic Acids Res. (2000) 28:1397-1406 !$#title Genome sequences of Chlamydia trachomatis MoPn and Chlamydia !1pneumoniae AR39. !$#cross-references MUID:20150255; PMID:10684935 !$#accession E81503 !'##molecule_type DNA !'##residues 1-98 ##label REA !'##cross-references GB:AE002266; GB:AE002161; NID:g7190009; !1PIDN:AAF38873.1; PID:g7190017; GSPDB:GN00122; TIGR:CP1105 !'##experimental_source strain AR39, HL cells GENETICS !$#gene CPn0767; CP1105 CLASSIFICATION #superfamily conserved hypothetical protein ssr2142 SUMMARY #length 98 #molecular-weight 11577 #checksum 4411 SEQUENCE /// ENTRY C71488 #type complete TITLE conserved hypothetical protein CT645 [imported] - Chlamydia trachomatis (serotype D, strain UW3/Cx) ORGANISM #formal_name Chlamydia trachomatis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Sep-2000 ACCESSIONS C71488 REFERENCE A71570 !$#authors Stephens, R.S.; Kalman, S.; Lammel, C.J.; Fan, J.; Marathe, !1R.; Aravind, L.; Mitchell, W.P.; Olinger, L.; Tatusov, R.L.; !1Zhao, Q.; Koonin, E.V.; Davis, R.W. !$#journal Science (1998) 282:754-759 !$#title Genome sequence of an obligate intracellular pathogen of !1humans: Chlamydia trachomatis. !$#cross-references MUID:99000809; PMID:9784136 !$#accession C71488 !'##status preliminary !'##molecule_type DNA !'##residues 1-98 ##label ARN !'##cross-references GB:AE001335; GB:AE001273; NID:g3329091; !1PID:g3329094 !'##experimental_source serotype D, strain UW-3/Cx GENETICS !$#gene CT645 CLASSIFICATION #superfamily conserved hypothetical protein ssr2142 SUMMARY #length 98 #molecular-weight 11835 #checksum 6715 SEQUENCE /// ENTRY B64842 #type complete TITLE trp repressor-binding protein - Escherichia coli (strain K-12) ALTERNATE_NAMES tryptophan repressor-binding protein ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS B64842; I59246 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64842 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-198 ##label BLAT !'##cross-references GB:AE000202; GB:U00096; NID:g1787233; !1PIDN:AAC74089.1; PID:g1787239; UWGP:b1004 !'##experimental_source strain K-12, substrain MG1655 REFERENCE I59246 !$#authors Weiping, Y.; Ni, L.; Somerville, R.L. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:5796-5800 !$#title A stationary-phase protein of Escherichia coli that affects !1the mode of association between the trp repressor protein !1and operator-bearing DNA. !$#cross-references MUID:93296226; PMID:8516330 !$#accession I59246 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-141,'A',143-198 ##label RES !'##cross-references GB:M99166; NID:g148263; PIDN:AAA24759.1; !1PID:g148264 !'##experimental_source strain K-12 GENETICS !$#gene wrbA FUNCTION !$#description functions as accessory element in blocking trpR-specific !1transcriptional processes that might be physiologically !1disadvantageous in the stationary phase of the bacterial !1life cycle !$#note does not interact alone with the trp operator; enhance !1formation or stability of noncovalent complexes between TrpR !1holorepressor and its primary operator targets CLASSIFICATION #superfamily trp repressor-binding protein; flavodoxin !1homology KEYWORDS flavoprotein; homodimer SUMMARY #length 198 #molecular-weight 20845 #checksum 7908 SEQUENCE /// ENTRY S43116 #type complete TITLE minor allergen - fungus (Cladosporium herbarum) ORGANISM #formal_name Cladosporium herbarum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 29-Oct-1999 ACCESSIONS S43116 REFERENCE S43108 !$#authors Achatz, G.; Oberkofler, H.; Simon, B.; Lechenauer, E.; !1Unger, A.; Kandler, D.; Prillinger, H.J.; Ebner, C.; Kraft, !1D.; Breitenbach, M. !$#submission submitted to the EMBL Data Library, March 1994 !$#description Molecular characterization of allergens of Cladosporium !1herbarum and Alternaria alternata. !$#accession S43116 !'##molecule_type mRNA !'##residues 1-204 ##label ACH !'##cross-references EMBL:X78224; NID:g467628; PID:g467629 CLASSIFICATION #superfamily trp repressor-binding protein; flavodoxin !1homology KEYWORDS flavoprotein SUMMARY #length 204 #molecular-weight 22355 #checksum 420 SEQUENCE /// ENTRY A45029 #type complete TITLE brefeldin A resistance protein obr1 - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES protein p25 ORGANISM #formal_name Schizosaccharomyces pombe DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A45029; S34240; T38700 REFERENCE A45029 !$#authors Toda, T.; Shimanuki, M.; Saka, Y.; Yamano, H.; Adachi, Y.; !1Shirakawa, M.; Kyogoku, Y.; Yanagida, M. !$#journal Mol. Cell. Biol. (1992) 12:5474-5484 !$#title Fission yeast pap1-dependent transcription is negatively !1regulated by an essential nuclear protein, crm1. !$#cross-references MUID:93078747; PMID:1448080 !$#accession A45029 !'##molecule_type DNA !'##residues 1-202 ##label TOD !'##cross-references GB:D13038; NID:g218548; PIDN:BAA02370.1; !1PID:g287631 !'##note sequence extracted from NCBI backbone (NCBIN:119055, !1NCBIP:119056) !'##note part of this sequence was confirmed by protein sequencing REFERENCE S34240 !$#authors Turi, T.G.; Webster, P.; Rose, J.K. !$#submission submitted to the EMBL Data Library, April 1993 !$#description Isolation of mutant and plasmids conferring brefeldin A !1resistence in S. pombe. !$#accession S34240 !'##molecule_type DNA !'##residues 1-202 ##label TUR !'##cross-references EMBL:X73558; NID:g311845; PID:g311846 REFERENCE Z21805 !$#authors Brown, D.; Churcher, C.M.; Wood, V.; Barrell, B.G.; !1Rajandream, M.A. !$#submission submitted to the EMBL Data Library, September 1997 !$#accession T38700 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-202 ##label BRO !'##cross-references EMBL:Z99568; PIDN:CAB16744.1; GSPDB:GN00066; !1SPDB:SPAC3C7.14c !'##experimental_source strain 972h-; cosmid c3C7 GENETICS !$#gene obr1 !$#map_position 1 CLASSIFICATION #superfamily trp repressor-binding protein; flavodoxin !1homology KEYWORDS flavoprotein SUMMARY #length 202 #molecular-weight 21899 #checksum 4696 SEQUENCE /// ENTRY S43111 #type complete TITLE minor allergen - Alternaria alternata ORGANISM #formal_name Alternaria alternata DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 29-Oct-1999 ACCESSIONS S43111 REFERENCE S43108 !$#authors Achatz, G.; Oberkofler, H.; Simon, B.; Lechenauer, E.; !1Unger, A.; Kandler, D.; Prillinger, H.J.; Ebner, C.; Kraft, !1D.; Breitenbach, M. !$#submission submitted to the EMBL Data Library, March 1994 !$#description Molecular characterization of allergens of Cladosporium !1herbarum and Alternaria alternata. !$#accession S43111 !'##molecule_type mRNA !'##residues 1-204 ##label ACH !'##cross-references EMBL:X78225; NID:g467618; PID:g467619 CLASSIFICATION #superfamily trp repressor-binding protein; flavodoxin !1homology KEYWORDS flavoprotein SUMMARY #length 204 #molecular-weight 22056 #checksum 6123 SEQUENCE /// ENTRY G69292 #type complete TITLE tryptophan repressor binding protein (wrbA) homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69292 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession G69292 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-191 ##label KLE !'##cross-references GB:AE001081; GB:AE000782; NID:g2689404; !1PIDN:AAB90893.1; PID:g2650293; TIGR:AF0343 CLASSIFICATION #superfamily trp repressor-binding protein; flavodoxin !1homology KEYWORDS flavoprotein SUMMARY #length 191 #molecular-weight 20913 #checksum 2273 SEQUENCE /// ENTRY F69821 #type complete TITLE flavodoxin homolog yhcB - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F69821 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69821 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-176 ##label KUN !'##cross-references GB:Z99108; GB:AL009126; NID:g2633055; !1PIDN:CAB12730.1; PID:g2633225 !'##experimental_source strain 168 GENETICS !$#gene yhcB CLASSIFICATION #superfamily trp repressor-binding protein; flavodoxin !1homology KEYWORDS flavoprotein SUMMARY #length 176 #molecular-weight 19015 #checksum 4890 SEQUENCE /// ENTRY F70465 #type complete TITLE N-methylhydantoinase (ATP-hydrolyzing) (EC 3.5.2.14) - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F70465 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession F70465 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-521 ##label AQF !'##cross-references GB:AE000763; GB:AE000657; NID:g2984178; !1PIDN:AAC07716.1; PID:g2984184 !'##experimental_source strain VF5 GENETICS !$#gene hyuB CLASSIFICATION #superfamily N-methylhydantoinase (ATP-hydrolyzing) KEYWORDS hydrolase SUMMARY #length 521 #molecular-weight 57560 #checksum 6630 SEQUENCE /// ENTRY C64420 #type complete TITLE N-methylhydantoinase (ATP-hydrolyzing) (EC 3.5.2.14) - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C64420 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession C64420 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-563 ##label BUL !'##cross-references GB:U67539; GB:L77117; NID:g1591619; !1PIDN:AAB98965.1; PID:g1591627; TIGR:MJ0963 GENETICS !$#map_position REV897002-895311 CLASSIFICATION #superfamily N-methylhydantoinase (ATP-hydrolyzing) KEYWORDS hydrolase SUMMARY #length 563 #molecular-weight 62148 #checksum 7119 SEQUENCE /// ENTRY C42594 #type complete TITLE L-amino acid hydantoin hydrolase (ATP-hydrolyzing) (EC 3.5.2.-) hyuB [validated] - Pseudomonas sp. plasmid pHN671 ORGANISM #formal_name Pseudomonas sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-May-2000 ACCESSIONS C42594 REFERENCE A42594 !$#authors Watabe, K.; Ishikawa, T.; Mukohara, Y.; Nakamura, H. !$#journal J. Bacteriol. (1992) 174:962-969 !$#title Cloning and sequencing of the genes involved in the !1conversion of 5-substituted hydantoins to the corresponding !1L-amino acids from the native plasmid of Pseudomonas sp. !1strain NS671. !$#cross-references MUID:92121137; PMID:1732229 !$#accession C42594 !'##status preliminary !'##molecule_type DNA !'##residues 1-592 ##label WAT !'##cross-references GB:M72717; NID:g151280; PIDN:AAA25846.1; !1PID:g151283 !'##note sequence extracted from NCBI backbone (NCBIN:77753, !1NCBIP:77761) CLASSIFICATION #superfamily N-methylhydantoinase (ATP-hydrolyzing) KEYWORDS hydrolase SUMMARY #length 592 #molecular-weight 64858 #checksum 5879 SEQUENCE /// ENTRY S38058 #type complete TITLE hypothetical protein YKL215c - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein F1286 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S38058; S38053; S44323; S17009 REFERENCE S38054 !$#authors Alexandraki, D.; Tzermia, M. !$#submission submitted to the Protein Sequence Database, March 1994 !$#accession S38058 !'##molecule_type DNA !'##residues 1-1286 ##label ALE !'##cross-references EMBL:Z28215; NID:g486384; PID:g486385; !1GSPDB:GN00011; MIPS:YKL215c !'##experimental_source strain S288C REFERENCE S37897 !$#authors Pohl, T.M.; Pohl, F.M. !$#submission submitted to the Protein Sequence Database, March 1994 !$#accession S38053 !'##molecule_type DNA !'##residues 1-1182 ##label POH !'##cross-references EMBL:Z28215; GSPDB:GN00011; MIPS:YKL215c !'##experimental_source strain S288C REFERENCE S44319 !$#authors Tzermia, M.; Horaitis, O.; Alexandraki, D. !$#journal Yeast (1994) 10:663-679 !$#title The complete sequencing of a 24.6 kb segment of yeast !1chromosome XI identified the known loci URA1, SAC1 and TRP3, !1and revealed 6 new open reading frames including homologues !1to the threonine dehydratases, membrane transporters, !1hydantoinases and the phospholipase A(2)-activating protein. !$#cross-references MUID:95028164; PMID:7941750 !$#accession S44323 !'##molecule_type DNA !'##residues 1-1286 ##label TZE !'##cross-references EMBL:X75951; NID:g473130; PIDN:CAA53558.1; !1PID:g473135 REFERENCE S17008 !$#authors Roy, A. !$#submission submitted to the EMBL Data Library, May 1991 !$#description The URA1 gene of Saccharomyces cerevisiae encoding the !1dihydroorotic acid dehydrogenase. !$#accession S17009 !'##molecule_type DNA !'##residues 1003-1285 ##label ROY !'##cross-references EMBL:X59371 GENETICS !$#gene MIPS:YKL215c !'##cross-references SGD:S0001698 !$#map_position 11L CLASSIFICATION #superfamily hypothetical protein YKL215c SUMMARY #length 1286 #molecular-weight 140426 #checksum 7308 SEQUENCE /// ENTRY E70627 #type complete TITLE hypothetical protein Rv0266c - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E70627 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession E70627 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-1209 ##label COL !'##cross-references GB:Z86089; GB:AL123456; NID:g3261711; !1PIDN:CAB06678.1; PID:g1850111 !'##experimental_source strain H37Rv GENETICS !$#gene Rv0266c CLASSIFICATION #superfamily hypothetical protein YKL215c SUMMARY #length 1209 #molecular-weight 129649 #checksum 2260 SEQUENCE /// ENTRY S77037 #type complete TITLE hypothetical protein slr0697 - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S77037 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S77037 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1252 ##label KAN !'##cross-references EMBL:D64005; GB:AB001339; NID:g1001779; !1PID:g1006579 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily hypothetical protein YKL215c SUMMARY #length 1252 #molecular-weight 136051 #checksum 8249 SEQUENCE /// ENTRY S64322 #type complete TITLE probable membrane protein YGR031w - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein G4070 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S64322 REFERENCE S64071 !$#authors Rieger, M.; Mueller-Auer, S.; Brueckner, M.; Schaefer, M. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64322 !'##molecule_type DNA !'##residues 1-342 ##label RIE !'##cross-references EMBL:Z72816; NID:g1323009; PID:g1323010; !1GSPDB:GN00007; MIPS:YGR031w !'##experimental_source strain S288C GENETICS !$#gene MIPS:YGR031w !'##cross-references SGD:S0003263 !$#map_position 7R CLASSIFICATION #superfamily probable membrane protein YGR031w KEYWORDS transmembrane protein FEATURE !$147-163 #domain transmembrane #status predicted #label TMM SUMMARY #length 342 #molecular-weight 38510 #checksum 2149 SEQUENCE /// ENTRY E64203 #type complete TITLE ATP-dependent nuclease addA homolog - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 21-Jul-2000 ACCESSIONS E64203 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession E64203 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-666 ##label TIGR !'##cross-references GB:U39682; GB:L43967; NID:g3844634; !1PIDN:AAC71248.1; PID:g1045703; TIGR:MG032 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily ATP-dependent nuclease addA homolog SUMMARY #length 666 #molecular-weight 77302 #checksum 3239 SEQUENCE /// ENTRY S73445 #type complete TITLE MG032 homolog B01_orf666 - Mycoplasma pneumoniae (strain ATCC 29342) ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 10-Dec-1999 ACCESSIONS S73445 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73445 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-666 ##label HIM !'##cross-references EMBL:AE000014; GB:U00089; NID:g1673770; !1PIDN:AAB95767.1; PID:g1673777 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily ATP-dependent nuclease addA homolog SUMMARY #length 666 #molecular-weight 76898 #checksum 4042 SEQUENCE /// ENTRY S73438 #type complete TITLE MG032 homolog B01_orf672 - Mycoplasma pneumoniae (strain ATCC 29342) ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 10-Dec-1999 ACCESSIONS S73438 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73438 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-672 ##label HIM !'##cross-references EMBL:AE000013; GB:U00089; NID:g1673762; !1PIDN:AAB95760.1; PID:g1673769 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily ATP-dependent nuclease addA homolog SUMMARY #length 672 #molecular-weight 77588 #checksum 9360 SEQUENCE /// ENTRY S73444 #type complete TITLE MG032 homolog B01_orf673 - Mycoplasma pneumoniae (strain ATCC 29342) ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 10-Dec-1999 ACCESSIONS S73444 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73444 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-673 ##label HIM !'##cross-references EMBL:AE000014; GB:U00089; NID:g1673770; !1PIDN:AAB95766.1; PID:g1673776 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily ATP-dependent nuclease addA homolog SUMMARY #length 673 #molecular-weight 76629 #checksum 8329 SEQUENCE /// ENTRY S64306 #type complete TITLE hypothetical protein YGR015c - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein G4020 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S64306 REFERENCE S64071 !$#authors Rieger, M.; Mueller-Auer, S.; Brueckner, M.; Schaefer, M. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64306 !'##molecule_type DNA !'##residues 1-328 ##label RIE !'##cross-references EMBL:Z72800; NID:g1322979; PID:g1322980; !1GSPDB:GN00007; MIPS:YGR015c !'##experimental_source strain S288C GENETICS !$#gene MIPS:YGR015c !'##cross-references SGD:S0003247 !$#map_position 7R CLASSIFICATION #superfamily hypothetical protein YGR015c SUMMARY #length 328 #molecular-weight 37936 #checksum 1686 SEQUENCE /// ENTRY C64503 #type complete TITLE conserved hypothetical protein MJ1629 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C64503 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession C64503 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-292 ##label BUL !'##cross-references GB:U67603; GB:L77117; NID:g1592220; !1PIDN:AAB99650.1; PID:g1500528; TIGR:MJ1629 GENETICS !$#map_position REV1607294-1606416 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ1629 SUMMARY #length 292 #molecular-weight 34049 #checksum 7185 SEQUENCE /// ENTRY E71092 #type complete TITLE hypothetical protein PH1002 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E71092 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession E71092 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-352 ##label KAW !'##cross-references GB:AP000004; NID:g3236131; PIDN:BAA30099.1; !1PID:g3257416 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1002 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ1629 SUMMARY #length 352 #molecular-weight 39351 #checksum 4428 SEQUENCE /// ENTRY H69312 #type complete TITLE conserved hypothetical protein AF0504 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H69312 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession H69312 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-301 ##label KLE !'##cross-references GB:AE001069; GB:AE000782; NID:g2689392; !1PIDN:AAB90734.1; PID:g2650122; TIGR:AF0504 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ1629 SUMMARY #length 301 #molecular-weight 34490 #checksum 8039 SEQUENCE /// ENTRY C64647 #type complete TITLE serine proteinase (EC 3.4.21.-) - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS C64647 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession C64647 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-443 ##label TOM !'##cross-references GB:AE000610; GB:AE000511; NID:g2314160; !1PIDN:AAD08063.1; PID:g2314163; TIGR:HP1019 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily Helicobacter serine proteinase KEYWORDS hydrolase; serine proteinase SUMMARY #length 443 #molecular-weight 47983 #checksum 5112 SEQUENCE /// ENTRY I40059 #type complete TITLE htrA-like protein - Brucella abortus ORGANISM #formal_name Brucella abortus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS I40059 REFERENCE I40059 !$#authors Tatum, F.M.; Cheville, N.F.; Morfitt, D. !$#journal Microb. Pathog. (1994) 17:23-36 !$#title Cloning, characterization and construction of htrA and !1htrA-like mutants of Brucella abortus and their survival in !1BALB/c mice. !$#cross-references MUID:95165990; PMID:7861951 !$#accession I40059 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-474 ##label RES !'##cross-references EMBL:U07351; NID:g497154; PIDN:AAA70163.1; !1PID:g497155 CLASSIFICATION #superfamily Helicobacter serine proteinase SUMMARY #length 474 #molecular-weight 50159 #checksum 6556 SEQUENCE /// ENTRY S15337 #type complete TITLE heat shock protein htrA - Salmonella typhimurium ORGANISM #formal_name Salmonella typhimurium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S15337; S21327 REFERENCE S15337 !$#authors Johnson, K.; Charles, I.; Dougan, G.; Pickard, D.; O'Gaora, !1P.; Costa, G.; Ali, T.; Miller, I.; Hormaeche, C. !$#journal Mol. Microbiol. (1991) 5:401-407 !$#title The role of a stress-response protein in Salmonella !1typhimurium virulence. !$#cross-references MUID:91251770; PMID:1645840 !$#accession S15337 !'##molecule_type DNA !'##residues 1-475 ##label COS !'##cross-references EMBL:X54548; NID:g47929; PID:g47930 GENETICS !$#gene htrA CLASSIFICATION #superfamily Helicobacter serine proteinase SUMMARY #length 475 #molecular-weight 49315 #checksum 2814 SEQUENCE /// ENTRY A64113 #type complete TITLE heat shock protein htrA - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES periplasmic serine proteinase Do homolog ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS A64113 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession A64113 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-466 ##label TIGR !'##cross-references GB:U32805; GB:L42023; NID:g1574180; !1PIDN:AAC22906.1; PID:g1574189; TIGR:HI1259 GENETICS !$#gene htrA CLASSIFICATION #superfamily Helicobacter serine proteinase SUMMARY #length 466 #molecular-weight 49434 #checksum 4407 SEQUENCE /// ENTRY B70426 #type complete TITLE periplasmic serine proteinase (EC 3.4.21.-) - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B70426 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession B70426 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-453 ##label AQF !'##cross-references GB:AE000741; GB:AE000657; NID:g2983841; !1PIDN:AAC07399.1; PID:g2983845 !'##experimental_source strain VF5 GENETICS !$#gene htrA CLASSIFICATION #superfamily Helicobacter serine proteinase KEYWORDS hydrolase; serine proteinase SUMMARY #length 453 #molecular-weight 49958 #checksum 4021 SEQUENCE /// ENTRY F71275 #type complete TITLE probable periplasmic serine proteinase DO (htrA-2) - syphilis spirochete ORGANISM #formal_name Treponema pallidum subsp. pallidum #common_name syphilis spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS F71275 REFERENCE A71250 !$#authors Fraser, C.M.; Norris, S.J.; Weinstock, G.M.; White, O.; !1Sutton, G.G.; Dodson, R.; Gwinn, M.; Hickey, E.K.; Clayton, !1R.; Ketchum, K.A.; Sodergren, E.; Hardham, J.M.; McLeod, !1M.P.; Salzberg, S.; Peterson, J.; Khalak, H.; Richardson, !1D.; Howell, J.K.; Chidambaram, M.; Utterback, T.; McDonald, !1L.; Artiach, P.; Bowman, C.; Cotton, M.D.; Fujii, C.; !1Garland, S.; Hatch, B.; Horst, K.; Roberts, K.; Watthey, L.; !1Weidman, J.; Smith, H.O.; Venter, J.C. !$#journal Science (1998) 281:375-388 !$#title Complete genome sequence of Treponema pallidum, the syphilis !1spirochete. !$#cross-references MUID:98332770; PMID:9665876 !$#accession F71275 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-485 ##label COL !'##cross-references GB:AE001254; GB:AE000520; NID:g3323148; !1PIDN:AAC65807.1; PID:g3323153 !'##experimental_source strain Nichols GENETICS !$#gene TP0841 CLASSIFICATION #superfamily Helicobacter serine proteinase SUMMARY #length 485 #molecular-weight 51678 #checksum 801 SEQUENCE /// ENTRY I64103 #type complete TITLE trypsin-like proteinase degS (EC 3.4.21.-) HI0945 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Dec-2002 ACCESSIONS I64103 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession I64103 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-340 ##label TIGR !'##cross-references GB:U32775; GB:L42023; NID:g1573951; !1PIDN:AAC22599.1; PID:g1573965; TIGR:HI0945 CLASSIFICATION #superfamily Escherichia coli trypsin-like proteinase degS; !1GLGF domain homology; trypsin homology KEYWORDS hydrolase; serine proteinase FEATURE !$92,122,197 #active_site His, Asp, Ser #status predicted SUMMARY #length 340 #molecular-weight 36039 #checksum 8887 SEQUENCE /// ENTRY JC6052 #type complete TITLE trypsin-like proteinase degS (EC 3.4.21.-) - Escherichia coli (strain K-12) ALTERNATE_NAMES HhoB protein ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Dec-2002 ACCESSIONS JC6052; E65115 REFERENCE JC6051 !$#authors Bass, S.; Gu, Q.; Christen, A. !$#journal J. Bacteriol. (1996) 178:1154-1161 !$#title Multicopy suppressors of Prc mutant Escherichia coli include !1two HtrA (DegP) protease homologs (HhoAB), DksA, and a !1truncated RlpA. !$#cross-references MUID:96165273; PMID:8576052 !$#accession JC6052 !'##molecule_type DNA !'##residues 1-355 ##label BAS !'##cross-references GB:U15661; NID:g558911; PIDN:AAC43993.1; !1PID:g558913 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65115 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-355 ##label BLAT !'##cross-references GB:AE000402; GB:U00096; NID:g1789619; !1PIDN:AAC76267.1; PID:g1789630; UWGP:b3235 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene hhoB CLASSIFICATION #superfamily Escherichia coli trypsin-like proteinase degS; !1GLGF domain homology; trypsin homology KEYWORDS hydrolase; serine proteinase FEATURE !$96,126,201 #active_site His, Asp, Ser #status predicted SUMMARY #length 355 #molecular-weight 37581 #checksum 2524 SEQUENCE /// ENTRY D69109 #type complete TITLE serine proteinase HtrA - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Dec-2002 ACCESSIONS D69109 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession D69109 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-328 ##label MTH !'##cross-references GB:AE000935; GB:AE000666; NID:g2622945; !1PIDN:AAB86279.1; PID:g2622946 !'##experimental_source strain Delta H GENETICS !$#gene MTH1813 CLASSIFICATION #superfamily Escherichia coli trypsin-like proteinase degS; !1GLGF domain homology; trypsin homology SUMMARY #length 328 #molecular-weight 35299 #checksum 2163 SEQUENCE /// ENTRY C64772 #type complete TITLE probable transport protein yajR - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS C64772 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64772 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-456 ##label BLAT !'##cross-references GB:AE000149; GB:U00096; NID:g1786628; !1PIDN:AAC73530.1; PID:g1786630; UWGP:b0427 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yajR CLASSIFICATION #superfamily Escherichia coli probable transport protein !1yajR KEYWORDS transmembrane protein; transport protein FEATURE !$21-37 #domain transmembrane #status predicted #label TM1\ !$50-66 #domain transmembrane #status predicted #label TM2\ !$82-98 #domain transmembrane #status predicted #label TM3\ !$111-127 #domain transmembrane #status predicted #label TM4\ !$140-156 #domain transmembrane #status predicted #label TM5\ !$172-188 #domain transmembrane #status predicted #label TM6\ !$221-237 #domain transmembrane #status predicted #label TM7\ !$255-271 #domain transmembrane #status predicted #label TM8\ !$282-298 #domain transmembrane #status predicted #label TM9\ !$313-329 #domain transmembrane #status predicted #label TM10\ !$371-387 #domain transmembrane #status predicted #label TM11 SUMMARY #length 456 #molecular-weight 49040 #checksum 1189 SEQUENCE /// ENTRY A70406 #type complete TITLE transporter (major facilitator family) - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A70406 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession A70406 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-392 ##label AQF !'##cross-references GB:AE000729; GB:AE000657; NID:g2983659; !1PIDN:AAC07232.1; PID:g2983666 !'##experimental_source strain VF5 GENETICS !$#gene mffT2 CLASSIFICATION #superfamily Escherichia coli probable transport protein !1yajR SUMMARY #length 392 #molecular-weight 43056 #checksum 8454 SEQUENCE /// ENTRY E64667 #type complete TITLE multidrug-efflux transporter - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS E64667 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession E64667 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-443 ##label TOM !'##cross-references GB:AE000624; GB:AE000511; NID:g2314340; !1PIDN:AAD08227.1; PID:g2314341; TIGR:HP1181 CLASSIFICATION #superfamily Escherichia coli probable transport protein !1yajR SUMMARY #length 443 #molecular-weight 48844 #checksum 5565 SEQUENCE /// ENTRY C64971 #type complete TITLE hypothetical 36.1 kD protein in cpsB 5'region - Escherichia coli (strain K-12) ALTERNATE_NAMES cpsB 5'-region hypothetical protein 2 ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS C64971; D55239 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64971 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-321 ##label BLAT !'##cross-references GB:AE000295; GB:U00096; NID:g1788354; !1PIDN:AAC75113.1; PID:g1788365; UWGP:b2052 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A55239 !$#authors Aoyama, K.; Haase, A.M.; Reeves, P.R. !$#journal Mol. Biol. Evol. (1994) 11:829-838 !$#title Evidence for effect of random genetic drift on G+C content !1after lateral transfer of fucose pathway genes to !1Escherichia coli K-12. !$#cross-references MUID:95115532; PMID:7815923 !$#accession D55239 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-254,'DV',257-321 ##label AOY !'##cross-references GB:U38473; GB:L11721; NID:g3041811; !1PIDN:AAC77843.1; PID:g1407613 GENETICS !$#gene yefB CLASSIFICATION #superfamily Escherichia coli probable UDPglucose !14-epimerase SUMMARY #length 321 #molecular-weight 36141 #checksum 9326 SEQUENCE /// ENTRY C70714 #type complete TITLE probable epiA protein - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C70714 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession C70714 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-322 ##label COL !'##cross-references GB:Z79701; GB:AL123456; NID:g3261635; !1PIDN:CAB02026.1; PID:g1524259 !'##experimental_source strain H37Rv GENETICS !$#gene epiA CLASSIFICATION #superfamily Escherichia coli probable UDPglucose !14-epimerase SUMMARY #length 322 #molecular-weight 34537 #checksum 294 SEQUENCE /// ENTRY E64525 #type complete TITLE nodulation protein - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS E64525 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession E64525 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-310 ##label TOM !'##cross-references GB:AE000526; GB:AE000511; NID:g2313116; !1PIDN:AAD07113.1; PID:g2313120; TIGR:HP0045 CLASSIFICATION #superfamily Escherichia coli probable UDPglucose !14-epimerase SUMMARY #length 310 #molecular-weight 34812 #checksum 4748 SEQUENCE /// ENTRY S74432 #type complete TITLE hypothetical protein sll1213 - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S74432 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74432 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-312 ##label KAN !'##cross-references EMBL:D90899; GB:AB001339; NID:g1651650; !1PIDN:BAA16584.1; PID:g1651656 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily Escherichia coli probable UDPglucose !14-epimerase SUMMARY #length 312 #molecular-weight 34719 #checksum 6148 SEQUENCE /// ENTRY S12516 #type complete TITLE hypothetical protein - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 11-Jan-2000 ACCESSIONS S12516 REFERENCE S12516 !$#authors Szikora, J.P.; van Pel, A.; Brichard, V.; Andre, M.; van !1Baren, N.; Henry, P.; de Plaen, E.; Boon, T. !$#journal EMBO J. (1990) 9:1041-1050 !$#title Structure of the gene of tum(-) transplantation antigen !1P35B: presence of a point mutation in the antigenic allele. !$#cross-references MUID:90214611; PMID:2108859 !$#accession S12516 !'##status preliminary !'##molecule_type DNA !'##residues 1-271 ##label SZI CLASSIFICATION #superfamily Escherichia coli probable UDPglucose !14-epimerase SUMMARY #length 271 #molecular-weight 30080 #checksum 3927 SEQUENCE /// ENTRY A71183 #type complete TITLE probable UDP-glucose 4-epimerase - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A71183 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession A71183 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-306 ##label KAW !'##cross-references GB:AP000007; NID:g3236134; PIDN:BAA30856.1; !1PID:g3258173 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1742 CLASSIFICATION #superfamily Escherichia coli probable UDPglucose !14-epimerase SUMMARY #length 306 #molecular-weight 34069 #checksum 8100 SEQUENCE /// ENTRY F64103 #type complete TITLE suppressor protein suhB - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS F64103 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession F64103 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-267 ##label TIGR !'##cross-references GB:U32775; GB:L42023; NID:g1573951; !1PIDN:AAC22595.1; PID:g1573958; TIGR:HI0937 GENETICS !$#gene suhB CLASSIFICATION #superfamily suppressor protein suhB SUMMARY #length 267 #molecular-weight 29499 #checksum 6689 SEQUENCE /// ENTRY D65030 #type complete TITLE inositol-1(or 4)-monophosphatase (EC 3.1.3.25) [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES suppressor protein suhB ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS D65030; A35158 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65030 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-267 ##label BLAT !'##cross-references GB:AE000339; GB:U00096; NID:g1788870; !1PIDN:AAC75586.1; PID:g1788882; UWGP:b2533 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A35158 !$#authors Yano, R.; Nagai, H.; Shiba, K.; Yura, T. !$#journal J. Bacteriol. (1990) 172:2124-2130 !$#title A mutation that enhances synthesis of sigma(32) and !1suppresses temperature-sensitive growth of the rpoH15 mutant !1of Escherichia coli. !$#cross-references MUID:90202735; PMID:2138605 !$#accession A35158 !'##status preliminary !'##molecule_type DNA !'##residues 1-140,'L',142-267 ##label YAN !'##cross-references GB:M34828; NID:g147898; PIDN:AAA67506.1; !1PID:g147899 GENETICS !$#gene suhB COMPLEX monomer [validated, MUID:20213266] FUNCTION !$#description EC 3.1.3.25 [validated, MUID:20213266] !$#note inositol-1-phosphatase activity is neither sufficient nor !1required for complementation of suhB mutant suppressor !1effects CLASSIFICATION #superfamily suppressor protein suhB KEYWORDS phosphoric monoester hydrolase SUMMARY #length 267 #molecular-weight 29172 #checksum 7494 SEQUENCE /// ENTRY S75686 #type complete TITLE suppressor protein suhB - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein sll1383 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S75686 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75686 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-287 ##label KAN !'##cross-references EMBL:D90912; GB:AB001339; NID:g1653228; !1PIDN:BAA18247.1; PID:g1653332 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene suhB CLASSIFICATION #superfamily suppressor protein suhB SUMMARY #length 287 #molecular-weight 31296 #checksum 7019 SEQUENCE /// ENTRY C70470 #type complete TITLE myo-inositol-1(or 4)-monophosphatase - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C70470 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession C70470 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-264 ##label AQF !'##cross-references GB:AE000766; GB:AE000657; NID:g2984216; !1PIDN:AAC07753.1; PID:g2984224 !'##experimental_source strain VF5 GENETICS !$#gene imp2 CLASSIFICATION #superfamily suppressor protein suhB SUMMARY #length 264 #molecular-weight 29336 #checksum 512 SEQUENCE /// ENTRY S24343 #type complete TITLE inositol-1(or 4)-monophosphatase (EC 3.1.3.25) - African clawed frog ORGANISM #formal_name Xenopus laevis #common_name African clawed frog DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S24343 REFERENCE S24343 !$#authors Wreggett, K.A. !$#journal Biochem. J. (1992) 286:147-152 !$#title Inositol monophosphatase is a highly conserved enzyme having !1localized structural similarity to both glycerol 3-phosphate !1dehydrogenase and haemoglobin. !$#cross-references MUID:92392269; PMID:1325777 !$#accession S24343 !'##status preliminary !'##molecule_type mRNA !'##residues 1-284 ##label WRE !'##cross-references EMBL:X65513; NID:g64853; PIDN:CAA46486.1; !1PID:g64854 CLASSIFICATION #superfamily suppressor protein suhB KEYWORDS phosphoric monoester hydrolase SUMMARY #length 284 #molecular-weight 30642 #checksum 9088 SEQUENCE /// ENTRY A35223 #type complete TITLE inositol-1(or 4)-monophosphatase (EC 3.1.3.25) - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS A35223 REFERENCE A35223 !$#authors Diehl, R.E.; Whiting, P.; Potter, J.; Gee, N.; Ragan, C.I.; !1Linemeyer, D.; Schoepfer, R.; Bennett, C.; Dixon, R.A.F. !$#journal J. Biol. Chem. (1990) 265:5946-5949 !$#title Cloning and expression of bovine brain inositol !1monophosphatase. !$#cross-references MUID:90202852; PMID:1690719 !$#accession A35223 !'##status preliminary !'##molecule_type mRNA !'##residues 1-277 ##label DIE !'##cross-references GB:J05394; NID:g163224; PIDN:AAA30589.1; !1PID:g163225 CLASSIFICATION #superfamily suppressor protein suhB KEYWORDS phosphoric monoester hydrolase SUMMARY #length 277 #molecular-weight 30055 #checksum 4106 SEQUENCE /// ENTRY S23130 #type complete TITLE inositol-1(or 4)-monophosphatase (EC 3.1.3.25) - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Jun-2002 ACCESSIONS S23130 REFERENCE S23130 !$#authors McAllister, G.; Whiting, P.; Hammond, E.A.; Knowles, M.R.; !1Atack, J.R.; Bailey, F.J.; Maigetter, R.; Ragan, C.I. !$#journal Biochem. J. (1992) 284:749-754 !$#title cDNA cloning of human and rat brain myo-inositol !1monophosphatase. Expression and characterization of the !1human recombinant enzyme. !$#cross-references MUID:92321996; PMID:1377913 !$#accession S23130 !'##status preliminary !'##molecule_type mRNA !'##residues 1-277 ##label MCA !'##cross-references GB:X66922; GB:S38980; NID:g395339; PIDN:CAA47359.1; !1PID:g395340 GENETICS !$#gene GDB:IMPA1; IMPA !'##cross-references GDB:134653; OMIM:602064 !$#map_position 8q21.1-8q21.3 CLASSIFICATION #superfamily suppressor protein suhB KEYWORDS phosphoric monoester hydrolase SUMMARY #length 277 #molecular-weight 30189 #checksum 5824 SEQUENCE /// ENTRY E69864 #type complete TITLE myo-inositol-1(or 4)-monophosphatase homolog yktC - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69864 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69864 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-265 ##label KUN !'##cross-references GB:Z99111; GB:AL009126; NID:g2633699; !1PIDN:CAB13340.1; PID:g2633838 !'##experimental_source strain 168 GENETICS !$#gene yktC CLASSIFICATION #superfamily suppressor protein suhB SUMMARY #length 265 #molecular-weight 29759 #checksum 1200 SEQUENCE /// ENTRY H70530 #type complete TITLE probable extragenic suppressor protein SuhB - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H70530 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession H70530 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-290 ##label COL !'##cross-references GB:Z96072; GB:AL123456; NID:g3261793; !1PIDN:CAB09491.1; PID:g2181992 !'##experimental_source strain H37Rv GENETICS !$#gene suhB CLASSIFICATION #superfamily suppressor protein suhB SUMMARY #length 290 #molecular-weight 30027 #checksum 4335 SEQUENCE /// ENTRY F64159 #type complete TITLE hypothetical protein HI0841 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS F64159 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession F64159 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-585 ##label TIGR !'##cross-references GB:U32766; GB:L42023; NID:g1573854; !1PIDN:AAC22500.1; PID:g1573856; TIGR:HI0841 !'##note best homolog was a hypothetical protein from Escherichia coli CLASSIFICATION #superfamily hypothetical protein HI0841 SUMMARY #length 585 #molecular-weight 67737 #checksum 3379 SEQUENCE /// ENTRY C64988 #type complete TITLE probable sulfatase [imported] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS C64988 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64988 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-586 ##label BLAT !'##cross-references GB:AE000308; GB:U00096; NID:g1788508; !1PIDN:AAC75249.1; PID:g1788515; UWGP:b2188 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yejM CLASSIFICATION #superfamily hypothetical protein HI0841 SUMMARY #length 586 #molecular-weight 67295 #checksum 6907 SEQUENCE /// ENTRY C70356 #type complete TITLE conserved hypothetical protein aq_632 - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C70356 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession C70356 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-317 ##label AQF !'##cross-references GB:AE000699; GB:AE000657; NID:g2983238; !1PIDN:AAC06843.1; PID:g2983247 !'##experimental_source strain VF5 GENETICS !$#gene aq_632 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0486 SUMMARY #length 317 #molecular-weight 36509 #checksum 902 SEQUENCE /// ENTRY D69999 #type complete TITLE conserved hypothetical protein ytqA - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69999 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D69999 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-322 ##label KUN !'##cross-references GB:Z99119; GB:AL009126; NID:g2635411; !1PIDN:CAB15026.1; PID:g2635532 !'##experimental_source strain 168 GENETICS !$#gene ytqA CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0486 SUMMARY #length 322 #molecular-weight 36764 #checksum 6304 SEQUENCE /// ENTRY E65112 #type complete TITLE hypothetical 34.6 kD protein in arcB-gltB intergenic region - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS E65112 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65112 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-309 ##label BLAT !'##cross-references GB:AE000400; GB:U00096; NID:g2367203; !1PIDN:AAC76243.1; PID:g2367204; UWGP:b3211 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yhcC CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0486 SUMMARY #length 309 #molecular-weight 34606 #checksum 2650 SEQUENCE /// ENTRY F64360 #type complete TITLE conserved hypothetical protein homolog MJ0486 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F64360 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession F64360 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-322 ##label BUL !'##cross-references GB:U67498; GB:L77117; NID:g1591180; !1PIDN:AAB98477.1; PID:g1591189; TIGR:MJ0486 GENETICS !$#map_position REV430647-429679 !$#start_codon TTG CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0486 SUMMARY #length 322 #molecular-weight 37390 #checksum 1059 SEQUENCE /// ENTRY F64361 #type complete TITLE hypothetical protein MJ0494 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F64361 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession F64361 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-134 ##label BUL !'##cross-references GB:U67499; GB:L77117; NID:g1591190; !1PIDN:AAB98484.1; PID:g1591198; TIGR:MJ0494 GENETICS !$#map_position FOR436492-436896 !$#start_codon GTG CLASSIFICATION #superfamily hypothetical protein MJ0494 SUMMARY #length 134 #molecular-weight 15941 #checksum 8526 SEQUENCE /// ENTRY D71023 #type complete TITLE hypothetical protein PH1481 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D71023 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession D71023 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-120 ##label KAW !'##cross-references GB:AP000006; NID:g3236133; PIDN:BAA30588.1; !1PID:g3257905 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1481 CLASSIFICATION #superfamily hypothetical protein MJ0494 SUMMARY #length 120 #molecular-weight 14044 #checksum 5017 SEQUENCE /// ENTRY E69191 #type complete TITLE conserved hypothetical protein MTH687 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69191 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession E69191 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-124 ##label MTH !'##cross-references GB:AE000848; GB:AE000666; NID:g2621761; !1PIDN:AAB85192.1; PID:g2621772 !'##experimental_source strain Delta H GENETICS !$#gene MTH687 CLASSIFICATION #superfamily hypothetical protein MJ0494 SUMMARY #length 124 #molecular-weight 14568 #checksum 6847 SEQUENCE /// ENTRY A69311 #type complete TITLE conserved hypothetical protein AF0489 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A69311 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession A69311 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-132 ##label KLE !'##cross-references GB:AE001070; GB:AE000782; NID:g2689393; !1PIDN:AAB90748.1; PID:g2650137; TIGR:AF0489 CLASSIFICATION #superfamily hypothetical protein MJ0494 SUMMARY #length 132 #molecular-weight 15013 #checksum 5014 SEQUENCE /// ENTRY F64364 #type complete TITLE conserved hypothetical protein MJ0518 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F64364 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession F64364 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-94 ##label BUL !'##cross-references GB:U67501; GB:L77117; NID:g2826289; !1PIDN:AAB98507.1; PID:g1499317; TIGR:MJ0518 GENETICS !$#map_position REV460020-459736 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0518 SUMMARY #length 94 #molecular-weight 10552 #checksum 451 SEQUENCE /// ENTRY C69151 #type complete TITLE conserved hypothetical protein MTH395 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69151 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession C69151 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-108 ##label MTH !'##cross-references GB:AE000824; GB:AE000666; NID:g2621443; !1PIDN:AAB84901.1; PID:g2621457 !'##experimental_source strain Delta H GENETICS !$#gene MTH395 !$#start_codon GTG CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0518 SUMMARY #length 108 #molecular-weight 11877 #checksum 9286 SEQUENCE /// ENTRY F64368 #type complete TITLE conserved hypothetical protein MJ0550 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F64368 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession F64368 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-365 ##label BUL !'##cross-references GB:U67504; GB:L77117; NID:g1591248; !1PIDN:AAB98542.1; PID:g1591255; TIGR:MJ0550 GENETICS !$#map_position REV487108-486011 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0550 SUMMARY #length 365 #molecular-weight 42518 #checksum 186 SEQUENCE /// ENTRY C69101 #type complete TITLE conserved hypothetical protein MTH1751 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69101 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession C69101 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-311 ##label MTH !'##cross-references GB:AE000930; GB:AE000666; NID:g2622872; !1PIDN:AAB86221.1; PID:g2622883 !'##experimental_source strain Delta H GENETICS !$#gene MTH1751 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0550 SUMMARY #length 311 #molecular-weight 35662 #checksum 7503 SEQUENCE /// ENTRY D69376 #type complete TITLE conserved hypothetical protein AF1012 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69376 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession D69376 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-312 ##label KLE !'##cross-references GB:AE001034; GB:AE000782; NID:g2689357; !1PIDN:AAB90230.1; PID:g2649583; TIGR:AF1012 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0550 SUMMARY #length 312 #molecular-weight 35493 #checksum 5679 SEQUENCE /// ENTRY C71202 #type complete TITLE hypothetical protein PH1888 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C71202 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession C71202 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-329 ##label KAW !'##cross-references GB:AP000007; NID:g3236134; PIDN:BAA31010.1; !1PID:g3258327 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1888 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0550 SUMMARY #length 329 #molecular-weight 37884 #checksum 6939 SEQUENCE /// ENTRY F64369 #type complete TITLE conserved hypothetical protein MJ0558 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F64369 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession F64369 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-261 ##label BUL !'##cross-references GB:U67505; GB:L77117; NID:g2826297; !1PIDN:AAB98552.1; PID:g1591264; TIGR:MJ0558 GENETICS !$#map_position REV493986-493201 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0558 SUMMARY #length 261 #molecular-weight 29206 #checksum 4531 SEQUENCE /// ENTRY G69084 #type complete TITLE conserved hypothetical protein MTH163 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69084 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession G69084 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-265 ##label MTH !'##cross-references GB:AE000804; GB:AE000666; NID:g2621196; !1PIDN:AAB84669.1; PID:g2621205 !'##experimental_source strain Delta H GENETICS !$#gene MTH163 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0558 SUMMARY #length 265 #molecular-weight 29517 #checksum 2647 SEQUENCE /// ENTRY F69374 #type complete TITLE conserved hypothetical protein AF0998 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F69374 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession F69374 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-258 ##label KLE !'##cross-references GB:AE001035; GB:AE000782; NID:g2689358; !1PIDN:AAB90243.1; PID:g2649597; TIGR:AF0998 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0558 SUMMARY #length 258 #molecular-weight 28703 #checksum 4209 SEQUENCE /// ENTRY F64370 #type complete TITLE ferrous iron transport protein B - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS F64370 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession F64370 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-668 ##label BUL !'##cross-references GB:U67505; GB:L77117; NID:g2826297; !1PIDN:AAB98557.1; PID:g1591272; TIGR:MJ0566 GENETICS !$#map_position REV504509-502503 CLASSIFICATION #superfamily ferrous iron transport protein B; translation !1elongation factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop FEATURE !$10-17 #region nucleotide-binding motif A (P-loop)\ !$116-119 #region GTP-binding NKXD motif\ !$573-575 #region GTP-binding SAK/L motif SUMMARY #length 668 #molecular-weight 74454 #checksum 9972 SEQUENCE /// ENTRY G71063 #type complete TITLE probable ferrous iron transport protein B - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS G71063 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession G71063 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-661 ##label KAW !'##cross-references GB:AP000005; NID:g3236132; PIDN:BAA30305.1; !1PID:g3257622 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1205 CLASSIFICATION #superfamily ferrous iron transport protein B; translation !1elongation factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop FEATURE !$9-16 #region nucleotide-binding motif A (P-loop)\ !$116-119 #region GTP-binding NKXD motif SUMMARY #length 661 #molecular-weight 73605 #checksum 8360 SEQUENCE /// ENTRY C69549 #type complete TITLE iron (II) transporter (feoB-2) homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS C69549 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession C69549 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-563 ##label KLE !'##cross-references GB:AE001111; GB:AE000782; NID:g2689434; !1PIDN:AAB91270.1; PID:g2650700; TIGR:AF2394 CLASSIFICATION #superfamily ferrous iron transport protein B; translation !1elongation factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop FEATURE !$3-10 #region nucleotide-binding motif A (P-loop) SUMMARY #length 563 #molecular-weight 62038 #checksum 155 SEQUENCE /// ENTRY A69048 #type complete TITLE ferrous iron transport protein B - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS A69048 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession A69048 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-661 ##label MTH !'##cross-references GB:AE000899; GB:AE000666; NID:g2622468; !1PIDN:AAB85838.1; PID:g2622469 !'##experimental_source strain Delta H GENETICS !$#gene MTH1361 CLASSIFICATION #superfamily ferrous iron transport protein B; translation !1elongation factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop FEATURE !$8-15 #region nucleotide-binding motif A (P-loop) SUMMARY #length 661 #molecular-weight 72706 #checksum 8416 SEQUENCE /// ENTRY E70408 #type complete TITLE ferrous iron transport protein B - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS E70408 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession E70408 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-689 ##label AQF !'##cross-references GB:AE000731; GB:AE000657; NID:g2983691; !1PIDN:AAC07257.1; PID:g2983693 !'##experimental_source strain VF5 GENETICS !$#gene feoB CLASSIFICATION #superfamily ferrous iron transport protein B; translation !1elongation factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop FEATURE !$4-119 #domain translation elongation factor Tu homology !8#label ETU\ !$10-17 #region nucleotide-binding motif A (P-loop) SUMMARY #length 689 #molecular-weight 77434 #checksum 647 SEQUENCE /// ENTRY A36932 #type complete TITLE iron(II) transport system protein feoB - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS A36932; D65136 REFERENCE A36932 !$#authors Kammler, M.; Schon, C.; Hantke, K. !$#journal J. Bacteriol. (1993) 175:6212-6219 !$#title Characterization of the ferrous iron uptake system of !1Escherichia coli. !$#cross-references MUID:94012482; PMID:8407793 !$#contents K-12 !$#accession A36932 !'##status preliminary !'##molecule_type DNA !'##residues 1-773 ##label KAM !'##cross-references GB:X71063; NID:g414745; PIDN:CAA50387.1; !1PID:g1199515 !'##note sequence extracted from NCBI backbone (NCBIN:138048, !1NCBIP:138049) REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65136 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-773 ##label BLAT !'##cross-references GB:AE000416; GB:U00096; NID:g2367219; !1PIDN:AAC76434.1; PID:g1789813; UWGP:b3409 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene feoB CLASSIFICATION #superfamily ferrous iron transport protein B; translation !1elongation factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop; transmembrane !1protein FEATURE !$10-17 #region nucleotide-binding motif A (P-loop) SUMMARY #length 773 #molecular-weight 84473 #checksum 4092 SEQUENCE /// ENTRY S75294 #type complete TITLE ferrous iron transport protein B - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein slr1392 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S75294 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75294 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-614 ##label KAN !'##cross-references EMBL:D90904; GB:AB001339; NID:g1652225; !1PIDN:BAA17208.1; PID:g1652285 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene feoB CLASSIFICATION #superfamily ferrous iron transport protein B; translation !1elongation factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop FEATURE !$19-134 #domain translation elongation factor Tu homology !8#label ETU\ !$25-32 #region nucleotide-binding motif A (P-loop) SUMMARY #length 614 #molecular-weight 67405 #checksum 3342 SEQUENCE /// ENTRY C69126 #type complete TITLE ferrous iron transport protein B - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS C69126 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession C69126 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-638 ##label MTH !'##cross-references GB:AE000808; GB:AE000666; NID:g2621254; !1PIDN:AAB84719.1; PID:g2621259 !'##experimental_source strain Delta H GENETICS !$#gene MTH213 !$#start_codon TTG CLASSIFICATION #superfamily ferrous iron transport protein B; translation !1elongation factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop FEATURE !$14-21 #region nucleotide-binding motif A (P-loop) SUMMARY #length 638 #molecular-weight 70086 #checksum 9217 SEQUENCE /// ENTRY F69280 #type complete TITLE iron (II) transporter (feoB-1) homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS F69280 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession F69280 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-639 ##label KLE !'##cross-references GB:AE001089; GB:AE000782; NID:g2689412; !1PIDN:AAB90987.1; PID:g2650395; TIGR:AF0246 CLASSIFICATION #superfamily ferrous iron transport protein B; translation !1elongation factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop FEATURE !$21-28 #region nucleotide-binding motif A (P-loop) SUMMARY #length 639 #molecular-weight 70367 #checksum 5410 SEQUENCE /// ENTRY F64376 #type complete TITLE hypothetical protein MJ0614 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F64376 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession F64376 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-130 ##label BUL !'##cross-references GB:U67509; GB:L77117; NID:g1591315; !1PIDN:AAB98608.1; PID:g1591324; TIGR:MJ0614 GENETICS !$#map_position REV545452-545060 !$#start_codon TTG CLASSIFICATION #superfamily hypothetical protein MJ0614 SUMMARY #length 130 #molecular-weight 14873 #checksum 5108 SEQUENCE /// ENTRY D69227 #type complete TITLE hypothetical protein MTH952 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69227 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession D69227 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-128 ##label MTH !'##cross-references GB:AE000869; GB:AE000666; NID:g2622042; !1PIDN:AAB85448.1; PID:g2622049 !'##experimental_source strain Delta H GENETICS !$#gene MTH952 !$#start_codon GTG CLASSIFICATION #superfamily hypothetical protein MJ0614 SUMMARY #length 128 #molecular-weight 14175 #checksum 3948 SEQUENCE /// ENTRY S70955 #type complete TITLE otnF protein - Vibrio cholerae ORGANISM #formal_name Vibrio cholerae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S70955 REFERENCE S70952 !$#authors Bik, E.M.; Bunschoten, A.E.; Willems, R.J.L.; Chang, A.C.Y.; !1Mooi, F.R. !$#journal Mol. Microbiol. (1996) 20:799-811 !$#title Genetic organization and functional analysis of the otn DNA !1essential for cell-wall polysaccharide synthesis in Vibrio !1cholerae O139. !$#cross-references MUID:96386047; PMID:8793876 !$#accession S70955 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-288 ##label BIK !'##cross-references EMBL:X90547; NID:g1469276; PID:g1107920 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1995 GENETICS !$#gene otnF CLASSIFICATION #superfamily hypothetical protein b0985 SUMMARY #length 288 #molecular-weight 32136 #checksum 8920 SEQUENCE /// ENTRY G64839 #type complete TITLE ymcB protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS G64839 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64839 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-248 ##label BLAT !'##cross-references GB:AE000200; GB:U00096; NID:g2367111; !1PIDN:AAC74070.1; PID:g1787220; UWGP:b0985 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ymcB CLASSIFICATION #superfamily hypothetical protein b0985 SUMMARY #length 248 #molecular-weight 27296 #checksum 9756 SEQUENCE /// ENTRY C65210 #type complete TITLE hypothetical 26.3 kD protein in pgi-xylE intergenic region - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS C65210 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65210 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-245 ##label BLAT !'##cross-references GB:AE000476; GB:U00096; NID:g1790456; !1PIDN:AAC76998.1; PID:g1790460; UWGP:b4028 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yjbG CLASSIFICATION #superfamily hypothetical protein b0985 SUMMARY #length 245 #molecular-weight 26281 #checksum 1478 SEQUENCE /// ENTRY F64380 #type complete TITLE hypothetical protein MJ0646 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F64380 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession F64380 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-164 ##label BUL !'##cross-references GB:U67512; GB:L77117; NID:g1591352; !1PIDN:AAB98640.1; PID:g1591358; TIGR:MJ0646 GENETICS !$#map_position FOR574759-575253 CLASSIFICATION #superfamily Methanococcus jannaschi hypothetical protein !1MJ0646 SUMMARY #length 164 #molecular-weight 19895 #checksum 7206 SEQUENCE /// ENTRY D69208 #type complete TITLE conserved hypothetical protein MTH811 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69208 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession D69208 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-155 ##label MTH !'##cross-references GB:AE000858; GB:AE000666; NID:g2621885; !1PIDN:AAB85311.1; PID:g2621901 !'##experimental_source strain Delta H GENETICS !$#gene MTH811 !$#start_codon GTG CLASSIFICATION #superfamily Methanococcus jannaschi hypothetical protein !1MJ0646 SUMMARY #length 155 #molecular-weight 17352 #checksum 2206 SEQUENCE /// ENTRY E69208 #type complete TITLE conserved hypothetical protein MTH812 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69208 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession E69208 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-174 ##label MTH !'##cross-references GB:AE000859; GB:AE000666; NID:g2621902; !1PIDN:AAB85312.1; PID:g2621903 !'##experimental_source strain Delta H GENETICS !$#gene MTH812 CLASSIFICATION #superfamily Methanococcus jannaschi hypothetical protein !1MJ0646 SUMMARY #length 174 #molecular-weight 20394 #checksum 5807 SEQUENCE /// ENTRY A69021 #type complete TITLE tetrahydromethanopterin S-methyltransferase (EC 2.1.1.86) chain H MTH1156 [similarity] - Methanobacterium thermoautotrophicum (strain Delta H) ALTERNATE_NAMES N5-methyltetrahydromethanopterin-coenzyme M methyltransferase mtrH 34K chain ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 09-Jun-2000 #sequence_revision 09-Jun-2000 #text_change 18-Aug-2000 ACCESSIONS A69021 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession A69021 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-310 ##label MTH !'##cross-references GB:AE000885; GB:AE000666; NID:g2622256; !1PIDN:AAB85645.1; PID:g2622262 !'##experimental_source strain Delta H GENETICS !$#gene mtrH; MTH1156 FUNCTION !$#description catalyzes the reaction of N(5)-methyltetrahydromethanopterin !1and coenzyme M to form methyl-coenzyme M and !1tetrahydromethanopterin !$#pathway methanogenesis CLASSIFICATION #superfamily Methanobacterium tetrahydromethanopterin !1S-methyltransferase chain H KEYWORDS membrane-associated complex; methanogenesis; !1methyltransferase SUMMARY #length 310 #molecular-weight 33428 #checksum 1217 SEQUENCE /// ENTRY S68977 #type complete TITLE tetrahydromethanopterin S-methyltransferase (EC 2.1.1.86) chain H mtrH [validated] - Methanobacterium thermoautotrophicum (strain Marburg) ALTERNATE_NAMES N5-methyltetrahydromethanopterin-coenzyme M methyltransferase mtrH 34K chain ORGANISM #formal_name Methanobacterium thermoautotrophicum #variety strain Marburg, DSM 2133 DATE 09-Jun-2000 #sequence_revision 09-Jun-2000 #text_change 18-Aug-2000 ACCESSIONS S68977; S30345 REFERENCE S68974 !$#authors Harms, U.; Weiss, D.S.; Gaertner, P.; Linder, D.; Thauer, !1R.K. !$#journal Eur. J. Biochem. (1995) 228:640-648 !$#title The energy conserving N !1(5)-methyltetrahydromethanopterin:coenzyme M !1methyltransferase complex from Methanobacterium !1thermoautotrophicum is composed of eight different subunits. !$#cross-references MUID:95255265; PMID:7737157 !$#accession S68977 !'##molecule_type DNA !'##residues 1-310 ##label HAR !'##cross-references EMBL:X84219; NID:g668976; PIDN:CAA59003.1; !1PID:g668979 !'##experimental_source strain Marburg, DSM 2133 REFERENCE S30341 !$#authors Gaertner, P.; Ecker, A.; Fischer, R.; Linder, D.; Fuchs, G.; !1Thauer, R.K. !$#journal Eur. J. Biochem. (1993) 213:537-545 !$#title Purification and properties of N !1(5)-methyltetrahydromethanopterin: coenzyme M !1methyltransferase from Methanobacterium thermoautotrophicum. !$#cross-references MUID:93238732; PMID:8477726 !$#accession S30345 !'##molecule_type protein !'##residues 1-2;4-30 ##label GAE !'##experimental_source strain Marburg, DSM 2133 GENETICS !$#gene mtrH COMPLEX membrane-associated complex; heterooctamer of chains A (see !1PIR:S38369), B (see PIR:S38368), C (see PIR:S38367), D (see !1PIR:S38366), E (see PIR:S68974), F (see PIR:S68975), G (see !1PIR:S68976), and H FUNCTION !$#description catalyzes the reaction of N(5)-methyltetrahydromethanopterin !1and coenzyme M to form methyl-coenzyme M and !1tetrahydromethanopterin !$#pathway methanogenesis CLASSIFICATION #superfamily Methanobacterium tetrahydromethanopterin !1S-methyltransferase chain H KEYWORDS membrane-associated complex; methanogenesis; !1methyltransferase SUMMARY #length 310 #molecular-weight 33474 #checksum 1067 SEQUENCE /// ENTRY F64406 #type complete TITLE tetrahydromethanopterin S-methyltransferase (EC 2.1.1.86) chain H MJ0854 [similarity] - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 18-Aug-2000 ACCESSIONS F64406 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession F64406 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-333 ##label BUL !'##cross-references GB:U67529; GB:L77117; NID:g1591532; !1PIDN:AAB98859.1; PID:g1591539; TIGR:MJ0854 GENETICS !$#map_position FOR777714-778715 !$#start_codon TTG CLASSIFICATION #superfamily Methanobacterium tetrahydromethanopterin !1S-methyltransferase chain H KEYWORDS methyltransferase SUMMARY #length 333 #molecular-weight 36471 #checksum 7585 SEQUENCE /// ENTRY A69251 #type complete TITLE tetrahydromethanopterin S-methyltransferase (EC 2.1.1.86) chain H AF0009 [similarity] - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 18-Aug-2000 ACCESSIONS A69251 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession A69251 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-293 ##label KLE !'##cross-references GB:AE001106; GB:AE000782; NID:g2689429; !1PIDN:AAB91219.1; PID:g2650643; TIGR:AF0009 CLASSIFICATION #superfamily Methanobacterium tetrahydromethanopterin !1S-methyltransferase chain H KEYWORDS methyltransferase SUMMARY #length 293 #molecular-weight 32021 #checksum 3984 SEQUENCE /// ENTRY F64440 #type complete TITLE conserved hypothetical protein MJ1127 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F64440 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession F64440 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-280 ##label BUL !'##cross-references GB:U67555; GB:L77117; NID:g1591760; !1PIDN:AAB99129.1; PID:g1499979; TIGR:MJ1127 GENETICS !$#map_position FOR1068206-1069048 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ1127 SUMMARY #length 280 #molecular-weight 31671 #checksum 4613 SEQUENCE /// ENTRY B69174 #type complete TITLE conserved hypothetical protein MTH560 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69174 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession B69174 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-277 ##label MTH !'##cross-references GB:AE000838; GB:AE000666; NID:g2621625; !1PIDN:AAB85066.1; PID:g2621636 !'##experimental_source strain Delta H GENETICS !$#gene MTH560 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ1127 SUMMARY #length 277 #molecular-weight 30862 #checksum 2827 SEQUENCE /// ENTRY D71067 #type complete TITLE hypothetical protein PH1234 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D71067 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession D71067 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-279 ##label KAW !'##cross-references GB:AP000005; NID:g3236132; PIDN:BAA30334.1; !1PID:g3257651 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1234 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ1127 SUMMARY #length 279 #molecular-weight 31755 #checksum 5031 SEQUENCE /// ENTRY C69362 #type complete TITLE conserved hypothetical protein AF0899 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69362 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession C69362 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-274 ##label KLE !'##cross-references GB:AE001041; GB:AE000782; NID:g2689364; !1PIDN:AAB90339.1; PID:g2649698; TIGR:AF0899 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ1127 SUMMARY #length 274 #molecular-weight 30903 #checksum 7173 SEQUENCE /// ENTRY F64447 #type complete TITLE conserved hypothetical protein MJ1183 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F64447 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession F64447 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-161 ##label BUL !'##cross-references GB:U67559; GB:L77117; NID:g1591798; !1PIDN:AAB99184.1; PID:g1591810; TIGR:MJ1183 GENETICS !$#map_position FOR1122190-1122675 !$#start_codon TTG CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ1183 SUMMARY #length 161 #molecular-weight 18309 #checksum 3280 SEQUENCE /// ENTRY B69215 #type complete TITLE conserved hypothetical protein MTH862 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69215 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession B69215 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-153 ##label MTH !'##cross-references GB:AE000862; GB:AE000666; NID:g2621943; !1PIDN:AAB85360.1; PID:g2621954 !'##experimental_source strain Delta H GENETICS !$#gene MTH862 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ1183 SUMMARY #length 153 #molecular-weight 16874 #checksum 5295 SEQUENCE /// ENTRY F64450 #type complete TITLE hypothetical protein MJ1207 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F64450 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession F64450 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-226 ##label BUL !'##cross-references GB:U67562; GB:L77117; NID:g2826374; !1PIDN:AAB99211.1; PID:g1591837; TIGR:MJ1207 GENETICS !$#map_position FOR1150579-1151259 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ1207 SUMMARY #length 226 #molecular-weight 26939 #checksum 4214 SEQUENCE /// ENTRY A69315 #type complete TITLE proteinase synthase / sporulation regulator Pai1 homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A69315 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession A69315 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-147 ##label KLE !'##cross-references GB:AE001068; GB:AE000782; NID:g2689391; !1PIDN:AAB90723.1; PID:g2650111; TIGR:AF0521 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ1207 SUMMARY #length 147 #molecular-weight 17235 #checksum 2789 SEQUENCE /// ENTRY H70428 #type complete TITLE conserved hypothetical protein aq_1482 - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H70428 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession H70428 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-161 ##label AQF !'##cross-references GB:AE000742; GB:AE000657; NID:g2983858; !1PIDN:AAC07426.1; PID:g2983873 !'##experimental_source strain VF5 GENETICS !$#gene aq_1482 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ1207 SUMMARY #length 161 #molecular-weight 18866 #checksum 9403 SEQUENCE /// ENTRY E71208 #type complete TITLE hypothetical protein PH1933 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E71208 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession E71208 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-159 ##label KAW !'##cross-references GB:AP000007; NID:g3236134; PIDN:BAA31060.1; !1PID:g3258377 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1933 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ1207 SUMMARY #length 159 #molecular-weight 18463 #checksum 7774 SEQUENCE /// ENTRY B69143 #type complete TITLE hypothetical protein MTH336 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69143 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession B69143 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-173 ##label MTH !'##cross-references GB:AE000818; GB:AE000666; NID:g2621384; !1PIDN:AAB84842.1; PID:g2621392 !'##experimental_source strain Delta H GENETICS !$#gene MTH336 !$#start_codon TTG CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ1207 SUMMARY #length 173 #molecular-weight 20426 #checksum 9042 SEQUENCE /// ENTRY B69131 #type complete TITLE conserved hypothetical protein MTH249 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69131 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession B69131 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-197 ##label MTH !'##cross-references GB:AE000812; GB:AE000666; NID:g2621298; !1PIDN:AAB84755.1; PID:g2621299 !'##experimental_source strain Delta H GENETICS !$#gene MTH249 !$#start_codon TTG CLASSIFICATION #superfamily conserved hypothetical protein MJ1247 SUMMARY #length 197 #molecular-weight 21570 #checksum 2823 SEQUENCE /// ENTRY C69073 #type complete TITLE conserved hypothetical protein MTH1546 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69073 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession C69073 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-254 ##label MTH !'##cross-references GB:AE000915; GB:AE000666; NID:g2622664; !1PIDN:AAB86020.1; PID:g2622667 !'##experimental_source strain Delta H GENETICS !$#gene MTH1546 !$#start_codon GTG CLASSIFICATION #superfamily conserved hypothetical protein MJ1247 SUMMARY #length 254 #molecular-weight 28218 #checksum 8943 SEQUENCE /// ENTRY C69474 #type complete TITLE conserved hypothetical protein AF1796 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69474 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession C69474 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-183 ##label KLE !'##cross-references GB:AE000979; GB:AE000782; NID:g2689302; !1PIDN:AAB89472.1; PID:g2648766; TIGR:AF1796 CLASSIFICATION #superfamily conserved hypothetical protein MJ1247 SUMMARY #length 183 #molecular-weight 20147 #checksum 668 SEQUENCE /// ENTRY H69760 #type complete TITLE conserved hypothetical protein yckF - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H69760 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69760 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-185 ##label KUN !'##cross-references GB:Z99105; GB:AL009126; NID:g2632457; !1PIDN:CAB12139.1; PID:g2632631 !'##experimental_source strain 168 GENETICS !$#gene yckF CLASSIFICATION #superfamily conserved hypothetical protein MJ1247 SUMMARY #length 185 #molecular-weight 19963 #checksum 9693 SEQUENCE /// ENTRY F64455 #type complete TITLE hypothetical protein homolog MJ1247 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F64455 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession F64455 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-180 ##label BUL !'##cross-references GB:U67565; GB:L77117; NID:g1591874; !1PIDN:AAB99251.1; PID:g1591880; TIGR:MJ1247 GENETICS !$#map_position FOR1190147-1190689 !$#start_codon GTG CLASSIFICATION #superfamily conserved hypothetical protein MJ1247 SUMMARY #length 180 #molecular-weight 20443 #checksum 7619 SEQUENCE /// ENTRY F64462 #type complete TITLE polyferredoxin 2 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F64462 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession F64462 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-501 ##label BUL !'##cross-references GB:U67571; GB:L77117; NID:g1591939; !1PIDN:AAB99312.1; PID:g1591942; TIGR:MJ1303 GENETICS !$#map_position REV1252164-1250659 !$#start_codon TTG CLASSIFICATION #superfamily Methanococcus jannaschii polyferredoxin 2; !1ferredoxin 2[4Fe-4S] homology FEATURE !$222-284 #domain ferredoxin 2[4Fe-4S] homology #label FER4 SUMMARY #length 501 #molecular-weight 56296 #checksum 9193 SEQUENCE /// ENTRY H69032 #type complete TITLE polyferredoxin 2 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H69032 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession H69032 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-448 ##label MTH !'##cross-references GB:AE000891; GB:AE000666; NID:g2622345; !1PIDN:AAB85730.1; PID:g2622353 !'##experimental_source strain Delta H GENETICS !$#gene MTH1241 CLASSIFICATION #superfamily Methanococcus jannaschii polyferredoxin 2; !1ferredoxin 2[4Fe-4S] homology SUMMARY #length 448 #molecular-weight 48877 #checksum 5349 SEQUENCE /// ENTRY F64475 #type complete TITLE conserved hypothetical protein MJ1407 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F64475 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession F64475 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-129 ##label BUL !'##cross-references GB:U67581; GB:L77117; NID:g2826404; !1PIDN:AAB99415.1; PID:g1592056; TIGR:MJ1407 GENETICS !$#map_position FOR1368410-1368799 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ1407 SUMMARY #length 129 #molecular-weight 13724 #checksum 7153 SEQUENCE /// ENTRY F71142 #type complete TITLE hypothetical protein PH0353 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F71142 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession F71142 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-134 ##label KAW !'##cross-references GB:AP000002; NID:g3236129; PIDN:BAA29427.1; !1PID:g3256744 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0353 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ1407 SUMMARY #length 134 #molecular-weight 13982 #checksum 6330 SEQUENCE /// ENTRY B69071 #type complete TITLE conserved hypothetical protein MTH1530 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69071 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession B69071 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-131 ##label MTH !'##cross-references GB:AE000913; GB:AE000666; NID:g2622646; !1PIDN:AAB86004.1; PID:g2622649 !'##experimental_source strain Delta H GENETICS !$#gene MTH1530 !$#start_codon GTG CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ1407 SUMMARY #length 131 #molecular-weight 13823 #checksum 1088 SEQUENCE /// ENTRY G69256 #type complete TITLE conserved hypothetical protein AF0055 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69256 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession G69256 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-132 ##label KLE !'##cross-references GB:AE001102; GB:AE000782; NID:g2689425; !1PIDN:AAB91166.1; PID:g2650587; TIGR:AF0055 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ1407 SUMMARY #length 132 #molecular-weight 14189 #checksum 9121 SEQUENCE /// ENTRY B69475 #type complete TITLE conserved hypothetical protein AF1803 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69475 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession B69475 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-310 ##label KLE !'##cross-references GB:AE000978; GB:AE000782; NID:g2689301; !1PIDN:AAB89446.1; PID:g2648743; TIGR:AF1803 CLASSIFICATION #superfamily Archaeoglobus fulgidus conserved hypothetical !1protein AF1803 SUMMARY #length 310 #molecular-weight 34885 #checksum 190 SEQUENCE /// ENTRY B71051 #type complete TITLE conserved hypothetical protein PH1105 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B71051 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession B71051 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-342 ##label KAW !'##cross-references GB:AP000005; NID:g3236132; PIDN:BAA30204.1; !1PID:g3257521 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1105 CLASSIFICATION #superfamily Archaeoglobus fulgidus conserved hypothetical !1protein AF1803 SUMMARY #length 342 #molecular-weight 38464 #checksum 9375 SEQUENCE /// ENTRY C69042 #type complete TITLE conserved hypothetical protein MTH1319 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69042 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession C69042 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-330 ##label MTH !'##cross-references GB:AE000896; GB:AE000666; NID:g2622424; !1PIDN:AAB85797.1; PID:g2622425 !'##experimental_source strain Delta H GENETICS !$#gene MTH1319 CLASSIFICATION #superfamily Archaeoglobus fulgidus conserved hypothetical !1protein AF1803 SUMMARY #length 330 #molecular-weight 36485 #checksum 8566 SEQUENCE /// ENTRY C64360 #type complete TITLE conserved hypothetical protein MJ0483 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C64360 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession C64360 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-340 ##label BUL !'##cross-references GB:U67498; GB:L77117; NID:g1591180; !1PIDN:AAB98474.1; PID:g1591186; TIGR:MJ0483 GENETICS !$#map_position REV425125-424103 !$#start_codon TTG CLASSIFICATION #superfamily Archaeoglobus fulgidus conserved hypothetical !1protein AF1803 SUMMARY #length 340 #molecular-weight 40014 #checksum 9064 SEQUENCE /// ENTRY S48469 #type complete TITLE probable membrane protein YIL103w - yeast (Saccharomyces cerevisiae) ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S48469 REFERENCE S48455 !$#authors Bowman, S.; Churcher, C. !$#submission submitted to the EMBL Data Library, September 1994 !$#accession S48469 !'##molecule_type DNA !'##residues 1-425 ##label BOW !'##cross-references GB:Z47047; EMBL:Z38125; NID:g603997; PID:g763243; !1GSPDB:GN00009; MIPS:YIL103w GENETICS !$#gene MIPS:YIL103w !'##cross-references SGD:S0001365 !$#map_position 9L CLASSIFICATION #superfamily Archaeoglobus fulgidus conserved hypothetical !1protein AF1803 KEYWORDS transmembrane protein FEATURE !$155-171 #domain transmembrane #status predicted #label TM1\ !$334-350 #domain transmembrane #status predicted #label TM2 SUMMARY #length 425 #molecular-weight 48310 #checksum 8020 SEQUENCE /// ENTRY S48821 #type complete TITLE probable membrane protein YML076c - yeast (Saccharomyces cerevisiae) ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S48821 REFERENCE S48816 !$#authors Brown, D.; Bowman, S. !$#submission submitted to the EMBL Data Library, October 1994 !$#accession S48821 !'##molecule_type DNA !'##residues 1-944 ##label BRO !'##cross-references EMBL:Z46373; NID:g587529; PIDN:CAA86502.1; !1PID:g587535; GSPDB:GN00013; MIPS:YML076c GENETICS !$#gene MIPS:YML076c !'##cross-references SGD:S0004541 !$#map_position 13L CLASSIFICATION #superfamily yeast probable membrane protein YML076c; GAL4 !1zinc binuclear cluster homology KEYWORDS transmembrane protein FEATURE !$71-114 #domain GAL4 zinc binuclear cluster homology #label !8GAL4\ !$392-408 #domain transmembrane #status predicted #label TM1\ !$509-525 #domain transmembrane #status predicted #label TM2 SUMMARY #length 944 #molecular-weight 107559 #checksum 6903 SEQUENCE /// ENTRY B71209 #type complete TITLE probable D-arabino 3-hexulose 6-phosphate formaldehyde lyase - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B71209 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession B71209 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-406 ##label KAW !'##cross-references GB:AP000007; NID:g3236134; PIDN:BAA31065.1; !1PID:g3258382 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1938 CLASSIFICATION #superfamily probable D-arabino 3-hexulose 6-phosphate !1formaldehyde lyase SUMMARY #length 406 #molecular-weight 44409 #checksum 6207 SEQUENCE /// ENTRY E69357 #type complete TITLE D-arabino 3-hexulose 6-phosphate formaldehyde lyase (hps-1) homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69357 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession E69357 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-432 ##label KLE !'##cross-references GB:AE001045; GB:AE000782; NID:g2689368; !1PIDN:AAB90381.1; PID:g2649745; TIGR:AF0861 CLASSIFICATION #superfamily probable D-arabino 3-hexulose 6-phosphate !1formaldehyde lyase SUMMARY #length 432 #molecular-weight 46683 #checksum 1440 SEQUENCE /// ENTRY F64493 #type complete TITLE conserved hypothetical protein MJ1551 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F64493 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession F64493 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-57 ##label BUL !'##cross-references GB:U67596; GB:L77117; NID:g2826430; !1PIDN:AAB99571.1; PID:g1500444; TIGR:MJ1551 GENETICS !$#map_position FOR1528048-1528221 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ1551 SUMMARY #length 57 #molecular-weight 6515 #checksum 1194 SEQUENCE /// ENTRY D69466 #type complete TITLE conserved hypothetical protein AF1733 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69466 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession D69466 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-45 ##label KLE !'##cross-references GB:AE000983; GB:AE000782; NID:g2689306; !1PIDN:AAB89518.1; PID:g2648820; TIGR:AF1733 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ1551 SUMMARY #length 45 #molecular-weight 5241 #checksum 8298 SEQUENCE /// ENTRY B69017 #type complete TITLE conserved hypothetical protein MTH1128 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69017 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession B69017 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-64 ##label MTH !'##cross-references GB:AE000883; GB:AE000666; NID:g2622231; !1PIDN:AAB85617.1; PID:g2622232 !'##experimental_source strain Delta H GENETICS !$#gene MTH1128 !$#start_codon GTG CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ1551 SUMMARY #length 64 #molecular-weight 7429 #checksum 5490 SEQUENCE /// ENTRY F64494 #type complete TITLE conserved hypothetical protein MJ1559 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F64494 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession F64494 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-188 ##label BUL !'##cross-references GB:U67596; GB:L77117; NID:g2826430; !1PIDN:AAB99578.1; PID:g1500452; TIGR:MJ1559 GENETICS !$#map_position FOR1534701-1535267 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ1559 SUMMARY #length 188 #molecular-weight 21287 #checksum 4500 SEQUENCE /// ENTRY C71128 #type complete TITLE hypothetical protein PH0792 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C71128 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession C71128 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-172 ##label KAW !'##cross-references GB:AP000003; NID:g3236130; PIDN:BAA29885.1; !1PID:g3257202 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0792 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ1559 SUMMARY #length 172 #molecular-weight 19354 #checksum 3752 SEQUENCE /// ENTRY G69008 #type complete TITLE conserved hypothetical protein MTH1068 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69008 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession G69008 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-174 ##label MTH !'##cross-references GB:AE000877; GB:AE000666; NID:g2622157; !1PIDN:AAB85557.1; PID:g2622166 !'##experimental_source strain Delta H GENETICS !$#gene MTH1068 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ1559 SUMMARY #length 174 #molecular-weight 19425 #checksum 7108 SEQUENCE /// ENTRY F69351 #type complete TITLE conserved hypothetical protein AF0814 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F69351 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession F69351 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-165 ##label KLE !'##cross-references GB:AE001048; GB:AE000782; NID:g2689371; !1PIDN:AAB90428.1; PID:g2649795; TIGR:AF0814 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ1559 SUMMARY #length 165 #molecular-weight 18855 #checksum 2990 SEQUENCE /// ENTRY G70411 #type complete TITLE conserved hypothetical protein aq_1292 - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G70411 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession G70411 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-178 ##label AQF !'##cross-references GB:AE000733; GB:AE000657; NID:g2983720; !1PIDN:AAC07294.1; PID:g2983732 !'##experimental_source strain VF5 GENETICS !$#gene aq_1292 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ1559 SUMMARY #length 178 #molecular-weight 20555 #checksum 7880 SEQUENCE /// ENTRY F64497 #type complete TITLE hypothetical protein MJ1583 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F64497 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession F64497 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-126 ##label BUL !'##cross-references GB:U67598; GB:L77117; NID:g1592196; !1PIDN:AAB99603.1; PID:g1500478; TIGR:MJ1583 GENETICS !$#map_position FOR1557432-1557812 CLASSIFICATION #superfamily conserved hypothetical protein MJ1583 SUMMARY #length 126 #molecular-weight 14800 #checksum 6266 SEQUENCE /// ENTRY D71099 #type complete TITLE hypothetical protein PH1056 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D71099 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession D71099 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-136 ##label KAW !'##cross-references GB:AP000004; NID:g3236131; PIDN:BAA30154.1; !1PID:g3257471 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1056 CLASSIFICATION #superfamily conserved hypothetical protein MJ1583 SUMMARY #length 136 #molecular-weight 16014 #checksum 1671 SEQUENCE /// ENTRY A69280 #type complete TITLE conserved hypothetical protein AF0241 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A69280 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession A69280 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-139 ##label KLE !'##cross-references GB:AE001089; GB:AE000782; NID:g2689412; !1PIDN:AAB90992.1; PID:g2650400; TIGR:AF0241 CLASSIFICATION #superfamily conserved hypothetical protein MJ1583 SUMMARY #length 139 #molecular-weight 15809 #checksum 7359 SEQUENCE /// ENTRY A69107 #type complete TITLE conserved hypothetical protein MTH1797 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A69107 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession A69107 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-137 ##label MTH !'##cross-references GB:AE000934; GB:AE000666; NID:g2622924; !1PIDN:AAB86263.1; PID:g2622929 !'##experimental_source strain Delta H GENETICS !$#gene MTH1797 CLASSIFICATION #superfamily conserved hypothetical protein MJ1583 SUMMARY #length 137 #molecular-weight 15524 #checksum 750 SEQUENCE /// ENTRY C47040 #type complete TITLE orf3 3' to rcsF - Escherichia coli ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 24-Sep-1999 ACCESSIONS C47040 REFERENCE A47040 !$#authors Gervais, F.G.; Drapeau, G.R. !$#journal J. Bacteriol. (1992) 174:8016-8022 !$#title Identification, cloning, and characterization of rcsF, a new !1regulator gene for exopolysaccharide synthesis that !1suppresses the division mutation ftsZ84 in Escherichia coli !1K-12. !$#cross-references MUID:93094132; PMID:1459951 !$#contents K-12 !$#accession C47040 !'##status preliminary !'##molecule_type DNA !'##residues 1-161 ##label GER !'##cross-references GB:L04474; NID:g147530; PIDN:AAA24509.1; !1PID:g147533 !'##note sequence extracted from NCBI backbone (NCBIN:119949, !1NCBIP:119952) CLASSIFICATION #superfamily conserved hypothetical protein MJ1583 SUMMARY #length 161 #molecular-weight 18112 #checksum 2455 SEQUENCE /// ENTRY F64502 #type complete TITLE hypothetical protein MJ1624 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F64502 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession F64502 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-139 ##label BUL !'##cross-references GB:U67602; GB:L77117; NID:g1592214; !1PIDN:AAB99642.1; PID:g1592338; TIGR:MJ1624 GENETICS !$#map_position REV1600019-1599600 !$#start_codon TTG CLASSIFICATION #superfamily conserved hypothetical protein MJ1624 SUMMARY #length 139 #molecular-weight 16453 #checksum 3446 SEQUENCE /// ENTRY F71177 #type complete TITLE hypothetical protein PH1700 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F71177 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession F71177 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-132 ##label KAW !'##cross-references GB:AP000007; NID:g3236134; PIDN:BAA30813.1; !1PID:g3258130 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1700 CLASSIFICATION #superfamily conserved hypothetical protein MJ1624 SUMMARY #length 132 #molecular-weight 15398 #checksum 9880 SEQUENCE /// ENTRY A69363 #type complete TITLE conserved hypothetical protein AF0905 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A69363 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession A69363 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-124 ##label KLE !'##cross-references GB:AE001041; GB:AE000782; NID:g2689364; !1PIDN:AAB90335.1; PID:g2649694; TIGR:AF0905 CLASSIFICATION #superfamily conserved hypothetical protein MJ1624 SUMMARY #length 124 #molecular-weight 13948 #checksum 5916 SEQUENCE /// ENTRY A69219 #type complete TITLE conserved hypothetical protein MTH890 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A69219 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession A69219 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-138 ##label MTH !'##cross-references GB:AE000865; GB:AE000666; NID:g2621984; !1PIDN:AAB85388.1; PID:g2621985 !'##experimental_source strain Delta H GENETICS !$#gene MTH890 CLASSIFICATION #superfamily conserved hypothetical protein MJ1624 SUMMARY #length 138 #molecular-weight 15934 #checksum 6374 SEQUENCE /// ENTRY F64509 #type complete TITLE conserved hypothetical protein MJ1680 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F64509 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession F64509 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-155 ##label BUL !'##cross-references GB:U67608; GB:L77117; NID:g1592245; !1PIDN:AAB99701.1; PID:g1592247; TIGR:MJ1680 GENETICS !$#map_position FOR1662403-1662870 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ1680 SUMMARY #length 155 #molecular-weight 17778 #checksum 3987 SEQUENCE /// ENTRY H69286 #type complete TITLE conserved hypothetical protein AF0296 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H69286 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession H69286 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-157 ##label KLE !'##cross-references GB:AE001084; GB:AE000782; NID:g2689407; !1PIDN:AAB90932.1; PID:g2650335; TIGR:AF0296 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ1680 SUMMARY #length 157 #molecular-weight 18574 #checksum 3244 SEQUENCE /// ENTRY H71235 #type complete TITLE hypothetical protein PH0146 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H71235 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession H71235 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-167 ##label KAW !'##cross-references GB:AP000001; NID:g3236128; PIDN:BAA29215.1; !1PID:g3256532 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0146 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ1680 SUMMARY #length 167 #molecular-weight 19883 #checksum 1535 SEQUENCE /// ENTRY G71158 #type complete TITLE hypothetical protein PH0469 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G71158 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession G71158 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-146 ##label KAW !'##cross-references GB:AP000002; NID:g3236129; PIDN:BAA29556.1; !1PID:g3256873 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0469 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ1680 SUMMARY #length 146 #molecular-weight 16392 #checksum 7194 SEQUENCE /// ENTRY F64632 #type complete TITLE hypothetical protein HP0902 - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS F64632 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession F64632 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-99 ##label TOM !'##cross-references GB:AE000599; GB:AE000511; NID:g2314028; !1PIDN:AAD07951.1; PID:g2314040; TIGR:HP0902 CLASSIFICATION #superfamily hypothetical protein HP0902 SUMMARY #length 99 #molecular-weight 11030 #checksum 2678 SEQUENCE /// ENTRY D70381 #type complete TITLE hypothetical protein aq_943 - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D70381 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession D70381 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-107 ##label AQF !'##cross-references GB:AE000715; GB:AE000657; NID:g2983460; !1PIDN:AAC07054.1; PID:g2983474 !'##experimental_source strain VF5 GENETICS !$#gene aq_943 CLASSIFICATION #superfamily hypothetical protein HP0902 SUMMARY #length 107 #molecular-weight 12080 #checksum 6951 SEQUENCE /// ENTRY E64444 #type complete TITLE hypothetical protein MJ1157 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E64444 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession E64444 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-341 ##label BUL !'##cross-references GB:U67558; GB:L77117; NID:g1591786; !1PIDN:AAB99161.1; PID:g1592323; TIGR:MJ1157 GENETICS !$#map_position FOR1097616-1098641 CLASSIFICATION #superfamily conserved hypothetical protein MJ1157 SUMMARY #length 341 #molecular-weight 40094 #checksum 6665 SEQUENCE /// ENTRY E64484 #type complete TITLE hypothetical protein MJ1478 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E64484 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession E64484 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-303 ##label BUL !'##cross-references GB:U67588; GB:L77117; NID:g2826411; !1PIDN:AAB99482.1; PID:g1592117; TIGR:MJ1478 GENETICS !$#map_position REV1449450-1448539 CLASSIFICATION #superfamily conserved hypothetical protein MJ1157 SUMMARY #length 303 #molecular-weight 35542 #checksum 4746 SEQUENCE /// ENTRY F71455 #type complete TITLE hypothetical protein PH0300 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F71455 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession F71455 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-310 ##label KAW !'##cross-references GB:AP000001; NID:g3236128; PIDN:BAA29373.1; !1PID:g3256690 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0300 CLASSIFICATION #superfamily conserved hypothetical protein MJ1157 SUMMARY #length 310 #molecular-weight 35632 #checksum 7592 SEQUENCE /// ENTRY A69100 #type complete TITLE conserved hypothetical protein MTH1742 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A69100 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession A69100 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-270 ##label MTH !'##cross-references GB:AE000930; GB:AE000666; NID:g2622872; !1PIDN:AAB86212.1; PID:g2622874 !'##experimental_source strain Delta H GENETICS !$#gene MTH1742 CLASSIFICATION #superfamily conserved hypothetical protein MJ1157 SUMMARY #length 270 #molecular-weight 30292 #checksum 745 SEQUENCE /// ENTRY H69414 #type complete TITLE conserved hypothetical protein AF1321 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H69414 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession H69414 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-287 ##label KLE !'##cross-references GB:AE001012; GB:AE000782; NID:g2689335; !1PIDN:AAB89924.1; PID:g2649255; TIGR:AF1321 CLASSIFICATION #superfamily conserved hypothetical protein MJ1157 SUMMARY #length 287 #molecular-weight 32879 #checksum 8408 SEQUENCE /// ENTRY B69449 #type complete TITLE conserved hypothetical protein AF1595 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69449 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession B69449 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-304 ##label KLE !'##cross-references GB:AE000992; GB:AE000782; NID:g2689315; !1PIDN:AAB89651.1; PID:g2648962; TIGR:AF1595 CLASSIFICATION #superfamily conserved hypothetical protein MJ1157 SUMMARY #length 304 #molecular-weight 35365 #checksum 243 SEQUENCE /// ENTRY B69025 #type complete TITLE conserved hypothetical protein MTH1186 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69025 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession B69025 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-278 ##label MTH !'##cross-references GB:AE000887; GB:AE000666; NID:g2622289; !1PIDN:AAB85675.1; PID:g2622294 !'##experimental_source strain Delta H GENETICS !$#gene MTH1186 CLASSIFICATION #superfamily conserved hypothetical protein MJ1157 SUMMARY #length 278 #molecular-weight 31419 #checksum 4030 SEQUENCE /// ENTRY E70415 #type complete TITLE conserved hypothetical protein aq_1333 - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E70415 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession E70415 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-301 ##label AQF !'##cross-references GB:AE000735; GB:AE000657; NID:g2983749; !1PIDN:AAC07321.1; PID:g2983761 !'##experimental_source strain VF5 GENETICS !$#gene aq_1333 CLASSIFICATION #superfamily conserved hypothetical protein MJ1157 SUMMARY #length 301 #molecular-weight 34686 #checksum 8739 SEQUENCE /// ENTRY H71048 #type complete TITLE hypothetical protein PH1680 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H71048 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession H71048 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-320 ##label KAW !'##cross-references GB:AP000006; NID:g3236133; PIDN:BAA30792.1; !1PID:g3258109 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1680 CLASSIFICATION #superfamily conserved hypothetical protein MJ1157 SUMMARY #length 320 #molecular-weight 37040 #checksum 4773 SEQUENCE /// ENTRY F64667 #type complete TITLE conserved hypothetical protein HP1182 - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS F64667 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession F64667 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-253 ##label TOM !'##cross-references GB:AE000624; GB:AE000511; NID:g2314340; !1PIDN:AAD08228.1; PID:g2314342; TIGR:HP1182 CLASSIFICATION #superfamily conserved hypothetical protein MJ1157 SUMMARY #length 253 #molecular-weight 28569 #checksum 3803 SEQUENCE /// ENTRY C64884 #type complete TITLE ydaO protein - Escherichia coli (strain K-12) ALTERNATE_NAMES conserved hypothetical protein b1344 ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS C64884 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64884 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-311 ##label BLAT !'##cross-references GB:AE000232; GB:U00096; NID:g1787600; !1PIDN:AAC74426.1; PID:g1787606; UWGP:b1344 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ydaO CLASSIFICATION #superfamily conserved hypothetical protein MJ1157 SUMMARY #length 311 #molecular-weight 35561 #checksum 673 SEQUENCE /// ENTRY C69121 #type complete TITLE hypothetical protein MTH1904 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69121 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession C69121 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-122 ##label MTH !'##cross-references GB:AE000941; GB:AE000666; NID:g2623025; !1PIDN:AAB86364.1; PID:g2623037 !'##experimental_source strain Delta H GENETICS !$#gene MTH1904 CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum !1hypothetical protein MTH1904 SUMMARY #length 122 #molecular-weight 13458 #checksum 3282 SEQUENCE /// ENTRY E69397 #type complete TITLE hypothetical protein AF1182 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69397 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession E69397 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-118 ##label KLE !'##cross-references GB:AE001022; GB:AE000782; NID:g2689345; !1PIDN:AAB90064.1; PID:g2649405; TIGR:AF1182 CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum !1hypothetical protein MTH1904 SUMMARY #length 118 #molecular-weight 13383 #checksum 679 SEQUENCE /// ENTRY F64713 #type complete TITLE protein-export membrane protein - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS F64713 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession F64713 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-503 ##label TOM !'##cross-references GB:AE000652; GB:AE000511; NID:g2314720; !1PIDN:AAD08588.1; PID:g2314730; TIGR:HP1550 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily protein export membrane protein secD SUMMARY #length 503 #molecular-weight 54247 #checksum 3320 SEQUENCE /// ENTRY C70384 #type complete TITLE protein export membrane protein SecD - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C70384 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession C70384 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-501 ##label AQF !'##cross-references GB:AE000716; GB:AE000657; NID:g2983478; !1PIDN:AAC07060.1; PID:g2983481 !'##experimental_source strain VF5 GENETICS !$#gene secD CLASSIFICATION #superfamily protein export membrane protein secD SUMMARY #length 501 #molecular-weight 55459 #checksum 2250 SEQUENCE /// ENTRY I64056 #type complete TITLE secretion protein secD - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS I64056 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession I64056 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-616 ##label TIGR !'##cross-references GB:U32710; GB:L42023; NID:g1573200; !1PIDN:AAC21908.1; PID:g1573205; TIGR:HI0240 GENETICS !$#gene secD CLASSIFICATION #superfamily protein export membrane protein secD KEYWORDS inner membrane; protein export; transmembrane protein FEATURE !$10-30 #domain transmembrane #status predicted #label TM1\ !$457-473 #domain transmembrane #status predicted #label TM2\ !$478-498 #domain transmembrane #status predicted #label TM3\ !$503-519 #domain transmembrane #status predicted #label TM4\ !$565-581 #domain transmembrane #status predicted #label TM5\ !$587-606 #domain transmembrane #status predicted #label TM6 SUMMARY #length 616 #molecular-weight 66986 #checksum 7076 SEQUENCE /// ENTRY H64769 #type complete TITLE preprotein translocase chain secD [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES protein-export membrane protein secD; secretion protein secD ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS H64769; JQ0696; S12301 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64769 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-615 ##label BLAT !'##cross-references GB:AE000147; GB:U00096; NID:g1786603; !1PIDN:AAC73511.1; PID:g1786609; UWGP:b0408 !'##experimental_source strain K-12, substrain MG1655 REFERENCE JQ0693 !$#authors Gardel, C.; Johnson, K.; Jacq, A.; Beckwith, J. !$#journal EMBO J. (1990) 9:3209-3216 !$#title The secD locus of E.coli codes for two membrane proteins !1required for protein export. !$#cross-references MUID:91006014; PMID:2170107 !$#accession JQ0696 !'##molecule_type DNA !'##residues 1-77,'S',79-154,'A',156-615 ##label GAR !'##cross-references GB:X56175; NID:g42929; PIDN:CAA39634.1; PID:g581230 REFERENCE S12298 !$#authors Gardel, C.; Johnson, K.; Jacq, A.; Beckwith, J. !$#journal EMBO J. (1990) 9:4205-4206 !$#cross-references MUID:91065354; PMID:2249673 !$#contents erratum !$#accession S12301 !'##molecule_type DNA !'##residues 1-77,'S',79-154,'A',156-615 ##label GA2 !'##cross-references EMBL:X56175; NID:g42929; PID:g581230 REFERENCE A36969 !$#authors Pogliano, K.J.; Beckwith, J. !$#journal J. Bacteriol. (1994) 176:804-814 !$#title Genetic and molecular characterization of the Escherichia !1coli secD operon and its products. !$#cross-references MUID:94131960; PMID:7507921 !$#contents annotation; membrane topology GENETICS !$#gene secD !$#start_codon GTG COMPLEX heterohexamer; chains secY (PIR:QQECSY), secE (PIR:VXECSE), !1secG (PIR:S40402), secD (PIR:H64769), secF (PIR:JQ0697), and !1yajC (PIR:B64735); preprotein translocase contains a !1membrane-embedded trimeric complex of secY, secE and secG !1and the peripheral secA protein; the proteins secD, secF and !1yajC also form an integral membrane heterotrimeric complex. !1These two trimeric complexes are associated to form !1SecYEGDFyajC, the hexameric integral membrane domain of the !1pre-protein translocase FUNCTION !$#description the secD protein is a transmembrane component of the protein !1export complex [validated, MUID:91006014] CLASSIFICATION #superfamily protein export membrane protein secD KEYWORDS inner membrane; protein export; transmembrane protein FEATURE !$10-30 #domain transmembrane #status predicted #label TM1\ !$31-455 #domain periplasmic #status predicted #label PP1\ !$456-472 #domain transmembrane #status predicted #label TM2\ !$477-497 #domain transmembrane #status predicted #label TM3\ !$498-501 #domain periplasmic #status predicted #label PP2\ !$502-518 #domain transmembrane #status predicted #label TM4\ !$564-580 #domain transmembrane #status predicted #label TM5\ !$581-585 #domain periplasmic #status predicted #label PP3\ !$586-605 #domain transmembrane #status predicted #label TM6 SUMMARY #length 615 #molecular-weight 66631 #checksum 9609 SEQUENCE /// ENTRY S76266 #type complete TITLE hypothetical protein - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S76266 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76266 !'##status preliminary !'##molecule_type DNA !'##residues 1-472 ##label KAN !'##cross-references EMBL:D64000; GB:AB001339; NID:g1001484; !1PID:g1001493 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily protein export membrane protein secD SUMMARY #length 472 #molecular-weight 50468 #checksum 5774 SEQUENCE /// ENTRY H71326 #type complete TITLE probable protein-export membrane protein (secD) - syphilis spirochete ORGANISM #formal_name Treponema pallidum subsp. pallidum #common_name syphilis spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS H71326 REFERENCE A71250 !$#authors Fraser, C.M.; Norris, S.J.; Weinstock, G.M.; White, O.; !1Sutton, G.G.; Dodson, R.; Gwinn, M.; Hickey, E.K.; Clayton, !1R.; Ketchum, K.A.; Sodergren, E.; Hardham, J.M.; McLeod, !1M.P.; Salzberg, S.; Peterson, J.; Khalak, H.; Richardson, !1D.; Howell, J.K.; Chidambaram, M.; Utterback, T.; McDonald, !1L.; Artiach, P.; Bowman, C.; Cotton, M.D.; Fujii, C.; !1Garland, S.; Hatch, B.; Horst, K.; Roberts, K.; Watthey, L.; !1Weidman, J.; Smith, H.O.; Venter, J.C. !$#journal Science (1998) 281:375-388 !$#title Complete genome sequence of Treponema pallidum, the syphilis !1spirochete. !$#cross-references MUID:98332770; PMID:9665876 !$#accession H71326 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-583 ##label COL !'##cross-references GB:AE001219; GB:AE000520; NID:g3322693; !1PIDN:AAC65398.1; PID:g3322694 !'##experimental_source strain Nichols GENETICS !$#gene TP0410 CLASSIFICATION #superfamily protein export membrane protein secD SUMMARY #length 583 #molecular-weight 63860 #checksum 7295 SEQUENCE /// ENTRY S45776 #type complete TITLE uracil transport protein homolog YBL042c - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YBL0406 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S45776; S50783 REFERENCE S45745 !$#authors Goffeau, A.; Jonniaux, J.L.; Purnelle, B.; Skala, J.; de !1Wergifosse, P.; van Dyck, L. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S45776 !'##molecule_type DNA !'##residues 1-639 ##label GOF !'##cross-references EMBL:Z35803; NID:g536058; PID:g536059; !1GSPDB:GN00002; MIPS:YBL042c !'##experimental_source strain S288C REFERENCE S50284 !$#authors de Wergifosse, P.; Jacques, B.; Jonniaux, J.L.; Purnelle, !1B.; Skala, J.; Goffeau, A. !$#journal Yeast (1994) 10:1489-1496 !$#title The sequence of a 22.4 kb DNA fragment from the left arm of !1yeast chromosome II reveals homologues to bacterial proline !1synthetase and murine alpha-adaptin, as well as a new !1permease and a DNA-binding protein. !$#cross-references MUID:95176707; PMID:7871888 !$#accession S50783 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-639 ##label DEW !'##cross-references EMBL:X78214; NID:g463261; PIDN:CAA55059.1; !1PID:g872301 !'##experimental_source strain S288C GENETICS !$#gene SGD:FUI1; MIPS:YBL042c !'##cross-references SGD:S0000138 !$#map_position 2L CLASSIFICATION #superfamily uracil transport protein KEYWORDS transmembrane protein FEATURE !$162-181 #domain transmembrane #status predicted #label TM1\ !$199-218 #domain transmembrane #status predicted #label TM2\ !$222-238 #domain transmembrane #status predicted #label TM3\ !$257-278 #domain transmembrane #status predicted #label TM4\ !$289-305 #domain transmembrane #status predicted #label TM5\ !$332-348 #domain transmembrane #status predicted #label TM6\ !$364-393 #domain transmembrane #status predicted #label TM7\ !$417-433 #domain transmembrane #status predicted #label TM8\ !$460-478 #domain transmembrane #status predicted #label TM9\ !$482-503 #domain transmembrane #status predicted #label TM10\ !$537-554 #domain transmembrane #status predicted #label TM11\ !$570-590 #domain transmembrane #status predicted #label TM12 SUMMARY #length 639 #molecular-weight 72164 #checksum 158 SEQUENCE /// ENTRY H70064 #type complete TITLE permease homolog ywoE - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H70064 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H70064 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-490 ##label KUN !'##cross-references GB:Z99122; GB:AL009126; NID:g2636029; !1PIDN:CAB15664.1; PID:g2636172 !'##experimental_source strain 168 GENETICS !$#gene ywoE CLASSIFICATION #superfamily Escherichia coli probable transport protein !1b0511 SUMMARY #length 490 #molecular-weight 53982 #checksum 884 SEQUENCE /// ENTRY F64782 #type complete TITLE probable transport protein b0511 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS F64782 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64782 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-437 ##label BLAT !'##cross-references GB:AE000157; GB:U00096; NID:g1786716; !1PIDN:AAC73613.1; PID:g1786721; UWGP:b0511 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily Escherichia coli probable transport protein !1b0511 KEYWORDS transmembrane protein FEATURE !$15-31 #domain transmembrane #status predicted #label TM1\ !$82-98 #domain transmembrane #status predicted #label TM2\ !$105-121 #domain transmembrane #status predicted #label TM3\ !$143-159 #domain transmembrane #status predicted #label TM4\ !$179-195 #domain transmembrane #status predicted #label TM5\ !$221-237 #domain transmembrane #status predicted #label TM6\ !$259-275 #domain transmembrane #status predicted #label TM7\ !$304-320 #domain transmembrane #status predicted #label TM8\ !$328-344 #domain transmembrane #status predicted #label TM9\ !$375-391 #domain transmembrane #status predicted #label TM10\ !$405-421 #domain transmembrane #status predicted #label TM11 SUMMARY #length 437 #molecular-weight 46682 #checksum 3277 SEQUENCE /// ENTRY E42594 #type complete TITLE hypothetical protein ORF5 hyuC 3'-region, hyuE 5'-region - Pseudomonas sp. plasmid pHN671 ORGANISM #formal_name Pseudomonas sp. DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E42594; A41895 REFERENCE A42594 !$#authors Watabe, K.; Ishikawa, T.; Mukohara, Y.; Nakamura, H. !$#journal J. Bacteriol. (1992) 174:962-969 !$#title Cloning and sequencing of the genes involved in the !1conversion of 5-substituted hydantoins to the corresponding !1L-amino acids from the native plasmid of Pseudomonas sp. !1strain NS671. !$#cross-references MUID:92121137; PMID:1732229 !$#accession E42594 !'##status preliminary !'##molecule_type DNA !'##residues 1-245 ##label WA2 !'##cross-references GB:D10494; GB:D90469; NID:g216829; PIDN:BAA01380.1; !1PID:g216834 !'##note sequence extracted from NCBI backbone (NCBIN:77753, !1NCBIP:77764) REFERENCE A41895 !$#authors Watabe, K.; Ishikawa, T.; Mukohara, Y.; Nakamura, H. !$#journal J. Bacteriol. (1992) 174:3461-3466 !$#title Identification and sequencing of a gene encoding a hydantoin !1racemase from the native plasmid of Pseudomonas sp. strain !1NS671. !$#cross-references MUID:92276321; PMID:1339422 !$#accession A41895 !'##status preliminary !'##molecule_type DNA !'##residues 244-456 ##label WAT !'##experimental_source strain NS671 !'##note sequence extracted from NCBI backbone (NCBIN:104597, !1NCBIP:104598) GENETICS !$#genome plasmid CLASSIFICATION #superfamily Escherichia coli probable transport protein !1b0511 SUMMARY #length 456 #molecular-weight 50627 #checksum 9487 SEQUENCE /// ENTRY F64837 #type complete TITLE probable methyltransferase b0967 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS F64837 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64837 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-367 ##label BLAT !'##cross-references GB:AE000198; GB:U00096; NID:g1787189; !1PIDN:AAC74053.1; PID:g1787201; UWGP:b0967 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily probable methyltransferase b0967 SUMMARY #length 367 #molecular-weight 41054 #checksum 3485 SEQUENCE /// ENTRY S39674 #type complete TITLE ywbD protein - Bacillus subtilis ALTERNATE_NAMES hypothetical protein ipa-19d ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S39674; B70051 REFERENCE S39655 !$#authors Glaser, P.; Kunst, F.; Arnaud, M.; Coudart, M.P.; Gonzales, !1W.; Hullo, M.F.; Ionescu, M.; Lubochinsky, B.; Marcelino, !1L.; Moszer, I.; Presecan, E.; Santana, M.; Schneider, E.; !1Schweizer, J.; Vertes, A.; Rapoport, G.; Danchin, A. !$#journal Mol. Microbiol. (1993) 10:371-384 !$#title Bacillus subtilis genome project: cloning and sequencing of !1the 97 kb region from 325 degrees to 333 degrees. !$#cross-references MUID:95020537; PMID:7934828 !$#accession S39674 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-396 ##label GLA !'##cross-references EMBL:X73124; NID:g413923; PIDN:CAA51575.1; !1PID:g413943 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1993 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B70051 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-396 ##label KUN !'##cross-references GB:Z99123; GB:AL009126; NID:g2636240; !1PIDN:CAB15862.1; PID:g2636371 !'##experimental_source strain 168 GENETICS !$#gene ywbD CLASSIFICATION #superfamily probable methyltransferase b0967 SUMMARY #length 396 #molecular-weight 44443 #checksum 9547 SEQUENCE /// ENTRY A71206 #type complete TITLE hypothetical protein PH1915 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A71206 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession A71206 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-396 ##label KAW !'##cross-references GB:AP000007; NID:g3236134; PIDN:BAA31040.1; !1PID:g3258357 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1915 CLASSIFICATION #superfamily probable methyltransferase b0967 SUMMARY #length 396 #molecular-weight 44606 #checksum 5606 SEQUENCE /// ENTRY F70477 #type complete TITLE conserved hypothetical protein aq_2071 - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F70477 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession F70477 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-391 ##label AQF !'##cross-references GB:AE000771; GB:AE000657; NID:g2984286; !1PIDN:AAC07819.1; PID:g2984295 !'##experimental_source strain VF5 GENETICS !$#gene aq_2071 CLASSIFICATION #superfamily probable methyltransferase b0967 SUMMARY #length 391 #molecular-weight 44983 #checksum 396 SEQUENCE /// ENTRY C70348 #type complete TITLE conserved hypothetical protein aq_533 - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C70348 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession C70348 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-380 ##label AQF !'##cross-references GB:AE000694; GB:AE000657; NID:g2983162; !1PIDN:AAC06779.1; PID:g2983178 !'##experimental_source strain VF5 GENETICS !$#gene aq_533 CLASSIFICATION #superfamily probable methyltransferase b0967 SUMMARY #length 380 #molecular-weight 44277 #checksum 7727 SEQUENCE /// ENTRY F64941 #type complete TITLE rnd protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS F64941; S41588 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64941 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-193 ##label BLAT !'##cross-references GB:AE000275; GB:U00096; NID:g1788106; !1PIDN:AAC74876.1; PID:g1788108; UWGP:b1806 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S41588 !$#authors Fulda, M.; Heinz, E.; Wolter, F.P. !$#journal Mol. Gen. Genet. (1994) 242:241-249 !$#title The fadD gene of Escherichia coli K12 is located close to !1rnd at 39.6 min of the chromosomal map and is a new member !1of the AMP-binding protein family. !$#cross-references MUID:94150456; PMID:8107670 !$#accession S41588 !'##molecule_type DNA !'##residues 121-123,'P',125-193 ##label FUL GENETICS !$#gene rnd CLASSIFICATION #superfamily rnd protein SUMMARY #length 193 #molecular-weight 20921 #checksum 4328 SEQUENCE /// ENTRY S47726 #type complete TITLE outer-membrane lipoprotein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS S47726; E65148; I57857 REFERENCE S47666 !$#authors Plunkett, G. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S47726 !'##status preliminary !'##molecule_type DNA !'##residues 1-199 ##label PLU !'##cross-references EMBL:U00039; NID:g466582; PID:g466643 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65148 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-199 ##label BLAT !'##cross-references GB:AE000427; GB:U00096; NID:g1789919; !1PIDN:AAC76531.1; PID:g1789922; UWGP:b3506 !'##experimental_source strain K-12, substrain MG1655 REFERENCE I57857 !$#authors Alexander, D.M.; St John, A.C. !$#journal Mol. Microbiol. (1994) 11:1059-1071 !$#title Characterization of the carbon starvation-inducible and !1stationary phase-inducible gene slp encoding an outer !1membrane lipoprotein in Escherichia coli. !$#cross-references MUID:94293775; PMID:8022277 !$#accession I57857 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 12-199 ##label RES !'##cross-references GB:L23635; NID:g387931; PIDN:AAA60370.1; !1PID:g387932 GENETICS !$#gene slp CLASSIFICATION #superfamily rnd protein SUMMARY #length 199 #molecular-weight 22226 #checksum 3788 SEQUENCE /// ENTRY I64006 #type complete TITLE hypothetical protein HI0389 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS I64006 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession I64006 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-183 ##label TIGR !'##cross-references GB:U32722; GB:L42023; NID:g1573348; !1PIDN:AAC22047.1; PID:g1573359; TIGR:HI0389 CLASSIFICATION #superfamily rnd protein SUMMARY #length 183 #molecular-weight 21170 #checksum 6811 SEQUENCE /// ENTRY D64059 #type complete TITLE 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase (EC 4.1.3.-) HI0283 [similarity] - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS D64059 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession D64059 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-568 ##label TIGR !'##cross-references GB:U32714; GB:L42023; NID:g1573241; !1PIDN:AAC21946.1; PID:g1573248; TIGR:HI0283 CLASSIFICATION #superfamily menD protein KEYWORDS carbon-carbon lyase; oxo-acid-lyase SUMMARY #length 568 #molecular-weight 63097 #checksum 7321 SEQUENCE /// ENTRY G69656 #type complete TITLE 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase (EC 4.1.3.-) [validated] - Bacillus subtilis ALTERNATE_NAMES menCF protein; menD protein CONTAINS 2-oxoglutarate decarboxylase (EC 4.1.1.71) ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS G69656; A61649; S27509; S27510; T46640; T46641 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69656 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-580 ##label KUN !'##cross-references GB:Z99119; GB:AL009126; NID:g2635411; !1PIDN:CAB15060.1; PID:g2635566 !'##experimental_source strain 168 REFERENCE A61649 !$#authors Rowland, B.; Hill, K.; Mueller, J.; Driscoll, J.; Taber, H. !$#journal Gene (1995) 167:105-109 !$#title Structural organization of a Bacillus subtilis operon !1encoding menaquinone biosynthetic enzymes. !$#cross-references MUID:96144257; PMID:8566759 !$#accession A61649 !'##molecule_type DNA !'##residues 1-111,'R',113-151,'P',153-539,'RRQTS',545,'DSI' ##label RO2 !'##cross-references GB:M74538; GB:M74182; GB:M74183; NID:g1185287; !1PIDN:AAC37014.1; PID:g1185289 !'##note this is a revision to the sequence from reference S27507 REFERENCE S27507 !$#authors Rowland, B.; Hill, K.; Mueller, J.; Driscoll, J.; Taber, H. !$#submission submitted to the EMBL Data Library, October 1991 !$#description Organization of an operon involved in menaquinone !1biosynthesis in Bacillus subtilis. !$#accession S27509 !'##molecule_type DNA !'##residues 'MS',30,'LKIYT',36-111,'R',113-164,'ALSM' ##label ROW1 !'##cross-references EMBL:M74538; GB:M74182; GB:M74183; NID:g1185287 !'##note this sequence has been revised in reference A61649 !$#accession S27510 !'##molecule_type DNA !'##residues 178-539,'RRQTS',545,'DSI' ##label ROW2 !'##cross-references EMBL:M74538; GB:M74182; GB:M74183; NID:g1185287 !'##note this sequence has been revised in reference A61649 REFERENCE A42715 !$#authors Driscoll, J.R.; Taber, H.W. !$#journal J. Bacteriol. (1992) 174:5063-5071 !$#title Sequence organization and regulation of the Bacillus !1subtilis menBE operon. !$#cross-references MUID:92332443; PMID:1629163 !$#accession T46640 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 'MS',30,'LKIYT',36-111,'R',113-164,'ALSM' ##label DRI !'##cross-references EMBL:M74521; NID:g557486; PIDN:AAA50398.1; !1PID:g557489 !$#accession T46641 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 178-539,'RRQTS',545,'DSI' ##label DR2 !'##cross-references EMBL:M74521; NID:g557486; PIDN:AAA50399.1; !1PID:g557490 GENETICS !$#gene menD; menCF !$#start_codon TTG FUNCTION !$#pathway ubiquinone biosynthesis !$#note thiamine diphosphate cofactor CLASSIFICATION #superfamily menD protein KEYWORDS carbon-carbon lyase; carboxy-lyase; oxo-acid-lyase SUMMARY #length 580 #molecular-weight 64091 #checksum 8419 SEQUENCE /// ENTRY F70548 #type complete TITLE 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase (EC 4.1.3.-) menD [similarity] - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F70548 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession F70548 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-554 ##label COL !'##cross-references GB:Z95558; GB:AL123456; NID:g3261781; !1PIDN:CAB08966.1; PID:g2114017 !'##experimental_source strain H37Rv GENETICS !$#gene menD CLASSIFICATION #superfamily menD protein KEYWORDS carbon-carbon lyase; oxo-acid-lyase SUMMARY #length 554 #molecular-weight 57835 #checksum 445 SEQUENCE /// ENTRY D64758 #type complete TITLE probable transcription regulator yahB - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS D64758 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64758 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-310 ##label BLAT !'##cross-references GB:AE000138; GB:U00096; NID:g1786501; !1PIDN:AAC73419.1; PID:g1786508; UWGP:b0316 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yahB CLASSIFICATION #superfamily probable transcription regulator ybbS KEYWORDS DNA binding; transcription regulation FEATURE !$22-41 #region helix-turn-helix motif SUMMARY #length 310 #molecular-weight 34866 #checksum 6904 SEQUENCE /// ENTRY G64781 #type complete TITLE probable transcription regulator ybbS - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS G64781 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64781 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-308 ##label BLAT !'##cross-references GB:AE000156; GB:U00096; NID:g1786705; !1PIDN:AAC73606.1; PID:g1786713; UWGP:b0504 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ybbS CLASSIFICATION #superfamily probable transcription regulator ybbS KEYWORDS DNA binding; transcription regulation FEATURE !$19-38 #region helix-turn-helix motif SUMMARY #length 308 #molecular-weight 34511 #checksum 7547 SEQUENCE /// ENTRY E64923 #type complete TITLE probable transcription regulator ydbH - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS E64923 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64923 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-310 ##label BLAT !'##cross-references GB:AE000261; GB:U00096; NID:g1787945; !1PIDN:AAC74731.1; PID:g1787949; UWGP:b1659 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ydhB CLASSIFICATION #superfamily probable transcription regulator ybbS KEYWORDS DNA binding; transcription regulation FEATURE !$18-48 #region regulatory protein lysR motif\ !$19-38 #region helix-turn-helix motif SUMMARY #length 310 #molecular-weight 35250 #checksum 726 SEQUENCE /// ENTRY F65099 #type complete TITLE hypothetical transcription regulator exuR-tdcC intergenic region - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS F65099 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65099 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-298 ##label BLAT !'##cross-references GB:AE000392; GB:U00096; NID:g2367194; !1PIDN:AAC76140.1; PID:g1789492; UWGP:b3105 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yhaJ CLASSIFICATION #superfamily probable transcription regulator ybbS SUMMARY #length 298 #molecular-weight 33256 #checksum 8077 SEQUENCE /// ENTRY F64966 #type complete TITLE probable transcription regulator yeeY - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS F64966 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64966 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-316 ##label BLAT !'##cross-references GB:AE000293; GB:U00096; NID:g2367127; !1PIDN:AAC75076.1; PID:g1788326; UWGP:b2015 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yeeY CLASSIFICATION #superfamily probable transcription regulator ybbS KEYWORDS DNA binding; nucleotide binding; P-loop; transcription !1regulation FEATURE !$307-314 #region nucleotide-binding motif A (P-loop) SUMMARY #length 316 #molecular-weight 34900 #checksum 2893 SEQUENCE /// ENTRY A64362 #type complete TITLE hypothetical protein MJ0497 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A64362 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession A64362 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-133 ##label BUL !'##cross-references GB:U67499; GB:L77117; NID:g1591190; !1PIDN:AAB98490.1; PID:g1499294; TIGR:MJ0497 GENETICS !$#map_position REV439221-438820 CLASSIFICATION #superfamily hypothetical protein MJ0497 SUMMARY #length 133 #molecular-weight 15232 #checksum 2438 SEQUENCE /// ENTRY B71004 #type complete TITLE hypothetical protein PH1328 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B71004 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession B71004 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-124 ##label KAW !'##cross-references GB:AP000006; NID:g3236133; PIDN:BAA30434.1; !1PID:g3257751 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1328 CLASSIFICATION #superfamily hypothetical protein MJ0497 SUMMARY #length 124 #molecular-weight 13654 #checksum 6965 SEQUENCE /// ENTRY D69495 #type complete TITLE conserved hypothetical protein AF1965 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69495 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession D69495 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-136 ##label KLE !'##cross-references GB:AE000967; GB:AE000782; NID:g2689290; !1PIDN:AAB89293.1; PID:g2648580; TIGR:AF1965 CLASSIFICATION #superfamily hypothetical protein MJ0497 SUMMARY #length 136 #molecular-weight 15437 #checksum 307 SEQUENCE /// ENTRY F69036 #type complete TITLE conserved hypothetical protein MTH1270 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F69036 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession F69036 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-136 ##label MTH !'##cross-references GB:AE000893; GB:AE000666; NID:g2622375; !1PIDN:AAB85757.1; PID:g2622382 !'##experimental_source strain Delta H GENETICS !$#gene MTH1270 CLASSIFICATION #superfamily hypothetical protein MJ0497 SUMMARY #length 136 #molecular-weight 15395 #checksum 9403 SEQUENCE /// ENTRY F69100 #type complete TITLE conserved hypothetical protein MTH1747 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F69100 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession F69100 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-264 ##label MTH !'##cross-references GB:AE000930; GB:AE000666; NID:g2622872; !1PIDN:AAB86217.1; PID:g2622879 !'##experimental_source strain Delta H GENETICS !$#gene MTH1747 !$#start_codon TTG CLASSIFICATION #superfamily conserved hypothetical protein MTH1747 SUMMARY #length 264 #molecular-weight 28996 #checksum 4086 SEQUENCE /// ENTRY S28373 #type complete TITLE hypothetical protein 260 - Methanothermus fervidus ORGANISM #formal_name Methanothermus fervidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S28373; S78469 REFERENCE S28373 !$#authors Haas, E.S.; Brown, J.W.; Daniels, C.J.; Reeve, J.N. !$#journal Gene (1990) 90:51-59 !$#title Genes encoding the 7S RNA and tRNA(Ser) are linked to one of !1the two rRNA operons in the genome of the extremely !1thermophilic archaebacterium Methanothermus fervidus. !$#cross-references MUID:90337347; PMID:2116370 !$#accession S28373 !'##molecule_type DNA !'##residues 1-260 ##label HAA !'##cross-references EMBL:M32222 REFERENCE S78469 !$#authors Daniels, C.J. !$#submission submitted to the EMBL Data Library, February 1990 !$#accession S78469 !'##status preliminary !'##molecule_type DNA !'##residues 1-249,'EC' ##label DAN !'##cross-references EMBL:M32222; NID:g149810; PID:g149811 CLASSIFICATION #superfamily conserved hypothetical protein MTH1747 SUMMARY #length 260 #molecular-weight 29663 #checksum 988 SEQUENCE /// ENTRY C69185 #type complete TITLE conserved hypothetical protein MTH641 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69185 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession C69185 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-140 ##label MTH !'##cross-references GB:AE000844; GB:AE000666; NID:g2621707; !1PIDN:AAB85146.1; PID:g2621722 !'##experimental_source strain Delta H GENETICS !$#gene MTH641 CLASSIFICATION #superfamily Methanobacterium conserved hypothetical protein !1MTH641 SUMMARY #length 140 #molecular-weight 16051 #checksum 7325 SEQUENCE /// ENTRY G69297 #type complete TITLE endonuclease III homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69297 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession G69297 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-100 ##label KLE !'##cross-references GB:AE001078; GB:AE000782; NID:g2689401; !1PIDN:AAB90863.1; PID:g2650260; TIGR:AF0383 CLASSIFICATION #superfamily Methanobacterium conserved hypothetical protein !1MTH641 SUMMARY #length 100 #molecular-weight 11462 #checksum 8554 SEQUENCE /// ENTRY D71107 #type complete TITLE hypothetical protein PH0629 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D71107 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession D71107 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-139 ##label KAW !'##cross-references GB:AP000003; NID:g3236130; PIDN:BAA29718.1; !1PID:g3257035 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0629 CLASSIFICATION #superfamily Methanobacterium conserved hypothetical protein !1MTH641 SUMMARY #length 139 #molecular-weight 16351 #checksum 1402 SEQUENCE /// ENTRY G71196 #type complete TITLE probable ribokinase - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G71196 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession G71196 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-296 ##label KAW !'##cross-references GB:AP000007; NID:g3236134; PIDN:BAA30966.1; !1PID:g3258283 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1845 CLASSIFICATION #superfamily probable ribokinase SUMMARY #length 296 #molecular-weight 32492 #checksum 4139 SEQUENCE /// ENTRY A69073 #type complete TITLE ribokinase - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A69073 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession A69073 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-309 ##label MTH !'##cross-references GB:AE000915; GB:AE000666; NID:g2622664; !1PIDN:AAB86018.1; PID:g2622665 !'##experimental_source strain Delta H GENETICS !$#gene MTH1544 CLASSIFICATION #superfamily probable ribokinase SUMMARY #length 309 #molecular-weight 33672 #checksum 8244 SEQUENCE /// ENTRY C69113 #type complete TITLE ribokinase - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69113 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession C69113 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-278 ##label MTH !'##cross-references GB:AE000937; GB:AE000666; NID:g2622974; !1PIDN:AAB86307.1; PID:g2622976 !'##experimental_source strain Delta H GENETICS !$#gene MTH1841 !$#start_codon TTG CLASSIFICATION #superfamily probable ribokinase SUMMARY #length 278 #molecular-weight 29847 #checksum 7961 SEQUENCE /// ENTRY D69294 #type complete TITLE carbohydrate kinase, pfkB family homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69294 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession D69294 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-250 ##label KLE !'##cross-references GB:AE001080; GB:AE000782; NID:g2689403; !1PIDN:AAB90880.1; PID:g2650279; TIGR:AF0356 CLASSIFICATION #superfamily probable ribokinase SUMMARY #length 250 #molecular-weight 27536 #checksum 4485 SEQUENCE /// ENTRY F69152 #type complete TITLE ribokinase - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F69152 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession F69152 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-298 ##label MTH !'##cross-references GB:AE000825; GB:AE000666; NID:g2621465; !1PIDN:AAB84910.1; PID:g2621467 !'##experimental_source strain Delta H GENETICS !$#gene MTH404 CLASSIFICATION #superfamily probable ribokinase SUMMARY #length 298 #molecular-weight 31406 #checksum 4113 SEQUENCE /// ENTRY F69178 #type complete TITLE conserved hypothetical protein MTH593 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F69178 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession F69178 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-233 ##label MTH !'##cross-references GB:AE000841; GB:AE000666; NID:g2621665; !1PIDN:AAB85099.1; PID:g2621672 !'##experimental_source strain Delta H GENETICS !$#gene MTH593 CLASSIFICATION #superfamily conserved hypothetical protein MTH593 SUMMARY #length 233 #molecular-weight 24993 #checksum 5095 SEQUENCE /// ENTRY E69178 #type complete TITLE conserved hypothetical protein MTH592 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69178 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession E69178 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-224 ##label MTH !'##cross-references GB:AE000841; GB:AE000666; NID:g2621665; !1PIDN:AAB85098.1; PID:g2621671 !'##experimental_source strain Delta H GENETICS !$#gene MTH592 CLASSIFICATION #superfamily conserved hypothetical protein MTH593 SUMMARY #length 224 #molecular-weight 24457 #checksum 7018 SEQUENCE /// ENTRY G69293 #type complete TITLE conserved hypothetical protein AF0351 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69293 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession G69293 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-226 ##label KLE !'##cross-references GB:AE001080; GB:AE000782; NID:g2689403; !1PIDN:AAB90883.1; PID:g2650282; TIGR:AF0351 CLASSIFICATION #superfamily conserved hypothetical protein MTH593 SUMMARY #length 226 #molecular-weight 24820 #checksum 4053 SEQUENCE /// ENTRY A71241 #type complete TITLE hypothetical protein PH0187 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A71241 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession A71241 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-251 ##label KAW !'##cross-references GB:AP000001; NID:g3236128; PIDN:BAA29256.1; !1PID:g3256573 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0187 CLASSIFICATION #superfamily conserved hypothetical protein MTH593 SUMMARY #length 251 #molecular-weight 28699 #checksum 6394 SEQUENCE /// ENTRY F69217 #type complete TITLE hypothetical protein MTH880 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F69217 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession F69217 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-67 ##label MTH !'##cross-references GB:AE000864; GB:AE000666; NID:g2621970; !1PIDN:AAB85378.1; PID:g2621974 !'##experimental_source strain Delta H GENETICS !$#gene MTH880 CLASSIFICATION #superfamily hypothetical protein MTH880 SUMMARY #length 67 #molecular-weight 7863 #checksum 1786 SEQUENCE /// ENTRY H69358 #type complete TITLE hypothetical protein AF0872 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H69358 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession H69358 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-64 ##label KLE !'##cross-references GB:AE001044; GB:AE000782; NID:g2689367; !1PIDN:AAB90380.1; PID:g2649741; TIGR:AF0872 CLASSIFICATION #superfamily hypothetical protein MTH880 SUMMARY #length 64 #molecular-weight 7503 #checksum 6879 SEQUENCE /// ENTRY H69283 #type complete TITLE conserved hypothetical protein AF0272 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H69283 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession H69283 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-143 ##label KLE !'##cross-references GB:AE001086; GB:AE000782; NID:g2689409; !1PIDN:AAB90960.1; PID:g2650364; TIGR:AF0272 CLASSIFICATION #superfamily conserved hypothetical protein AF0272 SUMMARY #length 143 #molecular-weight 15730 #checksum 1205 SEQUENCE /// ENTRY D69464 #type complete TITLE hypothetical protein AF1717 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69464 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession D69464 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-140 ##label KLE !'##cross-references GB:AE000985; GB:AE000782; NID:g2689308; !1PIDN:AAB89538.1; PID:g2648842; TIGR:AF1717 CLASSIFICATION #superfamily conserved hypothetical protein AF0272 SUMMARY #length 140 #molecular-weight 16316 #checksum 2386 SEQUENCE /// ENTRY F69319 #type complete TITLE conserved hypothetical protein AF0558 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F69319 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession F69319 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-137 ##label KLE !'##cross-references GB:AE001066; GB:AE000782; NID:g2689389; !1PIDN:AAB90688.1; PID:g2650072; TIGR:AF0558 CLASSIFICATION #superfamily conserved hypothetical protein AF0272 SUMMARY #length 137 #molecular-weight 15169 #checksum 7933 SEQUENCE /// ENTRY F69459 #type complete TITLE probable vtpJ-therm 1 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F69459 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession F69459 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-391 ##label KLE !'##cross-references GB:AE000987; GB:AE000782; NID:g2689310; !1PIDN:AAB89567.1; PID:g2648872; TIGR:AF1679 CLASSIFICATION #superfamily probable vtpJ-therm SUMMARY #length 391 #molecular-weight 44328 #checksum 8987 SEQUENCE /// ENTRY H69351 #type complete TITLE probable vtpJ-therm 2 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H69351 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession H69351 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-418 ##label KLE !'##cross-references GB:AE001048; GB:AE000782; NID:g2689371; !1PIDN:AAB90426.1; PID:g2649793; TIGR:AF0816 CLASSIFICATION #superfamily probable vtpJ-therm SUMMARY #length 418 #molecular-weight 47424 #checksum 5374 SEQUENCE /// ENTRY F69463 #type complete TITLE conserved hypothetical protein AF1711 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F69463 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession F69463 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-147 ##label KLE !'##cross-references GB:AE000985; GB:AE000782; NID:g2689308; !1PIDN:AAB89534.1; PID:g2648838; TIGR:AF1711 CLASSIFICATION #superfamily Archaeoglobus fulgidus conserved hypothetical !1protein AF1711 SUMMARY #length 147 #molecular-weight 16770 #checksum 507 SEQUENCE /// ENTRY H69385 #type complete TITLE hypothetical protein AF1089 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H69385 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession H69385 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-141 ##label KLE !'##cross-references GB:AE001028; GB:AE000782; NID:g2689351; !1PIDN:AAB90162.1; PID:g2649509; TIGR:AF1089 CLASSIFICATION #superfamily Archaeoglobus fulgidus conserved hypothetical !1protein AF1711 SUMMARY #length 141 #molecular-weight 16218 #checksum 8131 SEQUENCE /// ENTRY F69513 #type complete TITLE conserved hypothetical protein AF2110 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F69513 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession F69513 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-241 ##label KLE !'##cross-references GB:AE000958; GB:AE000782; NID:g2689281; !1PIDN:AAB89147.1; PID:g2648424; TIGR:AF2110 CLASSIFICATION #superfamily Archaeoglobus fulgidus conserved hypothetical !1protein AF2110 SUMMARY #length 241 #molecular-weight 27613 #checksum 1875 SEQUENCE /// ENTRY C69934 #type complete TITLE conserved hypothetical protein ypdP - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69934 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69934 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-229 ##label KUN !'##cross-references GB:Z99115; GB:AL009126; NID:g2634478; !1PIDN:CAB14116.1; PID:g2634618 !'##experimental_source strain 168 GENETICS !$#gene ypdP CLASSIFICATION #superfamily Archaeoglobus fulgidus conserved hypothetical !1protein AF2110 SUMMARY #length 229 #molecular-weight 25671 #checksum 6827 SEQUENCE /// ENTRY B70106 #type complete TITLE conserved hypothetical integral membrane protein BB0050 - Lyme disease spirochete ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B70106 REFERENCE A70100 !$#authors Fraser, C.M.; Casjens, S.; Huang, W.M.; Sutton, G.G.; !1Clayton, R.; Lathigra, R.; White, O.; Ketchum, K.A.; Dodson, !1R.; Hickey, E.K.; Gwinn, M.; Dougherty, B.; Tomb, J.F.; !1Fleischmann, R.D.; Richardson, D.; Peterson, J.; Kerlavage, !1A.R.; Quackenbush, J.; Salzberg, S.; Hanson, M.; Vugt, R.V.; !1Palmer, N.; Adams, M.D.; Gocayne, J.; Weidman, J.; !1Utterback, T.; Watthey, L.; McDonald, L.; Artiach, P.; !1Bowman, C.; Garland, S.; Fujii, C.; Cotton, M.D.; Horst, K.; !1Roberts, K.; Hatch, B.; Smith, H.O.; Venter, J.C. !$#journal Nature (1997) 390:580-586 !$#title Genomic sequence of a Lyme disease spirochaete, Borrelia !1burgdorferi. !$#cross-references MUID:98065943; PMID:9403685 !$#accession B70106 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-224 ##label KLE !'##cross-references GB:AE001118; GB:AE000783; NID:g2687921; !1PIDN:AAC66433.1; PID:g2687925; TIGR:BB0050 !'##experimental_source strain B31 CLASSIFICATION #superfamily Archaeoglobus fulgidus conserved hypothetical !1protein AF2110 SUMMARY #length 224 #molecular-weight 25450 #checksum 7340 SEQUENCE /// ENTRY C70106 #type complete TITLE conserved hypothetical integral membrane protein BB0051 - Lyme disease spirochete ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C70106 REFERENCE A70100 !$#authors Fraser, C.M.; Casjens, S.; Huang, W.M.; Sutton, G.G.; !1Clayton, R.; Lathigra, R.; White, O.; Ketchum, K.A.; Dodson, !1R.; Hickey, E.K.; Gwinn, M.; Dougherty, B.; Tomb, J.F.; !1Fleischmann, R.D.; Richardson, D.; Peterson, J.; Kerlavage, !1A.R.; Quackenbush, J.; Salzberg, S.; Hanson, M.; Vugt, R.V.; !1Palmer, N.; Adams, M.D.; Gocayne, J.; Weidman, J.; !1Utterback, T.; Watthey, L.; McDonald, L.; Artiach, P.; !1Bowman, C.; Garland, S.; Fujii, C.; Cotton, M.D.; Horst, K.; !1Roberts, K.; Hatch, B.; Smith, H.O.; Venter, J.C. !$#journal Nature (1997) 390:580-586 !$#title Genomic sequence of a Lyme disease spirochaete, Borrelia !1burgdorferi. !$#cross-references MUID:98065943; PMID:9403685 !$#accession C70106 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-233 ##label KLE !'##cross-references GB:AE001118; GB:AE000783; NID:g2687921; !1PIDN:AAC66432.1; PID:g2687924; TIGR:BB0051 !'##experimental_source strain B31 CLASSIFICATION #superfamily Archaeoglobus fulgidus conserved hypothetical !1protein AF2110 SUMMARY #length 233 #molecular-weight 26882 #checksum 8060 SEQUENCE /// ENTRY D69372 #type complete TITLE osmoprotection protein (proW-2) homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69372 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession D69372 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-218 ##label KLE !'##cross-references GB:AE001036; GB:AE000782; NID:g2689359; !1PIDN:AAB90261.1; PID:g2649616; TIGR:AF0980 CLASSIFICATION #superfamily glycine betaine/carnitine/choline ABC !1transporter SUMMARY #length 218 #molecular-weight 23722 #checksum 5230 SEQUENCE /// ENTRY G64980 #type complete TITLE hypothetical 25.5 kD protein in molR-bglX intergenic region - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS G64980 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64980 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-243 ##label BLAT !'##cross-references GB:AE000302; GB:U00096; NID:g1788447; !1PIDN:AAC75189.1; PID:g1788449; UWGP:b2128 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yehW CLASSIFICATION #superfamily glycine betaine/carnitine/choline ABC !1transporter SUMMARY #length 243 #molecular-weight 25514 #checksum 9011 SEQUENCE /// ENTRY A70118 #type complete TITLE glycine betaine, L-proline ABC transporter, permease protein (proW) homolog - Lyme disease spirochete ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A70118 REFERENCE A70100 !$#authors Fraser, C.M.; Casjens, S.; Huang, W.M.; Sutton, G.G.; !1Clayton, R.; Lathigra, R.; White, O.; Ketchum, K.A.; Dodson, !1R.; Hickey, E.K.; Gwinn, M.; Dougherty, B.; Tomb, J.F.; !1Fleischmann, R.D.; Richardson, D.; Peterson, J.; Kerlavage, !1A.R.; Quackenbush, J.; Salzberg, S.; Hanson, M.; Vugt, R.V.; !1Palmer, N.; Adams, M.D.; Gocayne, J.; Weidman, J.; !1Utterback, T.; Watthey, L.; McDonald, L.; Artiach, P.; !1Bowman, C.; Garland, S.; Fujii, C.; Cotton, M.D.; Horst, K.; !1Roberts, K.; Hatch, B.; Smith, H.O.; Venter, J.C. !$#journal Nature (1997) 390:580-586 !$#title Genomic sequence of a Lyme disease spirochaete, Borrelia !1burgdorferi. !$#cross-references MUID:98065943; PMID:9403685 !$#accession A70118 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-299 ##label KLE !'##cross-references GB:AE001125; GB:AE000783; NID:g2688021; !1PIDN:AAC66524.1; PID:g2688023; TIGR:BB0145 !'##experimental_source strain B31 CLASSIFICATION #superfamily glycine betaine/carnitine/choline ABC !1transporter SUMMARY #length 299 #molecular-weight 33734 #checksum 6242 SEQUENCE /// ENTRY I40536 #type complete TITLE glycine betaine ABC transporter (permease) opuAB - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS I40536; E69669 REFERENCE A57322 !$#authors Kempf, B.; Bremer, E. !$#journal J. Biol. Chem. (1995) 270:16701-16713 !$#title OpuA, an osmotically regulated binding protein-dependent !1transport system for the osmoprotectant glycine betaine in !1Bacillus subtilis. !$#cross-references MUID:95348093; PMID:7622480 !$#accession I40536 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-282 ##label RES !'##cross-references EMBL:U17292; NID:g984802; PIDN:AAC43456.1; !1PID:g984804 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69669 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-282 ##label KUN !'##cross-references GB:Z99105; GB:AL009126; NID:g2632457; !1PIDN:CAB12093.1; PID:g2632585 !'##experimental_source strain 168 GENETICS !$#gene opuAB CLASSIFICATION #superfamily glycine betaine/carnitine/choline ABC !1transporter SUMMARY #length 282 #molecular-weight 30247 #checksum 8879 SEQUENCE /// ENTRY MMECPW #type complete TITLE glycine betaine/L-proline transport system permease protein P - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1989 #sequence_revision 31-Dec-1989 #text_change 01-Mar-2002 ACCESSIONS JS0129; G65047 REFERENCE JS0128 !$#authors Gowrishankar, J. !$#journal J. Bacteriol. (1989) 171:1923-1931 !$#title Nucleotide sequence of the osmoregulatory proU operon of !1Escherichia coli. !$#cross-references MUID:89197759; PMID:2649479 !$#accession JS0129 !'##molecule_type DNA !'##residues 1-354 ##label GOW !'##cross-references GB:M24856; NID:g147372; PIDN:AAA24428.1; !1PID:g147374 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65047 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-354 ##label BLAT !'##cross-references GB:AE000352; GB:U00096; NID:g1789024; !1PIDN:AAC75725.1; PID:g1789033; UWGP:b2678 !'##experimental_source strain K-12, substrain MG1655 COMMENT This membrane protein is one of the three components of the !1transport system for glycine betaine and L-proline. It is !1similar to other integral membrane components of binding !1protein-dependent transport systems. GENETICS !$#gene proW CLASSIFICATION #superfamily glycine betaine/carnitine/choline ABC !1transporter KEYWORDS binding protein-dependent transport system; membrane protein SUMMARY #length 354 #molecular-weight 37619 #checksum 5571 SEQUENCE /// ENTRY C69372 #type complete TITLE osmoprotection protein (proW-1) homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69372 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession C69372 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-204 ##label KLE !'##cross-references GB:AE001036; GB:AE000782; NID:g2689359; !1PIDN:AAB90262.1; PID:g2649617; TIGR:AF0979 CLASSIFICATION #superfamily glycine betaine/carnitine/choline ABC !1transporter SUMMARY #length 204 #molecular-weight 21461 #checksum 6536 SEQUENCE /// ENTRY I40516 #type complete TITLE spaF protein - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS I40516 REFERENCE I40511 !$#authors Klein, C.; Entian, K.D. !$#journal Appl. Environ. Microbiol. (1994) 60:2793-2801 !$#title Genes involved in self-protection against the lantibiotic !1subtilin produced by Bacillus subtilis ATCC 6633. !$#cross-references MUID:94368094; PMID:8085823 !$#accession I40516 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-456 ##label RES !'##cross-references EMBL:U09819; NID:g595315; PID:g595321 GENETICS !$#gene spaF CLASSIFICATION #superfamily Bacillus subtilis spaF protein; ATP-binding !1cassette homology KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$30-214 #domain ATP-binding cassette homology #label ABC\ !$47-54 #region nucleotide-binding motif A (P-loop) SUMMARY #length 456 #molecular-weight 51231 #checksum 5241 SEQUENCE /// ENTRY E69652 #type complete TITLE lincomycin-resistance protein lmrB - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69652 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69652 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-479 ##label KUN !'##cross-references GB:Z99105; GB:AL009126; NID:g2632457; !1PIDN:CAB12061.1; PID:g2632553 !'##experimental_source strain 168 GENETICS !$#gene lmrB CLASSIFICATION #superfamily lincomycin-resistance protein lmrB SUMMARY #length 479 #molecular-weight 51708 #checksum 7218 SEQUENCE /// ENTRY E69821 #type complete TITLE multidrug resistance protein homolog yhcA - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69821 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69821 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-532 ##label KUN !'##cross-references GB:Z99108; GB:AL009126; NID:g2633055; !1PIDN:CAB12729.1; PID:g2633224 !'##experimental_source strain 168 GENETICS !$#gene yhcA CLASSIFICATION #superfamily lincomycin-resistance protein lmrB SUMMARY #length 532 #molecular-weight 58341 #checksum 1148 SEQUENCE /// ENTRY F69763 #type complete TITLE multidrug resistance protein homolog ycnB - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F69763 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69763 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-472 ##label KUN !'##cross-references GB:Z99106; GB:AL009126; NID:g2632653; !1PIDN:CAB12192.1; PID:g2632685 !'##experimental_source strain 168 GENETICS !$#gene ycnB CLASSIFICATION #superfamily lincomycin-resistance protein lmrB SUMMARY #length 472 #molecular-weight 50797 #checksum 5272 SEQUENCE /// ENTRY B69532 #type complete TITLE multidrug resistance protein homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69532 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession B69532 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-503 ##label KLE !'##cross-references GB:AE000948; GB:AE000782; NID:g2689271; !1PIDN:AAB88991.1; PID:g2648258; TIGR:AF2258 CLASSIFICATION #superfamily lincomycin-resistance protein lmrB SUMMARY #length 503 #molecular-weight 55068 #checksum 6423 SEQUENCE /// ENTRY E70391 #type complete TITLE major facilitator family transporter - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E70391 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession E70391 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-511 ##label AQF !'##cross-references GB:AE000721; GB:AE000657; NID:g2983544; !1PIDN:AAC07127.1; PID:g2983553 !'##experimental_source strain VF5 GENETICS !$#gene emrB CLASSIFICATION #superfamily lincomycin-resistance protein lmrB SUMMARY #length 511 #molecular-weight 58153 #checksum 7206 SEQUENCE /// ENTRY F70705 #type complete TITLE hypothetical protein Rv2333c - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F70705 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession F70705 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-537 ##label COL !'##cross-references GB:Z79702; GB:AL123456; NID:g3261642; !1PIDN:CAB02058.1; PID:g1524267 !'##experimental_source strain H37Rv GENETICS !$#gene Rv2333c CLASSIFICATION #superfamily lincomycin-resistance protein lmrB SUMMARY #length 537 #molecular-weight 57115 #checksum 7481 SEQUENCE /// ENTRY C69221 #type complete TITLE hypothetical protein MTH906 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69221 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession C69221 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-140 ##label MTH !'##cross-references GB:AE000866; GB:AE000666; NID:g2621998; !1PIDN:AAB85404.1; PID:g2622002 !'##experimental_source strain Delta H GENETICS !$#gene MTH906 !$#start_codon GTG CLASSIFICATION #superfamily Methanobacterium hypothetical protein MTH906 SUMMARY #length 140 #molecular-weight 16097 #checksum 2447 SEQUENCE /// ENTRY E69476 #type complete TITLE hypothetical protein AF1814 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69476 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession E69476 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-118 ##label KLE !'##cross-references GB:AE000977; GB:AE000782; NID:g2689300; !1PIDN:AAB89439.1; PID:g2648735; TIGR:AF1814 CLASSIFICATION #superfamily Methanobacterium hypothetical protein MTH906 SUMMARY #length 118 #molecular-weight 13689 #checksum 1238 SEQUENCE /// ENTRY G70406 #type complete TITLE siroheme synthase - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G70406 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession G70406 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-187 ##label AQF !'##cross-references GB:AE000730; GB:AE000657; NID:g2983674; !1PIDN:AAC07241.1; PID:g2983676 !'##experimental_source strain VF5 GENETICS !$#gene cysG CLASSIFICATION #superfamily Aquifex aeolicus siroheme synthase SUMMARY #length 187 #molecular-weight 21652 #checksum 4376 SEQUENCE /// ENTRY F69877 #type complete TITLE uroporphyrin-III C-methyltransferase homolog ylnF - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F69877 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69877 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-162 ##label KUN !'##cross-references GB:Z99112; GB:AL009126; NID:g2633902; !1PIDN:CAB13437.1; PID:g2633936 !'##experimental_source strain 168 GENETICS !$#gene ylnF CLASSIFICATION #superfamily Aquifex aeolicus siroheme synthase SUMMARY #length 162 #molecular-weight 18004 #checksum 618 SEQUENCE /// ENTRY E64317 #type complete TITLE hypothetical protein MJ0140 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E64317 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession E64317 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-206 ##label BUL !'##cross-references GB:U67471; GB:L77117; NID:g2826249; !1PIDN:AAB98123.1; PID:g1590903; TIGR:MJ0140 GENETICS !$#map_position FOR138922-139542 !$#start_codon TTG CLASSIFICATION #superfamily Aquifex aeolicus siroheme synthase SUMMARY #length 206 #molecular-weight 23989 #checksum 2533 SEQUENCE /// ENTRY G69448 #type complete TITLE conserved hypothetical protein AF1592 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69448 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession G69448 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-251 ##label KLE !'##cross-references GB:AE000992; GB:AE000782; NID:g2689315; !1PIDN:AAB89653.1; PID:g2648964; TIGR:AF1592 CLASSIFICATION #superfamily Aquifex aeolicus siroheme synthase SUMMARY #length 251 #molecular-weight 28276 #checksum 9591 SEQUENCE /// ENTRY F69951 #type complete TITLE conserved hypothetical protein yqeJ - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F69951 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69951 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-189 ##label KUN !'##cross-references GB:Z99117; GB:AL009126; NID:g2634966; !1PIDN:CAB14506.1; PID:g2635010 !'##experimental_source strain 168 GENETICS !$#gene yqeJ CLASSIFICATION #superfamily Bacillus subtilis conserved hypothetical !1protein yqeJ SUMMARY #length 189 #molecular-weight 22156 #checksum 3022 SEQUENCE /// ENTRY H70685 #type complete TITLE hypothetical protein Rv2421c - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H70685 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession H70685 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-211 ##label COL !'##cross-references GB:Z81368; GB:AL123456; NID:g3261656; !1PIDN:CAB03753.1; PID:g3261661 !'##experimental_source strain H37Rv GENETICS !$#gene Rv2421c CLASSIFICATION #superfamily Bacillus subtilis conserved hypothetical !1protein yqeJ SUMMARY #length 211 #molecular-weight 23053 #checksum 9377 SEQUENCE /// ENTRY B71286 #type complete TITLE conserved hypothetical protein TP0741 - syphilis spirochete ORGANISM #formal_name Treponema pallidum subsp. pallidum #common_name syphilis spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS B71286 REFERENCE A71250 !$#authors Fraser, C.M.; Norris, S.J.; Weinstock, G.M.; White, O.; !1Sutton, G.G.; Dodson, R.; Gwinn, M.; Hickey, E.K.; Clayton, !1R.; Ketchum, K.A.; Sodergren, E.; Hardham, J.M.; McLeod, !1M.P.; Salzberg, S.; Peterson, J.; Khalak, H.; Richardson, !1D.; Howell, J.K.; Chidambaram, M.; Utterback, T.; McDonald, !1L.; Artiach, P.; Bowman, C.; Cotton, M.D.; Fujii, C.; !1Garland, S.; Hatch, B.; Horst, K.; Roberts, K.; Watthey, L.; !1Weidman, J.; Smith, H.O.; Venter, J.C. !$#journal Science (1998) 281:375-388 !$#title Complete genome sequence of Treponema pallidum, the syphilis !1spirochete. !$#cross-references MUID:98332770; PMID:9665876 !$#accession B71286 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-204 ##label COL !'##cross-references GB:AE001246; GB:AE000520; NID:g3323046; !1PIDN:AAC65710.1; PID:g3323048 !'##experimental_source strain Nichols GENETICS !$#gene TP0741 CLASSIFICATION #superfamily Bacillus subtilis conserved hypothetical !1protein yqeJ SUMMARY #length 204 #molecular-weight 22650 #checksum 2587 SEQUENCE /// ENTRY E64798 #type complete TITLE Nicotinate-nucleotide adenylyltransferase (EC 2.7.7.18) [similarity] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS E64798 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64798 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-213 ##label BLAT !'##cross-references GB:AE000168; GB:U00096; NID:g1786849; !1PIDN:AAC73740.1; PID:g1786858; UWGP:b0639 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily Bacillus subtilis conserved hypothetical !1protein yqeJ KEYWORDS nucleotidyltransferase SUMMARY #length 213 #molecular-weight 24528 #checksum 643 SEQUENCE /// ENTRY A70303 #type complete TITLE conserved hypothetical protein aq_036 - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A70303 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession A70303 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-168 ##label AQF !'##cross-references GB:AE000670; GB:AE000657; NID:g2982779; !1PIDN:AAC06417.1; PID:g2982792 !'##experimental_source strain VF5 GENETICS !$#gene aq_036 CLASSIFICATION #superfamily Bacillus subtilis conserved hypothetical !1protein yqeJ SUMMARY #length 168 #molecular-weight 19998 #checksum 3843 SEQUENCE /// ENTRY E70197 #type complete TITLE conserved hypothetical protein BB0782 - Lyme disease spirochete ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E70197 REFERENCE A70100 !$#authors Fraser, C.M.; Casjens, S.; Huang, W.M.; Sutton, G.G.; !1Clayton, R.; Lathigra, R.; White, O.; Ketchum, K.A.; Dodson, !1R.; Hickey, E.K.; Gwinn, M.; Dougherty, B.; Tomb, J.F.; !1Fleischmann, R.D.; Richardson, D.; Peterson, J.; Kerlavage, !1A.R.; Quackenbush, J.; Salzberg, S.; Hanson, M.; Vugt, R.V.; !1Palmer, N.; Adams, M.D.; Gocayne, J.; Weidman, J.; !1Utterback, T.; Watthey, L.; McDonald, L.; Artiach, P.; !1Bowman, C.; Garland, S.; Fujii, C.; Cotton, M.D.; Horst, K.; !1Roberts, K.; Hatch, B.; Smith, H.O.; Venter, J.C. !$#journal Nature (1997) 390:580-586 !$#title Genomic sequence of a Lyme disease spirochaete, Borrelia !1burgdorferi. !$#cross-references MUID:98065943; PMID:9403685 !$#accession E70197 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-206 ##label KLE !'##cross-references GB:AE001177; GB:AE000783; NID:g2688711; !1PIDN:AAC67126.1; PID:g2688718; TIGR:BB0782 !'##experimental_source strain B31 CLASSIFICATION #superfamily Bacillus subtilis conserved hypothetical !1protein yqeJ SUMMARY #length 206 #molecular-weight 23768 #checksum 6340 SEQUENCE /// ENTRY C69224 #type complete TITLE cobalamin biosynthesis protein N - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69224 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession C69224 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-1668 ##label MTH !'##cross-references GB:AE000868; GB:AE000666; NID:g2622025; !1PIDN:AAB85426.1; PID:g2622026 !'##experimental_source strain Delta H GENETICS !$#gene MTH928 !$#start_codon GTG CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum cobalamin !1biosynthesis protein N SUMMARY #length 1668 #molecular-weight 184731 #checksum 6302 SEQUENCE /// ENTRY C69145 #type complete TITLE protoporphyrin IX magnesium chelatase (EC 4.99.1.-) - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69145 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession C69145 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-1561 ##label MTH !'##cross-references GB:AE000820; GB:AE000666; NID:g2621405; !1PIDN:AAB84857.1; PID:g2621409 !'##experimental_source strain Delta H GENETICS !$#gene MTH351 CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum cobalamin !1biosynthesis protein N KEYWORDS lyase SUMMARY #length 1561 #molecular-weight 170574 #checksum 5607 SEQUENCE /// ENTRY S76868 #type complete TITLE hypothetical protein - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S76868 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76868 !'##status preliminary !'##molecule_type DNA !'##residues 1-152 ##label KAN !'##cross-references EMBL:D90917; GB:AB001339; NID:g1653836; !1PIDN:BAA18780.1; PID:g1653870 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily Haemophilus influenzae conserved hypothetical !1protein HI0305 SUMMARY #length 152 #molecular-weight 16944 #checksum 8408 SEQUENCE /// ENTRY D69979 #type complete TITLE conserved hypothetical protein yrrK - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS D69979 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D69979 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-138 ##label KUN !'##cross-references GB:Z99117; GB:Z99118; GB:AL009126; NID:g2635200; !1PID:g2635203; NID:g2634966; PID:g2635185 !'##experimental_source strain 168 GENETICS !$#gene yrrK CLASSIFICATION #superfamily Haemophilus influenzae conserved hypothetical !1protein HI0305 SUMMARY #length 138 #molecular-weight 15210 #checksum 3936 SEQUENCE /// ENTRY F70660 #type complete TITLE hypothetical protein Rv2554c - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F70660 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession F70660 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-170 ##label COL !'##cross-references GB:Z83863; GB:AL123456; NID:g3261685; !1PIDN:CAB06184.1; PID:g1781048 !'##experimental_source strain H37Rv GENETICS !$#gene Rv2554c CLASSIFICATION #superfamily Haemophilus influenzae conserved hypothetical !1protein HI0305 SUMMARY #length 170 #molecular-weight 18065 #checksum 8769 SEQUENCE /// ENTRY D71689 #type complete TITLE hypothetical protein RP330 - Rickettsia prowazekii ORGANISM #formal_name Rickettsia prowazekii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Nov-2000 ACCESSIONS D71689 REFERENCE A71630 !$#authors Andersson, S.G.E.; Zomorodipour, A.; Andersson, J.O.; !1Sicheritz-Ponten, T.; Alsmark, U.C.M.; Podowski, R.M.; !1Naeslund, A.K.; Eriksson, A.S.; Winkler, H.H.; Kurland, C.G. !$#journal Nature (1998) 396:133-140 !$#title The genome sequence of Rickettsia prowazekii and the origin !1of mitochondria. !$#cross-references MUID:99039499; PMID:9823893 !$#accession D71689 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-156 ##label AND !'##cross-references GB:AJ235271; GB:AJ235269; NID:g3868717; !1PIDN:CAA14790.1; PID:g3860890; GSPDB:GN00081 !'##experimental_source strain Madrid E GENETICS !$#gene RP330 CLASSIFICATION #superfamily Haemophilus influenzae conserved hypothetical !1protein HI0305 SUMMARY #length 156 #molecular-weight 17435 #checksum 1652 SEQUENCE /// ENTRY C70430 #type complete TITLE conserved hypothetical protein aq_1498 - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C70430 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession C70430 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-131 ##label AQF !'##cross-references GB:AE000743; GB:AE000657; NID:g2983875; !1PIDN:AAC07442.1; PID:g2983890 !'##experimental_source strain VF5 GENETICS !$#gene aq_1498 CLASSIFICATION #superfamily Haemophilus influenzae conserved hypothetical !1protein HI0305 SUMMARY #length 131 #molecular-weight 14697 #checksum 3993 SEQUENCE /// ENTRY D65080 #type complete TITLE hypothetical protein b2949 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS D65080 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65080 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-138 ##label BLAT !'##cross-references GB:AE000377; GB:U00096; NID:g2367178; !1PIDN:AAC75986.1; PID:g1789318; UWGP:b2949 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily Haemophilus influenzae conserved hypothetical !1protein HI0305 SUMMARY #length 138 #molecular-weight 15186 #checksum 3472 SEQUENCE /// ENTRY H64005 #type complete TITLE conserved hypothetical protein HI0305 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS H64005 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession H64005 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-139 ##label TIGR !'##cross-references GB:U32716; GB:L42023; NID:g1573268; !1PIDN:AAC21970.1; PID:g1573274; TIGR:HI0305 CLASSIFICATION #superfamily Haemophilus influenzae conserved hypothetical !1protein HI0305 SUMMARY #length 139 #molecular-weight 15339 #checksum 3388 SEQUENCE /// ENTRY H64006 #type complete TITLE hypothetical protein HI0388 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS H64006 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession H64006 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-236 ##label TIGR !'##cross-references GB:U32722; GB:L42023; NID:g1573348; !1PIDN:AAC22046.1; PID:g1573358; TIGR:HI0388 CLASSIFICATION #superfamily hypothetical protein HI0388 SUMMARY #length 236 #molecular-weight 26083 #checksum 2813 SEQUENCE /// ENTRY G64941 #type complete TITLE hypothetical protein b1807 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS G64941 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64941 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-231 ##label BLAT !'##cross-references GB:AE000275; GB:U00096; NID:g1788106; !1PIDN:AAC74877.1; PID:g1788109; UWGP:b1807 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily hypothetical protein HI0388 SUMMARY #length 231 #molecular-weight 25181 #checksum 5891 SEQUENCE /// ENTRY B70738 #type complete TITLE hypothetical protein Rv3421c - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B70738 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession B70738 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-211 ##label COL !'##cross-references GB:Z77165; GB:AL123456; NID:g3261609; !1PIDN:CAB01035.1; PID:g1449366 !'##experimental_source strain H37Rv GENETICS !$#gene Rv3421c CLASSIFICATION #superfamily hypothetical protein HI0388 SUMMARY #length 211 #molecular-weight 21572 #checksum 1685 SEQUENCE /// ENTRY H64014 #type complete TITLE hypothetical protein HI0857 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS H64014 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession H64014 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-100 ##label TIGR !'##cross-references GB:U32767; GB:L42023; NID:g1573868; !1PIDN:AAC22516.1; PID:g1573872; TIGR:HI0857 CLASSIFICATION #superfamily hypothetical protein HI0857 SUMMARY #length 100 #molecular-weight 11422 #checksum 9075 SEQUENCE /// ENTRY F65075 #type complete TITLE hypothetical 12.7 kD protein in pepP-ssr intergenic region - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS F65075 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65075 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-109 ##label BLAT !'##cross-references GB:AE000374; GB:U00096; NID:g1789270; !1PIDN:AAC75948.1; PID:g1789277; UWGP:b2910 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ygfE CLASSIFICATION #superfamily hypothetical protein HI0857 SUMMARY #length 109 #molecular-weight 12594 #checksum 912 SEQUENCE /// ENTRY H64056 #type complete TITLE protein-export protein secF homolog - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS H64056 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession H64056 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-325 ##label TIGR !'##cross-references GB:U32710; GB:L42023; NID:g1573200; !1PIDN:AAC21907.1; PID:g1573204; TIGR:HI0239 CLASSIFICATION #superfamily Escherichia coli preprotein translocase chain !1secF SUMMARY #length 325 #molecular-weight 36051 #checksum 5310 SEQUENCE /// ENTRY JQ0697 #type complete TITLE preprotein translocase chain secF [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES protein-export membrane protein secF; secretion protein secF ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS JQ0697; S12302; A64770 REFERENCE JQ0693 !$#authors Gardel, C.; Johnson, K.; Jacq, A.; Beckwith, J. !$#journal EMBO J. (1990) 9:3209-3216 !$#title The secD locus of E.coli codes for two membrane proteins !1required for protein export. !$#cross-references MUID:91006014; PMID:2170107 !$#accession JQ0697 !'##molecule_type DNA !'##residues 1-323 ##label GAR !'##cross-references GB:X56175; NID:g42929; PIDN:CAA39635.1; PID:g581231 !'##experimental_source strain K-12 REFERENCE S12298 !$#authors Gardel, C.; Johnson, K.; Jacq, A.; Beckwith, J. !$#journal EMBO J. (1990) 9:4205-4206 !$#cross-references MUID:91065354; PMID:2249673 !$#contents erratum !$#accession S12302 !'##molecule_type DNA !'##residues 1-323 ##label GA2 !'##cross-references EMBL:X56175; NID:g42929; PID:g581231 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A64770 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-323 ##label BLAT !'##cross-references GB:AE000147; GB:U00096; NID:g1786603; !1PIDN:AAC73512.1; PID:g1786610; UWGP:b0409 !'##experimental_source strain K-12, substrain MG1655 COMMENT Preprotein translocase contains a membrane-embedded trimeric !1complex of SecY, SecE and SecG and the peripheral SecA !1protein. The proteins SecD, SecF and YajC also form an !1integral membrane heterotrimeric complex. These two trimeric !1complexes are associated to form SecYEGDFyajC, the hexameric !1integral membrane domain of the pre- protein translocase !1'holoenzyme'. GENETICS !$#gene secF !$#start_codon GTG COMPLEX heterohexamer; chains secY (PIR:QQECSY), secE (PIR:VXECSE), !1secG (PIR:S40402), secD (PIR:H64769), secF (PIR:JQ0697), and !1yajC (PIR:B64735) FUNCTION !$#description the secD protein is a transmembrane component of the protein !1export complex [validated, MUID:91006014] CLASSIFICATION #superfamily Escherichia coli preprotein translocase chain !1secF KEYWORDS inner membrane; protein export; transmembrane protein FEATURE !$27-43 #domain transmembrane #status predicted #label TM1\ !$147-163 #domain transmembrane #status predicted #label TM2\ !$172-188 #domain transmembrane #status predicted #label TM3\ !$195-211 #domain transmembrane #status predicted #label TM4\ !$249-265 #domain transmembrane #status predicted #label TM5\ !$275-291 #domain transmembrane #status predicted #label TM6 SUMMARY #length 323 #molecular-weight 35382 #checksum 6904 SEQUENCE /// ENTRY F70438 #type complete TITLE protein-export membrane protein - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F70438 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession F70438 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-288 ##label AQF !'##cross-references GB:AE000747; GB:AE000657; NID:g2983944; !1PIDN:AAC07496.1; PID:g2983948 !'##experimental_source strain VF5 GENETICS !$#gene secF CLASSIFICATION #superfamily Escherichia coli preprotein translocase chain !1secF SUMMARY #length 288 #molecular-weight 31632 #checksum 2190 SEQUENCE /// ENTRY H71720 #type complete TITLE protein-export membrane protein secF (secF) RP114 - Rickettsia prowazekii ORGANISM #formal_name Rickettsia prowazekii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Nov-2000 ACCESSIONS H71720 REFERENCE A71630 !$#authors Andersson, S.G.E.; Zomorodipour, A.; Andersson, J.O.; !1Sicheritz-Ponten, T.; Alsmark, U.C.M.; Podowski, R.M.; !1Naeslund, A.K.; Eriksson, A.S.; Winkler, H.H.; Kurland, C.G. !$#journal Nature (1998) 396:133-140 !$#title The genome sequence of Rickettsia prowazekii and the origin !1of mitochondria. !$#cross-references MUID:99039499; PMID:9823893 !$#accession H71720 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-311 ##label AND !'##cross-references GB:AJ235270; GB:AJ235269; NID:g3860572; !1PIDN:CAA14583.1; PID:g3860682; GSPDB:GN00081 !'##experimental_source strain Madrid E GENETICS !$#gene secF; RP114 CLASSIFICATION #superfamily Escherichia coli preprotein translocase chain !1secF SUMMARY #length 311 #molecular-weight 35175 #checksum 6780 SEQUENCE /// ENTRY E64713 #type complete TITLE protein-export membrane protein - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS E64713 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession E64713 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-323 ##label TOM !'##cross-references GB:AE000652; GB:AE000511; NID:g2314720; !1PIDN:AAD08587.1; PID:g2314729; TIGR:HP1549 CLASSIFICATION #superfamily Escherichia coli preprotein translocase chain !1secF SUMMARY #length 323 #molecular-weight 36276 #checksum 4871 SEQUENCE /// ENTRY D70181 #type complete TITLE protein-export membrane protein (secF) homolog - Lyme disease spirochete ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D70181 REFERENCE A70100 !$#authors Fraser, C.M.; Casjens, S.; Huang, W.M.; Sutton, G.G.; !1Clayton, R.; Lathigra, R.; White, O.; Ketchum, K.A.; Dodson, !1R.; Hickey, E.K.; Gwinn, M.; Dougherty, B.; Tomb, J.F.; !1Fleischmann, R.D.; Richardson, D.; Peterson, J.; Kerlavage, !1A.R.; Quackenbush, J.; Salzberg, S.; Hanson, M.; Vugt, R.V.; !1Palmer, N.; Adams, M.D.; Gocayne, J.; Weidman, J.; !1Utterback, T.; Watthey, L.; McDonald, L.; Artiach, P.; !1Bowman, C.; Garland, S.; Fujii, C.; Cotton, M.D.; Horst, K.; !1Roberts, K.; Hatch, B.; Smith, H.O.; Venter, J.C. !$#journal Nature (1997) 390:580-586 !$#title Genomic sequence of a Lyme disease spirochaete, Borrelia !1burgdorferi. !$#cross-references MUID:98065943; PMID:9403685 !$#accession D70181 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-299 ##label KLE !'##cross-references GB:AE001166; GB:AE000783; NID:g2688571; !1PIDN:AAC66992.1; PID:g2688573; TIGR:BB0653 !'##experimental_source strain B31 CLASSIFICATION #superfamily Escherichia coli preprotein translocase chain !1secF SUMMARY #length 299 #molecular-weight 34057 #checksum 6199 SEQUENCE /// ENTRY H64068 #type complete TITLE protein-export protein secG - Haemophilus influenzae (strain Rd KW20) ALTERNATE_NAMES p12 protein; preprotein translocase ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS H64068 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession H64068 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-112 ##label TIGR !'##cross-references GB:U32727; GB:L42023; NID:g1573415; !1PIDN:AAC22104.1; PID:g1573421; TIGR:HI0445 GENETICS !$#gene secG FUNCTION !$#description involved in protein translocation across the cytoplasmic !1membrane CLASSIFICATION #superfamily protein-export protein secG KEYWORDS protein transport; transmembrane protein SUMMARY #length 112 #molecular-weight 11538 #checksum 9093 SEQUENCE /// ENTRY S40402 #type complete TITLE protein-export protein secG - Escherichia coli (strain K-12) ALTERNATE_NAMES p12 protein; preprotein translocase ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS S40402; A65108 REFERENCE S40402 !$#authors Nishiyama, K.; Mizushima, S.; Tokuda, H. !$#journal EMBO J. (1993) 12:3409-3415 !$#title A novel membrane protein involved in protein translocation !1across the cytoplasmic membrane of Escherichia coli. !$#cross-references MUID:94074540; PMID:8253068 !$#accession S40402 !'##status preliminary !'##molecule_type DNA !'##residues 1-110 ##label NIS !'##cross-references EMBL:D16463; NID:g414342; PIDN:BAA03930.1; !1PID:g431135 !'##experimental_source strain K12 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65108 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-110 ##label BLAT !'##cross-references GB:AE000398; GB:U00096; NID:g1789562; !1PIDN:AAC76207.1; PID:g1789565; UWGP:b3175 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene secG FUNCTION !$#description involved in protein translocation across the cytoplasmic !1membrane CLASSIFICATION #superfamily protein-export protein secG KEYWORDS inner membrane; protein transport; transmembrane protein SUMMARY #length 110 #molecular-weight 11365 #checksum 2971 SEQUENCE /// ENTRY F70309 #type complete TITLE protein export membrane protein SecG - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F70309 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession F70309 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-100 ##label AQF !'##cross-references GB:AE000673; GB:AE000657; NID:g2982834; !1PIDN:AAC06462.1; PID:g2982840 !'##experimental_source strain VF5 GENETICS !$#gene secG CLASSIFICATION #superfamily protein-export protein secG SUMMARY #length 100 #molecular-weight 10464 #checksum 9274 SEQUENCE /// ENTRY A70028 #type complete TITLE hypothetical protein yvaL - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A70028 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A70028 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-76 ##label KUN !'##cross-references GB:Z99121; GB:AL009126; NID:g2635827; !1PIDN:CAB15368.1; PID:g2635876 !'##experimental_source strain 168 GENETICS !$#gene yvaL CLASSIFICATION #superfamily protein-export protein secG SUMMARY #length 76 #molecular-weight 7996 #checksum 8138 SEQUENCE /// ENTRY F71716 #type complete TITLE protein-export membrane protein secG (secG) RP079 - Rickettsia prowazekii ORGANISM #formal_name Rickettsia prowazekii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Nov-2000 ACCESSIONS F71716 REFERENCE A71630 !$#authors Andersson, S.G.E.; Zomorodipour, A.; Andersson, J.O.; !1Sicheritz-Ponten, T.; Alsmark, U.C.M.; Podowski, R.M.; !1Naeslund, A.K.; Eriksson, A.S.; Winkler, H.H.; Kurland, C.G. !$#journal Nature (1998) 396:133-140 !$#title The genome sequence of Rickettsia prowazekii and the origin !1of mitochondria. !$#cross-references MUID:99039499; PMID:9823893 !$#accession F71716 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-100 ##label AND !'##cross-references GB:AJ235270; GB:AJ235269; NID:g3860572; !1PIDN:CAA14549.1; PID:g3860648; GSPDB:GN00081 !'##experimental_source strain Madrid E GENETICS !$#gene secG; RP079 CLASSIFICATION #superfamily protein-export protein secG SUMMARY #length 100 #molecular-weight 10656 #checksum 8096 SEQUENCE /// ENTRY H64130 #type complete TITLE glycosyl transferase homolog HI1578 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS H64130 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession H64130 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-323 ##label TIGR !'##cross-references GB:U32832; GB:L42023; NID:g1574421; !1PIDN:AAC23227.1; PID:g1574422; TIGR:HI1578 CLASSIFICATION #superfamily Neisseria meningitidis glycosyl transferase A SUMMARY #length 323 #molecular-weight 37680 #checksum 8773 SEQUENCE /// ENTRY S70813 #type complete TITLE glycosyl transferase A (EC 2.4.-.-) - Neisseria meningitidis ORGANISM #formal_name Neisseria meningitidis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S70813 REFERENCE S70812 !$#authors Jennings, M.P.; Hood, D.W.; Peak, I.R.A.; Virji, M.; Moxon, !1E.R. !$#journal Mol. Microbiol. (1995) 18:729-740 !$#title Molecular analysis of a locus for the biosynthesis and !1phase-variable expression of the lacto-N-neotetraose !1terminal lipopolysaccharide structure in Neisseria !1meningitidis. !$#cross-references MUID:96414473; PMID:8817494 !$#accession S70813 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-333 ##label JEN !'##cross-references EMBL:U25839; NID:g973183; PIDN:AAC44084.1; !1PID:g973185 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1995 GENETICS !$#gene lgtA !$#start_codon TTG CLASSIFICATION #superfamily Neisseria meningitidis glycosyl transferase A KEYWORDS glycosyltransferase SUMMARY #length 333 #molecular-weight 38562 #checksum 2027 SEQUENCE /// ENTRY E71690 #type complete TITLE minor teichoic acids biosynthesis protein ggab (ggaB) RP339 - Rickettsia prowazekii ORGANISM #formal_name Rickettsia prowazekii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Nov-2000 ACCESSIONS E71690 REFERENCE A71630 !$#authors Andersson, S.G.E.; Zomorodipour, A.; Andersson, J.O.; !1Sicheritz-Ponten, T.; Alsmark, U.C.M.; Podowski, R.M.; !1Naeslund, A.K.; Eriksson, A.S.; Winkler, H.H.; Kurland, C.G. !$#journal Nature (1998) 396:133-140 !$#title The genome sequence of Rickettsia prowazekii and the origin !1of mitochondria. !$#cross-references MUID:99039499; PMID:9823893 !$#accession E71690 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-318 ##label AND !'##cross-references GB:AJ235271; GB:AJ235269; NID:g3868717; !1PIDN:CAA14799.1; PID:g3860899; GSPDB:GN00081 !'##experimental_source strain Madrid E GENETICS !$#gene ggaB; RP339 CLASSIFICATION #superfamily Neisseria meningitidis glycosyl transferase A SUMMARY #length 318 #molecular-weight 36866 #checksum 1777 SEQUENCE /// ENTRY G71153 #type complete TITLE hypothetical protein PH0430 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G71153 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession G71153 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-334 ##label KAW !'##cross-references GB:AP000002; NID:g3236129; PIDN:BAA29516.1; !1PID:g3256833 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0430 CLASSIFICATION #superfamily Neisseria meningitidis glycosyl transferase A SUMMARY #length 334 #molecular-weight 38998 #checksum 8902 SEQUENCE /// ENTRY D69765 #type complete TITLE lactam utilization protein ycsF - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69765; I39894 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D69765 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-211 ##label KUN !'##cross-references GB:Z99106; GB:AL009126; NID:g2632653; !1PIDN:CAB12213.1; PID:g2632706 !'##experimental_source strain 168 REFERENCE I39887 !$#authors Ogasawara, N.; Fujita, Y.; Kobayashi, Y.; Sadaie, Y.; !1Tanaka, T.; Takahashi, H.; Yamane, K.; Yoshikawa, H. !$#journal Microbiology (1995) 141:257-259 !$#title Systematic sequencing of the Bacillus subtilis genome: !1progress report of the Japanese group. !$#cross-references MUID:95219077; PMID:7704252 !$#accession I39894 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 46-211 ##label RES !'##cross-references GB:D38161; NID:g1032472; PIDN:BAA07357.1; !1PID:g707083 GENETICS !$#gene ycsF CLASSIFICATION #superfamily Bacillus subtilis lactam utilization protein !1ycsF SUMMARY #length 211 #molecular-weight 22731 #checksum 4089 SEQUENCE /// ENTRY E71090 #type complete TITLE probable lactam utilization protein - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E71090 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession E71090 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-255 ##label KAW !'##cross-references GB:AP000004; NID:g3236131; PIDN:BAA30083.1; !1PID:g3257400 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0986 CLASSIFICATION #superfamily Bacillus subtilis lactam utilization protein !1ycsF SUMMARY #length 255 #molecular-weight 28430 #checksum 6058 SEQUENCE /// ENTRY H64806 #type complete TITLE ybgL protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS H64806 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64806 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-244 ##label BLAT !'##cross-references GB:AE000174; GB:U00096; NID:g1786920; !1PIDN:AAC73807.1; PID:g1786931; UWGP:b0713 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ybgL CLASSIFICATION #superfamily Bacillus subtilis lactam utilization protein !1ycsF SUMMARY #length 244 #molecular-weight 25800 #checksum 2715 SEQUENCE /// ENTRY H64138 #type complete TITLE lactam utilization protein homolog - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS H64138 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession H64138 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-257 ##label TIGR !'##cross-references GB:U32845; GB:L42023; NID:g3212236; !1PIDN:AAC23375.1; PID:g1574585; TIGR:HI1729 CLASSIFICATION #superfamily Bacillus subtilis lactam utilization protein !1ycsF SUMMARY #length 257 #molecular-weight 28225 #checksum 8314 SEQUENCE /// ENTRY B42064 #type complete TITLE lactam utilization protein lamB - Emericella nidulans ORGANISM #formal_name Emericella nidulans, Aspergillus nidulans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS B42064 REFERENCE A42064 !$#authors Richardson, I.B.; Katz, M.E.; Hynes, M.J. !$#journal Mol. Cell. Biol. (1992) 12:337-346 !$#title Molecular characterization of the lam locus and sequences !1involved in regulation by the amdR protein of Aspergillus !1nidulans. !$#cross-references MUID:92107186; PMID:1729609 !$#accession B42064 !'##status preliminary !'##molecule_type DNA !'##residues 1-262 ##label RIC !'##cross-references GB:M77283; NID:g168058; PIDN:AAA33313.1; !1PID:g168060 !'##note the authors translated the codon GGT for residue 121 as Met, !1and ATG for residue 122 as Gly CLASSIFICATION #superfamily Bacillus subtilis lactam utilization protein !1ycsF SUMMARY #length 262 #molecular-weight 29617 #checksum 350 SEQUENCE /// ENTRY A35851 #type complete TITLE nudC protein - Emericella nidulans ORGANISM #formal_name Emericella nidulans, Aspergillus nidulans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS A35851 REFERENCE A35851 !$#authors Osmani, A.H.; Osmani, S.A.; Morris, N.R. !$#journal J. Cell Biol. (1990) 111:543-551 !$#title The molecular cloning and identification of a gene product !1specifically required for nuclear movement in Aspergillus !1nidulans. !$#cross-references MUID:90338109; PMID:2199460 !$#accession A35851 !'##status preliminary !'##molecule_type DNA !'##residues 1-198 ##label OSM !'##cross-references GB:X52565; NID:g2366; PIDN:CAA36799.1; PID:g2367 CLASSIFICATION #superfamily Emericella nidulans nudC protein SUMMARY #length 198 #molecular-weight 22353 #checksum 7759 SEQUENCE /// ENTRY D64989 #type complete TITLE heme exporter protein D - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS D64989 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64989 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-69 ##label BLAT !'##cross-references GB:AE000309; GB:U00096; NID:g1788520; !1PIDN:AAC75258.1; PID:g1788526; UWGP:b2198 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ccmD CLASSIFICATION #superfamily heme export protein D SUMMARY #length 69 #molecular-weight 7745 #checksum 3665 SEQUENCE /// ENTRY H64166 #type complete TITLE heme export protein D homolog HI1092 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS H64166 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession H64166 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-67 ##label TIGR !'##cross-references GB:U32789; GB:L42023; NID:g1574642; !1PIDN:AAC22749.1; PID:g1574647; TIGR:HI1092 CLASSIFICATION #superfamily heme export protein D SUMMARY #length 67 #molecular-weight 7847 #checksum 3872 SEQUENCE /// ENTRY H64169 #type complete TITLE hypothetical protein HI1262 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS H64169 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession H64169 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-244 ##label TIGR !'##cross-references GB:U32806; GB:L42023; NID:g1574717; !1PIDN:AAC22915.1; PID:g1574720; TIGR:HI1262 !'##note best homolog was a hypothetical protein from Escherichia coli CLASSIFICATION #superfamily conserved hypothetical protein HI1262 SUMMARY #length 244 #molecular-weight 28188 #checksum 2836 SEQUENCE /// ENTRY G64982 #type complete TITLE sanA protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS G64982 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64982 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-239 ##label BLAT !'##cross-references GB:AE000303; GB:U00096; NID:g1788456; !1PIDN:AAC75205.1; PID:g1788466; UWGP:b2144 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene sanA CLASSIFICATION #superfamily conserved hypothetical protein HI1262 SUMMARY #length 239 #molecular-weight 27287 #checksum 1827 SEQUENCE /// ENTRY C65097 #type complete TITLE hypothetical 25.5 kD protein in ebgC-exuT intergenic region - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS C65097 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65097 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-230 ##label BLAT !'##cross-references GB:AE000390; GB:U00096; NID:g2367189; !1PIDN:AAC76121.1; PID:g1789468; UWGP:b3086 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ygjQ CLASSIFICATION #superfamily conserved hypothetical protein HI1262 SUMMARY #length 230 #molecular-weight 25480 #checksum 1227 SEQUENCE /// ENTRY C69307 #type complete TITLE conserved hypothetical protein AF0459 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69307 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession C69307 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-736 ##label KLE !'##cross-references GB:AE001073; GB:AE000782; NID:g2689396; !1PIDN:AAB90778.1; PID:g2650170; TIGR:AF0459 CLASSIFICATION #superfamily Archaeoglobus conserved hypothetical protein !1AF0459 SUMMARY #length 736 #molecular-weight 81942 #checksum 9679 SEQUENCE /// ENTRY D69403 #type complete TITLE conserved hypothetical protein AF1229 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69403 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession D69403 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-750 ##label KLE !'##cross-references GB:AE001019; GB:AE000782; NID:g2689342; !1PIDN:AAB90013.1; PID:g2649351; TIGR:AF1229 CLASSIFICATION #superfamily Archaeoglobus conserved hypothetical protein !1AF0459 SUMMARY #length 750 #molecular-weight 82015 #checksum 6472 SEQUENCE /// ENTRY H64170 #type complete TITLE hypothetical protein HI1314 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS H64170 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession H64170 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-161 ##label TIGR !'##cross-references GB:U32810; GB:L42023; NID:g1574760; !1PIDN:AAC22960.1; PID:g1574772; TIGR:HI1314 CLASSIFICATION #superfamily conserved hypothetical protein HI1314 SUMMARY #length 161 #molecular-weight 18388 #checksum 169 SEQUENCE /// ENTRY D64929 #type complete TITLE probable lipoprotein nlpC precursor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS D64929 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64929 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-154 ##label BLAT !'##cross-references GB:AE000266; GB:U00096; NID:g1787997; !1PIDN:AAC74778.1; PID:g1788001; UWGP:b1708 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene nlpC CLASSIFICATION #superfamily conserved hypothetical protein HI1314 KEYWORDS lipoprotein FEATURE !$1-14 #domain signal sequence #status predicted #label SIG\ !$15-154 #product probable lipoprotein nlpC #status predicted !8#label MAT SUMMARY #length 154 #molecular-weight 17283 #checksum 7756 SEQUENCE /// ENTRY F64986 #type complete TITLE probable lipoprotein [imported] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS F64986 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64986 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-188 ##label BLAT !'##cross-references GB:AE000307; GB:U00096; NID:g1788498; !1PIDN:AAC75236.1; PID:g1788501; UWGP:b2175 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily conserved hypothetical protein HI1314 SUMMARY #length 188 #molecular-weight 21040 #checksum 3124 SEQUENCE /// ENTRY H64173 #type complete TITLE hypothetical protein HI1652 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS H64173 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession H64173 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-183 ##label TIGR !'##cross-references GB:U32838; GB:L42023; NID:g1574497; !1PIDN:AAC23297.1; PID:g1574501; TIGR:HI1652 !'##note best homolog was a hypothetical protein from Escherichia coli CLASSIFICATION #superfamily conserved hypothetical protein HI1314 SUMMARY #length 183 #molecular-weight 20585 #checksum 6025 SEQUENCE /// ENTRY H64235 #type complete TITLE X-Pro aminopeptidase (EC 3.4.11.9) - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Feb-2002 ACCESSIONS H64235 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession H64235 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-354 ##label TIGR !'##cross-references GB:U39715; GB:L43967; NID:g1046026; PID:g1046027; !1TIGR:MG324 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily X-Pro aminopeptidase KEYWORDS aminopeptidase SUMMARY #length 354 #molecular-weight 39815 #checksum 8809 SEQUENCE /// ENTRY S73697 #type complete TITLE probable X-Pro dipeptidase (EC 3.4.13.9) pepX - Mycoplasma pneumoniae (strain ATCC 29342) ALTERNATE_NAMES hypothetical protein P01_orf354 ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S73697 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73697 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-354 ##label HIM !'##cross-references EMBL:AE000035; GB:U00089; NID:g1674044; !1PIDN:AAB96019.1; PID:g1674050 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#gene pepX !$#genetic_code SGC3 CLASSIFICATION #superfamily X-Pro aminopeptidase KEYWORDS dipeptide hydrolase SUMMARY #length 354 #molecular-weight 39624 #checksum 9739 SEQUENCE /// ENTRY F64400 #type complete TITLE X-Pro dipeptidase (EC 3.4.13.9) - Methanococcus jannaschii ALTERNATE_NAMES xaa-pro dipeptidase ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F64400 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession F64400 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-347 ##label BUL !'##cross-references GB:U67525; GB:L77117; NID:g2826325; !1PIDN:AAB98806.1; PID:g1591498; TIGR:MJ0806 GENETICS !$#map_position REV730039-728996 !$#start_codon TTG CLASSIFICATION #superfamily X-Pro aminopeptidase KEYWORDS dipeptide hydrolase SUMMARY #length 347 #molecular-weight 40549 #checksum 9141 SEQUENCE /// ENTRY E64649 #type complete TITLE probable X-Pro dipeptidase (EC 3.4.13.9) - Helicobacter pylori (strains 26695 and NCTC 11637) ALTERNATE_NAMES conserved hypothetical protein HP1037; hypothetical protein 2 aroQ 3'-region ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E64649; S72448 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession E64649 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-357 ##label TOM !'##cross-references GB:AE000611; GB:AE000511; NID:g2314173; !1PIDN:AAD08080.1; PID:g2314181; TIGR:HP1037 !'##experimental_source strain 26695 REFERENCE S72447 !$#authors Bottomley, J.R.; Clayton, C.L.; Chalk, P.A.; Kleanthous, C. !$#journal Biochem. J. (1996) 319:559-565 !$#title Cloning, sequencing, expression, purification and !1preliminary characterization of a type II dehydroquinase !1from Heliobacter pylori. !$#cross-references MUID:97069712; PMID:8912695 !$#accession S72448 !'##molecule_type DNA !'##residues 1,'S',3-69,'AR',72-73,'G' ##label BOT !'##cross-references EMBL:X98878; NID:g1419552; PIDN:CAA67381.1; !1PID:g1806001 !'##experimental_source strain NCTC 11637 GENETICS !$#gene HP1037 CLASSIFICATION #superfamily X-Pro aminopeptidase KEYWORDS dipeptide hydrolase SUMMARY #length 357 #molecular-weight 40796 #checksum 762 SEQUENCE /// ENTRY D69231 #type complete TITLE probable X-Pro dipeptidase (EC 3.4.13.9) - Methanobacterium thermoautotrophicum (strain Delta H) ALTERNATE_NAMES hypothetical protein MTH981 ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69231 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession D69231 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-336 ##label MTH !'##cross-references GB:AE000871; GB:AE000666; NID:g2622069; !1PIDN:AAB85477.1; PID:g2622080 !'##experimental_source strain Delta H GENETICS !$#gene MTH981 CLASSIFICATION #superfamily X-Pro aminopeptidase KEYWORDS dipeptide hydrolase SUMMARY #length 336 #molecular-weight 36988 #checksum 6268 SEQUENCE /// ENTRY S52202 #type complete TITLE X-Pro dipeptidase (EC 3.4.13.9) [validated] - Lactobacillus delbrueckii ALTERNATE_NAMES prolidase ORGANISM #formal_name Lactobacillus delbrueckii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S55037; S52202 REFERENCE S55037 !$#authors Stucky, K.; Klein, J.R.; Schueller, A.; Matern, H.; Henrich, !1B.; Plapp, R. !$#journal Mol. Gen. Genet. (1995) 247:494-500 !$#title Cloning and DNA sequence analysis of pepQ, a prolidase gene !1from Lactobacillus delbrueckii subsp. lactis DSM7290 and !1partial characterization of its product. !$#cross-references MUID:95287873; PMID:7770058 !$#accession S55037 !'##molecule_type DNA !'##residues 1-368 ##label ST2 !'##cross-references EMBL:Z34896; NID:g609077; PID:g609078 !'##experimental_source DSM7290 GENETICS !$#gene pepQ FUNCTION !$#description EC 3.4.13.9 [validated, MUID:95287873] CLASSIFICATION #superfamily X-Pro aminopeptidase KEYWORDS dipeptide hydrolase; metalloproteinase SUMMARY #length 368 #molecular-weight 41082 #checksum 1348 SEQUENCE /// ENTRY C70433 #type complete TITLE probable X-Pro dipeptidase (EC 3.4.13.9) - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C70433 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession C70433 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-354 ##label AQF !'##cross-references GB:AE000744; GB:AE000657; NID:g2983891; !1PIDN:AAC07447.1; PID:g2983896 !'##experimental_source strain VF5 GENETICS !$#gene pepQ CLASSIFICATION #superfamily X-Pro aminopeptidase KEYWORDS dipeptide hydrolase SUMMARY #length 354 #molecular-weight 40692 #checksum 4234 SEQUENCE /// ENTRY C70658 #type complete TITLE probable pepQ - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C70658 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession C70658 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-372 ##label COL !'##cross-references GB:Z83863; GB:AL123456; NID:g3261685; !1PIDN:CAB06173.1; PID:g1781067 !'##experimental_source strain H37Rv GENETICS !$#gene pepQ CLASSIFICATION #superfamily X-Pro aminopeptidase SUMMARY #length 372 #molecular-weight 38791 #checksum 4923 SEQUENCE /// ENTRY G69869 #type complete TITLE Xaa-Pro dipeptidase homolog ykvY - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69869 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69869 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-363 ##label KUN !'##cross-references GB:Z99111; GB:AL009126; NID:g2633699; !1PIDN:CAB13259.1; PID:g2633757 !'##experimental_source strain 168 GENETICS !$#gene ykvY CLASSIFICATION #superfamily X-Pro aminopeptidase SUMMARY #length 363 #molecular-weight 40334 #checksum 1975 SEQUENCE /// ENTRY A71089 #type complete TITLE probable dipeptidase - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A71089 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession A71089 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-356 ##label KAW !'##cross-references GB:AP000004; NID:g3236131; PIDN:BAA30071.1; !1PID:g3257388 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0974 CLASSIFICATION #superfamily X-Pro aminopeptidase SUMMARY #length 356 #molecular-weight 40175 #checksum 1337 SEQUENCE /// ENTRY F65012 #type complete TITLE hypothetical protein b2385 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS F65012 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65012 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-361 ##label BLAT !'##cross-references GB:AE000326; GB:U00096; NID:g1788718; !1PIDN:AAC75444.1; PID:g1788728; UWGP:b2385 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily X-Pro aminopeptidase SUMMARY #length 361 #molecular-weight 39624 #checksum 2355 SEQUENCE /// ENTRY G71056 #type complete TITLE probable X-Pro dipeptidase - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G71056 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession G71056 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-351 ##label KAW !'##cross-references GB:AP000005; NID:g3236132; PIDN:BAA30249.1; !1PID:g3257566 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1149 CLASSIFICATION #superfamily X-Pro aminopeptidase SUMMARY #length 351 #molecular-weight 39400 #checksum 2746 SEQUENCE /// ENTRY C69960 #type complete TITLE Xaa-Pro dipeptidase homolog yqhT - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69960 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69960 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-353 ##label KUN !'##cross-references GB:Z99116; GB:AL009126; NID:g2634723; !1PIDN:CAB14377.1; PID:g2634880 !'##experimental_source strain 168 GENETICS !$#gene yqhT CLASSIFICATION #superfamily X-Pro aminopeptidase SUMMARY #length 353 #molecular-weight 38120 #checksum 6451 SEQUENCE /// ENTRY H64306 #type complete TITLE conserved hypothetical protein MJ0056 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H64306 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession H64306 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-136 ##label BUL !'##cross-references GB:U67463; GB:L77117; NID:g1590846; !1PIDN:AAB98036.1; PID:g1590850; TIGR:MJ0056 GENETICS !$#map_position REV56166-55756 !$#start_codon TTG CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0056 SUMMARY #length 136 #molecular-weight 15685 #checksum 7068 SEQUENCE /// ENTRY B69067 #type complete TITLE conserved hypothetical protein MTH1500 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69067 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession B69067 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-122 ##label MTH !'##cross-references GB:AE000910; GB:AE000666; NID:g2622610; !1PIDN:AAB85975.1; PID:g2622617 !'##experimental_source strain Delta H GENETICS !$#gene MTH1500 !$#start_codon GTG CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0056 SUMMARY #length 122 #molecular-weight 13438 #checksum 3298 SEQUENCE /// ENTRY E71111 #type complete TITLE hypothetical protein PH0660 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E71111 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession E71111 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-212 ##label KAW !'##cross-references GB:AP000003; NID:g3236130; PIDN:BAA29751.1; !1PID:g3257068 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0660 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0056 SUMMARY #length 212 #molecular-weight 23744 #checksum 2416 SEQUENCE /// ENTRY B69513 #type complete TITLE conserved hypothetical protein AF2106 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69513 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession B69513 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-233 ##label KLE !'##cross-references GB:AE000958; GB:AE000782; NID:g2689281; !1PIDN:AAB89142.1; PID:g2648419; TIGR:AF2106 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0056 SUMMARY #length 233 #molecular-weight 26975 #checksum 9882 SEQUENCE /// ENTRY H64327 #type complete TITLE conserved hypothetical protein MJ0223 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H64327 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession H64327 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-104 ##label BUL !'##cross-references GB:U67478; GB:L77117; NID:g1590958; !1PIDN:AAB98215.1; PID:g1590961; TIGR:MJ0223 GENETICS !$#map_position REV214474-214160 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0223 SUMMARY #length 104 #molecular-weight 11805 #checksum 2358 SEQUENCE /// ENTRY G71214 #type complete TITLE hypothetical protein PH1983 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G71214 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession G71214 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-123 ##label KAW !'##cross-references GB:AP000007; NID:g3236134; PIDN:BAA31110.1; !1PID:g3258427 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1983 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0223 SUMMARY #length 123 #molecular-weight 14212 #checksum 6087 SEQUENCE /// ENTRY F69228 #type complete TITLE hypothetical protein MTH961 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F69228 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession F69228 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-107 ##label MTH !'##cross-references GB:AE000869; GB:AE000666; NID:g2622042; !1PIDN:AAB85457.1; PID:g2622058 !'##experimental_source strain Delta H GENETICS !$#gene MTH961 !$#start_codon GTG CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0223 SUMMARY #length 107 #molecular-weight 11823 #checksum 7380 SEQUENCE /// ENTRY C70437 #type complete TITLE ATP synthase F0 subunit b - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C70437 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession C70437 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-144 ##label AQF !'##cross-references GB:AE000746; GB:AE000657; NID:g2983925; !1PIDN:AAC07477.1; PID:g2983928 !'##experimental_source strain VF5 GENETICS !$#gene atpF1 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0223 SUMMARY #length 144 #molecular-weight 16719 #checksum 2535 SEQUENCE /// ENTRY H64334 #type complete TITLE conserved hypothetical protein MJ0279 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H64334 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession H64334 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-283 ##label BUL !'##cross-references GB:U67483; GB:L77117; NID:g2826270; !1PIDN:AAB98267.1; PID:g1591005; TIGR:MJ0279 GENETICS !$#map_position FOR265366-266217 !$#start_codon TTG CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0279 SUMMARY #length 283 #molecular-weight 31753 #checksum 8638 SEQUENCE /// ENTRY H71220 #type complete TITLE hypothetical protein PH0027 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H71220 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession H71220 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-277 ##label KAW !'##cross-references GB:AP000001; NID:g3236128; PIDN:BAA29095.1; !1PID:g3256412 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0027 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0279 SUMMARY #length 277 #molecular-weight 30123 #checksum 2889 SEQUENCE /// ENTRY H69012 #type complete TITLE conserved hypothetical protein MTH1098 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H69012 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession H69012 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-281 ##label MTH !'##cross-references GB:AE000880; GB:AE000666; NID:g2622192; !1PIDN:AAB85587.1; PID:g2622199 !'##experimental_source strain Delta H GENETICS !$#gene MTH1098 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0279 SUMMARY #length 281 #molecular-weight 30132 #checksum 5007 SEQUENCE /// ENTRY D69300 #type complete TITLE 4-hydroxybenzoate octaprenyltransferase homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69300 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession D69300 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-293 ##label KLE !'##cross-references GB:AE001076; GB:AE000782; NID:g2689399; !1PIDN:AAB90826.1; PID:g2650221; TIGR:AF0404 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0279 SUMMARY #length 293 #molecular-weight 32651 #checksum 4392 SEQUENCE /// ENTRY S52775 #type complete TITLE hypothetical protein 2 - Chloroflexus aurantiacus ORGANISM #formal_name Chloroflexus aurantiacus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S52775 REFERENCE S43678 !$#authors Niedermeier, G.; Shiozawa, J.A.; Lottspeich, F.; Feick, R.G. !$#journal FEBS Lett. (1994) 342:61-65 !$#title The primary structure of two chlorosome proteins from !1Chloroflexus aurantiacus. !$#cross-references MUID:94192803; PMID:7511541 !$#accession S52775 !'##status preliminary !'##molecule_type DNA !'##residues 1-305 ##label NIE !'##cross-references EMBL:Z34000; NID:g496485; PIDN:CAA83969.1; !1PID:g496488 !'##note only a part of the coding sequence is given in this paper !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1May 1994 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0279 SUMMARY #length 305 #molecular-weight 33674 #checksum 712 SEQUENCE /// ENTRY H64360 #type complete TITLE hypothetical protein MJ0488 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H64360 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession H64360 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-158 ##label BUL !'##cross-references GB:U67499; GB:L77117; NID:g1591190; !1PIDN:AAB98479.1; PID:g1591192; TIGR:MJ0488 GENETICS !$#map_position FOR432383-432859 !$#start_codon GTG CLASSIFICATION #superfamily hypothetical protein MJ0488 SUMMARY #length 158 #molecular-weight 17784 #checksum 2327 SEQUENCE /// ENTRY D69019 #type complete TITLE conserved hypothetical protein MTH1144 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69019 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession D69019 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-156 ##label MTH !'##cross-references GB:AE000884; GB:AE000666; NID:g2622242; !1PIDN:AAB85633.1; PID:g2622249 !'##experimental_source strain Delta H GENETICS !$#gene MTH1144 CLASSIFICATION #superfamily hypothetical protein MJ0488 SUMMARY #length 156 #molecular-weight 17537 #checksum 834 SEQUENCE /// ENTRY H64365 #type complete TITLE conserved hypothetical protein MJ0528 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H64365 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession H64365 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-98 ##label BUL !'##cross-references GB:U67502; GB:L77117; NID:g2826293; !1PIDN:AAB98519.1; PID:g1591231; TIGR:MJ0528 GENETICS !$#map_position REV465444-465148 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0528 SUMMARY #length 98 #molecular-weight 10936 #checksum 9927 SEQUENCE /// ENTRY G69149 #type complete TITLE conserved hypothetical protein MTH384 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69149 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession G69149 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-105 ##label MTH !'##cross-references GB:AE000824; GB:AE000666; NID:g2621443; !1PIDN:AAB84890.1; PID:g2621446 !'##experimental_source strain Delta H GENETICS !$#gene MTH384 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0528 SUMMARY #length 105 #molecular-weight 11173 #checksum 6298 SEQUENCE /// ENTRY H64370 #type complete TITLE hypothetical protein MJ0568 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H64370 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession H64370 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-125 ##label BUL !'##cross-references GB:U67506; GB:L77117; NID:g1591274; !1PIDN:AAB98562.1; PID:g1592296; TIGR:MJ0568 GENETICS !$#map_position FOR504849-505226 CLASSIFICATION #superfamily conserved hypothetical protein MJ0568 SUMMARY #length 125 #molecular-weight 14588 #checksum 4101 SEQUENCE /// ENTRY H69472 #type complete TITLE iron-dependent repressor homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H69472 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession H69472 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-191 ##label KLE !'##cross-references GB:AE000979; GB:AE000782; NID:g2689302; !1PIDN:AAB89462.1; PID:g2648760; TIGR:AF1785 CLASSIFICATION #superfamily conserved hypothetical protein MJ0568 SUMMARY #length 191 #molecular-weight 21862 #checksum 3960 SEQUENCE /// ENTRY E71058 #type complete TITLE hypothetical protein PH1163 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E71058 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession E71058 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-148 ##label KAW !'##cross-references GB:AP000005; NID:g3236132; PIDN:BAA30263.1; !1PID:g3257580 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1163 CLASSIFICATION #superfamily conserved hypothetical protein MJ0568 SUMMARY #length 148 #molecular-weight 17401 #checksum 7626 SEQUENCE /// ENTRY D69549 #type complete TITLE iron-dependent repressor homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69549 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession D69549 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-148 ##label KLE !'##cross-references GB:AE001111; GB:AE000782; NID:g2689434; !1PIDN:AAB91276.1; PID:g2650706; TIGR:AF2395 CLASSIFICATION #superfamily conserved hypothetical protein MJ0568 SUMMARY #length 148 #molecular-weight 17304 #checksum 9190 SEQUENCE /// ENTRY D71357 #type complete TITLE probable cation-activated repressor protein (troR) - syphilis spirochete ORGANISM #formal_name Treponema pallidum subsp. pallidum #common_name syphilis spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS D71357 REFERENCE A71250 !$#authors Fraser, C.M.; Norris, S.J.; Weinstock, G.M.; White, O.; !1Sutton, G.G.; Dodson, R.; Gwinn, M.; Hickey, E.K.; Clayton, !1R.; Ketchum, K.A.; Sodergren, E.; Hardham, J.M.; McLeod, !1M.P.; Salzberg, S.; Peterson, J.; Khalak, H.; Richardson, !1D.; Howell, J.K.; Chidambaram, M.; Utterback, T.; McDonald, !1L.; Artiach, P.; Bowman, C.; Cotton, M.D.; Fujii, C.; !1Garland, S.; Hatch, B.; Horst, K.; Roberts, K.; Watthey, L.; !1Weidman, J.; Smith, H.O.; Venter, J.C. !$#journal Science (1998) 281:375-388 !$#title Complete genome sequence of Treponema pallidum, the syphilis !1spirochete. !$#cross-references MUID:98332770; PMID:9665876 !$#accession D71357 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-153 ##label COL !'##cross-references GB:AE001201; GB:AE000520; NID:g3322431; !1PIDN:AAC65157.1; PID:g3322435 !'##experimental_source strain Nichols GENETICS !$#gene TP0167 CLASSIFICATION #superfamily conserved hypothetical protein MJ0568 SUMMARY #length 153 #molecular-weight 17122 #checksum 1955 SEQUENCE /// ENTRY E69959 #type complete TITLE transcription regulator homolog yqhN - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69959 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69959 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-142 ##label KUN !'##cross-references GB:Z99116; GB:AL009126; NID:g2634723; !1PIDN:CAB14383.1; PID:g2634886 !'##experimental_source strain 168 GENETICS !$#gene yqhN CLASSIFICATION #superfamily conserved hypothetical protein MJ0568 SUMMARY #length 142 #molecular-weight 16745 #checksum 2567 SEQUENCE /// ENTRY D69225 #type complete TITLE iron repressor - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69225 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession D69225 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-140 ##label MTH !'##cross-references GB:AE000868; GB:AE000666; NID:g2622025; !1PIDN:AAB85434.1; PID:g2622034 !'##experimental_source strain Delta H GENETICS !$#gene MTH936 !$#start_codon TTG CLASSIFICATION #superfamily conserved hypothetical protein MJ0568 SUMMARY #length 140 #molecular-weight 16349 #checksum 59 SEQUENCE /// ENTRY C69331 #type complete TITLE hypothetical protein AF0651 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69331 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession C69331 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-76 ##label KLE !'##cross-references GB:AE001060; GB:AE000782; NID:g2689383; !1PIDN:AAB90606.1; PID:g2649985; TIGR:AF0651 CLASSIFICATION #superfamily Archaeoglobus fulgidus transcription regulator !1asnC SUMMARY #length 76 #molecular-weight 8296 #checksum 1158 SEQUENCE /// ENTRY E71108 #type complete TITLE probable regulatory protein AsnC - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E71108 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession E71108 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-75 ##label KAW !'##cross-references GB:AP000003; NID:g3236130; PIDN:BAA29727.1; !1PID:g3257044 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PHS023 CLASSIFICATION #superfamily Archaeoglobus fulgidus transcription regulator !1asnC SUMMARY #length 75 #molecular-weight 8602 #checksum 9132 SEQUENCE /// ENTRY C69425 #type complete TITLE transcription regulator asnC - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69425 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession C69425 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-77 ##label KLE !'##cross-references GB:AE001007; GB:AE000782; NID:g2689330; !1PIDN:AAB89844.1; PID:g2649171; TIGR:AF1404 CLASSIFICATION #superfamily Archaeoglobus fulgidus transcription regulator !1asnC SUMMARY #length 77 #molecular-weight 8576 #checksum 2645 SEQUENCE /// ENTRY A64221 #type complete TITLE MgPa operon hypothetical protein MG190 - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 07-Dec-1999 ACCESSIONS A64221; JQ0091 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession A64221 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-361 ##label TIGR !'##cross-references GB:U39696; GB:L43967; NID:g1045869; PID:g1045875; !1TIGR:MG190 !'##experimental_source strain G-37 REFERENCE JQ0090 !$#authors Inamine, J.M.; Loechel, S.; Collier, A.M.; Barile, M.F.; Hu, !1P.C. !$#journal Gene (1989) 82:259-267 !$#title Nucleotide sequence of the MgPa (mgp) operon of Mycoplasma !1genitalium and comparison to the P1 (mpp) operon of !1Mycoplasma pneumoniae. !$#cross-references MUID:90060815; PMID:2583522 !$#accession JQ0091 !'##molecule_type DNA !'##residues 109-312,'E',314-361 ##label INA !'##cross-references GB:M31431; NID:g150157; PIDN:AAA25419.1; !1PID:g150158 !'##experimental_source strain G-37, ATCC 33530 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily Mycoplasma conserved hypothetical protein MG190 SUMMARY #length 361 #molecular-weight 41521 #checksum 7720 SEQUENCE /// ENTRY S73340 #type complete TITLE hypothetical protein 4 - Mycoplasma pneumoniae (strain ATCC 29342) ALTERNATE_NAMES hypothetical protein E07_orf324 ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 10-Dec-1999 ACCESSIONS S73340; JS0068 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73340 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-324 ##label HIM !'##cross-references EMBL:AE000002; GB:U00089; NID:g1673651; !1PIDN:AAB95662.1; PID:g1673660 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 REFERENCE JS0068 !$#authors Inamine, J.M.; Loechel, S.; Hu, P.C. !$#journal Gene (1988) 73:175-183 !$#title Analysis of the nucleotide sequence of the P1 operon of !1Mycoplasma pneumoniae. !$#cross-references MUID:89211947; PMID:2468577 !$#accession JS0068 !'##molecule_type DNA !'##residues 84-324 ##label INA !'##cross-references GB:M21519; GB:M20916; NID:g150138; PIDN:AAA88324.1; !1PID:g1196657 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily Mycoplasma conserved hypothetical protein MG190 SUMMARY #length 324 #molecular-weight 37144 #checksum 6569 SEQUENCE /// ENTRY F69999 #type complete TITLE conserved hypothetical protein ytqI - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 21-Jul-2000 ACCESSIONS F69999 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69999 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-313 ##label KUN !'##cross-references GB:Z99118; GB:AL009126; NID:g2635200; !1PIDN:CAB14885.1; PID:g2635390 !'##experimental_source strain 168 GENETICS !$#gene ytqI CLASSIFICATION #superfamily Mycoplasma conserved hypothetical protein MG190 SUMMARY #length 313 #molecular-weight 35084 #checksum 7316 SEQUENCE /// ENTRY A64241 #type complete TITLE hypothetical protein homolog MG371 - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 07-Dec-1999 ACCESSIONS A64241 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession A64241 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-324 ##label TIGR !'##cross-references GB:U39722; GB:L43967; NID:g1046079; PID:g1046081; !1TIGR:MG371 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily Mycoplasma conserved hypothetical protein MG190 SUMMARY #length 324 #molecular-weight 37232 #checksum 7462 SEQUENCE /// ENTRY S73619 #type complete TITLE hypothetical protein G12_orf325 - Mycoplasma pneumoniae (strain ATCC 29342) ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 10-Dec-1999 ACCESSIONS S73619 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73619 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-325 ##label HIM !'##cross-references EMBL:AE000027; GB:U00089; NID:g1673941; !1PIDN:AAB95941.1; PID:g1673964 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily Mycoplasma conserved hypothetical protein MG190 SUMMARY #length 325 #molecular-weight 36767 #checksum 8029 SEQUENCE /// ENTRY B70177 #type complete TITLE conserved hypothetical protein BB0619 - Lyme disease spirochete ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 21-Jul-2000 ACCESSIONS B70177 REFERENCE A70100 !$#authors Fraser, C.M.; Casjens, S.; Huang, W.M.; Sutton, G.G.; !1Clayton, R.; Lathigra, R.; White, O.; Ketchum, K.A.; Dodson, !1R.; Hickey, E.K.; Gwinn, M.; Dougherty, B.; Tomb, J.F.; !1Fleischmann, R.D.; Richardson, D.; Peterson, J.; Kerlavage, !1A.R.; Quackenbush, J.; Salzberg, S.; Hanson, M.; Vugt, R.V.; !1Palmer, N.; Adams, M.D.; Gocayne, J.; Weidman, J.; !1Utterback, T.; Watthey, L.; McDonald, L.; Artiach, P.; !1Bowman, C.; Garland, S.; Fujii, C.; Cotton, M.D.; Horst, K.; !1Roberts, K.; Hatch, B.; Smith, H.O.; Venter, J.C. !$#journal Nature (1997) 390:580-586 !$#title Genomic sequence of a Lyme disease spirochaete, Borrelia !1burgdorferi. !$#cross-references MUID:98065943; PMID:9403685 !$#accession B70177 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-330 ##label KLE !'##cross-references GB:AE001163; GB:AE000783; NID:g2688541; !1PIDN:AAC66977.1; PID:g2688546; TIGR:BB0619 !'##experimental_source strain B31 CLASSIFICATION #superfamily Mycoplasma conserved hypothetical protein MG190 SUMMARY #length 330 #molecular-weight 37377 #checksum 7271 SEQUENCE /// ENTRY H64390 #type complete TITLE carbon-monoxide dehydrogenase (EC 1.2.99.2) beta chain MJ0728 [similarity] - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS H64390 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession H64390 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-628 ##label BUL !'##cross-references GB:U67519; GB:L77117; NID:g1591436; PID:g1591444; !1TIGR:MJ0728; PID:g1510815 GENETICS !$#map_position REV662463-660577 !$#start_codon TTG CLASSIFICATION #superfamily carbon-monoxide dehydrogenase beta chain; !1hybrid cluster [4Fe-2S-3O] homology KEYWORDS 4Fe-2S-3O; 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein; oxidoreductase FEATURE !$233-576 #domain hybrid cluster [4Fe-2S-3O] homology #label !8HCL\ !$50,53,58,69 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$260,302,340,448, !$479,520,555 #binding_site Ni-3Fe-2S-3O cluster (His, Glu, Cys, !8Cys, Cys, Cys, Glu) (covalent) #status predicted\ !$448 #modified_site cysteine persulfide (Cys) #status !8predicted SUMMARY #length 628 #molecular-weight 67808 #checksum 975 SEQUENCE /// ENTRY C42957 #type complete TITLE carbon-monoxide dehydrogenase (EC 1.2.99.2) beta chain CooS [similarity] - Rhodospirillum rubrum ORGANISM #formal_name Rhodospirillum rubrum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Sep-2000 ACCESSIONS C42957; T51321 REFERENCE A42957 !$#authors Kerby, R.L.; Hong, S.S.; Ensign, S.A.; Coppoc, L.J.; Ludden, !1P.W.; Roberts, G.P. !$#journal J. Bacteriol. (1992) 174:5284-5294 !$#title Genetic and physiological characterization of the !1Rhodospirillum rubrum carbon monoxide dehydrogenase system. !$#cross-references MUID:92355502; PMID:1644755 !$#accession C42957 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA; protein !'##residues 1-639 ##label KER !'##cross-references GB:U65510; GB:U43789; GB:M90421; GB:S41762; !1GB:U20508; NID:g1515463; PIDN:AAC45123.1; PID:g1498748 !'##experimental_source strain UR1 !'##note sequence extracted from NCBI backbone (NCBIP:110361) GENETICS !$#gene cooS CLASSIFICATION #superfamily carbon-monoxide dehydrogenase beta chain; !1hybrid cluster [4Fe-2S-3O] homology KEYWORDS 4Fe-2S-3O; 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein; oxidoreductase FEATURE !$238-587 #domain hybrid cluster [4Fe-2S-3O] homology #label !8HCL\ !$50,53,58,72 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$265,304,338,451, !$481,531,566 #binding_site Ni-3Fe-2S-3O cluster (His, Glu, Cys, !8Cys, Cys, Cys, Ser) (covalent) #status predicted\ !$451 #modified_site cysteine persulfide (Cys) #status !8predicted SUMMARY #length 639 #molecular-weight 66853 #checksum 293 SEQUENCE /// ENTRY A41670 #type complete TITLE carbon-monoxide dehydrogenase (EC 1.2.99.2) beta chain [similarity] - Clostridium thermaceticum ORGANISM #formal_name Clostridium thermaceticum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS A41670 REFERENCE A41670 !$#authors Morton, T.A.; Runquist, J.A.; Ragsdale, S.W.; !1Shanmugasundaram, T.; Wood, H.G.; Ljungdahl, L.G. !$#journal J. Biol. Chem. (1991) 266:23824-23828 !$#title The primary structure of the subunits of carbon monoxide !1dehydrogenase/acetyl-CoA synthase from Clostridium !1thermoaceticum. !$#cross-references MUID:92084676; PMID:1748656 !$#accession A41670 !'##status preliminary !'##molecule_type DNA !'##residues 1-674 ##label MOR !'##cross-references GB:M62727; NID:g144784; PIDN:AAA23228.1; !1PID:g144785 CLASSIFICATION #superfamily carbon-monoxide dehydrogenase beta chain; !1hybrid cluster [4Fe-2S-3O] homology KEYWORDS 4Fe-2S-3O; 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein; oxidoreductase FEATURE !$256-606 #domain hybrid cluster [4Fe-2S-3O] homology #label !8HCL\ !$68,71,76,90 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$283,321,355,470, !$500,550,585 #binding_site Ni-3Fe-2S-3O cluster (His, Glu, Cys, !8Cys, Cys, Cys, Ser) (covalent) #status predicted\ !$470 #modified_site cysteine persulfide (Cys) #status !8predicted SUMMARY #length 674 #molecular-weight 72923 #checksum 9461 SEQUENCE /// ENTRY H69480 #type complete TITLE carbon-monoxide dehydrogenase (EC 1.2.99.2) beta chain AF1849 [similarity] - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS H69480 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession H69480 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-622 ##label KLE !'##cross-references GB:AE000975; GB:AE000782; NID:g2689298; !1PIDN:AAB89403.1; PID:g2648697; TIGR:AF1849 CLASSIFICATION #superfamily carbon-monoxide dehydrogenase beta chain; !1hybrid cluster [4Fe-2S-3O] homology KEYWORDS 4Fe-2S-3O; 4Fe-4S; electron transfer; iron-sulfur protein; !1metalloprotein; oxidoreductase FEATURE !$229-570 #domain hybrid cluster [4Fe-2S-3O] homology #label !8HCL\ !$49,52,57,68 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8predicted\ !$256,296,334,442, !$473,514,549 #binding_site Ni-3Fe-2S-3O cluster (His, Glu, Cys, !8Cys, Cys, Cys, Glu) (covalent) #status predicted\ !$442 #modified_site cysteine persulfide (Cys) #status !8predicted SUMMARY #length 622 #molecular-weight 67496 #checksum 6993 SEQUENCE /// ENTRY H64394 #type complete TITLE conserved hypothetical protein MJ0760 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H64394 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession H64394 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-275 ##label BUL !'##cross-references GB:U67521; GB:L77117; NID:g1591463; !1PIDN:AAB98751.1; PID:g1499579; TIGR:MJ0760 GENETICS !$#map_position REV683873-683046 !$#start_codon GTG CLASSIFICATION #superfamily Methanococcus jannaschii hypothetical protein !1MJ0760 SUMMARY #length 275 #molecular-weight 30542 #checksum 3110 SEQUENCE /// ENTRY G69055 #type complete TITLE conserved hypothetical protein MTH1417 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69055 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession G69055 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-269 ##label MTH !'##cross-references GB:AE000904; GB:AE000666; NID:g2622528; !1PIDN:AAB85894.1; PID:g2622530 !'##experimental_source strain Delta H GENETICS !$#gene MTH1417 CLASSIFICATION #superfamily Methanococcus jannaschii hypothetical protein !1MJ0760 SUMMARY #length 269 #molecular-weight 29419 #checksum 7251 SEQUENCE /// ENTRY A64222 #type complete TITLE heat shock protein dnaJ homolog MG200 - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 07-Dec-1999 ACCESSIONS A64222; T09695 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession A64222 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-601 ##label TIGR !'##cross-references GB:U39697; GB:L43967; NID:g1045878; PID:g1045885; !1TIGR:MG200 !'##experimental_source strain G-37 REFERENCE Z16818 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.L.; Nguyen, !1D.T.; Utterback, T.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Venter, J.C. !$#submission submitted to the EMBL Data Library, October 1998 !$#accession T09695 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-601 ##label FRA !'##cross-references EMBL:U39699; NID:g3844790; PID:g3844797 !'##experimental_source isolate G37 GENETICS !$#gene MG200 !$#genetic_code SGC3 CLASSIFICATION #superfamily Mycoplasma heat shock protein dnaJ homolog !1MG200; dnaJ amino-terminal homology KEYWORDS molecular chaperone FEATURE !$7-71 #domain dnaJ amino-terminal homology #label DNJ SUMMARY #length 601 #molecular-weight 68537 #checksum 3916 SEQUENCE /// ENTRY H64395 #type complete TITLE hypothetical protein MJ0768 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Dec-2002 ACCESSIONS H64395 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession H64395 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-249 ##label BUL !'##cross-references GB:U67522; GB:L77117; NID:g2826315; !1PIDN:AAB98763.1; PID:g1499588; TIGR:MJ0768 GENETICS !$#map_position FOR689591-690340 CLASSIFICATION #superfamily uncharacterized conserved protein SUMMARY #length 249 #molecular-weight 27147 #checksum 3325 SEQUENCE /// ENTRY H69531 #type complete TITLE conserved hypothetical protein AF2256 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Dec-2002 ACCESSIONS H69531 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession H69531 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-249 ##label KLE !'##cross-references GB:AE000949; GB:AE000782; NID:g2689272; !1PIDN:AAB89001.1; PID:g2648269; TIGR:AF2256 CLASSIFICATION #superfamily uncharacterized conserved protein SUMMARY #length 249 #molecular-weight 27261 #checksum 4948 SEQUENCE /// ENTRY G71493 #type complete TITLE hypothetical protein CT611 - Chlamydia trachomatis (serotype D, strain UW3/Cx) ORGANISM #formal_name Chlamydia trachomatis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Dec-2002 ACCESSIONS G71493 REFERENCE A71570 !$#authors Stephens, R.S.; Kalman, S.; Lammel, C.J.; Fan, J.; Marathe, !1R.; Aravind, L.; Mitchell, W.P.; Olinger, L.; Tatusov, R.L.; !1Zhao, Q.; Koonin, E.V.; Davis, R.W. !$#journal Science (1998) 282:754-759 !$#title Genome sequence of an obligate intracellular pathogen of !1humans: Chlamydia trachomatis. !$#cross-references MUID:99000809; PMID:9784136 !$#accession G71493 !'##status preliminary !'##molecule_type DNA !'##residues 1-243 ##label ARN !'##cross-references GB:AE001331; GB:AE001273; NID:g3329046; !1PID:g3329056 !'##experimental_source serotype D, strain UW-3/Cx GENETICS !$#gene CT611 CLASSIFICATION #superfamily uncharacterized conserved protein SUMMARY #length 243 #molecular-weight 27115 #checksum 1451 SEQUENCE /// ENTRY H69002 #type complete TITLE conserved hypothetical protein MTH1019 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Dec-2002 ACCESSIONS H69002 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession H69002 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-252 ##label MTH !'##cross-references GB:AE000874; GB:AE000666; NID:g2622110; !1PIDN:AAB85515.1; PID:g2622121 !'##experimental_source strain Delta H GENETICS !$#gene MTH1019 CLASSIFICATION #superfamily uncharacterized conserved protein SUMMARY #length 252 #molecular-weight 26538 #checksum 8295 SEQUENCE /// ENTRY S73361 #type complete TITLE dnaJ homolog protein C09_orf910 - Mycoplasma pneumoniae (strain ATCC 29342) ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 10-Dec-1999 ACCESSIONS S73361 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73361 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-910 ##label HIM !'##cross-references EMBL:AE000004; GB:U00089; NID:g1673671; !1PIDN:AAB95683.1; PID:g1673683 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily Mycoplasma heat shock protein dnaJ homolog !1C09_orf910; dnaJ amino-terminal homology FEATURE !$7-71 #domain dnaJ amino-terminal homology #label DNJ SUMMARY #length 910 #molecular-weight 100190 #checksum 3719 SEQUENCE /// ENTRY C69405 #type complete TITLE hypothetical protein AF1244 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69405 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession C69405 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-161 ##label KLE !'##cross-references GB:AE001018; GB:AE000782; NID:g2689341; !1PIDN:AAB90005.1; PID:g2649342; TIGR:AF1244 CLASSIFICATION #superfamily Archaeoglobus hypothetical protein AF1244 SUMMARY #length 161 #molecular-weight 17496 #checksum 6520 SEQUENCE /// ENTRY B70474 #type complete TITLE hypothetical protein aq_2028 - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B70474 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession B70474 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-169 ##label AQF !'##cross-references GB:AE000768; GB:AE000657; NID:g2984249; !1PIDN:AAC07786.1; PID:g2984259 !'##experimental_source strain VF5 GENETICS !$#gene aq_2028 CLASSIFICATION #superfamily Archaeoglobus hypothetical protein AF1244 SUMMARY #length 169 #molecular-weight 19020 #checksum 5180 SEQUENCE /// ENTRY G70591 #type complete TITLE hypothetical protein Rv3237c - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G70591 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession G70591 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-160 ##label COL !'##cross-references GB:Z95121; GB:AL123456; NID:g3261742; !1PIDN:CAB08338.1; PID:g2072704 !'##experimental_source strain H37Rv GENETICS !$#gene Rv3237c CLASSIFICATION #superfamily Archaeoglobus hypothetical protein AF1244 SUMMARY #length 160 #molecular-weight 17233 #checksum 2331 SEQUENCE /// ENTRY S73720 #type complete TITLE cytadherence accessory protein HMW1 - Mycoplasma pneumoniae (strain ATCC 29342) ALTERNATE_NAMES hypothetical protein H08_orf1018 ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 10-Dec-1999 ACCESSIONS S73720; S49064; S49065 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73720 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1018 ##label HIM !'##cross-references EMBL:AE000038; GB:U00089; NID:g1674074; !1PIDN:AAB96042.1; PID:g1674076 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 REFERENCE S49059 !$#authors Proft, T.; Herrmann, R. !$#journal Mol. Microbiol. (1994) 13:337-348 !$#title Identification and characterization of hitherto unknown !1Mycoplasma pneumoniae proteins. !$#cross-references MUID:95075318; PMID:7984111 !$#accession S49064 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 127-242 ##label PRO !'##cross-references EMBL:Z32661; NID:g474075; PIDN:CAA83580.1; !1PID:g474076 !'##experimental_source clone H8-1F !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1994 !$#accession S49065 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 62-113 ##label PRW !'##cross-references EMBL:Z32662; NID:g474077; PIDN:CAA83581.1; !1PID:g474078 !'##experimental_source clone E9-4B !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1April 1994 GENETICS !$#gene hmw1 !$#genetic_code SGC3 CLASSIFICATION #superfamily cytadherence-accessory protein hmw1 SUMMARY #length 1018 #molecular-weight 112214 #checksum 2522 SEQUENCE /// ENTRY E64234 #type complete TITLE cytadherence-accessory protein (hmw1) homolog MG312 - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 21-Jul-2000 ACCESSIONS E64234 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession E64234 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-1139 ##label TIGR !'##cross-references GB:U39712; GB:L43967; NID:g3844889; !1PIDN:AAC71534.1; PID:g1046012; TIGR:MG312 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily cytadherence-accessory protein hmw1 SUMMARY #length 1139 #molecular-weight 130531 #checksum 7212 SEQUENCE /// ENTRY C70019 #type complete TITLE methylglyoxalase homolog yurT - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C70019 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C70019 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-127 ##label KUN !'##cross-references GB:Z99120; GB:AL009126; NID:g2635613; !1PIDN:CAB15255.1; PID:g2635762 !'##experimental_source strain 168 GENETICS !$#gene yurT CLASSIFICATION #superfamily Bacillus probable methylglyoxalase yurT SUMMARY #length 127 #molecular-weight 14438 #checksum 8376 SEQUENCE /// ENTRY C69434 #type complete TITLE conserved hypothetical protein AF1476 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69434 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession C69434 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-177 ##label KLE !'##cross-references GB:AE001000; GB:AE000782; NID:g2689323; !1PIDN:AAB89765.1; PID:g2649084; TIGR:AF1476 CLASSIFICATION #superfamily Bacillus probable methylglyoxalase yurT SUMMARY #length 177 #molecular-weight 20368 #checksum 9784 SEQUENCE /// ENTRY E69798 #type complete TITLE conserved hypothetical protein yetH - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69798 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69798 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-120 ##label KUN !'##cross-references GB:Z99107; GB:AL009126; NID:g2632866; !1PIDN:CAB12535.1; PID:g2633029 !'##experimental_source strain 168 GENETICS !$#gene yetH CLASSIFICATION #superfamily Bacillus probable methylglyoxalase yurT SUMMARY #length 120 #molecular-weight 13634 #checksum 712 SEQUENCE /// ENTRY S73715 #type complete TITLE cytadherence accessory protein HMW3 - Mycoplasma pneumoniae ALTERNATE_NAMES hypothetical protein H08_orf672 ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 21-Jul-2000 ACCESSIONS S73715; A43851; PH0112 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73715 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-672 ##label HIM !'##cross-references EMBL:AE000037; GB:U00089; NID:g1674065; !1PIDN:AAB96037.1; PID:g1674070 !'##experimental_source ATCC 29342 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 REFERENCE A43851 !$#authors Ogle, K.F.; Lee, K.K.; Krause, D.C. !$#journal Infect. Immun. (1992) 60:1633-1641 !$#title Nucleotide sequence analysis reveals novel features of the !1phase-variable cytadherence accessory protein HMW3 of !1Mycoplasma pneumoniae. !$#cross-references MUID:92192840; PMID:1548085 !$#accession A43851 !'##status preliminary !'##molecule_type DNA !'##residues 1-672 ##label OGL1 !'##cross-references GB:L38997; GB:M82965; GB:S89246; GB:U11381; !1NID:g639784; PIDN:AAA61692.1; PID:g639785 !'##note sequence extracted from NCBI backbone (NCBIN:89246, !1NCBIP:89247) REFERENCE PH0112 !$#authors Ogle, K.F.; Lee, K.K.; Krause, D.C. !$#journal Gene (1991) 97:69-75 !$#title Cloning and analysis of the gene encoding the cytadherence !1phase-variable protein HMW3 from Mycoplasma pneumoniae. !$#cross-references MUID:91138988; PMID:1899847 !$#accession PH0112 !'##molecule_type protein !'##residues 279-287,'R',289-290 ##label OGL2 !'##note the amino end of the mature protein is blocked GENETICS !$#gene hmw3 !$#genetic_code SGC3 CLASSIFICATION #superfamily cytadherence-accessory protein hmw3 KEYWORDS blocked amino end SUMMARY #length 672 #molecular-weight 73721 #checksum 3983 SEQUENCE /// ENTRY A64235 #type complete TITLE cytadherence-accessory protein (hmw3) homolog MG317 - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 07-Dec-1999 ACCESSIONS A64235 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession A64235 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-599 ##label TIGR !'##cross-references GB:U39713; GB:L43967; NID:g1046014; PID:g1046018; !1TIGR:MG317 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily cytadherence-accessory protein hmw3 SUMMARY #length 599 #molecular-weight 68720 #checksum 1981 SEQUENCE /// ENTRY D69023 #type complete TITLE cell division inhibitor related protein - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69023 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession D69023 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-298 ##label MTH !'##cross-references GB:AE000886; GB:AE000666; NID:g2622276; !1PIDN:AAB85662.1; PID:g2622280 !'##experimental_source strain Delta H GENETICS !$#gene MTH1173 !$#start_codon GTG CLASSIFICATION #superfamily cell division inhibitor related protein; !1ferredoxin 2[4Fe-4S] homology FEATURE !$65-122 #domain ferredoxin 2[4Fe-4S] homology #label FER SUMMARY #length 298 #molecular-weight 32138 #checksum 3583 SEQUENCE /// ENTRY E69547 #type complete TITLE iron-sulfur cluster binding protein homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69547 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession E69547 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-283 ##label KLE !'##cross-references GB:AE001112; GB:AE000782; NID:g2689435; !1PIDN:AAB91284.1; PID:g2650715; TIGR:AF2381 CLASSIFICATION #superfamily cell division inhibitor related protein; !1ferredoxin 2[4Fe-4S] homology FEATURE !$60-113 #domain ferredoxin 2[4Fe-4S] homology #label FER2 SUMMARY #length 283 #molecular-weight 30969 #checksum 9605 SEQUENCE /// ENTRY B71090 #type complete TITLE hypothetical protein PH0983 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B71090 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession B71090 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-300 ##label KAW !'##cross-references GB:AP000004; NID:g3236131; PIDN:BAA30080.1; !1PID:g3257397 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0983 CLASSIFICATION #superfamily cell division inhibitor related protein; !1ferredoxin 2[4Fe-4S] homology FEATURE !$67-123 #domain ferredoxin 2[4Fe-4S] homology #label FER1 SUMMARY #length 300 #molecular-weight 32619 #checksum 4224 SEQUENCE /// ENTRY B64372 #type complete TITLE ferredoxin - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B64372 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession B64372 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-276 ##label BUL !'##cross-references GB:U67506; GB:L77117; NID:g1591274; !1PIDN:AAB98569.1; PID:g1591285; TIGR:MJ0578 GENETICS !$#map_position REV514290-513460 !$#start_codon TTG CLASSIFICATION #superfamily cell division inhibitor related protein; !1ferredoxin 2[4Fe-4S] homology FEATURE !$69-119 #domain ferredoxin 2[4Fe-4S] homology #label FER SUMMARY #length 276 #molecular-weight 30794 #checksum 8967 SEQUENCE /// ENTRY D69547 #type complete TITLE iron-sulfur cluster binding protein homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69547 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession D69547 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-262 ##label KLE !'##cross-references GB:AE001112; GB:AE000782; NID:g2689435; !1PIDN:AAB91285.1; PID:g2650716; TIGR:AF2380 CLASSIFICATION #superfamily cell division inhibitor related protein; !1ferredoxin 2[4Fe-4S] homology FEATURE !$52-109 #domain ferredoxin 2[4Fe-4S] homology #label FER SUMMARY #length 262 #molecular-weight 28793 #checksum 1418 SEQUENCE /// ENTRY A71090 #type complete TITLE hypothetical protein PH0982 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A71090 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession A71090 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-286 ##label KAW !'##cross-references GB:AP000004; NID:g3236131; PIDN:BAA30079.1; !1PID:g3257396 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0982 CLASSIFICATION #superfamily cell division inhibitor related protein; !1ferredoxin 2[4Fe-4S] homology FEATURE !$62-118 #domain ferredoxin 2[4Fe-4S] homology #label FER SUMMARY #length 286 #molecular-weight 31564 #checksum 4638 SEQUENCE /// ENTRY E69023 #type complete TITLE cell division inhibitor related protein - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69023 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession E69023 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-291 ##label MTH !'##cross-references GB:AE000886; GB:AE000666; NID:g2622276; !1PIDN:AAB85663.1; PID:g2622281 !'##experimental_source strain Delta H GENETICS !$#gene MTH1174 CLASSIFICATION #superfamily cell division inhibitor related protein; !1ferredoxin 2[4Fe-4S] homology SUMMARY #length 291 #molecular-weight 31736 #checksum 7939 SEQUENCE /// ENTRY D30191 #type complete TITLE conserved hypothetical protein yviA - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 21-Jul-2000 ACCESSIONS I40386; D30191; A70042; S28596 REFERENCE I40386 !$#authors Londono-Vallejo, J.A.; Dubnau, D. !$#journal Mol. Microbiol. (1993) 9:119-131 !$#title comF, a Bacillus subtilis late competence locus, encodes a !1protein similar to ATP-dependent RNA/DNA helicases. !$#cross-references MUID:94018599; PMID:8412657 !$#accession I40386 !'##molecule_type DNA !'##residues 1-281 ##label RES !'##cross-references EMBL:Z18629; NID:g39847; PIDN:CAA79225.1; !1PID:g39848 REFERENCE A30191 !$#authors Henner, D.J.; Yang, M.; Ferrari, E. !$#journal J. Bacteriol. (1988) 170:5102-5109 !$#title Localization of Bacillus subtilis sacU(Hy) mutations to two !1linked genes with similarities to the conserved procaryotic !1family of two-component signalling systems. !$#cross-references MUID:89033891; PMID:3141378 !$#accession D30191 !'##molecule_type DNA !'##residues 1-107 ##label HEN REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A70042 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-281 ##label KUN !'##cross-references GB:Z99122; GB:AL009126; NID:g2636029; !1PIDN:CAB15565.1; PID:g2636074 !'##experimental_source strain 168 GENETICS !$#gene yviA CLASSIFICATION #superfamily Mycoplasma hypothetical protein MG326 SUMMARY #length 281 #molecular-weight 31580 #checksum 6037 SEQUENCE /// ENTRY A64236 #type complete TITLE hypothetical protein homolog MG326 - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 07-Dec-1999 ACCESSIONS A64236 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession A64236 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-295 ##label TIGR !'##cross-references GB:U39715; GB:L43967; NID:g1046026; PID:g1046029; !1TIGR:MG326 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily Mycoplasma hypothetical protein MG326 SUMMARY #length 295 #molecular-weight 33413 #checksum 8707 SEQUENCE /// ENTRY S73695 #type complete TITLE degV homolog P01_orf293 - Mycoplasma pneumoniae (strain ATCC 29342) ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 10-Dec-1999 ACCESSIONS S73695 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73695 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-293 ##label HIM !'##cross-references EMBL:AE000035; GB:U00089; NID:g1674044; !1PIDN:AAB96017.1; PID:g1674048 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily Mycoplasma hypothetical protein MG326 SUMMARY #length 293 #molecular-weight 32779 #checksum 1481 SEQUENCE /// ENTRY S74557 #type complete TITLE acetylpolyamine aminohydrolase - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES hypothetical protein slr0245 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S74557 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74557 !'##status preliminary !'##molecule_type DNA !'##residues 1-304 ##label KAN !'##cross-references EMBL:D90900; GB:AB001339; NID:g1651768; !1PIDN:BAA16709.1; PID:g1651782 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily acetylpolyamine aminohydrolase; RPD3/acuC !1homology SUMMARY #length 304 #molecular-weight 33649 #checksum 4903 SEQUENCE /// ENTRY C69026 #type complete TITLE acetylpolyamine aminohydrolase - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69026 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession C69026 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-331 ##label MTH !'##cross-references GB:AE000887; GB:AE000666; NID:g2622289; !1PIDN:AAB85683.1; PID:g2622302 !'##experimental_source strain Delta H GENETICS !$#gene MTH1194 CLASSIFICATION #superfamily acetylpolyamine aminohydrolase; RPD3/acuC !1homology FEATURE !$3-298 #domain RPD3/acuC homology #label RAH1 SUMMARY #length 331 #molecular-weight 36722 #checksum 7627 SEQUENCE /// ENTRY B69266 #type complete TITLE acetylpolyamine aminohydrolase (aphA) homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69266 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession B69266 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-359 ##label KLE !'##cross-references GB:AE001097; GB:AE000782; NID:g2689420; !1PIDN:AAB91099.1; PID:g2650515; TIGR:AF0130 CLASSIFICATION #superfamily acetylpolyamine aminohydrolase; RPD3/acuC !1homology FEATURE !$5-303 #domain RPD3/acuC homology #label RAH1 SUMMARY #length 359 #molecular-weight 40468 #checksum 3888 SEQUENCE /// ENTRY A70481 #type complete TITLE acetoin utilization protein - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A70481 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession A70481 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-310 ##label AQF !'##cross-references GB:AE000773; GB:AE000657; NID:g2984313; !1PIDN:AAC07842.1; PID:g2984320 !'##experimental_source strain VF5 GENETICS !$#gene acuC2 CLASSIFICATION #superfamily acetylpolyamine aminohydrolase; RPD3/acuC !1homology FEATURE !$6-303 #domain RPD3/acuC homology #label RAH1 SUMMARY #length 310 #molecular-weight 34829 #checksum 1189 SEQUENCE /// ENTRY H71071 #type complete TITLE hypothetical protein PH1267 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H71071 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession H71071 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-335 ##label KAW !'##cross-references GB:AP000005; NID:g3236132; PIDN:BAA30370.1; !1PID:g3257687 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1267 CLASSIFICATION #superfamily acetylpolyamine aminohydrolase; RPD3/acuC !1homology SUMMARY #length 335 #molecular-weight 37509 #checksum 3514 SEQUENCE /// ENTRY G64366 #type complete TITLE acetylpolyamine aminohydrolase - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G64366 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession G64366 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-343 ##label BUL !'##cross-references GB:U67502; GB:L77117; NID:g2826293; !1PIDN:AAB98526.1; PID:g1591238; TIGR:MJ0535 GENETICS !$#map_position REV471360-470329 !$#start_codon TTG CLASSIFICATION #superfamily acetylpolyamine aminohydrolase; RPD3/acuC !1homology FEATURE !$8-300 #domain RPD3/acuC homology #label RAH1 SUMMARY #length 343 #molecular-weight 38174 #checksum 7547 SEQUENCE /// ENTRY I40422 #type complete TITLE conserved hypothetical protein ysxC - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 19-Jan-2001 ACCESSIONS I40422; C69987; S45102 REFERENCE I40420 !$#authors Riethdorf, S.; Volker, U.; Gerth, U.; Winkler, A.; !1Engelmann, S.; Hecker, M. !$#journal J. Bacteriol. (1994) 176:6518-6527 !$#title Cloning, nucleotide sequence, and expression of the Bacillus !1subtilis lon gene. !$#cross-references MUID:95050209; PMID:7961402 !$#accession I40422 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-195 ##label RES !'##cross-references EMBL:X76424; NID:g496556; PIDN:CAA53985.1; !1PID:g496558 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69987 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-195 ##label KUN !'##cross-references GB:Z99118; GB:AL009126; NID:g2635200; !1PIDN:CAB14779.1; PID:g2635284 !'##experimental_source strain 168 GENETICS !$#gene ysxC CLASSIFICATION #superfamily Bacillus subtilis conserved hypothetical !1protein ysxC; translation elongation factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop FEATURE !$24-145 #domain translation elongation factor Tu homology !8#label ETU\ !$30-37 #region nucleotide-binding motif A (P-loop) SUMMARY #length 195 #molecular-weight 22026 #checksum 1749 SEQUENCE /// ENTRY E70456 #type complete TITLE conserved hypothetical protein aq_1815 - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 19-Jan-2001 ACCESSIONS E70456 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession E70456 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-183 ##label AQF !'##cross-references GB:AE000757; NID:g2984092; PIDN:AAC07648.1; !1PID:g2984110; GB:AE000657 !'##experimental_source strain VF5 GENETICS !$#gene aq_1815 CLASSIFICATION #superfamily Bacillus subtilis conserved hypothetical !1protein ysxC; translation elongation factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop FEATURE !$19-140 #domain translation elongation factor Tu homology !8#label ETU\ !$25-32 #region nucleotide-binding motif A (P-loop) SUMMARY #length 183 #molecular-weight 20862 #checksum 6073 SEQUENCE /// ENTRY A64237 #type complete TITLE hypothetical protein homolog MG335 - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 19-Jan-2001 ACCESSIONS A64237 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession A64237 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-191 ##label TIGR !'##cross-references GB:U39716; GB:L43967; NID:g1046037; PID:g1046039; !1TIGR:MG335 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily Bacillus subtilis conserved hypothetical !1protein ysxC; translation elongation factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop FEATURE !$21-139 #domain translation elongation factor Tu homology !8#label ETU\ !$27-34 #region nucleotide-binding motif A (P-loop)\ !$136-139 #region GTP-binding NKXD motif SUMMARY #length 191 #molecular-weight 21835 #checksum 5293 SEQUENCE /// ENTRY S73686 #type complete TITLE hypothetical protein yihA - Mycoplasma pneumoniae (strain ATCC 29342) ALTERNATE_NAMES hypothetical protein P01_orf193 ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 19-Jan-2001 ACCESSIONS S73686 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73686 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-193 ##label HIM !'##cross-references EMBL:AE000034; GB:U00089; NID:g1674031; !1PIDN:AAB96008.1; PID:g1674038 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#gene yihA !$#genetic_code SGC3 CLASSIFICATION #superfamily Bacillus subtilis conserved hypothetical !1protein ysxC; translation elongation factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop FEATURE !$21-139 #domain translation elongation factor Tu homology !8#label ETU\ !$27-34 #region nucleotide-binding motif A (P-loop)\ !$136-139 #region GTP-binding NKXD motif\ !$168-170 #region GTP-binding SAK/L motif SUMMARY #length 193 #molecular-weight 21818 #checksum 9610 SEQUENCE /// ENTRY G64715 #type complete TITLE conserved hypothetical ATP-binding protein HP1567 - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 19-Jan-2001 ACCESSIONS G64715 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession G64715 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-208 ##label TOM !'##cross-references GB:AE000654; GB:AE000511; NID:g2314743; !1PIDN:AAD08606.1; PID:g2314750; TIGR:HP1567 CLASSIFICATION #superfamily Bacillus subtilis conserved hypothetical !1protein ysxC; translation elongation factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop FEATURE !$25-157 #domain translation elongation factor Tu homology !8#label ETU\ !$31-38 #region nucleotide-binding motif A (P-loop) SUMMARY #length 208 #molecular-weight 23559 #checksum 3172 SEQUENCE /// ENTRY D71802 #type complete TITLE hypothetical protein jhp1475 - Helicobacter pylori (strain J99) ORGANISM #formal_name Helicobacter pylori #variety strain J99 DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 21-Jan-2000 ACCESSIONS D71802 REFERENCE A71800 !$#authors Alm, R.A.; Ling, L.S.L.; Moir, D.T.; King, B.L.; Brown, !1E.D.; Doig, P.C.; Smith, D.R.; Noonan, B.; Guild, B.C.; !1deJonge, B.L.; Carmel, G.; Tummino, P.J.; Caruso, A.; !1Uria-Nickelsen, M.; Mills, D.M.; Ives, C.; Gibson, R.; !1Merberg, D.; Mills, S.D.; Jiang, Q.; Taylor, D.E.; Vovis, !1G.F.; Trust, T.J. !$#journal Nature (1999) 397:176-180 !$#title Genomic sequence comparison of two unrelated isolates of the !1human gastric pathogen Helicobacter pylori. !$#cross-references MUID:99120557; PMID:9923682 !$#accession D71802 !'##status preliminary !'##molecule_type DNA !'##residues 1-208 ##label ARN !'##cross-references GB:AE001569; GB:AE001439; NID:g4156095; !1PIDN:AAD07059.1; PID:g4156107 !'##experimental_source strain J99 GENETICS !$#gene jhp1475 CLASSIFICATION #superfamily Bacillus subtilis conserved hypothetical !1protein ysxC; translation elongation factor Tu homology FEATURE !$25-157 #domain translation elongation factor Tu homology !8#label ETU SUMMARY #length 208 #molecular-weight 23597 #checksum 3874 SEQUENCE /// ENTRY S40810 #type complete TITLE hypothetical protein f199 - Escherichia coli (strain K-12) ALTERNATE_NAMES hypothetical protein b3865 ORGANISM #formal_name Escherichia coli DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 01-Mar-2002 ACCESSIONS S40810; D65191 REFERENCE S40802 !$#authors Plunkett III, G.; Burland, V.; Daniels, D.L.; Blattner, F.R. !$#journal Nucleic Acids Res. (1993) 21:3391-3398 !$#title Analysis of the Escherichia coli genome. III. DNA sequence !1of the region from 87.2 to 89.2 minutes. !$#cross-references MUID:93347969; PMID:8346018 !$#accession S40810 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-199 ##label PLU !'##cross-references EMBL:L19201; NID:g304961; PIDN:AAB02999.1; !1PID:g304970 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1993 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65191 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-199 ##label BLAT !'##cross-references GB:AE000462; GB:U00096; NID:g1790295; !1PIDN:AAC76862.1; PID:g1790296; UWGP:b3865 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily Bacillus subtilis conserved hypothetical !1protein ysxC; translation elongation factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop FEATURE !$16-137 #domain translation elongation factor Tu homology !8#label ETU\ !$22-29 #region nucleotide-binding motif A (P-loop) SUMMARY #length 199 #molecular-weight 22214 #checksum 629 SEQUENCE /// ENTRY D71719 #type complete TITLE hypothetical protein RP102 - Rickettsia prowazekii ORGANISM #formal_name Rickettsia prowazekii DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 19-Jan-2001 ACCESSIONS D71719 REFERENCE A71630 !$#authors Andersson, S.G.E.; Zomorodipour, A.; Andersson, J.O.; !1Sicheritz-Ponten, T.; Alsmark, U.C.M.; Podowski, R.M.; !1Naeslund, A.K.; Eriksson, A.S.; Winkler, H.H.; Kurland, C.G. !$#journal Nature (1998) 396:133-140 !$#title The genome sequence of Rickettsia prowazekii and the origin !1of mitochondria. !$#cross-references MUID:99039499; PMID:9823893 !$#accession D71719 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-214 ##label AND !'##cross-references GB:AJ235270; GB:AJ235269; NID:g3860572; !1PIDN:CAA14571.1; PID:g3860670; GSPDB:GN00081 !'##experimental_source strain Madrid E GENETICS !$#gene RP102 CLASSIFICATION #superfamily Bacillus subtilis conserved hypothetical !1protein ysxC; translation elongation factor Tu homology KEYWORDS GTP binding; nucleotide binding; P-loop FEATURE !$42-163 #domain translation elongation factor Tu homology !8#label ETU\ !$48-55 #region nucleotide-binding motif A (P-loop) SUMMARY #length 214 #molecular-weight 24424 #checksum 9332 SEQUENCE /// ENTRY B64200 #type complete TITLE heat shock protein dnaJ homolog MG002 - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 21-Jul-2000 ACCESSIONS B64200 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession B64200 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-310 ##label TIGR !'##cross-references GB:U39679; GB:L43967; NID:g3844619; !1PIDN:AAC71218.1; PID:g1045670; TIGR:MG002 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily Mycoplasma dnaJ homolog MG002; dnaJ !1amino-terminal homology KEYWORDS molecular chaperone FEATURE !$2-64 #domain dnaJ amino-terminal homology #label DNJ SUMMARY #length 310 #molecular-weight 37364 #checksum 8129 SEQUENCE /// ENTRY S62835 #type complete TITLE dnaJ protein homolog xdj1 - Mycoplasma pneumoniae (strain ATCC 29342) ALTERNATE_NAMES hypothetical protein K05_orf309 ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 10-Dec-1999 ACCESSIONS S62835; S73478 REFERENCE S62797 !$#authors Hilbert, H.; Himmelreich, R.; Plagens, H.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:628-639 !$#title Sequence analysis of 56 kb from the genome of the bacterium !1Mycoplasma pneumoniae comprising the dnaA region, the atp !1operon and a cluster of ribosomal protein genes. !$#cross-references MUID:96177562; PMID:8604303 !$#accession S62835 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-309 ##label HIL !'##cross-references EMBL:U34816; NID:g1209514; PIDN:AAC43644.1; !1PID:g1209516 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1995 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73478 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-309 ##label HIM !'##cross-references EMBL:AE000017; GB:U00089; NID:g1673812; !1PIDN:AAB95800.1; PID:g1673813 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#gene xdj1 !$#genetic_code SGC3 CLASSIFICATION #superfamily Mycoplasma dnaJ homolog MG002; dnaJ !1amino-terminal homology KEYWORDS molecular chaperone FEATURE !$2-64 #domain dnaJ amino-terminal homology #label DNJ SUMMARY #length 309 #molecular-weight 37132 #checksum 8284 SEQUENCE /// ENTRY C69502 #type complete TITLE hypothetical protein AF2020 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69502 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession C69502 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-191 ##label KLE !'##cross-references GB:AE000963; GB:AE000782; NID:g2689286; !1PIDN:AAB89241.1; PID:g2648523; TIGR:AF2020 CLASSIFICATION #superfamily Archaeoglobus hypothetical protein AF2020 SUMMARY #length 191 #molecular-weight 22252 #checksum 4812 SEQUENCE /// ENTRY H69266 #type complete TITLE hypothetical protein AF0136 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H69266 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession H69266 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-185 ##label KLE !'##cross-references GB:AE001097; GB:AE000782; NID:g2689420; !1PIDN:AAB91104.1; PID:g2650520; TIGR:AF0136 CLASSIFICATION #superfamily Archaeoglobus hypothetical protein AF2020 SUMMARY #length 185 #molecular-weight 22027 #checksum 2354 SEQUENCE /// ENTRY G69193 #type complete TITLE acetyl-CoA synthetase related protein - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69193 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession G69193 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-124 ##label MTH !'##cross-references GB:AE000849; GB:AE000666; NID:g2621780; !1PIDN:AAB85207.1; PID:g2621788 !'##experimental_source strain Delta H GENETICS !$#gene MTH702 CLASSIFICATION #superfamily Methanobacterium acetyl-CoA synthetase related !1protein; acetate-CoA ligase homology FEATURE !$1-112 #domain acetate-CoA ligase homology #status atypical !8#label ACL SUMMARY #length 124 #molecular-weight 14075 #checksum 8900 SEQUENCE /// ENTRY E64479 #type complete TITLE cobalamin (5'-phosphate) synthase - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E64479 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession E64479 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-258 ##label BUL !'##cross-references GB:U67584; GB:L77117; NID:g1592077; !1PIDN:AAB99447.1; PID:g1592086; TIGR:MJ1438 GENETICS !$#map_position FOR1405757-1406533 !$#start_codon TTG CLASSIFICATION #superfamily Methanococcus cobalamin (5'-phosphate) synthase SUMMARY #length 258 #molecular-weight 28777 #checksum 2678 SEQUENCE /// ENTRY B71145 #type complete TITLE probable cobalamin synthase - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B71145 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession B71145 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-230 ##label KAW !'##cross-references GB:AP000002; NID:g3236129; PIDN:BAA29447.1; !1PID:g3256764 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0373 CLASSIFICATION #superfamily Methanococcus cobalamin (5'-phosphate) synthase SUMMARY #length 230 #molecular-weight 25365 #checksum 4958 SEQUENCE /// ENTRY E69254 #type complete TITLE cobalamin (5'-phosphate) synthase (cobS-1) homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69254 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession E69254 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-265 ##label KLE !'##cross-references GB:AE001104; GB:AE000782; NID:g2689427; !1PIDN:AAB91192.1; PID:g2650615; TIGR:AF0037 CLASSIFICATION #superfamily Methanococcus cobalamin (5'-phosphate) synthase SUMMARY #length 265 #molecular-weight 29074 #checksum 5756 SEQUENCE /// ENTRY C69540 #type complete TITLE cobalamin (5'-phosphate) synthase (cobS-2) homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69540 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession C69540 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-231 ##label KLE !'##cross-references GB:AE000944; GB:AE000782; NID:g2689267; !1PIDN:AAB88933.1; PID:g2648196; TIGR:AF2323 CLASSIFICATION #superfamily Methanococcus cobalamin (5'-phosphate) synthase SUMMARY #length 231 #molecular-weight 25071 #checksum 2909 SEQUENCE /// ENTRY B64224 #type complete TITLE IgA-specific metalloendopeptidase (EC 3.4.24.13) type 1 precursor homolog - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 07-Dec-1999 ACCESSIONS B64224 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession B64224 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-148 ##label TIGR !'##cross-references GB:U39700; GB:L43967; NID:g1045906; PID:g1045907; !1TIGR:MG219 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily Mycoplasma metalloendopeptidase homolog KEYWORDS hydrolase; metalloproteinase SUMMARY #length 148 #molecular-weight 16616 #checksum 3418 SEQUENCE /// ENTRY C69880 #type complete TITLE conserved hypothetical protein ylqC - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69880 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69880 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-81 ##label KUN !'##cross-references GB:Z99112; GB:AL009126; NID:g2633902; !1PIDN:CAB13473.1; PID:g2633972 !'##experimental_source strain 168 GENETICS !$#gene ylqC CLASSIFICATION #superfamily Bacillus conserved hypothetical protein ylqC SUMMARY #length 81 #molecular-weight 9062 #checksum 8541 SEQUENCE /// ENTRY A70312 #type complete TITLE conserved hypothetical protein aq_124a - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A70312 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession A70312 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-79 ##label AQF !'##cross-references GB:AE000675; GB:AE000657; NID:g2982863; !1PIDN:AAC06503.1; PID:g2982883 !'##experimental_source strain VF5 GENETICS !$#gene aq_124a CLASSIFICATION #superfamily Bacillus conserved hypothetical protein ylqC SUMMARY #length 79 #molecular-weight 8747 #checksum 3655 SEQUENCE /// ENTRY G71267 #type complete TITLE conserved hypothetical protein TP0906 - syphilis spirochete ORGANISM #formal_name Treponema pallidum subsp. pallidum #common_name syphilis spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS G71267 REFERENCE A71250 !$#authors Fraser, C.M.; Norris, S.J.; Weinstock, G.M.; White, O.; !1Sutton, G.G.; Dodson, R.; Gwinn, M.; Hickey, E.K.; Clayton, !1R.; Ketchum, K.A.; Sodergren, E.; Hardham, J.M.; McLeod, !1M.P.; Salzberg, S.; Peterson, J.; Khalak, H.; Richardson, !1D.; Howell, J.K.; Chidambaram, M.; Utterback, T.; McDonald, !1L.; Artiach, P.; Bowman, C.; Cotton, M.D.; Fujii, C.; !1Garland, S.; Hatch, B.; Horst, K.; Roberts, K.; Watthey, L.; !1Weidman, J.; Smith, H.O.; Venter, J.C. !$#journal Science (1998) 281:375-388 !$#title Complete genome sequence of Treponema pallidum, the syphilis !1spirochete. !$#cross-references MUID:98332770; PMID:9665876 !$#accession G71267 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-80 ##label COL !'##cross-references GB:AE001259; GB:AE000520; NID:g3323209; !1PIDN:AAC65858.1; PID:g3323219 !'##experimental_source strain Nichols GENETICS !$#gene TP0906 CLASSIFICATION #superfamily Bacillus conserved hypothetical protein ylqC SUMMARY #length 80 #molecular-weight 8686 #checksum 5879 SEQUENCE /// ENTRY G70186 #type complete TITLE conserved hypothetical protein BB0696 - Lyme disease spirochete ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G70186 REFERENCE A70100 !$#authors Fraser, C.M.; Casjens, S.; Huang, W.M.; Sutton, G.G.; !1Clayton, R.; Lathigra, R.; White, O.; Ketchum, K.A.; Dodson, !1R.; Hickey, E.K.; Gwinn, M.; Dougherty, B.; Tomb, J.F.; !1Fleischmann, R.D.; Richardson, D.; Peterson, J.; Kerlavage, !1A.R.; Quackenbush, J.; Salzberg, S.; Hanson, M.; Vugt, R.V.; !1Palmer, N.; Adams, M.D.; Gocayne, J.; Weidman, J.; !1Utterback, T.; Watthey, L.; McDonald, L.; Artiach, P.; !1Bowman, C.; Garland, S.; Fujii, C.; Cotton, M.D.; Horst, K.; !1Roberts, K.; Hatch, B.; Smith, H.O.; Venter, J.C. !$#journal Nature (1997) 390:580-586 !$#title Genomic sequence of a Lyme disease spirochaete, Borrelia !1burgdorferi. !$#cross-references MUID:98065943; PMID:9403685 !$#accession G70186 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-82 ##label KLE !'##cross-references GB:AE001170; GB:AE000783; NID:g2688623; !1PIDN:AAC67047.1; PID:g2688632; TIGR:BB0696 !'##experimental_source strain B31 CLASSIFICATION #superfamily Bacillus conserved hypothetical protein ylqC SUMMARY #length 82 #molecular-weight 9253 #checksum 719 SEQUENCE /// ENTRY G70927 #type complete TITLE hypothetical protein Rv2908c - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G70927 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession G70927 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-80 ##label COL !'##cross-references GB:Z74024; GB:AL123456; NID:g3250700; !1PIDN:CAA98345.1; PID:g1403430 !'##experimental_source strain H37Rv GENETICS !$#gene Rv2908c CLASSIFICATION #superfamily Bacillus conserved hypothetical protein ylqC SUMMARY #length 80 #molecular-weight 8521 #checksum 8400 SEQUENCE /// ENTRY S76250 #type complete TITLE hypothetical protein slr0287 - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S76250 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76250 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-118 ##label KAN !'##cross-references EMBL:D90914; GB:AB001339; NID:g1653477; !1PIDN:BAA18509.1; PID:g1653596 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily Bacillus conserved hypothetical protein ylqC SUMMARY #length 118 #molecular-weight 13615 #checksum 6133 SEQUENCE /// ENTRY B64226 #type complete TITLE hypothetical protein MG237 - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 07-Dec-1999 ACCESSIONS B64226 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession B64226 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-294 ##label TIGR !'##cross-references GB:U39701; GB:L43967; NID:g1045915; PID:g1045926; !1TIGR:MG237 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily Mycoplasma hypothetical protein MG237 SUMMARY #length 294 #molecular-weight 34572 #checksum 2101 SEQUENCE /// ENTRY S73832 #type complete TITLE MG237 homolog F10_orf294 - Mycoplasma pneumoniae (strain ATCC 29342) ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 10-Dec-1999 ACCESSIONS S73832 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73832 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-294 ##label HIM !'##cross-references EMBL:AE000050; GB:U00089; NID:g1674197; !1PIDN:AAB96154.1; PID:g1674200 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily Mycoplasma hypothetical protein MG237 SUMMARY #length 294 #molecular-weight 34135 #checksum 7566 SEQUENCE /// ENTRY B64228 #type complete TITLE hypothetical protein MG255 - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 07-Dec-1999 ACCESSIONS B64228 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession B64228 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-365 ##label TIGR !'##cross-references GB:U39703; GB:L43967; NID:g1045933; PID:g1045946; !1TIGR:MG255 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily Mycoplasma hypothetical protein MG255 SUMMARY #length 365 #molecular-weight 42440 #checksum 1300 SEQUENCE /// ENTRY S73804 #type complete TITLE MG255 homolog H91_orf534 - Mycoplasma pneumoniae (strain ATCC 29342) ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 10-Dec-1999 ACCESSIONS S73804 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73804 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-534 ##label HIM !'##cross-references EMBL:AE000047; GB:U00089; NID:g1674162; !1PIDN:AAB96126.1; PID:g1674169 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily Mycoplasma hypothetical protein MG255 homolog SUMMARY #length 534 #molecular-weight 62643 #checksum 7867 SEQUENCE /// ENTRY B64234 #type complete TITLE hypothetical protein MG309 - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 07-Dec-1999 ACCESSIONS B64234 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession B64234 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-1225 ##label TIGR !'##cross-references GB:U39712; GB:L43967; NID:g1046005; PID:g1046009; !1TIGR:MG309 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily Mycoplasma hypothetical protein MG309 SUMMARY #length 1225 #molecular-weight 138375 #checksum 6138 SEQUENCE /// ENTRY S73723 #type complete TITLE probable lipoprotein H08_orf1325 - Mycoplasma pneumoniae (strain ATCC 29342) ALTERNATE_NAMES MG309 homolog H08_orf1325 ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 10-Dec-1999 ACCESSIONS S73723 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73723 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-1325 ##label HIM !'##cross-references EMBL:AE000038; GB:U00089; NID:g1674074; !1PIDN:AAB96045.1; PID:g1674079 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily Mycoplasma hypothetical protein MG309 SUMMARY #length 1325 #molecular-weight 146276 #checksum 4278 SEQUENCE /// ENTRY C69901 #type complete TITLE probable two-component sensor histidine kinase yocF - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69901 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69901 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-370 ##label KUN !'##cross-references GB:Z99114; GB:AL009126; NID:g2634230; !1PIDN:CAB13811.1; PID:g2634312 !'##experimental_source strain 168 GENETICS !$#gene yocF CLASSIFICATION #superfamily probable Bacillus subtilis two-component sensor !1histidine kinase yocF SUMMARY #length 370 #molecular-weight 42673 #checksum 4689 SEQUENCE /// ENTRY C70039 #type complete TITLE two-component sensor histidine kinase homolog yvfT - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C70039 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C70039 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-328 ##label KUN !'##cross-references GB:Z99121; GB:AL009126; NID:g2635827; !1PIDN:CAB15412.1; PID:g2635920 !'##experimental_source strain 168 GENETICS !$#gene yvfT CLASSIFICATION #superfamily probable Bacillus subtilis two-component sensor !1histidine kinase yocF SUMMARY #length 328 #molecular-weight 37362 #checksum 2554 SEQUENCE /// ENTRY B70080 #type complete TITLE two-component sensor histidine kinase homolog yxjM - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B70080 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B70080 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-406 ##label KUN !'##cross-references GB:Z99123; GB:AL009126; NID:g2636240; !1PIDN:CAB15916.1; PID:g2636425 !'##experimental_source strain 168 GENETICS !$#gene yxjM CLASSIFICATION #superfamily probable Bacillus subtilis two-component sensor !1histidine kinase yocF SUMMARY #length 406 #molecular-weight 45235 #checksum 2727 SEQUENCE /// ENTRY F69780 #type complete TITLE two-component sensor histidine kinase homolog ydfH - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F69780 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69780 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-407 ##label KUN !'##cross-references GB:Z99106; GB:AL009126; NID:g2632653; !1PIDN:CAB12348.1; PID:g2632841 !'##experimental_source strain 168 GENETICS !$#gene ydfH CLASSIFICATION #superfamily probable Bacillus subtilis two-component sensor !1histidine kinase yocF SUMMARY #length 407 #molecular-weight 46505 #checksum 7640 SEQUENCE /// ENTRY C69985 #type complete TITLE probable DNA-dependent DNA polymerase beta chain yshC - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69985 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69985 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-570 ##label KUN !'##cross-references GB:Z99118; GB:AL009126; NID:g2635200; !1PIDN:CAB14819.1; PID:g2635324 !'##experimental_source strain 168 GENETICS !$#gene yshC CLASSIFICATION #superfamily DNA-dependent DNA polymerase beta chain yshC SUMMARY #length 570 #molecular-weight 64119 #checksum 4226 SEQUENCE /// ENTRY F70423 #type complete TITLE DNA polymerase beta family - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F70423 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession F70423 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-581 ##label AQF !'##cross-references GB:AE000739; GB:AE000657; NID:g2983813; !1PIDN:AAC07374.1; PID:g2983818 !'##experimental_source strain VF5 GENETICS !$#gene dpbF CLASSIFICATION #superfamily DNA-dependent DNA polymerase beta chain yshC SUMMARY #length 581 #molecular-weight 66961 #checksum 8621 SEQUENCE /// ENTRY G69172 #type complete TITLE DNA-dependent DNA polymerase family X - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69172 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession G69172 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-550 ##label MTH !'##cross-references GB:AE000838; GB:AE000666; NID:g2621625; !1PIDN:AAB85056.1; PID:g2621626 !'##experimental_source strain Delta H GENETICS !$#gene MTH550 CLASSIFICATION #superfamily DNA-dependent DNA polymerase beta chain yshC SUMMARY #length 550 #molecular-weight 61309 #checksum 9697 SEQUENCE /// ENTRY G64005 #type complete TITLE hypothetical protein HI0304 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS G64005 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession G64005 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-186 ##label TIGR !'##cross-references GB:U32716; GB:L42023; NID:g1573268; !1PIDN:AAC21969.1; PID:g1573273; TIGR:HI0304 CLASSIFICATION #superfamily hypothetical protein HI0304 SUMMARY #length 186 #molecular-weight 20921 #checksum 8003 SEQUENCE /// ENTRY C65080 #type complete TITLE hypothetical protein b2948 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS C65080 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65080 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-211 ##label BLAT !'##cross-references GB:AE000377; GB:U00096; NID:g2367178; !1PIDN:AAC75985.1; PID:g1789317; UWGP:b2948 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily hypothetical protein HI0304 SUMMARY #length 211 #molecular-weight 23332 #checksum 7459 SEQUENCE /// ENTRY G64018 #type complete TITLE hypothetical protein HI1036 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS G64018 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession G64018 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-184 ##label TIGR !'##cross-references GB:U32784; GB:L42023; NID:g3212210; !1PIDN:AAC22696.1; PID:g1574069; TIGR:HI1036 CLASSIFICATION #superfamily hypothetical protein HI1036 SUMMARY #length 184 #molecular-weight 20534 #checksum 9340 SEQUENCE /// ENTRY G65080 #type complete TITLE probable resistance protein yggT [similarity] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS G65080 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65080 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-188 ##label BLAT !'##cross-references GB:AE000378; GB:U00096; NID:g1789319; !1PIDN:AAC75989.1; PID:g1789322; UWGP:b2952 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily hypothetical protein HI1036 SUMMARY #length 188 #molecular-weight 21167 #checksum 2895 SEQUENCE /// ENTRY G64144 #type complete TITLE hypothetical protein HI0177 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS G64144 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession G64144 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-262 ##label TIGR !'##cross-references GB:U32703; GB:L42023; NID:g1573133; !1PIDN:AAC21847.1; PID:g1573134; TIGR:HI0177 !'##note best homolog was a hypothetical protein from Pseudomonas !1aeruginosa CLASSIFICATION #superfamily conserved hypothetical protein HI0177 SUMMARY #length 262 #molecular-weight 29347 #checksum 3259 SEQUENCE /// ENTRY F65037 #type complete TITLE hypothetical protein b2595 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS F65037 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65037 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-245 ##label BLAT !'##cross-references GB:AE000346; GB:U00096; NID:g2367141; !1PIDN:AAC75644.1; PID:g1788947; UWGP:b2595 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily conserved hypothetical protein HI0177 SUMMARY #length 245 #molecular-weight 27829 #checksum 9264 SEQUENCE /// ENTRY S26603 #type complete TITLE hypothetical protein 341 - Pseudomonas aeruginosa ORGANISM #formal_name Pseudomonas aeruginosa DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S33676; S26603 REFERENCE S33673 !$#authors Hobbs, M.; Collie, E.S.R.; Free, P.D.; Livingston, S.P.; !1Mattick, J.S. !$#journal Mol. Microbiol. (1993) 7:669-682 !$#title PilS and PilR, a two-component transcriptional regulatory !1system controlling expression of type 4 fimbriae in !1Pseudomonas aeruginosa. !$#cross-references MUID:93225810; PMID:8097014 !$#accession S33676 !'##status preliminary !'##molecule_type DNA !'##residues 1-341 ##label HO2 !'##cross-references EMBL:Z12154; NID:g45399; PIDN:CAA78141.1; !1PID:g45403 CLASSIFICATION #superfamily conserved hypothetical protein HI0177 SUMMARY #length 341 #molecular-weight 38561 #checksum 8325 SEQUENCE /// ENTRY S71020 #type complete TITLE peptidoglycan-linked lipoprotein precursor - Neisseria gonorrhoeae ORGANISM #formal_name Neisseria gonorrhoeae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S71020 REFERENCE S71019 !$#authors Fussenegger, M.; Facius, D.; Meier, J.; Meyer, T.F. !$#journal Mol. Microbiol. (1996) 19:1095-1105 !$#title A novel peptidoglycan-linked lipoprotein (ComL) that !1functions in natural transformation competence of Neisseria !1gonorrhoeae. !$#cross-references MUID:96249702; PMID:8830266 !$#accession S71020 !'##status preliminary !'##molecule_type DNA !'##residues 1-267 ##label FUS !'##cross-references EMBL:Z49895; NID:g1107832; PIDN:CAA90076.1; !1PID:g1107833 GENETICS !$#gene comL CLASSIFICATION #superfamily conserved hypothetical protein HI0177 FEATURE !$1-17 #domain signal sequence #status predicted #label SIG\ !$18-267 #product peptidoglycan-linked lipoprotein #status !8predicted #label MAT SUMMARY #length 267 #molecular-weight 30839 #checksum 3639 SEQUENCE /// ENTRY G64157 #type complete TITLE probable organic solvent tolerance protein precursor HI0730 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS G64157 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession G64157 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-782 ##label TIGR !'##cross-references GB:U32756; GB:L42023; NID:g1573729; !1PIDN:AAC22389.1; PID:g1573734; TIGR:HI0730 CLASSIFICATION #superfamily organic solvent tolerance protein KEYWORDS periplasmic space FEATURE !$1-23 #domain signal sequence #status predicted #label SIG\ !$24-782 #product organic solvent tolerance protein #status !8predicted #label MAT SUMMARY #length 782 #molecular-weight 90083 #checksum 9100 SEQUENCE /// ENTRY F64726 #type complete TITLE organic solvent tolerance protein precursor - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS F64726 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F64726 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-784 ##label BLAT !'##cross-references GB:AE000115; GB:U00096; NID:g1786230; !1PIDN:AAC73165.1; PID:g1786239; UWGP:b0054 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene imp CLASSIFICATION #superfamily organic solvent tolerance protein KEYWORDS periplasmic space FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-784 #product organic solvent tolerance protein #status !8predicted #label MAT SUMMARY #length 784 #molecular-weight 89671 #checksum 5807 SEQUENCE /// ENTRY H70031 #type complete TITLE conserved hypothetical protein yvcJ - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H70031 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H70031 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-295 ##label KUN !'##cross-references GB:Z99121; GB:AL009126; NID:g2635827; !1PIDN:CAB15482.1; PID:g2635990 !'##experimental_source strain 168 GENETICS !$#gene yvcJ CLASSIFICATION #superfamily Bacillus subtilis conserved hypothetical !1protein yvcJ SUMMARY #length 295 #molecular-weight 33851 #checksum 8351 SEQUENCE /// ENTRY B70903 #type complete TITLE hypothetical protein Rv1421 - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B70903 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession B70903 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-301 ##label COL !'##cross-references GB:Z80108; GB:AL123456; NID:g3256012; !1PIDN:CAB02169.1; PID:g1542930 !'##experimental_source strain H37Rv GENETICS !$#gene Rv1421 CLASSIFICATION #superfamily Bacillus subtilis conserved hypothetical !1protein yvcJ SUMMARY #length 301 #molecular-weight 32912 #checksum 2069 SEQUENCE /// ENTRY G64167 #type complete TITLE hypothetical protein HI1146 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS G64167 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession G64167 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-289 ##label TIGR !'##cross-references GB:U32794; GB:L42023; NID:g1574694; !1PIDN:AAC22801.1; PID:g1574702; TIGR:HI1146 !'##note best homolog was a hypothetical protein from Escherichia coli GENETICS !$#start_codon GTG CLASSIFICATION #superfamily Bacillus subtilis conserved hypothetical !1protein yvcJ SUMMARY #length 289 #molecular-weight 32994 #checksum 2278 SEQUENCE /// ENTRY I76721 #type complete TITLE hypothetical protein b3205 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS I76721; G65111; S38618 REFERENCE I57054 !$#authors Jones, D.H.A.; Franklin, C.F.H.; Thomas, C.M. !$#journal Microbiology (1994) 140:1035-1043 !$#title Molecular analysis of the operon which encodes the RNA !1polymerase sigma factor sigma54 of Escherichia coli. !$#cross-references MUID:94297724; PMID:8025669 !$#accession I76721 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-284 ##label RES !'##cross-references EMBL:Z27094; NID:g414884; PID:g414888 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65111 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-284 ##label BLAT !'##cross-references GB:AE000400; GB:U00096; NID:g2367203; !1PIDN:AAC76237.1; PID:g1789598; UWGP:b3205 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily Bacillus subtilis conserved hypothetical !1protein yvcJ SUMMARY #length 284 #molecular-weight 32492 #checksum 9223 SEQUENCE /// ENTRY S60666 #type complete TITLE probable ATP-binding protein - Klebsiella pneumoniae ORGANISM #formal_name Klebsiella pneumoniae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S60666; S07662 REFERENCE S60666 !$#authors Merrick, M.J.; Taylor, M. !$#submission submitted to the EMBL Data Library, August 1995 !$#description Sequence and characterisation of distal genes in the !1Klebsiella pneumoniae rpoN operon. !$#accession S60666 !'##status preliminary !'##molecule_type DNA !'##residues 1-284 ##label MER !'##cross-references EMBL:Z50803; NID:g950054; PID:g950055 REFERENCE S07659 !$#authors Merrick, M.J.; Coppard, J.R. !$#journal Mol. Microbiol. (1989) 3:1765-1775 !$#title Mutations in genes downstream of the rpoN gene (encoding !1sigma54) of Klebsiella pneumoniae affect expression from !1sigma54-dependent promoters. !$#cross-references MUID:90158124; PMID:2695747 !$#accession S07662 !'##molecule_type DNA !'##residues 1-193 ##label ME2 !'##cross-references EMBL:X16335; NID:g43924; PIDN:CAA34393.1; !1PID:g43928 CLASSIFICATION #superfamily Bacillus subtilis conserved hypothetical !1protein yvcJ KEYWORDS nucleotide binding; P-loop FEATURE !$8-15 #region nucleotide-binding motif A (P-loop) SUMMARY #length 284 #molecular-weight 32523 #checksum 9698 SEQUENCE /// ENTRY H71053 #type complete TITLE hypothetical protein PH1127 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-Jan-2003 ACCESSIONS H71053 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession H71053 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-121 ##label KAW !'##cross-references GB:AP000005; NID:g3236132; PIDN:BAA30226.1; !1PID:g3257543 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1127 CLASSIFICATION #superfamily uncharacterized conserved protein SUMMARY #length 121 #molecular-weight 14277 #checksum 5157 SEQUENCE /// ENTRY A69441 #type complete TITLE conserved hypothetical protein AF1530 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-Jan-2003 ACCESSIONS A69441 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession A69441 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-119 ##label KLE !'##cross-references GB:AE000997; GB:AE000782; NID:g2689320; !1PIDN:AAB89718.1; PID:g2649034; TIGR:AF1530 CLASSIFICATION #superfamily uncharacterized conserved protein SUMMARY #length 119 #molecular-weight 14025 #checksum 9086 SEQUENCE /// ENTRY G64304 #type complete TITLE hypothetical protein MJ0039 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-Jan-2003 ACCESSIONS G64304 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession G64304 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-115 ##label BUL !'##cross-references GB:U67462; GB:L77117; NID:g1590835; !1PIDN:AAB98020.1; PID:g1590840; TIGR:MJ0039 GENETICS !$#map_position REV39998-39651 !$#start_codon TTG CLASSIFICATION #superfamily uncharacterized conserved protein SUMMARY #length 115 #molecular-weight 13389 #checksum 8128 SEQUENCE /// ENTRY A69043 #type complete TITLE conserved hypothetical protein MTH1324 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-Jan-2003 ACCESSIONS A69043 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession A69043 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-116 ##label MTH !'##cross-references GB:AE000896; GB:AE000666; NID:g2622424; !1PIDN:AAB85802.1; PID:g2622430 !'##experimental_source strain Delta H GENETICS !$#gene MTH1324 !$#start_codon GTG CLASSIFICATION #superfamily uncharacterized conserved protein SUMMARY #length 116 #molecular-weight 13479 #checksum 390 SEQUENCE /// ENTRY G64346 #type complete TITLE hypothetical protein MJ0375 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G64346 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession G64346 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-254 ##label BUL !'##cross-references GB:U67490; GB:L77117; NID:g2826276; !1PIDN:AAB98364.1; PID:g1591082; TIGR:MJ0375 GENETICS !$#map_position FOR339920-340684 CLASSIFICATION #superfamily conserved hypothetical protein MJ0375 SUMMARY #length 254 #molecular-weight 30184 #checksum 9106 SEQUENCE /// ENTRY A69012 #type complete TITLE conserved hypothetical protein MTH1091 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A69012 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession A69012 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-154 ##label MTH !'##cross-references GB:AE000879; GB:AE000666; NID:g2622175; !1PIDN:AAB85580.1; PID:g2622191 !'##experimental_source strain Delta H GENETICS !$#gene MTH1091 !$#start_codon GTG CLASSIFICATION #superfamily conserved hypothetical protein MJ0375 SUMMARY #length 154 #molecular-weight 18541 #checksum 7057 SEQUENCE /// ENTRY H69258 #type complete TITLE conserved hypothetical protein AF0072 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H69258 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession H69258 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-241 ##label KLE !'##cross-references GB:AE001101; GB:AE000782; NID:g2689424; !1PIDN:AAB91154.1; PID:g2650574; TIGR:AF0072 CLASSIFICATION #superfamily conserved hypothetical protein MJ0375 SUMMARY #length 241 #molecular-weight 27611 #checksum 8950 SEQUENCE /// ENTRY G71069 #type complete TITLE hypothetical protein PH1252 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G71069 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession G71069 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-267 ##label KAW !'##cross-references GB:AP000005; NID:g3236132; PIDN:BAA30353.1; !1PID:g3257670 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1252 CLASSIFICATION #superfamily conserved hypothetical protein MJ0375 SUMMARY #length 267 #molecular-weight 31522 #checksum 4465 SEQUENCE /// ENTRY C71142 #type complete TITLE hypothetical protein PH0350 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C71142 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession C71142 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-239 ##label KAW !'##cross-references GB:AP000002; NID:g3236129; PIDN:BAA29424.1; !1PID:g3256741 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0350 CLASSIFICATION #superfamily conserved hypothetical protein MJ0375 SUMMARY #length 239 #molecular-weight 27476 #checksum 9735 SEQUENCE /// ENTRY A64454 #type complete TITLE hypothetical protein MJ1234 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A64454 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession A64454 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-241 ##label BUL !'##cross-references GB:U67564; GB:L77117; NID:g1591863; !1PIDN:AAB99238.1; PID:g1591866; TIGR:MJ1234 GENETICS !$#map_position REV1178671-1177946 CLASSIFICATION #superfamily conserved hypothetical protein MJ0375 SUMMARY #length 241 #molecular-weight 28840 #checksum 4768 SEQUENCE /// ENTRY G71237 #type complete TITLE hypothetical protein PH0161 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G71237 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession G71237 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-242 ##label KAW !'##cross-references GB:AP000001; NID:g3236128; PIDN:BAA29230.1; !1PID:g3256547 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0161 CLASSIFICATION #superfamily conserved hypothetical protein MJ0375 SUMMARY #length 242 #molecular-weight 28715 #checksum 7346 SEQUENCE /// ENTRY G64370 #type complete TITLE conserved hypothetical protein MJ0567 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G64370 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession G64370 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-82 ##label BUL !'##cross-references GB:U67505; GB:L77117; NID:g2826297; !1PIDN:AAB98558.1; PID:g1591273; TIGR:MJ0567 GENETICS !$#map_position REV504744-504496 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0567 SUMMARY #length 82 #molecular-weight 8766 #checksum 827 SEQUENCE /// ENTRY E69549 #type complete TITLE conserved hypothetical protein AF2396 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69549 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession E69549 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-78 ##label KLE !'##cross-references GB:AE001111; GB:AE000782; NID:g2689434; !1PIDN:AAB91275.1; PID:g2650705; TIGR:AF2396 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0567 SUMMARY #length 78 #molecular-weight 7975 #checksum 3603 SEQUENCE /// ENTRY B64235 #type complete TITLE fibronectin-binding protein homolog - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 07-Dec-1999 ACCESSIONS B64235 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession B64235 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-280 ##label TIGR !'##cross-references GB:U39713; GB:L43967; NID:g1046014; PID:g1046019; !1TIGR:MG318 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily fibronectin-binding protein homolog KEYWORDS fibronectin binding SUMMARY #length 280 #molecular-weight 32150 #checksum 6569 SEQUENCE /// ENTRY A41461 #type complete TITLE fibronectin-binding protein homolog - Mycoplasma pneumoniae (strain ATCC 29342) ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 10-Dec-1999 ACCESSIONS A41461; S73714 REFERENCE A41461 !$#authors Dallo, S.F.; Chavoya, A.; Baseman, J.B. !$#journal Infect. Immun. (1990) 58:4163-4165 !$#title Characterization of the gene for a 30-kilodalton !1adhesin-related protein of Mycoplasma pneumoniae. !$#cross-references MUID:91071908; PMID:2123834 !$#accession A41461 !'##status not compared with conceptual translation !'##molecule_type DNA !'##residues 1-274 ##label DAL REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73714 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-274 ##label HIM !'##cross-references EMBL:AE000037; GB:U00089; NID:g1674065; !1PIDN:AAB96036.1; PID:g1674069 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily fibronectin-binding protein homolog SUMMARY #length 274 #molecular-weight 29741 #checksum 6372 SEQUENCE /// ENTRY B64239 #type complete TITLE hypothetical protein MG354 - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 07-Dec-1999 ACCESSIONS B64239 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession B64239 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-137 ##label TIGR !'##cross-references GB:U39719; GB:L43967; NID:g1046055; PID:g1046061; !1TIGR:MG354 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily Mycoplasma hypothetical protein MG354 SUMMARY #length 137 #molecular-weight 15704 #checksum 758 SEQUENCE /// ENTRY S73638 #type complete TITLE MG354 homolog G12_orf136 - Mycoplasma pneumoniae (strain ATCC 29342) ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 10-Dec-1999 ACCESSIONS S73638 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73638 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-136 ##label HIM !'##cross-references EMBL:AE000028; GB:U00089; NID:g1673972; !1PIDN:AAB95960.1; PID:g1673984 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily Mycoplasma hypothetical protein MG354 SUMMARY #length 136 #molecular-weight 15584 #checksum 7586 SEQUENCE /// ENTRY B64248 #type complete TITLE hypothetical protein MG436 - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 07-Dec-1999 ACCESSIONS B64248 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession B64248 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-118 ##label TIGR !'##cross-references GB:U39730; GB:L43967; NID:g1046149; !1PIDN:AAB01626.1; PID:g1046153; TIGR:MG436 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily Mycoplasma hypothetical protein MG436 SUMMARY #length 118 #molecular-weight 13628 #checksum 2230 SEQUENCE /// ENTRY B64201 #type complete TITLE hypothetical protein MG011 - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 07-Dec-1999 ACCESSIONS B64201 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession B64201 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-287 ##label TIGR !'##cross-references GB:U39679; GB:L43967; NID:g1045668; PID:g1045679; !1TIGR:MG011 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily ribosomal protein S6 modification protein rimK SUMMARY #length 287 #molecular-weight 33433 #checksum 7664 SEQUENCE /// ENTRY S73465 #type complete TITLE MG011 homolog D12_orf285 - Mycoplasma pneumoniae (strain ATCC 29342) ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 10-Dec-1999 ACCESSIONS S73465 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73465 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-285 ##label HIM !'##cross-references EMBL:AE000016; GB:U00089; NID:g1673796; !1PIDN:AAB95787.1; PID:g1673799 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily ribosomal protein S6 modification protein rimK SUMMARY #length 285 #molecular-weight 33446 #checksum 9183 SEQUENCE /// ENTRY S73464 #type complete TITLE ribosomal protein S6 modification protein rimK - Mycoplasma pneumoniae (strain ATCC 29342) ALTERNATE_NAMES hypothetical protein D12_orf288 ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 10-Dec-1999 ACCESSIONS S73464 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73464 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-288 ##label HIM !'##cross-references EMBL:AE000016; GB:U00089; NID:g1673796; !1PIDN:AAB95786.1; PID:g1673798 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#gene rimK !$#genetic_code SGC3 CLASSIFICATION #superfamily ribosomal protein S6 modification protein rimK SUMMARY #length 288 #molecular-weight 32435 #checksum 1069 SEQUENCE /// ENTRY C64201 #type complete TITLE ribosomal protein S6 modification protein rimK homolog - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 07-Dec-1999 ACCESSIONS C64201 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession C64201 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-225 ##label TIGR !'##cross-references GB:U39679; GB:L43967; NID:g1045668; PID:g1045680; !1TIGR:MG012 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily ribosomal protein S6 modification protein rimK SUMMARY #length 225 #molecular-weight 25659 #checksum 8244 SEQUENCE /// ENTRY G64371 #type complete TITLE conserved hypothetical protein MJ0575 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G64371 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession G64371 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-229 ##label BUL !'##cross-references GB:U67506; GB:L77117; NID:g1591274; !1PIDN:AAB98566.1; PID:g1591282; TIGR:MJ0575 GENETICS !$#map_position FOR511123-511812 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0575 SUMMARY #length 229 #molecular-weight 26218 #checksum 3544 SEQUENCE /// ENTRY F64404 #type complete TITLE hypothetical protein MJ0838 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F64404 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession F64404 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-223 ##label BUL !'##cross-references GB:U67528; GB:L77117; NID:g2826335; !1PIDN:AAB98843.1; PID:g1591525; TIGR:MJ0838 GENETICS !$#map_position FOR764150-764821 !$#start_codon GTG CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0575 SUMMARY #length 223 #molecular-weight 25837 #checksum 6921 SEQUENCE /// ENTRY C69047 #type complete TITLE conserved hypothetical protein MTH1356 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69047 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession C69047 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-215 ##label MTH !'##cross-references GB:AE000898; GB:AE000666; NID:g2622453; !1PIDN:AAB85833.1; PID:g2622463 !'##experimental_source strain Delta H GENETICS !$#gene MTH1356 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0575 SUMMARY #length 215 #molecular-weight 24078 #checksum 1788 SEQUENCE /// ENTRY F69460 #type complete TITLE conserved hypothetical protein AF1687 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F69460 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession F69460 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-215 ##label KLE !'##cross-references GB:AE000987; GB:AE000782; NID:g2689310; !1PIDN:AAB89562.1; PID:g2648868; TIGR:AF1687 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0575 SUMMARY #length 215 #molecular-weight 24150 #checksum 5451 SEQUENCE /// ENTRY G64400 #type complete TITLE conserved hypothetical protein MJ0807 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G64400 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession G64400 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-184 ##label BUL !'##cross-references GB:U67525; GB:L77117; NID:g2826325; !1PIDN:AAB98807.1; PID:g1591499; TIGR:MJ0807 GENETICS !$#map_position FOR730121-730675 !$#start_codon TTG CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0807 SUMMARY #length 184 #molecular-weight 21548 #checksum 2729 SEQUENCE /// ENTRY B69085 #type complete TITLE conserved hypothetical protein MTH1632 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69085 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession B69085 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-179 ##label MTH !'##cross-references GB:AE000922; GB:AE000666; NID:g2622754; !1PIDN:AAB86105.1; PID:g2622759 !'##experimental_source strain Delta H GENETICS !$#gene MTH1632 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0807 SUMMARY #length 179 #molecular-weight 20813 #checksum 2036 SEQUENCE /// ENTRY C69424 #type complete TITLE conserved hypothetical protein AF1396 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69424 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession C69424 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-162 ##label KLE !'##cross-references GB:AE001008; GB:AE000782; NID:g2689331; !1PIDN:AAB89851.1; PID:g2649178; TIGR:AF1396 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0807 SUMMARY #length 162 #molecular-weight 18949 #checksum 7496 SEQUENCE /// ENTRY G64387 #type complete TITLE hypothetical protein MJ0703 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G64387 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession G64387 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-226 ##label BUL !'##cross-references GB:U67516; GB:L77117; NID:g2826307; !1PIDN:AAB98695.1; PID:g1591418; TIGR:MJ0703 GENETICS !$#map_position FOR629861-630541 CLASSIFICATION #superfamily hypothetical protein MJ0703 SUMMARY #length 226 #molecular-weight 25067 #checksum 8037 SEQUENCE /// ENTRY A69189 #type complete TITLE phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase related protein - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A69189 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession A69189 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-227 ##label MTH !'##cross-references GB:AE000846; GB:AE000666; NID:g2621740; !1PIDN:AAB85174.1; PID:g2621752 !'##experimental_source strain Delta H GENETICS !$#gene MTH669 CLASSIFICATION #superfamily hypothetical protein MJ0703 SUMMARY #length 227 #molecular-weight 24965 #checksum 7816 SEQUENCE /// ENTRY G64453 #type complete TITLE conserved hypothetical protein MJ1232 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G64453 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession G64453 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-296 ##label BUL !'##cross-references GB:U67564; GB:L77117; NID:g1591863; !1PIDN:AAB99237.1; PID:g1591864; TIGR:MJ1232 GENETICS !$#map_position REV1176336-1175446 CLASSIFICATION #superfamily conserved hypothetical protein MJ1232; CBS !1homology FEATURE !$239-287 #domain CBS homology #label CBS SUMMARY #length 296 #molecular-weight 33204 #checksum 1969 SEQUENCE /// ENTRY S75379 #type complete TITLE MJ1232 protein homolog c04012 - Sulfolobus solfataricus ORGANISM #formal_name Sulfolobus solfataricus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S75379 REFERENCE S73076 !$#authors Sensen, C.W.; Klenk, H.P.; Singh, R.K.; Allard, G.; Chan, !1C.C.Y.; Liu, Q.Y.; Penny, S.L.; Young, F.; Schenk, M.E.; !1Gaasterland, T.; Doolittle, W.F.; Ragan, M.A.; Charlebois, !1R.L. !$#journal Mol. Microbiol. (1996) 22:175-191 !$#title Organizational characteristics and information content of an !1archaeal genome: 156 kb of sequence from Sulfolobus !1solfataricus P2. !$#cross-references MUID:97055432; PMID:8899719 !$#accession S75379 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-300 ##label SEN !'##cross-references EMBL:Y08257; NID:g1707772; PID:g1707784 !'##experimental_source strain P2 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1September 1996 CLASSIFICATION #superfamily conserved hypothetical protein MJ1232; CBS !1homology FEATURE !$244-292 #domain CBS homology #label CBS SUMMARY #length 300 #molecular-weight 33521 #checksum 9488 SEQUENCE /// ENTRY D69035 #type complete TITLE MJ1232 protein homolog MTH126 - Methanobacterium thermoautotrophicum (strain Delta H) ALTERNATE_NAMES inosine-5'-monophosphate dehydrogenase related protein VII [misnomer] ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69035 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession D69035 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-302 ##label MTH !'##cross-references GB:AE000802; GB:AE000666; NID:g2621163; !1PIDN:AAB84632.1; PID:g2621166 !'##experimental_source strain Delta H GENETICS !$#gene MTH126 !$#start_codon TTG CLASSIFICATION #superfamily conserved hypothetical protein MJ1232; CBS !1homology FEATURE !$189-236 #domain CBS homology #label CBS SUMMARY #length 302 #molecular-weight 32403 #checksum 481 SEQUENCE /// ENTRY G69263 #type complete TITLE MJ1232 protein homolog AF0111 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69263 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession G69263 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-299 ##label KLE !'##cross-references GB:AE001099; GB:AE000782; NID:g2689422; !1PIDN:AAB91120.1; PID:g2650538; TIGR:AF0111 CLASSIFICATION #superfamily conserved hypothetical protein MJ1232; CBS !1homology FEATURE !$246-294 #domain CBS homology #label CBS SUMMARY #length 299 #molecular-weight 32510 #checksum 745 SEQUENCE /// ENTRY G64456 #type complete TITLE conserved hypothetical protein MJ1256 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G64456 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession G64456 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-311 ##label BUL !'##cross-references GB:U67566; GB:L77117; NID:g1591887; !1PIDN:AAB99260.1; PID:g1591890; TIGR:MJ1256 GENETICS !$#map_position FOR1198613-1199548 !$#start_codon GTG CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ1256 SUMMARY #length 311 #molecular-weight 34599 #checksum 8655 SEQUENCE /// ENTRY E69364 #type complete TITLE conserved hypothetical protein AF0917 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69364 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession E69364 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-296 ##label KLE !'##cross-references GB:AE001040; GB:AE000782; NID:g2689363; !1PIDN:AAB90320.1; PID:g2649679; TIGR:AF0917 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ1256 SUMMARY #length 296 #molecular-weight 33087 #checksum 9613 SEQUENCE /// ENTRY F70977 #type complete TITLE hypothetical protein Rv3261 - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F70977 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession F70977 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-331 ##label COL !'##cross-references GB:Z92771; GB:AL123456; NID:g3242259; !1PIDN:CAB07094.1; PID:g1877316 !'##experimental_source strain H37Rv GENETICS !$#gene Rv3261 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ1256 SUMMARY #length 331 #molecular-weight 35335 #checksum 3099 SEQUENCE /// ENTRY G69002 #type complete TITLE conserved hypothetical protein MTH1018 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69002 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession G69002 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-306 ##label MTH !'##cross-references GB:AE000874; GB:AE000666; NID:g2622110; !1PIDN:AAB85514.1; PID:g2622120 !'##experimental_source strain Delta H GENETICS !$#gene MTH1018 !$#start_codon GTG CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ1256 SUMMARY #length 306 #molecular-weight 33492 #checksum 9315 SEQUENCE /// ENTRY G64472 #type complete TITLE hypothetical protein MJ1384 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G64472 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession G64472 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-198 ##label BUL !'##cross-references GB:U67578; GB:L77117; NID:g2826403; !1PIDN:AAB99394.1; PID:g1592030; TIGR:MJ1384 GENETICS !$#map_position REV1333191-1332595 !$#start_codon TTG CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum !1NADPH-oxidoreductase SUMMARY #length 198 #molecular-weight 22403 #checksum 7798 SEQUENCE /// ENTRY E69021 #type complete TITLE conserved hypothetical protein MTH116 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69021 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession E69021 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-247 ##label MTH !'##cross-references GB:AE000801; GB:AE000666; NID:g2621145; !1PIDN:AAB84622.1; PID:g2621155 !'##experimental_source strain Delta H GENETICS !$#gene MTH116 CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum !1NADPH-oxidoreductase SUMMARY #length 247 #molecular-weight 28229 #checksum 7061 SEQUENCE /// ENTRY B69278 #type complete TITLE NADH oxidase (noxC) homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69278 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession B69278 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-172 ##label KLE !'##cross-references GB:AE001090; GB:AE000782; NID:g2689413; !1PIDN:AAB91006.1; PID:g2650415; TIGR:AF0226 CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum !1NADPH-oxidoreductase SUMMARY #length 172 #molecular-weight 19342 #checksum 6334 SEQUENCE /// ENTRY C69533 #type complete TITLE NAD(P)H-flavin oxidoreductase homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69533 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession C69533 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-174 ##label KLE !'##cross-references GB:AE000948; GB:AE000782; NID:g2689271; !1PIDN:AAB88993.1; PID:g2648259; TIGR:AF2267 CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum !1NADPH-oxidoreductase SUMMARY #length 174 #molecular-weight 20098 #checksum 4376 SEQUENCE /// ENTRY B69027 #type complete TITLE NADPH-oxidoreductase - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69027 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession B69027 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-191 ##label MTH !'##cross-references GB:AE000801; GB:AE000666; NID:g2621145; !1PIDN:AAB84626.1; PID:g2621159 !'##experimental_source strain Delta H GENETICS !$#gene MTH120 CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum !1NADPH-oxidoreductase SUMMARY #length 191 #molecular-weight 21687 #checksum 2897 SEQUENCE /// ENTRY D69425 #type complete TITLE conserved hypothetical protein AF1405 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69425 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession D69425 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-154 ##label KLE !'##cross-references GB:AE001007; GB:AE000782; NID:g2689330; !1PIDN:AAB89845.1; PID:g2649170; TIGR:AF1405 CLASSIFICATION #superfamily conserved hypothetical protein AF1405 SUMMARY #length 154 #molecular-weight 17352 #checksum 2486 SEQUENCE /// ENTRY G64478 #type complete TITLE hypothetical protein YER007c-a homolog - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G64478 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession G64478 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-162 ##label BUL !'##cross-references GB:U67584; GB:L77117; NID:g1592077; !1PIDN:AAB99442.1; PID:g1592081; TIGR:MJ1432 GENETICS !$#map_position FOR1402425-1402913 !$#start_codon TTG CLASSIFICATION #superfamily conserved hypothetical protein AF1405 SUMMARY #length 162 #molecular-weight 18365 #checksum 1855 SEQUENCE /// ENTRY E69186 #type complete TITLE conserved hypothetical protein MTH650 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69186 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession E69186 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-160 ##label MTH !'##cross-references GB:AE000845; GB:AE000666; NID:g2621726; !1PIDN:AAB85155.1; PID:g2621732 !'##experimental_source strain Delta H GENETICS !$#gene MTH650 !$#start_codon GTG CLASSIFICATION #superfamily conserved hypothetical protein AF1405 SUMMARY #length 160 #molecular-weight 17830 #checksum 1550 SEQUENCE /// ENTRY G71120 #type complete TITLE hypothetical protein PH0734 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G71120 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession G71120 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-175 ##label KAW !'##cross-references GB:AP000003; NID:g3236130; PIDN:BAA29825.1; !1PID:g3257142 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0734 CLASSIFICATION #superfamily conserved hypothetical protein AF1405 SUMMARY #length 175 #molecular-weight 20035 #checksum 3786 SEQUENCE /// ENTRY S53543 #type complete TITLE hypothetical protein YER007c-a - yeast (Saccharomyces cerevisiae) ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S53543 REFERENCE S50433 !$#authors Dietrich, F.S. !$#submission submitted to the EMBL Data Library, December 1994 !$#description The sequence of S. cerevisiae cosmids 9537, 9581, 9495, !19867, and lambda clone 5898. !$#accession S53543 !'##molecule_type DNA !'##residues 1-181 ##label DIE !'##cross-references EMBL:U18778; NID:g603592; PID:g1877417; !1GSPDB:GN00005; MIPS:YER007c-a GENETICS !$#gene MIPS:YER007c-a !'##cross-references SGD:S0002957 !$#map_position 5R CLASSIFICATION #superfamily conserved hypothetical protein AF1405 SUMMARY #length 181 #molecular-weight 20277 #checksum 7111 SEQUENCE /// ENTRY G64493 #type complete TITLE hypothetical protein homolog MJ1552 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS G64493 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession G64493 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-142 ##label BUL !'##cross-references GB:U67596; GB:L77117; NID:g1592181; PID:g1592182; !1TIGR:MJ1552; PID:g1511553 GENETICS !$#map_position FOR1528322-1528750 !$#start_codon TTG CLASSIFICATION #superfamily conserved hypothetical protein MJ1552 SUMMARY #length 142 #molecular-weight 16521 #checksum 1382 SEQUENCE /// ENTRY B69552 #type complete TITLE conserved hypothetical protein AF2417 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69552 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession B69552 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-122 ##label KLE !'##cross-references GB:AE001108; GB:AE000782; NID:g2689431; !1PIDN:AAB91245.1; PID:g2650672; TIGR:AF2417 CLASSIFICATION #superfamily conserved hypothetical protein MJ1552 SUMMARY #length 122 #molecular-weight 14282 #checksum 6037 SEQUENCE /// ENTRY A69053 #type complete TITLE conserved hypothetical protein MTH1398 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A69053 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession A69053 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-133 ##label MTH !'##cross-references GB:AE000902; GB:AE000666; NID:g2622500; !1PIDN:AAB85875.1; PID:g2622509 !'##experimental_source strain Delta H GENETICS !$#gene MTH1398 CLASSIFICATION #superfamily conserved hypothetical protein MJ1552 SUMMARY #length 133 #molecular-weight 15223 #checksum 4427 SEQUENCE /// ENTRY D71113 #type complete TITLE hypothetical protein PH0675 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D71113 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession D71113 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-134 ##label KAW !'##cross-references GB:AP000003; NID:g3236130; PIDN:BAA29766.1; !1PID:g3257083 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0675 CLASSIFICATION #superfamily conserved hypothetical protein MJ1552 SUMMARY #length 134 #molecular-weight 15603 #checksum 6664 SEQUENCE /// ENTRY C69411 #type complete TITLE conserved hypothetical protein AF1292 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69411 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession C69411 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-136 ##label KLE !'##cross-references GB:AE001015; GB:AE000782; NID:g2689338; !1PIDN:AAB89963.1; PID:g2649296; TIGR:AF1292 CLASSIFICATION #superfamily conserved hypothetical protein MJ1552 SUMMARY #length 136 #molecular-weight 15113 #checksum 9963 SEQUENCE /// ENTRY D69285 #type complete TITLE conserved hypothetical protein AF0284 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69285 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession D69285 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-165 ##label KLE !'##cross-references GB:AE001085; GB:AE000782; NID:g2689408; !1PIDN:AAB90949.1; PID:g2650352; TIGR:AF0284 CLASSIFICATION #superfamily conserved hypothetical protein MJ1552 SUMMARY #length 165 #molecular-weight 18736 #checksum 3349 SEQUENCE /// ENTRY F69370 #type complete TITLE conserved hypothetical protein AF0966 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F69370 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession F69370 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-176 ##label KLE !'##cross-references GB:AE001038; GB:AE000782; NID:g2689361; !1PIDN:AAB90277.1; PID:g2649633; TIGR:AF0966 CLASSIFICATION #superfamily conserved hypothetical protein MJ1552 SUMMARY #length 176 #molecular-weight 19685 #checksum 8476 SEQUENCE /// ENTRY E69304 #type complete TITLE conserved hypothetical protein AF0437 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69304 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession E69304 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-131 ##label KLE !'##cross-references GB:AE001074; GB:AE000782; NID:g2689397; !1PIDN:AAB90796.1; PID:g2650188; TIGR:AF0437 CLASSIFICATION #superfamily conserved hypothetical protein MJ1552 SUMMARY #length 131 #molecular-weight 15003 #checksum 2614 SEQUENCE /// ENTRY E69370 #type complete TITLE conserved hypothetical protein AF0965 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69370 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession E69370 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-154 ##label KLE !'##cross-references GB:AE001038; GB:AE000782; NID:g2689361; !1PIDN:AAB90278.1; PID:g2649634; TIGR:AF0965 CLASSIFICATION #superfamily conserved hypothetical protein MJ1552 SUMMARY #length 154 #molecular-weight 17754 #checksum 7801 SEQUENCE /// ENTRY C69275 #type complete TITLE conserved hypothetical protein AF0203 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69275 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession C69275 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-149 ##label KLE !'##cross-references GB:AE001092; GB:AE000782; NID:g2689415; !1PIDN:AAB91034.1; PID:g2650445; TIGR:AF0203 CLASSIFICATION #superfamily conserved hypothetical protein MJ1552 SUMMARY #length 149 #molecular-weight 17114 #checksum 7545 SEQUENCE /// ENTRY D69266 #type complete TITLE conserved hypothetical protein AF0132 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69266 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession D69266 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-157 ##label KLE !'##cross-references GB:AE001097; GB:AE000782; NID:g2689420; !1PIDN:AAB91097.1; PID:g2650513; TIGR:AF0132 CLASSIFICATION #superfamily conserved hypothetical protein MJ1552 SUMMARY #length 157 #molecular-weight 17346 #checksum 1662 SEQUENCE /// ENTRY C69252 #type complete TITLE conserved hypothetical protein AF0019 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69252 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession C69252 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-160 ##label KLE !'##cross-references GB:AE001105; GB:AE000782; NID:g2689428; !1PIDN:AAB91207.1; PID:g2650631; TIGR:AF0019 CLASSIFICATION #superfamily conserved hypothetical protein MJ1552 SUMMARY #length 160 #molecular-weight 18362 #checksum 4101 SEQUENCE /// ENTRY G64509 #type complete TITLE conserved hypothetical protein MJ1681 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G64509 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession G64509 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-380 ##label BUL !'##cross-references GB:U67608; GB:L77117; NID:g1592245; !1PIDN:AAB99702.1; PID:g1592248; TIGR:MJ1681 GENETICS !$#map_position REV1664002-1662860 !$#start_codon GTG CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ1681; ferredoxin 2[4Fe-4S] homology FEATURE !$289-344 #domain ferredoxin 2[4Fe-4S] homology #label FER SUMMARY #length 380 #molecular-weight 42580 #checksum 8871 SEQUENCE /// ENTRY B69092 #type complete TITLE conserved hypothetical protein MTH1684 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69092 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession B69092 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-431 ##label MTH !'##cross-references GB:AE000926; GB:AE000666; NID:g2622806; !1PIDN:AAB86156.1; PID:g2622814 !'##experimental_source strain Delta H GENETICS !$#gene MTH1684 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ1681; ferredoxin 2[4Fe-4S] homology FEATURE !$338-389 #domain ferredoxin 2[4Fe-4S] homology #label FER SUMMARY #length 431 #molecular-weight 46950 #checksum 7186 SEQUENCE /// ENTRY G64591 #type complete TITLE conserved hypothetical membrane protein HP0575 - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS G64591 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession G64591 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-232 ##label TOM !'##cross-references GB:AE000571; GB:AE000511; NID:g2313686; !1PIDN:AAD07642.1; PID:g2313694; TIGR:HP0575 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily conserved hypothetical membrane protein HP0575 SUMMARY #length 232 #molecular-weight 26063 #checksum 5183 SEQUENCE /// ENTRY G70459 #type complete TITLE conserved hypothetical protein aq_1853 - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G70459 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession G70459 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-217 ##label AQF !'##cross-references GB:AE000759; GB:AE000657; NID:g2984125; !1PIDN:AAC07673.1; PID:g2984137 !'##experimental_source strain VF5 GENETICS !$#gene aq_1853 CLASSIFICATION #superfamily conserved hypothetical membrane protein HP0575 SUMMARY #length 217 #molecular-weight 24137 #checksum 9995 SEQUENCE /// ENTRY D70057 #type complete TITLE conserved hypothetical protein ywhC - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D70057 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D70057 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-219 ##label KUN !'##cross-references GB:Z99123; GB:AL009126; NID:g2636240; !1PIDN:CAB15780.1; PID:g2636289 !'##experimental_source strain 168 GENETICS !$#gene ywhC CLASSIFICATION #superfamily conserved hypothetical membrane protein HP0575 SUMMARY #length 219 #molecular-weight 24703 #checksum 6792 SEQUENCE /// ENTRY F64705 #type complete TITLE conserved hypothetical integral membrane protein HP1486 - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS F64705 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession F64705 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-376 ##label TOM !'##cross-references GB:AE000647; GB:AE000511; NID:g2314645; !1PIDN:AAD08521.1; PID:g2314658; TIGR:HP1486 CLASSIFICATION #superfamily conserved hypothetical integral membrane !1protein HP1486 SUMMARY #length 376 #molecular-weight 42545 #checksum 4936 SEQUENCE /// ENTRY G64705 #type complete TITLE conserved hypothetical integral membrane protein HP1487 - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Jun-2000 ACCESSIONS G64705 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession G64705 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-365 ##label TOM !'##cross-references GB:AE000647; GB:AE000511; NID:g2314645; !1PIDN:AAD08522.1; PID:g2314659; TIGR:HP1487 GENETICS !$#start_codon TTG CLASSIFICATION #superfamily conserved hypothetical integral membrane !1protein HP1486 SUMMARY #length 365 #molecular-weight 41089 #checksum 7998 SEQUENCE /// ENTRY G64890 #type complete TITLE Phenylacetic acid degradation protein paaI - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS G64890 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64890 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-140 ##label BLAT !'##cross-references GB:AE000236; GB:U00096; NID:g1787652; !1PIDN:AAC74478.1; PID:g1787662; UWGP:b1396 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily hypothetical protein b1396 SUMMARY #length 140 #molecular-weight 14851 #checksum 5012 SEQUENCE /// ENTRY H69532 #type complete TITLE conserved hypothetical protein AF2264 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H69532 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession H69532 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-154 ##label KLE !'##cross-references GB:AE000948; GB:AE000782; NID:g2689271; !1PIDN:AAB88986.1; PID:g2648253; TIGR:AF2264 CLASSIFICATION #superfamily hypothetical protein b1396 SUMMARY #length 154 #molecular-weight 17124 #checksum 432 SEQUENCE /// ENTRY C69873 #type complete TITLE glutaminase homolog ylaM - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69873 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69873 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-309 ##label KUN !'##cross-references GB:Z99111; GB:AL009126; NID:g2633699; !1PIDN:CAB13356.1; PID:g2633854 !'##experimental_source strain 168 GENETICS !$#gene ylaM CLASSIFICATION #superfamily Escherichia coli glutaminase homolog yneH SUMMARY #length 309 #molecular-weight 34012 #checksum 2520 SEQUENCE /// ENTRY D69751 #type complete TITLE glutaminase homolog ybgJ - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69751 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D69751 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-327 ##label KUN !'##cross-references GB:Z99105; GB:AL009126; NID:g2632457; !1PIDN:CAB12037.1; PID:g2632529 !'##experimental_source strain 168 GENETICS !$#gene ybgJ CLASSIFICATION #superfamily Escherichia coli glutaminase homolog yneH SUMMARY #length 327 #molecular-weight 36186 #checksum 4195 SEQUENCE /// ENTRY G64906 #type complete TITLE glutaminase homolog yneH - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS G64906 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64906 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-308 ##label BLAT !'##cross-references GB:AE000250; GB:U00096; NID:g1787801; !1PIDN:AAC74597.1; PID:g1787804; UWGP:b1524 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yneH CLASSIFICATION #superfamily Escherichia coli glutaminase homolog yneH SUMMARY #length 308 #molecular-weight 33515 #checksum 9276 SEQUENCE /// ENTRY D64779 #type complete TITLE probable membrane protein ybaS - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS D64779 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64779 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-310 ##label BLAT !'##cross-references GB:AE000155; GB:U00096; NID:g1786692; !1PIDN:AAC73587.1; PID:g1786693; UWGP:b0485 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ybaS CLASSIFICATION #superfamily Escherichia coli glutaminase homolog yneH KEYWORDS transmembrane protein FEATURE !$30-46 #domain transmembrane #status predicted #label TM1\ !$262-278 #domain transmembrane #status predicted #label TM2 SUMMARY #length 310 #molecular-weight 32903 #checksum 947 SEQUENCE /// ENTRY S75105 #type complete TITLE hypothetical protein slr2079 - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S75105 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75105 !'##status preliminary !'##molecule_type DNA !'##residues 1-327 ##label KAN !'##cross-references EMBL:D90910; GB:AB001339; NID:g1652956; !1PIDN:BAA17967.1; PID:g1653050 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily Escherichia coli glutaminase homolog yneH SUMMARY #length 327 #molecular-weight 36040 #checksum 6023 SEQUENCE /// ENTRY G65129 #type complete TITLE hypothetical protein b3356 - Escherichia coli (strain K-12) ALTERNATE_NAMES 14K hypothetical protein (crp region) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS G65129; S19719; S17106 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65129 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-134 ##label BLAT !'##cross-references GB:AE000411; GB:U00096; NID:g2367213; !1PIDN:AAC76381.1; PID:g1789755; UWGP:b3356 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S19719 !$#authors Bhasin, R.; Freundlich, M. !$#journal Biochim. Biophys. Acta (1991) 1129:109-111 !$#title The nucleotide sequence of the Escherichia coli crp !1divergent RNA and an overlapping ORF. !$#cross-references MUID:92096448; PMID:1756168 !$#accession S19719 !'##status preliminary !'##molecule_type DNA !'##residues 1-76,'ADT',80-134 ##label BHA !'##cross-references EMBL:X61919; NID:g48974; PIDN:CAA43921.1; !1PID:g48975 CLASSIFICATION #superfamily Escherichia coli hypothetical protein b3356 SUMMARY #length 134 #molecular-weight 14517 #checksum 4366 SEQUENCE /// ENTRY E70434 #type complete TITLE conserved hypothetical protein aq_1549 - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E70434 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession E70434 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-132 ##label AQF !'##cross-references GB:AE000745; GB:AE000657; NID:g2983907; !1PIDN:AAC07473.1; PID:g2983923 !'##experimental_source strain VF5 GENETICS !$#gene aq_1549 CLASSIFICATION #superfamily Escherichia coli hypothetical protein b3356 SUMMARY #length 132 #molecular-weight 15012 #checksum 4608 SEQUENCE /// ENTRY H71021 #type complete TITLE hypothetical protein PH1469 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H71021 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession H71021 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-148 ##label KAW !'##cross-references GB:AP000006; NID:g3236133; PIDN:BAA30576.1; !1PID:g3257893 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1469 CLASSIFICATION #superfamily Escherichia coli hypothetical protein b3356 SUMMARY #length 148 #molecular-weight 16690 #checksum 7979 SEQUENCE /// ENTRY G69048 #type complete TITLE conserved hypothetical protein MTH1367 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69048 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession G69048 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-61 ##label MTH !'##cross-references GB:AE000899; GB:AE000666; NID:g2622468; !1PIDN:AAB85844.1; PID:g2622475 !'##experimental_source strain Delta H GENETICS !$#gene MTH1367 !$#start_codon GTG CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum conserved !1hypothetical protein MTH1367 SUMMARY #length 61 #molecular-weight 6915 #checksum 7090 SEQUENCE /// ENTRY G69219 #type complete TITLE hypothetical protein MTH896 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69219 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession G69219 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-69 ##label MTH !'##cross-references GB:AE000865; GB:AE000666; NID:g2621984; !1PIDN:AAB85394.1; PID:g2621991 !'##experimental_source strain Delta H GENETICS !$#gene MTH896 CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum conserved !1hypothetical protein MTH1367 SUMMARY #length 69 #molecular-weight 7812 #checksum 9111 SEQUENCE /// ENTRY G69097 #type complete TITLE citrate synthase I - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69097 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession G69097 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-312 ##label MTH !'##cross-references GB:AE000929; GB:AE000666; NID:g2622853; !1PIDN:AAB86196.1; PID:g2622857 !'##experimental_source strain Delta H GENETICS !$#gene MTH1726 !$#start_codon GTG CLASSIFICATION #superfamily Aquifex aeolicus citrate synthase SUMMARY #length 312 #molecular-weight 35046 #checksum 5707 SEQUENCE /// ENTRY B70314 #type complete TITLE citrate synthase - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B70314 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession B70314 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-259 ##label AQF !'##cross-references GB:AE000675; GB:AE000657; NID:g2982863; !1PIDN:AAC06486.1; PID:g2982866 !'##experimental_source strain VF5 GENETICS !$#gene gltA CLASSIFICATION #superfamily Aquifex aeolicus citrate synthase SUMMARY #length 259 #molecular-weight 29075 #checksum 1076 SEQUENCE /// ENTRY G69110 #type complete TITLE conserved hypothetical protein MTH1823 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69110 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession G69110 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-146 ##label MTH !'##cross-references GB:AE000935; GB:AE000666; NID:g2622945; !1PIDN:AAB86289.1; PID:g2622956 !'##experimental_source strain Delta H GENETICS !$#gene MTH1823 !$#start_codon GTG CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum conserved !1hypothetical protein MTH1823; histidine triad homology SUMMARY #length 146 #molecular-weight 17717 #checksum 3583 SEQUENCE /// ENTRY E69231 #type complete TITLE conserved hypothetical protein MTH982 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69231 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession E69231 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-163 ##label MTH !'##cross-references GB:AE000871; GB:AE000666; NID:g2622069; !1PIDN:AAB85478.1; PID:g2622081 !'##experimental_source strain Delta H GENETICS !$#gene MTH982 !$#start_codon GTG CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum conserved !1hypothetical protein MTH1823; histidine triad homology SUMMARY #length 163 #molecular-weight 19202 #checksum 4939 SEQUENCE /// ENTRY D71092 #type complete TITLE hypothetical protein PH1001 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D71092 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession D71092 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-150 ##label KAW !'##cross-references GB:AP000004; NID:g3236131; PIDN:BAA30098.1; !1PID:g3257415 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1001 CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum conserved !1hypothetical protein MTH1823; histidine triad homology FEATURE !$3-99 #domain histidine triad homology #label HIT SUMMARY #length 150 #molecular-weight 17091 #checksum 9716 SEQUENCE /// ENTRY B69144 #type complete TITLE rhamnosyl transferase - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69144 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession B69144 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-328 ##label MTH !'##cross-references GB:AE000819; GB:AE000666; NID:g2621396; !1PIDN:AAB84849.1; PID:g2621400 !'##experimental_source strain Delta H GENETICS !$#gene MTH343 !$#start_codon TTG CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum rhamnosyl !1transferase SUMMARY #length 328 #molecular-weight 37533 #checksum 9300 SEQUENCE /// ENTRY A71153 #type complete TITLE hypothetical protein PH0424 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A71153 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession A71153 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-348 ##label KAW !'##cross-references GB:AP000002; NID:g3236129; PIDN:BAA29510.1; !1PID:g3256827 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0424 CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum rhamnosyl !1transferase SUMMARY #length 348 #molecular-weight 40467 #checksum 764 SEQUENCE /// ENTRY G69144 #type complete TITLE conserved hypothetical protein MTH348 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69144 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession G69144 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-313 ##label MTH !'##cross-references GB:AE000820; GB:AE000666; NID:g2621405; !1PIDN:AAB84854.1; PID:g2621406 !'##experimental_source strain Delta H GENETICS !$#gene MTH348 CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum rhamnosyl !1transferase SUMMARY #length 313 #molecular-weight 36308 #checksum 9971 SEQUENCE /// ENTRY B70696 #type complete TITLE probable rfbE protein - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B70696 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession B70696 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-304 ##label COL !'##cross-references GB:Z80343; GB:AL123456; NID:g3261648; !1PIDN:CAB02461.1; PID:g1552865 !'##experimental_source strain H37Rv GENETICS !$#gene rfbE CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum rhamnosyl !1transferase SUMMARY #length 304 #molecular-weight 33864 #checksum 6804 SEQUENCE /// ENTRY B69290 #type complete TITLE rhamnosyl transferase (rfbQ) homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69290 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession B69290 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-286 ##label KLE !'##cross-references GB:AE001082; GB:AE000782; NID:g2689405; !1PIDN:AAB90912.1; PID:g2650313; TIGR:AF0322 CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum rhamnosyl !1transferase SUMMARY #length 286 #molecular-weight 32859 #checksum 3222 SEQUENCE /// ENTRY G69160 #type complete TITLE conserved hypothetical protein MTH464 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69160 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession G69160 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-153 ##label MTH !'##cross-references GB:AE000830; GB:AE000666; NID:g2621523; !1PIDN:AAB84970.1; PID:g2621532 !'##experimental_source strain Delta H GENETICS !$#gene MTH464 !$#start_codon GTG CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum conserved !1hypothetical protein MTH464 SUMMARY #length 153 #molecular-weight 18207 #checksum 1860 SEQUENCE /// ENTRY B69153 #type complete TITLE hypothetical protein MTH408 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69153 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession B69153 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-139 ##label MTH !'##cross-references GB:AE000825; GB:AE000666; NID:g2621465; !1PIDN:AAB84914.1; PID:g2621471 !'##experimental_source strain Delta H GENETICS !$#gene MTH408 CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum conserved !1hypothetical protein MTH464 SUMMARY #length 139 #molecular-weight 16098 #checksum 273 SEQUENCE /// ENTRY C71157 #type complete TITLE hypothetical protein PH0458 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C71157 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession C71157 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-129 ##label KAW !'##cross-references GB:AP000002; NID:g3236129; PIDN:BAA29544.1; !1PID:g3256861 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0458 CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum conserved !1hypothetical protein MTH464 SUMMARY #length 129 #molecular-weight 15368 #checksum 2299 SEQUENCE /// ENTRY G69201 #type complete TITLE conserved hypothetical protein MTH761 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69201 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession G69201 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-383 ##label MTH !'##cross-references GB:AE000854; GB:AE000666; NID:g2621839; !1PIDN:AAB85264.1; PID:g2621850 !'##experimental_source strain Delta H GENETICS !$#gene MTH761 CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum conserved !1hypothetical protein MTH761 SUMMARY #length 383 #molecular-weight 40890 #checksum 6196 SEQUENCE /// ENTRY D69442 #type complete TITLE conserved hypothetical protein AF1541 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69442 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession D69442 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-372 ##label KLE !'##cross-references GB:AE000996; GB:AE000782; NID:g2689319; !1PIDN:AAB89705.1; PID:g2649020; TIGR:AF1541 CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum conserved !1hypothetical protein MTH761 SUMMARY #length 372 #molecular-weight 40069 #checksum 2800 SEQUENCE /// ENTRY E70729 #type complete TITLE hypothetical protein Rv2265 - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E70729 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession E70729 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-409 ##label COL !'##cross-references GB:Z77163; GB:AL123456; NID:g3261610; !1PIDN:CAB00970.1; PID:g1449355 !'##experimental_source strain H37Rv GENETICS !$#gene Rv2265 CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum conserved !1hypothetical protein MTH761 SUMMARY #length 409 #molecular-weight 41890 #checksum 5457 SEQUENCE /// ENTRY G71118 #type complete TITLE hypothetical protein PH0718 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G71118 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession G71118 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-398 ##label KAW !'##cross-references GB:AP000003; NID:g3236130; PIDN:BAA29809.1; !1PID:g3257126 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0718 CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum conserved !1hypothetical protein MTH761 SUMMARY #length 398 #molecular-weight 43975 #checksum 5620 SEQUENCE /// ENTRY D64464 #type complete TITLE hypothetical protein MJ1317 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D64464 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession D64464 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-398 ##label BUL !'##cross-references GB:U67571; GB:L77117; NID:g1591939; !1PIDN:AAB99324.1; PID:g1591956; TIGR:MJ1317 GENETICS !$#map_position REV1263017-1261821 CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum conserved !1hypothetical protein MTH761 SUMMARY #length 398 #molecular-weight 44096 #checksum 7102 SEQUENCE /// ENTRY G69206 #type complete TITLE hypothetical protein MTH80 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69206 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession G69206 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-81 ##label MTH !'##cross-references GB:AE000799; GB:AE000666; NID:g2621112; !1PIDN:AAB84586.1; PID:g2621117 !'##experimental_source strain Delta H GENETICS !$#gene MTH80 !$#start_codon TTG CLASSIFICATION #superfamily Methanobacterium hypothetical protein MTH80 SUMMARY #length 81 #molecular-weight 9420 #checksum 6259 SEQUENCE /// ENTRY H69198 #type complete TITLE hypothetical protein MTH74 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H69198 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession H69198 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-91 ##label MTH !'##cross-references GB:AE000666; NID:g2621094; PIDN:AAB84578.1; !1PID:g2621108 !'##experimental_source strain Delta H GENETICS !$#gene MTH74 CLASSIFICATION #superfamily Methanobacterium hypothetical protein MTH80 SUMMARY #length 91 #molecular-weight 10684 #checksum 486 SEQUENCE /// ENTRY A69265 #type complete TITLE conserved hypothetical protein AF0121 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A69265 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession A69265 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-255 ##label KLE !'##cross-references GB:AE001098; GB:AE000782; NID:g2689421; !1PIDN:AAB91109.1; PID:g2650526; TIGR:AF0121 CLASSIFICATION #superfamily conserved hypothetical protein AF0119 SUMMARY #length 255 #molecular-weight 28974 #checksum 7579 SEQUENCE /// ENTRY B69265 #type complete TITLE conserved hypothetical protein AF0122 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69265 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession B69265 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-210 ##label KLE !'##cross-references GB:AE001098; GB:AE000782; NID:g2689421; !1PIDN:AAB91117.1; PID:g2650532; TIGR:AF0122 CLASSIFICATION #superfamily conserved hypothetical protein AF0119 SUMMARY #length 210 #molecular-weight 24129 #checksum 6006 SEQUENCE /// ENTRY B69272 #type complete TITLE conserved hypothetical protein AF0178 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B69272 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession B69272 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-320 ##label KLE !'##cross-references GB:AE001093; GB:AE000782; NID:g2689416; !1PIDN:AAB91043.1; PID:g2650455; TIGR:AF0178 CLASSIFICATION #superfamily conserved hypothetical protein AF0119 SUMMARY #length 320 #molecular-weight 37301 #checksum 6049 SEQUENCE /// ENTRY G69259 #type complete TITLE hypothetical protein AF0079 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69259 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession G69259 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-431 ##label KLE !'##cross-references GB:AE001101; GB:AE000782; NID:g2689424; !1PIDN:AAB91157.1; PID:g2650577; TIGR:AF0079 CLASSIFICATION #superfamily conserved hypothetical protein AF0119 SUMMARY #length 431 #molecular-weight 48728 #checksum 7580 SEQUENCE /// ENTRY H69332 #type complete TITLE conserved hypothetical protein AF0664 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H69332 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession H69332 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-402 ##label KLE !'##cross-references GB:AE001059; GB:AE000782; NID:g2689382; !1PIDN:AAB90577.1; PID:g2649955; TIGR:AF0664 CLASSIFICATION #superfamily conserved hypothetical protein AF0119 SUMMARY #length 402 #molecular-weight 43887 #checksum 5612 SEQUENCE /// ENTRY G70333 #type complete TITLE hypothetical protein aq_377 - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G70333 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession G70333 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-111 ##label AQF !'##cross-references GB:AE000687; GB:AE000657; NID:g2983050; !1PIDN:AAC06660.1; PID:g2983052 !'##experimental_source strain VF5 GENETICS !$#gene aq_377 CLASSIFICATION #superfamily Aquifex aeolicus hypothetical protein aq_377 SUMMARY #length 111 #molecular-weight 12574 #checksum 8608 SEQUENCE /// ENTRY G69482 #type complete TITLE hypothetical protein AF1864 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69482 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession G69482 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-104 ##label KLE !'##cross-references GB:AE000974; GB:AE000782; NID:g2689297; !1PIDN:AAB89396.1; PID:g2648689; TIGR:AF1864 CLASSIFICATION #superfamily Aquifex aeolicus hypothetical protein aq_377 SUMMARY #length 104 #molecular-weight 11845 #checksum 1537 SEQUENCE /// ENTRY G69522 #type complete TITLE hypothetical protein AF2183 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69522 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession G69522 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-217 ##label KLE !'##cross-references GB:AE000954; GB:AE000782; NID:g2689277; !1PIDN:AAB89075.1; PID:g2648348; TIGR:AF2183 CLASSIFICATION #superfamily Archaeoglobus fulgidus hypothetical protein !1AF2183 SUMMARY #length 217 #molecular-weight 23660 #checksum 3062 SEQUENCE /// ENTRY E69389 #type complete TITLE hypothetical protein AF1118 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69389 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession E69389 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-178 ##label KLE !'##cross-references GB:AE001027; GB:AE000782; NID:g2689350; !1PIDN:AAB90141.1; PID:g2649487; TIGR:AF1118 CLASSIFICATION #superfamily Archaeoglobus fulgidus hypothetical protein !1AF2183 SUMMARY #length 178 #molecular-weight 19319 #checksum 3185 SEQUENCE /// ENTRY D69256 #type complete TITLE hypothetical protein AF0052 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69256 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession D69256 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-158 ##label KLE !'##cross-references GB:AE001102; GB:AE000782; NID:g2689425; !1PIDN:AAB91174.1; PID:g2650595; TIGR:AF0052 CLASSIFICATION #superfamily Archaeoglobus fulgidus hypothetical protein !1AF2183 SUMMARY #length 158 #molecular-weight 17369 #checksum 270 SEQUENCE /// ENTRY G69614 #type complete TITLE diacylglycerol kinase dgkA - Bacillus subtilis ALTERNATE_NAMES hypothetical protein (cdd 5' region) ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69614; PE0002; S04424 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69614 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-114 ##label KUN !'##cross-references GB:Z99116; GB:Z99117; GB:AL009126; NID:g2634966; !1PID:g2634977; NID:g2634723; PID:g2634963 !'##experimental_source strain 168 REFERENCE JE0022 !$#authors Song, B.H.; Neuhard, J. !$#journal Mol. Gen. Genet. (1989) 216:462-468 !$#title Chromosomal location, cloning and nucleotide sequence of the !1Bacillus subtilis cdd gene encoding cytidine/deoxycytidine !1deaminase. !$#cross-references MUID:89313687; PMID:2526291 !$#accession PE0002 !'##molecule_type DNA !'##residues 3-114 ##label SON !'##cross-references GB:X17430; NID:g39831; PIDN:CAB57857.1; !1PID:g6018366 GENETICS !$#gene dgkA !$#map_position 225 (degrees) CLASSIFICATION #superfamily Bacillus subtilis diacylglycerol kinase dgkA KEYWORDS transmembrane protein SUMMARY #length 114 #molecular-weight 12544 #checksum 3685 SEQUENCE /// ENTRY A36933 #type complete TITLE diacylglycerol kinase homolog - Streptococcus mutans ORGANISM #formal_name Streptococcus mutans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A36933 REFERENCE A36933 !$#authors Yamashita, Y.; Takehara, T.; Kuramitsu, H.K. !$#journal J. Bacteriol. (1993) 175:6220-6228 !$#title Molecular characterization of a STreptococcus mutans mutant !1altered in environmental stress responses. !$#cross-references MUID:94012483; PMID:8407794 !$#contents GS5 !$#accession A36933 !'##status preliminary !'##molecule_type DNA !'##residues 1-137 ##label YAM !'##note sequence extracted from NCBI backbone (NCBIN:138054, !1NCBIP:138056) CLASSIFICATION #superfamily Bacillus subtilis diacylglycerol kinase dgkA SUMMARY #length 137 #molecular-weight 15364 #checksum 8516 SEQUENCE /// ENTRY S74361 #type complete TITLE diacylglycerol kinase dgkA - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES hypothetical protein slr0054 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S74361 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74361 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-175 ##label KAN !'##cross-references EMBL:D64001; GB:AB001339; NID:g1001102; !1PID:g1001137 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene dgkA CLASSIFICATION #superfamily Bacillus subtilis diacylglycerol kinase dgkA SUMMARY #length 175 #molecular-weight 18247 #checksum 5527 SEQUENCE /// ENTRY E64062 #type complete TITLE diacylglycerol kinase homolog HI0335 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS E64062 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession E64062 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-118 ##label TIGR !'##cross-references GB:U32718; GB:L42023; NID:g1573299; !1PIDN:AAC21997.1; PID:g1573304; TIGR:HI0335 CLASSIFICATION #superfamily Bacillus subtilis diacylglycerol kinase dgkA SUMMARY #length 118 #molecular-weight 13025 #checksum 8423 SEQUENCE /// ENTRY KIECDG #type complete TITLE probable diacylglycerol kinase (EC 2.7.1.107) - Escherichia coli (strain K-12) ALTERNATE_NAMES diglyceride kinase ORGANISM #formal_name Escherichia coli DATE 17-May-1985 #sequence_revision 17-May-1985 #text_change 21-Jun-2002 ACCESSIONS A00667; A65212 REFERENCE A92393 !$#authors Lightner, V.A.; Bell, R.M.; Modrich, P. !$#journal J. Biol. Chem. (1983) 258:10856-10861 !$#title The DNA sequences encoding plsB and dgk loci of Escherichia !1coli. !$#cross-references MUID:83291031; PMID:6309817 !$#accession A00667 !'##molecule_type DNA !'##residues 1-122 ##label LIG !'##cross-references GB:K00127; NID:g147293; PIDN:AAA24394.1; !1PID:g457112 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65212 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-122 ##label BLAT !'##cross-references GB:AE000477; GB:U00096; NID:g2367338; !1PIDN:AAC77012.1; PID:g1790475; UWGP:b4042 !'##experimental_source strain K-12, substrain MG1655 COMMENT The size of this polypeptide is consistent with that of !1diacylglycerol kinase, and the map position of the gene that !1codes for this polypeptide coincides with dgkA loci !1determined by genetic analysis. However, direct evidence for !1positive identification of the protein is not yet available. GENETICS !$#gene dgkA !$#map_position 92 min CLASSIFICATION #superfamily Bacillus subtilis diacylglycerol kinase dgkA KEYWORDS phosphotransferase; transmembrane protein SUMMARY #length 122 #molecular-weight 13245 #checksum 2245 SEQUENCE /// ENTRY G69782 #type complete TITLE conserved hypothetical protein ydgE - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS G69782 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69782 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-157 ##label KUN !'##cross-references GB:Z99106; GB:Z99107; GB:AL009126; NID:g2632866; !1PID:g2632873; NID:g2632653; PID:g2632860 !'##experimental_source strain 168 GENETICS !$#gene ydgE CLASSIFICATION #superfamily Bacillus subtilis conserved hypothetical !1protein ydgE SUMMARY #length 157 #molecular-weight 18374 #checksum 1913 SEQUENCE /// ENTRY B70090 #type complete TITLE conserved hypothetical protein yycN - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B70090 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B70090 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-156 ##label KUN !'##cross-references GB:Z99124; GB:AL009126; NID:g2636442; !1PIDN:CAB16066.1; PID:g2636576 !'##experimental_source strain 168 GENETICS !$#gene yycN CLASSIFICATION #superfamily Bacillus subtilis conserved hypothetical !1protein ydgE SUMMARY #length 156 #molecular-weight 18165 #checksum 9941 SEQUENCE /// ENTRY S76652 #type complete TITLE hypothetical protein - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S76652 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76652 !'##status preliminary !'##molecule_type DNA !'##residues 1-204 ##label KAN !'##cross-references EMBL:D64004; GB:AB001339; NID:g1001701; !1PID:g1001758 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily Bacillus subtilis conserved hypothetical !1protein ydgE SUMMARY #length 204 #molecular-weight 23376 #checksum 2663 SEQUENCE /// ENTRY C69883 #type complete TITLE ribonucleoprotein homolog ymaA - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C69883 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69883 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-130 ##label KUN !'##cross-references GB:Z99113; GB:AL009126; NID:g2634090; !1PIDN:CAB13621.1; PID:g2634121 !'##experimental_source strain 168 GENETICS !$#gene ymaA CLASSIFICATION #superfamily Bacillus subtilis conserved hypothetical !1protein yosM SUMMARY #length 130 #molecular-weight 14603 #checksum 6312 SEQUENCE /// ENTRY S70890 #type complete TITLE hypothetical protein b2674 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS S70890; C65047 REFERENCE S70890 !$#authors Jordan, A.; Aragall, E.; Gibert, I.; Barbe, J. !$#journal Mol. Microbiol. (1996) 19:777-790 !$#title Promoter identification and expression analysis of !1Salmonella typhimurium and Escherichia coli nrdEF operons !1encoding one of two class I ribonucleotide reductases !1present in both bacteria. !$#cross-references MUID:96417857; PMID:8820648 !$#accession S70890 !'##status preliminary; translation not shown !'##molecule_type DNA !'##residues 1-136 ##label JOR !'##cross-references EMBL:X79787; NID:g1050468; PIDN:CAA56185.1; !1PID:g1050471 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C65047 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-136 ##label BLAT !'##cross-references GB:AE000352; GB:U00096; NID:g1789024; !1PIDN:AAC75721.1; PID:g1789029; UWGP:b2674 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily Bacillus subtilis conserved hypothetical !1protein yosM SUMMARY #length 136 #molecular-weight 15340 #checksum 1196 SEQUENCE /// ENTRY E70648 #type complete TITLE probable nrdI protein - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E70648 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession E70648 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-150 ##label COL !'##cross-references GB:Z83866; GB:AL123456; NID:g3261691; !1PIDN:CAB06244.1; PID:g1781162 !'##experimental_source strain H37Rv GENETICS !$#gene nrdI CLASSIFICATION #superfamily Bacillus subtilis conserved hypothetical !1protein yosM SUMMARY #length 150 #molecular-weight 16491 #checksum 4038 SEQUENCE /// ENTRY S73839 #type complete TITLE MG230 homolog F10_orf153 - Mycoplasma pneumoniae (strain ATCC 29342) ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S73839 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73839 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-153 ##label HIM !'##cross-references EMBL:AE000050; GB:U00089; NID:g1674197; !1PIDN:AAB96161.1; PID:g1674207 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily Bacillus subtilis conserved hypothetical !1protein yosM SUMMARY #length 153 #molecular-weight 17150 #checksum 1097 SEQUENCE /// ENTRY D64225 #type complete TITLE hypothetical protein MG230 - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 07-Dec-1999 ACCESSIONS D64225 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession D64225 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-153 ##label TIGR !'##cross-references GB:U39701; GB:L43967; NID:g1045915; PID:g1045919; !1TIGR:MG230 !'##experimental_source strain G-37 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily Bacillus subtilis conserved hypothetical !1protein yosM SUMMARY #length 153 #molecular-weight 17203 #checksum 1979 SEQUENCE /// ENTRY H70344 #type complete TITLE 6-phosphogluconate dehydrogenase - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H70344 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession H70344 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-300 ##label AQF !'##cross-references GB:AE000692; GB:AE000657; NID:g2983130; !1PIDN:AAC06739.1; PID:g2983136 !'##experimental_source strain VF5 GENETICS !$#gene gnd CLASSIFICATION #superfamily Aquifex aeolicus 6-phosphogluconate !1dehydrogenase; 3-hydroxyisobutyrate dehydrogenase homology FEATURE !$4-268 #domain 3-hydroxyisobutyrate dehydrogenase homology !8#label HIB SUMMARY #length 300 #molecular-weight 34191 #checksum 8330 SEQUENCE /// ENTRY G69950 #type complete TITLE 6-phosphogluconate dehydrogenase (pentose) homolog yqeC - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69950 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69950 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-297 ##label KUN !'##cross-references GB:Z99117; GB:AL009126; NID:g2634966; !1PIDN:CAB14514.1; PID:g2635018 !'##experimental_source strain 168 GENETICS !$#gene yqeC CLASSIFICATION #superfamily Aquifex aeolicus 6-phosphogluconate !1dehydrogenase; 3-hydroxyisobutyrate dehydrogenase homology FEATURE !$3-266 #domain 3-hydroxyisobutyrate dehydrogenase homology !8#label HIB SUMMARY #length 297 #molecular-weight 32769 #checksum 1271 SEQUENCE /// ENTRY S70988 #type complete TITLE gnd protein - Mycobacterium smegmatis ORGANISM #formal_name Mycobacterium smegmatis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S70988 REFERENCE S70980 !$#authors Salazar, L.; Fsihi, H.; de Rossi, E.; Riccardi, G.; Rios, !1C.; Cole, S.T.; Takiff, H.E. !$#journal Mol. Microbiol. (1996) 20:283-293 !$#title Organization of the origins of replication of the !1chromosomes of Mycobacterium smegmatis, Mycobacterium leprae !1and Mycobacterium tuberculosis and isolation of a functional !1origin from M. smegmatis. !$#cross-references MUID:96310367; PMID:8733228 !$#accession S70988 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-297 ##label SAL !'##cross-references EMBL:X92503; NID:g1321891; PIDN:CAA63250.1; !1PID:g1321895 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1995 GENETICS !$#gene gnd CLASSIFICATION #superfamily Aquifex aeolicus 6-phosphogluconate !1dehydrogenase; 3-hydroxyisobutyrate dehydrogenase homology FEATURE !$3-262 #domain 3-hydroxyisobutyrate dehydrogenase homology !8#label HIB SUMMARY #length 297 #molecular-weight 31536 #checksum 8531 SEQUENCE /// ENTRY C70538 #type complete TITLE probable 6-phosphogluconate dehydrogenase - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C70538 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession C70538 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-340 ##label COL !'##cross-references GB:Z95585; GB:AL123456; NID:g3261787; !1PIDN:CAB09054.1; PID:g2117216 !'##experimental_source strain H37Rv GENETICS !$#gene gnd2 CLASSIFICATION #superfamily Aquifex aeolicus 6-phosphogluconate !1dehydrogenase; 3-hydroxyisobutyrate dehydrogenase homology FEATURE !$3-308 #domain 3-hydroxyisobutyrate dehydrogenase homology !8#label HIB SUMMARY #length 340 #molecular-weight 36358 #checksum 4217 SEQUENCE /// ENTRY G69952 #type complete TITLE conserved hypothetical protein yqeY - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69952 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69952 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-148 ##label KUN !'##cross-references GB:Z99117; GB:AL009126; NID:g2634966; !1PIDN:CAB14482.1; PID:g2634986 !'##experimental_source strain 168 GENETICS !$#gene yqeY CLASSIFICATION #superfamily Bacillus subtilis conserved hypothetical !1protein yqeY SUMMARY #length 148 #molecular-weight 16766 #checksum 7432 SEQUENCE /// ENTRY S70830 #type complete TITLE hypothetical protein 1 - Myxococcus xanthus ORGANISM #formal_name Myxococcus xanthus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S70830 REFERENCE S70829 !$#authors Davis, J.M.; Mayor, J.; Plamann, L. !$#journal Mol. Microbiol. (1995) 18:943-952 !$#title A missense mutation in rpoD results in an A-signalling !1defect in Myxococcus xanthus. !$#cross-references MUID:96422481; PMID:8825098 !$#accession S70830 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-175 ##label DAV !'##cross-references EMBL:U20669; NID:g710339; PIDN:AAB60206.1; !1PID:g710341 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1February 1995 CLASSIFICATION #superfamily Bacillus subtilis conserved hypothetical !1protein yqeY SUMMARY #length 175 #molecular-weight 18549 #checksum 2374 SEQUENCE /// ENTRY A70792 #type complete TITLE hypothetical protein Rv3688c - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A70792 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession A70792 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-154 ##label COL !'##cross-references GB:AL022121; GB:AL123456; NID:g3261559; !1PIDN:CAA18010.1; PID:g2960112 !'##experimental_source strain H37Rv GENETICS !$#gene Rv3688c CLASSIFICATION #superfamily Bacillus subtilis conserved hypothetical !1protein yqeY SUMMARY #length 154 #molecular-weight 16701 #checksum 6908 SEQUENCE /// ENTRY S60942 #type complete TITLE hypothetical protein YOR215c - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein O5025; hypothetical protein YOR50-5 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S60942; S67108; S71717 REFERENCE S60938 !$#authors Galisson, F.; Dujon, B. !$#submission submitted to the EMBL Data Library, October 1995 !$#description Sequence and analysis of a 33 kb fragment from the right arm !1of chromosome XV of the yeast Saccharomyces cerevisiae. !$#accession S60942 !'##molecule_type DNA !'##residues 1-185 ##label GAL !'##cross-references EMBL:X92441; NID:g1050762; PID:g1050767 REFERENCE S67104 !$#authors Boyer, J.; Fairhead, C.; Gaillon, L.; Galisson, F.; Michaux, !1G.; Thierry, A.; Dujon, B. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67108 !'##molecule_type DNA !'##residues 1-185 ##label BOY !'##cross-references EMBL:Z75123; NID:g1420500; PID:g1420501; !1GSPDB:GN00015; MIPS:YOR215c !'##experimental_source strain S288C REFERENCE S71713 !$#authors Galisson, F.; Dujon, B. !$#journal Yeast (1996) 12:877-885 !$#title Sequence and analysis of a 33 kb fragment from the right arm !1of chromosome XV of the yeast Saccharomyces cerevisiae. !$#cross-references MUID:96437977; PMID:8840505 !$#accession S71717 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-185 ##label GAW !'##cross-references EMBL:X92441; NID:g1050762; PIDN:CAA63178.1; !1PID:g1050767 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1October 1995 GENETICS !$#gene MIPS:YOR215c !'##cross-references SGD:S0005741 !$#map_position 15R CLASSIFICATION #superfamily Bacillus subtilis conserved hypothetical !1protein yqeY SUMMARY #length 185 #molecular-weight 21229 #checksum 2053 SEQUENCE /// ENTRY G69970 #type complete TITLE spore coat protein homolog yraG - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69970 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69970 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-81 ##label KUN !'##cross-references GB:Z99117; GB:AL009126; NID:g2634966; !1PIDN:CAB14636.1; PID:g2635140 !'##experimental_source strain 168 GENETICS !$#gene yraG CLASSIFICATION #superfamily Bacillus subtilis spore coat protein homolog !1yraG SUMMARY #length 81 #molecular-weight 9205 #checksum 8159 SEQUENCE /// ENTRY E69970 #type complete TITLE spore coat protein homolog yraE - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69970 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69970 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-65 ##label KUN !'##cross-references GB:Z99117; GB:AL009126; NID:g2634966; !1PIDN:CAB14639.1; PID:g2635143 !'##experimental_source strain 168 GENETICS !$#gene yraE CLASSIFICATION #superfamily Bacillus subtilis spore coat protein homolog !1yraG SUMMARY #length 65 #molecular-weight 7475 #checksum 8979 SEQUENCE /// ENTRY G70007 #type complete TITLE conserved hypothetical protein yueF - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G70007 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G70007 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-369 ##label KUN !'##cross-references GB:Z99120; GB:AL009126; NID:g2635613; !1PIDN:CAB15168.1; PID:g2635675 !'##experimental_source strain 168 GENETICS !$#gene yueF CLASSIFICATION #superfamily Bacillus subtilis conserved hypothetical !1protein yueF SUMMARY #length 369 #molecular-weight 40896 #checksum 3871 SEQUENCE /// ENTRY D70006 #type complete TITLE conserved hypothetical protein yubA - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D70006 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D70006 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-388 ##label KUN !'##cross-references GB:Z99119; GB:AL009126; NID:g2635411; !1PIDN:CAB15094.1; PID:g2635600 !'##experimental_source strain 168 GENETICS !$#gene yubA CLASSIFICATION #superfamily Bacillus subtilis conserved hypothetical !1protein yueF SUMMARY #length 388 #molecular-weight 43610 #checksum 4721 SEQUENCE /// ENTRY C69979 #type complete TITLE conserved hypothetical protein yrrI - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS C69979 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69979 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-353 ##label KUN !'##cross-references GB:Z99117; GB:Z99118; GB:AL009126; NID:g2635200; !1PID:g2635205; NID:g2634966; PID:g2635187 !'##experimental_source strain 168 GENETICS !$#gene yrrI CLASSIFICATION #superfamily Bacillus subtilis conserved hypothetical !1protein yueF SUMMARY #length 353 #molecular-weight 39600 #checksum 3621 SEQUENCE /// ENTRY D65025 #type complete TITLE probable permease [imported] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS D65025 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65025 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-353 ##label BLAT !'##cross-references GB:AE000335; GB:U00096; NID:g1788821; !1PIDN:AAC75546.1; PID:g1788838; UWGP:b2493 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily Bacillus subtilis conserved hypothetical !1protein yueF SUMMARY #length 353 #molecular-weight 39194 #checksum 5194 SEQUENCE /// ENTRY S74365 #type complete TITLE hypothetical protein sll0063 - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S74365 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74365 !'##status preliminary !'##molecule_type DNA !'##residues 1-395 ##label KAN !'##cross-references EMBL:D64001; GB:AB001339; NID:g1001102; !1PID:g1001141 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily Bacillus subtilis conserved hypothetical !1protein yueF SUMMARY #length 395 #molecular-weight 43113 #checksum 9413 SEQUENCE /// ENTRY G65063 #type complete TITLE hypothetical protein b2811 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS G65063 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65063 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-147 ##label BLAT !'##cross-references GB:AE000364; GB:U00096; NID:g2367162; !1PIDN:AAC75853.1; PID:g1789176; UWGP:b2811 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily hypothetical protein b2811 SUMMARY #length 147 #molecular-weight 15940 #checksum 582 SEQUENCE /// ENTRY B64025 #type complete TITLE conserved hypothetical protein HI1293 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 21-Jul-2000 #text_change 21-Jul-2000 ACCESSIONS T09422; B64025; C64025 REFERENCE Z16667 !$#authors White, O.; Clayton, R.A.; Kerlavage, A.R.; Fleischmann, !1R.D.; Peterson, J.; Hickey, E.; Dodson, R.; Gwinn, M. !$#submission submitted to the EMBL Data Library, May 1998 !$#accession T09422 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-126 ##label WHI !'##cross-references EMBL:U32809; NID:g3212217; PIDN:AAC22947.1; !1PID:g3212218; TIGR:HI1293 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession B64025 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 46-126 ##label TIGR !'##cross-references GB:U32809 !'##note the sequence is revised in GenBank entry U32809, release 115, !1(PIDN:AAC22947.1) GENETICS !$#gene HI1293 CLASSIFICATION #superfamily hypothetical protein b2811 SUMMARY #length 126 #molecular-weight 14643 #checksum 7388 SEQUENCE /// ENTRY G64925 #type complete TITLE ynhA protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS G64925 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64925 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-138 ##label BLAT !'##cross-references GB:AE000263; GB:U00096; NID:g1787966; !1PIDN:AAC74749.1; PID:g1787969; UWGP:b1679 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ynhA CLASSIFICATION #superfamily hypothetical protein b2811 SUMMARY #length 138 #molecular-weight 15800 #checksum 5488 SEQUENCE /// ENTRY S76716 #type complete TITLE hypothetical protein - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S76716 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76716 !'##status preliminary !'##molecule_type DNA !'##residues 1-159 ##label KAN !'##cross-references EMBL:D90916; GB:AB001339; NID:g1653715; !1PIDN:BAA18628.1; PID:g1653717 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily hypothetical protein b2811 SUMMARY #length 159 #molecular-weight 17683 #checksum 562 SEQUENCE /// ENTRY E70980 #type complete TITLE hypothetical protein Rv3284 - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E70980 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession E70980 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-143 ##label COL !'##cross-references GB:Z92771; GB:AL123456; NID:g3242259; !1PIDN:CAB07067.1; PID:g1877339 !'##experimental_source strain H37Rv GENETICS !$#gene Rv3284 CLASSIFICATION #superfamily hypothetical protein b2811 SUMMARY #length 143 #molecular-weight 15394 #checksum 8855 SEQUENCE /// ENTRY G69646 #type complete TITLE sigma-H activator ispU - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69646 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69646 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-277 ##label KUN !'##cross-references GB:Z99110; GB:AL009126; NID:g2633472; !1PIDN:CAB13177.1; PID:g2633674 !'##experimental_source strain 168 GENETICS !$#gene ispU CLASSIFICATION #superfamily sigma-H activator ispU SUMMARY #length 277 #molecular-weight 32387 #checksum 7431 SEQUENCE /// ENTRY E69906 #type complete TITLE conserved hypothetical protein yojH - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69906 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69906 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-282 ##label KUN !'##cross-references GB:Z99114; GB:AL009126; NID:g2634230; !1PIDN:CAB13837.1; PID:g2634338 !'##experimental_source strain 168 GENETICS !$#gene yojH CLASSIFICATION #superfamily sigma-H activator ispU SUMMARY #length 282 #molecular-weight 32109 #checksum 1053 SEQUENCE /// ENTRY D69958 #type complete TITLE conserved hypothetical protein yqhA - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69958 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D69958 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-278 ##label KUN !'##cross-references GB:Z99116; GB:AL009126; NID:g2634723; !1PIDN:CAB14407.1; PID:g2634910 !'##experimental_source strain 168 GENETICS !$#gene yqhA CLASSIFICATION #superfamily sigma-H activator ispU SUMMARY #length 278 #molecular-weight 31810 #checksum 9745 SEQUENCE /// ENTRY E69701 #type complete TITLE positive regulator of sigma-B activity rsbR - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69701 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession E69701 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-274 ##label KUN !'##cross-references GB:Z99106; GB:AL009126; NID:g2632653; !1PIDN:CAB12274.1; PID:g2632767 !'##experimental_source strain 168 GENETICS !$#gene rsbR CLASSIFICATION #superfamily sigma-H activator ispU SUMMARY #length 274 #molecular-weight 31050 #checksum 241 SEQUENCE /// ENTRY E64452 #type complete TITLE conserved hypothetical protein MJ1222 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E64452 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession E64452 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-243 ##label BUL !'##cross-references GB:U67563; GB:L77117; NID:g2826379; !1PIDN:AAB99226.1; PID:g1591853; TIGR:MJ1222 GENETICS !$#map_position REV1165714-1164983 !$#start_codon GTG CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum !1dolichyl-phosphate mannose synthase related protein SUMMARY #length 243 #molecular-weight 27428 #checksum 2863 SEQUENCE /// ENTRY A71037 #type complete TITLE hypothetical protein PH1585 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A71037 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession A71037 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-313 ##label KAW !'##cross-references GB:AP000006; NID:g3236133; PIDN:BAA30697.1; !1PID:g3258014 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1585 CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum !1dolichyl-phosphate mannose synthase related protein SUMMARY #length 313 #molecular-weight 34626 #checksum 1277 SEQUENCE /// ENTRY G69047 #type complete TITLE conserved hypothetical protein MTH136 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69047 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession G69047 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-220 ##label MTH !'##cross-references GB:AE000802; GB:AE000666; NID:g2621163; !1PIDN:AAB84642.1; PID:g2621176 !'##experimental_source strain Delta H GENETICS !$#gene MTH136 !$#start_codon GTG CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum !1dolichyl-phosphate mannose synthase related protein SUMMARY #length 220 #molecular-weight 23853 #checksum 9799 SEQUENCE /// ENTRY G69148 #type complete TITLE dolichyl-phosphate mannose synthase related protein 1 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69148 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession G69148 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-248 ##label MTH !'##cross-references GB:AE000823; GB:AE000666; NID:g2621432; !1PIDN:AAB84883.1; PID:g2621438 !'##experimental_source strain Delta H GENETICS !$#gene MTH377 CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum !1dolichyl-phosphate mannose synthase related protein SUMMARY #length 248 #molecular-weight 27307 #checksum 9067 SEQUENCE /// ENTRY D71038 #type complete TITLE hypothetical protein PH1596 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D71038 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession D71038 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-215 ##label KAW !'##cross-references GB:AP000006; NID:g3236133; PIDN:BAA30708.1; !1PID:g3258025 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1596 CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum !1dolichyl-phosphate mannose synthase related protein SUMMARY #length 215 #molecular-weight 24286 #checksum 3266 SEQUENCE /// ENTRY D69148 #type complete TITLE dolichyl-phosphate mannose synthase related protein 2 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69148 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession D69148 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-291 ##label MTH !'##cross-references GB:AE000823; GB:AE000666; NID:g2621432; !1PIDN:AAB84880.1; PID:g2621435 !'##experimental_source strain Delta H GENETICS !$#gene MTH374 CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum !1dolichyl-phosphate mannose synthase related protein SUMMARY #length 291 #molecular-weight 31765 #checksum 1205 SEQUENCE /// ENTRY D64811 #type complete TITLE aldose 1-epimerase (EC 5.1.3.3) - Escherichia coli (strain K-12) ALTERNATE_NAMES mutarotase ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS D64811; S53654 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D64811 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-346 ##label BLAT !'##cross-references GB:AE000178; GB:U00096; NID:g1786967; !1PIDN:AAC73843.1; PID:g1786971; UWGP:b0756 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S53653 !$#authors Bouffard, G.G.; Rudd, K.E.; Adhya, S.L. !$#journal J. Mol. Biol. (1994) 244:269-278 !$#title Dependence of lactose metabolism upon mutarotase encoded in !1the gal operon in Escherichia coli. !$#cross-references MUID:95055764; PMID:7966338 !$#accession S53654 !'##molecule_type DNA !'##residues 1-346 ##label BOU !'##cross-references GB:U13636; NID:g1620033; PIDN:AAB17020.1; !1PID:g725494 GENETICS !$#gene galM !$#start_codon GTG FUNCTION !$#description isomerase !$#pathway carbohydrate metabolism CLASSIFICATION #superfamily aldose 1-epimerase KEYWORDS carbohydrate metabolism; isomerase SUMMARY #length 346 #molecular-weight 38190 #checksum 7195 SEQUENCE /// ENTRY C64096 #type complete TITLE aldose 1-epimerase (EC 5.1.3.3) - Haemophilus influenzae ALTERNATE_NAMES mutarotase ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS C64096; S27989; S21448 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession C64096 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-340 ##label TIGR !'##cross-references GB:U32764; GB:L42023; NID:g1573827; !1PIDN:AAC22477.1; PID:g1573831; TIGR:HI0818 !'##experimental_source strain Rd KW20 REFERENCE S27986 !$#authors Maskell, D.J.; Szabo, M.J.; Deadman, M.E.; Moxon, E.R. !$#journal Mol. Microbiol. (1992) 6:3051-3063 !$#title The gal locus from Haemophilus influenzae: cloning, !1sequencing and the use of gal mutants to study !1lipopolysaccharide. !$#cross-references MUID:93125127; PMID:1282642 !$#accession S27989 !'##molecule_type DNA !'##residues 'M',1-41,'I',43-45,'G',47-57,'E',59-112,'K',114-115,'K' !1##label MAS !'##cross-references EMBL:X65934; NID:g43562; PIDN:CAA46732.1; !1PID:g43566 !'##experimental_source strain RM.7004 !'##note the authors translated the codon TAT for residue 15 as Ile and !1CGT for residue 27 as Thr GENETICS !$#gene galM CLASSIFICATION #superfamily aldose 1-epimerase KEYWORDS isomerase SUMMARY #length 340 #molecular-weight 38102 #checksum 1771 SEQUENCE /// ENTRY A29277 #type complete TITLE aldose 1-epimerase (EC 5.1.3.3) - Acinetobacter calcoaceticus ORGANISM #formal_name Acinetobacter calcoaceticus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A29277; B24487 REFERENCE A29277 !$#authors Gatz, C.; Hillen, W. !$#journal Nucleic Acids Res. (1986) 14:4309-4323 !$#title Acinetobacter calcoaceticus encoded mutarotase: nucleotide !1sequence analysis of the gene and characterization of its !1secretion in Escherichia coli. !$#cross-references MUID:86232560; PMID:3012466 !$#accession A29277 !'##molecule_type DNA !'##residues 1-381 ##label GAT !'##cross-references GB:X03893; NID:g38721; PIDN:CAA27530.1; PID:g38722 REFERENCE A24487 !$#authors Gatz, C.; Altschmied, J.; Hillen, W. !$#journal J. Bacteriol. (1986) 168:31-39 !$#title Cloning and expression of the Acinetobacter calcoaceticus !1mutarotase gene in Escherichia coli. !$#cross-references MUID:87008396; PMID:3531172 !$#accession B24487 !'##status preliminary !'##molecule_type protein !'##residues 306-381 ##label GA2 GENETICS !$#gene mro CLASSIFICATION #superfamily aldose 1-epimerase KEYWORDS isomerase SUMMARY #length 381 #molecular-weight 41550 #checksum 4335 SEQUENCE /// ENTRY T01933 #type complete TITLE probable aldose 1-epimerase (EC 5.1.3.3) - common tobacco ORGANISM #formal_name Nicotiana tabacum #common_name common tobacco DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS T01933 REFERENCE Z14460 !$#authors Heese-Peck, A.; Raikhel, N.V. !$#submission submitted to the EMBL Data Library, November 1997 !$#description A glycoprotein modified with terminal N-acetylglucosamine !1and localized at the nuclear periphery shows sequence !1similarity to aldose-1-epimerases. !$#accession T01933 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-356 ##label HEE !'##cross-references EMBL:AF032386; NID:g2739167; PID:g2739168 GENETICS !$#gene GP40 CLASSIFICATION #superfamily aldose 1-epimerase KEYWORDS isomerase SUMMARY #length 356 #molecular-weight 39229 #checksum 1539 SEQUENCE /// ENTRY B44509 #type complete TITLE aldose 1-epimerase (EC 5.1.3.3) - Streptococcus thermophilus ORGANISM #formal_name Streptococcus thermophilus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B44509 REFERENCE A44509 !$#authors Poolman, B.; Royer, T.J.; Mainzer, S.E.; Schmidt, B.F. !$#journal J. Bacteriol. (1990) 172:4037-4047 !$#title Carbohydrate utilization in Streptococcus thermophilus: !1characterization of the genes for aldose 1-epimerase !1(mutarotase) and UDPglucose 4-epimerase. !$#cross-references MUID:90299833; PMID:1694527 !$#accession B44509 !'##status preliminary !'##molecule_type DNA !'##residues 1-348 ##label POO !'##cross-references EMBL:M38175; NID:g153748; PID:g153750 CLASSIFICATION #superfamily aldose 1-epimerase KEYWORDS isomerase SUMMARY #length 348 #molecular-weight 39012 #checksum 5351 SEQUENCE /// ENTRY JE0292 #type complete TITLE fungal stress protein - Rhizopus nigricans ORGANISM #formal_name Rhizopus nigricans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS JE0292 REFERENCE JE0292 !$#authors Cresnar, B.; Plaper, A.; Breskvar, K.; Hudnik-Plevnik, T. !$#journal Biochem. Biophys. Res. Commun. (1998) 250:664-667 !$#title cDNA sequence and deduced amino acid sequence of a fungal !1stress protein induced in Rhizopus nigricans by steroids. !$#cross-references MUID:99003515; PMID:9784403 !$#accession JE0292 !'##molecule_type mRNA !'##residues 1-364 ##label CRE !'##cross-references GB:Y10414 CLASSIFICATION #superfamily aldose 1-epimerase SUMMARY #length 364 #molecular-weight 40275 #checksum 7477 SEQUENCE /// ENTRY A31752 #type complete TITLE transcription factor AP-2A - human ALTERNATE_NAMES enhancer-binding protein AP-2 ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 29-Sep-1999 ACCESSIONS A31752 REFERENCE A31752 !$#authors Williams, T.; Admon, A.; Luescher, B.; Tjian, R. !$#journal Genes Dev. (1988) 2:1557-1569 !$#title Cloning and expression of AP-2, a cell-type-specific !1transcription factor that activates inducible enhancer !1elements. !$#cross-references MUID:89107991; PMID:3063603 !$#accession A31752 !'##molecule_type mRNA !'##residues 1-437 ##label WIL !'##cross-references GB:X52611; GB:Y00229; NID:g28717; PIDN:CAA36842.1; !1PID:g28718; GB:M36711; NID:g178702; PIDN:AAA35539.1; !1PID:g178703 GENETICS !$#gene GDB:TFAP2A; AP-2; AP2TF; TFAP2 !'##cross-references GDB:128106; OMIM:107580 !$#map_position 6pter-6p22.3 CLASSIFICATION #superfamily transcription factor AP-2 KEYWORDS alternative splicing; DNA binding; homodimer; transcription !1factor SUMMARY #length 437 #molecular-weight 48062 #checksum 501 SEQUENCE /// ENTRY S64732 #type complete TITLE scaffold attachment factor B - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 29-Sep-1999 ACCESSIONS S64732 REFERENCE S64732 !$#authors Renz, A.; Fackelmayer, F.O. !$#journal Nucleic Acids Res. (1996) 24:843-849 !$#title Purification and molecular cloning of the scaffold !1attachment factor B (SAF-B), a novel human nuclear protein !1that specifically binds to S/MAR-DNA. !$#cross-references MUID:96174649; PMID:8600450 !$#accession S64732 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-849 ##label REN !'##cross-references EMBL:L43631 !'##experimental_source cell line HeLa S3; cervix carcinoma !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1996 GENETICS !$#gene GDB:SAB !'##cross-references GDB:9834067; OMIM:602895 !$#map_position 19p13.3-19p13.2 FUNCTION !$#description binds specifically to scaffold or matrix attachment region !1DNA elements CLASSIFICATION #superfamily human scaffold attachment factor B; !1ribonucleoprotein repeat homology FEATURE !$341-408 #domain ribonucleoprotein repeat homology #label RRM2 SUMMARY #length 849 #molecular-weight 96703 #checksum 1963 SEQUENCE /// ENTRY S60735 #type complete TITLE splicing factor SF3a 120K chain - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S60735; S60733 REFERENCE S60733 !$#authors Kraemer, A.; Mulhauser, F.; Wersig, C.; Groening, K.; Bilbe, !1G. !$#journal RNA (1995) 1:260-272 !$#title Mammalian splicing factor SF3a120 represents a new member of !1the SURP family of proteins and is homologous to the !1essential splicing factor PRP21p of Saccharomyces !1cerevisiae. !$#cross-references MUID:96079958; PMID:7489498 !$#accession S60735 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-793 ##label KRA !'##cross-references EMBL:X85237; NID:g899297; PIDN:CAA59494.1; !1PID:g899298 !$#accession S60733 !'##molecule_type protein !'##residues 51-62;82-94;270-275;397-414;448-463 ##label KRA2 GENETICS !$#gene GDB:SF3A120; PRP21; SAP114 !'##cross-references GDB:9955873 !$#map_position 22q12.1-22qter CLASSIFICATION #superfamily human splicing factor SF3a 120K chain; !1ubiquitin homology KEYWORDS pre-mRNA splicing FEATURE !$714-790 #domain ubiquitin homology #label UBH SUMMARY #length 793 #molecular-weight 88886 #checksum 9486 SEQUENCE /// ENTRY S50096 #type complete TITLE probable splicing factor Ceprp21 - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S50096; T33806 REFERENCE S50095 !$#authors Spikes, D.A.; Kramer, J.; Bingham, P.M.; van Doren, K. !$#journal Nucleic Acids Res. (1994) 22:4510-4519 !$#title SWAP pre-mRNA splicing regulators are a novel, ancient !1protein family sharing a highly conserved sequence motif !1with the prp21 family of constitutive splicing proteins. !$#cross-references MUID:95061415; PMID:7971282 !$#accession S50096 !'##status preliminary !'##molecule_type mRNA !'##residues 1-655 ##label SPI !'##cross-references EMBL:U09415; NID:g498845; PIDN:AAA82164.1; !1PID:g498846 REFERENCE Z21414 !$#authors Latreille, P.; Wamsley, P. !$#submission submitted to the EMBL Data Library, November 1998 !$#description The sequence of C. elegans cosmid W07E6. !$#accession T33806 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-655 ##label LAT !'##cross-references EMBL:AF106576; PIDN:AAC78179.1; GSPDB:GN00020; !1CESP:W07E6.4 !'##experimental_source strain Bristol N2; clone W07E6 GENETICS !$#gene CESP:W07E6.4 !$#map_position 2 !$#introns 36/1; 132/2; 185/3; 309/1; 402/2; 464/1; 532/3; 598/3 CLASSIFICATION #superfamily Caenorhabditis elegans probable splicing factor !1Ceprp21 SUMMARY #length 655 #molecular-weight 73812 #checksum 5287 SEQUENCE /// ENTRY A55473 #type complete TITLE early switch protein xol-1 2.5k splice form - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A55473 REFERENCE A55473 !$#authors Rhind, N.R.; Miller, L.M.; Kopczynski, J.B.; Meyer, B.J. !$#journal Cell (1995) 80:71-82 !$#title xol-1 acts as an early switch in the Caenorhabditis elegans !1male/hermaphrodite decision. !$#cross-references MUID:95112352; PMID:7813020 !$#accession A55473 !'##status preliminary !'##molecule_type DNA !'##residues 1-355 ##label RHI !'##cross-references GB:L35129; NID:g520796; PIDN:AAA67048.1; !1PID:g520797 GENETICS !$#introns 26/2; 56/3; 118/3; 146/1; 197/2 CLASSIFICATION #superfamily early switch protein xol KEYWORDS alternative splicing SUMMARY #length 355 #molecular-weight 40569 #checksum 3464 SEQUENCE /// ENTRY A47328 #type complete TITLE natural killer cell tumor-recognition protein - human ALTERNATE_NAMES cyclophilin-related NK-tumor recognition protein; natural killer-tumor recognition protein (NK-TR) ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 24-Sep-1999 ACCESSIONS A47328 REFERENCE A47328 !$#authors Anderson, S.K.; Gallinger, S.; Roder, J.; Frey, J.; Young, !1H.A.; Ortaldo, J.R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1993) 90:542-546 !$#title A cyclophilin-related protein involved in the function of !1natural killer cells. !$#cross-references MUID:93133824; PMID:8421688 !$#accession A47328 !'##status preliminary !'##molecule_type mRNA !'##residues 1-1403 ##label AND !'##cross-references GB:L04288; NID:g181251; PIDN:AAA35734.1; !1PID:g181252 !'##experimental_source NK killer cells from adult blood !'##note sequence extracted from NCBI backbone (NCBIN:122798, !1NCBIP:122800) GENETICS !$#gene GDB:NKTR !'##cross-references GDB:137171; OMIM:161565 !$#map_position 3p23-3p21 CLASSIFICATION #superfamily natural killer cell tumor-recognition protein; !1cyclophilin homology KEYWORDS alternative splicing; lymphocyte FEATURE !$60-230 #domain cyclophilin homology #label CYP SUMMARY #length 1403 #molecular-weight 157711 #checksum 780 SEQUENCE /// ENTRY JC5314 #type complete TITLE CDC28/cdc2-like kinase associating arginine-serine cyclophilin - human ALTERNATE_NAMES CARS-Cyp ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS JC5314; G02262 REFERENCE JC5314 !$#authors Nestel, F.P.; Colwill, K.; Harper, S.; Pawson, T.; Anderson, !1S.K. !$#journal Gene (1996) 180:151-155 !$#title RS cyclophilins: Identification of an NK-TR1-related !1cyclophilin. !$#cross-references MUID:97128820; PMID:8973360 !$#accession JC5314 !'##molecule_type mRNA !'##residues 1-754 ##label NES !'##cross-references EMBL:U40763; NID:g1117967; PIDN:AAB40347.1; !1PID:g1117968 !'##experimental_source thymus !'##note submitted to the EMBL Data Library, November 1995 COMMENT This protein contains a cyclophilin-related domain, two 140K !1nuclear phosphoprotein related domains and a large !1arginine-serine repeat domain. It plays a role in the !1regulation of pre-mRNA splicing by binding to splicing !1factors containing serine-arginine repeats protein. GENETICS !$#gene GDB:CYP; CARS-CYP !'##cross-references GDB:9956062 CLASSIFICATION #superfamily CARS cyclophilin; cyclophilin homology FEATURE !$7-177 #domain cyclophilin homology #label CYP SUMMARY #length 754 #molecular-weight 88618 #checksum 6312 SEQUENCE /// ENTRY S58884 #type complete TITLE Ran-binding protein 2 - human ALTERNATE_NAMES giant nucleopore protein Nup358; nucleoporin Nup358; RanBP2 protein ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S58884; A57545 REFERENCE S58884 !$#authors Yokoyama, N.; Hayashi, N.; Seki, T.; Pante, N.; Ohba, T.; !1Nishii, K.; Kuma, K.; Hayashida, T.; Miyata, T.; Aebi, U.; !1Fukui, M.; Nishimoto, T. !$#journal Nature (1995) 376:184-188 !$#title A giant nucleopore protein that binds Ran/TC4. !$#cross-references MUID:95327194; PMID:7603572 !$#accession S58884 !'##status nucleic acid sequence not shown !'##molecule_type mRNA !'##residues 1-3224 ##label YOK !'##cross-references EMBL:D42063; NID:g924266; PIDN:BAA07662.1; !1PID:g1009337 !'##experimental_source cell type B-lymphocyte REFERENCE A57545 !$#authors Wu, J.; Matunis, M.J.; Kraemer, D.; Blobel, G.; Coutavas, E. !$#journal J. Biol. Chem. (1995) 270:14209-14213 !$#title Nup358, a cytoplasmically exposed nucleoporin with peptide !1repeats, Ran-GTP binding sites, zinc fingers, a cyclophilin !1A homologous domain, and a leucine-rich region. !$#cross-references MUID:95294031; PMID:7775481 !$#accession A57545 !'##status preliminary !'##molecule_type mRNA !'##residues 1-776,'R',778-783,'R',785-3224 ##label WUA !'##cross-references GB:L41840; NID:g857367; PIDN:AAC41758.1; !1PID:g857368 !'##experimental_source cell line HeLa GENETICS !$#gene GDB:RANBP2; NUP358 !'##cross-references GDB:4642758; OMIM:601181 !$#map_position 2cen-2q13 FUNCTION !$#description may play a role in nuclear protein import CLASSIFICATION #superfamily nucleoporin Nup358; cyclophilin homology; !1tetratricopeptide repeat homology KEYWORDS leucine zipper FEATURE !$26-59 #domain tetratricopeptide repeat homology #label TT1\ !$60-93 #domain tetratricopeptide repeat homology #label TT2\ !$450-471 #domain leucine zipper #status predicted #label LEU\ !$3063-3224 #domain cyclophilin homology #label CYP SUMMARY #length 3224 #molecular-weight 358168 #checksum 9244 SEQUENCE /// ENTRY T02809 #type complete TITLE probable peptidylprolyl isomerase (EC 5.2.1.8) PPCTIB [similarity] - Leishmania major (strain Friedlin) ORGANISM #formal_name Leishmania major DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Sep-2000 ACCESSIONS E81457; T02809 REFERENCE A81455 !$#authors Myler, P.J.; Audleman, L.; deVos, T.; Hixson, G.; Kiser, P.; !1Lemley, C.; Magness, C.; Rickel, E.; Sisk, E.; Sunkin, S.; !1Swartzell, S.; Westlake, T.; Bastien, P.; Fu, G.; Ivens, A.; !1Stuart, K. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1999) 96:2902-2906 !$#title Leishmania major Friedlin chromosome 1 has an unusual !1distribution of protein-coding genes. !$#cross-references MUID:99178987; PMID:10077609 !$#accession E81457 !'##status preliminary !'##molecule_type DNA !'##residues 1-335 ##label PYL !'##cross-references GB:AE001274; NID:g3264850; PIDN:AAC24632.1; !1PID:g2995585; GSPDB:GN00125 !'##experimental_source strain MHOM/IL/81/Friedlin GENETICS !$#gene PPCTIB !$#map_position 1 CLASSIFICATION #superfamily hypothetical protein PPCTIB; cyclophilin !1homology KEYWORDS cis-trans-isomerase FEATURE !$149-331 #domain cyclophilin homology #label CYP SUMMARY #length 335 #molecular-weight 36186 #checksum 5328 SEQUENCE /// ENTRY S64705 #type complete TITLE cyclophilin-like protein CyP-60 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S64705 REFERENCE S64705 !$#authors Wang, B.B.; Hayenga, K.J.; Payan, D.G.; Fisher, J.M. !$#journal Biochem. J. (1996) 314:313-319 !$#title Identification of a nuclear-specific cyclophilin which !1interacts with the proteinase inhibitor eglin c. !$#cross-references MUID:96195145; PMID:8660300 !$#accession S64705 !'##status preliminary !'##molecule_type mRNA !'##residues 1-520 ##label WAN !'##cross-references EMBL:U37219; NID:g1199597; PIDN:AAC50376.1; !1PID:g1199598 CLASSIFICATION #superfamily peptidylprolyl isomerase CyP-60; cyclophilin !1homology FEATURE !$274-434 #domain cyclophilin homology #label CYP SUMMARY #length 520 #molecular-weight 58823 #checksum 8167 SEQUENCE /// ENTRY S62590 #type complete TITLE peptidyl-prolyl cis-trans isomerase - fission yeast (Schizosaccharomyces pombe) ORGANISM #formal_name Schizosaccharomyces pombe DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 11-Jan-2000 ACCESSIONS S62590; T38137 REFERENCE S62586 !$#authors McLean, J.; Harris, D. !$#submission submitted to the EMBL Data Library, November 1995 !$#accession S62590 !'##status preliminary !'##molecule_type DNA !'##residues 1-471 ##label MCL !'##cross-references EMBL:Z67999; NID:g1067216; PID:g1067221 REFERENCE Z21773 !$#authors McLean, J.; Harris, D.; Wood, V.; Barrell, B.G.; Rajandream, !1M.A.; Walsh, S.V. !$#submission submitted to the EMBL Data Library, November 1995 !$#accession T38137 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-471 ##label MC2 !'##cross-references EMBL:Z67999; PIDN:CAA91964.1; GSPDB:GN00066; !1SPDB:SPAC21E11.05c !'##experimental_source strain 972h-; cosmid c21E11 GENETICS !$#gene SPAC21E11.05c !$#map_position 1L !$#introns 5/3; 26/2; 331/2 CLASSIFICATION #superfamily peptidylprolyl isomerase CyP-60; cyclophilin !1homology FEATURE !$225-384 #domain cyclophilin homology #label CYP SUMMARY #length 471 #molecular-weight 53573 #checksum 3220 SEQUENCE /// ENTRY S30697 #type complete TITLE cyaY protein - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS S30697; S24976; H65184 REFERENCE S30660 !$#authors Daniels, D.L.; Plunkett III, G.; Burland, V.; Blattner, F.R. !$#journal Science (1992) 257:771-778 !$#title Analysis of the Escherichia coli genome: DNA sequence of the !1region from 84.5 to 86.5 minutes. !$#cross-references MUID:92358234; PMID:1379743 !$#accession S30697 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-106 ##label DAN !'##cross-references EMBL:M87049; NID:g836656; PIDN:AAA67603.1; !1PID:g148206 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1992 REFERENCE S24974 !$#authors Glaser, P.; Sismeiro, O.; Danchin, A. !$#submission submitted to the EMBL Data Library, June 1992 !$#description Phylogeny of enterobacterial cya locus. !$#accession S24976 !'##status preliminary !'##molecule_type DNA !'##residues 1-106 ##label GLA !'##cross-references EMBL:X66782; NID:g41185; PIDN:CAA47281.1; !1PID:g41188 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65184 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-106 ##label BLAT !'##cross-references GB:AE000456; GB:U00096; NID:g2367291; !1PIDN:AAC76810.1; PID:g1790239; UWGP:b3807 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene cyaY !$#map_position 86 min CLASSIFICATION #superfamily cyaY protein SUMMARY #length 106 #molecular-weight 12231 #checksum 6681 SEQUENCE /// ENTRY S24982 #type complete TITLE cyaY protein - Yersinia intermedia ORGANISM #formal_name Yersinia intermedia DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 08-Oct-1999 ACCESSIONS S24982 REFERENCE S24974 !$#authors Glaser, P.; Sismeiro, O.; Danchin, A. !$#submission submitted to the EMBL Data Library, June 1992 !$#description Phylogeny of enterobacterial cya locus. !$#accession S24982 !'##status preliminary !'##molecule_type DNA !'##residues 1-107 ##label GLA !'##cross-references EMBL:X66781; NID:g48613; PIDN:CAA47278.1; !1PID:g581838 GENETICS !$#start_codon GTG CLASSIFICATION #superfamily cyaY protein SUMMARY #length 107 #molecular-weight 12101 #checksum 1521 SEQUENCE /// ENTRY S23700 #type complete TITLE cyaY protein - Erwinia chrysanthemi ORGANISM #formal_name Erwinia chrysanthemi DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 08-Oct-1999 ACCESSIONS S23700 REFERENCE S23698 !$#authors Danchin, A.; Lenzen, G. !$#journal Second Messengers Phosphoproteins (1988) 12:7-28 !$#title Structure and evolution of bacterial adenylate cyclase: !1comparison between Escherichia coli and Erwinia !1chrysanthemi. !$#cross-references MUID:89055613; PMID:3057176 !$#accession S23700 !'##status preliminary; translation not shown !'##molecule_type DNA !'##residues 1-106 ##label DAN !'##cross-references EMBL:X63207; NID:g41670; PIDN:CAA44892.1; !1PID:g41673 CLASSIFICATION #superfamily cyaY protein SUMMARY #length 106 #molecular-weight 12036 #checksum 5791 SEQUENCE /// ENTRY E71688 #type complete TITLE cyay protein (cyaY) RP323 - Rickettsia prowazekii ORGANISM #formal_name Rickettsia prowazekii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Nov-2000 ACCESSIONS E71688 REFERENCE A71630 !$#authors Andersson, S.G.E.; Zomorodipour, A.; Andersson, J.O.; !1Sicheritz-Ponten, T.; Alsmark, U.C.M.; Podowski, R.M.; !1Naeslund, A.K.; Eriksson, A.S.; Winkler, H.H.; Kurland, C.G. !$#journal Nature (1998) 396:133-140 !$#title The genome sequence of Rickettsia prowazekii and the origin !1of mitochondria. !$#cross-references MUID:99039499; PMID:9823893 !$#accession E71688 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-104 ##label AND !'##cross-references GB:AJ235271; GB:AJ235269; NID:g3868717; !1PIDN:CAA14783.1; PID:g3860883; GSPDB:GN00081 !'##experimental_source strain Madrid E GENETICS !$#gene cyaY; RP323 CLASSIFICATION #superfamily cyaY protein SUMMARY #length 104 #molecular-weight 11960 #checksum 681 SEQUENCE /// ENTRY S25820 #type complete TITLE dynamin-related protein VPS1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES interferon-regulated resistance protein homolog; probable GTP-binding protein VPS1; protein YKR001c; SPO15 protein ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S25820; S38070; S13053; S14224; S29366; A35627 REFERENCE S25322 !$#authors Duesterhoeft, A.; Philippsen, P. !$#journal Yeast (1992) 8:749-759 !$#title DNA sequencing and analysis of a 24.7 kb segment !1encompassing centromere CEN11 of Saccharomyces cerevisiae !1reveals nine previously unknown open reading frames. !$#cross-references MUID:93070612; PMID:1441752 !$#accession S25820 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-704 ##label DUE !'##cross-references EMBL:X65124; NID:g3517; PIDN:CAA46251.1; PID:g3528 !'##experimental_source strain S288C !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1March 1992 REFERENCE S37811 !$#authors Duesterhoeft, A.; Moestl, D.; Poehlmann, R.; Philippsen, P. !$#submission submitted to the Protein Sequence Database, March 1994 !$#accession S38070 !'##molecule_type DNA !'##residues 1-704 ##label DU2 !'##cross-references EMBL:Z28226; NID:g486404; PID:g486405; !1GSPDB:GN00011; MIPS:YKR001c !'##experimental_source strain S288C REFERENCE A35627 !$#authors Rothman, J.H.; Raymond, C.K.; Gilbert, T.; O'Hara, P.J.; !1Stevens, T.H. !$#journal Cell (1990) 61:1063-1074 !$#title A putative GTP binding protein homologous to !1interferon-inducible Mx proteins performs an essential !1function in yeast protein sorting. !$#cross-references MUID:90275602; PMID:2112425 !$#accession S13053 !'##molecule_type DNA !'##residues 1-32,'N',34-110,'E',112-704 ##label ROT !'##cross-references EMBL:M33315; NID:g173182; PIDN:AAA35216.1; !1PID:g173183 !'##note the authors translated the codon GAA for residue 111 as Asn REFERENCE S14224 !$#authors Bloom, K.S. !$#submission submitted to the EMBL Data Library, August 1990 !$#accession S14224 !'##molecule_type DNA !'##residues 1-140,'Q',142-704 ##label BLO !'##cross-references EMBL:X54316; NID:g4527; PID:g4528 REFERENCE S29366 !$#authors Yeh, E.; Driscoll, R.; Coltrera, M.; Olins, A.; Bloom, K. !$#journal Nature (1991) 349:713-715 !$#title A dynamin-like protein encoded by the yeast sporulation gene !1SPO15. !$#cross-references MUID:91141584; PMID:1825352 !$#accession S29366 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-140,'Q',142-704 ##label YEH !'##cross-references EMBL:X54316; NID:g4527; PIDN:CAA38214.1; PID:g4528 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1990 GENETICS !$#gene SGD:VPS1; SPO15; MIPS:YKR001c !'##cross-references SGD:S0001709; MIPS:YKR001c !$#map_position 11R CLASSIFICATION #superfamily dynamin-related protein VPS1 KEYWORDS GTP binding; P-loop; purine nucleotide binding FEATURE !$36-43 #region nucleotide-binding motif A (P-loop)\ !$174-179 #region nucleotide-binding motif B\ !$42 #binding_site GTP (Lys) #status predicted SUMMARY #length 704 #molecular-weight 78736 #checksum 1565 SEQUENCE /// ENTRY S64742 #type complete TITLE dynamin-related protein DNM1 - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein L1381; protein YLL001w ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S64742; S64743; S55713; S70576 REFERENCE S64742 !$#authors Vandenbol, M.; Portetelle, D.; Hilger, F. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64742 !'##molecule_type DNA !'##residues 1-757 ##label VAN !'##cross-references EMBL:Z73106; NID:g1360156; PID:g1360157; !1GSPDB:GN00012; MIPS:YLL001w !'##experimental_source strain S288C REFERENCE S64743 !$#authors Miosga, T.; Zimmermann, F.K. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64743 !'##molecule_type DNA !'##residues 1-757 ##label MIO !'##cross-references EMBL:Z73106; NID:g1360156; PID:g1360157; !1GSPDB:GN00012; MIPS:YLL001w !'##experimental_source strain S288C REFERENCE S55713 !$#authors Gammie, A.E.; Kurihara, L.J.; Vallee, R.B.; Rose, M.D. !$#submission submitted to the EMBL Data Library, April 1995 !$#description DNM1, a dynamin-related gene, participates in !1receptor-mediated endocytosis in yeast. !$#accession S55713 !'##molecule_type DNA !'##residues 1-123,'ISPD',125-757 ##label GAM !'##cross-references EMBL:L40588; NID:g710601; PID:g710602 REFERENCE S70557 !$#authors Miosga, T.; Zimmermann, F.K. !$#journal Yeast (1996) 12:693-708 !$#title Sequence analysis of the CEN12 region of Saccharomyces !1cerevisiae on a 43.7 kb fragment of chromosome XII including !1an open reading frame homologous to the human cystic !1fibrosis transmembrane conductance regulator protein CFTR. !$#cross-references MUID:96405918; PMID:8810043 !$#accession S70576 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-757 ##label MIW !'##cross-references EMBL:X91488; NID:g1495203; PIDN:CAA62769.1; !1PID:g1495224 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1September 1995 GENETICS !$#gene SGD:DNM1; MIPS:YLL001w !'##cross-references SGD:S0003924; MIPS:YLL001w !$#map_position 12L CLASSIFICATION #superfamily dynamin-related protein VPS1 KEYWORDS GTP binding; P-loop; purine nucleotide binding; !1transmembrane protein FEATURE !$35-42 #region nucleotide-binding motif A (P-loop)\ !$171-176 #region nucleotide-binding motif B\ !$198-214 #domain transmembrane #status predicted #label TMM SUMMARY #length 757 #molecular-weight 84971 #checksum 8428 SEQUENCE /// ENTRY JC5695 #type complete TITLE Dnm1p/Vps1p-like protein - human ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 20-Apr-2000 ACCESSIONS JC5695; JE0281 REFERENCE JC5695 !$#authors Shin, H.; Shinotsuka, C.; Torii, S.; Murakami, K.; Nakayama, !1K. !$#journal J. Biochem. (1997) 122:525-530 !$#title Identification and subcellular localization of a novel !1mammalian dynamin-related protein homologous to yeast Vps1p !1and Dnm1p. !$#cross-references MUID:98006302; PMID:9348079 !$#accession JC5695 !'##molecule_type mRNA !'##residues 1-737 ##label SHI !'##cross-references DDBJ:AB006965 REFERENCE JE0281 !$#authors Hong, Y.R.; Chen, C.H.; Cheng, D.S.; Howng, S.L.; Chow, C.C. !$#journal Biochem. Biophys. Res. Commun. (1998) 249:697-703 !$#title Human dynamin-like protein interacts with the glycogen !1synthase kinase 3beta. !$#cross-references MUID:98401153; PMID:9731200 !$#accession JE0281 !'##status preliminary !'##molecule_type mRNA !'##residues 1-70,'T',72-207,'C',209-393 ##label HON !'##cross-references GB:AF061795 COMMENT This protein localizes to the trans-Golgi network, and !1lysosomal/endosomal compartments. It plays a fundamental !1role in cellular function. GENETICS !$#gene GDB:DYMPLE; DRP1; DVLP !'##cross-references GDB:9958967; OMIM:603850 CLASSIFICATION #superfamily dynamin-related protein VPS1 KEYWORDS GTP binding; P-loop; purine nucleotide binding FEATURE !$1-305 #domain GTP-binding #status predicted #label GTP\ !$31-39,146-149, !$215-218 #domain GTPase/GTP-binding consensus #status !8predicted #label GCO\ !$32-39 #region nucleotide-binding motif A (P-loop)\ !$142-147 #region nucleotide-binding motif B SUMMARY #length 737 #molecular-weight 81933 #checksum 6752 SEQUENCE /// ENTRY T04982 #type complete TITLE dynamin-like protein ADL2 - Arabidopsis thaliana ALTERNATE_NAMES protein T16L1.140 ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS T04982 REFERENCE Z15393 !$#authors Bevan, M.; Obermaier, B.; Deutschenbaur, S.; Piravandi, E.; !1Hoheisel, J.; Mewes, H.W.; Mayer, K.F.X.; Schueller, C. !$#submission submitted to the Protein Sequence Database, November 1998 !$#accession T04982 !'##molecule_type DNA !'##residues 1-808 ##label BEV !'##cross-references EMBL:AL031394 !'##experimental_source cultivar Columbia; BAC clone T16L1 GENETICS !$#gene ADL2 !$#map_position 4 !$#introns 138/3; 233/1; 242/3; 276/3; 299/3; 319/3; 357/3; 374/1; 410/ !13; 441/3; 472/3; 518/3; 556/3; 588/3; 602/1; 651/3; 700/3; !1718/2; 751/3 !$#note T16L1.140 CLASSIFICATION #superfamily dynamin-related protein VPS1 KEYWORDS P-loop; purine nucleotide binding FEATURE !$66-73 #region nucleotide-binding motif A (P-loop)\ !$168-173 #region nucleotide-binding motif B SUMMARY #length 808 #molecular-weight 89626 #checksum 1582 SEQUENCE /// ENTRY JC4305 #type complete TITLE dynamin II - human ALTERNATE_NAMES microtubule-binding protein ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS JC4305 REFERENCE JC4305 !$#authors Diatloff-Zito, C.; Gordon, A.J.E.; Duchaud, E.; Merlin, G. !$#journal Gene (1995) 163:301-306 !$#title Isolation of an ubiquitously expressed cDNA encoding human !1dynamin II,a member of the large GTP-binding protein family. !$#cross-references MUID:96011652; PMID:7590285 !$#accession JC4305 !'##molecule_type mRNA !'##residues 1-866 ##label DIA !'##cross-references GB:L36983 COMMENT This protein is a cytoskeletal protein that functions in !1endocytosis and synaptic vesicule recycling in brain. GENETICS !$#gene GDB:DNM2 !'##cross-references GDB:696233 !$#map_position 9q12-9q12 CLASSIFICATION #superfamily human dynamin II; pleckstrin repeat homology KEYWORDS GTP binding; membrane trafficking; nucleotide binding; !1P-loop; phosphoprotein FEATURE !$38-45 #region nucleotide-binding motif A (P-loop)\ !$132-137 #region nucleotide-binding motif B\ !$508-620 #domain protein kinase C substrate #status predicted !8#label PKC\ !$514-619 #domain pleckstrin repeat homology #label PLK\ !$740-866 #region proline-rich\ !$116,126,760 #binding_site phosphate (Ser) (covalent) (by cdc2 !8kinase) #status predicted\ !$175,274,323,404, !$742,762 #binding_site phosphate (Thr) (covalent) (by cdc2 !8kinase) #status predicted SUMMARY #length 866 #molecular-weight 97591 #checksum 8592 SEQUENCE /// ENTRY S34399 #type complete TITLE dynamin 3 - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S34399; S15497 REFERENCE S16130 !$#authors Chen, M.S.; Obar, R.A.; Schroeder, C.C.; Austin, T.W.; !1Poodry, C.A.; Wadsworth, S.C.; Vallee, R.B. !$#journal Nature (1991) 351:583-586 !$#title Multiple forms of dynamin are encoded by shibire, a !1Drosophila gene involved in endocytosis. !$#cross-references MUID:91260878; PMID:1828536 !$#accession S34399 !'##molecule_type mRNA !'##residues 1-836 ##label CHE !'##cross-references EMBL:X59448; NID:g7830; PIDN:CAA42067.1; PID:g7831 GENETICS !$#gene shibire !'##cross-references FlyBase:FBgn0003392 CLASSIFICATION #superfamily human dynamin II; pleckstrin repeat homology KEYWORDS alternative splicing; membrane trafficking; microtubule !1binding; nucleotide binding; P-loop FEATURE !$33-40 #region nucleotide-binding motif A (P-loop)\ !$127-132 #region nucleotide-binding motif B\ !$200-203 #region nucleotide binding #status predicted\ !$512-619 #domain pleckstrin repeat homology #label PLK SUMMARY #length 836 #molecular-weight 93758 #checksum 9216 SEQUENCE /// ENTRY A65146 #type complete TITLE probable ABC transporter yhiH - Escherichia coli (strain K-12) ALTERNATE_NAMES hyoithetical protein, rhsB-pit intergenic region ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS A65146; S47705; S47706 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65146 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-894 ##label BLAT !'##cross-references GB:AE000424; GB:U00096; NID:g2367230; !1PIDN:AAC76511.1; PID:g2367231; UWGP:b3486 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S47666 !$#authors Plunkett, G. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S47705 !'##status preliminary !'##molecule_type DNA !'##residues 'M',248-894 ##label PLU !'##cross-references EMBL:U00039; NID:g466582; PID:g912462 !'##note this sequence has been corrected; sequence change joins ORFs !1from this earlier version !$#accession S47706 !'##status preliminary !'##molecule_type DNA !'##residues 1-223,'XLRWKKHL' ##label PL2 !'##cross-references EMBL:U00039; NID:g466582; PID:g912463 !'##note this sequence has been corrected; sequence change joins ORFs !1from this earlier version GENETICS !$#gene yhiH; yhiH !$#start_codon GTG CLASSIFICATION #superfamily Escherichia coli probable ABC transporter yhiH; !1ATP-binding cassette homology KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$11-207 #domain ATP-binding cassette homology #label ABC1\ !$28-35 #region nucleotide-binding motif A (P-loop)\ !$275-466 #domain ATP-binding cassette homology #label ABC2\ !$292-299 #region nucleotide-binding motif A (P-loop) SUMMARY #length 894 #molecular-weight 99062 #checksum 15 SEQUENCE /// ENTRY S76566 #type complete TITLE hypothetical protein - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S76566 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76566 !'##status preliminary !'##molecule_type DNA !'##residues 1-151 ##label KAN !'##cross-references EMBL:D64002; GB:AB001339; NID:g1001612; !1PID:g1001677 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily Synechocystis sp. 17K hypothetical protein; !1ribonucleoprotein repeat homology FEATURE !$4-72 #domain ribonucleoprotein repeat homology #label RRM1 SUMMARY #length 151 #molecular-weight 16616 #checksum 4053 SEQUENCE /// ENTRY Q3ECX6 #type complete TITLE hypothetical membrane protein yiaA - Escherichia coli (strain K-12) ALTERNATE_NAMES hypothetical protein in glyQ-xylB intergenic region ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS S47783; A30267; D65155 REFERENCE S47666 !$#authors Plunkett, G. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S47783 !'##molecule_type DNA !'##residues 1-146 ##label PLU !'##cross-references EMBL:U00039; NID:g466582; PID:g912475 REFERENCE A90043 !$#authors Lawlis, V.B.; Dennis, M.S.; Chen, E.Y.; Smith, D.H.; Henner, !1D.J. !$#journal Appl. Environ. Microbiol. (1984) 47:15-21 !$#title Cloning and sequencing of the xylose isomerase and xylulose !1kinase genes of Escherichia coli. !$#cross-references MUID:84126725; PMID:6320721 !$#accession A30267 !'##molecule_type DNA !'##residues 2-146 ##label LAW !'##cross-references GB:K01996; NID:g148278; PIDN:AAA24770.1; !1PID:g148281 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65155 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-146 ##label BLAT !'##cross-references GB:AE000433; GB:U00096; NID:g1789977; !1PIDN:AAC76586.1; PID:g1789985; UWGP:b3562 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yiaA !$#map_position 80 min !$#start_codon GTG CLASSIFICATION #superfamily Escherichia coli hypothetical protein yiaA KEYWORDS membrane protein FEATURE !$15-35 #domain transmembrane #status predicted #label TM1\ !$79-100 #domain transmembrane #status predicted #label TM2\ !$106-122 #domain transmembrane #status predicted #label TM3 SUMMARY #length 146 #molecular-weight 16254 #checksum 2730 SEQUENCE /// ENTRY Q3ECX1 #type complete TITLE hypothetical protein yiaB - Escherichia coli (strain K-12) ALTERNATE_NAMES hypothetical protein f117 ORGANISM #formal_name Escherichia coli DATE 31-Mar-1989 #sequence_revision 17-Oct-1997 #text_change 01-Mar-2002 ACCESSIONS S47784; E65155; A30265 REFERENCE S47666 !$#authors Plunkett, G. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S47784 !'##status preliminary !'##molecule_type DNA !'##residues 1-117 ##label PLU !'##cross-references EMBL:U00039; NID:g466582; PIDN:AAB18540.1; !1PID:g466701 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65155 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-117 ##label BLAT !'##cross-references GB:AE000433; GB:U00096; NID:g1789977; !1PIDN:AAC76587.1; PID:g1789986; UWGP:b3563 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A90043 !$#authors Lawlis, V.B.; Dennis, M.S.; Chen, E.Y.; Smith, D.H.; Henner, !1D.J. !$#journal Appl. Environ. Microbiol. (1984) 47:15-21 !$#title Cloning and sequencing of the xylose isomerase and xylulose !1kinase genes of Escherichia coli. !$#cross-references MUID:84126725; PMID:6320721 !$#accession A30265 !'##molecule_type DNA !'##residues 1-80,'V',82-88,'DLSILMKW' ##label LAW !'##cross-references GB:X04691; NID:g43313; PIDN:CAA28396.1; PID:g43316 GENETICS !$#gene yiaB !$#map_position 80 min CLASSIFICATION #superfamily Escherichia coli hypothetical protein yiaA KEYWORDS membrane protein FEATURE !$10-30 #domain transmembrane #status predicted #label TM1\ !$70-91 #domain transmembrane #status predicted #label TM2\ !$96-113 #domain transmembrane #status predicted #label TM3 SUMMARY #length 117 #molecular-weight 13028 #checksum 2855 SEQUENCE /// ENTRY Q0ECTR #type complete TITLE hypothetical 45.2K protein (tdcR-rnpB intergenic region) - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS JU0026; JQ0615; S05361; F65101 REFERENCE A93688 !$#authors Schweizer, H.P.; Datta, P. !$#journal Nucleic Acids Res. (1989) 17:3994 !$#title The complete nucleotide sequence of the tdc region of !1Escherichia coli. !$#cross-references MUID:89282418; PMID:2660107 !$#accession JU0026 !'##molecule_type DNA !'##residues 1-185 ##label SCH !'##cross-references GB:X14430; NID:g43038; PIDN:CAA32589.1; PID:g43039 REFERENCE JQ0612 !$#authors Komine, Y.; Inokuchi, H. !$#submission submitted to JIPID, September 1990 !$#accession JQ0615 !'##molecule_type DNA !'##residues 149-395 ##label KOM !'##experimental_source strain K12, W3110 REFERENCE S05359 !$#authors Schweizer, H.P.; Datta, P. !$#journal Mol. Gen. Genet. (1989) 218:516-522 !$#title Identification and DNA sequence of tdcR, a positive !1regulatory gene of the tdc operon of Escherichia coli. !$#cross-references MUID:90066355; PMID:2573820 !$#accession S05361 !'##molecule_type DNA !'##residues 1-184 ##label SC2 !'##cross-references EMBL:X16445 !'##note the authors translated the codon GGA for residue 60 as Glu and !1GAA for residue 135 as Gln REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession F65101 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-395 ##label BLAT !'##cross-references GB:AE000393; GB:U00096; NID:g1789499; !1PIDN:AAC76156.1; PID:g1789509; UWGP:b3121 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yhaC !$#map_position 68 min CLASSIFICATION #superfamily Escherichia coli hypothetical 45.2K protein !1(tdcR-rnpB intergenic region) SUMMARY #length 395 #molecular-weight 45250 #checksum 2282 SEQUENCE /// ENTRY H65169 #type complete TITLE probable transport protein yidK - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS H65169 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65169 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-571 ##label BLAT !'##cross-references GB:AE000445; GB:U00096; NID:g1790105; !1PIDN:AAC76702.1; PID:g1790113; UWGP:b3679 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene yidK CLASSIFICATION #superfamily Escherichia coli probable transport protein !1yidK SUMMARY #length 571 #molecular-weight 62084 #checksum 8315 SEQUENCE /// ENTRY I64009 #type complete TITLE hypothetical protein HI0585 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS I64009 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession I64009 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-279 ##label TIGR !'##cross-references GB:U32740; GB:L42023; NID:g1573572; !1PIDN:AAC22249.1; PID:g1573575; TIGR:HI0585 CLASSIFICATION #superfamily Haemophilus influenzae hypothetical protein !1HI0585 SUMMARY #length 279 #molecular-weight 28990 #checksum 594 SEQUENCE /// ENTRY F71701 #type complete TITLE hypothetical protein RP431 - Rickettsia prowazekii ORGANISM #formal_name Rickettsia prowazekii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Nov-2000 ACCESSIONS F71701 REFERENCE A71630 !$#authors Andersson, S.G.E.; Zomorodipour, A.; Andersson, J.O.; !1Sicheritz-Ponten, T.; Alsmark, U.C.M.; Podowski, R.M.; !1Naeslund, A.K.; Eriksson, A.S.; Winkler, H.H.; Kurland, C.G. !$#journal Nature (1998) 396:133-140 !$#title The genome sequence of Rickettsia prowazekii and the origin !1of mitochondria. !$#cross-references MUID:99039499; PMID:9823893 !$#accession F71701 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-266 ##label AND !'##cross-references GB:AJ235271; GB:AJ235269; NID:g3868717; !1PIDN:CAA14888.1; PID:g3860988; GSPDB:GN00081 !'##experimental_source strain Madrid E GENETICS !$#gene RP431 CLASSIFICATION #superfamily Rickettsia prowazekii hypothetical protein !1RP431 SUMMARY #length 266 #molecular-weight 30551 #checksum 9038 SEQUENCE /// ENTRY S76273 #type complete TITLE hypothetical protein - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S76273 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76273 !'##status preliminary !'##molecule_type DNA !'##residues 1-373 ##label KAN !'##cross-references EMBL:D64000; GB:AB001339; NID:g1001484; !1PID:g1001500 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily Synechocystis sp. 41K hypothetical protein; !1ATP-binding cassette homology KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$21-221 #domain ATP-binding cassette homology #label ABC\ !$38-45 #region nucleotide-binding motif A (P-loop) SUMMARY #length 373 #molecular-weight 41194 #checksum 3511 SEQUENCE /// ENTRY S76423 #type complete TITLE hypothetical protein - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S76423 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76423 !'##status preliminary !'##molecule_type DNA !'##residues 1-631 ##label KAN !'##cross-references EMBL:D90915; GB:AB001339; NID:g1653604; !1PIDN:BAA18552.1; PID:g1653640 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily Synechocystis sp. 71K hypothetical protein; !1protein kinase homology FEATURE !$28-280 #domain protein kinase homology #label KIN SUMMARY #length 631 #molecular-weight 70659 #checksum 8634 SEQUENCE /// ENTRY S23413 #type complete TITLE hypothetical protein epiY' - Staphylococcus epidermidis ALTERNATE_NAMES probable ABC transporter ORGANISM #formal_name Staphylococcus epidermidis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S23413 REFERENCE S23413 !$#authors Schnell, N.; Engelke, G.; Augustin, J.; Rosenstein, R.; !1Ungermann, V.; Goetz, F.; Entian, K.D. !$#journal Eur. J. Biochem. (1992) 204:57-68 !$#title Analysis of genes involved in the biosynthesis of !1lantibiotic epidermin. !$#cross-references MUID:92155237; PMID:1740156 !$#accession S23413 !'##status preliminary !'##molecule_type DNA !'##residues 1-275 ##label SCH !'##cross-references EMBL:X62386 !'##note the authors translated the codon TTT for residue 144 as Glu, !1CTT for residue 255 as Lys, GAT for residue 256 as Leu, and !1AAA for residue 257 as Asp CLASSIFICATION #superfamily Staphylococcus epidermidis hypothetical protein SUMMARY #length 275 #molecular-weight 31847 #checksum 5462 SEQUENCE /// ENTRY B70023 #type complete TITLE conserved hypothetical protein yusY - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B70023 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B70023 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-98 ##label KUN !'##cross-references GB:Z99120; GB:AL009126; NID:g2635613; !1PIDN:CAB15286.1; PID:g2635793 !'##experimental_source strain 168 GENETICS !$#gene yusY CLASSIFICATION #superfamily Bacillus subtilis conserved hypothetical !1protein yusY SUMMARY #length 98 #molecular-weight 10834 #checksum 7715 SEQUENCE /// ENTRY G70047 #type complete TITLE conserved hypothetical protein yvrM - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS G70047 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G70047 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-253 ##label KUN !'##cross-references GB:Z99120; GB:Z99121; GB:AL009126; NID:g2635827; !1PID:g2635839; NID:g2635613; PID:g2635823 !'##experimental_source strain 168 GENETICS !$#gene yvrM CLASSIFICATION #superfamily Bacillus subtilis conserved hypothetical !1protein yvrM SUMMARY #length 253 #molecular-weight 27347 #checksum 5096 SEQUENCE /// ENTRY C70910 #type complete TITLE hypothetical protein Rv0608 - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C70910 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession C70910 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-81 ##label COL !'##cross-references GB:Z97182; GB:AL123456; NID:g3250720; !1PIDN:CAB09964.1; PID:g2222750 !'##experimental_source strain H37Rv GENETICS !$#gene Rv0608 CLASSIFICATION #superfamily Mycobacterium tuberculosis hypothetical protein !1Rv0608 SUMMARY #length 81 #molecular-weight 8813 #checksum 5149 SEQUENCE /// ENTRY C70740 #type complete TITLE hypothetical protein Rv1348 - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C70740 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession C70740 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-859 ##label COL !'##cross-references GB:Z75555; GB:AL123456; NID:g3261608; !1PIDN:CAA99981.1; PID:g1419051 !'##experimental_source strain H37Rv GENETICS !$#gene Rv1348 CLASSIFICATION #superfamily Mycobacterium tuberculosis hypothetical protein !1Rv1348; ATP-binding cassette homology KEYWORDS ATP FEATURE !$626-819 #domain ATP-binding cassette homology #label ABC SUMMARY #length 859 #molecular-weight 92965 #checksum 8548 SEQUENCE /// ENTRY D70740 #type complete TITLE hypothetical protein Rv1349 - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D70740 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession D70740 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-579 ##label COL !'##cross-references GB:Z75555; GB:AL123456; NID:g3261608; !1PIDN:CAA99982.1; PID:g1419052 !'##experimental_source strain H37Rv GENETICS !$#gene Rv1349 CLASSIFICATION #superfamily Mycobacterium tuberculosis hypothetical protein !1Rv1349; ATP-binding cassette homology KEYWORDS ATP FEATURE !$349-543 #domain ATP-binding cassette homology #label ABC SUMMARY #length 579 #molecular-weight 60954 #checksum 3047 SEQUENCE /// ENTRY A69093 #type complete TITLE hypothetical protein MTH1690 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A69093 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession A69093 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-77 ##label MTH !'##cross-references GB:AE000926; GB:AE000666; NID:g2622806; !1PIDN:AAB86162.1; PID:g2622820 !'##experimental_source strain Delta H GENETICS !$#gene MTH1690 CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum !1hypothetical protein MTH1690 SUMMARY #length 77 #molecular-weight 9092 #checksum 1496 SEQUENCE /// ENTRY G64421 #type complete TITLE hypothetical protein MJ0975 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G64421 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession G64421 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-68 ##label BUL !'##cross-references GB:U67540; GB:L77117; NID:g1591631; !1PIDN:AAB98981.1; PID:g1591638; TIGR:MJ0975 GENETICS !$#map_position REV908367-908161 CLASSIFICATION #superfamily Methanococcus jannaschii hypothetical protein !1MJ0975 SUMMARY #length 68 #molecular-weight 7656 #checksum 8338 SEQUENCE /// ENTRY A71421 #type complete TITLE hypothetical 15.5K protein - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress #variety columbia DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A71421 REFERENCE A71400 !$#authors Bevan, M.; Bancroft, I.; Bent, E.; Love, K.; Goodman, H.; !1Dean, C.; Bergkamp, R.; Dirkse, W.; Van Staveren, M.; !1Stiekema, W.; Drost, L.; Ridley, P.; Hudson, S.A.; Patel, !1K.; Murphy, G.; Piffanelli, P.; Wedler, H.; Wedler, E.; !1Wambutt, R.; Weitzenegger, T.; Pohl, T.M.; Terryn, N.; !1Gielen, J.; Villarroel, R.; De Clerck, R.; Van Montagu, M.; !1Lecharny, A.; Auborg, S.; Gy, I.; Kreis, M.; Lao, N.; !1Kavanagh, T.; Hempel, S.; Kotter, P.; Entian, K.D.; Rieger, !1M.; Schaeffer, M.; Funk, B.; Mueller-Auer, S.; Silvey, M.; !1James, R.; Montfort, A.; Pons, A.; Puigdomenech, P.; Douka, !1A.; Voukelatou, E.; Milioni, D.; Hatzopoulos, P.; Piravandi, !1E.; Obermaier, B.; Hilbert, H.; Duesterhoft, A.; Moores, T.; !1Jones, J.D.G.; Eneva, T.; Palme, K.; Benes, V.; Rechman, S.; !1Ansorge, W.; Cooke, R.; Berger, C.; Delseny, M.; Voet, M.; !1Volckaert, G.; Mewes, H.W.; Klosterman, S.; Schueller, C.; !1Chalwatzis, N. !$#journal Nature (1998) 391:485-488 !$#title Analysis of 1.9 Mb of contiguous sequence from chromosome 4 !1of Arabidopsis thaliana. !$#cross-references MUID:98121113; PMID:9461215 !$#accession A71421 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-146 ##label BEV !'##cross-references GB:Z97339; NID:g2244901; PID:g2244917 GENETICS !$#map_position 4COP9-4G3845 CLASSIFICATION #superfamily Arabidopsis thaliana hypothetical 15.5K protein SUMMARY #length 146 #molecular-weight 15540 #checksum 3080 SEQUENCE /// ENTRY S46838 #type complete TITLE hypothetical protein YHL024w - yeast (Saccharomyces cerevisiae) ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S46838 REFERENCE S46796 !$#authors Favello, T. !$#submission submitted to the EMBL Data Library, June 1994 !$#description The sequence of S. cerevisiae cosmid 9433. !$#accession S46838 !'##molecule_type DNA !'##residues 1-713 ##label FAV !'##cross-references EMBL:U11582; NID:g2289793; PID:g508760; !1GSPDB:GN00008; MIPS:YHL024w GENETICS !$#gene SGD:RIM4; MIPS:YHL024w !'##cross-references SGD:S0001016 !$#map_position 8L CLASSIFICATION #superfamily yeast hypothetical protein YHL024w; !1ribonucleoprotein repeat homology FEATURE !$92-162 #domain ribonucleoprotein repeat homology #label RRM SUMMARY #length 713 #molecular-weight 80108 #checksum 3241 SEQUENCE /// ENTRY S57789 #type complete TITLE hypothetical protein (clone ES2A) - barley ORGANISM #formal_name Hordeum vulgare #common_name barley DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S57789 REFERENCE S57787 !$#authors Speulman, E.; Salamini, F. !$#journal Plant Mol. Biol. (1995) 28:915-926 !$#title GA(3)-regulated cDNAs from Hordeum vulgare leaves. !$#cross-references MUID:95367651; PMID:7640362 !$#accession S57789 !'##status preliminary !'##molecule_type mRNA !'##residues 1-177 ##label SPE !'##cross-references EMBL:X79466; NID:g929668; PIDN:CAA55976.1; !1PID:g929669 CLASSIFICATION #superfamily barley hypothetical protein (clone ES2A) SUMMARY #length 177 #molecular-weight 18382 #checksum 4295 SEQUENCE /// ENTRY A25685 #type complete TITLE hypothetical protein ran 1+ - fission yeast (Schizosaccharomyces pombe) ORGANISM #formal_name Schizosaccharomyces pombe DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A25685 REFERENCE A25685 !$#authors McLeod, M.; Beach, D. !$#journal EMBO J. (1986) 5:3665-3671 !$#title Homology between the ran1+ gene of fission yeast and protein !1kinases. !$#cross-references MUID:87161777; PMID:3830131 !$#accession A25685 !'##molecule_type DNA !'##residues 1-470 ##label MCL !'##cross-references GB:X04728; NID:g5033; PIDN:CAA28437.1; PID:g5034 CLASSIFICATION #superfamily fission yeast hypothetical protein ran1+; !1protein kinase homology KEYWORDS serine/threonine-specific protein kinase FEATURE !$16-297 #domain protein kinase homology #label KIN SUMMARY #length 470 #molecular-weight 52169 #checksum 503 SEQUENCE /// ENTRY S62534 #type complete TITLE hypothetical protein SPAC12G12.3 - fission yeast (Schizosaccharomyces pombe) ORGANISM #formal_name Schizosaccharomyces pombe DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Dec-1999 ACCESSIONS S62534; T37598 REFERENCE S62532 !$#authors Devlin, K.; Odell, C.; Churcher, C.M. !$#submission submitted to the EMBL Data Library, November 1995 !$#accession S62534 !'##status preliminary !'##molecule_type DNA !'##residues 1-576 ##label DEV !'##cross-references EMBL:Z66568; NID:g1052518; PID:g1052521 REFERENCE Z21727 !$#authors Devlin, K.; Odell, C.; Churcher, C.M.; Barrell, B.G.; !1Rajandream, M.A.; Walsh, S.V. !$#submission submitted to the EMBL Data Library, November 1995 !$#accession T37598 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-576 ##label DE2 !'##cross-references EMBL:Z66568; PIDN:CAA91498.1; GSPDB:GN00066; !1SPDB:SPAC12G12.03 !'##experimental_source strain 972h-; cosmid c12G12 GENETICS !$#gene SPAC12G12.03 !$#map_position 1L CLASSIFICATION #superfamily fission yeast hypothetical protein SPAC12G12.3; !1ribonucleoprotein repeat homology FEATURE !$233-300 #domain ribonucleoprotein repeat homology #label RRM1 SUMMARY #length 576 #molecular-weight 62068 #checksum 3441 SEQUENCE /// ENTRY S62452 #type complete TITLE probable protein kinase SPAC22G7.08 - fission yeast (Schizosaccharomyces pombe) ORGANISM #formal_name Schizosaccharomyces pombe DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S62452; T11618 REFERENCE S62445 !$#authors Badcock, K.; Churcher, C.M. !$#submission submitted to the EMBL Data Library, October 1995 !$#accession S62452 !'##status preliminary !'##molecule_type DNA !'##residues 1-513 ##label BAD !'##cross-references EMBL:Z54328; NID:g1009451; PID:g1009458 REFERENCE Z17300 !$#authors Barrell, B.G.; Rajandream, M.A.; Walsh, S.V.; Wood, V. !$#submission submitted to the EMBL Data Library, October 1995 !$#accession T11618 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-513 ##label BAR !'##cross-references EMBL:Z54328; NID:g1009451; PID:g1009458 !'##experimental_source strain 972h(-) GENETICS !$#map_position 1L; IL !$#introns 22/3 !$#note SPAC22G7.08 CLASSIFICATION #superfamily fission yeast hypothetical protein SPAC22G7.08; !1protein kinase homology FEATURE !$239-503 #domain protein kinase homology #label KIN SUMMARY #length 513 #molecular-weight 58546 #checksum 2180 SEQUENCE /// ENTRY S49770 #type complete TITLE hypothetical protein YDR174w - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein YD9395.07 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S49770 REFERENCE S49764 !$#authors Murphy, L.; Harris, D.E. !$#submission submitted to the EMBL Data Library, November 1994 !$#accession S49770 !'##molecule_type DNA !'##residues 1-246 ##label MUR !'##cross-references EMBL:Z46727; NID:g1289283; PID:g1289289; !1GSPDB:GN00004; MIPS:YDR174w GENETICS !$#gene SGD:HMO1; MIPS:YDR174w !'##cross-references SGD:S0002581 !$#map_position 4R CLASSIFICATION #superfamily yeast hypothetical protein YDR174w; HMG box !1homology FEATURE !$103-185 #domain HMG box homology #label HMG1 SUMMARY #length 246 #molecular-weight 27544 #checksum 2494 SEQUENCE /// ENTRY S69704 #type complete TITLE hypothetical protein YDR421w - yeast (Saccharomyces cerevisiae) ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S69704 REFERENCE S69555 !$#authors Dietrich, F.S. !$#submission submitted to the EMBL Data Library, August 1995 !$#description The sequence of S. cerevisiae lambda 3641 and cosmids 9461, !19831, and 9410. !$#accession S69704 !'##molecule_type DNA !'##residues 1-950 ##label DIE !'##cross-references EMBL:U33007; NID:g927685; PID:g927697; !1GSPDB:GN00004; MIPS:YDR421w GENETICS !$#gene SGD:ARO80; MIPS:YDR421w !'##cross-references SGD:S0002829 !$#map_position 4R CLASSIFICATION #superfamily yeast hypothetical protein YDR421w; GAL4 zinc !1binuclear cluster homology FEATURE !$20-63 #domain GAL4 zinc binuclear cluster homology #label !8GAL4 SUMMARY #length 950 #molecular-weight 108204 #checksum 5486 SEQUENCE /// ENTRY S56226 #type complete TITLE hypothetical protein YFL028c - yeast (Saccharomyces cerevisiae) ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S56226 REFERENCE S56186 !$#authors Murakami, Y.; Naitou, M.; Hagiwara, H.; Shibata, T.; Ozawa, !1M.; Sasanuma, S.I.; Sasanuma, M.; Tsuchiya, Y.; Soeda, E.; !1Yokoyama, K.; Yamazaki, M.; Tashiro, H.; Eki, T. !$#submission submitted to the EMBL Data Library, May 1995 !$#description Analysis of the nucleotide sequence of chromosome VI from !1Saccaromyces cerevisiae. !$#accession S56226 !'##status preliminary !'##molecule_type DNA !'##residues 1-289 ##label MUR !'##cross-references EMBL:D50617; NID:g836685; PID:g836726; !1GSPDB:GN00006; MIPS:YFL028c GENETICS !$#gene SGD:CAF16; MIPS:YFL028c !'##cross-references SGD:S0001866; MIPS:YFL028c !$#map_position 6L CLASSIFICATION #superfamily yeast hypothetical protein YFL028c; ATP-binding !1cassette homology KEYWORDS ATP FEATURE !$24-214 #domain ATP-binding cassette homology #label ABC2 SUMMARY #length 289 #molecular-weight 33090 #checksum 8020 SEQUENCE /// ENTRY S64576 #type complete TITLE hypothetical protein YGR250c - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein G9135 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S64576; S64582 REFERENCE S64565 !$#authors Guerreiro, P.; Barreiros, T.; Azevedo, D.; !1Rodrigues-Pousada, C. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64576 !'##molecule_type DNA !'##residues 1-781 ##label GUE !'##cross-references EMBL:Z73035; NID:g1323453; PID:g1323454; !1GSPDB:GN00007; MIPS:YGR250c !'##experimental_source strain S288C REFERENCE S64577 !$#authors Agostoni Carbone, M.L.; Panzeri, L.; Melchioretto, P.; !1Carignani, G.; Feroli, F.; Frontali, L.; Mazzoni, C.; !1Rinaldi, T.; Ruzzi, M. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64582 !'##molecule_type DNA !'##residues 1-781 ##label AGO !'##cross-references EMBL:Z73035; NID:g1323453; PID:g1323454; !1GSPDB:GN00007; MIPS:YGR250c !'##experimental_source strain S288C GENETICS !$#gene MIPS:YGR250c !'##cross-references SGD:S0003482 !$#map_position 7R CLASSIFICATION #superfamily yeast hypothetical protein YGR250c; !1ribonucleoprotein repeat homology FEATURE !$541-627 #domain ribonucleoprotein repeat homology #status !8atypical #label RRM4 SUMMARY #length 781 #molecular-weight 89512 #checksum 1276 SEQUENCE /// ENTRY S62932 #type complete TITLE hypothetical protein YNL020c - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein N2823 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S62932 REFERENCE S62920 !$#authors Andre, B.; Iraqui Houssaini, I.; Urrestarazu, L.A.; Vissers, !1S. !$#submission submitted to the Protein Sequence Database, April 1996 !$#accession S62932 !'##molecule_type DNA !'##residues 1-638 ##label AND !'##cross-references EMBL:Z71296; NID:g1301848; PID:g1301849; !1GSPDB:GN00014; MIPS:YNL020c !'##experimental_source strain S288C GENETICS !$#gene SGD:ARK1; MIPS:YNL020c !'##cross-references SGD:S0004965 !$#map_position 14L CLASSIFICATION #superfamily yeast hypothetical protein YNL020c; protein !1kinase homology FEATURE !$20-298 #domain protein kinase homology #label KIN SUMMARY #length 638 #molecular-weight 71372 #checksum 6050 SEQUENCE /// ENTRY S60406 #type complete TITLE hypothetical protein YNL295w - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein N0462; hypothetical protein YNL0462 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S60406; S63271 REFERENCE S60394 !$#authors Maurer, K.C.T.; Urbanus, J.H.M.; Planta, R.J. !$#journal Yeast (1995) 11:1303-1310 !$#title Sequence analysis of a 30 kb DNA segment from yeast !1chromosome XIV carrying a ribosomal protein gene cluster, !1the genes encoding a plasma membrane protein and a subunit !1of replication factor C, and a novel putative serine/ !1threonine protein kinase gene. !$#cross-references MUID:96132033; PMID:8553702 !$#accession S60406 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-524 ##label MAU !'##cross-references EMBL:U23084; NID:g1050853; PIDN:AAC49104.1; !1PID:g1050866 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1March 1995 REFERENCE S63266 !$#authors Maurer, C.T.C.; Urbanus, J.H.M.; Planta, R.J. !$#submission submitted to the Protein Sequence Database, April 1996 !$#accession S63271 !'##molecule_type DNA !'##residues 1-524 ##label MAW !'##cross-references EMBL:Z71571; NID:g1302384; PID:g1302385; !1GSPDB:GN00014; MIPS:YNL295w !'##experimental_source strain S288C GENETICS !$#gene MIPS:YNL295w !'##cross-references SGD:S0005239 !$#map_position 14L CLASSIFICATION #superfamily yeast hypothetical protein YNL295w SUMMARY #length 524 #molecular-weight 61228 #checksum 8845 SEQUENCE /// ENTRY S51888 #type complete TITLE hypothetical protein YOL111c - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein HRE212; hypothetical protein O0732 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S51888; S59164; S66807 REFERENCE S51848 !$#authors Vandenbol, M.; Durand, P.; Portetelle, D.; Hilger, F. !$#submission submitted to the EMBL Data Library, January 1995 !$#description Sequence analysis of a 44kb DNA fragment of yeast chromosome !1XV including the Ty1-H3 retrotransposon, the suf1(+) !1frameshift suppressor gene for tRNA-Gly, the yeast transfer !1RNA-Thr-1a and a Delta. !$#accession S51888 !'##molecule_type DNA !'##residues 1-212 ##label VAN !'##cross-references EMBL:Z48149; NID:g663234; PID:g663243 REFERENCE S59156 !$#authors Vandenbol, M.; Durand, P.; Portetelle, D.; Hilger, F. !$#journal Yeast (1995) 11:1069-1075 !$#title Sequence analysis of a 44 kb DNA fragment of yeast !1chromosome XV including the Ty1-H3 retrotransposon, the suf1 !1(+) frameshift suppressor gene for tRNA-Gly, the yeast !1transfer RNA-Thr-1a and a delta element. !$#cross-references MUID:96076631; PMID:7502582 !$#accession S59164 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-212 ##label VAW !'##cross-references EMBL:Z48149; NID:g663234; PIDN:CAA88151.1; !1PID:g663243 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1995 REFERENCE S66791 !$#authors Durand, P.; Hilger, F.; Portetelle, D.; Vandenbol, M. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S66807 !'##molecule_type DNA !'##residues 1-212 ##label DUR !'##cross-references EMBL:Z74853; NID:g1419978; PID:g1419979; !1GSPDB:GN00015; MIPS:YOL111c !'##experimental_source strain S288C GENETICS !$#gene MIPS:YOL111c !'##cross-references SGD:S0005471 !$#map_position 15L CLASSIFICATION #superfamily yeast hypothetical protein YOL111c; ubiquitin !1homology FEATURE !$74-153 #domain ubiquitin homology #label UBH SUMMARY #length 212 #molecular-weight 23732 #checksum 5395 SEQUENCE /// ENTRY S61999 #type complete TITLE hypothetical protein YPL123c - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein LPH4c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S61999 REFERENCE S61996 !$#authors Schlenstedt, G.; Silver, P.A. !$#submission submitted to the EMBL Data Library, December 1995 !$#accession S61999 !'##molecule_type DNA !'##residues 1-434 ##label SCH !'##cross-references EMBL:U43503; NID:g1163087; PID:g1163091; !1GSPDB:GN00016; MIPS:YPL123c GENETICS !$#gene SGD:RNY1; MIPS:YPL123c !'##cross-references SGD:S0006044 !$#map_position 16L CLASSIFICATION #superfamily yeast hypothetical protein YPL123c SUMMARY #length 434 #molecular-weight 50171 #checksum 152 SEQUENCE /// ENTRY S61028 #type complete TITLE hypothetical protein YPL236c - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein P1057 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S61028; S65265; S65261 REFERENCE S61010 !$#authors Pohl, T.M. !$#submission submitted to the EMBL Data Library, November 1995 !$#accession S61028 !'##molecule_type DNA !'##residues 1-364 ##label POH !'##cross-references EMBL:Z67751; NID:g1061234; PID:g1061253 REFERENCE S64899 !$#authors Pohl, T.M. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S65265 !'##molecule_type DNA !'##residues 1-364 ##label POW !'##cross-references EMBL:Z73592; NID:g1370487; PID:g1370488; !1GSPDB:GN00016; MIPS:YPL236c !'##experimental_source strain S288C (AB972) REFERENCE S65251 !$#authors Urrestarazu, L.A.; Vissers, S. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S65261 !'##molecule_type DNA !'##residues 1-52 ##label URR !'##cross-references EMBL:Z73592; GSPDB:GN00016; MIPS:YPL236c !'##experimental_source strain S288C (AB972) GENETICS !$#gene MIPS:YPL236c !'##cross-references SGD:S0006157 !$#map_position 16L CLASSIFICATION #superfamily yeast hypothetical protein YPL236c; protein !1kinase homology FEATURE !$28-361 #domain protein kinase homology #label KIN SUMMARY #length 364 #molecular-weight 40748 #checksum 739 SEQUENCE /// ENTRY S45781 #type complete TITLE probable calcium-binding protein YBL047c - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein YBL0520 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S45781; S50284; S45782; S39841; S37339; S42498 REFERENCE S45745 !$#authors Goffeau, A.; Jonniaux, J.L.; Purnelle, B.; Skala, J.; de !1Wergifosse, P.; van Dyck, L. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S45781 !'##molecule_type DNA !'##residues 1-961 ##label GOF !'##cross-references EMBL:Z35808; GSPDB:GN00002; MIPS:YBL047c !'##experimental_source strain S288C REFERENCE S50284 !$#authors de Wergifosse, P.; Jacques, B.; Jonniaux, J.L.; Purnelle, !1B.; Skala, J.; Goffeau, A. !$#journal Yeast (1994) 10:1489-1496 !$#title The sequence of a 22.4 kb DNA fragment from the left arm of !1yeast chromosome II reveals homologues to bacterial proline !1synthetase and murine alpha-adaptin, as well as a new !1permease and a DNA-binding protein. !$#cross-references MUID:95176707; PMID:7871888 !$#accession S50284 !'##molecule_type DNA !'##residues 1-961 ##label DEF !'##cross-references EMBL:X78214 !'##experimental_source strain S288C REFERENCE S45782 !$#authors Dubois, E.; El Bakkoury, M.; Glansdorff, N.; Messenguy, F.; !1Pierard, A.; Scherens, B.; Vierendeels, F. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S45782 !'##molecule_type DNA !'##residues 579-1381 ##label DUB !'##cross-references EMBL:Z35808; GSPDB:GN00002; MIPS:YBL047c !'##experimental_source strain S288C REFERENCE S39824 !$#authors Scherens, B.; el Bakkoury, M.; Vierendeels, F.; Dubois, E.; !1Messenguy, F. !$#journal Yeast (1993) 9:1355-1371 !$#title Sequencing and functional analysis of a 32 560 bp segment on !1the left arm of yeast chromosome II. Identification of 26 !1open reading frames, including the KIP1 and SEC17 genes. !$#cross-references MUID:94205266; PMID:8154187 !$#accession S39841 !'##molecule_type DNA !'##residues 579-1381 ##label SCH !'##cross-references EMBL:Z23261; NID:g313733; PIDN:CAA80797.1; !1PID:g313748 !'##experimental_source strain S288C GENETICS !$#gene SGD:EDE1; MIPS:YBL047c !'##cross-references SGD:S0000143 !$#map_position 2L CLASSIFICATION #superfamily yeast probable calcium-binding protein YBL047c; !1calmodulin repeat homology KEYWORDS calcium binding; EF hand; transmembrane protein FEATURE !$167-199 #domain calmodulin repeat homology #label EF1\ !$560-576 #domain transmembrane #status predicted #label TMM SUMMARY #length 1381 #molecular-weight 150782 #checksum 381 SEQUENCE /// ENTRY S67781 #type complete TITLE probable membrane protein YDL218w - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein D0879 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S67781; S67777 REFERENCE S67778 !$#authors Rasmussen, S.W. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67781 !'##molecule_type DNA !'##residues 1-317 ##label RAS !'##cross-references EMBL:Z74266; NID:g1431365; PID:g1431366; !1GSPDB:GN00004; MIPS:YDL218w !'##experimental_source strain S288C REFERENCE S67756 !$#authors Schmidt, E.R.; Bahr, A.; Kraemer, C.; Hankeln, T.; !1Moeller-Rieker, S. !$#submission submitted to the Protein Sequence Database, July 1996 !$#accession S67777 !'##molecule_type DNA !'##residues 286-317 ##label SCH !'##cross-references EMBL:Z74266; GSPDB:GN00004; MIPS:YDL218w !'##experimental_source strain S288C GENETICS !$#gene MIPS:YDL218w !'##cross-references SGD:S0002377 !$#map_position 4L CLASSIFICATION #superfamily yeast probable membrane protein YDL218w KEYWORDS transmembrane protein FEATURE !$17-33 #domain transmembrane #status predicted #label TM1\ !$50-66 #domain transmembrane #status predicted #label TM2\ !$77-93 #domain transmembrane #status predicted #label TM3\ !$140-156 #domain transmembrane #status predicted #label TM4 SUMMARY #length 317 #molecular-weight 34449 #checksum 5393 SEQUENCE /// ENTRY S54484 #type complete TITLE probable fatty acid hydroxylase (EC 1.14.15.-) YMR272c - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YM8156.14c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S54484 REFERENCE S54014 !$#authors Lye, G.; Churcher, C.M. !$#submission submitted to the EMBL Data Library, May 1995 !$#accession S54484 !'##molecule_type DNA !'##residues 1-384 ##label LYE !'##cross-references EMBL:Z49260; NID:g809081; PID:g809095; !1GSPDB:GN00013; MIPS:YMR272c !'##experimental_source strain AB972 GENETICS !$#gene SGD:SCS7; MIPS:YMR272c !'##cross-references SGD:S0004885 !$#map_position 13R CLASSIFICATION #superfamily yeast probable membrane protein YMR272c; !1cytochrome b5 core homology KEYWORDS heme; iron; metalloprotein; oxidoreductase; transmembrane !1protein FEATURE !$9-89 #domain cytochrome b5 core homology #label CB5\ !$200-216 #domain transmembrane #status predicted #label TM1\ !$223-239 #domain transmembrane #status predicted #label TM2\ !$287-303 #domain transmembrane #status predicted #label TM3\ !$45,72 #binding_site heme iron (His) (axial ligands) #status !8predicted SUMMARY #length 384 #molecular-weight 44881 #checksum 2791 SEQUENCE /// ENTRY S63331 #type complete TITLE probable membrane protein YNR005c - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein N2036 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S63331 REFERENCE S62910 !$#authors Aert, R.; Verhasselt, P.; Voet, M.; Volckaert, G. !$#submission submitted to the Protein Sequence Database, April 1996 !$#accession S63331 !'##molecule_type DNA !'##residues 1-134 ##label AER !'##cross-references EMBL:Z71620; NID:g1302476; PID:g1302477; !1GSPDB:GN00014; MIPS:YNR005c !'##experimental_source strain S288C GENETICS !$#gene MIPS:YNR005c !'##cross-references SGD:S0005288 !$#map_position 14R CLASSIFICATION #superfamily yeast probable membrane protein YNR005c KEYWORDS transmembrane protein FEATURE !$53-69 #domain transmembrane #status predicted #label TM1\ !$111-127 #domain transmembrane #status predicted #label TM2 SUMMARY #length 134 #molecular-weight 14726 #checksum 1011 SEQUENCE /// ENTRY S28296 #type complete TITLE hypothetical protein C40H1.1 - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S28296 REFERENCE S28296 !$#authors Berks, M. !$#submission submitted to the EMBL Data Library, December 1992 !$#accession S28296 !'##molecule_type DNA !'##residues 1-372 ##label BER !'##cross-references EMBL:Z19154; NID:g6650; PID:g6651 GENETICS !$#introns 72/1; 109/1; 139/2; 252/3; 324/3 CLASSIFICATION #superfamily Caenorhabditis elegans hypothetical protein !1C40H1.1; ribonucleoprotein repeat homology FEATURE !$59-139 #domain ribonucleoprotein repeat homology #label RRM2 SUMMARY #length 372 #molecular-weight 42393 #checksum 2903 SEQUENCE /// ENTRY S20710 #type complete TITLE hypothetical protein, 16K - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S20710 REFERENCE S10451 !$#authors Bothwell, A.L.M.; Ballard, D.W.; Philbrick, W.M. !$#submission submitted to the EMBL Data Library, March 1990 !$#accession S20710 !'##status preliminary !'##molecule_type DNA !'##residues 1-573 ##label BOT !'##cross-references EMBL:X52102; NID:g53546; PID:g53547 GENETICS !$#introns 111/3 CLASSIFICATION #superfamily mouse hypothetical protein, 16K; !1ribonucleoprotein repeat homology FEATURE !$2-65 #domain ribonucleoprotein repeat homology #label !8RRM1\ !$79-138 #domain ribonucleoprotein repeat homology #label RRM2 SUMMARY #length 573 #molecular-weight 58734 #checksum 9719 SEQUENCE /// ENTRY H70414 #type complete TITLE conserved hypothetical protein aq_1328 - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS H70414 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession H70414 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-764 ##label AQF !'##cross-references GB:AE000734; GB:AE000657; NID:g2983733; !1PIDN:AAC07309.1; PID:g2983748 !'##experimental_source strain VF5 GENETICS !$#gene aq_1328 CLASSIFICATION #superfamily Aquifex aeolicus conserved hypothetical protein !1aq_1328 KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$70-77 #region nucleotide-binding motif A (P-loop)\ !$162-165 #region DEXH motif SUMMARY #length 764 #molecular-weight 88307 #checksum 4384 SEQUENCE /// ENTRY H70628 #type complete TITLE probable pknG protein - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H70628 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession H70628 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-750 ##label COL !'##cross-references GB:Z84724; GB:AL123456; NID:g3261708; !1PIDN:CAB06580.1; PID:g1817676 !'##experimental_source strain H37Rv GENETICS !$#gene pknG CLASSIFICATION #superfamily Mycobacterium tuberculosis probable pknG !1protein; protein kinase homology FEATURE !$149-393 #domain protein kinase homology #label KIN SUMMARY #length 750 #molecular-weight 81577 #checksum 3496 SEQUENCE /// ENTRY D70699 #type complete TITLE probable pknB protein - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D70699 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession D70699 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-626 ##label COL !'##cross-references GB:Z80233; GB:AL123456; NID:g3261645; !1PIDN:CAB02434.1; PID:g1552569 !'##experimental_source strain H37Rv GENETICS !$#gene pknB CLASSIFICATION #superfamily Mycobacterium tuberculosis probable pknB !1protein; protein kinase homology FEATURE !$10-274 #domain protein kinase homology #label KIN SUMMARY #length 626 #molecular-weight 66509 #checksum 7357 SEQUENCE /// ENTRY E70699 #type complete TITLE probable pknA protein - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E70699 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession E70699 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-431 ##label COL !'##cross-references GB:Z80233; GB:AL123456; NID:g3261645; !1PIDN:CAB02435.1; PID:g1552570 !'##experimental_source strain H37Rv GENETICS !$#gene pknA CLASSIFICATION #superfamily Mycobacterium tuberculosis probable pknA !1protein; protein kinase homology FEATURE !$11-272 #domain protein kinase homology #label KIN SUMMARY #length 431 #molecular-weight 45597 #checksum 7771 SEQUENCE /// ENTRY S50889 #type complete TITLE PRK1 protein - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES PAK1 protein; protein YI9910.01; protein YIL095w ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 12-Nov-1999 ACCESSIONS S50889; S59662 REFERENCE S49786 !$#authors Connor, R.; Churcher, C. !$#submission submitted to the EMBL Data Library, November 1994 !$#accession S50889 !'##molecule_type DNA !'##residues 1-810 ##label CON !'##cross-references GB:Z47047; EMBL:Z46728; NID:g603997; PID:g763251; !1GSPDB:GN00009; MIPS:YIL095w REFERENCE S59662 !$#authors Kinzler, K.W. !$#submission submitted to the EMBL Data Library, June 1995 !$#accession S59662 !'##molecule_type mRNA !'##residues 1-785,'R',787-810 ##label KINZ !'##cross-references EMBL:U24167; NID:g862487; PIDN:AAA86529.1; !1PID:g862488 GENETICS !$#gene SGD:PRK1; PAK1; MIPS:YIL095w !'##cross-references SGD:S0001357; MIPS:YIL095w !$#map_position 9L CLASSIFICATION #superfamily yeast PRK1 protein; protein kinase homology FEATURE !$20-297 #domain protein kinase homology #label KIN SUMMARY #length 810 #molecular-weight 91031 #checksum 9521 SEQUENCE /// ENTRY S69203 #type complete TITLE teichoic acid translocation ATP-binding protein tagH - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S69203; A69721 REFERENCE S69202 !$#authors Lazarevic, V.; Karamata, D. !$#journal Mol. Microbiol. (1995) 16:345-355 !$#title The tagGH operon of Bacillus subtilis 168 encodes a !1two-component ABC transporter involved in the metabolism of !1two wall teichoic acids. !$#cross-references MUID:96015447; PMID:7565096 !$#accession S69203 !'##status preliminary; nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-527 ##label LAZ !'##cross-references EMBL:U13832; NID:g755151; PIDN:AAB03363.1; !1PID:g755153 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69721 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-527 ##label KUN !'##cross-references GB:Z99122; GB:AL009126; NID:g2636029; !1PIDN:CAB15587.1; PID:g2636096 !'##experimental_source strain 168 GENETICS !$#gene tagH CLASSIFICATION #superfamily Bacillus subtilis teichoic acid ABC transporter !1tagH; ATP-binding cassette homology KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$39-218 #domain ATP-binding cassette homology #label ABC\ !$56-63 #region nucleotide-binding motif A (P-loop) SUMMARY #length 527 #molecular-weight 59243 #checksum 3826 SEQUENCE /// ENTRY D71338 #type complete TITLE probable ribose/galactose ABC transporter rbsA-2 - syphilis spirochete ORGANISM #formal_name Treponema pallidum subsp. pallidum #common_name syphilis spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS D71338 REFERENCE A71250 !$#authors Fraser, C.M.; Norris, S.J.; Weinstock, G.M.; White, O.; !1Sutton, G.G.; Dodson, R.; Gwinn, M.; Hickey, E.K.; Clayton, !1R.; Ketchum, K.A.; Sodergren, E.; Hardham, J.M.; McLeod, !1M.P.; Salzberg, S.; Peterson, J.; Khalak, H.; Richardson, !1D.; Howell, J.K.; Chidambaram, M.; Utterback, T.; McDonald, !1L.; Artiach, P.; Bowman, C.; Cotton, M.D.; Fujii, C.; !1Garland, S.; Hatch, B.; Horst, K.; Roberts, K.; Watthey, L.; !1Weidman, J.; Smith, H.O.; Venter, J.C. !$#journal Science (1998) 281:375-388 !$#title Complete genome sequence of Treponema pallidum, the syphilis !1spirochete. !$#cross-references MUID:98332770; PMID:9665876 !$#accession D71338 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-533 ##label COL !'##cross-references GB:AE001212; GB:AE000520; NID:g3322597; !1PIDN:AAC65309.1; PID:g3322598 !'##experimental_source strain Nichols GENETICS !$#gene TP0321 CLASSIFICATION #superfamily Bacillus subtilis probable ABC transporter !1yufO; ATP-binding cassette homology KEYWORDS ATP FEATURE !$20-217 #domain ATP-binding cassette homology #label ABC SUMMARY #length 533 #molecular-weight 58033 #checksum 3192 SEQUENCE /// ENTRY D70009 #type complete TITLE probable ABC transporter yufO - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS D70009 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession D70009 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-510 ##label KUN !'##cross-references GB:Z99120; GB:AL009126; NID:g2635613; !1PIDN:CAB15144.1; PID:g2635651 !'##experimental_source strain 168 GENETICS !$#gene yufO CLASSIFICATION #superfamily Bacillus subtilis probable ABC transporter !1yufO; ATP-binding cassette homology KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$20-216 #domain ATP-binding cassette homology #label ABC1\ !$37-44 #region nucleotide-binding motif A (P-loop)\ !$273-477 #domain ATP-binding cassette homology #label ABC2 SUMMARY #length 510 #molecular-weight 56300 #checksum 1370 SEQUENCE /// ENTRY D71179 #type complete TITLE probable sugar ABC transporter - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D71179 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession D71179 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-498 ##label KAW !'##cross-references GB:AP000007; NID:g3236134; PIDN:BAA30827.1; !1PID:g3258144 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1713 CLASSIFICATION #superfamily Bacillus subtilis probable ABC transporter !1yufO; ATP-binding cassette homology KEYWORDS ATP FEATURE !$20-215 #domain ATP-binding cassette homology #label ABC SUMMARY #length 498 #molecular-weight 55284 #checksum 8359 SEQUENCE /// ENTRY G69360 #type complete TITLE probable ribose ABC transporter rbsA-1 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS G69360 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession G69360 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-495 ##label KLE !'##cross-references GB:AE001042; GB:AE000782; NID:g2689365; !1PIDN:AAB90351.1; PID:g2649712; TIGR:AF0887 CLASSIFICATION #superfamily Bacillus subtilis probable ABC transporter !1yufO; ATP-binding cassette homology KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$14-210 #domain ATP-binding cassette homology #label ABC1\ !$31-38 #region nucleotide-binding motif A (P-loop)\ !$267-467 #domain ATP-binding cassette homology #label ABC2 SUMMARY #length 495 #molecular-weight 55529 #checksum 4441 SEQUENCE /// ENTRY D70184 #type complete TITLE probable ribose/galactose ABC transporter mglA - Lyme disease spirochete ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS D70184 REFERENCE A70100 !$#authors Fraser, C.M.; Casjens, S.; Huang, W.M.; Sutton, G.G.; !1Clayton, R.; Lathigra, R.; White, O.; Ketchum, K.A.; Dodson, !1R.; Hickey, E.K.; Gwinn, M.; Dougherty, B.; Tomb, J.F.; !1Fleischmann, R.D.; Richardson, D.; Peterson, J.; Kerlavage, !1A.R.; Quackenbush, J.; Salzberg, S.; Hanson, M.; Vugt, R.V.; !1Palmer, N.; Adams, M.D.; Gocayne, J.; Weidman, J.; !1Utterback, T.; Watthey, L.; McDonald, L.; Artiach, P.; !1Bowman, C.; Garland, S.; Fujii, C.; Cotton, M.D.; Horst, K.; !1Roberts, K.; Hatch, B.; Smith, H.O.; Venter, J.C. !$#journal Nature (1997) 390:580-586 !$#title Genomic sequence of a Lyme disease spirochaete, Borrelia !1burgdorferi. !$#cross-references MUID:98065943; PMID:9403685 !$#accession D70184 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-536 ##label KLE !'##cross-references GB:AE001168; GB:AE000783; NID:g2688598; !1PIDN:AAC67018.1; PID:g2688601; TIGR:BB0677 !'##experimental_source strain B31 CLASSIFICATION #superfamily Bacillus subtilis probable ABC transporter !1yufO; ATP-binding cassette homology KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$21-217 #domain ATP-binding cassette homology #label ABC1\ !$38-45 #region nucleotide-binding motif A (P-loop)\ !$274-513 #domain ATP-binding cassette homology #label ABC2 SUMMARY #length 536 #molecular-weight 60389 #checksum 6310 SEQUENCE /// ENTRY F71341 #type complete TITLE probable ribose/galactose ABC transporter rbsA-1 - syphilis spirochete ORGANISM #formal_name Treponema pallidum subsp. pallidum #common_name syphilis spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Sep-2000 ACCESSIONS F71341 REFERENCE A71250 !$#authors Fraser, C.M.; Norris, S.J.; Weinstock, G.M.; White, O.; !1Sutton, G.G.; Dodson, R.; Gwinn, M.; Hickey, E.K.; Clayton, !1R.; Ketchum, K.A.; Sodergren, E.; Hardham, J.M.; McLeod, !1M.P.; Salzberg, S.; Peterson, J.; Khalak, H.; Richardson, !1D.; Howell, J.K.; Chidambaram, M.; Utterback, T.; McDonald, !1L.; Artiach, P.; Bowman, C.; Cotton, M.D.; Fujii, C.; !1Garland, S.; Hatch, B.; Horst, K.; Roberts, K.; Watthey, L.; !1Weidman, J.; Smith, H.O.; Venter, J.C. !$#journal Science (1998) 281:375-388 !$#title Complete genome sequence of Treponema pallidum, the syphilis !1spirochete. !$#cross-references MUID:98332770; PMID:9665876 !$#accession F71341 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-516 ##label COL !'##cross-references GB:AE001210; GB:AE000520; NID:g3322571; !1PIDN:AAC65288.1; PID:g3322575 !'##experimental_source strain Nichols GENETICS !$#gene TP0300 CLASSIFICATION #superfamily Bacillus subtilis probable ABC transporter !1yufO; ATP-binding cassette homology KEYWORDS ATP FEATURE !$2-205 #domain ATP-binding cassette homology #label ABC SUMMARY #length 516 #molecular-weight 56871 #checksum 4256 SEQUENCE /// ENTRY B64816 #type complete TITLE ABC-type transport protein ybhF - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS B64816 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64816 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-583 ##label BLAT !'##cross-references GB:AE000181; GB:U00096; NID:g1786998; !1PIDN:AAC73881.1; PID:g1787012; UWGP:b0794 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ybhF CLASSIFICATION #superfamily Escherichia coli ABC transporter ybhF; !1ATP-binding cassette homology KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$28-218 #domain ATP-binding cassette homology #label ABC1\ !$45-52 #region nucleotide-binding motif A (P-loop)\ !$350-540 #domain ATP-binding cassette homology #label ABC2\ !$367-374 #region nucleotide-binding motif A (P-loop) SUMMARY #length 583 #molecular-weight 63764 #checksum 6561 SEQUENCE /// ENTRY E71536 #type complete TITLE probable transport ATP binding protein - Chlamydia trachomatis (serotype D, strain UW3/Cx) ORGANISM #formal_name Chlamydia trachomatis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS E71536 REFERENCE A71570 !$#authors Stephens, R.S.; Kalman, S.; Lammel, C.J.; Fan, J.; Marathe, !1R.; Aravind, L.; Mitchell, W.P.; Olinger, L.; Tatusov, R.L.; !1Zhao, Q.; Koonin, E.V.; Davis, R.W. !$#journal Science (1998) 282:754-759 !$#title Genome sequence of an obligate intracellular pathogen of !1humans: Chlamydia trachomatis. !$#cross-references MUID:99000809; PMID:9784136 !$#accession E71536 !'##status preliminary !'##molecule_type DNA !'##residues 1-646 ##label ARN !'##cross-references GB:AE001299; GB:AE001273; NID:g3328671; !1PID:g3328676 !'##experimental_source serotype D, strain UW-3/Cx GENETICS !$#gene msbA CLASSIFICATION #superfamily Chlamydia trachomatis probable transport ATP !1binding protein; ATP-binding cassette homology KEYWORDS ATP FEATURE !$416-609 #domain ATP-binding cassette homology #label ABC SUMMARY #length 646 #molecular-weight 72161 #checksum 1264 SEQUENCE /// ENTRY H70068 #type complete TITLE hypothetical protein ywrF - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H70068 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H70068 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-205 ##label KUN !'##cross-references GB:Z99122; GB:AL009126; NID:g2636029; !1PIDN:CAB15625.1; PID:g2636133 !'##experimental_source strain 168 GENETICS !$#gene ywrF CLASSIFICATION #superfamily Bacillus subtilis hypothetical protein ywrF SUMMARY #length 205 #molecular-weight 22584 #checksum 2106 SEQUENCE /// ENTRY G69069 #type complete TITLE hypothetical protein MTH152 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G69069 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession G69069 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-186 ##label MTH !'##cross-references GB:AE000803; GB:AE000666; NID:g2621179; !1PIDN:AAB84658.1; PID:g2621193 !'##experimental_source strain Delta H GENETICS !$#gene MTH152 !$#start_codon GTG CLASSIFICATION #superfamily Bacillus subtilis hypothetical protein ywrF SUMMARY #length 186 #molecular-weight 20323 #checksum 8928 SEQUENCE /// ENTRY D70380 #type complete TITLE hypothetical protein aq_928 - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D70380 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession D70380 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-196 ##label AQF !'##cross-references GB:AE000714; GB:AE000657; NID:g2983446; !1PIDN:AAC07037.1; PID:g2983456 !'##experimental_source strain VF5 GENETICS !$#gene aq_928 CLASSIFICATION #superfamily Bacillus subtilis hypothetical protein ywrF SUMMARY #length 196 #molecular-weight 22299 #checksum 3093 SEQUENCE /// ENTRY A69473 #type complete TITLE conserved hypothetical protein AF1786 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A69473 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession A69473 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-177 ##label KLE !'##cross-references GB:AE000979; GB:AE000782; NID:g2689302; !1PIDN:AAB89461.1; PID:g2648759; TIGR:AF1786 CLASSIFICATION #superfamily Bacillus subtilis hypothetical protein ywrF SUMMARY #length 177 #molecular-weight 19830 #checksum 3035 SEQUENCE /// ENTRY A69176 #type complete TITLE hypothetical protein MTH574 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS A69176 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession A69176 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-212 ##label MTH !'##cross-references GB:AE000839; GB:AE000666; NID:g2621637; !1PIDN:AAB85080.1; PID:g2621651 !'##experimental_source strain Delta H GENETICS !$#gene MTH574 CLASSIFICATION #superfamily Bacillus subtilis hypothetical protein ywrF SUMMARY #length 212 #molecular-weight 24236 #checksum 993 SEQUENCE /// ENTRY G64826 #type complete TITLE probable ABC transporter ybjZ - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS G64826 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64826 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-648 ##label BLAT !'##cross-references GB:AE000189; GB:U00096; NID:g1787097; !1PIDN:AAC73966.1; PID:g1787105; UWGP:b0879 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene ybjZ CLASSIFICATION #superfamily Escherichia coli probable ABC transporter ybjZ; !1ATP-binding cassette homology KEYWORDS ATP; nucleotide binding; P-loop; transmembrane protein FEATURE !$24-219 #domain ATP-binding cassette homology #label ABC\ !$41-48 #region nucleotide-binding motif A (P-loop)\ !$276-292 #domain transmembrane #status predicted #label TM1\ !$524-540 #domain transmembrane #status predicted #label TM2\ !$578-594 #domain transmembrane #status predicted #label TM3\ !$612-628 #domain transmembrane #status predicted #label TM4 SUMMARY #length 648 #molecular-weight 70702 #checksum 2618 SEQUENCE /// ENTRY H71527 #type complete TITLE probable excinuclease ABC chain A - Chlamydia trachomatis (serotype D, strain UW3/Cx) ORGANISM #formal_name Chlamydia trachomatis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS H71527 REFERENCE A71570 !$#authors Stephens, R.S.; Kalman, S.; Lammel, C.J.; Fan, J.; Marathe, !1R.; Aravind, L.; Mitchell, W.P.; Olinger, L.; Tatusov, R.L.; !1Zhao, Q.; Koonin, E.V.; Davis, R.W. !$#journal Science (1998) 282:754-759 !$#title Genome sequence of an obligate intracellular pathogen of !1humans: Chlamydia trachomatis. !$#cross-references MUID:99000809; PMID:9784136 !$#accession H71527 !'##status preliminary !'##molecule_type DNA !'##residues 1-1786 ##label ARN !'##cross-references GB:AE001306; GB:AE001273; NID:g3328748; !1PID:g3328752 !'##experimental_source serotype D, strain UW-3/Cx GENETICS !$#gene uvrA CLASSIFICATION #superfamily Chlamydia trachomatis probable excinuclease ABC !1chain A; ATP-binding cassette homology KEYWORDS ATP FEATURE !$608-883 #domain ATP-binding cassette homology #label ABCE SUMMARY #length 1786 #molecular-weight 196947 #checksum 8012 SEQUENCE /// ENTRY S77032 #type complete TITLE ABC transporter sll0778 - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein sll0778 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S77032 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S77032 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-790 ##label KAN !'##cross-references EMBL:D64005; GB:AB001339; NID:g1001779; !1PID:g1006575 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily Synechocystis ABC transporter sll0778; !1ATP-binding cassette homology KEYWORDS ATP; nucleotide binding; P-loop; transport protein FEATURE !$244-434 #domain ATP-binding cassette homology #label ABC\ !$261-268 #region nucleotide-binding motif A (P-loop) SUMMARY #length 790 #molecular-weight 87656 #checksum 7314 SEQUENCE /// ENTRY S74461 #type complete TITLE ABC transporter slr1494 - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein slr1494 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S74461 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S74461 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-613 ##label KAN !'##cross-references EMBL:D90899; GB:AB001339; NID:g1651650; !1PIDN:BAA16613.1; PID:g1651685 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily Synechocystis ABC transporter slr1494; !1ATP-binding cassette homology KEYWORDS ATP; nucleotide binding; P-loop; transport protein FEATURE !$389-591 #domain ATP-binding cassette homology #label ABC\ !$406-413 #region nucleotide-binding motif A (P-loop) SUMMARY #length 613 #molecular-weight 67786 #checksum 7193 SEQUENCE /// ENTRY T00089 #type complete TITLE ABC transporter rgpDc - Streptococcus mutans ORGANISM #formal_name Streptococcus mutans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS T00089 REFERENCE Z14108 !$#authors Yamashita, Y.; Tsukioka, Y.; Tomihisa, K.; Nakano, Y.; Koga, !1T. !$#journal J. Bacteriol. (1998) 181:5803-5807 !$#title Genes involved in cell wall localization and side chain !1formation of rhamnose-glucose polysaccharide in !1Streptococcus mutans. !$#accession T00089 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-405 ##label YAM !'##cross-references EMBL:AB010970 !'##experimental_source strain Xc GENETICS !$#gene rgpDc CLASSIFICATION #superfamily Streptococcus mutans ABC transporter rgpDc; !1ATP-binding cassette homology KEYWORDS ATP FEATURE !$47-227 #domain ATP-binding cassette homology #label ABC SUMMARY #length 405 #molecular-weight 45480 #checksum 2291 SEQUENCE /// ENTRY D70986 #type complete TITLE probable ABC transporter Rv1747 - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D70986 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession D70986 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-865 ##label COL !'##cross-references GB:Z95890; GB:AL123456; NID:g3242245; !1PIDN:CAB09333.1; PID:g2131012 !'##experimental_source strain H37Rv GENETICS !$#gene Rv1747 CLASSIFICATION #superfamily Mycobacterium tuberculosis probable ABC !1transporter Rv1747; ATP-binding cassette homology KEYWORDS ATP FEATURE !$335-528 #domain ATP-binding cassette homology #label ABC SUMMARY #length 865 #molecular-weight 92152 #checksum 8715 SEQUENCE /// ENTRY BVECHD #type complete TITLE molybdenum transport protein modC - Escherichia coli (strain K-12) ALTERNATE_NAMES molybdenum transport protein chlD ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 31-Oct-1997 #text_change 19-Jul-2002 ACCESSIONS E64812; B26871 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64812 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-352 ##label BLAT !'##cross-references GB:AE000179; GB:U00096; NID:g1786978; !1PIDN:AAC73852.1; PID:g1786981; UWGP:b0765 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A26871 !$#authors Johann, S.; Hinton, S.M. !$#journal J. Bacteriol. (1987) 169:1911-1916 !$#title Cloning and nucleotide sequence of the chlD locus. !$#cross-references MUID:87194564; PMID:3553151 !$#accession B26871 !'##molecule_type DNA !'##residues 1-243,'SALRDDR',251-268,'LRYYPHSGFRCFSWFYNRRSKP',269,'FVT', !1273,'AGKSC' ##label JOH !'##cross-references EMBL:X07875 !'##experimental_source strain K12 !'##note the authors translated the codon GAA for residue 74 as Gly GENETICS !$#gene modC; chlD !$#map_position 17 min FUNCTION !$#description nucleotide-binding protein component of the binding !1protein-dependent transport system for molybdenum CLASSIFICATION #superfamily molybdenum transport protein modC; ATP-binding !1cassette homology KEYWORDS ATP; inner membrane; molybdenum transport; nucleotide !1binding; P-loop FEATURE !$14-205 #domain ATP-binding cassette homology #label ABC\ !$31-38 #region nucleotide-binding motif A (P-loop)\ !$149-153 #region nucleotide-binding motif B SUMMARY #length 352 #molecular-weight 39102 #checksum 3708 SEQUENCE /// ENTRY C70666 #type complete TITLE probable membrane-bound ABC transporter modC - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jul-2002 ACCESSIONS C70666 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession C70666 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-369 ##label COL !'##cross-references GB:Z83859; GB:AL123456; NID:g3261678; !1PIDN:CAB06128.1; PID:g1781188 !'##experimental_source strain H37Rv GENETICS !$#gene modC CLASSIFICATION #superfamily molybdenum transport protein modC; ATP-binding !1cassette homology KEYWORDS ATP FEATURE !$14-215 #domain ATP-binding cassette homology #label ABC SUMMARY #length 369 #molecular-weight 38610 #checksum 177 SEQUENCE /// ENTRY S65587 #type complete TITLE ABC transporter strV - Streptomyces glaucescens ORGANISM #formal_name Streptomyces glaucescens DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S65587; S57561 REFERENCE S65585 !$#authors Beyer, S.; Distler, J.; Piepersberg, W. !$#journal Mol. Gen. Genet. (1996) 250:775-784 !$#title The str gene cluster for the biosynthesis of !15'-hydroxystreptomycin in Streptomyces glaucescens GLA.O !1(ETH 22794): new operons and evidence for pathway-specific !1regulation by StrR. !$#cross-references MUID:96204519; PMID:8628239 !$#accession S65587 !'##status preliminary !'##molecule_type DNA !'##residues 1-584 ##label BEY !'##cross-references EMBL:X89010; NID:g887633; PID:g887636 GENETICS !$#gene strV CLASSIFICATION #superfamily Streptomyces glaucescen ABC transporter strV; !1ATP-binding cassette homology KEYWORDS ATP FEATURE !$350-538 #domain ATP-binding cassette homology #label ABC SUMMARY #length 584 #molecular-weight 61861 #checksum 5176 SEQUENCE /// ENTRY H69424 #type complete TITLE probable iron(III) ABC transporter hemV-3 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS H69424 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession H69424 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-405 ##label KLE !'##cross-references GB:AE001007; GB:AE000782; NID:g2689330; !1PIDN:AAB89842.1; PID:g2649168; TIGR:AF1401 CLASSIFICATION #superfamily Archaeoglobus fulgidus probable iron(III) ABC !1transporter hemV-3; ATP-binding cassette homology KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$18-211 #domain ATP-binding cassette homology #label ABC\ !$35-42 #region nucleotide-binding motif A (P-loop) SUMMARY #length 405 #molecular-weight 44179 #checksum 8678 SEQUENCE /// ENTRY A69396 #type complete TITLE probable ribose ABC transporter rbsA-2 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS A69396 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession A69396 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-370 ##label KLE !'##cross-references GB:AE001023; GB:AE000782; NID:g2689346; !1PIDN:AAB90070.1; PID:g2649412; TIGR:AF1170 CLASSIFICATION #superfamily Archaeoglobus fulgidus probable ribose ABC !1transporter rbsA-2; ATP-binding cassette homology KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$22-208 #domain ATP-binding cassette homology #label ABC\ !$39-46 #region nucleotide-binding motif A (P-loop)\ !$239-246 #region nucleotide-binding motif A (P-loop) SUMMARY #length 370 #molecular-weight 41579 #checksum 124 SEQUENCE /// ENTRY D71416 #type complete TITLE probable PDR5-like ABC transporter - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress #variety columbia DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS D71416 REFERENCE A71400 !$#authors Bevan, M.; Bancroft, I.; Bent, E.; Love, K.; Goodman, H.; !1Dean, C.; Bergkamp, R.; Dirkse, W.; Van Staveren, M.; !1Stiekema, W.; Drost, L.; Ridley, P.; Hudson, S.A.; Patel, !1K.; Murphy, G.; Piffanelli, P.; Wedler, H.; Wedler, E.; !1Wambutt, R.; Weitzenegger, T.; Pohl, T.M.; Terryn, N.; !1Gielen, J.; Villarroel, R.; De Clerck, R.; Van Montagu, M.; !1Lecharny, A.; Auborg, S.; Gy, I.; Kreis, M.; Lao, N.; !1Kavanagh, T.; Hempel, S.; Kotter, P.; Entian, K.D.; Rieger, !1M.; Schaeffer, M.; Funk, B.; Mueller-Auer, S.; Silvey, M.; !1James, R.; Montfort, A.; Pons, A.; Puigdomenech, P.; Douka, !1A.; Voukelatou, E.; Milioni, D.; Hatzopoulos, P.; Piravandi, !1E.; Obermaier, B.; Hilbert, H.; Duesterhoft, A.; Moores, T.; !1Jones, J.D.G.; Eneva, T.; Palme, K.; Benes, V.; Rechman, S.; !1Ansorge, W.; Cooke, R.; Berger, C.; Delseny, M.; Voet, M.; !1Volckaert, G.; Mewes, H.W.; Klosterman, S.; Schueller, C.; !1Chalwatzis, N. !$#journal Nature (1998) 391:485-488 !$#title Analysis of 1.9 Mb of contiguous sequence from chromosome 4 !1of Arabidopsis thaliana. !$#cross-references MUID:98121113; PMID:9461215 !$#accession D71416 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-1177 ##label BEV !'##cross-references GB:Z97338; NID:g2244870; PID:g2244881 GENETICS !$#map_position 4COP9-4G3845 CLASSIFICATION #superfamily Arabidopsis thaliana probable PDR5-like ABC !1transporter; ATP-binding cassette homology KEYWORDS ATP FEATURE !$439-653 #domain ATP-binding cassette homology #label ABC2 SUMMARY #length 1177 #molecular-weight 134263 #checksum 2760 SEQUENCE /// ENTRY G71271 #type complete TITLE probable ABC transporter natA - syphilis spirochete ORGANISM #formal_name Treponema pallidum subsp. pallidum #common_name syphilis spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS G71271 REFERENCE A71250 !$#authors Fraser, C.M.; Norris, S.J.; Weinstock, G.M.; White, O.; !1Sutton, G.G.; Dodson, R.; Gwinn, M.; Hickey, E.K.; Clayton, !1R.; Ketchum, K.A.; Sodergren, E.; Hardham, J.M.; McLeod, !1M.P.; Salzberg, S.; Peterson, J.; Khalak, H.; Richardson, !1D.; Howell, J.K.; Chidambaram, M.; Utterback, T.; McDonald, !1L.; Artiach, P.; Bowman, C.; Cotton, M.D.; Fujii, C.; !1Garland, S.; Hatch, B.; Horst, K.; Roberts, K.; Watthey, L.; !1Weidman, J.; Smith, H.O.; Venter, J.C. !$#journal Science (1998) 281:375-388 !$#title Complete genome sequence of Treponema pallidum, the syphilis !1spirochete. !$#cross-references MUID:98332770; PMID:9665876 !$#accession G71271 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-268 ##label COL !'##cross-references GB:AE001257; GB:AE000520; NID:g3323182; !1PIDN:AAC65843.1; PID:g3323192 !'##experimental_source strain Nichols GENETICS !$#gene TP0881 CLASSIFICATION #superfamily syphilis spirochete probable ABC transporter !1natA; ATP-binding cassette homology KEYWORDS ATP FEATURE !$23-211 #domain ATP-binding cassette homology #label ABC SUMMARY #length 268 #molecular-weight 30045 #checksum 4861 SEQUENCE /// ENTRY B71676 #type complete TITLE probable ABC transporter msbA2 - Rickettsia prowazekii ORGANISM #formal_name Rickettsia prowazekii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 03-Nov-2000 ACCESSIONS B71676 REFERENCE A71630 !$#authors Andersson, S.G.E.; Zomorodipour, A.; Andersson, J.O.; !1Sicheritz-Ponten, T.; Alsmark, U.C.M.; Podowski, R.M.; !1Naeslund, A.K.; Eriksson, A.S.; Winkler, H.H.; Kurland, C.G. !$#journal Nature (1998) 396:133-140 !$#title The genome sequence of Rickettsia prowazekii and the origin !1of mitochondria. !$#cross-references MUID:99039499; PMID:9823893 !$#accession B71676 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-576 ##label AND !'##cross-references GB:AJ235272; GB:AJ235269; NID:g3861033; !1PIDN:CAA15132.1; PID:g3861232; GSPDB:GN00081 !'##experimental_source strain Madrid E GENETICS !$#gene msbA2; RP696 CLASSIFICATION #superfamily Rickettsia prowazekii probable ABC transporter !1msbA2; ATP-binding cassette homology KEYWORDS ATP FEATURE !$354-548 #domain ATP-binding cassette homology #label ABC SUMMARY #length 576 #molecular-weight 64927 #checksum 4607 SEQUENCE /// ENTRY B70558 #type complete TITLE probable ABC transporter cydC - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS B70558 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession B70558 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-576 ##label COL !'##cross-references GB:Z95554; GB:AL123456; NID:g3261771; !1PIDN:CAB08897.1; PID:g2113904 !'##experimental_source strain H37Rv GENETICS !$#gene cydC CLASSIFICATION #superfamily Mycobacterium tuberculosis probable ABC !1transporter cydC; ATP-binding cassette homology KEYWORDS ATP FEATURE !$358-556 #domain ATP-binding cassette homology #label ABC SUMMARY #length 576 #molecular-weight 59496 #checksum 9377 SEQUENCE /// ENTRY C70558 #type complete TITLE probable ABC transporter cydD - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C70558 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession C70558 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-527 ##label COL !'##cross-references GB:Z95554; GB:AL123456; NID:g3261771; !1PIDN:CAB08898.1; PID:g2113905 !'##experimental_source strain H37Rv GENETICS !$#gene cydD CLASSIFICATION #superfamily Mycobacterium tuberculosis probable ABC !1transporter cydD; ATP-binding cassette homology KEYWORDS ATP FEATURE !$331-525 #domain ATP-binding cassette homology #label ABC SUMMARY #length 527 #molecular-weight 54797 #checksum 9686 SEQUENCE /// ENTRY G70817 #type complete TITLE probable ABC transporter Rv1668c - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G70817 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession G70817 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-372 ##label COL !'##cross-references GB:AL022002; GB:AL123456; NID:g3261544; !1PIDN:CAA17599.1; PID:g2916967 !'##experimental_source strain H37Rv GENETICS !$#gene Rv1668c CLASSIFICATION #superfamily Mycobacterium tuberculosis probable ABC !1transporter Rv1668c; ATP-binding cassette homology KEYWORDS ATP FEATURE !$20-199 #domain ATP-binding cassette homology #label ABC SUMMARY #length 372 #molecular-weight 40339 #checksum 8843 SEQUENCE /// ENTRY G70837 #type complete TITLE probable ABC transporter Rv0194 - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G70837 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession G70837 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-1194 ##label COL !'##cross-references GB:AL021928; GB:AL123456; NID:g3261522; !1PIDN:CAA17316.1; PID:g2909592 !'##experimental_source strain H37Rv GENETICS !$#gene Rv0194 CLASSIFICATION #superfamily Mycobacterium tuberculosis probable ABC !1transporter Rv0194; ATP-binding cassette homology KEYWORDS ATP FEATURE !$350-544 #domain ATP-binding cassette homology #label ABC SUMMARY #length 1194 #molecular-weight 129249 #checksum 2174 SEQUENCE /// ENTRY JT0669 #type complete TITLE helicase II-like protein, B962L - African swine fever virus ORGANISM #formal_name African swine fever virus, ASFV DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS JT0669 REFERENCE JT0665 !$#authors Yanez, R.J.; Rodriguez, J.M.; Boursnell, M.; Rodriguez, !1J.F.; Vinuela, E. !$#journal Gene (1993) 134:161-174 !$#title Two putative African swine fever virus helicases similar to !1yeast `DEAH' pre-mRNA processing proteins and vaccinia virus !1ATPases D11L and D6R. !$#cross-references MUID:94085774; PMID:8262374 !$#accession JT0669 !'##molecule_type DNA !'##residues 1-962 ##label YAN !'##cross-references GB:U18466; NID:g780375; PIDN:AAA65302.1; !1PID:g780442 CLASSIFICATION #superfamily African swine fever virus probable helicase II !1B962L KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$56-63 #region nucleotide-binding motif A (P-loop)\ !$163-168 #region nucleotide-binding motif B\ !$167-170 #region DEAH motif SUMMARY #length 962 #molecular-weight 109629 #checksum 6464 SEQUENCE /// ENTRY G69602 #type complete TITLE late competence protein required for DNA uptake comFA - Bacillus subtilis ALTERNATE_NAMES ATP-dependent DNA helicase/translocase comF1 ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS G69602; S77620; S35011; I40387; S28597 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession G69602 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-463 ##label KUN !'##cross-references GB:Z99122; GB:AL009126; NID:g2636029; !1PIDN:CAB15564.1; PID:g2636073 !'##experimental_source strain 168 REFERENCE S77620 !$#authors Dubnau, D. !$#submission submitted to the EMBL Data Library, November 1992 !$#accession S77620 !'##molecule_type DNA !'##residues 1-463 ##label DUB !'##cross-references EMBL:Z18629; NID:g39847; PID:g580841 REFERENCE I40386 !$#authors Londono-Vallejo, J.A.; Dubnau, D. !$#journal Mol. Microbiol. (1993) 9:119-131 !$#title comF, a Bacillus subtilis late competence locus, encodes a !1protein similar to ATP-dependent RNA/DNA helicases. !$#cross-references MUID:94018599; PMID:8412657 !$#accession S35011 !'##molecule_type DNA !'##residues 108-154,156-212,214-229,231-441,443-451,453-463 ##label LON !'##cross-references EMBL:Z18629 GENETICS !$#gene comFA; comF1 !$#start_codon GTG CLASSIFICATION #superfamily Bacillus subtilis ATP-dependent DNA helicase !1comFA KEYWORDS ATP; DEAD box; DNA binding; nucleotide binding; P-loop FEATURE !$146-153 #region nucleotide-binding motif A (P-loop)\ !$229-234 #region nucleotide-binding motif B\ !$233-236 #region DEAD motif SUMMARY #length 463 #molecular-weight 52565 #checksum 3339 SEQUENCE /// ENTRY A55311 #type complete TITLE DNA helicase RECQL - human ALTERNATE_NAMES RecQ helicase homolog ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS A58836; A55311; S50114 REFERENCE A55311 !$#authors Puranam, K.L.; Blackshear, P.J. !$#journal J. Biol. Chem. (1994) 269:29838-29845 !$#title Cloning and characterization of RECQL, a potential human !1homologue of the Escherichia coli DNA helicase RecQ. !$#cross-references MUID:95050841; PMID:7961977 !$#accession A58836 !'##status nucleic acid sequence not shown; not compared with conceptual !1translation !'##molecule_type mRNA; protein !'##residues 1-659 ##label PUR !'##cross-references GB:L36140; NID:g619862; PID:g619863 !'##note this sequence from Figure 3 differs from the sequence in Figure !12 !$#accession A55311 !'##status not compared with conceptual translation !'##molecule_type mRNA; protein !'##residues 1-111,'CYAYRRWKELMLPVTSIMFRW',133-659 ##label PU2 !'##cross-references GB:L36140 !'##note this sequence is from Figure 2 and is apparently translated !1using a different reading frame between 111-Leu and 113-Phe REFERENCE S50114 !$#authors Seki, M.; Miyazawa, H.; Tada, S.; Yanagisawa, J.; Yamaoka, !1T.; Hoshino, S.; Ozawa, K.; Eki, T.; Nogami, M.; Okumura, !1K.; Taguchi, H.; Hanaoka, F.; Enomoto, T. !$#journal Nucleic Acids Res. (1994) 22:4566-4573 !$#title Molecular cloning of cDNA encoding human DNA helicase Q1 !1which has homology to Escherichia coli Rec Q helicase and !1localization of the gene at chromosome 12p12. !$#cross-references MUID:95075633; PMID:7527136 !$#accession S50114 !'##molecule_type mRNA !'##residues 'S',2-174,'A',176-452,'C',454-486,'K',488-565,'T',567-614, !1'MEEKNSGNFQKKAANMLQQSGSKNTGAKKRKIDDA' ##label SEK !'##cross-references EMBL:D37984; NID:g531242; PIDN:BAA07200.1; !1PID:g531243 GENETICS !$#gene GDB:RECQL !'##cross-references GDB:307451; OMIM:600537 !$#map_position 12p12-12p12 CLASSIFICATION #superfamily human DNA helicase RECQL; recQ helicase !1homology KEYWORDS ATP; DNA repair; nucleotide binding; nucleus; P-loop FEATURE !$113-120 #region nucleotide-binding motif A (P-loop)\ !$215-220 #region nucleotide-binding motif B\ !$219-222 #region DEXH motif\ !$439-478 #domain recQ helicase homology #label RHH SUMMARY #length 659 #molecular-weight 74829 #checksum 7084 SEQUENCE /// ENTRY F70354 #type complete TITLE ATP-dependent RNA helicase DeaD - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F70354 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession F70354 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-293 ##label AQF !'##cross-references GB:AE000698; GB:AE000657; NID:g2983224; !1PIDN:AAC06826.1; PID:g2983229 !'##experimental_source strain VF5 GENETICS !$#gene deaD CLASSIFICATION #superfamily Aquifex aeolicus ATP-dependent RNA helicase !1DeaD SUMMARY #length 293 #molecular-weight 33673 #checksum 8640 SEQUENCE /// ENTRY S56822 #type complete TITLE SKI2 protein homolog YJL050w - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein J1158 ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S56822 REFERENCE S56793 !$#authors Pohl, T.M.; Aljinovic, G. !$#submission submitted to the Protein Sequence Database, September 1995 !$#accession S56822 !'##molecule_type DNA !'##residues 1-1073 ##label TOV !'##cross-references EMBL:Z49325; NID:g1008184; PIDN:CAA89341.1; !1PID:g1008185; GSPDB:GN00010; MIPS:YJL050w GENETICS !$#gene SGD:MTR4; MIPS:YJL050w !'##cross-references SGD:S0003586; MIPS:YJL050w !$#map_position 10L CLASSIFICATION #superfamily yeast probable SKI2 protein YJL050w KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$171-178 #region nucleotide-binding motif A (P-loop)\ !$258-263 #region nucleotide-binding motif B\ !$262-265 #region DEXH motif SUMMARY #length 1073 #molecular-weight 122054 #checksum 9540 SEQUENCE /// ENTRY G71081 #type complete TITLE probable helicase protein PH0917 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS G71081 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession G71081 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-526 ##label KAW !'##cross-references GB:AP000004; NID:g3236131; PIDN:BAA30013.1; !1PID:g3257330 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0917 CLASSIFICATION #superfamily Pyrococcus horikoshii probable helicase PH0917 KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$54-61 #region nucleotide-binding motif A (P-loop)\ !$165-170 #region nucleotide-binding motif B\ !$169-172 #region DEAH motif SUMMARY #length 526 #molecular-weight 60145 #checksum 1957 SEQUENCE /// ENTRY S28762 #type complete TITLE gene Dbp73D protein - fruit fly (Drosophila melanogaster) ORGANISM #formal_name Drosophila melanogaster DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jan-2001 ACCESSIONS S28762 REFERENCE S28762 !$#authors Patterson, L.F.; Harvey, M.; Lasko, P.F. !$#journal Nucleic Acids Res. (1992) 20:3063-3067 !$#title Dbp73D, a Drosophila gene expressed in ovary, encodes a !1novel D-E-A-D box protein. !$#cross-references MUID:92319633; PMID:1620603 !$#accession S28762 !'##molecule_type DNA !'##residues 1-572 ##label PAT !'##cross-references GB:S39064; EMBL:M74824; NID:g250810; PID:g250811 GENETICS !$#gene Dbp73D !'##cross-references FlyBase:FBgn0004556 !$#introns 8/2; 282/1 CLASSIFICATION #superfamily fruit fly gene Dbp73D protein KEYWORDS ATP; nucleotide binding; nucleus; P-loop FEATURE !$190-197 #region nucleotide-binding motif A (P-loop)\ !$301-306 #region nucleotide-binding motif B\ !$305-308 #region DEAD motif SUMMARY #length 572 #molecular-weight 64730 #checksum 9431 SEQUENCE /// ENTRY A57667 #type complete TITLE pop-1 protein - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS A57667 REFERENCE A57667 !$#authors Lin, R.; Thompson, S.; Priess, J.R. !$#journal Cell (1995) 83:599-609 !$#title pop-1 encodes an HMG box protein required for the !1specification of a mesoderm precursor in early !1Caenorhabditis elegans embryos. !$#cross-references MUID:96069861; PMID:7585963 !$#accession A57667 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-438 ##label LIN !'##cross-references GB:U37532; NID:g1145288; PID:g1145289 COMMENT pop-1 is a maternal gene. GENETICS !$#gene pop-1 CLASSIFICATION #superfamily Caenorhabditis elegans pop-1 protein; HMG box !1homology FEATURE !$189-266 #domain HMG box homology #label HMG1 SUMMARY #length 438 #molecular-weight 48703 #checksum 8168 SEQUENCE /// ENTRY S69204 #type complete TITLE pheromone response factor 1 - smut fungus (Ustilago maydis) ORGANISM #formal_name Ustilago maydis #common_name corn smut DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S69204 REFERENCE S69204 !$#authors Hartmann, H.A.; Kahmann, R.; Boelker, M. !$#journal EMBO J. (1996) 15:1632-1641 !$#title The pheromone response factor coordinates filamentous growth !1and pathogenicity in Ustilago maydis. !$#cross-references MUID:96203081; PMID:8612587 !$#accession S69204 !'##status preliminary !'##molecule_type DNA !'##residues 1-840 ##label HAR !'##cross-references EMBL:U40753; NID:g3451033; PIDN:AAC32736.1; !1PID:g1117966 GENETICS !$#gene prf1 CLASSIFICATION #superfamily smut fungus pheromone response factor 1; HMG !1box homology FEATURE !$123-199 #domain HMG box homology #label HMG1 SUMMARY #length 840 #molecular-weight 91576 #checksum 1439 SEQUENCE /// ENTRY I38239 #type complete TITLE transcription factor SOX3 - human ALTERNATE_NAMES SRY (sex determining region Y)-box 3 ORGANISM #formal_name Homo sapiens #common_name man DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jan-2000 ACCESSIONS I38239; I38242; S67816 REFERENCE I38239 !$#authors Stevanovic, M.; Lovell-Badge, R.; Collignon, J.; Goodfellow, !1P.N. !$#journal Hum. Mol. Genet. (1993) 2:2013-2018 !$#title SOX3 is an X-linked gene related to SRY. !$#cross-references MUID:94154672; PMID:8111369 !$#accession I38239 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-443 ##label STE1 !'##cross-references EMBL:X71135; NID:g468790; PIDN:CAA50465.1; !1PID:g530020 !$#accession I38242 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 143-158,'P',160-218 ##label STE2 !'##cross-references EMBL:X71137; NID:g468793; PIDN:CAA50467.1; !1PID:g468794 GENETICS !$#gene GDB:SOX3; SOX-3; SOXB !'##cross-references GDB:250376; OMIM:313430 !$#map_position Xq26-Xq27 CLASSIFICATION #superfamily human SOX3 protein; HMG box homology FEATURE !$136-211 #domain HMG box homology #label HMG SUMMARY #length 443 #molecular-weight 44884 #checksum 1688 SEQUENCE /// ENTRY E71429 #type complete TITLE probable FCA gamma - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress #variety columbia DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 18-Aug-2000 ACCESSIONS E71429 REFERENCE A71400 !$#authors Bevan, M.; Bancroft, I.; Bent, E.; Love, K.; Goodman, H.; !1Dean, C.; Bergkamp, R.; Dirkse, W.; Van Staveren, M.; !1Stiekema, W.; Drost, L.; Ridley, P.; Hudson, S.A.; Patel, !1K.; Murphy, G.; Piffanelli, P.; Wedler, H.; Wedler, E.; !1Wambutt, R.; Weitzenegger, T.; Pohl, T.M.; Terryn, N.; !1Gielen, J.; Villarroel, R.; De Clerck, R.; Van Montagu, M.; !1Lecharny, A.; Auborg, S.; Gy, I.; Kreis, M.; Lao, N.; !1Kavanagh, T.; Hempel, S.; Kotter, P.; Entian, K.D.; Rieger, !1M.; Schaeffer, M.; Funk, B.; Mueller-Auer, S.; Silvey, M.; !1James, R.; Montfort, A.; Pons, A.; Puigdomenech, P.; Douka, !1A.; Voukelatou, E.; Milioni, D.; Hatzopoulos, P.; Piravandi, !1E.; Obermaier, B.; Hilbert, H.; Duesterhoft, A.; Moores, T.; !1Jones, J.D.G.; Eneva, T.; Palme, K.; Benes, V.; Rechman, S.; !1Ansorge, W.; Cooke, R.; Berger, C.; Delseny, M.; Voet, M.; !1Volckaert, G.; Mewes, H.W.; Klosterman, S.; Schueller, C.; !1Chalwatzis, N. !$#journal Nature (1998) 391:485-488 !$#title Analysis of 1.9 Mb of contiguous sequence from chromosome 4 !1of Arabidopsis thaliana. !$#cross-references MUID:98121113; PMID:9461215 !$#accession E71429 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-747 ##label BEV !'##cross-references GB:Z97340; NID:g2244950; PID:g2244986 GENETICS !$#map_position 4COP9-4G3845 CLASSIFICATION #superfamily Arabidopsis thaliana probable FCA gamma; !1ribonucleoprotein repeat homology; WW repeat homology FEATURE !$212-270 #domain ribonucleoprotein repeat homology #label !8RRM1\ !$591-628 #domain WW repeat homology #label WWR SUMMARY #length 747 #molecular-weight 81716 #checksum 8989 SEQUENCE /// ENTRY S59863 #type complete TITLE polyA binding protein II - bovine ORGANISM #formal_name Bos primigenius taurus #common_name cattle DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 05-Nov-1999 ACCESSIONS S59863 REFERENCE S59863 !$#authors Nemeth, A.; Krause, S.; Blank, D.; Jenny, A.; Jenoe, P.; !1Lustig, A.; Wahle, E. !$#journal Nucleic Acids Res. (1995) 23:4034-4041 !$#title Isolation of genomic and cDNA clones encoding bovine poly(A) !1binding protein II. !$#cross-references MUID:96071160; PMID:7479061 !$#accession S59863 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type mRNA !'##residues 1-306 ##label NEM !'##cross-references EMBL:X89969; NID:g1065677; PIDN:CAA62006.1; !1PID:g1051125 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1July 1995 CLASSIFICATION #superfamily bovine polyA binding protein II; !1ribonucleoprotein repeat homology FEATURE !$173-239 #domain ribonucleoprotein repeat homology #label RRM2 SUMMARY #length 306 #molecular-weight 32766 #checksum 8904 SEQUENCE /// ENTRY S16815 #type complete TITLE SNP1 protein - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YIL061c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S16815; S48418 REFERENCE S16815 !$#authors Smith, V.; Barrell, B.G. !$#journal EMBO J. (1991) 10:2627-2634 !$#title Cloning of a yeast U1 snRNP 70K protein homologue: !1functional conservation of an RNA-binding domain between !1humans and yeast. !$#cross-references MUID:91330888; PMID:1714384 !$#accession S16815 !'##molecule_type DNA !'##residues 1-300 ##label SMI !'##cross-references EMBL:X59986; NID:g4503; PIDN:CAA42602.1; PID:g4504 !'##experimental_source strain AB972 REFERENCE S48407 !$#authors Smith, V. !$#submission submitted to the EMBL Data Library, September 1994 !$#accession S48418 !'##molecule_type DNA !'##residues 1-300 ##label SM2 !'##cross-references GB:Z47047; EMBL:Z38060; NID:g603997; PID:g763285; !1GSPDB:GN00009; MIPS:YIL061c !'##experimental_source strain AB972 GENETICS !$#gene SGD:SNP1; MIPS:YIL061c !'##cross-references SGD:S0001323; MIPS:YIL061c !$#map_position 9L CLASSIFICATION #superfamily yeast SNP1 protein; ribonucleoprotein repeat !1homology KEYWORDS nucleus FEATURE !$108-178 #domain ribonucleoprotein repeat homology #label RRM2 SUMMARY #length 300 #molecular-weight 34447 #checksum 7255 SEQUENCE /// ENTRY S48529 #type complete TITLE NAB3 protein - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES probable RNA/ssDNA-binding protein HMD1; protein P1945; protein YPL190c ORGANISM #formal_name Saccharomyces cerevisiae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Apr-2002 ACCESSIONS S48529; S65209; S60122 REFERENCE S48529 !$#authors Wilson, S.M.; Oberdorf, A.M.; Datar, K.V.; Swedlow, J.R.; !1Paddy, M.R.; Swanson, M.S. !$#submission submitted to the EMBL Data Library, January 1994 !$#description Characterization of Nuclear Polyadenylated RNA-Binding !1Proteins from Saccharomyces cerevisiae. !$#accession S48529 !'##molecule_type DNA !'##residues 1-802 ##label WIL !'##cross-references EMBL:U05314; NID:g476219; PID:g476220 REFERENCE S65202 !$#authors Rieger, M.; Mueller-Auer, S.; Schaefer, M. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S65209 !'##molecule_type DNA !'##residues 1-802 ##label RIE !'##cross-references EMBL:Z73546; NID:g1370396; PID:g1370397; !1GSPDB:GN00016; MIPS:YPL190c !'##experimental_source strain S288C (AB972) REFERENCE S60122 !$#authors Sugimoto, K.; Matsumoto, K.; Kornberg, R.D.; Reed, S.I.; !1Wittenberg, C. !$#journal Mol. Gen. Genet. (1995) 248:712-718 !$#title Dosage suppressors of the dominant G1 cyclin mutant CLN3-2: !1identification of a yeast gene encoding a putative RNA/ssDNA !1binding protein. !$#cross-references MUID:96069710; PMID:7476874 !$#accession S60122 !'##status nucleic acid sequence not shown !'##molecule_type DNA !'##residues 1-340,'I',342-802 ##label SUG !'##cross-references GB:D37935; NID:g1235749; PID:g1235750 GENETICS !$#gene SGD:NAB3; NAB3; HMD1; MIPS:YPL190c !'##cross-references SGD:S0006111 !$#map_position 16L CLASSIFICATION #superfamily yeast NAB3 protein; ribonucleoprotein repeat !1homology KEYWORDS nucleus; RNA binding FEATURE !$331-396 #domain ribonucleoprotein repeat homology #label RRM1 SUMMARY #length 802 #molecular-weight 90438 #checksum 7656 SEQUENCE /// ENTRY S44920 #type complete TITLE ZK688.5 protein - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS S44920 REFERENCE S44913 !$#authors Wilson, R. !$#submission submitted to the EMBL Data Library, May 1993 !$#description Sequence of the C. elegans cosmid ZK688. !$#accession S44920 !'##status preliminary !'##molecule_type DNA !'##residues 1-1799 ##label WIL !'##cross-references EMBL:L16621; NID:g289775; PID:g289783 GENETICS !$#introns 40/3; 96/2; 200/2; 269/2; 357/1; 486/3; 1129/3; 1194/1; !11425/1; 1503/1; 1560/1; 1588/3; 1603/3; 1638/3; 1694/2; !11735/3 CLASSIFICATION #superfamily Caenorhabditis elegans ZK688.5 protein; !1ubiquitin homology FEATURE !$21-96 #domain ubiquitin homology #label UBH SUMMARY #length 1799 #molecular-weight 202639 #checksum 5052 SEQUENCE /// ENTRY S52657 #type complete TITLE seed biotin-containing protein SPB65 [validated] - garden pea ORGANISM #formal_name Pisum sativum #common_name garden pea DATE 01-Sep-2000 #sequence_revision 01-Sep-2000 #text_change 01-Feb-2002 ACCESSIONS S52657; S52658; S45066 REFERENCE S52657 !$#authors Duval, M.; DeRose, R.T.; Job, C.; Faucher, D.; Douce, R.; !1Job, D. !$#journal Plant Mol. Biol. (1994) 26:265-273 !$#title The major biotinyl protein from Pisum sativum seeds !1covalently binds biotin at a novel site. !$#cross-references MUID:95035998; PMID:7948875 !$#accession S52657 !'##molecule_type mRNA !'##residues 1-551 ##label DUV !'##cross-references EMBL:X75880; NID:g512401; PIDN:CAA53474.1; !1PID:g512402 !$#accession S52658 !'##molecule_type protein !'##residues 17-27;29-35;37-49;62-74;93-125;129-146 ##label DUW CLASSIFICATION #superfamily pea seed biotin-containing protein KEYWORDS biotin binding; seed FEATURE !$103 #binding_site biotin (Lys) (covalent) #status !8experimental SUMMARY #length 551 #molecular-weight 59553 #checksum 7830 SEQUENCE /// ENTRY T07064 #type complete TITLE seed biotin-containing protein LEA [validated] - soybean ORGANISM #formal_name Glycine max #common_name soybean DATE 01-Sep-2000 #sequence_revision 01-Sep-2000 #text_change 01-Feb-2002 ACCESSIONS T07064 REFERENCE Z15895 !$#authors Hsing, Y.C.; Tsou, C.H.; Hsu, T.F.; Chen, Z.Y.; Hsieh, K.L.; !1Hsieh, J.S.; Chow, T.Y. !$#journal Plant Mol. Biol. (1998) 38:481-490 !$#title Tissue- and stage-specific expression of a soybean (Glycine !1max L.) seed-maturation, biotinylated protein. !$#cross-references MUID:98418627; PMID:9747855 !$#accession T07064 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-643 ##label HSI !'##cross-references EMBL:U59626; NID:g1389896; PIDN:AAC61783.1; !1PID:g1389897 !'##experimental_source strain Shi-Shi; cotyledon CLASSIFICATION #superfamily pea seed biotin-containing protein KEYWORDS biotin binding; seed FEATURE !$125 #binding_site biotin (Lys) (covalent) #status !8predicted SUMMARY #length 643 #molecular-weight 67878 #checksum 3390 SEQUENCE /// ENTRY S24065 #type complete TITLE preprotein translocase secY [validated] - Methanococcus vannielii ORGANISM #formal_name Methanococcus vannielii DATE 18-Feb-2000 #sequence_revision 18-Feb-2000 #text_change 18-Feb-2000 ACCESSIONS S24065 REFERENCE S24065 !$#authors Auer, J.; Spicker, G.; Boeck, A. !$#journal Biochimie (1991) 73:683-688 !$#title Presence of a gene in the archaebacterium Methanococcus !1vannielii homologous to secY of eubacteria. !$#cross-references MUID:92110434; PMID:1764515 !$#accession S24065 !'##status preliminary !'##molecule_type DNA !'##residues 1-438 ##label AUE !'##cross-references EMBL:X62045; NID:g44771; PIDN:CAA43978.1; !1PID:g44772 FUNCTION !$#description essential for preprotein translocation across the !1cytoplasmic membrane [validated, MUID:92110434] !$#note Methanococcus secY protein can complement a ts mutant in !1Escherichia coli CLASSIFICATION #superfamily yeast SSH1 protein KEYWORDS protein transport; transmembrane protein FEATURE !$30-46 #domain transmembrane #status predicted #label TM1\ !$72-88 #domain transmembrane #status predicted #label TM2\ !$112-128 #domain transmembrane #status predicted #label TM3\ !$138-154 #domain transmembrane #status predicted #label TM4\ !$169-185 #domain transmembrane #status predicted #label TM5\ !$211-227 #domain transmembrane #status predicted #label TM6\ !$252-268 #domain transmembrane #status predicted #label TM7\ !$318-334 #domain transmembrane #status predicted #label TM8\ !$377-393 #domain transmembrane #status predicted #label TM9 SUMMARY #length 438 #molecular-weight 47615 #checksum 6472 SEQUENCE /// ENTRY F64359 #type complete TITLE preprotein translocase secY [similarity] - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 18-Feb-2000 #sequence_revision 18-Feb-2000 #text_change 18-Feb-2000 ACCESSIONS F64359 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession F64359 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-440 ##label BUL !'##cross-references GB:U67498; GB:L77117; NID:g1591180; PID:g1591181; !1TIGR:MJ0478; PID:g1510552 GENETICS !$#map_position FOR420364-421686 !$#start_codon TTG CLASSIFICATION #superfamily yeast SSH1 protein KEYWORDS protein transport; transmembrane protein FEATURE !$36-52 #domain transmembrane #status predicted #label TM1\ !$82-98 #domain transmembrane #status predicted #label TM2\ !$117-133 #domain transmembrane #status predicted #label TM3\ !$143-159 #domain transmembrane #status predicted #label TM4\ !$174-190 #domain transmembrane #status predicted #label TM5\ !$214-230 #domain transmembrane #status predicted #label TM6\ !$255-271 #domain transmembrane #status predicted #label TM7\ !$321-337 #domain transmembrane #status predicted #label TM8\ !$387-403 #domain transmembrane #status predicted #label TM9 SUMMARY #length 440 #molecular-weight 47931 #checksum 4764 SEQUENCE /// ENTRY B65051 #type complete TITLE hypothetical protein b2710 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS B65051 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B65051 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-479 ##label BLAT !'##cross-references GB:AE000355; GB:U00096; NID:g2367151; !1PIDN:AAC75752.1; PID:g1789064; UWGP:b2710 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily Escherichia coli hypothetical protein b2710; !1rubredoxin homology KEYWORDS iron; metalloprotein FEATURE !$425-471 #domain rubredoxin homology #label RUB\ !$428,431,461,464 #binding_site iron (Cys) #status predicted SUMMARY #length 479 #molecular-weight 54234 #checksum 5424 SEQUENCE /// ENTRY S01830 #type complete TITLE transport system permease protein P69 homolog - Mycoplasma hyorhinis ORGANISM #formal_name Mycoplasma hyorhinis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 07-Dec-1999 ACCESSIONS S01830 REFERENCE S01828 !$#authors Dudler, R.; Schmidhauser, C.; Parish, R.W.; Wettenhall, !1R.E.H.; Schmidt, T. !$#journal EMBO J. (1988) 7:3963-3970 !$#title A mycoplasma high-affinity transport system and the in vitro !1invasiveness of mouse sarcoma cells. !$#cross-references MUID:89091146; PMID:3208756 !$#accession S01830 !'##molecule_type DNA !'##residues 1-580 ##label DUD !'##cross-references EMBL:M37339; NID:g150173; PID:g150176 GENETICS !$#genetic_code SGC3 CLASSIFICATION #superfamily transport system permease protein P69 KEYWORDS transmembrane protein SUMMARY #length 580 #molecular-weight 69233 #checksum 9428 SEQUENCE /// ENTRY Q3ECTH #type complete TITLE hypothetical 40.5K protein (secB-tdh 5' region) - Escherichia coli (strain K-12) ALTERNATE_NAMES hypothetical protein f344 ORGANISM #formal_name Escherichia coli DATE 31-Mar-1989 #sequence_revision 17-Oct-1997 #text_change 03-Feb-2003 ACCESSIONS S47836; A65162; A30268; B33276 REFERENCE S47666 !$#authors Plunkett, G. !$#submission submitted to the EMBL Data Library, March 1994 !$#accession S47836 !'##status preliminary !'##molecule_type DNA !'##residues 1-344 ##label PLU !'##cross-references EMBL:U00039; NID:g466582; PIDN:AAB18592.1; !1PID:g466753 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65162 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-344 ##label BLAT !'##cross-references GB:AE000439; GB:U00096; NID:g1790036; !1PIDN:AAC76639.1; PID:g1790044; UWGP:b3615 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A94493 !$#authors Somerville, R.L.; Ravnikar, P.D.; Aronson, B.D. !$#submission submitted to the EMBL Data Library, January 1988 !$#accession A30268 !'##molecule_type DNA !'##residues 'MRAMI',9,'ALV','WK',27-76,'G',78-198 ##label SOM REFERENCE A33276 !$#authors Aronson, B.D.; Somerville, R.L.; Epperly, B.R.; Dekker, E.E. !$#journal J. Biol. Chem. (1989) 264:5226-5232 !$#title The primary structure of Escherichia coli L-threonine !1dehydrogenase. !$#cross-references MUID:89174812; PMID:2647748 !$#accession B33276 !'##status preliminary !'##molecule_type DNA !'##residues 'MI',9,'ALV','WK',27-76,'G',78-198 ##label ARO !'##cross-references EMBL:X06690 !'##note the authors translated the codon ATT for residue 184 as Ser, !1GCC for residue 185 as Cys, GGA for residue 186 as Arg, TTA !1for residue 187 as Ile, CAT for residue 188 as Thr, CAT for !1residue 189 as Ser, and CAG for residue 190 as Ser GENETICS !$#gene yibD !$#map_position 1 min CLASSIFICATION #superfamily stress response protein csbB (secB-tdh 5' !1region) SUMMARY #length 344 #molecular-weight 40524 #checksum 8505 SEQUENCE /// ENTRY BSTDY #type complete TITLE bombesin precursor - yellow-bellied toad ORGANISM #formal_name Bombina variegata #common_name yellow-bellied toad DATE 31-Dec-1991 #sequence_revision 01-Dec-2000 #text_change 08-Dec-2000 ACCESSIONS S09095; B01564; A01564 REFERENCE S09095 !$#authors Richter, K.; Egger, R.; Kreil, G. !$#journal FEBS Lett. (1990) 262:353-355 !$#title Molecular cloning of a cDNA encoding the bombesin precursor !1in skin of Bombina variegata. !$#cross-references MUID:90242964; PMID:2335218 !$#accession S09095 !'##molecule_type mRNA !'##residues 1-107 ##label RIC REFERENCE A01564 !$#authors Anastasi, A.; Erspamer, V.; Bucci, M. !$#journal Arch. Biochem. Biophys. (1972) 148:443-446 !$#title Isolation and amino acid sequences of alytesin and bombesin, !1two analogous active tetradecapeptides from the skin of !1European discoglossid frogs. !$#cross-references MUID:72163516; PMID:4537042 !$#accession B01564 !'##molecule_type protein !'##residues 42-55 ##label ANA CLASSIFICATION #superfamily ranatensin KEYWORDS amidated carboxyl end; cutaneous gland; hormone; !1neuropeptide; pyroglutamic acid; secretagogue; vasodilator FEATURE !$1-24 #domain signal sequence #status predicted #label SIG\ !$25-41 #domain amino-terminal propeptide #status predicted !8#label PRO\ !$42-55 #product bombesin #status experimental #label MAT\ !$56-107 #domain carboxyl-terminal propeptide #status !8predicted #label CPT\ !$42 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$55 #modified_site amidated carboxyl end (Met) (amide in !8mature form from following glycine) #status !8experimental SUMMARY #length 107 #molecular-weight 12341 #checksum 3699 SEQUENCE /// ENTRY B64222 #type complete TITLE heat shock protein grpE - Mycoplasma genitalium ORGANISM #formal_name Mycoplasma genitalium DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 07-Dec-1999 ACCESSIONS B64222; T09696 REFERENCE A64200 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; !1Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, !1C.A.; Venter, J.C. !$#journal Science (1995) 270:397-403 !$#title The minimal gene complement of Mycoplasma genitalium. !$#cross-references MUID:96026346; PMID:7569993 !$#accession B64222 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-217 ##label TIGR !'##cross-references GB:U39697; GB:L43967; NID:g1045878; PID:g1045886; !1TIGR:MG201 !'##experimental_source strain G-37 REFERENCE Z16818 !$#authors Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; !1Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, !1A.R.; Sutton, G.G.; Kelley, J.M.; Fritchman, J.L.; Weidman, !1J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.L.; Nguyen, !1D.T.; Utterback, T.; Saudek, D.M.; Phillips, C.A.; Merrick, !1J.M.; Tomb, J.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; !1Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Venter, J.C. !$#submission submitted to the EMBL Data Library, October 1998 !$#accession T09696 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-217 ##label FRA !'##cross-references EMBL:U39699; NID:g3844790; PID:g3844798 !'##experimental_source isolate G37 GENETICS !$#gene MG201 !$#genetic_code SGC3 CLASSIFICATION #superfamily heat shock protein grpE SUMMARY #length 217 #molecular-weight 25014 #checksum 7392 SEQUENCE /// ENTRY S73360 #type complete TITLE heat shock protein GrpE - Mycoplasma pneumoniae (strain ATCC 29342) ALTERNATE_NAMES hypothetical protein C09_orf217 ORGANISM #formal_name Mycoplasma pneumoniae #variety ATCC 29342 DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 10-Dec-1999 ACCESSIONS S73360 REFERENCE S73327 !$#authors Himmelreich, R.; Hilbert, H.; Plagens, H.; Pirkl, E.; Li, !1B.C.; Herrmann, R. !$#journal Nucleic Acids Res. (1996) 24:4420-4449 !$#title Complete sequence analysis of the genome of the bacterium !1Mycoplasma pneumoniae. !$#cross-references MUID:97105885; PMID:8948633 !$#accession S73360 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-217 ##label HIM !'##cross-references EMBL:AE000004; GB:U00089; NID:g1673671; !1PIDN:AAB95682.1; PID:g1673682 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1996 GENETICS !$#gene grpE !$#genetic_code SGC3 CLASSIFICATION #superfamily heat shock protein grpE SUMMARY #length 217 #molecular-weight 24705 #checksum 8747 SEQUENCE /// ENTRY B86676 #type complete TITLE ATP-dependent RNA helicase [imported] - Lactococcus lactis subsp. lactis (strain IL1403) ORGANISM #formal_name Lactococcus lactis subsp. lactis DATE 23-Mar-2001 #sequence_revision 23-Mar-2001 #text_change 24-Aug-2001 ACCESSIONS B86676 REFERENCE A86625 !$#authors Bolotin, A.; Wincker, P.; Mauger, S.; Jaillon, O.; Malarme, !1K.; Weissenbach, J.; Ehrlich, S.D.; Sorokin, A. !$#journal Genome Res. (2001) 11:731-753 !$#title The complete genome sequence of the lactic acid bacterium !1Lactococcus lactis ssp. lactis IL1403. !$#cross-references MUID:21235186; PMID:11337471 !$#accession B86676 !'##status preliminary !'##molecule_type DNA !'##residues 1-446 ##label STO !'##cross-references GB:AE005176; PID:g12723284; PIDN:AAK04508.1; !1GSPDB:GN00146 !'##experimental_source strain IL1403 GENETICS !$#gene rheB CLASSIFICATION #superfamily Lactococcus lactis ATP-dependent RNA helicase KEYWORDS ATP; nucleotide binding; P-loop FEATURE !$45-52 #region nucleotide-binding motif A (P-loop)\ !$148-153 #region nucleotide-binding motif B\ !$152-155 #region DEAD motif SUMMARY #length 446 #molecular-weight 50517 #checksum 7392 SEQUENCE /// ENTRY S06630 #type complete TITLE hyperglycemic hormone precursor - green crab ORGANISM #formal_name Carcinus maenas #common_name green crab, common shore crab DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Dec-1999 ACCESSIONS S06630; S74098; S74099; S05665 REFERENCE S06630 !$#authors Weidemann, W.; Gromoll, J.; Keller, R. !$#journal FEBS Lett. (1989) 257:31-34 !$#title Cloning and sequence analysis of cDNA for precursor of a !1crustacean hyperglycemic hormone. !$#cross-references MUID:90033347; PMID:2806562 !$#accession S06630 !'##molecule_type mRNA !'##residues 1-142 ##label WEI !'##cross-references EMBL:X17596; NID:g6999; PIDN:CAA35605.1; PID:g7000 REFERENCE S74098 !$#authors Chung, J.S.; Webster, S.G. !$#journal Eur. J. Biochem. (1996) 240:358-364 !$#title Does the N-terminal pyroglutamate residue have any !1physiological significance for crab hyperglycemic !1neuropeptides? !$#cross-references MUID:96439064; PMID:8841399 !$#accession S74098 !'##molecule_type protein !'##residues 67-72,'X',74-88,'X',90-91,'X',93-104,'X',106-108,'X', !1110-117,'X',119-138 ##label CHU !$#accession S74099 !'##molecule_type protein !'##residues 67-72,'X',74-88,'X',90-91,'X',93-104,'X',106-108,'X', !1110-117,'X',119-138 ##label CH2 REFERENCE S05665 !$#authors Kegel, G.; Reichwein, B.; Weese, S.; Gaus, G.; !1Peter-Katalinic, J.; Keller, R. !$#journal FEBS Lett. (1989) 255:10-14 !$#title Amino acid sequence of the crustacean hyperglycemic hormone !1(CHH) from the shore crab, Carcinus maenas. !$#cross-references MUID:90005943; PMID:2792364 !$#accession S05665 !'##molecule_type protein !'##residues 67-138 ##label KEG CLASSIFICATION #superfamily hyperglycemic hormone KEYWORDS blocked amino end; hormone; pyroglutamic acid FEATURE !$1-26 #domain signal sequence #status predicted #label SIG\ !$27-64 #region peptide C #status predicted\ !$67-142 #product hyperglycemic hormone #status predicted !8#label MAT\ !$67 #modified_site pyrrolidone carboxylic acid (Gln) (in !8mature form) #status experimental\ !$73-109,89-105, !$92-118 #disulfide_bonds #status experimental SUMMARY #length 142 #molecular-weight 16137 #checksum 3658 SEQUENCE /// ENTRY S18946 #type complete TITLE ultra high-sulfur keratin 1 - human ALTERNATE_NAMES UHS keratin; ultra high-sulfur matrix protein ORGANISM #formal_name Homo sapiens #common_name man DATE 22-Oct-1999 #sequence_revision 22-Oct-1999 #text_change 22-Oct-1999 ACCESSIONS S18946; B36686 REFERENCE S18946 !$#authors Drabent, B.; Doenecke, D. !$#submission submitted to the EMBL Data Library, December 1991 !$#description Nucleotide sequence of a Human high-sulphur keratin cDNA. !$#accession S18946 !'##molecule_type mRNA !'##residues 1-169 ##label DRA !'##cross-references EMBL:X63755; NID:g32471; PIDN:CAA45283.1; !1PID:g32472 REFERENCE A36686 !$#authors MacKinnon, P.J.; Powell, B.C.; Rogers, G.E. !$#journal J. Cell Biol. (1990) 111:2587-2600 !$#title Structure and expression of genes for a class of !1cysteine-rich proteins of the cuticle layers of !1differentiating wool and hair follicles. !$#cross-references MUID:91115951; PMID:1703541 !$#accession B36686 !'##molecule_type DNA !'##residues 1-39,'Y',41-169 ##label MAC !'##cross-references GB:X55293; NID:g34078; PIDN:CAA39005.1; PID:g34079 GENETICS !$#gene GDB:KRN1 !'##cross-references GDB:125257; OMIM:148021 !$#map_position 11q13-11q13 CLASSIFICATION #superfamily ultra-high-sulfur keratin KEYWORDS hair; tandem repeat FEATURE !$7-15 #region Ser-rich nonapeptide repeat\ !$59-68 #region Gly-rich decapeptide repeat\ !$69-78 #region Gly-rich decapeptide repeat\ !$79-88 #region Cys-rich decapeptide repeat\ !$89-97 #region Ser-rich nonapeptide repeat\ !$98-107 #region Cys-rich decapeptide repeat\ !$108-117 #region Cys-rich decapeptide repeat\ !$118-126 #region Ser-rich nonapeptide repeat\ !$127-136 #region Cys-rich decapeptide repeat\ !$137-145 #region Ser-rich nonapeptide repeat\ !$146-155 #region Cys-rich decapeptide repeat\ !$156-165 #region Cys-rich decapeptide repeat SUMMARY #length 169 #molecular-weight 16216 #checksum 1822 SEQUENCE /// ENTRY S63968 #type complete TITLE ribosomal protein S17.eR [validated] - Haloarcula marismortui ALTERNATE_NAMES ribosomal protein HS26 ORGANISM #formal_name Haloarcula marismortui DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 21-Jul-2000 ACCESSIONS S63968; S49027 REFERENCE S63964 !$#authors Engemann, S.; Noelle, R.; Herfurth, E.; Briesemeister, U.; !1Grelle, G.; Wittmann-Liebold, B. !$#journal Eur. J. Biochem. (1995) 234:24-31 !$#title Cartography of ribosomal proteins of the 30S subunit from !1the halophilic Haloarcula marismortui and complete sequence !1analysis of protein HS26. !$#cross-references MUID:96096717; PMID:8529646 !$#accession S63968 !'##molecule_type protein !'##residues 1-62 ##label ENG REFERENCE S49023 !$#authors Engemann, S.; Herfurth, E.; Briesemeister, U.; Grelle, G.; !1Wittmann-Liebold, B. !$#submission submitted to the Protein Sequence Database, November 1994 !$#description Cartography of ribosomal proteins of the 30S subunit from !1the halophilic Haloarcula marismortui. !$#accession S49027 !'##molecule_type protein !'##residues 1-30 ##label EN2 CLASSIFICATION #superfamily ribosomal protein HS26 KEYWORDS protein biosynthesis; ribosome FEATURE !$1-62 #product ribosomal protein S17.eR #status !8experimental #label MAT SUMMARY #length 62 #molecular-weight 6997 #checksum 7823 SEQUENCE /// ENTRY JC4911 #type complete TITLE ribosomal protein L10, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 01-Sep-2000 ACCESSIONS JC4911 REFERENCE JC4911 !$#authors Chan, Y.L.; Diaz, J.J.; Denoroy, L.; Madjar, J.J.; Wool, !1I.G. !$#journal Biochem. Biophys. Res. Commun. (1996) 225:952-956 !$#title The primary structure of rat ribosomal protein L10: !1Relationship to a jun-binding protein and to a putative !1wilms' tumor suppressor. !$#cross-references MUID:96374425; PMID:8780716 !$#accession JC4911 !'##molecule_type mRNA !'##residues 1-214 ##label CHA !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing !'##note the protein is designated as ribosomal protein L10 CLASSIFICATION #superfamily rat ribosomal protein L10 FEATURE !$2-214 #product ribosomal protein L10 #status experimental !8#label MAT SUMMARY #length 214 #molecular-weight 24604 #checksum 6362 SEQUENCE /// ENTRY T43436 #type complete TITLE pyridoxine 4-dehydrogenase (EC 1.1.1.65) [validated] - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES pyridoxal reductase; pyridoxin dehydrogenase; pyridoxine:NADP+ 4-oxidoreductase ORGANISM #formal_name Schizosaccharomyces pombe DATE 18-Feb-2000 #sequence_revision 18-Feb-2000 #text_change 21-Jul-2000 ACCESSIONS T43436; T43007 REFERENCE Z22512 !$#authors Ashiuchi, M.; Yagi, T. !$#submission submitted to the EMBL Data Library, November 1998 !$#description Primary structure of pyridoxal reductase from !1Schizosaccharomyces pombe. !$#accession T43436 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-333 ##label ASH !'##cross-references EMBL:AB019429; PIDN:BAA34350.1 !'##experimental_source strain IFO 0346 REFERENCE Z17323 !$#authors Yoshioka, S.; Kato, K.; Nakai, K.; Okayama, H.; Nojima, H. !$#journal DNA Res. (1997) 4:363-369 !$#title Identification of open reading frames in Schizosaccharomyces !1pombe cDNAs. !$#cross-references MUID:98162722; PMID:9501991 !$#accession T43007 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-333 ##label YOS !'##cross-references EMBL:D89205; NID:g1749617; PIDN:BAA13866.1; !1PID:g1749618 !'##experimental_source strain PR745 GENETICS !$#gene PLR FUNCTION RPH1 !$#description catalyzes the reduction of pyridoxal by NADPH to form !1pyridoxine and NADP(+) FUNCTION RPH2 !$#description pyridoxal and 2-nitrobenzaldehyde are shown as excellent !1substrates, no measurable activity was observed with short !1chain aliphatic aldehydes [validated, MUID:99367443] CLASSIFICATION #superfamily fission yeast pyridoxine 4-dehydrogenase KEYWORDS monomer; oxidoreductase SUMMARY #length 333 #molecular-weight 36933 #checksum 9548 SEQUENCE /// ENTRY QQECHD #type complete TITLE hydrogenase 1 maturation factor hyaD [similarity] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 09-Dec-2002 ACCESSIONS JV0075; E64838 REFERENCE JV0072 !$#authors Menon, N.K.; Robbins, J.; Peck Jr., H.D.; Chatelus, C.Y.; !1Choi, E.S.; Przybyla, A.E. !$#journal J. Bacteriol. (1990) 172:1969-1977 !$#title Cloning and sequencing of a putative Escherichia coli [NiFe] !1hydrogenase-1 operon containing six open reading frames. !$#cross-references MUID:90202716; PMID:2180913 !$#accession JV0075 !'##molecule_type DNA !'##residues 1-195 ##label MEN !'##cross-references GB:M34825; NID:g146419; PIDN:AAA24000.1; !1PID:g146423 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64838 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-195 ##label BLAT !'##cross-references GB:AE000199; GB:U00096; NID:g1787202; !1PIDN:AAC74060.1; PID:g1787209; UWGP:b0975 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene hyaD !$#map_position 21 min CLASSIFICATION #superfamily Ni,Fe-Hydrogenase maturation protease SUMMARY #length 195 #molecular-weight 21546 #checksum 38 SEQUENCE /// ENTRY G65085 #type complete TITLE hydrogenase 2 maturation factor hybD [similarity] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Dec-2002 ACCESSIONS G65085; D55516 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65085 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-164 ##label BLAT !'##cross-references GB:AE000382; GB:U00096; NID:g2367182; !1PIDN:AAC76029.1; PID:g1789367; UWGP:b2993 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A55516 !$#authors Menon, N.K.; Chatelus, C.Y.; Dervartanian, M.; Wendt, J.C.; !1Shanmugam, K.T.; Peck Jr., H.D.; Przybyla, A.E. !$#journal J. Bacteriol. (1994) 176:4416-4423 !$#title Cloning, sequencing, and mutational analysis of the hyb !1operon encoding Escherichia coli hydrogenase 2. !$#cross-references MUID:94292472; PMID:8021226 !$#accession D55516 !'##status preliminary !'##molecule_type DNA !'##residues 1-159,'SDS' ##label MEN !'##cross-references GB:U09177; NID:g501051; PIDN:AAA21592.1; !1PID:g544486 GENETICS !$#gene hybD CLASSIFICATION #superfamily Ni,Fe-Hydrogenase maturation protease SUMMARY #length 164 #molecular-weight 17751 #checksum 2097 SEQUENCE /// ENTRY A40591 #type complete TITLE hydrogenase maturation factor hynC [similarity] - Desulfovibrio fructosovorans ORGANISM #formal_name Desulfovibrio fructosovorans DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Dec-2002 ACCESSIONS A40591 REFERENCE A40591 !$#authors Rousset, M.; Dermoun, Z.; Wall, J.D.; Belaich, J.P. !$#journal J. Bacteriol. (1993) 175:3388-3393 !$#title Analysis of the periplasmic [NiFe] hydrogenase transcription !1unit from Desulfovibrio fructosovorans. !$#cross-references MUID:93273705; PMID:8501043 !$#accession A40591 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-164 ##label ROU GENETICS !$#gene hynC CLASSIFICATION #superfamily Ni,Fe-Hydrogenase maturation protease SUMMARY #length 164 #molecular-weight 17693 #checksum 3351 SEQUENCE /// ENTRY S39401 #type complete TITLE hydrogenase maturation factor hupD [similarity] - Bradyrhizobium japonicum ORGANISM #formal_name Bradyrhizobium japonicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Dec-2002 ACCESSIONS S39401 REFERENCE S39400 !$#authors van Soom, C.; Browaeys, J.; Verreth, C.; Vanderleyden, J. !$#journal J. Mol. Biol. (1993) 234:508-512 !$#title Nucleotide sequence analysis of four genes, hupC, hupD, hupF !1and hupG, downstream of the hydrogenase structural genes in !1Bradyrhizobium japonicum. !$#cross-references MUID:94047099; PMID:8230232 !$#accession S39401 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-193 ##label VAN !'##cross-references EMBL:Z21948; NID:g311536; PID:g311538 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1March 1993 CLASSIFICATION #superfamily Ni,Fe-Hydrogenase maturation protease SUMMARY #length 193 #molecular-weight 21429 #checksum 6514 SEQUENCE /// ENTRY B41892 #type complete TITLE hydrogenase maturation factor hupD [similarity] - Rhizobium leguminosarum ORGANISM #formal_name Rhizobium leguminosarum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Dec-2002 ACCESSIONS B41892 REFERENCE A41892 !$#authors Hidalgo, E.; Palacios, J.M.; Murillo, J.; Ruiz-Argueso, T. !$#journal J. Bacteriol. (1992) 174:4130-4139 !$#title Nucleotide sequence and characterization of four additional !1genes of the hydrogenase structural operon from Rhizobium !1leguminosarum bv. viciae. !$#cross-references MUID:92283771; PMID:1597428 !$#accession B41892 !'##status preliminary !'##molecule_type DNA !'##residues 1-202 ##label HID !'##cross-references GB:X52974; NID:g1167855; PIDN:CAA37151.1; !1PID:g48724 !'##experimental_source bv. viciae, UPM791 !'##note sequence extracted from NCBI backbone (NCBIN:106282, !1NCBIP:106286) CLASSIFICATION #superfamily Ni,Fe-Hydrogenase maturation protease SUMMARY #length 202 #molecular-weight 22047 #checksum 3183 SEQUENCE /// ENTRY S53657 #type complete TITLE hydrogenase maturation factor hupM [similarity] - Azotobacter chroococcum ORGANISM #formal_name Azotobacter chroococcum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Dec-2002 ACCESSIONS S53657 REFERENCE S53655 !$#authors Du, L.; Tibelius, K.H.; Souza, E.M.; Garg, R.P.; Yates, M.G. !$#journal J. Mol. Biol. (1994) 243:549-557 !$#title Sequences, organization and analysis of the hupZMNOQRTV !1genes from the Azotobacter chroococcum hydrogenase gene !1cluster. !$#cross-references MUID:95055698; PMID:7966281 !$#accession S53657 !'##status preliminary !'##molecule_type DNA !'##residues 1-209 ##label DUL !'##cross-references EMBL:L25315; NID:g408900; PIDN:AAA64448.1; !1PID:g408903 CLASSIFICATION #superfamily Ni,Fe-Hydrogenase maturation protease SUMMARY #length 209 #molecular-weight 22833 #checksum 7017 SEQUENCE /// ENTRY A44915 #type complete TITLE hydrogenase maturation factor hoxM [similarity] - Azotobacter vinelandii ORGANISM #formal_name Azotobacter vinelandii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Dec-2002 ACCESSIONS A44915 REFERENCE A44915 !$#authors Menon, A.L.; Mortenson, L.E.; Robson, R.L. !$#journal J. Bacteriol. (1992) 174:4549-4557 !$#title Nucleotide sequences and genetic analysis of hydrogen !1oxidation (hox) genes in Azotobacter vinelandii. !$#cross-references MUID:92325046; PMID:1624446 !$#accession A44915 !'##status preliminary !'##molecule_type DNA !'##residues 1-207 ##label MEN !'##cross-references GB:L23970; NID:g397996; PIDN:AAA19501.1; !1PID:g398000 !'##note sequence extracted from NCBI backbone (NCBIN:108128, !1NCBIP:108129) CLASSIFICATION #superfamily Ni,Fe-Hydrogenase maturation protease SUMMARY #length 207 #molecular-weight 22769 #checksum 2786 SEQUENCE /// ENTRY S32941 #type complete TITLE hydrogenase maturation factor hupD [similarity] - Rhodobacter capsulatus ORGANISM #formal_name Rhodobacter capsulatus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Dec-2002 ACCESSIONS S32941; S25686 REFERENCE S32941 !$#authors Colbeau, A.; Richaud, P.; Toussaint, B.; Caballero, F.J.; !1Elster, C.; Delphin, C.; Smith, R.L.; Chabert, J.; Vignais, !1P.M. !$#journal Mol. Microbiol. (1993) 8:15-29 !$#title Organization of the genes necessary for hydrogenase !1expression in Rhodobacter capsulatus. Sequence analysis and !1identification of two hyp regulatory mutants. !$#cross-references MUID:93268090; PMID:8497190 !$#accession S32941 !'##status preliminary !'##molecule_type DNA !'##residues 1-210 ##label COL !'##cross-references EMBL:Z15089; NID:g313868; PIDN:CAA78798.1; !1PID:g46042 GENETICS !$#gene hupD CLASSIFICATION #superfamily Ni,Fe-Hydrogenase maturation protease SUMMARY #length 210 #molecular-weight 22833 #checksum 1353 SEQUENCE /// ENTRY E43255 #type complete TITLE Ni,Fe-Hydrogenase maturation protease (EC 3.4.24.-) [validated] - Alcaligenes eutrophus ORGANISM #formal_name Alcaligenes eutrophus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 23-Dec-2002 ACCESSIONS E43255 REFERENCE A43255 !$#authors Kortluke, C.; Horstmann, K.; Schwartz, E.; Rohde, M.; !1Binsack, R.; Friedrich, B. !$#journal J. Bacteriol. (1992) 174:6277-6289 !$#title A gene complex coding for the membrane-bound hydrogenase of !1Alcaligenes eutrophus H16. !$#cross-references MUID:93015670; PMID:1383192 !$#contents H16, megaplasmid pHG1 !$#accession E43255 !'##status preliminary; not compared with conceptual translation !'##molecule_type DNA !'##residues 1-202 ##label KOR !'##cross-references GB:M96433; NID:g141932; PID:g141937 !'##note sequence extracted from NCBI backbone (NCBIP:115460) CLASSIFICATION #superfamily Ni,Fe-Hydrogenase maturation protease KEYWORDS hydrolase; metalloproteinase SUMMARY #length 202 #molecular-weight 22254 #checksum 6061 SEQUENCE /// ENTRY F70358 #type complete TITLE hydrogenase maturation factor hupD [similarity] - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 09-Dec-2002 ACCESSIONS F70358 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession F70358 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-162 ##label AQF !'##cross-references GB:AE000701; GB:AE000657; NID:g2983260; !1PIDN:AAC06858.1; PID:g2983264 !'##experimental_source strain VF5 GENETICS !$#gene hupD CLASSIFICATION #superfamily Ni,Fe-Hydrogenase maturation protease SUMMARY #length 162 #molecular-weight 18177 #checksum 501 SEQUENCE /// ENTRY XYECHM #type complete TITLE site-specific DNA-methyltransferase (adenine-specific) (EC 2.1.1.72) EcoK - Escherichia coli (strain K-12) ALTERNATE_NAMES DNA methylase M; type I restriction enzyme, EcoK, M chain; type I restriction-modification system, EcoK, M chain; type I site-specific deoxyribonuclease, EcoK, M chain ORGANISM #formal_name Escherichia coli DATE 31-Mar-1990 #sequence_revision 31-Mar-1990 #text_change 16-Aug-2002 ACCESSIONS B30375; S56575; G65249; Q10648 REFERENCE A30375 !$#authors Loenen, W.A.M.; Daniel, A.S.; Braymer, H.D.; Murray, N.E. !$#journal J. Mol. Biol. (1987) 198:159-170 !$#title Organization and sequence of the hsd genes of Escherichia !1coli K-12. !$#cross-references MUID:88118919; PMID:3323532 !$#accession B30375 !'##molecule_type DNA !'##residues 1-529 ##label LOE !'##cross-references GB:X06545; NID:g41751; PIDN:CAA29792.1; PID:g41753 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56575 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-529 ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97246.1; !1PID:g537191 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65249 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-529 ##label BLAT !'##cross-references GB:AE000505; GB:U00096; NID:g2367375; !1PIDN:AAC77305.1; PID:g1790808; UWGP:b4349 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene hsdM !$#map_position 99 min COMPLEX heterotrimer (S, R, and M chains) FUNCTION !$#description type I site-specific deoxyribonuclease, a multifunctional !1enzyme complex that requires ATP, S-adenosylmethionine, and !1Mg ion as cofactors; the site-specificity determinant for !1the catalytic activities of the enzyme CLASSIFICATION #superfamily type I site-specific deoxyribonuclease chain !1hsdM KEYWORDS methyltransferase; restriction modification system; !1S-adenosylmethionine SUMMARY #length 529 #molecular-weight 59306 #checksum 1147 SEQUENCE /// ENTRY S34504 #type complete TITLE photosystem I protein psaM - Euglena gracilis chloroplast ORGANISM #formal_name chloroplast Euglena gracilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 29-Oct-1999 ACCESSIONS S34504; S34871 REFERENCE S34494 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.; Monfort, !1A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#submission submitted to the EMBL Data Library, January 1993 !$#description The complete sequence of the Euglena gracilis chloroplast !1genome (tentative). !$#accession S34504 !'##molecule_type DNA !'##residues 1-31 ##label HAL1 !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50083.1; !1PID:g415739 REFERENCE S34862 !$#authors Hallick, R.B.; Hong, L.; Drager, R.G.; Favreau, M.R.; !1Monfort, A.; Orsat, B.; Spielmann, A.; Stutz, E. !$#journal Nucleic Acids Res. (1993) 21:3537-3544 !$#title Complete sequence of Euglena gracilis chloroplast DNA. !$#cross-references MUID:93347989; PMID:8346031 !$#accession S34871 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-31 ##label HAL2 !'##cross-references EMBL:X70810; NID:g415327; PIDN:CAA50083.1; !1PID:g415739 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1January 1993 GENETICS !$#gene psaM !$#genome chloroplast CLASSIFICATION #superfamily Euglena gracilis chloroplast photosystem I !1protein psaM KEYWORDS chloroplast; photosynthesis; photosystem I; thylakoid SUMMARY #length 31 #molecular-weight 3443 #checksum 7206 SEQUENCE /// ENTRY E65206 #type complete TITLE thiamin biosynthesis protein thiC - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 01-Mar-2002 ACCESSIONS E65206; S35117 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E65206 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-631 ##label BLAT !'##cross-references GB:AE000473; GB:U00096; NID:g2367336; !1PIDN:AAC76968.1; PID:g1790427; UWGP:b3994 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S35117 !$#authors Vander Horn, P.B.; Backstrom, A.D.; Stewart, V.; Begley, !1T.P. !$#journal J. Bacteriol. (1993) 175:982-992 !$#title Structural genes for thiamine biosynthetic enzymes !1(thiCEFGH) in Escherichia coli K-12. !$#cross-references MUID:93163063; PMID:8432721 !$#accession S35117 !'##status preliminary !'##molecule_type DNA !'##residues 1-622,'RNLPA' ##label VAN !'##cross-references EMBL:M88701; NID:g1469146; PIDN:AAB95616.1; !1PID:g414232 !'##note the authors translated the codon CAG for residue 409 as Ser GENETICS !$#gene thiC FUNCTION !$#description involved in the synthesis of !14-amino-2-methyl-5-hydroxymethylpyrimidine !$#pathway thiamin biosynthesis CLASSIFICATION #superfamily thiamin biosynthesis protein thiC KEYWORDS thiamin biosynthesis SUMMARY #length 631 #molecular-weight 70850 #checksum 8181 SEQUENCE /// ENTRY A34933 #type complete TITLE glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase (EC 2.4.1.40) A1 allele [validated] - human ALTERNATE_NAMES alpha-3-N-acetylgalactosaminyltransferase; blood-group substance A-dependent acetylgalactosaminyltransferase; glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase; histo-blood group A glycosyltransferase ORGANISM #formal_name Homo sapiens #common_name man DATE 18-Aug-2000 #sequence_revision 18-Aug-2000 #text_change 19-Jul-2002 ACCESSIONS A34933; S09593; S13173; PC1164 REFERENCE A34933 !$#authors Yamamoto, F.; Marken, J.; Tsuji, T.; White, T.; Clausen, H.; !1Hakomori, S. !$#journal J. Biol. Chem. (1990) 265:1146-1151 !$#title Cloning and characterization of DNA complementary to human !1UDP-GalNAc: Fucalpha1->2Gal alpha1->3GalNAc transferase !1(histo-blood group A transferase) mRNA. !$#cross-references MUID:90110098; PMID:2104828 !$#accession A34933 !'##molecule_type mRNA !'##residues 1-353 ##label YAM1 !'##cross-references GB:J05175; NID:g340077; PIDN:AAA36792.1; !1PID:g340078 REFERENCE S09593 !$#authors Yamamoto, F.I.; Clausen, H.; White, T.; Marken, J.; !1Hakomori, S.I. !$#journal Nature (1990) 345:229-233 !$#title Molecular genetic basis of the histo-blood group ABO system. !$#cross-references MUID:90238543; PMID:2333095 !$#accession S09593 !'##status preliminary; nucleic acid sequence not shown; not compared !1with conceptual translation !'##molecule_type mRNA !'##residues 1-353 ##label YAM2 REFERENCE S13173 !$#authors Navaratnam, N.; Findlay, J.B.C.; Keen, J.N.; Watkins, W.M. !$#journal Biochem. J. (1990) 271:93-98 !$#title Purification, properties and partial amino acid sequence of !1the blood-group-A-gene-associated !1alpha-3-N-acetylgalactosaminyltransferase from human gut !1mucosal tissue. !$#cross-references MUID:91024951; PMID:2121135 !$#accession S13173 !'##status preliminary !'##molecule_type protein !'##residues 'X',65-73,'IS',76-77 ##label NAV REFERENCE PC1164 !$#authors Kominato, Y.; McNeill, P.D.; Yamamoto, M.; Russell, M.; !1Hakomori, S.; Yamamoto, F. !$#journal Biochem. Biophys. Res. Commun. (1992) 189:154-164 !$#title Animal histo-blood group ABO genes. !$#cross-references MUID:93080551; PMID:1449469 !$#accession PC1164 !'##molecule_type DNA !'##residues 145-154,'P',156-333 ##label KOM COMMENT This enzyme forms group A blood type determinants from H !1antigen determinants found in group O blood type. Allelic !1variants are responsible for the type B determinants (see !1PIR:PC1165) and minor subtypes, for example A2 (see !1PIR:PC1120). Inactive alleles are responsible for group O !1blood types. GENETICS !$#gene GDB:ABO !'##cross-references GDB:118956; OMIM:110300 !$#map_position 9q34.1-9q34.2 COMPLEX homodimer FUNCTION !$#description transfers N-acetylgalactosamine from !1UDP-N-acetylgalactosamine to !1glycoprotein-fucosylgalactosides CLASSIFICATION #superfamily histo-blood group 1 transferase KEYWORDS glycoprotein; glycosyltransferase; Golgi apparatus; !1hexosyltransferase; polymorphism; transmembrane protein FEATURE !$1-11 #domain intracellular #status predicted #label INT\ !$12-37 #domain transmembrane #status predicted #label TMM\ !$38-353 #domain trans-Golgi network lumenal #status predicted !8#label LUM\ !$112 #binding_site carbohydrate (Asn) (covalent) #status !8predicted SUMMARY #length 353 #molecular-weight 40876 #checksum 9703 SEQUENCE /// ENTRY S24124 #type complete TITLE trimethylamine dehydrogenase (EC 1.5.99.7) [validated] - Methylophilus methylotrophus W3A1 ALTERNATE_NAMES TMADH ORGANISM #formal_name Methylophilus methylotrophus W3A1 DATE 20-Apr-2000 #sequence_revision 20-Apr-2000 #text_change 20-Apr-2000 ACCESSIONS S24124; A42423; A13543 REFERENCE S24124 !$#authors Boyd, G.; Mathews, F.S.; Packman, L.C.; Scrutton, N.S. !$#journal FEBS Lett. (1992) 308:271-276 !$#title Trimethylamine dehydrogenase of bacterium W(3)A(1). !1Molecular cloning, sequence determination and !1over-expression of the gene. !$#cross-references MUID:92371642; PMID:1505666 !$#accession S24124 !'##molecule_type DNA !'##residues 1-730 ##label BOY !'##cross-references GB:X68079; GB:S43308; NID:g44466; PIDN:CAA48212.1; !1PID:g44467 !'##note the source is designated as bacterium W3A1 REFERENCE A42423 !$#authors Barber, M.J.; Neame, P.J.; Lim, L.W.; White, S.; Matthews, !1F.S. !$#journal J. Biol. Chem. (1992) 267:6611-6619 !$#title Correlation of x-ray deduced and experimental amino acid !1sequences of trimethylamine dehydrogenase. !$#cross-references MUID:92202205; PMID:1551870 !$#contents X-ray crystallography, 2.4 angstroms !$#accession A42423 !'##status significant sequence differences !'##molecule_type protein !'##cross-references PIDN:AAB21886.1; PID:g247843 !'##note the source is designated as bacterium W3A1 !'##note sequence extracted from NCBI backbone (NCBIP:89868) REFERENCE A13543 !$#authors Kenney, W.C.; McIntire, W.; Steenkamp, D.J.; Benisek, W.F. !$#journal FEBS Lett. (1978) 85:137-140 !$#title Amino acid sequence of a cofactor peptide from !1trimethylamine dehydrogenase. !$#cross-references MUID:78084818; PMID:620783 !$#accession A13543 !'##molecule_type protein !'##residues 31-42 ##label KEN REFERENCE A52120 !$#authors Mathews, F.S.; Lim, L.W.; White, S. !$#submission submitted to the Brookhaven Protein Data Bank, October 1993 !$#cross-references PDB:2TMD !$#contents annotation; X-ray crystallography, 2.4 angstroms, residues !12-730 COMPLEX homodimer FUNCTION !$#description catalyzes the oxidative N-demethylation of trimethylamine to !1dimethylamine and formaldehyde CLASSIFICATION #superfamily Methylophilus methylotrophus W3A1 !1trimethylamine dehydrogenase KEYWORDS 4Fe-4S; flavoprotein; FMN; homodimer; iron-sulfur protein; !1metalloprotein; oxidoreductase; phosphoprotein FEATURE !$2-729 #product trimethylamine dehydrogenase #status !8experimental #label MAT\ !$392-420 #region beta-alpha-beta FMN nucleotide-binding fold\ !$31 #modified_site S-(6-FMN)-cysteine (Cys) #status !8experimental\ !$346,349,352,365 #binding_site 4Fe-4S cluster (Cys) (covalent) #status !8experimental SUMMARY #length 730 #molecular-weight 81629 #checksum 4285 SEQUENCE /// ENTRY G69308 #type complete TITLE probable 2-oxoglutarate synthase (EC 1.2.7.3) gamma chain - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 05-May-2000 ACCESSIONS G69308 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession G69308 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-187 ##label KLE !'##cross-references GB:AE001072; GB:AE000782; NID:g2689395; !1PIDN:AAB90767.1; PID:g2650158; TIGR:AF0471 CLASSIFICATION #superfamily pyruvate synthase gamma chain KEYWORDS coenzyme A; oxidoreductase SUMMARY #length 187 #molecular-weight 20637 #checksum 9090 SEQUENCE /// ENTRY G71046 #type complete TITLE probable ferredoxin oxidoreductase gamma subunit - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 21-Jul-2000 ACCESSIONS G71046 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession G71046 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-170 ##label KAW !'##cross-references GB:AP000006; NID:g3236133; PIDN:BAA30775.1; !1PID:g3258092 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1663 CLASSIFICATION #superfamily pyruvate synthase gamma chain SUMMARY #length 170 #molecular-weight 18197 #checksum 8369 SEQUENCE /// ENTRY H69114 #type complete TITLE indolepyruvate oxidoreductase, beta subunit - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 21-Jul-2000 ACCESSIONS H69114 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession H69114 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-196 ##label MTH !'##cross-references GB:AE000938; GB:AE000666; NID:g2622986; !1PIDN:AAB86319.1; PID:g2622989 !'##experimental_source strain Delta H GENETICS !$#gene MTH1853 CLASSIFICATION #superfamily pyruvate synthase gamma chain SUMMARY #length 196 #molecular-weight 20948 #checksum 779 SEQUENCE /// ENTRY E69503 #type complete TITLE indolepyruvate ferredoxin oxidoreductase, subunit beta (iorB) homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 21-Jul-2000 ACCESSIONS E69503 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession E69503 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-201 ##label KLE !'##cross-references GB:AE000963; GB:AE000782; NID:g2689286; !1PIDN:AAB89225.1; PID:g2648506; TIGR:AF2030 CLASSIFICATION #superfamily pyruvate synthase gamma chain SUMMARY #length 201 #molecular-weight 21328 #checksum 3923 SEQUENCE /// ENTRY F71246 #type complete TITLE probable indolepyruvate ferredoxin oxidoreductase beta subunit - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 21-Jul-2000 ACCESSIONS F71246 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession F71246 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-196 ##label KAW !'##cross-references GB:AP000001; NID:g3236128; PIDN:BAA29301.1; !1PID:g3256618 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0229 CLASSIFICATION #superfamily pyruvate synthase gamma chain SUMMARY #length 196 #molecular-weight 22066 #checksum 3448 SEQUENCE /// ENTRY E71124 #type complete TITLE probable indolepyruvate ferredoxin oxidoreductase beta subunit - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 21-Jul-2000 ACCESSIONS E71124 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession E71124 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-202 ##label KAW !'##cross-references GB:AP000003; NID:g3236130; PIDN:BAA29855.1; !1PID:g3257172 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0764 CLASSIFICATION #superfamily pyruvate synthase gamma chain SUMMARY #length 202 #molecular-weight 21810 #checksum 6283 SEQUENCE /// ENTRY KIECD3 #type complete TITLE aspartate kinase (EC 2.7.2.4) III, lysine-sensitive - Escherichia coli (strain K-12) ALTERNATE_NAMES aspartokinase III ORGANISM #formal_name Escherichia coli DATE 31-Mar-1988 #sequence_revision 17-Oct-1997 #text_change 21-Jun-2002 ACCESSIONS G65209; A25659; I41098 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G65209 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-449 ##label BLAT !'##cross-references GB:AE000475; GB:U00096; NID:g1790448; !1PIDN:AAC76994.1; PID:g1790455; UWGP:b4024 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A25659 !$#authors Cassan, M.; Parsot, C.; Cohen, G.N.; Patte, J.C. !$#journal J. Biol. Chem. (1986) 261:1052-1057 !$#title Nucleotide sequence of lysC gene encoding the !1lysine-sensitive aspartokinase III of Escherichia coli K12: !1evolutionary pathway leading to three isofunctional enzymes. !$#cross-references MUID:86111734; PMID:3003049 !$#accession A25659 !'##molecule_type DNA !'##residues 1-57,'C',59-400,'A',402-449 ##label CAS !'##cross-references GB:M11812; NID:g146682; PIDN:AAA24095.1; !1PID:g146683 !'##experimental_source K12 REFERENCE I41098 !$#authors Cassan, M.; Ronceray, J.; Patte, J.C. !$#journal Nucleic Acids Res. (1983) 11:6157-6166 !$#title Nucleotide sequence of the promoter region of the E. coli !1lysC gene. !$#cross-references MUID:84015362; PMID:6312411 !$#accession I41098 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-13,'AS',16-19,'E' ##label RES !'##cross-references EMBL:X00008; NID:g41937; PIDN:CAA24910.1; !1PID:g41938 COMMENT The active enzyme is a dimer of identical chains; unlike the !1other two aspartokinases (I and II) in E. coli, it is not !1part of a bifunctional protein. Its synthesis and activity !1are sensitive to lysine, which is one of the end metabolites !1of the aspartic acid family branched pathway. GENETICS !$#gene lysC !$#map_position 91 min CLASSIFICATION #superfamily aspartate kinase I; aspartate kinase homology KEYWORDS ATP; lysine biosynthesis; phosphotransferase FEATURE !$4-448 #domain aspartate kinase homology #label DKI SUMMARY #length 449 #molecular-weight 48531 #checksum 7390 SEQUENCE /// ENTRY A65165 #type complete TITLE pantothenate metabolism flavoprotein dfp - Escherichia coli (strain K-12) ALTERNATE_NAMES probable aspartate 1-decarboxylase activase ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS A65165 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65165 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-430 ##label BLAT !'##cross-references GB:AE000441; GB:U00096; NID:g1790063; !1PIDN:AAC76663.1; PID:g1790070; UWGP:b3639 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene dfp CLASSIFICATION #superfamily pantothenate metabolism flavoprotein dfp SUMMARY #length 430 #molecular-weight 46300 #checksum 1652 SEQUENCE /// ENTRY T45547 #type complete TITLE arylsulfatase activating enzyme (EC 1.-.-.-) atsB [validated] - Klebsiella pneumoniae ALTERNATE_NAMES regulatory protein astB [misnomer] ORGANISM #formal_name Klebsiella pneumoniae DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 21-Jul-2000 ACCESSIONS T45547; A35159 REFERENCE Z23004 !$#authors Szameit, C.; Miech, C.; Balleininger, M.; Schmidt, B.; von !1Figura, K.; Dierks, T. !$#journal J. Biol. Chem. (1999) 274:15375-15381 !$#title The iron sulfur protein AtsB is required for !1posttranslational formation of formylglycine in the !1Klebsiella sulfatase. !$#cross-references MUID:99269066; PMID:10336424 !$#accession T45547 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-395 ##label SZA !'##cross-references EMBL:AJ131525; PIDN:CAB40960.1 !'##experimental_source DSM 681 REFERENCE A35159 !$#authors Murooka, Y.; Ishibashi, K.; Yasumoto, M.; Sasaki, M.; !1Sugino, H.; Azakami, H.; Yamashita, M. !$#journal J. Bacteriol. (1990) 172:2131-2140 !$#title A sulfur- and tyramine-regulated Klebsiella aerogenes operon !1containing the arylsulfatase (atsA) gene and the atsB gene. !$#cross-references MUID:90202736; PMID:2180918 !$#accession A35159 !'##status preliminary !'##molecule_type DNA !'##residues 1-139,'S',141-196,'D',198-283,'P',285-296,'A',298-392, !1'AYCVAPYPDDIPL' ##label MUR !'##cross-references GB:M31938; NID:g149164; PIDN:AAA25050.1; !1PID:g149165 GENETICS !$#gene atsB FUNCTION !$#description catalyzes the activation of arylsulfatase atsA by oxidizing !1a serine residue to 3-oxoalanine [validated, MUID:99269066] CLASSIFICATION #superfamily arylsulfatase activating enzyme atsB KEYWORDS iron-sulfur protein; metalloprotein; oxidoreductase FEATURE !$35,39,42,331,334, !$340,344 #binding_site iron-sulfur clusters (Cys) (covalent) !8#status predicted SUMMARY #length 395 #molecular-weight 44236 #checksum 574 SEQUENCE /// ENTRY C64328 #type complete TITLE conserved hypothetical protein MJ0226 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C64328 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession C64328 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-193 ##label BUL !'##cross-references GB:U67478; GB:L77117; NID:g1590958; !1PIDN:AAB98211.1; PID:g1590963; TIGR:MJ0226 GENETICS !$#map_position FOR216394-216975 !$#start_codon TTG CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0226 SUMMARY #length 193 #molecular-weight 22202 #checksum 736 SEQUENCE /// ENTRY C71206 #type complete TITLE hypothetical protein PH1917 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C71206 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession C71206 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-186 ##label KAW !'##cross-references GB:AP000007; NID:g3236134; PIDN:BAA31042.1; !1PID:g3258359 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1917 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0226 SUMMARY #length 186 #molecular-weight 21205 #checksum 4298 SEQUENCE /// ENTRY E69529 #type complete TITLE HAM1 protein homolog - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 29-Sep-1999 ACCESSIONS E69529 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession E69529 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-181 ##label KLE !'##cross-references GB:AE000950; GB:AE000782; NID:g2689273; !1PIDN:AAB89015.1; PID:g2648284; TIGR:AF2237 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0226 SUMMARY #length 181 #molecular-weight 20953 #checksum 7010 SEQUENCE /// ENTRY G69056 #type complete TITLE conserved hypothetical protein MTH1424 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 29-Sep-1999 ACCESSIONS G69056 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession G69056 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-187 ##label MTH !'##cross-references GB:AE000904; GB:AE000666; NID:g2622528; !1PIDN:AAB85901.1; PID:g2622537 !'##experimental_source strain Delta H GENETICS !$#gene MTH1424 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0226 SUMMARY #length 187 #molecular-weight 21127 #checksum 3865 SEQUENCE /// ENTRY S76403 #type complete TITLE hypothetical protein - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S76403 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76403 !'##status preliminary !'##molecule_type DNA !'##residues 1-194 ##label KAN !'##cross-references EMBL:D90915; GB:AB001339; NID:g1653604; !1PIDN:BAA18532.1; PID:g1653620 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0226 SUMMARY #length 194 #molecular-weight 21188 #checksum 5824 SEQUENCE /// ENTRY C69986 #type complete TITLE conserved hypothetical protein ysnA - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS C69986 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession C69986 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-198 ##label KUN !'##cross-references GB:Z99118; GB:AL009126; NID:g2635200; !1PIDN:CAB14796.1; PID:g2635301 !'##experimental_source strain 168 GENETICS !$#gene ysnA CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0226 SUMMARY #length 198 #molecular-weight 21933 #checksum 8174 SEQUENCE /// ENTRY D64146 #type complete TITLE hypothetical protein HI0260 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 29-Sep-1999 ACCESSIONS D64146 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession D64146 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-195 ##label TIGR !'##cross-references GB:U32712; GB:L42023; NID:g1573225; !1PIDN:AAC21925.1; PID:g1573226; TIGR:HI0260 !'##note best homolog was a hypothetical protein from Mycobacterium !1leprae CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0226 SUMMARY #length 195 #molecular-weight 20972 #checksum 884 SEQUENCE /// ENTRY A65081 #type complete TITLE hypothetical protein b2954 - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS A65081 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65081 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-197 ##label BLAT !'##cross-references GB:AE000378; GB:U00096; NID:g1789319; !1PIDN:AAC75991.1; PID:g1789324; UWGP:b2954 !'##experimental_source strain K-12, substrain MG1655 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0226 SUMMARY #length 197 #molecular-weight 21039 #checksum 8031 SEQUENCE /// ENTRY H70318 #type complete TITLE conserved hypothetical protein aq_202 - Aquifex aeolicus ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 29-Sep-1999 ACCESSIONS H70318 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession H70318 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-202 ##label AQF !'##cross-references GB:AE000678; NID:g2982921; PIDN:AAC06551.1; !1PID:g2982934; GB:AE000657 !'##experimental_source strain VF5 GENETICS !$#gene aq_202 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0226 SUMMARY #length 202 #molecular-weight 23115 #checksum 3304 SEQUENCE /// ENTRY G70130 #type complete TITLE conserved hypothetical protein BB0247 - Lyme disease spirochete ORGANISM #formal_name Borrelia burgdorferi #common_name Lyme disease spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 29-Sep-1999 ACCESSIONS G70130 REFERENCE A70100 !$#authors Fraser, C.M.; Casjens, S.; Huang, W.M.; Sutton, G.G.; !1Clayton, R.; Lathigra, R.; White, O.; Ketchum, K.A.; Dodson, !1R.; Hickey, E.K.; Gwinn, M.; Dougherty, B.; Tomb, J.F.; !1Fleischmann, R.D.; Richardson, D.; Peterson, J.; Kerlavage, !1A.R.; Quackenbush, J.; Salzberg, S.; Hanson, M.; Vugt, R.V.; !1Palmer, N.; Adams, M.D.; Gocayne, J.; Weidman, J.; !1Utterback, T.; Watthey, L.; McDonald, L.; Artiach, P.; !1Bowman, C.; Garland, S.; Fujii, C.; Cotton, M.D.; Horst, K.; !1Roberts, K.; Hatch, B.; Smith, H.O.; Venter, J.C. !$#journal Nature (1997) 390:580-586 !$#title Genomic sequence of a Lyme disease spirochaete, Borrelia !1burgdorferi. !$#cross-references MUID:98065943; PMID:9403685 !$#accession G70130 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-201 ##label KLE !'##cross-references GB:AE001135; GB:AE000783; NID:g2688144; !1PIDN:AAB91499.1; PID:g2688151; TIGR:BB0247 !'##experimental_source strain B31 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0226 SUMMARY #length 201 #molecular-weight 23138 #checksum 9372 SEQUENCE /// ENTRY S28549 #type complete TITLE acetyl-CoA hydrolase (EC 3.1.2.1) [validated] - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES acetyl-CoA deacylase; acetyl-CoA thiolesterase; protein YBL015w; protein YBL0304 ORGANISM #formal_name Saccharomyces cerevisiae DATE 02-Feb-2001 #sequence_revision 02-Feb-2001 #text_change 02-Feb-2001 ACCESSIONS S28549; S45749; A35195; B35195 REFERENCE S25329 !$#authors van Dyck, L.; Purnelle, B.; Skala, J.; Goffeau, A. !$#journal Yeast (1992) 8:769-776 !$#title An 11.4 kb DNA segment on the left arm of yeast chromosome !1II carries the carboxypeptidase Y sorting gene PEP1, as well !1as ACH1, FUS3 and a putative ARS. !$#cross-references MUID:93070614; PMID:1441754 !$#accession S28549 !'##status translation not shown !'##molecule_type DNA !'##residues 1-526 ##label DYC !'##cross-references EMBL:X68577; NID:g3302; PIDN:CAA48570.1; PID:g3305 REFERENCE S45745 !$#authors Goffeau, A.; Jonniaux, J.L.; Purnelle, B.; Skala, J.; de !1Wergifosse, P.; van Dyck, L. !$#submission submitted to the Protein Sequence Database, August 1994 !$#accession S45749 !'##molecule_type DNA !'##residues 1-526 ##label GOF !'##cross-references EMBL:Z35776; NID:g536004; PIDN:CAA84834.1; !1PID:g536005; MIPS:YBL015w REFERENCE A35195 !$#authors Lee, F.J.S.; Lin, L.W.; Smith, J.A. !$#journal J. Biol. Chem. (1990) 265:7413-7418 !$#title A glucose-repressible gene encodes acetyl-CoA hydrolase from !1Saccharomyces cerevisiae. !$#cross-references MUID:90237039; PMID:1970569 !$#accession A35195 !'##molecule_type mRNA !'##residues 1-307,'L',309-319,'S',321-362,'FP',365-526 ##label LEE !'##cross-references EMBL:M31036; NID:g170979; PIDN:AAA34388.1; !1PID:g170980 !$#accession B35195 !'##molecule_type protein !'##residues !169-83;93-99;111-132;139-159;175-189;202-221;225-259;264-279; !1296-307;350-361;406-437;469-478 ##label LE2 !'##note blocked amino end; monomeric; mannose-binding GENETICS !$#gene SGD:ACH1 !'##cross-references SGD:S0000111; MIPS:YBL015w !$#map_position 2L COMPLEX monomer FUNCTION !$#description EC 3.1.2.1 [validated, MUID:90237039]; acetyl-CoA hydrolase; !1catalyzes the hydrolysis of acetyl-CoA (or longer chain !1derivate) to coenzyme A and acetate (or longer chain !1derivate) !$#pathway acetate metabolism; acetyl-CoA metabolism CLASSIFICATION #superfamily acetyl-CoA hydrolase KEYWORDS blocked amino end; coenzyme A; glycoprotein; thiolester !1hydrolase FEATURE !$2 #modified_site blocked amino end (Thr) (in mature !8form) (probably acetylated) #status experimental SUMMARY #length 526 #molecular-weight 58711 #checksum 608 SEQUENCE /// ENTRY C64736 #type complete TITLE aspartate 1-decarboxylase (EC 4.1.1.11) [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES panD protein ORGANISM #formal_name Escherichia coli DATE 13-Aug-1999 #sequence_revision 13-Aug-1999 #text_change 01-Mar-2002 ACCESSIONS C64736 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64736 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-126 ##label BLAT !'##cross-references GB:AE000122; GB:U00096; NID:g1786315; !1PIDN:AAC73242.1; PID:g1786323; UWGP:b0131 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A73091 !$#authors Albert, A.; Dhanaraj, V.; Genschel, U.; Khan, G.; Ramjee, !1M.K.; Pulido, R.; Sybanda, B.L.; Vondelf, F.; Witty, M.; !1Blundell, T.L.; Smith, A.G.; Abell, C. !$#submission submitted to the Brookhaven Protein Data Bank, October 1997 !$#cross-references PDB:1AW8 !$#contents annotation; X-ray crystallography, 2.2 angstroms, residues !11-24;25-105 REFERENCE A59049 !$#authors Albert, A.; Dhanaraj, V.; Genschel, U.; Khan, G.; Ramjee, !1M.K.; Pulido, R.; Sibanda, B.L.; von Delft, F.; Witty, M.; !1Blundell, T.L.; Smith, A.G.; Abell, C. !$#journal Nat. Struct. Biol. (1998) 5:289-293 !$#title Crystal structure of aspartate decarboxylase at 2.2 !1angstroms resolution provides evidence for an ester in !1protein self-processing. !$#cross-references MUID:98206295; PMID:9546220 !$#contents annotation; X-ray crystallography, 2.2 angstroms !$#note in this preparation 1 of 4 subunits remained an intermediate !1ester; Met-1 was modeled GENETICS !$#gene panD COMPLEX homotetramer FUNCTION !$#description catalyzes the decarboxylation of aspartic acid to !1beta-alanine !$#pathway coenzyme A biosynthesis CLASSIFICATION #superfamily aspartate 1-decarboxylase KEYWORDS blocked amino end; carbon-carbon lyase; carboxy-lyase; !1coenzyme A biosynthesis; homotetramer FEATURE !$1-24,25-126 #product aspartate 1-decarboxylase #status !8experimental #label MAT\ !$1-24 #domain aspartate 1-decarboxylase beta chain #status !8experimental #label BET\ !$25-126 #domain aspartate 1-decarboxylase alpha chain #status !8experimental #label ALP\ !$9,11,58 #active_site Lys, His, Tyr #status predicted\ !$24-25 #cleavage_site Gly-Ser (autolytic) #status !8experimental\ !$25 #modified_site pyruvic acid (Ser) (in mature form) !8#status experimental\ !$54 #binding_site substrate (Arg) #status predicted SUMMARY #length 126 #molecular-weight 13834 #checksum 4290 SEQUENCE /// ENTRY A69672 #type complete TITLE aspartate 1-decarboxylase (EC 4.1.1.11) - Bacillus subtilis ALTERNATE_NAMES panD protein ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS A69672 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession A69672 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-127 ##label KUN !'##cross-references GB:Z99115; GB:AL009126; NID:g2634478; !1PIDN:CAB14157.1; PID:g2634659 !'##experimental_source strain 168 GENETICS !$#gene panD CLASSIFICATION #superfamily aspartate 1-decarboxylase KEYWORDS blocked amino end; carbon-carbon lyase; carboxy-lyase; !1coenzyme A biosynthesis FEATURE !$9,11,58 #active_site Lys, His, Tyr #status predicted\ !$24-25 #cleavage_site Gly-Ser (autolytic) #status predicted\ !$25 #modified_site pyruvic acid (Ser) (in mature form) !8#status predicted\ !$54 #binding_site substrate (Arg) #status predicted SUMMARY #length 127 #molecular-weight 13900 #checksum 7638 SEQUENCE /// ENTRY B70955 #type complete TITLE aspartate 1-decarboxylase (EC 4.1.1.11) - Mycobacterium tuberculosis (strain H37RV) ALTERNATE_NAMES panD protein ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS B70955 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession B70955 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-139 ##label COL !'##cross-references GB:Z95557; GB:AL123456; NID:g3242276; !1PIDN:CAB08943.1; PID:g2113975 !'##experimental_source strain H37Rv GENETICS !$#gene panD CLASSIFICATION #superfamily aspartate 1-decarboxylase KEYWORDS blocked amino end; carbon-carbon lyase; carboxy-lyase; !1coenzyme A biosynthesis FEATURE !$9,11,58 #active_site Lys, His, Tyr #status predicted\ !$24-25 #cleavage_site Gly-Ser (autolytic) #status predicted\ !$25 #modified_site pyruvic acid (Ser) (in mature form) !8#status predicted\ !$54 #binding_site substrate (Arg) #status predicted SUMMARY #length 139 #molecular-weight 14885 #checksum 4739 SEQUENCE /// ENTRY A70343 #type complete TITLE aspartate 1-decarboxylase (EC 4.1.1.11) - Aquifex aeolicus ALTERNATE_NAMES panD protein ORGANISM #formal_name Aquifex aeolicus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 29-Sep-1999 ACCESSIONS A70343 REFERENCE A70300 !$#authors Deckert, G.; Warren, P.V.; Gaasterland, T.; Young, W.G.; !1Lenox, A.L.; Graham, D.E.; Overbeek, R.; Snead, M.A.; !1Keller, M.; Aujay, M.; Huber, R.; Feldman, R.A.; Short, !1J.M.; Olson, G.J.; Swanson, R.V. !$#journal Nature (1998) 392:353-358 !$#title The complete genome of the hyperthermophilic bacterium !1Aquifex aeolicus. !$#cross-references MUID:98196666; PMID:9537320 !$#accession A70343 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-124 ##label AQF !'##cross-references GB:AE000692; NID:g2983130; PIDN:AAC06737.1; !1PID:g2983134; GB:AE000657 !'##experimental_source strain VF5 GENETICS !$#gene panD CLASSIFICATION #superfamily aspartate 1-decarboxylase KEYWORDS blocked amino end; carbon-carbon lyase; carboxy-lyase; !1coenzyme A biosynthesis FEATURE !$9,11,58 #active_site Lys, His, Tyr #status predicted\ !$24-25 #cleavage_site Gly-Ser (autolytic) #status predicted\ !$25 #modified_site pyruvic acid (Ser) (in mature form) !8#status predicted\ !$54 #binding_site substrate (Arg) #status predicted SUMMARY #length 124 #molecular-weight 14163 #checksum 4265 SEQUENCE /// ENTRY C72316 #type complete TITLE aspartate 1-decarboxylase (EC 4.1.1.11) - Thermotoga maritima (strain MSB8) ALTERNATE_NAMES panD protein ORGANISM #formal_name Thermotoga maritima DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C72316 REFERENCE A72200 !$#authors Nelson, K.E.; Clayton, R.A.; Gill, S.R.; Gwinn, M.L.; !1Dodson, R.J.; Haft, D.H.; Hickey, E.K.; Peterson, J.D.; !1Nelson, W.C.; Ketchum, K.A.; McDonald, L.; Utterback, T.R.; !1Malek, J.A.; Linher, K.D.; Garrett, M.M.; Stewart, A.M.; !1Cotton, M.D.; Pratt, M.S.; Phillips, C.A.; Richardson, D.; !1Heidelberg, J.; Sutton, G.G.; Fleischmann, R.D.; White, O.; !1Salzberg, S.L.; Smith, H.O.; Venter, J.C.; Fraser, C.M. !$#journal Nature (1999) 399:323-329 !$#title Evidence for lateral gene transfer between Archaea and !1Bacteria from genome sequence of Thermotoga maritima. !$#cross-references MUID:99287316; PMID:10360571 !$#accession C72316 !'##status preliminary !'##molecule_type DNA !'##residues 1-114 ##label ARN !'##cross-references GB:AE001757; GB:AE000512; NID:g4981464; !1PIDN:AAD36020.1; PID:g4981477; TIGR:TM0939 !'##experimental_source strain MSB8 GENETICS !$#gene TM0939 CLASSIFICATION #superfamily aspartate 1-decarboxylase KEYWORDS blocked amino end; carbon-carbon lyase; carboxy-lyase; !1coenzyme A biosynthesis FEATURE !$9,11,58 #active_site Lys, His, Tyr #status predicted\ !$24-25 #cleavage_site Gly-Ser (autolytic) #status predicted\ !$25 #modified_site pyruvic acid (Ser) (in mature form) !8#status predicted\ !$54 #binding_site substrate (Arg) #status predicted SUMMARY #length 114 #molecular-weight 12838 #checksum 749 SEQUENCE /// ENTRY S75734 #type complete TITLE aspartate 1-decarboxylase (EC 4.1.1.11) - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES panD protein; protein sll0892 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S75734 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75734 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-145 ##label KAN !'##cross-references EMBL:D64003; GB:AB001339; NID:g1001200; !1PIDN:BAA10469.1; PID:g1001229 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene panD CLASSIFICATION #superfamily aspartate 1-decarboxylase KEYWORDS blocked amino end; carbon-carbon lyase; carboxy-lyase; !1coenzyme A biosynthesis FEATURE !$10,12,59 #active_site Lys, His, Tyr #status predicted\ !$25-26 #cleavage_site Gly-Ser (autolytic) #status predicted\ !$26 #modified_site pyruvic acid (Ser) (in mature form) !8#status predicted\ !$55 #binding_site substrate (Arg) #status predicted SUMMARY #length 145 #molecular-weight 16129 #checksum 8940 SEQUENCE /// ENTRY B64569 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) HP0394 - Helicobacter pylori (strain 26695) ORGANISM #formal_name Helicobacter pylori DATE 09-Aug-1997 #sequence_revision 09-Aug-1997 #text_change 24-Aug-2001 ACCESSIONS B64569 REFERENCE A64520 !$#authors Tomb, J.F.; White, O.; Kerlavage, A.R.; Clayton, R.A.; !1Sutton, G.G.; Fleischmann, R.D.; Ketchum, K.A.; Klenk, H.P.; !1Gill, S.; Dougherty, B.A.; Nelson, K.; Quackenbush, J.; !1Zhou, L.; Kirkness, E.F.; Peterson, S.; Loftus, B.; !1Richardson, D.; Dodson, R.; Khalak, H.G.; Glodek, A.; !1McKenney, K.; Fitzegerald, L.M.; Lee, N.; Adams, M.D.; !1Hickey, E.K.; Berg, D.E.; Gocayne, J.D.; Utterback, T.R.; !1Peterson, J.D.; Kelley, J.M.; Cotton, M.D.; Weidman, J.M.; !1Fujii, C.; Bowman, C.; Watthey, L.; Wallin, E.; Hayes, W.S.; !1Borodovsky, M.; Karpk, P.D.; Smith, H.O.; Fraser, C.M.; !1Venter, J.C. !$#journal Nature (1997) 388:539-547 !$#title The complete genome sequence of the gastric pathogen !1Helicobacter pylori. !$#cross-references MUID:97394467; PMID:9252185 !$#accession B64569 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-252 ##label TOM !'##cross-references GB:AE000555; GB:AE000511; NID:g2313485; !1PIDN:AAD07466.1; PID:g2313502; TIGR:HP0394 COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene HP0394 CLASSIFICATION #superfamily Helicobacter pylori probable phosphoesterase !1HP0394; phosphoesterase core homology KEYWORDS hydrolase FEATURE !$10-85 #domain phosphoesterase core homology #label PEC SUMMARY #length 252 #molecular-weight 29506 #checksum 1075 SEQUENCE /// ENTRY F71864 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) jhp0987 - Helicobacter pylori (strain J99) ORGANISM #formal_name Helicobacter pylori #variety strain J99 DATE 12-Feb-1999 #sequence_revision 12-Feb-1999 #text_change 24-Aug-2001 ACCESSIONS F71864 REFERENCE A71800 !$#authors Alm, R.A.; Ling, L.S.L.; Moir, D.T.; King, B.L.; Brown, !1E.D.; Doig, P.C.; Smith, D.R.; Noonan, B.; Guild, B.C.; !1deJonge, B.L.; Carmel, G.; Tummino, P.J.; Caruso, A.; !1Uria-Nickelsen, M.; Mills, D.M.; Ives, C.; Gibson, R.; !1Merberg, D.; Mills, S.D.; Jiang, Q.; Taylor, D.E.; Vovis, !1G.F.; Trust, T.J. !$#journal Nature (1999) 397:176-180 !$#title Genomic sequence comparison of two unrelated isolates of the !1human gastric pathogen Helicobacter pylori. !$#cross-references MUID:99120557; PMID:9923682 !$#accession F71864 !'##molecule_type DNA !'##residues 1-252 ##label ARN !'##cross-references GB:AE001527; GB:AE001439; NID:g4155558; !1PIDN:AAD06566.1; PID:g4155572 !'##experimental_source strain J99 COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene jhp0987 CLASSIFICATION #superfamily Helicobacter pylori probable phosphoesterase !1HP0394; phosphoesterase core homology KEYWORDS hydrolase FEATURE !$10-85 #domain phosphoesterase core homology #label PEC SUMMARY #length 252 #molecular-weight 29565 #checksum 1082 SEQUENCE /// ENTRY G83242 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) PA3219 [similarity] - Pseudomonas aeruginosa (strain PAO1) ORGANISM #formal_name Pseudomonas aeruginosa DATE 03-Aug-2001 #sequence_revision 03-Aug-2001 #text_change 24-Aug-2001 ACCESSIONS G83242 REFERENCE A82950 !$#authors Stover, C.K.; Pham, X.Q.; Erwin, A.L.; Mizoguchi, S.D.; !1Warrener, P.; Hickey, M.J.; Brinkman, F.S.L.; Hufnagle, !1W.O.; Kowalik, D.J.; Lagrou, M.; Garber, R.L.; Goltry, L.; !1Tolentino, E.; Westbrook-Wadman, S.; Yuan, Y.; Brody, L.L.; !1Coulter, S.N.; Folger, K.R.; Kas, A.; Larbig, K.; Lim, R.M.; !1Smith, K.A.; Spencer, D.H.; Wong, G.K.S.; Wu, Z.; Paulsen, !1I.T.; Reizer, J.; Saier, M.H.; Hancock, R.E.W.; Lory, S.; !1Olson, M.V. !$#journal Nature (2000) 406:959-964 !$#title Complete genome sequence of Pseudomonas aeruginosa PA01, an !1opportunistic pathogen. !$#cross-references MUID:20437337; PMID:10984043 !$#accession G83242 !'##molecule_type DNA !'##residues 1-270 ##label STO !'##cross-references GB:AE004745; GB:AE004091; NID:g9949336; !1PIDN:AAG06607.1; GSPDB:GN00131; PASP:PA3219 !'##experimental_source strain PAO1 COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene PA3219 CLASSIFICATION #superfamily Helicobacter pylori probable phosphoesterase !1HP0394; phosphoesterase core homology KEYWORDS hydrolase FEATURE !$16-94 #domain phosphoesterase core homology #label PEC SUMMARY #length 270 #molecular-weight 31292 #checksum 9947 SEQUENCE /// ENTRY F87663 #type complete TITLE probable phosphoesterase (EC3.1.-.-) CC3344 [similarity] - Caulobacter crescentus ORGANISM #formal_name Caulobacter crescentus DATE 03-Aug-2001 #sequence_revision 03-Aug-2001 #text_change 24-Aug-2001 ACCESSIONS F87663 REFERENCE A87249 !$#authors Nierman, W.C.; Feldblyum, T.V.; Paulsen, I.T.; Nelson, K.E.; !1Eisen, J.; Heidelberg, J.F.; Alley, M.; Ohta, N.; Maddock, !1J.R.; Potocka, I.; Nelson, W.C.; Newton, A.; Stephens, C.; !1Phadke, N.D.; Ely, B.; Laub, M.T.; DeBoy, R.T.; Dodson, !1R.J.; Durkin, A.S.; Gwinn, M.L.; Haft, D.H.; Kolonay, J.F.; !1Smit, J.; Craven, M.; Khouri, H.; Shetty, J.; Berry, K.; !1Utterback, T.; Tran, K.; Wolf, A.; Vamathevan, J.; !1Ermolaeva, M.; White, O.; Salzberg, S.L.; Shapiro, L.; !1Venter, J.C.; Fraser, C.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (2001) 98:4136-4141 !$#title Complete Genome Sequence of Caulobacter crescentus. !$#cross-references MUID:21173698; PMID:11259647 !$#accession F87663 !'##molecule_type DNA !'##residues 1-281 ##label STO !'##cross-references GB:AE005673; NID:g13425046; PIDN:AAK25306.1; !1GSPDB:GN00148 COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene CC3344 CLASSIFICATION #superfamily Helicobacter pylori probable phosphoesterase !1HP0394; phosphoesterase core homology KEYWORDS hydrolase FEATURE !$11-89 #domain phosphoesterase core homology #label PEC SUMMARY #length 281 #molecular-weight 31723 #checksum 6242 SEQUENCE /// ENTRY C64989 #type complete TITLE cytochrome-c biosynthesis heme-carrier protein ccmE - Escherichia coli (strain K-12) ALTERNATE_NAMES cytochrome c-type biogenesis protein ccmE ORGANISM #formal_name Escherichia coli DATE 24-Sep-1999 #sequence_revision 24-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS C64989; A58862 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession C64989 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-159 ##label BLAT !'##cross-references GB:AE000309; GB:U00096; NID:g1788520; !1PIDN:AAC75257.1; PID:g1788525; UWGP:b2197 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A58862 !$#authors Schulz, H.; Hennecke, H.; Thoeny-Meyer, L. !$#journal Science (1998) 281:1197-1200 !$#title Prototype of a heme chaperone essential for cytochrome c !1maturation. !$#cross-references MUID:98378584; PMID:9712585 !$#accession A58862 !'##molecule_type protein !'##residues 'X',131-140,'X' ##label SCH !'##note mass spectrographic identification of heme attached to 130-His GENETICS !$#gene ccmE CLASSIFICATION #superfamily Escherichia coli cytochrome-c biosynthesis !1heme-carrier protein ccmE KEYWORDS carrier protein; chromoprotein; heme; iron; metalloprotein FEATURE !$9-30 #domain transmembrane #status predicted #label TRM\ !$130 #binding_site heme (His) (covalent) #status !8experimental SUMMARY #length 159 #molecular-weight 17698 #checksum 2789 SEQUENCE /// ENTRY S23064 #type complete TITLE mcpA protein - Caulobacter crescentus ORGANISM #formal_name Caulobacter crescentus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 18-Jul-2001 ACCESSIONS S23064; E87302 REFERENCE S23064 !$#authors Alley, M.R.K.; Maddock, J.R.; Shapiro, L. !$#journal Genes Dev. (1992) 6:825-836 !$#title Polar localization of a bacterial chemoreceptor. !$#cross-references MUID:92249774; PMID:1577276 !$#accession S23064 !'##status preliminary !'##molecule_type DNA !'##residues 1-657 ##label ALL !'##cross-references EMBL:X66502; NID:g40423; PIDN:CAA47122.1; !1PID:g40424 REFERENCE A87249 !$#authors Nierman, W.C.; Feldblyum, T.V.; Paulsen, I.T.; Nelson, K.E.; !1Eisen, J.; Heidelberg, J.F.; Alley, M.; Ohta, N.; Maddock, !1J.R.; Potocka, I.; Nelson, W.C.; Newton, A.; Stephens, C.; !1Phadke, N.D.; Ely, B.; Laub, M.T.; DeBoy, R.T.; Dodson, !1R.J.; Durkin, A.S.; Gwinn, M.L.; Haft, D.H.; Kolonay, J.F.; !1Smit, J.; Craven, M.; Khouri, H.; Shetty, J.; Berry, K.; !1Utterback, T.; Tran, K.; Wolf, A.; Vamathevan, J.; !1Ermolaeva, M.; White, O.; Salzberg, S.L.; Shapiro, L.; !1Venter, J.C.; Fraser, C.M. !$#journal Proc. Natl. Acad. Sci. U.S.A. (2001) 98:4136-4141 !$#title Complete Genome Sequence of Caulobacter crescentus. !$#cross-references MUID:21173698; PMID:11259647 !$#accession E87302 !'##status preliminary !'##molecule_type DNA !'##residues 1-657 ##label STO !'##cross-references GB:AE005673; NID:g13421597; PIDN:AAK22417.1; !1GSPDB:GN00148 GENETICS !$#gene CC0430 CLASSIFICATION #superfamily methyl-accepting chemotaxis protein mcpA KEYWORDS methylated amino acid; transmembrane protein FEATURE !$378,574 #modified_site glutamate methyl ester (Gln) (by !8cheB-dependent deamidation and methylation) #status !8predicted\ !$385 #modified_site glutamate methyl ester (Glu) #status !8predicted SUMMARY #length 657 #molecular-weight 69345 #checksum 3137 SEQUENCE /// ENTRY JC4735 #type complete TITLE methyl-accepting chemotaxis protein A - Rhodobacter capsulatus ORGANISM #formal_name Rhodobacter capsulatus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 29-Sep-1999 ACCESSIONS JC4735 REFERENCE JC4735 !$#authors Michotey, V.; Toussaint, B.; Richaud, P.; Vignais, P.M. !$#journal Gene (1996) 170:73-76 !$#title Characterisation of the mcpA and mcpB genes capable of !1encoding methyl-accepting type chemoreceptors in Rhodobacter !1capsulatus. !$#cross-references MUID:96200858; PMID:8621092 !$#accession JC4735 !'##molecule_type DNA !'##residues 1-645 ##label MIC !'##cross-references GB:L48927; NID:g1066849; PIDN:AAB05214.1; !1PID:g1066850 GENETICS !$#gene mcpA CLASSIFICATION #superfamily methyl-accepting chemotaxis protein mcpA KEYWORDS membrane protein FEATURE !$6-35 #domain hydrophobic #status predicted #label HYD1\ !$183-212 #domain hydrophobic #status predicted #label HYD2 SUMMARY #length 645 #molecular-weight 69164 #checksum 8189 SEQUENCE /// ENTRY B70978 #type complete TITLE probable wbbL protein - Mycobacterium tuberculosis (strain H37RV) ORGANISM #formal_name Mycobacterium tuberculosis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS B70978 REFERENCE A70500 !$#authors Cole, S.T.; Brosch, R.; Parkhill, J.; Garnier, T.; Churcher, !1C.; Harris, D.; Gordon, S.V.; Eiglmeier, K.; Gas, S.; Barry !1III, C.E.; Tekaia, F.; Badcock, K.; Basham, D.; Brown, D.; !1Chillingworth, T.; Connor, R.; Davies, R.; Devlin, K.; !1Feltwell, T.; Gentles, S.; Hamlin, N.; Holroyd, S.; Hornsby, !1T.; Jagels, K.; Krogh, A.; McLean, J.; Moule, S.; Murphy, !1L.; Oliver, S.; Osborne, J.; Quail, M.A.; Rajandream, M.A.; !1Rogers, J.; Rutter, S.; Seeger, K.; Skelton, S.; Squares, !1S.; Sqares, R.; Sulston, J.E.; Taylor, K.; Whitehead, S.; !1Barrell, B.G. !$#journal Nature (1998) 393:537-544 !$#title Deciphering the biology of Mycobacterium tuberculosis from !1the complete genome sequence. !$#cross-references MUID:98295987; PMID:9634230 !$#accession B70978 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-301 ##label COL !'##cross-references GB:Z92771; GB:AL123456; NID:g3242259; !1PIDN:CAB07092.1; PID:g1877320 !'##experimental_source strain H37Rv GENETICS !$#gene wbbL CLASSIFICATION #superfamily probable glycosyl transferase MTH172 SUMMARY #length 301 #molecular-weight 33295 #checksum 8678 SEQUENCE /// ENTRY H69880 #type complete TITLE flhB-related protein ylqH - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS H69880 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession H69880 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-93 ##label KUN !'##cross-references GB:Z99112; GB:AL009126; NID:g2633902; !1PIDN:CAB13481.1; PID:g2633980 !'##experimental_source strain 168 GENETICS !$#gene ylqH CLASSIFICATION #superfamily flhB-related protein ylqH; flhB !1carboxyl-terminal homology FEATURE !$10-82 #domain flhB carboxyl-terminal homology #label FCT SUMMARY #length 93 #molecular-weight 10603 #checksum 4433 SEQUENCE /// ENTRY F72225 #type complete TITLE flhB-related protein TM1672 - Thermotoga maritima (strain MSB8) ORGANISM #formal_name Thermotoga maritima DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS F72225 REFERENCE A72200 !$#authors Nelson, K.E.; Clayton, R.A.; Gill, S.R.; Gwinn, M.L.; !1Dodson, R.J.; Haft, D.H.; Hickey, E.K.; Peterson, J.D.; !1Nelson, W.C.; Ketchum, K.A.; McDonald, L.; Utterback, T.R.; !1Malek, J.A.; Linher, K.D.; Garrett, M.M.; Stewart, A.M.; !1Cotton, M.D.; Pratt, M.S.; Phillips, C.A.; Richardson, D.; !1Heidelberg, J.; Sutton, G.G.; Fleischmann, R.D.; White, O.; !1Salzberg, S.L.; Smith, H.O.; Venter, J.C.; Fraser, C.M. !$#journal Nature (1999) 399:323-329 !$#title Evidence for lateral gene transfer between Archaea and !1Bacteria from genome sequence of Thermotoga maritima. !$#cross-references MUID:99287316; PMID:10360571 !$#accession F72225 !'##molecule_type DNA !'##residues 1-86 ##label ARN !'##cross-references GB:AE001808; GB:AE000512; NID:g4982233; !1PIDN:AAD36739.1; PID:g4982247; TIGR:TM1672 !'##experimental_source strain MSB8 GENETICS !$#gene TM1672 CLASSIFICATION #superfamily flhB-related protein ylqH; flhB !1carboxyl-terminal homology FEATURE !$9-81 #domain flhB carboxyl-terminal homology #label FCT SUMMARY #length 86 #molecular-weight 9961 #checksum 5891 SEQUENCE /// ENTRY D71268 #type complete TITLE flhB-related protein TP0911 - syphilis spirochete ORGANISM #formal_name Treponema pallidum subsp. pallidum #common_name syphilis spirochete DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 28-Jul-2000 ACCESSIONS D71268 REFERENCE A71250 !$#authors Fraser, C.M.; Norris, S.J.; Weinstock, G.M.; White, O.; !1Sutton, G.G.; Dodson, R.; Gwinn, M.; Hickey, E.K.; Clayton, !1R.; Ketchum, K.A.; Sodergren, E.; Hardham, J.M.; McLeod, !1M.P.; Salzberg, S.; Peterson, J.; Khalak, H.; Richardson, !1D.; Howell, J.K.; Chidambaram, M.; Utterback, T.; McDonald, !1L.; Artiach, P.; Bowman, C.; Cotton, M.D.; Fujii, C.; !1Garland, S.; Hatch, B.; Horst, K.; Roberts, K.; Watthey, L.; !1Weidman, J.; Smith, H.O.; Venter, J.C. !$#journal Science (1998) 281:375-388 !$#title Complete genome sequence of Treponema pallidum, the syphilis !1spirochete. !$#cross-references MUID:98332770; PMID:9665876 !$#accession D71268 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-83 ##label COL !'##cross-references GB:AE001259; GB:AE000520; NID:g3323209; !1PIDN:AAC65862.1; PID:g3323223 !'##experimental_source strain Nichols GENETICS !$#gene TP0911 CLASSIFICATION #superfamily flhB-related protein ylqH; flhB !1carboxyl-terminal homology FEATURE !$8-79 #domain flhB carboxyl-terminal homology #label FCT SUMMARY #length 83 #molecular-weight 8995 #checksum 104 SEQUENCE /// ENTRY S77273 #type complete TITLE penicillin-binding protein 5 regulation protein - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S77273 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S77273 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-481 ##label KAN !'##cross-references EMBL:D90907; GB:AB001339; NID:g1652618; !1PIDN:BAA17607.1; PID:g1652687 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily Synechocystis penicillin-binding protein 5 !1regulation protein SUMMARY #length 481 #molecular-weight 53110 #checksum 1174 SEQUENCE /// ENTRY S75661 #type complete TITLE membrane-bound protein lytR - Synechocystis sp. (strain PCC 6803) ALTERNATE_NAMES protein sll1872 ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS S75661 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S75661 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-463 ##label KAN !'##cross-references EMBL:D90912; GB:AB001339; NID:g1653228; !1PIDN:BAA18222.1; PID:g1653307 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 GENETICS !$#gene lytR !$#start_codon GTG CLASSIFICATION #superfamily Synechocystis penicillin-binding protein 5 !1regulation protein KEYWORDS membrane bound SUMMARY #length 463 #molecular-weight 50774 #checksum 7070 SEQUENCE /// ENTRY G71029 #type complete TITLE probable phosphate cyclase - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G71029 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession G71029 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-369 ##label KAW !'##cross-references GB:AP000006; NID:g3236133; PIDN:BAA30639.1; !1PID:g3257956 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1529 CLASSIFICATION #superfamily Methanococcus jannaschii conserved hypothetical !1protein MJ0025 SUMMARY #length 369 #molecular-weight 40501 #checksum 3044 SEQUENCE /// ENTRY C71071 #type complete TITLE hypothetical protein PH1263 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C71071 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession C71071 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-320 ##label KAW !'##cross-references GB:AP000005; NID:g3236132; PIDN:BAA30365.1; !1PID:g3257682 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1263 CLASSIFICATION #superfamily Methanobacterium thermoautotrophicum conserved !1hypothetical protein MTH196 SUMMARY #length 320 #molecular-weight 38430 #checksum 8816 SEQUENCE /// ENTRY D65252 #type complete TITLE ribosomal-protein-alanine N-acetyltransferase (EC 2.3.1.128) rimI - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 24-Sep-1999 #sequence_revision 24-Sep-1999 #text_change 01-Mar-2002 ACCESSIONS D65252; S56597; B48647; S01083 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession D65252 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-148 ##label BLAT !'##cross-references GB:AE000507; GB:U00096; NID:g2367380; !1PIDN:AAC77326.1; PID:g2367381; UWGP:b4373 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S56314 !$#authors Burland, V.; Plunkett III, G.; Sofia, H.J.; Daniels, D.L.; !1Blattner, F.R. !$#journal Nucleic Acids Res. (1995) 23:2105-2119 !$#title Analysis of the Escherichia coli genome VI: DNA sequence of !1the region from 92.8 through 100 minutes. !$#cross-references MUID:95334362; PMID:7610040 !$#accession S56597 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-142,'RCQSVCNTRWNNEVGLDFL' ##label BUR !'##cross-references EMBL:U14003; NID:g1263172; PIDN:AAA97269.1; !1PID:g537213 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1August 1994 REFERENCE A48647 !$#authors Carter, J.R.; Franden, M.A.; Aebersold, R.; McHenry, C.S. !$#journal J. Bacteriol. (1993) 175:5604-5610 !$#title Identification, isolation, and overexpression of the gene !1encoding the psi subunit of DNA polymerase III holoenzyme. !$#cross-references MUID:93374856; PMID:8366044 !$#accession B48647 !'##status translation not shown; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-30 ##label CAR !'##cross-references GB:L05387; NID:g146389; PIDN:AAA03077.1; !1PID:g409555 !'##experimental_source strain MAF102 REFERENCE S01083 !$#authors Yoshikawa, A.; Isono, S.; Sheback, A.; Isono, K. !$#journal Mol. Gen. Genet. (1987) 209:481-488 !$#title Cloning and nucleotide sequencing of the genes rimI and rimJ !1which encode enzymes acetylating ribosomal proteins S18 and !1S5 of Escherichia coli K12. !$#cross-references MUID:88121676; PMID:2828880 !$#accession S01083 !'##molecule_type DNA !'##residues 1-142,'RCQSVCNTRWNNEVGLDFL' ##label YOS !'##cross-references EMBL:X06117; NID:g42741; PIDN:CAA29489.1; !1PID:g42742 COMMENT For ribosomal protein S18, see PIR:R3EC18. GENETICS !$#gene rimI !$#map_position 99.3 min FUNCTION !$#description catalyzes the acetylation by acetyl-CoA of the !1amino-terminal alanine of ribosomal protein S18 CLASSIFICATION #superfamily Escherichia coli ribosomal-protein-alanine !1N-acetyltransferase rimI KEYWORDS acetyl-CoA; acyltransferase; coenzyme A SUMMARY #length 148 #molecular-weight 16610 #checksum 2477 SEQUENCE /// ENTRY H69166 #type complete TITLE conserved hypothetical protein MTH508 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 21-Jul-2000 ACCESSIONS H69166 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession H69166 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-178 ##label MTH !'##cross-references GB:AE000834; GB:AE000666; NID:g2621574; !1PIDN:AAB85014.1; PID:g2621580 !'##experimental_source strain Delta H GENETICS !$#gene MTH508 !$#start_codon GTG CLASSIFICATION #superfamily Methanobacterium hypothetical protein MTH508 SUMMARY #length 178 #molecular-weight 19850 #checksum 9548 SEQUENCE /// ENTRY F69029 #type complete TITLE hypothetical protein MTH1218 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 21-Jul-2000 ACCESSIONS F69029 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession F69029 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-166 ##label MTH !'##cross-references GB:AE000889; GB:AE000666; NID:g2622318; !1PIDN:AAB85707.1; PID:g2622328 !'##experimental_source strain Delta H GENETICS !$#gene MTH1218 CLASSIFICATION #superfamily Methanobacterium hypothetical protein MTH508 SUMMARY #length 166 #molecular-weight 18277 #checksum 1591 SEQUENCE /// ENTRY A69167 #type complete TITLE hypothetical protein MTH509 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 29-Oct-1999 ACCESSIONS A69167 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession A69167 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-154 ##label MTH !'##cross-references GB:AE000834; GB:AE000666; NID:g2621574; !1PIDN:AAB85015.1; PID:g2621581 !'##experimental_source strain Delta H GENETICS !$#gene MTH509 CLASSIFICATION #superfamily Methanobacterium hypothetical protein MTH508 SUMMARY #length 154 #molecular-weight 17475 #checksum 9638 SEQUENCE /// ENTRY H69208 #type complete TITLE hypothetical protein MTH815 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 21-Jul-2000 ACCESSIONS H69208 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession H69208 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-99 ##label MTH !'##cross-references GB:AE000859; GB:AE000666; NID:g2621902; !1PIDN:AAB85315.1; PID:g2621906 !'##experimental_source strain Delta H GENETICS !$#gene MTH815 CLASSIFICATION #superfamily Methanobacterium hypothetical protein MTH815 SUMMARY #length 99 #molecular-weight 10943 #checksum 735 SEQUENCE /// ENTRY F69115 #type complete TITLE hypothetical protein MTH1859 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 15-Oct-1999 #sequence_revision 15-Oct-1999 #text_change 21-Jul-2000 ACCESSIONS F69115 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession F69115 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-77 ##label MTH !'##cross-references GB:AE000938; GB:AE000666; NID:g2622986; !1PIDN:AAB86325.1; PID:g2622995 !'##experimental_source strain Delta H GENETICS !$#gene MTH1859 CLASSIFICATION #superfamily Methanobacterium hypothetical protein MTH815 SUMMARY #length 77 #molecular-weight 8241 #checksum 9838 SEQUENCE /// ENTRY S76634 #type complete TITLE hypothetical protein - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 16-Jun-2000 ACCESSIONS S76634 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76634 !'##status preliminary !'##molecule_type DNA !'##residues 1-337 ##label KAN !'##cross-references EMBL:D64004; GB:AB001339; NID:g1001701; !1PID:g1001741 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily hypothetical protein 135 SUMMARY #length 337 #molecular-weight 37633 #checksum 9811 SEQUENCE /// ENTRY H64463 #type complete TITLE hypothetical protein MJ1313 - Methanococcus jannaschii ORGANISM #formal_name Methanococcus jannaschii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS H64463 REFERENCE A64300 !$#authors Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, !1R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, !1R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, !1J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, !1E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, !1J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; !1Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; !1Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; !1Hurst, M.A.; Kaine, B.P.; Borodovsky, M.; Klenk, H.P.; !1Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. !$#journal Science (1996) 273:1058-1073 !$#title Complete genome sequence of the methanogenic archaeon, !1Methanococcus jannaschii. !$#cross-references MUID:96337999; PMID:8688087 !$#accession H64463 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-403 ##label BUL !'##cross-references GB:U67571; GB:L77117; NID:g1591939; !1PIDN:AAB99320.1; PID:g1591952; TIGR:MJ1313 GENETICS !$#map_position FOR1258390-1259601 CLASSIFICATION #superfamily hypothetical protein PH0354 SUMMARY #length 403 #molecular-weight 44600 #checksum 245 SEQUENCE /// ENTRY G71142 #type complete TITLE hypothetical protein PH0354 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS G71142 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession G71142 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-388 ##label KAW !'##cross-references GB:AP000002; NID:g3236129; PIDN:BAA29428.1; !1PID:g3256745 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH0354 CLASSIFICATION #superfamily hypothetical protein PH0354 SUMMARY #length 388 #molecular-weight 42663 #checksum 4559 SEQUENCE /// ENTRY D69056 #type complete TITLE conserved hypothetical protein MTH1421 - Methanobacterium thermoautotrophicum (strain Delta H) ORGANISM #formal_name Methanobacterium thermoautotrophicum DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS D69056 REFERENCE A69000 !$#authors Smith, D.R.; Doucette-Stamm, L.A.; Deloughery, C.; Lee, H.; !1Dubois, J.; Aldredge, T.; Bashirzadeh, R.; Blakely, D.; !1Cook, R.; Gilbert, K.; Harrison, D.; Hoang, L.; Keagle, P.; !1Lumm, W.; Pothier, B.; Qiu, D.; Spadafora, R.; Vicaire, R.; !1Wang, Y.; Wierzbowski, J.; Gibson, R.; Jiwani, N.; Caruso, !1A.; Bush, D.; Safer, H.; Patwell, D.; Prabhakar, S.; !1McDougall, S.; Shimer, G.; Goyal, A.; Pietrokovski, S.; !1Church, G.M.; Daniels, C.J.; Mao, J.; Rice, P.; Noelling, !1J.; Reeve, J.N. !$#journal J. Bacteriol. (1997) 179:7135-7155 !$#title Complete genome sequence of Methanobacterium !1thermoautotrophicum Delta H: functional analysis and !1comparative genomics. !$#cross-references MUID:98037514; PMID:9371463 !$#accession D69056 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-399 ##label MTH !'##cross-references GB:AE000904; GB:AE000666; NID:g2622528; !1PIDN:AAB85898.1; PID:g2622534 !'##experimental_source strain Delta H GENETICS !$#gene MTH1421 CLASSIFICATION #superfamily hypothetical protein PH0354 SUMMARY #length 399 #molecular-weight 42592 #checksum 6909 SEQUENCE /// ENTRY E69541 #type complete TITLE conserved hypothetical protein AF2333 - Archaeoglobus fulgidus ORGANISM #formal_name Archaeoglobus fulgidus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS E69541 REFERENCE A69250 !$#authors Klenk, H.P.; Clayton, R.A.; Tomb, J.F.; White, O.; Nelson, !1K.E.; Ketchum, K.A.; Dodson, R.J.; Gwinn, M.; Hickey, E.K.; !1Peterson, J.D.; Richardson, D.L.; Kerlavage, A.R.; Graham, !1D.E.; Kyrpides, N.C.; Fleischmann, R.D.; Quackenbush, J.; !1Lee, N.H.; Sutton, G.G.; Gill, S.; Kirkness, E.F.; !1Dougherty, B.A.; McKenny, K.; Adams, M.D.; Loftus, B.; !1Peterson, S.; Reich, C.I.; McNeil, L.K.; Badger, J.H.; !1Glodek, A.; Zhou, L.; Overbeek, R.; Gocayne, J.D.; Weidman, !1J.F.; McDonald, L.; Utterback, T.; Cotton, M.D.; Spriggs, !1T.; Artiach, P.; Kaine, B.P.; Sykes, S.M.; Sadow, P.W.; !1D'Andrea, K.P.; Bowman, C.; Fujii, C.; Garland, S.A.; Mason, !1T.M.; Olsen, G.J.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; !1Venter, J.C. !$#journal Nature (1997) 390:364-370 !$#title The complete genome sequence of the hyperthermophilic, !1sulfate-reducing archaeon Archaeoglobus fulgidus. !$#cross-references MUID:98049343; PMID:9389475 !$#accession E69541 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-380 ##label KLE !'##cross-references GB:AE000943; GB:AE000782; NID:g2689266; !1PIDN:AAB88919.1; PID:g2648180; TIGR:AF2333 CLASSIFICATION #superfamily hypothetical protein PH0354 SUMMARY #length 380 #molecular-weight 42566 #checksum 3696 SEQUENCE /// ENTRY S55040 #type complete TITLE C 3.4.25.1 proteasome endopeptidase complex () beta chain C7-I - human ALTERNATE_NAMES proteasome beta-2; proteasome chain C7-I ORGANISM #formal_name Homo sapiens #common_name man DATE 02-Jun-2000 #sequence_revision 02-Jun-2000 #text_change 03-Jun-2002 ACCESSIONS S55040; PC2323; S50148 REFERENCE S50147 !$#authors Nothwang, H.G.; Tamura, T.; Tanaka, K.; Ichihara, A. !$#journal Biochim. Biophys. Acta (1994) 1219:361-368 !$#title Sequence analyses and inter-species comparisons of three !1novel human proteasomal subunits, HsN3, HsC7-I and HsC10-II, !1confine potential proteolytic active-site residues. !$#cross-references MUID:95002149; PMID:7918633 !$#accession S55040 !'##molecule_type mRNA !'##residues 1-201 ##label NOT !'##cross-references GB:D26599; NID:g565648; PIDN:BAA05646.1; !1PID:g565649 REFERENCE PC2315 !$#authors Kristensen, P.; Johnsen, A.H.; Uerkvitz, W.; Tanaka, K.; !1Hendil, K.B. !$#journal Biochem. Biophys. Res. Commun. (1994) 205:1785-1789 !$#title Human proteasome subunits from 2-dimensional gels identified !1by partial sequencing. !$#cross-references MUID:95110324; PMID:7811265 !$#accession PC2323 !'##molecule_type protein !'##residues 72-85 ##label KRI !'##experimental_source placenta COMMENT The proteasome consists of subunits of 21K-30K arranged in 4 !1stacked rings. GENETICS !$#gene GDB:PSMB2; HC7-I !'##cross-references GDB:567222 CLASSIFICATION #superfamily human multicatalytic endopeptidase complex beta !1chain C7 KEYWORDS hydrolase; proteinase SUMMARY #length 201 #molecular-weight 22836 #checksum 9277 SEQUENCE /// ENTRY S24354 #type complete TITLE p53-binding protein mdm2 - human ALTERNATE_NAMES mdm-2 oncogene; mouse double minute 2 homolog; p53-associated phosphoprotein CONTAINS p53-binding protein mdm2, splice form A ORGANISM #formal_name Homo sapiens #common_name man DATE 17-Mar-2000 #sequence_revision 17-Mar-2000 #text_change 17-Mar-2000 ACCESSIONS S24354; S57338; G02026 REFERENCE S24354 !$#authors Oliner, J.D.; Kinzler, K.W.; Meltzer, P.S.; George, D.L.; !1Vogelstein, B. !$#journal Nature (1992) 358:80-83 !$#title Amplification of a gene encoding a p53-associated protein in !1human sarcomas. !$#cross-references MUID:92310576; PMID:1614537 !$#accession S24354 !'##molecule_type mRNA !'##residues 1-491 ##label OLI !'##cross-references EMBL:Z12020; NID:g35211; PIDN:CAA78055.1; !1PID:g35212 REFERENCE S57338 !$#authors Zauberman, A.; Flusberg, D.; Haupt, Y.; Barak, Y.; Oren, M. !$#journal Nucleic Acids Res. (1995) 23:2584-2592 !$#title A functional p53-responsive intronic promoter is contained !1within the human mdm2 gene. !$#cross-references MUID:95380270; PMID:7651818 !$#accession S57338 !'##status translation not shown !'##molecule_type DNA !'##residues 1-16,'P',18-24 ##label ZAU !'##cross-references EMBL:U28935; NID:g904033; PIDN:AAA82237.1; !1PID:g904034 REFERENCE G09070 !$#authors Lunec, J. !$#submission submitted to the EMBL Data Library, August 1995 !$#description Multiple alternate spliced mdm2 transcripts with loss of p53 !1binding domain sequences: transforming ability and frequent !1detection in human cancer. !$#accession G02026 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-27,223-491 ##label LUN !'##cross-references EMBL:U33199; NID:g992676; PIDN:AAA75514.1; !1PID:g992677 !'##experimental_source splice form A GENETICS !$#gene GDB:MDM2 !'##cross-references GDB:250456; OMIM:164785 !$#map_position 12q14.3-12q15 CLASSIFICATION #superfamily human p53-binding protein mdm2 KEYWORDS alternative splicing; oncogene; phosphoprotein FEATURE !$1-491 #product p53-binding protein mdm-2 #status predicted !8#label MAT1\ !$1-27,223-491 #product p53-binding protein mdm-2, splice form A !8#status predicted #label MAT2 SUMMARY #length 491 #molecular-weight 55232 #checksum 3945 SEQUENCE /// ENTRY SYECDB #type complete TITLE dethiobiotin synthase (EC 6.3.3.3) bioD [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES dethiobiotin synthetase ORGANISM #formal_name Escherichia coli DATE 31-Mar-1990 #sequence_revision 31-Oct-1997 #text_change 19-Jul-2002 ACCESSIONS B64814; F32025; S43866; Q00157 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession B64814 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-225 ##label BLAT !'##cross-references GB:AE000180; GB:U00096; NID:g1786988; !1PIDN:AAC73865.1; PID:g1786995; UWGP:b0778 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A32025 !$#authors Otsuka, A.J.; Buoncristiani, M.R.; Howard, P.K.; Flamm, J.; !1Johnson, C.; Yamamoto, R.; Uchida, K.; Cook, C.; Ruppert, !1J.; Matsuzaki, J. !$#journal J. Biol. Chem. (1988) 263:19577-19585 !$#title The Escherichia coli biotin biosynthetic enzyme sequences !1predicted from the nucleotide sequence of the bio operon. !$#cross-references MUID:89066784; PMID:3058702 !$#accession F32025 !'##molecule_type DNA !'##residues 1-28,'R',30-197,'RRCWERS',205,'G',207,'QKIQKMRQPEST' !1##label OTS !'##cross-references GB:J04423; NID:g145422; PIDN:AAA23518.1; !1PID:g145428 REFERENCE S43866 !$#authors Alexeev, D.; Bury, S.M.; Boys, C.W.G.; Turner, M.A.; Sawyer, !1L.; Ramsey, A.J.; Baxter, H.C.; Baxter, R.L. !$#journal J. Mol. Biol. (1994) 235:774-776 !$#title Sequence and crystallization of Escherichia coli !1dethiobiotin synthetase, the penultimate enzyme of biotin !1biosynthesis. !$#cross-references MUID:94118326; PMID:8289297 !$#accession S43866 !'##molecule_type DNA !'##residues 1-152,'T',154-225 ##label ALE !'##cross-references GB:S68059; NID:g460900; PIDN:AAB29683.1; !1PID:g460901 GENETICS !$#gene bioD !$#map_position 18 min !$#start_codon GTG FUNCTION !$#description catalyzes the ATP-driven condensation of 7, !18-diaminononanoate and carbon dioxide to form dethiobiotin !$#pathway biotin biosynthesis !$#note requires magnesium CLASSIFICATION #superfamily dethiobiotin synthetase KEYWORDS biotin biosynthesis; cyclo-ligase; magnesium SUMMARY #length 225 #molecular-weight 24139 #checksum 8566 SEQUENCE /// ENTRY I64123 #type complete TITLE dethiobiotin synthetase homolog HI1445 - Haemophilus influenzae (strain Rd KW20) ORGANISM #formal_name Haemophilus influenzae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jul-2002 ACCESSIONS I64123 REFERENCE A64000 !$#authors Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; !1Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; !1Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; !1FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, !1R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; !1Phillips, C.A.; Spriggs, T.; Hedblom, E.; Cotton, M.D.; !1Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; !1Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; !1Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; !1Fraser, C.M.; Smith, H.O.; Venter, J.C. !$#journal Science (1995) 269:496-512 !$#title Whole-genome random sequencing and assembly of Haemophilus !1influenzae Rd. !$#cross-references MUID:95350630; PMID:7542800 !$#accession I64123 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-242 ##label TIGR !'##cross-references GB:U32823; GB:L42023; NID:g1574281; !1PIDN:AAC23095.1; PID:g1574285; TIGR:HI1445 CLASSIFICATION #superfamily dethiobiotin synthetase SUMMARY #length 242 #molecular-weight 26967 #checksum 2955 SEQUENCE /// ENTRY S76661 #type complete TITLE hypothetical protein - Synechocystis sp. (strain PCC 6803) ORGANISM #formal_name Synechocystis sp. #variety PCC 6803 DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jul-2002 ACCESSIONS S76661 REFERENCE S74322 !$#authors Kaneko, T.; Sato, S.; Kotani, H.; Tanaka, A.; Asamizu, E.; !1Nakamura, Y.; Miyajima, N.; Hirosawa, M.; Sugiura, M.; !1Sasamoto, S.; Kimura, T.; Hosouchi, T.; Matsuno, A.; Muraki, !1A.; Nakazaki, N.; Naruo, K.; Okumura, S.; Shimpo, S.; !1Takeuchi, C.; Wada, T.; Watanabe, A.; Yamada, M.; Yasuda, !1M.; Tabata, S. !$#journal DNA Res. (1996) 3:109-136 !$#title Sequence analysis of the genome of the unicellular !1cyanobacterium Synechocystis sp. PCC6803. II. Sequence !1determination of the entire genome and assignment of !1potential protein-coding regions. !$#cross-references MUID:97061201; PMID:8905231 !$#accession S76661 !'##status preliminary !'##molecule_type DNA !'##residues 1-237 ##label KAN !'##cross-references EMBL:D64004; GB:AB001339; NID:g1001701; !1PIDN:BAA10605.1; PID:g1001767 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1June 1996 CLASSIFICATION #superfamily dethiobiotin synthetase SUMMARY #length 237 #molecular-weight 25805 #checksum 8251 SEQUENCE /// ENTRY JQ0506 #type complete TITLE dethiobiotin synthase (EC 6.3.3.3) - Bacillus sphaericus ORGANISM #formal_name Bacillus sphaericus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jul-2002 ACCESSIONS JQ0506 REFERENCE JQ0506 !$#authors Gloeckler, R.; Ohsawa, I.; Speck, D.; Ledoux, C.; Bernard, !1S.; Zinsius, M.; Villeval, D.; Kisou, T.; Kamogawa, K.; !1Lemoine, Y. !$#journal Gene (1990) 87:63-70 !$#title Cloning and characterization of the Bacillus sphaericus !1genes controlling the bioconversion of pimelate into !1dethiobiotin. !$#cross-references MUID:90236299; PMID:2110099 !$#accession JQ0506 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-234 ##label GLO !'##cross-references GB:M29292; NID:g142587; PIDN:AAB02324.1; !1PID:g551693 !'##experimental_source strain IFO3525 COMMENT This enzyme catalyzes the condensation of 7, !18-diaminononanoate and carbon dioxide to form dethiobiotin. GENETICS !$#gene bioD !$#start_codon TTG CLASSIFICATION #superfamily dethiobiotin synthetase KEYWORDS biotin biosynthesis; cyclo-ligase SUMMARY #length 234 #molecular-weight 26488 #checksum 2857 SEQUENCE /// ENTRY S72693 #type complete TITLE dethiobiotin synthase (EC 6.3.3.3) bioD - Mycobacterium leprae ALTERNATE_NAMES dethiobiotin synthetase bioD; Lepb1170_C1_159 protein ORGANISM #formal_name Mycobacterium leprae DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 19-Jul-2002 ACCESSIONS S72693 REFERENCE S72693 !$#authors Smith, D.R.; Robison, K. !$#submission submitted to the EMBL Data Library, November 1993 !$#description Mycobacterium leprae cosmid B1170. !$#accession S72693 !'##status preliminary !'##molecule_type DNA !'##residues 1-223 ##label SMI !'##cross-references EMBL:U00010; NID:g466780; PIDN:AAA17057.1; !1PID:g466781 GENETICS !$#gene bioD !$#start_codon GTG CLASSIFICATION #superfamily dethiobiotin synthetase KEYWORDS cyclo-ligase SUMMARY #length 223 #molecular-weight 22624 #checksum 6661 SEQUENCE /// ENTRY B55513 #type complete TITLE hoxX protein - Alcaligenes eutrophus ORGANISM #formal_name Alcaligenes eutrophus DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 10-Sep-1999 ACCESSIONS B55513 REFERENCE A55513 !$#authors Lenz, O.; Schwartz, E.; Dernedde, J.; Eitinger, M.; !1Friedrich, B. !$#journal J. Bacteriol. (1994) 176:4385-4393 !$#title The Alcaligenes eutrophus H16 hoxX gene participates in !1hydrogenase regulation. !$#cross-references MUID:94292469; PMID:8021224 !$#accession B55513 !'##status preliminary !'##molecule_type DNA !'##residues 1-597 ##label LEN !'##cross-references GB:X74670; NID:g516858; PID:g516859 GENETICS !$#gene hoxX CLASSIFICATION #superfamily hydrogenase regulation protein hoxX; enoyl-CoA !1hydratase homology FEATURE !$325-485 #domain enoyl-CoA hydratase homology #label ECH SUMMARY #length 597 #molecular-weight 65739 #checksum 4633 SEQUENCE /// ENTRY C71022 #type complete TITLE hypothetical protein PH1472 - Pyrococcus horikoshii ORGANISM #formal_name Pyrococcus horikoshii DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 21-Jul-2000 ACCESSIONS C71022 REFERENCE A71000 !$#authors Kawarabayasi, Y.; Sawada, M.; Horikawa, H.; Haikawa, Y.; !1Hino, Y.; Yamamoto, S.; Sekine, M.; Baba, S.; Kosugi, H.; !1Hosoyama, A.; Nagai, Y.; Sakai, M.; Ogura, K.; Otsuka, R.; !1Nakazawa, H.; Takamiya, M.; Ohfuku, Y.; Funahashi, T.; !1Tanaka, T.; Kudoh, Y.; Yamazaki, J.; Kushida, N.; Oguchi, !1A.; Aoki, K.; Yoshizawa, T.; Nakamura, Y.; Robb, F.T.; !1Horikoshi, K.; Masuchi, Y.; Shizuya, H.; Kikuchi, H. !$#journal DNA Res. (1998) 5:55-76 !$#title Complete sequence and gene organization of the genome of a !1hyper-thermophilic archaebacterium, Pyrococcus horikoshii !1OT3. !$#cross-references MUID:98344137; PMID:9679194 !$#accession C71022 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-197 ##label KAW !'##cross-references GB:AP000006; NID:g3236133; PIDN:BAA30579.1; !1PID:g3257896 !'##experimental_source strain OT3 !'##note this accession replaces an interim accession for a sequence !1replaced by GenBank GENETICS !$#gene PH1472 CLASSIFICATION #superfamily Archaeoglobus probable DNA-polymerase SUMMARY #length 197 #molecular-weight 22608 #checksum 4923 SEQUENCE /// ENTRY S14384 #type complete TITLE UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diamino-pimelate ligase (EC 6.3.2.13) [validated] - Escherichia coli (strain K-12) ALTERNATE_NAMES meso-diaminopimelate-adding enzyme; UDP-MurNac-tripeptide synthetase murE; UDP-N-acetylmuramyl-tripeptide synthetase ORGANISM #formal_name Escherichia coli DATE 02-Feb-2001 #sequence_revision 02-Feb-2001 #text_change 03-Jun-2002 ACCESSIONS S14384; S13862; E64730; S40595; S10691 REFERENCE S14384 !$#authors Tao, J.S.; Ishiguro, E.E. !$#journal Can. J. Microbiol. (1989) 35:1051-1054 !$#title Nucleotide sequence of the murE gene of Escherichia coli. !$#cross-references MUID:90124047; PMID:2692800 !$#accession S14384 !'##molecule_type DNA !'##residues 1-495 ##label TAO !'##cross-references EMBL:X55034; NID:g40841; PIDN:CAA38862.1; !1PID:g581032 !'##experimental_source strain K-12, substrain W3110 REFERENCE S13862 !$#authors Michaud, C.; Mengin-Lecreulx, D.; van Heijenoort, J.; !1Blanot, D. !$#journal Eur. J. Biochem. (1990) 194:853-861 !$#title Over-production, purification and properties of the !1uridine-diphosphate-N-acetylmuramoyl-L-alanyl-D-glutamate: !1meso-2,6-diaminopimelate ligase from Escherichia coli. !$#cross-references MUID:91099368; PMID:2269304 !$#accession S13862 !'##molecule_type DNA; protein !'##residues 2-19 ##label MIC REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession E64730 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-495 ##label BLAT !'##cross-references GB:AE000118; GB:U00096; NID:g1786262; !1PIDN:AAC73196.1; PID:g1786273; UWGP:b0085 !'##experimental_source strain K-12, substrain MG1655 REFERENCE S40531 !$#authors Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; !1Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. !$#submission submitted to the EMBL Data Library, December 1992 !$#description Systematic sequencing of the Escherichia coli genome: !1analysis of the 0-2.4min region. !$#accession S40595 !'##molecule_type DNA !'##residues 'V',2-495 ##label YUR !'##cross-references EMBL:D10483 !'##experimental_source strain K-12 REFERENCE S10690 !$#authors Michaud, C.; Parquet, C.; Flouret, B.; Blanot, D.; van !1Heijenoort, J. !$#journal Biochem. J. (1990) 269:277-278 !$#title Revised interpretation of the sequence containing the murE !1gene encoding the UDP-N-acetylmuramyl-tripeptide synthetase !1of Escherichia coli. !$#cross-references MUID:90328986; PMID:2198024 !$#accession S10691 !'##molecule_type DNA !'##residues 1-124 ##label MI2 !'##cross-references GB:X55814; NID:g296013; PIDN:CAA39334.1; !1PID:g581175 GENETICS !$#gene murE !$#start_codon GTG COMPLEX monomer [validated, MUID:91099368] FUNCTION !$#description EC 6.3.2.13 [validated, MUID:91099368] !$#pathway peptidoglycan biosynthesis CLASSIFICATION #superfamily UDP-N-acetylmuramoylalanyl-D-glutamate-2, !16-diaminopimelate ligase KEYWORDS ATP; cell division; cell wall; ligase; peptidoglycan !1biosynthesis; transmembrane protein SUMMARY #length 495 #molecular-weight 53343 #checksum 5100 SEQUENCE /// ENTRY A59159 #type complete TITLE methionine salvage pathway enzyme E-2/E-2' [validated] - Klebsiella oxytoca CONTAINS 5-methylthio-3-oxo-1-penten-1,2-diol dioxygenase (EC 1.13.11.-) ORGANISM #formal_name Klebsiella oxytoca DATE 02-Jun-2000 #sequence_revision 02-Jun-2000 #text_change 19-Jan-2001 ACCESSIONS A59159; B49101 REFERENCE A59159 !$#authors Mo, H.; Dai, Y.; Pochapsky, S.S.; Pochapsky, T.C. !$#submission submitted to BioMagResBank, March 1999 !$#description (1)H, (13)C and (15)N NMR assignments for a carbon monoxide !1generating metalloenzyme from Klebsiella pneumoniae. !$#accession A59159 !'##molecule_type protein !'##residues 2-180 ##label MOH !'##cross-references BMRB:4313 !'##note the source is designated as Klebsiella pneumoniae, but the !1cited sequence is from Klebsiella oxytoca; the initial !1methionine was not experimentally observed REFERENCE A49101 !$#authors Balakrishnan, R.; Frohlich, M.; Rahaim, P.T.; Backman, K.; !1Yocum, R.R. !$#journal J. Biol. Chem. (1993) 268:24792-24795 !$#title Cloning and sequence of the gene encoding enzyme E-1 from !1the methionine salvage pathway of Klebsiella oxytoca. !$#cross-references MUID:94043338; PMID:8227040 !$#accession B49101 !'##molecule_type DNA !'##residues 1-82 ##label BAL !'##cross-references GB:U00148; NID:g392019; PIDN:AAC43184.1; !1PID:g392021 COMMENT Athough His-138 is one of the residues predicted to be !1involved in nickel binding, it is not conserved in !1homologous proteins. GENETICS !$#gene masB CLASSIFICATION #superfamily Klebsiella methionine salvage pathway enzyme !1E-2/E-2' KEYWORDS metalloprotein; methionine biosynthesis; nickel; !1oxidoreductase FEATURE !$96,97,99,141 #binding_site nickel (Glu, His, His, His) #status !8predicted\ !$115-127 #disulfide_bonds #status experimental SUMMARY #length 180 #molecular-weight 20328 #checksum 2891 SEQUENCE /// ENTRY A55093 #type complete TITLE fatty acid transport protein precursor - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 08-Sep-2000 ACCESSIONS A55093; I49132 REFERENCE A55093 !$#authors Schaffer, J.E.; Lodish, H.F. !$#journal Cell (1994) 79:427-436 !$#title Expression cloning and characterization of a novel adipocyte !1long chain fatty acid transport protein. !$#cross-references MUID:95042740; PMID:7954810 !$#accession A55093 !'##status preliminary !'##molecule_type mRNA !'##residues 1-646 ##label SCH !'##cross-references GB:U15976; NID:g563828; PIDN:AAC71060.1; !1PID:g563829 GENETICS !$#gene FATP CLASSIFICATION #superfamily Mycobacterium tuberculosis probable fadD6 !1protein; acetate-CoA ligase homology FEATURE !$124-604 #domain acetate-CoA ligase homology #label ACL SUMMARY #length 646 #molecular-weight 71275 #checksum 6477 SEQUENCE /// ENTRY JW0107 #type complete TITLE very-long-chain acyl-CoA synthetase related protein - mouse ALTERNATE_NAMES VLACSR ORGANISM #formal_name Mus musculus #common_name house mouse DATE 10-Sep-1999 #sequence_revision 10-Sep-1999 #text_change 08-Sep-2000 ACCESSIONS JW0107 REFERENCE JW0107 !$#authors Berger, J.; Truppe, C.; Neumann, H.; Forss-Petter, S. !$#journal Biochem. Biophys. Res. Commun. (1998) 247:255-260 !$#title A novel relative of the very-long-chain acyl-CoA synthetase !1and fatty acid transporter protein genes with a distinct !1expression pattern. !$#cross-references MUID:98308102; PMID:9642112 !$#accession JW0107 !'##molecule_type mRNA !'##residues 1-689 ##label BER !'##cross-references GB:AJ223959 !'##experimental_source liver COMMENT This protein likely functions as a plasma membrane !1transporter of long chain fatty acid and as a peroxisomal !1membrane associated enzyme responsible for the activation of !1lomg chain fatty acids. CLASSIFICATION #superfamily Mycobacterium tuberculosis probable fadD6 !1protein; acetate-CoA ligase homology FEATURE !$169-647 #domain acetate-CoA ligase homology #label ACL SUMMARY #length 689 #molecular-weight 76200 #checksum 593 SEQUENCE /// ENTRY A38742 #type complete TITLE ecotin precursor [validated] - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 19-May-2000 #sequence_revision 19-May-2000 #text_change 01-Mar-2002 ACCESSIONS A38742; S16981; G64990 REFERENCE A38742 !$#authors McGrath, M.E.; Hines, W.M.; Sakanari, J.A.; Fletterick, !1R.J.; Craik, C.S. !$#journal J. Biol. Chem. (1991) 266:6620-6625 !$#title The sequence and reactive site of ecotin. A general !1inhibitor of pancreatic serine proteases from Escherichia !1coli. !$#cross-references MUID:91177925; PMID:2007606 !$#accession A38742 !'##status preliminary !'##molecule_type DNA !'##residues 1-162 ##label MCG !'##cross-references GB:M60876; NID:g145823; PIDN:AAA23719.1; !1PID:g145824 REFERENCE S16981 !$#authors Lee, H.R.; Seol, J.H.; Kim, O.M.; Lee, C.S.; Suh, S.W.; !1Hong, Y.M.; Tanaka, K.; Ichihara, A.; Ha, D.B.; Chung, C.H. !$#journal FEBS Lett. (1991) 287:53-56 !$#title Molecular cloning of the Ecotin gene in Escherichia coli. !$#cross-references MUID:91348229; PMID:1879537 !$#accession S16981 !'##status preliminary !'##molecule_type DNA !'##residues 1-162 ##label LEE !'##cross-references GB:X61951; NID:g41327; PIDN:CAA43954.1; PID:g41328 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession G64990 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-162 ##label BLAT !'##cross-references GB:AE000310; GB:U00096; NID:g2367131; !1PIDN:AAC75269.1; PID:g1788538; UWGP:b2209 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A73134 !$#authors Perona, J.J.; Fletterick, R.J. !$#submission submitted to the Brookhaven Protein Data Bank, November 1997 !$#cross-references PDB:1AZZ !$#contents annotation; X-ray crystallography, 2.3 angstroms, residues !126-162 REFERENCE A59231 !$#authors Perona, J.J.; Tsu, C.A.; Craik, C.S.; Fletterick, R.J. !$#journal Biochemistry (1997) 36:5381-5392 !$#title Crystal structure of an ecotin-collagenase complex suggests !1a model for recognition and cleavage of the collagen triple !1helix. !$#cross-references MUID:97299771; PMID:9154920 !$#contents annotation; X-ray crystallography, 2.5 angstroms REFERENCE A65493 !$#authors Shin, D.H.; Suh, S.W. !$#submission submitted to the Brookhaven Protein Data Bank, August 1996 !$#cross-references PDB:1ECY !$#contents annotation; X-ray crystallography, 2.19 angstroms, residues !121-142 REFERENCE A65494 !$#authors Shin, D.H.; Suh, S.W. !$#submission submitted to the Brookhaven Protein Data Bank, August 1996 !$#cross-references PDB:1ECZ !$#contents annotation; X-ray crystallography, 2.68 angstroms, residues !121-142 GENETICS !$#gene eco; eti CLASSIFICATION #superfamily Escherichia coli ecotin KEYWORDS periplasmic space; serine proteinase inhibitor FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-162 #product ecotin #status experimental #label MAT\ !$70-107 #disulfide_bonds #status experimental\ !$104 #inhibitory_site Met (serine proteinase) #status !8experimental SUMMARY #length 162 #molecular-weight 18192 #checksum 4263 SEQUENCE /// ENTRY I39710 #type complete TITLE cellulose biosynthesis protein celD - Agrobacterium tumefaciens ORGANISM #formal_name Agrobacterium tumefaciens DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Dec-1999 ACCESSIONS I39710 REFERENCE I39709 !$#authors Matthysse, A.G.; White, S.; Lightfoot, R. !$#journal J. Bacteriol. (1995) 177:1069-1075 !$#title Genes required for cellulose synthesis in Agrobacterium !1tumefaciens. !$#cross-references MUID:95164506; PMID:7860585 !$#accession I39710 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-584 ##label RES !'##cross-references GB:L38609; NID:g710486; PIDN:AAC41431.1; !1PID:g710488 COMMENT This protein is required for cellulose biosynthesis. GENETICS !$#gene celD CLASSIFICATION #superfamily Agrobacterium tumefaciens cellulose !1biosynthesis protein celD SUMMARY #length 584 #molecular-weight 65787 #checksum 4007 SEQUENCE /// ENTRY S71357 #type complete TITLE nodulation protein noeB - Rhizobium meliloti ORGANISM #formal_name Rhizobium meliloti DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Dec-1999 ACCESSIONS S71357 REFERENCE S71357 !$#authors Ardourel, M.; Lortet, G.; Maillet, F.; Roche, P.; Truchet, !1G.; Prome, J.C.; Rosenberg, C. !$#journal Mol. Microbiol. (1995) 17:687-699 !$#title In Rhizobium meliloti, the operon associated with the nod !1box n5 comprises nodL, noeA and noeB, three host-range genes !1specifically required for the nodulation of particular !1Medicago species. !$#cross-references MUID:96111489; PMID:8801423 !$#accession S71357 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-553 ##label ARD !'##cross-references EMBL:U26430; NID:g1326068; PIDN:AAC44092.1; !1PID:g1326071 !'##experimental_source strain RCR2011 (=SU47) !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1May 1996 GENETICS !$#gene noeB CLASSIFICATION #superfamily Rhizobium meliloti nodulation protein noeB KEYWORDS host range; nodulation SUMMARY #length 553 #molecular-weight 60732 #checksum 9748 SEQUENCE /// ENTRY D43735 #type complete TITLE cellulose biosynthesis protein bcsD - Acetobacter pasteurianus ORGANISM #formal_name Acetobacter pasteurianus DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Dec-1999 ACCESSIONS D43735 REFERENCE A43735 !$#authors Wong, H.C.; Fear, A.L.; Calhoon, R.D.; Eichinger, G.H.; !1Mayer, R.; Amikam, D.; Benziman, M.; Gelfand, D.H.; Meade, !1J.H.; Emerick, A.W.; Bruner, R.; Ben-Bassat, A.; Tal, R. !$#journal Proc. Natl. Acad. Sci. U.S.A. (1990) 87:8130-8134 !$#title Genetic organization of the cellulose synthase operon in !1Acetobacter xylinum. !$#cross-references MUID:91045951; PMID:2146681 !$#accession D43735 !'##status translation not shown !'##molecule_type DNA !'##residues 1-156 ##label WON !'##cross-references EMBL:M37202; NID:g141731; PIDN:AAA21887.1; !1PID:g141735 !'##note the source is designated as Acetobacter xylinum COMMENT This protein is required for cellulose biosynthesis. CLASSIFICATION #superfamily Acetobacter pasteurianus cellulose biosynthesis !1protein bcsD SUMMARY #length 156 #molecular-weight 17298 #checksum 182 SEQUENCE /// ENTRY S61388 #type complete TITLE dotA protein - Legionella pneumophila ORGANISM #formal_name Legionella pneumophila DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Dec-1999 ACCESSIONS S61388 REFERENCE S61388 !$#authors Berger, K.H.; Merriam, J.J.; Isberg, R.R. !$#journal Mol. Microbiol. (1994) 14:809-822 !$#title Altered intracellular targeting properties associated with !1mutations in the Legionella pneumophila dotA gene. !$#cross-references MUID:95198553; PMID:7891566 !$#accession S61388 !'##molecule_type DNA !'##residues 1-1048 ##label BER !'##cross-references EMBL:U07940; NID:g563802; PIDN:AAA79902.1; !1PID:g563803 COMMENT This protein is involved in the intracellular targeting of !1this organism. GENETICS !$#gene dotA CLASSIFICATION #superfamily Legionella pneumophila dotA protein SUMMARY #length 1048 #molecular-weight 113187 #checksum 8160 SEQUENCE /// ENTRY B30754 #type complete TITLE tellurium resistance protein terB - Alcaligenes sp. plasmid pMJ606 ORGANISM #formal_name Alcaligenes sp. DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 18-Aug-2000 ACCESSIONS JT0362; B30754 REFERENCE JT0361 !$#authors Jobling, M.G.; Ritchie, D.A. !$#journal Gene (1988) 66:245-258 !$#title Nucleotide sequence of a plasmid determinant for resistance !1to tellurium anions. !$#cross-references MUID:89006266; PMID:3049247 !$#accession JT0362 !'##molecule_type DNA !'##residues 1-122 ##label JO1 !'##cross-references GB:M20238; NID:g141975; PIDN:AAA98290.1; !1PID:g1088256 REFERENCE A30754 !$#authors Jobling, M.G. !$#submission submitted to GenBank, September 1988 !$#accession B30754 !'##molecule_type DNA !'##residues 1-122 ##label JO2 CLASSIFICATION #superfamily Alcaligenes tellurium resistance protein terB SUMMARY #length 122 #molecular-weight 13725 #checksum 1514 SEQUENCE /// ENTRY H64847 #type complete TITLE acidic protein msyB - Escherichia coli (strain K-12) ALTERNATE_NAMES multicopy suppressor of secY ORGANISM #formal_name Escherichia coli DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 01-Mar-2002 ACCESSIONS H64847; C42290 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H64847 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-125 ##label BLAT !'##cross-references GB:AE000206; GB:U00096; NID:g1787282; !1PIDN:AAC74135.1; PID:g1787289; UWGP:b1051 !'##experimental_source strain K-12, substrain MG1655 REFERENCE A42290 !$#authors Ueguchi, C.; Ito, K. !$#journal J. Bacteriol. (1992) 174:1454-1461 !$#title Multicopy suppression: an approach to understanding !1intracellular functioning of the protein export system. !$#cross-references MUID:92165719; PMID:1537791 !$#accession C42290 !'##status preliminary !'##molecule_type DNA !'##residues 2-125 ##label UEG !'##cross-references EMBL:X59939; NID:g42028; PIDN:CAA42563.1; !1PID:g42030 !'##experimental_source strain K-12 GENETICS !$#gene msyB FUNCTION !$#description may participate in protein export CLASSIFICATION #superfamily Escherichia coli acidic protein msyB SUMMARY #length 125 #molecular-weight 14390 #checksum 463 SEQUENCE /// ENTRY S70969 #type complete TITLE bundle-forming pilus locus protein bfpC - Escherichia coli plasmid EAF ORGANISM #formal_name Escherichia coli DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 16-Jun-2000 ACCESSIONS S70969 REFERENCE S70966 !$#authors Stone, K.D.; Zhang, H.Z.; Carlson, L.K.; Donnenberg, M.S. !$#journal Mol. Microbiol. (1996) 20:325-337 !$#title A cluster of fourteen genes from enteropathogenic !1Escherichia coli is sufficient for the biogenesis of a type !1IV pilus. !$#cross-references MUID:96310370; PMID:8733231 !$#accession S70969 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-402 ##label STO !'##cross-references EMBL:Z68186; NID:g1122399; PIDN:CAA92329.1; !1PID:g1122403 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1December 1995 COMMENT Proteins of the bfp locus are required for type IV pilus !1biogenesis, which is associated with the localized adherence !1property of pathogenic E. coli. GENETICS !$#gene bfpC !$#genome plasmid CLASSIFICATION #superfamily Escherichia coli plasmid EAF bundle-forming !1pilus locus protein bfpC SUMMARY #length 402 #molecular-weight 45301 #checksum 8133 SEQUENCE /// ENTRY S08619 #type complete TITLE formate hydrogenlyase regulatory protein - Escherichia coli (strain K-12) ALTERNATE_NAMES hydrogenase-3 protein A ORGANISM #formal_name Escherichia coli DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 01-Mar-2002 ACCESSIONS S08619; A65053 REFERENCE S08619 !$#authors Boehm, R.; Sauter, M.; Boeck, A. !$#journal Mol. Microbiol. (1990) 4:231-243 !$#title Nucleotide sequence and expression of an operon in !1Escherichia coli coding for formate hydrogenylase !1components. !$#cross-references MUID:90251163; PMID:2187144 !$#accession S08619 !'##molecule_type DNA !'##residues 1-153 ##label BOE !'##cross-references EMBL:X17506; NID:g556890; PIDN:CAA35546.1; !1PID:g41680 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession A65053 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-153 ##label BLAT !'##cross-references GB:AE000356; GB:U00096; NID:g2367153; !1PIDN:AAC75767.1; PID:g1789080; UWGP:b2725 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene hycA !$#map_position 58-59 min CLASSIFICATION #superfamily Escherichia coli formate hydrogenlyase !1regulatory protein KEYWORDS transcription regulation SUMMARY #length 153 #molecular-weight 17627 #checksum 9302 SEQUENCE /// ENTRY H65205 #type complete TITLE heat shock protein htrC - Escherichia coli (strain K-12) ORGANISM #formal_name Escherichia coli DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 01-Mar-2002 ACCESSIONS H65205 REFERENCE A64720 !$#authors Blattner, F.R.; Plunkett III, G.; Bloch, C.A.; Perna, N.T.; !1Burland, V.; Riley, M.; Collado-Vides, J.; Glasner, J.D.; !1Rode, C.K.; Mayhew, G.F.; Gregor, J.; Davis, N.W.; !1Kirkpatrick, H.A.; Goeden, M.A.; Rose, D.J.; Mau, B.; Shao, !1Y. !$#journal Science (1997) 277:1453-1462 !$#title The complete genome sequence of Escherichia coli K-12. !$#cross-references MUID:97426617; PMID:9278503 !$#accession H65205 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-179 ##label BLAT !'##cross-references GB:AE000473; GB:U00096; NID:g2367336; !1PIDN:AAC76963.1; PID:g1790422; UWGP:b3989 !'##experimental_source strain K-12, substrain MG1655 GENETICS !$#gene htrC CLASSIFICATION #superfamily Escherichia coli heat shock protein htrC SUMMARY #length 179 #molecular-weight 21131 #checksum 3009 SEQUENCE /// ENTRY S02828 #type complete TITLE albicidin resistance protein - Klebsiella oxytoca ORGANISM #formal_name Klebsiella oxytoca DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Dec-1999 ACCESSIONS S02828 REFERENCE S02828 !$#authors Walker, M.J.; Birch, R.G.; Pemberton, J.M. !$#journal Mol. Microbiol. (1988) 2:443-454 !$#title Cloning and characterization of an albicidin resistance gene !1from Klebsiella oxytoca. !$#cross-references MUID:89013885; PMID:2845223 !$#accession S02828 !'##molecule_type DNA !'##residues 1-218 ##label WAL !'##cross-references EMBL:Y00558; NID:g43785; PIDN:CAA68640.1; !1PID:g43786 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing COMMENT This protein forms an inactive complex with albicidin. CLASSIFICATION #superfamily Klebsiella oxytoca albicidin resistance protein KEYWORDS antibiotic resistance FEATURE !$1-218 #product albicidin resistance protein #status !8experimental #label MAT SUMMARY #length 218 #molecular-weight 25858 #checksum 7627 SEQUENCE /// ENTRY JN0523 #type complete TITLE toxin coregulated pilus biosynthesis protein tcpS precursor - Vibrio cholerae ALTERNATE_NAMES tcpE protein ORGANISM #formal_name Vibrio cholerae DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Dec-1999 ACCESSIONS JN0523; S23270 REFERENCE JN0521 !$#authors Ogierman, M.A.; Zabihi, S.; Mourtzios, L.; Manning, P.A. !$#journal Gene (1993) 126:51-60 !$#title Genetic organization and sequence of the promoter-distal !1region of the tcp gene cluster of Vibrio cholerae. !$#cross-references MUID:93231537; PMID:8097178 !$#accession JN0523 !'##molecule_type DNA !'##residues 1-152 ##label OGI !'##cross-references EMBL:X64098; NID:g48404; PIDN:CAA45461.1; !1PID:g48414 GENETICS !$#gene tcpS CLASSIFICATION #superfamily Vibrio cholerae toxin coregulated pilus !1biosynthesis protein tcpS FEATURE !$1-20 #domain signal sequence #status predicted #label SIG\ !$21-152 #product tcpS protein #status predicted #label MAT SUMMARY #length 152 #molecular-weight 17417 #checksum 7318 SEQUENCE /// ENTRY A38705 #type complete TITLE heterocyst development protein hetR - Anabaena sp. (strain PCC 7120) ORGANISM #formal_name Anabaena sp. DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Dec-1999 ACCESSIONS A38705 REFERENCE A38705 !$#authors Buikema, W.J.; Haselkorn, R. !$#journal Genes Dev. (1991) 5:321-330 !$#title Characterization of a gene controlling heterocyst !1differentiation in the cyanobacterium Anabaena 7120. !$#cross-references MUID:91138965; PMID:1840555 !$#accession A38705 !'##molecule_type DNA !'##residues 1-299 ##label BUI !'##cross-references GB:M37779; NID:g142021; PIDN:AAA21998.1; !1PID:g142022 COMMENT This protein is required for and probably controls !1heterocyst development. CLASSIFICATION #superfamily Anabaena heterocyst development protein hetR SUMMARY #length 299 #molecular-weight 34969 #checksum 7634 SEQUENCE /// ENTRY A41970 #type complete TITLE coat morphogenesis sporulation protein spoIVA - Bacillus subtilis ALTERNATE_NAMES spore cortex formation and coat assembly protein spoIVA; stage IV sporulation protein spoIVA ORGANISM #formal_name Bacillus subtilis DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 21-Jul-2000 ACCESSIONS A41970; A44922; F69713 REFERENCE A41970 !$#authors Roels, S.; Driks, A.; Losick, R. !$#journal J. Bacteriol. (1992) 174:575-585 !$#title Characterization of spoIVA, a sporulation gene involved in !1coat morphogenesis in Bacillus subtilis. !$#cross-references MUID:92105027; PMID:1729246 !$#accession A41970 !'##molecule_type DNA !'##residues 1-492 ##label ROE !'##cross-references GB:M80926; NID:g143649; PIDN:AAB59029.1; !1PID:g143651 !'##note sequence inconsistent with the nucleotide translation !'##note sequence extracted from NCBI backbone (NCBIN:75483, !1NCBIP:75486) REFERENCE A44922 !$#authors Stevens, C.M.; Daniel, R.; Illing, N.; Errington, J. !$#journal J. Bacteriol. (1992) 174:586-594 !$#title Characterization of a sporulation gene, spoIVA, involved in !1spore coat morphogenesis in Bacillus subtilis. !$#cross-references MUID:92105028; PMID:1729247 !$#accession A44922 !'##molecule_type DNA !'##residues 1-492 ##label STE !'##cross-references GB:M81169; NID:g143635; PIDN:AAA22802.1; !1PID:g143636 !'##note sequence extracted from NCBI backbone (NCBIN:75495, !1NCBIP:75497) REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession F69713 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-492 ##label KUN !'##cross-references GB:Z99115; GB:AL009126; NID:g2634478; !1PIDN:CAB14196.1; PID:g2634698 !'##experimental_source strain 168 COMMENT This protein is required in the mother cell compartment for !1correct assembly of the spore coat. GENETICS !$#gene spoIVA !$#start_codon TTG !$#note gene is transcribed from a sigma E-dependent promoter CLASSIFICATION #superfamily Bacillus subtilis coat morphogenesis !1sporulation protein spoIVA KEYWORDS sporulation SUMMARY #length 492 #molecular-weight 55174 #checksum 8307 SEQUENCE /// ENTRY B69598 #type complete TITLE spore maturation protein cgeC - Bacillus subtilis ORGANISM #formal_name Bacillus subtilis DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 16-Jun-2000 ACCESSIONS B69598 REFERENCE A69580 !$#authors Kunst, F.; Ogasawara, N.; Moszer, I.; Albertini, A.M.; !1Alloni, G.; Azevedo, V.; Bertero, M.G.; Bessieres, P.; !1Bolotin, A.; Borchert, S.; Boriss, R.; Boursier, L.; Brans, !1A.; Braun, M.; Brignell, S.C.; Bron, S.; Brouillet, S.; !1Bruschi, C.V.; Caldwell, B.; Capuano, V.; Carter, N.M.; !1Choi, S.K.; Codani, J.J.; Connerton, I.F.; Cummings, N.J.; !1Daniel, R.A.; Denizot, F.; Devine, K.M.; Duesterhoeft, A.; !1Ehrlich, S.D.; Emmerson, P.T.; Entian, K.D.; Errington, J.; !1Fabret, C.; Ferrari, E.; Foulger, D.; Fritz, C.; Fujita, M.; !1Fujita, Y.; Fuma, S.; Galizzi, A.; Galleron, N.; Ghim, S.Y.; !1Glaser, P.; Goffeau, A.; Golightly, E.J.; Grandi, G.; !1Guiseppi, G.; Guy, B.J.; Haga, K.; Haiech, J.; Harwood, !1C.R.; Henaut, A.; Hilbert, H.; Holsappel, S.; Hosono, S.; !1Hullo, M.F.; Itaya, M.; Jones, L.; Joris, B.; Karamata, D.; !1Kasahara, Y.; Klaerr-Blanchard, M.; Klein, C.; Kobayashi, !1Y.; Koetter, P.; Koningstein, G.; Krogh, S.; Kumano, M.; !1Kurita, K.; Lapidus, A.; Lardinois, S.; Lauber, J.; !1Lazarevic, V.; Lee, S.M.; Levine, A.; Liu, H.; Masuda, S.; !1Maueel, C.; Medigue, C.; Medina, N.; Mellado, R.P.; Mizuno, !1M.; Moestl, D.; Nakai, S.; Noback, M.; Noone, D.; O'Reilly, !1M.; Ogawa, K.; Ogiwara, A.; Oudega, B.; Park, S.H.; Parro, !1V.; Pohl, T.M.; Portetelle, D.; Porwolik, S.; Prescott, !1A.M.; Presecan, E.; Pujic, P.; Purnelle, B.; Rapoport, G.; !1Rey, M.; Reynolds, S.; Rieger, M.; Rivolta, C.; Rocha, E.; !1Roche, B.; Rose, M.; Sadaie, Y.; Sato, T.; Scanlon, E.; !1Schleich, S.; Schroeter, R.; Scoffone, F.; Sekiguchi, J.; !1Sekowska, A.; Seror, S.J.; Serror, P.; Shin, B.S.; Soldo, !1B.; Sorokin, A.; Tacconi, E.; Takagi, T.; Takahashi, H.; !1Takemaru, K.; Takeuchi, M.; Tamakoshi, A.; Tanaka, T.; !1Terpstra, P.; Tognoni, A.; Tosato, V.; Uchiyama, S.; !1Vandenbol, M.; Vannier, F.; Vassarotti, A.; Viari, A.; !1Wambutt, R.; Wedler, E.; Wedler, H.; Weitzenegger, T.; !1Winters, P.; Wipat, A.; Yamamoto, H.; Yamane, K.; Yasumoto, !1K.; Yata, K.; Yoshida, K.; Yoshikawa, H.F.; Zumstein, E.; !1Yoshikawa, H.; Danchin, A. !$#journal Nature (1997) 390:249-256 !$#title The complete genome sequence of the Gram-positive bacterium !1Bacillus subtilis. !$#cross-references MUID:98044033; PMID:9384377 !$#accession B69598 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-101 ##label KUN !'##cross-references GB:Z99114; GB:AL009126; NID:g2634230; !1PIDN:CAB13868.1; PID:g2634369 !'##experimental_source strain 168 GENETICS !$#gene cgeC CLASSIFICATION #superfamily Bacillus subtilis spore maturation protein cgeC SUMMARY #length 101 #molecular-weight 11382 #checksum 5714 SEQUENCE /// ENTRY JC6042 #type complete TITLE cytosol nonspecific dipeptidase (EC 3.4.13.18) - Lactobacillus helveticus ALTERNATE_NAMES dehydropeptidase-I; dipeptidase A; pepDA protein ORGANISM #formal_name Lactobacillus helveticus DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Jun-2002 ACCESSIONS JC6042 REFERENCE JC6042 !$#authors Dudley, E.G.; Husgen, A.C.; He, W.; Steele, J.L. !$#journal J. Bacteriol. (1996) 178:701-704 !$#title Sequencing, distribution, and inactivation of the !1dipeptidase A gene (pepDA) from Lactobacillus helveticus !1CNRZ32. !$#cross-references MUID:96146518; PMID:8550503 !$#accession JC6042 !'##molecule_type DNA !'##residues 1-474 ##label DUD !'##cross-references GB:U34257; NID:g1072049; PIDN:AAC43971.1; !1PID:g1072051 !'##experimental_source CNR32 COMMENT This enzyme plays a role in cheese flavor development in !1milk. GENETICS !$#gene pepDA CLASSIFICATION #superfamily Lactobacillus helveticus cytosol non-specific !1dipeptidase KEYWORDS cytosol; dipeptide hydrolase SUMMARY #length 474 #molecular-weight 53512 #checksum 1684 SEQUENCE /// ENTRY G01589 #type complete TITLE ionizing radiation resistance conferring protein - human ORGANISM #formal_name Homo sapiens #common_name man DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Dec-1999 ACCESSIONS G01589 REFERENCE G07863 !$#authors Henning, K.A. !$#submission submitted to the EMBL Data Library, December 1994 !$#accession G01589 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-382 ##label HEN !'##cross-references EMBL:U18321; NID:g603763; PIDN:AAA57443.1; !1PID:g603764 CLASSIFICATION #superfamily human ionizing radiation resistance conferring !1protein SUMMARY #length 382 #molecular-weight 43611 #checksum 7672 SEQUENCE /// ENTRY I38927 #type complete TITLE melanoma antigen p15 - human ORGANISM #formal_name Homo sapiens #common_name man DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 20-Apr-2000 ACCESSIONS I38927 REFERENCE I38927 !$#authors Robbins, P.F.; el-Gamil, M.; Li, Y.F.; Topalian, S.L.; !1Rivoltini, L.; Sakaguchi, K.; Appella, E.; Kawakami, Y.; !1Rosenberg, S.A. !$#journal J. Immunol. (1995) 154:5944-5950 !$#title Cloning of a new gene encoding an antigen recognized by !1melanoma-specific HLA-A24-restricted tumor-infiltrating !1lymphocytes. !$#cross-references MUID:95270988; PMID:7751637 !$#accession I38927 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-128 ##label RES !'##cross-references EMBL:U19796; NID:g836929; PIDN:AAC50181.1; !1PID:g836930 GENETICS !$#gene GDB:MAAT1 !'##cross-references GDB:9954395 CLASSIFICATION #superfamily human melanoma antigen p15 SUMMARY #length 128 #molecular-weight 14849 #checksum 7230 SEQUENCE /// ENTRY S61532 #type complete TITLE RET oncogene fusion partner RFG - human ALTERNATE_NAMES ELE1 protein; protein DKFZp762E1112.1 ORGANISM #formal_name Homo sapiens #common_name man DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 09-Jun-2000 ACCESSIONS S61532; I37340; T47162; I38154 REFERENCE S61532 !$#authors Santoro, M.; Dathan, N.A.; Berlingieri, M.T.; Bongarzone, !1I.; Paulin, C.; Grieco, M.; Pierotti, M.A.; Vecchio, G.; !1Fusco, A. !$#journal Oncogene (1994) 9:509-516 !$#title Molecular characterization of RET/PTC3; a novel rearranged !1version of the RETproto-oncogene in a human thyroid !1papillary carcinoma. !$#cross-references MUID:94119592; PMID:8290261 !$#accession S61532 !'##molecule_type mRNA !'##residues 1-614 ##label SAN !'##cross-references EMBL:X77548; NID:g469145; PIDN:CAA54673.1; !1PID:g469146 !'##experimental_source normal thyroid cDNA library REFERENCE I37340 !$#authors Bongarzone, I.; Butti, M.G.; Coronelli, S.; Borrello, M.G.; !1Santoro, M.; Mondellini, P.; Pilotti, S.; Fusco, A.; Della !1Porta, G.; Pierotti, M.A. !$#journal Cancer Res. (1994) 54:2979-2985 !$#title Frequent activation of ret protooncogene by fusion with a !1new activating gene in papillary thyroid carcinomas. !$#cross-references MUID:94243818; PMID:8187085 !$#accession I37340 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-161,'T',163-182,'S',184-238 ##label RES !'##cross-references EMBL:X71413; NID:g296286; PIDN:CAA50536.1; !1PID:g557270 REFERENCE Z24375 !$#authors Ansorge, W.; Wirkner, U.; Mewes, H.W.; Weil, B.; Wiemann, S. !$#submission submitted to the Protein Sequence Database, March 2000 !$#accession T47162 !'##molecule_type mRNA !'##residues 1-315,'KP',318-363,'G',365-614 ##label AAA !'##cross-references EMBL:AL162047 !'##experimental_source adult melanoma (MeWo cell line); clone !1DKFZp762E1112 COMMENT The gene RFG (RET-fused gene) was identified as the fusion !1partner of the receptor tyrosine kinse proto-oncogene RET in !1thyroid papillary carcinoma. The sequence shown here is !1wild-type RFG from normal thyroid. GENETICS !$#gene GDB:ELE1; RFG; ARA70; NCOA4 !'##cross-references GDB:9954453; OMIM:601984 !$#map_position 10q11.2-10q11.2 !$#note DKFZp762E1112.1 CLASSIFICATION #superfamily human RET oncogene fusion partner RFG SUMMARY #length 614 #molecular-weight 69699 #checksum 1014 SEQUENCE /// ENTRY A40157 #type complete TITLE androgen-regulated protein precursor, renal - mouse ORGANISM #formal_name Mus musculus #common_name house mouse DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 03-Dec-1999 ACCESSIONS A40157 REFERENCE A40157 !$#authors Meseguer, A.; Watson, C.S.; Catterall, J.F. !$#journal Mol. Endocrinol. (1989) 3:962-967 !$#title Nucleotide sequence of kidney androgen-regulated protein !1mRNA and its cell-specific expression in Tfm/Y mice. !$#cross-references MUID:89295446; PMID:2739660 !$#accession A40157 !'##molecule_type mRNA !'##residues 1-121 ##label MES !'##cross-references GB:M22810; NID:g198565; PIDN:AAB01364.1; !1PID:g309418 GENETICS !$#gene KAP CLASSIFICATION #superfamily mouse androgen-regulated protein, renal FEATURE !$1-18 #domain signal sequence #status predicted #label SIG\ !$19-121 #product androgen-regulated protein #status predicted !8#label MAT SUMMARY #length 121 #molecular-weight 13263 #checksum 4242 SEQUENCE /// ENTRY S53048 #type complete TITLE alpha-mannosidase (EC 3.2.1.24) - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein G1861; protein YGL156w ORGANISM #formal_name Saccharomyces cerevisiae DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 21-Jul-2000 ACCESSIONS S60420; A33511; S64172; S53048 REFERENCE S60417 !$#authors James, C.M.; Indge, K.J.; Oliver, S.G. !$#journal Yeast (1995) 11:1413-1419 !$#title DNA sequence analysis of a 35 kb segment from Saccharomyces !1cerevisiae chromosome VII reveals 19 open reading frames !1including RAD54, ACE1/CUP2, PMR1, RCK1, AMS1 and CAL1/CDC43. !$#cross-references MUID:96158061; PMID:8585324 !$#accession S60420 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 1-1083 ##label JAM1 !'##cross-references EMBL:Z48618; NID:g728690; PIDN:CAA88536.1; !1PID:g728694 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1March 1995 REFERENCE A33511 !$#authors Yoshihisa, T.; Anraku, Y. !$#journal Biochem. Biophys. Res. Commun. (1989) 163:908-915 !$#title Nucleotide sequence of AMS1, the structure gene of vacuolar !1alpha-mannosidase of Saccharomyces cerevisiae. !$#cross-references MUID:89392009; PMID:2675832 !$#accession A33511 !'##molecule_type DNA !'##residues 1-785,'L',787-797,'A',799-1083 ##label YOS !'##cross-references GB:M29146; NID:g171056; PIDN:AAA34423.1; !1PID:g171058; GB:M27809 !'##note the authors translated the codon CTT for residue 786 as Val, !1and GCT for residue 798 as Val REFERENCE S64165 !$#authors James, C.M.; Indge, K.J.; Oliver, S.G. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64172 !'##molecule_type DNA !'##residues 1-1083 ##label JAM2 !'##cross-references EMBL:Z72678; NID:g1322745; PIDN:CAA96868.1; !1PID:g1322746; GSPDB:GN00007; MIPS:YGL156w !'##experimental_source strain S288C GENETICS !$#gene SGD:AMS1; MIPS:YGL156w !'##cross-references SGD:S0003124; MIPS:YGL156w !$#map_position 7L CLASSIFICATION #superfamily Saccharomyces alpha-mannosidase KEYWORDS blocked amino end; glycosidase; hydrolase; yeast vacuole SUMMARY #length 1083 #molecular-weight 124498 #checksum 3458 SEQUENCE /// ENTRY T46931 #type complete TITLE alpha-mannosidase (EC 3.2.1.24), cytosolic [similarity] - human ALTERNATE_NAMES protein DKFZp434D175.1 ORGANISM #formal_name Homo sapiens #common_name man DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 05-May-2000 ACCESSIONS T46931; JE0137; G02152; JC5676 REFERENCE Z24138 !$#authors Duesterhoeft, A.; Lauber, J.; Mewes, H.W.; Weil, B.; !1Wiemann, S. !$#submission submitted to the Protein Sequence Database, February 2000 !$#accession T46931 !'##molecule_type mRNA !'##residues 1-1040 ##label AAA !'##cross-references EMBL:AL136876; NID:g7018433; PIDN:CAB66810.1; !1PID:g7018434 !'##experimental_source adult testis; clone DKFZp434D175 REFERENCE JE0137 !$#authors Zhang, L.X.; Zhu, L.P.; Shi, W.; Ma, F.R.; Zhu, Q.L.; Zhang, !1S.Z.; Wang, X.; Li, G.Y. !$#journal Chinese J. Microbiol. Immunol. (1997) 17:34-38 !$#title Cloning of a human cDNA homologous to the cDNA encoding a !1rat ER alpha-mannosidase. !$#accession JE0137 !'##molecule_type mRNA !'##residues 638-1013, !1'SGQPPEAHLFSLPSAVPVARASASATLSPWGWGFVCRRLWGLLISASPA' ##label !1ZHA !'##cross-references EMBL:U37248; NID:g1017778; PIDN:AAC00568.1; !1PID:g1017779 !'##experimental_source tissue tonsil !'##note the journal is cited in GenBank entry HSU37248, release 113.0, !1as "Chung-Hua Min Kuo Wei Sheng Wu Chi Mien I Hsueh Tsa !1Chih" GENETICS !$#gene GDB:MAN2C1; MANA1; MANA; 6A8 !'##cross-references GDB:119375; OMIM:154580 !$#map_position 15q11-15qter !$#note DKFZp434D175.1 CLASSIFICATION #superfamily Saccharomyces alpha-mannosidase KEYWORDS glycoprotein; glycosidase; hydrolase SUMMARY #length 1040 #molecular-weight 115834 #checksum 4774 SEQUENCE /// ENTRY A38306 #type complete TITLE alpha-mannosidase (EC 3.2.1.24) - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 05-May-2000 #sequence_revision 05-May-2000 #text_change 05-May-2000 ACCESSIONS A38306 REFERENCE A38306 !$#authors Bischoff, J.; Moremen, K.; Lodish, H.F. !$#journal J. Biol. Chem. (1990) 265:17110-17117 !$#title Isolation, characterization, and expression of cDNA encoding !1a rat liver endoplasmic reticulum alpha-mannosidase. !$#cross-references MUID:91009139; PMID:2211613 !$#accession A38306 !'##status preliminary !'##molecule_type mRNA !'##residues 1-1040 ##label BIS !'##cross-references GB:M57547; GB:J05632; NID:g205298; PIDN:AAA41565.1; !1PID:g205299 CLASSIFICATION #superfamily Saccharomyces alpha-mannosidase KEYWORDS glycosidase; hydrolase SUMMARY #length 1040 #molecular-weight 115970 #checksum 6385 SEQUENCE /// ENTRY T08228 #type complete TITLE plasmid replication protein repH [validated] - Halobacterium sp. (strain NRC-1) plasmid pNRC100 ALTERNATE_NAMES hypothetical protein H0136 ORGANISM #formal_name Halobacterium sp. #variety strain NRC-1 DATE 18-Feb-2000 #sequence_revision 18-Feb-2000 #text_change 18-Feb-2000 ACCESSIONS T08228; A40600 REFERENCE Z16408 !$#authors Ng, W.V.; Ciufo, S.A.; Smith, T.M.; Bumgarner, R.E.; Baskin, !1D.; Faust, J.; Hall, B.; Loretz, C.; Seto, J.; Slagel, J.; !1Hood, L.; DasSarma, S. !$#journal Genome Res. (1998) 8:1131-1141 !$#title Snapshot of a large dynamic replicon in a halophilic !1Archaeon: megaplasmid or minichromosome? !$#cross-references MUID:99063795; PMID:9847077 !$#accession T08228 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-1073 ##label NGW !'##cross-references EMBL:AF016485; NID:g2822278; PID:g2822289; !1HALOSP:H0136 !'##experimental_source strain NRC-1 REFERENCE A40600 !$#authors Ng, W.L.; DasSarma, S. !$#journal J. Bacteriol. (1993) 175:4584-4596 !$#title Minimal replication origin of the 200-kilobase Halobacterium !1plasmid pNRC100. !$#cross-references MUID:93328662; PMID:8335618 !$#accession A40600 !'##molecule_type DNA !'##residues 65-806,'PPGRGD',807-1073 ##label NGA !'##cross-references GB:L19296 !'##note the source is designated as Halobacterium halobium GENETICS !$#gene repH; H0136 !$#genome plasmid pNRC100 FUNCTION !$#description required for replication of plasmid pNRC100 [validated, !1MUID:93328662] CLASSIFICATION #superfamily Halobacterium plasmid pNRC100 replication !1protein repH KEYWORDS plasmid replication SUMMARY #length 1073 #molecular-weight 120578 #checksum 1370 SEQUENCE /// ENTRY T08322 #type complete TITLE plasmid replication protein repJ [similarity] - Halobacterium sp. (strain NRC-1) plasmid pNRC100 ALTERNATE_NAMES hypothetical protein H1260 ORGANISM #formal_name Halobacterium sp. #variety strain NRC-1 DATE 18-Feb-2000 #sequence_revision 18-Feb-2000 #text_change 18-Feb-2000 ACCESSIONS T08322 REFERENCE Z16408 !$#authors Ng, W.V.; Ciufo, S.A.; Smith, T.M.; Bumgarner, R.E.; Baskin, !1D.; Faust, J.; Hall, B.; Loretz, C.; Seto, J.; Slagel, J.; !1Hood, L.; DasSarma, S. !$#journal Genome Res. (1998) 8:1131-1141 !$#title Snapshot of a large dynamic replicon in a halophilic !1Archaeon: megaplasmid or minichromosome? !$#cross-references MUID:99063795; PMID:9847077 !$#accession T08322 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-1128 ##label DAS !'##cross-references EMBL:AF016485; NID:g2822278; PID:g2822383; !1HALOSP:H1260 !'##experimental_source strain NRC-1 GENETICS !$#gene repJ; HALOSP:H1260 !$#genome plasmid pNRC100 CLASSIFICATION #superfamily Halobacterium plasmid pNRC100 replication !1protein repH KEYWORDS plasmid replication SUMMARY #length 1128 #molecular-weight 122447 #checksum 4618 SEQUENCE /// ENTRY T08312 #type complete TITLE plasmid replication protein repI [similarity] - Halobacterium sp. (strain NRC-1) plasmid pNRC100 ALTERNATE_NAMES hypothetical protein H1080 ORGANISM #formal_name Halobacterium sp. #variety strain NRC-1 DATE 18-Feb-2000 #sequence_revision 18-Feb-2000 #text_change 18-Feb-2000 ACCESSIONS T08312 REFERENCE Z16408 !$#authors Ng, W.V.; Ciufo, S.A.; Smith, T.M.; Bumgarner, R.E.; Baskin, !1D.; Faust, J.; Hall, B.; Loretz, C.; Seto, J.; Slagel, J.; !1Hood, L.; DasSarma, S. !$#journal Genome Res. (1998) 8:1131-1141 !$#title Snapshot of a large dynamic replicon in a halophilic !1Archaeon: megaplasmid or minichromosome? !$#cross-references MUID:99063795; PMID:9847077 !$#accession T08312 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-1128 ##label DAS !'##cross-references EMBL:AF016485; NID:g2822278; PID:g2822373; !1HALOSP:H1080 !'##experimental_source strain NRC-1 GENETICS !$#gene repI; HALOSP:H1080 !$#genome plasmid pNRC100 CLASSIFICATION #superfamily Halobacterium plasmid pNRC100 replication !1protein repH KEYWORDS plasmid replication SUMMARY #length 1128 #molecular-weight 122497 #checksum 1971 SEQUENCE /// ENTRY S37784 #type complete TITLE plasmid replication protein [validated] - Halobacterium salinarum plasmid pHH1 ORGANISM #formal_name Halobacterium salinarum DATE 18-Feb-2000 #sequence_revision 18-Feb-2000 #text_change 18-Feb-2000 ACCESSIONS S37784 REFERENCE S34806 !$#authors Pfeifer, F.; Ghahraman, P. !$#journal Mol. Gen. Genet. (1993) 238:193-200 !$#title Plasmid pHH1 of Halobacterium salinarium: characterization !1of the replicon region, the gas vesicle gene cluster and !1insertion elements. !$#cross-references MUID:93241154; PMID:8386798 !$#accession S37784 !'##status translation not shown !'##molecule_type DNA !'##residues 1-301 ##label PFE !'##cross-references EMBL:X67101 !'##note the source is designated as Halobacterium salinarium GENETICS !$#genome plasmid pHH1 FUNCTION !$#description required for plasmid pHH1 replication [validated, !1MUID:93241154] !$#note this corresponds to the amino-terminal region of the !1corresponding protein from plasmid pNRC100 CLASSIFICATION #superfamily Halobacterium plasmid pHH1 replication protein KEYWORDS plasmid replication SUMMARY #length 301 #molecular-weight 34268 #checksum 9476 SEQUENCE /// ENTRY A32447 #type complete TITLE potassium channel-activating protein - human ALTERNATE_NAMES delayed rectifier potassium channel ORGANISM #formal_name Homo sapiens #common_name man DATE 28-Jan-2000 #sequence_revision 28-Jan-2000 #text_change 21-Jul-2000 ACCESSIONS A32447; I53911 REFERENCE A32447 !$#authors Murai, T.; Kakizuka, A.; Takumi, T.; Ohkubo, H.; Nakanishi, !1S. !$#journal Biochem. Biophys. Res. Commun. (1989) 161:176-181 !$#title Molecular cloning and sequence analysis of human genomic DNA !1encoding a novel membrane protein which exhibits a slowly !1activating potassium channel activity. !$#cross-references MUID:89273632; PMID:2730656 !$#accession A32447 !'##status preliminary !'##molecule_type DNA !'##residues 1-129 ##label MUR !'##cross-references GB:M26685; NID:g186569; PIDN:AAA36129.1; !1PID:g386838 REFERENCE I53911 !$#authors Lai, L.P.; Deng, C.L.; Moss, A.J.; Kass, R.S.; Liang, C.S. !$#journal Gene (1994) 151:339-340 !$#title Polymorphism of the gene encoding a human minimal potassium !1ion channel (minK). !$#cross-references MUID:95129890; PMID:7828904 !$#accession I53911 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-37,'G',39-129 ##label LAI !'##cross-references GB:L33815; NID:g603450; PIDN:AAA63905.1; !1PID:g603451 GENETICS !$#gene GDB:KCNE1; ISK !'##cross-references GDB:127909; OMIM:176261 !$#map_position 21q22.1-21q22.2 CLASSIFICATION #superfamily human potassium channel-activating protein KEYWORDS phosphoprotein; transmembrane protein FEATURE !$44-66 #domain transmembrane #status predicted #label TMM SUMMARY #length 129 #molecular-weight 14675 #checksum 3322 SEQUENCE /// ENTRY E90447 #type complete TITLE phosphoesterase-related protein SSO2725 [similarity] - Sulfolobus solfataricus ORGANISM #formal_name Sulfolobus solfataricus DATE 24-May-2001 #sequence_revision 24-May-2001 #text_change 02-Nov-2001 ACCESSIONS E90447 REFERENCE A99139 !$#authors She, Q.; Singh, R.K.; Confalonieri, F.; Zivanovic, Y.; !1Allard, G.; Awayez, M.J.; Chan-Weiher, C.C.Y.; Clausen, !1I.G.; Curtis, B.A.; De Moors, A.; Erauso, G.; Fletcher, C.; !1Gordon, P.M.K.; Heikamp-de Jong, I.; Jeffries, A.C.; Kozera, !1C.J.; Medina, N.; Peng, X.; Thi-Ngoc, H.P.; Redder, P.; !1Schenk, M.E.; Theriault, C.; Tolstrup, N.; Charlebois, R.L.; !1Doolittle, W.F.; Duguet, M.; Gaasterland, T.; Garrett, R.A.; !1Ragan, M.A.; Sensen, C.W.; Van der Oost, J. !$#submission submitted to GenBank, April 2001 !$#description Sulfolobus solfataricus complete genome. !$#accession E90447 !'##molecule_type DNA !'##residues 1-324 ##label KUR !'##cross-references GB:AE006641; NID:g13816048; PIDN:AAK42836.1; !1GSPDB:GN00155 COMMENT Although this sequence has motifs characteristic of a !1variety of phosphoesterases, a critical active site residue !1is not conserved. GENETICS !$#gene SSO2725 CLASSIFICATION #superfamily Sulfolobus solfataricus phosphoesterase-related !1protein SSO2725; phosphoesterase core homology FEATURE !$18-151 #domain phosphoesterase core homology #label PEC SUMMARY #length 324 #molecular-weight 36626 #checksum 4285 SEQUENCE /// ENTRY G90393 #type complete TITLE phosphoesterase-related protein SSO2237 [similarity] - Sulfolobus solfataricus ORGANISM #formal_name Sulfolobus solfataricus DATE 24-May-2001 #sequence_revision 24-May-2001 #text_change 02-Nov-2001 ACCESSIONS G90393 REFERENCE A99139 !$#authors She, Q.; Singh, R.K.; Confalonieri, F.; Zivanovic, Y.; !1Allard, G.; Awayez, M.J.; Chan-Weiher, C.C.Y.; Clausen, !1I.G.; Curtis, B.A.; De Moors, A.; Erauso, G.; Fletcher, C.; !1Gordon, P.M.K.; Heikamp-de Jong, I.; Jeffries, A.C.; Kozera, !1C.J.; Medina, N.; Peng, X.; Thi-Ngoc, H.P.; Redder, P.; !1Schenk, M.E.; Theriault, C.; Tolstrup, N.; Charlebois, R.L.; !1Doolittle, W.F.; Duguet, M.; Gaasterland, T.; Garrett, R.A.; !1Ragan, M.A.; Sensen, C.W.; Van der Oost, J. !$#submission submitted to GenBank, April 2001 !$#description Sulfolobus solfataricus complete genome. !$#accession G90393 !'##molecule_type DNA !'##residues 1-325 ##label KUR !'##cross-references GB:AE006641; NID:g13815538; PIDN:AAK42406.1; !1GSPDB:GN00155 COMMENT Although this sequence has motifs characteristic of a !1variety of phosphoesterases, a critical active site residue !1is not conserved. GENETICS !$#gene SSO2237 CLASSIFICATION #superfamily Sulfolobus solfataricus phosphoesterase-related !1protein SSO2725; phosphoesterase core homology FEATURE !$19-152 #domain phosphoesterase core homology #label PEC SUMMARY #length 325 #molecular-weight 36850 #checksum 6079 SEQUENCE /// ENTRY A90448 #type complete TITLE phosphoesterase-related protein SSO2729 [similarity] - Sulfolobus solfataricus ORGANISM #formal_name Sulfolobus solfataricus DATE 24-May-2001 #sequence_revision 24-May-2001 #text_change 02-Nov-2001 ACCESSIONS A90448 REFERENCE A99139 !$#authors She, Q.; Singh, R.K.; Confalonieri, F.; Zivanovic, Y.; !1Allard, G.; Awayez, M.J.; Chan-Weiher, C.C.Y.; Clausen, !1I.G.; Curtis, B.A.; De Moors, A.; Erauso, G.; Fletcher, C.; !1Gordon, P.M.K.; Heikamp-de Jong, I.; Jeffries, A.C.; Kozera, !1C.J.; Medina, N.; Peng, X.; Thi-Ngoc, H.P.; Redder, P.; !1Schenk, M.E.; Theriault, C.; Tolstrup, N.; Charlebois, R.L.; !1Doolittle, W.F.; Duguet, M.; Gaasterland, T.; Garrett, R.A.; !1Ragan, M.A.; Sensen, C.W.; Van der Oost, J. !$#submission submitted to GenBank, April 2001 !$#description Sulfolobus solfataricus complete genome. !$#accession A90448 !'##molecule_type DNA !'##residues 1-302 ##label KUR !'##cross-references GB:AE006641; NID:g13816055; PIDN:AAK42840.1; !1GSPDB:GN00155 COMMENT Although this sequence has motifs characteristic of a !1variety of phosphoesterases, a critical active site residue !1is not conserved. GENETICS !$#gene SSO2729 CLASSIFICATION #superfamily Sulfolobus solfataricus phosphoesterase-related !1protein SSO2725; phosphoesterase core homology FEATURE !$6-132 #domain phosphoesterase core homology #label PEC SUMMARY #length 302 #molecular-weight 34851 #checksum 5674 SEQUENCE /// ENTRY A99376 #type complete TITLE phosphoesterase-related protein SSO2085 [similarity] - Sulfolobus solfataricus ALTERNATE_NAMES hypothetical protein c0613 ORGANISM #formal_name Sulfolobus solfataricus DATE 24-May-2001 #sequence_revision 24-May-2001 #text_change 02-Nov-2001 ACCESSIONS A99376; S73080 REFERENCE A99139 !$#authors She, Q.; Singh, R.K.; Confalonieri, F.; Zivanovic, Y.; !1Allard, G.; Awayez, M.J.; Chan-Weiher, C.C.Y.; Clausen, !1I.G.; Curtis, B.A.; De Moors, A.; Erauso, G.; Fletcher, C.; !1Gordon, P.M.K.; Heikamp-de Jong, I.; Jeffries, A.C.; Kozera, !1C.J.; Medina, N.; Peng, X.; Thi-Ngoc, H.P.; Redder, P.; !1Schenk, M.E.; Theriault, C.; Tolstrup, N.; Charlebois, R.L.; !1Doolittle, W.F.; Duguet, M.; Gaasterland, T.; Garrett, R.A.; !1Ragan, M.A.; Sensen, C.W.; Van der Oost, J. !$#submission submitted to GenBank, April 2001 !$#description Sulfolobus solfataricus complete genome. !$#accession A99376 !'##molecule_type DNA !'##residues 1-316 ##label KUR !'##cross-references GB:AE006641; NID:g13815368; PIDN:AAK42264.1; !1GSPDB:GN00155 REFERENCE S73076 !$#authors Sensen, C.W.; Klenk, H.P.; Singh, R.K.; Allard, G.; Chan, !1C.C.Y.; Liu, Q.Y.; Penny, S.L.; Young, F.; Schenk, M.E.; !1Gaasterland, T.; Doolittle, W.F.; Ragan, M.A.; Charlebois, !1R.L. !$#journal Mol. Microbiol. (1996) 22:175-191 !$#title Organizational characteristics and information content of an !1archaeal genome: 156 kb of sequence from Sulfolobus !1solfataricus P2. !$#cross-references MUID:97055432; PMID:8899719 !$#accession S73080 !'##status nucleic acid sequence not shown; translation not shown !'##molecule_type DNA !'##residues 8-316 ##label SEN !'##cross-references EMBL:Y08256; NID:g1707679; PID:e284008; !1PID:g1707692 !'##experimental_source strain P2 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1September 1996 COMMENT Although this sequence has motifs characteristic of a !1variety of phosphoesterases, an active site sequence is not !1conserved. GENETICS !$#gene SSO2085 CLASSIFICATION #superfamily Sulfolobus solfataricus phosphoesterase-related !1protein SSO2725; phosphoesterase core homology FEATURE !$13-140 #domain phosphoesterase core homology #status !8atypical #label PEC SUMMARY #length 316 #molecular-weight 35688 #checksum 5381 SEQUENCE /// ENTRY S69334 #type complete TITLE chloride peroxidase (EC 1.11.1.10) [validated] - Curvularia inaequalis ALTERNATE_NAMES vanadium-containing chloroperoxidase ORGANISM #formal_name Curvularia inaequalis DATE 28-Jan-2000 #sequence_revision 28-Jan-2000 #text_change 15-Sep-2000 ACCESSIONS S69334; S53117 REFERENCE S69334 !$#authors Simons, B.H.; Barnett, P.; Vollenbroek, E.G.M.; Dekker, !1H.L.; Muijsers, A.O.; Messerschmidt, A.; Wever, R. !$#journal Eur. J. Biochem. (1995) 229:566-574 !$#title Primary structure and characterization of the vanadium !1chloroperoxidase from the fungus Curvularia inaequalis. !$#cross-references MUID:95262722; PMID:7744081 !$#accession S69334 !'##molecule_type mRNA !'##residues 1-609 ##label SIM !'##cross-references EMBL:X85369; NID:g732617; PIDN:CAA59686.1; !1PID:g732618 !'##experimental_source CBS 102.42 !'##note part of this sequence was confirmed by sequence analysis of !1genomic DNA REFERENCE A66871 !$#authors Messerschmidt, A.; Wever, R. !$#submission submitted to the Brookhaven Protein Data Bank, September !11995 !$#cross-references PDB:1VNC !$#contents annotation; X-ray crystallography, 2.1 angstroms, 3-543,'E', !1545-578 !$#note the authors believe that 544-Glu is correct from modeling !1evidence GENETICS !$#gene vCPO FUNCTION !$#description catalyzes the formation of two carbon-chlorine bonds and two !1water molecules from two carbon-hydrogen bonds, two chloride !1ions and hydrogen peroxide CLASSIFICATION #superfamily Curvularia inaequalis chloride peroxidase; !1glucose-6-phosphatase catalytic domain homology KEYWORDS blocked amino end; chloride; metalloprotein; oxidoreductase; !1vanadium FEATURE !$329-511 #domain glucose-6-phosphatase catalytic domain !8homology #label GPH\ !$404 #active_site His #status predicted\ !$496 #binding_site vanadate (His) #status predicted SUMMARY #length 609 #molecular-weight 67530 #checksum 1282 SEQUENCE /// ENTRY T39382 #type complete TITLE DNA-directed DNA polymerase (EC 2.7.7.7) delta chain cdm1 [validated] - fission yeast (Schizosaccharomyces pombe) ALTERNATE_NAMES DNA polymerase delta, small subunit ORGANISM #formal_name Schizosaccharomyces pombe DATE 18-Feb-2000 #sequence_revision 18-Feb-2000 #text_change 21-Jul-2000 ACCESSIONS T39382; T43669 REFERENCE Z21850 !$#authors Lyne, M.; Rajandream, M.A.; Barrell, B.G.; Xiang, Z.; Aves, !1S. !$#submission submitted to the EMBL Data Library, January 1999 !$#accession T39382 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-160 ##label LYN !'##cross-references EMBL:AL035085; PIDN:CAA22676.1; GSPDB:GN00067; !1SPDB:SPBC12D12.02c !'##experimental_source strain 972h-; cosmid c12D12 REFERENCE Z22616 !$#authors Reynolds, N.; Watt, A.; Fantes, P.A.; MacNeill, S.A. !$#journal Curr. Genet. (1998) 34:250-258 !$#title Cdm1, the smallest subunit of DNA polymerase delta in the !1fission yeast Schizosaccharomyces pombe, is non-essential !1for growth and division. !$#cross-references MUID:99015975; PMID:9799358 !$#accession T43669 !'##status translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-160 ##label REY !'##cross-references EMBL:AJ006032; NID:g3130024; PIDN:CAA06824.1; !1PID:g3130025 GENETICS !$#gene cdm1; SPDB:SPBC12D12.02c !$#map_position 2 FUNCTION !$#description DNA polymerase delta DNA polymerase delta plays an essential !1role in DNA replication, repair, and recombination CLASSIFICATION #superfamily Schizosaccharomyces DNA polymerase delta, small !1chain KEYWORDS DNA biosynthesis; nucleotidyltransferase SUMMARY #length 160 #molecular-weight 18588 #checksum 7416 SEQUENCE /// ENTRY S64445 #type complete TITLE hypothetical protein YGR136w - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein G6409 ORGANISM #formal_name Saccharomyces cerevisiae DATE 03-Nov-2000 #sequence_revision 03-Nov-2000 #text_change 19-Apr-2002 ACCESSIONS S64445 REFERENCE S64428 !$#authors Van Dyck, L.; Skala, J.; de Wergifosse, P.; Purnelle, B.; !1Talla, E.; Nawrocki, A.; Del Bino, S.; Goffeau, A. !$#submission submitted to the Protein Sequence Database, May 1996 !$#accession S64445 !'##molecule_type DNA !'##residues 1-241 ##label VAN !'##cross-references EMBL:Z72921; EMBL:Y13135; NID:g1323226; !1PIDN:CAA97149.1; PID:g1323227; GSPDB:GN00007; MIPS:YGR136w !'##experimental_source strain S288C GENETICS !$#gene SGD:LSB1; MIPS:YGR136w !'##cross-references SGD:S0003368 !$#map_position 7R CLASSIFICATION #superfamily Saccharomyces cerevisiae hypothetical protein !1YGR136w; SH3 homology FEATURE !$60-107 #domain SH3 homology #label SH3 SUMMARY #length 241 #molecular-weight 26139 #checksum 3671 SEQUENCE /// ENTRY S61138 #type complete TITLE hypothetical protein YPR154w - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein P9584.5 ORGANISM #formal_name Saccharomyces cerevisiae DATE 03-Nov-2000 #sequence_revision 03-Nov-2000 #text_change 19-Apr-2002 ACCESSIONS S61138 REFERENCE S61139 !$#authors Stellyes, L. !$#submission submitted to the EMBL Data Library, June 1995 !$#description The sequence of S. cerevisiae cosmid 9584. !$#accession S61138 !'##molecule_type DNA !'##residues 1-215 ##label STE !'##cross-references EMBL:U28371; NID:g849161; PID:g849162; !1GSPDB:GN00016; MIPS:YPR154w GENETICS !$#gene SGD:PIN3; MIPS:YPR154w !'##cross-references SGD:S0006358 !$#map_position 16R CLASSIFICATION #superfamily Saccharomyces cerevisiae hypothetical protein !1YGR136w; SH3 homology FEATURE !$61-108 #domain SH3 homology #label SH3 SUMMARY #length 215 #molecular-weight 23539 #checksum 7100 SEQUENCE /// ENTRY T44983 #type complete TITLE methylmalonyl-CoA decarboxylase (EC 4.1.1.41) delta chain [validated] - Propionigenium modestum ORGANISM #formal_name Propionigenium modestum DATE 21-Jan-2000 #sequence_revision 21-Jan-2000 #text_change 22-Oct-2001 ACCESSIONS T44983 REFERENCE Z22888 !$#authors Bott, M.; Pfister, K.; Burda, P.; Kalbermatter, O.; Woehlke, !1G.; Dimroth, P. !$#journal Eur. J. Biochem. (1997) 250:590-599 !$#title Methylmalonyl-CoA decarboxylase from Propionigenium !1modestum: Cloning and sequencing of the structural genes and !1purification of the enzmye complex. !$#cross-references MUID:98088990; PMID:9428714 !$#accession T44983 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-137 ##label BOT !'##cross-references EMBL:AJ002015; NID:g2706397; PIDN:CAA05138.1; !1PID:g2706399 !'##experimental_source DSM 2376 COMMENT Methylmalonyl-CoA decarboxylase catalyses the only !1energy-conserving step during succinate fermentation by !1Propionigenium modestum: the decarboxylation of !1(S)-methylmalonyl-CoA to propionyl-CoA is coupled to the !1vectorial transport of Na+ across the cytoplasmic membrane, !1thereby creating a sodium ion motive force that is used for !1ATP synthesis. GENETICS !$#gene mmdD COMPLEX heterotetramer [validated, MUID:98088990] FUNCTION !$#description EC 4.1.1.41 [validated, MUID:98088990] !$#note specific activity up to 25 U/mg protein; Km value for !1(S)-methylmalonyl-CoA of approximately 12 microM [validated, !1MUID:98088990] CLASSIFICATION #superfamily Propionigenium modestum methylmalonyl-CoA !1decarboxylase delta chain KEYWORDS carbon-carbon lyase; carboxy-lyase; heterotetramer; sodium !1transport SUMMARY #length 137 #molecular-weight 14165 #checksum 8743 SEQUENCE /// ENTRY JC4808 #type complete TITLE ribosomal protein L14, cytosolic [validated] - rat ORGANISM #formal_name Rattus norvegicus #common_name Norway rat DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 19-Jan-2001 ACCESSIONS JC4808 REFERENCE JC4808 !$#authors Chan, Y.L.; Olvera, J.; Wool, I.G. !$#journal Biochem. Biophys. Res. Commun. (1996) 222:427-431 !$#title The primary structure of rat ribosomal protein L14. !$#cross-references MUID:96222520; PMID:8670222 !$#accession JC4808 !'##molecule_type mRNA !'##residues 1-214 ##label CHA !'##cross-references EMBL:X94242; NID:g1430943; PIDN:CAA63926.1; !1PID:g1430944 !'##note part of this sequence, including the amino end of the mature !1protein, was confirmed by protein sequencing !'##note the protein is designated as ribosomal protein L14 CLASSIFICATION #superfamily rat ribosomal protein L14 KEYWORDS leucine zipper; ribosome FEATURE !$2-214 #product ribosomal protein L14 #status experimental !8#label MAT\ !$109-158 #region leucine zipper motif\ !$170-189 #region 5-residue repeats (Q-K-A-[AS]-X)\ !$192-197 #region 3 residue repeats (K-G-Q) SUMMARY #length 214 #molecular-weight 23339 #checksum 9771 SEQUENCE /// ENTRY T26280 #type complete TITLE linoleoyl-CoA desaturase (EC 1.14.19.3) W08D2.4 - Caenorhabditis elegans ALTERNATE_NAMES Delta6 fatty acid desaturase ORGANISM #formal_name Caenorhabditis elegans DATE 09-Jun-2000 #sequence_revision 09-Jun-2000 #text_change 03-Jun-2002 ACCESSIONS T26280; T37238 REFERENCE Z20188 !$#authors Swinburne, J.; Ainscough, R. !$#submission submitted to the EMBL Data Library, March 1996 !$#accession T26280 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-473 ##label WIL !'##cross-references EMBL:Z70271; PIDN:CAA94233.1; GSPDB:GN00022; !1CESP:W08D2.4 !'##experimental_source clone W08D2 REFERENCE Z21637 !$#authors Napier, J.A.; Hey, S.J.; Lacey, D.J.; Shewry, P.R. !$#journal Biochem. J. (1998) 330:611-614 !$#title Identification of a caenorhabditis elegans !1Delta6-fatty-acid-desaturase by heterologous expression in !1saccharomyces cerevisiae. !$#cross-references MUID:98149727; PMID:9480865 !$#accession T37238 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-38,69-430,'V',432-473 ##label NAP !'##cross-references EMBL:AF031477; NID:g3088519; PIDN:AAC15586.1; !1PID:g3088520 GENETICS !$#gene CESP:W08D2.4 !$#map_position 4 !$#introns 13/3; 39/2; 234/3; 277/3; 378/1; 413/3 CLASSIFICATION #superfamily Caenorhabditis elegans Delta6 fatty acid !1desaturase KEYWORDS alternative splicing; oxidoreductase; unsaturated fatty acid !1biosynthesis SUMMARY #length 473 #molecular-weight 55122 #checksum 6505 SEQUENCE /// ENTRY T43319 #type complete TITLE Delta5 fatty acid desaturase (EC 1.14.99.-) T13F2.1 [validated] - Caenorhabditis elegans ORGANISM #formal_name Caenorhabditis elegans DATE 09-Jun-2000 #sequence_revision 09-Jun-2000 #text_change 21-Jul-2000 ACCESSIONS T43319; T24875 REFERENCE Z22422 !$#authors Michaelson, L.V.; Napier, J.A.; Lewis, M.; Griffiths, G.; !1Lazarus, C.M.; Stobart, A.K. !$#journal FEBS Lett. (1998) 439:215-218 !$#title Functional identification of a fatty acid delta5 desaturase !1gene from Caenorhabditis elegans. !$#cross-references MUID:99059458; PMID:9845325 !$#accession T43319 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-447 ##label MIC !'##cross-references EMBL:AF078796; NID:g4003522; PIDN:AAC95143.1; !1PID:g4003523 REFERENCE Z19947 !$#authors Swinburne, J. !$#submission submitted to the EMBL Data Library, October 1996 !$#accession T24875 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-197,'VSHIFNN',198-447 ##label WIL !'##cross-references EMBL:Z81122; PIDN:CAB03352.1; GSPDB:GN00022; !1CESP:T13F2.1 !'##experimental_source clone T13F2 GENETICS !$#gene CESP:T13F2.1; des-5 !$#map_position 4 !$#introns 43/3; 80/3; 197/3; 295/3; 318/2; 349/1; 384/3 CLASSIFICATION #superfamily Caenorhabditis elegans Delta6 fatty acid !1desaturase KEYWORDS oxidoreductase; unsaturated fatty acid biosynthesis SUMMARY #length 447 #molecular-weight 52348 #checksum 8843 SEQUENCE /// ENTRY S57749 #type complete TITLE SURF1 protein - human ORGANISM #formal_name Homo sapiens #common_name man DATE 17-Nov-2000 #sequence_revision 17-Nov-2000 #text_change 17-Nov-2000 ACCESSIONS S57749 REFERENCE S57747 !$#authors Lennard, A.; Gaston, K.; Fried, M. !$#submission submitted to the EMBL Data Library, July 1994 !$#description The Surf-1 and Surf-2 genes and their essential !1bidirectional promoter elements are conserved between mouse !1and human. !$#accession S57749 !'##molecule_type mRNA !'##residues 1-300 ##label LEN !'##cross-references EMBL:Z35093; NID:g895848; PIDN:CAA84476.1; !1PID:g895849 COMMENT This protein is thought to be involved in cytochrome c !1oxidase biogenesis. Mutations are associated with Leigh's !1syndrome, a severe neurological disorder characterized by !1cytochrome c oxidase deficiency. GENETICS !$#gene GDB:SURF1 !'##cross-references GDB:6071094; OMIM:185620 !$#map_position 9q33-9q34 CLASSIFICATION #superfamily human SURF1 protein SUMMARY #length 300 #molecular-weight 33331 #checksum 4517 SEQUENCE /// ENTRY S54305 #type complete TITLE taxis protein cheJ [validated] - Halobacterium salinarum ORGANISM #formal_name Halobacterium salinarum DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 18-Aug-2000 ACCESSIONS S54305 REFERENCE S54304 !$#authors Rudolph, J.; Oesterhelt, D. !$#journal EMBO J. (1995) 14:667-673 !$#title Chemotaxis and phototaxis require a CheA histidine kinase in !1the archaeon Halobacterium salinarium. !$#cross-references MUID:95188871; PMID:7882970 !$#accession S54305 !'##status preliminary; nucleic acid sequence not shown; translation not !1shown !'##molecule_type DNA !'##residues 1-195 ##label RUD !'##cross-references EMBL:X82645; NID:g671099; PID:g671101 !'##note the nucleotide sequence was submitted to the EMBL Data Library, !1November 1994 !'##note the source is designated as Halobacterium salinarium GENETICS !$#gene cheJ FUNCTION !$#description cheJ affects the ratio of forward/reverse swimming in !1unstimulated bacteria [validated, MUID:96016197] CLASSIFICATION #superfamily Halobacterium salinarum taxis protein cheJ SUMMARY #length 195 #molecular-weight 20958 #checksum 4057 SEQUENCE /// ENTRY S46676 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) YHR202w [similarity] - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein H9998.1 ORGANISM #formal_name Saccharomyces cerevisiae DATE 28-Oct-1994 #sequence_revision 28-Oct-1994 #text_change 19-Apr-2002 ACCESSIONS S46676 REFERENCE S46674 !$#authors Macri, C. !$#submission submitted to the EMBL Data Library, February 1994 !$#description The sequence of S. cerevisiae cosmid 9998. !$#accession S46676 !'##molecule_type DNA !'##residues 1-602 ##label MAC !'##cross-references EMBL:U00030; NID:g458927; PID:g458928; !1GSPDB:GN00008; MIPS:YHR202w COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene MIPS:YHR202w !'##cross-references SGD:S0001245 !$#map_position 8R CLASSIFICATION #superfamily Saccharomyces cerevisiae probable !1phosphoesterase YHR202w; phosphoesterase core homology KEYWORDS hydrolase FEATURE !$45-133 #domain phosphoesterase core homology #label PEC SUMMARY #length 602 #molecular-weight 68998 #checksum 5064 SEQUENCE /// ENTRY T50052 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) SPAC1039.02 [similarity] - fission yeast (Schizosaccharomyces pombe) ORGANISM #formal_name Schizosaccharomyces pombe DATE 09-Jun-2000 #sequence_revision 09-Jun-2000 #text_change 22-Oct-2001 ACCESSIONS T50052 REFERENCE Z25031 !$#authors Hunt, C.; Aves, S.; McDougall, R.C.; Rajandream, M.A.; !1Barrell, B.G. !$#submission submitted to the EMBL Data Library, December 1999 !$#accession T50052 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-601 ##label HUN !'##cross-references EMBL:AL133521; PIDN:CAB63538.1; GSPDB:GN00066; !1SPDB:SPAC1039.02 !'##experimental_source strain 972h(-); cosmid c1039 COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene SPDB:SPAC1039.02 !$#map_position 1 CLASSIFICATION #superfamily Saccharomyces cerevisiae probable !1phosphoesterase YHR202w; phosphoesterase core homology KEYWORDS hydrolase FEATURE !$49-137 #domain phosphoesterase core homology #label PEC SUMMARY #length 601 #molecular-weight 68065 #checksum 6758 SEQUENCE /// ENTRY T37835 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) SPAC17G6.03 [similarity] - fission yeast (Schizosaccharomyces pombe) ORGANISM #formal_name Schizosaccharomyces pombe DATE 03-Dec-1999 #sequence_revision 03-Dec-1999 #text_change 22-Oct-2001 ACCESSIONS T37835 REFERENCE Z21749 !$#authors Murphy, L.; Harris, D.; Barrell, B.G.; Rajandream, M.A.; !1Wood, V. !$#submission submitted to the EMBL Data Library, September 1997 !$#accession T37835 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-635 ##label MUR !'##cross-references EMBL:Z99162; PIDN:CAB16214.1; GSPDB:GN00066; !1SPDB:SPAC17G6.03 !'##experimental_source strain 972h-; cosmid c17G6 COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene SPDB:SPAC17G6.03 !$#map_position 1 CLASSIFICATION #superfamily Saccharomyces cerevisiae probable !1phosphoesterase YHR202w; phosphoesterase core homology KEYWORDS hydrolase FEATURE !$39-127 #domain phosphoesterase core homology #label PEC SUMMARY #length 635 #molecular-weight 71441 #checksum 361 SEQUENCE /// ENTRY S48466 #type complete TITLE MOB1 protein [validated] - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES protein YIL106w ORGANISM #formal_name Saccharomyces cerevisiae DATE 09-Jun-2000 #sequence_revision 09-Jun-2000 #text_change 09-Jun-2000 ACCESSIONS S48466 REFERENCE S48455 !$#authors Bowman, S.; Churcher, C. !$#submission submitted to the EMBL Data Library, September 1994 !$#accession S48466 !'##molecule_type DNA !'##residues 1-314 ##label BOW !'##cross-references EMBL:Z38125; NID:g558688; PIDN:CAA86274.1; !1PID:g558700; GSPDB:GN00009; MIPS:YIL106w REFERENCE A59298 !$#authors Luca, F.C.; Winey, M. !$#journal Mol. Biol. Cell (1998) 9:29-46 !$#title MOB1, an essential yeast gene required for completion of !1mitosis and maintenance of ploidy. !$#cross-references MUID:98099687; PMID:9436989 !$#contents annotation GENETICS !$#gene SGD:MOB1; MIPS:YIL106w !'##cross-references SGD:S0001368; MIPS:YIL106w !$#map_position 9L !$#introns 7/2 FUNCTION !$#description required for normal cell cycle progression; required for !1completion of mitosis; required for maintenance of ploidy; !1Mob1 is a phosphoprotein in vivo [validated, MUID:98099687] CLASSIFICATION #superfamily Saccharomyces cerevisiae mob1 protein KEYWORDS phosphoprotein SUMMARY #length 314 #molecular-weight 35882 #checksum 8078 SEQUENCE /// ENTRY T52057 #type complete TITLE trehalose-phosphatase (EC 3.1.3.12) A [validated] - Arabidopsis thaliana ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 17-Nov-2000 #sequence_revision 17-Nov-2000 #text_change 17-Nov-2000 ACCESSIONS T52057 REFERENCE Z25925 !$#authors Vogel, G.; Aeschbacher, R.A.; Mueller, J.; Boller, T.; !1Wiemken, A. !$#journal Plant J. (1998) 13:673-683 !$#title Trehalose-6-phosphate phosphatases from Arabidopsis !1thaliana: identification by funtional complementation of the !1yeast tps2 mutant. !$#cross-references MUID:98345987; PMID:9681009 !$#accession T52057 !'##status preliminary; translated from GB/EMBL/DDBJ !'##molecule_type mRNA !'##residues 1-385 ##label VOG !'##cross-references EMBL:AF007778; PIDN:AAC39369.1 GENETICS !$#gene TPPA FUNCTION !$#description EC 3.1.3.12 [validated, MUID:98345987] !$#note dephosphorylates trehalose-6-phosphate but not !1glucose-6-phosphate or sucrose-6-phosphate CLASSIFICATION #superfamily Arabidopsis trehalose-phosphatase KEYWORDS phosphoric monoester hydrolase SUMMARY #length 385 #molecular-weight 43192 #checksum 6406 SEQUENCE /// ENTRY E75186 #type complete TITLE probable phosphoesterase (EC3.1.-.-) PAB0011 [similarity] - Pyrococcus abyssi (strain Orsay) ORGANISM #formal_name Pyrococcus abyssi DATE 03-Aug-2001 #sequence_revision 03-Aug-2001 #text_change 03-Aug-2001 ACCESSIONS E75186 REFERENCE A75001 !$#authors anonymous, Genoscope !$#submission submitted to the EMBL Data Library, July 1999 !$#description Pyrococcus abyssi genome sequence: insights into archaeal !1chromosome structure and evolution. !$#accession E75186 !'##molecule_type DNA !'##residues 1-248 ##label KAW !'##cross-references GB:AJ248283; GB:AL096836; NID:g5457433; !1PIDN:CAB48940.1; PID:e1514834; PID:g5457449 !'##experimental_source strain Orsay GENETICS !$#gene PAB0011 CLASSIFICATION #superfamily Pyrococcus abyssi probable phosphoesterase !1PAB0011; phosphoesterase core homology KEYWORDS hydrolase FEATURE !$2-64 #domain phosphoesterase core homology #label PEC SUMMARY #length 248 #molecular-weight 27967 #checksum 8443 SEQUENCE /// ENTRY B86746 #type complete TITLE probable phosphoesterase (EC3.1.-.-) yjjH [similarity] - Lactococcus lactis subsp. lactis (strain IL1403) ORGANISM #formal_name Lactococcus lactis subsp. lactis DATE 03-Aug-2001 #sequence_revision 03-Aug-2001 #text_change 03-Aug-2001 ACCESSIONS B86746 REFERENCE A86625 !$#authors Bolotin, A.; Wincker, P.; Mauger, S.; Jaillon, O.; Malarme, !1K.; Weissenbach, J.; Ehrlich, S.D.; Sorokin, A. !$#journal Genome Res. (2001) 11:731-753 !$#title The complete genome sequence of the lactic acid bacterium !1Lactococcus lactis ssp. lactis IL1403. !$#cross-references MUID:21235186; PMID:11337471 !$#accession B86746 !'##molecule_type DNA !'##residues 1-243 ##label STO !'##cross-references GB:AE005176; NID:g12723910; PIDN:AAK05068.1; !1GSPDB:GN00146 !'##experimental_source strain IL1403 GENETICS !$#gene yjjH CLASSIFICATION #superfamily Pyrococcus abyssi probable phosphoesterase !1PAB0011; phosphoesterase core homology KEYWORDS hydrolase FEATURE !$6-77 #domain phosphoesterase core homology #label PEC SUMMARY #length 243 #molecular-weight 28645 #checksum 47 SEQUENCE /// ENTRY F90045 #type complete TITLE probable phosphoesterase (EC3.1.-.-) SA2225 [similarity] - Staphylococcus aureus (strain N315) ORGANISM #formal_name Staphylococcus aureus DATE 03-Aug-2001 #sequence_revision 03-Aug-2001 #text_change 22-Oct-2001 ACCESSIONS F90045 REFERENCE A89758 !$#authors Kuroda, M.; Ohta, T.; Uchiyama, I.; Baba, T.; Yuzawa, H.; !1Kobayashi, I.; Cui, L.; Oguchi, A.; Aoki, K.; Nagai, Y.; !1Lian, J.; Ito, T.; Kanamori, M.; Matsumaru, H.; Maruyama, !1A.; Murakami, H.; Hosoyama, A.; Mizutani-Ui, Y.; Kobayashi, !1N.; Sawano, T.; Inoue, R.; Kaito, C.; Sekimizu, K.; !1Hirakawa, H.; Kuhara, S.; Goto, S.; Yabuzaki, J.; Kanehisa, !1M.; Yamashita, A.; Oshima, K.; Furuya, K.; Yoshino, C.; !1Shiba, T.; Hattori, M.; Ogasawara, N.; Hayashi, H.; !1Hiramatsu, K. !$#journal Lancet (2001) 357:1225-1240 !$#title Whole genome sequencing of meticillin-resistant !1Stapylococcus aureus. !$#cross-references MUID:21311952; PMID:11418146 !$#accession F90045 !'##molecule_type DNA !'##residues 1-268 ##label KUR !'##cross-references GB:BA000018; NID:g13702386; PIDN:BAB43527.1; !1GSPDB:GN00149 !'##experimental_source strain N315 GENETICS !$#gene SA2225 CLASSIFICATION #superfamily Pyrococcus abyssi probable phosphoesterase !1PAB0011; phosphoesterase core homology KEYWORDS hydrolase FEATURE !$2-74 #domain phosphoesterase core homology #label PEC SUMMARY #length 268 #molecular-weight 31339 #checksum 5680 SEQUENCE /// ENTRY S69731 #type complete TITLE endopolyphosphatase (EC 3.6.1.10) PPN1 precursor [validated] - yeast (Saccharomyces cerevisiae) ALTERNATE_NAMES hypothetical protein YDR452w ORGANISM #formal_name Saccharomyces cerevisiae DATE 22-Aug-1996 #sequence_revision 06-Sep-1996 #text_change 19-Apr-2002 ACCESSIONS S69731 REFERENCE S69555 !$#authors Dietrich, F.S. !$#submission submitted to the EMBL Data Library, August 1995 !$#description The sequence of S. cerevisiae lambda 3641 and cosmids 9461, !19831, and 9410. !$#accession S69731 !'##molecule_type DNA !'##residues 1-674 ##label DIE !'##cross-references EMBL:U33007; NID:g927685; PID:g927706; !1GSPDB:GN00004; MIPS:YDR452w GENETICS !$#gene SGD:PHM5; PPN1; MIPS:YDR452w !'##cross-references SGD:S0002860 !$#map_position 4R COMPLEX homodimer of chains of about 350 amino acids derived by !1proteolysis from amino half of precursor sequence !1[validated, PMID:11447286] FUNCTION !$#description hydrolyze long inorganic phosphate chains to shorter chains !1(predominantly of 60 and 3 phosphate units) [validated, !1PMID:11447286] CLASSIFICATION #superfamily Saccharomyces cerevisiae endopolyphosphatase !1PPN1; phosphoesterase core homology KEYWORDS hydrolase FEATURE !$1-39 #domain signal sequence #status predicted #label SIG\ !$96-226 #domain phosphoesterase core homology #label PEC SUMMARY #length 674 #molecular-weight 78344 #checksum 5592 SEQUENCE /// ENTRY T50959 #type complete TITLE probable endopolyphosphatase (EC 3.6.1.10) B24P7.140 precursor [similarity] - Neurospora crassa ORGANISM #formal_name Neurospora crassa DATE 21-Jul-2000 #sequence_revision 21-Jul-2000 #text_change 22-Oct-2001 ACCESSIONS T50959 REFERENCE Z25286 !$#authors Schulte, U.; Aign, V.; Hoheisel, J.; Brandt, P.; Fartmann, !1B.; Holland, R.; Nyakatura, G.; Mewes, H.W.; Mannhaupt, G. !$#submission submitted to the Protein Sequence Database, July 2000 !$#accession T50959 !'##molecule_type DNA !'##residues 1-757 ##label SCH !'##cross-references EMBL:AL389890; GSPDB:GN00116; NCSP:B24P7.140 !'##experimental_source BAC clone B24P7; strain OR74A GENETICS !$#gene NCSP:B24P7.140 !$#map_position 6 !$#introns 88/1 FUNCTION !$#description hydrolyze long inorganic phosphate chains to shorter chains CLASSIFICATION #superfamily Neurospora crassa endopolyphosphatase !1B24P7.140; phosphoesterase core homology KEYWORDS hydrolase FEATURE !$1-45 #domain signal sequence #status predicted #label SIG\ !$82-206 #domain phosphoesterase core homology #label PEC SUMMARY #length 757 #molecular-weight 86523 #checksum 4657 SEQUENCE /// ENTRY D84908 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) At2g46880 - Arabidopsis thaliana ALTERNATE_NAMES hypothetical protein F14M4.29; hypothetical protein F19D11.16 ORGANISM #formal_name Arabidopsis thaliana #common_name mouse-ear cress DATE 02-Feb-2001 #sequence_revision 02-Feb-2001 #text_change 22-Oct-2001 ACCESSIONS D84908; T02199; T02689 REFERENCE A84420 !$#authors Lin, X.; Kaul, S.; Rounsley, S.D.; Shea, T.P.; Benito, M.I.; !1Town, C.D.; Fujii, C.Y.; Mason, T.M.; Bowman, C.L.; !1Barnstead, M.E.; Feldblyum, T.V.; Buell, C.R.; Ketchum, !1K.A.; Lee, J.J.; Ronning, C.M.; Koo, H.; Moffat, K.S.; !1Cronin, L.A.; Shen, M.; VanAken, S.E.; Umayam, L.; Tallon, !1L.J.; Gill, J.E.; Adams, M.D.; Carrera, A.J.; Creasy, T.H.; !1Goodman, H.M.; Somerville, C.R.; Copenhaver, G.P.; Preuss, !1D.; Nierman, W.C.; White, O.; Eisen, J.A.; Salzberg, S.L.; !1Fraser, C.M.; Venter, J.C. !$#journal Nature (1999) 402:761-768 !$#title Sequence and analysis of chromosome 2 of the plant !1Arabidopsis thaliana. !$#cross-references MUID:20083487; PMID:10617197 !$#accession D84908 !'##molecule_type DNA !'##residues 1-387 ##label STO !'##cross-references GB:AC004411; NID:g6598415; PIDN:AAC34232.1; !1GSPDB:GN00139 REFERENCE Z14609 !$#authors Rounsley, S.D.; Lin, X.; Kaul, S.; Shea, T.P.; Fujii, C.Y.; !1Mason, T.M.; Shen, M.; Ronning, C.M.; Fraser, C.M.; !1Somerville, C.R.; Venter, J.C. !$#submission submitted to the EMBL Data Library, September 1998 !$#description Arabidopsis thaliana chromosome II BAC F14M4 genomic !1sequence. !$#accession T02199 !'##status translated from GB/EMBL/DDBJ !'##molecule_type DNA !'##residues 1-387 ##label ROW !'##cross-references EMBL:AC004411; NID:g3522932; PID:g3522950 !'##experimental_source cultivar Columbia COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene At2g46880; F19D11.16; F14M4.29 !$#map_position 2 CLASSIFICATION #superfamily Arabidopsis thaliana probable phosphoesterase !1At2g46880; phosphoesterase core homology KEYWORDS hydrolase FEATURE !$47-138 #domain phosphoesterase core homology #label PEC SUMMARY #length 387 #molecular-weight 44031 #checksum 5177 SEQUENCE /// ENTRY H86714 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) yhcH [similarity] - Lactococcus lactis subsp. lactis (strain IL1403) ORGANISM #formal_name Lactococcus lactis subsp. lactis DATE 23-Mar-2001 #sequence_revision 23-Mar-2001 #text_change 22-Oct-2001 ACCESSIONS H86714 REFERENCE A86625 !$#authors Bolotin, A.; Wincker, P.; Mauger, S.; Jaillon, O.; Malarme, !1K.; Weissenbach, J.; Ehrlich, S.D.; Sorokin, A. !$#journal Genome Res. (2001) 11:731-753 !$#title The complete genome sequence of the lactic acid bacterium !1Lactococcus lactis ssp. lactis IL1403. !$#cross-references MUID:21235186; PMID:11337471 !$#accession H86714 !'##molecule_type DNA !'##residues 1-312 ##label STO !'##cross-references GB:AE005176; PID:g12723632; PIDN:AAK04818.1; !1GSPDB:GN00146 !'##experimental_source strain IL1403 COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene yhcH CLASSIFICATION #superfamily Lactococcus lactis probable phosphoesterase !1yhcH; phosphoesterase core homology KEYWORDS hydrolase FEATURE !$71-139 #domain phosphoesterase core homology #label PEC SUMMARY #length 312 #molecular-weight 35506 #checksum 8236 SEQUENCE /// ENTRY F90425 #type complete TITLE phosphoesterase-related protein SSO2531 [similarity] - Sulfolobus solfataricus ORGANISM #formal_name Sulfolobus solfataricus DATE 24-May-2001 #sequence_revision 24-May-2001 #text_change 11-Jan-2002 ACCESSIONS F90425 REFERENCE A99139 !$#authors She, Q.; Singh, R.K.; Confalonieri, F.; Zivanovic, Y.; !1Allard, G.; Awayez, M.J.; Chan-Weiher, C.C.Y.; Clausen, !1I.G.; Curtis, B.A.; De Moors, A.; Erauso, G.; Fletcher, C.; !1Gordon, P.M.K.; Heikamp-de Jong, I.; Jeffries, A.C.; Kozera, !1C.J.; Medina, N.; Peng, X.; Thi-Ngoc, H.P.; Redder, P.; !1Schenk, M.E.; Theriault, C.; Tolstrup, N.; Charlebois, R.L.; !1Doolittle, W.F.; Duguet, M.; Gaasterland, T.; Garrett, R.A.; !1Ragan, M.A.; Sensen, C.W.; Van der Oost, J. !$#submission submitted to GenBank, April 2001 !$#description Sulfolobus solfataricus complete genome. !$#accession F90425 !'##molecule_type DNA !'##residues 1-190 ##label KUR !'##cross-references GB:AE006641; NID:g13815833; PIDN:AAK42661.1; !1GSPDB:GN00155 COMMENT Although this sequence has motifs characteristic of a !1variety of phosphoesterases, a critical active site residue !1is not conserved. GENETICS !$#gene SSO2531 CLASSIFICATION #superfamily Sulfolobus solfataricus phosphoesterase homolog !1SSO2531; phosphoesterase core homology FEATURE !$11-75 #domain phosphoesterase core homology #label PEC SUMMARY #length 190 #molecular-weight 22144 #checksum 3408 SEQUENCE /// ENTRY A99320 #type complete TITLE phosphoesterase-related protein SSO1605 [similarity] - Sulfolobus solfataricus ORGANISM #formal_name Sulfolobus solfataricus DATE 24-May-2001 #sequence_revision 24-May-2001 #text_change 11-Jan-2002 ACCESSIONS A99320 REFERENCE A99139 !$#authors She, Q.; Singh, R.K.; Confalonieri, F.; Zivanovic, Y.; !1Allard, G.; Awayez, M.J.; Chan-Weiher, C.C.Y.; Clausen, !1I.G.; Curtis, B.A.; De Moors, A.; Erauso, G.; Fletcher, C.; !1Gordon, P.M.K.; Heikamp-de Jong, I.; Jeffries, A.C.; Kozera, !1C.J.; Medina, N.; Peng, X.; Thi-Ngoc, H.P.; Redder, P.; !1Schenk, M.E.; Theriault, C.; Tolstrup, N.; Charlebois, R.L.; !1Doolittle, W.F.; Duguet, M.; Gaasterland, T.; Garrett, R.A.; !1Ragan, M.A.; Sensen, C.W.; Van der Oost, J. !$#submission submitted to GenBank, April 2001 !$#description Sulfolobus solfataricus complete genome. !$#accession A99320 !'##molecule_type DNA !'##residues 1-190 ##label KUR !'##cross-references GB:AE006641; NID:g13814840; PIDN:AAK41816.1; !1GSPDB:GN00155 COMMENT Although this sequence has motifs characteristic of a !1variety of phosphoesterases, a critical active site residue !1is not conserved. GENETICS !$#gene SSO1605 CLASSIFICATION #superfamily Sulfolobus solfataricus phosphoesterase homolog !1SSO2531; phosphoesterase core homology FEATURE !$11-75 #domain phosphoesterase core homology #label PEC SUMMARY #length 190 #molecular-weight 22230 #checksum 2518 SEQUENCE /// ENTRY H95860 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) SMb20152 [similarity] - Sinorhizobium meliloti (strain 1021) magaplasmid pSymB ORGANISM #formal_name Sinorhizobium meliloti DATE 24-Aug-2001 #sequence_revision 24-Aug-2001 #text_change 22-Oct-2001 ACCESSIONS H95860 REFERENCE A95842 !$#authors Finan, T.M.; Weidner, S.; Wong, K.; Buhrmester, J.; Chain, !1P.; Vorholter, F.J.; Hernandez-Lucas, I.; Becker, A.; Cowie, !1A.; Gouzy, J.; Golding, B.; Puhler, A. !$#journal Proc. Natl. Acad. Sci. U.S.A. (2001) 98:9889-9894 !$#title The complete sequence of the 1,683-kb pSymB megaplasmid from !1the N2-fixing endosymbiont Sinorhizobium meliloti. !$#cross-references MUID:21396508; PMID:11481431 !$#accession H95860 !'##molecule_type DNA !'##residues 1-572 ##label KUR !'##cross-references GB:AL591985; PIDN:CAC48552.1; PID:g15140024; !1GSPDB:GN00167 !'##experimental_source strain 1021, megaplasmid pSymB REFERENCE A96039 !$#authors Galibert, F.; Finan, T.M.; Long, S.R.; Puhler, A.; Abola, !1P.; Ampe, F.; Barloy-Hubler, F.; Barnett, M.J.; Becker, A.; !1Boistard, P.; Bothe, G.; Boutry, M.; Bowser, L.; Buhrmester, !1J.; Cadieu, E.; Capela, D.; Chain, P.; Cowie, A.; Davis, !1R.W.; Dreano, S.; Federspiel, N.A.; Fisher, R.F.; Gloux, S.; !1Godrie, T.; Goffeau, A.; Golding, B.; Gouzy, J.; Gurjal, M.; !1Hernandez-Lucas, I.; Hong, A.; Huizar, L.; Hyman, R.W.; !1Jones, T.; Kahn, D.; Kahn, M.L.; Kalman, S.; Keating, D.H.; !1Kiss, E.; Komp, C.; Lelaure, V.; Masuy, D.; Palm, C.; Peck, !1M.C.; Pohl, T.M.; Portetelle, D.; Purnelle, B.; Ramsperger, !1U.; Surzycki, R.; Thebault, P.; Vandenbol, M.; Vorholter, !1F.J.; Weidner, S.; Wells, D.H.; Wong, K.; Yeh, K.C.; Batut, !1J. !$#journal Science (2001) 293:668-672 !$#title The composite genome of the legume symbiont Sinorhizobium !1meliloti. !$#cross-references MUID:21368234; PMID:11474104 !$#contents annotation COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene SMb20152 !$#genome plasmid CLASSIFICATION #superfamily Sinorhizobium meliloti probable phosphoesterase !1SMb20152; phosphoesterase core homology KEYWORDS hydrolase FEATURE !$8-114 #domain phosphoesterase core homology #label PEC SUMMARY #length 572 #molecular-weight 62894 #checksum 6569 SEQUENCE /// ENTRY A97033 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) CAC1078 [similarity] - Clostridium acetobutylicum ORGANISM #formal_name Clostridium acetobutylicum DATE 14-Sep-2001 #sequence_revision 14-Sep-2001 #text_change 22-Oct-2001 ACCESSIONS A97033 REFERENCE A96900 !$#authors Nolling, J.; Breton, G.; Omelchenko, M.V.; Markarova, K.S.; !1Zeng, Q.; Gibson, R.; Lee, H.M.; Dubois, J.; Qiu, D.; Hitti, !1J.; Wolf, Y.I.; Tatusov, R.L.; Sabathe, F.; Doucette-Stamm, !1L.; Soucaille, P.; Daly, M.J.; Bennett, G.N.; Koonin, E.V.; !1Smith, D.R. !$#journal J. Bacteriol. (2001) 183:4823-4838 !$#title Genome Sequence and Comparative Analysis of the !1Solvent-Producing Bacterium Clostridium acetobutylicum. !$#cross-references MUID:21359325; PMID:21359325 !$#accession A97033 !'##molecule_type DNA !'##residues 1-356 ##label KUR !'##cross-references GB:AE001437; PIDN:AAK79052.1; PID:g15023992; !1GSPDB:GN00168 !'##experimental_source Clostridium acetobutylicum ATCC824 COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene CAC1078 CLASSIFICATION #superfamily Clostridium acetobutylicum probable !1phosphoesterase CAC1078; phosphoesterase core homology KEYWORDS hydrolase FEATURE !$33-127 #domain phosphoesterase core homology #label PEC SUMMARY #length 356 #molecular-weight 39168 #checksum 8468 SEQUENCE /// ENTRY G97024 #type complete TITLE probable phosphoesterase (EC 3.1.-.-) CAC1010 [similarity] - Clostridium acetobutylicum ORGANISM #formal_name Clostridium acetobutylicum DATE 14-Sep-2001 #sequence_revision 14-Sep-2001 #text_change 22-Oct-2001 ACCESSIONS G97024 REFERENCE A96900 !$#authors Nolling, J.; Breton, G.; Omelchenko, M.V.; Markarova, K.S.; !1Zeng, Q.; Gibson, R.; Lee, H.M.; Dubois, J.; Qiu, D.; Hitti, !1J.; Wolf, Y.I.; Tatusov, R.L.; Sabathe, F.; Doucette-Stamm, !1L.; Soucaille, P.; Daly, M.J.; Bennett, G.N.; Koonin, E.V.; !1Smith, D.R. !$#journal J. Bacteriol. (2001) 183:4823-4838 !$#title Genome Sequence and Comparative Analysis of the !1Solvent-Producing Bacterium Clostridium acetobutylicum. !$#cross-references MUID:21359325; PMID:21359325 !$#accession G97024 !'##molecule_type DNA !'##residues 1-345 ##label KUR !'##cross-references GB:AE001437; PIDN:AAK78986.1; PID:g15023919; !1GSPDB:GN00168 !'##experimental_source Clostridium acetobutylicum ATCC824 COMMENT This sequence has motifs characteristic of a variety of !1phosphoesterases. GENETICS !$#gene CAC1010 CLASSIFICATION #superfamily Clostridium acetobutylicum probable !1phosphoesterase CAC1078; phosphoesterase core homology KEYWORDS hydrolase FEATURE !$33-120 #domain phosphoesterase core homology #label PEC SUMMARY #length 345 #molecular-weight 38556 #checksum 9870 SEQUENCE ///